data_8X3H
# 
_entry.id   8X3H 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.380 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   8X3H         pdb_00008x3h 10.2210/pdb8x3h/pdb 
WWPDB D_1300042411 ?            ?                   
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8X3H 
_pdbx_database_status.recvd_initial_deposition_date   2023-11-13 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Toyoda, M.'   1 ? 
'Mikami, B.'   2 ? 
'Mizutani, K.' 3 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Crystal structure of iron-bound ovotransferrin N-lobe at atomic resolution' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Toyoda, M.'   1 ? 
primary 'Tanabe, A.'   2 ? 
primary 'Mikami, B.'   3 ? 
primary 'Hirose, M.'   4 ? 
primary 'Mizutani, K.' 5 ? 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8X3H 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     46.346 
_cell.length_a_esd                 ? 
_cell.length_b                     75.518 
_cell.length_b_esd                 ? 
_cell.length_c                     84.647 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8X3H 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man Ovotransferrin  36528.309 1   ? ? ? ? 
2 non-polymer nat 'FE (III) ION'  55.845    1   ? ? ? ? 
3 non-polymer syn 'CARBONATE ION' 60.009    1   ? ? ? ? 
4 non-polymer syn GLYCEROL        92.094    1   ? ? ? ? 
5 water       nat water           18.015    540 ? ? ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;APPKSVIRWCTISSPEEKKCNNLRDLTQQERISLTCVQKATYLDCIKAIANNEADAISLDGGQVFEAGLAPYKLKPIAAE
VYEHTEGSTTSYYAVAVVKKGTEFTVNDLQGKTSCHTGLGRSAGWNIPIGTLIHRGAIEWEGIESGSVEQAVAKFFSASC
VPGATIEQKLCRQCKGDPKTKCARNAPYSGYSGAFHCLKDGKGDVAFVKHTTVNENAPDQKDEYELLCLDGSRQPVDNYK
TCNWARVAAHAVVARDDNKVEDIWSFLSKAQSDFGVDTKSDFHLFGPPGKKDPVLKDLLFKDSAIMLKRVPSLMDSQLYL
GFEYYSAIQSMR
;
_entity_poly.pdbx_seq_one_letter_code_can   
;APPKSVIRWCTISSPEEKKCNNLRDLTQQERISLTCVQKATYLDCIKAIANNEADAISLDGGQVFEAGLAPYKLKPIAAE
VYEHTEGSTTSYYAVAVVKKGTEFTVNDLQGKTSCHTGLGRSAGWNIPIGTLIHRGAIEWEGIESGSVEQAVAKFFSASC
VPGATIEQKLCRQCKGDPKTKCARNAPYSGYSGAFHCLKDGKGDVAFVKHTTVNENAPDQKDEYELLCLDGSRQPVDNYK
TCNWARVAAHAVVARDDNKVEDIWSFLSKAQSDFGVDTKSDFHLFGPPGKKDPVLKDLLFKDSAIMLKRVPSLMDSQLYL
GFEYYSAIQSMR
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   ALA n 
1 2   PRO n 
1 3   PRO n 
1 4   LYS n 
1 5   SER n 
1 6   VAL n 
1 7   ILE n 
1 8   ARG n 
1 9   TRP n 
1 10  CYS n 
1 11  THR n 
1 12  ILE n 
1 13  SER n 
1 14  SER n 
1 15  PRO n 
1 16  GLU n 
1 17  GLU n 
1 18  LYS n 
1 19  LYS n 
1 20  CYS n 
1 21  ASN n 
1 22  ASN n 
1 23  LEU n 
1 24  ARG n 
1 25  ASP n 
1 26  LEU n 
1 27  THR n 
1 28  GLN n 
1 29  GLN n 
1 30  GLU n 
1 31  ARG n 
1 32  ILE n 
1 33  SER n 
1 34  LEU n 
1 35  THR n 
1 36  CYS n 
1 37  VAL n 
1 38  GLN n 
1 39  LYS n 
1 40  ALA n 
1 41  THR n 
1 42  TYR n 
1 43  LEU n 
1 44  ASP n 
1 45  CYS n 
1 46  ILE n 
1 47  LYS n 
1 48  ALA n 
1 49  ILE n 
1 50  ALA n 
1 51  ASN n 
1 52  ASN n 
1 53  GLU n 
1 54  ALA n 
1 55  ASP n 
1 56  ALA n 
1 57  ILE n 
1 58  SER n 
1 59  LEU n 
1 60  ASP n 
1 61  GLY n 
1 62  GLY n 
1 63  GLN n 
1 64  VAL n 
1 65  PHE n 
1 66  GLU n 
1 67  ALA n 
1 68  GLY n 
1 69  LEU n 
1 70  ALA n 
1 71  PRO n 
1 72  TYR n 
1 73  LYS n 
1 74  LEU n 
1 75  LYS n 
1 76  PRO n 
1 77  ILE n 
1 78  ALA n 
1 79  ALA n 
1 80  GLU n 
1 81  VAL n 
1 82  TYR n 
1 83  GLU n 
1 84  HIS n 
1 85  THR n 
1 86  GLU n 
1 87  GLY n 
1 88  SER n 
1 89  THR n 
1 90  THR n 
1 91  SER n 
1 92  TYR n 
1 93  TYR n 
1 94  ALA n 
1 95  VAL n 
1 96  ALA n 
1 97  VAL n 
1 98  VAL n 
1 99  LYS n 
1 100 LYS n 
1 101 GLY n 
1 102 THR n 
1 103 GLU n 
1 104 PHE n 
1 105 THR n 
1 106 VAL n 
1 107 ASN n 
1 108 ASP n 
1 109 LEU n 
1 110 GLN n 
1 111 GLY n 
1 112 LYS n 
1 113 THR n 
1 114 SER n 
1 115 CYS n 
1 116 HIS n 
1 117 THR n 
1 118 GLY n 
1 119 LEU n 
1 120 GLY n 
1 121 ARG n 
1 122 SER n 
1 123 ALA n 
1 124 GLY n 
1 125 TRP n 
1 126 ASN n 
1 127 ILE n 
1 128 PRO n 
1 129 ILE n 
1 130 GLY n 
1 131 THR n 
1 132 LEU n 
1 133 ILE n 
1 134 HIS n 
1 135 ARG n 
1 136 GLY n 
1 137 ALA n 
1 138 ILE n 
1 139 GLU n 
1 140 TRP n 
1 141 GLU n 
1 142 GLY n 
1 143 ILE n 
1 144 GLU n 
1 145 SER n 
1 146 GLY n 
1 147 SER n 
1 148 VAL n 
1 149 GLU n 
1 150 GLN n 
1 151 ALA n 
1 152 VAL n 
1 153 ALA n 
1 154 LYS n 
1 155 PHE n 
1 156 PHE n 
1 157 SER n 
1 158 ALA n 
1 159 SER n 
1 160 CYS n 
1 161 VAL n 
1 162 PRO n 
1 163 GLY n 
1 164 ALA n 
1 165 THR n 
1 166 ILE n 
1 167 GLU n 
1 168 GLN n 
1 169 LYS n 
1 170 LEU n 
1 171 CYS n 
1 172 ARG n 
1 173 GLN n 
1 174 CYS n 
1 175 LYS n 
1 176 GLY n 
1 177 ASP n 
1 178 PRO n 
1 179 LYS n 
1 180 THR n 
1 181 LYS n 
1 182 CYS n 
1 183 ALA n 
1 184 ARG n 
1 185 ASN n 
1 186 ALA n 
1 187 PRO n 
1 188 TYR n 
1 189 SER n 
1 190 GLY n 
1 191 TYR n 
1 192 SER n 
1 193 GLY n 
1 194 ALA n 
1 195 PHE n 
1 196 HIS n 
1 197 CYS n 
1 198 LEU n 
1 199 LYS n 
1 200 ASP n 
1 201 GLY n 
1 202 LYS n 
1 203 GLY n 
1 204 ASP n 
1 205 VAL n 
1 206 ALA n 
1 207 PHE n 
1 208 VAL n 
1 209 LYS n 
1 210 HIS n 
1 211 THR n 
1 212 THR n 
1 213 VAL n 
1 214 ASN n 
1 215 GLU n 
1 216 ASN n 
1 217 ALA n 
1 218 PRO n 
1 219 ASP n 
1 220 GLN n 
1 221 LYS n 
1 222 ASP n 
1 223 GLU n 
1 224 TYR n 
1 225 GLU n 
1 226 LEU n 
1 227 LEU n 
1 228 CYS n 
1 229 LEU n 
1 230 ASP n 
1 231 GLY n 
1 232 SER n 
1 233 ARG n 
1 234 GLN n 
1 235 PRO n 
1 236 VAL n 
1 237 ASP n 
1 238 ASN n 
1 239 TYR n 
1 240 LYS n 
1 241 THR n 
1 242 CYS n 
1 243 ASN n 
1 244 TRP n 
1 245 ALA n 
1 246 ARG n 
1 247 VAL n 
1 248 ALA n 
1 249 ALA n 
1 250 HIS n 
1 251 ALA n 
1 252 VAL n 
1 253 VAL n 
1 254 ALA n 
1 255 ARG n 
1 256 ASP n 
1 257 ASP n 
1 258 ASN n 
1 259 LYS n 
1 260 VAL n 
1 261 GLU n 
1 262 ASP n 
1 263 ILE n 
1 264 TRP n 
1 265 SER n 
1 266 PHE n 
1 267 LEU n 
1 268 SER n 
1 269 LYS n 
1 270 ALA n 
1 271 GLN n 
1 272 SER n 
1 273 ASP n 
1 274 PHE n 
1 275 GLY n 
1 276 VAL n 
1 277 ASP n 
1 278 THR n 
1 279 LYS n 
1 280 SER n 
1 281 ASP n 
1 282 PHE n 
1 283 HIS n 
1 284 LEU n 
1 285 PHE n 
1 286 GLY n 
1 287 PRO n 
1 288 PRO n 
1 289 GLY n 
1 290 LYS n 
1 291 LYS n 
1 292 ASP n 
1 293 PRO n 
1 294 VAL n 
1 295 LEU n 
1 296 LYS n 
1 297 ASP n 
1 298 LEU n 
1 299 LEU n 
1 300 PHE n 
1 301 LYS n 
1 302 ASP n 
1 303 SER n 
1 304 ALA n 
1 305 ILE n 
1 306 MET n 
1 307 LEU n 
1 308 LYS n 
1 309 ARG n 
1 310 VAL n 
1 311 PRO n 
1 312 SER n 
1 313 LEU n 
1 314 MET n 
1 315 ASP n 
1 316 SER n 
1 317 GLN n 
1 318 LEU n 
1 319 TYR n 
1 320 LEU n 
1 321 GLY n 
1 322 PHE n 
1 323 GLU n 
1 324 TYR n 
1 325 TYR n 
1 326 SER n 
1 327 ALA n 
1 328 ILE n 
1 329 GLN n 
1 330 SER n 
1 331 MET n 
1 332 ARG n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   332 
_entity_src_gen.gene_src_common_name               chicken 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 TFEW 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Gallus gallus' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9031 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Komagataella pastoris' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     4922 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               KM71 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    Q4ADJ7_CHICK 
_struct_ref.pdbx_db_accession          Q4ADJ7 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;APPKSVIRWCTISSPEEKKCNNLRDLTQQERISLTCVQKATYLDCIKAIANNEADAISLDGGQVFEAGLAPYKLKPIAAE
VYEHTEGSTTSYYAVAVVKKGTEFTVNDLQGKTSCHTGLGRSAGWNIPIGTLIHRGAIEWEGIESGSVEQAVAKFFSASC
VPGATIEQKLCRQCKGDPKTKCARNAPYSGYSGAFHCLKDGKGDVAFVKHTTVNENAPDQKDEYELLCLDGSRQPVDNYK
TCNWARVAAHAVVARDDNKVEDIWSFLSKAQSDFGVDTKSDFHLFGPPGKKDPVLKDLLFKDSAIMLKRVPSLMDSQLYL
GFEYYSAIQSMR
;
_struct_ref.pdbx_align_begin           20 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              8X3H 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 332 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q4ADJ7 
_struct_ref_seq.db_align_beg                  20 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  351 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       332 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ?                               'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ?                               'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ?                               'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ?                               'C4 H7 N O4'     133.103 
CO3 non-polymer         . 'CARBONATE ION' ?                               'C O3 -2'        60.009  
CYS 'L-peptide linking' y CYSTEINE        ?                               'C3 H7 N O2 S'   121.158 
FE  non-polymer         . 'FE (III) ION'  ?                               'Fe 3'           55.845  
GLN 'L-peptide linking' y GLUTAMINE       ?                               'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ?                               'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ?                               'C2 H5 N O2'     75.067  
GOL non-polymer         . GLYCEROL        'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'       92.094  
HIS 'L-peptide linking' y HISTIDINE       ?                               'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER           ?                               'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE      ?                               'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ?                               'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ?                               'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ?                               'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE   ?                               'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ?                               'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ?                               'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE       ?                               'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ?                               'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE        ?                               'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE          ?                               'C5 H11 N O2'    117.146 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8X3H 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.03 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          39.31 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              7.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '100mM HEPES-Na buffer, 21% PEG 3350, 200mM Sodium acetate' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     'IMAGE PLATE' 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'RIGAKU RAXIS V' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2007-12-10 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.7 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SPRING-8 BEAMLINE BL38B1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.7 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL38B1 
_diffrn_source.pdbx_synchrotron_site       SPring-8 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8X3H 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              0.93 
_reflns.d_resolution_low                               50 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     190261 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           95.4 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                7.8 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          62.5 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.045 
_reflns.pdbx_Rpim_I_all                                0.015 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.997 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    0.93 
_reflns_shell.d_res_low                                     0.95 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           5.2 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             7502 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               6.3 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               0.491 
_reflns_shell.pdbx_Rpim_I_all                               0.188 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.865 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          76.1 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 8X3H 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            0.93 
_refine.ls_d_res_low                             10 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     180290 
_refine.ls_number_reflns_R_free                  ? 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    90.58 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_R_free                       0.1237 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1029 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       0.93 
_refine_hist.d_res_low                        10 
_refine_hist.number_atoms_solvent             540 
_refine_hist.number_atoms_total               3114 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        2563 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         11 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
_struct.entry_id                     8X3H 
_struct.title                        
'Crystal structure of iron-bound recombinant ovotransferrin N-lobe at 0.93 angstrom resolution' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        8X3H 
_struct_keywords.text            'transferrin, atomic resolution, METAL TRANSPORT' 
_struct_keywords.pdbx_keywords   'METAL TRANSPORT' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 5 ? 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 SER A 13  ? GLN A 28  ? SER A 13  GLN A 28  1 ? 16 
HELX_P HELX_P2  AA2 THR A 41  ? ASN A 51  ? THR A 41  ASN A 51  1 ? 11 
HELX_P HELX_P3  AA3 ASP A 60  ? LEU A 69  ? ASP A 60  LEU A 69  1 ? 10 
HELX_P HELX_P4  AA4 THR A 105 ? LEU A 109 ? THR A 105 LEU A 109 5 ? 5  
HELX_P HELX_P5  AA5 TRP A 125 ? ARG A 135 ? TRP A 125 ARG A 135 1 ? 11 
HELX_P HELX_P6  AA6 GLY A 142 ? GLY A 146 ? GLY A 142 GLY A 146 5 ? 5  
HELX_P HELX_P7  AA7 SER A 147 ? PHE A 156 ? SER A 147 PHE A 156 1 ? 10 
HELX_P HELX_P8  AA8 GLU A 167 ? ARG A 172 ? GLU A 167 ARG A 172 5 ? 6  
HELX_P HELX_P9  AA9 SER A 189 ? ASP A 200 ? SER A 189 ASP A 200 1 ? 12 
HELX_P HELX_P10 AB1 THR A 211 ? ALA A 217 ? THR A 211 ALA A 217 1 ? 7  
HELX_P HELX_P11 AB2 PRO A 218 ? ASP A 222 ? PRO A 218 ASP A 222 5 ? 5  
HELX_P HELX_P12 AB3 ASP A 237 ? CYS A 242 ? ASP A 237 CYS A 242 5 ? 6  
HELX_P HELX_P13 AB4 LYS A 259 ? GLY A 275 ? LYS A 259 GLY A 275 1 ? 17 
HELX_P HELX_P14 AB5 ASP A 292 ? LYS A 296 ? ASP A 292 LYS A 296 5 ? 5  
HELX_P HELX_P15 AB6 ASP A 315 ? GLY A 321 ? ASP A 315 GLY A 321 1 ? 7  
HELX_P HELX_P16 AB7 GLY A 321 ? MET A 331 ? GLY A 321 MET A 331 1 ? 11 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1 disulf ? ? A CYS 10  SG  ? ? ? 1_555 A CYS 45  SG ? ? A CYS 10  A CYS 45  1_555 ? ? ? ? ? ? ? 2.051 ? ? 
disulf2 disulf ? ? A CYS 20  SG  ? ? ? 1_555 A CYS 36  SG ? ? A CYS 20  A CYS 36  1_555 ? ? ? ? ? ? ? 2.045 ? ? 
disulf3 disulf ? ? A CYS 115 SG  ? ? ? 1_555 A CYS 197 SG ? ? A CYS 115 A CYS 197 1_555 ? ? ? ? ? ? ? 2.046 ? ? 
disulf4 disulf ? ? A CYS 160 SG  ? ? ? 1_555 A CYS 174 SG ? ? A CYS 160 A CYS 174 1_555 ? ? ? ? ? ? ? 2.066 ? ? 
disulf5 disulf ? ? A CYS 171 SG  A ? ? 1_555 A CYS 182 SG A ? A CYS 171 A CYS 182 1_555 ? ? ? ? ? ? ? 2.041 ? ? 
disulf6 disulf ? ? A CYS 171 SG  B ? ? 1_555 A CYS 182 SG B ? A CYS 171 A CYS 182 1_555 ? ? ? ? ? ? ? 2.025 ? ? 
disulf7 disulf ? ? A CYS 228 SG  ? ? ? 1_555 A CYS 242 SG ? ? A CYS 228 A CYS 242 1_555 ? ? ? ? ? ? ? 2.041 ? ? 
metalc1 metalc ? ? A ASP 60  OD1 ? ? ? 1_555 B FE  .   FE ? ? A ASP 60  A FE  401 1_555 ? ? ? ? ? ? ? 2.123 ? ? 
metalc2 metalc ? ? A TYR 92  OH  ? ? ? 1_555 B FE  .   FE ? ? A TYR 92  A FE  401 1_555 ? ? ? ? ? ? ? 1.993 ? ? 
metalc3 metalc ? ? A TYR 191 OH  ? ? ? 1_555 B FE  .   FE ? ? A TYR 191 A FE  401 1_555 ? ? ? ? ? ? ? 2.012 ? ? 
metalc4 metalc ? ? A HIS 250 NE2 ? ? ? 1_555 B FE  .   FE ? ? A HIS 250 A FE  401 1_555 ? ? ? ? ? ? ? 2.152 ? ? 
metalc5 metalc ? ? B FE  .   FE  ? ? ? 1_555 C CO3 .   O1 ? ? A FE  401 A CO3 402 1_555 ? ? ? ? ? ? ? 2.174 ? ? 
metalc6 metalc ? ? B FE  .   FE  ? ? ? 1_555 C CO3 .   O3 ? ? A FE  401 A CO3 402 1_555 ? ? ? ? ? ? ? 2.100 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
metalc ? ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 ALA 70  A . ? ALA 70  A PRO 71  A ? PRO 71  A 1 5.57 
2 GLY 286 A . ? GLY 286 A PRO 287 A ? PRO 287 A 1 4.99 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 4 ? 
AA3 ? 4 ? 
AA4 ? 6 ? 
AA5 ? 5 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel      
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA4 1 2 ? parallel      
AA4 2 3 ? parallel      
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA4 5 6 ? anti-parallel 
AA5 1 2 ? parallel      
AA5 2 3 ? parallel      
AA5 3 4 ? anti-parallel 
AA5 4 5 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 SER A 5   ? THR A 11  ? SER A 5   THR A 11  
AA1 2 ILE A 32  ? GLN A 38  ? ILE A 32  GLN A 38  
AA2 1 ILE A 57  ? LEU A 59  ? ILE A 57  LEU A 59  
AA2 2 ALA A 251 ? ALA A 254 ? ALA A 251 ALA A 254 
AA2 3 LYS A 75  ? HIS A 84  ? LYS A 75  HIS A 84  
AA2 4 GLY A 87  ? THR A 89  ? GLY A 87  THR A 89  
AA3 1 ILE A 57  ? LEU A 59  ? ILE A 57  LEU A 59  
AA3 2 ALA A 251 ? ALA A 254 ? ALA A 251 ALA A 254 
AA3 3 LYS A 75  ? HIS A 84  ? LYS A 75  HIS A 84  
AA3 4 ALA A 304 ? ARG A 309 ? ALA A 304 ARG A 309 
AA4 1 ALA A 158 ? CYS A 160 ? ALA A 158 CYS A 160 
AA4 2 THR A 113 ? HIS A 116 ? THR A 113 HIS A 116 
AA4 3 VAL A 205 ? LYS A 209 ? VAL A 205 LYS A 209 
AA4 4 SER A 91  ? LYS A 99  ? SER A 91  LYS A 99  
AA4 5 TYR A 224 ? LEU A 227 ? TYR A 224 LEU A 227 
AA4 6 ARG A 233 ? PRO A 235 ? ARG A 233 PRO A 235 
AA5 1 ALA A 158 ? CYS A 160 ? ALA A 158 CYS A 160 
AA5 2 THR A 113 ? HIS A 116 ? THR A 113 HIS A 116 
AA5 3 VAL A 205 ? LYS A 209 ? VAL A 205 LYS A 209 
AA5 4 SER A 91  ? LYS A 99  ? SER A 91  LYS A 99  
AA5 5 ALA A 245 ? ALA A 248 ? ALA A 245 ALA A 248 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N TRP A 9   ? N TRP A 9   O THR A 35  ? O THR A 35  
AA2 1 2 N LEU A 59  ? N LEU A 59  O ALA A 251 ? O ALA A 251 
AA2 2 3 O VAL A 252 ? O VAL A 252 N ILE A 77  ? N ILE A 77  
AA2 3 4 N TYR A 82  ? N TYR A 82  O THR A 89  ? O THR A 89  
AA3 1 2 N LEU A 59  ? N LEU A 59  O ALA A 251 ? O ALA A 251 
AA3 2 3 O VAL A 252 ? O VAL A 252 N ILE A 77  ? N ILE A 77  
AA3 3 4 N VAL A 81  ? N VAL A 81  O ILE A 305 ? O ILE A 305 
AA4 1 2 O CYS A 160 ? O CYS A 160 N HIS A 116 ? N HIS A 116 
AA4 2 3 N CYS A 115 ? N CYS A 115 O PHE A 207 ? O PHE A 207 
AA4 3 4 O ALA A 206 ? O ALA A 206 N VAL A 97  ? N VAL A 97  
AA4 4 5 N VAL A 98  ? N VAL A 98  O GLU A 225 ? O GLU A 225 
AA4 5 6 N LEU A 226 ? N LEU A 226 O GLN A 234 ? O GLN A 234 
AA5 1 2 O CYS A 160 ? O CYS A 160 N HIS A 116 ? N HIS A 116 
AA5 2 3 N CYS A 115 ? N CYS A 115 O PHE A 207 ? O PHE A 207 
AA5 3 4 O ALA A 206 ? O ALA A 206 N VAL A 97  ? N VAL A 97  
AA5 4 5 N TYR A 92  ? N TYR A 92  O VAL A 247 ? O VAL A 247 
# 
_atom_sites.entry_id                    8X3H 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.021577 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.013242 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.011814 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
FE 
H  
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N    . ALA A 1 1   ? 6.511  35.668  24.956 1.000 46.84 ? 1    ALA A N    1 
ATOM   2    C  CA   . ALA A 1 1   ? 7.517  34.611  25.030 1.000 42.16 ? 1    ALA A CA   1 
ATOM   3    C  C    . ALA A 1 1   ? 8.082  34.289  23.653 1.000 35.86 ? 1    ALA A C    1 
ATOM   4    O  O    . ALA A 1 1   ? 7.537  34.624  22.593 1.000 41.38 ? 1    ALA A O    1 
ATOM   5    C  CB   . ALA A 1 1   ? 6.962  33.352  25.671 1.000 44.48 ? 1    ALA A CB   1 
ATOM   6    N  N    . PRO A 1 2   ? 9.388  33.501  23.961 1.000 31.74 ? 2    PRO A N    1 
ATOM   7    C  CA   . PRO A 1 2   ? 10.058 33.317  22.639 1.000 24.03 ? 2    PRO A CA   1 
ATOM   8    C  C    . PRO A 1 2   ? 9.208  32.437  21.727 1.000 21.41 ? 2    PRO A C    1 
ATOM   9    O  O    . PRO A 1 2   ? 8.233  31.899  22.175 1.000 25.97 ? 2    PRO A O    1 
ATOM   10   C  CB   . PRO A 1 2   ? 11.351 32.567  22.999 1.000 23.72 ? 2    PRO A CB   1 
ATOM   11   C  CG   . PRO A 1 2   ? 11.574 33.015  24.437 1.000 32.12 ? 2    PRO A CG   1 
ATOM   12   C  CD   . PRO A 1 2   ? 10.181 32.894  25.058 1.000 32.12 ? 2    PRO A CD   1 
ATOM   13   N  N    . PRO A 1 3   ? 9.613  32.282  20.421 1.000 22.25 ? 3    PRO A N    1 
ATOM   14   C  CA   . PRO A 1 3   ? 8.786  31.482  19.535 1.000 20.07 ? 3    PRO A CA   1 
ATOM   15   C  C    . PRO A 1 3   ? 8.715  29.989  19.946 1.000 15.43 ? 3    PRO A C    1 
ATOM   16   O  O    . PRO A 1 3   ? 9.554  29.479  20.689 1.000 17.97 ? 3    PRO A O    1 
ATOM   17   C  CB   . PRO A 1 3   ? 9.507  31.681  18.183 1.000 22.27 ? 3    PRO A CB   1 
ATOM   18   C  CG   . PRO A 1 3   ? 10.228 32.999  18.340 1.000 25.64 ? 3    PRO A CG   1 
ATOM   19   C  CD   . PRO A 1 3   ? 10.772 32.907  19.764 1.000 27.16 ? 3    PRO A CD   1 
ATOM   20   N  N    . LYS A 1 4   ? 7.667  29.339  19.379 1.000 17.01 ? 4    LYS A N    1 
ATOM   21   C  CA   A LYS A 1 4   ? 7.607  27.895  19.517 0.503 13.86 ? 4    LYS A CA   1 
ATOM   22   C  CA   B LYS A 1 4   ? 7.563  27.893  19.448 0.497 14.51 ? 4    LYS A CA   1 
ATOM   23   C  C    . LYS A 1 4   ? 8.765  27.145  18.889 1.000 14.38 ? 4    LYS A C    1 
ATOM   24   O  O    . LYS A 1 4   ? 9.377  27.550  17.907 1.000 16.48 ? 4    LYS A O    1 
ATOM   25   C  CB   A LYS A 1 4   ? 6.326  27.418  18.823 0.503 14.80 ? 4    LYS A CB   1 
ATOM   26   C  CB   B LYS A 1 4   ? 6.348  27.439  18.626 0.497 15.81 ? 4    LYS A CB   1 
ATOM   27   C  CG   A LYS A 1 4   ? 5.060  28.042  19.396 0.503 18.31 ? 4    LYS A CG   1 
ATOM   28   C  CG   B LYS A 1 4   ? 5.025  27.737  19.314 0.497 17.04 ? 4    LYS A CG   1 
ATOM   29   C  CD   A LYS A 1 4   ? 3.853  27.598  18.564 0.503 19.71 ? 4    LYS A CD   1 
ATOM   30   C  CD   B LYS A 1 4   ? 3.896  26.940  18.655 0.497 18.49 ? 4    LYS A CD   1 
ATOM   31   C  CE   A LYS A 1 4   ? 3.849  26.088  18.401 0.503 20.79 ? 4    LYS A CE   1 
ATOM   32   C  CE   B LYS A 1 4   ? 2.627  27.083  19.502 0.497 18.92 ? 4    LYS A CE   1 
ATOM   33   N  NZ   A LYS A 1 4   ? 2.462  25.548  18.227 0.503 28.42 ? 4    LYS A NZ   1 
ATOM   34   N  NZ   B LYS A 1 4   ? 1.546  26.217  18.928 0.497 18.72 ? 4    LYS A NZ   1 
ATOM   35   N  N    . SER A 1 5   ? 9.048  25.973  19.517 1.000 10.37 ? 5    SER A N    1 
ATOM   36   C  CA   . SER A 1 5   ? 10.089 25.079  18.965 1.000 9.20  ? 5    SER A CA   1 
ATOM   37   C  C    . SER A 1 5   ? 9.761  23.653  19.464 1.000 7.71  ? 5    SER A C    1 
ATOM   38   O  O    . SER A 1 5   ? 8.765  23.447  20.153 1.000 9.01  ? 5    SER A O    1 
ATOM   39   C  CB   . SER A 1 5   ? 11.453 25.596  19.356 1.000 9.28  ? 5    SER A CB   1 
ATOM   40   O  OG   . SER A 1 5   ? 12.489 24.848  18.782 1.000 9.44  ? 5    SER A OG   1 
ATOM   41   H  HB2  . SER A 1 5   ? 11.535 26.521  19.076 1.000 11.13 ? 5    SER A HB2  1 
ATOM   42   H  HB3  . SER A 1 5   ? 11.539 25.569  20.322 1.000 11.13 ? 5    SER A HB3  1 
ATOM   43   H  HG   . SER A 1 5   ? 12.428 24.879  17.965 1.000 14.16 ? 5    SER A HG   1 
ATOM   44   N  N    . VAL A 1 6   ? 10.625 22.710  19.121 1.000 7.77  ? 6    VAL A N    1 
ATOM   45   C  CA   . VAL A 1 6   ? 10.436 21.300  19.391 1.000 7.38  ? 6    VAL A CA   1 
ATOM   46   C  C    . VAL A 1 6   ? 11.695 20.747  20.020 1.000 7.15  ? 6    VAL A C    1 
ATOM   47   O  O    . VAL A 1 6   ? 12.793 21.195  19.680 1.000 7.89  ? 6    VAL A O    1 
ATOM   48   C  CB   . VAL A 1 6   ? 10.135 20.550  18.071 1.000 9.06  ? 6    VAL A CB   1 
ATOM   49   C  CG1  . VAL A 1 6   ? 9.897  19.081  18.300 1.000 11.56 ? 6    VAL A CG1  1 
ATOM   50   C  CG2  . VAL A 1 6   ? 8.970  21.206  17.330 1.000 11.07 ? 6    VAL A CG2  1 
ATOM   51   H  HA   . VAL A 1 6   ? 9.685  21.185  20.010 1.000 8.85  ? 6    VAL A HA   1 
ATOM   52   H  HG22 . VAL A 1 6   ? 8.861  20.783  16.475 1.000 16.61 ? 6    VAL A HG22 1 
ATOM   53   N  N    . ILE A 1 7   ? 11.570 19.786  20.926 1.000 6.32  ? 7    ILE A N    1 
ATOM   54   C  CA   . ILE A 1 7   ? 12.694 18.996  21.381 1.000 6.60  ? 7    ILE A CA   1 
ATOM   55   C  C    . ILE A 1 7   ? 12.473 17.551  20.957 1.000 6.33  ? 7    ILE A C    1 
ATOM   56   O  O    . ILE A 1 7   ? 11.356 17.067  20.858 1.000 6.96  ? 7    ILE A O    1 
ATOM   57   C  CB   . ILE A 1 7   ? 12.938 19.098  22.902 1.000 6.78  ? 7    ILE A CB   1 
ATOM   58   C  CG1  . ILE A 1 7   ? 11.825 18.462  23.723 1.000 8.23  ? 7    ILE A CG1  1 
ATOM   59   C  CG2  . ILE A 1 7   ? 13.193 20.531  23.308 1.000 7.96  ? 7    ILE A CG2  1 
ATOM   60   C  CD1  . ILE A 1 7   ? 12.244 18.154  25.152 1.000 8.26  ? 7    ILE A CD1  1 
ATOM   61   H  H    . ILE A 1 7   ? 10.791 19.626  21.255 1.000 7.59  ? 7    ILE A H    1 
ATOM   62   H  HB   . ILE A 1 7   ? 13.757 18.597  23.095 1.000 8.13  ? 7    ILE A HB   1 
ATOM   63   H  HG12 . ILE A 1 7   ? 11.069 19.069  23.737 1.000 9.88  ? 7    ILE A HG12 1 
ATOM   64   H  HG23 . ILE A 1 7   ? 13.452 20.557  24.232 1.000 11.93 ? 7    ILE A HG23 1 
ATOM   65   N  N    . ARG A 1 8   ? 13.594 16.865  20.711 1.000 6.26  ? 8    ARG A N    1 
ATOM   66   C  CA   . ARG A 1 8   ? 13.611 15.477  20.272 1.000 6.21  ? 8    ARG A CA   1 
ATOM   67   C  C    . ARG A 1 8   ? 14.192 14.618  21.372 1.000 5.50  ? 8    ARG A C    1 
ATOM   68   O  O    . ARG A 1 8   ? 15.377 14.682  21.711 1.000 6.80  ? 8    ARG A O    1 
ATOM   69   C  CB   . ARG A 1 8   ? 14.475 15.327  19.019 1.000 6.79  ? 8    ARG A CB   1 
ATOM   70   C  CG   . ARG A 1 8   ? 14.017 16.211  17.860 1.000 8.06  ? 8    ARG A CG   1 
ATOM   71   C  CD   . ARG A 1 8   ? 15.059 16.391  16.770 1.000 9.01  ? 8    ARG A CD   1 
ATOM   72   N  NE   . ARG A 1 8   ? 16.226 17.065  17.291 1.000 8.44  ? 8    ARG A NE   1 
ATOM   73   C  CZ   . ARG A 1 8   ? 17.327 17.316  16.636 1.000 8.34  ? 8    ARG A CZ   1 
ATOM   74   N  NH1  . ARG A 1 8   ? 17.449 16.951  15.377 1.000 11.22 ? 8    ARG A NH1  1 
ATOM   75   N  NH2  . ARG A 1 8   ? 18.328 17.901  17.262 1.000 8.52  ? 8    ARG A NH2  1 
ATOM   76   H  H    . ARG A 1 8   ? 14.347 17.266  20.818 1.000 7.51  ? 8    ARG A H    1 
ATOM   77   H  HA   . ARG A 1 8   ? 12.696 15.184  20.076 1.000 7.46  ? 8    ARG A HA   1 
ATOM   78   H  HB2  . ARG A 1 8   ? 15.392 15.550  19.241 1.000 8.15  ? 8    ARG A HB2  1 
ATOM   79   H  HB3  . ARG A 1 8   ? 14.457 14.400  18.733 1.000 8.15  ? 8    ARG A HB3  1 
ATOM   80   H  HG2  . ARG A 1 8   ? 13.282 15.764  17.463 1.000 9.67  ? 8    ARG A HG2  1 
ATOM   81   H  HD2  . ARG A 1 8   ? 15.319 15.523  16.424 1.000 10.82 ? 8    ARG A HD2  1 
ATOM   82   H  HE   . ARG A 1 8   ? 16.193 17.326  18.110 1.000 10.13 ? 8    ARG A HE   1 
ATOM   83   H  HH11 . ARG A 1 8   ? 16.801 16.546  14.982 1.000 13.46 ? 8    ARG A HH11 1 
ATOM   84   H  HH12 . ARG A 1 8   ? 18.176 17.118  14.950 1.000 13.46 ? 8    ARG A HH12 1 
ATOM   85   N  N    . TRP A 1 9   ? 13.341 13.781  21.971 1.000 5.66  ? 9    TRP A N    1 
ATOM   86   C  CA   . TRP A 1 9   ? 13.776 12.874  23.042 1.000 5.38  ? 9    TRP A CA   1 
ATOM   87   C  C    . TRP A 1 9   ? 14.223 11.572  22.437 1.000 5.80  ? 9    TRP A C    1 
ATOM   88   O  O    . TRP A 1 9   ? 13.578 11.064  21.498 1.000 7.94  ? 9    TRP A O    1 
ATOM   89   C  CB   . TRP A 1 9   ? 12.617 12.607  24.031 1.000 5.88  ? 9    TRP A CB   1 
ATOM   90   C  CG   . TRP A 1 9   ? 13.166 12.213  25.363 1.000 5.40  ? 9    TRP A CG   1 
ATOM   91   C  CD1  . TRP A 1 9   ? 13.506 11.005  25.844 1.000 6.04  ? 9    TRP A CD1  1 
ATOM   92   C  CD2  . TRP A 1 9   ? 13.503 13.139  26.416 1.000 5.54  ? 9    TRP A CD2  1 
ATOM   93   N  NE1  . TRP A 1 9   ? 14.036 11.075  27.104 1.000 5.96  ? 9    TRP A NE1  1 
ATOM   94   C  CE2  . TRP A 1 9   ? 14.040 12.403  27.488 1.000 5.62  ? 9    TRP A CE2  1 
ATOM   95   C  CE3  . TRP A 1 9   ? 13.384 14.540  26.558 1.000 5.80  ? 9    TRP A CE3  1 
ATOM   96   C  CZ2  . TRP A 1 9   ? 14.477 13.000  28.660 1.000 6.09  ? 9    TRP A CZ2  1 
ATOM   97   C  CZ3  . TRP A 1 9   ? 13.819 15.126  27.715 1.000 6.44  ? 9    TRP A CZ3  1 
ATOM   98   C  CH2  . TRP A 1 9   ? 14.348 14.352  28.744 1.000 6.38  ? 9    TRP A CH2  1 
ATOM   99   H  H    . TRP A 1 9   ? 12.517 13.773  21.724 1.000 6.79  ? 9    TRP A H    1 
ATOM   100  H  HA   . TRP A 1 9   ? 14.525 13.280  23.524 1.000 6.46  ? 9    TRP A HA   1 
ATOM   101  H  HB2  . TRP A 1 9   ? 12.077 13.407  24.124 1.000 7.05  ? 9    TRP A HB2  1 
ATOM   102  H  HB3  . TRP A 1 9   ? 12.051 11.898  23.688 1.000 7.05  ? 9    TRP A HB3  1 
ATOM   103  H  HD1  . TRP A 1 9   ? 13.395 10.210  25.373 1.000 7.25  ? 9    TRP A HD1  1 
ATOM   104  H  HE1  . TRP A 1 9   ? 14.317 10.411  27.573 1.000 7.15  ? 9    TRP A HE1  1 
ATOM   105  H  HE3  . TRP A 1 9   ? 13.016 15.054  25.876 1.000 6.96  ? 9    TRP A HE3  1 
ATOM   106  H  HZ3  . TRP A 1 9   ? 13.762 16.049  27.814 1.000 7.73  ? 9    TRP A HZ3  1 
ATOM   107  H  HH2  . TRP A 1 9   ? 14.624 14.777  29.524 1.000 7.66  ? 9    TRP A HH2  1 
ATOM   108  N  N    . CYS A 1 10  ? 15.300 10.976  22.986 1.000 5.40  ? 10   CYS A N    1 
ATOM   109  C  CA   . CYS A 1 10  ? 15.811 9.712   22.470 1.000 5.50  ? 10   CYS A CA   1 
ATOM   110  C  C    . CYS A 1 10  ? 15.472 8.581   23.448 1.000 5.41  ? 10   CYS A C    1 
ATOM   111  O  O    . CYS A 1 10  ? 15.806 8.649   24.631 1.000 6.11  ? 10   CYS A O    1 
ATOM   112  C  CB   . CYS A 1 10  ? 17.319 9.837   22.211 1.000 6.14  ? 10   CYS A CB   1 
ATOM   113  S  SG   . CYS A 1 10  ? 17.920 8.559   21.086 1.000 7.13  ? 10   CYS A SG   1 
ATOM   114  H  H    . CYS A 1 10  ? 15.693 11.348  23.654 1.000 6.48  ? 10   CYS A H    1 
ATOM   115  H  HA   . CYS A 1 10  ? 15.367 9.525   21.616 1.000 6.60  ? 10   CYS A HA   1 
ATOM   116  H  HB2  . CYS A 1 10  ? 17.507 10.710  21.832 1.000 7.37  ? 10   CYS A HB2  1 
ATOM   117  H  HB3  . CYS A 1 10  ? 17.795 9.770   23.054 1.000 7.37  ? 10   CYS A HB3  1 
ATOM   118  N  N    . THR A 1 11  ? 14.764 7.593   22.919 1.000 5.61  ? 11   THR A N    1 
ATOM   119  C  CA   . THR A 1 11  ? 14.268 6.487   23.693 1.000 5.79  ? 11   THR A CA   1 
ATOM   120  C  C    . THR A 1 11  ? 15.041 5.205   23.346 1.000 6.24  ? 11   THR A C    1 
ATOM   121  O  O    . THR A 1 11  ? 15.657 5.110   22.283 1.000 6.42  ? 11   THR A O    1 
ATOM   122  C  CB   . THR A 1 11  ? 12.754 6.270   23.432 1.000 6.20  ? 11   THR A CB   1 
ATOM   123  O  OG1  . THR A 1 11  ? 12.557 5.834   22.103 1.000 6.73  ? 11   THR A OG1  1 
ATOM   124  C  CG2  . THR A 1 11  ? 11.967 7.526   23.752 1.000 7.50  ? 11   THR A CG2  1 
ATOM   125  H  H    . THR A 1 11  ? 14.593 7.615   22.076 1.000 6.74  ? 11   THR A H    1 
ATOM   126  H  HA   . THR A 1 11  ? 14.398 6.685   24.644 1.000 6.94  ? 11   THR A HA   1 
ATOM   127  H  HB   . THR A 1 11  ? 12.444 5.560   24.031 1.000 7.44  ? 11   THR A HB   1 
ATOM   128  H  HG1  . THR A 1 11  ? 12.042 6.345   21.721 1.000 10.10 ? 11   THR A HG1  1 
ATOM   129  N  N    . ILE A 1 12  ? 14.977 4.235   24.274 1.000 5.79  ? 12   ILE A N    1 
ATOM   130  C  CA   . ILE A 1 12  ? 15.836 3.033   24.194 1.000 6.51  ? 12   ILE A CA   1 
ATOM   131  C  C    . ILE A 1 12  ? 15.036 1.752   24.168 1.000 6.80  ? 12   ILE A C    1 
ATOM   132  O  O    . ILE A 1 12  ? 15.617 0.674   24.313 1.000 7.62  ? 12   ILE A O    1 
ATOM   133  C  CB   . ILE A 1 12  ? 16.968 3.081   25.249 1.000 6.76  ? 12   ILE A CB   1 
ATOM   134  C  CG1  . ILE A 1 12  ? 16.493 3.243   26.658 1.000 7.02  ? 12   ILE A CG1  1 
ATOM   135  C  CG2  . ILE A 1 12  ? 17.948 4.203   24.871 1.000 8.19  ? 12   ILE A CG2  1 
ATOM   136  C  CD1  . ILE A 1 12  ? 15.486 2.243   27.210 1.000 8.02  ? 12   ILE A CD1  1 
ATOM   137  H  H    . ILE A 1 12  ? 14.425 4.315   24.928 1.000 6.95  ? 12   ILE A H    1 
ATOM   138  H  HA   . ILE A 1 12  ? 16.283 3.084   23.323 1.000 7.81  ? 12   ILE A HA   1 
ATOM   139  H  HB   . ILE A 1 12  ? 17.456 2.232   25.198 1.000 8.11  ? 12   ILE A HB   1 
ATOM   140  H  HG12 . ILE A 1 12  ? 17.272 3.224   27.236 1.000 8.42  ? 12   ILE A HG12 1 
ATOM   141  H  HG13 . ILE A 1 12  ? 16.102 4.127   26.736 1.000 8.42  ? 12   ILE A HG13 1 
ATOM   142  H  HD11 . ILE A 1 12  ? 15.274 2.471   28.119 1.000 12.04 ? 12   ILE A HD11 1 
ATOM   143  H  HD12 . ILE A 1 12  ? 14.686 2.268   26.679 1.000 12.04 ? 12   ILE A HD12 1 
ATOM   144  H  HD13 . ILE A 1 12  ? 15.862 1.361   27.181 1.000 12.04 ? 12   ILE A HD13 1 
ATOM   145  N  N    . SER A 1 13  ? 13.705 1.847   23.970 1.000 6.94  ? 13   SER A N    1 
ATOM   146  C  CA   . SER A 1 13  ? 12.857 0.671   23.903 1.000 7.65  ? 13   SER A CA   1 
ATOM   147  C  C    . SER A 1 13  ? 11.530 1.090   23.325 1.000 7.02  ? 13   SER A C    1 
ATOM   148  O  O    . SER A 1 13  ? 11.175 2.274   23.319 1.000 7.17  ? 13   SER A O    1 
ATOM   149  C  CB   . SER A 1 13  ? 12.628 0.068   25.269 1.000 7.80  ? 13   SER A CB   1 
ATOM   150  O  OG   . SER A 1 13  ? 11.745 0.885   26.030 1.000 7.77  ? 13   SER A OG   1 
ATOM   151  H  H    . SER A 1 13  ? 13.350 2.625   23.881 1.000 8.33  ? 13   SER A H    1 
ATOM   152  H  HA   . SER A 1 13  ? 13.271 0.003   23.317 1.000 9.18  ? 13   SER A HA   1 
ATOM   153  H  HB2  . SER A 1 13  ? 12.249 -0.819  25.174 1.000 9.36  ? 13   SER A HB2  1 
ATOM   154  H  HB3  . SER A 1 13  ? 13.476 -0.014  25.734 1.000 9.36  ? 13   SER A HB3  1 
ATOM   155  N  N    . SER A 1 14  ? 10.787 0.099   22.859 1.000 8.56  ? 14   SER A N    1 
ATOM   156  C  CA   . SER A 1 14  ? 9.457  0.413   22.347 1.000 8.53  ? 14   SER A CA   1 
ATOM   157  C  C    . SER A 1 14  ? 8.498  0.905   23.422 1.000 8.05  ? 14   SER A C    1 
ATOM   158  O  O    . SER A 1 14  ? 7.755  1.869   23.176 1.000 7.80  ? 14   SER A O    1 
ATOM   159  C  CB   . SER A 1 14  ? 8.882  -0.787  21.578 1.000 11.52 ? 14   SER A CB   1 
ATOM   160  O  OG   . SER A 1 14  ? 9.642  -0.945  20.406 1.000 16.37 ? 14   SER A OG   1 
ATOM   161  H  HA   . SER A 1 14  ? 9.563  1.143   21.702 1.000 10.24 ? 14   SER A HA   1 
ATOM   162  H  HB2  . SER A 1 14  ? 8.934  -1.588  22.122 1.000 13.83 ? 14   SER A HB2  1 
ATOM   163  H  HB3  . SER A 1 14  ? 7.952  -0.626  21.355 1.000 13.83 ? 14   SER A HB3  1 
ATOM   164  N  N    . PRO A 1 15  ? 8.491  0.354   24.636 1.000 8.33  ? 15   PRO A N    1 
ATOM   165  C  CA   . PRO A 1 15  ? 7.644  0.917   25.692 1.000 8.44  ? 15   PRO A CA   1 
ATOM   166  C  C    . PRO A 1 15  ? 8.020  2.376   25.967 1.000 7.09  ? 15   PRO A C    1 
ATOM   167  O  O    . PRO A 1 15  ? 7.131  3.195   26.220 1.000 7.28  ? 15   PRO A O    1 
ATOM   168  C  CB   . PRO A 1 15  ? 7.845  -0.028  26.890 1.000 9.94  ? 15   PRO A CB   1 
ATOM   169  C  CG   . PRO A 1 15  ? 8.143  -1.341  26.216 1.000 11.04 ? 15   PRO A CG   1 
ATOM   170  C  CD   . PRO A 1 15  ? 9.059  -0.965  25.052 1.000 9.69  ? 15   PRO A CD   1 
ATOM   171  H  HA   . PRO A 1 15  ? 6.708  0.877   25.406 1.000 10.13 ? 15   PRO A HA   1 
ATOM   172  H  HB2  . PRO A 1 15  ? 8.574  0.267   27.458 1.000 11.92 ? 15   PRO A HB2  1 
ATOM   173  H  HG2  . PRO A 1 15  ? 8.590  -1.949  26.826 1.000 13.25 ? 15   PRO A HG2  1 
ATOM   174  H  HG3  . PRO A 1 15  ? 7.329  -1.758  25.895 1.000 13.25 ? 15   PRO A HG3  1 
ATOM   175  N  N    . GLU A 1 16  ? 9.324  2.692   25.960 1.000 6.64  ? 16   GLU A N    1 
ATOM   176  C  CA   . GLU A 1 16  ? 9.687  4.076   26.147 1.000 6.13  ? 16   GLU A CA   1 
ATOM   177  C  C    . GLU A 1 16  ? 9.171  4.964   25.015 1.000 5.86  ? 16   GLU A C    1 
ATOM   178  O  O    . GLU A 1 16  ? 8.709  6.085   25.264 1.000 6.12  ? 16   GLU A O    1 
ATOM   179  C  CB   . GLU A 1 16  ? 11.204 4.279   26.226 1.000 6.60  ? 16   GLU A CB   1 
ATOM   180  C  CG   . GLU A 1 16  ? 11.820 4.027   27.593 1.000 7.07  ? 16   GLU A CG   1 
ATOM   181  C  CD   . GLU A 1 16  ? 13.140 4.752   27.774 1.000 6.35  ? 16   GLU A CD   1 
ATOM   182  O  OE1  . GLU A 1 16  ? 13.522 4.835   28.946 1.000 6.61  ? 16   GLU A OE1  1 
ATOM   183  O  OE2  . GLU A 1 16  ? 13.770 5.194   26.773 1.000 6.36  ? 16   GLU A OE2  1 
ATOM   184  H  HA   . GLU A 1 16  ? 9.290  4.387   26.988 1.000 7.36  ? 16   GLU A HA   1 
ATOM   185  H  HG3  . GLU A 1 16  ? 11.961 3.073   27.700 1.000 8.48  ? 16   GLU A HG3  1 
ATOM   186  N  N    . GLU A 1 17  ? 9.338  4.503   23.772 1.000 6.41  ? 17   GLU A N    1 
ATOM   187  C  CA   . GLU A 1 17  ? 8.861  5.293   22.641 1.000 6.55  ? 17   GLU A CA   1 
ATOM   188  C  C    . GLU A 1 17  ? 7.365  5.558   22.752 1.000 6.37  ? 17   GLU A C    1 
ATOM   189  O  O    . GLU A 1 17  ? 6.891  6.658   22.464 1.000 7.27  ? 17   GLU A O    1 
ATOM   190  C  CB   . GLU A 1 17  ? 9.266  4.601   21.348 1.000 7.48  ? 17   GLU A CB   1 
ATOM   191  C  CG   . GLU A 1 17  ? 8.850  5.340   20.082 1.000 8.49  ? 17   GLU A CG   1 
ATOM   192  C  CD   . GLU A 1 17  ? 9.680  6.573   19.746 1.000 8.20  ? 17   GLU A CD   1 
ATOM   193  O  OE1  . GLU A 1 17  ? 10.581 6.996   20.465 1.000 8.87  ? 17   GLU A OE1  1 
ATOM   194  O  OE2  . GLU A 1 17  ? 9.313  7.158   18.650 1.000 9.59  ? 17   GLU A OE2  1 
ATOM   195  H  H    . GLU A 1 17  ? 9.725  3.746   23.639 1.000 7.70  ? 17   GLU A H    1 
ATOM   196  H  HA   . GLU A 1 17  ? 9.319  6.159   22.670 1.000 7.86  ? 17   GLU A HA   1 
ATOM   197  H  HB2  . GLU A 1 17  ? 10.230 4.493   21.342 1.000 8.98  ? 17   GLU A HB2  1 
ATOM   198  H  HB3  . GLU A 1 17  ? 8.871  3.715   21.334 1.000 8.98  ? 17   GLU A HB3  1 
ATOM   199  H  HG2  . GLU A 1 17  ? 8.924  4.724   19.337 1.000 10.19 ? 17   GLU A HG2  1 
ATOM   200  N  N    . LYS A 1 18  ? 6.605  4.549   23.161 1.000 6.87  ? 18   LYS A N    1 
ATOM   201  C  CA   . LYS A 1 18  ? 5.164  4.655   23.317 1.000 7.02  ? 18   LYS A CA   1 
ATOM   202  C  C    . LYS A 1 18  ? 4.840  5.703   24.397 1.000 6.31  ? 18   LYS A C    1 
ATOM   203  O  O    . LYS A 1 18  ? 3.952  6.557   24.204 1.000 7.06  ? 18   LYS A O    1 
ATOM   204  C  CB   . LYS A 1 18  ? 4.554  3.318   23.622 1.000 8.10  ? 18   LYS A CB   1 
ATOM   205  C  CG   . LYS A 1 18  ? 3.057  3.334   23.737 1.000 10.47 ? 18   LYS A CG   1 
ATOM   206  C  CD   . LYS A 1 18  ? 2.470  1.973   24.065 1.000 16.66 ? 18   LYS A CD   1 
ATOM   207  C  CE   . LYS A 1 18  ? 0.914  1.940   24.115 1.000 24.98 ? 18   LYS A CE   1 
ATOM   208  N  NZ   . LYS A 1 18  ? 0.448  0.523   24.029 1.000 34.44 ? 18   LYS A NZ   1 
ATOM   209  H  H    . LYS A 1 18  ? 6.983  3.799   23.343 1.000 8.24  ? 18   LYS A H    1 
ATOM   210  H  HA   . LYS A 1 18  ? 4.790  4.971   22.468 1.000 8.42  ? 18   LYS A HA   1 
ATOM   211  H  HB2  . LYS A 1 18  ? 4.805  2.694   22.923 1.000 9.72  ? 18   LYS A HB2  1 
ATOM   212  H  HB3  . LYS A 1 18  ? 4.926  2.989   24.456 1.000 9.72  ? 18   LYS A HB3  1 
ATOM   213  H  HG2  . LYS A 1 18  ? 2.801  3.964   24.429 1.000 12.57 ? 18   LYS A HG2  1 
ATOM   214  H  HG3  . LYS A 1 18  ? 2.680  3.646   22.899 1.000 12.57 ? 18   LYS A HG3  1 
ATOM   215  N  N    . LYS A 1 19  ? 5.500  5.647   25.530 1.000 5.98  ? 19   LYS A N    1 
ATOM   216  C  CA   . LYS A 1 19  ? 5.287  6.645   26.590 1.000 5.70  ? 19   LYS A CA   1 
ATOM   217  C  C    . LYS A 1 19  ? 5.635  8.043   26.085 1.000 5.84  ? 19   LYS A C    1 
ATOM   218  O  O    . LYS A 1 19  ? 4.897  9.013   26.314 1.000 6.16  ? 19   LYS A O    1 
ATOM   219  C  CB   . LYS A 1 19  ? 6.095  6.294   27.823 1.000 6.07  ? 19   LYS A CB   1 
ATOM   220  C  CG   . LYS A 1 19  ? 5.918  7.288   28.950 1.000 5.73  ? 19   LYS A CG   1 
ATOM   221  C  CD   . LYS A 1 19  ? 6.678  6.918   30.202 1.000 5.82  ? 19   LYS A CD   1 
ATOM   222  C  CE   . LYS A 1 19  ? 6.616  7.998   31.269 1.000 5.93  ? 19   LYS A CE   1 
ATOM   223  N  NZ   . LYS A 1 19  ? 7.246  7.543   32.529 1.000 5.86  ? 19   LYS A NZ   1 
ATOM   224  H  H    . LYS A 1 19  ? 6.068  5.014   25.656 1.000 7.18  ? 19   LYS A H    1 
ATOM   225  H  HA   . LYS A 1 19  ? 4.338  6.635   26.834 1.000 6.84  ? 19   LYS A HA   1 
ATOM   226  H  HB2  . LYS A 1 19  ? 5.830  5.415   28.134 1.000 7.28  ? 19   LYS A HB2  1 
ATOM   227  H  HB3  . LYS A 1 19  ? 7.034  6.253   27.583 1.000 7.28  ? 19   LYS A HB3  1 
ATOM   228  H  HG2  . LYS A 1 19  ? 6.215  8.161   28.648 1.000 6.87  ? 19   LYS A HG2  1 
ATOM   229  H  HG3  . LYS A 1 19  ? 4.974  7.355   29.164 1.000 6.87  ? 19   LYS A HG3  1 
ATOM   230  H  HD2  . LYS A 1 19  ? 6.312  6.096   30.563 1.000 6.98  ? 19   LYS A HD2  1 
ATOM   231  H  HD3  . LYS A 1 19  ? 7.606  6.754   29.972 1.000 6.98  ? 19   LYS A HD3  1 
ATOM   232  H  HE3  . LYS A 1 19  ? 5.689  8.228   31.440 1.000 7.12  ? 19   LYS A HE3  1 
ATOM   233  H  HZ1  . LYS A 1 19  ? 7.194  8.190   33.138 1.000 8.79  ? 19   LYS A HZ1  1 
ATOM   234  H  HZ2  . LYS A 1 19  ? 7.193  8.196   33.132 1.000 8.79  ? 19   LYS A HZ2  1 
ATOM   235  H  HZ3  . LYS A 1 19  ? 8.101  7.348   32.376 1.000 8.79  ? 19   LYS A HZ3  1 
ATOM   236  N  N    . CYS A 1 20  ? 6.769  8.159   25.394 1.000 5.74  ? 20   CYS A N    1 
ATOM   237  C  CA   . CYS A 1 20  ? 7.188  9.433   24.848 1.000 5.82  ? 20   CYS A CA   1 
ATOM   238  C  C    . CYS A 1 20  ? 6.151  9.995   23.897 1.000 5.61  ? 20   CYS A C    1 
ATOM   239  O  O    . CYS A 1 20  ? 5.812  11.171  23.945 1.000 6.04  ? 20   CYS A O    1 
ATOM   240  C  CB   . CYS A 1 20  ? 8.566  9.261   24.198 1.000 6.17  ? 20   CYS A CB   1 
ATOM   241  S  SG   . CYS A 1 20  ? 9.330  10.770  23.589 1.000 6.84  ? 20   CYS A SG   1 
ATOM   242  H  HA   . CYS A 1 20  ? 7.284  10.062  25.594 1.000 6.98  ? 20   CYS A HA   1 
ATOM   243  H  HB2  . CYS A 1 20  ? 9.161  8.854   24.847 1.000 7.40  ? 20   CYS A HB2  1 
ATOM   244  N  N    . ASN A 1 21  ? 5.607  9.134   23.000 1.000 5.88  ? 21   ASN A N    1 
ATOM   245  C  CA   . ASN A 1 21  ? 4.644  9.622   22.041 1.000 5.94  ? 21   ASN A CA   1 
ATOM   246  C  C    . ASN A 1 21  ? 3.286  9.928   22.697 1.000 5.95  ? 21   ASN A C    1 
ATOM   247  O  O    . ASN A 1 21  ? 2.560  10.822  22.225 1.000 7.10  ? 21   ASN A O    1 
ATOM   248  C  CB   . ASN A 1 21  ? 4.529  8.639   20.881 1.000 6.58  ? 21   ASN A CB   1 
ATOM   249  C  CG   . ASN A 1 21  ? 5.611  8.935   19.843 1.000 6.73  ? 21   ASN A CG   1 
ATOM   250  O  OD1  . ASN A 1 21  ? 5.971  10.103  19.635 1.000 7.43  ? 21   ASN A OD1  1 
ATOM   251  N  ND2  . ASN A 1 21  ? 6.089  7.890   19.192 1.000 7.92  ? 21   ASN A ND2  1 
ATOM   252  H  H    . ASN A 1 21  ? 5.834  8.304   23.003 1.000 7.06  ? 21   ASN A H    1 
ATOM   253  H  HA   . ASN A 1 21  ? 4.991  10.463  21.678 1.000 7.12  ? 21   ASN A HA   1 
ATOM   254  H  HB2  . ASN A 1 21  ? 4.630  7.732   21.210 1.000 7.89  ? 21   ASN A HB2  1 
ATOM   255  H  HB3  . ASN A 1 21  ? 3.652  8.716   20.472 1.000 7.89  ? 21   ASN A HB3  1 
ATOM   256  H  HD22 . ASN A 1 21  ? 5.803  7.102   19.387 1.000 9.51  ? 21   ASN A HD22 1 
ATOM   257  N  N    . ASN A 1 22  ? 2.957  9.290   23.808 1.000 6.52  ? 22   ASN A N    1 
ATOM   258  C  CA   . ASN A 1 22  ? 1.789  9.700   24.590 1.000 6.86  ? 22   ASN A CA   1 
ATOM   259  C  C    . ASN A 1 22  ? 2.016  11.115  25.132 1.000 6.81  ? 22   ASN A C    1 
ATOM   260  O  O    . ASN A 1 22  ? 1.109  11.975  25.082 1.000 8.08  ? 22   ASN A O    1 
ATOM   261  C  CB   A ASN A 1 22  ? 1.583  8.698   25.717 0.380 8.50  ? 22   ASN A CB   1 
ATOM   262  C  CB   B ASN A 1 22  ? 1.490  8.693   25.677 0.620 7.36  ? 22   ASN A CB   1 
ATOM   263  C  CG   A ASN A 1 22  ? 0.844  7.484   25.177 0.380 13.45 ? 22   ASN A CG   1 
ATOM   264  C  CG   B ASN A 1 22  ? 0.204  8.824   26.445 0.620 7.91  ? 22   ASN A CG   1 
ATOM   265  O  OD1  A ASN A 1 22  ? 0.185  7.509   24.156 0.380 23.15 ? 22   ASN A OD1  1 
ATOM   266  O  OD1  B ASN A 1 22  ? -0.616 9.778   26.273 0.620 11.09 ? 22   ASN A OD1  1 
ATOM   267  N  ND2  A ASN A 1 22  ? 1.032  6.407   25.934 0.380 15.37 ? 22   ASN A ND2  1 
ATOM   268  N  ND2  B ASN A 1 22  ? -0.032 7.894   27.308 0.620 8.90  ? 22   ASN A ND2  1 
ATOM   269  H  HB2  B ASN A 1 22  ? 1.503  7.811   25.273 0.620 8.83  ? 22   ASN A HB2  1 
ATOM   270  H  HB3  B ASN A 1 22  ? 2.219  8.724   26.316 0.620 8.83  ? 22   ASN A HB3  1 
ATOM   271  N  N    . LEU A 1 23  ? 3.205  11.382  25.664 1.000 6.62  ? 23   LEU A N    1 
ATOM   272  C  CA   . LEU A 1 23  ? 3.540  12.721  26.151 1.000 6.72  ? 23   LEU A CA   1 
ATOM   273  C  C    . LEU A 1 23  ? 3.524  13.724  25.015 1.000 6.67  ? 23   LEU A C    1 
ATOM   274  O  O    . LEU A 1 23  ? 3.062  14.856  25.191 1.000 7.41  ? 23   LEU A O    1 
ATOM   275  C  CB   . LEU A 1 23  ? 4.901  12.668  26.857 1.000 6.57  ? 23   LEU A CB   1 
ATOM   276  C  CG   . LEU A 1 23  ? 5.347  13.990  27.479 1.000 7.66  ? 23   LEU A CG   1 
ATOM   277  C  CD1  . LEU A 1 23  ? 4.330  14.571  28.456 1.000 9.17  ? 23   LEU A CD1  1 
ATOM   278  C  CD2  . LEU A 1 23  ? 6.721  13.757  28.121 1.000 9.20  ? 23   LEU A CD2  1 
ATOM   279  H  H    . LEU A 1 23  ? 3.791  10.755  25.722 1.000 7.95  ? 23   LEU A H    1 
ATOM   280  H  HA   . LEU A 1 23  ? 2.863  12.988  26.808 1.000 8.07  ? 23   LEU A HA   1 
ATOM   281  H  HB2  . LEU A 1 23  ? 4.863  11.995  27.554 1.000 7.89  ? 23   LEU A HB2  1 
ATOM   282  H  HB3  . LEU A 1 23  ? 5.572  12.386  26.215 1.000 7.89  ? 23   LEU A HB3  1 
ATOM   283  H  HG   . LEU A 1 23  ? 5.464  14.637  26.752 1.000 9.19  ? 23   LEU A HG   1 
ATOM   284  H  HD11 . LEU A 1 23  ? 4.162  13.934  29.155 1.000 13.75 ? 23   LEU A HD11 1 
ATOM   285  H  HD12 . LEU A 1 23  ? 4.682  15.379  28.836 1.000 13.75 ? 23   LEU A HD12 1 
ATOM   286  H  HD21 . LEU A 1 23  ? 7.317  13.397  27.461 1.000 13.80 ? 23   LEU A HD21 1 
ATOM   287  H  HD23 . LEU A 1 23  ? 6.632  13.134  28.846 1.000 13.80 ? 23   LEU A HD23 1 
ATOM   288  N  N    . ARG A 1 24  ? 4.034  13.345  23.840 1.000 6.44  ? 24   ARG A N    1 
ATOM   289  C  CA   . ARG A 1 24  ? 3.927  14.201  22.646 1.000 6.42  ? 24   ARG A CA   1 
ATOM   290  C  C    . ARG A 1 24  ? 2.499  14.629  22.429 1.000 6.87  ? 24   ARG A C    1 
ATOM   291  O  O    . ARG A 1 24  ? 2.192  15.811  22.244 1.000 7.65  ? 24   ARG A O    1 
ATOM   292  C  CB   . ARG A 1 24  ? 4.446  13.448  21.411 1.000 6.40  ? 24   ARG A CB   1 
ATOM   293  C  CG   . ARG A 1 24  ? 4.101  14.117  20.115 1.000 7.46  ? 24   ARG A CG   1 
ATOM   294  C  CD   . ARG A 1 24  ? 4.228  13.195  18.891 1.000 7.92  ? 24   ARG A CD   1 
ATOM   295  N  NE   . ARG A 1 24  ? 3.253  12.113  18.989 1.000 7.87  ? 24   ARG A NE   1 
ATOM   296  C  CZ   . ARG A 1 24  ? 3.206  11.081  18.173 1.000 7.03  ? 24   ARG A CZ   1 
ATOM   297  N  NH1  . ARG A 1 24  ? 4.026  10.999  17.132 1.000 7.75  ? 24   ARG A NH1  1 
ATOM   298  N  NH2  . ARG A 1 24  ? 2.340  10.085  18.399 1.000 8.53  ? 24   ARG A NH2  1 
ATOM   299  H  H    . ARG A 1 24  ? 4.432  12.585  23.779 1.000 7.73  ? 24   ARG A H    1 
ATOM   300  H  HA   . ARG A 1 24  ? 4.478  15.001  22.781 1.000 7.70  ? 24   ARG A HA   1 
ATOM   301  H  HB2  . ARG A 1 24  ? 5.411  13.366  21.476 1.000 7.68  ? 24   ARG A HB2  1 
ATOM   302  H  HB3  . ARG A 1 24  ? 4.074  12.552  21.411 1.000 7.68  ? 24   ARG A HB3  1 
ATOM   303  H  HG2  . ARG A 1 24  ? 3.191  14.447  20.165 1.000 8.96  ? 24   ARG A HG2  1 
ATOM   304  H  HG3  . ARG A 1 24  ? 4.686  14.881  19.992 1.000 8.96  ? 24   ARG A HG3  1 
ATOM   305  H  HD2  . ARG A 1 24  ? 4.071  13.704  18.080 1.000 9.51  ? 24   ARG A HD2  1 
ATOM   306  H  HD3  . ARG A 1 24  ? 5.124  12.826  18.849 1.000 9.51  ? 24   ARG A HD3  1 
ATOM   307  H  HE   . ARG A 1 24  ? 2.672  12.152  19.622 1.000 9.45  ? 24   ARG A HE   1 
ATOM   308  H  HH21 . ARG A 1 24  ? 1.816  10.120  19.080 1.000 10.24 ? 24   ARG A HH21 1 
ATOM   309  N  N    . ASP A 1 25  ? 1.599  13.653  22.430 1.000 7.30  ? 25   ASP A N    1 
ATOM   310  C  CA   . ASP A 1 25  ? 0.187  13.973  22.129 1.000 8.00  ? 25   ASP A CA   1 
ATOM   311  C  C    . ASP A 1 25  ? -0.374 14.951  23.164 1.000 8.01  ? 25   ASP A C    1 
ATOM   312  O  O    . ASP A 1 25  ? -1.166 15.817  22.802 1.000 12.19 ? 25   ASP A O    1 
ATOM   313  C  CB   . ASP A 1 25  ? -0.617 12.713  22.045 1.000 8.70  ? 25   ASP A CB   1 
ATOM   314  C  CG   . ASP A 1 25  ? -0.245 11.750  20.946 1.000 11.10 ? 25   ASP A CG   1 
ATOM   315  O  OD1  . ASP A 1 25  ? -0.744 10.606  21.041 1.000 14.68 ? 25   ASP A OD1  1 
ATOM   316  O  OD2  . ASP A 1 25  ? 0.448  12.119  20.016 1.000 12.90 ? 25   ASP A OD2  1 
ATOM   317  H  H    . ASP A 1 25  ? 1.835  12.845  22.605 1.000 8.77  ? 25   ASP A H    1 
ATOM   318  H  HA   . ASP A 1 25  ? 0.156  14.410  21.252 1.000 9.59  ? 25   ASP A HA   1 
ATOM   319  H  HB2  . ASP A 1 25  ? -0.562 12.259  22.870 1.000 10.44 ? 25   ASP A HB2  1 
ATOM   320  N  N    . LEU A 1 26  ? 0.044  14.815  24.407 1.000 7.56  ? 26   LEU A N    1 
ATOM   321  C  CA   . LEU A 1 26  ? -0.466 15.619  25.506 1.000 8.36  ? 26   LEU A CA   1 
ATOM   322  C  C    . LEU A 1 26  ? 0.188  17.000  25.596 1.000 8.21  ? 26   LEU A C    1 
ATOM   323  O  O    . LEU A 1 26  ? -0.245 17.782  26.435 1.000 9.88  ? 26   LEU A O    1 
ATOM   324  C  CB   . LEU A 1 26  ? -0.290 14.899  26.824 1.000 9.97  ? 26   LEU A CB   1 
ATOM   325  C  CG   . LEU A 1 26  ? -1.157 13.662  26.998 1.000 11.04 ? 26   LEU A CG   1 
ATOM   326  C  CD1  . LEU A 1 26  ? -0.772 12.776  28.121 1.000 16.22 ? 26   LEU A CD1  1 
ATOM   327  C  CD2  . LEU A 1 26  ? -2.617 14.197  27.203 1.000 20.04 ? 26   LEU A CD2  1 
ATOM   328  H  HA   . LEU A 1 26  ? -1.427 15.751  25.361 1.000 10.03 ? 26   LEU A HA   1 
ATOM   329  H  HG   . LEU A 1 26  ? -1.129 13.143  26.167 1.000 13.25 ? 26   LEU A HG   1 
ATOM   330  H  HD11 . LEU A 1 26  ? -1.347 12.949  28.870 1.000 24.33 ? 26   LEU A HD11 1 
ATOM   331  N  N    . THR A 1 27  ? 1.233  17.279  24.813 1.000 8.37  ? 27   THR A N    1 
ATOM   332  C  CA   . THR A 1 27  ? 1.970  18.511  24.850 1.000 8.18  ? 27   THR A CA   1 
ATOM   333  C  C    . THR A 1 27  ? 2.036  19.211  23.498 1.000 9.15  ? 27   THR A C    1 
ATOM   334  O  O    . THR A 1 27  ? 2.755  20.211  23.333 1.000 9.68  ? 27   THR A O    1 
ATOM   335  C  CB   . THR A 1 27  ? 3.407  18.332  25.411 1.000 8.40  ? 27   THR A CB   1 
ATOM   336  O  OG1  . THR A 1 27  ? 4.100  17.378  24.567 1.000 8.42  ? 27   THR A OG1  1 
ATOM   337  C  CG2  . THR A 1 27  ? 3.398  17.898  26.841 1.000 9.36  ? 27   THR A CG2  1 
ATOM   338  H  HB   . THR A 1 27  ? 3.872  19.192  25.351 1.000 10.08 ? 27   THR A HB   1 
ATOM   339  H  HG21 . THR A 1 27  ? 3.090  18.610  27.389 1.000 14.03 ? 27   THR A HG21 1 
ATOM   340  H  HG22 . THR A 1 27  ? 2.844  17.159  26.972 1.000 14.03 ? 27   THR A HG22 1 
ATOM   341  N  N    . GLN A 1 28  ? 1.216  18.733  22.548 1.000 9.90  ? 28   GLN A N    1 
ATOM   342  C  CA   A GLN A 1 28  ? 1.211  19.253  21.192 0.401 12.91 ? 28   GLN A CA   1 
ATOM   343  C  CA   B GLN A 1 28  ? 1.397  19.255  21.176 0.599 11.53 ? 28   GLN A CA   1 
ATOM   344  C  C    . GLN A 1 28  ? 1.035  20.751  21.065 1.000 12.99 ? 28   GLN A C    1 
ATOM   345  O  O    . GLN A 1 28  ? 1.564  21.361  20.111 1.000 16.98 ? 28   GLN A O    1 
ATOM   346  C  CB   A GLN A 1 28  ? 0.027  18.618  20.410 0.401 16.03 ? 28   GLN A CB   1 
ATOM   347  C  CB   B GLN A 1 28  ? 0.598  18.306  20.284 0.599 12.47 ? 28   GLN A CB   1 
ATOM   348  C  CG   A GLN A 1 28  ? 0.559  17.376  19.721 0.401 15.03 ? 28   GLN A CG   1 
ATOM   349  C  CG   B GLN A 1 28  ? 0.765  18.538  18.784 0.599 12.70 ? 28   GLN A CG   1 
ATOM   350  C  CD   A GLN A 1 28  ? 1.763  17.700  18.850 0.401 18.55 ? 28   GLN A CD   1 
ATOM   351  C  CD   B GLN A 1 28  ? 2.235  18.370  18.425 0.599 14.65 ? 28   GLN A CD   1 
ATOM   352  O  OE1  A GLN A 1 28  ? 2.583  16.853  18.507 0.401 25.46 ? 28   GLN A OE1  1 
ATOM   353  O  OE1  B GLN A 1 28  ? 2.721  17.326  18.765 0.599 23.56 ? 28   GLN A OE1  1 
ATOM   354  N  NE2  A GLN A 1 28  ? 1.880  18.967  18.457 0.401 25.95 ? 28   GLN A NE2  1 
ATOM   355  N  NE2  B GLN A 1 28  ? 2.832  19.391  17.860 0.599 20.84 ? 28   GLN A NE2  1 
ATOM   356  N  N    . GLN A 1 29  ? 0.225  21.290  21.991 1.000 12.49 ? 29   GLN A N    1 
ATOM   357  C  CA   . GLN A 1 29  ? -0.110 22.699  21.828 1.000 15.65 ? 29   GLN A CA   1 
ATOM   358  C  C    . GLN A 1 29  ? 0.776  23.570  22.726 1.000 15.83 ? 29   GLN A C    1 
ATOM   359  O  O    . GLN A 1 29  ? 0.565  24.776  22.793 1.000 20.39 ? 29   GLN A O    1 
ATOM   360  C  CB   A GLN A 1 29  ? -1.565 22.936  22.148 0.581 22.57 ? 29   GLN A CB   1 
ATOM   361  C  CB   B GLN A 1 29  ? -1.556 22.976  22.189 0.419 21.73 ? 29   GLN A CB   1 
ATOM   362  C  CG   A GLN A 1 29  ? -2.588 21.970  21.575 0.581 29.21 ? 29   GLN A CG   1 
ATOM   363  C  CG   B GLN A 1 29  ? -2.488 22.523  21.052 0.419 30.68 ? 29   GLN A CG   1 
ATOM   364  C  CD   A GLN A 1 29  ? -2.376 21.385  20.192 0.581 38.17 ? 29   GLN A CD   1 
ATOM   365  C  CD   B GLN A 1 29  ? -2.579 20.999  21.006 0.419 34.77 ? 29   GLN A CD   1 
ATOM   366  O  OE1  A GLN A 1 29  ? -2.031 22.097  19.232 0.581 45.73 ? 29   GLN A OE1  1 
ATOM   367  O  OE1  B GLN A 1 29  ? -2.346 20.327  19.989 0.419 41.30 ? 29   GLN A OE1  1 
ATOM   368  N  NE2  A GLN A 1 29  ? -2.601 20.067  20.004 0.581 45.35 ? 29   GLN A NE2  1 
ATOM   369  N  NE2  B GLN A 1 29  ? -2.899 20.460  22.176 0.419 32.97 ? 29   GLN A NE2  1 
ATOM   370  N  N    . GLU A 1 30  ? 1.756  23.012  23.425 1.000 12.00 ? 30   GLU A N    1 
ATOM   371  C  CA   . GLU A 1 30  ? 2.645  23.796  24.263 1.000 11.37 ? 30   GLU A CA   1 
ATOM   372  C  C    . GLU A 1 30  ? 3.624  24.589  23.405 1.000 12.31 ? 30   GLU A C    1 
ATOM   373  O  O    . GLU A 1 30  ? 3.854  24.309  22.234 1.000 13.25 ? 30   GLU A O    1 
ATOM   374  C  CB   . GLU A 1 30  ? 3.429  22.910  25.251 1.000 11.09 ? 30   GLU A CB   1 
ATOM   375  C  CG   . GLU A 1 30  ? 2.565  22.126  26.207 1.000 11.06 ? 30   GLU A CG   1 
ATOM   376  C  CD   . GLU A 1 30  ? 1.727  22.949  27.153 1.000 12.98 ? 30   GLU A CD   1 
ATOM   377  O  OE1  . GLU A 1 30  ? 0.836  22.367  27.793 1.000 13.39 ? 30   GLU A OE1  1 
ATOM   378  O  OE2  . GLU A 1 30  ? 1.992  24.143  27.300 1.000 19.35 ? 30   GLU A OE2  1 
ATOM   379  H  HA   . GLU A 1 30  ? 2.103  24.429  24.779 1.000 13.64 ? 30   GLU A HA   1 
ATOM   380  H  HB2  . GLU A 1 30  ? 3.974  22.288  24.744 1.000 13.31 ? 30   GLU A HB2  1 
ATOM   381  H  HB3  . GLU A 1 30  ? 4.028  23.473  25.765 1.000 13.31 ? 30   GLU A HB3  1 
ATOM   382  H  HG2  . GLU A 1 30  ? 1.965  21.567  25.688 1.000 13.28 ? 30   GLU A HG2  1 
ATOM   383  N  N    . ARG A 1 31  ? 4.215  25.629  23.999 1.000 12.28 ? 31   ARG A N    1 
ATOM   384  C  CA   . ARG A 1 31  ? 5.184  26.400  23.236 1.000 12.22 ? 31   ARG A CA   1 
ATOM   385  C  C    . ARG A 1 31  ? 6.344  25.547  22.734 1.000 9.85  ? 31   ARG A C    1 
ATOM   386  O  O    . ARG A 1 31  ? 6.717  25.622  21.568 1.000 10.77 ? 31   ARG A O    1 
ATOM   387  C  CB   . ARG A 1 31  ? 5.721  27.549  24.154 1.000 12.59 ? 31   ARG A CB   1 
ATOM   388  C  CG   . ARG A 1 31  ? 6.622  28.502  23.347 1.000 12.82 ? 31   ARG A CG   1 
ATOM   389  C  CD   . ARG A 1 31  ? 7.145  29.629  24.224 1.000 14.40 ? 31   ARG A CD   1 
ATOM   390  N  NE   . ARG A 1 31  ? 8.053  29.172  25.294 1.000 15.38 ? 31   ARG A NE   1 
ATOM   391  C  CZ   . ARG A 1 31  ? 9.377  29.012  25.055 1.000 13.59 ? 31   ARG A CZ   1 
ATOM   392  N  NH1  . ARG A 1 31  ? 9.891  29.271  23.853 1.000 15.25 ? 31   ARG A NH1  1 
ATOM   393  N  NH2  . ARG A 1 31  ? 10.149 28.618  26.017 1.000 15.51 ? 31   ARG A NH2  1 
ATOM   394  H  HA   . ARG A 1 31  ? 4.731  26.800  22.465 1.000 14.66 ? 31   ARG A HA   1 
ATOM   395  H  HG2  . ARG A 1 31  ? 7.369  28.006  22.979 1.000 15.38 ? 31   ARG A HG2  1 
ATOM   396  H  HG3  . ARG A 1 31  ? 6.116  28.876  22.609 1.000 15.38 ? 31   ARG A HG3  1 
ATOM   397  H  HD2  . ARG A 1 31  ? 7.576  30.298  23.668 1.000 17.28 ? 31   ARG A HD2  1 
ATOM   398  N  N    . ILE A 1 32  ? 6.891  24.746  23.651 1.000 9.44  ? 32   ILE A N    1 
ATOM   399  C  CA   . ILE A 1 32  ? 7.854  23.717  23.283 1.000 7.87  ? 32   ILE A CA   1 
ATOM   400  C  C    . ILE A 1 32  ? 7.146  22.389  23.210 1.000 7.18  ? 32   ILE A C    1 
ATOM   401  O  O    . ILE A 1 32  ? 6.584  21.918  24.202 1.000 8.35  ? 32   ILE A O    1 
ATOM   402  C  CB   . ILE A 1 32  ? 9.040  23.666  24.259 1.000 8.36  ? 32   ILE A CB   1 
ATOM   403  C  CG1  . ILE A 1 32  ? 9.741  25.014  24.490 1.000 9.62  ? 32   ILE A CG1  1 
ATOM   404  C  CG2  . ILE A 1 32  ? 10.026 22.594  23.788 1.000 7.82  ? 32   ILE A CG2  1 
ATOM   405  C  CD1  . ILE A 1 32  ? 10.243 25.717  23.197 1.000 10.45 ? 32   ILE A CD1  1 
ATOM   406  H  HA   . ILE A 1 32  ? 8.202  23.928  22.392 1.000 9.44  ? 32   ILE A HA   1 
ATOM   407  H  HB   . ILE A 1 32  ? 8.687  23.373  25.125 1.000 10.04 ? 32   ILE A HB   1 
ATOM   408  H  HG12 . ILE A 1 32  ? 9.125  25.608  24.946 1.000 11.55 ? 32   ILE A HG12 1 
ATOM   409  H  HG13 . ILE A 1 32  ? 10.499 24.871  25.078 1.000 11.55 ? 32   ILE A HG13 1 
ATOM   410  H  HG22 . ILE A 1 32  ? 10.397 22.869  22.947 1.000 11.73 ? 32   ILE A HG22 1 
ATOM   411  N  N    . SER A 1 33  ? 7.133  21.767  22.024 1.000 7.38  ? 33   SER A N    1 
ATOM   412  C  CA   . SER A 1 33  ? 6.542  20.489  21.785 1.000 7.49  ? 33   SER A CA   1 
ATOM   413  C  C    . SER A 1 33  ? 7.638  19.403  21.649 1.000 6.70  ? 33   SER A C    1 
ATOM   414  O  O    . SER A 1 33  ? 8.839  19.719  21.790 1.000 7.15  ? 33   SER A O    1 
ATOM   415  C  CB   . SER A 1 33  ? 5.610  20.508  20.604 1.000 8.74  ? 33   SER A CB   1 
ATOM   416  O  OG   . SER A 1 33  ? 6.261  20.971  19.458 1.000 10.53 ? 33   SER A OG   1 
ATOM   417  H  H    . SER A 1 33  ? 7.507  22.165  21.359 1.000 8.86  ? 33   SER A H    1 
ATOM   418  H  HA   . SER A 1 33  ? 6.006  20.265  22.574 1.000 8.99  ? 33   SER A HA   1 
ATOM   419  H  HB2  . SER A 1 33  ? 5.274  19.612  20.445 1.000 10.49 ? 33   SER A HB2  1 
ATOM   420  H  HB3  . SER A 1 33  ? 4.853  21.082  20.800 1.000 10.49 ? 33   SER A HB3  1 
ATOM   421  N  N    . LEU A 1 34  ? 7.229  18.183  21.424 1.000 7.03  ? 34   LEU A N    1 
ATOM   422  C  CA   . LEU A 1 34  ? 8.071  17.017  21.597 1.000 6.61  ? 34   LEU A CA   1 
ATOM   423  C  C    . LEU A 1 34  ? 7.941  16.091  20.398 1.000 6.69  ? 34   LEU A C    1 
ATOM   424  O  O    . LEU A 1 34  ? 6.839  15.816  19.949 1.000 7.73  ? 34   LEU A O    1 
ATOM   425  C  CB   . LEU A 1 34  ? 7.625  16.244  22.839 1.000 7.04  ? 34   LEU A CB   1 
ATOM   426  C  CG   . LEU A 1 34  ? 8.334  14.954  23.166 1.000 6.54  ? 34   LEU A CG   1 
ATOM   427  C  CD1  . LEU A 1 34  ? 9.782  15.177  23.517 1.000 8.27  ? 34   LEU A CD1  1 
ATOM   428  C  CD2  . LEU A 1 34  ? 7.579  14.229  24.294 1.000 7.70  ? 34   LEU A CD2  1 
ATOM   429  H  HA   . LEU A 1 34  ? 9.005  17.297  21.699 1.000 7.93  ? 34   LEU A HA   1 
ATOM   430  H  HB3  . LEU A 1 34  ? 6.680  16.046  22.739 1.000 8.44  ? 34   LEU A HB3  1 
ATOM   431  H  HG   . LEU A 1 34  ? 8.302  14.385  22.369 1.000 7.85  ? 34   LEU A HG   1 
ATOM   432  H  HD11 . LEU A 1 34  ? 10.196 14.335  23.718 1.000 12.40 ? 34   LEU A HD11 1 
ATOM   433  H  HD12 . LEU A 1 34  ? 10.232 15.586  22.774 1.000 12.40 ? 34   LEU A HD12 1 
ATOM   434  H  HD13 . LEU A 1 34  ? 9.840  15.753  24.283 1.000 12.40 ? 34   LEU A HD13 1 
ATOM   435  H  HD21 . LEU A 1 34  ? 8.028  13.408  24.507 1.000 11.55 ? 34   LEU A HD21 1 
ATOM   436  H  HD22 . LEU A 1 34  ? 7.559  14.794  25.070 1.000 11.55 ? 34   LEU A HD22 1 
ATOM   437  N  N    . THR A 1 35  ? 9.075  15.524  19.950 1.000 6.41  ? 35   THR A N    1 
ATOM   438  C  CA   . THR A 1 35  ? 9.059  14.334  19.131 1.000 6.45  ? 35   THR A CA   1 
ATOM   439  C  C    . THR A 1 35  ? 10.019 13.316  19.779 1.000 5.88  ? 35   THR A C    1 
ATOM   440  O  O    . THR A 1 35  ? 10.826 13.656  20.637 1.000 6.58  ? 35   THR A O    1 
ATOM   441  C  CB   . THR A 1 35  ? 9.379  14.552  17.645 1.000 6.92  ? 35   THR A CB   1 
ATOM   442  O  OG1  . THR A 1 35  ? 10.764 14.946  17.567 1.000 7.90  ? 35   THR A OG1  1 
ATOM   443  C  CG2  . THR A 1 35  ? 8.468  15.574  16.998 1.000 8.68  ? 35   THR A CG2  1 
ATOM   444  H  HA   . THR A 1 35  ? 8.156  13.956  19.182 1.000 7.74  ? 35   THR A HA   1 
ATOM   445  H  HG1  . THR A 1 35  ? 10.821 15.668  17.182 1.000 11.86 ? 35   THR A HG1  1 
ATOM   446  N  N    . CYS A 1 36  ? 9.874  12.065  19.318 1.000 6.26  ? 36   CYS A N    1 
ATOM   447  C  CA   . CYS A 1 36  ? 10.489 10.928  19.981 1.000 6.35  ? 36   CYS A CA   1 
ATOM   448  C  C    . CYS A 1 36  ? 11.184 10.069  18.947 1.000 6.20  ? 36   CYS A C    1 
ATOM   449  O  O    . CYS A 1 36  ? 10.568 9.620   17.994 1.000 8.69  ? 36   CYS A O    1 
ATOM   450  C  CB   . CYS A 1 36  ? 9.388  10.090  20.645 1.000 6.60  ? 36   CYS A CB   1 
ATOM   451  S  SG   . CYS A 1 36  ? 8.363  11.047  21.809 1.000 7.17  ? 36   CYS A SG   1 
ATOM   452  H  H    . CYS A 1 36  ? 9.404  11.933  18.611 1.000 7.52  ? 36   CYS A H    1 
ATOM   453  H  HA   . CYS A 1 36  ? 11.132 11.235  20.653 1.000 7.62  ? 36   CYS A HA   1 
ATOM   454  N  N    A VAL A 1 37  ? 12.440 9.727   19.214 0.705 6.26  ? 37   VAL A N    1 
ATOM   455  N  N    B VAL A 1 37  ? 12.476 9.814   19.093 0.295 6.48  ? 37   VAL A N    1 
ATOM   456  C  CA   A VAL A 1 37  ? 13.190 8.859   18.308 0.705 6.88  ? 37   VAL A CA   1 
ATOM   457  C  CA   B VAL A 1 37  ? 13.116 8.783   18.276 0.295 9.00  ? 37   VAL A CA   1 
ATOM   458  C  C    A VAL A 1 37  ? 13.799 7.718   19.132 0.705 6.26  ? 37   VAL A C    1 
ATOM   459  C  C    B VAL A 1 37  ? 13.385 7.640   19.236 0.295 8.21  ? 37   VAL A C    1 
ATOM   460  O  O    A VAL A 1 37  ? 14.454 7.944   20.126 0.705 6.27  ? 37   VAL A O    1 
ATOM   461  O  O    B VAL A 1 37  ? 13.438 7.683   20.444 0.295 8.72  ? 37   VAL A O    1 
ATOM   462  C  CB   A VAL A 1 37  ? 14.243 9.618   17.493 0.705 8.54  ? 37   VAL A CB   1 
ATOM   463  C  CB   B VAL A 1 37  ? 14.365 9.252   17.514 0.295 9.76  ? 37   VAL A CB   1 
ATOM   464  C  CG1  A VAL A 1 37  ? 15.228 10.329  18.352 0.705 9.74  ? 37   VAL A CG1  1 
ATOM   465  C  CG1  B VAL A 1 37  ? 14.010 10.574  16.833 0.295 16.00 ? 37   VAL A CG1  1 
ATOM   466  C  CG2  A VAL A 1 37  ? 14.995 8.594   16.694 0.705 10.79 ? 37   VAL A CG2  1 
ATOM   467  C  CG2  B VAL A 1 37  ? 15.575 9.414   18.390 0.295 16.05 ? 37   VAL A CG2  1 
ATOM   468  H  HA   A VAL A 1 37  ? 12.552 8.464   17.678 0.705 8.25  ? 37   VAL A HA   1 
ATOM   469  H  HA   B VAL A 1 37  ? 12.461 8.473   17.616 0.295 10.80 ? 37   VAL A HA   1 
ATOM   470  H  HB   A VAL A 1 37  ? 13.805 10.255  16.892 0.705 10.24 ? 37   VAL A HB   1 
ATOM   471  H  HG21 A VAL A 1 37  ? 14.383 8.118   16.128 0.705 16.18 ? 37   VAL A HG21 1 
ATOM   472  H  HG22 A VAL A 1 37  ? 15.656 9.032   16.153 0.705 16.18 ? 37   VAL A HG22 1 
ATOM   473  H  HG23 A VAL A 1 37  ? 15.427 7.977   17.289 0.705 16.18 ? 37   VAL A HG23 1 
ATOM   474  N  N    . GLN A 1 38  ? 13.520 6.481   18.651 1.000 7.21  ? 38   GLN A N    1 
ATOM   475  C  CA   . GLN A 1 38  ? 13.964 5.280   19.327 1.000 7.14  ? 38   GLN A CA   1 
ATOM   476  C  C    . GLN A 1 38  ? 15.257 4.790   18.701 1.000 7.65  ? 38   GLN A C    1 
ATOM   477  O  O    . GLN A 1 38  ? 15.361 4.734   17.469 1.000 10.03 ? 38   GLN A O    1 
ATOM   478  C  CB   . GLN A 1 38  ? 12.863 4.212   19.224 1.000 8.14  ? 38   GLN A CB   1 
ATOM   479  C  CG   . GLN A 1 38  ? 13.113 2.980   20.077 1.000 9.01  ? 38   GLN A CG   1 
ATOM   480  C  CD   . GLN A 1 38  ? 11.995 1.922   19.903 1.000 9.31  ? 38   GLN A CD   1 
ATOM   481  O  OE1  . GLN A 1 38  ? 10.887 2.272   19.563 1.000 12.42 ? 38   GLN A OE1  1 
ATOM   482  N  NE2  . GLN A 1 38  ? 12.369 0.685   20.188 1.000 12.45 ? 38   GLN A NE2  1 
ATOM   483  H  HE22 . GLN A 1 38  ? 13.179 0.538   20.437 1.000 14.94 ? 38   GLN A HE22 1 
ATOM   484  N  N    . LYS A 1 39  ? 16.191 4.403   19.532 1.000 7.80  ? 39   LYS A N    1 
ATOM   485  C  CA   . LYS A 1 39  ? 17.414 3.756   19.093 1.000 8.52  ? 39   LYS A CA   1 
ATOM   486  C  C    . LYS A 1 39  ? 17.595 2.422   19.822 1.000 8.40  ? 39   LYS A C    1 
ATOM   487  O  O    . LYS A 1 39  ? 16.992 2.152   20.820 1.000 8.83  ? 39   LYS A O    1 
ATOM   488  C  CB   . LYS A 1 39  ? 18.596 4.675   19.371 1.000 9.77  ? 39   LYS A CB   1 
ATOM   489  C  CG   . LYS A 1 39  ? 18.638 6.003   18.695 1.000 9.82  ? 39   LYS A CG   1 
ATOM   490  C  CD   . LYS A 1 39  ? 18.699 5.834   17.198 1.000 12.30 ? 39   LYS A CD   1 
ATOM   491  C  CE   . LYS A 1 39  ? 18.848 7.167   16.508 1.000 14.65 ? 39   LYS A CE   1 
ATOM   492  N  NZ   . LYS A 1 39  ? 18.717 7.006   15.014 1.000 21.37 ? 39   LYS A NZ   1 
ATOM   493  H  H    . LYS A 1 39  ? 16.075 4.538   20.373 1.000 9.36  ? 39   LYS A H    1 
ATOM   494  H  HA   . LYS A 1 39  ? 17.359 3.588   18.129 1.000 10.22 ? 39   LYS A HA   1 
ATOM   495  H  HB3  . LYS A 1 39  ? 19.404 4.198   19.125 1.000 11.72 ? 39   LYS A HB3  1 
ATOM   496  H  HG2  . LYS A 1 39  ? 17.842 6.506   18.928 1.000 11.78 ? 39   LYS A HG2  1 
ATOM   497  N  N    . ALA A 1 40  ? 18.534 1.641   19.271 1.000 9.81  ? 40   ALA A N    1 
ATOM   498  C  CA   . ALA A 1 40  ? 18.754 0.310   19.817 1.000 11.04 ? 40   ALA A CA   1 
ATOM   499  C  C    . ALA A 1 40  ? 19.298 0.362   21.237 1.000 8.59  ? 40   ALA A C    1 
ATOM   500  O  O    . ALA A 1 40  ? 18.917 -0.469  22.076 1.000 10.54 ? 40   ALA A O    1 
ATOM   501  C  CB   . ALA A 1 40  ? 19.751 -0.445  18.941 1.000 12.14 ? 40   ALA A CB   1 
ATOM   502  H  H    . ALA A 1 40  ? 19.000 1.923   18.606 1.000 11.78 ? 40   ALA A H    1 
ATOM   503  H  HB1  . ALA A 1 40  ? 19.900 -1.319  19.311 1.000 18.21 ? 40   ALA A HB1  1 
ATOM   504  N  N    . THR A 1 41  ? 20.189 1.292   21.517 1.000 8.73  ? 41   THR A N    1 
ATOM   505  C  CA   . THR A 1 41  ? 20.806 1.442   22.825 1.000 8.31  ? 41   THR A CA   1 
ATOM   506  C  C    . THR A 1 41  ? 21.044 2.911   23.155 1.000 7.47  ? 41   THR A C    1 
ATOM   507  O  O    . THR A 1 41  ? 21.026 3.787   22.294 1.000 7.88  ? 41   THR A O    1 
ATOM   508  C  CB   . THR A 1 41  ? 22.170 0.728   22.989 1.000 11.28 ? 41   THR A CB   1 
ATOM   509  O  OG1  . THR A 1 41  ? 23.160 1.527   22.341 1.000 13.78 ? 41   THR A OG1  1 
ATOM   510  C  CG2  . THR A 1 41  ? 22.159 -0.694  22.446 1.000 12.72 ? 41   THR A CG2  1 
ATOM   511  H  H    . THR A 1 41  ? 20.417 1.839   20.894 1.000 10.47 ? 41   THR A H    1 
ATOM   512  H  HA   . THR A 1 41  ? 20.191 1.077   23.494 1.000 9.97  ? 41   THR A HA   1 
ATOM   513  N  N    . TYR A 1 42  ? 21.276 3.140   24.441 1.000 7.61  ? 42   TYR A N    1 
ATOM   514  C  CA   . TYR A 1 42  ? 21.570 4.485   24.918 1.000 7.65  ? 42   TYR A CA   1 
ATOM   515  C  C    . TYR A 1 42  ? 22.772 5.075   24.173 1.000 7.02  ? 42   TYR A C    1 
ATOM   516  O  O    . TYR A 1 42  ? 22.884 6.279   24.057 1.000 6.92  ? 42   TYR A O    1 
ATOM   517  C  CB   . TYR A 1 42  ? 21.818 4.490   26.477 1.000 8.99  ? 42   TYR A CB   1 
ATOM   518  C  CG   . TYR A 1 42  ? 23.172 3.925   26.744 1.000 9.10  ? 42   TYR A CG   1 
ATOM   519  C  CD1  . TYR A 1 42  ? 23.445 2.609   26.714 1.000 11.55 ? 42   TYR A CD1  1 
ATOM   520  C  CD2  . TYR A 1 42  ? 24.303 4.761   26.861 1.000 9.17  ? 42   TYR A CD2  1 
ATOM   521  C  CE1  . TYR A 1 42  ? 24.703 2.059   26.871 1.000 11.95 ? 42   TYR A CE1  1 
ATOM   522  C  CE2  . TYR A 1 42  ? 25.527 4.266   26.940 1.000 9.53  ? 42   TYR A CE2  1 
ATOM   523  C  CZ   . TYR A 1 42  ? 25.731 2.903   26.970 1.000 10.42 ? 42   TYR A CZ   1 
ATOM   524  O  OH   . TYR A 1 42  ? 26.986 2.336   27.060 1.000 13.11 ? 42   TYR A OH   1 
ATOM   525  H  H    . TYR A 1 42  ? 21.253 2.486   25.000 1.000 9.13  ? 42   TYR A H    1 
ATOM   526  H  HB2  . TYR A 1 42  ? 21.765 5.397   26.818 1.000 10.78 ? 42   TYR A HB2  1 
ATOM   527  H  HB3  . TYR A 1 42  ? 21.142 3.956   26.922 1.000 10.78 ? 42   TYR A HB3  1 
ATOM   528  H  HD1  . TYR A 1 42  ? 22.735 2.025   26.576 1.000 13.86 ? 42   TYR A HD1  1 
ATOM   529  H  HD2  . TYR A 1 42  ? 24.185 5.683   26.883 1.000 11.00 ? 42   TYR A HD2  1 
ATOM   530  H  HE2  . TYR A 1 42  ? 26.256 4.842   26.975 1.000 11.43 ? 42   TYR A HE2  1 
ATOM   531  N  N    . LEU A 1 43  ? 23.745 4.215   23.781 1.000 7.59  ? 43   LEU A N    1 
ATOM   532  C  CA   . LEU A 1 43  ? 24.937 4.760   23.113 1.000 7.69  ? 43   LEU A CA   1 
ATOM   533  C  C    . LEU A 1 43  ? 24.583 5.334   21.761 1.000 7.11  ? 43   LEU A C    1 
ATOM   534  O  O    . LEU A 1 43  ? 25.106 6.351   21.322 1.000 7.73  ? 43   LEU A O    1 
ATOM   535  C  CB   . LEU A 1 43  ? 26.060 3.717   23.057 1.000 9.24  ? 43   LEU A CB   1 
ATOM   536  C  CG   . LEU A 1 43  ? 27.330 4.221   22.381 1.000 10.99 ? 43   LEU A CG   1 
ATOM   537  C  CD1  . LEU A 1 43  ? 27.924 5.390   23.140 1.000 13.29 ? 43   LEU A CD1  1 
ATOM   538  C  CD2  . LEU A 1 43  ? 28.345 3.060   22.281 1.000 13.64 ? 43   LEU A CD2  1 
ATOM   539  H  HB2  . LEU A 1 43  ? 26.269 3.436   23.962 1.000 11.09 ? 43   LEU A HB2  1 
ATOM   540  H  HD12 . LEU A 1 43  ? 27.280 6.100   23.192 1.000 19.94 ? 43   LEU A HD12 1 
ATOM   541  H  HD13 . LEU A 1 43  ? 28.136 5.084   24.025 1.000 19.94 ? 43   LEU A HD13 1 
ATOM   542  H  HD23 . LEU A 1 43  ? 28.557 2.750   23.165 1.000 20.46 ? 43   LEU A HD23 1 
ATOM   543  N  N    . ASP A 1 44  ? 23.641 4.660   21.053 1.000 7.73  ? 44   ASP A N    1 
ATOM   544  C  CA   . ASP A 1 44  ? 23.140 5.240   19.812 1.000 7.97  ? 44   ASP A CA   1 
ATOM   545  C  C    . ASP A 1 44  ? 22.470 6.562   20.062 1.000 6.77  ? 44   ASP A C    1 
ATOM   546  O  O    . ASP A 1 44  ? 22.554 7.479   19.243 1.000 7.52  ? 44   ASP A O    1 
ATOM   547  C  CB   . ASP A 1 44  ? 22.188 4.242   19.156 1.000 8.56  ? 44   ASP A CB   1 
ATOM   548  C  CG   . ASP A 1 44  ? 22.863 2.919   18.826 1.000 11.05 ? 44   ASP A CG   1 
ATOM   549  O  OD1  . ASP A 1 44  ? 22.320 1.890   19.289 1.000 17.52 ? 44   ASP A OD1  1 
ATOM   550  O  OD2  . ASP A 1 44  ? 23.862 2.946   18.134 1.000 12.92 ? 44   ASP A OD2  1 
ATOM   551  H  H    . ASP A 1 44  ? 23.344 3.903   21.333 1.000 9.27  ? 44   ASP A H    1 
ATOM   552  H  HA   . ASP A 1 44  ? 23.899 5.386   19.210 1.000 9.57  ? 44   ASP A HA   1 
ATOM   553  H  HB2  . ASP A 1 44  ? 21.448 4.071   19.760 1.000 10.27 ? 44   ASP A HB2  1 
ATOM   554  N  N    . CYS A 1 45  ? 21.784 6.678   21.217 1.000 6.57  ? 45   CYS A N    1 
ATOM   555  C  CA   . CYS A 1 45  ? 21.214 7.978   21.565 1.000 6.37  ? 45   CYS A CA   1 
ATOM   556  C  C    . CYS A 1 45  ? 22.260 9.041   21.859 1.000 6.23  ? 45   CYS A C    1 
ATOM   557  O  O    . CYS A 1 45  ? 22.096 10.181  21.442 1.000 6.68  ? 45   CYS A O    1 
ATOM   558  C  CB   . CYS A 1 45  ? 20.255 7.816   22.748 1.000 6.28  ? 45   CYS A CB   1 
ATOM   559  S  SG   . CYS A 1 45  ? 18.651 7.108   22.338 1.000 6.57  ? 45   CYS A SG   1 
ATOM   560  H  H    . CYS A 1 45  ? 21.684 6.001   21.739 1.000 7.89  ? 45   CYS A H    1 
ATOM   561  H  HA   . CYS A 1 45  ? 20.688 8.285   20.797 1.000 7.65  ? 45   CYS A HA   1 
ATOM   562  H  HB2  . CYS A 1 45  ? 20.679 7.252   23.414 1.000 7.53  ? 45   CYS A HB2  1 
ATOM   563  H  HB3  . CYS A 1 45  ? 20.113 8.687   23.151 1.000 7.53  ? 45   CYS A HB3  1 
ATOM   564  N  N    . ILE A 1 46  ? 23.317 8.686   22.603 1.000 6.27  ? 46   ILE A N    1 
ATOM   565  C  CA   . ILE A 1 46  ? 24.395 9.633   22.833 1.000 6.36  ? 46   ILE A CA   1 
ATOM   566  C  C    . ILE A 1 46  ? 24.935 10.134  21.512 1.000 6.61  ? 46   ILE A C    1 
ATOM   567  O  O    . ILE A 1 46  ? 25.127 11.332  21.308 1.000 6.98  ? 46   ILE A O    1 
ATOM   568  C  CB   . ILE A 1 46  ? 25.496 9.009   23.710 1.000 6.59  ? 46   ILE A CB   1 
ATOM   569  C  CG1  . ILE A 1 46  ? 24.974 8.775   25.137 1.000 6.75  ? 46   ILE A CG1  1 
ATOM   570  C  CG2  . ILE A 1 46  ? 26.785 9.798   23.672 1.000 7.62  ? 46   ILE A CG2  1 
ATOM   571  C  CD1  . ILE A 1 46  ? 25.916 7.903   25.979 1.000 7.77  ? 46   ILE A CD1  1 
ATOM   572  H  H    . ILE A 1 46  ? 23.357 7.897   22.943 1.000 7.52  ? 46   ILE A H    1 
ATOM   573  H  HA   . ILE A 1 46  ? 24.024 10.400  23.317 1.000 7.63  ? 46   ILE A HA   1 
ATOM   574  H  HB   . ILE A 1 46  ? 25.692 8.126   23.332 1.000 7.90  ? 46   ILE A HB   1 
ATOM   575  H  HG12 . ILE A 1 46  ? 24.858 9.635   25.570 1.000 8.10  ? 46   ILE A HG12 1 
ATOM   576  H  HG23 . ILE A 1 46  ? 26.621 10.683  24.007 1.000 11.43 ? 46   ILE A HG23 1 
ATOM   577  N  N    . LYS A 1 47  ? 25.206 9.191   20.599 1.000 6.82  ? 47   LYS A N    1 
ATOM   578  C  CA   . LYS A 1 47  ? 25.731 9.559   19.271 1.000 7.49  ? 47   LYS A CA   1 
ATOM   579  C  C    . LYS A 1 47  ? 24.790 10.495  18.530 1.000 7.31  ? 47   LYS A C    1 
ATOM   580  O  O    . LYS A 1 47  ? 25.180 11.495  17.957 1.000 8.20  ? 47   LYS A O    1 
ATOM   581  C  CB   . LYS A 1 47  ? 26.006 8.267   18.461 1.000 8.80  ? 47   LYS A CB   1 
ATOM   582  C  CG   . LYS A 1 47  ? 27.190 7.461   18.967 1.000 9.55  ? 47   LYS A CG   1 
ATOM   583  C  CD   . LYS A 1 47  ? 27.231 6.054   18.329 1.000 11.34 ? 47   LYS A CD   1 
ATOM   584  C  CE   . LYS A 1 47  ? 28.514 5.357   18.737 1.000 12.44 ? 47   LYS A CE   1 
ATOM   585  N  NZ   . LYS A 1 47  ? 28.517 3.912   18.291 1.000 14.48 ? 47   LYS A NZ   1 
ATOM   586  H  H    . LYS A 1 47  ? 25.071 8.363   20.790 1.000 8.19  ? 47   LYS A H    1 
ATOM   587  H  HA   . LYS A 1 47  ? 26.584 10.024  19.400 1.000 8.99  ? 47   LYS A HA   1 
ATOM   588  H  HG3  . LYS A 1 47  ? 27.116 7.365   19.929 1.000 11.47 ? 47   LYS A HG3  1 
ATOM   589  H  HE3  . LYS A 1 47  ? 28.569 5.374   19.705 1.000 14.93 ? 47   LYS A HE3  1 
ATOM   590  N  N    . ALA A 1 48  ? 23.469 10.143  18.562 1.000 7.29  ? 48   ALA A N    1 
ATOM   591  C  CA   . ALA A 1 48  ? 22.474 10.935  17.885 1.000 7.64  ? 48   ALA A CA   1 
ATOM   592  C  C    . ALA A 1 48  ? 22.418 12.366  18.462 1.000 6.74  ? 48   ALA A C    1 
ATOM   593  O  O    . ALA A 1 48  ? 22.335 13.336  17.720 1.000 7.75  ? 48   ALA A O    1 
ATOM   594  C  CB   . ALA A 1 48  ? 21.115 10.276  17.953 1.000 8.82  ? 48   ALA A CB   1 
ATOM   595  H  H    . ALA A 1 48  ? 23.229 9.439   18.992 1.000 8.75  ? 48   ALA A H    1 
ATOM   596  H  HB1  . ALA A 1 48  ? 20.864 10.151  18.871 1.000 13.22 ? 48   ALA A HB1  1 
ATOM   597  N  N    . ILE A 1 49  ? 22.456 12.483  19.774 1.000 6.15  ? 49   ILE A N    1 
ATOM   598  C  CA   . ILE A 1 49  ? 22.412 13.807  20.393 1.000 6.42  ? 49   ILE A CA   1 
ATOM   599  C  C    . ILE A 1 49  ? 23.649 14.612  20.034 1.000 6.33  ? 49   ILE A C    1 
ATOM   600  O  O    . ILE A 1 49  ? 23.558 15.771  19.639 1.000 6.60  ? 49   ILE A O    1 
ATOM   601  C  CB   . ILE A 1 49  ? 22.199 13.685  21.909 1.000 5.89  ? 49   ILE A CB   1 
ATOM   602  C  CG1  . ILE A 1 49  ? 20.831 13.081  22.212 1.000 6.29  ? 49   ILE A CG1  1 
ATOM   603  C  CG2  . ILE A 1 49  ? 22.384 15.027  22.572 1.000 6.63  ? 49   ILE A CG2  1 
ATOM   604  C  CD1  . ILE A 1 49  ? 20.667 12.580  23.630 1.000 7.07  ? 49   ILE A CD1  1 
ATOM   605  H  H    . ILE A 1 49  ? 22.506 11.779  20.267 1.000 7.38  ? 49   ILE A H    1 
ATOM   606  H  HB   . ILE A 1 49  ? 22.882 13.077  22.261 1.000 7.06  ? 49   ILE A HB   1 
ATOM   607  H  HG12 . ILE A 1 49  ? 20.151 13.751  22.040 1.000 7.55  ? 49   ILE A HG12 1 
ATOM   608  H  HG13 . ILE A 1 49  ? 20.675 12.343  21.603 1.000 7.55  ? 49   ILE A HG13 1 
ATOM   609  H  HG21 . ILE A 1 49  ? 23.254 15.372  22.358 1.000 9.94  ? 49   ILE A HG21 1 
ATOM   610  H  HG22 . ILE A 1 49  ? 21.711 15.635  22.257 1.000 9.94  ? 49   ILE A HG22 1 
ATOM   611  H  HG23 . ILE A 1 49  ? 22.305 14.927  23.523 1.000 9.94  ? 49   ILE A HG23 1 
ATOM   612  H  HD11 . ILE A 1 49  ? 19.785 12.217  23.742 1.000 10.61 ? 49   ILE A HD11 1 
ATOM   613  H  HD12 . ILE A 1 49  ? 21.319 11.897  23.805 1.000 10.61 ? 49   ILE A HD12 1 
ATOM   614  H  HD13 . ILE A 1 49  ? 20.794 13.308  24.243 1.000 10.61 ? 49   ILE A HD13 1 
ATOM   615  N  N    . ALA A 1 50  ? 24.817 14.004  20.101 1.000 6.67  ? 50   ALA A N    1 
ATOM   616  C  CA   . ALA A 1 50  ? 26.041 14.713  19.705 1.000 7.09  ? 50   ALA A CA   1 
ATOM   617  C  C    . ALA A 1 50  ? 26.013 15.097  18.251 1.000 7.66  ? 50   ALA A C    1 
ATOM   618  O  O    . ALA A 1 50  ? 26.573 16.142  17.871 1.000 10.16 ? 50   ALA A O    1 
ATOM   619  C  CB   . ALA A 1 50  ? 27.280 13.892  20.019 1.000 7.86  ? 50   ALA A CB   1 
ATOM   620  H  H    . ALA A 1 50  ? 24.863 13.191  20.378 1.000 8.01  ? 50   ALA A H    1 
ATOM   621  H  HA   . ALA A 1 50  ? 26.090 15.539  20.230 1.000 8.51  ? 50   ALA A HA   1 
ATOM   622  H  HB2  . ALA A 1 50  ? 27.322 13.713  20.961 1.000 11.78 ? 50   ALA A HB2  1 
ATOM   623  H  HB3  . ALA A 1 50  ? 27.233 13.062  19.538 1.000 11.78 ? 50   ALA A HB3  1 
ATOM   624  N  N    . ASN A 1 51  ? 25.344 14.318  17.405 1.000 7.97  ? 51   ASN A N    1 
ATOM   625  C  CA   . ASN A 1 51  ? 25.207 14.615  15.982 1.000 8.82  ? 51   ASN A CA   1 
ATOM   626  C  C    . ASN A 1 51  ? 24.010 15.503  15.655 1.000 9.04  ? 51   ASN A C    1 
ATOM   627  O  O    . ASN A 1 51  ? 23.712 15.702  14.467 1.000 11.09 ? 51   ASN A O    1 
ATOM   628  C  CB   A ASN A 1 51  ? 25.114 13.322  15.182 0.614 10.31 ? 51   ASN A CB   1 
ATOM   629  C  CB   B ASN A 1 51  ? 25.199 13.297  15.197 0.386 11.99 ? 51   ASN A CB   1 
ATOM   630  C  CG   A ASN A 1 51  ? 26.428 12.602  15.077 0.614 14.70 ? 51   ASN A CG   1 
ATOM   631  C  CG   B ASN A 1 51  ? 25.609 13.508  13.752 0.386 14.36 ? 51   ASN A CG   1 
ATOM   632  O  OD1  A ASN A 1 51  ? 27.461 13.280  15.061 0.614 21.51 ? 51   ASN A OD1  1 
ATOM   633  O  OD1  B ASN A 1 51  ? 26.570 14.199  13.433 0.386 17.56 ? 51   ASN A OD1  1 
ATOM   634  N  ND2  A ASN A 1 51  ? 26.363 11.260  14.974 0.614 19.95 ? 51   ASN A ND2  1 
ATOM   635  N  ND2  B ASN A 1 51  ? 24.849 12.950  12.826 0.386 21.12 ? 51   ASN A ND2  1 
ATOM   636  H  H    . ASN A 1 51  ? 24.975 13.605  17.711 1.000 9.56  ? 51   ASN A H    1 
ATOM   637  N  N    . ASN A 1 52  ? 23.330 16.043  16.647 1.000 8.16  ? 52   ASN A N    1 
ATOM   638  C  CA   A ASN A 1 52  ? 22.206 16.957  16.423 0.892 7.79  ? 52   ASN A CA   1 
ATOM   639  C  CA   B ASN A 1 52  ? 22.236 16.958  16.354 0.108 7.59  ? 52   ASN A CA   1 
ATOM   640  C  C    . ASN A 1 52  ? 21.088 16.288  15.639 1.000 7.73  ? 52   ASN A C    1 
ATOM   641  O  O    . ASN A 1 52  ? 20.373 16.924  14.871 1.000 9.10  ? 52   ASN A O    1 
ATOM   642  C  CB   A ASN A 1 52  ? 22.664 18.271  15.775 0.892 9.02  ? 52   ASN A CB   1 
ATOM   643  C  CB   B ASN A 1 52  ? 22.839 18.122  15.541 0.108 10.13 ? 52   ASN A CB   1 
ATOM   644  C  CG   A ASN A 1 52  ? 21.639 19.390  15.858 0.892 9.42  ? 52   ASN A CG   1 
ATOM   645  C  CG   B ASN A 1 52  ? 23.750 18.866  16.518 0.108 9.85  ? 52   ASN A CG   1 
ATOM   646  O  OD1  A ASN A 1 52  ? 20.694 19.424  16.639 0.892 8.84  ? 52   ASN A OD1  1 
ATOM   647  O  OD1  B ASN A 1 52  ? 23.159 19.547  17.347 0.108 11.12 ? 52   ASN A OD1  1 
ATOM   648  N  ND2  A ASN A 1 52  ? 21.805 20.342  14.934 0.892 12.55 ? 52   ASN A ND2  1 
ATOM   649  N  ND2  B ASN A 1 52  ? 25.061 18.742  16.399 0.108 11.60 ? 52   ASN A ND2  1 
ATOM   650  H  H    A ASN A 1 52  ? 23.554 15.851  17.455 1.000 9.80  ? 52   ASN A H    1 
ATOM   651  H  HA   A ASN A 1 52  ? 21.842 17.184  17.304 0.892 9.35  ? 52   ASN A HA   1 
ATOM   652  H  HA   B ASN A 1 52  ? 21.901 17.318  17.202 0.108 9.11  ? 52   ASN A HA   1 
ATOM   653  H  HB2  A ASN A 1 52  ? 23.481 18.563  16.208 0.892 10.83 ? 52   ASN A HB2  1 
ATOM   654  H  HB3  A ASN A 1 52  ? 22.868 18.104  14.842 0.892 10.83 ? 52   ASN A HB3  1 
ATOM   655  N  N    . GLU A 1 53  ? 20.861 15.026  15.943 1.000 8.01  ? 53   GLU A N    1 
ATOM   656  C  CA   A GLU A 1 53  ? 19.730 14.232  15.448 0.456 8.31  ? 53   GLU A CA   1 
ATOM   657  C  CA   B GLU A 1 53  ? 19.748 14.209  15.456 0.544 7.90  ? 53   GLU A CA   1 
ATOM   658  C  C    . GLU A 1 53  ? 18.678 14.008  16.550 1.000 8.08  ? 53   GLU A C    1 
ATOM   659  O  O    . GLU A 1 53  ? 17.571 13.527  16.237 1.000 10.85 ? 53   GLU A O    1 
ATOM   660  C  CB   A GLU A 1 53  ? 20.195 12.893  14.898 0.456 9.20  ? 53   GLU A CB   1 
ATOM   661  C  CB   B GLU A 1 53  ? 20.195 12.837  15.027 0.544 10.86 ? 53   GLU A CB   1 
ATOM   662  C  CG   A GLU A 1 53  ? 21.008 13.054  13.623 0.456 12.28 ? 53   GLU A CG   1 
ATOM   663  C  CG   B GLU A 1 53  ? 21.192 12.725  13.891 0.544 13.62 ? 53   GLU A CG   1 
ATOM   664  C  CD   A GLU A 1 53  ? 21.945 11.912  13.336 0.456 14.46 ? 53   GLU A CD   1 
ATOM   665  C  CD   B GLU A 1 53  ? 21.704 11.295  13.817 0.544 20.38 ? 53   GLU A CD   1 
ATOM   666  O  OE1  A GLU A 1 53  ? 22.708 12.067  12.368 0.456 20.01 ? 53   GLU A OE1  1 
ATOM   667  O  OE1  B GLU A 1 53  ? 20.856 10.384  13.918 0.544 29.29 ? 53   GLU A OE1  1 
ATOM   668  O  OE2  A GLU A 1 53  ? 22.009 10.863  14.020 0.456 15.95 ? 53   GLU A OE2  1 
ATOM   669  O  OE2  B GLU A 1 53  ? 22.932 11.092  13.677 0.544 22.85 ? 53   GLU A OE2  1 
ATOM   670  H  H    A GLU A 1 53  ? 21.417 14.639  16.472 1.000 9.61  ? 53   GLU A H    1 
ATOM   671  H  HA   A GLU A 1 53  ? 19.305 14.729  14.719 0.456 9.98  ? 53   GLU A HA   1 
ATOM   672  H  HA   B GLU A 1 53  ? 19.335 14.661  14.690 0.544 9.48  ? 53   GLU A HA   1 
ATOM   673  H  HB2  A GLU A 1 53  ? 20.684 12.445  15.589 0.456 11.03 ? 53   GLU A HB2  1 
ATOM   674  H  HG2  A GLU A 1 53  ? 20.398 13.150  12.876 0.456 14.73 ? 53   GLU A HG2  1 
ATOM   675  H  HG2  B GLU A 1 53  ? 20.765 12.967  13.054 0.544 16.34 ? 53   GLU A HG2  1 
ATOM   676  H  HG3  A GLU A 1 53  ? 21.526 13.872  13.687 0.456 14.73 ? 53   GLU A HG3  1 
ATOM   677  H  HG3  B GLU A 1 53  ? 21.932 13.333  14.042 0.544 16.34 ? 53   GLU A HG3  1 
ATOM   678  N  N    . ALA A 1 54  ? 19.009 14.312  17.770 1.000 6.98  ? 54   ALA A N    1 
ATOM   679  C  CA   . ALA A 1 54  ? 18.123 14.244  18.913 1.000 6.57  ? 54   ALA A CA   1 
ATOM   680  C  C    . ALA A 1 54  ? 18.677 15.235  19.935 1.000 6.06  ? 54   ALA A C    1 
ATOM   681  O  O    . ALA A 1 54  ? 19.791 15.706  19.764 1.000 6.41  ? 54   ALA A O    1 
ATOM   682  C  CB   . ALA A 1 54  ? 17.981 12.840  19.484 1.000 7.83  ? 54   ALA A CB   1 
ATOM   683  H  H    . ALA A 1 54  ? 19.816 14.574  17.908 1.000 8.37  ? 54   ALA A H    1 
ATOM   684  H  HB2  . ALA A 1 54  ? 17.620 12.254  18.816 1.000 11.75 ? 54   ALA A HB2  1 
ATOM   685  N  N    . ASP A 1 55  ? 17.888 15.493  20.992 1.000 5.83  ? 55   ASP A N    1 
ATOM   686  C  CA   . ASP A 1 55  ? 18.301 16.545  21.947 1.000 5.58  ? 55   ASP A CA   1 
ATOM   687  C  C    . ASP A 1 55  ? 18.530 16.075  23.361 1.000 5.48  ? 55   ASP A C    1 
ATOM   688  O  O    . ASP A 1 55  ? 19.279 16.756  24.080 1.000 6.10  ? 55   ASP A O    1 
ATOM   689  C  CB   . ASP A 1 55  ? 17.267 17.680  21.950 1.000 6.23  ? 55   ASP A CB   1 
ATOM   690  C  CG   . ASP A 1 55  ? 17.122 18.256  20.550 1.000 6.55  ? 55   ASP A CG   1 
ATOM   691  O  OD1  . ASP A 1 55  ? 18.160 18.664  20.003 1.000 7.43  ? 55   ASP A OD1  1 
ATOM   692  O  OD2  . ASP A 1 55  ? 15.992 18.278  20.030 1.000 6.96  ? 55   ASP A OD2  1 
ATOM   693  H  H    . ASP A 1 55  ? 17.158 15.055  21.111 1.000 7.00  ? 55   ASP A H    1 
ATOM   694  H  HA   . ASP A 1 55  ? 19.146 16.920  21.623 1.000 6.70  ? 55   ASP A HA   1 
ATOM   695  H  HB2  . ASP A 1 55  ? 16.411 17.340  22.253 1.000 7.47  ? 55   ASP A HB2  1 
ATOM   696  H  HB3  . ASP A 1 55  ? 17.550 18.377  22.562 1.000 7.47  ? 55   ASP A HB3  1 
ATOM   697  N  N    . ALA A 1 56  ? 17.893 14.998  23.845 1.000 5.43  ? 56   ALA A N    1 
ATOM   698  C  CA   . ALA A 1 56  ? 18.003 14.706  25.279 1.000 5.44  ? 56   ALA A CA   1 
ATOM   699  C  C    . ALA A 1 56  ? 17.682 13.239  25.532 1.000 5.24  ? 56   ALA A C    1 
ATOM   700  O  O    . ALA A 1 56  ? 16.951 12.601  24.789 1.000 5.81  ? 56   ALA A O    1 
ATOM   701  C  CB   . ALA A 1 56  ? 16.970 15.542  26.049 1.000 6.57  ? 56   ALA A CB   1 
ATOM   702  H  HA   . ALA A 1 56  ? 18.907 14.912  25.596 1.000 6.52  ? 56   ALA A HA   1 
ATOM   703  H  HB1  . ALA A 1 56  ? 17.040 15.352  26.988 1.000 9.86  ? 56   ALA A HB1  1 
ATOM   704  H  HB2  . ALA A 1 56  ? 17.136 16.475  25.898 1.000 9.86  ? 56   ALA A HB2  1 
ATOM   705  H  HB3  . ALA A 1 56  ? 16.087 15.320  25.744 1.000 9.86  ? 56   ALA A HB3  1 
ATOM   706  N  N    . ILE A 1 57  ? 18.247 12.753  26.647 1.000 5.34  ? 57   ILE A N    1 
ATOM   707  C  CA   . ILE A 1 57  ? 17.998 11.403  27.159 1.000 5.23  ? 57   ILE A CA   1 
ATOM   708  C  C    . ILE A 1 57  ? 18.336 11.419  28.644 1.000 5.01  ? 57   ILE A C    1 
ATOM   709  O  O    . ILE A 1 57  ? 19.295 12.104  29.042 1.000 5.81  ? 57   ILE A O    1 
ATOM   710  C  CB   . ILE A 1 57  ? 18.824 10.327  26.411 1.000 5.36  ? 57   ILE A CB   1 
ATOM   711  C  CG1  . ILE A 1 57  ? 18.494 8.919   26.950 1.000 6.25  ? 57   ILE A CG1  1 
ATOM   712  C  CG2  . ILE A 1 57  ? 20.318 10.610  26.492 1.000 5.70  ? 57   ILE A CG2  1 
ATOM   713  C  CD1  . ILE A 1 57  ? 18.984 7.816   26.038 1.000 6.68  ? 57   ILE A CD1  1 
ATOM   714  H  H    . ILE A 1 57  ? 18.784 13.262  27.086 1.000 6.40  ? 57   ILE A H    1 
ATOM   715  H  HA   . ILE A 1 57  ? 17.045 11.197  27.055 1.000 6.28  ? 57   ILE A HA   1 
ATOM   716  H  HB   . ILE A 1 57  ? 18.564 10.354  25.466 1.000 6.43  ? 57   ILE A HB   1 
ATOM   717  H  HG21 . ILE A 1 57  ? 20.479 11.481  26.167 1.000 8.55  ? 57   ILE A HG21 1 
ATOM   718  H  HG23 . ILE A 1 57  ? 20.787 9.975   25.971 1.000 8.55  ? 57   ILE A HG23 1 
ATOM   719  H  HD11 . ILE A 1 57  ? 18.837 6.958   26.435 1.000 10.03 ? 57   ILE A HD11 1 
ATOM   720  N  N    . SER A 1 58  ? 17.617 10.665  29.469 1.000 5.06  ? 58   SER A N    1 
ATOM   721  C  CA   A SER A 1 58  ? 18.006 10.466  30.873 0.471 5.29  ? 58   SER A CA   1 
ATOM   722  C  CA   B SER A 1 58  ? 17.986 10.427  30.860 0.529 5.46  ? 58   SER A CA   1 
ATOM   723  C  C    . SER A 1 58  ? 18.885 9.224   30.989 1.000 5.15  ? 58   SER A C    1 
ATOM   724  O  O    . SER A 1 58  ? 18.577 8.176   30.431 1.000 7.60  ? 58   SER A O    1 
ATOM   725  C  CB   A SER A 1 58  ? 16.763 10.345  31.766 0.471 6.88  ? 58   SER A CB   1 
ATOM   726  C  CB   B SER A 1 58  ? 16.749 10.031  31.698 0.529 7.61  ? 58   SER A CB   1 
ATOM   727  O  OG   A SER A 1 58  ? 17.126 10.359  33.150 0.471 5.53  ? 58   SER A OG   1 
ATOM   728  O  OG   B SER A 1 58  ? 15.820 11.026  31.587 0.529 6.34  ? 58   SER A OG   1 
ATOM   729  H  H    A SER A 1 58  ? 16.905 10.284  29.174 1.000 6.07  ? 58   SER A H    1 
ATOM   730  H  HA   A SER A 1 58  ? 18.526 11.244  31.166 0.471 6.35  ? 58   SER A HA   1 
ATOM   731  H  HA   B SER A 1 58  ? 18.418 11.220  31.241 0.529 6.55  ? 58   SER A HA   1 
ATOM   732  N  N    . LEU A 1 59  ? 19.960 9.373   31.735 1.000 5.00  ? 59   LEU A N    1 
ATOM   733  C  CA   . LEU A 1 59  ? 20.942 8.290   31.866 1.000 4.95  ? 59   LEU A CA   1 
ATOM   734  C  C    . LEU A 1 59  ? 21.295 8.029   33.329 1.000 4.61  ? 59   LEU A C    1 
ATOM   735  O  O    . LEU A 1 59  ? 21.398 8.962   34.141 1.000 5.06  ? 59   LEU A O    1 
ATOM   736  C  CB   . LEU A 1 59  ? 22.230 8.668   31.131 1.000 5.01  ? 59   LEU A CB   1 
ATOM   737  C  CG   . LEU A 1 59  ? 22.105 8.831   29.626 1.000 5.44  ? 59   LEU A CG   1 
ATOM   738  C  CD1  . LEU A 1 59  ? 23.446 9.322   29.062 1.000 6.37  ? 59   LEU A CD1  1 
ATOM   739  C  CD2  . LEU A 1 59  ? 21.663 7.547   28.920 1.000 6.39  ? 59   LEU A CD2  1 
ATOM   740  H  HA   . LEU A 1 59  ? 20.575 7.472   31.472 1.000 5.94  ? 59   LEU A HA   1 
ATOM   741  H  HB2  . LEU A 1 59  ? 22.560 9.501   31.502 1.000 6.01  ? 59   LEU A HB2  1 
ATOM   742  H  HB3  . LEU A 1 59  ? 22.895 7.986   31.311 1.000 6.01  ? 59   LEU A HB3  1 
ATOM   743  H  HG   . LEU A 1 59  ? 21.431 9.520   29.451 1.000 6.53  ? 59   LEU A HG   1 
ATOM   744  H  HD11 . LEU A 1 59  ? 23.708 10.126  29.516 1.000 9.55  ? 59   LEU A HD11 1 
ATOM   745  H  HD12 . LEU A 1 59  ? 24.116 8.647   29.195 1.000 9.55  ? 59   LEU A HD12 1 
ATOM   746  H  HD13 . LEU A 1 59  ? 23.353 9.499   28.124 1.000 9.55  ? 59   LEU A HD13 1 
ATOM   747  N  N    . ASP A 1 60  ? 21.547 6.768   33.622 1.000 4.80  ? 60   ASP A N    1 
ATOM   748  C  CA   . ASP A 1 60  ? 22.227 6.412   34.854 1.000 5.02  ? 60   ASP A CA   1 
ATOM   749  C  C    . ASP A 1 60  ? 23.586 7.082   34.898 1.000 4.89  ? 60   ASP A C    1 
ATOM   750  O  O    . ASP A 1 60  ? 24.218 7.353   33.853 1.000 5.08  ? 60   ASP A O    1 
ATOM   751  C  CB   . ASP A 1 60  ? 22.395 4.875   34.905 1.000 5.08  ? 60   ASP A CB   1 
ATOM   752  C  CG   . ASP A 1 60  ? 23.250 4.452   36.082 1.000 5.09  ? 60   ASP A CG   1 
ATOM   753  O  OD1  . ASP A 1 60  ? 22.789 4.453   37.231 1.000 5.61  ? 60   ASP A OD1  1 
ATOM   754  O  OD2  . ASP A 1 60  ? 24.459 4.158   35.796 1.000 6.05  ? 60   ASP A OD2  1 
ATOM   755  H  HA   . ASP A 1 60  ? 21.692 6.707   35.620 1.000 6.02  ? 60   ASP A HA   1 
ATOM   756  H  HB2  . ASP A 1 60  ? 21.521 4.459   34.976 1.000 6.09  ? 60   ASP A HB2  1 
ATOM   757  H  HB3  . ASP A 1 60  ? 22.806 4.569   34.082 1.000 6.09  ? 60   ASP A HB3  1 
ATOM   758  N  N    . GLY A 1 61  ? 24.114 7.323   36.103 1.000 5.56  ? 61   GLY A N    1 
ATOM   759  C  CA   . GLY A 1 61  ? 25.402 7.979   36.210 1.000 5.60  ? 61   GLY A CA   1 
ATOM   760  C  C    . GLY A 1 61  ? 26.530 7.315   35.467 1.000 5.64  ? 61   GLY A C    1 
ATOM   761  O  O    . GLY A 1 61  ? 27.430 8.004   34.948 1.000 6.09  ? 61   GLY A O    1 
ATOM   762  H  H    . GLY A 1 61  ? 23.689 7.088   36.813 1.000 6.67  ? 61   GLY A H    1 
ATOM   763  H  HA2  . GLY A 1 61  ? 25.311 8.887   35.881 1.000 6.72  ? 61   GLY A HA2  1 
ATOM   764  H  HA3  . GLY A 1 61  ? 25.642 8.032   37.148 1.000 6.72  ? 61   GLY A HA3  1 
ATOM   765  N  N    . GLY A 1 62  ? 26.532 5.977   35.379 1.000 5.82  ? 62   GLY A N    1 
ATOM   766  C  CA   . GLY A 1 62  ? 27.572 5.339   34.605 1.000 6.30  ? 62   GLY A CA   1 
ATOM   767  C  C    . GLY A 1 62  ? 27.553 5.710   33.139 1.000 6.10  ? 62   GLY A C    1 
ATOM   768  O  O    . GLY A 1 62  ? 28.603 5.764   32.474 1.000 7.26  ? 62   GLY A O    1 
ATOM   769  H  H    . GLY A 1 62  ? 25.928 5.509   35.774 1.000 6.98  ? 62   GLY A H    1 
ATOM   770  H  HA2  . GLY A 1 62  ? 28.433 5.581   34.979 1.000 7.56  ? 62   GLY A HA2  1 
ATOM   771  H  HA3  . GLY A 1 62  ? 27.476 4.377   34.685 1.000 7.56  ? 62   GLY A HA3  1 
ATOM   772  N  N    . GLN A 1 63  ? 26.359 5.950   32.606 1.000 6.20  ? 63   GLN A N    1 
ATOM   773  C  CA   . GLN A 1 63  ? 26.225 6.401   31.220 1.000 6.07  ? 63   GLN A CA   1 
ATOM   774  C  C    . GLN A 1 63  ? 26.330 7.902   31.085 1.000 5.41  ? 63   GLN A C    1 
ATOM   775  O  O    . GLN A 1 63  ? 26.756 8.371   30.018 1.000 5.95  ? 63   GLN A O    1 
ATOM   776  C  CB   A GLN A 1 63  ? 24.967 5.846   30.555 0.792 7.49  ? 63   GLN A CB   1 
ATOM   777  C  CB   B GLN A 1 63  ? 25.005 5.673   30.634 0.208 5.54  ? 63   GLN A CB   1 
ATOM   778  C  CG   A GLN A 1 63  ? 25.095 4.368   30.174 0.792 6.97  ? 63   GLN A CG   1 
ATOM   779  C  CG   B GLN A 1 63  ? 25.313 4.175   30.812 0.208 7.04  ? 63   GLN A CG   1 
ATOM   780  C  CD   A GLN A 1 63  ? 24.896 3.456   31.378 0.792 7.80  ? 63   GLN A CD   1 
ATOM   781  C  CD   B GLN A 1 63  ? 24.187 3.206   30.677 0.208 6.87  ? 63   GLN A CD   1 
ATOM   782  O  OE1  A GLN A 1 63  ? 23.953 3.609   32.119 0.792 9.45  ? 63   GLN A OE1  1 
ATOM   783  O  OE1  B GLN A 1 63  ? 23.007 3.529   30.645 0.208 13.32 ? 63   GLN A OE1  1 
ATOM   784  N  NE2  A GLN A 1 63  ? 25.787 2.484   31.530 0.792 10.05 ? 63   GLN A NE2  1 
ATOM   785  N  NE2  B GLN A 1 63  ? 24.546 1.923   30.545 0.208 9.98  ? 63   GLN A NE2  1 
ATOM   786  H  HA   A GLN A 1 63  ? 26.986 6.025   30.731 1.000 7.28  ? 63   GLN A HA   1 
ATOM   787  H  HB2  A GLN A 1 63  ? 24.261 5.932   31.197 0.792 8.99  ? 63   GLN A HB2  1 
ATOM   788  H  HB3  B GLN A 1 63  ? 24.881 6.118   29.797 0.208 6.65  ? 63   GLN A HB3  1 
ATOM   789  H  HG2  A GLN A 1 63  ? 24.439 4.092   29.532 0.792 8.36  ? 63   GLN A HG2  1 
ATOM   790  N  N    . VAL A 1 64  ? 26.033 8.691   32.132 1.000 5.15  ? 64   VAL A N    1 
ATOM   791  C  CA   . VAL A 1 64  ? 26.396 10.093  32.140 1.000 5.14  ? 64   VAL A CA   1 
ATOM   792  C  C    . VAL A 1 64  ? 27.912 10.257  31.935 1.000 4.95  ? 64   VAL A C    1 
ATOM   793  O  O    . VAL A 1 64  ? 28.366 11.098  31.174 1.000 5.65  ? 64   VAL A O    1 
ATOM   794  C  CB   . VAL A 1 64  ? 25.949 10.783  33.463 1.000 5.04  ? 64   VAL A CB   1 
ATOM   795  C  CG1  . VAL A 1 64  ? 26.505 12.188  33.589 1.000 6.30  ? 64   VAL A CG1  1 
ATOM   796  C  CG2  . VAL A 1 64  ? 24.421 10.807  33.591 1.000 5.62  ? 64   VAL A CG2  1 
ATOM   797  H  H    . VAL A 1 64  ? 25.619 8.358   32.808 1.000 6.18  ? 64   VAL A H    1 
ATOM   798  H  HA   . VAL A 1 64  ? 25.937 10.533  31.395 1.000 6.16  ? 64   VAL A HA   1 
ATOM   799  H  HB   . VAL A 1 64  ? 26.302 10.255  34.209 1.000 6.04  ? 64   VAL A HB   1 
ATOM   800  H  HG12 . VAL A 1 64  ? 26.136 12.739  32.896 1.000 9.45  ? 64   VAL A HG12 1 
ATOM   801  H  HG13 . VAL A 1 64  ? 26.266 12.549  34.446 1.000 9.45  ? 64   VAL A HG13 1 
ATOM   802  H  HG21 . VAL A 1 64  ? 24.079 9.914   33.510 1.000 8.43  ? 64   VAL A HG21 1 
ATOM   803  H  HG22 . VAL A 1 64  ? 24.177 11.167  34.448 1.000 8.43  ? 64   VAL A HG22 1 
ATOM   804  H  HG23 . VAL A 1 64  ? 24.050 11.356  32.897 1.000 8.43  ? 64   VAL A HG23 1 
ATOM   805  N  N    . PHE A 1 65  ? 28.666 9.397   32.587 1.000 5.35  ? 65   PHE A N    1 
ATOM   806  C  CA   . PHE A 1 65  ? 30.133 9.375   32.408 1.000 5.44  ? 65   PHE A CA   1 
ATOM   807  C  C    . PHE A 1 65  ? 30.454 9.184   30.941 1.000 5.51  ? 65   PHE A C    1 
ATOM   808  O  O    . PHE A 1 65  ? 31.209 9.933   30.330 1.000 6.06  ? 65   PHE A O    1 
ATOM   809  C  CB   . PHE A 1 65  ? 30.721 8.227   33.260 1.000 6.13  ? 65   PHE A CB   1 
ATOM   810  C  CG   . PHE A 1 65  ? 32.200 8.017   33.093 1.000 6.84  ? 65   PHE A CG   1 
ATOM   811  C  CD1  . PHE A 1 65  ? 33.068 8.594   34.049 1.000 8.45  ? 65   PHE A CD1  1 
ATOM   812  C  CD2  . PHE A 1 65  ? 32.743 7.318   32.038 1.000 10.37 ? 65   PHE A CD2  1 
ATOM   813  C  CE1  . PHE A 1 65  ? 34.426 8.444   33.941 1.000 10.48 ? 65   PHE A CE1  1 
ATOM   814  C  CE2  . PHE A 1 65  ? 34.134 7.175   31.937 1.000 11.32 ? 65   PHE A CE2  1 
ATOM   815  C  CZ   . PHE A 1 65  ? 34.951 7.729   32.902 1.000 10.99 ? 65   PHE A CZ   1 
ATOM   816  H  H    . PHE A 1 65  ? 28.297 8.837   33.126 1.000 6.43  ? 65   PHE A H    1 
ATOM   817  H  HA   . PHE A 1 65  ? 30.508 10.228  32.713 1.000 6.52  ? 65   PHE A HA   1 
ATOM   818  H  HB3  . PHE A 1 65  ? 30.262 7.405   33.028 1.000 7.36  ? 65   PHE A HB3  1 
ATOM   819  H  HD1  . PHE A 1 65  ? 32.714 9.081   34.758 1.000 10.14 ? 65   PHE A HD1  1 
ATOM   820  H  HD2  . PHE A 1 65  ? 32.188 6.940   31.395 1.000 12.45 ? 65   PHE A HD2  1 
ATOM   821  N  N    . GLU A 1 66  ? 29.872 8.119   30.319 1.000 5.82  ? 66   GLU A N    1 
ATOM   822  C  CA   . GLU A 1 66  ? 30.209 7.824   28.939 1.000 6.60  ? 66   GLU A CA   1 
ATOM   823  C  C    . GLU A 1 66  ? 29.812 8.958   28.002 1.000 6.25  ? 66   GLU A C    1 
ATOM   824  O  O    . GLU A 1 66  ? 30.506 9.286   27.050 1.000 7.43  ? 66   GLU A O    1 
ATOM   825  C  CB   A GLU A 1 66  ? 29.560 6.480   28.598 0.491 5.66  ? 66   GLU A CB   1 
ATOM   826  C  CB   B GLU A 1 66  ? 29.490 6.574   28.430 0.509 8.77  ? 66   GLU A CB   1 
ATOM   827  C  CG   A GLU A 1 66  ? 29.903 5.909   27.257 0.491 7.07  ? 66   GLU A CG   1 
ATOM   828  C  CG   B GLU A 1 66  ? 30.137 5.394   29.118 0.509 9.27  ? 66   GLU A CG   1 
ATOM   829  C  CD   A GLU A 1 66  ? 29.336 4.531   26.971 0.491 6.85  ? 66   GLU A CD   1 
ATOM   830  C  CD   B GLU A 1 66  ? 29.663 4.121   28.462 0.509 12.46 ? 66   GLU A CD   1 
ATOM   831  O  OE1  A GLU A 1 66  ? 28.517 4.026   27.780 0.491 8.67  ? 66   GLU A OE1  1 
ATOM   832  O  OE1  B GLU A 1 66  ? 28.996 4.162   27.421 0.509 19.09 ? 66   GLU A OE1  1 
ATOM   833  O  OE2  A GLU A 1 66  ? 29.664 3.951   25.926 0.491 9.52  ? 66   GLU A OE2  1 
ATOM   834  O  OE2  B GLU A 1 66  ? 30.022 3.070   29.036 0.509 23.49 ? 66   GLU A OE2  1 
ATOM   835  H  HA   A GLU A 1 66  ? 31.181 7.713   28.884 1.000 7.92  ? 66   GLU A HA   1 
ATOM   836  H  HB2  B GLU A 1 66  ? 28.535 6.600   28.553 0.509 10.52 ? 66   GLU A HB2  1 
ATOM   837  H  HB3  A GLU A 1 66  ? 28.606 6.611   28.564 0.491 6.79  ? 66   GLU A HB3  1 
ATOM   838  N  N    . ALA A 1 67  ? 28.642 9.554   28.262 1.000 5.81  ? 67   ALA A N    1 
ATOM   839  C  CA   . ALA A 1 67  ? 28.105 10.604  27.420 1.000 6.05  ? 67   ALA A CA   1 
ATOM   840  C  C    . ALA A 1 67  ? 28.980 11.858  27.434 1.000 5.75  ? 67   ALA A C    1 
ATOM   841  O  O    . ALA A 1 67  ? 28.949 12.620  26.472 1.000 6.45  ? 67   ALA A O    1 
ATOM   842  C  CB   . ALA A 1 67  ? 26.700 10.958  27.860 1.000 6.49  ? 67   ALA A CB   1 
ATOM   843  H  H    . ALA A 1 67  ? 28.193 9.305   28.952 1.000 6.97  ? 67   ALA A H    1 
ATOM   844  H  HA   . ALA A 1 67  ? 28.064 10.269  26.500 1.000 7.26  ? 67   ALA A HA   1 
ATOM   845  H  HB1  . ALA A 1 67  ? 26.354 11.654  27.296 1.000 9.73  ? 67   ALA A HB1  1 
ATOM   846  H  HB2  . ALA A 1 67  ? 26.138 10.183  27.792 1.000 9.73  ? 67   ALA A HB2  1 
ATOM   847  H  HB3  . ALA A 1 67  ? 26.716 11.262  28.770 1.000 9.73  ? 67   ALA A HB3  1 
ATOM   848  N  N    . GLY A 1 68  ? 29.706 12.082  28.513 1.000 5.51  ? 68   GLY A N    1 
ATOM   849  C  CA   . GLY A 1 68  ? 30.550 13.228  28.621 1.000 5.91  ? 68   GLY A CA   1 
ATOM   850  C  C    . GLY A 1 68  ? 31.904 13.100  27.976 1.000 5.81  ? 68   GLY A C    1 
ATOM   851  O  O    . GLY A 1 68  ? 32.587 14.128  27.818 1.000 6.86  ? 68   GLY A O    1 
ATOM   852  H  H    . GLY A 1 68  ? 29.670 11.524  29.167 1.000 6.61  ? 68   GLY A H    1 
ATOM   853  H  HA2  . GLY A 1 68  ? 30.092 13.985  28.224 1.000 7.09  ? 68   GLY A HA2  1 
ATOM   854  H  HA3  . GLY A 1 68  ? 30.678 13.426  29.562 1.000 7.09  ? 68   GLY A HA3  1 
ATOM   855  N  N    . LEU A 1 69  ? 32.325 11.938  27.613 1.000 6.51  ? 69   LEU A N    1 
ATOM   856  C  CA   . LEU A 1 69  ? 33.632 11.738  26.981 1.000 7.04  ? 69   LEU A CA   1 
ATOM   857  C  C    . LEU A 1 69  ? 33.647 12.314  25.575 1.000 7.29  ? 69   LEU A C    1 
ATOM   858  O  O    . LEU A 1 69  ? 32.627 12.344  24.887 1.000 7.59  ? 69   LEU A O    1 
ATOM   859  C  CB   . LEU A 1 69  ? 33.972 10.250  26.911 1.000 7.38  ? 69   LEU A CB   1 
ATOM   860  C  CG   . LEU A 1 69  ? 34.042 9.540   28.283 1.000 8.32  ? 69   LEU A CG   1 
ATOM   861  C  CD1  . LEU A 1 69  ? 34.352 8.064   28.045 1.000 10.92 ? 69   LEU A CD1  1 
ATOM   862  C  CD2  . LEU A 1 69  ? 35.034 10.207  29.228 1.000 10.71 ? 69   LEU A CD2  1 
ATOM   863  H  H    . LEU A 1 69  ? 31.820 11.254  27.747 1.000 7.81  ? 69   LEU A H    1 
ATOM   864  H  HA   . LEU A 1 69  ? 34.315 12.194  27.517 1.000 8.45  ? 69   LEU A HA   1 
ATOM   865  H  HB2  . LEU A 1 69  ? 33.303 9.806   26.366 1.000 8.85  ? 69   LEU A HB2  1 
ATOM   866  H  HB3  . LEU A 1 69  ? 34.827 10.149  26.465 1.000 8.85  ? 69   LEU A HB3  1 
ATOM   867  H  HG   . LEU A 1 69  ? 33.155 9.596   28.694 1.000 9.98  ? 69   LEU A HG   1 
ATOM   868  H  HD12 . LEU A 1 69  ? 34.405 7.611   28.890 1.000 16.38 ? 69   LEU A HD12 1 
ATOM   869  H  HD23 . LEU A 1 69  ? 35.917 10.140  28.858 1.000 16.06 ? 69   LEU A HD23 1 
ATOM   870  N  N    . ALA A 1 70  ? 34.847 12.673  25.116 1.000 8.45  ? 70   ALA A N    1 
ATOM   871  C  CA   . ALA A 1 70  ? 35.010 12.964  23.697 1.000 9.10  ? 70   ALA A CA   1 
ATOM   872  C  C    . ALA A 1 70  ? 34.672 11.693  22.919 1.000 8.89  ? 70   ALA A C    1 
ATOM   873  O  O    . ALA A 1 70  ? 35.017 10.595  23.394 1.000 10.12 ? 70   ALA A O    1 
ATOM   874  C  CB   . ALA A 1 70  ? 36.467 13.412  23.436 1.000 11.44 ? 70   ALA A CB   1 
ATOM   875  H  H    . ALA A 1 70  ? 35.518 12.731  25.651 1.000 10.14 ? 70   ALA A H    1 
ATOM   876  H  HB2  . ALA A 1 70  ? 37.065 12.797  23.868 1.000 17.15 ? 70   ALA A HB2  1 
ATOM   877  N  N    . PRO A 1 71  ? 34.076 11.779  21.753 1.000 9.96  ? 71   PRO A N    1 
ATOM   878  C  CA   . PRO A 1 71  ? 33.769 13.000  21.006 1.000 11.00 ? 71   PRO A CA   1 
ATOM   879  C  C    . PRO A 1 71  ? 32.328 13.513  21.240 1.000 10.75 ? 71   PRO A C    1 
ATOM   880  O  O    . PRO A 1 71  ? 31.786 14.296  20.435 1.000 15.84 ? 71   PRO A O    1 
ATOM   881  C  CB   . PRO A 1 71  ? 33.858 12.527  19.541 1.000 13.10 ? 71   PRO A CB   1 
ATOM   882  C  CG   . PRO A 1 71  ? 33.350 11.115  19.610 1.000 12.85 ? 71   PRO A CG   1 
ATOM   883  C  CD   . PRO A 1 71  ? 33.807 10.589  20.932 1.000 11.34 ? 71   PRO A CD   1 
ATOM   884  H  HD2  . PRO A 1 71  ? 33.119 10.040  21.338 1.000 13.61 ? 71   PRO A HD2  1 
ATOM   885  H  HD3  . PRO A 1 71  ? 34.611 10.056  20.828 1.000 13.61 ? 71   PRO A HD3  1 
ATOM   886  N  N    . TYR A 1 72  ? 31.692 13.076  22.305 1.000 8.13  ? 72   TYR A N    1 
ATOM   887  C  CA   . TYR A 1 72  ? 30.290 13.398  22.552 1.000 7.56  ? 72   TYR A CA   1 
ATOM   888  C  C    . TYR A 1 72  ? 30.131 14.634  23.417 1.000 7.15  ? 72   TYR A C    1 
ATOM   889  O  O    . TYR A 1 72  ? 29.394 15.571  23.053 1.000 8.07  ? 72   TYR A O    1 
ATOM   890  C  CB   . TYR A 1 72  ? 29.575 12.186  23.197 1.000 7.73  ? 72   TYR A CB   1 
ATOM   891  C  CG   . TYR A 1 72  ? 29.829 10.923  22.422 1.000 7.77  ? 72   TYR A CG   1 
ATOM   892  C  CD1  . TYR A 1 72  ? 29.547 10.829  21.069 1.000 9.00  ? 72   TYR A CD1  1 
ATOM   893  C  CD2  . TYR A 1 72  ? 30.359 9.836   23.053 1.000 8.74  ? 72   TYR A CD2  1 
ATOM   894  C  CE1  . TYR A 1 72  ? 29.780 9.686   20.361 1.000 10.37 ? 72   TYR A CE1  1 
ATOM   895  C  CE2  . TYR A 1 72  ? 30.596 8.671   22.327 1.000 9.19  ? 72   TYR A CE2  1 
ATOM   896  C  CZ   . TYR A 1 72  ? 30.309 8.616   21.005 1.000 10.08 ? 72   TYR A CZ   1 
ATOM   897  O  OH   . TYR A 1 72  ? 30.532 7.448   20.256 1.000 14.07 ? 72   TYR A OH   1 
ATOM   898  H  H    . TYR A 1 72  ? 32.115 12.587  22.872 1.000 9.75  ? 72   TYR A H    1 
ATOM   899  H  HA   . TYR A 1 72  ? 29.863 13.577  21.688 1.000 9.07  ? 72   TYR A HA   1 
ATOM   900  H  HB2  . TYR A 1 72  ? 29.911 12.073  24.100 1.000 9.27  ? 72   TYR A HB2  1 
ATOM   901  H  HD1  . TYR A 1 72  ? 29.188 11.567  20.630 1.000 10.80 ? 72   TYR A HD1  1 
ATOM   902  H  HD2  . TYR A 1 72  ? 30.561 9.873   23.960 1.000 10.48 ? 72   TYR A HD2  1 
