data_1OSE
# 
_entry.id   1OSE 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.397 
_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   1OSE         pdb_00001ose 10.2210/pdb1ose/pdb 
WWPDB D_1000175503 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 1997-04-01 
2 'Structure model' 1 1 2008-03-24 
3 'Structure model' 1 2 2011-07-13 
4 'Structure model' 2 0 2019-12-25 
5 'Structure model' 3 0 2020-07-29 
6 'Structure model' 3 1 2024-10-09 
# 
loop_
_pdbx_audit_revision_details.ordinal 
_pdbx_audit_revision_details.revision_ordinal 
_pdbx_audit_revision_details.data_content_type 
_pdbx_audit_revision_details.provider 
_pdbx_audit_revision_details.type 
_pdbx_audit_revision_details.description 
_pdbx_audit_revision_details.details 
1 1 'Structure model' repository 'Initial release' ?                          ? 
2 5 'Structure model' repository Remediation       'Carbohydrate remediation' ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1  2 'Structure model' 'Version format compliance' 
2  3 'Structure model' 'Version format compliance' 
3  4 'Structure model' 'Data collection'           
4  4 'Structure model' 'Derived calculations'      
5  4 'Structure model' 'Polymer sequence'          
6  5 'Structure model' 'Atomic model'              
7  5 'Structure model' 'Data collection'           
8  5 'Structure model' 'Derived calculations'      
9  5 'Structure model' 'Structure summary'         
10 6 'Structure model' 'Data collection'           
11 6 'Structure model' 'Database references'       
12 6 'Structure model' 'Derived calculations'      
13 6 'Structure model' 'Structure summary'         
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1  4 'Structure model' chem_comp                     
2  4 'Structure model' entity_poly                   
3  4 'Structure model' pdbx_struct_mod_residue       
4  4 'Structure model' struct_conn                   
5  5 'Structure model' atom_site                     
6  5 'Structure model' chem_comp                     
7  5 'Structure model' entity                        
8  5 'Structure model' pdbx_branch_scheme            
9  5 'Structure model' pdbx_chem_comp_identifier     
10 5 'Structure model' pdbx_entity_branch            
11 5 'Structure model' pdbx_entity_branch_descriptor 
12 5 'Structure model' pdbx_entity_branch_link       
13 5 'Structure model' pdbx_entity_branch_list       
14 5 'Structure model' pdbx_entity_nonpoly           
15 5 'Structure model' pdbx_nonpoly_scheme           
16 5 'Structure model' pdbx_struct_assembly_gen      
17 5 'Structure model' pdbx_struct_conn_angle        
18 5 'Structure model' struct_asym                   
19 5 'Structure model' struct_conn                   
20 5 'Structure model' struct_site                   
21 5 'Structure model' struct_site_gen               
22 6 'Structure model' chem_comp                     
23 6 'Structure model' chem_comp_atom                
24 6 'Structure model' chem_comp_bond                
25 6 'Structure model' database_2                    
26 6 'Structure model' pdbx_entry_details            
27 6 'Structure model' pdbx_modification_feature     
28 6 'Structure model' struct_conn                   
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1  4 'Structure model' '_chem_comp.type'                             
2  4 'Structure model' '_entity_poly.pdbx_seq_one_letter_code_can'   
3  4 'Structure model' '_pdbx_struct_mod_residue.parent_comp_id'     
4  4 'Structure model' '_struct_conn.pdbx_leaving_atom_flag'         
5  5 'Structure model' '_atom_site.B_iso_or_equiv'                   
6  5 'Structure model' '_atom_site.Cartn_x'                          
7  5 'Structure model' '_atom_site.Cartn_y'                          
8  5 'Structure model' '_atom_site.Cartn_z'                          
9  5 'Structure model' '_atom_site.auth_asym_id'                     
10 5 'Structure model' '_atom_site.auth_atom_id'                     
11 5 'Structure model' '_atom_site.auth_comp_id'                     
12 5 'Structure model' '_atom_site.auth_seq_id'                      
13 5 'Structure model' '_atom_site.label_asym_id'                    
14 5 'Structure model' '_atom_site.label_atom_id'                    
15 5 'Structure model' '_atom_site.label_comp_id'                    
16 5 'Structure model' '_atom_site.label_entity_id'                  
17 5 'Structure model' '_atom_site.type_symbol'                      
18 5 'Structure model' '_chem_comp.name'                             
19 5 'Structure model' '_chem_comp.type'                             
20 5 'Structure model' '_pdbx_struct_assembly_gen.asym_id_list'      
21 5 'Structure model' '_pdbx_struct_conn_angle.ptnr1_auth_comp_id'  
22 5 'Structure model' '_pdbx_struct_conn_angle.ptnr1_auth_seq_id'   
23 5 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_asym_id' 
24 5 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_atom_id' 
25 5 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_comp_id' 
26 5 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_seq_id'  
27 5 'Structure model' '_pdbx_struct_conn_angle.ptnr2_label_asym_id' 
28 5 'Structure model' '_pdbx_struct_conn_angle.ptnr3_auth_comp_id'  
29 5 'Structure model' '_pdbx_struct_conn_angle.ptnr3_auth_seq_id'   
30 5 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_asym_id' 
31 5 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_atom_id' 
32 5 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_comp_id' 
33 5 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_seq_id'  
34 5 'Structure model' '_pdbx_struct_conn_angle.value'               
35 5 'Structure model' '_struct_conn.conn_type_id'                   
36 5 'Structure model' '_struct_conn.id'                             
37 5 'Structure model' '_struct_conn.pdbx_dist_value'                
38 5 'Structure model' '_struct_conn.pdbx_leaving_atom_flag'         
39 5 'Structure model' '_struct_conn.ptnr1_auth_asym_id'             
40 5 'Structure model' '_struct_conn.ptnr1_auth_comp_id'             
41 5 'Structure model' '_struct_conn.ptnr1_auth_seq_id'              
42 5 'Structure model' '_struct_conn.ptnr1_label_asym_id'            
43 5 'Structure model' '_struct_conn.ptnr1_label_atom_id'            
44 5 'Structure model' '_struct_conn.ptnr1_label_comp_id'            
45 5 'Structure model' '_struct_conn.ptnr1_label_seq_id'             
46 5 'Structure model' '_struct_conn.ptnr2_auth_asym_id'             
47 5 'Structure model' '_struct_conn.ptnr2_auth_comp_id'             
48 5 'Structure model' '_struct_conn.ptnr2_auth_seq_id'              
49 5 'Structure model' '_struct_conn.ptnr2_label_asym_id'            
50 5 'Structure model' '_struct_conn.ptnr2_label_atom_id'            
51 5 'Structure model' '_struct_conn.ptnr2_label_comp_id'            
52 5 'Structure model' '_struct_conn.ptnr2_label_seq_id'             
53 6 'Structure model' '_chem_comp.pdbx_synonyms'                    
54 6 'Structure model' '_database_2.pdbx_DOI'                        
55 6 'Structure model' '_database_2.pdbx_database_accession'         
56 6 'Structure model' '_struct_conn.pdbx_leaving_atom_flag'         
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        1OSE 
_pdbx_database_status.recvd_initial_deposition_date   1996-03-20 
_pdbx_database_status.deposit_site                    ? 
_pdbx_database_status.process_site                    BNL 
_pdbx_database_status.SG_entry                        . 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.status_code_nmr_data            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Gilles, C.' 1 
'Payan, F.'  2 
# 
loop_
_citation.id 
_citation.title 
_citation.journal_abbrev 
_citation.journal_volume 
_citation.page_first 
_citation.page_last 
_citation.year 
_citation.journal_id_ASTM 
_citation.country 
_citation.journal_id_ISSN 
_citation.journal_id_CSD 
_citation.book_publisher 
_citation.pdbx_database_id_PubMed 
_citation.pdbx_database_id_DOI 
primary 'Crystal structure of pig pancreatic alpha-amylase isoenzyme II, in complex with the carbohydrate inhibitor acarbose.' 
Eur.J.Biochem. 238 561  569 1996 EJBCAI IX 0014-2956 0262 ? 8681972 10.1111/j.1432-1033.1996.0561z.x 
1       
;Carbohydrate Binding Sites in a Pancreatic Alpha-Amylase-Substrate Complex, Derived from X-Ray Structure Analysis at 2.1 A Resolution
;
'Protein Sci.' 4   747  ?   1995 PRCIEI US 0961-8368 0795 ? ?       ?                                
2       
;The Active Center of a Mammalian Alpha-Amylase. Structure of the Complex of a Pancreatic Alpha-Amylase with a Carbohydrate Inhibitor Refined to 2.2-A Resolution
;
Biochemistry   33  6284 ?   1994 BICHAW US 0006-2960 0033 ? ?       ?                                
3       'Structure and Molecular Model Refinement of Pig Pancreatic Alpha-Amylase at 2.1 A Resolution' J.Mol.Biol.    231 785  ?   
1993 JMOBAK UK 0022-2836 0070 ? ?       ?                                
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Gilles, C.'         1  ? 
primary 'Astier, J.P.'       2  ? 
primary 'Marchis-Mouren, G.' 3  ? 
primary 'Cambillau, C.'      4  ? 
primary 'Payan, F.'          5  ? 
1       'Qian, M.'           6  ? 
1       'Haser, R.'          7  ? 
1       'Payan, F.'          8  ? 
2       'Qian, M.'           9  ? 
2       'Haser, R.'          10 ? 
2       'Buisson, G.'        11 ? 
2       'Duee, E.'           12 ? 
2       'Payan, F.'          13 ? 
3       'Qian, M.'           14 ? 
3       'Haser, R.'          15 ? 
3       'Payan, F.'          16 ? 
# 
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     nat 'PORCINE ALPHA-AMYLASE' 55415.711 1   3.2.1.1 ? ? ? 
2 branched    man 
;4,6-dideoxy-4-{[(1S,4R,5S,6S)-4,5,6-trihydroxy-3-(hydroxymethyl)cyclohex-2-en-1-yl]amino}-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-4,6-dideoxy-4-{[(1S,4R,5S,6S)-4,5,6-trihydroxy-3-(hydroxymethyl)cyclohex-2-en-1-yl]amino}-alpha-D-glucopyranose-(1-4)-beta-D-glucopyranose
;
948.914   1   ?       ? ? ? 
3 non-polymer man beta-D-glucopyranose 180.156   1   ?       ? ? ? 
4 non-polymer syn 'CHLORIDE ION' 35.453    1   ?       ? ? ? 
5 non-polymer syn 'CALCIUM ION' 40.078    1   ?       ? ? ? 
6 water       nat water 18.015    403 ?       ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        PPA 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   yes 
_entity_poly.pdbx_seq_one_letter_code       
;(PCA)YAPQTQSGRTSIVHLFEWRWVDIALECERYLGPKGFGGVQVSPPNENIVVTNPSRPWWERYQPVSYKLCTRSGNE
NEFRDMVTRCNNVGVRIYVDAVINHMCGSGAAAGTGTTCGSYCNPGSREFPAVPYSAWDFNDGKCKTASGGIESYNDPYQ
VRDCQLVGLLDLALEKDYVRSMIADYLNKLIDIGVAGFRIDASKHMWPGDIKAVLDKLHNLNTNWFPAGSRPFIFQEVID
LGGEAIQSSEYFGNGRVTEFKYGAKLGTVVRKWSGEKMSYLKNWGEGWGFMPSDRALVFVDNHDNQRGHGAGGASILTFW
DARLYKVAVGFMLAHPYGFTRVMSSYRWARNFVNGEDVNDWIGPPNNNGVIKEVTINADTTCGNDWVCEHRWREIRNMVW
FRNVVDGEPFANWWDNGSNQVAFGRGNRGFIVFNNDDWQLSSTLQTGLPGGTYCDVISGDKVGNSCTGIKVYVSSDGTAQ
FSISNSAEDPFIAIHAESKL
;
_entity_poly.pdbx_seq_one_letter_code_can   
;QYAPQTQSGRTSIVHLFEWRWVDIALECERYLGPKGFGGVQVSPPNENIVVTNPSRPWWERYQPVSYKLCTRSGNENEFR
DMVTRCNNVGVRIYVDAVINHMCGSGAAAGTGTTCGSYCNPGSREFPAVPYSAWDFNDGKCKTASGGIESYNDPYQVRDC
QLVGLLDLALEKDYVRSMIADYLNKLIDIGVAGFRIDASKHMWPGDIKAVLDKLHNLNTNWFPAGSRPFIFQEVIDLGGE
AIQSSEYFGNGRVTEFKYGAKLGTVVRKWSGEKMSYLKNWGEGWGFMPSDRALVFVDNHDNQRGHGAGGASILTFWDARL
YKVAVGFMLAHPYGFTRVMSSYRWARNFVNGEDVNDWIGPPNNNGVIKEVTINADTTCGNDWVCEHRWREIRNMVWFRNV
VDGEPFANWWDNGSNQVAFGRGNRGFIVFNNDDWQLSSTLQTGLPGGTYCDVISGDKVGNSCTGIKVYVSSDGTAQFSIS
NSAEDPFIAIHAESKL
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 beta-D-glucopyranose BGC 
4 'CHLORIDE ION'       CL  
5 'CALCIUM ION'        CA  
6 water                HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   PCA n 
1 2   TYR n 
1 3   ALA n 
1 4   PRO n 
1 5   GLN n 
1 6   THR n 
1 7   GLN n 
1 8   SER n 
1 9   GLY n 
1 10  ARG n 
1 11  THR n 
1 12  SER n 
1 13  ILE n 
1 14  VAL n 
1 15  HIS n 
1 16  LEU n 
1 17  PHE n 
1 18  GLU n 
1 19  TRP n 
1 20  ARG n 
1 21  TRP n 
1 22  VAL n 
1 23  ASP n 
1 24  ILE n 
1 25  ALA n 
1 26  LEU n 
1 27  GLU n 
1 28  CYS n 
1 29  GLU n 
1 30  ARG n 
1 31  TYR n 
1 32  LEU n 
1 33  GLY n 
1 34  PRO n 
1 35  LYS n 
1 36  GLY n 
1 37  PHE n 
1 38  GLY n 
1 39  GLY n 
1 40  VAL n 
1 41  GLN n 
1 42  VAL n 
1 43  SER n 
1 44  PRO n 
1 45  PRO n 
1 46  ASN n 
1 47  GLU n 
1 48  ASN n 
1 49  ILE n 
1 50  VAL n 
1 51  VAL n 
1 52  THR n 
1 53  ASN n 
1 54  PRO n 
1 55  SER n 
1 56  ARG n 
1 57  PRO n 
1 58  TRP n 
1 59  TRP n 
1 60  GLU n 
1 61  ARG n 
1 62  TYR n 
1 63  GLN n 
1 64  PRO n 
1 65  VAL n 
1 66  SER n 
1 67  TYR n 
1 68  LYS n 
1 69  LEU n 
1 70  CYS n 
1 71  THR n 
1 72  ARG n 
1 73  SER n 
1 74  GLY n 
1 75  ASN n 
1 76  GLU n 
1 77  ASN n 
1 78  GLU n 
1 79  PHE n 
1 80  ARG n 
1 81  ASP n 
1 82  MET n 
1 83  VAL n 
1 84  THR n 
1 85  ARG n 
1 86  CYS n 
1 87  ASN n 
1 88  ASN n 
1 89  VAL n 
1 90  GLY n 
1 91  VAL n 
1 92  ARG n 
1 93  ILE n 
1 94  TYR n 
1 95  VAL n 
1 96  ASP n 
1 97  ALA n 
1 98  VAL n 
1 99  ILE n 
1 100 ASN n 
1 101 HIS n 
1 102 MET n 
1 103 CYS n 
1 104 GLY n 
1 105 SER n 
1 106 GLY n 
1 107 ALA n 
1 108 ALA n 
1 109 ALA n 
1 110 GLY n 
1 111 THR n 
1 112 GLY n 
1 113 THR n 
1 114 THR n 
1 115 CYS n 
1 116 GLY n 
1 117 SER n 
1 118 TYR n 
1 119 CYS n 
1 120 ASN n 
1 121 PRO n 
1 122 GLY n 
1 123 SER n 
1 124 ARG n 
1 125 GLU n 
1 126 PHE n 
1 127 PRO n 
1 128 ALA n 
1 129 VAL n 
1 130 PRO n 
1 131 TYR n 
1 132 SER n 
1 133 ALA n 
1 134 TRP n 
1 135 ASP n 
1 136 PHE n 
1 137 ASN n 
1 138 ASP n 
1 139 GLY n 
1 140 LYS n 
1 141 CYS n 
1 142 LYS n 
1 143 THR n 
1 144 ALA n 
1 145 SER n 
1 146 GLY n 
1 147 GLY n 
1 148 ILE n 
1 149 GLU n 
1 150 SER n 
1 151 TYR n 
1 152 ASN n 
1 153 ASP n 
1 154 PRO n 
1 155 TYR n 
1 156 GLN n 
1 157 VAL n 
1 158 ARG n 
1 159 ASP n 
1 160 CYS n 
1 161 GLN n 
1 162 LEU n 
1 163 VAL n 
1 164 GLY n 
1 165 LEU n 
1 166 LEU n 
1 167 ASP n 
1 168 LEU n 
1 169 ALA n 
1 170 LEU n 
1 171 GLU n 
1 172 LYS n 
1 173 ASP n 
1 174 TYR n 
1 175 VAL n 
1 176 ARG n 
1 177 SER n 
1 178 MET n 
1 179 ILE n 
1 180 ALA n 
1 181 ASP n 
1 182 TYR n 
1 183 LEU n 
1 184 ASN n 
1 185 LYS n 
1 186 LEU n 
1 187 ILE n 
1 188 ASP n 
1 189 ILE n 
1 190 GLY n 
1 191 VAL n 
1 192 ALA n 
1 193 GLY n 
1 194 PHE n 
1 195 ARG n 
1 196 ILE n 
1 197 ASP n 
1 198 ALA n 
1 199 SER n 
1 200 LYS n 
1 201 HIS n 
1 202 MET n 
1 203 TRP n 
1 204 PRO n 
1 205 GLY n 
1 206 ASP n 
1 207 ILE n 
1 208 LYS n 
1 209 ALA n 
1 210 VAL n 
1 211 LEU n 
1 212 ASP n 
1 213 LYS n 
1 214 LEU n 
1 215 HIS n 
1 216 ASN n 
1 217 LEU n 
1 218 ASN n 
1 219 THR n 
1 220 ASN n 
1 221 TRP n 
1 222 PHE n 
1 223 PRO n 
1 224 ALA n 
1 225 GLY n 
1 226 SER n 
1 227 ARG n 
1 228 PRO n 
1 229 PHE n 
1 230 ILE n 
1 231 PHE n 
1 232 GLN n 
1 233 GLU n 
1 234 VAL n 
1 235 ILE n 
1 236 ASP n 
1 237 LEU n 
1 238 GLY n 
1 239 GLY n 
1 240 GLU n 
1 241 ALA n 
1 242 ILE n 
1 243 GLN n 
1 244 SER n 
1 245 SER n 
1 246 GLU n 
1 247 TYR n 
1 248 PHE n 
1 249 GLY n 
1 250 ASN n 
1 251 GLY n 
1 252 ARG n 
1 253 VAL n 
1 254 THR n 
1 255 GLU n 
1 256 PHE n 
1 257 LYS n 
1 258 TYR n 
1 259 GLY n 
1 260 ALA n 
1 261 LYS n 
1 262 LEU n 
1 263 GLY n 
1 264 THR n 
1 265 VAL n 
1 266 VAL n 
1 267 ARG n 
1 268 LYS n 
1 269 TRP n 
1 270 SER n 
1 271 GLY n 
1 272 GLU n 
1 273 LYS n 
1 274 MET n 
1 275 SER n 
1 276 TYR n 
1 277 LEU n 
1 278 LYS n 
1 279 ASN n 
1 280 TRP n 
1 281 GLY n 
1 282 GLU n 
1 283 GLY n 
1 284 TRP n 
1 285 GLY n 
1 286 PHE n 
1 287 MET n 
1 288 PRO n 
1 289 SER n 
1 290 ASP n 
1 291 ARG n 
1 292 ALA n 
1 293 LEU n 
1 294 VAL n 
1 295 PHE n 
1 296 VAL n 
1 297 ASP n 
1 298 ASN n 
1 299 HIS n 
1 300 ASP n 
1 301 ASN n 
1 302 GLN n 
1 303 ARG n 
1 304 GLY n 
1 305 HIS n 
1 306 GLY n 
1 307 ALA n 
1 308 GLY n 
1 309 GLY n 
1 310 ALA n 
1 311 SER n 
1 312 ILE n 
1 313 LEU n 
1 314 THR n 
1 315 PHE n 
1 316 TRP n 
1 317 ASP n 
1 318 ALA n 
1 319 ARG n 
1 320 LEU n 
1 321 TYR n 
1 322 LYS n 
1 323 VAL n 
1 324 ALA n 
1 325 VAL n 
1 326 GLY n 
1 327 PHE n 
1 328 MET n 
1 329 LEU n 
1 330 ALA n 
1 331 HIS n 
1 332 PRO n 
1 333 TYR n 
1 334 GLY n 
1 335 PHE n 
1 336 THR n 
1 337 ARG n 
1 338 VAL n 
1 339 MET n 
1 340 SER n 
1 341 SER n 
1 342 TYR n 
1 343 ARG n 
1 344 TRP n 
1 345 ALA n 
1 346 ARG n 
1 347 ASN n 
1 348 PHE n 
1 349 VAL n 
1 350 ASN n 
1 351 GLY n 
1 352 GLU n 
1 353 ASP n 
1 354 VAL n 
1 355 ASN n 
1 356 ASP n 
1 357 TRP n 
1 358 ILE n 
1 359 GLY n 
1 360 PRO n 
1 361 PRO n 
1 362 ASN n 
1 363 ASN n 
1 364 ASN n 
1 365 GLY n 
1 366 VAL n 
1 367 ILE n 
1 368 LYS n 
1 369 GLU n 
1 370 VAL n 
1 371 THR n 
1 372 ILE n 
1 373 ASN n 
1 374 ALA n 
1 375 ASP n 
1 376 THR n 
1 377 THR n 
1 378 CYS n 
1 379 GLY n 
1 380 ASN n 
1 381 ASP n 
1 382 TRP n 
1 383 VAL n 
1 384 CYS n 
1 385 GLU n 
1 386 HIS n 
1 387 ARG n 
1 388 TRP n 
1 389 ARG n 
1 390 GLU n 
1 391 ILE n 
1 392 ARG n 
1 393 ASN n 
1 394 MET n 
1 395 VAL n 
1 396 TRP n 
1 397 PHE n 
1 398 ARG n 
1 399 ASN n 
1 400 VAL n 
1 401 VAL n 
1 402 ASP n 
1 403 GLY n 
1 404 GLU n 
1 405 PRO n 
1 406 PHE n 
1 407 ALA n 
1 408 ASN n 
1 409 TRP n 
1 410 TRP n 
1 411 ASP n 
1 412 ASN n 
1 413 GLY n 
1 414 SER n 
1 415 ASN n 
1 416 GLN n 
1 417 VAL n 
1 418 ALA n 
1 419 PHE n 
1 420 GLY n 
1 421 ARG n 
1 422 GLY n 
1 423 ASN n 
1 424 ARG n 
1 425 GLY n 
1 426 PHE n 
1 427 ILE n 
1 428 VAL n 
1 429 PHE n 
1 430 ASN n 
1 431 ASN n 
1 432 ASP n 
1 433 ASP n 
1 434 TRP n 
1 435 GLN n 
1 436 LEU n 
1 437 SER n 
1 438 SER n 
1 439 THR n 
1 440 LEU n 
1 441 GLN n 
1 442 THR n 
1 443 GLY n 
1 444 LEU n 
1 445 PRO n 
1 446 GLY n 
1 447 GLY n 
1 448 THR n 
1 449 TYR n 
1 450 CYS n 
1 451 ASP n 
1 452 VAL n 
1 453 ILE n 
1 454 SER n 
1 455 GLY n 
1 456 ASP n 
1 457 LYS n 
1 458 VAL n 
1 459 GLY n 
1 460 ASN n 
1 461 SER n 
1 462 CYS n 
1 463 THR n 
1 464 GLY n 
1 465 ILE n 
1 466 LYS n 
1 467 VAL n 
1 468 TYR n 
1 469 VAL n 
1 470 SER n 
1 471 SER n 
1 472 ASP n 
1 473 GLY n 
1 474 THR n 
1 475 ALA n 
1 476 GLN n 
1 477 PHE n 
1 478 SER n 
1 479 ILE n 
1 480 SER n 
1 481 ASN n 
1 482 SER n 
1 483 ALA n 
1 484 GLU n 
1 485 ASP n 
1 486 PRO n 
1 487 PHE n 
1 488 ILE n 
1 489 ALA n 
1 490 ILE n 
1 491 HIS n 
1 492 ALA n 
1 493 GLU n 
1 494 SER n 
1 495 LYS n 
1 496 LEU n 
# 
_entity_src_nat.entity_id                  1 
_entity_src_nat.pdbx_src_id                1 
_entity_src_nat.pdbx_alt_source_flag       sample 
_entity_src_nat.pdbx_beg_seq_num           ? 
_entity_src_nat.pdbx_end_seq_num           ? 
_entity_src_nat.common_name                pig 
_entity_src_nat.pdbx_organism_scientific   'Sus scrofa' 
_entity_src_nat.pdbx_ncbi_taxonomy_id      9823 
_entity_src_nat.genus                      Sus 
_entity_src_nat.species                    ? 
_entity_src_nat.strain                     ? 
_entity_src_nat.tissue                     ? 
_entity_src_nat.tissue_fraction            ? 
_entity_src_nat.pdbx_secretion             ? 
_entity_src_nat.pdbx_fragment              ? 
_entity_src_nat.pdbx_variant               ? 
_entity_src_nat.pdbx_cell_line             ? 
_entity_src_nat.pdbx_atcc                  ? 
_entity_src_nat.pdbx_cellular_location     ? 
_entity_src_nat.pdbx_organ                 PANCREAS 
_entity_src_nat.pdbx_organelle             ? 
_entity_src_nat.pdbx_cell                  ? 
_entity_src_nat.pdbx_plasmid_name          ? 
_entity_src_nat.pdbx_plasmid_details       ? 
_entity_src_nat.details                    ? 
# 
_pdbx_entity_branch.entity_id   2 
_pdbx_entity_branch.type        oligosaccharide 
# 
loop_
_pdbx_entity_branch_descriptor.ordinal 
_pdbx_entity_branch_descriptor.entity_id 
_pdbx_entity_branch_descriptor.descriptor 
_pdbx_entity_branch_descriptor.type 
_pdbx_entity_branch_descriptor.program 
_pdbx_entity_branch_descriptor.program_version 
1 2 
;WURCS=2.0/4,4,3/[a2122h-1b_1-5][a2122m-1a_1-5][a2122h-1a_1-5][a2122m-1a_1-5_4*NC^SC^SC^SC^RCCO/7=^ZC$3/6O/5O/4O]/1-2-3-4/a4-b1_b4n2-c1n1*1OC^RC^RC^SC^SN*2/6C=^ZCCO/10$3/5O/4O_c4-d1
;
WURCS  PDB2Glycan 1.1.0 
2 2 
;[][b-D-Glcp]{[(4+1)][a-D-6-deoxy-Glcp4N]{[(4+1)][non_ch_ring]{[(4+1)][a-D-Glcp]{[(4+1)][a-D-6-deoxy-Glcp4N]{[(4+1)][&lt;C7O4&gt;]{}}}}}}
;
LINUCS PDB-CARE   ?     
# 
loop_
_pdbx_entity_branch_link.link_id 
_pdbx_entity_branch_link.entity_id 
_pdbx_entity_branch_link.entity_branch_list_num_1 
_pdbx_entity_branch_link.comp_id_1 
_pdbx_entity_branch_link.atom_id_1 
_pdbx_entity_branch_link.leaving_atom_id_1 
_pdbx_entity_branch_link.entity_branch_list_num_2 
_pdbx_entity_branch_link.comp_id_2 
_pdbx_entity_branch_link.atom_id_2 
_pdbx_entity_branch_link.leaving_atom_id_2 
_pdbx_entity_branch_link.value_order 
_pdbx_entity_branch_link.details 
1 2 2 AC1 C1 O1 1 BGC O4 HO4 sing ? 
2 2 3 GLC C1 O1 2 AC1 O4 HO4 sing ? 
3 2 4 AC1 C1 O1 3 GLC O4 HO4 sing ? 
# 
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 
AC1 D-saccharide                  . 
'4,6-dideoxy-4-{[(1S,4R,5S,6S)-4,5,6-trihydroxy-3-(hydroxymethyl)cyclohex-2-en-1-yl]amino}-alpha-D-glucopyranose' 
;6-METHYL-5-(4,5,6-TRIHYDROXY-3-HYDROXYMETHYL-CYCLOHEX-2-ENYLAMINO)-TETRAHYDRO-PYRAN-2,3,4-TRIOL; 4,6-dideoxy-4-{[(1S,4R,5S,6S)-4,5,6-trihydroxy-3-(hydroxymethyl)cyclohex-2-en-1-yl]amino}-alpha-D-glucose; 4,6-dideoxy-4-{[(1S,4R,5S,6S)-4,5,6-trihydroxy-3-(hydroxymethyl)cyclohex-2-en-1-yl]amino}-D-glucose; 4,6-dideoxy-4-{[(1S,4R,5S,6S)-4,5,6-trihydroxy-3-(hydroxymethyl)cyclohex-2-en-1-yl]amino}-glucose
;
'C13 H23 N O8'   321.324 
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 
BGC 'D-saccharide, beta linking'  . beta-D-glucopyranose 'beta-D-glucose; D-glucose; glucose' 'C6 H12 O6'      180.156 
CA  non-polymer                   . 'CALCIUM ION' ? 'Ca 2'           40.078  
CL  non-polymer                   . 'CHLORIDE ION' ? 'Cl -1'          35.453  
CYS 'L-peptide linking'           y CYSTEINE ? 'C3 H7 N O2 S'   121.158 
GLC 'D-saccharide, alpha linking' . alpha-D-glucopyranose 'alpha-D-glucose; D-glucose; glucose' 'C6 H12 O6'      180.156 
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  
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 
PCA 'L-peptide linking'           n 'PYROGLUTAMIC ACID' ? 'C5 H7 N O3'     129.114 
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 
# 
loop_
_pdbx_chem_comp_identifier.comp_id 
_pdbx_chem_comp_identifier.type 
_pdbx_chem_comp_identifier.program 
_pdbx_chem_comp_identifier.program_version 
_pdbx_chem_comp_identifier.identifier 
BGC 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DGlcpb            
BGC 'COMMON NAME'                         GMML     1.0 b-D-glucopyranose 
BGC 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 b-D-Glcp          
BGC 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 Glc               
GLC 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DGlcpa            
GLC 'COMMON NAME'                         GMML     1.0 a-D-glucopyranose 
GLC 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 a-D-Glcp          
GLC 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 Glc               
# 
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   PCA 1   1   1   PCA PCA A . n 
A 1 2   TYR 2   2   2   TYR TYR A . n 
A 1 3   ALA 3   3   3   ALA ALA A . n 
A 1 4   PRO 4   4   4   PRO PRO A . n 
A 1 5   GLN 5   5   5   GLN GLN A . n 
A 1 6   THR 6   6   6   THR THR A . n 
A 1 7   GLN 7   7   7   GLN GLN A . n 
A 1 8   SER 8   8   8   SER SER A . n 
A 1 9   GLY 9   9   9   GLY GLY A . n 
A 1 10  ARG 10  10  10  ARG ARG A . n 
A 1 11  THR 11  11  11  THR THR A . n 
A 1 12  SER 12  12  12  SER SER A . n 
A 1 13  ILE 13  13  13  ILE ILE A . n 
A 1 14  VAL 14  14  14  VAL VAL A . n 
A 1 15  HIS 15  15  15  HIS HIS A . n 
A 1 16  LEU 16  16  16  LEU LEU A . n 
A 1 17  PHE 17  17  17  PHE PHE A . n 
A 1 18  GLU 18  18  18  GLU GLU A . n 
A 1 19  TRP 19  19  19  TRP TRP A . n 
A 1 20  ARG 20  20  20  ARG ARG A . n 
A 1 21  TRP 21  21  21  TRP TRP A . n 
A 1 22  VAL 22  22  22  VAL VAL A . n 
A 1 23  ASP 23  23  23  ASP ASP A . n 
A 1 24  ILE 24  24  24  ILE ILE A . n 
A 1 25  ALA 25  25  25  ALA ALA A . n 
A 1 26  LEU 26  26  26  LEU LEU A . n 
A 1 27  GLU 27  27  27  GLU GLU A . n 
A 1 28  CYS 28  28  28  CYS CYS A . n 
A 1 29  GLU 29  29  29  GLU GLU A . n 
A 1 30  ARG 30  30  30  ARG ARG A . n 
A 1 31  TYR 31  31  31  TYR TYR A . n 
A 1 32  LEU 32  32  32  LEU LEU A . n 
A 1 33  GLY 33  33  33  GLY GLY A . n 
A 1 34  PRO 34  34  34  PRO PRO A . n 
A 1 35  LYS 35  35  35  LYS LYS A . n 
A 1 36  GLY 36  36  36  GLY GLY A . n 
A 1 37  PHE 37  37  37  PHE PHE A . n 
A 1 38  GLY 38  38  38  GLY GLY A . n 
A 1 39  GLY 39  39  39  GLY GLY A . n 
A 1 40  VAL 40  40  40  VAL VAL A . n 
A 1 41  GLN 41  41  41  GLN GLN A . n 
A 1 42  VAL 42  42  42  VAL VAL A . n 
A 1 43  SER 43  43  43  SER SER A . n 
A 1 44  PRO 44  44  44  PRO PRO A . n 
A 1 45  PRO 45  45  45  PRO PRO A . n 
A 1 46  ASN 46  46  46  ASN ASN A . n 
A 1 47  GLU 47  47  47  GLU GLU A . n 
A 1 48  ASN 48  48  48  ASN ASN A . n 
A 1 49  ILE 49  49  49  ILE ILE A . n 
A 1 50  VAL 50  50  50  VAL VAL A . n 
A 1 51  VAL 51  51  51  VAL VAL A . n 
A 1 52  THR 52  52  52  THR THR A . n 
A 1 53  ASN 53  53  53  ASN ASN A . n 
A 1 54  PRO 54  54  54  PRO PRO A . n 
A 1 55  SER 55  55  55  SER SER A . n 
A 1 56  ARG 56  56  56  ARG ARG A . n 
A 1 57  PRO 57  57  57  PRO PRO A . n 
A 1 58  TRP 58  58  58  TRP TRP A . n 
A 1 59  TRP 59  59  59  TRP TRP A . n 
A 1 60  GLU 60  60  60  GLU GLU A . n 
A 1 61  ARG 61  61  61  ARG ARG A . n 
A 1 62  TYR 62  62  62  TYR TYR A . n 
A 1 63  GLN 63  63  63  GLN GLN A . n 
A 1 64  PRO 64  64  64  PRO PRO A . n 
A 1 65  VAL 65  65  65  VAL VAL A . n 
A 1 66  SER 66  66  66  SER SER A . n 
A 1 67  TYR 67  67  67  TYR TYR A . n 
A 1 68  LYS 68  68  68  LYS LYS A . n 
A 1 69  LEU 69  69  69  LEU LEU A . n 
A 1 70  CYS 70  70  70  CYS CYS A . n 
A 1 71  THR 71  71  71  THR THR A . n 
A 1 72  ARG 72  72  72  ARG ARG A . n 
A 1 73  SER 73  73  73  SER SER A . n 
A 1 74  GLY 74  74  74  GLY GLY A . n 
A 1 75  ASN 75  75  75  ASN ASN A . n 
A 1 76  GLU 76  76  76  GLU GLU A . n 
A 1 77  ASN 77  77  77  ASN ASN A . n 
A 1 78  GLU 78  78  78  GLU GLU A . n 
A 1 79  PHE 79  79  79  PHE PHE A . n 
A 1 80  ARG 80  80  80  ARG ARG A . n 
A 1 81  ASP 81  81  81  ASP ASP A . n 
A 1 82  MET 82  82  82  MET MET A . n 
A 1 83  VAL 83  83  83  VAL VAL A . n 
A 1 84  THR 84  84  84  THR THR A . n 
A 1 85  ARG 85  85  85  ARG ARG A . n 
A 1 86  CYS 86  86  86  CYS CYS A . n 
A 1 87  ASN 87  87  87  ASN ASN A . n 
A 1 88  ASN 88  88  88  ASN ASN A . n 
A 1 89  VAL 89  89  89  VAL VAL A . n 
A 1 90  GLY 90  90  90  GLY GLY A . n 
A 1 91  VAL 91  91  91  VAL VAL A . n 
A 1 92  ARG 92  92  92  ARG ARG A . n 
A 1 93  ILE 93  93  93  ILE ILE A . n 
A 1 94  TYR 94  94  94  TYR TYR A . n 
A 1 95  VAL 95  95  95  VAL VAL A . n 
A 1 96  ASP 96  96  96  ASP ASP A . n 
A 1 97  ALA 97  97  97  ALA ALA A . n 
A 1 98  VAL 98  98  98  VAL VAL A . n 
A 1 99  ILE 99  99  99  ILE ILE A . n 
A 1 100 ASN 100 100 100 ASN ASN A . n 
A 1 101 HIS 101 101 101 HIS HIS A . n 
A 1 102 MET 102 102 102 MET MET A . n 
A 1 103 CYS 103 103 103 CYS CYS A . n 
A 1 104 GLY 104 104 104 GLY GLY A . n 
A 1 105 SER 105 105 105 SER SER A . n 
A 1 106 GLY 106 106 106 GLY GLY A . n 
A 1 107 ALA 107 107 107 ALA ALA A . n 
A 1 108 ALA 108 108 108 ALA ALA A . n 
A 1 109 ALA 109 109 109 ALA ALA A . n 
A 1 110 GLY 110 110 110 GLY GLY A . n 
A 1 111 THR 111 111 111 THR THR A . n 
A 1 112 GLY 112 112 112 GLY GLY A . n 
A 1 113 THR 113 113 113 THR THR A . n 
A 1 114 THR 114 114 114 THR THR A . n 
A 1 115 CYS 115 115 115 CYS CYS A . n 
A 1 116 GLY 116 116 116 GLY GLY A . n 
A 1 117 SER 117 117 117 SER SER A . n 
A 1 118 TYR 118 118 118 TYR TYR A . n 
A 1 119 CYS 119 119 119 CYS CYS A . n 
A 1 120 ASN 120 120 120 ASN ASN A . n 
A 1 121 PRO 121 121 121 PRO PRO A . n 
A 1 122 GLY 122 122 122 GLY GLY A . n 
A 1 123 SER 123 123 123 SER SER A . n 
A 1 124 ARG 124 124 124 ARG ARG A . n 
A 1 125 GLU 125 125 125 GLU GLU A . n 
A 1 126 PHE 126 126 126 PHE PHE A . n 
A 1 127 PRO 127 127 127 PRO PRO A . n 
A 1 128 ALA 128 128 128 ALA ALA A . n 
A 1 129 VAL 129 129 129 VAL VAL A . n 
A 1 130 PRO 130 130 130 PRO PRO A . n 
A 1 131 TYR 131 131 131 TYR TYR A . n 
A 1 132 SER 132 132 132 SER SER A . n 
A 1 133 ALA 133 133 133 ALA ALA A . n 
A 1 134 TRP 134 134 134 TRP TRP A . n 
A 1 135 ASP 135 135 135 ASP ASP A . n 
A 1 136 PHE 136 136 136 PHE PHE A . n 
A 1 137 ASN 137 137 137 ASN ASN A . n 
A 1 138 ASP 138 138 138 ASP ASP A . n 
A 1 139 GLY 139 139 139 GLY GLY A . n 
A 1 140 LYS 140 140 140 LYS LYS A . n 
A 1 141 CYS 141 141 141 CYS CYS A . n 
A 1 142 LYS 142 142 142 LYS LYS A . n 
A 1 143 THR 143 143 143 THR THR A . n 
A 1 144 ALA 144 144 144 ALA ALA 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 GLY 147 147 147 GLY GLY A . n 
A 1 148 ILE 148 148 148 ILE ILE A . n 
A 1 149 GLU 149 149 149 GLU GLU A . n 
A 1 150 SER 150 150 150 SER SER A . n 
A 1 151 TYR 151 151 151 TYR TYR A . n 
A 1 152 ASN 152 152 152 ASN ASN A . n 
A 1 153 ASP 153 153 153 ASP ASP A . n 
A 1 154 PRO 154 154 154 PRO PRO A . n 
A 1 155 TYR 155 155 155 TYR TYR A . n 
A 1 156 GLN 156 156 156 GLN GLN A . n 
A 1 157 VAL 157 157 157 VAL VAL A . n 
A 1 158 ARG 158 158 158 ARG ARG A . n 
A 1 159 ASP 159 159 159 ASP ASP A . n 
A 1 160 CYS 160 160 160 CYS CYS A . n 
A 1 161 GLN 161 161 161 GLN GLN A . n 
A 1 162 LEU 162 162 162 LEU LEU A . n 
A 1 163 VAL 163 163 163 VAL VAL A . n 
A 1 164 GLY 164 164 164 GLY GLY A . n 
A 1 165 LEU 165 165 165 LEU LEU A . n 
A 1 166 LEU 166 166 166 LEU LEU A . n 
A 1 167 ASP 167 167 167 ASP ASP A . n 
A 1 168 LEU 168 168 168 LEU LEU A . n 
A 1 169 ALA 169 169 169 ALA ALA A . n 
A 1 170 LEU 170 170 170 LEU LEU A . n 
A 1 171 GLU 171 171 171 GLU GLU A . n 
A 1 172 LYS 172 172 172 LYS LYS A . n 
A 1 173 ASP 173 173 173 ASP ASP A . n 
A 1 174 TYR 174 174 174 TYR TYR A . n 
A 1 175 VAL 175 175 175 VAL VAL A . n 
A 1 176 ARG 176 176 176 ARG ARG A . n 
A 1 177 SER 177 177 177 SER SER A . n 
A 1 178 MET 178 178 178 MET MET A . n 
A 1 179 ILE 179 179 179 ILE ILE A . n 
A 1 180 ALA 180 180 180 ALA ALA A . n 
A 1 181 ASP 181 181 181 ASP ASP A . n 
A 1 182 TYR 182 182 182 TYR TYR A . n 
A 1 183 LEU 183 183 183 LEU LEU A . n 
A 1 184 ASN 184 184 184 ASN ASN A . n 
A 1 185 LYS 185 185 185 LYS LYS A . n 
A 1 186 LEU 186 186 186 LEU LEU A . n 
A 1 187 ILE 187 187 187 ILE ILE A . n 
A 1 188 ASP 188 188 188 ASP ASP A . n 
A 1 189 ILE 189 189 189 ILE ILE A . n 
A 1 190 GLY 190 190 190 GLY GLY A . n 
A 1 191 VAL 191 191 191 VAL VAL A . n 
A 1 192 ALA 192 192 192 ALA ALA A . n 
A 1 193 GLY 193 193 193 GLY GLY A . n 
A 1 194 PHE 194 194 194 PHE PHE A . n 
A 1 195 ARG 195 195 195 ARG ARG A . n 
A 1 196 ILE 196 196 196 ILE ILE A . n 
A 1 197 ASP 197 197 197 ASP ASP A . n 
A 1 198 ALA 198 198 198 ALA ALA A . n 
A 1 199 SER 199 199 199 SER SER A . n 
A 1 200 LYS 200 200 200 LYS LYS A . n 
A 1 201 HIS 201 201 201 HIS HIS A . n 
A 1 202 MET 202 202 202 MET MET A . n 
A 1 203 TRP 203 203 203 TRP TRP A . n 
A 1 204 PRO 204 204 204 PRO PRO A . n 
A 1 205 GLY 205 205 205 GLY GLY A . n 
A 1 206 ASP 206 206 206 ASP ASP A . n 
A 1 207 ILE 207 207 207 ILE ILE A . n 
A 1 208 LYS 208 208 208 LYS LYS A . n 
A 1 209 ALA 209 209 209 ALA ALA A . n 
A 1 210 VAL 210 210 210 VAL VAL A . n 
A 1 211 LEU 211 211 211 LEU LEU A . n 
A 1 212 ASP 212 212 212 ASP ASP A . n 
A 1 213 LYS 213 213 213 LYS LYS A . n 
A 1 214 LEU 214 214 214 LEU LEU A . n 
A 1 215 HIS 215 215 215 HIS HIS A . n 
A 1 216 ASN 216 216 216 ASN ASN A . n 
A 1 217 LEU 217 217 217 LEU LEU A . n 
A 1 218 ASN 218 218 218 ASN ASN A . n 
A 1 219 THR 219 219 219 THR THR A . n 
A 1 220 ASN 220 220 220 ASN ASN A . n 
A 1 221 TRP 221 221 221 TRP TRP A . n 
A 1 222 PHE 222 222 222 PHE PHE A . n 
A 1 223 PRO 223 223 223 PRO PRO A . n 
A 1 224 ALA 224 224 224 ALA ALA A . n 
A 1 225 GLY 225 225 225 GLY GLY A . n 
A 1 226 SER 226 226 226 SER SER A . n 
A 1 227 ARG 227 227 227 ARG ARG A . n 
A 1 228 PRO 228 228 228 PRO PRO A . n 
A 1 229 PHE 229 229 229 PHE PHE A . n 
A 1 230 ILE 230 230 230 ILE ILE A . n 
A 1 231 PHE 231 231 231 PHE PHE A . n 
A 1 232 GLN 232 232 232 GLN GLN A . n 
A 1 233 GLU 233 233 233 GLU GLU A . n 
A 1 234 VAL 234 234 234 VAL VAL A . n 
A 1 235 ILE 235 235 235 ILE ILE A . n 
A 1 236 ASP 236 236 236 ASP ASP A . n 
A 1 237 LEU 237 237 237 LEU LEU A . n 
A 1 238 GLY 238 238 238 GLY GLY A . n 
A 1 239 GLY 239 239 239 GLY GLY A . n 
A 1 240 GLU 240 240 240 GLU GLU A . n 
A 1 241 ALA 241 241 241 ALA ALA A . n 
A 1 242 ILE 242 242 242 ILE ILE A . n 
A 1 243 GLN 243 243 243 GLN GLN A . n 
A 1 244 SER 244 244 244 SER SER A . n 
A 1 245 SER 245 245 245 SER SER A . n 
A 1 246 GLU 246 246 246 GLU GLU A . n 
A 1 247 TYR 247 247 247 TYR TYR A . n 
A 1 248 PHE 248 248 248 PHE PHE A . n 
A 1 249 GLY 249 249 249 GLY GLY A . n 
A 1 250 ASN 250 250 250 ASN ASN A . n 
A 1 251 GLY 251 251 251 GLY GLY A . n 
A 1 252 ARG 252 252 252 ARG ARG A . n 
A 1 253 VAL 253 253 253 VAL VAL A . n 
A 1 254 THR 254 254 254 THR THR A . n 
A 1 255 GLU 255 255 255 GLU GLU A . n 
A 1 256 PHE 256 256 256 PHE PHE A . n 
A 1 257 LYS 257 257 257 LYS LYS A . n 
A 1 258 TYR 258 258 258 TYR TYR A . n 
A 1 259 GLY 259 259 259 GLY GLY A . n 
A 1 260 ALA 260 260 260 ALA ALA A . n 
A 1 261 LYS 261 261 261 LYS LYS A . n 
A 1 262 LEU 262 262 262 LEU LEU A . n 
A 1 263 GLY 263 263 263 GLY GLY A . n 
A 1 264 THR 264 264 264 THR THR A . n 
A 1 265 VAL 265 265 265 VAL VAL A . n 
A 1 266 VAL 266 266 266 VAL VAL A . n 
A 1 267 ARG 267 267 267 ARG ARG A . n 
A 1 268 LYS 268 268 268 LYS LYS A . n 
A 1 269 TRP 269 269 269 TRP TRP A . n 
A 1 270 SER 270 270 270 SER SER A . n 
A 1 271 GLY 271 271 271 GLY GLY A . n 
A 1 272 GLU 272 272 272 GLU GLU A . n 
A 1 273 LYS 273 273 273 LYS LYS A . n 
A 1 274 MET 274 274 274 MET MET A . n 
A 1 275 SER 275 275 275 SER SER A . n 
A 1 276 TYR 276 276 276 TYR TYR A . n 
A 1 277 LEU 277 277 277 LEU LEU A . n 
A 1 278 LYS 278 278 278 LYS LYS A . n 
A 1 279 ASN 279 279 279 ASN ASN A . n 
A 1 280 TRP 280 280 280 TRP TRP A . n 
A 1 281 GLY 281 281 281 GLY GLY A . n 
A 1 282 GLU 282 282 282 GLU GLU A . n 
A 1 283 GLY 283 283 283 GLY GLY A . n 
A 1 284 TRP 284 284 284 TRP TRP A . n 
A 1 285 GLY 285 285 285 GLY GLY A . n 
A 1 286 PHE 286 286 286 PHE PHE A . n 
A 1 287 MET 287 287 287 MET MET A . n 
A 1 288 PRO 288 288 288 PRO PRO A . n 
A 1 289 SER 289 289 289 SER SER A . n 
A 1 290 ASP 290 290 290 ASP ASP A . n 
A 1 291 ARG 291 291 291 ARG ARG A . n 
A 1 292 ALA 292 292 292 ALA ALA A . n 
A 1 293 LEU 293 293 293 LEU LEU A . n 
A 1 294 VAL 294 294 294 VAL VAL A . n 
A 1 295 PHE 295 295 295 PHE PHE A . n 
A 1 296 VAL 296 296 296 VAL VAL A . n 
A 1 297 ASP 297 297 297 ASP ASP A . n 
A 1 298 ASN 298 298 298 ASN ASN A . n 
A 1 299 HIS 299 299 299 HIS HIS A . n 
A 1 300 ASP 300 300 300 ASP ASP A . n 
A 1 301 ASN 301 301 301 ASN ASN A . n 
A 1 302 GLN 302 302 302 GLN GLN A . n 
A 1 303 ARG 303 303 303 ARG ARG A . n 
A 1 304 GLY 304 304 304 GLY GLY A . n 
A 1 305 HIS 305 305 305 HIS HIS A . n 
A 1 306 GLY 306 306 306 GLY GLY A . n 
A 1 307 ALA 307 307 307 ALA ALA A . n 
A 1 308 GLY 308 308 308 GLY GLY A . n 
A 1 309 GLY 309 309 309 GLY GLY A . n 
A 1 310 ALA 310 310 310 ALA ALA A . n 
A 1 311 SER 311 311 311 SER SER A . n 
A 1 312 ILE 312 312 312 ILE ILE A . n 
A 1 313 LEU 313 313 313 LEU LEU A . n 
A 1 314 THR 314 314 314 THR THR A . n 
A 1 315 PHE 315 315 315 PHE PHE A . n 
A 1 316 TRP 316 316 316 TRP TRP A . n 
A 1 317 ASP 317 317 317 ASP ASP A . n 
A 1 318 ALA 318 318 318 ALA ALA A . n 
A 1 319 ARG 319 319 319 ARG ARG A . n 
A 1 320 LEU 320 320 320 LEU LEU A . n 
A 1 321 TYR 321 321 321 TYR TYR A . n 
A 1 322 LYS 322 322 322 LYS LYS A . n 
A 1 323 VAL 323 323 323 VAL VAL A . n 
A 1 324 ALA 324 324 324 ALA ALA A . n 
A 1 325 VAL 325 325 325 VAL VAL A . n 
A 1 326 GLY 326 326 326 GLY GLY A . n 
A 1 327 PHE 327 327 327 PHE PHE A . n 
A 1 328 MET 328 328 328 MET MET A . n 
A 1 329 LEU 329 329 329 LEU LEU A . n 
A 1 330 ALA 330 330 330 ALA ALA A . n 
A 1 331 HIS 331 331 331 HIS HIS A . n 
A 1 332 PRO 332 332 332 PRO PRO A . n 
A 1 333 TYR 333 333 333 TYR TYR A . n 
A 1 334 GLY 334 334 334 GLY GLY A . n 
A 1 335 PHE 335 335 335 PHE PHE A . n 
A 1 336 THR 336 336 336 THR THR A . n 
A 1 337 ARG 337 337 337 ARG ARG A . n 
A 1 338 VAL 338 338 338 VAL VAL A . n 
A 1 339 MET 339 339 339 MET MET A . n 
A 1 340 SER 340 340 340 SER SER A . n 
A 1 341 SER 341 341 341 SER SER A . n 
A 1 342 TYR 342 342 342 TYR TYR A . n 
A 1 343 ARG 343 343 343 ARG ARG A . n 
A 1 344 TRP 344 344 344 TRP TRP A . n 
A 1 345 ALA 345 345 345 ALA ALA A . n 
A 1 346 ARG 346 346 346 ARG ARG A . n 
A 1 347 ASN 347 347 347 ASN ASN A . n 
A 1 348 PHE 348 348 348 PHE PHE A . n 
A 1 349 VAL 349 349 349 VAL VAL A . n 
A 1 350 ASN 350 350 350 ASN ASN A . n 
A 1 351 GLY 351 351 351 GLY GLY A . n 
A 1 352 GLU 352 352 352 GLU GLU A . n 
A 1 353 ASP 353 353 353 ASP ASP A . n 
A 1 354 VAL 354 354 354 VAL VAL A . n 
A 1 355 ASN 355 355 355 ASN ASN A . n 
A 1 356 ASP 356 356 356 ASP ASP A . n 
A 1 357 TRP 357 357 357 TRP TRP A . n 
A 1 358 ILE 358 358 358 ILE ILE A . n 
A 1 359 GLY 359 359 359 GLY GLY A . n 
A 1 360 PRO 360 360 360 PRO PRO A . n 
A 1 361 PRO 361 361 361 PRO PRO A . n 
A 1 362 ASN 362 362 362 ASN ASN A . n 
A 1 363 ASN 363 363 363 ASN ASN A . n 
A 1 364 ASN 364 364 364 ASN ASN A . n 
A 1 365 GLY 365 365 365 GLY GLY A . n 
A 1 366 VAL 366 366 366 VAL VAL A . n 
A 1 367 ILE 367 367 367 ILE ILE A . n 
A 1 368 LYS 368 368 368 LYS LYS A . n 
A 1 369 GLU 369 369 369 GLU GLU A . n 
A 1 370 VAL 370 370 370 VAL VAL A . n 
A 1 371 THR 371 371 371 THR THR A . n 
A 1 372 ILE 372 372 372 ILE ILE A . n 
A 1 373 ASN 373 373 373 ASN ASN A . n 
A 1 374 ALA 374 374 374 ALA ALA A . n 
A 1 375 ASP 375 375 375 ASP ASP A . n 
A 1 376 THR 376 376 376 THR THR A . n 
A 1 377 THR 377 377 377 THR THR A . n 
A 1 378 CYS 378 378 378 CYS CYS A . n 
A 1 379 GLY 379 379 379 GLY GLY A . n 
A 1 380 ASN 380 380 380 ASN ASN A . n 
A 1 381 ASP 381 381 381 ASP ASP A . n 
A 1 382 TRP 382 382 382 TRP TRP A . n 
A 1 383 VAL 383 383 383 VAL VAL A . n 
A 1 384 CYS 384 384 384 CYS CYS A . n 
A 1 385 GLU 385 385 385 GLU GLU A . n 
A 1 386 HIS 386 386 386 HIS HIS A . n 
A 1 387 ARG 387 387 387 ARG ARG A . n 
A 1 388 TRP 388 388 388 TRP TRP A . n 
A 1 389 ARG 389 389 389 ARG ARG A . n 
A 1 390 GLU 390 390 390 GLU GLU A . n 
A 1 391 ILE 391 391 391 ILE ILE A . n 
A 1 392 ARG 392 392 392 ARG ARG A . n 
A 1 393 ASN 393 393 393 ASN ASN A . n 
A 1 394 MET 394 394 394 MET MET A . n 
A 1 395 VAL 395 395 395 VAL VAL A . n 
A 1 396 TRP 396 396 396 TRP TRP A . n 
A 1 397 PHE 397 397 397 PHE PHE A . n 
A 1 398 ARG 398 398 398 ARG ARG A . n 
A 1 399 ASN 399 399 399 ASN ASN A . n 
A 1 400 VAL 400 400 400 VAL VAL A . n 
A 1 401 VAL 401 401 401 VAL VAL A . n 
A 1 402 ASP 402 402 402 ASP ASP A . n 
A 1 403 GLY 403 403 403 GLY GLY A . n 
A 1 404 GLU 404 404 404 GLU GLU A . n 
A 1 405 PRO 405 405 405 PRO PRO A . n 
A 1 406 PHE 406 406 406 PHE PHE A . n 
A 1 407 ALA 407 407 407 ALA ALA A . n 
A 1 408 ASN 408 408 408 ASN ASN A . n 
A 1 409 TRP 409 409 409 TRP TRP A . n 
A 1 410 TRP 410 410 410 TRP TRP A . n 
A 1 411 ASP 411 411 411 ASP ASP A . n 
A 1 412 ASN 412 412 412 ASN ASN A . n 
A 1 413 GLY 413 413 413 GLY GLY A . n 
A 1 414 SER 414 414 414 SER SER A . n 
A 1 415 ASN 415 415 415 ASN ASN A . n 
A 1 416 GLN 416 416 416 GLN GLN A . n 
A 1 417 VAL 417 417 417 VAL VAL A . n 
A 1 418 ALA 418 418 418 ALA ALA A . n 
A 1 419 PHE 419 419 419 PHE PHE A . n 
A 1 420 GLY 420 420 420 GLY GLY A . n 
A 1 421 ARG 421 421 421 ARG ARG A . n 
A 1 422 GLY 422 422 422 GLY GLY A . n 
A 1 423 ASN 423 423 423 ASN ASN A . n 
A 1 424 ARG 424 424 424 ARG ARG A . n 
A 1 425 GLY 425 425 425 GLY GLY A . n 
A 1 426 PHE 426 426 426 PHE PHE A . n 
A 1 427 ILE 427 427 427 ILE ILE A . n 
A 1 428 VAL 428 428 428 VAL VAL A . n 
A 1 429 PHE 429 429 429 PHE PHE A . n 
A 1 430 ASN 430 430 430 ASN ASN A . n 
A 1 431 ASN 431 431 431 ASN ASN A . n 
A 1 432 ASP 432 432 432 ASP ASP A . n 
A 1 433 ASP 433 433 433 ASP ASP A . n 
A 1 434 TRP 434 434 434 TRP TRP A . n 
A 1 435 GLN 435 435 435 GLN GLN A . n 
A 1 436 LEU 436 436 436 LEU LEU A . n 
A 1 437 SER 437 437 437 SER SER A . n 
A 1 438 SER 438 438 438 SER SER A . n 
A 1 439 THR 439 439 439 THR THR A . n 
A 1 440 LEU 440 440 440 LEU LEU A . n 
A 1 441 GLN 441 441 441 GLN GLN A . n 
A 1 442 THR 442 442 442 THR THR A . n 
A 1 443 GLY 443 443 443 GLY GLY A . n 
A 1 444 LEU 444 444 444 LEU LEU A . n 
A 1 445 PRO 445 445 445 PRO PRO A . n 
A 1 446 GLY 446 446 446 GLY GLY A . n 
A 1 447 GLY 447 447 447 GLY GLY A . n 
A 1 448 THR 448 448 448 THR THR A . n 
A 1 449 TYR 449 449 449 TYR TYR A . n 
A 1 450 CYS 450 450 450 CYS CYS A . n 
A 1 451 ASP 451 451 451 ASP ASP A . n 
A 1 452 VAL 452 452 452 VAL VAL A . n 
A 1 453 ILE 453 453 453 ILE ILE A . n 
A 1 454 SER 454 454 454 SER SER A . n 
A 1 455 GLY 455 455 455 GLY GLY A . n 
A 1 456 ASP 456 456 456 ASP ASP A . n 
A 1 457 LYS 457 457 457 LYS LYS A . n 
A 1 458 VAL 458 458 458 VAL VAL A . n 
A 1 459 GLY 459 459 459 GLY GLY A . n 
A 1 460 ASN 460 460 460 ASN ASN A . n 
A 1 461 SER 461 461 461 SER SER A . n 
A 1 462 CYS 462 462 462 CYS CYS A . n 
A 1 463 THR 463 463 463 THR THR A . n 
A 1 464 GLY 464 464 464 GLY GLY A . n 
A 1 465 ILE 465 465 465 ILE ILE A . n 
A 1 466 LYS 466 466 466 LYS LYS A . n 
A 1 467 VAL 467 467 467 VAL VAL A . n 
A 1 468 TYR 468 468 468 TYR TYR A . n 
A 1 469 VAL 469 469 469 VAL VAL A . n 
A 1 470 SER 470 470 470 SER SER A . n 
A 1 471 SER 471 471 471 SER SER A . n 
A 1 472 ASP 472 472 472 ASP ASP A . n 
A 1 473 GLY 473 473 473 GLY GLY A . n 
A 1 474 THR 474 474 474 THR THR A . n 
A 1 475 ALA 475 475 475 ALA ALA A . n 
A 1 476 GLN 476 476 476 GLN GLN A . n 
A 1 477 PHE 477 477 477 PHE PHE A . n 
A 1 478 SER 478 478 478 SER SER A . n 
A 1 479 ILE 479 479 479 ILE ILE A . n 
A 1 480 SER 480 480 480 SER SER A . n 
A 1 481 ASN 481 481 481 ASN ASN A . n 
A 1 482 SER 482 482 482 SER SER A . n 
A 1 483 ALA 483 483 483 ALA ALA A . n 
A 1 484 GLU 484 484 484 GLU GLU A . n 
A 1 485 ASP 485 485 485 ASP ASP A . n 
A 1 486 PRO 486 486 486 PRO PRO A . n 
A 1 487 PHE 487 487 487 PHE PHE A . n 
A 1 488 ILE 488 488 488 ILE ILE A . n 
A 1 489 ALA 489 489 489 ALA ALA A . n 
A 1 490 ILE 490 490 490 ILE ILE A . n 
A 1 491 HIS 491 491 491 HIS HIS A . n 
A 1 492 ALA 492 492 492 ALA ALA A . n 
A 1 493 GLU 493 493 493 GLU GLU A . n 
A 1 494 SER 494 494 494 SER SER A . n 
A 1 495 LYS 495 495 495 LYS LYS A . n 
A 1 496 LEU 496 496 496 LEU LEU A . n 
# 
loop_
_pdbx_branch_scheme.asym_id 
_pdbx_branch_scheme.entity_id 
_pdbx_branch_scheme.mon_id 
_pdbx_branch_scheme.num 
_pdbx_branch_scheme.pdb_asym_id 
_pdbx_branch_scheme.pdb_mon_id 
_pdbx_branch_scheme.pdb_seq_num 
_pdbx_branch_scheme.auth_asym_id 
_pdbx_branch_scheme.auth_mon_id 
_pdbx_branch_scheme.auth_seq_num 
_pdbx_branch_scheme.hetero 
B 2 BGC 1 B BGC 1 A BGC 993 n 
B 2 AC1 2 B AC1 2 A AC1 992 n 
B 2 GLC 3 B GLC 3 A GLC 991 n 
B 2 AC1 4 B AC1 4 A AC1 990 n 
# 
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 
C 3 BGC 1   996  996  BGC BGC A . 
D 4 CL  1   498  498  CL  CL  A . 
E 5 CA  1   500  500  CA  CA  A . 
F 6 HOH 1   997  997  HOH HOH A . 
F 6 HOH 2   998  998  HOH HOH A . 
F 6 HOH 3   999  999  HOH HOH A . 
F 6 HOH 4   1000 1000 HOH HOH A . 
F 6 HOH 5   1001 1001 HOH HOH A . 
F 6 HOH 6   1002 1002 HOH HOH A . 
F 6 HOH 7   1003 1003 HOH HOH A . 
F 6 HOH 8   1004 1004 HOH HOH A . 
F 6 HOH 9   1005 1005 HOH HOH A . 
F 6 HOH 10  1006 1006 HOH HOH A . 
F 6 HOH 11  1007 1007 HOH HOH A . 
F 6 HOH 12  1008 1008 HOH HOH A . 
F 6 HOH 13  1009 1009 HOH HOH A . 
F 6 HOH 14  1010 1010 HOH HOH A . 
F 6 HOH 15  1011 1011 HOH HOH A . 
F 6 HOH 16  1012 1012 HOH HOH A . 
F 6 HOH 17  1013 1013 HOH HOH A . 
F 6 HOH 18  1014 1014 HOH HOH A . 
F 6 HOH 19  1015 1015 HOH HOH A . 
F 6 HOH 20  1016 1016 HOH HOH A . 
F 6 HOH 21  1017 1017 HOH HOH A . 
F 6 HOH 22  1018 1018 HOH HOH A . 
F 6 HOH 23  1019 1019 HOH HOH A . 
F 6 HOH 24  1020 1020 HOH HOH A . 
F 6 HOH 25  1021 1021 HOH HOH A . 
F 6 HOH 26  1022 1022 HOH HOH A . 
F 6 HOH 27  1023 1023 HOH HOH A . 
F 6 HOH 28  1024 1024 HOH HOH A . 
F 6 HOH 29  1025 1025 HOH HOH A . 
F 6 HOH 30  1026 1026 HOH HOH A . 
F 6 HOH 31  1027 1027 HOH HOH A . 
F 6 HOH 32  1028 1028 HOH HOH A . 
F 6 HOH 33  1029 1029 HOH HOH A . 
F 6 HOH 34  1030 1030 HOH HOH A . 
F 6 HOH 35  1031 1031 HOH HOH A . 
F 6 HOH 36  1032 1032 HOH HOH A . 
F 6 HOH 37  1033 1033 HOH HOH A . 
F 6 HOH 38  1034 1034 HOH HOH A . 
F 6 HOH 39  1035 1035 HOH HOH A . 
F 6 HOH 40  1036 1036 HOH HOH A . 
F 6 HOH 41  1037 1037 HOH HOH A . 
F 6 HOH 42  1038 1038 HOH HOH A . 
F 6 HOH 43  1039 1039 HOH HOH A . 
F 6 HOH 44  1040 1040 HOH HOH A . 
F 6 HOH 45  1041 1041 HOH HOH A . 
F 6 HOH 46  1042 1042 HOH HOH A . 
F 6 HOH 47  1043 1043 HOH HOH A . 
F 6 HOH 48  1044 1044 HOH HOH A . 
F 6 HOH 49  1045 1045 HOH HOH A . 
F 6 HOH 50  1046 1046 HOH HOH A . 
F 6 HOH 51  1047 1047 HOH HOH A . 
F 6 HOH 52  1048 1048 HOH HOH A . 
F 6 HOH 53  1049 1049 HOH HOH A . 
F 6 HOH 54  1050 1050 HOH HOH A . 
F 6 HOH 55  1051 1051 HOH HOH A . 
F 6 HOH 56  1052 1052 HOH HOH A . 
F 6 HOH 57  1053 1053 HOH HOH A . 
F 6 HOH 58  1054 1054 HOH HOH A . 
F 6 HOH 59  1055 1055 HOH HOH A . 
F 6 HOH 60  1056 1056 HOH HOH A . 
F 6 HOH 61  1057 1057 HOH HOH A . 
F 6 HOH 62  1058 1058 HOH HOH A . 
F 6 HOH 63  1059 1059 HOH HOH A . 
F 6 HOH 64  1060 1060 HOH HOH A . 
F 6 HOH 65  1061 1061 HOH HOH A . 
F 6 HOH 66  1062 1062 HOH HOH A . 
F 6 HOH 67  1063 1063 HOH HOH A . 
F 6 HOH 68  1064 1064 HOH HOH A . 
F 6 HOH 69  1065 1065 HOH HOH A . 
F 6 HOH 70  1066 1066 HOH HOH A . 
F 6 HOH 71  1067 1067 HOH HOH A . 
F 6 HOH 72  1068 1068 HOH HOH A . 
F 6 HOH 73  1069 1069 HOH HOH A . 
F 6 HOH 74  1070 1070 HOH HOH A . 
F 6 HOH 75  1071 1071 HOH HOH A . 
F 6 HOH 76  1072 1072 HOH HOH A . 
F 6 HOH 77  1073 1073 HOH HOH A . 
F 6 HOH 78  1074 1074 HOH HOH A . 
F 6 HOH 79  1075 1075 HOH HOH A . 
F 6 HOH 80  1076 1076 HOH HOH A . 
F 6 HOH 81  1077 1077 HOH HOH A . 
F 6 HOH 82  1078 1078 HOH HOH A . 
F 6 HOH 83  1079 1079 HOH HOH A . 
F 6 HOH 84  1080 1080 HOH HOH A . 
F 6 HOH 85  1081 1081 HOH HOH A . 
F 6 HOH 86  1082 1082 HOH HOH A . 
F 6 HOH 87  1083 1083 HOH HOH A . 
F 6 HOH 88  1084 1084 HOH HOH A . 
F 6 HOH 89  1085 1085 HOH HOH A . 
F 6 HOH 90  1086 1086 HOH HOH A . 
F 6 HOH 91  1087 1087 HOH HOH A . 
F 6 HOH 92  1088 1088 HOH HOH A . 
F 6 HOH 93  1089 1089 HOH HOH A . 
F 6 HOH 94  1090 1090 HOH HOH A . 
F 6 HOH 95  1091 1091 HOH HOH A . 
F 6 HOH 96  1092 1092 HOH HOH A . 
F 6 HOH 97  1093 1093 HOH HOH A . 
F 6 HOH 98  1094 1094 HOH HOH A . 
F 6 HOH 99  1095 1095 HOH HOH A . 
F 6 HOH 100 1096 1096 HOH HOH A . 
F 6 HOH 101 1097 1097 HOH HOH A . 
F 6 HOH 102 1098 1098 HOH HOH A . 
F 6 HOH 103 1099 1099 HOH HOH A . 
F 6 HOH 104 1100 1100 HOH HOH A . 
F 6 HOH 105 1101 1101 HOH HOH A . 
F 6 HOH 106 1102 1102 HOH HOH A . 
F 6 HOH 107 1103 1103 HOH HOH A . 
F 6 HOH 108 1104 1104 HOH HOH A . 
F 6 HOH 109 1105 1105 HOH HOH A . 
F 6 HOH 110 1106 1106 HOH HOH A . 
F 6 HOH 111 1107 1107 HOH HOH A . 
F 6 HOH 112 1108 1108 HOH HOH A . 
F 6 HOH 113 1109 1109 HOH HOH A . 
F 6 HOH 114 1110 1110 HOH HOH A . 
F 6 HOH 115 1111 1111 HOH HOH A . 
F 6 HOH 116 1112 1112 HOH HOH A . 
F 6 HOH 117 1113 1113 HOH HOH A . 
F 6 HOH 118 1114 1114 HOH HOH A . 
F 6 HOH 119 1115 1115 HOH HOH A . 
F 6 HOH 120 1116 1116 HOH HOH A . 
F 6 HOH 121 1117 1117 HOH HOH A . 
F 6 HOH 122 1118 1118 HOH HOH A . 
F 6 HOH 123 1119 1119 HOH HOH A . 
F 6 HOH 124 1120 1120 HOH HOH A . 
F 6 HOH 125 1121 1121 HOH HOH A . 
F 6 HOH 126 1122 1122 HOH HOH A . 
F 6 HOH 127 1123 1123 HOH HOH A . 
F 6 HOH 128 1124 1124 HOH HOH A . 
F 6 HOH 129 1125 1125 HOH HOH A . 
F 6 HOH 130 1126 1126 HOH HOH A . 
F 6 HOH 131 1127 1127 HOH HOH A . 
F 6 HOH 132 1128 1128 HOH HOH A . 
F 6 HOH 133 1129 1129 HOH HOH A . 
F 6 HOH 134 1130 1130 HOH HOH A . 
F 6 HOH 135 1131 1131 HOH HOH A . 
F 6 HOH 136 1132 1132 HOH HOH A . 
F 6 HOH 137 1133 1133 HOH HOH A . 
F 6 HOH 138 1134 1134 HOH HOH A . 
F 6 HOH 139 1135 1135 HOH HOH A . 
F 6 HOH 140 1136 1136 HOH HOH A . 
F 6 HOH 141 1137 1137 HOH HOH A . 
F 6 HOH 142 1138 1138 HOH HOH A . 
F 6 HOH 143 1139 1139 HOH HOH A . 
F 6 HOH 144 1140 1140 HOH HOH A . 
F 6 HOH 145 1141 1141 HOH HOH A . 
F 6 HOH 146 1142 1142 HOH HOH A . 
F 6 HOH 147 1143 1143 HOH HOH A . 
F 6 HOH 148 1144 1144 HOH HOH A . 
F 6 HOH 149 1145 1145 HOH HOH A . 
F 6 HOH 150 1146 1146 HOH HOH A . 
F 6 HOH 151 1147 1147 HOH HOH A . 
F 6 HOH 152 1148 1148 HOH HOH A . 
F 6 HOH 153 1149 1149 HOH HOH A . 
F 6 HOH 154 1150 1150 HOH HOH A . 
F 6 HOH 155 1151 1151 HOH HOH A . 
F 6 HOH 156 1152 1152 HOH HOH A . 
F 6 HOH 157 1153 1153 HOH HOH A . 
F 6 HOH 158 1154 1154 HOH HOH A . 
F 6 HOH 159 1155 1155 HOH HOH A . 
F 6 HOH 160 1156 1156 HOH HOH A . 
F 6 HOH 161 1157 1157 HOH HOH A . 
F 6 HOH 162 1158 1158 HOH HOH A . 
F 6 HOH 163 1159 1159 HOH HOH A . 
F 6 HOH 164 1160 1160 HOH HOH A . 
F 6 HOH 165 1161 1161 HOH HOH A . 
F 6 HOH 166 1162 1162 HOH HOH A . 
F 6 HOH 167 1163 1163 HOH HOH A . 
F 6 HOH 168 1164 1164 HOH HOH A . 
F 6 HOH 169 1165 1165 HOH HOH A . 
F 6 HOH 170 1166 1166 HOH HOH A . 
F 6 HOH 171 1167 1167 HOH HOH A . 
F 6 HOH 172 1168 1168 HOH HOH A . 
F 6 HOH 173 1169 1169 HOH HOH A . 
F 6 HOH 174 1170 1170 HOH HOH A . 
F 6 HOH 175 1171 1171 HOH HOH A . 
F 6 HOH 176 1172 1172 HOH HOH A . 
F 6 HOH 177 1173 1173 HOH HOH A . 
F 6 HOH 178 1174 1174 HOH HOH A . 
F 6 HOH 179 1175 1175 HOH HOH A . 
F 6 HOH 180 1176 1176 HOH HOH A . 
F 6 HOH 181 1177 1177 HOH HOH A . 
F 6 HOH 182 1178 1178 HOH HOH A . 
F 6 HOH 183 1179 1179 HOH HOH A . 
F 6 HOH 184 1180 1180 HOH HOH A . 
F 6 HOH 185 1181 1181 HOH HOH A . 
F 6 HOH 186 1182 1182 HOH HOH A . 
F 6 HOH 187 1183 1183 HOH HOH A . 
F 6 HOH 188 1184 1184 HOH HOH A . 
F 6 HOH 189 1185 1185 HOH HOH A . 
F 6 HOH 190 1186 1186 HOH HOH A . 
F 6 HOH 191 1187 1187 HOH HOH A . 
F 6 HOH 192 1188 1188 HOH HOH A . 
F 6 HOH 193 1189 1189 HOH HOH A . 
F 6 HOH 194 1190 1190 HOH HOH A . 
F 6 HOH 195 1191 1191 HOH HOH A . 
F 6 HOH 196 1192 1192 HOH HOH A . 
F 6 HOH 197 1193 1193 HOH HOH A . 
F 6 HOH 198 1194 1194 HOH HOH A . 
F 6 HOH 199 1195 1195 HOH HOH A . 
F 6 HOH 200 1196 1196 HOH HOH A . 
F 6 HOH 201 1197 1197 HOH HOH A . 
F 6 HOH 202 1198 1198 HOH HOH A . 
F 6 HOH 203 1199 1199 HOH HOH A . 
F 6 HOH 204 1200 1200 HOH HOH A . 
F 6 HOH 205 1201 1201 HOH HOH A . 
F 6 HOH 206 1202 1202 HOH HOH A . 
F 6 HOH 207 1203 1203 HOH HOH A . 
F 6 HOH 208 1204 1204 HOH HOH A . 
F 6 HOH 209 1205 1205 HOH HOH A . 
F 6 HOH 210 1206 1206 HOH HOH A . 
F 6 HOH 211 1207 1207 HOH HOH A . 
F 6 HOH 212 1208 1208 HOH HOH A . 
F 6 HOH 213 1209 1209 HOH HOH A . 
F 6 HOH 214 1210 1210 HOH HOH A . 
F 6 HOH 215 1211 1211 HOH HOH A . 
F 6 HOH 216 1212 1212 HOH HOH A . 
F 6 HOH 217 1213 1213 HOH HOH A . 
F 6 HOH 218 1214 1214 HOH HOH A . 
F 6 HOH 219 1215 1215 HOH HOH A . 
F 6 HOH 220 1216 1216 HOH HOH A . 
F 6 HOH 221 1217 1217 HOH HOH A . 
F 6 HOH 222 1218 1218 HOH HOH A . 
F 6 HOH 223 1219 1219 HOH HOH A . 
F 6 HOH 224 1220 1220 HOH HOH A . 
F 6 HOH 225 1221 1221 HOH HOH A . 
F 6 HOH 226 1222 1222 HOH HOH A . 
F 6 HOH 227 1223 1223 HOH HOH A . 
F 6 HOH 228 1224 1224 HOH HOH A . 
F 6 HOH 229 1225 1225 HOH HOH A A 
F 6 HOH 230 1226 1226 HOH HOH A A 
F 6 HOH 231 1227 1227 HOH HOH A A 
F 6 HOH 232 1228 1228 HOH HOH A A 
F 6 HOH 233 1229 1229 HOH HOH A A 
F 6 HOH 234 1230 1230 HOH HOH A A 
F 6 HOH 235 1231 1231 HOH HOH A A 
F 6 HOH 236 1232 1232 HOH HOH A A 
F 6 HOH 237 1233 1233 HOH HOH A A 
F 6 HOH 238 1234 1234 HOH HOH A A 
F 6 HOH 239 1235 1235 HOH HOH A A 
F 6 HOH 240 1236 1236 HOH HOH A A 
F 6 HOH 241 1237 1237 HOH HOH A A 
F 6 HOH 242 1238 1238 HOH HOH A A 
F 6 HOH 243 1239 1239 HOH HOH A A 
F 6 HOH 244 1240 1240 HOH HOH A A 
F 6 HOH 245 1241 1241 HOH HOH A B 
F 6 HOH 246 1242 1242 HOH HOH A B 
F 6 HOH 247 1243 1243 HOH HOH A B 
F 6 HOH 248 1244 1244 HOH HOH A B 
F 6 HOH 249 1245 1245 HOH HOH A B 
F 6 HOH 250 1246 1246 HOH HOH A B 
F 6 HOH 251 1247 1247 HOH HOH A B 
F 6 HOH 252 1248 1248 HOH HOH A B 
F 6 HOH 253 1249 1249 HOH HOH A B 
F 6 HOH 254 1250 1250 HOH HOH A B 
F 6 HOH 255 1251 1251 HOH HOH A B 
F 6 HOH 256 1252 1252 HOH HOH A B 
F 6 HOH 257 1253 1253 HOH HOH A B 
F 6 HOH 258 1254 1254 HOH HOH A B 
F 6 HOH 259 1255 1255 HOH HOH A B 
F 6 HOH 260 1256 1256 HOH HOH A B 
F 6 HOH 261 1257 1257 HOH HOH A B 
F 6 HOH 262 1258 1258 HOH HOH A B 
F 6 HOH 263 1259 1259 HOH HOH A B 
F 6 HOH 264 1260 1260 HOH HOH A B 
F 6 HOH 265 1261 1261 HOH HOH A B 
F 6 HOH 266 1262 1262 HOH HOH A B 
F 6 HOH 267 1263 1263 HOH HOH A B 
F 6 HOH 268 1264 1264 HOH HOH A B 
F 6 HOH 269 1265 1265 HOH HOH A B 
F 6 HOH 270 1266 1266 HOH HOH A B 
F 6 HOH 271 1267 1267 HOH HOH A B 
F 6 HOH 272 1268 1268 HOH HOH A B 
F 6 HOH 273 1269 1269 HOH HOH A B 
F 6 HOH 274 1270 1270 HOH HOH A B 
F 6 HOH 275 1271 1271 HOH HOH A B 
F 6 HOH 276 1272 1272 HOH HOH A B 
F 6 HOH 277 1273 1273 HOH HOH A B 
F 6 HOH 278 1274 1274 HOH HOH A B 
F 6 HOH 279 1275 1275 HOH HOH A B 
F 6 HOH 280 1276 1276 HOH HOH A B 
F 6 HOH 281 1277 1277 HOH HOH A B 
F 6 HOH 282 1278 1278 HOH HOH A B 
F 6 HOH 283 1279 1279 HOH HOH A B 
F 6 HOH 284 1280 1280 HOH HOH A B 
F 6 HOH 285 1281 1281 HOH HOH A B 
F 6 HOH 286 1282 1282 HOH HOH A B 
F 6 HOH 287 1283 1283 HOH HOH A B 
F 6 HOH 288 1284 1284 HOH HOH A B 
F 6 HOH 289 1285 1285 HOH HOH A B 
F 6 HOH 290 1286 1286 HOH HOH A B 
F 6 HOH 291 1287 1287 HOH HOH A B 
F 6 HOH 292 1288 1288 HOH HOH A B 
F 6 HOH 293 1289 1289 HOH HOH A B 
F 6 HOH 294 1290 1290 HOH HOH A B 
F 6 HOH 295 1291 1291 HOH HOH A B 
F 6 HOH 296 1292 1292 HOH HOH A B 
F 6 HOH 297 1293 1293 HOH HOH A B 
F 6 HOH 298 1294 1294 HOH HOH A B 
F 6 HOH 299 1295 1295 HOH HOH A B 
F 6 HOH 300 1296 1296 HOH HOH A B 
F 6 HOH 301 1297 1297 HOH HOH A B 
F 6 HOH 302 1298 1298 HOH HOH A B 
F 6 HOH 303 1299 1299 HOH HOH A B 
F 6 HOH 304 1300 1300 HOH HOH A B 
F 6 HOH 305 1301 1301 HOH HOH A B 
F 6 HOH 306 1302 1302 HOH HOH A B 
F 6 HOH 307 1303 1303 HOH HOH A B 
F 6 HOH 308 1304 1304 HOH HOH A B 
F 6 HOH 309 1305 1305 HOH HOH A B 
F 6 HOH 310 1306 1306 HOH HOH A B 
F 6 HOH 311 1307 1307 HOH HOH A B 
F 6 HOH 312 1308 1308 HOH HOH A B 
F 6 HOH 313 1309 1309 HOH HOH A B 
F 6 HOH 314 1310 1310 HOH HOH A B 
F 6 HOH 315 1311 1311 HOH HOH A B 
F 6 HOH 316 1312 1312 HOH HOH A B 
F 6 HOH 317 1313 1313 HOH HOH A B 
F 6 HOH 318 1314 1314 HOH HOH A B 
F 6 HOH 319 1315 1315 HOH HOH A B 
F 6 HOH 320 1316 1316 HOH HOH A B 
F 6 HOH 321 1317 1317 HOH HOH A B 
F 6 HOH 322 1318 1318 HOH HOH A B 
F 6 HOH 323 1319 1319 HOH HOH A B 
F 6 HOH 324 1320 1320 HOH HOH A B 
F 6 HOH 325 1321 1321 HOH HOH A B 
F 6 HOH 326 1322 1322 HOH HOH A B 
F 6 HOH 327 1323 1323 HOH HOH A B 
F 6 HOH 328 1324 1324 HOH HOH A B 
F 6 HOH 329 1325 1325 HOH HOH A B 
F 6 HOH 330 1326 1326 HOH HOH A B 
F 6 HOH 331 1327 1327 HOH HOH A B 
F 6 HOH 332 1328 1328 HOH HOH A B 
F 6 HOH 333 1329 1329 HOH HOH A B 
F 6 HOH 334 1330 1330 HOH HOH A B 
F 6 HOH 335 1331 1331 HOH HOH A B 
F 6 HOH 336 1332 1332 HOH HOH A B 
F 6 HOH 337 1333 1333 HOH HOH A B 
F 6 HOH 338 1334 1334 HOH HOH A B 
F 6 HOH 339 1335 1335 HOH HOH A B 
F 6 HOH 340 1336 1336 HOH HOH A B 
F 6 HOH 341 1337 1337 HOH HOH A B 
F 6 HOH 342 1338 1338 HOH HOH A B 
F 6 HOH 343 1339 1339 HOH HOH A B 
F 6 HOH 344 1340 1340 HOH HOH A B 
F 6 HOH 345 1341 1341 HOH HOH A B 
F 6 HOH 346 1342 1342 HOH HOH A B 
F 6 HOH 347 1343 1343 HOH HOH A B 
F 6 HOH 348 1344 1344 HOH HOH A B 
F 6 HOH 349 1345 1345 HOH HOH A B 
F 6 HOH 350 1346 1346 HOH HOH A B 
F 6 HOH 351 1347 1347 HOH HOH A B 
F 6 HOH 352 1348 1348 HOH HOH A B 
F 6 HOH 353 1349 1349 HOH HOH A B 
F 6 HOH 354 1350 1350 HOH HOH A B 
F 6 HOH 355 1351 1351 HOH HOH A B 
F 6 HOH 356 1352 1352 HOH HOH A B 
F 6 HOH 357 1353 1353 HOH HOH A B 
F 6 HOH 358 1354 1354 HOH HOH A B 
F 6 HOH 359 1355 1355 HOH HOH A B 
F 6 HOH 360 1356 1356 HOH HOH A B 
F 6 HOH 361 1357 1357 HOH HOH A B 
F 6 HOH 362 1358 1358 HOH HOH A B 
F 6 HOH 363 1359 1359 HOH HOH A B 
F 6 HOH 364 1360 1360 HOH HOH A B 
F 6 HOH 365 1361 1361 HOH HOH A B 
F 6 HOH 366 1362 1362 HOH HOH A B 
F 6 HOH 367 1363 1363 HOH HOH A B 
F 6 HOH 368 1364 1364 HOH HOH A B 
F 6 HOH 369 1365 1365 HOH HOH A B 
F 6 HOH 370 1366 1366 HOH HOH A B 
F 6 HOH 371 1367 1367 HOH HOH A B 
F 6 HOH 372 1368 1368 HOH HOH A B 
F 6 HOH 373 1369 1369 HOH HOH A B 
F 6 HOH 374 1370 1370 HOH HOH A B 
F 6 HOH 375 1371 1371 HOH HOH A B 
F 6 HOH 376 1372 1372 HOH HOH A B 
F 6 HOH 377 1373 1373 HOH HOH A B 
F 6 HOH 378 1374 1374 HOH HOH A B 
F 6 HOH 379 1375 1375 HOH HOH A B 
F 6 HOH 380 1376 1376 HOH HOH A B 
F 6 HOH 381 1377 1377 HOH HOH A B 
F 6 HOH 382 1378 1378 HOH HOH A B 
F 6 HOH 383 1379 1379 HOH HOH A B 
F 6 HOH 384 1380 1380 HOH HOH A B 
F 6 HOH 385 1381 1381 HOH HOH A B 
F 6 HOH 386 1382 1382 HOH HOH A B 
F 6 HOH 387 1383 1383 HOH HOH A B 
F 6 HOH 388 1384 1384 HOH HOH A B 
F 6 HOH 389 1385 1385 HOH HOH A B 
F 6 HOH 390 1386 1386 HOH HOH A B 
F 6 HOH 391 1387 1387 HOH HOH A B 
F 6 HOH 392 1388 1388 HOH HOH A B 
F 6 HOH 393 1389 1389 HOH HOH A B 
F 6 HOH 394 1390 1390 HOH HOH A B 
F 6 HOH 395 1391 1391 HOH HOH A B 
F 6 HOH 396 1392 1392 HOH HOH A B 
F 6 HOH 397 1393 1393 HOH HOH A B 
F 6 HOH 398 1394 1394 HOH HOH A B 
F 6 HOH 399 1395 1395 HOH HOH A B 
F 6 HOH 400 1396 1396 HOH HOH A B 
F 6 HOH 401 1397 1397 HOH HOH A B 
F 6 HOH 402 1398 1398 HOH HOH A B 
F 6 HOH 403 1399 1399 HOH HOH A B 
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
XDS    'data scaling'   .   ? 1 
X-PLOR 'model building' 3.1 ? 2 
X-PLOR refinement       3.1 ? 3 
XDS    'data reduction' .   ? 4 
X-PLOR phasing          3.1 ? 5 
# 
_cell.entry_id           1OSE 
_cell.length_a           70.600 
_cell.length_b           114.700 
_cell.length_c           118.500 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.00 
_cell.angle_gamma        90.00 
_cell.Z_PDB              4 
_cell.pdbx_unique_axis   ? 
_cell.length_a_esd       ? 
_cell.length_b_esd       ? 
_cell.length_c_esd       ? 
_cell.angle_alpha_esd    ? 
_cell.angle_beta_esd     ? 
_cell.angle_gamma_esd    ? 
# 
_symmetry.entry_id                         1OSE 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
# 
_exptl.entry_id          1OSE 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   ? 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      4.33 
_exptl_crystal.density_percent_sol   72.0 
_exptl_crystal.description           ? 
_exptl_crystal.F_000                 ? 
_exptl_crystal.preparation           ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           ? 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               'IMAGE PLATE' 
_diffrn_detector.type                   'MAR scanner 180 mm plate' 
_diffrn_detector.pdbx_collection_date   ? 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.pdbx_diffrn_protocol             ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.5418 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      ? 
_diffrn_source.type                        ? 
_diffrn_source.pdbx_synchrotron_site       ? 
_diffrn_source.pdbx_synchrotron_beamline   ? 