ATOM   903  H  HE2  . TYR A 1 72  ? 30.954 7.926   22.753 1.000 11.03 ? 72   TYR A HE2  1 
ATOM   904  N  N    . LYS A 1 73  ? 30.811 14.688  24.564 1.000 6.49  ? 73   LYS A N    1 
ATOM   905  C  CA   . LYS A 1 73  ? 30.891 15.893  25.365 1.000 6.54  ? 73   LYS A CA   1 
ATOM   906  C  C    . LYS A 1 73  ? 29.533 16.382  25.805 1.000 5.81  ? 73   LYS A C    1 
ATOM   907  O  O    . LYS A 1 73  ? 29.300 17.575  25.946 1.000 6.66  ? 73   LYS A O    1 
ATOM   908  C  CB   . LYS A 1 73  ? 31.712 17.001  24.652 1.000 7.65  ? 73   LYS A CB   1 
ATOM   909  C  CG   . LYS A 1 73  ? 33.138 16.530  24.279 1.000 9.68  ? 73   LYS A CG   1 
ATOM   910  C  CD   . LYS A 1 73  ? 34.081 16.180  25.374 1.000 10.53 ? 73   LYS A CD   1 
ATOM   911  C  CE   . LYS A 1 73  ? 34.359 17.316  26.259 1.000 11.52 ? 73   LYS A CE   1 
ATOM   912  N  NZ   . LYS A 1 73  ? 35.627 17.100  27.132 1.000 11.73 ? 73   LYS A NZ   1 
ATOM   913  H  H    . LYS A 1 73  ? 31.218 13.982  24.837 1.000 7.78  ? 73   LYS A H    1 
ATOM   914  H  HA   . LYS A 1 73  ? 31.383 15.658  26.179 1.000 7.85  ? 73   LYS A HA   1 
ATOM   915  H  HB2  . LYS A 1 73  ? 31.250 17.258  23.839 1.000 9.18  ? 73   LYS A HB2  1 
ATOM   916  H  HG3  . LYS A 1 73  ? 33.544 17.238  23.754 1.000 11.62 ? 73   LYS A HG3  1 
ATOM   917  N  N    . LEU A 1 74  ? 28.606 15.459  26.073 1.000 5.94  ? 74   LEU A N    1 
ATOM   918  C  CA   . LEU A 1 74  ? 27.301 15.849  26.594 1.000 5.86  ? 74   LEU A CA   1 
ATOM   919  C  C    . LEU A 1 74  ? 27.446 16.197  28.062 1.000 5.58  ? 74   LEU A C    1 
ATOM   920  O  O    . LEU A 1 74  ? 28.358 15.678  28.750 1.000 6.11  ? 74   LEU A O    1 
ATOM   921  C  CB   . LEU A 1 74  ? 26.269 14.745  26.397 1.000 5.84  ? 74   LEU A CB   1 
ATOM   922  C  CG   . LEU A 1 74  ? 26.128 14.238  24.957 1.000 6.42  ? 74   LEU A CG   1 
ATOM   923  C  CD1  . LEU A 1 74  ? 24.959 13.265  24.839 1.000 7.05  ? 74   LEU A CD1  1 
ATOM   924  C  CD2  . LEU A 1 74  ? 26.014 15.352  23.930 1.000 6.67  ? 74   LEU A CD2  1 
ATOM   925  H  H    . LEU A 1 74  ? 28.780 14.628  25.937 1.000 7.13  ? 74   LEU A H    1 
ATOM   926  H  HA   . LEU A 1 74  ? 27.000 16.647  26.112 1.000 7.03  ? 74   LEU A HA   1 
ATOM   927  H  HB2  . LEU A 1 74  ? 26.507 13.996  26.966 1.000 7.01  ? 74   LEU A HB2  1 
ATOM   928  H  HB3  . LEU A 1 74  ? 25.406 15.075  26.694 1.000 7.01  ? 74   LEU A HB3  1 
ATOM   929  H  HG   . LEU A 1 74  ? 26.943 13.735  24.748 1.000 7.70  ? 74   LEU A HG   1 
ATOM   930  H  HD12 . LEU A 1 74  ? 24.138 13.738  24.995 1.000 10.57 ? 74   LEU A HD12 1 
ATOM   931  H  HD13 . LEU A 1 74  ? 24.944 12.879  23.960 1.000 10.57 ? 74   LEU A HD13 1 
ATOM   932  H  HD21 . LEU A 1 74  ? 26.759 15.950  24.024 1.000 10.01 ? 74   LEU A HD21 1 
ATOM   933  H  HD22 . LEU A 1 74  ? 26.015 14.975  23.048 1.000 10.01 ? 74   LEU A HD22 1 
ATOM   934  H  HD23 . LEU A 1 74  ? 25.197 15.835  24.071 1.000 10.01 ? 74   LEU A HD23 1 
ATOM   935  N  N    . LYS A 1 75  ? 26.538 17.021  28.594 1.000 6.11  ? 75   LYS A N    1 
ATOM   936  C  CA   . LYS A 1 75  ? 26.571 17.405  29.979 1.000 6.43  ? 75   LYS A CA   1 
ATOM   937  C  C    . LYS A 1 75  ? 25.178 17.178  30.590 1.000 6.03  ? 75   LYS A C    1 
ATOM   938  O  O    . LYS A 1 75  ? 24.155 17.350  29.915 1.000 6.52  ? 75   LYS A O    1 
ATOM   939  C  CB   A LYS A 1 75  ? 26.980 18.873  30.125 0.573 6.71  ? 75   LYS A CB   1 
ATOM   940  C  CB   B LYS A 1 75  ? 26.882 18.889  30.223 0.427 9.41  ? 75   LYS A CB   1 
ATOM   941  C  CG   A LYS A 1 75  ? 28.417 19.224  29.724 0.573 13.16 ? 75   LYS A CG   1 
ATOM   942  C  CG   B LYS A 1 75  ? 28.302 19.284  29.825 0.427 6.90  ? 75   LYS A CG   1 
ATOM   943  C  CD   A LYS A 1 75  ? 28.665 20.727  29.632 0.573 10.90 ? 75   LYS A CD   1 
ATOM   944  C  CD   B LYS A 1 75  ? 28.596 20.739  30.135 0.427 10.23 ? 75   LYS A CD   1 
ATOM   945  C  CE   A LYS A 1 75  ? 28.583 21.416  30.984 0.573 11.66 ? 75   LYS A CE   1 
ATOM   946  C  CE   B LYS A 1 75  ? 30.062 21.057  29.847 0.427 9.83  ? 75   LYS A CE   1 
ATOM   947  N  NZ   A LYS A 1 75  ? 29.034 22.845  30.946 0.573 13.14 ? 75   LYS A NZ   1 
ATOM   948  N  NZ   B LYS A 1 75  ? 30.186 22.552  30.049 0.427 11.84 ? 75   LYS A NZ   1 
ATOM   949  H  H    . LYS A 1 75  ? 25.914 17.332  28.091 1.000 7.33  ? 75   LYS A H    1 
ATOM   950  H  HA   A LYS A 1 75  ? 27.221 16.844  30.450 1.000 7.72  ? 75   LYS A HA   1 
ATOM   951  H  HB2  A LYS A 1 75  ? 26.376 19.410  29.588 0.573 8.05  ? 75   LYS A HB2  1 
ATOM   952  H  HB2  B LYS A 1 75  ? 26.253 19.429  29.720 0.427 11.29 ? 75   LYS A HB2  1 
ATOM   953  H  HB3  A LYS A 1 75  ? 26.852 19.132  31.051 0.573 8.05  ? 75   LYS A HB3  1 
ATOM   954  H  HB3  B LYS A 1 75  ? 26.754 19.086  31.165 0.427 11.29 ? 75   LYS A HB3  1 
ATOM   955  N  N    . PRO A 1 76  ? 25.135 16.862  31.889 1.000 6.16  ? 76   PRO A N    1 
ATOM   956  C  CA   . PRO A 1 76  ? 23.855 16.719  32.587 1.000 5.79  ? 76   PRO A CA   1 
ATOM   957  C  C    . PRO A 1 76  ? 23.234 18.077  32.830 1.000 5.95  ? 76   PRO A C    1 
ATOM   958  O  O    . PRO A 1 76  ? 23.906 18.999  33.316 1.000 7.45  ? 76   PRO A O    1 
ATOM   959  C  CB   . PRO A 1 76  ? 24.275 16.020  33.904 1.000 7.06  ? 76   PRO A CB   1 
ATOM   960  C  CG   . PRO A 1 76  ? 25.695 16.510  34.139 1.000 7.66  ? 76   PRO A CG   1 
ATOM   961  C  CD   . PRO A 1 76  ? 26.295 16.605  32.748 1.000 7.10  ? 76   PRO A CD   1 
ATOM   962  H  HA   . PRO A 1 76  ? 23.245 16.149  32.075 1.000 6.94  ? 76   PRO A HA   1 
ATOM   963  H  HB2  . PRO A 1 76  ? 23.693 16.279  34.635 1.000 8.47  ? 76   PRO A HB2  1 
ATOM   964  H  HB3  . PRO A 1 76  ? 24.252 15.055  33.808 1.000 8.47  ? 76   PRO A HB3  1 
ATOM   965  H  HD3  . PRO A 1 76  ? 26.657 15.743  32.535 1.000 8.52  ? 76   PRO A HD3  1 
ATOM   966  N  N    . ILE A 1 77  ? 21.946 18.211  32.515 1.000 5.58  ? 77   ILE A N    1 
ATOM   967  C  CA   . ILE A 1 77  ? 21.213 19.461  32.647 1.000 6.11  ? 77   ILE A CA   1 
ATOM   968  C  C    . ILE A 1 77  ? 20.082 19.378  33.641 1.000 5.70  ? 77   ILE A C    1 
ATOM   969  O  O    . ILE A 1 77  ? 19.567 20.428  34.044 1.000 6.43  ? 77   ILE A O    1 
ATOM   970  C  CB   . ILE A 1 77  ? 20.728 19.980  31.286 1.000 6.78  ? 77   ILE A CB   1 
ATOM   971  C  CG1  . ILE A 1 77  ? 19.714 19.051  30.632 1.000 8.81  ? 77   ILE A CG1  1 
ATOM   972  C  CG2  . ILE A 1 77  ? 21.934 20.236  30.378 1.000 8.16  ? 77   ILE A CG2  1 
ATOM   973  C  CD1  . ILE A 1 77  ? 18.977 19.664  29.437 1.000 11.44 ? 77   ILE A CD1  1 
ATOM   974  H  H    . ILE A 1 77  ? 21.526 17.523  32.217 1.000 6.70  ? 77   ILE A H    1 
ATOM   975  H  HA   . ILE A 1 77  ? 21.846 20.125  32.993 1.000 7.33  ? 77   ILE A HA   1 
ATOM   976  H  HB   . ILE A 1 77  ? 20.285 20.840  31.438 1.000 8.14  ? 77   ILE A HB   1 
ATOM   977  H  HG12 . ILE A 1 77  ? 20.173 18.249  30.336 1.000 10.57 ? 77   ILE A HG12 1 
ATOM   978  H  HG13 . ILE A 1 77  ? 19.060 18.786  31.298 1.000 10.57 ? 77   ILE A HG13 1 
ATOM   979  H  HG22 . ILE A 1 77  ? 22.365 19.416  30.206 1.000 12.24 ? 77   ILE A HG22 1 
ATOM   980  N  N    . ALA A 1 78  ? 19.664 18.199  34.048 1.000 6.19  ? 78   ALA A N    1 
ATOM   981  C  CA   . ALA A 1 78  ? 18.586 18.038  35.020 1.000 6.64  ? 78   ALA A CA   1 
ATOM   982  C  C    . ALA A 1 78  ? 18.818 16.751  35.771 1.000 5.91  ? 78   ALA A C    1 
ATOM   983  O  O    . ALA A 1 78  ? 19.178 15.743  35.133 1.000 8.78  ? 78   ALA A O    1 
ATOM   984  C  CB   . ALA A 1 78  ? 17.227 18.024  34.338 1.000 8.02  ? 78   ALA A CB   1 
ATOM   985  H  H    . ALA A 1 78  ? 20.041 17.495  33.728 1.000 7.43  ? 78   ALA A H    1 
ATOM   986  H  HA   . ALA A 1 78  ? 18.616 18.785  35.653 1.000 7.96  ? 78   ALA A HA   1 
ATOM   987  H  HB1  . ALA A 1 78  ? 16.565 17.943  35.017 1.000 12.03 ? 78   ALA A HB1  1 
ATOM   988  H  HB2  . ALA A 1 78  ? 17.098 18.805  33.823 1.000 12.03 ? 78   ALA A HB2  1 
ATOM   989  N  N    . ALA A 1 79  ? 18.624 16.753  37.073 1.000 5.58  ? 79   ALA A N    1 
ATOM   990  C  CA   . ALA A 1 79  ? 18.800 15.586  37.913 1.000 5.44  ? 79   ALA A CA   1 
ATOM   991  C  C    . ALA A 1 79  ? 17.437 15.087  38.368 1.000 4.70  ? 79   ALA A C    1 
ATOM   992  O  O    . ALA A 1 79  ? 16.590 15.866  38.778 1.000 5.33  ? 79   ALA A O    1 
ATOM   993  C  CB   . ALA A 1 79  ? 19.605 15.945  39.149 1.000 6.56  ? 79   ALA A CB   1 
ATOM   994  H  H    . ALA A 1 79  ? 18.380 17.489  37.445 1.000 6.70  ? 79   ALA A H    1 
ATOM   995  H  HA   . ALA A 1 79  ? 19.260 14.882  37.411 1.000 6.53  ? 79   ALA A HA   1 
ATOM   996  H  HB2  . ALA A 1 79  ? 20.466 16.277  38.885 1.000 9.84  ? 79   ALA A HB2  1 
ATOM   997  H  HB3  . ALA A 1 79  ? 19.135 16.624  39.638 1.000 9.84  ? 79   ALA A HB3  1 
ATOM   998  N  N    . GLU A 1 80  ? 17.252 13.774  38.368 1.000 4.78  ? 80   GLU A N    1 
ATOM   999  C  CA   . GLU A 1 80  ? 16.113 13.209  39.064 1.000 4.94  ? 80   GLU A CA   1 
ATOM   1000 C  C    . GLU A 1 80  ? 16.222 13.504  40.558 1.000 4.85  ? 80   GLU A C    1 
ATOM   1001 O  O    . GLU A 1 80  ? 17.284 13.584  41.141 1.000 5.64  ? 80   GLU A O    1 
ATOM   1002 C  CB   . GLU A 1 80  ? 16.016 11.712  38.797 1.000 5.38  ? 80   GLU A CB   1 
ATOM   1003 C  CG   . GLU A 1 80  ? 15.589 11.345  37.412 1.000 6.06  ? 80   GLU A CG   1 
ATOM   1004 C  CD   . GLU A 1 80  ? 15.432 9.835   37.164 1.000 5.35  ? 80   GLU A CD   1 
ATOM   1005 O  OE1  . GLU A 1 80  ? 15.817 9.052   38.055 1.000 6.00  ? 80   GLU A OE1  1 
ATOM   1006 O  OE2  . GLU A 1 80  ? 14.948 9.499   36.087 1.000 7.00  ? 80   GLU A OE2  1 
ATOM   1007 H  H    . GLU A 1 80  ? 17.806 13.260  37.957 1.000 5.73  ? 80   GLU A H    1 
ATOM   1008 H  HA   . GLU A 1 80  ? 15.300 13.636  38.723 1.000 5.93  ? 80   GLU A HA   1 
ATOM   1009 H  HB3  . GLU A 1 80  ? 15.380 11.334  39.424 1.000 6.46  ? 80   GLU A HB3  1 
ATOM   1010 H  HG3  . GLU A 1 80  ? 16.240 11.700  36.786 1.000 7.27  ? 80   GLU A HG3  1 
ATOM   1011 N  N    . VAL A 1 81  ? 15.038 13.651  41.149 1.000 5.08  ? 81   VAL A N    1 
ATOM   1012 C  CA   . VAL A 1 81  ? 14.833 13.860  42.557 1.000 5.23  ? 81   VAL A CA   1 
ATOM   1013 C  C    . VAL A 1 81  ? 14.064 12.666  43.107 1.000 5.13  ? 81   VAL A C    1 
ATOM   1014 O  O    . VAL A 1 81  ? 13.074 12.256  42.472 1.000 5.77  ? 81   VAL A O    1 
ATOM   1015 C  CB   . VAL A 1 81  ? 14.039 15.157  42.802 1.000 5.69  ? 81   VAL A CB   1 
ATOM   1016 C  CG1  . VAL A 1 81  ? 13.785 15.390  44.278 1.000 6.61  ? 81   VAL A CG1  1 
ATOM   1017 C  CG2  . VAL A 1 81  ? 14.775 16.365  42.175 1.000 6.09  ? 81   VAL A CG2  1 
ATOM   1018 H  H    . VAL A 1 81  ? 14.339 13.619  40.649 1.000 6.09  ? 81   VAL A H    1 
ATOM   1019 H  HA   . VAL A 1 81  ? 15.701 13.921  43.006 1.000 6.27  ? 81   VAL A HA   1 
ATOM   1020 H  HB   . VAL A 1 81  ? 13.170 15.068  42.357 1.000 6.83  ? 81   VAL A HB   1 
ATOM   1021 H  HG11 . VAL A 1 81  ? 13.290 16.204  44.393 1.000 9.91  ? 81   VAL A HG11 1 
ATOM   1022 H  HG12 . VAL A 1 81  ? 13.281 14.656  44.636 1.000 9.91  ? 81   VAL A HG12 1 
ATOM   1023 H  HG13 . VAL A 1 81  ? 14.624 15.457  44.740 1.000 9.91  ? 81   VAL A HG13 1 
ATOM   1024 H  HG21 . VAL A 1 81  ? 14.930 16.185  41.244 1.000 9.14  ? 81   VAL A HG21 1 
ATOM   1025 H  HG23 . VAL A 1 81  ? 15.616 16.496  42.620 1.000 9.14  ? 81   VAL A HG23 1 
ATOM   1026 N  N    . TYR A 1 82  ? 14.489 12.134  44.231 1.000 5.68  ? 82   TYR A N    1 
ATOM   1027 C  CA   . TYR A 1 82  ? 13.844 10.991  44.877 1.000 5.58  ? 82   TYR A CA   1 
ATOM   1028 C  C    . TYR A 1 82  ? 13.301 11.413  46.214 1.000 5.69  ? 82   TYR A C    1 
ATOM   1029 O  O    . TYR A 1 82  ? 13.715 12.399  46.819 1.000 6.60  ? 82   TYR A O    1 
ATOM   1030 C  CB   . TYR A 1 82  ? 14.855 9.806   45.012 1.000 5.83  ? 82   TYR A CB   1 
ATOM   1031 C  CG   . TYR A 1 82  ? 15.545 9.516   43.703 1.000 5.51  ? 82   TYR A CG   1 
ATOM   1032 C  CD1  . TYR A 1 82  ? 14.858 9.023   42.624 1.000 5.51  ? 82   TYR A CD1  1 
ATOM   1033 C  CD2  . TYR A 1 82  ? 16.902 9.790   43.535 1.000 5.71  ? 82   TYR A CD2  1 
ATOM   1034 C  CE1  . TYR A 1 82  ? 15.473 8.783   41.408 1.000 5.61  ? 82   TYR A CE1  1 
ATOM   1035 C  CE2  . TYR A 1 82  ? 17.513 9.579   42.313 1.000 5.97  ? 82   TYR A CE2  1 
ATOM   1036 C  CZ   . TYR A 1 82  ? 16.829 9.073   41.245 1.000 5.49  ? 82   TYR A CZ   1 
ATOM   1037 O  OH   . TYR A 1 82  ? 17.469 8.871   40.054 1.000 5.60  ? 82   TYR A OH   1 
ATOM   1038 H  H    . TYR A 1 82  ? 15.183 12.475  44.606 1.000 6.81  ? 82   TYR A H    1 
ATOM   1039 H  HA   . TYR A 1 82  ? 13.096 10.698  44.316 1.000 6.69  ? 82   TYR A HA   1 
ATOM   1040 H  HB3  . TYR A 1 82  ? 14.386 9.010   45.306 1.000 7.00  ? 82   TYR A HB3  1 
ATOM   1041 H  HD2  . TYR A 1 82  ? 17.399 10.117  44.250 1.000 6.86  ? 82   TYR A HD2  1 
ATOM   1042 H  HE1  . TYR A 1 82  ? 14.985 8.430   40.700 1.000 6.74  ? 82   TYR A HE1  1 
ATOM   1043 N  N    . GLU A 1 83  ? 12.392 10.612  46.756 1.000 6.07  ? 83   GLU A N    1 
ATOM   1044 C  CA   . GLU A 1 83  ? 11.891 10.806  48.097 1.000 6.21  ? 83   GLU A CA   1 
ATOM   1045 C  C    . GLU A 1 83  ? 13.019 10.648  49.080 1.000 6.90  ? 83   GLU A C    1 
ATOM   1046 O  O    . GLU A 1 83  ? 13.927 9.796   48.896 1.000 7.94  ? 83   GLU A O    1 
ATOM   1047 C  CB   A GLU A 1 83  ? 10.731 9.830   48.342 0.561 8.37  ? 83   GLU A CB   1 
ATOM   1048 C  CB   B GLU A 1 83  ? 10.823 9.779   48.422 0.439 7.09  ? 83   GLU A CB   1 
ATOM   1049 C  CG   A GLU A 1 83  ? 9.971  10.085  49.620 0.561 8.55  ? 83   GLU A CG   1 
ATOM   1050 C  CG   B GLU A 1 83  ? 9.555  9.919   47.601 0.439 10.44 ? 83   GLU A CG   1 
ATOM   1051 C  CD   A GLU A 1 83  ? 8.811  9.133   49.836 0.561 13.79 ? 83   GLU A CD   1 
ATOM   1052 C  CD   B GLU A 1 83  ? 8.632  8.823   48.144 0.439 13.81 ? 83   GLU A CD   1 
ATOM   1053 O  OE1  A GLU A 1 83  ? 8.400  8.402   48.921 0.561 15.96 ? 83   GLU A OE1  1 
ATOM   1054 O  OE1  B GLU A 1 83  ? 8.111  8.062   47.296 0.439 32.15 ? 83   GLU A OE1  1 
ATOM   1055 O  OE2  A GLU A 1 83  ? 8.266  9.140   50.950 0.561 17.80 ? 83   GLU A OE2  1 
ATOM   1056 O  OE2  B GLU A 1 83  ? 8.483  8.633   49.357 0.439 22.93 ? 83   GLU A OE2  1 
ATOM   1057 H  H    . GLU A 1 83  ? 12.090 9.954   46.292 1.000 7.29  ? 83   GLU A H    1 
ATOM   1058 H  HA   A GLU A 1 83  ? 11.545 11.720  48.168 1.000 7.46  ? 83   GLU A HA   1 
ATOM   1059 H  HB2  A GLU A 1 83  ? 10.114 9.886   47.596 0.561 10.05 ? 83   GLU A HB2  1 
ATOM   1060 H  HB2  B GLU A 1 83  ? 11.190 8.893   48.279 0.439 8.51  ? 83   GLU A HB2  1 
ATOM   1061 H  HB3  A GLU A 1 83  ? 11.084 8.927   48.364 0.561 10.05 ? 83   GLU A HB3  1 
ATOM   1062 H  HB3  B GLU A 1 83  ? 10.595 9.854   49.362 0.439 8.51  ? 83   GLU A HB3  1 
ATOM   1063 N  N    . HIS A 1 84  ? 12.968 11.392  50.173 1.000 7.29  ? 84   HIS A N    1 
ATOM   1064 C  CA   . HIS A 1 84  ? 13.882 11.250  51.280 1.000 7.87  ? 84   HIS A CA   1 
ATOM   1065 C  C    . HIS A 1 84  ? 13.114 11.535  52.563 1.000 8.04  ? 84   HIS A C    1 
ATOM   1066 O  O    . HIS A 1 84  ? 12.134 12.305  52.525 1.000 8.64  ? 84   HIS A O    1 
ATOM   1067 C  CB   . HIS A 1 84  ? 15.047 12.233  51.099 1.000 7.83  ? 84   HIS A CB   1 
ATOM   1068 C  CG   . HIS A 1 84  ? 16.176 11.998  52.058 1.000 8.38  ? 84   HIS A CG   1 
ATOM   1069 N  ND1  . HIS A 1 84  ? 16.172 12.497  53.355 1.000 10.03 ? 84   HIS A ND1  1 
ATOM   1070 C  CD2  . HIS A 1 84  ? 17.324 11.250  51.862 1.000 9.78  ? 84   HIS A CD2  1 
ATOM   1071 C  CE1  . HIS A 1 84  ? 17.296 12.072  53.907 1.000 10.78 ? 84   HIS A CE1  1 
ATOM   1072 N  NE2  . HIS A 1 84  ? 18.008 11.336  53.074 1.000 11.60 ? 84   HIS A NE2  1 
ATOM   1073 H  H    . HIS A 1 84  ? 12.356 11.994  50.227 1.000 8.75  ? 84   HIS A H    1 
ATOM   1074 H  HB2  . HIS A 1 84  ? 15.384 12.158  50.193 1.000 9.39  ? 84   HIS A HB2  1 
ATOM   1075 H  HB3  . HIS A 1 84  ? 14.717 13.138  51.218 1.000 9.39  ? 84   HIS A HB3  1 
ATOM   1076 N  N    . THR A 1 85  ? 13.558 10.983  53.687 1.000 9.25  ? 85   THR A N    1 
ATOM   1077 C  CA   . THR A 1 85  ? 12.907 11.279  54.938 1.000 11.53 ? 85   THR A CA   1 
ATOM   1078 C  C    . THR A 1 85  ? 12.914 12.749  55.285 1.000 10.25 ? 85   THR A C    1 
ATOM   1079 O  O    . THR A 1 85  ? 12.002 13.211  55.991 1.000 13.04 ? 85   THR A O    1 
ATOM   1080 C  CB   . THR A 1 85  ? 13.553 10.438  56.073 1.000 14.74 ? 85   THR A CB   1 
ATOM   1081 O  OG1  . THR A 1 85  ? 14.935 10.583  56.053 1.000 17.46 ? 85   THR A OG1  1 
ATOM   1082 C  CG2  . THR A 1 85  ? 13.278 8.991   55.835 1.000 22.90 ? 85   THR A CG2  1 
ATOM   1083 N  N    . GLU A 1 86  ? 13.860 13.528  54.809 1.000 8.74  ? 86   GLU A N    1 
ATOM   1084 C  CA   A GLU A 1 86  ? 13.868 14.940  55.026 0.561 10.02 ? 86   GLU A CA   1 
ATOM   1085 C  CA   B GLU A 1 86  ? 13.824 14.945  55.101 0.439 8.75  ? 86   GLU A CA   1 
ATOM   1086 C  C    . GLU A 1 86  ? 13.052 15.706  54.018 1.000 8.00  ? 86   GLU A C    1 
ATOM   1087 O  O    . GLU A 1 86  ? 12.864 16.924  54.219 1.000 10.32 ? 86   GLU A O    1 
ATOM   1088 C  CB   A GLU A 1 86  ? 15.330 15.433  54.930 0.561 13.64 ? 86   GLU A CB   1 
ATOM   1089 C  CB   B GLU A 1 86  ? 15.220 15.506  55.288 0.439 11.39 ? 86   GLU A CB   1 
ATOM   1090 C  CG   A GLU A 1 86  ? 16.050 14.858  56.142 0.561 14.36 ? 86   GLU A CG   1 
ATOM   1091 C  CG   B GLU A 1 86  ? 16.021 15.896  54.076 0.439 14.79 ? 86   GLU A CG   1 
ATOM   1092 C  CD   A GLU A 1 86  ? 17.517 15.094  56.254 0.561 14.93 ? 86   GLU A CD   1 
ATOM   1093 C  CD   B GLU A 1 86  ? 17.358 16.530  54.408 0.439 19.41 ? 86   GLU A CD   1 
ATOM   1094 O  OE1  A GLU A 1 86  ? 18.039 16.177  55.953 0.561 24.20 ? 86   GLU A OE1  1 
ATOM   1095 O  OE1  B GLU A 1 86  ? 17.897 17.255  53.542 0.439 13.62 ? 86   GLU A OE1  1 
ATOM   1096 O  OE2  A GLU A 1 86  ? 18.247 14.178  56.697 0.561 21.76 ? 86   GLU A OE2  1 
ATOM   1097 O  OE2  B GLU A 1 86  ? 17.877 16.293  55.528 0.439 27.00 ? 86   GLU A OE2  1 
ATOM   1098 H  H    A GLU A 1 86  ? 14.497 13.175  54.352 1.000 10.49 ? 86   GLU A H    1 
ATOM   1099 N  N    . GLY A 1 87  ? 12.588 15.067  52.979 1.000 7.84  ? 87   GLY A N    1 
ATOM   1100 C  CA   . GLY A 1 87  ? 11.808 15.671  51.905 1.000 8.11  ? 87   GLY A CA   1 
ATOM   1101 C  C    . GLY A 1 87  ? 12.194 15.078  50.585 1.000 7.23  ? 87   GLY A C    1 
ATOM   1102 O  O    . GLY A 1 87  ? 11.490 14.265  49.980 1.000 8.87  ? 87   GLY A O    1 
ATOM   1103 H  HA3  . GLY A 1 87  ? 11.977 16.626  51.885 1.000 9.73  ? 87   GLY A HA3  1 
ATOM   1104 N  N    . SER A 1 88  ? 13.372 15.470  50.099 1.000 6.79  ? 88   SER A N    1 
ATOM   1105 C  CA   . SER A 1 88  ? 13.806 15.061  48.773 1.000 6.67  ? 88   SER A CA   1 
ATOM   1106 C  C    . SER A 1 88  ? 15.342 14.991  48.717 1.000 6.67  ? 88   SER A C    1 
ATOM   1107 O  O    . SER A 1 88  ? 16.031 15.534  49.567 1.000 8.16  ? 88   SER A O    1 
ATOM   1108 C  CB   . SER A 1 88  ? 13.269 16.004  47.718 1.000 8.07  ? 88   SER A CB   1 
ATOM   1109 O  OG   . SER A 1 88  ? 13.888 17.269  47.736 1.000 9.82  ? 88   SER A OG   1 
ATOM   1110 H  H    . SER A 1 88  ? 13.882 15.972  50.576 1.000 8.14  ? 88   SER A H    1 
ATOM   1111 H  HA   . SER A 1 88  ? 13.450 14.165  48.595 1.000 8.00  ? 88   SER A HA   1 
ATOM   1112 H  HB2  . SER A 1 88  ? 13.389 15.606  46.842 1.000 9.69  ? 88   SER A HB2  1 
ATOM   1113 H  HG   . SER A 1 88  ? 13.547 17.732  48.320 1.000 14.73 ? 88   SER A HG   1 
ATOM   1114 N  N    . THR A 1 89  ? 15.829 14.288  47.677 1.000 7.16  ? 89   THR A N    1 
ATOM   1115 C  CA   . THR A 1 89  ? 17.274 14.140  47.469 1.000 7.05  ? 89   THR A CA   1 
ATOM   1116 C  C    . THR A 1 89  ? 17.556 13.919  46.009 1.000 6.21  ? 89   THR A C    1 
ATOM   1117 O  O    . THR A 1 89  ? 16.759 13.380  45.293 1.000 8.41  ? 89   THR A O    1 
ATOM   1118 C  CB   . THR A 1 89  ? 17.726 12.898  48.314 1.000 8.25  ? 89   THR A CB   1 
ATOM   1119 O  OG1  . THR A 1 89  ? 19.126 12.733  48.192 1.000 10.34 ? 89   THR A OG1  1 
ATOM   1120 C  CG2  . THR A 1 89  ? 17.062 11.597  47.896 1.000 8.95  ? 89   THR A CG2  1 
ATOM   1121 H  HA   . THR A 1 89  ? 17.740 14.943  47.781 1.000 8.46  ? 89   THR A HA   1 
ATOM   1122 H  HB   . THR A 1 89  ? 17.513 13.068  49.256 1.000 9.90  ? 89   THR A HB   1 
ATOM   1123 H  HG1  . THR A 1 89  ? 19.504 13.427  48.411 1.000 15.51 ? 89   THR A HG1  1 
ATOM   1124 H  HG22 . THR A 1 89  ? 17.287 11.407  46.983 1.000 13.43 ? 89   THR A HG22 1 
ATOM   1125 H  HG23 . THR A 1 89  ? 17.372 10.883  48.458 1.000 13.43 ? 89   THR A HG23 1 
ATOM   1126 N  N    . THR A 1 90  ? 18.758 14.273  45.578 1.000 6.68  ? 90   THR A N    1 
ATOM   1127 C  CA   . THR A 1 90  ? 19.254 13.997  44.241 1.000 6.45  ? 90   THR A CA   1 
ATOM   1128 C  C    . THR A 1 90  ? 20.343 12.918  44.229 1.000 6.36  ? 90   THR A C    1 
ATOM   1129 O  O    . THR A 1 90  ? 21.224 12.917  43.373 1.000 7.11  ? 90   THR A O    1 
ATOM   1130 C  CB   . THR A 1 90  ? 19.726 15.267  43.530 1.000 7.43  ? 90   THR A CB   1 
ATOM   1131 O  OG1  . THR A 1 90  ? 20.716 15.901  44.371 1.000 9.43  ? 90   THR A OG1  1 
ATOM   1132 C  CG2  . THR A 1 90  ? 18.564 16.225  43.270 1.000 8.68  ? 90   THR A CG2  1 
ATOM   1133 H  H    . THR A 1 90  ? 19.275 14.691  46.123 1.000 8.01  ? 90   THR A H    1 
ATOM   1134 H  HA   . THR A 1 90  ? 18.499 13.646  43.724 1.000 7.74  ? 90   THR A HA   1 
ATOM   1135 H  HB   . THR A 1 90  ? 20.139 15.023  42.675 1.000 8.92  ? 90   THR A HB   1 
ATOM   1136 H  HG22 . THR A 1 90  ? 18.162 16.471  44.106 1.000 13.02 ? 90   THR A HG22 1 
ATOM   1137 H  HG23 . THR A 1 90  ? 18.901 17.011  42.833 1.000 13.02 ? 90   THR A HG23 1 
ATOM   1138 N  N    . SER A 1 91  ? 20.279 11.990  45.156 1.000 8.16  ? 91   SER A N    1 
ATOM   1139 C  CA   A SER A 1 91  ? 21.128 10.798  45.143 0.823 7.35  ? 91   SER A CA   1 
ATOM   1140 C  CA   B SER A 1 91  ? 21.132 10.832  45.293 0.177 7.79  ? 91   SER A CA   1 
ATOM   1141 C  C    . SER A 1 91  ? 20.303 9.594   45.613 1.000 6.77  ? 91   SER A C    1 
ATOM   1142 O  O    . SER A 1 91  ? 19.191 9.745   46.138 1.000 8.12  ? 91   SER A O    1 
ATOM   1143 C  CB   A SER A 1 91  ? 22.361 11.006  45.996 0.823 8.74  ? 91   SER A CB   1 
ATOM   1144 C  CB   B SER A 1 91  ? 22.141 11.028  46.426 0.177 8.41  ? 91   SER A CB   1 
ATOM   1145 O  OG   A SER A 1 91  ? 21.937 11.310  47.307 0.823 11.82 ? 91   SER A OG   1 
ATOM   1146 O  OG   B SER A 1 91  ? 23.065 12.039  46.049 0.177 9.63  ? 91   SER A OG   1 
ATOM   1147 H  H    A SER A 1 91  ? 19.714 12.087  45.798 1.000 9.79  ? 91   SER A H    1 
ATOM   1148 N  N    . TYR A 1 92  ? 20.845 8.433   45.381 1.000 6.23  ? 92   TYR A N    1 
ATOM   1149 C  CA   . TYR A 1 92  ? 20.178 7.178   45.793 1.000 6.07  ? 92   TYR A CA   1 
ATOM   1150 C  C    . TYR A 1 92  ? 21.222 6.201   46.281 1.000 6.22  ? 92   TYR A C    1 
ATOM   1151 O  O    . TYR A 1 92  ? 22.439 6.413   46.121 1.000 9.03  ? 92   TYR A O    1 
ATOM   1152 C  CB   . TYR A 1 92  ? 19.344 6.601   44.665 1.000 5.71  ? 92   TYR A CB   1 
ATOM   1153 C  CG   . TYR A 1 92  ? 20.012 6.251   43.383 1.000 5.24  ? 92   TYR A CG   1 
ATOM   1154 C  CD1  . TYR A 1 92  ? 20.281 7.202   42.430 1.000 5.92  ? 92   TYR A CD1  1 
ATOM   1155 C  CD2  . TYR A 1 92  ? 20.360 4.931   43.065 1.000 5.21  ? 92   TYR A CD2  1 
ATOM   1156 C  CE1  . TYR A 1 92  ? 20.884 6.891   41.215 1.000 5.62  ? 92   TYR A CE1  1 
ATOM   1157 C  CE2  . TYR A 1 92  ? 20.928 4.604   41.837 1.000 5.14  ? 92   TYR A CE2  1 
ATOM   1158 C  CZ   . TYR A 1 92  ? 21.181 5.592   40.891 1.000 4.95  ? 92   TYR A CZ   1 
ATOM   1159 O  OH   . TYR A 1 92  ? 21.724 5.295   39.697 1.000 5.26  ? 92   TYR A OH   1 
ATOM   1160 H  HA   . TYR A 1 92  ? 19.579 7.383   46.541 1.000 7.29  ? 92   TYR A HA   1 
ATOM   1161 H  HB2  . TYR A 1 92  ? 18.914 5.798   45.000 1.000 6.85  ? 92   TYR A HB2  1 
ATOM   1162 H  HB3  . TYR A 1 92  ? 18.640 7.238   44.465 1.000 6.85  ? 92   TYR A HB3  1 
ATOM   1163 H  HD1  . TYR A 1 92  ? 20.053 8.087   42.603 1.000 7.11  ? 92   TYR A HD1  1 
ATOM   1164 H  HD2  . TYR A 1 92  ? 20.208 4.259   43.689 1.000 6.25  ? 92   TYR A HD2  1 
ATOM   1165 H  HE1  . TYR A 1 92  ? 21.088 7.572   40.615 1.000 6.74  ? 92   TYR A HE1  1 
ATOM   1166 H  HE2  . TYR A 1 92  ? 21.139 3.718   41.647 1.000 6.17  ? 92   TYR A HE2  1 
ATOM   1167 N  N    . TYR A 1 93  ? 20.754 5.111   46.892 1.000 5.86  ? 93   TYR A N    1 
ATOM   1168 C  CA   . TYR A 1 93  ? 21.631 4.138   47.481 1.000 6.14  ? 93   TYR A CA   1 
ATOM   1169 C  C    . TYR A 1 93  ? 21.617 2.841   46.684 1.000 5.95  ? 93   TYR A C    1 
ATOM   1170 O  O    . TYR A 1 93  ? 20.574 2.308   46.341 1.000 6.70  ? 93   TYR A O    1 
ATOM   1171 C  CB   . TYR A 1 93  ? 21.184 3.816   48.900 1.000 7.35  ? 93   TYR A CB   1 
ATOM   1172 C  CG   . TYR A 1 93  ? 21.344 4.953   49.879 1.000 8.46  ? 93   TYR A CG   1 
ATOM   1173 C  CD1  . TYR A 1 93  ? 22.527 5.113   50.569 1.000 11.23 ? 93   TYR A CD1  1 
ATOM   1174 C  CD2  . TYR A 1 93  ? 20.295 5.822   50.160 1.000 9.37  ? 93   TYR A CD2  1 
ATOM   1175 C  CE1  . TYR A 1 93  ? 22.689 6.128   51.501 1.000 13.18 ? 93   TYR A CE1  1 
ATOM   1176 C  CE2  . TYR A 1 93  ? 20.459 6.803   51.096 1.000 11.18 ? 93   TYR A CE2  1 
ATOM   1177 C  CZ   . TYR A 1 93  ? 21.628 6.964   51.756 1.000 12.27 ? 93   TYR A CZ   1 
ATOM   1178 O  OH   . TYR A 1 93  ? 21.837 7.948   52.693 1.000 15.50 ? 93   TYR A OH   1 
ATOM   1179 H  H    . TYR A 1 93  ? 19.903 4.988   46.934 1.000 7.04  ? 93   TYR A H    1 
ATOM   1180 H  HA   . TYR A 1 93  ? 22.543 4.495   47.502 1.000 7.37  ? 93   TYR A HA   1 
ATOM   1181 H  HB2  . TYR A 1 93  ? 20.250 3.554   48.879 1.000 8.82  ? 93   TYR A HB2  1 
ATOM   1182 H  HB3  . TYR A 1 93  ? 21.694 3.057   49.221 1.000 8.82  ? 93   TYR A HB3  1 
ATOM   1183 H  HD2  . TYR A 1 93  ? 19.484 5.734   49.712 1.000 11.25 ? 93   TYR A HD2  1 
ATOM   1184 H  HE2  . TYR A 1 93  ? 19.749 7.375   51.284 1.000 13.41 ? 93   TYR A HE2  1 
ATOM   1185 N  N    . ALA A 1 94  ? 22.839 2.328   46.432 1.000 6.01  ? 94   ALA A N    1 
ATOM   1186 C  CA   . ALA A 1 94  ? 23.067 1.028   45.856 1.000 5.78  ? 94   ALA A CA   1 
ATOM   1187 C  C    . ALA A 1 94  ? 23.009 -0.023  46.977 1.000 5.33  ? 94   ALA A C    1 
ATOM   1188 O  O    . ALA A 1 94  ? 23.701 0.110   47.982 1.000 6.56  ? 94   ALA A O    1 
ATOM   1189 C  CB   . ALA A 1 94  ? 24.412 0.985   45.198 1.000 6.76  ? 94   ALA A CB   1 
ATOM   1190 H  H    . ALA A 1 94  ? 23.526 2.808   46.629 1.000 7.21  ? 94   ALA A H    1 
ATOM   1191 H  HA   . ALA A 1 94  ? 22.371 0.838   45.192 1.000 6.93  ? 94   ALA A HA   1 
ATOM   1192 H  HB1  . ALA A 1 94  ? 24.554 0.116   44.817 1.000 10.15 ? 94   ALA A HB1  1 
ATOM   1193 H  HB2  . ALA A 1 94  ? 24.450 1.649   44.505 1.000 10.15 ? 94   ALA A HB2  1 
ATOM   1194 H  HB3  . ALA A 1 94  ? 25.093 1.164   45.850 1.000 10.15 ? 94   ALA A HB3  1 
ATOM   1195 N  N    . VAL A 1 95  ? 22.214 -1.057  46.769 1.000 5.39  ? 95   VAL A N    1 
ATOM   1196 C  CA   . VAL A 1 95  ? 22.063 -2.140  47.756 1.000 5.54  ? 95   VAL A CA   1 
ATOM   1197 C  C    . VAL A 1 95  ? 22.161 -3.471  47.015 1.000 5.70  ? 95   VAL A C    1 
ATOM   1198 O  O    . VAL A 1 95  ? 21.982 -3.590  45.796 1.000 7.37  ? 95   VAL A O    1 
ATOM   1199 C  CB   . VAL A 1 95  ? 20.730 -2.043  48.510 1.000 6.14  ? 95   VAL A CB   1 
ATOM   1200 C  CG1  . VAL A 1 95  ? 20.628 -0.790  49.343 1.000 7.01  ? 95   VAL A CG1  1 
ATOM   1201 C  CG2  . VAL A 1 95  ? 19.527 -2.154  47.603 1.000 7.35  ? 95   VAL A CG2  1 
ATOM   1202 H  H    . VAL A 1 95  ? 21.770 -1.099  46.034 1.000 6.47  ? 95   VAL A H    1 
ATOM   1203 H  HA   . VAL A 1 95  ? 22.797 -2.082  48.403 1.000 6.65  ? 95   VAL A HA   1 
ATOM   1204 H  HB   . VAL A 1 95  ? 20.694 -2.803  49.128 1.000 7.37  ? 95   VAL A HB   1 
ATOM   1205 H  HG11 . VAL A 1 95  ? 21.395 -0.725  49.917 1.000 10.52 ? 95   VAL A HG11 1 
ATOM   1206 H  HG12 . VAL A 1 95  ? 20.594 -0.024  48.766 1.000 10.52 ? 95   VAL A HG12 1 
ATOM   1207 H  HG13 . VAL A 1 95  ? 19.831 -0.824  49.876 1.000 10.52 ? 95   VAL A HG13 1 
ATOM   1208 N  N    . ALA A 1 96  ? 22.478 -4.507  47.802 1.000 5.77  ? 96   ALA A N    1 
ATOM   1209 C  CA   . ALA A 1 96  ? 22.545 -5.876  47.324 1.000 5.68  ? 96   ALA A CA   1 
ATOM   1210 C  C    . ALA A 1 96  ? 21.431 -6.659  47.978 1.000 5.61  ? 96   ALA A C    1 
ATOM   1211 O  O    . ALA A 1 96  ? 21.487 -6.916  49.182 1.000 6.96  ? 96   ALA A O    1 
ATOM   1212 C  CB   . ALA A 1 96  ? 23.925 -6.456  47.650 1.000 6.45  ? 96   ALA A CB   1 
ATOM   1213 H  H    . ALA A 1 96  ? 22.651 -4.354  48.630 1.000 6.93  ? 96   ALA A H    1 
ATOM   1214 H  HA   . ALA A 1 96  ? 22.415 -5.883  46.353 1.000 6.82  ? 96   ALA A HA   1 
ATOM   1215 H  HB1  . ALA A 1 96  ? 23.974 -7.362  47.336 1.000 9.68  ? 96   ALA A HB1  1 
ATOM   1216 H  HB2  . ALA A 1 96  ? 24.603 -5.931  47.219 1.000 9.68  ? 96   ALA A HB2  1 
ATOM   1217 H  HB3  . ALA A 1 96  ? 24.063 -6.439  48.600 1.000 9.68  ? 96   ALA A HB3  1 
ATOM   1218 N  N    . VAL A 1 97  ? 20.405 -6.980  47.191 1.000 5.81  ? 97   VAL A N    1 
ATOM   1219 C  CA   . VAL A 1 97  ? 19.215 -7.649  47.717 1.000 5.86  ? 97   VAL A CA   1 
ATOM   1220 C  C    . VAL A 1 97  ? 19.360 -9.143  47.565 1.000 5.78  ? 97   VAL A C    1 
ATOM   1221 O  O    . VAL A 1 97  ? 19.770 -9.647  46.514 1.000 6.10  ? 97   VAL A O    1 
ATOM   1222 C  CB   . VAL A 1 97  ? 17.943 -7.152  46.974 1.000 6.47  ? 97   VAL A CB   1 
ATOM   1223 C  CG1  . VAL A 1 97  ? 16.681 -7.811  47.488 1.000 7.30  ? 97   VAL A CG1  1 
ATOM   1224 C  CG2  . VAL A 1 97  ? 17.824 -5.624  47.092 1.000 7.02  ? 97   VAL A CG2  1 
ATOM   1225 H  HA   . VAL A 1 97  ? 19.128 -7.435  48.670 1.000 7.03  ? 97   VAL A HA   1 
ATOM   1226 H  HB   . VAL A 1 97  ? 18.038 -7.377  46.025 1.000 7.76  ? 97   VAL A HB   1 
ATOM   1227 H  HG11 . VAL A 1 97  ? 16.763 -8.764  47.411 1.000 10.94 ? 97   VAL A HG11 1 
ATOM   1228 H  HG12 . VAL A 1 97  ? 16.549 -7.574  48.409 1.000 10.94 ? 97   VAL A HG12 1 
ATOM   1229 H  HG13 . VAL A 1 97  ? 15.930 -7.511  46.970 1.000 10.94 ? 97   VAL A HG13 1 
ATOM   1230 H  HG21 . VAL A 1 97  ? 18.625 -5.220  46.750 1.000 10.53 ? 97   VAL A HG21 1 
ATOM   1231 H  HG22 . VAL A 1 97  ? 17.068 -5.310  46.589 1.000 10.53 ? 97   VAL A HG22 1 
ATOM   1232 N  N    . VAL A 1 98  ? 18.984 -9.849  48.626 1.000 6.07  ? 98   VAL A N    1 
ATOM   1233 C  CA   . VAL A 1 98  ? 18.980 -11.292 48.705 1.000 6.75  ? 98   VAL A CA   1 
ATOM   1234 C  C    . VAL A 1 98  ? 17.666 -11.741 49.308 1.000 7.00  ? 98   VAL A C    1 
ATOM   1235 O  O    . VAL A 1 98  ? 16.872 -10.945 49.842 1.000 7.69  ? 98   VAL A O    1 
ATOM   1236 C  CB   . VAL A 1 98  ? 20.186 -11.787 49.531 1.000 7.04  ? 98   VAL A CB   1 
ATOM   1237 C  CG1  . VAL A 1 98  ? 21.484 -11.529 48.794 1.000 7.33  ? 98   VAL A CG1  1 
ATOM   1238 C  CG2  . VAL A 1 98  ? 20.236 -11.158 50.896 1.000 8.21  ? 98   VAL A CG2  1 
ATOM   1239 H  H    . VAL A 1 98  ? 18.721 -9.413  49.319 1.000 7.29  ? 98   VAL A H    1 
ATOM   1240 H  HG11 . VAL A 1 98  ? 21.444 -11.933 47.924 1.000 10.99 ? 98   VAL A HG11 1 
ATOM   1241 H  HG12 . VAL A 1 98  ? 21.617 -10.583 48.701 1.000 10.99 ? 98   VAL A HG12 1 
ATOM   1242 H  HG13 . VAL A 1 98  ? 22.214 -11.908 49.289 1.000 10.99 ? 98   VAL A HG13 1 
ATOM   1243 H  HG21 . VAL A 1 98  ? 20.363 -10.212 50.800 1.000 12.31 ? 98   VAL A HG21 1 
ATOM   1244 N  N    A LYS A 1 99  ? 17.362 -13.033 49.190 0.623 7.87  ? 99   LYS A N    1 
ATOM   1245 N  N    B LYS A 1 99  ? 17.369 -13.035 49.229 0.377 7.83  ? 99   LYS A N    1 
ATOM   1246 C  CA   A LYS A 1 99  ? 16.175 -13.568 49.839 0.623 8.14  ? 99   LYS A CA   1 
ATOM   1247 C  CA   B LYS A 1 99  ? 16.213 -13.604 49.899 0.377 8.32  ? 99   LYS A CA   1 
ATOM   1248 C  C    A LYS A 1 99  ? 16.432 -13.864 51.304 0.623 9.62  ? 99   LYS A C    1 
ATOM   1249 C  C    B LYS A 1 99  ? 16.520 -14.040 51.330 0.377 9.64  ? 99   LYS A C    1 
ATOM   1250 O  O    A LYS A 1 99  ? 17.494 -14.366 51.686 0.623 12.09 ? 99   LYS A O    1 
ATOM   1251 O  O    B LYS A 1 99  ? 17.640 -14.454 51.646 0.377 12.91 ? 99   LYS A O    1 
ATOM   1252 C  CB   A LYS A 1 99  ? 15.727 -14.860 49.138 0.623 8.33  ? 99   LYS A CB   1 
ATOM   1253 C  CB   B LYS A 1 99  ? 15.715 -14.845 49.141 0.377 8.41  ? 99   LYS A CB   1 
ATOM   1254 C  CG   A LYS A 1 99  ? 15.159 -14.528 47.781 0.623 9.94  ? 99   LYS A CG   1 
ATOM   1255 C  CG   B LYS A 1 99  ? 15.174 -14.513 47.773 0.377 10.10 ? 99   LYS A CG   1 
ATOM   1256 C  CD   A LYS A 1 99  ? 14.533 -15.722 47.098 0.623 11.28 ? 99   LYS A CD   1 
ATOM   1257 C  CD   B LYS A 1 99  ? 14.549 -15.716 47.094 0.377 11.75 ? 99   LYS A CD   1 
ATOM   1258 C  CE   A LYS A 1 99  ? 13.875 -15.241 45.800 0.623 15.94 ? 99   LYS A CE   1 
ATOM   1259 C  CE   B LYS A 1 99  ? 13.861 -15.259 45.807 0.377 15.27 ? 99   LYS A CE   1 
ATOM   1260 N  NZ   A LYS A 1 99  ? 13.138 -16.402 45.186 0.623 17.25 ? 99   LYS A NZ   1 
ATOM   1261 N  NZ   B LYS A 1 99  ? 13.187 -16.422 45.146 0.377 17.83 ? 99   LYS A NZ   1 
ATOM   1262 H  H    A LYS A 1 99  ? 17.869 -13.553 48.729 0.623 9.44  ? 99   LYS A H    1 
ATOM   1263 H  H    B LYS A 1 99  ? 17.877 -13.551 48.766 0.377 9.40  ? 99   LYS A H    1 
ATOM   1264 H  HA   A LYS A 1 99  ? 15.454 -12.907 49.773 0.623 9.77  ? 99   LYS A HA   1 
ATOM   1265 H  HA   B LYS A 1 99  ? 15.496 -12.935 49.918 0.377 9.98  ? 99   LYS A HA   1 
ATOM   1266 H  HB2  A LYS A 1 99  ? 16.484 -15.459 49.039 0.623 10.00 ? 99   LYS A HB2  1 
ATOM   1267 H  HB2  B LYS A 1 99  ? 16.448 -15.474 49.048 0.377 10.09 ? 99   LYS A HB2  1 
ATOM   1268 H  HB3  A LYS A 1 99  ? 15.054 -15.308 49.675 0.623 10.00 ? 99   LYS A HB3  1 
ATOM   1269 H  HB3  B LYS A 1 99  ? 15.019 -15.275 49.662 0.377 10.09 ? 99   LYS A HB3  1 
ATOM   1270 H  HG2  A LYS A 1 99  ? 14.506 -13.842 47.845 0.623 11.93 ? 99   LYS A HG2  1 
ATOM   1271 H  HG2  B LYS A 1 99  ? 14.522 -13.825 47.833 0.377 12.12 ? 99   LYS A HG2  1 
ATOM   1272 H  HD3  A LYS A 1 99  ? 13.848 -16.039 47.689 0.623 13.54 ? 99   LYS A HD3  1 
ATOM   1273 H  HD3  B LYS A 1 99  ? 13.864 -16.034 47.685 0.377 14.10 ? 99   LYS A HD3  1 
ATOM   1274 N  N    A LYS A 1 100 ? 15.343 -13.467 52.031 0.623 9.67  ? 100  LYS A N    1 
ATOM   1275 N  N    B LYS A 1 100 ? 15.635 -14.007 52.339 0.377 9.57  ? 100  LYS A N    1 
ATOM   1276 C  CA   A LYS A 1 100 ? 15.434 -13.691 53.486 0.623 9.22  ? 100  LYS A CA   1 
ATOM   1277 C  CA   B LYS A 1 100 ? 15.912 -14.618 53.630 0.377 9.70  ? 100  LYS A CA   1 
ATOM   1278 C  C    A LYS A 1 100 ? 15.649 -15.168 53.745 0.623 10.15 ? 100  LYS A C    1 
ATOM   1279 C  C    B LYS A 1 100 ? 16.041 -16.145 53.523 0.377 13.91 ? 100  LYS A C    1 
ATOM   1280 O  O    A LYS A 1 100 ? 15.034 -16.072 53.180 0.623 12.53 ? 100  LYS A O    1 
ATOM   1281 O  O    B LYS A 1 100 ? 15.345 -16.752 52.696 0.377 13.19 ? 100  LYS A O    1 
ATOM   1282 C  CB   A LYS A 1 100 ? 14.188 -13.188 54.169 0.623 10.47 ? 100  LYS A CB   1 
ATOM   1283 C  CB   B LYS A 1 100 ? 14.820 -14.275 54.623 0.377 9.86  ? 100  LYS A CB   1 
ATOM   1284 C  CG   A LYS A 1 100 ? 14.260 -13.552 55.684 0.623 12.97 ? 100  LYS A CG   1 
ATOM   1285 C  CG   B LYS A 1 100 ? 14.911 -12.828 55.093 0.377 10.10 ? 100  LYS A CG   1 
ATOM   1286 C  CD   A LYS A 1 100 ? 13.171 -12.888 56.468 0.623 10.65 ? 100  LYS A CD   1 
ATOM   1287 C  CD   B LYS A 1 100 ? 13.972 -12.536 56.214 0.377 9.46  ? 100  LYS A CD   1 
ATOM   1288 C  CE   A LYS A 1 100 ? 13.500 -11.408 56.736 0.623 12.49 ? 100  LYS A CE   1 
ATOM   1289 C  CE   B LYS A 1 100 ? 13.917 -11.068 56.628 0.377 10.67 ? 100  LYS A CE   1 
ATOM   1290 N  NZ   A LYS A 1 100 ? 12.396 -10.719 57.465 0.623 10.53 ? 100  LYS A NZ   1 
ATOM   1291 N  NZ   B LYS A 1 100 ? 12.591 -10.768 57.255 0.377 16.70 ? 100  LYS A NZ   1 
ATOM   1292 N  N    A GLY A 1 101 ? 16.617 -15.410 54.612 0.623 11.86 ? 101  GLY A N    1 
ATOM   1293 N  N    B GLY A 1 101 ? 16.933 -16.669 54.368 0.377 16.50 ? 101  GLY A N    1 
ATOM   1294 C  CA   A GLY A 1 101 ? 16.991 -16.697 55.135 0.623 11.25 ? 101  GLY A CA   1 
ATOM   1295 C  CA   B GLY A 1 101 ? 17.161 -18.098 54.401 0.377 15.64 ? 101  GLY A CA   1 
ATOM   1296 C  C    A GLY A 1 101 ? 18.075 -17.436 54.357 0.623 13.90 ? 101  GLY A C    1 
ATOM   1297 C  C    B GLY A 1 101 ? 18.331 -18.617 53.571 0.377 16.82 ? 101  GLY A C    1 
ATOM   1298 O  O    A GLY A 1 101 ? 18.409 -18.556 54.768 0.623 14.89 ? 101  GLY A O    1 
ATOM   1299 O  O    B GLY A 1 101 ? 18.601 -19.839 53.599 0.377 23.55 ? 101  GLY A O    1 
ATOM   1300 N  N    A THR A 1 102 ? 18.656 -16.841 53.296 0.623 11.91 ? 102  THR A N    1 
ATOM   1301 N  N    B THR A 1 102 ? 19.033 -17.752 52.809 0.377 13.36 ? 102  THR A N    1 
ATOM   1302 C  CA   A THR A 1 102 ? 19.723 -17.587 52.582 0.623 12.18 ? 102  THR A CA   1 
ATOM   1303 C  CA   B THR A 1 102 ? 20.154 -18.233 51.988 0.377 15.51 ? 102  THR A CA   1 
ATOM   1304 C  C    A THR A 1 102 ? 21.093 -17.388 53.232 0.623 11.45 ? 102  THR A C    1 
ATOM   1305 C  C    B THR A 1 102 ? 21.554 -18.097 52.570 0.377 14.02 ? 102  THR A C    1 
ATOM   1306 O  O    A THR A 1 102 ? 22.026 -18.025 52.717 0.623 13.29 ? 102  THR A O    1 
ATOM   1307 O  O    B THR A 1 102 ? 22.527 -18.430 51.875 0.377 17.73 ? 102  THR A O    1 
ATOM   1308 C  CB   A THR A 1 102 ? 19.772 -17.326 51.079 0.623 12.17 ? 102  THR A CB   1 
ATOM   1309 C  CB   B THR A 1 102 ? 20.103 -17.484 50.639 0.377 14.59 ? 102  THR A CB   1 
ATOM   1310 O  OG1  A THR A 1 102 ? 20.036 -15.958 50.776 0.623 14.88 ? 102  THR A OG1  1 
ATOM   1311 O  OG1  B THR A 1 102 ? 20.001 -16.072 50.878 0.377 9.58  ? 102  THR A OG1  1 
ATOM   1312 C  CG2  A THR A 1 102 ? 18.433 -17.663 50.439 0.623 13.82 ? 102  THR A CG2  1 
ATOM   1313 C  CG2  B THR A 1 102 ? 18.846 -17.893 49.888 0.377 18.93 ? 102  THR A CG2  1 
ATOM   1314 N  N    A GLU A 1 103 ? 21.276 -16.582 54.262 0.623 12.04 ? 103  GLU A N    1 
ATOM   1315 N  N    B GLU A 1 103 ? 21.667 -17.630 53.769 0.377 16.46 ? 103  GLU A N    1 
ATOM   1316 C  CA   A GLU A 1 103 ? 22.401 -16.502 55.193 0.623 13.53 ? 103  GLU A CA   1 
ATOM   1317 C  CA   B GLU A 1 103 ? 22.540 -17.270 54.861 0.377 18.80 ? 103  GLU A CA   1 
ATOM   1318 C  C    A GLU A 1 103 ? 23.778 -16.090 54.675 0.623 13.51 ? 103  GLU A C    1 
ATOM   1319 C  C    B GLU A 1 103 ? 23.906 -16.734 54.426 0.377 18.56 ? 103  GLU A C    1 
ATOM   1320 O  O    A GLU A 1 103 ? 24.553 -15.443 55.417 0.623 15.90 ? 103  GLU A O    1 
ATOM   1321 O  O    B GLU A 1 103 ? 24.777 -16.279 55.169 0.377 21.85 ? 103  GLU A O    1 
ATOM   1322 C  CB   A GLU A 1 103 ? 22.525 -17.894 55.851 0.623 18.03 ? 103  GLU A CB   1 
ATOM   1323 C  CB   B GLU A 1 103 ? 22.632 -18.444 55.858 0.377 23.02 ? 103  GLU A CB   1 
ATOM   1324 C  CG   A GLU A 1 103 ? 21.280 -18.377 56.604 0.623 26.98 ? 103  GLU A CG   1 
ATOM   1325 C  CG   B GLU A 1 103 ? 21.300 -18.646 56.610 0.377 27.63 ? 103  GLU A CG   1 
ATOM   1326 C  CD   A GLU A 1 103 ? 21.637 -19.629 57.376 0.623 34.70 ? 103  GLU A CD   1 
ATOM   1327 C  CD   B GLU A 1 103 ? 21.437 -19.679 57.710 0.377 35.75 ? 103  GLU A CD   1 
ATOM   1328 O  OE1  A GLU A 1 103 ? 22.832 -19.811 57.719 0.623 41.11 ? 103  GLU A OE1  1 
ATOM   1329 O  OE1  B GLU A 1 103 ? 20.418 -20.130 58.284 0.377 45.62 ? 103  GLU A OE1  1 
ATOM   1330 O  OE2  A GLU A 1 103 ? 20.732 -20.453 57.637 0.623 46.90 ? 103  GLU A OE2  1 
ATOM   1331 O  OE2  B GLU A 1 103 ? 22.596 -20.059 58.006 0.377 40.15 ? 103  GLU A OE2  1 
ATOM   1332 N  N    A PHE A 1 104 ? 24.188 -16.464 53.469 0.623 14.85 ? 104  PHE A N    1 
ATOM   1333 N  N    B PHE A 1 104 ? 24.276 -16.651 53.164 0.377 16.27 ? 104  PHE A N    1 
ATOM   1334 C  CA   A PHE A 1 104 ? 25.511 -16.171 52.946 0.623 14.57 ? 104  PHE A CA   1 
ATOM   1335 C  CA   B PHE A 1 104 ? 25.609 -16.200 52.794 0.377 15.58 ? 104  PHE A CA   1 
ATOM   1336 C  C    A PHE A 1 104 ? 25.737 -14.642 53.028 0.623 12.30 ? 104  PHE A C    1 
ATOM   1337 C  C    B PHE A 1 104 ? 25.748 -14.683 52.957 0.377 12.77 ? 104  PHE A C    1 
ATOM   1338 O  O    A PHE A 1 104 ? 24.755 -13.887 52.921 0.623 12.38 ? 104  PHE A O    1 
ATOM   1339 O  O    B PHE A 1 104 ? 24.773 -13.924 52.895 0.377 12.52 ? 104  PHE A O    1 
ATOM   1340 C  CB   A PHE A 1 104 ? 25.710 -16.685 51.518 0.623 13.22 ? 104  PHE A CB   1 
ATOM   1341 C  CB   B PHE A 1 104 ? 25.898 -16.675 51.359 0.377 15.14 ? 104  PHE A CB   1 
ATOM   1342 C  CG   A PHE A 1 104 ? 24.888 -16.019 50.422 0.623 11.63 ? 104  PHE A CG   1 
ATOM   1343 C  CG   B PHE A 1 104 ? 24.951 -16.043 50.349 0.377 11.73 ? 104  PHE A CG   1 
ATOM   1344 C  CD1  A PHE A 1 104 ? 25.191 -14.830 49.808 0.623 10.50 ? 104  PHE A CD1  1 
ATOM   1345 C  CD1  B PHE A 1 104 ? 25.225 -14.793 49.842 0.377 10.49 ? 104  PHE A CD1  1 
ATOM   1346 C  CD2  A PHE A 1 104 ? 23.702 -16.613 49.969 0.623 12.87 ? 104  PHE A CD2  1 
ATOM   1347 C  CD2  B PHE A 1 104 ? 23.794 -16.664 49.898 0.377 12.60 ? 104  PHE A CD2  1 
ATOM   1348 C  CE1  A PHE A 1 104 ? 24.409 -14.219 48.848 0.623 10.53 ? 104  PHE A CE1  1 
ATOM   1349 C  CE1  B PHE A 1 104 ? 24.391 -14.181 48.923 0.377 10.32 ? 104  PHE A CE1  1 
ATOM   1350 C  CE2  A PHE A 1 104 ? 22.886 -16.017 49.003 0.623 11.22 ? 104  PHE A CE2  1 
ATOM   1351 C  CE2  B PHE A 1 104 ? 22.936 -16.057 48.979 0.377 10.89 ? 104  PHE A CE2  1 
ATOM   1352 C  CZ   A PHE A 1 104 ? 23.217 -14.820 48.432 0.623 9.98  ? 104  PHE A CZ   1 
ATOM   1353 C  CZ   B PHE A 1 104 ? 23.228 -14.808 48.487 0.377 9.88  ? 104  PHE A CZ   1 
ATOM   1354 H  HB2  A PHE A 1 104 ? 26.614 -16.525 51.247 0.623 15.86 ? 104  PHE A HB2  1 
ATOM   1355 H  HB2  B PHE A 1 104 ? 26.802 -16.514 51.086 0.377 18.17 ? 104  PHE A HB2  1 
ATOM   1356 H  HD1  A PHE A 1 104 ? 25.979 -14.404 50.057 0.623 12.60 ? 104  PHE A HD1  1 
ATOM   1357 H  HD1  B PHE A 1 104 ? 25.991 -14.348 50.125 0.377 12.58 ? 104  PHE A HD1  1 
ATOM   1358 H  HD2  A PHE A 1 104 ? 23.448 -17.433 50.325 0.623 15.44 ? 104  PHE A HD2  1 
ATOM   1359 H  HD2  B PHE A 1 104 ? 23.584 -17.511 50.218 0.377 15.12 ? 104  PHE A HD2  1 
ATOM   1360 H  HE1  A PHE A 1 104 ? 24.676 -13.409 48.478 0.623 12.64 ? 104  PHE A HE1  1 
ATOM   1361 H  HE1  B PHE A 1 104 ? 24.610 -13.339 48.593 0.377 12.38 ? 104  PHE A HE1  1 
ATOM   1362 H  HE2  A PHE A 1 104 ? 22.102 -16.444 48.743 0.623 13.47 ? 104  PHE A HE2  1 
ATOM   1363 H  HE2  B PHE A 1 104 ? 22.166 -16.498 48.700 0.377 13.07 ? 104  PHE A HE2  1 
ATOM   1364 N  N    . THR A 1 105 ? 26.984 -14.259 53.161 1.000 13.15 ? 105  THR A N    1 
ATOM   1365 C  CA   . THR A 1 105 ? 27.299 -12.845 53.350 1.000 11.95 ? 105  THR A CA   1 
ATOM   1366 C  C    . THR A 1 105 ? 28.003 -12.303 52.108 1.000 11.11 ? 105  THR A C    1 
ATOM   1367 O  O    . THR A 1 105 ? 28.269 -13.054 51.123 1.000 11.25 ? 105  THR A O    1 
ATOM   1368 C  CB   . THR A 1 105 ? 28.179 -12.613 54.586 1.000 12.90 ? 105  THR A CB   1 
ATOM   1369 O  OG1  . THR A 1 105 ? 29.505 -13.055 54.161 1.000 14.50 ? 105  THR A OG1  1 
ATOM   1370 C  CG2  . THR A 1 105 ? 27.594 -13.391 55.775 1.000 17.95 ? 105  THR A CG2  1 
ATOM   1371 H  H    A THR A 1 105 ? 27.616 -14.841 53.137 1.000 15.78 ? 105  THR A H    1 
ATOM   1372 N  N    . VAL A 1 106 ? 28.366 -11.030 52.168 1.000 11.31 ? 106  VAL A N    1 
ATOM   1373 C  CA   . VAL A 1 106 ? 29.157 -10.419 51.112 1.000 11.14 ? 106  VAL A CA   1 
ATOM   1374 C  C    . VAL A 1 106 ? 30.481 -11.158 50.862 1.000 12.27 ? 106  VAL A C    1 
ATOM   1375 O  O    . VAL A 1 106 ? 31.013 -11.104 49.792 1.000 16.89 ? 106  VAL A O    1 
ATOM   1376 C  CB   . VAL A 1 106 ? 29.440 -8.938  51.476 1.000 11.20 ? 106  VAL A CB   1 
ATOM   1377 C  CG1  . VAL A 1 106 ? 30.261 -8.798  52.752 1.000 12.36 ? 106  VAL A CG1  1 
ATOM   1378 C  CG2  . VAL A 1 106 ? 30.083 -8.149  50.344 1.000 15.08 ? 106  VAL A CG2  1 
ATOM   1379 H  HA   . VAL A 1 106 ? 28.632 -10.438 50.284 1.000 13.37 ? 106  VAL A HA   1 
ATOM   1380 H  HB   . VAL A 1 106 ? 28.571 -8.520  51.652 1.000 13.44 ? 106  VAL A HB   1 
ATOM   1381 H  HG12 . VAL A 1 106 ? 31.143 -9.147  52.603 1.000 18.54 ? 106  VAL A HG12 1 
ATOM   1382 H  HG23 . VAL A 1 106 ? 30.964 -8.496  50.185 1.000 22.62 ? 106  VAL A HG23 1 
ATOM   1383 N  N    . ASN A 1 107 ? 30.973 -11.823 51.881 1.000 10.77 ? 107  ASN A N    1 
ATOM   1384 C  CA   . ASN A 1 107 ? 32.255 -12.522 51.725 1.000 11.75 ? 107  ASN A CA   1 
ATOM   1385 C  C    . ASN A 1 107 ? 32.101 -13.882 51.102 1.000 12.01 ? 107  ASN A C    1 
ATOM   1386 O  O    . ASN A 1 107 ? 33.110 -14.579 50.876 1.000 14.39 ? 107  ASN A O    1 
ATOM   1387 C  CB   . ASN A 1 107 ? 32.894 -12.652 53.131 1.000 13.28 ? 107  ASN A CB   1 
ATOM   1388 C  CG   . ASN A 1 107 ? 33.203 -11.297 53.678 1.000 14.31 ? 107  ASN A CG   1 
ATOM   1389 O  OD1  . ASN A 1 107 ? 33.865 -10.509 53.015 1.000 17.43 ? 107  ASN A OD1  1 
ATOM   1390 N  ND2  . ASN A 1 107 ? 32.766 -11.016 54.911 1.000 19.44 ? 107  ASN A ND2  1 
ATOM   1391 H  H    . ASN A 1 107 ? 30.551 -11.849 52.629 1.000 12.93 ? 107  ASN A H    1 
ATOM   1392 H  HB2  . ASN A 1 107 ? 32.263 -13.089 53.724 1.000 15.93 ? 107  ASN A HB2  1 
ATOM   1393 N  N    . ASP A 1 108 ? 30.890 -14.300 50.801 1.000 11.72 ? 108  ASP A N    1 
ATOM   1394 C  CA   . ASP A 1 108 ? 30.510 -15.600 50.279 1.000 12.43 ? 108  ASP A CA   1 
ATOM   1395 C  C    . ASP A 1 108 ? 29.908 -15.484 48.882 1.000 10.75 ? 108  ASP A C    1 
ATOM   1396 O  O    . ASP A 1 108 ? 29.233 -16.424 48.444 1.000 12.98 ? 108  ASP A O    1 
ATOM   1397 C  CB   . ASP A 1 108 ? 29.506 -16.284 51.210 1.000 17.19 ? 108  ASP A CB   1 
ATOM   1398 C  CG   . ASP A 1 108 ? 29.918 -16.359 52.641 1.000 22.67 ? 108  ASP A CG   1 
ATOM   1399 O  OD1  . ASP A 1 108 ? 31.099 -16.656 52.963 1.000 27.52 ? 108  ASP A OD1  1 
ATOM   1400 O  OD2  . ASP A 1 108 ? 29.029 -16.189 53.539 1.000 20.24 ? 108  ASP A OD2  1 
ATOM   1401 H  HB3  . ASP A 1 108 ? 29.346 -17.184 50.886 1.000 20.62 ? 108  ASP A HB3  1 
ATOM   1402 N  N    . LEU A 1 109 ? 30.184 -14.426 48.157 1.000 9.66  ? 109  LEU A N    1 
ATOM   1403 C  CA   . LEU A 1 109 ? 29.540 -14.264 46.830 1.000 8.83  ? 109  LEU A CA   1 
ATOM   1404 C  C    . LEU A 1 109 ? 30.174 -15.082 45.722 1.000 8.95  ? 109  LEU A C    1 
ATOM   1405 O  O    . LEU A 1 109 ? 29.543 -15.264 44.688 1.000 8.95  ? 109  LEU A O    1 
ATOM   1406 C  CB   . LEU A 1 109 ? 29.499 -12.777 46.489 1.000 8.73  ? 109  LEU A CB   1 
ATOM   1407 C  CG   . LEU A 1 109 ? 28.416 -11.975 47.220 1.000 8.96  ? 109  LEU A CG   1 
ATOM   1408 C  CD1  . LEU A 1 109 ? 28.677 -10.494 47.031 1.000 9.92  ? 109  LEU A CD1  1 
ATOM   1409 C  CD2  . LEU A 1 109 ? 27.039 -12.338 46.732 1.000 11.93 ? 109  LEU A CD2  1 
ATOM   1410 H  HA   . LEU A 1 109 ? 28.612 -14.567 46.920 1.000 10.60 ? 109  LEU A HA   1 
ATOM   1411 H  HB3  . LEU A 1 109 ? 29.344 -12.693 45.535 1.000 10.48 ? 109  LEU A HB3  1 
ATOM   1412 H  HD12 . LEU A 1 109 ? 28.601 -10.276 46.099 1.000 14.88 ? 109  LEU A HD12 1 
ATOM   1413 H  HD13 . LEU A 1 109 ? 28.030 -9.992  47.531 1.000 14.88 ? 109  LEU A HD13 1 
ATOM   1414 H  HD22 . LEU A 1 109 ? 26.972 -12.166 45.790 1.000 17.90 ? 109  LEU A HD22 1 
ATOM   1415 H  HD23 . LEU A 1 109 ? 26.890 -13.272 46.898 1.000 17.90 ? 109  LEU A HD23 1 
ATOM   1416 N  N    . GLN A 1 110 ? 31.424 -15.521 45.899 1.000 9.25  ? 110  GLN A N    1 
ATOM   1417 C  CA   . GLN A 1 110 ? 32.043 -16.308 44.838 1.000 9.01  ? 110  GLN A CA   1 
ATOM   1418 C  C    . GLN A 1 110 ? 31.120 -17.507 44.547 1.000 9.02  ? 110  GLN A C    1 
ATOM   1419 O  O    . GLN A 1 110 ? 30.634 -18.181 45.446 1.000 9.92  ? 110  GLN A O    1 
ATOM   1420 C  CB   . GLN A 1 110 ? 33.465 -16.738 45.201 1.000 9.73  ? 110  GLN A CB   1 
ATOM   1421 C  CG   . GLN A 1 110 ? 34.266 -17.331 44.084 1.000 10.32 ? 110  GLN A CG   1 
ATOM   1422 C  CD   . GLN A 1 110 ? 33.969 -18.802 43.740 1.000 9.46  ? 110  GLN A CD   1 
ATOM   1423 O  OE1  . GLN A 1 110 ? 33.280 -19.489 44.501 1.000 10.73 ? 110  GLN A OE1  1 
ATOM   1424 N  NE2  . GLN A 1 110 ? 34.465 -19.259 42.636 1.000 10.92 ? 110  GLN A NE2  1 
ATOM   1425 H  H    . GLN A 1 110 ? 31.854 -15.343 46.622 1.000 11.10 ? 110  GLN A H    1 
ATOM   1426 H  HA   . GLN A 1 110 ? 32.087 -15.754 44.031 1.000 10.81 ? 110  GLN A HA   1 
ATOM   1427 H  HB3  . GLN A 1 110 ? 33.410 -17.396 45.912 1.000 11.68 ? 110  GLN A HB3  1 
ATOM   1428 H  HE22 . GLN A 1 110 ? 34.930 -18.725 42.149 1.000 13.11 ? 110  GLN A HE22 1 
ATOM   1429 N  N    . GLY A 1 111 ? 30.934 -17.789 43.253 1.000 9.11  ? 111  GLY A N    1 
ATOM   1430 C  CA   . GLY A 1 111 ? 30.193 -18.961 42.847 1.000 9.29  ? 111  GLY A CA   1 
ATOM   1431 C  C    . GLY A 1 111 ? 28.687 -18.799 42.864 1.000 9.35  ? 111  GLY A C    1 
ATOM   1432 O  O    . GLY A 1 111 ? 27.983 -19.687 42.384 1.000 11.42 ? 111  GLY A O    1 
ATOM   1433 H  HA2  . GLY A 1 111 ? 30.468 -19.204 41.949 1.000 11.14 ? 111  GLY A HA2  1 
ATOM   1434 H  HA3  . GLY A 1 111 ? 30.431 -19.695 43.434 1.000 11.14 ? 111  GLY A HA3  1 
ATOM   1435 N  N    . LYS A 1 112 ? 28.178 -17.673 43.362 1.000 8.56  ? 112  LYS A N    1 
ATOM   1436 C  CA   . LYS A 1 112 ? 26.769 -17.412 43.340 1.000 8.19  ? 112  LYS A CA   1 
ATOM   1437 C  C    . LYS A 1 112 ? 26.362 -16.968 41.944 1.000 7.81  ? 112  LYS A C    1 
ATOM   1438 O  O    . LYS A 1 112 ? 27.174 -16.578 41.114 1.000 8.77  ? 112  LYS A O    1 
ATOM   1439 C  CB   . LYS A 1 112 ? 26.383 -16.329 44.379 1.000 8.85  ? 112  LYS A CB   1 
ATOM   1440 C  CG   . LYS A 1 112 ? 26.676 -16.714 45.839 1.000 11.66 ? 112  LYS A CG   1 
ATOM   1441 C  CD   . LYS A 1 112 ? 25.900 -17.942 46.312 1.000 15.19 ? 112  LYS A CD   1 
ATOM   1442 C  CE   . LYS A 1 112 ? 26.164 -18.252 47.766 1.000 18.99 ? 112  LYS A CE   1 
ATOM   1443 N  NZ   . LYS A 1 112 ? 27.563 -18.687 48.037 1.000 18.14 ? 112  LYS A NZ   1 
ATOM   1444 H  H    . LYS A 1 112 ? 28.707 -17.088 43.705 1.000 10.27 ? 112  LYS A H    1 
ATOM   1445 H  HD3  . LYS A 1 112 ? 26.197 -18.692 45.773 1.000 18.22 ? 112  LYS A HD3  1 
ATOM   1446 N  N    . THR A 1 113 ? 25.047 -16.983 41.694 1.000 7.60  ? 113  THR A N    1 
ATOM   1447 C  CA   . THR A 1 113 ? 24.468 -16.370 40.489 1.000 7.25  ? 113  THR A CA   1 
ATOM   1448 C  C    . THR A 1 113 ? 24.043 -14.952 40.836 1.000 6.59  ? 113  THR A C    1 
ATOM   1449 O  O    . THR A 1 113 ? 23.652 -14.663 41.968 1.000 7.22  ? 113  THR A O    1 
ATOM   1450 C  CB   . THR A 1 113 ? 23.315 -17.185 39.935 1.000 7.40  ? 113  THR A CB   1 
ATOM   1451 O  OG1  . THR A 1 113 ? 22.345 -17.296 40.963 1.000 8.26  ? 113  THR A OG1  1 
ATOM   1452 C  CG2  . THR A 1 113 ? 23.766 -18.578 39.448 1.000 8.90  ? 113  THR A CG2  1 
ATOM   1453 H  H    . THR A 1 113 ? 24.522 -17.364 42.259 1.000 9.12  ? 113  THR A H    1 
ATOM   1454 H  HA   . THR A 1 113 ? 25.167 -16.321 39.804 1.000 8.71  ? 113  THR A HA   1 
ATOM   1455 H  HB   . THR A 1 113 ? 22.921 -16.700 39.180 1.000 8.88  ? 113  THR A HB   1 
ATOM   1456 H  HG21 . THR A 1 113 ? 24.424 -18.488 38.755 1.000 13.35 ? 113  THR A HG21 1 
ATOM   1457 N  N    . SER A 1 114 ? 24.102 -14.040 39.848 1.000 6.34  ? 114  SER A N    1 
ATOM   1458 C  CA   . SER A 1 114 ? 23.852 -12.639 40.115 1.000 6.19  ? 114  SER A CA   1 
ATOM   1459 C  C    . SER A 1 114 ? 23.037 -11.996 39.038 1.000 6.04  ? 114  SER A C    1 
ATOM   1460 O  O    . SER A 1 114 ? 23.124 -12.314 37.850 1.000 6.81  ? 114  SER A O    1 
ATOM   1461 C  CB   . SER A 1 114 ? 25.177 -11.895 40.287 1.000 6.60  ? 114  SER A CB   1 
ATOM   1462 O  OG   . SER A 1 114 ? 25.940 -11.905 39.089 1.000 6.86  ? 114  SER A OG   1 
ATOM   1463 H  H    . SER A 1 114 ? 24.290 -14.292 39.048 1.000 7.61  ? 114  SER A H    1 
ATOM   1464 H  HA   . SER A 1 114 ? 23.353 -12.573 40.956 1.000 7.42  ? 114  SER A HA   1 
ATOM   1465 H  HB2  . SER A 1 114 ? 24.998 -10.978 40.546 1.000 7.92  ? 114  SER A HB2  1 
ATOM   1466 H  HB3  . SER A 1 114 ? 25.689 -12.313 40.997 1.000 7.92  ? 114  SER A HB3  1 
ATOM   1467 N  N    . CYS A 1 115 ? 22.253 -10.985 39.479 1.000 5.59  ? 115  CYS A N    1 
ATOM   1468 C  CA   . CYS A 1 115 ? 21.365 -10.194 38.633 1.000 5.37  ? 115  CYS A CA   1 
ATOM   1469 C  C    . CYS A 1 115 ? 21.763 -8.723  38.722 1.000 5.35  ? 115  CYS A C    1 
ATOM   1470 O  O    . CYS A 1 115 ? 21.864 -8.180  39.812 1.000 6.12  ? 115  CYS A O    1 
ATOM   1471 C  CB   . CYS A 1 115 ? 19.932 -10.338 39.071 1.000 6.27  ? 115  CYS A CB   1 
ATOM   1472 S  SG   . CYS A 1 115 ? 19.333 -12.044 39.198 1.000 7.16  ? 115  CYS A SG   1 
ATOM   1473 H  H    . CYS A 1 115 ? 22.280 -10.794 40.317 1.000 6.71  ? 115  CYS A H    1 
ATOM   1474 H  HA   . CYS A 1 115 ? 21.450 -10.496 37.704 1.000 6.44  ? 115  CYS A HA   1 
ATOM   1475 H  HB2  . CYS A 1 115 ? 19.831 -9.911  39.936 1.000 7.52  ? 115  CYS A HB2  1 
ATOM   1476 H  HB3  . CYS A 1 115 ? 19.369 -9.860  38.442 1.000 7.52  ? 115  CYS A HB3  1 
ATOM   1477 N  N    . HIS A 1 116 ? 21.984 -8.099  37.558 1.000 5.43  ? 116  HIS A N    1 
ATOM   1478 C  CA   . HIS A 1 116 ? 22.478 -6.743  37.473 1.000 5.43  ? 116  HIS A CA   1 
ATOM   1479 C  C    . HIS A 1 116 ? 21.543 -5.921  36.590 1.000 4.91  ? 116  HIS A C    1 
ATOM   1480 O  O    . HIS A 1 116 ? 20.957 -6.405  35.638 1.000 5.70  ? 116  HIS A O    1 
ATOM   1481 C  CB   . HIS A 1 116 ? 23.876 -6.766  36.837 1.000 5.35  ? 116  HIS A CB   1 
ATOM   1482 C  CG   . HIS A 1 116 ? 24.850 -7.614  37.584 1.000 5.59  ? 116  HIS A CG   1 
ATOM   1483 N  ND1  . HIS A 1 116 ? 25.824 -7.076  38.379 1.000 6.20  ? 116  HIS A ND1  1 
ATOM   1484 C  CD2  . HIS A 1 116 ? 25.023 -8.951  37.669 1.000 6.29  ? 116  HIS A CD2  1 
ATOM   1485 C  CE1  . HIS A 1 116 ? 26.515 -8.116  38.901 1.000 6.43  ? 116  HIS A CE1  1 
ATOM   1486 N  NE2  . HIS A 1 116 ? 26.055 -9.275  38.492 1.000 6.52  ? 116  HIS A NE2  1 
ATOM   1487 H  H    . HIS A 1 116 ? 21.825 -8.524  36.828 1.000 6.51  ? 116  HIS A H    1 
ATOM   1488 H  HA   . HIS A 1 116 ? 22.524 -6.347  38.368 1.000 6.52  ? 116  HIS A HA   1 
ATOM   1489 H  HB2  . HIS A 1 116 ? 23.803 -7.096  35.929 1.000 6.42  ? 116  HIS A HB2  1 
ATOM   1490 H  HB3  . HIS A 1 116 ? 24.217 -5.859  36.795 1.000 6.42  ? 116  HIS A HB3  1 
ATOM   1491 H  HD1  . HIS A 1 116 ? 25.969 -6.240  38.519 1.000 7.45  ? 116  HIS A HD1  1 
ATOM   1492 H  HE1  . HIS A 1 116 ? 27.234 -8.021  39.483 1.000 7.71  ? 116  HIS A HE1  1 
ATOM   1493 N  N    . THR A 1 117 ? 21.460 -4.605  36.874 1.000 5.04  ? 117  THR A N    1 
ATOM   1494 C  CA   . THR A 1 117 ? 20.582 -3.748  36.060 1.000 4.84  ? 117  THR A CA   1 
ATOM   1495 C  C    . THR A 1 117 ? 21.020 -3.633  34.624 1.000 4.82  ? 117  THR A C    1 
ATOM   1496 O  O    . THR A 1 117 ? 20.193 -3.548  33.717 1.000 5.24  ? 117  THR A O    1 
ATOM   1497 C  CB   . THR A 1 117 ? 20.484 -2.344  36.703 1.000 5.19  ? 117  THR A CB   1 
ATOM   1498 O  OG1  . THR A 1 117 ? 21.774 -1.768  36.584 1.000 5.31  ? 117  THR A OG1  1 
ATOM   1499 C  CG2  . THR A 1 117 ? 19.999 -2.378  38.126 1.000 5.69  ? 117  THR A CG2  1 
ATOM   1500 H  H    . THR A 1 117 ? 21.914 -4.271  37.524 1.000 6.05  ? 117  THR A H    1 
ATOM   1501 H  HA   . THR A 1 117 ? 19.686 -4.144  36.068 1.000 5.81  ? 117  THR A HA   1 
ATOM   1502 H  HB   . THR A 1 117 ? 19.857 -1.807  36.176 1.000 6.23  ? 117  THR A HB   1 
ATOM   1503 H  HG1  . THR A 1 117 ? 21.861 -1.176  37.145 1.000 7.97  ? 117  THR A HG1  1 
ATOM   1504 H  HG21 . THR A 1 117 ? 19.130 -2.785  38.153 1.000 8.53  ? 117  THR A HG21 1 
ATOM   1505 H  HG23 . THR A 1 117 ? 19.945 -1.483  38.469 1.000 8.53  ? 117  THR A HG23 1 
ATOM   1506 N  N    . GLY A 1 118 ? 22.336 -3.589  34.416 1.000 5.38  ? 118  GLY A N    1 
ATOM   1507 C  CA   . GLY A 1 118 ? 22.933 -3.388  33.094 1.000 5.45  ? 118  GLY A CA   1 
ATOM   1508 C  C    . GLY A 1 118 ? 24.403 -3.146  33.236 1.000 5.30  ? 118  GLY A C    1 
ATOM   1509 O  O    . GLY A 1 118 ? 24.879 -2.610  34.257 1.000 5.88  ? 118  GLY A O    1 
ATOM   1510 H  H    . GLY A 1 118 ? 22.860 -3.682  35.092 1.000 6.46  ? 118  GLY A H    1 
ATOM   1511 H  HA2  . GLY A 1 118 ? 22.783 -4.173  32.545 1.000 6.54  ? 118  GLY A HA2  1 
ATOM   1512 H  HA3  . GLY A 1 118 ? 22.517 -2.629  32.658 1.000 6.54  ? 118  GLY A HA3  1 
ATOM   1513 N  N    . LEU A 1 119 ? 25.139 -3.489  32.204 1.000 5.50  ? 119  LEU A N    1 
ATOM   1514 C  CA   . LEU A 1 119 ? 26.578 -3.287  32.174 1.000 5.67  ? 119  LEU A CA   1 
ATOM   1515 C  C    . LEU A 1 119 ? 26.863 -1.808  32.308 1.000 5.63  ? 119  LEU A C    1 
ATOM   1516 O  O    . LEU A 1 119 ? 26.275 -0.942  31.612 1.000 6.71  ? 119  LEU A O    1 
ATOM   1517 C  CB   . LEU A 1 119 ? 27.120 -3.826  30.842 1.000 6.22  ? 119  LEU A CB   1 
ATOM   1518 C  CG   . LEU A 1 119 ? 28.637 -3.727  30.695 1.000 7.27  ? 119  LEU A CG   1 
ATOM   1519 C  CD1  . LEU A 1 119 ? 29.275 -4.765  31.575 1.000 11.55 ? 119  LEU A CD1  1 
ATOM   1520 C  CD2  . LEU A 1 119 ? 29.042 -3.966  29.248 1.000 8.59  ? 119  LEU A CD2  1 
ATOM   1521 H  H    . LEU A 1 119 ? 24.756 -3.845  31.522 1.000 6.60  ? 119  LEU A H    1 
ATOM   1522 H  HA   . LEU A 1 119 ? 26.993 -3.770  32.918 1.000 6.80  ? 119  LEU A HA   1 
ATOM   1523 H  HB2  . LEU A 1 119 ? 26.859 -4.756  30.754 1.000 7.46  ? 119  LEU A HB2  1 
ATOM   1524 H  HB3  . LEU A 1 119 ? 26.705 -3.334  30.116 1.000 7.46  ? 119  LEU A HB3  1 
ATOM   1525 H  HG   . LEU A 1 119 ? 28.935 -2.836  30.974 1.000 8.73  ? 119  LEU A HG   1 
ATOM   1526 H  HD11 . LEU A 1 119 ? 29.011 -4.608  32.484 1.000 17.32 ? 119  LEU A HD11 1 
ATOM   1527 H  HD13 . LEU A 1 119 ? 30.230 -4.695  31.502 1.000 17.32 ? 119  LEU A HD13 1 
ATOM   1528 H  HD21 . LEU A 1 119 ? 28.625 -3.298  28.699 1.000 12.88 ? 119  LEU A HD21 1 
ATOM   1529 H  HD23 . LEU A 1 119 ? 28.740 -4.836  28.978 1.000 12.88 ? 119  LEU A HD23 1 
ATOM   1530 N  N    . GLY A 1 120 ? 27.814 -1.452  33.184 1.000 5.82  ? 120  GLY A N    1 
ATOM   1531 C  CA   . GLY A 1 120 ? 28.241 -0.081  33.302 1.000 6.13  ? 120  GLY A CA   1 
ATOM   1532 C  C    . GLY A 1 120 ? 27.336 0.855   34.058 1.000 5.83  ? 120  GLY A C    1 
ATOM   1533 O  O    . GLY A 1 120 ? 27.658 2.039   34.158 1.000 6.79  ? 120  GLY A O    1 
ATOM   1534 H  H    . GLY A 1 120 ? 28.175 -2.052  33.683 1.000 6.98  ? 120  GLY A H    1 
ATOM   1535 H  HA2  . GLY A 1 120 ? 29.110 -0.073  33.735 1.000 7.35  ? 120  GLY A HA2  1 
ATOM   1536 H  HA3  . GLY A 1 120 ? 28.362 0.275   32.408 1.000 7.35  ? 120  GLY A HA3  1 
ATOM   1537 N  N    . ARG A 1 121 ? 26.224 0.373   34.590 1.000 5.47  ? 121  ARG A N    1 
ATOM   1538 C  CA   . ARG A 1 121 ? 25.333 1.187   35.411 1.000 5.04  ? 121  ARG A CA   1 
ATOM   1539 C  C    . ARG A 1 121 ? 25.825 1.257   36.838 1.000 4.96  ? 121  ARG A C    1 
ATOM   1540 O  O    . ARG A 1 121 ? 26.543 0.358   37.304 1.000 6.12  ? 121  ARG A O    1 
ATOM   1541 C  CB   . ARG A 1 121 ? 23.904 0.656   35.329 1.000 5.11  ? 121  ARG A CB   1 
ATOM   1542 C  CG   . ARG A 1 121 ? 23.276 0.799   33.952 1.000 5.55  ? 121  ARG A CG   1 
ATOM   1543 C  CD   . ARG A 1 121 ? 21.909 0.219   33.796 1.000 5.56  ? 121  ARG A CD   1 
ATOM   1544 N  NE   . ARG A 1 121 ? 20.943 0.851   34.709 1.000 5.22  ? 121  ARG A NE   1 
ATOM   1545 C  CZ   . ARG A 1 121 ? 19.627 0.759   34.597 1.000 5.10  ? 121  ARG A CZ   1 
ATOM   1546 N  NH1  . ARG A 1 121 ? 19.066 0.165   33.552 1.000 5.47  ? 121  ARG A NH1  1 
ATOM   1547 N  NH2  . ARG A 1 121 ? 18.879 1.255   35.562 1.000 5.56  ? 121  ARG A NH2  1 
ATOM   1548 H  H    . ARG A 1 121 ? 26.019 -0.450  34.447 1.000 6.57  ? 121  ARG A H    1 
ATOM   1549 H  HA   . ARG A 1 121 ? 25.337 2.096   35.047 1.000 6.04  ? 121  ARG A HA   1 
ATOM   1550 H  HB2  . ARG A 1 121 ? 23.904 -0.282  35.577 1.000 6.13  ? 121  ARG A HB2  1 
ATOM   1551 H  HB3  . ARG A 1 121 ? 23.357 1.131   35.974 1.000 6.13  ? 121  ARG A HB3  1 
ATOM   1552 H  HG2  . ARG A 1 121 ? 23.233 1.743   33.734 1.000 6.67  ? 121  ARG A HG2  1 
ATOM   1553 H  HG3  . ARG A 1 121 ? 23.862 0.378   33.305 1.000 6.67  ? 121  ARG A HG3  1 
ATOM   1554 H  HD2  . ARG A 1 121 ? 21.612 0.341   32.881 1.000 6.68  ? 121  ARG A HD2  1 
ATOM   1555 H  HD3  . ARG A 1 121 ? 21.943 -0.734  33.975 1.000 6.68  ? 121  ARG A HD3  1 
ATOM   1556 H  HE   . ARG A 1 121 ? 21.257 1.313   35.362 1.000 6.27  ? 121  ARG A HE   1 
ATOM   1557 H  HH11 . ARG A 1 121 ? 18.210 0.102   33.501 1.000 6.56  ? 121  ARG A HH11 1 
ATOM   1558 H  HH12 . ARG A 1 121 ? 19.559 -0.158  32.925 1.000 6.56  ? 121  ARG A HH12 1 
ATOM   1559 H  HH21 . ARG A 1 121 ? 19.247 1.628   36.244 1.000 6.67  ? 121  ARG A HH21 1 
ATOM   1560 H  HH22 . ARG A 1 121 ? 18.022 1.207   35.510 1.000 6.67  ? 121  ARG A HH22 1 
ATOM   1561 N  N    . SER A 1 122 ? 25.428 2.291   37.577 1.000 5.19  ? 122  SER A N    1 
ATOM   1562 C  CA   . SER A 1 122 ? 25.925 2.518   38.910 1.000 5.46  ? 122  SER A CA   1 
ATOM   1563 C  C    . SER A 1 122 ? 25.649 1.421   39.921 1.000 5.10  ? 122  SER A C    1 
ATOM   1564 O  O    . SER A 1 122 ? 26.537 0.718   40.375 1.000 5.71  ? 122  SER A O    1 
ATOM   1565 C  CB   . SER A 1 122 ? 25.377 3.849   39.421 1.000 6.64  ? 122  SER A CB   1 
ATOM   1566 O  OG   . SER A 1 122 ? 25.846 4.958   38.651 1.000 8.01  ? 122  SER A OG   1 
ATOM   1567 H  H    . SER A 1 122 ? 24.855 2.841   37.248 1.000 6.22  ? 122  SER A H    1 
ATOM   1568 H  HA   . SER A 1 122 ? 26.899 2.612   38.844 1.000 6.55  ? 122  SER A HA   1 
ATOM   1569 H  HG   . SER A 1 122 ? 26.663 4.999   38.700 1.000 12.01 ? 122  SER A HG   1 
ATOM   1570 N  N    . ALA A 1 123 ? 24.377 1.316   40.331 1.000 5.08  ? 123  ALA A N    1 
ATOM   1571 C  CA   . ALA A 1 123 ? 24.032 0.321   41.340 1.000 5.54  ? 123  ALA A CA   1 
ATOM   1572 C  C    . ALA A 1 123 ? 24.184 -1.095  40.814 1.000 5.35  ? 123  ALA A C    1 
ATOM   1573 O  O    . ALA A 1 123 ? 24.497 -2.031  41.560 1.000 5.95  ? 123  ALA A O    1 
ATOM   1574 C  CB   . ALA A 1 123 ? 22.628 0.551   41.852 1.000 6.33  ? 123  ALA A CB   1 
ATOM   1575 H  H    . ALA A 1 123 ? 23.771 1.830   40.003 1.000 6.10  ? 123  ALA A H    1 
ATOM   1576 H  HA   . ALA A 1 123 ? 24.649 0.430   42.094 1.000 6.64  ? 123  ALA A HA   1 
ATOM   1577 H  HB1  . ALA A 1 123 ? 22.423 -0.128  42.496 1.000 7.60  ? 123  ALA A HB1  1 
ATOM   1578 N  N    . GLY A 1 124 ? 23.916 -1.273  39.515 1.000 5.31  ? 124  GLY A N    1 
ATOM   1579 C  CA   . GLY A 1 124 ? 23.930 -2.612  38.966 1.000 5.41  ? 124  GLY A CA   1 
ATOM   1580 C  C    . GLY A 1 124 ? 25.294 -3.171  38.644 1.000 5.79  ? 124  GLY A C    1 
ATOM   1581 O  O    . GLY A 1 124 ? 25.431 -4.385  38.432 1.000 6.73  ? 124  GLY A O    1 
ATOM   1582 H  H    . GLY A 1 124 ? 23.738 -0.598  39.012 1.000 6.38  ? 124  GLY A H    1 
ATOM   1583 H  HA2  . GLY A 1 124 ? 23.497 -3.207  39.599 1.000 6.49  ? 124  GLY A HA2  1 
ATOM   1584 H  HA3  . GLY A 1 124 ? 23.399 -2.616  38.154 1.000 6.49  ? 124  GLY A HA3  1 
ATOM   1585 N  N    . TRP A 1 125 ? 26.322 -2.314  38.536 1.000 5.58  ? 125  TRP A N    1 
ATOM   1586 C  CA   . TRP A 1 125 ? 27.606 -2.778  37.999 1.000 5.64  ? 125  TRP A CA   1 
ATOM   1587 C  C    . TRP A 1 125 ? 28.771 -2.022  38.642 1.000 5.55  ? 125  TRP A C    1 
ATOM   1588 O  O    . TRP A 1 125 ? 29.635 -2.627  39.278 1.000 5.98  ? 125  TRP A O    1 
ATOM   1589 C  CB   . TRP A 1 125 ? 27.627 -2.652  36.476 1.000 6.24  ? 125  TRP A CB   1 
ATOM   1590 C  CG   . TRP A 1 125 ? 28.863 -3.231  35.867 1.000 6.23  ? 125  TRP A CG   1 
ATOM   1591 C  CD1  . TRP A 1 125 ? 29.986 -2.572  35.458 1.000 7.49  ? 125  TRP A CD1  1 
ATOM   1592 C  CD2  . TRP A 1 125 ? 29.100 -4.634  35.616 1.000 6.38  ? 125  TRP A CD2  1 
ATOM   1593 N  NE1  . TRP A 1 125 ? 30.915 -3.449  34.959 1.000 8.16  ? 125  TRP A NE1  1 
ATOM   1594 C  CE2  . TRP A 1 125 ? 30.389 -4.714  35.040 1.000 7.46  ? 125  TRP A CE2  1 
ATOM   1595 C  CE3  . TRP A 1 125 ? 28.368 -5.797  35.826 1.000 7.45  ? 125  TRP A CE3  1 
ATOM   1596 C  CZ2  . TRP A 1 125 ? 30.937 -5.943  34.648 1.000 8.61  ? 125  TRP A CZ2  1 
ATOM   1597 C  CZ3  . TRP A 1 125 ? 28.909 -6.980  35.442 1.000 9.35  ? 125  TRP A CZ3  1 
ATOM   1598 C  CH2  . TRP A 1 125 ? 30.181 -7.056  34.864 1.000 9.70  ? 125  TRP A CH2  1 
ATOM   1599 H  H    . TRP A 1 125 ? 26.229 -1.495  38.782 1.000 6.70  ? 125  TRP A H    1 
ATOM   1600 H  HA   . TRP A 1 125 ? 27.701 -3.727  38.225 1.000 6.77  ? 125  TRP A HA   1 
ATOM   1601 H  HB2  . TRP A 1 125 ? 26.851 -3.106  36.110 1.000 7.49  ? 125  TRP A HB2  1 
ATOM   1602 H  HB3  . TRP A 1 125 ? 27.564 -1.715  36.235 1.000 7.49  ? 125  TRP A HB3  1 
ATOM   1603 H  HE1  . TRP A 1 125 ? 31.691 -3.242  34.650 1.000 9.80  ? 125  TRP A HE1  1 
ATOM   1604 H  HE3  . TRP A 1 125 ? 27.527 -5.764  36.221 1.000 8.95  ? 125  TRP A HE3  1 
ATOM   1605 N  N    . ASN A 1 126 ? 28.877 -0.714  38.399 1.000 5.85  ? 126  ASN A N    1 
ATOM   1606 C  CA   . ASN A 1 126 ? 30.094 -0.030  38.800 1.000 6.20  ? 126  ASN A CA   1 
ATOM   1607 C  C    . ASN A 1 126 ? 30.319 -0.142  40.291 1.000 6.04  ? 126  ASN A C    1 
ATOM   1608 O  O    . ASN A 1 126 ? 31.455 -0.383  40.746 1.000 6.87  ? 126  ASN A O    1 
ATOM   1609 C  CB   . ASN A 1 126 ? 30.062 1.442   38.400 1.000 6.76  ? 126  ASN A CB   1 
ATOM   1610 C  CG   . ASN A 1 126 ? 30.052 1.674   36.937 1.000 7.55  ? 126  ASN A CG   1 
ATOM   1611 O  OD1  . ASN A 1 126 ? 30.382 0.785   36.121 1.000 8.57  ? 126  ASN A OD1  1 
ATOM   1612 N  ND2  . ASN A 1 126 ? 29.722 2.904   36.536 1.000 9.89  ? 126  ASN A ND2  1 
ATOM   1613 H  H    . ASN A 1 126 ? 28.239 -0.286  38.013 1.000 7.02  ? 126  ASN A H    1 
ATOM   1614 H  HA   . ASN A 1 126 ? 30.849 -0.456  38.343 1.000 7.44  ? 126  ASN A HA   1 
ATOM   1615 H  HB3  . ASN A 1 126 ? 30.834 1.891   38.780 1.000 8.12  ? 126  ASN A HB3  1 
ATOM   1616 N  N    . ILE A 1 127 ? 29.262 0.080   41.080 1.000 6.00  ? 127  ILE A N    1 
ATOM   1617 C  CA   . ILE A 1 127 ? 29.414 0.010   42.527 1.000 5.98  ? 127  ILE A CA   1 
ATOM   1618 C  C    . ILE A 1 127 ? 29.684 -1.426  42.974 1.000 5.95  ? 127  ILE A C    1 
ATOM   1619 O  O    . ILE A 1 127 ? 30.706 -1.647  43.679 1.000 6.83  ? 127  ILE A O    1 
ATOM   1620 C  CB   A ILE A 1 127 ? 28.259 0.701   43.275 0.513 5.86  ? 127  ILE A CB   1 
ATOM   1621 C  CB   B ILE A 1 127 ? 28.154 0.574   43.234 0.487 6.16  ? 127  ILE A CB   1 
ATOM   1622 C  CG1  A ILE A 1 127 ? 28.278 2.224   42.930 0.513 6.34  ? 127  ILE A CG1  1 
ATOM   1623 C  CG1  B ILE A 1 127 ? 28.076 2.096   42.958 0.487 7.02  ? 127  ILE A CG1  1 
ATOM   1624 C  CG2  A ILE A 1 127 ? 28.350 0.459   44.758 0.513 5.99  ? 127  ILE A CG2  1 
ATOM   1625 C  CG2  B ILE A 1 127 ? 28.127 0.230   44.697 0.487 6.47  ? 127  ILE A CG2  1 
ATOM   1626 C  CD1  A ILE A 1 127 ? 26.934 2.898   43.118 0.513 6.00  ? 127  ILE A CD1  1 
ATOM   1627 C  CD1  B ILE A 1 127 ? 29.315 2.826   43.363 0.487 7.60  ? 127  ILE A CD1  1 
ATOM   1628 H  HA   A ILE A 1 127 ? 30.223 0.520   42.742 1.000 7.18  ? 127  ILE A HA   1 
ATOM   1629 H  HB   A ILE A 1 127 ? 27.414 0.323   42.953 0.513 7.03  ? 127  ILE A HB   1 
ATOM   1630 H  HB   B ILE A 1 127 ? 27.371 0.157   42.818 0.487 7.39  ? 127  ILE A HB   1 
ATOM   1631 H  HG21 A ILE A 1 127 ? 28.315 -0.484  44.936 0.513 8.98  ? 127  ILE A HG21 1 
ATOM   1632 H  HG21 B ILE A 1 127 ? 28.181 -0.724  44.785 0.487 9.70  ? 127  ILE A HG21 1 
ATOM   1633 H  HG22 A ILE A 1 127 ? 29.171 0.819   45.101 0.513 8.98  ? 127  ILE A HG22 1 
ATOM   1634 H  HG22 B ILE A 1 127 ? 28.893 0.634   45.110 0.487 9.70  ? 127  ILE A HG22 1 
ATOM   1635 N  N    . PRO A 1 128 ? 28.861 -2.439  42.657 1.000 5.90  ? 128  PRO A N    1 
ATOM   1636 C  CA   . PRO A 1 128 ? 29.145 -3.783  43.206 1.000 6.24  ? 128  PRO A CA   1 
ATOM   1637 C  C    . PRO A 1 128 ? 30.471 -4.349  42.683 1.000 6.21  ? 128  PRO A C    1 
ATOM   1638 O  O    . PRO A 1 128 ? 31.249 -4.919  43.465 1.000 7.03  ? 128  PRO A O    1 
ATOM   1639 C  CB   . PRO A 1 128 ? 27.947 -4.614  42.794 1.000 6.95  ? 128  PRO A CB   1 
ATOM   1640 C  CG   . PRO A 1 128 ? 27.362 -3.853  41.629 1.000 6.43  ? 128  PRO A CG   1 
ATOM   1641 C  CD   . PRO A 1 128 ? 27.549 -2.411  41.982 1.000 5.95  ? 128  PRO A CD   1 
ATOM   1642 H  HA   . PRO A 1 128 ? 29.180 -3.731  44.184 1.000 7.49  ? 128  PRO A HA   1 
ATOM   1643 H  HB3  . PRO A 1 128 ? 27.311 -4.677  43.524 1.000 8.35  ? 128  PRO A HB3  1 
ATOM   1644 H  HG2  . PRO A 1 128 ? 27.830 -4.069  40.807 1.000 7.71  ? 128  PRO A HG2  1 
ATOM   1645 H  HG3  . PRO A 1 128 ? 26.421 -4.062  41.519 1.000 7.71  ? 128  PRO A HG3  1 
ATOM   1646 H  HD2  . PRO A 1 128 ? 27.569 -1.851  41.190 1.000 7.14  ? 128  PRO A HD2  1 
ATOM   1647 H  HD3  . PRO A 1 128 ? 26.850 -2.098  42.578 1.000 7.14  ? 128  PRO A HD3  1 
ATOM   1648 N  N    . ILE A 1 129 ? 30.711 -4.231  41.385 1.000 6.29  ? 129  ILE A N    1 
ATOM   1649 C  CA   . ILE A 1 129 ? 31.952 -4.814  40.836 1.000 6.57  ? 129  ILE A CA   1 
ATOM   1650 C  C    . ILE A 1 129 ? 33.167 -4.056  41.313 1.000 6.90  ? 129  ILE A C    1 
ATOM   1651 O  O    . ILE A 1 129 ? 34.162 -4.658  41.735 1.000 8.13  ? 129  ILE A O    1 
ATOM   1652 C  CB   . ILE A 1 129 ? 31.873 -4.928  39.305 1.000 6.73  ? 129  ILE A CB   1 
ATOM   1653 C  CG1  . ILE A 1 129 ? 30.662 -5.792  38.878 1.000 7.19  ? 129  ILE A CG1  1 
ATOM   1654 C  CG2  . ILE A 1 129 ? 33.146 -5.515  38.748 1.000 7.97  ? 129  ILE A CG2  1 
ATOM   1655 C  CD1  . ILE A 1 129 ? 30.512 -7.127  39.573 1.000 7.51  ? 129  ILE A CD1  1 
ATOM   1656 H  HA   . ILE A 1 129 ? 32.023 -5.725  41.190 1.000 7.89  ? 129  ILE A HA   1 
ATOM   1657 H  HB   . ILE A 1 129 ? 31.758 -4.028  38.933 1.000 8.08  ? 129  ILE A HB   1 
ATOM   1658 H  HG12 . ILE A 1 129 ? 29.854 -5.278  39.032 1.000 8.63  ? 129  ILE A HG12 1 
ATOM   1659 H  HG13 . ILE A 1 129 ? 30.726 -5.952  37.923 1.000 8.63  ? 129  ILE A HG13 1 
ATOM   1660 H  HG21 . ILE A 1 129 ? 33.084 -5.587  37.793 1.000 11.95 ? 129  ILE A HG21 1 
ATOM   1661 H  HG22 . ILE A 1 129 ? 33.871 -4.930  38.979 1.000 11.95 ? 129  ILE A HG22 1 
ATOM   1662 H  HD11 . ILE A 1 129 ? 29.738 -7.588  39.241 1.000 11.26 ? 129  ILE A HD11 1 
ATOM   1663 H  HD13 . ILE A 1 129 ? 30.414 -6.976  40.516 1.000 11.26 ? 129  ILE A HD13 1 
ATOM   1664 N  N    . GLY A 1 130 ? 33.127 -2.721  41.294 1.000 7.46  ? 130  GLY A N    1 
ATOM   1665 C  CA   . GLY A 1 130 ? 34.251 -1.968  41.791 1.000 8.48  ? 130  GLY A CA   1 
ATOM   1666 C  C    . GLY A 1 130 ? 34.502 -2.259  43.234 1.000 8.40  ? 130  GLY A C    1 
ATOM   1667 O  O    . GLY A 1 130 ? 35.678 -2.345  43.674 1.000 10.39 ? 130  GLY A O    1 
ATOM   1668 H  H    . GLY A 1 130 ? 32.434 -2.314  40.987 1.000 8.95  ? 130  GLY A H    1 
ATOM   1669 H  HA3  . GLY A 1 130 ? 34.070 -1.020  41.687 1.000 10.18 ? 130  GLY A HA3  1 
ATOM   1670 N  N    . THR A 1 131 ? 33.479 -2.440  44.036 1.000 8.07  ? 131  THR A N    1 
ATOM   1671 C  CA   . THR A 1 131 ? 33.647 -2.778  45.427 1.000 8.76  ? 131  THR A CA   1 
ATOM   1672 C  C    . THR A 1 131 ? 34.290 -4.143  45.618 1.000 8.50  ? 131  THR A C    1 
ATOM   1673 O  O    . THR A 1 131 ? 35.182 -4.318  46.433 1.000 10.10 ? 131  THR A O    1 
ATOM   1674 C  CB   . THR A 1 131 ? 32.275 -2.747  46.152 1.000 9.82  ? 131  THR A CB   1 
ATOM   1675 O  OG1  . THR A 1 131 ? 31.771 -1.393  46.136 1.000 11.17 ? 131  THR A OG1  1 
ATOM   1676 C  CG2  . THR A 1 131 ? 32.401 -3.180  47.595 1.000 11.73 ? 131  THR A CG2  1 
ATOM   1677 H  H    . THR A 1 131 ? 32.683 -2.353  43.722 1.000 9.69  ? 131  THR A H    1 
ATOM   1678 H  HA   . THR A 1 131 ? 34.227 -2.104  45.839 1.000 10.51 ? 131  THR A HA   1 
ATOM   1679 H  HB   . THR A 1 131 ? 31.646 -3.337  45.687 1.000 11.78 ? 131  THR A HB   1 
ATOM   1680 H  HG22 . THR A 1 131 ? 33.011 -2.594  48.049 1.000 17.59 ? 131  THR A HG22 1 
ATOM   1681 N  N    . LEU A 1 132 ? 33.804 -5.125  44.871 1.000 8.10  ? 132  LEU A N    1 
ATOM   1682 C  CA   . LEU A 1 132 ? 34.365 -6.479  44.997 1.000 8.44  ? 132  LEU A CA   1 
ATOM   1683 C  C    . LEU A 1 132 ? 35.784 -6.532  44.506 1.000 9.22  ? 132  LEU A C    1 
ATOM   1684 O  O    . LEU A 1 132 ? 36.598 -7.303  45.064 1.000 10.91 ? 132  LEU A O    1 
ATOM   1685 C  CB   . LEU A 1 132 ? 33.461 -7.469  44.248 1.000 8.94  ? 132  LEU A CB   1 
ATOM   1686 C  CG   . LEU A 1 132 ? 32.131 -7.702  44.961 1.000 9.03  ? 132  LEU A CG   1 
ATOM   1687 C  CD1  . LEU A 1 132 ? 31.160 -8.404  44.009 1.000 11.69 ? 132  LEU A CD1  1 
ATOM   1688 C  CD2  . LEU A 1 132 ? 32.335 -8.505  46.268 1.000 11.68 ? 132  LEU A CD2  1 
ATOM   1689 H  H    . LEU A 1 132 ? 33.165 -4.971  44.317 1.000 9.72  ? 132  LEU A H    1 
ATOM   1690 H  HA   . LEU A 1 132 ? 34.362 -6.723  45.946 1.000 10.12 ? 132  LEU A HA   1 
ATOM   1691 H  HB3  . LEU A 1 132 ? 33.931 -8.315  44.181 1.000 10.73 ? 132  LEU A HB3  1 
ATOM   1692 H  HG   . LEU A 1 132 ? 31.753 -6.828  45.195 1.000 10.84 ? 132  LEU A HG   1 
ATOM   1693 H  HD23 . LEU A 1 132 ? 32.186 -9.437  46.094 1.000 17.52 ? 132  LEU A HD23 1 
ATOM   1694 N  N    . ILE A 1 133 ? 36.145 -5.752  43.498 1.000 9.34  ? 133  ILE A N    1 
ATOM   1695 C  CA   . ILE A 1 133 ? 37.579 -5.629  43.103 1.000 11.24 ? 133  ILE A CA   1 
ATOM   1696 C  C    . ILE A 1 133 ? 38.379 -5.013  44.230 1.000 11.83 ? 133  ILE A C    1 
ATOM   1697 O  O    . ILE A 1 133 ? 39.433 -5.487  44.668 1.000 14.42 ? 133  ILE A O    1 
ATOM   1698 C  CB   . ILE A 1 133 ? 37.715 -4.818  41.820 1.000 11.20 ? 133  ILE A CB   1 
ATOM   1699 C  CG1  . ILE A 1 133 ? 37.117 -5.602  40.642 1.000 11.07 ? 133  ILE A CG1  1 
ATOM   1700 C  CG2  . ILE A 1 133 ? 39.170 -4.383  41.619 1.000 14.19 ? 133  ILE A CG2  1 
ATOM   1701 C  CD1  . ILE A 1 133 ? 36.955 -4.746  39.385 1.000 12.80 ? 133  ILE A CD1  1 
ATOM   1702 H  HD11 . ILE A 1 133 ? 36.584 -5.285  38.682 1.000 19.21 ? 133  ILE A HD11 1 
ATOM   1703 N  N    . HIS A 1 134 ? 37.877 -3.924  44.825 1.000 11.77 ? 134  HIS A N    1 
ATOM   1704 C  CA   . HIS A 1 134 ? 38.610 -3.245  45.892 1.000 13.94 ? 134  HIS A CA   1 
ATOM   1705 C  C    . HIS A 1 134 ? 38.806 -4.151  47.101 1.000 16.19 ? 134  HIS A C    1 
ATOM   1706 O  O    . HIS A 1 134 ? 39.878 -4.163  47.752 1.000 18.36 ? 134  HIS A O    1 
ATOM   1707 C  CB   . HIS A 1 134 ? 37.828 -1.982  46.320 1.000 16.67 ? 134  HIS A CB   1 
ATOM   1708 C  CG   . HIS A 1 134 ? 38.454 -1.260  47.424 1.000 23.18 ? 134  HIS A CG   1 
ATOM   1709 N  ND1  . HIS A 1 134 ? 38.050 -1.235  48.731 1.000 28.38 ? 134  HIS A ND1  1 
ATOM   1710 C  CD2  . HIS A 1 134 ? 39.553 -0.475  47.313 1.000 31.98 ? 134  HIS A CD2  1 
ATOM   1711 C  CE1  . HIS A 1 134 ? 38.867 -0.473  49.403 1.000 36.71 ? 134  HIS A CE1  1 
ATOM   1712 N  NE2  . HIS A 1 134 ? 39.782 -0.006  48.565 1.000 38.59 ? 134  HIS A NE2  1 
ATOM   1713 N  N    . ARG A 1 135 ? 37.832 -4.967  47.416 1.000 12.79 ? 135  ARG A N    1 
ATOM   1714 C  CA   . ARG A 1 135 ? 37.912 -5.929  48.524 1.000 15.43 ? 135  ARG A CA   1 
ATOM   1715 C  C    . ARG A 1 135 ? 38.785 -7.141  48.236 1.000 17.04 ? 135  ARG A C    1 
ATOM   1716 O  O    . ARG A 1 135 ? 39.069 -7.927  49.143 1.000 19.17 ? 135  ARG A O    1 
ATOM   1717 C  CB   . ARG A 1 135 ? 36.511 -6.441  48.853 1.000 14.56 ? 135  ARG A CB   1 
ATOM   1718 C  CG   . ARG A 1 135 ? 35.567 -5.393  49.454 1.000 15.01 ? 135  ARG A CG   1 
ATOM   1719 C  CD   . ARG A 1 135 ? 34.150 -5.838  49.600 1.000 17.91 ? 135  ARG A CD   1 
ATOM   1720 N  NE   . ARG A 1 135 ? 34.005 -6.872  50.615 1.000 18.00 ? 135  ARG A NE   1 
ATOM   1721 C  CZ   . ARG A 1 135 ? 33.658 -6.698  51.882 1.000 18.18 ? 135  ARG A CZ   1 
ATOM   1722 N  NH1  . ARG A 1 135 ? 33.419 -5.479  52.314 1.000 20.50 ? 135  ARG A NH1  1 
ATOM   1723 N  NH2  . ARG A 1 135 ? 33.552 -7.761  52.691 1.000 26.22 ? 135  ARG A NH2  1 
ATOM   1724 H  HG3  . ARG A 1 135 ? 35.593 -4.620  48.869 1.000 18.01 ? 135  ARG A HG3  1 
ATOM   1725 H  HH21 . ARG A 1 135 ? 33.340 -7.627  53.514 1.000 31.46 ? 135  ARG A HH21 1 
ATOM   1726 N  N    . GLY A 1 136 ? 39.245 -7.245  46.975 1.000 15.49 ? 136  GLY A N    1 
ATOM   1727 C  CA   . GLY A 1 136 ? 40.027 -8.424  46.670 1.000 18.16 ? 136  GLY A CA   1 
ATOM   1728 C  C    . GLY A 1 136 ? 39.274 -9.697  46.379 1.000 17.66 ? 136  GLY A C    1 
ATOM   1729 O  O    . GLY A 1 136 ? 39.877 -10.741 46.167 1.000 19.02 ? 136  GLY A O    1 
ATOM   1730 N  N    . ALA A 1 137 ? 37.958 -9.616  46.316 1.000 13.41 ? 137  ALA A N    1 
ATOM   1731 C  CA   . ALA A 1 137 ? 37.156 -10.754 45.957 1.000 13.83 ? 137  ALA A CA   1 
ATOM   1732 C  C    . ALA A 1 137 ? 37.282 -11.074 44.470 1.000 13.72 ? 137  ALA A C    1 
ATOM   1733 O  O    . ALA A 1 137 ? 37.335 -12.223 44.093 1.000 15.09 ? 137  ALA A O    1 
ATOM   1734 C  CB   . ALA A 1 137 ? 35.715 -10.467 46.366 1.000 14.00 ? 137  ALA A CB   1 
ATOM   1735 H  H    . ALA A 1 137 ? 37.573 -8.868  46.492 1.000 16.09 ? 137  ALA A H    1 
ATOM   1736 H  HB1  . ALA A 1 137 ? 35.161 -11.211 46.115 1.000 20.99 ? 137  ALA A HB1  1 
ATOM   1737 N  N    . ILE A 1 138 ? 37.285 -10.026 43.652 1.000 14.14 ? 138  ILE A N    1 
ATOM   1738 C  CA   . ILE A 1 138 ? 37.429 -10.151 42.191 1.000 15.18 ? 138  ILE A CA   1 
ATOM   1739 C  C    . ILE A 1 138 ? 38.824 -9.642  41.841 1.000 16.24 ? 138  ILE A C    1 
ATOM   1740 O  O    . ILE A 1 138 ? 39.162 -8.522  42.206 1.000 16.56 ? 138  ILE A O    1 
ATOM   1741 C  CB   . ILE A 1 138 ? 36.347 -9.385  41.414 1.000 12.25 ? 138  ILE A CB   1 
ATOM   1742 C  CG1  . ILE A 1 138 ? 34.999 -9.962  41.696 1.000 13.05 ? 138  ILE A CG1  1 
ATOM   1743 C  CG2  . ILE A 1 138 ? 36.770 -9.334  39.930 1.000 17.05 ? 138  ILE A CG2  1 
ATOM   1744 C  CD1  . ILE A 1 138 ? 33.859 -9.271  41.021 1.000 13.49 ? 138  ILE A CD1  1 
ATOM   1745 H  H    . ILE A 1 138 ? 37.198 -9.240  43.990 1.000 16.97 ? 138  ILE A H    1 
ATOM   1746 H  HB   . ILE A 1 138 ? 36.346 -8.464  41.748 1.000 14.70 ? 138  ILE A HB   1 
ATOM   1747 H  HD12 . ILE A 1 138 ? 33.822 -8.374  41.363 1.000 20.23 ? 138  ILE A HD12 1 
ATOM   1748 N  N    . GLU A 1 139 ? 39.518 -10.544 41.197 1.000 22.65 ? 139  GLU A N    1 
ATOM   1749 C  CA   . GLU A 1 139 ? 40.947 -10.235 41.020 1.000 23.03 ? 139  GLU A CA   1 
ATOM   1750 C  C    . GLU A 1 139 ? 40.998 -9.563  39.691 1.000 20.50 ? 139  GLU A C    1 
ATOM   1751 O  O    . GLU A 1 139 ? 40.482 -10.080 38.721 1.000 28.10 ? 139  GLU A O    1 
ATOM   1752 C  CB   A GLU A 1 139 ? 41.783 -11.509 41.151 0.324 32.65 ? 139  GLU A CB   1 
ATOM   1753 C  CB   B GLU A 1 139 ? 41.717 -11.541 41.115 0.676 32.49 ? 139  GLU A CB   1 
ATOM   1754 C  CG   A GLU A 1 139 ? 41.570 -12.182 42.504 0.324 34.26 ? 139  GLU A CG   1 
ATOM   1755 C  CG   B GLU A 1 139 ? 41.260 -12.683 41.927 0.676 39.47 ? 139  GLU A CG   1 
ATOM   1756 C  CD   A GLU A 1 139 ? 42.245 -13.538 42.640 0.324 41.66 ? 139  GLU A CD   1 
ATOM   1757 C  CD   B GLU A 1 139 ? 40.012 -13.107 42.607 0.676 41.21 ? 139  GLU A CD   1 
ATOM   1758 O  OE1  A GLU A 1 139 ? 43.365 -13.719 42.109 0.324 55.01 ? 139  GLU A OE1  1 
ATOM   1759 O  OE1  B GLU A 1 139 ? 39.967 -13.126 43.863 0.676 43.96 ? 139  GLU A OE1  1 
ATOM   1760 O  OE2  A GLU A 1 139 ? 41.644 -14.406 43.307 0.324 43.54 ? 139  GLU A OE2  1 
ATOM   1761 O  OE2  B GLU A 1 139 ? 39.029 -13.412 41.874 0.676 40.06 ? 139  GLU A OE2  1 
ATOM   1762 N  N    . TRP A 1 140 ? 41.507 -8.351  39.722 1.000 20.94 ? 140  TRP A N    1 
ATOM   1763 C  CA   . TRP A 1 140 ? 41.579 -7.611  38.450 1.000 19.02 ? 140  TRP A CA   1 
ATOM   1764 C  C    . TRP A 1 140 ? 42.603 -6.488  38.498 1.000 19.56 ? 140  TRP A C    1 
ATOM   1765 O  O    . TRP A 1 140 ? 42.457 -5.534  39.199 1.000 25.32 ? 140  TRP A O    1 
ATOM   1766 C  CB   . TRP A 1 140 ? 40.215 -7.075  38.089 1.000 20.44 ? 140  TRP A CB   1 
ATOM   1767 C  CG   . TRP A 1 140 ? 40.167 -6.467  36.696 1.000 18.13 ? 140  TRP A CG   1 
ATOM   1768 C  CD1  . TRP A 1 140 ? 40.210 -7.118  35.495 1.000 19.45 ? 140  TRP A CD1  1 
ATOM   1769 C  CD2  . TRP A 1 140 ? 40.076 -5.051  36.418 1.000 18.08 ? 140  TRP A CD2  1 
ATOM   1770 N  NE1  . TRP A 1 140 ? 40.147 -6.193  34.459 1.000 18.10 ? 140  TRP A NE1  1 
ATOM   1771 C  CE2  . TRP A 1 140 ? 40.047 -4.933  35.004 1.000 17.34 ? 140  TRP A CE2  1 
ATOM   1772 C  CE3  . TRP A 1 140 ? 39.988 -3.927  37.217 1.000 16.09 ? 140  TRP A CE3  1 
ATOM   1773 C  CZ2  . TRP A 1 140 ? 39.943 -3.697  34.351 1.000 20.45 ? 140  TRP A CZ2  1 
ATOM   1774 C  CZ3  . TRP A 1 140 ? 39.879 -2.705  36.564 1.000 19.93 ? 140  TRP A CZ3  1 
ATOM   1775 C  CH2  . TRP A 1 140 ? 39.859 -2.594  35.174 1.000 19.14 ? 140  TRP A CH2  1 
ATOM   1776 H  HA   . TRP A 1 140 ? 41.852 -8.239  37.749 1.000 22.83 ? 140  TRP A HA   1 
ATOM   1777 H  HE1  . TRP A 1 140 ? 40.167 -6.377  33.619 1.000 21.72 ? 140  TRP A HE1  1 
ATOM   1778 N  N    . GLU A 1 141 ? 43.673 -6.688  37.705 1.000 19.01 ? 141  GLU A N    1 
ATOM   1779 C  CA   A GLU A 1 141 ? 44.806 -5.785  37.811 0.687 17.42 ? 141  GLU A CA   1 
ATOM   1780 C  CA   B GLU A 1 141 ? 44.814 -5.786  37.825 0.313 17.60 ? 141  GLU A CA   1 
ATOM   1781 C  C    . GLU A 1 141 ? 44.663 -4.671  36.793 1.000 21.72 ? 141  GLU A C    1 
ATOM   1782 O  O    . GLU A 1 141 ? 45.645 -3.883  36.748 1.000 31.02 ? 141  GLU A O    1 
ATOM   1783 C  CB   A GLU A 1 141 ? 46.178 -6.478  37.647 0.687 18.25 ? 141  GLU A CB   1 
ATOM   1784 C  CB   B GLU A 1 141 ? 46.163 -6.488  37.721 0.313 18.72 ? 141  GLU A CB   1 
ATOM   1785 C  CG   A GLU A 1 141 ? 46.524 -7.308  38.866 0.687 18.60 ? 141  GLU A CG   1 
ATOM   1786 C  CG   B GLU A 1 141 ? 46.778 -6.808  36.384 0.313 22.28 ? 141  GLU A CG   1 
ATOM   1787 C  CD   A GLU A 1 141 ? 47.827 -8.052  38.905 0.687 21.61 ? 141  GLU A CD   1 
ATOM   1788 C  CD   B GLU A 1 141 ? 47.925 -7.806  36.417 0.313 25.52 ? 141  GLU A CD   1 
ATOM   1789 O  OE1  A GLU A 1 141 ? 48.728 -7.766  38.132 0.687 22.04 ? 141  GLU A OE1  1 
ATOM   1790 O  OE1  B GLU A 1 141 ? 48.310 -8.183  37.552 0.313 26.18 ? 141  GLU A OE1  1 
ATOM   1791 O  OE2  A GLU A 1 141 ? 47.980 -8.957  39.751 0.687 26.89 ? 141  GLU A OE2  1 
ATOM   1792 O  OE2  B GLU A 1 141 ? 48.455 -8.235  35.372 0.313 15.00 ? 141  GLU A OE2  1 
ATOM   1793 N  N    . GLY A 1 142 ? 43.574 -4.523  36.037 1.000 19.09 ? 142  GLY A N    1 
ATOM   1794 C  CA   . GLY A 1 142 ? 43.380 -3.411  35.144 1.000 19.67 ? 142  GLY A CA   1 
ATOM   1795 C  C    . GLY A 1 142 ? 43.144 -3.867  33.738 1.000 20.23 ? 142  GLY A C    1 
ATOM   1796 O  O    . GLY A 1 142 ? 43.193 -5.014  33.352 1.000 19.47 ? 142  GLY A O    1 
ATOM   1797 N  N    . ILE A 1 143 ? 42.738 -2.881  32.971 1.000 20.04 ? 143  ILE A N    1 
ATOM   1798 C  CA   . ILE A 1 143 ? 42.191 -3.177  31.643 1.000 18.70 ? 143  ILE A CA   1 
ATOM   1799 C  C    . ILE A 1 143 ? 43.138 -3.918  30.759 1.000 19.45 ? 143  ILE A C    1 
ATOM   1800 O  O    . ILE A 1 143 ? 42.769 -4.731  29.893 1.000 19.37 ? 143  ILE A O    1 
ATOM   1801 C  CB   . ILE A 1 143 ? 41.667 -1.862  31.009 1.000 22.67 ? 143  ILE A CB   1 
ATOM   1802 C  CG1  . ILE A 1 143 ? 40.578 -1.993  29.924 1.000 26.74 ? 143  ILE A CG1  1 
ATOM   1803 C  CG2  . ILE A 1 143 ? 42.879 -1.032  30.583 1.000 28.26 ? 143  ILE A CG2  1 
ATOM   1804 C  CD1  . ILE A 1 143 ? 39.429 -2.946  30.289 1.000 28.21 ? 143  ILE A CD1  1 
ATOM   1805 N  N    . GLU A 1 144 ? 44.439 -3.678  30.954 1.000 19.29 ? 144  GLU A N    1 
ATOM   1806 C  CA   . GLU A 1 144 ? 45.371 -4.308  30.075 1.000 21.88 ? 144  GLU A CA   1 
ATOM   1807 C  C    . GLU A 1 144 ? 45.432 -5.827  30.356 1.000 21.03 ? 144  GLU A C    1 
ATOM   1808 O  O    . GLU A 1 144 ? 45.806 -6.538  29.419 1.000 23.89 ? 144  GLU A O    1 
ATOM   1809 C  CB   . GLU A 1 144 ? 46.795 -3.743  30.251 1.000 23.90 ? 144  GLU A CB   1 
ATOM   1810 C  CG   . GLU A 1 144 ? 46.876 -2.216  30.124 1.000 24.67 ? 144  GLU A CG   1 
ATOM   1811 C  CD   . GLU A 1 144 ? 46.580 -1.436  31.381 1.000 22.47 ? 144  GLU A CD   1 
ATOM   1812 O  OE1  . GLU A 1 144 ? 46.053 -1.960  32.409 1.000 28.03 ? 144  GLU A OE1  1 
ATOM   1813 O  OE2  . GLU A 1 144 ? 46.876 -0.217  31.340 1.000 26.13 ? 144  GLU A OE2  1 
ATOM   1814 N  N    . SER A 1 145 ? 45.148 -6.231  31.575 1.000 19.28 ? 145  SER A N    1 
ATOM   1815 C  CA   . SER A 1 145 ? 45.213 -7.639  31.975 1.000 20.60 ? 145  SER A CA   1 
ATOM   1816 C  C    . SER A 1 145 ? 44.029 -8.381  31.350 1.000 20.32 ? 145  SER A C    1 
ATOM   1817 O  O    . SER A 1 145 ? 44.043 -9.603  31.300 1.000 24.72 ? 145  SER A O    1 
ATOM   1818 C  CB   . SER A 1 145 ? 45.197 -7.797  33.516 1.000 22.13 ? 145  SER A CB   1 
ATOM   1819 O  OG   . SER A 1 145 ? 43.943 -7.427  34.089 1.000 21.54 ? 145  SER A OG   1 
ATOM   1820 H  HA   . SER A 1 145 ? 46.044 -8.026  31.628 1.000 24.71 ? 145  SER A HA   1 
ATOM   1821 N  N    . GLY A 1 146 ? 42.951 -7.744  30.912 1.000 18.29 ? 146  GLY A N    1 
ATOM   1822 C  CA   . GLY A 1 146 ? 41.774 -8.447  30.481 1.000 16.26 ? 146  GLY A CA   1 
ATOM   1823 C  C    . GLY A 1 146 ? 40.519 -7.622  30.866 1.000 12.96 ? 146  GLY A C    1 
ATOM   1824 O  O    . GLY A 1 146 ? 40.603 -6.657  31.646 1.000 14.96 ? 146  GLY A O    1 
ATOM   1825 N  N    . SER A 1 147 ? 39.370 -7.991  30.333 1.000 12.49 ? 147  SER A N    1 
ATOM   1826 C  CA   . SER A 1 147 ? 38.174 -7.175  30.573 1.000 11.33 ? 147  SER A CA   1 
ATOM   1827 C  C    . SER A 1 147 ? 37.624 -7.373  31.970 1.000 9.67  ? 147  SER A C    1 
ATOM   1828 O  O    . SER A 1 147 ? 37.806 -8.377  32.659 1.000 10.78 ? 147  SER A O    1 
ATOM   1829 C  CB   . SER A 1 147 ? 37.086 -7.576  29.570 1.000 11.64 ? 147  SER A CB   1 
ATOM   1830 O  OG   . SER A 1 147 ? 36.623 -8.859  29.758 1.000 12.69 ? 147  SER A OG   1 
ATOM   1831 H  HA   . SER A 1 147 ? 38.397 -6.229  30.445 1.000 13.59 ? 147  SER A HA   1 
ATOM   1832 H  HB3  . SER A 1 147 ? 37.408 -7.381  28.676 1.000 13.97 ? 147  SER A HB3  1 
ATOM   1833 N  N    . VAL A 1 148 ? 36.864 -6.383  32.393 1.000 9.78  ? 148  VAL A N    1 
ATOM   1834 C  CA   . VAL A 1 148 ? 36.127 -6.502  33.642 1.000 8.73  ? 148  VAL A CA   1 
ATOM   1835 C  C    . VAL A 1 148 ? 35.117 -7.633  33.551 1.000 8.37  ? 148  VAL A C    1 
ATOM   1836 O  O    . VAL A 1 148 ? 34.974 -8.429  34.485 1.000 8.98  ? 148  VAL A O    1 
ATOM   1837 C  CB   . VAL A 1 148 ? 35.457 -5.148  34.026 1.000 9.88  ? 148  VAL A CB   1 
ATOM   1838 C  CG1  . VAL A 1 148 ? 34.655 -5.296  35.299 1.000 10.92 ? 148  VAL A CG1  1 
ATOM   1839 C  CG2  . VAL A 1 148 ? 36.485 -4.069  34.209 1.000 11.59 ? 148  VAL A CG2  1 
ATOM   1840 H  H    . VAL A 1 148 ? 36.803 -5.662  31.928 1.000 11.74 ? 148  VAL A H    1 
ATOM   1841 H  HA   . VAL A 1 148 ? 36.768 -6.729  34.348 1.000 10.48 ? 148  VAL A HA   1 
ATOM   1842 H  HG12 . VAL A 1 148 ? 35.242 -5.526  36.023 1.000 16.38 ? 148  VAL A HG12 1 
ATOM   1843 H  HG23 . VAL A 1 148 ? 37.069 -4.301  34.935 1.000 17.39 ? 148  VAL A HG23 1 
ATOM   1844 N  N    A GLU A 1 149 ? 34.415 -7.724  32.412 0.601 9.19  ? 149  GLU A N    1 
ATOM   1845 N  N    B GLU A 1 149 ? 34.434 -7.735  32.396 0.399 7.44  ? 149  GLU A N    1 
ATOM   1846 C  CA   . GLU A 1 149 ? 33.453 -8.801  32.219 1.000 7.57  ? 149  GLU A CA   1 
ATOM   1847 C  C    A GLU A 1 149 ? 34.103 -10.161 32.494 0.601 7.61  ? 149  GLU A C    1 
ATOM   1848 C  C    B GLU A 1 149 ? 34.067 -10.170 32.460 0.399 9.09  ? 149  GLU A C    1 
ATOM   1849 O  O    A GLU A 1 149 ? 33.518 -10.980 33.169 0.601 9.33  ? 149  GLU A O    1 
ATOM   1850 O  O    B GLU A 1 149 ? 33.453 -11.030 33.072 0.399 9.20  ? 149  GLU A O    1 
ATOM   1851 C  CB   A GLU A 1 149 ? 32.912 -8.851  30.794 0.601 8.52  ? 149  GLU A CB   1 
ATOM   1852 C  CB   B GLU A 1 149 ? 32.802 -8.736  30.836 0.399 7.63  ? 149  GLU A CB   1 
ATOM   1853 C  CG   A GLU A 1 149 ? 31.813 -7.812  30.507 0.601 7.57  ? 149  GLU A CG   1 
ATOM   1854 C  CG   B GLU A 1 149 ? 31.904 -7.505  30.717 0.399 13.89 ? 149  GLU A CG   1 
ATOM   1855 C  CD   A GLU A 1 149 ? 31.085 -8.148  29.215 0.601 9.10  ? 149  GLU A CD   1 
ATOM   1856 C  CD   B GLU A 1 149 ? 31.516 -7.036  29.349 0.399 13.42 ? 149  GLU A CD   1 
ATOM   1857 O  OE1  A GLU A 1 149 ? 30.845 -7.157  28.429 0.601 17.52 ? 149  GLU A OE1  1 
ATOM   1858 O  OE1  B GLU A 1 149 ? 31.863 -5.865  28.983 0.399 19.35 ? 149  GLU A OE1  1 
ATOM   1859 O  OE2  A GLU A 1 149 ? 30.754 -9.323  28.920 0.601 11.49 ? 149  GLU A OE2  1 
ATOM   1860 O  OE2  B GLU A 1 149 ? 30.855 -7.770  28.585 0.399 20.43 ? 149  GLU A OE2  1 
ATOM   1861 N  N    A GLN A 1 150 ? 35.307 -10.389 31.944 0.689 8.74  ? 150  GLN A N    1 
ATOM   1862 N  N    B GLN A 1 150 ? 35.284 -10.391 31.945 0.311 9.51  ? 150  GLN A N    1 
ATOM   1863 C  CA   A GLN A 1 150 ? 36.015 -11.654 32.116 0.689 10.62 ? 150  GLN A CA   1 
ATOM   1864 C  CA   B GLN A 1 150 ? 35.862 -11.740 32.131 0.311 11.42 ? 150  GLN A CA   1 
ATOM   1865 C  C    A GLN A 1 150 ? 36.238 -11.965 33.600 0.689 10.16 ? 150  GLN A C    1 
ATOM   1866 C  C    B GLN A 1 150 ? 36.163 -11.953 33.615 0.311 10.79 ? 150  GLN A C    1 
ATOM   1867 O  O    A GLN A 1 150 ? 36.044 -13.075 34.047 0.689 10.92 ? 150  GLN A O    1 
ATOM   1868 O  O    B GLN A 1 150 ? 35.892 -13.022 34.158 0.311 14.49 ? 150  GLN A O    1 
ATOM   1869 C  CB   A GLN A 1 150 ? 37.378 -11.578 31.438 0.689 10.93 ? 150  GLN A CB   1 
ATOM   1870 C  CB   B GLN A 1 150 ? 37.058 -11.912 31.194 0.311 14.12 ? 150  GLN A CB   1 
ATOM   1871 C  CG   A GLN A 1 150 ? 38.224 -12.832 31.648 0.689 12.81 ? 150  GLN A CG   1 
ATOM   1872 C  CG   B GLN A 1 150 ? 36.677 -12.592 29.903 0.311 19.91 ? 150  GLN A CG   1 
ATOM   1873 C  CD   A GLN A 1 150 ? 39.540 -12.655 30.903 0.689 16.50 ? 150  GLN A CD   1 
ATOM   1874 C  CD   B GLN A 1 150 ? 37.324 -12.297 28.584 0.311 15.49 ? 150  GLN A CD   1 
ATOM   1875 O  OE1  A GLN A 1 150 ? 40.362 -11.817 31.240 0.689 16.90 ? 150  GLN A OE1  1 
ATOM   1876 O  OE1  B GLN A 1 150 ? 37.263 -13.143 27.662 0.311 13.79 ? 150  GLN A OE1  1 
ATOM   1877 N  NE2  A GLN A 1 150 ? 39.738 -13.446 29.863 0.689 28.29 ? 150  GLN A NE2  1 
ATOM   1878 N  NE2  B GLN A 1 150 ? 37.924 -11.114 28.447 0.311 19.97 ? 150  GLN A NE2  1 
ATOM   1879 N  N    . ALA A 1 151 ? 36.670 -10.953 34.327 1.000 9.92  ? 151  ALA A N    1 
ATOM   1880 C  CA   . ALA A 1 151 ? 36.923 -11.120 35.757 1.000 10.66 ? 151  ALA A CA   1 
ATOM   1881 C  C    . ALA A 1 151 ? 35.632 -11.421 36.510 1.000 9.80  ? 151  ALA A C    1 
ATOM   1882 O  O    . ALA A 1 151 ? 35.602 -12.281 37.391 1.000 11.23 ? 151  ALA A O    1 
ATOM   1883 C  CB   . ALA A 1 151 ? 37.636 -9.920  36.343 1.000 13.02 ? 151  ALA A CB   1 
ATOM   1884 H  H    A ALA A 1 151 ? 36.805 -10.189 33.957 1.000 11.90 ? 151  ALA A H    1 
ATOM   1885 H  HB3  . ALA A 1 151 ? 37.005 -9.353  36.741 1.000 19.53 ? 151  ALA A HB3  1 
ATOM   1886 N  N    . VAL A 1 152 ? 34.528 -10.757 36.178 1.000 8.47  ? 152  VAL A N    1 
ATOM   1887 C  CA   . VAL A 1 152 ? 33.256 -11.017 36.867 1.000 8.42  ? 152  VAL A CA   1 
ATOM   1888 C  C    . VAL A 1 152 ? 32.739 -12.405 36.569 1.000 8.49  ? 152  VAL A C    1 
ATOM   1889 O  O    . VAL A 1 152 ? 32.246 -13.052 37.476 1.000 10.20 ? 152  VAL A O    1 
ATOM   1890 C  CB   . VAL A 1 152 ? 32.251 -9.899  36.475 1.000 7.91  ? 152  VAL A CB   1 
ATOM   1891 C  CG1  . VAL A 1 152 ? 30.882 -10.187 37.075 1.000 8.58  ? 152  VAL A CG1  1 
ATOM   1892 C  CG2  . VAL A 1 152 ? 32.780 -8.525  36.937 1.000 8.72  ? 152  VAL A CG2  1 
ATOM   1893 H  H    . VAL A 1 152 ? 34.558 -10.169 35.552 1.000 10.16 ? 152  VAL A H    1 
ATOM   1894 H  HA   . VAL A 1 152 ? 33.417 -10.954 37.832 1.000 10.11 ? 152  VAL A HA   1 
ATOM   1895 H  HB   . VAL A 1 152 ? 32.166 -9.886  35.499 1.000 9.49  ? 152  VAL A HB   1 
ATOM   1896 H  HG12 . VAL A 1 152 ? 30.984 -10.121 38.007 1.000 12.87 ? 152  VAL A HG12 1 
ATOM   1897 H  HG13 . VAL A 1 152 ? 30.266 -9.538  36.777 1.000 12.87 ? 152  VAL A HG13 1 
ATOM   1898 H  HG23 . VAL A 1 152 ? 33.108 -8.565  37.819 1.000 13.07 ? 152  VAL A HG23 1 
ATOM   1899 N  N    . ALA A 1 153 ? 32.869 -12.827 35.311 1.000 8.96  ? 153  ALA A N    1 
ATOM   1900 C  CA   . ALA A 1 153 ? 32.420 -14.168 34.902 1.000 10.46 ? 153  ALA A CA   1 
ATOM   1901 C  C    . ALA A 1 153 ? 33.224 -15.301 35.581 1.000 10.65 ? 153  ALA A C    1 
ATOM   1902 O  O    . ALA A 1 153 ? 32.737 -16.393 35.679 1.000 12.90 ? 153  ALA A O    1 
ATOM   1903 C  CB   . ALA A 1 153 ? 32.508 -14.290 33.391 1.000 11.99 ? 153  ALA A CB   1 
ATOM   1904 H  H    . ALA A 1 153 ? 33.221 -12.304 34.726 1.000 10.76 ? 153  ALA A H    1 
ATOM   1905 H  HA   . ALA A 1 153 ? 31.480 -14.265 35.160 1.000 12.55 ? 153  ALA A HA   1 
ATOM   1906 H  HB2  . ALA A 1 153 ? 31.803 -13.784 33.018 1.000 17.98 ? 153  ALA A HB2  1 
ATOM   1907 N  N    . LYS A 1 154 ? 34.428 -14.988 35.989 1.000 10.45 ? 154  LYS A N    1 
ATOM   1908 C  CA   . LYS A 1 154 ? 35.221 -15.962 36.758 1.000 11.94 ? 154  LYS A CA   1 
ATOM   1909 C  C    . LYS A 1 154 ? 34.770 -16.049 38.204 1.000 11.51 ? 154  LYS A C    1 
ATOM   1910 O  O    . LYS A 1 154 ? 35.054 -17.031 38.891 1.000 13.75 ? 154  LYS A O    1 
ATOM   1911 C  CB   . LYS A 1 154 ? 36.716 -15.595 36.718 1.000 13.30 ? 154  LYS A CB   1 
ATOM   1912 C  CG   . LYS A 1 154 ? 37.349 -15.855 35.389 1.000 17.96 ? 154  LYS A CG   1 
ATOM   1913 C  CD   . LYS A 1 154 ? 38.801 -15.457 35.453 1.000 22.14 ? 154  LYS A CD   1 
ATOM   1914 C  CE   . LYS A 1 154 ? 39.383 -15.751 34.079 1.000 22.19 ? 154  LYS A CE   1 
ATOM   1915 N  NZ   . LYS A 1 154 ? 40.684 -15.008 34.004 1.000 25.93 ? 154  LYS A NZ   1 
ATOM   1916 H  H    . LYS A 1 154 ? 34.756 -14.214 35.807 1.000 12.54 ? 154  LYS A H    1 
ATOM   1917 H  HB2  . LYS A 1 154 ? 36.815 -14.655 36.935 1.000 15.96 ? 154  LYS A HB2  1 
ATOM   1918 H  HB3  . LYS A 1 154 ? 37.184 -16.107 37.395 1.000 15.96 ? 154  LYS A HB3  1 
ATOM   1919 N  N    . PHE A 1 155 ? 34.123 -15.009 38.707 1.000 9.36  ? 155  PHE A N    1 
ATOM   1920 C  CA   . PHE A 1 155 ? 33.732 -14.884 40.087 1.000 9.36  ? 155  PHE A CA   1 
ATOM   1921 C  C    . PHE A 1 155 ? 32.337 -15.450 40.354 1.000 8.89  ? 155  PHE A C    1 
ATOM   1922 O  O    . PHE A 1 155 ? 32.165 -16.394 41.131 1.000 9.96  ? 155  PHE A O    1 
ATOM   1923 C  CB   . PHE A 1 155 ? 33.825 -13.409 40.507 1.000 9.77  ? 155  PHE A CB   1 
ATOM   1924 C  CG   . PHE A 1 155 ? 33.493 -13.201 41.969 1.000 9.15  ? 155  PHE A CG   1 
ATOM   1925 C  CD1  . PHE A 1 155 ? 34.368 -13.539 42.961 1.000 9.87  ? 155  PHE A CD1  1 
ATOM   1926 C  CD2  . PHE A 1 155 ? 32.275 -12.612 42.338 1.000 9.38  ? 155  PHE A CD2  1 
ATOM   1927 C  CE1  . PHE A 1 155 ? 34.118 -13.331 44.292 1.000 10.33 ? 155  PHE A CE1  1 
ATOM   1928 C  CE2  . PHE A 1 155 ? 32.001 -12.374 43.687 1.000 10.13 ? 155  PHE A CE2  1 
ATOM   1929 C  CZ   . PHE A 1 155 ? 32.912 -12.716 44.672 1.000 10.06 ? 155  PHE A CZ   1 
ATOM   1930 H  HA   . PHE A 1 155 ? 34.371 -15.392 40.629 1.000 11.23 ? 155  PHE A HA   1 
ATOM   1931 H  HE1  . PHE A 1 155 ? 34.736 -13.594 44.935 1.000 12.40 ? 155  PHE A HE1  1 
ATOM   1932 H  HZ   . PHE A 1 155 ? 32.730 -12.541 45.567 1.000 12.08 ? 155  PHE A HZ   1 
ATOM   1933 N  N    . PHE A 1 156 ? 31.304 -14.886 39.695 1.000 9.35  ? 156  PHE A N    1 
ATOM   1934 C  CA   . PHE A 1 156 ? 29.958 -15.413 39.741 1.000 8.62  ? 156  PHE A CA   1 
ATOM   1935 C  C    . PHE A 1 156 ? 29.873 -16.624 38.817 1.000 9.15  ? 156  PHE A C    1 
ATOM   1936 O  O    . PHE A 1 156 ? 30.467 -16.627 37.753 1.000 11.14 ? 156  PHE A O    1 
ATOM   1937 C  CB   . PHE A 1 156 ? 28.949 -14.359 39.364 1.000 9.06  ? 156  PHE A CB   1 
ATOM   1938 C  CG   . PHE A 1 156 ? 28.867 -13.204 40.339 1.000 8.61  ? 156  PHE A CG   1 
ATOM   1939 C  CD1  . PHE A 1 156 ? 28.462 -13.398 41.636 1.000 8.82  ? 156  PHE A CD1  1 
ATOM   1940 C  CD2  . PHE A 1 156 ? 29.210 -11.932 39.967 1.000 9.63  ? 156  PHE A CD2  1 
ATOM   1941 C  CE1  . PHE A 1 156 ? 28.371 -12.315 42.502 1.000 10.04 ? 156  PHE A CE1  1 
ATOM   1942 C  CE2  . PHE A 1 156 ? 29.118 -10.862 40.838 1.000 10.67 ? 156  PHE A CE2  1 
ATOM   1943 C  CZ   . PHE A 1 156 ? 28.721 -11.043 42.124 1.000 10.46 ? 156  PHE A CZ   1 
ATOM   1944 H  HA   . PHE A 1 156 ? 29.772 -15.707 40.657 1.000 10.34 ? 156  PHE A HA   1 
ATOM   1945 H  HD1  . PHE A 1 156 ? 28.249 -14.253 41.934 1.000 10.59 ? 156  PHE A HD1  1 
ATOM   1946 H  HD2  . PHE A 1 156 ? 29.514 -11.783 39.100 1.000 11.55 ? 156  PHE A HD2  1 
ATOM   1947 H  HE1  . PHE A 1 156 ? 28.062 -12.457 43.368 1.000 12.05 ? 156  PHE A HE1  1 
ATOM   1948 H  HZ   . PHE A 1 156 ? 28.688 -10.334 42.724 1.000 12.55 ? 156  PHE A HZ   1 
ATOM   1949 N  N    . SER A 1 157 ? 29.075 -17.616 39.205 1.000 8.83  ? 157  SER A N    1 
ATOM   1950 C  CA   . SER A 1 157 ? 28.958 -18.802 38.335 1.000 9.37  ? 157  SER A CA   1 
ATOM   1951 C  C    . SER A 1 157 ? 28.184 -18.532 37.070 1.000 8.68  ? 157  SER A C    1 
ATOM   1952 O  O    . SER A 1 157 ? 28.486 -19.165 36.025 1.000 10.08 ? 157  SER A O    1 
ATOM   1953 C  CB   . SER A 1 157 ? 28.342 -19.955 39.106 1.000 10.45 ? 157  SER A CB   1 
ATOM   1954 O  OG   . SER A 1 157 ? 27.061 -19.605 39.595 1.000 11.57 ? 157  SER A OG   1 
ATOM   1955 H  H    . SER A 1 157 ? 28.638 -17.566 39.944 1.000 10.60 ? 157  SER A H    1 
ATOM   1956 H  HB2  . SER A 1 157 ? 28.266 -20.728 38.526 1.000 12.54 ? 157  SER A HB2  1 
ATOM   1957 H  HB3  . SER A 1 157 ? 28.918 -20.192 39.850 1.000 12.54 ? 157  SER A HB3  1 
ATOM   1958 N  N    . ALA A 1 158 ? 27.224 -17.639 37.124 1.000 8.32  ? 158  ALA A N    1 
ATOM   1959 C  CA   . ALA A 1 158 ? 26.402 -17.264 35.966 1.000 8.73  ? 158  ALA A CA   1 
ATOM   1960 C  C    . ALA A 1 158 ? 25.678 -15.992 36.394 1.000 7.42  ? 158  ALA A C    1 
ATOM   1961 O  O    . ALA A 1 158 ? 25.393 -15.822 37.562 1.000 8.43  ? 158  ALA A O    1 
ATOM   1962 C  CB   . ALA A 1 158 ? 25.366 -18.336 35.585 1.000 11.23 ? 158  ALA A CB   1 
ATOM   1963 N  N    . SER A 1 159 ? 25.346 -15.153 35.409 1.000 6.95  ? 159  SER A N    1 
ATOM   1964 C  CA   . SER A 1 159 ? 24.714 -13.879 35.730 1.000 6.45  ? 159  SER A CA   1 
ATOM   1965 C  C    . SER A 1 159 ? 23.731 -13.484 34.647 1.000 6.38  ? 159  SER A C    1 
ATOM   1966 O  O    . SER A 1 159 ? 23.678 -14.073 33.565 1.000 6.79  ? 159  SER A O    1 
ATOM   1967 C  CB   . SER A 1 159 ? 25.771 -12.799 35.901 1.000 6.61  ? 159  SER A CB   1 
ATOM   1968 O  OG   . SER A 1 159 ? 26.811 -13.161 36.785 1.000 7.65  ? 159  SER A OG   1 
ATOM   1969 H  H    . SER A 1 159 ? 25.504 -15.363 34.590 1.000 8.34  ? 159  SER A H    1 
ATOM   1970 H  HA   . SER A 1 159 ? 24.227 -13.976 36.575 1.000 7.74  ? 159  SER A HA   1 
ATOM   1971 H  HB2  . SER A 1 159 ? 26.159 -12.610 35.032 1.000 7.93  ? 159  SER A HB2  1 
ATOM   1972 N  N    . CYS A 1 160 ? 22.948 -12.425 34.962 1.000 6.11  ? 160  CYS A N    1 
ATOM   1973 C  CA   . CYS A 1 160 ? 22.270 -11.650 33.964 1.000 5.97  ? 160  CYS A CA   1 
ATOM   1974 C  C    . CYS A 1 160 ? 22.792 -10.221 34.052 1.000 5.75  ? 160  CYS A C    1 
ATOM   1975 O  O    . CYS A 1 160 ? 22.561 -9.526  35.070 1.000 6.24  ? 160  CYS A O    1 
ATOM   1976 C  CB   . CYS A 1 160 ? 20.744 -11.673 34.071 1.000 6.50  ? 160  CYS A CB   1 
ATOM   1977 S  SG   . CYS A 1 160 ? 19.961 -10.761 32.723 1.000 7.21  ? 160  CYS A SG   1 
ATOM   1978 H  H    . CYS A 1 160 ? 22.855 -12.209 35.790 1.000 7.34  ? 160  CYS A H    1 
ATOM   1979 H  HA   . CYS A 1 160 ? 22.516 -12.008 33.085 1.000 7.16  ? 160  CYS A HA   1 
ATOM   1980 H  HB2  . CYS A 1 160 ? 20.436 -12.593 34.056 1.000 7.80  ? 160  CYS A HB2  1 
ATOM   1981 H  HB3  . CYS A 1 160 ? 20.477 -11.283 34.919 1.000 7.80  ? 160  CYS A HB3  1 
ATOM   1982 N  N    . VAL A 1 161 ? 23.484 -9.789  33.019 1.000 5.75  ? 161  VAL A N    1 
ATOM   1983 C  CA   . VAL A 1 161 ? 24.098 -8.465  32.905 1.000 6.12  ? 161  VAL A CA   1 
ATOM   1984 C  C    . VAL A 1 161 ? 23.672 -7.877  31.553 1.000 5.84  ? 161  VAL A C    1 
ATOM   1985 O  O    . VAL A 1 161 ? 24.357 -8.040  30.554 1.000 6.58  ? 161  VAL A O    1 
ATOM   1986 C  CB   . VAL A 1 161 ? 25.613 -8.486  33.008 1.000 6.10  ? 161  VAL A CB   1 
ATOM   1987 C  CG1  . VAL A 1 161 ? 26.134 -7.053  33.000 1.000 7.48  ? 161  VAL A CG1  1 
ATOM   1988 C  CG2  . VAL A 1 161 ? 26.095 -9.238  34.248 1.000 6.55  ? 161  VAL A CG2  1 
ATOM   1989 H  H    . VAL A 1 161 ? 23.584 -10.329 32.358 1.000 6.90  ? 161  VAL A H    1 
ATOM   1990 H  HA   . VAL A 1 161 ? 23.745 -7.894  33.619 1.000 7.34  ? 161  VAL A HA   1 
ATOM   1991 H  HB   . VAL A 1 161 ? 25.967 -8.944  32.216 1.000 7.32  ? 161  VAL A HB   1 
ATOM   1992 H  HG12 . VAL A 1 161 ? 25.807 -6.592  33.776 1.000 11.22 ? 161  VAL A HG12 1 
ATOM   1993 H  HG13 . VAL A 1 161 ? 27.094 -7.054  33.008 1.000 11.22 ? 161  VAL A HG13 1 
ATOM   1994 H  HG21 . VAL A 1 161 ? 25.758 -10.136 34.224 1.000 9.83  ? 161  VAL A HG21 1 
ATOM   1995 N  N    . PRO A 1 162 ? 22.488 -7.253  31.513 1.000 5.96  ? 162  PRO A N    1 
ATOM   1996 C  CA   . PRO A 1 162 ? 21.985 -6.692  30.258 1.000 5.93  ? 162  PRO A CA   1 
ATOM   1997 C  C    . PRO A 1 162 ? 23.043 -5.789  29.618 1.000 5.70  ? 162  PRO A C    1 
ATOM   1998 O  O    . PRO A 1 162 ? 23.609 -4.896  30.279 1.000 6.79  ? 162  PRO A O    1 
ATOM   1999 C  CB   . PRO A 1 162 ? 20.724 -5.979  30.694 1.000 7.00  ? 162  PRO A CB   1 
ATOM   2000 C  CG   . PRO A 1 162 ? 20.229 -6.822  31.863 1.000 8.03  ? 162  PRO A CG   1 
ATOM   2001 C  CD   . PRO A 1 162 ? 21.516 -7.120  32.612 1.000 6.80  ? 162  PRO A CD   1 
ATOM   2002 H  HA   . PRO A 1 162 ? 21.756 -7.418  29.642 1.000 7.12  ? 162  PRO A HA   1 
ATOM   2003 H  HB2  . PRO A 1 162 ? 20.915 -5.070  30.975 1.000 8.40  ? 162  PRO A HB2  1 
ATOM   2004 H  HB3  . PRO A 1 162 ? 20.070 -5.957  29.978 1.000 8.40  ? 162  PRO A HB3  1 
ATOM   2005 H  HG3  . PRO A 1 162 ? 19.815 -7.639  31.543 1.000 9.64  ? 162  PRO A HG3  1 
ATOM   2006 H  HD2  . PRO A 1 162 ? 21.755 -6.392  33.208 1.000 8.16  ? 162  PRO A HD2  1 
ATOM   2007 H  HD3  . PRO A 1 162 ? 21.446 -7.941  33.123 1.000 8.16  ? 162  PRO A HD3  1 
ATOM   2008 N  N    . GLY A 1 163 ? 23.338 -6.014  28.351 1.000 6.19  ? 163  GLY A N    1 
ATOM   2009 C  CA   . GLY A 1 163 ? 24.373 -5.301  27.646 1.000 6.61  ? 163  GLY A CA   1 
ATOM   2010 C  C    . GLY A 1 163 ? 25.728 -5.964  27.617 1.000 7.11  ? 163  GLY A C    1 
ATOM   2011 O  O    . GLY A 1 163 ? 26.587 -5.464  26.860 1.000 8.23  ? 163  GLY A O    1 
ATOM   2012 H  H    . GLY A 1 163 ? 22.891 -6.614  27.927 1.000 7.43  ? 163  GLY A H    1 
ATOM   2013 H  HA2  . GLY A 1 163 ? 24.081 -5.166  26.731 1.000 7.93  ? 163  GLY A HA2  1 
ATOM   2014 H  HA3  . GLY A 1 163 ? 24.472 -4.426  28.052 1.000 7.93  ? 163  GLY A HA3  1 
ATOM   2015 N  N    . ALA A 1 164 ? 25.970 -7.011  28.374 1.000 7.55  ? 164  ALA A N    1 
ATOM   2016 C  CA   . ALA A 1 164 ? 27.257 -7.680  28.305 1.000 8.00  ? 164  ALA A CA   1 
ATOM   2017 C  C    . ALA A 1 164 ? 27.440 -8.352  26.943 1.000 8.16  ? 164  ALA A C    1 
ATOM   2018 O  O    . ALA A 1 164 ? 26.555 -9.046  26.448 1.000 10.90 ? 164  ALA A O    1 
ATOM   2019 C  CB   . ALA A 1 164 ? 27.359 -8.756  29.366 1.000 10.42 ? 164  ALA A CB   1 
ATOM   2020 H  H    . ALA A 1 164 ? 25.364 -7.300  28.911 1.000 9.06  ? 164  ALA A H    1 
ATOM   2021 H  HA   . ALA A 1 164 ? 27.972 -7.023  28.441 1.000 9.60  ? 164  ALA A HA   1 
ATOM   2022 H  HB1  . ALA A 1 164 ? 28.215 -9.186  29.304 1.000 15.63 ? 164  ALA A HB1  1 
ATOM   2023 H  HB2  . ALA A 1 164 ? 27.261 -8.359  30.234 1.000 15.63 ? 164  ALA A HB2  1 
ATOM   2024 H  HB3  . ALA A 1 164 ? 26.664 -9.405  29.231 1.000 15.63 ? 164  ALA A HB3  1 
ATOM   2025 N  N    . THR A 1 165 ? 28.645 -8.176  26.379 1.000 9.73  ? 165  THR A N    1 
ATOM   2026 C  CA   . THR A 1 165 ? 28.911 -8.800  25.066 1.000 11.50 ? 165  THR A CA   1 
ATOM   2027 C  C    . THR A 1 165 ? 30.194 -9.637  25.059 1.000 9.76  ? 165  THR A C    1 
ATOM   2028 O  O    . THR A 1 165 ? 30.402 -10.368 24.084 1.000 13.40 ? 165  THR A O    1 
ATOM   2029 C  CB   . THR A 1 165 ? 29.024 -7.744  23.950 1.000 16.22 ? 165  THR A CB   1 
ATOM   2030 O  OG1  . THR A 1 165 ? 30.128 -6.908  24.320 1.000 19.22 ? 165  THR A OG1  1 
ATOM   2031 C  CG2  . THR A 1 165 ? 27.762 -6.960  23.857 1.000 22.01 ? 165  THR A CG2  1 
ATOM   2032 N  N    . ILE A 1 166 ? 31.062 -9.551  26.051 1.000 9.95  ? 166  ILE A N    1 
ATOM   2033 C  CA   . ILE A 1 166 ? 32.339 -10.268 26.019 1.000 10.84 ? 166  ILE A CA   1 
ATOM   2034 C  C    . ILE A 1 166 ? 32.264 -11.645 26.612 1.000 9.82  ? 166  ILE A C    1 
ATOM   2035 O  O    . ILE A 1 166 ? 33.035 -12.476 26.146 1.000 12.02 ? 166  ILE A O    1 
ATOM   2036 C  CB   . ILE A 1 166 ? 33.443 -9.453  26.819 1.000 12.71 ? 166  ILE A CB   1 
ATOM   2037 C  CG1  . ILE A 1 166 ? 33.572 -8.099  26.184 1.000 14.28 ? 166  ILE A CG1  1 
ATOM   2038 C  CG2  . ILE A 1 166 ? 34.767 -10.229 26.921 1.000 15.04 ? 166  ILE A CG2  1 
ATOM   2039 C  CD1  . ILE A 1 166 ? 34.537 -7.254  26.949 1.000 18.13 ? 166  ILE A CD1  1 
ATOM   2040 H  HA   . ILE A 1 166 ? 32.628 -10.348 25.086 1.000 13.01 ? 166  ILE A HA   1 
ATOM   2041 H  HG12 . ILE A 1 166 ? 34.026 -8.226  25.345 1.000 17.14 ? 166  ILE A HG12 1 
ATOM   2042 N  N    . GLU A 1 167 ? 31.427 -11.843 27.592 1.000 10.07 ? 167  GLU A N    1 
ATOM   2043 C  CA   A GLU A 1 167 ? 31.369 -13.118 28.317 0.438 10.01 ? 167  GLU A CA   1 
ATOM   2044 C  CA   B GLU A 1 167 ? 31.364 -13.073 28.320 0.562 9.06  ? 167  GLU A CA   1 
ATOM   2045 C  C    . GLU A 1 167 ? 29.951 -13.677 28.278 1.000 8.14  ? 167  GLU A C    1 
ATOM   2046 O  O    . GLU A 1 167 ? 29.022 -13.101 28.920 1.000 9.30  ? 167  GLU A O    1 
ATOM   2047 C  CB   A GLU A 1 167 ? 31.774 -12.978 29.771 0.438 9.24  ? 167  GLU A CB   1 
ATOM   2048 C  CB   B GLU A 1 167 ? 31.731 -12.824 29.793 0.562 14.90 ? 167  GLU A CB   1 
ATOM   2049 C  CG   A GLU A 1 167 ? 33.231 -12.780 29.985 0.438 9.63  ? 167  GLU A CG   1 
ATOM   2050 C  CG   B GLU A 1 167 ? 31.238 -14.131 30.434 0.562 18.37 ? 167  GLU A CG   1 
ATOM   2051 C  CD   A GLU A 1 167 ? 34.105 -14.015 29.797 0.438 13.55 ? 167  GLU A CD   1 
ATOM   2052 C  CD   B GLU A 1 167 ? 32.162 -15.314 30.109 0.562 19.14 ? 167  GLU A CD   1 
ATOM   2053 O  OE1  A GLU A 1 167 ? 33.656 -15.138 29.575 0.438 11.62 ? 167  GLU A OE1  1 
ATOM   2054 O  OE1  B GLU A 1 167 ? 33.396 -15.112 30.104 0.562 24.24 ? 167  GLU A OE1  1 
ATOM   2055 O  OE2  A GLU A 1 167 ? 35.339 -13.849 29.851 0.438 26.75 ? 167  GLU A OE2  1 
ATOM   2056 O  OE2  B GLU A 1 167 ? 31.545 -16.362 29.833 0.562 13.97 ? 167  GLU A OE2  1 
ATOM   2057 H  H    A GLU A 1 167 ? 30.893 -11.208 27.821 1.000 12.08 ? 167  GLU A H    1 
ATOM   2058 H  HA   A GLU A 1 167 ? 31.972 -13.757 27.882 0.438 12.02 ? 167  GLU A HA   1 
ATOM   2059 N  N    . GLN A 1 168 ? 29.759 -14.775 27.611 1.000 8.96  ? 168  GLN A N    1 
ATOM   2060 C  CA   A GLN A 1 168 ? 28.425 -15.336 27.478 0.619 8.35  ? 168  GLN A CA   1 
ATOM   2061 C  CA   B GLN A 1 168 ? 28.503 -15.471 27.461 0.381 7.70  ? 168  GLN A CA   1 
ATOM   2062 C  C    . GLN A 1 168 ? 27.833 -15.757 28.811 1.000 8.12  ? 168  GLN A C    1 
ATOM   2063 O  O    . GLN A 1 168 ? 26.612 -15.753 28.948 1.000 8.19  ? 168  GLN A O    1 
ATOM   2064 C  CB   A GLN A 1 168 ? 28.465 -16.575 26.558 0.619 7.91  ? 168  GLN A CB   1 
ATOM   2065 C  CB   B GLN A 1 168 ? 28.827 -16.740 26.645 0.381 11.99 ? 168  GLN A CB   1 
ATOM   2066 C  CG   A GLN A 1 168 ? 28.667 -16.196 25.081 0.619 8.52  ? 168  GLN A CG   1 
ATOM   2067 C  CG   B GLN A 1 168 ? 29.630 -16.634 25.379 0.381 16.03 ? 168  GLN A CG   1 
ATOM   2068 C  CD   A GLN A 1 168 ? 27.586 -15.241 24.640 0.619 8.91  ? 168  GLN A CD   1 
ATOM   2069 C  CD   B GLN A 1 168 ? 31.145 -16.757 25.185 0.381 16.94 ? 168  GLN A CD   1 
ATOM   2070 O  OE1  A GLN A 1 168 ? 27.900 -14.084 24.285 0.619 11.67 ? 168  GLN A OE1  1 
ATOM   2071 O  OE1  B GLN A 1 168 ? 31.728 -15.815 25.874 0.381 15.06 ? 168  GLN A OE1  1 
ATOM   2072 N  NE2  A GLN A 1 168 ? 26.351 -15.687 24.652 0.619 8.86  ? 168  GLN A NE2  1 
ATOM   2073 N  NE2  B GLN A 1 168 ? 31.688 -17.778 24.320 0.381 5.91  ? 168  GLN A NE2  1 
ATOM   2074 H  H    A GLN A 1 168 ? 30.427 -15.174 27.245 1.000 10.76 ? 168  GLN A H    1 
ATOM   2075 N  N    . LYS A 1 169 ? 28.631 -16.124 29.825 1.000 8.50  ? 169  LYS A N    1 
ATOM   2076 C  CA   A LYS A 1 169 ? 28.133 -16.471 31.131 0.244 9.12  ? 169  LYS A CA   1 
ATOM   2077 C  CA   B LYS A 1 169 ? 28.152 -16.463 31.143 0.438 10.55 ? 169  LYS A CA   1 
ATOM   2078 C  CA   C LYS A 1 169 ? 28.014 -16.541 31.086 0.318 10.61 ? 169  LYS A CA   1 
ATOM   2079 C  C    . LYS A 1 169 ? 27.359 -15.333 31.785 1.000 7.87  ? 169  LYS A C    1 
ATOM   2080 O  O    . LYS A 1 169 ? 26.526 -15.568 32.657 1.000 8.10  ? 169  LYS A O    1 
ATOM   2081 C  CB   A LYS A 1 169 ? 29.341 -16.845 32.034 0.244 9.75  ? 169  LYS A CB   1 
ATOM   2082 C  CB   B LYS A 1 169 ? 29.351 -16.799 32.080 0.438 12.05 ? 169  LYS A CB   1 
ATOM   2083 C  CB   C LYS A 1 169 ? 29.020 -17.269 31.991 0.318 13.95 ? 169  LYS A CB   1 
ATOM   2084 C  CG   A LYS A 1 169 ? 29.893 -18.209 31.621 0.244 8.07  ? 169  LYS A CG   1 
ATOM   2085 C  CG   B LYS A 1 169 ? 29.799 -18.247 31.898 0.438 13.80 ? 169  LYS A CG   1 
ATOM   2086 C  CG   C LYS A 1 169 ? 29.794 -16.435 32.992 0.318 18.40 ? 169  LYS A CG   1 
ATOM   2087 C  CD   A LYS A 1 169 ? 31.123 -18.592 32.429 0.244 10.24 ? 169  LYS A CD   1 
ATOM   2088 C  CD   B LYS A 1 169 ? 31.204 -18.465 32.444 0.438 13.86 ? 169  LYS A CD   1 
ATOM   2089 C  CD   C LYS A 1 169 ? 30.467 -17.283 34.073 0.318 14.88 ? 169  LYS A CD   1 
ATOM   2090 C  CE   A LYS A 1 169 ? 30.898 -18.719 33.915 0.244 9.21  ? 169  LYS A CE   1 
ATOM   2091 C  CE   B LYS A 1 169 ? 31.344 -18.094 33.917 0.438 15.22 ? 169  LYS A CE   1 
ATOM   2092 C  CE   C LYS A 1 169 ? 31.128 -18.495 33.429 0.318 14.89 ? 169  LYS A CE   1 
ATOM   2093 N  NZ   A LYS A 1 169 ? 30.623 -17.437 34.616 0.244 10.49 ? 169  LYS A NZ   1 
ATOM   2094 N  NZ   B LYS A 1 169 ? 32.206 -19.115 34.570 0.438 10.35 ? 169  LYS A NZ   1 
ATOM   2095 N  NZ   C LYS A 1 169 ? 32.253 -18.057 32.557 0.318 14.63 ? 169  LYS A NZ   1 
ATOM   2096 H  H    A LYS A 1 169 ? 29.480 -16.154 29.689 1.000 10.19 ? 169  LYS A H    1 
ATOM   2097 N  N    . LEU A 1 170 ? 27.686 -14.090 31.402 1.000 7.75  ? 170  LEU A N    1 
ATOM   2098 C  CA   . LEU A 1 170 ? 26.999 -12.949 31.952 1.000 7.36  ? 170  LEU A CA   1 
ATOM   2099 C  C    . LEU A 1 170 ? 25.605 -12.741 31.369 1.000 6.92  ? 170  LEU A C    1 
ATOM   2100 O  O    . LEU A 1 170 ? 24.909 -11.848 31.846 1.000 7.60  ? 170  LEU A O    1 
ATOM   2101 C  CB   . LEU A 1 170 ? 27.835 -11.680 31.810 1.000 7.87  ? 170  LEU A CB   1 
ATOM   2102 C  CG   . LEU A 1 170 ? 29.214 -11.727 32.485 1.000 8.98  ? 170  LEU A CG   1 
ATOM   2103 C  CD1  . LEU A 1 170 ? 29.900 -10.387 32.279 1.000 10.46 ? 170  LEU A CD1  1 
ATOM   2104 C  CD2  . LEU A 1 170 ? 29.099 -12.065 33.983 1.000 9.80  ? 170  LEU A CD2  1 
ATOM   2105 H  H    . LEU A 1 170 ? 28.311 -13.973 30.823 1.000 9.31  ? 170  LEU A H    1 
ATOM   2106 H  HA   . LEU A 1 170 ? 26.888 -13.115 32.911 1.000 8.83  ? 170  LEU A HA   1 
ATOM   2107 H  HB3  . LEU A 1 170 ? 27.335 -10.934 32.176 1.000 9.44  ? 170  LEU A HB3  1 
ATOM   2108 H  HD12 . LEU A 1 170 ? 29.389 -9.704  32.718 1.000 15.69 ? 170  LEU A HD12 1 
ATOM   2109 H  HD13 . LEU A 1 170 ? 30.785 -10.413 32.650 1.000 15.69 ? 170  LEU A HD13 1 
ATOM   2110 H  HD21 . LEU A 1 170 ? 29.048 -13.018 34.081 1.000 14.70 ? 170  LEU A HD21 1 
ATOM   2111 N  N    A CYS A 1 171 ? 25.211 -13.540 30.384 0.915 7.01  ? 171  CYS A N    1 
ATOM   2112 N  N    B CYS A 1 171 ? 25.149 -13.561 30.429 0.085 8.04  ? 171  CYS A N    1 
ATOM   2113 C  CA   A CYS A 1 171 ? 23.870 -13.542 29.834 0.915 7.07  ? 171  CYS A CA   1 
ATOM   2114 C  CA   B CYS A 1 171 ? 23.750 -13.481 30.025 0.085 8.40  ? 171  CYS A CA   1 
ATOM   2115 C  C    A CYS A 1 171 ? 23.088 -14.814 30.215 0.915 7.09  ? 171  CYS A C    1 
ATOM   2116 C  C    B CYS A 1 171 ? 23.009 -14.773 30.350 0.085 6.47  ? 171  CYS A C    1 
ATOM   2117 O  O    A CYS A 1 171 ? 21.914 -14.913 29.859 0.915 7.97  ? 171  CYS A O    1 
ATOM   2118 O  O    B CYS A 1 171 ? 21.797 -14.891 30.149 0.085 10.20 ? 171  CYS A O    1 
ATOM   2119 C  CB   A CYS A 1 171 ? 23.921 -13.419 28.318 0.915 7.36  ? 171  CYS A CB   1 
ATOM   2120 C  CB   B CYS A 1 171 ? 23.658 -13.171 28.527 0.085 9.68  ? 171  CYS A CB   1 
ATOM   2121 S  SG   A CYS A 1 171 ? 24.566 -11.853 27.704 0.915 8.42  ? 171  CYS A SG   1 
ATOM   2122 S  SG   B CYS A 1 171 ? 21.952 -12.878 27.996 0.085 15.31 ? 171  CYS A SG   1 
ATOM   2123 H  H    A CYS A 1 171 ? 25.785 -14.088 30.052 0.915 8.41  ? 171  CYS A H    1 
ATOM   2124 H  H    B CYS A 1 171 ? 25.675 -14.135 30.062 0.085 9.65  ? 171  CYS A H    1 
ATOM   2125 H  HA   A CYS A 1 171 ? 23.390 -12.766 30.190 0.915 8.48  ? 171  CYS A HA   1 
ATOM   2126 H  HA   B CYS A 1 171 ? 23.327 -12.748 30.519 0.085 10.08 ? 171  CYS A HA   1 
ATOM   2127 H  HB2  A CYS A 1 171 ? 24.472 -14.137 27.969 0.915 8.83  ? 171  CYS A HB2  1 
ATOM   2128 H  HB3  A CYS A 1 171 ? 23.025 -13.541 27.968 0.915 8.83  ? 171  CYS A HB3  1 
ATOM   2129 N  N    . ARG A 1 172 ? 23.746 -15.766 30.851 1.000 7.25  ? 172  ARG A N    1 
ATOM   2130 C  CA   A ARG A 1 172 ? 23.140 -17.088 30.990 0.247 7.65  ? 172  ARG A CA   1 
ATOM   2131 C  CA   B ARG A 1 172 ? 23.188 -17.088 31.041 0.753 8.37  ? 172  ARG A CA   1 
ATOM   2132 C  C    . ARG A 1 172 ? 21.855 -17.086 31.839 1.000 8.28  ? 172  ARG A C    1 
ATOM   2133 O  O    . ARG A 1 172 ? 20.995 -17.938 31.582 1.000 9.25  ? 172  ARG A O    1 
ATOM   2134 C  CB   A ARG A 1 172 ? 24.143 -18.101 31.561 0.247 11.52 ? 172  ARG A CB   1 
ATOM   2135 C  CB   B ARG A 1 172 ? 24.262 -18.002 31.703 0.753 9.34  ? 172  ARG A CB   1 
ATOM   2136 C  CG   A ARG A 1 172 ? 25.506 -18.094 30.928 0.247 12.44 ? 172  ARG A CG   1 
ATOM   2137 C  CG   B ARG A 1 172 ? 23.810 -19.424 31.901 0.753 11.29 ? 172  ARG A CG   1 
ATOM   2138 C  CD   A ARG A 1 172 ? 25.638 -18.951 29.684 0.247 21.54 ? 172  ARG A CD   1 
ATOM   2139 C  CD   B ARG A 1 172 ? 23.553 -20.227 30.676 0.753 15.55 ? 172  ARG A CD   1 
ATOM   2140 N  NE   A ARG A 1 172 ? 27.065 -19.311 29.515 0.247 16.85 ? 172  ARG A NE   1 
ATOM   2141 N  NE   B ARG A 1 172 ? 23.151 -21.575 30.932 0.753 21.87 ? 172  ARG A NE   1 
ATOM   2142 C  CZ   A ARG A 1 172 ? 27.331 -20.519 30.061 0.247 24.28 ? 172  ARG A CZ   1 
ATOM   2143 C  CZ   B ARG A 1 172 ? 23.845 -22.685 31.217 0.753 30.42 ? 172  ARG A CZ   1 
ATOM   2144 N  NH1  A ARG A 1 172 ? 28.478 -21.151 30.103 0.247 24.99 ? 172  ARG A NH1  1 
ATOM   2145 N  NH1  B ARG A 1 172 ? 23.183 -23.839 31.371 0.753 42.13 ? 172  ARG A NH1  1 
ATOM   2146 N  NH2  A ARG A 1 172 ? 26.248 -21.077 30.595 0.247 26.42 ? 172  ARG A NH2  1 
ATOM   2147 N  NH2  B ARG A 1 172 ? 25.177 -22.659 31.364 0.753 34.43 ? 172  ARG A NH2  1 
ATOM   2148 H  H    A ARG A 1 172 ? 24.525 -15.609 31.181 1.000 8.70  ? 172  ARG A H    1 
ATOM   2149 N  N    . GLN A 1 173 ? 21.739 -16.168 32.792 1.000 7.54  ? 173  GLN A N    1 
ATOM   2150 C  CA   . GLN A 1 173 ? 20.591 -16.150 33.690 1.000 7.68  ? 173  GLN A CA   1 
ATOM   2151 C  C    . GLN A 1 173 ? 19.479 -15.265 33.170 1.000 8.10  ? 173  GLN A C    1 
ATOM   2152 O  O    . GLN A 1 173 ? 18.438 -15.151 33.843 1.000 9.72  ? 173  GLN A O    1 
ATOM   2153 C  CB   . GLN A 1 173 ? 21.022 -15.707 35.084 1.000 8.13  ? 173  GLN A CB   1 
ATOM   2154 C  CG   . GLN A 1 173 ? 22.073 -16.624 35.714 1.000 8.26  ? 173  GLN A CG   1 
ATOM   2155 C  CD   . GLN A 1 173 ? 21.677 -18.069 35.728 1.000 9.27  ? 173  GLN A CD   1 
ATOM   2156 O  OE1  . GLN A 1 173 ? 22.080 -18.824 34.837 1.000 11.15 ? 173  GLN A OE1  1 
ATOM   2157 N  NE2  . GLN A 1 173 ? 20.900 -18.466 36.726 1.000 9.78  ? 173  GLN A NE2  1 
ATOM   2158 H  H    . GLN A 1 173 ? 22.354 -15.573 32.881 1.000 9.05  ? 173  GLN A H    1 
ATOM   2159 H  HA   . GLN A 1 173 ? 20.245 -17.064 33.757 1.000 9.21  ? 173  GLN A HA   1 
ATOM   2160 H  HB3  . GLN A 1 173 ? 20.258 -15.691 35.661 1.000 9.75  ? 173  GLN A HB3  1 
ATOM   2161 H  HG2  . GLN A 1 173 ? 22.904 -16.532 35.222 1.000 9.91  ? 173  GLN A HG2  1 
ATOM   2162 H  HG3  . GLN A 1 173 ? 22.236 -16.334 36.625 1.000 9.91  ? 173  GLN A HG3  1 
ATOM   2163 N  N    . CYS A 1 174 ? 19.677 -14.632 32.023 1.000 7.33  ? 174  CYS A N    1 
ATOM   2164 C  CA   . CYS A 1 174 ? 18.689 -13.682 31.528 1.000 7.79  ? 174  CYS A CA   1 
ATOM   2165 C  C    . CYS A 1 174 ? 17.473 -14.388 30.962 1.000 8.12  ? 174  CYS A C    1 
ATOM   2166 O  O    . CYS A 1 174 ? 17.546 -15.418 30.330 1.000 13.35 ? 174  CYS A O    1 
ATOM   2167 C  CB   . CYS A 1 174 ? 19.286 -12.783 30.476 1.000 8.29  ? 174  CYS A CB   1 
ATOM   2168 S  SG   . CYS A 1 174 ? 20.669 -11.721 31.036 1.000 7.86  ? 174  CYS A SG   1 
ATOM   2169 H  H    . CYS A 1 174 ? 20.392 -14.781 31.569 1.000 8.80  ? 174  CYS A H    1 
ATOM   2170 H  HA   . CYS A 1 174 ? 18.397 -13.124 32.279 1.000 9.35  ? 174  CYS A HA   1 
ATOM   2171 H  HB2  . CYS A 1 174 ? 19.602 -13.335 29.744 1.000 9.95  ? 174  CYS A HB2  1 
ATOM   2172 H  HB3  . CYS A 1 174 ? 18.584 -12.211 30.128 1.000 9.95  ? 174  CYS A HB3  1 
ATOM   2173 N  N    . LYS A 1 175 ? 16.281 -13.792 31.133 1.000 8.96  ? 175  LYS A N    1 
ATOM   2174 C  CA   . LYS A 1 175 ? 15.006 -14.238 30.657 1.000 9.64  ? 175  LYS A CA   1 
ATOM   2175 C  C    . LYS A 1 175 ? 14.618 -13.576 29.335 1.000 8.29  ? 175  LYS A C    1 
ATOM   2176 O  O    . LYS A 1 175 ? 14.772 -12.354 29.202 1.000 9.40  ? 175  LYS A O    1 
ATOM   2177 C  CB   . LYS A 1 175 ? 13.930 -13.831 31.657 1.000 11.61 ? 175  LYS A CB   1 
ATOM   2178 C  CG   . LYS A 1 175 ? 12.490 -14.099 31.210 1.000 13.18 ? 175  LYS A CG   1 
ATOM   2179 C  CD   . LYS A 1 175 ? 11.504 -13.775 32.330 1.000 14.89 ? 175  LYS A CD   1 
ATOM   2180 C  CE   . LYS A 1 175 ? 10.063 -14.134 31.893 1.000 22.14 ? 175  LYS A CE   1 
ATOM   2181 N  NZ   . LYS A 1 175 ? 9.119  -13.607 32.909 1.000 36.77 ? 175  LYS A NZ   1 
ATOM   2182 H  H    . LYS A 1 175 ? 16.284 -13.057 31.580 1.000 10.76 ? 175  LYS A H    1 
ATOM   2183 H  HA   . LYS A 1 175 ? 15.012 -15.213 30.553 1.000 11.56 ? 175  LYS A HA   1 
ATOM   2184 H  HD2  . LYS A 1 175 ? 11.738 -14.278 33.126 1.000 17.87 ? 175  LYS A HD2  1 
ATOM   2185 H  HD3  . LYS A 1 175 ? 11.553 -12.830 32.545 1.000 17.87 ? 175  LYS A HD3  1 
ATOM   2186 N  N    . GLY A 1 176 ? 14.070 -14.351 28.395 1.000 10.06 ? 176  GLY A N    1 
ATOM   2187 C  CA   . GLY A 1 176 ? 13.443 -13.719 27.234 1.000 10.75 ? 176  GLY A CA   1 
ATOM   2188 C  C    . GLY A 1 176 ? 13.777 -14.496 25.982 1.000 9.15  ? 176  GLY A C    1 
ATOM   2189 O  O    . GLY A 1 176 ? 14.224 -15.636 26.016 1.000 12.42 ? 176  GLY A O    1 
ATOM   2190 H  H    . GLY A 1 176 ? 14.085 -15.207 28.472 1.000 12.07 ? 176  GLY A H    1 
ATOM   2191 N  N    . ASP A 1 177 ? 13.473 -13.887 24.861 1.000 9.03  ? 177  ASP A N    1 
ATOM   2192 C  CA   . ASP A 1 177 ? 13.754 -14.491 23.547 1.000 10.02 ? 177  ASP A CA   1 
ATOM   2193 C  C    . ASP A 1 177 ? 15.268 -14.448 23.318 1.000 8.19  ? 177  ASP A C    1 
ATOM   2194 O  O    . ASP A 1 177 ? 15.990 -13.564 23.828 1.000 9.01  ? 177  ASP A O    1 
ATOM   2195 C  CB   . ASP A 1 177 ? 13.072 -13.657 22.488 1.000 13.54 ? 177  ASP A CB   1 
ATOM   2196 C  CG   . ASP A 1 177 ? 11.579 -13.638 22.553 1.000 18.85 ? 177  ASP A CG   1 
ATOM   2197 O  OD1  . ASP A 1 177 ? 11.052 -14.720 22.853 1.000 21.89 ? 177  ASP A OD1  1 
ATOM   2198 O  OD2  . ASP A 1 177 ? 11.001 -12.559 22.303 1.000 27.24 ? 177  ASP A OD2  1 
ATOM   2199 H  H    . ASP A 1 177 ? 13.099 -13.113 24.893 1.000 10.83 ? 177  ASP A H    1 
ATOM   2200 N  N    . PRO A 1 178 ? 15.824 -15.381 22.539 1.000 9.33  ? 178  PRO A N    1 
ATOM   2201 C  CA   . PRO A 1 178 ? 17.252 -15.374 22.347 1.000 10.02 ? 178  PRO A CA   1 
ATOM   2202 C  C    . PRO A 1 178 ? 17.814 -14.057 21.857 1.000 8.99  ? 178  PRO A C    1 
ATOM   2203 O  O    . PRO A 1 178 ? 18.887 -13.637 22.326 1.000 9.34  ? 178  PRO A O    1 
ATOM   2204 C  CB   . PRO A 1 178 ? 17.431 -16.513 21.269 1.000 11.85 ? 178  PRO A CB   1 
ATOM   2205 C  CG   . PRO A 1 178 ? 16.344 -17.468 21.636 1.000 12.11 ? 178  PRO A CG   1 
ATOM   2206 C  CD   . PRO A 1 178 ? 15.150 -16.578 21.966 1.000 10.97 ? 178  PRO A CD   1 
ATOM   2207 H  HD2  . PRO A 1 178 ? 14.638 -16.364 21.170 1.000 13.16 ? 178  PRO A HD2  1 
ATOM   2208 N  N    . LYS A 1 179 ? 17.121 -13.369 20.952 1.000 9.52  ? 179  LYS A N    1 
ATOM   2209 C  CA   . LYS A 1 179 ? 17.724 -12.205 20.347 1.000 10.42 ? 179  LYS A CA   1 
ATOM   2210 C  C    . LYS A 1 179 ? 17.762 -11.019 21.288 1.000 9.63  ? 179  LYS A C    1 
ATOM   2211 O  O    . LYS A 1 179 ? 18.551 -10.103 21.084 1.000 12.85 ? 179  LYS A O    1 
ATOM   2212 C  CB   . LYS A 1 179 ? 16.949 -11.846 19.110 1.000 12.80 ? 179  LYS A CB   1 
ATOM   2213 C  CG   . LYS A 1 179 ? 17.754 -10.896 18.196 1.000 17.55 ? 179  LYS A CG   1 
ATOM   2214 C  CD   . LYS A 1 179 ? 17.081 -10.715 16.863 1.000 24.10 ? 179  LYS A CD   1 
ATOM   2215 C  CE   . LYS A 1 179 ? 17.951 -9.984  15.853 1.000 35.25 ? 179  LYS A CE   1 
ATOM   2216 N  NZ   . LYS A 1 179 ? 19.071 -10.807 15.292 1.000 56.29 ? 179  LYS A NZ   1 
ATOM   2217 H  H    . LYS A 1 179 ? 16.327 -13.614 20.731 1.000 11.43 ? 179  LYS A H    1 
ATOM   2218 H  HB2  . LYS A 1 179 ? 16.680 -12.638 18.650 1.000 15.36 ? 179  LYS A HB2  1 
ATOM   2219 N  N    . THR A 1 180 ? 16.919 -10.982 22.349 1.000 8.72  ? 180  THR A N    1 
ATOM   2220 C  CA   . THR A 1 180 ? 16.791 -9.821  23.184 1.000 9.22  ? 180  THR A CA   1 
ATOM   2221 C  C    . THR A 1 180 ? 16.981 -10.061 24.698 1.000 8.04  ? 180  THR A C    1 
ATOM   2222 O  O    . THR A 1 180 ? 17.025 -9.119  25.463 1.000 8.98  ? 180  THR A O    1 
ATOM   2223 C  CB   . THR A 1 180 ? 15.440 -9.114  22.929 1.000 11.68 ? 180  THR A CB   1 
ATOM   2224 O  OG1  . THR A 1 180 ? 14.455 -10.096 23.195 1.000 13.18 ? 180  THR A OG1  1 
ATOM   2225 C  CG2  . THR A 1 180 ? 15.311 -8.627  21.497 1.000 14.84 ? 180  THR A CG2  1 
ATOM   2226 H  H    . THR A 1 180 ? 16.445 -11.677 22.527 1.000 10.46 ? 180  THR A H    1 
ATOM   2227 H  HG1  . THR A 1 180 ? 13.754 -9.888  22.825 1.000 19.77 ? 180  THR A HG1  1 
ATOM   2228 N  N    . LYS A 1 181 ? 17.097 -11.319 25.157 1.000 7.37  ? 181  LYS A N    1 
ATOM   2229 C  CA   . LYS A 1 181 ? 17.179 -11.558 26.582 1.000 7.60  ? 181  LYS A CA   1 
ATOM   2230 C  C    . LYS A 1 181 ? 18.363 -10.877 27.271 1.000 7.01  ? 181  LYS A C    1 
ATOM   2231 O  O    . LYS A 1 181 ? 18.266 -10.574 28.452 1.000 7.91  ? 181  LYS A O    1 
ATOM   2232 C  CB   . LYS A 1 181 ? 17.205 -13.072 26.869 1.000 8.00  ? 181  LYS A CB   1 
ATOM   2233 C  CG   . LYS A 1 181 ? 18.403 -13.785 26.285 1.000 8.53  ? 181  LYS A CG   1 
ATOM   2234 C  CD   . LYS A 1 181 ? 18.613 -15.185 26.817 1.000 10.93 ? 181  LYS A CD   1 
ATOM   2235 C  CE   . LYS A 1 181 ? 17.398 -16.091 26.656 1.000 14.84 ? 181  LYS A CE   1 
ATOM   2236 N  NZ   . LYS A 1 181 ? 17.793 -17.495 26.948 1.000 15.00 ? 181  LYS A NZ   1 
ATOM   2237 H  H    . LYS A 1 181 ? 17.121 -11.979 24.606 1.000 8.84  ? 181  LYS A H    1 
ATOM   2238 H  HA   . LYS A 1 181 ? 16.362 -11.199 26.986 1.000 9.13  ? 181  LYS A HA   1 
ATOM   2239 H  HB2  . LYS A 1 181 ? 17.202 -13.202 27.830 1.000 9.60  ? 181  LYS A HB2  1 
ATOM   2240 N  N    A CYS A 1 182 ? 19.465 -10.654 26.535 0.915 6.92  ? 182  CYS A N    1 
ATOM   2241 N  N    B CYS A 1 182 ? 19.460 -10.614 26.573 0.085 7.63  ? 182  CYS A N    1 
ATOM   2242 C  CA   A CYS A 1 182 ? 20.622 -9.993  27.138 0.915 6.68  ? 182  CYS A CA   1 
ATOM   2243 C  CA   B CYS A 1 182 ? 20.639 -9.946  27.089 0.085 8.66  ? 182  CYS A CA   1 
ATOM   2244 C  C    A CYS A 1 182 ? 20.753 -8.556  26.647 0.915 6.61  ? 182  CYS A C    1 
ATOM   2245 C  C    B CYS A 1 182 ? 20.557 -8.431  26.969 0.085 8.65  ? 182  CYS A C    1 
ATOM   2246 O  O    A CYS A 1 182 ? 21.812 -7.931  26.888 0.915 7.62  ? 182  CYS A O    1 
ATOM   2247 O  O    B CYS A 1 182 ? 21.215 -7.674  27.677 0.085 14.59 ? 182  CYS A O    1 
ATOM   2248 C  CB   A CYS A 1 182 ? 21.902 -10.822 26.858 0.915 7.63  ? 182  CYS A CB   1 
ATOM   2249 C  CB   B CYS A 1 182 ? 21.890 -10.384 26.308 0.085 9.91  ? 182  CYS A CB   1 
ATOM   2250 S  SG   A CYS A 1 182 ? 23.119 -10.499 28.194 0.915 7.95  ? 182  CYS A SG   1 
ATOM   2251 S  SG   B CYS A 1 182 ? 22.100 -12.157 26.109 0.085 15.70 ? 182  CYS A SG   1 
ATOM   2252 H  H    A CYS A 1 182 ? 19.490 -10.899 25.711 0.915 8.30  ? 182  CYS A H    1 
ATOM   2253 H  H    B CYS A 1 182 ? 19.473 -10.860 25.749 0.085 9.15  ? 182  CYS A H    1 
ATOM   2254 H  HA   A CYS A 1 182 ? 20.484 -9.970  28.108 0.915 8.01  ? 182  CYS A HA   1 
ATOM   2255 H  HB3  A CYS A 1 182 ? 22.271 -10.476 26.049 0.915 9.15  ? 182  CYS A HB3  1 
ATOM   2256 N  N    . ALA A 1 183 ? 19.744 -8.003  26.014 1.000 7.02  ? 183  ALA A N    1 
ATOM   2257 C  CA   . ALA A 1 183 ? 19.777 -6.601  25.606 1.000 7.44  ? 183  ALA A CA   1 
ATOM   2258 C  C    . ALA A 1 183 ? 19.662 -5.700  26.806 1.000 6.90  ? 183  ALA A C    1 
ATOM   2259 O  O    . ALA A 1 183 ? 19.111 -6.083  27.850 1.000 7.15  ? 183  ALA A O    1 
ATOM   2260 C  CB   . ALA A 1 183 ? 18.606 -6.335  24.628 1.000 9.80  ? 183  ALA A CB   1 
ATOM   2261 H  HA   . ALA A 1 183 ? 20.625 -6.420  25.149 1.000 8.93  ? 183  ALA A HA   1 
ATOM   2262 N  N    . ARG A 1 184 ? 20.036 -4.450  26.650 1.000 7.25  ? 184  ARG A N    1 
ATOM   2263 C  CA   . ARG A 1 184 ? 19.975 -3.477  27.738 1.000 7.37  ? 184  ARG A CA   1 
ATOM   2264 C  C    . ARG A 1 184 ? 18.561 -3.130  28.149 1.000 6.69  ? 184  ARG A C    1 
ATOM   2265 O  O    . ARG A 1 184 ? 18.397 -2.588  29.246 1.000 7.30  ? 184  ARG A O    1 
ATOM   2266 C  CB   . ARG A 1 184 ? 20.737 -2.220  27.378 1.000 7.05  ? 184  ARG A CB   1 
ATOM   2267 C  CG   . ARG A 1 184 ? 22.257 -2.445  27.432 1.000 7.66  ? 184  ARG A CG   1 
ATOM   2268 C  CD   . ARG A 1 184 ? 22.996 -1.201  27.014 1.000 8.34  ? 184  ARG A CD   1 
ATOM   2269 N  NE   . ARG A 1 184 ? 24.445 -1.364  27.135 1.000 8.26  ? 184  ARG A NE   1 
ATOM   2270 C  CZ   . ARG A 1 184 ? 25.128 -1.164  28.265 1.000 7.99  ? 184  ARG A CZ   1 
ATOM   2271 N  NH1  . ARG A 1 184 ? 24.530 -0.780  29.383 1.000 9.10  ? 184  ARG A NH1  1 
ATOM   2272 N  NH2  . ARG A 1 184 ? 26.431 -1.351  28.243 1.000 10.04 ? 184  ARG A NH2  1 
ATOM   2273 H  H    . ARG A 1 184 ? 20.327 -4.196  25.881 1.000 8.70  ? 184  ARG A H    1 
ATOM   2274 H  HB2  . ARG A 1 184 ? 20.486 -1.937  26.485 1.000 8.46  ? 184  ARG A HB2  1 
ATOM   2275 H  HB3  . ARG A 1 184 ? 20.496 -1.511  27.995 1.000 8.46  ? 184  ARG A HB3  1 
ATOM   2276 H  HG2  . ARG A 1 184 ? 22.517 -2.687  28.334 1.000 9.19  ? 184  ARG A HG2  1 
ATOM   2277 H  HG3  . ARG A 1 184 ? 22.497 -3.177  26.842 1.000 9.19  ? 184  ARG A HG3  1 
ATOM   2278 H  HH21 . ARG A 1 184 ? 26.896 -1.223  28.956 1.000 12.05 ? 184  ARG A HH21 1 
ATOM   2279 H  HH22 . ARG A 1 184 ? 26.818 -1.600  27.517 1.000 12.05 ? 184  ARG A HH22 1 
ATOM   2280 N  N    . ASN A 1 185 ? 17.545 -3.457  27.312 1.000 6.79  ? 185  ASN A N    1 
ATOM   2281 C  CA   . ASN A 1 185 ? 16.151 -3.246  27.606 1.000 7.17  ? 185  ASN A CA   1 
ATOM   2282 C  C    . ASN A 1 185 ? 15.383 -4.556  27.786 1.000 6.82  ? 185  ASN A C    1 
ATOM   2283 O  O    . ASN A 1 185 ? 14.147 -4.599  27.687 1.000 7.99  ? 185  ASN A O    1 
ATOM   2284 C  CB   . ASN A 1 185 ? 15.513 -2.358  26.520 1.000 6.98  ? 185  ASN A CB   1 
ATOM   2285 C  CG   . ASN A 1 185 ? 15.614 -2.976  25.186 1.000 7.14  ? 185  ASN A CG   1 
ATOM   2286 O  OD1  . ASN A 1 185 ? 15.928 -4.173  25.036 1.000 9.10  ? 185  ASN A OD1  1 
ATOM   2287 N  ND2  . ASN A 1 185 ? 15.366 -2.188  24.135 1.000 7.97  ? 185  ASN A ND2  1 
ATOM   2288 H  H    . ASN A 1 185 ? 17.746 -3.815  26.556 1.000 8.15  ? 185  ASN A H    1 
ATOM   2289 H  HA   . ASN A 1 185 ? 16.100 -2.757  28.453 1.000 8.60  ? 185  ASN A HA   1 
ATOM   2290 H  HB2  . ASN A 1 185 ? 14.579 -2.210  26.734 1.000 8.38  ? 185  ASN A HB2  1 
ATOM   2291 H  HB3  . ASN A 1 185 ? 15.957 -1.496  26.509 1.000 8.38  ? 185  ASN A HB3  1 
ATOM   2292 H  HD21 . ASN A 1 185 ? 15.436 -2.498  23.336 1.000 9.56  ? 185  ASN A HD21 1 
ATOM   2293 N  N    . ALA A 1 186 ? 16.091 -5.634  28.097 1.000 6.92  ? 186  ALA A N    1 
ATOM   2294 C  CA   . ALA A 1 186 ? 15.529 -6.964  28.244 1.000 7.88  ? 186  ALA A CA   1 
ATOM   2295 C  C    . ALA A 1 186 ? 14.602 -7.084  29.420 1.000 6.63  ? 186  ALA A C    1 
ATOM   2296 O  O    . ALA A 1 186 ? 14.566 -6.222  30.320 1.000 6.58  ? 186  ALA A O    1 
ATOM   2297 C  CB   . ALA A 1 186 ? 16.688 -7.953  28.485 1.000 11.04 ? 186  ALA A CB   1 
ATOM   2298 H  H    . ALA A 1 186 ? 16.937 -5.539  28.220 1.000 8.31  ? 186  ALA A H    1 
ATOM   2299 N  N    . PRO A 1 187 ? 13.866 -8.194  29.524 1.000 6.91  ? 187  PRO A N    1 
ATOM   2300 C  CA   . PRO A 1 187 ? 12.993 -8.401  30.681 1.000 7.45  ? 187  PRO A CA   1 
ATOM   2301 C  C    . PRO A 1 187 ? 13.670 -8.255  32.034 1.000 7.11  ? 187  PRO A C    1 
ATOM   2302 O  O    . PRO A 1 187 ? 13.054 -7.723  32.966 1.000 9.01  ? 187  PRO A O    1 
ATOM   2303 C  CB   . PRO A 1 187 ? 12.428 -9.809  30.440 1.000 9.01  ? 187  PRO A CB   1 
ATOM   2304 C  CG   . PRO A 1 187 ? 12.323 -9.880  28.908 1.000 10.17 ? 187  PRO A CG   1 
ATOM   2305 C  CD   . PRO A 1 187 ? 13.662 -9.245  28.497 1.000 8.72  ? 187  PRO A CD   1 
ATOM   2306 H  HA   . PRO A 1 187 ? 12.256 -7.758  30.632 1.000 8.94  ? 187  PRO A HA   1 
ATOM   2307 H  HB2  . PRO A 1 187 ? 13.028 -10.490 30.782 1.000 10.81 ? 187  PRO A HB2  1 
ATOM   2308 H  HB3  . PRO A 1 187 ? 11.558 -9.913  30.856 1.000 10.81 ? 187  PRO A HB3  1 
ATOM   2309 H  HD3  . PRO A 1 187 ? 13.511 -8.796  27.667 1.000 10.46 ? 187  PRO A HD3  1 
ATOM   2310 N  N    . TYR A 1 188 ? 14.915 -8.708  32.177 1.000 5.92  ? 188  TYR A N    1 
ATOM   2311 C  CA   . TYR A 1 188 ? 15.610 -8.613  33.460 1.000 5.72  ? 188  TYR A CA   1 
ATOM   2312 C  C    . TYR A 1 188 ? 16.488 -7.363  33.572 1.000 5.49  ? 188  TYR A C    1 
ATOM   2313 O  O    . TYR A 1 188 ? 17.305 -7.246  34.467 1.000 6.16  ? 188  TYR A O    1 
ATOM   2314 C  CB   . TYR A 1 188 ? 16.423 -9.872  33.734 1.000 6.30  ? 188  TYR A CB   1 
ATOM   2315 C  CG   . TYR A 1 188 ? 15.612 -11.077 34.170 1.000 5.87  ? 188  TYR A CG   1 
ATOM   2316 C  CD1  . TYR A 1 188 ? 14.282 -11.047 34.526 1.000 6.74  ? 188  TYR A CD1  1 
ATOM   2317 C  CD2  . TYR A 1 188 ? 16.265 -12.292 34.281 1.000 6.46  ? 188  TYR A CD2  1 
ATOM   2318 C  CE1  . TYR A 1 188 ? 13.621 -12.187 34.965 1.000 7.17  ? 188  TYR A CE1  1 
ATOM   2319 C  CE2  . TYR A 1 188 ? 15.648 -13.432 34.751 1.000 7.34  ? 188  TYR A CE2  1 
ATOM   2320 C  CZ   . TYR A 1 188 ? 14.303 -13.389 35.085 1.000 7.19  ? 188  TYR A CZ   1 
ATOM   2321 O  OH   . TYR A 1 188 ? 13.723 -14.523 35.532 1.000 8.56  ? 188  TYR A OH   1 
ATOM   2322 H  HA   . TYR A 1 188 ? 14.925 -8.551  34.159 1.000 6.87  ? 188  TYR A HA   1 
ATOM   2323 H  HB2  . TYR A 1 188 ? 16.911 -10.104 32.928 1.000 7.57  ? 188  TYR A HB2  1 
ATOM   2324 H  HB3  . TYR A 1 188 ? 17.075 -9.674  34.423 1.000 7.57  ? 188  TYR A HB3  1 
ATOM   2325 H  HD1  . TYR A 1 188 ? 13.815 -10.244 34.471 1.000 8.09  ? 188  TYR A HD1  1 
ATOM   2326 H  HD2  . TYR A 1 188 ? 17.159 -12.342 34.028 1.000 7.76  ? 188  TYR A HD2  1 
ATOM   2327 H  HE1  . TYR A 1 188 ? 12.716 -12.145 35.179 1.000 8.61  ? 188  TYR A HE1  1 
ATOM   2328 H  HE2  . TYR A 1 188 ? 16.129 -14.223 34.843 1.000 8.81  ? 188  TYR A HE2  1 
ATOM   2329 H  HH   . TYR A 1 188 ? 12.909 -14.422 35.558 1.000 12.84 ? 188  TYR A HH   1 
ATOM   2330 N  N    . SER A 1 189 ? 16.286 -6.371  32.694 1.000 5.64  ? 189  SER A N    1 
ATOM   2331 C  CA   . SER A 1 189 ? 17.014 -5.136  32.773 1.000 5.55  ? 189  SER A CA   1 
ATOM   2332 C  C    . SER A 1 189 ? 16.424 -4.145  33.752 1.000 4.92  ? 189  SER A C    1 
ATOM   2333 O  O    . SER A 1 189 ? 15.255 -4.187  34.110 1.000 5.58  ? 189  SER A O    1 
ATOM   2334 C  CB   . SER A 1 189 ? 17.170 -4.476  31.402 1.000 6.23  ? 189  SER A CB   1 
ATOM   2335 O  OG   . SER A 1 189 ? 15.935 -3.976  30.920 1.000 6.22  ? 189  SER A OG   1 
ATOM   2336 H  H    . SER A 1 189 ? 15.706 -6.476  32.068 1.000 6.77  ? 189  SER A H    1 
ATOM   2337 H  HA   . SER A 1 189 ? 17.915 -5.353  33.091 1.000 6.66  ? 189  SER A HA   1 
ATOM   2338 H  HB2  . SER A 1 189 ? 17.807 -3.748  31.468 1.000 7.47  ? 189  SER A HB2  1 
ATOM   2339 H  HB3  . SER A 1 189 ? 17.520 -5.125  30.772 1.000 7.47  ? 189  SER A HB3  1 
ATOM   2340 H  HG   . SER A 1 189 ? 15.393 -4.589  30.870 1.000 9.33  ? 189  SER A HG   1 
ATOM   2341 N  N    . GLY A 1 190 ? 17.277 -3.192  34.136 1.000 5.01  ? 190  GLY A N    1 
ATOM   2342 C  CA   . GLY A 1 190 ? 16.846 -2.173  35.093 1.000 5.11  ? 190  GLY A CA   1 
ATOM   2343 C  C    . GLY A 1 190 ? 16.806 -2.700  36.487 1.000 5.02  ? 190  GLY A C    1 
ATOM   2344 O  O    . GLY A 1 190 ? 16.976 -3.896  36.770 1.000 5.24  ? 190  GLY A O    1 
ATOM   2345 H  HA2  . GLY A 1 190 ? 17.456 -1.419  35.054 1.000 6.14  ? 190  GLY A HA2  1 
ATOM   2346 H  HA3  . GLY A 1 190 ? 15.963 -1.855  34.846 1.000 6.14  ? 190  GLY A HA3  1 
ATOM   2347 N  N    . TYR A 1 191 ? 16.554 -1.783  37.435 1.000 4.88  ? 191  TYR A N    1 
ATOM   2348 C  CA   . TYR A 1 191 ? 16.423 -2.200  38.830 1.000 5.10  ? 191  TYR A CA   1 
ATOM   2349 C  C    . TYR A 1 191 ? 15.335 -3.266  38.973 1.000 4.92  ? 191  TYR A C    1 
ATOM   2350 O  O    . TYR A 1 191 ? 15.495 -4.243  39.716 1.000 5.38  ? 191  TYR A O    1 
ATOM   2351 C  CB   . TYR A 1 191 ? 16.062 -1.011  39.692 1.000 5.11  ? 191  TYR A CB   1 
ATOM   2352 C  CG   . TYR A 1 191 ? 16.957 0.185   39.550 1.000 4.64  ? 191  TYR A CG   1 
ATOM   2353 C  CD1  . TYR A 1 191 ? 18.191 0.261   40.178 1.000 4.88  ? 191  TYR A CD1  1 
ATOM   2354 C  CD2  . TYR A 1 191 ? 16.555 1.272   38.799 1.000 5.15  ? 191  TYR A CD2  1 
ATOM   2355 C  CE1  . TYR A 1 191 ? 19.003 1.372   40.049 1.000 4.74  ? 191  TYR A CE1  1 
ATOM   2356 C  CE2  . TYR A 1 191 ? 17.358 2.392   38.679 1.000 5.16  ? 191  TYR A CE2  1 
ATOM   2357 C  CZ   . TYR A 1 191 ? 18.581 2.483   39.316 1.000 4.76  ? 191  TYR A CZ   1 
ATOM   2358 O  OH   . TYR A 1 191 ? 19.298 3.626   39.276 1.000 5.08  ? 191  TYR A OH   1 
ATOM   2359 H  HA   . TYR A 1 191 ? 17.278 -2.570  39.136 1.000 6.12  ? 191  TYR A HA   1 
ATOM   2360 H  HB2  . TYR A 1 191 ? 15.155 -0.742  39.477 1.000 6.14  ? 191  TYR A HB2  1 
ATOM   2361 H  HB3  . TYR A 1 191 ? 16.071 -1.292  40.620 1.000 6.14  ? 191  TYR A HB3  1 
ATOM   2362 H  HD1  . TYR A 1 191 ? 18.480 -0.453  40.699 1.000 5.85  ? 191  TYR A HD1  1 
ATOM   2363 H  HD2  . TYR A 1 191 ? 15.732 1.250   38.367 1.000 6.18  ? 191  TYR A HD2  1 
ATOM   2364 H  HE1  . TYR A 1 191 ? 19.839 1.379   40.455 1.000 5.69  ? 191  TYR A HE1  1 
ATOM   2365 H  HE2  . TYR A 1 191 ? 17.067 3.103   38.155 1.000 6.19  ? 191  TYR A HE2  1 
ATOM   2366 N  N    . SER A 1 192 ? 14.187 -3.020  38.327 1.000 5.14  ? 192  SER A N    1 
ATOM   2367 C  CA   . SER A 1 192 ? 13.058 -3.951  38.514 1.000 5.33  ? 192  SER A CA   1 
ATOM   2368 C  C    . SER A 1 192 ? 13.290 -5.249  37.803 1.000 5.19  ? 192  SER A C    1 
ATOM   2369 O  O    . SER A 1 192 ? 12.878 -6.302  38.310 1.000 5.92  ? 192  SER A O    1 
ATOM   2370 C  CB   . SER A 1 192 ? 11.752 -3.262  38.084 1.000 6.30  ? 192  SER A CB   1 
ATOM   2371 O  OG   . SER A 1 192 ? 11.407 -2.232  38.984 1.000 6.86  ? 192  SER A OG   1 
ATOM   2372 H  HA   . SER A 1 192 ? 12.989 -4.145  39.472 1.000 6.40  ? 192  SER A HA   1 
ATOM   2373 N  N    . GLY A 1 193 ? 13.918 -5.247  36.632 1.000 5.18  ? 193  GLY A N    1 
ATOM   2374 C  CA   . GLY A 1 193 ? 14.225 -6.493  35.977 1.000 5.37  ? 193  GLY A CA   1 
ATOM   2375 C  C    . GLY A 1 193 ? 15.210 -7.336  36.821 1.000 4.98  ? 193  GLY A C    1 
ATOM   2376 O  O    . GLY A 1 193 ? 15.051 -8.549  36.924 1.000 6.00  ? 193  GLY A O    1 
ATOM   2377 H  H    . GLY A 1 193 ? 14.140 -4.501  36.265 1.000 6.21  ? 193  GLY A H    1 
ATOM   2378 H  HA2  . GLY A 1 193 ? 13.407 -6.995  35.839 1.000 6.45  ? 193  GLY A HA2  1 
ATOM   2379 H  HA3  . GLY A 1 193 ? 14.618 -6.313  35.109 1.000 6.45  ? 193  GLY A HA3  1 
ATOM   2380 N  N    . ALA A 1 194 ? 16.209 -6.672  37.424 1.000 5.16  ? 194  ALA A N    1 
ATOM   2381 C  CA   . ALA A 1 194 ? 17.162 -7.414  38.239 1.000 5.27  ? 194  ALA A CA   1 
ATOM   2382 C  C    . ALA A 1 194 ? 16.502 -7.967  39.477 1.000 5.38  ? 194  ALA A C    1 
ATOM   2383 O  O    . ALA A 1 194 ? 16.798 -9.095  39.898 1.000 5.92  ? 194  ALA A O    1 
ATOM   2384 C  CB   . ALA A 1 194 ? 18.345 -6.505  38.581 1.000 5.62  ? 194  ALA A CB   1 
ATOM   2385 H  H    . ALA A 1 194 ? 16.285 -5.821  37.331 1.000 6.19  ? 194  ALA A H    1 
ATOM   2386 H  HA   . ALA A 1 194 ? 17.498 -8.167  37.709 1.000 6.32  ? 194  ALA A HA   1 
ATOM   2387 H  HB1  . ALA A 1 194 ? 18.977 -6.994  39.112 1.000 8.42  ? 194  ALA A HB1  1 
ATOM   2388 H  HB3  . ALA A 1 194 ? 18.035 -5.741  39.073 1.000 8.42  ? 194  ALA A HB3  1 
ATOM   2389 N  N    . PHE A 1 195 ? 15.579 -7.211  40.075 1.000 5.45  ? 195  PHE A N    1 
ATOM   2390 C  CA   . PHE A 1 195 ? 14.808 -7.754  41.206 1.000 5.71  ? 195  PHE A CA   1 
ATOM   2391 C  C    . PHE A 1 195 ? 14.037 -8.998  40.786 1.000 5.75  ? 195  PHE A C    1 
ATOM   2392 O  O    . PHE A 1 195 ? 14.007 -9.981  41.511 1.000 6.19  ? 195  PHE A O    1 
ATOM   2393 C  CB   . PHE A 1 195 ? 13.850 -6.670  41.759 1.000 7.02  ? 195  PHE A CB   1 
ATOM   2394 C  CG   . PHE A 1 195 ? 12.920 -7.282  42.791 1.000 7.13  ? 195  PHE A CG   1 
ATOM   2395 C  CD1  . PHE A 1 195 ? 13.337 -7.450  44.083 1.000 7.90  ? 195  PHE A CD1  1 
ATOM   2396 C  CD2  . PHE A 1 195 ? 11.667 -7.691  42.428 1.000 8.41  ? 195  PHE A CD2  1 
ATOM   2397 C  CE1  . PHE A 1 195 ? 12.480 -8.118  45.006 1.000 9.23  ? 195  PHE A CE1  1 
ATOM   2398 C  CE2  . PHE A 1 195 ? 10.820 -8.346  43.302 1.000 9.10  ? 195  PHE A CE2  1 
ATOM   2399 C  CZ   . PHE A 1 195 ? 11.241 -8.517  44.591 1.000 9.46  ? 195  PHE A CZ   1 
ATOM   2400 H  H    . PHE A 1 195 ? 15.435 -6.409  39.800 1.000 6.54  ? 195  PHE A H    1 
ATOM   2401 H  HA   . PHE A 1 195 ? 15.436 -8.004  41.916 1.000 6.85  ? 195  PHE A HA   1 
ATOM   2402 H  HB2  . PHE A 1 195 ? 14.365 -5.956  42.165 1.000 8.43  ? 195  PHE A HB2  1 
ATOM   2403 H  HB3  . PHE A 1 195 ? 13.330 -6.293  41.032 1.000 8.43  ? 195  PHE A HB3  1 
ATOM   2404 H  HD1  . PHE A 1 195 ? 14.168 -7.134  44.356 1.000 9.47  ? 195  PHE A HD1  1 
ATOM   2405 H  HD2  . PHE A 1 195 ? 11.375 -7.522  41.561 1.000 10.09 ? 195  PHE A HD2  1 
ATOM   2406 H  HZ   . PHE A 1 195 ? 10.667 -8.918  45.204 1.000 11.35 ? 195  PHE A HZ   1 
ATOM   2407 N  N    . HIS A 1 196 ? 13.360 -8.946  39.634 1.000 5.97  ? 196  HIS A N    1 
ATOM   2408 C  CA   . HIS A 1 196 ? 12.591 -10.104 39.191 1.000 6.20  ? 196  HIS A CA   1 
ATOM   2409 C  C    . HIS A 1 196 ? 13.491 -11.298 38.878 1.000 6.04  ? 196  HIS A C    1 
ATOM   2410 O  O    . HIS A 1 196 ? 13.102 -12.424 39.115 1.000 6.76  ? 196  HIS A O    1 
ATOM   2411 C  CB   . HIS A 1 196 ? 11.659 -9.742  38.048 1.000 7.26  ? 196  HIS A CB   1 
ATOM   2412 C  CG   . HIS A 1 196 ? 10.443 -9.036  38.573 1.000 7.32  ? 196  HIS A CG   1 
ATOM   2413 N  ND1  . HIS A 1 196 ? 9.376  -9.776  39.097 1.000 11.84 ? 196  HIS A ND1  1 
ATOM   2414 C  CD2  . HIS A 1 196 ? 10.182 -7.717  38.778 1.000 7.82  ? 196  HIS A CD2  1 
ATOM   2415 C  CE1  . HIS A 1 196 ? 8.490  -8.889  39.543 1.000 11.68 ? 196  HIS A CE1  1 
ATOM   2416 N  NE2  . HIS A 1 196 ? 8.932  -7.666  39.350 1.000 9.10  ? 196  HIS A NE2  1 
ATOM   2417 H  H    . HIS A 1 196 ? 13.378 -8.232  39.155 1.000 7.17  ? 196  HIS A H    1 
ATOM   2418 H  HA   . HIS A 1 196 ? 12.023 -10.370 39.944 1.000 7.44  ? 196  HIS A HA   1 
ATOM   2419 H  HB2  . HIS A 1 196 ? 12.123 -9.167  37.420 1.000 8.71  ? 196  HIS A HB2  1 
ATOM   2420 H  HB3  . HIS A 1 196 ? 11.391 -10.547 37.579 1.000 8.71  ? 196  HIS A HB3  1 
ATOM   2421 H  HE2  . HIS A 1 196 ? 8.506  -6.947  39.551 1.000 10.92 ? 196  HIS A HE2  1 
ATOM   2422 N  N    . CYS A 1 197 ? 14.708 -11.032 38.393 1.000 5.94  ? 197  CYS A N    1 
ATOM   2423 C  CA   . CYS A 1 197 ? 15.707 -12.090 38.221 1.000 6.48  ? 197  CYS A CA   1 
ATOM   2424 C  C    . CYS A 1 197 ? 15.984 -12.810 39.562 1.000 6.25  ? 197  CYS A C    1 
ATOM   2425 O  O    . CYS A 1 197 ? 16.019 -14.036 39.614 1.000 7.01  ? 197  CYS A O    1 
ATOM   2426 C  CB   . CYS A 1 197 ? 16.918 -11.431 37.600 1.000 6.08  ? 197  CYS A CB   1 
ATOM   2427 S  SG   . CYS A 1 197 ? 18.417 -12.399 37.403 1.000 7.12  ? 197  CYS A SG   1 
ATOM   2428 H  HB2  . CYS A 1 197 ? 16.660 -11.107 36.723 1.000 7.30  ? 197  CYS A HB2  1 
ATOM   2429 H  HB3  . CYS A 1 197 ? 17.138 -10.654 38.137 1.000 7.30  ? 197  CYS A HB3  1 
ATOM   2430 N  N    . LEU A 1 198 ? 16.085 -12.055 40.651 1.000 5.77  ? 198  LEU A N    1 
ATOM   2431 C  CA   . LEU A 1 198 ? 16.304 -12.648 41.990 1.000 6.21  ? 198  LEU A CA   1 
ATOM   2432 C  C    . LEU A 1 198 ? 15.021 -13.396 42.395 1.000 6.24  ? 198  LEU A C    1 
ATOM   2433 O  O    . LEU A 1 198 ? 15.064 -14.559 42.819 1.000 7.03  ? 198  LEU A O    1 
ATOM   2434 C  CB   . LEU A 1 198 ? 16.604 -11.546 42.989 1.000 6.19  ? 198  LEU A CB   1 
ATOM   2435 C  CG   . LEU A 1 198 ? 16.566 -11.949 44.450 1.000 6.76  ? 198  LEU A CG   1 
ATOM   2436 C  CD1  . LEU A 1 198 ? 17.719 -12.857 44.836 1.000 8.23  ? 198  LEU A CD1  1 
ATOM   2437 C  CD2  . LEU A 1 198 ? 16.595 -10.697 45.325 1.000 7.63  ? 198  LEU A CD2  1 
ATOM   2438 H  H    . LEU A 1 198 ? 16.022 -11.200 40.577 1.000 6.92  ? 198  LEU A H    1 
ATOM   2439 H  HB2  . LEU A 1 198 ? 17.485 -11.190 42.794 1.000 7.43  ? 198  LEU A HB2  1 
ATOM   2440 H  HB3  . LEU A 1 198 ? 15.964 -10.830 42.853 1.000 7.43  ? 198  LEU A HB3  1 
ATOM   2441 H  HG   . LEU A 1 198 ? 15.726 -12.425 44.619 1.000 8.12  ? 198  LEU A HG   1 
ATOM   2442 H  HD11 . LEU A 1 198 ? 17.651 -13.083 45.767 1.000 12.35 ? 198  LEU A HD11 1 
ATOM   2443 H  HD12 . LEU A 1 198 ? 17.685 -13.659 44.309 1.000 12.35 ? 198  LEU A HD12 1 
ATOM   2444 H  HD13 . LEU A 1 198 ? 18.550 -12.405 44.677 1.000 12.35 ? 198  LEU A HD13 1 
ATOM   2445 H  HD23 . LEU A 1 198 ? 15.829 -10.156 45.123 1.000 11.44 ? 198  LEU A HD23 1 
ATOM   2446 N  N    . LYS A 1 199 ? 13.865 -12.742 42.310 1.000 6.61  ? 199  LYS A N    1 
ATOM   2447 C  CA   . LYS A 1 199 ? 12.584 -13.335 42.699 1.000 7.05  ? 199  LYS A CA   1 
ATOM   2448 C  C    . LYS A 1 199 ? 12.373 -14.670 41.984 1.000 6.66  ? 199  LYS A C    1 
ATOM   2449 O  O    . LYS A 1 199 ? 11.896 -15.638 42.618 1.000 7.95  ? 199  LYS A O    1 
ATOM   2450 C  CB   . LYS A 1 199 ? 11.470 -12.365 42.429 1.000 7.20  ? 199  LYS A CB   1 
ATOM   2451 C  CG   . LYS A 1 199 ? 10.086 -12.922 42.683 1.000 8.49  ? 199  LYS A CG   1 
ATOM   2452 C  CD   . LYS A 1 199 ? 9.028  -11.851 42.480 1.000 10.38 ? 199  LYS A CD   1 
ATOM   2453 C  CE   . LYS A 1 199 ? 7.582  -12.366 42.512 1.000 14.08 ? 199  LYS A CE   1 
ATOM   2454 N  NZ   . LYS A 1 199 ? 7.295  -13.295 41.363 1.000 16.76 ? 199  LYS A NZ   1 
ATOM   2455 H  H    . LYS A 1 199 ? 13.871 -11.935 42.013 1.000 7.93  ? 199  LYS A H    1 
ATOM   2456 H  HA   . LYS A 1 199 ? 12.610 -13.508 43.663 1.000 8.46  ? 199  LYS A HA   1 
ATOM   2457 H  HB2  . LYS A 1 199 ? 11.597 -11.582 42.987 1.000 8.64  ? 199  LYS A HB2  1 
ATOM   2458 H  HB3  . LYS A 1 199 ? 11.524 -12.079 41.504 1.000 8.64  ? 199  LYS A HB3  1 
ATOM   2459 H  HE2  . LYS A 1 199 ? 7.481  -12.863 43.321 1.000 16.89 ? 199  LYS A HE2  1 
ATOM   2460 N  N    . ASP A 1 200 ? 12.676 -14.702 40.721 1.000 6.76  ? 200  ASP A N    1 
ATOM   2461 C  CA   . ASP A 1 200 ? 12.489 -15.877 39.856 1.000 7.02  ? 200  ASP A CA   1 
ATOM   2462 C  C    . ASP A 1 200 ? 13.524 -16.956 40.097 1.000 7.45  ? 200  ASP A C    1 
ATOM   2463 O  O    . ASP A 1 200 ? 13.439 -18.035 39.448 1.000 8.91  ? 200  ASP A O    1 
ATOM   2464 C  CB   . ASP A 1 200 ? 12.499 -15.444 38.396 1.000 7.65  ? 200  ASP A CB   1 
ATOM   2465 C  CG   . ASP A 1 200 ? 11.361 -14.600 37.941 1.000 8.26  ? 200  ASP A CG   1 
ATOM   2466 O  OD1  . ASP A 1 200 ? 10.382 -14.439 38.671 1.000 8.69  ? 200  ASP A OD1  1 
ATOM   2467 O  OD2  . ASP A 1 200 ? 11.459 -14.097 36.777 1.000 9.22  ? 200  ASP A OD2  1 
ATOM   2468 H  H    . ASP A 1 200 ? 13.007 -13.992 40.368 1.000 8.12  ? 200  ASP A H    1 
ATOM   2469 H  HA   . ASP A 1 200 ? 11.607 -16.257 40.051 1.000 8.42  ? 200  ASP A HA   1 
ATOM   2470 H  HB2  . ASP A 1 200 ? 13.321 -14.955 38.232 1.000 9.18  ? 200  ASP A HB2  1 
ATOM   2471 H  HB3  . ASP A 1 200 ? 12.522 -16.241 37.844 1.000 9.18  ? 200  ASP A HB3  1 
ATOM   2472 N  N    . GLY A 1 201 ? 14.506 -16.735 40.949 1.000 7.17  ? 201  GLY A N    1 
ATOM   2473 C  CA   . GLY A 1 201 ? 15.508 -17.771 41.229 1.000 7.89  ? 201  GLY A CA   1 
ATOM   2474 C  C    . GLY A 1 201 ? 16.625 -17.830 40.247 1.000 8.02  ? 201  GLY A C    1 
ATOM   2475 O  O    . GLY A 1 201 ? 17.402 -18.775 40.280 1.000 10.40 ? 201  GLY A O    1 
ATOM   2476 H  HA2  . GLY A 1 201 ? 15.881 -17.608 42.110 1.000 9.47  ? 201  GLY A HA2  1 
ATOM   2477 N  N    . LYS A 1 202 ? 16.749 -16.812 39.377 1.000 7.03  ? 202  LYS A N    1 
ATOM   2478 C  CA   . LYS A 1 202 ? 17.821 -16.774 38.398 1.000 7.11  ? 202  LYS A CA   1 
ATOM   2479 C  C    . LYS A 1 202 ? 19.078 -16.109 38.922 1.000 7.12  ? 202  LYS A C    1 
ATOM   2480 O  O    . LYS A 1 202 ? 20.133 -16.263 38.318 1.000 9.05  ? 202  LYS A O    1 
ATOM   2481 C  CB   . LYS A 1 202 ? 17.304 -16.142 37.115 1.000 7.41  ? 202  LYS A CB   1 
ATOM   2482 C  CG   . LYS A 1 202 ? 16.314 -17.026 36.352 1.000 9.63  ? 202  LYS A CG   1 
ATOM   2483 C  CD   . LYS A 1 202 ? 16.965 -18.320 35.882 1.000 20.95 ? 202  LYS A CD   1 
ATOM   2484 C  CE   . LYS A 1 202 ? 16.089 -19.133 34.961 1.000 26.61 ? 202  LYS A CE   1 
ATOM   2485 N  NZ   . LYS A 1 202 ? 16.932 -20.245 34.417 1.000 36.40 ? 202  LYS A NZ   1 
ATOM   2486 H  H    . LYS A 1 202 ? 16.180 -16.168 39.401 1.000 8.43  ? 202  LYS A H    1 
ATOM   2487 H  HA   . LYS A 1 202 ? 18.052 -17.703 38.188 1.000 8.53  ? 202  LYS A HA   1 
ATOM   2488 H  HB2  . LYS A 1 202 ? 16.871 -15.302 37.332 1.000 8.89  ? 202  LYS A HB2  1 
ATOM   2489 H  HB3  . LYS A 1 202 ? 18.058 -15.945 36.537 1.000 8.89  ? 202  LYS A HB3  1 
ATOM   2490 H  HG2  . LYS A 1 202 ? 15.618 -17.261 36.956 1.000 11.55 ? 202  LYS A HG2  1 
ATOM   2491 N  N    . GLY A 1 203 ? 18.997 -15.407 40.051 1.000 7.14  ? 203  GLY A N    1 
ATOM   2492 C  CA   . GLY A 1 203 ? 20.143 -14.977 40.787 1.000 6.88  ? 203  GLY A CA   1 
ATOM   2493 C  C    . GLY A 1 203 ? 19.945 -15.211 42.261 1.000 6.98  ? 203  GLY A C    1 
ATOM   2494 O  O    . GLY A 1 203 ? 18.825 -15.210 42.750 1.000 8.76  ? 203  GLY A O    1 
ATOM   2495 H  H    . GLY A 1 203 ? 18.218 -15.202 40.352 1.000 8.57  ? 203  GLY A H    1 
ATOM   2496 H  HA2  . GLY A 1 203 ? 20.929 -15.457 40.479 1.000 8.25  ? 203  GLY A HA2  1 
ATOM   2497 N  N    . ASP A 1 204 ? 21.078 -15.354 42.973 1.000 6.74  ? 204  ASP A N    1 
ATOM   2498 C  CA   . ASP A 1 204 ? 21.120 -15.371 44.410 1.000 6.88  ? 204  ASP A CA   1 
ATOM   2499 C  C    . ASP A 1 204 ? 21.133 -13.962 45.018 1.000 6.51  ? 204  ASP A C    1 
ATOM   2500 O  O    . ASP A 1 204 ? 20.844 -13.782 46.208 1.000 7.32  ? 204  ASP A O    1 
ATOM   2501 C  CB   . ASP A 1 204 ? 22.401 -16.093 44.891 1.000 7.87  ? 204  ASP A CB   1 
ATOM   2502 C  CG   . ASP A 1 204 ? 22.403 -17.567 44.499 1.000 9.31  ? 204  ASP A CG   1 
ATOM   2503 O  OD1  . ASP A 1 204 ? 23.394 -17.981 43.892 1.000 10.53 ? 204  ASP A OD1  1 
ATOM   2504 O  OD2  . ASP A 1 204 ? 21.407 -18.264 44.842 1.000 13.19 ? 204  ASP A OD2  1 
ATOM   2505 H  H    . ASP A 1 204 ? 21.818 -15.440 42.545 1.000 8.09  ? 204  ASP A H    1 
ATOM   2506 H  HA   . ASP A 1 204 ? 20.336 -15.855 44.745 1.000 8.26  ? 204  ASP A HA   1 
ATOM   2507 H  HB3  . ASP A 1 204 ? 22.418 -16.071 45.847 1.000 9.44  ? 204  ASP A HB3  1 
ATOM   2508 N  N    . VAL A 1 205 ? 21.484 -12.971 44.200 1.000 6.69  ? 205  VAL A N    1 
ATOM   2509 C  CA   . VAL A 1 205 ? 21.651 -11.589 44.628 1.000 6.22  ? 205  VAL A CA   1 
ATOM   2510 C  C    . VAL A 1 205 ? 21.266 -10.713 43.463 1.000 5.84  ? 205  VAL A C    1 
ATOM   2511 O  O    . VAL A 1 205 ? 21.541 -11.050 42.302 1.000 6.94  ? 205  VAL A O    1 
ATOM   2512 C  CB   . VAL A 1 205 ? 23.073 -11.332 45.115 1.000 6.53  ? 205  VAL A CB   1 
ATOM   2513 C  CG1  . VAL A 1 205 ? 24.118 -11.617 44.027 1.000 7.30  ? 205  VAL A CG1  1 
ATOM   2514 C  CG2  . VAL A 1 205 ? 23.265 -9.904  45.663 1.000 7.01  ? 205  VAL A CG2  1 
ATOM   2515 H  H    . VAL A 1 205 ? 21.621 -13.158 43.372 1.000 8.03  ? 205  VAL A H    1 
ATOM   2516 H  HA   . VAL A 1 205 ? 21.031 -11.414 45.368 1.000 7.47  ? 205  VAL A HA   1 
ATOM   2517 H  HB   . VAL A 1 205 ? 23.244 -11.953 45.854 1.000 7.84  ? 205  VAL A HB   1 
ATOM   2518 H  HG11 . VAL A 1 205 ? 24.997 -11.443 44.374 1.000 10.95 ? 205  VAL A HG11 1 
ATOM   2519 H  HG12 . VAL A 1 205 ? 24.057 -12.536 43.756 1.000 10.95 ? 205  VAL A HG12 1 
ATOM   2520 H  HG13 . VAL A 1 205 ? 23.955 -11.049 43.271 1.000 10.95 ? 205  VAL A HG13 1 
ATOM   2521 H  HG21 . VAL A 1 205 ? 22.629 -9.740  46.363 1.000 10.51 ? 205  VAL A HG21 1 
ATOM   2522 H  HG23 . VAL A 1 205 ? 23.116 -9.286  44.943 1.000 10.51 ? 205  VAL A HG23 1 
ATOM   2523 N  N    . ALA A 1 206 ? 20.649 -9.568  43.769 1.000 5.51  ? 206  ALA A N    1 
ATOM   2524 C  CA   . ALA A 1 206 ? 20.332 -8.528  42.777 1.000 5.44  ? 206  ALA A CA   1 
ATOM   2525 C  C    . ALA A 1 206 ? 20.961 -7.221  43.257 1.000 5.20  ? 206  ALA A C    1 
ATOM   2526 O  O    . ALA A 1 206 ? 20.770 -6.785  44.374 1.000 6.31  ? 206  ALA A O    1 
ATOM   2527 C  CB   . ALA A 1 206 ? 18.833 -8.351  42.621 1.000 6.75  ? 206  ALA A CB   1 
ATOM   2528 H  H    . ALA A 1 206 ? 20.426 -9.431  44.588 1.000 6.61  ? 206  ALA A H    1 
ATOM   2529 H  HA   . ALA A 1 206 ? 20.721 -8.776  41.912 1.000 6.52  ? 206  ALA A HA   1 
ATOM   2530 H  HB1  . ALA A 1 206 ? 18.666 -7.669  41.967 1.000 10.12 ? 206  ALA A HB1  1 
ATOM   2531 N  N    . PHE A 1 207 ? 21.697 -6.587  42.349 1.000 4.98  ? 207  PHE A N    1 
ATOM   2532 C  CA   . PHE A 1 207 ? 22.391 -5.315  42.618 1.000 4.89  ? 207  PHE A CA   1 
ATOM   2533 C  C    . PHE A 1 207 ? 21.502 -4.197  42.071 1.000 5.02  ? 207  PHE A C    1 
ATOM   2534 O  O    . PHE A 1 207 ? 21.432 -3.982  40.862 1.000 5.44  ? 207  PHE A O    1 
ATOM   2535 C  CB   . PHE A 1 207 ? 23.763 -5.335  41.994 1.000 5.64  ? 207  PHE A CB   1 
ATOM   2536 C  CG   . PHE A 1 207 ? 24.652 -6.377  42.654 1.000 5.34  ? 207  PHE A CG   1 
ATOM   2537 C  CD1  . PHE A 1 207 ? 25.102 -6.181  43.939 1.000 6.17  ? 207  PHE A CD1  1 
ATOM   2538 C  CD2  . PHE A 1 207 ? 25.019 -7.526  41.976 1.000 6.51  ? 207  PHE A CD2  1 
ATOM   2539 C  CE1  . PHE A 1 207 ? 25.952 -7.103  44.552 1.000 6.69  ? 207  PHE A CE1  1 
ATOM   2540 C  CE2  . PHE A 1 207 ? 25.858 -8.471  42.561 1.000 7.05  ? 207  PHE A CE2  1 
ATOM   2541 C  CZ   . PHE A 1 207 ? 26.327 -8.229  43.851 1.000 7.11  ? 207  PHE A CZ   1 
ATOM   2542 H  H    . PHE A 1 207 ? 21.772 -6.936  41.567 1.000 5.98  ? 207  PHE A H    1 
ATOM   2543 H  HA   . PHE A 1 207 ? 22.484 -5.202  43.587 1.000 5.87  ? 207  PHE A HA   1 
ATOM   2544 H  HB2  . PHE A 1 207 ? 23.683 -5.533  41.048 1.000 6.77  ? 207  PHE A HB2  1 
ATOM   2545 H  HB3  . PHE A 1 207 ? 24.170 -4.460  42.084 1.000 6.77  ? 207  PHE A HB3  1 
ATOM   2546 H  HD1  . PHE A 1 207 ? 24.837 -5.423  44.406 1.000 7.41  ? 207  PHE A HD1  1 
ATOM   2547 H  HE1  . PHE A 1 207 ? 26.259 -6.960  45.418 1.000 8.03  ? 207  PHE A HE1  1 
ATOM   2548 N  N    . VAL A 1 208 ? 20.772 -3.572  43.016 1.000 5.14  ? 208  VAL A N    1 
ATOM   2549 C  CA   . VAL A 1 208 ? 19.685 -2.660  42.681 1.000 4.87  ? 208  VAL A CA   1 
ATOM   2550 C  C    . VAL A 1 208 ? 19.751 -1.434  43.630 1.000 4.65  ? 208  VAL A C    1 
ATOM   2551 O  O    . VAL A 1 208 ? 20.845 -1.143  44.187 1.000 5.28  ? 208  VAL A O    1 
ATOM   2552 C  CB   . VAL A 1 208 ? 18.345 -3.376  42.663 1.000 5.43  ? 208  VAL A CB   1 
ATOM   2553 C  CG1  . VAL A 1 208 ? 18.322 -4.468  41.602 1.000 5.95  ? 208  VAL A CG1  1 
ATOM   2554 C  CG2  . VAL A 1 208 ? 18.015 -3.959  44.038 1.000 6.12  ? 208  VAL A CG2  1 
ATOM   2555 H  H    . VAL A 1 208 ? 20.954 -3.715  43.844 1.000 6.17  ? 208  VAL A H    1 
ATOM   2556 H  HA   . VAL A 1 208 ? 19.851 -2.333  41.772 1.000 5.84  ? 208  VAL A HA   1 
ATOM   2557 H  HB   . VAL A 1 208 ? 17.653 -2.720  42.437 1.000 6.51  ? 208  VAL A HB   1 
ATOM   2558 H  HG11 . VAL A 1 208 ? 17.467 -4.904  41.609 1.000 8.92  ? 208  VAL A HG11 1 
ATOM   2559 H  HG12 . VAL A 1 208 ? 18.474 -4.077  40.739 1.000 8.92  ? 208  VAL A HG12 1 
ATOM   2560 H  HG21 . VAL A 1 208 ? 17.169 -4.411  43.998 1.000 9.18  ? 208  VAL A HG21 1 
ATOM   2561 H  HG23 . VAL A 1 208 ? 17.967 -3.244  44.676 1.000 9.18  ? 208  VAL A HG23 1 
ATOM   2562 N  N    . LYS A 1 209 ? 18.649 -0.691  43.759 1.000 5.28  ? 209  LYS A N    1 
ATOM   2563 C  CA   . LYS A 1 209 ? 18.650 0.529   44.568 1.000 5.14  ? 209  LYS A CA   1 
ATOM   2564 C  C    . LYS A 1 209 ? 17.701 0.370   45.730 1.000 5.20  ? 209  LYS A C    1 
ATOM   2565 O  O    . LYS A 1 209 ? 16.968 -0.602  45.907 1.000 5.39  ? 209  LYS A O    1 
ATOM   2566 C  CB   . LYS A 1 209 ? 18.346 1.770   43.748 1.000 5.31  ? 209  LYS A CB   1 
ATOM   2567 C  CG   . LYS A 1 209 ? 16.956 1.871   43.170 1.000 5.21  ? 209  LYS A CG   1 
ATOM   2568 C  CD   . LYS A 1 209 ? 16.646 3.192   42.526 1.000 5.58  ? 209  LYS A CD   1 
ATOM   2569 C  CE   . LYS A 1 209 ? 16.589 4.331   43.546 1.000 6.04  ? 209  LYS A CE   1 
ATOM   2570 N  NZ   . LYS A 1 209 ? 16.392 5.635   42.855 1.000 6.22  ? 209  LYS A NZ   1 
ATOM   2571 H  H    . LYS A 1 209 ? 17.927 -0.934  43.360 1.000 6.34  ? 209  LYS A H    1 
ATOM   2572 H  HA   . LYS A 1 209 ? 19.551 0.635   44.938 1.000 6.16  ? 209  LYS A HA   1 
ATOM   2573 H  HB2  . LYS A 1 209 ? 18.498 2.547   44.308 1.000 6.37  ? 209  LYS A HB2  1 
ATOM   2574 H  HB3  . LYS A 1 209 ? 18.982 1.812   43.017 1.000 6.37  ? 209  LYS A HB3  1 
ATOM   2575 H  HG2  . LYS A 1 209 ? 16.843 1.170   42.509 1.000 6.25  ? 209  LYS A HG2  1 
ATOM   2576 H  HG3  . LYS A 1 209 ? 16.313 1.712   43.878 1.000 6.25  ? 209  LYS A HG3  1 
ATOM   2577 H  HD2  . LYS A 1 209 ? 17.336 3.388   41.874 1.000 6.70  ? 209  LYS A HD2  1 
ATOM   2578 H  HE2  . LYS A 1 209 ? 15.858 4.178   44.165 1.000 7.24  ? 209  LYS A HE2  1 
ATOM   2579 H  HE3  . LYS A 1 209 ? 17.415 4.354   44.055 1.000 7.24  ? 209  LYS A HE3  1 
ATOM   2580 H  HZ1  . LYS A 1 209 ? 15.585 5.642   42.480 1.000 9.33  ? 209  LYS A HZ1  1 
ATOM   2581 H  HZ2  . LYS A 1 209 ? 16.435 6.268   43.479 1.000 9.33  ? 209  LYS A HZ2  1 
ATOM   2582 N  N    . HIS A 1 210 ? 17.684 1.423   46.587 1.000 5.53  ? 210  HIS A N    1 
ATOM   2583 C  CA   . HIS A 1 210 ? 17.035 1.314   47.876 1.000 5.92  ? 210  HIS A CA   1 
ATOM   2584 C  C    . HIS A 1 210 ? 15.515 1.231   47.796 1.000 6.09  ? 210  HIS A C    1 
ATOM   2585 O  O    . HIS A 1 210 ? 14.898 0.749   48.774 1.000 8.43  ? 210  HIS A O    1 
ATOM   2586 C  CB   . HIS A 1 210 ? 17.430 2.479   48.801 1.000 6.46  ? 210  HIS A CB   1 
ATOM   2587 C  CG   . HIS A 1 210 ? 17.021 3.810   48.313 1.000 6.88  ? 210  HIS A CG   1 
ATOM   2588 N  ND1  . HIS A 1 210 ? 17.719 4.555   47.361 1.000 6.78  ? 210  HIS A ND1  1 
ATOM   2589 C  CD2  . HIS A 1 210 ? 15.898 4.537   48.672 1.000 7.81  ? 210  HIS A CD2  1 
ATOM   2590 C  CE1  . HIS A 1 210 ? 17.013 5.667   47.212 1.000 7.57  ? 210  HIS A CE1  1 
ATOM   2591 N  NE2  . HIS A 1 210 ? 15.892 5.717   47.963 1.000 7.92  ? 210  HIS A NE2  1 
ATOM   2592 H  H    . HIS A 1 210 ? 18.063 2.161   46.362 1.000 6.63  ? 210  HIS A H    1 
ATOM   2593 H  HA   . HIS A 1 210 ? 17.353 0.486   48.294 1.000 7.10  ? 210  HIS A HA   1 
ATOM   2594 H  HB2  . HIS A 1 210 ? 17.031 2.332   49.673 1.000 7.75  ? 210  HIS A HB2  1 
ATOM   2595 H  HB3  . HIS A 1 210 ? 18.393 2.472   48.915 1.000 7.75  ? 210  HIS A HB3  1 
ATOM   2596 H  HD2  . HIS A 1 210 ? 15.256 4.273   49.290 1.000 9.37  ? 210  HIS A HD2  1 
ATOM   2597 N  N    . THR A 1 211 ? 14.882 1.675   46.723 1.000 6.04  ? 211  THR A N    1 
ATOM   2598 C  CA   . THR A 1 211 ? 13.441 1.586   46.536 1.000 6.31  ? 211  THR A CA   1 
ATOM   2599 C  C    . THR A 1 211 ? 12.989 0.322   45.827 1.000 6.11  ? 211  THR A C    1 
ATOM   2600 O  O    . THR A 1 211 ? 11.796 0.095   45.693 1.000 6.79  ? 211  THR A O    1 
ATOM   2601 C  CB   . THR A 1 211 ? 12.929 2.789   45.695 1.000 7.75  ? 211  THR A CB   1 
ATOM   2602 O  OG1  . THR A 1 211 ? 13.582 2.744   44.412 1.000 7.31  ? 211  THR A OG1  1 
ATOM   2603 C  CG2  . THR A 1 211 ? 13.200 4.130   46.343 1.000 9.09  ? 211  THR A CG2  1 
ATOM   2604 H  H    . THR A 1 211 ? 15.349 2.038   46.099 1.000 7.24  ? 211  THR A H    1 
ATOM   2605 H  HA   . THR A 1 211 ? 13.011 1.618   47.416 1.000 7.58  ? 211  THR A HA   1 
ATOM   2606 H  HB   . THR A 1 211 ? 11.963 2.693   45.561 1.000 9.30  ? 211  THR A HB   1 
ATOM   2607 H  HG1  . THR A 1 211 ? 13.031 2.566   43.831 1.000 10.97 ? 211  THR A HG1  1 
ATOM   2608 H  HG21 . THR A 1 211 ? 13.002 4.106   47.270 1.000 13.64 ? 211  THR A HG21 1 
ATOM   2609 N  N    . THR A 1 212 ? 13.940 -0.487  45.315 1.000 5.45  ? 212  THR A N    1 
ATOM   2610 C  CA   . THR A 1 212 ? 13.549 -1.505  44.363 1.000 5.56  ? 212  THR A CA   1 
ATOM   2611 C  C    . THR A 1 212 ? 12.590 -2.552  44.925 1.000 5.71  ? 212  THR A C    1 
ATOM   2612 O  O    . THR A 1 212 ? 11.628 -2.922  44.259 1.000 6.54  ? 212  THR A O    1 
ATOM   2613 C  CB   . THR A 1 212 ? 14.805 -2.147  43.755 1.000 5.46  ? 212  THR A CB   1 
ATOM   2614 O  OG1  . THR A 1 212 ? 15.640 -1.129  43.200 1.000 5.23  ? 212  THR A OG1  1 
ATOM   2615 C  CG2  . THR A 1 212 ? 14.448 -3.175  42.693 1.000 6.46  ? 212  THR A CG2  1 
ATOM   2616 H  H    . THR A 1 212 ? 14.763 -0.400  45.551 1.000 6.54  ? 212  THR A H    1 
ATOM   2617 H  HA   . THR A 1 212 ? 13.080 -1.048  43.634 1.000 6.67  ? 212  THR A HA   1 
ATOM   2618 H  HB   . THR A 1 212 ? 15.300 -2.598  44.470 1.000 6.55  ? 212  THR A HB   1 
ATOM   2619 H  HG1  . THR A 1 212 ? 15.188 -0.633  42.727 1.000 6.27  ? 212  THR A HG1  1 
ATOM   2620 H  HG21 . THR A 1 212 ? 13.888 -3.852  43.079 1.000 9.69  ? 212  THR A HG21 1 
ATOM   2621 H  HG22 . THR A 1 212 ? 13.980 -2.744  41.975 1.000 9.69  ? 212  THR A HG22 1 
ATOM   2622 H  HG23 . THR A 1 212 ? 15.251 -3.578  42.355 1.000 9.69  ? 212  THR A HG23 1 
ATOM   2623 N  N    . VAL A 1 213 ? 12.875 -3.056  46.117 1.000 6.18  ? 213  VAL A N    1 
ATOM   2624 C  CA   . VAL A 1 213 ? 11.985 -4.100  46.643 1.000 7.02  ? 213  VAL A CA   1 
ATOM   2625 C  C    . VAL A 1 213 ? 10.577 -3.512  46.828 1.000 7.41  ? 213  VAL A C    1 
ATOM   2626 O  O    . VAL A 1 213 ? 9.586  -4.127  46.465 1.000 8.84  ? 213  VAL A O    1 
ATOM   2627 C  CB   . VAL A 1 213 ? 12.530 -4.725  47.922 1.000 7.39  ? 213  VAL A CB   1 
ATOM   2628 C  CG1  . VAL A 1 213 ? 11.548 -5.767  48.470 1.000 9.38  ? 213  VAL A CG1  1 
ATOM   2629 C  CG2  . VAL A 1 213 ? 13.890 -5.365  47.676 1.000 7.41  ? 213  VAL A CG2  1 
ATOM   2630 H  H    . VAL A 1 213 ? 13.556 -2.782  46.566 1.000 7.42  ? 213  VAL A H    1 
ATOM   2631 H  HA   . VAL A 1 213 ? 11.926 -4.808  45.968 1.000 8.42  ? 213  VAL A HA   1 
ATOM   2632 H  HB   . VAL A 1 213 ? 12.637 -4.018  48.592 1.000 8.87  ? 213  VAL A HB   1 
ATOM   2633 H  HG12 . VAL A 1 213 ? 11.458 -6.475  47.828 1.000 14.08 ? 213  VAL A HG12 1 
ATOM   2634 H  HG21 . VAL A 1 213 ? 14.206 -5.753  48.496 1.000 11.11 ? 213  VAL A HG21 1 
ATOM   2635 N  N    . ASN A 1 214 ? 10.483 -2.322  47.413 1.000 8.14  ? 214  ASN A N    1 
ATOM   2636 C  CA   A ASN A 1 214 ? 9.182  -1.706  47.629 0.793 10.05 ? 214  ASN A CA   1 
ATOM   2637 C  CA   B ASN A 1 214 ? 9.186  -1.687  47.619 0.207 8.93  ? 214  ASN A CA   1 
ATOM   2638 C  C    . ASN A 1 214 ? 8.459  -1.447  46.301 1.000 9.41  ? 214  ASN A C    1 
ATOM   2639 O  O    . ASN A 1 214 ? 7.213  -1.565  46.214 1.000 11.46 ? 214  ASN A O    1 
ATOM   2640 C  CB   A ASN A 1 214 ? 9.334  -0.399  48.381 0.793 13.47 ? 214  ASN A CB   1 
ATOM   2641 C  CB   B ASN A 1 214 ? 9.339  -0.368  48.381 0.207 12.62 ? 214  ASN A CB   1 
ATOM   2642 C  CG   A ASN A 1 214 ? 8.001  -0.034  49.005 0.793 16.89 ? 214  ASN A CG   1 
ATOM   2643 C  CG   B ASN A 1 214 ? 9.012  -0.569  49.849 0.207 16.91 ? 214  ASN A CG   1 
ATOM   2644 O  OD1  A ASN A 1 214 ? 7.474  -0.833  49.795 0.793 26.72 ? 214  ASN A OD1  1 
ATOM   2645 O  OD1  B ASN A 1 214 ? 9.870  -0.901  50.654 0.207 20.66 ? 214  ASN A OD1  1 
ATOM   2646 N  ND2  A ASN A 1 214 ? 7.526  1.148   48.663 0.793 26.27 ? 214  ASN A ND2  1 
ATOM   2647 N  ND2  B ASN A 1 214 ? 7.743  -0.387  50.197 0.207 26.20 ? 214  ASN A ND2  1 
ATOM   2648 H  H    A ASN A 1 214 ? 11.196 -1.913  47.666 1.000 9.77  ? 214  ASN A H    1 
ATOM   2649 N  N    . GLU A 1 215 ? 9.166  -1.080  45.231 1.000 8.32  ? 215  GLU A N    1 
ATOM   2650 C  CA   . GLU A 1 215 ? 8.564  -0.851  43.937 1.000 9.27  ? 215  GLU A CA   1 
ATOM   2651 C  C    . GLU A 1 215 ? 7.944  -2.110  43.337 1.000 9.31  ? 215  GLU A C    1 
ATOM   2652 O  O    . GLU A 1 215 ? 7.038  -2.003  42.510 1.000 14.10 ? 215  GLU A O    1 
ATOM   2653 C  CB   . GLU A 1 215 ? 9.604  -0.312  42.928 1.000 8.37  ? 215  GLU A CB   1 
ATOM   2654 C  CG   . GLU A 1 215 ? 10.014 1.128   43.125 1.000 8.10  ? 215  GLU A CG   1 
ATOM   2655 C  CD   . GLU A 1 215 ? 10.925 1.596   41.975 1.000 7.11  ? 215  GLU A CD   1 
ATOM   2656 O  OE1  . GLU A 1 215 ? 10.601 1.324   40.800 1.000 7.61  ? 215  GLU A OE1  1 
ATOM   2657 O  OE2  . GLU A 1 215 ? 11.979 2.219   42.290 1.000 7.86  ? 215  GLU A OE2  1 
ATOM   2658 H  HB3  . GLU A 1 215 ? 9.223  -0.377  42.057 1.000 10.04 ? 215  GLU A HB3  1 
ATOM   2659 H  HG3  . GLU A 1 215 ? 10.438 1.261   43.972 1.000 9.72  ? 215  GLU A HG3  1 
ATOM   2660 N  N    . ASN A 1 216 ? 8.515  -3.254  43.666 1.000 8.64  ? 216  ASN A N    1 
ATOM   2661 C  CA   . ASN A 1 216 ? 8.159  -4.487  42.966 1.000 8.76  ? 216  ASN A CA   1 
ATOM   2662 C  C    . ASN A 1 216 ? 7.383  -5.491  43.795 1.000 9.72  ? 216  ASN A C    1 
ATOM   2663 O  O    . ASN A 1 216 ? 6.633  -6.283  43.193 1.000 11.77 ? 216  ASN A O    1 
ATOM   2664 C  CB   . ASN A 1 216 ? 9.459  -5.186  42.463 1.000 9.06  ? 216  ASN A CB   1 
ATOM   2665 C  CG   . ASN A 1 216 ? 9.977  -4.422  41.283 1.000 7.82  ? 216  ASN A CG   1 
ATOM   2666 O  OD1  . ASN A 1 216 ? 9.501  -4.605  40.162 1.000 10.56 ? 216  ASN A OD1  1 
ATOM   2667 N  ND2  . ASN A 1 216 ? 10.928 -3.517  41.493 1.000 7.57  ? 216  ASN A ND2  1 
ATOM   2668 H  H    . ASN A 1 216 ? 9.101  -3.274  44.296 1.000 10.36 ? 216  ASN A H    1 
ATOM   2669 H  HA   . ASN A 1 216 ? 7.617  -4.250  42.185 1.000 10.52 ? 216  ASN A HA   1 
ATOM   2670 H  HB2  . ASN A 1 216 ? 10.110 -5.214  43.156 1.000 10.87 ? 216  ASN A HB2  1 
ATOM   2671 H  HD21 . ASN A 1 216 ? 11.223 -3.043  40.839 1.000 9.08  ? 216  ASN A HD21 1 
ATOM   2672 H  HD22 . ASN A 1 216 ? 11.247 -3.405  42.284 1.000 9.08  ? 216  ASN A HD22 1 
ATOM   2673 N  N    . ALA A 1 217 ? 7.557  -5.491  45.086 1.000 10.73 ? 217  ALA A N    1 
ATOM   2674 C  CA   . ALA A 1 217 ? 6.976  -6.446  46.009 1.000 11.75 ? 217  ALA A CA   1 
ATOM   2675 C  C    . ALA A 1 217 ? 6.632  -5.808  47.328 1.000 12.52 ? 217  ALA A C    1 
ATOM   2676 O  O    . ALA A 1 217 ? 7.061  -6.261  48.393 1.000 13.87 ? 217  ALA A O    1 
ATOM   2677 C  CB   . ALA A 1 217 ? 7.944  -7.593  46.153 1.000 13.42 ? 217  ALA A CB   1 
ATOM   2678 H  H    . ALA A 1 217 ? 8.056  -4.875  45.418 1.000 12.88 ? 217  ALA A H    1 
ATOM   2679 H  HA   . ALA A 1 217 ? 6.150  -6.792  45.611 1.000 14.10 ? 217  ALA A HA   1 
ATOM   2680 N  N    . PRO A 1 218 ? 5.840  -4.759  47.312 1.000 13.00 ? 218  PRO A N    1 
ATOM   2681 C  CA   . PRO A 1 218 ? 5.574  -4.039  48.561 1.000 15.14 ? 218  PRO A CA   1 
ATOM   2682 C  C    . PRO A 1 218 ? 4.969  -4.912  49.647 1.000 16.99 ? 218  PRO A C    1 
ATOM   2683 O  O    . PRO A 1 218 ? 5.252  -4.713  50.814 1.000 21.90 ? 218  PRO A O    1 
ATOM   2684 C  CB   . PRO A 1 218 ? 4.605  -2.918  48.125 1.000 17.05 ? 218  PRO A CB   1 
ATOM   2685 C  CG   . PRO A 1 218 ? 3.981  -3.423  46.860 1.000 16.01 ? 218  PRO A CG   1 
ATOM   2686 C  CD   . PRO A 1 218 ? 5.120  -4.153  46.175 1.000 13.68 ? 218  PRO A CD   1 
ATOM   2687 N  N    . ASP A 1 219 ? 4.197  -5.899  49.317 1.000 15.98 ? 219  ASP A N    1 
ATOM   2688 C  CA   . ASP A 1 219 ? 3.561  -6.761  50.341 1.000 19.80 ? 219  ASP A CA   1 
ATOM   2689 C  C    . ASP A 1 219 ? 4.349  -8.027  50.631 1.000 17.89 ? 219  ASP A C    1 
ATOM   2690 O  O    . ASP A 1 219 ? 3.970  -8.829  51.494 1.000 22.74 ? 219  ASP A O    1 
ATOM   2691 C  CB   . ASP A 1 219 ? 2.148  -7.062  49.865 1.000 22.77 ? 219  ASP A CB   1 
ATOM   2692 C  CG   . ASP A 1 219 ? 1.285  -5.804  49.843 1.000 25.47 ? 219  ASP A CG   1 
ATOM   2693 O  OD1  . ASP A 1 219 ? 0.531  -5.681  48.848 1.000 40.45 ? 219  ASP A OD1  1 
ATOM   2694 O  OD2  . ASP A 1 219 ? 1.402  -5.016  50.811 1.000 32.33 ? 219  ASP A OD2  1 
ATOM   2695 H  H    . ASP A 1 219 ? 4.050  -6.058  48.484 1.000 19.17 ? 219  ASP A H    1 
ATOM   2696 N  N    . GLN A 1 220 ? 5.484  -8.258  49.961 1.000 15.65 ? 220  GLN A N    1 
ATOM   2697 C  CA   . GLN A 1 220 ? 6.402  -9.343  50.253 1.000 15.35 ? 220  GLN A CA   1 
ATOM   2698 C  C    . GLN A 1 220 ? 7.803  -8.858  50.620 1.000 12.37 ? 220  GLN A C    1 
ATOM   2699 O  O    . GLN A 1 220 ? 8.741  -9.629  50.608 1.000 13.43 ? 220  GLN A O    1 
ATOM   2700 C  CB   . GLN A 1 220 ? 6.545  -10.370 49.133 1.000 17.34 ? 220  GLN A CB   1 
ATOM   2701 C  CG   . GLN A 1 220 ? 5.196  -11.096 48.839 1.000 21.76 ? 220  GLN A CG   1 
ATOM   2702 C  CD   . GLN A 1 220 ? 4.244  -10.322 47.943 1.000 25.42 ? 220  GLN A CD   1 
ATOM   2703 O  OE1  . GLN A 1 220 ? 4.636  -9.633  46.976 1.000 25.94 ? 220  GLN A OE1  1 
ATOM   2704 N  NE2  . GLN A 1 220 ? 2.933  -10.374 48.234 1.000 29.18 ? 220  GLN A NE2  1 
ATOM   2705 H  HB2  . GLN A 1 220 ? 6.830  -9.929  48.334 1.000 20.80 ? 220  GLN A HB2  1 
ATOM   2706 N  N    A LYS A 1 221 ? 7.890  -7.569  50.950 0.480 12.93 ? 221  LYS A N    1 
ATOM   2707 N  N    B LYS A 1 221 ? 7.899  -7.583  50.942 0.520 12.31 ? 221  LYS A N    1 
ATOM   2708 C  CA   A LYS A 1 221 ? 9.212  -7.026  51.202 0.480 13.13 ? 221  LYS A CA   1 
ATOM   2709 C  CA   B LYS A 1 221 ? 9.137  -6.890  51.080 0.520 11.97 ? 221  LYS A CA   1 
ATOM   2710 C  C    A LYS A 1 221 ? 9.888  -7.771  52.349 0.480 14.03 ? 221  LYS A C    1 
ATOM   2711 C  C    B LYS A 1 221 ? 10.108 -7.607  52.007 0.520 10.92 ? 221  LYS A C    1 
ATOM   2712 O  O    A LYS A 1 221 ? 11.120 -7.854  52.349 0.480 14.93 ? 221  LYS A O    1 
ATOM   2713 O  O    B LYS A 1 221 ? 11.280 -7.827  51.782 0.520 12.68 ? 221  LYS A O    1 
ATOM   2714 C  CB   A LYS A 1 221 ? 9.144  -5.527  51.418 0.480 15.07 ? 221  LYS A CB   1 
ATOM   2715 C  CB   B LYS A 1 221 ? 8.897  -5.473  51.638 0.520 13.57 ? 221  LYS A CB   1 
ATOM   2716 C  CG   A LYS A 1 221 ? 8.561  -4.972  52.694 0.480 17.75 ? 221  LYS A CG   1 
ATOM   2717 C  CG   B LYS A 1 221 ? 10.194 -4.747  51.918 0.520 15.39 ? 221  LYS A CG   1 
ATOM   2718 C  CD   A LYS A 1 221 ? 9.300  -3.643  53.003 0.480 20.05 ? 221  LYS A CD   1 
ATOM   2719 C  CD   B LYS A 1 221 ? 10.048 -3.442  52.665 0.520 18.99 ? 221  LYS A CD   1 
ATOM   2720 C  CE   A LYS A 1 221 ? 8.612  -2.493  52.299 0.480 21.65 ? 221  LYS A CE   1 
ATOM   2721 C  CE   B LYS A 1 221 ? 9.443  -2.331  51.838 0.520 19.89 ? 221  LYS A CE   1 
ATOM   2722 N  NZ   A LYS A 1 221 ? 9.192  -1.189  52.754 0.480 15.32 ? 221  LYS A NZ   1 
ATOM   2723 N  NZ   B LYS A 1 221 ? 8.899  -1.272  52.751 0.520 25.63 ? 221  LYS A NZ   1 
ATOM   2724 N  N    A ASP A 1 222 ? 9.119  -8.366  53.265 0.480 13.71 ? 222  ASP A N    1 
ATOM   2725 N  N    B ASP A 1 222 ? 9.622  -7.962  53.180 0.520 11.62 ? 222  ASP A N    1 
ATOM   2726 C  CA   A ASP A 1 222 ? 9.743  -9.010  54.412 0.480 13.13 ? 222  ASP A CA   1 
ATOM   2727 C  CA   B ASP A 1 222 ? 10.482 -8.515  54.225 0.520 10.33 ? 222  ASP A CA   1 
ATOM   2728 C  C    A ASP A 1 222 ? 10.401 -10.324 54.118 0.480 11.34 ? 222  ASP A C    1 
ATOM   2729 C  C    B ASP A 1 222 ? 10.606 -10.030 54.033 0.520 12.87 ? 222  ASP A C    1 
ATOM   2730 O  O    A ASP A 1 222 ? 11.056 -11.043 54.851 0.480 14.61 ? 222  ASP A O    1 
ATOM   2731 O  O    B ASP A 1 222 ? 11.134 -10.665 54.988 0.520 12.63 ? 222  ASP A O    1 
ATOM   2732 C  CB   A ASP A 1 222 ? 8.709  -9.181  55.540 0.480 16.84 ? 222  ASP A CB   1 
ATOM   2733 C  CB   B ASP A 1 222 ? 10.007 -8.019  55.571 0.520 8.46  ? 222  ASP A CB   1 
ATOM   2734 C  CG   A ASP A 1 222 ? 8.321  -7.783  55.959 0.480 19.48 ? 222  ASP A CG   1 
ATOM   2735 C  CG   B ASP A 1 222 ? 10.324 -6.523  55.740 0.520 8.33  ? 222  ASP A CG   1 
ATOM   2736 O  OD1  A ASP A 1 222 ? 9.034  -6.818  56.155 0.480 26.14 ? 222  ASP A OD1  1 
ATOM   2737 O  OD1  B ASP A 1 222 ? 11.226 -5.963  55.071 0.520 8.60  ? 222  ASP A OD1  1 
ATOM   2738 O  OD2  A ASP A 1 222 ? 7.101  -7.739  56.289 0.480 26.02 ? 222  ASP A OD2  1 
ATOM   2739 O  OD2  B ASP A 1 222 ? 9.603  -5.889  56.599 0.520 9.62  ? 222  ASP A OD2  1 
ATOM   2740 N  N    . GLU A 1 223 ? 10.257 -10.679 52.886 1.000 11.43 ? 223  GLU A N    1 
ATOM   2741 C  CA   A GLU A 1 223 ? 10.815 -11.918 52.396 0.687 12.45 ? 223  GLU A CA   1 
ATOM   2742 C  CA   B GLU A 1 223 ? 10.874 -11.912 52.500 0.313 12.43 ? 223  GLU A CA   1 
ATOM   2743 C  C    . GLU A 1 223 ? 12.235 -11.720 51.791 1.000 11.76 ? 223  GLU A C    1 
ATOM   2744 O  O    . GLU A 1 223 ? 12.882 -12.667 51.375 1.000 17.08 ? 223  GLU A O    1 
ATOM   2745 C  CB   A GLU A 1 223 ? 9.962  -12.625 51.348 0.687 14.60 ? 223  GLU A CB   1 
ATOM   2746 C  CB   B GLU A 1 223 ? 9.962  -12.687 51.551 0.313 11.50 ? 223  GLU A CB   1 
ATOM   2747 C  CG   A GLU A 1 223 ? 8.669  -13.129 51.976 0.687 19.49 ? 223  GLU A CG   1 
ATOM   2748 C  CG   B GLU A 1 223 ? 8.533  -12.664 52.075 0.313 12.29 ? 223  GLU A CG   1 
ATOM   2749 C  CD   A GLU A 1 223 ? 7.935  -14.208 51.226 0.687 23.69 ? 223  GLU A CD   1 
ATOM   2750 C  CD   B GLU A 1 223 ? 8.434  -13.202 53.475 0.313 17.91 ? 223  GLU A CD   1 
ATOM   2751 O  OE1  A GLU A 1 223 ? 6.680  -14.140 51.328 0.687 34.41 ? 223  GLU A OE1  1 
ATOM   2752 O  OE1  B GLU A 1 223 ? 7.313  -13.057 53.996 0.313 31.21 ? 223  GLU A OE1  1 
ATOM   2753 O  OE2  A GLU A 1 223 ? 8.521  -15.116 50.562 0.687 42.07 ? 223  GLU A OE2  1 
ATOM   2754 O  OE2  B GLU A 1 223 ? 9.347  -13.759 54.067 0.313 11.85 ? 223  GLU A OE2  1 
ATOM   2755 H  H    A GLU A 1 223 ? 9.821  -10.169 52.348 1.000 13.71 ? 223  GLU A H    1 
ATOM   2756 H  HA   A GLU A 1 223 ? 10.904 -12.524 53.161 0.687 14.94 ? 223  GLU A HA   1 
ATOM   2757 N  N    . TYR A 1 224 ? 12.673 -10.510 51.680 1.000 8.62  ? 224  TYR A N    1 
ATOM   2758 C  CA   . TYR A 1 224 ? 13.970 -10.093 51.171 1.000 8.09  ? 224  TYR A CA   1 
ATOM   2759 C  C    . TYR A 1 224 ? 14.731 -9.413  52.288 1.000 7.30  ? 224  TYR A C    1 
ATOM   2760 O  O    . TYR A 1 224 ? 14.187 -9.051  53.315 1.000 8.67  ? 224  TYR A O    1 
ATOM   2761 C  CB   . TYR A 1 224 ? 13.815 -9.166  49.950 1.000 8.56  ? 224  TYR A CB   1 
ATOM   2762 C  CG   . TYR A 1 224 ? 13.055 -9.867  48.842 1.000 8.23  ? 224  TYR A CG   1 
ATOM   2763 C  CD1  . TYR A 1 224 ? 11.690 -9.844  48.799 1.000 9.28  ? 224  TYR A CD1  1 
ATOM   2764 C  CD2  . TYR A 1 224 ? 13.729 -10.616 47.889 1.000 8.44  ? 224  TYR A CD2  1 
ATOM   2765 C  CE1  . TYR A 1 224 ? 10.959 -10.507 47.807 1.000 9.80  ? 224  TYR A CE1  1 
ATOM   2766 C  CE2  . TYR A 1 224 ? 13.001 -11.296 46.902 1.000 9.21  ? 224  TYR A CE2  1 
ATOM   2767 C  CZ   . TYR A 1 224 ? 11.649 -11.240 46.868 1.000 9.82  ? 224  TYR A CZ   1 
ATOM   2768 O  OH   . TYR A 1 224 ? 10.951 -11.937 45.895 1.000 11.70 ? 224  TYR A OH   1 
ATOM   2769 H  HA   . TYR A 1 224 ? 14.468 -10.891 50.896 1.000 9.70  ? 224  TYR A HA   1 
ATOM   2770 H  HB2  . TYR A 1 224 ? 13.340 -8.362  50.211 1.000 10.27 ? 224  TYR A HB2  1 
ATOM   2771 H  HB3  . TYR A 1 224 ? 14.692 -8.906  49.626 1.000 10.27 ? 224  TYR A HB3  1 
ATOM   2772 H  HD1  . TYR A 1 224 ? 11.229 -9.371  49.454 1.000 11.14 ? 224  TYR A HD1  1 
ATOM   2773 H  HD2  . TYR A 1 224 ? 14.657 -10.666 47.904 1.000 10.12 ? 224  TYR A HD2  1 
ATOM   2774 H  HH   . TYR A 1 224 ? 10.156 -11.740 45.934 1.000 17.55 ? 224  TYR A HH   1 
ATOM   2775 N  N    . GLU A 1 225 ? 16.038 -9.265  52.063 1.000 7.17  ? 225  GLU A N    1 
ATOM   2776 C  CA   . GLU A 1 225 ? 16.940 -8.536  52.974 1.000 6.94  ? 225  GLU A CA   1 
ATOM   2777 C  C    . GLU A 1 225 ? 18.148 -8.090  52.158 1.000 6.67  ? 225  GLU A C    1 
ATOM   2778 O  O    . GLU A 1 225 ? 18.218 -8.321  50.958 1.000 6.96  ? 225  GLU A O    1 
ATOM   2779 C  CB   . GLU A 1 225 ? 17.244 -9.336  54.258 1.000 7.36  ? 225  GLU A CB   1 
ATOM   2780 C  CG   . GLU A 1 225 ? 17.936 -10.654 53.960 1.000 7.83  ? 225  GLU A CG   1 
ATOM   2781 C  CD   . GLU A 1 225 ? 17.972 -11.596 55.165 1.000 7.70  ? 225  GLU A CD   1 
ATOM   2782 O  OE1  . GLU A 1 225 ? 17.630 -11.180 56.281 1.000 9.04  ? 225  GLU A OE1  1 
ATOM   2783 O  OE2  . GLU A 1 225 ? 18.352 -12.782 54.960 1.000 9.13  ? 225  GLU A OE2  1 
ATOM   2784 H  HA   . GLU A 1 225 ? 16.468 -7.723  53.251 1.000 8.32  ? 225  GLU A HA   1 
ATOM   2785 H  HB2  . GLU A 1 225 ? 17.803 -8.801  54.803 1.000 8.83  ? 225  GLU A HB2  1 
ATOM   2786 H  HG2  . GLU A 1 225 ? 17.469 -11.123 53.288 1.000 9.39  ? 225  GLU A HG2  1 
ATOM   2787 N  N    . LEU A 1 226 ? 19.091 -7.435  52.843 1.000 6.67  ? 226  LEU A N    1 
ATOM   2788 C  CA   . LEU A 1 226 ? 20.209 -6.766  52.211 1.000 6.82  ? 226  LEU A CA   1 
ATOM   2789 C  C    . LEU A 1 226 ? 21.513 -7.382  52.730 1.000 6.96  ? 226  LEU A C    1 
ATOM   2790 O  O    . LEU A 1 226 ? 21.641 -7.682  53.908 1.000 7.84  ? 226  LEU A O    1 
ATOM   2791 C  CB   . LEU A 1 226 ? 20.222 -5.288  52.505 1.000 6.51  ? 226  LEU A CB   1 
ATOM   2792 C  CG   . LEU A 1 226 ? 18.961 -4.503  52.165 1.000 6.71  ? 226  LEU A CG   1 
ATOM   2793 C  CD1  . LEU A 1 226 ? 19.168 -3.030  52.521 1.000 7.45  ? 226  LEU A CD1  1 
ATOM   2794 C  CD2  . LEU A 1 226 ? 18.537 -4.682  50.720 1.000 6.87  ? 226  LEU A CD2  1 
ATOM   2795 H  H    . LEU A 1 226 ? 19.031 -7.409  53.700 1.000 8.00  ? 226  LEU A H    1 
ATOM   2796 H  HA   . LEU A 1 226 ? 20.155 -6.899  51.241 1.000 8.18  ? 226  LEU A HA   1 
ATOM   2797 H  HB2  . LEU A 1 226 ? 20.402 -5.172  53.451 1.000 7.81  ? 226  LEU A HB2  1 
ATOM   2798 H  HB3  . LEU A 1 226 ? 20.962 -4.892  52.020 1.000 7.81  ? 226  LEU A HB3  1 
ATOM   2799 H  HG   . LEU A 1 226 ? 18.237 -4.845  52.730 1.000 8.05  ? 226  LEU A HG   1 
ATOM   2800 H  HD12 . LEU A 1 226 ? 19.979 -2.715  52.115 1.000 11.17 ? 226  LEU A HD12 1 
ATOM   2801 H  HD22 . LEU A 1 226 ? 17.712 -4.216  50.566 1.000 10.30 ? 226  LEU A HD22 1 
ATOM   2802 H  HD23 . LEU A 1 226 ? 19.218 -4.325  50.145 1.000 10.30 ? 226  LEU A HD23 1 
ATOM   2803 N  N    . LEU A 1 227 ? 22.511 -7.464  51.823 1.000 6.88  ? 227  LEU A N    1 
ATOM   2804 C  CA   . LEU A 1 227 ? 23.870 -7.808  52.171 1.000 7.81  ? 227  LEU A CA   1 
ATOM   2805 C  C    . LEU A 1 227 ? 24.640 -6.531  52.509 1.000 7.92  ? 227  LEU A C    1 
ATOM   2806 O  O    . LEU A 1 227 ? 24.778 -5.657  51.665 1.000 8.75  ? 227  LEU A O    1 
ATOM   2807 C  CB   A LEU A 1 227 ? 24.750 -8.439  51.113 0.818 9.20  ? 227  LEU A CB   1 
ATOM   2808 C  CB   B LEU A 1 227 ? 24.411 -8.550  50.951 0.182 8.62  ? 227  LEU A CB   1 
ATOM   2809 C  CG   A LEU A 1 227 ? 24.170 -9.741  50.556 0.818 9.42  ? 227  LEU A CG   1 
ATOM   2810 C  CG   B LEU A 1 227 ? 25.219 -9.821  51.068 0.182 6.01  ? 227  LEU A CG   1 
ATOM   2811 C  CD1  A LEU A 1 227 ? 25.087 -10.215 49.420 0.818 8.96  ? 227  LEU A CD1  1 
ATOM   2812 C  CD1  B LEU A 1 227 ? 24.436 -10.913 51.800 0.182 9.55  ? 227  LEU A CD1  1 
ATOM   2813 C  CD2  A LEU A 1 227 ? 24.037 -10.836 51.585 0.818 10.66 ? 227  LEU A CD2  1 
ATOM   2814 C  CD2  B LEU A 1 227 ? 25.698 -10.384 49.733 0.182 6.19  ? 227  LEU A CD2  1 
ATOM   2815 H  H    . LEU A 1 227 ? 22.329 -7.304  50.998 1.000 8.26  ? 227  LEU A H    1 
ATOM   2816 H  HD11 A LEU A 1 227 ? 24.589 -10.521 48.672 0.818 13.44 ? 227  LEU A HD11 1 
ATOM   2817 H  HD21 A LEU A 1 227 ? 23.670 -11.638 51.261 0.818 15.99 ? 227  LEU A HD21 1 
ATOM   2818 H  HD22 A LEU A 1 227 ? 24.916 -10.970 51.889 0.818 15.99 ? 227  LEU A HD22 1 
ATOM   2819 N  N    . CYS A 1 228 ? 25.183 -6.440  53.729 1.000 8.41  ? 228  CYS A N    1 
ATOM   2820 C  CA   . CYS A 1 228 ? 25.941 -5.249  54.146 1.000 8.91  ? 228  CYS A CA   1 
ATOM   2821 C  C    . CYS A 1 228 ? 27.419 -5.511  53.941 1.000 9.70  ? 228  CYS A C    1 
ATOM   2822 O  O    . CYS A 1 228 ? 27.921 -6.641  54.056 1.000 10.41 ? 228  CYS A O    1 
ATOM   2823 C  CB   . CYS A 1 228 ? 25.665 -4.915  55.589 1.000 9.61  ? 228  CYS A CB   1 
ATOM   2824 S  SG   . CYS A 1 228 ? 23.899 -5.050  56.062 1.000 9.10  ? 228  CYS A SG   1 
ATOM   2825 H  HA   . CYS A 1 228 ? 25.672 -4.490  53.588 1.000 10.69 ? 228  CYS A HA   1 
ATOM   2826 N  N    . LEU A 1 229 ? 28.163 -4.412  53.716 1.000 10.30 ? 229  LEU A N    1 
ATOM   2827 C  CA   . LEU A 1 229 ? 29.613 -4.548  53.497 1.000 11.58 ? 229  LEU A CA   1 
ATOM   2828 C  C    . LEU A 1 229 ? 30.335 -5.087  54.727 1.000 12.69 ? 229  LEU A C    1 
ATOM   2829 O  O    . LEU A 1 229 ? 31.436 -5.637  54.566 1.000 14.79 ? 229  LEU A O    1 
ATOM   2830 C  CB   . LEU A 1 229 ? 30.180 -3.198  53.078 1.000 13.56 ? 229  LEU A CB   1 
ATOM   2831 C  CG   . LEU A 1 229 ? 29.738 -2.702  51.709 1.000 18.58 ? 229  LEU A CG   1 
ATOM   2832 C  CD1  . LEU A 1 229 ? 30.287 -1.297  51.467 1.000 25.53 ? 229  LEU A CD1  1 
ATOM   2833 C  CD2  . LEU A 1 229 ? 30.158 -3.685  50.648 1.000 23.24 ? 229  LEU A CD2  1 
ATOM   2834 H  HA   . LEU A 1 229 ? 29.752 -5.179  52.760 1.000 13.90 ? 229  LEU A HA   1 
ATOM   2835 H  HB3  . LEU A 1 229 ? 31.134 -3.307  53.020 1.000 16.28 ? 229  LEU A HB3  1 
ATOM   2836 N  N    . ASP A 1 230 ? 29.783 -4.934  55.913 1.000 12.29 ? 230  ASP A N    1 
ATOM   2837 C  CA   . ASP A 1 230 ? 30.489 -5.360  57.109 1.000 13.21 ? 230  ASP A CA   1 
ATOM   2838 C  C    . ASP A 1 230 ? 30.264 -6.826  57.374 1.000 13.27 ? 230  ASP A C    1 
ATOM   2839 O  O    . ASP A 1 230 ? 30.703 -7.270  58.431 1.000 16.25 ? 230  ASP A O    1 
ATOM   2840 C  CB   . ASP A 1 230 ? 30.043 -4.552  58.324 1.000 17.13 ? 230  ASP A CB   1 
ATOM   2841 C  CG   . ASP A 1 230 ? 28.674 -4.873  58.857 1.000 16.74 ? 230  ASP A CG   1 
ATOM   2842 O  OD1  . ASP A 1 230 ? 27.867 -5.530  58.148 1.000 14.92 ? 230  ASP A OD1  1 
ATOM   2843 O  OD2  . ASP A 1 230 ? 28.399 -4.430  59.999 1.000 27.33 ? 230  ASP A OD2  1 
ATOM   2844 H  HB2  . ASP A 1 230 ? 30.689 -4.695  59.033 1.000 20.56 ? 230  ASP A HB2  1 
ATOM   2845 N  N    . GLY A 1 231 ? 29.533 -7.566  56.485 1.000 11.47 ? 231  GLY A N    1 
ATOM   2846 C  CA   . GLY A 1 231 ? 29.322 -8.986  56.631 1.000 12.24 ? 231  GLY A CA   1 
ATOM   2847 C  C    . GLY A 1 231 ? 27.970 -9.350  57.191 1.000 11.53 ? 231  GLY A C    1 
ATOM   2848 O  O    . GLY A 1 231 ? 27.593 -10.530 57.242 1.000 14.84 ? 231  GLY A O    1 
ATOM   2849 N  N    . SER A 1 232 ? 27.220 -8.374  57.648 1.000 11.43 ? 232  SER A N    1 
ATOM   2850 C  CA   . SER A 1 232 ? 25.898 -8.584  58.209 1.000 11.50 ? 232  SER A CA   1 
ATOM   2851 C  C    . SER A 1 232 ? 24.846 -8.677  57.079 1.000 8.82  ? 232  SER A C    1 
ATOM   2852 O  O    . SER A 1 232 ? 25.098 -8.356  55.939 1.000 9.15  ? 232  SER A O    1 
ATOM   2853 C  CB   . SER A 1 232 ? 25.519 -7.460  59.211 1.000 12.12 ? 232  SER A CB   1 
ATOM   2854 O  OG   . SER A 1 232 ? 25.367 -6.194  58.626 1.000 13.17 ? 232  SER A OG   1 
ATOM   2855 H  HA   . SER A 1 232 ? 25.904 -9.436  58.693 1.000 13.80 ? 232  SER A HA   1 
ATOM   2856 H  HB2  . SER A 1 232 ? 24.688 -7.702  59.649 1.000 14.54 ? 232  SER A HB2  1 
ATOM   2857 H  HB3  . SER A 1 232 ? 26.206 -7.407  59.894 1.000 14.54 ? 232  SER A HB3  1 
ATOM   2858 N  N    . ARG A 1 233 ? 23.638 -9.113  57.465 1.000 8.68  ? 233  ARG A N    1 
ATOM   2859 C  CA   . ARG A 1 233 ? 22.399 -8.902  56.698 1.000 8.03  ? 233  ARG A CA   1 
ATOM   2860 C  C    . ARG A 1 233 ? 21.487 -7.995  57.491 1.000 7.90  ? 233  ARG A C    1 
ATOM   2861 O  O    . ARG A 1 233 ? 21.443 -8.075  58.725 1.000 7.62  ? 233  ARG A O    1 
ATOM   2862 C  CB   . ARG A 1 233 ? 21.660 -10.169 56.337 1.000 8.90  ? 233  ARG A CB   1 
ATOM   2863 C  CG   . ARG A 1 233 ? 22.365 -11.036 55.266 1.000 8.87  ? 233  ARG A CG   1 
ATOM   2864 C  CD   . ARG A 1 233 ? 21.572 -12.254 54.947 1.000 9.73  ? 233  ARG A CD   1 
ATOM   2865 N  NE   . ARG A 1 233 ? 22.135 -13.010 53.870 1.000 9.88  ? 233  ARG A NE   1 
ATOM   2866 C  CZ   . ARG A 1 233 ? 21.440 -13.683 52.958 1.000 9.35  ? 233  ARG A CZ   1 
ATOM   2867 N  NH1  . ARG A 1 233 ? 20.120 -13.759 52.982 1.000 9.70  ? 233  ARG A NH1  1 
ATOM   2868 N  NH2  . ARG A 1 233 ? 22.032 -14.317 51.952 1.000 11.20 ? 233  ARG A NH2  1 
ATOM   2869 H  HA   . ARG A 1 233 ? 22.634 -8.442  55.865 1.000 9.63  ? 233  ARG A HA   1 
ATOM   2870 H  HB2  . ARG A 1 233 ? 21.545 -10.700 57.141 1.000 10.68 ? 233  ARG A HB2  1 
ATOM   2871 H  HB3  . ARG A 1 233 ? 20.777 -9.932  56.013 1.000 10.68 ? 233  ARG A HB3  1 
ATOM   2872 H  HG2  . ARG A 1 233 ? 22.489 -10.512 54.459 1.000 10.65 ? 233  ARG A HG2  1 
ATOM   2873 H  HG3  . ARG A 1 233 ? 23.241 -11.298 55.591 1.000 10.65 ? 233  ARG A HG3  1 
ATOM   2874 H  HH11 . ARG A 1 233 ? 19.717 -13.360 53.580 1.000 11.63 ? 233  ARG A HH11 1 
ATOM   2875 H  HH21 . ARG A 1 233 ? 21.589 -14.753 51.420 1.000 13.44 ? 233  ARG A HH21 1 
ATOM   2876 N  N    . GLN A 1 234 ? 20.782 -7.121  56.801 1.000 7.56  ? 234  GLN A N    1 
ATOM   2877 C  CA   . GLN A 1 234 ? 19.847 -6.218  57.404 1.000 7.01  ? 234  GLN A CA   1 
ATOM   2878 C  C    . GLN A 1 234 ? 18.582 -6.135  56.603 1.000 6.83  ? 234  GLN A C    1 
ATOM   2879 O  O    . GLN A 1 234 ? 18.556 -6.425  55.403 1.000 6.79  ? 234  GLN A O    1 
ATOM   2880 C  CB   A GLN A 1 234 ? 20.434 -4.790  57.651 0.817 7.10  ? 234  GLN A CB   1 
ATOM   2881 C  CB   B GLN A 1 234 ? 20.551 -4.827  57.379 0.183 9.47  ? 234  GLN A CB   1 
ATOM   2882 C  CG   A GLN A 1 234 ? 21.477 -4.746  58.742 0.817 8.39  ? 234  GLN A CG   1 
ATOM   2883 C  CG   B GLN A 1 234 ? 21.512 -4.884  58.584 0.183 10.14 ? 234  GLN A CG   1 
ATOM   2884 C  CD   A GLN A 1 234 ? 22.000 -3.340  58.990 0.817 8.86  ? 234  GLN A CD   1 
ATOM   2885 C  CD   B GLN A 1 234 ? 20.564 -5.014  59.750 0.183 13.53 ? 234  GLN A CD   1 
ATOM   2886 O  OE1  A GLN A 1 234 ? 21.251 -2.369  58.993 0.817 9.74  ? 234  GLN A OE1  1 
ATOM   2887 O  OE1  B GLN A 1 234 ? 20.030 -4.012  60.252 0.183 17.93 ? 234  GLN A OE1  1 
ATOM   2888 N  NE2  A GLN A 1 234 ? 23.325 -3.265  59.168 0.817 12.96 ? 234  GLN A NE2  1 
ATOM   2889 N  NE2  B GLN A 1 234 ? 20.273 -6.177  60.333 0.183 27.69 ? 234  GLN A NE2  1 
ATOM   2890 H  H    . GLN A 1 234 ? 20.888 -7.092  55.948 1.000 9.07  ? 234  GLN A H    1 
ATOM   2891 H  HA   A GLN A 1 234 ? 19.611 -6.589  58.280 1.000 8.41  ? 234  GLN A HA   1 
ATOM   2892 H  HB2  A GLN A 1 234 ? 20.883 -4.538  56.840 0.817 8.52  ? 234  GLN A HB2  1 
ATOM   2893 H  HB2  B GLN A 1 234 ? 21.001 -4.577  56.567 0.183 11.36 ? 234  GLN A HB2  1 
ATOM   2894 N  N    . PRO A 1 235 ? 17.479 -5.659  57.221 1.000 6.92  ? 235  PRO A N    1 
ATOM   2895 C  CA   . PRO A 1 235 ? 16.225 -5.516  56.506 1.000 7.72  ? 235  PRO A CA   1 
ATOM   2896 C  C    . PRO A 1 235 ? 16.331 -4.564  55.326 1.000 6.71  ? 235  PRO A C    1 
ATOM   2897 O  O    . PRO A 1 235 ? 17.114 -3.645  55.285 1.000 7.52  ? 235  PRO A O    1 
ATOM   2898 C  CB   . PRO A 1 235 ? 15.321 -4.845  57.573 1.000 8.84  ? 235  PRO A CB   1 
ATOM   2899 C  CG   . PRO A 1 235 ? 15.854 -5.337  58.875 1.000 9.29  ? 235  PRO A CG   1 
ATOM   2900 C  CD   . PRO A 1 235 ? 17.338 -5.408  58.681 1.000 8.22  ? 235  PRO A CD   1 
ATOM   2901 H  HA   . PRO A 1 235 ? 15.869 -6.387  56.232 1.000 9.27  ? 235  PRO A HA   1 
ATOM   2902 H  HB3  . PRO A 1 235 ? 14.465 -5.199  57.408 1.000 10.61 ? 235  PRO A HB3  1 
ATOM   2903 H  HD3  . PRO A 1 235 ? 17.704 -6.122  59.195 1.000 9.86  ? 235  PRO A HD3  1 
ATOM   2904 N  N    . VAL A 1 236 ? 15.410 -4.774  54.371 1.000 7.37  ? 236  VAL A N    1 
ATOM   2905 C  CA   . VAL A 1 236 ? 15.294 -3.886  53.204 1.000 7.70  ? 236  VAL A CA   1 
ATOM   2906 C  C    . VAL A 1 236 ? 15.206 -2.413  53.605 1.000 7.24  ? 236  VAL A C    1 
ATOM   2907 O  O    . VAL A 1 236 ? 15.780 -1.561  52.940 1.000 8.02  ? 236  VAL A O    1 
ATOM   2908 C  CB   . VAL A 1 236 ? 14.109 -4.317  52.351 1.000 10.07 ? 236  VAL A CB   1 
ATOM   2909 C  CG1  . VAL A 1 236 ? 13.734 -3.362  51.269 1.000 12.57 ? 236  VAL A CG1  1 
ATOM   2910 C  CG2  . VAL A 1 236 ? 14.404 -5.687  51.739 1.000 11.41 ? 236  VAL A CG2  1 
ATOM   2911 H  HA   . VAL A 1 236 ? 16.104 -3.998  52.664 1.000 9.24  ? 236  VAL A HA   1 
ATOM   2912 H  HB   . VAL A 1 236 ? 13.334 -4.415  52.944 1.000 12.08 ? 236  VAL A HB   1 
ATOM   2913 H  HG11 . VAL A 1 236 ? 13.074 -3.739  50.705 1.000 18.86 ? 236  VAL A HG11 1 
ATOM   2914 H  HG12 . VAL A 1 236 ? 13.397 -2.600  51.711 1.000 18.86 ? 236  VAL A HG12 1 
ATOM   2915 H  HG23 . VAL A 1 236 ? 15.221 -5.639  51.285 1.000 17.11 ? 236  VAL A HG23 1 
ATOM   2916 N  N    . ASP A 1 237 ? 14.441 -2.094  54.643 1.000 7.49  ? 237  ASP A N    1 
ATOM   2917 C  CA   . ASP A 1 237 ? 14.240 -0.723  55.052 1.000 8.35  ? 237  ASP A CA   1 
ATOM   2918 C  C    . ASP A 1 237 ? 15.466 -0.124  55.737 1.000 8.01  ? 237  ASP A C    1 
ATOM   2919 O  O    . ASP A 1 237 ? 15.467 1.067   56.028 1.000 9.80  ? 237  ASP A O    1 
ATOM   2920 C  CB   . ASP A 1 237 ? 13.027 -0.632  55.975 1.000 10.95 ? 237  ASP A CB   1 
ATOM   2921 C  CG   . ASP A 1 237 ? 11.674 -0.776  55.300 1.000 12.36 ? 237  ASP A CG   1 
ATOM   2922 O  OD1  . ASP A 1 237 ? 11.626 -0.760  54.082 1.000 13.50 ? 237  ASP A OD1  1 
ATOM   2923 O  OD2  . ASP A 1 237 ? 10.700 -0.894  56.066 1.000 16.37 ? 237  ASP A OD2  1 
ATOM   2924 H  H    . ASP A 1 237 ? 14.054 -2.722  55.085 1.000 8.99  ? 237  ASP A H    1 
ATOM   2925 H  HA   . ASP A 1 237 ? 14.051 -0.193  54.250 1.000 10.02 ? 237  ASP A HA   1 
ATOM   2926 H  HB3  . ASP A 1 237 ? 13.033 0.210   56.433 1.000 13.14 ? 237  ASP A HB3  1 
ATOM   2927 N  N    . ASN A 1 238 ? 16.496 -0.940  55.999 1.000 7.63  ? 238  ASN A N    1 
ATOM   2928 C  CA   . ASN A 1 238 ? 17.729 -0.497  56.686 1.000 7.73  ? 238  ASN A CA   1 
ATOM   2929 C  C    . ASN A 1 238 ? 18.799 -0.088  55.708 1.000 7.31  ? 238  ASN A C    1 
ATOM   2930 O  O    . ASN A 1 238 ? 19.983 -0.064  56.068 1.000 8.08  ? 238  ASN A O    1 
ATOM   2931 C  CB   . ASN A 1 238 ? 18.255 -1.569  57.629 1.000 9.09  ? 238  ASN A CB   1 
ATOM   2932 C  CG   . ASN A 1 238 ? 17.561 -1.620  58.956 1.000 9.84  ? 238  ASN A CG   1 
ATOM   2933 O  OD1  . ASN A 1 238 ? 16.401 -1.268  59.056 1.000 11.17 ? 238  ASN A OD1  1 
ATOM   2934 N  ND2  . ASN A 1 238 ? 18.303 -2.117  59.945 1.000 10.97 ? 238  ASN A ND2  1 
ATOM   2935 H  H    . ASN A 1 238 ? 16.437 -1.763  55.756 1.000 9.15  ? 238  ASN A H    1 
ATOM   2936 H  HA   . ASN A 1 238 ? 17.503 0.289   57.225 1.000 9.27  ? 238  ASN A HA   1 
ATOM   2937 N  N    . TYR A 1 239 ? 18.453 0.260   54.461 1.000 7.04  ? 239  TYR A N    1 
ATOM   2938 C  CA   . TYR A 1 239 ? 19.476 0.592   53.498 1.000 7.34  ? 239  TYR A CA   1 
ATOM   2939 C  C    . TYR A 1 239 ? 20.389 1.693   53.962 1.000 7.54  ? 239  TYR A C    1 
ATOM   2940 O  O    . TYR A 1 239 ? 21.567 1.673   53.566 1.000 7.91  ? 239  TYR A O    1 
ATOM   2941 C  CB   . TYR A 1 239 ? 18.819 0.966   52.161 1.000 8.35  ? 239  TYR A CB   1 
ATOM   2942 C  CG   . TYR A 1 239 ? 17.867 2.085   52.212 1.000 8.82  ? 239  TYR A CG   1 
ATOM   2943 C  CD1  . TYR A 1 239 ? 18.352 3.406   52.019 1.000 10.49 ? 239  TYR A CD1  1 
ATOM   2944 C  CD2  . TYR A 1 239 ? 16.493 1.878   52.415 1.000 11.03 ? 239  TYR A CD2  1 
ATOM   2945 C  CE1  . TYR A 1 239 ? 17.473 4.427   52.045 1.000 14.81 ? 239  TYR A CE1  1 
ATOM   2946 C  CE2  . TYR A 1 239 ? 15.577 2.930   52.426 1.000 14.15 ? 239  TYR A CE2  1 
ATOM   2947 C  CZ   . TYR A 1 239 ? 16.110 4.188   52.249 1.000 16.70 ? 239  TYR A CZ   1 
ATOM   2948 O  OH   . TYR A 1 239 ? 15.227 5.279   52.254 1.000 26.35 ? 239  TYR A OH   1 
ATOM   2949 H  H    . TYR A 1 239 ? 17.624 0.287   54.235 1.000 8.45  ? 239  TYR A H    1 
ATOM   2950 H  HA   . TYR A 1 239 ? 20.022 -0.209  53.352 1.000 8.80  ? 239  TYR A HA   1 
ATOM   2951 H  HB2  . TYR A 1 239 ? 19.528 1.206   51.571 1.000 10.03 ? 239  TYR A HB2  1 
ATOM   2952 H  HE1  . TYR A 1 239 ? 17.775 5.298   51.926 1.000 17.77 ? 239  TYR A HE1  1 
ATOM   2953 N  N    . LYS A 1 240 ? 19.971 2.673   54.765 1.000 7.89  ? 240  LYS A N    1 
ATOM   2954 C  CA   . LYS A 1 240 ? 20.895 3.707   55.164 1.000 9.39  ? 240  LYS A CA   1 
ATOM   2955 C  C    . LYS A 1 240 ? 22.038 3.173   56.014 1.000 9.03  ? 240  LYS A C    1 
ATOM   2956 O  O    . LYS A 1 240 ? 23.085 3.831   56.096 1.000 11.57 ? 240  LYS A O    1 
ATOM   2957 C  CB   . LYS A 1 240 ? 20.190 4.840   55.945 1.000 9.80  ? 240  LYS A CB   1 
ATOM   2958 C  CG   . LYS A 1 240 ? 19.291 5.626   55.049 1.000 12.71 ? 240  LYS A CG   1 
ATOM   2959 C  CD   . LYS A 1 240 ? 18.596 6.745   55.839 1.000 16.99 ? 240  LYS A CD   1 
ATOM   2960 C  CE   . LYS A 1 240 ? 17.570 7.426   54.864 1.000 17.18 ? 240  LYS A CE   1 
ATOM   2961 N  NZ   . LYS A 1 240 ? 16.812 8.489   55.609 1.000 21.85 ? 240  LYS A NZ   1 
ATOM   2962 H  H    . LYS A 1 240 ? 19.157 2.688   55.043 1.000 9.47  ? 240  LYS A H    1 
ATOM   2963 H  HA   . LYS A 1 240 ? 21.281 4.096   54.352 1.000 11.27 ? 240  LYS A HA   1 
ATOM   2964 N  N    . THR A 1 241 ? 21.874 2.028   56.663 1.000 8.61  ? 241  THR A N    1 
ATOM   2965 C  CA   . THR A 1 241 ? 22.930 1.408   57.456 1.000 9.84  ? 241  THR A CA   1 
ATOM   2966 C  C    . THR A 1 241 ? 23.417 0.124   56.825 1.000 8.28  ? 241  THR A C    1 
ATOM   2967 O  O    . THR A 1 241 ? 24.057 -0.683  57.482 1.000 10.03 ? 241  THR A O    1 
ATOM   2968 C  CB   . THR A 1 241 ? 22.500 1.180   58.921 1.000 10.34 ? 241  THR A CB   1 
ATOM   2969 O  OG1  . THR A 1 241 ? 21.312 0.405   58.981 1.000 10.80 ? 241  THR A OG1  1 
ATOM   2970 C  CG2  . THR A 1 241 ? 22.231 2.534   59.612 1.000 11.93 ? 241  THR A CG2  1 
ATOM   2971 N  N    . CYS A 1 242 ? 23.099 -0.113  55.532 1.000 7.71  ? 242  CYS A N    1 
ATOM   2972 C  CA   . CYS A 1 242 ? 23.433 -1.348  54.859 1.000 7.37  ? 242  CYS A CA   1 
ATOM   2973 C  C    . CYS A 1 242 ? 23.363 -1.107  53.334 1.000 7.07  ? 242  CYS A C    1 
ATOM   2974 O  O    . CYS A 1 242 ? 22.536 -1.701  52.654 1.000 7.58  ? 242  CYS A O    1 
ATOM   2975 C  CB   . CYS A 1 242 ? 22.492 -2.450  55.295 1.000 8.15  ? 242  CYS A CB   1 
ATOM   2976 S  SG   . CYS A 1 242 ? 22.891 -4.066  54.585 1.000 7.75  ? 242  CYS A SG   1 
ATOM   2977 H  H    . CYS A 1 242 ? 22.682 0.496   55.092 1.000 9.25  ? 242  CYS A H    1 
ATOM   2978 H  HA   . CYS A 1 242 ? 24.349 -1.601  55.098 1.000 8.85  ? 242  CYS A HA   1 
ATOM   2979 H  HB2  . CYS A 1 242 ? 22.438 -2.445  56.252 1.000 9.78  ? 242  CYS A HB2  1 
ATOM   2980 N  N    . ASN A 1 243 ? 24.213 -0.213  52.849 1.000 6.95  ? 243  ASN A N    1 
ATOM   2981 C  CA   . ASN A 1 243 ? 24.302 0.088   51.435 1.000 6.83  ? 243  ASN A CA   1 
ATOM   2982 C  C    . ASN A 1 243 ? 25.746 -0.023  51.006 1.000 6.36  ? 243  ASN A C    1 
ATOM   2983 O  O    . ASN A 1 243 ? 26.697 -0.025  51.800 1.000 8.14  ? 243  ASN A O    1 
ATOM   2984 C  CB   . ASN A 1 243 ? 23.692 1.440   51.109 1.000 7.06  ? 243  ASN A CB   1 
ATOM   2985 C  CG   . ASN A 1 243 ? 24.498 2.575   51.696 1.000 7.89  ? 243  ASN A CG   1 
ATOM   2986 O  OD1  . ASN A 1 243 ? 25.507 2.993   51.090 1.000 9.63  ? 243  ASN A OD1  1 
ATOM   2987 N  ND2  . ASN A 1 243 ? 24.083 3.043   52.856 1.000 9.14  ? 243  ASN A ND2  1 
ATOM   2988 H  H    . ASN A 1 243 ? 24.732 0.203   53.395 1.000 8.34  ? 243  ASN A H    1 
ATOM   2989 H  HA   . ASN A 1 243 ? 23.793 -0.595  50.951 1.000 8.19  ? 243  ASN A HA   1 
ATOM   2990 H  HB2  . ASN A 1 243 ? 23.645 1.546   50.146 1.000 8.47  ? 243  ASN A HB2  1 
ATOM   2991 H  HB3  . ASN A 1 243 ? 22.788 1.475   51.458 1.000 8.47  ? 243  ASN A HB3  1 
ATOM   2992 N  N    . TRP A 1 244 ? 25.914 -0.103  49.671 1.000 6.84  ? 244  TRP A N    1 
ATOM   2993 C  CA   . TRP A 1 244 ? 27.270 -0.227  49.112 1.000 7.16  ? 244  TRP A CA   1 
ATOM   2994 C  C    . TRP A 1 244 ? 27.807 1.128   48.682 1.000 7.67  ? 244  TRP A C    1 
ATOM   2995 O  O    . TRP A 1 244 ? 29.033 1.288   48.586 1.000 9.96  ? 244  TRP A O    1 
ATOM   2996 C  CB   . TRP A 1 244 ? 27.292 -1.224  47.999 1.000 7.43  ? 244  TRP A CB   1 
ATOM   2997 C  CG   . TRP A 1 244 ? 27.069 -2.630  48.448 1.000 7.74  ? 244  TRP A CG   1 
ATOM   2998 C  CD1  . TRP A 1 244 ? 26.244 -3.143  49.420 1.000 7.82  ? 244  TRP A CD1  1 
ATOM   2999 C  CD2  . TRP A 1 244 ? 27.746 -3.817  47.889 1.000 7.14  ? 244  TRP A CD2  1 
ATOM   3000 N  NE1  . TRP A 1 244 ? 26.353 -4.501  49.529 1.000 8.13  ? 244  TRP A NE1  1 
ATOM   3001 C  CE2  . TRP A 1 244 ? 27.273 -4.950  48.577 1.000 7.32  ? 244  TRP A CE2  1 
ATOM   3002 C  CE3  . TRP A 1 244 ? 28.688 -4.006  46.897 1.000 7.52  ? 244  TRP A CE3  1 
ATOM   3003 C  CZ2  . TRP A 1 244 ? 27.678 -6.236  48.306 1.000 7.77  ? 244  TRP A CZ2  1 
ATOM   3004 C  CZ3  . TRP A 1 244 ? 29.125 -5.269  46.612 1.000 8.27  ? 244  TRP A CZ3  1 
ATOM   3005 C  CH2  . TRP A 1 244 ? 28.621 -6.364  47.310 1.000 8.30  ? 244  TRP A CH2  1 
ATOM   3006 H  HA   . TRP A 1 244 ? 27.853 -0.564  49.824 1.000 8.59  ? 244  TRP A HA   1 
ATOM   3007 H  HB2  . TRP A 1 244 ? 26.606 -0.989  47.355 1.000 8.91  ? 244  TRP A HB2  1 
ATOM   3008 H  HB3  . TRP A 1 244 ? 28.150 -1.171  47.549 1.000 8.91  ? 244  TRP A HB3  1 
ATOM   3009 H  HD1  . TRP A 1 244 ? 25.675 -2.625  49.943 1.000 9.38  ? 244  TRP A HD1  1 
ATOM   3010 H  HE3  . TRP A 1 244 ? 29.022 -3.277  46.426 1.000 9.02  ? 244  TRP A HE3  1 
ATOM   3011 H  HH2  . TRP A 1 244 ? 28.934 -7.214  47.097 1.000 9.96  ? 244  TRP A HH2  1 
ATOM   3012 N  N    . ALA A 1 245 ? 26.944 2.108   48.399 1.000 7.12  ? 245  ALA A N    1 
ATOM   3013 C  CA   . ALA A 1 245 ? 27.357 3.436   48.040 1.000 6.99  ? 245  ALA A CA   1 
ATOM   3014 C  C    . ALA A 1 245 ? 26.114 4.298   47.931 1.000 6.40  ? 245  ALA A C    1 
ATOM   3015 O  O    . ALA A 1 245 ? 25.003 3.821   47.731 1.000 7.93  ? 245  ALA A O    1 
ATOM   3016 C  CB   . ALA A 1 245 ? 28.103 3.542   46.715 1.000 9.20  ? 245  ALA A CB   1 
ATOM   3017 H  HA   . ALA A 1 245 ? 27.927 3.792   48.753 1.000 8.38  ? 245  ALA A HA   1 
ATOM   3018 H  HB3  . ALA A 1 245 ? 27.562 3.170   46.046 1.000 13.80 ? 245  ALA A HB3  1 
ATOM   3019 N  N    . ARG A 1 246 ? 26.331 5.618   47.992 1.000 7.08  ? 246  ARG A N    1 
ATOM   3020 C  CA   . ARG A 1 246 ? 25.349 6.628   47.632 1.000 6.96  ? 246  ARG A CA   1 
ATOM   3021 C  C    . ARG A 1 246 ? 25.796 7.228   46.330 1.000 7.13  ? 246  ARG A C    1 
ATOM   3022 O  O    . ARG A 1 246 ? 27.019 7.558   46.231 1.000 11.99 ? 246  ARG A O    1 
ATOM   3023 C  CB   A ARG A 1 246 ? 25.165 7.655   48.740 0.434 8.46  ? 246  ARG A CB   1 
ATOM   3024 C  CB   B ARG A 1 246 ? 25.325 7.701   48.703 0.566 11.36 ? 246  ARG A CB   1 
ATOM   3025 C  CG   A ARG A 1 246 ? 23.937 8.534   48.516 0.434 13.74 ? 246  ARG A CG   1 
ATOM   3026 C  CG   B ARG A 1 246 ? 24.182 8.679   48.559 0.566 16.21 ? 246  ARG A CG   1 
ATOM   3027 C  CD   A ARG A 1 246 ? 23.524 9.316   49.744 0.434 18.30 ? 246  ARG A CD   1 
ATOM   3028 C  CD   B ARG A 1 246 ? 24.006 9.573   49.786 0.566 19.80 ? 246  ARG A CD   1 
ATOM   3029 N  NE   A ARG A 1 246 ? 24.487 10.312  50.175 0.434 24.12 ? 246  ARG A NE   1 
ATOM   3030 N  NE   B ARG A 1 246 ? 22.656 10.138  49.743 0.566 18.71 ? 246  ARG A NE   1 
ATOM   3031 C  CZ   A ARG A 1 246 ? 24.991 11.378  49.590 0.434 28.48 ? 246  ARG A CZ   1 
ATOM   3032 C  CZ   B ARG A 1 246 ? 21.901 10.712  50.644 0.566 20.50 ? 246  ARG A CZ   1 
ATOM   3033 N  NH1  A ARG A 1 246 ? 25.880 12.133  50.234 0.434 28.98 ? 246  ARG A NH1  1 
ATOM   3034 N  NH1  B ARG A 1 246 ? 20.679 11.131  50.284 0.566 29.79 ? 246  ARG A NH1  1 
ATOM   3035 N  NH2  A ARG A 1 246 ? 24.704 11.804  48.369 0.434 29.93 ? 246  ARG A NH2  1 
ATOM   3036 N  NH2  B ARG A 1 246 ? 22.404 10.835  51.850 0.566 29.58 ? 246  ARG A NH2  1 
ATOM   3037 H  H    . ARG A 1 246 ? 27.102 5.887   48.262 1.000 8.49  ? 246  ARG A H    1 
ATOM   3038 H  HA   A ARG A 1 246 ? 24.490 6.180   47.483 1.000 8.35  ? 246  ARG A HA   1 
ATOM   3039 H  HB2  A ARG A 1 246 ? 25.075 7.194   49.589 0.434 10.16 ? 246  ARG A HB2  1 
ATOM   3040 H  HB2  B ARG A 1 246 ? 25.265 7.275   49.572 0.566 13.64 ? 246  ARG A HB2  1 
ATOM   3041 H  HB3  A ARG A 1 246 ? 25.954 8.216   48.788 0.434 10.16 ? 246  ARG A HB3  1 
ATOM   3042 H  HB3  B ARG A 1 246 ? 26.162 8.192   48.673 0.566 13.64 ? 246  ARG A HB3  1 
ATOM   3043 N  N    A VAL A 1 247 ? 24.888 7.327   45.386 0.703 7.12  ? 247  VAL A N    1 
ATOM   3044 N  N    B VAL A 1 247 ? 25.015 7.382   45.298 0.297 7.65  ? 247  VAL A N    1 
ATOM   3045 C  CA   A VAL A 1 247 ? 25.345 7.754   44.037 0.703 11.17 ? 247  VAL A CA   1 
ATOM   3046 C  CA   B VAL A 1 247 ? 25.475 7.877   43.979 0.297 5.23  ? 247  VAL A CA   1 
ATOM   3047 C  C    A VAL A 1 247 ? 24.417 8.834   43.457 0.703 7.70  ? 247  VAL A C    1 
ATOM   3048 C  C    B VAL A 1 247 ? 24.454 8.903   43.517 0.297 6.73  ? 247  VAL A C    1 
ATOM   3049 O  O    A VAL A 1 247 ? 23.244 8.935   43.821 0.703 6.37  ? 247  VAL A O    1 
ATOM   3050 O  O    B VAL A 1 247 ? 23.292 9.049   43.913 0.297 10.07 ? 247  VAL A O    1 
ATOM   3051 C  CB   A VAL A 1 247 ? 25.516 6.556   43.119 0.703 8.62  ? 247  VAL A CB   1 
ATOM   3052 C  CB   B VAL A 1 247 ? 25.538 6.741   42.957 0.297 6.33  ? 247  VAL A CB   1 
ATOM   3053 C  CG1  A VAL A 1 247 ? 24.131 6.064   42.664 0.703 13.93 ? 247  VAL A CG1  1 
ATOM   3054 C  CG1  B VAL A 1 247 ? 26.696 5.789   43.175 0.297 8.05  ? 247  VAL A CG1  1 
ATOM   3055 C  CG2  A VAL A 1 247 ? 26.294 6.876   41.899 0.703 10.50 ? 247  VAL A CG2  1 
ATOM   3056 C  CG2  B VAL A 1 247 ? 24.231 5.889   43.011 0.297 5.54  ? 247  VAL A CG2  1 
ATOM   3057 H  H    A VAL A 1 247 ? 24.061 7.152   45.542 0.703 8.54  ? 247  VAL A H    1 
ATOM   3058 H  H    B VAL A 1 247 ? 24.183 7.185   45.388 0.297 9.18  ? 247  VAL A H    1 
ATOM   3059 H  HG11 A VAL A 1 247 ? 23.599 5.847   43.433 0.703 20.90 ? 247  VAL A HG11 1 
ATOM   3060 H  HG12 A VAL A 1 247 ? 23.696 6.755   42.159 0.703 20.90 ? 247  VAL A HG12 1 
ATOM   3061 H  HG12 B VAL A 1 247 ? 27.509 6.301   43.238 0.297 12.08 ? 247  VAL A HG12 1 
ATOM   3062 H  HG13 A VAL A 1 247 ? 24.233 5.282   42.115 0.703 20.90 ? 247  VAL A HG13 1 
ATOM   3063 H  HG21 B VAL A 1 247 ? 23.471 6.460   42.876 0.297 8.31  ? 247  VAL A HG21 1 
ATOM   3064 H  HG22 B VAL A 1 247 ? 24.256 5.221   42.321 0.297 8.31  ? 247  VAL A HG22 1 
ATOM   3065 H  HG23 B VAL A 1 247 ? 24.162 5.462   43.868 0.297 8.31  ? 247  VAL A HG23 1 
ATOM   3066 N  N    . ALA A 1 248 ? 24.973 9.655   42.600 1.000 7.36  ? 248  ALA A N    1 
ATOM   3067 C  CA   . ALA A 1 248 ? 24.221 10.740  41.981 1.000 6.04  ? 248  ALA A CA   1 
ATOM   3068 C  C    . ALA A 1 248 ? 23.035 10.211  41.187 1.000 5.15  ? 248  ALA A C    1 
ATOM   3069 O  O    . ALA A 1 248 ? 23.116 9.195   40.500 1.000 6.24  ? 248  ALA A O    1 
ATOM   3070 C  CB   . ALA A 1 248 ? 25.136 11.499  41.025 1.000 7.32  ? 248  ALA A CB   1 
ATOM   3071 H  HA   . ALA A 1 248 ? 23.899 11.351  42.677 1.000 7.24  ? 248  ALA A HA   1 
ATOM   3072 H  HB2  . ALA A 1 248 ? 25.802 11.947  41.519 1.000 10.98 ? 248  ALA A HB2  1 
ATOM   3073 H  HB3  . ALA A 1 248 ? 25.560 10.879  40.457 1.000 10.98 ? 248  ALA A HB3  1 
ATOM   3074 N  N    . ALA A 1 249 ? 21.942 10.970  41.236 1.000 5.31  ? 249  ALA A N    1 
ATOM   3075 C  CA   . ALA A 1 249 ? 20.736 10.670  40.505 1.000 5.04  ? 249  ALA A CA   1 
ATOM   3076 C  C    . ALA A 1 249 ? 20.987 10.505  39.021 1.000 4.55  ? 249  ALA A C    1 
ATOM   3077 O  O    . ALA A 1 249 ? 21.879 11.098  38.412 1.000 5.25  ? 249  ALA A O    1 
ATOM   3078 C  CB   . ALA A 1 249 ? 19.717 11.789  40.678 1.000 5.63  ? 249  ALA A CB   1 
ATOM   3079 H  H    . ALA A 1 249 ? 21.956 11.675  41.729 1.000 6.37  ? 249  ALA A H    1 
ATOM   3080 H  HA   . ALA A 1 249 ? 20.354 9.838   40.855 1.000 6.05  ? 249  ALA A HA   1 
ATOM   3081 H  HB1  . ALA A 1 249 ? 18.921 11.575  40.186 1.000 8.45  ? 249  ALA A HB1  1 
ATOM   3082 H  HB2  . ALA A 1 249 ? 19.502 11.885  41.609 1.000 8.45  ? 249  ALA A HB2  1 
ATOM   3083 H  HB3  . ALA A 1 249 ? 20.086 12.611  40.348 1.000 8.45  ? 249  ALA A HB3  1 
ATOM   3084 N  N    . HIS A 1 250 ? 20.116 9.707   38.387 1.000 5.09  ? 250  HIS A N    1 
ATOM   3085 C  CA   . HIS A 1 250 ? 20.041 9.756   36.932 1.000 4.68  ? 250  HIS A CA   1 
ATOM   3086 C  C    . HIS A 1 250 ? 19.826 11.199  36.478 1.000 4.77  ? 250  HIS A C    1 
ATOM   3087 O  O    . HIS A 1 250 ? 19.193 11.997  37.174 1.000 5.57  ? 250  HIS A O    1 
ATOM   3088 C  CB   . HIS A 1 250 ? 18.927 8.872   36.400 1.000 4.77  ? 250  HIS A CB   1 
ATOM   3089 C  CG   . HIS A 1 250 ? 19.207 7.426   36.564 1.000 4.45  ? 250  HIS A CG   1 
ATOM   3090 N  ND1  . HIS A 1 250 ? 18.678 6.452   35.748 1.000 5.17  ? 250  HIS A ND1  1 
ATOM   3091 C  CD2  . HIS A 1 250 ? 19.999 6.735   37.443 1.000 4.66  ? 250  HIS A CD2  1 
ATOM   3092 C  CE1  . HIS A 1 250 ? 19.158 5.276   36.129 1.000 4.97  ? 250  HIS A CE1  1 
ATOM   3093 N  NE2  . HIS A 1 250 ? 19.964 5.388   37.156 1.000 4.86  ? 250  HIS A NE2  1 
ATOM   3094 H  H    . HIS A 1 250 ? 19.608 9.175   38.832 1.000 6.11  ? 250  HIS A H    1 
ATOM   3095 H  HA   . HIS A 1 250 ? 20.892 9.438   36.565 1.000 5.62  ? 250  HIS A HA   1 
ATOM   3096 H  HB2  . HIS A 1 250 ? 18.103 9.088   36.864 1.000 5.72  ? 250  HIS A HB2  1 
ATOM   3097 H  HB3  . HIS A 1 250 ? 18.795 9.063   35.458 1.000 5.72  ? 250  HIS A HB3  1 
ATOM   3098 H  HD1  . HIS A 1 250 ? 18.128 6.584   35.100 1.000 6.20  ? 250  HIS A HD1  1 
ATOM   3099 H  HD2  . HIS A 1 250 ? 20.488 7.120   38.133 1.000 5.60  ? 250  HIS A HD2  1 
ATOM   3100 H  HE1  . HIS A 1 250 ? 18.948 4.469   35.718 1.000 5.96  ? 250  HIS A HE1  1 
ATOM   3101 N  N    . ALA A 1 251 ? 20.382 11.519  35.309 1.000 4.80  ? 251  ALA A N    1 
ATOM   3102 C  CA   . ALA A 1 251 ? 20.324 12.881  34.801 1.000 5.02  ? 251  ALA A CA   1 
ATOM   3103 C  C    . ALA A 1 251 ? 19.992 12.902  33.335 1.000 4.89  ? 251  ALA A C    1 
ATOM   3104 O  O    . ALA A 1 251 ? 20.434 12.034  32.553 1.000 5.38  ? 251  ALA A O    1 
ATOM   3105 C  CB   . ALA A 1 251 ? 21.634 13.600  35.021 1.000 6.19  ? 251  ALA A CB   1 
ATOM   3106 H  H    . ALA A 1 251 ? 20.781 10.912  34.848 1.000 5.76  ? 251  ALA A H    1 
ATOM   3107 H  HA   . ALA A 1 251 ? 19.621 13.362  35.285 1.000 6.02  ? 251  ALA A HA   1 
ATOM   3108 H  HB1  . ALA A 1 251 ? 22.275 13.163  34.477 1.000 9.28  ? 251  ALA A HB1  1 
ATOM   3109 N  N    . VAL A 1 252 ? 19.268 13.931  32.940 1.000 5.33  ? 252  VAL A N    1 
ATOM   3110 C  CA   . VAL A 1 252 ? 19.059 14.247  31.529 1.000 4.88  ? 252  VAL A CA   1 
ATOM   3111 C  C    . VAL A 1 252 ? 20.355 14.872  31.021 1.000 5.34  ? 252  VAL A C    1 
ATOM   3112 O  O    . VAL A 1 252 ? 20.854 15.842  31.616 1.000 6.16  ? 252  VAL A O    1 
ATOM   3113 C  CB   . VAL A 1 252 ? 17.908 15.256  31.361 1.000 5.66  ? 252  VAL A CB   1 
ATOM   3114 C  CG1  . VAL A 1 252 ? 17.751 15.641  29.914 1.000 6.74  ? 252  VAL A CG1  1 
ATOM   3115 C  CG2  . VAL A 1 252 ? 16.617 14.675  31.945 1.000 6.42  ? 252  VAL A CG2  1 
ATOM   3116 H  H    . VAL A 1 252 ? 18.906 14.435  33.535 1.000 6.40  ? 252  VAL A H    1 
ATOM   3117 H  HA   . VAL A 1 252 ? 18.862 13.428  31.028 1.000 5.86  ? 252  VAL A HA   1 
ATOM   3118 H  HB   . VAL A 1 252 ? 18.135 16.063  31.868 1.000 6.79  ? 252  VAL A HB   1 
ATOM   3119 H  HG12 . VAL A 1 252 ? 17.524 14.867  29.438 1.000 10.10 ? 252  VAL A HG12 1 
ATOM   3120 H  HG21 . VAL A 1 252 ? 16.757 14.416  32.853 1.000 9.63  ? 252  VAL A HG21 1 
ATOM   3121 N  N    . VAL A 1 253 ? 20.875 14.343  29.920 1.000 5.00  ? 253  VAL A N    1 
ATOM   3122 C  CA   . VAL A 1 253 ? 22.052 14.888  29.275 1.000 5.50  ? 253  VAL A CA   1 
ATOM   3123 C  C    . VAL A 1 253 ? 21.676 15.499  27.931 1.000 5.39  ? 253  VAL A C    1 
ATOM   3124 O  O    . VAL A 1 253 ? 20.682 15.116  27.291 1.000 6.01  ? 253  VAL A O    1 
ATOM   3125 C  CB   . VAL A 1 253 ? 23.195 13.869  29.128 1.000 5.55  ? 253  VAL A CB   1 
ATOM   3126 C  CG1  . VAL A 1 253 ? 23.596 13.307  30.497 1.000 6.63  ? 253  VAL A CG1  1 
ATOM   3127 C  CG2  . VAL A 1 253 ? 22.853 12.768  28.151 1.000 6.31  ? 253  VAL A CG2  1 
ATOM   3128 H  H    . VAL A 1 253 ? 20.498 13.650  29.577 1.000 6.00  ? 253  VAL A H    1 
ATOM   3129 H  HA   . VAL A 1 253 ? 22.382 15.615  29.842 1.000 6.60  ? 253  VAL A HA   1 
ATOM   3130 H  HG21 . VAL A 1 253 ? 22.607 13.154  27.307 1.000 9.47  ? 253  VAL A HG21 1 
ATOM   3131 H  HG22 . VAL A 1 253 ? 23.615 12.197  28.032 1.000 9.47  ? 253  VAL A HG22 1 
ATOM   3132 H  HG23 . VAL A 1 253 ? 22.118 12.254  28.493 1.000 9.47  ? 253  VAL A HG23 1 
ATOM   3133 N  N    . ALA A 1 254 ? 22.539 16.423  27.499 1.000 5.53  ? 254  ALA A N    1 
ATOM   3134 C  CA   . ALA A 1 254 ? 22.281 17.209  26.283 1.000 5.68  ? 254  ALA A CA   1 
ATOM   3135 C  C    . ALA A 1 254 ? 23.617 17.786  25.809 1.000 5.88  ? 254  ALA A C    1 