_diffrn_source.pdbx_wavelength             1.5418 
_diffrn_source.pdbx_wavelength_list        ? 
# 
_reflns.entry_id                     1OSE 
_reflns.observed_criterion_sigma_I   1. 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             30.00 
_reflns.d_resolution_high            2.3 
_reflns.number_obs                   41389 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         96.74 
_reflns.pdbx_Rmerge_I_obs            0.157 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        ? 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_redundancy              3.1 
_reflns.R_free_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.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.pdbx_chi_squared             ? 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
# 
_refine.entry_id                                 1OSE 
_refine.ls_number_reflns_obs                     37212 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0. 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             8.00 
_refine.ls_d_res_high                            2.30 
_refine.ls_percent_reflns_obs                    90.0 
_refine.ls_R_factor_obs                          0.176 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.176 
_refine.ls_R_factor_R_free                       0.222 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 10.00 
_refine.ls_number_reflns_R_free                  ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.B_iso_mean                               ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_ls_cross_valid_method               ? 
_refine.details                                  ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_B                             ? 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.B_iso_min                                ? 
_refine.B_iso_max                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_analyze.entry_id                        1OSE 
_refine_analyze.Luzzati_coordinate_error_obs    0.18 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.pdbx_Luzzati_d_res_high_obs     ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        3907 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         79 
_refine_hist.number_atoms_solvent             403 
_refine_hist.number_atoms_total               4389 
_refine_hist.d_res_high                       2.30 
_refine_hist.d_res_low                        8.00 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
x_bond_d                0.024 ? ? ? 'X-RAY DIFFRACTION' ? 
x_bond_d_na             ?     ? ? ? 'X-RAY DIFFRACTION' ? 
x_bond_d_prot           ?     ? ? ? 'X-RAY DIFFRACTION' ? 
x_angle_d               ?     ? ? ? 'X-RAY DIFFRACTION' ? 
x_angle_d_na            ?     ? ? ? 'X-RAY DIFFRACTION' ? 
x_angle_d_prot          ?     ? ? ? 'X-RAY DIFFRACTION' ? 
x_angle_deg             2.29  ? ? ? 'X-RAY DIFFRACTION' ? 
x_angle_deg_na          ?     ? ? ? 'X-RAY DIFFRACTION' ? 
x_angle_deg_prot        ?     ? ? ? 'X-RAY DIFFRACTION' ? 
x_dihedral_angle_d      24.79 ? ? ? 'X-RAY DIFFRACTION' ? 
x_dihedral_angle_d_na   ?     ? ? ? 'X-RAY DIFFRACTION' ? 
x_dihedral_angle_d_prot ?     ? ? ? 'X-RAY DIFFRACTION' ? 
x_improper_angle_d      1.53  ? ? ? 'X-RAY DIFFRACTION' ? 
x_improper_angle_d_na   ?     ? ? ? 'X-RAY DIFFRACTION' ? 
x_improper_angle_d_prot ?     ? ? ? 'X-RAY DIFFRACTION' ? 
x_mcbond_it             ?     ? ? ? 'X-RAY DIFFRACTION' ? 
x_mcangle_it            ?     ? ? ? 'X-RAY DIFFRACTION' ? 
x_scbond_it             ?     ? ? ? 'X-RAY DIFFRACTION' ? 
x_scangle_it            ?     ? ? ? 'X-RAY DIFFRACTION' ? 
# 
_database_PDB_matrix.entry_id          1OSE 
_database_PDB_matrix.origx[1][1]       1.000000 
_database_PDB_matrix.origx[1][2]       0.000000 
_database_PDB_matrix.origx[1][3]       0.000000 
_database_PDB_matrix.origx[2][1]       0.000000 
_database_PDB_matrix.origx[2][2]       1.000000 
_database_PDB_matrix.origx[2][3]       0.000000 
_database_PDB_matrix.origx[3][1]       0.000000 
_database_PDB_matrix.origx[3][2]       0.000000 
_database_PDB_matrix.origx[3][3]       1.000000 
_database_PDB_matrix.origx_vector[1]   0.00000 
_database_PDB_matrix.origx_vector[2]   0.00000 
_database_PDB_matrix.origx_vector[3]   0.00000 
# 
_struct.entry_id                  1OSE 
_struct.title                     'Porcine pancreatic alpha-amylase complexed with acarbose' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        1OSE 
_struct_keywords.pdbx_keywords   HYDROLASE 
_struct_keywords.text            'ALPHA-AMYLASE, ACARBOSE, HYDROLASE (O-GLYCOSYL), HYDROLASE' 
# 
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 ? 
F N N 6 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    AMYP_PIG 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_db_accession          P00690 
_struct_ref.pdbx_align_begin           1 
_struct_ref.pdbx_seq_one_letter_code   
;QYAPQTQSGRTSIVHLFEWRWVDIALECERYLGPKGFGGVQVSPPNENIVVTNPSRPWWERYQPVSYKLCTRSGNENEFR
DMVTRCNNVGVRIYVDAVINHMCGSGAAAGTGTTCGSYCNPGSREFPAVPYSAWDFNDGKCKTASGGIESYNDPYQVRDC
QLVGLLDLALEKDYVRSMIADYLNKLIDIGVAGFRIDASKHMWPGDIKAVLDKLHNLNTNWFPAGSRPFIFQEVIDLGGE
AIQSSEYFGNGRVTEFKYGAKLGTVVRKWSGEKMSYLKNWGEGWGFMPSDRALVFVDNHDNQRGHGAGGASILTFWDARL
YKVAVGFMLAHPYGFTRVMSSYRWARNFVNGEDVNDWIGPPNNNGVIKEVTINADTTCGNDWVCEHRWREIRNMVWFRNV
VDGEPFANWWDNGSNQVAFGRGNRGFIVFNNDDWQLSSTLQTGLPGGTYCDVISGDKVGNSCTGIKVYVSSDGTAQFSIS
NSAEDPFIAIHAESKL
;
_struct_ref.pdbx_db_isoform            ? 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              1OSE 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 2 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 496 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P00690 
_struct_ref_seq.db_align_beg                  2 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  496 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       2 
_struct_ref_seq.pdbx_auth_seq_align_end       496 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_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,F 
# 
_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 
# 
_struct_biol.id        1 
_struct_biol.details   ? 
# 
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  A1A ARG A 20  ? ARG A 30  ? ARG A 20  ARG A 30  1 ?                          11 
HELX_P HELX_P2  A1B TYR A 31  ? GLY A 36  ? TYR A 31  GLY A 36  1 ?                          6  
HELX_P HELX_P3  H1  PRO A 57  ? GLN A 63  ? PRO A 57  GLN A 63  1 '3 CONSECUTIVE BETA TURNS' 7  
HELX_P HELX_P4  A2  ASN A 75  ? ARG A 92  ? ASN A 75  ARG A 92  1 ?                          18 
HELX_P HELX_P5  H2  ASN A 120 ? ARG A 124 ? ASN A 120 ARG A 124 1 '2 CONSECUTIVE BETA TURNS' 5  
HELX_P HELX_P6  A3  LYS A 172 ? GLY A 190 ? LYS A 172 GLY A 190 1 ?                          19 
HELX_P HELX_P7  A4  TRP A 203 ? ASP A 212 ? TRP A 203 ASP A 212 1 ?                          10 
HELX_P HELX_P8  A5  SER A 244 ? ASN A 250 ? SER A 244 ASN A 250 5 ?                          7  
HELX_P HELX_P9  A6A PHE A 256 ? LYS A 268 ? PHE A 256 LYS A 268 1 ?                          13 
HELX_P HELX_P10 A6B LYS A 273 ? TRP A 280 ? LYS A 273 TRP A 280 5 '2 CONSECUTIVE BETA TURNS' 8  
HELX_P HELX_P11 H3  GLY A 281 ? GLY A 285 ? GLY A 281 GLY A 285 5 '2 CONSECUTIVE BETA TURNS' 5  
HELX_P HELX_P12 H4  PRO A 288 ? ALA A 292 ? PRO A 288 ALA A 292 5 '2 CONSECUTIVE BETA TURNS' 5  
HELX_P HELX_P13 H5  ASP A 300 ? GLY A 304 ? ASP A 300 GLY A 304 5 '2 CONSECUTIVE BETA TURNS' 5  
HELX_P HELX_P14 A7  ASP A 317 ? HIS A 331 ? ASP A 317 HIS A 331 1 ?                          15 
HELX_P HELX_P15 H6  CYS A 384 ? TRP A 388 ? CYS A 384 TRP A 388 5 '2 CONSECUTIVE BETA TURNS' 5  
HELX_P HELX_P16 A8  TRP A 388 ? ASP A 402 ? TRP A 388 ASP A 402 1 ?                          15 
HELX_P HELX_P17 B1  ASP A 153 ? ASP A 159 ? ASP A 153 ASP A 159 1 ?                          7  
# 
_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 28  SG  ? ? ? 1_555 A CYS 86  SG ? ? A CYS 28  A CYS 86   1_555 ? ? ? ? ? ? ? 2.028 ? ? 
disulf2 disulf ?    ? A CYS 70  SG  ? ? ? 1_555 A CYS 115 SG ? ? A CYS 70  A CYS 115  1_555 ? ? ? ? ? ? ? 2.031 ? ? 
disulf3 disulf ?    ? A CYS 141 SG  ? ? ? 1_555 A CYS 160 SG ? ? A CYS 141 A CYS 160  1_555 ? ? ? ? ? ? ? 2.028 ? ? 
disulf4 disulf ?    ? A CYS 378 SG  ? ? ? 1_555 A CYS 384 SG ? ? A CYS 378 A CYS 384  1_555 ? ? ? ? ? ? ? 2.022 ? ? 
disulf5 disulf ?    ? A CYS 450 SG  ? ? ? 1_555 A CYS 462 SG ? ? A CYS 450 A CYS 462  1_555 ? ? ? ? ? ? ? 2.021 ? ? 
covale1 covale both ? A PCA 1   C   ? ? ? 1_555 A TYR 2   N  ? ? A PCA 1   A TYR 2    1_555 ? ? ? ? ? ? ? 1.333 ? ? 
covale2 covale both ? B BGC .   O4  ? ? ? 1_555 B AC1 .   C1 ? ? B BGC 1   B AC1 2    1_555 ? ? ? ? ? ? ? 1.396 ? ? 
covale3 covale one  ? B AC1 .   O4  ? ? ? 1_555 B GLC .   C1 ? ? B AC1 2   B GLC 3    1_555 ? ? ? ? ? ? ? 1.402 ? ? 
covale4 covale both ? B GLC .   O4  ? ? ? 1_555 B AC1 .   C1 ? ? B GLC 3   B AC1 4    1_555 ? ? ? ? ? ? ? 1.403 ? ? 
metalc1 metalc ?    ? A ASN 100 OD1 ? ? ? 1_555 E CA  .   CA ? ? A ASN 100 A CA  500  1_555 ? ? ? ? ? ? ? 2.202 ? ? 
metalc2 metalc ?    ? A ARG 158 O   ? ? ? 1_555 E CA  .   CA ? ? A ARG 158 A CA  500  1_555 ? ? ? ? ? ? ? 2.400 ? ? 
metalc3 metalc ?    ? A ASP 167 OD2 ? ? ? 1_555 E CA  .   CA ? ? A ASP 167 A CA  500  1_555 ? ? ? ? ? ? ? 2.392 ? ? 
metalc4 metalc ?    ? A ASP 167 OD1 ? ? ? 1_555 E CA  .   CA ? ? A ASP 167 A CA  500  1_555 ? ? ? ? ? ? ? 2.544 ? ? 
metalc5 metalc ?    ? A HIS 201 O   ? ? ? 1_555 E CA  .   CA ? ? A HIS 201 A CA  500  1_555 ? ? ? ? ? ? ? 2.323 ? ? 
metalc6 metalc ?    ? E CA  .   CA  ? ? ? 1_555 F HOH .   O  ? ? A CA  500 A HOH 1016 1_555 ? ? ? ? ? ? ? 2.338 ? ? 
metalc7 metalc ?    ? E CA  .   CA  ? ? ? 1_555 F HOH .   O  ? ? A CA  500 A HOH 1023 1_555 ? ? ? ? ? ? ? 2.250 ? ? 
metalc8 metalc ?    ? E CA  .   CA  ? ? ? 1_555 F HOH .   O  ? ? A CA  500 A HOH 1035 1_555 ? ? ? ? ? ? ? 2.287 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
metalc ? ? 
# 
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 ASN 100 ? A ASN 100  ? 1_555 CA ? E CA . ? A CA 500 ? 1_555 O   ? A ARG 158 ? A ARG 158  ? 1_555 156.5 ? 
2  OD1 ? A ASN 100 ? A ASN 100  ? 1_555 CA ? E CA . ? A CA 500 ? 1_555 OD2 ? A ASP 167 ? A ASP 167  ? 1_555 127.1 ? 
3  O   ? A ARG 158 ? A ARG 158  ? 1_555 CA ? E CA . ? A CA 500 ? 1_555 OD2 ? A ASP 167 ? A ASP 167  ? 1_555 76.4  ? 
4  OD1 ? A ASN 100 ? A ASN 100  ? 1_555 CA ? E CA . ? A CA 500 ? 1_555 OD1 ? A ASP 167 ? A ASP 167  ? 1_555 82.7  ? 
5  O   ? A ARG 158 ? A ARG 158  ? 1_555 CA ? E CA . ? A CA 500 ? 1_555 OD1 ? A ASP 167 ? A ASP 167  ? 1_555 117.3 ? 
6  OD2 ? A ASP 167 ? A ASP 167  ? 1_555 CA ? E CA . ? A CA 500 ? 1_555 OD1 ? A ASP 167 ? A ASP 167  ? 1_555 52.4  ? 
7  OD1 ? A ASN 100 ? A ASN 100  ? 1_555 CA ? E CA . ? A CA 500 ? 1_555 O   ? A HIS 201 ? A HIS 201  ? 1_555 73.8  ? 
8  O   ? A ARG 158 ? A ARG 158  ? 1_555 CA ? E CA . ? A CA 500 ? 1_555 O   ? A HIS 201 ? A HIS 201  ? 1_555 82.7  ? 
9  OD2 ? A ASP 167 ? A ASP 167  ? 1_555 CA ? E CA . ? A CA 500 ? 1_555 O   ? A HIS 201 ? A HIS 201  ? 1_555 158.8 ? 
10 OD1 ? A ASP 167 ? A ASP 167  ? 1_555 CA ? E CA . ? A CA 500 ? 1_555 O   ? A HIS 201 ? A HIS 201  ? 1_555 140.0 ? 
11 OD1 ? A ASN 100 ? A ASN 100  ? 1_555 CA ? E CA . ? A CA 500 ? 1_555 O   ? F HOH .   ? A HOH 1016 ? 1_555 70.4  ? 
12 O   ? A ARG 158 ? A ARG 158  ? 1_555 CA ? E CA . ? A CA 500 ? 1_555 O   ? F HOH .   ? A HOH 1016 ? 1_555 124.8 ? 
13 OD2 ? A ASP 167 ? A ASP 167  ? 1_555 CA ? E CA . ? A CA 500 ? 1_555 O   ? F HOH .   ? A HOH 1016 ? 1_555 71.6  ? 
14 OD1 ? A ASP 167 ? A ASP 167  ? 1_555 CA ? E CA . ? A CA 500 ? 1_555 O   ? F HOH .   ? A HOH 1016 ? 1_555 74.3  ? 
15 O   ? A HIS 201 ? A HIS 201  ? 1_555 CA ? E CA . ? A CA 500 ? 1_555 O   ? F HOH .   ? A HOH 1016 ? 1_555 124.5 ? 
16 OD1 ? A ASN 100 ? A ASN 100  ? 1_555 CA ? E CA . ? A CA 500 ? 1_555 O   ? F HOH .   ? A HOH 1023 ? 1_555 105.0 ? 
17 O   ? A ARG 158 ? A ARG 158  ? 1_555 CA ? E CA . ? A CA 500 ? 1_555 O   ? F HOH .   ? A HOH 1023 ? 1_555 74.0  ? 
18 OD2 ? A ASP 167 ? A ASP 167  ? 1_555 CA ? E CA . ? A CA 500 ? 1_555 O   ? F HOH .   ? A HOH 1023 ? 1_555 84.9  ? 
19 OD1 ? A ASP 167 ? A ASP 167  ? 1_555 CA ? E CA . ? A CA 500 ? 1_555 O   ? F HOH .   ? A HOH 1023 ? 1_555 68.6  ? 
20 O   ? A HIS 201 ? A HIS 201  ? 1_555 CA ? E CA . ? A CA 500 ? 1_555 O   ? F HOH .   ? A HOH 1023 ? 1_555 86.6  ? 
21 O   ? F HOH .   ? A HOH 1016 ? 1_555 CA ? E CA . ? A CA 500 ? 1_555 O   ? F HOH .   ? A HOH 1023 ? 1_555 142.9 ? 
22 OD1 ? A ASN 100 ? A ASN 100  ? 1_555 CA ? E CA . ? A CA 500 ? 1_555 O   ? F HOH .   ? A HOH 1035 ? 1_555 104.1 ? 
23 O   ? A ARG 158 ? A ARG 158  ? 1_555 CA ? E CA . ? A CA 500 ? 1_555 O   ? F HOH .   ? A HOH 1035 ? 1_555 70.3  ? 
24 OD2 ? A ASP 167 ? A ASP 167  ? 1_555 CA ? E CA . ? A CA 500 ? 1_555 O   ? F HOH .   ? A HOH 1035 ? 1_555 95.2  ? 
25 OD1 ? A ASP 167 ? A ASP 167  ? 1_555 CA ? E CA . ? A CA 500 ? 1_555 O   ? F HOH .   ? A HOH 1035 ? 1_555 137.7 ? 
26 O   ? A HIS 201 ? A HIS 201  ? 1_555 CA ? E CA . ? A CA 500 ? 1_555 O   ? F HOH .   ? A HOH 1035 ? 1_555 80.2  ? 
27 O   ? F HOH .   ? A HOH 1016 ? 1_555 CA ? E CA . ? A CA 500 ? 1_555 O   ? F HOH .   ? A HOH 1035 ? 1_555 69.3  ? 
28 O   ? F HOH .   ? A HOH 1023 ? 1_555 CA ? E CA . ? A CA 500 ? 1_555 O   ? F HOH .   ? A HOH 1035 ? 1_555 143.1 ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 PCA A 1   ? .   . .   . PCA A 1   ? 1_555 .   . .   . .     .  .  GLN 1 PCA 'Pyrrolidone carboxylic acid' 
'Named protein modification' 
2 CYS A 28  ? CYS A 86  ? CYS A 28  ? 1_555 CYS A 86  ? 1_555 SG SG .   . .   None                          'Disulfide bridge' 
3 CYS A 70  ? CYS A 115 ? CYS A 70  ? 1_555 CYS A 115 ? 1_555 SG SG .   . .   None                          'Disulfide bridge' 
4 CYS A 141 ? CYS A 160 ? CYS A 141 ? 1_555 CYS A 160 ? 1_555 SG SG .   . .   None                          'Disulfide bridge' 
5 CYS A 378 ? CYS A 384 ? CYS A 378 ? 1_555 CYS A 384 ? 1_555 SG SG .   . .   None                          'Disulfide bridge' 
6 CYS A 450 ? CYS A 462 ? CYS A 450 ? 1_555 CYS A 462 ? 1_555 SG SG .   . .   None                          'Disulfide bridge' 
# 
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 ASN 53  A . ? ASN 53  A PRO 54  A ? PRO 54  A 1 -0.17 
2 VAL 129 A . ? VAL 129 A PRO 130 A ? PRO 130 A 1 0.33  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
A1 ? 8 ? 
A2 ? 4 ? 
A3 ? 2 ? 
A4 ? 2 ? 
B1 ? 4 ? 
B2 ? 3 ? 
B3 ? 3 ? 
C1 ? 4 ? 
C2 ? 4 ? 
C3 ? 2 ? 
# 
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 
A1 1 2 ? parallel      
A1 2 3 ? parallel      
A1 3 4 ? parallel      
A1 4 5 ? parallel      
A1 5 6 ? parallel      
A1 6 7 ? parallel      
A1 7 8 ? parallel      
A2 1 2 ? anti-parallel 
A2 2 3 ? parallel      
A2 3 4 ? anti-parallel 
A3 1 2 ? anti-parallel 
A4 1 2 ? anti-parallel 
B1 1 2 ? anti-parallel 
B1 2 3 ? anti-parallel 
B1 3 4 ? anti-parallel 
B2 1 2 ? anti-parallel 
B2 2 3 ? anti-parallel 
B3 1 2 ? parallel      
B3 2 3 ? parallel      
C1 1 2 ? anti-parallel 
C1 2 3 ? anti-parallel 
C1 3 4 ? anti-parallel 
C2 1 2 ? anti-parallel 
C2 2 3 ? anti-parallel 
C2 3 4 ? anti-parallel 
C3 1 2 ? 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 
A1 1 SER A 12  ? LEU A 16  ? SER A 12  LEU A 16  
A1 2 GLY A 38  ? VAL A 42  ? GLY A 38  VAL A 42  
A1 3 ARG A 92  ? ALA A 97  ? ARG A 92  ALA A 97  
A1 4 ALA A 192 ? ASP A 197 ? ALA A 192 ASP A 197 
A1 5 PHE A 229 ? GLU A 233 ? PHE A 229 GLU A 233 
A1 6 ARG A 252 ? GLU A 255 ? ARG A 252 GLU A 255 
A1 7 ARG A 291 ? VAL A 294 ? ARG A 291 VAL A 294 
A1 8 PHE A 335 ? SER A 340 ? PHE A 335 SER A 340 
A2 1 SER A 73  ? GLU A 76  ? SER A 73  GLU A 76  
A2 2 LEU A 69  ? THR A 71  ? LEU A 69  THR A 71  
A2 3 PRO A 45  ? VAL A 50  ? PRO A 45  VAL A 50  
A2 4 GLY A 110 ? THR A 114 ? GLY A 110 THR A 114 
A3 1 ASN A 347 ? VAL A 349 ? ASN A 347 VAL A 349 
A3 2 GLU A 352 ? VAL A 354 ? GLU A 352 VAL A 354 
A4 1 THR A 371 ? ASN A 373 ? THR A 371 ASN A 373 
A4 2 THR A 376 ? GLY A 379 ? THR A 376 GLY A 379 
B1 1 GLY A 110 ? THR A 114 ? GLY A 110 THR A 114 
B1 2 CYS A 119 ? PRO A 121 ? CYS A 119 PRO A 121 
B1 3 ARG A 124 ? PRO A 127 ? ARG A 124 PRO A 127 
B1 4 TYR A 131 ? ALA A 133 ? TYR A 131 ALA A 133 
B2 1 ASN A 100 ? SER A 105 ? ASN A 100 SER A 105 
B2 2 GLY A 164 ? ALA A 169 ? GLY A 164 ALA A 169 
B2 3 ASP A 135 ? ASN A 137 ? ASP A 135 ASN A 137 
B3 1 GLY A 146 ? ILE A 148 ? GLY A 146 ILE A 148 
B3 2 GLN A 161 ? LEU A 162 ? GLN A 161 LEU A 162 
B3 3 GLY A 164 ? ALA A 169 ? GLY A 164 ALA A 169 
C1 1 PRO A 405 ? ASN A 412 ? PRO A 405 ASN A 412 
C1 2 ASN A 415 ? GLY A 422 ? ASN A 415 GLY A 422 
C1 3 ARG A 424 ? ASN A 431 ? ARG A 424 ASN A 431 
C1 4 PRO A 486 ? ALA A 492 ? PRO A 486 ALA A 492 
C2 1 LEU A 436 ? THR A 442 ? LEU A 436 THR A 442 
C2 2 GLY A 473 ? ILE A 479 ? GLY A 473 ILE A 479 
C2 3 ILE A 465 ? SER A 470 ? ILE A 465 SER A 470 
C2 4 GLY A 447 ? ASP A 451 ? GLY A 447 ASP A 451 
C3 1 ASP A 456 ? VAL A 458 ? ASP A 456 VAL A 458 
C3 2 SER A 461 ? THR A 463 ? SER A 461 THR A 463 
# 
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 
A1 1 2 O SER A 12  ? O SER A 12  N GLY A 38  ? N GLY A 38  
A1 2 3 O GLY A 38  ? O GLY A 38  N ARG A 92  ? N ARG A 92  
A1 3 4 O ILE A 93  ? O ILE A 93  N ALA A 192 ? N ALA A 192 
A1 4 5 O ALA A 192 ? O ALA A 192 N PHE A 229 ? N PHE A 229 
A1 5 6 O ILE A 230 ? O ILE A 230 N ARG A 252 ? N ARG A 252 
A1 6 7 N VAL A 253 ? N VAL A 253 O ARG A 291 ? O ARG A 291 
A1 7 8 O ALA A 292 ? O ALA A 292 N PHE A 335 ? N PHE A 335 
A2 1 2 N SER A 73  ? N SER A 73  O CYS A 70  ? O CYS A 70  
A2 2 3 N CYS A 70  ? N CYS A 70  O PRO A 45  ? O PRO A 45  
A2 3 4 O ASN A 48  ? O ASN A 48  N THR A 114 ? N THR A 114 
A3 1 2 O ASN A 347 ? O ASN A 347 N VAL A 354 ? N VAL A 354 
A4 1 2 O THR A 371 ? O THR A 371 N GLY A 379 ? N GLY A 379 
B1 1 2 N GLY A 110 ? N GLY A 110 O CYS A 119 ? O CYS A 119 
B1 2 3 O PRO A 121 ? O PRO A 121 N ARG A 124 ? N ARG A 124 
B1 3 4 O ARG A 124 ? O ARG A 124 N ALA A 133 ? N ALA A 133 
B2 1 2 O ASN A 100 ? O ASN A 100 N LEU A 168 ? N LEU A 168 
B2 2 3 N ALA A 169 ? N ALA A 169 O ASP A 135 ? O ASP A 135 
B3 1 2 O GLY A 146 ? O GLY A 146 N GLN A 161 ? N GLN A 161 
B3 2 3 O LEU A 162 ? O LEU A 162 N LEU A 165 ? N LEU A 165 
C1 1 2 N ASN A 412 ? N ASN A 412 O GLN A 416 ? O GLN A 416 
C1 2 3 O ASN A 415 ? O ASN A 415 N ASN A 431 ? N ASN A 431 
C1 3 4 N ASN A 430 ? N ASN A 430 O PRO A 486 ? O PRO A 486 
C2 1 2 N THR A 442 ? N THR A 442 O GLY A 473 ? O GLY A 473 
C2 2 3 N GLY A 473 ? N GLY A 473 O SER A 470 ? O SER A 470 
C2 3 4 O VAL A 469 ? O VAL A 469 N GLY A 447 ? N GLY A 447 
C3 1 2 O ASP A 456 ? O ASP A 456 N THR A 463 ? N THR A 463 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AS1 Unknown ? ? ? ? 3 'ACTIVE SITE, SUGAR BINDING SITE.' 
AS2 Unknown ? ? ? ? 3 'ACTIVE SITE, SUGAR BINDING SITE.' 
AS3 Unknown ? ? ? ? 4 'ACTIVE SITE, SUGAR BINDING SITE.' 
AS4 Unknown ? ? ? ? 3 'ACTIVE SITE, SUGAR BINDING SITE.' 
AS5 Unknown ? ? ? ? 2 'ACTIVE SITE, SUGAR BINDING SITE.' 
CAL Unknown ? ? ? ? 4 'CALCIUM BINDING SITE.' 
CLO Unknown ? ? ? ? 3 
'CHLORIDE BINDING SITE. THERE ARE SIX BOUND SUGAR RINGS. SITE *CAL* CONTAINS 3 WATERS. SITE *CLO* CONTAINS 1 WATER.' 
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1  AS1 3 VAL A 163 ? VAL A 163 . ? 1_555 ? 
2  AS1 3 GLN A 63  ? GLN A 63  . ? 1_555 ? 
3  AS1 3 LEU A 165 ? LEU A 165 . ? 1_555 ? 
4  AS2 3 HIS A 305 ? HIS A 305 . ? 1_555 ? 
5  AS2 3 GLN A 63  ? GLN A 63  . ? 1_555 ? 
6  AS2 3 TRP A 59  ? TRP A 59  . ? 1_555 ? 
7  AS3 4 ASP A 300 ? ASP A 300 . ? 1_555 ? 
8  AS3 4 HIS A 299 ? HIS A 299 . ? 1_555 ? 
9  AS3 4 ASP A 197 ? ASP A 197 . ? 1_555 ? 
10 AS3 4 HIS A 101 ? HIS A 101 . ? 1_555 ? 
11 AS4 3 HIS A 201 ? HIS A 201 . ? 1_555 ? 
12 AS4 3 GLU A 233 ? GLU A 233 . ? 1_555 ? 
13 AS4 3 ASP A 300 ? ASP A 300 . ? 1_555 ? 
14 AS5 2 GLU A 240 ? GLU A 240 . ? 1_555 ? 
15 AS5 2 LYS A 200 ? LYS A 200 . ? 1_555 ? 
16 CAL 4 ASN A 100 ? ASN A 100 . ? 1_555 ? 
17 CAL 4 ARG A 158 ? ARG A 158 . ? 1_555 ? 
18 CAL 4 ASP A 167 ? ASP A 167 . ? 1_555 ? 
19 CAL 4 HIS A 201 ? HIS A 201 . ? 1_555 ? 
20 CLO 3 ARG A 195 ? ARG A 195 . ? 1_555 ? 
21 CLO 3 ASN A 298 ? ASN A 298 . ? 1_555 ? 
22 CLO 3 ARG A 337 ? ARG A 337 . ? 1_555 ? 
# 
_pdbx_entry_details.entry_id                   1OSE 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             CA 
_pdbx_validate_rmsd_angle.auth_asym_id_1             A 
_pdbx_validate_rmsd_angle.auth_comp_id_1             VAL 
_pdbx_validate_rmsd_angle.auth_seq_id_1              323 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             CB 
_pdbx_validate_rmsd_angle.auth_asym_id_2             A 
_pdbx_validate_rmsd_angle.auth_comp_id_2             VAL 
_pdbx_validate_rmsd_angle.auth_seq_id_2              323 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             CG2 
_pdbx_validate_rmsd_angle.auth_asym_id_3             A 
_pdbx_validate_rmsd_angle.auth_comp_id_3             VAL 
_pdbx_validate_rmsd_angle.auth_seq_id_3              323 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                132.32 
_pdbx_validate_rmsd_angle.angle_target_value         110.90 
_pdbx_validate_rmsd_angle.angle_deviation            21.42 
_pdbx_validate_rmsd_angle.angle_standard_deviation   1.50 
_pdbx_validate_rmsd_angle.linker_flag                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 TYR A 31  ? ? -135.34 -60.30  
2 1 SER A 55  ? ? -61.33  99.47   
3 1 SER A 66  ? ? -171.93 -177.62 
4 1 MET A 102 ? ? -113.58 -151.84 
5 1 ASP A 317 ? ? -110.18 57.90   
6 1 SER A 414 ? ? -137.79 -105.72 
7 1 PRO A 486 ? ? -70.60  35.74   
# 
_pdbx_struct_mod_residue.id               1 
_pdbx_struct_mod_residue.label_asym_id    A 
_pdbx_struct_mod_residue.label_comp_id    PCA 
_pdbx_struct_mod_residue.label_seq_id     1 
_pdbx_struct_mod_residue.auth_asym_id     A 
_pdbx_struct_mod_residue.auth_comp_id     PCA 
_pdbx_struct_mod_residue.auth_seq_id      1 
_pdbx_struct_mod_residue.PDB_ins_code     ? 
_pdbx_struct_mod_residue.parent_comp_id   GLN 
_pdbx_struct_mod_residue.details          'PYROGLUTAMIC ACID' 
# 
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 
AC1 C1   C  N S 1   
AC1 O2   O  N N 2   
AC1 C2   C  N R 3   
AC1 C4A  C  N R 4   
AC1 C3   C  N S 5   
AC1 O3   O  N N 6   
AC1 C4   C  N S 7   
AC1 N4A  N  N N 8   
AC1 C5   C  N R 9   
AC1 O5   O  N N 10  
AC1 C6   C  N N 11  
AC1 C1B  C  N S 12  
AC1 C2B  C  N S 13  
AC1 O2B  O  N N 14  
AC1 C3B  C  N S 15  
AC1 O3B  O  N N 16  
AC1 O4   O  N N 17  
AC1 C5B  C  N N 18  
AC1 C7B  C  N N 19  
AC1 C6B  C  N N 20  
AC1 O6B  O  N N 21  
AC1 O1   O  N N 22  
AC1 H1   H  N N 23  
AC1 HO2  H  N N 24  
AC1 H2   H  N N 25  
AC1 HC4  H  N N 26  
AC1 H3   H  N N 27  
AC1 HO3  H  N N 28  
AC1 H4   H  N N 29  
AC1 HN4  H  N N 30  
AC1 H5   H  N N 31  
AC1 H61  H  N N 32  
AC1 H62  H  N N 33  
AC1 H63  H  N N 34  
AC1 HCB1 H  N N 35  
AC1 HCB2 H  N N 36  
AC1 HO2B H  N N 37  
AC1 HCB3 H  N N 38  
AC1 HOB3 H  N N 39  
AC1 HO4  H  N N 40  
AC1 HC7  H  N N 41  
AC1 HC61 H  N N 42  
AC1 HC62 H  N N 43  
AC1 HO6B H  N N 44  
AC1 HO1  H  N N 45  
ALA N    N  N N 46  
ALA CA   C  N S 47  
ALA C    C  N N 48  
ALA O    O  N N 49  
ALA CB   C  N N 50  
ALA OXT  O  N N 51  
ALA H    H  N N 52  
ALA H2   H  N N 53  
ALA HA   H  N N 54  
ALA HB1  H  N N 55  
ALA HB2  H  N N 56  
ALA HB3  H  N N 57  
ALA HXT  H  N N 58  
ARG N    N  N N 59  
ARG CA   C  N S 60  
ARG C    C  N N 61  
ARG O    O  N N 62  
ARG CB   C  N N 63  
ARG CG   C  N N 64  
ARG CD   C  N N 65  
ARG NE   N  N N 66  
ARG CZ   C  N N 67  
ARG NH1  N  N N 68  
ARG NH2  N  N N 69  
ARG OXT  O  N N 70  
ARG H    H  N N 71  
ARG H2   H  N N 72  
ARG HA   H  N N 73  
ARG HB2  H  N N 74  
ARG HB3  H  N N 75  
ARG HG2  H  N N 76  
ARG HG3  H  N N 77  
ARG HD2  H  N N 78  
ARG HD3  H  N N 79  
ARG HE   H  N N 80  
ARG HH11 H  N N 81  
ARG HH12 H  N N 82  
ARG HH21 H  N N 83  
ARG HH22 H  N N 84  
ARG HXT  H  N N 85  
ASN N    N  N N 86  
ASN CA   C  N S 87  
ASN C    C  N N 88  
ASN O    O  N N 89  
ASN CB   C  N N 90  
ASN CG   C  N N 91  
ASN OD1  O  N N 92  
ASN ND2  N  N N 93  
ASN OXT  O  N N 94  
ASN H    H  N N 95  
ASN H2   H  N N 96  
ASN HA   H  N N 97  
ASN HB2  H  N N 98  
ASN HB3  H  N N 99  
ASN HD21 H  N N 100 
ASN HD22 H  N N 101 
ASN HXT  H  N N 102 
ASP N    N  N N 103 
ASP CA   C  N S 104 
ASP C    C  N N 105 
ASP O    O  N N 106 
ASP CB   C  N N 107 
ASP CG   C  N N 108 
ASP OD1  O  N N 109 
ASP OD2  O  N N 110 
ASP OXT  O  N N 111 
ASP H    H  N N 112 
ASP H2   H  N N 113 
ASP HA   H  N N 114 
ASP HB2  H  N N 115 
ASP HB3  H  N N 116 
ASP HD2  H  N N 117 
ASP HXT  H  N N 118 
BGC C2   C  N R 119 
BGC C3   C  N S 120 
BGC C4   C  N S 121 
BGC C5   C  N R 122 
BGC C6   C  N N 123 
BGC C1   C  N R 124 
BGC O1   O  N N 125 
BGC O2   O  N N 126 
BGC O3   O  N N 127 
BGC O4   O  N N 128 
BGC O5   O  N N 129 
BGC O6   O  N N 130 
BGC H2   H  N N 131 
BGC H3   H  N N 132 
BGC H4   H  N N 133 
BGC H5   H  N N 134 
BGC H61  H  N N 135 
BGC H62  H  N N 136 
BGC H1   H  N N 137 
BGC HO1  H  N N 138 
BGC HO2  H  N N 139 
BGC HO3  H  N N 140 
BGC HO4  H  N N 141 
BGC HO6  H  N N 142 
CA  CA   CA N N 143 
CL  CL   CL N N 144 
CYS N    N  N N 145 
CYS CA   C  N R 146 
CYS C    C  N N 147 
CYS O    O  N N 148 
CYS CB   C  N N 149 
CYS SG   S  N N 150 
CYS OXT  O  N N 151 
CYS H    H  N N 152 
CYS H2   H  N N 153 
CYS HA   H  N N 154 
CYS HB2  H  N N 155 
CYS HB3  H  N N 156 
CYS HG   H  N N 157 
CYS HXT  H  N N 158 
GLC C1   C  N S 159 
GLC C2   C  N R 160 
GLC C3   C  N S 161 
GLC C4   C  N S 162 
GLC C5   C  N R 163 
GLC C6   C  N N 164 
GLC O1   O  N N 165 
GLC O2   O  N N 166 
GLC O3   O  N N 167 
GLC O4   O  N N 168 
GLC O5   O  N N 169 
GLC O6   O  N N 170 
GLC H1   H  N N 171 
GLC H2   H  N N 172 
GLC H3   H  N N 173 
GLC H4   H  N N 174 
GLC H5   H  N N 175 
GLC H61  H  N N 176 
GLC H62  H  N N 177 
GLC HO1  H  N N 178 
GLC HO2  H  N N 179 
GLC HO3  H  N N 180 
GLC HO4  H  N N 181 
GLC HO6  H  N N 182 
GLN N    N  N N 183 
GLN CA   C  N S 184 
GLN C    C  N N 185 
GLN O    O  N N 186 
GLN CB   C  N N 187 
GLN CG   C  N N 188 
GLN CD   C  N N 189 
GLN OE1  O  N N 190 
GLN NE2  N  N N 191 
GLN OXT  O  N N 192 
GLN H    H  N N 193 
GLN H2   H  N N 194 
GLN HA   H  N N 195 
GLN HB2  H  N N 196 
GLN HB3  H  N N 197 
GLN HG2  H  N N 198 
GLN HG3  H  N N 199 
GLN HE21 H  N N 200 
GLN HE22 H  N N 201 
GLN HXT  H  N N 202 
GLU N    N  N N 203 
GLU CA   C  N S 204 
GLU C    C  N N 205 
GLU O    O  N N 206 
GLU CB   C  N N 207 
GLU CG   C  N N 208 
GLU CD   C  N N 209 
GLU OE1  O  N N 210 
GLU OE2  O  N N 211 
GLU OXT  O  N N 212 
GLU H    H  N N 213 
GLU H2   H  N N 214 
GLU HA   H  N N 215 
GLU HB2  H  N N 216 
GLU HB3  H  N N 217 
GLU HG2  H  N N 218 
GLU HG3  H  N N 219 
GLU HE2  H  N N 220 
GLU HXT  H  N N 221 
GLY N    N  N N 222 
GLY CA   C  N N 223 
GLY C    C  N N 224 
GLY O    O  N N 225 
GLY OXT  O  N N 226 
GLY H    H  N N 227 
GLY H2   H  N N 228 
GLY HA2  H  N N 229 
GLY HA3  H  N N 230 
GLY HXT  H  N N 231 
HIS N    N  N N 232 
HIS CA   C  N S 233 
HIS C    C  N N 234 
HIS O    O  N N 235 
HIS CB   C  N N 236 
HIS CG   C  Y N 237 
HIS ND1  N  Y N 238 
HIS CD2  C  Y N 239 
HIS CE1  C  Y N 240 
HIS NE2  N  Y N 241 
HIS OXT  O  N N 242 
HIS H    H  N N 243 
HIS H2   H  N N 244 
HIS HA   H  N N 245 
HIS HB2  H  N N 246 
HIS HB3  H  N N 247 
HIS HD1  H  N N 248 
HIS HD2  H  N N 249 
HIS HE1  H  N N 250 
HIS HE2  H  N N 251 
HIS HXT  H  N N 252 
HOH O    O  N N 253 
HOH H1   H  N N 254 
HOH H2   H  N N 255 
ILE N    N  N N 256 
ILE CA   C  N S 257 
ILE C    C  N N 258 
ILE O    O  N N 259 
ILE CB   C  N S 260 
ILE CG1  C  N N 261 
ILE CG2  C  N N 262 
ILE CD1  C  N N 263 
ILE OXT  O  N N 264 
ILE H    H  N N 265 
ILE H2   H  N N 266 
ILE HA   H  N N 267 
ILE HB   H  N N 268 
ILE HG12 H  N N 269 
ILE HG13 H  N N 270 
ILE HG21 H  N N 271 
ILE HG22 H  N N 272 
ILE HG23 H  N N 273 
ILE HD11 H  N N 274 
ILE HD12 H  N N 275 
ILE HD13 H  N N 276 
ILE HXT  H  N N 277 
LEU N    N  N N 278 
LEU CA   C  N S 279 
LEU C    C  N N 280 
LEU O    O  N N 281 
LEU CB   C  N N 282 
LEU CG   C  N N 283 
LEU CD1  C  N N 284 
LEU CD2  C  N N 285 
LEU OXT  O  N N 286 
LEU H    H  N N 287 
LEU H2   H  N N 288 
LEU HA   H  N N 289 
LEU HB2  H  N N 290 
LEU HB3  H  N N 291 
LEU HG   H  N N 292 
LEU HD11 H  N N 293 
LEU HD12 H  N N 294 
LEU HD13 H  N N 295 
LEU HD21 H  N N 296 
LEU HD22 H  N N 297 
LEU HD23 H  N N 298 
LEU HXT  H  N N 299 
LYS N    N  N N 300 
LYS CA   C  N S 301 
LYS C    C  N N 302 
LYS O    O  N N 303 
LYS CB   C  N N 304 
LYS CG   C  N N 305 
LYS CD   C  N N 306 
LYS CE   C  N N 307 
LYS NZ   N  N N 308 
LYS OXT  O  N N 309 
LYS H    H  N N 310 
LYS H2   H  N N 311 
LYS HA   H  N N 312 
LYS HB2  H  N N 313 
LYS HB3  H  N N 314 
LYS HG2  H  N N 315 
LYS HG3  H  N N 316 
LYS HD2  H  N N 317 
LYS HD3  H  N N 318 
LYS HE2  H  N N 319 
LYS HE3  H  N N 320 
LYS HZ1  H  N N 321 
LYS HZ2  H  N N 322 
LYS HZ3  H  N N 323 
LYS HXT  H  N N 324 
MET N    N  N N 325 
MET CA   C  N S 326 
MET C    C  N N 327 
MET O    O  N N 328 
MET CB   C  N N 329 
MET CG   C  N N 330 
MET SD   S  N N 331 
MET CE   C  N N 332 
MET OXT  O  N N 333 
MET H    H  N N 334 
MET H2   H  N N 335 
MET HA   H  N N 336 
MET HB2  H  N N 337 
MET HB3  H  N N 338 
MET HG2  H  N N 339 
MET HG3  H  N N 340 
MET HE1  H  N N 341 
MET HE2  H  N N 342 
MET HE3  H  N N 343 
MET HXT  H  N N 344 
PCA N    N  N N 345 
PCA CA   C  N S 346 
PCA CB   C  N N 347 
PCA CG   C  N N 348 
PCA CD   C  N N 349 
PCA OE   O  N N 350 
PCA C    C  N N 351 
PCA O    O  N N 352 
PCA OXT  O  N N 353 
PCA H    H  N N 354 
PCA HA   H  N N 355 
PCA HB2  H  N N 356 
PCA HB3  H  N N 357 
PCA HG2  H  N N 358 
PCA HG3  H  N N 359 
PCA HXT  H  N N 360 
PHE N    N  N N 361 
PHE CA   C  N S 362 
PHE C    C  N N 363 
PHE O    O  N N 364 
PHE CB   C  N N 365 
PHE CG   C  Y N 366 
PHE CD1  C  Y N 367 
PHE CD2  C  Y N 368 
PHE CE1  C  Y N 369 
PHE CE2  C  Y N 370 
PHE CZ   C  Y N 371 
PHE OXT  O  N N 372 
PHE H    H  N N 373 
PHE H2   H  N N 374 
PHE HA   H  N N 375 
PHE HB2  H  N N 376 
PHE HB3  H  N N 377 
PHE HD1  H  N N 378 
PHE HD2  H  N N 379 
PHE HE1  H  N N 380 
PHE HE2  H  N N 381 
PHE HZ   H  N N 382 
PHE HXT  H  N N 383 
PRO N    N  N N 384 
PRO CA   C  N S 385 
PRO C    C  N N 386 
PRO O    O  N N 387 
PRO CB   C  N N 388 
PRO CG   C  N N 389 
PRO CD   C  N N 390 
PRO OXT  O  N N 391 
PRO H    H  N N 392 
PRO HA   H  N N 393 
PRO HB2  H  N N 394 
PRO HB3  H  N N 395 
PRO HG2  H  N N 396 
PRO HG3  H  N N 397 
PRO HD2  H  N N 398 
PRO HD3  H  N N 399 
PRO HXT  H  N N 400 
SER N    N  N N 401 
SER CA   C  N S 402 
SER C    C  N N 403 
SER O    O  N N 404 
SER CB   C  N N 405 
SER OG   O  N N 406 
SER OXT  O  N N 407 
SER H    H  N N 408 
SER H2   H  N N 409 
SER HA   H  N N 410 
SER HB2  H  N N 411 
SER HB3  H  N N 412 
SER HG   H  N N 413 
SER HXT  H  N N 414 
THR N    N  N N 415 
THR CA   C  N S 416 
THR C    C  N N 417 
THR O    O  N N 418 
THR CB   C  N R 419 
THR OG1  O  N N 420 
THR CG2  C  N N 421 
THR OXT  O  N N 422 
THR H    H  N N 423 
THR H2   H  N N 424 
THR HA   H  N N 425 
THR HB   H  N N 426 
THR HG1  H  N N 427 
THR HG21 H  N N 428 
THR HG22 H  N N 429 
THR HG23 H  N N 430 
THR HXT  H  N N 431 
TRP N    N  N N 432 
TRP CA   C  N S 433 
TRP C    C  N N 434 
TRP O    O  N N 435 
TRP CB   C  N N 436 
TRP CG   C  Y N 437 
TRP CD1  C  Y N 438 
TRP CD2  C  Y N 439 
TRP NE1  N  Y N 440 
TRP CE2  C  Y N 441 
TRP CE3  C  Y N 442 
TRP CZ2  C  Y N 443 
TRP CZ3  C  Y N 444 
TRP CH2  C  Y N 445 
TRP OXT  O  N N 446 
TRP H    H  N N 447 
TRP H2   H  N N 448 
TRP HA   H  N N 449 
TRP HB2  H  N N 450 
TRP HB3  H  N N 451 
TRP HD1  H  N N 452 
TRP HE1  H  N N 453 
TRP HE3  H  N N 454 
TRP HZ2  H  N N 455 
TRP HZ3  H  N N 456 
TRP HH2  H  N N 457 
TRP HXT  H  N N 458 
TYR N    N  N N 459 
TYR CA   C  N S 460 
TYR C    C  N N 461 
TYR O    O  N N 462 
TYR CB   C  N N 463 
TYR CG   C  Y N 464 
TYR CD1  C  Y N 465 
TYR CD2  C  Y N 466 
TYR CE1  C  Y N 467 
TYR CE2  C  Y N 468 
TYR CZ   C  Y N 469 
TYR OH   O  N N 470 
TYR OXT  O  N N 471 
TYR H    H  N N 472 
TYR H2   H  N N 473 
TYR HA   H  N N 474 
TYR HB2  H  N N 475 
TYR HB3  H  N N 476 
TYR HD1  H  N N 477 
TYR HD2  H  N N 478 
TYR HE1  H  N N 479 
TYR HE2  H  N N 480 
TYR HH   H  N N 481 
TYR HXT  H  N N 482 
VAL N    N  N N 483 
VAL CA   C  N S 484 
VAL C    C  N N 485 
VAL O    O  N N 486 
VAL CB   C  N N 487 
VAL CG1  C  N N 488 
VAL CG2  C  N N 489 
VAL OXT  O  N N 490 
VAL H    H  N N 491 
VAL H2   H  N N 492 
VAL HA   H  N N 493 
VAL HB   H  N N 494 
VAL HG11 H  N N 495 
VAL HG12 H  N N 496 
VAL HG13 H  N N 497 
VAL HG21 H  N N 498 
VAL HG22 H  N N 499 
VAL HG23 H  N N 500 
VAL HXT  H  N N 501 
# 
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 
AC1 C1  C2   sing N N 1   
AC1 C1  O5   sing N N 2   
AC1 C1  O1   sing N N 3   
AC1 C1  H1   sing N N 4   
AC1 O2  C2   sing N N 5   
AC1 O2  HO2  sing N N 6   
AC1 C2  C3   sing N N 7   
AC1 C2  H2   sing N N 8   
AC1 C4A C3B  sing N N 9   
AC1 C4A O4   sing N N 10  
AC1 C4A C5B  sing N N 11  
AC1 C4A HC4  sing N N 12  
AC1 C3  O3   sing N N 13  
AC1 C3  C4   sing N N 14  
AC1 C3  H3   sing N N 15  
AC1 O3  HO3  sing N N 16  
AC1 C4  N4A  sing N N 17  
AC1 C4  C5   sing N N 18  
AC1 C4  H4   sing N N 19  
AC1 N4A C1B  sing N N 20  
AC1 N4A HN4  sing N N 21  
AC1 C5  O5   sing N N 22  
AC1 C5  C6   sing N N 23  
AC1 C5  H5   sing N N 24  
AC1 C6  H61  sing N N 25  
AC1 C6  H62  sing N N 26  
AC1 C6  H63  sing N N 27  
AC1 C1B C2B  sing N N 28  
AC1 C1B C7B  sing N N 29  
AC1 C1B HCB1 sing N N 30  
AC1 C2B O2B  sing N N 31  
AC1 C2B C3B  sing N N 32  
AC1 C2B HCB2 sing N N 33  
AC1 O2B HO2B sing N N 34  
AC1 C3B O3B  sing N N 35  
AC1 C3B HCB3 sing N N 36  
AC1 O3B HOB3 sing N N 37  
AC1 O4  HO4  sing N N 38  
AC1 C5B C7B  doub N N 39  
AC1 C5B C6B  sing N N 40  
AC1 C7B HC7  sing N N 41  
AC1 C6B O6B  sing N N 42  
AC1 C6B HC61 sing N N 43  
AC1 C6B HC62 sing N N 44  
AC1 O6B HO6B sing N N 45  
AC1 O1  HO1  sing N N 46  
ALA N   CA   sing N N 47  
ALA N   H    sing N N 48  
ALA N   H2   sing N N 49  
ALA CA  C    sing N N 50  
ALA CA  CB   sing N N 51  
ALA CA  HA   sing N N 52  
ALA C   O    doub N N 53  
ALA C   OXT  sing N N 54  
ALA CB  HB1  sing N N 55  
ALA CB  HB2  sing N N 56  
ALA CB  HB3  sing N N 57  
ALA OXT HXT  sing N N 58  
ARG N   CA   sing N N 59  
ARG N   H    sing N N 60  
ARG N   H2   sing N N 61  
ARG CA  C    sing N N 62  
ARG CA  CB   sing N N 63  
ARG CA  HA   sing N N 64  
ARG C   O    doub N N 65  
ARG C   OXT  sing N N 66  
ARG CB  CG   sing N N 67  
ARG CB  HB2  sing N N 68  
ARG CB  HB3  sing N N 69  
ARG CG  CD   sing N N 70  
ARG CG  HG2  sing N N 71  
ARG CG  HG3  sing N N 72  
ARG CD  NE   sing N N 73  
ARG CD  HD2  sing N N 74  
ARG CD  HD3  sing N N 75  
ARG NE  CZ   sing N N 76  
ARG NE  HE   sing N N 77  
ARG CZ  NH1  sing N N 78  
ARG CZ  NH2  doub N N 79  
ARG NH1 HH11 sing N N 80  
ARG NH1 HH12 sing N N 81  
ARG NH2 HH21 sing N N 82  
ARG NH2 HH22 sing N N 83  
ARG OXT HXT  sing N N 84  
ASN N   CA   sing N N 85  
ASN N   H    sing N N 86  
ASN N   H2   sing N N 87  
ASN CA  C    sing N N 88  
ASN CA  CB   sing N N 89  
ASN CA  HA   sing N N 90  
ASN C   O    doub N N 91  
ASN C   OXT  sing N N 92  
ASN CB  CG   sing N N 93  
ASN CB  HB2  sing N N 94  
ASN CB  HB3  sing N N 95  
ASN CG  OD1  doub N N 96  
ASN CG  ND2  sing N N 97  
ASN ND2 HD21 sing N N 98  
ASN ND2 HD22 sing N N 99  
ASN OXT HXT  sing N N 100 
ASP N   CA   sing N N 101 
ASP N   H    sing N N 102 
ASP N   H2   sing N N 103 
ASP CA  C    sing N N 104 
ASP CA  CB   sing N N 105 
ASP CA  HA   sing N N 106 
ASP C   O    doub N N 107 
ASP C   OXT  sing N N 108 
ASP CB  CG   sing N N 109 
ASP CB  HB2  sing N N 110 
ASP CB  HB3  sing N N 111 
ASP CG  OD1  doub N N 112 
ASP CG  OD2  sing N N 113 
ASP OD2 HD2  sing N N 114 
ASP OXT HXT  sing N N 115 
BGC C2  C3   sing N N 116 
BGC C2  C1   sing N N 117 
BGC C2  O2   sing N N 118 
BGC C2  H2   sing N N 119 
BGC C3  C4   sing N N 120 
BGC C3  O3   sing N N 121 
BGC C3  H3   sing N N 122 
BGC C4  C5   sing N N 123 
BGC C4  O4   sing N N 124 
BGC C4  H4   sing N N 125 
BGC C5  C6   sing N N 126 
BGC C5  O5   sing N N 127 
BGC C5  H5   sing N N 128 
BGC C6  O6   sing N N 129 
BGC C6  H61  sing N N 130 
BGC C6  H62  sing N N 131 
BGC C1  O1   sing N N 132 
BGC C1  O5   sing N N 133 
BGC C1  H1   sing N N 134 
BGC O1  HO1  sing N N 135 
BGC O2  HO2  sing N N 136 
BGC O3  HO3  sing N N 137 
BGC O4  HO4  sing N N 138 
BGC O6  HO6  sing N N 139 
CYS N   CA   sing N N 140 
CYS N   H    sing N N 141 
CYS N   H2   sing N N 142 
CYS CA  C    sing N N 143 
CYS CA  CB   sing N N 144 
CYS CA  HA   sing N N 145 
CYS C   O    doub N N 146 
CYS C   OXT  sing N N 147 
CYS CB  SG   sing N N 148 
CYS CB  HB2  sing N N 149 
CYS CB  HB3  sing N N 150 
CYS SG  HG   sing N N 151 
CYS OXT HXT  sing N N 152 
GLC C1  C2   sing N N 153 
GLC C1  O1   sing N N 154 
GLC C1  O5   sing N N 155 
GLC C1  H1   sing N N 156 
GLC C2  C3   sing N N 157 
GLC C2  O2   sing N N 158 
GLC C2  H2   sing N N 159 
GLC C3  C4   sing N N 160 
GLC C3  O3   sing N N 161 
GLC C3  H3   sing N N 162 
GLC C4  C5   sing N N 163 
GLC C4  O4   sing N N 164 
GLC C4  H4   sing N N 165 
GLC C5  C6   sing N N 166 
GLC C5  O5   sing N N 167 
GLC C5  H5   sing N N 168 
GLC C6  O6   sing N N 169 
GLC C6  H61  sing N N 170 
GLC C6  H62  sing N N 171 
GLC O1  HO1  sing N N 172 
GLC O2  HO2  sing N N 173 
GLC O3  HO3  sing N N 174 
GLC O4  HO4  sing N N 175 
GLC O6  HO6  sing N N 176 
GLN N   CA   sing N N 177 
GLN N   H    sing N N 178 
GLN N   H2   sing N N 179 
GLN CA  C    sing N N 180 
GLN CA  CB   sing N N 181 
GLN CA  HA   sing N N 182 
GLN C   O    doub N N 183 
GLN C   OXT  sing N N 184 
GLN CB  CG   sing N N 185 
GLN CB  HB2  sing N N 186 
GLN CB  HB3  sing N N 187 
GLN CG  CD   sing N N 188 
GLN CG  HG2  sing N N 189 
GLN CG  HG3  sing N N 190 
GLN CD  OE1  doub N N 191 
GLN CD  NE2  sing N N 192 
GLN NE2 HE21 sing N N 193 
GLN NE2 HE22 sing N N 194 
GLN OXT HXT  sing N N 195 
GLU N   CA   sing N N 196 
GLU N   H    sing N N 197 
GLU N   H2   sing N N 198 
GLU CA  C    sing N N 199 
GLU CA  CB   sing N N 200 
GLU CA  HA   sing N N 201 
GLU C   O    doub N N 202 
GLU C   OXT  sing N N 203 
GLU CB  CG   sing N N 204 
GLU CB  HB2  sing N N 205 
GLU CB  HB3  sing N N 206 
GLU CG  CD   sing N N 207 
GLU CG  HG2  sing N N 208 
GLU CG  HG3  sing N N 209 
GLU CD  OE1  doub N N 210 
GLU CD  OE2  sing N N 211 
GLU OE2 HE2  sing N N 212 
GLU OXT HXT  sing N N 213 
GLY N   CA   sing N N 214 
GLY N   H    sing N N 215 
GLY N   H2   sing N N 216 
GLY CA  C    sing N N 217 
GLY CA  HA2  sing N N 218 
GLY CA  HA3  sing N N 219 
GLY C   O    doub N N 220 
GLY C   OXT  sing N N 221 
GLY OXT HXT  sing N N 222 
HIS N   CA   sing N N 223 
HIS N   H    sing N N 224 
HIS N   H2   sing N N 225 
HIS CA  C    sing N N 226 
HIS CA  CB   sing N N 227 
HIS CA  HA   sing N N 228 
HIS C   O    doub N N 229 
HIS C   OXT  sing N N 230 
HIS CB  CG   sing N N 231 
HIS CB  HB2  sing N N 232 
HIS CB  HB3  sing N N 233 
HIS CG  ND1  sing Y N 234 
HIS CG  CD2  doub Y N 235 
HIS ND1 CE1  doub Y N 236 
HIS ND1 HD1  sing N N 237 
HIS CD2 NE2  sing Y N 238 
HIS CD2 HD2  sing N N 239 
HIS CE1 NE2  sing Y N 240 
HIS CE1 HE1  sing N N 241 
HIS NE2 HE2  sing N N 242 
HIS OXT HXT  sing N N 243 
HOH O   H1   sing N N 244 
HOH O   H2   sing N N 245 
ILE N   CA   sing N N 246 
ILE N   H    sing N N 247 
ILE N   H2   sing N N 248 
ILE CA  C    sing N N 249 
ILE CA  CB   sing N N 250 
ILE CA  HA   sing N N 251 
ILE C   O    doub N N 252 
ILE C   OXT  sing N N 253 
ILE CB  CG1  sing N N 254 
ILE CB  CG2  sing N N 255 
ILE CB  HB   sing N N 256 
ILE CG1 CD1  sing N N 257 
ILE CG1 HG12 sing N N 258 
ILE CG1 HG13 sing N N 259 
ILE CG2 HG21 sing N N 260 
ILE CG2 HG22 sing N N 261 
ILE CG2 HG23 sing N N 262 
ILE CD1 HD11 sing N N 263 
ILE CD1 HD12 sing N N 264 
ILE CD1 HD13 sing N N 265 
ILE OXT HXT  sing N N 266 
LEU N   CA   sing N N 267 
LEU N   H    sing N N 268 
LEU N   H2   sing N N 269 
LEU CA  C    sing N N 270 
LEU CA  CB   sing N N 271 
LEU CA  HA   sing N N 272 
LEU C   O    doub N N 273 
LEU C   OXT  sing N N 274 
LEU CB  CG   sing N N 275 
LEU CB  HB2  sing N N 276 
LEU CB  HB3  sing N N 277 
LEU CG  CD1  sing N N 278 
LEU CG  CD2  sing N N 279 
LEU CG  HG   sing N N 280 
LEU CD1 HD11 sing N N 281 
LEU CD1 HD12 sing N N 282 
LEU CD1 HD13 sing N N 283 
LEU CD2 HD21 sing N N 284 
LEU CD2 HD22 sing N N 285 
LEU CD2 HD23 sing N N 286 
LEU OXT HXT  sing N N 287 
LYS N   CA   sing N N 288 
LYS N   H    sing N N 289 
LYS N   H2   sing N N 290 
LYS CA  C    sing N N 291 
LYS CA  CB   sing N N 292 
LYS CA  HA   sing N N 293 
LYS C   O    doub N N 294 
LYS C   OXT  sing N N 295 
LYS CB  CG   sing N N 296 
LYS CB  HB2  sing N N 297 
LYS CB  HB3  sing N N 298 
LYS CG  CD   sing N N 299 
LYS CG  HG2  sing N N 300 
LYS CG  HG3  sing N N 301 
LYS CD  CE   sing N N 302 
LYS CD  HD2  sing N N 303 
LYS CD  HD3  sing N N 304 
LYS CE  NZ   sing N N 305 
LYS CE  HE2  sing N N 306 
LYS CE  HE3  sing N N 307 
LYS NZ  HZ1  sing N N 308 
LYS NZ  HZ2  sing N N 309 
LYS NZ  HZ3  sing N N 310 
LYS OXT HXT  sing N N 311 
MET N   CA   sing N N 312 
MET N   H    sing N N 313 
MET N   H2   sing N N 314 
MET CA  C    sing N N 315 
MET CA  CB   sing N N 316 
MET CA  HA   sing N N 317 
MET C   O    doub N N 318 
MET C   OXT  sing N N 319 
MET CB  CG   sing N N 320 
MET CB  HB2  sing N N 321 
MET CB  HB3  sing N N 322 
MET CG  SD   sing N N 323 
MET CG  HG2  sing N N 324 
MET CG  HG3  sing N N 325 
MET SD  CE   sing N N 326 
MET CE  HE1  sing N N 327 
MET CE  HE2  sing N N 328 
MET CE  HE3  sing N N 329 
MET OXT HXT  sing N N 330 
PCA N   CA   sing N N 331 
PCA N   CD   sing N N 332 
PCA N   H    sing N N 333 
PCA CA  CB   sing N N 334 
PCA CA  C    sing N N 335 
PCA CA  HA   sing N N 336 
PCA CB  CG   sing N N 337 
PCA CB  HB2  sing N N 338 
PCA CB  HB3  sing N N 339 
PCA CG  CD   sing N N 340 
PCA CG  HG2  sing N N 341 
PCA CG  HG3  sing N N 342 
PCA CD  OE   doub N N 343 
PCA C   O    doub N N 344 
PCA C   OXT  sing N N 345 
PCA OXT HXT  sing N N 346 
PHE N   CA   sing N N 347 
PHE N   H    sing N N 348 
PHE N   H2   sing N N 349 
PHE CA  C    sing N N 350 
PHE CA  CB   sing N N 351 
PHE CA  HA   sing N N 352 
PHE C   O    doub N N 353 
PHE C   OXT  sing N N 354 
PHE CB  CG   sing N N 355 
PHE CB  HB2  sing N N 356 
PHE CB  HB3  sing N N 357 
PHE CG  CD1  doub Y N 358 
PHE CG  CD2  sing Y N 359 
PHE CD1 CE1  sing Y N 360 
PHE CD1 HD1  sing N N 361 
PHE CD2 CE2  doub Y N 362 
PHE CD2 HD2  sing N N 363 
PHE CE1 CZ   doub Y N 364 
PHE CE1 HE1  sing N N 365 
PHE CE2 CZ   sing Y N 366 
PHE CE2 HE2  sing N N 367 
PHE CZ  HZ   sing N N 368 
PHE OXT HXT  sing N N 369 
PRO N   CA   sing N N 370 
PRO N   CD   sing N N 371 
PRO N   H    sing N N 372 
PRO CA  C    sing N N 373 
PRO CA  CB   sing N N 374 
PRO CA  HA   sing N N 375 
PRO C   O    doub N N 376 
PRO C   OXT  sing N N 377 
PRO CB  CG   sing N N 378 
PRO CB  HB2  sing N N 379 
PRO CB  HB3  sing N N 380 
PRO CG  CD   sing N N 381 
PRO CG  HG2  sing N N 382 
PRO CG  HG3  sing N N 383 
PRO CD  HD2  sing N N 384 
PRO CD  HD3  sing N N 385 
PRO OXT HXT  sing N N 386 
SER N   CA   sing N N 387 
SER N   H    sing N N 388 
SER N   H2   sing N N 389 
SER CA  C    sing N N 390 
SER CA  CB   sing N N 391 
SER CA  HA   sing N N 392 
SER C   O    doub N N 393 
SER C   OXT  sing N N 394 
SER CB  OG   sing N N 395 
SER CB  HB2  sing N N 396 
SER CB  HB3  sing N N 397 
SER OG  HG   sing N N 398 
SER OXT HXT  sing N N 399 
THR N   CA   sing N N 400 
THR N   H    sing N N 401 
THR N   H2   sing N N 402 
THR CA  C    sing N N 403 
THR CA  CB   sing N N 404 
THR CA  HA   sing N N 405 
THR C   O    doub N N 406 
THR C   OXT  sing N N 407 
THR CB  OG1  sing N N 408 
THR CB  CG2  sing N N 409 
THR CB  HB   sing N N 410 
THR OG1 HG1  sing N N 411 
THR CG2 HG21 sing N N 412 
THR CG2 HG22 sing N N 413 
THR CG2 HG23 sing N N 414 
THR OXT HXT  sing N N 415 
TRP N   CA   sing N N 416 
TRP N   H    sing N N 417 
TRP N   H2   sing N N 418 
TRP CA  C    sing N N 419 
TRP CA  CB   sing N N 420 
TRP CA  HA   sing N N 421 
TRP C   O    doub N N 422 
TRP C   OXT  sing N N 423 
TRP CB  CG   sing N N 424 
TRP CB  HB2  sing N N 425 
TRP CB  HB3  sing N N 426 
TRP CG  CD1  doub Y N 427 
TRP CG  CD2  sing Y N 428 
TRP CD1 NE1  sing Y N 429 
TRP CD1 HD1  sing N N 430 
TRP CD2 CE2  doub Y N 431 
TRP CD2 CE3  sing Y N 432 
TRP NE1 CE2  sing Y N 433 
TRP NE1 HE1  sing N N 434 
TRP CE2 CZ2  sing Y N 435 
TRP CE3 CZ3  doub Y N 436 
TRP CE3 HE3  sing N N 437 
TRP CZ2 CH2  doub Y N 438 
TRP CZ2 HZ2  sing N N 439 
TRP CZ3 CH2  sing Y N 440 
TRP CZ3 HZ3  sing N N 441 
TRP CH2 HH2  sing N N 442 
TRP OXT HXT  sing N N 443 
TYR N   CA   sing N N 444 
TYR N   H    sing N N 445 
TYR N   H2   sing N N 446 
TYR CA  C    sing N N 447 
TYR CA  CB   sing N N 448 
TYR CA  HA   sing N N 449 
TYR C   O    doub N N 450 
TYR C   OXT  sing N N 451 
TYR CB  CG   sing N N 452 
TYR CB  HB2  sing N N 453 
TYR CB  HB3  sing N N 454 
TYR CG  CD1  doub Y N 455 
TYR CG  CD2  sing Y N 456 
TYR CD1 CE1  sing Y N 457 
TYR CD1 HD1  sing N N 458 
TYR CD2 CE2  doub Y N 459 
TYR CD2 HD2  sing N N 460 
TYR CE1 CZ   doub Y N 461 
TYR CE1 HE1  sing N N 462 
TYR CE2 CZ   sing Y N 463 
TYR CE2 HE2  sing N N 464 
TYR CZ  OH   sing N N 465 
TYR OH  HH   sing N N 466 
TYR OXT HXT  sing N N 467 
VAL N   CA   sing N N 468 
VAL N   H    sing N N 469 
VAL N   H2   sing N N 470 
VAL CA  C    sing N N 471 
VAL CA  CB   sing N N 472 
VAL CA  HA   sing N N 473 
VAL C   O    doub N N 474 
VAL C   OXT  sing N N 475 
VAL CB  CG1  sing N N 476 
VAL CB  CG2  sing N N 477 
VAL CB  HB   sing N N 478 
VAL CG1 HG11 sing N N 479 
VAL CG1 HG12 sing N N 480 
VAL CG1 HG13 sing N N 481 
VAL CG2 HG21 sing N N 482 
VAL CG2 HG22 sing N N 483 
VAL CG2 HG23 sing N N 484 
VAL OXT HXT  sing N N 485 
# 
loop_
_pdbx_entity_branch_list.entity_id 
_pdbx_entity_branch_list.comp_id 
_pdbx_entity_branch_list.num 
_pdbx_entity_branch_list.hetero 
2 BGC 1 n 
2 AC1 2 n 
2 GLC 3 n 
2 AC1 4 n 
# 
_atom_sites.entry_id                    1OSE 
_atom_sites.fract_transf_matrix[1][1]   0.014164 
_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]   0.008718 
_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]   0.008439 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
CA 
CL 
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 
HETATM 1    N  N   . PCA A 1 1   ? 41.002 44.319 25.144  1.00 25.94 ? 1    PCA A N   1 
HETATM 2    C  CA  . PCA A 1 1   ? 40.524 43.817 23.853  1.00 22.58 ? 1    PCA A CA  1 
HETATM 3    C  CB  . PCA A 1 1   ? 41.438 44.552 22.917  1.00 23.48 ? 1    PCA A CB  1 
HETATM 4    C  CG  . PCA A 1 1   ? 42.055 45.646 23.764  1.00 26.62 ? 1    PCA A CG  1 
HETATM 5    C  CD  . PCA A 1 1   ? 41.855 45.340 25.273  1.00 27.53 ? 1    PCA A CD  1 
HETATM 6    O  OE  . PCA A 1 1   ? 42.446 45.997 26.129  1.00 38.77 ? 1    PCA A OE  1 
HETATM 7    C  C   . PCA A 1 1   ? 40.691 42.298 23.828  1.00 19.43 ? 1    PCA A C   1 
HETATM 8    O  O   . PCA A 1 1   ? 40.068 41.626 23.010  1.00 20.05 ? 1    PCA A O   1 
ATOM   9    N  N   . TYR A 1 2   ? 41.551 41.767 24.697  1.00 16.14 ? 2    TYR A N   1 
ATOM   10   C  CA  . TYR A 1 2   ? 41.817 40.333 24.736  1.00 13.52 ? 2    TYR A CA  1 
ATOM   11   C  C   . TYR A 1 2   ? 40.852 39.547 25.605  1.00 14.70 ? 2    TYR A C   1 
ATOM   12   O  O   . TYR A 1 2   ? 40.657 38.356 25.387  1.00 17.71 ? 2    TYR A O   1 
ATOM   13   C  CB  . TYR A 1 2   ? 43.250 40.074 25.202  1.00 14.15 ? 2    TYR A CB  1 
ATOM   14   C  CG  . TYR A 1 2   ? 44.261 40.952 24.515  1.00 15.45 ? 2    TYR A CG  1 
ATOM   15   C  CD1 . TYR A 1 2   ? 44.593 40.759 23.178  1.00 15.89 ? 2    TYR A CD1 1 
ATOM   16   C  CD2 . TYR A 1 2   ? 44.850 42.018 25.192  1.00 18.88 ? 2    TYR A CD2 1 
ATOM   17   C  CE1 . TYR A 1 2   ? 45.488 41.614 22.530  1.00 18.95 ? 2    TYR A CE1 1 
ATOM   18   C  CE2 . TYR A 1 2   ? 45.743 42.876 24.557  1.00 16.33 ? 2    TYR A CE2 1 
ATOM   19   C  CZ  . TYR A 1 2   ? 46.057 42.671 23.232  1.00 17.74 ? 2    TYR A CZ  1 
ATOM   20   O  OH  . TYR A 1 2   ? 46.945 43.525 22.624  1.00 17.05 ? 2    TYR A OH  1 
ATOM   21   N  N   . ALA A 1 3   ? 40.289 40.193 26.619  1.00 13.16 ? 3    ALA A N   1 
ATOM   22   C  CA  . ALA A 1 3   ? 39.344 39.531 27.512  1.00 10.99 ? 3    ALA A CA  1 
ATOM   23   C  C   . ALA A 1 3   ? 38.001 39.436 26.811  1.00 15.10 ? 3    ALA A C   1 
ATOM   24   O  O   . ALA A 1 3   ? 37.468 40.444 26.351  1.00 17.24 ? 3    ALA A O   1 
ATOM   25   C  CB  . ALA A 1 3   ? 39.195 40.319 28.793  1.00 6.38  ? 3    ALA A CB  1 
ATOM   26   N  N   . PRO A 1 4   ? 37.430 38.224 26.726  1.00 15.84 ? 4    PRO A N   1 
ATOM   27   C  CA  . PRO A 1 4   ? 36.133 37.993 26.078  1.00 14.18 ? 4    PRO A CA  1 
ATOM   28   C  C   . PRO A 1 4   ? 34.948 38.694 26.737  1.00 15.38 ? 4    PRO A C   1 
ATOM   29   O  O   . PRO A 1 4   ? 33.901 38.854 26.114  1.00 11.97 ? 4    PRO A O   1 
ATOM   30   C  CB  . PRO A 1 4   ? 35.995 36.468 26.115  1.00 13.86 ? 4    PRO A CB  1 
ATOM   31   C  CG  . PRO A 1 4   ? 36.795 36.081 27.300  1.00 17.37 ? 4    PRO A CG  1 
ATOM   32   C  CD  . PRO A 1 4   ? 38.016 36.951 27.171  1.00 15.31 ? 4    PRO A CD  1 
ATOM   33   N  N   . GLN A 1 5   ? 35.115 39.103 27.995  1.00 14.74 ? 5    GLN A N   1 
ATOM   34   C  CA  . GLN A 1 5   ? 34.068 39.800 28.745  1.00 18.73 ? 5    GLN A CA  1 
ATOM   35   C  C   . GLN A 1 5   ? 32.822 38.952 28.988  1.00 19.69 ? 5    GLN A C   1 
ATOM   36   O  O   . GLN A 1 5   ? 31.730 39.493 29.173  1.00 18.70 ? 5    GLN A O   1 
ATOM   37   C  CB  . GLN A 1 5   ? 33.652 41.111 28.057  1.00 18.55 ? 5    GLN A CB  1 
ATOM   38   C  CG  . GLN A 1 5   ? 34.775 42.110 27.798  1.00 21.78 ? 5    GLN A CG  1 
ATOM   39   C  CD  . GLN A 1 5   ? 35.429 42.647 29.060  1.00 22.99 ? 5    GLN A CD  1 
ATOM   40   O  OE1 . GLN A 1 5   ? 36.512 43.221 28.997  1.00 27.84 ? 5    GLN A OE1 1 
ATOM   41   N  NE2 . GLN A 1 5   ? 34.776 42.484 30.202  1.00 27.22 ? 5    GLN A NE2 1 
ATOM   42   N  N   . THR A 1 6   ? 32.981 37.631 28.990  1.00 22.76 ? 6    THR A N   1 
ATOM   43   C  CA  . THR A 1 6   ? 31.860 36.726 29.234  1.00 20.39 ? 6    THR A CA  1 
ATOM   44   C  C   . THR A 1 6   ? 31.620 36.683 30.734  1.00 21.00 ? 6    THR A C   1 
ATOM   45   O  O   . THR A 1 6   ? 32.494 37.054 31.525  1.00 18.80 ? 6    THR A O   1 
ATOM   46   C  CB  . THR A 1 6   ? 32.164 35.276 28.772  1.00 19.23 ? 6    THR A CB  1 
ATOM   47   O  OG1 . THR A 1 6   ? 33.373 34.822 29.390  1.00 18.40 ? 6    THR A OG1 1 
ATOM   48   C  CG2 . THR A 1 6   ? 32.307 35.195 27.262  1.00 17.76 ? 6    THR A CG2 1 
ATOM   49   N  N   . GLN A 1 7   ? 30.435 36.242 31.127  1.00 22.63 ? 7    GLN A N   1 
ATOM   50   C  CA  . GLN A 1 7   ? 30.120 36.125 32.533  1.00 28.26 ? 7    GLN A CA  1 
ATOM   51   C  C   . GLN A 1 7   ? 31.079 35.086 33.097  1.00 30.56 ? 7    GLN A C   1 
ATOM   52   O  O   . GLN A 1 7   ? 31.413 34.109 32.424  1.00 32.80 ? 7    GLN A O   1 
ATOM   53   C  CB  . GLN A 1 7   ? 28.679 35.681 32.710  1.00 31.86 ? 7    GLN A CB  1 
ATOM   54   C  CG  . GLN A 1 7   ? 28.250 35.599 34.145  1.00 38.77 ? 7    GLN A CG  1 
ATOM   55   C  CD  . GLN A 1 7   ? 26.756 35.460 34.280  1.00 43.65 ? 7    GLN A CD  1 
ATOM   56   O  OE1 . GLN A 1 7   ? 26.230 34.351 34.409  1.00 46.92 ? 7    GLN A OE1 1 
ATOM   57   N  NE2 . GLN A 1 7   ? 26.055 36.587 34.242  1.00 45.30 ? 7    GLN A NE2 1 
ATOM   58   N  N   . SER A 1 8   ? 31.577 35.341 34.299  1.00 35.00 ? 8    SER A N   1 
ATOM   59   C  CA  . SER A 1 8   ? 32.528 34.452 34.960  1.00 35.23 ? 8    SER A CA  1 
ATOM   60   C  C   . SER A 1 8   ? 32.161 32.978 34.844  1.00 33.71 ? 8    SER A C   1 
ATOM   61   O  O   . SER A 1 8   ? 31.003 32.597 35.031  1.00 33.50 ? 8    SER A O   1 
ATOM   62   C  CB  . SER A 1 8   ? 32.654 34.829 36.436  1.00 38.93 ? 8    SER A CB  1 
ATOM   63   O  OG  . SER A 1 8   ? 33.680 34.084 37.072  1.00 45.45 ? 8    SER A OG  1 
ATOM   64   N  N   . GLY A 1 9   ? 33.158 32.161 34.512  1.00 30.22 ? 9    GLY A N   1 
ATOM   65   C  CA  . GLY A 1 9   ? 32.938 30.734 34.383  1.00 28.03 ? 9    GLY A CA  1 
ATOM   66   C  C   . GLY A 1 9   ? 32.508 30.259 33.004  1.00 29.52 ? 9    GLY A C   1 
ATOM   67   O  O   . GLY A 1 9   ? 32.416 29.054 32.783  1.00 35.10 ? 9    GLY A O   1 
ATOM   68   N  N   . ARG A 1 10  ? 32.250 31.179 32.078  1.00 22.06 ? 10   ARG A N   1 
ATOM   69   C  CA  . ARG A 1 10  ? 31.828 30.799 30.737  1.00 17.60 ? 10   ARG A CA  1 
ATOM   70   C  C   . ARG A 1 10  ? 32.997 30.974 29.782  1.00 16.14 ? 10   ARG A C   1 
ATOM   71   O  O   . ARG A 1 10  ? 33.554 32.063 29.656  1.00 22.33 ? 10   ARG A O   1 
ATOM   72   C  CB  . ARG A 1 10  ? 30.606 31.608 30.335  1.00 18.57 ? 10   ARG A CB  1 
ATOM   73   C  CG  . ARG A 1 10  ? 29.390 31.267 31.184  1.00 13.69 ? 10   ARG A CG  1 
ATOM   74   C  CD  . ARG A 1 10  ? 28.297 32.285 30.985  1.00 21.09 ? 10   ARG A CD  1 
ATOM   75   N  NE  . ARG A 1 10  ? 27.003 31.678 30.696  1.00 23.96 ? 10   ARG A NE  1 
ATOM   76   C  CZ  . ARG A 1 10  ? 26.084 31.403 31.613  1.00 25.16 ? 10   ARG A CZ  1 
ATOM   77   N  NH1 . ARG A 1 10  ? 26.305 31.673 32.891  1.00 31.18 ? 10   ARG A NH1 1 
ATOM   78   N  NH2 . ARG A 1 10  ? 24.940 30.860 31.250  1.00 26.05 ? 10   ARG A NH2 1 
ATOM   79   N  N   . THR A 1 11  ? 33.327 29.908 29.063  1.00 13.18 ? 11   THR A N   1 
ATOM   80   C  CA  . THR A 1 11  ? 34.501 29.895 28.201  1.00 7.27  ? 11   THR A CA  1 
ATOM   81   C  C   . THR A 1 11  ? 34.392 29.752 26.683  1.00 8.59  ? 11   THR A C   1 
ATOM   82   O  O   . THR A 1 11  ? 35.423 29.585 26.031  1.00 10.97 ? 11   THR A O   1 
ATOM   83   C  CB  . THR A 1 11  ? 35.474 28.797 28.697  1.00 8.16  ? 11   THR A CB  1 
ATOM   84   O  OG1 . THR A 1 11  ? 34.764 27.556 28.800  1.00 7.51  ? 11   THR A OG1 1 
ATOM   85   C  CG2 . THR A 1 11  ? 36.026 29.143 30.073  1.00 3.41  ? 11   THR A CG2 1 
ATOM   86   N  N   . SER A 1 12  ? 33.190 29.785 26.110  1.00 7.80  ? 12   SER A N   1 
ATOM   87   C  CA  . SER A 1 12  ? 33.061 29.655 24.658  1.00 9.08  ? 12   SER A CA  1 
ATOM   88   C  C   . SER A 1 12  ? 31.948 30.512 24.082  1.00 10.61 ? 12   SER A C   1 
ATOM   89   O  O   . SER A 1 12  ? 31.080 30.987 24.817  1.00 11.45 ? 12   SER A O   1 
ATOM   90   C  CB  . SER A 1 12  ? 32.790 28.200 24.271  1.00 10.48 ? 12   SER A CB  1 
ATOM   91   O  OG  . SER A 1 12  ? 33.800 27.341 24.765  1.00 15.99 ? 12   SER A OG  1 
ATOM   92   N  N   . ILE A 1 13  ? 32.001 30.733 22.771  1.00 8.18  ? 13   ILE A N   1 
ATOM   93   C  CA  . ILE A 1 13  ? 30.969 31.489 22.068  1.00 10.04 ? 13   ILE A CA  1 
ATOM   94   C  C   . ILE A 1 13  ? 30.484 30.630 20.898  1.00 7.82  ? 13   ILE A C   1 
ATOM   95   O  O   . ILE A 1 13  ? 31.198 29.740 20.442  1.00 6.75  ? 13   ILE A O   1 
ATOM   96   C  CB  . ILE A 1 13  ? 31.468 32.882 21.568  1.00 11.54 ? 13   ILE A CB  1 
ATOM   97   C  CG1 . ILE A 1 13  ? 32.542 32.735 20.502  1.00 12.63 ? 13   ILE A CG1 1 
ATOM   98   C  CG2 . ILE A 1 13  ? 32.022 33.706 22.733  1.00 11.97 ? 13   ILE A CG2 1 
ATOM   99   C  CD1 . ILE A 1 13  ? 33.085 34.066 20.023  1.00 16.57 ? 13   ILE A CD1 1 
ATOM   100  N  N   . VAL A 1 14  ? 29.254 30.853 20.454  1.00 7.74  ? 14   VAL A N   1 
ATOM   101  C  CA  . VAL A 1 14  ? 28.692 30.087 19.347  1.00 9.62  ? 14   VAL A CA  1 