ATOM   3136 O  O    . ALA A 1 254 ? 24.594 17.875  26.571 1.000 6.15  ? 254  ALA A O    1 
ATOM   3137 C  CB   . ALA A 1 254 ? 21.323 18.356  26.594 1.000 6.15  ? 254  ALA A CB   1 
ATOM   3138 H  HB1  . ALA A 1 254 ? 21.321 19.017  25.915 1.000 9.23  ? 254  ALA A HB1  1 
ATOM   3139 H  HB2  . ALA A 1 254 ? 20.450 18.008  26.725 1.000 9.23  ? 254  ALA A HB2  1 
ATOM   3140 N  N    . ARG A 1 255 ? 23.658 18.212  24.570 1.000 5.82  ? 255  ARG A N    1 
ATOM   3141 C  CA   . ARG A 1 255 ? 24.794 18.979  24.080 1.000 6.23  ? 255  ARG A CA   1 
ATOM   3142 C  C    . ARG A 1 255 ? 24.967 20.245  24.941 1.000 6.15  ? 255  ARG A C    1 
ATOM   3143 O  O    . ARG A 1 255 ? 24.021 20.803  25.448 1.000 6.75  ? 255  ARG A O    1 
ATOM   3144 C  CB   . ARG A 1 255 ? 24.553 19.469  22.640 1.000 6.76  ? 255  ARG A CB   1 
ATOM   3145 C  CG   . ARG A 1 255 ? 24.430 18.335  21.611 1.000 6.38  ? 255  ARG A CG   1 
ATOM   3146 C  CD   . ARG A 1 255 ? 24.211 18.902  20.203 1.000 6.67  ? 255  ARG A CD   1 
ATOM   3147 N  NE   . ARG A 1 255 ? 22.993 19.718  20.150 1.000 7.06  ? 255  ARG A NE   1 
ATOM   3148 C  CZ   . ARG A 1 255 ? 21.759 19.194  20.044 1.000 6.42  ? 255  ARG A CZ   1 
ATOM   3149 N  NH1  . ARG A 1 255 ? 21.572 17.893  19.860 1.000 6.51  ? 255  ARG A NH1  1 
ATOM   3150 N  NH2  . ARG A 1 255 ? 20.718 19.991  20.119 1.000 7.49  ? 255  ARG A NH2  1 
ATOM   3151 H  H    . ARG A 1 255 ? 23.005 18.036  24.039 1.000 6.98  ? 255  ARG A H    1 
ATOM   3152 H  HB2  . ARG A 1 255 ? 23.740 19.998  22.621 1.000 8.11  ? 255  ARG A HB2  1 
ATOM   3153 H  HB3  . ARG A 1 255 ? 25.287 20.049  22.380 1.000 8.11  ? 255  ARG A HB3  1 
ATOM   3154 H  HG2  . ARG A 1 255 ? 25.238 17.799  21.623 1.000 7.66  ? 255  ARG A HG2  1 
ATOM   3155 H  HG3  . ARG A 1 255 ? 23.685 17.762  21.849 1.000 7.66  ? 255  ARG A HG3  1 
ATOM   3156 H  HD3  . ARG A 1 255 ? 24.105 18.165  19.613 1.000 8.01  ? 255  ARG A HD3  1 
ATOM   3157 H  HH11 . ARG A 1 255 ? 20.774 17.579  19.792 1.000 7.81  ? 255  ARG A HH11 1 
ATOM   3158 H  HH12 . ARG A 1 255 ? 22.248 17.363  19.810 1.000 7.81  ? 255  ARG A HH12 1 
ATOM   3159 H  HH22 . ARG A 1 255 ? 20.833 20.800  20.221 1.000 8.99  ? 255  ARG A HH22 1 
ATOM   3160 N  N    . ASP A 1 256 ? 26.231 20.700  24.976 1.000 6.98  ? 256  ASP A N    1 
ATOM   3161 C  CA   . ASP A 1 256 ? 26.531 22.002  25.567 1.000 7.64  ? 256  ASP A CA   1 
ATOM   3162 C  C    . ASP A 1 256 ? 26.300 23.103  24.547 1.000 7.53  ? 256  ASP A C    1 
ATOM   3163 O  O    . ASP A 1 256 ? 27.205 23.604  23.900 1.000 9.19  ? 256  ASP A O    1 
ATOM   3164 C  CB   . ASP A 1 256 ? 27.970 22.048  26.066 1.000 9.29  ? 256  ASP A CB   1 
ATOM   3165 C  CG   . ASP A 1 256 ? 28.249 23.300  26.881 1.000 10.17 ? 256  ASP A CG   1 
ATOM   3166 O  OD1  . ASP A 1 256 ? 27.339 24.114  27.136 1.000 12.12 ? 256  ASP A OD1  1 
ATOM   3167 O  OD2  . ASP A 1 256 ? 29.468 23.446  27.252 1.000 14.00 ? 256  ASP A OD2  1 
ATOM   3168 H  HA   . ASP A 1 256 ? 25.930 22.147  26.327 1.000 9.17  ? 256  ASP A HA   1 
ATOM   3169 H  HB3  . ASP A 1 256 ? 28.557 22.011  25.329 1.000 11.15 ? 256  ASP A HB3  1 
ATOM   3170 N  N    . ASP A 1 257 ? 25.005 23.401  24.341 1.000 7.65  ? 257  ASP A N    1 
ATOM   3171 C  CA   . ASP A 1 257 ? 24.612 24.461  23.398 1.000 7.99  ? 257  ASP A CA   1 
ATOM   3172 C  C    . ASP A 1 257 ? 23.315 25.069  23.923 1.000 8.62  ? 257  ASP A C    1 
ATOM   3173 O  O    . ASP A 1 257 ? 22.837 24.782  25.021 1.000 9.79  ? 257  ASP A O    1 
ATOM   3174 C  CB   . ASP A 1 257 ? 24.588 24.008  21.967 1.000 8.45  ? 257  ASP A CB   1 
ATOM   3175 C  CG   . ASP A 1 257 ? 23.474 23.036  21.631 1.000 8.41  ? 257  ASP A CG   1 
ATOM   3176 O  OD1  . ASP A 1 257 ? 23.564 22.391  20.553 1.000 9.12  ? 257  ASP A OD1  1 
ATOM   3177 O  OD2  . ASP A 1 257 ? 22.467 22.950  22.368 1.000 8.38  ? 257  ASP A OD2  1 
ATOM   3178 H  H    . ASP A 1 257 ? 24.398 22.966  24.767 1.000 9.18  ? 257  ASP A H    1 
ATOM   3179 H  HA   . ASP A 1 257 ? 25.296 25.161  23.460 1.000 9.59  ? 257  ASP A HA   1 
ATOM   3180 N  N    . ASN A 1 258 ? 22.790 26.013  23.131 1.000 10.35 ? 258  ASN A N    1 
ATOM   3181 C  CA   A ASN A 1 258 ? 21.605 26.791  23.480 0.231 12.46 ? 258  ASN A CA   1 
ATOM   3182 C  CA   B ASN A 1 258 ? 21.648 26.764  23.697 0.481 13.09 ? 258  ASN A CA   1 
ATOM   3183 C  CA   C ASN A 1 258 ? 21.616 26.778  23.530 0.288 12.77 ? 258  ASN A CA   1 
ATOM   3184 C  C    . ASN A 1 258 ? 20.351 25.948  23.662 1.000 9.51  ? 258  ASN A C    1 
ATOM   3185 O  O    . ASN A 1 258 ? 19.355 26.430  24.289 1.000 11.37 ? 258  ASN A O    1 
ATOM   3186 C  CB   A ASN A 1 258 ? 21.268 27.875  22.431 0.231 13.51 ? 258  ASN A CB   1 
ATOM   3187 C  CB   B ASN A 1 258 ? 21.556 28.160  23.055 0.481 15.71 ? 258  ASN A CB   1 
ATOM   3188 C  CB   C ASN A 1 258 ? 21.394 27.925  22.533 0.288 15.40 ? 258  ASN A CB   1 
ATOM   3189 C  CG   A ASN A 1 258 ? 20.185 28.839  22.895 0.231 16.32 ? 258  ASN A CG   1 
ATOM   3190 C  CG   B ASN A 1 258 ? 22.724 29.073  23.394 0.481 24.68 ? 258  ASN A CG   1 
ATOM   3191 C  CG   C ASN A 1 258 ? 21.601 27.539  21.081 0.288 19.21 ? 258  ASN A CG   1 
ATOM   3192 O  OD1  A ASN A 1 258 ? 19.124 29.074  22.280 0.231 15.71 ? 258  ASN A OD1  1 
ATOM   3193 O  OD1  B ASN A 1 258 ? 23.163 29.068  24.552 0.481 33.53 ? 258  ASN A OD1  1 
ATOM   3194 O  OD1  C ASN A 1 258 ? 22.647 27.004  20.708 0.288 30.22 ? 258  ASN A OD1  1 
ATOM   3195 N  ND2  A ASN A 1 258 ? 20.437 29.462  24.046 0.231 18.44 ? 258  ASN A ND2  1 
ATOM   3196 N  ND2  B ASN A 1 258 ? 23.207 29.836  22.426 0.481 30.75 ? 258  ASN A ND2  1 
ATOM   3197 N  ND2  C ASN A 1 258 ? 20.559 27.859  20.300 0.288 19.57 ? 258  ASN A ND2  1 
ATOM   3198 N  N    . LYS A 1 259 ? 20.297 24.748  23.119 1.000 8.76  ? 259  LYS A N    1 
ATOM   3199 C  CA   . LYS A 1 259 ? 19.031 23.998  23.139 1.000 7.88  ? 259  LYS A CA   1 
ATOM   3200 C  C    . LYS A 1 259 ? 18.634 23.553  24.528 1.000 7.35  ? 259  LYS A C    1 
ATOM   3201 O  O    . LYS A 1 259 ? 17.489 23.162  24.753 1.000 7.81  ? 259  LYS A O    1 
ATOM   3202 C  CB   . LYS A 1 259 ? 19.131 22.807  22.139 1.000 8.31  ? 259  LYS A CB   1 
ATOM   3203 C  CG   . LYS A 1 259 ? 17.782 22.188  21.813 1.000 8.10  ? 259  LYS A CG   1 
ATOM   3204 C  CD   . LYS A 1 259 ? 16.800 23.172  21.185 1.000 8.53  ? 259  LYS A CD   1 
ATOM   3205 C  CE   . LYS A 1 259 ? 15.592 22.446  20.685 1.000 9.17  ? 259  LYS A CE   1 
ATOM   3206 N  NZ   . LYS A 1 259 ? 14.567 23.405  20.138 1.000 9.27  ? 259  LYS A NZ   1 
ATOM   3207 H  HA   . LYS A 1 259 ? 18.329 24.598  22.811 1.000 9.45  ? 259  LYS A HA   1 
ATOM   3208 H  HG3  . LYS A 1 259 ? 17.384 21.823  22.618 1.000 9.73  ? 259  LYS A HG3  1 
ATOM   3209 H  HD2  . LYS A 1 259 ? 16.534 23.833  21.844 1.000 10.23 ? 259  LYS A HD2  1 
ATOM   3210 H  HD3  . LYS A 1 259 ? 17.229 23.636  20.448 1.000 10.23 ? 259  LYS A HD3  1 
ATOM   3211 H  HE3  . LYS A 1 259 ? 15.200 21.941  21.415 1.000 11.01 ? 259  LYS A HE3  1 
ATOM   3212 H  HZ3  . LYS A 1 259 ? 14.919 23.859  19.458 1.000 13.90 ? 259  LYS A HZ3  1 
ATOM   3213 N  N    . VAL A 1 260 ? 19.566 23.649  25.482 1.000 7.61  ? 260  VAL A N    1 
ATOM   3214 C  CA   . VAL A 1 260 ? 19.275 23.283  26.856 1.000 7.19  ? 260  VAL A CA   1 
ATOM   3215 C  C    . VAL A 1 260 ? 18.074 24.069  27.376 1.000 7.21  ? 260  VAL A C    1 
ATOM   3216 O  O    . VAL A 1 260 ? 17.297 23.536  28.189 1.000 8.05  ? 260  VAL A O    1 
ATOM   3217 C  CB   A VAL A 1 260 ? 20.462 23.423  27.816 0.515 7.09  ? 260  VAL A CB   1 
ATOM   3218 C  CB   B VAL A 1 260 ? 20.535 23.601  27.688 0.485 7.96  ? 260  VAL A CB   1 
ATOM   3219 C  CG1  A VAL A 1 260 ? 21.578 22.505  27.336 0.515 6.57  ? 260  VAL A CG1  1 
ATOM   3220 C  CG1  B VAL A 1 260 ? 20.226 23.398  29.152 0.485 8.33  ? 260  VAL A CG1  1 
ATOM   3221 C  CG2  A VAL A 1 260 ? 20.901 24.852  27.906 0.515 7.21  ? 260  VAL A CG2  1 
ATOM   3222 C  CG2  B VAL A 1 260 ? 21.744 22.738  27.319 0.485 11.69 ? 260  VAL A CG2  1 
ATOM   3223 H  H    . VAL A 1 260 ? 20.351 23.934  25.278 1.000 9.13  ? 260  VAL A H    1 
ATOM   3224 H  HA   A VAL A 1 260 ? 19.019 22.337  26.852 1.000 8.63  ? 260  VAL A HA   1 
ATOM   3225 H  HG11 A VAL A 1 260 ? 21.266 21.599  27.276 0.515 9.85  ? 260  VAL A HG11 1 
ATOM   3226 H  HG11 B VAL A 1 260 ? 20.995 23.683  29.650 0.485 12.50 ? 260  VAL A HG11 1 
ATOM   3227 H  HG12 A VAL A 1 260 ? 21.886 22.796  26.475 0.515 9.85  ? 260  VAL A HG12 1 
ATOM   3228 H  HG12 B VAL A 1 260 ? 20.050 22.472  29.336 0.485 12.50 ? 260  VAL A HG12 1 
ATOM   3229 H  HG21 A VAL A 1 260 ? 21.634 24.915  28.522 0.515 10.82 ? 260  VAL A HG21 1 
ATOM   3230 H  HG21 B VAL A 1 260 ? 21.897 22.862  26.380 0.485 17.54 ? 260  VAL A HG21 1 
ATOM   3231 H  HG23 B VAL A 1 260 ? 21.573 21.810  27.496 0.485 17.54 ? 260  VAL A HG23 1 
ATOM   3232 N  N    . GLU A 1 261 ? 17.903 25.317  26.966 1.000 7.74  ? 261  GLU A N    1 
ATOM   3233 C  CA   . GLU A 1 261 ? 16.804 26.111  27.513 1.000 7.97  ? 261  GLU A CA   1 
ATOM   3234 C  C    . GLU A 1 261 ? 15.449 25.539  27.113 1.000 7.17  ? 261  GLU A C    1 
ATOM   3235 O  O    . GLU A 1 261 ? 14.554 25.420  27.957 1.000 7.78  ? 261  GLU A O    1 
ATOM   3236 C  CB   . GLU A 1 261 ? 16.941 27.583  27.105 1.000 11.68 ? 261  GLU A CB   1 
ATOM   3237 C  CG   . GLU A 1 261 ? 18.199 28.229  27.625 1.000 15.54 ? 261  GLU A CG   1 
ATOM   3238 C  CD   . GLU A 1 261 ? 18.336 28.184  29.123 1.000 18.99 ? 261  GLU A CD   1 
ATOM   3239 O  OE1  . GLU A 1 261 ? 19.493 28.039  29.579 1.000 28.61 ? 261  GLU A OE1  1 
ATOM   3240 O  OE2  . GLU A 1 261 ? 17.256 28.275  29.808 1.000 24.41 ? 261  GLU A OE2  1 
ATOM   3241 H  HA   . GLU A 1 261 ? 16.866 26.068  28.490 1.000 9.57  ? 261  GLU A HA   1 
ATOM   3242 N  N    . ASP A 1 262 ? 15.277 25.175  25.850 1.000 7.22  ? 262  ASP A N    1 
ATOM   3243 C  CA   . ASP A 1 262 ? 14.036 24.563  25.410 1.000 6.85  ? 262  ASP A CA   1 
ATOM   3244 C  C    . ASP A 1 262 ? 13.784 23.221  26.127 1.000 6.47  ? 262  ASP A C    1 
ATOM   3245 O  O    . ASP A 1 262 ? 12.654 22.881  26.418 1.000 6.67  ? 262  ASP A O    1 
ATOM   3246 C  CB   . ASP A 1 262 ? 14.005 24.379  23.910 1.000 7.37  ? 262  ASP A CB   1 
ATOM   3247 C  CG   . ASP A 1 262 ? 13.831 25.626  23.075 1.000 8.22  ? 262  ASP A CG   1 
ATOM   3248 O  OD1  . ASP A 1 262 ? 13.586 26.690  23.659 1.000 9.03  ? 262  ASP A OD1  1 
ATOM   3249 O  OD2  . ASP A 1 262 ? 13.907 25.494  21.838 1.000 8.88  ? 262  ASP A OD2  1 
ATOM   3250 H  H    . ASP A 1 262 ? 15.909 25.304  25.282 1.000 8.66  ? 262  ASP A H    1 
ATOM   3251 H  HA   . ASP A 1 262 ? 13.305 25.170  25.650 1.000 8.22  ? 262  ASP A HA   1 
ATOM   3252 H  HB2  . ASP A 1 262 ? 14.833 23.950  23.643 1.000 8.85  ? 262  ASP A HB2  1 
ATOM   3253 H  HB3  . ASP A 1 262 ? 13.282 23.770  23.696 1.000 8.85  ? 262  ASP A HB3  1 
ATOM   3254 N  N    . ILE A 1 263 ? 14.871 22.433  26.273 1.000 6.24  ? 263  ILE A N    1 
ATOM   3255 C  CA   . ILE A 1 263 ? 14.711 21.138  26.939 1.000 6.07  ? 263  ILE A CA   1 
ATOM   3256 C  C    . ILE A 1 263 ? 14.187 21.349  28.366 1.000 5.91  ? 263  ILE A C    1 
ATOM   3257 O  O    . ILE A 1 263 ? 13.239 20.697  28.800 1.000 6.40  ? 263  ILE A O    1 
ATOM   3258 C  CB   . ILE A 1 263 ? 16.004 20.305  26.915 1.000 6.12  ? 263  ILE A CB   1 
ATOM   3259 C  CG1  . ILE A 1 263 ? 16.492 20.041  25.479 1.000 6.71  ? 263  ILE A CG1  1 
ATOM   3260 C  CG2  . ILE A 1 263 ? 15.807 19.037  27.689 1.000 6.90  ? 263  ILE A CG2  1 
ATOM   3261 C  CD1  . ILE A 1 263 ? 17.953 19.650  25.400 1.000 7.34  ? 263  ILE A CD1  1 
ATOM   3262 H  HA   . ILE A 1 263 ? 14.029 20.636  26.446 1.000 7.29  ? 263  ILE A HA   1 
ATOM   3263 H  HB   . ILE A 1 263 ? 16.698 20.824  27.372 1.000 7.35  ? 263  ILE A HB   1 
ATOM   3264 H  HG12 . ILE A 1 263 ? 15.956 19.332  25.091 1.000 8.05  ? 263  ILE A HG12 1 
ATOM   3265 H  HG13 . ILE A 1 263 ? 16.352 20.841  24.949 1.000 8.05  ? 263  ILE A HG13 1 
ATOM   3266 H  HG21 . ILE A 1 263 ? 16.616 18.522  27.670 1.000 10.35 ? 263  ILE A HG21 1 
ATOM   3267 H  HG22 . ILE A 1 263 ? 15.583 19.248  28.598 1.000 10.35 ? 263  ILE A HG22 1 
ATOM   3268 H  HG23 . ILE A 1 263 ? 15.095 18.528  27.294 1.000 10.35 ? 263  ILE A HG23 1 
ATOM   3269 H  HD11 . ILE A 1 263 ? 18.195 19.500  24.483 1.000 11.01 ? 263  ILE A HD11 1 
ATOM   3270 H  HD12 . ILE A 1 263 ? 18.494 20.356  25.762 1.000 11.01 ? 263  ILE A HD12 1 
ATOM   3271 H  HD13 . ILE A 1 263 ? 18.098 18.846  25.905 1.000 11.01 ? 263  ILE A HD13 1 
ATOM   3272 N  N    . TRP A 1 264 ? 14.801 22.271  29.103 1.000 6.16  ? 264  TRP A N    1 
ATOM   3273 C  CA   . TRP A 1 264 ? 14.346 22.537  30.451 1.000 6.45  ? 264  TRP A CA   1 
ATOM   3274 C  C    . TRP A 1 264 ? 12.954 23.141  30.486 1.000 6.74  ? 264  TRP A C    1 
ATOM   3275 O  O    . TRP A 1 264 ? 12.137 22.777  31.319 1.000 7.57  ? 264  TRP A O    1 
ATOM   3276 C  CB   . TRP A 1 264 ? 15.393 23.438  31.236 1.000 6.86  ? 264  TRP A CB   1 
ATOM   3277 C  CG   . TRP A 1 264 ? 14.809 23.669  32.582 1.000 7.25  ? 264  TRP A CG   1 
ATOM   3278 C  CD1  . TRP A 1 264 ? 14.255 24.824  33.048 1.000 8.83  ? 264  TRP A CD1  1 
ATOM   3279 C  CD2  . TRP A 1 264 ? 14.624 22.683  33.610 1.000 7.45  ? 264  TRP A CD2  1 
ATOM   3280 N  NE1  . TRP A 1 264 ? 13.736 24.640  34.313 1.000 9.14  ? 264  TRP A NE1  1 
ATOM   3281 C  CE2  . TRP A 1 264 ? 13.945 23.332  34.670 1.000 8.12  ? 264  TRP A CE2  1 
ATOM   3282 C  CE3  . TRP A 1 264 ? 14.925 21.339  33.724 1.000 8.12  ? 264  TRP A CE3  1 
ATOM   3283 C  CZ2  . TRP A 1 264 ? 13.604 22.640  35.863 1.000 9.11  ? 264  TRP A CZ2  1 
ATOM   3284 C  CZ3  . TRP A 1 264 ? 14.564 20.695  34.880 1.000 9.12  ? 264  TRP A CZ3  1 
ATOM   3285 C  CH2  . TRP A 1 264 ? 13.908 21.329  35.924 1.000 8.97  ? 264  TRP A CH2  1 
ATOM   3286 H  H    . TRP A 1 264 ? 15.466 22.709  28.779 1.000 7.40  ? 264  TRP A H    1 
ATOM   3287 H  HA   . TRP A 1 264 ? 14.300 21.675  30.916 1.000 7.74  ? 264  TRP A HA   1 
ATOM   3288 H  HB2  . TRP A 1 264 ? 16.245 22.981  31.308 1.000 8.23  ? 264  TRP A HB2  1 
ATOM   3289 H  HD1  . TRP A 1 264 ? 14.229 25.626  32.577 1.000 10.59 ? 264  TRP A HD1  1 
ATOM   3290 H  HE1  . TRP A 1 264 ? 13.349 25.240  34.794 1.000 10.96 ? 264  TRP A HE1  1 
ATOM   3291 H  HE3  . TRP A 1 264 ? 15.359 20.885  33.038 1.000 9.75  ? 264  TRP A HE3  1 
ATOM   3292 H  HZ2  . TRP A 1 264 ? 13.187 23.074  36.572 1.000 10.94 ? 264  TRP A HZ2  1 
ATOM   3293 H  HZ3  . TRP A 1 264 ? 14.769 19.792  34.967 1.000 10.95 ? 264  TRP A HZ3  1 
ATOM   3294 N  N    . SER A 1 265 ? 12.658 24.056  29.546 1.000 6.98  ? 265  SER A N    1 
ATOM   3295 C  CA   . SER A 1 265 ? 11.307 24.621  29.513 1.000 7.58  ? 265  SER A CA   1 
ATOM   3296 C  C    . SER A 1 265 ? 10.257 23.514  29.382 1.000 6.87  ? 265  SER A C    1 
ATOM   3297 O  O    . SER A 1 265 ? 9.241  23.497  30.075 1.000 7.81  ? 265  SER A O    1 
ATOM   3298 C  CB   A SER A 1 265 ? 11.157 25.601  28.347 0.692 8.29  ? 265  SER A CB   1 
ATOM   3299 C  CB   B SER A 1 265 ? 11.187 25.544  28.290 0.308 8.88  ? 265  SER A CB   1 
ATOM   3300 O  OG   A SER A 1 265 ? 11.933 26.772  28.519 0.692 9.13  ? 265  SER A OG   1 
ATOM   3301 O  OG   B SER A 1 265 ? 9.866  26.063  28.284 0.308 12.77 ? 265  SER A OG   1 
ATOM   3302 H  H    . SER A 1 265 ? 13.251 24.305  28.976 1.000 8.37  ? 265  SER A H    1 
ATOM   3303 H  HA   A SER A 1 265 ? 11.149 25.105  30.350 1.000 9.09  ? 265  SER A HA   1 
ATOM   3304 H  HB3  A SER A 1 265 ? 10.225 25.843  28.232 0.692 9.95  ? 265  SER A HB3  1 
ATOM   3305 N  N    . PHE A 1 266 ? 10.514 22.592  28.453 1.000 6.62  ? 266  PHE A N    1 
ATOM   3306 C  CA   . PHE A 1 266 ? 9.574  21.504  28.256 1.000 6.79  ? 266  PHE A CA   1 
ATOM   3307 C  C    . PHE A 1 266 ? 9.439  20.662  29.525 1.000 6.05  ? 266  PHE A C    1 
ATOM   3308 O  O    . PHE A 1 266 ? 8.329  20.321  29.935 1.000 6.79  ? 266  PHE A O    1 
ATOM   3309 C  CB   . PHE A 1 266 ? 10.108 20.596  27.094 1.000 6.43  ? 266  PHE A CB   1 
ATOM   3310 C  CG   . PHE A 1 266 ? 9.212  19.402  26.890 1.000 6.69  ? 266  PHE A CG   1 
ATOM   3311 C  CD1  . PHE A 1 266 ? 8.085  19.523  26.070 1.000 7.63  ? 266  PHE A CD1  1 
ATOM   3312 C  CD2  . PHE A 1 266 ? 9.443  18.193  27.534 1.000 7.68  ? 266  PHE A CD2  1 
ATOM   3313 C  CE1  . PHE A 1 266 ? 7.196  18.454  25.974 1.000 8.79  ? 266  PHE A CE1  1 
ATOM   3314 C  CE2  . PHE A 1 266 ? 8.541  17.154  27.432 1.000 8.22  ? 266  PHE A CE2  1 
ATOM   3315 C  CZ   . PHE A 1 266 ? 7.418  17.273  26.650 1.000 9.20  ? 266  PHE A CZ   1 
ATOM   3316 H  HB2  . PHE A 1 266 ? 10.150 21.112  26.274 1.000 7.72  ? 266  PHE A HB2  1 
ATOM   3317 H  HB3  . PHE A 1 266 ? 11.005 20.294  27.306 1.000 7.72  ? 266  PHE A HB3  1 
ATOM   3318 H  HD2  . PHE A 1 266 ? 10.216 18.083  28.039 1.000 9.22  ? 266  PHE A HD2  1 
ATOM   3319 H  HE1  . PHE A 1 266 ? 6.438  18.539  25.442 1.000 10.55 ? 266  PHE A HE1  1 
ATOM   3320 N  N    . LEU A 1 267 ? 10.563 20.260  30.119 1.000 6.23  ? 267  LEU A N    1 
ATOM   3321 C  CA   . LEU A 1 267 ? 10.503 19.387  31.275 1.000 6.19  ? 267  LEU A CA   1 
ATOM   3322 C  C    . LEU A 1 267 ? 9.875  20.041  32.484 1.000 6.09  ? 267  LEU A C    1 
ATOM   3323 O  O    . LEU A 1 267 ? 9.135  19.394  33.236 1.000 6.34  ? 267  LEU A O    1 
ATOM   3324 C  CB   . LEU A 1 267 ? 11.950 18.921  31.635 1.000 6.25  ? 267  LEU A CB   1 
ATOM   3325 C  CG   . LEU A 1 267 ? 12.571 17.942  30.648 1.000 6.58  ? 267  LEU A CG   1 
ATOM   3326 C  CD1  . LEU A 1 267 ? 14.026 17.743  30.993 1.000 7.36  ? 267  LEU A CD1  1 
ATOM   3327 C  CD2  . LEU A 1 267 ? 11.854 16.597  30.592 1.000 7.63  ? 267  LEU A CD2  1 
ATOM   3328 H  H    . LEU A 1 267 ? 11.326 20.518  29.816 1.000 7.47  ? 267  LEU A H    1 
ATOM   3329 H  HA   . LEU A 1 267 ? 9.973  18.597  31.039 1.000 7.43  ? 267  LEU A HA   1 
ATOM   3330 H  HB2  . LEU A 1 267 ? 12.521 19.703  31.694 1.000 7.51  ? 267  LEU A HB2  1 
ATOM   3331 H  HB3  . LEU A 1 267 ? 11.932 18.506  32.511 1.000 7.51  ? 267  LEU A HB3  1 
ATOM   3332 H  HG   . LEU A 1 267 ? 12.526 18.344  29.756 1.000 7.89  ? 267  LEU A HG   1 
ATOM   3333 H  HD11 . LEU A 1 267 ? 14.421 17.126  30.373 1.000 11.04 ? 267  LEU A HD11 1 
ATOM   3334 H  HD12 . LEU A 1 267 ? 14.485 18.585  30.943 1.000 11.04 ? 267  LEU A HD12 1 
ATOM   3335 H  HD13 . LEU A 1 267 ? 14.099 17.392  31.884 1.000 11.04 ? 267  LEU A HD13 1 
ATOM   3336 H  HD23 . LEU A 1 267 ? 11.922 16.174  31.452 1.000 11.45 ? 267  LEU A HD23 1 
ATOM   3337 N  N    . SER A 1 268 ? 10.178 21.313  32.708 1.000 6.28  ? 268  SER A N    1 
ATOM   3338 C  CA   A SER A 1 268 ? 9.602  22.059  33.787 0.628 6.17  ? 268  SER A CA   1 
ATOM   3339 C  CA   B SER A 1 268 ? 9.592  21.978  33.859 0.372 7.22  ? 268  SER A CA   1 
ATOM   3340 C  C    . SER A 1 268 ? 8.069  22.075  33.702 1.000 6.43  ? 268  SER A C    1 
ATOM   3341 O  O    . SER A 1 268 ? 7.362  21.849  34.683 1.000 7.86  ? 268  SER A O    1 
ATOM   3342 C  CB   A SER A 1 268 ? 10.168 23.465  33.833 0.628 7.60  ? 268  SER A CB   1 
ATOM   3343 C  CB   B SER A 1 268 ? 10.196 23.352  34.064 0.372 7.78  ? 268  SER A CB   1 
ATOM   3344 O  OG   A SER A 1 268 ? 9.627  24.188  34.913 0.628 12.49 ? 268  SER A OG   1 
ATOM   3345 O  OG   B SER A 1 268 ? 10.003 24.187  32.939 0.372 10.26 ? 268  SER A OG   1 
ATOM   3346 H  H    A SER A 1 268 ? 10.739 21.703  32.187 1.000 7.54  ? 268  SER A H    1 
ATOM   3347 H  HA   A SER A 1 268 ? 9.849  21.611  34.623 0.628 7.40  ? 268  SER A HA   1 
ATOM   3348 H  HB2  A SER A 1 268 ? 11.133 23.422  33.923 0.628 9.12  ? 268  SER A HB2  1 
ATOM   3349 H  HB2  B SER A 1 268 ? 9.791  23.765  34.842 0.372 9.33  ? 268  SER A HB2  1 
ATOM   3350 H  HB3  A SER A 1 268 ? 9.964  23.923  33.003 0.628 9.12  ? 268  SER A HB3  1 
ATOM   3351 H  HB3  B SER A 1 268 ? 11.146 23.261  34.234 0.372 9.33  ? 268  SER A HB3  1 
ATOM   3352 N  N    . LYS A 1 269 ? 7.577  22.345  32.505 1.000 6.82  ? 269  LYS A N    1 
ATOM   3353 C  CA   A LYS A 1 269 ? 6.124  22.355  32.281 0.523 7.73  ? 269  LYS A CA   1 
ATOM   3354 C  CA   B LYS A 1 269 ? 6.120  22.364  32.365 0.477 8.65  ? 269  LYS A CA   1 
ATOM   3355 C  C    . LYS A 1 269 ? 5.534  20.937  32.407 1.000 6.96  ? 269  LYS A C    1 
ATOM   3356 O  O    . LYS A 1 269 ? 4.489  20.733  33.013 1.000 8.13  ? 269  LYS A O    1 
ATOM   3357 C  CB   A LYS A 1 269 ? 5.840  23.030  30.937 0.523 9.04  ? 269  LYS A CB   1 
ATOM   3358 C  CB   B LYS A 1 269 ? 5.660  23.106  31.101 0.477 9.70  ? 269  LYS A CB   1 
ATOM   3359 C  CG   A LYS A 1 269 ? 4.373  23.225  30.541 0.523 11.07 ? 269  LYS A CG   1 
ATOM   3360 C  CG   B LYS A 1 269 ? 4.168  23.409  31.208 0.477 9.87  ? 269  LYS A CG   1 
ATOM   3361 C  CD   A LYS A 1 269 ? 3.686  24.051  31.607 0.523 11.82 ? 269  LYS A CD   1 
ATOM   3362 C  CD   B LYS A 1 269 ? 3.621  24.196  30.031 0.477 11.05 ? 269  LYS A CD   1 
ATOM   3363 C  CE   A LYS A 1 269 ? 2.405  24.757  31.123 0.523 10.85 ? 269  LYS A CE   1 
ATOM   3364 C  CE   B LYS A 1 269 ? 2.188  24.635  30.270 0.477 10.76 ? 269  LYS A CE   1 
ATOM   3365 N  NZ   A LYS A 1 269 ? 1.389  23.803  30.548 0.523 9.10  ? 269  LYS A NZ   1 
ATOM   3366 N  NZ   B LYS A 1 269 ? 1.216  23.510  30.238 0.477 15.45 ? 269  LYS A NZ   1 
ATOM   3367 H  HB2  A LYS A 1 269 ? 6.266  23.901  30.945 0.523 10.84 ? 269  LYS A HB2  1 
ATOM   3368 H  HB2  B LYS A 1 269 ? 6.158  23.933  31.005 0.477 11.64 ? 269  LYS A HB2  1 
ATOM   3369 H  HB3  A LYS A 1 269 ? 6.270  22.506  30.243 0.523 10.84 ? 269  LYS A HB3  1 
ATOM   3370 H  HB3  B LYS A 1 269 ? 5.828  22.557  30.318 0.477 11.64 ? 269  LYS A HB3  1 
ATOM   3371 N  N    . ALA A 1 270 ? 6.243  19.960  31.813 1.000 6.92  ? 270  ALA A N    1 
ATOM   3372 C  CA   . ALA A 1 270 ? 5.728  18.600  31.842 1.000 6.59  ? 270  ALA A CA   1 
ATOM   3373 C  C    . ALA A 1 270 ? 5.614  18.073  33.249 1.000 6.46  ? 270  ALA A C    1 
ATOM   3374 O  O    . ALA A 1 270 ? 4.636  17.384  33.567 1.000 6.98  ? 270  ALA A O    1 
ATOM   3375 C  CB   . ALA A 1 270 ? 6.639  17.683  31.001 1.000 7.25  ? 270  ALA A CB   1 
ATOM   3376 H  H    . ALA A 1 270 ? 6.988  20.137  31.422 1.000 8.30  ? 270  ALA A H    1 
ATOM   3377 H  HA   . ALA A 1 270 ? 4.835  18.599  31.439 1.000 7.90  ? 270  ALA A HA   1 
ATOM   3378 H  HB1  . ALA A 1 270 ? 6.288  16.790  31.028 1.000 10.88 ? 270  ALA A HB1  1 
ATOM   3379 H  HB2  . ALA A 1 270 ? 6.656  17.993  30.093 1.000 10.88 ? 270  ALA A HB2  1 
ATOM   3380 N  N    . GLN A 1 271 ? 6.595  18.343  34.128 1.000 6.33  ? 271  GLN A N    1 
ATOM   3381 C  CA   . GLN A 1 271 ? 6.494  17.831  35.487 1.000 6.31  ? 271  GLN A CA   1 
ATOM   3382 C  C    . GLN A 1 271 ? 5.470  18.596  36.312 1.000 6.83  ? 271  GLN A C    1 
ATOM   3383 O  O    . GLN A 1 271 ? 4.941  18.076  37.279 1.000 8.84  ? 271  GLN A O    1 
ATOM   3384 C  CB   . GLN A 1 271 ? 7.832  17.774  36.195 1.000 6.47  ? 271  GLN A CB   1 
ATOM   3385 C  CG   . GLN A 1 271 ? 8.406  19.139  36.555 1.000 6.27  ? 271  GLN A CG   1 
ATOM   3386 C  CD   . GLN A 1 271 ? 9.773  19.000  37.180 1.000 6.31  ? 271  GLN A CD   1 
ATOM   3387 O  OE1  . GLN A 1 271 ? 10.222 17.876  37.420 1.000 7.99  ? 271  GLN A OE1  1 
ATOM   3388 N  NE2  . GLN A 1 271 ? 10.432 20.096  37.460 1.000 7.18  ? 271  GLN A NE2  1 
ATOM   3389 H  H    . GLN A 1 271 ? 7.274  18.813  33.890 1.000 7.60  ? 271  GLN A H    1 
ATOM   3390 H  HA   . GLN A 1 271 ? 6.170  16.908  35.419 1.000 7.57  ? 271  GLN A HA   1 
ATOM   3391 H  HE21 . GLN A 1 271 ? 11.209 20.049  37.826 1.000 8.61  ? 271  GLN A HE21 1 
ATOM   3392 H  HE22 . GLN A 1 271 ? 10.088 20.863  37.279 1.000 8.61  ? 271  GLN A HE22 1 
ATOM   3393 N  N    . SER A 1 272 ? 5.215  19.854  35.939 1.000 7.39  ? 272  SER A N    1 
ATOM   3394 C  CA   . SER A 1 272 ? 4.119  20.590  36.575 1.000 8.32  ? 272  SER A CA   1 
ATOM   3395 C  C    . SER A 1 272 ? 2.760  19.996  36.232 1.000 7.55  ? 272  SER A C    1 
ATOM   3396 O  O    . SER A 1 272 ? 1.834  20.026  37.049 1.000 10.68 ? 272  SER A O    1 
ATOM   3397 C  CB   A SER A 1 272 ? 4.160  22.057  36.119 0.520 13.12 ? 272  SER A CB   1 
ATOM   3398 C  CB   B SER A 1 272 ? 4.194  22.061  36.151 0.306 10.20 ? 272  SER A CB   1 
ATOM   3399 C  CB   C SER A 1 272 ? 4.205  22.073  36.214 0.174 10.40 ? 272  SER A CB   1 
ATOM   3400 O  OG   A SER A 1 272 ? 5.243  22.752  36.695 0.520 14.14 ? 272  SER A OG   1 
ATOM   3401 O  OG   B SER A 1 272 ? 3.289  22.741  37.008 0.306 11.22 ? 272  SER A OG   1 
ATOM   3402 O  OG   C SER A 1 272 ? 3.769  22.330  34.895 0.174 10.48 ? 272  SER A OG   1 
ATOM   3403 H  H    . SER A 1 272 ? 5.691  20.229  35.329 1.000 8.87  ? 272  SER A H    1 
ATOM   3404 H  HA   A SER A 1 272 ? 4.240  20.558  37.547 1.000 9.98  ? 272  SER A HA   1 
ATOM   3405 N  N    . ASP A 1 273 ? 2.601  19.498  35.026 1.000 7.09  ? 273  ASP A N    1 
ATOM   3406 C  CA   . ASP A 1 273 ? 1.342  19.026  34.511 1.000 7.55  ? 273  ASP A CA   1 
ATOM   3407 C  C    . ASP A 1 273 ? 1.105  17.532  34.725 1.000 7.00  ? 273  ASP A C    1 
ATOM   3408 O  O    . ASP A 1 273 ? -0.046 17.105  34.840 1.000 8.40  ? 273  ASP A O    1 
ATOM   3409 C  CB   . ASP A 1 273 ? 1.191  19.365  33.046 1.000 8.21  ? 273  ASP A CB   1 
ATOM   3410 C  CG   . ASP A 1 273 ? 1.092  20.845  32.783 1.000 9.19  ? 273  ASP A CG   1 
ATOM   3411 O  OD1  . ASP A 1 273 ? 0.655  21.591  33.670 1.000 18.91 ? 273  ASP A OD1  1 
ATOM   3412 O  OD2  . ASP A 1 273 ? 1.446  21.293  31.722 1.000 9.88  ? 273  ASP A OD2  1 
ATOM   3413 H  H    . ASP A 1 273 ? 3.291  19.450  34.515 1.000 8.51  ? 273  ASP A H    1 
ATOM   3414 H  HA   . ASP A 1 273 ? 0.635  19.503  34.994 1.000 9.06  ? 273  ASP A HA   1 
ATOM   3415 H  HB3  . ASP A 1 273 ? 0.429  18.918  32.692 1.000 9.86  ? 273  ASP A HB3  1 
ATOM   3416 N  N    . PHE A 1 274 ? 2.192  16.725  34.714 1.000 6.34  ? 274  PHE A N    1 
ATOM   3417 C  CA   . PHE A 1 274 ? 2.174  15.303  34.683 1.000 6.19  ? 274  PHE A CA   1 
ATOM   3418 C  C    . PHE A 1 274 ? 3.008  14.671  35.775 1.000 6.43  ? 274  PHE A C    1 
ATOM   3419 O  O    . PHE A 1 274 ? 3.413  13.517  35.669 1.000 7.44  ? 274  PHE A O    1 
ATOM   3420 C  CB   . PHE A 1 274 ? 2.558  14.751  33.294 1.000 6.62  ? 274  PHE A CB   1 
ATOM   3421 C  CG   . PHE A 1 274 ? 1.681  15.319  32.200 1.000 7.05  ? 274  PHE A CG   1 
ATOM   3422 C  CD1  . PHE A 1 274 ? 0.334  14.951  32.110 1.000 8.08  ? 274  PHE A CD1  1 
ATOM   3423 C  CD2  . PHE A 1 274 ? 2.180  16.261  31.300 1.000 7.53  ? 274  PHE A CD2  1 
ATOM   3424 C  CE1  . PHE A 1 274 ? -0.514 15.489  31.158 1.000 9.17  ? 274  PHE A CE1  1 
ATOM   3425 C  CE2  . PHE A 1 274 ? 1.358  16.812  30.327 1.000 8.58  ? 274  PHE A CE2  1 
ATOM   3426 C  CZ   . PHE A 1 274 ? 0.034  16.458  30.261 1.000 9.03  ? 274  PHE A CZ   1 
ATOM   3427 H  H    . PHE A 1 274 ? 2.963  17.106  34.728 1.000 7.60  ? 274  PHE A H    1 
ATOM   3428 H  HA   . PHE A 1 274 ? 1.247  15.031  34.846 1.000 7.43  ? 274  PHE A HA   1 
ATOM   3429 H  HB2  . PHE A 1 274 ? 3.485  14.971  33.108 1.000 7.94  ? 274  PHE A HB2  1 
ATOM   3430 H  HB3  . PHE A 1 274 ? 2.476  13.785  33.301 1.000 7.94  ? 274  PHE A HB3  1 
ATOM   3431 H  HD1  . PHE A 1 274 ? -0.003 14.325  32.710 1.000 9.70  ? 274  PHE A HD1  1 
ATOM   3432 H  HD2  . PHE A 1 274 ? 3.071  16.523  31.353 1.000 9.03  ? 274  PHE A HD2  1 
ATOM   3433 H  HZ   . PHE A 1 274 ? -0.516 16.854  29.623 1.000 10.83 ? 274  PHE A HZ   1 
ATOM   3434 N  N    . GLY A 1 275 ? 3.287  15.446  36.810 1.000 6.76  ? 275  GLY A N    1 
ATOM   3435 C  CA   . GLY A 1 275 ? 4.097  14.985  37.943 1.000 6.60  ? 275  GLY A CA   1 
ATOM   3436 C  C    . GLY A 1 275 ? 3.257  14.195  38.924 1.000 6.40  ? 275  GLY A C    1 
ATOM   3437 O  O    . GLY A 1 275 ? 2.190  13.695  38.620 1.000 7.35  ? 275  GLY A O    1 
ATOM   3438 H  H    . GLY A 1 275 ? 2.983  16.250  36.819 1.000 8.11  ? 275  GLY A H    1 
ATOM   3439 H  HA2  . GLY A 1 275 ? 4.821  14.429  37.617 1.000 7.92  ? 275  GLY A HA2  1 
ATOM   3440 H  HA3  . GLY A 1 275 ? 4.485  15.751  38.395 1.000 7.92  ? 275  GLY A HA3  1 
ATOM   3441 N  N    . VAL A 1 276 ? 3.813  14.054  40.135 1.000 7.04  ? 276  VAL A N    1 
ATOM   3442 C  CA   . VAL A 1 276 ? 3.202  13.136  41.099 1.000 7.19  ? 276  VAL A CA   1 
ATOM   3443 C  C    . VAL A 1 276 ? 1.787  13.595  41.475 1.000 7.53  ? 276  VAL A C    1 
ATOM   3444 O  O    . VAL A 1 276 ? 0.992  12.736  41.853 1.000 9.81  ? 276  VAL A O    1 
ATOM   3445 C  CB   . VAL A 1 276 ? 4.111  12.974  42.347 1.000 7.86  ? 276  VAL A CB   1 
ATOM   3446 C  CG1  . VAL A 1 276 ? 5.424  12.338  41.984 1.000 8.62  ? 276  VAL A CG1  1 
ATOM   3447 C  CG2  . VAL A 1 276 ? 4.343  14.285  43.106 1.000 9.85  ? 276  VAL A CG2  1 
ATOM   3448 H  H    . VAL A 1 276 ? 4.520  14.497  40.344 1.000 8.45  ? 276  VAL A H    1 
ATOM   3449 H  HA   . VAL A 1 276 ? 3.127  12.258  40.669 1.000 8.63  ? 276  VAL A HA   1 
ATOM   3450 H  HB   . VAL A 1 276 ? 3.654  12.362  42.960 1.000 9.43  ? 276  VAL A HB   1 
ATOM   3451 H  HG11 . VAL A 1 276 ? 5.229  11.513  41.591 1.000 12.93 ? 276  VAL A HG11 1 
ATOM   3452 H  HG12 . VAL A 1 276 ? 5.895  12.886  41.376 1.000 12.93 ? 276  VAL A HG12 1 
ATOM   3453 H  HG21 . VAL A 1 276 ? 3.551  14.580  43.525 1.000 14.78 ? 276  VAL A HG21 1 
ATOM   3454 H  HG22 . VAL A 1 276 ? 5.021  14.182  43.757 1.000 14.78 ? 276  VAL A HG22 1 
ATOM   3455 N  N    . ASP A 1 277 ? 1.521  14.877  41.395 1.000 7.08  ? 277  ASP A N    1 
ATOM   3456 C  CA   . ASP A 1 277 ? 0.252  15.501  41.757 1.000 7.45  ? 277  ASP A CA   1 
ATOM   3457 C  C    . ASP A 1 277 ? -0.656 15.678  40.551 1.000 7.61  ? 277  ASP A C    1 
ATOM   3458 O  O    . ASP A 1 277 ? -1.646 16.446  40.639 1.000 8.81  ? 277  ASP A O    1 
ATOM   3459 C  CB   . ASP A 1 277 ? 0.475  16.830  42.454 1.000 7.43  ? 277  ASP A CB   1 
ATOM   3460 C  CG   . ASP A 1 277 ? 1.258  17.840  41.633 1.000 8.16  ? 277  ASP A CG   1 
ATOM   3461 O  OD1  . ASP A 1 277 ? 2.043  17.432  40.730 1.000 8.47  ? 277  ASP A OD1  1 
ATOM   3462 O  OD2  . ASP A 1 277 ? 1.078  19.033  41.899 1.000 15.81 ? 277  ASP A OD2  1 
ATOM   3463 H  HB2  . ASP A 1 277 ? -0.388 17.213  42.678 1.000 8.91  ? 277  ASP A HB2  1 
ATOM   3464 H  HB3  . ASP A 1 277 ? 0.950  16.670  43.285 1.000 8.91  ? 277  ASP A HB3  1 
ATOM   3465 N  N    . THR A 1 278 ? -0.382 14.997  39.432 1.000 7.62  ? 278  THR A N    1 
ATOM   3466 C  CA   . THR A 1 278 ? -1.181 15.231  38.219 1.000 7.56  ? 278  THR A CA   1 
ATOM   3467 C  C    . THR A 1 278 ? -2.630 14.804  38.385 1.000 7.73  ? 278  THR A C    1 
ATOM   3468 O  O    . THR A 1 278 ? -2.940 13.888  39.156 1.000 8.95  ? 278  THR A O    1 
ATOM   3469 C  CB   . THR A 1 278 ? -0.538 14.473  37.032 1.000 7.23  ? 278  THR A CB   1 
ATOM   3470 O  OG1  . THR A 1 278 ? -1.184 14.851  35.836 1.000 7.84  ? 278  THR A OG1  1 
ATOM   3471 C  CG2  . THR A 1 278 ? -0.587 12.979  37.123 1.000 8.26  ? 278  THR A CG2  1 
ATOM   3472 H  HB   . THR A 1 278 ? 0.402  14.744  36.971 1.000 8.67  ? 278  THR A HB   1 
ATOM   3473 H  HG21 . THR A 1 278 ? -0.156 12.696  37.933 1.000 12.38 ? 278  THR A HG21 1 
ATOM   3474 H  HG22 . THR A 1 278 ? -1.503 12.691  37.131 1.000 12.38 ? 278  THR A HG22 1 
ATOM   3475 N  N    . LYS A 1 279 ? -3.484 15.443  37.598 1.000 7.91  ? 279  LYS A N    1 
ATOM   3476 C  CA   A LYS A 1 279 ? -4.875 15.054  37.376 0.591 7.72  ? 279  LYS A CA   1 
ATOM   3477 C  CA   B LYS A 1 279 ? -4.864 14.916  37.492 0.409 9.62  ? 279  LYS A CA   1 
ATOM   3478 C  C    . LYS A 1 279 ? -5.002 14.089  36.213 1.000 7.70  ? 279  LYS A C    1 
ATOM   3479 O  O    . LYS A 1 279 ? -6.104 13.525  35.980 1.000 8.52  ? 279  LYS A O    1 
ATOM   3480 C  CB   A LYS A 1 279 ? -5.766 16.253  37.018 0.591 8.04  ? 279  LYS A CB   1 
ATOM   3481 C  CB   B LYS A 1 279 ? -5.846 16.082  37.586 0.409 12.65 ? 279  LYS A CB   1 
ATOM   3482 C  CG   A LYS A 1 279 ? -5.565 16.795  35.613 0.591 10.10 ? 279  LYS A CG   1 
ATOM   3483 C  CG   B LYS A 1 279 ? -5.777 16.998  36.380 0.409 16.15 ? 279  LYS A CG   1 
ATOM   3484 C  CD   A LYS A 1 279 ? -6.220 18.170  35.327 0.591 11.24 ? 279  LYS A CD   1 
ATOM   3485 C  CD   B LYS A 1 279 ? -6.530 18.293  36.577 0.409 19.95 ? 279  LYS A CD   1 
ATOM   3486 C  CE   A LYS A 1 279 ? -5.830 18.614  33.907 0.591 13.52 ? 279  LYS A CE   1 
ATOM   3487 C  CE   B LYS A 1 279 ? -7.123 18.829  35.287 0.409 19.28 ? 279  LYS A CE   1 
ATOM   3488 N  NZ   A LYS A 1 279 ? -6.176 20.035  33.603 0.591 13.20 ? 279  LYS A NZ   1 
ATOM   3489 N  NZ   B LYS A 1 279 ? -6.056 19.321  34.367 0.409 19.90 ? 279  LYS A NZ   1 
ATOM   3490 H  HA   A LYS A 1 279 ? -5.221 14.627  38.187 0.591 9.26  ? 279  LYS A HA   1 
ATOM   3491 N  N    . SER A 1 280 ? -3.928 13.911  35.422 1.000 7.52  ? 280  SER A N    1 
ATOM   3492 C  CA   . SER A 1 280 ? -3.974 13.095  34.232 1.000 8.23  ? 280  SER A CA   1 
ATOM   3493 C  C    . SER A 1 280 ? -3.849 11.621  34.523 1.000 8.11  ? 280  SER A C    1 
ATOM   3494 O  O    . SER A 1 280 ? -3.359 11.205  35.555 1.000 9.16  ? 280  SER A O    1 
ATOM   3495 C  CB   . SER A 1 280 ? -2.802 13.539  33.363 1.000 8.08  ? 280  SER A CB   1 
ATOM   3496 O  OG   . SER A 1 280 ? -2.799 12.883  32.100 1.000 8.95  ? 280  SER A OG   1 
ATOM   3497 H  HA   . SER A 1 280 ? -4.814 13.262  33.756 1.000 9.87  ? 280  SER A HA   1 
ATOM   3498 H  HB2  . SER A 1 280 ? -2.844 14.504  33.273 1.000 9.70  ? 280  SER A HB2  1 
ATOM   3499 N  N    . ASP A 1 281 ? -4.213 10.800  33.541 1.000 8.73  ? 281  ASP A N    1 
ATOM   3500 C  CA   . ASP A 1 281 ? -3.855 9.411   33.520 1.000 10.02 ? 281  ASP A CA   1 
ATOM   3501 C  C    . ASP A 1 281 ? -2.354 9.206   33.219 1.000 9.16  ? 281  ASP A C    1 
ATOM   3502 O  O    . ASP A 1 281 ? -1.800 8.178   33.529 1.000 11.87 ? 281  ASP A O    1 
ATOM   3503 C  CB   . ASP A 1 281 ? -4.651 8.629   32.486 1.000 12.93 ? 281  ASP A CB   1 
ATOM   3504 C  CG   . ASP A 1 281 ? -4.569 9.173   31.085 1.000 14.12 ? 281  ASP A CG   1 
ATOM   3505 O  OD1  . ASP A 1 281 ? -5.135 10.250  30.888 1.000 14.69 ? 281  ASP A OD1  1 
ATOM   3506 O  OD2  . ASP A 1 281 ? -3.924 8.519   30.230 1.000 21.27 ? 281  ASP A OD2  1 
ATOM   3507 H  H    . ASP A 1 281 ? -4.682 11.114  32.893 1.000 10.47 ? 281  ASP A H    1 
ATOM   3508 H  HB2  . ASP A 1 281 ? -4.334 7.729   32.468 1.000 15.51 ? 281  ASP A HB2  1 
ATOM   3509 N  N    . PHE A 1 282 ? -1.759 10.201  32.544 1.000 8.38  ? 282  PHE A N    1 
ATOM   3510 C  CA   . PHE A 1 282 ? -0.338 10.101  32.172 1.000 7.87  ? 282  PHE A CA   1 
ATOM   3511 C  C    . PHE A 1 282 ? 0.510  10.620  33.330 1.000 7.37  ? 282  PHE A C    1 
ATOM   3512 O  O    . PHE A 1 282 ? 0.324  11.740  33.781 1.000 8.23  ? 282  PHE A O    1 
ATOM   3513 C  CB   . PHE A 1 282 ? -0.087 10.940  30.910 1.000 7.94  ? 282  PHE A CB   1 
ATOM   3514 C  CG   . PHE A 1 282 ? 1.364  10.854  30.478 1.000 7.87  ? 282  PHE A CG   1 
ATOM   3515 C  CD1  . PHE A 1 282 ? 1.769  9.858   29.595 1.000 9.22  ? 282  PHE A CD1  1 
ATOM   3516 C  CD2  . PHE A 1 282 ? 2.307  11.753  30.981 1.000 8.52  ? 282  PHE A CD2  1 
ATOM   3517 C  CE1  . PHE A 1 282 ? 3.103  9.732   29.250 1.000 9.94  ? 282  PHE A CE1  1 
ATOM   3518 C  CE2  . PHE A 1 282 ? 3.631  11.575  30.659 1.000 9.31  ? 282  PHE A CE2  1 
ATOM   3519 C  CZ   . PHE A 1 282 ? 4.024  10.570  29.810 1.000 10.00 ? 282  PHE A CZ   1 
ATOM   3520 H  H    . PHE A 1 282 ? -2.210 10.900  32.327 1.000 10.05 ? 282  PHE A H    1 
ATOM   3521 H  HA   . PHE A 1 282 ? -0.111 9.165   31.993 1.000 9.45  ? 282  PHE A HA   1 
ATOM   3522 H  HB2  . PHE A 1 282 ? -0.656 10.621  30.192 1.000 9.53  ? 282  PHE A HB2  1 
ATOM   3523 H  HB3  . PHE A 1 282 ? -0.316 11.866  31.087 1.000 9.53  ? 282  PHE A HB3  1 
ATOM   3524 H  HE1  . PHE A 1 282 ? 3.370  9.081   28.641 1.000 11.92 ? 282  PHE A HE1  1 
ATOM   3525 H  HZ   . PHE A 1 282 ? 4.927  10.459  29.614 1.000 12.00 ? 282  PHE A HZ   1 
ATOM   3526 N  N    . HIS A 1 283 ? 1.494  9.793   33.698 1.000 7.25  ? 283  HIS A N    1 
ATOM   3527 C  CA   A HIS A 1 283 ? 2.461  10.160  34.693 0.569 7.37  ? 283  HIS A CA   1 
ATOM   3528 C  CA   B HIS A 1 283 ? 2.458  10.175  34.696 0.431 7.60  ? 283  HIS A CA   1 
ATOM   3529 C  C    . HIS A 1 283 ? 3.854  10.189  34.079 1.000 6.69  ? 283  HIS A C    1 
ATOM   3530 O  O    . HIS A 1 283 ? 4.336  9.216   33.545 1.000 7.46  ? 283  HIS A O    1 
ATOM   3531 C  CB   A HIS A 1 283 ? 2.426  9.138   35.835 0.569 9.14  ? 283  HIS A CB   1 
ATOM   3532 C  CB   B HIS A 1 283 ? 2.518  9.216   35.876 0.431 8.45  ? 283  HIS A CB   1 
ATOM   3533 C  CG   A HIS A 1 283 ? 1.053  9.108   36.441 0.569 11.40 ? 283  HIS A CG   1 
ATOM   3534 C  CG   B HIS A 1 283 ? 1.361  9.296   36.811 0.431 8.76  ? 283  HIS A CG   1 
ATOM   3535 N  ND1  A HIS A 1 283 ? -0.070 8.474   35.956 0.569 15.20 ? 283  HIS A ND1  1 
ATOM   3536 N  ND1  B HIS A 1 283 ? 1.462  9.499   38.168 0.431 10.38 ? 283  HIS A ND1  1 
ATOM   3537 C  CD2  A HIS A 1 283 ? 0.666  9.734   37.587 0.569 11.63 ? 283  HIS A CD2  1 
ATOM   3538 C  CD2  B HIS A 1 283 ? 0.043  9.188   36.541 0.431 12.24 ? 283  HIS A CD2  1 
ATOM   3539 C  CE1  A HIS A 1 283 ? -1.087 8.687   36.749 0.569 14.92 ? 283  HIS A CE1  1 
ATOM   3540 C  CE1  B HIS A 1 283 ? 0.266  9.502   38.689 0.431 11.27 ? 283  HIS A CE1  1 
ATOM   3541 N  NE2  A HIS A 1 283 ? -0.656 9.446   37.749 0.569 13.65 ? 283  HIS A NE2  1 
ATOM   3542 N  NE2  B HIS A 1 283 ? -0.624 9.322   37.732 0.431 11.13 ? 283  HIS A NE2  1 
ATOM   3543 H  HA   A HIS A 1 283 ? 2.244  11.048  35.045 0.569 8.84  ? 283  HIS A HA   1 
ATOM   3544 H  HA   B HIS A 1 283 ? 2.243  11.074  35.024 0.431 9.12  ? 283  HIS A HA   1 
ATOM   3545 H  HB2  A HIS A 1 283 ? 2.654  8.259   35.496 0.569 10.96 ? 283  HIS A HB2  1 
ATOM   3546 H  HB2  B HIS A 1 283 ? 2.576  8.310   35.534 0.431 10.13 ? 283  HIS A HB2  1 
ATOM   3547 H  HB3  A HIS A 1 283 ? 3.078  9.381   36.512 0.569 10.96 ? 283  HIS A HB3  1 
ATOM   3548 H  HB3  B HIS A 1 283 ? 3.331  9.392   36.376 0.431 10.13 ? 283  HIS A HB3  1 
ATOM   3549 N  N    . LEU A 1 284 ? 4.529  11.349  34.220 1.000 6.52  ? 284  LEU A N    1 
ATOM   3550 C  CA   . LEU A 1 284 ? 5.911  11.426  33.808 1.000 6.63  ? 284  LEU A CA   1 
ATOM   3551 C  C    . LEU A 1 284 ? 6.799  10.444  34.590 1.000 6.24  ? 284  LEU A C    1 
ATOM   3552 O  O    . LEU A 1 284 ? 7.740  9.885   34.014 1.000 6.94  ? 284  LEU A O    1 
ATOM   3553 C  CB   . LEU A 1 284 ? 6.384  12.866  33.971 1.000 7.42  ? 284  LEU A CB   1 
ATOM   3554 C  CG   . LEU A 1 284 ? 7.694  13.257  33.326 1.000 8.49  ? 284  LEU A CG   1 
ATOM   3555 C  CD1  . LEU A 1 284 ? 7.516  13.172  31.797 1.000 11.60 ? 284  LEU A CD1  1 
ATOM   3556 C  CD2  . LEU A 1 284 ? 8.063  14.685  33.697 1.000 9.47  ? 284  LEU A CD2  1 
ATOM   3557 H  HA   . LEU A 1 284 ? 5.961  11.193  32.858 1.000 7.96  ? 284  LEU A HA   1 
ATOM   3558 H  HB2  . LEU A 1 284 ? 5.693  13.447  33.616 1.000 8.90  ? 284  LEU A HB2  1 
ATOM   3559 H  HB3  . LEU A 1 284 ? 6.453  13.051  34.920 1.000 8.90  ? 284  LEU A HB3  1 
ATOM   3560 H  HD11 . LEU A 1 284 ? 7.820  12.326  31.532 1.000 17.40 ? 284  LEU A HD11 1 
ATOM   3561 H  HD22 . LEU A 1 284 ? 7.396  15.259  33.376 1.000 14.20 ? 284  LEU A HD22 1 
ATOM   3562 H  HD23 . LEU A 1 284 ? 8.065  14.735  34.640 1.000 14.20 ? 284  LEU A HD23 1 
ATOM   3563 N  N    . PHE A 1 285 ? 6.507  10.294  35.870 1.000 6.38  ? 285  PHE A N    1 
ATOM   3564 C  CA   . PHE A 1 285 ? 7.279  9.482   36.778 1.000 6.68  ? 285  PHE A CA   1 
ATOM   3565 C  C    . PHE A 1 285 ? 6.439  8.283   37.222 1.000 6.88  ? 285  PHE A C    1 
ATOM   3566 O  O    . PHE A 1 285 ? 5.503  8.396   38.038 1.000 8.96  ? 285  PHE A O    1 
ATOM   3567 C  CB   . PHE A 1 285 ? 7.718  10.279  38.002 1.000 7.59  ? 285  PHE A CB   1 
ATOM   3568 C  CG   . PHE A 1 285 ? 8.354  11.608  37.689 1.000 7.20  ? 285  PHE A CG   1 
ATOM   3569 C  CD1  . PHE A 1 285 ? 9.483  11.714  36.873 1.000 7.87  ? 285  PHE A CD1  1 
ATOM   3570 C  CD2  . PHE A 1 285 ? 7.819  12.774  38.180 1.000 7.21  ? 285  PHE A CD2  1 
ATOM   3571 C  CE1  . PHE A 1 285 ? 10.029 12.953  36.584 1.000 8.22  ? 285  PHE A CE1  1 
ATOM   3572 C  CE2  . PHE A 1 285 ? 8.387  14.013  37.896 1.000 7.70  ? 285  PHE A CE2  1 
ATOM   3573 C  CZ   . PHE A 1 285 ? 9.518  14.098  37.114 1.000 8.03  ? 285  PHE A CZ   1 
ATOM   3574 H  H    . PHE A 1 285 ? 5.817  10.705  36.180 1.000 7.66  ? 285  PHE A H    1 
ATOM   3575 H  HA   . PHE A 1 285 ? 8.076  9.155   36.311 1.000 8.02  ? 285  PHE A HA   1 
ATOM   3576 H  HB2  . PHE A 1 285 ? 6.986  10.405  38.593 1.000 9.11  ? 285  PHE A HB2  1 
ATOM   3577 H  HE1  . PHE A 1 285 ? 10.762 13.004  36.014 1.000 9.86  ? 285  PHE A HE1  1 
ATOM   3578 H  HE2  . PHE A 1 285 ? 8.001  14.788  38.237 1.000 9.24  ? 285  PHE A HE2  1 
ATOM   3579 N  N    . GLY A 1 286 ? 6.736  7.102   36.725 1.000 7.12  ? 286  GLY A N    1 
ATOM   3580 C  CA   . GLY A 1 286 ? 6.062  5.916   37.207 1.000 8.18  ? 286  GLY A CA   1 
ATOM   3581 C  C    . GLY A 1 286 ? 4.586  5.922   36.920 1.000 8.75  ? 286  GLY A C    1 
ATOM   3582 O  O    . GLY A 1 286 ? 4.188  6.112   35.768 1.000 10.21 ? 286  GLY A O    1 
ATOM   3583 H  H    . GLY A 1 286 ? 7.334  7.035   36.111 1.000 8.54  ? 286  GLY A H    1 
ATOM   3584 H  HA3  . GLY A 1 286 ? 6.209  5.796   38.141 1.000 9.81  ? 286  GLY A HA3  1 
ATOM   3585 N  N    . PRO A 1 287 ? 3.752  5.725   37.922 1.000 10.60 ? 287  PRO A N    1 
ATOM   3586 C  CA   . PRO A 1 287 ? 4.100  5.595   39.338 1.000 10.69 ? 287  PRO A CA   1 
ATOM   3587 C  C    . PRO A 1 287 ? 4.661  4.179   39.582 1.000 8.74  ? 287  PRO A C    1 
ATOM   3588 O  O    . PRO A 1 287 ? 4.473  3.255   38.812 1.000 10.36 ? 287  PRO A O    1 
ATOM   3589 C  CB   . PRO A 1 287 ? 2.794  5.792   40.105 1.000 15.15 ? 287  PRO A CB   1 
ATOM   3590 C  CG   . PRO A 1 287 ? 1.781  5.385   39.080 1.000 22.99 ? 287  PRO A CG   1 
ATOM   3591 C  CD   . PRO A 1 287 ? 2.276  5.645   37.688 1.000 14.11 ? 287  PRO A CD   1 
ATOM   3592 N  N    . PRO A 1 288 ? 5.352  4.040   40.706 1.000 9.75  ? 288  PRO A N    1 
ATOM   3593 C  CA   . PRO A 1 288 ? 5.872  2.748   41.065 1.000 11.82 ? 288  PRO A CA   1 
ATOM   3594 C  C    . PRO A 1 288 ? 4.734  1.790   41.384 1.000 12.08 ? 288  PRO A C    1 
ATOM   3595 O  O    . PRO A 1 288 ? 3.638  2.200   41.760 1.000 15.19 ? 288  PRO A O    1 
ATOM   3596 C  CB   . PRO A 1 288 ? 6.627  3.075   42.341 1.000 17.86 ? 288  PRO A CB   1 
ATOM   3597 C  CG   . PRO A 1 288 ? 6.110  4.404   42.841 1.000 19.47 ? 288  PRO A CG   1 
ATOM   3598 C  CD   . PRO A 1 288 ? 5.647  5.152   41.646 1.000 13.16 ? 288  PRO A CD   1 
ATOM   3599 N  N    . GLY A 1 289 ? 5.115  0.493   41.353 1.000 13.42 ? 289  GLY A N    1 
ATOM   3600 C  CA   . GLY A 1 289 ? 4.165  -0.501  41.828 1.000 17.64 ? 289  GLY A CA   1 
ATOM   3601 C  C    . GLY A 1 289 ? 4.350  -1.818  41.109 1.000 13.93 ? 289  GLY A C    1 
ATOM   3602 O  O    . GLY A 1 289 ? 5.064  -1.939  40.170 1.000 12.65 ? 289  GLY A O    1 
ATOM   3603 N  N    . LYS A 1 290 ? 3.679  -2.813  41.626 1.000 16.44 ? 290  LYS A N    1 
ATOM   3604 C  CA   . LYS A 1 290 ? 3.790  -4.198  41.145 1.000 15.63 ? 290  LYS A CA   1 
ATOM   3605 C  C    . LYS A 1 290 ? 3.240  -4.293  39.731 1.000 18.26 ? 290  LYS A C    1 
ATOM   3606 O  O    . LYS A 1 290 ? 2.079  -4.122  39.438 1.000 29.10 ? 290  LYS A O    1 
ATOM   3607 C  CB   . LYS A 1 290 ? 3.155  -5.118  42.167 1.000 20.29 ? 290  LYS A CB   1 
ATOM   3608 C  CG   . LYS A 1 290 ? 3.229  -6.582  41.902 1.000 18.70 ? 290  LYS A CG   1 
ATOM   3609 C  CD   . LYS A 1 290 ? 2.537  -7.296  43.072 1.000 20.44 ? 290  LYS A CD   1 
ATOM   3610 C  CE   . LYS A 1 290 ? 2.643  -8.796  42.882 1.000 28.72 ? 290  LYS A CE   1 
ATOM   3611 N  NZ   . LYS A 1 290 ? 2.056  -9.673  43.885 1.000 34.15 ? 290  LYS A NZ   1 
ATOM   3612 N  N    . LYS A 1 291 ? 4.071  -4.671  38.767 1.000 14.30 ? 291  LYS A N    1 
ATOM   3613 C  CA   A LYS A 1 291 ? 3.712  -4.942  37.395 0.562 16.48 ? 291  LYS A CA   1 
ATOM   3614 C  CA   B LYS A 1 291 ? 3.708  -4.912  37.385 0.438 14.42 ? 291  LYS A CA   1 
ATOM   3615 C  C    . LYS A 1 291 ? 4.963  -5.347  36.616 1.000 12.26 ? 291  LYS A C    1 
ATOM   3616 O  O    . LYS A 1 291 ? 6.090  -5.388  37.192 1.000 13.92 ? 291  LYS A O    1 
ATOM   3617 C  CB   A LYS A 1 291 ? 3.015  -3.713  36.835 0.562 17.66 ? 291  LYS A CB   1 
ATOM   3618 C  CB   B LYS A 1 291 ? 3.021  -3.721  36.736 0.438 16.16 ? 291  LYS A CB   1 
ATOM   3619 C  CG   A LYS A 1 291 ? 4.032  -2.538  36.832 0.562 21.46 ? 291  LYS A CG   1 
ATOM   3620 C  CG   B LYS A 1 291 ? 3.895  -2.467  36.662 0.438 17.49 ? 291  LYS A CG   1 
ATOM   3621 C  CD   A LYS A 1 291 ? 4.059  -2.122  35.361 0.562 23.59 ? 291  LYS A CD   1 
ATOM   3622 C  CD   B LYS A 1 291 ? 3.017  -1.276  36.245 0.438 20.80 ? 291  LYS A CD   1 
ATOM   3623 C  CE   A LYS A 1 291 ? 3.001  -1.063  35.166 0.562 23.92 ? 291  LYS A CE   1 
ATOM   3624 C  CE   B LYS A 1 291 ? 3.927  -0.065  36.134 0.438 25.40 ? 291  LYS A CE   1 
ATOM   3625 N  NZ   A LYS A 1 291 ? 2.064  -1.270  34.029 0.562 35.75 ? 291  LYS A NZ   1 
ATOM   3626 N  NZ   B LYS A 1 291 ? 3.107  1.093   35.751 0.438 32.59 ? 291  LYS A NZ   1 
ATOM   3627 N  N    . ASP A 1 292 ? 4.802  -5.720  35.346 1.000 13.92 ? 292  ASP A N    1 
ATOM   3628 C  CA   A ASP A 1 292 ? 5.966  -6.276  34.589 0.607 12.69 ? 292  ASP A CA   1 
ATOM   3629 C  CA   B ASP A 1 292 ? 5.906  -6.221  34.510 0.393 13.62 ? 292  ASP A CA   1 
ATOM   3630 C  C    . ASP A 1 292 ? 7.100  -5.270  34.457 1.000 11.47 ? 292  ASP A C    1 
ATOM   3631 O  O    . ASP A 1 292 ? 6.954  -4.093  34.130 1.000 13.34 ? 292  ASP A O    1 
ATOM   3632 C  CB   A ASP A 1 292 ? 5.639  -6.721  33.177 0.607 15.13 ? 292  ASP A CB   1 
ATOM   3633 C  CB   B ASP A 1 292 ? 5.375  -6.432  33.102 0.393 14.21 ? 292  ASP A CB   1 
ATOM   3634 C  CG   A ASP A 1 292 ? 6.695  -7.629  32.547 0.607 19.57 ? 292  ASP A CG   1 
ATOM   3635 C  CG   B ASP A 1 292 ? 6.300  -7.237  32.215 0.393 14.54 ? 292  ASP A CG   1 
ATOM   3636 O  OD1  A ASP A 1 292 ? 7.661  -7.206  31.870 0.607 20.63 ? 292  ASP A OD1  1 
ATOM   3637 O  OD1  B ASP A 1 292 ? 7.534  -7.209  32.377 0.393 10.50 ? 292  ASP A OD1  1 
ATOM   3638 O  OD2  A ASP A 1 292 ? 6.559  -8.869  32.697 0.607 25.26 ? 292  ASP A OD2  1 
ATOM   3639 O  OD2  B ASP A 1 292 ? 5.852  -7.960  31.292 0.393 22.56 ? 292  ASP A OD2  1 
ATOM   3640 N  N    . PRO A 1 293 ? 8.344  -5.732  34.738 1.000 10.96 ? 293  PRO A N    1 
ATOM   3641 C  CA   . PRO A 1 293 ? 9.441  -4.790  34.757 1.000 11.61 ? 293  PRO A CA   1 
ATOM   3642 C  C    . PRO A 1 293 ? 9.661  -4.115  33.397 1.000 10.13 ? 293  PRO A C    1 
ATOM   3643 O  O    . PRO A 1 293 ? 10.257 -3.005  33.434 1.000 10.46 ? 293  PRO A O    1 
ATOM   3644 C  CB   . PRO A 1 293 ? 10.583 -5.666  35.195 1.000 14.90 ? 293  PRO A CB   1 
ATOM   3645 C  CG   . PRO A 1 293 ? 10.240 -7.069  34.985 1.000 14.42 ? 293  PRO A CG   1 
ATOM   3646 C  CD   . PRO A 1 293 ? 8.746  -7.092  35.161 1.000 10.33 ? 293  PRO A CD   1 
ATOM   3647 H  HB2  . PRO A 1 293 ? 11.259 -5.553  34.519 1.000 17.88 ? 293  PRO A HB2  1 
ATOM   3648 H  HD2  . PRO A 1 293 ? 8.377  -7.758  34.588 1.000 12.40 ? 293  PRO A HD2  1 
ATOM   3649 N  N    . VAL A 1 294 ? 9.264  -4.659  32.251 1.000 11.62 ? 294  VAL A N    1 
ATOM   3650 C  CA   A VAL A 1 294 ? 9.544  -3.916  31.003 0.621 12.18 ? 294  VAL A CA   1 
ATOM   3651 C  CA   B VAL A 1 294 ? 9.405  -3.966  30.987 0.379 12.56 ? 294  VAL A CA   1 
ATOM   3652 C  C    . VAL A 1 294 ? 8.663  -2.641  30.945 1.000 11.08 ? 294  VAL A C    1 
ATOM   3653 O  O    . VAL A 1 294 ? 8.940  -1.798  30.077 1.000 11.57 ? 294  VAL A O    1 
ATOM   3654 C  CB   A VAL A 1 294 ? 9.421  -4.678  29.658 0.621 16.60 ? 294  VAL A CB   1 
ATOM   3655 C  CB   B VAL A 1 294 ? 8.887  -4.964  29.931 0.379 10.67 ? 294  VAL A CB   1 
ATOM   3656 C  CG1  A VAL A 1 294 ? 10.224 -5.982  29.759 0.621 19.36 ? 294  VAL A CG1  1 
ATOM   3657 C  CG1  B VAL A 1 294 ? 8.905  -4.352  28.567 0.379 15.06 ? 294  VAL A CG1  1 
ATOM   3658 C  CG2  A VAL A 1 294 ? 7.985  -4.968  29.302 0.621 21.82 ? 294  VAL A CG2  1 
ATOM   3659 C  CG2  B VAL A 1 294 ? 9.768  -6.206  29.985 0.379 13.48 ? 294  VAL A CG2  1 
ATOM   3660 H  H    A VAL A 1 294 ? 8.858  -5.417  32.236 1.000 13.94 ? 294  VAL A H    1 
ATOM   3661 N  N    . LEU A 1 295 ? 7.714  -2.473  31.838 1.000 10.34 ? 295  LEU A N    1 
ATOM   3662 C  CA   . LEU A 1 295 ? 6.901  -1.267  31.913 1.000 10.70 ? 295  LEU A CA   1 
ATOM   3663 C  C    . LEU A 1 295 ? 7.470  -0.217  32.838 1.000 7.85  ? 295  LEU A C    1 
ATOM   3664 O  O    . LEU A 1 295 ? 6.847  0.825   33.040 1.000 8.87  ? 295  LEU A O    1 
ATOM   3665 C  CB   . LEU A 1 295 ? 5.471  -1.646  32.424 1.000 14.94 ? 295  LEU A CB   1 
ATOM   3666 C  CG   . LEU A 1 295 ? 4.821  -2.724  31.587 1.000 22.81 ? 295  LEU A CG   1 
ATOM   3667 C  CD1  . LEU A 1 295 ? 3.520  -3.169  32.243 1.000 26.28 ? 295  LEU A CD1  1 
ATOM   3668 C  CD2  . LEU A 1 295 ? 4.578  -2.216  30.176 1.000 26.29 ? 295  LEU A CD2  1 
ATOM   3669 H  HA   . LEU A 1 295 ? 6.823  -0.884  31.014 1.000 12.84 ? 295  LEU A HA   1 
ATOM   3670 N  N    . LYS A 1 296 ? 8.608  -0.491  33.454 1.000 7.88  ? 296  LYS A N    1 
ATOM   3671 C  CA   . LYS A 1 296 ? 9.137  0.324   34.535 1.000 7.39  ? 296  LYS A CA   1 
ATOM   3672 C  C    . LYS A 1 296 ? 10.306 1.175   34.097 1.000 5.91  ? 296  LYS A C    1 
ATOM   3673 O  O    . LYS A 1 296 ? 11.095 0.825   33.216 1.000 6.47  ? 296  LYS A O    1 
ATOM   3674 C  CB   A LYS A 1 296 ? 9.488  -0.607  35.700 0.581 8.16  ? 296  LYS A CB   1 
ATOM   3675 C  CB   B LYS A 1 296 ? 9.671  -0.595  35.641 0.419 11.13 ? 296  LYS A CB   1 
ATOM   3676 C  CG   A LYS A 1 296 ? 8.156  -1.116  36.315 0.581 8.58  ? 296  LYS A CG   1 
ATOM   3677 C  CG   B LYS A 1 296 ? 8.660  -1.512  36.283 0.419 10.74 ? 296  LYS A CG   1 
ATOM   3678 C  CD   A LYS A 1 296 ? 8.498  -2.015  37.472 0.581 11.95 ? 296  LYS A CD   1 
ATOM   3679 C  CD   B LYS A 1 296 ? 7.561  -0.863  37.055 0.419 13.56 ? 296  LYS A CD   1 
ATOM   3680 C  CE   A LYS A 1 296 ? 7.296  -2.458  38.267 0.581 16.61 ? 296  LYS A CE   1 
ATOM   3681 C  CE   B LYS A 1 296 ? 7.057  -1.909  38.042 0.419 13.68 ? 296  LYS A CE   1 
ATOM   3682 N  NZ   A LYS A 1 296 ? 7.661  -2.283  39.704 0.581 22.06 ? 296  LYS A NZ   1 
ATOM   3683 N  NZ   B LYS A 1 296 ? 7.761  -2.027  39.341 0.419 13.63 ? 296  LYS A NZ   1 
ATOM   3684 H  H    . LYS A 1 296 ? 9.055  -1.182  33.204 1.000 9.46  ? 296  LYS A H    1 
ATOM   3685 H  HA   A LYS A 1 296 ? 8.424  0.925   34.835 1.000 8.87  ? 296  LYS A HA   1 
ATOM   3686 N  N    . ASP A 1 297 ? 10.412 2.325   34.781 1.000 5.54  ? 297  ASP A N    1 
ATOM   3687 C  CA   . ASP A 1 297 ? 11.505 3.261   34.607 1.000 5.38  ? 297  ASP A CA   1 
ATOM   3688 C  C    . ASP A 1 297 ? 11.578 3.785   33.174 1.000 5.02  ? 297  ASP A C    1 
ATOM   3689 O  O    . ASP A 1 297 ? 12.655 4.028   32.635 1.000 5.66  ? 297  ASP A O    1 
ATOM   3690 C  CB   . ASP A 1 297 ? 12.850 2.679   35.057 1.000 5.47  ? 297  ASP A CB   1 
ATOM   3691 C  CG   . ASP A 1 297 ? 12.868 2.285   36.526 1.000 5.32  ? 297  ASP A CG   1 
ATOM   3692 O  OD1  . ASP A 1 297 ? 12.178 2.920   37.351 1.000 5.99  ? 297  ASP A OD1  1 
ATOM   3693 O  OD2  . ASP A 1 297 ? 13.614 1.328   36.856 1.000 5.88  ? 297  ASP A OD2  1 
ATOM   3694 H  H    . ASP A 1 297 ? 9.798  2.517   35.352 1.000 6.65  ? 297  ASP A H    1 
ATOM   3695 H  HA   . ASP A 1 297 ? 11.318 4.030   35.185 1.000 6.46  ? 297  ASP A HA   1 
ATOM   3696 H  HB2  . ASP A 1 297 ? 13.051 1.898   34.518 1.000 6.57  ? 297  ASP A HB2  1 
ATOM   3697 H  HB3  . ASP A 1 297 ? 13.547 3.335   34.898 1.000 6.57  ? 297  ASP A HB3  1 
ATOM   3698 N  N    . LEU A 1 298 ? 10.418 3.983   32.563 1.000 5.54  ? 298  LEU A N    1 
ATOM   3699 C  CA   . LEU A 1 298 ? 10.361 4.449   31.199 1.000 5.14  ? 298  LEU A CA   1 
ATOM   3700 C  C    . LEU A 1 298 ? 10.574 5.953   31.142 1.000 4.91  ? 298  LEU A C    1 
ATOM   3701 O  O    . LEU A 1 298 ? 9.824  6.748   31.732 1.000 5.19  ? 298  LEU A O    1 
ATOM   3702 C  CB   . LEU A 1 298 ? 9.005  4.107   30.577 1.000 5.72  ? 298  LEU A CB   1 
ATOM   3703 C  CG   . LEU A 1 298 ? 8.651  2.628   30.575 1.000 6.49  ? 298  LEU A CG   1 
ATOM   3704 C  CD1  . LEU A 1 298 ? 7.304  2.457   29.905 1.000 8.16  ? 298  LEU A CD1  1 
ATOM   3705 C  CD2  . LEU A 1 298 ? 9.687  1.774   29.876 1.000 7.30  ? 298  LEU A CD2  1 
ATOM   3706 H  H    . LEU A 1 298 ? 9.686  3.831   32.988 1.000 6.65  ? 298  LEU A H    1 
ATOM   3707 H  HA   . LEU A 1 298 ? 11.068 4.007   30.682 1.000 6.17  ? 298  LEU A HA   1 
ATOM   3708 H  HB2  . LEU A 1 298 ? 8.315  4.588   31.061 1.000 6.87  ? 298  LEU A HB2  1 
ATOM   3709 H  HB3  . LEU A 1 298 ? 8.996  4.427   29.662 1.000 6.87  ? 298  LEU A HB3  1 
ATOM   3710 H  HG   . LEU A 1 298 ? 8.576  2.326   31.504 1.000 7.79  ? 298  LEU A HG   1 
ATOM   3711 H  HD12 . LEU A 1 298 ? 6.657  2.787   30.504 1.000 12.25 ? 298  LEU A HD12 1 
ATOM   3712 H  HD13 . LEU A 1 298 ? 7.245  2.932   29.103 1.000 12.25 ? 298  LEU A HD13 1 
ATOM   3713 H  HD22 . LEU A 1 298 ? 9.751  2.040   28.966 1.000 10.94 ? 298  LEU A HD22 1 
ATOM   3714 N  N    . LEU A 1 299 ? 11.641 6.372   30.432 1.000 5.25  ? 299  LEU A N    1 
ATOM   3715 C  CA   . LEU A 1 299 ? 12.067 7.773   30.239 1.000 5.25  ? 299  LEU A CA   1 
ATOM   3716 C  C    . LEU A 1 299 ? 12.775 8.338   31.469 1.000 4.87  ? 299  LEU A C    1 
ATOM   3717 O  O    . LEU A 1 299 ? 13.861 8.920   31.359 1.000 6.03  ? 299  LEU A O    1 
ATOM   3718 C  CB   . LEU A 1 299 ? 10.959 8.733   29.784 1.000 5.72  ? 299  LEU A CB   1 
ATOM   3719 C  CG   . LEU A 1 299 ? 10.201 8.274   28.545 1.000 6.53  ? 299  LEU A CG   1 
ATOM   3720 C  CD1  . LEU A 1 299 ? 9.116  9.319   28.240 1.000 7.55  ? 299  LEU A CD1  1 
ATOM   3721 C  CD2  . LEU A 1 299 ? 11.080 8.034   27.354 1.000 7.32  ? 299  LEU A CD2  1 
ATOM   3722 H  H    . LEU A 1 299 ? 12.120 5.765   30.055 1.000 6.30  ? 299  LEU A H    1 
ATOM   3723 H  HA   . LEU A 1 299 ? 12.733 7.762   29.520 1.000 6.30  ? 299  LEU A HA   1 
ATOM   3724 H  HB2  . LEU A 1 299 ? 10.327 8.845   30.511 1.000 6.87  ? 299  LEU A HB2  1 
ATOM   3725 H  HB3  . LEU A 1 299 ? 11.355 9.600   29.603 1.000 6.87  ? 299  LEU A HB3  1 
ATOM   3726 H  HG   . LEU A 1 299 ? 9.753  7.430   28.763 1.000 7.83  ? 299  LEU A HG   1 
ATOM   3727 H  HD12 . LEU A 1 299 ? 8.547  9.454   28.987 1.000 11.32 ? 299  LEU A HD12 1 
ATOM   3728 H  HD13 . LEU A 1 299 ? 9.560  10.129  28.049 1.000 11.32 ? 299  LEU A HD13 1 
ATOM   3729 H  HD21 . LEU A 1 299 ? 10.535 7.672   26.667 1.000 10.97 ? 299  LEU A HD21 1 
ATOM   3730 H  HD22 . LEU A 1 299 ? 11.423 8.857   27.084 1.000 10.97 ? 299  LEU A HD22 1 
ATOM   3731 N  N    . PHE A 1 300 ? 12.133 8.203   32.627 1.000 4.89  ? 300  PHE A N    1 
ATOM   3732 C  CA   . PHE A 1 300 ? 12.621 8.565   33.930 1.000 4.74  ? 300  PHE A CA   1 
ATOM   3733 C  C    . PHE A 1 300 ? 12.370 7.374   34.861 1.000 4.84  ? 300  PHE A C    1 
ATOM   3734 O  O    . PHE A 1 300 ? 11.481 6.557   34.586 1.000 5.39  ? 300  PHE A O    1 
ATOM   3735 C  CB   . PHE A 1 300 ? 11.879 9.793   34.491 1.000 5.24  ? 300  PHE A CB   1 
ATOM   3736 C  CG   . PHE A 1 300 ? 12.088 10.976  33.583 1.000 5.93  ? 300  PHE A CG   1 
ATOM   3737 C  CD1  . PHE A 1 300 ? 11.053 11.330  32.698 1.000 8.74  ? 300  PHE A CD1  1 
ATOM   3738 C  CD2  . PHE A 1 300 ? 13.285 11.665  33.593 1.000 8.17  ? 300  PHE A CD2  1 
ATOM   3739 C  CE1  . PHE A 1 300 ? 11.250 12.354  31.778 1.000 14.19 ? 300  PHE A CE1  1 
ATOM   3740 C  CE2  . PHE A 1 300 ? 13.491 12.692  32.682 1.000 13.29 ? 300  PHE A CE2  1 
ATOM   3741 C  CZ   . PHE A 1 300 ? 12.502 12.998  31.775 1.000 15.81 ? 300  PHE A CZ   1 
ATOM   3742 H  H    . PHE A 1 300 ? 11.343 7.864   32.592 1.000 5.86  ? 300  PHE A H    1 
ATOM   3743 H  HA   . PHE A 1 300 ? 13.582 8.752   33.883 1.000 5.69  ? 300  PHE A HA   1 
ATOM   3744 H  HB2  . PHE A 1 300 ? 10.931 9.598   34.561 1.000 6.28  ? 300  PHE A HB2  1 
ATOM   3745 H  HB3  . PHE A 1 300 ? 12.212 9.999   35.378 1.000 6.28  ? 300  PHE A HB3  1 
ATOM   3746 H  HE1  . PHE A 1 300 ? 10.578 12.605  31.186 1.000 17.03 ? 300  PHE A HE1  1 
ATOM   3747 N  N    . LYS A 1 301 ? 13.096 7.312   35.964 1.000 4.92  ? 301  LYS A N    1 
ATOM   3748 C  CA   . LYS A 1 301 ? 12.826 6.264   36.937 1.000 4.95  ? 301  LYS A CA   1 
ATOM   3749 C  C    . LYS A 1 301 ? 11.470 6.445   37.577 1.000 4.96  ? 301  LYS A C    1 
ATOM   3750 O  O    . LYS A 1 301 ? 11.015 7.560   37.891 1.000 5.48  ? 301  LYS A O    1 
ATOM   3751 C  CB   . LYS A 1 301 ? 13.957 6.241   37.968 1.000 4.99  ? 301  LYS A CB   1 
ATOM   3752 C  CG   . LYS A 1 301 ? 15.197 5.561   37.409 1.000 5.55  ? 301  LYS A CG   1 
ATOM   3753 C  CD   . LYS A 1 301 ? 16.489 5.865   38.172 1.000 5.20  ? 301  LYS A CD   1 
ATOM   3754 C  CE   . LYS A 1 301 ? 16.372 5.597   39.648 1.000 5.28  ? 301  LYS A CE   1 
ATOM   3755 N  NZ   . LYS A 1 301 ? 17.701 5.750   40.319 1.000 5.84  ? 301  LYS A NZ   1 
ATOM   3756 H  H    . LYS A 1 301 ? 13.721 7.886   36.105 1.000 5.91  ? 301  LYS A H    1 
ATOM   3757 H  HA   . LYS A 1 301 ? 12.827 5.405   36.466 1.000 5.94  ? 301  LYS A HA   1 
ATOM   3758 H  HB2  . LYS A 1 301 ? 14.177 7.149   38.226 1.000 5.99  ? 301  LYS A HB2  1 
ATOM   3759 H  HB3  . LYS A 1 301 ? 13.660 5.768   38.761 1.000 5.99  ? 301  LYS A HB3  1 
ATOM   3760 H  HG3  . LYS A 1 301 ? 15.337 5.871   36.503 1.000 6.66  ? 301  LYS A HG3  1 
ATOM   3761 H  HD2  . LYS A 1 301 ? 17.206 5.322   37.808 1.000 6.25  ? 301  LYS A HD2  1 
ATOM   3762 H  HD3  . LYS A 1 301 ? 16.724 6.796   38.037 1.000 6.25  ? 301  LYS A HD3  1 
ATOM   3763 H  HE2  . LYS A 1 301 ? 15.737 6.217   40.040 1.000 6.34  ? 301  LYS A HE2  1 
ATOM   3764 H  HE3  . LYS A 1 301 ? 16.040 4.697   39.788 1.000 6.34  ? 301  LYS A HE3  1 
ATOM   3765 H  HZ1  . LYS A 1 301 ? 17.614 5.589   41.190 1.000 8.77  ? 301  LYS A HZ1  1 
ATOM   3766 H  HZ2  . LYS A 1 301 ? 18.280 5.173   39.967 1.000 8.77  ? 301  LYS A HZ2  1 
ATOM   3767 H  HZ3  . LYS A 1 301 ? 18.000 6.580   40.200 1.000 8.77  ? 301  LYS A HZ3  1 
ATOM   3768 N  N    . ASP A 1 302 ? 10.829 5.309   37.881 1.000 5.01  ? 302  ASP A N    1 
ATOM   3769 C  CA   . ASP A 1 302 ? 9.536  5.310   38.558 1.000 5.66  ? 302  ASP A CA   1 
ATOM   3770 C  C    . ASP A 1 302 ? 9.625  5.928   39.961 1.000 5.73  ? 302  ASP A C    1 
ATOM   3771 O  O    . ASP A 1 302 ? 8.613  6.379   40.468 1.000 6.83  ? 302  ASP A O    1 
ATOM   3772 C  CB   . ASP A 1 302 ? 9.011  3.900   38.702 1.000 5.81  ? 302  ASP A CB   1 
ATOM   3773 C  CG   . ASP A 1 302 ? 8.518  3.256   37.421 1.000 6.12  ? 302  ASP A CG   1 
ATOM   3774 O  OD1  . ASP A 1 302 ? 8.567  3.867   36.352 1.000 6.50  ? 302  ASP A OD1  1 
ATOM   3775 O  OD2  . ASP A 1 302 ? 8.078  2.079   37.505 1.000 8.76  ? 302  ASP A OD2  1 
ATOM   3776 H  H    . ASP A 1 302 ? 11.190 4.557   37.671 1.000 6.01  ? 302  ASP A H    1 
ATOM   3777 H  HA   . ASP A 1 302 ? 8.900  5.830   38.023 1.000 6.80  ? 302  ASP A HA   1 
ATOM   3778 H  HB3  . ASP A 1 302 ? 8.253  3.905   39.298 1.000 6.98  ? 302  ASP A HB3  1 
ATOM   3779 N  N    . SER A 1 303 ? 10.810 5.858   40.569 1.000 5.40  ? 303  SER A N    1 
ATOM   3780 C  CA   . SER A 1 303 ? 11.069 6.409   41.893 1.000 5.68  ? 303  SER A CA   1 
ATOM   3781 C  C    . SER A 1 303 ? 11.348 7.924   41.861 1.000 5.14  ? 303  SER A C    1 
ATOM   3782 O  O    . SER A 1 303 ? 11.427 8.512   42.940 1.000 5.92  ? 303  SER A O    1 
ATOM   3783 C  CB   . SER A 1 303 ? 12.244 5.681   42.543 1.000 5.91  ? 303  SER A CB   1 
ATOM   3784 O  OG   . SER A 1 303 ? 13.417 5.737   41.737 1.000 6.31  ? 303  SER A OG   1 
ATOM   3785 H  H    . SER A 1 303 ? 11.456 5.467   40.158 1.000 6.48  ? 303  SER A H    1 
ATOM   3786 H  HA   . SER A 1 303 ? 10.274 6.258   42.446 1.000 6.82  ? 303  SER A HA   1 
ATOM   3787 H  HB2  . SER A 1 303 ? 12.431 6.083   43.406 1.000 7.09  ? 303  SER A HB2  1 
ATOM   3788 H  HB3  . SER A 1 303 ? 12.003 4.754   42.692 1.000 7.09  ? 303  SER A HB3  1 
ATOM   3789 N  N    . ALA A 1 304 ? 11.503 8.525   40.695 1.000 5.20  ? 304  ALA A N    1 
ATOM   3790 C  CA   . ALA A 1 304 ? 11.678 9.966   40.635 1.000 5.23  ? 304  ALA A CA   1 
ATOM   3791 C  C    . ALA A 1 304 ? 10.353 10.645  41.015 1.000 5.21  ? 304  ALA A C    1 
ATOM   3792 O  O    . ALA A 1 304 ? 9.256  10.142  40.722 1.000 5.78  ? 304  ALA A O    1 
ATOM   3793 C  CB   . ALA A 1 304 ? 12.112 10.395  39.261 1.000 5.75  ? 304  ALA A CB   1 
ATOM   3794 H  H    . ALA A 1 304 ? 11.501 8.062   39.971 1.000 6.24  ? 304  ALA A H    1 
ATOM   3795 H  HA   . ALA A 1 304 ? 12.365 10.229  41.281 1.000 6.28  ? 304  ALA A HA   1 
ATOM   3796 H  HB1  . ALA A 1 304 ? 12.221 11.349  39.244 1.000 8.63  ? 304  ALA A HB1  1 
ATOM   3797 H  HB2  . ALA A 1 304 ? 12.947 9.974   39.043 1.000 8.63  ? 304  ALA A HB2  1 
ATOM   3798 H  HB3  . ALA A 1 304 ? 11.446 10.138  38.620 1.000 8.63  ? 304  ALA A HB3  1 
ATOM   3799 N  N    . ILE A 1 305 ? 10.472 11.818  41.651 1.000 5.23  ? 305  ILE A N    1 
ATOM   3800 C  CA   . ILE A 1 305 ? 9.332  12.612  42.044 1.000 5.48  ? 305  ILE A CA   1 
ATOM   3801 C  C    . ILE A 1 305 ? 9.375  14.024  41.497 1.000 5.31  ? 305  ILE A C    1 
ATOM   3802 O  O    . ILE A 1 305 ? 8.412  14.785  41.686 1.000 5.93  ? 305  ILE A O    1 
ATOM   3803 C  CB   . ILE A 1 305 ? 9.140  12.589  43.588 1.000 5.90  ? 305  ILE A CB   1 
ATOM   3804 C  CG1  . ILE A 1 305 ? 10.313 13.262  44.290 1.000 6.14  ? 305  ILE A CG1  1 
ATOM   3805 C  CG2  . ILE A 1 305 ? 8.893  11.179  44.037 1.000 6.64  ? 305  ILE A CG2  1 
ATOM   3806 C  CD1  . ILE A 1 305 ? 10.179 13.346  45.803 1.000 7.40  ? 305  ILE A CD1  1 
ATOM   3807 H  H    . ILE A 1 305 ? 11.261 12.110  41.832 1.000 6.27  ? 305  ILE A H    1 
ATOM   3808 H  HA   . ILE A 1 305 ? 8.542  12.182  41.655 1.000 6.57  ? 305  ILE A HA   1 
ATOM   3809 H  HB   . ILE A 1 305 ? 8.335  13.109  43.793 1.000 7.09  ? 305  ILE A HB   1 
ATOM   3810 H  HG12 . ILE A 1 305 ? 11.123 12.772  44.077 1.000 7.37  ? 305  ILE A HG12 1 
ATOM   3811 H  HG13 . ILE A 1 305 ? 10.412 14.159  43.937 1.000 7.37  ? 305  ILE A HG13 1 
ATOM   3812 H  HG21 . ILE A 1 305 ? 8.145  10.817  43.558 1.000 9.96  ? 305  ILE A HG21 1 
ATOM   3813 H  HG22 . ILE A 1 305 ? 9.673  10.647  43.863 1.000 9.96  ? 305  ILE A HG22 1 
ATOM   3814 H  HG23 . ILE A 1 305 ? 8.705  11.172  44.979 1.000 9.96  ? 305  ILE A HG23 1 
ATOM   3815 H  HD12 . ILE A 1 305 ? 9.335  13.720  46.007 1.000 11.10 ? 305  ILE A HD12 1 
ATOM   3816 N  N    . MET A 1 306 ? 10.458 14.382  40.841 1.000 5.30  ? 306  MET A N    1 
ATOM   3817 C  CA   . MET A 1 306 ? 10.683 15.692  40.261 1.000 5.26  ? 306  MET A CA   1 
ATOM   3818 C  C    . MET A 1 306 ? 12.000 15.619  39.501 1.000 5.08  ? 306  MET A C    1 
ATOM   3819 O  O    . MET A 1 306 ? 12.772 14.671  39.681 1.000 5.53  ? 306  MET A O    1 
ATOM   3820 C  CB   . MET A 1 306 ? 10.747 16.793  41.360 1.000 5.54  ? 306  MET A CB   1 
ATOM   3821 C  CG   . MET A 1 306 ? 10.369 18.206  40.920 1.000 6.35  ? 306  MET A CG   1 
ATOM   3822 S  SD   . MET A 1 306 ? 8.639  18.348  40.374 1.000 8.29  ? 306  MET A SD   1 
ATOM   3823 C  CE   . MET A 1 306 ? 7.796  18.270  41.933 1.000 8.63  ? 306  MET A CE   1 
ATOM   3824 H  HA   . MET A 1 306 ? 9.958  15.899  39.635 1.000 6.31  ? 306  MET A HA   1 
ATOM   3825 H  HB2  . MET A 1 306 ? 10.158 16.533  42.085 1.000 6.65  ? 306  MET A HB2  1 
ATOM   3826 H  HB3  . MET A 1 306 ? 11.650 16.817  41.714 1.000 6.65  ? 306  MET A HB3  1 
ATOM   3827 H  HG2  . MET A 1 306 ? 10.517 18.816  41.659 1.000 7.63  ? 306  MET A HG2  1 
ATOM   3828 H  HG3  . MET A 1 306 ? 10.951 18.476  40.192 1.000 7.63  ? 306  MET A HG3  1 
ATOM   3829 H  HE1  . MET A 1 306 ? 6.906  18.524  41.784 1.000 12.94 ? 306  MET A HE1  1 
ATOM   3830 H  HE3  . MET A 1 306 ? 8.203  18.852  42.546 1.000 12.94 ? 306  MET A HE3  1 
ATOM   3831 N  N    . LEU A 1 307 ? 12.270 16.667  38.742 1.000 5.13  ? 307  LEU A N    1 
ATOM   3832 C  CA   . LEU A 1 307 ? 13.588 16.953  38.150 1.000 5.31  ? 307  LEU A CA   1 
ATOM   3833 C  C    . LEU A 1 307 ? 14.050 18.291  38.691 1.000 5.59  ? 307  LEU A C    1 
ATOM   3834 O  O    . LEU A 1 307 ? 13.230 19.240  38.812 1.000 7.18  ? 307  LEU A O    1 
ATOM   3835 C  CB   . LEU A 1 307 ? 13.489 17.038  36.630 1.000 6.22  ? 307  LEU A CB   1 
ATOM   3836 C  CG   . LEU A 1 307 ? 13.073 15.735  35.951 1.000 6.41  ? 307  LEU A CG   1 
ATOM   3837 C  CD1  . LEU A 1 307 ? 12.562 15.930  34.555 1.000 10.41 ? 307  LEU A CD1  1 
ATOM   3838 C  CD2  . LEU A 1 307 ? 14.224 14.754  35.913 1.000 12.57 ? 307  LEU A CD2  1 
ATOM   3839 H  H    . LEU A 1 307 ? 11.631 17.220  38.582 1.000 6.16  ? 307  LEU A H    1 
ATOM   3840 H  HA   . LEU A 1 307 ? 14.226 16.254  38.404 1.000 6.37  ? 307  LEU A HA   1 
ATOM   3841 H  HB3  . LEU A 1 307 ? 14.355 17.247  36.276 1.000 7.46  ? 307  LEU A HB3  1 
ATOM   3842 H  HG   . LEU A 1 307 ? 12.353 15.335  36.483 1.000 7.69  ? 307  LEU A HG   1 
ATOM   3843 H  HD11 . LEU A 1 307 ? 11.830 16.551  34.566 1.000 15.62 ? 307  LEU A HD11 1 
ATOM   3844 H  HD12 . LEU A 1 307 ? 13.266 16.274  34.002 1.000 15.62 ? 307  LEU A HD12 1 
ATOM   3845 H  HD13 . LEU A 1 307 ? 12.262 15.088  34.204 1.000 15.62 ? 307  LEU A HD13 1 
ATOM   3846 H  HD21 . LEU A 1 307 ? 14.718 14.980  35.141 1.000 18.85 ? 307  LEU A HD21 1 
ATOM   3847 H  HD22 . LEU A 1 307 ? 13.930 13.862  35.898 1.000 18.85 ? 307  LEU A HD22 1 
ATOM   3848 N  N    . LYS A 1 308 ? 15.347 18.405  38.947 1.000 5.69  ? 308  LYS A N    1 
ATOM   3849 C  CA   . LYS A 1 308 ? 15.973 19.631  39.471 1.000 6.03  ? 308  LYS A CA   1 
ATOM   3850 C  C    . LYS A 1 308 ? 17.036 20.057  38.477 1.000 5.57  ? 308  LYS A C    1 
ATOM   3851 O  O    . LYS A 1 308 ? 17.921 19.286  38.129 1.000 6.82  ? 308  LYS A O    1 
ATOM   3852 C  CB   A LYS A 1 308 ? 16.606 19.400  40.849 0.655 8.04  ? 308  LYS A CB   1 
ATOM   3853 C  CB   B LYS A 1 308 ? 16.493 19.439  40.884 0.345 4.98  ? 308  LYS A CB   1 
ATOM   3854 C  CG   A LYS A 1 308 ? 17.054 20.664  41.529 0.655 6.88  ? 308  LYS A CG   1 
ATOM   3855 C  CG   B LYS A 1 308 ? 16.898 20.745  41.530 0.345 7.91  ? 308  LYS A CG   1 
ATOM   3856 C  CD   A LYS A 1 308 ? 17.856 20.443  42.801 0.655 7.15  ? 308  LYS A CD   1 
ATOM   3857 C  CD   B LYS A 1 308 ? 16.830 20.620  43.054 0.345 9.79  ? 308  LYS A CD   1 
ATOM   3858 C  CE   A LYS A 1 308 ? 18.015 21.638  43.725 0.655 8.21  ? 308  LYS A CE   1 
ATOM   3859 C  CE   B LYS A 1 308 ? 17.880 19.668  43.560 0.345 9.83  ? 308  LYS A CE   1 
ATOM   3860 N  NZ   A LYS A 1 308 ? 18.730 22.810  43.083 0.655 8.16  ? 308  LYS A NZ   1 
ATOM   3861 N  NZ   B LYS A 1 308 ? 19.227 20.234  43.199 0.345 10.76 ? 308  LYS A NZ   1 
ATOM   3862 H  HA   A LYS A 1 308 ? 15.295 20.336  39.541 1.000 7.24  ? 308  LYS A HA   1 
ATOM   3863 H  HB2  A LYS A 1 308 ? 15.898 19.048  41.395 0.655 9.64  ? 308  LYS A HB2  1 
ATOM   3864 H  HB2  B LYS A 1 308 ? 15.780 19.101  41.432 0.345 5.97  ? 308  LYS A HB2  1 
ATOM   3865 H  HG2  A LYS A 1 308 ? 17.594 21.176  40.907 0.655 8.26  ? 308  LYS A HG2  1 
ATOM   3866 H  HG2  B LYS A 1 308 ? 17.801 20.976  41.262 0.345 9.49  ? 308  LYS A HG2  1 
ATOM   3867 H  HG3  A LYS A 1 308 ? 16.271 21.195  41.744 0.655 8.26  ? 308  LYS A HG3  1 
ATOM   3868 H  HG3  B LYS A 1 308 ? 16.304 21.453  41.235 0.345 9.49  ? 308  LYS A HG3  1 
ATOM   3869 H  HZ1  A LYS A 1 308 ? 18.793 23.476  43.670 0.655 12.24 ? 308  LYS A HZ1  1 
ATOM   3870 H  HZ2  A LYS A 1 308 ? 19.545 22.558  42.832 0.655 12.24 ? 308  LYS A HZ2  1 
ATOM   3871 H  HZ3  A LYS A 1 308 ? 18.271 23.083  42.371 0.655 12.24 ? 308  LYS A HZ3  1 
ATOM   3872 N  N    . ARG A 1 309 ? 16.963 21.303  38.001 1.000 6.16  ? 309  ARG A N    1 
ATOM   3873 C  CA   . ARG A 1 309 ? 17.908 21.770  36.977 1.000 6.59  ? 309  ARG A CA   1 
ATOM   3874 C  C    . ARG A 1 309 ? 19.298 21.776  37.554 1.000 7.13  ? 309  ARG A C    1 
ATOM   3875 O  O    . ARG A 1 309 ? 19.527 22.298  38.611 1.000 11.40 ? 309  ARG A O    1 
ATOM   3876 C  CB   A ARG A 1 309 ? 17.629 23.120  36.312 0.429 12.97 ? 309  ARG A CB   1 
ATOM   3877 C  CB   B ARG A 1 309 ? 17.387 23.135  36.479 0.571 7.42  ? 309  ARG A CB   1 
ATOM   3878 C  CG   A ARG A 1 309 ? 18.674 23.526  35.241 0.429 15.69 ? 309  ARG A CG   1 
ATOM   3879 C  CG   B ARG A 1 309 ? 18.131 23.502  35.195 0.571 10.08 ? 309  ARG A CG   1 
ATOM   3880 C  CD   A ARG A 1 309 ? 18.562 23.009  33.836 0.429 19.21 ? 309  ARG A CD   1 
ATOM   3881 C  CD   B ARG A 1 309 ? 17.709 24.781  34.503 0.571 9.93  ? 309  ARG A CD   1 
ATOM   3882 N  NE   A ARG A 1 309 ? 19.734 23.098  32.900 0.429 17.38 ? 309  ARG A NE   1 
ATOM   3883 N  NE   B ARG A 1 309 ? 18.544 24.905  33.307 0.571 13.46 ? 309  ARG A NE   1 
ATOM   3884 C  CZ   A ARG A 1 309 ? 19.957 24.296  32.367 0.429 19.94 ? 309  ARG A CZ   1 
ATOM   3885 C  CZ   B ARG A 1 309 ? 18.363 25.867  32.383 0.571 16.57 ? 309  ARG A CZ   1 
ATOM   3886 N  NH1  A ARG A 1 309 ? 19.118 25.274  32.703 0.429 31.80 ? 309  ARG A NH1  1 
ATOM   3887 N  NH1  B ARG A 1 309 ? 17.351 26.720  32.546 0.571 22.38 ? 309  ARG A NH1  1 
ATOM   3888 N  NH2  A ARG A 1 309 ? 20.944 24.542  31.511 0.429 26.94 ? 309  ARG A NH2  1 
ATOM   3889 N  NH2  B ARG A 1 309 ? 19.185 25.928  31.337 0.571 22.66 ? 309  ARG A NH2  1 
ATOM   3890 H  HA   A ARG A 1 309 ? 17.904 21.099  36.263 1.000 7.91  ? 309  ARG A HA   1 
ATOM   3891 H  HB2  A ARG A 1 309 ? 16.753 23.087  35.896 0.429 15.57 ? 309  ARG A HB2  1 
ATOM   3892 H  HB2  B ARG A 1 309 ? 16.434 23.083  36.307 0.571 8.90  ? 309  ARG A HB2  1 
ATOM   3893 H  HB3  A ARG A 1 309 ? 17.603 23.806  36.997 0.429 15.57 ? 309  ARG A HB3  1 
ATOM   3894 H  HB3  B ARG A 1 309 ? 17.539 23.815  37.155 0.571 8.90  ? 309  ARG A HB3  1 
ATOM   3895 N  N    . VAL A 1 310 ? 20.245 21.227  36.794 1.000 6.91  ? 310  VAL A N    1 
ATOM   3896 C  CA   . VAL A 1 310 ? 21.650 21.203  37.145 1.000 7.23  ? 310  VAL A CA   1 
ATOM   3897 C  C    . VAL A 1 310 ? 22.281 22.538  36.734 1.000 7.11  ? 310  VAL A C    1 
ATOM   3898 O  O    . VAL A 1 310 ? 22.026 23.012  35.636 1.000 8.84  ? 310  VAL A O    1 
ATOM   3899 C  CB   . VAL A 1 310 ? 22.344 19.992  36.455 1.000 7.85  ? 310  VAL A CB   1 
ATOM   3900 C  CG1  . VAL A 1 310 ? 23.842 20.035  36.620 1.000 7.96  ? 310  VAL A CG1  1 
ATOM   3901 C  CG2  . VAL A 1 310 ? 21.777 18.698  36.967 1.000 8.90  ? 310  VAL A CG2  1 
ATOM   3902 H  H    . VAL A 1 310 ? 20.008 20.866  36.051 1.000 8.30  ? 310  VAL A H    1 
ATOM   3903 H  HA   . VAL A 1 310 ? 21.731 21.101  38.117 1.000 8.68  ? 310  VAL A HA   1 
ATOM   3904 H  HB   . VAL A 1 310 ? 22.148 20.044  35.496 1.000 9.42  ? 310  VAL A HB   1 
ATOM   3905 H  HG11 . VAL A 1 310 ? 24.177 20.870  36.286 1.000 11.94 ? 310  VAL A HG11 1 
ATOM   3906 H  HG12 . VAL A 1 310 ? 24.064 19.950  37.550 1.000 11.94 ? 310  VAL A HG12 1 
ATOM   3907 H  HG13 . VAL A 1 310 ? 24.239 19.312  36.129 1.000 11.94 ? 310  VAL A HG13 1 
ATOM   3908 H  HG21 . VAL A 1 310 ? 20.924 18.586  36.585 1.000 13.35 ? 310  VAL A HG21 1 
ATOM   3909 H  HG23 . VAL A 1 310 ? 21.714 18.751  37.903 1.000 13.35 ? 310  VAL A HG23 1 
ATOM   3910 N  N    . PRO A 1 311 ? 23.090 23.170  37.564 1.000 7.41  ? 311  PRO A N    1 
ATOM   3911 C  CA   . PRO A 1 311 ? 23.749 24.396  37.149 1.000 8.10  ? 311  PRO A CA   1 
ATOM   3912 C  C    . PRO A 1 311 ? 24.599 24.164  35.882 1.000 7.45  ? 311  PRO A C    1 
ATOM   3913 O  O    . PRO A 1 311 ? 25.239 23.144  35.735 1.000 7.80  ? 311  PRO A O    1 
ATOM   3914 C  CB   . PRO A 1 311 ? 24.649 24.763  38.335 1.000 11.58 ? 311  PRO A CB   1 
ATOM   3915 C  CG   . PRO A 1 311 ? 23.976 24.096  39.503 1.000 14.35 ? 311  PRO A CG   1 
ATOM   3916 C  CD   . PRO A 1 311 ? 23.461 22.765  38.957 1.000 8.95  ? 311  PRO A CD   1 
ATOM   3917 H  HA   . PRO A 1 311 ? 23.088 25.102  36.991 1.000 9.73  ? 311  PRO A HA   1 
ATOM   3918 H  HB2  . PRO A 1 311 ? 25.548 24.422  38.210 1.000 13.90 ? 311  PRO A HB2  1 
ATOM   3919 H  HB3  . PRO A 1 311 ? 24.689 25.724  38.459 1.000 13.90 ? 311  PRO A HB3  1 
ATOM   3920 N  N    . SER A 1 312 ? 24.597 25.171  34.972 1.000 8.82  ? 312  SER A N    1 
ATOM   3921 C  CA   . SER A 1 312 ? 25.306 25.034  33.714 1.000 10.89 ? 312  SER A CA   1 
ATOM   3922 C  C    . SER A 1 312 ? 26.773 24.769  33.884 1.000 10.82 ? 312  SER A C    1 
ATOM   3923 O  O    . SER A 1 312 ? 27.394 24.136  33.036 1.000 14.70 ? 312  SER A O    1 
ATOM   3924 C  CB   A SER A 1 312 ? 25.107 26.247  32.795 0.329 13.71 ? 312  SER A CB   1 
ATOM   3925 C  CB   B SER A 1 312 ? 25.175 26.398  33.011 0.437 13.29 ? 312  SER A CB   1 
ATOM   3926 C  CB   C SER A 1 312 ? 25.136 26.310  32.869 0.234 12.72 ? 312  SER A CB   1 
ATOM   3927 O  OG   A SER A 1 312 ? 25.585 27.354  33.509 0.329 15.36 ? 312  SER A OG   1 
ATOM   3928 O  OG   B SER A 1 312 ? 25.576 26.339  31.668 0.437 13.22 ? 312  SER A OG   1 
ATOM   3929 O  OG   C SER A 1 312 ? 23.849 26.304  32.277 0.234 14.62 ? 312  SER A OG   1 
ATOM   3930 H  H    . SER A 1 312 ? 24.170 25.898  35.143 1.000 10.58 ? 312  SER A H    1 
ATOM   3931 H  HA   A SER A 1 312 ? 24.925 24.258  33.252 1.000 13.06 ? 312  SER A HA   1 
ATOM   3932 N  N    . LEU A 1 313 ? 27.324 25.283  34.988 1.000 10.05 ? 313  LEU A N    1 
ATOM   3933 C  CA   . LEU A 1 313 ? 28.764 25.112  35.150 1.000 10.93 ? 313  LEU A CA   1 
ATOM   3934 C  C    . LEU A 1 313 ? 29.079 23.681  35.563 1.000 12.45 ? 313  LEU A C    1 
ATOM   3935 O  O    . LEU A 1 313 ? 30.283 23.353  35.596 1.000 21.20 ? 313  LEU A O    1 
ATOM   3936 C  CB   . LEU A 1 313 ? 29.313 26.133  36.140 1.000 11.50 ? 313  LEU A CB   1 
ATOM   3937 C  CG   . LEU A 1 313 ? 28.749 26.103  37.558 1.000 13.94 ? 313  LEU A CG   1 
ATOM   3938 C  CD1  . LEU A 1 313 ? 29.281 25.036  38.486 1.000 16.51 ? 313  LEU A CD1  1 
ATOM   3939 C  CD2  . LEU A 1 313 ? 29.084 27.431  38.251 1.000 17.78 ? 313  LEU A CD2  1 
ATOM   3940 H  H    . LEU A 1 313 ? 26.852 25.696  35.576 1.000 12.06 ? 313  LEU A H    1 
ATOM   3941 H  HD22 . LEU A 1 313 ? 29.285 28.113  37.630 1.000 26.66 ? 313  LEU A HD22 1 
ATOM   3942 H  HD23 . LEU A 1 313 ? 28.465 27.681  38.928 1.000 26.66 ? 313  LEU A HD23 1 
ATOM   3943 N  N    . MET A 1 314 ? 28.156 22.815  35.930 1.000 8.51  ? 314  MET A N    1 
ATOM   3944 C  CA   A MET A 1 314 ? 28.486 21.423  36.209 0.684 9.31  ? 314  MET A CA   1 
ATOM   3945 C  CA   B MET A 1 314 ? 28.455 21.410  36.243 0.316 9.18  ? 314  MET A CA   1 
ATOM   3946 C  C    . MET A 1 314 ? 28.538 20.597  34.954 1.000 9.37  ? 314  MET A C    1 
ATOM   3947 O  O    . MET A 1 314 ? 27.591 20.532  34.194 1.000 15.14 ? 314  MET A O    1 
ATOM   3948 C  CB   A MET A 1 314 ? 27.511 20.633  37.041 0.684 11.14 ? 314  MET A CB   1 
ATOM   3949 C  CB   B MET A 1 314 ? 27.414 21.013  37.273 0.316 11.97 ? 314  MET A CB   1 
ATOM   3950 C  CG   A MET A 1 314 ? 27.532 21.046  38.499 0.684 15.18 ? 314  MET A CG   1 
ATOM   3951 C  CG   B MET A 1 314 ? 27.422 19.684  37.952 0.316 7.90  ? 314  MET A CG   1 
ATOM   3952 S  SD   A MET A 1 314 ? 26.412 20.000  39.482 0.684 15.52 ? 314  MET A SD   1 
ATOM   3953 S  SD   B MET A 1 314 ? 26.421 19.514  39.469 0.316 8.13  ? 314  MET A SD   1 
ATOM   3954 C  CE   A MET A 1 314 ? 27.540 19.571  40.818 0.684 13.66 ? 314  MET A CE   1 
ATOM   3955 C  CE   B MET A 1 314 ? 27.740 19.714  40.671 0.316 9.72  ? 314  MET A CE   1 
ATOM   3956 H  H    A MET A 1 314 ? 27.340 23.077  36.008 1.000 10.21 ? 314  MET A H    1 
ATOM   3957 H  HA   A MET A 1 314 ? 29.365 21.391  36.641 0.684 11.17 ? 314  MET A HA   1 
ATOM   3958 H  HA   B MET A 1 314 ? 29.334 21.378  36.675 0.316 11.02 ? 314  MET A HA   1 
ATOM   3959 H  HE1  A MET A 1 314 ? 27.141 19.019  41.476 0.684 20.49 ? 314  MET A HE1  1 
ATOM   3960 H  HE1  B MET A 1 314 ? 27.374 19.508  41.500 0.316 14.58 ? 314  MET A HE1  1 
ATOM   3961 N  N    . ASP A 1 315 ? 29.653 19.926  34.772 1.000 7.88  ? 315  ASP A N    1 
ATOM   3962 C  CA   . ASP A 1 315 ? 29.848 18.931  33.742 1.000 7.31  ? 315  ASP A CA   1 
ATOM   3963 C  C    . ASP A 1 315 ? 29.646 17.531  34.339 1.000 6.13  ? 315  ASP A C    1 
ATOM   3964 O  O    . ASP A 1 315 ? 29.280 17.359  35.496 1.000 6.58  ? 315  ASP A O    1 
ATOM   3965 C  CB   . ASP A 1 315 ? 31.236 19.095  33.061 1.000 7.55  ? 315  ASP A CB   1 
ATOM   3966 C  CG   . ASP A 1 315 ? 32.396 18.878  34.011 1.000 6.70  ? 315  ASP A CG   1 
ATOM   3967 O  OD1  . ASP A 1 315 ? 33.551 18.978  33.501 1.000 8.16  ? 315  ASP A OD1  1 
ATOM   3968 O  OD2  . ASP A 1 315 ? 32.169 18.613  35.198 1.000 7.46  ? 315  ASP A OD2  1 
ATOM   3969 H  H    . ASP A 1 315 ? 30.311 20.090  35.301 1.000 9.45  ? 315  ASP A H    1 
ATOM   3970 H  HA   . ASP A 1 315 ? 29.159 19.068  33.058 1.000 8.77  ? 315  ASP A HA   1 
ATOM   3971 H  HB3  . ASP A 1 315 ? 31.312 19.961  32.653 1.000 9.06  ? 315  ASP A HB3  1 
ATOM   3972 N  N    . SER A 1 316 ? 29.888 16.494  33.521 1.000 6.14  ? 316  SER A N    1 
ATOM   3973 C  CA   . SER A 1 316 ? 29.671 15.139  34.029 1.000 5.82  ? 316  SER A CA   1 
ATOM   3974 C  C    . SER A 1 316 ? 30.591 14.800  35.196 1.000 5.64  ? 316  SER A C    1 
ATOM   3975 O  O    . SER A 1 316 ? 30.165 14.122  36.136 1.000 6.00  ? 316  SER A O    1 
ATOM   3976 C  CB   . SER A 1 316 ? 29.816 14.110  32.910 1.000 6.31  ? 316  SER A CB   1 
ATOM   3977 O  OG   . SER A 1 316 ? 31.077 14.169  32.260 1.000 6.86  ? 316  SER A OG   1 
ATOM   3978 H  H    . SER A 1 316 ? 30.163 16.623  32.717 1.000 7.37  ? 316  SER A H    1 
ATOM   3979 H  HB2  . SER A 1 316 ? 29.693 13.222  33.280 1.000 7.57  ? 316  SER A HB2  1 
ATOM   3980 H  HB3  . SER A 1 316 ? 29.116 14.257  32.254 1.000 7.57  ? 316  SER A HB3  1 
ATOM   3981 H  HG   . SER A 1 316 ? 31.125 14.857  31.818 1.000 10.29 ? 316  SER A HG   1 
ATOM   3982 N  N    . GLN A 1 317 ? 31.843 15.266  35.149 1.000 5.72  ? 317  GLN A N    1 
ATOM   3983 C  CA   . GLN A 1 317 ? 32.765 14.954  36.249 1.000 5.43  ? 317  GLN A CA   1 
ATOM   3984 C  C    . GLN A 1 317 ? 32.342 15.621  37.563 1.000 5.87  ? 317  GLN A C    1 
ATOM   3985 O  O    . GLN A 1 317 ? 32.332 14.979  38.601 1.000 6.65  ? 317  GLN A O    1 
ATOM   3986 C  CB   . GLN A 1 317 ? 34.161 15.340  35.842 1.000 5.98  ? 317  GLN A CB   1 
ATOM   3987 C  CG   . GLN A 1 317 ? 35.218 15.104  36.907 1.000 6.70  ? 317  GLN A CG   1 
ATOM   3988 C  CD   . GLN A 1 317 ? 36.613 15.201  36.323 1.000 6.84  ? 317  GLN A CD   1 
ATOM   3989 O  OE1  . GLN A 1 317 ? 36.881 16.125  35.555 1.000 8.08  ? 317  GLN A OE1  1 
ATOM   3990 N  NE2  . GLN A 1 317 ? 37.515 14.288  36.687 1.000 7.41  ? 317  GLN A NE2  1 
ATOM   3991 H  H    . GLN A 1 317 ? 32.106 15.743  34.483 1.000 6.86  ? 317  GLN A H    1 
ATOM   3992 H  HA   . GLN A 1 317 ? 32.749 13.983  36.387 1.000 6.52  ? 317  GLN A HA   1 
ATOM   3993 H  HB2  . GLN A 1 317 ? 34.403 14.836  35.049 1.000 7.17  ? 317  GLN A HB2  1 
ATOM   3994 H  HB3  . GLN A 1 317 ? 34.165 16.280  35.605 1.000 7.17  ? 317  GLN A HB3  1 
ATOM   3995 H  HG2  . GLN A 1 317 ? 35.118 15.762  37.612 1.000 8.04  ? 317  GLN A HG2  1 
ATOM   3996 H  HG3  . GLN A 1 317 ? 35.093 14.225  37.297 1.000 8.04  ? 317  GLN A HG3  1 
ATOM   3997 N  N    . LEU A 1 318 ? 32.004 16.914  37.490 1.000 6.26  ? 318  LEU A N    1 
ATOM   3998 C  CA   . LEU A 1 318 ? 31.527 17.572  38.701 1.000 6.45  ? 318  LEU A CA   1 
ATOM   3999 C  C    . LEU A 1 318 ? 30.218 16.998  39.229 1.000 6.38  ? 318  LEU A C    1 
ATOM   4000 O  O    . LEU A 1 318 ? 30.002 16.910  40.427 1.000 7.29  ? 318  LEU A O    1 
ATOM   4001 C  CB   . LEU A 1 318 ? 31.360 19.068  38.447 1.000 8.24  ? 318  LEU A CB   1 
ATOM   4002 C  CG   . LEU A 1 318 ? 32.663 19.844  38.193 1.000 7.96  ? 318  LEU A CG   1 
ATOM   4003 C  CD1  . LEU A 1 318 ? 32.364 21.178  37.516 1.000 12.91 ? 318  LEU A CD1  1 
ATOM   4004 C  CD2  . LEU A 1 318 ? 33.403 20.044  39.507 1.000 15.91 ? 318  LEU A CD2  1 
ATOM   4005 H  HA   . LEU A 1 318 ? 32.209 17.458  39.395 1.000 7.74  ? 318  LEU A HA   1 
ATOM   4006 H  HG   . LEU A 1 318 ? 33.229 19.312  37.595 1.000 9.55  ? 318  LEU A HG   1 
ATOM   4007 N  N    . TYR A 1 319 ? 29.340 16.615  38.303 1.000 6.01  ? 319  TYR A N    1 
ATOM   4008 C  CA   . TYR A 1 319 ? 28.036 16.049  38.646 1.000 5.85  ? 319  TYR A CA   1 
ATOM   4009 C  C    . TYR A 1 319 ? 28.158 14.743  39.396 1.000 5.78  ? 319  TYR A C    1 
ATOM   4010 O  O    . TYR A 1 319 ? 27.544 14.495  40.418 1.000 6.88  ? 319  TYR A O    1 
ATOM   4011 C  CB   . TYR A 1 319 ? 27.187 15.923  37.336 1.000 6.28  ? 319  TYR A CB   1 
ATOM   4012 C  CG   . TYR A 1 319 ? 25.831 15.315  37.668 1.000 5.50  ? 319  TYR A CG   1 
ATOM   4013 C  CD1  . TYR A 1 319 ? 24.851 16.084  38.222 1.000 6.08  ? 319  TYR A CD1  1 
ATOM   4014 C  CD2  . TYR A 1 319 ? 25.602 13.951  37.501 1.000 5.85  ? 319  TYR A CD2  1 
ATOM   4015 C  CE1  . TYR A 1 319 ? 23.624 15.543  38.559 1.000 5.88  ? 319  TYR A CE1  1 
ATOM   4016 C  CE2  . TYR A 1 319 ? 24.378 13.405  37.872 1.000 5.61  ? 319  TYR A CE2  1 
ATOM   4017 C  CZ   . TYR A 1 319 ? 23.417 14.203  38.402 1.000 5.24  ? 319  TYR A CZ   1 
ATOM   4018 O  OH   . TYR A 1 319 ? 22.197 13.699  38.853 1.000 6.52  ? 319  TYR A OH   1 
ATOM   4019 H  H    . TYR A 1 319 ? 29.547 16.704  37.473 1.000 7.21  ? 319  TYR A H    1 
ATOM   4020 H  HA   . TYR A 1 319 ? 27.581 16.688  39.234 1.000 7.02  ? 319  TYR A HA   1 
ATOM   4021 H  HB2  . TYR A 1 319 ? 27.066 16.799  36.938 1.000 7.54  ? 319  TYR A HB2  1 
ATOM   4022 H  HB3  . TYR A 1 319 ? 27.652 15.360  36.697 1.000 7.54  ? 319  TYR A HB3  1 
ATOM   4023 H  HD1  . TYR A 1 319 ? 25.011 16.987  38.377 1.000 7.30  ? 319  TYR A HD1  1 
ATOM   4024 H  HD2  . TYR A 1 319 ? 26.265 13.407  37.143 1.000 7.02  ? 319  TYR A HD2  1 
ATOM   4025 H  HE2  . TYR A 1 319 ? 24.219 12.496  37.758 1.000 6.73  ? 319  TYR A HE2  1 
ATOM   4026 H  HH   . TYR A 1 319 ? 22.181 12.886  38.747 1.000 9.78  ? 319  TYR A HH   1 
ATOM   4027 N  N    . LEU A 1 320 ? 28.991 13.829  38.833 1.000 6.21  ? 320  LEU A N    1 
ATOM   4028 C  CA   . LEU A 1 320 ? 29.220 12.556  39.483 1.000 6.46  ? 320  LEU A CA   1 
ATOM   4029 C  C    . LEU A 1 320 ? 30.100 12.669  40.703 1.000 7.45  ? 320  LEU A C    1 
ATOM   4030 O  O    . LEU A 1 320 ? 30.049 11.810  41.587 1.000 8.94  ? 320  LEU A O    1 
ATOM   4031 C  CB   . LEU A 1 320 ? 29.832 11.571  38.473 1.000 6.34  ? 320  LEU A CB   1 
ATOM   4032 C  CG   . LEU A 1 320 ? 28.888 11.238  37.298 1.000 6.43  ? 320  LEU A CG   1 
ATOM   4033 C  CD1  . LEU A 1 320 ? 29.632 10.372  36.298 1.000 9.06  ? 320  LEU A CD1  1 
ATOM   4034 C  CD2  . LEU A 1 320 ? 27.619 10.556  37.717 1.000 7.64  ? 320  LEU A CD2  1 
ATOM   4035 H  H    . LEU A 1 320 ? 29.383 14.007  38.089 1.000 7.45  ? 320  LEU A H    1 
ATOM   4036 H  HA   . LEU A 1 320 ? 28.352 12.199  39.767 1.000 7.75  ? 320  LEU A HA   1 
ATOM   4037 H  HB3  . LEU A 1 320 ? 30.064 10.750  38.936 1.000 7.61  ? 320  LEU A HB3  1 
ATOM   4038 H  HG   . LEU A 1 320 ? 28.648 12.078  36.854 1.000 7.72  ? 320  LEU A HG   1 
ATOM   4039 H  HD11 . LEU A 1 320 ? 30.443 10.814  36.034 1.000 13.58 ? 320  LEU A HD11 1 
ATOM   4040 H  HD12 . LEU A 1 320 ? 29.845 9.528   36.701 1.000 13.58 ? 320  LEU A HD12 1 
ATOM   4041 H  HD13 . LEU A 1 320 ? 29.080 10.229  35.526 1.000 13.58 ? 320  LEU A HD13 1 
ATOM   4042 H  HD21 . LEU A 1 320 ? 27.158 11.102  38.358 1.000 11.46 ? 320  LEU A HD21 1 
ATOM   4043 H  HD23 . LEU A 1 320 ? 27.839 9.711   38.115 1.000 11.46 ? 320  LEU A HD23 1 
ATOM   4044 N  N    . GLY A 1 321 ? 30.904 13.717  40.725 1.000 7.21  ? 321  GLY A N    1 
ATOM   4045 C  CA   . GLY A 1 321 ? 31.891 13.985  41.756 1.000 8.07  ? 321  GLY A CA   1 
ATOM   4046 C  C    . GLY A 1 321 ? 33.196 13.296  41.401 1.000 7.45  ? 321  GLY A C    1 
ATOM   4047 O  O    . GLY A 1 321 ? 33.230 12.268  40.751 1.000 7.53  ? 321  GLY A O    1 
ATOM   4048 H  H    . GLY A 1 321 ? 30.838 14.282  40.081 1.000 8.65  ? 321  GLY A H    1 
ATOM   4049 H  HA2  . GLY A 1 321 ? 32.035 14.941  41.831 1.000 9.69  ? 321  GLY A HA2  1 
ATOM   4050 H  HA3  . GLY A 1 321 ? 31.570 13.658  42.611 1.000 9.69  ? 321  GLY A HA3  1 
ATOM   4051 N  N    . PHE A 1 322 ? 34.283 13.910  41.849 1.000 8.25  ? 322  PHE A N    1 
ATOM   4052 C  CA   . PHE A 1 322 ? 35.600 13.413  41.467 1.000 8.35  ? 322  PHE A CA   1 
ATOM   4053 C  C    . PHE A 1 322 ? 35.821 11.984  41.954 1.000 8.93  ? 322  PHE A C    1 
ATOM   4054 O  O    . PHE A 1 322 ? 36.488 11.232  41.223 1.000 9.45  ? 322  PHE A O    1 
ATOM   4055 C  CB   . PHE A 1 322 ? 36.711 14.350  41.994 1.000 9.40  ? 322  PHE A CB   1 
ATOM   4056 C  CG   . PHE A 1 322 ? 36.734 15.686  41.322 1.000 8.71  ? 322  PHE A CG   1 
ATOM   4057 C  CD1  . PHE A 1 322 ? 37.263 15.806  40.028 1.000 8.92  ? 322  PHE A CD1  1 
ATOM   4058 C  CD2  . PHE A 1 322 ? 36.261 16.824  41.908 1.000 11.24 ? 322  PHE A CD2  1 
ATOM   4059 C  CE1  . PHE A 1 322 ? 37.303 17.021  39.369 1.000 9.98  ? 322  PHE A CE1  1 
ATOM   4060 C  CE2  . PHE A 1 322 ? 36.252 18.036  41.251 1.000 12.37 ? 322  PHE A CE2  1 
ATOM   4061 C  CZ   . PHE A 1 322 ? 36.767 18.176  39.942 1.000 12.05 ? 322  PHE A CZ   1 
ATOM   4062 H  H    . PHE A 1 322 ? 34.211 14.597  42.361 1.000 9.90  ? 322  PHE A H    1 
ATOM   4063 H  HA   . PHE A 1 322 ? 35.649 13.409  40.488 1.000 10.02 ? 322  PHE A HA   1 
ATOM   4064 H  HD1  . PHE A 1 322 ? 37.595 15.049  39.603 1.000 10.71 ? 322  PHE A HD1  1 
ATOM   4065 H  HD2  . PHE A 1 322 ? 35.934 16.780  42.777 1.000 13.49 ? 322  PHE A HD2  1 
ATOM   4066 H  HE2  . PHE A 1 322 ? 35.898 18.781  41.681 1.000 14.85 ? 322  PHE A HE2  1 
ATOM   4067 N  N    . GLU A 1 323 ? 35.327 11.614  43.127 1.000 9.76  ? 323  GLU A N    1 
ATOM   4068 C  CA   . GLU A 1 323 ? 35.617 10.304  43.638 1.000 12.13 ? 323  GLU A CA   1 
ATOM   4069 C  C    . GLU A 1 323 ? 34.961 9.235   42.770 1.000 10.58 ? 323  GLU A C    1 
ATOM   4070 O  O    . GLU A 1 323 ? 35.600 8.253   42.361 1.000 11.73 ? 323  GLU A O    1 
ATOM   4071 C  CB   A GLU A 1 323 ? 35.169 10.081  45.096 0.518 12.97 ? 323  GLU A CB   1 
ATOM   4072 C  CB   B GLU A 1 323 ? 35.145 10.274  45.110 0.482 13.53 ? 323  GLU A CB   1 
ATOM   4073 C  CG   A GLU A 1 323 ? 35.647 8.744   45.655 0.518 16.25 ? 323  GLU A CG   1 
ATOM   4074 C  CG   B GLU A 1 323 ? 36.296 10.614  45.986 0.482 20.21 ? 323  GLU A CG   1 
ATOM   4075 C  CD   A GLU A 1 323 ? 35.368 8.573   47.152 0.518 21.44 ? 323  GLU A CD   1 
ATOM   4076 C  CD   B GLU A 1 323 ? 36.582 11.597  47.026 0.482 28.89 ? 323  GLU A CD   1 
ATOM   4077 O  OE1  A GLU A 1 323 ? 35.250 7.429   47.604 0.518 35.67 ? 323  GLU A OE1  1 
ATOM   4078 O  OE1  B GLU A 1 323 ? 35.878 11.704  48.082 0.482 30.39 ? 323  GLU A OE1  1 
ATOM   4079 O  OE2  A GLU A 1 323 ? 35.265 9.627   47.796 0.518 36.56 ? 323  GLU A OE2  1 
ATOM   4080 O  OE2  B GLU A 1 323 ? 37.598 12.364  46.859 0.482 26.69 ? 323  GLU A OE2  1 
ATOM   4081 H  HA   A GLU A 1 323 ? 36.588 10.172  43.597 1.000 14.56 ? 323  GLU A HA   1 
ATOM   4082 N  N    . TYR A 1 324 ? 33.664 9.303   42.522 1.000 9.52  ? 324  TYR A N    1 
ATOM   4083 C  CA   . TYR A 1 324 ? 33.039 8.268   41.673 1.000 8.96  ? 324  TYR A CA   1 
ATOM   4084 C  C    . TYR A 1 324 ? 33.534 8.323   40.272 1.000 7.96  ? 324  TYR A C    1 
ATOM   4085 O  O    . TYR A 1 324 ? 33.732 7.286   39.619 1.000 8.71  ? 324  TYR A O    1 
ATOM   4086 C  CB   . TYR A 1 324 ? 31.498 8.430   41.777 1.000 9.10  ? 324  TYR A CB   1 
ATOM   4087 C  CG   . TYR A 1 324 ? 30.711 7.402   40.983 1.000 8.36  ? 324  TYR A CG   1 
ATOM   4088 C  CD1  . TYR A 1 324 ? 31.034 6.047   40.987 1.000 9.42  ? 324  TYR A CD1  1 
ATOM   4089 C  CD2  . TYR A 1 324 ? 29.593 7.777   40.251 1.000 9.41  ? 324  TYR A CD2  1 
ATOM   4090 C  CE1  . TYR A 1 324 ? 30.269 5.153   40.265 1.000 9.60  ? 324  TYR A CE1  1 
ATOM   4091 C  CE2  . TYR A 1 324 ? 28.851 6.885   39.527 1.000 9.34  ? 324  TYR A CE2  1 
ATOM   4092 C  CZ   . TYR A 1 324 ? 29.167 5.582   39.549 1.000 8.63  ? 324  TYR A CZ   1 
ATOM   4093 O  OH   . TYR A 1 324 ? 28.496 4.598   38.797 1.000 9.97  ? 324  TYR A OH   1 
ATOM   4094 H  HA   . TYR A 1 324 ? 33.275 7.392   42.043 1.000 10.75 ? 324  TYR A HA   1 
ATOM   4095 H  HB3  . TYR A 1 324 ? 31.233 9.290   41.462 1.000 10.92 ? 324  TYR A HB3  1 
ATOM   4096 H  HD1  . TYR A 1 324 ? 31.765 5.744   41.476 1.000 11.30 ? 324  TYR A HD1  1 
ATOM   4097 H  HE1  . TYR A 1 324 ? 30.497 4.251   40.260 1.000 11.52 ? 324  TYR A HE1  1 
ATOM   4098 N  N    . TYR A 1 325 ? 33.785 9.539   39.745 1.000 7.64  ? 325  TYR A N    1 
ATOM   4099 C  CA   . TYR A 1 325 ? 34.301 9.656   38.391 1.000 7.45  ? 325  TYR A CA   1 
ATOM   4100 C  C    . TYR A 1 325 ? 35.629 8.885   38.275 1.000 8.28  ? 325  TYR A C    1 
ATOM   4101 O  O    . TYR A 1 325 ? 35.850 8.165   37.309 1.000 8.94  ? 325  TYR A O    1 
ATOM   4102 C  CB   . TYR A 1 325 ? 34.434 11.145  38.031 1.000 7.45  ? 325  TYR A CB   1 
ATOM   4103 C  CG   . TYR A 1 325 ? 34.598 11.381  36.551 1.000 6.52  ? 325  TYR A CG   1 
ATOM   4104 C  CD1  . TYR A 1 325 ? 33.467 11.592  35.773 1.000 6.40  ? 325  TYR A CD1  1 
ATOM   4105 C  CD2  . TYR A 1 325 ? 35.825 11.426  35.902 1.000 7.23  ? 325  TYR A CD2  1 
ATOM   4106 C  CE1  . TYR A 1 325 ? 33.545 11.839  34.403 1.000 6.09  ? 325  TYR A CE1  1 
ATOM   4107 C  CE2  . TYR A 1 325 ? 35.918 11.640  34.544 1.000 6.99  ? 325  TYR A CE2  1 
ATOM   4108 C  CZ   . TYR A 1 325 ? 34.783 11.841  33.782 1.000 6.32  ? 325  TYR A CZ   1 
ATOM   4109 O  OH   . TYR A 1 325 ? 34.910 12.045  32.445 1.000 7.21  ? 325  TYR A OH   1 
ATOM   4110 H  H    . TYR A 1 325 ? 33.640 10.247  40.211 1.000 9.17  ? 325  TYR A H    1 
ATOM   4111 H  HB2  . TYR A 1 325 ? 33.674 11.620  38.308 1.000 8.94  ? 325  TYR A HB2  1 
ATOM   4112 H  HD1  . TYR A 1 325 ? 32.631 11.567  36.179 1.000 7.68  ? 325  TYR A HD1  1 
ATOM   4113 H  HD2  . TYR A 1 325 ? 36.604 11.308  36.397 1.000 8.68  ? 325  TYR A HD2  1 
ATOM   4114 H  HE1  . TYR A 1 325 ? 32.773 12.002  33.910 1.000 7.31  ? 325  TYR A HE1  1 
ATOM   4115 H  HE2  . TYR A 1 325 ? 36.754 11.649  34.136 1.000 8.39  ? 325  TYR A HE2  1 
ATOM   4116 N  N    . SER A 1 326 ? 36.480 9.051   39.292 1.000 9.07  ? 326  SER A N    1 
ATOM   4117 C  CA   . SER A 1 326 ? 37.790 8.360   39.261 1.000 10.77 ? 326  SER A CA   1 
ATOM   4118 C  C    . SER A 1 326 ? 37.606 6.843   39.425 1.000 11.63 ? 326  SER A C    1 
ATOM   4119 O  O    . SER A 1 326 ? 38.373 6.080   38.851 1.000 13.33 ? 326  SER A O    1 
ATOM   4120 C  CB   . SER A 1 326 ? 38.706 8.940   40.302 1.000 14.63 ? 326  SER A CB   1 
ATOM   4121 O  OG   . SER A 1 326 ? 39.936 8.300   40.398 1.000 21.63 ? 326  SER A OG   1 
ATOM   4122 H  HA   . SER A 1 326 ? 38.193 8.521   38.383 1.000 12.92 ? 326  SER A HA   1 
ATOM   4123 H  HB2  . SER A 1 326 ? 38.857 9.876   40.097 1.000 17.55 ? 326  SER A HB2  1 
ATOM   4124 H  HB3  . SER A 1 326 ? 38.264 8.896   41.165 1.000 17.55 ? 326  SER A HB3  1 
ATOM   4125 N  N    . ALA A 1 327 ? 36.600 6.411   40.203 1.000 11.48 ? 327  ALA A N    1 
ATOM   4126 C  CA   . ALA A 1 327 ? 36.303 4.981   40.316 1.000 12.77 ? 327  ALA A CA   1 
ATOM   4127 C  C    . ALA A 1 327 ? 35.923 4.361   38.976 1.000 11.65 ? 327  ALA A C    1 
ATOM   4128 O  O    . ALA A 1 327 ? 36.351 3.276   38.638 1.000 13.78 ? 327  ALA A O    1 
ATOM   4129 C  CB   . ALA A 1 327 ? 35.217 4.766   41.362 1.000 13.38 ? 327  ALA A CB   1 
ATOM   4130 N  N    . ILE A 1 328 ? 35.123 5.093   38.178 1.000 9.87  ? 328  ILE A N    1 
ATOM   4131 C  CA   . ILE A 1 328 ? 34.797 4.639   36.866 1.000 9.52  ? 328  ILE A CA   1 
ATOM   4132 C  C    . ILE A 1 328 ? 36.049 4.670   35.983 1.000 10.72 ? 328  ILE A C    1 
ATOM   4133 O  O    . ILE A 1 328 ? 36.263 3.667   35.285 1.000 12.45 ? 328  ILE A O    1 
ATOM   4134 C  CB   . ILE A 1 328 ? 33.647 5.475   36.241 1.000 8.55  ? 328  ILE A CB   1 
ATOM   4135 C  CG1  . ILE A 1 328 ? 32.380 5.411   37.130 1.000 8.56  ? 328  ILE A CG1  1 
ATOM   4136 C  CG2  . ILE A 1 328 ? 33.362 5.011   34.833 1.000 9.89  ? 328  ILE A CG2  1 
ATOM   4137 C  CD1  . ILE A 1 328 ? 31.292 6.351   36.633 1.000 9.91  ? 328  ILE A CD1  1 
ATOM   4138 H  H    . ILE A 1 328 ? 34.806 5.840   38.462 1.000 11.85 ? 328  ILE A H    1 
ATOM   4139 H  HA   . ILE A 1 328 ? 34.495 3.709   36.932 1.000 11.43 ? 328  ILE A HA   1 
ATOM   4140 H  HG12 . ILE A 1 328 ? 32.040 4.503   37.137 1.000 10.27 ? 328  ILE A HG12 1 
ATOM   4141 H  HG13 . ILE A 1 328 ? 32.616 5.649   38.041 1.000 10.27 ? 328  ILE A HG13 1 
ATOM   4142 H  HG22 . ILE A 1 328 ? 33.119 4.097   34.867 1.000 14.84 ? 328  ILE A HG22 1 
ATOM   4143 H  HG23 . ILE A 1 328 ? 32.648 5.513   34.470 1.000 14.84 ? 328  ILE A HG23 1 
ATOM   4144 H  HD12 . ILE A 1 328 ? 31.424 7.160   37.083 1.000 14.86 ? 328  ILE A HD12 1 
ATOM   4145 N  N    . GLN A 1 329 ? 36.842 5.709   36.050 1.000 11.24 ? 329  GLN A N    1 
ATOM   4146 C  CA   . GLN A 1 329 ? 38.106 5.752   35.259 1.000 12.35 ? 329  GLN A CA   1 
ATOM   4147 C  C    . GLN A 1 329 ? 38.924 4.492   35.563 1.000 14.94 ? 329  GLN A C    1 
ATOM   4148 O  O    . GLN A 1 329 ? 39.525 3.905   34.638 1.000 17.02 ? 329  GLN A O    1 
ATOM   4149 C  CB   . GLN A 1 329 ? 38.923 6.987   35.617 1.000 12.00 ? 329  GLN A CB   1 
ATOM   4150 C  CG   . GLN A 1 329 ? 38.376 8.361   35.194 1.000 11.27 ? 329  GLN A CG   1 
ATOM   4151 C  CD   . GLN A 1 329 ? 39.176 9.482   35.724 1.000 10.82 ? 329  GLN A CD   1 
ATOM   4152 O  OE1  . GLN A 1 329 ? 39.723 9.434   36.833 1.000 14.33 ? 329  GLN A OE1  1 
ATOM   4153 N  NE2  . GLN A 1 329 ? 39.211 10.649  34.967 1.000 11.11 ? 329  GLN A NE2  1 
ATOM   4154 H  HA   . GLN A 1 329 ? 37.889 5.774   34.304 1.000 14.82 ? 329  GLN A HA   1 
ATOM   4155 H  HG2  . GLN A 1 329 ? 38.363 8.411   34.226 1.000 13.52 ? 329  GLN A HG2  1 
ATOM   4156 H  HG3  . GLN A 1 329 ? 37.462 8.448   35.508 1.000 13.52 ? 329  GLN A HG3  1 
ATOM   4157 N  N    . SER A 1 330 ? 38.925 4.053   36.861 1.000 16.03 ? 330  SER A N    1 
ATOM   4158 C  CA   A SER A 1 330 ? 39.760 2.911   37.258 0.452 18.96 ? 330  SER A CA   1 
ATOM   4159 C  CA   B SER A 1 330 ? 39.828 2.920   37.150 0.548 17.77 ? 330  SER A CA   1 
ATOM   4160 C  C    . SER A 1 330 ? 39.301 1.627   36.646 1.000 16.88 ? 330  SER A C    1 
ATOM   4161 O  O    . SER A 1 330 ? 40.015 0.595   36.620 1.000 21.63 ? 330  SER A O    1 
ATOM   4162 C  CB   A SER A 1 330 ? 39.763 2.812   38.790 0.452 21.99 ? 330  SER A CB   1 
ATOM   4163 C  CB   B SER A 1 330 ? 40.101 2.908   38.665 0.548 21.43 ? 330  SER A CB   1 
ATOM   4164 O  OG   A SER A 1 330 ? 38.739 1.955   39.282 0.452 21.28 ? 330  SER A OG   1 
ATOM   4165 O  OG   B SER A 1 330 ? 40.901 4.031   38.960 0.548 21.72 ? 330  SER A OG   1 
ATOM   4166 H  H    A SER A 1 330 ? 38.434 4.448   37.446 1.000 19.24 ? 330  SER A H    1 
ATOM   4167 N  N    . MET A 1 331 ? 38.078 1.570   36.163 1.000 13.57 ? 331  MET A N    1 
ATOM   4168 C  CA   . MET A 1 331 ? 37.552 0.311   35.668 1.000 13.93 ? 331  MET A CA   1 
ATOM   4169 C  C    . MET A 1 331 ? 37.580 0.267   34.147 1.000 16.71 ? 331  MET A C    1 
ATOM   4170 O  O    . MET A 1 331 ? 37.044 -0.615  33.485 1.000 24.30 ? 331  MET A O    1 
ATOM   4171 C  CB   A MET A 1 331 ? 36.092 0.214   36.165 0.565 18.43 ? 331  MET A CB   1 
ATOM   4172 C  CB   B MET A 1 331 ? 36.114 0.075   36.169 0.435 17.41 ? 331  MET A CB   1 
ATOM   4173 C  CG   A MET A 1 331 ? 35.815 0.076   37.644 0.565 16.65 ? 331  MET A CG   1 
ATOM   4174 C  CG   B MET A 1 331 ? 36.133 -0.716  37.474 0.435 18.88 ? 331  MET A CG   1 
ATOM   4175 S  SD   A MET A 1 331 ? 34.122 -0.152  38.278 0.565 14.51 ? 331  MET A SD   1 
ATOM   4176 S  SD   B MET A 1 331 ? 34.611 -1.407  38.101 0.435 19.19 ? 331  MET A SD   1 
ATOM   4177 C  CE   A MET A 1 331 ? 33.670 -1.752  37.618 0.565 13.02 ? 331  MET A CE   1 
ATOM   4178 C  CE   B MET A 1 331 ? 33.604 -1.701  36.650 0.435 27.62 ? 331  MET A CE   1 
ATOM   4179 N  N    . ARG A 1 332 ? 38.235 1.201   33.495 1.000 17.19 ? 332  ARG A N    1 
ATOM   4180 C  CA   A ARG A 1 332 ? 38.309 1.179   32.031 0.555 22.24 ? 332  ARG A CA   1 
ATOM   4181 C  CA   B ARG A 1 332 ? 38.323 1.346   32.058 0.445 22.14 ? 332  ARG A CA   1 
ATOM   4182 C  C    . ARG A 1 332 ? 39.731 1.419   31.504 1.000 26.12 ? 332  ARG A C    1 
ATOM   4183 O  O    A ARG A 1 332 ? 40.606 1.673   32.369 0.555 25.61 ? 332  ARG A O    1 
ATOM   4184 O  O    B ARG A 1 332 ? 40.762 1.428   32.201 0.445 31.05 ? 332  ARG A O    1 
ATOM   4185 C  CB   A ARG A 1 332 ? 37.540 2.295   31.348 0.555 24.35 ? 332  ARG A CB   1 
ATOM   4186 C  CB   B ARG A 1 332 ? 37.652 2.681   31.651 0.445 21.95 ? 332  ARG A CB   1 
ATOM   4187 C  CG   A ARG A 1 332 ? 36.314 2.849   31.998 0.555 23.32 ? 332  ARG A CG   1 
ATOM   4188 C  CG   B ARG A 1 332 ? 36.160 2.611   31.910 0.445 22.00 ? 332  ARG A CG   1 
ATOM   4189 C  CD   A ARG A 1 332 ? 36.082 4.262   31.524 0.555 23.56 ? 332  ARG A CD   1 
ATOM   4190 C  CD   B ARG A 1 332 ? 35.593 3.963   31.523 0.445 22.61 ? 332  ARG A CD   1 
ATOM   4191 N  NE   A ARG A 1 332 ? 35.872 4.359   30.078 0.555 24.07 ? 332  ARG A NE   1 
ATOM   4192 N  NE   B ARG A 1 332 ? 36.260 4.401   30.276 0.445 24.62 ? 332  ARG A NE   1 
ATOM   4193 C  CZ   A ARG A 1 332 ? 36.460 5.196   29.229 0.555 22.11 ? 332  ARG A CZ   1 
ATOM   4194 C  CZ   B ARG A 1 332 ? 35.591 4.494   29.116 0.445 23.26 ? 332  ARG A CZ   1 
ATOM   4195 N  NH1  A ARG A 1 332 ? 37.355 6.050   29.723 0.555 28.25 ? 332  ARG A NH1  1 
ATOM   4196 N  NH1  B ARG A 1 332 ? 34.287 4.177   29.067 0.445 28.31 ? 332  ARG A NH1  1 
ATOM   4197 N  NH2  A ARG A 1 332 ? 36.223 5.258   27.915 0.555 29.67 ? 332  ARG A NH2  1 
ATOM   4198 N  NH2  B ARG A 1 332 ? 36.193 4.894   28.002 0.445 27.19 ? 332  ARG A NH2  1 
ATOM   4199 O  OXT  A ARG A 1 332 ? 39.903 1.355   30.271 0.555 38.74 ? 332  ARG A OXT  1 
ATOM   4200 O  OXT  B ARG A 1 332 ? 39.792 1.485   30.240 0.445 38.02 ? 332  ARG A OXT  1 
HETATM 4201 FE FE   . FE  B 2 .   ? 21.055 3.977   38.360 1.000 3.89  ? 401  FE  A FE   1 
HETATM 4202 C  C    . CO3 C 3 .   ? 21.759 1.554   38.165 1.000 5.15  ? 402  CO3 A C    1 
HETATM 4203 O  O1   . CO3 C 3 .   ? 21.004 2.110   37.247 1.000 5.53  ? 402  CO3 A O1   1 
HETATM 4204 O  O2   . CO3 C 3 .   ? 22.144 0.353   38.086 1.000 5.54  ? 402  CO3 A O2   1 
HETATM 4205 O  O3   . CO3 C 3 .   ? 22.110 2.329   39.121 1.000 4.91  ? 402  CO3 A O3   1 
HETATM 4206 C  C1   . GOL D 4 .   ? 34.190 15.472  32.092 1.000 8.24  ? 403  GOL A C1   1 
HETATM 4207 O  O1   . GOL D 4 .   ? 33.238 16.328  32.665 1.000 7.76  ? 403  GOL A O1   1 
HETATM 4208 C  C2   . GOL D 4 .   ? 34.259 15.619  30.562 1.000 9.15  ? 403  GOL A C2   1 
HETATM 4209 O  O2   . GOL D 4 .   ? 34.786 16.914  30.223 1.000 13.09 ? 403  GOL A O2   1 
HETATM 4210 C  C3   . GOL D 4 .   ? 35.147 14.567  29.926 1.000 9.36  ? 403  GOL A C3   1 
HETATM 4211 O  O3   . GOL D 4 .   ? 35.131 14.655  28.526 1.000 9.32  ? 403  GOL A O3   1 
HETATM 4212 O  O    . HOH E 5 .   ? 15.475 -18.608 52.467 0.623 37.08 ? 501  HOH A O    1 
HETATM 4213 O  O    . HOH E 5 .   ? 21.416 22.564  19.797 1.000 52.62 ? 502  HOH A O    1 
HETATM 4214 O  O    . HOH E 5 .   ? 7.922  27.079  27.647 1.000 24.53 ? 503  HOH A O    1 
HETATM 4215 O  O    . HOH E 5 .   ? -0.298 5.354   23.524 1.000 31.10 ? 504  HOH A O    1 
HETATM 4216 O  O    . HOH E 5 .   ? 13.096 4.690   51.492 1.000 54.96 ? 505  HOH A O    1 
HETATM 4217 O  O    . HOH E 5 .   ? 26.440 -3.351  60.752 1.000 52.85 ? 506  HOH A O    1 
HETATM 4218 O  O    . HOH E 5 .   ? 19.838 17.164  57.179 1.000 38.89 ? 507  HOH A O    1 
HETATM 4219 O  O    . HOH E 5 .   ? 26.255 -17.051 56.885 1.000 36.29 ? 508  HOH A O    1 
HETATM 4220 O  O    . HOH E 5 .   ? 26.036 7.298   39.191 1.000 19.39 ? 509  HOH A O    1 
HETATM 4221 O  O    . HOH E 5 .   ? 20.331 -18.223 47.061 1.000 34.33 ? 510  HOH A O    1 
HETATM 4222 O  O    . HOH E 5 .   ? 38.190 7.193   31.744 1.000 26.75 ? 511  HOH A O    1 
HETATM 4223 O  O    A HOH E 5 .   ? 40.843 6.315   39.234 0.692 14.31 ? 512  HOH A O    1 
HETATM 4224 O  O    B HOH E 5 .   ? 41.657 7.465   37.488 0.308 13.45 ? 512  HOH A O    1 
HETATM 4225 O  O    . HOH E 5 .   ? 6.564  -8.182  53.899 1.000 30.15 ? 513  HOH A O    1 
HETATM 4226 O  O    . HOH E 5 .   ? 2.113  0.968   32.940 1.000 33.55 ? 514  HOH A O    1 
HETATM 4227 O  O    . HOH E 5 .   ? 34.651 -17.878 33.248 1.000 17.40 ? 515  HOH A O    1 
HETATM 4228 O  O    . HOH E 5 .   ? 27.264 24.176  29.779 1.000 20.90 ? 516  HOH A O    1 
HETATM 4229 O  O    . HOH E 5 .   ? 23.931 -13.503 56.893 1.000 27.78 ? 517  HOH A O    1 
HETATM 4230 O  O    . HOH E 5 .   ? 10.040 25.041  37.251 1.000 32.13 ? 518  HOH A O    1 
HETATM 4231 O  O    . HOH E 5 .   ? 6.128  -10.536 45.150 1.000 17.20 ? 519  HOH A O    1 
HETATM 4232 O  O    . HOH E 5 .   ? 3.006  23.689  19.853 1.000 20.87 ? 520  HOH A O    1 
HETATM 4233 O  O    . HOH E 5 .   ? 8.586  2.219   18.506 1.000 37.55 ? 521  HOH A O    1 
HETATM 4234 O  O    . HOH E 5 .   ? 46.011 -1.451  37.364 1.000 58.39 ? 522  HOH A O    1 
HETATM 4235 O  O    . HOH E 5 .   ? -2.277 7.273   23.521 1.000 45.96 ? 523  HOH A O    1 
HETATM 4236 O  O    . HOH E 5 .   ? 24.211 9.317   14.997 1.000 25.56 ? 524  HOH A O    1 
HETATM 4237 O  O    A HOH E 5 .   ? 11.287 -1.837  29.064 0.590 9.43  ? 525  HOH A O    1 
HETATM 4238 O  O    B HOH E 5 .   ? 11.266 -1.249  28.404 0.410 15.11 ? 525  HOH A O    1 
HETATM 4239 O  O    . HOH E 5 .   ? 2.347  5.964   28.085 1.000 43.69 ? 526  HOH A O    1 
HETATM 4240 O  O    . HOH E 5 .   ? 5.334  -5.808  53.127 1.000 38.87 ? 527  HOH A O    1 
HETATM 4241 O  O    . HOH E 5 .   ? 32.424 -18.647 29.079 1.000 23.03 ? 528  HOH A O    1 
HETATM 4242 O  O    . HOH E 5 .   ? 9.645  -12.899 35.408 1.000 34.39 ? 529  HOH A O    1 
HETATM 4243 O  O    . HOH E 5 .   ? -0.244 -3.415  40.277 1.000 44.96 ? 530  HOH A O    1 
HETATM 4244 O  O    . HOH E 5 .   ? 35.995 -1.561  31.331 1.000 37.39 ? 531  HOH A O    1 
HETATM 4245 O  O    . HOH E 5 .   ? 29.889 1.414   25.515 1.000 36.10 ? 532  HOH A O    1 
HETATM 4246 O  O    . HOH E 5 .   ? 22.477 13.935  47.697 1.000 27.76 ? 533  HOH A O    1 
HETATM 4247 O  O    . HOH E 5 .   ? 29.948 -5.469  26.458 1.000 45.10 ? 534  HOH A O    1 
HETATM 4248 O  O    A HOH E 5 .   ? 15.228 -5.720  23.076 0.706 18.50 ? 535  HOH A O    1 
HETATM 4249 O  O    B HOH E 5 .   ? 16.876 -5.025  22.090 0.294 24.25 ? 535  HOH A O    1 
HETATM 4250 O  O    . HOH E 5 .   ? -2.061 9.634   23.054 1.000 24.75 ? 536  HOH A O    1 
HETATM 4251 O  O    . HOH E 5 .   ? 41.418 9.355   42.250 1.000 35.52 ? 537  HOH A O    1 
HETATM 4252 O  O    . HOH E 5 .   ? 8.012  11.558  51.863 1.000 41.28 ? 538  HOH A O    1 
HETATM 4253 O  O    . HOH E 5 .   ? 8.372  -12.009 46.194 1.000 17.15 ? 539  HOH A O    1 
HETATM 4254 O  O    . HOH E 5 .   ? 39.900 -12.430 37.771 1.000 26.35 ? 540  HOH A O    1 
HETATM 4255 O  O    . HOH E 5 .   ? 26.792 -3.093  25.810 1.000 24.05 ? 541  HOH A O    1 
HETATM 4256 O  O    . HOH E 5 .   ? 32.876 -12.039 48.235 1.000 24.98 ? 542  HOH A O    1 
HETATM 4257 O  O    . HOH E 5 .   ? 13.613 -7.000  55.041 1.000 9.84  ? 543  HOH A O    1 
HETATM 4258 O  O    . HOH E 5 .   ? 46.497 -4.094  33.838 1.000 24.04 ? 544  HOH A O    1 
HETATM 4259 O  O    . HOH E 5 .   ? 42.925 -2.986  38.866 1.000 65.46 ? 545  HOH A O    1 
HETATM 4260 O  O    . HOH E 5 .   ? 29.123 -16.923 56.045 1.000 40.10 ? 546  HOH A O    1 
HETATM 4261 O  O    A HOH E 5 .   ? 24.020 7.881   54.132 0.342 21.80 ? 547  HOH A O    1 
HETATM 4262 O  O    B HOH E 5 .   ? 24.987 9.501   52.981 0.658 17.38 ? 547  HOH A O    1 
HETATM 4263 O  O    . HOH E 5 .   ? 5.922  24.786  35.189 1.000 31.36 ? 548  HOH A O    1 
HETATM 4264 O  O    . HOH E 5 .   ? 8.921  -9.529  31.772 1.000 26.96 ? 549  HOH A O    1 
HETATM 4265 O  O    . HOH E 5 .   ? -1.553 7.560   29.646 1.000 29.67 ? 550  HOH A O    1 
HETATM 4266 O  O    . HOH E 5 .   ? 19.354 -18.803 43.298 1.000 27.48 ? 551  HOH A O    1 
HETATM 4267 O  O    A HOH E 5 .   ? 31.587 22.671  31.535 0.573 26.21 ? 552  HOH A O    1 
HETATM 4268 O  O    B HOH E 5 .   ? 30.464 22.655  32.825 0.427 17.51 ? 552  HOH A O    1 
HETATM 4269 O  O    . HOH E 5 .   ? 20.134 14.248  50.087 1.000 30.34 ? 553  HOH A O    1 
HETATM 4270 O  O    . HOH E 5 .   ? 31.428 5.055   24.320 1.000 19.32 ? 554  HOH A O    1 
HETATM 4271 O  O    . HOH E 5 .   ? 24.217 -8.235  25.560 1.000 18.57 ? 555  HOH A O    1 
HETATM 4272 O  O    . HOH E 5 .   ? 12.183 -14.105 49.286 1.000 33.34 ? 556  HOH A O    1 
HETATM 4273 O  O    . HOH E 5 .   ? 5.644  32.385  22.181 1.000 37.92 ? 557  HOH A O    1 
HETATM 4274 O  O    . HOH E 5 .   ? 32.600 12.163  31.184 1.000 6.68  ? 558  HOH A O    1 
HETATM 4275 O  O    . HOH E 5 .   ? 31.633 5.371   21.451 1.000 16.07 ? 559  HOH A O    1 
HETATM 4276 O  O    . HOH E 5 .   ? 3.728  26.074  26.824 1.000 16.31 ? 560  HOH A O    1 
HETATM 4277 O  O    A HOH E 5 .   ? 8.962  13.671  50.468 0.697 16.79 ? 561  HOH A O    1 
HETATM 4278 O  O    B HOH E 5 .   ? 9.312  12.848  49.601 0.303 9.06  ? 561  HOH A O    1 
HETATM 4279 O  O    . HOH E 5 .   ? 26.364 -1.808  58.119 1.000 33.99 ? 562  HOH A O    1 
HETATM 4280 O  O    . HOH E 5 .   ? -0.448 26.169  20.665 1.000 34.34 ? 563  HOH A O    1 
HETATM 4281 O  O    A HOH E 5 .   ? 23.747 -0.334  19.166 0.680 21.53 ? 564  HOH A O    1 
HETATM 4282 O  O    B HOH E 5 .   ? 23.527 -0.188  17.855 0.320 30.61 ? 564  HOH A O    1 
HETATM 4283 O  O    . HOH E 5 .   ? 23.751 -20.524 43.250 1.000 27.49 ? 565  HOH A O    1 
HETATM 4284 O  O    . HOH E 5 .   ? 0.968  10.431  43.157 1.000 22.97 ? 566  HOH A O    1 
HETATM 4285 O  O    . HOH E 5 .   ? 27.965 17.928  19.249 1.000 13.13 ? 567  HOH A O    1 
HETATM 4286 O  O    . HOH E 5 .   ? 14.487 -20.190 38.308 1.000 32.07 ? 568  HOH A O    1 
HETATM 4287 O  O    . HOH E 5 .   ? 5.241  16.907  18.029 1.000 12.26 ? 569  HOH A O    1 
HETATM 4288 O  O    . HOH E 5 .   ? 33.730 19.492  30.898 1.000 20.14 ? 570  HOH A O    1 
HETATM 4289 O  O    . HOH E 5 .   ? 34.290 -14.812 25.905 1.000 20.39 ? 571  HOH A O    1 
HETATM 4290 O  O    . HOH E 5 .   ? 17.094 -21.171 41.400 1.000 29.83 ? 572  HOH A O    1 
HETATM 4291 O  O    . HOH E 5 .   ? 17.115 -12.798 58.333 1.000 8.23  ? 573  HOH A O    1 
HETATM 4292 O  O    . HOH E 5 .   ? 10.719 -1.224  58.710 1.000 16.96 ? 574  HOH A O    1 
HETATM 4293 O  O    . HOH E 5 .   ? 15.029 -18.299 44.709 1.000 17.98 ? 575  HOH A O    1 
HETATM 4294 O  O    . HOH E 5 .   ? 12.499 -3.759  55.869 1.000 12.54 ? 576  HOH A O    1 
HETATM 4295 O  O    . HOH E 5 .   ? 23.691 6.902   38.880 1.000 8.05  ? 577  HOH A O    1 
HETATM 4296 O  O    . HOH E 5 .   ? 2.435  3.978   43.346 1.000 33.92 ? 578  HOH A O    1 
HETATM 4297 O  O    . HOH E 5 .   ? 42.224 -0.067  33.860 1.000 29.06 ? 579  HOH A O    1 
HETATM 4298 O  O    . HOH E 5 .   ? 19.013 -17.510 29.557 1.000 24.10 ? 580  HOH A O    1 
HETATM 4299 O  O    . HOH E 5 .   ? 12.624 0.513   28.524 1.000 11.56 ? 581  HOH A O    1 
HETATM 4300 O  O    . HOH E 5 .   ? 32.456 -18.829 37.214 1.000 16.41 ? 582  HOH A O    1 
HETATM 4301 O  O    . HOH E 5 .   ? 23.789 24.680  30.147 1.000 21.20 ? 583  HOH A O    1 
HETATM 4302 O  O    . HOH E 5 .   ? 31.937 0.435   33.966 1.000 20.94 ? 584  HOH A O    1 
HETATM 4303 O  O    . HOH E 5 .   ? 31.513 0.370   48.148 1.000 16.22 ? 585  HOH A O    1 
HETATM 4304 O  O    . HOH E 5 .   ? 25.747 -12.062 58.438 1.000 19.14 ? 586  HOH A O    1 
HETATM 4305 O  O    . HOH E 5 .   ? 1.867  6.439   22.363 1.000 11.47 ? 587  HOH A O    1 
HETATM 4306 O  O    . HOH E 5 .   ? 46.601 -10.149 35.670 1.000 38.61 ? 588  HOH A O    1 
HETATM 4307 O  O    . HOH E 5 .   ? 42.970 -12.228 30.765 1.000 36.63 ? 589  HOH A O    1 
HETATM 4308 O  O    . HOH E 5 .   ? 15.666 7.068   27.074 1.000 6.62  ? 590  HOH A O    1 
HETATM 4309 O  O    . HOH E 5 .   ? -2.741 15.930  20.633 1.000 52.96 ? 591  HOH A O    1 
HETATM 4310 O  O    . HOH E 5 .   ? 16.295 12.577  14.072 1.000 21.49 ? 592  HOH A O    1 
HETATM 4311 O  O    A HOH E 5 .   ? 28.487 2.649   30.089 0.711 13.55 ? 593  HOH A O    1 
HETATM 4312 O  O    B HOH E 5 .   ? 27.480 1.688   29.760 0.289 16.78 ? 593  HOH A O    1 
HETATM 4313 O  O    . HOH E 5 .   ? 9.038  1.211   55.834 1.000 37.12 ? 594  HOH A O    1 
HETATM 4314 O  O    . HOH E 5 .   ? 6.079  7.048   48.742 1.000 39.49 ? 595  HOH A O    1 
HETATM 4315 O  O    . HOH E 5 .   ? 12.693 21.850  39.200 1.000 8.56  ? 596  HOH A O    1 
HETATM 4316 O  O    . HOH E 5 .   ? 14.021 27.720  20.327 1.000 14.09 ? 597  HOH A O    1 
HETATM 4317 O  O    . HOH E 5 .   ? 28.839 -20.120 45.975 1.000 25.35 ? 598  HOH A O    1 
HETATM 4318 O  O    . HOH E 5 .   ? 0.709  19.724  28.306 1.000 10.29 ? 599  HOH A O    1 
HETATM 4319 O  O    . HOH E 5 .   ? -2.227 18.195  23.500 1.000 20.33 ? 600  HOH A O    1 
HETATM 4320 O  O    . HOH E 5 .   ? 12.324 -0.132  51.467 1.000 24.91 ? 601  HOH A O    1 
HETATM 4321 O  O    . HOH E 5 .   ? -4.538 14.220  30.530 1.000 13.46 ? 602  HOH A O    1 
HETATM 4322 O  O    . HOH E 5 .   ? 13.310 -11.045 25.453 1.000 16.38 ? 603  HOH A O    1 
HETATM 4323 O  O    . HOH E 5 .   ? 8.901  -15.764 40.506 1.000 12.88 ? 604  HOH A O    1 
HETATM 4324 O  O    . HOH E 5 .   ? 29.000 8.182   44.497 1.000 23.97 ? 605  HOH A O    1 
HETATM 4325 O  O    . HOH E 5 .   ? 9.232  -3.167  56.083 1.000 33.31 ? 606  HOH A O    1 
HETATM 4326 O  O    . HOH E 5 .   ? 37.359 -14.693 45.202 1.000 38.98 ? 607  HOH A O    1 
HETATM 4327 O  O    . HOH E 5 .   ? 8.608  -12.404 38.904 1.000 12.72 ? 608  HOH A O    1 
HETATM 4328 O  O    . HOH E 5 .   ? 11.785 7.984   45.574 1.000 7.39  ? 609  HOH A O    1 
HETATM 4329 O  O    . HOH E 5 .   ? 16.344 -10.604 30.548 1.000 8.16  ? 610  HOH A O    1 
HETATM 4330 O  O    . HOH E 5 .   ? 22.997 -21.355 35.151 1.000 31.60 ? 611  HOH A O    1 
HETATM 4331 O  O    . HOH E 5 .   ? 5.475  2.458   36.422 1.000 19.51 ? 612  HOH A O    1 
HETATM 4332 O  O    . HOH E 5 .   ? 27.111 5.074   51.760 1.000 26.81 ? 613  HOH A O    1 
HETATM 4333 O  O    . HOH E 5 .   ? 3.785  9.823   39.577 1.000 10.58 ? 614  HOH A O    1 
HETATM 4334 O  O    . HOH E 5 .   ? 12.598 29.150  23.084 1.000 14.32 ? 615  HOH A O    1 
HETATM 4335 O  O    . HOH E 5 .   ? 30.013 3.242   33.553 1.000 12.59 ? 616  HOH A O    1 
HETATM 4336 O  O    . HOH E 5 .   ? 13.658 7.403   47.643 1.000 8.74  ? 617  HOH A O    1 
HETATM 4337 O  O    . HOH E 5 .   ? 42.390 -9.625  34.444 1.000 29.48 ? 618  HOH A O    1 
HETATM 4338 O  O    . HOH E 5 .   ? 17.640 6.161   28.870 1.000 6.67  ? 619  HOH A O    1 
HETATM 4339 O  O    . HOH E 5 .   ? 0.884  8.451   20.733 1.000 14.30 ? 620  HOH A O    1 
HETATM 4340 O  O    . HOH E 5 .   ? 13.981 0.393   41.676 1.000 7.29  ? 621  HOH A O    1 
HETATM 4341 O  O    . HOH E 5 .   ? 6.765  -8.995  43.028 1.000 15.77 ? 622  HOH A O    1 
HETATM 4342 O  O    . HOH E 5 .   ? 12.595 0.206   39.195 1.000 6.30  ? 623  HOH A O    1 
HETATM 4343 O  O    . HOH E 5 .   ? 34.172 8.045   23.835 1.000 13.22 ? 624  HOH A O    1 
HETATM 4344 O  O    . HOH E 5 .   ? 16.709 26.396  23.647 1.000 11.18 ? 625  HOH A O    1 
HETATM 4345 O  O    . HOH E 5 .   ? 30.468 -13.180 24.348 1.000 10.94 ? 626  HOH A O    1 
HETATM 4346 O  O    . HOH E 5 .   ? 27.073 8.228   41.613 0.297 8.21  ? 627  HOH A O    1 
HETATM 4347 O  O    . HOH E 5 .   ? 7.620  8.365   42.047 1.000 8.70  ? 628  HOH A O    1 
HETATM 4348 O  O    . HOH E 5 .   ? 8.133  0.665   39.846 1.000 9.88  ? 629  HOH A O    1 
HETATM 4349 O  O    . HOH E 5 .   ? 34.150 -9.487  49.855 1.000 46.49 ? 630  HOH A O    1 
HETATM 4350 O  O    . HOH E 5 .   ? -1.620 12.327  40.961 1.000 15.48 ? 631  HOH A O    1 
HETATM 4351 O  O    . HOH E 5 .   ? 17.239 -16.927 44.156 1.000 22.67 ? 632  HOH A O    1 
HETATM 4352 O  O    . HOH E 5 .   ? 22.808 22.615  33.052 1.000 12.90 ? 633  HOH A O    1 
HETATM 4353 O  O    A HOH E 5 .   ? 34.960 -16.787 27.835 0.861 18.59 ? 634  HOH A O    1 
HETATM 4354 O  O    B HOH E 5 .   ? 35.413 -15.506 28.116 0.139 12.56 ? 634  HOH A O    1 
HETATM 4355 O  O    . HOH E 5 .   ? 12.591 -1.591  33.354 1.000 7.84  ? 635  HOH A O    1 
HETATM 4356 O  O    . HOH E 5 .   ? 8.127  29.086  16.027 1.000 33.88 ? 636  HOH A O    1 
HETATM 4357 O  O    . HOH E 5 .   ? 20.561 21.962  41.116 1.000 11.85 ? 637  HOH A O    1 
HETATM 4358 O  O    . HOH E 5 .   ? 12.336 -10.200 21.474 1.000 24.56 ? 638  HOH A O    1 
HETATM 4359 O  O    . HOH E 5 .   ? 19.598 -14.929 56.101 1.000 21.69 ? 639  HOH A O    1 
HETATM 4360 O  O    . HOH E 5 .   ? 39.981 -10.060 33.299 1.000 17.91 ? 640  HOH A O    1 
HETATM 4361 O  O    . HOH E 5 .   ? 15.728 5.437   14.852 1.000 43.89 ? 641  HOH A O    1 
HETATM 4362 O  O    . HOH E 5 .   ? -8.874 19.811  33.218 1.000 9.62  ? 642  HOH A O    1 
HETATM 4363 O  O    . HOH E 5 .   ? 11.397 -6.104  58.652 1.000 12.40 ? 643  HOH A O    1 
HETATM 4364 O  O    . HOH E 5 .   ? 41.460 -7.160  42.806 1.000 40.09 ? 644  HOH A O    1 
HETATM 4365 O  O    . HOH E 5 .   ? 26.814 -2.033  53.853 1.000 12.17 ? 645  HOH A O    1 
HETATM 4366 O  O    . HOH E 5 .   ? 25.754 22.337  18.908 1.000 10.09 ? 646  HOH A O    1 
HETATM 4367 O  O    . HOH E 5 .   ? -0.650 20.469  24.454 1.000 17.05 ? 647  HOH A O    1 
HETATM 4368 O  O    . HOH E 5 .   ? 12.927 18.079  56.704 1.000 24.10 ? 648  HOH A O    1 
HETATM 4369 O  O    . HOH E 5 .   ? 18.752 1.355   59.220 1.000 17.39 ? 649  HOH A O    1 
HETATM 4370 O  O    . HOH E 5 .   ? 12.269 29.772  20.429 1.000 17.44 ? 650  HOH A O    1 
HETATM 4371 O  O    . HOH E 5 .   ? 30.070 -8.592  60.750 1.000 48.05 ? 651  HOH A O    1 
HETATM 4372 O  O    . HOH E 5 .   ? 24.121 4.854   16.178 1.000 42.08 ? 652  HOH A O    1 
HETATM 4373 O  O    . HOH E 5 .   ? 31.906 7.817   17.908 1.000 30.65 ? 653  HOH A O    1 
HETATM 4374 O  O    . HOH E 5 .   ? 25.304 21.301  32.783 1.000 10.05 ? 654  HOH A O    1 
HETATM 4375 O  O    . HOH E 5 .   ? 13.436 2.848   55.526 1.000 32.46 ? 655  HOH A O    1 
HETATM 4376 O  O    . HOH E 5 .   ? 7.552  11.372  17.779 1.000 7.53  ? 656  HOH A O    1 
HETATM 4377 O  O    . HOH E 5 .   ? 21.512 21.018  24.075 1.000 7.46  ? 657  HOH A O    1 
HETATM 4378 O  O    . HOH E 5 .   ? 7.571  25.659  33.832 1.000 28.59 ? 658  HOH A O    1 
HETATM 4379 O  O    . HOH E 5 .   ? 24.111 -2.412  44.257 1.000 12.85 ? 659  HOH A O    1 
HETATM 4380 O  O    . HOH E 5 .   ? -2.840 17.864  27.347 1.000 16.38 ? 660  HOH A O    1 
HETATM 4381 O  O    . HOH E 5 .   ? 23.164 14.784  44.956 1.000 20.36 ? 661  HOH A O    1 
HETATM 4382 O  O    . HOH E 5 .   ? 31.447 -18.463 48.062 1.000 36.39 ? 662  HOH A O    1 
HETATM 4383 O  O    . HOH E 5 .   ? 26.570 -12.099 22.915 1.000 29.88 ? 663  HOH A O    1 
HETATM 4384 O  O    . HOH E 5 .   ? 37.598 16.866  25.222 1.000 28.99 ? 664  HOH A O    1 
HETATM 4385 O  O    . HOH E 5 .   ? 14.844 13.153  16.128 1.000 26.45 ? 665  HOH A O    1 
HETATM 4386 O  O    . HOH E 5 .   ? 26.290 2.722   19.417 1.000 17.67 ? 666  HOH A O    1 
HETATM 4387 O  O    . HOH E 5 .   ? 17.427 3.002   56.140 1.000 14.40 ? 667  HOH A O    1 
HETATM 4388 O  O    . HOH E 5 .   ? 27.942 17.634  21.940 1.000 10.57 ? 668  HOH A O    1 
HETATM 4389 O  O    . HOH E 5 .   ? 5.653  5.488   33.452 1.000 8.64  ? 669  HOH A O    1 
HETATM 4390 O  O    . HOH E 5 .   ? -7.626 10.119  32.068 1.000 21.44 ? 670  HOH A O    1 
HETATM 4391 O  O    . HOH E 5 .   ? 14.822 -1.610  31.806 1.000 6.97  ? 671  HOH A O    1 
HETATM 4392 O  O    A HOH E 5 .   ? 1.494  20.672  39.712 0.808 20.65 ? 672  HOH A O    1 
HETATM 4393 O  O    B HOH E 5 .   ? 2.125  21.930  39.009 0.192 6.77  ? 672  HOH A O    1 
HETATM 4394 O  O    . HOH E 5 .   ? 37.449 12.251  31.378 1.000 21.98 ? 673  HOH A O    1 
HETATM 4395 O  O    . HOH E 5 .   ? 6.129  15.628  40.375 1.000 9.17  ? 674  HOH A O    1 
HETATM 4396 O  O    . HOH E 5 .   ? 15.088 1.122   59.517 1.000 38.80 ? 675  HOH A O    1 
HETATM 4397 O  O    . HOH E 5 .   ? 28.521 19.340  23.964 1.000 8.87  ? 676  HOH A O    1 
HETATM 4398 O  O    . HOH E 5 .   ? -5.496 12.186  28.944 1.000 16.54 ? 677  HOH A O    1 
HETATM 4399 O  O    . HOH E 5 .   ? 31.048 19.210  27.335 1.000 13.40 ? 678  HOH A O    1 
HETATM 4400 O  O    . HOH E 5 .   ? 2.302  -8.229  53.620 1.000 62.47 ? 679  HOH A O    1 
HETATM 4401 O  O    . HOH E 5 .   ? 13.173 -16.916 34.254 1.000 21.24 ? 680  HOH A O    1 
HETATM 4402 O  O    . HOH E 5 .   ? 11.390 16.619  15.450 1.000 13.69 ? 681  HOH A O    1 
HETATM 4403 O  O    . HOH E 5 .   ? 8.751  6.276   34.966 1.000 7.01  ? 682  HOH A O    1 
HETATM 4404 O  O    . HOH E 5 .   ? 38.162 15.856  33.113 1.000 16.49 ? 683  HOH A O    1 
HETATM 4405 O  O    . HOH E 5 .   ? -0.980 20.139  43.389 1.000 11.57 ? 684  HOH A O    1 
HETATM 4406 O  O    . HOH E 5 .   ? 36.434 -17.760 41.182 1.000 15.89 ? 685  HOH A O    1 
HETATM 4407 O  O    . HOH E 5 .   ? 21.238 18.432  23.061 1.000 6.84  ? 686  HOH A O    1 
HETATM 4408 O  O    . HOH E 5 .   ? 9.888  12.040  57.350 1.000 30.35 ? 687  HOH A O    1 
HETATM 4409 O  O    . HOH E 5 .   ? 12.826 3.613   40.047 1.000 6.72  ? 688  HOH A O    1 
HETATM 4410 O  O    . HOH E 5 .   ? 11.789 -2.474  22.584 1.000 26.53 ? 689  HOH A O    1 
HETATM 4411 O  O    . HOH E 5 .   ? 34.138 -5.487  30.528 1.000 18.99 ? 690  HOH A O    1 
HETATM 4412 O  O    . HOH E 5 .   ? 18.072 -8.900  57.803 1.000 8.24  ? 691  HOH A O    1 
HETATM 4413 O  O    . HOH E 5 .   ? 5.630  19.453  17.220 1.000 16.63 ? 692  HOH A O    1 
HETATM 4414 O  O    . HOH E 5 .   ? 20.225 -19.053 40.600 1.000 12.61 ? 693  HOH A O    1 
HETATM 4415 O  O    A HOH E 5 .   ? 15.841 4.798   30.478 0.607 6.45  ? 694  HOH A O    1 
HETATM 4416 O  O    B HOH E 5 .   ? 15.244 6.131   30.465 0.393 8.98  ? 694  HOH A O    1 
HETATM 4417 O  O    . HOH E 5 .   ? 4.422  17.708  21.825 1.000 8.63  ? 695  HOH A O    1 
HETATM 4418 O  O    A HOH E 5 .   ? 25.288 -21.717 39.237 0.527 18.98 ? 696  HOH A O    1 
HETATM 4419 O  O    B HOH E 5 .   ? 25.359 -21.483 37.862 0.473 17.39 ? 696  HOH A O    1 
HETATM 4420 O  O    . HOH E 5 .   ? 15.988 1.348   35.408 1.000 7.64  ? 697  HOH A O    1 
HETATM 4421 O  O    . HOH E 5 .   ? 33.370 -19.987 47.236 1.000 23.53 ? 698  HOH A O    1 
HETATM 4422 O  O    . HOH E 5 .   ? 13.510 2.470   30.412 1.000 10.39 ? 699  HOH A O    1 
HETATM 4423 O  O    . HOH E 5 .   ? 25.333 15.321  41.894 1.000 20.59 ? 700  HOH A O    1 
HETATM 4424 O  O    . HOH E 5 .   ? 1.475  17.395  38.004 1.000 9.35  ? 701  HOH A O    1 
HETATM 4425 O  O    . HOH E 5 .   ? 43.851 -9.218  36.552 1.000 39.16 ? 702  HOH A O    1 
HETATM 4426 O  O    . HOH E 5 .   ? 5.847  23.725  19.361 1.000 13.90 ? 703  HOH A O    1 
HETATM 4427 O  O    . HOH E 5 .   ? 19.294 -15.018 48.169 1.000 8.88  ? 704  HOH A O    1 
HETATM 4428 O  O    . HOH E 5 .   ? 12.865 27.828  26.101 1.000 12.91 ? 705  HOH A O    1 
HETATM 4429 O  O    . HOH E 5 .   ? 4.473  11.641  37.442 1.000 8.67  ? 706  HOH A O    1 
HETATM 4430 O  O    . HOH E 5 .   ? 0.615  -8.516  45.977 1.000 34.17 ? 707  HOH A O    1 
HETATM 4431 O  O    . HOH E 5 .   ? 27.049 -9.295  54.045 1.000 11.04 ? 708  HOH A O    1 
HETATM 4432 O  O    . HOH E 5 .   ? 27.255 0.247   25.223 1.000 20.52 ? 709  HOH A O    1 
HETATM 4433 O  O    . HOH E 5 .   ? 22.815 7.220   16.470 1.000 15.74 ? 710  HOH A O    1 
HETATM 4434 O  O    . HOH E 5 .   ? 4.633  2.503   27.272 1.000 15.75 ? 711  HOH A O    1 
HETATM 4435 O  O    . HOH E 5 .   ? 32.987 -7.782  55.471 1.000 32.75 ? 712  HOH A O    1 
HETATM 4436 O  O    . HOH E 5 .   ? 12.909 -4.743  32.691 1.000 9.33  ? 713  HOH A O    1 
HETATM 4437 O  O    . HOH E 5 .   ? 4.714  18.129  40.070 1.000 10.48 ? 714  HOH A O    1 
HETATM 4438 O  O    . HOH E 5 .   ? 6.418  22.577  26.920 1.000 9.52  ? 715  HOH A O    1 
HETATM 4439 O  O    . HOH E 5 .   ? 7.543  3.484   33.771 1.000 7.84  ? 716  HOH A O    1 
HETATM 4440 O  O    . HOH E 5 .   ? 31.813 11.189  43.675 1.000 11.56 ? 717  HOH A O    1 
HETATM 4441 O  O    . HOH E 5 .   ? 33.064 1.726   41.654 1.000 30.15 ? 718  HOH A O    1 
HETATM 4442 O  O    . HOH E 5 .   ? 13.640 -1.348  36.019 1.000 7.52  ? 719  HOH A O    1 
HETATM 4443 O  O    . HOH E 5 .   ? 15.396 -18.849 27.483 1.000 37.86 ? 720  HOH A O    1 
HETATM 4444 O  O    . HOH E 5 .   ? 31.362 -12.905 56.436 1.000 31.20 ? 721  HOH A O    1 
HETATM 4445 O  O    . HOH E 5 .   ? 12.650 19.049  49.516 1.000 8.84  ? 722  HOH A O    1 
HETATM 4446 O  O    . HOH E 5 .   ? 10.825 -15.924 53.066 1.000 30.90 ? 723  HOH A O    1 
HETATM 4447 O  O    . HOH E 5 .   ? 28.971 16.269  42.957 1.000 28.04 ? 724  HOH A O    1 
HETATM 4448 O  O    . HOH E 5 .   ? 28.051 10.147  42.645 1.000 10.59 ? 725  HOH A O    1 
HETATM 4449 O  O    . HOH E 5 .   ? 15.154 0.032   20.926 1.000 17.36 ? 726  HOH A O    1 
HETATM 4450 O  O    . HOH E 5 .   ? 30.366 16.349  30.637 1.000 7.68  ? 727  HOH A O    1 
HETATM 4451 O  O    . HOH E 5 .   ? 12.056 12.570  16.803 1.000 17.08 ? 728  HOH A O    1 
HETATM 4452 O  O    . HOH E 5 .   ? -2.681 10.133  39.574 1.000 21.79 ? 729  HOH A O    1 
HETATM 4453 O  O    . HOH E 5 .   ? -0.360 25.683  27.348 1.000 43.95 ? 730  HOH A O    1 
HETATM 4454 O  O    . HOH E 5 .   ? 18.754 8.673   48.702 1.000 17.55 ? 731  HOH A O    1 
HETATM 4455 O  O    . HOH E 5 .   ? 32.296 -6.108  22.709 1.000 22.05 ? 732  HOH A O    1 
HETATM 4456 O  O    . HOH E 5 .   ? 20.242 9.899   54.013 1.000 25.81 ? 733  HOH A O    1 
HETATM 4457 O  O    . HOH E 5 .   ? 4.402  1.763   31.995 1.000 21.79 ? 734  HOH A O    1 
HETATM 4458 O  O    . HOH E 5 .   ? 28.261 4.316   15.512 1.000 62.24 ? 735  HOH A O    1 
HETATM 4459 O  O    . HOH E 5 .   ? 21.185 25.591  34.595 1.000 40.13 ? 736  HOH A O    1 
HETATM 4460 O  O    . HOH E 5 .   ? 14.944 5.616   33.077 1.000 7.71  ? 737  HOH A O    1 
HETATM 4461 O  O    A HOH E 5 .   ? 24.635 24.913  27.225 0.751 18.20 ? 738  HOH A O    1 
HETATM 4462 O  O    B HOH E 5 .   ? 23.740 25.691  27.517 0.249 13.67 ? 738  HOH A O    1 
HETATM 4463 O  O    . HOH E 5 .   ? 15.174 9.131   28.870 1.000 5.73  ? 739  HOH A O    1 
HETATM 4464 O  O    . HOH E 5 .   ? 27.979 -11.446 26.876 1.000 22.98 ? 740  HOH A O    1 
HETATM 4465 O  O    . HOH E 5 .   ? 18.205 -0.334  24.821 1.000 11.54 ? 741  HOH A O    1 
HETATM 4466 O  O    . HOH E 5 .   ? -0.848 19.503  37.762 1.000 34.07 ? 742  HOH A O    1 
HETATM 4467 O  O    . HOH E 5 .   ? 3.141  20.011  29.862 1.000 9.74  ? 743  HOH A O    1 
HETATM 4468 O  O    . HOH E 5 .   ? 37.765 -0.981  42.347 1.000 28.27 ? 744  HOH A O    1 
HETATM 4469 O  O    . HOH E 5 .   ? 11.943 -3.107  26.736 1.000 12.31 ? 745  HOH A O    1 
HETATM 4470 O  O    . HOH E 5 .   ? 37.221 12.326  26.610 1.000 22.34 ? 746  HOH A O    1 
HETATM 4471 O  O    . HOH E 5 .   ? -2.438 18.242  33.853 1.000 40.36 ? 747  HOH A O    1 
HETATM 4472 O  O    . HOH E 5 .   ? 33.347 -15.318 48.157 1.000 30.43 ? 748  HOH A O    1 
HETATM 4473 O  O    . HOH E 5 .   ? 16.320 -1.285  50.130 1.000 8.40  ? 749  HOH A O    1 
HETATM 4474 O  O    . HOH E 5 .   ? 2.560  7.223   32.611 1.000 25.35 ? 750  HOH A O    1 
HETATM 4475 O  O    . HOH E 5 .   ? 5.256  0.237   45.253 1.000 35.74 ? 751  HOH A O    1 
HETATM 4476 O  O    . HOH E 5 .   ? 21.166 -10.176 20.008 1.000 37.19 ? 752  HOH A O    1 
HETATM 4477 O  O    . HOH E 5 .   ? 15.254 8.775   53.184 1.000 19.36 ? 753  HOH A O    1 
HETATM 4478 O  O    . HOH E 5 .   ? 8.348  25.892  31.288 1.000 24.87 ? 754  HOH A O    1 
HETATM 4479 O  O    . HOH E 5 .   ? 20.314 1.063   26.104 1.000 8.34  ? 755  HOH A O    1 
HETATM 4480 O  O    . HOH E 5 .   ? 37.770 -12.801 39.133 1.000 18.14 ? 756  HOH A O    1 
HETATM 4481 O  O    . HOH E 5 .   ? 16.404 7.749   34.406 1.000 7.30  ? 757  HOH A O    1 
HETATM 4482 O  O    . HOH E 5 .   ? 0.466  6.332   34.186 1.000 41.20 ? 758  HOH A O    1 
HETATM 4483 O  O    . HOH E 5 .   ? 25.671 -21.190 41.484 1.000 50.03 ? 759  HOH A O    1 
HETATM 4484 O  O    . HOH E 5 .   ? 23.079 -3.660  50.598 1.000 7.41  ? 760  HOH A O    1 
HETATM 4485 O  O    . HOH E 5 .   ? -2.967 9.855   19.457 1.000 41.52 ? 761  HOH A O    1 
HETATM 4486 O  O    . HOH E 5 .   ? 0.978  -6.037  46.072 1.000 30.87 ? 762  HOH A O    1 
HETATM 4487 O  O    . HOH E 5 .   ? 13.203 -8.005  57.608 1.000 10.72 ? 763  HOH A O    1 
HETATM 4488 O  O    . HOH E 5 .   ? 35.828 -13.835 51.195 1.000 38.71 ? 764  HOH A O    1 
HETATM 4489 O  O    . HOH E 5 .   ? 24.942 -2.247  24.486 1.000 36.26 ? 765  HOH A O    1 
HETATM 4490 O  O    . HOH E 5 .   ? 35.856 -15.326 32.329 1.000 20.53 ? 766  HOH A O    1 
HETATM 4491 O  O    . HOH E 5 .   ? 15.800 12.639  57.815 1.000 30.10 ? 767  HOH A O    1 
HETATM 4492 O  O    . HOH E 5 .   ? 41.663 11.134  38.028 1.000 14.32 ? 768  HOH A O    1 
HETATM 4493 O  O    . HOH E 5 .   ? 35.127 -19.610 37.696 1.000 18.86 ? 769  HOH A O    1 
HETATM 4494 O  O    . HOH E 5 .   ? 20.094 -1.855  31.408 1.000 6.67  ? 770  HOH A O    1 
HETATM 4495 O  O    . HOH E 5 .   ? 0.942  1.941   40.886 1.000 53.18 ? 771  HOH A O    1 
HETATM 4496 O  O    . HOH E 5 .   ? -2.012 19.215  40.093 1.000 19.42 ? 772  HOH A O    1 
HETATM 4497 O  O    . HOH E 5 .   ? 19.863 29.421  32.042 1.000 38.13 ? 773  HOH A O    1 
HETATM 4498 O  O    A HOH E 5 .   ? 16.228 8.501   49.975 0.751 15.19 ? 774  HOH A O    1 
HETATM 4499 O  O    B HOH E 5 .   ? 16.967 7.888   51.036 0.249 10.77 ? 774  HOH A O    1 
HETATM 4500 O  O    . HOH E 5 .   ? 31.906 7.567   25.254 1.000 12.21 ? 775  HOH A O    1 
HETATM 4501 O  O    . HOH E 5 .   ? 10.780 -14.760 46.279 1.000 35.46 ? 776  HOH A O    1 
HETATM 4502 O  O    . HOH E 5 .   ? 19.308 -8.819  35.759 1.000 7.41  ? 777  HOH A O    1 
HETATM 4503 O  O    . HOH E 5 .   ? 9.532  13.052  53.441 1.000 30.71 ? 778  HOH A O    1 
HETATM 4504 O  O    . HOH E 5 .   ? 25.322 -0.032  23.374 1.000 18.54 ? 779  HOH A O    1 
HETATM 4505 O  O    . HOH E 5 .   ? 17.463 0.113   29.127 1.000 9.93  ? 780  HOH A O    1 
HETATM 4506 O  O    . HOH E 5 .   ? 27.707 17.565  15.660 1.000 39.96 ? 781  HOH A O    1 
HETATM 4507 O  O    . HOH E 5 .   ? 28.488 1.846   53.024 1.000 50.08 ? 782  HOH A O    1 
HETATM 4508 O  O    . HOH E 5 .   ? 0.902  27.375  23.951 1.000 40.11 ? 783  HOH A O    1 
HETATM 4509 O  O    . HOH E 5 .   ? 15.426 -2.328  47.596 1.000 8.50  ? 784  HOH A O    1 
HETATM 4510 O  O    . HOH E 5 .   ? 12.689 -1.178  48.840 1.000 9.86  ? 785  HOH A O    1 
HETATM 4511 O  O    . HOH E 5 .   ? 14.837 -14.367 19.535 1.000 14.25 ? 786  HOH A O    1 
HETATM 4512 O  O    . HOH E 5 .   ? 23.211 27.576  35.704 1.000 24.86 ? 787  HOH A O    1 
HETATM 4513 O  O    . HOH E 5 .   ? 15.379 16.812  13.391 1.000 22.10 ? 788  HOH A O    1 
HETATM 4514 O  O    . HOH E 5 .   ? 3.666  -6.933  46.688 1.000 18.64 ? 789  HOH A O    1 
HETATM 4515 O  O    . HOH E 5 .   ? 21.845 -0.056  30.115 1.000 9.00  ? 790  HOH A O    1 
HETATM 4516 O  O    . HOH E 5 .   ? 12.867 -15.718 51.321 1.000 23.28 ? 791  HOH A O    1 
HETATM 4517 O  O    . HOH E 5 .   ? 16.268 0.392   32.922 1.000 6.31  ? 792  HOH A O    1 
HETATM 4518 O  O    . HOH E 5 .   ? 30.587 -21.123 36.212 1.000 31.42 ? 793  HOH A O    1 
HETATM 4519 O  O    . HOH E 5 .   ? 28.980 6.391   48.810 1.000 26.30 ? 794  HOH A O    1 
HETATM 4520 O  O    . HOH E 5 .   ? 37.767 12.390  38.918 1.000 9.34  ? 795  HOH A O    1 
HETATM 4521 O  O    . HOH E 5 .   ? 19.711 2.256   16.716 1.000 22.62 ? 796  HOH A O    1 
HETATM 4522 O  O    . HOH E 5 .   ? 20.153 -11.432 23.848 1.000 13.31 ? 797  HOH A O    1 
HETATM 4523 O  O    . HOH E 5 .   ? 0.617  14.589  18.543 1.000 23.68 ? 798  HOH A O    1 
HETATM 4524 O  O    A HOH E 5 .   ? 21.323 4.749   31.579 0.821 12.93 ? 799  HOH A O    1 
HETATM 4525 O  O    B HOH E 5 .   ? 21.301 4.084   30.469 0.179 5.92  ? 799  HOH A O    1 
HETATM 4526 O  O    . HOH E 5 .   ? 40.155 -12.325 34.914 1.000 26.64 ? 800  HOH A O    1 
HETATM 4527 O  O    . HOH E 5 .   ? 15.135 23.188  39.196 1.000 8.77  ? 801  HOH A O    1 
HETATM 4528 O  O    . HOH E 5 .   ? 40.427 -5.359  28.320 1.000 30.89 ? 802  HOH A O    1 
HETATM 4529 O  O    . HOH E 5 .   ? 7.629  7.233   44.567 1.000 15.10 ? 803  HOH A O    1 
HETATM 4530 O  O    . HOH E 5 .   ? 37.891 6.830   43.412 1.000 29.13 ? 804  HOH A O    1 
HETATM 4531 O  O    . HOH E 5 .   ? 32.974 -6.185  59.862 1.000 44.37 ? 805  HOH A O    1 
HETATM 4532 O  O    . HOH E 5 .   ? 8.595  22.454  37.232 1.000 14.05 ? 806  HOH A O    1 
HETATM 4533 O  O    . HOH E 5 .   ? 24.401 20.428  28.294 1.000 11.71 ? 807  HOH A O    1 
HETATM 4534 O  O    . HOH E 5 .   ? 21.513 -3.884  24.224 1.000 17.63 ? 808  HOH A O    1 
HETATM 4535 O  O    . HOH E 5 .   ? 14.589 27.229  30.237 1.000 18.16 ? 809  HOH A O    1 
HETATM 4536 O  O    . HOH E 5 .   ? 19.316 -17.695 24.491 1.000 14.93 ? 810  HOH A O    1 
HETATM 4537 O  O    . HOH E 5 .   ? -3.278 6.316   35.186 1.000 25.97 ? 811  HOH A O    1 
HETATM 4538 O  O    . HOH E 5 .   ? 22.556 14.740  41.534 1.000 9.92  ? 812  HOH A O    1 
HETATM 4539 O  O    A HOH E 5 .   ? 3.247  20.820  41.167 0.453 19.24 ? 813  HOH A O    1 
HETATM 4540 O  O    B HOH E 5 .   ? 4.290  20.978  40.090 0.547 29.06 ? 813  HOH A O    1 
HETATM 4541 O  O    . HOH E 5 .   ? 27.191 13.711  30.540 1.000 7.13  ? 814  HOH A O    1 
HETATM 4542 O  O    . HOH E 5 .   ? 21.141 -10.104 17.206 1.000 48.78 ? 815  HOH A O    1 
HETATM 4543 O  O    . HOH E 5 .   ? 20.253 25.108  38.767 1.000 31.20 ? 816  HOH A O    1 
HETATM 4544 O  O    . HOH E 5 .   ? 5.181  5.174   19.705 1.000 11.98 ? 817  HOH A O    1 
HETATM 4545 O  O    . HOH E 5 .   ? 21.638 -16.987 27.833 1.000 16.48 ? 818  HOH A O    1 
HETATM 4546 O  O    . HOH E 5 .   ? 16.771 24.086  41.345 1.000 14.05 ? 819  HOH A O    1 
HETATM 4547 O  O    . HOH E 5 .   ? 33.484 13.096  44.829 1.000 15.40 ? 820  HOH A O    1 
HETATM 4548 O  O    . HOH E 5 .   ? 28.059 11.291  17.551 1.000 17.82 ? 821  HOH A O    1 
HETATM 4549 O  O    . HOH E 5 .   ? 15.089 -2.536  21.252 1.000 38.30 ? 822  HOH A O    1 
HETATM 4550 O  O    . HOH E 5 .   ? 13.867 -17.178 29.096 1.000 23.94 ? 823  HOH A O    1 
HETATM 4551 O  O    . HOH E 5 .   ? 16.299 17.531  46.104 1.000 20.90 ? 824  HOH A O    1 
HETATM 4552 O  O    . HOH E 5 .   ? 32.108 -19.059 39.929 1.000 16.05 ? 825  HOH A O    1 
HETATM 4553 O  O    . HOH E 5 .   ? 16.987 -19.744 57.034 1.000 28.90 ? 826  HOH A O    1 
HETATM 4554 O  O    . HOH E 5 .   ? 6.531  -6.232  40.268 1.000 11.00 ? 827  HOH A O    1 
HETATM 4555 O  O    . HOH E 5 .   ? 16.245 18.140  57.184 1.000 34.95 ? 828  HOH A O    1 
HETATM 4556 O  O    . HOH E 5 .   ? 23.957 -14.048 24.220 1.000 19.57 ? 829  HOH A O    1 
HETATM 4557 O  O    . HOH E 5 .   ? 34.069 -2.780  51.365 1.000 20.92 ? 830  HOH A O    1 
HETATM 4558 O  O    . HOH E 5 .   ? 36.442 -4.111  30.579 1.000 16.22 ? 831  HOH A O    1 
HETATM 4559 O  O    . HOH E 5 .   ? 33.493 15.745  44.008 1.000 13.69 ? 832  HOH A O    1 
HETATM 4560 O  O    . HOH E 5 .   ? 40.241 5.460   32.245 1.000 31.63 ? 833  HOH A O    1 
HETATM 4561 O  O    A HOH E 5 .   ? 33.257 -2.090  33.806 0.656 19.77 ? 834  HOH A O    1 
HETATM 4562 O  O    B HOH E 5 .   ? 32.592 -3.144  32.363 0.344 14.88 ? 834  HOH A O    1 
HETATM 4563 O  O    . HOH E 5 .   ? 25.891 27.681  36.423 1.000 20.03 ? 835  HOH A O    1 
HETATM 4564 O  O    . HOH E 5 .   ? 19.855 -20.264 33.544 1.000 29.45 ? 836  HOH A O    1 
HETATM 4565 O  O    . HOH E 5 .   ? 19.732 -21.122 37.261 1.000 42.51 ? 837  HOH A O    1 
HETATM 4566 O  O    . HOH E 5 .   ? -2.676 18.043  36.453 1.000 18.74 ? 838  HOH A O    1 
HETATM 4567 O  O    . HOH E 5 .   ? -3.309 9.549   27.475 1.000 31.54 ? 839  HOH A O    1 
HETATM 4568 O  O    . HOH E 5 .   ? 26.119 0.880   54.832 1.000 14.88 ? 840  HOH A O    1 
HETATM 4569 O  O    . HOH E 5 .   ? 27.146 -19.971 50.676 1.000 26.74 ? 841  HOH A O    1 
HETATM 4570 O  O    . HOH E 5 .   ? 12.736 -3.771  30.162 1.000 12.93 ? 842  HOH A O    1 
HETATM 4571 O  O    . HOH E 5 .   ? 6.357  29.234  27.737 1.000 28.54 ? 843  HOH A O    1 
HETATM 4572 O  O    . HOH E 5 .   ? 20.221 19.348  40.536 1.000 13.62 ? 844  HOH A O    1 
HETATM 4573 O  O    . HOH E 5 .   ? 20.228 15.675  47.759 1.000 22.79 ? 845  HOH A O    1 
HETATM 4574 O  O    . HOH E 5 .   ? 24.949 13.283  44.101 1.000 36.29 ? 846  HOH A O    1 
HETATM 4575 O  O    . HOH E 5 .   ? 28.849 -0.250  29.598 1.000 14.17 ? 847  HOH A O    1 
HETATM 4576 O  O    . HOH E 5 .   ? -1.057 25.505  30.376 1.000 47.86 ? 848  HOH A O    1 
HETATM 4577 O  O    . HOH E 5 .   ? 1.679  -2.115  43.734 1.000 23.04 ? 849  HOH A O    1 
HETATM 4578 O  O    . HOH E 5 .   ? -1.677 22.261  26.176 1.000 30.73 ? 850  HOH A O    1 
HETATM 4579 O  O    A HOH E 5 .   ? 12.561 -6.812  26.441 0.541 21.34 ? 851  HOH A O    1 
HETATM 4580 O  O    B HOH E 5 .   ? 14.431 -6.410  25.030 0.459 32.39 ? 851  HOH A O    1 
HETATM 4581 O  O    . HOH E 5 .   ? -0.792 10.679  17.699 1.000 21.78 ? 852  HOH A O    1 
HETATM 4582 O  O    . HOH E 5 .   ? 28.851 25.898  31.085 1.000 48.85 ? 853  HOH A O    1 
HETATM 4583 O  O    . HOH E 5 .   ? 10.824 15.589  57.411 1.000 33.10 ? 854  HOH A O    1 
HETATM 4584 O  O    . HOH E 5 .   ? 17.978 6.349   32.748 1.000 20.45 ? 855  HOH A O    1 
HETATM 4585 O  O    . HOH E 5 .   ? 5.701  31.076  17.888 1.000 56.62 ? 856  HOH A O    1 
HETATM 4586 O  O    . HOH E 5 .   ? 25.181 5.419   54.364 1.000 32.28 ? 857  HOH A O    1 
HETATM 4587 O  O    . HOH E 5 .   ? 38.911 -1.007  39.857 1.000 31.53 ? 858  HOH A O    1 
HETATM 4588 O  O    . HOH E 5 .   ? 28.854 -15.085 35.660 1.000 11.70 ? 859  HOH A O    1 
HETATM 4589 O  O    . HOH E 5 .   ? 39.936 5.558   41.675 1.000 25.63 ? 860  HOH A O    1 
HETATM 4590 O  O    . HOH E 5 .   ? 33.481 -18.798 26.536 1.000 12.63 ? 861  HOH A O    1 
HETATM 4591 O  O    . HOH E 5 .   ? 16.837 -2.707  62.531 1.000 14.04 ? 862  HOH A O    1 
HETATM 4592 O  O    . HOH E 5 .   ? 6.435  25.190  26.616 1.000 16.35 ? 863  HOH A O    1 
HETATM 4593 O  O    A HOH E 5 .   ? 29.466 -22.223 41.631 0.502 17.45 ? 864  HOH A O    1 
HETATM 4594 O  O    B HOH E 5 .   ? 28.228 -22.282 42.072 0.498 18.81 ? 864  HOH A O    1 
HETATM 4595 O  O    . HOH E 5 .   ? 9.243  -16.180 43.986 1.000 30.63 ? 865  HOH A O    1 
HETATM 4596 O  O    . HOH E 5 .   ? 20.953 -0.296  61.916 1.000 53.71 ? 866  HOH A O    1 
HETATM 4597 O  O    . HOH E 5 .   ? 16.142 28.561  21.972 1.000 21.06 ? 867  HOH A O    1 
HETATM 4598 O  O    . HOH E 5 .   ? 9.611  14.923  55.209 1.000 41.00 ? 868  HOH A O    1 
HETATM 4599 O  O    . HOH E 5 .   ? 32.076 18.056  29.433 1.000 11.86 ? 869  HOH A O    1 
HETATM 4600 O  O    . HOH E 5 .   ? 28.287 -2.304  56.290 1.000 19.31 ? 870  HOH A O    1 
HETATM 4601 O  O    . HOH E 5 .   ? 41.260 -12.452 27.407 1.000 53.74 ? 871  HOH A O    1 
HETATM 4602 O  O    . HOH E 5 .   ? 18.625 -7.057  20.819 1.000 38.95 ? 872  HOH A O    1 
HETATM 4603 O  O    . HOH E 5 .   ? 7.632  8.813   16.703 1.000 9.13  ? 873  HOH A O    1 
HETATM 4604 O  O    . HOH E 5 .   ? 18.744 -2.831  24.398 1.000 24.12 ? 874  HOH A O    1 
HETATM 4605 O  O    . HOH E 5 .   ? -1.071 20.313  30.281 1.000 19.07 ? 875  HOH A O    1 
HETATM 4606 O  O    . HOH E 5 .   ? 34.403 -19.341 30.754 1.000 34.31 ? 876  HOH A O    1 
HETATM 4607 O  O    . HOH E 5 .   ? 31.244 3.455   19.673 1.000 44.63 ? 877  HOH A O    1 
HETATM 4608 O  O    . HOH E 5 .   ? 10.717 -9.711  33.410 1.000 28.76 ? 878  HOH A O    1 
HETATM 4609 O  O    . HOH E 5 .   ? 27.905 -19.076 53.425 1.000 60.92 ? 879  HOH A O    1 
HETATM 4610 O  O    . HOH E 5 .   ? 17.176 24.919  44.770 1.000 13.35 ? 880  HOH A O    1 
HETATM 4611 O  O    . HOH E 5 .   ? 16.302 -17.097 32.653 1.000 45.06 ? 881  HOH A O    1 
HETATM 4612 O  O    . HOH E 5 .   ? 4.028  -12.054 44.426 1.000 52.22 ? 882  HOH A O    1 
HETATM 4613 O  O    . HOH E 5 .   ? 5.554  20.481  28.463 1.000 9.65  ? 883  HOH A O    1 
HETATM 4614 O  O    . HOH E 5 .   ? 28.290 -10.859 21.789 1.000 26.75 ? 884  HOH A O    1 
HETATM 4615 O  O    . HOH E 5 .   ? 36.294 6.650   25.075 1.000 38.52 ? 885  HOH A O    1 
HETATM 4616 O  O    . HOH E 5 .   ? 42.574 4.428   33.966 1.000 83.49 ? 886  HOH A O    1 
HETATM 4617 O  O    . HOH E 5 .   ? 30.176 13.336  17.880 1.000 44.97 ? 887  HOH A O    1 
HETATM 4618 O  O    . HOH E 5 .   ? 5.345  10.087  51.810 1.000 30.11 ? 888  HOH A O    1 
HETATM 4619 O  O    . HOH E 5 .   ? 9.842  -16.510 34.107 1.000 46.00 ? 889  HOH A O    1 
HETATM 4620 O  O    . HOH E 5 .   ? 38.439 15.808  28.039 1.000 47.56 ? 890  HOH A O    1 
HETATM 4621 O  O    . HOH E 5 .   ? 30.163 -11.977 58.562 1.000 31.67 ? 891  HOH A O    1 
HETATM 4622 O  O    . HOH E 5 .   ? 12.509 -18.679 36.411 1.000 36.35 ? 892  HOH A O    1 
HETATM 4623 O  O    . HOH E 5 .   ? 15.176 27.720  34.797 1.000 49.40 ? 893  HOH A O    1 
HETATM 4624 O  O    . HOH E 5 .   ? 26.598 -21.445 44.815 1.000 46.93 ? 894  HOH A O    1 
HETATM 4625 O  O    . HOH E 5 .   ? 4.484  -9.815  56.302 1.000 48.64 ? 895  HOH A O    1 
HETATM 4626 O  O    . HOH E 5 .   ? 16.812 3.962   34.435 1.000 8.51  ? 896  HOH A O    1 
HETATM 4627 O  O    . HOH E 5 .   ? 24.314 -0.855  61.335 1.000 63.77 ? 897  HOH A O    1 
HETATM 4628 O  O    . HOH E 5 .   ? 14.154 19.964  53.398 1.000 17.35 ? 898  HOH A O    1 
HETATM 4629 O  O    . HOH E 5 .   ? -2.093 22.890  29.644 1.000 43.52 ? 899  HOH A O    1 
HETATM 4630 O  O    . HOH E 5 .   ? 17.167 1.064   61.457 1.000 34.10 ? 900  HOH A O    1 
HETATM 4631 O  O    A HOH E 5 .   ? 18.913 3.477   32.656 0.806 10.92 ? 901  HOH A O    1 
HETATM 4632 O  O    B HOH E 5 .   ? 17.897 3.982   31.844 0.194 7.50  ? 901  HOH A O    1 
HETATM 4633 O  O    . HOH E 5 .   ? 5.394  6.629   45.745 1.000 18.70 ? 902  HOH A O    1 
HETATM 4634 O  O    . HOH E 5 .   ? 21.235 -8.717  22.762 1.000 38.04 ? 903  HOH A O    1 
HETATM 4635 O  O    . HOH E 5 .   ? 4.905  -8.194  38.843 1.000 15.03 ? 904  HOH A O    1 
HETATM 4636 O  O    . HOH E 5 .   ? 35.978 1.422   41.547 1.000 51.56 ? 905  HOH A O    1 
HETATM 4637 O  O    . HOH E 5 .   ? 24.711 -5.321  61.928 1.000 22.78 ? 906  HOH A O    1 
HETATM 4638 O  O    . HOH E 5 .   ? 5.397  -0.879  23.604 1.000 23.58 ? 907  HOH A O    1 
HETATM 4639 O  O    . HOH E 5 .   ? 26.427 -2.742  45.140 1.000 13.53 ? 908  HOH A O    1 
HETATM 4640 O  O    . HOH E 5 .   ? 12.543 8.169   51.881 1.000 29.23 ? 909  HOH A O    1 
HETATM 4641 O  O    . HOH E 5 .   ? 26.051 0.328   20.777 1.000 36.70 ? 910  HOH A O    1 
HETATM 4642 O  O    . HOH E 5 .   ? 15.365 5.284   55.819 1.000 40.26 ? 911  HOH A O    1 
HETATM 4643 O  O    . HOH E 5 .   ? 29.018 9.264   16.174 1.000 30.47 ? 912  HOH A O    1 
HETATM 4644 O  O    . HOH E 5 .   ? 8.903  -10.473 35.639 1.000 47.05 ? 913  HOH A O    1 
HETATM 4645 O  O    . HOH E 5 .   ? 5.142  0.406   21.237 1.000 22.90 ? 914  HOH A O    1 
HETATM 4646 O  O    . HOH E 5 .   ? 15.392 -18.615 49.636 1.000 33.01 ? 915  HOH A O    1 
HETATM 4647 O  O    . HOH E 5 .   ? 30.142 6.304   44.995 1.000 48.54 ? 916  HOH A O    1 
HETATM 4648 O  O    . HOH E 5 .   ? 38.166 8.382   27.113 1.000 61.14 ? 917  HOH A O    1 
HETATM 4649 O  O    . HOH E 5 .   ? -6.949 13.488  32.469 1.000 37.62 ? 918  HOH A O    1 
HETATM 4650 O  O    . HOH E 5 .   ? 31.011 -0.804  31.619 1.000 24.32 ? 919  HOH A O    1 
HETATM 4651 O  O    . HOH E 5 .   ? 18.807 18.008  46.612 1.000 39.79 ? 920  HOH A O    1 
HETATM 4652 O  O    . HOH E 5 .   ? 16.714 -21.515 37.820 1.000 28.75 ? 921  HOH A O    1 
HETATM 4653 O  O    . HOH E 5 .   ? 32.859 -2.760  56.293 1.000 45.21 ? 922  HOH A O    1 
HETATM 4654 O  O    . HOH E 5 .   ? 15.927 -12.039 13.913 1.000 34.78 ? 923  HOH A O    1 
HETATM 4655 O  O    . HOH E 5 .   ? 14.994 1.029   17.525 1.000 46.38 ? 924  HOH A O    1 
HETATM 4656 O  O    . HOH E 5 .   ? 37.538 12.113  20.408 1.000 42.70 ? 925  HOH A O    1 
HETATM 4657 O  O    . HOH E 5 .   ? 16.314 20.157  55.276 1.000 40.98 ? 926  HOH A O    1 
HETATM 4658 O  O    . HOH E 5 .   ? 33.249 6.013   44.244 1.000 30.28 ? 927  HOH A O    1 
HETATM 4659 O  O    . HOH E 5 .   ? 30.475 -1.286  56.368 1.000 47.12 ? 928  HOH A O    1 
HETATM 4660 O  O    . HOH E 5 .   ? 4.965  15.441  15.972 1.000 22.03 ? 929  HOH A O    1 
HETATM 4661 O  O    . HOH E 5 .   ? 0.606  6.768   18.717 1.000 13.12 ? 930  HOH A O    1 
HETATM 4662 O  O    . HOH E 5 .   ? 14.033 14.588  58.846 1.000 40.44 ? 931  HOH A O    1 
HETATM 4663 O  O    . HOH E 5 .   ? 34.809 -14.115 55.564 1.000 40.84 ? 932  HOH A O    1 
HETATM 4664 O  O    . HOH E 5 .   ? 49.442 -6.839  30.498 1.000 40.25 ? 933  HOH A O    1 
HETATM 4665 O  O    . HOH E 5 .   ? 5.453  -9.995  40.890 1.000 17.09 ? 934  HOH A O    1 
HETATM 4666 O  O    . HOH E 5 .   ? 13.150 28.214  31.847 1.000 31.15 ? 935  HOH A O    1 
HETATM 4667 O  O    . HOH E 5 .   ? 35.062 16.051  21.364 1.000 26.72 ? 936  HOH A O    1 
HETATM 4668 O  O    A HOH E 5 .   ? 15.060 -0.692  29.139 0.589 8.11  ? 937  HOH A O    1 
HETATM 4669 O  O    B HOH E 5 .   ? 14.512 0.066   29.700 0.411 18.31 ? 937  HOH A O    1 
HETATM 4670 O  O    . HOH E 5 .   ? 4.842  8.604   41.876 1.000 14.51 ? 938  HOH A O    1 
HETATM 4671 O  O    . HOH E 5 .   ? 3.065  28.971  22.340 1.000 34.75 ? 939  HOH A O    1 
HETATM 4672 O  O    . HOH E 5 .   ? 8.722  -11.098 29.916 1.000 30.72 ? 940  HOH A O    1 
HETATM 4673 O  O    . HOH E 5 .   ? -3.440 11.852  24.499 1.000 40.29 ? 941  HOH A O    1 
HETATM 4674 O  O    . HOH E 5 .   ? 34.187 6.650   21.495 1.000 19.03 ? 942  HOH A O    1 
HETATM 4675 O  O    . HOH E 5 .   ? 42.502 -7.580  26.976 1.000 58.26 ? 943  HOH A O    1 
HETATM 4676 O  O    . HOH E 5 .   ? 33.398 17.915  20.708 1.000 51.26 ? 944  HOH A O    1 
HETATM 4677 O  O    . HOH E 5 .   ? 6.145  -9.441  36.617 1.000 55.60 ? 945  HOH A O    1 
HETATM 4678 O  O    . HOH E 5 .   ? 30.288 -0.688  27.418 1.000 20.69 ? 946  HOH A O    1 
HETATM 4679 O  O    . HOH E 5 .   ? 40.138 -0.830  43.666 1.000 35.61 ? 947  HOH A O    1 
HETATM 4680 O  O    . HOH E 5 .   ? 37.815 -16.665 31.282 1.000 32.57 ? 948  HOH A O    1 
HETATM 4681 O  O    . HOH E 5 .   ? 16.755 2.195   30.980 1.000 14.52 ? 949  HOH A O    1 
HETATM 4682 O  O    . HOH E 5 .   ? 25.110 22.357  30.235 1.000 13.21 ? 950  HOH A O    1 
HETATM 4683 O  O    . HOH E 5 .   ? -3.069 18.913  31.301 1.000 18.73 ? 951  HOH A O    1 
HETATM 4684 O  O    . HOH E 5 .   ? 21.818 -14.634 25.841 1.000 20.38 ? 952  HOH A O    1 
HETATM 4685 O  O    . HOH E 5 .   ? 10.680 -10.544 25.808 1.000 39.21 ? 953  HOH A O    1 
HETATM 4686 O  O    . HOH E 5 .   ? 21.013 -21.456 39.502 1.000 33.98 ? 954  HOH A O    1 
HETATM 4687 O  O    . HOH E 5 .   ? 12.400 -3.509  58.737 1.000 16.83 ? 955  HOH A O    1 
HETATM 4688 O  O    . HOH E 5 .   ? 26.795 -6.868  62.891 1.000 42.20 ? 956  HOH A O    1 
HETATM 4689 O  O    . HOH E 5 .   ? 23.754 -6.709  23.474 1.000 32.06 ? 957  HOH A O    1 
HETATM 4690 O  O    . HOH E 5 .   ? 11.988 6.246   49.647 1.000 27.94 ? 958  HOH A O    1 
HETATM 4691 O  O    . HOH E 5 .   ? -3.064 8.290   40.890 1.000 71.64 ? 959  HOH A O    1 
HETATM 4692 O  O    . HOH E 5 .   ? 35.016 1.205   45.668 1.000 53.98 ? 960  HOH A O    1 
HETATM 4693 O  O    . HOH E 5 .   ? -4.316 17.103  25.139 1.000 23.28 ? 961  HOH A O    1 
HETATM 4694 O  O    . HOH E 5 .   ? 17.958 -16.944 46.712 1.000 21.89 ? 962  HOH A O    1 
HETATM 4695 O  O    . HOH E 5 .   ? 14.337 -21.312 41.858 1.000 38.70 ? 963  HOH A O    1 
HETATM 4696 O  O    A HOH E 5 .   ? -3.336 6.926   26.413 0.591 34.07 ? 964  HOH A O    1 
HETATM 4697 O  O    B HOH E 5 .   ? -2.030 5.005   27.506 0.409 30.65 ? 964  HOH A O    1 
HETATM 4698 O  O    . HOH E 5 .   ? 24.158 -11.247 23.803 1.000 54.76 ? 965  HOH A O    1 
HETATM 4699 O  O    . HOH E 5 .   ? 12.717 -18.021 49.671 1.000 18.19 ? 966  HOH A O    1 
HETATM 4700 O  O    . HOH E 5 .   ? 19.836 1.524   28.727 1.000 9.20  ? 967  HOH A O    1 
HETATM 4701 O  O    . HOH E 5 .   ? 12.506 -6.290  23.768 1.000 34.04 ? 968  HOH A O    1 
HETATM 4702 O  O    . HOH E 5 .   ? 12.246 0.757   59.632 1.000 30.40 ? 969  HOH A O    1 
HETATM 4703 O  O    . HOH E 5 .   ? 15.941 -20.049 24.112 1.000 25.01 ? 970  HOH A O    1 
HETATM 4704 O  O    . HOH E 5 .   ? 1.063  1.909   45.129 1.000 42.75 ? 971  HOH A O    1 
HETATM 4705 O  O    . HOH E 5 .   ? 6.493  24.138  16.625 1.000 26.41 ? 972  HOH A O    1 
HETATM 4706 O  O    . HOH E 5 .   ? 10.170 -12.625 28.280 1.000 33.93 ? 973  HOH A O    1 
HETATM 4707 O  O    . HOH E 5 .   ? 32.921 -9.726  61.125 1.000 46.26 ? 974  HOH A O    1 
HETATM 4708 O  O    . HOH E 5 .   ? 30.835 9.709   45.691 1.000 41.96 ? 975  HOH A O    1 
HETATM 4709 O  O    . HOH E 5 .   ? 23.015 -21.990 37.911 1.000 30.59 ? 976  HOH A O    1 
HETATM 4710 O  O    . HOH E 5 .   ? 5.711  27.094  28.273 1.000 45.68 ? 977  HOH A O    1 
HETATM 4711 O  O    . HOH E 5 .   ? 29.882 -2.877  25.906 1.000 26.10 ? 978  HOH A O    1 
HETATM 4712 O  O    A HOH E 5 .   ? 19.610 4.181   29.199 0.802 10.56 ? 979  HOH A O    1 
HETATM 4713 O  O    B HOH E 5 .   ? 19.853 4.418   30.505 0.198 7.32  ? 979  HOH A O    1 
HETATM 4714 O  O    . HOH E 5 .   ? 6.460  -3.155  23.171 1.000 24.24 ? 980  HOH A O    1 
HETATM 4715 O  O    . HOH E 5 .   ? 10.948 -7.928  21.928 1.000 52.55 ? 981  HOH A O    1 
HETATM 4716 O  O    . HOH E 5 .   ? 4.232  30.578  26.742 1.000 36.66 ? 982  HOH A O    1 
HETATM 4717 O  O    . HOH E 5 .   ? -2.962 12.025  43.461 1.000 31.13 ? 983  HOH A O    1 
HETATM 4718 O  O    . HOH E 5 .   ? 13.061 -10.550 19.069 1.000 36.83 ? 984  HOH A O    1 
HETATM 4719 O  O    . HOH E 5 .   ? 45.242 -5.401  42.555 1.000 39.15 ? 985  HOH A O    1 
HETATM 4720 O  O    . HOH E 5 .   ? 21.673 -14.063 58.421 1.000 31.51 ? 986  HOH A O    1 
HETATM 4721 O  O    . HOH E 5 .   ? 33.419 -0.395  50.083 1.000 23.20 ? 987  HOH A O    1 
HETATM 4722 O  O    . HOH E 5 .   ? 18.028 3.760   58.565 1.000 21.88 ? 988  HOH A O    1 
HETATM 4723 O  O    . HOH E 5 .   ? 37.543 -17.494 28.656 1.000 35.71 ? 989  HOH A O    1 
HETATM 4724 O  O    . HOH E 5 .   ? 12.973 15.224  13.741 1.000 25.05 ? 990  HOH A O    1 
HETATM 4725 O  O    . HOH E 5 .   ? 14.278 30.238  26.330 1.000 56.90 ? 991  HOH A O    1 
HETATM 4726 O  O    . HOH E 5 .   ? -1.702 15.667  18.201 1.000 32.91 ? 992  HOH A O    1 
HETATM 4727 O  O    . HOH E 5 .   ? 36.909 17.187  22.856 1.000 32.07 ? 993  HOH A O    1 
HETATM 4728 O  O    . HOH E 5 .   ? 11.002 -4.140  24.547 1.000 33.14 ? 994  HOH A O    1 
HETATM 4729 O  O    . HOH E 5 .   ? 27.073 -23.617 37.614 1.000 42.39 ? 995  HOH A O    1 
HETATM 4730 O  O    . HOH E 5 .   ? 15.379 -16.929 18.351 1.000 12.24 ? 996  HOH A O    1 
HETATM 4731 O  O    . HOH E 5 .   ? 13.584 12.918  14.257 1.000 19.47 ? 997  HOH A O    1 
HETATM 4732 O  O    . HOH E 5 .   ? -1.134 9.761   44.496 1.000 49.28 ? 998  HOH A O    1 
HETATM 4733 O  O    . HOH E 5 .   ? 39.081 14.607  25.616 1.000 44.69 ? 999  HOH A O    1 
HETATM 4734 O  O    . HOH E 5 .   ? 4.449  -0.694  26.433 1.000 33.64 ? 1000 HOH A O    1 
HETATM 4735 O  O    . HOH E 5 .   ? 14.000 -17.760 31.958 1.000 28.23 ? 1001 HOH A O    1 
HETATM 4736 O  O    . HOH E 5 .   ? -5.108 11.205  26.434 1.000 21.77 ? 1002 HOH A O    1 
HETATM 4737 O  O    . HOH E 5 .   ? 31.395 9.840   50.194 1.000 38.82 ? 1003 HOH A O    1 
HETATM 4738 O  O    . HOH E 5 .   ? 30.434 -2.451  23.376 1.000 45.73 ? 1004 HOH A O    1 
HETATM 4739 O  O    . HOH E 5 .   ? -8.094 13.132  28.887 1.000 17.89 ? 1005 HOH A O    1 
HETATM 4740 O  O    . HOH E 5 .   ? 36.136 -15.341 47.251 1.000 36.77 ? 1006 HOH A O    1 
HETATM 4741 O  O    . HOH E 5 .   ? 47.928 -0.828  26.893 1.000 59.93 ? 1007 HOH A O    1 
HETATM 4742 O  O    . HOH E 5 .   ? 31.151 16.452  44.874 1.000 17.03 ? 1008 HOH A O    1 
HETATM 4743 O  O    . HOH E 5 .   ? 34.222 -0.378  29.820 1.000 47.25 ? 1009 HOH A O    1 
HETATM 4744 O  O    . HOH E 5 .   ? 3.950  4.185   31.552 1.000 24.50 ? 1010 HOH A O    1 
HETATM 4745 O  O    . HOH E 5 .   ? 4.957  3.949   45.989 1.000 40.12 ? 1011 HOH A O    1 
HETATM 4746 O  O    . HOH E 5 .   ? 2.289  5.043   20.135 1.000 14.61 ? 1012 HOH A O    1 
HETATM 4747 O  O    . HOH E 5 .   ? 4.240  0.803   29.182 1.000 46.84 ? 1013 HOH A O    1 
HETATM 4748 O  O    . HOH E 5 .   ? 2.633  -0.057  45.716 1.000 46.60 ? 1014 HOH A O    1 
HETATM 4749 O  O    . HOH E 5 .   ? 3.898  30.964  24.122 1.000 26.24 ? 1015 HOH A O    1 
HETATM 4750 O  O    A HOH E 5 .   ? 21.285 -3.901  19.962 0.258 18.79 ? 1016 HOH A O    1 
HETATM 4751 O  O    B HOH E 5 .   ? 23.083 -3.013  19.937 0.742 29.50 ? 1016 HOH A O    1 
HETATM 4752 O  O    . HOH E 5 .   ? 9.141  17.899  14.251 1.000 36.00 ? 1017 HOH A O    1 
HETATM 4753 O  O    . HOH E 5 .   ? 37.355 -4.415  27.918 1.000 38.63 ? 1018 HOH A O    1 
HETATM 4754 O  O    . HOH E 5 .   ? -3.974 16.777  29.619 1.000 21.74 ? 1019 HOH A O    1 
HETATM 4755 O  O    . HOH E 5 .   ? 10.068 -7.916  26.631 1.000 23.33 ? 1020 HOH A O    1 
HETATM 4756 O  O    . HOH E 5 .   ? 6.886  -14.683 45.939 1.000 50.06 ? 1021 HOH A O    1 
HETATM 4757 O  O    . HOH E 5 .   ? 6.103  27.078  31.170 1.000 32.80 ? 1022 HOH A O    1 
HETATM 4758 O  O    . HOH E 5 .   ? 1.269  6.177   43.332 1.000 31.52 ? 1023 HOH A O    1 
HETATM 4759 O  O    . HOH E 5 .   ? 39.724 11.134  22.077 1.000 48.74 ? 1024 HOH A O    1 
HETATM 4760 O  O    . HOH E 5 .   ? 34.637 -7.690  61.383 1.000 28.34 ? 1025 HOH A O    1 
HETATM 4761 O  O    . HOH E 5 .   ? 3.892  27.433  32.845 1.000 38.69 ? 1026 HOH A O    1 
HETATM 4762 O  O    . HOH E 5 .   ? 31.778 11.068  16.317 1.000 59.62 ? 1027 HOH A O    1 
HETATM 4763 O  O    . HOH E 5 .   ? 31.367 -22.486 48.055 1.000 40.49 ? 1028 HOH A O    1 
HETATM 4764 O  O    . HOH E 5 .   ? 7.794  -4.634  24.948 1.000 47.90 ? 1029 HOH A O    1 
HETATM 4765 O  O    . HOH E 5 .   ? 13.225 -12.829 17.776 1.000 25.91 ? 1030 HOH A O    1 
HETATM 4766 O  O    . HOH E 5 .   ? 16.567 -19.269 47.654 1.000 39.79 ? 1031 HOH A O    1 
HETATM 4767 O  O    . HOH E 5 .   ? 3.694  7.627   44.076 1.000 28.44 ? 1032 HOH A O    1 
HETATM 4768 O  O    . HOH E 5 .   ? 18.886 -21.170 48.347 1.000 47.07 ? 1033 HOH A O    1 
HETATM 4769 O  O    . HOH E 5 .   ? 1.320  0.797   29.261 1.000 47.40 ? 1034 HOH A O    1 
HETATM 4770 O  O    A HOH E 5 .   ? 19.405 5.821   59.571 0.228 19.55 ? 1035 HOH A O    1 
HETATM 4771 O  O    B HOH E 5 .   ? 21.473 6.449   58.943 0.772 39.45 ? 1035 HOH A O    1 
HETATM 4772 O  O    . HOH E 5 .   ? 27.792 -25.026 43.125 1.000 42.23 ? 1036 HOH A O    1 
HETATM 4773 O  O    . HOH E 5 .   ? 33.268 19.790  22.859 1.000 21.94 ? 1037 HOH A O    1 
HETATM 4774 O  O    . HOH E 5 .   ? 34.917 12.679  16.011 1.000 42.72 ? 1038 HOH A O    1 
HETATM 4775 O  O    . HOH E 5 .   ? -3.690 14.562  16.832 1.000 49.18 ? 1039 HOH A O    1 
HETATM 4776 O  O    . HOH E 5 .   ? 14.971 -16.059 15.791 1.000 16.80 ? 1040 HOH A O    1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N  N   . ALA A 1   ? 0.4323 0.4155 0.8258 -0.0516 0.1449  -0.3833 1    ALA A N   
2    C  CA  . ALA A 1   ? 0.5722 0.2533 0.6809 -0.0798 0.3413  -0.1369 1    ALA A CA  
3    C  C   . ALA A 1   ? 0.4304 0.2793 0.5718 0.0224  0.2486  0.0092  1    ALA A C   
4    O  O   . ALA A 1   ? 0.4909 0.3013 0.6864 0.1098  0.2368  0.1609  1    ALA A O   
5    C  CB  . ALA A 1   ? 0.6366 0.4082 0.5446 -0.3275 0.3461  -0.2383 1    ALA A CB  
6    N  N   . PRO A 2   ? 0.3976 0.3072 0.4291 -0.0280 0.1183  -0.0784 2    PRO A N   
7    C  CA  . PRO A 2   ? 0.3639 0.0958 0.3988 0.0147  0.0944  -0.0009 2    PRO A CA  
8    C  C   . PRO A 2   ? 0.2558 0.1362 0.3731 0.0357  0.1033  0.0160  2    PRO A C   
9    O  O   . PRO A 2   ? 0.3150 0.1854 0.4276 -0.0085 0.1382  0.0177  2    PRO A O   
10   C  CB  . PRO A 2   ? 0.3408 0.1613 0.3453 -0.0146 0.0452  0.0231  2    PRO A CB  
11   C  CG  . PRO A 2   ? 0.4716 0.2923 0.3838 0.0775  0.0518  -0.0866 2    PRO A CG  
12   C  CD  . PRO A 2   ? 0.5408 0.2430 0.3640 -0.0682 0.0971  -0.0835 2    PRO A CD  
13   N  N   . PRO A 3   ? 0.3432 0.1174 0.3347 -0.0157 0.0785  0.0655  3    PRO A N   
14   C  CA  . PRO A 3   ? 0.2666 0.1057 0.3449 0.0179  0.0819  0.0698  3    PRO A CA  
15   C  C   . PRO A 3   ? 0.1691 0.1088 0.2735 0.0258  0.0484  0.0544  3    PRO A C   
16   O  O   . PRO A 3   ? 0.1608 0.1358 0.3454 0.0226  0.0179  0.0590  3    PRO A O   
17   C  CB  . PRO A 3   ? 0.2919 0.1915 0.3125 -0.0381 0.0418  0.0949  3    PRO A CB  
18   C  CG  . PRO A 3   ? 0.3493 0.2286 0.3382 -0.0842 0.0090  0.1240  3    PRO A CG  
19   C  CD  . PRO A 3   ? 0.3463 0.3206 0.3034 -0.1037 0.0485  0.0650  3    PRO A CD  
20   N  N   . LYS A 4   ? 0.1470 0.1266 0.3344 0.0283  0.0354  0.0822  4    LYS A N   
21   C  CA  A LYS A 4   ? 0.1444 0.1134 0.2374 0.0333  0.0115  0.0545  4    LYS A CA  
22   C  CA  B LYS A 4   ? 0.1227 0.1169 0.2790 0.0263  0.0242  0.0778  4    LYS A CA  
23   C  C   . LYS A 4   ? 0.1359 0.1314 0.2466 0.0327  0.0325  0.0971  4    LYS A C   
24   O  O   . LYS A 4   ? 0.2038 0.1415 0.2435 0.0527  0.0560  0.1036  4    LYS A O   
25   C  CB  A LYS A 4   ? 0.1374 0.1482 0.2433 0.0313  -0.0073 0.1039  4    LYS A CB  
26   C  CB  B LYS A 4   ? 0.1440 0.1597 0.2611 0.0301  0.0071  0.0795  4    LYS A CB  
27   C  CG  A LYS A 4   ? 0.1291 0.2027 0.3224 -0.0045 0.0397  0.0629  4    LYS A CG  
28   C  CG  B LYS A 4   ? 0.1141 0.1823 0.3127 0.0266  0.0012  0.0942  4    LYS A CG  
29   C  CD  A LYS A 4   ? 0.1354 0.2080 0.3610 0.0121  -0.0030 0.1063  4    LYS A CD  
30   C  CD  B LYS A 4   ? 0.1486 0.1441 0.3679 0.0344  -0.0046 0.0439  4    LYS A CD  
31   C  CE  A LYS A 4   ? 0.2589 0.2262 0.2578 -0.0114 0.0547  0.0070  4    LYS A CE  
32   C  CE  B LYS A 4   ? 0.1236 0.2143 0.3382 -0.0158 -0.0269 0.0606  4    LYS A CE  
33   N  NZ  A LYS A 4   ? 0.2999 0.2894 0.4261 -0.0727 0.0811  -0.0701 4    LYS A NZ  
34   N  NZ  B LYS A 4   ? 0.1688 0.2087 0.2916 -0.0143 -0.0346 0.0275  4    LYS A NZ  
35   N  N   . SER A 5   ? 0.1252 0.1035 0.1418 0.0241  0.0152  0.0396  5    SER A N   
36   C  CA  . SER A 5   ? 0.1202 0.0919 0.1165 0.0034  0.0094  0.0249  5    SER A CA  
37   C  C   . SER A 5   ? 0.1066 0.0912 0.0778 0.0022  0.0001  0.0211  5    SER A C   
38   O  O   . SER A 5   ? 0.1107 0.0949 0.1163 0.0093  0.0207  0.0158  5    SER A O   
39   C  CB  . SER A 5   ? 0.1140 0.1030 0.1145 0.0020  0.0083  0.0194  5    SER A CB  
40   O  OG  . SER A 5   ? 0.1263 0.1165 0.0946 0.0098  0.0003  0.0149  5    SER A OG  
44   N  N   . VAL A 6   ? 0.0949 0.0865 0.0964 0.0138  0.0002  0.0235  6    VAL A N   
45   C  CA  . VAL A 6   ? 0.0823 0.0950 0.0863 0.0008  0.0024  0.0210  6    VAL A CA  
46   C  C   . VAL A 6   ? 0.0880 0.0924 0.0752 0.0079  0.0131  0.0184  6    VAL A C   
47   O  O   . VAL A 6   ? 0.0870 0.1026 0.0923 -0.0005 0.0072  0.0228  6    VAL A O   
48   C  CB  . VAL A 6   ? 0.1398 0.0978 0.0860 0.0162  -0.0032 0.0050  6    VAL A CB  
49   C  CG1 . VAL A 6   ? 0.1917 0.1132 0.1081 -0.0277 -0.0272 0.0119  6    VAL A CG1 
50   C  CG2 . VAL A 6   ? 0.1296 0.1756 0.0905 -0.0062 -0.0293 0.0176  6    VAL A CG2 
53   N  N   . ILE A 7   ? 0.0782 0.0801 0.0677 0.0023  0.0049  0.0072  7    ILE A N   
54   C  CA  . ILE A 7   ? 0.0814 0.0844 0.0701 0.0030  0.0015  0.0062  7    ILE A CA  
55   C  C   . ILE A 7   ? 0.0814 0.0784 0.0662 0.0034  0.0064  0.0076  7    ILE A C   
56   O  O   . ILE A 7   ? 0.0790 0.0854 0.0844 -0.0009 0.0053  -0.0054 7    ILE A O   
57   C  CB  . ILE A 7   ? 0.0845 0.0806 0.0770 0.0034  -0.0038 0.0075  7    ILE A CB  
58   C  CG1 . ILE A 7   ? 0.1153 0.1105 0.0683 -0.0129 0.0091  0.0053  7    ILE A CG1 
59   C  CG2 . ILE A 7   ? 0.1181 0.0863 0.0799 0.0081  0.0016  -0.0083 7    ILE A CG2 
60   C  CD1 . ILE A 7   ? 0.1227 0.0942 0.0783 -0.0041 0.0042  0.0170  7    ILE A CD1 
65   N  N   . ARG A 8   ? 0.0832 0.0751 0.0654 -0.0035 0.0015  0.0103  8    ARG A N   
66   C  CA  . ARG A 8   ? 0.0831 0.0801 0.0588 0.0086  -0.0046 0.0035  8    ARG A CA  
67   C  C   . ARG A 8   ? 0.0732 0.0714 0.0521 0.0068  0.0007  0.0023  8    ARG A C   
68   O  O   . ARG A 8   ? 0.0768 0.0960 0.0703 -0.0046 -0.0040 0.0240  8    ARG A O   
69   C  CB  . ARG A 8   ? 0.0795 0.1051 0.0582 0.0075  -0.0051 0.0053  8    ARG A CB  
70   C  CG  . ARG A 8   ? 0.0952 0.1341 0.0587 0.0005  -0.0083 0.0161  8    ARG A CG  
71   C  CD  . ARG A 8   ? 0.1009 0.1638 0.0575 0.0000  -0.0062 0.0139  8    ARG A CD  
72   N  NE  . ARG A 8   ? 0.1010 0.1319 0.0686 0.0042  0.0082  0.0228  8    ARG A NE  
73   C  CZ  . ARG A 8   ? 0.1029 0.1253 0.0700 0.0077  0.0091  0.0299  8    ARG A CZ  
74   N  NH1 . ARG A 8   ? 0.1131 0.2097 0.0781 -0.0302 0.0223  0.0064  8    ARG A NH1 
75   N  NH2 . ARG A 8   ? 0.1059 0.1199 0.0787 0.0013  0.0108  0.0231  8    ARG A NH2 
85   N  N   . TRP A 9   ? 0.0781 0.0660 0.0581 -0.0007 -0.0086 0.0052  9    TRP A N   
86   C  CA  . TRP A 9   ? 0.0727 0.0636 0.0560 -0.0005 -0.0066 0.0047  9    TRP A CA  
87   C  C   . TRP A 9   ? 0.0709 0.0807 0.0557 0.0093  -0.0116 0.0013  9    TRP A C   
88   O  O   . TRP A 9   ? 0.1064 0.0977 0.0797 0.0200  -0.0377 -0.0206 9    TRP A O   
89   C  CB  . TRP A 9   ? 0.0670 0.0832 0.0598 -0.0064 -0.0025 0.0011  9    TRP A CB  
90   C  CG  . TRP A 9   ? 0.0651 0.0720 0.0558 -0.0079 0.0037  0.0029  9    TRP A CG  
91   C  CD1 . TRP A 9   ? 0.0803 0.0695 0.0660 0.0004  0.0021  0.0006  9    TRP A CD1 
92   C  CD2 . TRP A 9   ? 0.0673 0.0776 0.0531 0.0022  0.0051  0.0035  9    TRP A CD2 
93   N  NE1 . TRP A 9   ? 0.0838 0.0715 0.0577 0.0049  0.0015  0.0050  9    TRP A NE1 
94   C  CE2 . TRP A 9   ? 0.0727 0.0746 0.0535 0.0058  0.0025  0.0027  9    TRP A CE2 
95   C  CE3 . TRP A 9   ? 0.0743 0.0762 0.0567 0.0066  0.0035  0.0037  9    TRP A CE3 
96   C  CZ2 . TRP A 9   ? 0.0708 0.0889 0.0579 0.0026  0.0009  -0.0018 9    TRP A CZ2 
97   C  CZ3 . TRP A 9   ? 0.0821 0.0824 0.0657 0.0128  0.0041  -0.0030 9    TRP A CZ3 
98   C  CH2 . TRP A 9   ? 0.0806 0.0880 0.0595 -0.0015 0.0020  -0.0102 9    TRP A CH2 
108  N  N   . CYS A 10  ? 0.0802 0.0658 0.0471 0.0041  -0.0071 0.0025  10   CYS A N   
109  C  CA  . CYS A 10  ? 0.0747 0.0649 0.0568 0.0041  -0.0075 0.0012  10   CYS A CA  
110  C  C   . CYS A 10  ? 0.0732 0.0635 0.0565 0.0091  -0.0056 -0.0034 10   CYS A C   
111  O  O   . CYS A 10  ? 0.0907 0.0730 0.0548 -0.0044 -0.0133 0.0019  10   CYS A O   
112  C  CB  . CYS A 10  ? 0.0839 0.0759 0.0595 0.0056  0.0016  0.0037  10   CYS A CB  
113  S  SG  . CYS A 10  ? 0.0926 0.0991 0.0630 0.0158  0.0041  -0.0019 10   CYS A SG  
118  N  N   . THR A 11  ? 0.0830 0.0687 0.0489 0.0039  -0.0064 0.0010  11   THR A N   
119  C  CA  . THR A 11  ? 0.0903 0.0675 0.0491 0.0052  0.0004  -0.0024 11   THR A CA  
120  C  C   . THR A 11  ? 0.0960 0.0723 0.0546 0.0084  -0.0062 -0.0071 11   THR A C   
121  O  O   . THR A 11  ? 0.0972 0.0769 0.0553 0.0126  -0.0006 -0.0004 11   THR A O   
122  C  CB  . THR A 11  ? 0.0880 0.0762 0.0573 0.0031  -0.0080 -0.0004 11   THR A CB  
123  O  OG1 . THR A 11  ? 0.0847 0.0907 0.0653 0.0121  -0.0126 -0.0168 11   THR A OG1 
124  C  CG2 . THR A 11  ? 0.1023 0.0885 0.0773 0.0111  0.0065  -0.0137 11   THR A CG2 
129  N  N   . ILE A 12  ? 0.0812 0.0655 0.0601 0.0121  -0.0015 0.0009  12   ILE A N   
130  C  CA  . ILE A 12  ? 0.0965 0.0628 0.0733 0.0125  -0.0016 -0.0007 12   ILE A CA  
131  C  C   . ILE A 12  ? 0.1023 0.0725 0.0680 0.0116  -0.0133 -0.0025 12   ILE A C   
132  O  O   . ILE A 12  ? 0.1056 0.0694 0.0973 0.0142  -0.0115 -0.0088 12   ILE A O   
133  C  CB  . ILE A 12  ? 0.0844 0.0784 0.0788 0.0082  -0.0071 0.0043  12   ILE A CB  
134  C  CG1 . ILE A 12  ? 0.0943 0.0823 0.0741 0.0117  -0.0159 0.0015  12   ILE A CG1 
135  C  CG2 . ILE A 12  ? 0.0967 0.0923 0.1037 -0.0104 -0.0009 -0.0051 12   ILE A CG2 
136  C  CD1 . ILE A 12  ? 0.1131 0.0928 0.0809 0.0099  -0.0051 0.0060  12   ILE A CD1 
145  N  N   . SER A 13  ? 0.1001 0.0659 0.0820 0.0090  -0.0196 -0.0103 13   SER A N   
146  C  CA  . SER A 13  ? 0.1031 0.0731 0.0973 0.0104  -0.0240 -0.0145 13   SER A CA  
147  C  C   . SER A 13  ? 0.0947 0.0754 0.0807 0.0040  -0.0165 -0.0104 13   SER A C   
148  O  O   . SER A 13  ? 0.0981 0.0783 0.0797 0.0100  -0.0179 -0.0161 13   SER A O   
149  C  CB  . SER A 13  ? 0.0991 0.0749 0.1045 0.0092  -0.0232 -0.0063 13   SER A CB  
150  O  OG  . SER A 13  ? 0.0998 0.0808 0.0972 0.0158  -0.0241 -0.0057 13   SER A OG  
155  N  N   . SER A 14  ? 0.1135 0.0898 0.1027 0.0093  -0.0331 -0.0206 14   SER A N   
156  C  CA  . SER A 14  ? 0.1042 0.0913 0.1094 -0.0026 -0.0320 -0.0287 14   SER A CA  
157  C  C   . SER A 14  ? 0.1089 0.0806 0.0980 -0.0068 -0.0300 -0.0200 14   SER A C   
158  O  O   . SER A 14  ? 0.0942 0.0869 0.0978 0.0019  -0.0218 -0.0131 14   SER A O   
159  C  CB  . SER A 14  ? 0.1321 0.1353 0.1443 -0.0066 -0.0244 -0.0729 14   SER A CB  
160  O  OG  . SER A 14  ? 0.1907 0.2154 0.1789 -0.0529 0.0231  -0.1120 14   SER A OG  
164  N  N   . PRO A 15  ? 0.1164 0.0755 0.1058 -0.0009 -0.0349 -0.0112 15   PRO A N   
165  C  CA  . PRO A 15  ? 0.1096 0.0833 0.1087 -0.0130 -0.0134 -0.0061 15   PRO A CA  
166  C  C   . PRO A 15  ? 0.1012 0.0738 0.0783 -0.0115 -0.0187 -0.0018 15   PRO A C   
167  O  O   . PRO A 15  ? 0.0907 0.0803 0.0891 -0.0045 -0.0126 0.0014  15   PRO A O   
168  C  CB  . PRO A 15  ? 0.1549 0.0814 0.1187 -0.0176 -0.0213 0.0036  15   PRO A CB  
169  C  CG  . PRO A 15  ? 0.1654 0.0855 0.1436 -0.0129 -0.0380 0.0082  15   PRO A CG  
170  C  CD  . PRO A 15  ? 0.1341 0.0700 0.1423 0.0044  -0.0310 -0.0049 15   PRO A CD  
175  N  N   . GLU A 16  ? 0.0872 0.0794 0.0706 -0.0012 -0.0144 -0.0005 16   GLU A N   
176  C  CA  . GLU A 16  ? 0.0805 0.0765 0.0620 0.0005  -0.0133 -0.0110 16   GLU A CA  
177  C  C   . GLU A 16  ? 0.0711 0.0797 0.0586 -0.0044 -0.0124 -0.0081 16   GLU A C   
178  O  O   . GLU A 16  ? 0.0762 0.0787 0.0636 0.0045  -0.0063 -0.0046 16   GLU A O   
179  C  CB  . GLU A 16  ? 0.0750 0.0923 0.0687 0.0018  -0.0180 -0.0154 16   GLU A CB  
180  C  CG  . GLU A 16  ? 0.0911 0.0854 0.0762 0.0020  -0.0214 0.0013  16   GLU A CG  
181  C  CD  . GLU A 16  ? 0.0848 0.0785 0.0637 0.0013  -0.0047 -0.0122 16   GLU A CD  
182  O  OE1 . GLU A 16  ? 0.0757 0.0957 0.0650 0.0036  -0.0049 -0.0142 16   GLU A OE1 
183  O  OE2 . GLU A 16  ? 0.0834 0.0794 0.0646 0.0039  -0.0118 -0.0084 16   GLU A OE2 
186  N  N   . GLU A 17  ? 0.0894 0.0790 0.0608 0.0051  -0.0118 -0.0089 17   GLU A N   
187  C  CA  . GLU A 17  ? 0.0917 0.0820 0.0603 0.0097  -0.0134 -0.0048 17   GLU A CA  
188  C  C   . GLU A 17  ? 0.0875 0.0804 0.0596 0.0015  -0.0131 -0.0111 17   GLU A C   
189  O  O   . GLU A 17  ? 0.1013 0.0956 0.0630 0.0182  -0.0181 -0.0078 17   GLU A O   
190  C  CB  . GLU A 17  ? 0.1070 0.0999 0.0604 0.0175  -0.0152 -0.0049 17   GLU A CB  
191  C  CG  . GLU A 17  ? 0.1318 0.1102 0.0615 0.0150  -0.0084 -0.0010 17   GLU A CG  
192  C  CD  . GLU A 17  ? 0.1181 0.0971 0.0777 0.0207  -0.0228 0.0035  17   GLU A CD  
193  O  OE1 . GLU A 17  ? 0.1216 0.1184 0.0769 0.0114  -0.0175 -0.0034 17   GLU A OE1 
194  O  OE2 . GLU A 17  ? 0.1347 0.1275 0.0805 -0.0069 -0.0269 0.0095  17   GLU A OE2 
200  N  N   . LYS A 18  ? 0.0887 0.0908 0.0661 0.0067  -0.0152 -0.0094 18   LYS A N   
201  C  CA  . LYS A 18  ? 0.0828 0.0962 0.0718 0.0033  -0.0180 -0.0163 18   LYS A CA  
202  C  C   . LYS A 18  ? 0.0754 0.0837 0.0664 -0.0048 -0.0117 -0.0047 18   LYS A C   
203  O  O   . LYS A 18  ? 0.0862 0.0931 0.0731 -0.0001 -0.0161 -0.0070 18   LYS A O   
204  C  CB  . LYS A 18  ? 0.1022 0.0924 0.0949 -0.0005 -0.0214 -0.0145 18   LYS A CB  
205  C  CG  . LYS A 18  ? 0.1056 0.1189 0.1496 -0.0202 -0.0113 0.0059  18   LYS A CG  
206  C  CD  . LYS A 18  ? 0.1328 0.1253 0.3373 -0.0284 0.0244  0.0026  18   LYS A CD  
207  C  CE  . LYS A 18  ? 0.1354 0.2419 0.5152 -0.0599 0.0653  -0.0243 18   LYS A CE  
208  N  NZ  . LYS A 18  ? 0.2521 0.2933 0.6851 -0.1539 -0.0023 0.1169  18   LYS A NZ  
215  N  N   . LYS A 19  ? 0.0732 0.0807 0.0598 -0.0063 -0.0133 -0.0074 19   LYS A N   
216  C  CA  . LYS A 19  ? 0.0717 0.0732 0.0589 -0.0020 -0.0001 -0.0043 19   LYS A CA  
217  C  C   . LYS A 19  ? 0.0718 0.0810 0.0558 -0.0029 -0.0122 -0.0042 19   LYS A C   
218  O  O   . LYS A 19  ? 0.0809 0.0805 0.0586 0.0042  -0.0014 -0.0038 19   LYS A O   
219  C  CB  . LYS A 19  ? 0.0826 0.0781 0.0560 -0.0041 -0.0004 -0.0048 19   LYS A CB  
220  C  CG  . LYS A 19  ? 0.0687 0.0765 0.0594 0.0015  -0.0049 -0.0019 19   LYS A CG  
221  C  CD  . LYS A 19  ? 0.0690 0.0750 0.0639 -0.0030 -0.0059 0.0019  19   LYS A CD  
222  C  CE  . LYS A 19  ? 0.0688 0.0865 0.0567 0.0092  -0.0033 -0.0057 19   LYS A CE  
223  N  NZ  . LYS A 19  ? 0.0680 0.0891 0.0523 0.0055  -0.0019 -0.0102 19   LYS A NZ  
236  N  N   . CYS A 20  ? 0.0682 0.0832 0.0536 0.0001  -0.0068 0.0025  20   CYS A N   
237  C  CA  . CYS A 20  ? 0.0765 0.0783 0.0531 0.0064  -0.0087 -0.0019 20   CYS A CA  
238  C  C   . CYS A 20  ? 0.0702 0.0764 0.0539 0.0030  -0.0041 0.0016  20   CYS A C   
239  O  O   . CYS A 20  ? 0.0697 0.0827 0.0633 0.0069  -0.0077 -0.0040 20   CYS A O   
240  C  CB  . CYS A 20  ? 0.0760 0.0842 0.0602 0.0074  -0.0039 0.0063  20   CYS A CB  
241  S  SG  . CYS A 20  ? 0.0793 0.0888 0.0763 -0.0021 0.0014  -0.0017 20   CYS A SG  
244  N  N   . ASN A 21  ? 0.0706 0.0831 0.0565 0.0037  -0.0108 0.0030  21   ASN A N   
245  C  CA  . ASN A 21  ? 0.0711 0.0835 0.0575 0.0046  -0.0152 0.0024  21   ASN A CA  
246  C  C   . ASN A 21  ? 0.0721 0.0809 0.0596 -0.0004 -0.0120 -0.0070 21   ASN A C   
247  O  O   . ASN A 21  ? 0.0791 0.1023 0.0721 0.0106  -0.0122 -0.0001 21   ASN A O   
248  C  CB  . ASN A 21  ? 0.0817 0.0974 0.0560 0.0048  -0.0185 -0.0051 21   ASN A CB  
249  C  CG  . ASN A 21  ? 0.0911 0.0985 0.0509 0.0103  -0.0204 -0.0083 21   ASN A CG  
250  O  OD1 . ASN A 21  ? 0.0949 0.0991 0.0716 -0.0035 -0.0050 -0.0031 21   ASN A OD1 
251  N  ND2 . ASN A 21  ? 0.1152 0.0974 0.0706 0.0087  -0.0076 -0.0066 21   ASN A ND2 
257  N  N   . ASN A 22  ? 0.0796 0.0974 0.0560 -0.0019 -0.0054 -0.0094 22   ASN A N   
258  C  CA  . ASN A 22  ? 0.0756 0.0985 0.0710 0.0055  -0.0051 -0.0071 22   ASN A CA  
259  C  C   . ASN A 22  ? 0.0719 0.0991 0.0724 0.0007  0.0054  -0.0045 22   ASN A C   
260  O  O   . ASN A 22  ? 0.0863 0.1141 0.0882 0.0146  -0.0017 -0.0177 22   ASN A O   
261  C  CB  A ASN A 22  ? 0.1225 0.0921 0.0890 0.0094  0.0362  -0.0076 22   ASN A CB  
262  C  CB  B ASN A 22  ? 0.0626 0.1109 0.0893 -0.0121 -0.0070 0.0120  22   ASN A CB  
263  C  CG  A ASN A 22  ? 0.2094 0.1312 0.1401 -0.0542 0.0332  -0.0066 22   ASN A CG  
264  C  CG  B ASN A 22  ? 0.0831 0.1111 0.0883 -0.0029 0.0096  -0.0180 22   ASN A CG  
265  O  OD1 A ASN A 22  ? 0.4474 0.2186 0.1611 -0.2127 -0.0576 0.0311  22   ASN A OD1 
266  O  OD1 B ASN A 22  ? 0.1175 0.1600 0.1189 0.0365  0.0138  -0.0085 22   ASN A OD1 
267  N  ND2 A ASN A 22  ? 0.1145 0.1220 0.3126 -0.0352 0.0381  0.0444  22   ASN A ND2 
268  N  ND2 B ASN A 22  ? 0.0871 0.1244 0.1064 0.0028  0.0298  0.0031  22   ASN A ND2 
271  N  N   . LEU A 23  ? 0.0813 0.0929 0.0624 0.0037  -0.0057 -0.0086 23   LEU A N   
272  C  CA  . LEU A 23  ? 0.0808 0.0978 0.0617 0.0080  -0.0044 -0.0104 23   LEU A CA  
273  C  C   . LEU A 23  ? 0.0754 0.0949 0.0679 0.0019  -0.0119 -0.0135 23   LEU A C   
274  O  O   . LEU A 23  ? 0.0929 0.0941 0.0777 0.0210  -0.0115 -0.0201 23   LEU A O   
275  C  CB  . LEU A 23  ? 0.0812 0.0927 0.0610 -0.0028 -0.0054 0.0008  23   LEU A CB  
276  C  CG  . LEU A 23  ? 0.1149 0.0997 0.0589 -0.0150 -0.0137 -0.0013 23   LEU A CG  
277  C  CD1 . LEU A 23  ? 0.1570 0.1049 0.0657 -0.0168 0.0028  -0.0153 23   LEU A CD1 
278  C  CD2 . LEU A 23  ? 0.1148 0.1393 0.0746 -0.0315 -0.0246 0.0064  23   LEU A CD2 
288  N  N   . ARG A 24  ? 0.0812 0.0830 0.0660 0.0138  -0.0124 -0.0117 24   ARG A N   
289  C  CA  . ARG A 24  ? 0.0817 0.0820 0.0657 0.0078  -0.0120 -0.0080 24   ARG A CA  
290  C  C   . ARG A 24  ? 0.0850 0.0946 0.0660 0.0139  -0.0092 -0.0167 24   ARG A C   
291  O  O   . ARG A 24  ? 0.0939 0.0948 0.0848 0.0220  -0.0133 -0.0104 24   ARG A O   
292  C  CB  . ARG A 24  ? 0.0763 0.0882 0.0642 0.0023  -0.0104 -0.0083 24   ARG A CB  
293  C  CG  . ARG A 24  ? 0.1058 0.0909 0.0701 0.0033  -0.0152 -0.0138 24   ARG A CG  
294  C  CD  . ARG A 24  ? 0.0995 0.1064 0.0773 0.0052  -0.0150 -0.0179 24   ARG A CD  
295  N  NE  . ARG A 24  ? 0.0960 0.1132 0.0721 -0.0002 -0.0102 -0.0286 24   ARG A NE  
296  C  CZ  . ARG A 24  ? 0.0814 0.0977 0.0722 0.0071  -0.0155 -0.0127 24   ARG A CZ  
297  N  NH1 . ARG A 24  ? 0.1108 0.1098 0.0562 0.0154  -0.0110 -0.0096 24   ARG A NH1 
298  N  NH2 . ARG A 24  ? 0.1128 0.1233 0.0688 -0.0117 -0.0103 -0.0161 24   ARG A NH2 
309  N  N   . ASP A 25  ? 0.0754 0.1082 0.0774 0.0144  -0.0129 -0.0124 25   ASP A N   
310  C  CA  . ASP A 25  ? 0.0728 0.1345 0.0783 0.0166  -0.0146 -0.0129 25   ASP A CA  
311  C  C   . ASP A 25  ? 0.0806 0.1234 0.0823 0.0123  -0.0075 -0.0089 25   ASP A C   
312  O  O   . ASP A 25  ? 0.1362 0.2009 0.0985 0.0856  -0.0159 -0.0127 25   ASP A O   
313  C  CB  . ASP A 25  ? 0.0857 0.1287 0.0964 0.0131  -0.0124 -0.0228 25   ASP A CB  
314  C  CG  . ASP A 25  ? 0.0827 0.1841 0.1298 0.0281  -0.0349 -0.0632 25   ASP A CG  
315  O  OD1 . ASP A 25  ? 0.1174 0.1765 0.2306 0.0188  -0.0347 -0.0926 25   ASP A OD1 
316  O  OD2 . ASP A 25  ? 0.1026 0.2469 0.1114 0.0404  -0.0184 -0.0726 25   ASP A OD2 
320  N  N   . LEU A 26  ? 0.0745 0.1193 0.0763 0.0120  -0.0022 -0.0180 26   LEU A N   
321  C  CA  . LEU A 26  ? 0.0961 0.1206 0.0818 0.0158  0.0021  -0.0171 26   LEU A CA  
322  C  C   . LEU A 26  ? 0.0781 0.1120 0.1035 0.0185  -0.0048 -0.0225 26   LEU A C   
323  O  O   . LEU A 26  ? 0.1007 0.1264 0.1259 0.0260  0.0081  -0.0302 26   LEU A O   
324  C  CB  . LEU A 26  ? 0.1471 0.1297 0.0795 0.0265  0.0019  -0.0139 26   LEU A CB  
325  C  CG  . LEU A 26  ? 0.1631 0.1302 0.1014 0.0158  0.0449  -0.0077 26   LEU A CG  
326  C  CD1 . LEU A 26  ? 0.3374 0.1557 0.0865 0.0230  0.0135  0.0011  26   LEU A CD1 
327  C  CD2 . LEU A 26  ? 0.1781 0.2635 0.2744 0.0369  0.1284  0.0386  26   LEU A CD2 
331  N  N   . THR A 27  ? 0.1006 0.1005 0.0979 0.0203  -0.0022 -0.0225 27   THR A N   
332  C  CA  . THR A 27  ? 0.0929 0.1004 0.0991 0.0176  0.0006  -0.0165 27   THR A CA  
333  C  C   . THR A 27  ? 0.1032 0.1091 0.1147 0.0297  -0.0080 -0.0079 27   THR A C   
334  O  O   . THR A 27  ? 0.1096 0.0987 0.1377 0.0169  -0.0067 -0.0045 27   THR A O   
335  C  CB  . THR A 27  ? 0.0958 0.1008 0.1037 0.0180  -0.0010 -0.0156 27   THR A CB  
336  O  OG1 . THR A 27  ? 0.0976 0.1059 0.0972 0.0241  0.0023  -0.0135 27   THR A OG1 
337  C  CG2 . THR A 27  ? 0.1073 0.1351 0.0919 0.0256  -0.0040 -0.0274 27   THR A CG2 
341  N  N   . GLN A 28  ? 0.1315 0.1150 0.1074 0.0120  -0.0118 -0.0052 28   GLN A N   
342  C  CA  A GLN A 28  ? 0.1867 0.1663 0.1081 0.0166  -0.0125 0.0120  28   GLN A CA  
343  C  CA  B GLN A 28  ? 0.1357 0.1631 0.1133 -0.0013 -0.0106 0.0082  28   GLN A CA  
344  C  C   . GLN A 28  ? 0.1805 0.1692 0.1143 0.0008  -0.0194 0.0401  28   GLN A C   
345  O  O   . GLN A 28  ? 0.2393 0.2011 0.1663 -0.0298 -0.0016 0.0479  28   GLN A O   
346  C  CB  A GLN A 28  ? 0.2630 0.1935 0.1164 0.0022  -0.0500 -0.0177 28   GLN A CB  
347  C  CB  B GLN A 28  ? 0.1357 0.2000 0.1099 -0.0302 -0.0255 0.0243  28   GLN A CB  
348  C  CG  A GLN A 28  ? 0.1851 0.1807 0.1714 0.0109  -0.0404 -0.0082 28   GLN A CG  
349  C  CG  B GLN A 28  ? 0.1401 0.2021 0.1117 0.0260  -0.0137 0.0242  28   GLN A CG  
350  C  CD  A GLN A 28  ? 0.2372 0.2153 0.2102 -0.0489 -0.0018 -0.0233 28   GLN A CD  
351  C  CD  B GLN A 28  ? 0.1475 0.2304 0.1455 0.0010  -0.0020 0.0106  28   GLN A CD  
352  O  OE1 A GLN A 28  ? 0.2270 0.3966 0.2863 0.1120  0.0566  0.2204  28   GLN A OE1 
353  O  OE1 B GLN A 28  ? 0.1876 0.2572 0.3971 0.0911  0.0438  -0.0063 28   GLN A OE1 
354  N  NE2 A GLN A 28  ? 0.3464 0.2998 0.2812 -0.0156 -0.0181 0.1320  28   GLN A NE2 
355  N  NE2 B GLN A 28  ? 0.2511 0.3065 0.1872 -0.1253 0.0319  -0.0263 28   GLN A NE2 
356  N  N   . GLN A 29  ? 0.1109 0.1476 0.1876 0.0147  -0.0299 0.0288  29   GLN A N   
357  C  CA  . GLN A 29  ? 0.1496 0.1657 0.2440 0.0258  -0.0621 0.0440  29   GLN A CA  
358  C  C   . GLN A 29  ? 0.1567 0.1201 0.2889 0.0223  -0.0546 0.0343  29   GLN A C   
359  O  O   . GLN A 29  ? 0.1848 0.1325 0.4112 0.0484  -0.0980 0.0290  29   GLN A O   
360  C  CB  A GLN A 29  ? 0.1428 0.1840 0.4799 0.0472  -0.0691 0.0107  29   GLN A CB  
361  C  CB  B GLN A 29  ? 0.1430 0.2092 0.4243 0.0633  -0.0859 0.0035  29   GLN A CB  
362  C  CG  A GLN A 29  ? 0.1373 0.3590 0.5476 0.0730  -0.1574 -0.1144 29   GLN A CG  
363  C  CG  B GLN A 29  ? 0.1720 0.3820 0.5421 0.0918  -0.1448 -0.1163 29   GLN A CG  
364  C  CD  A GLN A 29  ? 0.3635 0.4645 0.5361 0.0843  -0.1663 -0.1266 29   GLN A CD  
365  C  CD  B GLN A 29  ? 0.2863 0.3893 0.5669 0.0463  -0.2113 -0.1374 29   GLN A CD  
366  O  OE1 A GLN A 29  ? 0.4452 0.7253 0.4635 0.1570  -0.3295 0.0320  29   GLN A OE1 
367  O  OE1 B GLN A 29  ? 0.5298 0.3927 0.5534 -0.0279 -0.1904 -0.1431 29   GLN A OE1 
368  N  NE2 A GLN A 29  ? 0.4824 0.4314 0.7066 0.2365  -0.2871 -0.2273 29   GLN A NE2 
369  N  NE2 B GLN A 29  ? 0.3390 0.3099 0.5294 0.2233  -0.2683 -0.1125 29   GLN A NE2 
370  N  N   . GLU A 30  ? 0.1011 0.1112 0.2163 0.0174  -0.0167 0.0099  30   GLU A N   
371  C  CA  . GLU A 30  ? 0.1065 0.0883 0.2114 0.0192  0.0119  -0.0066 30   GLU A CA  
372  C  C   . GLU A 30  ? 0.1342 0.0931 0.2125 0.0193  0.0333  -0.0063 30   GLU A C   
373  O  O   . GLU A 30  ? 0.1491 0.1277 0.1965 0.0116  0.0036  0.0118  30   GLU A O   
374  C  CB  . GLU A 30  ? 0.1240 0.1201 0.1523 0.0235  0.0042  -0.0189 30   GLU A CB  
375  C  CG  . GLU A 30  ? 0.1238 0.1195 0.1520 0.0074  0.0063  -0.0343 30   GLU A CG  
376  C  CD  . GLU A 30  ? 0.1543 0.1148 0.1949 0.0240  0.0407  -0.0175 30   GLU A CD  
377  O  OE1 . GLU A 30  ? 0.1745 0.1429 0.1611 0.0160  0.0340  -0.0104 30   GLU A OE1 
378  O  OE2 . GLU A 30  ? 0.1933 0.1490 0.3492 -0.0063 0.0966  -0.0858 30   GLU A OE2 
383  N  N   . ARG A 31  ? 0.1025 0.1032 0.2332 0.0205  0.0189  -0.0096 31   ARG A N   
384  C  CA  . ARG A 31  ? 0.1233 0.0875 0.2259 0.0260  0.0133  -0.0065 31   ARG A CA  
385  C  C   . ARG A 31  ? 0.1164 0.0838 0.1517 0.0190  0.0173  0.0094  31   ARG A C   
386  O  O   . ARG A 31  ? 0.1412 0.0914 0.1523 0.0269  0.0073  0.0302  31   ARG A O   
387  C  CB  . ARG A 31  ? 0.1441 0.0825 0.2233 0.0174  0.0383  -0.0204 31   ARG A CB  
388  C  CG  . ARG A 31  ? 0.1449 0.0937 0.2193 0.0194  0.0134  0.0164  31   ARG A CG  
389  C  CD  . ARG A 31  ? 0.1499 0.1184 0.2462 -0.0059 0.0228  -0.0015 31   ARG A CD  
390  N  NE  . ARG A 31  ? 0.1701 0.1351 0.2442 0.0076  0.0107  -0.0333 31   ARG A NE  
391  C  CZ  . ARG A 31  ? 0.1717 0.1078 0.2062 0.0293  0.0328  -0.0051 31   ARG A CZ  
392  N  NH1 . ARG A 31  ? 0.1894 0.1374 0.2180 -0.0109 0.0157  0.0193  31   ARG A NH1 
393  N  NH2 . ARG A 31  ? 0.1845 0.1761 0.1937 0.0250  0.0098  -0.0238 31   ARG A NH2 
398  N  N   . ILE A 32  ? 0.1301 0.0760 0.1312 0.0166  0.0197  0.0066  32   ILE A N   
399  C  CA  . ILE A 32  ? 0.1155 0.0778 0.0878 0.0204  0.0140  0.0002  32   ILE A CA  
400  C  C   . ILE A 32  ? 0.0965 0.0839 0.0760 0.0277  0.0085  0.0152  32   ILE A C   
401  O  O   . ILE A 32  ? 0.1037 0.1056 0.0891 0.0168  0.0200  0.0136  32   ILE A O   
402  C  CB  . ILE A 32  ? 0.1056 0.0968 0.0965 0.0020  0.0255  -0.0020 32   ILE A CB  
403  C  CG1 . ILE A 32  ? 0.1339 0.0945 0.1155 -0.0028 0.0233  -0.0151 32   ILE A CG1 
404  C  CG2 . ILE A 32  ? 0.0954 0.1001 0.0837 0.0194  0.0141  0.0040  32   ILE A CG2 
405  C  CD1 . ILE A 32  ? 0.1312 0.1133 0.1288 -0.0122 0.0064  0.0064  32   ILE A CD1 
411  N  N   . SER A 33  ? 0.0912 0.0796 0.0929 0.0105  0.0155  0.0093  33   SER A N   
412  C  CA  . SER A 33  ? 0.0996 0.0729 0.0953 0.0165  0.0102  0.0106  33   SER A CA  
413  C  C   . SER A 33  ? 0.0815 0.0763 0.0817 0.0055  0.0185  0.0073  33   SER A C   
414  O  O   . SER A 33  ? 0.0842 0.0797 0.0915 0.0069  0.0090  0.0089  33   SER A O   
415  C  CB  . SER A 33  ? 0.0940 0.0874 0.1310 0.0003  -0.0109 0.0190  33   SER A CB  
416  O  OG  . SER A 33  ? 0.1180 0.1461 0.1123 0.0069  0.0015  0.0133  33   SER A OG  
421  N  N   . LEU A 34  ? 0.0893 0.0753 0.0866 0.0083  -0.0038 0.0003  34   LEU A N   
422  C  CA  . LEU A 34  ? 0.0793 0.0828 0.0740 0.0060  -0.0003 -0.0009 34   LEU A CA  
423  C  C   . LEU A 34  ? 0.0930 0.0786 0.0675 0.0110  -0.0115 0.0040  34   LEU A C   
424  O  O   . LEU A 34  ? 0.0855 0.0955 0.0951 0.0137  -0.0141 -0.0069 34   LEU A O   
425  C  CB  . LEU A 34  ? 0.0880 0.0904 0.0730 0.0123  0.0006  0.0027  34   LEU A CB  
426  C  CG  . LEU A 34  ? 0.0826 0.0754 0.0758 0.0018  0.0055  -0.0010 34   LEU A CG  
427  C  CD1 . LEU A 34  ? 0.0822 0.1197 0.0935 0.0156  -0.0102 0.0181  34   LEU A CD1 
428  C  CD2 . LEU A 34  ? 0.1090 0.0839 0.0823 0.0025  0.0060  -0.0007 34   LEU A CD2 
437  N  N   . THR A 35  ? 0.0877 0.0753 0.0662 0.0045  -0.0039 -0.0002 35   THR A N   
438  C  CA  . THR A 35  ? 0.0941 0.0719 0.0646 0.0025  -0.0083 -0.0013 35   THR A CA  
439  C  C   . THR A 35  ? 0.0781 0.0785 0.0533 0.0026  0.0023  -0.0012 35   THR A C   
440  O  O   . THR A 35  ? 0.0840 0.0754 0.0758 0.0002  -0.0137 -0.0032 35   THR A O   
441  C  CB  . THR A 35  ? 0.0947 0.0905 0.0621 0.0032  -0.0040 0.0073  35   THR A CB  
442  O  OG1 . THR A 35  ? 0.1041 0.0921 0.0862 -0.0046 -0.0043 0.0156  35   THR A OG1 
443  C  CG2 . THR A 35  ? 0.1248 0.1047 0.0807 0.0153  -0.0230 0.0034  35   THR A CG2 
446  N  N   . CYS A 36  ? 0.0847 0.0805 0.0585 0.0054  -0.0134 -0.0007 36   CYS A N   
447  C  CA  . CYS A 36  ? 0.0906 0.0745 0.0617 0.0019  -0.0092 -0.0030 36   CYS A CA  
448  C  C   . CYS A 36  ? 0.0842 0.0803 0.0572 0.0033  -0.0127 -0.0057 36   CYS A C   
449  O  O   . CYS A 36  ? 0.0936 0.1410 0.0759 0.0139  -0.0203 -0.0300 36   CYS A O   
450  C  CB  . CYS A 36  ? 0.0906 0.0771 0.0681 0.0048  -0.0085 0.0002  36   CYS A CB  
451  S  SG  . CYS A 36  ? 0.0901 0.0926 0.0736 0.0096  0.0047  0.0092  36   CYS A SG  
454  N  N   A VAL A 37  ? 0.0850 0.0744 0.0644 0.0047  -0.0031 -0.0059 37   VAL A N   
455  N  N   B VAL A 37  ? 0.1002 0.1089 0.0223 0.0360  -0.0176 0.0123  37   VAL A N   
456  C  CA  A VAL A 37  ? 0.0976 0.1066 0.0415 0.0194  -0.0105 -0.0093 37   VAL A CA  
457  C  CA  B VAL A 37  ? 0.1373 0.1183 0.0660 0.0438  0.0365  0.0183  37   VAL A CA  
458  C  C   A VAL A 37  ? 0.0763 0.0908 0.0565 0.0112  0.0011  -0.0030 37   VAL A C   
459  C  C   B VAL A 37  ? 0.1282 0.1138 0.0515 0.0579  -0.0237 -0.0079 37   VAL A C   
460  O  O   A VAL A 37  ? 0.0999 0.0793 0.0447 0.0027  -0.0141 -0.0027 37   VAL A O   
461  O  O   B VAL A 37  ? 0.1614 0.1007 0.0494 0.0375  -0.0039 -0.0069 37   VAL A O   
462  C  CB  A VAL A 37  ? 0.1079 0.1182 0.0788 0.0057  0.0066  0.0071  37   VAL A CB  
463  C  CB  B VAL A 37  ? 0.0765 0.1590 0.1133 0.0380  0.0079  0.0081  37   VAL A CB  
464  C  CG1 A VAL A 37  ? 0.1105 0.1529 0.0847 0.0031  -0.0041 0.0104  37   VAL A CG1 
465  C  CG1 B VAL A 37  ? 0.1914 0.2851 0.0952 0.0425  0.0294  0.1421  37   VAL A CG1 
466  C  CG2 A VAL A 37  ? 0.1026 0.1626 0.1203 0.0068  0.0195  -0.0142 37   VAL A CG2 
467  C  CG2 B VAL A 37  ? 0.1796 0.1302 0.2636 -0.0004 -0.1123 0.0501  37   VAL A CG2 
474  N  N   . GLN A 38  ? 0.0991 0.0965 0.0620 0.0116  -0.0041 -0.0114 38   GLN A N   
475  C  CA  . GLN A 38  ? 0.1067 0.0890 0.0596 0.0100  -0.0092 -0.0113 38   GLN A CA  
476  C  C   . GLN A 38  ? 0.1233 0.0912 0.0590 0.0194  -0.0141 -0.0147 38   GLN A C   
477  O  O   . GLN A 38  ? 0.1426 0.1561 0.0596 0.0528  -0.0024 -0.0162 38   GLN A O   
478  C  CB  . GLN A 38  ? 0.1267 0.0926 0.0717 0.0055  -0.0108 -0.0212 38   GLN A CB  
479  C  CG  . GLN A 38  ? 0.1397 0.0859 0.0962 -0.0018 -0.0187 -0.0134 38   GLN A CG  
480  C  CD  . GLN A 38  ? 0.1442 0.1143 0.0740 -0.0072 0.0025  -0.0161 38   GLN A CD  
481  O  OE1 . GLN A 38  ? 0.1414 0.1601 0.1424 -0.0066 -0.0197 -0.0389 38   GLN A OE1 
482  N  NE2 . GLN A 38  ? 0.2121 0.1009 0.1320 -0.0227 -0.0089 -0.0171 38   GLN A NE2 
484  N  N   . LYS A 39  ? 0.1125 0.1070 0.0592 0.0240  -0.0058 -0.0176 39   LYS A N   
485  C  CA  . LYS A 39  ? 0.1241 0.1021 0.0781 0.0290  -0.0077 -0.0212 39   LYS A CA  
486  C  C   . LYS A 39  ? 0.1198 0.1044 0.0759 0.0273  -0.0177 -0.0203 39   LYS A C   
487  O  O   . LYS A 39  ? 0.1357 0.0894 0.0904 0.0185  -0.0059 -0.0107 39   LYS A O   
488  C  CB  . LYS A 39  ? 0.1156 0.1121 0.1214 0.0310  -0.0139 -0.0181 39   LYS A CB  
489  C  CG  . LYS A 39  ? 0.1237 0.1141 0.1130 0.0206  0.0073  -0.0226 39   LYS A CG  
490  C  CD  . LYS A 39  ? 0.1870 0.1461 0.1063 0.0015  -0.0133 -0.0149 39   LYS A CD  
491  C  CE  . LYS A 39  ? 0.1996 0.1843 0.1395 -0.0266 -0.0162 0.0150  39   LYS A CE  
492  N  NZ  . LYS A 39  ? 0.3414 0.2945 0.1278 -0.1087 -0.0005 0.0398  39   LYS A NZ  
497  N  N   . ALA A 40  ? 0.1435 0.1115 0.0956 0.0344  -0.0053 -0.0193 40   ALA A N   
498  C  CA  . ALA A 40  ? 0.1861 0.0934 0.1148 0.0329  -0.0372 -0.0292 40   ALA A CA  
499  C  C   . ALA A 40  ? 0.1185 0.0854 0.1032 0.0159  -0.0098 -0.0142 40   ALA A C   
500  O  O   . ALA A 40  ? 0.1462 0.0986 0.1317 -0.0121 -0.0015 -0.0103 40   ALA A O   
501  C  CB  . ALA A 40  ? 0.2030 0.1113 0.1195 0.0438  -0.0312 -0.0343 40   ALA A CB  
504  N  N   . THR A 41  ? 0.1290 0.0838 0.0991 0.0045  -0.0055 -0.0091 41   THR A N   
505  C  CA  . THR A 41  ? 0.1302 0.0754 0.0913 0.0196  -0.0102 -0.0040 41   THR A CA  
506  C  C   . THR A 41  ? 0.1177 0.0732 0.0761 0.0177  0.0047  0.0036  41   THR A C   
507  O  O   . THR A 41  ? 0.1108 0.0829 0.0880 0.0037  0.0054  0.0024  41   THR A O   
508  C  CB  . THR A 41  ? 0.1310 0.0786 0.1934 0.0251  -0.0377 -0.0229 41   THR A CB  
509  O  OG1 . THR A 41  ? 0.1162 0.1171 0.2592 0.0166  -0.0025 -0.0611 41   THR A OG1 
510  C  CG2 . THR A 41  ? 0.1595 0.0988 0.1963 0.0357  -0.0496 -0.0466 41   THR A CG2 
513  N  N   . TYR A 42  ? 0.1186 0.0649 0.0883 0.0028  0.0064  0.0032  42   TYR A N   
514  C  CA  . TYR A 42  ? 0.1137 0.0638 0.0960 0.0028  0.0194  -0.0025 42   TYR A CA  
515  C  C   . TYR A 42  ? 0.1009 0.0686 0.0813 0.0059  0.0084  -0.0050 42   TYR A C   
516  O  O   . TYR A 42  ? 0.0895 0.0736 0.0842 0.0056  0.0142  -0.0006 42   TYR A O   
517  C  CB  . TYR A 42  ? 0.1437 0.0863 0.0911 -0.0152 0.0256  -0.0131 42   TYR A CB  
518  C  CG  . TYR A 42  ? 0.1650 0.0841 0.0760 -0.0165 -0.0067 -0.0006 42   TYR A CG  
519  C  CD1 . TYR A 42  ? 0.1976 0.0835 0.1316 -0.0193 -0.0539 0.0054  42   TYR A CD1 
520  C  CD2 . TYR A 42  ? 0.1469 0.0801 0.1006 -0.0077 0.0193  -0.0145 42   TYR A CD2 
521  C  CE1 . TYR A 42  ? 0.2101 0.0922 0.1249 -0.0127 -0.0703 0.0101  42   TYR A CE1 
522  C  CE2 . TYR A 42  ? 0.1516 0.0905 0.0984 0.0081  0.0057  0.0018  42   TYR A CE2 
523  C  CZ  . TYR A 42  ? 0.1754 0.0831 0.1137 0.0117  -0.0231 -0.0082 42   TYR A CZ  
524  O  OH  . TYR A 42  ? 0.2008 0.1092 0.1586 0.0307  -0.0388 -0.0009 42   TYR A OH  
531  N  N   . LEU A 43  ? 0.0987 0.0769 0.0955 0.0130  0.0097  0.0021  43   LEU A N   
532  C  CA  . LEU A 43  ? 0.0894 0.0911 0.0942 0.0137  0.0150  -0.0024 43   LEU A CA  
533  C  C   . LEU A 43  ? 0.0910 0.0877 0.0755 0.0143  0.0155  -0.0160 43   LEU A C   
534  O  O   . LEU A 43  ? 0.0978 0.0915 0.0870 0.0094  0.0171  -0.0091 43   LEU A O   
535  C  CB  . LEU A 43  ? 0.1138 0.0974 0.1189 0.0334  0.0168  0.0024  43   LEU A CB  
536  C  CG  . LEU A 43  ? 0.1011 0.1275 0.1640 0.0340  0.0247  -0.0032 43   LEU A CG  
537  C  CD1 . LEU A 43  ? 0.1078 0.1355 0.2317 0.0198  0.0289  -0.0112 43   LEU A CD1 
538  C  CD2 . LEU A 43  ? 0.1230 0.1495 0.2148 0.0602  0.0188  0.0063  43   LEU A CD2 
543  N  N   . ASP A 44  ? 0.1034 0.0855 0.0872 0.0114  0.0127  -0.0123 44   ASP A N   
544  C  CA  . ASP A 44  ? 0.1147 0.0959 0.0743 0.0029  0.0178  -0.0188 44   ASP A CA  
545  C  C   . ASP A 44  ? 0.0810 0.0957 0.0653 -0.0024 0.0113  -0.0151 44   ASP A C   
546  O  O   . ASP A 44  ? 0.1000 0.0954 0.0732 0.0032  0.0115  -0.0068 44   ASP A O   
547  C  CB  . ASP A 44  ? 0.1092 0.1076 0.0890 0.0000  0.0105  -0.0244 44   ASP A CB  
548  C  CG  . ASP A 44  ? 0.1670 0.1044 0.1235 0.0072  0.0205  -0.0371 44   ASP A CG  
549  O  OD1 . ASP A 44  ? 0.2287 0.1109 0.2863 -0.0105 0.0840  -0.0270 44   ASP A OD1 
550  O  OD2 . ASP A 44  ? 0.1855 0.1314 0.1449 0.0224  0.0462  -0.0345 44   ASP A OD2 
554  N  N   . CYS A 45  ? 0.0878 0.0784 0.0687 0.0067  0.0069  -0.0100 45   CYS A N   
555  C  CA  . CYS A 45  ? 0.0896 0.0733 0.0649 0.0107  0.0017  -0.0011 45   CYS A CA  
556  C  C   . CYS A 45  ? 0.0863 0.0796 0.0569 0.0028  0.0136  -0.0011 45   CYS A C   
557  O  O   . CYS A 45  ? 0.0817 0.0862 0.0708 0.0003  0.0091  0.0026  45   CYS A O   
558  C  CB  . CYS A 45  ? 0.0888 0.0776 0.0580 0.0035  0.0046  -0.0040 45   CYS A CB  
559  S  SG  . CYS A 45  ? 0.0826 0.0842 0.0680 -0.0007 0.0023  -0.0046 45   CYS A SG  
564  N  N   . ILE A 46  ? 0.0850 0.0724 0.0666 0.0022  0.0103  -0.0038 46   ILE A N   
565  C  CA  . ILE A 46  ? 0.0732 0.0813 0.0728 0.0044  0.0104  -0.0047 46   ILE A CA  
566  C  C   . ILE A 46  ? 0.0787 0.0857 0.0717 0.0005  0.0115  -0.0053 46   ILE A C   
567  O  O   . ILE A 46  ? 0.0830 0.0875 0.0788 -0.0085 0.0072  -0.0003 46   ILE A O   
568  C  CB  . ILE A 46  ? 0.0817 0.0840 0.0697 0.0072  0.0063  -0.0018 46   ILE A CB  
569  C  CG1 . ILE A 46  ? 0.0793 0.0913 0.0706 -0.0038 0.0056  0.0012  46   ILE A CG1 
570  C  CG2 . ILE A 46  ? 0.0860 0.0870 0.0992 -0.0065 0.0114  0.0010  46   ILE A CG2 
571  C  CD1 . ILE A 46  ? 0.1016 0.0980 0.0782 0.0075  -0.0046 0.0010  46   ILE A CD1 
577  N  N   . LYS A 47  ? 0.0901 0.0848 0.0689 0.0067  0.0137  -0.0012 47   LYS A N   
578  C  CA  . LYS A 47  ? 0.0961 0.0998 0.0717 0.0071  0.0211  -0.0080 47   LYS A CA  
579  C  C   . LYS A 47  ? 0.1026 0.0939 0.0647 0.0008  0.0090  -0.0100 47   LYS A C   
580  O  O   . LYS A 47  ? 0.1092 0.1118 0.0718 -0.0003 0.0148  0.0070  47   LYS A O   
581  C  CB  . LYS A 47  ? 0.1221 0.1041 0.0883 0.0179  0.0233  -0.0132 47   LYS A CB  
582  C  CG  . LYS A 47  ? 0.1067 0.1408 0.0939 0.0274  0.0126  -0.0294 47   LYS A CG  
583  C  CD  . LYS A 47  ? 0.1034 0.1233 0.1786 0.0126  0.0310  -0.0341 47   LYS A CD  
584  C  CE  . LYS A 47  ? 0.1429 0.1291 0.1726 0.0460  0.0407  -0.0140 47   LYS A CE  
585  N  NZ  . LYS A 47  ? 0.1593 0.1395 0.2185 0.0233  0.0352  -0.0396 47   LYS A NZ  
590  N  N   . ALA A 48  ? 0.0941 0.1001 0.0664 0.0007  0.0123  -0.0062 48   ALA A N   
591  C  CA  . ALA A 48  ? 0.0990 0.0972 0.0770 -0.0052 0.0025  -0.0034 48   ALA A CA  
592  C  C   . ALA A 48  ? 0.0819 0.1019 0.0571 -0.0060 0.0031  0.0001  48   ALA A C   
593  O  O   . ALA A 48  ? 0.1081 0.1084 0.0606 -0.0032 0.0048  0.0105  48   ALA A O   
594  C  CB  . ALA A 48  ? 0.1023 0.1202 0.0925 -0.0184 -0.0153 -0.0032 48   ALA A CB  
597  N  N   . ILE A 49  ? 0.0763 0.0855 0.0579 0.0011  0.0100  0.0064  49   ILE A N   
598  C  CA  . ILE A 49  ? 0.0808 0.0851 0.0636 -0.0058 0.0134  0.0015  49   ILE A CA  
599  C  C   . ILE A 49  ? 0.0831 0.0873 0.0559 -0.0051 0.0040  0.0053  49   ILE A C   
600  O  O   . ILE A 49  ? 0.0802 0.0839 0.0717 0.0002  0.0056  0.0116  49   ILE A O   
601  C  CB  . ILE A 49  ? 0.0745 0.0798 0.0561 0.0050  0.0025  0.0095  49   ILE A CB  
602  C  CG1 . ILE A 49  ? 0.0770 0.0811 0.0666 0.0069  0.0103  0.0064  49   ILE A CG1 
603  C  CG2 . ILE A 49  ? 0.0922 0.0867 0.0579 0.0034  -0.0023 0.0070  49   ILE A CG2 
604  C  CD1 . ILE A 49  ? 0.0771 0.0920 0.0835 0.0015  0.0101  0.0184  49   ILE A CD1 
615  N  N   . ALA A 50  ? 0.0787 0.0874 0.0724 -0.0017 0.0064  0.0112  50   ALA A N   
616  C  CA  . ALA A 50  ? 0.0789 0.1004 0.0741 -0.0038 0.0059  0.0132  50   ALA A CA  
617  C  C   . ALA A 50  ? 0.0853 0.1088 0.0796 -0.0015 0.0171  0.0142  50   ALA A C   
618  O  O   . ALA A 50  ? 0.1316 0.1324 0.0989 -0.0292 0.0170  0.0255  50   ALA A O   
619  C  CB  . ALA A 50  ? 0.0801 0.1150 0.0857 -0.0023 0.0129  0.0115  50   ALA A CB  
624  N  N   . ASN A 51  ? 0.0909 0.1252 0.0685 0.0037  0.0097  0.0091  51   ASN A N   
625  C  CA  . ASN A 51  ? 0.1036 0.1517 0.0599 0.0061  0.0222  0.0143  51   ASN A CA  
626  C  C   . ASN A 51  ? 0.0894 0.1704 0.0633 0.0048  0.0106  0.0138  51   ASN A C   
627  O  O   . ASN A 51  ? 0.1240 0.2042 0.0678 0.0225  0.0130  0.0224  51   ASN A O   
628  C  CB  A ASN A 51  ? 0.1341 0.1599 0.0744 0.0069  0.0317  0.0035  51   ASN A CB  
629  C  CB  B ASN A 51  ? 0.1612 0.1822 0.0849 0.0346  -0.0011 -0.0160 51   ASN A CB  
630  C  CG  A ASN A 51  ? 0.1853 0.2334 0.1066 0.0644  0.0278  -0.0551 51   ASN A CG  
631  C  CG  B ASN A 51  ? 0.1781 0.2265 0.1084 0.0317  0.0493  -0.0287 51   ASN A CG  
632  O  OD1 A ASN A 51  ? 0.1272 0.3355 0.3060 0.0730  -0.0129 -0.1670 51   ASN A OD1 
633  O  OD1 B ASN A 51  ? 0.1912 0.2859 0.1503 0.0034  0.0686  -0.0360 51   ASN A OD1 
634  N  ND2 A ASN A 51  ? 0.3445 0.2215 0.1469 0.1122  0.0291  -0.0618 51   ASN A ND2 
635  N  ND2 B ASN A 51  ? 0.2251 0.4608 0.0687 -0.0724 0.0604  -0.0268 51   ASN A ND2 
637  N  N   . ASN A 52  ? 0.0952 0.1355 0.0609 0.0054  0.0089  0.0216  52   ASN A N   
638  C  CA  A ASN A 52  ? 0.1007 0.1143 0.0633 -0.0014 0.0081  0.0273  52   ASN A CA  
639  C  CA  B ASN A 52  ? 0.0808 0.1318 0.0586 -0.0088 0.0197  0.0398  52   ASN A CA  
640  C  C   . ASN A 52  ? 0.0974 0.1268 0.0519 0.0044  0.0116  0.0137  52   ASN A C   
641  O  O   . ASN A 52  ? 0.1001 0.1476 0.0775 0.0082  0.0006  0.0254  52   ASN A O   
642  C  CB  A ASN A 52  ? 0.1074 0.1224 0.0927 -0.0098 0.0186  0.0341  52   ASN A CB  
643  C  CB  B ASN A 52  ? 0.0749 0.1814 0.1058 -0.0120 0.0148  0.0885  52   ASN A CB  
644  C  CG  A ASN A 52  ? 0.1034 0.1036 0.1296 -0.0097 0.0160  0.0311  52   ASN A CG  
645  C  CG  B ASN A 52  ? 0.1070 0.1190 0.1260 -0.0152 -0.0120 0.1145  52   ASN A CG  
646  O  OD1 A ASN A 52  ? 0.1092 0.1078 0.0988 -0.0025 0.0182  0.0251  52   ASN A OD1 
647  O  OD1 B ASN A 52  ? 0.0330 0.2911 0.0734 -0.0380 -0.0145 0.0808  52   ASN A OD1 
648  N  ND2 A ASN A 52  ? 0.1457 0.1353 0.1674 -0.0032 0.0367  0.0619  52   ASN A ND2 
649  N  ND2 B ASN A 52  ? 0.1095 0.1878 0.1172 -0.0749 0.0414  -0.0235 52   ASN A ND2 
655  N  N   . GLU A 53  ? 0.0983 0.1324 0.0555 -0.0051 -0.0008 0.0106  53   GLU A N   
656  C  CA  A GLU A 53  ? 0.0972 0.1410 0.0590 0.0016  0.0025  -0.0120 53   GLU A CA  
657  C  CA  B GLU A 53  ? 0.0949 0.1353 0.0521 0.0027  -0.0084 0.0152  53   GLU A CA  
658  C  C   . GLU A 53  ? 0.0999 0.1359 0.0527 -0.0103 0.0014  -0.0063 53   GLU A C   
659  O  O   . GLU A 53  ? 0.1061 0.2048 0.0767 -0.0270 -0.0048 -0.0168 53   GLU A O   
660  C  CB  A GLU A 53  ? 0.1343 0.1447 0.0496 0.0109  -0.0090 -0.0172 53   GLU A CB  
661  C  CB  B GLU A 53  ? 0.1506 0.1405 0.0968 -0.0163 0.0324  -0.0150 53   GLU A CB  
662  C  CG  A GLU A 53  ? 0.1610 0.1922 0.0856 0.0078  0.0303  -0.0402 53   GLU A CG  
663  C  CG  B GLU A 53  ? 0.1275 0.2179 0.1412 -0.0104 0.0392  -0.0523 53   GLU A CG  
664  C  CD  A GLU A 53  ? 0.1977 0.1681 0.1509 -0.0081 0.0577  -0.0661 53   GLU A CD  
665  C  CD  B GLU A 53  ? 0.2475 0.2335 0.2473 0.0293  0.1023  -0.0499 53   GLU A CD  
666  O  OE1 A GLU A 53  ? 0.2719 0.2760 0.1670 0.0856  0.1046  -0.0077 53   GLU A OE1 
667  O  OE1 B GLU A 53  ? 0.2852 0.2033 0.5580 0.0031  0.0349  -0.1537 53   GLU A OE1 
668  O  OE2 A GLU A 53  ? 0.1928 0.2068 0.1704 0.0416  0.0650  -0.0353 53   GLU A OE2 
669  O  OE2 B GLU A 53  ? 0.2658 0.2593 0.2913 0.0696  0.1095  -0.0676 53   GLU A OE2 
678  N  N   . ALA A 54  ? 0.0771 0.1118 0.0604 0.0007  0.0033  0.0007  54   ALA A N   
679  C  CA  . ALA A 54  ? 0.0801 0.0948 0.0599 -0.0040 0.0031  -0.0019 54   ALA A CA  
680  C  C   . ALA A 54  ? 0.0787 0.0859 0.0521 -0.0018 -0.0042 0.0045  54   ALA A C   
681  O  O   . ALA A 54  ? 0.0748 0.0887 0.0655 -0.0038 0.0036  0.0049  54   ALA A O   
682  C  CB  . ALA A 54  ? 0.1161 0.0852 0.0785 -0.0111 0.0111  -0.0057 54   ALA A CB  
685  N  N   . ASP A 55  ? 0.0731 0.0800 0.0553 -0.0083 -0.0018 0.0051  55   ASP A N   
686  C  CA  . ASP A 55  ? 0.0720 0.0763 0.0512 -0.0037 0.0013  0.0041  55   ASP A CA  
687  C  C   . ASP A 55  ? 0.0755 0.0644 0.0558 0.0019  0.0039  0.0042  55   ASP A C   
688  O  O   . ASP A 55  ? 0.0845 0.0804 0.0530 -0.0089 -0.0018 0.0083  55   ASP A O   
689  C  CB  . ASP A 55  ? 0.0838 0.0778 0.0610 -0.0006 -0.0044 0.0090  55   ASP A CB  
690  C  CG  . ASP A 55  ? 0.0885 0.0855 0.0601 -0.0042 -0.0041 0.0123  55   ASP A CG  
691  O  OD1 . ASP A 55  ? 0.0888 0.0985 0.0781 -0.0036 0.0042  0.0261  55   ASP A OD1 
692  O  OD2 . ASP A 55  ? 0.0788 0.0945 0.0753 0.0016  -0.0009 0.0214  55   ASP A OD2 
697  N  N   . ALA A 56  ? 0.0637 0.0722 0.0581 -0.0036 0.0057  0.0069  56   ALA A N   
698  C  CA  . ALA A 56  ? 0.0752 0.0728 0.0463 -0.0036 -0.0014 0.0031  56   ALA A CA  
699  C  C   . ALA A 56  ? 0.0730 0.0707 0.0435 0.0035  0.0012  0.0024  56   ALA A C   
700  O  O   . ALA A 56  ? 0.0721 0.0806 0.0550 -0.0043 -0.0042 0.0041  56   ALA A O   
701  C  CB  . ALA A 56  ? 0.1014 0.0731 0.0604 0.0051  0.0146  0.0021  56   ALA A CB  
706  N  N   . ILE A 57  ? 0.0685 0.0648 0.0573 -0.0067 -0.0008 0.0019  57   ILE A N   
707  C  CA  . ILE A 57  ? 0.0635 0.0686 0.0548 0.0013  0.0013  0.0085  57   ILE A CA  
708  C  C   . ILE A 57  ? 0.0563 0.0674 0.0551 0.0016  -0.0009 0.0019  57   ILE A C   
709  O  O   . ILE A 57  ? 0.0756 0.0824 0.0496 -0.0125 0.0015  0.0035  57   ILE A O   
710  C  CB  . ILE A 57  ? 0.0737 0.0722 0.0455 -0.0047 -0.0012 0.0052  57   ILE A CB  
711  C  CG1 . ILE A 57  ? 0.0927 0.0670 0.0636 -0.0059 0.0056  0.0006  57   ILE A CG1 
712  C  CG2 . ILE A 57  ? 0.0646 0.0784 0.0608 0.0010  0.0051  0.0057  57   ILE A CG2 
713  C  CD1 . ILE A 57  ? 0.0960 0.0709 0.0719 -0.0017 0.0033  -0.0012 57   ILE A CD1 
720  N  N   . SER A 58  ? 0.0575 0.0735 0.0498 -0.0040 -0.0033 0.0057  58   SER A N   
721  C  CA  A SER A 58  ? 0.0546 0.0818 0.0526 0.0012  0.0016  0.0046  58   SER A CA  
722  C  CA  B SER A 58  ? 0.0636 0.0817 0.0498 0.0000  -0.0011 0.0058  58   SER A CA  
723  C  C   . SER A 58  ? 0.0644 0.0624 0.0573 -0.0154 -0.0054 0.0127  58   SER A C   
724  O  O   . SER A 58  ? 0.0946 0.0661 0.1110 -0.0101 -0.0399 0.0087  58   SER A O   
725  C  CB  A SER A 58  ? 0.0762 0.1197 0.0498 0.0073  0.0067  0.0270  58   SER A CB  
726  C  CB  B SER A 58  ? 0.0697 0.1367 0.0657 0.0112  0.0032  0.0301  58   SER A CB  
727  O  OG  A SER A 58  ? 0.0564 0.0856 0.0555 0.0013  0.0037  0.0030  58   SER A OG  
728  O  OG  B SER A 58  ? 0.0782 0.0785 0.0700 0.0031  0.0024  -0.0086 58   SER A OG  
732  N  N   . LEU A 59  ? 0.0627 0.0685 0.0476 -0.0004 -0.0026 0.0022  59   LEU A N   
733  C  CA  . LEU A 59  ? 0.0627 0.0609 0.0532 0.0011  -0.0015 -0.0005 59   LEU A CA  
734  C  C   . LEU A 59  ? 0.0450 0.0637 0.0559 0.0007  0.0087  -0.0017 59   LEU A C   
735  O  O   . LEU A 59  ? 0.0595 0.0732 0.0482 0.0027  0.0018  0.0009  59   LEU A O   
736  C  CB  . LEU A 59  ? 0.0630 0.0649 0.0511 -0.0059 0.0026  -0.0025 59   LEU A CB  
737  C  CG  . LEU A 59  ? 0.0670 0.0709 0.0565 0.0047  0.0023  0.0019  59   LEU A CG  
738  C  CD1 . LEU A 59  ? 0.0780 0.0942 0.0553 0.0048  0.0162  0.0091  59   LEU A CD1 
739  C  CD2 . LEU A 59  ? 0.0959 0.0853 0.0472 -0.0011 0.0005  -0.0067 59   LEU A CD2 
747  N  N   . ASP A 60  ? 0.0633 0.0570 0.0513 0.0018  0.0025  0.0027  60   ASP A N   
748  C  CA  . ASP A 60  ? 0.0629 0.0612 0.0551 0.0045  0.0070  0.0008  60   ASP A CA  
749  C  C   . ASP A 60  ? 0.0632 0.0606 0.0511 0.0072  0.0016  -0.0035 60   ASP A C   
750  O  O   . ASP A 60  ? 0.0613 0.0668 0.0535 -0.0015 -0.0003 0.0037  60   ASP A O   
751  C  CB  . ASP A 60  ? 0.0731 0.0576 0.0509 0.0054  0.0010  -0.0009 60   ASP A CB  
752  C  CG  . ASP A 60  ? 0.0637 0.0525 0.0657 0.0010  0.0027  0.0077  60   ASP A CG  
753  O  OD1 . ASP A 60  ? 0.0754 0.0685 0.0566 -0.0101 -0.0035 0.0055  60   ASP A OD1 
754  O  OD2 . ASP A 60  ? 0.0730 0.0675 0.0755 0.0070  0.0051  0.0062  60   ASP A OD2 
758  N  N   . GLY A 61  ? 0.0672 0.0811 0.0505 -0.0020 0.0038  -0.0006 61   GLY A N   
759  C  CA  . GLY A 61  ? 0.0689 0.0710 0.0602 -0.0058 -0.0075 -0.0012 61   GLY A CA  
760  C  C   . GLY A 61  ? 0.0648 0.0769 0.0599 -0.0044 -0.0095 0.0115  61   GLY A C   
761  O  O   . GLY A 61  ? 0.0700 0.0754 0.0722 -0.0085 -0.0022 0.0101  61   GLY A O   
765  N  N   . GLY A 62  ? 0.0676 0.0719 0.0683 -0.0008 -0.0026 0.0123  62   GLY A N   
766  C  CA  . GLY A 62  ? 0.0639 0.0700 0.0911 0.0017  -0.0007 0.0104  62   GLY A CA  
767  C  C   . GLY A 62  ? 0.0696 0.0570 0.0915 0.0037  0.0045  -0.0054 62   GLY A C   
768  O  O   . GLY A 62  ? 0.0739 0.0891 0.0964 0.0059  0.0112  -0.0052 62   GLY A O   
772  N  N   . GLN A 63  ? 0.0767 0.0637 0.0810 0.0023  0.0021  0.0041  63   GLN A N   
773  C  CA  . GLN A 63  ? 0.0699 0.0716 0.0754 0.0012  0.0080  -0.0049 63   GLN A CA  
774  C  C   . GLN A 63  ? 0.0624 0.0674 0.0635 0.0004  0.0059  0.0010  63   GLN A C   
775  O  O   . GLN A 63  ? 0.0676 0.0855 0.0596 -0.0041 0.0082  -0.0004 63   GLN A O   
776  C  CB  A GLN A 63  ? 0.0949 0.0693 0.1035 -0.0149 -0.0134 -0.0033 63   GLN A CB  
777  C  CB  B GLN A 63  ? 0.0425 0.0674 0.0881 0.0168  0.0213  -0.0298 63   GLN A CB  
778  C  CG  A GLN A 63  ? 0.1094 0.0693 0.0703 -0.0156 -0.0005 -0.0012 63   GLN A CG  
779  C  CG  B GLN A 63  ? 0.0766 0.0654 0.1097 0.0019  0.0284  -0.0147 63   GLN A CG  
780  C  CD  A GLN A 63  ? 0.1372 0.0820 0.0594 0.0100  0.0139  -0.0006 63   GLN A CD  
781  C  CD  B GLN A 63  ? 0.0888 0.0898 0.0667 -0.0193 0.0042  0.0250  63   GLN A CD  
782  O  OE1 A GLN A 63  ? 0.1739 0.0772 0.0866 -0.0001 0.0477  0.0066  63   GLN A OE1 
783  O  OE1 B GLN A 63  ? 0.0798 0.1529 0.2432 -0.0126 -0.0117 0.0322  63   GLN A OE1 
784  N  NE2 A GLN A 63  ? 0.1627 0.1041 0.0922 0.0327  0.0130  0.0172  63   GLN A NE2 
785  N  NE2 B GLN A 63  ? 0.1266 0.0950 0.1351 -0.0312 0.0314  -0.0533 63   GLN A NE2 
790  N  N   . VAL A 64  ? 0.0598 0.0663 0.0578 -0.0046 0.0095  0.0034  64   VAL A N   
791  C  CA  . VAL A 64  ? 0.0621 0.0645 0.0569 0.0013  0.0069  -0.0001 64   VAL A CA  
792  C  C   . VAL A 64  ? 0.0644 0.0570 0.0555 -0.0037 0.0047  -0.0009 64   VAL A C   
793  O  O   . VAL A 64  ? 0.0644 0.0677 0.0700 -0.0010 0.0083  0.0029  64   VAL A O   
794  C  CB  . VAL A 64  ? 0.0572 0.0657 0.0570 -0.0018 0.0010  0.0026  64   VAL A CB  
795  C  CG1 . VAL A 64  ? 0.0813 0.0678 0.0760 -0.0082 0.0091  -0.0079 64   VAL A CG1 
796  C  CG2 . VAL A 64  ? 0.0657 0.0674 0.0676 -0.0006 0.0091  -0.0016 64   VAL A CG2 
805  N  N   . PHE A 65  ? 0.0603 0.0670 0.0641 -0.0034 0.0043  0.0022  65   PHE A N   
806  C  CA  . PHE A 65  ? 0.0625 0.0709 0.0609 0.0023  0.0037  -0.0026 65   PHE A CA  
807  C  C   . PHE A 65  ? 0.0538 0.0716 0.0716 0.0076  0.0046  -0.0029 65   PHE A C   
808  O  O   . PHE A 65  ? 0.0662 0.0776 0.0729 0.0014  0.0079  0.0007  65   PHE A O   
809  C  CB  . PHE A 65  ? 0.0614 0.0790 0.0788 0.0082  -0.0021 0.0042  65   PHE A CB  
810  C  CG  . PHE A 65  ? 0.0718 0.0876 0.0849 0.0123  0.0052  0.0146  65   PHE A CG  
811  C  CD1 . PHE A 65  ? 0.0719 0.0864 0.1438 0.0017  -0.0147 -0.0015 65   PHE A CD1 
812  C  CD2 . PHE A 65  ? 0.1188 0.1614 0.0904 0.0676  0.0083  -0.0060 65   PHE A CD2 
813  C  CE1 . PHE A 65  ? 0.0748 0.1019 0.1979 -0.0001 -0.0085 0.0223  65   PHE A CE1 
814  C  CE2 . PHE A 65  ? 0.1304 0.1694 0.1047 0.0572  0.0289  0.0429  65   PHE A CE2 
815  C  CZ  . PHE A 65  ? 0.0926 0.1430 0.1570 0.0231  0.0146  0.0605  65   PHE A CZ  
821  N  N   . GLU A 66  ? 0.0706 0.0652 0.0721 0.0088  0.0044  -0.0031 66   GLU A N   
822  C  CA  . GLU A 66  ? 0.0742 0.0926 0.0690 0.0079  0.0014  -0.0111 66   GLU A CA  
823  C  C   . GLU A 66  ? 0.0749 0.0835 0.0649 -0.0085 0.0091  -0.0110 66   GLU A C   
824  O  O   . GLU A 66  ? 0.0820 0.1164 0.0673 -0.0094 0.0181  -0.0103 66   GLU A O   
825  C  CB  A GLU A 66  ? 0.0496 0.0798 0.0727 0.0079  0.0130  -0.0096 66   GLU A CB  
826  C  CB  B GLU A 66  ? 0.1408 0.0775 0.0950 0.0105  -0.0167 -0.0146 66   GLU A CB  
827  C  CG  A GLU A 66  ? 0.1061 0.0927 0.0539 -0.0070 -0.0002 -0.0019 66   GLU A CG  
828  C  CG  B GLU A 66  ? 0.1156 0.0930 0.1227 0.0210  -0.0160 -0.0072 66   GLU A CG  
829  C  CD  A GLU A 66  ? 0.0853 0.0721 0.0873 0.0164  0.0017  -0.0117 66   GLU A CD  
830  C  CD  B GLU A 66  ? 0.1532 0.0830 0.2091 0.0196  -0.0334 -0.0215 66   GLU A CD  
831  O  OE1 A GLU A 66  ? 0.1007 0.1092 0.0999 -0.0226 -0.0025 -0.0020 66   GLU A OE1 
832  O  OE1 B GLU A 66  ? 0.2971 0.0955 0.2895 -0.0049 -0.1399 -0.0558 66   GLU A OE1 
833  O  OE2 A GLU A 66  ? 0.1606 0.0980 0.0818 -0.0041 0.0106  -0.0191 66   GLU A OE2 
834  O  OE2 B GLU A 66  ? 0.4324 0.0953 0.3115 0.0157  -0.0990 0.0237  66   GLU A OE2 
838  N  N   . ALA A 67  ? 0.0660 0.0802 0.0613 -0.0038 0.0047  0.0050  67   ALA A N   
839  C  CA  . ALA A 67  ? 0.0671 0.0896 0.0595 -0.0120 0.0006  0.0038  67   ALA A CA  
840  C  C   . ALA A 67  ? 0.0672 0.0801 0.0584 0.0025  0.0110  0.0031  67   ALA A C   
841  O  O   . ALA A 67  ? 0.0766 0.0926 0.0613 0.0001  0.0039  0.0043  67   ALA A O   
842  C  CB  . ALA A 67  ? 0.0657 0.0815 0.0845 -0.0059 -0.0020 0.0104  67   ALA A CB  
848  N  N   . GLY A 68  ? 0.0634 0.0753 0.0581 -0.0008 0.0058  0.0008  68   GLY A N   
849  C  CA  . GLY A 68  ? 0.0664 0.0820 0.0627 0.0011  0.0015  -0.0019 68   GLY A CA  
850  C  C   . GLY A 68  ? 0.0644 0.0744 0.0689 -0.0055 0.0032  0.0005  68   GLY A C   
851  O  O   . GLY A 68  ? 0.0684 0.0875 0.0892 -0.0031 0.0115  -0.0041 68   GLY A O   
855  N  N   . LEU A 69  ? 0.0672 0.0823 0.0831 -0.0021 0.0108  -0.0013 69   LEU A N   
856  C  CA  . LEU A 69  ? 0.0626 0.1091 0.0800 0.0089  0.0071  -0.0018 69   LEU A CA  
857  C  C   . LEU A 69  ? 0.0698 0.0986 0.0921 0.0083  0.0235  0.0033  69   LEU A C   
858  O  O   . LEU A 69  ? 0.0800 0.1096 0.0815 0.0047  0.0185  0.0068  69   LEU A O   
859  C  CB  . LEU A 69  ? 0.0767 0.0975 0.0894 0.0082  0.0166  -0.0006 69   LEU A CB  
860  C  CG  . LEU A 69  ? 0.0877 0.1156 0.0939 0.0242  0.0190  0.0062  69   LEU A CG  
861  C  CD1 . LEU A 69  ? 0.1485 0.1080 0.1338 0.0332  0.0339  0.0233  69   LEU A CD1 
862  C  CD2 . LEU A 69  ? 0.1217 0.1641 0.0969 0.0130  -0.0080 0.0077  69   LEU A CD2 
870  N  N   . ALA A 70  ? 0.0786 0.1164 0.1069 -0.0090 0.0241  -0.0042 70   ALA A N   
871  C  CA  . ALA A 70  ? 0.0840 0.1264 0.1147 -0.0027 0.0447  -0.0035 70   ALA A CA  
872  C  C   . ALA A 70  ? 0.0856 0.1293 0.1028 0.0069  0.0411  -0.0097 70   ALA A C   
873  O  O   . ALA A 70  ? 0.0948 0.1290 0.1380 0.0153  0.0331  -0.0062 70   ALA A O   
874  C  CB  . ALA A 70  ? 0.0985 0.1698 0.1404 -0.0252 0.0500  -0.0038 70   ALA A CB  
877  N  N   . PRO A 71  ? 0.1022 0.1482 0.1056 0.0117  0.0457  -0.0130 71   PRO A N   
878  C  CA  . PRO A 71  ? 0.1194 0.1694 0.1041 0.0179  0.0618  0.0106  71   PRO A CA  
879  C  C   . PRO A 71  ? 0.1185 0.1517 0.1140 0.0176  0.0471  0.0299  71   PRO A C   
880  O  O   . PRO A 71  ? 0.1722 0.2329 0.1608 0.0632  0.0810  0.0999  71   PRO A O   
881  C  CB  . PRO A 71  ? 0.1653 0.1999 0.1028 0.0164  0.0502  -0.0095 71   PRO A CB  
882  C  CG  . PRO A 71  ? 0.1450 0.2117 0.1025 -0.0008 0.0377  -0.0192 71   PRO A CG  
883  C  CD  . PRO A 71  ? 0.1181 0.1684 0.1187 0.0093  0.0295  -0.0348 71   PRO A CD  
886  N  N   . TYR A 72  ? 0.0861 0.1343 0.0700 0.0059  0.0280  -0.0033 72   TYR A N   
887  C  CA  . TYR A 72  ? 0.0860 0.1195 0.0647 0.0057  0.0124  -0.0029 72   TYR A CA  
888  C  C   . TYR A 72  ? 0.0827 0.1097 0.0630 0.0000  0.0177  0.0061  72   TYR A C   
889  O  O   . TYR A 72  ? 0.0997 0.1101 0.0786 0.0205  0.0137  0.0142  72   TYR A O   
890  C  CB  . TYR A 72  ? 0.0766 0.1137 0.0857 -0.0066 0.0137  -0.0146 72   TYR A CB  
891  C  CG  . TYR A 72  ? 0.0702 0.1150 0.0926 0.0012  0.0211  -0.0119 72   TYR A CG  
892  C  CD1 . TYR A 72  ? 0.0946 0.1339 0.0929 0.0076  0.0155  -0.0210 72   TYR A CD1 
893  C  CD2 . TYR A 72  ? 0.0862 0.1198 0.1062 0.0085  0.0059  -0.0176 72   TYR A CD2 
894  C  CE1 . TYR A 72  ? 0.1352 0.1348 0.1005 -0.0034 -0.0037 -0.0230 72   TYR A CE1 
895  C  CE2 . TYR A 72  ? 0.0959 0.1124 0.1201 0.0001  0.0045  -0.0172 72   TYR A CE2 
896  C  CZ  . TYR A 72  ? 0.1222 0.1198 0.1182 -0.0005 0.0059  -0.0285 72   TYR A CZ  
897  O  OH  . TYR A 72  ? 0.1892 0.1640 0.1496 0.0395  -0.0069 -0.0654 72   TYR A OH  
904  N  N   . LYS A 73  ? 0.0750 0.0893 0.0675 0.0049  0.0149  0.0083  73   LYS A N   
905  C  CA  . LYS A 73  ? 0.0749 0.0852 0.0737 -0.0077 0.0080  0.0105  73   LYS A CA  
906  C  C   . LYS A 73  ? 0.0722 0.0801 0.0554 -0.0004 0.0064  0.0076  73   LYS A C   
907  O  O   . LYS A 73  ? 0.0834 0.0802 0.0744 -0.0021 0.0096  0.0072  73   LYS A O   
908  C  CB  . LYS A 73  ? 0.0783 0.1040 0.0910 -0.0114 0.0285  0.0160  73   LYS A CB  
909  C  CG  . LYS A 73  ? 0.0752 0.1232 0.1476 -0.0045 0.0250  0.0302  73   LYS A CG  
910  C  CD  . LYS A 73  ? 0.1126 0.1468 0.1170 -0.0258 -0.0005 0.0108  73   LYS A CD  
911  C  CE  . LYS A 73  ? 0.1604 0.1429 0.1083 0.0269  0.0199  -0.0044 73   LYS A CE  
912  N  NZ  . LYS A 73  ? 0.1526 0.1515 0.1150 -0.0561 0.0071  -0.0097 73   LYS A NZ  
917  N  N   . LEU A 74  ? 0.0707 0.0768 0.0647 0.0028  0.0113  0.0046  74   LEU A N   
918  C  CA  . LEU A 74  ? 0.0657 0.0835 0.0600 -0.0012 0.0076  0.0027  74   LEU A CA  