ATOM   102  C  C   . VAL A 1 14  ? 28.432 31.011 18.177  1.00 9.71  ? 14   VAL A C   1 
ATOM   103  O  O   . VAL A 1 14  ? 27.939 32.123 18.359  1.00 10.97 ? 14   VAL A O   1 
ATOM   104  C  CB  . VAL A 1 14  ? 27.284 29.500 19.668  1.00 9.39  ? 14   VAL A CB  1 
ATOM   105  C  CG1 . VAL A 1 14  ? 27.091 28.184 18.947  1.00 10.84 ? 14   VAL A CG1 1 
ATOM   106  C  CG2 . VAL A 1 14  ? 27.047 29.383 21.144  1.00 15.19 ? 14   VAL A CG2 1 
ATOM   107  N  N   . HIS A 1 15  ? 28.717 30.548 16.971  1.00 7.71  ? 15   HIS A N   1 
ATOM   108  C  CA  . HIS A 1 15  ? 28.420 31.356 15.812  1.00 9.30  ? 15   HIS A CA  1 
ATOM   109  C  C   . HIS A 1 15  ? 27.051 30.894 15.308  1.00 8.56  ? 15   HIS A C   1 
ATOM   110  O  O   . HIS A 1 15  ? 26.944 29.864 14.647  1.00 9.99  ? 15   HIS A O   1 
ATOM   111  C  CB  . HIS A 1 15  ? 29.481 31.192 14.717  1.00 3.27  ? 15   HIS A CB  1 
ATOM   112  C  CG  . HIS A 1 15  ? 29.243 32.057 13.517  1.00 4.12  ? 15   HIS A CG  1 
ATOM   113  N  ND1 . HIS A 1 15  ? 28.316 33.080 13.512  1.00 6.52  ? 15   HIS A ND1 1 
ATOM   114  C  CD2 . HIS A 1 15  ? 29.781 32.034 12.274  1.00 3.55  ? 15   HIS A CD2 1 
ATOM   115  C  CE1 . HIS A 1 15  ? 28.286 33.642 12.316  1.00 3.90  ? 15   HIS A CE1 1 
ATOM   116  N  NE2 . HIS A 1 15  ? 29.167 33.027 11.548  1.00 6.48  ? 15   HIS A NE2 1 
ATOM   117  N  N   . LEU A 1 16  ? 25.997 31.606 15.690  1.00 10.97 ? 16   LEU A N   1 
ATOM   118  C  CA  . LEU A 1 16  ? 24.655 31.259 15.226  1.00 8.96  ? 16   LEU A CA  1 
ATOM   119  C  C   . LEU A 1 16  ? 24.520 31.895 13.846  1.00 8.45  ? 16   LEU A C   1 
ATOM   120  O  O   . LEU A 1 16  ? 23.905 32.945 13.666  1.00 10.60 ? 16   LEU A O   1 
ATOM   121  C  CB  . LEU A 1 16  ? 23.581 31.749 16.207  1.00 6.47  ? 16   LEU A CB  1 
ATOM   122  C  CG  . LEU A 1 16  ? 23.621 31.028 17.562  1.00 7.01  ? 16   LEU A CG  1 
ATOM   123  C  CD1 . LEU A 1 16  ? 22.455 31.435 18.442  1.00 7.20  ? 16   LEU A CD1 1 
ATOM   124  C  CD2 . LEU A 1 16  ? 23.597 29.527 17.335  1.00 5.46  ? 16   LEU A CD2 1 
ATOM   125  N  N   . PHE A 1 17  ? 25.158 31.241 12.886  1.00 7.50  ? 17   PHE A N   1 
ATOM   126  C  CA  . PHE A 1 17  ? 25.215 31.674 11.498  1.00 7.96  ? 17   PHE A CA  1 
ATOM   127  C  C   . PHE A 1 17  ? 23.856 31.916 10.848  1.00 10.25 ? 17   PHE A C   1 
ATOM   128  O  O   . PHE A 1 17  ? 23.028 31.013 10.766  1.00 14.69 ? 17   PHE A O   1 
ATOM   129  C  CB  . PHE A 1 17  ? 26.024 30.635 10.704  1.00 6.52  ? 17   PHE A CB  1 
ATOM   130  C  CG  . PHE A 1 17  ? 26.308 31.017 9.274   1.00 3.93  ? 17   PHE A CG  1 
ATOM   131  C  CD1 . PHE A 1 17  ? 26.762 32.289 8.948   1.00 2.25  ? 17   PHE A CD1 1 
ATOM   132  C  CD2 . PHE A 1 17  ? 26.146 30.079 8.254   1.00 3.49  ? 17   PHE A CD2 1 
ATOM   133  C  CE1 . PHE A 1 17  ? 27.056 32.624 7.626   1.00 4.49  ? 17   PHE A CE1 1 
ATOM   134  C  CE2 . PHE A 1 17  ? 26.435 30.402 6.933   1.00 5.16  ? 17   PHE A CE2 1 
ATOM   135  C  CZ  . PHE A 1 17  ? 26.890 31.676 6.615   1.00 2.37  ? 17   PHE A CZ  1 
ATOM   136  N  N   . GLU A 1 18  ? 23.628 33.154 10.416  1.00 12.71 ? 18   GLU A N   1 
ATOM   137  C  CA  . GLU A 1 18  ? 22.393 33.544 9.727   1.00 10.79 ? 18   GLU A CA  1 
ATOM   138  C  C   . GLU A 1 18  ? 21.084 33.452 10.515  1.00 10.67 ? 18   GLU A C   1 
ATOM   139  O  O   . GLU A 1 18  ? 20.006 33.573 9.928   1.00 11.33 ? 18   GLU A O   1 
ATOM   140  C  CB  . GLU A 1 18  ? 22.250 32.762 8.413   1.00 8.43  ? 18   GLU A CB  1 
ATOM   141  C  CG  . GLU A 1 18  ? 23.205 33.198 7.308   1.00 11.60 ? 18   GLU A CG  1 
ATOM   142  C  CD  . GLU A 1 18  ? 22.750 34.454 6.555   1.00 15.61 ? 18   GLU A CD  1 
ATOM   143  O  OE1 . GLU A 1 18  ? 21.715 35.054 6.918   1.00 16.03 ? 18   GLU A OE1 1 
ATOM   144  O  OE2 . GLU A 1 18  ? 23.429 34.836 5.578   1.00 14.82 ? 18   GLU A OE2 1 
ATOM   145  N  N   . TRP A 1 19  ? 21.164 33.255 11.829  1.00 7.20  ? 19   TRP A N   1 
ATOM   146  C  CA  . TRP A 1 19  ? 19.954 33.167 12.644  1.00 8.40  ? 19   TRP A CA  1 
ATOM   147  C  C   . TRP A 1 19  ? 19.242 34.515 12.721  1.00 9.37  ? 19   TRP A C   1 
ATOM   148  O  O   . TRP A 1 19  ? 19.864 35.563 12.554  1.00 12.65 ? 19   TRP A O   1 
ATOM   149  C  CB  . TRP A 1 19  ? 20.283 32.702 14.062  1.00 7.61  ? 19   TRP A CB  1 
ATOM   150  C  CG  . TRP A 1 19  ? 20.521 31.232 14.208  1.00 7.42  ? 19   TRP A CG  1 
ATOM   151  C  CD1 . TRP A 1 19  ? 21.248 30.432 13.380  1.00 7.94  ? 19   TRP A CD1 1 
ATOM   152  C  CD2 . TRP A 1 19  ? 20.062 30.394 15.275  1.00 8.59  ? 19   TRP A CD2 1 
ATOM   153  N  NE1 . TRP A 1 19  ? 21.277 29.147 13.865  1.00 7.61  ? 19   TRP A NE1 1 
ATOM   154  C  CE2 . TRP A 1 19  ? 20.556 29.094 15.029  1.00 8.37  ? 19   TRP A CE2 1 
ATOM   155  C  CE3 . TRP A 1 19  ? 19.280 30.615 16.417  1.00 8.66  ? 19   TRP A CE3 1 
ATOM   156  C  CZ2 . TRP A 1 19  ? 20.297 28.016 15.882  1.00 9.10  ? 19   TRP A CZ2 1 
ATOM   157  C  CZ3 . TRP A 1 19  ? 19.019 29.546 17.267  1.00 10.23 ? 19   TRP A CZ3 1 
ATOM   158  C  CH2 . TRP A 1 19  ? 19.529 28.259 16.993  1.00 9.03  ? 19   TRP A CH2 1 
ATOM   159  N  N   . ARG A 1 20  ? 17.936 34.479 12.963  1.00 11.72 ? 20   ARG A N   1 
ATOM   160  C  CA  . ARG A 1 20  ? 17.138 35.692 13.092  1.00 10.01 ? 20   ARG A CA  1 
ATOM   161  C  C   . ARG A 1 20  ? 17.283 36.147 14.528  1.00 10.88 ? 20   ARG A C   1 
ATOM   162  O  O   . ARG A 1 20  ? 17.436 35.317 15.422  1.00 13.71 ? 20   ARG A O   1 
ATOM   163  C  CB  . ARG A 1 20  ? 15.673 35.400 12.794  1.00 10.60 ? 20   ARG A CB  1 
ATOM   164  C  CG  . ARG A 1 20  ? 15.415 34.950 11.377  1.00 16.74 ? 20   ARG A CG  1 
ATOM   165  C  CD  . ARG A 1 20  ? 14.133 34.145 11.288  1.00 23.89 ? 20   ARG A CD  1 
ATOM   166  N  NE  . ARG A 1 20  ? 12.944 34.927 11.613  1.00 28.72 ? 20   ARG A NE  1 
ATOM   167  C  CZ  . ARG A 1 20  ? 12.041 34.581 12.527  1.00 31.74 ? 20   ARG A CZ  1 
ATOM   168  N  NH1 . ARG A 1 20  ? 12.196 33.480 13.247  1.00 31.30 ? 20   ARG A NH1 1 
ATOM   169  N  NH2 . ARG A 1 20  ? 10.989 35.358 12.743  1.00 37.64 ? 20   ARG A NH2 1 
ATOM   170  N  N   . TRP A 1 21  ? 17.210 37.456 14.755  1.00 14.48 ? 21   TRP A N   1 
ATOM   171  C  CA  . TRP A 1 21  ? 17.357 38.010 16.098  1.00 13.40 ? 21   TRP A CA  1 
ATOM   172  C  C   . TRP A 1 21  ? 16.375 37.405 17.094  1.00 12.67 ? 21   TRP A C   1 
ATOM   173  O  O   . TRP A 1 21  ? 16.756 37.087 18.218  1.00 16.23 ? 21   TRP A O   1 
ATOM   174  C  CB  . TRP A 1 21  ? 17.213 39.533 16.091  1.00 12.62 ? 21   TRP A CB  1 
ATOM   175  C  CG  . TRP A 1 21  ? 18.097 40.283 15.116  1.00 9.83  ? 21   TRP A CG  1 
ATOM   176  C  CD1 . TRP A 1 21  ? 17.790 41.454 14.490  1.00 10.23 ? 21   TRP A CD1 1 
ATOM   177  C  CD2 . TRP A 1 21  ? 19.411 39.920 14.658  1.00 10.31 ? 21   TRP A CD2 1 
ATOM   178  N  NE1 . TRP A 1 21  ? 18.818 41.843 13.673  1.00 11.85 ? 21   TRP A NE1 1 
ATOM   179  C  CE2 . TRP A 1 21  ? 19.829 40.922 13.754  1.00 10.38 ? 21   TRP A CE2 1 
ATOM   180  C  CE3 . TRP A 1 21  ? 20.276 38.848 14.918  1.00 11.32 ? 21   TRP A CE3 1 
ATOM   181  C  CZ2 . TRP A 1 21  ? 21.070 40.887 13.108  1.00 8.57  ? 21   TRP A CZ2 1 
ATOM   182  C  CZ3 . TRP A 1 21  ? 21.516 38.815 14.269  1.00 10.37 ? 21   TRP A CZ3 1 
ATOM   183  C  CH2 . TRP A 1 21  ? 21.895 39.829 13.376  1.00 9.77  ? 21   TRP A CH2 1 
ATOM   184  N  N   . VAL A 1 22  ? 15.114 37.252 16.702  1.00 15.15 ? 22   VAL A N   1 
ATOM   185  C  CA  . VAL A 1 22  ? 14.120 36.668 17.610  1.00 16.88 ? 22   VAL A CA  1 
ATOM   186  C  C   . VAL A 1 22  ? 14.485 35.252 18.055  1.00 15.18 ? 22   VAL A C   1 
ATOM   187  O  O   . VAL A 1 22  ? 14.395 34.934 19.243  1.00 19.75 ? 22   VAL A O   1 
ATOM   188  C  CB  . VAL A 1 22  ? 12.691 36.668 17.014  1.00 18.20 ? 22   VAL A CB  1 
ATOM   189  C  CG1 . VAL A 1 22  ? 12.173 38.093 16.905  1.00 22.06 ? 22   VAL A CG1 1 
ATOM   190  C  CG2 . VAL A 1 22  ? 12.674 35.989 15.653  1.00 17.73 ? 22   VAL A CG2 1 
ATOM   191  N  N   . ASP A 1 23  ? 14.942 34.423 17.119  1.00 11.09 ? 23   ASP A N   1 
ATOM   192  C  CA  . ASP A 1 23  ? 15.324 33.053 17.444  1.00 11.40 ? 23   ASP A CA  1 
ATOM   193  C  C   . ASP A 1 23  ? 16.522 33.001 18.387  1.00 11.57 ? 23   ASP A C   1 
ATOM   194  O  O   . ASP A 1 23  ? 16.573 32.161 19.280  1.00 14.18 ? 23   ASP A O   1 
ATOM   195  C  CB  . ASP A 1 23  ? 15.590 32.249 16.171  1.00 12.89 ? 23   ASP A CB  1 
ATOM   196  C  CG  . ASP A 1 23  ? 14.316 31.964 15.387  1.00 13.96 ? 23   ASP A CG  1 
ATOM   197  O  OD1 . ASP A 1 23  ? 13.259 31.748 16.014  1.00 15.23 ? 23   ASP A OD1 1 
ATOM   198  O  OD2 . ASP A 1 23  ? 14.366 31.956 14.144  1.00 15.03 ? 23   ASP A OD2 1 
ATOM   199  N  N   . ILE A 1 24  ? 17.477 33.908 18.201  1.00 10.17 ? 24   ILE A N   1 
ATOM   200  C  CA  . ILE A 1 24  ? 18.645 33.969 19.070  1.00 6.50  ? 24   ILE A CA  1 
ATOM   201  C  C   . ILE A 1 24  ? 18.206 34.357 20.475  1.00 8.75  ? 24   ILE A C   1 
ATOM   202  O  O   . ILE A 1 24  ? 18.658 33.764 21.448  1.00 13.69 ? 24   ILE A O   1 
ATOM   203  C  CB  . ILE A 1 24  ? 19.677 34.992 18.565  1.00 5.86  ? 24   ILE A CB  1 
ATOM   204  C  CG1 . ILE A 1 24  ? 20.278 34.525 17.237  1.00 5.70  ? 24   ILE A CG1 1 
ATOM   205  C  CG2 . ILE A 1 24  ? 20.773 35.191 19.595  1.00 6.30  ? 24   ILE A CG2 1 
ATOM   206  C  CD1 . ILE A 1 24  ? 21.339 35.456 16.694  1.00 2.66  ? 24   ILE A CD1 1 
ATOM   207  N  N   . ALA A 1 25  ? 17.306 35.335 20.574  1.00 11.00 ? 25   ALA A N   1 
ATOM   208  C  CA  . ALA A 1 25  ? 16.800 35.808 21.869  1.00 10.53 ? 25   ALA A CA  1 
ATOM   209  C  C   . ALA A 1 25  ? 16.193 34.653 22.650  1.00 11.44 ? 25   ALA A C   1 
ATOM   210  O  O   . ALA A 1 25  ? 16.444 34.493 23.848  1.00 13.64 ? 25   ALA A O   1 
ATOM   211  C  CB  . ALA A 1 25  ? 15.765 36.906 21.665  1.00 10.68 ? 25   ALA A CB  1 
ATOM   212  N  N   . LEU A 1 26  ? 15.379 33.862 21.961  1.00 11.72 ? 26   LEU A N   1 
ATOM   213  C  CA  . LEU A 1 26  ? 14.741 32.694 22.551  1.00 10.85 ? 26   LEU A CA  1 
ATOM   214  C  C   . LEU A 1 26  ? 15.801 31.677 22.960  1.00 14.71 ? 26   LEU A C   1 
ATOM   215  O  O   . LEU A 1 26  ? 15.800 31.184 24.094  1.00 15.04 ? 26   LEU A O   1 
ATOM   216  C  CB  . LEU A 1 26  ? 13.793 32.050 21.535  1.00 10.81 ? 26   LEU A CB  1 
ATOM   217  C  CG  . LEU A 1 26  ? 12.495 32.808 21.261  1.00 13.05 ? 26   LEU A CG  1 
ATOM   218  C  CD1 . LEU A 1 26  ? 11.783 32.233 20.053  1.00 14.59 ? 26   LEU A CD1 1 
ATOM   219  C  CD2 . LEU A 1 26  ? 11.613 32.733 22.490  1.00 12.57 ? 26   LEU A CD2 1 
ATOM   220  N  N   . GLU A 1 27  ? 16.716 31.387 22.035  1.00 12.29 ? 27   GLU A N   1 
ATOM   221  C  CA  . GLU A 1 27  ? 17.787 30.430 22.269  1.00 9.56  ? 27   GLU A CA  1 
ATOM   222  C  C   . GLU A 1 27  ? 18.610 30.787 23.499  1.00 12.73 ? 27   GLU A C   1 
ATOM   223  O  O   . GLU A 1 27  ? 19.046 29.896 24.227  1.00 17.45 ? 27   GLU A O   1 
ATOM   224  C  CB  . GLU A 1 27  ? 18.680 30.323 21.034  1.00 13.58 ? 27   GLU A CB  1 
ATOM   225  C  CG  . GLU A 1 27  ? 19.656 29.140 21.043  1.00 15.68 ? 27   GLU A CG  1 
ATOM   226  C  CD  . GLU A 1 27  ? 18.979 27.775 20.924  1.00 19.06 ? 27   GLU A CD  1 
ATOM   227  O  OE1 . GLU A 1 27  ? 17.746 27.674 21.072  1.00 20.83 ? 27   GLU A OE1 1 
ATOM   228  O  OE2 . GLU A 1 27  ? 19.690 26.787 20.679  1.00 18.30 ? 27   GLU A OE2 1 
ATOM   229  N  N   . CYS A 1 28  ? 18.808 32.083 23.742  1.00 13.99 ? 28   CYS A N   1 
ATOM   230  C  CA  . CYS A 1 28  ? 19.566 32.554 24.905  1.00 12.39 ? 28   CYS A CA  1 
ATOM   231  C  C   . CYS A 1 28  ? 18.889 32.157 26.212  1.00 13.39 ? 28   CYS A C   1 
ATOM   232  O  O   . CYS A 1 28  ? 19.532 31.652 27.134  1.00 12.76 ? 28   CYS A O   1 
ATOM   233  C  CB  . CYS A 1 28  ? 19.708 34.082 24.883  1.00 12.85 ? 28   CYS A CB  1 
ATOM   234  S  SG  . CYS A 1 28  ? 21.049 34.711 23.825  1.00 16.91 ? 28   CYS A SG  1 
ATOM   235  N  N   . GLU A 1 29  ? 17.577 32.346 26.258  1.00 12.02 ? 29   GLU A N   1 
ATOM   236  C  CA  . GLU A 1 29  ? 16.789 32.057 27.445  1.00 15.76 ? 29   GLU A CA  1 
ATOM   237  C  C   . GLU A 1 29  ? 16.500 30.578 27.704  1.00 19.32 ? 29   GLU A C   1 
ATOM   238  O  O   . GLU A 1 29  ? 16.543 30.127 28.852  1.00 18.93 ? 29   GLU A O   1 
ATOM   239  C  CB  . GLU A 1 29  ? 15.484 32.842 27.368  1.00 16.19 ? 29   GLU A CB  1 
ATOM   240  C  CG  . GLU A 1 29  ? 15.713 34.336 27.136  1.00 18.14 ? 29   GLU A CG  1 
ATOM   241  C  CD  . GLU A 1 29  ? 14.441 35.102 26.852  1.00 17.60 ? 29   GLU A CD  1 
ATOM   242  O  OE1 . GLU A 1 29  ? 13.495 34.515 26.283  1.00 19.11 ? 29   GLU A OE1 1 
ATOM   243  O  OE2 . GLU A 1 29  ? 14.395 36.300 27.192  1.00 18.28 ? 29   GLU A OE2 1 
ATOM   244  N  N   . ARG A 1 30  ? 16.216 29.829 26.641  1.00 15.87 ? 30   ARG A N   1 
ATOM   245  C  CA  . ARG A 1 30  ? 15.895 28.414 26.767  1.00 15.83 ? 30   ARG A CA  1 
ATOM   246  C  C   . ARG A 1 30  ? 17.076 27.455 26.755  1.00 18.48 ? 30   ARG A C   1 
ATOM   247  O  O   . ARG A 1 30  ? 16.978 26.359 27.305  1.00 23.72 ? 30   ARG A O   1 
ATOM   248  C  CB  . ARG A 1 30  ? 14.912 27.994 25.668  1.00 11.70 ? 30   ARG A CB  1 
ATOM   249  C  CG  . ARG A 1 30  ? 15.514 27.986 24.284  1.00 12.36 ? 30   ARG A CG  1 
ATOM   250  C  CD  . ARG A 1 30  ? 14.467 27.782 23.201  1.00 9.72  ? 30   ARG A CD  1 
ATOM   251  N  NE  . ARG A 1 30  ? 15.054 27.997 21.879  1.00 13.20 ? 30   ARG A NE  1 
ATOM   252  C  CZ  . ARG A 1 30  ? 14.370 28.298 20.778  1.00 12.62 ? 30   ARG A CZ  1 
ATOM   253  N  NH1 . ARG A 1 30  ? 13.055 28.444 20.822  1.00 17.54 ? 30   ARG A NH1 1 
ATOM   254  N  NH2 . ARG A 1 30  ? 15.005 28.471 19.628  1.00 11.60 ? 30   ARG A NH2 1 
ATOM   255  N  N   . TYR A 1 31  ? 18.197 27.858 26.165  1.00 18.84 ? 31   TYR A N   1 
ATOM   256  C  CA  . TYR A 1 31  ? 19.333 26.949 26.072  1.00 14.53 ? 31   TYR A CA  1 
ATOM   257  C  C   . TYR A 1 31  ? 20.722 27.508 26.406  1.00 15.52 ? 31   TYR A C   1 
ATOM   258  O  O   . TYR A 1 31  ? 21.383 27.017 27.323  1.00 18.58 ? 31   TYR A O   1 
ATOM   259  C  CB  . TYR A 1 31  ? 19.336 26.316 24.674  1.00 11.52 ? 31   TYR A CB  1 
ATOM   260  C  CG  . TYR A 1 31  ? 20.363 25.235 24.468  1.00 14.33 ? 31   TYR A CG  1 
ATOM   261  C  CD1 . TYR A 1 31  ? 20.092 23.913 24.811  1.00 14.88 ? 31   TYR A CD1 1 
ATOM   262  C  CD2 . TYR A 1 31  ? 21.614 25.534 23.939  1.00 14.01 ? 31   TYR A CD2 1 
ATOM   263  C  CE1 . TYR A 1 31  ? 21.047 22.919 24.634  1.00 16.48 ? 31   TYR A CE1 1 
ATOM   264  C  CE2 . TYR A 1 31  ? 22.572 24.550 23.760  1.00 15.04 ? 31   TYR A CE2 1 
ATOM   265  C  CZ  . TYR A 1 31  ? 22.284 23.248 24.110  1.00 17.25 ? 31   TYR A CZ  1 
ATOM   266  O  OH  . TYR A 1 31  ? 23.239 22.281 23.943  1.00 21.98 ? 31   TYR A OH  1 
ATOM   267  N  N   . LEU A 1 32  ? 21.170 28.518 25.666  1.00 14.30 ? 32   LEU A N   1 
ATOM   268  C  CA  . LEU A 1 32  ? 22.503 29.089 25.876  1.00 11.07 ? 32   LEU A CA  1 
ATOM   269  C  C   . LEU A 1 32  ? 22.776 29.490 27.316  1.00 12.54 ? 32   LEU A C   1 
ATOM   270  O  O   . LEU A 1 32  ? 23.833 29.174 27.866  1.00 11.54 ? 32   LEU A O   1 
ATOM   271  C  CB  . LEU A 1 32  ? 22.725 30.279 24.943  1.00 10.59 ? 32   LEU A CB  1 
ATOM   272  C  CG  . LEU A 1 32  ? 22.575 29.945 23.455  1.00 13.67 ? 32   LEU A CG  1 
ATOM   273  C  CD1 . LEU A 1 32  ? 22.609 31.205 22.620  1.00 10.05 ? 32   LEU A CD1 1 
ATOM   274  C  CD2 . LEU A 1 32  ? 23.663 28.979 23.016  1.00 12.51 ? 32   LEU A CD2 1 
ATOM   275  N  N   . GLY A 1 33  ? 21.822 30.186 27.923  1.00 15.42 ? 33   GLY A N   1 
ATOM   276  C  CA  . GLY A 1 33  ? 21.985 30.614 29.299  1.00 11.34 ? 33   GLY A CA  1 
ATOM   277  C  C   . GLY A 1 33  ? 22.108 29.424 30.224  1.00 12.32 ? 33   GLY A C   1 
ATOM   278  O  O   . GLY A 1 33  ? 23.144 29.228 30.848  1.00 11.15 ? 33   GLY A O   1 
ATOM   279  N  N   . PRO A 1 34  ? 21.072 28.585 30.311  1.00 13.72 ? 34   PRO A N   1 
ATOM   280  C  CA  . PRO A 1 34  ? 21.126 27.414 31.186  1.00 12.99 ? 34   PRO A CA  1 
ATOM   281  C  C   . PRO A 1 34  ? 22.311 26.473 30.923  1.00 16.30 ? 34   PRO A C   1 
ATOM   282  O  O   . PRO A 1 34  ? 22.838 25.879 31.861  1.00 19.97 ? 34   PRO A O   1 
ATOM   283  C  CB  . PRO A 1 34  ? 19.795 26.732 30.907  1.00 14.00 ? 34   PRO A CB  1 
ATOM   284  C  CG  . PRO A 1 34  ? 18.890 27.889 30.626  1.00 14.03 ? 34   PRO A CG  1 
ATOM   285  C  CD  . PRO A 1 34  ? 19.731 28.735 29.720  1.00 13.89 ? 34   PRO A CD  1 
ATOM   286  N  N   . LYS A 1 35  ? 22.747 26.353 29.670  1.00 16.01 ? 35   LYS A N   1 
ATOM   287  C  CA  . LYS A 1 35  ? 23.855 25.460 29.342  1.00 16.15 ? 35   LYS A CA  1 
ATOM   288  C  C   . LYS A 1 35  ? 25.263 26.032 29.404  1.00 16.72 ? 35   LYS A C   1 
ATOM   289  O  O   . LYS A 1 35  ? 26.194 25.456 28.835  1.00 22.71 ? 35   LYS A O   1 
ATOM   290  C  CB  . LYS A 1 35  ? 23.624 24.752 28.006  1.00 20.13 ? 35   LYS A CB  1 
ATOM   291  C  CG  . LYS A 1 35  ? 22.799 23.475 28.121  1.00 23.01 ? 35   LYS A CG  1 
ATOM   292  C  CD  . LYS A 1 35  ? 21.400 23.765 28.622  1.00 29.45 ? 35   LYS A CD  1 
ATOM   293  C  CE  . LYS A 1 35  ? 20.528 22.513 28.638  1.00 34.04 ? 35   LYS A CE  1 
ATOM   294  N  NZ  . LYS A 1 35  ? 21.021 21.475 29.585  1.00 39.44 ? 35   LYS A NZ  1 
ATOM   295  N  N   . GLY A 1 36  ? 25.421 27.163 30.078  1.00 14.11 ? 36   GLY A N   1 
ATOM   296  C  CA  . GLY A 1 36  ? 26.737 27.755 30.247  1.00 12.35 ? 36   GLY A CA  1 
ATOM   297  C  C   . GLY A 1 36  ? 27.503 28.268 29.041  1.00 13.44 ? 36   GLY A C   1 
ATOM   298  O  O   . GLY A 1 36  ? 28.735 28.320 29.077  1.00 12.85 ? 36   GLY A O   1 
ATOM   299  N  N   . PHE A 1 37  ? 26.807 28.644 27.974  1.00 12.11 ? 37   PHE A N   1 
ATOM   300  C  CA  . PHE A 1 37  ? 27.494 29.180 26.809  1.00 11.01 ? 37   PHE A CA  1 
ATOM   301  C  C   . PHE A 1 37  ? 27.897 30.622 27.099  1.00 13.38 ? 37   PHE A C   1 
ATOM   302  O  O   . PHE A 1 37  ? 27.126 31.386 27.675  1.00 11.88 ? 37   PHE A O   1 
ATOM   303  C  CB  . PHE A 1 37  ? 26.609 29.102 25.575  1.00 11.53 ? 37   PHE A CB  1 
ATOM   304  C  CG  . PHE A 1 37  ? 26.621 27.757 24.909  1.00 12.42 ? 37   PHE A CG  1 
ATOM   305  C  CD1 . PHE A 1 37  ? 25.805 26.726 25.371  1.00 12.74 ? 37   PHE A CD1 1 
ATOM   306  C  CD2 . PHE A 1 37  ? 27.438 27.523 23.807  1.00 14.43 ? 37   PHE A CD2 1 
ATOM   307  C  CE1 . PHE A 1 37  ? 25.798 25.480 24.743  1.00 11.89 ? 37   PHE A CE1 1 
ATOM   308  C  CE2 . PHE A 1 37  ? 27.442 26.278 23.166  1.00 15.92 ? 37   PHE A CE2 1 
ATOM   309  C  CZ  . PHE A 1 37  ? 26.619 25.255 23.636  1.00 15.36 ? 37   PHE A CZ  1 
ATOM   310  N  N   . GLY A 1 38  ? 29.121 30.976 26.728  1.00 14.36 ? 38   GLY A N   1 
ATOM   311  C  CA  . GLY A 1 38  ? 29.620 32.317 26.977  1.00 12.10 ? 38   GLY A CA  1 
ATOM   312  C  C   . GLY A 1 38  ? 28.995 33.441 26.174  1.00 15.58 ? 38   GLY A C   1 
ATOM   313  O  O   . GLY A 1 38  ? 28.793 34.532 26.704  1.00 15.92 ? 38   GLY A O   1 
ATOM   314  N  N   . GLY A 1 39  ? 28.713 33.201 24.897  1.00 12.77 ? 39   GLY A N   1 
ATOM   315  C  CA  . GLY A 1 39  ? 28.117 34.235 24.074  1.00 11.39 ? 39   GLY A CA  1 
ATOM   316  C  C   . GLY A 1 39  ? 27.799 33.778 22.665  1.00 12.01 ? 39   GLY A C   1 
ATOM   317  O  O   . GLY A 1 39  ? 28.023 32.619 22.317  1.00 12.83 ? 39   GLY A O   1 
ATOM   318  N  N   . VAL A 1 40  ? 27.324 34.701 21.837  1.00 10.35 ? 40   VAL A N   1 
ATOM   319  C  CA  . VAL A 1 40  ? 26.956 34.390 20.466  1.00 8.26  ? 40   VAL A CA  1 
ATOM   320  C  C   . VAL A 1 40  ? 27.531 35.400 19.486  1.00 12.54 ? 40   VAL A C   1 
ATOM   321  O  O   . VAL A 1 40  ? 27.548 36.601 19.759  1.00 15.81 ? 40   VAL A O   1 
ATOM   322  C  CB  . VAL A 1 40  ? 25.413 34.391 20.305  1.00 6.70  ? 40   VAL A CB  1 
ATOM   323  C  CG1 . VAL A 1 40  ? 25.006 34.138 18.859  1.00 5.47  ? 40   VAL A CG1 1 
ATOM   324  C  CG2 . VAL A 1 40  ? 24.790 33.344 21.203  1.00 7.63  ? 40   VAL A CG2 1 
ATOM   325  N  N   . GLN A 1 41  ? 28.082 34.897 18.386  1.00 9.02  ? 41   GLN A N   1 
ATOM   326  C  CA  . GLN A 1 41  ? 28.598 35.745 17.324  1.00 5.54  ? 41   GLN A CA  1 
ATOM   327  C  C   . GLN A 1 41  ? 27.452 35.774 16.315  1.00 8.27  ? 41   GLN A C   1 
ATOM   328  O  O   . GLN A 1 41  ? 27.011 34.726 15.837  1.00 12.31 ? 41   GLN A O   1 
ATOM   329  C  CB  . GLN A 1 41  ? 29.837 35.129 16.672  1.00 4.49  ? 41   GLN A CB  1 
ATOM   330  C  CG  . GLN A 1 41  ? 30.257 35.854 15.395  1.00 4.82  ? 41   GLN A CG  1 
ATOM   331  C  CD  . GLN A 1 41  ? 31.448 35.219 14.698  1.00 6.70  ? 41   GLN A CD  1 
ATOM   332  O  OE1 . GLN A 1 41  ? 32.396 34.778 15.337  1.00 8.49  ? 41   GLN A OE1 1 
ATOM   333  N  NE2 . GLN A 1 41  ? 31.405 35.185 13.375  1.00 6.16  ? 41   GLN A NE2 1 
ATOM   334  N  N   . VAL A 1 42  ? 26.947 36.962 16.018  1.00 10.82 ? 42   VAL A N   1 
ATOM   335  C  CA  . VAL A 1 42  ? 25.844 37.106 15.083  1.00 6.12  ? 42   VAL A CA  1 
ATOM   336  C  C   . VAL A 1 42  ? 26.329 37.503 13.695  1.00 10.34 ? 42   VAL A C   1 
ATOM   337  O  O   . VAL A 1 42  ? 27.480 37.910 13.516  1.00 13.16 ? 42   VAL A O   1 
ATOM   338  C  CB  . VAL A 1 42  ? 24.815 38.163 15.587  1.00 7.47  ? 42   VAL A CB  1 
ATOM   339  C  CG1 . VAL A 1 42  ? 24.234 37.744 16.928  1.00 2.00  ? 42   VAL A CG1 1 
ATOM   340  C  CG2 . VAL A 1 42  ? 25.472 39.542 15.699  1.00 6.01  ? 42   VAL A CG2 1 
ATOM   341  N  N   . SER A 1 43  ? 25.459 37.341 12.708  1.00 6.78  ? 43   SER A N   1 
ATOM   342  C  CA  . SER A 1 43  ? 25.773 37.714 11.344  1.00 8.54  ? 43   SER A CA  1 
ATOM   343  C  C   . SER A 1 43  ? 25.721 39.248 11.249  1.00 9.65  ? 43   SER A C   1 
ATOM   344  O  O   . SER A 1 43  ? 25.163 39.907 12.136  1.00 10.12 ? 43   SER A O   1 
ATOM   345  C  CB  . SER A 1 43  ? 24.766 37.065 10.395  1.00 10.84 ? 43   SER A CB  1 
ATOM   346  O  OG  . SER A 1 43  ? 25.042 35.680 10.246  1.00 10.38 ? 43   SER A OG  1 
ATOM   347  N  N   . PRO A 1 44  ? 26.328 39.836 10.198  1.00 8.09  ? 44   PRO A N   1 
ATOM   348  C  CA  . PRO A 1 44  ? 26.315 41.299 10.057  1.00 7.45  ? 44   PRO A CA  1 
ATOM   349  C  C   . PRO A 1 44  ? 24.905 41.850 10.233  1.00 7.21  ? 44   PRO A C   1 
ATOM   350  O  O   . PRO A 1 44  ? 23.997 41.508 9.475   1.00 10.70 ? 44   PRO A O   1 
ATOM   351  C  CB  . PRO A 1 44  ? 26.835 41.506 8.636   1.00 5.48  ? 44   PRO A CB  1 
ATOM   352  C  CG  . PRO A 1 44  ? 27.811 40.395 8.481   1.00 2.92  ? 44   PRO A CG  1 
ATOM   353  C  CD  . PRO A 1 44  ? 27.041 39.215 9.067   1.00 4.58  ? 44   PRO A CD  1 
ATOM   354  N  N   . PRO A 1 45  ? 24.706 42.696 11.257  1.00 6.27  ? 45   PRO A N   1 
ATOM   355  C  CA  . PRO A 1 45  ? 23.415 43.310 11.572  1.00 9.70  ? 45   PRO A CA  1 
ATOM   356  C  C   . PRO A 1 45  ? 23.070 44.578 10.782  1.00 13.59 ? 45   PRO A C   1 
ATOM   357  O  O   . PRO A 1 45  ? 21.972 45.121 10.934  1.00 18.81 ? 45   PRO A O   1 
ATOM   358  C  CB  . PRO A 1 45  ? 23.552 43.605 13.066  1.00 7.17  ? 45   PRO A CB  1 
ATOM   359  C  CG  . PRO A 1 45  ? 24.976 44.028 13.167  1.00 4.37  ? 45   PRO A CG  1 
ATOM   360  C  CD  . PRO A 1 45  ? 25.704 43.015 12.301  1.00 3.40  ? 45   PRO A CD  1 
ATOM   361  N  N   . ASN A 1 46  ? 24.001 45.054 9.957   1.00 15.19 ? 46   ASN A N   1 
ATOM   362  C  CA  . ASN A 1 46  ? 23.787 46.261 9.160   1.00 13.16 ? 46   ASN A CA  1 
ATOM   363  C  C   . ASN A 1 46  ? 23.249 45.932 7.771   1.00 18.46 ? 46   ASN A C   1 
ATOM   364  O  O   . ASN A 1 46  ? 23.439 44.827 7.263   1.00 19.35 ? 46   ASN A O   1 
ATOM   365  C  CB  . ASN A 1 46  ? 25.085 47.053 9.027   1.00 12.21 ? 46   ASN A CB  1 
ATOM   366  C  CG  . ASN A 1 46  ? 26.161 46.284 8.289   1.00 13.82 ? 46   ASN A CG  1 
ATOM   367  O  OD1 . ASN A 1 46  ? 26.632 45.251 8.759   1.00 12.86 ? 46   ASN A OD1 1 
ATOM   368  N  ND2 . ASN A 1 46  ? 26.561 46.786 7.135   1.00 15.71 ? 46   ASN A ND2 1 
ATOM   369  N  N   . GLU A 1 47  ? 22.616 46.920 7.149   1.00 16.43 ? 47   GLU A N   1 
ATOM   370  C  CA  . GLU A 1 47  ? 22.019 46.769 5.828   1.00 12.26 ? 47   GLU A CA  1 
ATOM   371  C  C   . GLU A 1 47  ? 22.986 46.358 4.719   1.00 11.81 ? 47   GLU A C   1 
ATOM   372  O  O   . GLU A 1 47  ? 24.083 46.917 4.578   1.00 14.25 ? 47   GLU A O   1 
ATOM   373  C  CB  . GLU A 1 47  ? 21.319 48.061 5.450   1.00 12.39 ? 47   GLU A CB  1 
ATOM   374  C  CG  . GLU A 1 47  ? 20.531 47.983 4.188   1.00 13.59 ? 47   GLU A CG  1 
ATOM   375  C  CD  . GLU A 1 47  ? 19.976 49.317 3.784   1.00 14.88 ? 47   GLU A CD  1 
ATOM   376  O  OE1 . GLU A 1 47  ? 20.274 50.326 4.460   1.00 11.42 ? 47   GLU A OE1 1 
ATOM   377  O  OE2 . GLU A 1 47  ? 19.234 49.352 2.784   1.00 15.00 ? 47   GLU A OE2 1 
ATOM   378  N  N   . ASN A 1 48  ? 22.538 45.425 3.887   1.00 8.55  ? 48   ASN A N   1 
ATOM   379  C  CA  . ASN A 1 48  ? 23.352 44.918 2.791   1.00 8.45  ? 48   ASN A CA  1 
ATOM   380  C  C   . ASN A 1 48  ? 22.603 44.959 1.468   1.00 11.59 ? 48   ASN A C   1 
ATOM   381  O  O   . ASN A 1 48  ? 21.399 45.239 1.423   1.00 15.52 ? 48   ASN A O   1 
ATOM   382  C  CB  . ASN A 1 48  ? 23.821 43.480 3.088   1.00 8.52  ? 48   ASN A CB  1 
ATOM   383  C  CG  . ASN A 1 48  ? 22.668 42.481 3.169   1.00 10.05 ? 48   ASN A CG  1 
ATOM   384  O  OD1 . ASN A 1 48  ? 22.121 42.231 4.248   1.00 8.81  ? 48   ASN A OD1 1 
ATOM   385  N  ND2 . ASN A 1 48  ? 22.306 41.892 2.028   1.00 6.42  ? 48   ASN A ND2 1 
ATOM   386  N  N   . ILE A 1 49  ? 23.324 44.700 0.385   1.00 10.15 ? 49   ILE A N   1 
ATOM   387  C  CA  . ILE A 1 49  ? 22.722 44.698 -0.938  1.00 14.94 ? 49   ILE A CA  1 
ATOM   388  C  C   . ILE A 1 49  ? 21.972 43.387 -1.186  1.00 15.30 ? 49   ILE A C   1 
ATOM   389  O  O   . ILE A 1 49  ? 22.350 42.338 -0.660  1.00 15.77 ? 49   ILE A O   1 
ATOM   390  C  CB  . ILE A 1 49  ? 23.798 44.914 -2.030  1.00 14.68 ? 49   ILE A CB  1 
ATOM   391  C  CG1 . ILE A 1 49  ? 23.142 45.380 -3.330  1.00 17.43 ? 49   ILE A CG1 1 
ATOM   392  C  CG2 . ILE A 1 49  ? 24.593 43.638 -2.257  1.00 13.92 ? 49   ILE A CG2 1 
ATOM   393  C  CD1 . ILE A 1 49  ? 24.082 46.113 -4.254  1.00 17.65 ? 49   ILE A CD1 1 
ATOM   394  N  N   . VAL A 1 50  ? 20.881 43.462 -1.940  1.00 15.24 ? 50   VAL A N   1 
ATOM   395  C  CA  . VAL A 1 50  ? 20.096 42.280 -2.272  1.00 11.63 ? 50   VAL A CA  1 
ATOM   396  C  C   . VAL A 1 50  ? 20.642 41.659 -3.559  1.00 14.82 ? 50   VAL A C   1 
ATOM   397  O  O   . VAL A 1 50  ? 20.582 42.272 -4.631  1.00 18.43 ? 50   VAL A O   1 
ATOM   398  C  CB  . VAL A 1 50  ? 18.604 42.621 -2.475  1.00 9.73  ? 50   VAL A CB  1 
ATOM   399  C  CG1 . VAL A 1 50  ? 17.850 41.402 -2.991  1.00 11.88 ? 50   VAL A CG1 1 
ATOM   400  C  CG2 . VAL A 1 50  ? 17.986 43.086 -1.168  1.00 9.46  ? 50   VAL A CG2 1 
ATOM   401  N  N   . VAL A 1 51  ? 21.243 40.480 -3.427  1.00 15.36 ? 51   VAL A N   1 
ATOM   402  C  CA  . VAL A 1 51  ? 21.787 39.751 -4.564  1.00 15.31 ? 51   VAL A CA  1 
ATOM   403  C  C   . VAL A 1 51  ? 20.708 38.768 -5.008  1.00 19.20 ? 51   VAL A C   1 
ATOM   404  O  O   . VAL A 1 51  ? 20.305 37.888 -4.244  1.00 24.49 ? 51   VAL A O   1 
ATOM   405  C  CB  . VAL A 1 51  ? 23.076 38.989 -4.180  1.00 14.77 ? 51   VAL A CB  1 
ATOM   406  C  CG1 . VAL A 1 51  ? 23.593 38.181 -5.369  1.00 14.34 ? 51   VAL A CG1 1 
ATOM   407  C  CG2 . VAL A 1 51  ? 24.145 39.971 -3.740  1.00 13.81 ? 51   VAL A CG2 1 
ATOM   408  N  N   . THR A 1 52  ? 20.204 38.965 -6.222  1.00 19.79 ? 52   THR A N   1 
ATOM   409  C  CA  . THR A 1 52  ? 19.148 38.131 -6.786  1.00 17.05 ? 52   THR A CA  1 
ATOM   410  C  C   . THR A 1 52  ? 19.704 37.027 -7.691  1.00 20.51 ? 52   THR A C   1 
ATOM   411  O  O   . THR A 1 52  ? 18.977 36.121 -8.094  1.00 20.54 ? 52   THR A O   1 
ATOM   412  C  CB  . THR A 1 52  ? 18.159 38.998 -7.593  1.00 15.78 ? 52   THR A CB  1 
ATOM   413  O  OG1 . THR A 1 52  ? 18.880 39.720 -8.598  1.00 16.29 ? 52   THR A OG1 1 
ATOM   414  C  CG2 . THR A 1 52  ? 17.461 39.994 -6.692  1.00 14.11 ? 52   THR A CG2 1 
ATOM   415  N  N   . ASN A 1 53  ? 20.987 37.112 -8.024  1.00 22.94 ? 53   ASN A N   1 
ATOM   416  C  CA  . ASN A 1 53  ? 21.623 36.109 -8.866  1.00 22.63 ? 53   ASN A CA  1 
ATOM   417  C  C   . ASN A 1 53  ? 23.019 35.777 -8.341  1.00 23.93 ? 53   ASN A C   1 
ATOM   418  O  O   . ASN A 1 53  ? 23.971 36.533 -8.567  1.00 21.61 ? 53   ASN A O   1 
ATOM   419  C  CB  . ASN A 1 53  ? 21.712 36.595 -10.311 1.00 31.10 ? 53   ASN A CB  1 
ATOM   420  C  CG  . ASN A 1 53  ? 22.238 35.523 -11.257 1.00 38.86 ? 53   ASN A CG  1 
ATOM   421  O  OD1 . ASN A 1 53  ? 21.552 34.537 -11.542 1.00 42.15 ? 53   ASN A OD1 1 
ATOM   422  N  ND2 . ASN A 1 53  ? 23.462 35.710 -11.743 1.00 41.33 ? 53   ASN A ND2 1 
ATOM   423  N  N   . PRO A 1 54  ? 23.156 34.654 -7.607  1.00 22.01 ? 54   PRO A N   1 
ATOM   424  C  CA  . PRO A 1 54  ? 22.092 33.704 -7.250  1.00 18.86 ? 54   PRO A CA  1 
ATOM   425  C  C   . PRO A 1 54  ? 21.107 34.232 -6.192  1.00 17.74 ? 54   PRO A C   1 
ATOM   426  O  O   . PRO A 1 54  ? 21.339 35.281 -5.585  1.00 19.57 ? 54   PRO A O   1 
ATOM   427  C  CB  . PRO A 1 54  ? 22.878 32.487 -6.767  1.00 18.29 ? 54   PRO A CB  1 
ATOM   428  C  CG  . PRO A 1 54  ? 24.115 33.093 -6.186  1.00 19.70 ? 54   PRO A CG  1 
ATOM   429  C  CD  . PRO A 1 54  ? 24.475 34.134 -7.205  1.00 19.94 ? 54   PRO A CD  1 
ATOM   430  N  N   . SER A 1 55  ? 20.014 33.504 -5.983  1.00 18.06 ? 55   SER A N   1 
ATOM   431  C  CA  . SER A 1 55  ? 18.963 33.893 -5.042  1.00 18.45 ? 55   SER A CA  1 
ATOM   432  C  C   . SER A 1 55  ? 19.336 34.031 -3.571  1.00 19.97 ? 55   SER A C   1 
ATOM   433  O  O   . SER A 1 55  ? 19.375 33.040 -2.831  1.00 22.90 ? 55   SER A O   1 
ATOM   434  C  CB  . SER A 1 55  ? 17.774 32.934 -5.154  1.00 21.65 ? 55   SER A CB  1 
ATOM   435  O  OG  . SER A 1 55  ? 17.258 32.916 -6.474  1.00 32.63 ? 55   SER A OG  1 
ATOM   436  N  N   . ARG A 1 56  ? 19.556 35.272 -3.149  1.00 17.27 ? 56   ARG A N   1 
ATOM   437  C  CA  . ARG A 1 56  ? 19.880 35.601 -1.763  1.00 14.73 ? 56   ARG A CA  1 
ATOM   438  C  C   . ARG A 1 56  ? 20.956 34.711 -1.148  1.00 14.98 ? 56   ARG A C   1 
ATOM   439  O  O   . ARG A 1 56  ? 20.688 33.957 -0.209  1.00 16.55 ? 56   ARG A O   1 
ATOM   440  C  CB  . ARG A 1 56  ? 18.612 35.543 -0.901  1.00 13.36 ? 56   ARG A CB  1 
ATOM   441  C  CG  . ARG A 1 56  ? 17.376 36.181 -1.540  1.00 11.60 ? 56   ARG A CG  1 
ATOM   442  C  CD  . ARG A 1 56  ? 17.654 37.597 -2.020  1.00 12.84 ? 56   ARG A CD  1 
ATOM   443  N  NE  . ARG A 1 56  ? 18.119 38.463 -0.939  1.00 13.68 ? 56   ARG A NE  1 
ATOM   444  C  CZ  . ARG A 1 56  ? 17.321 39.051 -0.056  1.00 11.83 ? 56   ARG A CZ  1 
ATOM   445  N  NH1 . ARG A 1 56  ? 16.007 38.890 -0.131  1.00 15.75 ? 56   ARG A NH1 1 
ATOM   446  N  NH2 . ARG A 1 56  ? 17.835 39.814 0.896   1.00 12.28 ? 56   ARG A NH2 1 
ATOM   447  N  N   . PRO A 1 57  ? 22.189 34.780 -1.673  1.00 13.14 ? 57   PRO A N   1 
ATOM   448  C  CA  . PRO A 1 57  ? 23.268 33.952 -1.128  1.00 9.73  ? 57   PRO A CA  1 
ATOM   449  C  C   . PRO A 1 57  ? 23.642 34.401 0.282   1.00 13.79 ? 57   PRO A C   1 
ATOM   450  O  O   . PRO A 1 57  ? 23.268 35.497 0.717   1.00 17.80 ? 57   PRO A O   1 
ATOM   451  C  CB  . PRO A 1 57  ? 24.403 34.190 -2.117  1.00 6.99  ? 57   PRO A CB  1 
ATOM   452  C  CG  . PRO A 1 57  ? 24.157 35.596 -2.572  1.00 10.59 ? 57   PRO A CG  1 
ATOM   453  C  CD  . PRO A 1 57  ? 22.674 35.611 -2.788  1.00 11.56 ? 57   PRO A CD  1 
ATOM   454  N  N   . TRP A 1 58  ? 24.370 33.559 1.006   1.00 12.78 ? 58   TRP A N   1 
ATOM   455  C  CA  . TRP A 1 58  ? 24.782 33.912 2.363   1.00 10.02 ? 58   TRP A CA  1 
ATOM   456  C  C   . TRP A 1 58  ? 25.768 35.086 2.345   1.00 12.99 ? 58   TRP A C   1 
ATOM   457  O  O   . TRP A 1 58  ? 25.779 35.913 3.267   1.00 11.64 ? 58   TRP A O   1 
ATOM   458  C  CB  . TRP A 1 58  ? 25.411 32.707 3.085   1.00 7.71  ? 58   TRP A CB  1 
ATOM   459  C  CG  . TRP A 1 58  ? 26.676 32.186 2.435   1.00 10.41 ? 58   TRP A CG  1 
ATOM   460  C  CD1 . TRP A 1 58  ? 26.765 31.204 1.490   1.00 9.14  ? 58   TRP A CD1 1 
ATOM   461  C  CD2 . TRP A 1 58  ? 28.018 32.654 2.654   1.00 9.30  ? 58   TRP A CD2 1 
ATOM   462  N  NE1 . TRP A 1 58  ? 28.070 31.039 1.103   1.00 10.92 ? 58   TRP A NE1 1 
ATOM   463  C  CE2 . TRP A 1 58  ? 28.862 31.915 1.797   1.00 9.69  ? 58   TRP A CE2 1 
ATOM   464  C  CE3 . TRP A 1 58  ? 28.587 33.628 3.485   1.00 9.58  ? 58   TRP A CE3 1 
ATOM   465  C  CZ2 . TRP A 1 58  ? 30.245 32.119 1.744   1.00 7.17  ? 58   TRP A CZ2 1 
ATOM   466  C  CZ3 . TRP A 1 58  ? 29.961 33.831 3.431   1.00 8.73  ? 58   TRP A CZ3 1 
ATOM   467  C  CH2 . TRP A 1 58  ? 30.774 33.077 2.565   1.00 7.32  ? 58   TRP A CH2 1 
ATOM   468  N  N   . TRP A 1 59  ? 26.584 35.164 1.291   1.00 11.95 ? 59   TRP A N   1 
ATOM   469  C  CA  . TRP A 1 59  ? 27.582 36.220 1.180   1.00 12.61 ? 59   TRP A CA  1 
ATOM   470  C  C   . TRP A 1 59  ? 27.121 37.635 0.865   1.00 14.44 ? 59   TRP A C   1 
ATOM   471  O  O   . TRP A 1 59  ? 27.915 38.568 0.967   1.00 14.58 ? 59   TRP A O   1 
ATOM   472  C  CB  . TRP A 1 59  ? 28.757 35.816 0.274   1.00 10.44 ? 59   TRP A CB  1 
ATOM   473  C  CG  . TRP A 1 59  ? 28.419 35.172 -1.034  1.00 11.66 ? 59   TRP A CG  1 
ATOM   474  C  CD1 . TRP A 1 59  ? 28.571 33.851 -1.351  1.00 11.44 ? 59   TRP A CD1 1 
ATOM   475  C  CD2 . TRP A 1 59  ? 27.979 35.823 -2.234  1.00 11.09 ? 59   TRP A CD2 1 
ATOM   476  N  NE1 . TRP A 1 59  ? 28.269 33.643 -2.672  1.00 13.49 ? 59   TRP A NE1 1 
ATOM   477  C  CE2 . TRP A 1 59  ? 27.900 34.834 -3.240  1.00 13.33 ? 59   TRP A CE2 1 
ATOM   478  C  CE3 . TRP A 1 59  ? 27.650 37.145 -2.560  1.00 12.40 ? 59   TRP A CE3 1 
ATOM   479  C  CZ2 . TRP A 1 59  ? 27.507 35.126 -4.551  1.00 14.36 ? 59   TRP A CZ2 1 
ATOM   480  C  CZ3 . TRP A 1 59  ? 27.259 37.438 -3.863  1.00 11.51 ? 59   TRP A CZ3 1 
ATOM   481  C  CH2 . TRP A 1 59  ? 27.191 36.431 -4.843  1.00 12.74 ? 59   TRP A CH2 1 
ATOM   482  N  N   . GLU A 1 60  ? 25.848 37.824 0.536   1.00 12.95 ? 60   GLU A N   1 
ATOM   483  C  CA  . GLU A 1 60  ? 25.376 39.176 0.252   1.00 14.05 ? 60   GLU A CA  1 
ATOM   484  C  C   . GLU A 1 60  ? 25.452 40.042 1.517   1.00 11.93 ? 60   GLU A C   1 
ATOM   485  O  O   . GLU A 1 60  ? 25.478 41.265 1.432   1.00 14.62 ? 60   GLU A O   1 
ATOM   486  C  CB  . GLU A 1 60  ? 23.943 39.173 -0.293  1.00 9.94  ? 60   GLU A CB  1 
ATOM   487  C  CG  . GLU A 1 60  ? 22.894 38.768 0.725   1.00 8.52  ? 60   GLU A CG  1 
ATOM   488  C  CD  . GLU A 1 60  ? 21.486 39.059 0.268   1.00 10.13 ? 60   GLU A CD  1 
ATOM   489  O  OE1 . GLU A 1 60  ? 21.215 38.999 -0.949  1.00 12.50 ? 60   GLU A OE1 1 
ATOM   490  O  OE2 . GLU A 1 60  ? 20.639 39.344 1.135   1.00 15.10 ? 60   GLU A OE2 1 
ATOM   491  N  N   . ARG A 1 61  ? 25.491 39.405 2.687   1.00 8.93  ? 61   ARG A N   1 
ATOM   492  C  CA  . ARG A 1 61  ? 25.570 40.130 3.953   1.00 7.08  ? 61   ARG A CA  1 
ATOM   493  C  C   . ARG A 1 61  ? 26.957 40.719 4.205   1.00 8.62  ? 61   ARG A C   1 
ATOM   494  O  O   . ARG A 1 61  ? 27.174 41.412 5.198   1.00 10.90 ? 61   ARG A O   1 
ATOM   495  C  CB  . ARG A 1 61  ? 25.155 39.233 5.120   1.00 5.86  ? 61   ARG A CB  1 
ATOM   496  C  CG  . ARG A 1 61  ? 23.707 38.784 5.053   1.00 7.01  ? 61   ARG A CG  1 
ATOM   497  C  CD  . ARG A 1 61  ? 23.267 38.052 6.315   1.00 4.94  ? 61   ARG A CD  1 
ATOM   498  N  NE  . ARG A 1 61  ? 23.054 38.940 7.458   1.00 4.87  ? 61   ARG A NE  1 
ATOM   499  C  CZ  . ARG A 1 61  ? 22.241 38.661 8.475   1.00 5.91  ? 61   ARG A CZ  1 
ATOM   500  N  NH1 . ARG A 1 61  ? 21.533 37.544 8.471   1.00 6.83  ? 61   ARG A NH1 1 
ATOM   501  N  NH2 . ARG A 1 61  ? 22.101 39.510 9.478   1.00 4.50  ? 61   ARG A NH2 1 
ATOM   502  N  N   . TYR A 1 62  ? 27.904 40.411 3.322   1.00 11.66 ? 62   TYR A N   1 
ATOM   503  C  CA  . TYR A 1 62  ? 29.263 40.925 3.440   1.00 8.92  ? 62   TYR A CA  1 
ATOM   504  C  C   . TYR A 1 62  ? 29.494 42.036 2.430   1.00 11.98 ? 62   TYR A C   1 
ATOM   505  O  O   . TYR A 1 62  ? 30.633 42.384 2.107   1.00 14.64 ? 62   TYR A O   1 
ATOM   506  C  CB  . TYR A 1 62  ? 30.291 39.789 3.317   1.00 9.39  ? 62   TYR A CB  1 
ATOM   507  C  CG  . TYR A 1 62  ? 30.252 38.878 4.529   1.00 9.51  ? 62   TYR A CG  1 
ATOM   508  C  CD1 . TYR A 1 62  ? 30.982 39.184 5.670   1.00 8.93  ? 62   TYR A CD1 1 
ATOM   509  C  CD2 . TYR A 1 62  ? 29.390 37.785 4.579   1.00 9.06  ? 62   TYR A CD2 1 
ATOM   510  C  CE1 . TYR A 1 62  ? 30.849 38.437 6.830   1.00 9.38  ? 62   TYR A CE1 1 
ATOM   511  C  CE2 . TYR A 1 62  ? 29.249 37.036 5.743   1.00 8.63  ? 62   TYR A CE2 1 
ATOM   512  C  CZ  . TYR A 1 62  ? 29.977 37.371 6.862   1.00 9.54  ? 62   TYR A CZ  1 
ATOM   513  O  OH  . TYR A 1 62  ? 29.814 36.668 8.031   1.00 10.24 ? 62   TYR A OH  1 
ATOM   514  N  N   . GLN A 1 63  ? 28.388 42.597 1.946   1.00 12.14 ? 63   GLN A N   1 
ATOM   515  C  CA  . GLN A 1 63  ? 28.404 43.711 1.002   1.00 11.57 ? 63   GLN A CA  1 
ATOM   516  C  C   . GLN A 1 63  ? 27.477 44.799 1.560   1.00 12.20 ? 63   GLN A C   1 
ATOM   517  O  O   . GLN A 1 63  ? 26.306 44.887 1.184   1.00 11.61 ? 63   GLN A O   1 
ATOM   518  C  CB  . GLN A 1 63  ? 27.923 43.263 -0.374  1.00 10.77 ? 63   GLN A CB  1 
ATOM   519  C  CG  . GLN A 1 63  ? 28.792 42.209 -1.015  1.00 10.96 ? 63   GLN A CG  1 
ATOM   520  C  CD  . GLN A 1 63  ? 28.370 41.929 -2.434  1.00 15.96 ? 63   GLN A CD  1 
ATOM   521  O  OE1 . GLN A 1 63  ? 28.020 42.848 -3.169  1.00 20.82 ? 63   GLN A OE1 1 
ATOM   522  N  NE2 . GLN A 1 63  ? 28.393 40.666 -2.830  1.00 19.14 ? 63   GLN A NE2 1 
ATOM   523  N  N   . PRO A 1 64  ? 27.987 45.613 2.502   1.00 11.22 ? 64   PRO A N   1 
ATOM   524  C  CA  . PRO A 1 64  ? 27.241 46.702 3.144   1.00 9.67  ? 64   PRO A CA  1 
ATOM   525  C  C   . PRO A 1 64  ? 26.804 47.828 2.208   1.00 10.67 ? 64   PRO A C   1 
ATOM   526  O  O   . PRO A 1 64  ? 27.450 48.092 1.193   1.00 12.21 ? 64   PRO A O   1 
ATOM   527  C  CB  . PRO A 1 64  ? 28.244 47.241 4.171   1.00 6.64  ? 64   PRO A CB  1 
ATOM   528  C  CG  . PRO A 1 64  ? 29.108 46.074 4.478   1.00 7.03  ? 64   PRO A CG  1 
ATOM   529  C  CD  . PRO A 1 64  ? 29.322 45.473 3.111   1.00 8.67  ? 64   PRO A CD  1 
ATOM   530  N  N   . VAL A 1 65  ? 25.686 48.466 2.551   1.00 12.75 ? 65   VAL A N   1 
ATOM   531  C  CA  . VAL A 1 65  ? 25.174 49.611 1.802   1.00 13.25 ? 65   VAL A CA  1 
ATOM   532  C  C   . VAL A 1 65  ? 24.875 50.769 2.760   1.00 13.64 ? 65   VAL A C   1 
ATOM   533  O  O   . VAL A 1 65  ? 24.661 51.896 2.326   1.00 20.08 ? 65   VAL A O   1 
ATOM   534  C  CB  . VAL A 1 65  ? 23.930 49.287 0.921   1.00 12.59 ? 65   VAL A CB  1 
ATOM   535  C  CG1 . VAL A 1 65  ? 24.278 48.232 -0.138  1.00 11.32 ? 65   VAL A CG1 1 
ATOM   536  C  CG2 . VAL A 1 65  ? 22.768 48.853 1.764   1.00 12.49 ? 65   VAL A CG2 1 
ATOM   537  N  N   . SER A 1 66  ? 24.875 50.485 4.060   1.00 11.18 ? 66   SER A N   1 
ATOM   538  C  CA  . SER A 1 66  ? 24.652 51.504 5.087   1.00 11.37 ? 66   SER A CA  1 
ATOM   539  C  C   . SER A 1 66  ? 24.920 50.867 6.444   1.00 11.43 ? 66   SER A C   1 
ATOM   540  O  O   . SER A 1 66  ? 25.307 49.703 6.513   1.00 11.70 ? 66   SER A O   1 
ATOM   541  C  CB  . SER A 1 66  ? 23.223 52.055 5.032   1.00 8.91  ? 66   SER A CB  1 
ATOM   542  O  OG  . SER A 1 66  ? 22.318 51.261 5.780   1.00 10.00 ? 66   SER A OG  1 
ATOM   543  N  N   . TYR A 1 67  ? 24.725 51.619 7.520   1.00 12.96 ? 67   TYR A N   1 
ATOM   544  C  CA  . TYR A 1 67  ? 24.941 51.080 8.853   1.00 13.42 ? 67   TYR A CA  1 
ATOM   545  C  C   . TYR A 1 67  ? 23.644 50.971 9.646   1.00 14.07 ? 67   TYR A C   1 
ATOM   546  O  O   . TYR A 1 67  ? 23.657 50.913 10.879  1.00 14.36 ? 67   TYR A O   1 
ATOM   547  C  CB  . TYR A 1 67  ? 26.001 51.893 9.603   1.00 13.42 ? 67   TYR A CB  1 
ATOM   548  C  CG  . TYR A 1 67  ? 27.359 51.825 8.936   1.00 14.11 ? 67   TYR A CG  1 
ATOM   549  C  CD1 . TYR A 1 67  ? 27.998 50.604 8.739   1.00 14.54 ? 67   TYR A CD1 1 
ATOM   550  C  CD2 . TYR A 1 67  ? 27.980 52.970 8.462   1.00 14.94 ? 67   TYR A CD2 1 
ATOM   551  C  CE1 . TYR A 1 67  ? 29.218 50.526 8.083   1.00 15.24 ? 67   TYR A CE1 1 
ATOM   552  C  CE2 . TYR A 1 67  ? 29.200 52.904 7.804   1.00 16.17 ? 67   TYR A CE2 1 
ATOM   553  C  CZ  . TYR A 1 67  ? 29.812 51.679 7.619   1.00 17.04 ? 67   TYR A CZ  1 
ATOM   554  O  OH  . TYR A 1 67  ? 31.019 51.618 6.967   1.00 18.83 ? 67   TYR A OH  1 
ATOM   555  N  N   . LYS A 1 68  ? 22.525 50.939 8.926   1.00 13.84 ? 68   LYS A N   1 
ATOM   556  C  CA  . LYS A 1 68  ? 21.206 50.792 9.544   1.00 16.97 ? 68   LYS A CA  1 
ATOM   557  C  C   . LYS A 1 68  ? 21.048 49.337 9.981   1.00 14.82 ? 68   LYS A C   1 
ATOM   558  O  O   . LYS A 1 68  ? 21.390 48.427 9.221   1.00 14.16 ? 68   LYS A O   1 
ATOM   559  C  CB  . LYS A 1 68  ? 20.102 51.127 8.539   1.00 22.05 ? 68   LYS A CB  1 
ATOM   560  C  CG  . LYS A 1 68  ? 20.142 52.547 7.986   1.00 27.32 ? 68   LYS A CG  1 
ATOM   561  C  CD  . LYS A 1 68  ? 19.009 52.757 6.992   1.00 31.18 ? 68   LYS A CD  1 
ATOM   562  C  CE  . LYS A 1 68  ? 19.045 54.143 6.368   1.00 36.84 ? 68   LYS A CE  1 
ATOM   563  N  NZ  . LYS A 1 68  ? 17.982 54.306 5.323   1.00 39.64 ? 68   LYS A NZ  1 
ATOM   564  N  N   . LEU A 1 69  ? 20.554 49.123 11.201  1.00 12.15 ? 69   LEU A N   1 
ATOM   565  C  CA  . LEU A 1 69  ? 20.349 47.777 11.747  1.00 10.06 ? 69   LEU A CA  1 
ATOM   566  C  C   . LEU A 1 69  ? 19.077 47.223 11.135  1.00 10.76 ? 69   LEU A C   1 
ATOM   567  O  O   . LEU A 1 69  ? 18.042 47.117 11.798  1.00 12.89 ? 69   LEU A O   1 
ATOM   568  C  CB  . LEU A 1 69  ? 20.233 47.841 13.270  1.00 8.68  ? 69   LEU A CB  1 
ATOM   569  C  CG  . LEU A 1 69  ? 21.536 47.727 14.064  1.00 7.01  ? 69   LEU A CG  1 
ATOM   570  C  CD1 . LEU A 1 69  ? 22.668 48.424 13.353  1.00 9.50  ? 69   LEU A CD1 1 
ATOM   571  C  CD2 . LEU A 1 69  ? 21.336 48.298 15.460  1.00 8.61  ? 69   LEU A CD2 1 
ATOM   572  N  N   . CYS A 1 70  ? 19.191 46.784 9.891   1.00 9.84  ? 70   CYS A N   1 
ATOM   573  C  CA  . CYS A 1 70  ? 18.036 46.322 9.142   1.00 12.42 ? 70   CYS A CA  1 
ATOM   574  C  C   . CYS A 1 70  ? 18.430 45.240 8.120   1.00 12.24 ? 70   CYS A C   1 
ATOM   575  O  O   . CYS A 1 70  ? 18.951 45.543 7.036   1.00 10.07 ? 70   CYS A O   1 
ATOM   576  C  CB  . CYS A 1 70  ? 17.507 47.571 8.455   1.00 17.70 ? 70   CYS A CB  1 
ATOM   577  S  SG  . CYS A 1 70  ? 15.915 47.545 7.608   1.00 31.13 ? 70   CYS A SG  1 
ATOM   578  N  N   . THR A 1 71  ? 18.163 43.982 8.463   1.00 9.82  ? 71   THR A N   1 
ATOM   579  C  CA  . THR A 1 71  ? 18.524 42.845 7.615   1.00 9.35  ? 71   THR A CA  1 
ATOM   580  C  C   . THR A 1 71  ? 17.474 41.732 7.659   1.00 11.07 ? 71   THR A C   1 
ATOM   581  O  O   . THR A 1 71  ? 16.435 41.870 8.310   1.00 15.01 ? 71   THR A O   1 
ATOM   582  C  CB  . THR A 1 71  ? 19.840 42.220 8.111   1.00 6.15  ? 71   THR A CB  1 
ATOM   583  O  OG1 . THR A 1 71  ? 19.700 41.884 9.498   1.00 6.11  ? 71   THR A OG1 1 
ATOM   584  C  CG2 . THR A 1 71  ? 20.989 43.180 7.958   1.00 7.11  ? 71   THR A CG2 1 
ATOM   585  N  N   . ARG A 1 72  ? 17.787 40.605 7.020   1.00 12.83 ? 72   ARG A N   1 
ATOM   586  C  CA  . ARG A 1 72  ? 16.896 39.447 7.000   1.00 12.88 ? 72   ARG A CA  1 
ATOM   587  C  C   . ARG A 1 72  ? 16.770 38.810 8.379   1.00 17.66 ? 72   ARG A C   1 
ATOM   588  O  O   . ARG A 1 72  ? 15.851 38.015 8.624   1.00 17.51 ? 72   ARG A O   1 
ATOM   589  C  CB  . ARG A 1 72  ? 17.380 38.405 5.999   1.00 11.24 ? 72   ARG A CB  1 
ATOM   590  C  CG  . ARG A 1 72  ? 17.101 38.761 4.559   1.00 13.39 ? 72   ARG A CG  1 
ATOM   591  C  CD  . ARG A 1 72  ? 17.905 37.877 3.627   1.00 14.43 ? 72   ARG A CD  1 
ATOM   592  N  NE  . ARG A 1 72  ? 17.305 36.572 3.398   1.00 11.81 ? 72   ARG A NE  1 
ATOM   593  C  CZ  . ARG A 1 72  ? 17.958 35.533 2.884   1.00 13.28 ? 72   ARG A CZ  1 
ATOM   594  N  NH1 . ARG A 1 72  ? 19.260 35.607 2.616   1.00 9.58  ? 72   ARG A NH1 1 
ATOM   595  N  NH2 . ARG A 1 72  ? 17.315 34.392 2.694   1.00 14.97 ? 72   ARG A NH2 1 
ATOM   596  N  N   . SER A 1 73  ? 17.714 39.127 9.261   1.00 17.87 ? 73   SER A N   1 
ATOM   597  C  CA  . SER A 1 73  ? 17.683 38.612 10.622  1.00 18.07 ? 73   SER A CA  1 
ATOM   598  C  C   . SER A 1 73  ? 16.715 39.452 11.450  1.00 17.65 ? 73   SER A C   1 
ATOM   599  O  O   . SER A 1 73  ? 16.257 39.016 12.509  1.00 20.23 ? 73   SER A O   1 
ATOM   600  C  CB  . SER A 1 73  ? 19.080 38.640 11.248  1.00 17.99 ? 73   SER A CB  1 
ATOM   601  O  OG  . SER A 1 73  ? 19.923 37.654 10.679  1.00 13.12 ? 73   SER A OG  1 
ATOM   602  N  N   . GLY A 1 74  ? 16.398 40.649 10.969  1.00 19.42 ? 74   GLY A N   1 
ATOM   603  C  CA  . GLY A 1 74  ? 15.472 41.500 11.693  1.00 18.56 ? 74   GLY A CA  1 
ATOM   604  C  C   . GLY A 1 74  ? 15.809 42.978 11.677  1.00 19.10 ? 74   GLY A C   1 
ATOM   605  O  O   . GLY A 1 74  ? 16.761 43.400 11.022  1.00 22.72 ? 74   GLY A O   1 
ATOM   606  N  N   . ASN A 1 75  ? 15.016 43.761 12.403  1.00 20.20 ? 75   ASN A N   1 
ATOM   607  C  CA  . ASN A 1 75  ? 15.197 45.203 12.496  1.00 20.30 ? 75   ASN A CA  1 
ATOM   608  C  C   . ASN A 1 75  ? 15.864 45.596 13.813  1.00 19.50 ? 75   ASN A C   1 
ATOM   609  O  O   . ASN A 1 75  ? 16.135 44.741 14.660  1.00 22.22 ? 75   ASN A O   1 
ATOM   610  C  CB  . ASN A 1 75  ? 13.850 45.923 12.332  1.00 21.05 ? 75   ASN A CB  1 
ATOM   611  C  CG  . ASN A 1 75  ? 12.850 45.571 13.428  1.00 23.62 ? 75   ASN A CG  1 
ATOM   612  O  OD1 . ASN A 1 75  ? 13.223 45.306 14.573  1.00 24.78 ? 75   ASN A OD1 1 
ATOM   613  N  ND2 . ASN A 1 75  ? 11.572 45.574 13.080  1.00 22.94 ? 75   ASN A ND2 1 
ATOM   614  N  N   . GLU A 1 76  ? 16.096 46.893 13.994  1.00 20.74 ? 76   GLU A N   1 
ATOM   615  C  CA  . GLU A 1 76  ? 16.739 47.406 15.198  1.00 20.48 ? 76   GLU A CA  1 
ATOM   616  C  C   . GLU A 1 76  ? 16.025 47.094 16.508  1.00 20.39 ? 76   GLU A C   1 
ATOM   617  O  O   . GLU A 1 76  ? 16.677 46.889 17.530  1.00 23.81 ? 76   GLU A O   1 
ATOM   618  C  CB  . GLU A 1 76  ? 16.971 48.907 15.090  1.00 20.65 ? 76   GLU A CB  1 
ATOM   619  C  CG  . GLU A 1 76  ? 17.798 49.447 16.235  1.00 26.40 ? 76   GLU A CG  1 
ATOM   620  C  CD  . GLU A 1 76  ? 18.135 50.910 16.084  1.00 27.75 ? 76   GLU A CD  1 
ATOM   621  O  OE1 . GLU A 1 76  ? 18.382 51.360 14.947  1.00 31.82 ? 76   GLU A OE1 1 
ATOM   622  O  OE2 . GLU A 1 76  ? 18.165 51.610 17.114  1.00 30.58 ? 76   GLU A OE2 1 
ATOM   623  N  N   . ASN A 1 77  ? 14.696 47.077 16.493  1.00 23.30 ? 77   ASN A N   1 
ATOM   624  C  CA  . ASN A 1 77  ? 13.930 46.772 17.701  1.00 23.33 ? 77   ASN A CA  1 
ATOM   625  C  C   . ASN A 1 77  ? 14.240 45.351 18.122  1.00 19.92 ? 77   ASN A C   1 
ATOM   626  O  O   . ASN A 1 77  ? 14.548 45.081 19.285  1.00 16.42 ? 77   ASN A O   1 
ATOM   627  C  CB  . ASN A 1 77  ? 12.426 46.879 17.449  1.00 30.55 ? 77   ASN A CB  1 
ATOM   628  C  CG  . ASN A 1 77  ? 11.973 48.295 17.227  1.00 37.27 ? 77   ASN A CG  1 
ATOM   629  O  OD1 . ASN A 1 77  ? 11.254 48.581 16.267  1.00 44.28 ? 77   ASN A OD1 1 
ATOM   630  N  ND2 . ASN A 1 77  ? 12.395 49.202 18.101  1.00 39.00 ? 77   ASN A ND2 1 
ATOM   631  N  N   . GLU A 1 78  ? 14.145 44.445 17.157  1.00 15.81 ? 78   GLU A N   1 
ATOM   632  C  CA  . GLU A 1 78  ? 14.411 43.039 17.388  1.00 15.87 ? 78   GLU A CA  1 
ATOM   633  C  C   . GLU A 1 78  ? 15.855 42.829 17.818  1.00 15.65 ? 78   GLU A C   1 
ATOM   634  O  O   . GLU A 1 78  ? 16.122 42.020 18.706  1.00 16.64 ? 78   GLU A O   1 
ATOM   635  C  CB  . GLU A 1 78  ? 14.065 42.244 16.138  1.00 14.14 ? 78   GLU A CB  1 
ATOM   636  C  CG  . GLU A 1 78  ? 12.582 42.322 15.824  1.00 16.44 ? 78   GLU A CG  1 
ATOM   637  C  CD  . GLU A 1 78  ? 12.225 41.775 14.467  1.00 20.02 ? 78   GLU A CD  1 
ATOM   638  O  OE1 . GLU A 1 78  ? 13.057 41.868 13.547  1.00 23.75 ? 78   GLU A OE1 1 
ATOM   639  O  OE2 . GLU A 1 78  ? 11.102 41.256 14.315  1.00 25.28 ? 78   GLU A OE2 1 
ATOM   640  N  N   . PHE A 1 79  ? 16.776 43.586 17.224  1.00 14.89 ? 79   PHE A N   1 
ATOM   641  C  CA  . PHE A 1 79  ? 18.183 43.481 17.588  1.00 14.18 ? 79   PHE A CA  1 
ATOM   642  C  C   . PHE A 1 79  ? 18.377 43.886 19.052  1.00 14.56 ? 79   PHE A C   1 
ATOM   643  O  O   . PHE A 1 79  ? 18.944 43.127 19.842  1.00 20.80 ? 79   PHE A O   1 
ATOM   644  C  CB  . PHE A 1 79  ? 19.056 44.355 16.681  1.00 13.91 ? 79   PHE A CB  1 
ATOM   645  C  CG  . PHE A 1 79  ? 20.531 44.230 16.962  1.00 14.93 ? 79   PHE A CG  1 
ATOM   646  C  CD1 . PHE A 1 79  ? 21.280 43.215 16.375  1.00 13.70 ? 79   PHE A CD1 1 
ATOM   647  C  CD2 . PHE A 1 79  ? 21.159 45.092 17.856  1.00 12.38 ? 79   PHE A CD2 1 
ATOM   648  C  CE1 . PHE A 1 79  ? 22.628 43.057 16.680  1.00 14.19 ? 79   PHE A CE1 1 
ATOM   649  C  CE2 . PHE A 1 79  ? 22.507 44.940 18.167  1.00 15.01 ? 79   PHE A CE2 1 
ATOM   650  C  CZ  . PHE A 1 79  ? 23.242 43.919 17.577  1.00 15.55 ? 79   PHE A CZ  1 
ATOM   651  N  N   . ARG A 1 80  ? 17.880 45.065 19.417  1.00 14.21 ? 80   ARG A N   1 
ATOM   652  C  CA  . ARG A 1 80  ? 17.994 45.570 20.783  1.00 14.43 ? 80   ARG A CA  1 
ATOM   653  C  C   . ARG A 1 80  ? 17.377 44.619 21.804  1.00 12.42 ? 80   ARG A C   1 
ATOM   654  O  O   . ARG A 1 80  ? 17.902 44.438 22.906  1.00 16.32 ? 80   ARG A O   1 
ATOM   655  C  CB  . ARG A 1 80  ? 17.318 46.936 20.903  1.00 19.31 ? 80   ARG A CB  1 
ATOM   656  C  CG  . ARG A 1 80  ? 18.010 48.059 20.159  1.00 22.52 ? 80   ARG A CG  1 
ATOM   657  C  CD  . ARG A 1 80  ? 17.282 49.375 20.399  1.00 27.62 ? 80   ARG A CD  1 
ATOM   658  N  NE  . ARG A 1 80  ? 18.021 50.513 19.857  1.00 34.09 ? 80   ARG A NE  1 
ATOM   659  C  CZ  . ARG A 1 80  ? 18.852 51.278 20.565  1.00 37.39 ? 80   ARG A CZ  1 
ATOM   660  N  NH1 . ARG A 1 80  ? 19.043 51.042 21.861  1.00 38.10 ? 80   ARG A NH1 1 
ATOM   661  N  NH2 . ARG A 1 80  ? 19.486 52.289 19.980  1.00 35.79 ? 80   ARG A NH2 1 
ATOM   662  N  N   . ASP A 1 81  ? 16.243 44.036 21.443  1.00 11.85 ? 81   ASP A N   1 
ATOM   663  C  CA  . ASP A 1 81  ? 15.536 43.107 22.310  1.00 15.24 ? 81   ASP A CA  1 
ATOM   664  C  C   . ASP A 1 81  ? 16.393 41.870 22.578  1.00 15.69 ? 81   ASP A C   1 
ATOM   665  O  O   . ASP A 1 81  ? 16.535 41.423 23.720  1.00 14.01 ? 81   ASP A O   1 
ATOM   666  C  CB  . ASP A 1 81  ? 14.214 42.717 21.651  1.00 19.14 ? 81   ASP A CB  1 
ATOM   667  C  CG  . ASP A 1 81  ? 13.349 41.854 22.536  1.00 25.58 ? 81   ASP A CG  1 
ATOM   668  O  OD1 . ASP A 1 81  ? 13.050 42.272 23.678  1.00 30.85 ? 81   ASP A OD1 1 
ATOM   669  O  OD2 . ASP A 1 81  ? 12.961 40.759 22.084  1.00 29.60 ? 81   ASP A OD2 1 
ATOM   670  N  N   . MET A 1 82  ? 17.000 41.352 21.518  1.00 12.82 ? 82   MET A N   1 
ATOM   671  C  CA  . MET A 1 82  ? 17.854 40.181 21.616  1.00 11.61 ? 82   MET A CA  1 
ATOM   672  C  C   . MET A 1 82  ? 19.043 40.427 22.539  1.00 14.53 ? 82   MET A C   1 
ATOM   673  O  O   . MET A 1 82  ? 19.307 39.628 23.441  1.00 17.30 ? 82   MET A O   1 
ATOM   674  C  CB  . MET A 1 82  ? 18.349 39.782 20.231  1.00 11.04 ? 82   MET A CB  1 
ATOM   675  C  CG  . MET A 1 82  ? 19.513 38.800 20.248  1.00 12.70 ? 82   MET A CG  1 
ATOM   676  S  SD  . MET A 1 82  ? 20.305 38.678 18.644  1.00 15.87 ? 82   MET A SD  1 
ATOM   677  C  CE  . MET A 1 82  ? 21.300 40.135 18.667  1.00 8.90  ? 82   MET A CE  1 
ATOM   678  N  N   . VAL A 1 83  ? 19.752 41.534 22.320  1.00 13.32 ? 83   VAL A N   1 
ATOM   679  C  CA  . VAL A 1 83  ? 20.917 41.875 23.131  1.00 11.92 ? 83   VAL A CA  1 
ATOM   680  C  C   . VAL A 1 83  ? 20.544 41.977 24.610  1.00 15.34 ? 83   VAL A C   1 
ATOM   681  O  O   . VAL A 1 83  ? 21.235 41.441 25.481  1.00 19.51 ? 83   VAL A O   1 
ATOM   682  C  CB  . VAL A 1 83  ? 21.559 43.210 22.677  1.00 10.26 ? 83   VAL A CB  1 
ATOM   683  C  CG1 . VAL A 1 83  ? 22.680 43.600 23.624  1.00 10.16 ? 83   VAL A CG1 1 
ATOM   684  C  CG2 . VAL A 1 83  ? 22.104 43.085 21.267  1.00 6.74  ? 83   VAL A CG2 1 
ATOM   685  N  N   . THR A 1 84  ? 19.429 42.640 24.887  1.00 16.01 ? 84   THR A N   1 
ATOM   686  C  CA  . THR A 1 84  ? 18.967 42.809 26.254  1.00 16.31 ? 84   THR A CA  1 
ATOM   687  C  C   . THR A 1 84  ? 18.636 41.470 26.905  1.00 14.73 ? 84   THR A C   1 
ATOM   688  O  O   . THR A 1 84  ? 19.140 41.160 27.987  1.00 13.77 ? 84   THR A O   1 
ATOM   689  C  CB  . THR A 1 84  ? 17.738 43.729 26.295  1.00 18.15 ? 84   THR A CB  1 
ATOM   690  O  OG1 . THR A 1 84  ? 18.099 45.015 25.780  1.00 21.24 ? 84   THR A OG1 1 
ATOM   691  C  CG2 . THR A 1 84  ? 17.219 43.878 27.711  1.00 18.57 ? 84   THR A CG2 1 
ATOM   692  N  N   . ARG A 1 85  ? 17.839 40.658 26.215  1.00 12.24 ? 85   ARG A N   1 
ATOM   693  C  CA  . ARG A 1 85  ? 17.435 39.357 26.735  1.00 13.50 ? 85   ARG A CA  1 
ATOM   694  C  C   . ARG A 1 85  ? 18.597 38.391 26.941  1.00 13.47 ? 85   ARG A C   1 
ATOM   695  O  O   . ARG A 1 85  ? 18.625 37.649 27.927  1.00 13.45 ? 85   ARG A O   1 
ATOM   696  C  CB  . ARG A 1 85  ? 16.368 38.752 25.835  1.00 11.43 ? 85   ARG A CB  1 
ATOM   697  C  CG  . ARG A 1 85  ? 15.098 39.558 25.882  1.00 13.61 ? 85   ARG A CG  1 
ATOM   698  C  CD  . ARG A 1 85  ? 14.159 39.208 24.768  1.00 13.36 ? 85   ARG A CD  1 
ATOM   699  N  NE  . ARG A 1 85  ? 13.686 37.837 24.846  1.00 13.36 ? 85   ARG A NE  1 
ATOM   700  C  CZ  . ARG A 1 85  ? 12.880 37.286 23.946  1.00 16.40 ? 85   ARG A CZ  1 
ATOM   701  N  NH1 . ARG A 1 85  ? 12.460 37.995 22.909  1.00 15.38 ? 85   ARG A NH1 1 
ATOM   702  N  NH2 . ARG A 1 85  ? 12.485 36.027 24.081  1.00 18.09 ? 85   ARG A NH2 1 
ATOM   703  N  N   . CYS A 1 86  ? 19.568 38.432 26.033  1.00 12.99 ? 86   CYS A N   1 
ATOM   704  C  CA  . CYS A 1 86  ? 20.747 37.576 26.124  1.00 10.90 ? 86   CYS A CA  1 
ATOM   705  C  C   . CYS A 1 86  ? 21.673 38.011 27.253  1.00 10.04 ? 86   CYS A C   1 
ATOM   706  O  O   . CYS A 1 86  ? 22.107 37.181 28.055  1.00 12.51 ? 86   CYS A O   1 
ATOM   707  C  CB  . CYS A 1 86  ? 21.489 37.536 24.789  1.00 13.40 ? 86   CYS A CB  1 
ATOM   708  S  SG  . CYS A 1 86  ? 20.564 36.651 23.486  1.00 15.39 ? 86   CYS A SG  1 
ATOM   709  N  N   . ASN A 1 87  ? 21.955 39.307 27.347  1.00 11.69 ? 87   ASN A N   1 
ATOM   710  C  CA  . ASN A 1 87  ? 22.809 39.806 28.425  1.00 11.40 ? 87   ASN A CA  1 
ATOM   711  C  C   . ASN A 1 87  ? 22.148 39.482 29.764  1.00 14.32 ? 87   ASN A C   1 
ATOM   712  O  O   . ASN A 1 87  ? 22.822 39.107 30.730  1.00 14.28 ? 87   ASN A O   1 
ATOM   713  C  CB  . ASN A 1 87  ? 23.007 41.320 28.319  1.00 9.11  ? 87   ASN A CB  1 
ATOM   714  C  CG  . ASN A 1 87  ? 24.167 41.702 27.428  1.00 12.00 ? 87   ASN A CG  1 
ATOM   715  O  OD1 . ASN A 1 87  ? 25.173 40.999 27.349  1.00 12.82 ? 87   ASN A OD1 1 
ATOM   716  N  ND2 . ASN A 1 87  ? 24.047 42.843 26.774  1.00 14.19 ? 87   ASN A ND2 1 
ATOM   717  N  N   . ASN A 1 88  ? 20.820 39.597 29.802  1.00 13.87 ? 88   ASN A N   1 
ATOM   718  C  CA  . ASN A 1 88  ? 20.047 39.322 31.013  1.00 18.66 ? 88   ASN A CA  1 
ATOM   719  C  C   . ASN A 1 88  ? 20.152 37.885 31.517  1.00 19.85 ? 88   ASN A C   1 
ATOM   720  O  O   . ASN A 1 88  ? 19.924 37.622 32.694  1.00 27.29 ? 88   ASN A O   1 
ATOM   721  C  CB  . ASN A 1 88  ? 18.581 39.721 30.827  1.00 19.16 ? 88   ASN A CB  1 
ATOM   722  C  CG  . ASN A 1 88  ? 18.354 41.216 31.007  1.00 19.97 ? 88   ASN A CG  1 
ATOM   723  O  OD1 . ASN A 1 88  ? 19.241 41.942 31.454  1.00 23.05 ? 88   ASN A OD1 1 
ATOM   724  N  ND2 . ASN A 1 88  ? 17.162 41.676 30.679  1.00 21.45 ? 88   ASN A ND2 1 
ATOM   725  N  N   . VAL A 1 89  ? 20.470 36.947 30.630  1.00 20.67 ? 89   VAL A N   1 
ATOM   726  C  CA  . VAL A 1 89  ? 20.628 35.556 31.038  1.00 15.61 ? 89   VAL A CA  1 