919  C  C   . LEU A 74  ? 0.0602 0.0751 0.0641 -0.0014 0.0093  0.0029  74   LEU A C   
920  O  O   . LEU A 74  ? 0.0674 0.0890 0.0619 0.0029  -0.0004 -0.0037 74   LEU A O   
921  C  CB  . LEU A 74  ? 0.0646 0.0821 0.0618 0.0040  0.0011  0.0001  74   LEU A CB  
922  C  CG  . LEU A 74  ? 0.0782 0.0883 0.0628 0.0020  0.0035  -0.0031 74   LEU A CG  
923  C  CD1 . LEU A 74  ? 0.0913 0.0832 0.0773 0.0044  -0.0148 0.0026  74   LEU A CD1 
924  C  CD2 . LEU A 74  ? 0.0792 0.0878 0.0714 0.0067  -0.0083 0.0024  74   LEU A CD2 
935  N  N   . LYS A 75  ? 0.0635 0.0968 0.0581 0.0061  0.0083  0.0021  75   LYS A N   
936  C  CA  . LYS A 75  ? 0.0707 0.0988 0.0603 -0.0028 0.0066  -0.0094 75   LYS A CA  
937  C  C   . LYS A 75  ? 0.0655 0.0890 0.0609 0.0032  0.0016  -0.0086 75   LYS A C   
938  O  O   . LYS A 75  ? 0.0636 0.1072 0.0621 0.0040  -0.0009 -0.0035 75   LYS A O   
939  C  CB  A LYS A 75  ? 0.0715 0.1035 0.0649 -0.0020 -0.0226 0.0034  75   LYS A CB  
940  C  CB  B LYS A 75  ? 0.0921 0.1129 0.1311 -0.0173 0.0665  -0.0489 75   LYS A CB  
941  C  CG  A LYS A 75  ? 0.1172 0.1416 0.2114 -0.0498 0.0409  -0.0243 75   LYS A CG  
942  C  CG  B LYS A 75  ? 0.0817 0.0864 0.0785 -0.0076 0.0176  -0.0340 75   LYS A CG  
943  C  CD  A LYS A 75  ? 0.1174 0.1435 0.1286 -0.0374 0.0228  -0.0060 75   LYS A CD  
944  C  CD  B LYS A 75  ? 0.1439 0.0916 0.1300 -0.0309 0.0514  -0.0436 75   LYS A CD  
945  C  CE  A LYS A 75  ? 0.1585 0.1492 0.1091 -0.0573 0.0068  0.0024  75   LYS A CE  
946  C  CE  B LYS A 75  ? 0.1164 0.0810 0.1538 -0.0233 -0.0278 -0.0080 75   LYS A CE  
947  N  NZ  A LYS A 75  ? 0.1960 0.1330 0.1405 -0.0464 -0.0211 0.0087  75   LYS A NZ  
948  N  NZ  B LYS A 75  ? 0.1592 0.0844 0.1795 -0.0327 0.0096  -0.0193 75   LYS A NZ  
955  N  N   . PRO A 76  ? 0.0587 0.0993 0.0622 0.0022  0.0053  -0.0056 76   PRO A N   
956  C  CA  . PRO A 76  ? 0.0626 0.0833 0.0609 0.0012  0.0056  -0.0099 76   PRO A CA  
957  C  C   . PRO A 76  ? 0.0692 0.0864 0.0571 -0.0040 0.0049  -0.0048 76   PRO A C   
958  O  O   . PRO A 76  ? 0.0724 0.0910 0.1028 -0.0032 -0.0108 -0.0239 76   PRO A O   
959  C  CB  . PRO A 76  ? 0.0725 0.1166 0.0631 0.0027  0.0096  -0.0001 76   PRO A CB  
960  C  CG  . PRO A 76  ? 0.0710 0.1346 0.0680 -0.0028 0.0036  0.0045  76   PRO A CG  
961  C  CD  . PRO A 76  ? 0.0594 0.1308 0.0636 0.0154  -0.0032 -0.0128 76   PRO A CD  
966  N  N   . ILE A 77  ? 0.0656 0.0777 0.0563 -0.0028 0.0019  -0.0015 77   ILE A N   
967  C  CA  . ILE A 77  ? 0.0774 0.0788 0.0620 -0.0062 0.0082  -0.0003 77   ILE A CA  
968  C  C   . ILE A 77  ? 0.0722 0.0701 0.0613 0.0056  0.0022  0.0031  77   ILE A C   
969  O  O   . ILE A 77  ? 0.0826 0.0719 0.0752 0.0102  0.0100  0.0033  77   ILE A O   
970  C  CB  . ILE A 77  ? 0.0821 0.0858 0.0744 0.0008  0.0087  0.0166  77   ILE A CB  
971  C  CG1 . ILE A 77  ? 0.0937 0.1356 0.0854 -0.0133 -0.0150 0.0285  77   ILE A CG1 
972  C  CG2 . ILE A 77  ? 0.0976 0.1184 0.0754 0.0004  0.0111  0.0151  77   ILE A CG2 
973  C  CD1 . ILE A 77  ? 0.1077 0.2037 0.0974 0.0166  -0.0225 0.0298  77   ILE A CD1 
980  N  N   . ALA A 78  ? 0.0696 0.0756 0.0761 0.0063  0.0154  0.0072  78   ALA A N   
981  C  CA  . ALA A 78  ? 0.0815 0.0726 0.0831 0.0109  0.0313  0.0042  78   ALA A CA  
982  C  C   . ALA A 78  ? 0.0749 0.0644 0.0717 0.0030  0.0198  -0.0025 78   ALA A C   
983  O  O   . ALA A 78  ? 0.1685 0.0741 0.0710 0.0353  0.0207  -0.0032 78   ALA A O   
984  C  CB  . ALA A 78  ? 0.0691 0.1079 0.1096 0.0092  0.0245  0.0317  78   ALA A CB  
989  N  N   . ALA A 79  ? 0.0720 0.0585 0.0690 -0.0002 0.0189  -0.0051 79   ALA A N   
990  C  CA  . ALA A 79  ? 0.0644 0.0628 0.0673 0.0050  0.0118  0.0007  79   ALA A CA  
991  C  C   . ALA A 79  ? 0.0635 0.0588 0.0458 -0.0008 0.0014  -0.0086 79   ALA A C   
992  O  O   . ALA A 79  ? 0.0610 0.0562 0.0732 0.0027  0.0083  -0.0070 79   ALA A O   
993  C  CB  . ALA A 79  ? 0.0633 0.0802 0.0908 -0.0020 -0.0025 -0.0092 79   ALA A CB  
998  N  N   . GLU A 80  ? 0.0595 0.0583 0.0528 0.0008  0.0040  -0.0043 80   GLU A N   
999  C  CA  . GLU A 80  ? 0.0553 0.0611 0.0602 0.0024  -0.0005 0.0033  80   GLU A CA  
1000 C  C   . GLU A 80  ? 0.0559 0.0554 0.0619 0.0048  0.0026  0.0003  80   GLU A C   
1001 O  O   . GLU A 80  ? 0.0549 0.0844 0.0621 0.0045  -0.0005 -0.0024 80   GLU A O   
1002 C  CB  . GLU A 80  ? 0.0706 0.0580 0.0638 -0.0054 0.0016  0.0050  80   GLU A CB  
1003 C  CG  . GLU A 80  ? 0.0787 0.0676 0.0702 -0.0043 -0.0080 0.0004  80   GLU A CG  
1004 C  CD  . GLU A 80  ? 0.0621 0.0718 0.0573 0.0097  0.0008  -0.0057 80   GLU A CD  
1005 O  OE1 . GLU A 80  ? 0.0735 0.0683 0.0724 0.0042  -0.0032 -0.0014 80   GLU A OE1 
1006 O  OE2 . GLU A 80  ? 0.0873 0.0750 0.0877 0.0023  -0.0213 -0.0056 80   GLU A OE2 
1011 N  N   . VAL A 81  ? 0.0543 0.0707 0.0563 0.0007  0.0020  -0.0027 81   VAL A N   
1012 C  CA  . VAL A 81  ? 0.0621 0.0669 0.0579 0.0007  0.0077  -0.0025 81   VAL A CA  
1013 C  C   . VAL A 81  ? 0.0637 0.0731 0.0465 0.0061  0.0043  -0.0074 81   VAL A C   
1014 O  O   . VAL A 81  ? 0.0570 0.0823 0.0667 -0.0045 0.0000  -0.0008 81   VAL A O   
1015 C  CB  . VAL A 81  ? 0.0671 0.0679 0.0683 0.0021  -0.0004 -0.0048 81   VAL A CB  
1016 C  CG1 . VAL A 81  ? 0.0826 0.0766 0.0769 0.0019  0.0149  -0.0095 81   VAL A CG1 
1017 C  CG2 . VAL A 81  ? 0.0736 0.0681 0.0760 -0.0020 0.0088  0.0003  81   VAL A CG2 
1026 N  N   . TYR A 82  ? 0.0690 0.0714 0.0624 -0.0020 0.0013  -0.0056 82   TYR A N   
1027 C  CA  . TYR A 82  ? 0.0712 0.0613 0.0668 -0.0031 -0.0011 -0.0023 82   TYR A CA  
1028 C  C   . TYR A 82  ? 0.0711 0.0658 0.0663 0.0075  0.0023  0.0033  82   TYR A C   
1029 O  O   . TYR A 82  ? 0.0828 0.0803 0.0727 0.0018  0.0091  -0.0103 82   TYR A O   
1030 C  CB  . TYR A 82  ? 0.0728 0.0762 0.0595 0.0016  0.0042  0.0015  82   TYR A CB  
1031 C  CG  . TYR A 82  ? 0.0653 0.0689 0.0627 0.0063  0.0018  0.0055  82   TYR A CG  
1032 C  CD1 . TYR A 82  ? 0.0663 0.0639 0.0667 -0.0021 0.0018  -0.0040 82   TYR A CD1 
1033 C  CD2 . TYR A 82  ? 0.0596 0.0841 0.0605 -0.0073 -0.0032 0.0042  82   TYR A CD2 
1034 C  CE1 . TYR A 82  ? 0.0661 0.0648 0.0697 -0.0033 0.0015  -0.0078 82   TYR A CE1 
1035 C  CE2 . TYR A 82  ? 0.0686 0.0803 0.0645 -0.0045 -0.0021 0.0041  82   TYR A CE2 
1036 C  CZ  . TYR A 82  ? 0.0663 0.0675 0.0623 0.0038  0.0047  0.0056  82   TYR A CZ  
1037 O  OH  . TYR A 82  ? 0.0731 0.0674 0.0598 0.0031  0.0100  -0.0016 82   TYR A OH  
1043 N  N   . GLU A 83  ? 0.0701 0.0784 0.0686 0.0007  0.0109  -0.0049 83   GLU A N   
1044 C  CA  . GLU A 83  ? 0.0878 0.0727 0.0615 0.0078  0.0061  -0.0018 83   GLU A CA  
1045 C  C   . GLU A 83  ? 0.0964 0.0806 0.0696 0.0067  0.0078  -0.0059 83   GLU A C   
1046 O  O   . GLU A 83  ? 0.1025 0.0971 0.0841 0.0182  -0.0058 -0.0133 83   GLU A O   
1047 C  CB  A GLU A 83  ? 0.1005 0.1083 0.0904 -0.0166 0.0257  -0.0071 83   GLU A CB  
1048 C  CB  B GLU A 83  ? 0.0793 0.1035 0.0705 0.0142  0.0226  0.0090  83   GLU A CB  
1049 C  CG  A GLU A 83  ? 0.0807 0.1417 0.0832 -0.0148 0.0148  -0.0069 83   GLU A CG  
1050 C  CG  B GLU A 83  ? 0.0814 0.1800 0.1117 0.0055  0.0003  -0.0328 83   GLU A CG  
1051 C  CD  A GLU A 83  ? 0.1754 0.2079 0.1093 -0.0863 0.0631  -0.0377 83   GLU A CD  
1052 C  CD  B GLU A 83  ? 0.1299 0.2341 0.1294 -0.0464 -0.0157 -0.0098 83   GLU A CD  
1053 O  OE1 A GLU A 83  ? 0.1820 0.2818 0.1066 -0.1417 0.0209  -0.0119 83   GLU A OE1 
1054 O  OE1 B GLU A 83  ? 0.6000 0.3656 0.1833 -0.3283 -0.1558 0.0795  83   GLU A OE1 
1055 O  OE2 A GLU A 83  ? 0.2188 0.2831 0.1343 -0.1026 0.1094  -0.0351 83   GLU A OE2 
1056 O  OE2 B GLU A 83  ? 0.3485 0.3325 0.1384 -0.1489 0.0282  -0.0092 83   GLU A OE2 
1063 N  N   . HIS A 84  ? 0.1029 0.0913 0.0664 0.0130  -0.0060 -0.0052 84   HIS A N   
1064 C  CA  . HIS A 84  ? 0.0989 0.1007 0.0819 0.0090  -0.0055 -0.0048 84   HIS A CA  
1065 C  C   . HIS A 84  ? 0.1132 0.1055 0.0686 -0.0005 -0.0055 0.0066  84   HIS A C   
1066 O  O   . HIS A 84  ? 0.1027 0.1303 0.0756 0.0006  -0.0011 -0.0081 84   HIS A O   
1067 C  CB  . HIS A 84  ? 0.0945 0.0993 0.0859 0.0139  0.0004  -0.0023 84   HIS A CB  
1068 C  CG  . HIS A 84  ? 0.0944 0.1074 0.0976 0.0106  -0.0094 -0.0105 84   HIS A CG  
1069 N  ND1 . HIS A 84  ? 0.1220 0.1403 0.0961 0.0286  -0.0181 -0.0240 84   HIS A ND1 
1070 C  CD2 . HIS A 84  ? 0.1006 0.1370 0.1119 0.0190  -0.0056 -0.0146 84   HIS A CD2 
1071 C  CE1 . HIS A 84  ? 0.1199 0.1420 0.1234 0.0373  -0.0319 -0.0242 84   HIS A CE1 
1072 N  NE2 . HIS A 84  ? 0.1045 0.1736 0.1363 0.0338  -0.0243 -0.0263 84   HIS A NE2 
1076 N  N   . THR A 85  ? 0.1348 0.1237 0.0720 -0.0098 -0.0095 0.0074  85   THR A N   
1077 C  CA  . THR A 85  ? 0.1979 0.1408 0.0734 -0.0124 0.0115  0.0177  85   THR A CA  
1078 C  C   . THR A 85  ? 0.1489 0.1468 0.0706 0.0234  0.0107  0.0079  85   THR A C   
1079 O  O   . THR A 85  ? 0.1437 0.2270 0.0953 0.0316  0.0256  -0.0001 85   THR A O   
1080 C  CB  . THR A 85  ? 0.3006 0.1470 0.0791 0.0209  0.0068  0.0242  85   THR A CB  
1081 O  OG1 . THR A 85  ? 0.2917 0.2092 0.1232 0.0888  -0.0266 0.0133  85   THR A OG1 
1082 C  CG2 . THR A 85  ? 0.5489 0.1429 0.1266 -0.0225 0.0071  0.0482  85   THR A CG2 
1083 N  N   . GLU A 86  ? 0.1182 0.1134 0.0807 0.0291  -0.0148 -0.0103 86   GLU A N   
1084 C  CA  A GLU A 86  ? 0.1077 0.1233 0.1269 0.0327  -0.0486 -0.0406 86   GLU A CA  
1085 C  CA  B GLU A 86  ? 0.1103 0.1273 0.0749 0.0312  -0.0108 -0.0295 86   GLU A CA  
1086 C  C   . GLU A 86  ? 0.0906 0.1045 0.0909 0.0161  -0.0001 -0.0184 86   GLU A C   
1087 O  O   . GLU A 86  ? 0.1317 0.1180 0.1191 0.0238  -0.0194 -0.0203 86   GLU A O   
1088 C  CB  A GLU A 86  ? 0.1332 0.1455 0.2086 0.0016  -0.0672 -0.0253 86   GLU A CB  
1089 C  CB  B GLU A 86  ? 0.1355 0.1276 0.1438 0.0068  -0.0432 0.0167  86   GLU A CB  
1090 C  CG  A GLU A 86  ? 0.1380 0.1193 0.2559 0.0428  -0.1087 -0.0562 86   GLU A CG  
1091 C  CG  B GLU A 86  ? 0.1601 0.2019 0.1664 -0.0696 -0.0410 0.0318  86   GLU A CG  
1092 C  CD  A GLU A 86  ? 0.1469 0.2160 0.1707 -0.0024 -0.0563 0.0130  86   GLU A CD  
1093 C  CD  B GLU A 86  ? 0.1967 0.2937 0.2030 -0.1168 -0.0867 0.0848  86   GLU A CD  
1094 O  OE1 A GLU A 86  ? 0.3047 0.2665 0.2936 -0.1236 -0.0523 -0.0237 86   GLU A OE1 
1095 O  OE1 B GLU A 86  ? 0.1211 0.2157 0.1498 -0.0554 -0.0150 -0.0063 86   GLU A OE1 
1096 O  OE2 A GLU A 86  ? 0.1421 0.2384 0.3968 0.0692  -0.1458 -0.1050 86   GLU A OE2 
1097 O  OE2 B GLU A 86  ? 0.1464 0.5678 0.2506 -0.1254 -0.0943 0.1828  86   GLU A OE2 
1099 N  N   . GLY A 87  ? 0.0945 0.1178 0.0680 0.0214  -0.0007 -0.0052 87   GLY A N   
1100 C  CA  . GLY A 87  ? 0.0915 0.1173 0.0809 0.0253  0.0056  0.0040  87   GLY A CA  
1101 C  C   . GLY A 87  ? 0.0804 0.1079 0.0699 0.0092  -0.0017 0.0034  87   GLY A C   
1102 O  O   . GLY A 87  ? 0.0895 0.1364 0.0910 -0.0109 0.0014  -0.0133 87   GLY A O   
1104 N  N   . SER A 88  ? 0.0803 0.0846 0.0775 0.0074  0.0038  -0.0090 88   SER A N   
1105 C  CA  . SER A 88  ? 0.0742 0.0926 0.0715 -0.0056 0.0008  -0.0124 88   SER A CA  
1106 C  C   . SER A 88  ? 0.0784 0.0896 0.0704 0.0066  0.0000  -0.0128 88   SER A C   
1107 O  O   . SER A 88  ? 0.0802 0.1055 0.1058 0.0081  -0.0109 -0.0299 88   SER A O   
1108 C  CB  . SER A 88  ? 0.1009 0.1138 0.0737 0.0244  -0.0021 -0.0116 88   SER A CB  
1109 O  OG  . SER A 88  ? 0.1203 0.1156 0.1151 0.0236  0.0355  0.0154  88   SER A OG  
1114 N  N   . THR A 89  ? 0.0766 0.0977 0.0816 0.0066  0.0030  -0.0165 89   THR A N   
1115 C  CA  . THR A 89  ? 0.0706 0.0978 0.0835 -0.0015 -0.0079 -0.0168 89   THR A CA  
1116 C  C   . THR A 89  ? 0.0781 0.0704 0.0732 0.0019  -0.0058 -0.0092 89   THR A C   
1117 O  O   . THR A 89  ? 0.0804 0.1439 0.0760 -0.0260 0.0099  -0.0274 89   THR A O   
1118 C  CB  . THR A 89  ? 0.0813 0.1316 0.0819 0.0184  0.0048  -0.0009 89   THR A CB  
1119 O  OG1 . THR A 89  ? 0.0895 0.1780 0.1019 0.0422  0.0052  0.0041  89   THR A OG1 
1120 C  CG2 . THR A 89  ? 0.1246 0.1033 0.0919 0.0180  0.0119  0.0055  89   THR A CG2 
1126 N  N   . THR A 90  ? 0.0763 0.0755 0.0867 -0.0029 0.0004  -0.0211 90   THR A N   
1127 C  CA  . THR A 90  ? 0.0739 0.0676 0.0890 0.0044  0.0027  -0.0080 90   THR A CA  
1128 C  C   . THR A 90  ? 0.0730 0.0748 0.0796 0.0008  -0.0075 -0.0138 90   THR A C   
1129 O  O   . THR A 90  ? 0.0871 0.0919 0.0749 0.0146  -0.0061 -0.0103 90   THR A O   
1130 C  CB  . THR A 90  ? 0.0767 0.0839 0.1049 -0.0024 0.0097  -0.0066 90   THR A CB  
1131 O  OG1 . THR A 90  ? 0.1010 0.0851 0.1510 -0.0224 -0.0005 -0.0066 90   THR A OG1 
1132 C  CG2 . THR A 90  ? 0.1033 0.0869 0.1200 0.0148  0.0056  0.0134  90   THR A CG2 
1138 N  N   . SER A 91  ? 0.0919 0.0765 0.1231 0.0103  0.0333  0.0024  91   SER A N   
1139 C  CA  A SER A 91  ? 0.0890 0.0658 0.1076 0.0028  -0.0191 -0.0047 91   SER A CA  
1140 C  CA  B SER A 91  ? 0.1088 0.0612 0.1085 0.0058  0.0007  -0.0137 91   SER A CA  
1141 C  C   . SER A 91  ? 0.0989 0.0705 0.0726 0.0059  -0.0009 -0.0053 91   SER A C   
1142 O  O   . SER A 91  ? 0.1078 0.0716 0.1109 0.0076  0.0034  -0.0051 91   SER A O   
1143 C  CB  A SER A 91  ? 0.1203 0.0958 0.0963 -0.0144 -0.0231 -0.0137 91   SER A CB  
1144 C  CB  B SER A 91  ? 0.1649 0.0116 0.1240 0.0033  -0.0278 -0.0288 91   SER A CB  
1145 O  OG  A SER A 91  ? 0.1756 0.1369 0.1098 0.0180  -0.0211 -0.0423 91   SER A OG  
1146 O  OG  B SER A 91  ? 0.0851 0.1163 0.1427 -0.0008 0.0082  -0.0123 91   SER A OG  
1148 N  N   . TYR A 92  ? 0.0996 0.0625 0.0606 0.0056  -0.0105 -0.0025 92   TYR A N   
1149 C  CA  . TYR A 92  ? 0.0965 0.0630 0.0575 0.0085  -0.0044 -0.0009 92   TYR A CA  
1150 C  C   . TYR A 92  ? 0.0813 0.0754 0.0655 -0.0013 -0.0141 0.0006  92   TYR A C   
1151 O  O   . TYR A 92  ? 0.0903 0.0972 0.1350 -0.0165 -0.0361 0.0377  92   TYR A O   
1152 C  CB  . TYR A 92  ? 0.0756 0.0724 0.0559 0.0023  -0.0030 -0.0013 92   TYR A CB  
1153 C  CG  . TYR A 92  ? 0.0695 0.0620 0.0557 0.0062  -0.0077 -0.0029 92   TYR A CG  
1154 C  CD1 . TYR A 92  ? 0.0916 0.0608 0.0592 0.0013  -0.0059 -0.0028 92   TYR A CD1 
1155 C  CD2 . TYR A 92  ? 0.0631 0.0646 0.0585 -0.0034 -0.0049 0.0033  92   TYR A CD2 
1156 C  CE1 . TYR A 92  ? 0.0818 0.0630 0.0559 0.0015  -0.0099 0.0014  92   TYR A CE1 
1157 C  CE2 . TYR A 92  ? 0.0660 0.0632 0.0547 0.0003  0.0030  -0.0001 92   TYR A CE2 
1158 C  CZ  . TYR A 92  ? 0.0583 0.0632 0.0555 0.0000  -0.0078 -0.0039 92   TYR A CZ  
1159 O  OH  . TYR A 92  ? 0.0731 0.0635 0.0515 -0.0038 0.0005  -0.0013 92   TYR A OH  
1167 N  N   . TYR A 93  ? 0.0763 0.0709 0.0623 0.0080  -0.0084 0.0053  93   TYR A N   
1168 C  CA  . TYR A 93  ? 0.0804 0.0690 0.0701 0.0075  -0.0131 0.0008  93   TYR A CA  
1169 C  C   . TYR A 93  ? 0.0736 0.0669 0.0723 0.0025  -0.0105 0.0052  93   TYR A C   
1170 O  O   . TYR A 93  ? 0.0726 0.0797 0.0870 0.0049  -0.0120 -0.0109 93   TYR A O   
1171 C  CB  . TYR A 93  ? 0.1119 0.0866 0.0641 0.0063  -0.0180 0.0072  93   TYR A CB  
1172 C  CG  . TYR A 93  ? 0.1323 0.1045 0.0654 0.0140  -0.0104 -0.0042 93   TYR A CG  
1173 C  CD1 . TYR A 93  ? 0.1520 0.1388 0.1106 0.0236  -0.0496 -0.0298 93   TYR A CD1 
1174 C  CD2 . TYR A 93  ? 0.1266 0.1212 0.0871 0.0090  0.0036  -0.0126 93   TYR A CD2 
1175 C  CE1 . TYR A 93  ? 0.1901 0.1714 0.1093 0.0524  -0.0574 -0.0450 93   TYR A CE1 
1176 C  CE2 . TYR A 93  ? 0.1685 0.1148 0.1161 0.0320  -0.0207 -0.0191 93   TYR A CE2 
1177 C  CZ  . TYR A 93  ? 0.1860 0.1440 0.1085 0.0261  -0.0378 -0.0387 93   TYR A CZ  
1178 O  OH  . TYR A 93  ? 0.2201 0.1715 0.1622 0.0293  -0.0377 -0.0780 93   TYR A OH  
1185 N  N   . ALA A 94  ? 0.0775 0.0605 0.0766 0.0007  -0.0023 0.0014  94   ALA A N   
1186 C  CA  . ALA A 94  ? 0.0802 0.0659 0.0604 0.0021  -0.0077 0.0047  94   ALA A CA  
1187 C  C   . ALA A 94  ? 0.0711 0.0638 0.0557 0.0083  -0.0013 -0.0021 94   ALA A C   
1188 O  O   . ALA A 94  ? 0.0906 0.0799 0.0639 -0.0037 -0.0132 0.0068  94   ALA A O   
1189 C  CB  . ALA A 94  ? 0.0812 0.0783 0.0822 0.0031  0.0029  0.0093  94   ALA A CB  
1195 N  N   . VAL A 95  ? 0.0806 0.0637 0.0484 0.0007  -0.0061 0.0011  95   VAL A N   
1196 C  CA  . VAL A 95  ? 0.0822 0.0593 0.0565 0.0105  -0.0056 0.0053  95   VAL A CA  
1197 C  C   . VAL A 95  ? 0.0883 0.0644 0.0511 0.0100  -0.0042 0.0026  95   VAL A C   
1198 O  O   . VAL A 95  ? 0.1313 0.0737 0.0582 0.0096  -0.0198 0.0049  95   VAL A O   
1199 C  CB  . VAL A 95  ? 0.0868 0.0723 0.0604 0.0034  0.0011  0.0086  95   VAL A CB  
1200 C  CG1 . VAL A 95  ? 0.0931 0.0903 0.0672 0.0139  0.0025  0.0015  95   VAL A CG1 
1201 C  CG2 . VAL A 95  ? 0.0886 0.1000 0.0742 -0.0021 -0.0011 0.0171  95   VAL A CG2 
1208 N  N   . ALA A 96  ? 0.0836 0.0659 0.0568 0.0060  0.0010  0.0038  96   ALA A N   
1209 C  CA  . ALA A 96  ? 0.0779 0.0670 0.0582 0.0034  0.0067  0.0041  96   ALA A CA  
1210 C  C   . ALA A 96  ? 0.0838 0.0667 0.0499 0.0026  0.0127  0.0070  96   ALA A C   
1211 O  O   . ALA A 96  ? 0.0890 0.1042 0.0553 -0.0007 0.0038  0.0155  96   ALA A O   
1212 C  CB  . ALA A 96  ? 0.0872 0.0724 0.0710 0.0134  0.0035  0.0091  96   ALA A CB  
1218 N  N   . VAL A 97  ? 0.0804 0.0754 0.0518 0.0015  0.0071  0.0046  97   VAL A N   
1219 C  CA  . VAL A 97  ? 0.0898 0.0687 0.0509 -0.0057 0.0069  0.0045  97   VAL A CA  
1220 C  C   . VAL A 97  ? 0.0765 0.0788 0.0511 -0.0051 0.0082  0.0050  97   VAL A C   
1221 O  O   . VAL A 97  ? 0.0822 0.0777 0.0581 -0.0053 0.0143  0.0025  97   VAL A O   
1222 C  CB  . VAL A 97  ? 0.0902 0.0858 0.0551 -0.0002 0.0079  -0.0009 97   VAL A CB  
1223 C  CG1 . VAL A 97  ? 0.0847 0.0880 0.0880 -0.0002 0.0147  -0.0030 97   VAL A CG1 
1224 C  CG2 . VAL A 97  ? 0.1002 0.0772 0.0736 0.0086  0.0014  0.0100  97   VAL A CG2 
1232 N  N   . VAL A 98  ? 0.0897 0.0683 0.0590 -0.0019 0.0110  0.0002  98   VAL A N   
1233 C  CA  . VAL A 98  ? 0.0989 0.0658 0.0766 -0.0003 0.0178  0.0070  98   VAL A CA  
1234 C  C   . VAL A 98  ? 0.1036 0.0833 0.0633 -0.0134 0.0098  0.0031  98   VAL A C   
1235 O  O   . VAL A 98  ? 0.1041 0.0845 0.0862 -0.0141 0.0321  -0.0060 98   VAL A O   
1236 C  CB  . VAL A 98  ? 0.1044 0.0806 0.0664 0.0027  0.0129  0.0067  98   VAL A CB  
1237 C  CG1 . VAL A 98  ? 0.1070 0.0899 0.0649 0.0050  0.0091  0.0005  98   VAL A CG1 
1238 C  CG2 . VAL A 98  ? 0.1260 0.0926 0.0747 0.0056  0.0183  0.0079  98   VAL A CG2 
1244 N  N   A LYS A 99  ? 0.1197 0.0738 0.0877 -0.0122 0.0216  0.0017  99   LYS A N   
1245 N  N   B LYS A 99  ? 0.1155 0.0769 0.0874 -0.0130 0.0220  0.0004  99   LYS A N   
1246 C  CA  A LYS A 99  ? 0.1114 0.0921 0.0874 -0.0202 0.0328  -0.0039 99   LYS A CA  
1247 C  CA  B LYS A 99  ? 0.1246 0.0903 0.0824 -0.0250 0.0345  -0.0043 99   LYS A CA  
1248 C  C   A LYS A 99  ? 0.1408 0.1139 0.0889 -0.0448 0.0264  -0.0129 99   LYS A C   
1249 C  C   B LYS A 99  ? 0.1576 0.1067 0.0803 -0.0282 0.0317  -0.0106 99   LYS A C   
1250 O  O   A LYS A 99  ? 0.1470 0.2044 0.0807 -0.0410 0.0220  0.0336  99   LYS A O   
1251 O  O   B LYS A 99  ? 0.1581 0.2114 0.0918 -0.0421 -0.0073 0.0005  99   LYS A O   
1252 C  CB  A LYS A 99  ? 0.1359 0.0819 0.0800 -0.0225 0.0191  0.0027  99   LYS A CB  
1253 C  CB  B LYS A 99  ? 0.1375 0.0804 0.0825 -0.0245 0.0197  0.0036  99   LYS A CB  
1254 C  CG  A LYS A 99  ? 0.1626 0.0998 0.0929 -0.0410 0.0000  0.0161  99   LYS A CG  
1255 C  CG  B LYS A 99  ? 0.1625 0.1033 0.0951 -0.0430 -0.0002 0.0146  99   LYS A CG  
1256 C  CD  A LYS A 99  ? 0.1868 0.1236 0.0928 -0.0606 -0.0092 0.0150  99   LYS A CD  
1257 C  CD  B LYS A 99  ? 0.2017 0.1249 0.0932 -0.0684 -0.0099 0.0173  99   LYS A CD  
1258 C  CE  A LYS A 99  ? 0.3110 0.1636 0.0948 -0.1171 -0.0414 0.0330  99   LYS A CE  
1259 C  CE  B LYS A 99  ? 0.2977 0.1548 0.0932 -0.0949 -0.0361 0.0243  99   LYS A CE  
1260 N  NZ  A LYS A 99  ? 0.3322 0.1367 0.1475 -0.0960 -0.0920 0.0274  99   LYS A NZ  
1261 N  NZ  B LYS A 99  ? 0.3596 0.1388 0.1389 -0.0907 -0.0969 0.0313  99   LYS A NZ  
1274 N  N   A LYS A 100 ? 0.1749 0.0995 0.0713 -0.0295 0.0412  0.0049  100  LYS A N   
1275 N  N   B LYS A 100 ? 0.1845 0.0852 0.0721 -0.0631 0.0373  -0.0070 100  LYS A N   
1276 C  CA  A LYS A 100 ? 0.1390 0.1050 0.0853 -0.0125 0.0257  0.0134  100  LYS A CA  
1277 C  CA  B LYS A 100 ? 0.1447 0.0958 0.1062 0.0027  0.0514  0.0261  100  LYS A CA  
1278 C  C   A LYS A 100 ? 0.1414 0.1178 0.1033 -0.0008 0.0370  0.0299  100  LYS A C   
1279 C  C   B LYS A 100 ? 0.2654 0.1080 0.1238 0.0364  0.0455  -0.0016 100  LYS A C   
1280 O  O   A LYS A 100 ? 0.2433 0.0952 0.1092 -0.0111 0.0209  0.0308  100  LYS A O   
1281 O  O   B LYS A 100 ? 0.1774 0.0938 0.2002 -0.0133 0.0836  -0.0002 100  LYS A O   
1282 C  CB  A LYS A 100 ? 0.1777 0.1070 0.0894 0.0111  0.0485  0.0275  100  LYS A CB  
1283 C  CB  B LYS A 100 ? 0.1675 0.1077 0.0772 0.0069  0.0444  0.0044  100  LYS A CB  
1284 C  CG  A LYS A 100 ? 0.2491 0.1312 0.0832 0.0155  0.0636  0.0068  100  LYS A CG  
1285 C  CG  B LYS A 100 ? 0.1458 0.1173 0.0978 -0.0322 0.0578  -0.0040 100  LYS A CG  
1286 C  CD  A LYS A 100 ? 0.1694 0.1191 0.0919 -0.0067 0.0233  -0.0144 100  LYS A CD  
1287 C  CD  B LYS A 100 ? 0.1764 0.1045 0.0573 -0.0160 0.0408  -0.0035 100  LYS A CD  
1288 C  CE  A LYS A 100 ? 0.2035 0.1332 0.1094 0.0067  -0.0230 -0.0458 100  LYS A CE  
1289 C  CE  B LYS A 100 ? 0.1385 0.1065 0.1361 0.0038  -0.0105 -0.0264 100  LYS A CE  
1290 N  NZ  A LYS A 100 ? 0.1786 0.1138 0.0840 0.0150  -0.0285 0.0020  100  LYS A NZ  
1291 N  NZ  B LYS A 100 ? 0.2164 0.1506 0.2297 0.0531  0.0773  0.0091  100  LYS A NZ  
1292 N  N   A GLY A 101 ? 0.1845 0.1347 0.1046 0.0120  0.0239  0.0451  101  GLY A N   
1293 N  N   B GLY A 101 ? 0.3087 0.1054 0.1756 0.0337  0.0266  0.0480  101  GLY A N   
1294 C  CA  A GLY A 101 ? 0.1604 0.1167 0.1248 0.0025  0.0215  0.0330  101  GLY A CA  
1295 C  CA  B GLY A 101 ? 0.3119 0.0902 0.1569 0.0042  0.0355  0.0279  101  GLY A CA  
1296 C  C   A GLY A 101 ? 0.2477 0.1366 0.1124 0.0372  0.0549  0.0537  101  GLY A C   
1297 C  C   B GLY A 101 ? 0.2934 0.1335 0.1741 0.0281  0.0292  0.0325  101  GLY A C   
1298 O  O   A GLY A 101 ? 0.2561 0.1230 0.1529 0.0418  0.0584  0.0572  101  GLY A O   
1299 O  O   B GLY A 101 ? 0.3331 0.1724 0.3360 0.1043  0.1527  0.1564  101  GLY A O   
1300 N  N   A THR A 102 ? 0.1861 0.1156 0.1240 0.0161  0.0416  0.0453  102  THR A N   
1301 N  N   B THR A 102 ? 0.2478 0.0949 0.1349 0.0185  -0.0073 0.0003  102  THR A N   
1302 C  CA  A THR A 102 ? 0.1997 0.1224 0.1132 0.0208  0.0383  0.0218  102  THR A CA  
1303 C  CA  B THR A 102 ? 0.2577 0.1280 0.1685 0.0446  0.0111  0.0228  102  THR A CA  
1304 C  C   A THR A 102 ? 0.1980 0.0927 0.1184 0.0277  0.0400  0.0069  102  THR A C   
1305 C  C   B THR A 102 ? 0.2505 0.0730 0.1774 0.0256  0.0234  0.0460  102  THR A C   
1306 O  O   A THR A 102 ? 0.2119 0.1335 0.1295 0.0706  0.0247  0.0052  102  THR A O   
1307 O  O   B THR A 102 ? 0.2710 0.1588 0.2037 0.0960  0.0182  0.0446  102  THR A O   
1308 C  CB  A THR A 102 ? 0.2138 0.1052 0.1159 -0.0188 0.0334  0.0349  102  THR A CB  
1309 C  CB  B THR A 102 ? 0.2270 0.1308 0.1634 -0.0446 0.0042  0.0235  102  THR A CB  
1310 O  OG1 A THR A 102 ? 0.2439 0.1095 0.1784 -0.0392 -0.0130 0.0562  102  THR A OG1 
1311 O  OG1 B THR A 102 ? 0.1232 0.1398 0.0794 -0.0061 -0.0023 0.0177  102  THR A OG1 
1312 C  CG2 A THR A 102 ? 0.2222 0.1163 0.1552 -0.0324 0.0035  0.0765  102  THR A CG2 
1313 C  CG2 B THR A 102 ? 0.2949 0.1765 0.2051 -0.1073 -0.0481 0.0467  102  THR A CG2 
1314 N  N   A GLU A 103 ? 0.2393 0.1060 0.0851 0.0294  0.0340  0.0216  103  GLU A N   
1315 N  N   B GLU A 103 ? 0.2563 0.1343 0.1976 0.0143  0.0129  0.0099  103  GLU A N   
1316 C  CA  A GLU A 103 ? 0.2554 0.1190 0.1091 0.0632  0.0073  0.0217  103  GLU A CA  
1317 C  CA  B GLU A 103 ? 0.2964 0.1936 0.1818 -0.0046 -0.0161 0.0659  103  GLU A CA  
1318 C  C   A GLU A 103 ? 0.2498 0.1218 0.1112 0.0495  -0.0094 0.0297  103  GLU A C   
1319 C  C   B GLU A 103 ? 0.2919 0.1990 0.1723 -0.0155 -0.0364 0.0628  103  GLU A C   
1320 O  O   A GLU A 103 ? 0.2477 0.2077 0.1128 0.0484  -0.0069 -0.0054 103  GLU A O   
1321 O  O   B GLU A 103 ? 0.3135 0.2918 0.1754 -0.0386 -0.0656 0.0928  103  GLU A O   
1322 C  CB  A GLU A 103 ? 0.3614 0.1485 0.1342 0.0549  0.0233  0.0711  103  GLU A CB  
1323 C  CB  B GLU A 103 ? 0.3991 0.2190 0.2044 0.0122  0.0346  0.0950  103  GLU A CB  
1324 C  CG  A GLU A 103 ? 0.4720 0.2157 0.2762 0.0594  0.1594  0.0921  103  GLU A CG  
1325 C  CG  B GLU A 103 ? 0.4884 0.2429 0.2559 0.0753  0.1462  0.0972  103  GLU A CG  
1326 C  CD  A GLU A 103 ? 0.5760 0.3900 0.2737 0.0413  0.1358  0.2349  103  GLU A CD  
1327 C  CD  B GLU A 103 ? 0.5784 0.3811 0.3178 0.0458  0.1514  0.1983  103  GLU A CD  
1328 O  OE1 A GLU A 103 ? 0.5817 0.4208 0.4666 0.1486  0.1711  0.2661  103  GLU A OE1 
1329 O  OE1 B GLU A 103 ? 0.6192 0.5845 0.4265 -0.0869 0.1005  0.3045  103  GLU A OE1 
1330 O  OE2 A GLU A 103 ? 0.7328 0.3804 0.5627 -0.0925 -0.0227 0.3063  103  GLU A OE2 
1331 O  OE2 B GLU A 103 ? 0.6318 0.4021 0.4008 0.1426  0.1952  0.2904  103  GLU A OE2 
1332 N  N   A PHE A 104 ? 0.2428 0.1678 0.1199 -0.0073 0.0056  0.0045  104  PHE A N   
1333 N  N   B PHE A 104 ? 0.2559 0.1599 0.1656 0.0066  -0.0613 0.1141  104  PHE A N   
1334 C  CA  A PHE A 104 ? 0.2171 0.1469 0.1567 0.0326  0.0009  0.0459  104  PHE A CA  
1335 C  CA  B PHE A 104 ? 0.2281 0.1511 0.1776 0.0301  -0.0512 0.0528  104  PHE A CA  
1336 C  C   A PHE A 104 ? 0.1871 0.1524 0.1001 0.0263  -0.0109 0.0200  104  PHE A C   
1337 C  C   B PHE A 104 ? 0.1916 0.1589 0.1059 0.0232  -0.0239 0.0245  104  PHE A C   
1338 O  O   A PHE A 104 ? 0.1759 0.1446 0.1220 0.0212  -0.0084 0.0136  104  PHE A O   
1339 O  O   B PHE A 104 ? 0.1726 0.1513 0.1234 0.0123  -0.0119 0.0129  104  PHE A O   
1340 C  CB  A PHE A 104 ? 0.1541 0.1320 0.1863 0.0564  -0.0076 0.0057  104  PHE A CB  
1341 C  CB  B PHE A 104 ? 0.2037 0.1248 0.2125 0.0355  -0.0639 0.0036  104  PHE A CB  
1342 C  CG  A PHE A 104 ? 0.1553 0.0995 0.1607 0.0463  -0.0147 -0.0073 104  PHE A CG  
1343 C  CG  B PHE A 104 ? 0.1590 0.1026 0.1577 0.0395  -0.0198 -0.0067 104  PHE A CG  
1344 C  CD1 A PHE A 104 ? 0.1299 0.1132 0.1323 0.0261  0.0075  -0.0172 104  PHE A CD1 
1345 C  CD1 B PHE A 104 ? 0.1362 0.1158 0.1227 0.0256  0.0077  -0.0127 104  PHE A CD1 
1346 C  CD2 A PHE A 104 ? 0.1801 0.1002 0.1794 0.0169  -0.0164 0.0158  104  PHE A CD2 
1347 C  CD2 B PHE A 104 ? 0.1689 0.0967 0.1846 0.0275  -0.0235 0.0075  104  PHE A CD2 
1348 C  CE1 A PHE A 104 ? 0.1646 0.1087 0.1031 0.0161  0.0112  -0.0129 104  PHE A CE1 
1349 C  CE1 B PHE A 104 ? 0.1548 0.1101 0.1036 0.0226  0.0111  -0.0097 104  PHE A CE1 
1350 C  CE2 A PHE A 104 ? 0.1486 0.1063 0.1462 0.0241  -0.0072 -0.0125 104  PHE A CE2 
1351 C  CE2 B PHE A 104 ? 0.1465 0.0996 0.1432 0.0331  -0.0064 -0.0140 104  PHE A CE2 
1352 C  CZ  A PHE A 104 ? 0.1431 0.1158 0.0976 0.0330  0.0103  -0.0149 104  PHE A CZ  
1353 C  CZ  B PHE A 104 ? 0.1440 0.1122 0.0969 0.0316  0.0109  -0.0129 104  PHE A CZ  
1364 N  N   . THR A 105 ? 0.1772 0.1697 0.1232 0.0401  -0.0174 0.0069  105  THR A N   
1365 C  CA  . THR A 105 ? 0.1570 0.1661 0.1040 0.0356  0.0079  -0.0057 105  THR A CA  
1366 C  C   . THR A 105 ? 0.1367 0.1702 0.0901 0.0462  -0.0042 -0.0050 105  THR A C   
1367 O  O   . THR A 105 ? 0.1415 0.1618 0.0985 0.0445  -0.0103 -0.0038 105  THR A O   
1368 C  CB  . THR A 105 ? 0.1605 0.2060 0.0944 0.0056  0.0167  0.0104  105  THR A CB  
1369 O  OG1 . THR A 105 ? 0.1769 0.2480 0.0930 0.0487  -0.0076 0.0228  105  THR A OG1 
1370 C  CG2 . THR A 105 ? 0.2494 0.2819 0.1100 0.0079  0.0275  0.0418  105  THR A CG2 
1372 N  N   . VAL A 106 ? 0.1498 0.1702 0.0842 0.0459  -0.0021 -0.0006 106  VAL A N   
1373 C  CA  . VAL A 106 ? 0.1223 0.1899 0.0859 0.0572  0.0026  0.0090  106  VAL A CA  
1374 C  C   . VAL A 106 ? 0.1499 0.2089 0.0796 0.0633  0.0031  0.0146  106  VAL A C   
1375 O  O   . VAL A 106 ? 0.1760 0.3241 0.1036 0.1370  0.0317  0.0449  106  VAL A O   
1376 C  CB  . VAL A 106 ? 0.1094 0.1900 0.1008 0.0513  0.0061  0.0262  106  VAL A CB  
1377 C  CG1 . VAL A 106 ? 0.1201 0.2073 0.1143 0.0393  0.0003  -0.0043 106  VAL A CG1 
1378 C  CG2 . VAL A 106 ? 0.1604 0.2431 0.1353 0.0404  0.0300  0.0552  106  VAL A CG2 
1383 N  N   . ASN A 107 ? 0.1343 0.1565 0.0942 0.0564  -0.0125 0.0010  107  ASN A N   
1384 C  CA  . ASN A 107 ? 0.1300 0.1748 0.1149 0.0552  0.0027  0.0092  107  ASN A CA  
1385 C  C   . ASN A 107 ? 0.1447 0.1807 0.1038 0.0706  0.0068  0.0128  107  ASN A C   
1386 O  O   . ASN A 107 ? 0.1512 0.1878 0.1751 0.0781  0.0023  -0.0036 107  ASN A O   
1387 C  CB  . ASN A 107 ? 0.1324 0.1972 0.1449 0.0529  -0.0307 0.0163  107  ASN A CB  
1388 C  CG  . ASN A 107 ? 0.1332 0.2281 0.1502 0.0387  -0.0279 -0.0041 107  ASN A CG  
1389 O  OD1 . ASN A 107 ? 0.1789 0.2465 0.1974 -0.0203 -0.0134 -0.0263 107  ASN A OD1 
1390 N  ND2 . ASN A 107 ? 0.2563 0.2820 0.1564 0.0461  -0.0097 -0.0280 107  ASN A ND2 
1393 N  N   . ASP A 108 ? 0.1625 0.1579 0.0984 0.0633  0.0063  0.0057  108  ASP A N   
1394 C  CA  . ASP A 108 ? 0.1697 0.1484 0.1261 0.0504  0.0092  0.0241  108  ASP A CA  
1395 C  C   . ASP A 108 ? 0.1478 0.1120 0.1243 0.0370  0.0102  0.0161  108  ASP A C   
1396 O  O   . ASP A 108 ? 0.1610 0.1317 0.1712 0.0152  -0.0075 0.0342  108  ASP A O   
1397 C  CB  . ASP A 108 ? 0.2839 0.1612 0.1689 0.0641  0.0741  0.0701  108  ASP A CB  
1398 C  CG  . ASP A 108 ? 0.3122 0.3148 0.1831 0.1723  0.0691  0.1306  108  ASP A CG  
1399 O  OD1 . ASP A 108 ? 0.3137 0.4611 0.2084 0.2146  0.0724  0.1016  108  ASP A OD1 
1400 O  OD2 . ASP A 108 ? 0.2832 0.2966 0.1433 0.1523  0.0269  0.0595  108  ASP A OD2 
1402 N  N   . LEU A 109 ? 0.1374 0.1087 0.0989 0.0475  0.0053  0.0048  109  LEU A N   
1403 C  CA  . LEU A 109 ? 0.1177 0.1012 0.0967 0.0321  0.0006  -0.0044 109  LEU A CA  
1404 C  C   . LEU A 109 ? 0.1326 0.0872 0.0999 0.0416  0.0011  -0.0016 109  LEU A C   
1405 O  O   . LEU A 109 ? 0.1212 0.0967 0.1017 0.0418  -0.0031 -0.0042 109  LEU A O   
1406 C  CB  . LEU A 109 ? 0.1212 0.0965 0.0943 0.0394  0.0028  0.0023  109  LEU A CB  
1407 C  CG  . LEU A 109 ? 0.1320 0.0992 0.0888 0.0362  0.0056  -0.0023 109  LEU A CG  
1408 C  CD1 . LEU A 109 ? 0.1540 0.0948 0.1057 0.0420  0.0197  0.0121  109  LEU A CD1 
1409 C  CD2 . LEU A 109 ? 0.1226 0.1405 0.1634 0.0375  0.0242  -0.0311 109  LEU A CD2 
1416 N  N   . GLN A 110 ? 0.1224 0.0930 0.1150 0.0273  -0.0029 -0.0096 110  GLN A N   
1417 C  CA  . GLN A 110 ? 0.1164 0.1023 0.1030 0.0394  0.0053  -0.0044 110  GLN A CA  
1418 C  C   . GLN A 110 ? 0.1247 0.0916 0.1062 0.0448  -0.0125 -0.0056 110  GLN A C   
1419 O  O   . GLN A 110 ? 0.1320 0.1086 0.1137 0.0282  -0.0110 0.0039  110  GLN A O   
1420 C  CB  . GLN A 110 ? 0.1309 0.1014 0.1155 0.0347  -0.0094 -0.0073 110  GLN A CB  
1421 C  CG  . GLN A 110 ? 0.1195 0.0960 0.1532 0.0347  0.0018  -0.0157 110  GLN A CG  
1422 C  CD  . GLN A 110 ? 0.1273 0.0916 0.1191 0.0458  0.0015  0.0137  110  GLN A CD  
1423 O  OE1 . GLN A 110 ? 0.1279 0.1006 0.1550 0.0454  0.0031  0.0152  110  GLN A OE1 
1424 N  NE2 . GLN A 110 ? 0.1777 0.0993 0.1133 0.0421  -0.0114 -0.0038 110  GLN A NE2 
1429 N  N   . GLY A 111 ? 0.1210 0.0912 0.1132 0.0449  -0.0103 -0.0024 111  GLY A N   
1430 C  CA  . GLY A 111 ? 0.1399 0.0931 0.0988 0.0408  -0.0177 -0.0063 111  GLY A CA  
1431 C  C   . GLY A 111 ? 0.1271 0.0898 0.1170 0.0240  -0.0109 0.0064  111  GLY A C   
1432 O  O   . GLY A 111 ? 0.1604 0.1012 0.1465 0.0106  -0.0173 -0.0159 111  GLY A O   
1435 N  N   . LYS A 112 ? 0.1121 0.0940 0.0997 0.0211  -0.0103 0.0056  112  LYS A N   
1436 C  CA  . LYS A 112 ? 0.1058 0.0940 0.0928 0.0178  -0.0075 0.0069  112  LYS A CA  
1437 C  C   . LYS A 112 ? 0.1113 0.0770 0.0909 0.0258  0.0048  0.0100  112  LYS A C   
1438 O  O   . LYS A 112 ? 0.1070 0.0949 0.1113 0.0126  0.0043  0.0220  112  LYS A O   
1439 C  CB  . LYS A 112 ? 0.1168 0.1094 0.0900 0.0299  -0.0046 0.0036  112  LYS A CB  
1440 C  CG  . LYS A 112 ? 0.1884 0.1353 0.0929 0.0102  0.0093  0.0085  112  LYS A CG  
1441 C  CD  . LYS A 112 ? 0.2381 0.1904 0.1142 -0.0480 -0.0270 0.0366  112  LYS A CD  
1442 C  CE  . LYS A 112 ? 0.2918 0.2607 0.1261 0.0368  0.0229  0.0840  112  LYS A CE  
1443 N  NZ  . LYS A 112 ? 0.2853 0.1606 0.2022 -0.0301 -0.0645 0.0521  112  LYS A NZ  
1446 N  N   . THR A 113 ? 0.1106 0.0698 0.0914 0.0073  0.0017  0.0130  113  THR A N   
1447 C  CA  . THR A 113 ? 0.1035 0.0785 0.0773 0.0214  0.0045  0.0088  113  THR A CA  
1448 C  C   . THR A 113 ? 0.0942 0.0673 0.0739 0.0080  0.0062  0.0126  113  THR A C   
1449 O  O   . THR A 113 ? 0.1132 0.0756 0.0691 0.0054  0.0124  0.0103  113  THR A O   
1450 C  CB  . THR A 113 ? 0.1086 0.0712 0.0845 0.0131  0.0015  0.0039  113  THR A CB  
1451 O  OG1 . THR A 113 ? 0.1234 0.0773 0.0946 0.0028  0.0185  0.0086  113  THR A OG1 
1452 C  CG2 . THR A 113 ? 0.1228 0.0924 0.1029 0.0139  0.0194  -0.0010 113  THR A CG2 
1457 N  N   . SER A 114 ? 0.0962 0.0646 0.0657 0.0123  0.0105  0.0064  114  SER A N   
1458 C  CA  . SER A 114 ? 0.0892 0.0642 0.0676 0.0116  0.0096  0.0041  114  SER A CA  
1459 C  C   . SER A 114 ? 0.0876 0.0603 0.0678 -0.0034 0.0083  0.0078  114  SER A C   
1460 O  O   . SER A 114 ? 0.1062 0.0773 0.0597 0.0247  0.0073  -0.0001 114  SER A O   
1461 C  CB  . SER A 114 ? 0.0957 0.0765 0.0637 0.0111  0.0046  -0.0007 114  SER A CB  
1462 O  OG  . SER A 114 ? 0.0847 0.0811 0.0794 0.0110  0.0116  0.0050  114  SER A OG  
1467 N  N   . CYS A 115 ? 0.0884 0.0572 0.0543 0.0075  0.0032  0.0019  115  CYS A N   
1468 C  CA  . CYS A 115 ? 0.0771 0.0582 0.0566 0.0040  0.0092  0.0038  115  CYS A CA  
1469 C  C   . CYS A 115 ? 0.0781 0.0649 0.0481 0.0094  0.0119  0.0002  115  CYS A C   
1470 O  O   . CYS A 115 ? 0.0941 0.0679 0.0568 0.0030  0.0141  0.0011  115  CYS A O   
1471 C  CB  . CYS A 115 ? 0.0816 0.0627 0.0798 0.0032  0.0066  0.0018  115  CYS A CB  
1472 S  SG  . CYS A 115 ? 0.0880 0.0688 0.0992 -0.0045 0.0068  0.0141  115  CYS A SG  
1477 N  N   . HIS A 116 ? 0.0774 0.0576 0.0589 -0.0028 0.0110  0.0005  116  HIS A N   
1478 C  CA  . HIS A 116 ? 0.0838 0.0529 0.0573 0.0010  0.0046  0.0026  116  HIS A CA  
1479 C  C   . HIS A 116 ? 0.0691 0.0552 0.0511 0.0001  0.0047  -0.0009 116  HIS A C   
1480 O  O   . HIS A 116 ? 0.0786 0.0662 0.0590 0.0041  0.0010  0.0004  116  HIS A O   
1481 C  CB  . HIS A 116 ? 0.0653 0.0596 0.0664 -0.0010 0.0061  -0.0019 116  HIS A CB  
1482 C  CG  . HIS A 116 ? 0.0723 0.0614 0.0659 0.0054  0.0113  -0.0005 116  HIS A CG  
1483 N  ND1 . HIS A 116 ? 0.0793 0.0641 0.0784 0.0051  0.0002  0.0020  116  HIS A ND1 
1484 C  CD2 . HIS A 116 ? 0.0800 0.0645 0.0804 0.0109  0.0086  0.0012  116  HIS A CD2 
1485 C  CE1 . HIS A 116 ? 0.0714 0.0729 0.0854 0.0118  0.0019  0.0064  116  HIS A CE1 
1486 N  NE2 . HIS A 116 ? 0.0810 0.0702 0.0817 0.0091  0.0078  0.0072  116  HIS A NE2 
1493 N  N   . THR A 117 ? 0.0628 0.0574 0.0598 -0.0016 -0.0059 0.0032  117  THR A N   
1494 C  CA  . THR A 117 ? 0.0556 0.0610 0.0565 0.0001  -0.0006 0.0045  117  THR A CA  
1495 C  C   . THR A 117 ? 0.0600 0.0528 0.0593 0.0017  0.0071  -0.0062 117  THR A C   
1496 O  O   . THR A 117 ? 0.0643 0.0680 0.0549 0.0032  -0.0001 -0.0010 117  THR A O   
1497 C  CB  . THR A 117 ? 0.0617 0.0662 0.0574 0.0066  0.0005  -0.0043 117  THR A CB  
1498 O  OG1 . THR A 117 ? 0.0657 0.0624 0.0618 -0.0016 0.0051  -0.0035 117  THR A OG1 
1499 C  CG2 . THR A 117 ? 0.0648 0.0770 0.0615 -0.0002 0.0048  -0.0024 117  THR A CG2 
1506 N  N   . GLY A 118 ? 0.0651 0.0739 0.0532 -0.0028 0.0000  -0.0016 118  GLY A N   
1507 C  CA  . GLY A 118 ? 0.0683 0.0714 0.0551 0.0020  0.0054  -0.0033 118  GLY A CA  
1508 C  C   . GLY A 118 ? 0.0728 0.0665 0.0501 0.0051  -0.0002 -0.0004 118  GLY A C   
1509 O  O   . GLY A 118 ? 0.0659 0.0839 0.0603 -0.0006 0.0031  -0.0066 118  GLY A O   
1513 N  N   . LEU A 119 ? 0.0696 0.0697 0.0573 -0.0007 0.0065  -0.0083 119  LEU A N   
1514 C  CA  . LEU A 119 ? 0.0679 0.0746 0.0601 -0.0031 0.0073  -0.0068 119  LEU A CA  
1515 C  C   . LEU A 119 ? 0.0666 0.0745 0.0602 0.0008  0.0133  0.0010  119  LEU A C   
1516 O  O   . LEU A 119 ? 0.0846 0.0803 0.0751 -0.0030 -0.0036 0.0025  119  LEU A O   
1517 C  CB  . LEU A 119 ? 0.0810 0.0741 0.0670 -0.0008 0.0137  -0.0050 119  LEU A CB  
1518 C  CG  . LEU A 119 ? 0.0746 0.0995 0.0858 0.0086  0.0202  -0.0099 119  LEU A CG  
1519 C  CD1 . LEU A 119 ? 0.0880 0.2241 0.1005 0.0490  0.0272  0.0239  119  LEU A CD1 
1520 C  CD2 . LEU A 119 ? 0.1010 0.1155 0.0903 0.0100  0.0268  -0.0155 119  LEU A CD2 
1530 N  N   . GLY A 120 ? 0.0746 0.0744 0.0589 0.0012  0.0079  -0.0059 120  GLY A N   
1531 C  CA  . GLY A 120 ? 0.0634 0.0820 0.0734 -0.0033 0.0101  -0.0135 120  GLY A CA  
1532 C  C   . GLY A 120 ? 0.0729 0.0731 0.0622 0.0001  0.0108  -0.0002 120  GLY A C   
1533 O  O   . GLY A 120 ? 0.0777 0.0758 0.0892 -0.0098 0.0134  -0.0055 120  GLY A O   
1537 N  N   . ARG A 121 ? 0.0690 0.0626 0.0639 -0.0009 0.0104  -0.0034 121  ARG A N   
1538 C  CA  . ARG A 121 ? 0.0616 0.0625 0.0558 0.0060  0.0066  0.0006  121  ARG A CA  
1539 C  C   . ARG A 121 ? 0.0603 0.0516 0.0652 0.0007  0.0041  0.0018  121  ARG A C   
1540 O  O   . ARG A 121 ? 0.0753 0.0716 0.0718 0.0111  -0.0047 -0.0039 121  ARG A O   
1541 C  CB  . ARG A 121 ? 0.0647 0.0642 0.0538 0.0053  0.0071  0.0014  121  ARG A CB  
1542 C  CG  . ARG A 121 ? 0.0719 0.0773 0.0492 0.0020  0.0035  -0.0051 121  ARG A CG  
1543 C  CD  . ARG A 121 ? 0.0703 0.0710 0.0575 0.0022  0.0020  -0.0080 121  ARG A CD  
1544 N  NE  . ARG A 121 ? 0.0636 0.0641 0.0589 0.0013  -0.0023 -0.0040 121  ARG A NE  
1545 C  CZ  . ARG A 121 ? 0.0670 0.0619 0.0533 -0.0036 -0.0051 0.0059  121  ARG A CZ  
1546 N  NH1 . ARG A 121 ? 0.0635 0.0734 0.0584 -0.0042 -0.0031 0.0001  121  ARG A NH1 
1547 N  NH2 . ARG A 121 ? 0.0612 0.0794 0.0580 0.0030  -0.0039 -0.0089 121  ARG A NH2 
1561 N  N   . SER A 122 ? 0.0606 0.0678 0.0570 0.0060  -0.0041 -0.0016 122  SER A N   
1562 C  CA  . SER A 122 ? 0.0679 0.0729 0.0543 -0.0016 0.0035  -0.0004 122  SER A CA  
1563 C  C   . SER A 122 ? 0.0643 0.0636 0.0544 0.0063  -0.0031 -0.0043 122  SER A C   
1564 O  O   . SER A 122 ? 0.0648 0.0746 0.0647 0.0070  -0.0024 0.0056  122  SER A O   
1565 C  CB  . SER A 122 ? 0.1249 0.0604 0.0518 -0.0020 -0.0085 0.0032  122  SER A CB  
1566 O  OG  . SER A 122 ? 0.1286 0.0785 0.0790 -0.0260 -0.0180 0.0075  122  SER A OG  
1570 N  N   . ALA A 123 ? 0.0618 0.0636 0.0562 0.0090  0.0044  0.0032  123  ALA A N   
1571 C  CA  . ALA A 123 ? 0.0674 0.0664 0.0639 0.0063  0.0079  0.0078  123  ALA A CA  
1572 C  C   . ALA A 123 ? 0.0627 0.0645 0.0639 0.0054  -0.0030 0.0075  123  ALA A C   
1573 O  O   . ALA A 123 ? 0.0673 0.0701 0.0752 0.0067  0.0016  0.0089  123  ALA A O   
1574 C  CB  . ALA A 123 ? 0.0763 0.0854 0.0645 0.0176  0.0113  0.0133  123  ALA A CB  
1578 N  N   . GLY A 124 ? 0.0688 0.0619 0.0592 0.0026  0.0034  0.0098  124  GLY A N   
1579 C  CA  . GLY A 124 ? 0.0687 0.0599 0.0645 -0.0005 -0.0022 0.0022  124  GLY A CA  
1580 C  C   . GLY A 124 ? 0.0830 0.0655 0.0584 0.0000  -0.0073 0.0003  124  GLY A C   
1581 O  O   . GLY A 124 ? 0.0824 0.0590 0.0990 0.0056  -0.0051 -0.0021 124  GLY A O   
1585 N  N   . TRP A 125 ? 0.0664 0.0613 0.0717 0.0077  0.0030  0.0014  125  TRP A N   
1586 C  CA  . TRP A 125 ? 0.0709 0.0610 0.0695 0.0080  0.0040  0.0044  125  TRP A CA  
1587 C  C   . TRP A 125 ? 0.0685 0.0714 0.0584 0.0082  0.0084  -0.0003 125  TRP A C   
1588 O  O   . TRP A 125 ? 0.0671 0.0779 0.0687 0.0127  -0.0014 0.0044  125  TRP A O   
1589 C  CB  . TRP A 125 ? 0.0809 0.0747 0.0675 0.0107  -0.0054 -0.0099 125  TRP A CB  
1590 C  CG  . TRP A 125 ? 0.0850 0.0810 0.0567 0.0188  -0.0017 -0.0045 125  TRP A CG  
1591 C  CD1 . TRP A 125 ? 0.0941 0.0863 0.0871 0.0167  0.0170  0.0169  125  TRP A CD1 
1592 C  CD2 . TRP A 125 ? 0.0812 0.0825 0.0643 0.0225  -0.0031 -0.0082 125  TRP A CD2 
1593 N  NE1 . TRP A 125 ? 0.0865 0.1082 0.0971 0.0230  0.0117  0.0100  125  TRP A NE1 
1594 C  CE2 . TRP A 125 ? 0.0940 0.0987 0.0739 0.0337  0.0053  0.0063  125  TRP A CE2 
1595 C  CE3 . TRP A 125 ? 0.0929 0.0788 0.0946 0.0198  -0.0159 0.0007  125  TRP A CE3 
1596 C  CZ2 . TRP A 125 ? 0.1007 0.1132 0.0937 0.0416  -0.0067 -0.0093 125  TRP A CZ2 
1597 C  CZ3 . TRP A 125 ? 0.1172 0.0914 0.1254 0.0253  -0.0316 -0.0184 125  TRP A CZ3 
1598 C  CH2 . TRP A 125 ? 0.1246 0.1022 0.1198 0.0409  -0.0283 -0.0218 125  TRP A CH2 
1605 N  N   . ASN A 126 ? 0.0687 0.0629 0.0775 0.0037  0.0050  0.0030  126  ASN A N   
1606 C  CA  . ASN A 126 ? 0.0672 0.0791 0.0752 0.0051  0.0051  0.0022  126  ASN A CA  
1607 C  C   . ASN A 126 ? 0.0668 0.0709 0.0783 0.0065  -0.0004 0.0064  126  ASN A C   
1608 O  O   . ASN A 126 ? 0.0641 0.0919 0.0895 0.0068  -0.0009 0.0065  126  ASN A O   
1609 C  CB  . ASN A 126 ? 0.0821 0.0777 0.0820 -0.0087 -0.0048 0.0062  126  ASN A CB  
1610 C  CG  . ASN A 126 ? 0.1017 0.0801 0.0879 -0.0048 0.0005  0.0053  126  ASN A CG  
1611 O  OD1 . ASN A 126 ? 0.1206 0.0941 0.0914 0.0044  0.0191  0.0075  126  ASN A OD1 
1612 N  ND2 . ASN A 126 ? 0.1768 0.0777 0.0991 -0.0020 -0.0009 0.0160  126  ASN A ND2 
1616 N  N   . ILE A 127 ? 0.0651 0.0742 0.0752 0.0024  0.0008  0.0024  127  ILE A N   
1617 C  CA  . ILE A 127 ? 0.0617 0.0765 0.0756 0.0109  0.0006  -0.0016 127  ILE A CA  
1618 C  C   . ILE A 127 ? 0.0630 0.0791 0.0704 0.0120  0.0016  0.0026  127  ILE A C   
1619 O  O   . ILE A 127 ? 0.0699 0.0940 0.0802 0.0172  -0.0119 0.0014  127  ILE A O   
1620 C  CB  A ILE A 127 ? 0.0664 0.0640 0.0790 0.0005  0.0013  -0.0075 127  ILE A CB  
1621 C  CB  B ILE A 127 ? 0.0666 0.0809 0.0725 0.0195  -0.0094 -0.0107 127  ILE A CB  
1622 C  CG1 A ILE A 127 ? 0.0674 0.0605 0.0988 0.0040  -0.0236 -0.0086 127  ILE A CG1 
1623 C  CG1 B ILE A 127 ? 0.0741 0.0784 0.0982 0.0063  0.0242  -0.0054 127  ILE A CG1 
1624 C  CG2 A ILE A 127 ? 0.0777 0.0575 0.0788 -0.0063 0.0098  -0.0102 127  ILE A CG2 
1625 C  CG2 B ILE A 127 ? 0.0746 0.0813 0.0752 0.0011  0.0097  -0.0094 127  ILE A CG2 
1626 C  CD1 A ILE A 127 ? 0.0779 0.0642 0.0723 0.0047  0.0030  -0.0038 127  ILE A CD1 
1627 C  CD1 B ILE A 127 ? 0.0925 0.0869 0.0920 0.0092  0.0052  -0.0088 127  ILE A CD1 
1635 N  N   . PRO A 128 ? 0.0628 0.0761 0.0719 0.0131  0.0023  0.0009  128  PRO A N   
1636 C  CA  . PRO A 128 ? 0.0752 0.0828 0.0651 0.0157  0.0033  0.0110  128  PRO A CA  
1637 C  C   . PRO A 128 ? 0.0683 0.0733 0.0804 0.0136  0.0033  0.0062  128  PRO A C   
1638 O  O   . PRO A 128 ? 0.0809 0.0938 0.0765 0.0213  0.0000  0.0034  128  PRO A O   
1639 C  CB  . PRO A 128 ? 0.0704 0.0909 0.0872 0.0048  0.0126  0.0193  128  PRO A CB  
1640 C  CG  . PRO A 128 ? 0.0602 0.0815 0.0878 0.0047  0.0024  0.0083  128  PRO A CG  
1641 C  CD  . PRO A 128 ? 0.0618 0.0826 0.0683 0.0111  -0.0008 0.0079  128  PRO A CD  
1648 N  N   . ILE A 129 ? 0.0701 0.0806 0.0741 0.0154  0.0019  0.0031  129  ILE A N   
1649 C  CA  . ILE A 129 ? 0.0769 0.0750 0.0830 0.0192  0.0070  0.0021  129  ILE A CA  
1650 C  C   . ILE A 129 ? 0.0749 0.0930 0.0785 0.0186  0.0087  -0.0001 129  ILE A C   
1651 O  O   . ILE A 129 ? 0.0709 0.1059 0.1138 0.0291  0.0037  -0.0024 129  ILE A O   
1652 C  CB  . ILE A 129 ? 0.0828 0.0768 0.0809 0.0253  0.0034  0.0006  129  ILE A CB  
1653 C  CG1 . ILE A 129 ? 0.0846 0.0819 0.0904 0.0175  0.0061  -0.0122 129  ILE A CG1 
1654 C  CG2 . ILE A 129 ? 0.0799 0.1101 0.0947 0.0131  0.0253  -0.0137 129  ILE A CG2 
1655 C  CD1 . ILE A 129 ? 0.0840 0.0859 0.0983 0.0068  0.0021  -0.0072 129  ILE A CD1 
1664 N  N   . GLY A 130 ? 0.0677 0.0926 0.1063 0.0095  0.0022  -0.0001 130  GLY A N   
1665 C  CA  . GLY A 130 ? 0.0734 0.0992 0.1304 0.0082  -0.0051 0.0016  130  GLY A CA  
1666 C  C   . GLY A 130 ? 0.0705 0.1045 0.1252 0.0146  -0.0105 -0.0071 130  GLY A C   
1667 O  O   . GLY A 130 ? 0.0719 0.1427 0.1568 0.0062  -0.0293 -0.0026 130  GLY A O   
1670 N  N   . THR A 131 ? 0.0721 0.1025 0.1139 0.0176  -0.0225 -0.0065 131  THR A N   
1671 C  CA  . THR A 131 ? 0.0873 0.1159 0.1097 0.0271  -0.0229 -0.0143 131  THR A CA  
1672 C  C   . THR A 131 ? 0.0964 0.1200 0.0873 0.0299  -0.0181 -0.0104 131  THR A C   
1673 O  O   . THR A 131 ? 0.1013 0.1343 0.1253 0.0221  -0.0359 0.0027  131  THR A O   
1674 C  CB  . THR A 131 ? 0.1036 0.1512 0.0961 0.0461  -0.0227 -0.0069 131  THR A CB  
1675 O  OG1 . THR A 131 ? 0.1335 0.1588 0.1068 0.0672  -0.0359 -0.0365 131  THR A OG1 
1676 C  CG2 . THR A 131 ? 0.1302 0.2030 0.0858 0.0499  -0.0201 -0.0082 131  THR A CG2 
1681 N  N   . LEU A 132 ? 0.0706 0.1112 0.1075 0.0201  -0.0189 -0.0053 132  LEU A N   
1682 C  CA  . LEU A 132 ? 0.0876 0.1060 0.1079 0.0213  -0.0084 0.0054  132  LEU A CA  
1683 C  C   . LEU A 132 ? 0.0823 0.1378 0.1092 0.0286  -0.0175 -0.0026 132  LEU A C   
1684 O  O   . LEU A 132 ? 0.0965 0.1328 0.1606 0.0368  -0.0188 0.0158  132  LEU A O   
1685 C  CB  . LEU A 132 ? 0.0971 0.1084 0.1141 0.0304  -0.0216 -0.0001 132  LEU A CB  
1686 C  CG  . LEU A 132 ? 0.0967 0.1081 0.1180 0.0153  -0.0106 0.0189  132  LEU A CG  
1687 C  CD1 . LEU A 132 ? 0.1208 0.1474 0.1496 -0.0089 -0.0327 0.0239  132  LEU A CD1 
1688 C  CD2 . LEU A 132 ? 0.1379 0.1432 0.1364 0.0296  -0.0111 0.0444  132  LEU A CD2 
1694 N  N   . ILE A 133 ? 0.0814 0.1222 0.1300 0.0237  -0.0009 -0.0007 133  ILE A N   
1695 C  CA  . ILE A 133 ? 0.0799 0.1657 0.1559 0.0293  0.0025  0.0049  133  ILE A CA  
1696 C  C   . ILE A 133 ? 0.0781 0.1403 0.2045 0.0153  -0.0167 0.0068  133  ILE A C   
1697 O  O   . ILE A 133 ? 0.0870 0.1901 0.2383 0.0324  -0.0253 0.0324  133  ILE A O   
1698 C  CB  . ILE A 133 ? 0.0848 0.1277 0.1876 0.0207  0.0181  0.0165  133  ILE A CB  
1699 C  CG1 . ILE A 133 ? 0.1008 0.1359 0.1589 0.0480  0.0245  0.0043  133  ILE A CG1 
1700 C  CG2 . ILE A 133 ? 0.0808 0.1649 0.2612 0.0213  0.0371  0.0219  133  ILE A CG2 
1701 C  CD1 . ILE A 133 ? 0.1063 0.1660 0.1852 0.0301  0.0391  0.0422  133  ILE A CD1 
1703 N  N   . HIS A 134 ? 0.0792 0.1504 0.1908 0.0026  -0.0284 0.0015  134  HIS A N   
1704 C  CA  . HIS A 134 ? 0.1237 0.1851 0.1893 0.0127  -0.0408 -0.0111 134  HIS A CA  
1705 C  C   . HIS A 134 ? 0.1471 0.1741 0.2572 0.0008  -0.1150 0.0221  134  HIS A C   
1706 O  O   . HIS A 134 ? 0.1402 0.2369 0.2791 0.0063  -0.1168 -0.0139 134  HIS A O   
1707 C  CB  . HIS A 134 ? 0.1600 0.1476 0.2879 0.0211  -0.1082 -0.0247 134  HIS A CB  
1708 C  CG  . HIS A 134 ? 0.2519 0.1965 0.3800 0.0366  -0.1634 -0.0907 134  HIS A CG  
1709 N  ND1 . HIS A 134 ? 0.3663 0.2858 0.3618 0.0782  -0.1785 -0.1502 134  HIS A ND1 
1710 C  CD2 . HIS A 134 ? 0.3379 0.3149 0.4899 -0.0753 -0.2628 -0.0526 134  HIS A CD2 
1711 C  CE1 . HIS A 134 ? 0.4817 0.3543 0.4757 0.0513  -0.2602 -0.1945 134  HIS A CE1 
1712 N  NE2 . HIS A 134 ? 0.4903 0.3205 0.5682 -0.0432 -0.2869 -0.1672 134  HIS A NE2 
1713 N  N   . ARG A 135 ? 0.1172 0.1908 0.1489 0.0283  -0.0524 -0.0060 135  ARG A N   
1714 C  CA  . ARG A 135 ? 0.1606 0.2137 0.1771 0.0421  -0.0716 0.0192  135  ARG A CA  
1715 C  C   . ARG A 135 ? 0.1677 0.2208 0.2202 0.0542  -0.1015 0.0187  135  ARG A C   
1716 O  O   . ARG A 135 ? 0.2031 0.2164 0.2653 0.0385  -0.1216 0.0455  135  ARG A O   
1717 C  CB  . ARG A 135 ? 0.1945 0.1745 0.1513 0.0275  -0.0368 0.0177  135  ARG A CB  
1718 C  CG  . ARG A 135 ? 0.1897 0.1914 0.1552 0.0397  -0.0435 0.0145  135  ARG A CG  
1719 C  CD  . ARG A 135 ? 0.1776 0.3014 0.1609 0.0307  -0.0655 0.0172  135  ARG A CD  
1720 N  NE  . ARG A 135 ? 0.1382 0.2707 0.2345 0.0042  -0.0505 0.0306  135  ARG A NE  
1721 C  CZ  . ARG A 135 ? 0.1226 0.2802 0.2469 0.0360  -0.0065 0.0878  135  ARG A CZ  
1722 N  NH1 . ARG A 135 ? 0.1891 0.3211 0.2221 0.1006  -0.0023 0.0692  135  ARG A NH1 
1723 N  NH2 . ARG A 135 ? 0.1725 0.3587 0.4055 0.1094  0.0800  0.2010  135  ARG A NH2 
1726 N  N   . GLY A 136 ? 0.1330 0.1673 0.2531 0.0366  -0.0634 0.0037  136  GLY A N   
1727 C  CA  . GLY A 136 ? 0.1289 0.1807 0.3391 0.0471  -0.1018 -0.0256 136  GLY A CA  
1728 C  C   . GLY A 136 ? 0.1447 0.1688 0.3176 0.0531  -0.0987 -0.0170 136  GLY A C   
1729 O  O   . GLY A 136 ? 0.1532 0.1655 0.3608 0.0577  -0.0629 0.0038  136  GLY A O   
1730 N  N   . ALA A 137 ? 0.1355 0.1372 0.2063 0.0402  -0.0456 0.0134  137  ALA A N   
1731 C  CA  . ALA A 137 ? 0.1483 0.1482 0.1978 0.0329  -0.0509 0.0239  137  ALA A CA  
1732 C  C   . ALA A 137 ? 0.1416 0.1428 0.2057 0.0647  -0.0278 0.0016  137  ALA A C   
1733 O  O   . ALA A 137 ? 0.1486 0.1394 0.2513 0.0436  -0.0183 0.0001  137  ALA A O   
1734 C  CB  . ALA A 137 ? 0.1519 0.1867 0.1615 0.0262  -0.0376 0.0142  137  ALA A CB  
1737 N  N   . ILE A 138 ? 0.1858 0.1352 0.1844 0.0579  -0.0072 -0.0036 138  ILE A N   
1738 C  CA  . ILE A 138 ? 0.1896 0.1523 0.2006 0.0677  0.0357  -0.0073 138  ILE A CA  
1739 C  C   . ILE A 138 ? 0.1908 0.1602 0.2293 0.0726  0.0279  -0.0046 138  ILE A C   
1740 O  O   . ILE A 138 ? 0.1443 0.2008 0.2465 0.0541  0.0001  -0.0385 138  ILE A O   
1741 C  CB  . ILE A 138 ? 0.1881 0.0997 0.1499 0.0206  0.0211  -0.0080 138  ILE A CB  
1742 C  CG1 . ILE A 138 ? 0.1947 0.0887 0.1829 -0.0078 0.0012  -0.0023 138  ILE A CG1 
1743 C  CG2 . ILE A 138 ? 0.3055 0.1530 0.1509 0.0163  0.0568  -0.0280 138  ILE A CG2 
1744 C  CD1 . ILE A 138 ? 0.1927 0.1275 0.1618 -0.0259 -0.0132 0.0066  138  ILE A CD1 
1748 N  N   . GLU A 139 ? 0.2268 0.1988 0.3837 0.0578  0.1112  -0.0636 139  GLU A N   
1749 C  CA  . GLU A 139 ? 0.1955 0.2686 0.3588 0.1101  0.0386  -0.0002 139  GLU A CA  
1750 C  C   . GLU A 139 ? 0.1320 0.2494 0.3512 0.0366  0.0121  -0.0104 139  GLU A C   
1751 O  O   . GLU A 139 ? 0.3479 0.2407 0.4154 0.0957  -0.1269 -0.0201 139  GLU A O   
1752 C  CB  A GLU A 139 ? 0.2879 0.2994 0.5795 0.1585  -0.0132 0.0458  139  GLU A CB  
1753 C  CB  B GLU A 139 ? 0.3008 0.3039 0.5563 0.1690  -0.0225 0.0412  139  GLU A CB  
1754 C  CG  A GLU A 139 ? 0.3643 0.2277 0.6321 0.1893  0.0594  0.0638  139  GLU A CG  
1755 C  CG  B GLU A 139 ? 0.4023 0.3111 0.6968 0.1650  0.0269  0.0902  139  GLU A CG  
1756 C  CD  A GLU A 139 ? 0.4963 0.2589 0.7332 0.2494  0.0742  0.0722  139  GLU A CD  
1757 C  CD  B GLU A 139 ? 0.3672 0.3675 0.7378 0.0876  -0.0292 0.1049  139  GLU A CD  
1758 O  OE1 A GLU A 139 ? 0.6792 0.2589 1.0275 0.3356  0.2954  0.0581  139  GLU A OE1 
1759 O  OE1 B GLU A 139 ? 0.2407 0.5892 0.7410 0.0342  0.0465  -0.1095 139  GLU A OE1 
1760 O  OE2 A GLU A 139 ? 0.6780 0.1791 0.6989 0.2426  0.1315  0.0142  139  GLU A OE2 
1761 O  OE2 B GLU A 139 ? 0.4430 0.2178 0.7708 0.1292  -0.0057 -0.2085 139  GLU A OE2 
1762 N  N   . TRP A 140 ? 0.1536 0.2637 0.3310 0.0489  0.0863  -0.0450 140  TRP A N   
1763 C  CA  . TRP A 140 ? 0.1288 0.2204 0.3305 0.0108  0.0478  -0.0575 140  TRP A CA  
1764 C  C   . TRP A 140 ? 0.1432 0.2183 0.3375 0.0060  0.0421  -0.0969 140  TRP A C   
1765 O  O   . TRP A 140 ? 0.1836 0.3047 0.4163 0.0188  0.0025  -0.1864 140  TRP A O   
1766 C  CB  . TRP A 140 ? 0.1347 0.2932 0.3025 0.0106  0.0272  -0.0750 140  TRP A CB  
1767 C  CG  . TRP A 140 ? 0.1395 0.2163 0.2920 0.0016  0.0089  -0.1174 140  TRP A CG  
1768 C  CD1 . TRP A 140 ? 0.1772 0.2208 0.2972 -0.0577 0.0398  -0.1129 140  TRP A CD1 
1769 C  CD2 . TRP A 140 ? 0.1103 0.2287 0.3071 0.0200  0.0046  -0.1077 140  TRP A CD2 
1770 N  NE1 . TRP A 140 ? 0.1153 0.2336 0.2979 -0.0301 0.0341  -0.1093 140  TRP A NE1 
1771 C  CE2 . TRP A 140 ? 0.0863 0.2291 0.3040 0.0049  0.0319  -0.1000 140  TRP A CE2 
1772 C  CE3 . TRP A 140 ? 0.1269 0.1858 0.2623 0.0045  0.0107  -0.0512 140  TRP A CE3 
1773 C  CZ2 . TRP A 140 ? 0.1221 0.2480 0.3605 0.0264  -0.0532 -0.0656 140  TRP A CZ2 
1774 C  CZ3 . TRP A 140 ? 0.1864 0.2215 0.3044 0.0407  -0.0224 -0.0058 140  TRP A CZ3 
1775 C  CH2 . TRP A 140 ? 0.1654 0.2226 0.2960 0.0350  -0.0461 -0.0212 140  TRP A CH2 
1778 N  N   . GLU A 141 ? 0.1139 0.2217 0.3436 0.0049  0.0204  -0.0750 141  GLU A N   
1779 C  CA  A GLU A 141 ? 0.1128 0.2126 0.2970 0.0100  -0.0239 -0.0601 141  GLU A CA  
1780 C  CA  B GLU A 141 ? 0.1260 0.2347 0.2680 -0.0045 -0.0180 -0.0593 141  GLU A CA  
1781 C  C   . GLU A 141 ? 0.0966 0.2934 0.3861 -0.0016 -0.0240 0.0262  141  GLU A C   
1782 O  O   . GLU A 141 ? 0.1665 0.3965 0.5452 -0.0872 -0.1328 0.1504  141  GLU A O   
1783 C  CB  A GLU A 141 ? 0.1207 0.2170 0.3144 0.0022  0.0269  -0.0104 141  GLU A CB  
1784 C  CB  B GLU A 141 ? 0.1206 0.2224 0.3259 -0.0150 -0.0187 -0.0214 141  GLU A CB  
1785 C  CG  A GLU A 141 ? 0.1190 0.2552 0.2904 0.0382  -0.0161 -0.0432 141  GLU A CG  
1786 C  CG  B GLU A 141 ? 0.1321 0.2850 0.3790 0.0276  0.0103  -0.0712 141  GLU A CG  
1787 C  CD  A GLU A 141 ? 0.1200 0.3070 0.3451 0.0497  -0.0386 -0.0555 141  GLU A CD  
1788 C  CD  B GLU A 141 ? 0.2490 0.3173 0.3455 0.1078  -0.0228 -0.0237 141  GLU A CD  
1789 O  OE1 A GLU A 141 ? 0.1160 0.3024 0.3693 0.0189  -0.0286 -0.1063 141  GLU A OE1 
1790 O  OE1 B GLU A 141 ? 0.1709 0.4300 0.3345 0.0108  -0.0850 -0.0672 141  GLU A OE1 
1791 O  OE2 A GLU A 141 ? 0.1702 0.3413 0.4494 0.0891  -0.0426 0.0083  141  GLU A OE2 
1792 O  OE2 B GLU A 141 ? 0.0894 0.1198 0.3269 0.0247  -0.0585 0.0063  141  GLU A OE2 
1793 N  N   . GLY A 142 ? 0.1417 0.2129 0.3276 -0.0075 -0.0521 -0.0443 142  GLY A N   
1794 C  CA  . GLY A 142 ? 0.1492 0.2180 0.3357 0.0044  -0.0493 -0.0411 142  GLY A CA  
1795 C  C   . GLY A 142 ? 0.1742 0.2257 0.3231 0.0646  -0.0206 -0.0380 142  GLY A C   
1796 O  O   . GLY A 142 ? 0.1387 0.2234 0.3337 0.0102  -0.0472 -0.0421 142  GLY A O   
1797 N  N   . ILE A 143 ? 0.1462 0.2281 0.3418 -0.0020 -0.0368 -0.0033 143  ILE A N   
1798 C  CA  . ILE A 143 ? 0.1178 0.1945 0.3560 -0.0223 -0.0366 -0.0020 143  ILE A CA  
1799 C  C   . ILE A 143 ? 0.1155 0.2197 0.3596 -0.0494 -0.0064 -0.0115 143  ILE A C   
1800 O  O   . ILE A 143 ? 0.1304 0.2371 0.3245 -0.0236 -0.0273 0.0026  143  ILE A O   
1801 C  CB  . ILE A 143 ? 0.1875 0.2281 0.3945 -0.0094 -0.0557 0.0361  143  ILE A CB  
1802 C  CG1 . ILE A 143 ? 0.1957 0.3444 0.4155 -0.0251 -0.0732 0.0915  143  ILE A CG1 
1803 C  CG2 . ILE A 143 ? 0.2273 0.2242 0.5585 -0.0467 -0.0592 0.0737  143  ILE A CG2 
1804 C  CD1 . ILE A 143 ? 0.1378 0.2898 0.5805 0.0080  -0.0648 0.0549  143  ILE A CD1 
1805 N  N   . GLU A 144 ? 0.1185 0.2388 0.3318 -0.0005 -0.0477 0.0120  144  GLU A N   
1806 C  CA  . GLU A 144 ? 0.1268 0.2662 0.3890 -0.0652 0.0363  0.0189  144  GLU A CA  
1807 C  C   . GLU A 144 ? 0.1156 0.2477 0.3880 -0.0155 0.0332  0.0076  144  GLU A C   
1808 O  O   . GLU A 144 ? 0.1468 0.3188 0.3879 -0.0151 0.0249  -0.0280 144  GLU A O   
1809 C  CB  . GLU A 144 ? 0.1158 0.2711 0.4672 -0.0460 -0.0138 0.0355  144  GLU A CB  
1810 C  CG  . GLU A 144 ? 0.1351 0.2739 0.4727 -0.0590 -0.0646 0.0396  144  GLU A CG  
1811 C  CD  . GLU A 144 ? 0.1223 0.2256 0.4549 -0.0188 -0.0374 0.0871  144  GLU A CD  
1812 O  OE1 . GLU A 144 ? 0.2170 0.3208 0.4638 -0.1227 -0.0368 0.0924  144  GLU A OE1 
1813 O  OE2 . GLU A 144 ? 0.2082 0.2227 0.5028 -0.0172 0.0293  0.0752  144  GLU A OE2 
1814 N  N   . SER A 145 ? 0.1072 0.2198 0.3618 -0.0085 -0.0240 -0.0096 145  SER A N   
1815 C  CA  . SER A 145 ? 0.1312 0.2354 0.3693 -0.0351 0.0068  0.0036  145  SER A CA  
1816 C  C   . SER A 145 ? 0.1313 0.1984 0.3964 0.0214  -0.0090 -0.0675 145  SER A C   
1817 O  O   . SER A 145 ? 0.1857 0.1941 0.5036 0.0359  0.0107  -0.0859 145  SER A O   
1818 C  CB  . SER A 145 ? 0.1284 0.3003 0.3621 -0.0430 -0.0061 0.0208  145  SER A CB  
1819 O  OG  . SER A 145 ? 0.1497 0.2878 0.3322 0.0060  -0.0194 -0.0110 145  SER A OG  
1821 N  N   . GLY A 146 ? 0.1119 0.1992 0.3423 0.0063  0.0175  -0.0537 146  GLY A N   
1822 C  CA  . GLY A 146 ? 0.1133 0.1747 0.2932 -0.0028 0.0258  -0.0379 146  GLY A CA  
1823 C  C   . GLY A 146 ? 0.1104 0.1635 0.1893 -0.0144 0.0200  -0.0432 146  GLY A C   
1824 O  O   . GLY A 146 ? 0.1081 0.2046 0.2219 -0.0042 -0.0200 -0.0674 146  GLY A O   
1825 N  N   . SER A 147 ? 0.1185 0.1641 0.1637 -0.0084 0.0165  -0.0569 147  SER A N   
1826 C  CA  . SER A 147 ? 0.1120 0.1603 0.1325 -0.0100 0.0200  -0.0146 147  SER A CA  
1827 C  C   . SER A 147 ? 0.0734 0.1361 0.1361 0.0032  0.0071  -0.0030 147  SER A C   
1828 O  O   . SER A 147 ? 0.0939 0.1396 0.1515 0.0164  0.0046  -0.0063 147  SER A O   
1829 C  CB  . SER A 147 ? 0.1329 0.1540 0.1289 -0.0223 0.0158  0.0070  147  SER A CB  
1830 O  OG  . SER A 147 ? 0.1898 0.1228 0.1409 -0.0079 -0.0379 -0.0098 147  SER A OG  
1833 N  N   . VAL A 148 ? 0.1148 0.1273 0.1075 -0.0024 0.0046  -0.0120 148  VAL A N   
1834 C  CA  . VAL A 148 ? 0.0991 0.1129 0.1000 0.0002  -0.0076 0.0019  148  VAL A CA  
1835 C  C   . VAL A 148 ? 0.1036 0.0987 0.0967 0.0071  0.0071  -0.0116 148  VAL A C   
1836 O  O   . VAL A 148 ? 0.1139 0.0974 0.1095 0.0010  -0.0086 0.0034  148  VAL A O   
1837 C  CB  . VAL A 148 ? 0.1280 0.1032 0.1219 -0.0184 0.0107  -0.0096 148  VAL A CB  
1838 C  CG1 . VAL A 148 ? 0.1366 0.1249 0.1287 0.0385  0.0115  -0.0007 148  VAL A CG1 
1839 C  CG2 . VAL A 148 ? 0.1357 0.1118 0.1668 -0.0057 -0.0194 -0.0157 148  VAL A CG2 
1844 N  N   A GLU A 149 ? 0.0940 0.1189 0.1154 -0.0099 -0.0165 0.0165  149  GLU A N   
1845 N  N   B GLU A 149 ? 0.1042 0.0797 0.0820 0.0032  0.0172  -0.0168 149  GLU A N   
1846 C  CA  . GLU A 149 ? 0.0903 0.0859 0.0943 0.0032  0.0081  -0.0049 149  GLU A CA  
1847 C  C   A GLU A 149 ? 0.0910 0.1064 0.0746 0.0163  -0.0093 -0.0113 149  GLU A C   
1848 C  C   B GLU A 149 ? 0.1236 0.0784 0.1228 0.0002  0.0138  -0.0088 149  GLU A C   
1849 O  O   A GLU A 149 ? 0.1094 0.1120 0.1120 0.0326  0.0186  0.0139  149  GLU A O   
1850 O  O   B GLU A 149 ? 0.1538 0.0837 0.0913 -0.0400 -0.0323 -0.0089 149  GLU A O   
1851 C  CB  A GLU A 149 ? 0.0997 0.0917 0.1131 0.0223  -0.0170 -0.0033 149  GLU A CB  
1852 C  CB  B GLU A 149 ? 0.0650 0.1300 0.0775 -0.0018 0.0355  -0.0146 149  GLU A CB  
1853 C  CG  A GLU A 149 ? 0.0758 0.0975 0.0972 0.0102  0.0206  -0.0041 149  GLU A CG  
1854 C  CG  B GLU A 149 ? 0.0954 0.2461 0.1548 0.0890  0.0050  -0.0130 149  GLU A CG  
1855 C  CD  A GLU A 149 ? 0.0791 0.1649 0.0812 0.0248  0.0120  0.0147  149  GLU A CD  
1856 C  CD  B GLU A 149 ? 0.1115 0.1837 0.1844 0.0064  -0.0737 -0.0193 149  GLU A CD  
1857 O  OE1 A GLU A 149 ? 0.1787 0.2826 0.1648 0.0616  0.0116  0.1054  149  GLU A OE1 
1858 O  OE1 B GLU A 149 ? 0.2919 0.1420 0.2574 0.0934  0.0797  -0.0177 149  GLU A OE1 
1859 O  OE2 A GLU A 149 ? 0.0972 0.2086 0.1047 0.0062  0.0141  -0.0588 149  GLU A OE2 
1860 O  OE2 B GLU A 149 ? 0.0715 0.4447 0.2140 -0.0581 0.0148  -0.1685 149  GLU A OE2 
1861 N  N   A GLN A 150 ? 0.0970 0.0954 0.1197 0.0060  0.0130  -0.0313 150  GLN A N   
1862 N  N   B GLN A 150 ? 0.1194 0.1249 0.0953 0.0388  -0.0102 0.0034  150  GLN A N   
1863 C  CA  A GLN A 150 ? 0.1189 0.1305 0.1300 0.0353  0.0121  -0.0106 150  GLN A CA  
1864 C  CA  B GLN A 150 ? 0.1410 0.1381 0.1289 0.0493  -0.0246 0.0171  150  GLN A CA  
1865 C  C   A GLN A 150 ? 0.1171 0.1119 0.1340 0.0440  0.0118  -0.0265 150  GLN A C   
1866 C  C   B GLN A 150 ? 0.1408 0.1026 0.1421 0.0142  -0.0454 0.0216  150  GLN A C   
1867 O  O   A GLN A 150 ? 0.1396 0.1097 0.1409 0.0556  -0.0330 -0.0177 150  GLN A O   
1868 O  O   B GLN A 150 ? 0.2124 0.1744 0.1309 -0.0707 0.0602  0.0311  150  GLN A O   
1869 C  CB  A GLN A 150 ? 0.1059 0.1430 0.1415 0.0416  0.0136  -0.0167 150  GLN A CB  
1870 C  CB  B GLN A 150 ? 0.1587 0.1712 0.1746 0.0816  -0.0023 -0.0063 150  GLN A CB  
1871 C  CG  A GLN A 150 ? 0.0918 0.1339 0.2321 0.0325  -0.0291 -0.0321 150  GLN A CG  
1872 C  CG  B GLN A 150 ? 0.2317 0.2697 0.2100 -0.0167 0.0519  -0.0758 150  GLN A CG  
1873 C  CD  A GLN A 150 ? 0.1041 0.1787 0.3067 0.0453  0.0113  -0.1007 150  GLN A CD  
1874 C  CD  B GLN A 150 ? 0.1195 0.2202 0.2139 0.0004  0.0422  -0.0992 150  GLN A CD  
1875 O  OE1 A GLN A 150 ? 0.1038 0.2509 0.2493 0.0072  0.0155  -0.0910 150  GLN A OE1 
1876 O  OE1 B GLN A 150 ? 0.1391 0.1555 0.1982 0.0095  0.0119  -0.0525 150  GLN A OE1 
1877 N  NE2 A GLN A 150 ? 0.1746 0.3734 0.4628 0.0236  0.0602  -0.2794 150  GLN A NE2 
1878 N  NE2 B GLN A 150 ? 0.1728 0.2629 0.2779 -0.0635 0.1313  -0.1781 150  GLN A NE2 
1879 N  N   . ALA A 151 ? 0.1043 0.1174 0.1328 0.0237  -0.0023 0.0043  151  ALA A N   
1880 C  CA  . ALA A 151 ? 0.0996 0.1478 0.1335 0.0191  -0.0195 -0.0070 151  ALA A CA  
1881 C  C   . ALA A 151 ? 0.1286 0.1071 0.1144 0.0369  -0.0030 0.0026  151  ALA A C   
1882 O  O   . ALA A 151 ? 0.1447 0.1057 0.1510 0.0369  -0.0086 0.0219  151  ALA A O   
1883 C  CB  . ALA A 151 ? 0.1458 0.1439 0.1755 0.0094  -0.0321 -0.0076 151  ALA A CB  
1886 N  N   . VAL A 152 ? 0.1179 0.0876 0.0970 0.0233  -0.0019 -0.0041 152  VAL A N   
1887 C  CA  . VAL A 152 ? 0.1160 0.0852 0.0999 0.0246  0.0044  -0.0019 152  VAL A CA  
1888 C  C   . VAL A 152 ? 0.1129 0.0777 0.1128 0.0342  0.0074  0.0084  152  VAL A C   
1889 O  O   . VAL A 152 ? 0.1395 0.0919 0.1332 0.0410  0.0346  0.0184  152  VAL A O   
1890 C  CB  . VAL A 152 ? 0.1212 0.0702 0.0913 0.0206  0.0033  0.0058  152  VAL A CB  
1891 C  CG1 . VAL A 152 ? 0.1155 0.0918 0.0991 0.0291  0.0135  -0.0009 152  VAL A CG1 
1892 C  CG2 . VAL A 152 ? 0.1191 0.0849 0.1075 0.0250  -0.0121 0.0029  152  VAL A CG2 
1899 N  N   . ALA A 153 ? 0.1162 0.0878 0.1162 0.0187  0.0086  -0.0073 153  ALA A N   
1900 C  CA  . ALA A 153 ? 0.1285 0.0882 0.1569 0.0204  0.0155  -0.0141 153  ALA A CA  
1901 C  C   . ALA A 153 ? 0.1431 0.0856 0.1520 0.0233  0.0240  -0.0078 153  ALA A C   
1902 O  O   . ALA A 153 ? 0.2071 0.0793 0.1744 0.0072  0.0327  -0.0131 153  ALA A O   
1903 C  CB  . ALA A 153 ? 0.1698 0.1122 0.1462 0.0097  -0.0244 -0.0356 153  ALA A CB  
1907 N  N   . LYS A 154 ? 0.1490 0.0945 0.1298 0.0345  0.0202  0.0043  154  LYS A N   
1908 C  CA  . LYS A 154 ? 0.1750 0.1039 0.1479 0.0747  0.0308  0.0080  154  LYS A CA  
1909 C  C   . LYS A 154 ? 0.1814 0.0917 0.1383 0.0532  0.0070  0.0056  154  LYS A C   
1910 O  O   . LYS A 154 ? 0.2344 0.0994 0.1576 0.0663  0.0070  0.0160  154  LYS A O   
1911 C  CB  . LYS A 154 ? 0.1656 0.1457 0.1639 0.0789  0.0066  0.0134  154  LYS A CB  
1912 C  CG  . LYS A 154 ? 0.2055 0.2163 0.2198 0.0480  0.0575  -0.0128 154  LYS A CG  
1913 C  CD  . LYS A 154 ? 0.2001 0.2700 0.3211 0.0330  0.0718  -0.0158 154  LYS A CD  
1914 C  CE  . LYS A 154 ? 0.2260 0.2503 0.3166 0.0448  0.0836  0.0104  154  LYS A CE  
1915 N  NZ  . LYS A 154 ? 0.2120 0.3416 0.3729 0.0370  0.0965  0.0376  154  LYS A NZ  
1919 N  N   . PHE A 155 ? 0.1325 0.0820 0.1198 0.0343  0.0011  -0.0036 155  PHE A N   
1920 C  CA  . PHE A 155 ? 0.1270 0.0781 0.1292 0.0273  -0.0063 0.0064  155  PHE A CA  
1921 C  C   . PHE A 155 ? 0.1229 0.0736 0.1212 0.0280  -0.0050 0.0052  155  PHE A C   
1922 O  O   . PHE A 155 ? 0.1441 0.0904 0.1215 0.0178  -0.0198 0.0167  155  PHE A O   
1923 C  CB  . PHE A 155 ? 0.1343 0.0892 0.1255 0.0144  0.0081  -0.0104 155  PHE A CB  
1924 C  CG  . PHE A 155 ? 0.1111 0.0919 0.1240 0.0071  0.0021  0.0018  155  PHE A CG  
1925 C  CD1 . PHE A 155 ? 0.1257 0.0964 0.1307 0.0213  -0.0151 -0.0133 155  PHE A CD1 
1926 C  CD2 . PHE A 155 ? 0.1245 0.0956 0.1151 0.0231  0.0071  0.0156  155  PHE A CD2 
1927 C  CE1 . PHE A 155 ? 0.1467 0.0926 0.1299 0.0255  -0.0098 -0.0005 155  PHE A CE1 
1928 C  CE2 . PHE A 155 ? 0.1289 0.1095 0.1234 0.0182  0.0119  0.0181  155  PHE A CE2 
1929 C  CZ  . PHE A 155 ? 0.1509 0.0999 0.1088 0.0071  0.0051  0.0017  155  PHE A CZ  
1933 N  N   . PHE A 156 ? 0.1231 0.0796 0.1312 0.0223  -0.0027 0.0167  156  PHE A N   
1934 C  CA  . PHE A 156 ? 0.1269 0.0892 0.0919 0.0023  -0.0062 0.0145  156  PHE A CA  
1935 C  C   . PHE A 156 ? 0.1411 0.0942 0.0915 0.0147  0.0030  0.0159  156  PHE A C   
1936 O  O   . PHE A 156 ? 0.1629 0.1302 0.1050 0.0187  0.0108  0.0076  156  PHE A O   
1937 C  CB  . PHE A 156 ? 0.1336 0.0936 0.0964 0.0063  -0.0117 0.0160  156  PHE A CB  
1938 C  CG  . PHE A 156 ? 0.1033 0.0964 0.1078 0.0258  -0.0012 0.0177  156  PHE A CG  
1939 C  CD1 . PHE A 156 ? 0.0963 0.1094 0.1096 0.0174  0.0033  0.0095  156  PHE A CD1 
1940 C  CD2 . PHE A 156 ? 0.1183 0.0897 0.1359 0.0248  0.0092  0.0213  156  PHE A CD2 
1941 C  CE1 . PHE A 156 ? 0.1028 0.1362 0.1198 0.0277  -0.0092 -0.0032 156  PHE A CE1 
1942 C  CE2 . PHE A 156 ? 0.1327 0.0972 0.1514 0.0223  -0.0271 0.0072  156  PHE A CE2 
1943 C  CZ  . PHE A 156 ? 0.1128 0.1152 0.1458 0.0418  -0.0269 -0.0199 156  PHE A CZ  
1949 N  N   . SER A 157 ? 0.1314 0.0865 0.0977 0.0192  0.0020  0.0086  157  SER A N   
1950 C  CA  . SER A 157 ? 0.1382 0.0931 0.1035 0.0286  -0.0039 -0.0005 157  SER A CA  
1951 C  C   . SER A 157 ? 0.1156 0.0905 0.1040 0.0306  0.0073  0.0034  157  SER A C   
1952 O  O   . SER A 157 ? 0.1457 0.1013 0.1131 0.0325  -0.0135 -0.0171 157  SER A O   
1953 C  CB  . SER A 157 ? 0.1652 0.0783 0.1298 0.0311  -0.0038 0.0098  157  SER A CB  
1954 O  OG  . SER A 157 ? 0.1758 0.0836 0.1539 0.0104  0.0118  0.0196  157  SER A OG  
1958 N  N   . ALA A 158 ? 0.1284 0.0740 0.0948 0.0227  0.0040  0.0117  158  ALA A N   
1959 C  CA  . ALA A 158 ? 0.1341 0.0733 0.1047 0.0288  -0.0103 -0.0014 158  ALA A CA  
1960 C  C   . ALA A 158 ? 0.1120 0.0810 0.0721 0.0238  0.0102  -0.0002 158  ALA A C   
1961 O  O   . ALA A 158 ? 0.1469 0.0867 0.0676 0.0286  0.0102  0.0073  158  ALA A O   
1962 C  CB  . ALA A 158 ? 0.1527 0.0852 0.1634 0.0264  -0.0233 -0.0293 158  ALA A CB  
1963 N  N   . SER A 159 ? 0.1062 0.0717 0.0706 0.0206  0.0146  0.0055  159  SER A N   
1964 C  CA  . SER A 159 ? 0.1012 0.0663 0.0630 0.0141  0.0064  -0.0039 159  SER A CA  
1965 C  C   . SER A 159 ? 0.0967 0.0670 0.0643 0.0061  0.0055  0.0033  159  SER A C   
1966 O  O   . SER A 159 ? 0.0998 0.0686 0.0743 0.0081  0.0076  -0.0064 159  SER A O   
1967 C  CB  . SER A 159 ? 0.0877 0.0789 0.0696 0.0156  0.0059  0.0052  159  SER A CB  
1968 O  OG  . SER A 159 ? 0.0985 0.0874 0.0875 0.0115  0.0036  0.0011  159  SER A OG  
1972 N  N   . CYS A 160 ? 0.0888 0.0719 0.0578 0.0087  0.0080  -0.0019 160  CYS A N   
1973 C  CA  . CYS A 160 ? 0.0871 0.0666 0.0595 0.0074  0.0079  -0.0024 160  CYS A CA  
1974 C  C   . CYS A 160 ? 0.0767 0.0672 0.0615 0.0122  -0.0015 -0.0011 160  CYS A C   
1975 O  O   . CYS A 160 ? 0.0904 0.0756 0.0571 0.0100  0.0083  -0.0035 160  CYS A O   
1976 C  CB  . CYS A 160 ? 0.0822 0.0724 0.0775 -0.0010 0.0065  -0.0037 160  CYS A CB  
1977 S  SG  . CYS A 160 ? 0.0862 0.0823 0.0889 0.0037  0.0003  0.0013  160  CYS A SG  
1982 N  N   . VAL A 161 ? 0.0825 0.0648 0.0582 0.0096  0.0074  -0.0049 161  VAL A N   
1983 C  CA  . VAL A 161 ? 0.0802 0.0688 0.0696 0.0054  0.0040  0.0036  161  VAL A CA  
1984 C  C   . VAL A 161 ? 0.0793 0.0695 0.0599 0.0093  0.0068  -0.0056 161  VAL A C   
1985 O  O   . VAL A 161 ? 0.0793 0.0885 0.0674 0.0088  0.0083  0.0002  161  VAL A O   
1986 C  CB  . VAL A 161 ? 0.0743 0.0750 0.0688 0.0102  0.0059  0.0082  161  VAL A CB  
1987 C  CG1 . VAL A 161 ? 0.0834 0.0817 0.1022 -0.0021 -0.0053 0.0088  161  VAL A CG1 
1988 C  CG2 . VAL A 161 ? 0.0878 0.0761 0.0702 0.0078  -0.0035 0.0074  161  VAL A CG2 
1995 N  N   . PRO A 162 ? 0.0828 0.0752 0.0549 0.0056  0.0021  0.0004  162  PRO A N   
1996 C  CA  . PRO A 162 ? 0.0875 0.0664 0.0581 0.0047  -0.0015 -0.0012 162  PRO A CA  
1997 C  C   . PRO A 162 ? 0.0770 0.0716 0.0551 0.0037  -0.0031 -0.0016 162  PRO A C   
1998 O  O   . PRO A 162 ? 0.1020 0.0744 0.0662 -0.0013 0.0018  -0.0069 162  PRO A O   
1999 C  CB  . PRO A 162 ? 0.0871 0.0948 0.0681 0.0139  0.0020  0.0099  162  PRO A CB  
2000 C  CG  . PRO A 162 ? 0.0841 0.1054 0.0976 0.0165  0.0103  0.0234  162  PRO A CG  
2001 C  CD  . PRO A 162 ? 0.0912 0.0825 0.0693 0.0175  0.0110  0.0093  162  PRO A CD  
2008 N  N   . GLY A 163 ? 0.0953 0.0710 0.0551 -0.0006 0.0049  -0.0044 163  GLY A N   
2009 C  CA  . GLY A 163 ? 0.0914 0.0793 0.0654 -0.0033 0.0004  0.0057  163  GLY A CA  
2010 C  C   . GLY A 163 ? 0.0986 0.0847 0.0706 0.0013  0.0153  -0.0060 163  GLY A C   
2011 O  O   . GLY A 163 ? 0.0974 0.0979 0.0989 -0.0024 0.0247  0.0029  163  GLY A O   
2015 N  N   . ALA A 164 ? 0.1008 0.1063 0.0628 0.0173  0.0156  0.0059  164  ALA A N   
2016 C  CA  . ALA A 164 ? 0.0912 0.1166 0.0780 0.0088  0.0116  0.0019  164  ALA A CA  
2017 C  C   . ALA A 164 ? 0.1088 0.0924 0.0905 0.0120  0.0186  -0.0034 164  ALA A C   
2018 O  O   . ALA A 164 ? 0.1177 0.1295 0.1424 0.0030  0.0053  -0.0388 164  ALA A O   
2019 C  CB  . ALA A 164 ? 0.1140 0.1749 0.0835 0.0538  0.0230  0.0278  164  ALA A CB  
2025 N  N   . THR A 165 ? 0.1405 0.1150 0.0922 0.0061  0.0444  -0.0154 165  THR A N   
2026 C  CA  . THR A 165 ? 0.1884 0.1323 0.0902 0.0335  0.0468  -0.0047 165  THR A CA  
2027 C  C   . THR A 165 ? 0.1440 0.1052 0.0994 -0.0035 0.0480  -0.0122 165  THR A C   
2028 O  O   . THR A 165 ? 0.1792 0.1899 0.1098 0.0376  0.0316  -0.0418 165  THR A O   
2029 C  CB  . THR A 165 ? 0.2698 0.1782 0.1314 0.0804  0.0969  0.0374  165  THR A CB  
2030 O  OG1 . THR A 165 ? 0.3523 0.1273 0.2073 0.0238  0.1476  0.0238  165  THR A OG1 
2031 C  CG2 . THR A 165 ? 0.3600 0.2800 0.1464 0.1671  0.1018  0.0878  165  THR A CG2 
2032 N  N   . ILE A 166 ? 0.1389 0.1024 0.1142 0.0019  0.0433  -0.0143 166  ILE A N   
2033 C  CA  . ILE A 166 ? 0.1143 0.1418 0.1312 -0.0092 0.0478  -0.0239 166  ILE A CA  
2034 C  C   . ILE A 166 ? 0.1155 0.1483 0.0870 0.0160  0.0241  -0.0257 166  ILE A C   
2035 O  O   . ILE A 166 ? 0.1493 0.1694 0.1109 0.0317  0.0402  -0.0068 166  ILE A O   
2036 C  CB  . ILE A 166 ? 0.1286 0.1957 0.1297 -0.0120 0.0110  -0.0217 166  ILE A CB  
2037 C  CG1 . ILE A 166 ? 0.1628 0.1845 0.1630 -0.0445 0.0244  -0.0415 166  ILE A CG1 
2038 C  CG2 . ILE A 166 ? 0.1435 0.2542 0.1399 0.0240  -0.0015 -0.0659 166  ILE A CG2 
2039 C  CD1 . ILE A 166 ? 0.1534 0.1992 0.2953 -0.0113 -0.0214 -0.0795 166  ILE A CD1 
2042 N  N   . GLU A 167 ? 0.1219 0.1186 0.1193 -0.0005 0.0391  -0.0309 167  GLU A N   
2043 C  CA  A GLU A 167 ? 0.1077 0.1489 0.1012 -0.0003 0.0031  -0.0113 167  GLU A CA  
2044 C  CA  B GLU A 167 ? 0.1149 0.1098 0.0989 0.0145  0.0435  -0.0516 167  GLU A CA  
2045 C  C   . GLU A 167 ? 0.1057 0.1110 0.0742 0.0107  0.0174  -0.0091 167  GLU A C   
2046 O  O   . GLU A 167 ? 0.1218 0.1037 0.1067 0.0181  0.0284  -0.0115 167  GLU A O   
2047 C  CB  A GLU A 167 ? 0.0900 0.1380 0.1022 0.0195  0.0243  -0.0632 167  GLU A CB  
2048 C  CB  B GLU A 167 ? 0.1797 0.2313 0.1214 -0.0296 -0.0298 -0.0312 167  GLU A CB  
2049 C  CG  A GLU A 167 ? 0.0925 0.1558 0.0959 -0.0194 0.0244  -0.0829 167  GLU A CG  
2050 C  CG  B GLU A 167 ? 0.2362 0.2439 0.1763 0.0902  0.0616  0.0510  167  GLU A CG  
2051 C  CD  A GLU A 167 ? 0.0747 0.2492 0.1603 0.0293  -0.0027 -0.1666 167  GLU A CD  
2052 C  CD  B GLU A 167 ? 0.1999 0.2779 0.2061 0.0963  0.0065  0.0112  167  GLU A CD  
2053 O  OE1 A GLU A 167 ? 0.1026 0.1619 0.1509 0.0513  0.0447  -0.0289 167  GLU A OE1 
2054 O  OE1 B GLU A 167 ? 0.2171 0.1973 0.4519 0.0666  0.0527  -0.0318 167  GLU A OE1 
2055 O  OE2 A GLU A 167 ? 0.0898 0.3952 0.4708 0.0285  -0.0355 -0.3774 167  GLU A OE2 
2056 O  OE2 B GLU A 167 ? 0.1195 0.2765 0.1033 0.1153  0.0240  -0.0075 167  GLU A OE2 
2059 N  N   . GLN A 168 ? 0.1185 0.1153 0.0865 0.0058  0.0219  -0.0266 168  GLN A N   
2060 C  CA  A GLN A 168 ? 0.1275 0.1006 0.0701 -0.0008 0.0181  -0.0151 168  GLN A CA  
2061 C  CA  B GLN A 168 ? 0.0991 0.0887 0.0872 0.0200  0.0066  0.0145  168  GLN A CA  
2062 C  C   . GLN A 168 ? 0.1192 0.0867 0.0842 0.0243  0.0174  -0.0104 168  GLN A C   
2063 O  O   . GLN A 168 ? 0.1008 0.0929 0.0988 0.0117  0.0142  -0.0163 168  GLN A O   
2064 C  CB  A GLN A 168 ? 0.1012 0.1065 0.0748 0.0074  0.0218  -0.0147 168  GLN A CB  
2065 C  CB  B GLN A 168 ? 0.1889 0.1430 0.0965 -0.0163 0.0212  -0.0479 168  GLN A CB  
2066 C  CG  A GLN A 168 ? 0.1234 0.1201 0.0609 -0.0243 0.0050  -0.0303 168  GLN A CG  
2067 C  CG  B GLN A 168 ? 0.1661 0.2496 0.1571 0.0185  0.0585  -0.0709 168  GLN A CG  
2068 C  CD  A GLN A 168 ? 0.1110 0.1527 0.0546 -0.0206 0.0084  -0.0084 168  GLN A CD  
2069 C  CD  B GLN A 168 ? 0.1706 0.2333 0.2014 0.0255  0.0351  -0.1027 168  GLN A CD  
2070 O  OE1 A GLN A 168 ? 0.0920 0.1953 0.1297 -0.0242 -0.0153 0.0767  168  GLN A OE1 
2071 O  OE1 B GLN A 168 ? 0.1227 0.3051 0.1105 0.0843  0.0207  -0.1449 168  GLN A OE1 
2072 N  NE2 A GLN A 168 ? 0.1237 0.1149 0.0779 -0.0250 -0.0037 -0.0188 168  GLN A NE2 
2073 N  NE2 B GLN A 168 ? 0.0680 0.0925 0.0506 -0.0441 0.0183  -0.0034 168  GLN A NE2 
2075 N  N   . LYS A 169 ? 0.1111 0.1111 0.0814 0.0373  0.0149  -0.0068 169  LYS A N   
2076 C  CA  A LYS A 169 ? 0.1389 0.1038 0.0830 0.0256  0.0278  -0.0071 169  LYS A CA  
2077 C  CA  B LYS A 169 ? 0.1569 0.1095 0.1107 0.0718  0.0512  0.0421  169  LYS A CA  
2078 C  CA  C LYS A 169 ? 0.1714 0.1083 0.0993 0.0669  0.0460  0.0203  169  LYS A CA  
2079 C  C   . LYS A 169 ? 0.1174 0.0947 0.0692 0.0257  0.0164  -0.0005 169  LYS A C   
2080 O  O   . LYS A 169 ? 0.1174 0.0901 0.0821 0.0280  0.0205  0.0012  169  LYS A O   
2081 C  CB  A LYS A 169 ? 0.1439 0.1128 0.0918 0.0397  0.0269  0.0192  169  LYS A CB  
2082 C  CB  B LYS A 169 ? 0.1854 0.1572 0.0879 0.0889  0.0342  0.0244  169  LYS A CB  
2083 C  CB  C LYS A 169 ? 0.2260 0.1581 0.1143 0.1031  0.0257  0.0323  169  LYS A CB  
2084 C  CG  A LYS A 169 ? 0.1333 0.0994 0.0555 0.0042  -0.0195 -0.0221 169  LYS A CG  
2085 C  CG  B LYS A 169 ? 0.1690 0.1670 0.1572 0.1128  0.0217  0.0268  169  LYS A CG  
2086 C  CG  C LYS A 169 ? 0.2379 0.2491 0.1706 0.1003  -0.0220 -0.0030 169  LYS A CG  
2087 C  CD  A LYS A 169 ? 0.1347 0.1261 0.1049 0.0323  -0.0177 -0.0016 169  LYS A CD  
2088 C  CD  B LYS A 169 ? 0.1856 0.1576 0.1521 0.0840  -0.0161 -0.0037 169  LYS A CD  
2089 C  CD  C LYS A 169 ? 0.1521 0.2020 0.1777 0.0041  0.0033  0.0422  169  LYS A CD  
2090 C  CE  A LYS A 169 ? 0.1298 0.0895 0.1098 -0.0456 -0.0439 0.0672  169  LYS A CE  
2091 C  CE  B LYS A 169 ? 0.2248 0.1729 0.1462 0.0450  0.0083  0.0219  169  LYS A CE  
2092 C  CE  C LYS A 169 ? 0.1844 0.1694 0.1783 0.0004  -0.0655 0.0194  169  LYS A CE  
2093 N  NZ  A LYS A 169 ? 0.1368 0.1799 0.0580 0.0269  -0.0159 0.0317  169  LYS A NZ  
2094 N  NZ  B LYS A 169 ? 0.1398 0.1039 0.1262 -0.0301 -0.0111 0.0108  169  LYS A NZ  
2095 N  NZ  C LYS A 169 ? 0.1989 0.1040 0.2197 0.0461  -0.0114 -0.0217 169  LYS A NZ  
2097 N  N   . LEU A 170 ? 0.1074 0.0988 0.0709 0.0248  0.0190  -0.0045 170  LEU A N   
2098 C  CA  . LEU A 170 ? 0.1016 0.0880 0.0732 0.0191  0.0118  -0.0066 170  LEU A CA  
2099 C  C   . LEU A 170 ? 0.0865 0.0767 0.0842 0.0000  0.0190  -0.0035 170  LEU A C   
2100 O  O   . LEU A 170 ? 0.0879 0.0866 0.0972 0.0161  0.0162  -0.0148 170  LEU A O   
2101 C  CB  . LEU A 170 ? 0.0763 0.1172 0.0876 0.0096  0.0036  -0.0221 170  LEU A CB  
2102 C  CG  . LEU A 170 ? 0.0883 0.1450 0.0876 0.0109  0.0000  -0.0238 170  LEU A CG  
2103 C  CD1 . LEU A 170 ? 0.0846 0.1722 0.1168 -0.0149 -0.0049 -0.0190 170  LEU A CD1 
2104 C  CD2 . LEU A 170 ? 0.1036 0.1628 0.0837 0.0310  0.0011  -0.0176 170  LEU A CD2 
2111 N  N   A CYS A 171 ? 0.0960 0.0845 0.0701 0.0177  0.0026  -0.0048 171  CYS A N   
2112 N  N   B CYS A 171 ? 0.1127 0.0748 0.0998 -0.0038 0.0095  -0.0124 171  CYS A N   
2113 C  CA  A CYS A 171 ? 0.0832 0.0778 0.0916 0.0156  0.0121  -0.0056 171  CYS A CA  
2114 C  CA  B CYS A 171 ? 0.1225 0.0693 0.1084 0.0005  -0.0045 -0.0182 171  CYS A CA  
2115 C  C   A CYS A 171 ? 0.1019 0.0835 0.0680 0.0059  0.0101  -0.0083 171  CYS A C   
2116 C  C   B CYS A 171 ? 0.0878 0.0566 0.0869 0.0218  0.0258  -0.0385 171  CYS A C   
2117 O  O   A CYS A 171 ? 0.1009 0.1058 0.0781 0.0014  0.0046  -0.0050 171  CYS A O   
2118 O  O   B CYS A 171 ? 0.0693 0.0700 0.2253 0.0431  0.0580  -0.0538 171  CYS A O   
2119 C  CB  A CYS A 171 ? 0.0906 0.0915 0.0808 0.0141  0.0014  0.0040  171  CYS A CB  
2120 C  CB  B CYS A 171 ? 0.1135 0.1156 0.1168 0.0298  0.0126  0.0139  171  CYS A CB  
2121 S  SG  A CYS A 171 ? 0.0877 0.1099 0.1032 0.0059  0.0062  0.0187  171  CYS A SG  
2122 S  SG  B CYS A 171 ? 0.1317 0.2118 0.2037 -0.0079 -0.0451 0.0418  171  CYS A SG  
2129 N  N   . ARG A 172 ? 0.1019 0.0792 0.0781 0.0143  0.0138  -0.0068 172  ARG A N   
2130 C  CA  A ARG A 172 ? 0.1286 0.0858 0.0588 0.0022  0.0114  0.0043  172  ARG A CA  
2131 C  CA  B ARG A 172 ? 0.1138 0.0693 0.1160 0.0159  0.0254  -0.0128 172  ARG A CA  
2132 C  C   . ARG A 172 ? 0.1301 0.0801 0.0855 -0.0047 0.0173  -0.0054 172  ARG A C   
2133 O  O   . ARG A 172 ? 0.1370 0.0851 0.1085 -0.0143 0.0169  -0.0152 172  ARG A O   
2134 C  CB  A ARG A 172 ? 0.1366 0.0759 0.1990 0.0063  -0.0252 0.0081  172  ARG A CB  
2135 C  CB  B ARG A 172 ? 0.1575 0.0841 0.0923 0.0320  0.0223  0.0039  172  ARG A CB  
2136 C  CG  A ARG A 172 ? 0.1428 0.1426 0.1593 0.0263  -0.0243 -0.0236 172  ARG A CG  
2137 C  CG  B ARG A 172 ? 0.2198 0.0934 0.0902 0.0154  0.0000  -0.0047 172  ARG A CG  
2138 C  CD  A ARG A 172 ? 0.2220 0.3218 0.2259 -0.0886 0.0003  -0.1514 172  ARG A CD  
2139 C  CD  B ARG A 172 ? 0.3153 0.1318 0.1086 -0.0453 0.0313  -0.0326 172  ARG A CD  
2140 N  NE  A ARG A 172 ? 0.2357 0.1852 0.1814 -0.1147 0.0624  -0.1615 172  ARG A NE  
2141 N  NE  B ARG A 172 ? 0.5206 0.1134 0.1474 -0.0332 0.0473  -0.0484 172  ARG A NE  
2142 C  CZ  A ARG A 172 ? 0.3965 0.3056 0.1654 -0.0114 0.0495  -0.0760 172  ARG A CZ  
2143 C  CZ  B ARG A 172 ? 0.5906 0.1773 0.3193 0.0174  0.1859  0.0886  172  ARG A CZ  
2144 N  NH1 A ARG A 172 ? 0.4335 0.2806 0.1789 0.0154  0.0942  -0.1205 172  ARG A NH1 
2145 N  NH1 B ARG A 172 ? 0.9368 0.1230 0.4457 -0.0467 0.3711  -0.0350 172  ARG A NH1 
2146 N  NH2 A ARG A 172 ? 0.4723 0.3554 0.1164 0.1307  0.1640  0.1374  172  ARG A NH2 
2147 N  NH2 B ARG A 172 ? 0.6419 0.3324 0.2558 0.1197  -0.0658 -0.1500 172  ARG A NH2 
2149 N  N   . GLN A 173 ? 0.1126 0.0820 0.0749 0.0061  0.0117  0.0009  173  GLN A N   
2150 C  CA  . GLN A 173 ? 0.1015 0.0893 0.0834 -0.0043 0.0128  -0.0006 173  GLN A CA  
2151 C  C   . GLN A 173 ? 0.1125 0.0948 0.0823 0.0029  0.0150  0.0012  173  GLN A C   
2152 O  O   . GLN A 173 ? 0.1169 0.1178 0.1126 0.0133  0.0336  0.0218  173  GLN A O   
2153 C  CB  . GLN A 173 ? 0.1100 0.1023 0.0781 0.0051  0.0196  0.0126  173  GLN A CB  
2154 C  CG  . GLN A 173 ? 0.1230 0.0900 0.0821 0.0072  0.0118  0.0034  173  GLN A CG  
2155 C  CD  . GLN A 173 ? 0.1685 0.0847 0.0781 0.0056  0.0031  -0.0022 173  GLN A CD  
2156 O  OE1 . GLN A 173 ? 0.1815 0.0926 0.1242 0.0150  0.0273  -0.0137 173  GLN A OE1 
2157 N  NE2 . GLN A 173 ? 0.1488 0.0875 0.1133 0.0004  0.0199  0.0079  173  GLN A NE2 
2163 N  N   . CYS A 174 ? 0.0899 0.0981 0.0740 -0.0016 0.0098  -0.0024 174  CYS A N   
2164 C  CA  . CYS A 174 ? 0.1047 0.1025 0.0711 0.0038  0.0086  -0.0124 174  CYS A CA  
2165 C  C   . CYS A 174 ? 0.1130 0.1000 0.0773 -0.0043 -0.0046 -0.0136 174  CYS A C   
2166 O  O   . CYS A 174 ? 0.1404 0.1639 0.1729 0.0012  -0.0091 -0.0867 174  CYS A O   
2167 C  CB  . CYS A 174 ? 0.1254 0.0970 0.0738 0.0017  0.0075  -0.0089 174  CYS A CB  
2168 S  SG  . CYS A 174 ? 0.0921 0.1121 0.0765 0.0022  0.0038  0.0057  174  CYS A SG  
2173 N  N   . LYS A 175 ? 0.1090 0.1000 0.1113 -0.0034 -0.0096 -0.0202 175  LYS A N   
2174 C  CA  . LYS A 175 ? 0.1100 0.1331 0.1012 -0.0257 -0.0042 -0.0124 175  LYS A CA  
2175 C  C   . LYS A 175 ? 0.0845 0.1199 0.0919 -0.0169 0.0015  -0.0269 175  LYS A C   
2176 O  O   . LYS A 175 ? 0.1065 0.1238 0.1058 -0.0049 -0.0073 -0.0176 175  LYS A O   
2177 C  CB  . LYS A 175 ? 0.1204 0.2158 0.0786 -0.0324 -0.0032 -0.0068 175  LYS A CB  
2178 C  CG  . LYS A 175 ? 0.1130 0.2352 0.1228 -0.0127 -0.0040 -0.0372 175  LYS A CG  
2179 C  CD  . LYS A 175 ? 0.1292 0.2719 0.1311 -0.0574 0.0157  -0.0084 175  LYS A CD  
2180 C  CE  . LYS A 175 ? 0.0901 0.4666 0.2345 -0.0094 -0.0183 0.0060  175  LYS A CE  
2181 N  NZ  . LYS A 175 ? 0.1502 0.9321 0.2315 -0.1160 0.0555  -0.1405 175  LYS A NZ  
2186 N  N   . GLY A 176 ? 0.1242 0.1459 0.0892 -0.0233 0.0045  -0.0261 176  GLY A N   
2187 C  CA  . GLY A 176 ? 0.1224 0.1683 0.0935 0.0194  -0.0088 -0.0404 176  GLY A CA  
2188 C  C   . GLY A 176 ? 0.1045 0.1194 0.1030 0.0070  -0.0108 -0.0352 176  GLY A C   
2189 O  O   . GLY A 176 ? 0.1903 0.1404 0.1133 0.0302  -0.0226 -0.0392 176  GLY A O   
2191 N  N   . ASP A 177 ? 0.1143 0.1157 0.0926 -0.0069 0.0055  -0.0358 177  ASP A N   
2192 C  CA  . ASP A 177 ? 0.1052 0.1552 0.0975 -0.0030 -0.0131 -0.0506 177  ASP A CA  
2193 C  C   . ASP A 177 ? 0.1096 0.0927 0.0904 -0.0024 0.0001  -0.0300 177  ASP A C   
2194 O  O   . ASP A 177 ? 0.1154 0.1086 0.0980 -0.0011 -0.0032 -0.0419 177  ASP A O   
2195 C  CB  . ASP A 177 ? 0.1371 0.2426 0.1040 0.0424  -0.0238 -0.0429 177  ASP A CB  
2196 C  CG  . ASP A 177 ? 0.1438 0.3246 0.2051 0.0398  -0.0637 0.0014  177  ASP A CG  
2197 O  OD1 . ASP A 177 ? 0.1634 0.3698 0.2492 -0.0220 -0.0273 -0.0293 177  ASP A OD1 
2198 O  OD2 . ASP A 177 ? 0.2100 0.3631 0.4005 0.1224  -0.0640 -0.0310 177  ASP A OD2 
2200 N  N   . PRO A 178 ? 0.1293 0.1081 0.0958 0.0059  -0.0011 -0.0367 178  PRO A N   
2201 C  CA  . PRO A 178 ? 0.1253 0.1071 0.1256 0.0197  0.0055  -0.0346 178  PRO A CA  
2202 C  C   . PRO A 178 ? 0.1027 0.1234 0.0950 0.0218  -0.0018 -0.0314 178  PRO A C   
2203 O  O   . PRO A 178 ? 0.1111 0.1153 0.1074 0.0085  0.0072  -0.0175 178  PRO A O   
2204 C  CB  . PRO A 178 ? 0.1321 0.1273 0.1640 0.0205  -0.0085 -0.0650 178  PRO A CB  
2205 C  CG  . PRO A 178 ? 0.1539 0.1256 0.1532 0.0098  0.0042  -0.0486 178  PRO A CG  
2206 C  CD  . PRO A 178 ? 0.1534 0.1119 0.1266 -0.0031 -0.0053 -0.0511 178  PRO A CD  
2208 N  N   . LYS A 179 ? 0.1185 0.1311 0.0907 0.0091  0.0048  -0.0175 179  LYS A N   
2209 C  CA  . LYS A 179 ? 0.1354 0.1437 0.0932 0.0166  -0.0049 -0.0060 179  LYS A CA  
2210 C  C   . LYS A 179 ? 0.1283 0.1166 0.0994 0.0025  -0.0023 0.0174  179  LYS A C   
2211 O  O   . LYS A 179 ? 0.1777 0.1616 0.1199 -0.0304 0.0133  -0.0006 179  LYS A O   
2212 C  CB  . LYS A 179 ? 0.2125 0.1525 0.0923 0.0377  -0.0094 -0.0038 179  LYS A CB  
2213 C  CG  . LYS A 179 ? 0.3344 0.1515 0.1412 -0.0196 -0.0171 0.0261  179  LYS A CG  
2214 C  CD  . LYS A 179 ? 0.5582 0.1665 0.1365 -0.0346 -0.0688 0.0391  179  LYS A CD  
2215 C  CE  . LYS A 179 ? 0.7928 0.3158 0.1509 -0.2360 -0.0788 0.0629  179  LYS A CE  
2216 N  NZ  . LYS A 179 ? 0.9835 0.6796 0.3485 -0.3631 0.2872  -0.2986 179  LYS A NZ  
2219 N  N   . THR A 180 ? 0.1146 0.0973 0.0997 0.0129  -0.0191 -0.0017 180  THR A N   
2220 C  CA  . THR A 180 ? 0.1192 0.0888 0.1215 0.0107  -0.0239 -0.0028 180  THR A CA  
2221 C  C   . THR A 180 ? 0.0857 0.0794 0.1221 -0.0025 -0.0202 -0.0183 180  THR A C   
2222 O  O   . THR A 180 ? 0.1030 0.0707 0.1470 0.0079  -0.0198 -0.0242 180  THR A O   
2223 C  CB  . THR A 180 ? 0.1567 0.1162 0.1444 0.0368  -0.0381 -0.0127 180  THR A CB  
2224 O  OG1 . THR A 180 ? 0.1174 0.1766 0.1769 0.0260  -0.0119 -0.0189 180  THR A OG1 
2225 C  CG2 . THR A 180 ? 0.2295 0.1440 0.1567 0.0421  -0.0718 0.0029  180  THR A CG2 
2228 N  N   . LYS A 181 ? 0.0936 0.0717 0.0981 -0.0027 -0.0162 -0.0172 181  LYS A N   
2229 C  CA  . LYS A 181 ? 0.0964 0.0781 0.0972 -0.0125 0.0079  -0.0223 181  LYS A CA  
2230 C  C   . LYS A 181 ? 0.0933 0.0744 0.0827 -0.0033 0.0021  -0.0073 181  LYS A C   
2231 O  O   . LYS A 181 ? 0.1039 0.0945 0.0844 -0.0068 0.0042  -0.0171 181  LYS A O   
2232 C  CB  . LYS A 181 ? 0.1100 0.0861 0.0897 0.0012  -0.0005 -0.0076 181  LYS A CB  
2233 C  CG  . LYS A 181 ? 0.1229 0.0759 0.1060 -0.0016 0.0160  -0.0206 181  LYS A CG  
2234 C  CD  . LYS A 181 ? 0.1578 0.0859 0.1469 0.0202  0.0231  0.0008  181  LYS A CD  
2235 C  CE  . LYS A 181 ? 0.1823 0.0759 0.2721 0.0000  0.0552  -0.0114 181  LYS A CE  
2236 N  NZ  . LYS A 181 ? 0.2142 0.0928 0.2289 0.0162  0.0784  0.0027  181  LYS A NZ  
2240 N  N   A CYS A 182 ? 0.0854 0.0707 0.0910 0.0043  -0.0033 -0.0134 182  CYS A N   
2241 N  N   B CYS A 182 ? 0.1116 0.0950 0.0661 -0.0333 -0.0058 0.0098  182  CYS A N   
2242 C  CA  A CYS A 182 ? 0.0828 0.0743 0.0815 0.0027  -0.0051 -0.0123 182  CYS A CA  
2243 C  CA  B CYS A 182 ? 0.1176 0.1075 0.0842 -0.0443 -0.0355 0.0514  182  CYS A CA  
2244 C  C   A CYS A 182 ? 0.0784 0.0821 0.0759 -0.0019 -0.0015 -0.0214 182  CYS A C   
2245 C  C   B CYS A 182 ? 0.1103 0.1021 0.0968 -0.0369 -0.0285 0.0185  182  CYS A C   
2246 O  O   A CYS A 182 ? 0.0978 0.0884 0.0859 -0.0085 -0.0126 -0.0072 182  CYS A O   
2247 O  O   B CYS A 182 ? 0.1927 0.1325 0.1963 -0.1321 -0.1075 0.0836  182  CYS A O   
2248 C  CB  A CYS A 182 ? 0.0759 0.0922 0.1044 0.0064  0.0060  0.0018  182  CYS A CB  
2249 C  CB  B CYS A 182 ? 0.0895 0.1518 0.1127 -0.0115 -0.0906 -0.0312 182  CYS A CB  
2250 S  SG  A CYS A 182 ? 0.0900 0.0926 0.1014 0.0001  -0.0099 0.0003  182  CYS A SG  
2251 S  SG  B CYS A 182 ? 0.2270 0.1510 0.1830 0.0258  -0.0844 0.0104  182  CYS A SG  
2256 N  N   . ALA A 183 ? 0.0981 0.0751 0.0778 -0.0003 -0.0066 -0.0061 183  ALA A N   
2257 C  CA  . ALA A 183 ? 0.1041 0.0771 0.0847 -0.0098 -0.0036 -0.0064 183  ALA A CA  
2258 C  C   . ALA A 183 ? 0.0971 0.0667 0.0829 -0.0019 -0.0174 0.0028  183  ALA A C   
2259 O  O   . ALA A 183 ? 0.1088 0.0626 0.0841 -0.0041 -0.0068 -0.0052 183  ALA A O   
2260 C  CB  . ALA A 183 ? 0.1759 0.0703 0.1040 -0.0044 -0.0492 0.0032  183  ALA A CB  
2262 N  N   . ARG A 184 ? 0.0990 0.0682 0.0918 -0.0065 -0.0134 -0.0029 184  ARG A N   
2263 C  CA  . ARG A 184 ? 0.1025 0.0611 0.0997 -0.0060 -0.0208 -0.0059 184  ARG A CA  
2264 C  C   . ARG A 184 ? 0.1023 0.0593 0.0775 -0.0127 -0.0172 0.0030  184  ARG A C   
2265 O  O   . ARG A 184 ? 0.1051 0.0815 0.0740 -0.0121 -0.0178 0.0052  184  ARG A O   
2266 C  CB  . ARG A 184 ? 0.0966 0.0678 0.0875 0.0006  -0.0118 -0.0007 184  ARG A CB  
2267 C  CG  . ARG A 184 ? 0.0950 0.0839 0.0948 0.0017  -0.0129 0.0052  184  ARG A CG  
2268 C  CD  . ARG A 184 ? 0.0965 0.0879 0.1135 -0.0110 -0.0237 0.0087  184  ARG A CD  
2269 N  NE  . ARG A 184 ? 0.0930 0.0915 0.1106 -0.0082 -0.0121 0.0126  184  ARG A NE  
2270 C  CZ  . ARG A 184 ? 0.0899 0.0822 0.1135 -0.0069 -0.0187 0.0252  184  ARG A CZ  
2271 N  NH1 . ARG A 184 ? 0.1033 0.1250 0.0967 -0.0225 -0.0160 0.0221  184  ARG A NH1 
2272 N  NH2 . ARG A 184 ? 0.0972 0.1271 0.1345 -0.0067 -0.0168 0.0318  184  ARG A NH2 
2280 N  N   . ASN A 185 ? 0.0981 0.0631 0.0814 -0.0016 -0.0213 0.0018  185  ASN A N   
2281 C  CA  . ASN A 185 ? 0.0918 0.0775 0.0869 -0.0029 -0.0251 -0.0025 185  ASN A CA  
2282 C  C   . ASN A 185 ? 0.1053 0.0749 0.0634 -0.0060 -0.0070 0.0026  185  ASN A C   
2283 O  O   . ASN A 185 ? 0.1033 0.0952 0.0872 -0.0149 -0.0159 0.0063  185  ASN A O   
2284 C  CB  . ASN A 185 ? 0.0989 0.0744 0.0762 -0.0019 -0.0151 0.0074  185  ASN A CB  
2285 C  CG  . ASN A 185 ? 0.0965 0.0638 0.0950 -0.0017 -0.0273 0.0062  185  ASN A CG  
2286 O  OD1 . ASN A 185 ? 0.1501 0.0686 0.1064 0.0106  -0.0366 -0.0056 185  ASN A OD1 
2287 N  ND2 . ASN A 185 ? 0.1221 0.0878 0.0748 0.0045  -0.0239 -0.0023 185  ASN A ND2 
2293 N  N   . ALA A 186 ? 0.1170 0.0677 0.0627 -0.0074 -0.0171 -0.0010 186  ALA A N   
2294 C  CA  . ALA A 186 ? 0.1310 0.0745 0.0762 -0.0202 0.0036  -0.0126 186  ALA A CA  
2295 C  C   . ALA A 186 ? 0.1040 0.0674 0.0656 -0.0007 -0.0148 -0.0037 186  ALA A C   
2296 O  O   . ALA A 186 ? 0.0911 0.0666 0.0774 0.0045  -0.0115 -0.0039 186  ALA A O   
2297 C  CB  . ALA A 186 ? 0.1541 0.0631 0.1772 0.0065  0.0731  -0.0088 186  ALA A CB  
2299 N  N   . PRO A 187 ? 0.0954 0.0733 0.0781 -0.0067 -0.0184 -0.0066 187  PRO A N   
2300 C  CA  . PRO A 187 ? 0.0839 0.0876 0.0946 -0.0021 -0.0144 -0.0065 187  PRO A CA  
2301 C  C   . PRO A 187 ? 0.0795 0.0929 0.0818 -0.0016 0.0037  -0.0040 187  PRO A C   
2302 O  O   . PRO A 187 ? 0.0891 0.1404 0.0927 0.0226  0.0006  -0.0140 187  PRO A O   
2303 C  CB  . PRO A 187 ? 0.1180 0.1012 0.1027 -0.0295 -0.0091 0.0030  187  PRO A CB  
2304 C  CG  . PRO A 187 ? 0.1520 0.1024 0.1090 -0.0466 -0.0281 -0.0042 187  PRO A CG  
2305 C  CD  . PRO A 187 ? 0.1456 0.0907 0.0753 -0.0353 -0.0176 -0.0082 187  PRO A CD  
2310 N  N   . TYR A 188 ? 0.0796 0.0690 0.0630 -0.0015 -0.0052 -0.0004 188  TYR A N   
2311 C  CA  . TYR A 188 ? 0.0775 0.0630 0.0639 -0.0014 0.0037  0.0017  188  TYR A CA  
2312 C  C   . TYR A 188 ? 0.0729 0.0610 0.0624 0.0033  0.0016  -0.0095 188  TYR A C   
2313 O  O   . TYR A 188 ? 0.0841 0.0744 0.0616 -0.0062 -0.0008 0.0018  188  TYR A O   
2314 C  CB  . TYR A 188 ? 0.0806 0.0645 0.0802 0.0008  0.0017  -0.0085 188  TYR A CB  
2315 C  CG  . TYR A 188 ? 0.0833 0.0674 0.0590 -0.0052 -0.0043 -0.0022 188  TYR A CG  
2316 C  CD1 . TYR A 188 ? 0.0917 0.0730 0.0763 -0.0071 0.0104  0.0003  188  TYR A CD1 
2317 C  CD2 . TYR A 188 ? 0.0942 0.0727 0.0640 -0.0094 0.0091  -0.0068 188  TYR A CD2 
2318 C  CE1 . TYR A 188 ? 0.0896 0.0697 0.0971 -0.0151 0.0046  0.0010  188  TYR A CE1 
2319 C  CE2 . TYR A 188 ? 0.1098 0.0717 0.0807 -0.0044 0.0019  0.0003  188  TYR A CE2 
2320 C  CZ  . TYR A 188 ? 0.1060 0.0723 0.0785 -0.0182 0.0062  -0.0013 188  TYR A CZ  
2321 O  OH  . TYR A 188 ? 0.1296 0.0775 0.0988 -0.0221 0.0180  0.0053  188  TYR A OH  
2330 N  N   . SER A 189 ? 0.0753 0.0629 0.0634 -0.0017 -0.0024 -0.0042 189  SER A N   
2331 C  CA  . SER A 189 ? 0.0756 0.0624 0.0604 0.0039  0.0035  -0.0053 189  SER A CA  
2332 C  C   . SER A 189 ? 0.0683 0.0564 0.0510 0.0018  0.0024  0.0027  189  SER A C   
2333 O  O   . SER A 189 ? 0.0699 0.0674 0.0620 0.0017  0.0078  -0.0015 189  SER A O   
2334 C  CB  . SER A 189 ? 0.0853 0.0790 0.0582 0.0041  0.0055  -0.0016 189  SER A CB  
2335 O  OG  . SER A 189 ? 0.0936 0.0624 0.0663 0.0032  -0.0044 -0.0064 189  SER A OG  
2341 N  N   . GLY A 190 ? 0.0694 0.0580 0.0514 -0.0009 0.0035  -0.0029 190  GLY A N   
2342 C  CA  . GLY A 190 ? 0.0651 0.0593 0.0584 -0.0013 0.0025  -0.0049 190  GLY A CA  
2343 C  C   . GLY A 190 ? 0.0608 0.0604 0.0581 -0.0083 0.0042  -0.0046 190  GLY A C   
2344 O  O   . GLY A 190 ? 0.0755 0.0566 0.0552 -0.0005 0.0073  -0.0009 190  GLY A O   
2347 N  N   . TYR A 191 ? 0.0643 0.0581 0.0518 -0.0012 0.0070  -0.0021 191  TYR A N   
2348 C  CA  . TYR A 191 ? 0.0670 0.0638 0.0515 -0.0025 0.0038  -0.0006 191  TYR A CA  
2349 C  C   . TYR A 191 ? 0.0687 0.0617 0.0454 0.0003  0.0033  -0.0030 191  TYR A C   
2350 O  O   . TYR A 191 ? 0.0696 0.0661 0.0564 -0.0066 0.0042  0.0006  191  TYR A O   
2351 C  CB  . TYR A 191 ? 0.0611 0.0641 0.0576 -0.0049 0.0077  -0.0043 191  TYR A CB  
2352 C  CG  . TYR A 191 ? 0.0603 0.0580 0.0476 -0.0042 0.0100  -0.0081 191  TYR A CG  
2353 C  CD1 . TYR A 191 ? 0.0643 0.0611 0.0489 0.0113  -0.0023 0.0030  191  TYR A CD1 
2354 C  CD2 . TYR A 191 ? 0.0633 0.0687 0.0519 0.0017  -0.0058 -0.0038 191  TYR A CD2 
2355 C  CE1 . TYR A 191 ? 0.0591 0.0592 0.0510 0.0013  0.0011  -0.0039 191  TYR A CE1 
2356 C  CE2 . TYR A 191 ? 0.0673 0.0588 0.0584 0.0047  -0.0068 0.0016  191  TYR A CE2 
2357 C  CZ  . TYR A 191 ? 0.0653 0.0518 0.0529 0.0041  0.0018  -0.0046 191  TYR A CZ  
2358 O  OH  . TYR A 191 ? 0.0679 0.0497 0.0639 0.0018  0.0012  0.0000  191  TYR A OH  
2366 N  N   . SER A 192 ? 0.0621 0.0636 0.0579 -0.0088 0.0006  0.0006  192  SER A N   
2367 C  CA  . SER A 192 ? 0.0638 0.0656 0.0610 -0.0061 0.0074  0.0055  192  SER A CA  
2368 C  C   . SER A 192 ? 0.0637 0.0632 0.0586 -0.0072 -0.0026 0.0053  192  SER A C   
2369 O  O   . SER A 192 ? 0.0749 0.0655 0.0711 -0.0118 0.0116  0.0015  192  SER A O   
2370 C  CB  . SER A 192 ? 0.0702 0.0672 0.0878 0.0028  0.0041  -0.0013 192  SER A CB  
2371 O  OG  . SER A 192 ? 0.0751 0.0768 0.0931 0.0075  0.0168  0.0025  192  SER A OG  
2373 N  N   . GLY A 193 ? 0.0633 0.0636 0.0581 -0.0046 -0.0007 -0.0007 193  GLY A N   
2374 C  CA  . GLY A 193 ? 0.0658 0.0701 0.0562 -0.0062 0.0050  -0.0020 193  GLY A CA  
2375 C  C   . GLY A 193 ? 0.0703 0.0578 0.0499 -0.0097 0.0067  0.0026  193  GLY A C   
2376 O  O   . GLY A 193 ? 0.0819 0.0644 0.0680 -0.0114 0.0047  0.0005  193  GLY A O   
2380 N  N   . ALA A 194 ? 0.0710 0.0581 0.0553 -0.0035 0.0048  0.0031  194  ALA A N   
2381 C  CA  . ALA A 194 ? 0.0688 0.0577 0.0616 -0.0089 0.0008  0.0015  194  ALA A CA  
2382 C  C   . ALA A 194 ? 0.0707 0.0619 0.0596 -0.0051 -0.0036 -0.0010 194  ALA A C   
2383 O  O   . ALA A 194 ? 0.0787 0.0700 0.0628 0.0009  0.0019  0.0063  194  ALA A O   
2384 C  CB  . ALA A 194 ? 0.0685 0.0617 0.0704 -0.0073 -0.0029 0.0022  194  ALA A CB  
2389 N  N   . PHE A 195 ? 0.0741 0.0625 0.0580 -0.0063 0.0045  0.0033  195  PHE A N   
2390 C  CA  . PHE A 195 ? 0.0721 0.0653 0.0666 -0.0026 0.0103  0.0029  195  PHE A CA  
2391 C  C   . PHE A 195 ? 0.0721 0.0638 0.0697 -0.0019 0.0086  0.0079  195  PHE A C   
2392 O  O   . PHE A 195 ? 0.0916 0.0675 0.0623 -0.0098 0.0107  0.0042  195  PHE A O   
2393 C  CB  . PHE A 195 ? 0.1055 0.0610 0.0845 -0.0069 0.0355  0.0030  195  PHE A CB  
2394 C  CG  . PHE A 195 ? 0.0974 0.0767 0.0807 -0.0048 0.0306  0.0012  195  PHE A CG  
2395 C  CD1 . PHE A 195 ? 0.1252 0.0861 0.0709 -0.0166 0.0306  -0.0062 195  PHE A CD1 
2396 C  CD2 . PHE A 195 ? 0.0990 0.1106 0.0909 -0.0021 0.0238  0.0119  195  PHE A CD2 
2397 C  CE1 . PHE A 195 ? 0.1379 0.1038 0.0880 -0.0215 0.0429  0.0029  195  PHE A CE1 
2398 C  CE2 . PHE A 195 ? 0.1143 0.0990 0.1118 -0.0167 0.0415  0.0028  195  PHE A CE2 
2399 C  CZ  . PHE A 195 ? 0.1304 0.1024 0.1053 -0.0209 0.0402  0.0081  195  PHE A CZ  
2407 N  N   . HIS A 196 ? 0.0846 0.0640 0.0647 -0.0133 0.0064  0.0069  196  HIS A N   
2408 C  CA  . HIS A 196 ? 0.0823 0.0643 0.0748 -0.0181 0.0044  0.0109  196  HIS A CA  
2409 C  C   . HIS A 196 ? 0.0768 0.0629 0.0762 -0.0214 0.0004  0.0045  196  HIS A C   
2410 O  O   . HIS A 196 ? 0.0915 0.0657 0.0843 -0.0145 0.0084  0.0059  196  HIS A O   
2411 C  CB  . HIS A 196 ? 0.0836 0.0825 0.0932 -0.0162 -0.0017 0.0081  196  HIS A CB  
2412 C  CG  . HIS A 196 ? 0.0779 0.0871 0.0967 -0.0145 -0.0102 0.0115  196  HIS A CG  
2413 N  ND1 . HIS A 196 ? 0.0903 0.0961 0.2367 -0.0155 0.0399  0.0108  196  HIS A ND1 
2414 C  CD2 . HIS A 196 ? 0.0963 0.0988 0.0844 -0.0101 0.0102  0.0039  196  HIS A CD2 
2415 C  CE1 . HIS A 196 ? 0.0947 0.1139 0.2088 -0.0002 0.0301  0.0213  196  HIS A CE1 
2416 N  NE2 . HIS A 196 ? 0.0904 0.1082 0.1266 0.0037  0.0170  0.0263  196  HIS A NE2 
2422 N  N   . CYS A 197 ? 0.0828 0.0634 0.0660 -0.0094 0.0011  0.0036  197  CYS A N   
2423 C  CA  . CYS A 197 ? 0.0987 0.0603 0.0724 -0.0084 0.0098  0.0024  197  CYS A CA  
2424 C  C   . CYS A 197 ? 0.0886 0.0651 0.0696 -0.0070 0.0096  -0.0005 197  CYS A C   
2425 O  O   . CYS A 197 ? 0.1135 0.0595 0.0774 -0.0055 0.0117  0.0042  197  CYS A O   
2426 C  CB  . CYS A 197 ? 0.0925 0.0629 0.0620 -0.0083 0.0090  -0.0046 197  CYS A CB  
2427 S  SG  . CYS A 197 ? 0.0995 0.0672 0.0877 -0.0052 0.0199  -0.0039 197  CYS A SG  
2430 N  N   . LEU A 198 ? 0.0777 0.0627 0.0656 -0.0061 0.0046  0.0071  198  LEU A N   
2431 C  CA  . LEU A 198 ? 0.0864 0.0714 0.0640 -0.0189 0.0096  0.0071  198  LEU A CA  
2432 C  C   . LEU A 198 ? 0.0923 0.0665 0.0642 -0.0165 0.0101  0.0057  198  LEU A C   
2433 O  O   . LEU A 198 ? 0.1080 0.0569 0.0863 -0.0095 0.0179  0.0081  198  LEU A O   
2434 C  CB  . LEU A 198 ? 0.0847 0.0663 0.0703 -0.0053 0.0102  -0.0005 198  LEU A CB  
2435 C  CG  . LEU A 198 ? 0.1017 0.0721 0.0680 -0.0024 0.0160  0.0075  198  LEU A CG  
2436 C  CD1 . LEU A 198 ? 0.1194 0.1006 0.0741 0.0071  0.0046  0.0052  198  LEU A CD1 
2437 C  CD2 . LEU A 198 ? 0.1029 0.0918 0.0779 -0.0055 0.0025  -0.0057 198  LEU A CD2 
2446 N  N   . LYS A 199 ? 0.0904 0.0634 0.0824 -0.0105 0.0176  0.0058  199  LYS A N   
2447 C  CA  . LYS A 199 ? 0.0918 0.0749 0.0852 -0.0119 0.0128  0.0123  199  LYS A CA  
2448 C  C   . LYS A 199 ? 0.0833 0.0768 0.0779 -0.0186 0.0091  0.0134  199  LYS A C   
2449 O  O   . LYS A 199 ? 0.1174 0.0675 0.0994 -0.0226 0.0204  0.0090  199  LYS A O   
2450 C  CB  . LYS A 199 ? 0.0886 0.0747 0.0939 -0.0112 0.0082  0.0138  199  LYS A CB  
2451 C  CG  . LYS A 199 ? 0.0903 0.0981 0.1151 -0.0171 0.0158  0.0045  199  LYS A CG  
2452 C  CD  . LYS A 199 ? 0.0885 0.1166 0.1657 -0.0081 0.0062  0.0193  199  LYS A CD  
2453 C  CE  . LYS A 199 ? 0.0915 0.2204 0.1910 -0.0305 0.0014  0.0456  199  LYS A CE  
2454 N  NZ  . LYS A 199 ? 0.1465 0.2633 0.1890 -0.0974 -0.0430 0.0676  199  LYS A NZ  
2460 N  N   . ASP A 200 ? 0.0912 0.0622 0.0883 -0.0156 0.0103  0.0065  200  ASP A N   
2461 C  CA  . ASP A 200 ? 0.0919 0.0715 0.0875 -0.0250 0.0133  0.0053  200  ASP A CA  
2462 C  C   . ASP A 200 ? 0.1142 0.0630 0.0892 -0.0177 0.0110  0.0065  200  ASP A C   
2463 O  O   . ASP A 200 ? 0.1142 0.0746 0.1297 -0.0197 0.0118  -0.0129 200  ASP A O   
2464 C  CB  . ASP A 200 ? 0.0969 0.0808 0.0958 -0.0314 0.0079  0.0051  200  ASP A CB  
2465 C  CG  . ASP A 200 ? 0.1058 0.0875 0.1020 -0.0278 -0.0002 0.0058  200  ASP A CG  
2466 O  OD1 . ASP A 200 ? 0.1094 0.0915 0.1098 -0.0151 0.0108  0.0110  200  ASP A OD1 
2467 O  OD2 . ASP A 200 ? 0.1154 0.1192 0.0950 -0.0271 0.0031  0.0159  200  ASP A OD2 
2472 N  N   . GLY A 201 ? 0.0996 0.0649 0.0916 -0.0135 0.0113  0.0135  201  GLY A N   
2473 C  CA  . GLY A 201 ? 0.1053 0.0745 0.1022 -0.0127 0.0120  0.0147  201  GLY A CA  
2474 C  C   . GLY A 201 ? 0.1145 0.0669 0.1053 -0.0009 0.0156  0.0066  201  GLY A C   
2475 O  O   . GLY A 201 ? 0.1298 0.0873 0.1543 0.0162  0.0395  0.0321  201  GLY A O   
2477 N  N   . LYS A 202 ? 0.0971 0.0652 0.0887 -0.0074 0.0151  0.0041  202  LYS A N   
2478 C  CA  . LYS A 202 ? 0.1072 0.0667 0.0802 -0.0074 0.0128  -0.0003 202  LYS A CA  
2479 C  C   . LYS A 202 ? 0.1096 0.0709 0.0740 -0.0063 0.0107  0.0050  202  LYS A C   
2480 O  O   . LYS A 202 ? 0.1020 0.1380 0.0835 -0.0145 0.0215  -0.0172 202  LYS A O   
2481 C  CB  . LYS A 202 ? 0.1093 0.0734 0.0821 -0.0121 0.0078  0.0018  202  LYS A CB  
2482 C  CG  . LYS A 202 ? 0.1395 0.0984 0.1061 -0.0274 -0.0009 -0.0124 202  LYS A CG  
2483 C  CD  . LYS A 202 ? 0.2809 0.1103 0.3574 0.0324  -0.1605 -0.0843 202  LYS A CD  
2484 C  CE  . LYS A 202 ? 0.3999 0.1999 0.3510 0.0139  -0.1369 -0.1680 202  LYS A CE  
2485 N  NZ  . LYS A 202 ? 0.4741 0.2685 0.5579 0.0623  -0.1122 -0.2473 202  LYS A NZ  
2491 N  N   . GLY A 203 ? 0.1041 0.0737 0.0773 -0.0008 0.0086  0.0005  203  GLY A N   
2492 C  CA  . GLY A 203 ? 0.0919 0.0732 0.0807 -0.0011 0.0051  0.0095  203  GLY A CA  
2493 C  C   . GLY A 203 ? 0.1017 0.0692 0.0785 -0.0038 0.0054  -0.0012 203  GLY A C   
2494 O  O   . GLY A 203 ? 0.1052 0.1156 0.0924 0.0068  0.0167  0.0011  203  GLY A O   
2497 N  N   . ASP A 204 ? 0.0919 0.0707 0.0782 -0.0024 0.0068  0.0080  204  ASP A N   
2498 C  CA  . ASP A 204 ? 0.0980 0.0734 0.0744 -0.0036 0.0048  0.0091  204  ASP A CA  
2499 C  C   . ASP A 204 ? 0.0903 0.0782 0.0639 0.0011  0.0024  0.0138  204  ASP A C   
2500 O  O   . ASP A 204 ? 0.1056 0.0842 0.0716 0.0034  0.0179  0.0121  204  ASP A O   
2501 C  CB  . ASP A 204 ? 0.1275 0.0747 0.0790 0.0141  -0.0036 0.0088  204  ASP A CB  
2502 C  CG  . ASP A 204 ? 0.1504 0.0761 0.1061 0.0047  0.0144  0.0203  204  ASP A CG  
2503 O  OD1 . ASP A 204 ? 0.1767 0.0846 0.1150 0.0223  0.0093  0.0097  204  ASP A OD1 
2504 O  OD2 . ASP A 204 ? 0.1819 0.0759 0.2136 -0.0138 0.0223  0.0260  204  ASP A OD2 
2508 N  N   . VAL A 205 ? 0.1070 0.0666 0.0654 0.0045  0.0115  0.0053  205  VAL A N   
2509 C  CA  . VAL A 205 ? 0.0945 0.0713 0.0566 0.0069  0.0133  0.0071  205  VAL A CA  
2510 C  C   . VAL A 205 ? 0.0837 0.0658 0.0592 -0.0013 0.0127  0.0016  205  VAL A C   
2511 O  O   . VAL A 205 ? 0.1130 0.0751 0.0598 0.0096  0.0166  -0.0003 205  VAL A O   
2512 C  CB  . VAL A 205 ? 0.0899 0.0689 0.0746 0.0080  0.0116  0.0143  205  VAL A CB  
2513 C  CG1 . VAL A 205 ? 0.0861 0.0876 0.0871 0.0131  0.0052  -0.0046 205  VAL A CG1 
2514 C  CG2 . VAL A 205 ? 0.0961 0.0790 0.0754 0.0047  0.0083  -0.0005 205  VAL A CG2 
2523 N  N   . ALA A 206 ? 0.0816 0.0633 0.0519 0.0042  0.0040  0.0076  206  ALA A N   
2524 C  CA  . ALA A 206 ? 0.0809 0.0579 0.0555 0.0015  0.0075  0.0047  206  ALA A CA  
2525 C  C   . ALA A 206 ? 0.0669 0.0689 0.0501 0.0043  0.0081  0.0048  206  ALA A C   
2526 O  O   . ALA A 206 ? 0.0956 0.0823 0.0475 -0.0141 0.0088  -0.0010 206  ALA A O   
2527 C  CB  . ALA A 206 ? 0.0804 0.0790 0.0817 -0.0052 -0.0096 0.0182  206  ALA A CB  
2531 N  N   . PHE A 207 ? 0.0708 0.0601 0.0472 0.0014  0.0075  0.0006  207  PHE A N   
2532 C  CA  . PHE A 207 ? 0.0638 0.0574 0.0535 0.0029  0.0013  0.0028  207  PHE A CA  
2533 C  C   . PHE A 207 ? 0.0611 0.0651 0.0531 0.0044  -0.0033 0.0007  207  PHE A C   
2534 O  O   . PHE A 207 ? 0.0705 0.0733 0.0505 0.0109  0.0051  0.0041  207  PHE A O   
2535 C  CB  . PHE A 207 ? 0.0703 0.0653 0.0659 0.0110  0.0069  0.0041  207  PHE A CB  
2536 C  CG  . PHE A 207 ? 0.0630 0.0653 0.0627 0.0043  0.0065  0.0118  207  PHE A CG  
2537 C  CD1 . PHE A 207 ? 0.0741 0.0720 0.0745 0.0035  0.0005  0.0089  207  PHE A CD1 
2538 C  CD2 . PHE A 207 ? 0.0774 0.0737 0.0816 0.0102  0.0043  0.0094  207  PHE A CD2 
2539 C  CE1 . PHE A 207 ? 0.0702 0.0969 0.0720 0.0111  -0.0018 0.0084  207  PHE A CE1 
2540 C  CE2 . PHE A 207 ? 0.0820 0.0859 0.0841 0.0189  0.0009  0.0121  207  PHE A CE2 
2541 C  CZ  . PHE A 207 ? 0.0753 0.0900 0.0887 0.0142  0.0028  0.0137  207  PHE A CZ  
2548 N  N   . VAL A 208 ? 0.0636 0.0664 0.0538 0.0089  0.0035  0.0034  208  VAL A N   
2549 C  CA  . VAL A 208 ? 0.0633 0.0551 0.0556 0.0094  -0.0044 0.0071  208  VAL A CA  
2550 C  C   . VAL A 208 ? 0.0683 0.0518 0.0459 0.0042  0.0000  0.0065  208  VAL A C   
2551 O  O   . VAL A 208 ? 0.0655 0.0666 0.0567 0.0049  -0.0018 0.0004  208  VAL A O   
2552 C  CB  . VAL A 208 ? 0.0711 0.0645 0.0583 0.0023  0.0016  0.0054  208  VAL A CB  
2553 C  CG1 . VAL A 208 ? 0.0760 0.0725 0.0640 -0.0010 -0.0038 -0.0003 208  VAL A CG1 
2554 C  CG2 . VAL A 208 ? 0.0709 0.0810 0.0667 -0.0039 0.0061  0.0045  208  VAL A CG2 
2562 N  N   . LYS A 209 ? 0.0675 0.0677 0.0536 0.0053  -0.0014 -0.0033 209  LYS A N   
2563 C  CA  . LYS A 209 ? 0.0612 0.0654 0.0569 0.0086  -0.0026 -0.0055 209  LYS A CA  
2564 C  C   . LYS A 209 ? 0.0655 0.0637 0.0568 0.0109  0.0005  0.0053  209  LYS A C   
2565 O  O   . LYS A 209 ? 0.0701 0.0701 0.0525 0.0029  -0.0023 0.0048  209  LYS A O   
2566 C  CB  . LYS A 209 ? 0.0651 0.0735 0.0510 0.0006  0.0061  -0.0008 209  LYS A CB  
2567 C  CG  . LYS A 209 ? 0.0685 0.0688 0.0487 0.0054  -0.0020 -0.0014 209  LYS A CG  
2568 C  CD  . LYS A 209 ? 0.0768 0.0686 0.0541 0.0000  0.0060  0.0016  209  LYS A CD  
2569 C  CE  . LYS A 209 ? 0.0854 0.0694 0.0609 0.0063  -0.0049 -0.0017 209  LYS A CE  
2570 N  NZ  . LYS A 209 ? 0.0818 0.0694 0.0711 0.0082  -0.0100 0.0024  209  LYS A NZ  
2582 N  N   . HIS A 210 ? 0.0850 0.0632 0.0492 0.0078  0.0037  0.0028  210  HIS A N   
2583 C  CA  . HIS A 210 ? 0.0768 0.0756 0.0591 0.0078  0.0062  -0.0009 210  HIS A CA  
2584 C  C   . HIS A 210 ? 0.0811 0.0791 0.0573 -0.0007 0.0073  -0.0040 210  HIS A C   
2585 O  O   . HIS A 210 ? 0.0981 0.1305 0.0725 -0.0081 0.0150  0.0180  210  HIS A O   
2586 C  CB  . HIS A 210 ? 0.0801 0.0904 0.0604 -0.0021 0.0046  -0.0095 210  HIS A CB  
2587 C  CG  . HIS A 210 ? 0.0919 0.0820 0.0719 -0.0035 0.0129  -0.0130 210  HIS A CG  
2588 N  ND1 . HIS A 210 ? 0.0939 0.0842 0.0643 0.0093  0.0137  -0.0020 210  HIS A ND1 
2589 C  CD2 . HIS A 210 ? 0.0913 0.0984 0.0894 0.0035  0.0313  -0.0053 210  HIS A CD2 
2590 C  CE1 . HIS A 210 ? 0.0925 0.0889 0.0890 0.0099  0.0250  -0.0072 210  HIS A CE1 