ATOM   727  C  C   . VAL A 1 89  ? 22.104 35.158 31.050  1.00 18.90 ? 89   VAL A C   1 
ATOM   728  O  O   . VAL A 1 89  ? 22.436 33.973 31.067  1.00 21.46 ? 89   VAL A O   1 
ATOM   729  C  CB  . VAL A 1 89  ? 19.817 34.576 30.158  1.00 15.03 ? 89   VAL A CB  1 
ATOM   730  C  CG1 . VAL A 1 89  ? 18.336 34.721 30.451  1.00 13.32 ? 89   VAL A CG1 1 
ATOM   731  C  CG2 . VAL A 1 89  ? 20.104 34.808 28.684  1.00 10.79 ? 89   VAL A CG2 1 
ATOM   732  N  N   . GLY A 1 90  ? 22.986 36.154 31.008  1.00 17.72 ? 90   GLY A N   1 
ATOM   733  C  CA  . GLY A 1 90  ? 24.414 35.890 31.054  1.00 14.52 ? 90   GLY A CA  1 
ATOM   734  C  C   . GLY A 1 90  ? 25.117 35.538 29.756  1.00 14.85 ? 90   GLY A C   1 
ATOM   735  O  O   . GLY A 1 90  ? 26.291 35.179 29.781  1.00 15.71 ? 90   GLY A O   1 
ATOM   736  N  N   . VAL A 1 91  ? 24.421 35.654 28.629  1.00 12.54 ? 91   VAL A N   1 
ATOM   737  C  CA  . VAL A 1 91  ? 25.001 35.347 27.328  1.00 9.89  ? 91   VAL A CA  1 
ATOM   738  C  C   . VAL A 1 91  ? 25.314 36.648 26.579  1.00 13.59 ? 91   VAL A C   1 
ATOM   739  O  O   . VAL A 1 91  ? 24.417 37.447 26.303  1.00 11.72 ? 91   VAL A O   1 
ATOM   740  C  CB  . VAL A 1 91  ? 24.047 34.477 26.492  1.00 9.14  ? 91   VAL A CB  1 
ATOM   741  C  CG1 . VAL A 1 91  ? 24.717 34.054 25.195  1.00 6.49  ? 91   VAL A CG1 1 
ATOM   742  C  CG2 . VAL A 1 91  ? 23.624 33.251 27.292  1.00 8.27  ? 91   VAL A CG2 1 
ATOM   743  N  N   . ARG A 1 92  ? 26.585 36.851 26.250  1.00 12.47 ? 92   ARG A N   1 
ATOM   744  C  CA  . ARG A 1 92  ? 27.019 38.059 25.559  1.00 10.82 ? 92   ARG A CA  1 
ATOM   745  C  C   . ARG A 1 92  ? 26.791 37.965 24.051  1.00 11.96 ? 92   ARG A C   1 
ATOM   746  O  O   . ARG A 1 92  ? 26.625 36.879 23.505  1.00 13.21 ? 92   ARG A O   1 
ATOM   747  C  CB  . ARG A 1 92  ? 28.499 38.324 25.828  1.00 10.24 ? 92   ARG A CB  1 
ATOM   748  C  CG  . ARG A 1 92  ? 28.974 37.983 27.235  1.00 13.42 ? 92   ARG A CG  1 
ATOM   749  C  CD  . ARG A 1 92  ? 28.966 39.161 28.176  1.00 13.88 ? 92   ARG A CD  1 
ATOM   750  N  NE  . ARG A 1 92  ? 27.657 39.418 28.756  1.00 21.89 ? 92   ARG A NE  1 
ATOM   751  C  CZ  . ARG A 1 92  ? 27.445 39.653 30.051  1.00 22.65 ? 92   ARG A CZ  1 
ATOM   752  N  NH1 . ARG A 1 92  ? 28.458 39.655 30.910  1.00 18.84 ? 92   ARG A NH1 1 
ATOM   753  N  NH2 . ARG A 1 92  ? 26.214 39.878 30.489  1.00 22.43 ? 92   ARG A NH2 1 
ATOM   754  N  N   . ILE A 1 93  ? 26.801 39.112 23.382  1.00 13.85 ? 93   ILE A N   1 
ATOM   755  C  CA  . ILE A 1 93  ? 26.602 39.176 21.943  1.00 10.28 ? 93   ILE A CA  1 
ATOM   756  C  C   . ILE A 1 93  ? 27.809 39.843 21.305  1.00 13.69 ? 93   ILE A C   1 
ATOM   757  O  O   . ILE A 1 93  ? 28.247 40.906 21.751  1.00 16.19 ? 93   ILE A O   1 
ATOM   758  C  CB  . ILE A 1 93  ? 25.354 39.993 21.581  1.00 9.15  ? 93   ILE A CB  1 
ATOM   759  C  CG1 . ILE A 1 93  ? 24.101 39.290 22.100  1.00 10.80 ? 93   ILE A CG1 1 
ATOM   760  C  CG2 . ILE A 1 93  ? 25.273 40.196 20.069  1.00 4.78  ? 93   ILE A CG2 1 
ATOM   761  C  CD1 . ILE A 1 93  ? 23.892 37.908 21.521  1.00 13.11 ? 93   ILE A CD1 1 
ATOM   762  N  N   . TYR A 1 94  ? 28.343 39.211 20.265  1.00 10.55 ? 94   TYR A N   1 
ATOM   763  C  CA  . TYR A 1 94  ? 29.500 39.720 19.546  1.00 6.64  ? 94   TYR A CA  1 
ATOM   764  C  C   . TYR A 1 94  ? 29.064 39.947 18.117  1.00 7.40  ? 94   TYR A C   1 
ATOM   765  O  O   . TYR A 1 94  ? 28.480 39.056 17.495  1.00 9.29  ? 94   TYR A O   1 
ATOM   766  C  CB  . TYR A 1 94  ? 30.637 38.703 19.609  1.00 8.03  ? 94   TYR A CB  1 
ATOM   767  C  CG  . TYR A 1 94  ? 31.029 38.390 21.030  1.00 5.97  ? 94   TYR A CG  1 
ATOM   768  C  CD1 . TYR A 1 94  ? 31.870 39.242 21.746  1.00 6.65  ? 94   TYR A CD1 1 
ATOM   769  C  CD2 . TYR A 1 94  ? 30.498 37.287 21.686  1.00 5.07  ? 94   TYR A CD2 1 
ATOM   770  C  CE1 . TYR A 1 94  ? 32.164 39.003 23.090  1.00 6.39  ? 94   TYR A CE1 1 
ATOM   771  C  CE2 . TYR A 1 94  ? 30.782 37.041 23.026  1.00 2.26  ? 94   TYR A CE2 1 
ATOM   772  C  CZ  . TYR A 1 94  ? 31.610 37.901 23.721  1.00 5.36  ? 94   TYR A CZ  1 
ATOM   773  O  OH  . TYR A 1 94  ? 31.861 37.661 25.052  1.00 9.57  ? 94   TYR A OH  1 
ATOM   774  N  N   . VAL A 1 95  ? 29.339 41.137 17.594  1.00 8.77  ? 95   VAL A N   1 
ATOM   775  C  CA  . VAL A 1 95  ? 28.927 41.483 16.237  1.00 7.21  ? 95   VAL A CA  1 
ATOM   776  C  C   . VAL A 1 95  ? 29.990 41.306 15.161  1.00 6.35  ? 95   VAL A C   1 
ATOM   777  O  O   . VAL A 1 95  ? 31.165 41.612 15.365  1.00 7.37  ? 95   VAL A O   1 
ATOM   778  C  CB  . VAL A 1 95  ? 28.364 42.930 16.191  1.00 5.74  ? 95   VAL A CB  1 
ATOM   779  C  CG1 . VAL A 1 95  ? 28.153 43.389 14.769  1.00 8.77  ? 95   VAL A CG1 1 
ATOM   780  C  CG2 . VAL A 1 95  ? 27.047 42.982 16.922  1.00 6.79  ? 95   VAL A CG2 1 
ATOM   781  N  N   . ASP A 1 96  ? 29.567 40.805 14.008  1.00 7.42  ? 96   ASP A N   1 
ATOM   782  C  CA  . ASP A 1 96  ? 30.466 40.624 12.883  1.00 7.19  ? 96   ASP A CA  1 
ATOM   783  C  C   . ASP A 1 96  ? 30.492 42.001 12.217  1.00 10.19 ? 96   ASP A C   1 
ATOM   784  O  O   . ASP A 1 96  ? 29.515 42.407 11.570  1.00 9.43  ? 96   ASP A O   1 
ATOM   785  C  CB  . ASP A 1 96  ? 29.898 39.562 11.930  1.00 10.02 ? 96   ASP A CB  1 
ATOM   786  C  CG  . ASP A 1 96  ? 30.896 39.108 10.866  1.00 12.74 ? 96   ASP A CG  1 
ATOM   787  O  OD1 . ASP A 1 96  ? 31.882 39.825 10.582  1.00 10.39 ? 96   ASP A OD1 1 
ATOM   788  O  OD2 . ASP A 1 96  ? 30.682 38.018 10.300  1.00 13.76 ? 96   ASP A OD2 1 
ATOM   789  N  N   . ALA A 1 97  ? 31.578 42.738 12.433  1.00 8.57  ? 97   ALA A N   1 
ATOM   790  C  CA  . ALA A 1 97  ? 31.735 44.079 11.870  1.00 6.35  ? 97   ALA A CA  1 
ATOM   791  C  C   . ALA A 1 97  ? 32.404 44.074 10.492  1.00 9.97  ? 97   ALA A C   1 
ATOM   792  O  O   . ALA A 1 97  ? 33.610 43.823 10.381  1.00 7.94  ? 97   ALA A O   1 
ATOM   793  C  CB  . ALA A 1 97  ? 32.536 44.956 12.836  1.00 6.31  ? 97   ALA A CB  1 
ATOM   794  N  N   . VAL A 1 98  ? 31.626 44.347 9.446   1.00 10.79 ? 98   VAL A N   1 
ATOM   795  C  CA  . VAL A 1 98  ? 32.150 44.394 8.073   1.00 11.43 ? 98   VAL A CA  1 
ATOM   796  C  C   . VAL A 1 98  ? 32.480 45.869 7.811   1.00 12.12 ? 98   VAL A C   1 
ATOM   797  O  O   . VAL A 1 98  ? 31.615 46.649 7.409   1.00 12.70 ? 98   VAL A O   1 
ATOM   798  C  CB  . VAL A 1 98  ? 31.094 43.881 7.039   1.00 9.67  ? 98   VAL A CB  1 
ATOM   799  C  CG1 . VAL A 1 98  ? 31.722 43.745 5.675   1.00 9.47  ? 98   VAL A CG1 1 
ATOM   800  C  CG2 . VAL A 1 98  ? 30.523 42.533 7.474   1.00 6.03  ? 98   VAL A CG2 1 
ATOM   801  N  N   . ILE A 1 99  ? 33.734 46.241 8.060   1.00 10.97 ? 99   ILE A N   1 
ATOM   802  C  CA  . ILE A 1 99  ? 34.180 47.627 7.927   1.00 10.21 ? 99   ILE A CA  1 
ATOM   803  C  C   . ILE A 1 99  ? 35.285 47.947 6.914   1.00 12.16 ? 99   ILE A C   1 
ATOM   804  O  O   . ILE A 1 99  ? 35.685 49.104 6.792   1.00 15.07 ? 99   ILE A O   1 
ATOM   805  C  CB  . ILE A 1 99  ? 34.641 48.167 9.306   1.00 10.92 ? 99   ILE A CB  1 
ATOM   806  C  CG1 . ILE A 1 99  ? 35.864 47.378 9.792   1.00 7.24  ? 99   ILE A CG1 1 
ATOM   807  C  CG2 . ILE A 1 99  ? 33.500 48.054 10.331  1.00 7.36  ? 99   ILE A CG2 1 
ATOM   808  C  CD1 . ILE A 1 99  ? 36.433 47.847 11.125  1.00 4.91  ? 99   ILE A CD1 1 
ATOM   809  N  N   . ASN A 1 100 ? 35.797 46.950 6.201   1.00 10.81 ? 100  ASN A N   1 
ATOM   810  C  CA  . ASN A 1 100 ? 36.871 47.200 5.234   1.00 9.65  ? 100  ASN A CA  1 
ATOM   811  C  C   . ASN A 1 100 ? 36.336 47.655 3.895   1.00 10.33 ? 100  ASN A C   1 
ATOM   812  O  O   . ASN A 1 100 ? 37.052 48.278 3.109   1.00 11.13 ? 100  ASN A O   1 
ATOM   813  C  CB  . ASN A 1 100 ? 37.727 45.937 5.026   1.00 9.81  ? 100  ASN A CB  1 
ATOM   814  C  CG  . ASN A 1 100 ? 38.542 45.972 3.727   1.00 10.27 ? 100  ASN A CG  1 
ATOM   815  O  OD1 . ASN A 1 100 ? 39.606 46.590 3.656   1.00 14.45 ? 100  ASN A OD1 1 
ATOM   816  N  ND2 . ASN A 1 100 ? 38.052 45.287 2.703   1.00 9.93  ? 100  ASN A ND2 1 
ATOM   817  N  N   . HIS A 1 101 ? 35.050 47.431 3.666   1.00 9.99  ? 101  HIS A N   1 
ATOM   818  C  CA  . HIS A 1 101 ? 34.479 47.749 2.372   1.00 10.25 ? 101  HIS A CA  1 
ATOM   819  C  C   . HIS A 1 101 ? 32.971 47.904 2.400   1.00 11.34 ? 101  HIS A C   1 
ATOM   820  O  O   . HIS A 1 101 ? 32.321 47.666 3.424   1.00 11.84 ? 101  HIS A O   1 
ATOM   821  C  CB  . HIS A 1 101 ? 34.816 46.590 1.433   1.00 8.76  ? 101  HIS A CB  1 
ATOM   822  C  CG  . HIS A 1 101 ? 34.465 45.248 2.003   1.00 11.11 ? 101  HIS A CG  1 
ATOM   823  N  ND1 . HIS A 1 101 ? 33.175 44.769 2.033   1.00 13.32 ? 101  HIS A ND1 1 
ATOM   824  C  CD2 . HIS A 1 101 ? 35.223 44.319 2.636   1.00 10.89 ? 101  HIS A CD2 1 
ATOM   825  C  CE1 . HIS A 1 101 ? 33.150 43.609 2.665   1.00 12.24 ? 101  HIS A CE1 1 
ATOM   826  N  NE2 . HIS A 1 101 ? 34.380 43.315 3.041   1.00 10.28 ? 101  HIS A NE2 1 
ATOM   827  N  N   . MET A 1 102 ? 32.432 48.286 1.246   1.00 11.67 ? 102  MET A N   1 
ATOM   828  C  CA  . MET A 1 102 ? 30.999 48.426 1.045   1.00 16.51 ? 102  MET A CA  1 
ATOM   829  C  C   . MET A 1 102 ? 30.638 47.328 0.030   1.00 17.49 ? 102  MET A C   1 
ATOM   830  O  O   . MET A 1 102 ? 31.333 46.312 -0.022  1.00 21.52 ? 102  MET A O   1 
ATOM   831  C  CB  . MET A 1 102 ? 30.634 49.826 0.540   1.00 13.95 ? 102  MET A CB  1 
ATOM   832  C  CG  . MET A 1 102 ? 30.852 50.935 1.568   1.00 12.43 ? 102  MET A CG  1 
ATOM   833  S  SD  . MET A 1 102 ? 30.016 50.644 3.148   1.00 13.36 ? 102  MET A SD  1 
ATOM   834  C  CE  . MET A 1 102 ? 28.431 51.230 2.799   1.00 7.50  ? 102  MET A CE  1 
ATOM   835  N  N   . CYS A 1 103 ? 29.595 47.516 -0.776  1.00 17.74 ? 103  CYS A N   1 
ATOM   836  C  CA  . CYS A 1 103 ? 29.184 46.486 -1.737  1.00 17.18 ? 103  CYS A CA  1 
ATOM   837  C  C   . CYS A 1 103 ? 30.064 46.348 -2.988  1.00 18.04 ? 103  CYS A C   1 
ATOM   838  O  O   . CYS A 1 103 ? 31.025 47.105 -3.185  1.00 18.73 ? 103  CYS A O   1 
ATOM   839  C  CB  . CYS A 1 103 ? 27.719 46.684 -2.139  1.00 16.51 ? 103  CYS A CB  1 
ATOM   840  S  SG  . CYS A 1 103 ? 27.427 48.071 -3.246  1.00 20.13 ? 103  CYS A SG  1 
ATOM   841  N  N   . GLY A 1 104 ? 29.746 45.354 -3.815  1.00 18.04 ? 104  GLY A N   1 
ATOM   842  C  CA  . GLY A 1 104 ? 30.510 45.125 -5.030  1.00 20.23 ? 104  GLY A CA  1 
ATOM   843  C  C   . GLY A 1 104 ? 30.459 46.320 -5.960  1.00 18.18 ? 104  GLY A C   1 
ATOM   844  O  O   . GLY A 1 104 ? 29.386 46.858 -6.217  1.00 19.34 ? 104  GLY A O   1 
ATOM   845  N  N   . SER A 1 105 ? 31.612 46.721 -6.482  1.00 19.84 ? 105  SER A N   1 
ATOM   846  C  CA  . SER A 1 105 ? 31.695 47.868 -7.381  1.00 25.83 ? 105  SER A CA  1 
ATOM   847  C  C   . SER A 1 105 ? 30.868 47.686 -8.647  1.00 29.32 ? 105  SER A C   1 
ATOM   848  O  O   . SER A 1 105 ? 30.478 48.666 -9.293  1.00 31.31 ? 105  SER A O   1 
ATOM   849  C  CB  . SER A 1 105 ? 33.151 48.145 -7.756  1.00 23.70 ? 105  SER A CB  1 
ATOM   850  O  OG  . SER A 1 105 ? 33.751 47.012 -8.356  1.00 27.15 ? 105  SER A OG  1 
ATOM   851  N  N   . GLY A 1 106 ? 30.608 46.429 -8.997  1.00 30.43 ? 106  GLY A N   1 
ATOM   852  C  CA  . GLY A 1 106 ? 29.833 46.127 -10.182 1.00 29.15 ? 106  GLY A CA  1 
ATOM   853  C  C   . GLY A 1 106 ? 28.333 46.091 -9.958  1.00 28.77 ? 106  GLY A C   1 
ATOM   854  O  O   . GLY A 1 106 ? 27.571 45.970 -10.917 1.00 33.91 ? 106  GLY A O   1 
ATOM   855  N  N   . ALA A 1 107 ? 27.898 46.180 -8.706  1.00 28.70 ? 107  ALA A N   1 
ATOM   856  C  CA  . ALA A 1 107 ? 26.471 46.151 -8.401  1.00 31.05 ? 107  ALA A CA  1 
ATOM   857  C  C   . ALA A 1 107 ? 25.731 47.303 -9.086  1.00 31.60 ? 107  ALA A C   1 
ATOM   858  O  O   . ALA A 1 107 ? 26.317 48.346 -9.398  1.00 34.46 ? 107  ALA A O   1 
ATOM   859  C  CB  . ALA A 1 107 ? 26.253 46.198 -6.907  1.00 28.01 ? 107  ALA A CB  1 
ATOM   860  N  N   . ALA A 1 108 ? 24.440 47.112 -9.323  1.00 32.91 ? 108  ALA A N   1 
ATOM   861  C  CA  . ALA A 1 108 ? 23.638 48.130 -9.983  1.00 31.21 ? 108  ALA A CA  1 
ATOM   862  C  C   . ALA A 1 108 ? 23.085 49.159 -9.008  1.00 31.08 ? 108  ALA A C   1 
ATOM   863  O  O   . ALA A 1 108 ? 22.755 48.840 -7.861  1.00 33.29 ? 108  ALA A O   1 
ATOM   864  C  CB  . ALA A 1 108 ? 22.506 47.483 -10.763 1.00 31.78 ? 108  ALA A CB  1 
ATOM   865  N  N   . ALA A 1 109 ? 22.999 50.398 -9.476  1.00 29.50 ? 109  ALA A N   1 
ATOM   866  C  CA  . ALA A 1 109 ? 22.474 51.494 -8.674  1.00 29.05 ? 109  ALA A CA  1 
ATOM   867  C  C   . ALA A 1 109 ? 20.995 51.241 -8.432  1.00 27.82 ? 109  ALA A C   1 
ATOM   868  O  O   . ALA A 1 109 ? 20.306 50.702 -9.307  1.00 28.79 ? 109  ALA A O   1 
ATOM   869  C  CB  . ALA A 1 109 ? 22.657 52.808 -9.414  1.00 28.65 ? 109  ALA A CB  1 
ATOM   870  N  N   . GLY A 1 110 ? 20.510 51.588 -7.246  1.00 27.04 ? 110  GLY A N   1 
ATOM   871  C  CA  . GLY A 1 110 ? 19.105 51.382 -6.961  1.00 25.26 ? 110  GLY A CA  1 
ATOM   872  C  C   . GLY A 1 110 ? 18.784 51.173 -5.499  1.00 27.05 ? 110  GLY A C   1 
ATOM   873  O  O   . GLY A 1 110 ? 19.589 51.490 -4.622  1.00 30.39 ? 110  GLY A O   1 
ATOM   874  N  N   . THR A 1 111 ? 17.584 50.663 -5.240  1.00 29.67 ? 111  THR A N   1 
ATOM   875  C  CA  . THR A 1 111 ? 17.133 50.399 -3.883  1.00 29.58 ? 111  THR A CA  1 
ATOM   876  C  C   . THR A 1 111 ? 16.965 48.901 -3.606  1.00 29.43 ? 111  THR A C   1 
ATOM   877  O  O   . THR A 1 111 ? 16.149 48.501 -2.766  1.00 30.88 ? 111  THR A O   1 
ATOM   878  C  CB  . THR A 1 111 ? 15.824 51.163 -3.565  1.00 31.69 ? 111  THR A CB  1 
ATOM   879  O  OG1 . THR A 1 111 ? 14.899 51.019 -4.652  1.00 35.19 ? 111  THR A OG1 1 
ATOM   880  C  CG2 . THR A 1 111 ? 16.111 52.641 -3.336  1.00 28.78 ? 111  THR A CG2 1 
ATOM   881  N  N   . GLY A 1 112 ? 17.716 48.073 -4.334  1.00 24.89 ? 112  GLY A N   1 
ATOM   882  C  CA  . GLY A 1 112 ? 17.660 46.636 -4.116  1.00 20.92 ? 112  GLY A CA  1 
ATOM   883  C  C   . GLY A 1 112 ? 18.554 46.348 -2.921  1.00 17.76 ? 112  GLY A C   1 
ATOM   884  O  O   . GLY A 1 112 ? 19.626 45.760 -3.056  1.00 16.14 ? 112  GLY A O   1 
ATOM   885  N  N   . THR A 1 113 ? 18.109 46.793 -1.751  1.00 14.17 ? 113  THR A N   1 
ATOM   886  C  CA  . THR A 1 113 ? 18.855 46.649 -0.516  1.00 13.64 ? 113  THR A CA  1 
ATOM   887  C  C   . THR A 1 113 ? 17.902 46.130 0.563   1.00 16.33 ? 113  THR A C   1 
ATOM   888  O  O   . THR A 1 113 ? 16.686 46.265 0.429   1.00 17.58 ? 113  THR A O   1 
ATOM   889  C  CB  . THR A 1 113 ? 19.438 48.019 -0.107  1.00 15.41 ? 113  THR A CB  1 
ATOM   890  O  OG1 . THR A 1 113 ? 18.369 48.939 0.139   1.00 14.70 ? 113  THR A OG1 1 
ATOM   891  C  CG2 . THR A 1 113 ? 20.311 48.592 -1.226  1.00 7.01  ? 113  THR A CG2 1 
ATOM   892  N  N   . THR A 1 114 ? 18.436 45.555 1.635   1.00 17.76 ? 114  THR A N   1 
ATOM   893  C  CA  . THR A 1 114 ? 17.585 45.001 2.680   1.00 18.20 ? 114  THR A CA  1 
ATOM   894  C  C   . THR A 1 114 ? 16.710 46.000 3.420   1.00 21.99 ? 114  THR A C   1 
ATOM   895  O  O   . THR A 1 114 ? 15.723 45.613 4.040   1.00 24.76 ? 114  THR A O   1 
ATOM   896  C  CB  . THR A 1 114 ? 18.388 44.165 3.691   1.00 16.84 ? 114  THR A CB  1 
ATOM   897  O  OG1 . THR A 1 114 ? 19.456 44.950 4.238   1.00 19.86 ? 114  THR A OG1 1 
ATOM   898  C  CG2 . THR A 1 114 ? 18.960 42.935 3.010   1.00 16.72 ? 114  THR A CG2 1 
ATOM   899  N  N   . CYS A 1 115 ? 17.049 47.282 3.347   1.00 25.78 ? 115  CYS A N   1 
ATOM   900  C  CA  . CYS A 1 115 ? 16.243 48.282 4.039   1.00 27.36 ? 115  CYS A CA  1 
ATOM   901  C  C   . CYS A 1 115 ? 15.674 49.367 3.125   1.00 26.39 ? 115  CYS A C   1 
ATOM   902  O  O   . CYS A 1 115 ? 14.984 50.275 3.590   1.00 24.72 ? 115  CYS A O   1 
ATOM   903  C  CB  . CYS A 1 115 ? 17.039 48.917 5.178   1.00 28.65 ? 115  CYS A CB  1 
ATOM   904  S  SG  . CYS A 1 115 ? 16.014 49.319 6.624   1.00 32.37 ? 115  CYS A SG  1 
ATOM   905  N  N   . GLY A 1 116 ? 15.961 49.275 1.829   1.00 25.78 ? 116  GLY A N   1 
ATOM   906  C  CA  . GLY A 1 116 ? 15.445 50.258 0.894   1.00 26.61 ? 116  GLY A CA  1 
ATOM   907  C  C   . GLY A 1 116 ? 16.327 51.473 0.668   1.00 27.48 ? 116  GLY A C   1 
ATOM   908  O  O   . GLY A 1 116 ? 15.962 52.368 -0.099  1.00 31.37 ? 116  GLY A O   1 
ATOM   909  N  N   . SER A 1 117 ? 17.468 51.528 1.351   1.00 25.94 ? 117  SER A N   1 
ATOM   910  C  CA  . SER A 1 117 ? 18.399 52.639 1.186   1.00 23.67 ? 117  SER A CA  1 
ATOM   911  C  C   . SER A 1 117 ? 18.886 52.652 -0.252  1.00 23.47 ? 117  SER A C   1 
ATOM   912  O  O   . SER A 1 117 ? 19.096 51.593 -0.857  1.00 23.00 ? 117  SER A O   1 
ATOM   913  C  CB  . SER A 1 117 ? 19.617 52.487 2.106   1.00 19.85 ? 117  SER A CB  1 
ATOM   914  O  OG  . SER A 1 117 ? 19.300 52.756 3.458   1.00 22.66 ? 117  SER A OG  1 
ATOM   915  N  N   . TYR A 1 118 ? 19.048 53.849 -0.800  1.00 22.95 ? 118  TYR A N   1 
ATOM   916  C  CA  . TYR A 1 118 ? 19.541 53.989 -2.157  1.00 22.19 ? 118  TYR A CA  1 
ATOM   917  C  C   . TYR A 1 118 ? 21.057 53.930 -2.119  1.00 21.87 ? 118  TYR A C   1 
ATOM   918  O  O   . TYR A 1 118 ? 21.678 54.295 -1.118  1.00 25.78 ? 118  TYR A O   1 
ATOM   919  C  CB  . TYR A 1 118 ? 19.114 55.337 -2.754  1.00 20.46 ? 118  TYR A CB  1 
ATOM   920  C  CG  . TYR A 1 118 ? 19.714 55.614 -4.121  1.00 19.34 ? 118  TYR A CG  1 
ATOM   921  C  CD1 . TYR A 1 118 ? 19.099 55.147 -5.278  1.00 16.87 ? 118  TYR A CD1 1 
ATOM   922  C  CD2 . TYR A 1 118 ? 20.925 56.300 -4.252  1.00 21.01 ? 118  TYR A CD2 1 
ATOM   923  C  CE1 . TYR A 1 118 ? 19.671 55.347 -6.530  1.00 17.50 ? 118  TYR A CE1 1 
ATOM   924  C  CE2 . TYR A 1 118 ? 21.509 56.503 -5.505  1.00 18.87 ? 118  TYR A CE2 1 
ATOM   925  C  CZ  . TYR A 1 118 ? 20.873 56.020 -6.637  1.00 19.46 ? 118  TYR A CZ  1 
ATOM   926  O  OH  . TYR A 1 118 ? 21.441 56.198 -7.879  1.00 22.74 ? 118  TYR A OH  1 
ATOM   927  N  N   . CYS A 1 119 ? 21.651 53.459 -3.204  1.00 22.08 ? 119  CYS A N   1 
ATOM   928  C  CA  . CYS A 1 119 ? 23.097 53.420 -3.319  1.00 23.22 ? 119  CYS A CA  1 
ATOM   929  C  C   . CYS A 1 119 ? 23.420 53.309 -4.795  1.00 22.68 ? 119  CYS A C   1 
ATOM   930  O  O   . CYS A 1 119 ? 22.602 52.820 -5.579  1.00 24.73 ? 119  CYS A O   1 
ATOM   931  C  CB  . CYS A 1 119 ? 23.691 52.239 -2.546  1.00 22.63 ? 119  CYS A CB  1 
ATOM   932  S  SG  . CYS A 1 119 ? 23.368 50.637 -3.264  1.00 27.22 ? 119  CYS A SG  1 
ATOM   933  N  N   . ASN A 1 120 ? 24.575 53.835 -5.184  1.00 21.82 ? 120  ASN A N   1 
ATOM   934  C  CA  . ASN A 1 120 ? 25.025 53.779 -6.569  1.00 23.11 ? 120  ASN A CA  1 
ATOM   935  C  C   . ASN A 1 120 ? 26.494 53.379 -6.530  1.00 23.14 ? 120  ASN A C   1 
ATOM   936  O  O   . ASN A 1 120 ? 27.380 54.238 -6.458  1.00 21.28 ? 120  ASN A O   1 
ATOM   937  C  CB  . ASN A 1 120 ? 24.867 55.148 -7.237  1.00 26.17 ? 120  ASN A CB  1 
ATOM   938  C  CG  . ASN A 1 120 ? 25.289 55.143 -8.702  1.00 27.99 ? 120  ASN A CG  1 
ATOM   939  O  OD1 . ASN A 1 120 ? 25.819 54.159 -9.217  1.00 28.11 ? 120  ASN A OD1 1 
ATOM   940  N  ND2 . ASN A 1 120 ? 25.054 56.257 -9.376  1.00 31.98 ? 120  ASN A ND2 1 
ATOM   941  N  N   . PRO A 1 121 ? 26.770 52.063 -6.525  1.00 23.98 ? 121  PRO A N   1 
ATOM   942  C  CA  . PRO A 1 121 ? 28.135 51.526 -6.484  1.00 22.32 ? 121  PRO A CA  1 
ATOM   943  C  C   . PRO A 1 121 ? 29.036 52.088 -7.576  1.00 24.08 ? 121  PRO A C   1 
ATOM   944  O  O   . PRO A 1 121 ? 30.207 52.384 -7.324  1.00 27.40 ? 121  PRO A O   1 
ATOM   945  C  CB  . PRO A 1 121 ? 27.911 50.025 -6.651  1.00 20.90 ? 121  PRO A CB  1 
ATOM   946  C  CG  . PRO A 1 121 ? 26.599 49.817 -5.970  1.00 21.19 ? 121  PRO A CG  1 
ATOM   947  C  CD  . PRO A 1 121 ? 25.783 50.967 -6.510  1.00 22.71 ? 121  PRO A CD  1 
ATOM   948  N  N   . GLY A 1 122 ? 28.474 52.282 -8.766  1.00 26.78 ? 122  GLY A N   1 
ATOM   949  C  CA  . GLY A 1 122 ? 29.238 52.813 -9.885  1.00 26.13 ? 122  GLY A CA  1 
ATOM   950  C  C   . GLY A 1 122 ? 29.898 54.151 -9.608  1.00 29.93 ? 122  GLY A C   1 
ATOM   951  O  O   . GLY A 1 122 ? 31.044 54.371 -10.007 1.00 31.35 ? 122  GLY A O   1 
ATOM   952  N  N   . SER A 1 123 ? 29.180 55.049 -8.936  1.00 32.76 ? 123  SER A N   1 
ATOM   953  C  CA  . SER A 1 123 ? 29.711 56.374 -8.606  1.00 34.83 ? 123  SER A CA  1 
ATOM   954  C  C   . SER A 1 123 ? 30.167 56.480 -7.150  1.00 32.83 ? 123  SER A C   1 
ATOM   955  O  O   . SER A 1 123 ? 30.501 57.570 -6.674  1.00 33.31 ? 123  SER A O   1 
ATOM   956  C  CB  . SER A 1 123 ? 28.671 57.462 -8.903  1.00 37.08 ? 123  SER A CB  1 
ATOM   957  O  OG  . SER A 1 123 ? 28.407 57.570 -10.294 1.00 43.56 ? 123  SER A OG  1 
ATOM   958  N  N   . ARG A 1 124 ? 30.199 55.346 -6.454  1.00 30.84 ? 124  ARG A N   1 
ATOM   959  C  CA  . ARG A 1 124 ? 30.598 55.310 -5.051  1.00 28.74 ? 124  ARG A CA  1 
ATOM   960  C  C   . ARG A 1 124 ? 29.681 56.191 -4.197  1.00 27.24 ? 124  ARG A C   1 
ATOM   961  O  O   . ARG A 1 124 ? 30.141 56.902 -3.303  1.00 28.29 ? 124  ARG A O   1 
ATOM   962  C  CB  . ARG A 1 124 ? 32.056 55.752 -4.884  1.00 29.37 ? 124  ARG A CB  1 
ATOM   963  C  CG  . ARG A 1 124 ? 33.103 54.695 -5.213  1.00 29.00 ? 124  ARG A CG  1 
ATOM   964  C  CD  . ARG A 1 124 ? 33.252 54.495 -6.696  1.00 33.75 ? 124  ARG A CD  1 
ATOM   965  N  NE  . ARG A 1 124 ? 34.374 53.618 -7.026  1.00 35.17 ? 124  ARG A NE  1 
ATOM   966  C  CZ  . ARG A 1 124 ? 34.344 52.693 -7.985  1.00 36.69 ? 124  ARG A CZ  1 
ATOM   967  N  NH1 . ARG A 1 124 ? 33.239 52.500 -8.699  1.00 36.36 ? 124  ARG A NH1 1 
ATOM   968  N  NH2 . ARG A 1 124 ? 35.413 51.945 -8.222  1.00 34.61 ? 124  ARG A NH2 1 
ATOM   969  N  N   . GLU A 1 125 ? 28.388 56.165 -4.506  1.00 27.20 ? 125  GLU A N   1 
ATOM   970  C  CA  . GLU A 1 125 ? 27.398 56.946 -3.774  1.00 25.97 ? 125  GLU A CA  1 
ATOM   971  C  C   . GLU A 1 125 ? 26.681 56.070 -2.766  1.00 23.85 ? 125  GLU A C   1 
ATOM   972  O  O   . GLU A 1 125 ? 25.983 55.125 -3.141  1.00 26.02 ? 125  GLU A O   1 
ATOM   973  C  CB  . GLU A 1 125 ? 26.334 57.508 -4.707  1.00 31.52 ? 125  GLU A CB  1 
ATOM   974  C  CG  . GLU A 1 125 ? 26.737 58.666 -5.583  1.00 41.08 ? 125  GLU A CG  1 
ATOM   975  C  CD  . GLU A 1 125 ? 25.560 59.161 -6.419  1.00 46.90 ? 125  GLU A CD  1 
ATOM   976  O  OE1 . GLU A 1 125 ? 24.522 59.535 -5.827  1.00 49.64 ? 125  GLU A OE1 1 
ATOM   977  O  OE2 . GLU A 1 125 ? 25.660 59.152 -7.665  1.00 50.26 ? 125  GLU A OE2 1 
ATOM   978  N  N   . PHE A 1 126 ? 26.849 56.383 -1.491  1.00 19.00 ? 126  PHE A N   1 
ATOM   979  C  CA  . PHE A 1 126 ? 26.182 55.647 -0.432  1.00 16.42 ? 126  PHE A CA  1 
ATOM   980  C  C   . PHE A 1 126 ? 25.562 56.712 0.468   1.00 17.14 ? 126  PHE A C   1 
ATOM   981  O  O   . PHE A 1 126 ? 26.080 57.036 1.538   1.00 22.51 ? 126  PHE A O   1 
ATOM   982  C  CB  . PHE A 1 126 ? 27.175 54.735 0.300   1.00 14.73 ? 126  PHE A CB  1 
ATOM   983  C  CG  . PHE A 1 126 ? 27.716 53.624 -0.572  1.00 13.29 ? 126  PHE A CG  1 
ATOM   984  C  CD1 . PHE A 1 126 ? 27.040 52.412 -0.678  1.00 11.12 ? 126  PHE A CD1 1 
ATOM   985  C  CD2 . PHE A 1 126 ? 28.867 53.809 -1.329  1.00 9.80  ? 126  PHE A CD2 1 
ATOM   986  C  CE1 . PHE A 1 126 ? 27.497 51.404 -1.530  1.00 9.68  ? 126  PHE A CE1 1 
ATOM   987  C  CE2 . PHE A 1 126 ? 29.334 52.807 -2.185  1.00 12.38 ? 126  PHE A CE2 1 
ATOM   988  C  CZ  . PHE A 1 126 ? 28.642 51.601 -2.285  1.00 11.19 ? 126  PHE A CZ  1 
ATOM   989  N  N   . PRO A 1 127 ? 24.462 57.318 -0.003  1.00 18.43 ? 127  PRO A N   1 
ATOM   990  C  CA  . PRO A 1 127 ? 23.680 58.374 0.647   1.00 19.16 ? 127  PRO A CA  1 
ATOM   991  C  C   . PRO A 1 127 ? 23.309 58.133 2.100   1.00 20.28 ? 127  PRO A C   1 
ATOM   992  O  O   . PRO A 1 127 ? 23.363 59.052 2.911   1.00 24.10 ? 127  PRO A O   1 
ATOM   993  C  CB  . PRO A 1 127 ? 22.427 58.439 -0.219  1.00 16.80 ? 127  PRO A CB  1 
ATOM   994  C  CG  . PRO A 1 127 ? 22.951 58.114 -1.560  1.00 17.64 ? 127  PRO A CG  1 
ATOM   995  C  CD  . PRO A 1 127 ? 23.831 56.937 -1.280  1.00 17.58 ? 127  PRO A CD  1 
ATOM   996  N  N   . ALA A 1 128 ? 22.947 56.900 2.430   1.00 21.08 ? 128  ALA A N   1 
ATOM   997  C  CA  . ALA A 1 128 ? 22.526 56.560 3.785   1.00 18.89 ? 128  ALA A CA  1 
ATOM   998  C  C   . ALA A 1 128 ? 23.597 56.586 4.867   1.00 19.59 ? 128  ALA A C   1 
ATOM   999  O  O   . ALA A 1 128 ? 23.261 56.481 6.048   1.00 21.55 ? 128  ALA A O   1 
ATOM   1000 C  CB  . ALA A 1 128 ? 21.816 55.217 3.788   1.00 21.08 ? 128  ALA A CB  1 
ATOM   1001 N  N   . VAL A 1 129 ? 24.870 56.701 4.485   1.00 19.84 ? 129  VAL A N   1 
ATOM   1002 C  CA  . VAL A 1 129 ? 25.960 56.722 5.472   1.00 19.46 ? 129  VAL A CA  1 
ATOM   1003 C  C   . VAL A 1 129 ? 26.286 58.113 6.046   1.00 22.73 ? 129  VAL A C   1 
ATOM   1004 O  O   . VAL A 1 129 ? 26.113 58.345 7.255   1.00 23.33 ? 129  VAL A O   1 
ATOM   1005 C  CB  . VAL A 1 129 ? 27.249 56.030 4.934   1.00 16.38 ? 129  VAL A CB  1 
ATOM   1006 C  CG1 . VAL A 1 129 ? 28.370 56.146 5.952   1.00 8.66  ? 129  VAL A CG1 1 
ATOM   1007 C  CG2 . VAL A 1 129 ? 26.969 54.561 4.629   1.00 15.21 ? 129  VAL A CG2 1 
ATOM   1008 N  N   . PRO A 1 130 ? 26.728 59.070 5.201   1.00 21.31 ? 130  PRO A N   1 
ATOM   1009 C  CA  . PRO A 1 130 ? 26.951 58.989 3.750   1.00 21.45 ? 130  PRO A CA  1 
ATOM   1010 C  C   . PRO A 1 130 ? 28.414 58.791 3.347   1.00 19.64 ? 130  PRO A C   1 
ATOM   1011 O  O   . PRO A 1 130 ? 29.333 59.187 4.066   1.00 21.08 ? 130  PRO A O   1 
ATOM   1012 C  CB  . PRO A 1 130 ? 26.451 60.347 3.275   1.00 20.40 ? 130  PRO A CB  1 
ATOM   1013 C  CG  . PRO A 1 130 ? 26.973 61.252 4.347   1.00 18.65 ? 130  PRO A CG  1 
ATOM   1014 C  CD  . PRO A 1 130 ? 26.702 60.479 5.636   1.00 20.06 ? 130  PRO A CD  1 
ATOM   1015 N  N   . TYR A 1 131 ? 28.620 58.165 2.193   1.00 15.62 ? 131  TYR A N   1 
ATOM   1016 C  CA  . TYR A 1 131 ? 29.958 57.947 1.656   1.00 15.84 ? 131  TYR A CA  1 
ATOM   1017 C  C   . TYR A 1 131 ? 29.918 58.453 0.225   1.00 17.75 ? 131  TYR A C   1 
ATOM   1018 O  O   . TYR A 1 131 ? 28.870 58.388 -0.432  1.00 18.65 ? 131  TYR A O   1 
ATOM   1019 C  CB  . TYR A 1 131 ? 30.334 56.458 1.650   1.00 15.06 ? 131  TYR A CB  1 
ATOM   1020 C  CG  . TYR A 1 131 ? 30.840 55.908 2.968   1.00 14.49 ? 131  TYR A CG  1 
ATOM   1021 C  CD1 . TYR A 1 131 ? 31.704 56.652 3.782   1.00 10.81 ? 131  TYR A CD1 1 
ATOM   1022 C  CD2 . TYR A 1 131 ? 30.468 54.633 3.394   1.00 11.53 ? 131  TYR A CD2 1 
ATOM   1023 C  CE1 . TYR A 1 131 ? 32.181 56.134 4.988   1.00 10.14 ? 131  TYR A CE1 1 
ATOM   1024 C  CE2 . TYR A 1 131 ? 30.937 54.107 4.595   1.00 8.73  ? 131  TYR A CE2 1 
ATOM   1025 C  CZ  . TYR A 1 131 ? 31.790 54.858 5.388   1.00 10.81 ? 131  TYR A CZ  1 
ATOM   1026 O  OH  . TYR A 1 131 ? 32.244 54.329 6.577   1.00 6.59  ? 131  TYR A OH  1 
ATOM   1027 N  N   . SER A 1 132 ? 31.053 58.946 -0.256  1.00 17.89 ? 132  SER A N   1 
ATOM   1028 C  CA  . SER A 1 132 ? 31.160 59.448 -1.620  1.00 19.99 ? 132  SER A CA  1 
ATOM   1029 C  C   . SER A 1 132 ? 32.457 58.934 -2.214  1.00 19.17 ? 132  SER A C   1 
ATOM   1030 O  O   . SER A 1 132 ? 33.287 58.371 -1.495  1.00 18.61 ? 132  SER A O   1 
ATOM   1031 C  CB  . SER A 1 132 ? 31.148 60.972 -1.632  1.00 23.81 ? 132  SER A CB  1 
ATOM   1032 O  OG  . SER A 1 132 ? 29.927 61.466 -1.108  1.00 35.76 ? 132  SER A OG  1 
ATOM   1033 N  N   . ALA A 1 133 ? 32.659 59.193 -3.501  1.00 18.34 ? 133  ALA A N   1 
ATOM   1034 C  CA  . ALA A 1 133 ? 33.843 58.738 -4.212  1.00 19.20 ? 133  ALA A CA  1 
ATOM   1035 C  C   . ALA A 1 133 ? 35.182 58.938 -3.514  1.00 21.30 ? 133  ALA A C   1 
ATOM   1036 O  O   . ALA A 1 133 ? 36.069 58.100 -3.644  1.00 22.20 ? 133  ALA A O   1 
ATOM   1037 C  CB  . ALA A 1 133 ? 33.884 59.346 -5.597  1.00 19.54 ? 133  ALA A CB  1 
ATOM   1038 N  N   . TRP A 1 134 ? 35.336 60.029 -2.772  1.00 25.23 ? 134  TRP A N   1 
ATOM   1039 C  CA  . TRP A 1 134 ? 36.600 60.294 -2.088  1.00 28.10 ? 134  TRP A CA  1 
ATOM   1040 C  C   . TRP A 1 134 ? 36.800 59.551 -0.770  1.00 26.32 ? 134  TRP A C   1 
ATOM   1041 O  O   . TRP A 1 134 ? 37.785 59.775 -0.066  1.00 25.40 ? 134  TRP A O   1 
ATOM   1042 C  CB  . TRP A 1 134 ? 36.815 61.799 -1.896  1.00 36.15 ? 134  TRP A CB  1 
ATOM   1043 C  CG  . TRP A 1 134 ? 35.694 62.501 -1.215  1.00 47.32 ? 134  TRP A CG  1 
ATOM   1044 C  CD1 . TRP A 1 134 ? 35.525 62.669 0.131   1.00 51.44 ? 134  TRP A CD1 1 
ATOM   1045 C  CD2 . TRP A 1 134 ? 34.574 63.139 -1.845  1.00 54.47 ? 134  TRP A CD2 1 
ATOM   1046 N  NE1 . TRP A 1 134 ? 34.367 63.370 0.379   1.00 56.54 ? 134  TRP A NE1 1 
ATOM   1047 C  CE2 . TRP A 1 134 ? 33.762 63.669 -0.814  1.00 57.82 ? 134  TRP A CE2 1 
ATOM   1048 C  CE3 . TRP A 1 134 ? 34.175 63.313 -3.180  1.00 56.93 ? 134  TRP A CE3 1 
ATOM   1049 C  CZ2 . TRP A 1 134 ? 32.571 64.364 -1.077  1.00 59.16 ? 134  TRP A CZ2 1 
ATOM   1050 C  CZ3 . TRP A 1 134 ? 32.991 64.003 -3.442  1.00 59.30 ? 134  TRP A CZ3 1 
ATOM   1051 C  CH2 . TRP A 1 134 ? 32.203 64.517 -2.392  1.00 58.94 ? 134  TRP A CH2 1 
ATOM   1052 N  N   . ASP A 1 135 ? 35.866 58.673 -0.428  1.00 23.85 ? 135  ASP A N   1 
ATOM   1053 C  CA  . ASP A 1 135 ? 35.985 57.904 0.801   1.00 21.09 ? 135  ASP A CA  1 
ATOM   1054 C  C   . ASP A 1 135 ? 36.498 56.501 0.485   1.00 20.28 ? 135  ASP A C   1 
ATOM   1055 O  O   . ASP A 1 135 ? 36.624 55.665 1.377   1.00 19.15 ? 135  ASP A O   1 
ATOM   1056 C  CB  . ASP A 1 135 ? 34.637 57.832 1.528   1.00 20.79 ? 135  ASP A CB  1 
ATOM   1057 C  CG  . ASP A 1 135 ? 34.152 59.197 2.002   1.00 21.77 ? 135  ASP A CG  1 
ATOM   1058 O  OD1 . ASP A 1 135 ? 34.968 59.971 2.544   1.00 20.75 ? 135  ASP A OD1 1 
ATOM   1059 O  OD2 . ASP A 1 135 ? 32.951 59.500 1.836   1.00 26.23 ? 135  ASP A OD2 1 
ATOM   1060 N  N   . PHE A 1 136 ? 36.822 56.262 -0.785  1.00 18.35 ? 136  PHE A N   1 
ATOM   1061 C  CA  . PHE A 1 136 ? 37.309 54.964 -1.230  1.00 16.82 ? 136  PHE A CA  1 
ATOM   1062 C  C   . PHE A 1 136 ? 38.753 54.998 -1.703  1.00 18.33 ? 136  PHE A C   1 
ATOM   1063 O  O   . PHE A 1 136 ? 39.278 56.056 -2.052  1.00 18.15 ? 136  PHE A O   1 
ATOM   1064 C  CB  . PHE A 1 136 ? 36.382 54.393 -2.296  1.00 15.21 ? 136  PHE A CB  1 
ATOM   1065 C  CG  . PHE A 1 136 ? 34.997 54.146 -1.793  1.00 14.76 ? 136  PHE A CG  1 
ATOM   1066 C  CD1 . PHE A 1 136 ? 34.058 55.168 -1.778  1.00 14.92 ? 136  PHE A CD1 1 
ATOM   1067 C  CD2 . PHE A 1 136 ? 34.645 52.912 -1.268  1.00 14.46 ? 136  PHE A CD2 1 
ATOM   1068 C  CE1 . PHE A 1 136 ? 32.786 54.964 -1.242  1.00 15.89 ? 136  PHE A CE1 1 
ATOM   1069 C  CE2 . PHE A 1 136 ? 33.379 52.699 -0.731  1.00 13.74 ? 136  PHE A CE2 1 
ATOM   1070 C  CZ  . PHE A 1 136 ? 32.446 53.727 -0.718  1.00 12.12 ? 136  PHE A CZ  1 
ATOM   1071 N  N   . ASN A 1 137 ? 39.380 53.827 -1.708  1.00 18.22 ? 137  ASN A N   1 
ATOM   1072 C  CA  . ASN A 1 137 ? 40.782 53.668 -2.071  1.00 17.98 ? 137  ASN A CA  1 
ATOM   1073 C  C   . ASN A 1 137 ? 41.109 53.501 -3.535  1.00 20.95 ? 137  ASN A C   1 
ATOM   1074 O  O   . ASN A 1 137 ? 42.235 53.128 -3.867  1.00 24.08 ? 137  ASN A O   1 
ATOM   1075 C  CB  . ASN A 1 137 ? 41.383 52.486 -1.311  1.00 15.98 ? 137  ASN A CB  1 
ATOM   1076 C  CG  . ASN A 1 137 ? 41.742 52.831 0.106   1.00 20.05 ? 137  ASN A CG  1 
ATOM   1077 O  OD1 . ASN A 1 137 ? 41.915 53.999 0.445   1.00 25.52 ? 137  ASN A OD1 1 
ATOM   1078 N  ND2 . ASN A 1 137 ? 41.875 51.817 0.949   1.00 20.83 ? 137  ASN A ND2 1 
ATOM   1079 N  N   . ASP A 1 138 ? 40.151 53.755 -4.413  1.00 22.08 ? 138  ASP A N   1 
ATOM   1080 C  CA  . ASP A 1 138 ? 40.396 53.598 -5.842  1.00 25.98 ? 138  ASP A CA  1 
ATOM   1081 C  C   . ASP A 1 138 ? 41.701 54.255 -6.281  1.00 29.30 ? 138  ASP A C   1 
ATOM   1082 O  O   . ASP A 1 138 ? 42.520 53.628 -6.962  1.00 31.26 ? 138  ASP A O   1 
ATOM   1083 C  CB  . ASP A 1 138 ? 39.226 54.159 -6.643  1.00 26.40 ? 138  ASP A CB  1 
ATOM   1084 C  CG  . ASP A 1 138 ? 37.931 53.431 -6.359  1.00 29.93 ? 138  ASP A CG  1 
ATOM   1085 O  OD1 . ASP A 1 138 ? 37.796 52.272 -6.799  1.00 32.36 ? 138  ASP A OD1 1 
ATOM   1086 O  OD2 . ASP A 1 138 ? 37.052 54.015 -5.696  1.00 32.95 ? 138  ASP A OD2 1 
ATOM   1087 N  N   . GLY A 1 139 ? 41.924 55.486 -5.835  1.00 28.54 ? 139  GLY A N   1 
ATOM   1088 C  CA  . GLY A 1 139 ? 43.135 56.199 -6.204  1.00 28.27 ? 139  GLY A CA  1 
ATOM   1089 C  C   . GLY A 1 139 ? 44.419 55.675 -5.587  1.00 28.03 ? 139  GLY A C   1 
ATOM   1090 O  O   . GLY A 1 139 ? 45.496 55.870 -6.149  1.00 31.92 ? 139  GLY A O   1 
ATOM   1091 N  N   . LYS A 1 140 ? 44.313 55.011 -4.439  1.00 29.89 ? 140  LYS A N   1 
ATOM   1092 C  CA  . LYS A 1 140 ? 45.483 54.477 -3.749  1.00 28.34 ? 140  LYS A CA  1 
ATOM   1093 C  C   . LYS A 1 140 ? 45.941 53.124 -4.303  1.00 27.72 ? 140  LYS A C   1 
ATOM   1094 O  O   . LYS A 1 140 ? 47.129 52.791 -4.240  1.00 27.25 ? 140  LYS A O   1 
ATOM   1095 C  CB  . LYS A 1 140 ? 45.217 54.378 -2.245  1.00 28.83 ? 140  LYS A CB  1 
ATOM   1096 C  CG  . LYS A 1 140 ? 46.485 54.256 -1.424  1.00 34.45 ? 140  LYS A CG  1 
ATOM   1097 C  CD  . LYS A 1 140 ? 46.215 54.090 0.067   1.00 39.15 ? 140  LYS A CD  1 
ATOM   1098 C  CE  . LYS A 1 140 ? 45.679 55.349 0.725   1.00 42.70 ? 140  LYS A CE  1 
ATOM   1099 N  NZ  . LYS A 1 140 ? 44.265 55.635 0.364   1.00 45.92 ? 140  LYS A NZ  1 
ATOM   1100 N  N   . CYS A 1 141 ? 45.002 52.336 -4.820  1.00 24.35 ? 141  CYS A N   1 
ATOM   1101 C  CA  . CYS A 1 141 ? 45.337 51.033 -5.384  1.00 23.11 ? 141  CYS A CA  1 
ATOM   1102 C  C   . CYS A 1 141 ? 46.168 51.246 -6.634  1.00 25.67 ? 141  CYS A C   1 
ATOM   1103 O  O   . CYS A 1 141 ? 45.780 52.011 -7.518  1.00 27.28 ? 141  CYS A O   1 
ATOM   1104 C  CB  . CYS A 1 141 ? 44.079 50.245 -5.738  1.00 20.22 ? 141  CYS A CB  1 
ATOM   1105 S  SG  . CYS A 1 141 ? 44.442 48.652 -6.546  1.00 19.10 ? 141  CYS A SG  1 
ATOM   1106 N  N   . LYS A 1 142 ? 47.294 50.548 -6.723  1.00 29.83 ? 142  LYS A N   1 
ATOM   1107 C  CA  . LYS A 1 142 ? 48.182 50.694 -7.867  1.00 33.15 ? 142  LYS A CA  1 
ATOM   1108 C  C   . LYS A 1 142 ? 48.071 49.626 -8.948  1.00 32.60 ? 142  LYS A C   1 
ATOM   1109 O  O   . LYS A 1 142 ? 48.720 49.738 -9.986  1.00 33.19 ? 142  LYS A O   1 
ATOM   1110 C  CB  . LYS A 1 142 ? 49.637 50.810 -7.402  1.00 40.29 ? 142  LYS A CB  1 
ATOM   1111 C  CG  . LYS A 1 142 ? 49.900 51.941 -6.403  1.00 49.33 ? 142  LYS A CG  1 
ATOM   1112 C  CD  . LYS A 1 142 ? 49.428 53.298 -6.926  1.00 55.55 ? 142  LYS A CD  1 
ATOM   1113 C  CE  . LYS A 1 142 ? 49.546 54.378 -5.851  1.00 60.06 ? 142  LYS A CE  1 
ATOM   1114 N  NZ  . LYS A 1 142 ? 48.901 55.664 -6.263  1.00 62.35 ? 142  LYS A NZ  1 
ATOM   1115 N  N   . THR A 1 143 ? 47.266 48.591 -8.728  1.00 31.82 ? 143  THR A N   1 
ATOM   1116 C  CA  . THR A 1 143 ? 47.139 47.553 -9.744  1.00 29.82 ? 143  THR A CA  1 
ATOM   1117 C  C   . THR A 1 143 ? 46.315 48.047 -10.925 1.00 30.68 ? 143  THR A C   1 
ATOM   1118 O  O   . THR A 1 143 ? 45.534 48.996 -10.802 1.00 31.93 ? 143  THR A O   1 
ATOM   1119 C  CB  . THR A 1 143 ? 46.532 46.245 -9.190  1.00 28.80 ? 143  THR A CB  1 
ATOM   1120 O  OG1 . THR A 1 143 ? 45.218 46.490 -8.672  1.00 32.44 ? 143  THR A OG1 1 
ATOM   1121 C  CG2 . THR A 1 143 ? 47.415 45.680 -8.100  1.00 26.27 ? 143  THR A CG2 1 
ATOM   1122 N  N   . ALA A 1 144 ? 46.510 47.401 -12.070 1.00 32.81 ? 144  ALA A N   1 
ATOM   1123 C  CA  . ALA A 1 144 ? 45.810 47.744 -13.303 1.00 32.65 ? 144  ALA A CA  1 
ATOM   1124 C  C   . ALA A 1 144 ? 44.314 47.499 -13.197 1.00 32.17 ? 144  ALA A C   1 
ATOM   1125 O  O   . ALA A 1 144 ? 43.511 48.313 -13.649 1.00 33.69 ? 144  ALA A O   1 
ATOM   1126 C  CB  . ALA A 1 144 ? 46.382 46.944 -14.459 1.00 35.87 ? 144  ALA A CB  1 
ATOM   1127 N  N   . SER A 1 145 ? 43.950 46.360 -12.617 1.00 31.61 ? 145  SER A N   1 
ATOM   1128 C  CA  . SER A 1 145 ? 42.550 45.991 -12.454 1.00 28.78 ? 145  SER A CA  1 
ATOM   1129 C  C   . SER A 1 145 ? 41.905 46.640 -11.232 1.00 27.75 ? 145  SER A C   1 
ATOM   1130 O  O   . SER A 1 145 ? 40.679 46.647 -11.104 1.00 32.56 ? 145  SER A O   1 
ATOM   1131 C  CB  . SER A 1 145 ? 42.418 44.469 -12.337 1.00 26.20 ? 145  SER A CB  1 
ATOM   1132 O  OG  . SER A 1 145 ? 43.057 43.981 -11.166 1.00 26.96 ? 145  SER A OG  1 
ATOM   1133 N  N   . GLY A 1 146 ? 42.724 47.155 -10.320 1.00 23.53 ? 146  GLY A N   1 
ATOM   1134 C  CA  . GLY A 1 146 ? 42.188 47.760 -9.115  1.00 21.97 ? 146  GLY A CA  1 
ATOM   1135 C  C   . GLY A 1 146 ? 41.863 46.692 -8.083  1.00 19.83 ? 146  GLY A C   1 
ATOM   1136 O  O   . GLY A 1 146 ? 41.304 46.985 -7.026  1.00 19.60 ? 146  GLY A O   1 
ATOM   1137 N  N   . GLY A 1 147 ? 42.229 45.450 -8.386  1.00 19.23 ? 147  GLY A N   1 
ATOM   1138 C  CA  . GLY A 1 147 ? 41.983 44.347 -7.479  1.00 17.41 ? 147  GLY A CA  1 
ATOM   1139 C  C   . GLY A 1 147 ? 43.290 43.789 -6.954  1.00 16.80 ? 147  GLY A C   1 
ATOM   1140 O  O   . GLY A 1 147 ? 44.363 44.209 -7.382  1.00 16.48 ? 147  GLY A O   1 
ATOM   1141 N  N   . ILE A 1 148 ? 43.206 42.862 -6.008  1.00 17.88 ? 148  ILE A N   1 
ATOM   1142 C  CA  . ILE A 1 148 ? 44.398 42.254 -5.430  1.00 17.21 ? 148  ILE A CA  1 
ATOM   1143 C  C   . ILE A 1 148 ? 44.956 41.246 -6.429  1.00 21.28 ? 148  ILE A C   1 
ATOM   1144 O  O   . ILE A 1 148 ? 44.382 40.175 -6.634  1.00 26.19 ? 148  ILE A O   1 
ATOM   1145 C  CB  . ILE A 1 148 ? 44.077 41.538 -4.100  1.00 15.14 ? 148  ILE A CB  1 
ATOM   1146 C  CG1 . ILE A 1 148 ? 43.288 42.476 -3.174  1.00 12.91 ? 148  ILE A CG1 1 
ATOM   1147 C  CG2 . ILE A 1 148 ? 45.366 41.085 -3.427  1.00 13.33 ? 148  ILE A CG2 1 
ATOM   1148 C  CD1 . ILE A 1 148 ? 42.844 41.844 -1.872  1.00 11.48 ? 148  ILE A CD1 1 
ATOM   1149 N  N   . GLU A 1 149 ? 46.054 41.608 -7.077  1.00 21.53 ? 149  GLU A N   1 
ATOM   1150 C  CA  . GLU A 1 149 ? 46.675 40.733 -8.061  1.00 25.81 ? 149  GLU A CA  1 
ATOM   1151 C  C   . GLU A 1 149 ? 47.765 39.859 -7.442  1.00 26.08 ? 149  GLU A C   1 
ATOM   1152 O  O   . GLU A 1 149 ? 48.150 38.833 -8.010  1.00 28.49 ? 149  GLU A O   1 
ATOM   1153 C  CB  . GLU A 1 149 ? 47.235 41.557 -9.224  1.00 26.47 ? 149  GLU A CB  1 
ATOM   1154 C  CG  . GLU A 1 149 ? 46.152 42.257 -10.063 1.00 31.58 ? 149  GLU A CG  1 
ATOM   1155 C  CD  . GLU A 1 149 ? 46.714 43.186 -11.141 1.00 33.60 ? 149  GLU A CD  1 
ATOM   1156 O  OE1 . GLU A 1 149 ? 47.949 43.215 -11.346 1.00 35.73 ? 149  GLU A OE1 1 
ATOM   1157 O  OE2 . GLU A 1 149 ? 45.913 43.895 -11.785 1.00 35.23 ? 149  GLU A OE2 1 
ATOM   1158 N  N   . SER A 1 150 ? 48.242 40.253 -6.269  1.00 23.88 ? 150  SER A N   1 
ATOM   1159 C  CA  . SER A 1 150 ? 49.275 39.502 -5.580  1.00 22.01 ? 150  SER A CA  1 
ATOM   1160 C  C   . SER A 1 150 ? 49.145 39.645 -4.077  1.00 23.63 ? 150  SER A C   1 
ATOM   1161 O  O   . SER A 1 150 ? 49.041 40.755 -3.557  1.00 28.05 ? 150  SER A O   1 
ATOM   1162 C  CB  . SER A 1 150 ? 50.654 39.991 -6.004  1.00 22.22 ? 150  SER A CB  1 
ATOM   1163 O  OG  . SER A 1 150 ? 51.651 39.482 -5.134  1.00 26.54 ? 150  SER A OG  1 
ATOM   1164 N  N   . TYR A 1 151 ? 49.161 38.518 -3.379  1.00 21.70 ? 151  TYR A N   1 
ATOM   1165 C  CA  . TYR A 1 151 ? 49.074 38.528 -1.927  1.00 18.53 ? 151  TYR A CA  1 
ATOM   1166 C  C   . TYR A 1 151 ? 50.467 38.669 -1.303  1.00 17.44 ? 151  TYR A C   1 
ATOM   1167 O  O   . TYR A 1 151 ? 50.627 38.624 -0.081  1.00 18.97 ? 151  TYR A O   1 
ATOM   1168 C  CB  . TYR A 1 151 ? 48.357 37.275 -1.422  1.00 16.39 ? 151  TYR A CB  1 
ATOM   1169 C  CG  . TYR A 1 151 ? 46.862 37.458 -1.267  1.00 17.01 ? 151  TYR A CG  1 
ATOM   1170 C  CD1 . TYR A 1 151 ? 45.989 37.251 -2.337  1.00 17.09 ? 151  TYR A CD1 1 
ATOM   1171 C  CD2 . TYR A 1 151 ? 46.319 37.853 -0.046  1.00 15.39 ? 151  TYR A CD2 1 
ATOM   1172 C  CE1 . TYR A 1 151 ? 44.607 37.438 -2.189  1.00 15.81 ? 151  TYR A CE1 1 
ATOM   1173 C  CE2 . TYR A 1 151 ? 44.951 38.040 0.112   1.00 15.54 ? 151  TYR A CE2 1 
ATOM   1174 C  CZ  . TYR A 1 151 ? 44.101 37.834 -0.957  1.00 16.94 ? 151  TYR A CZ  1 
ATOM   1175 O  OH  . TYR A 1 151 ? 42.753 38.041 -0.779  1.00 19.56 ? 151  TYR A OH  1 
ATOM   1176 N  N   . ASN A 1 152 ? 51.470 38.860 -2.151  1.00 17.41 ? 152  ASN A N   1 
ATOM   1177 C  CA  . ASN A 1 152 ? 52.841 39.034 -1.688  1.00 22.91 ? 152  ASN A CA  1 
ATOM   1178 C  C   . ASN A 1 152 ? 53.141 40.525 -1.483  1.00 21.58 ? 152  ASN A C   1 
ATOM   1179 O  O   . ASN A 1 152 ? 54.204 40.904 -0.982  1.00 16.59 ? 152  ASN A O   1 
ATOM   1180 C  CB  . ASN A 1 152 ? 53.821 38.431 -2.698  1.00 28.34 ? 152  ASN A CB  1 
ATOM   1181 C  CG  . ASN A 1 152 ? 55.216 38.290 -2.134  1.00 37.15 ? 152  ASN A CG  1 
ATOM   1182 O  OD1 . ASN A 1 152 ? 56.166 38.919 -2.612  1.00 41.95 ? 152  ASN A OD1 1 
ATOM   1183 N  ND2 . ASN A 1 152 ? 55.350 37.476 -1.099  1.00 40.00 ? 152  ASN A ND2 1 
ATOM   1184 N  N   . ASP A 1 153 ? 52.183 41.364 -1.866  1.00 20.72 ? 153  ASP A N   1 
ATOM   1185 C  CA  . ASP A 1 153 ? 52.303 42.812 -1.740  1.00 20.07 ? 153  ASP A CA  1 
ATOM   1186 C  C   . ASP A 1 153 ? 51.268 43.330 -0.740  1.00 17.36 ? 153  ASP A C   1 
ATOM   1187 O  O   . ASP A 1 153 ? 50.090 43.447 -1.070  1.00 20.92 ? 153  ASP A O   1 
ATOM   1188 C  CB  . ASP A 1 153 ? 52.083 43.462 -3.114  1.00 21.68 ? 153  ASP A CB  1 
ATOM   1189 C  CG  . ASP A 1 153 ? 52.309 44.970 -3.111  1.00 23.55 ? 153  ASP A CG  1 
ATOM   1190 O  OD1 . ASP A 1 153 ? 52.729 45.544 -2.084  1.00 25.01 ? 153  ASP A OD1 1 
ATOM   1191 O  OD2 . ASP A 1 153 ? 52.062 45.589 -4.163  1.00 27.16 ? 153  ASP A OD2 1 
ATOM   1192 N  N   . PRO A 1 154 ? 51.707 43.696 0.478   1.00 15.48 ? 154  PRO A N   1 
ATOM   1193 C  CA  . PRO A 1 154 ? 50.855 44.213 1.557   1.00 14.92 ? 154  PRO A CA  1 
ATOM   1194 C  C   . PRO A 1 154 ? 49.961 45.369 1.123   1.00 14.73 ? 154  PRO A C   1 
ATOM   1195 O  O   . PRO A 1 154 ? 48.820 45.490 1.569   1.00 19.43 ? 154  PRO A O   1 
ATOM   1196 C  CB  . PRO A 1 154 ? 51.872 44.687 2.589   1.00 13.87 ? 154  PRO A CB  1 
ATOM   1197 C  CG  . PRO A 1 154 ? 52.987 43.736 2.401   1.00 12.84 ? 154  PRO A CG  1 
ATOM   1198 C  CD  . PRO A 1 154 ? 53.116 43.693 0.902   1.00 13.16 ? 154  PRO A CD  1 
ATOM   1199 N  N   . TYR A 1 155 ? 50.489 46.215 0.246   1.00 14.65 ? 155  TYR A N   1 
ATOM   1200 C  CA  . TYR A 1 155 ? 49.760 47.368 -0.255  1.00 11.64 ? 155  TYR A CA  1 
ATOM   1201 C  C   . TYR A 1 155 ? 48.561 46.991 -1.102  1.00 13.78 ? 155  TYR A C   1 
ATOM   1202 O  O   . TYR A 1 155 ? 47.495 47.575 -0.950  1.00 20.43 ? 155  TYR A O   1 
ATOM   1203 C  CB  . TYR A 1 155 ? 50.701 48.297 -1.026  1.00 15.30 ? 155  TYR A CB  1 
ATOM   1204 C  CG  . TYR A 1 155 ? 51.699 48.994 -0.125  1.00 15.00 ? 155  TYR A CG  1 
ATOM   1205 C  CD1 . TYR A 1 155 ? 52.900 48.382 0.222   1.00 14.87 ? 155  TYR A CD1 1 
ATOM   1206 C  CD2 . TYR A 1 155 ? 51.418 50.250 0.418   1.00 15.78 ? 155  TYR A CD2 1 
ATOM   1207 C  CE1 . TYR A 1 155 ? 53.792 49.001 1.090   1.00 18.97 ? 155  TYR A CE1 1 
ATOM   1208 C  CE2 . TYR A 1 155 ? 52.300 50.876 1.282   1.00 16.93 ? 155  TYR A CE2 1 
ATOM   1209 C  CZ  . TYR A 1 155 ? 53.484 50.246 1.615   1.00 20.03 ? 155  TYR A CZ  1 
ATOM   1210 O  OH  . TYR A 1 155 ? 54.358 50.857 2.484   1.00 26.43 ? 155  TYR A OH  1 
ATOM   1211 N  N   . GLN A 1 156 ? 48.711 45.997 -1.971  1.00 14.09 ? 156  GLN A N   1 
ATOM   1212 C  CA  . GLN A 1 156 ? 47.595 45.571 -2.810  1.00 12.16 ? 156  GLN A CA  1 
ATOM   1213 C  C   . GLN A 1 156 ? 46.495 44.967 -1.967  1.00 11.62 ? 156  GLN A C   1 
ATOM   1214 O  O   . GLN A 1 156 ? 45.329 45.305 -2.130  1.00 12.55 ? 156  GLN A O   1 
ATOM   1215 C  CB  . GLN A 1 156 ? 48.027 44.525 -3.831  1.00 13.79 ? 156  GLN A CB  1 
ATOM   1216 C  CG  . GLN A 1 156 ? 48.931 45.045 -4.915  1.00 19.25 ? 156  GLN A CG  1 
ATOM   1217 C  CD  . GLN A 1 156 ? 49.212 43.998 -5.954  1.00 17.83 ? 156  GLN A CD  1 
ATOM   1218 O  OE1 . GLN A 1 156 ? 48.375 43.137 -6.222  1.00 19.41 ? 156  GLN A OE1 1 
ATOM   1219 N  NE2 . GLN A 1 156 ? 50.386 44.064 -6.557  1.00 21.79 ? 156  GLN A NE2 1 
ATOM   1220 N  N   . VAL A 1 157 ? 46.865 44.092 -1.041  1.00 10.23 ? 157  VAL A N   1 
ATOM   1221 C  CA  . VAL A 1 157 ? 45.856 43.441 -0.226  1.00 14.00 ? 157  VAL A CA  1 
ATOM   1222 C  C   . VAL A 1 157 ? 45.095 44.392 0.690   1.00 14.62 ? 157  VAL A C   1 
ATOM   1223 O  O   . VAL A 1 157 ? 43.893 44.199 0.935   1.00 16.39 ? 157  VAL A O   1 
ATOM   1224 C  CB  . VAL A 1 157 ? 46.400 42.142 0.499   1.00 13.28 ? 157  VAL A CB  1 
ATOM   1225 C  CG1 . VAL A 1 157 ? 47.902 42.126 0.552   1.00 12.85 ? 157  VAL A CG1 1 
ATOM   1226 C  CG2 . VAL A 1 157 ? 45.823 41.995 1.891   1.00 14.82 ? 157  VAL A CG2 1 
ATOM   1227 N  N   . ARG A 1 158 ? 45.735 45.487 1.083   1.00 16.50 ? 158  ARG A N   1 
ATOM   1228 C  CA  . ARG A 1 158 ? 45.082 46.446 1.966   1.00 14.67 ? 158  ARG A CA  1 
ATOM   1229 C  C   . ARG A 1 158 ? 44.444 47.649 1.280   1.00 14.06 ? 158  ARG A C   1 
ATOM   1230 O  O   . ARG A 1 158 ? 43.374 48.114 1.711   1.00 9.51  ? 158  ARG A O   1 
ATOM   1231 C  CB  . ARG A 1 158 ? 46.041 46.877 3.071   1.00 12.29 ? 158  ARG A CB  1 
ATOM   1232 C  CG  . ARG A 1 158 ? 46.704 45.673 3.707   1.00 14.82 ? 158  ARG A CG  1 
ATOM   1233 C  CD  . ARG A 1 158 ? 47.140 45.919 5.109   1.00 15.82 ? 158  ARG A CD  1 
ATOM   1234 N  NE  . ARG A 1 158 ? 48.563 45.669 5.259   1.00 20.03 ? 158  ARG A NE  1 
ATOM   1235 C  CZ  . ARG A 1 158 ? 49.094 44.895 6.195   1.00 19.60 ? 158  ARG A CZ  1 
ATOM   1236 N  NH1 . ARG A 1 158 ? 48.329 44.273 7.077   1.00 18.08 ? 158  ARG A NH1 1 
ATOM   1237 N  NH2 . ARG A 1 158 ? 50.407 44.795 6.282   1.00 26.45 ? 158  ARG A NH2 1 
ATOM   1238 N  N   . ASP A 1 159 ? 45.034 48.082 0.165   1.00 15.56 ? 159  ASP A N   1 
ATOM   1239 C  CA  . ASP A 1 159 ? 44.542 49.244 -0.588  1.00 14.43 ? 159  ASP A CA  1 
ATOM   1240 C  C   . ASP A 1 159 ? 43.697 48.941 -1.826  1.00 13.01 ? 159  ASP A C   1 
ATOM   1241 O  O   . ASP A 1 159 ? 43.044 49.838 -2.365  1.00 13.50 ? 159  ASP A O   1 
ATOM   1242 C  CB  . ASP A 1 159 ? 45.704 50.162 -0.988  1.00 13.48 ? 159  ASP A CB  1 
ATOM   1243 C  CG  . ASP A 1 159 ? 46.491 50.665 0.208   1.00 14.70 ? 159  ASP A CG  1 
ATOM   1244 O  OD1 . ASP A 1 159 ? 45.946 50.662 1.330   1.00 17.62 ? 159  ASP A OD1 1 
ATOM   1245 O  OD2 . ASP A 1 159 ? 47.659 51.069 0.029   1.00 17.17 ? 159  ASP A OD2 1 
ATOM   1246 N  N   . CYS A 1 160 ? 43.711 47.695 -2.286  1.00 10.03 ? 160  CYS A N   1 
ATOM   1247 C  CA  . CYS A 1 160 ? 42.934 47.328 -3.460  1.00 9.33  ? 160  CYS A CA  1 
ATOM   1248 C  C   . CYS A 1 160 ? 41.672 46.555 -3.119  1.00 11.71 ? 160  CYS A C   1 
ATOM   1249 O  O   . CYS A 1 160 ? 41.451 46.173 -1.961  1.00 16.34 ? 160  CYS A O   1 
ATOM   1250 C  CB  . CYS A 1 160 ? 43.795 46.557 -4.452  1.00 9.55  ? 160  CYS A CB  1 
ATOM   1251 S  SG  . CYS A 1 160 ? 45.210 47.532 -5.040  1.00 16.78 ? 160  CYS A SG  1 
ATOM   1252 N  N   . GLN A 1 161 ? 40.846 46.329 -4.135  1.00 12.52 ? 161  GLN A N   1 
ATOM   1253 C  CA  . GLN A 1 161 ? 39.577 45.639 -3.964  1.00 15.50 ? 161  GLN A CA  1 
ATOM   1254 C  C   . GLN A 1 161 ? 39.620 44.123 -3.765  1.00 16.23 ? 161  GLN A C   1 
ATOM   1255 O  O   . GLN A 1 161 ? 40.155 43.386 -4.605  1.00 17.68 ? 161  GLN A O   1 
ATOM   1256 C  CB  . GLN A 1 161 ? 38.653 45.958 -5.139  1.00 17.85 ? 161  GLN A CB  1 
ATOM   1257 C  CG  . GLN A 1 161 ? 38.310 47.427 -5.304  1.00 19.00 ? 161  GLN A CG  1 
ATOM   1258 C  CD  . GLN A 1 161 ? 37.435 47.689 -6.524  1.00 20.43 ? 161  GLN A CD  1 
ATOM   1259 O  OE1 . GLN A 1 161 ? 36.900 48.778 -6.687  1.00 21.30 ? 161  GLN A OE1 1 
ATOM   1260 N  NE2 . GLN A 1 161 ? 37.296 46.693 -7.388  1.00 24.42 ? 161  GLN A NE2 1 
ATOM   1261 N  N   . LEU A 1 162 ? 39.044 43.679 -2.648  1.00 13.67 ? 162  LEU A N   1 
ATOM   1262 C  CA  . LEU A 1 162 ? 38.925 42.262 -2.307  1.00 14.00 ? 162  LEU A CA  1 
ATOM   1263 C  C   . LEU A 1 162 ? 37.704 41.813 -3.116  1.00 15.99 ? 162  LEU A C   1 
ATOM   1264 O  O   . LEU A 1 162 ? 36.604 42.319 -2.892  1.00 15.44 ? 162  LEU A O   1 
ATOM   1265 C  CB  . LEU A 1 162 ? 38.605 42.106 -0.816  1.00 12.34 ? 162  LEU A CB  1 
ATOM   1266 C  CG  . LEU A 1 162 ? 38.923 40.828 -0.030  1.00 13.99 ? 162  LEU A CG  1 
ATOM   1267 C  CD1 . LEU A 1 162 ? 37.838 40.631 1.013   1.00 12.72 ? 162  LEU A CD1 1 
ATOM   1268 C  CD2 . LEU A 1 162 ? 39.032 39.610 -0.917  1.00 13.36 ? 162  LEU A CD2 1 
ATOM   1269 N  N   . VAL A 1 163 ? 37.905 40.904 -4.070  1.00 15.97 ? 163  VAL A N   1 
ATOM   1270 C  CA  . VAL A 1 163 ? 36.838 40.396 -4.939  1.00 16.24 ? 163  VAL A CA  1 
ATOM   1271 C  C   . VAL A 1 163 ? 35.835 41.449 -5.435  1.00 17.20 ? 163  VAL A C   1 
ATOM   1272 O  O   . VAL A 1 163 ? 34.624 41.241 -5.393  1.00 19.97 ? 163  VAL A O   1 
ATOM   1273 C  CB  . VAL A 1 163 ? 36.095 39.159 -4.334  1.00 14.93 ? 163  VAL A CB  1 
ATOM   1274 C  CG1 . VAL A 1 163 ? 37.071 38.024 -4.133  1.00 17.51 ? 163  VAL A CG1 1 
ATOM   1275 C  CG2 . VAL A 1 163 ? 35.407 39.497 -3.025  1.00 14.33 ? 163  VAL A CG2 1 
ATOM   1276 N  N   . GLY A 1 164 ? 36.358 42.572 -5.926  1.00 15.73 ? 164  GLY A N   1 
ATOM   1277 C  CA  . GLY A 1 164 ? 35.519 43.634 -6.454  1.00 12.02 ? 164  GLY A CA  1 
ATOM   1278 C  C   . GLY A 1 164 ? 34.749 44.479 -5.465  1.00 13.78 ? 164  GLY A C   1 
ATOM   1279 O  O   . GLY A 1 164 ? 33.939 45.307 -5.865  1.00 18.10 ? 164  GLY A O   1 
ATOM   1280 N  N   . LEU A 1 165 ? 34.957 44.259 -4.176  1.00 13.98 ? 165  LEU A N   1 
ATOM   1281 C  CA  . LEU A 1 165 ? 34.270 45.043 -3.154  1.00 13.97 ? 165  LEU A CA  1 
ATOM   1282 C  C   . LEU A 1 165 ? 34.930 46.427 -3.016  1.00 14.65 ? 165  LEU A C   1 
ATOM   1283 O  O   . LEU A 1 165 ? 36.162 46.527 -2.939  1.00 15.84 ? 165  LEU A O   1 
ATOM   1284 C  CB  . LEU A 1 165 ? 34.300 44.303 -1.810  1.00 10.79 ? 165  LEU A CB  1 
ATOM   1285 C  CG  . LEU A 1 165 ? 33.181 43.332 -1.392  1.00 12.85 ? 165  LEU A CG  1 
ATOM   1286 C  CD1 . LEU A 1 165 ? 32.103 43.189 -2.444  1.00 4.23  ? 165  LEU A CD1 1 
ATOM   1287 C  CD2 . LEU A 1 165 ? 33.786 41.997 -1.032  1.00 7.20  ? 165  LEU A CD2 1 
ATOM   1288 N  N   . LEU A 1 166 ? 34.109 47.479 -2.983  1.00 12.66 ? 166  LEU A N   1 
ATOM   1289 C  CA  . LEU A 1 166 ? 34.595 48.854 -2.860  1.00 11.45 ? 166  LEU A CA  1 
ATOM   1290 C  C   . LEU A 1 166 ? 35.379 49.034 -1.568  1.00 11.63 ? 166  LEU A C   1 
ATOM   1291 O  O   . LEU A 1 166 ? 34.822 48.913 -0.474  1.00 13.19 ? 166  LEU A O   1 
ATOM   1292 C  CB  . LEU A 1 166 ? 33.416 49.833 -2.926  1.00 14.66 ? 166  LEU A CB  1 
ATOM   1293 C  CG  . LEU A 1 166 ? 32.717 49.885 -4.287  1.00 13.49 ? 166  LEU A CG  1 
ATOM   1294 C  CD1 . LEU A 1 166 ? 31.472 50.745 -4.228  1.00 15.43 ? 166  LEU A CD1 1 
ATOM   1295 C  CD2 . LEU A 1 166 ? 33.701 50.427 -5.308  1.00 12.33 ? 166  LEU A CD2 1 
ATOM   1296 N  N   . ASP A 1 167 ? 36.663 49.358 -1.701  1.00 11.06 ? 167  ASP A N   1 
ATOM   1297 C  CA  . ASP A 1 167 ? 37.547 49.506 -0.549  1.00 7.99  ? 167  ASP A CA  1 
ATOM   1298 C  C   . ASP A 1 167 ? 37.513 50.868 0.136   1.00 9.99  ? 167  ASP A C   1 
ATOM   1299 O  O   . ASP A 1 167 ? 37.893 51.876 -0.451  1.00 14.83 ? 167  ASP A O   1 
ATOM   1300 C  CB  . ASP A 1 167 ? 38.980 49.159 -0.956  1.00 7.22  ? 167  ASP A CB  1 
ATOM   1301 C  CG  . ASP A 1 167 ? 39.765 48.498 0.166   1.00 7.09  ? 167  ASP A CG  1 
ATOM   1302 O  OD1 . ASP A 1 167 ? 39.351 47.420 0.633   1.00 9.26  ? 167  ASP A OD1 1 
ATOM   1303 O  OD2 . ASP A 1 167 ? 40.800 49.050 0.581   1.00 11.88 ? 167  ASP A OD2 1 
ATOM   1304 N  N   . LEU A 1 168 ? 37.110 50.873 1.404   1.00 10.85 ? 168  LEU A N   1 
ATOM   1305 C  CA  . LEU A 1 168 ? 37.026 52.094 2.210   1.00 8.23  ? 168  LEU A CA  1 
ATOM   1306 C  C   . LEU A 1 168 ? 38.405 52.687 2.523   1.00 12.29 ? 168  LEU A C   1 
ATOM   1307 O  O   . LEU A 1 168 ? 39.333 51.957 2.884   1.00 15.33 ? 168  LEU A O   1 
ATOM   1308 C  CB  . LEU A 1 168 ? 36.313 51.781 3.529   1.00 7.66  ? 168  LEU A CB  1 
ATOM   1309 C  CG  . LEU A 1 168 ? 34.891 52.260 3.836   1.00 8.95  ? 168  LEU A CG  1 
ATOM   1310 C  CD1 . LEU A 1 168 ? 34.225 52.869 2.626   1.00 10.37 ? 168  LEU A CD1 1 
ATOM   1311 C  CD2 . LEU A 1 168 ? 34.079 51.108 4.388   1.00 2.89  ? 168  LEU A CD2 1 
ATOM   1312 N  N   . ALA A 1 169 ? 38.529 54.010 2.426   1.00 14.53 ? 169  ALA A N   1 
ATOM   1313 C  CA  . ALA A 1 169 ? 39.791 54.696 2.713   1.00 14.50 ? 169  ALA A CA  1 
ATOM   1314 C  C   . ALA A 1 169 ? 39.860 54.897 4.218   1.00 16.78 ? 169  ALA A C   1 
ATOM   1315 O  O   . ALA A 1 169 ? 39.593 55.987 4.733   1.00 17.39 ? 169  ALA A O   1 
ATOM   1316 C  CB  . ALA A 1 169 ? 39.846 56.031 1.998   1.00 15.10 ? 169  ALA A CB  1 
ATOM   1317 N  N   . LEU A 1 170 ? 40.221 53.830 4.920   1.00 16.68 ? 170  LEU A N   1 
ATOM   1318 C  CA  . LEU A 1 170 ? 40.290 53.855 6.372   1.00 18.39 ? 170  LEU A CA  1 
ATOM   1319 C  C   . LEU A 1 170 ? 41.326 54.752 7.019   1.00 19.55 ? 170  LEU A C   1 
ATOM   1320 O  O   . LEU A 1 170 ? 41.407 54.795 8.237   1.00 18.16 ? 170  LEU A O   1 
ATOM   1321 C  CB  . LEU A 1 170 ? 40.401 52.437 6.929   1.00 18.87 ? 170  LEU A CB  1 
ATOM   1322 C  CG  . LEU A 1 170 ? 39.057 51.844 7.348   1.00 20.33 ? 170  LEU A CG  1 
ATOM   1323 C  CD1 . LEU A 1 170 ? 38.809 50.540 6.628   1.00 19.34 ? 170  LEU A CD1 1 
ATOM   1324 C  CD2 . LEU A 1 170 ? 39.030 51.656 8.855   1.00 21.74 ? 170  LEU A CD2 1 
ATOM   1325 N  N   . GLU A 1 171 ? 42.155 55.425 6.229   1.00 21.91 ? 171  GLU A N   1 
ATOM   1326 C  CA  . GLU A 1 171 ? 43.143 56.310 6.834   1.00 23.16 ? 171  GLU A CA  1 
ATOM   1327 C  C   . GLU A 1 171 ? 42.505 57.677 7.087   1.00 22.77 ? 171  GLU A C   1 
ATOM   1328 O  O   . GLU A 1 171 ? 42.998 58.460 7.891   1.00 24.25 ? 171  GLU A O   1 
ATOM   1329 C  CB  . GLU A 1 171 ? 44.419 56.426 5.980   1.00 25.24 ? 171  GLU A CB  1 
ATOM   1330 C  CG  . GLU A 1 171 ? 44.336 57.312 4.740   1.00 30.84 ? 171  GLU A CG  1 
ATOM   1331 C  CD  . GLU A 1 171 ? 43.648 56.659 3.545   1.00 37.20 ? 171  GLU A CD  1 
ATOM   1332 O  OE1 . GLU A 1 171 ? 43.356 55.435 3.574   1.00 38.12 ? 171  GLU A OE1 1 
ATOM   1333 O  OE2 . GLU A 1 171 ? 43.411 57.388 2.556   1.00 39.36 ? 171  GLU A OE2 1 
ATOM   1334 N  N   . LYS A 1 172 ? 41.392 57.946 6.414   1.00 19.47 ? 172  LYS A N   1 
ATOM   1335 C  CA  . LYS A 1 172 ? 40.695 59.207 6.579   1.00 19.96 ? 172  LYS A CA  1 
ATOM   1336 C  C   . LYS A 1 172 ? 39.952 59.203 7.902   1.00 21.79 ? 172  LYS A C   1 
ATOM   1337 O  O   . LYS A 1 172 ? 39.303 58.217 8.250   1.00 25.44 ? 172  LYS A O   1 
ATOM   1338 C  CB  . LYS A 1 172 ? 39.698 59.416 5.439   1.00 18.48 ? 172  LYS A CB  1 
ATOM   1339 C  CG  . LYS A 1 172 ? 40.335 59.553 4.074   1.00 23.15 ? 172  LYS A CG  1 
ATOM   1340 C  CD  . LYS A 1 172 ? 39.297 59.845 2.997   1.00 28.42 ? 172  LYS A CD  1 
ATOM   1341 C  CE  . LYS A 1 172 ? 38.555 61.152 3.258   1.00 30.76 ? 172  LYS A CE  1 
ATOM   1342 N  NZ  . LYS A 1 172 ? 37.638 61.526 2.141   1.00 32.68 ? 172  LYS A NZ  1 
ATOM   1343 N  N   . ASP A 1 173 ? 40.011 60.311 8.630   1.00 25.03 ? 173  ASP A N   1 
ATOM   1344 C  CA  . ASP A 1 173 ? 39.317 60.383 9.906   1.00 24.20 ? 173  ASP A CA  1 
ATOM   1345 C  C   . ASP A 1 173 ? 37.803 60.360 9.726   1.00 19.67 ? 173  ASP A C   1 
ATOM   1346 O  O   . ASP A 1 173 ? 37.087 59.872 10.596  1.00 17.79 ? 173  ASP A O   1 
ATOM   1347 C  CB  . ASP A 1 173 ? 39.748 61.606 10.714  1.00 32.37 ? 173  ASP A CB  1 
ATOM   1348 C  CG  . ASP A 1 173 ? 39.286 61.534 12.168  1.00 40.20 ? 173  ASP A CG  1 
ATOM   1349 O  OD1 . ASP A 1 173 ? 39.460 60.465 12.804  1.00 39.68 ? 173  ASP A OD1 1 
ATOM   1350 O  OD2 . ASP A 1 173 ? 38.740 62.541 12.672  1.00 45.44 ? 173  ASP A OD2 1 
ATOM   1351 N  N   . TYR A 1 174 ? 37.314 60.877 8.601   1.00 17.71 ? 174  TYR A N   1 
ATOM   1352 C  CA  . TYR A 1 174 ? 35.877 60.875 8.332   1.00 14.82 ? 174  TYR A CA  1 
ATOM   1353 C  C   . TYR A 1 174 ? 35.345 59.439 8.333   1.00 15.02 ? 174  TYR A C   1 
ATOM   1354 O  O   . TYR A 1 174 ? 34.393 59.114 9.038   1.00 16.47 ? 174  TYR A O   1 
ATOM   1355 C  CB  . TYR A 1 174 ? 35.572 61.517 6.974   1.00 11.87 ? 174  TYR A CB  1 
ATOM   1356 C  CG  . TYR A 1 174 ? 34.099 61.474 6.622   1.00 15.14 ? 174  TYR A CG  1 
ATOM   1357 C  CD1 . TYR A 1 174 ? 33.185 62.300 7.275   1.00 14.93 ? 174  TYR A CD1 1 
ATOM   1358 C  CD2 . TYR A 1 174 ? 33.611 60.576 5.671   1.00 17.22 ? 174  TYR A CD2 1 
ATOM   1359 C  CE1 . TYR A 1 174 ? 31.825 62.231 6.995   1.00 15.59 ? 174  TYR A CE1 1 
ATOM   1360 C  CE2 . TYR A 1 174 ? 32.251 60.500 5.385   1.00 15.40 ? 174  TYR A CE2 1 
ATOM   1361 C  CZ  . TYR A 1 174 ? 31.366 61.330 6.051   1.00 16.63 ? 174  TYR A CZ  1 
ATOM   1362 O  OH  . TYR A 1 174 ? 30.020 61.264 5.781   1.00 20.47 ? 174  TYR A OH  1 
ATOM   1363 N  N   . VAL A 1 175 ? 35.976 58.589 7.532   1.00 15.69 ? 175  VAL A N   1 
ATOM   1364 C  CA  . VAL A 1 175 ? 35.597 57.184 7.426   1.00 15.25 ? 175  VAL A CA  1 
ATOM   1365 C  C   . VAL A 1 175 ? 35.776 56.508 8.785   1.00 14.91 ? 175  VAL A C   1 
ATOM   1366 O  O   . VAL A 1 175 ? 34.868 55.829 9.275   1.00 15.26 ? 175  VAL A O   1 
ATOM   1367 C  CB  . VAL A 1 175 ? 36.436 56.475 6.340   1.00 12.76 ? 175  VAL A CB  1 
ATOM   1368 C  CG1 . VAL A 1 175 ? 36.082 55.007 6.271   1.00 12.03 ? 175  VAL A CG1 1 
ATOM   1369 C  CG2 . VAL A 1 175 ? 36.182 57.132 4.992   1.00 9.63  ? 175  VAL A CG2 1 
ATOM   1370 N  N   . ARG A 1 176 ? 36.929 56.742 9.405   1.00 12.16 ? 176  ARG A N   1 
ATOM   1371 C  CA  . ARG A 1 176 ? 37.232 56.195 10.721  1.00 14.90 ? 176  ARG A CA  1 
ATOM   1372 C  C   . ARG A 1 176 ? 36.098 56.513 11.694  1.00 15.58 ? 176  ARG A C   1 
ATOM   1373 O  O   . ARG A 1 176 ? 35.632 55.644 12.432  1.00 22.47 ? 176  ARG A O   1 
ATOM   1374 C  CB  . ARG A 1 176 ? 38.528 56.810 11.255  1.00 15.78 ? 176  ARG A CB  1 
ATOM   1375 C  CG  . ARG A 1 176 ? 39.628 55.821 11.476  1.00 18.59 ? 176  ARG A CG  1 
ATOM   1376 C  CD  . ARG A 1 176 ? 40.793 56.065 10.546  1.00 16.97 ? 176  ARG A CD  1 
ATOM   1377 N  NE  . ARG A 1 176 ? 41.791 56.958 11.117  1.00 21.13 ? 176  ARG A NE  1 
ATOM   1378 C  CZ  . ARG A 1 176 ? 43.107 56.804 10.974  1.00 22.88 ? 176  ARG A CZ  1 
ATOM   1379 N  NH1 . ARG A 1 176 ? 43.599 55.793 10.270  1.00 20.87 ? 176  ARG A NH1 1 
ATOM   1380 N  NH2 . ARG A 1 176 ? 43.937 57.669 11.533  1.00 23.93 ? 176  ARG A NH2 1 
ATOM   1381 N  N   . SER A 1 177 ? 35.626 57.756 11.648  1.00 16.40 ? 177  SER A N   1 
ATOM   1382 C  CA  . SER A 1 177 ? 34.556 58.225 12.522  1.00 14.51 ? 177  SER A CA  1 
ATOM   1383 C  C   . SER A 1 177 ? 33.185 57.634 12.217  1.00 12.31 ? 177  SER A C   1 
ATOM   1384 O  O   . SER A 1 177 ? 32.424 57.350 13.138  1.00 12.33 ? 177  SER A O   1 
ATOM   1385 C  CB  . SER A 1 177 ? 34.496 59.751 12.495  1.00 19.01 ? 177  SER A CB  1 
ATOM   1386 O  OG  . SER A 1 177 ? 35.746 60.297 12.888  1.00 23.11 ? 177  SER A OG  1 
ATOM   1387 N  N   . MET A 1 178 ? 32.865 57.456 10.936  1.00 11.23 ? 178  MET A N   1 
ATOM   1388 C  CA  . MET A 1 178 ? 31.578 56.878 10.539  1.00 14.37 ? 178  MET A CA  1 
ATOM   1389 C  C   . MET A 1 178 ? 31.485 55.466 11.097  1.00 14.80 ? 178  MET A C   1 
ATOM   1390 O  O   . MET A 1 178 ? 30.468 55.078 11.675  1.00 16.05 ? 178  MET A O   1 
ATOM   1391 C  CB  . MET A 1 178 ? 31.446 56.818 9.018   1.00 20.34 ? 178  MET A CB  1 
ATOM   1392 C  CG  . MET A 1 178 ? 31.127 58.139 8.355   1.00 26.17 ? 178  MET A CG  1 
ATOM   1393 S  SD  . MET A 1 178 ? 29.486 58.738 8.782   1.00 36.35 ? 178  MET A SD  1 
ATOM   1394 C  CE  . MET A 1 178 ? 29.923 60.062 9.916   1.00 34.35 ? 178  MET A CE  1 
ATOM   1395 N  N   . ILE A 1 179 ? 32.564 54.710 10.930  1.00 12.38 ? 179  ILE A N   1 
ATOM   1396 C  CA  . ILE A 1 179 ? 32.632 53.344 11.420  1.00 11.76 ? 179  ILE A CA  1 
ATOM   1397 C  C   . ILE A 1 179 ? 32.560 53.310 12.940  1.00 12.29 ? 179  ILE A C   1 
ATOM   1398 O  O   . ILE A 1 179 ? 31.829 52.499 13.504  1.00 16.66 ? 179  ILE A O   1 
ATOM   1399 C  CB  . ILE A 1 179 ? 33.905 52.642 10.918  1.00 11.13 ? 179  ILE A CB  1 
ATOM   1400 C  CG1 . ILE A 1 179 ? 33.791 52.411 9.409   1.00 6.81  ? 179  ILE A CG1 1 
ATOM   1401 C  CG2 . ILE A 1 179 ? 34.127 51.330 11.666  1.00 9.92  ? 179  ILE A CG2 1 
ATOM   1402 C  CD1 . ILE A 1 179 ? 35.090 52.042 8.752   1.00 12.86 ? 179  ILE A CD1 1 
ATOM   1403 N  N   . ALA A 1 180 ? 33.290 54.205 13.603  1.00 11.60 ? 180  ALA A N   1 
ATOM   1404 C  CA  . ALA A 1 180 ? 33.278 54.257 15.066  1.00 9.67  ? 180  ALA A CA  1 
ATOM   1405 C  C   . ALA A 1 180 ? 31.878 54.552 15.603  1.00 10.16 ? 180  ALA A C   1 
ATOM   1406 O  O   . ALA A 1 180 ? 31.451 53.972 16.595  1.00 10.90 ? 180  ALA A O   1 
ATOM   1407 C  CB  . ALA A 1 180 ? 34.258 55.294 15.569  1.00 9.00  ? 180  ALA A CB  1 
ATOM   1408 N  N   . ASP A 1 181 ? 31.159 55.454 14.945  1.00 12.18 ? 181  ASP A N   1 
ATOM   1409 C  CA  . ASP A 1 181 ? 29.807 55.795 15.377  1.00 12.55 ? 181  ASP A CA  1 
ATOM   1410 C  C   . ASP A 1 181 ? 28.884 54.589 15.280  1.00 11.25 ? 181  ASP A C   1 
ATOM   1411 O  O   . ASP A 1 181 ? 28.011 54.395 16.129  1.00 14.88 ? 181  ASP A O   1 
ATOM   1412 C  CB  . ASP A 1 181 ? 29.252 56.963 14.560  1.00 14.35 ? 181  ASP A CB  1 
ATOM   1413 C  CG  . ASP A 1 181 ? 29.990 58.274 14.822  1.00 18.28 ? 181  ASP A CG  1 
ATOM   1414 O  OD1 . ASP A 1 181 ? 30.823 58.338 15.755  1.00 14.45 ? 181  ASP A OD1 1 
ATOM   1415 O  OD2 . ASP A 1 181 ? 29.739 59.247 14.081  1.00 20.24 ? 181  ASP A OD2 1 
ATOM   1416 N  N   . TYR A 1 182 ? 29.101 53.766 14.260  1.00 10.93 ? 182  TYR A N   1 
ATOM   1417 C  CA  . TYR A 1 182 ? 28.301 52.565 14.054  1.00 9.29  ? 182  TYR A CA  1 
ATOM   1418 C  C   . TYR A 1 182 ? 28.582 51.579 15.187  1.00 9.22  ? 182  TYR A C   1 
ATOM   1419 O  O   . TYR A 1 182 ? 27.660 51.101 15.844  1.00 12.10 ? 182  TYR A O   1 
ATOM   1420 C  CB  . TYR A 1 182 ? 28.623 51.952 12.681  1.00 11.53 ? 182  TYR A CB  1 
ATOM   1421 C  CG  . TYR A 1 182 ? 28.191 50.510 12.494  1.00 12.64 ? 182  TYR A CG  1 
ATOM   1422 C  CD1 . TYR A 1 182 ? 26.876 50.105 12.742  1.00 13.11 ? 182  TYR A CD1 1 
ATOM   1423 C  CD2 . TYR A 1 182 ? 29.112 49.542 12.089  1.00 12.47 ? 182  TYR A CD2 1 
ATOM   1424 C  CE1 . TYR A 1 182 ? 26.493 48.768 12.596  1.00 13.08 ? 182  TYR A CE1 1 
ATOM   1425 C  CE2 . TYR A 1 182 ? 28.740 48.212 11.941  1.00 14.40 ? 182  TYR A CE2 1 
ATOM   1426 C  CZ  . TYR A 1 182 ? 27.431 47.829 12.199  1.00 14.45 ? 182  TYR A CZ  1 
ATOM   1427 O  OH  . TYR A 1 182 ? 27.074 46.503 12.070  1.00 13.00 ? 182  TYR A OH  1 
ATOM   1428 N  N   . LEU A 1 183 ? 29.861 51.341 15.460  1.00 6.74  ? 183  LEU A N   1 
ATOM   1429 C  CA  . LEU A 1 183 ? 30.260 50.413 16.512  1.00 7.42  ? 183  LEU A CA  1 
ATOM   1430 C  C   . LEU A 1 183 ? 29.846 50.902 17.892  1.00 8.75  ? 183  LEU A C   1 
ATOM   1431 O  O   . LEU A 1 183 ? 29.405 50.112 18.731  1.00 12.16 ? 183  LEU A O   1 
ATOM   1432 C  CB  . LEU A 1 183 ? 31.767 50.169 16.462  1.00 2.74  ? 183  LEU A CB  1 
ATOM   1433 C  CG  . LEU A 1 183 ? 32.272 49.621 15.125  1.00 6.92  ? 183  LEU A CG  1 
ATOM   1434 C  CD1 . LEU A 1 183 ? 33.755 49.310 15.208  1.00 4.75  ? 183  LEU A CD1 1 
ATOM   1435 C  CD2 . LEU A 1 183 ? 31.483 48.378 14.745  1.00 9.44  ? 183  LEU A CD2 1 
ATOM   1436 N  N   . ASN A 1 184 ? 29.959 52.208 18.115  1.00 11.74 ? 184  ASN A N   1 
ATOM   1437 C  CA  . ASN A 1 184 ? 29.591 52.811 19.393  1.00 8.49  ? 184  ASN A CA  1 
ATOM   1438 C  C   . ASN A 1 184 ? 28.114 52.669 19.702  1.00 8.16  ? 184  ASN A C   1 
ATOM   1439 O  O   . ASN A 1 184 ? 27.737 52.499 20.858  1.00 12.40 ? 184  ASN A O   1 
ATOM   1440 C  CB  . ASN A 1 184 ? 29.996 54.279 19.434  1.00 12.10 ? 184  ASN A CB  1 
ATOM   1441 C  CG  . ASN A 1 184 ? 31.417 54.467 19.905  1.00 12.06 ? 184  ASN A CG  1 
ATOM   1442 O  OD1 . ASN A 1 184 ? 31.929 53.664 20.682  1.00 15.80 ? 184  ASN A OD1 1 
ATOM   1443 N  ND2 . ASN A 1 184 ? 32.064 55.529 19.453  1.00 12.32 ? 184  ASN A ND2 1 
ATOM   1444 N  N   . LYS A 1 185 ? 27.283 52.726 18.667  1.00 11.36 ? 185  LYS A N   1 
ATOM   1445 C  CA  . LYS A 1 185 ? 25.840 52.582 18.820  1.00 12.71 ? 185  LYS A CA  1 
ATOM   1446 C  C   . LYS A 1 185 ? 25.535 51.177 19.328  1.00 13.98 ? 185  LYS A C   1 
ATOM   1447 O  O   . LYS A 1 185 ? 24.694 50.990 20.208  1.00 16.69 ? 185  LYS A O   1 
ATOM   1448 C  CB  . LYS A 1 185 ? 25.152 52.803 17.480  1.00 14.25 ? 185  LYS A CB  1 
ATOM   1449 C  CG  . LYS A 1 185 ? 23.645 52.690 17.536  1.00 22.44 ? 185  LYS A CG  1 
ATOM   1450 C  CD  . LYS A 1 185 ? 23.046 52.792 16.142  1.00 23.32 ? 185  LYS A CD  1 
ATOM   1451 C  CE  . LYS A 1 185 ? 21.524 52.721 16.176  1.00 25.38 ? 185  LYS A CE  1 
ATOM   1452 N  NZ  . LYS A 1 185 ? 20.970 52.843 14.797  1.00 30.24 ? 185  LYS A NZ  1 
ATOM   1453 N  N   . LEU A 1 186 ? 26.232 50.196 18.762  1.00 15.00 ? 186  LEU A N   1 
ATOM   1454 C  CA  . LEU A 1 186 ? 26.087 48.793 19.139  1.00 9.81  ? 186  LEU A CA  1 
ATOM   1455 C  C   . LEU A 1 186 ? 26.556 48.578 20.577  1.00 10.89 ? 186  LEU A C   1 
ATOM   1456 O  O   . LEU A 1 186 ? 25.866 47.931 21.380  1.00 9.80  ? 186  LEU A O   1 
ATOM   1457 C  CB  . LEU A 1 186 ? 26.900 47.916 18.180  1.00 11.33 ? 186  LEU A CB  1 
ATOM   1458 C  CG  . LEU A 1 186 ? 26.257 47.424 16.880  1.00 6.00  ? 186  LEU A CG  1 
ATOM   1459 C  CD1 . LEU A 1 186 ? 25.219 48.383 16.372  1.00 11.90 ? 186  LEU A CD1 1 
ATOM   1460 C  CD2 . LEU A 1 186 ? 27.335 47.201 15.841  1.00 6.60  ? 186  LEU A CD2 1 
ATOM   1461 N  N   . ILE A 1 187 ? 27.723 49.124 20.906  1.00 6.57  ? 187  ILE A N   1 
ATOM   1462 C  CA  . ILE A 1 187 ? 28.258 49.001 22.256  1.00 7.12  ? 187  ILE A CA  1 
ATOM   1463 C  C   . ILE A 1 187 ? 27.256 49.544 23.278  1.00 9.29  ? 187  ILE A C   1 
ATOM   1464 O  O   . ILE A 1 187 ? 26.987 48.905 24.291  1.00 8.63  ? 187  ILE A O   1 
ATOM   1465 C  CB  . ILE A 1 187 ? 29.601 49.740 22.398  1.00 7.98  ? 187  ILE A CB  1 
ATOM   1466 C  CG1 . ILE A 1 187 ? 30.651 49.088 21.499  1.00 3.90  ? 187  ILE A CG1 1 
ATOM   1467 C  CG2 . ILE A 1 187 ? 30.063 49.740 23.858  1.00 7.72  ? 187  ILE A CG2 1 
ATOM   1468 C  CD1 . ILE A 1 187 ? 32.018 49.700 21.631  1.00 3.08  ? 187  ILE A CD1 1 
ATOM   1469 N  N   . ASP A 1 188 ? 26.683 50.711 22.992  1.00 11.99 ? 188  ASP A N   1 
ATOM   1470 C  CA  . ASP A 1 188 ? 25.703 51.325 23.882  1.00 11.40 ? 188  ASP A CA  1 
ATOM   1471 C  C   . ASP A 1 188 ? 24.456 50.452 24.006  1.00 12.70 ? 188  ASP A C   1 
ATOM   1472 O  O   . ASP A 1 188 ? 23.833 50.391 25.068  1.00 12.60 ? 188  ASP A O   1 
ATOM   1473 C  CB  . ASP A 1 188 ? 25.333 52.728 23.392  1.00 12.91 ? 188  ASP A CB  1 
ATOM   1474 C  CG  . ASP A 1 188 ? 26.414 53.767 23.687  1.00 12.57 ? 188  ASP A CG  1 
ATOM   1475 O  OD1 . ASP A 1 188 ? 27.466 53.431 24.274  1.00 13.54 ? 188  ASP A OD1 1 
ATOM   1476 O  OD2 . ASP A 1 188 ? 26.203 54.936 23.326  1.00 13.01 ? 188  ASP A OD2 1 
ATOM   1477 N  N   . ILE A 1 189 ? 24.088 49.787 22.915  1.00 13.07 ? 189  ILE A N   1 
ATOM   1478 C  CA  . ILE A 1 189 ? 22.936 48.889 22.921  1.00 13.02 ? 189  ILE A CA  1 
ATOM   1479 C  C   . ILE A 1 189 ? 23.198 47.732 23.896  1.00 11.65 ? 189  ILE A C   1 
ATOM   1480 O  O   . ILE A 1 189 ? 22.282 47.259 24.560  1.00 16.56 ? 189  ILE A O   1 
ATOM   1481 C  CB  . ILE A 1 189 ? 22.618 48.366 21.495  1.00 9.63  ? 189  ILE A CB  1 
ATOM   1482 C  CG1 . ILE A 1 189 ? 21.991 49.491 20.667  1.00 8.61  ? 189  ILE A CG1 1 
ATOM   1483 C  CG2 . ILE A 1 189 ? 21.690 47.161 21.550  1.00 12.21 ? 189  ILE A CG2 1 
ATOM   1484 C  CD1 . ILE A 1 189 ? 21.776 49.166 19.196  1.00 6.80  ? 189  ILE A CD1 1 
ATOM   1485 N  N   . GLY A 1 190 ? 24.456 47.324 24.024  1.00 12.72 ? 190  GLY A N   1 
ATOM   1486 C  CA  . GLY A 1 190 ? 24.792 46.253 24.947  1.00 10.30 ? 190  GLY A CA  1 
ATOM   1487 C  C   . GLY A 1 190 ? 25.743 45.190 24.416  1.00 12.85 ? 190  GLY A C   1 
ATOM   1488 O  O   . GLY A 1 190 ? 26.029 44.222 25.123  1.00 16.46 ? 190  GLY A O   1 
ATOM   1489 N  N   . VAL A 1 191 ? 26.211 45.347 23.181  1.00 11.72 ? 191  VAL A N   1 
ATOM   1490 C  CA  . VAL A 1 191 ? 27.134 44.390 22.571  1.00 11.05 ? 191  VAL A CA  1 
ATOM   1491 C  C   . VAL A 1 191 ? 28.448 44.337 23.361  1.00 14.53 ? 191  VAL A C   1 
ATOM   1492 O  O   . VAL A 1 191 ? 28.894 45.355 23.895  1.00 16.38 ? 191  VAL A O   1 
ATOM   1493 C  CB  . VAL A 1 191 ? 27.356 44.740 21.080  1.00 10.18 ? 191  VAL A CB  1 
ATOM   1494 C  CG1 . VAL A 1 191 ? 28.548 44.007 20.508  1.00 13.42 ? 191  VAL A CG1 1 
ATOM   1495 C  CG2 . VAL A 1 191 ? 26.105 44.381 20.285  1.00 8.03  ? 191  VAL A CG2 1 
ATOM   1496 N  N   . ALA A 1 192 ? 29.037 43.146 23.472  1.00 13.07 ? 192  ALA A N   1 
ATOM   1497 C  CA  . ALA A 1 192 ? 30.280 42.953 24.230  1.00 10.13 ? 192  ALA A CA  1 
ATOM   1498 C  C   . ALA A 1 192 ? 31.586 43.008 23.441  1.00 9.50  ? 192  ALA A C   1 
ATOM   1499 O  O   . ALA A 1 192 ? 32.666 43.134 24.025  1.00 10.68 ? 192  ALA A O   1 
ATOM   1500 C  CB  . ALA A 1 192 ? 30.213 41.650 25.005  1.00 11.37 ? 192  ALA A CB  1 
ATOM   1501 N  N   . GLY A 1 193 ? 31.505 42.889 22.124  1.00 9.53  ? 193  GLY A N   1 
ATOM   1502 C  CA  . GLY A 1 193 ? 32.716 42.911 21.334  1.00 6.78  ? 193  GLY A CA  1 
ATOM   1503 C  C   . GLY A 1 193 ? 32.436 42.705 19.870  1.00 4.58  ? 193  GLY A C   1 
ATOM   1504 O  O   . GLY A 1 193 ? 31.279 42.562 19.481  1.00 4.76  ? 193  GLY A O   1 
ATOM   1505 N  N   . PHE A 1 194 ? 33.489 42.623 19.066  1.00 5.27  ? 194  PHE A N   1 
ATOM   1506 C  CA  . PHE A 1 194 ? 33.312 42.485 17.625  1.00 8.28  ? 194  PHE A CA  1 
ATOM   1507 C  C   . PHE A 1 194 ? 34.278 41.544 16.957  1.00 10.32 ? 194  PHE A C   1 
ATOM   1508 O  O   . PHE A 1 194 ? 35.374 41.278 17.453  1.00 11.28 ? 194  PHE A O   1 
ATOM   1509 C  CB  . PHE A 1 194 ? 33.513 43.842 16.930  1.00 6.35  ? 194  PHE A CB  1 
ATOM   1510 C  CG  . PHE A 1 194 ? 32.668 44.943 17.480  1.00 9.04  ? 194  PHE A CG  1 
ATOM   1511 C  CD1 . PHE A 1 194 ? 31.359 45.111 17.048  1.00 5.98  ? 194  PHE A CD1 1 
ATOM   1512 C  CD2 . PHE A 1 194 ? 33.179 45.809 18.442  1.00 9.42  ? 194  PHE A CD2 1 
ATOM   1513 C  CE1 . PHE A 1 194 ? 30.567 46.119 17.565  1.00 6.25  ? 194  PHE A CE1 1 
ATOM   1514 C  CE2 . PHE A 1 194 ? 32.393 46.824 18.968  1.00 10.33 ? 194  PHE A CE2 1 
ATOM   1515 C  CZ  . PHE A 1 194 ? 31.081 46.979 18.527  1.00 9.02  ? 194  PHE A CZ  1 
ATOM   1516 N  N   . ARG A 1 195 ? 33.873 41.086 15.784  1.00 11.37 ? 195  ARG A N   1 
ATOM   1517 C  CA  . ARG A 1 195 ? 34.718 40.255 14.966  1.00 12.27 ? 195  ARG A CA  1 
ATOM   1518 C  C   . ARG A 1 195 ? 35.017 41.218 13.847  1.00 13.07 ? 195  ARG A C   1 
ATOM   1519 O  O   . ARG A 1 195 ? 34.087 41.671 13.167  1.00 19.63 ? 195  ARG A O   1 
ATOM   1520 C  CB  . ARG A 1 195 ? 33.964 39.076 14.376  1.00 10.98 ? 195  ARG A CB  1 
ATOM   1521 C  CG  . ARG A 1 195 ? 34.903 38.161 13.631  1.00 14.91 ? 195  ARG A CG  1 
ATOM   1522 C  CD  . ARG A 1 195 ? 34.168 37.204 12.770  1.00 13.65 ? 195  ARG A CD  1 
ATOM   1523 N  NE  . ARG A 1 195 ? 33.826 37.846 11.522  1.00 17.33 ? 195  ARG A NE  1 
ATOM   1524 C  CZ  . ARG A 1 195 ? 34.117 37.334 10.339  1.00 14.46 ? 195  ARG A CZ  1 
ATOM   1525 N  NH1 . ARG A 1 195 ? 34.744 36.172 10.277  1.00 12.56 ? 195  ARG A NH1 1 
ATOM   1526 N  NH2 . ARG A 1 195 ? 33.775 37.981 9.237   1.00 8.36  ? 195  ARG A NH2 1 
ATOM   1527 N  N   . ILE A 1 196 ? 36.277 41.594 13.684  1.00 11.66 ? 196  ILE A N   1 
ATOM   1528 C  CA  . ILE A 1 196 ? 36.621 42.518 12.616  1.00 10.30 ? 196  ILE A CA  1 
ATOM   1529 C  C   . ILE A 1 196 ? 36.830 41.711 11.342  1.00 10.02 ? 196  ILE A C   1 
ATOM   1530 O  O   . ILE A 1 196 ? 37.847 41.022 11.170  1.00 8.43  ? 196  ILE A O   1 
ATOM   1531 C  CB  . ILE A 1 196 ? 37.879 43.362 12.935  1.00 12.48 ? 196  ILE A CB  1 
ATOM   1532 C  CG1 . ILE A 1 196 ? 37.743 44.033 14.307  1.00 8.45  ? 196  ILE A CG1 1 
ATOM   1533 C  CG2 . ILE A 1 196 ? 38.075 44.425 11.847  1.00 10.30 ? 196  ILE A CG2 1 
ATOM   1534 C  CD1 . ILE A 1 196 ? 36.525 44.911 14.443  1.00 8.31  ? 196  ILE A CD1 1 
ATOM   1535 N  N   . ASP A 1 197 ? 35.840 41.786 10.463  1.00 8.60  ? 197  ASP A N   1 
ATOM   1536 C  CA  . ASP A 1 197 ? 35.860 41.072 9.199   1.00 7.72  ? 197  ASP A CA  1 
ATOM   1537 C  C   . ASP A 1 197 ? 36.924 41.593 8.240   1.00 10.20 ? 197  ASP A C   1 
ATOM   1538 O  O   . ASP A 1 197 ? 37.076 42.803 8.064   1.00 15.10 ? 197  ASP A O   1 
ATOM   1539 C  CB  . ASP A 1 197 ? 34.477 41.168 8.551   1.00 8.22  ? 197  ASP A CB  1 
ATOM   1540 C  CG  . ASP A 1 197 ? 34.441 40.583 7.158   1.00 7.68  ? 197  ASP A CG  1 
ATOM   1541 O  OD1 . ASP A 1 197 ? 34.438 39.347 7.027   1.00 6.52  ? 197  ASP A OD1 1 
ATOM   1542 O  OD2 . ASP A 1 197 ? 34.412 41.362 6.189   1.00 12.06 ? 197  ASP A OD2 1 
ATOM   1543 N  N   . ALA A 1 198 ? 37.636 40.664 7.605   1.00 10.84 ? 198  ALA A N   1 
ATOM   1544 C  CA  . ALA A 1 198 ? 38.680 40.973 6.626   1.00 5.50  ? 198  ALA A CA  1 
ATOM   1545 C  C   . ALA A 1 198 ? 39.734 41.947 7.132   1.00 7.35  ? 198  ALA A C   1 
ATOM   1546 O  O   . ALA A 1 198 ? 40.118 42.878 6.412   1.00 6.44  ? 198  ALA A O   1 
ATOM   1547 C  CB  . ALA A 1 198 ? 38.047 41.503 5.332   1.00 4.19  ? 198  ALA A CB  1 
ATOM   1548 N  N   . SER A 1 199 ? 40.232 41.705 8.342   1.00 8.79  ? 199  SER A N   1 
ATOM   1549 C  CA  . SER A 1 199 ? 41.246 42.565 8.955   1.00 10.33 ? 199  SER A CA  1 
ATOM   1550 C  C   . SER A 1 199 ? 42.540 42.599 8.161   1.00 9.70  ? 199  SER A C   1 
ATOM   1551 O  O   . SER A 1 199 ? 43.222 43.617 8.094   1.00 12.90 ? 199  SER A O   1 
ATOM   1552 C  CB  . SER A 1 199 ? 41.522 42.125 10.390  1.00 7.75  ? 199  SER A CB  1 
ATOM   1553 O  OG  . SER A 1 199 ? 40.392 42.383 11.206  1.00 10.72 ? 199  SER A OG  1 
ATOM   1554 N  N   . LYS A 1 200 ? 42.859 41.472 7.553   1.00 8.76  ? 200  LYS A N   1 
ATOM   1555 C  CA  . LYS A 1 200 ? 44.054 41.330 6.744   1.00 9.01  ? 200  LYS A CA  1 
ATOM   1556 C  C   . LYS A 1 200 ? 44.064 42.371 5.614   1.00 10.39 ? 200  LYS A C   1 
ATOM   1557 O  O   . LYS A 1 200 ? 45.115 42.702 5.070   1.00 11.76 ? 200  LYS A O   1 
ATOM   1558 C  CB  . LYS A 1 200 ? 44.052 39.914 6.167   1.00 8.91  ? 200  LYS A CB  1 
ATOM   1559 C  CG  . LYS A 1 200 ? 45.192 39.537 5.250   1.00 13.14 ? 200  LYS A CG  1 
ATOM   1560 C  CD  . LYS A 1 200 ? 45.017 38.078 4.902   1.00 15.25 ? 200  LYS A CD  1 
ATOM   1561 C  CE  . LYS A 1 200 ? 46.035 37.582 3.922   1.00 14.94 ? 200  LYS A CE  1 
ATOM   1562 N  NZ  . LYS A 1 200 ? 45.918 36.106 3.835   1.00 13.03 ? 200  LYS A NZ  1 
ATOM   1563 N  N   . HIS A 1 201 ? 42.888 42.879 5.259   1.00 9.84  ? 201  HIS A N   1 
ATOM   1564 C  CA  . HIS A 1 201 ? 42.774 43.852 4.184   1.00 10.13 ? 201  HIS A CA  1 
ATOM   1565 C  C   . HIS A 1 201 ? 42.715 45.297 4.664   1.00 10.85 ? 201  HIS A C   1 
ATOM   1566 O  O   . HIS A 1 201 ? 42.285 46.204 3.924   1.00 12.54 ? 201  HIS A O   1 
ATOM   1567 C  CB  . HIS A 1 201 ? 41.576 43.493 3.309   1.00 8.02  ? 201  HIS A CB  1 
ATOM   1568 C  CG  . HIS A 1 201 ? 41.677 42.124 2.717   1.00 9.30  ? 201  HIS A CG  1 
ATOM   1569 N  ND1 . HIS A 1 201 ? 42.337 41.875 1.536   1.00 9.48  ? 201  HIS A ND1 1 
ATOM   1570 C  CD2 . HIS A 1 201 ? 41.269 40.921 3.182   1.00 5.83  ? 201  HIS A CD2 1 
ATOM   1571 C  CE1 . HIS A 1 201 ? 42.337 40.575 1.298   1.00 12.07 ? 201  HIS A CE1 1 
ATOM   1572 N  NE2 . HIS A 1 201 ? 41.696 39.976 2.283   1.00 10.22 ? 201  HIS A NE2 1 
ATOM   1573 N  N   . MET A 1 202 ? 43.182 45.505 5.891   1.00 8.49  ? 202  MET A N   1 
ATOM   1574 C  CA  . MET A 1 202 ? 43.229 46.817 6.512   1.00 10.17 ? 202  MET A CA  1 
ATOM   1575 C  C   . MET A 1 202 ? 44.561 46.938 7.230   1.00 12.42 ? 202  MET A C   1 
ATOM   1576 O  O   . MET A 1 202 ? 45.161 45.937 7.614   1.00 15.18 ? 202  MET A O   1 
ATOM   1577 C  CB  . MET A 1 202 ? 42.082 46.985 7.512   1.00 9.86  ? 202  MET A CB  1 
ATOM   1578 C  CG  . MET A 1 202 ? 40.710 47.048 6.860   1.00 13.01 ? 202  MET A CG  1 
ATOM   1579 S  SD  . MET A 1 202 ? 39.395 47.306 8.043   1.00 14.56 ? 202  MET A SD  1 
ATOM   1580 C  CE  . MET A 1 202 ? 39.129 45.646 8.639   1.00 12.94 ? 202  MET A CE  1 
ATOM   1581 N  N   . TRP A 1 203 ? 45.064 48.158 7.351   1.00 11.29 ? 203  TRP A N   1 
ATOM   1582 C  CA  . TRP A 1 203 ? 46.320 48.371 8.038   1.00 5.50  ? 203  TRP A CA  1 
ATOM   1583 C  C   . TRP A 1 203 ? 46.036 48.295 9.528   1.00 8.25  ? 203  TRP A C   1 
ATOM   1584 O  O   . TRP A 1 203 ? 45.034 48.842 10.004  1.00 12.91 ? 203  TRP A O   1 
ATOM   1585 C  CB  . TRP A 1 203 ? 46.900 49.738 7.668   1.00 6.70  ? 203  TRP A CB  1 
ATOM   1586 C  CG  . TRP A 1 203 ? 47.232 49.849 6.224   1.00 5.94  ? 203  TRP A CG  1 
ATOM   1587 C  CD1 . TRP A 1 203 ? 46.430 50.336 5.232   1.00 8.46  ? 203  TRP A CD1 1 
ATOM   1588 C  CD2 . TRP A 1 203 ? 48.440 49.416 5.586   1.00 8.80  ? 203  TRP A CD2 1 
ATOM   1589 N  NE1 . TRP A 1 203 ? 47.062 50.229 4.014   1.00 7.53  ? 203  TRP A NE1 1 
ATOM   1590 C  CE2 . TRP A 1 203 ? 48.296 49.669 4.204   1.00 8.25  ? 203  TRP A CE2 1 
ATOM   1591 C  CE3 . TRP A 1 203 ? 49.627 48.834 6.050   1.00 9.01  ? 203  TRP A CE3 1 
ATOM   1592 C  CZ2 . TRP A 1 203 ? 49.298 49.360 3.278   1.00 10.52 ? 203  TRP A CZ2 1 
ATOM   1593 C  CZ3 . TRP A 1 203 ? 50.620 48.527 5.130   1.00 8.45  ? 203  TRP A CZ3 1 
ATOM   1594 C  CH2 . TRP A 1 203 ? 50.448 48.791 3.759   1.00 10.33 ? 203  TRP A CH2 1 
ATOM   1595 N  N   . PRO A 1 204 ? 46.883 47.579 10.286  1.00 9.45  ? 204  PRO A N   1 
ATOM   1596 C  CA  . PRO A 1 204 ? 46.691 47.455 11.731  1.00 8.06  ? 204  PRO A CA  1 
ATOM   1597 C  C   . PRO A 1 204 ? 46.482 48.819 12.388  1.00 9.55  ? 204  PRO A C   1 
ATOM   1598 O  O   . PRO A 1 204 ? 45.700 48.946 13.332  1.00 16.10 ? 204  PRO A O   1 
ATOM   1599 C  CB  . PRO A 1 204 ? 48.002 46.812 12.183  1.00 7.91  ? 204  PRO A CB  1 
ATOM   1600 C  CG  . PRO A 1 204 ? 48.330 45.932 11.046  1.00 7.28  ? 204  PRO A CG  1 
ATOM   1601 C  CD  . PRO A 1 204 ? 48.071 46.821 9.856   1.00 7.07  ? 204  PRO A CD  1 
ATOM   1602 N  N   . GLY A 1 205 ? 47.170 49.833 11.869  1.00 11.75 ? 205  GLY A N   1 
ATOM   1603 C  CA  . GLY A 1 205 ? 47.054 51.183 12.398  1.00 8.77  ? 205  GLY A CA  1 
ATOM   1604 C  C   . GLY A 1 205 ? 45.679 51.790 12.201  1.00 9.37  ? 205  GLY A C   1 
ATOM   1605 O  O   . GLY A 1 205 ? 45.172 52.476 13.085  1.00 14.53 ? 205  GLY A O   1 
ATOM   1606 N  N   . ASP A 1 206 ? 45.074 51.552 11.044  1.00 8.19  ? 206  ASP A N   1 
ATOM   1607 C  CA  . ASP A 1 206 ? 43.741 52.073 10.773  1.00 10.35 ? 206  ASP A CA  1 
ATOM   1608 C  C   . ASP A 1 206 ? 42.714 51.455 11.711  1.00 14.17 ? 206  ASP A C   1 
ATOM   1609 O  O   . ASP A 1 206 ? 41.834 52.149 12.219  1.00 19.27 ? 206  ASP A O   1 
ATOM   1610 C  CB  . ASP A 1 206 ? 43.347 51.817 9.321   1.00 12.90 ? 206  ASP A CB  1 
ATOM   1611 C  CG  . ASP A 1 206 ? 44.158 52.641 8.344   1.00 14.60 ? 206  ASP A CG  1 
ATOM   1612 O  OD1 . ASP A 1 206 ? 44.900 53.555 8.782   1.00 14.66 ? 206  ASP A OD1 1 
ATOM   1613 O  OD2 . ASP A 1 206 ? 44.048 52.372 7.132   1.00 13.16 ? 206  ASP A OD2 1 
ATOM   1614 N  N   . ILE A 1 207 ? 42.834 50.152 11.949  1.00 13.93 ? 207  ILE A N   1 
ATOM   1615 C  CA  . ILE A 1 207 ? 41.920 49.451 12.849  1.00 12.11 ? 207  ILE A CA  1 
ATOM   1616 C  C   . ILE A 1 207 ? 42.094 50.033 14.250  1.00 12.61 ? 207  ILE A C   1 
ATOM   1617 O  O   . ILE A 1 207 ? 41.118 50.303 14.952  1.00 13.06 ? 207  ILE A O   1 
ATOM   1618 C  CB  . ILE A 1 207 ? 42.229 47.934 12.898  1.00 12.42 ? 207  ILE A CB  1 
ATOM   1619 C  CG1 . ILE A 1 207 ? 42.060 47.312 11.509  1.00 9.46  ? 207  ILE A CG1 1 
ATOM   1620 C  CG2 . ILE A 1 207 ? 41.317 47.238 13.895  1.00 11.07 ? 207  ILE A CG2 1 
ATOM   1621 C  CD1 . ILE A 1 207 ? 42.470 45.858 11.427  1.00 7.28  ? 207  ILE A CD1 1 
ATOM   1622 N  N   . LYS A 1 208 ? 43.347 50.243 14.639  1.00 12.49 ? 208  LYS A N   1 
ATOM   1623 C  CA  . LYS A 1 208 ? 43.669 50.801 15.946  1.00 14.80 ? 208  LYS A CA  1 
ATOM   1624 C  C   . LYS A 1 208 ? 43.012 52.169 16.132  1.00 13.90 ? 208  LYS A C   1 
ATOM   1625 O  O   . LYS A 1 208 ? 42.366 52.417 17.152  1.00 13.66 ? 208  LYS A O   1 
ATOM   1626 C  CB  . LYS A 1 208 ? 45.183 50.923 16.115  1.00 16.07 ? 208  LYS A CB  1 
ATOM   1627 C  CG  . LYS A 1 208 ? 45.620 51.267 17.533  1.00 26.67 ? 208  LYS A CG  1 
ATOM   1628 C  CD  . LYS A 1 208 ? 45.112 50.225 18.528  1.00 32.73 ? 208  LYS A CD  1 
ATOM   1629 C  CE  . LYS A 1 208 ? 45.541 50.533 19.955  1.00 37.48 ? 208  LYS A CE  1 
ATOM   1630 N  NZ  . LYS A 1 208 ? 44.977 49.529 20.910  1.00 41.80 ? 208  LYS A NZ  1 
ATOM   1631 N  N   . ALA A 1 209 ? 43.146 53.035 15.133  1.00 13.76 ? 209  ALA A N   1 
ATOM   1632 C  CA  . ALA A 1 209 ? 42.555 54.368 15.188  1.00 13.03 ? 209  ALA A CA  1 
ATOM   1633 C  C   . ALA A 1 209 ? 41.051 54.301 15.423  1.00 13.90 ? 209  ALA A C   1 
ATOM   1634 O  O   . ALA A 1 209 ? 40.493 55.147 16.117  1.00 19.47 ? 209  ALA A O   1 
ATOM   1635 C  CB  . ALA A 1 209 ? 42.855 55.122 13.918  1.00 13.64 ? 209  ALA A CB  1 
ATOM   1636 N  N   . VAL A 1 210 ? 40.398 53.300 14.833  1.00 14.06 ? 210  VAL A N   1 
ATOM   1637 C  CA  . VAL A 1 210 ? 38.958 53.100 15.006  1.00 9.59  ? 210  VAL A CA  1 
ATOM   1638 C  C   . VAL A 1 210 ? 38.667 52.602 16.430  1.00 11.48 ? 210  VAL A C   1 
ATOM   1639 O  O   . VAL A 1 210 ? 37.814 53.145 17.136  1.00 11.86 ? 210  VAL A O   1 
ATOM   1640 C  CB  . VAL A 1 210 ? 38.408 52.069 13.988  1.00 11.31 ? 210  VAL A CB  1 
ATOM   1641 C  CG1 . VAL A 1 210 ? 36.931 51.788 14.254  1.00 10.36 ? 210  VAL A CG1 1 
ATOM   1642 C  CG2 . VAL A 1 210 ? 38.592 52.585 12.572  1.00 7.81  ? 210  VAL A CG2 1 
ATOM   1643 N  N   . LEU A 1 211 ? 39.405 51.585 16.858  1.00 13.31 ? 211  LEU A N   1 
ATOM   1644 C  CA  . LEU A 1 211 ? 39.228 51.013 18.186  1.00 14.61 ? 211  LEU A CA  1 
ATOM   1645 C  C   . LEU A 1 211 ? 39.385 52.028 19.308  1.00 17.34 ? 211  LEU A C   1 
ATOM   1646 O  O   . LEU A 1 211 ? 38.640 51.993 20.288  1.00 19.95 ? 211  LEU A O   1 
ATOM   1647 C  CB  . LEU A 1 211 ? 40.198 49.852 18.394  1.00 16.74 ? 211  LEU A CB  1 
ATOM   1648 C  CG  . LEU A 1 211 ? 39.758 48.430 18.016  1.00 17.74 ? 211  LEU A CG  1 
ATOM   1649 C  CD1 . LEU A 1 211 ? 38.433 48.395 17.261  1.00 14.62 ? 211  LEU A CD1 1 
ATOM   1650 C  CD2 . LEU A 1 211 ? 40.863 47.781 17.211  1.00 15.24 ? 211  LEU A CD2 1 
ATOM   1651 N  N   . ASP A 1 212 ? 40.337 52.940 19.163  1.00 19.63 ? 212  ASP A N   1 
ATOM   1652 C  CA  . ASP A 1 212 ? 40.567 53.961 20.181  1.00 21.34 ? 212  ASP A CA  1 
ATOM   1653 C  C   . ASP A 1 212 ? 39.376 54.900 20.397  1.00 18.53 ? 212  ASP A C   1 
ATOM   1654 O  O   . ASP A 1 212 ? 39.296 55.580 21.420  1.00 19.39 ? 212  ASP A O   1 
ATOM   1655 C  CB  . ASP A 1 212 ? 41.821 54.777 19.847  1.00 27.11 ? 212  ASP A CB  1 
ATOM   1656 C  CG  . ASP A 1 212 ? 43.106 53.989 20.046  1.00 33.73 ? 212  ASP A CG  1 
ATOM   1657 O  OD1 . ASP A 1 212 ? 43.089 52.960 20.760  1.00 37.67 ? 212  ASP A OD1 1 
ATOM   1658 O  OD2 . ASP A 1 212 ? 44.145 54.406 19.490  1.00 38.25 ? 212  ASP A OD2 1 
ATOM   1659 N  N   . LYS A 1 213 ? 38.452 54.933 19.444  1.00 16.42 ? 213  LYS A N   1 
ATOM   1660 C  CA  . LYS A 1 213 ? 37.281 55.794 19.543  1.00 12.79 ? 213  LYS A CA  1 
ATOM   1661 C  C   . LYS A 1 213 ? 36.102 55.110 20.218  1.00 12.98 ? 213  LYS A C   1 
ATOM   1662 O  O   . LYS A 1 213 ? 35.099 55.757 20.515  1.00 17.77 ? 213  LYS A O   1 
ATOM   1663 C  CB  . LYS A 1 213 ? 36.847 56.244 18.146  1.00 11.86 ? 213  LYS A CB  1 
ATOM   1664 C  CG  . LYS A 1 213 ? 37.810 57.184 17.441  1.00 11.30 ? 213  LYS A CG  1 
ATOM   1665 C  CD  . LYS A 1 213 ? 37.321 57.480 16.025  1.00 13.47 ? 213  LYS A CD  1 
ATOM   1666 C  CE  . LYS A 1 213 ? 38.045 58.662 15.414  1.00 11.85 ? 213  LYS A CE  1 
ATOM   1667 N  NZ  . LYS A 1 213 ? 39.513 58.432 15.384  1.00 22.25 ? 213  LYS A NZ  1 
ATOM   1668 N  N   . LEU A 1 214 ? 36.216 53.811 20.463  1.00 14.18 ? 214  LEU A N   1 
ATOM   1669 C  CA  . LEU A 1 214 ? 35.126 53.048 21.055  1.00 10.61 ? 214  LEU A CA  1 
ATOM   1670 C  C   . LEU A 1 214 ? 34.801 53.327 22.509  1.00 10.75 ? 214  LEU A C   1 
ATOM   1671 O  O   . LEU A 1 214 ? 35.671 53.622 23.317  1.00 12.67 ? 214  LEU A O   1 
ATOM   1672 C  CB  . LEU A 1 214 ? 35.346 51.547 20.855  1.00 9.91  ? 214  LEU A CB  1 
ATOM   1673 C  CG  . LEU A 1 214 ? 35.518 51.096 19.403  1.00 12.70 ? 214  LEU A CG  1 
ATOM   1674 C  CD1 . LEU A 1 214 ? 35.504 49.583 19.339  1.00 15.51 ? 214  LEU A CD1 1 
ATOM   1675 C  CD2 . LEU A 1 214 ? 34.419 51.659 18.535  1.00 6.90  ? 214  LEU A CD2 1 
ATOM   1676 N  N   . HIS A 1 215 ? 33.515 53.212 22.816  1.00 11.73 ? 215  HIS A N   1 
ATOM   1677 C  CA  . HIS A 1 215 ? 32.976 53.422 24.146  1.00 9.54  ? 215  HIS A CA  1 
ATOM   1678 C  C   . HIS A 1 215 ? 33.294 52.218 25.033  1.00 13.47 ? 215  HIS A C   1 
ATOM   1679 O  O   . HIS A 1 215 ? 33.610 51.135 24.538  1.00 14.59 ? 215  HIS A O   1 
ATOM   1680 C  CB  . HIS A 1 215 ? 31.450 53.525 24.062  1.00 7.13  ? 215  HIS A CB  1 
ATOM   1681 C  CG  . HIS A 1 215 ? 30.944 54.806 23.472  1.00 9.56  ? 215  HIS A CG  1 
ATOM   1682 N  ND1 . HIS A 1 215 ? 29.600 55.046 23.275  1.00 10.67 ? 215  HIS A ND1 1 
ATOM   1683 C  CD2 . HIS A 1 215 ? 31.589 55.924 23.069  1.00 10.61 ? 215  HIS A CD2 1 
ATOM   1684 C  CE1 . HIS A 1 215 ? 29.439 56.260 22.778  1.00 10.38 ? 215  HIS A CE1 1 
ATOM   1685 N  NE2 . HIS A 1 215 ? 30.630 56.815 22.643  1.00 8.25  ? 215  HIS A NE2 1 
ATOM   1686 N  N   . ASN A 1 216 ? 33.213 52.420 26.344  1.00 16.17 ? 216  ASN A N   1 
ATOM   1687 C  CA  . ASN A 1 216 ? 33.403 51.338 27.303  1.00 13.98 ? 216  ASN A CA  1 
ATOM   1688 C  C   . ASN A 1 216 ? 32.073 50.591 27.263  1.00 14.47 ? 216  ASN A C   1 
ATOM   1689 O  O   . ASN A 1 216 ? 31.049 51.156 26.860  1.00 15.71 ? 216  ASN A O   1 
ATOM   1690 C  CB  . ASN A 1 216 ? 33.627 51.876 28.715  1.00 14.21 ? 216  ASN A CB  1 
ATOM   1691 C  CG  . ASN A 1 216 ? 34.968 52.552 28.883  1.00 15.79 ? 216  ASN A CG  1 
ATOM   1692 O  OD1 . ASN A 1 216 ? 35.916 52.293 28.138  1.00 14.11 ? 216  ASN A OD1 1 
ATOM   1693 N  ND2 . ASN A 1 216 ? 35.065 53.411 29.888  1.00 17.26 ? 216  ASN A ND2 1 
ATOM   1694 N  N   . LEU A 1 217 ? 32.068 49.345 27.707  1.00 14.85 ? 217  LEU A N   1 
ATOM   1695 C  CA  . LEU A 1 217 ? 30.854 48.546 27.680  1.00 12.95 ? 217  LEU A CA  1 
ATOM   1696 C  C   . LEU A 1 217 ? 29.749 49.079 28.588  1.00 14.18 ? 217  LEU A C   1 
ATOM   1697 O  O   . LEU A 1 217 ? 30.012 49.686 29.632  1.00 12.87 ? 217  LEU A O   1 
ATOM   1698 C  CB  . LEU A 1 217 ? 31.184 47.093 28.002  1.00 15.00 ? 217  LEU A CB  1 
ATOM   1699 C  CG  . LEU A 1 217 ? 32.229 46.489 27.063  1.00 13.83 ? 217  LEU A CG  1 
ATOM   1700 C  CD1 . LEU A 1 217 ? 32.463 45.042 27.427  1.00 14.73 ? 217  LEU A CD1 1 
ATOM   1701 C  CD2 . LEU A 1 217 ? 31.770 46.609 25.616  1.00 10.17 ? 217  LEU A CD2 1 
ATOM   1702 N  N   . ASN A 1 218 ? 28.511 48.847 28.167  1.00 10.72 ? 218  ASN A N   1 
ATOM   1703 C  CA  . ASN A 1 218 ? 27.329 49.301 28.887  1.00 14.61 ? 218  ASN A CA  1 
ATOM   1704 C  C   . ASN A 1 218 ? 27.319 48.790 30.331  1.00 18.73 ? 218  ASN A C   1 
ATOM   1705 O  O   . ASN A 1 218 ? 27.205 47.586 30.576  1.00 19.97 ? 218  ASN A O   1 
ATOM   1706 C  CB  . ASN A 1 218 ? 26.080 48.840 28.136  1.00 11.32 ? 218  ASN A CB  1 
ATOM   1707 C  CG  . ASN A 1 218 ? 24.809 49.441 28.686  1.00 14.04 ? 218  ASN A CG  1 
ATOM   1708 O  OD1 . ASN A 1 218 ? 24.631 49.552 29.898  1.00 14.53 ? 218  ASN A OD1 1 
ATOM   1709 N  ND2 . ASN A 1 218 ? 23.900 49.808 27.797  1.00 15.84 ? 218  ASN A ND2 1 
ATOM   1710 N  N   . THR A 1 219 ? 27.397 49.713 31.287  1.00 24.07 ? 219  THR A N   1 
ATOM   1711 C  CA  . THR A 1 219 ? 27.422 49.365 32.707  1.00 24.75 ? 219  THR A CA  1 
ATOM   1712 C  C   . THR A 1 219 ? 26.212 48.635 33.286  1.00 25.45 ? 219  THR A C   1 
ATOM   1713 O  O   . THR A 1 219 ? 26.244 48.226 34.447  1.00 29.00 ? 219  THR A O   1 
ATOM   1714 C  CB  . THR A 1 219 ? 27.758 50.579 33.586  1.00 23.12 ? 219  THR A CB  1 
ATOM   1715 O  OG1 . THR A 1 219 ? 26.940 51.691 33.206  1.00 30.28 ? 219  THR A OG1 1 
ATOM   1716 C  CG2 . THR A 1 219 ? 29.216 50.947 33.437  1.00 21.66 ? 219  THR A CG2 1 
ATOM   1717 N  N   . ASN A 1 220 ? 25.150 48.466 32.500  1.00 24.61 ? 220  ASN A N   1 
ATOM   1718 C  CA  . ASN A 1 220 ? 23.978 47.734 32.981  1.00 22.45 ? 220  ASN A CA  1 
ATOM   1719 C  C   . ASN A 1 220 ? 24.357 46.278 33.187  1.00 19.98 ? 220  ASN A C   1 
ATOM   1720 O  O   . ASN A 1 220 ? 23.753 45.585 34.003  1.00 25.13 ? 220  ASN A O   1 
ATOM   1721 C  CB  . ASN A 1 220 ? 22.821 47.787 31.978  1.00 29.29 ? 220  ASN A CB  1 
ATOM   1722 C  CG  . ASN A 1 220 ? 22.071 49.098 32.012  1.00 35.78 ? 220  ASN A CG  1 
ATOM   1723 O  OD1 . ASN A 1 220 ? 22.025 49.778 33.037  1.00 41.50 ? 220  ASN A OD1 1 
ATOM   1724 N  ND2 . ASN A 1 220 ? 21.462 49.456 30.890  1.00 40.37 ? 220  ASN A ND2 1 
ATOM   1725 N  N   . TRP A 1 221 ? 25.359 45.817 32.443  1.00 15.92 ? 221  TRP A N   1 
ATOM   1726 C  CA  . TRP A 1 221 ? 25.796 44.427 32.528  1.00 15.48 ? 221  TRP A CA  1 
ATOM   1727 C  C   . TRP A 1 221 ? 27.287 44.248 32.774  1.00 17.21 ? 221  TRP A C   1 
ATOM   1728 O  O   . TRP A 1 221 ? 27.713 43.225 33.317  1.00 24.41 ? 221  TRP A O   1 
ATOM   1729 C  CB  . TRP A 1 221 ? 25.424 43.684 31.246  1.00 11.89 ? 221  TRP A CB  1 
ATOM   1730 C  CG  . TRP A 1 221 ? 23.958 43.747 30.903  1.00 14.35 ? 221  TRP A CG  1 
ATOM   1731 C  CD1 . TRP A 1 221 ? 22.952 43.005 31.458  1.00 13.49 ? 221  TRP A CD1 1 
ATOM   1732 C  CD2 . TRP A 1 221 ? 23.337 44.594 29.924  1.00 15.15 ? 221  TRP A CD2 1 
ATOM   1733 N  NE1 . TRP A 1 221 ? 21.747 43.338 30.885  1.00 11.68 ? 221  TRP A NE1 1 
ATOM   1734 C  CE2 . TRP A 1 221 ? 21.952 44.309 29.942  1.00 14.19 ? 221  TRP A CE2 1 
ATOM   1735 C  CE3 . TRP A 1 221 ? 23.815 45.563 29.033  1.00 15.76 ? 221  TRP A CE3 1 
ATOM   1736 C  CZ2 . TRP A 1 221 ? 21.043 44.959 29.104  1.00 14.40 ? 221  TRP A CZ2 1 
ATOM   1737 C  CZ3 . TRP A 1 221 ? 22.911 46.206 28.202  1.00 19.16 ? 221  TRP A CZ3 1 
ATOM   1738 C  CH2 . TRP A 1 221 ? 21.540 45.901 28.244  1.00 16.06 ? 221  TRP A CH2 1 
ATOM   1739 N  N   . PHE A 1 222 ? 28.084 45.234 32.382  1.00 17.17 ? 222  PHE A N   1 
ATOM   1740 C  CA  . PHE A 1 222 ? 29.527 45.138 32.543  1.00 13.22 ? 222  PHE A CA  1 
ATOM   1741 C  C   . PHE A 1 222 ? 30.077 46.111 33.571  1.00 18.07 ? 222  PHE A C   1 
ATOM   1742 O  O   . PHE A 1 222 ? 29.489 47.160 33.825  1.00 21.91 ? 222  PHE A O   1 
ATOM   1743 C  CB  . PHE A 1 222 ? 30.205 45.397 31.202  1.00 11.49 ? 222  PHE A CB  1 
ATOM   1744 C  CG  . PHE A 1 222 ? 29.669 44.556 30.076  1.00 9.26  ? 222  PHE A CG  1 
ATOM   1745 C  CD1 . PHE A 1 222 ? 30.226 43.317 29.786  1.00 8.08  ? 222  PHE A CD1 1 
ATOM   1746 C  CD2 . PHE A 1 222 ? 28.624 45.017 29.289  1.00 9.10  ? 222  PHE A CD2 1 
ATOM   1747 C  CE1 . PHE A 1 222 ? 29.749 42.551 28.726  1.00 6.33  ? 222  PHE A CE1 1 
ATOM   1748 C  CE2 . PHE A 1 222 ? 28.137 44.260 28.224  1.00 9.52  ? 222  PHE A CE2 1 
ATOM   1749 C  CZ  . PHE A 1 222 ? 28.703 43.022 27.943  1.00 8.41  ? 222  PHE A CZ  1 
ATOM   1750 N  N   . PRO A 1 223 ? 31.203 45.755 34.205  1.00 21.25 ? 223  PRO A N   1 
ATOM   1751 C  CA  . PRO A 1 223 ? 31.845 46.606 35.210  1.00 19.67 ? 223  PRO A CA  1 
ATOM   1752 C  C   . PRO A 1 223 ? 32.326 47.880 34.529  1.00 21.04 ? 223  PRO A C   1 
ATOM   1753 O  O   . PRO A 1 223 ? 32.657 47.869 33.338  1.00 20.32 ? 223  PRO A O   1 
ATOM   1754 C  CB  . PRO A 1 223 ? 33.048 45.767 35.644  1.00 20.17 ? 223  PRO A CB  1 
ATOM   1755 C  CG  . PRO A 1 223 ? 32.589 44.372 35.427  1.00 22.76 ? 223  PRO A CG  1 
ATOM   1756 C  CD  . PRO A 1 223 ? 31.905 44.466 34.092  1.00 21.48 ? 223  PRO A CD  1 
ATOM   1757 N  N   . ALA A 1 224 ? 32.362 48.974 35.280  1.00 21.35 ? 224  ALA A N   1 
ATOM   1758 C  CA  . ALA A 1 224 ? 32.808 50.252 34.745  1.00 20.01 ? 224  ALA A CA  1 
ATOM   1759 C  C   . ALA A 1 224 ? 34.206 50.131 34.147  1.00 18.90 ? 224  ALA A C   1 
ATOM   1760 O  O   . ALA A 1 224 ? 35.048 49.394 34.660  1.00 22.47 ? 224  ALA A O   1 
ATOM   1761 C  CB  . ALA A 1 224 ? 32.794 51.310 35.838  1.00 22.00 ? 224  ALA A CB  1 
ATOM   1762 N  N   . GLY A 1 225 ? 34.432 50.830 33.042  1.00 20.07 ? 225  GLY A N   1 
ATOM   1763 C  CA  . GLY A 1 225 ? 35.729 50.805 32.394  1.00 16.49 ? 225  GLY A CA  1 
ATOM   1764 C  C   . GLY A 1 225 ? 36.053 49.560 31.583  1.00 18.69 ? 225  GLY A C   1 
ATOM   1765 O  O   . GLY A 1 225 ? 37.211 49.355 31.242  1.00 19.69 ? 225  GLY A O   1 
ATOM   1766 N  N   . SER A 1 226 ? 35.053 48.751 31.242  1.00 18.81 ? 226  SER A N   1 
ATOM   1767 C  CA  . SER A 1 226 ? 35.295 47.538 30.462  1.00 16.35 ? 226  SER A CA  1 
ATOM   1768 C  C   . SER A 1 226 ? 35.508 47.835 28.978  1.00 17.27 ? 226  SER A C   1 
ATOM   1769 O  O   . SER A 1 226 ? 34.711 48.517 28.339  1.00 14.96 ? 226  SER A O   1 
ATOM   1770 C  CB  . SER A 1 226 ? 34.146 46.543 30.639  1.00 18.84 ? 226  SER A CB  1 
ATOM   1771 O  OG  . SER A 1 226 ? 34.070 46.070 31.976  1.00 19.62 ? 226  SER A OG  1 
ATOM   1772 N  N   . ARG A 1 227 ? 36.599 47.313 28.441  1.00 14.88 ? 227  ARG A N   1 
ATOM   1773 C  CA  . ARG A 1 227 ? 36.954 47.491 27.045  1.00 15.57 ? 227  ARG A CA  1 
ATOM   1774 C  C   . ARG A 1 227 ? 36.305 46.347 26.244  1.00 18.61 ? 227  ARG A C   1 
ATOM   1775 O  O   . ARG A 1 227 ? 36.216 45.216 26.727  1.00 19.57 ? 227  ARG A O   1 
ATOM   1776 C  CB  . ARG A 1 227 ? 38.473 47.428 26.930  1.00 18.33 ? 227  ARG A CB  1 
ATOM   1777 C  CG  . ARG A 1 227 ? 39.120 48.468 26.031  1.00 26.82 ? 227  ARG A CG  1 
ATOM   1778 C  CD  . ARG A 1 227 ? 39.165 49.854 26.658  1.00 25.63 ? 227  ARG A CD  1 
ATOM   1779 N  NE  . ARG A 1 227 ? 37.973 50.656 26.382  1.00 28.33 ? 227  ARG A NE  1 
ATOM   1780 C  CZ  . ARG A 1 227 ? 37.632 51.135 25.186  1.00 27.36 ? 227  ARG A CZ  1 
ATOM   1781 N  NH1 . ARG A 1 227 ? 38.371 50.902 24.110  1.00 29.07 ? 227  ARG A NH1 1 
ATOM   1782 N  NH2 . ARG A 1 227 ? 36.531 51.853 25.066  1.00 31.55 ? 227  ARG A NH2 1 
ATOM   1783 N  N   . PRO A 1 228 ? 35.808 46.632 25.026  1.00 19.64 ? 228  PRO A N   1 
ATOM   1784 C  CA  . PRO A 1 228 ? 35.178 45.587 24.212  1.00 15.87 ? 228  PRO A CA  1 
ATOM   1785 C  C   . PRO A 1 228 ? 36.156 44.529 23.698  1.00 18.02 ? 228  PRO A C   1 
ATOM   1786 O  O   . PRO A 1 228 ? 37.315 44.835 23.389  1.00 16.68 ? 228  PRO A O   1 
ATOM   1787 C  CB  . PRO A 1 228 ? 34.557 46.381 23.058  1.00 15.88 ? 228  PRO A CB  1 
ATOM   1788 C  CG  . PRO A 1 228 ? 35.482 47.529 22.904  1.00 16.71 ? 228  PRO A CG  1 
ATOM   1789 C  CD  . PRO A 1 228 ? 35.748 47.936 24.340  1.00 17.96 ? 228  PRO A CD  1 
ATOM   1790 N  N   . PHE A 1 229 ? 35.668 43.292 23.610  1.00 14.58 ? 229  PHE A N   1 
ATOM   1791 C  CA  . PHE A 1 229 ? 36.449 42.154 23.127  1.00 12.49 ? 229  PHE A CA  1 
ATOM   1792 C  C   . PHE A 1 229 ? 36.634 42.299 21.619  1.00 13.06 ? 229  PHE A C   1 
ATOM   1793 O  O   . PHE A 1 229 ? 35.670 42.542 20.888  1.00 11.26 ? 229  PHE A O   1 
ATOM   1794 C  CB  . PHE A 1 229 ? 35.701 40.852 23.432  1.00 12.22 ? 229  PHE A CB  1 
ATOM   1795 C  CG  . PHE A 1 229 ? 36.424 39.607 22.996  1.00 12.24 ? 229  PHE A CG  1 
ATOM   1796 C  CD1 . PHE A 1 229 ? 37.786 39.451 23.229  1.00 11.08 ? 229  PHE A CD1 1 
ATOM   1797 C  CD2 . PHE A 1 229 ? 35.725 38.561 22.391  1.00 12.34 ? 229  PHE A CD2 1 
ATOM   1798 C  CE1 . PHE A 1 229 ? 38.439 38.275 22.870  1.00 9.42  ? 229  PHE A CE1 1 
ATOM   1799 C  CE2 . PHE A 1 229 ? 36.373 37.378 22.030  1.00 10.82 ? 229  PHE A CE2 1 
ATOM   1800 C  CZ  . PHE A 1 229 ? 37.731 37.236 22.270  1.00 9.43  ? 229  PHE A CZ  1 
ATOM   1801 N  N   . ILE A 1 230 ? 37.857 42.109 21.146  1.00 13.52 ? 230  ILE A N   1 
ATOM   1802 C  CA  . ILE A 1 230 ? 38.137 42.253 19.724  1.00 8.02  ? 230  ILE A CA  1 
ATOM   1803 C  C   . ILE A 1 230 ? 38.862 41.047 19.149  1.00 10.11 ? 230  ILE A C   1 
ATOM   1804 O  O   . ILE A 1 230 ? 39.886 40.627 19.688  1.00 11.70 ? 230  ILE A O   1 
ATOM   1805 C  CB  . ILE A 1 230 ? 39.059 43.491 19.453  1.00 8.62  ? 230  ILE A CB  1 
ATOM   1806 C  CG1 . ILE A 1 230 ? 38.406 44.786 19.944  1.00 7.99  ? 230  ILE A CG1 1 
ATOM   1807 C  CG2 . ILE A 1 230 ? 39.411 43.589 17.974  1.00 2.00  ? 230  ILE A CG2 1 
ATOM   1808 C  CD1 . ILE A 1 230 ? 37.206 45.218 19.136  1.00 8.80  ? 230  ILE A CD1 1 
ATOM   1809 N  N   . PHE A 1 231 ? 38.308 40.455 18.095  1.00 7.18  ? 231  PHE A N   1 
ATOM   1810 C  CA  . PHE A 1 231 ? 38.998 39.372 17.413  1.00 5.38  ? 231  PHE A CA  1 
ATOM   1811 C  C   . PHE A 1 231 ? 38.967 39.661 15.925  1.00 4.78  ? 231  PHE A C   1 
ATOM   1812 O  O   . PHE A 1 231 ? 37.914 39.894 15.332  1.00 7.05  ? 231  PHE A O   1 
ATOM   1813 C  CB  . PHE A 1 231 ? 38.533 37.950 17.797  1.00 5.75  ? 231  PHE A CB  1 
ATOM   1814 C  CG  . PHE A 1 231 ? 37.067 37.682 17.628  1.00 5.81  ? 231  PHE A CG  1 
ATOM   1815 C  CD1 . PHE A 1 231 ? 36.155 38.081 18.604  1.00 8.11  ? 231  PHE A CD1 1 
ATOM   1816 C  CD2 . PHE A 1 231 ? 36.611 36.916 16.562  1.00 7.39  ? 231  PHE A CD2 1 
ATOM   1817 C  CE1 . PHE A 1 231 ? 34.810 37.705 18.519  1.00 8.73  ? 231  PHE A CE1 1 
ATOM   1818 C  CE2 . PHE A 1 231 ? 35.278 36.536 16.470  1.00 4.13  ? 231  PHE A CE2 1 
ATOM   1819 C  CZ  . PHE A 1 231 ? 34.375 36.930 17.452  1.00 5.12  ? 231  PHE A CZ  1 
ATOM   1820 N  N   . GLN A 1 232 ? 40.150 39.719 15.339  1.00 7.36  ? 232  GLN A N   1 
ATOM   1821 C  CA  . GLN A 1 232 ? 40.286 40.056 13.939  1.00 6.34  ? 232  GLN A CA  1 
ATOM   1822 C  C   . GLN A 1 232 ? 40.428 38.867 13.033  1.00 7.76  ? 232  GLN A C   1 
ATOM   1823 O  O   . GLN A 1 232 ? 41.194 37.954 13.325  1.00 12.50 ? 232  GLN A O   1 
ATOM   1824 C  CB  . GLN A 1 232 ? 41.491 40.972 13.779  1.00 8.85  ? 232  GLN A CB  1 
ATOM   1825 C  CG  . GLN A 1 232 ? 41.422 42.185 14.684  1.00 12.15 ? 232  GLN A CG  1 
ATOM   1826 C  CD  . GLN A 1 232 ? 42.782 42.714 15.040  1.00 12.65 ? 232  GLN A CD  1 
ATOM   1827 O  OE1 . GLN A 1 232 ? 43.299 43.615 14.382  1.00 15.78 ? 232  GLN A OE1 1 
ATOM   1828 N  NE2 . GLN A 1 232 ? 43.380 42.154 16.082  1.00 11.72 ? 232  GLN A NE2 1 
ATOM   1829 N  N   . GLU A 1 233 ? 39.682 38.862 11.934  1.00 8.24  ? 233  GLU A N   1 
ATOM   1830 C  CA  . GLU A 1 233 ? 39.796 37.760 11.001  1.00 8.05  ? 233  GLU A CA  1 
ATOM   1831 C  C   . GLU A 1 233 ? 41.013 37.980 10.125  1.00 8.43  ? 233  GLU A C   1 
ATOM   1832 O  O   . GLU A 1 233 ? 40.988 38.818 9.220   1.00 11.22 ? 233  GLU A O   1 
ATOM   1833 C  CB  . GLU A 1 233 ? 38.570 37.628 10.105  1.00 7.06  ? 233  GLU A CB  1 
ATOM   1834 C  CG  . GLU A 1 233 ? 38.665 36.390 9.216   1.00 7.93  ? 233  GLU A CG  1 
ATOM   1835 C  CD  . GLU A 1 233 ? 38.231 36.620 7.781   1.00 11.30 ? 233  GLU A CD  1 
ATOM   1836 O  OE1 . GLU A 1 233 ? 37.981 37.777 7.390   1.00 15.46 ? 233  GLU A OE1 1 
ATOM   1837 O  OE2 . GLU A 1 233 ? 38.115 35.626 7.039   1.00 13.47 ? 233  GLU A OE2 1 
ATOM   1838 N  N   . VAL A 1 234 ? 42.082 37.249 10.409  1.00 9.74  ? 234  VAL A N   1 
ATOM   1839 C  CA  . VAL A 1 234 ? 43.309 37.342 9.631   1.00 7.93  ? 234  VAL A CA  1 
ATOM   1840 C  C   . VAL A 1 234 ? 43.701 35.929 9.251   1.00 8.02  ? 234  VAL A C   1 
ATOM   1841 O  O   . VAL A 1 234 ? 44.076 35.129 10.109  1.00 10.72 ? 234  VAL A O   1 
ATOM   1842 C  CB  . VAL A 1 234 ? 44.479 37.975 10.431  1.00 6.73  ? 234  VAL A CB  1 
ATOM   1843 C  CG1 . VAL A 1 234 ? 45.753 37.988 9.593   1.00 5.16  ? 234  VAL A CG1 1 
ATOM   1844 C  CG2 . VAL A 1 234 ? 44.135 39.384 10.852  1.00 7.07  ? 234  VAL A CG2 1 
ATOM   1845 N  N   . ILE A 1 235 ? 43.553 35.603 7.974   1.00 8.36  ? 235  ILE A N   1 
ATOM   1846 C  CA  . ILE A 1 235 ? 43.915 34.281 7.483   1.00 11.20 ? 235  ILE A CA  1 
ATOM   1847 C  C   . ILE A 1 235 ? 45.419 34.240 7.212   1.00 12.13 ? 235  ILE A C   1 
ATOM   1848 O  O   . ILE A 1 235 ? 45.898 34.851 6.262   1.00 16.39 ? 235  ILE A O   1 
ATOM   1849 C  CB  . ILE A 1 235 ? 43.143 33.931 6.190   1.00 11.25 ? 235  ILE A CB  1 
ATOM   1850 C  CG1 . ILE A 1 235 ? 41.641 33.842 6.482   1.00 7.71  ? 235  ILE A CG1 1 
ATOM   1851 C  CG2 . ILE A 1 235 ? 43.658 32.618 5.597   1.00 10.75 ? 235  ILE A CG2 1 
ATOM   1852 C  CD1 . ILE A 1 235 ? 40.790 33.653 5.249   1.00 5.95  ? 235  ILE A CD1 1 
ATOM   1853 N  N   . ASP A 1 236 ? 46.160 33.560 8.081   1.00 14.39 ? 236  ASP A N   1 
ATOM   1854 C  CA  . ASP A 1 236 ? 47.607 33.436 7.936   1.00 13.09 ? 236  ASP A CA  1 
ATOM   1855 C  C   . ASP A 1 236 ? 48.040 32.005 8.253   1.00 16.12 ? 236  ASP A C   1 
ATOM   1856 O  O   . ASP A 1 236 ? 48.198 31.624 9.417   1.00 17.50 ? 236  ASP A O   1 
ATOM   1857 C  CB  . ASP A 1 236 ? 48.336 34.429 8.858   1.00 12.29 ? 236  ASP A CB  1 
ATOM   1858 C  CG  . ASP A 1 236 ? 49.838 34.195 8.904   1.00 13.15 ? 236  ASP A CG  1 
ATOM   1859 O  OD1 . ASP A 1 236 ? 50.389 33.684 7.909   1.00 12.40 ? 236  ASP A OD1 1 
ATOM   1860 O  OD2 . ASP A 1 236 ? 50.469 34.520 9.935   1.00 13.49 ? 236  ASP A OD2 1 
ATOM   1861 N  N   . LEU A 1 237 ? 48.249 31.229 7.201   1.00 16.44 ? 237  LEU A N   1 
ATOM   1862 C  CA  . LEU A 1 237 ? 48.668 29.843 7.327   1.00 18.31 ? 237  LEU A CA  1 
ATOM   1863 C  C   . LEU A 1 237 ? 50.186 29.748 7.257   1.00 19.13 ? 237  LEU A C   1 
ATOM   1864 O  O   . LEU A 1 237 ? 50.737 28.677 7.018   1.00 21.18 ? 237  LEU A O   1 
ATOM   1865 C  CB  . LEU A 1 237 ? 48.032 29.008 6.208   1.00 19.13 ? 237  LEU A CB  1 
ATOM   1866 C  CG  . LEU A 1 237 ? 46.629 28.424 6.403   1.00 20.72 ? 237  LEU A CG  1 
ATOM   1867 C  CD1 . LEU A 1 237 ? 45.727 29.356 7.184   1.00 23.23 ? 237  LEU A CD1 1 
ATOM   1868 C  CD2 . LEU A 1 237 ? 46.031 28.103 5.045   1.00 20.90 ? 237  LEU A CD2 1 
ATOM   1869 N  N   . GLY A 1 238 ? 50.854 30.873 7.493   1.00 23.62 ? 238  GLY A N   1 
ATOM   1870 C  CA  . GLY A 1 238 ? 52.304 30.916 7.444   1.00 23.46 ? 238  GLY A CA  1 
ATOM   1871 C  C   . GLY A 1 238 ? 52.792 31.052 6.016   1.00 27.38 ? 238  GLY A C   1 
ATOM   1872 O  O   . GLY A 1 238 ? 52.061 30.744 5.071   1.00 29.69 ? 238  GLY A O   1 
ATOM   1873 N  N   . GLY A 1 239 ? 54.006 31.561 5.846   1.00 28.08 ? 239  GLY A N   1 
ATOM   1874 C  CA  . GLY A 1 239 ? 54.555 31.704 4.509   1.00 32.20 ? 239  GLY A CA  1 
ATOM   1875 C  C   . GLY A 1 239 ? 53.863 32.680 3.569   1.00 31.28 ? 239  GLY A C   1 
ATOM   1876 O  O   . GLY A 1 239 ? 53.706 32.397 2.373   1.00 29.59 ? 239  GLY A O   1 
ATOM   1877 N  N   . GLU A 1 240 ? 53.430 33.815 4.108   1.00 32.51 ? 240  GLU A N   1 
ATOM   1878 C  CA  . GLU A 1 240 ? 52.793 34.853 3.308   1.00 28.83 ? 240  GLU A CA  1 
ATOM   1879 C  C   . GLU A 1 240 ? 53.283 36.208 3.802   1.00 25.92 ? 240  GLU A C   1 
ATOM   1880 O  O   . GLU A 1 240 ? 53.786 36.314 4.921   1.00 21.99 ? 240  GLU A O   1 
ATOM   1881 C  CB  . GLU A 1 240 ? 51.271 34.754 3.374   1.00 34.29 ? 240  GLU A CB  1 
ATOM   1882 C  CG  . GLU A 1 240 ? 50.611 35.288 2.111   1.00 42.88 ? 240  GLU A CG  1 
ATOM   1883 C  CD  . GLU A 1 240 ? 49.148 34.915 1.998   1.00 47.02 ? 240  GLU A CD  1 
ATOM   1884 O  OE1 . GLU A 1 240 ? 48.302 35.667 2.523   1.00 48.64 ? 240  GLU A OE1 1 
ATOM   1885 O  OE2 . GLU A 1 240 ? 48.843 33.876 1.369   1.00 49.54 ? 240  GLU A OE2 1 
ATOM   1886 N  N   . ALA A 1 241 ? 53.175 37.231 2.958   1.00 24.11 ? 241  ALA A N   1 
ATOM   1887 C  CA  . ALA A 1 241 ? 53.642 38.573 3.305   1.00 19.37 ? 241  ALA A CA  1 
ATOM   1888 C  C   . ALA A 1 241 ? 53.060 39.155 4.595   1.00 17.82 ? 241  ALA A C   1 
ATOM   1889 O  O   . ALA A 1 241 ? 53.793 39.699 5.419   1.00 21.80 ? 241  ALA A O   1 
ATOM   1890 C  CB  . ALA A 1 241 ? 53.419 39.521 2.148   1.00 18.08 ? 241  ALA A CB  1 
ATOM   1891 N  N   . ILE A 1 242 ? 51.748 39.069 4.762   1.00 15.08 ? 242  ILE A N   1 
ATOM   1892 C  CA  . ILE A 1 242 ? 51.110 39.595 5.962   1.00 14.19 ? 242  ILE A CA  1 
ATOM   1893 C  C   . ILE A 1 242 ? 51.056 38.529 7.046   1.00 15.83 ? 242  ILE A C   1 
ATOM   1894 O  O   . ILE A 1 242 ? 50.618 37.408 6.799   1.00 17.85 ? 242  ILE A O   1 
ATOM   1895 C  CB  . ILE A 1 242 ? 49.688 40.104 5.660   1.00 13.71 ? 242  ILE A CB  1 
ATOM   1896 C  CG1 . ILE A 1 242 ? 49.765 41.286 4.688   1.00 11.85 ? 242  ILE A CG1 1 
ATOM   1897 C  CG2 . ILE A 1 242 ? 48.966 40.488 6.960   1.00 12.18 ? 242  ILE A CG2 1 
ATOM   1898 C  CD1 . ILE A 1 242 ? 48.432 41.733 4.171   1.00 13.22 ? 242  ILE A CD1 1 
ATOM   1899 N  N   . GLN A 1 243 ? 51.524 38.881 8.239   1.00 20.00 ? 243  GLN A N   1 
ATOM   1900 C  CA  . GLN A 1 243 ? 51.540 37.967 9.377   1.00 20.00 ? 243  GLN A CA  1 
ATOM   1901 C  C   . GLN A 1 243 ? 50.468 38.349 10.392  1.00 20.00 ? 243  GLN A C   1 
ATOM   1902 O  O   . GLN A 1 243 ? 50.238 39.534 10.641  1.00 20.00 ? 243  GLN A O   1 
ATOM   1903 C  CB  . GLN A 1 243 ? 52.910 38.010 10.065  1.00 20.00 ? 243  GLN A CB  1 
ATOM   1904 C  CG  . GLN A 1 243 ? 54.012 37.322 9.257   1.00 20.00 ? 243  GLN A CG  1 
ATOM   1905 C  CD  . GLN A 1 243 ? 55.417 37.630 9.779   1.00 20.00 ? 243  GLN A CD  1 
ATOM   1906 O  OE1 . GLN A 1 243 ? 56.042 38.588 9.328   1.00 20.00 ? 243  GLN A OE1 1 
ATOM   1907 N  NE2 . GLN A 1 243 ? 55.957 36.869 10.709  1.00 20.00 ? 243  GLN A NE2 1 
ATOM   1908 N  N   . SER A 1 244 ? 49.863 37.354 11.031  1.00 13.97 ? 244  SER A N   1 
ATOM   1909 C  CA  . SER A 1 244 ? 48.829 37.630 12.016  1.00 15.45 ? 244  SER A CA  1 
ATOM   1910 C  C   . SER A 1 244 ? 49.370 38.444 13.190  1.00 14.53 ? 244  SER A C   1 
ATOM   1911 O  O   . SER A 1 244 ? 48.641 39.229 13.798  1.00 15.85 ? 244  SER A O   1 
ATOM   1912 C  CB  . SER A 1 244 ? 48.187 36.329 12.495  1.00 14.65 ? 244  SER A CB  1 
ATOM   1913 O  OG  . SER A 1 244 ? 49.162 35.344 12.768  1.00 24.01 ? 244  SER A OG  1 
ATOM   1914 N  N   . SER A 1 245 ? 50.665 38.314 13.461  1.00 13.34 ? 245  SER A N   1 
ATOM   1915 C  CA  . SER A 1 245 ? 51.291 39.030 14.565  1.00 14.87 ? 245  SER A CA  1 
ATOM   1916 C  C   . SER A 1 245 ? 51.247 40.542 14.420  1.00 14.36 ? 245  SER A C   1 
ATOM   1917 O  O   . SER A 1 245 ? 51.400 41.260 15.406  1.00 19.00 ? 245  SER A O   1 
ATOM   1918 C  CB  . SER A 1 245 ? 52.733 38.565 14.756  1.00 15.15 ? 245  SER A CB  1 
ATOM   1919 O  OG  . SER A 1 245 ? 53.411 38.508 13.515  1.00 23.31 ? 245  SER A OG  1 
ATOM   1920 N  N   . GLU A 1 246 ? 51.038 41.029 13.202  1.00 12.79 ? 246  GLU A N   1 
ATOM   1921 C  CA  . GLU A 1 246 ? 50.959 42.470 12.963  1.00 9.76  ? 246  GLU A CA  1 
ATOM   1922 C  C   . GLU A 1 246 ? 49.712 43.067 13.615  1.00 10.56 ? 246  GLU A C   1 
ATOM   1923 O  O   . GLU A 1 246 ? 49.605 44.287 13.747  1.00 13.83 ? 246  GLU A O   1 
ATOM   1924 C  CB  . GLU A 1 246 ? 50.890 42.762 11.466  1.00 6.79  ? 246  GLU A CB  1 
ATOM   1925 C  CG  . GLU A 1 246 ? 52.131 42.410 10.672  1.00 8.98  ? 246  GLU A CG  1 
ATOM   1926 C  CD  . GLU A 1 246 ? 51.899 42.560 9.178   1.00 13.40 ? 246  GLU A CD  1 
ATOM   1927 O  OE1 . GLU A 1 246 ? 51.212 43.521 8.768   1.00 14.99 ? 246  GLU A OE1 1 
ATOM   1928 O  OE2 . GLU A 1 246 ? 52.396 41.713 8.407   1.00 16.32 ? 246  GLU A OE2 1 
ATOM   1929 N  N   . TYR A 1 247 ? 48.773 42.212 14.015  1.00 10.07 ? 247  TYR A N   1 
ATOM   1930 C  CA  . TYR A 1 247 ? 47.508 42.655 14.611  1.00 8.89  ? 247  TYR A CA  1 
ATOM   1931 C  C   . TYR A 1 247 ? 47.354 42.417 16.099  1.00 6.71  ? 247  TYR A C   1 
ATOM   1932 O  O   . TYR A 1 247 ? 46.310 42.740 16.670  1.00 14.33 ? 247  TYR A O   1 
ATOM   1933 C  CB  . TYR A 1 247 ? 46.344 41.982 13.882  1.00 5.97  ? 247  TYR A CB  1 
ATOM   1934 C  CG  . TYR A 1 247 ? 46.305 42.315 12.414  1.00 3.37  ? 247  TYR A CG  1 
ATOM   1935 C  CD1 . TYR A 1 247 ? 47.173 41.702 11.522  1.00 5.27  ? 247  TYR A CD1 1 
ATOM   1936 C  CD2 . TYR A 1 247 ? 45.424 43.274 11.920  1.00 5.01  ? 247  TYR A CD2 1 
ATOM   1937 C  CE1 . TYR A 1 247 ? 47.169 42.034 10.173  1.00 5.51  ? 247  TYR A CE1 1 
ATOM   1938 C  CE2 . TYR A 1 247 ? 45.413 43.614 10.577  1.00 5.18  ? 247  TYR A CE2 1 
ATOM   1939 C  CZ  . TYR A 1 247 ? 46.288 42.989 9.713   1.00 4.43  ? 247  TYR A CZ  1 
ATOM   1940 O  OH  . TYR A 1 247 ? 46.272 43.315 8.393   1.00 8.76  ? 247  TYR A OH  1 
ATOM   1941 N  N   . PHE A 1 248 ? 48.391 41.887 16.738  1.00 8.78  ? 248  PHE A N   1 
ATOM   1942 C  CA  . PHE A 1 248 ? 48.335 41.585 18.166  1.00 8.80  ? 248  PHE A CA  1 
ATOM   1943 C  C   . PHE A 1 248 ? 48.071 42.790 19.064  1.00 8.88  ? 248  PHE A C   1 
ATOM   1944 O  O   . PHE A 1 248 ? 47.649 42.630 20.208  1.00 10.81 ? 248  PHE A O   1 
ATOM   1945 C  CB  . PHE A 1 248 ? 49.621 40.881 18.620  1.00 12.25 ? 248  PHE A CB  1 
ATOM   1946 C  CG  . PHE A 1 248 ? 49.764 39.463 18.116  1.00 13.01 ? 248  PHE A CG  1 
ATOM   1947 C  CD1 . PHE A 1 248 ? 48.712 38.822 17.461  1.00 12.37 ? 248  PHE A CD1 1 
ATOM   1948 C  CD2 . PHE A 1 248 ? 50.953 38.764 18.316  1.00 11.29 ? 248  PHE A CD2 1 
ATOM   1949 C  CE1 . PHE A 1 248 ? 48.840 37.512 17.015  1.00 11.45 ? 248  PHE A CE1 1 
ATOM   1950 C  CE2 . PHE A 1 248 ? 51.094 37.450 17.874  1.00 11.78 ? 248  PHE A CE2 1 
ATOM   1951 C  CZ  . PHE A 1 248 ? 50.035 36.822 17.221  1.00 14.26 ? 248  PHE A CZ  1 
ATOM   1952 N  N   . GLY A 1 249 ? 48.318 43.990 18.554  1.00 10.10 ? 249  GLY A N   1 
ATOM   1953 C  CA  . GLY A 1 249 ? 48.113 45.183 19.359  1.00 11.41 ? 249  GLY A CA  1 
ATOM   1954 C  C   . GLY A 1 249 ? 46.674 45.639 19.448  1.00 13.24 ? 249  GLY A C   1 
ATOM   1955 O  O   . GLY A 1 249 ? 46.304 46.374 20.365  1.00 16.45 ? 249  GLY A O   1 
ATOM   1956 N  N   . ASN A 1 250 ? 45.860 45.204 18.494  1.00 11.72 ? 250  ASN A N   1 
ATOM   1957 C  CA  . ASN A 1 250 ? 44.454 45.584 18.454  1.00 9.27  ? 250  ASN A CA  1 
ATOM   1958 C  C   . ASN A 1 250 ? 43.565 44.648 19.266  1.00 10.23 ? 250  ASN A C   1 
ATOM   1959 O  O   . ASN A 1 250 ? 42.545 45.071 19.810  1.00 15.78 ? 250  ASN A O   1 
ATOM   1960 C  CB  . ASN A 1 250 ? 43.966 45.623 17.001  1.00 9.06  ? 250  ASN A CB  1 
ATOM   1961 C  CG  . ASN A 1 250 ? 44.750 46.607 16.145  1.00 7.90  ? 250  ASN A CG  1 
ATOM   1962 O  OD1 . ASN A 1 250 ? 45.237 47.623 16.640  1.00 6.62  ? 250  ASN A OD1 1 
ATOM   1963 N  ND2 . ASN A 1 250 ? 44.885 46.302 14.860  1.00 4.53  ? 250  ASN A ND2 1 
ATOM   1964 N  N   . GLY A 1 251 ? 43.946 43.381 19.349  1.00 10.89 ? 251  GLY A N   1 
ATOM   1965 C  CA  . GLY A 1 251 ? 43.147 42.422 20.083  1.00 10.73 ? 251  GLY A CA  1 
ATOM   1966 C  C   . GLY A 1 251 ? 43.538 41.022 19.675  1.00 12.47 ? 251  GLY A C   1 
ATOM   1967 O  O   . GLY A 1 251 ? 44.642 40.811 19.168  1.00 11.01 ? 251  GLY A O   1 
ATOM   1968 N  N   . ARG A 1 252 ? 42.644 40.062 19.890  1.00 12.59 ? 252  ARG A N   1 
ATOM   1969 C  CA  . ARG A 1 252 ? 42.926 38.683 19.516  1.00 13.62 ? 252  ARG A CA  1 
ATOM   1970 C  C   . ARG A 1 252 ? 42.793 38.525 18.002  1.00 11.37 ? 252  ARG A C   1 
ATOM   1971 O  O   . ARG A 1 252 ? 42.225 39.391 17.320  1.00 12.96 ? 252  ARG A O   1 
ATOM   1972 C  CB  . ARG A 1 252 ? 42.012 37.717 20.278  1.00 13.07 ? 252  ARG A CB  1 
ATOM   1973 C  CG  . ARG A 1 252 ? 42.227 37.793 21.777  1.00 15.10 ? 252  ARG A CG  1 
ATOM   1974 C  CD  . ARG A 1 252 ? 41.322 36.879 22.579  1.00 14.43 ? 252  ARG A CD  1 
ATOM   1975 N  NE  . ARG A 1 252 ? 41.950 35.602 22.885  1.00 19.99 ? 252  ARG A NE  1 
ATOM   1976 C  CZ  . ARG A 1 252 ? 42.185 35.144 24.114  1.00 16.10 ? 252  ARG A CZ  1 
ATOM   1977 N  NH1 . ARG A 1 252 ? 41.838 35.845 25.183  1.00 12.87 ? 252  ARG A NH1 1 
ATOM   1978 N  NH2 . ARG A 1 252 ? 42.766 33.966 24.269  1.00 19.50 ? 252  ARG A NH2 1 