2591 N  NE2 . HIS A 210 ? 0.0983 0.0812 0.1036 0.0069  0.0289  -0.0133 210  HIS A NE2 
2597 N  N   . THR A 211 ? 0.0716 0.0840 0.0601 0.0116  0.0104  0.0025  211  THR A N   
2598 C  CA  . THR A 211 ? 0.0707 0.0812 0.0736 0.0165  0.0142  -0.0035 211  THR A CA  
2599 C  C   . THR A 211 ? 0.0749 0.0874 0.0560 0.0082  0.0091  0.0075  211  THR A C   
2600 O  O   . THR A 211 ? 0.0709 0.0942 0.0777 0.0091  0.0143  0.0060  211  THR A O   
2601 C  CB  . THR A 211 ? 0.0993 0.0936 0.0840 0.0344  -0.0070 -0.0068 211  THR A CB  
2602 O  OG1 . THR A 211 ? 0.0939 0.0912 0.0764 0.0068  -0.0045 0.0076  211  THR A OG1 
2603 C  CG2 . THR A 211 ? 0.1300 0.0894 0.1054 0.0188  -0.0106 -0.0075 211  THR A CG2 
2609 N  N   . THR A 212 ? 0.0643 0.0728 0.0577 0.0090  0.0080  0.0065  212  THR A N   
2610 C  CA  . THR A 212 ? 0.0706 0.0715 0.0563 0.0039  0.0060  0.0035  212  THR A CA  
2611 C  C   . THR A 212 ? 0.0709 0.0820 0.0511 0.0080  0.0034  -0.0012 212  THR A C   
2612 O  O   . THR A 212 ? 0.0710 0.0990 0.0637 -0.0044 0.0043  0.0076  212  THR A O   
2613 C  CB  . THR A 212 ? 0.0686 0.0738 0.0527 -0.0001 0.0024  0.0056  212  THR A CB  
2614 O  OG1 . THR A 212 ? 0.0619 0.0733 0.0517 -0.0026 0.0020  0.0052  212  THR A OG1 
2615 C  CG2 . THR A 212 ? 0.0782 0.0843 0.0682 -0.0066 0.0147  -0.0092 212  THR A CG2 
2623 N  N   . VAL A 213 ? 0.0733 0.0865 0.0612 0.0018  0.0094  0.0113  213  VAL A N   
2624 C  CA  . VAL A 213 ? 0.0829 0.0955 0.0724 -0.0068 0.0102  0.0136  213  VAL A CA  
2625 C  C   . VAL A 213 ? 0.0750 0.1185 0.0713 -0.0013 0.0118  0.0298  213  VAL A C   
2626 O  O   . VAL A 213 ? 0.0813 0.1293 0.1054 -0.0097 0.0050  0.0298  213  VAL A O   
2627 C  CB  . VAL A 213 ? 0.0881 0.0998 0.0761 -0.0035 0.0104  0.0135  213  VAL A CB  
2628 C  CG1 . VAL A 213 ? 0.1187 0.1207 0.0959 -0.0128 0.0234  0.0322  213  VAL A CG1 
2629 C  CG2 . VAL A 213 ? 0.0987 0.0957 0.0703 0.0038  0.0069  0.0063  213  VAL A CG2 
2635 N  N   . ASN A 214 ? 0.0753 0.1288 0.0868 0.0040  0.0245  0.0167  214  ASN A N   
2636 C  CA  A ASN A 214 ? 0.0979 0.1525 0.1089 0.0207  0.0354  0.0211  214  ASN A CA  
2637 C  CA  B ASN A 214 ? 0.0744 0.1463 0.0983 -0.0025 0.0537  0.0225  214  ASN A CA  
2638 C  C   . ASN A 214 ? 0.0717 0.1450 0.1195 0.0087  0.0317  0.0247  214  ASN A C   
2639 O  O   . ASN A 214 ? 0.0779 0.1759 0.1555 0.0026  0.0352  0.0298  214  ASN A O   
2640 C  CB  A ASN A 214 ? 0.1379 0.2074 0.1360 0.0415  0.0308  -0.0411 214  ASN A CB  
2641 C  CB  B ASN A 214 ? 0.0827 0.1935 0.1749 0.0282  0.0227  -0.0437 214  ASN A CB  
2642 C  CG  A ASN A 214 ? 0.1690 0.2836 0.1511 0.0742  0.0514  -0.0392 214  ASN A CG  
2643 C  CG  B ASN A 214 ? 0.1714 0.2651 0.1678 0.0956  0.0375  -0.0707 214  ASN A CG  
2644 O  OD1 A ASN A 214 ? 0.3051 0.4072 0.2425 0.1032  0.1789  0.0309  214  ASN A OD1 
2645 O  OD1 B ASN A 214 ? 0.2433 0.2504 0.2444 0.0025  -0.0031 0.1151  214  ASN A OD1 
2646 N  ND2 A ASN A 214 ? 0.2670 0.2846 0.3870 0.1384  0.1259  -0.0280 214  ASN A ND2 
2647 N  ND2 B ASN A 214 ? 0.2278 0.4643 0.2440 0.1614  0.1316  -0.0403 214  ASN A ND2 
2649 N  N   . GLU A 215 ? 0.0795 0.1193 0.0984 0.0124  0.0196  0.0197  215  GLU A N   
2650 C  CA  . GLU A 215 ? 0.0654 0.1403 0.1256 0.0095  0.0047  0.0349  215  GLU A CA  
2651 C  C   . GLU A 215 ? 0.0645 0.1483 0.1199 -0.0049 -0.0010 0.0427  215  GLU A C   
2652 O  O   . GLU A 215 ? 0.1037 0.1860 0.2141 -0.0274 -0.0586 0.0640  215  GLU A O   
2653 C  CB  . GLU A 215 ? 0.0819 0.1144 0.1028 -0.0017 -0.0036 0.0214  215  GLU A CB  
2654 C  CG  . GLU A 215 ? 0.0887 0.1103 0.0904 0.0111  0.0011  0.0165  215  GLU A CG  
2655 C  CD  . GLU A 215 ? 0.0842 0.0845 0.0855 0.0194  0.0051  0.0009  215  GLU A CD  
2656 O  OE1 . GLU A 215 ? 0.0906 0.1002 0.0811 -0.0001 0.0008  -0.0064 215  GLU A OE1 
2657 O  OE2 . GLU A 215 ? 0.1013 0.0883 0.0914 0.0083  0.0019  -0.0043 215  GLU A OE2 
2660 N  N   . ASN A 216 ? 0.0847 0.1403 0.0835 -0.0017 0.0168  0.0226  216  ASN A N   
2661 C  CA  . ASN A 216 ? 0.0781 0.1423 0.0926 -0.0217 0.0051  0.0189  216  ASN A CA  
2662 C  C   . ASN A 216 ? 0.0840 0.1661 0.0971 -0.0205 0.0044  0.0309  216  ASN A C   
2663 O  O   . ASN A 216 ? 0.0996 0.2023 0.1186 -0.0467 -0.0020 0.0268  216  ASN A O   
2664 C  CB  . ASN A 216 ? 0.0930 0.1310 0.0998 -0.0076 0.0148  0.0225  216  ASN A CB  
2665 C  CG  . ASN A 216 ? 0.0777 0.1282 0.0737 -0.0168 0.0001  0.0011  216  ASN A CG  
2666 O  OD1 . ASN A 216 ? 0.1134 0.1786 0.0854 -0.0542 -0.0027 0.0057  216  ASN A OD1 
2667 N  ND2 . ASN A 216 ? 0.0781 0.1224 0.0699 -0.0119 0.0017  -0.0038 216  ASN A ND2 
2673 N  N   . ALA A 217 ? 0.0959 0.1873 0.1003 -0.0310 0.0138  0.0328  217  ALA A N   
2674 C  CA  . ALA A 217 ? 0.1039 0.2066 0.1095 -0.0495 0.0117  0.0469  217  ALA A CA  
2675 C  C   . ALA A 217 ? 0.0821 0.2639 0.1013 -0.0383 0.0110  0.0509  217  ALA A C   
2676 O  O   . ALA A 217 ? 0.1194 0.2724 0.1036 -0.0320 0.0182  0.0615  217  ALA A O   
2677 C  CB  . ALA A 217 ? 0.1297 0.2093 0.1406 -0.0341 0.0069  0.0720  217  ALA A CB  
2680 N  N   . PRO A 218 ? 0.1006 0.2612 0.1025 -0.0331 0.0056  0.0297  218  PRO A N   
2681 C  CA  . PRO A 218 ? 0.1040 0.3147 0.1224 -0.0240 0.0253  0.0092  218  PRO A CA  
2682 C  C   . PRO A 218 ? 0.1210 0.3808 0.1053 -0.0369 0.0162  0.0269  218  PRO A C   
2683 O  O   . PRO A 218 ? 0.1616 0.5076 0.1133 -0.0750 0.0317  0.0006  218  PRO A O   
2684 C  CB  . PRO A 218 ? 0.1177 0.3331 0.1585 0.0021  0.0274  0.0033  218  PRO A CB  
2685 C  CG  . PRO A 218 ? 0.1066 0.3027 0.1630 -0.0024 0.0147  0.0179  218  PRO A CG  
2686 C  CD  . PRO A 218 ? 0.0993 0.2591 0.1304 -0.0137 0.0130  0.0399  218  PRO A CD  
2687 N  N   . ASP A 219 ? 0.0863 0.3606 0.1239 -0.0260 0.0293  0.0564  219  ASP A N   
2688 C  CA  . ASP A 219 ? 0.1135 0.4319 0.1621 -0.0322 0.0477  0.0947  219  ASP A CA  
2689 C  C   . ASP A 219 ? 0.1487 0.3541 0.1365 -0.0727 0.0393  0.0576  219  ASP A C   
2690 O  O   . ASP A 219 ? 0.1834 0.4132 0.2160 -0.0580 0.0915  0.1140  219  ASP A O   
2691 C  CB  . ASP A 219 ? 0.1242 0.4618 0.2277 -0.0719 0.0435  0.0886  219  ASP A CB  
2692 C  CG  . ASP A 219 ? 0.1028 0.5739 0.2333 0.0036  0.0547  0.0772  219  ASP A CG  
2693 O  OD1 . ASP A 219 ? 0.2541 0.8949 0.2963 0.1713  -0.0181 0.0655  219  ASP A OD1 
2694 O  OD2 . ASP A 219 ? 0.2499 0.5802 0.3251 0.0203  0.0887  0.0114  219  ASP A OD2 
2696 N  N   . GLN A 220 ? 0.0982 0.3375 0.1235 -0.0721 -0.0017 0.0713  220  GLN A N   
2697 C  CA  . GLN A 220 ? 0.1347 0.3077 0.1060 -0.0776 -0.0101 0.0703  220  GLN A CA  
2698 C  C   . GLN A 220 ? 0.1120 0.2427 0.0872 -0.0386 0.0131  0.0350  220  GLN A C   
2699 O  O   . GLN A 220 ? 0.1292 0.2365 0.1142 -0.0314 0.0212  0.0166  220  GLN A O   
2700 C  CB  . GLN A 220 ? 0.1883 0.2722 0.1590 -0.1238 -0.0207 0.0537  220  GLN A CB  
2701 C  CG  . GLN A 220 ? 0.1850 0.3648 0.2278 -0.1582 0.0185  0.0210  220  GLN A CG  
2702 C  CD  . GLN A 220 ? 0.1706 0.4803 0.2574 -0.1552 -0.0251 0.0179  220  GLN A CD  
2703 O  OE1 . GLN A 220 ? 0.2289 0.4912 0.2068 -0.1251 -0.0491 0.0214  220  GLN A OE1 
2704 N  NE2 . GLN A 220 ? 0.1852 0.4454 0.4119 -0.0982 0.0228  -0.0306 220  GLN A NE2 
2706 N  N   A LYS A 221 ? 0.1065 0.2361 0.1194 -0.0233 0.0289  0.0382  221  LYS A N   
2707 N  N   B LYS A 221 ? 0.1006 0.2297 0.1095 -0.0161 -0.0032 0.0513  221  LYS A N   
2708 C  CA  A LYS A 221 ? 0.1035 0.2108 0.1548 -0.0226 0.0429  0.0297  221  LYS A CA  
2709 C  CA  B LYS A 221 ? 0.1129 0.2321 0.0829 -0.0234 0.0137  0.0123  221  LYS A CA  
2710 C  C   A LYS A 221 ? 0.1175 0.2396 0.1443 -0.0042 0.0158  0.0066  221  LYS A C   
2711 C  C   B LYS A 221 ? 0.0944 0.2269 0.0691 -0.0126 0.0142  -0.0250 221  LYS A C   
2712 O  O   A LYS A 221 ? 0.1201 0.1521 0.2613 0.0285  0.0292  -0.0088 221  LYS A O   
2713 O  O   B LYS A 221 ? 0.0902 0.2382 0.1248 -0.0084 0.0110  -0.0927 221  LYS A O   
2714 C  CB  A LYS A 221 ? 0.1326 0.2169 0.1890 -0.0137 0.0456  0.0109  221  LYS A CB  
2715 C  CB  B LYS A 221 ? 0.1356 0.2243 0.1252 -0.0151 0.0113  0.0151  221  LYS A CB  
2716 C  CG  A LYS A 221 ? 0.1772 0.2455 0.2118 -0.0235 0.0725  -0.0077 221  LYS A CG  
2717 C  CG  B LYS A 221 ? 0.1333 0.2355 0.1812 -0.0149 0.0116  -0.0221 221  LYS A CG  
2718 C  CD  A LYS A 221 ? 0.2130 0.2763 0.2272 -0.0445 0.0640  -0.0387 221  LYS A CD  
2719 C  CD  B LYS A 221 ? 0.2390 0.1919 0.2477 -0.0519 0.0284  0.0014  221  LYS A CD  
2720 C  CE  A LYS A 221 ? 0.2612 0.2357 0.2769 -0.0336 0.0950  -0.0337 221  LYS A CE  
2721 C  CE  B LYS A 221 ? 0.1972 0.2539 0.2595 0.0270  0.0553  -0.0050 221  LYS A CE  
2722 N  NZ  A LYS A 221 ? 0.0862 0.2842 0.1770 -0.0003 -0.0078 -0.0338 221  LYS A NZ  
2723 N  NZ  B LYS A 221 ? 0.3410 0.1982 0.3766 -0.0275 0.0386  -0.0896 221  LYS A NZ  
2724 N  N   A ASP A 222 ? 0.1436 0.1998 0.1464 0.0232  0.0233  0.0196  222  ASP A N   
2725 N  N   B ASP A 222 ? 0.1152 0.2403 0.0598 0.0362  0.0031  -0.0196 222  ASP A N   
2726 C  CA  A ASP A 222 ? 0.1118 0.2329 0.1246 0.0132  0.0184  -0.0023 222  ASP A CA  
2727 C  CA  B ASP A 222 ? 0.0846 0.2064 0.0780 0.0198  -0.0030 -0.0256 222  ASP A CA  
2728 C  C   A ASP A 222 ? 0.1229 0.2035 0.0790 -0.0123 0.0052  0.0512  222  ASP A C   
2729 C  C   B ASP A 222 ? 0.1539 0.2096 0.0964 0.0372  0.0360  -0.0236 222  ASP A C   
2730 O  O   A ASP A 222 ? 0.1191 0.2399 0.1631 -0.0181 -0.0054 0.1126  222  ASP A O   
2731 O  O   B ASP A 222 ? 0.1637 0.1872 0.1005 0.0166  -0.0080 -0.0437 222  ASP A O   
2732 C  CB  A ASP A 222 ? 0.1776 0.2744 0.1498 -0.0187 0.0568  0.0038  222  ASP A CB  
2733 C  CB  B ASP A 222 ? 0.1031 0.1299 0.0692 0.0015  0.0131  0.0087  222  ASP A CB  
2734 C  CG  A ASP A 222 ? 0.1834 0.3363 0.1764 -0.0136 0.0294  -0.1171 222  ASP A CG  
2735 C  CG  B ASP A 222 ? 0.0918 0.1339 0.0720 -0.0017 0.0119  0.0066  222  ASP A CG  
2736 O  OD1 A ASP A 222 ? 0.2968 0.3862 0.2510 -0.0656 -0.0191 -0.1840 222  ASP A OD1 
2737 O  OD1 B ASP A 222 ? 0.1013 0.1248 0.0812 -0.0056 0.0238  -0.0111 222  ASP A OD1 
2738 O  OD2 A ASP A 222 ? 0.1997 0.4477 0.2822 0.0454  0.0614  -0.0616 222  ASP A OD2 
2739 O  OD2 B ASP A 222 ? 0.1172 0.1298 0.0967 -0.0029 0.0288  -0.0180 222  ASP A OD2 
2740 N  N   . GLU A 223 ? 0.1076 0.2000 0.1007 -0.0056 0.0275  0.0071  223  GLU A N   
2741 C  CA  A GLU A 223 ? 0.0892 0.1822 0.1734 -0.0243 0.0254  0.0102  223  GLU A CA  
2742 C  CA  B GLU A 223 ? 0.1352 0.1831 0.1258 -0.0491 0.0576  -0.0329 223  GLU A CA  
2743 C  C   . GLU A 223 ? 0.1198 0.1365 0.1640 -0.0315 0.0511  -0.0243 223  GLU A C   
2744 O  O   . GLU A 223 ? 0.1551 0.1545 0.3009 -0.0594 0.1066  -0.0796 223  GLU A O   
2745 C  CB  A GLU A 223 ? 0.1467 0.1932 0.1819 -0.0508 0.0244  -0.0054 223  GLU A CB  
2746 C  CB  B GLU A 223 ? 0.1103 0.2119 0.0889 -0.0231 0.0272  0.0046  223  GLU A CB  
2747 C  CG  A GLU A 223 ? 0.1424 0.3134 0.2404 -0.0963 -0.0104 0.0482  223  GLU A CG  
2748 C  CG  B GLU A 223 ? 0.1116 0.2405 0.0869 -0.0043 0.0264  0.0118  223  GLU A CG  
2749 C  CD  A GLU A 223 ? 0.2582 0.3361 0.2523 -0.1779 0.0356  0.0333  223  GLU A CD  
2750 C  CD  B GLU A 223 ? 0.1261 0.3425 0.1714 0.0008  0.0418  0.1412  223  GLU A CD  
2751 O  OE1 A GLU A 223 ? 0.2464 0.6059 0.3773 -0.2499 -0.0252 0.0024  223  GLU A OE1 
2752 O  OE1 B GLU A 223 ? 0.1922 0.7334 0.1897 0.1600  0.1111  0.2179  223  GLU A OE1 
2753 O  OE2 A GLU A 223 ? 0.5679 0.5803 0.3550 -0.1946 0.1729  -0.1821 223  GLU A OE2 
2754 O  OE2 B GLU A 223 ? 0.1327 0.1938 0.0968 -0.0274 -0.0008 0.0004  223  GLU A OE2 
2757 N  N   . TYR A 224 ? 0.0929 0.1442 0.0708 -0.0118 0.0160  -0.0001 224  TYR A N   
2758 C  CA  . TYR A 224 ? 0.0985 0.1130 0.0774 -0.0114 0.0228  -0.0067 224  TYR A CA  
2759 C  C   . TYR A 224 ? 0.0989 0.1010 0.0609 0.0012  0.0185  0.0030  224  TYR A C   
2760 O  O   . TYR A 224 ? 0.1024 0.1351 0.0721 -0.0089 0.0205  -0.0060 224  TYR A O   
2761 C  CB  . TYR A 224 ? 0.1134 0.1332 0.0593 -0.0149 0.0105  -0.0041 224  TYR A CB  
2762 C  CG  . TYR A 224 ? 0.1119 0.1098 0.0725 -0.0174 0.0172  -0.0037 224  TYR A CG  
2763 C  CD1 . TYR A 224 ? 0.1080 0.1383 0.0854 -0.0327 0.0239  -0.0186 224  TYR A CD1 
2764 C  CD2 . TYR A 224 ? 0.1088 0.1172 0.0754 -0.0278 0.0233  -0.0131 224  TYR A CD2 
2765 C  CE1 . TYR A 224 ? 0.1262 0.1453 0.0788 -0.0321 0.0033  -0.0003 224  TYR A CE1 
2766 C  CE2 . TYR A 224 ? 0.1405 0.1108 0.0778 -0.0165 0.0088  -0.0066 224  TYR A CE2 
2767 C  CZ  . TYR A 224 ? 0.1457 0.1156 0.0896 -0.0313 -0.0004 -0.0075 224  TYR A CZ  
2768 O  OH  . TYR A 224 ? 0.1773 0.1334 0.1075 -0.0315 -0.0268 -0.0104 224  TYR A OH  
2775 N  N   . GLU A 225 ? 0.1006 0.0880 0.0678 -0.0010 0.0164  0.0066  225  GLU A N   
2776 C  CA  . GLU A 225 ? 0.1089 0.0817 0.0572 -0.0027 0.0184  0.0004  225  GLU A CA  
2777 C  C   . GLU A 225 ? 0.1071 0.0842 0.0470 0.0031  0.0119  0.0106  225  GLU A C   
2778 O  O   . GLU A 225 ? 0.1087 0.0902 0.0499 -0.0083 0.0113  0.0020  225  GLU A O   
2779 C  CB  . GLU A 225 ? 0.1153 0.0913 0.0563 -0.0032 0.0181  0.0074  225  GLU A CB  
2780 C  CG  . GLU A 225 ? 0.1333 0.0875 0.0589 0.0028  0.0092  0.0064  225  GLU A CG  
2781 C  CD  . GLU A 225 ? 0.1285 0.0832 0.0636 -0.0084 0.0191  0.0051  225  GLU A CD  
2782 O  OE1 . GLU A 225 ? 0.1691 0.0910 0.0630 -0.0090 0.0275  0.0092  225  GLU A OE1 
2783 O  OE2 . GLU A 225 ? 0.1581 0.0836 0.0844 0.0131  0.0302  0.0149  225  GLU A OE2 
2787 N  N   . LEU A 226 ? 0.1003 0.0873 0.0506 -0.0040 0.0167  0.0067  226  LEU A N   
2788 C  CA  . LEU A 226 ? 0.0962 0.0942 0.0532 0.0080  0.0100  0.0083  226  LEU A CA  
2789 C  C   . LEU A 226 ? 0.1005 0.0947 0.0535 0.0115  0.0094  0.0109  226  LEU A C   
2790 O  O   . LEU A 226 ? 0.1157 0.1132 0.0513 0.0238  0.0119  0.0159  226  LEU A O   
2791 C  CB  . LEU A 226 ? 0.0868 0.0859 0.0598 -0.0025 0.0041  0.0079  226  LEU A CB  
2792 C  CG  . LEU A 226 ? 0.0900 0.0859 0.0638 -0.0052 0.0169  0.0005  226  LEU A CG  
2793 C  CD1 . LEU A 226 ? 0.0863 0.0847 0.0951 0.0026  0.0138  0.0049  226  LEU A CD1 
2794 C  CD2 . LEU A 226 ? 0.0876 0.0915 0.0663 0.0017  0.0019  0.0191  226  LEU A CD2 
2803 N  N   . LEU A 227 ? 0.1060 0.0876 0.0523 0.0115  0.0070  0.0158  227  LEU A N   
2804 C  CA  . LEU A 227 ? 0.1056 0.1067 0.0669 0.0379  0.0174  0.0210  227  LEU A CA  
2805 C  C   . LEU A 227 ? 0.0906 0.1189 0.0736 0.0296  0.0056  0.0249  227  LEU A C   
2806 O  O   . LEU A 227 ? 0.0937 0.1353 0.0837 0.0134  0.0061  0.0371  227  LEU A O   
2807 C  CB  A LEU A 227 ? 0.1174 0.1341 0.0772 0.0253  0.0070  -0.0054 227  LEU A CB  
2808 C  CB  B LEU A 227 ? 0.1839 0.0765 0.0477 0.0669  0.0380  0.0577  227  LEU A CB  
2809 C  CG  A LEU A 227 ? 0.1600 0.1134 0.0632 0.0170  0.0293  0.0068  227  LEU A CG  
2810 C  CG  B LEU A 227 ? 0.0590 0.0683 0.0874 0.0202  -0.0469 0.0043  227  LEU A CG  
2811 C  CD1 A LEU A 227 ? 0.1150 0.1272 0.0781 0.0362  0.0141  -0.0005 227  LEU A CD1 
2812 C  CD1 B LEU A 227 ? 0.2741 0.0263 0.0410 -0.0069 -0.0067 -0.0130 227  LEU A CD1 
2813 C  CD2 A LEU A 227 ? 0.1389 0.1521 0.0900 -0.0027 0.0131  0.0241  227  LEU A CD2 
2814 C  CD2 B LEU A 227 ? 0.0694 0.0514 0.1006 0.0095  -0.0237 0.0070  227  LEU A CD2 
2819 N  N   . CYS A 228 ? 0.1014 0.1250 0.0741 0.0269  0.0064  0.0294  228  CYS A N   
2820 C  CA  . CYS A 228 ? 0.1019 0.1203 0.0960 0.0186  0.0046  0.0274  228  CYS A CA  
2821 C  C   . CYS A 228 ? 0.0926 0.1527 0.1015 0.0257  -0.0126 0.0348  228  CYS A C   
2822 O  O   . CYS A 228 ? 0.1127 0.1526 0.1066 0.0353  -0.0044 0.0265  228  CYS A O   
2823 C  CB  . CYS A 228 ? 0.1083 0.1449 0.0903 0.0197  -0.0053 0.0228  228  CYS A CB  
2824 S  SG  . CYS A 228 ? 0.1160 0.1190 0.0903 0.0215  0.0072  0.0247  228  CYS A SG  
2826 N  N   . LEU A 229 ? 0.0980 0.1572 0.1129 0.0188  -0.0071 0.0324  229  LEU A N   
2827 C  CA  . LEU A 229 ? 0.0801 0.2210 0.1128 0.0123  -0.0080 0.0445  229  LEU A CA  
2828 C  C   . LEU A 229 ? 0.1039 0.2228 0.1269 0.0234  -0.0141 0.0585  229  LEU A C   
2829 O  O   . LEU A 229 ? 0.0984 0.2669 0.1632 0.0395  -0.0154 0.0688  229  LEU A O   
2830 C  CB  . LEU A 229 ? 0.0996 0.2290 0.1560 0.0075  -0.0082 0.0910  229  LEU A CB  
2831 C  CG  . LEU A 229 ? 0.0945 0.3528 0.2164 -0.0073 -0.0364 0.1660  229  LEU A CG  
2832 C  CD1 . LEU A 229 ? 0.1306 0.3578 0.4240 0.0463  0.0535  0.2955  229  LEU A CD1 
2833 C  CD2 . LEU A 229 ? 0.1905 0.5176 0.1224 -0.0164 -0.0406 0.1257  229  LEU A CD2 
2836 N  N   . ASP A 230 ? 0.1353 0.1925 0.1114 0.0184  -0.0267 0.0344  230  ASP A N   
2837 C  CA  . ASP A 230 ? 0.1415 0.2087 0.1219 0.0196  -0.0399 0.0285  230  ASP A CA  
2838 C  C   . ASP A 230 ? 0.1318 0.2265 0.1160 0.0035  -0.0363 0.0559  230  ASP A C   
2839 O  O   . ASP A 230 ? 0.1930 0.2495 0.1382 0.0182  -0.0609 0.0645  230  ASP A O   
2840 C  CB  . ASP A 230 ? 0.2138 0.2805 0.1180 -0.0136 -0.0486 -0.0140 230  ASP A CB  
2841 C  CG  . ASP A 230 ? 0.2150 0.2421 0.1411 0.0446  -0.0155 -0.0312 230  ASP A CG  
2842 O  OD1 . ASP A 230 ? 0.1631 0.2348 0.1353 0.0384  -0.0093 0.0176  230  ASP A OD1 
2843 O  OD2 . ASP A 230 ? 0.3437 0.4440 0.1887 0.0320  0.0429  -0.1129 230  ASP A OD2 
2845 N  N   . GLY A 231 ? 0.1171 0.1908 0.1020 0.0301  -0.0085 0.0308  231  GLY A N   
2846 C  CA  . GLY A 231 ? 0.1133 0.1923 0.1317 0.0479  0.0019  0.0424  231  GLY A CA  
2847 C  C   . GLY A 231 ? 0.1292 0.1949 0.0879 0.0375  0.0073  0.0388  231  GLY A C   
2848 O  O   . GLY A 231 ? 0.1922 0.1968 0.1412 0.0316  0.0576  0.0373  231  GLY A O   
2849 N  N   . SER A 232 ? 0.1141 0.2028 0.0917 0.0467  0.0025  0.0431  232  SER A N   
2850 C  CA  . SER A 232 ? 0.1217 0.2021 0.0870 0.0327  0.0014  0.0440  232  SER A CA  
2851 C  C   . SER A 232 ? 0.1221 0.1260 0.0668 0.0339  0.0126  0.0324  232  SER A C   
2852 O  O   . SER A 232 ? 0.1289 0.1214 0.0767 0.0319  0.0071  0.0263  232  SER A O   
2853 C  CB  . SER A 232 ? 0.1348 0.2255 0.0728 0.0014  0.0031  0.0160  232  SER A CB  
2854 O  OG  . SER A 232 ? 0.1596 0.2150 0.0962 0.0287  -0.0107 0.0068  232  SER A OG  
2858 N  N   . ARG A 233 ? 0.1169 0.1273 0.0661 0.0316  0.0057  0.0285  233  ARG A N   
2859 C  CA  . ARG A 233 ? 0.1246 0.1039 0.0584 0.0185  0.0129  0.0264  233  ARG A CA  
2860 C  C   . ARG A 233 ? 0.0999 0.1115 0.0709 0.0159  0.0146  0.0303  233  ARG A C   
2861 O  O   . ARG A 233 ? 0.1086 0.1059 0.0577 0.0116  0.0088  0.0147  233  ARG A O   
2862 C  CB  . ARG A 233 ? 0.1268 0.1158 0.0754 0.0195  0.0206  0.0207  233  ARG A CB  
2863 C  CG  . ARG A 233 ? 0.1269 0.1131 0.0771 0.0128  0.0172  0.0118  233  ARG A CG  
2864 C  CD  . ARG A 233 ? 0.1360 0.1303 0.0812 0.0103  0.0109  0.0047  233  ARG A CD  
2865 N  NE  . ARG A 233 ? 0.1633 0.1214 0.0684 0.0116  -0.0029 0.0109  233  ARG A NE  
2866 C  CZ  . ARG A 233 ? 0.1441 0.1053 0.0845 0.0084  0.0187  0.0141  233  ARG A CZ  
2867 N  NH1 . ARG A 233 ? 0.1465 0.1143 0.0856 -0.0075 0.0208  0.0094  233  ARG A NH1 
2868 N  NH2 . ARG A 233 ? 0.1727 0.1312 0.0963 0.0064  0.0233  -0.0127 233  ARG A NH2 
2876 N  N   . GLN A 234 ? 0.1156 0.0970 0.0575 0.0127  0.0093  0.0139  234  GLN A N   
2877 C  CA  . GLN A 234 ? 0.0982 0.0963 0.0560 0.0053  0.0141  0.0102  234  GLN A CA  
2878 C  C   . GLN A 234 ? 0.1061 0.0832 0.0548 0.0046  0.0179  0.0107  234  GLN A C   
2879 O  O   . GLN A 234 ? 0.1034 0.0874 0.0518 0.0054  0.0126  0.0055  234  GLN A O   
2880 C  CB  A GLN A 234 ? 0.1152 0.0947 0.0436 0.0012  0.0151  0.0102  234  GLN A CB  
2881 C  CB  B GLN A 234 ? 0.1292 0.0916 0.1175 0.0054  -0.0338 0.0061  234  GLN A CB  
2882 C  CG  A GLN A 234 ? 0.1090 0.1163 0.0746 0.0101  0.0019  0.0160  234  GLN A CG  
2883 C  CG  B GLN A 234 ? 0.1903 0.1317 0.0404 -0.0290 -0.0120 0.0057  234  GLN A CG  
2884 C  CD  A GLN A 234 ? 0.1199 0.1280 0.0685 -0.0040 -0.0083 0.0066  234  GLN A CD  
2885 C  CD  B GLN A 234 ? 0.1715 0.1923 0.1199 0.0110  0.0347  0.0049  234  GLN A CD  
2886 O  OE1 A GLN A 234 ? 0.1302 0.1180 0.1001 -0.0047 0.0118  -0.0071 234  GLN A OE1 
2887 O  OE1 B GLN A 234 ? 0.1582 0.2313 0.2514 -0.0626 0.0412  -0.1348 234  GLN A OE1 
2888 N  NE2 A GLN A 234 ? 0.1324 0.1403 0.1905 -0.0090 -0.0451 0.0216  234  GLN A NE2 
2889 N  NE2 B GLN A 234 ? 0.3548 0.2811 0.3535 0.1116  0.2751  0.1526  234  GLN A NE2 
2894 N  N   . PRO A 235 ? 0.1040 0.0878 0.0553 0.0120  0.0158  0.0126  235  PRO A N   
2895 C  CA  . PRO A 235 ? 0.1039 0.1042 0.0678 0.0108  0.0260  0.0200  235  PRO A CA  
2896 C  C   . PRO A 235 ? 0.1025 0.0890 0.0481 0.0125  0.0151  0.0048  235  PRO A C   
2897 O  O   . PRO A 235 ? 0.1196 0.0914 0.0578 0.0065  0.0089  0.0129  235  PRO A O   
2898 C  CB  . PRO A 235 ? 0.0992 0.1374 0.0792 0.0187  0.0317  0.0143  235  PRO A CB  
2899 C  CG  . PRO A 235 ? 0.1166 0.1414 0.0738 0.0135  0.0296  -0.0003 235  PRO A CG  
2900 C  CD  . PRO A 235 ? 0.1238 0.1099 0.0600 0.0251  0.0272  0.0187  235  PRO A CD  
2904 N  N   . VAL A 236 ? 0.0978 0.0983 0.0673 0.0116  0.0153  0.0083  236  VAL A N   
2905 C  CA  . VAL A 236 ? 0.1062 0.1060 0.0630 0.0115  0.0141  0.0119  236  VAL A CA  
2906 C  C   . VAL A 236 ? 0.0914 0.1067 0.0605 0.0054  0.0152  0.0170  236  VAL A C   
2907 O  O   . VAL A 236 ? 0.1079 0.1096 0.0692 -0.0027 0.0190  0.0121  236  VAL A O   
2908 C  CB  . VAL A 236 ? 0.1408 0.1180 0.1011 -0.0012 -0.0294 0.0110  236  VAL A CB  
2909 C  CG1 . VAL A 236 ? 0.1892 0.1366 0.1234 -0.0139 -0.0455 0.0298  236  VAL A CG1 
2910 C  CG2 . VAL A 236 ? 0.1767 0.1233 0.1078 0.0018  -0.0423 -0.0012 236  VAL A CG2 
2916 N  N   . ASP A 237 ? 0.1023 0.0966 0.0688 0.0075  0.0181  0.0168  237  ASP A N   
2917 C  CA  . ASP A 237 ? 0.1071 0.1074 0.0839 0.0250  0.0151  0.0076  237  ASP A CA  
2918 C  C   . ASP A 237 ? 0.1153 0.0942 0.0766 0.0185  0.0188  0.0042  237  ASP A C   
2919 O  O   . ASP A 237 ? 0.1208 0.1084 0.1210 0.0177  0.0238  -0.0106 237  ASP A O   
2920 C  CB  . ASP A 237 ? 0.1190 0.1386 0.1337 0.0103  0.0359  -0.0168 237  ASP A CB  
2921 C  CG  . ASP A 237 ? 0.1242 0.1784 0.1390 0.0280  0.0307  0.0341  237  ASP A CG  
2922 O  OD1 . ASP A 237 ? 0.1422 0.1883 0.1519 0.0277  -0.0040 0.0254  237  ASP A OD1 
2923 O  OD2 . ASP A 237 ? 0.1249 0.2190 0.2409 0.0059  0.0640  0.0557  237  ASP A OD2 
2927 N  N   . ASN A 238 ? 0.1093 0.0999 0.0633 0.0092  0.0146  0.0031  238  ASN A N   
2928 C  CA  . ASN A 238 ? 0.1170 0.0953 0.0640 0.0090  0.0117  0.0030  238  ASN A CA  
2929 C  C   . ASN A 238 ? 0.1086 0.0888 0.0637 0.0096  0.0062  -0.0016 238  ASN A C   
2930 O  O   . ASN A 238 ? 0.1054 0.1016 0.0818 0.0047  -0.0025 0.0083  238  ASN A O   
2931 C  CB  . ASN A 238 ? 0.1312 0.1264 0.0671 0.0123  0.0081  0.0248  238  ASN A CB  
2932 C  CG  . ASN A 238 ? 0.1587 0.1231 0.0697 0.0120  0.0158  0.0005  238  ASN A CG  
2933 O  OD1 . ASN A 238 ? 0.1460 0.1650 0.0881 0.0047  0.0267  0.0063  238  ASN A OD1 
2934 N  ND2 . ASN A 238 ? 0.2050 0.1157 0.0713 -0.0046 -0.0115 0.0124  238  ASN A ND2 
2937 N  N   . TYR A 239 ? 0.1041 0.0825 0.0650 0.0096  0.0071  0.0001  239  TYR A N   
2938 C  CA  . TYR A 239 ? 0.1155 0.0882 0.0584 0.0038  0.0142  -0.0028 239  TYR A CA  
2939 C  C   . TYR A 239 ? 0.1180 0.0846 0.0669 0.0040  0.0165  0.0000  239  TYR A C   
2940 O  O   . TYR A 239 ? 0.1100 0.0977 0.0750 -0.0020 0.0093  -0.0034 239  TYR A O   
2941 C  CB  . TYR A 239 ? 0.1230 0.1139 0.0617 -0.0089 0.0160  0.0044  239  TYR A CB  
2942 C  CG  . TYR A 239 ? 0.1392 0.1118 0.0643 0.0012  -0.0065 0.0078  239  TYR A CG  
2943 C  CD1 . TYR A 239 ? 0.1822 0.1160 0.0766 -0.0167 -0.0276 0.0028  239  TYR A CD1 
2944 C  CD2 . TYR A 239 ? 0.1362 0.1691 0.0886 0.0169  0.0079  0.0372  239  TYR A CD2 
2945 C  CE1 . TYR A 239 ? 0.2486 0.1171 0.1634 0.0078  -0.0871 0.0143  239  TYR A CE1 
2946 C  CE2 . TYR A 239 ? 0.1584 0.2096 0.1376 0.0560  0.0219  0.0223  239  TYR A CE2 
2947 C  CZ  . TYR A 239 ? 0.2215 0.1718 0.2035 0.0693  -0.0702 -0.0203 239  TYR A CZ  
2948 O  OH  . TYR A 239 ? 0.3311 0.2240 0.3865 0.1450  -0.1020 0.0268  239  TYR A OH  
2953 N  N   . LYS A 240 ? 0.1167 0.0900 0.0753 0.0081  0.0063  -0.0080 240  LYS A N   
2954 C  CA  . LYS A 240 ? 0.1540 0.0876 0.0939 0.0039  -0.0084 -0.0143 240  LYS A CA  
2955 C  C   . LYS A 240 ? 0.1353 0.0942 0.0930 0.0013  0.0024  -0.0172 240  LYS A C   
2956 O  O   . LYS A 240 ? 0.1560 0.1031 0.1544 -0.0170 -0.0204 0.0036  240  LYS A O   
2957 C  CB  . LYS A 240 ? 0.1553 0.0908 0.1041 0.0117  0.0070  -0.0108 240  LYS A CB  
2958 C  CG  . LYS A 240 ? 0.1797 0.1008 0.1736 0.0235  -0.0396 -0.0190 240  LYS A CG  
2959 C  CD  . LYS A 240 ? 0.2723 0.1245 0.2104 0.0904  -0.0537 -0.0165 240  LYS A CD  
2960 C  CE  . LYS A 240 ? 0.2619 0.1317 0.2203 0.0683  -0.0735 -0.0139 240  LYS A CE  
2961 N  NZ  . LYS A 240 ? 0.3418 0.1700 0.2691 0.1372  -0.0345 0.0055  240  LYS A NZ  
2964 N  N   . THR A 241 ? 0.1293 0.0971 0.0813 -0.0015 0.0005  -0.0155 241  THR A N   
2965 C  CA  . THR A 241 ? 0.1590 0.1208 0.0720 0.0088  -0.0093 -0.0124 241  THR A CA  
2966 C  C   . THR A 241 ? 0.1030 0.1299 0.0628 0.0082  -0.0073 -0.0025 241  THR A C   
2967 O  O   . THR A 241 ? 0.1474 0.1349 0.0763 0.0234  -0.0205 0.0034  241  THR A O   
2968 C  CB  . THR A 241 ? 0.1564 0.1337 0.0794 0.0006  -0.0029 -0.0139 241  THR A CB  
2969 O  OG1 . THR A 241 ? 0.1599 0.1386 0.0876 -0.0075 0.0037  -0.0156 241  THR A OG1 
2970 C  CG2 . THR A 241 ? 0.2064 0.1384 0.0816 -0.0175 0.0219  -0.0253 241  THR A CG2 
2971 N  N   . CYS A 242 ? 0.1074 0.1088 0.0593 0.0125  -0.0019 0.0044  242  CYS A N   
2972 C  CA  . CYS A 242 ? 0.1017 0.0945 0.0673 0.0057  -0.0054 0.0059  242  CYS A CA  
2973 C  C   . CYS A 242 ? 0.0895 0.1032 0.0599 0.0114  0.0006  0.0004  242  CYS A C   
2974 O  O   . CYS A 242 ? 0.0937 0.1072 0.0697 -0.0032 -0.0061 0.0062  242  CYS A O   
2975 C  CB  . CYS A 242 ? 0.1222 0.0974 0.0715 0.0176  0.0117  0.0120  242  CYS A CB  
2976 S  SG  . CYS A 242 ? 0.1013 0.0997 0.0758 0.0112  0.0025  0.0069  242  CYS A SG  
2980 N  N   . ASN A 243 ? 0.0926 0.0994 0.0562 0.0041  -0.0058 0.0046  243  ASN A N   
2981 C  CA  . ASN A 243 ? 0.0844 0.0976 0.0619 0.0064  0.0001  0.0042  243  ASN A CA  
2982 C  C   . ASN A 243 ? 0.0810 0.0819 0.0643 0.0035  -0.0059 0.0043  243  ASN A C   
2983 O  O   . ASN A 243 ? 0.0922 0.1288 0.0699 0.0082  -0.0131 0.0114  243  ASN A O   
2984 C  CB  . ASN A 243 ? 0.0924 0.0903 0.0695 0.0098  0.0046  0.0141  243  ASN A CB  
2985 C  CG  . ASN A 243 ? 0.1063 0.0930 0.0827 0.0029  0.0072  -0.0032 243  ASN A CG  
2986 O  OD1 . ASN A 243 ? 0.1200 0.1008 0.1234 -0.0109 0.0329  -0.0029 243  ASN A OD1 
2987 N  ND2 . ASN A 243 ? 0.1367 0.0951 0.0947 -0.0067 0.0183  -0.0099 243  ASN A ND2 
2992 N  N   . TRP A 244 ? 0.0855 0.0945 0.0643 0.0093  -0.0010 0.0097  244  TRP A N   
2993 C  CA  . TRP A 244 ? 0.0794 0.1079 0.0684 0.0165  -0.0017 0.0106  244  TRP A CA  
2994 C  C   . TRP A 244 ? 0.0752 0.1078 0.0913 0.0066  -0.0027 0.0013  244  TRP A C   
2995 O  O   . TRP A 244 ? 0.0801 0.1037 0.1719 0.0074  0.0149  -0.0099 244  TRP A O   
2996 C  CB  . TRP A 244 ? 0.0926 0.1034 0.0694 0.0127  0.0068  0.0095  244  TRP A CB  
2997 C  CG  . TRP A 244 ? 0.1048 0.1009 0.0707 0.0061  0.0095  0.0078  244  TRP A CG  
2998 C  CD1 . TRP A 244 ? 0.0854 0.1020 0.0920 0.0099  0.0147  0.0075  244  TRP A CD1 
2999 C  CD2 . TRP A 244 ? 0.0965 0.0959 0.0628 0.0151  0.0008  0.0069  244  TRP A CD2 
3000 N  NE1 . TRP A 244 ? 0.0920 0.1000 0.0987 0.0056  0.0173  0.0138  244  TRP A NE1 
3001 C  CE2 . TRP A 244 ? 0.0831 0.0994 0.0791 0.0065  -0.0046 0.0097  244  TRP A CE2 
3002 C  CE3 . TRP A 244 ? 0.0853 0.1063 0.0770 0.0216  0.0044  0.0141  244  TRP A CE3 
3003 C  CZ2 . TRP A 244 ? 0.0912 0.1023 0.0842 0.0152  -0.0039 0.0080  244  TRP A CZ2 
3004 C  CZ3 . TRP A 244 ? 0.1105 0.1065 0.0785 0.0274  0.0056  0.0091  244  TRP A CZ3 
3005 C  CH2 . TRP A 244 ? 0.1135 0.1058 0.0774 0.0287  0.0006  0.0095  244  TRP A CH2 
3012 N  N   . ALA A 245 ? 0.0770 0.1021 0.0756 0.0011  -0.0052 0.0078  245  ALA A N   
3013 C  CA  . ALA A 245 ? 0.0827 0.0950 0.0719 -0.0053 -0.0055 -0.0032 245  ALA A CA  
3014 C  C   . ALA A 245 ? 0.0709 0.1020 0.0559 -0.0047 -0.0059 0.0035  245  ALA A C   
3015 O  O   . ALA A 245 ? 0.0797 0.1019 0.1016 -0.0091 -0.0131 0.0037  245  ALA A O   
3016 C  CB  . ALA A 245 ? 0.1163 0.1091 0.1033 -0.0027 0.0330  -0.0004 245  ALA A CB  
3019 N  N   . ARG A 246 ? 0.0713 0.1024 0.0791 -0.0058 -0.0153 0.0126  246  ARG A N   
3020 C  CA  . ARG A 246 ? 0.0728 0.1036 0.0723 -0.0044 -0.0153 0.0052  246  ARG A CA  
3021 C  C   . ARG A 246 ? 0.0820 0.1001 0.0725 0.0070  -0.0074 0.0067  246  ARG A C   
3022 O  O   . ARG A 246 ? 0.0809 0.2223 0.1251 -0.0077 -0.0076 0.0641  246  ARG A O   
3023 C  CB  A ARG A 246 ? 0.0906 0.1235 0.0884 -0.0102 0.0174  -0.0078 246  ARG A CB  
3024 C  CB  B ARG A 246 ? 0.1658 0.1667 0.0736 0.0795  -0.0442 -0.0267 246  ARG A CB  
3025 C  CG  A ARG A 246 ? 0.1637 0.2190 0.1083 0.0740  0.0099  -0.0379 246  ARG A CG  
3026 C  CG  B ARG A 246 ? 0.2250 0.2261 0.1283 0.1355  -0.0872 -0.0629 246  ARG A CG  
3027 C  CD  A ARG A 246 ? 0.2475 0.2676 0.1390 0.0976  0.0271  -0.0651 246  ARG A CD  
3028 C  CD  B ARG A 246 ? 0.2641 0.2688 0.1746 0.1570  -0.0777 -0.1028 246  ARG A CD  
3029 N  NE  A ARG A 246 ? 0.3977 0.2810 0.1832 0.0557  -0.0389 -0.0963 246  ARG A NE  
3030 N  NE  B ARG A 246 ? 0.2619 0.2647 0.1419 0.1602  -0.0731 -0.0709 246  ARG A NE  
3031 C  CZ  A ARG A 246 ? 0.3045 0.4257 0.2875 -0.0412 -0.0115 -0.0459 246  ARG A CZ  
3032 C  CZ  B ARG A 246 ? 0.2998 0.3098 0.1230 0.1924  -0.0189 0.0072  246  ARG A CZ  
3033 N  NH1 A ARG A 246 ? 0.3875 0.4228 0.2254 -0.0418 -0.0011 -0.0937 246  ARG A NH1 
3034 N  NH1 B ARG A 246 ? 0.2698 0.4984 0.2963 0.2468  0.0936  0.2044  246  ARG A NH1 
3035 N  NH2 A ARG A 246 ? 0.4045 0.2154 0.4495 -0.1163 -0.2096 0.0475  246  ARG A NH2 
3036 N  NH2 B ARG A 246 ? 0.6844 0.2427 0.1298 0.2629  -0.1023 -0.0435 246  ARG A NH2 
3043 N  N   A VAL A 247 ? 0.1105 0.0774 0.0665 0.0208  -0.0276 -0.0120 247  VAL A N   
3044 N  N   B VAL A 247 ? 0.0718 0.1371 0.0646 -0.0150 0.0087  0.0163  247  VAL A N   
3045 C  CA  A VAL A 247 ? 0.2122 0.1189 0.0678 0.0839  -0.0120 -0.0011 247  VAL A CA  
3046 C  CA  B VAL A 247 ? 0.0264 0.0810 0.0795 -0.0395 0.0106  0.0190  247  VAL A CA  
3047 C  C   A VAL A 247 ? 0.1154 0.1009 0.0587 0.0384  -0.0006 -0.0080 247  VAL A C   
3048 C  C   B VAL A 247 ? 0.0723 0.0688 0.0995 -0.0059 -0.0080 -0.0079 247  VAL A C   
3049 O  O   A VAL A 247 ? 0.1021 0.0611 0.0645 -0.0151 -0.0245 0.0036  247  VAL A O   
3050 O  O   B VAL A 247 ? 0.0968 0.1466 0.1163 0.0421  0.0215  0.0130  247  VAL A O   
3051 C  CB  A VAL A 247 ? 0.1083 0.1078 0.0920 0.0202  -0.0006 -0.0142 247  VAL A CB  
3052 C  CB  B VAL A 247 ? 0.0630 0.0845 0.0788 0.0121  0.0018  0.0182  247  VAL A CB  
3053 C  CG1 A VAL A 247 ? 0.0725 0.0686 0.3568 0.0047  -0.0346 0.0254  247  VAL A CG1 
3054 C  CG1 B VAL A 247 ? 0.0557 0.1147 0.1173 0.0185  -0.0055 0.0285  247  VAL A CG1 
3055 C  CG2 A VAL A 247 ? 0.1382 0.1423 0.0946 -0.0243 0.0114  -0.0096 247  VAL A CG2 
3056 C  CG2 B VAL A 247 ? 0.0715 0.0657 0.0609 -0.0037 -0.0486 0.0184  247  VAL A CG2 
3066 N  N   . ALA A 248 ? 0.0980 0.1047 0.0605 0.0327  -0.0058 -0.0018 248  ALA A N   
3067 C  CA  . ALA A 248 ? 0.0675 0.0827 0.0656 0.0139  -0.0087 -0.0059 248  ALA A CA  
3068 C  C   . ALA A 248 ? 0.0674 0.0588 0.0578 0.0024  -0.0061 0.0021  248  ALA A C   
3069 O  O   . ALA A 248 ? 0.0985 0.0608 0.0636 0.0114  0.0004  -0.0012 248  ALA A O   
3070 C  CB  . ALA A 248 ? 0.0615 0.1077 0.0923 -0.0052 -0.0006 0.0003  248  ALA A CB  
3074 N  N   . ALA A 249 ? 0.0714 0.0630 0.0553 -0.0013 -0.0054 -0.0065 249  ALA A N   
3075 C  CA  . ALA A 249 ? 0.0578 0.0631 0.0593 -0.0058 -0.0045 -0.0024 249  ALA A CA  
3076 C  C   . ALA A 249 ? 0.0483 0.0633 0.0510 0.0014  0.0005  0.0050  249  ALA A C   
3077 O  O   . ALA A 249 ? 0.0586 0.0701 0.0587 -0.0067 0.0045  0.0000  249  ALA A O   
3078 C  CB  . ALA A 249 ? 0.0590 0.0790 0.0632 0.0010  -0.0040 -0.0087 249  ALA A CB  
3084 N  N   . HIS A 250 ? 0.0666 0.0628 0.0525 -0.0038 0.0044  -0.0002 250  HIS A N   
3085 C  CA  . HIS A 250 ? 0.0649 0.0580 0.0444 -0.0002 -0.0004 -0.0029 250  HIS A CA  
3086 C  C   . HIS A 250 ? 0.0529 0.0671 0.0506 0.0049  -0.0009 -0.0079 250  HIS A C   
3087 O  O   . HIS A 250 ? 0.0719 0.0633 0.0638 0.0081  0.0122  -0.0002 250  HIS A O   
3088 C  CB  . HIS A 250 ? 0.0540 0.0620 0.0545 -0.0003 0.0011  0.0032  250  HIS A CB  
3089 C  CG  . HIS A 250 ? 0.0496 0.0585 0.0511 -0.0011 0.0023  0.0012  250  HIS A CG  
3090 N  ND1 . HIS A 250 ? 0.0612 0.0636 0.0599 -0.0008 -0.0083 -0.0017 250  HIS A ND1 
3091 C  CD2 . HIS A 250 ? 0.0547 0.0590 0.0529 -0.0051 -0.0012 0.0023  250  HIS A CD2 
3092 C  CE1 . HIS A 250 ? 0.0608 0.0583 0.0585 -0.0003 -0.0006 0.0013  250  HIS A CE1 
3093 N  NE2 . HIS A 250 ? 0.0560 0.0573 0.0602 -0.0020 0.0020  -0.0016 250  HIS A NE2 
3101 N  N   . ALA A 251 ? 0.0653 0.0566 0.0494 0.0102  0.0026  -0.0003 251  ALA A N   
3102 C  CA  . ALA A 251 ? 0.0665 0.0611 0.0518 0.0017  0.0031  -0.0047 251  ALA A CA  
3103 C  C   . ALA A 251 ? 0.0610 0.0612 0.0526 0.0008  0.0021  0.0038  251  ALA A C   
3104 O  O   . ALA A 251 ? 0.0712 0.0668 0.0541 0.0079  -0.0023 -0.0068 251  ALA A O   
3105 C  CB  . ALA A 251 ? 0.0848 0.0685 0.0679 -0.0074 -0.0110 0.0010  251  ALA A CB  
3109 N  N   . VAL A 252 ? 0.0771 0.0641 0.0492 0.0050  0.0017  0.0007  252  VAL A N   
3110 C  CA  . VAL A 252 ? 0.0605 0.0682 0.0458 0.0033  0.0022  0.0014  252  VAL A CA  
3111 C  C   . VAL A 252 ? 0.0663 0.0710 0.0536 0.0030  -0.0040 0.0049  252  VAL A C   
3112 O  O   . VAL A 252 ? 0.0770 0.0691 0.0739 -0.0044 0.0045  -0.0091 252  VAL A O   
3113 C  CB  . VAL A 252 ? 0.0717 0.0654 0.0651 0.0066  0.0036  0.0053  252  VAL A CB  
3114 C  CG1 . VAL A 252 ? 0.0810 0.0927 0.0671 0.0123  -0.0028 0.0074  252  VAL A CG1 
3115 C  CG2 . VAL A 252 ? 0.0616 0.1016 0.0663 0.0080  0.0008  0.0130  252  VAL A CG2 
3121 N  N   . VAL A 253 ? 0.0643 0.0678 0.0467 0.0000  0.0024  0.0041  253  VAL A N   
3122 C  CA  . VAL A 253 ? 0.0712 0.0747 0.0506 -0.0049 -0.0016 0.0052  253  VAL A CA  
3123 C  C   . VAL A 253 ? 0.0728 0.0706 0.0491 0.0054  0.0033  0.0034  253  VAL A C   
3124 O  O   . VAL A 253 ? 0.0767 0.0813 0.0567 -0.0061 -0.0067 0.0058  253  VAL A O   
3125 C  CB  . VAL A 253 ? 0.0652 0.0779 0.0552 -0.0019 0.0033  0.0074  253  VAL A CB  
3126 C  CG1 . VAL A 253 ? 0.0673 0.0984 0.0711 0.0122  -0.0060 0.0044  253  VAL A CG1 
3127 C  CG2 . VAL A 253 ? 0.0795 0.0801 0.0660 0.0027  0.0048  0.0006  253  VAL A CG2 
3133 N  N   . ALA A 254 ? 0.0657 0.0750 0.0570 -0.0007 0.0003  0.0124  254  ALA A N   
3134 C  CA  . ALA A 254 ? 0.0686 0.0777 0.0567 0.0026  0.0099  0.0097  254  ALA A CA  
3135 C  C   . ALA A 254 ? 0.0741 0.0789 0.0573 0.0031  0.0080  0.0058  254  ALA A C   
3136 O  O   . ALA A 254 ? 0.0688 0.0867 0.0641 -0.0018 0.0056  0.0077  254  ALA A O   
3137 C  CB  . ALA A 254 ? 0.0716 0.0824 0.0659 0.0061  0.0117  0.0125  254  ALA A CB  
3140 N  N   . ARG A 255 ? 0.0677 0.0810 0.0591 -0.0033 0.0077  0.0053  255  ARG A N   
3141 C  CA  . ARG A 255 ? 0.0831 0.0797 0.0597 -0.0156 0.0129  0.0046  255  ARG A CA  
3142 C  C   . ARG A 255 ? 0.0839 0.0793 0.0566 -0.0012 0.0051  0.0091  255  ARG A C   
3143 O  O   . ARG A 255 ? 0.0850 0.0804 0.0759 -0.0031 0.0067  0.0018  255  ARG A O   
3144 C  CB  . ARG A 255 ? 0.0938 0.0851 0.0624 -0.0208 0.0002  0.0088  255  ARG A CB  
3145 C  CG  . ARG A 255 ? 0.0838 0.0814 0.0628 -0.0069 0.0093  0.0059  255  ARG A CG  
3146 C  CD  . ARG A 255 ? 0.0855 0.0892 0.0637 -0.0075 0.0083  0.0020  255  ARG A CD  
3147 N  NE  . ARG A 255 ? 0.0927 0.0886 0.0709 -0.0128 0.0064  0.0132  255  ARG A NE  
3148 C  CZ  . ARG A 255 ? 0.0885 0.0862 0.0549 -0.0044 0.0129  0.0064  255  ARG A CZ  
3149 N  NH1 . ARG A 255 ? 0.0826 0.0936 0.0563 -0.0112 -0.0009 0.0101  255  ARG A NH1 
3150 N  NH2 . ARG A 255 ? 0.0974 0.0981 0.0723 0.0029  0.0052  0.0175  255  ARG A NH2 
3160 N  N   . ASP A 256 ? 0.0907 0.0818 0.0770 -0.0103 0.0029  0.0052  256  ASP A N   
3161 C  CA  . ASP A 256 ? 0.0962 0.0943 0.0824 -0.0129 -0.0059 -0.0041 256  ASP A CA  
3162 C  C   . ASP A 256 ? 0.0975 0.0800 0.0916 -0.0158 0.0084  -0.0013 256  ASP A C   
3163 O  O   . ASP A 256 ? 0.0985 0.1033 0.1265 -0.0018 0.0169  0.0175  256  ASP A O   
3164 C  CB  . ASP A 256 ? 0.0998 0.1164 0.1160 -0.0183 -0.0106 -0.0036 256  ASP A CB  
3165 C  CG  . ASP A 256 ? 0.1328 0.1244 0.1062 -0.0391 -0.0298 0.0046  256  ASP A CG  
3166 O  OD1 . ASP A 256 ? 0.1822 0.1189 0.1319 -0.0259 -0.0247 -0.0156 256  ASP A OD1 
3167 O  OD2 . ASP A 256 ? 0.1619 0.1718 0.1666 -0.0658 -0.0503 0.0059  256  ASP A OD2 
3170 N  N   . ASP A 257 ? 0.0981 0.0828 0.0924 -0.0096 0.0159  0.0099  257  ASP A N   
3171 C  CA  . ASP A 257 ? 0.0920 0.0771 0.1165 -0.0018 0.0133  0.0097  257  ASP A CA  
3172 C  C   . ASP A 257 ? 0.0949 0.0815 0.1316 -0.0038 0.0175  0.0105  257  ASP A C   
3173 O  O   . ASP A 257 ? 0.1061 0.1174 0.1264 0.0053  0.0275  0.0039  257  ASP A O   
3174 C  CB  . ASP A 257 ? 0.1129 0.0920 0.0971 -0.0123 0.0056  0.0171  257  ASP A CB  
3175 C  CG  . ASP A 257 ? 0.1014 0.0893 0.1098 -0.0104 0.0178  0.0125  257  ASP A CG  
3176 O  OD1 . ASP A 257 ? 0.1126 0.0986 0.1146 -0.0135 0.0211  -0.0018 257  ASP A OD1 
3177 O  OD2 . ASP A 257 ? 0.0948 0.0976 0.1072 -0.0047 0.0112  0.0181  257  ASP A OD2 
3180 N  N   . ASN A 258 ? 0.1003 0.0897 0.1797 -0.0002 -0.0042 0.0216  258  ASN A N   
3181 C  CA  A ASN A 258 ? 0.1092 0.0890 0.2471 0.0063  -0.0130 0.0101  258  ASN A CA  
3182 C  CA  B ASN A 258 ? 0.1088 0.0855 0.2736 0.0100  -0.0043 0.0066  258  ASN A CA  
3183 C  CA  C ASN A 258 ? 0.1156 0.0764 0.2644 0.0084  -0.0033 0.0176  258  ASN A CA  
3184 C  C   . ASN A 258 ? 0.0949 0.0951 0.1498 0.0144  -0.0121 0.0064  258  ASN A C   
3185 O  O   . ASN A 258 ? 0.1256 0.1211 0.1595 0.0256  -0.0008 -0.0034 258  ASN A O   
3186 C  CB  A ASN A 258 ? 0.1151 0.0875 0.2803 -0.0093 -0.0145 0.0343  258  ASN A CB  
3187 C  CB  B ASN A 258 ? 0.1388 0.0911 0.3315 0.0031  -0.0437 0.0255  258  ASN A CB  
3188 C  CB  C ASN A 258 ? 0.1174 0.1083 0.3244 -0.0078 -0.0285 0.0640  258  ASN A CB  
3189 C  CG  A ASN A 258 ? 0.1937 0.0949 0.2947 0.0296  0.0219  0.0515  258  ASN A CG  
3190 C  CG  B ASN A 258 ? 0.2619 0.1207 0.4994 -0.0727 -0.0849 -0.0062 258  ASN A CG  
3191 C  CG  C ASN A 258 ? 0.1923 0.1795 0.3149 0.0606  0.0381  0.1142  258  ASN A CG  
3192 O  OD1 A ASN A 258 ? 0.1014 0.1523 0.3076 0.0038  0.0786  0.0129  258  ASN A OD1 
3193 O  OD1 B ASN A 258 ? 0.3409 0.2512 0.6059 -0.1809 -0.2316 0.0819  258  ASN A OD1 
3194 O  OD1 C ASN A 258 ? 0.2570 0.5385 0.2843 0.2081  0.1489  0.3182  258  ASN A OD1 
3195 N  ND2 A ASN A 258 ? 0.1792 0.0214 0.4582 -0.0312 -0.0228 -0.0496 258  ASN A ND2 
3196 N  ND2 B ASN A 258 ? 0.3523 0.2516 0.4947 -0.2017 0.0318  -0.0824 258  ASN A ND2 
3197 N  ND2 C ASN A 258 ? 0.2335 0.2044 0.2615 0.1092  0.0303  0.0467  258  ASN A ND2 
3198 N  N   . LYS A 259 ? 0.1116 0.0932 0.1082 0.0001  0.0128  0.0104  259  LYS A N   
3199 C  CA  . LYS A 259 ? 0.0950 0.1018 0.0847 0.0075  -0.0047 0.0021  259  LYS A CA  
3200 C  C   . LYS A 259 ? 0.0846 0.0931 0.0849 0.0065  -0.0016 -0.0087 259  LYS A C   
3201 O  O   . LYS A 259 ? 0.0901 0.1032 0.0859 0.0005  -0.0020 0.0052  259  LYS A O   
3202 C  CB  . LYS A 259 ? 0.1066 0.1047 0.0858 0.0083  0.0001  -0.0008 259  LYS A CB  
3203 C  CG  . LYS A 259 ? 0.0970 0.1195 0.0731 0.0069  0.0044  0.0018  259  LYS A CG  
3204 C  CD  . LYS A 259 ? 0.1039 0.1145 0.0863 0.0007  0.0053  0.0196  259  LYS A CD  
3205 C  CE  . LYS A 259 ? 0.1011 0.1136 0.1130 0.0019  0.0077  0.0146  259  LYS A CE  
3206 N  NZ  . LYS A 259 ? 0.1036 0.1180 0.1095 0.0024  0.0068  0.0207  259  LYS A NZ  
3213 N  N   . VAL A 260 ? 0.0808 0.1114 0.0797 0.0043  0.0042  0.0024  260  VAL A N   
3214 C  CA  . VAL A 260 ? 0.0829 0.0977 0.0765 0.0023  0.0014  0.0034  260  VAL A CA  
3215 C  C   . VAL A 260 ? 0.0936 0.0870 0.0772 0.0030  0.0030  0.0022  260  VAL A C   
3216 O  O   . VAL A 260 ? 0.1004 0.0898 0.0976 -0.0030 0.0233  0.0097  260  VAL A O   
3217 C  CB  A VAL A 260 ? 0.0890 0.0840 0.0803 -0.0116 0.0066  0.0035  260  VAL A CB  
3218 C  CB  B VAL A 260 ? 0.0928 0.1056 0.0860 0.0079  -0.0006 -0.0050 260  VAL A CB  
3219 C  CG1 A VAL A 260 ? 0.0765 0.0988 0.0594 -0.0018 -0.0003 0.0218  260  VAL A CG1 
3220 C  CG1 B VAL A 260 ? 0.1087 0.0980 0.0911 -0.0049 -0.0081 -0.0059 260  VAL A CG1 
3221 C  CG2 A VAL A 260 ? 0.0894 0.0860 0.0823 -0.0069 -0.0025 0.0110  260  VAL A CG2 
3222 C  CG2 B VAL A 260 ? 0.0876 0.1496 0.1806 0.0166  0.0171  -0.0324 260  VAL A CG2 
3232 N  N   . GLU A 261 ? 0.0820 0.0906 0.1039 -0.0046 0.0125  0.0036  261  GLU A N   
3233 C  CA  . GLU A 261 ? 0.1012 0.0800 0.1036 0.0022  0.0100  0.0025  261  GLU A CA  
3234 C  C   . GLU A 261 ? 0.1015 0.0708 0.0840 0.0042  0.0077  0.0114  261  GLU A C   
3235 O  O   . GLU A 261 ? 0.1006 0.0889 0.0883 0.0042  0.0207  0.0110  261  GLU A O   
3236 C  CB  . GLU A 261 ? 0.1201 0.0706 0.2266 -0.0054 0.0143  0.0053  261  GLU A CB  
3237 C  CG  . GLU A 261 ? 0.1651 0.1197 0.2706 -0.0343 -0.0308 0.0195  261  GLU A CG  
3238 C  CD  . GLU A 261 ? 0.2394 0.1616 0.2774 -0.0411 -0.0705 0.0346  261  GLU A CD  
3239 O  OE1 . GLU A 261 ? 0.3187 0.3261 0.3776 0.0130  -0.1757 -0.0389 261  GLU A OE1 
3240 O  OE2 . GLU A 261 ? 0.3497 0.2457 0.2769 -0.0584 0.0019  -0.1033 261  GLU A OE2 
3242 N  N   . ASP A 262 ? 0.0898 0.0857 0.0824 0.0055  0.0134  0.0158  262  ASP A N   
3243 C  CA  . ASP A 262 ? 0.0912 0.0716 0.0821 0.0033  0.0083  0.0106  262  ASP A CA  
3244 C  C   . ASP A 262 ? 0.0953 0.0733 0.0625 0.0059  0.0109  0.0069  262  ASP A C   
3245 O  O   . ASP A 262 ? 0.0845 0.0852 0.0688 0.0009  0.0058  0.0118  262  ASP A O   
3246 C  CB  . ASP A 262 ? 0.0996 0.0879 0.0759 0.0006  0.0095  0.0157  262  ASP A CB  
3247 C  CG  . ASP A 262 ? 0.1128 0.0960 0.0851 0.0183  0.0110  0.0147  262  ASP A CG  
3248 O  OD1 . ASP A 262 ? 0.1340 0.0897 0.0991 0.0144  0.0075  0.0173  262  ASP A OD1 
3249 O  OD2 . ASP A 262 ? 0.1376 0.1039 0.0758 0.0043  0.0046  0.0142  262  ASP A OD2 
3254 N  N   . ILE A 263 ? 0.0825 0.0784 0.0619 0.0095  0.0061  0.0054  263  ILE A N   
3255 C  CA  . ILE A 263 ? 0.0825 0.0686 0.0659 0.0015  0.0006  0.0008  263  ILE A CA  
3256 C  C   . ILE A 263 ? 0.0793 0.0774 0.0543 0.0016  0.0048  0.0081  263  ILE A C   
3257 O  O   . ILE A 263 ? 0.0758 0.0770 0.0760 -0.0010 0.0122  0.0061  263  ILE A O   
3258 C  CB  . ILE A 263 ? 0.0794 0.0771 0.0623 0.0053  0.0014  0.0048  263  ILE A CB  
3259 C  CG1 . ILE A 263 ? 0.0830 0.0840 0.0727 0.0063  0.0060  -0.0053 263  ILE A CG1 
3260 C  CG2 . ILE A 263 ? 0.0862 0.0799 0.0804 0.0038  -0.0042 0.0100  263  ILE A CG2 
3261 C  CD1 . ILE A 263 ? 0.0813 0.1011 0.0800 0.0091  -0.0001 -0.0085 263  ILE A CD1 
3272 N  N   . TRP A 264 ? 0.0755 0.0846 0.0601 -0.0056 0.0080  0.0037  264  TRP A N   
3273 C  CA  . TRP A 264 ? 0.0875 0.0893 0.0536 -0.0100 0.0061  0.0050  264  TRP A CA  
3274 C  C   . TRP A 264 ? 0.0864 0.0927 0.0617 -0.0095 0.0099  -0.0042 264  TRP A C   
3275 O  O   . TRP A 264 ? 0.0948 0.1076 0.0680 -0.0143 0.0157  0.0008  264  TRP A O   
3276 C  CB  . TRP A 264 ? 0.0848 0.0889 0.0713 -0.0090 -0.0005 0.0029  264  TRP A CB  
3277 C  CG  . TRP A 264 ? 0.0990 0.0952 0.0647 -0.0157 0.0032  -0.0051 264  TRP A CG  
3278 C  CD1 . TRP A 264 ? 0.1335 0.1023 0.0796 -0.0131 0.0092  -0.0029 264  TRP A CD1 
3279 C  CD2 . TRP A 264 ? 0.0827 0.1101 0.0734 0.0019  0.0070  0.0030  264  TRP A CD2 
3280 N  NE1 . TRP A 264 ? 0.1266 0.1166 0.0833 0.0015  0.0144  -0.0176 264  TRP A NE1 
3281 C  CE2 . TRP A 264 ? 0.0959 0.1256 0.0688 0.0028  0.0055  -0.0012 264  TRP A CE2 
3282 C  CE3 . TRP A 264 ? 0.0986 0.1066 0.0851 0.0145  0.0139  0.0159  264  TRP A CE3 
3283 C  CZ2 . TRP A 264 ? 0.1025 0.1461 0.0771 0.0065  0.0122  0.0026  264  TRP A CZ2 
3284 C  CZ3 . TRP A 264 ? 0.1014 0.1239 0.1006 0.0220  0.0213  0.0307  264  TRP A CZ3 
3285 C  CH2 . TRP A 264 ? 0.1001 0.1451 0.0753 0.0098  -0.0061 0.0167  264  TRP A CH2 
3294 N  N   . SER A 265 ? 0.0862 0.0838 0.0794 -0.0019 0.0151  0.0007  265  SER A N   
3295 C  CA  . SER A 265 ? 0.0833 0.0831 0.1043 0.0018  0.0167  -0.0010 265  SER A CA  
3296 C  C   . SER A 265 ? 0.0880 0.0725 0.0849 0.0065  0.0104  0.0052  265  SER A C   
3297 O  O   . SER A 265 ? 0.0898 0.0921 0.0970 0.0021  0.0183  0.0013  265  SER A O   
3298 C  CB  A SER A 265 ? 0.0827 0.0793 0.1342 0.0094  0.0322  0.0203  265  SER A CB  
3299 C  CB  B SER A 265 ? 0.1116 0.0633 0.1423 -0.0163 -0.0235 0.0136  265  SER A CB  
3300 O  OG  A SER A 265 ? 0.1121 0.0767 0.1375 0.0030  0.0144  0.0069  265  SER A OG  
3301 O  OG  B SER A 265 ? 0.1570 0.1764 0.1229 0.0688  0.0214  0.0241  265  SER A OG  
3305 N  N   . PHE A 266 ? 0.0844 0.0831 0.0689 0.0007  0.0030  0.0111  266  PHE A N   
3306 C  CA  . PHE A 266 ? 0.0823 0.0900 0.0706 0.0000  0.0028  0.0051  266  PHE A CA  
3307 C  C   . PHE A 266 ? 0.0734 0.0846 0.0580 0.0000  0.0031  0.0024  266  PHE A C   
3308 O  O   . PHE A 266 ? 0.0759 0.0939 0.0728 0.0072  0.0040  0.0135  266  PHE A O   
3309 C  CB  . PHE A 266 ? 0.0814 0.0849 0.0636 0.0060  0.0041  0.0074  266  PHE A CB  
3310 C  CG  . PHE A 266 ? 0.0766 0.0967 0.0656 0.0040  0.0095  0.0018  266  PHE A CG  
3311 C  CD1 . PHE A 266 ? 0.0791 0.1171 0.0763 0.0141  -0.0026 -0.0158 266  PHE A CD1 
3312 C  CD2 . PHE A 266 ? 0.0972 0.0962 0.0811 0.0012  0.0050  0.0050  266  PHE A CD2 
3313 C  CE1 . PHE A 266 ? 0.0891 0.1219 0.1030 0.0070  -0.0054 -0.0382 266  PHE A CE1 
3314 C  CE2 . PHE A 266 ? 0.1076 0.0869 0.0994 -0.0048 0.0186  -0.0126 266  PHE A CE2 
3315 C  CZ  . PHE A 266 ? 0.0978 0.1199 0.1110 -0.0057 0.0242  -0.0312 266  PHE A CZ  
3320 N  N   . LEU A 267 ? 0.0739 0.0828 0.0658 0.0012  0.0020  0.0099  267  LEU A N   
3321 C  CA  . LEU A 267 ? 0.0757 0.0798 0.0659 -0.0034 0.0032  0.0083  267  LEU A CA  
3322 C  C   . LEU A 267 ? 0.0648 0.0821 0.0709 0.0079  0.0073  0.0111  267  LEU A C   
3323 O  O   . LEU A 267 ? 0.0734 0.0834 0.0700 0.0040  0.0032  0.0099  267  LEU A O   
3324 C  CB  . LEU A 267 ? 0.0732 0.0796 0.0707 0.0112  0.0061  0.0093  267  LEU A CB  
3325 C  CG  . LEU A 267 ? 0.0804 0.0857 0.0690 0.0077  0.0107  0.0151  267  LEU A CG  
3326 C  CD1 . LEU A 267 ? 0.0790 0.0935 0.0905 0.0148  0.0140  0.0083  267  LEU A CD1 
3327 C  CD2 . LEU A 267 ? 0.1002 0.0833 0.0893 0.0019  0.0151  0.0089  267  LEU A CD2 
3337 N  N   . SER A 268 ? 0.0644 0.0896 0.0706 -0.0020 0.0105  0.0048  268  SER A N   
3338 C  CA  A SER A 268 ? 0.0818 0.0913 0.0472 -0.0043 0.0041  0.0068  268  SER A CA  
3339 C  CA  B SER A 268 ? 0.0756 0.0830 0.0994 0.0309  0.0093  -0.0058 268  SER A CA  
3340 C  C   . SER A 268 ? 0.0807 0.0789 0.0702 0.0068  0.0080  -0.0039 268  SER A C   
3341 O  O   . SER A 268 ? 0.0808 0.1190 0.0811 0.0176  0.0146  0.0103  268  SER A O   
3342 C  CB  A SER A 268 ? 0.0992 0.0936 0.0789 -0.0124 0.0175  0.0041  268  SER A CB  
3343 C  CB  B SER A 268 ? 0.0773 0.1045 0.0961 0.0077  0.0065  -0.0158 268  SER A CB  
3344 O  OG  A SER A 268 ? 0.1790 0.1244 0.1429 -0.0094 0.0477  -0.0322 268  SER A OG  
3345 O  OG  B SER A 268 ? 0.1755 0.1094 0.0819 -0.0305 0.0343  -0.0079 268  SER A OG  
3352 N  N   . LYS A 269 ? 0.0778 0.0865 0.0794 0.0099  0.0089  0.0109  269  LYS A N   
3353 C  CA  A LYS A 269 ? 0.0862 0.0936 0.0965 0.0114  0.0015  -0.0014 269  LYS A CA  
3354 C  CA  B LYS A 269 ? 0.0915 0.0832 0.1342 0.0184  -0.0165 0.0325  269  LYS A CA  
3355 C  C   . LYS A 269 ? 0.0734 0.0932 0.0820 0.0108  -0.0021 0.0020  269  LYS A C   
3356 O  O   . LYS A 269 ? 0.0709 0.1105 0.1092 0.0162  0.0108  0.0087  269  LYS A O   
3357 C  CB  A LYS A 269 ? 0.0948 0.0975 0.1306 0.0148  -0.0237 0.0233  269  LYS A CB  
3358 C  CB  B LYS A 269 ? 0.1002 0.1304 0.1161 0.0001  -0.0161 0.0404  269  LYS A CB  
3359 C  CG  A LYS A 269 ? 0.0751 0.1493 0.1710 0.0442  0.0131  0.0514  269  LYS A CG  
3360 C  CG  B LYS A 269 ? 0.1001 0.0710 0.1817 0.0170  -0.0313 0.0437  269  LYS A CG  
3361 C  CD  A LYS A 269 ? 0.1271 0.1047 0.1907 0.0507  -0.0103 0.0252  269  LYS A CD  
3362 C  CD  B LYS A 269 ? 0.1330 0.1192 0.1425 0.0110  -0.0483 0.0245  269  LYS A CD  
3363 C  CE  A LYS A 269 ? 0.0893 0.1537 0.1446 0.0471  -0.0089 -0.0085 269  LYS A CE  
3364 C  CE  B LYS A 269 ? 0.1330 0.1257 0.1257 0.0384  -0.0699 0.0037  269  LYS A CE  
3365 N  NZ  A LYS A 269 ? 0.1201 0.0761 0.1290 0.0365  0.0226  0.0144  269  LYS A NZ  
3366 N  NZ  B LYS A 269 ? 0.1187 0.1421 0.2914 0.0273  -0.0420 -0.0402 269  LYS A NZ  
3371 N  N   . ALA A 270 ? 0.0731 0.0933 0.0807 0.0104  -0.0004 0.0031  270  ALA A N   
3372 C  CA  . ALA A 270 ? 0.0617 0.0917 0.0819 0.0008  -0.0009 0.0001  270  ALA A CA  
3373 C  C   . ALA A 270 ? 0.0617 0.0903 0.0787 0.0036  0.0113  -0.0028 270  ALA A C   
3374 O  O   . ALA A 270 ? 0.0667 0.1069 0.0758 -0.0024 0.0070  0.0025  270  ALA A O   
3375 C  CB  . ALA A 270 ? 0.0885 0.0952 0.0753 0.0068  0.0100  0.0013  270  ALA A CB  
3380 N  N   . GLN A 271 ? 0.0689 0.0884 0.0690 0.0034  0.0010  0.0023  271  GLN A N   
3381 C  CA  . GLN A 271 ? 0.0747 0.0750 0.0757 -0.0018 0.0039  0.0010  271  GLN A CA  
3382 C  C   . GLN A 271 ? 0.0620 0.1026 0.0796 -0.0045 0.0068  0.0041  271  GLN A C   
3383 O  O   . GLN A 271 ? 0.0895 0.1258 0.1005 -0.0015 0.0321  0.0034  271  GLN A O   
3384 C  CB  . GLN A 271 ? 0.0732 0.0832 0.0749 0.0062  -0.0061 0.0060  271  GLN A CB  
3385 C  CG  . GLN A 271 ? 0.0667 0.0775 0.0800 0.0016  -0.0005 0.0068  271  GLN A CG  
3386 C  CD  . GLN A 271 ? 0.0787 0.0896 0.0572 0.0073  -0.0033 0.0038  271  GLN A CD  
3387 O  OE1 . GLN A 271 ? 0.0848 0.1072 0.0935 0.0226  -0.0111 -0.0005 271  GLN A OE1 
3388 N  NE2 . GLN A 271 ? 0.0695 0.1048 0.0821 -0.0028 -0.0062 0.0010  271  GLN A NE2 
3393 N  N   . SER A 272 ? 0.0749 0.1000 0.0891 0.0065  0.0067  -0.0126 272  SER A N   
3394 C  CA  . SER A 272 ? 0.0858 0.1066 0.1049 0.0117  0.0062  -0.0233 272  SER A CA  
3395 C  C   . SER A 272 ? 0.0806 0.1127 0.0766 0.0242  0.0035  -0.0032 272  SER A C   
3396 O  O   . SER A 272 ? 0.0985 0.1943 0.0888 0.0082  0.0218  -0.0152 272  SER A O   
3397 C  CB  A SER A 272 ? 0.1625 0.0864 0.2198 0.0050  -0.0215 -0.0494 272  SER A CB  
3398 C  CB  B SER A 272 ? 0.0588 0.1216 0.1840 0.0290  0.0499  0.0073  272  SER A CB  
3399 C  CB  C SER A 272 ? 0.1236 0.1025 0.1454 0.0160  0.0088  -0.0289 272  SER A CB  
3400 O  OG  A SER A 272 ? 0.1289 0.1129 0.2634 -0.0267 0.0149  -0.0380 272  SER A OG  
3401 O  OG  B SER A 272 ? 0.1471 0.1129 0.1408 0.0387  0.0534  -0.0066 272  SER A OG  
3402 O  OG  C SER A 272 ? 0.1517 0.0946 0.1282 -0.0214 0.0327  -0.0091 272  SER A OG  
3405 N  N   . ASP A 273 ? 0.0766 0.0923 0.0846 0.0125  0.0042  -0.0003 273  ASP A N   
3406 C  CA  . ASP A 273 ? 0.0648 0.1127 0.0924 0.0150  0.0044  0.0046  273  ASP A CA  
3407 C  C   . ASP A 273 ? 0.0615 0.1117 0.0769 0.0081  0.0094  -0.0023 273  ASP A C   
3408 O  O   . ASP A 273 ? 0.0669 0.1174 0.1159 0.0059  0.0047  -0.0065 273  ASP A O   
3409 C  CB  . ASP A 273 ? 0.0799 0.1247 0.0890 0.0192  0.0058  0.0049  273  ASP A CB  
3410 C  CG  . ASP A 273 ? 0.1036 0.1314 0.0932 0.0407  0.0015  0.0133  273  ASP A CG  
3411 O  OD1 . ASP A 273 ? 0.3815 0.1614 0.1326 0.1427  0.0878  0.0314  273  ASP A OD1 
3412 O  OD2 . ASP A 273 ? 0.1259 0.1283 0.0987 0.0179  0.0049  0.0020  273  ASP A OD2 
3416 N  N   . PHE A 274 ? 0.0568 0.1020 0.0676 0.0003  0.0057  -0.0003 274  PHE A N   
3417 C  CA  . PHE A 274 ? 0.0574 0.1006 0.0634 -0.0014 0.0065  -0.0062 274  PHE A CA  
3418 C  C   . PHE A 274 ? 0.0736 0.0926 0.0637 0.0063  0.0134  -0.0026 274  PHE A C   
3419 O  O   . PHE A 274 ? 0.0903 0.1037 0.0718 0.0185  0.0013  -0.0045 274  PHE A O   
3420 C  CB  . PHE A 274 ? 0.0632 0.1048 0.0686 0.0076  0.0112  -0.0020 274  PHE A CB  
3421 C  CG  . PHE A 274 ? 0.0769 0.1108 0.0641 0.0033  0.0012  -0.0030 274  PHE A CG  
3422 C  CD1 . PHE A 274 ? 0.0778 0.1339 0.0770 0.0052  0.0020  0.0012  274  PHE A CD1 
3423 C  CD2 . PHE A 274 ? 0.0882 0.1145 0.0662 -0.0091 -0.0023 -0.0062 274  PHE A CD2 
3424 C  CE1 . PHE A 274 ? 0.1029 0.1434 0.0812 0.0092  -0.0149 -0.0058 274  PHE A CE1 
3425 C  CE2 . PHE A 274 ? 0.1220 0.1198 0.0649 0.0108  -0.0102 -0.0072 274  PHE A CE2 
3426 C  CZ  . PHE A 274 ? 0.1097 0.1401 0.0727 0.0074  -0.0217 -0.0076 274  PHE A CZ  
3434 N  N   . GLY A 275 ? 0.0731 0.0964 0.0719 0.0042  -0.0030 -0.0057 275  GLY A N   
3435 C  CA  . GLY A 275 ? 0.0777 0.0943 0.0637 0.0098  0.0039  -0.0033 275  GLY A CA  
3436 C  C   . GLY A 275 ? 0.0710 0.0947 0.0631 0.0099  -0.0041 -0.0083 275  GLY A C   
3437 O  O   . GLY A 275 ? 0.0723 0.1153 0.0749 0.0025  0.0011  -0.0116 275  GLY A O   
3441 N  N   . VAL A 276 ? 0.0814 0.1082 0.0620 0.0056  -0.0019 -0.0042 276  VAL A N   
3442 C  CA  . VAL A 276 ? 0.0814 0.0959 0.0795 0.0027  0.0017  0.0012  276  VAL A CA  
3443 C  C   . VAL A 276 ? 0.0902 0.1203 0.0587 0.0024  0.0122  -0.0064 276  VAL A C   
3444 O  O   . VAL A 276 ? 0.1060 0.1310 0.1135 -0.0031 0.0265  0.0130  276  VAL A O   
3445 C  CB  . VAL A 276 ? 0.1016 0.1106 0.0686 0.0005  0.0009  0.0092  276  VAL A CB  
3446 C  CG1 . VAL A 276 ? 0.1049 0.1101 0.0930 0.0178  -0.0015 0.0068  276  VAL A CG1 
3447 C  CG2 . VAL A 276 ? 0.1100 0.1423 0.0998 0.0126  -0.0184 -0.0166 276  VAL A CG2 
3455 N  N   . ASP A 277 ? 0.0827 0.1155 0.0548 0.0076  0.0106  -0.0095 277  ASP A N   
3456 C  CA  . ASP A 277 ? 0.0804 0.1160 0.0698 -0.0024 0.0113  -0.0143 277  ASP A CA  
3457 C  C   . ASP A 277 ? 0.0743 0.1321 0.0655 -0.0008 0.0014  -0.0091 277  ASP A C   
3458 O  O   . ASP A 277 ? 0.0840 0.1469 0.0840 0.0119  0.0041  -0.0182 277  ASP A O   
3459 C  CB  . ASP A 277 ? 0.0777 0.1146 0.0731 0.0016  0.0080  -0.0186 277  ASP A CB  
3460 C  CG  . ASP A 277 ? 0.0971 0.0956 0.0987 0.0189  0.0135  -0.0041 277  ASP A CG  
3461 O  OD1 . ASP A 277 ? 0.1117 0.1119 0.0791 0.0033  0.0164  0.0009  277  ASP A OD1 
3462 O  OD2 . ASP A 277 ? 0.2139 0.1149 0.2360 0.0214  0.1252  -0.0046 277  ASP A OD2 
3465 N  N   . THR A 278 ? 0.0817 0.1234 0.0673 -0.0052 0.0029  -0.0118 278  THR A N   
3466 C  CA  . THR A 278 ? 0.0596 0.1412 0.0693 0.0013  0.0062  -0.0157 278  THR A CA  
3467 C  C   . THR A 278 ? 0.0745 0.1264 0.0753 -0.0110 0.0111  -0.0167 278  THR A C   
3468 O  O   . THR A 278 ? 0.0770 0.1498 0.0928 -0.0159 0.0158  -0.0054 278  THR A O   
3469 C  CB  . THR A 278 ? 0.0668 0.1242 0.0672 -0.0043 0.0034  -0.0130 278  THR A CB  
3470 O  OG1 . THR A 278 ? 0.0685 0.1461 0.0654 -0.0119 0.0009  -0.0091 278  THR A OG1 
3471 C  CG2 . THR A 278 ? 0.0772 0.1184 0.0994 -0.0060 0.0041  -0.0153 278  THR A CG2 
3475 N  N   . LYS A 279 ? 0.0655 0.1384 0.0789 -0.0117 0.0042  -0.0226 279  LYS A N   
3476 C  CA  A LYS A 279 ? 0.0665 0.1295 0.0797 -0.0132 0.0164  -0.0134 279  LYS A CA  
3477 C  CA  B LYS A 279 ? 0.0587 0.1559 0.1291 0.0050  0.0132  -0.0649 279  LYS A CA  
3478 C  C   . LYS A 279 ? 0.0627 0.1287 0.0837 0.0095  -0.0013 -0.0204 279  LYS A C   
3479 O  O   . LYS A 279 ? 0.0568 0.1460 0.1016 0.0068  -0.0002 -0.0323 279  LYS A O   
3480 C  CB  A LYS A 279 ? 0.0605 0.1234 0.1035 -0.0056 0.0114  -0.0458 279  LYS A CB  
3481 C  CB  B LYS A 279 ? 0.0884 0.1992 0.1646 0.0455  0.0352  -0.0536 279  LYS A CB  
3482 C  CG  A LYS A 279 ? 0.1412 0.1147 0.1051 0.0452  -0.0278 -0.0328 279  LYS A CG  
3483 C  CG  B LYS A 279 ? 0.1677 0.1762 0.2333 0.0475  0.0526  -0.0173 279  LYS A CG  
3484 C  CD  A LYS A 279 ? 0.1353 0.1098 0.1566 0.0415  -0.0570 -0.0531 279  LYS A CD  
3485 C  CD  B LYS A 279 ? 0.1852 0.2333 0.2945 0.1104  -0.0007 -0.0328 279  LYS A CD  
3486 C  CE  A LYS A 279 ? 0.1781 0.1058 0.1992 0.0304  -0.0344 0.0056  279  LYS A CE  
3487 C  CE  B LYS A 279 ? 0.1877 0.2117 0.2895 0.0472  0.0136  0.0043  279  LYS A CE  
3488 N  NZ  A LYS A 279 ? 0.1364 0.1238 0.2113 0.0595  -0.0374 -0.0216 279  LYS A NZ  
3489 N  NZ  B LYS A 279 ? 0.0797 0.2008 0.4308 -0.0280 -0.0661 0.1057  279  LYS A NZ  
3491 N  N   . SER A 280 ? 0.0726 0.1241 0.0721 0.0067  0.0054  -0.0192 280  SER A N   
3492 C  CA  . SER A 280 ? 0.0664 0.1476 0.0800 0.0066  0.0000  -0.0288 280  SER A CA  
3493 C  C   . SER A 280 ? 0.0523 0.1411 0.0965 -0.0028 0.0097  -0.0278 280  SER A C   
3494 O  O   . SER A 280 ? 0.0873 0.1370 0.1028 0.0004  0.0009  -0.0125 280  SER A O   
3495 C  CB  . SER A 280 ? 0.0861 0.1347 0.0679 0.0063  0.0051  -0.0159 280  SER A CB  
3496 O  OG  . SER A 280 ? 0.0896 0.1533 0.0768 0.0145  0.0029  -0.0296 280  SER A OG  
3499 N  N   . ASP A 281 ? 0.0675 0.1329 0.1113 -0.0106 0.0067  -0.0310 281  ASP A N   
3500 C  CA  . ASP A 281 ? 0.0882 0.1218 0.1479 -0.0074 0.0061  -0.0290 281  ASP A CA  
3501 C  C   . ASP A 281 ? 0.0840 0.1283 0.1151 -0.0057 0.0089  -0.0214 281  ASP A C   
3502 O  O   . ASP A 281 ? 0.1027 0.1480 0.1736 -0.0006 0.0265  0.0064  281  ASP A O   
3503 C  CB  . ASP A 281 ? 0.0873 0.1657 0.2089 -0.0217 0.0096  -0.0793 281  ASP A CB  
3504 C  CG  . ASP A 281 ? 0.0797 0.2567 0.1682 -0.0042 -0.0097 -0.1053 281  ASP A CG  
3505 O  OD1 . ASP A 281 ? 0.1114 0.2663 0.1472 -0.0116 0.0025  -0.0692 281  ASP A OD1 
3506 O  OD2 . ASP A 281 ? 0.1381 0.3989 0.2231 0.0427  0.0032  -0.1628 281  ASP A OD2 
3509 N  N   . PHE A 282 ? 0.0686 0.1289 0.1019 0.0080  0.0060  -0.0244 282  PHE A N   
3510 C  CA  . PHE A 282 ? 0.0686 0.1198 0.0929 0.0120  0.0048  -0.0236 282  PHE A CA  
3511 C  C   . PHE A 282 ? 0.0727 0.1194 0.0711 0.0097  0.0098  -0.0096 282  PHE A C   
3512 O  O   . PHE A 282 ? 0.0872 0.1204 0.0865 0.0171  -0.0012 -0.0160 282  PHE A O   
3513 C  CB  . PHE A 282 ? 0.0698 0.1366 0.0774 0.0137  -0.0036 -0.0169 282  PHE A CB  
3514 C  CG  . PHE A 282 ? 0.0733 0.1412 0.0667 0.0232  0.0064  -0.0110 282  PHE A CG  
3515 C  CD1 . PHE A 282 ? 0.0959 0.1726 0.0610 0.0413  -0.0027 -0.0204 282  PHE A CD1 
3516 C  CD2 . PHE A 282 ? 0.0823 0.1307 0.0915 0.0090  0.0041  0.0056  282  PHE A CD2 
3517 C  CE1 . PHE A 282 ? 0.1040 0.1753 0.0757 0.0661  0.0095  0.0010  282  PHE A CE1 
3518 C  CE2 . PHE A 282 ? 0.0817 0.1548 0.0962 0.0106  0.0111  0.0344  282  PHE A CE2 
3519 C  CZ  . PHE A 282 ? 0.0842 0.1829 0.0902 0.0303  0.0271  0.0392  282  PHE A CZ  
3526 N  N   . HIS A 283 ? 0.0738 0.1065 0.0789 0.0062  0.0085  -0.0031 283  HIS A N   
3527 C  CA  A HIS A 283 ? 0.0713 0.1170 0.0750 0.0048  0.0056  -0.0022 283  HIS A CA  
3528 C  CA  B HIS A 283 ? 0.0698 0.1223 0.0793 0.0048  0.0055  -0.0041 283  HIS A CA  
3529 C  C   . HIS A 283 ? 0.0709 0.1041 0.0640 0.0107  0.0011  -0.0079 283  HIS A C   
3530 O  O   . HIS A 283 ? 0.0727 0.0998 0.0941 0.0045  0.0041  -0.0102 283  HIS A O   
3531 C  CB  A HIS A 283 ? 0.1160 0.1335 0.0769 0.0185  0.0287  0.0090  283  HIS A CB  
3532 C  CB  B HIS A 283 ? 0.0772 0.1301 0.0944 0.0117  0.0132  0.0098  283  HIS A CB  
3533 C  CG  A HIS A 283 ? 0.1183 0.1922 0.0969 -0.0020 0.0273  0.0336  283  HIS A CG  
3534 C  CG  B HIS A 283 ? 0.0991 0.1126 0.1014 0.0131  0.0223  0.0167  283  HIS A CG  
3535 N  ND1 A HIS A 283 ? 0.1298 0.2954 0.1179 -0.0325 0.0368  -0.0040 283  HIS A ND1 
3536 N  ND1 B HIS A 283 ? 0.1297 0.1383 0.1028 0.0370  0.0248  0.0007  283  HIS A ND1 
3537 C  CD2 A HIS A 283 ? 0.1025 0.1926 0.1205 0.0140  0.0486  0.0199  283  HIS A CD2 
3538 C  CD2 B HIS A 283 ? 0.0935 0.2407 0.1032 -0.0213 0.0447  0.0450  283  HIS A CD2 
3539 C  CE1 A HIS A 283 ? 0.1187 0.2911 0.1232 -0.0110 0.0268  0.0149  283  HIS A CE1 
3540 C  CE1 B HIS A 283 ? 0.1396 0.1489 0.1143 0.0241  0.0382  0.0059  283  HIS A CE1 
3541 N  NE2 A HIS A 283 ? 0.0867 0.2535 0.1475 0.0279  0.0155  0.0016  283  HIS A NE2 
3542 N  NE2 B HIS A 283 ? 0.1217 0.1672 0.1087 0.0150  0.0467  0.0324  283  HIS A NE2 
3549 N  N   . LEU A 284 ? 0.0770 0.1020 0.0541 0.0052  0.0027  0.0027  284  LEU A N   
3550 C  CA  . LEU A 284 ? 0.0834 0.0994 0.0541 -0.0016 0.0034  -0.0079 284  LEU A CA  
3551 C  C   . LEU A 284 ? 0.0713 0.0892 0.0626 -0.0075 0.0066  -0.0212 284  LEU A C   
3552 O  O   . LEU A 284 ? 0.0629 0.1058 0.0795 -0.0015 0.0048  -0.0214 284  LEU A O   
3553 C  CB  . LEU A 284 ? 0.0986 0.0966 0.0699 0.0046  0.0082  -0.0016 284  LEU A CB  
3554 C  CG  . LEU A 284 ? 0.1105 0.1146 0.0782 -0.0102 0.0023  0.0006  284  LEU A CG  
3555 C  CD1 . LEU A 284 ? 0.1629 0.1784 0.0732 -0.0621 0.0251  0.0020  284  LEU A CD1 
3556 C  CD2 . LEU A 284 ? 0.1225 0.1046 0.1112 -0.0076 -0.0038 0.0063  284  LEU A CD2 
3563 N  N   . PHE A 285 ? 0.0752 0.0902 0.0626 0.0016  0.0014  -0.0052 285  PHE A N   
3564 C  CA  . PHE A 285 ? 0.0730 0.0892 0.0765 0.0101  0.0014  -0.0098 285  PHE A CA  
3565 C  C   . PHE A 285 ? 0.0816 0.0972 0.0671 0.0150  -0.0068 -0.0055 285  PHE A C   
3566 O  O   . PHE A 285 ? 0.1073 0.1082 0.1045 0.0108  0.0247  -0.0067 285  PHE A O   
3567 C  CB  . PHE A 285 ? 0.0865 0.1063 0.0786 0.0024  -0.0134 -0.0008 285  PHE A CB  
3568 C  CG  . PHE A 285 ? 0.0811 0.1048 0.0714 0.0032  -0.0173 -0.0095 285  PHE A CG  
3569 C  CD1 . PHE A 285 ? 0.0845 0.1157 0.0810 -0.0001 -0.0064 -0.0173 285  PHE A CD1 
3570 C  CD2 . PHE A 285 ? 0.0903 0.1009 0.0662 0.0005  -0.0106 -0.0116 285  PHE A CD2 
3571 C  CE1 . PHE A 285 ? 0.0741 0.1280 0.0915 -0.0041 -0.0057 -0.0201 285  PHE A CE1 
3572 C  CE2 . PHE A 285 ? 0.0949 0.1039 0.0764 0.0062  -0.0067 -0.0160 285  PHE A CE2 
3573 C  CZ  . PHE A 285 ? 0.0901 0.1104 0.0865 -0.0117 -0.0128 -0.0133 285  PHE A CZ  
3579 N  N   . GLY A 286 ? 0.0802 0.0948 0.0794 0.0088  0.0063  0.0031  286  GLY A N   
3580 C  CA  . GLY A 286 ? 0.0934 0.1074 0.0913 0.0067  0.0113  0.0136  286  GLY A CA  
3581 C  C   . GLY A 286 ? 0.0861 0.1088 0.1176 0.0139  0.0255  0.0078  286  GLY A C   
3582 O  O   . GLY A 286 ? 0.0954 0.1307 0.1386 -0.0033 -0.0033 0.0258  286  GLY A O   
3585 N  N   . PRO A 287 ? 0.0954 0.1306 0.1527 0.0051  0.0357  0.0291  287  PRO A N   
3586 C  CA  . PRO A 287 ? 0.1398 0.1146 0.1274 0.0145  0.0556  0.0071  287  PRO A CA  
3587 C  C   . PRO A 287 ? 0.0918 0.1104 0.1102 -0.0094 0.0275  -0.0007 287  PRO A C   
3588 O  O   . PRO A 287 ? 0.1249 0.1010 0.1442 -0.0054 0.0069  -0.0063 287  PRO A O   
3589 C  CB  . PRO A 287 ? 0.1450 0.1889 0.2073 0.0350  0.0854  0.0203  287  PRO A CB  
3590 C  CG  . PRO A 287 ? 0.1288 0.4665 0.2260 -0.0267 0.0816  0.0278  287  PRO A CG  
3591 C  CD  . PRO A 287 ? 0.0908 0.1863 0.2272 -0.0027 0.0399  0.0790  287  PRO A CD  
3592 N  N   . PRO A 288 ? 0.0906 0.1219 0.1358 -0.0102 0.0157  -0.0072 288  PRO A N   
3593 C  CA  . PRO A 288 ? 0.0951 0.1476 0.1798 0.0022  -0.0232 -0.0100 288  PRO A CA  
3594 C  C   . PRO A 288 ? 0.1376 0.1321 0.1620 0.0226  0.0419  0.0323  288  PRO A C   
3595 O  O   . PRO A 288 ? 0.1528 0.1297 0.2602 0.0237  0.0886  0.0544  288  PRO A O   
3596 C  CB  . PRO A 288 ? 0.1568 0.2818 0.1997 0.0872  -0.0752 -0.0660 288  PRO A CB  
3597 C  CG  . PRO A 288 ? 0.2657 0.2283 0.2015 0.0382  -0.0843 -0.0579 288  PRO A CG  
3598 C  CD  . PRO A 288 ? 0.1415 0.1708 0.1579 -0.0195 0.0108  -0.0473 288  PRO A CD  
3599 N  N   . GLY A 289 ? 0.1583 0.1351 0.1862 0.0308  0.0452  0.0163  289  GLY A N   
3600 C  CA  . GLY A 289 ? 0.2560 0.1260 0.2485 0.0346  0.1263  0.0334  289  GLY A CA  
3601 C  C   . GLY A 289 ? 0.1357 0.1532 0.2088 0.0156  0.0446  0.0086  289  GLY A C   
3602 O  O   . GLY A 289 ? 0.1391 0.1547 0.1580 0.0229  -0.0006 -0.0080 289  GLY A O   
3603 N  N   . LYS A 290 ? 0.2110 0.1484 0.2280 -0.0030 0.0391  0.0039  290  LYS A N   
3604 C  CA  . LYS A 290 ? 0.1627 0.1583 0.2375 0.0076  0.0183  -0.0195 290  LYS A CA  
3605 C  C   . LYS A 290 ? 0.1466 0.2287 0.2771 0.0822  -0.0151 -0.0693 290  LYS A C   
3606 O  O   . LYS A 290 ? 0.1732 0.5168 0.3499 0.1709  -0.0510 -0.1081 290  LYS A O   
3607 C  CB  . LYS A 290 ? 0.1583 0.1896 0.3770 -0.0199 0.0283  0.0533  290  LYS A CB  
3608 C  CG  . LYS A 290 ? 0.1216 0.2123 0.3342 0.0036  0.0269  0.0687  290  LYS A CG  
3609 C  CD  . LYS A 290 ? 0.2126 0.2228 0.2950 0.0111  0.0417  0.0834  290  LYS A CD  
3610 C  CE  . LYS A 290 ? 0.3604 0.2236 0.4422 0.0835  0.2052  0.0966  290  LYS A CE  
3611 N  NZ  . LYS A 290 ? 0.3832 0.2305 0.6066 -0.0817 0.2555  0.0503  290  LYS A NZ  
3612 N  N   . LYS A 291 ? 0.1346 0.1457 0.2306 0.0047  -0.0041 -0.0127 291  LYS A N   
3613 C  CA  A LYS A 291 ? 0.1684 0.1900 0.2306 0.0299  -0.0238 -0.0082 291  LYS A CA  
3614 C  CA  B LYS A 291 ? 0.1661 0.1210 0.2279 0.0136  -0.0184 0.0089  291  LYS A CA  
3615 C  C   . LYS A 291 ? 0.1234 0.1180 0.1966 -0.0152 -0.0457 0.0056  291  LYS A C   
3616 O  O   . LYS A 291 ? 0.1489 0.1324 0.2161 -0.0152 -0.0587 0.0211  291  LYS A O   
3617 C  CB  A LYS A 291 ? 0.1693 0.2076 0.2542 0.0463  -0.0155 -0.0042 291  LYS A CB  
3618 C  CB  B LYS A 291 ? 0.1858 0.1327 0.2590 0.0243  0.0238  0.0459  291  LYS A CB  
3619 C  CG  A LYS A 291 ? 0.2460 0.1750 0.3459 0.0351  -0.0441 -0.0050 291  LYS A CG  
3620 C  CG  B LYS A 291 ? 0.2470 0.1158 0.2623 0.0055  -0.1584 0.0314  291  LYS A CG  
3621 C  CD  A LYS A 291 ? 0.2731 0.2014 0.3686 0.0546  0.0545  0.0287  291  LYS A CD  
3622 C  CD  B LYS A 291 ? 0.2944 0.1246 0.3242 0.0305  -0.1449 0.0428  291  LYS A CD  
3623 C  CE  A LYS A 291 ? 0.3366 0.1246 0.3936 0.0300  -0.0980 -0.0188 291  LYS A CE  
3624 C  CE  B LYS A 291 ? 0.3989 0.1018 0.4070 -0.0080 -0.2377 0.0175  291  LYS A CE  
3625 N  NZ  A LYS A 291 ? 0.3534 0.5588 0.3653 -0.1234 -0.1119 0.1648  291  LYS A NZ  
3626 N  NZ  B LYS A 291 ? 0.4775 0.0904 0.5968 -0.0023 -0.3891 -0.0299 291  LYS A NZ  
3627 N  N   . ASP A 292 ? 0.1272 0.1432 0.2269 -0.0083 -0.0359 -0.0246 292  ASP A N   
3628 C  CA  A ASP A 292 ? 0.1185 0.1173 0.2175 0.0023  -0.0599 -0.0275 292  ASP A CA  
3629 C  CA  B ASP A 292 ? 0.1257 0.1194 0.2416 -0.0056 -0.0499 -0.0585 292  ASP A CA  
3630 C  C   . ASP A 292 ? 0.1194 0.1176 0.1728 0.0058  -0.0436 -0.0156 292  ASP A C   
3631 O  O   . ASP A 292 ? 0.1287 0.1062 0.2416 0.0178  -0.0656 -0.0318 292  ASP A O   
3632 C  CB  A ASP A 292 ? 0.1934 0.1274 0.2197 0.0032  -0.0775 -0.0419 292  ASP A CB  
3633 C  CB  B ASP A 292 ? 0.0836 0.1922 0.2320 -0.0085 -0.0421 -0.0363 292  ASP A CB  
3634 C  CG  A ASP A 292 ? 0.2619 0.1583 0.2791 0.0249  -0.0551 -0.0826 292  ASP A CG  
3635 C  CG  B ASP A 292 ? 0.1427 0.1431 0.2340 -0.0036 -0.0698 -0.0677 292  ASP A CG  
3636 O  OD1 A ASP A 292 ? 0.2432 0.2423 0.2517 0.0917  -0.0524 -0.0255 292  ASP A OD1 
3637 O  OD1 B ASP A 292 ? 0.1224 0.0939 0.1588 -0.0464 0.0194  -0.0528 292  ASP A OD1 
3638 O  OD2 A ASP A 292 ? 0.2886 0.1385 0.4756 0.0277  -0.1146 -0.1042 292  ASP A OD2 
3639 O  OD2 B ASP A 292 ? 0.2365 0.2905 0.2790 -0.0211 -0.1207 -0.1398 292  ASP A OD2 
3640 N  N   . PRO A 293 ? 0.1136 0.1019 0.1762 -0.0104 -0.0498 -0.0004 293  PRO A N   
3641 C  CA  . PRO A 293 ? 0.1210 0.1172 0.1765 -0.0167 -0.0479 -0.0020 293  PRO A CA  
3642 C  C   . PRO A 293 ? 0.1111 0.0857 0.1652 -0.0019 -0.0278 -0.0267 293  PRO A C   
3643 O  O   . PRO A 293 ? 0.0974 0.0910 0.1852 -0.0095 -0.0196 -0.0400 293  PRO A O   
3644 C  CB  . PRO A 293 ? 0.1003 0.1917 0.2404 -0.0223 -0.0607 0.0534  293  PRO A CB  
3645 C  CG  . PRO A 293 ? 0.1120 0.1654 0.2378 0.0192  0.0214  0.0775  293  PRO A CG  
3646 C  CD  . PRO A 293 ? 0.1010 0.1158 0.1523 0.0065  -0.0092 0.0029  293  PRO A CD  
3649 N  N   . VAL A 294 ? 0.1361 0.0929 0.1862 0.0065  -0.0684 -0.0292 294  VAL A N   
3650 C  CA  A VAL A 294 ? 0.1726 0.0970 0.1655 0.0304  -0.0521 -0.0511 294  VAL A CA  
3651 C  CA  B VAL A 294 ? 0.1616 0.1107 0.1765 0.0357  -0.0529 -0.0342 294  VAL A CA  
3652 C  C   . VAL A 294 ? 0.1184 0.0905 0.1870 0.0076  -0.0469 -0.0320 294  VAL A C   
3653 O  O   . VAL A 294 ? 0.1230 0.1025 0.1880 0.0104  -0.0256 -0.0292 294  VAL A O   
3654 C  CB  A VAL A 294 ? 0.2570 0.1503 0.1859 0.0774  -0.1252 -0.0815 294  VAL A CB  
3655 C  CB  B VAL A 294 ? 0.1314 0.0993 0.1506 -0.0274 0.0063  -0.0169 294  VAL A CB  
3656 C  CG1 A VAL A 294 ? 0.3558 0.1452 0.1908 0.1108  -0.0584 -0.0706 294  VAL A CG1 
3657 C  CG1 B VAL A 294 ? 0.2959 0.1153 0.1270 -0.0563 0.0806  -0.0255 294  VAL A CG1 
3658 C  CG2 A VAL A 294 ? 0.2992 0.1630 0.3173 0.0104  -0.1731 -0.0806 294  VAL A CG2 
3659 C  CG2 B VAL A 294 ? 0.1142 0.1154 0.2522 -0.0230 0.0021  -0.0599 294  VAL A CG2 
3661 N  N   . LEU A 295 ? 0.1078 0.0805 0.1810 -0.0017 -0.0472 -0.0289 295  LEU A N   
3662 C  CA  . LEU A 295 ? 0.0917 0.0852 0.2053 -0.0047 -0.0357 -0.0183 295  LEU A CA  
3663 C  C   . LEU A 295 ? 0.0877 0.0735 0.1193 -0.0060 0.0089  0.0026  295  LEU A C   
3664 O  O   . LEU A 295 ? 0.0953 0.0803 0.1415 -0.0023 0.0084  0.0094  295  LEU A O   
3665 C  CB  . LEU A 295 ? 0.0908 0.1168 0.3263 -0.0121 -0.0338 -0.0095 295  LEU A CB  
3666 C  CG  . LEU A 295 ? 0.1375 0.1616 0.5160 -0.0456 -0.1522 -0.0179 295  LEU A CG  
3667 C  CD1 . LEU A 295 ? 0.1442 0.1568 0.6379 -0.0552 -0.1182 -0.0156 295  LEU A CD1 
3668 C  CD2 . LEU A 295 ? 0.2267 0.2723 0.4404 -0.0049 -0.1589 -0.1088 295  LEU A CD2 
3670 N  N   . LYS A 296 ? 0.0697 0.0831 0.1288 -0.0140 0.0109  -0.0153 296  LYS A N   
3671 C  CA  . LYS A 296 ? 0.0869 0.0699 0.1073 -0.0075 0.0170  0.0002  296  LYS A CA  
3672 C  C   . LYS A 296 ? 0.0682 0.0648 0.0784 -0.0021 -0.0002 0.0032  296  LYS A C   
3673 O  O   . LYS A 296 ? 0.0757 0.0784 0.0773 -0.0043 0.0067  -0.0122 296  LYS A O   
3674 C  CB  A LYS A 296 ? 0.1269 0.0712 0.0933 0.0008  0.0359  -0.0023 296  LYS A CB  
3675 C  CB  B LYS A 296 ? 0.1461 0.1422 0.1095 -0.0421 0.0103  0.0517  296  LYS A CB  
3676 C  CG  A LYS A 296 ? 0.0979 0.1022 0.1065 -0.0106 -0.0006 0.0208  296  LYS A CG  
3677 C  CG  B LYS A 296 ? 0.1962 0.0555 0.1320 -0.0389 0.0659  -0.0139 296  LYS A CG  
3678 C  CD  A LYS A 296 ? 0.0770 0.1956 0.1545 0.0169  0.0145  0.0862  296  LYS A CD  
3679 C  CD  B LYS A 296 ? 0.1122 0.1991 0.1735 0.0188  0.0239  0.0098  296  LYS A CD  
3680 C  CE  A LYS A 296 ? 0.1878 0.2686 0.1371 -0.0535 0.0653  0.0499  296  LYS A CE  
3681 C  CE  B LYS A 296 ? 0.1129 0.2198 0.1560 -0.0674 0.0434  -0.0336 296  LYS A CE  
3682 N  NZ  A LYS A 296 ? 0.2163 0.4349 0.1371 0.0602  0.0144  0.1142  296  LYS A NZ  
3683 N  NZ  B LYS A 296 ? 0.2282 0.1611 0.0979 -0.1065 0.0527  -0.0648 296  LYS A NZ  
3686 N  N   . ASP A 297 ? 0.0656 0.0684 0.0641 0.0049  0.0011  0.0030  297  ASP A N   
3687 C  CA  . ASP A 297 ? 0.0678 0.0676 0.0571 -0.0010 -0.0056 -0.0007 297  ASP A CA  
3688 C  C   . ASP A 297 ? 0.0626 0.0592 0.0575 -0.0006 -0.0070 -0.0016 297  ASP A C   
3689 O  O   . ASP A 297 ? 0.0700 0.0774 0.0548 -0.0045 -0.0055 0.0045  297  ASP A O   
3690 C  CB  . ASP A 297 ? 0.0666 0.0792 0.0498 0.0008  -0.0058 -0.0006 297  ASP A CB  
3691 C  CG  . ASP A 297 ? 0.0739 0.0600 0.0561 -0.0015 -0.0100 -0.0022 297  ASP A CG  
3692 O  OD1 . ASP A 297 ? 0.0840 0.0731 0.0568 0.0066  0.0054  0.0033  297  ASP A OD1 
3693 O  OD2 . ASP A 297 ? 0.0721 0.0795 0.0584 0.0120  0.0000  0.0074  297  ASP A OD2 
3698 N  N   . LEU A 298 ? 0.0679 0.0692 0.0608 -0.0036 -0.0061 0.0033  298  LEU A N   
3699 C  CA  . LEU A 298 ? 0.0629 0.0707 0.0502 0.0012  -0.0078 0.0011  298  LEU A CA  
3700 C  C   . LEU A 298 ? 0.0558 0.0701 0.0496 -0.0061 -0.0119 -0.0014 298  LEU A C   
3701 O  O   . LEU A 298 ? 0.0584 0.0708 0.0563 0.0006  -0.0051 0.0006  298  LEU A O   
3702 C  CB  . LEU A 298 ? 0.0677 0.0799 0.0570 -0.0097 -0.0143 0.0027  298  LEU A CB  
3703 C  CG  . LEU A 298 ? 0.0855 0.0811 0.0653 -0.0175 -0.0102 0.0029  298  LEU A CG  
3704 C  CD1 . LEU A 298 ? 0.0924 0.0997 0.0996 -0.0248 -0.0308 0.0071  298  LEU A CD1 
3705 C  CD2 . LEU A 298 ? 0.0992 0.0762 0.0853 -0.0141 -0.0084 0.0001  298  LEU A CD2 
3714 N  N   . LEU A 299 ? 0.0680 0.0704 0.0493 -0.0016 -0.0014 -0.0008 299  LEU A N   
3715 C  CA  . LEU A 299 ? 0.0656 0.0662 0.0559 -0.0070 -0.0018 0.0045  299  LEU A CA  
3716 C  C   . LEU A 299 ? 0.0644 0.0608 0.0490 -0.0002 -0.0020 0.0026  299  LEU A C   
3717 O  O   . LEU A 299 ? 0.0661 0.0908 0.0585 -0.0194 0.0032  -0.0032 299  LEU A O   
3718 C  CB  . LEU A 299 ? 0.0806 0.0679 0.0560 0.0003  -0.0089 0.0087  299  LEU A CB  
3719 C  CG  . LEU A 299 ? 0.0720 0.0978 0.0634 -0.0003 -0.0056 0.0081  299  LEU A CG  
3720 C  CD1 . LEU A 299 ? 0.0834 0.1056 0.0808 0.0033  -0.0077 0.0108  299  LEU A CD1 
3721 C  CD2 . LEU A 299 ? 0.0855 0.1198 0.0561 0.0013  -0.0141 -0.0026 299  LEU A CD2 
3731 N  N   . PHE A 300 ? 0.0606 0.0625 0.0515 -0.0006 -0.0030 -0.0009 300  PHE A N   
3732 C  CA  . PHE A 300 ? 0.0558 0.0632 0.0503 -0.0012 0.0012  0.0017  300  PHE A CA  
3733 C  C   . PHE A 300 ? 0.0577 0.0618 0.0535 -0.0021 -0.0015 -0.0018 300  PHE A C   
3734 O  O   . PHE A 300 ? 0.0677 0.0657 0.0592 -0.0078 -0.0060 0.0060  300  PHE A O   
3735 C  CB  . PHE A 300 ? 0.0714 0.0596 0.0562 -0.0019 0.0049  -0.0014 300  PHE A CB  
3736 C  CG  . PHE A 300 ? 0.0970 0.0566 0.0583 0.0039  0.0146  0.0005  300  PHE A CG  
3737 C  CD1 . PHE A 300 ? 0.1440 0.1039 0.0644 0.0541  0.0041  0.0045  300  PHE A CD1 
3738 C  CD2 . PHE A 300 ? 0.1142 0.0609 0.1169 -0.0098 0.0530  -0.0177 300  PHE A CD2 
3739 C  CE1 . PHE A 300 ? 0.2967 0.1196 0.0909 0.1009  0.0356  0.0338  300  PHE A CE1 
3740 C  CE2 . PHE A 300 ? 0.2488 0.0716 0.1544 -0.0250 0.1271  -0.0154 300  PHE A CE2 
3741 C  CZ  . PHE A 300 ? 0.3546 0.0793 0.1312 0.0633  0.1372  0.0415  300  PHE A CZ  
3747 N  N   . LYS A 301 ? 0.0673 0.0593 0.0494 -0.0101 -0.0018 0.0016  301  LYS A N   
3748 C  CA  . LYS A 301 ? 0.0708 0.0597 0.0465 0.0006  -0.0001 -0.0012 301  LYS A CA  
3749 C  C   . LYS A 301 ? 0.0664 0.0591 0.0517 -0.0010 -0.0058 0.0019  301  LYS A C   
3750 O  O   . LYS A 301 ? 0.0707 0.0691 0.0559 0.0077  0.0000  0.0032  301  LYS A O   
3751 C  CB  . LYS A 301 ? 0.0596 0.0664 0.0523 -0.0035 -0.0039 0.0025  301  LYS A CB  
3752 C  CG  . LYS A 301 ? 0.0667 0.0748 0.0568 0.0030  -0.0029 0.0035  301  LYS A CG  
3753 C  CD  . LYS A 301 ? 0.0625 0.0586 0.0649 0.0017  -0.0002 0.0021  301  LYS A CD  
3754 C  CE  . LYS A 301 ? 0.0597 0.0647 0.0643 0.0014  -0.0034 0.0004  301  LYS A CE  
3755 N  NZ  . LYS A 301 ? 0.0636 0.0763 0.0689 -0.0059 -0.0138 0.0074  301  LYS A NZ  
3768 N  N   . ASP A 302 ? 0.0561 0.0683 0.0544 0.0005  0.0000  0.0007  302  ASP A N   
3769 C  CA  . ASP A 302 ? 0.0654 0.0773 0.0597 -0.0007 0.0031  0.0012  302  ASP A CA  
3770 C  C   . ASP A 302 ? 0.0701 0.0778 0.0569 -0.0016 0.0100  0.0028  302  ASP A C   
3771 O  O   . ASP A 302 ? 0.0700 0.1008 0.0732 0.0020  0.0098  -0.0084 302  ASP A O   
3772 C  CB  . ASP A 302 ? 0.0659 0.0774 0.0645 -0.0103 0.0044  0.0007  302  ASP A CB  
3773 C  CG  . ASP A 302 ? 0.0621 0.0908 0.0656 0.0015  -0.0001 0.0016  302  ASP A CG  
3774 O  OD1 . ASP A 302 ? 0.0727 0.1029 0.0568 0.0039  0.0008  -0.0017 302  ASP A OD1 
3775 O  OD2 . ASP A 302 ? 0.1187 0.0886 0.1056 -0.0234 -0.0193 -0.0046 302  ASP A OD2 
3779 N  N   . SER A 303 ? 0.0634 0.0749 0.0547 0.0012  -0.0015 -0.0047 303  SER A N   
3780 C  CA  . SER A 303 ? 0.0810 0.0699 0.0522 -0.0048 0.0079  -0.0023 303  SER A CA  
3781 C  C   . SER A 303 ? 0.0562 0.0732 0.0544 0.0005  -0.0030 0.0000  303  SER A C   
3782 O  O   . SER A 303 ? 0.0760 0.0774 0.0580 -0.0017 0.0043  -0.0094 303  SER A O   
3783 C  CB  . SER A 303 ? 0.0872 0.0741 0.0499 0.0039  0.0030  0.0026  303  SER A CB  
3784 O  OG  . SER A 303 ? 0.0804 0.0737 0.0713 0.0062  -0.0017 -0.0015 303  SER A OG  
3789 N  N   . ALA A 304 ? 0.0600 0.0703 0.0555 0.0033  0.0019  -0.0046 304  ALA A N   
3790 C  CA  . ALA A 304 ? 0.0617 0.0659 0.0593 0.0041  -0.0015 -0.0033 304  ALA A CA  
3791 C  C   . ALA A 304 ? 0.0691 0.0629 0.0540 0.0029  0.0037  0.0078  304  ALA A C   
3792 O  O   . ALA A 304 ? 0.0586 0.0734 0.0744 -0.0023 -0.0040 -0.0058 304  ALA A O   
3793 C  CB  . ALA A 304 ? 0.0696 0.0653 0.0706 0.0063  0.0068  0.0009  304  ALA A CB  
3799 N  N   . ILE A 305 ? 0.0593 0.0600 0.0674 0.0038  0.0034  -0.0013 305  ILE A N   
3800 C  CA  . ILE A 305 ? 0.0601 0.0645 0.0712 0.0066  0.0068  -0.0047 305  ILE A CA  
3801 C  C   . ILE A 305 ? 0.0684 0.0697 0.0516 0.0056  0.0025  -0.0023 305  ILE A C   
3802 O  O   . ILE A 305 ? 0.0622 0.0720 0.0777 0.0101  0.0079  0.0025  305  ILE A O   
3803 C  CB  . ILE A 305 ? 0.0753 0.0724 0.0633 0.0077  0.0069  0.0007  305  ILE A CB  
3804 C  CG1 . ILE A 305 ? 0.0651 0.0781 0.0764 0.0089  0.0042  -0.0054 305  ILE A CG1 
3805 C  CG2 . ILE A 305 ? 0.0819 0.0770 0.0784 -0.0028 0.0110  0.0049  305  ILE A CG2 
3806 C  CD1 . ILE A 305 ? 0.1017 0.0990 0.0637 0.0263  -0.0024 -0.0083 305  ILE A CD1 
3816 N  N   . MET A 306 ? 0.0604 0.0643 0.0645 0.0034  0.0074  -0.0024 306  MET A N   
3817 C  CA  . MET A 306 ? 0.0669 0.0581 0.0629 0.0051  0.0016  0.0014  306  MET A CA  
3818 C  C   . MET A 306 ? 0.0620 0.0661 0.0536 -0.0003 -0.0029 -0.0060 306  MET A C   
3819 O  O   . MET A 306 ? 0.0607 0.0702 0.0667 0.0111  0.0059  0.0059  306  MET A O   
3820 C  CB  . MET A 306 ? 0.0627 0.0737 0.0617 0.0073  -0.0009 -0.0024 306  MET A CB  
3821 C  CG  . MET A 306 ? 0.0989 0.0590 0.0692 0.0059  0.0124  -0.0044 306  MET A CG  
3822 S  SD  . MET A 306 ? 0.0990 0.1174 0.0797 0.0428  0.0104  0.0052  306  MET A SD  
3823 C  CE  . MET A 306 ? 0.0979 0.1160 0.0944 0.0142  0.0163  -0.0155 306  MET A CE  
3831 N  N   . LEU A 307 ? 0.0511 0.0682 0.0641 0.0040  0.0036  0.0017  307  LEU A N   
3832 C  CA  . LEU A 307 ? 0.0515 0.0736 0.0647 0.0013  0.0106  -0.0018 307  LEU A CA  
3833 C  C   . LEU A 307 ? 0.0681 0.0637 0.0677 0.0035  0.0091  -0.0022 307  LEU A C   
3834 O  O   . LEU A 307 ? 0.0686 0.0670 0.1208 0.0047  0.0033  -0.0124 307  LEU A O   
3835 C  CB  . LEU A 307 ? 0.0716 0.0821 0.0684 -0.0058 0.0073  0.0018  307  LEU A CB  
3836 C  CG  . LEU A 307 ? 0.0891 0.0813 0.0586 -0.0031 0.0016  -0.0030 307  LEU A CG  
3837 C  CD1 . LEU A 307 ? 0.1808 0.1164 0.0750 0.0447  -0.0370 -0.0126 307  LEU A CD1 
3838 C  CD2 . LEU A 307 ? 0.2144 0.1053 0.1293 0.0670  -0.0907 -0.0536 307  LEU A CD2 
3848 N  N   . LYS A 308 ? 0.0635 0.0631 0.0768 -0.0029 0.0071  -0.0061 308  LYS A N   
3849 C  CA  . LYS A 308 ? 0.0737 0.0625 0.0793 -0.0025 0.0110  -0.0139 308  LYS A CA  
3850 C  C   . LYS A 308 ? 0.0695 0.0603 0.0693 0.0009  0.0097  -0.0162 308  LYS A C   
3851 O  O   . LYS A 308 ? 0.0820 0.0654 0.0965 0.0066  0.0264  -0.0090 308  LYS A O   
3852 C  CB  A LYS A 308 ? 0.1002 0.1204 0.0666 -0.0442 0.0171  -0.0140 308  LYS A CB  
3853 C  CB  B LYS A 308 ? 0.0675 0.0359 0.0744 0.0302  0.0139  -0.0117 308  LYS A CB  
3854 C  CG  A LYS A 308 ? 0.0883 0.0836 0.0740 0.0102  -0.0002 -0.0083 308  LYS A CG  
3855 C  CG  B LYS A 308 ? 0.0988 0.0993 0.0846 -0.0615 0.0463  -0.0341 308  LYS A CG  
3856 C  CD  A LYS A 308 ? 0.0938 0.0948 0.0670 -0.0152 -0.0004 -0.0059 308  LYS A CD  
3857 C  CD  B LYS A 308 ? 0.1016 0.1690 0.0793 -0.0148 -0.0082 -0.0433 308  LYS A CD  
3858 C  CE  A LYS A 308 ? 0.1092 0.1113 0.0729 -0.0068 -0.0063 -0.0179 308  LYS A CE  
3859 C  CE  B LYS A 308 ? 0.1212 0.1132 0.1169 -0.0164 0.0201  -0.0390 308  LYS A CE  
3860 N  NZ  A LYS A 308 ? 0.1094 0.1041 0.0781 0.0121  0.0027  -0.0148 308  LYS A NZ  
3861 N  NZ  B LYS A 308 ? 0.1079 0.0925 0.1842 0.0169  0.0404  -0.0057 308  LYS A NZ  
3872 N  N   . ARG A 309 ? 0.0636 0.0683 0.0881 0.0043  0.0114  -0.0043 309  ARG A N   
3873 C  CA  . ARG A 309 ? 0.0829 0.0695 0.0832 0.0031  0.0147  -0.0054 309  ARG A CA  
3874 C  C   . ARG A 309 ? 0.0751 0.0974 0.0823 -0.0201 0.0095  -0.0143 309  ARG A C   
3875 O  O   . ARG A 309 ? 0.1004 0.2100 0.0970 -0.0223 0.0090  -0.0493 309  ARG A O   
3876 C  CB  A ARG A 309 ? 0.0980 0.1020 0.2634 0.0117  0.0341  0.0773  309  ARG A CB  
3877 C  CB  B ARG A 309 ? 0.0951 0.0788 0.0910 -0.0151 0.0124  -0.0002 309  ARG A CB  
3878 C  CG  A ARG A 309 ? 0.2188 0.1562 0.1858 -0.0612 0.0283  0.0625  309  ARG A CG  
3879 C  CG  B ARG A 309 ? 0.1113 0.1227 0.1261 0.0307  0.0167  0.0494  309  ARG A CG  
3880 C  CD  A ARG A 309 ? 0.2930 0.2040 0.1895 -0.0053 -0.0460 0.0546  309  ARG A CD  
3881 C  CD  B ARG A 309 ? 0.1550 0.0836 0.1161 -0.0224 -0.0340 0.0304  309  ARG A CD  
3882 N  NE  A ARG A 309 ? 0.3620 0.1431 0.1160 -0.0874 -0.0400 0.0195  309  ARG A NE  
3883 N  NE  B ARG A 309 ? 0.1960 0.1702 0.1147 -0.0500 -0.0235 0.0649  309  ARG A NE  
3884 C  CZ  A ARG A 309 ? 0.3804 0.1351 0.1970 -0.0597 -0.0570 0.0310  309  ARG A CZ  
3885 C  CZ  B ARG A 309 ? 0.3222 0.1568 0.1132 -0.0954 -0.0877 0.0618  309  ARG A CZ  
3886 N  NH1 A ARG A 309 ? 0.5085 0.2483 0.3794 0.0957  -0.1868 -0.0273 309  ARG A NH1 
3887 N  NH1 B ARG A 309 ? 0.2237 0.1915 0.3843 -0.1063 -0.1472 0.1863  309  ARG A NH1 
3888 N  NH2 A ARG A 309 ? 0.4893 0.3436 0.1298 -0.1599 -0.0694 0.1314  309  ARG A NH2 
3889 N  NH2 B ARG A 309 ? 0.4807 0.2243 0.1045 -0.1890 -0.0375 0.0674  309  ARG A NH2 
3895 N  N   . VAL A 310 ? 0.0746 0.0949 0.0776 -0.0052 0.0076  -0.0098 310  VAL A N   
3896 C  CA  . VAL A 310 ? 0.0769 0.1048 0.0767 -0.0078 0.0011  0.0010  310  VAL A CA  
3897 C  C   . VAL A 310 ? 0.0687 0.1131 0.0721 -0.0121 0.0017  0.0035  310  VAL A C   
3898 O  O   . VAL A 310 ? 0.0870 0.1557 0.0734 -0.0366 -0.0122 0.0241  310  VAL A O   
3899 C  CB  . VAL A 310 ? 0.0829 0.1116 0.0861 0.0013  0.0053  -0.0093 310  VAL A CB  
3900 C  CG1 . VAL A 310 ? 0.0783 0.1098 0.0964 -0.0042 0.0033  -0.0163 310  VAL A CG1 
3901 C  CG2 . VAL A 310 ? 0.0805 0.1054 0.1322 -0.0060 0.0084  0.0010  310  VAL A CG2 
3910 N  N   . PRO A 311 ? 0.0836 0.1092 0.0720 -0.0058 -0.0058 -0.0038 311  PRO A N   
3911 C  CA  . PRO A 311 ? 0.0861 0.1056 0.0978 0.0040  -0.0100 -0.0147 311  PRO A CA  
3912 C  C   . PRO A 311 ? 0.0781 0.1033 0.0848 -0.0248 -0.0131 -0.0059 311  PRO A C   
3913 O  O   . PRO A 311 ? 0.0752 0.0986 0.1048 -0.0170 0.0105  -0.0058 311  PRO A O   
3914 C  CB  . PRO A 311 ? 0.1543 0.1648 0.0947 -0.0428 -0.0076 -0.0398 311  PRO A CB  
3915 C  CG  . PRO A 311 ? 0.2332 0.1873 0.0923 -0.0818 -0.0191 -0.0138 311  PRO A CG  
3916 C  CD  . PRO A 311 ? 0.1075 0.1413 0.0710 -0.0132 -0.0072 -0.0103 311  PRO A CD  
3920 N  N   . SER A 312 ? 0.1042 0.1048 0.1061 -0.0175 -0.0161 -0.0018 312  SER A N   
3921 C  CA  . SER A 312 ? 0.1441 0.1526 0.0924 -0.0583 -0.0145 0.0178  312  SER A CA  
3922 C  C   . SER A 312 ? 0.1466 0.1229 0.1172 -0.0457 0.0355  0.0096  312  SER A C   
3923 O  O   . SER A 312 ? 0.2046 0.2048 0.1158 -0.0436 0.0726  -0.0059 312  SER A O   
3924 C  CB  A SER A 312 ? 0.1950 0.1613 0.1336 -0.0639 -0.0293 0.0440  312  SER A CB  
3925 C  CB  B SER A 312 ? 0.1956 0.1539 0.1256 -0.0309 0.0040  0.0274  312  SER A CB  
3926 C  CB  C SER A 312 ? 0.2011 0.1444 0.1091 -0.0667 -0.0437 0.0201  312  SER A CB  
3927 O  OG  A SER A 312 ? 0.1961 0.1590 0.1940 -0.0552 -0.0138 0.0173  312  SER A OG  
3928 O  OG  B SER A 312 ? 0.2229 0.1198 0.1298 -0.0456 0.0188  0.0220  312  SER A OG  
3929 O  OG  C SER A 312 ? 0.2079 0.1216 0.1930 -0.0242 -0.0681 0.0103  312  SER A OG  
3932 N  N   . LEU A 313 ? 0.0882 0.1059 0.1650 -0.0140 0.0137  -0.0180 313  LEU A N   
3933 C  CA  . LEU A 313 ? 0.1027 0.0981 0.1898 -0.0246 0.0253  -0.0085 313  LEU A CA  
3934 C  C   . LEU A 313 ? 0.0911 0.1051 0.2485 -0.0022 0.0480  -0.0026 313  LEU A C   
3935 O  O   . LEU A 313 ? 0.0884 0.1162 0.5528 -0.0110 0.0821  0.0171  313  LEU A O   
3936 C  CB  . LEU A 313 ? 0.1242 0.1209 0.1657 -0.0325 -0.0200 0.0259  313  LEU A CB  
3937 C  CG  . LEU A 313 ? 0.1253 0.2470 0.1258 -0.0289 -0.0482 0.0033  313  LEU A CG  
3938 C  CD1 . LEU A 313 ? 0.2252 0.2056 0.1592 -0.0790 -0.0463 0.0338  313  LEU A CD1 
3939 C  CD2 . LEU A 313 ? 0.2008 0.2110 0.2234 0.0425  -0.0640 -0.0340 313  LEU A CD2 
3943 N  N   . MET A 314 ? 0.0647 0.0924 0.1470 -0.0078 0.0183  -0.0242 314  MET A N   
3944 C  CA  A MET A 314 ? 0.0871 0.0994 0.1461 -0.0086 0.0229  -0.0223 314  MET A CA  
3945 C  CA  B MET A 314 ? 0.0787 0.0982 0.1512 -0.0075 0.0224  -0.0206 314  MET A CA  
3946 C  C   . MET A 314 ? 0.0842 0.0914 0.1592 0.0015  -0.0203 -0.0287 314  MET A C   
3947 O  O   . MET A 314 ? 0.1248 0.1547 0.2616 0.0401  -0.0755 -0.0900 314  MET A O   
3948 C  CB  A MET A 314 ? 0.0974 0.1512 0.1494 -0.0282 -0.0013 0.0069  314  MET A CB  
3949 C  CB  B MET A 314 ? 0.0920 0.1509 0.1848 0.0034  0.0254  0.0425  314  MET A CB  
3950 C  CG  A MET A 314 ? 0.1251 0.2551 0.1622 -0.0278 0.0634  -0.0637 314  MET A CG  
3951 C  CG  B MET A 314 ? 0.0698 0.0957 0.1168 -0.0104 0.0009  -0.0284 314  MET A CG  
3952 S  SD  A MET A 314 ? 0.1088 0.3328 0.1130 -0.0307 0.0107  -0.0268 314  MET A SD  
3953 S  SD  B MET A 314 ? 0.0682 0.1198 0.1025 0.0059  -0.0040 -0.0115 314  MET A SD  
3954 C  CE  A MET A 314 ? 0.1235 0.2018 0.1628 0.0009  -0.0133 -0.0711 314  MET A CE  
3955 C  CE  B MET A 314 ? 0.1322 0.0878 0.1274 -0.0104 -0.0455 0.0223  314  MET A CE  
3961 N  N   . ASP A 315 ? 0.0838 0.0821 0.1155 -0.0031 -0.0014 -0.0137 315  ASP A N   
3962 C  CA  . ASP A 315 ? 0.0849 0.0806 0.0955 -0.0121 -0.0045 -0.0040 315  ASP A CA  
3963 C  C   . ASP A 315 ? 0.0602 0.0752 0.0837 -0.0068 -0.0054 -0.0069 315  ASP A C   
3964 O  O   . ASP A 315 ? 0.0684 0.0806 0.0862 -0.0025 0.0066  -0.0089 315  ASP A O   
3965 C  CB  . ASP A 315 ? 0.0883 0.0865 0.0952 -0.0126 0.0055  0.0059  315  ASP A CB  
3966 C  CG  . ASP A 315 ? 0.0819 0.0656 0.0918 -0.0098 0.0076  0.0015  315  ASP A CG  
3967 O  OD1 . ASP A 315 ? 0.0828 0.1025 0.1061 -0.0164 0.0180  -0.0045 315  ASP A OD1 
3968 O  OD2 . ASP A 315 ? 0.0848 0.0918 0.0899 -0.0160 0.0074  -0.0067 315  ASP A OD2 
3972 N  N   . SER A 316 ? 0.0598 0.0779 0.0817 -0.0034 0.0012  -0.0037 316  SER A N   
3973 C  CA  . SER A 316 ? 0.0632 0.0732 0.0716 -0.0079 -0.0051 -0.0071 316  SER A CA  
3974 C  C   . SER A 316 ? 0.0580 0.0746 0.0690 -0.0047 0.0065  -0.0139 316  SER A C   
3975 O  O   . SER A 316 ? 0.0582 0.0833 0.0730 -0.0129 0.0025  -0.0038 316  SER A O   
3976 C  CB  . SER A 316 ? 0.0664 0.0841 0.0749 -0.0115 -0.0013 -0.0111 316  SER A CB  
3977 O  OG  . SER A 316 ? 0.0739 0.0866 0.0846 -0.0057 0.0115  -0.0173 316  SER A OG  
3982 N  N   . GLN A 317 ? 0.0553 0.0758 0.0733 -0.0084 0.0004  -0.0051 317  GLN A N   
3983 C  CA  . GLN A 317 ? 0.0506 0.0685 0.0751 -0.0023 0.0000  -0.0039 317  GLN A CA  
3984 C  C   . GLN A 317 ? 0.0501 0.0818 0.0777 -0.0147 0.0038  -0.0123 317  GLN A C   
3985 O  O   . GLN A 317 ? 0.0616 0.0974 0.0786 -0.0087 0.0034  -0.0068 317  GLN A O   
3986 C  CB  . GLN A 317 ? 0.0553 0.0797 0.0787 -0.0031 -0.0004 -0.0103 317  GLN A CB  
3987 C  CG  . GLN A 317 ? 0.0509 0.1084 0.0801 -0.0068 0.0042  -0.0072 317  GLN A CG  
3988 C  CD  . GLN A 317 ? 0.0521 0.0944 0.0979 -0.0111 -0.0021 -0.0075 317  GLN A CD  
3989 O  OE1 . GLN A 317 ? 0.0590 0.1158 0.1140 -0.0147 0.0108  0.0026  317  GLN A OE1 
3990 N  NE2 . GLN A 317 ? 0.0614 0.1060 0.0973 0.0041  0.0036  -0.0210 317  GLN A NE2 
3997 N  N   . LEU A 318 ? 0.0540 0.0822 0.0874 -0.0084 0.0001  -0.0176 318  LEU A N   
3998 C  CA  . LEU A 318 ? 0.0617 0.0925 0.0762 -0.0107 -0.0026 -0.0185 318  LEU A CA  
3999 C  C   . LEU A 318 ? 0.0575 0.0871 0.0833 -0.0058 -0.0012 -0.0234 318  LEU A C   
4000 O  O   . LEU A 318 ? 0.0693 0.1149 0.0763 -0.0182 0.0017  -0.0289 318  LEU A O   
4001 C  CB  . LEU A 318 ? 0.0664 0.0815 0.1467 -0.0228 0.0179  -0.0359 318  LEU A CB  
4002 C  CG  . LEU A 318 ? 0.0594 0.1077 0.1173 -0.0314 0.0225  -0.0438 318  LEU A CG  
4003 C  CD1 . LEU A 318 ? 0.0807 0.0824 0.2981 -0.0181 0.0498  -0.0231 318  LEU A CD1 
4004 C  CD2 . LEU A 318 ? 0.1404 0.3095 0.1187 -0.1381 0.0161  -0.0723 318  LEU A CD2 
4007 N  N   . TYR A 319 ? 0.0530 0.0902 0.0715 -0.0105 0.0065  -0.0142 319  TYR A N   
4008 C  CA  . TYR A 319 ? 0.0552 0.0838 0.0702 -0.0141 0.0029  -0.0209 319  TYR A CA  
4009 C  C   . TYR A 319 ? 0.0564 0.0856 0.0646 -0.0139 0.0008  -0.0131 319  TYR A C   
4010 O  O   . TYR A 319 ? 0.0656 0.1095 0.0707 -0.0060 0.0049  -0.0060 319  TYR A O   
4011 C  CB  . TYR A 319 ? 0.0589 0.0979 0.0677 -0.0179 0.0070  -0.0069 319  TYR A CB  
4012 C  CG  . TYR A 319 ? 0.0542 0.0820 0.0605 -0.0130 -0.0023 -0.0022 319  TYR A CG  
4013 C  CD1 . TYR A 319 ? 0.0629 0.0734 0.0810 -0.0114 0.0012  -0.0059 319  TYR A CD1 
4014 C  CD2 . TYR A 319 ? 0.0605 0.0804 0.0680 -0.0075 0.0065  -0.0137 319  TYR A CD2 
4015 C  CE1 . TYR A 319 ? 0.0590 0.0750 0.0763 -0.0097 0.0032  -0.0077 319  TYR A CE1 
4016 C  CE2 . TYR A 319 ? 0.0584 0.0738 0.0681 -0.0076 0.0032  -0.0124 319  TYR A CE2 
4017 C  CZ  . TYR A 319 ? 0.0530 0.0713 0.0628 -0.0057 0.0073  -0.0011 319  TYR A CZ  
4018 O  OH  . TYR A 319 ? 0.0660 0.0744 0.0925 -0.0096 0.0272  -0.0080 319  TYR A OH  
4027 N  N   . LEU A 320 ? 0.0720 0.0839 0.0660 -0.0095 0.0075  -0.0097 320  LEU A N   
4028 C  CA  . LEU A 320 ? 0.0708 0.0874 0.0725 -0.0152 0.0043  -0.0075 320  LEU A CA  
4029 C  C   . LEU A 320 ? 0.0912 0.1038 0.0712 -0.0229 -0.0027 -0.0081 320  LEU A C   
4030 O  O   . LEU A 320 ? 0.1147 0.1278 0.0768 -0.0250 -0.0140 0.0102  320  LEU A O   
4031 C  CB  . LEU A 320 ? 0.0722 0.0779 0.0764 -0.0078 -0.0028 -0.0109 320  LEU A CB  
4032 C  CG  . LEU A 320 ? 0.0733 0.0839 0.0726 -0.0138 0.0029  -0.0108 320  LEU A CG  
4033 C  CD1 . LEU A 320 ? 0.0784 0.1264 0.1188 -0.0163 0.0102  -0.0578 320  LEU A CD1 
4034 C  CD2 . LEU A 320 ? 0.0747 0.0988 0.0996 -0.0215 0.0066  -0.0103 320  LEU A CD2 
4044 N  N   . GLY A 321 ? 0.0795 0.1065 0.0716 -0.0128 -0.0071 -0.0066 321  GLY A N   
4045 C  CA  . GLY A 321 ? 0.0909 0.1226 0.0750 -0.0201 -0.0012 -0.0224 321  GLY A CA  
4046 C  C   . GLY A 321 ? 0.0931 0.1022 0.0707 -0.0225 -0.0101 -0.0062 321  GLY A C   
4047 O  O   . GLY A 321 ? 0.0906 0.1040 0.0746 -0.0127 -0.0123 -0.0030 321  GLY A O   
4051 N  N   . PHE A 322 ? 0.0792 0.1409 0.0746 -0.0256 -0.0055 -0.0168 322  PHE A N   
4052 C  CA  . PHE A 322 ? 0.0871 0.1305 0.0808 -0.0209 -0.0223 -0.0044 322  PHE A CA  
4053 C  C   . PHE A 322 ? 0.0915 0.1393 0.0884 -0.0225 -0.0287 0.0075  322  PHE A C   
4054 O  O   . PHE A 322 ? 0.0939 0.1303 0.1135 -0.0135 -0.0263 0.0177  322  PHE A O   
4055 C  CB  . PHE A 322 ? 0.0859 0.1550 0.0948 -0.0263 -0.0206 -0.0130 322  PHE A CB  
4056 C  CG  . PHE A 322 ? 0.0792 0.1262 0.1059 -0.0264 0.0034  -0.0403 322  PHE A CG  
4057 C  CD1 . PHE A 322 ? 0.0965 0.1162 0.1061 -0.0243 0.0123  -0.0403 322  PHE A CD1 
4058 C  CD2 . PHE A 322 ? 0.1207 0.1364 0.1445 -0.0561 0.0414  -0.0655 322  PHE A CD2 
4059 C  CE1 . PHE A 322 ? 0.1058 0.1086 0.1420 -0.0304 0.0357  -0.0399 322  PHE A CE1 
4060 C  CE2 . PHE A 322 ? 0.1292 0.1147 0.1982 -0.0433 0.0687  -0.0719 322  PHE A CE2 
4061 C  CZ  . PHE A 322 ? 0.1371 0.1146 0.1789 -0.0431 0.0533  -0.0550 322  PHE A CZ  
4067 N  N   . GLU A 323 ? 0.1073 0.1540 0.0876 -0.0341 -0.0297 0.0098  323  GLU A N   
4068 C  CA  . GLU A 323 ? 0.1561 0.1780 0.0993 -0.0575 -0.0580 0.0375  323  GLU A CA  
4069 C  C   . GLU A 323 ? 0.1412 0.1429 0.0938 -0.0359 -0.0549 0.0414  323  GLU A C   
4070 O  O   . GLU A 323 ? 0.1287 0.1465 0.1440 -0.0234 -0.0516 0.0466  323  GLU A O   
4071 C  CB  A GLU A 323 ? 0.1813 0.1884 0.0939 -0.0592 -0.0491 0.0230  323  GLU A CB  
4072 C  CB  B GLU A 323 ? 0.1692 0.2218 0.0924 -0.0497 -0.0487 0.0361  323  GLU A CB  
4073 C  CG  A GLU A 323 ? 0.2664 0.2209 0.0935 -0.0193 -0.0633 0.0365  323  GLU A CG  
4074 C  CG  B GLU A 323 ? 0.2673 0.3166 0.1382 -0.0945 -0.1051 -0.0213 323  GLU A CG  
4075 C  CD  A GLU A 323 ? 0.3465 0.3179 0.1018 -0.0783 -0.0808 0.0703  323  GLU A CD  
4076 C  CD  B GLU A 323 ? 0.4689 0.3823 0.1813 -0.1452 -0.0916 -0.0685 323  GLU A CD  
4077 O  OE1 A GLU A 323 ? 0.5395 0.4100 0.3251 0.1244  0.0627  0.2657  323  GLU A OE1 
4078 O  OE1 B GLU A 323 ? 0.6305 0.3373 0.1181 -0.1731 -0.0761 -0.0320 323  GLU A OE1 
4079 O  OE2 A GLU A 323 ? 0.7497 0.4771 0.0796 -0.0467 -0.1279 -0.0606 323  GLU A OE2 
4080 O  OE2 B GLU A 323 ? 0.6864 0.1272 0.1401 -0.1758 -0.0564 -0.0011 323  GLU A OE2 
4082 N  N   . TYR A 324 ? 0.1172 0.1354 0.0875 -0.0362 -0.0329 0.0274  324  TYR A N   
4083 C  CA  . TYR A 324 ? 0.1207 0.1137 0.0855 -0.0196 -0.0224 0.0212  324  TYR A CA  
4084 C  C   . TYR A 324 ? 0.0809 0.1105 0.0930 -0.0082 -0.0238 0.0179  324  TYR A C   
4085 O  O   . TYR A 324 ? 0.0988 0.0964 0.1159 -0.0081 -0.0221 0.0181  324  TYR A O   
4086 C  CB  . TYR A 324 ? 0.1064 0.1165 0.1022 -0.0298 -0.0140 0.0198  324  TYR A CB  
4087 C  CG  . TYR A 324 ? 0.1159 0.1003 0.0825 -0.0280 0.0096  0.0069  324  TYR A CG  
4088 C  CD1 . TYR A 324 ? 0.1104 0.1130 0.1132 -0.0188 0.0045  0.0130  324  TYR A CD1 
4089 C  CD2 . TYR A 324 ? 0.1362 0.0948 0.1052 -0.0330 -0.0205 0.0095  324  TYR A CD2 
4090 C  CE1 . TYR A 324 ? 0.1039 0.1004 0.1389 -0.0248 0.0291  0.0002  324  TYR A CE1 
4091 C  CE2 . TYR A 324 ? 0.1364 0.0969 0.1003 -0.0471 -0.0067 0.0073  324  TYR A CE2 
4092 C  CZ  . TYR A 324 ? 0.1157 0.1022 0.0905 -0.0356 0.0110  0.0052  324  TYR A CZ  
4093 O  OH  . TYR A 324 ? 0.1406 0.0995 0.1163 -0.0417 0.0176  -0.0151 324  TYR A OH  
4098 N  N   . TYR A 325 ? 0.0899 0.1004 0.0827 -0.0077 -0.0173 0.0144  325  TYR A N   
4099 C  CA  . TYR A 325 ? 0.0813 0.0934 0.0913 -0.0101 -0.0152 0.0089  325  TYR A CA  
4100 C  C   . TYR A 325 ? 0.0793 0.1016 0.1148 -0.0119 -0.0051 0.0127  325  TYR A C   
4101 O  O   . TYR A 325 ? 0.0814 0.1173 0.1209 0.0016  -0.0064 0.0088  325  TYR A O   
4102 C  CB  . TYR A 325 ? 0.0858 0.0962 0.0843 -0.0086 -0.0098 -0.0013 325  TYR A CB  
4103 C  CG  . TYR A 325 ? 0.0806 0.0733 0.0791 -0.0069 -0.0076 -0.0066 325  TYR A CG  
4104 C  CD1 . TYR A 325 ? 0.0707 0.0780 0.0800 -0.0106 -0.0002 -0.0061 325  TYR A CD1 
4105 C  CD2 . TYR A 325 ? 0.0687 0.0964 0.0934 -0.0072 -0.0058 -0.0064 325  TYR A CD2 
4106 C  CE1 . TYR A 325 ? 0.0622 0.0802 0.0753 -0.0036 -0.0025 -0.0052 325  TYR A CE1 
4107 C  CE2 . TYR A 325 ? 0.0654 0.0920 0.0926 -0.0040 0.0030  -0.0081 325  TYR A CE2 
4108 C  CZ  . TYR A 325 ? 0.0734 0.0775 0.0750 -0.0046 0.0074  -0.0067 325  TYR A CZ  
4109 O  OH  . TYR A 325 ? 0.0754 0.0988 0.0835 -0.0074 0.0056  -0.0070 325  TYR A OH  
4116 N  N   . SER A 326 ? 0.0769 0.1112 0.1362 -0.0102 -0.0290 0.0170  326  SER A N   
4117 C  CA  . SER A 326 ? 0.0917 0.1222 0.1708 0.0093  -0.0216 -0.0043 326  SER A CA  
4118 C  C   . SER A 326 ? 0.1144 0.1290 0.1723 0.0251  -0.0413 0.0112  326  SER A C   
4119 O  O   . SER A 326 ? 0.1319 0.1316 0.2128 0.0299  -0.0358 0.0091  326  SER A O   
4120 C  CB  . SER A 326 ? 0.1212 0.1787 0.2228 0.0266  -0.0856 -0.0163 326  SER A CB  
4121 O  OG  . SER A 326 ? 0.1412 0.2402 0.3917 0.0379  -0.1016 -0.0531 326  SER A OG  
4125 N  N   . ALA A 327 ? 0.1194 0.1344 0.1564 -0.0007 -0.0570 0.0226  327  ALA A N   
4126 C  CA  . ALA A 327 ? 0.1510 0.1354 0.1699 0.0140  -0.0658 0.0226  327  ALA A CA  
4127 C  C   . ALA A 327 ? 0.1212 0.1154 0.1795 0.0130  -0.0511 0.0121  327  ALA A C   
4128 O  O   . ALA A 327 ? 0.1585 0.1083 0.2256 0.0330  -0.0629 0.0081  327  ALA A O   
4129 C  CB  . ALA A 327 ? 0.1854 0.1305 0.1622 -0.0246 -0.0606 0.0395  327  ALA A CB  
4130 N  N   . ILE A 328 ? 0.1026 0.1186 0.1316 0.0146  -0.0267 0.0074  328  ILE A N   
4131 C  CA  . ILE A 328 ? 0.1128 0.0969 0.1307 0.0169  -0.0148 0.0115  328  ILE A CA  
4132 C  C   . ILE A 328 ? 0.1070 0.1276 0.1486 0.0292  -0.0146 -0.0031 328  ILE A C   
4133 O  O   . ILE A 328 ? 0.1336 0.1529 0.1583 0.0287  -0.0080 -0.0195 328  ILE A O   
4134 C  CB  . ILE A 328 ? 0.0996 0.1005 0.1054 0.0105  -0.0021 0.0129  328  ILE A CB  
4135 C  CG1 . ILE A 328 ? 0.0879 0.1111 0.1067 -0.0071 -0.0062 0.0235  328  ILE A CG1 
4136 C  CG2 . ILE A 328 ? 0.1117 0.1288 0.1131 0.0107  -0.0051 0.0033  328  ILE A CG2 
4137 C  CD1 . ILE A 328 ? 0.0869 0.1236 0.1436 0.0021  0.0044  0.0263  328  ILE A CD1 
4145 N  N   . GLN A 329 ? 0.0967 0.1367 0.1681 0.0134  0.0083  0.0100  329  GLN A N   
4146 C  CA  . GLN A 329 ? 0.1093 0.1443 0.1877 0.0180  0.0096  -0.0237 329  GLN A CA  
4147 C  C   . GLN A 329 ? 0.1015 0.1488 0.2834 0.0248  -0.0081 -0.0384 329  GLN A C   
4148 O  O   . GLN A 329 ? 0.1137 0.1705 0.3238 0.0301  0.0351  -0.0295 329  GLN A O   
4149 C  CB  . GLN A 329 ? 0.0991 0.1405 0.1893 0.0007  -0.0049 0.0097  329  GLN A CB  
4150 C  CG  . GLN A 329 ? 0.0993 0.1352 0.1680 0.0020  0.0006  -0.0215 329  GLN A CG  
4151 C  CD  . GLN A 329 ? 0.1030 0.1429 0.1409 -0.0164 0.0036  -0.0188 329  GLN A CD  
4152 O  OE1 . GLN A 329 ? 0.1787 0.1460 0.1875 -0.0416 -0.0288 0.0094  329  GLN A OE1 
4153 N  NE2 . GLN A 329 ? 0.0740 0.1426 0.1804 -0.0018 0.0212  -0.0034 329  GLN A NE2 
4157 N  N   . SER A 330 ? 0.1469 0.1493 0.2768 0.0564  -0.0633 -0.0444 330  SER A N   
4158 C  CA  A SER A 330 ? 0.1532 0.1643 0.3600 0.0626  -0.0781 -0.0366 330  SER A CA  
4159 C  CA  B SER A 330 ? 0.1276 0.1565 0.3508 0.0490  -0.0376 -0.0214 330  SER A CA  
4160 C  C   . SER A 330 ? 0.1608 0.1472 0.2953 0.0606  -0.0704 -0.0061 330  SER A C   
4161 O  O   . SER A 330 ? 0.2113 0.1706 0.3911 0.0898  -0.0959 -0.0490 330  SER A O   
4162 C  CB  A SER A 330 ? 0.2139 0.2190 0.3529 0.0879  -0.1660 -0.0438 330  SER A CB  
4163 C  CB  B SER A 330 ? 0.1734 0.2045 0.3879 0.0164  -0.1657 -0.0223 330  SER A CB  
4164 O  OG  A SER A 330 ? 0.3117 0.1900 0.2588 0.0778  -0.1722 0.0077  330  SER A OG  
4165 O  OG  B SER A 330 ? 0.1605 0.1530 0.4625 0.0429  -0.1241 -0.0292 330  SER A OG  
4167 N  N   . MET A 331 ? 0.1437 0.1340 0.2073 0.0304  -0.0068 0.0136  331  MET A N   
4168 C  CA  . MET A 331 ? 0.1532 0.1462 0.1984 0.0277  -0.0090 -0.0017 331  MET A CA  
4169 C  C   . MET A 331 ? 0.2102 0.1932 0.1937 0.0426  -0.0264 0.0008  331  MET A C   
4170 O  O   . MET A 331 ? 0.4363 0.1990 0.2329 0.0082  -0.1024 -0.0108 331  MET A O   
4171 C  CB  A MET A 331 ? 0.1790 0.1990 0.2805 -0.0129 0.0290  0.0899  331  MET A CB  
4172 C  CB  B MET A 331 ? 0.1485 0.2387 0.2348 -0.0052 -0.0360 0.0502  331  MET A CB  
4173 C  CG  A MET A 331 ? 0.1298 0.2134 0.2516 -0.0090 0.0221  -0.0366 331  MET A CG  
4174 C  CG  B MET A 331 ? 0.2006 0.3280 0.1462 0.0406  -0.0042 0.0107  331  MET A CG  
4175 S  SD  A MET A 331 ? 0.1262 0.1660 0.2261 -0.0050 0.0125  0.0027  331  MET A SD  
4176 S  SD  B MET A 331 ? 0.2332 0.2631 0.1893 0.0736  0.0307  0.0455  331  MET A SD  
4177 C  CE  A MET A 331 ? 0.1632 0.1523 0.1498 -0.0070 0.0116  0.0358  331  MET A CE  
4178 C  CE  B MET A 331 ? 0.3821 0.2141 0.3907 -0.1125 -0.1302 0.0624  331  MET A CE  
4179 N  N   . ARG A 332 ? 0.2156 0.2075 0.1912 0.0739  0.0292  0.0013  332  ARG A N   
4180 C  CA  A ARG A 332 ? 0.2323 0.3760 0.1864 0.0743  0.0207  0.0102  332  ARG A CA  
4181 C  CA  B ARG A 332 ? 0.2258 0.3752 0.1902 0.0734  0.0184  0.0246  332  ARG A CA  
4182 C  C   . ARG A 332 ? 0.2634 0.4056 0.2644 0.1044  0.0859  0.0263  332  ARG A C   
4183 O  O   A ARG A 332 ? 0.2205 0.2797 0.4147 0.0732  0.0974  -0.1457 332  ARG A O   
4184 O  O   B ARG A 332 ? 0.2258 0.3635 0.5202 0.0655  0.0171  0.1348  332  ARG A O   
4185 C  CB  A ARG A 332 ? 0.2445 0.4408 0.1848 0.0774  -0.0237 0.0362  332  ARG A CB  
4186 C  CB  B ARG A 332 ? 0.2306 0.4094 0.1443 0.0860  -0.0080 0.0393  332  ARG A CB  
4187 C  CG  A ARG A 332 ? 0.3088 0.3314 0.1931 0.1020  -0.0085 -0.0085 332  ARG A CG  
4188 C  CG  B ARG A 332 ? 0.2307 0.3516 0.2037 0.0665  -0.0184 -0.0044 332  ARG A CG  
4189 C  CD  A ARG A 332 ? 0.2936 0.3349 0.2134 0.0402  -0.1257 0.0131  332  ARG A CD  
4190 C  CD  B ARG A 332 ? 0.2467 0.3381 0.2230 0.0792  -0.0478 -0.0479 332  ARG A CD  
4191 N  NE  A ARG A 332 ? 0.3526 0.3080 0.1994 0.0595  -0.0754 -0.0203 332  ARG A NE  
4192 N  NE  B ARG A 332 ? 0.3352 0.3315 0.2131 0.0743  -0.0618 -0.0073 332  ARG A NE  
4193 C  CZ  A ARG A 332 ? 0.2822 0.2988 0.2092 0.1138  -0.0399 -0.0231 332  ARG A CZ  
4194 C  CZ  B ARG A 332 ? 0.3555 0.2566 0.2189 0.1281  -0.0839 -0.0815 332  ARG A CZ  
4195 N  NH1 A ARG A 332 ? 0.2252 0.3129 0.4715 0.1060  -0.0359 -0.0552 332  ARG A NH1 
4196 N  NH1 B ARG A 332 ? 0.3435 0.2451 0.4228 0.1611  -0.1277 -0.1767 332  ARG A NH1 
4197 N  NH2 A ARG A 332 ? 0.4551 0.3923 0.2130 0.2516  -0.0455 0.0314  332  ARG A NH2 
4198 N  NH2 B ARG A 332 ? 0.4985 0.2881 0.1849 0.1951  -0.0575 -0.0832 332  ARG A NH2 
4199 O  OXT A ARG A 332 ? 0.4142 0.6673 0.3026 0.1163  0.1871  -0.0744 332  ARG A OXT 
4200 O  OXT B ARG A 332 ? 0.5084 0.5617 0.2885 0.1688  0.1998  0.1075  332  ARG A OXT 
4201 FE FE  . FE  B .   ? 0.0480 0.0482 0.0427 0.0014  0.0008  0.0010  401  FE  A FE  
4202 C  C   . CO3 C .   ? 0.0621 0.0680 0.0538 -0.0058 0.0044  0.0012  402  CO3 A C   
4203 O  O1  . CO3 C .   ? 0.0641 0.0823 0.0513 -0.0012 -0.0020 0.0022  402  CO3 A O1  
4204 O  O2  . CO3 C .   ? 0.0748 0.0664 0.0566 0.0033  0.0018  -0.0027 402  CO3 A O2  
4205 O  O3  . CO3 C .   ? 0.0589 0.0653 0.0513 -0.0023 -0.0004 -0.0029 402  CO3 A O3  
4206 C  C1  . GOL D .   ? 0.0901 0.1118 0.0925 0.0025  0.0031  -0.0110 403  GOL A C1  
4207 O  O1  . GOL D .   ? 0.0909 0.0949 0.0916 -0.0093 0.0101  -0.0046 403  GOL A O1  
4208 C  C2  . GOL D .   ? 0.1133 0.1140 0.0996 -0.0108 0.0278  -0.0105 403  GOL A C2  
4209 O  O2  . GOL D .   ? 0.2267 0.1280 0.1130 -0.0308 0.0398  -0.0063 403  GOL A O2  
4210 C  C3  . GOL D .   ? 0.1028 0.1366 0.0949 -0.0016 0.0113  -0.0147 403  GOL A C3  
4211 O  O3  . GOL D .   ? 0.0995 0.1354 0.0981 -0.0188 0.0202  -0.0114 403  GOL A O3  
4212 O  O   . HOH E .   ? 0.4136 0.5797 0.3316 -0.3693 -0.0968 0.1846  501  HOH A O   
4213 O  O   . HOH E .   ? 0.4921 0.2500 1.1380 -0.0436 0.5254  -0.1613 502  HOH A O   
4214 O  O   . HOH E .   ? 0.2776 0.2284 0.3704 -0.0018 0.0042  -0.0723 503  HOH A O   
4215 O  O   . HOH E .   ? 0.1879 0.4384 0.4849 -0.0689 0.0034  0.1541  504  HOH A O   
4216 O  O   . HOH E .   ? 0.8960 0.4266 0.6413 0.3337  -0.0109 0.2043  505  HOH A O   
4217 O  O   . HOH E .   ? 0.4555 0.5201 0.9131 -0.1124 0.1399  -0.3226 506  HOH A O   
4218 O  O   . HOH E .   ? 0.2983 0.2267 0.8645 -0.0261 -0.2754 -0.1141 507  HOH A O   
4219 O  O   . HOH E .   ? 0.4158 0.5531 0.3278 0.0714  -0.0438 0.0896  508  HOH A O   
4220 O  O   . HOH E .   ? 0.2118 0.2285 0.2526 -0.0409 0.0004  -0.0325 509  HOH A O   
4221 O  O   . HOH E .   ? 0.4422 0.3546 0.4298 -0.0967 0.1461  0.0871  510  HOH A O   
4222 O  O   . HOH E .   ? 0.1426 0.3651 0.4484 -0.0215 0.1013  -0.1396 511  HOH A O   
4223 O  O   A HOH E .   ? 0.1129 0.1235 0.2748 0.0228  -0.0750 -0.0124 512  HOH A O   
4224 O  O   B HOH E .   ? 0.0989 0.1116 0.2703 0.0063  -0.0201 -0.0655 512  HOH A O   
4225 O  O   . HOH E .   ? 0.2919 0.5111 0.2743 0.0520  0.1795  0.1280  513  HOH A O   
4226 O  O   . HOH E .   ? 0.2470 0.5634 0.3884 -0.0608 0.0283  -0.1756 514  HOH A O   
4227 O  O   . HOH E .   ? 0.2009 0.2095 0.2115 0.0402  -0.0166 -0.0178 515  HOH A O   
4228 O  O   . HOH E .   ? 0.3511 0.1847 0.2109 -0.0874 0.1062  -0.0416 516  HOH A O   
4229 O  O   . HOH E .   ? 0.3105 0.2884 0.3938 0.0928  -0.0154 0.1310  517  HOH A O   
4230 O  O   . HOH E .   ? 0.8359 0.1849 0.1274 0.0156  -0.0356 -0.0085 518  HOH A O   
4231 O  O   . HOH E .   ? 0.1845 0.2635 0.1666 -0.0549 -0.0245 0.0508  519  HOH A O   
4232 O  O   . HOH E .   ? 0.2361 0.2498 0.2598 -0.0304 0.0453  0.0518  520  HOH A O   
4233 O  O   . HOH E .   ? 0.3213 0.4641 0.5565 0.2085  -0.3044 -0.3901 521  HOH A O   
4234 O  O   . HOH E .   ? 0.4934 0.5043 1.0888 -0.0350 0.2999  -0.2319 522  HOH A O   
4235 O  O   . HOH E .   ? 0.5486 0.6053 0.4883 -0.3747 0.1871  -0.2295 523  HOH A O   
4236 O  O   . HOH E .   ? 0.4464 0.2279 0.2390 -0.0397 0.1361  -0.0045 524  HOH A O   