ATOM   1979 N  N   . VAL A 1 253 ? 43.363 37.448 17.473  1.00 10.64 ? 253  VAL A N   1 
ATOM   1980 C  CA  . VAL A 1 253 ? 43.339 37.170 16.039  1.00 10.14 ? 253  VAL A CA  1 
ATOM   1981 C  C   . VAL A 1 253 ? 42.863 35.738 15.803  1.00 9.54  ? 253  VAL A C   1 
ATOM   1982 O  O   . VAL A 1 253 ? 43.136 34.856 16.617  1.00 10.38 ? 253  VAL A O   1 
ATOM   1983 C  CB  . VAL A 1 253 ? 44.762 37.318 15.436  1.00 8.67  ? 253  VAL A CB  1 
ATOM   1984 C  CG1 . VAL A 1 253 ? 44.725 37.167 13.931  1.00 8.14  ? 253  VAL A CG1 1 
ATOM   1985 C  CG2 . VAL A 1 253 ? 45.364 38.668 15.811  1.00 8.61  ? 253  VAL A CG2 1 
ATOM   1986 N  N   . THR A 1 254 ? 42.128 35.512 14.717  1.00 9.72  ? 254  THR A N   1 
ATOM   1987 C  CA  . THR A 1 254 ? 41.647 34.174 14.372  1.00 8.72  ? 254  THR A CA  1 
ATOM   1988 C  C   . THR A 1 254 ? 42.840 33.287 13.965  1.00 10.74 ? 254  THR A C   1 
ATOM   1989 O  O   . THR A 1 254 ? 43.567 33.618 13.019  1.00 12.71 ? 254  THR A O   1 
ATOM   1990 C  CB  . THR A 1 254 ? 40.696 34.223 13.173  1.00 6.32  ? 254  THR A CB  1 
ATOM   1991 O  OG1 . THR A 1 254 ? 41.325 34.944 12.108  1.00 8.39  ? 254  THR A OG1 1 
ATOM   1992 C  CG2 . THR A 1 254 ? 39.391 34.893 13.540  1.00 6.22  ? 254  THR A CG2 1 
ATOM   1993 N  N   . GLU A 1 255 ? 43.055 32.179 14.668  1.00 9.43  ? 255  GLU A N   1 
ATOM   1994 C  CA  . GLU A 1 255 ? 44.159 31.284 14.325  1.00 8.20  ? 255  GLU A CA  1 
ATOM   1995 C  C   . GLU A 1 255 ? 43.653 30.211 13.368  1.00 10.84 ? 255  GLU A C   1 
ATOM   1996 O  O   . GLU A 1 255 ? 43.157 29.177 13.802  1.00 16.49 ? 255  GLU A O   1 
ATOM   1997 C  CB  . GLU A 1 255 ? 44.751 30.641 15.585  1.00 6.46  ? 255  GLU A CB  1 
ATOM   1998 C  CG  . GLU A 1 255 ? 45.886 29.664 15.324  1.00 6.67  ? 255  GLU A CG  1 
ATOM   1999 C  CD  . GLU A 1 255 ? 47.055 30.283 14.571  1.00 8.42  ? 255  GLU A CD  1 
ATOM   2000 O  OE1 . GLU A 1 255 ? 46.983 30.424 13.333  1.00 8.90  ? 255  GLU A OE1 1 
ATOM   2001 O  OE2 . GLU A 1 255 ? 48.067 30.604 15.213  1.00 8.97  ? 255  GLU A OE2 1 
ATOM   2002 N  N   . PHE A 1 256 ? 43.791 30.456 12.069  1.00 9.74  ? 256  PHE A N   1 
ATOM   2003 C  CA  . PHE A 1 256 ? 43.329 29.516 11.049  1.00 10.13 ? 256  PHE A CA  1 
ATOM   2004 C  C   . PHE A 1 256 ? 44.188 28.255 10.883  1.00 11.43 ? 256  PHE A C   1 
ATOM   2005 O  O   . PHE A 1 256 ? 43.756 27.289 10.250  1.00 11.92 ? 256  PHE A O   1 
ATOM   2006 C  CB  . PHE A 1 256 ? 43.171 30.227 9.696   1.00 7.00  ? 256  PHE A CB  1 
ATOM   2007 C  CG  . PHE A 1 256 ? 41.885 30.994 9.562   1.00 8.64  ? 256  PHE A CG  1 
ATOM   2008 C  CD1 . PHE A 1 256 ? 41.795 32.314 9.979   1.00 9.95  ? 256  PHE A CD1 1 
ATOM   2009 C  CD2 . PHE A 1 256 ? 40.759 30.392 9.012   1.00 9.72  ? 256  PHE A CD2 1 
ATOM   2010 C  CE1 . PHE A 1 256 ? 40.602 33.024 9.851   1.00 9.31  ? 256  PHE A CE1 1 
ATOM   2011 C  CE2 . PHE A 1 256 ? 39.565 31.097 8.882   1.00 14.55 ? 256  PHE A CE2 1 
ATOM   2012 C  CZ  . PHE A 1 256 ? 39.489 32.416 9.304   1.00 10.89 ? 256  PHE A CZ  1 
ATOM   2013 N  N   . LYS A 1 257 ? 45.409 28.274 11.415  1.00 10.13 ? 257  LYS A N   1 
ATOM   2014 C  CA  . LYS A 1 257 ? 46.293 27.108 11.329  1.00 11.38 ? 257  LYS A CA  1 
ATOM   2015 C  C   . LYS A 1 257 ? 45.733 25.995 12.202  1.00 12.89 ? 257  LYS A C   1 
ATOM   2016 O  O   . LYS A 1 257 ? 45.933 24.810 11.923  1.00 15.42 ? 257  LYS A O   1 
ATOM   2017 C  CB  . LYS A 1 257 ? 47.698 27.437 11.844  1.00 10.24 ? 257  LYS A CB  1 
ATOM   2018 C  CG  . LYS A 1 257 ? 48.472 28.444 11.031  1.00 9.64  ? 257  LYS A CG  1 
ATOM   2019 C  CD  . LYS A 1 257 ? 49.760 28.785 11.740  1.00 9.83  ? 257  LYS A CD  1 
ATOM   2020 C  CE  . LYS A 1 257 ? 50.534 29.842 10.994  1.00 12.94 ? 257  LYS A CE  1 
ATOM   2021 N  NZ  . LYS A 1 257 ? 51.722 30.259 11.766  1.00 13.10 ? 257  LYS A NZ  1 
ATOM   2022 N  N   . TYR A 1 258 ? 45.035 26.394 13.261  1.00 10.62 ? 258  TYR A N   1 
ATOM   2023 C  CA  . TYR A 1 258 ? 44.455 25.469 14.220  1.00 10.78 ? 258  TYR A CA  1 
ATOM   2024 C  C   . TYR A 1 258 ? 43.507 24.470 13.560  1.00 14.03 ? 258  TYR A C   1 
ATOM   2025 O  O   . TYR A 1 258 ? 43.688 23.257 13.689  1.00 16.07 ? 258  TYR A O   1 
ATOM   2026 C  CB  . TYR A 1 258 ? 43.749 26.260 15.319  1.00 7.33  ? 258  TYR A CB  1 
ATOM   2027 C  CG  . TYR A 1 258 ? 43.322 25.449 16.518  1.00 6.95  ? 258  TYR A CG  1 
ATOM   2028 C  CD1 . TYR A 1 258 ? 42.210 24.617 16.459  1.00 5.99  ? 258  TYR A CD1 1 
ATOM   2029 C  CD2 . TYR A 1 258 ? 44.009 25.545 17.726  1.00 8.37  ? 258  TYR A CD2 1 
ATOM   2030 C  CE1 . TYR A 1 258 ? 41.790 23.903 17.567  1.00 6.75  ? 258  TYR A CE1 1 
ATOM   2031 C  CE2 . TYR A 1 258 ? 43.593 24.836 18.845  1.00 8.34  ? 258  TYR A CE2 1 
ATOM   2032 C  CZ  . TYR A 1 258 ? 42.482 24.017 18.753  1.00 7.99  ? 258  TYR A CZ  1 
ATOM   2033 O  OH  . TYR A 1 258 ? 42.056 23.297 19.839  1.00 9.52  ? 258  TYR A OH  1 
ATOM   2034 N  N   . GLY A 1 259 ? 42.531 24.979 12.815  1.00 16.02 ? 259  GLY A N   1 
ATOM   2035 C  CA  . GLY A 1 259 ? 41.573 24.113 12.156  1.00 12.31 ? 259  GLY A CA  1 
ATOM   2036 C  C   . GLY A 1 259 ? 42.145 23.319 11.000  1.00 13.69 ? 259  GLY A C   1 
ATOM   2037 O  O   . GLY A 1 259 ? 41.747 22.175 10.776  1.00 16.09 ? 259  GLY A O   1 
ATOM   2038 N  N   . ALA A 1 260 ? 43.054 23.930 10.246  1.00 10.79 ? 260  ALA A N   1 
ATOM   2039 C  CA  . ALA A 1 260 ? 43.679 23.279 9.096   1.00 10.83 ? 260  ALA A CA  1 
ATOM   2040 C  C   . ALA A 1 260 ? 44.512 22.065 9.506   1.00 11.15 ? 260  ALA A C   1 
ATOM   2041 O  O   . ALA A 1 260 ? 44.399 20.995 8.904   1.00 15.08 ? 260  ALA A O   1 
ATOM   2042 C  CB  . ALA A 1 260 ? 44.544 24.280 8.332   1.00 7.38  ? 260  ALA A CB  1 
ATOM   2043 N  N   . LYS A 1 261 ? 45.343 22.242 10.533  1.00 14.97 ? 261  LYS A N   1 
ATOM   2044 C  CA  . LYS A 1 261 ? 46.200 21.174 11.049  1.00 14.20 ? 261  LYS A CA  1 
ATOM   2045 C  C   . LYS A 1 261 ? 45.412 20.075 11.765  1.00 16.46 ? 261  LYS A C   1 
ATOM   2046 O  O   . LYS A 1 261 ? 45.645 18.885 11.536  1.00 18.30 ? 261  LYS A O   1 
ATOM   2047 C  CB  . LYS A 1 261 ? 47.249 21.740 12.010  1.00 16.59 ? 261  LYS A CB  1 
ATOM   2048 C  CG  . LYS A 1 261 ? 48.598 22.049 11.389  1.00 16.65 ? 261  LYS A CG  1 
ATOM   2049 C  CD  . LYS A 1 261 ? 48.492 23.116 10.337  1.00 23.06 ? 261  LYS A CD  1 
ATOM   2050 C  CE  . LYS A 1 261 ? 49.857 23.479 9.804   1.00 25.86 ? 261  LYS A CE  1 
ATOM   2051 N  NZ  . LYS A 1 261 ? 50.734 23.961 10.906  1.00 32.88 ? 261  LYS A NZ  1 
ATOM   2052 N  N   . LEU A 1 262 ? 44.489 20.478 12.636  1.00 10.71 ? 262  LEU A N   1 
ATOM   2053 C  CA  . LEU A 1 262 ? 43.687 19.531 13.392  1.00 10.10 ? 262  LEU A CA  1 
ATOM   2054 C  C   . LEU A 1 262 ? 42.884 18.637 12.450  1.00 12.50 ? 262  LEU A C   1 
ATOM   2055 O  O   . LEU A 1 262 ? 42.814 17.421 12.645  1.00 14.22 ? 262  LEU A O   1 
ATOM   2056 C  CB  . LEU A 1 262 ? 42.759 20.273 14.365  1.00 10.44 ? 262  LEU A CB  1 
ATOM   2057 C  CG  . LEU A 1 262 ? 41.987 19.461 15.412  1.00 8.75  ? 262  LEU A CG  1 
ATOM   2058 C  CD1 . LEU A 1 262 ? 42.951 18.736 16.330  1.00 8.07  ? 262  LEU A CD1 1 
ATOM   2059 C  CD2 . LEU A 1 262 ? 41.077 20.375 16.221  1.00 9.98  ? 262  LEU A CD2 1 
ATOM   2060 N  N   . GLY A 1 263 ? 42.302 19.240 11.418  1.00 12.39 ? 263  GLY A N   1 
ATOM   2061 C  CA  . GLY A 1 263 ? 41.527 18.478 10.461  1.00 12.81 ? 263  GLY A CA  1 
ATOM   2062 C  C   . GLY A 1 263 ? 42.389 17.414 9.806   1.00 16.04 ? 263  GLY A C   1 
ATOM   2063 O  O   . GLY A 1 263 ? 41.962 16.273 9.646   1.00 17.21 ? 263  GLY A O   1 
ATOM   2064 N  N   . THR A 1 264 ? 43.628 17.772 9.483   1.00 13.12 ? 264  THR A N   1 
ATOM   2065 C  CA  . THR A 1 264 ? 44.552 16.855 8.839   1.00 13.37 ? 264  THR A CA  1 
ATOM   2066 C  C   . THR A 1 264 ? 44.978 15.714 9.761   1.00 16.28 ? 264  THR A C   1 
ATOM   2067 O  O   . THR A 1 264 ? 45.066 14.558 9.336   1.00 18.12 ? 264  THR A O   1 
ATOM   2068 C  CB  . THR A 1 264 ? 45.785 17.607 8.312   1.00 13.10 ? 264  THR A CB  1 
ATOM   2069 O  OG1 . THR A 1 264 ? 45.361 18.595 7.363   1.00 15.57 ? 264  THR A OG1 1 
ATOM   2070 C  CG2 . THR A 1 264 ? 46.750 16.654 7.628   1.00 10.24 ? 264  THR A CG2 1 
ATOM   2071 N  N   . VAL A 1 265 ? 45.235 16.041 11.020  1.00 15.39 ? 265  VAL A N   1 
ATOM   2072 C  CA  . VAL A 1 265 ? 45.643 15.056 12.013  1.00 10.92 ? 265  VAL A CA  1 
ATOM   2073 C  C   . VAL A 1 265 ? 44.510 14.063 12.287  1.00 14.46 ? 265  VAL A C   1 
ATOM   2074 O  O   . VAL A 1 265 ? 44.705 12.854 12.196  1.00 15.03 ? 265  VAL A O   1 
ATOM   2075 C  CB  . VAL A 1 265 ? 46.058 15.749 13.333  1.00 10.12 ? 265  VAL A CB  1 
ATOM   2076 C  CG1 . VAL A 1 265 ? 46.368 14.718 14.402  1.00 12.73 ? 265  VAL A CG1 1 
ATOM   2077 C  CG2 . VAL A 1 265 ? 47.262 16.641 13.095  1.00 6.74  ? 265  VAL A CG2 1 
ATOM   2078 N  N   . VAL A 1 266 ? 43.317 14.577 12.578  1.00 15.28 ? 266  VAL A N   1 
ATOM   2079 C  CA  . VAL A 1 266 ? 42.159 13.728 12.865  1.00 12.89 ? 266  VAL A CA  1 
ATOM   2080 C  C   . VAL A 1 266 ? 41.762 12.849 11.673  1.00 10.14 ? 266  VAL A C   1 
ATOM   2081 O  O   . VAL A 1 266 ? 41.258 11.752 11.863  1.00 14.68 ? 266  VAL A O   1 
ATOM   2082 C  CB  . VAL A 1 266 ? 40.959 14.571 13.382  1.00 14.84 ? 266  VAL A CB  1 
ATOM   2083 C  CG1 . VAL A 1 266 ? 39.705 13.716 13.520  1.00 13.81 ? 266  VAL A CG1 1 
ATOM   2084 C  CG2 . VAL A 1 266 ? 41.305 15.167 14.728  1.00 10.98 ? 266  VAL A CG2 1 
ATOM   2085 N  N   . ARG A 1 267 ? 42.005 13.321 10.452  1.00 10.41 ? 267  ARG A N   1 
ATOM   2086 C  CA  . ARG A 1 267 ? 41.704 12.545 9.244   1.00 6.56  ? 267  ARG A CA  1 
ATOM   2087 C  C   . ARG A 1 267 ? 42.850 11.569 8.934   1.00 11.09 ? 267  ARG A C   1 
ATOM   2088 O  O   . ARG A 1 267 ? 42.705 10.677 8.095   1.00 11.64 ? 267  ARG A O   1 
ATOM   2089 C  CB  . ARG A 1 267 ? 41.532 13.463 8.031   1.00 5.39  ? 267  ARG A CB  1 
ATOM   2090 C  CG  . ARG A 1 267 ? 40.291 14.335 8.027   1.00 4.52  ? 267  ARG A CG  1 
ATOM   2091 C  CD  . ARG A 1 267 ? 40.374 15.274 6.839   1.00 7.22  ? 267  ARG A CD  1 
ATOM   2092 N  NE  . ARG A 1 267 ? 39.231 16.174 6.716   1.00 10.40 ? 267  ARG A NE  1 
ATOM   2093 C  CZ  . ARG A 1 267 ? 38.053 15.832 6.205   1.00 12.47 ? 267  ARG A CZ  1 
ATOM   2094 N  NH1 . ARG A 1 267 ? 37.828 14.588 5.805   1.00 12.79 ? 267  ARG A NH1 1 
ATOM   2095 N  NH2 . ARG A 1 267 ? 37.082 16.731 6.126   1.00 11.15 ? 267  ARG A NH2 1 
ATOM   2096 N  N   . LYS A 1 268 ? 43.989 11.769 9.594   1.00 12.75 ? 268  LYS A N   1 
ATOM   2097 C  CA  . LYS A 1 268 ? 45.182 10.947 9.409   1.00 14.69 ? 268  LYS A CA  1 
ATOM   2098 C  C   . LYS A 1 268 ? 45.776 11.084 8.005   1.00 15.58 ? 268  LYS A C   1 
ATOM   2099 O  O   . LYS A 1 268 ? 46.167 10.095 7.374   1.00 19.62 ? 268  LYS A O   1 
ATOM   2100 C  CB  . LYS A 1 268 ? 44.896 9.483  9.759   1.00 13.28 ? 268  LYS A CB  1 
ATOM   2101 C  CG  . LYS A 1 268 ? 44.689 9.256  11.239  1.00 18.01 ? 268  LYS A CG  1 
ATOM   2102 C  CD  . LYS A 1 268 ? 44.381 7.801  11.574  1.00 21.73 ? 268  LYS A CD  1 
ATOM   2103 C  CE  . LYS A 1 268 ? 42.979 7.402  11.151  1.00 23.79 ? 268  LYS A CE  1 
ATOM   2104 N  NZ  . LYS A 1 268 ? 42.612 6.040  11.636  1.00 27.56 ? 268  LYS A NZ  1 
ATOM   2105 N  N   . TRP A 1 269 ? 45.893 12.332 7.554   1.00 17.45 ? 269  TRP A N   1 
ATOM   2106 C  CA  . TRP A 1 269 ? 46.442 12.659 6.240   1.00 16.43 ? 269  TRP A CA  1 
ATOM   2107 C  C   . TRP A 1 269 ? 47.883 13.131 6.371   1.00 15.88 ? 269  TRP A C   1 
ATOM   2108 O  O   . TRP A 1 269 ? 48.322 13.502 7.457   1.00 17.41 ? 269  TRP A O   1 
ATOM   2109 C  CB  . TRP A 1 269 ? 45.623 13.779 5.583   1.00 15.66 ? 269  TRP A CB  1 
ATOM   2110 C  CG  . TRP A 1 269 ? 44.265 13.371 5.073   1.00 18.10 ? 269  TRP A CG  1 
ATOM   2111 C  CD1 . TRP A 1 269 ? 43.720 12.115 5.082   1.00 18.63 ? 269  TRP A CD1 1 
ATOM   2112 C  CD2 . TRP A 1 269 ? 43.303 14.218 4.428   1.00 19.22 ? 269  TRP A CD2 1 
ATOM   2113 N  NE1 . TRP A 1 269 ? 42.486 12.128 4.476   1.00 19.37 ? 269  TRP A NE1 1 
ATOM   2114 C  CE2 . TRP A 1 269 ? 42.205 13.404 4.065   1.00 20.04 ? 269  TRP A CE2 1 
ATOM   2115 C  CE3 . TRP A 1 269 ? 43.265 15.585 4.117   1.00 18.28 ? 269  TRP A CE3 1 
ATOM   2116 C  CZ2 . TRP A 1 269 ? 41.078 13.913 3.403   1.00 21.24 ? 269  TRP A CZ2 1 
ATOM   2117 C  CZ3 . TRP A 1 269 ? 42.147 16.091 3.459   1.00 19.71 ? 269  TRP A CZ3 1 
ATOM   2118 C  CH2 . TRP A 1 269 ? 41.067 15.254 3.109   1.00 20.81 ? 269  TRP A CH2 1 
ATOM   2119 N  N   . SER A 1 270 ? 48.616 13.104 5.260   1.00 17.53 ? 270  SER A N   1 
ATOM   2120 C  CA  . SER A 1 270 ? 50.003 13.558 5.219   1.00 14.78 ? 270  SER A CA  1 
ATOM   2121 C  C   . SER A 1 270 ? 50.897 12.946 6.302   1.00 15.79 ? 270  SER A C   1 
ATOM   2122 O  O   . SER A 1 270 ? 51.851 13.580 6.763   1.00 16.79 ? 270  SER A O   1 
ATOM   2123 C  CB  . SER A 1 270 ? 50.042 15.085 5.327   1.00 18.84 ? 270  SER A CB  1 
ATOM   2124 O  OG  . SER A 1 270 ? 49.179 15.693 4.376   1.00 23.92 ? 270  SER A OG  1 
ATOM   2125 N  N   . GLY A 1 271 ? 50.600 11.712 6.690   1.00 12.49 ? 271  GLY A N   1 
ATOM   2126 C  CA  . GLY A 1 271 ? 51.384 11.050 7.718   1.00 13.18 ? 271  GLY A CA  1 
ATOM   2127 C  C   . GLY A 1 271 ? 51.189 11.561 9.140   1.00 16.06 ? 271  GLY A C   1 
ATOM   2128 O  O   . GLY A 1 271 ? 51.946 11.180 10.035  1.00 18.08 ? 271  GLY A O   1 
ATOM   2129 N  N   . GLU A 1 272 ? 50.176 12.396 9.367   1.00 14.19 ? 272  GLU A N   1 
ATOM   2130 C  CA  . GLU A 1 272 ? 49.926 12.934 10.699  1.00 17.19 ? 272  GLU A CA  1 
ATOM   2131 C  C   . GLU A 1 272 ? 49.214 11.924 11.594  1.00 18.13 ? 272  GLU A C   1 
ATOM   2132 O  O   . GLU A 1 272 ? 48.436 11.103 11.110  1.00 17.96 ? 272  GLU A O   1 
ATOM   2133 C  CB  . GLU A 1 272 ? 49.131 14.240 10.609  1.00 19.38 ? 272  GLU A CB  1 
ATOM   2134 C  CG  . GLU A 1 272 ? 49.831 15.366 9.828   1.00 21.53 ? 272  GLU A CG  1 
ATOM   2135 C  CD  . GLU A 1 272 ? 51.073 15.925 10.517  1.00 22.72 ? 272  GLU A CD  1 
ATOM   2136 O  OE1 . GLU A 1 272 ? 51.862 15.151 11.088  1.00 27.26 ? 272  GLU A OE1 1 
ATOM   2137 O  OE2 . GLU A 1 272 ? 51.278 17.153 10.474  1.00 26.96 ? 272  GLU A OE2 1 
ATOM   2138 N  N   . LYS A 1 273 ? 49.515 11.962 12.891  1.00 18.80 ? 273  LYS A N   1 
ATOM   2139 C  CA  . LYS A 1 273 ? 48.917 11.052 13.869  1.00 16.29 ? 273  LYS A CA  1 
ATOM   2140 C  C   . LYS A 1 273 ? 48.499 11.865 15.085  1.00 17.20 ? 273  LYS A C   1 
ATOM   2141 O  O   . LYS A 1 273 ? 49.147 12.867 15.405  1.00 18.22 ? 273  LYS A O   1 
ATOM   2142 C  CB  . LYS A 1 273 ? 49.948 10.029 14.347  1.00 17.87 ? 273  LYS A CB  1 
ATOM   2143 C  CG  . LYS A 1 273 ? 50.646 9.239  13.272  1.00 25.77 ? 273  LYS A CG  1 
ATOM   2144 C  CD  . LYS A 1 273 ? 51.793 8.474  13.889  1.00 33.07 ? 273  LYS A CD  1 
ATOM   2145 C  CE  . LYS A 1 273 ? 52.698 7.880  12.837  1.00 41.34 ? 273  LYS A CE  1 
ATOM   2146 N  NZ  . LYS A 1 273 ? 53.944 7.355  13.470  1.00 48.55 ? 273  LYS A NZ  1 
ATOM   2147 N  N   . MET A 1 274 ? 47.461 11.416 15.792  1.00 14.15 ? 274  MET A N   1 
ATOM   2148 C  CA  . MET A 1 274 ? 47.003 12.114 16.992  1.00 15.13 ? 274  MET A CA  1 
ATOM   2149 C  C   . MET A 1 274 ? 48.082 12.158 18.068  1.00 13.91 ? 274  MET A C   1 
ATOM   2150 O  O   . MET A 1 274 ? 48.099 13.068 18.888  1.00 17.99 ? 274  MET A O   1 
ATOM   2151 C  CB  . MET A 1 274 ? 45.729 11.484 17.577  1.00 17.55 ? 274  MET A CB  1 
ATOM   2152 C  CG  . MET A 1 274 ? 44.429 12.107 17.081  1.00 21.94 ? 274  MET A CG  1 
ATOM   2153 S  SD  . MET A 1 274 ? 43.017 11.734 18.132  1.00 25.34 ? 274  MET A SD  1 
ATOM   2154 C  CE  . MET A 1 274 ? 42.911 13.216 19.115  1.00 25.41 ? 274  MET A CE  1 
ATOM   2155 N  N   . SER A 1 275 ? 48.996 11.195 18.065  1.00 13.03 ? 275  SER A N   1 
ATOM   2156 C  CA  . SER A 1 275 ? 50.049 11.188 19.071  1.00 12.43 ? 275  SER A CA  1 
ATOM   2157 C  C   . SER A 1 275 ? 50.971 12.405 18.948  1.00 12.84 ? 275  SER A C   1 
ATOM   2158 O  O   . SER A 1 275 ? 51.672 12.750 19.897  1.00 16.67 ? 275  SER A O   1 
ATOM   2159 C  CB  . SER A 1 275 ? 50.848 9.882  19.021  1.00 11.49 ? 275  SER A CB  1 
ATOM   2160 O  OG  . SER A 1 275 ? 51.544 9.728  17.801  1.00 15.97 ? 275  SER A OG  1 
ATOM   2161 N  N   . TYR A 1 276 ? 50.935 13.072 17.794  1.00 14.47 ? 276  TYR A N   1 
ATOM   2162 C  CA  . TYR A 1 276 ? 51.755 14.264 17.549  1.00 14.22 ? 276  TYR A CA  1 
ATOM   2163 C  C   . TYR A 1 276 ? 51.180 15.493 18.260  1.00 15.52 ? 276  TYR A C   1 
ATOM   2164 O  O   . TYR A 1 276 ? 51.860 16.513 18.414  1.00 16.34 ? 276  TYR A O   1 
ATOM   2165 C  CB  . TYR A 1 276 ? 51.830 14.565 16.047  1.00 15.54 ? 276  TYR A CB  1 
ATOM   2166 C  CG  . TYR A 1 276 ? 52.578 13.545 15.207  1.00 18.26 ? 276  TYR A CG  1 
ATOM   2167 C  CD1 . TYR A 1 276 ? 53.460 12.629 15.785  1.00 21.57 ? 276  TYR A CD1 1 
ATOM   2168 C  CD2 . TYR A 1 276 ? 52.415 13.509 13.825  1.00 19.54 ? 276  TYR A CD2 1 
ATOM   2169 C  CE1 . TYR A 1 276 ? 54.157 11.706 15.004  1.00 19.41 ? 276  TYR A CE1 1 
ATOM   2170 C  CE2 . TYR A 1 276 ? 53.108 12.592 13.038  1.00 18.71 ? 276  TYR A CE2 1 
ATOM   2171 C  CZ  . TYR A 1 276 ? 53.973 11.696 13.632  1.00 21.34 ? 276  TYR A CZ  1 
ATOM   2172 O  OH  . TYR A 1 276 ? 54.659 10.795 12.850  1.00 26.18 ? 276  TYR A OH  1 
ATOM   2173 N  N   . LEU A 1 277 ? 49.927 15.396 18.695  1.00 15.35 ? 277  LEU A N   1 
ATOM   2174 C  CA  . LEU A 1 277 ? 49.259 16.505 19.363  1.00 15.54 ? 277  LEU A CA  1 
ATOM   2175 C  C   . LEU A 1 277 ? 49.733 16.772 20.786  1.00 17.18 ? 277  LEU A C   1 
ATOM   2176 O  O   . LEU A 1 277 ? 49.250 17.703 21.433  1.00 20.77 ? 277  LEU A O   1 
ATOM   2177 C  CB  . LEU A 1 277 ? 47.744 16.298 19.351  1.00 11.60 ? 277  LEU A CB  1 
ATOM   2178 C  CG  . LEU A 1 277 ? 47.088 16.221 17.975  1.00 12.09 ? 277  LEU A CG  1 
ATOM   2179 C  CD1 . LEU A 1 277 ? 45.617 15.941 18.141  1.00 13.40 ? 277  LEU A CD1 1 
ATOM   2180 C  CD2 . LEU A 1 277 ? 47.298 17.512 17.202  1.00 10.46 ? 277  LEU A CD2 1 
ATOM   2181 N  N   . LYS A 1 278 ? 50.712 16.004 21.257  1.00 18.36 ? 278  LYS A N   1 
ATOM   2182 C  CA  . LYS A 1 278 ? 51.228 16.170 22.612  1.00 18.14 ? 278  LYS A CA  1 
ATOM   2183 C  C   . LYS A 1 278 ? 51.640 17.606 22.931  1.00 17.90 ? 278  LYS A C   1 
ATOM   2184 O  O   . LYS A 1 278 ? 51.367 18.118 24.019  1.00 17.29 ? 278  LYS A O   1 
ATOM   2185 C  CB  . LYS A 1 278 ? 52.415 15.234 22.852  1.00 23.22 ? 278  LYS A CB  1 
ATOM   2186 C  CG  . LYS A 1 278 ? 52.943 15.285 24.281  1.00 27.60 ? 278  LYS A CG  1 
ATOM   2187 C  CD  . LYS A 1 278 ? 54.120 14.360 24.479  1.00 33.68 ? 278  LYS A CD  1 
ATOM   2188 C  CE  . LYS A 1 278 ? 54.638 14.459 25.904  1.00 38.38 ? 278  LYS A CE  1 
ATOM   2189 N  NZ  . LYS A 1 278 ? 55.785 13.537 26.142  1.00 46.03 ? 278  LYS A NZ  1 
ATOM   2190 N  N   . ASN A 1 279 ? 52.326 18.237 21.987  1.00 16.20 ? 279  ASN A N   1 
ATOM   2191 C  CA  . ASN A 1 279 ? 52.786 19.610 22.150  1.00 17.14 ? 279  ASN A CA  1 
ATOM   2192 C  C   . ASN A 1 279 ? 51.925 20.590 21.359  1.00 18.89 ? 279  ASN A C   1 
ATOM   2193 O  O   . ASN A 1 279 ? 52.398 21.640 20.931  1.00 22.28 ? 279  ASN A O   1 
ATOM   2194 C  CB  . ASN A 1 279 ? 54.247 19.736 21.721  1.00 13.79 ? 279  ASN A CB  1 
ATOM   2195 C  CG  . ASN A 1 279 ? 54.444 19.522 20.225  1.00 18.29 ? 279  ASN A CG  1 
ATOM   2196 O  OD1 . ASN A 1 279 ? 55.348 20.108 19.627  1.00 22.57 ? 279  ASN A OD1 1 
ATOM   2197 N  ND2 . ASN A 1 279 ? 53.608 18.688 19.614  1.00 15.66 ? 279  ASN A ND2 1 
ATOM   2198 N  N   . TRP A 1 280 ? 50.656 20.239 21.180  1.00 19.50 ? 280  TRP A N   1 
ATOM   2199 C  CA  . TRP A 1 280 ? 49.701 21.078 20.465  1.00 16.92 ? 280  TRP A CA  1 
ATOM   2200 C  C   . TRP A 1 280 ? 49.721 22.482 21.054  1.00 15.65 ? 280  TRP A C   1 
ATOM   2201 O  O   . TRP A 1 280 ? 49.956 22.657 22.253  1.00 19.33 ? 280  TRP A O   1 
ATOM   2202 C  CB  . TRP A 1 280 ? 48.304 20.483 20.613  1.00 14.00 ? 280  TRP A CB  1 
ATOM   2203 C  CG  . TRP A 1 280 ? 47.228 21.180 19.861  1.00 9.13  ? 280  TRP A CG  1 
ATOM   2204 C  CD1 . TRP A 1 280 ? 46.118 21.767 20.388  1.00 7.42  ? 280  TRP A CD1 1 
ATOM   2205 C  CD2 . TRP A 1 280 ? 47.084 21.253 18.437  1.00 8.77  ? 280  TRP A CD2 1 
ATOM   2206 N  NE1 . TRP A 1 280 ? 45.277 22.181 19.385  1.00 7.17  ? 280  TRP A NE1 1 
ATOM   2207 C  CE2 . TRP A 1 280 ? 45.846 21.880 18.176  1.00 7.19  ? 280  TRP A CE2 1 
ATOM   2208 C  CE3 . TRP A 1 280 ? 47.874 20.839 17.358  1.00 9.27  ? 280  TRP A CE3 1 
ATOM   2209 C  CZ2 . TRP A 1 280 ? 45.378 22.099 16.880  1.00 7.46  ? 280  TRP A CZ2 1 
ATOM   2210 C  CZ3 . TRP A 1 280 ? 47.407 21.060 16.065  1.00 5.65  ? 280  TRP A CZ3 1 
ATOM   2211 C  CH2 . TRP A 1 280 ? 46.169 21.683 15.841  1.00 7.38  ? 280  TRP A CH2 1 
ATOM   2212 N  N   . GLY A 1 281 ? 49.465 23.474 20.215  1.00 13.57 ? 281  GLY A N   1 
ATOM   2213 C  CA  . GLY A 1 281 ? 49.462 24.840 20.683  1.00 10.51 ? 281  GLY A CA  1 
ATOM   2214 C  C   . GLY A 1 281 ? 50.655 25.552 20.099  1.00 12.07 ? 281  GLY A C   1 
ATOM   2215 O  O   . GLY A 1 281 ? 51.020 25.324 18.948  1.00 15.83 ? 281  GLY A O   1 
ATOM   2216 N  N   . GLU A 1 282 ? 51.299 26.383 20.898  1.00 15.87 ? 282  GLU A N   1 
ATOM   2217 C  CA  . GLU A 1 282 ? 52.452 27.131 20.431  1.00 20.61 ? 282  GLU A CA  1 
ATOM   2218 C  C   . GLU A 1 282 ? 53.583 26.246 19.913  1.00 21.91 ? 282  GLU A C   1 
ATOM   2219 O  O   . GLU A 1 282 ? 54.338 26.659 19.030  1.00 25.02 ? 282  GLU A O   1 
ATOM   2220 C  CB  . GLU A 1 282 ? 52.909 28.102 21.515  1.00 25.54 ? 282  GLU A CB  1 
ATOM   2221 C  CG  . GLU A 1 282 ? 51.831 29.144 21.809  1.00 34.27 ? 282  GLU A CG  1 
ATOM   2222 C  CD  . GLU A 1 282 ? 52.105 29.984 23.040  1.00 39.35 ? 282  GLU A CD  1 
ATOM   2223 O  OE1 . GLU A 1 282 ? 53.131 30.706 23.056  1.00 43.10 ? 282  GLU A OE1 1 
ATOM   2224 O  OE2 . GLU A 1 282 ? 51.275 29.939 23.980  1.00 39.34 ? 282  GLU A OE2 1 
ATOM   2225 N  N   . GLY A 1 283 ? 53.638 25.001 20.383  1.00 20.81 ? 283  GLY A N   1 
ATOM   2226 C  CA  . GLY A 1 283 ? 54.658 24.073 19.923  1.00 14.24 ? 283  GLY A CA  1 
ATOM   2227 C  C   . GLY A 1 283 ? 54.508 23.762 18.441  1.00 18.32 ? 283  GLY A C   1 
ATOM   2228 O  O   . GLY A 1 283 ? 55.457 23.330 17.787  1.00 20.12 ? 283  GLY A O   1 
ATOM   2229 N  N   . TRP A 1 284 ? 53.308 23.969 17.906  1.00 17.40 ? 284  TRP A N   1 
ATOM   2230 C  CA  . TRP A 1 284 ? 53.043 23.719 16.491  1.00 16.18 ? 284  TRP A CA  1 
ATOM   2231 C  C   . TRP A 1 284 ? 53.213 24.970 15.629  1.00 16.81 ? 284  TRP A C   1 
ATOM   2232 O  O   . TRP A 1 284 ? 52.864 24.968 14.447  1.00 16.78 ? 284  TRP A O   1 
ATOM   2233 C  CB  . TRP A 1 284 ? 51.636 23.151 16.306  1.00 14.32 ? 284  TRP A CB  1 
ATOM   2234 C  CG  . TRP A 1 284 ? 51.552 21.685 16.526  1.00 10.02 ? 284  TRP A CG  1 
ATOM   2235 C  CD1 . TRP A 1 284 ? 51.848 21.009 17.669  1.00 9.35  ? 284  TRP A CD1 1 
ATOM   2236 C  CD2 . TRP A 1 284 ? 51.122 20.710 15.577  1.00 10.07 ? 284  TRP A CD2 1 
ATOM   2237 N  NE1 . TRP A 1 284 ? 51.623 19.667 17.494  1.00 12.17 ? 284  TRP A NE1 1 
ATOM   2238 C  CE2 . TRP A 1 284 ? 51.173 19.454 16.216  1.00 11.66 ? 284  TRP A CE2 1 
ATOM   2239 C  CE3 . TRP A 1 284 ? 50.692 20.774 14.245  1.00 10.33 ? 284  TRP A CE3 1 
ATOM   2240 C  CZ2 . TRP A 1 284 ? 50.808 18.265 15.571  1.00 13.21 ? 284  TRP A CZ2 1 
ATOM   2241 C  CZ3 . TRP A 1 284 ? 50.328 19.591 13.600  1.00 13.50 ? 284  TRP A CZ3 1 
ATOM   2242 C  CH2 . TRP A 1 284 ? 50.390 18.353 14.268  1.00 12.91 ? 284  TRP A CH2 1 
ATOM   2243 N  N   . GLY A 1 285 ? 53.744 26.031 16.235  1.00 20.28 ? 285  GLY A N   1 
ATOM   2244 C  CA  . GLY A 1 285 ? 53.954 27.282 15.529  1.00 19.45 ? 285  GLY A CA  1 
ATOM   2245 C  C   . GLY A 1 285 ? 52.760 28.224 15.530  1.00 20.11 ? 285  GLY A C   1 
ATOM   2246 O  O   . GLY A 1 285 ? 52.694 29.133 14.705  1.00 24.84 ? 285  GLY A O   1 
ATOM   2247 N  N   . PHE A 1 286 ? 51.803 27.996 16.423  1.00 15.48 ? 286  PHE A N   1 
ATOM   2248 C  CA  . PHE A 1 286 ? 50.621 28.846 16.511  1.00 13.00 ? 286  PHE A CA  1 
ATOM   2249 C  C   . PHE A 1 286 ? 50.980 30.117 17.263  1.00 14.18 ? 286  PHE A C   1 
ATOM   2250 O  O   . PHE A 1 286 ? 52.039 30.195 17.889  1.00 16.11 ? 286  PHE A O   1 
ATOM   2251 C  CB  . PHE A 1 286 ? 49.500 28.137 17.273  1.00 8.76  ? 286  PHE A CB  1 
ATOM   2252 C  CG  . PHE A 1 286 ? 48.988 26.898 16.608  1.00 7.58  ? 286  PHE A CG  1 
ATOM   2253 C  CD1 . PHE A 1 286 ? 49.356 26.578 15.306  1.00 5.56  ? 286  PHE A CD1 1 
ATOM   2254 C  CD2 . PHE A 1 286 ? 48.126 26.044 17.290  1.00 5.27  ? 286  PHE A CD2 1 
ATOM   2255 C  CE1 . PHE A 1 286 ? 48.872 25.425 14.700  1.00 6.70  ? 286  PHE A CE1 1 
ATOM   2256 C  CE2 . PHE A 1 286 ? 47.641 24.893 16.687  1.00 5.98  ? 286  PHE A CE2 1 
ATOM   2257 C  CZ  . PHE A 1 286 ? 48.011 24.582 15.393  1.00 2.23  ? 286  PHE A CZ  1 
ATOM   2258 N  N   . MET A 1 287 ? 50.078 31.093 17.241  1.00 14.82 ? 287  MET A N   1 
ATOM   2259 C  CA  . MET A 1 287 ? 50.292 32.353 17.942  1.00 14.28 ? 287  MET A CA  1 
ATOM   2260 C  C   . MET A 1 287 ? 50.139 32.101 19.438  1.00 14.94 ? 287  MET A C   1 
ATOM   2261 O  O   . MET A 1 287 ? 49.706 31.024 19.854  1.00 17.14 ? 287  MET A O   1 
ATOM   2262 C  CB  . MET A 1 287 ? 49.259 33.385 17.489  1.00 14.09 ? 287  MET A CB  1 
ATOM   2263 C  CG  . MET A 1 287 ? 47.825 32.969 17.760  1.00 15.07 ? 287  MET A CG  1 
ATOM   2264 S  SD  . MET A 1 287 ? 46.643 34.193 17.182  1.00 15.17 ? 287  MET A SD  1 
ATOM   2265 C  CE  . MET A 1 287 ? 46.852 34.025 15.443  1.00 10.87 ? 287  MET A CE  1 
ATOM   2266 N  N   . PRO A 1 288 ? 50.503 33.086 20.272  1.00 12.52 ? 288  PRO A N   1 
ATOM   2267 C  CA  . PRO A 1 288 ? 50.369 32.887 21.713  1.00 10.40 ? 288  PRO A CA  1 
ATOM   2268 C  C   . PRO A 1 288 ? 48.910 32.612 22.057  1.00 13.01 ? 288  PRO A C   1 
ATOM   2269 O  O   . PRO A 1 288 ? 48.006 33.257 21.520  1.00 16.52 ? 288  PRO A O   1 
ATOM   2270 C  CB  . PRO A 1 288 ? 50.832 34.228 22.281  1.00 10.96 ? 288  PRO A CB  1 
ATOM   2271 C  CG  . PRO A 1 288 ? 51.816 34.698 21.262  1.00 10.61 ? 288  PRO A CG  1 
ATOM   2272 C  CD  . PRO A 1 288 ? 51.100 34.400 19.982  1.00 11.72 ? 288  PRO A CD  1 
ATOM   2273 N  N   . SER A 1 289 ? 48.693 31.659 22.954  1.00 13.78 ? 289  SER A N   1 
ATOM   2274 C  CA  . SER A 1 289 ? 47.358 31.272 23.392  1.00 15.09 ? 289  SER A CA  1 
ATOM   2275 C  C   . SER A 1 289 ? 46.446 32.453 23.728  1.00 15.67 ? 289  SER A C   1 
ATOM   2276 O  O   . SER A 1 289 ? 45.281 32.457 23.345  1.00 16.33 ? 289  SER A O   1 
ATOM   2277 C  CB  . SER A 1 289 ? 47.471 30.329 24.596  1.00 14.46 ? 289  SER A CB  1 
ATOM   2278 O  OG  . SER A 1 289 ? 46.204 29.899 25.058  1.00 15.77 ? 289  SER A OG  1 
ATOM   2279 N  N   . ASP A 1 290 ? 46.990 33.468 24.397  1.00 15.00 ? 290  ASP A N   1 
ATOM   2280 C  CA  . ASP A 1 290 ? 46.204 34.637 24.795  1.00 16.57 ? 290  ASP A CA  1 
ATOM   2281 C  C   . ASP A 1 290 ? 45.903 35.654 23.692  1.00 12.64 ? 290  ASP A C   1 
ATOM   2282 O  O   . ASP A 1 290 ? 45.304 36.697 23.944  1.00 12.84 ? 290  ASP A O   1 
ATOM   2283 C  CB  . ASP A 1 290 ? 46.810 35.319 26.035  1.00 23.42 ? 290  ASP A CB  1 
ATOM   2284 C  CG  . ASP A 1 290 ? 48.287 35.674 25.870  1.00 33.33 ? 290  ASP A CG  1 
ATOM   2285 O  OD1 . ASP A 1 290 ? 48.806 35.666 24.732  1.00 38.22 ? 290  ASP A OD1 1 
ATOM   2286 O  OD2 . ASP A 1 290 ? 48.935 35.968 26.900  1.00 38.41 ? 290  ASP A OD2 1 
ATOM   2287 N  N   . ARG A 1 291 ? 46.317 35.352 22.472  1.00 8.33  ? 291  ARG A N   1 
ATOM   2288 C  CA  . ARG A 1 291 ? 46.048 36.223 21.344  1.00 7.24  ? 291  ARG A CA  1 
ATOM   2289 C  C   . ARG A 1 291 ? 45.197 35.449 20.365  1.00 6.31  ? 291  ARG A C   1 
ATOM   2290 O  O   . ARG A 1 291 ? 44.778 35.987 19.350  1.00 10.21 ? 291  ARG A O   1 
ATOM   2291 C  CB  . ARG A 1 291 ? 47.345 36.619 20.642  1.00 4.01  ? 291  ARG A CB  1 
ATOM   2292 C  CG  . ARG A 1 291 ? 48.204 37.570 21.429  1.00 9.46  ? 291  ARG A CG  1 
ATOM   2293 C  CD  . ARG A 1 291 ? 47.492 38.888 21.646  1.00 8.50  ? 291  ARG A CD  1 
ATOM   2294 N  NE  . ARG A 1 291 ? 48.227 39.745 22.573  1.00 17.09 ? 291  ARG A NE  1 
ATOM   2295 C  CZ  . ARG A 1 291 ? 48.058 39.748 23.894  1.00 19.07 ? 291  ARG A CZ  1 
ATOM   2296 N  NH1 . ARG A 1 291 ? 47.158 38.949 24.460  1.00 19.38 ? 291  ARG A NH1 1 
ATOM   2297 N  NH2 . ARG A 1 291 ? 48.779 40.566 24.652  1.00 20.45 ? 291  ARG A NH2 1 
ATOM   2298 N  N   . ALA A 1 292 ? 44.858 34.216 20.716  1.00 7.02  ? 292  ALA A N   1 
ATOM   2299 C  CA  . ALA A 1 292 ? 44.124 33.375 19.789  1.00 7.81  ? 292  ALA A CA  1 
ATOM   2300 C  C   . ALA A 1 292 ? 42.656 33.087 20.012  1.00 7.34  ? 292  ALA A C   1 
ATOM   2301 O  O   . ALA A 1 292 ? 42.197 32.926 21.143  1.00 11.11 ? 292  ALA A O   1 
ATOM   2302 C  CB  . ALA A 1 292 ? 44.866 32.057 19.617  1.00 4.23  ? 292  ALA A CB  1 
ATOM   2303 N  N   . LEU A 1 293 ? 41.926 33.053 18.902  1.00 6.67  ? 293  LEU A N   1 
ATOM   2304 C  CA  . LEU A 1 293 ? 40.519 32.680 18.893  1.00 8.96  ? 293  LEU A CA  1 
ATOM   2305 C  C   . LEU A 1 293 ? 40.577 31.439 18.004  1.00 10.57 ? 293  LEU A C   1 
ATOM   2306 O  O   . LEU A 1 293 ? 40.992 31.525 16.842  1.00 8.76  ? 293  LEU A O   1 
ATOM   2307 C  CB  . LEU A 1 293 ? 39.623 33.730 18.246  1.00 2.72  ? 293  LEU A CB  1 
ATOM   2308 C  CG  . LEU A 1 293 ? 38.189 33.194 18.309  1.00 6.32  ? 293  LEU A CG  1 
ATOM   2309 C  CD1 . LEU A 1 293 ? 37.327 34.063 19.196  1.00 7.81  ? 293  LEU A CD1 1 
ATOM   2310 C  CD2 . LEU A 1 293 ? 37.612 33.061 16.923  1.00 5.47  ? 293  LEU A CD2 1 
ATOM   2311 N  N   . VAL A 1 294 ? 40.230 30.286 18.564  1.00 10.28 ? 294  VAL A N   1 
ATOM   2312 C  CA  . VAL A 1 294 ? 40.298 29.041 17.817  1.00 9.12  ? 294  VAL A CA  1 
ATOM   2313 C  C   . VAL A 1 294 ? 38.941 28.425 17.519  1.00 8.38  ? 294  VAL A C   1 
ATOM   2314 O  O   . VAL A 1 294 ? 37.946 28.718 18.185  1.00 10.15 ? 294  VAL A O   1 
ATOM   2315 C  CB  . VAL A 1 294 ? 41.239 28.027 18.511  1.00 7.33  ? 294  VAL A CB  1 
ATOM   2316 C  CG1 . VAL A 1 294 ? 42.600 28.667 18.707  1.00 7.37  ? 294  VAL A CG1 1 
ATOM   2317 C  CG2 . VAL A 1 294 ? 40.676 27.592 19.861  1.00 5.12  ? 294  VAL A CG2 1 
ATOM   2318 N  N   . PHE A 1 295 ? 38.921 27.576 16.498  1.00 7.63  ? 295  PHE A N   1 
ATOM   2319 C  CA  . PHE A 1 295 ? 37.713 26.921 16.021  1.00 7.98  ? 295  PHE A CA  1 
ATOM   2320 C  C   . PHE A 1 295 ? 38.132 25.791 15.091  1.00 8.05  ? 295  PHE A C   1 
ATOM   2321 O  O   . PHE A 1 295 ? 39.281 25.744 14.642  1.00 10.10 ? 295  PHE A O   1 
ATOM   2322 C  CB  . PHE A 1 295 ? 36.864 27.932 15.234  1.00 7.64  ? 295  PHE A CB  1 
ATOM   2323 C  CG  . PHE A 1 295 ? 37.658 28.748 14.231  1.00 6.51  ? 295  PHE A CG  1 
ATOM   2324 C  CD1 . PHE A 1 295 ? 38.378 29.873 14.640  1.00 6.80  ? 295  PHE A CD1 1 
ATOM   2325 C  CD2 . PHE A 1 295 ? 37.707 28.380 12.891  1.00 6.74  ? 295  PHE A CD2 1 
ATOM   2326 C  CE1 . PHE A 1 295 ? 39.136 30.614 13.732  1.00 2.00  ? 295  PHE A CE1 1 
ATOM   2327 C  CE2 . PHE A 1 295 ? 38.462 29.115 11.976  1.00 3.84  ? 295  PHE A CE2 1 
ATOM   2328 C  CZ  . PHE A 1 295 ? 39.178 30.232 12.400  1.00 4.89  ? 295  PHE A CZ  1 
ATOM   2329 N  N   . VAL A 1 296 ? 37.212 24.873 14.820  1.00 6.47  ? 296  VAL A N   1 
ATOM   2330 C  CA  . VAL A 1 296 ? 37.496 23.756 13.929  1.00 7.64  ? 296  VAL A CA  1 
ATOM   2331 C  C   . VAL A 1 296 ? 37.163 24.176 12.497  1.00 7.75  ? 296  VAL A C   1 
ATOM   2332 O  O   . VAL A 1 296 ? 37.943 23.954 11.574  1.00 10.78 ? 296  VAL A O   1 
ATOM   2333 C  CB  . VAL A 1 296 ? 36.704 22.490 14.344  1.00 6.98  ? 296  VAL A CB  1 
ATOM   2334 C  CG1 . VAL A 1 296 ? 36.945 21.360 13.352  1.00 8.69  ? 296  VAL A CG1 1 
ATOM   2335 C  CG2 . VAL A 1 296 ? 37.138 22.047 15.736  1.00 6.77  ? 296  VAL A CG2 1 
ATOM   2336 N  N   . ASP A 1 297 ? 36.022 24.831 12.333  1.00 10.73 ? 297  ASP A N   1 
ATOM   2337 C  CA  . ASP A 1 297 ? 35.580 25.323 11.031  1.00 7.72  ? 297  ASP A CA  1 
ATOM   2338 C  C   . ASP A 1 297 ? 34.841 26.627 11.296  1.00 7.79  ? 297  ASP A C   1 
ATOM   2339 O  O   . ASP A 1 297 ? 34.465 26.892 12.438  1.00 7.94  ? 297  ASP A O   1 
ATOM   2340 C  CB  . ASP A 1 297 ? 34.641 24.308 10.354  1.00 6.39  ? 297  ASP A CB  1 
ATOM   2341 C  CG  . ASP A 1 297 ? 33.339 24.077 11.130  1.00 8.41  ? 297  ASP A CG  1 
ATOM   2342 O  OD1 . ASP A 1 297 ? 33.357 24.061 12.380  1.00 7.54  ? 297  ASP A OD1 1 
ATOM   2343 O  OD2 . ASP A 1 297 ? 32.285 23.895 10.478  1.00 10.19 ? 297  ASP A OD2 1 
ATOM   2344 N  N   . ASN A 1 298 ? 34.707 27.469 10.274  1.00 9.17  ? 298  ASN A N   1 
ATOM   2345 C  CA  . ASN A 1 298 ? 33.975 28.732 10.394  1.00 6.96  ? 298  ASN A CA  1 
ATOM   2346 C  C   . ASN A 1 298 ? 33.042 28.827 9.181   1.00 7.91  ? 298  ASN A C   1 
ATOM   2347 O  O   . ASN A 1 298 ? 33.121 27.996 8.281   1.00 6.85  ? 298  ASN A O   1 
ATOM   2348 C  CB  . ASN A 1 298 ? 34.932 29.941 10.521  1.00 8.66  ? 298  ASN A CB  1 
ATOM   2349 C  CG  . ASN A 1 298 ? 35.513 30.401 9.190   1.00 6.89  ? 298  ASN A CG  1 
ATOM   2350 O  OD1 . ASN A 1 298 ? 35.526 29.662 8.208   1.00 9.84  ? 298  ASN A OD1 1 
ATOM   2351 N  ND2 . ASN A 1 298 ? 35.996 31.642 9.157   1.00 6.74  ? 298  ASN A ND2 1 
ATOM   2352 N  N   . HIS A 1 299 ? 32.143 29.806 9.156   1.00 8.32  ? 299  HIS A N   1 
ATOM   2353 C  CA  . HIS A 1 299 ? 31.190 29.922 8.045   1.00 6.23  ? 299  HIS A CA  1 
ATOM   2354 C  C   . HIS A 1 299 ? 31.787 29.848 6.642   1.00 9.92  ? 299  HIS A C   1 
ATOM   2355 O  O   . HIS A 1 299 ? 31.121 29.405 5.710   1.00 12.66 ? 299  HIS A O   1 
ATOM   2356 C  CB  . HIS A 1 299 ? 30.320 31.185 8.182   1.00 9.13  ? 299  HIS A CB  1 
ATOM   2357 C  CG  . HIS A 1 299 ? 31.032 32.464 7.863   1.00 7.05  ? 299  HIS A CG  1 
ATOM   2358 N  ND1 . HIS A 1 299 ? 31.803 33.142 8.784   1.00 7.17  ? 299  HIS A ND1 1 
ATOM   2359 C  CD2 . HIS A 1 299 ? 31.081 33.195 6.723   1.00 9.02  ? 299  HIS A CD2 1 
ATOM   2360 C  CE1 . HIS A 1 299 ? 32.293 34.234 8.226   1.00 9.14  ? 299  HIS A CE1 1 
ATOM   2361 N  NE2 . HIS A 1 299 ? 31.870 34.290 6.976   1.00 7.82  ? 299  HIS A NE2 1 
ATOM   2362 N  N   . ASP A 1 300 ? 33.035 30.283 6.497   1.00 10.47 ? 300  ASP A N   1 
ATOM   2363 C  CA  . ASP A 1 300 ? 33.711 30.286 5.210   1.00 9.19  ? 300  ASP A CA  1 
ATOM   2364 C  C   . ASP A 1 300 ? 34.263 28.944 4.768   1.00 11.83 ? 300  ASP A C   1 
ATOM   2365 O  O   . ASP A 1 300 ? 33.911 28.442 3.691   1.00 9.37  ? 300  ASP A O   1 
ATOM   2366 C  CB  . ASP A 1 300 ? 34.880 31.272 5.225   1.00 16.80 ? 300  ASP A CB  1 
ATOM   2367 C  CG  . ASP A 1 300 ? 34.495 32.659 4.773   1.00 19.70 ? 300  ASP A CG  1 
ATOM   2368 O  OD1 . ASP A 1 300 ? 33.437 32.830 4.133   1.00 22.25 ? 300  ASP A OD1 1 
ATOM   2369 O  OD2 . ASP A 1 300 ? 35.283 33.586 5.045   1.00 22.28 ? 300  ASP A OD2 1 
ATOM   2370 N  N   . ASN A 1 301 ? 35.158 28.378 5.575   1.00 8.77  ? 301  ASN A N   1 
ATOM   2371 C  CA  . ASN A 1 301 ? 35.792 27.125 5.198   1.00 9.91  ? 301  ASN A CA  1 
ATOM   2372 C  C   . ASN A 1 301 ? 34.960 25.852 5.272   1.00 10.68 ? 301  ASN A C   1 
ATOM   2373 O  O   . ASN A 1 301 ? 35.385 24.816 4.768   1.00 10.85 ? 301  ASN A O   1 
ATOM   2374 C  CB  . ASN A 1 301 ? 37.178 26.960 5.852   1.00 4.78  ? 301  ASN A CB  1 
ATOM   2375 C  CG  . ASN A 1 301 ? 37.121 26.857 7.350   1.00 6.51  ? 301  ASN A CG  1 
ATOM   2376 O  OD1 . ASN A 1 301 ? 36.084 26.551 7.924   1.00 11.88 ? 301  ASN A OD1 1 
ATOM   2377 N  ND2 . ASN A 1 301 ? 38.248 27.097 7.998   1.00 8.93  ? 301  ASN A ND2 1 
ATOM   2378 N  N   . GLN A 1 302 ? 33.769 25.915 5.859   1.00 12.85 ? 302  GLN A N   1 
ATOM   2379 C  CA  . GLN A 1 302 ? 32.930 24.723 5.907   1.00 13.30 ? 302  GLN A CA  1 
ATOM   2380 C  C   . GLN A 1 302 ? 32.314 24.478 4.525   1.00 15.05 ? 302  GLN A C   1 
ATOM   2381 O  O   . GLN A 1 302 ? 31.838 23.378 4.238   1.00 19.72 ? 302  GLN A O   1 
ATOM   2382 C  CB  . GLN A 1 302 ? 31.833 24.839 6.971   1.00 12.30 ? 302  GLN A CB  1 
ATOM   2383 C  CG  . GLN A 1 302 ? 30.741 25.847 6.677   1.00 9.22  ? 302  GLN A CG  1 
ATOM   2384 C  CD  . GLN A 1 302 ? 29.517 25.677 7.574   1.00 9.41  ? 302  GLN A CD  1 
ATOM   2385 O  OE1 . GLN A 1 302 ? 28.452 26.226 7.294   1.00 12.93 ? 302  GLN A OE1 1 
ATOM   2386 N  NE2 . GLN A 1 302 ? 29.663 24.921 8.654   1.00 7.67  ? 302  GLN A NE2 1 
ATOM   2387 N  N   . ARG A 1 303 ? 32.381 25.494 3.664   1.00 13.28 ? 303  ARG A N   1 
ATOM   2388 C  CA  . ARG A 1 303 ? 31.836 25.433 2.309   1.00 16.29 ? 303  ARG A CA  1 
ATOM   2389 C  C   . ARG A 1 303 ? 32.830 25.832 1.221   1.00 20.99 ? 303  ARG A C   1 
ATOM   2390 O  O   . ARG A 1 303 ? 32.439 26.433 0.219   1.00 23.74 ? 303  ARG A O   1 
ATOM   2391 C  CB  . ARG A 1 303 ? 30.577 26.304 2.188   1.00 13.88 ? 303  ARG A CB  1 
ATOM   2392 C  CG  . ARG A 1 303 ? 30.729 27.707 2.746   1.00 12.01 ? 303  ARG A CG  1 
ATOM   2393 C  CD  . ARG A 1 303 ? 29.539 28.600 2.420   1.00 8.27  ? 303  ARG A CD  1 
ATOM   2394 N  NE  . ARG A 1 303 ? 28.242 28.053 2.821   1.00 5.31  ? 303  ARG A NE  1 
ATOM   2395 C  CZ  . ARG A 1 303 ? 27.864 27.815 4.074   1.00 7.64  ? 303  ARG A CZ  1 
ATOM   2396 N  NH1 . ARG A 1 303 ? 28.697 28.019 5.088   1.00 7.72  ? 303  ARG A NH1 1 
ATOM   2397 N  NH2 . ARG A 1 303 ? 26.655 27.329 4.316   1.00 7.97  ? 303  ARG A NH2 1 
ATOM   2398 N  N   . GLY A 1 304 ? 34.108 25.535 1.432   1.00 27.04 ? 304  GLY A N   1 
ATOM   2399 C  CA  . GLY A 1 304 ? 35.125 25.847 0.435   1.00 29.26 ? 304  GLY A CA  1 
ATOM   2400 C  C   . GLY A 1 304 ? 35.692 27.254 0.340   1.00 31.40 ? 304  GLY A C   1 
ATOM   2401 O  O   . GLY A 1 304 ? 36.719 27.452 -0.317  1.00 35.44 ? 304  GLY A O   1 
ATOM   2402 N  N   . HIS A 1 305 ? 35.044 28.233 0.966   1.00 30.50 ? 305  HIS A N   1 
ATOM   2403 C  CA  . HIS A 1 305 ? 35.533 29.612 0.922   1.00 32.70 ? 305  HIS A CA  1 
ATOM   2404 C  C   . HIS A 1 305 ? 36.646 29.815 1.940   1.00 34.57 ? 305  HIS A C   1 
ATOM   2405 O  O   . HIS A 1 305 ? 36.904 28.932 2.760   1.00 37.79 ? 305  HIS A O   1 
ATOM   2406 C  CB  . HIS A 1 305 ? 34.393 30.593 1.196   1.00 34.14 ? 305  HIS A CB  1 
ATOM   2407 C  CG  . HIS A 1 305 ? 33.381 30.665 0.098   1.00 35.17 ? 305  HIS A CG  1 
ATOM   2408 N  ND1 . HIS A 1 305 ? 33.170 31.807 -0.644  1.00 38.43 ? 305  HIS A ND1 1 
ATOM   2409 C  CD2 . HIS A 1 305 ? 32.532 29.734 -0.398  1.00 35.85 ? 305  HIS A CD2 1 
ATOM   2410 C  CE1 . HIS A 1 305 ? 32.237 31.576 -1.551  1.00 37.55 ? 305  HIS A CE1 1 
ATOM   2411 N  NE2 . HIS A 1 305 ? 31.834 30.326 -1.421  1.00 36.60 ? 305  HIS A NE2 1 
ATOM   2412 N  N   . GLY A 1 306 ? 37.306 30.967 1.891   1.00 36.50 ? 306  GLY A N   1 
ATOM   2413 C  CA  . GLY A 1 306 ? 38.379 31.246 2.833   1.00 39.11 ? 306  GLY A CA  1 
ATOM   2414 C  C   . GLY A 1 306 ? 39.561 30.296 2.713   1.00 42.10 ? 306  GLY A C   1 
ATOM   2415 O  O   . GLY A 1 306 ? 39.994 29.986 1.600   1.00 43.69 ? 306  GLY A O   1 
ATOM   2416 N  N   . ALA A 1 307 ? 40.066 29.816 3.851   1.00 43.86 ? 307  ALA A N   1 
ATOM   2417 C  CA  . ALA A 1 307 ? 41.216 28.909 3.875   1.00 41.00 ? 307  ALA A CA  1 
ATOM   2418 C  C   . ALA A 1 307 ? 41.108 27.700 4.811   1.00 38.86 ? 307  ALA A C   1 
ATOM   2419 O  O   . ALA A 1 307 ? 40.543 27.772 5.911   1.00 37.39 ? 307  ALA A O   1 
ATOM   2420 C  CB  . ALA A 1 307 ? 42.481 29.689 4.189   1.00 43.51 ? 307  ALA A CB  1 
ATOM   2421 N  N   . GLY A 1 308 ? 41.723 26.607 4.377   1.00 35.87 ? 308  GLY A N   1 
ATOM   2422 C  CA  . GLY A 1 308 ? 41.724 25.370 5.132   1.00 30.45 ? 308  GLY A CA  1 
ATOM   2423 C  C   . GLY A 1 308 ? 41.717 24.222 4.140   1.00 30.08 ? 308  GLY A C   1 
ATOM   2424 O  O   . GLY A 1 308 ? 42.453 23.243 4.287   1.00 32.31 ? 308  GLY A O   1 
ATOM   2425 N  N   . GLY A 1 309 ? 40.879 24.350 3.116   1.00 21.77 ? 309  GLY A N   1 
ATOM   2426 C  CA  . GLY A 1 309 ? 40.803 23.332 2.092   1.00 19.21 ? 309  GLY A CA  1 
ATOM   2427 C  C   . GLY A 1 309 ? 40.000 22.103 2.454   1.00 20.43 ? 309  GLY A C   1 
ATOM   2428 O  O   . GLY A 1 309 ? 39.079 22.156 3.267   1.00 20.10 ? 309  GLY A O   1 
ATOM   2429 N  N   . ALA A 1 310 ? 40.370 20.981 1.849   1.00 18.09 ? 310  ALA A N   1 
ATOM   2430 C  CA  . ALA A 1 310 ? 39.676 19.725 2.072   1.00 18.99 ? 310  ALA A CA  1 
ATOM   2431 C  C   . ALA A 1 310 ? 39.842 19.143 3.468   1.00 17.98 ? 310  ALA A C   1 
ATOM   2432 O  O   . ALA A 1 310 ? 38.969 18.409 3.933   1.00 24.31 ? 310  ALA A O   1 
ATOM   2433 C  CB  . ALA A 1 310 ? 40.106 18.707 1.034   1.00 21.23 ? 310  ALA A CB  1 
ATOM   2434 N  N   . SER A 1 311 ? 40.938 19.479 4.142   1.00 13.26 ? 311  SER A N   1 
ATOM   2435 C  CA  . SER A 1 311 ? 41.199 18.940 5.472   1.00 13.27 ? 311  SER A CA  1 
ATOM   2436 C  C   . SER A 1 311 ? 40.231 19.387 6.552   1.00 13.07 ? 311  SER A C   1 
ATOM   2437 O  O   . SER A 1 311 ? 40.115 18.733 7.585   1.00 16.93 ? 311  SER A O   1 
ATOM   2438 C  CB  . SER A 1 311 ? 42.630 19.252 5.904   1.00 15.99 ? 311  SER A CB  1 
ATOM   2439 O  OG  . SER A 1 311 ? 42.840 20.647 6.007   1.00 25.11 ? 311  SER A OG  1 
ATOM   2440 N  N   . ILE A 1 312 ? 39.560 20.511 6.330   1.00 13.21 ? 312  ILE A N   1 
ATOM   2441 C  CA  . ILE A 1 312 ? 38.608 21.051 7.303   1.00 10.37 ? 312  ILE A CA  1 
ATOM   2442 C  C   . ILE A 1 312 ? 37.454 20.088 7.593   1.00 10.79 ? 312  ILE A C   1 
ATOM   2443 O  O   . ILE A 1 312 ? 36.829 19.562 6.673   1.00 8.57  ? 312  ILE A O   1 
ATOM   2444 C  CB  . ILE A 1 312 ? 38.023 22.420 6.819   1.00 8.77  ? 312  ILE A CB  1 
ATOM   2445 C  CG1 . ILE A 1 312 ? 39.151 23.441 6.632   1.00 2.22  ? 312  ILE A CG1 1 
ATOM   2446 C  CG2 . ILE A 1 312 ? 36.994 22.955 7.817   1.00 5.87  ? 312  ILE A CG2 1 
ATOM   2447 C  CD1 . ILE A 1 312 ? 39.874 23.793 7.903   1.00 2.00  ? 312  ILE A CD1 1 
ATOM   2448 N  N   . LEU A 1 313 ? 37.185 19.864 8.875   1.00 9.37  ? 313  LEU A N   1 
ATOM   2449 C  CA  . LEU A 1 313 ? 36.100 18.989 9.308   1.00 9.65  ? 313  LEU A CA  1 
ATOM   2450 C  C   . LEU A 1 313 ? 34.859 19.831 9.583   1.00 7.65  ? 313  LEU A C   1 
ATOM   2451 O  O   . LEU A 1 313 ? 34.957 20.919 10.132  1.00 8.75  ? 313  LEU A O   1 
ATOM   2452 C  CB  . LEU A 1 313 ? 36.508 18.218 10.565  1.00 9.01  ? 313  LEU A CB  1 
ATOM   2453 C  CG  . LEU A 1 313 ? 37.588 17.150 10.355  1.00 9.03  ? 313  LEU A CG  1 
ATOM   2454 C  CD1 . LEU A 1 313 ? 38.191 16.736 11.680  1.00 9.10  ? 313  LEU A CD1 1 
ATOM   2455 C  CD2 . LEU A 1 313 ? 36.986 15.961 9.641   1.00 5.45  ? 313  LEU A CD2 1 
ATOM   2456 N  N   . THR A 1 314 ? 33.699 19.335 9.173   1.00 8.30  ? 314  THR A N   1 
ATOM   2457 C  CA  . THR A 1 314 ? 32.441 20.047 9.359   1.00 8.51  ? 314  THR A CA  1 
ATOM   2458 C  C   . THR A 1 314 ? 31.394 19.057 9.861   1.00 10.83 ? 314  THR A C   1 
ATOM   2459 O  O   . THR A 1 314 ? 31.672 17.860 9.997   1.00 12.65 ? 314  THR A O   1 
ATOM   2460 C  CB  . THR A 1 314 ? 31.926 20.643 8.027   1.00 8.89  ? 314  THR A CB  1 
ATOM   2461 O  OG1 . THR A 1 314 ? 31.438 19.587 7.184   1.00 9.65  ? 314  THR A OG1 1 
ATOM   2462 C  CG2 . THR A 1 314 ? 33.033 21.385 7.301   1.00 4.76  ? 314  THR A CG2 1 
ATOM   2463 N  N   . PHE A 1 315 ? 30.180 19.543 10.091  1.00 11.96 ? 315  PHE A N   1 
ATOM   2464 C  CA  . PHE A 1 315 ? 29.101 18.686 10.564  1.00 10.12 ? 315  PHE A CA  1 
ATOM   2465 C  C   . PHE A 1 315 ? 28.805 17.569 9.560   1.00 12.10 ? 315  PHE A C   1 
ATOM   2466 O  O   . PHE A 1 315 ? 28.153 16.586 9.906   1.00 16.43 ? 315  PHE A O   1 
ATOM   2467 C  CB  . PHE A 1 315 ? 27.832 19.499 10.831  1.00 9.34  ? 315  PHE A CB  1 
ATOM   2468 C  CG  . PHE A 1 315 ? 27.196 20.069 9.588   1.00 6.60  ? 315  PHE A CG  1 
ATOM   2469 C  CD1 . PHE A 1 315 ? 26.272 19.328 8.858   1.00 5.09  ? 315  PHE A CD1 1 
ATOM   2470 C  CD2 . PHE A 1 315 ? 27.519 21.344 9.154   1.00 4.01  ? 315  PHE A CD2 1 
ATOM   2471 C  CE1 . PHE A 1 315 ? 25.683 19.854 7.717   1.00 2.80  ? 315  PHE A CE1 1 
ATOM   2472 C  CE2 . PHE A 1 315 ? 26.942 21.877 8.024   1.00 4.92  ? 315  PHE A CE2 1 
ATOM   2473 C  CZ  . PHE A 1 315 ? 26.017 21.132 7.297   1.00 5.27  ? 315  PHE A CZ  1 
ATOM   2474 N  N   . TRP A 1 316 ? 29.260 17.735 8.319   1.00 14.16 ? 316  TRP A N   1 
ATOM   2475 C  CA  . TRP A 1 316 ? 29.053 16.729 7.279   1.00 14.92 ? 316  TRP A CA  1 
ATOM   2476 C  C   . TRP A 1 316 ? 29.784 15.430 7.626   1.00 15.65 ? 316  TRP A C   1 
ATOM   2477 O  O   . TRP A 1 316 ? 29.355 14.350 7.232   1.00 18.52 ? 316  TRP A O   1 
ATOM   2478 C  CB  . TRP A 1 316 ? 29.539 17.240 5.924   1.00 12.85 ? 316  TRP A CB  1 
ATOM   2479 C  CG  . TRP A 1 316 ? 28.713 18.340 5.331   1.00 14.07 ? 316  TRP A CG  1 
ATOM   2480 C  CD1 . TRP A 1 316 ? 29.116 19.619 5.090   1.00 14.86 ? 316  TRP A CD1 1 
ATOM   2481 C  CD2 . TRP A 1 316 ? 27.371 18.244 4.843   1.00 12.54 ? 316  TRP A CD2 1 
ATOM   2482 N  NE1 . TRP A 1 316 ? 28.115 20.323 4.476   1.00 13.28 ? 316  TRP A NE1 1 
ATOM   2483 C  CE2 . TRP A 1 316 ? 27.030 19.506 4.313   1.00 13.96 ? 316  TRP A CE2 1 
ATOM   2484 C  CE3 . TRP A 1 316 ? 26.423 17.214 4.799   1.00 16.36 ? 316  TRP A CE3 1 
ATOM   2485 C  CZ2 . TRP A 1 316 ? 25.778 19.769 3.744   1.00 15.75 ? 316  TRP A CZ2 1 
ATOM   2486 C  CZ3 . TRP A 1 316 ? 25.174 17.476 4.231   1.00 15.88 ? 316  TRP A CZ3 1 
ATOM   2487 C  CH2 . TRP A 1 316 ? 24.867 18.746 3.713   1.00 15.90 ? 316  TRP A CH2 1 
ATOM   2488 N  N   . ASP A 1 317 ? 30.904 15.554 8.332   1.00 16.45 ? 317  ASP A N   1 
ATOM   2489 C  CA  . ASP A 1 317 ? 31.704 14.409 8.767   1.00 13.32 ? 317  ASP A CA  1 
ATOM   2490 C  C   . ASP A 1 317 ? 31.524 14.344 10.271  1.00 10.31 ? 317  ASP A C   1 
ATOM   2491 O  O   . ASP A 1 317 ? 32.490 14.398 11.029  1.00 13.48 ? 317  ASP A O   1 
ATOM   2492 C  CB  . ASP A 1 317 ? 33.172 14.641 8.430   1.00 17.23 ? 317  ASP A CB  1 
ATOM   2493 C  CG  . ASP A 1 317 ? 33.386 14.932 6.962   1.00 22.43 ? 317  ASP A CG  1 
ATOM   2494 O  OD1 . ASP A 1 317 ? 32.985 14.094 6.127   1.00 26.79 ? 317  ASP A OD1 1 
ATOM   2495 O  OD2 . ASP A 1 317 ? 33.942 16.002 6.642   1.00 26.80 ? 317  ASP A OD2 1 
ATOM   2496 N  N   . ALA A 1 318 ? 30.270 14.221 10.683  1.00 9.10  ? 318  ALA A N   1 
ATOM   2497 C  CA  . ALA A 1 318 ? 29.881 14.205 12.088  1.00 9.76  ? 318  ALA A CA  1 
ATOM   2498 C  C   . ALA A 1 318 ? 30.795 13.486 13.071  1.00 12.34 ? 318  ALA A C   1 
ATOM   2499 O  O   . ALA A 1 318 ? 31.240 14.088 14.049  1.00 18.59 ? 318  ALA A O   1 
ATOM   2500 C  CB  . ALA A 1 318 ? 28.456 13.697 12.224  1.00 5.18  ? 318  ALA A CB  1 
ATOM   2501 N  N   . ARG A 1 319 ? 31.110 12.223 12.802  1.00 12.97 ? 319  ARG A N   1 
ATOM   2502 C  CA  . ARG A 1 319 ? 31.940 11.438 13.711  1.00 11.71 ? 319  ARG A CA  1 
ATOM   2503 C  C   . ARG A 1 319 ? 33.307 12.045 14.003  1.00 10.20 ? 319  ARG A C   1 
ATOM   2504 O  O   . ARG A 1 319 ? 33.668 12.229 15.164  1.00 13.15 ? 319  ARG A O   1 
ATOM   2505 C  CB  . ARG A 1 319 ? 32.078 10.007 13.199  1.00 14.63 ? 319  ARG A CB  1 
ATOM   2506 C  CG  . ARG A 1 319 ? 32.577 9.023  14.239  1.00 16.68 ? 319  ARG A CG  1 
ATOM   2507 C  CD  . ARG A 1 319 ? 32.505 7.587  13.725  1.00 20.37 ? 319  ARG A CD  1 
ATOM   2508 N  NE  . ARG A 1 319 ? 33.063 6.633  14.681  1.00 22.84 ? 319  ARG A NE  1 
ATOM   2509 C  CZ  . ARG A 1 319 ? 34.313 6.180  14.641  1.00 24.56 ? 319  ARG A CZ  1 
ATOM   2510 N  NH1 . ARG A 1 319 ? 35.135 6.574  13.679  1.00 25.12 ? 319  ARG A NH1 1 
ATOM   2511 N  NH2 . ARG A 1 319 ? 34.738 5.318  15.556  1.00 25.85 ? 319  ARG A NH2 1 
ATOM   2512 N  N   . LEU A 1 320 ? 34.051 12.385 12.957  1.00 11.16 ? 320  LEU A N   1 
ATOM   2513 C  CA  . LEU A 1 320 ? 35.377 12.977 13.119  1.00 9.89  ? 320  LEU A CA  1 
ATOM   2514 C  C   . LEU A 1 320 ? 35.264 14.411 13.624  1.00 10.18 ? 320  LEU A C   1 
ATOM   2515 O  O   . LEU A 1 320 ? 36.104 14.881 14.393  1.00 9.58  ? 320  LEU A O   1 
ATOM   2516 C  CB  . LEU A 1 320 ? 36.137 12.941 11.790  1.00 13.92 ? 320  LEU A CB  1 
ATOM   2517 C  CG  . LEU A 1 320 ? 37.109 11.781 11.541  1.00 18.16 ? 320  LEU A CG  1 
ATOM   2518 C  CD1 . LEU A 1 320 ? 36.618 10.505 12.190  1.00 20.22 ? 320  LEU A CD1 1 
ATOM   2519 C  CD2 . LEU A 1 320 ? 37.313 11.592 10.047  1.00 15.69 ? 320  LEU A CD2 1 
ATOM   2520 N  N   . TYR A 1 321 ? 34.202 15.091 13.206  1.00 8.77  ? 321  TYR A N   1 
ATOM   2521 C  CA  . TYR A 1 321 ? 33.962 16.463 13.617  1.00 9.26  ? 321  TYR A CA  1 
ATOM   2522 C  C   . TYR A 1 321 ? 33.828 16.501 15.135  1.00 12.16 ? 321  TYR A C   1 
ATOM   2523 O  O   . TYR A 1 321 ? 34.437 17.342 15.802  1.00 16.11 ? 321  TYR A O   1 
ATOM   2524 C  CB  . TYR A 1 321 ? 32.693 17.002 12.957  1.00 10.28 ? 321  TYR A CB  1 
ATOM   2525 C  CG  . TYR A 1 321 ? 32.457 18.471 13.204  1.00 13.03 ? 321  TYR A CG  1 
ATOM   2526 C  CD1 . TYR A 1 321 ? 33.332 19.431 12.695  1.00 10.44 ? 321  TYR A CD1 1 
ATOM   2527 C  CD2 . TYR A 1 321 ? 31.366 18.908 13.953  1.00 12.15 ? 321  TYR A CD2 1 
ATOM   2528 C  CE1 . TYR A 1 321 ? 33.128 20.786 12.924  1.00 8.20  ? 321  TYR A CE1 1 
ATOM   2529 C  CE2 . TYR A 1 321 ? 31.158 20.262 14.188  1.00 10.52 ? 321  TYR A CE2 1 
ATOM   2530 C  CZ  . TYR A 1 321 ? 32.042 21.192 13.668  1.00 11.36 ? 321  TYR A CZ  1 
ATOM   2531 O  OH  . TYR A 1 321 ? 31.819 22.533 13.877  1.00 13.38 ? 321  TYR A OH  1 
ATOM   2532 N  N   . LYS A 1 322 ? 33.054 15.575 15.688  1.00 10.64 ? 322  LYS A N   1 
ATOM   2533 C  CA  . LYS A 1 322 ? 32.875 15.525 17.130  1.00 8.32  ? 322  LYS A CA  1 
ATOM   2534 C  C   . LYS A 1 322 ? 34.171 15.275 17.897  1.00 9.64  ? 322  LYS A C   1 
ATOM   2535 O  O   . LYS A 1 322 ? 34.376 15.868 18.960  1.00 10.99 ? 322  LYS A O   1 
ATOM   2536 C  CB  . LYS A 1 322 ? 31.810 14.502 17.519  1.00 8.81  ? 322  LYS A CB  1 
ATOM   2537 C  CG  . LYS A 1 322 ? 30.395 15.050 17.433  1.00 9.92  ? 322  LYS A CG  1 
ATOM   2538 C  CD  . LYS A 1 322 ? 29.362 13.991 17.726  1.00 8.28  ? 322  LYS A CD  1 
ATOM   2539 C  CE  . LYS A 1 322 ? 29.214 13.038 16.561  1.00 10.40 ? 322  LYS A CE  1 
ATOM   2540 N  NZ  . LYS A 1 322 ? 28.367 11.871 16.928  1.00 16.19 ? 322  LYS A NZ  1 
ATOM   2541 N  N   . VAL A 1 323 ? 35.071 14.445 17.374  1.00 20.00 ? 323  VAL A N   1 
ATOM   2542 C  CA  . VAL A 1 323 ? 36.305 14.222 18.117  1.00 20.00 ? 323  VAL A CA  1 
ATOM   2543 C  C   . VAL A 1 323 ? 37.229 15.450 18.059  1.00 20.00 ? 323  VAL A C   1 
ATOM   2544 O  O   . VAL A 1 323 ? 37.898 15.772 19.045  1.00 20.00 ? 323  VAL A O   1 
ATOM   2545 C  CB  . VAL A 1 323 ? 37.058 13.016 17.536  1.00 20.00 ? 323  VAL A CB  1 
ATOM   2546 C  CG1 . VAL A 1 323 ? 36.233 11.778 17.182  1.00 20.00 ? 323  VAL A CG1 1 
ATOM   2547 C  CG2 . VAL A 1 323 ? 38.347 12.902 16.723  1.00 20.00 ? 323  VAL A CG2 1 
ATOM   2548 N  N   . ALA A 1 324 ? 37.226 16.157 16.926  1.00 13.10 ? 324  ALA A N   1 
ATOM   2549 C  CA  . ALA A 1 324 ? 38.047 17.359 16.763  1.00 9.00  ? 324  ALA A CA  1 
ATOM   2550 C  C   . ALA A 1 324 ? 37.533 18.481 17.671  1.00 7.70  ? 324  ALA A C   1 
ATOM   2551 O  O   . ALA A 1 324 ? 38.311 19.141 18.355  1.00 9.17  ? 324  ALA A O   1 
ATOM   2552 C  CB  . ALA A 1 324 ? 38.051 17.805 15.311  1.00 8.12  ? 324  ALA A CB  1 
ATOM   2553 N  N   . VAL A 1 325 ? 36.219 18.683 17.692  1.00 6.79  ? 325  VAL A N   1 
ATOM   2554 C  CA  . VAL A 1 325 ? 35.618 19.706 18.547  1.00 4.55  ? 325  VAL A CA  1 
ATOM   2555 C  C   . VAL A 1 325 ? 35.880 19.340 20.005  1.00 7.89  ? 325  VAL A C   1 
ATOM   2556 O  O   . VAL A 1 325 ? 36.239 20.195 20.812  1.00 10.96 ? 325  VAL A O   1 
ATOM   2557 C  CB  . VAL A 1 325 ? 34.106 19.836 18.290  1.00 5.60  ? 325  VAL A CB  1 
ATOM   2558 C  CG1 . VAL A 1 325 ? 33.447 20.699 19.361  1.00 3.13  ? 325  VAL A CG1 1 
ATOM   2559 C  CG2 . VAL A 1 325 ? 33.870 20.442 16.919  1.00 2.30  ? 325  VAL A CG2 1 
ATOM   2560 N  N   . GLY A 1 326 ? 35.746 18.055 20.323  1.00 9.78  ? 326  GLY A N   1 
ATOM   2561 C  CA  . GLY A 1 326 ? 35.995 17.580 21.674  1.00 6.11  ? 326  GLY A CA  1 
ATOM   2562 C  C   . GLY A 1 326 ? 37.430 17.826 22.104  1.00 7.82  ? 326  GLY A C   1 
ATOM   2563 O  O   . GLY A 1 326 ? 37.684 18.244 23.238  1.00 9.84  ? 326  GLY A O   1 
ATOM   2564 N  N   . PHE A 1 327 ? 38.376 17.571 21.205  1.00 9.33  ? 327  PHE A N   1 
ATOM   2565 C  CA  . PHE A 1 327 ? 39.784 17.797 21.515  1.00 10.41 ? 327  PHE A CA  1 
ATOM   2566 C  C   . PHE A 1 327 ? 40.023 19.293 21.768  1.00 11.91 ? 327  PHE A C   1 
ATOM   2567 O  O   . PHE A 1 327 ? 40.678 19.667 22.744  1.00 11.72 ? 327  PHE A O   1 
ATOM   2568 C  CB  . PHE A 1 327 ? 40.680 17.307 20.373  1.00 10.87 ? 327  PHE A CB  1 
ATOM   2569 C  CG  . PHE A 1 327 ? 42.145 17.436 20.668  1.00 10.69 ? 327  PHE A CG  1 
ATOM   2570 C  CD1 . PHE A 1 327 ? 42.832 16.408 21.309  1.00 14.18 ? 327  PHE A CD1 1 
ATOM   2571 C  CD2 . PHE A 1 327 ? 42.833 18.603 20.349  1.00 11.26 ? 327  PHE A CD2 1 
ATOM   2572 C  CE1 . PHE A 1 327 ? 44.191 16.543 21.631  1.00 16.04 ? 327  PHE A CE1 1 
ATOM   2573 C  CE2 . PHE A 1 327 ? 44.188 18.748 20.666  1.00 12.14 ? 327  PHE A CE2 1 
ATOM   2574 C  CZ  . PHE A 1 327 ? 44.866 17.717 21.310  1.00 10.99 ? 327  PHE A CZ  1 
ATOM   2575 N  N   . MET A 1 328 ? 39.478 20.139 20.892  1.00 10.84 ? 328  MET A N   1 
ATOM   2576 C  CA  . MET A 1 328 ? 39.609 21.591 21.013  1.00 8.45  ? 328  MET A CA  1 
ATOM   2577 C  C   . MET A 1 328 ? 39.061 22.119 22.338  1.00 9.04  ? 328  MET A C   1 
ATOM   2578 O  O   . MET A 1 328 ? 39.727 22.889 23.036  1.00 9.80  ? 328  MET A O   1 
ATOM   2579 C  CB  . MET A 1 328 ? 38.871 22.288 19.868  1.00 7.16  ? 328  MET A CB  1 
ATOM   2580 C  CG  . MET A 1 328 ? 38.848 23.807 19.991  1.00 8.17  ? 328  MET A CG  1 
ATOM   2581 S  SD  . MET A 1 328 ? 37.810 24.574 18.743  1.00 10.05 ? 328  MET A SD  1 
ATOM   2582 C  CE  . MET A 1 328 ? 36.188 24.216 19.395  1.00 5.11  ? 328  MET A CE  1 
ATOM   2583 N  N   . LEU A 1 329 ? 37.830 21.729 22.654  1.00 6.99  ? 329  LEU A N   1 
ATOM   2584 C  CA  . LEU A 1 329 ? 37.155 22.148 23.878  1.00 6.11  ? 329  LEU A CA  1 
ATOM   2585 C  C   . LEU A 1 329 ? 37.841 21.637 25.149  1.00 9.60  ? 329  LEU A C   1 
ATOM   2586 O  O   . LEU A 1 329 ? 37.623 22.176 26.240  1.00 9.95  ? 329  LEU A O   1 
ATOM   2587 C  CB  . LEU A 1 329 ? 35.698 21.680 23.841  1.00 6.92  ? 329  LEU A CB  1 
ATOM   2588 C  CG  . LEU A 1 329 ? 34.571 22.640 23.435  1.00 10.03 ? 329  LEU A CG  1 
ATOM   2589 C  CD1 . LEU A 1 329 ? 35.086 23.912 22.798  1.00 8.36  ? 329  LEU A CD1 1 
ATOM   2590 C  CD2 . LEU A 1 329 ? 33.602 21.928 22.525  1.00 7.86  ? 329  LEU A CD2 1 
ATOM   2591 N  N   . ALA A 1 330 ? 38.657 20.595 25.012  1.00 10.11 ? 330  ALA A N   1 
ATOM   2592 C  CA  . ALA A 1 330 ? 39.370 20.028 26.153  1.00 8.81  ? 330  ALA A CA  1 
ATOM   2593 C  C   . ALA A 1 330 ? 40.757 20.639 26.354  1.00 9.45  ? 330  ALA A C   1 
ATOM   2594 O  O   . ALA A 1 330 ? 41.236 20.724 27.482  1.00 9.43  ? 330  ALA A O   1 
ATOM   2595 C  CB  . ALA A 1 330 ? 39.493 18.524 25.996  1.00 8.65  ? 330  ALA A CB  1 
ATOM   2596 N  N   . HIS A 1 331 ? 41.414 21.011 25.257  1.00 10.14 ? 331  HIS A N   1 
ATOM   2597 C  CA  . HIS A 1 331 ? 42.757 21.593 25.303  1.00 12.45 ? 331  HIS A CA  1 
ATOM   2598 C  C   . HIS A 1 331 ? 42.719 23.062 25.758  1.00 14.36 ? 331  HIS A C   1 
ATOM   2599 O  O   . HIS A 1 331 ? 41.919 23.853 25.261  1.00 15.86 ? 331  HIS A O   1 
ATOM   2600 C  CB  . HIS A 1 331 ? 43.428 21.470 23.930  1.00 12.42 ? 331  HIS A CB  1 
ATOM   2601 C  CG  . HIS A 1 331 ? 44.923 21.515 23.986  1.00 11.79 ? 331  HIS A CG  1 
ATOM   2602 N  ND1 . HIS A 1 331 ? 45.637 22.691 23.922  1.00 10.48 ? 331  HIS A ND1 1 
ATOM   2603 C  CD2 . HIS A 1 331 ? 45.837 20.529 24.147  1.00 12.58 ? 331  HIS A CD2 1 
ATOM   2604 C  CE1 . HIS A 1 331 ? 46.926 22.429 24.053  1.00 10.69 ? 331  HIS A CE1 1 
ATOM   2605 N  NE2 . HIS A 1 331 ? 47.073 21.126 24.191  1.00 10.50 ? 331  HIS A NE2 1 
ATOM   2606 N  N   . PRO A 1 332 ? 43.628 23.454 26.668  1.00 13.22 ? 332  PRO A N   1 
ATOM   2607 C  CA  . PRO A 1 332 ? 43.707 24.822 27.201  1.00 13.19 ? 332  PRO A CA  1 
ATOM   2608 C  C   . PRO A 1 332 ? 44.079 25.955 26.240  1.00 13.14 ? 332  PRO A C   1 
ATOM   2609 O  O   . PRO A 1 332 ? 43.968 27.126 26.596  1.00 15.89 ? 332  PRO A O   1 
ATOM   2610 C  CB  . PRO A 1 332 ? 44.746 24.689 28.321  1.00 12.26 ? 332  PRO A CB  1 
ATOM   2611 C  CG  . PRO A 1 332 ? 45.642 23.596 27.832  1.00 11.64 ? 332  PRO A CG  1 
ATOM   2612 C  CD  . PRO A 1 332 ? 44.648 22.590 27.296  1.00 14.12 ? 332  PRO A CD  1 
ATOM   2613 N  N   . TYR A 1 333 ? 44.474 25.625 25.019  1.00 12.38 ? 333  TYR A N   1 
ATOM   2614 C  CA  . TYR A 1 333 ? 44.884 26.652 24.070  1.00 12.91 ? 333  TYR A CA  1 
ATOM   2615 C  C   . TYR A 1 333 ? 43.764 27.508 23.471  1.00 13.71 ? 333  TYR A C   1 
ATOM   2616 O  O   . TYR A 1 333 ? 42.764 26.989 22.976  1.00 12.95 ? 333  TYR A O   1 
ATOM   2617 C  CB  . TYR A 1 333 ? 45.717 26.024 22.947  1.00 12.87 ? 333  TYR A CB  1 
ATOM   2618 C  CG  . TYR A 1 333 ? 46.231 27.018 21.929  1.00 14.22 ? 333  TYR A CG  1 
ATOM   2619 C  CD1 . TYR A 1 333 ? 45.459 27.369 20.828  1.00 11.46 ? 333  TYR A CD1 1 
ATOM   2620 C  CD2 . TYR A 1 333 ? 47.489 27.612 22.073  1.00 15.21 ? 333  TYR A CD2 1 
ATOM   2621 C  CE1 . TYR A 1 333 ? 45.915 28.278 19.901  1.00 14.06 ? 333  TYR A CE1 1 
ATOM   2622 C  CE2 . TYR A 1 333 ? 47.959 28.530 21.138  1.00 13.42 ? 333  TYR A CE2 1 
ATOM   2623 C  CZ  . TYR A 1 333 ? 47.161 28.857 20.057  1.00 12.86 ? 333  TYR A CZ  1 
ATOM   2624 O  OH  . TYR A 1 333 ? 47.585 29.768 19.127  1.00 16.86 ? 333  TYR A OH  1 
ATOM   2625 N  N   . GLY A 1 334 ? 43.974 28.822 23.508  1.00 12.34 ? 334  GLY A N   1 
ATOM   2626 C  CA  . GLY A 1 334 ? 43.048 29.791 22.938  1.00 11.53 ? 334  GLY A CA  1 
ATOM   2627 C  C   . GLY A 1 334 ? 41.641 29.903 23.491  1.00 12.70 ? 334  GLY A C   1 
ATOM   2628 O  O   . GLY A 1 334 ? 41.285 29.219 24.462  1.00 13.54 ? 334  GLY A O   1 
ATOM   2629 N  N   . PHE A 1 335 ? 40.876 30.838 22.921  1.00 9.06  ? 335  PHE A N   1 
ATOM   2630 C  CA  . PHE A 1 335 ? 39.486 31.050 23.302  1.00 7.50  ? 335  PHE A CA  1 
ATOM   2631 C  C   . PHE A 1 335 ? 38.709 30.398 22.176  1.00 8.17  ? 335  PHE A C   1 
ATOM   2632 O  O   . PHE A 1 335 ? 38.858 30.759 21.006  1.00 9.88  ? 335  PHE A O   1 
ATOM   2633 C  CB  . PHE A 1 335 ? 39.123 32.535 23.430  1.00 8.63  ? 335  PHE A CB  1 
ATOM   2634 C  CG  . PHE A 1 335 ? 37.772 32.761 24.058  1.00 7.62  ? 335  PHE A CG  1 
ATOM   2635 C  CD1 . PHE A 1 335 ? 37.603 32.636 25.436  1.00 9.45  ? 335  PHE A CD1 1 
ATOM   2636 C  CD2 . PHE A 1 335 ? 36.655 32.999 23.269  1.00 7.01  ? 335  PHE A CD2 1 
ATOM   2637 C  CE1 . PHE A 1 335 ? 36.340 32.733 26.012  1.00 5.90  ? 335  PHE A CE1 1 
ATOM   2638 C  CE2 . PHE A 1 335 ? 35.392 33.098 23.836  1.00 3.29  ? 335  PHE A CE2 1 
ATOM   2639 C  CZ  . PHE A 1 335 ? 35.232 32.964 25.204  1.00 5.41  ? 335  PHE A CZ  1 
ATOM   2640 N  N   . THR A 1 336 ? 37.899 29.418 22.548  1.00 11.12 ? 336  THR A N   1 
ATOM   2641 C  CA  . THR A 1 336 ? 37.135 28.607 21.613  1.00 10.71 ? 336  THR A CA  1 
ATOM   2642 C  C   . THR A 1 336 ? 35.813 29.112 21.060  1.00 10.17 ? 336  THR A C   1 
ATOM   2643 O  O   . THR A 1 336 ? 34.974 29.615 21.806  1.00 14.06 ? 336  THR A O   1 
ATOM   2644 C  CB  . THR A 1 336 ? 36.884 27.232 22.250  1.00 10.73 ? 336  THR A CB  1 
ATOM   2645 O  OG1 . THR A 1 336 ? 36.263 27.420 23.528  1.00 8.07  ? 336  THR A OG1 1 
ATOM   2646 C  CG2 . THR A 1 336 ? 38.197 26.481 22.441  1.00 6.68  ? 336  THR A CG2 1 
ATOM   2647 N  N   . ARG A 1 337 ? 35.618 28.943 19.753  1.00 9.89  ? 337  ARG A N   1 
ATOM   2648 C  CA  . ARG A 1 337 ? 34.358 29.315 19.109  1.00 11.87 ? 337  ARG A CA  1 
ATOM   2649 C  C   . ARG A 1 337 ? 33.749 28.047 18.497  1.00 13.70 ? 337  ARG A C   1 
ATOM   2650 O  O   . ARG A 1 337 ? 34.433 27.287 17.805  1.00 12.80 ? 337  ARG A O   1 
ATOM   2651 C  CB  . ARG A 1 337 ? 34.546 30.372 18.014  1.00 10.53 ? 337  ARG A CB  1 
ATOM   2652 C  CG  . ARG A 1 337 ? 33.214 30.795 17.361  1.00 6.52  ? 337  ARG A CG  1 
ATOM   2653 C  CD  . ARG A 1 337 ? 33.389 31.827 16.267  1.00 6.87  ? 337  ARG A CD  1 
ATOM   2654 N  NE  . ARG A 1 337 ? 34.288 31.363 15.216  1.00 9.51  ? 337  ARG A NE  1 
ATOM   2655 C  CZ  . ARG A 1 337 ? 34.886 32.160 14.335  1.00 10.62 ? 337  ARG A CZ  1 
ATOM   2656 N  NH1 . ARG A 1 337 ? 34.655 33.465 14.342  1.00 9.69  ? 337  ARG A NH1 1 
ATOM   2657 N  NH2 . ARG A 1 337 ? 35.704 31.647 13.430  1.00 10.17 ? 337  ARG A NH2 1 
ATOM   2658 N  N   . VAL A 1 338 ? 32.479 27.807 18.801  1.00 11.67 ? 338  VAL A N   1 
ATOM   2659 C  CA  . VAL A 1 338 ? 31.746 26.651 18.309  1.00 9.37  ? 338  VAL A CA  1 
ATOM   2660 C  C   . VAL A 1 338 ? 30.863 27.110 17.153  1.00 10.45 ? 338  VAL A C   1 
ATOM   2661 O  O   . VAL A 1 338 ? 30.224 28.158 17.225  1.00 15.62 ? 338  VAL A O   1 
ATOM   2662 C  CB  . VAL A 1 338 ? 30.868 26.041 19.444  1.00 11.61 ? 338  VAL A CB  1 
ATOM   2663 C  CG1 . VAL A 1 338 ? 29.918 24.993 18.900  1.00 11.87 ? 338  VAL A CG1 1 
ATOM   2664 C  CG2 . VAL A 1 338 ? 31.754 25.420 20.505  1.00 11.17 ? 338  VAL A CG2 1 
ATOM   2665 N  N   . MET A 1 339 ? 30.828 26.321 16.090  1.00 8.55  ? 339  MET A N   1 
ATOM   2666 C  CA  . MET A 1 339 ? 30.039 26.644 14.916  1.00 10.58 ? 339  MET A CA  1 
ATOM   2667 C  C   . MET A 1 339 ? 28.627 26.050 14.993  1.00 11.95 ? 339  MET A C   1 
ATOM   2668 O  O   . MET A 1 339 ? 28.421 24.979 15.575  1.00 16.04 ? 339  MET A O   1 
ATOM   2669 C  CB  . MET A 1 339 ? 30.764 26.113 13.680  1.00 6.51  ? 339  MET A CB  1 
ATOM   2670 C  CG  . MET A 1 339 ? 30.108 26.447 12.360  1.00 7.18  ? 339  MET A CG  1 
ATOM   2671 S  SD  . MET A 1 339 ? 30.203 28.182 11.945  1.00 9.04  ? 339  MET A SD  1 
ATOM   2672 C  CE  . MET A 1 339 ? 28.871 28.315 10.767  1.00 7.02  ? 339  MET A CE  1 
ATOM   2673 N  N   . SER A 1 340 ? 27.654 26.771 14.445  1.00 7.76  ? 340  SER A N   1 
ATOM   2674 C  CA  . SER A 1 340 ? 26.271 26.309 14.395  1.00 6.82  ? 340  SER A CA  1 
ATOM   2675 C  C   . SER A 1 340 ? 25.801 26.655 12.976  1.00 9.11  ? 340  SER A C   1 
ATOM   2676 O  O   . SER A 1 340 ? 25.659 27.825 12.624  1.00 8.58  ? 340  SER A O   1 
ATOM   2677 C  CB  . SER A 1 340 ? 25.425 27.000 15.457  1.00 6.04  ? 340  SER A CB  1 
ATOM   2678 O  OG  . SER A 1 340 ? 24.254 26.239 15.719  1.00 5.53  ? 340  SER A OG  1 
ATOM   2679 N  N   . SER A 1 341 ? 25.594 25.628 12.158  1.00 7.78  ? 341  SER A N   1 
ATOM   2680 C  CA  . SER A 1 341 ? 25.232 25.818 10.759  1.00 9.47  ? 341  SER A CA  1 
ATOM   2681 C  C   . SER A 1 341 ? 23.827 25.416 10.347  1.00 6.15  ? 341  SER A C   1 
ATOM   2682 O  O   . SER A 1 341 ? 22.977 25.108 11.178  1.00 9.07  ? 341  SER A O   1 
ATOM   2683 C  CB  . SER A 1 341 ? 26.214 25.026 9.892   1.00 10.80 ? 341  SER A CB  1 
ATOM   2684 O  OG  . SER A 1 341 ? 27.398 24.711 10.606  1.00 11.65 ? 341  SER A OG  1 
ATOM   2685 N  N   . TYR A 1 342 ? 23.612 25.448 9.036   1.00 7.74  ? 342  TYR A N   1 
ATOM   2686 C  CA  . TYR A 1 342 ? 22.371 25.042 8.409   1.00 9.24  ? 342  TYR A CA  1 
ATOM   2687 C  C   . TYR A 1 342 ? 22.776 24.122 7.261   1.00 8.48  ? 342  TYR A C   1 
ATOM   2688 O  O   . TYR A 1 342 ? 23.872 24.235 6.709   1.00 12.85 ? 342  TYR A O   1 
ATOM   2689 C  CB  . TYR A 1 342 ? 21.528 26.238 7.915   1.00 8.49  ? 342  TYR A CB  1 
ATOM   2690 C  CG  . TYR A 1 342 ? 22.178 27.156 6.905   1.00 10.59 ? 342  TYR A CG  1 
ATOM   2691 C  CD1 . TYR A 1 342 ? 22.270 26.804 5.555   1.00 10.00 ? 342  TYR A CD1 1 
ATOM   2692 C  CD2 . TYR A 1 342 ? 22.705 28.384 7.300   1.00 10.48 ? 342  TYR A CD2 1 
ATOM   2693 C  CE1 . TYR A 1 342 ? 22.881 27.652 4.627   1.00 10.30 ? 342  TYR A CE1 1 
ATOM   2694 C  CE2 . TYR A 1 342 ? 23.309 29.236 6.384   1.00 8.98  ? 342  TYR A CE2 1 
ATOM   2695 C  CZ  . TYR A 1 342 ? 23.398 28.867 5.052   1.00 11.87 ? 342  TYR A CZ  1 
ATOM   2696 O  OH  . TYR A 1 342 ? 24.019 29.714 4.158   1.00 12.45 ? 342  TYR A OH  1 
ATOM   2697 N  N   . ARG A 1 343 ? 21.903 23.179 6.951   1.00 12.33 ? 343  ARG A N   1 
ATOM   2698 C  CA  . ARG A 1 343 ? 22.131 22.202 5.905   1.00 11.48 ? 343  ARG A CA  1 
ATOM   2699 C  C   . ARG A 1 343 ? 21.786 22.796 4.546   1.00 12.60 ? 343  ARG A C   1 
ATOM   2700 O  O   . ARG A 1 343 ? 20.817 23.551 4.425   1.00 16.87 ? 343  ARG A O   1 
ATOM   2701 C  CB  . ARG A 1 343 ? 21.240 20.998 6.188   1.00 17.46 ? 343  ARG A CB  1 
ATOM   2702 C  CG  . ARG A 1 343 ? 21.803 19.671 5.759   1.00 26.82 ? 343  ARG A CG  1 
ATOM   2703 C  CD  . ARG A 1 343 ? 20.956 18.527 6.314   1.00 27.51 ? 343  ARG A CD  1 
ATOM   2704 N  NE  . ARG A 1 343 ? 21.069 18.383 7.769   1.00 31.18 ? 343  ARG A NE  1 
ATOM   2705 C  CZ  . ARG A 1 343 ? 20.088 18.646 8.631   1.00 33.23 ? 343  ARG A CZ  1 
ATOM   2706 N  NH1 . ARG A 1 343 ? 18.911 19.084 8.197   1.00 33.27 ? 343  ARG A NH1 1 
ATOM   2707 N  NH2 . ARG A 1 343 ? 20.282 18.480 9.934   1.00 31.13 ? 343  ARG A NH2 1 
ATOM   2708 N  N   . TRP A 1 344 ? 22.599 22.496 3.539   1.00 9.00  ? 344  TRP A N   1 
ATOM   2709 C  CA  . TRP A 1 344 ? 22.350 22.978 2.187   1.00 6.31  ? 344  TRP A CA  1 
ATOM   2710 C  C   . TRP A 1 344 ? 22.617 21.851 1.204   1.00 9.25  ? 344  TRP A C   1 
ATOM   2711 O  O   . TRP A 1 344 ? 23.300 20.880 1.530   1.00 10.21 ? 344  TRP A O   1 
ATOM   2712 C  CB  . TRP A 1 344 ? 23.203 24.206 1.853   1.00 9.74  ? 344  TRP A CB  1 
ATOM   2713 C  CG  . TRP A 1 344 ? 24.650 23.946 1.545   1.00 9.56  ? 344  TRP A CG  1 
ATOM   2714 C  CD1 . TRP A 1 344 ? 25.209 23.773 0.305   1.00 9.82  ? 344  TRP A CD1 1 
ATOM   2715 C  CD2 . TRP A 1 344 ? 25.736 23.881 2.486   1.00 8.52  ? 344  TRP A CD2 1 
ATOM   2716 N  NE1 . TRP A 1 344 ? 26.574 23.611 0.420   1.00 9.75  ? 344  TRP A NE1 1 
ATOM   2717 C  CE2 . TRP A 1 344 ? 26.923 23.671 1.744   1.00 8.29  ? 344  TRP A CE2 1 
ATOM   2718 C  CE3 . TRP A 1 344 ? 25.824 23.982 3.880   1.00 10.24 ? 344  TRP A CE3 1 
ATOM   2719 C  CZ2 . TRP A 1 344 ? 28.177 23.559 2.353   1.00 7.58  ? 344  TRP A CZ2 1 
ATOM   2720 C  CZ3 . TRP A 1 344 ? 27.076 23.871 4.483   1.00 8.16  ? 344  TRP A CZ3 1 
ATOM   2721 C  CH2 . TRP A 1 344 ? 28.232 23.660 3.718   1.00 5.65  ? 344  TRP A CH2 1 
ATOM   2722 N  N   . ALA A 1 345 ? 22.051 21.962 0.011   1.00 10.23 ? 345  ALA A N   1 
ATOM   2723 C  CA  . ALA A 1 345 ? 22.223 20.935 -1.002  1.00 13.19 ? 345  ALA A CA  1 
ATOM   2724 C  C   . ALA A 1 345 ? 23.565 21.031 -1.710  1.00 14.76 ? 345  ALA A C   1 
ATOM   2725 O  O   . ALA A 1 345 ? 23.691 21.747 -2.697  1.00 16.51 ? 345  ALA A O   1 
ATOM   2726 C  CB  . ALA A 1 345 ? 21.091 21.012 -2.012  1.00 10.93 ? 345  ALA A CB  1 
ATOM   2727 N  N   . ARG A 1 346 ? 24.575 20.340 -1.194  1.00 14.72 ? 346  ARG A N   1 
ATOM   2728 C  CA  . ARG A 1 346 ? 25.895 20.358 -1.822  1.00 16.60 ? 346  ARG A CA  1 
ATOM   2729 C  C   . ARG A 1 346 ? 25.824 19.642 -3.169  1.00 15.68 ? 346  ARG A C   1 
ATOM   2730 O  O   . ARG A 1 346 ? 25.040 18.709 -3.340  1.00 24.02 ? 346  ARG A O   1 
ATOM   2731 C  CB  . ARG A 1 346 ? 26.937 19.669 -0.941  1.00 15.99 ? 346  ARG A CB  1 
ATOM   2732 C  CG  . ARG A 1 346 ? 27.165 20.328 0.394   1.00 22.39 ? 346  ARG A CG  1 
ATOM   2733 C  CD  . ARG A 1 346 ? 28.481 19.887 1.006   1.00 24.32 ? 346  ARG A CD  1 
ATOM   2734 N  NE  . ARG A 1 346 ? 28.491 18.469 1.358   1.00 28.80 ? 346  ARG A NE  1 
ATOM   2735 C  CZ  . ARG A 1 346 ? 29.511 17.850 1.948   1.00 30.90 ? 346  ARG A CZ  1 
ATOM   2736 N  NH1 . ARG A 1 346 ? 30.609 18.522 2.273   1.00 27.16 ? 346  ARG A NH1 1 
ATOM   2737 N  NH2 . ARG A 1 346 ? 29.424 16.556 2.231   1.00 29.66 ? 346  ARG A NH2 1 
ATOM   2738 N  N   . ASN A 1 347 ? 26.628 20.088 -4.126  0.50 10.30 ? 347  ASN A N   1 
ATOM   2739 C  CA  . ASN A 1 347 ? 26.660 19.485 -5.448  0.50 7.34  ? 347  ASN A CA  1 
ATOM   2740 C  C   . ASN A 1 347 ? 28.050 19.703 -6.001  0.50 5.81  ? 347  ASN A C   1 
ATOM   2741 O  O   . ASN A 1 347 ? 28.367 20.776 -6.503  0.50 6.56  ? 347  ASN A O   1 
ATOM   2742 C  CB  . ASN A 1 347 ? 25.618 20.126 -6.365  0.50 10.93 ? 347  ASN A CB  1 
ATOM   2743 C  CG  . ASN A 1 347 ? 25.589 19.490 -7.745  0.50 14.11 ? 347  ASN A CG  1 
ATOM   2744 O  OD1 . ASN A 1 347 ? 25.576 20.183 -8.759  0.50 14.85 ? 347  ASN A OD1 1 
ATOM   2745 N  ND2 . ASN A 1 347 ? 25.576 18.163 -7.788  0.50 14.90 ? 347  ASN A ND2 1 
ATOM   2746 N  N   . PHE A 1 348 ? 28.892 18.690 -5.853  0.50 6.38  ? 348  PHE A N   1 
ATOM   2747 C  CA  . PHE A 1 348 ? 30.274 18.754 -6.298  0.50 8.25  ? 348  PHE A CA  1 
ATOM   2748 C  C   . PHE A 1 348 ? 30.503 18.394 -7.754  0.50 11.62 ? 348  PHE A C   1 
ATOM   2749 O  O   . PHE A 1 348 ? 30.304 17.252 -8.149  0.50 15.19 ? 348  PHE A O   1 
ATOM   2750 C  CB  . PHE A 1 348 ? 31.144 17.839 -5.438  0.50 6.26  ? 348  PHE A CB  1 
ATOM   2751 C  CG  . PHE A 1 348 ? 31.224 18.242 -3.997  0.50 4.98  ? 348  PHE A CG  1 
ATOM   2752 C  CD1 . PHE A 1 348 ? 30.310 17.752 -3.073  0.50 5.66  ? 348  PHE A CD1 1 
ATOM   2753 C  CD2 . PHE A 1 348 ? 32.230 19.083 -3.558  0.50 4.97  ? 348  PHE A CD2 1 
ATOM   2754 C  CE1 . PHE A 1 348 ? 30.405 18.096 -1.733  0.50 7.28  ? 348  PHE A CE1 1 
ATOM   2755 C  CE2 . PHE A 1 348 ? 32.334 19.433 -2.219  0.50 6.49  ? 348  PHE A CE2 1 
ATOM   2756 C  CZ  . PHE A 1 348 ? 31.422 18.940 -1.306  0.50 9.18  ? 348  PHE A CZ  1 
ATOM   2757 N  N   . VAL A 1 349 ? 30.896 19.377 -8.554  0.50 17.45 ? 349  VAL A N   1 
ATOM   2758 C  CA  . VAL A 1 349 ? 31.220 19.127 -9.949  0.50 20.86 ? 349  VAL A CA  1 
ATOM   2759 C  C   . VAL A 1 349 ? 32.694 19.516 -10.030 0.50 27.47 ? 349  VAL A C   1 
ATOM   2760 O  O   . VAL A 1 349 ? 33.075 20.639 -9.701  0.50 26.70 ? 349  VAL A O   1 
ATOM   2761 C  CB  . VAL A 1 349 ? 30.346 19.940 -10.954 0.50 19.56 ? 349  VAL A CB  1 
ATOM   2762 C  CG1 . VAL A 1 349 ? 28.870 19.761 -10.640 0.50 18.51 ? 349  VAL A CG1 1 
ATOM   2763 C  CG2 . VAL A 1 349 ? 30.726 21.403 -10.974 0.50 21.83 ? 349  VAL A CG2 1 
ATOM   2764 N  N   . ASN A 1 350 ? 33.531 18.528 -10.316 1.00 38.11 ? 350  ASN A N   1 
ATOM   2765 C  CA  . ASN A 1 350 ? 34.975 18.727 -10.411 1.00 46.17 ? 350  ASN A CA  1 
ATOM   2766 C  C   . ASN A 1 350 ? 35.638 19.119 -9.090  1.00 46.46 ? 350  ASN A C   1 
ATOM   2767 O  O   . ASN A 1 350 ? 36.572 19.926 -9.068  1.00 48.69 ? 350  ASN A O   1 
ATOM   2768 C  CB  . ASN A 1 350 ? 35.314 19.745 -11.505 1.00 53.58 ? 350  ASN A CB  1 
ATOM   2769 C  CG  . ASN A 1 350 ? 35.211 19.153 -12.892 1.00 59.41 ? 350  ASN A CG  1 
ATOM   2770 O  OD1 . ASN A 1 350 ? 34.181 19.274 -13.557 1.00 64.03 ? 350  ASN A OD1 1 
ATOM   2771 N  ND2 . ASN A 1 350 ? 36.270 18.477 -13.329 1.00 61.59 ? 350  ASN A ND2 1 
ATOM   2772 N  N   . GLY A 1 351 ? 35.173 18.515 -8.000  0.50 43.79 ? 351  GLY A N   1 
ATOM   2773 C  CA  . GLY A 1 351 ? 35.733 18.799 -6.688  0.50 41.74 ? 351  GLY A CA  1 
ATOM   2774 C  C   . GLY A 1 351 ? 35.420 20.187 -6.166  0.50 40.07 ? 351  GLY A C   1 
ATOM   2775 O  O   . GLY A 1 351 ? 36.087 20.685 -5.257  0.50 37.19 ? 351  GLY A O   1 
ATOM   2776 N  N   . GLU A 1 352 ? 34.398 20.812 -6.739  1.00 40.80 ? 352  GLU A N   1 
ATOM   2777 C  CA  . GLU A 1 352 ? 33.984 22.144 -6.335  1.00 41.05 ? 352  GLU A CA  1 
ATOM   2778 C  C   . GLU A 1 352 ? 32.474 22.089 -6.117  1.00 34.47 ? 352  GLU A C   1 
ATOM   2779 O  O   . GLU A 1 352 ? 31.741 21.523 -6.927  1.00 34.11 ? 352  GLU A O   1 
ATOM   2780 C  CB  . GLU A 1 352 ? 34.342 23.156 -7.433  1.00 50.80 ? 352  GLU A CB  1 
ATOM   2781 C  CG  . GLU A 1 352 ? 34.492 24.613 -6.971  1.00 62.02 ? 352  GLU A CG  1 
ATOM   2782 C  CD  . GLU A 1 352 ? 33.161 25.341 -6.788  1.00 69.35 ? 352  GLU A CD  1 
ATOM   2783 O  OE1 . GLU A 1 352 ? 32.407 25.477 -7.779  1.00 73.59 ? 352  GLU A OE1 1 
ATOM   2784 O  OE2 . GLU A 1 352 ? 32.876 25.797 -5.655  1.00 71.27 ? 352  GLU A OE2 1 
ATOM   2785 N  N   . ASP A 1 353 ? 32.025 22.602 -4.981  1.00 27.97 ? 353  ASP A N   1 
ATOM   2786 C  CA  . ASP A 1 353 ? 30.607 22.619 -4.658  1.00 24.40 ? 353  ASP A CA  1 
ATOM   2787 C  C   . ASP A 1 353 ? 29.998 23.830 -5.351  1.00 22.77 ? 353  ASP A C   1 
ATOM   2788 O  O   . ASP A 1 353 ? 30.233 24.965 -4.949  1.00 28.40 ? 353  ASP A O   1 
ATOM   2789 C  CB  . ASP A 1 353 ? 30.426 22.717 -3.137  1.00 22.17 ? 353  ASP A CB  1 
ATOM   2790 C  CG  . ASP A 1 353 ? 28.969 22.739 -2.706  1.00 20.70 ? 353  ASP A CG  1 
ATOM   2791 O  OD1 . ASP A 1 353 ? 28.073 22.508 -3.543  1.00 20.19 ? 353  ASP A OD1 1 
ATOM   2792 O  OD2 . ASP A 1 353 ? 28.718 22.996 -1.507  1.00 18.97 ? 353  ASP A OD2 1 
ATOM   2793 N  N   . VAL A 1 354 ? 29.204 23.592 -6.384  1.00 17.80 ? 354  VAL A N   1 
ATOM   2794 C  CA  . VAL A 1 354 ? 28.581 24.688 -7.115  1.00 18.88 ? 354  VAL A CA  1 
ATOM   2795 C  C   . VAL A 1 354 ? 27.418 25.335 -6.375  1.00 19.63 ? 354  VAL A C   1 
ATOM   2796 O  O   . VAL A 1 354 ? 26.843 26.325 -6.839  1.00 23.57 ? 354  VAL A O   1 
ATOM   2797 C  CB  . VAL A 1 354 ? 28.123 24.246 -8.514  1.00 19.10 ? 354  VAL A CB  1 
ATOM   2798 C  CG1 . VAL A 1 354 ? 29.324 23.880 -9.345  1.00 18.52 ? 354  VAL A CG1 1 
ATOM   2799 C  CG2 . VAL A 1 354 ? 27.165 23.073 -8.415  1.00 20.24 ? 354  VAL A CG2 1 
ATOM   2800 N  N   . ASN A 1 355 ? 27.057 24.763 -5.234  1.00 18.79 ? 355  ASN A N   1 
ATOM   2801 C  CA  . ASN A 1 355 ? 25.971 25.302 -4.430  1.00 14.83 ? 355  ASN A CA  1 
ATOM   2802 C  C   . ASN A 1 355 ? 26.478 25.929 -3.142  1.00 11.19 ? 355  ASN A C   1 
ATOM   2803 O  O   . ASN A 1 355 ? 25.712 26.137 -2.211  1.00 12.23 ? 355  ASN A O   1 
ATOM   2804 C  CB  . ASN A 1 355 ? 24.946 24.215 -4.109  1.00 17.12 ? 355  ASN A CB  1 
ATOM   2805 C  CG  . ASN A 1 355 ? 24.100 23.840 -5.304  1.00 18.00 ? 355  ASN A CG  1 
ATOM   2806 O  OD1 . ASN A 1 355 ? 24.282 24.368 -6.403  1.00 23.01 ? 355  ASN A OD1 1 
ATOM   2807 N  ND2 . ASN A 1 355 ? 23.149 22.936 -5.096  1.00 17.09 ? 355  ASN A ND2 1 
ATOM   2808 N  N   . ASP A 1 356 ? 27.762 26.267 -3.100  1.00 12.89 ? 356  ASP A N   1 
ATOM   2809 C  CA  . ASP A 1 356 ? 28.350 26.873 -1.901  1.00 15.86 ? 356  ASP A CA  1 
ATOM   2810 C  C   . ASP A 1 356 ? 27.771 28.247 -1.576  1.00 12.55 ? 356  ASP A C   1 
ATOM   2811 O  O   . ASP A 1 356 ? 28.086 28.824 -0.542  1.00 16.40 ? 356  ASP A O   1 
ATOM   2812 C  CB  . ASP A 1 356 ? 29.868 26.990 -2.053  1.00 18.81 ? 356  ASP A CB  1 
ATOM   2813 C  CG  . ASP A 1 356 ? 30.280 27.899 -3.198  1.00 20.85 ? 356  ASP A CG  1 
ATOM   2814 O  OD1 . ASP A 1 356 ? 29.428 28.298 -4.014  1.00 26.52 ? 356  ASP A OD1 1 
ATOM   2815 O  OD2 . ASP A 1 356 ? 31.476 28.215 -3.289  1.00 25.12 ? 356  ASP A OD2 1 
ATOM   2816 N  N   . TRP A 1 357 ? 26.970 28.783 -2.493  1.00 10.52 ? 357  TRP A N   1 
ATOM   2817 C  CA  . TRP A 1 357 ? 26.355 30.098 -2.331  1.00 11.34 ? 357  TRP A CA  1 
ATOM   2818 C  C   . TRP A 1 357 ? 25.037 30.095 -1.562  1.00 11.96 ? 357  TRP A C   1 
ATOM   2819 O  O   . TRP A 1 357 ? 24.613 31.132 -1.062  1.00 14.66 ? 357  TRP A O   1 
ATOM   2820 C  CB  . TRP A 1 357 ? 26.097 30.719 -3.705  1.00 11.47 ? 357  TRP A CB  1 
ATOM   2821 C  CG  . TRP A 1 357 ? 25.194 29.874 -4.575  1.00 13.37 ? 357  TRP A CG  1 
ATOM   2822 C  CD1 . TRP A 1 357 ? 25.584 28.942 -5.492  1.00 12.88 ? 357  TRP A CD1 1 
ATOM   2823 C  CD2 . TRP A 1 357 ? 23.754 29.855 -4.578  1.00 13.88 ? 357  TRP A CD2 1 
ATOM   2824 N  NE1 . TRP A 1 357 ? 24.485 28.338 -6.057  1.00 13.69 ? 357  TRP A NE1 1 
ATOM   2825 C  CE2 . TRP A 1 357 ? 23.349 28.880 -5.515  1.00 11.94 ? 357  TRP A CE2 1 
ATOM   2826 C  CE3 . TRP A 1 357 ? 22.769 30.569 -3.880  1.00 12.64 ? 357  TRP A CE3 1 
ATOM   2827 C  CZ2 . TRP A 1 357 ? 22.007 28.598 -5.771  1.00 12.73 ? 357  TRP A CZ2 1 
ATOM   2828 C  CZ3 . TRP A 1 357 ? 21.431 30.287 -4.135  1.00 9.91  ? 357  TRP A CZ3 1 
ATOM   2829 C  CH2 . TRP A 1 357 ? 21.064 29.310 -5.072  1.00 9.06  ? 357  TRP A CH2 1 
ATOM   2830 N  N   . ILE A 1 358 ? 24.382 28.939 -1.493  1.00 12.42 ? 358  ILE A N   1 
ATOM   2831 C  CA  . ILE A 1 358 ? 23.083 28.823 -0.846  1.00 12.14 ? 358  ILE A CA  1 
ATOM   2832 C  C   . ILE A 1 358 ? 22.963 29.501 0.509   1.00 12.88 ? 358  ILE A C   1 
ATOM   2833 O  O   . ILE A 1 358 ? 23.767 29.265 1.412   1.00 16.33 ? 358  ILE A O   1 
ATOM   2834 C  CB  . ILE A 1 358 ? 22.607 27.353 -0.778  1.00 11.61 ? 358  ILE A CB  1 
ATOM   2835 C  CG1 . ILE A 1 358 ? 22.419 26.816 -2.196  1.00 10.46 ? 358  ILE A CG1 1 
ATOM   2836 C  CG2 . ILE A 1 358 ? 21.288 27.259 -0.032  1.00 9.65  ? 358  ILE A CG2 1 
ATOM   2837 C  CD1 . ILE A 1 358 ? 22.002 25.366 -2.264  1.00 15.41 ? 358  ILE A CD1 1 
ATOM   2838 N  N   . GLY A 1 359 ? 21.965 30.372 0.619   1.00 11.03 ? 359  GLY A N   1 
ATOM   2839 C  CA  . GLY A 1 359 ? 21.726 31.101 1.845   1.00 9.89  ? 359  GLY A CA  1 
ATOM   2840 C  C   . GLY A 1 359 ? 20.994 30.253 2.860   1.00 12.27 ? 359  GLY A C   1 
ATOM   2841 O  O   . GLY A 1 359 ? 20.679 29.091 2.586   1.00 13.98 ? 359  GLY A O   1 
ATOM   2842 N  N   . PRO A 1 360 ? 20.686 30.816 4.040   1.00 10.53 ? 360  PRO A N   1 
ATOM   2843 C  CA  . PRO A 1 360 ? 19.983 30.112 5.114   1.00 10.00 ? 360  PRO A CA  1 
ATOM   2844 C  C   . PRO A 1 360 ? 18.607 29.600 4.705   1.00 13.00 ? 360  PRO A C   1 
ATOM   2845 O  O   . PRO A 1 360 ? 18.020 30.078 3.724   1.00 14.30 ? 360  PRO A O   1 
ATOM   2846 C  CB  . PRO A 1 360 ? 19.885 31.178 6.210   1.00 8.28  ? 360  PRO A CB  1 
ATOM   2847 C  CG  . PRO A 1 360 ? 19.822 32.446 5.433   1.00 10.78 ? 360  PRO A CG  1 
ATOM   2848 C  CD  . PRO A 1 360 ? 20.887 32.230 4.393   1.00 9.49  ? 360  PRO A CD  1 
ATOM   2849 N  N   . PRO A 1 361 ? 18.086 28.602 5.442   1.00 11.78 ? 361  PRO A N   1 
ATOM   2850 C  CA  . PRO A 1 361 ? 16.775 28.001 5.192   1.00 12.83 ? 361  PRO A CA  1 
ATOM   2851 C  C   . PRO A 1 361 ? 15.793 29.148 5.023   1.00 17.27 ? 361  PRO A C   1 
ATOM   2852 O  O   . PRO A 1 361 ? 15.698 30.024 5.894   1.00 18.40 ? 361  PRO A O   1 
ATOM   2853 C  CB  . PRO A 1 361 ? 16.513 27.242 6.487   1.00 13.42 ? 361  PRO A CB  1 
ATOM   2854 C  CG  . PRO A 1 361 ? 17.877 26.794 6.883   1.00 13.29 ? 361  PRO A CG  1 
ATOM   2855 C  CD  . PRO A 1 361 ? 18.691 28.035 6.660   1.00 12.53 ? 361  PRO A CD  1 
ATOM   2856 N  N   . ASN A 1 362 ? 15.054 29.147 3.922   1.00 17.68 ? 362  ASN A N   1 
ATOM   2857 C  CA  . ASN A 1 362 ? 14.143 30.247 3.665   1.00 20.21 ? 362  ASN A CA  1 
ATOM   2858 C  C   . ASN A 1 362 ? 12.907 29.868 2.884   1.00 21.27 ? 362  ASN A C   1 
ATOM   2859 O  O   . ASN A 1 362 ? 12.852 28.822 2.231   1.00 21.30 ? 362  ASN A O   1 
ATOM   2860 C  CB  . ASN A 1 362 ? 14.882 31.339 2.886   1.00 19.11 ? 362  ASN A CB  1 
ATOM   2861 C  CG  . ASN A 1 362 ? 15.160 30.941 1.443   1.00 20.63 ? 362  ASN A CG  1 
ATOM   2862 O  OD1 . ASN A 1 362 ? 14.383 31.260 0.545   1.00 25.50 ? 362  ASN A OD1 1 
ATOM   2863 N  ND2 . ASN A 1 362 ? 16.261 30.237 1.216   1.00 18.74 ? 362  ASN A ND2 1 
ATOM   2864 N  N   . ASN A 1 363 ? 11.929 30.765 2.935   1.00 24.73 ? 363  ASN A N   1 
ATOM   2865 C  CA  . ASN A 1 363 ? 10.672 30.617 2.220   1.00 27.56 ? 363  ASN A CA  1 
ATOM   2866 C  C   . ASN A 1 363 ? 10.597 31.793 1.270   1.00 26.37 ? 363  ASN A C   1 
ATOM   2867 O  O   . ASN A 1 363 ? 10.149 32.872 1.645   1.00 26.32 ? 363  ASN A O   1 
ATOM   2868 C  CB  . ASN A 1 363 ? 9.485  30.665 3.183   1.00 31.12 ? 363  ASN A CB  1 
ATOM   2869 C  CG  . ASN A 1 363 ? 9.274  29.361 3.910   1.00 37.84 ? 363  ASN A CG  1 
ATOM   2870 O  OD1 . ASN A 1 363 ? 9.232  29.326 5.142   1.00 41.48 ? 363  ASN A OD1 1 
ATOM   2871 N  ND2 . ASN A 1 363 ? 9.133  28.271 3.154   1.00 39.34 ? 363  ASN A ND2 1 
ATOM   2872 N  N   . ASN A 1 364 ? 11.091 31.606 0.054   1.00 29.29 ? 364  ASN A N   1 
ATOM   2873 C  CA  . ASN A 1 364 ? 11.077 32.667 -0.949  1.00 32.60 ? 364  ASN A CA  1 
ATOM   2874 C  C   . ASN A 1 364 ? 11.811 33.905 -0.441  1.00 31.44 ? 364  ASN A C   1 
ATOM   2875 O  O   . ASN A 1 364 ? 11.284 35.023 -0.481  1.00 32.68 ? 364  ASN A O   1 
ATOM   2876 C  CB  . ASN A 1 364 ? 9.633  33.028 -1.338  1.00 34.69 ? 364  ASN A CB  1 
ATOM   2877 C  CG  . ASN A 1 364 ? 8.832  31.822 -1.796  1.00 35.74 ? 364  ASN A CG  1 
ATOM   2878 O  OD1 . ASN A 1 364 ? 7.911  31.375 -1.108  1.00 35.03 ? 364  ASN A OD1 1 
ATOM   2879 N  ND2 . ASN A 1 364 ? 9.182  31.287 -2.958  1.00 36.07 ? 364  ASN A ND2 1 
ATOM   2880 N  N   . GLY A 1 365 ? 13.019 33.693 0.072   1.00 29.04 ? 365  GLY A N   1 
ATOM   2881 C  CA  . GLY A 1 365 ? 13.819 34.799 0.566   1.00 24.97 ? 365  GLY A CA  1 
ATOM   2882 C  C   . GLY A 1 365 ? 13.761 35.093 2.048   1.00 20.96 ? 365  GLY A C   1 
ATOM   2883 O  O   . GLY A 1 365 ? 14.728 35.618 2.590   1.00 23.14 ? 365  GLY A O   1 
ATOM   2884 N  N   . VAL A 1 366 ? 12.641 34.798 2.705   1.00 17.42 ? 366  VAL A N   1 
ATOM   2885 C  CA  . VAL A 1 366 ? 12.523 35.055 4.140   1.00 20.15 ? 366  VAL A CA  1 
ATOM   2886 C  C   . VAL A 1 366 ? 12.976 33.857 4.981   1.00 22.28 ? 366  VAL A C   1 
ATOM   2887 O  O   . VAL A 1 366 ? 12.501 32.730 4.802   1.00 22.49 ? 366  VAL A O   1 
ATOM   2888 C  CB  . VAL A 1 366 ? 11.102 35.561 4.537   1.00 20.86 ? 366  VAL A CB  1 
ATOM   2889 C  CG1 . VAL A 1 366 ? 10.044 34.953 3.660   1.00 22.81 ? 366  VAL A CG1 1 
ATOM   2890 C  CG2 . VAL A 1 366 ? 10.807 35.254 5.992   1.00 21.52 ? 366  VAL A CG2 1 
ATOM   2891 N  N   . ILE A 1 367 ? 13.912 34.118 5.888   1.00 18.39 ? 367  ILE A N   1 
ATOM   2892 C  CA  . ILE A 1 367 ? 14.497 33.095 6.745   1.00 15.79 ? 367  ILE A CA  1 
ATOM   2893 C  C   . ILE A 1 367 ? 13.508 32.349 7.643   1.00 15.61 ? 367  ILE A C   1 
ATOM   2894 O  O   . ILE A 1 367 ? 12.711 32.957 8.362   1.00 20.60 ? 367  ILE A O   1 
ATOM   2895 C  CB  . ILE A 1 367 ? 15.649 33.690 7.590   1.00 14.18 ? 367  ILE A CB  1 
ATOM   2896 C  CG1 . ILE A 1 367 ? 16.705 34.308 6.661   1.00 15.06 ? 367  ILE A CG1 1 
ATOM   2897 C  CG2 . ILE A 1 367 ? 16.291 32.612 8.457   1.00 13.19 ? 367  ILE A CG2 1 
ATOM   2898 C  CD1 . ILE A 1 367 ? 17.881 34.965 7.379   1.00 10.74 ? 367  ILE A CD1 1 
ATOM   2899 N  N   . LYS A 1 368 ? 13.573 31.025 7.589   1.00 13.92 ? 368  LYS A N   1 
ATOM   2900 C  CA  . LYS A 1 368 ? 12.710 30.163 8.386   1.00 17.14 ? 368  LYS A CA  1 
ATOM   2901 C  C   . LYS A 1 368 ? 13.091 30.198 9.855   1.00 18.40 ? 368  LYS A C   1 
ATOM   2902 O  O   . LYS A 1 368 ? 14.265 30.324 10.204  1.00 21.74 ? 368  LYS A O   1 
ATOM   2903 C  CB  . LYS A 1 368 ? 12.796 28.715 7.905   1.00 15.63 ? 368  LYS A CB  1 
ATOM   2904 C  CG  . LYS A 1 368 ? 12.173 28.449 6.566   1.00 14.68 ? 368  LYS A CG  1 
ATOM   2905 C  CD  . LYS A 1 368 ? 12.268 26.982 6.253   1.00 18.28 ? 368  LYS A CD  1 
ATOM   2906 C  CE  . LYS A 1 368 ? 11.717 26.662 4.890   1.00 20.59 ? 368  LYS A CE  1 
ATOM   2907 N  NZ  . LYS A 1 368 ? 11.858 25.208 4.624   1.00 26.48 ? 368  LYS A NZ  1 
ATOM   2908 N  N   . GLU A 1 369 ? 12.101 30.026 10.719  1.00 21.05 ? 369  GLU A N   1 
ATOM   2909 C  CA  . GLU A 1 369 ? 12.350 30.025 12.151  1.00 22.18 ? 369  GLU A CA  1 
ATOM   2910 C  C   . GLU A 1 369 ? 13.083 28.743 12.548  1.00 20.81 ? 369  GLU A C   1 
ATOM   2911 O  O   . GLU A 1 369 ? 13.031 27.731 11.844  1.00 18.16 ? 369  GLU A O   1 
ATOM   2912 C  CB  . GLU A 1 369 ? 11.031 30.107 12.918  1.00 27.22 ? 369  GLU A CB  1 
ATOM   2913 C  CG  . GLU A 1 369 ? 10.112 28.932 12.638  1.00 39.64 ? 369  GLU A CG  1 
ATOM   2914 C  CD  . GLU A 1 369 ? 8.924  28.851 13.575  1.00 46.00 ? 369  GLU A CD  1 
ATOM   2915 O  OE1 . GLU A 1 369 ? 9.082  29.142 14.783  1.00 49.79 ? 369  GLU A OE1 1 
ATOM   2916 O  OE2 . GLU A 1 369 ? 7.832  28.471 13.096  1.00 49.20 ? 369  GLU A OE2 1 
ATOM   2917 N  N   . VAL A 1 370 ? 13.775 28.795 13.676  1.00 20.47 ? 370  VAL A N   1 
ATOM   2918 C  CA  . VAL A 1 370 ? 14.480 27.635 14.178  1.00 19.08 ? 370  VAL A CA  1 
ATOM   2919 C  C   . VAL A 1 370 ? 13.472 26.875 15.034  1.00 21.17 ? 370  VAL A C   1 
ATOM   2920 O  O   . VAL A 1 370 ? 13.051 27.366 16.082  1.00 21.58 ? 370  VAL A O   1 
ATOM   2921 C  CB  . VAL A 1 370 ? 15.676 28.046 15.056  1.00 16.36 ? 370  VAL A CB  1 
ATOM   2922 C  CG1 . VAL A 1 370 ? 16.379 26.807 15.588  1.00 13.54 ? 370  VAL A CG1 1 
ATOM   2923 C  CG2 . VAL A 1 370 ? 16.640 28.904 14.254  1.00 15.64 ? 370  VAL A CG2 1 
ATOM   2924 N  N   . THR A 1 371 ? 13.014 25.727 14.550  1.00 20.44 ? 371  THR A N   1 
ATOM   2925 C  CA  . THR A 1 371 ? 12.063 24.930 15.313  1.00 19.70 ? 371  THR A CA  1 
ATOM   2926 C  C   . THR A 1 371 ? 12.827 23.935 16.181  1.00 21.53 ? 371  THR A C   1 
ATOM   2927 O  O   . THR A 1 371 ? 13.835 23.370 15.752  1.00 23.52 ? 371  THR A O   1 
ATOM   2928 C  CB  . THR A 1 371 ? 11.090 24.180 14.393  1.00 19.17 ? 371  THR A CB  1 
ATOM   2929 O  OG1 . THR A 1 371 ? 11.831 23.445 13.413  1.00 24.16 ? 371  THR A OG1 1 
ATOM   2930 C  CG2 . THR A 1 371 ? 10.170 25.149 13.691  1.00 15.16 ? 371  THR A CG2 1 
ATOM   2931 N  N   . ILE A 1 372 ? 12.385 23.768 17.421  1.00 21.23 ? 372  ILE A N   1 
ATOM   2932 C  CA  . ILE A 1 372 ? 13.031 22.837 18.334  1.00 22.94 ? 372  ILE A CA  1 
ATOM   2933 C  C   . ILE A 1 372 ? 12.170 21.584 18.445  1.00 26.48 ? 372  ILE A C   1 
ATOM   2934 O  O   . ILE A 1 372 ? 10.954 21.670 18.619  1.00 30.75 ? 372  ILE A O   1 
ATOM   2935 C  CB  . ILE A 1 372 ? 13.228 23.452 19.737  1.00 20.34 ? 372  ILE A CB  1 
ATOM   2936 C  CG1 . ILE A 1 372 ? 13.998 24.776 19.640  1.00 19.56 ? 372  ILE A CG1 1 
ATOM   2937 C  CG2 . ILE A 1 372 ? 13.952 22.470 20.648  1.00 16.52 ? 372  ILE A CG2 1 
ATOM   2938 C  CD1 . ILE A 1 372 ? 15.341 24.670 18.952  1.00 16.05 ? 372  ILE A CD1 1 
ATOM   2939 N  N   . ASN A 1 373 ? 12.799 20.425 18.287  1.00 28.60 ? 373  ASN A N   1 
ATOM   2940 C  CA  . ASN A 1 373 ? 12.106 19.149 18.372  1.00 30.66 ? 373  ASN A CA  1 
ATOM   2941 C  C   . ASN A 1 373 ? 12.175 18.628 19.799  1.00 35.66 ? 373  ASN A C   1 
ATOM   2942 O  O   . ASN A 1 373 ? 13.048 19.030 20.574  1.00 37.19 ? 373  ASN A O   1 
ATOM   2943 C  CB  . ASN A 1 373 ? 12.747 18.119 17.440  1.00 31.07 ? 373  ASN A CB  1 
ATOM   2944 C  CG  . ASN A 1 373 ? 12.665 18.509 15.980  1.00 32.78 ? 373  ASN A CG  1 
ATOM   2945 O  OD1 . ASN A 1 373 ? 13.630 18.356 15.233  1.00 35.66 ? 373  ASN A OD1 1 
ATOM   2946 N  ND2 . ASN A 1 373 ? 11.508 18.995 15.556  1.00 33.25 ? 373  ASN A ND2 1 
ATOM   2947 N  N   . ALA A 1 374 ? 11.290 17.687 20.117  1.00 38.60 ? 374  ALA A N   1 
ATOM   2948 C  CA  . ALA A 1 374 ? 11.225 17.073 21.443  1.00 38.95 ? 374  ALA A CA  1 
ATOM   2949 C  C   . ALA A 1 374 ? 12.569 16.508 21.912  1.00 38.88 ? 374  ALA A C   1 
ATOM   2950 O  O   . ALA A 1 374 ? 12.909 16.603 23.090  1.00 41.07 ? 374  ALA A O   1 
ATOM   2951 C  CB  . ALA A 1 374 ? 10.165 15.985 21.455  1.00 41.00 ? 374  ALA A CB  1 
ATOM   2952 N  N   . ASP A 1 375 ? 13.340 15.941 20.988  1.00 36.96 ? 375  ASP A N   1 
ATOM   2953 C  CA  . ASP A 1 375 ? 14.648 15.377 21.324  1.00 36.33 ? 375  ASP A CA  1 
ATOM   2954 C  C   . ASP A 1 375 ? 15.748 16.439 21.413  1.00 36.31 ? 375  ASP A C   1 
ATOM   2955 O  O   . ASP A 1 375 ? 16.933 16.114 21.368  1.00 39.37 ? 375  ASP A O   1 
ATOM   2956 C  CB  . ASP A 1 375 ? 15.045 14.289 20.314  1.00 40.11 ? 375  ASP A CB  1 
ATOM   2957 C  CG  . ASP A 1 375 ? 15.097 14.797 18.875  1.00 43.43 ? 375  ASP A CG  1 
ATOM   2958 O  OD1 . ASP A 1 375 ? 14.762 15.976 18.623  1.00 45.51 ? 375  ASP A OD1 1 
ATOM   2959 O  OD2 . ASP A 1 375 ? 15.472 14.004 17.985  1.00 46.24 ? 375  ASP A OD2 1 
ATOM   2960 N  N   . THR A 1 376 ? 15.335 17.701 21.527  1.00 32.16 ? 376  THR A N   1 
ATOM   2961 C  CA  . THR A 1 376 ? 16.216 18.868 21.628  1.00 30.46 ? 376  THR A CA  1 
ATOM   2962 C  C   . THR A 1 376 ? 17.020 19.236 20.376  1.00 29.24 ? 376  THR A C   1 
ATOM   2963 O  O   . THR A 1 376 ? 17.911 20.087 20.443  1.00 29.50 ? 376  THR A O   1 
ATOM   2964 C  CB  . THR A 1 376 ? 17.161 18.820 22.874  1.00 30.45 ? 376  THR A CB  1 
ATOM   2965 O  OG1 . THR A 1 376 ? 18.301 17.991 22.613  1.00 30.85 ? 376  THR A OG1 1 
ATOM   2966 C  CG2 . THR A 1 376 ? 16.422 18.291 24.090  1.00 29.44 ? 376  THR A CG2 1 
ATOM   2967 N  N   . THR A 1 377 ? 16.718 18.605 19.243  1.00 25.75 ? 377  THR A N   1 
ATOM   2968 C  CA  . THR A 1 377 ? 17.415 18.932 18.001  1.00 25.90 ? 377  THR A CA  1 
ATOM   2969 C  C   . THR A 1 377 ? 16.607 20.021 17.299  1.00 23.12 ? 377  THR A C   1 
ATOM   2970 O  O   . THR A 1 377 ? 15.514 20.367 17.746  1.00 21.31 ? 377  THR A O   1 
ATOM   2971 C  CB  . THR A 1 377 ? 17.561 17.707 17.053  1.00 29.04 ? 377  THR A CB  1 
ATOM   2972 O  OG1 . THR A 1 377 ? 16.268 17.156 16.754  1.00 29.01 ? 377  THR A OG1 1 
ATOM   2973 C  CG2 . THR A 1 377 ? 18.449 16.641 17.678  1.00 29.62 ? 377  THR A CG2 1 
ATOM   2974 N  N   . CYS A 1 378 ? 17.122 20.537 16.190  1.00 19.04 ? 378  CYS A N   1 
ATOM   2975 C  CA  . CYS A 1 378 ? 16.432 21.584 15.453  1.00 15.12 ? 378  CYS A CA  1 
ATOM   2976 C  C   . CYS A 1 378 ? 15.792 21.079 14.173  1.00 14.65 ? 378  CYS A C   1 
ATOM   2977 O  O   . CYS A 1 378 ? 16.242 20.094 13.580  1.00 15.03 ? 378  CYS A O   1 
ATOM   2978 C  CB  . CYS A 1 378 ? 17.397 22.709 15.100  1.00 10.72 ? 378  CYS A CB  1 
ATOM   2979 S  SG  . CYS A 1 378 ? 18.139 23.541 16.528  1.00 12.64 ? 378  CYS A SG  1 
ATOM   2980 N  N   . GLY A 1 379 ? 14.763 21.789 13.732  1.00 14.34 ? 379  GLY A N   1 
ATOM   2981 C  CA  . GLY A 1 379 ? 14.082 21.431 12.504  1.00 15.48 ? 379  GLY A CA  1 
ATOM   2982 C  C   . GLY A 1 379 ? 14.395 22.509 11.489  1.00 17.78 ? 379  GLY A C   1 
ATOM   2983 O  O   . GLY A 1 379 ? 15.295 23.329 11.709  1.00 19.75 ? 379  GLY A O   1 
ATOM   2984 N  N   . ASN A 1 380 ? 13.673 22.501 10.375  1.00 19.64 ? 380  ASN A N   1 
ATOM   2985 C  CA  . ASN A 1 380 ? 13.856 23.488 9.310   1.00 18.48 ? 380  ASN A CA  1 
ATOM   2986 C  C   . ASN A 1 380 ? 15.265 23.542 8.705   1.00 17.22 ? 380  ASN A C   1 
ATOM   2987 O  O   . ASN A 1 380 ? 15.660 24.542 8.108   1.00 17.28 ? 380  ASN A O   1 
ATOM   2988 C  CB  . ASN A 1 380 ? 13.395 24.877 9.787   1.00 19.50 ? 380  ASN A CB  1 
ATOM   2989 C  CG  . ASN A 1 380 ? 11.878 25.049 9.703   1.00 20.87 ? 380  ASN A CG  1 
ATOM   2990 O  OD1 . ASN A 1 380 ? 11.216 24.390 8.897   1.00 23.84 ? 380  ASN A OD1 1 
ATOM   2991 N  ND2 . ASN A 1 380 ? 11.325 25.926 10.530  1.00 16.57 ? 380  ASN A ND2 1 
ATOM   2992 N  N   . ASP A 1 381 ? 15.986 22.429 8.798   1.00 16.86 ? 381  ASP A N   1 
ATOM   2993 C  CA  . ASP A 1 381 ? 17.339 22.312 8.255   1.00 14.86 ? 381  ASP A CA  1 
ATOM   2994 C  C   . ASP A 1 381 ? 18.447 23.069 8.986   1.00 13.42 ? 381  ASP A C   1 
ATOM   2995 O  O   . ASP A 1 381 ? 19.504 23.329 8.419   1.00 13.19 ? 381  ASP A O   1 
ATOM   2996 C  CB  . ASP A 1 381 ? 17.377 22.615 6.748   1.00 16.10 ? 381  ASP A CB  1 
ATOM   2997 C  CG  . ASP A 1 381 ? 17.034 21.395 5.887   1.00 21.03 ? 381  ASP A CG  1 
ATOM   2998 O  OD1 . ASP A 1 381 ? 17.243 20.249 6.338   1.00 19.40 ? 381  ASP A OD1 1 
ATOM   2999 O  OD2 . ASP A 1 381 ? 16.577 21.582 4.738   1.00 25.29 ? 381  ASP A OD2 1 
ATOM   3000 N  N   . TRP A 1 382 ? 18.204 23.452 10.231  1.00 12.65 ? 382  TRP A N   1 
ATOM   3001 C  CA  . TRP A 1 382 ? 19.246 24.098 11.014  1.00 12.03 ? 382  TRP A CA  1 
ATOM   3002 C  C   . TRP A 1 382 ? 19.882 22.886 11.681  1.00 16.08 ? 382  TRP A C   1 
ATOM   3003 O  O   . TRP A 1 382 ? 19.169 22.091 12.298  1.00 18.79 ? 382  TRP A O   1 
ATOM   3004 C  CB  . TRP A 1 382 ? 18.639 25.019 12.064  1.00 12.11 ? 382  TRP A CB  1 
ATOM   3005 C  CG  . TRP A 1 382 ? 17.935 26.187 11.476  1.00 13.52 ? 382  TRP A CG  1 
ATOM   3006 C  CD1 . TRP A 1 382 ? 16.588 26.343 11.327  1.00 15.68 ? 382  TRP A CD1 1 
ATOM   3007 C  CD2 . TRP A 1 382 ? 18.538 27.377 10.954  1.00 15.44 ? 382  TRP A CD2 1 
ATOM   3008 N  NE1 . TRP A 1 382 ? 16.312 27.557 10.747  1.00 13.91 ? 382  TRP A NE1 1 
ATOM   3009 C  CE2 . TRP A 1 382 ? 17.490 28.214 10.506  1.00 14.60 ? 382  TRP A CE2 1 
ATOM   3010 C  CE3 . TRP A 1 382 ? 19.861 27.819 10.819  1.00 15.16 ? 382  TRP A CE3 1 
ATOM   3011 C  CZ2 . TRP A 1 382 ? 17.724 29.465 9.936   1.00 11.37 ? 382  TRP A CZ2 1 
ATOM   3012 C  CZ3 . TRP A 1 382 ? 20.094 29.068 10.248  1.00 13.05 ? 382  TRP A CZ3 1 
ATOM   3013 C  CH2 . TRP A 1 382 ? 19.027 29.875 9.816   1.00 12.03 ? 382  TRP A CH2 1 
ATOM   3014 N  N   . VAL A 1 383 ? 21.190 22.690 11.534  1.00 13.60 ? 383  VAL A N   1 
ATOM   3015 C  CA  . VAL A 1 383 ? 21.786 21.508 12.146  1.00 14.54 ? 383  VAL A CA  1 
ATOM   3016 C  C   . VAL A 1 383 ? 22.001 21.626 13.650  1.00 14.13 ? 383  VAL A C   1 
ATOM   3017 O  O   . VAL A 1 383 ? 21.907 20.637 14.368  1.00 19.73 ? 383  VAL A O   1 
ATOM   3018 C  CB  . VAL A 1 383 ? 23.045 20.957 11.366  1.00 14.50 ? 383  VAL A CB  1 
ATOM   3019 C  CG1 . VAL A 1 383 ? 23.215 21.642 10.034  1.00 7.65  ? 383  VAL A CG1 1 
ATOM   3020 C  CG2 . VAL A 1 383 ? 24.288 20.990 12.199  1.00 12.23 ? 383  VAL A CG2 1 
ATOM   3021 N  N   . CYS A 1 384 ? 22.244 22.839 14.133  1.00 11.67 ? 384  CYS A N   1 
ATOM   3022 C  CA  . CYS A 1 384 ? 22.435 23.074 15.562  1.00 8.73  ? 384  CYS A CA  1 
ATOM   3023 C  C   . CYS A 1 384 ? 23.459 22.196 16.275  1.00 9.92  ? 384  CYS A C   1 
ATOM   3024 O  O   . CYS A 1 384 ? 23.146 21.579 17.295  1.00 11.32 ? 384  CYS A O   1 
ATOM   3025 C  CB  . CYS A 1 384 ? 21.099 22.974 16.297  1.00 7.24  ? 384  CYS A CB  1 
ATOM   3026 S  SG  . CYS A 1 384 ? 19.894 24.239 15.806  1.00 10.38 ? 384  CYS A SG  1 
ATOM   3027 N  N   . GLU A 1 385 ? 24.704 22.232 15.808  1.00 9.56  ? 385  GLU A N   1 
ATOM   3028 C  CA  . GLU A 1 385 ? 25.787 21.455 16.404  1.00 7.39  ? 385  GLU A CA  1 
ATOM   3029 C  C   . GLU A 1 385 ? 25.887 21.738 17.898  1.00 7.65  ? 385  GLU A C   1 
ATOM   3030 O  O   . GLU A 1 385 ? 26.198 20.846 18.677  1.00 14.90 ? 385  GLU A O   1 
ATOM   3031 C  CB  . GLU A 1 385 ? 27.145 21.793 15.764  1.00 9.23  ? 385  GLU A CB  1 
ATOM   3032 C  CG  . GLU A 1 385 ? 27.316 21.425 14.294  1.00 10.93 ? 385  GLU A CG  1 
ATOM   3033 C  CD  . GLU A 1 385 ? 26.937 22.550 13.346  1.00 12.32 ? 385  GLU A CD  1 
ATOM   3034 O  OE1 . GLU A 1 385 ? 25.885 23.175 13.555  1.00 14.29 ? 385  GLU A OE1 1 
ATOM   3035 O  OE2 . GLU A 1 385 ? 27.677 22.803 12.375  1.00 11.84 ? 385  GLU A OE2 1 
ATOM   3036 N  N   . HIS A 1 386 ? 25.618 22.980 18.294  1.00 9.88  ? 386  HIS A N   1 
ATOM   3037 C  CA  . HIS A 1 386 ? 25.697 23.373 19.703  1.00 8.80  ? 386  HIS A CA  1 
ATOM   3038 C  C   . HIS A 1 386 ? 24.724 22.638 20.615  1.00 12.36 ? 386  HIS A C   1 
ATOM   3039 O  O   . HIS A 1 386 ? 24.829 22.724 21.840  1.00 15.61 ? 386  HIS A O   1 
ATOM   3040 C  CB  . HIS A 1 386 ? 25.553 24.891 19.861  1.00 3.79  ? 386  HIS A CB  1 
ATOM   3041 C  CG  . HIS A 1 386 ? 24.195 25.420 19.526  1.00 6.08  ? 386  HIS A CG  1 
ATOM   3042 N  ND1 . HIS A 1 386 ? 23.702 25.456 18.238  1.00 7.69  ? 386  HIS A ND1 1 
ATOM   3043 C  CD2 . HIS A 1 386 ? 23.224 25.941 20.314  1.00 4.30  ? 386  HIS A CD2 1 
ATOM   3044 C  CE1 . HIS A 1 386 ? 22.485 25.969 18.246  1.00 5.26  ? 386  HIS A CE1 1 
ATOM   3045 N  NE2 . HIS A 1 386 ? 22.172 26.273 19.493  1.00 9.05  ? 386  HIS A NE2 1 
ATOM   3046 N  N   . ARG A 1 387 ? 23.755 21.951 20.015  1.00 14.50 ? 387  ARG A N   1 
ATOM   3047 C  CA  . ARG A 1 387 ? 22.776 21.177 20.770  1.00 12.79 ? 387  ARG A CA  1 
ATOM   3048 C  C   . ARG A 1 387 ? 23.134 19.685 20.805  1.00 11.12 ? 387  ARG A C   1 
ATOM   3049 O  O   . ARG A 1 387 ? 22.525 18.924 21.551  1.00 18.62 ? 387  ARG A O   1 
ATOM   3050 C  CB  . ARG A 1 387 ? 21.365 21.400 20.220  1.00 9.07  ? 387  ARG A CB  1 
ATOM   3051 C  CG  . ARG A 1 387 ? 20.735 22.706 20.686  1.00 6.16  ? 387  ARG A CG  1 
ATOM   3052 C  CD  . ARG A 1 387 ? 19.418 22.982 19.988  1.00 5.85  ? 387  ARG A CD  1 
ATOM   3053 N  NE  . ARG A 1 387 ? 18.698 24.071 20.638  1.00 10.20 ? 387  ARG A NE  1 
ATOM   3054 C  CZ  . ARG A 1 387 ? 17.857 23.910 21.656  1.00 13.00 ? 387  ARG A CZ  1 
ATOM   3055 N  NH1 . ARG A 1 387 ? 17.581 22.695 22.112  1.00 14.50 ? 387  ARG A NH1 1 
ATOM   3056 N  NH2 . ARG A 1 387 ? 17.255 24.963 22.193  1.00 12.71 ? 387  ARG A NH2 1 
ATOM   3057 N  N   . TRP A 1 388 ? 24.117 19.265 20.007  1.00 8.19  ? 388  TRP A N   1 
ATOM   3058 C  CA  . TRP A 1 388 ? 24.552 17.866 20.011  1.00 7.57  ? 388  TRP A CA  1 
ATOM   3059 C  C   . TRP A 1 388 ? 25.124 17.614 21.411  1.00 9.59  ? 388  TRP A C   1 
ATOM   3060 O  O   . TRP A 1 388 ? 25.964 18.385 21.882  1.00 13.52 ? 388  TRP A O   1 
ATOM   3061 C  CB  . TRP A 1 388 ? 25.657 17.613 18.977  1.00 4.47  ? 388  TRP A CB  1 
ATOM   3062 C  CG  . TRP A 1 388 ? 25.247 17.701 17.531  1.00 5.98  ? 388  TRP A CG  1 
ATOM   3063 C  CD1 . TRP A 1 388 ? 24.032 18.083 17.036  1.00 5.90  ? 388  TRP A CD1 1 
ATOM   3064 C  CD2 . TRP A 1 388 ? 26.079 17.437 16.389  1.00 5.16  ? 388  TRP A CD2 1 
ATOM   3065 N  NE1 . TRP A 1 388 ? 24.058 18.081 15.660  1.00 8.16  ? 388  TRP A NE1 1 
ATOM   3066 C  CE2 . TRP A 1 388 ? 25.301 17.693 15.235  1.00 8.61  ? 388  TRP A CE2 1 
ATOM   3067 C  CE3 . TRP A 1 388 ? 27.406 17.013 16.229  1.00 5.62  ? 388  TRP A CE3 1 
ATOM   3068 C  CZ2 . TRP A 1 388 ? 25.808 17.542 13.934  1.00 4.55  ? 388  TRP A CZ2 1 
ATOM   3069 C  CZ3 . TRP A 1 388 ? 27.912 16.863 14.928  1.00 5.86  ? 388  TRP A CZ3 1 
ATOM   3070 C  CH2 . TRP A 1 388 ? 27.110 17.128 13.802  1.00 3.23  ? 388  TRP A CH2 1 
ATOM   3071 N  N   . ARG A 1 389 ? 24.694 16.533 22.057  1.00 9.32  ? 389  ARG A N   1 
ATOM   3072 C  CA  . ARG A 1 389 ? 25.143 16.195 23.409  1.00 11.53 ? 389  ARG A CA  1 
ATOM   3073 C  C   . ARG A 1 389 ? 26.652 16.226 23.553  1.00 9.98  ? 389  ARG A C   1 
ATOM   3074 O  O   . ARG A 1 389 ? 27.186 16.773 24.518  1.00 9.08  ? 389  ARG A O   1 
ATOM   3075 C  CB  . ARG A 1 389 ? 24.659 14.797 23.795  1.00 14.90 ? 389  ARG A CB  1 
ATOM   3076 C  CG  . ARG A 1 389 ? 25.006 14.395 25.233  1.00 19.22 ? 389  ARG A CG  1 
ATOM   3077 C  CD  . ARG A 1 389 ? 25.281 12.902 25.355  1.00 21.27 ? 389  ARG A CD  1 
ATOM   3078 N  NE  . ARG A 1 389 ? 24.280 12.098 24.661  1.00 27.27 ? 389  ARG A NE  1 
ATOM   3079 C  CZ  . ARG A 1 389 ? 24.553 11.192 23.724  1.00 28.46 ? 389  ARG A CZ  1 
ATOM   3080 N  NH1 . ARG A 1 389 ? 25.805 10.935 23.372  1.00 28.66 ? 389  ARG A NH1 1 
ATOM   3081 N  NH2 . ARG A 1 389 ? 23.566 10.523 23.149  1.00 32.55 ? 389  ARG A NH2 1 
ATOM   3082 N  N   . GLU A 1 390 ? 27.320 15.616 22.585  1.00 10.47 ? 390  GLU A N   1 
ATOM   3083 C  CA  . GLU A 1 390 ? 28.769 15.515 22.561  1.00 11.50 ? 390  GLU A CA  1 
ATOM   3084 C  C   . GLU A 1 390 ? 29.433 16.872 22.542  1.00 11.06 ? 390  GLU A C   1 
ATOM   3085 O  O   . GLU A 1 390 ? 30.503 17.049 23.114  1.00 18.16 ? 390  GLU A O   1 
ATOM   3086 C  CB  . GLU A 1 390 ? 29.226 14.683 21.360  1.00 9.95  ? 390  GLU A CB  1 
ATOM   3087 C  CG  . GLU A 1 390 ? 28.698 13.251 21.367  1.00 11.81 ? 390  GLU A CG  1 
ATOM   3088 C  CD  . GLU A 1 390 ? 27.362 13.086 20.659  1.00 13.59 ? 390  GLU A CD  1 
ATOM   3089 O  OE1 . GLU A 1 390 ? 26.667 14.088 20.394  1.00 15.39 ? 390  GLU A OE1 1 
ATOM   3090 O  OE2 . GLU A 1 390 ? 27.005 11.937 20.343  1.00 18.10 ? 390  GLU A OE2 1 
ATOM   3091 N  N   . ILE A 1 391 ? 28.787 17.839 21.902  1.00 10.41 ? 391  ILE A N   1 
ATOM   3092 C  CA  . ILE A 1 391 ? 29.335 19.182 21.837  1.00 8.80  ? 391  ILE A CA  1 
ATOM   3093 C  C   . ILE A 1 391 ? 28.940 20.012 23.059  1.00 7.76  ? 391  ILE A C   1 
ATOM   3094 O  O   . ILE A 1 391 ? 29.810 20.550 23.750  1.00 8.62  ? 391  ILE A O   1 
ATOM   3095 C  CB  . ILE A 1 391 ? 28.968 19.873 20.506  1.00 5.64  ? 391  ILE A CB  1 
ATOM   3096 C  CG1 . ILE A 1 391 ? 29.747 19.195 19.374  1.00 8.43  ? 391  ILE A CG1 1 
ATOM   3097 C  CG2 . ILE A 1 391 ? 29.290 21.355 20.561  1.00 4.84  ? 391  ILE A CG2 1 
ATOM   3098 C  CD1 . ILE A 1 391 ? 29.578 19.829 18.008  1.00 9.51  ? 391  ILE A CD1 1 
ATOM   3099 N  N   . ARG A 1 392 ? 27.656 20.026 23.405  1.00 5.84  ? 392  ARG A N   1 
ATOM   3100 C  CA  . ARG A 1 392 ? 27.227 20.803 24.561  1.00 9.84  ? 392  ARG A CA  1 
ATOM   3101 C  C   . ARG A 1 392 ? 27.876 20.365 25.870  1.00 10.62 ? 392  ARG A C   1 
ATOM   3102 O  O   . ARG A 1 392 ? 28.126 21.192 26.748  1.00 10.49 ? 392  ARG A O   1 
ATOM   3103 C  CB  . ARG A 1 392 ? 25.707 20.810 24.707  1.00 10.78 ? 392  ARG A CB  1 
ATOM   3104 C  CG  . ARG A 1 392 ? 25.095 19.523 25.168  1.00 17.56 ? 392  ARG A CG  1 
ATOM   3105 C  CD  . ARG A 1 392 ? 23.667 19.743 25.622  1.00 18.53 ? 392  ARG A CD  1 
ATOM   3106 N  NE  . ARG A 1 392 ? 22.917 18.493 25.598  1.00 25.26 ? 392  ARG A NE  1 
ATOM   3107 C  CZ  . ARG A 1 392 ? 22.995 17.549 26.533  1.00 30.93 ? 392  ARG A CZ  1 
ATOM   3108 N  NH1 . ARG A 1 392 ? 23.765 17.716 27.607  1.00 32.86 ? 392  ARG A NH1 1 
ATOM   3109 N  NH2 . ARG A 1 392 ? 22.275 16.443 26.409  1.00 33.69 ? 392  ARG A NH2 1 
ATOM   3110 N  N   . ASN A 1 393 ? 28.147 19.068 26.006  1.00 12.16 ? 393  ASN A N   1 
ATOM   3111 C  CA  . ASN A 1 393 ? 28.774 18.553 27.219  1.00 9.67  ? 393  ASN A CA  1 
ATOM   3112 C  C   . ASN A 1 393 ? 30.261 18.896 27.299  1.00 7.76  ? 393  ASN A C   1 
ATOM   3113 O  O   . ASN A 1 393 ? 30.819 18.985 28.395  1.00 10.36 ? 393  ASN A O   1 
ATOM   3114 C  CB  . ASN A 1 393 ? 28.532 17.048 27.377  1.00 12.48 ? 393  ASN A CB  1 
ATOM   3115 C  CG  . ASN A 1 393 ? 27.145 16.736 27.933  1.00 15.54 ? 393  ASN A CG  1 
ATOM   3116 O  OD1 . ASN A 1 393 ? 26.462 17.617 28.456  1.00 16.73 ? 393  ASN A OD1 1 
ATOM   3117 N  ND2 . ASN A 1 393 ? 26.727 15.488 27.822  1.00 16.81 ? 393  ASN A ND2 1 
ATOM   3118 N  N   . MET A 1 394 ? 30.897 19.093 26.144  1.00 6.83  ? 394  MET A N   1 
ATOM   3119 C  CA  . MET A 1 394 ? 32.304 19.477 26.105  1.00 9.30  ? 394  MET A CA  1 
ATOM   3120 C  C   . MET A 1 394 ? 32.439 20.971 26.399  1.00 10.88 ? 394  MET A C   1 
ATOM   3121 O  O   . MET A 1 394 ? 33.463 21.419 26.917  1.00 13.56 ? 394  MET A O   1 
ATOM   3122 C  CB  . MET A 1 394 ? 32.962 19.111 24.772  1.00 12.27 ? 394  MET A CB  1 
ATOM   3123 C  CG  . MET A 1 394 ? 33.366 17.640 24.671  1.00 10.22 ? 394  MET A CG  1 
ATOM   3124 S  SD  . MET A 1 394 ? 34.248 17.049 26.144  1.00 10.29 ? 394  MET A SD  1 
ATOM   3125 C  CE  . MET A 1 394 ? 35.758 17.952 26.022  1.00 11.62 ? 394  MET A CE  1 
ATOM   3126 N  N   . VAL A 1 395 ? 31.405 21.744 26.080  1.00 10.18 ? 395  VAL A N   1 
ATOM   3127 C  CA  . VAL A 1 395 ? 31.405 23.175 26.382  1.00 9.99  ? 395  VAL A CA  1 
ATOM   3128 C  C   . VAL A 1 395 ? 31.375 23.256 27.913  1.00 12.61 ? 395  VAL A C   1 
ATOM   3129 O  O   . VAL A 1 395 ? 32.105 24.035 28.528  1.00 16.32 ? 395  VAL A O   1 
ATOM   3130 C  CB  . VAL A 1 395 ? 30.161 23.902 25.757  1.00 10.00 ? 395  VAL A CB  1 
ATOM   3131 C  CG1 . VAL A 1 395 ? 29.911 25.247 26.447  1.00 7.41  ? 395  VAL A CG1 1 
ATOM   3132 C  CG2 . VAL A 1 395 ? 30.388 24.130 24.262  1.00 4.67  ? 395  VAL A CG2 1 
ATOM   3133 N  N   . TRP A 1 396 ? 30.567 22.394 28.520  1.00 12.79 ? 396  TRP A N   1 
ATOM   3134 C  CA  . TRP A 1 396 ? 30.454 22.323 29.969  1.00 16.13 ? 396  TRP A CA  1 
ATOM   3135 C  C   . TRP A 1 396 ? 31.806 21.916 30.572  1.00 14.17 ? 396  TRP A C   1 
ATOM   3136 O  O   . TRP A 1 396 ? 32.251 22.469 31.576  1.00 15.40 ? 396  TRP A O   1 
ATOM   3137 C  CB  . TRP A 1 396 ? 29.398 21.293 30.350  1.00 20.41 ? 396  TRP A CB  1 
ATOM   3138 C  CG  . TRP A 1 396 ? 28.992 21.410 31.748  1.00 28.24 ? 396  TRP A CG  1 
ATOM   3139 C  CD1 . TRP A 1 396 ? 29.416 20.649 32.793  1.00 29.68 ? 396  TRP A CD1 1 
ATOM   3140 C  CD2 . TRP A 1 396 ? 28.101 22.384 32.286  1.00 35.23 ? 396  TRP A CD2 1 
ATOM   3141 N  NE1 . TRP A 1 396 ? 28.848 21.094 33.957  1.00 33.09 ? 396  TRP A NE1 1 
ATOM   3142 C  CE2 . TRP A 1 396 ? 28.035 22.160 33.677  1.00 37.85 ? 396  TRP A CE2 1 
ATOM   3143 C  CE3 . TRP A 1 396 ? 27.351 23.431 31.730  1.00 37.86 ? 396  TRP A CE3 1 
ATOM   3144 C  CZ2 . TRP A 1 396 ? 27.244 22.948 34.525  1.00 40.28 ? 396  TRP A CZ2 1 
ATOM   3145 C  CZ3 . TRP A 1 396 ? 26.567 24.211 32.570  1.00 39.53 ? 396  TRP A CZ3 1 
ATOM   3146 C  CH2 . TRP A 1 396 ? 26.520 23.965 33.953  1.00 39.83 ? 396  TRP A CH2 1 
ATOM   3147 N  N   . PHE A 1 397 ? 32.424 20.914 29.962  1.00 13.30 ? 397  PHE A N   1 
ATOM   3148 C  CA  . PHE A 1 397 ? 33.724 20.408 30.375  1.00 11.58 ? 397  PHE A CA  1 
ATOM   3149 C  C   . PHE A 1 397 ? 34.709 21.570 30.447  1.00 11.21 ? 397  PHE A C   1 
ATOM   3150 O  O   . PHE A 1 397 ? 35.380 21.754 31.459  1.00 11.22 ? 397  PHE A O   1 
ATOM   3151 C  CB  . PHE A 1 397 ? 34.199 19.372 29.344  1.00 11.43 ? 397  PHE A CB  1 
ATOM   3152 C  CG  . PHE A 1 397 ? 35.506 18.696 29.686  1.00 11.87 ? 397  PHE A CG  1 
ATOM   3153 C  CD1 . PHE A 1 397 ? 36.722 19.341 29.475  1.00 9.52  ? 397  PHE A CD1 1 
ATOM   3154 C  CD2 . PHE A 1 397 ? 35.521 17.383 30.147  1.00 10.80 ? 397  PHE A CD2 1 
ATOM   3155 C  CE1 . PHE A 1 397 ? 37.930 18.689 29.714  1.00 7.86  ? 397  PHE A CE1 1 
ATOM   3156 C  CE2 . PHE A 1 397 ? 36.721 16.727 30.387  1.00 10.23 ? 397  PHE A CE2 1 
ATOM   3157 C  CZ  . PHE A 1 397 ? 37.931 17.384 30.169  1.00 9.84  ? 397  PHE A CZ  1 
ATOM   3158 N  N   . ARG A 1 398 ? 34.772 22.369 29.385  1.00 9.53  ? 398  ARG A N   1 
ATOM   3159 C  CA  . ARG A 1 398 ? 35.693 23.499 29.343  1.00 10.68 ? 398  ARG A CA  1 
ATOM   3160 C  C   . ARG A 1 398 ? 35.456 24.463 30.498  1.00 11.22 ? 398  ARG A C   1 
ATOM   3161 O  O   . ARG A 1 398 ? 36.411 24.956 31.099  1.00 12.63 ? 398  ARG A O   1 
ATOM   3162 C  CB  . ARG A 1 398 ? 35.607 24.236 28.007  1.00 8.28  ? 398  ARG A CB  1 
ATOM   3163 C  CG  . ARG A 1 398 ? 36.821 25.112 27.730  1.00 5.95  ? 398  ARG A CG  1 
ATOM   3164 C  CD  . ARG A 1 398 ? 36.777 25.673 26.330  1.00 5.73  ? 398  ARG A CD  1 
ATOM   3165 N  NE  . ARG A 1 398 ? 37.986 26.415 25.992  1.00 5.83  ? 398  ARG A NE  1 
ATOM   3166 C  CZ  . ARG A 1 398 ? 39.200 25.879 25.891  1.00 6.80  ? 398  ARG A CZ  1 
ATOM   3167 N  NH1 . ARG A 1 398 ? 39.386 24.585 26.116  1.00 7.39  ? 398  ARG A NH1 1 
ATOM   3168 N  NH2 . ARG A 1 398 ? 40.237 26.642 25.575  1.00 8.12  ? 398  ARG A NH2 1 
ATOM   3169 N  N   . ASN A 1 399 ? 34.188 24.712 30.822  1.00 14.45 ? 399  ASN A N   1 
ATOM   3170 C  CA  . ASN A 1 399 ? 33.843 25.596 31.935  1.00 12.39 ? 399  ASN A CA  1 
ATOM   3171 C  C   . ASN A 1 399 ? 34.394 24.997 33.224  1.00 14.34 ? 399  ASN A C   1 
ATOM   3172 O  O   . ASN A 1 399 ? 35.174 25.631 33.934  1.00 17.15 ? 399  ASN A O   1 
ATOM   3173 C  CB  . ASN A 1 399 ? 32.320 25.761 32.055  1.00 9.92  ? 399  ASN A CB  1 
ATOM   3174 C  CG  . ASN A 1 399 ? 31.730 26.686 30.997  1.00 8.80  ? 399  ASN A CG  1 
ATOM   3175 O  OD1 . ASN A 1 399 ? 30.520 26.867 30.930  1.00 13.17 ? 399  ASN A OD1 1 
ATOM   3176 N  ND2 . ASN A 1 399 ? 32.580 27.278 30.178  1.00 10.77 ? 399  ASN A ND2 1 
ATOM   3177 N  N   . VAL A 1 400 ? 34.042 23.739 33.472  1.00 16.05 ? 400  VAL A N   1 
ATOM   3178 C  CA  . VAL A 1 400 ? 34.473 23.011 34.663  1.00 14.92 ? 400  VAL A CA  1 
ATOM   3179 C  C   . VAL A 1 400 ? 35.987 22.979 34.907  1.00 15.33 ? 400  VAL A C   1 
ATOM   3180 O  O   . VAL A 1 400 ? 36.438 23.196 36.030  1.00 20.37 ? 400  VAL A O   1 
ATOM   3181 C  CB  . VAL A 1 400 ? 33.941 21.553 34.637  1.00 15.54 ? 400  VAL A CB  1 
ATOM   3182 C  CG1 . VAL A 1 400 ? 34.426 20.781 35.856  1.00 13.57 ? 400  VAL A CG1 1 
ATOM   3183 C  CG2 . VAL A 1 400 ? 32.432 21.550 34.597  1.00 12.58 ? 400  VAL A CG2 1 
ATOM   3184 N  N   . VAL A 1 401 ? 36.771 22.720 33.865  1.00 17.27 ? 401  VAL A N   1 
ATOM   3185 C  CA  . VAL A 1 401 ? 38.225 22.629 34.019  1.00 15.40 ? 401  VAL A CA  1 
ATOM   3186 C  C   . VAL A 1 401 ? 38.999 23.919 33.763  1.00 17.64 ? 401  VAL A C   1 
ATOM   3187 O  O   . VAL A 1 401 ? 40.234 23.914 33.768  1.00 14.59 ? 401  VAL A O   1 
ATOM   3188 C  CB  . VAL A 1 401 ? 38.827 21.508 33.121  1.00 12.15 ? 401  VAL A CB  1 
ATOM   3189 C  CG1 . VAL A 1 401 ? 38.046 20.222 33.284  1.00 5.37  ? 401  VAL A CG1 1 
ATOM   3190 C  CG2 . VAL A 1 401 ? 38.870 21.947 31.662  1.00 7.78  ? 401  VAL A CG2 1 
ATOM   3191 N  N   . ASP A 1 402 ? 38.286 25.017 33.545  1.00 18.73 ? 402  ASP A N   1 
ATOM   3192 C  CA  . ASP A 1 402 ? 38.925 26.300 33.271  1.00 20.08 ? 402  ASP A CA  1 
ATOM   3193 C  C   . ASP A 1 402 ? 40.037 26.633 34.263  1.00 20.99 ? 402  ASP A C   1 
ATOM   3194 O  O   . ASP A 1 402 ? 39.829 26.591 35.479  1.00 23.83 ? 402  ASP A O   1 
ATOM   3195 C  CB  . ASP A 1 402 ? 37.882 27.417 33.283  1.00 24.31 ? 402  ASP A CB  1 
ATOM   3196 C  CG  . ASP A 1 402 ? 38.479 28.780 32.963  1.00 29.13 ? 402  ASP A CG  1 
ATOM   3197 O  OD1 . ASP A 1 402 ? 39.261 28.882 31.986  1.00 29.62 ? 402  ASP A OD1 1 
ATOM   3198 O  OD2 . ASP A 1 402 ? 38.154 29.751 33.685  1.00 32.20 ? 402  ASP A OD2 1 
ATOM   3199 N  N   . GLY A 1 403 ? 41.222 26.947 33.744  1.00 18.76 ? 403  GLY A N   1 
ATOM   3200 C  CA  . GLY A 1 403 ? 42.335 27.293 34.613  1.00 20.47 ? 403  GLY A CA  1 
ATOM   3201 C  C   . GLY A 1 403 ? 43.213 26.141 35.075  1.00 22.75 ? 403  GLY A C   1 
ATOM   3202 O  O   . GLY A 1 403 ? 44.286 26.369 35.633  1.00 25.49 ? 403  GLY A O   1 
ATOM   3203 N  N   . GLU A 1 404 ? 42.748 24.908 34.892  1.00 20.00 ? 404  GLU A N   1 
ATOM   3204 C  CA  . GLU A 1 404 ? 43.521 23.736 35.282  1.00 20.00 ? 404  GLU A CA  1 
ATOM   3205 C  C   . GLU A 1 404 ? 44.531 23.487 34.173  1.00 20.00 ? 404  GLU A C   1 
ATOM   3206 O  O   . GLU A 1 404 ? 44.214 23.625 32.998  1.00 20.00 ? 404  GLU A O   1 
ATOM   3207 C  CB  . GLU A 1 404 ? 42.617 22.522 35.421  1.00 20.00 ? 404  GLU A CB  1 
ATOM   3208 C  CG  . GLU A 1 404 ? 41.580 22.682 36.534  1.00 20.00 ? 404  GLU A CG  1 
ATOM   3209 C  CD  . GLU A 1 404 ? 42.211 22.829 37.920  1.00 20.00 ? 404  GLU A CD  1 
ATOM   3210 O  OE1 . GLU A 1 404 ? 43.186 22.062 38.268  1.00 20.00 ? 404  GLU A OE1 1 
ATOM   3211 O  OE2 . GLU A 1 404 ? 41.764 23.717 38.742  1.00 20.00 ? 404  GLU A OE2 1 
ATOM   3212 N  N   . PRO A 1 405 ? 45.774 23.150 34.530  1.00 17.54 ? 405  PRO A N   1 
ATOM   3213 C  CA  . PRO A 1 405 ? 46.794 22.904 33.509  1.00 17.34 ? 405  PRO A CA  1 
ATOM   3214 C  C   . PRO A 1 405 ? 46.721 21.562 32.801  1.00 16.20 ? 405  PRO A C   1 
ATOM   3215 O  O   . PRO A 1 405 ? 46.227 20.574 33.345  1.00 18.73 ? 405  PRO A O   1 
ATOM   3216 C  CB  . PRO A 1 405 ? 48.091 23.019 34.306  1.00 19.33 ? 405  PRO A CB  1 
ATOM   3217 C  CG  . PRO A 1 405 ? 47.706 22.416 35.625  1.00 17.43 ? 405  PRO A CG  1 
ATOM   3218 C  CD  . PRO A 1 405 ? 46.344 23.054 35.885  1.00 19.04 ? 405  PRO A CD  1 
ATOM   3219 N  N   . PHE A 1 406 ? 47.238 21.551 31.580  1.00 15.97 ? 406  PHE A N   1 
ATOM   3220 C  CA  . PHE A 1 406 ? 47.326 20.358 30.753  1.00 17.26 ? 406  PHE A CA  1 
ATOM   3221 C  C   . PHE A 1 406 ? 48.173 19.390 31.584  1.00 20.84 ? 406  PHE A C   1 
ATOM   3222 O  O   . PHE A 1 406 ? 49.212 19.788 32.126  1.00 21.88 ? 406  PHE A O   1 
ATOM   3223 C  CB  . PHE A 1 406 ? 48.069 20.737 29.471  1.00 17.30 ? 406  PHE A CB  1 
ATOM   3224 C  CG  . PHE A 1 406 ? 48.304 19.601 28.520  1.00 18.49 ? 406  PHE A CG  1 
ATOM   3225 C  CD1 . PHE A 1 406 ? 47.268 19.097 27.743  1.00 18.13 ? 406  PHE A CD1 1 
ATOM   3226 C  CD2 . PHE A 1 406 ? 49.584 19.090 28.339  1.00 21.03 ? 406  PHE A CD2 1 
ATOM   3227 C  CE1 . PHE A 1 406 ? 47.509 18.107 26.797  1.00 19.32 ? 406  PHE A CE1 1 
ATOM   3228 C  CE2 . PHE A 1 406 ? 49.832 18.097 27.392  1.00 20.57 ? 406  PHE A CE2 1 
ATOM   3229 C  CZ  . PHE A 1 406 ? 48.792 17.609 26.621  1.00 20.27 ? 406  PHE A CZ  1 