4237 O  O   A HOH E .   ? 0.1188 0.1121 0.1062 0.0110  0.0095  0.0587  525  HOH A O   
4238 O  O   B HOH E .   ? 0.1344 0.2981 0.1076 0.0826  -0.0083 -0.0405 525  HOH A O   
4239 O  O   . HOH E .   ? 0.2938 0.7979 0.4694 -0.3175 -0.0913 0.2921  526  HOH A O   
4240 O  O   . HOH E .   ? 0.4009 0.3686 0.6194 0.0841  -0.1772 -0.1490 527  HOH A O   
4241 O  O   . HOH E .   ? 0.2806 0.3801 0.1621 0.1935  0.0437  0.0272  528  HOH A O   
4242 O  O   . HOH E .   ? 0.3193 0.7399 0.1698 0.2769  -0.0588 0.0215  529  HOH A O   
4243 O  O   . HOH E .   ? 0.2557 0.7702 0.5808 0.0911  -0.1380 -0.3819 530  HOH A O   
4244 O  O   . HOH E .   ? 0.4769 0.1597 0.6995 0.1098  -0.1123 -0.0899 531  HOH A O   
4245 O  O   . HOH E .   ? 0.8088 0.1984 0.2825 0.1237  0.2004  0.0199  532  HOH A O   
4246 O  O   . HOH E .   ? 0.4529 0.2068 0.3324 -0.1087 -0.0021 -0.0864 533  HOH A O   
4247 O  O   . HOH E .   ? 0.8489 0.4896 0.2730 -0.2270 0.3063  -0.1737 534  HOH A O   
4248 O  O   A HOH E .   ? 0.2487 0.1585 0.2538 0.0450  -0.1170 -0.1162 535  HOH A O   
4249 O  O   B HOH E .   ? 0.3360 0.1401 0.3906 -0.0129 -0.3146 0.0508  535  HOH A O   
4250 O  O   . HOH E .   ? 0.2530 0.3418 0.2896 -0.0989 0.0243  -0.0182 536  HOH A O   
4251 O  O   . HOH E .   ? 0.5113 0.3440 0.4139 0.2302  -0.1723 -0.1196 537  HOH A O   
4252 O  O   . HOH E .   ? 0.4005 0.5307 0.5436 -0.2817 -0.2721 0.3386  538  HOH A O   
4253 O  O   . HOH E .   ? 0.2035 0.2588 0.1504 -0.0983 -0.0266 0.0224  539  HOH A O   
4254 O  O   . HOH E .   ? 0.1701 0.4526 0.3187 0.0321  -0.0355 0.0224  540  HOH A O   
4255 O  O   . HOH E .   ? 0.5039 0.1641 0.1913 0.0567  0.0987  0.0250  541  HOH A O   
4256 O  O   . HOH E .   ? 0.3166 0.4532 0.1229 0.2217  0.0321  0.0005  542  HOH A O   
4257 O  O   . HOH E .   ? 0.1544 0.1059 0.0912 -0.0230 0.0427  -0.0012 543  HOH A O   
4258 O  O   . HOH E .   ? 0.1406 0.2137 0.5047 -0.0032 0.0029  -0.0528 544  HOH A O   
4259 O  O   . HOH E .   ? 0.8065 0.4961 1.0366 -0.1878 -0.3025 -0.0500 545  HOH A O   
4260 O  O   . HOH E .   ? 0.7284 0.4356 0.2688 0.2624  0.0482  0.1764  546  HOH A O   
4261 O  O   A HOH E .   ? 0.3871 0.1869 0.2052 0.1348  -0.2262 -0.1159 547  HOH A O   
4262 O  O   B HOH E .   ? 0.1804 0.2055 0.2351 0.0118  -0.0098 -0.0379 547  HOH A O   
4263 O  O   . HOH E .   ? 0.2682 0.1695 0.6828 0.0080  -0.1039 0.0305  548  HOH A O   
4264 O  O   . HOH E .   ? 0.2098 0.3628 0.3907 0.0324  -0.0593 -0.1305 549  HOH A O   
4265 O  O   . HOH E .   ? 0.2912 0.4950 0.2739 -0.0217 0.1067  -0.1312 550  HOH A O   
4266 O  O   . HOH E .   ? 0.2653 0.4758 0.2408 -0.1519 0.0345  -0.0962 551  HOH A O   
4267 O  O   A HOH E .   ? 0.2615 0.3043 0.3709 -0.0097 -0.1015 -0.0234 552  HOH A O   
4268 O  O   B HOH E .   ? 0.4182 0.1052 0.1024 0.0399  0.0360  -0.0261 552  HOH A O   
4269 O  O   . HOH E .   ? 0.1608 0.5248 0.3987 -0.0106 -0.0611 -0.1365 553  HOH A O   
4270 O  O   . HOH E .   ? 0.1721 0.1709 0.3476 0.0121  -0.0039 -0.0554 554  HOH A O   
4271 O  O   . HOH E .   ? 0.1098 0.3731 0.1806 -0.0099 0.0335  0.0530  555  HOH A O   
4272 O  O   . HOH E .   ? 0.2416 0.6825 0.2671 0.0528  0.0079  -0.1756 556  HOH A O   
4273 O  O   . HOH E .   ? 0.3445 0.2984 0.7121 0.0831  -0.1794 0.0253  557  HOH A O   
4274 O  O   . HOH E .   ? 0.0749 0.0901 0.0738 -0.0037 -0.0005 -0.0041 558  HOH A O   
4275 O  O   . HOH E .   ? 0.1951 0.1666 0.2126 0.0575  0.0421  -0.0099 559  HOH A O   
4276 O  O   . HOH E .   ? 0.1669 0.1656 0.2503 0.0011  0.0328  -0.0562 560  HOH A O   
4277 O  O   A HOH E .   ? 0.0962 0.2181 0.2856 0.0049  0.0603  -0.0054 561  HOH A O   
4278 O  O   B HOH E .   ? 0.0720 0.1070 0.1445 0.0066  0.0000  -0.0254 561  HOH A O   
4279 O  O   . HOH E .   ? 0.2966 0.6797 0.2382 0.2586  -0.0028 0.1209  562  HOH A O   
4280 O  O   . HOH E .   ? 0.3355 0.2596 0.6319 0.0468  -0.1397 0.1213  563  HOH A O   
4281 O  O   A HOH E .   ? 0.1966 0.2717 0.3009 -0.0248 -0.0692 -0.0571 564  HOH A O   
4282 O  O   B HOH E .   ? 0.3234 0.2425 0.5279 0.2042  -0.1835 -0.2607 564  HOH A O   
4283 O  O   . HOH E .   ? 0.4341 0.1182 0.4301 0.0476  0.0940  -0.0075 565  HOH A O   
4284 O  O   . HOH E .   ? 0.2372 0.1716 0.4120 -0.0111 0.0494  0.0133  566  HOH A O   
4285 O  O   . HOH E .   ? 0.2045 0.1390 0.1256 -0.0497 -0.0252 0.0323  567  HOH A O   
4286 O  O   . HOH E .   ? 0.3847 0.2815 0.4796 -0.0803 0.1566  -0.2000 568  HOH A O   
4287 O  O   . HOH E .   ? 0.1465 0.1438 0.1478 0.0115  -0.0186 0.0033  569  HOH A O   
4288 O  O   . HOH E .   ? 0.2168 0.3815 0.1212 -0.1984 -0.0275 0.0422  570  HOH A O   
4289 O  O   . HOH E .   ? 0.3490 0.2276 0.1520 0.1117  0.1000  0.0142  571  HOH A O   
4290 O  O   . HOH E .   ? 0.2801 0.1789 0.6067 -0.0015 0.0304  0.1856  572  HOH A O   
4291 O  O   . HOH E .   ? 0.1244 0.1074 0.0624 -0.0041 0.0213  0.0049  573  HOH A O   
4292 O  O   . HOH E .   ? 0.2061 0.1918 0.2083 0.0225  0.0379  -0.0152 574  HOH A O   
4293 O  O   . HOH E .   ? 0.2356 0.2204 0.1865 -0.0623 0.0280  -0.0121 575  HOH A O   
4294 O  O   . HOH E .   ? 0.1350 0.1852 0.1278 0.0072  0.0373  0.0564  576  HOH A O   
4295 O  O   . HOH E .   ? 0.1234 0.0963 0.0679 -0.0446 0.0331  -0.0193 577  HOH A O   
4296 O  O   . HOH E .   ? 0.2901 0.5803 0.3418 -0.0055 0.1484  -0.0584 578  HOH A O   
4297 O  O   . HOH E .   ? 0.3610 0.2269 0.4507 -0.0567 -0.0687 0.0116  579  HOH A O   
4298 O  O   . HOH E .   ? 0.4578 0.1960 0.2075 0.1168  -0.0551 -0.0491 580  HOH A O   
4299 O  O   . HOH E .   ? 0.1166 0.1626 0.1339 0.0124  0.0069  0.0240  581  HOH A O   
4300 O  O   . HOH E .   ? 0.2242 0.1762 0.1862 0.0382  0.0008  0.0148  582  HOH A O   
4301 O  O   . HOH E .   ? 0.3013 0.2129 0.2434 0.0510  -0.1220 -0.0460 583  HOH A O   
4302 O  O   . HOH E .   ? 0.2024 0.3000 0.2459 0.0257  0.0855  0.0406  584  HOH A O   
4303 O  O   . HOH E .   ? 0.1108 0.2567 0.2120 0.0401  -0.0121 -0.1207 585  HOH A O   
4304 O  O   . HOH E .   ? 0.2318 0.2151 0.2370 0.0268  0.0352  0.0787  586  HOH A O   
4305 O  O   . HOH E .   ? 0.1209 0.1517 0.1372 0.0070  -0.0502 -0.0063 587  HOH A O   
4306 O  O   . HOH E .   ? 0.3777 0.5399 0.4619 0.1444  -0.0739 0.1766  588  HOH A O   
4307 O  O   . HOH E .   ? 0.2665 0.3158 0.7267 -0.0983 0.1678  -0.1800 589  HOH A O   
4308 O  O   . HOH E .   ? 0.0960 0.0780 0.0625 -0.0053 -0.0081 0.0016  590  HOH A O   
4309 O  O   . HOH E .   ? 0.5671 0.8983 0.4271 0.0648  -0.3775 0.0636  591  HOH A O   
4310 O  O   . HOH E .   ? 0.2175 0.3080 0.2422 -0.0248 -0.0416 -0.1340 592  HOH A O   
4311 O  O   A HOH E .   ? 0.1571 0.1581 0.1689 0.0413  0.0067  -0.0334 593  HOH A O   
4312 O  O   B HOH E .   ? 0.1724 0.2303 0.1969 0.0807  0.0239  0.0276  593  HOH A O   
4313 O  O   . HOH E .   ? 0.2898 0.5513 0.4853 0.1760  0.0873  0.2240  594  HOH A O   
4314 O  O   . HOH E .   ? 0.1830 0.3290 0.8991 -0.0318 0.0663  0.2371  595  HOH A O   
4315 O  O   . HOH E .   ? 0.1030 0.0946 0.1083 0.0084  0.0122  -0.0107 596  HOH A O   
4316 O  O   . HOH E .   ? 0.2362 0.1522 0.1152 -0.0061 0.0332  0.0448  597  HOH A O   
4317 O  O   . HOH E .   ? 0.3767 0.2794 0.2495 -0.1002 0.0243  -0.0244 598  HOH A O   
4318 O  O   . HOH E .   ? 0.1028 0.1363 0.1288 0.0248  -0.0097 -0.0242 599  HOH A O   
4319 O  O   . HOH E .   ? 0.2944 0.1923 0.2397 0.0278  -0.0681 -0.0002 600  HOH A O   
4320 O  O   . HOH E .   ? 0.5192 0.2239 0.1471 -0.0227 0.0655  -0.0295 601  HOH A O   
4321 O  O   . HOH E .   ? 0.1119 0.2511 0.1180 0.0683  -0.0238 -0.0182 602  HOH A O   
4322 O  O   . HOH E .   ? 0.2655 0.1647 0.1549 0.0280  -0.0015 -0.0231 603  HOH A O   
4323 O  O   . HOH E .   ? 0.1209 0.1467 0.1927 -0.0194 0.0199  0.0303  604  HOH A O   
4324 O  O   . HOH E .   ? 0.1206 0.5107 0.2253 0.0435  0.0110  0.2053  605  HOH A O   
4325 O  O   . HOH E .   ? 0.1976 0.2799 0.7127 -0.0418 -0.0067 0.1888  606  HOH A O   
4326 O  O   . HOH E .   ? 0.3570 0.4981 0.5377 0.2142  0.1076  0.0993  607  HOH A O   
4327 O  O   . HOH E .   ? 0.1039 0.1261 0.2245 -0.0099 0.0184  0.0300  608  HOH A O   
4328 O  O   . HOH E .   ? 0.1062 0.0875 0.0703 -0.0094 -0.0019 -0.0025 609  HOH A O   
4329 O  O   . HOH E .   ? 0.1077 0.1106 0.0733 -0.0002 0.0078  -0.0085 610  HOH A O   
4330 O  O   . HOH E .   ? 0.6975 0.1433 0.2885 0.1157  0.0449  0.0088  611  HOH A O   
4331 O  O   . HOH E .   ? 0.1531 0.3497 0.1944 -0.0318 -0.0186 -0.0562 612  HOH A O   
4332 O  O   . HOH E .   ? 0.3448 0.3707 0.2424 -0.1703 -0.0365 -0.0108 613  HOH A O   
4333 O  O   . HOH E .   ? 0.1491 0.1168 0.1121 0.0136  0.0200  -0.0079 614  HOH A O   
4334 O  O   . HOH E .   ? 0.1753 0.1234 0.2130 0.0234  0.0287  0.0496  615  HOH A O   
4335 O  O   . HOH E .   ? 0.1451 0.1587 0.1461 -0.0391 0.0621  -0.0192 616  HOH A O   
4336 O  O   . HOH E .   ? 0.1124 0.0872 0.1129 0.0103  0.0060  -0.0051 617  HOH A O   
4337 O  O   . HOH E .   ? 0.2558 0.4002 0.3973 0.0990  0.0806  0.0942  618  HOH A O   
4338 O  O   . HOH E .   ? 0.0927 0.0781 0.0674 -0.0088 -0.0121 0.0111  619  HOH A O   
4339 O  O   . HOH E .   ? 0.1685 0.1879 0.1545 0.0403  -0.0059 -0.0145 620  HOH A O   
4340 O  O   . HOH E .   ? 0.0922 0.0981 0.0700 0.0204  -0.0003 0.0024  621  HOH A O   
4341 O  O   . HOH E .   ? 0.1912 0.1736 0.1989 -0.0122 -0.0139 0.0197  622  HOH A O   
4342 O  O   . HOH E .   ? 0.0860 0.0721 0.0670 0.0011  -0.0035 -0.0008 623  HOH A O   
4343 O  O   . HOH E .   ? 0.1513 0.1548 0.1663 -0.0101 0.0503  -0.0341 624  HOH A O   
4344 O  O   . HOH E .   ? 0.1427 0.1191 0.1375 -0.0047 0.0228  0.0301  625  HOH A O   
4345 O  O   . HOH E .   ? 0.1407 0.1582 0.0921 -0.0186 0.0143  -0.0211 626  HOH A O   
4346 O  O   . HOH E .   ? 0.0766 0.1300 0.0866 0.0271  -0.0054 -0.0202 627  HOH A O   
4347 O  O   . HOH E .   ? 0.0903 0.1063 0.1143 -0.0182 0.0333  -0.0198 628  HOH A O   
4348 O  O   . HOH E .   ? 0.1017 0.1261 0.1253 -0.0005 -0.0110 0.0093  629  HOH A O   
4349 O  O   . HOH E .   ? 0.9356 0.4448 0.2807 -0.3313 0.1446  -0.1198 630  HOH A O   
4350 O  O   . HOH E .   ? 0.1798 0.2189 0.1546 -0.0570 -0.0160 0.0498  631  HOH A O   
4351 O  O   . HOH E .   ? 0.3239 0.3568 0.1294 -0.2221 0.0420  -0.0059 632  HOH A O   
4352 O  O   . HOH E .   ? 0.1892 0.1547 0.1168 -0.0208 -0.0044 -0.0243 633  HOH A O   
4353 O  O   A HOH E .   ? 0.2227 0.2301 0.2116 0.0213  0.0142  -0.0825 634  HOH A O   
4354 O  O   B HOH E .   ? 0.1683 0.1925 0.0879 -0.1217 0.0798  -0.0941 634  HOH A O   
4355 O  O   . HOH E .   ? 0.0812 0.0927 0.1062 -0.0103 0.0064  -0.0039 635  HOH A O   
4356 O  O   . HOH E .   ? 0.3808 0.5771 0.2526 0.0839  0.0623  0.2139  636  HOH A O   
4357 O  O   . HOH E .   ? 0.1158 0.1746 0.1329 -0.0053 0.0002  0.0093  637  HOH A O   
4358 O  O   . HOH E .   ? 0.2200 0.4470 0.2107 0.0672  -0.0825 -0.0717 638  HOH A O   
4359 O  O   . HOH E .   ? 0.3156 0.1975 0.2619 0.0946  0.1283  0.1265  639  HOH A O   
4360 O  O   . HOH E .   ? 0.1250 0.2076 0.3073 0.0417  -0.0413 -0.0157 640  HOH A O   
4361 O  O   . HOH E .   ? 0.5551 0.8315 0.1816 0.3461  -0.0438 -0.1125 641  HOH A O   
4362 O  O   . HOH E .   ? 0.1202 0.1081 0.1154 0.0013  0.0017  -0.0165 642  HOH A O   
4363 O  O   . HOH E .   ? 0.1739 0.1587 0.1106 0.0096  0.0695  0.0257  643  HOH A O   
4364 O  O   . HOH E .   ? 0.1435 0.3999 0.8890 0.0353  -0.0824 0.1094  644  HOH A O   
4365 O  O   . HOH E .   ? 0.1184 0.1663 0.1502 0.0349  0.0155  0.0616  645  HOH A O   
4366 O  O   . HOH E .   ? 0.1290 0.1301 0.1014 -0.0147 0.0061  -0.0007 646  HOH A O   
4367 O  O   . HOH E .   ? 0.1656 0.1931 0.2507 0.0740  0.0331  0.0602  647  HOH A O   
4368 O  O   . HOH E .   ? 0.5497 0.1716 0.1400 0.1691  -0.1250 -0.0696 648  HOH A O   
4369 O  O   . HOH E .   ? 0.1625 0.2376 0.2213 0.0063  0.0114  -0.0692 649  HOH A O   
4370 O  O   . HOH E .   ? 0.1728 0.1976 0.2527 -0.0277 -0.0012 0.0980  650  HOH A O   
4371 O  O   . HOH E .   ? 0.4821 0.7001 0.5349 0.1036  0.0626  0.4776  651  HOH A O   
4372 O  O   . HOH E .   ? 1.0826 0.2333 0.1877 0.1088  0.2264  0.0554  652  HOH A O   
4373 O  O   . HOH E .   ? 0.5178 0.3314 0.2459 0.0171  0.1756  -0.0545 653  HOH A O   
4374 O  O   . HOH E .   ? 0.1176 0.1359 0.1056 -0.0191 -0.0029 -0.0111 654  HOH A O   
4375 O  O   . HOH E .   ? 0.3370 0.2590 0.5639 0.1378  0.1701  0.1518  655  HOH A O   
4376 O  O   . HOH E .   ? 0.1000 0.0942 0.0750 0.0021  -0.0186 0.0018  656  HOH A O   
4377 O  O   . HOH E .   ? 0.0852 0.0847 0.0968 -0.0010 0.0070  0.0106  657  HOH A O   
4378 O  O   . HOH E .   ? 0.3728 0.2997 0.3490 0.2012  0.0601  0.0036  658  HOH A O   
4379 O  O   . HOH E .   ? 0.2423 0.1266 0.0902 -0.0176 0.0510  -0.0043 659  HOH A O   
4380 O  O   . HOH E .   ? 0.1320 0.1905 0.2626 0.0334  0.0652  -0.0415 660  HOH A O   
4381 O  O   . HOH E .   ? 0.1302 0.1493 0.4480 -0.0067 0.0134  -0.0104 661  HOH A O   
4382 O  O   . HOH E .   ? 0.4908 0.5234 0.2861 0.3296  -0.0955 -0.0602 662  HOH A O   
4383 O  O   . HOH E .   ? 0.2911 0.3854 0.3911 0.0254  -0.0986 0.0967  663  HOH A O   
4384 O  O   . HOH E .   ? 0.1670 0.4684 0.4005 -0.0557 0.0915  -0.2126 664  HOH A O   
4385 O  O   . HOH E .   ? 0.2552 0.2300 0.4599 0.0076  -0.0480 0.0341  665  HOH A O   
4386 O  O   . HOH E .   ? 0.1705 0.1646 0.2962 0.0072  0.0024  -0.0247 666  HOH A O   
4387 O  O   . HOH E .   ? 0.1561 0.1461 0.2123 -0.0085 0.0582  -0.0738 667  HOH A O   
4388 O  O   . HOH E .   ? 0.1184 0.1318 0.1274 0.0075  0.0027  0.0404  668  HOH A O   
4389 O  O   . HOH E .   ? 0.0801 0.1032 0.1254 -0.0075 -0.0009 0.0184  669  HOH A O   
4390 O  O   . HOH E .   ? 0.1590 0.3585 0.2486 -0.0481 0.0095  0.0088  670  HOH A O   
4391 O  O   . HOH E .   ? 0.0860 0.0729 0.0903 0.0073  -0.0151 -0.0093 671  HOH A O   
4392 O  O   A HOH E .   ? 0.3468 0.2124 0.1785 0.1073  0.1118  0.0460  672  HOH A O   
4393 O  O   B HOH E .   ? 0.0530 0.1141 0.0748 0.0072  0.0228  -0.0106 672  HOH A O   
4394 O  O   . HOH E .   ? 0.0959 0.4355 0.2539 -0.0172 0.0147  0.1418  673  HOH A O   
4395 O  O   . HOH E .   ? 0.0912 0.1154 0.1211 0.0018  -0.0315 0.0059  674  HOH A O   
4396 O  O   . HOH E .   ? 0.3608 0.3834 0.6424 -0.0527 0.1492  -0.2595 675  HOH A O   
4397 O  O   . HOH E .   ? 0.1071 0.1128 0.0972 0.0153  0.0165  0.0226  676  HOH A O   
4398 O  O   . HOH E .   ? 0.1256 0.3030 0.1623 -0.0301 0.0167  -0.0699 677  HOH A O   
4399 O  O   . HOH E .   ? 0.1750 0.1747 0.1292 -0.0383 -0.0170 -0.0250 678  HOH A O   
4400 O  O   . HOH E .   ? 0.2198 1.6357 0.3768 0.0402  0.1095  0.3887  679  HOH A O   
4401 O  O   . HOH E .   ? 0.3329 0.1406 0.2856 -0.0290 -0.1166 -0.0564 680  HOH A O   
4402 O  O   . HOH E .   ? 0.1784 0.1901 0.1207 -0.0474 -0.0324 0.0652  681  HOH A O   
4403 O  O   . HOH E .   ? 0.0656 0.1094 0.0755 0.0002  -0.0014 -0.0059 682  HOH A O   
4404 O  O   . HOH E .   ? 0.1764 0.2727 0.1401 0.0332  0.0570  -0.0003 683  HOH A O   
4405 O  O   . HOH E .   ? 0.1156 0.1059 0.1917 -0.0147 0.0202  -0.0402 684  HOH A O   
4406 O  O   . HOH E .   ? 0.1725 0.2153 0.1799 0.0521  0.0367  0.0530  685  HOH A O   
4407 O  O   . HOH E .   ? 0.0857 0.0923 0.0663 -0.0083 0.0020  0.0115  686  HOH A O   
4408 O  O   . HOH E .   ? 0.3676 0.4165 0.3003 -0.0936 0.1613  0.0153  687  HOH A O   
4409 O  O   . HOH E .   ? 0.0980 0.0739 0.0683 0.0038  0.0015  0.0019  688  HOH A O   
4410 O  O   . HOH E .   ? 0.2724 0.1190 0.5565 0.0754  -0.1704 -0.1366 689  HOH A O   
4411 O  O   . HOH E .   ? 0.2998 0.2164 0.1622 -0.0356 -0.0303 0.0468  690  HOH A O   
4412 O  O   . HOH E .   ? 0.1289 0.0922 0.0734 0.0015  0.0015  0.0153  691  HOH A O   
4413 O  O   . HOH E .   ? 0.2409 0.1752 0.1782 -0.0426 -0.0079 0.0337  692  HOH A O   
4414 O  O   . HOH E .   ? 0.1420 0.1238 0.1847 -0.0098 0.0135  0.0131  693  HOH A O   
4415 O  O   A HOH E .   ? 0.0742 0.0873 0.0689 -0.0098 -0.0054 0.0138  694  HOH A O   
4416 O  O   B HOH E .   ? 0.1253 0.1146 0.0810 -0.0076 0.0070  -0.0222 694  HOH A O   
4417 O  O   . HOH E .   ? 0.0886 0.1101 0.1095 0.0041  0.0102  0.0054  695  HOH A O   
4418 O  O   A HOH E .   ? 0.3207 0.0851 0.2724 -0.0214 -0.0396 -0.0252 696  HOH A O   
4419 O  O   B HOH E .   ? 0.2531 0.1034 0.2649 -0.0093 0.0514  -0.0322 696  HOH A O   
4420 O  O   . HOH E .   ? 0.0657 0.1314 0.0760 0.0070  -0.0068 -0.0253 697  HOH A O   
4421 O  O   . HOH E .   ? 0.3173 0.2830 0.2407 0.1474  -0.0012 0.0721  698  HOH A O   
4422 O  O   . HOH E .   ? 0.1388 0.1162 0.1162 0.0318  0.0096  -0.0060 699  HOH A O   
4423 O  O   . HOH E .   ? 0.1295 0.4730 0.1331 0.0851  0.0035  -0.0726 700  HOH A O   
4424 O  O   . HOH E .   ? 0.0961 0.1470 0.0910 0.0241  0.0168  -0.0049 701  HOH A O   
4425 O  O   . HOH E .   ? 0.3419 0.5378 0.5194 -0.0176 0.1282  -0.2815 702  HOH A O   
4426 O  O   . HOH E .   ? 0.1621 0.1237 0.2111 0.0040  -0.0552 0.0355  703  HOH A O   
4427 O  O   . HOH E .   ? 0.1314 0.0825 0.1033 -0.0083 0.0236  0.0025  704  HOH A O   
4428 O  O   . HOH E .   ? 0.1882 0.1370 0.1362 0.0328  0.0383  0.0228  705  HOH A O   
4429 O  O   . HOH E .   ? 0.1163 0.1148 0.0785 0.0335  0.0082  -0.0029 706  HOH A O   
4430 O  O   . HOH E .   ? 0.2987 0.5662 0.3562 -0.0333 0.0241  -0.0689 707  HOH A O   
4431 O  O   . HOH E .   ? 0.1222 0.1733 0.0990 0.0297  0.0257  0.0118  708  HOH A O   
4432 O  O   . HOH E .   ? 0.2769 0.1722 0.2843 0.0417  -0.0503 -0.0499 709  HOH A O   
4433 O  O   . HOH E .   ? 0.2782 0.1821 0.1020 0.0083  0.0166  -0.0296 710  HOH A O   
4434 O  O   . HOH E .   ? 0.1157 0.2721 0.1750 -0.0511 -0.0326 0.0132  711  HOH A O   
4435 O  O   . HOH E .   ? 0.2011 0.5237 0.4453 0.0993  0.0083  0.2194  712  HOH A O   
4436 O  O   . HOH E .   ? 0.0990 0.1118 0.1225 0.0059  -0.0029 -0.0192 713  HOH A O   
4437 O  O   . HOH E .   ? 0.1132 0.1462 0.1151 0.0204  0.0081  0.0124  714  HOH A O   
4438 O  O   . HOH E .   ? 0.1174 0.1296 0.0931 0.0166  0.0105  -0.0005 715  HOH A O   
4439 O  O   . HOH E .   ? 0.0861 0.1090 0.0849 0.0054  -0.0051 -0.0052 716  HOH A O   
4440 O  O   . HOH E .   ? 0.1517 0.1729 0.0884 -0.0531 -0.0206 0.0075  717  HOH A O   
4441 O  O   . HOH E .   ? 0.3320 0.2240 0.5214 -0.1555 -0.1342 0.0154  718  HOH A O   
4442 O  O   . HOH E .   ? 0.1003 0.0736 0.0948 0.0092  0.0070  0.0177  719  HOH A O   
4443 O  O   . HOH E .   ? 0.2768 0.2000 0.8761 -0.0227 -0.0577 0.0884  720  HOH A O   
4444 O  O   . HOH E .   ? 0.3462 0.5816 0.1870 0.0689  -0.0115 0.1054  721  HOH A O   
4445 O  O   . HOH E .   ? 0.0861 0.1009 0.1289 0.0203  0.0008  -0.0101 722  HOH A O   
4446 O  O   . HOH E .   ? 0.4157 0.2525 0.4361 -0.0992 0.2400  -0.0846 723  HOH A O   
4447 O  O   . HOH E .   ? 0.3152 0.5589 0.1279 -0.2535 0.0265  0.0081  724  HOH A O   
4448 O  O   . HOH E .   ? 0.0863 0.1735 0.1186 0.0157  -0.0088 0.0178  725  HOH A O   
4449 O  O   . HOH E .   ? 0.1856 0.1418 0.2930 -0.0237 0.0105  -0.0216 726  HOH A O   
4450 O  O   . HOH E .   ? 0.0973 0.0962 0.0811 -0.0069 -0.0007 -0.0004 727  HOH A O   
4451 O  O   . HOH E .   ? 0.1763 0.1352 0.2987 -0.0131 0.0970  -0.0516 728  HOH A O   
4452 O  O   . HOH E .   ? 0.2045 0.3295 0.2447 0.0755  0.0119  -0.0472 729  HOH A O   
4453 O  O   . HOH E .   ? 0.3611 0.3306 0.8789 0.1440  0.3186  0.2042  730  HOH A O   
4454 O  O   . HOH E .   ? 0.2625 0.2077 0.1568 0.1047  0.0455  0.0237  731  HOH A O   
4455 O  O   . HOH E .   ? 0.2678 0.2048 0.3152 -0.0085 0.0682  -0.0647 732  HOH A O   
4456 O  O   . HOH E .   ? 0.1841 0.3921 0.3460 0.1210  -0.0612 0.0015  733  HOH A O   
4457 O  O   . HOH E .   ? 0.1218 0.2413 0.4154 -0.0135 -0.0281 0.0925  734  HOH A O   
4458 O  O   . HOH E .   ? 1.1386 0.8466 0.2389 -0.0532 0.3236  -0.1628 735  HOH A O   
4459 O  O   . HOH E .   ? 0.2460 0.2618 0.9262 -0.0446 -0.2277 0.2366  736  HOH A O   
4460 O  O   . HOH E .   ? 0.0823 0.1047 0.0886 -0.0238 -0.0080 -0.0026 737  HOH A O   
4461 O  O   A HOH E .   ? 0.1949 0.2682 0.1870 0.0757  -0.0392 -0.0813 738  HOH A O   
4462 O  O   B HOH E .   ? 0.2433 0.1649 0.0801 0.0234  -0.0251 0.0084  738  HOH A O   
4463 O  O   . HOH E .   ? 0.0674 0.0759 0.0614 -0.0068 -0.0040 0.0093  739  HOH A O   
4464 O  O   . HOH E .   ? 0.2029 0.2857 0.3324 0.0780  0.0008  0.0798  740  HOH A O   
4465 O  O   . HOH E .   ? 0.1093 0.0847 0.2184 -0.0050 0.0010  -0.0134 741  HOH A O   
4466 O  O   . HOH E .   ? 0.1873 0.5899 0.4403 -0.1264 0.0495  -0.2679 742  HOH A O   
4467 O  O   . HOH E .   ? 0.1081 0.1362 0.1039 -0.0017 0.0115  -0.0077 743  HOH A O   
4468 O  O   . HOH E .   ? 0.1773 0.2040 0.6287 0.0113  0.1197  0.0377  744  HOH A O   
4469 O  O   . HOH E .   ? 0.1411 0.1554 0.1434 0.0242  -0.0062 0.0042  745  HOH A O   
4470 O  O   . HOH E .   ? 0.0992 0.4161 0.2829 -0.0446 -0.0502 0.1040  746  HOH A O   
4471 O  O   . HOH E .   ? 0.1636 0.9251 0.3534 0.1937  0.0536  0.2641  747  HOH A O   
4472 O  O   . HOH E .   ? 0.1901 0.7081 0.1893 0.1419  -0.0472 -0.1994 748  HOH A O   
4473 O  O   . HOH E .   ? 0.1105 0.1230 0.0667 -0.0059 0.0065  0.0166  749  HOH A O   
4474 O  O   . HOH E .   ? 0.1327 0.2614 0.5117 0.0249  -0.0673 -0.2127 750  HOH A O   
4475 O  O   . HOH E .   ? 0.2815 0.5870 0.4086 0.2988  -0.1284 -0.1410 751  HOH A O   
4476 O  O   . HOH E .   ? 0.5323 0.1979 0.5986 -0.0208 0.3947  -0.1194 752  HOH A O   
4477 O  O   . HOH E .   ? 0.2905 0.1985 0.2029 0.0491  -0.0299 0.0857  753  HOH A O   
4478 O  O   . HOH E .   ? 0.1828 0.1425 0.5635 0.0180  0.0381  -0.0943 754  HOH A O   
4479 O  O   . HOH E .   ? 0.1166 0.0715 0.1101 0.0001  0.0091  0.0048  755  HOH A O   
4480 O  O   . HOH E .   ? 0.2228 0.2011 0.2244 0.0609  -0.0553 -0.0133 756  HOH A O   
4481 O  O   . HOH E .   ? 0.0807 0.1155 0.0647 -0.0108 -0.0008 0.0027  757  HOH A O   
4482 O  O   . HOH E .   ? 0.4752 0.3011 0.6958 0.1996  -0.3557 -0.2103 758  HOH A O   
4483 O  O   . HOH E .   ? 1.1703 0.3631 0.2543 0.2486  -0.0052 0.0973  759  HOH A O   
4484 O  O   . HOH E .   ? 0.0980 0.1012 0.0657 0.0075  -0.0035 0.0116  760  HOH A O   
4485 O  O   . HOH E .   ? 0.4544 0.7792 0.2502 -0.2921 -0.0717 -0.0452 761  HOH A O   
4486 O  O   . HOH E .   ? 0.1687 0.5373 0.3971 -0.0183 0.0099  0.0533  762  HOH A O   
4487 O  O   . HOH E .   ? 0.1474 0.1274 0.1083 0.0066  0.0355  0.0258  763  HOH A O   
4488 O  O   . HOH E .   ? 0.2858 0.6496 0.4480 0.1020  -0.1006 -0.0616 764  HOH A O   
4489 O  O   . HOH E .   ? 0.6518 0.4452 0.1987 0.2670  0.0625  0.1061  765  HOH A O   
4490 O  O   . HOH E .   ? 0.3036 0.1655 0.2644 0.0673  0.0228  -0.0755 766  HOH A O   
4491 O  O   . HOH E .   ? 0.5494 0.2883 0.2379 -0.0732 -0.1270 -0.0337 767  HOH A O   
4492 O  O   . HOH E .   ? 0.1765 0.1871 0.1480 0.0130  0.0056  -0.0246 768  HOH A O   
4493 O  O   . HOH E .   ? 0.2982 0.1496 0.2263 0.0761  0.0471  0.0234  769  HOH A O   
4494 O  O   . HOH E .   ? 0.0878 0.0797 0.0710 -0.0060 -0.0073 0.0036  770  HOH A O   
4495 O  O   . HOH E .   ? 0.4067 0.4592 1.0343 -0.2002 -0.3964 0.2724  771  HOH A O   
4496 O  O   . HOH E .   ? 0.3421 0.0914 0.2605 0.0236  0.0520  -0.0041 772  HOH A O   
4497 O  O   . HOH E .   ? 0.2724 0.5091 0.5811 -0.1026 0.1891  -0.0837 773  HOH A O   
4498 O  O   A HOH E .   ? 0.1715 0.1487 0.2225 0.0556  -0.0624 -0.0516 774  HOH A O   
4499 O  O   B HOH E .   ? 0.1112 0.0704 0.2033 0.0164  -0.0043 -0.0203 774  HOH A O   
4500 O  O   . HOH E .   ? 0.1480 0.1497 0.1385 0.0091  0.0336  -0.0365 775  HOH A O   
4501 O  O   . HOH E .   ? 0.4937 0.2021 0.5712 -0.0554 0.1971  0.0552  776  HOH A O   
4502 O  O   . HOH E .   ? 0.0925 0.0771 0.0951 -0.0019 -0.0084 0.0003  777  HOH A O   
4503 O  O   . HOH E .   ? 0.1578 0.6231 0.3164 0.0155  0.0266  -0.1183 778  HOH A O   
4504 O  O   . HOH E .   ? 0.2375 0.1671 0.2579 0.0413  -0.0506 -0.0574 779  HOH A O   
4505 O  O   . HOH E .   ? 0.1179 0.0931 0.1439 0.0038  0.0084  0.0148  780  HOH A O   
4506 O  O   . HOH E .   ? 0.8680 0.2709 0.2888 -0.2393 0.1920  0.0196  781  HOH A O   
4507 O  O   . HOH E .   ? 0.5492 0.4175 0.8228 0.1004  -0.3975 -0.1099 782  HOH A O   
4508 O  O   . HOH E .   ? 0.4172 0.2228 0.7932 0.1515  0.0592  -0.0074 783  HOH A O   
4509 O  O   . HOH E .   ? 0.1011 0.1168 0.0858 -0.0230 -0.0118 0.0286  784  HOH A O   
4510 O  O   . HOH E .   ? 0.1189 0.1353 0.0981 -0.0213 0.0157  0.0074  785  HOH A O   
4511 O  O   . HOH E .   ? 0.1915 0.1738 0.1439 -0.0091 -0.0388 -0.0267 786  HOH A O   
4512 O  O   . HOH E .   ? 0.2186 0.2073 0.4623 0.0982  -0.0022 0.0457  787  HOH A O   
4513 O  O   . HOH E .   ? 0.2331 0.4473 0.1092 -0.0884 0.0107  0.0328  788  HOH A O   
4514 O  O   . HOH E .   ? 0.1402 0.3640 0.1621 -0.0792 0.0247  0.0019  789  HOH A O   
4515 O  O   . HOH E .   ? 0.0987 0.1156 0.1072 -0.0278 0.0012  -0.0098 790  HOH A O   
4516 O  O   . HOH E .   ? 0.3139 0.2618 0.2561 -0.1510 0.0233  0.0051  791  HOH A O   
4517 O  O   . HOH E .   ? 0.0770 0.0847 0.0636 -0.0045 -0.0079 -0.0057 792  HOH A O   
4518 O  O   . HOH E .   ? 0.3045 0.4819 0.3364 0.2036  -0.1135 -0.2143 793  HOH A O   
4519 O  O   . HOH E .   ? 0.1938 0.1691 0.5770 -0.0052 -0.2162 -0.0683 794  HOH A O   
4520 O  O   . HOH E .   ? 0.0891 0.1288 0.1159 -0.0078 -0.0065 0.0034  795  HOH A O   
4521 O  O   . HOH E .   ? 0.4356 0.1986 0.1741 0.0982  0.0718  0.0020  796  HOH A O   
4522 O  O   . HOH E .   ? 0.1502 0.2097 0.1159 -0.0004 0.0191  -0.0277 797  HOH A O   
4523 O  O   . HOH E .   ? 0.2954 0.3332 0.2175 0.1395  -0.0392 -0.0549 798  HOH A O   
4524 O  O   A HOH E .   ? 0.3316 0.0711 0.0593 -0.0015 -0.0405 -0.0116 799  HOH A O   
4525 O  O   B HOH E .   ? 0.0714 0.0377 0.1023 0.0004  -0.0188 -0.0171 799  HOH A O   
4526 O  O   . HOH E .   ? 0.3190 0.2738 0.3592 0.1129  -0.0692 -0.0391 800  HOH A O   
4527 O  O   . HOH E .   ? 0.0864 0.0991 0.1280 0.0053  0.0311  -0.0179 801  HOH A O   
4528 O  O   . HOH E .   ? 0.3867 0.2807 0.4363 -0.1054 -0.1141 0.0815  802  HOH A O   
4529 O  O   . HOH E .   ? 0.2050 0.1728 0.1616 -0.0283 0.0010  0.0017  803  HOH A O   
4530 O  O   . HOH E .   ? 0.3403 0.3420 0.3586 0.0302  -0.2404 0.0419  804  HOH A O   
4531 O  O   . HOH E .   ? 0.6199 0.3340 0.6316 0.0358  -0.3994 0.1081  805  HOH A O   
4532 O  O   . HOH E .   ? 0.2621 0.1298 0.1100 0.0514  -0.0181 -0.0030 806  HOH A O   
4533 O  O   . HOH E .   ? 0.1483 0.1647 0.1053 0.0173  -0.0049 -0.0117 807  HOH A O   
4534 O  O   . HOH E .   ? 0.3250 0.1828 0.1221 -0.1099 0.0110  0.0190  808  HOH A O   
4535 O  O   . HOH E .   ? 0.2276 0.2306 0.1908 -0.0354 0.0198  -0.0642 809  HOH A O   
4536 O  O   . HOH E .   ? 0.2659 0.1259 0.1415 0.0105  0.0271  -0.0277 810  HOH A O   
4537 O  O   . HOH E .   ? 0.3236 0.2981 0.3062 0.0162  0.0842  -0.0278 811  HOH A O   
4538 O  O   . HOH E .   ? 0.1271 0.1285 0.0990 0.0113  0.0293  -0.0022 812  HOH A O   
4539 O  O   A HOH E .   ? 0.4006 0.1706 0.1162 0.0912  -0.1200 -0.0602 813  HOH A O   
4540 O  O   B HOH E .   ? 0.3378 0.4529 0.2478 0.0189  -0.1494 -0.1624 813  HOH A O   
4541 O  O   . HOH E .   ? 0.0751 0.0903 0.0893 0.0058  0.0078  0.0067  814  HOH A O   
4542 O  O   . HOH E .   ? 0.5560 0.8910 0.2960 -0.3838 -0.0704 0.2208  815  HOH A O   
4543 O  O   . HOH E .   ? 0.5196 0.2343 0.3611 0.0131  -0.0482 -0.0702 816  HOH A O   
4544 O  O   . HOH E .   ? 0.2283 0.1174 0.0826 -0.0128 0.0144  -0.0132 817  HOH A O   
4545 O  O   . HOH E .   ? 0.1448 0.2955 0.1485 0.0673  -0.0165 -0.0613 818  HOH A O   
4546 O  O   . HOH E .   ? 0.1955 0.1572 0.1492 -0.0229 -0.0225 -0.0049 819  HOH A O   
4547 O  O   . HOH E .   ? 0.1824 0.2816 0.0863 -0.0850 -0.0042 -0.0046 820  HOH A O   
4548 O  O   . HOH E .   ? 0.2038 0.2582 0.1749 -0.0105 0.0697  0.0015  821  HOH A O   
4549 O  O   . HOH E .   ? 0.9519 0.2041 0.2125 0.0846  -0.0587 0.0541  822  HOH A O   
4550 O  O   . HOH E .   ? 0.4398 0.1785 0.2372 -0.0983 -0.0537 -0.0250 823  HOH A O   
4551 O  O   . HOH E .   ? 0.1734 0.3306 0.2428 -0.0714 0.0342  -0.0250 824  HOH A O   
4552 O  O   . HOH E .   ? 0.2666 0.1315 0.1755 0.0245  -0.0428 -0.0063 825  HOH A O   
4553 O  O   . HOH E .   ? 0.4892 0.3412 0.2024 -0.1090 -0.0484 0.0773  826  HOH A O   
4554 O  O   . HOH E .   ? 0.0914 0.1497 0.1519 0.0047  -0.0070 -0.0038 827  HOH A O   
4555 O  O   . HOH E .   ? 0.4265 0.3942 0.4283 0.0491  -0.1102 -0.0519 828  HOH A O   
4556 O  O   . HOH E .   ? 0.1510 0.3126 0.2359 -0.0142 -0.0381 0.0306  829  HOH A O   
4557 O  O   . HOH E .   ? 0.1664 0.2833 0.2978 0.0358  -0.0573 0.0161  830  HOH A O   
4558 O  O   . HOH E .   ? 0.2580 0.1387 0.1830 -0.0105 -0.0135 0.0171  831  HOH A O   
4559 O  O   . HOH E .   ? 0.1256 0.2585 0.1052 -0.0760 0.0131  -0.0725 832  HOH A O   
4560 O  O   . HOH E .   ? 0.3083 0.3735 0.4485 -0.1269 0.0195  0.1447  833  HOH A O   
4561 O  O   A HOH E .   ? 0.1220 0.2042 0.3804 0.0502  0.0778  0.0798  834  HOH A O   
4562 O  O   B HOH E .   ? 0.1283 0.1735 0.2299 -0.0150 0.0112  0.0456  834  HOH A O   
4563 O  O   . HOH E .   ? 0.2123 0.1461 0.3572 0.0171  -0.1215 -0.0635 835  HOH A O   
4564 O  O   . HOH E .   ? 0.5055 0.2754 0.2712 -0.1777 0.0615  -0.1033 836  HOH A O   
4565 O  O   . HOH E .   ? 0.4476 0.2513 0.8203 -0.0888 0.1013  0.2642  837  HOH A O   
4566 O  O   . HOH E .   ? 0.1594 0.1458 0.3645 -0.0295 -0.0439 0.0769  838  HOH A O   
4567 O  O   . HOH E .   ? 0.1993 0.6625 0.2651 0.1154  0.0784  -0.1078 839  HOH A O   
4568 O  O   . HOH E .   ? 0.1634 0.2367 0.1315 -0.0529 -0.0289 -0.0282 840  HOH A O   
4569 O  O   . HOH E .   ? 0.4902 0.2325 0.2327 0.0441  -0.0093 0.0197  841  HOH A O   
4570 O  O   . HOH E .   ? 0.1642 0.1472 0.1505 0.0403  -0.0179 -0.0163 842  HOH A O   
4571 O  O   . HOH E .   ? 0.4375 0.3006 0.2816 0.0370  0.0394  -0.0821 843  HOH A O   
4572 O  O   . HOH E .   ? 0.1448 0.1230 0.2190 0.0174  -0.0616 -0.0472 844  HOH A O   
4573 O  O   . HOH E .   ? 0.1793 0.3529 0.2823 -0.0795 0.0234  -0.1776 845  HOH A O   
4574 O  O   . HOH E .   ? 0.3719 0.4467 0.4782 -0.0650 0.1665  -0.2446 846  HOH A O   
4575 O  O   . HOH E .   ? 0.1347 0.2038 0.1676 -0.0310 0.0225  0.0038  847  HOH A O   
4576 O  O   . HOH E .   ? 0.3903 0.8534 0.4667 0.4175  -0.2319 -0.3597 848  HOH A O   
4577 O  O   . HOH E .   ? 0.2886 0.2733 0.2615 -0.0167 0.0407  0.0385  849  HOH A O   
4578 O  O   . HOH E .   ? 0.2590 0.2849 0.5542 -0.0126 0.1935  -0.0555 850  HOH A O   
4579 O  O   A HOH E .   ? 0.3527 0.1477 0.2620 -0.0593 -0.2140 0.0380  851  HOH A O   
4580 O  O   B HOH E .   ? 0.5745 0.2578 0.3250 0.0047  -0.0413 -0.1396 851  HOH A O   
4581 O  O   . HOH E .   ? 0.2454 0.3372 0.1954 0.1571  -0.1010 -0.1610 852  HOH A O   
4582 O  O   . HOH E .   ? 1.3589 0.1704 0.2163 -0.2104 -0.0506 -0.0225 853  HOH A O   
4583 O  O   . HOH E .   ? 0.4148 0.5546 0.2135 0.2613  0.0520  -0.0200 854  HOH A O   
4584 O  O   . HOH E .   ? 0.2679 0.2541 0.2085 -0.0879 -0.0533 0.0232  855  HOH A O   
4585 O  O   . HOH E .   ? 0.6004 0.5767 0.8459 -0.3958 -0.3737 0.4521  856  HOH A O   
4586 O  O   . HOH E .   ? 0.6503 0.1551 0.3479 -0.0800 -0.2337 -0.0239 857  HOH A O   
4587 O  O   . HOH E .   ? 0.6588 0.1516 0.3163 0.0121  -0.1033 0.0161  858  HOH A O   
4588 O  O   . HOH E .   ? 0.1567 0.1240 0.1375 0.0173  0.0114  0.0174  859  HOH A O   
4589 O  O   . HOH E .   ? 0.2988 0.2175 0.3996 -0.0147 -0.1423 0.0343  860  HOH A O   
4590 O  O   . HOH E .   ? 0.1757 0.1411 0.1346 0.0192  0.0036  -0.0158 861  HOH A O   
4591 O  O   . HOH E .   ? 0.2445 0.1374 0.1197 0.0226  0.0526  0.0448  862  HOH A O   
4592 O  O   . HOH E .   ? 0.2306 0.1150 0.2387 0.0128  0.0803  0.0114  863  HOH A O   
4593 O  O   A HOH E .   ? 0.2576 0.1059 0.2601 0.0699  -0.0091 0.0404  864  HOH A O   
4594 O  O   B HOH E .   ? 0.1950 0.1495 0.3278 -0.0055 -0.1079 0.0461  864  HOH A O   
4595 O  O   . HOH E .   ? 0.5763 0.1124 0.4058 -0.0827 0.2686  -0.0202 865  HOH A O   
4596 O  O   . HOH E .   ? 1.2932 0.3471 0.2787 0.1031  -0.0025 0.0105  866  HOH A O   
4597 O  O   . HOH E .   ? 0.2606 0.2189 0.2729 0.0068  -0.0244 0.0924  867  HOH A O   
4598 O  O   . HOH E .   ? 0.3757 0.6520 0.4375 0.1766  0.1907  0.0201  868  HOH A O   
4599 O  O   . HOH E .   ? 0.1086 0.1471 0.1680 -0.0209 0.0203  0.0254  869  HOH A O   
4600 O  O   . HOH E .   ? 0.2422 0.2417 0.2060 -0.0480 -0.0373 0.0164  870  HOH A O   
4601 O  O   . HOH E .   ? 0.8260 0.5670 0.5274 0.2821  0.2899  0.0551  871  HOH A O   
4602 O  O   . HOH E .   ? 0.5604 0.3098 0.5215 -0.1873 -0.1110 0.0927  872  HOH A O   
4603 O  O   . HOH E .   ? 0.1157 0.1156 0.0948 0.0057  0.0076  0.0016  873  HOH A O   
4604 O  O   . HOH E .   ? 0.2622 0.2366 0.3632 0.0104  -0.0614 0.0236  874  HOH A O   
4605 O  O   . HOH E .   ? 0.1899 0.3365 0.1551 0.0903  0.0027  -0.0390 875  HOH A O   
4606 O  O   . HOH E .   ? 0.5302 0.4393 0.2564 0.2346  -0.1558 -0.1471 876  HOH A O   
4607 O  O   . HOH E .   ? 0.4157 0.4441 0.7349 0.1613  -0.1217 -0.4000 877  HOH A O   
4608 O  O   . HOH E .   ? 0.2931 0.3384 0.3962 -0.1555 0.1099  -0.0447 878  HOH A O   
4609 O  O   . HOH E .   ? 0.6788 0.2370 1.2612 0.0277  -0.1941 0.0439  879  HOH A O   
4610 O  O   . HOH E .   ? 0.1261 0.1477 0.2031 0.0198  -0.0077 -0.0172 880  HOH A O   
4611 O  O   . HOH E .   ? 0.9057 0.3385 0.3661 -0.3227 -0.2651 0.1609  881  HOH A O   
4612 O  O   . HOH E .   ? 0.5598 0.6376 0.6686 -0.4000 0.1174  -0.2684 882  HOH A O   
4613 O  O   . HOH E .   ? 0.1186 0.1375 0.0888 0.0104  0.0167  0.0159  883  HOH A O   
4614 O  O   . HOH E .   ? 0.4683 0.2815 0.2061 0.0782  -0.0446 0.0091  884  HOH A O   
4615 O  O   . HOH E .   ? 0.6490 0.3932 0.3340 0.2937  0.1544  0.0834  885  HOH A O   
4616 O  O   . HOH E .   ? 0.2314 1.3386 1.4133 -0.0489 -0.1651 0.0826  886  HOH A O   
4617 O  O   . HOH E .   ? 0.6090 0.6294 0.3686 -0.3332 0.2370  -0.1316 887  HOH A O   
4618 O  O   . HOH E .   ? 0.3823 0.3221 0.3715 0.1255  -0.0256 -0.0836 888  HOH A O   
4619 O  O   . HOH E .   ? 0.5792 0.4390 0.6256 -0.0979 0.0641  0.1884  889  HOH A O   
4620 O  O   . HOH E .   ? 0.6066 0.3851 0.7080 0.0685  0.1695  0.2927  890  HOH A O   
4621 O  O   . HOH E .   ? 0.3833 0.3351 0.4134 0.1301  -0.1100 0.0415  891  HOH A O   
4622 O  O   . HOH E .   ? 0.4952 0.1985 0.6053 -0.1164 -0.0777 -0.0036 892  HOH A O   
4623 O  O   . HOH E .   ? 0.9123 0.4713 0.3815 -0.4000 -0.0106 -0.1191 893  HOH A O   
4624 O  O   . HOH E .   ? 0.6426 0.3040 0.7302 -0.2237 0.0792  -0.0275 894  HOH A O   
4625 O  O   . HOH E .   ? 0.9972 0.2426 0.4984 -0.2687 -0.1296 0.0619  895  HOH A O   
4626 O  O   . HOH E .   ? 0.0801 0.1141 0.1099 0.0013  -0.0007 -0.0297 896  HOH A O   
4627 O  O   . HOH E .   ? 0.5745 0.9315 0.7726 0.0168  -0.4000 -0.2219 897  HOH A O   
4628 O  O   . HOH E .   ? 0.3355 0.1481 0.1362 0.0724  -0.0042 -0.0097 898  HOH A O   
4629 O  O   . HOH E .   ? 0.2054 0.3280 1.0215 0.0562  0.0393  0.0244  899  HOH A O   
4630 O  O   . HOH E .   ? 0.2481 0.4899 0.4803 0.0522  0.1502  0.0010  900  HOH A O   
4631 O  O   A HOH E .   ? 0.1235 0.1029 0.1640 -0.0098 -0.0067 0.0017  901  HOH A O   
4632 O  O   B HOH E .   ? 0.0482 0.1527 0.0670 -0.0480 0.0140  0.0093  901  HOH A O   
4633 O  O   . HOH E .   ? 0.2293 0.1958 0.2431 -0.0315 0.0114  -0.0025 902  HOH A O   
4634 O  O   . HOH E .   ? 0.7704 0.3584 0.2306 -0.1528 0.0770  -0.0144 903  HOH A O   
4635 O  O   . HOH E .   ? 0.1553 0.1536 0.2281 -0.0118 -0.0372 0.0081  904  HOH A O   
4636 O  O   . HOH E .   ? 0.7595 0.1410 0.9420 0.1332  -0.4000 -0.1395 905  HOH A O   
4637 O  O   . HOH E .   ? 0.2991 0.2609 0.2539 -0.0191 -0.0044 -0.0374 906  HOH A O   
4638 O  O   . HOH E .   ? 0.3140 0.2666 0.2620 -0.0986 -0.1045 -0.0366 907  HOH A O   
4639 O  O   . HOH E .   ? 0.1450 0.1831 0.1552 0.0050  -0.0195 0.0076  908  HOH A O   
4640 O  O   . HOH E .   ? 0.2024 0.2105 0.6316 -0.0166 -0.0425 0.0897  909  HOH A O   
4641 O  O   . HOH E .   ? 0.6830 0.2601 0.3683 -0.2156 -0.2743 0.1149  910  HOH A O   
4642 O  O   . HOH E .   ? 0.5728 0.1924 0.6732 -0.0293 0.2311  -0.0432 911  HOH A O   
4643 O  O   . HOH E .   ? 0.2929 0.3422 0.4536 0.0556  0.1372  -0.0025 912  HOH A O   
4644 O  O   . HOH E .   ? 0.8961 0.4023 0.3827 -0.0523 -0.3754 0.0515  913  HOH A O   
4645 O  O   . HOH E .   ? 0.3341 0.2088 0.2752 -0.0623 0.0815  -0.0263 914  HOH A O   
4646 O  O   . HOH E .   ? 0.2421 0.1841 0.7532 0.0196  -0.0591 -0.0110 915  HOH A O   
4647 O  O   . HOH E .   ? 0.5157 0.6961 0.5225 -0.2979 -0.2079 0.2547  916  HOH A O   
4648 O  O   . HOH E .   ? 0.2150 1.0391 0.9305 0.1074  0.1369  -0.2597 917  HOH A O   
4649 O  O   . HOH E .   ? 0.2144 0.5541 0.5759 0.1177  -0.1578 -0.3969 918  HOH A O   
4650 O  O   . HOH E .   ? 0.1780 0.2933 0.3979 -0.0163 0.0347  -0.0284 919  HOH A O   
4651 O  O   . HOH E .   ? 0.1386 0.5690 0.7142 -0.0150 0.0375  -0.3652 920  HOH A O   
4652 O  O   . HOH E .   ? 0.2874 0.2449 0.4950 -0.0430 -0.0951 -0.0134 921  HOH A O   
4653 O  O   . HOH E .   ? 0.4038 0.6176 0.5942 0.0340  0.1061  0.3518  922  HOH A O   
4654 O  O   . HOH E .   ? 0.5720 0.3447 0.3260 0.2751  -0.1769 0.0122  923  HOH A O   
4655 O  O   . HOH E .   ? 0.2550 0.8542 0.5481 0.0827  -0.0409 -0.3757 924  HOH A O   
4656 O  O   . HOH E .   ? 0.3138 0.8158 0.3960 0.2808  -0.1256 -0.3658 925  HOH A O   
4657 O  O   . HOH E .   ? 0.3627 0.7480 0.3535 0.2935  0.1077  0.1662  926  HOH A O   
4658 O  O   . HOH E .   ? 0.3851 0.4455 0.2514 -0.1187 -0.0966 0.1987  927  HOH A O   
4659 O  O   . HOH E .   ? 0.8108 0.3158 0.5572 0.1063  -0.4000 -0.0171 928  HOH A O   
4660 O  O   . HOH E .   ? 0.4681 0.1487 0.1704 0.0089  -0.1649 -0.0002 929  HOH A O   
4661 O  O   . HOH E .   ? 0.2134 0.1471 0.1083 0.0160  0.0166  -0.0002 930  HOH A O   
4662 O  O   . HOH E .   ? 0.8580 0.2999 0.2873 0.0815  -0.0989 -0.1006 931  HOH A O   
4663 O  O   . HOH E .   ? 0.4194 0.5505 0.4895 -0.0828 -0.1809 0.1641  932  HOH A O   
4664 O  O   . HOH E .   ? 0.4798 0.3125 0.6459 -0.0550 -0.4000 -0.0082 933  HOH A O   
4665 O  O   . HOH E .   ? 0.1974 0.1937 0.2197 -0.0089 0.0109  0.0223  934  HOH A O   
4666 O  O   . HOH E .   ? 0.3256 0.2992 0.4883 -0.0163 0.0218  -0.0671 935  HOH A O   
4667 O  O   . HOH E .   ? 0.3435 0.1805 0.4308 -0.0504 0.2146  -0.0128 936  HOH A O   
4668 O  O   A HOH E .   ? 0.0886 0.1002 0.1012 -0.0020 0.0166  -0.0006 937  HOH A O   
4669 O  O   B HOH E .   ? 0.3934 0.1530 0.1080 0.1310  0.0818  0.0423  937  HOH A O   
4670 O  O   . HOH E .   ? 0.1151 0.1835 0.2201 -0.0210 0.0056  0.0453  938  HOH A O   
4671 O  O   . HOH E .   ? 0.4018 0.3411 0.4987 0.1840  -0.1403 -0.1157 939  HOH A O   
4672 O  O   . HOH E .   ? 0.4543 0.2835 0.3600 -0.0582 0.0127  -0.0441 940  HOH A O   
4673 O  O   . HOH E .   ? 0.5607 0.4773 0.4018 0.0848  0.2836  0.0456  941  HOH A O   
4674 O  O   . HOH E .   ? 0.2388 0.2391 0.2019 0.0035  0.0648  -0.0505 942  HOH A O   
4675 O  O   . HOH E .   ? 1.1427 0.5126 0.4266 -0.3109 0.0598  0.0756  943  HOH A O   
4676 O  O   . HOH E .   ? 0.4886 0.6213 0.7216 -0.0952 -0.0866 0.4540  944  HOH A O   
4677 O  O   . HOH E .   ? 0.6500 0.3457 0.9910 -0.2207 -0.0486 -0.2138 945  HOH A O   
4678 O  O   . HOH E .   ? 0.1959 0.2385 0.3048 -0.0239 0.0468  -0.0229 946  HOH A O   
4679 O  O   . HOH E .   ? 0.4426 0.3373 0.4926 -0.1797 -0.1771 0.1391  947  HOH A O   
4680 O  O   . HOH E .   ? 0.4272 0.3120 0.4246 0.0097  0.0776  -0.1820 948  HOH A O   
4681 O  O   . HOH E .   ? 0.2980 0.1118 0.1091 0.0720  0.0629  0.0319  949  HOH A O   
4682 O  O   . HOH E .   ? 0.1887 0.1364 0.1468 -0.0194 0.0121  0.0010  950  HOH A O   
4683 O  O   . HOH E .   ? 0.1296 0.3005 0.2391 0.0314  0.0262  -0.0006 951  HOH A O   
4684 O  O   . HOH E .   ? 0.1611 0.4180 0.1492 -0.0416 -0.0062 -0.0963 952  HOH A O   
4685 O  O   . HOH E .   ? 0.3054 0.5633 0.5325 0.0078  -0.0100 -0.3638 953  HOH A O   
4686 O  O   . HOH E .   ? 0.2703 0.2378 0.7062 0.0051  0.0790  -0.0746 954  HOH A O   
4687 O  O   . HOH E .   ? 0.2616 0.1515 0.1882 0.0279  0.1174  0.0271  955  HOH A O   
4688 O  O   . HOH E .   ? 0.6662 0.5249 0.3166 0.2798  -0.1958 -0.0850 956  HOH A O   
4689 O  O   . HOH E .   ? 0.4011 0.3900 0.3543 0.0432  -0.0437 0.1876  957  HOH A O   
4690 O  O   . HOH E .   ? 0.4068 0.3635 0.2279 0.0151  0.1586  0.0756  958  HOH A O   
4691 O  O   . HOH E .   ? 1.1465 0.9719 0.4413 0.1610  0.2605  0.3265  959  HOH A O   
4692 O  O   . HOH E .   ? 0.4753 0.5913 0.8624 -0.1644 0.2598  -0.2355 960  HOH A O   
4693 O  O   . HOH E .   ? 0.1821 0.3829 0.2670 -0.0624 -0.0643 0.0344  961  HOH A O   
4694 O  O   . HOH E .   ? 0.4812 0.1719 0.1292 -0.1354 -0.0114 -0.0054 962  HOH A O   
4695 O  O   . HOH E .   ? 0.3024 0.8139 0.2665 -0.2604 0.0075  0.0777  963  HOH A O   
4696 O  O   A HOH E .   ? 0.3270 0.4903 0.4002 -0.1774 0.1950  -0.2447 964  HOH A O   
4697 O  O   B HOH E .   ? 0.3721 0.4099 0.3133 -0.0125 0.1989  -0.0391 964  HOH A O   
4698 O  O   . HOH E .   ? 0.8318 0.6147 0.5104 0.1869  0.1941  0.3730  965  HOH A O   
4699 O  O   . HOH E .   ? 0.2394 0.2342 0.1764 -0.0335 0.0083  -0.0194 966  HOH A O   
4700 O  O   . HOH E .   ? 0.1181 0.1145 0.0962 0.0038  0.0022  0.0039  967  HOH A O   
4701 O  O   . HOH E .   ? 0.6049 0.2880 0.3235 0.1245  0.0560  0.0581  968  HOH A O   
4702 O  O   . HOH E .   ? 0.4049 0.3130 0.3685 -0.0319 0.2080  -0.0266 969  HOH A O   
4703 O  O   . HOH E .   ? 0.3128 0.2428 0.3381 -0.0226 0.0399  -0.0409 970  HOH A O   
4704 O  O   . HOH E .   ? 0.5244 0.4554 0.5476 0.2171  -0.0573 -0.1098 971  HOH A O   
4705 O  O   . HOH E .   ? 0.4108 0.2249 0.3079 0.0683  -0.0424 0.0166  972  HOH A O   
4706 O  O   . HOH E .   ? 0.2995 0.4377 0.4750 -0.1248 0.0653  -0.2385 973  HOH A O   
4707 O  O   . HOH E .   ? 0.6198 0.4494 0.5839 0.1410  -0.3893 0.0890  974  HOH A O   
4708 O  O   . HOH E .   ? 0.3937 0.8479 0.2577 -0.4000 -0.0792 0.2637  975  HOH A O   
4709 O  O   . HOH E .   ? 0.2740 0.3366 0.4826 -0.0297 0.0153  0.0049  976  HOH A O   
4710 O  O   . HOH E .   ? 0.2275 0.7450 0.6596 -0.0926 0.1286  0.1213  977  HOH A O   
4711 O  O   . HOH E .   ? 0.3692 0.2633 0.3002 0.0249  0.0024  -0.0238 978  HOH A O   
4712 O  O   A HOH E .   ? 0.1857 0.1154 0.0763 0.0512  -0.0473 -0.0314 979  HOH A O   
4713 O  O   B HOH E .   ? 0.1001 0.0320 0.1293 -0.0130 -0.0360 0.0059  979  HOH A O   
4714 O  O   . HOH E .   ? 0.2613 0.2684 0.3365 0.0672  -0.0501 0.0230  980  HOH A O   
4715 O  O   . HOH E .   ? 0.4454 0.5257 0.9067 0.3058  -0.2454 -0.4000 981  HOH A O   
4716 O  O   . HOH E .   ? 0.5273 0.2890 0.4938 0.0820  0.2451  -0.0178 982  HOH A O   
4717 O  O   . HOH E .   ? 0.2437 0.4659 0.4026 0.0134  0.0985  0.1346  983  HOH A O   
4718 O  O   . HOH E .   ? 0.4462 0.6305 0.2393 0.0799  -0.0663 -0.2241 984  HOH A O   
4719 O  O   . HOH E .   ? 0.2835 0.4256 0.6897 -0.1696 -0.0977 0.0754  985  HOH A O   
4720 O  O   . HOH E .   ? 0.2694 0.5867 0.2697 0.2060  -0.0059 0.0000  986  HOH A O   
4721 O  O   . HOH E .   ? 0.1930 0.4018 0.2343 0.0272  -0.0734 -0.0614 987  HOH A O   
4722 O  O   . HOH E .   ? 0.2822 0.3149 0.1848 0.0175  -0.0248 -0.0191 988  HOH A O   
4723 O  O   . HOH E .   ? 0.4704 0.5554 0.2500 -0.1157 0.0816  -0.1876 989  HOH A O   
4724 O  O   . HOH E .   ? 0.4397 0.2105 0.2451 -0.1148 0.1696  -0.0541 990  HOH A O   
4725 O  O   . HOH E .   ? 0.3018 0.2397 1.4917 0.0239  -0.1785 -0.2512 991  HOH A O   
4726 O  O   . HOH E .   ? 0.2729 0.5666 0.3363 0.1896  -0.0789 -0.1098 992  HOH A O   
4727 O  O   . HOH E .   ? 0.3821 0.3508 0.4131 0.0470  0.0610  0.0594  993  HOH A O   
4728 O  O   . HOH E .   ? 0.4742 0.1919 0.5182 0.1017  -0.3390 -0.1401 994  HOH A O   
4729 O  O   . HOH E .   ? 0.4163 0.3475 0.7509 0.2410  -0.1659 -0.2629 995  HOH A O   
4730 O  O   . HOH E .   ? 0.1425 0.1439 0.1509 0.0103  0.0002  -0.0394 996  HOH A O   
4731 O  O   . HOH E .   ? 0.1726 0.2707 0.2525 0.0261  -0.0306 -0.1042 997  HOH A O   
4732 O  O   . HOH E .   ? 0.6371 0.3478 0.7761 0.1745  0.1855  0.2007  998  HOH A O   
4733 O  O   . HOH E .   ? 0.6402 0.4318 0.5247 0.0959  -0.0246 0.2518  999  HOH A O   
4734 O  O   . HOH E .   ? 0.1552 0.4951 0.5516 -0.0529 0.0134  -0.2302 1000 HOH A O   
4735 O  O   . HOH E .   ? 0.5325 0.2536 0.2225 -0.0624 0.0226  0.0023  1001 HOH A O   
4736 O  O   . HOH E .   ? 0.2829 0.2955 0.1996 0.0750  0.0292  -0.0119 1002 HOH A O   
4737 O  O   . HOH E .   ? 0.5469 0.4377 0.4026 -0.0495 -0.0963 0.1052  1003 HOH A O   
4738 O  O   . HOH E .   ? 0.6736 0.6570 0.3037 0.3273  0.0897  -0.1187 1004 HOH A O   
4739 O  O   . HOH E .   ? 0.1362 0.3073 0.1958 0.0434  0.0017  0.0118  1005 HOH A O   
4740 O  O   . HOH E .   ? 0.2239 0.6671 0.4230 0.2043  -0.1293 -0.2306 1006 HOH A O   
4741 O  O   . HOH E .   ? 0.9237 0.9306 0.2870 0.0115  0.2576  0.0943  1007 HOH A O   
4742 O  O   . HOH E .   ? 0.1795 0.2275 0.2016 -0.0265 0.0186  -0.0272 1008 HOH A O   
4743 O  O   . HOH E .   ? 0.7388 0.3325 0.6171 0.0100  -0.2120 0.1405  1009 HOH A O   
4744 O  O   . HOH E .   ? 0.2197 0.3183 0.3374 -0.0001 -0.1212 -0.0156 1010 HOH A O   
4745 O  O   . HOH E .   ? 0.6368 0.4286 0.3683 -0.2392 0.1805  -0.1508 1011 HOH A O   
4746 O  O   . HOH E .   ? 0.1955 0.1869 0.1395 0.0044  -0.0296 -0.0282 1012 HOH A O   
4747 O  O   . HOH E .   ? 0.3711 0.4321 0.8706 -0.2500 -0.3197 0.4070  1013 HOH A O   
4748 O  O   . HOH E .   ? 0.3629 0.4061 0.8960 0.2160  0.0001  0.0764  1014 HOH A O   
4749 O  O   . HOH E .   ? 0.2651 0.3348 0.3376 0.0783  0.0144  -0.0585 1015 HOH A O   
4750 O  O   A HOH E .   ? 0.4111 0.1384 0.1219 -0.0620 0.0949  -0.0552 1016 HOH A O   
4751 O  O   B HOH E .   ? 0.4525 0.3063 0.2952 0.0160  0.0126  -0.1780 1016 HOH A O   
4752 O  O   . HOH E .   ? 0.4729 0.3261 0.4875 -0.0748 -0.3217 0.1562  1017 HOH A O   
4753 O  O   . HOH E .   ? 0.8550 0.3105 0.2148 -0.1502 -0.0140 -0.0234 1018 HOH A O   
4754 O  O   . HOH E .   ? 0.3074 0.2816 0.1878 0.1382  0.0272  -0.0012 1019 HOH A O   
4755 O  O   . HOH E .   ? 0.3242 0.2780 0.2312 -0.0067 -0.1006 -0.0236 1020 HOH A O   
4756 O  O   . HOH E .   ? 0.7228 0.4436 0.6223 -0.3820 0.2079  -0.2059 1021 HOH A O   
4757 O  O   . HOH E .   ? 0.2812 0.2934 0.5975 -0.0366 0.1137  -0.1523 1022 HOH A O   
4758 O  O   . HOH E .   ? 0.4480 0.3953 0.2829 -0.1193 0.1578  -0.0598 1023 HOH A O   
4759 O  O   . HOH E .   ? 0.2685 1.0445 0.4286 -0.0573 -0.1176 0.0662  1024 HOH A O   
4760 O  O   . HOH E .   ? 0.3426 0.3354 0.3349 0.0666  -0.1083 0.0942  1025 HOH A O   
4761 O  O   . HOH E .   ? 0.5039 0.4340 0.4446 0.2528  -0.0125 -0.0895 1026 HOH A O   
4762 O  O   . HOH E .   ? 0.2779 1.4651 0.3873 0.1472  -0.0835 -0.2277 1027 HOH A O   
4763 O  O   . HOH E .   ? 0.5936 0.5295 0.3236 0.3539  0.0517  -0.0380 1028 HOH A O   
4764 O  O   . HOH E .   ? 0.5961 0.2192 0.8963 0.0811  -0.3984 -0.1018 1029 HOH A O   
4765 O  O   . HOH E .   ? 0.4094 0.2717 0.2447 0.0413  -0.0481 -0.0839 1030 HOH A O   
4766 O  O   . HOH E .   ? 0.6259 0.4520 0.3439 -0.2752 -0.1353 0.2031  1031 HOH A O   
4767 O  O   . HOH E .   ? 0.2806 0.4717 0.2640 0.0450  0.1052  0.0379  1032 HOH A O   
4768 O  O   . HOH E .   ? 0.2885 0.3616 1.0318 -0.0420 0.2609  -0.1453 1033 HOH A O   
4769 O  O   . HOH E .   ? 0.3528 0.9571 0.3838 -0.2577 -0.0329 0.2023  1034 HOH A O   
4770 O  O   A HOH E .   ? 0.3097 0.2871 0.1019 -0.1593 0.0399  -0.1223 1035 HOH A O   
4771 O  O   B HOH E .   ? 0.6630 0.4665 0.2800 -0.2048 0.0391  0.0282  1035 HOH A O   
4772 O  O   . HOH E .   ? 0.1433 0.6742 0.6914 0.0503  0.0744  0.0829  1036 HOH A O   
4773 O  O   . HOH E .   ? 0.2287 0.2698 0.2853 0.1200  0.0702  0.1099  1037 HOH A O   
4774 O  O   . HOH E .   ? 0.5122 0.6242 0.3901 -0.2355 0.1602  0.0256  1038 HOH A O   
4775 O  O   . HOH E .   ? 0.5615 0.7523 0.4435 0.3465  -0.1450 -0.3426 1039 HOH A O   
4776 O  O   . HOH E .   ? 0.2063 0.1962 0.1979 0.0479  -0.0792 -0.0469 1040 HOH A O   
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   ALA 1   1   1   ALA ALA A . n 
A 1 2   PRO 2   2   2   PRO PRO A . n 
A 1 3   PRO 3   3   3   PRO PRO A . n 
A 1 4   LYS 4   4   4   LYS LYS A . n 
A 1 5   SER 5   5   5   SER SER A . n 
A 1 6   VAL 6   6   6   VAL VAL A . n 
A 1 7   ILE 7   7   7   ILE ILE A . n 
A 1 8   ARG 8   8   8   ARG ARG A . n 
A 1 9   TRP 9   9   9   TRP TRP A . n 
A 1 10  CYS 10  10  10  CYS CYS A . n 
A 1 11  THR 11  11  11  THR THR A . n 
A 1 12  ILE 12  12  12  ILE ILE A . n 
A 1 13  SER 13  13  13  SER SER A . n 
A 1 14  SER 14  14  14  SER SER A . n 
A 1 15  PRO 15  15  15  PRO PRO A . n 
A 1 16  GLU 16  16  16  GLU GLU A . n 
A 1 17  GLU 17  17  17  GLU GLU A . n 
A 1 18  LYS 18  18  18  LYS LYS A . n 
A 1 19  LYS 19  19  19  LYS LYS A . n 
A 1 20  CYS 20  20  20  CYS CYS A . n 
A 1 21  ASN 21  21  21  ASN ASN A . n 
A 1 22  ASN 22  22  22  ASN ASN A . n 
A 1 23  LEU 23  23  23  LEU LEU A . n 
A 1 24  ARG 24  24  24  ARG ARG A . n 
A 1 25  ASP 25  25  25  ASP ASP A . n 
A 1 26  LEU 26  26  26  LEU LEU A . n 
A 1 27  THR 27  27  27  THR THR A . n 
A 1 28  GLN 28  28  28  GLN GLN A . n 
A 1 29  GLN 29  29  29  GLN GLN A . n 
A 1 30  GLU 30  30  30  GLU GLU A . n 
A 1 31  ARG 31  31  31  ARG ARG A . n 
A 1 32  ILE 32  32  32  ILE ILE A . n 
A 1 33  SER 33  33  33  SER SER A . n 
A 1 34  LEU 34  34  34  LEU LEU A . n 
A 1 35  THR 35  35  35  THR THR A . n 
A 1 36  CYS 36  36  36  CYS CYS A . n 
A 1 37  VAL 37  37  37  VAL VAL A . n 
A 1 38  GLN 38  38  38  GLN GLN A . n 
A 1 39  LYS 39  39  39  LYS LYS A . n 
A 1 40  ALA 40  40  40  ALA ALA A . n 
A 1 41  THR 41  41  41  THR THR A . n 
A 1 42  TYR 42  42  42  TYR TYR A . n 
A 1 43  LEU 43  43  43  LEU LEU A . n 
A 1 44  ASP 44  44  44  ASP ASP A . n 
A 1 45  CYS 45  45  45  CYS CYS A . n 
A 1 46  ILE 46  46  46  ILE ILE A . n 
A 1 47  LYS 47  47  47  LYS LYS A . n 
A 1 48  ALA 48  48  48  ALA ALA A . n 
A 1 49  ILE 49  49  49  ILE ILE A . n 
A 1 50  ALA 50  50  50  ALA ALA A . n 
A 1 51  ASN 51  51  51  ASN ASN A . n 
A 1 52  ASN 52  52  52  ASN ASN A . n 
A 1 53  GLU 53  53  53  GLU GLU A . n 
A 1 54  ALA 54  54  54  ALA ALA A . n 
A 1 55  ASP 55  55  55  ASP ASP A . n 
A 1 56  ALA 56  56  56  ALA ALA A . n 
A 1 57  ILE 57  57  57  ILE ILE A . n 
A 1 58  SER 58  58  58  SER SER A . n 
A 1 59  LEU 59  59  59  LEU LEU A . n 
A 1 60  ASP 60  60  60  ASP ASP A . n 
A 1 61  GLY 61  61  61  GLY GLY A . n 
A 1 62  GLY 62  62  62  GLY GLY A . n 
A 1 63  GLN 63  63  63  GLN GLN A . n 
A 1 64  VAL 64  64  64  VAL VAL A . n 
A 1 65  PHE 65  65  65  PHE PHE A . n 
A 1 66  GLU 66  66  66  GLU GLU A . n 
A 1 67  ALA 67  67  67  ALA ALA A . n 
A 1 68  GLY 68  68  68  GLY GLY A . n 
A 1 69  LEU 69  69  69  LEU LEU A . n 
A 1 70  ALA 70  70  70  ALA ALA A . n 
A 1 71  PRO 71  71  71  PRO PRO A . n 
A 1 72  TYR 72  72  72  TYR TYR A . n 
A 1 73  LYS 73  73  73  LYS LYS A . n 
A 1 74  LEU 74  74  74  LEU LEU A . n 
A 1 75  LYS 75  75  75  LYS LYS A . n 
A 1 76  PRO 76  76  76  PRO PRO A . n 
A 1 77  ILE 77  77  77  ILE ILE A . n 
A 1 78  ALA 78  78  78  ALA ALA A . n 
A 1 79  ALA 79  79  79  ALA ALA A . n 
A 1 80  GLU 80  80  80  GLU GLU A . n 
A 1 81  VAL 81  81  81  VAL VAL A . n 
A 1 82  TYR 82  82  82  TYR TYR A . n 
A 1 83  GLU 83  83  83  GLU GLU A . n 
A 1 84  HIS 84  84  84  HIS HIS A . n 
A 1 85  THR 85  85  85  THR THR A . n 
A 1 86  GLU 86  86  86  GLU GLU A . n 
A 1 87  GLY 87  87  87  GLY GLY A . n 
A 1 88  SER 88  88  88  SER SER A . n 
A 1 89  THR 89  89  89  THR THR A . n 
A 1 90  THR 90  90  90  THR THR A . n 
A 1 91  SER 91  91  91  SER SER A . n 
A 1 92  TYR 92  92  92  TYR TYR A . n 
A 1 93  TYR 93  93  93  TYR TYR A . n 
A 1 94  ALA 94  94  94  ALA ALA A . n 
A 1 95  VAL 95  95  95  VAL VAL A . n 
A 1 96  ALA 96  96  96  ALA ALA A . n 
A 1 97  VAL 97  97  97  VAL VAL A . n 
A 1 98  VAL 98  98  98  VAL VAL A . n 
A 1 99  LYS 99  99  99  LYS LYS A . n 
A 1 100 LYS 100 100 100 LYS LYS A . n 
A 1 101 GLY 101 101 101 GLY GLY A . n 
A 1 102 THR 102 102 102 THR THR A . n 
A 1 103 GLU 103 103 103 GLU GLU A . n 
A 1 104 PHE 104 104 104 PHE PHE A . n 
A 1 105 THR 105 105 105 THR THR A . n 
A 1 106 VAL 106 106 106 VAL VAL A . n 
A 1 107 ASN 107 107 107 ASN ASN A . n 
A 1 108 ASP 108 108 108 ASP ASP A . n 
A 1 109 LEU 109 109 109 LEU LEU A . n 
A 1 110 GLN 110 110 110 GLN GLN A . n 
A 1 111 GLY 111 111 111 GLY GLY A . n 
A 1 112 LYS 112 112 112 LYS LYS A . n 
A 1 113 THR 113 113 113 THR THR A . n 
A 1 114 SER 114 114 114 SER SER A . n 
A 1 115 CYS 115 115 115 CYS CYS A . n 
A 1 116 HIS 116 116 116 HIS HIS A . n 
A 1 117 THR 117 117 117 THR THR A . n 
A 1 118 GLY 118 118 118 GLY GLY A . n 
A 1 119 LEU 119 119 119 LEU LEU A . n 
A 1 120 GLY 120 120 120 GLY GLY A . n 
A 1 121 ARG 121 121 121 ARG ARG A . n 
A 1 122 SER 122 122 122 SER SER A . n 
A 1 123 ALA 123 123 123 ALA ALA A . n 
A 1 124 GLY 124 124 124 GLY GLY A . n 
A 1 125 TRP 125 125 125 TRP TRP A . n 
A 1 126 ASN 126 126 126 ASN ASN A . n 
A 1 127 ILE 127 127 127 ILE ILE A . n 
A 1 128 PRO 128 128 128 PRO PRO A . n 
A 1 129 ILE 129 129 129 ILE ILE A . n 
A 1 130 GLY 130 130 130 GLY GLY A . n 
A 1 131 THR 131 131 131 THR THR A . n 
A 1 132 LEU 132 132 132 LEU LEU A . n 
A 1 133 ILE 133 133 133 ILE ILE A . n 
A 1 134 HIS 134 134 134 HIS HIS A . n 
A 1 135 ARG 135 135 135 ARG ARG A . n 
A 1 136 GLY 136 136 136 GLY GLY A . n 
A 1 137 ALA 137 137 137 ALA ALA A . n 
A 1 138 ILE 138 138 138 ILE ILE A . n 
A 1 139 GLU 139 139 139 GLU GLU A . n 
A 1 140 TRP 140 140 140 TRP TRP A . n 
A 1 141 GLU 141 141 141 GLU GLU A . n 
A 1 142 GLY 142 142 142 GLY GLY A . n 
A 1 143 ILE 143 143 143 ILE ILE A . n 
A 1 144 GLU 144 144 144 GLU GLU A . n 
A 1 145 SER 145 145 145 SER SER A . n 
A 1 146 GLY 146 146 146 GLY GLY A . n 
A 1 147 SER 147 147 147 SER SER A . n 
A 1 148 VAL 148 148 148 VAL VAL A . n 
A 1 149 GLU 149 149 149 GLU GLU A . n 
A 1 150 GLN 150 150 150 GLN GLN A . n 
A 1 151 ALA 151 151 151 ALA ALA A . n 
A 1 152 VAL 152 152 152 VAL VAL A . n 
A 1 153 ALA 153 153 153 ALA ALA A . n 
A 1 154 LYS 154 154 154 LYS LYS A . n 
A 1 155 PHE 155 155 155 PHE PHE A . n 
A 1 156 PHE 156 156 156 PHE PHE A . n 
A 1 157 SER 157 157 157 SER SER A . n 
A 1 158 ALA 158 158 158 ALA ALA A . n 
A 1 159 SER 159 159 159 SER SER A . n 
A 1 160 CYS 160 160 160 CYS CYS A . n 
A 1 161 VAL 161 161 161 VAL VAL A . n 
A 1 162 PRO 162 162 162 PRO PRO A . n 
A 1 163 GLY 163 163 163 GLY GLY A . n 
A 1 164 ALA 164 164 164 ALA ALA A . n 
A 1 165 THR 165 165 165 THR THR A . n 
A 1 166 ILE 166 166 166 ILE ILE A . n 
A 1 167 GLU 167 167 167 GLU GLU A . n 
A 1 168 GLN 168 168 168 GLN GLN A . n 
A 1 169 LYS 169 169 169 LYS LYS A . n 
A 1 170 LEU 170 170 170 LEU LEU A . n 
A 1 171 CYS 171 171 171 CYS CYS A . n 
A 1 172 ARG 172 172 172 ARG ARG A . n 
A 1 173 GLN 173 173 173 GLN GLN A . n 
A 1 174 CYS 174 174 174 CYS CYS A . n 
A 1 175 LYS 175 175 175 LYS LYS A . n 
A 1 176 GLY 176 176 176 GLY GLY A . n 
A 1 177 ASP 177 177 177 ASP ASP A . n 
A 1 178 PRO 178 178 178 PRO PRO A . n 
A 1 179 LYS 179 179 179 LYS LYS A . n 
A 1 180 THR 180 180 180 THR THR A . n 
A 1 181 LYS 181 181 181 LYS LYS A . n 
A 1 182 CYS 182 182 182 CYS CYS A . n 
A 1 183 ALA 183 183 183 ALA ALA A . n 
A 1 184 ARG 184 184 184 ARG ARG A . n 
A 1 185 ASN 185 185 185 ASN ASN A . n 
A 1 186 ALA 186 186 186 ALA ALA A . n 
A 1 187 PRO 187 187 187 PRO PRO A . n 
A 1 188 TYR 188 188 188 TYR TYR A . n 
A 1 189 SER 189 189 189 SER SER A . n 
A 1 190 GLY 190 190 190 GLY GLY A . n 
A 1 191 TYR 191 191 191 TYR TYR A . n 
A 1 192 SER 192 192 192 SER SER A . n 
A 1 193 GLY 193 193 193 GLY GLY A . n 
A 1 194 ALA 194 194 194 ALA ALA A . n 
A 1 195 PHE 195 195 195 PHE PHE A . n 
A 1 196 HIS 196 196 196 HIS HIS A . n 
A 1 197 CYS 197 197 197 CYS CYS A . n 
A 1 198 LEU 198 198 198 LEU LEU A . n 
A 1 199 LYS 199 199 199 LYS LYS A . n 
A 1 200 ASP 200 200 200 ASP ASP A . n 
A 1 201 GLY 201 201 201 GLY GLY A . n 
A 1 202 LYS 202 202 202 LYS LYS A . n 
A 1 203 GLY 203 203 203 GLY GLY A . n 
A 1 204 ASP 204 204 204 ASP ASP A . n 
A 1 205 VAL 205 205 205 VAL VAL A . n 
A 1 206 ALA 206 206 206 ALA ALA A . n 
A 1 207 PHE 207 207 207 PHE PHE A . n 
A 1 208 VAL 208 208 208 VAL VAL A . n 
A 1 209 LYS 209 209 209 LYS LYS A . n 
A 1 210 HIS 210 210 210 HIS HIS A . n 
A 1 211 THR 211 211 211 THR THR A . n 
A 1 212 THR 212 212 212 THR THR A . n 
A 1 213 VAL 213 213 213 VAL VAL A . n 
A 1 214 ASN 214 214 214 ASN ASN A . n 
A 1 215 GLU 215 215 215 GLU GLU A . n 
A 1 216 ASN 216 216 216 ASN ASN A . n 
A 1 217 ALA 217 217 217 ALA ALA A . n 
A 1 218 PRO 218 218 218 PRO PRO A . n 
A 1 219 ASP 219 219 219 ASP ASP A . n 
A 1 220 GLN 220 220 220 GLN GLN A . n 
A 1 221 LYS 221 221 221 LYS LYS A . n 
A 1 222 ASP 222 222 222 ASP ASP A . n 
A 1 223 GLU 223 223 223 GLU GLU A . n 
A 1 224 TYR 224 224 224 TYR TYR A . n 
A 1 225 GLU 225 225 225 GLU GLU A . n 
A 1 226 LEU 226 226 226 LEU LEU A . n 
A 1 227 LEU 227 227 227 LEU LEU A . n 
A 1 228 CYS 228 228 228 CYS CYS A . n 
A 1 229 LEU 229 229 229 LEU LEU A . n 
A 1 230 ASP 230 230 230 ASP ASP A . n 
A 1 231 GLY 231 231 231 GLY GLY A . n 
A 1 232 SER 232 232 232 SER SER A . n 
A 1 233 ARG 233 233 233 ARG ARG A . n 
A 1 234 GLN 234 234 234 GLN GLN A . n 
A 1 235 PRO 235 235 235 PRO PRO A . n 
A 1 236 VAL 236 236 236 VAL VAL A . n 
A 1 237 ASP 237 237 237 ASP ASP A . n 
A 1 238 ASN 238 238 238 ASN ASN A . n 
A 1 239 TYR 239 239 239 TYR TYR A . n 
A 1 240 LYS 240 240 240 LYS LYS A . n 
A 1 241 THR 241 241 241 THR THR A . n 
A 1 242 CYS 242 242 242 CYS CYS A . n 
A 1 243 ASN 243 243 243 ASN ASN A . n 
A 1 244 TRP 244 244 244 TRP TRP A . n 
A 1 245 ALA 245 245 245 ALA ALA A . n 
A 1 246 ARG 246 246 246 ARG ARG A . n 
A 1 247 VAL 247 247 247 VAL VAL A . n 
A 1 248 ALA 248 248 248 ALA ALA A . n 
A 1 249 ALA 249 249 249 ALA ALA A . n 
A 1 250 HIS 250 250 250 HIS HIS A . n 
A 1 251 ALA 251 251 251 ALA ALA A . n 
A 1 252 VAL 252 252 252 VAL VAL A . n 
A 1 253 VAL 253 253 253 VAL VAL A . n 
A 1 254 ALA 254 254 254 ALA ALA A . n 
A 1 255 ARG 255 255 255 ARG ARG A . n 
A 1 256 ASP 256 256 256 ASP ASP A . n 
A 1 257 ASP 257 257 257 ASP ASP A . n 
A 1 258 ASN 258 258 258 ASN ASN A . n 
A 1 259 LYS 259 259 259 LYS LYS A . n 
A 1 260 VAL 260 260 260 VAL VAL A . n 
A 1 261 GLU 261 261 261 GLU GLU A . n 
A 1 262 ASP 262 262 262 ASP ASP A . n 
A 1 263 ILE 263 263 263 ILE ILE A . n 
A 1 264 TRP 264 264 264 TRP TRP A . n 
A 1 265 SER 265 265 265 SER SER A . n 
A 1 266 PHE 266 266 266 PHE PHE A . n 
A 1 267 LEU 267 267 267 LEU LEU A . n 
A 1 268 SER 268 268 268 SER SER A . n 
A 1 269 LYS 269 269 269 LYS LYS A . n 
A 1 270 ALA 270 270 270 ALA ALA A . n 
A 1 271 GLN 271 271 271 GLN GLN A . n 
A 1 272 SER 272 272 272 SER SER A . n 
A 1 273 ASP 273 273 273 ASP ASP A . n 
A 1 274 PHE 274 274 274 PHE PHE A . n 
A 1 275 GLY 275 275 275 GLY GLY A . n 
A 1 276 VAL 276 276 276 VAL VAL A . n 
A 1 277 ASP 277 277 277 ASP ASP A . n 
A 1 278 THR 278 278 278 THR THR A . n 
A 1 279 LYS 279 279 279 LYS LYS A . n 
A 1 280 SER 280 280 280 SER SER A . n 
A 1 281 ASP 281 281 281 ASP ASP A . n 
A 1 282 PHE 282 282 282 PHE PHE A . n 
A 1 283 HIS 283 283 283 HIS HIS A . n 
A 1 284 LEU 284 284 284 LEU LEU A . n 
A 1 285 PHE 285 285 285 PHE PHE A . n 
A 1 286 GLY 286 286 286 GLY GLY A . n 
A 1 287 PRO 287 287 287 PRO PRO A . n 
A 1 288 PRO 288 288 288 PRO PRO A . n 
A 1 289 GLY 289 289 289 GLY GLY A . n 
A 1 290 LYS 290 290 290 LYS LYS A . n 
A 1 291 LYS 291 291 291 LYS LYS A . n 
A 1 292 ASP 292 292 292 ASP ASP A . n 
A 1 293 PRO 293 293 293 PRO PRO A . n 
A 1 294 VAL 294 294 294 VAL VAL A . n 
A 1 295 LEU 295 295 295 LEU LEU A . n 
A 1 296 LYS 296 296 296 LYS LYS A . n 
A 1 297 ASP 297 297 297 ASP ASP A . n 
A 1 298 LEU 298 298 298 LEU LEU A . n 
A 1 299 LEU 299 299 299 LEU LEU A . n 
A 1 300 PHE 300 300 300 PHE PHE A . n 
A 1 301 LYS 301 301 301 LYS LYS A . n 
A 1 302 ASP 302 302 302 ASP ASP A . n 
A 1 303 SER 303 303 303 SER SER A . n 
A 1 304 ALA 304 304 304 ALA ALA A . n 
A 1 305 ILE 305 305 305 ILE ILE A . n 
A 1 306 MET 306 306 306 MET MET A . n 
A 1 307 LEU 307 307 307 LEU LEU A . n 
A 1 308 LYS 308 308 308 LYS LYS A . n 
A 1 309 ARG 309 309 309 ARG ARG A . n 
A 1 310 VAL 310 310 310 VAL VAL A . n 
A 1 311 PRO 311 311 311 PRO PRO A . n 
A 1 312 SER 312 312 312 SER SER A . n 
A 1 313 LEU 313 313 313 LEU LEU A . n 
A 1 314 MET 314 314 314 MET MET A . n 
A 1 315 ASP 315 315 315 ASP ASP A . n 
A 1 316 SER 316 316 316 SER SER A . n 
A 1 317 GLN 317 317 317 GLN GLN A . n 
A 1 318 LEU 318 318 318 LEU LEU A . n 
A 1 319 TYR 319 319 319 TYR TYR A . n 
A 1 320 LEU 320 320 320 LEU LEU A . n 
A 1 321 GLY 321 321 321 GLY GLY A . n 
A 1 322 PHE 322 322 322 PHE PHE A . n 
A 1 323 GLU 323 323 323 GLU GLU A . n 
A 1 324 TYR 324 324 324 TYR TYR A . n 
A 1 325 TYR 325 325 325 TYR TYR A . n 
A 1 326 SER 326 326 326 SER SER A . n 
A 1 327 ALA 327 327 327 ALA ALA A . n 
A 1 328 ILE 328 328 328 ILE ILE A . n 
A 1 329 GLN 329 329 329 GLN GLN A . n 
A 1 330 SER 330 330 330 SER SER A . n 
A 1 331 MET 331 331 331 MET MET A . n 
A 1 332 ARG 332 332 332 ARG ARG A . n 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              kmizutani@kais.kyoto-u.ac.jp 
_pdbx_contact_author.name_first         Kimihiko 
_pdbx_contact_author.name_last          Mizutani 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-1411-5429 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 FE  1   401  1333 FE  FE  A . 
C 3 CO3 1   402  1334 CO3 CO3 A . 
D 4 GOL 1   403  1335 GOL GOL A . 
E 5 HOH 1   501  2555 HOH HOH A . 
E 5 HOH 2   502  2296 HOH HOH A . 
E 5 HOH 3   503  2438 HOH HOH A . 
E 5 HOH 4   504  2533 HOH HOH A . 
E 5 HOH 5   505  2274 HOH HOH A . 
E 5 HOH 6   506  2458 HOH HOH A . 
E 5 HOH 7   507  2270 HOH HOH A . 
E 5 HOH 8   508  2595 HOH HOH A . 
E 5 HOH 9   509  2446 HOH HOH A . 
E 5 HOH 10  510  2179 HOH HOH A . 
E 5 HOH 11  511  2499 HOH HOH A . 
E 5 HOH 12  512  2383 HOH HOH A . 
E 5 HOH 13  513  2132 HOH HOH A . 
E 5 HOH 14  514  2264 HOH HOH A . 
E 5 HOH 15  515  2231 HOH HOH A . 
E 5 HOH 16  516  2409 HOH HOH A . 
E 5 HOH 17  517  2420 HOH HOH A . 
E 5 HOH 18  518  2268 HOH HOH A . 
E 5 HOH 19  519  2135 HOH HOH A . 
E 5 HOH 20  520  2257 HOH HOH A . 
E 5 HOH 21  521  2161 HOH HOH A . 
E 5 HOH 22  522  2624 HOH HOH A . 
E 5 HOH 23  523  2471 HOH HOH A . 
E 5 HOH 24  524  2184 HOH HOH A . 
E 5 HOH 25  525  2093 HOH HOH A . 
E 5 HOH 26  526  2538 HOH HOH A . 
E 5 HOH 27  527  2186 HOH HOH A . 
E 5 HOH 28  528  2524 HOH HOH A . 
E 5 HOH 29  529  2385 HOH HOH A . 
E 5 HOH 30  530  2455 HOH HOH A . 
E 5 HOH 31  531  2531 HOH HOH A . 
E 5 HOH 32  532  2437 HOH HOH A . 
E 5 HOH 33  533  2535 HOH HOH A . 
E 5 HOH 34  534  2442 HOH HOH A . 
E 5 HOH 35  535  2287 HOH HOH A . 
E 5 HOH 36  536  2418 HOH HOH A . 
E 5 HOH 37  537  2372 HOH HOH A . 
E 5 HOH 38  538  2425 HOH HOH A . 
E 5 HOH 39  539  2081 HOH HOH A . 
E 5 HOH 40  540  2357 HOH HOH A . 
E 5 HOH 41  541  2429 HOH HOH A . 
E 5 HOH 42  542  2130 HOH HOH A . 
E 5 HOH 43  543  2043 HOH HOH A . 
E 5 HOH 44  544  2522 HOH HOH A . 
E 5 HOH 45  545  2628 HOH HOH A . 
E 5 HOH 46  546  2583 HOH HOH A . 
E 5 HOH 47  547  2460 HOH HOH A . 
E 5 HOH 48  548  2582 HOH HOH A . 
E 5 HOH 49  549  2237 HOH HOH A . 
E 5 HOH 50  550  2176 HOH HOH A . 
E 5 HOH 51  551  2413 HOH HOH A . 
E 5 HOH 52  552  2210 HOH HOH A . 
E 5 HOH 53  553  2569 HOH HOH A . 
E 5 HOH 54  554  2520 HOH HOH A . 
E 5 HOH 55  555  2103 HOH HOH A . 
E 5 HOH 56  556  2559 HOH HOH A . 
E 5 HOH 57  557  2430 HOH HOH A . 
E 5 HOH 58  558  2011 HOH HOH A . 
E 5 HOH 59  559  2087 HOH HOH A . 
E 5 HOH 60  560  2111 HOH HOH A . 
E 5 HOH 61  561  2399 HOH HOH A . 
E 5 HOH 62  562  2215 HOH HOH A . 
E 5 HOH 63  563  2365 HOH HOH A . 
E 5 HOH 64  564  2331 HOH HOH A . 
E 5 HOH 65  565  2144 HOH HOH A . 
E 5 HOH 66  566  2206 HOH HOH A . 
E 5 HOH 67  567  2126 HOH HOH A . 
E 5 HOH 68  568  2232 HOH HOH A . 
E 5 HOH 69  569  2123 HOH HOH A . 
E 5 HOH 70  570  2076 HOH HOH A . 
E 5 HOH 71  571  2107 HOH HOH A . 
E 5 HOH 72  572  2229 HOH HOH A . 
E 5 HOH 73  573  2036 HOH HOH A . 
E 5 HOH 74  574  2182 HOH HOH A . 
E 5 HOH 75  575  2121 HOH HOH A . 
E 5 HOH 76  576  2077 HOH HOH A . 
E 5 HOH 77  577  2384 HOH HOH A . 
E 5 HOH 78  578  2302 HOH HOH A . 
E 5 HOH 79  579  2208 HOH HOH A . 
E 5 HOH 80  580  2527 HOH HOH A . 
E 5 HOH 81  581  2411 HOH HOH A . 
E 5 HOH 82  582  2119 HOH HOH A . 
E 5 HOH 83  583  2521 HOH HOH A . 
E 5 HOH 84  584  2403 HOH HOH A . 
E 5 HOH 85  585  2069 HOH HOH A . 
E 5 HOH 86  586  2316 HOH HOH A . 
E 5 HOH 87  587  2085 HOH HOH A . 
E 5 HOH 88  588  2367 HOH HOH A . 
E 5 HOH 89  589  2253 HOH HOH A . 
E 5 HOH 90  590  2014 HOH HOH A . 
E 5 HOH 91  591  2323 HOH HOH A . 
E 5 HOH 92  592  2128 HOH HOH A . 
E 5 HOH 93  593  2528 HOH HOH A . 
E 5 HOH 94  594  2427 HOH HOH A . 
E 5 HOH 95  595  2299 HOH HOH A . 
E 5 HOH 96  596  2027 HOH HOH A . 
E 5 HOH 97  597  2122 HOH HOH A . 
E 5 HOH 98  598  2202 HOH HOH A . 
E 5 HOH 99  599  2065 HOH HOH A . 
E 5 HOH 100 600  2159 HOH HOH A . 
E 5 HOH 101 601  2211 HOH HOH A . 
E 5 HOH 102 602  2079 HOH HOH A . 
E 5 HOH 103 603  2106 HOH HOH A . 
E 5 HOH 104 604  2059 HOH HOH A . 
E 5 HOH 105 605  2419 HOH HOH A . 
E 5 HOH 106 606  2224 HOH HOH A . 
E 5 HOH 107 607  2326 HOH HOH A . 
E 5 HOH 108 608  2055 HOH HOH A . 
E 5 HOH 109 609  2008 HOH HOH A . 
E 5 HOH 110 610  2033 HOH HOH A . 
E 5 HOH 111 611  2200 HOH HOH A . 
E 5 HOH 112 612  2168 HOH HOH A . 
E 5 HOH 113 613  2201 HOH HOH A . 
E 5 HOH 114 614  2073 HOH HOH A . 
E 5 HOH 115 615  2143 HOH HOH A . 
E 5 HOH 116 616  2515 HOH HOH A . 
E 5 HOH 117 617  2030 HOH HOH A . 
E 5 HOH 118 618  2269 HOH HOH A . 
E 5 HOH 119 619  2020 HOH HOH A . 
E 5 HOH 120 620  2125 HOH HOH A . 
E 5 HOH 121 621  2004 HOH HOH A . 
E 5 HOH 122 622  2129 HOH HOH A . 
E 5 HOH 123 623  2001 HOH HOH A . 
E 5 HOH 124 624  2083 HOH HOH A . 
E 5 HOH 125 625  2057 HOH HOH A . 
E 5 HOH 126 626  2060 HOH HOH A . 
E 5 HOH 127 627  2623 HOH HOH A . 
E 5 HOH 128 628  2024 HOH HOH A . 
E 5 HOH 129 629  2040 HOH HOH A . 
E 5 HOH 130 630  2292 HOH HOH A . 
E 5 HOH 131 631  2283 HOH HOH A . 
E 5 HOH 132 632  2110 HOH HOH A . 
E 5 HOH 133 633  2102 HOH HOH A . 
E 5 HOH 134 634  2190 HOH HOH A . 
E 5 HOH 135 635  2062 HOH HOH A . 
E 5 HOH 136 636  2187 HOH HOH A . 
E 5 HOH 137 637  2516 HOH HOH A . 
E 5 HOH 138 638  2529 HOH HOH A . 
E 5 HOH 139 639  2618 HOH HOH A . 
E 5 HOH 140 640  2115 HOH HOH A . 
E 5 HOH 141 641  2293 HOH HOH A . 
E 5 HOH 142 642  2053 HOH HOH A . 
E 5 HOH 143 643  2091 HOH HOH A . 
E 5 HOH 144 644  2568 HOH HOH A . 
E 5 HOH 145 645  2052 HOH HOH A . 
E 5 HOH 146 646  2051 HOH HOH A . 
E 5 HOH 147 647  2136 HOH HOH A . 
E 5 HOH 148 648  2124 HOH HOH A . 
E 5 HOH 149 649  2401 HOH HOH A . 
E 5 HOH 150 650  2180 HOH HOH A . 
E 5 HOH 151 651  2342 HOH HOH A . 
E 5 HOH 152 652  2198 HOH HOH A . 
E 5 HOH 153 653  2203 HOH HOH A . 
E 5 HOH 154 654  2313 HOH HOH A . 
E 5 HOH 155 655  2234 HOH HOH A . 
E 5 HOH 156 656  2037 HOH HOH A . 
E 5 HOH 157 657  2026 HOH HOH A . 
E 5 HOH 158 658  2546 HOH HOH A . 
E 5 HOH 159 659  2070 HOH HOH A . 
E 5 HOH 160 660  2157 HOH HOH A . 
E 5 HOH 161 661  2414 HOH HOH A . 
E 5 HOH 162 662  2259 HOH HOH A . 
E 5 HOH 163 663  2400 HOH HOH A . 
E 5 HOH 164 664  2298 HOH HOH A . 
E 5 HOH 165 665  2368 HOH HOH A . 
E 5 HOH 166 666  2088 HOH HOH A . 
E 5 HOH 167 667  2075 HOH HOH A . 
E 5 HOH 168 668  2067 HOH HOH A . 
E 5 HOH 169 669  2047 HOH HOH A . 
E 5 HOH 170 670  2526 HOH HOH A . 
E 5 HOH 171 671  2039 HOH HOH A . 
E 5 HOH 172 672  2416 HOH HOH A . 
E 5 HOH 173 673  2377 HOH HOH A . 
E 5 HOH 174 674  2046 HOH HOH A . 
E 5 HOH 175 675  2239 HOH HOH A . 
E 5 HOH 176 676  2038 HOH HOH A . 
E 5 HOH 177 677  2421 HOH HOH A . 
E 5 HOH 178 678  2261 HOH HOH A . 
E 5 HOH 179 679  2328 HOH HOH A . 
E 5 HOH 180 680  2138 HOH HOH A . 
E 5 HOH 181 681  2071 HOH HOH A . 
E 5 HOH 182 682  2010 HOH HOH A . 
E 5 HOH 183 683  2098 HOH HOH A . 
E 5 HOH 184 684  2063 HOH HOH A . 
E 5 HOH 185 685  2078 HOH HOH A . 
E 5 HOH 186 686  2003 HOH HOH A . 
E 5 HOH 187 687  2243 HOH HOH A . 
E 5 HOH 188 688  2013 HOH HOH A . 
E 5 HOH 189 689  2397 HOH HOH A . 
E 5 HOH 190 690  2620 HOH HOH A . 
E 5 HOH 191 691  2031 HOH HOH A . 
E 5 HOH 192 692  2378 HOH HOH A . 
E 5 HOH 193 693  2074 HOH HOH A . 
E 5 HOH 194 694  2588 HOH HOH A . 
E 5 HOH 195 695  2048 HOH HOH A . 
E 5 HOH 196 696  2327 HOH HOH A . 
E 5 HOH 197 697  2019 HOH HOH A . 
E 5 HOH 198 698  2199 HOH HOH A . 
E 5 HOH 199 699  2395 HOH HOH A . 
E 5 HOH 200 700  2390 HOH HOH A . 
E 5 HOH 201 701  2016 HOH HOH A . 
E 5 HOH 202 702  2295 HOH HOH A . 
E 5 HOH 203 703  2330 HOH HOH A . 
E 5 HOH 204 704  2025 HOH HOH A . 
E 5 HOH 205 705  2322 HOH HOH A . 
E 5 HOH 206 706  2012 HOH HOH A . 
E 5 HOH 207 707  2622 HOH HOH A . 
E 5 HOH 208 708  2049 HOH HOH A . 
E 5 HOH 209 709  2167 HOH HOH A . 
E 5 HOH 210 710  2149 HOH HOH A . 
E 5 HOH 211 711  2092 HOH HOH A . 
E 5 HOH 212 712  2435 HOH HOH A . 
E 5 HOH 213 713  2095 HOH HOH A . 
E 5 HOH 214 714  2045 HOH HOH A . 
E 5 HOH 215 715  2056 HOH HOH A . 
E 5 HOH 216 716  2005 HOH HOH A . 
E 5 HOH 217 717  2017 HOH HOH A . 
E 5 HOH 218 718  2173 HOH HOH A . 
E 5 HOH 219 719  2035 HOH HOH A . 
E 5 HOH 220 720  2245 HOH HOH A . 
E 5 HOH 221 721  2183 HOH HOH A . 
E 5 HOH 222 722  2022 HOH HOH A . 
E 5 HOH 223 723  2195 HOH HOH A . 
E 5 HOH 224 724  2332 HOH HOH A . 
E 5 HOH 225 725  2514 HOH HOH A . 
E 5 HOH 226 726  2080 HOH HOH A . 
E 5 HOH 227 727  2029 HOH HOH A . 
E 5 HOH 228 728  2120 HOH HOH A . 
E 5 HOH 229 729  2361 HOH HOH A . 
E 5 HOH 230 730  2267 HOH HOH A . 
E 5 HOH 231 731  2317 HOH HOH A . 
E 5 HOH 232 732  2172 HOH HOH A . 
E 5 HOH 233 733  2164 HOH HOH A . 
E 5 HOH 234 734  2150 HOH HOH A . 
E 5 HOH 235 735  2637 HOH HOH A . 
E 5 HOH 236 736  2163 HOH HOH A . 
E 5 HOH 237 737  2032 HOH HOH A . 
E 5 HOH 238 738  2426 HOH HOH A . 
E 5 HOH 239 739  2002 HOH HOH A . 
E 5 HOH 240 740  2417 HOH HOH A . 
E 5 HOH 241 741  2311 HOH HOH A . 
E 5 HOH 242 742  2297 HOH HOH A . 
E 5 HOH 243 743  2058 HOH HOH A . 
E 5 HOH 244 744  2196 HOH HOH A . 
E 5 HOH 245 745  2061 HOH HOH A . 
E 5 HOH 246 746  2141 HOH HOH A . 
E 5 HOH 247 747  2434 HOH HOH A . 
E 5 HOH 248 748  2410 HOH HOH A . 
E 5 HOH 249 749  2617 HOH HOH A . 
E 5 HOH 250 750  2142 HOH HOH A . 
E 5 HOH 251 751  2412 HOH HOH A . 
E 5 HOH 252 752  2290 HOH HOH A . 
E 5 HOH 253 753  2387 HOH HOH A . 
E 5 HOH 254 754  2415 HOH HOH A . 
E 5 HOH 255 755  2023 HOH HOH A . 
E 5 HOH 256 756  2619 HOH HOH A . 
E 5 HOH 257 757  2015 HOH HOH A . 
E 5 HOH 258 758  2445 HOH HOH A . 
E 5 HOH 259 759  2318 HOH HOH A . 
E 5 HOH 260 760  2006 HOH HOH A . 
E 5 HOH 261 761  2553 HOH HOH A . 
E 5 HOH 262 762  2246 HOH HOH A . 
E 5 HOH 263 763  2082 HOH HOH A . 
E 5 HOH 264 764  2271 HOH HOH A . 
E 5 HOH 265 765  2431 HOH HOH A . 
E 5 HOH 266 766  2177 HOH HOH A . 
E 5 HOH 267 767  2562 HOH HOH A . 
E 5 HOH 268 768  2404 HOH HOH A . 
E 5 HOH 269 769  2192 HOH HOH A . 
E 5 HOH 270 770  2009 HOH HOH A . 
E 5 HOH 271 771  2632 HOH HOH A . 
E 5 HOH 272 772  2321 HOH HOH A . 
E 5 HOH 273 773  2467 HOH HOH A . 
E 5 HOH 274 774  2405 HOH HOH A . 
E 5 HOH 275 775  2064 HOH HOH A . 
E 5 HOH 276 776  2641 HOH HOH A . 
E 5 HOH 277 777  2021 HOH HOH A . 
E 5 HOH 278 778  2556 HOH HOH A . 
E 5 HOH 279 779  2398 HOH HOH A . 
E 5 HOH 280 780  2054 HOH HOH A . 
E 5 HOH 281 781  2475 HOH HOH A . 
E 5 HOH 282 782  2578 HOH HOH A . 
E 5 HOH 283 783  2463 HOH HOH A . 
E 5 HOH 284 784  2028 HOH HOH A . 
E 5 HOH 285 785  2034 HOH HOH A . 
E 5 HOH 286 786  2100 HOH HOH A . 
E 5 HOH 287 787  2288 HOH HOH A . 
E 5 HOH 288 788  2147 HOH HOH A . 
E 5 HOH 289 789  2099 HOH HOH A . 
E 5 HOH 290 790  2389 HOH HOH A . 
E 5 HOH 291 791  2145 HOH HOH A . 
E 5 HOH 292 792  2007 HOH HOH A . 
E 5 HOH 293 793  2279 HOH HOH A . 
E 5 HOH 294 794  2137 HOH HOH A . 
E 5 HOH 295 795  2044 HOH HOH A . 
E 5 HOH 296 796  2131 HOH HOH A . 
E 5 HOH 297 797  2086 HOH HOH A . 
E 5 HOH 298 798  2221 HOH HOH A . 
E 5 HOH 299 799  2589 HOH HOH A . 
E 5 HOH 300 800  2218 HOH HOH A . 
E 5 HOH 301 801  2284 HOH HOH A . 
E 5 HOH 302 802  2294 HOH HOH A . 
E 5 HOH 303 803  2089 HOH HOH A . 
E 5 HOH 304 804  2213 HOH HOH A . 
E 5 HOH 305 805  2470 HOH HOH A . 
E 5 HOH 306 806  2285 HOH HOH A . 
E 5 HOH 307 807  2114 HOH HOH A . 
E 5 HOH 308 808  2109 HOH HOH A . 
E 5 HOH 309 809  2127 HOH HOH A . 
E 5 HOH 310 810  2116 HOH HOH A . 
E 5 HOH 311 811  2541 HOH HOH A . 
E 5 HOH 312 812  2386 HOH HOH A . 
E 5 HOH 313 813  2336 HOH HOH A . 
E 5 HOH 314 814  2258 HOH HOH A . 
E 5 HOH 315 815  2306 HOH HOH A . 
E 5 HOH 316 816  2310 HOH HOH A . 
E 5 HOH 317 817  2101 HOH HOH A . 
E 5 HOH 318 818  2393 HOH HOH A . 
E 5 HOH 319 819  2518 HOH HOH A . 
E 5 HOH 320 820  2042 HOH HOH A . 
E 5 HOH 321 821  2155 HOH HOH A . 
E 5 HOH 322 822  2193 HOH HOH A . 
E 5 HOH 323 823  2171 HOH HOH A . 
E 5 HOH 324 824  2291 HOH HOH A . 
E 5 HOH 325 825  2146 HOH HOH A . 
E 5 HOH 326 826  2542 HOH HOH A . 
E 5 HOH 327 827  2068 HOH HOH A . 
E 5 HOH 328 828  2359 HOH HOH A . 
E 5 HOH 329 829  2380 HOH HOH A . 
E 5 HOH 330 830  2250 HOH HOH A . 
E 5 HOH 331 831  2118 HOH HOH A . 
E 5 HOH 332 832  2041 HOH HOH A . 
E 5 HOH 333 833  2325 HOH HOH A . 
E 5 HOH 334 834  2392 HOH HOH A . 
E 5 HOH 335 835  2286 HOH HOH A . 
E 5 HOH 336 836  2315 HOH HOH A . 
E 5 HOH 337 837  2407 HOH HOH A . 
E 5 HOH 338 838  2096 HOH HOH A . 
E 5 HOH 339 839  2433 HOH HOH A . 
E 5 HOH 340 840  2388 HOH HOH A . 
E 5 HOH 341 841  2207 HOH HOH A . 
E 5 HOH 342 842  2162 HOH HOH A . 
E 5 HOH 343 843  2227 HOH HOH A . 
E 5 HOH 344 844  2072 HOH HOH A . 
E 5 HOH 345 845  2104 HOH HOH A . 
E 5 HOH 346 846  2440 HOH HOH A . 
E 5 HOH 347 847  2517 HOH HOH A . 
E 5 HOH 348 848  2307 HOH HOH A . 
E 5 HOH 349 849  2175 HOH HOH A . 
E 5 HOH 350 850  2209 HOH HOH A . 
E 5 HOH 351 851  2151 HOH HOH A . 
E 5 HOH 352 852  2394 HOH HOH A . 
E 5 HOH 353 853  2408 HOH HOH A . 
E 5 HOH 354 854  2289 HOH HOH A . 
E 5 HOH 355 855  2260 HOH HOH A . 
E 5 HOH 356 856  2465 HOH HOH A . 
E 5 HOH 357 857  2205 HOH HOH A . 
E 5 HOH 358 858  2225 HOH HOH A . 
E 5 HOH 359 859  2090 HOH HOH A . 
E 5 HOH 360 860  2560 HOH HOH A . 
E 5 HOH 361 861  2094 HOH HOH A . 
E 5 HOH 362 862  2134 HOH HOH A . 
E 5 HOH 363 863  2112 HOH HOH A . 
E 5 HOH 364 864  2303 HOH HOH A . 
E 5 HOH 365 865  2133 HOH HOH A . 
E 5 HOH 366 866  2644 HOH HOH A . 
E 5 HOH 367 867  2329 HOH HOH A . 
E 5 HOH 368 868  2249 HOH HOH A . 
E 5 HOH 369 869  2314 HOH HOH A . 
E 5 HOH 370 870  2153 HOH HOH A . 
E 5 HOH 371 871  2477 HOH HOH A . 
E 5 HOH 372 872  2226 HOH HOH A . 
E 5 HOH 373 873  2066 HOH HOH A . 
E 5 HOH 374 874  2354 HOH HOH A . 
E 5 HOH 375 875  2312 HOH HOH A . 
E 5 HOH 376 876  2251 HOH HOH A . 
E 5 HOH 377 877  2156 HOH HOH A . 
E 5 HOH 378 878  2212 HOH HOH A . 
E 5 HOH 379 879  2627 HOH HOH A . 
E 5 HOH 380 880  2084 HOH HOH A . 
E 5 HOH 381 881  2551 HOH HOH A . 
E 5 HOH 382 882  2549 HOH HOH A . 
E 5 HOH 383 883  2050 HOH HOH A . 
E 5 HOH 384 884  2539 HOH HOH A . 
E 5 HOH 385 885  2222 HOH HOH A . 
E 5 HOH 386 886  2626 HOH HOH A . 
E 5 HOH 387 887  2550 HOH HOH A . 
E 5 HOH 388 888  2547 HOH HOH A . 
E 5 HOH 389 889  2636 HOH HOH A . 
E 5 HOH 390 890  2593 HOH HOH A . 
E 5 HOH 391 891  2197 HOH HOH A . 
E 5 HOH 392 892  2220 HOH HOH A . 
E 5 HOH 393 893  2596 HOH HOH A . 
E 5 HOH 394 894  2236 HOH HOH A . 
E 5 HOH 395 895  2629 HOH HOH A . 
E 5 HOH 396 896  2018 HOH HOH A . 
E 5 HOH 397 897  2630 HOH HOH A . 
E 5 HOH 398 898  2376 HOH HOH A . 
E 5 HOH 399 899  2464 HOH HOH A . 
E 5 HOH 400 900  2432 HOH HOH A . 
E 5 HOH 401 901  2590 HOH HOH A . 
E 5 HOH 402 902  2174 HOH HOH A . 
E 5 HOH 403 903  2309 HOH HOH A . 
E 5 HOH 404 904  2519 HOH HOH A . 
E 5 HOH 405 905  2169 HOH HOH A . 
E 5 HOH 406 906  2500 HOH HOH A . 
E 5 HOH 407 907  2181 HOH HOH A . 
E 5 HOH 408 908  2097 HOH HOH A . 
E 5 HOH 409 909  2217 HOH HOH A . 
E 5 HOH 410 910  2188 HOH HOH A . 
E 5 HOH 411 911  2375 HOH HOH A . 
E 5 HOH 412 912  2228 HOH HOH A . 
E 5 HOH 413 913  2558 HOH HOH A . 
E 5 HOH 414 914  2402 HOH HOH A . 
E 5 HOH 415 915  2191 HOH HOH A . 
E 5 HOH 416 916  2235 HOH HOH A . 
E 5 HOH 417 917  2501 HOH HOH A . 
E 5 HOH 418 918  2148 HOH HOH A . 
E 5 HOH 419 919  2154 HOH HOH A . 
E 5 HOH 420 920  2256 HOH HOH A . 
E 5 HOH 421 921  2240 HOH HOH A . 
E 5 HOH 422 922  2343 HOH HOH A . 
E 5 HOH 423 923  2278 HOH HOH A . 
E 5 HOH 424 924  2566 HOH HOH A . 
E 5 HOH 425 925  2360 HOH HOH A . 
E 5 HOH 426 926  2333 HOH HOH A . 
E 5 HOH 427 927  2241 HOH HOH A . 
E 5 HOH 428 928  2371 HOH HOH A . 
E 5 HOH 429 929  2152 HOH HOH A . 
E 5 HOH 430 930  2262 HOH HOH A . 
E 5 HOH 431 931  2586 HOH HOH A . 
E 5 HOH 432 932  2625 HOH HOH A . 
E 5 HOH 433 933  2571 HOH HOH A . 
E 5 HOH 434 934  2108 HOH HOH A . 
E 5 HOH 435 935  2255 HOH HOH A . 
E 5 HOH 436 936  2248 HOH HOH A . 
E 5 HOH 437 937  2498 HOH HOH A . 
E 5 HOH 438 938  2117 HOH HOH A . 
E 5 HOH 439 939  2345 HOH HOH A . 
E 5 HOH 440 940  2505 HOH HOH A . 
E 5 HOH 441 941  2567 HOH HOH A . 
E 5 HOH 442 942  2139 HOH HOH A . 
E 5 HOH 443 943  2638 HOH HOH A . 
E 5 HOH 444 944  2337 HOH HOH A . 
E 5 HOH 445 945  2592 HOH HOH A . 
E 5 HOH 446 946  2349 HOH HOH A . 
E 5 HOH 447 947  2254 HOH HOH A . 
E 5 HOH 448 948  2247 HOH HOH A . 
E 5 HOH 449 949  2396 HOH HOH A . 
E 5 HOH 450 950  2379 HOH HOH A . 
E 5 HOH 451 951  2266 HOH HOH A . 
E 5 HOH 452 952  2591 HOH HOH A . 
E 5 HOH 453 953  2339 HOH HOH A . 
E 5 HOH 454 954  2457 HOH HOH A . 
E 5 HOH 455 955  2158 HOH HOH A . 
E 5 HOH 456 956  2572 HOH HOH A . 
E 5 HOH 457 957  2565 HOH HOH A . 
E 5 HOH 458 958  2189 HOH HOH A . 
E 5 HOH 459 959  2369 HOH HOH A . 
E 5 HOH 460 960  2643 HOH HOH A . 
E 5 HOH 461 961  2216 HOH HOH A . 
E 5 HOH 462 962  2113 HOH HOH A . 
E 5 HOH 463 963  2204 HOH HOH A . 
E 5 HOH 464 964  2492 HOH HOH A . 
E 5 HOH 465 965  2543 HOH HOH A . 
E 5 HOH 466 966  2238 HOH HOH A . 
E 5 HOH 467 967  2391 HOH HOH A . 
E 5 HOH 468 968  2308 HOH HOH A . 
E 5 HOH 469 969  2265 HOH HOH A . 
E 5 HOH 470 970  2233 HOH HOH A . 
E 5 HOH 471 971  2488 HOH HOH A . 
E 5 HOH 472 972  2621 HOH HOH A . 
E 5 HOH 473 973  2219 HOH HOH A . 
E 5 HOH 474 974  2544 HOH HOH A . 
E 5 HOH 475 975  2160 HOH HOH A . 
E 5 HOH 476 976  2503 HOH HOH A . 
E 5 HOH 477 977  2561 HOH HOH A . 
E 5 HOH 478 978  2370 HOH HOH A . 
E 5 HOH 479 979  2587 HOH HOH A . 
E 5 HOH 480 980  2536 HOH HOH A . 
E 5 HOH 481 981  2574 HOH HOH A . 
E 5 HOH 482 982  2599 HOH HOH A . 
E 5 HOH 483 983  2305 HOH HOH A . 
E 5 HOH 484 984  2344 HOH HOH A . 
E 5 HOH 485 985  2451 HOH HOH A . 
E 5 HOH 486 986  2545 HOH HOH A . 
E 5 HOH 487 987  2165 HOH HOH A . 
E 5 HOH 488 988  2406 HOH HOH A . 
E 5 HOH 489 989  2557 HOH HOH A . 
E 5 HOH 490 990  2140 HOH HOH A . 
E 5 HOH 491 991  2340 HOH HOH A . 
E 5 HOH 492 992  2338 HOH HOH A . 
E 5 HOH 493 993  2304 HOH HOH A . 
E 5 HOH 494 994  2534 HOH HOH A . 
E 5 HOH 495 995  2347 HOH HOH A . 
E 5 HOH 496 996  2105 HOH HOH A . 
E 5 HOH 497 997  2523 HOH HOH A . 
E 5 HOH 498 998  2633 HOH HOH A . 
E 5 HOH 499 999  2575 HOH HOH A . 
E 5 HOH 500 1000 2341 HOH HOH A . 
E 5 HOH 501 1001 2564 HOH HOH A . 
E 5 HOH 502 1002 2428 HOH HOH A . 
E 5 HOH 503 1003 2364 HOH HOH A . 
E 5 HOH 504 1004 2642 HOH HOH A . 
E 5 HOH 505 1005 2525 HOH HOH A . 
E 5 HOH 506 1006 2223 HOH HOH A . 
E 5 HOH 507 1007 2585 HOH HOH A . 
E 5 HOH 508 1008 2335 HOH HOH A . 
E 5 HOH 509 1009 2606 HOH HOH A . 
E 5 HOH 510 1010 2530 HOH HOH A . 
E 5 HOH 511 1011 2282 HOH HOH A . 
E 5 HOH 512 1012 2300 HOH HOH A . 
E 5 HOH 513 1013 2600 HOH HOH A . 
E 5 HOH 514 1014 2423 HOH HOH A . 
E 5 HOH 515 1015 2382 HOH HOH A . 
E 5 HOH 516 1016 2170 HOH HOH A . 
E 5 HOH 517 1017 2537 HOH HOH A . 
E 5 HOH 518 1018 2230 HOH HOH A . 
E 5 HOH 519 1019 2194 HOH HOH A . 
E 5 HOH 520 1020 2185 HOH HOH A . 
E 5 HOH 521 1021 2348 HOH HOH A . 
E 5 HOH 522 1022 2277 HOH HOH A . 
E 5 HOH 523 1023 2481 HOH HOH A . 
E 5 HOH 524 1024 2474 HOH HOH A . 
E 5 HOH 525 1025 2532 HOH HOH A . 
E 5 HOH 526 1026 2362 HOH HOH A . 
E 5 HOH 527 1027 2563 HOH HOH A . 
E 5 HOH 528 1028 2273 HOH HOH A . 
E 5 HOH 529 1029 2577 HOH HOH A . 
E 5 HOH 530 1030 2276 HOH HOH A . 
E 5 HOH 531 1031 2166 HOH HOH A . 
E 5 HOH 532 1032 2272 HOH HOH A . 
E 5 HOH 533 1033 2552 HOH HOH A . 
E 5 HOH 534 1034 2598 HOH HOH A . 
E 5 HOH 535 1035 2506 HOH HOH A . 
E 5 HOH 536 1036 2576 HOH HOH A . 
E 5 HOH 537 1037 2178 HOH HOH A . 
E 5 HOH 538 1038 2631 HOH HOH A . 
E 5 HOH 539 1039 2324 HOH HOH A . 
E 5 HOH 540 1040 2263 HOH HOH A . 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 310   ? 
1 MORE         -13   ? 
1 'SSA (A^2)'  14450 ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  OD1 ? A ASP 60  ? A ASP 60  ? 1_555 FE ? B FE . ? A FE 401 ? 1_555 OH  ? A TYR 92  ? A TYR 92  ? 1_555 86.2  ? 
2  OD1 ? A ASP 60  ? A ASP 60  ? 1_555 FE ? B FE . ? A FE 401 ? 1_555 OH  ? A TYR 191 ? A TYR 191 ? 1_555 173.8 ? 
3  OH  ? A TYR 92  ? A TYR 92  ? 1_555 FE ? B FE . ? A FE 401 ? 1_555 OH  ? A TYR 191 ? A TYR 191 ? 1_555 95.9  ? 
4  OD1 ? A ASP 60  ? A ASP 60  ? 1_555 FE ? B FE . ? A FE 401 ? 1_555 NE2 ? A HIS 250 ? A HIS 250 ? 1_555 88.3  ? 
5  OH  ? A TYR 92  ? A TYR 92  ? 1_555 FE ? B FE . ? A FE 401 ? 1_555 NE2 ? A HIS 250 ? A HIS 250 ? 1_555 96.4  ? 
6  OH  ? A TYR 191 ? A TYR 191 ? 1_555 FE ? B FE . ? A FE 401 ? 1_555 NE2 ? A HIS 250 ? A HIS 250 ? 1_555 85.8  ? 
7  OD1 ? A ASP 60  ? A ASP 60  ? 1_555 FE ? B FE . ? A FE 401 ? 1_555 O1  ? C CO3 .   ? A CO3 402 ? 1_555 86.5  ? 
8  OH  ? A TYR 92  ? A TYR 92  ? 1_555 FE ? B FE . ? A FE 401 ? 1_555 O1  ? C CO3 .   ? A CO3 402 ? 1_555 156.8 ? 
9  OH  ? A TYR 191 ? A TYR 191 ? 1_555 FE ? B FE . ? A FE 401 ? 1_555 O1  ? C CO3 .   ? A CO3 402 ? 1_555 93.6  ? 
10 NE2 ? A HIS 250 ? A HIS 250 ? 1_555 FE ? B FE . ? A FE 401 ? 1_555 O1  ? C CO3 .   ? A CO3 402 ? 1_555 105.4 ? 
11 OD1 ? A ASP 60  ? A ASP 60  ? 1_555 FE ? B FE . ? A FE 401 ? 1_555 O3  ? C CO3 .   ? A CO3 402 ? 1_555 87.6  ? 
12 OH  ? A TYR 92  ? A TYR 92  ? 1_555 FE ? B FE . ? A FE 401 ? 1_555 O3  ? C CO3 .   ? A CO3 402 ? 1_555 96.2  ? 
13 OH  ? A TYR 191 ? A TYR 191 ? 1_555 FE ? B FE . ? A FE 401 ? 1_555 O3  ? C CO3 .   ? A CO3 402 ? 1_555 97.9  ? 
14 NE2 ? A HIS 250 ? A HIS 250 ? 1_555 FE ? B FE . ? A FE 401 ? 1_555 O3  ? C CO3 .   ? A CO3 402 ? 1_555 166.5 ? 
15 O1  ? C CO3 .   ? A CO3 402 ? 1_555 FE ? B FE . ? A FE 401 ? 1_555 O3  ? C CO3 .   ? A CO3 402 ? 1_555 61.5  ? 
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2023-12-13 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? SHELXL   ? ? ? . 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? . 2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? . 3 
# 
_pdbx_entry_details.entry_id                   8X3H 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   ? 
# 
_pdbx_validate_rmsd_bond.id                        1 
_pdbx_validate_rmsd_bond.PDB_model_num             1 
_pdbx_validate_rmsd_bond.auth_atom_id_1            C 
_pdbx_validate_rmsd_bond.auth_asym_id_1            A 
_pdbx_validate_rmsd_bond.auth_comp_id_1            ALA 
_pdbx_validate_rmsd_bond.auth_seq_id_1             1 
_pdbx_validate_rmsd_bond.PDB_ins_code_1            ? 
_pdbx_validate_rmsd_bond.label_alt_id_1            ? 
_pdbx_validate_rmsd_bond.auth_atom_id_2            N 
_pdbx_validate_rmsd_bond.auth_asym_id_2            A 
_pdbx_validate_rmsd_bond.auth_comp_id_2            PRO 
_pdbx_validate_rmsd_bond.auth_seq_id_2             2 
_pdbx_validate_rmsd_bond.PDB_ins_code_2            ? 
_pdbx_validate_rmsd_bond.label_alt_id_2            ? 
_pdbx_validate_rmsd_bond.bond_value                1.556 
_pdbx_validate_rmsd_bond.bond_target_value         1.338 
_pdbx_validate_rmsd_bond.bond_deviation            0.218 
_pdbx_validate_rmsd_bond.bond_standard_deviation   0.019 
_pdbx_validate_rmsd_bond.linker_flag               Y 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1  1 O  A ALA 1   ? ? C  A ALA 1   ? ? N   A PRO 2   ? ? 132.53 121.10 11.43  1.90 Y 
2  1 C  A ALA 1   ? ? N  A PRO 2   ? ? CA  A PRO 2   ? ? 105.29 119.30 -14.01 1.50 Y 
3  1 C  A ALA 1   ? ? N  A PRO 2   ? ? CD  A PRO 2   ? ? 143.34 128.40 14.94  2.10 Y 
4  1 C  A THR 102 ? B N  A GLU 103 ? B CA  A GLU 103 ? B 147.69 121.70 25.99  2.50 Y 
5  1 O  A GLU 103 ? B C  A GLU 103 ? B N   A PHE 104 ? B 110.84 122.70 -11.86 1.60 Y 
6  1 CB A PHE 104 ? A CG A PHE 104 ? A CD1 A PHE 104 ? A 125.57 120.80 4.77   0.70 N 
7  1 CB A GLU 139 ? B CG A GLU 139 ? B CD  A GLU 139 ? B 137.31 114.20 23.11  2.70 N 
8  1 CB A GLN 168 ? B CG A GLN 168 ? B CD  A GLN 168 ? B 128.99 111.60 17.39  2.60 N 
9  1 CG A GLN 168 ? B CD A GLN 168 ? B OE1 A GLN 168 ? B 108.48 121.60 -13.12 2.00 N 
10 1 CD A ARG 172 ? A NE A ARG 172 ? A CZ  A ARG 172 ? A 111.13 123.60 -12.47 1.40 N 
11 1 CD A ARG 172 ? B NE A ARG 172 ? B CZ  A ARG 172 ? B 132.34 123.60 8.74   1.40 N 
12 1 NE A ARG 172 ? A CZ A ARG 172 ? A NH1 A ARG 172 ? A 128.03 120.30 7.73   0.50 N 
13 1 NE A ARG 172 ? A CZ A ARG 172 ? A NH2 A ARG 172 ? A 112.13 120.30 -8.17  0.50 N 
14 1 CB A TYR 188 ? ? CG A TYR 188 ? ? CD1 A TYR 188 ? ? 124.99 121.00 3.99   0.60 N 
15 1 CB A ASP 222 ? A CG A ASP 222 ? A OD1 A ASP 222 ? A 128.97 118.30 10.67  0.90 N 
16 1 CB A ASP 222 ? A CG A ASP 222 ? A OD2 A ASP 222 ? A 110.64 118.30 -7.66  0.90 N 
17 1 CD A ARG 246 ? A NE A ARG 246 ? A CZ  A ARG 246 ? A 132.69 123.60 9.09   1.40 N 
18 1 CD A ARG 246 ? B NE A ARG 246 ? B CZ  A ARG 246 ? B 132.94 123.60 9.34   1.40 N 
19 1 NE A ARG 246 ? A CZ A ARG 246 ? A NH2 A ARG 246 ? A 125.95 120.30 5.65   0.50 N 
20 1 NE A ARG 246 ? B CZ A ARG 246 ? B NH2 A ARG 246 ? B 116.92 120.30 -3.38  0.50 N 
21 1 NE A ARG 309 ? A CZ A ARG 309 ? A NH1 A ARG 309 ? A 117.05 120.30 -3.25  0.50 N 
22 1 NE A ARG 309 ? A CZ A ARG 309 ? A NH2 A ARG 309 ? A 123.31 120.30 3.01   0.50 N 
23 1 CB A GLU 323 ? B CG A GLU 323 ? B CD  A GLU 323 ? B 136.56 114.20 22.36  2.70 N 
24 1 NE A ARG 332 ? A CZ A ARG 332 ? A NH2 A ARG 332 ? A 125.35 120.30 5.05   0.50 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 GLU A 103 ? A 64.57   -35.77 
2 1 GLU A 103 ? B 33.22   -2.30  
3 1 SER A 122 ? ? -60.69  -72.22 
4 1 TRP A 125 ? ? -147.96 -65.64 
5 1 PHE A 155 ? ? -90.38  -60.86 
6 1 ALA A 217 ? ? -145.39 55.62  
7 1 CYS A 242 ? ? -161.27 62.37  
8 1 LYS A 291 ? ? 179.97  175.70 
9 1 LEU A 299 ? ? 77.08   -51.64 
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      A 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       1040 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   6.20 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CO3 C    C  N N 74  
CO3 O1   O  N N 75  
CO3 O2   O  N N 76  
CO3 O3   O  N N 77  
CYS N    N  N N 78  
CYS CA   C  N R 79  
CYS C    C  N N 80  
CYS O    O  N N 81  
CYS CB   C  N N 82  
CYS SG   S  N N 83  
CYS OXT  O  N N 84  
CYS H    H  N N 85  
CYS H2   H  N N 86  
CYS HA   H  N N 87  
CYS HB2  H  N N 88  
CYS HB3  H  N N 89  
CYS HG   H  N N 90  
CYS HXT  H  N N 91  
FE  FE   FE N N 92  
GLN N    N  N N 93  
GLN CA   C  N S 94  
GLN C    C  N N 95  
GLN O    O  N N 96  
GLN CB   C  N N 97  
GLN CG   C  N N 98  
GLN CD   C  N N 99  
GLN OE1  O  N N 100 
GLN NE2  N  N N 101 
GLN OXT  O  N N 102 
GLN H    H  N N 103 
GLN H2   H  N N 104 
GLN HA   H  N N 105 
GLN HB2  H  N N 106 
GLN HB3  H  N N 107 
GLN HG2  H  N N 108 
GLN HG3  H  N N 109 
GLN HE21 H  N N 110 
GLN HE22 H  N N 111 
GLN HXT  H  N N 112 
GLU N    N  N N 113 
GLU CA   C  N S 114 
GLU C    C  N N 115 
GLU O    O  N N 116 
GLU CB   C  N N 117 
GLU CG   C  N N 118 
GLU CD   C  N N 119 
GLU OE1  O  N N 120 
GLU OE2  O  N N 121 
GLU OXT  O  N N 122 
GLU H    H  N N 123 
GLU H2   H  N N 124 
GLU HA   H  N N 125 
GLU HB2  H  N N 126 
GLU HB3  H  N N 127 
GLU HG2  H  N N 128 
GLU HG3  H  N N 129 
GLU HE2  H  N N 130 
GLU HXT  H  N N 131 
GLY N    N  N N 132 
GLY CA   C  N N 133 
GLY C    C  N N 134 
GLY O    O  N N 135 
GLY OXT  O  N N 136 
GLY H    H  N N 137 
GLY H2   H  N N 138 
GLY HA2  H  N N 139 
GLY HA3  H  N N 140 
GLY HXT  H  N N 141 
GOL C1   C  N N 142 
GOL O1   O  N N 143 
GOL C2   C  N N 144 
GOL O2   O  N N 145 
GOL C3   C  N N 146 
GOL O3   O  N N 147 
GOL H11  H  N N 148 
GOL H12  H  N N 149 
GOL HO1  H  N N 150 
GOL H2   H  N N 151 
GOL HO2  H  N N 152 
GOL H31  H  N N 153 
GOL H32  H  N N 154 
GOL HO3  H  N N 155 
HIS N    N  N N 156 
HIS CA   C  N S 157 
HIS C    C  N N 158 
HIS O    O  N N 159 
HIS CB   C  N N 160 
HIS CG   C  Y N 161 
HIS ND1  N  Y N 162 
HIS CD2  C  Y N 163 
HIS CE1  C  Y N 164 
HIS NE2  N  Y N 165 
HIS OXT  O  N N 166 
HIS H    H  N N 167 
HIS H2   H  N N 168 
HIS HA   H  N N 169 
HIS HB2  H  N N 170 
HIS HB3  H  N N 171 
HIS HD1  H  N N 172 
HIS HD2  H  N N 173 
HIS HE1  H  N N 174 
HIS HE2  H  N N 175 
HIS HXT  H  N N 176 
HOH O    O  N N 177 
HOH H1   H  N N 178 
HOH H2   H  N N 179 
ILE N    N  N N 180 
ILE CA   C  N S 181 
ILE C    C  N N 182 
ILE O    O  N N 183 
ILE CB   C  N S 184 
ILE CG1  C  N N 185 
ILE CG2  C  N N 186 
ILE CD1  C  N N 187 
ILE OXT  O  N N 188 
ILE H    H  N N 189 
ILE H2   H  N N 190 
ILE HA   H  N N 191 
ILE HB   H  N N 192 
ILE HG12 H  N N 193 
ILE HG13 H  N N 194 
ILE HG21 H  N N 195 
ILE HG22 H  N N 196 
ILE HG23 H  N N 197 
ILE HD11 H  N N 198 
ILE HD12 H  N N 199 
ILE HD13 H  N N 200 
ILE HXT  H  N N 201 
LEU N    N  N N 202 
LEU CA   C  N S 203 
LEU C    C  N N 204 
LEU O    O  N N 205 
LEU CB   C  N N 206 
LEU CG   C  N N 207 
LEU CD1  C  N N 208 
LEU CD2  C  N N 209 
LEU OXT  O  N N 210 
LEU H    H  N N 211 
LEU H2   H  N N 212 
LEU HA   H  N N 213 
LEU HB2  H  N N 214 
LEU HB3  H  N N 215 
LEU HG   H  N N 216 
LEU HD11 H  N N 217 
LEU HD12 H  N N 218 
LEU HD13 H  N N 219 
LEU HD21 H  N N 220 
LEU HD22 H  N N 221 
LEU HD23 H  N N 222 
LEU HXT  H  N N 223 
LYS N    N  N N 224 
LYS CA   C  N S 225 
LYS C    C  N N 226 
LYS O    O  N N 227 
LYS CB   C  N N 228 
LYS CG   C  N N 229 
LYS CD   C  N N 230 
LYS CE   C  N N 231 
LYS NZ   N  N N 232 
LYS OXT  O  N N 233 
LYS H    H  N N 234 
LYS H2   H  N N 235 
LYS HA   H  N N 236 
LYS HB2  H  N N 237 
LYS HB3  H  N N 238 
LYS HG2  H  N N 239 
LYS HG3  H  N N 240 
LYS HD2  H  N N 241 
LYS HD3  H  N N 242 
LYS HE2  H  N N 243 
LYS HE3  H  N N 244 
LYS HZ1  H  N N 245 
LYS HZ2  H  N N 246 
LYS HZ3  H  N N 247 
LYS HXT  H  N N 248 
MET N    N  N N 249 
MET CA   C  N S 250 
MET C    C  N N 251 
MET O    O  N N 252 
MET CB   C  N N 253 
MET CG   C  N N 254 
MET SD   S  N N 255 
MET CE   C  N N 256 
MET OXT  O  N N 257 
MET H    H  N N 258 
MET H2   H  N N 259 
MET HA   H  N N 260 
MET HB2  H  N N 261 
MET HB3  H  N N 262 
MET HG2  H  N N 263 
MET HG3  H  N N 264 
MET HE1  H  N N 265 
MET HE2  H  N N 266 
MET HE3  H  N N 267 
MET HXT  H  N N 268 
PHE N    N  N N 269 
PHE CA   C  N S 270 
PHE C    C  N N 271 
PHE O    O  N N 272 
PHE CB   C  N N 273 
PHE CG   C  Y N 274 
PHE CD1  C  Y N 275 
PHE CD2  C  Y N 276 
PHE CE1  C  Y N 277 
PHE CE2  C  Y N 278 
PHE CZ   C  Y N 279 
PHE OXT  O  N N 280 
PHE H    H  N N 281 
PHE H2   H  N N 282 
PHE HA   H  N N 283 
PHE HB2  H  N N 284 
PHE HB3  H  N N 285 
PHE HD1  H  N N 286 
PHE HD2  H  N N 287 
PHE HE1  H  N N 288 
PHE HE2  H  N N 289 
PHE HZ   H  N N 290 
PHE HXT  H  N N 291 
PRO N    N  N N 292 
PRO CA   C  N S 293 
PRO C    C  N N 294 
PRO O    O  N N 295 
PRO CB   C  N N 296 
PRO CG   C  N N 297 
PRO CD   C  N N 298 
PRO OXT  O  N N 299 
PRO H    H  N N 300 
PRO HA   H  N N 301 
PRO HB2  H  N N 302 
PRO HB3  H  N N 303 
PRO HG2  H  N N 304 
PRO HG3  H  N N 305 
PRO HD2  H  N N 306 
PRO HD3  H  N N 307 
PRO HXT  H  N N 308 
SER N    N  N N 309 
SER CA   C  N S 310 
SER C    C  N N 311 
SER O    O  N N 312 
SER CB   C  N N 313 
SER OG   O  N N 314 
SER OXT  O  N N 315 
SER H    H  N N 316 
SER H2   H  N N 317 
SER HA   H  N N 318 
SER HB2  H  N N 319 
SER HB3  H  N N 320 
SER HG   H  N N 321 
SER HXT  H  N N 322 
THR N    N  N N 323 
THR CA   C  N S 324 
THR C    C  N N 325 
THR O    O  N N 326 
THR CB   C  N R 327 
THR OG1  O  N N 328 
THR CG2  C  N N 329 
THR OXT  O  N N 330 
THR H    H  N N 331 
THR H2   H  N N 332 
THR HA   H  N N 333 
THR HB   H  N N 334 
THR HG1  H  N N 335 
THR HG21 H  N N 336 
THR HG22 H  N N 337 
THR HG23 H  N N 338 
THR HXT  H  N N 339 
TRP N    N  N N 340 
TRP CA   C  N S 341 
TRP C    C  N N 342 
TRP O    O  N N 343 
TRP CB   C  N N 344 
TRP CG   C  Y N 345 
TRP CD1  C  Y N 346 
TRP CD2  C  Y N 347 
TRP NE1  N  Y N 348 
TRP CE2  C  Y N 349 
TRP CE3  C  Y N 350 
TRP CZ2  C  Y N 351 
TRP CZ3  C  Y N 352 
TRP CH2  C  Y N 353 
TRP OXT  O  N N 354 
TRP H    H  N N 355 
TRP H2   H  N N 356 
TRP HA   H  N N 357 
TRP HB2  H  N N 358 
TRP HB3  H  N N 359 
TRP HD1  H  N N 360 
TRP HE1  H  N N 361 
TRP HE3  H  N N 362 
TRP HZ2  H  N N 363 
TRP HZ3  H  N N 364 
TRP HH2  H  N N 365 
TRP HXT  H  N N 366 
TYR N    N  N N 367 
TYR CA   C  N S 368 
TYR C    C  N N 369 
TYR O    O  N N 370 
TYR CB   C  N N 371 
TYR CG   C  Y N 372 
TYR CD1  C  Y N 373 
TYR CD2  C  Y N 374 
TYR CE1  C  Y N 375 
TYR CE2  C  Y N 376 
TYR CZ   C  Y N 377 
TYR OH   O  N N 378 
TYR OXT  O  N N 379 
TYR H    H  N N 380 
TYR H2   H  N N 381 
TYR HA   H  N N 382 
TYR HB2  H  N N 383 
TYR HB3  H  N N 384 
TYR HD1  H  N N 385 
TYR HD2  H  N N 386 
TYR HE1  H  N N 387 
TYR HE2  H  N N 388 
TYR HH   H  N N 389 
TYR HXT  H  N N 390 
VAL N    N  N N 391 
VAL CA   C  N S 392 
VAL C    C  N N 393 
VAL O    O  N N 394 
VAL CB   C  N N 395 
VAL CG1  C  N N 396 
VAL CG2  C  N N 397 
VAL OXT  O  N N 398 
VAL H    H  N N 399 
VAL H2   H  N N 400 
VAL HA   H  N N 401 
VAL HB   H  N N 402 
VAL HG11 H  N N 403 
VAL HG12 H  N N 404 
VAL HG13 H  N N 405 
VAL HG21 H  N N 406 
VAL HG22 H  N N 407 
VAL HG23 H  N N 408 
VAL HXT  H  N N 409 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CO3 C   O1   doub N N 70  
CO3 C   O2   sing N N 71  
CO3 C   O3   sing N N 72  
CYS N   CA   sing N N 73  
CYS N   H    sing N N 74  
CYS N   H2   sing N N 75  
CYS CA  C    sing N N 76  
CYS CA  CB   sing N N 77  
CYS CA  HA   sing N N 78  
CYS C   O    doub N N 79  
CYS C   OXT  sing N N 80  
CYS CB  SG   sing N N 81  
CYS CB  HB2  sing N N 82  
CYS CB  HB3  sing N N 83  
CYS SG  HG   sing N N 84  
CYS OXT HXT  sing N N 85  
GLN N   CA   sing N N 86  
GLN N   H    sing N N 87  
GLN N   H2   sing N N 88  
GLN CA  C    sing N N 89  
GLN CA  CB   sing N N 90  
GLN CA  HA   sing N N 91  
GLN C   O    doub N N 92  
GLN C   OXT  sing N N 93  
GLN CB  CG   sing N N 94  
GLN CB  HB2  sing N N 95  
GLN CB  HB3  sing N N 96  
GLN CG  CD   sing N N 97  
GLN CG  HG2  sing N N 98  
GLN CG  HG3  sing N N 99  
GLN CD  OE1  doub N N 100 
GLN CD  NE2  sing N N 101 
GLN NE2 HE21 sing N N 102 
GLN NE2 HE22 sing N N 103 
GLN OXT HXT  sing N N 104 
GLU N   CA   sing N N 105 
GLU N   H    sing N N 106 
GLU N   H2   sing N N 107 
GLU CA  C    sing N N 108 
GLU CA  CB   sing N N 109 
GLU CA  HA   sing N N 110 
GLU C   O    doub N N 111 
GLU C   OXT  sing N N 112 
GLU CB  CG   sing N N 113 
GLU CB  HB2  sing N N 114 
GLU CB  HB3  sing N N 115 
GLU CG  CD   sing N N 116 
GLU CG  HG2  sing N N 117 
GLU CG  HG3  sing N N 118 
GLU CD  OE1  doub N N 119 
GLU CD  OE2  sing N N 120 
GLU OE2 HE2  sing N N 121 
GLU OXT HXT  sing N N 122 
GLY N   CA   sing N N 123 
GLY N   H    sing N N 124 
GLY N   H2   sing N N 125 
GLY CA  C    sing N N 126 
GLY CA  HA2  sing N N 127 
GLY CA  HA3  sing N N 128 
GLY C   O    doub N N 129 
GLY C   OXT  sing N N 130 
GLY OXT HXT  sing N N 131 
GOL C1  O1   sing N N 132 
GOL C1  C2   sing N N 133 
GOL C1  H11  sing N N 134 
GOL C1  H12  sing N N 135 
GOL O1  HO1  sing N N 136 
GOL C2  O2   sing N N 137 
GOL C2  C3   sing N N 138 
GOL C2  H2   sing N N 139 
GOL O2  HO2  sing N N 140 
GOL C3  O3   sing N N 141 
GOL C3  H31  sing N N 142 
GOL C3  H32  sing N N 143 
GOL O3  HO3  sing N N 144 
HIS N   CA   sing N N 145 
HIS N   H    sing N N 146 
HIS N   H2   sing N N 147 
HIS CA  C    sing N N 148 
HIS CA  CB   sing N N 149 
HIS CA  HA   sing N N 150 
HIS C   O    doub N N 151 
HIS C   OXT  sing N N 152 
HIS CB  CG   sing N N 153 
HIS CB  HB2  sing N N 154 
HIS CB  HB3  sing N N 155 
HIS CG  ND1  sing Y N 156 
HIS CG  CD2  doub Y N 157 
HIS ND1 CE1  doub Y N 158 
HIS ND1 HD1  sing N N 159 
HIS CD2 NE2  sing Y N 160 
HIS CD2 HD2  sing N N 161 
HIS CE1 NE2  sing Y N 162 
HIS CE1 HE1  sing N N 163 
HIS NE2 HE2  sing N N 164 
HIS OXT HXT  sing N N 165 
HOH O   H1   sing N N 166 
HOH O   H2   sing N N 167 
ILE N   CA   sing N N 168 
ILE N   H    sing N N 169 
ILE N   H2   sing N N 170 
ILE CA  C    sing N N 171 
ILE CA  CB   sing N N 172 
ILE CA  HA   sing N N 173 
ILE C   O    doub N N 174 
ILE C   OXT  sing N N 175 
ILE CB  CG1  sing N N 176 
ILE CB  CG2  sing N N 177 
ILE CB  HB   sing N N 178 
ILE CG1 CD1  sing N N 179 
ILE CG1 HG12 sing N N 180 
ILE CG1 HG13 sing N N 181 
ILE CG2 HG21 sing N N 182 
ILE CG2 HG22 sing N N 183 
ILE CG2 HG23 sing N N 184 
ILE CD1 HD11 sing N N 185 
ILE CD1 HD12 sing N N 186 
ILE CD1 HD13 sing N N 187 
ILE OXT HXT  sing N N 188 
LEU N   CA   sing N N 189 
LEU N   H    sing N N 190 
LEU N   H2   sing N N 191 
LEU CA  C    sing N N 192 
LEU CA  CB   sing N N 193 
LEU CA  HA   sing N N 194 
LEU C   O    doub N N 195 
LEU C   OXT  sing N N 196 
LEU CB  CG   sing N N 197 
LEU CB  HB2  sing N N 198 
LEU CB  HB3  sing N N 199 
LEU CG  CD1  sing N N 200 
LEU CG  CD2  sing N N 201 
LEU CG  HG   sing N N 202 
LEU CD1 HD11 sing N N 203 
LEU CD1 HD12 sing N N 204 
LEU CD1 HD13 sing N N 205 
LEU CD2 HD21 sing N N 206 
LEU CD2 HD22 sing N N 207 
LEU CD2 HD23 sing N N 208 
LEU OXT HXT  sing N N 209 
LYS N   CA   sing N N 210 
LYS N   H    sing N N 211 
LYS N   H2   sing N N 212 
LYS CA  C    sing N N 213 
LYS CA  CB   sing N N 214 
LYS CA  HA   sing N N 215 
LYS C   O    doub N N 216 
LYS C   OXT  sing N N 217 
LYS CB  CG   sing N N 218 
LYS CB  HB2  sing N N 219 
LYS CB  HB3  sing N N 220 
LYS CG  CD   sing N N 221 
LYS CG  HG2  sing N N 222 
LYS CG  HG3  sing N N 223 
LYS CD  CE   sing N N 224 
LYS CD  HD2  sing N N 225 
LYS CD  HD3  sing N N 226 
LYS CE  NZ   sing N N 227 
LYS CE  HE2  sing N N 228 
LYS CE  HE3  sing N N 229 
LYS NZ  HZ1  sing N N 230 
LYS NZ  HZ2  sing N N 231 
LYS NZ  HZ3  sing N N 232 
LYS OXT HXT  sing N N 233 
MET N   CA   sing N N 234 
MET N   H    sing N N 235 
MET N   H2   sing N N 236 
MET CA  C    sing N N 237 
MET CA  CB   sing N N 238 
MET CA  HA   sing N N 239 
MET C   O    doub N N 240 
MET C   OXT  sing N N 241 
MET CB  CG   sing N N 242 
MET CB  HB2  sing N N 243 
MET CB  HB3  sing N N 244 
MET CG  SD   sing N N 245 
MET CG  HG2  sing N N 246 
MET CG  HG3  sing N N 247 
MET SD  CE   sing N N 248 
MET CE  HE1  sing N N 249 
MET CE  HE2  sing N N 250 
MET CE  HE3  sing N N 251 
MET OXT HXT  sing N N 252 
PHE N   CA   sing N N 253 
PHE N   H    sing N N 254 
PHE N   H2   sing N N 255 
PHE CA  C    sing N N 256 
PHE CA  CB   sing N N 257 
PHE CA  HA   sing N N 258 
PHE C   O    doub N N 259 
PHE C   OXT  sing N N 260 
PHE CB  CG   sing N N 261 
PHE CB  HB2  sing N N 262 
PHE CB  HB3  sing N N 263 
PHE CG  CD1  doub Y N 264 
PHE CG  CD2  sing Y N 265 
PHE CD1 CE1  sing Y N 266 
PHE CD1 HD1  sing N N 267 
PHE CD2 CE2  doub Y N 268 
PHE CD2 HD2  sing N N 269 
PHE CE1 CZ   doub Y N 270 
PHE CE1 HE1  sing N N 271 
PHE CE2 CZ   sing Y N 272 
PHE CE2 HE2  sing N N 273 
PHE CZ  HZ   sing N N 274 
PHE OXT HXT  sing N N 275 
PRO N   CA   sing N N 276 
PRO N   CD   sing N N 277 
PRO N   H    sing N N 278 
PRO CA  C    sing N N 279 
PRO CA  CB   sing N N 280 
PRO CA  HA   sing N N 281 
PRO C   O    doub N N 282 
PRO C   OXT  sing N N 283 
PRO CB  CG   sing N N 284 
PRO CB  HB2  sing N N 285 
PRO CB  HB3  sing N N 286 
PRO CG  CD   sing N N 287 
PRO CG  HG2  sing N N 288 
PRO CG  HG3  sing N N 289 
PRO CD  HD2  sing N N 290 
PRO CD  HD3  sing N N 291 
PRO OXT HXT  sing N N 292 
SER N   CA   sing N N 293 
SER N   H    sing N N 294 
SER N   H2   sing N N 295 
SER CA  C    sing N N 296 
SER CA  CB   sing N N 297 
SER CA  HA   sing N N 298 
SER C   O    doub N N 299 
SER C   OXT  sing N N 300 
SER CB  OG   sing N N 301 
SER CB  HB2  sing N N 302 
SER CB  HB3  sing N N 303 
SER OG  HG   sing N N 304 
SER OXT HXT  sing N N 305 
THR N   CA   sing N N 306 
THR N   H    sing N N 307 
THR N   H2   sing N N 308 
THR CA  C    sing N N 309 
THR CA  CB   sing N N 310 
THR CA  HA   sing N N 311 
THR C   O    doub N N 312 
THR C   OXT  sing N N 313 
THR CB  OG1  sing N N 314 
THR CB  CG2  sing N N 315 
THR CB  HB   sing N N 316 
THR OG1 HG1  sing N N 317 
THR CG2 HG21 sing N N 318 
THR CG2 HG22 sing N N 319 
THR CG2 HG23 sing N N 320 
THR OXT HXT  sing N N 321 
TRP N   CA   sing N N 322 
TRP N   H    sing N N 323 
TRP N   H2   sing N N 324 
TRP CA  C    sing N N 325 
TRP CA  CB   sing N N 326 
TRP CA  HA   sing N N 327 
TRP C   O    doub N N 328 
TRP C   OXT  sing N N 329 
TRP CB  CG   sing N N 330 
TRP CB  HB2  sing N N 331 
TRP CB  HB3  sing N N 332 
TRP CG  CD1  doub Y N 333 
TRP CG  CD2  sing Y N 334 
TRP CD1 NE1  sing Y N 335 
TRP CD1 HD1  sing N N 336 
TRP CD2 CE2  doub Y N 337 
TRP CD2 CE3  sing Y N 338 
TRP NE1 CE2  sing Y N 339 
TRP NE1 HE1  sing N N 340 
TRP CE2 CZ2  sing Y N 341 
TRP CE3 CZ3  doub Y N 342 
TRP CE3 HE3  sing N N 343 
TRP CZ2 CH2  doub Y N 344 
TRP CZ2 HZ2  sing N N 345 
TRP CZ3 CH2  sing Y N 346 
TRP CZ3 HZ3  sing N N 347 
TRP CH2 HH2  sing N N 348 
TRP OXT HXT  sing N N 349 
TYR N   CA   sing N N 350 
TYR N   H    sing N N 351 
TYR N   H2   sing N N 352 
TYR CA  C    sing N N 353 
TYR CA  CB   sing N N 354 
TYR CA  HA   sing N N 355 
TYR C   O    doub N N 356 
TYR C   OXT  sing N N 357 
TYR CB  CG   sing N N 358 
TYR CB  HB2  sing N N 359 
TYR CB  HB3  sing N N 360 
TYR CG  CD1  doub Y N 361 
TYR CG  CD2  sing Y N 362 
TYR CD1 CE1  sing Y N 363 
TYR CD1 HD1  sing N N 364 
TYR CD2 CE2  doub Y N 365 
TYR CD2 HD2  sing N N 366 
TYR CE1 CZ   doub Y N 367 
TYR CE1 HE1  sing N N 368 
TYR CE2 CZ   sing Y N 369 
TYR CE2 HE2  sing N N 370 
TYR CZ  OH   sing N N 371 
TYR OH  HH   sing N N 372 
TYR OXT HXT  sing N N 373 
VAL N   CA   sing N N 374 
VAL N   H    sing N N 375 
VAL N   H2   sing N N 376 
VAL CA  C    sing N N 377 
VAL CA  CB   sing N N 378 
VAL CA  HA   sing N N 379 
VAL C   O    doub N N 380 
VAL C   OXT  sing N N 381 
VAL CB  CG1  sing N N 382 
VAL CB  CG2  sing N N 383 
VAL CB  HB   sing N N 384 
VAL CG1 HG11 sing N N 385 
VAL CG1 HG12 sing N N 386 
VAL CG1 HG13 sing N N 387 
VAL CG2 HG21 sing N N 388 
VAL CG2 HG22 sing N N 389 
VAL CG2 HG23 sing N N 390 
VAL OXT HXT  sing N N 391 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 FE  ? ? FE  ? ? 'SUBJECT OF INVESTIGATION' ? 
2 CO3 ? ? CO3 ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'FE (III) ION'  FE  
3 'CARBONATE ION' CO3 
4 GLYCEROL        GOL 
5 water           HOH 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   1iej 
_pdbx_initial_refinement_model.details          'The model could be used for initial refinement and phasing.' 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