ATOM   3230 N  N   . ALA A 1 407 ? 47.723 18.144 31.719  1.00 18.53 ? 407  ALA A N   1 
ATOM   3231 C  CA  . ALA A 1 407 ? 48.458 17.163 32.514  1.00 16.63 ? 407  ALA A CA  1 
ATOM   3232 C  C   . ALA A 1 407 ? 48.135 15.729 32.119  1.00 17.89 ? 407  ALA A C   1 
ATOM   3233 O  O   . ALA A 1 407 ? 47.247 15.479 31.304  1.00 17.69 ? 407  ALA A O   1 
ATOM   3234 C  CB  . ALA A 1 407 ? 48.158 17.373 34.000  1.00 14.55 ? 407  ALA A CB  1 
ATOM   3235 N  N   . ASN A 1 408 ? 48.909 14.796 32.668  1.00 16.43 ? 408  ASN A N   1 
ATOM   3236 C  CA  . ASN A 1 408 ? 48.718 13.363 32.439  1.00 13.14 ? 408  ASN A CA  1 
ATOM   3237 C  C   . ASN A 1 408 ? 48.503 12.927 30.996  1.00 13.56 ? 408  ASN A C   1 
ATOM   3238 O  O   . ASN A 1 408 ? 47.577 12.167 30.694  1.00 17.65 ? 408  ASN A O   1 
ATOM   3239 C  CB  . ASN A 1 408 ? 47.575 12.846 33.316  1.00 10.89 ? 408  ASN A CB  1 
ATOM   3240 C  CG  . ASN A 1 408 ? 47.878 12.970 34.785  1.00 9.85  ? 408  ASN A CG  1 
ATOM   3241 O  OD1 . ASN A 1 408 ? 47.194 13.684 35.519  1.00 13.72 ? 408  ASN A OD1 1 
ATOM   3242 N  ND2 . ASN A 1 408 ? 48.908 12.276 35.229  1.00 12.49 ? 408  ASN A ND2 1 
ATOM   3243 N  N   . TRP A 1 409 ? 49.363 13.403 30.106  1.00 14.24 ? 409  TRP A N   1 
ATOM   3244 C  CA  . TRP A 1 409 ? 49.274 13.025 28.706  1.00 13.11 ? 409  TRP A CA  1 
ATOM   3245 C  C   . TRP A 1 409 ? 49.676 11.563 28.555  1.00 14.52 ? 409  TRP A C   1 
ATOM   3246 O  O   . TRP A 1 409 ? 50.591 11.085 29.226  1.00 17.51 ? 409  TRP A O   1 
ATOM   3247 C  CB  . TRP A 1 409 ? 50.196 13.892 27.849  1.00 10.04 ? 409  TRP A CB  1 
ATOM   3248 C  CG  . TRP A 1 409 ? 50.297 13.420 26.419  1.00 8.91  ? 409  TRP A CG  1 
ATOM   3249 C  CD1 . TRP A 1 409 ? 51.208 12.539 25.914  1.00 9.02  ? 409  TRP A CD1 1 
ATOM   3250 C  CD2 . TRP A 1 409 ? 49.445 13.787 25.326  1.00 4.25  ? 409  TRP A CD2 1 
ATOM   3251 N  NE1 . TRP A 1 409 ? 50.974 12.332 24.575  1.00 9.08  ? 409  TRP A NE1 1 
ATOM   3252 C  CE2 . TRP A 1 409 ? 49.899 13.084 24.189  1.00 5.83  ? 409  TRP A CE2 1 
ATOM   3253 C  CE3 . TRP A 1 409 ? 48.346 14.635 25.196  1.00 3.74  ? 409  TRP A CE3 1 
ATOM   3254 C  CZ2 . TRP A 1 409 ? 49.289 13.204 22.943  1.00 5.21  ? 409  TRP A CZ2 1 
ATOM   3255 C  CZ3 . TRP A 1 409 ? 47.738 14.753 23.956  1.00 3.67  ? 409  TRP A CZ3 1 
ATOM   3256 C  CH2 . TRP A 1 409 ? 48.212 14.041 22.847  1.00 4.08  ? 409  TRP A CH2 1 
ATOM   3257 N  N   . TRP A 1 410 ? 49.010 10.879 27.637  1.00 13.92 ? 410  TRP A N   1 
ATOM   3258 C  CA  . TRP A 1 410 ? 49.276 9.486  27.343  1.00 11.86 ? 410  TRP A CA  1 
ATOM   3259 C  C   . TRP A 1 410 ? 48.963 9.271  25.873  1.00 11.03 ? 410  TRP A C   1 
ATOM   3260 O  O   . TRP A 1 410 ? 48.072 9.920  25.330  1.00 13.08 ? 410  TRP A O   1 
ATOM   3261 C  CB  . TRP A 1 410 ? 48.371 8.568  28.187  1.00 14.06 ? 410  TRP A CB  1 
ATOM   3262 C  CG  . TRP A 1 410 ? 48.457 7.118  27.768  1.00 11.53 ? 410  TRP A CG  1 
ATOM   3263 C  CD1 . TRP A 1 410 ? 49.385 6.200  28.176  1.00 13.41 ? 410  TRP A CD1 1 
ATOM   3264 C  CD2 . TRP A 1 410 ? 47.638 6.449  26.799  1.00 11.14 ? 410  TRP A CD2 1 
ATOM   3265 N  NE1 . TRP A 1 410 ? 49.204 5.012  27.512  1.00 11.56 ? 410  TRP A NE1 1 
ATOM   3266 C  CE2 . TRP A 1 410 ? 48.138 5.137  26.661  1.00 12.64 ? 410  TRP A CE2 1 
ATOM   3267 C  CE3 . TRP A 1 410 ? 46.531 6.833  26.030  1.00 13.76 ? 410  TRP A CE3 1 
ATOM   3268 C  CZ2 . TRP A 1 410 ? 47.569 4.205  25.784  1.00 13.63 ? 410  TRP A CZ2 1 
ATOM   3269 C  CZ3 . TRP A 1 410 ? 45.965 5.903  25.156  1.00 9.54  ? 410  TRP A CZ3 1 
ATOM   3270 C  CH2 . TRP A 1 410 ? 46.486 4.607  25.043  1.00 13.84 ? 410  TRP A CH2 1 
ATOM   3271 N  N   . ASP A 1 411 ? 49.712 8.380  25.233  1.00 13.89 ? 411  ASP A N   1 
ATOM   3272 C  CA  . ASP A 1 411 ? 49.479 8.020  23.836  1.00 13.29 ? 411  ASP A CA  1 
ATOM   3273 C  C   . ASP A 1 411 ? 50.054 6.630  23.566  1.00 13.86 ? 411  ASP A C   1 
ATOM   3274 O  O   . ASP A 1 411 ? 50.933 6.162  24.291  1.00 17.07 ? 411  ASP A O   1 
ATOM   3275 C  CB  . ASP A 1 411 ? 50.040 9.065  22.854  1.00 15.54 ? 411  ASP A CB  1 
ATOM   3276 C  CG  . ASP A 1 411 ? 51.551 9.116  22.830  1.00 14.66 ? 411  ASP A CG  1 
ATOM   3277 O  OD1 . ASP A 1 411 ? 52.161 8.363  22.052  1.00 20.02 ? 411  ASP A OD1 1 
ATOM   3278 O  OD2 . ASP A 1 411 ? 52.137 9.932  23.562  1.00 21.66 ? 411  ASP A OD2 1 
ATOM   3279 N  N   . ASN A 1 412 ? 49.516 5.951  22.562  1.00 13.66 ? 412  ASN A N   1 
ATOM   3280 C  CA  . ASN A 1 412 ? 49.984 4.617  22.210  1.00 12.32 ? 412  ASN A CA  1 
ATOM   3281 C  C   . ASN A 1 412 ? 50.985 4.671  21.062  1.00 14.05 ? 412  ASN A C   1 
ATOM   3282 O  O   . ASN A 1 412 ? 51.264 3.666  20.417  1.00 15.68 ? 412  ASN A O   1 
ATOM   3283 C  CB  . ASN A 1 412 ? 48.804 3.718  21.838  1.00 12.81 ? 412  ASN A CB  1 
ATOM   3284 C  CG  . ASN A 1 412 ? 48.194 4.074  20.497  1.00 12.50 ? 412  ASN A CG  1 
ATOM   3285 O  OD1 . ASN A 1 412 ? 48.325 5.202  20.009  1.00 14.70 ? 412  ASN A OD1 1 
ATOM   3286 N  ND2 . ASN A 1 412 ? 47.513 3.114  19.896  1.00 11.44 ? 412  ASN A ND2 1 
ATOM   3287 N  N   . GLY A 1 413 ? 51.517 5.861  20.807  1.00 16.86 ? 413  GLY A N   1 
ATOM   3288 C  CA  . GLY A 1 413 ? 52.483 6.035  19.742  1.00 15.08 ? 413  GLY A CA  1 
ATOM   3289 C  C   . GLY A 1 413 ? 51.855 6.053  18.365  1.00 17.38 ? 413  GLY A C   1 
ATOM   3290 O  O   . GLY A 1 413 ? 52.561 6.067  17.364  1.00 22.89 ? 413  GLY A O   1 
ATOM   3291 N  N   . SER A 1 414 ? 50.531 6.070  18.308  1.00 19.16 ? 414  SER A N   1 
ATOM   3292 C  CA  . SER A 1 414 ? 49.832 6.086  17.036  1.00 19.92 ? 414  SER A CA  1 
ATOM   3293 C  C   . SER A 1 414 ? 48.658 7.072  17.107  1.00 20.48 ? 414  SER A C   1 
ATOM   3294 O  O   . SER A 1 414 ? 48.876 8.283  17.121  1.00 22.54 ? 414  SER A O   1 
ATOM   3295 C  CB  . SER A 1 414 ? 49.372 4.666  16.684  1.00 19.91 ? 414  SER A CB  1 
ATOM   3296 O  OG  . SER A 1 414 ? 48.750 4.615  15.412  1.00 24.96 ? 414  SER A OG  1 
ATOM   3297 N  N   . ASN A 1 415 ? 47.426 6.569  17.196  1.00 17.77 ? 415  ASN A N   1 
ATOM   3298 C  CA  . ASN A 1 415 ? 46.258 7.442  17.264  1.00 13.90 ? 415  ASN A CA  1 
ATOM   3299 C  C   . ASN A 1 415 ? 45.361 7.285  18.489  1.00 11.81 ? 415  ASN A C   1 
ATOM   3300 O  O   . ASN A 1 415 ? 44.175 7.605  18.436  1.00 15.30 ? 415  ASN A O   1 
ATOM   3301 C  CB  . ASN A 1 415 ? 45.428 7.343  15.985  1.00 13.87 ? 415  ASN A CB  1 
ATOM   3302 C  CG  . ASN A 1 415 ? 46.176 7.845  14.774  1.00 16.91 ? 415  ASN A CG  1 
ATOM   3303 O  OD1 . ASN A 1 415 ? 46.292 9.054  14.553  1.00 18.53 ? 415  ASN A OD1 1 
ATOM   3304 N  ND2 . ASN A 1 415 ? 46.712 6.922  13.994  1.00 17.46 ? 415  ASN A ND2 1 
ATOM   3305 N  N   . GLN A 1 416 ? 45.897 6.728  19.567  1.00 8.72  ? 416  GLN A N   1 
ATOM   3306 C  CA  . GLN A 1 416 ? 45.130 6.603  20.798  1.00 11.79 ? 416  GLN A CA  1 
ATOM   3307 C  C   . GLN A 1 416 ? 45.836 7.597  21.693  1.00 15.72 ? 416  GLN A C   1 
ATOM   3308 O  O   . GLN A 1 416 ? 47.057 7.535  21.872  1.00 15.45 ? 416  GLN A O   1 
ATOM   3309 C  CB  . GLN A 1 416 ? 45.163 5.183  21.340  1.00 10.54 ? 416  GLN A CB  1 
ATOM   3310 C  CG  . GLN A 1 416 ? 44.307 4.257  20.504  1.00 12.91 ? 416  GLN A CG  1 
ATOM   3311 C  CD  . GLN A 1 416 ? 44.378 2.810  20.936  1.00 15.65 ? 416  GLN A CD  1 
ATOM   3312 O  OE1 . GLN A 1 416 ? 45.163 2.442  21.811  1.00 18.61 ? 416  GLN A OE1 1 
ATOM   3313 N  NE2 . GLN A 1 416 ? 43.559 1.975  20.315  1.00 15.63 ? 416  GLN A NE2 1 
ATOM   3314 N  N   . VAL A 1 417 ? 45.065 8.539  22.215  1.00 16.61 ? 417  VAL A N   1 
ATOM   3315 C  CA  . VAL A 1 417 ? 45.604 9.643  22.994  1.00 14.19 ? 417  VAL A CA  1 
ATOM   3316 C  C   . VAL A 1 417 ? 44.734 9.984  24.206  1.00 12.86 ? 417  VAL A C   1 
ATOM   3317 O  O   . VAL A 1 417 ? 43.530 9.735  24.202  1.00 15.13 ? 417  VAL A O   1 
ATOM   3318 C  CB  . VAL A 1 417 ? 45.708 10.865 22.022  1.00 15.04 ? 417  VAL A CB  1 
ATOM   3319 C  CG1 . VAL A 1 417 ? 45.283 12.168 22.674  1.00 17.00 ? 417  VAL A CG1 1 
ATOM   3320 C  CG2 . VAL A 1 417 ? 47.095 10.949 21.432  1.00 13.92 ? 417  VAL A CG2 1 
ATOM   3321 N  N   . ALA A 1 418 ? 45.341 10.576 25.226  1.00 8.46  ? 418  ALA A N   1 
ATOM   3322 C  CA  . ALA A 1 418 ? 44.621 10.967 26.431  1.00 9.36  ? 418  ALA A CA  1 
ATOM   3323 C  C   . ALA A 1 418 ? 45.391 12.027 27.201  1.00 10.76 ? 418  ALA A C   1 
ATOM   3324 O  O   . ALA A 1 418 ? 46.619 12.077 27.146  1.00 14.14 ? 418  ALA A O   1 
ATOM   3325 C  CB  . ALA A 1 418 ? 44.389 9.768  27.327  1.00 9.43  ? 418  ALA A CB  1 
ATOM   3326 N  N   . PHE A 1 419 ? 44.658 12.896 27.883  1.00 7.29  ? 419  PHE A N   1 
ATOM   3327 C  CA  . PHE A 1 419 ? 45.254 13.940 28.704  1.00 10.38 ? 419  PHE A CA  1 
ATOM   3328 C  C   . PHE A 1 419 ? 44.190 14.446 29.645  1.00 10.39 ? 419  PHE A C   1 
ATOM   3329 O  O   . PHE A 1 419 ? 42.997 14.213 29.433  1.00 11.71 ? 419  PHE A O   1 
ATOM   3330 C  CB  . PHE A 1 419 ? 45.859 15.096 27.877  1.00 7.27  ? 419  PHE A CB  1 
ATOM   3331 C  CG  . PHE A 1 419 ? 44.858 15.884 27.062  1.00 9.23  ? 419  PHE A CG  1 
ATOM   3332 C  CD1 . PHE A 1 419 ? 44.188 16.975 27.614  1.00 10.22 ? 419  PHE A CD1 1 
ATOM   3333 C  CD2 . PHE A 1 419 ? 44.628 15.570 25.726  1.00 7.53  ? 419  PHE A CD2 1 
ATOM   3334 C  CE1 . PHE A 1 419 ? 43.311 17.743 26.851  1.00 8.23  ? 419  PHE A CE1 1 
ATOM   3335 C  CE2 . PHE A 1 419 ? 43.754 16.330 24.954  1.00 7.58  ? 419  PHE A CE2 1 
ATOM   3336 C  CZ  . PHE A 1 419 ? 43.094 17.419 25.515  1.00 9.32  ? 419  PHE A CZ  1 
ATOM   3337 N  N   . GLY A 1 420 ? 44.635 15.099 30.707  1.00 12.82 ? 420  GLY A N   1 
ATOM   3338 C  CA  . GLY A 1 420 ? 43.726 15.644 31.690  1.00 12.51 ? 420  GLY A CA  1 
ATOM   3339 C  C   . GLY A 1 420 ? 43.948 17.128 31.884  1.00 14.43 ? 420  GLY A C   1 
ATOM   3340 O  O   . GLY A 1 420 ? 44.793 17.750 31.234  1.00 8.88  ? 420  GLY A O   1 
ATOM   3341 N  N   . ARG A 1 421 ? 43.166 17.702 32.783  1.00 13.34 ? 421  ARG A N   1 
ATOM   3342 C  CA  . ARG A 1 421 ? 43.249 19.113 33.093  1.00 9.97  ? 421  ARG A CA  1 
ATOM   3343 C  C   . ARG A 1 421 ? 43.247 19.222 34.602  1.00 11.39 ? 421  ARG A C   1 
ATOM   3344 O  O   . ARG A 1 421 ? 42.195 19.179 35.247  1.00 9.23  ? 421  ARG A O   1 
ATOM   3345 C  CB  . ARG A 1 421 ? 42.059 19.843 32.480  1.00 13.83 ? 421  ARG A CB  1 
ATOM   3346 C  CG  . ARG A 1 421 ? 42.171 20.006 30.975  1.00 13.97 ? 421  ARG A CG  1 
ATOM   3347 C  CD  . ARG A 1 421 ? 43.016 21.211 30.624  1.00 15.89 ? 421  ARG A CD  1 
ATOM   3348 N  NE  . ARG A 1 421 ? 42.230 22.156 29.834  1.00 23.80 ? 421  ARG A NE  1 
ATOM   3349 C  CZ  . ARG A 1 421 ? 41.968 23.409 30.184  1.00 23.73 ? 421  ARG A CZ  1 
ATOM   3350 N  NH1 . ARG A 1 421 ? 42.437 23.899 31.314  1.00 21.10 ? 421  ARG A NH1 1 
ATOM   3351 N  NH2 . ARG A 1 421 ? 41.234 24.176 29.391  1.00 30.45 ? 421  ARG A NH2 1 
ATOM   3352 N  N   . GLY A 1 422 ? 44.445 19.314 35.165  1.00 12.30 ? 422  GLY A N   1 
ATOM   3353 C  CA  . GLY A 1 422 ? 44.582 19.397 36.604  1.00 14.52 ? 422  GLY A CA  1 
ATOM   3354 C  C   . GLY A 1 422 ? 43.966 18.156 37.207  1.00 16.47 ? 422  GLY A C   1 
ATOM   3355 O  O   . GLY A 1 422 ? 44.265 17.039 36.783  1.00 19.73 ? 422  GLY A O   1 
ATOM   3356 N  N   . ASN A 1 423 ? 43.067 18.355 38.162  1.00 18.87 ? 423  ASN A N   1 
ATOM   3357 C  CA  . ASN A 1 423 ? 42.390 17.251 38.823  1.00 16.86 ? 423  ASN A CA  1 
ATOM   3358 C  C   . ASN A 1 423 ? 40.893 17.385 38.628  1.00 18.53 ? 423  ASN A C   1 
ATOM   3359 O  O   . ASN A 1 423 ? 40.105 16.819 39.386  1.00 20.31 ? 423  ASN A O   1 
ATOM   3360 C  CB  . ASN A 1 423 ? 42.719 17.244 40.319  1.00 19.96 ? 423  ASN A CB  1 
ATOM   3361 C  CG  . ASN A 1 423 ? 42.229 18.495 41.044  1.00 25.72 ? 423  ASN A CG  1 
ATOM   3362 O  OD1 . ASN A 1 423 ? 41.611 19.386 40.450  1.00 29.22 ? 423  ASN A OD1 1 
ATOM   3363 N  ND2 . ASN A 1 423 ? 42.505 18.565 42.340  1.00 25.67 ? 423  ASN A ND2 1 
ATOM   3364 N  N   . ARG A 1 424 ? 40.492 18.133 37.607  1.00 17.66 ? 424  ARG A N   1 
ATOM   3365 C  CA  . ARG A 1 424 ? 39.073 18.337 37.372  1.00 14.17 ? 424  ARG A CA  1 
ATOM   3366 C  C   . ARG A 1 424 ? 38.495 17.698 36.124  1.00 13.13 ? 424  ARG A C   1 
ATOM   3367 O  O   . ARG A 1 424 ? 37.275 17.662 35.960  1.00 16.38 ? 424  ARG A O   1 
ATOM   3368 C  CB  . ARG A 1 424 ? 38.743 19.830 37.435  1.00 18.33 ? 424  ARG A CB  1 
ATOM   3369 C  CG  . ARG A 1 424 ? 38.905 20.395 38.842  1.00 20.94 ? 424  ARG A CG  1 
ATOM   3370 C  CD  . ARG A 1 424 ? 38.555 21.863 38.929  1.00 29.79 ? 424  ARG A CD  1 
ATOM   3371 N  NE  . ARG A 1 424 ? 37.140 22.122 38.668  1.00 36.94 ? 424  ARG A NE  1 
ATOM   3372 C  CZ  . ARG A 1 424 ? 36.154 21.878 39.528  1.00 39.29 ? 424  ARG A CZ  1 
ATOM   3373 N  NH1 . ARG A 1 424 ? 36.414 21.346 40.718  1.00 43.21 ? 424  ARG A NH1 1 
ATOM   3374 N  NH2 . ARG A 1 424 ? 34.900 22.155 39.192  1.00 38.82 ? 424  ARG A NH2 1 
ATOM   3375 N  N   . GLY A 1 425 ? 39.346 17.156 35.262  1.00 11.01 ? 425  GLY A N   1 
ATOM   3376 C  CA  . GLY A 1 425 ? 38.835 16.529 34.059  1.00 5.63  ? 425  GLY A CA  1 
ATOM   3377 C  C   . GLY A 1 425 ? 39.866 15.695 33.339  1.00 9.70  ? 425  GLY A C   1 
ATOM   3378 O  O   . GLY A 1 425 ? 41.066 15.940 33.475  1.00 9.68  ? 425  GLY A O   1 
ATOM   3379 N  N   . PHE A 1 426 ? 39.393 14.724 32.557  1.00 9.28  ? 426  PHE A N   1 
ATOM   3380 C  CA  . PHE A 1 426 ? 40.251 13.821 31.797  1.00 9.91  ? 426  PHE A CA  1 
ATOM   3381 C  C   . PHE A 1 426 ? 39.472 13.393 30.554  1.00 10.17 ? 426  PHE A C   1 
ATOM   3382 O  O   . PHE A 1 426 ? 38.249 13.248 30.603  1.00 10.88 ? 426  PHE A O   1 
ATOM   3383 C  CB  . PHE A 1 426 ? 40.608 12.598 32.654  1.00 10.90 ? 426  PHE A CB  1 
ATOM   3384 C  CG  . PHE A 1 426 ? 41.660 11.698 32.050  1.00 10.17 ? 426  PHE A CG  1 
ATOM   3385 C  CD1 . PHE A 1 426 ? 43.010 12.042 32.105  1.00 9.13  ? 426  PHE A CD1 1 
ATOM   3386 C  CD2 . PHE A 1 426 ? 41.302 10.481 31.473  1.00 8.57  ? 426  PHE A CD2 1 
ATOM   3387 C  CE1 . PHE A 1 426 ? 43.990 11.183 31.595  1.00 8.17  ? 426  PHE A CE1 1 
ATOM   3388 C  CE2 . PHE A 1 426 ? 42.269 9.619  30.962  1.00 7.02  ? 426  PHE A CE2 1 
ATOM   3389 C  CZ  . PHE A 1 426 ? 43.617 9.971  31.025  1.00 9.78  ? 426  PHE A CZ  1 
ATOM   3390 N  N   . ILE A 1 427 ? 40.174 13.223 29.438  1.00 8.57  ? 427  ILE A N   1 
ATOM   3391 C  CA  . ILE A 1 427 ? 39.542 12.827 28.190  1.00 9.02  ? 427  ILE A CA  1 
ATOM   3392 C  C   . ILE A 1 427 ? 40.391 11.770 27.470  1.00 8.39  ? 427  ILE A C   1 
ATOM   3393 O  O   . ILE A 1 427 ? 41.619 11.837 27.486  1.00 9.54  ? 427  ILE A O   1 
ATOM   3394 C  CB  . ILE A 1 427 ? 39.286 14.074 27.291  1.00 11.16 ? 427  ILE A CB  1 
ATOM   3395 C  CG1 . ILE A 1 427 ? 38.507 13.678 26.037  1.00 9.79  ? 427  ILE A CG1 1 
ATOM   3396 C  CG2 . ILE A 1 427 ? 40.606 14.777 26.946  1.00 8.09  ? 427  ILE A CG2 1 
ATOM   3397 C  CD1 . ILE A 1 427 ? 37.802 14.840 25.380  1.00 11.43 ? 427  ILE A CD1 1 
ATOM   3398 N  N   . VAL A 1 428 ? 39.737 10.775 26.877  1.00 9.10  ? 428  VAL A N   1 
ATOM   3399 C  CA  . VAL A 1 428 ? 40.433 9.699  26.178  1.00 9.31  ? 428  VAL A CA  1 
ATOM   3400 C  C   . VAL A 1 428 ? 39.905 9.615  24.753  1.00 9.29  ? 428  VAL A C   1 
ATOM   3401 O  O   . VAL A 1 428 ? 38.701 9.714  24.538  1.00 11.57 ? 428  VAL A O   1 
ATOM   3402 C  CB  . VAL A 1 428 ? 40.188 8.335  26.868  1.00 9.44  ? 428  VAL A CB  1 
ATOM   3403 C  CG1 . VAL A 1 428 ? 41.204 7.314  26.389  1.00 8.12  ? 428  VAL A CG1 1 
ATOM   3404 C  CG2 . VAL A 1 428 ? 40.255 8.479  28.368  1.00 8.15  ? 428  VAL A CG2 1 
ATOM   3405 N  N   . PHE A 1 429 ? 40.798 9.365  23.801  1.00 11.25 ? 429  PHE A N   1 
ATOM   3406 C  CA  . PHE A 1 429 ? 40.455 9.272  22.381  1.00 10.72 ? 429  PHE A CA  1 
ATOM   3407 C  C   . PHE A 1 429 ? 41.013 7.993  21.754  1.00 12.82 ? 429  PHE A C   1 
ATOM   3408 O  O   . PHE A 1 429 ? 42.135 7.582  22.064  1.00 10.66 ? 429  PHE A O   1 
ATOM   3409 C  CB  . PHE A 1 429 ? 41.091 10.431 21.590  1.00 8.58  ? 429  PHE A CB  1 
ATOM   3410 C  CG  . PHE A 1 429 ? 40.565 11.789 21.937  1.00 8.44  ? 429  PHE A CG  1 
ATOM   3411 C  CD1 . PHE A 1 429 ? 39.443 12.300 21.288  1.00 8.37  ? 429  PHE A CD1 1 
ATOM   3412 C  CD2 . PHE A 1 429 ? 41.203 12.569 22.897  1.00 7.70  ? 429  PHE A CD2 1 
ATOM   3413 C  CE1 . PHE A 1 429 ? 38.965 13.566 21.595  1.00 7.95  ? 429  PHE A CE1 1 
ATOM   3414 C  CE2 . PHE A 1 429 ? 40.736 13.830 23.210  1.00 8.37  ? 429  PHE A CE2 1 
ATOM   3415 C  CZ  . PHE A 1 429 ? 39.609 14.331 22.557  1.00 10.32 ? 429  PHE A CZ  1 
ATOM   3416 N  N   . ASN A 1 430 ? 40.256 7.405  20.831  1.00 12.53 ? 430  ASN A N   1 
ATOM   3417 C  CA  . ASN A 1 430 ? 40.713 6.226  20.101  1.00 11.09 ? 430  ASN A CA  1 
ATOM   3418 C  C   . ASN A 1 430 ? 40.404 6.461  18.634  1.00 11.48 ? 430  ASN A C   1 
ATOM   3419 O  O   . ASN A 1 430 ? 39.260 6.289  18.200  1.00 13.30 ? 430  ASN A O   1 
ATOM   3420 C  CB  . ASN A 1 430 ? 40.023 4.940  20.550  1.00 11.05 ? 430  ASN A CB  1 
ATOM   3421 C  CG  . ASN A 1 430 ? 40.475 3.728  19.737  1.00 10.36 ? 430  ASN A CG  1 
ATOM   3422 O  OD1 . ASN A 1 430 ? 41.512 3.770  19.053  1.00 10.17 ? 430  ASN A OD1 1 
ATOM   3423 N  ND2 . ASN A 1 430 ? 39.707 2.650  19.802  1.00 10.53 ? 430  ASN A ND2 1 
ATOM   3424 N  N   . ASN A 1 431 ? 41.410 6.889  17.876  1.00 12.25 ? 431  ASN A N   1 
ATOM   3425 C  CA  . ASN A 1 431 ? 41.228 7.137  16.449  1.00 12.97 ? 431  ASN A CA  1 
ATOM   3426 C  C   . ASN A 1 431 ? 42.023 6.116  15.630  1.00 12.99 ? 431  ASN A C   1 
ATOM   3427 O  O   . ASN A 1 431 ? 42.304 6.327  14.452  1.00 12.51 ? 431  ASN A O   1 
ATOM   3428 C  CB  . ASN A 1 431 ? 41.641 8.568  16.094  1.00 12.38 ? 431  ASN A CB  1 
ATOM   3429 C  CG  . ASN A 1 431 ? 41.024 9.056  14.789  1.00 15.29 ? 431  ASN A CG  1 
ATOM   3430 O  OD1 . ASN A 1 431 ? 39.943 8.614  14.387  1.00 14.91 ? 431  ASN A OD1 1 
ATOM   3431 N  ND2 . ASN A 1 431 ? 41.700 9.987  14.135  1.00 12.85 ? 431  ASN A ND2 1 
ATOM   3432 N  N   . ASP A 1 432 ? 42.415 5.023  16.278  1.00 16.62 ? 432  ASP A N   1 
ATOM   3433 C  CA  . ASP A 1 432 ? 43.149 3.958  15.606  1.00 18.00 ? 432  ASP A CA  1 
ATOM   3434 C  C   . ASP A 1 432 ? 42.160 2.917  15.106  1.00 18.89 ? 432  ASP A C   1 
ATOM   3435 O  O   . ASP A 1 432 ? 41.016 2.875  15.548  1.00 18.88 ? 432  ASP A O   1 
ATOM   3436 C  CB  . ASP A 1 432 ? 44.132 3.287  16.558  1.00 13.49 ? 432  ASP A CB  1 
ATOM   3437 C  CG  . ASP A 1 432 ? 45.496 3.921  16.527  1.00 14.33 ? 432  ASP A CG  1 
ATOM   3438 O  OD1 . ASP A 1 432 ? 46.009 4.187  15.417  1.00 18.44 ? 432  ASP A OD1 1 
ATOM   3439 O  OD2 . ASP A 1 432 ? 46.072 4.136  17.616  1.00 13.12 ? 432  ASP A OD2 1 
ATOM   3440 N  N   . ASP A 1 433 ? 42.614 2.056  14.205  1.00 24.71 ? 433  ASP A N   1 
ATOM   3441 C  CA  . ASP A 1 433 ? 41.758 1.010  13.660  1.00 31.46 ? 433  ASP A CA  1 
ATOM   3442 C  C   . ASP A 1 433 ? 41.707 -0.252 14.516  1.00 28.89 ? 433  ASP A C   1 
ATOM   3443 O  O   . ASP A 1 433 ? 41.527 -1.351 13.997  1.00 29.74 ? 433  ASP A O   1 
ATOM   3444 C  CB  . ASP A 1 433 ? 42.168 0.671  12.227  1.00 36.50 ? 433  ASP A CB  1 
ATOM   3445 C  CG  . ASP A 1 433 ? 41.876 1.800  11.261  1.00 43.31 ? 433  ASP A CG  1 
ATOM   3446 O  OD1 . ASP A 1 433 ? 40.758 2.365  11.329  1.00 47.73 ? 433  ASP A OD1 1 
ATOM   3447 O  OD2 . ASP A 1 433 ? 42.760 2.125  10.438  1.00 48.41 ? 433  ASP A OD2 1 
ATOM   3448 N  N   . TRP A 1 434 ? 41.871 -0.092 15.826  1.00 26.96 ? 434  TRP A N   1 
ATOM   3449 C  CA  . TRP A 1 434 ? 41.811 -1.214 16.755  1.00 23.26 ? 434  TRP A CA  1 
ATOM   3450 C  C   . TRP A 1 434 ? 41.348 -0.783 18.143  1.00 23.39 ? 434  TRP A C   1 
ATOM   3451 O  O   . TRP A 1 434 ? 41.220 0.409  18.438  1.00 27.06 ? 434  TRP A O   1 
ATOM   3452 C  CB  . TRP A 1 434 ? 43.138 -1.980 16.824  1.00 19.69 ? 434  TRP A CB  1 
ATOM   3453 C  CG  . TRP A 1 434 ? 44.322 -1.189 17.276  1.00 18.73 ? 434  TRP A CG  1 
ATOM   3454 C  CD1 . TRP A 1 434 ? 44.747 -0.999 18.565  1.00 17.25 ? 434  TRP A CD1 1 
ATOM   3455 C  CD2 . TRP A 1 434 ? 45.257 -0.501 16.439  1.00 16.09 ? 434  TRP A CD2 1 
ATOM   3456 N  NE1 . TRP A 1 434 ? 45.890 -0.234 18.578  1.00 14.86 ? 434  TRP A NE1 1 
ATOM   3457 C  CE2 . TRP A 1 434 ? 46.225 0.086  17.289  1.00 14.61 ? 434  TRP A CE2 1 
ATOM   3458 C  CE3 . TRP A 1 434 ? 45.375 -0.324 15.055  1.00 17.30 ? 434  TRP A CE3 1 
ATOM   3459 C  CZ2 . TRP A 1 434 ? 47.297 0.838  16.797  1.00 13.71 ? 434  TRP A CZ2 1 
ATOM   3460 C  CZ3 . TRP A 1 434 ? 46.442 0.424  14.567  1.00 17.13 ? 434  TRP A CZ3 1 
ATOM   3461 C  CH2 . TRP A 1 434 ? 47.388 0.996  15.438  1.00 14.78 ? 434  TRP A CH2 1 
ATOM   3462 N  N   . GLN A 1 435 ? 41.080 -1.770 18.981  1.00 20.00 ? 435  GLN A N   1 
ATOM   3463 C  CA  . GLN A 1 435 ? 40.591 -1.558 20.330  1.00 20.00 ? 435  GLN A CA  1 
ATOM   3464 C  C   . GLN A 1 435 ? 41.544 -0.836 21.277  1.00 20.00 ? 435  GLN A C   1 
ATOM   3465 O  O   . GLN A 1 435 ? 42.768 -1.014 21.218  1.00 20.00 ? 435  GLN A O   1 
ATOM   3466 C  CB  . GLN A 1 435 ? 40.231 -2.932 20.968  1.00 20.00 ? 435  GLN A CB  1 
ATOM   3467 C  CG  . GLN A 1 435 ? 39.642 -2.823 22.375  1.00 20.00 ? 435  GLN A CG  1 
ATOM   3468 C  CD  . GLN A 1 435 ? 38.135 -2.558 22.372  1.00 20.00 ? 435  GLN A CD  1 
ATOM   3469 O  OE1 . GLN A 1 435 ? 37.689 -1.542 22.900  1.00 20.00 ? 435  GLN A OE1 1 
ATOM   3470 N  NE2 . GLN A 1 435 ? 37.314 -3.419 21.799  1.00 20.00 ? 435  GLN A NE2 1 
ATOM   3471 N  N   . LEU A 1 436 ? 40.962 -0.010 22.141  1.00 15.73 ? 436  LEU A N   1 
ATOM   3472 C  CA  . LEU A 1 436 ? 41.704 0.701  23.168  1.00 14.48 ? 436  LEU A CA  1 
ATOM   3473 C  C   . LEU A 1 436 ? 41.182 0.090  24.465  1.00 15.19 ? 436  LEU A C   1 
ATOM   3474 O  O   . LEU A 1 436 ? 39.975 0.084  24.711  1.00 14.54 ? 436  LEU A O   1 
ATOM   3475 C  CB  . LEU A 1 436 ? 41.401 2.207  23.147  1.00 13.53 ? 436  LEU A CB  1 
ATOM   3476 C  CG  . LEU A 1 436 ? 42.118 3.097  24.182  1.00 14.24 ? 436  LEU A CG  1 
ATOM   3477 C  CD1 . LEU A 1 436 ? 42.217 4.522  23.668  1.00 18.44 ? 436  LEU A CD1 1 
ATOM   3478 C  CD2 . LEU A 1 436 ? 41.410 3.093  25.523  1.00 15.66 ? 436  LEU A CD2 1 
ATOM   3479 N  N   . SER A 1 437 ? 42.080 -0.458 25.269  1.00 14.91 ? 437  SER A N   1 
ATOM   3480 C  CA  . SER A 1 437 ? 41.714 -1.054 26.546  1.00 17.09 ? 437  SER A CA  1 
ATOM   3481 C  C   . SER A 1 437 ? 42.932 -0.857 27.432  1.00 16.84 ? 437  SER A C   1 
ATOM   3482 O  O   . SER A 1 437 ? 43.907 -1.600 27.328  1.00 21.16 ? 437  SER A O   1 
ATOM   3483 C  CB  . SER A 1 437 ? 41.400 -2.546 26.376  1.00 17.73 ? 437  SER A CB  1 
ATOM   3484 O  OG  . SER A 1 437 ? 40.823 -3.101 27.551  1.00 23.47 ? 437  SER A OG  1 
ATOM   3485 N  N   . SER A 1 438 ? 42.903 0.179  28.261  1.00 16.55 ? 438  SER A N   1 
ATOM   3486 C  CA  . SER A 1 438 ? 44.031 0.456  29.133  1.00 14.84 ? 438  SER A CA  1 
ATOM   3487 C  C   . SER A 1 438 ? 43.631 1.080  30.442  1.00 13.24 ? 438  SER A C   1 
ATOM   3488 O  O   . SER A 1 438 ? 42.554 1.657  30.561  1.00 18.54 ? 438  SER A O   1 
ATOM   3489 C  CB  . SER A 1 438 ? 45.029 1.386  28.440  1.00 17.68 ? 438  SER A CB  1 
ATOM   3490 O  OG  . SER A 1 438 ? 45.673 0.737  27.361  1.00 26.39 ? 438  SER A OG  1 
ATOM   3491 N  N   . THR A 1 439 ? 44.497 0.926  31.434  1.00 10.94 ? 439  THR A N   1 
ATOM   3492 C  CA  . THR A 1 439 ? 44.279 1.515  32.737  1.00 15.84 ? 439  THR A CA  1 
ATOM   3493 C  C   . THR A 1 439 ? 45.168 2.752  32.724  1.00 16.61 ? 439  THR A C   1 
ATOM   3494 O  O   . THR A 1 439 ? 46.391 2.633  32.678  1.00 21.50 ? 439  THR A O   1 
ATOM   3495 C  CB  . THR A 1 439 ? 44.707 0.550  33.846  1.00 12.36 ? 439  THR A CB  1 
ATOM   3496 O  OG1 . THR A 1 439 ? 43.863 -0.605 33.810  1.00 15.46 ? 439  THR A OG1 1 
ATOM   3497 C  CG2 . THR A 1 439 ? 44.600 1.205  35.211  1.00 11.97 ? 439  THR A CG2 1 
ATOM   3498 N  N   . LEU A 1 440 ? 44.550 3.929  32.696  1.00 17.31 ? 440  LEU A N   1 
ATOM   3499 C  CA  . LEU A 1 440 ? 45.285 5.192  32.645  1.00 12.47 ? 440  LEU A CA  1 
ATOM   3500 C  C   . LEU A 1 440 ? 45.159 6.018  33.918  1.00 10.96 ? 440  LEU A C   1 
ATOM   3501 O  O   . LEU A 1 440 ? 44.187 5.886  34.664  1.00 12.62 ? 440  LEU A O   1 
ATOM   3502 C  CB  . LEU A 1 440 ? 44.792 6.028  31.465  1.00 7.42  ? 440  LEU A CB  1 
ATOM   3503 C  CG  . LEU A 1 440 ? 44.794 5.325  30.110  1.00 11.06 ? 440  LEU A CG  1 
ATOM   3504 C  CD1 . LEU A 1 440 ? 44.107 6.194  29.076  1.00 11.60 ? 440  LEU A CD1 1 
ATOM   3505 C  CD2 . LEU A 1 440 ? 46.222 5.014  29.699  1.00 7.58  ? 440  LEU A CD2 1 
ATOM   3506 N  N   . GLN A 1 441 ? 46.166 6.848  34.172  1.00 12.51 ? 441  GLN A N   1 
ATOM   3507 C  CA  . GLN A 1 441 ? 46.174 7.738  35.327  1.00 11.52 ? 441  GLN A CA  1 
ATOM   3508 C  C   . GLN A 1 441 ? 45.372 8.958  34.895  1.00 13.86 ? 441  GLN A C   1 
ATOM   3509 O  O   . GLN A 1 441 ? 45.749 9.653  33.945  1.00 12.78 ? 441  GLN A O   1 
ATOM   3510 C  CB  . GLN A 1 441 ? 47.609 8.147  35.681  1.00 9.41  ? 441  GLN A CB  1 
ATOM   3511 C  CG  . GLN A 1 441 ? 47.711 9.248  36.739  1.00 10.62 ? 441  GLN A CG  1 
ATOM   3512 C  CD  . GLN A 1 441 ? 47.022 8.892  38.046  1.00 15.01 ? 441  GLN A CD  1 
ATOM   3513 O  OE1 . GLN A 1 441 ? 46.079 9.568  38.474  1.00 15.96 ? 441  GLN A OE1 1 
ATOM   3514 N  NE2 . GLN A 1 441 ? 47.481 7.827  38.684  1.00 12.86 ? 441  GLN A NE2 1 
ATOM   3515 N  N   . THR A 1 442 ? 44.255 9.200  35.572  1.00 13.95 ? 442  THR A N   1 
ATOM   3516 C  CA  . THR A 1 442 ? 43.395 10.321 35.227  1.00 14.13 ? 442  THR A CA  1 
ATOM   3517 C  C   . THR A 1 442 ? 43.731 11.608 35.973  1.00 17.87 ? 442  THR A C   1 
ATOM   3518 O  O   . THR A 1 442 ? 43.403 12.703 35.515  1.00 24.29 ? 442  THR A O   1 
ATOM   3519 C  CB  . THR A 1 442 ? 41.926 9.982  35.484  1.00 8.06  ? 442  THR A CB  1 
ATOM   3520 O  OG1 . THR A 1 442 ? 41.705 9.847  36.894  1.00 10.79 ? 442  THR A OG1 1 
ATOM   3521 C  CG2 . THR A 1 442 ? 41.562 8.692  34.793  1.00 9.33  ? 442  THR A CG2 1 
ATOM   3522 N  N   . GLY A 1 443 ? 44.376 11.473 37.125  1.00 16.98 ? 443  GLY A N   1 
ATOM   3523 C  CA  . GLY A 1 443 ? 44.708 12.633 37.925  1.00 13.92 ? 443  GLY A CA  1 
ATOM   3524 C  C   . GLY A 1 443 ? 43.487 13.112 38.694  1.00 15.77 ? 443  GLY A C   1 
ATOM   3525 O  O   . GLY A 1 443 ? 43.534 14.138 39.373  1.00 19.07 ? 443  GLY A O   1 
ATOM   3526 N  N   . LEU A 1 444 ? 42.387 12.371 38.586  1.00 17.29 ? 444  LEU A N   1 
ATOM   3527 C  CA  . LEU A 1 444 ? 41.143 12.717 39.262  1.00 16.94 ? 444  LEU A CA  1 
ATOM   3528 C  C   . LEU A 1 444 ? 40.976 11.921 40.549  1.00 15.67 ? 444  LEU A C   1 
ATOM   3529 O  O   . LEU A 1 444 ? 41.558 10.850 40.704  1.00 17.91 ? 444  LEU A O   1 
ATOM   3530 C  CB  . LEU A 1 444 ? 39.950 12.454 38.340  1.00 18.94 ? 444  LEU A CB  1 
ATOM   3531 C  CG  . LEU A 1 444 ? 39.545 13.519 37.317  1.00 21.67 ? 444  LEU A CG  1 
ATOM   3532 C  CD1 . LEU A 1 444 ? 40.756 14.112 36.612  1.00 27.39 ? 444  LEU A CD1 1 
ATOM   3533 C  CD2 . LEU A 1 444 ? 38.597 12.901 36.310  1.00 22.43 ? 444  LEU A CD2 1 
ATOM   3534 N  N   . PRO A 1 445 ? 40.260 12.487 41.528  1.00 17.23 ? 445  PRO A N   1 
ATOM   3535 C  CA  . PRO A 1 445 ? 40.045 11.780 42.794  1.00 16.57 ? 445  PRO A CA  1 
ATOM   3536 C  C   . PRO A 1 445 ? 39.147 10.559 42.572  1.00 17.21 ? 445  PRO A C   1 
ATOM   3537 O  O   . PRO A 1 445 ? 38.338 10.537 41.642  1.00 17.58 ? 445  PRO A O   1 
ATOM   3538 C  CB  . PRO A 1 445 ? 39.387 12.849 43.678  1.00 15.24 ? 445  PRO A CB  1 
ATOM   3539 C  CG  . PRO A 1 445 ? 38.718 13.761 42.702  1.00 15.48 ? 445  PRO A CG  1 
ATOM   3540 C  CD  . PRO A 1 445 ? 39.718 13.856 41.582  1.00 14.85 ? 445  PRO A CD  1 
ATOM   3541 N  N   . GLY A 1 446 ? 39.310 9.543  43.415  1.00 13.91 ? 446  GLY A N   1 
ATOM   3542 C  CA  . GLY A 1 446 ? 38.531 8.325  43.277  1.00 12.58 ? 446  GLY A CA  1 
ATOM   3543 C  C   . GLY A 1 446 ? 37.026 8.518  43.281  1.00 11.35 ? 446  GLY A C   1 
ATOM   3544 O  O   . GLY A 1 446 ? 36.508 9.406  43.957  1.00 19.63 ? 446  GLY A O   1 
ATOM   3545 N  N   . GLY A 1 447 ? 36.320 7.678  42.533  1.00 10.94 ? 447  GLY A N   1 
ATOM   3546 C  CA  . GLY A 1 447 ? 34.872 7.767  42.484  1.00 9.98  ? 447  GLY A CA  1 
ATOM   3547 C  C   . GLY A 1 447 ? 34.327 7.260  41.168  1.00 12.08 ? 447  GLY A C   1 
ATOM   3548 O  O   . GLY A 1 447 ? 35.086 6.786  40.320  1.00 16.01 ? 447  GLY A O   1 
ATOM   3549 N  N   . THR A 1 448 ? 33.016 7.349  40.990  1.00 13.95 ? 448  THR A N   1 
ATOM   3550 C  CA  . THR A 1 448 ? 32.395 6.900  39.756  1.00 15.61 ? 448  THR A CA  1 
ATOM   3551 C  C   . THR A 1 448 ? 31.948 8.123  38.962  1.00 16.03 ? 448  THR A C   1 
ATOM   3552 O  O   . THR A 1 448 ? 31.212 8.964  39.470  1.00 14.92 ? 448  THR A O   1 
ATOM   3553 C  CB  . THR A 1 448 ? 31.211 5.984  40.055  1.00 16.10 ? 448  THR A CB  1 
ATOM   3554 O  OG1 . THR A 1 448 ? 31.658 4.923  40.910  1.00 20.98 ? 448  THR A OG1 1 
ATOM   3555 C  CG2 . THR A 1 448 ? 30.654 5.394  38.773  1.00 11.29 ? 448  THR A CG2 1 
ATOM   3556 N  N   . TYR A 1 449 ? 32.443 8.244  37.735  1.00 15.80 ? 449  TYR A N   1 
ATOM   3557 C  CA  . TYR A 1 449 ? 32.126 9.376  36.878  1.00 13.75 ? 449  TYR A CA  1 
ATOM   3558 C  C   . TYR A 1 449 ? 31.294 8.992  35.666  1.00 17.31 ? 449  TYR A C   1 
ATOM   3559 O  O   . TYR A 1 449 ? 31.505 7.938  35.069  1.00 18.41 ? 449  TYR A O   1 
ATOM   3560 C  CB  . TYR A 1 449 ? 33.419 10.029 36.382  1.00 14.28 ? 449  TYR A CB  1 
ATOM   3561 C  CG  . TYR A 1 449 ? 34.310 10.597 37.465  1.00 13.06 ? 449  TYR A CG  1 
ATOM   3562 C  CD1 . TYR A 1 449 ? 35.071 9.761  38.291  1.00 10.64 ? 449  TYR A CD1 1 
ATOM   3563 C  CD2 . TYR A 1 449 ? 34.409 11.974 37.653  1.00 10.56 ? 449  TYR A CD2 1 
ATOM   3564 C  CE1 . TYR A 1 449 ? 35.905 10.287 39.273  1.00 8.12  ? 449  TYR A CE1 1 
ATOM   3565 C  CE2 . TYR A 1 449 ? 35.240 12.506 38.626  1.00 10.51 ? 449  TYR A CE2 1 
ATOM   3566 C  CZ  . TYR A 1 449 ? 35.983 11.660 39.430  1.00 10.39 ? 449  TYR A CZ  1 
ATOM   3567 O  OH  . TYR A 1 449 ? 36.810 12.201 40.379  1.00 14.77 ? 449  TYR A OH  1 
ATOM   3568 N  N   . CYS A 1 450 ? 30.353 9.855  35.299  1.00 17.62 ? 450  CYS A N   1 
ATOM   3569 C  CA  . CYS A 1 450 ? 29.527 9.620  34.125  1.00 18.49 ? 450  CYS A CA  1 
ATOM   3570 C  C   . CYS A 1 450 ? 30.303 10.150 32.926  1.00 18.89 ? 450  CYS A C   1 
ATOM   3571 O  O   . CYS A 1 450 ? 30.910 11.223 32.992  1.00 19.19 ? 450  CYS A O   1 
ATOM   3572 C  CB  . CYS A 1 450 ? 28.201 10.385 34.202  1.00 19.40 ? 450  CYS A CB  1 
ATOM   3573 S  SG  . CYS A 1 450 ? 27.099 9.980  35.591  1.00 22.33 ? 450  CYS A SG  1 
ATOM   3574 N  N   . ASP A 1 451 ? 30.334 9.377  31.852  1.00 15.65 ? 451  ASP A N   1 
ATOM   3575 C  CA  . ASP A 1 451 ? 31.003 9.807  30.640  1.00 13.92 ? 451  ASP A CA  1 
ATOM   3576 C  C   . ASP A 1 451 ? 30.021 10.799 30.024  1.00 16.06 ? 451  ASP A C   1 
ATOM   3577 O  O   . ASP A 1 451 ? 28.863 10.438 29.789  1.00 17.70 ? 451  ASP A O   1 
ATOM   3578 C  CB  . ASP A 1 451 ? 31.214 8.606  29.716  1.00 11.08 ? 451  ASP A CB  1 
ATOM   3579 C  CG  . ASP A 1 451 ? 31.549 9.007  28.296  1.00 12.43 ? 451  ASP A CG  1 
ATOM   3580 O  OD1 . ASP A 1 451 ? 32.341 9.949  28.099  1.00 13.88 ? 451  ASP A OD1 1 
ATOM   3581 O  OD2 . ASP A 1 451 ? 31.015 8.378  27.365  1.00 14.18 ? 451  ASP A OD2 1 
ATOM   3582 N  N   . VAL A 1 452 ? 30.460 12.043 29.804  1.00 13.84 ? 452  VAL A N   1 
ATOM   3583 C  CA  . VAL A 1 452 ? 29.588 13.076 29.232  1.00 9.88  ? 452  VAL A CA  1 
ATOM   3584 C  C   . VAL A 1 452 ? 29.483 13.041 27.713  1.00 11.60 ? 452  VAL A C   1 
ATOM   3585 O  O   . VAL A 1 452 ? 28.767 13.843 27.116  1.00 14.34 ? 452  VAL A O   1 
ATOM   3586 C  CB  . VAL A 1 452 ? 29.975 14.507 29.683  1.00 9.92  ? 452  VAL A CB  1 
ATOM   3587 C  CG1 . VAL A 1 452 ? 29.835 14.634 31.187  1.00 10.49 ? 452  VAL A CG1 1 
ATOM   3588 C  CG2 . VAL A 1 452 ? 31.388 14.859 29.230  1.00 8.21  ? 452  VAL A CG2 1 
ATOM   3589 N  N   . ILE A 1 453 ? 30.219 12.136 27.081  1.00 11.47 ? 453  ILE A N   1 
ATOM   3590 C  CA  . ILE A 1 453 ? 30.149 12.009 25.636  1.00 13.21 ? 453  ILE A CA  1 
ATOM   3591 C  C   . ILE A 1 453 ? 29.013 11.049 25.262  1.00 13.61 ? 453  ILE A C   1 
ATOM   3592 O  O   . ILE A 1 453 ? 28.231 11.341 24.366  1.00 13.65 ? 453  ILE A O   1 
ATOM   3593 C  CB  . ILE A 1 453 ? 31.500 11.535 25.035  1.00 11.12 ? 453  ILE A CB  1 
ATOM   3594 C  CG1 . ILE A 1 453 ? 32.585 12.576 25.313  1.00 12.49 ? 453  ILE A CG1 1 
ATOM   3595 C  CG2 . ILE A 1 453 ? 31.374 11.322 23.534  1.00 6.71  ? 453  ILE A CG2 1 
ATOM   3596 C  CD1 . ILE A 1 453 ? 32.215 13.985 24.877  1.00 10.85 ? 453  ILE A CD1 1 
ATOM   3597 N  N   . SER A 1 454 ? 28.903 9.923  25.969  1.00 13.55 ? 454  SER A N   1 
ATOM   3598 C  CA  . SER A 1 454 ? 27.849 8.943  25.685  1.00 14.26 ? 454  SER A CA  1 
ATOM   3599 C  C   . SER A 1 454 ? 26.557 9.215  26.440  1.00 12.37 ? 454  SER A C   1 
ATOM   3600 O  O   . SER A 1 454 ? 25.501 8.705  26.067  1.00 19.22 ? 454  SER A O   1 
ATOM   3601 C  CB  . SER A 1 454 ? 28.314 7.528  26.020  1.00 12.37 ? 454  SER A CB  1 
ATOM   3602 O  OG  . SER A 1 454 ? 28.488 7.371  27.421  1.00 14.89 ? 454  SER A OG  1 
ATOM   3603 N  N   . GLY A 1 455 ? 26.642 9.984  27.518  1.00 9.76  ? 455  GLY A N   1 
ATOM   3604 C  CA  . GLY A 1 455 ? 25.451 10.273 28.286  1.00 9.85  ? 455  GLY A CA  1 
ATOM   3605 C  C   . GLY A 1 455 ? 25.588 11.501 29.147  1.00 13.67 ? 455  GLY A C   1 
ATOM   3606 O  O   . GLY A 1 455 ? 26.447 12.348 28.912  1.00 12.48 ? 455  GLY A O   1 
ATOM   3607 N  N   . ASP A 1 456 ? 24.736 11.577 30.161  1.00 15.86 ? 456  ASP A N   1 
ATOM   3608 C  CA  . ASP A 1 456 ? 24.712 12.689 31.093  1.00 18.36 ? 456  ASP A CA  1 
ATOM   3609 C  C   . ASP A 1 456 ? 24.517 12.134 32.487  1.00 20.86 ? 456  ASP A C   1 
ATOM   3610 O  O   . ASP A 1 456 ? 24.143 10.970 32.661  1.00 16.93 ? 456  ASP A O   1 
ATOM   3611 C  CB  . ASP A 1 456 ? 23.528 13.614 30.795  1.00 24.02 ? 456  ASP A CB  1 
ATOM   3612 C  CG  . ASP A 1 456 ? 23.711 14.424 29.530  1.00 30.67 ? 456  ASP A CG  1 
ATOM   3613 O  OD1 . ASP A 1 456 ? 24.458 15.425 29.568  1.00 35.64 ? 456  ASP A OD1 1 
ATOM   3614 O  OD2 . ASP A 1 456 ? 23.082 14.079 28.507  1.00 31.99 ? 456  ASP A OD2 1 
ATOM   3615 N  N   . LYS A 1 457 ? 24.763 12.975 33.485  1.00 24.29 ? 457  LYS A N   1 
ATOM   3616 C  CA  . LYS A 1 457 ? 24.565 12.586 34.870  1.00 29.73 ? 457  LYS A CA  1 
ATOM   3617 C  C   . LYS A 1 457 ? 23.186 13.104 35.245  1.00 35.66 ? 457  LYS A C   1 
ATOM   3618 O  O   . LYS A 1 457 ? 22.967 14.318 35.289  1.00 38.26 ? 457  LYS A O   1 
ATOM   3619 C  CB  . LYS A 1 457 ? 25.598 13.237 35.787  1.00 25.91 ? 457  LYS A CB  1 
ATOM   3620 C  CG  . LYS A 1 457 ? 25.371 12.896 37.254  1.00 25.85 ? 457  LYS A CG  1 
ATOM   3621 C  CD  . LYS A 1 457 ? 26.131 13.818 38.179  1.00 24.56 ? 457  LYS A CD  1 
ATOM   3622 C  CE  . LYS A 1 457 ? 25.719 13.566 39.608  1.00 28.66 ? 457  LYS A CE  1 
ATOM   3623 N  NZ  . LYS A 1 457 ? 26.277 14.591 40.524  1.00 33.59 ? 457  LYS A NZ  1 
ATOM   3624 N  N   . VAL A 1 458 ? 22.239 12.196 35.438  1.00 40.71 ? 458  VAL A N   1 
ATOM   3625 C  CA  . VAL A 1 458 ? 20.890 12.590 35.819  1.00 45.33 ? 458  VAL A CA  1 
ATOM   3626 C  C   . VAL A 1 458 ? 20.650 12.215 37.279  1.00 47.56 ? 458  VAL A C   1 
ATOM   3627 O  O   . VAL A 1 458 ? 20.617 11.033 37.641  1.00 49.04 ? 458  VAL A O   1 
ATOM   3628 C  CB  . VAL A 1 458 ? 19.814 11.954 34.901  1.00 47.24 ? 458  VAL A CB  1 
ATOM   3629 C  CG1 . VAL A 1 458 ? 19.944 12.500 33.485  1.00 46.65 ? 458  VAL A CG1 1 
ATOM   3630 C  CG2 . VAL A 1 458 ? 19.941 10.433 34.890  1.00 52.04 ? 458  VAL A CG2 1 
ATOM   3631 N  N   . GLY A 1 459 ? 20.542 13.233 38.125  1.00 50.17 ? 459  GLY A N   1 
ATOM   3632 C  CA  . GLY A 1 459 ? 20.318 12.999 39.538  1.00 50.13 ? 459  GLY A CA  1 
ATOM   3633 C  C   . GLY A 1 459 ? 21.519 12.314 40.154  1.00 50.25 ? 459  GLY A C   1 
ATOM   3634 O  O   . GLY A 1 459 ? 22.523 12.955 40.447  1.00 52.65 ? 459  GLY A O   1 
ATOM   3635 N  N   . ASN A 1 460 ? 21.429 11.001 40.312  1.00 50.62 ? 460  ASN A N   1 
ATOM   3636 C  CA  . ASN A 1 460 ? 22.513 10.225 40.892  1.00 53.73 ? 460  ASN A CA  1 
ATOM   3637 C  C   . ASN A 1 460 ? 22.752 8.992  40.042  1.00 50.94 ? 460  ASN A C   1 
ATOM   3638 O  O   . ASN A 1 460 ? 23.085 7.917  40.545  1.00 49.93 ? 460  ASN A O   1 
ATOM   3639 C  CB  . ASN A 1 460 ? 22.181 9.830  42.336  1.00 62.20 ? 460  ASN A CB  1 
ATOM   3640 C  CG  . ASN A 1 460 ? 20.853 9.096  42.454  1.00 68.53 ? 460  ASN A CG  1 
ATOM   3641 O  OD1 . ASN A 1 460 ? 20.810 7.866  42.522  1.00 71.77 ? 460  ASN A OD1 1 
ATOM   3642 N  ND2 . ASN A 1 460 ? 19.758 9.853  42.489  1.00 72.07 ? 460  ASN A ND2 1 
ATOM   3643 N  N   . SER A 1 461 ? 22.597 9.163  38.738  1.00 48.22 ? 461  SER A N   1 
ATOM   3644 C  CA  . SER A 1 461 ? 22.791 8.069  37.805  1.00 44.96 ? 461  SER A CA  1 
ATOM   3645 C  C   . SER A 1 461 ? 23.377 8.610  36.509  1.00 38.45 ? 461  SER A C   1 
ATOM   3646 O  O   . SER A 1 461 ? 23.290 9.807  36.223  1.00 37.70 ? 461  SER A O   1 
ATOM   3647 C  CB  . SER A 1 461 ? 21.451 7.387  37.522  1.00 49.23 ? 461  SER A CB  1 
ATOM   3648 O  OG  . SER A 1 461 ? 21.607 6.270  36.660  1.00 57.57 ? 461  SER A OG  1 
ATOM   3649 N  N   . CYS A 1 462 ? 24.015 7.727  35.758  1.00 29.93 ? 462  CYS A N   1 
ATOM   3650 C  CA  . CYS A 1 462 ? 24.604 8.078  34.482  1.00 25.94 ? 462  CYS A CA  1 
ATOM   3651 C  C   . CYS A 1 462 ? 23.696 7.475  33.426  1.00 26.03 ? 462  CYS A C   1 
ATOM   3652 O  O   . CYS A 1 462 ? 23.153 6.395  33.628  1.00 30.69 ? 462  CYS A O   1 
ATOM   3653 C  CB  . CYS A 1 462 ? 25.995 7.464  34.357  1.00 21.67 ? 462  CYS A CB  1 
ATOM   3654 S  SG  . CYS A 1 462 ? 27.147 7.961  35.670  1.00 22.12 ? 462  CYS A SG  1 
ATOM   3655 N  N   . THR A 1 463 ? 23.493 8.180  32.323  1.00 24.07 ? 463  THR A N   1 
ATOM   3656 C  CA  . THR A 1 463 ? 22.650 7.657  31.262  1.00 22.66 ? 463  THR A CA  1 
ATOM   3657 C  C   . THR A 1 463 ? 23.502 6.936  30.223  1.00 22.95 ? 463  THR A C   1 
ATOM   3658 O  O   . THR A 1 463 ? 22.977 6.263  29.335  1.00 28.08 ? 463  THR A O   1 
ATOM   3659 C  CB  . THR A 1 463 ? 21.804 8.765  30.596  1.00 21.38 ? 463  THR A CB  1 
ATOM   3660 O  OG1 . THR A 1 463 ? 22.662 9.763  30.037  1.00 26.08 ? 463  THR A OG1 1 
ATOM   3661 C  CG2 . THR A 1 463 ? 20.901 9.417  31.620  1.00 19.52 ? 463  THR A CG2 1 
ATOM   3662 N  N   . GLY A 1 464 ? 24.819 7.075  30.342  1.00 22.28 ? 464  GLY A N   1 
ATOM   3663 C  CA  . GLY A 1 464 ? 25.724 6.420  29.414  1.00 19.86 ? 464  GLY A CA  1 
ATOM   3664 C  C   . GLY A 1 464 ? 26.779 5.618  30.154  1.00 19.21 ? 464  GLY A C   1 
ATOM   3665 O  O   . GLY A 1 464 ? 26.501 5.014  31.189  1.00 23.29 ? 464  GLY A O   1 
ATOM   3666 N  N   . ILE A 1 465 ? 27.998 5.626  29.630  1.00 18.21 ? 465  ILE A N   1 
ATOM   3667 C  CA  . ILE A 1 465 ? 29.119 4.910  30.223  1.00 14.86 ? 465  ILE A CA  1 
ATOM   3668 C  C   . ILE A 1 465 ? 29.486 5.496  31.583  1.00 16.63 ? 465  ILE A C   1 
ATOM   3669 O  O   . ILE A 1 465 ? 29.380 6.707  31.799  1.00 17.63 ? 465  ILE A O   1 
ATOM   3670 C  CB  . ILE A 1 465 ? 30.354 4.964  29.283  1.00 15.01 ? 465  ILE A CB  1 
ATOM   3671 C  CG1 . ILE A 1 465 ? 30.037 4.244  27.972  1.00 16.46 ? 465  ILE A CG1 1 
ATOM   3672 C  CG2 . ILE A 1 465 ? 31.579 4.354  29.947  1.00 9.26  ? 465  ILE A CG2 1 
ATOM   3673 C  CD1 . ILE A 1 465 ? 31.092 4.415  26.895  1.00 17.38 ? 465  ILE A CD1 1 
ATOM   3674 N  N   . LYS A 1 466 ? 29.866 4.621  32.507  1.00 17.82 ? 466  LYS A N   1 
ATOM   3675 C  CA  . LYS A 1 466 ? 30.278 5.019  33.847  1.00 20.76 ? 466  LYS A CA  1 
ATOM   3676 C  C   . LYS A 1 466 ? 31.733 4.600  33.949  1.00 18.75 ? 466  LYS A C   1 
ATOM   3677 O  O   . LYS A 1 466 ? 32.126 3.570  33.402  1.00 20.85 ? 466  LYS A O   1 
ATOM   3678 C  CB  . LYS A 1 466 ? 29.452 4.289  34.913  1.00 25.99 ? 466  LYS A CB  1 
ATOM   3679 C  CG  . LYS A 1 466 ? 27.955 4.490  34.769  1.00 35.41 ? 466  LYS A CG  1 
ATOM   3680 C  CD  . LYS A 1 466 ? 27.148 3.524  35.624  1.00 42.87 ? 466  LYS A CD  1 
ATOM   3681 C  CE  . LYS A 1 466 ? 27.387 3.750  37.107  1.00 48.29 ? 466  LYS A CE  1 
ATOM   3682 N  NZ  . LYS A 1 466 ? 26.468 2.921  37.946  1.00 53.19 ? 466  LYS A NZ  1 
ATOM   3683 N  N   . VAL A 1 467 ? 32.541 5.423  34.598  1.00 18.04 ? 467  VAL A N   1 
ATOM   3684 C  CA  . VAL A 1 467 ? 33.953 5.130  34.748  1.00 15.25 ? 467  VAL A CA  1 
ATOM   3685 C  C   . VAL A 1 467 ? 34.293 5.140  36.223  1.00 16.14 ? 467  VAL A C   1 
ATOM   3686 O  O   . VAL A 1 467 ? 34.030 6.123  36.917  1.00 19.61 ? 467  VAL A O   1 
ATOM   3687 C  CB  . VAL A 1 467 ? 34.823 6.167  34.002  1.00 13.37 ? 467  VAL A CB  1 
ATOM   3688 C  CG1 . VAL A 1 467 ? 36.292 5.903  34.249  1.00 13.14 ? 467  VAL A CG1 1 
ATOM   3689 C  CG2 . VAL A 1 467 ? 34.529 6.117  32.508  1.00 13.24 ? 467  VAL A CG2 1 
ATOM   3690 N  N   . TYR A 1 468 ? 34.815 4.020  36.713  1.00 15.65 ? 468  TYR A N   1 
ATOM   3691 C  CA  . TYR A 1 468 ? 35.200 3.922  38.116  1.00 13.49 ? 468  TYR A CA  1 
ATOM   3692 C  C   . TYR A 1 468 ? 36.685 4.231  38.248  1.00 15.26 ? 468  TYR A C   1 
ATOM   3693 O  O   . TYR A 1 468 ? 37.521 3.522  37.672  1.00 16.24 ? 468  TYR A O   1 
ATOM   3694 C  CB  . TYR A 1 468 ? 34.910 2.526  38.680  1.00 11.37 ? 468  TYR A CB  1 
ATOM   3695 C  CG  . TYR A 1 468 ? 35.525 2.321  40.047  1.00 9.98  ? 468  TYR A CG  1 
ATOM   3696 C  CD1 . TYR A 1 468 ? 35.077 3.049  41.146  1.00 9.73  ? 468  TYR A CD1 1 
ATOM   3697 C  CD2 . TYR A 1 468 ? 36.607 1.467  40.225  1.00 8.34  ? 468  TYR A CD2 1 
ATOM   3698 C  CE1 . TYR A 1 468 ? 35.694 2.939  42.380  1.00 8.38  ? 468  TYR A CE1 1 
ATOM   3699 C  CE2 . TYR A 1 468 ? 37.232 1.350  41.460  1.00 8.19  ? 468  TYR A CE2 1 
ATOM   3700 C  CZ  . TYR A 1 468 ? 36.772 2.094  42.530  1.00 6.84  ? 468  TYR A CZ  1 
ATOM   3701 O  OH  . TYR A 1 468 ? 37.412 2.025  43.745  1.00 10.65 ? 468  TYR A OH  1 
ATOM   3702 N  N   . VAL A 1 469 ? 37.010 5.282  38.999  1.00 20.00 ? 469  VAL A N   1 
ATOM   3703 C  CA  . VAL A 1 469 ? 38.397 5.694  39.213  1.00 20.00 ? 469  VAL A CA  1 
ATOM   3704 C  C   . VAL A 1 469 ? 38.823 5.285  40.609  1.00 20.00 ? 469  VAL A C   1 
ATOM   3705 O  O   . VAL A 1 469 ? 38.130 5.591  41.584  1.00 20.00 ? 469  VAL A O   1 
ATOM   3706 C  CB  . VAL A 1 469 ? 38.521 7.208  39.070  1.00 20.00 ? 469  VAL A CB  1 
ATOM   3707 C  CG1 . VAL A 1 469 ? 39.990 7.572  39.277  1.00 20.00 ? 469  VAL A CG1 1 
ATOM   3708 C  CG2 . VAL A 1 469 ? 38.194 7.607  37.629  1.00 20.00 ? 469  VAL A CG2 1 
ATOM   3709 N  N   . SER A 1 470 ? 39.939 4.567  40.702  1.00 15.87 ? 470  SER A N   1 
ATOM   3710 C  CA  . SER A 1 470 ? 40.455 4.111  41.986  1.00 18.01 ? 470  SER A CA  1 
ATOM   3711 C  C   . SER A 1 470 ? 41.004 5.260  42.825  1.00 21.09 ? 470  SER A C   1 
ATOM   3712 O  O   . SER A 1 470 ? 41.195 6.374  42.331  1.00 19.35 ? 470  SER A O   1 
ATOM   3713 C  CB  . SER A 1 470 ? 41.551 3.065  41.780  1.00 18.47 ? 470  SER A CB  1 
ATOM   3714 O  OG  . SER A 1 470 ? 42.706 3.635  41.198  1.00 20.64 ? 470  SER A OG  1 
ATOM   3715 N  N   . SER A 1 471 ? 41.307 4.961  44.083  1.00 22.49 ? 471  SER A N   1 
ATOM   3716 C  CA  . SER A 1 471 ? 41.847 5.940  45.015  1.00 24.81 ? 471  SER A CA  1 
ATOM   3717 C  C   . SER A 1 471 ? 43.145 6.563  44.510  1.00 24.96 ? 471  SER A C   1 
ATOM   3718 O  O   . SER A 1 471 ? 43.490 7.678  44.893  1.00 31.51 ? 471  SER A O   1 
ATOM   3719 C  CB  . SER A 1 471 ? 42.084 5.283  46.374  1.00 24.69 ? 471  SER A CB  1 
ATOM   3720 O  OG  . SER A 1 471 ? 40.907 4.628  46.812  1.00 36.45 ? 471  SER A OG  1 
ATOM   3721 N  N   . ASP A 1 472 ? 43.861 5.845  43.653  1.00 25.28 ? 472  ASP A N   1 
ATOM   3722 C  CA  . ASP A 1 472 ? 45.115 6.348  43.106  1.00 24.71 ? 472  ASP A CA  1 
ATOM   3723 C  C   . ASP A 1 472 ? 44.962 7.041  41.751  1.00 19.96 ? 472  ASP A C   1 
ATOM   3724 O  O   . ASP A 1 472 ? 45.935 7.206  41.020  1.00 22.53 ? 472  ASP A O   1 
ATOM   3725 C  CB  . ASP A 1 472 ? 46.156 5.229  43.032  1.00 32.25 ? 472  ASP A CB  1 
ATOM   3726 C  CG  . ASP A 1 472 ? 45.625 3.980  42.369  1.00 41.56 ? 472  ASP A CG  1 
ATOM   3727 O  OD1 . ASP A 1 472 ? 45.667 3.903  41.124  1.00 47.03 ? 472  ASP A OD1 1 
ATOM   3728 O  OD2 . ASP A 1 472 ? 45.162 3.073  43.093  1.00 51.22 ? 472  ASP A OD2 1 
ATOM   3729 N  N   . GLY A 1 473 ? 43.736 7.402  41.399  1.00 18.29 ? 473  GLY A N   1 
ATOM   3730 C  CA  . GLY A 1 473 ? 43.495 8.095  40.146  1.00 14.92 ? 473  GLY A CA  1 
ATOM   3731 C  C   . GLY A 1 473 ? 43.429 7.287  38.869  1.00 14.24 ? 473  GLY A C   1 
ATOM   3732 O  O   . GLY A 1 473 ? 43.058 7.831  37.834  1.00 18.26 ? 473  GLY A O   1 
ATOM   3733 N  N   . THR A 1 474 ? 43.778 6.008  38.905  1.00 15.04 ? 474  THR A N   1 
ATOM   3734 C  CA  . THR A 1 474 ? 43.717 5.205  37.689  1.00 13.04 ? 474  THR A CA  1 
ATOM   3735 C  C   . THR A 1 474 ? 42.305 4.715  37.383  1.00 13.91 ? 474  THR A C   1 
ATOM   3736 O  O   . THR A 1 474 ? 41.456 4.637  38.272  1.00 13.88 ? 474  THR A O   1 
ATOM   3737 C  CB  . THR A 1 474 ? 44.660 3.999  37.753  1.00 14.65 ? 474  THR A CB  1 
ATOM   3738 O  OG1 . THR A 1 474 ? 44.266 3.130  38.822  1.00 16.42 ? 474  THR A OG1 1 
ATOM   3739 C  CG2 . THR A 1 474 ? 46.092 4.464  37.973  1.00 16.90 ? 474  THR A CG2 1 
ATOM   3740 N  N   . ALA A 1 475 ? 42.068 4.391  36.116  1.00 10.71 ? 475  ALA A N   1 
ATOM   3741 C  CA  . ALA A 1 475 ? 40.783 3.887  35.654  1.00 11.63 ? 475  ALA A CA  1 
ATOM   3742 C  C   . ALA A 1 475 ? 41.015 3.155  34.339  1.00 14.20 ? 475  ALA A C   1 
ATOM   3743 O  O   . ALA A 1 475 ? 42.023 3.385  33.662  1.00 13.68 ? 475  ALA A O   1 
ATOM   3744 C  CB  . ALA A 1 475 ? 39.811 5.031  35.448  1.00 11.92 ? 475  ALA A CB  1 
ATOM   3745 N  N   . GLN A 1 476 ? 40.105 2.254  33.989  1.00 12.53 ? 476  GLN A N   1 
ATOM   3746 C  CA  . GLN A 1 476 ? 40.234 1.517  32.744  1.00 14.38 ? 476  GLN A CA  1 
ATOM   3747 C  C   . GLN A 1 476 ? 39.316 2.133  31.707  1.00 15.29 ? 476  GLN A C   1 
ATOM   3748 O  O   . GLN A 1 476 ? 38.168 2.459  32.000  1.00 17.67 ? 476  GLN A O   1 
ATOM   3749 C  CB  . GLN A 1 476 ? 39.868 0.039  32.918  1.00 13.51 ? 476  GLN A CB  1 
ATOM   3750 C  CG  . GLN A 1 476 ? 40.000 -0.759 31.612  1.00 12.92 ? 476  GLN A CG  1 
ATOM   3751 C  CD  . GLN A 1 476 ? 39.395 -2.149 31.686  1.00 13.62 ? 476  GLN A CD  1 
ATOM   3752 O  OE1 . GLN A 1 476 ? 38.175 -2.303 31.781  1.00 16.71 ? 476  GLN A OE1 1 
ATOM   3753 N  NE2 . GLN A 1 476 ? 40.236 -3.168 31.620  1.00 13.68 ? 476  GLN A NE2 1 
ATOM   3754 N  N   . PHE A 1 477 ? 39.827 2.279  30.493  1.00 14.74 ? 477  PHE A N   1 
ATOM   3755 C  CA  . PHE A 1 477 ? 39.048 2.828  29.404  1.00 11.74 ? 477  PHE A CA  1 
ATOM   3756 C  C   . PHE A 1 477 ? 39.025 1.794  28.309  1.00 11.36 ? 477  PHE A C   1 
ATOM   3757 O  O   . PHE A 1 477 ? 40.064 1.262  27.924  1.00 15.77 ? 477  PHE A O   1 
ATOM   3758 C  CB  . PHE A 1 477 ? 39.654 4.137  28.911  1.00 10.18 ? 477  PHE A CB  1 
ATOM   3759 C  CG  . PHE A 1 477 ? 39.619 5.229  29.938  1.00 10.70 ? 477  PHE A CG  1 
ATOM   3760 C  CD1 . PHE A 1 477 ? 38.504 6.054  30.053  1.00 8.38  ? 477  PHE A CD1 1 
ATOM   3761 C  CD2 . PHE A 1 477 ? 40.683 5.405  30.824  1.00 7.03  ? 477  PHE A CD2 1 
ATOM   3762 C  CE1 . PHE A 1 477 ? 38.443 7.036  31.039  1.00 7.81  ? 477  PHE A CE1 1 
ATOM   3763 C  CE2 . PHE A 1 477 ? 40.634 6.381  31.815  1.00 6.17  ? 477  PHE A CE2 1 
ATOM   3764 C  CZ  . PHE A 1 477 ? 39.511 7.198  31.926  1.00 7.68  ? 477  PHE A CZ  1 
ATOM   3765 N  N   . SER A 1 478 ? 37.824 1.431  27.892  1.00 11.94 ? 478  SER A N   1 
ATOM   3766 C  CA  . SER A 1 478 ? 37.639 0.452  26.841  1.00 13.92 ? 478  SER A CA  1 
ATOM   3767 C  C   . SER A 1 478 ? 36.872 1.142  25.726  1.00 13.40 ? 478  SER A C   1 
ATOM   3768 O  O   . SER A 1 478 ? 35.688 1.445  25.871  1.00 19.28 ? 478  SER A O   1 
ATOM   3769 C  CB  . SER A 1 478 ? 36.854 -0.749 27.374  1.00 14.62 ? 478  SER A CB  1 
ATOM   3770 O  OG  . SER A 1 478 ? 36.647 -1.722 26.362  1.00 23.35 ? 478  SER A OG  1 
ATOM   3771 N  N   . ILE A 1 479 ? 37.556 1.424  24.624  1.00 13.46 ? 479  ILE A N   1 
ATOM   3772 C  CA  . ILE A 1 479 ? 36.927 2.083  23.494  1.00 11.98 ? 479  ILE A CA  1 
ATOM   3773 C  C   . ILE A 1 479 ? 37.201 1.316  22.206  1.00 14.36 ? 479  ILE A C   1 
ATOM   3774 O  O   . ILE A 1 479 ? 38.355 1.127  21.804  1.00 12.90 ? 479  ILE A O   1 
ATOM   3775 C  CB  . ILE A 1 479 ? 37.423 3.546  23.340  1.00 13.17 ? 479  ILE A CB  1 
ATOM   3776 C  CG1 . ILE A 1 479 ? 37.166 4.333  24.627  1.00 11.79 ? 479  ILE A CG1 1 
ATOM   3777 C  CG2 . ILE A 1 479 ? 36.721 4.220  22.173  1.00 14.90 ? 479  ILE A CG2 1 
ATOM   3778 C  CD1 . ILE A 1 479 ? 37.606 5.778  24.557  1.00 10.19 ? 479  ILE A CD1 1 
ATOM   3779 N  N   . SER A 1 480 ? 36.129 0.854  21.576  1.00 16.72 ? 480  SER A N   1 
ATOM   3780 C  CA  . SER A 1 480 ? 36.223 0.120  20.328  1.00 17.63 ? 480  SER A CA  1 
ATOM   3781 C  C   . SER A 1 480 ? 36.373 1.098  19.173  1.00 22.03 ? 480  SER A C   1 
ATOM   3782 O  O   . SER A 1 480 ? 35.796 2.185  19.191  1.00 24.04 ? 480  SER A O   1 
ATOM   3783 C  CB  . SER A 1 480 ? 34.964 -0.716 20.123  1.00 18.66 ? 480  SER A CB  1 
ATOM   3784 O  OG  . SER A 1 480 ? 34.992 -1.367 18.868  1.00 21.23 ? 480  SER A OG  1 
ATOM   3785 N  N   . ASN A 1 481 ? 37.109 0.689  18.147  1.00 23.45 ? 481  ASN A N   1 
ATOM   3786 C  CA  . ASN A 1 481 ? 37.320 1.530  16.971  1.00 25.42 ? 481  ASN A CA  1 
ATOM   3787 C  C   . ASN A 1 481 ? 36.012 1.736  16.209  1.00 26.09 ? 481  ASN A C   1 
ATOM   3788 O  O   . ASN A 1 481 ? 35.912 2.613  15.349  1.00 25.57 ? 481  ASN A O   1 
ATOM   3789 C  CB  . ASN A 1 481 ? 38.358 0.897  16.048  1.00 26.93 ? 481  ASN A CB  1 
ATOM   3790 C  CG  . ASN A 1 481 ? 37.994 -0.520 15.654  1.00 29.06 ? 481  ASN A CG  1 
ATOM   3791 O  OD1 . ASN A 1 481 ? 38.154 -1.454 16.440  1.00 32.44 ? 481  ASN A OD1 1 
ATOM   3792 N  ND2 . ASN A 1 481 ? 37.476 -0.685 14.448  1.00 31.92 ? 481  ASN A ND2 1 
ATOM   3793 N  N   . SER A 1 482 ? 35.010 0.922  16.523  1.00 26.86 ? 482  SER A N   1 
ATOM   3794 C  CA  . SER A 1 482 ? 33.715 1.029  15.864  1.00 28.11 ? 482  SER A CA  1 
ATOM   3795 C  C   . SER A 1 482 ? 32.661 1.688  16.760  1.00 26.39 ? 482  SER A C   1 
ATOM   3796 O  O   . SER A 1 482 ? 31.462 1.558  16.509  1.00 26.11 ? 482  SER A O   1 
ATOM   3797 C  CB  . SER A 1 482 ? 33.232 -0.352 15.399  1.00 29.30 ? 482  SER A CB  1 
ATOM   3798 O  OG  . SER A 1 482 ? 32.890 -1.182 16.497  1.00 33.06 ? 482  SER A OG  1 
ATOM   3799 N  N   . ALA A 1 483 ? 33.107 2.337  17.835  1.00 24.36 ? 483  ALA A N   1 
ATOM   3800 C  CA  . ALA A 1 483 ? 32.181 3.024  18.733  1.00 21.45 ? 483  ALA A CA  1 
ATOM   3801 C  C   . ALA A 1 483 ? 31.617 4.232  17.980  1.00 22.40 ? 483  ALA A C   1 
ATOM   3802 O  O   . ALA A 1 483 ? 32.298 4.815  17.126  1.00 19.20 ? 483  ALA A O   1 
ATOM   3803 C  CB  . ALA A 1 483 ? 32.894 3.471  19.994  1.00 18.53 ? 483  ALA A CB  1 
ATOM   3804 N  N   . GLU A 1 484 ? 30.376 4.596  18.285  1.00 26.13 ? 484  GLU A N   1 
ATOM   3805 C  CA  . GLU A 1 484 ? 29.735 5.727  17.623  1.00 28.42 ? 484  GLU A CA  1 
ATOM   3806 C  C   . GLU A 1 484 ? 30.558 6.980  17.898  1.00 24.98 ? 484  GLU A C   1 
ATOM   3807 O  O   . GLU A 1 484 ? 30.787 7.796  17.005  1.00 24.08 ? 484  GLU A O   1 
ATOM   3808 C  CB  . GLU A 1 484 ? 28.310 5.912  18.133  1.00 37.58 ? 484  GLU A CB  1 
ATOM   3809 C  CG  . GLU A 1 484 ? 27.478 6.825  17.251  1.00 50.36 ? 484  GLU A CG  1 
ATOM   3810 C  CD  . GLU A 1 484 ? 26.249 7.355  17.957  1.00 56.64 ? 484  GLU A CD  1 
ATOM   3811 O  OE1 . GLU A 1 484 ? 25.368 6.537  18.311  1.00 59.25 ? 484  GLU A OE1 1 
ATOM   3812 O  OE2 . GLU A 1 484 ? 26.172 8.590  18.159  1.00 60.36 ? 484  GLU A OE2 1 
ATOM   3813 N  N   . ASP A 1 485 ? 30.973 7.133  19.150  1.00 20.46 ? 485  ASP A N   1 
ATOM   3814 C  CA  . ASP A 1 485 ? 31.807 8.252  19.563  1.00 15.36 ? 485  ASP A CA  1 
ATOM   3815 C  C   . ASP A 1 485 ? 33.028 7.619  20.188  1.00 13.64 ? 485  ASP A C   1 
ATOM   3816 O  O   . ASP A 1 485 ? 32.991 7.166  21.329  1.00 14.26 ? 485  ASP A O   1 
ATOM   3817 C  CB  . ASP A 1 485 ? 31.069 9.151  20.547  1.00 14.62 ? 485  ASP A CB  1 
ATOM   3818 C  CG  . ASP A 1 485 ? 29.954 9.926  19.881  1.00 13.38 ? 485  ASP A CG  1 
ATOM   3819 O  OD1 . ASP A 1 485 ? 30.212 10.543 18.827  1.00 14.87 ? 485  ASP A OD1 1 
ATOM   3820 O  OD2 . ASP A 1 485 ? 28.821 9.893  20.390  1.00 12.36 ? 485  ASP A OD2 1 
ATOM   3821 N  N   . PRO A 1 486 ? 34.131 7.557  19.427  1.00 11.28 ? 486  PRO A N   1 
ATOM   3822 C  CA  . PRO A 1 486 ? 35.405 6.974  19.842  1.00 10.94 ? 486  PRO A CA  1 
ATOM   3823 C  C   . PRO A 1 486 ? 36.194 7.744  20.889  1.00 10.10 ? 486  PRO A C   1 
ATOM   3824 O  O   . PRO A 1 486 ? 37.423 7.772  20.833  1.00 10.84 ? 486  PRO A O   1 
ATOM   3825 C  CB  . PRO A 1 486 ? 36.165 6.874  18.523  1.00 15.28 ? 486  PRO A CB  1 
ATOM   3826 C  CG  . PRO A 1 486 ? 35.720 8.116  17.807  1.00 14.03 ? 486  PRO A CG  1 
ATOM   3827 C  CD  . PRO A 1 486 ? 34.234 8.133  18.071  1.00 11.46 ? 486  PRO A CD  1 
ATOM   3828 N  N   . PHE A 1 487 ? 35.499 8.373  21.834  1.00 6.68  ? 487  PHE A N   1 
ATOM   3829 C  CA  . PHE A 1 487 ? 36.171 9.104  22.904  1.00 7.86  ? 487  PHE A CA  1 
ATOM   3830 C  C   . PHE A 1 487 ? 35.300 9.207  24.153  1.00 5.67  ? 487  PHE A C   1 
ATOM   3831 O  O   . PHE A 1 487 ? 34.076 9.098  24.071  1.00 8.96  ? 487  PHE A O   1 
ATOM   3832 C  CB  . PHE A 1 487 ? 36.714 10.477 22.432  1.00 7.75  ? 487  PHE A CB  1 
ATOM   3833 C  CG  . PHE A 1 487 ? 35.658 11.511 22.104  1.00 9.71  ? 487  PHE A CG  1 
ATOM   3834 C  CD1 . PHE A 1 487 ? 34.806 11.348 21.016  1.00 10.09 ? 487  PHE A CD1 1 
ATOM   3835 C  CD2 . PHE A 1 487 ? 35.553 12.670 22.866  1.00 8.60  ? 487  PHE A CD2 1 
ATOM   3836 C  CE1 . PHE A 1 487 ? 33.867 12.321 20.691  1.00 10.02 ? 487  PHE A CE1 1 
ATOM   3837 C  CE2 . PHE A 1 487 ? 34.623 13.648 22.554  1.00 9.77  ? 487  PHE A CE2 1 
ATOM   3838 C  CZ  . PHE A 1 487 ? 33.774 13.476 21.462  1.00 10.26 ? 487  PHE A CZ  1 
ATOM   3839 N  N   . ILE A 1 488 ? 35.947 9.323  25.306  1.00 5.88  ? 488  ILE A N   1 
ATOM   3840 C  CA  . ILE A 1 488 ? 35.281 9.411  26.602  1.00 8.98  ? 488  ILE A CA  1 
ATOM   3841 C  C   . ILE A 1 488 ? 35.820 10.633 27.332  1.00 11.04 ? 488  ILE A C   1 
ATOM   3842 O  O   . ILE A 1 488 ? 36.997 10.954 27.210  1.00 15.29 ? 488  ILE A O   1 
ATOM   3843 C  CB  . ILE A 1 488 ? 35.590 8.152  27.474  1.00 11.74 ? 488  ILE A CB  1 
ATOM   3844 C  CG1 . ILE A 1 488 ? 34.910 6.916  26.885  1.00 14.76 ? 488  ILE A CG1 1 
ATOM   3845 C  CG2 . ILE A 1 488 ? 35.154 8.356  28.926  1.00 7.42  ? 488  ILE A CG2 1 
ATOM   3846 C  CD1 . ILE A 1 488 ? 35.247 5.628  27.621  1.00 17.15 ? 488  ILE A CD1 1 
ATOM   3847 N  N   . ALA A 1 489 ? 34.968 11.307 28.095  1.00 10.60 ? 489  ALA A N   1 
ATOM   3848 C  CA  . ALA A 1 489 ? 35.383 12.484 28.848  1.00 9.30  ? 489  ALA A CA  1 
ATOM   3849 C  C   . ALA A 1 489 ? 34.633 12.498 30.155  1.00 8.38  ? 489  ALA A C   1 
ATOM   3850 O  O   . ALA A 1 489 ? 33.421 12.264 30.189  1.00 8.88  ? 489  ALA A O   1 
ATOM   3851 C  CB  . ALA A 1 489 ? 35.086 13.754 28.070  1.00 6.82  ? 489  ALA A CB  1 
ATOM   3852 N  N   . ILE A 1 490 ? 35.355 12.764 31.232  1.00 7.94  ? 490  ILE A N   1 
ATOM   3853 C  CA  . ILE A 1 490 ? 34.770 12.812 32.564  1.00 8.03  ? 490  ILE A CA  1 
ATOM   3854 C  C   . ILE A 1 490 ? 35.321 14.046 33.285  1.00 10.73 ? 490  ILE A C   1 
ATOM   3855 O  O   . ILE A 1 490 ? 36.397 14.541 32.937  1.00 13.63 ? 490  ILE A O   1 
ATOM   3856 C  CB  . ILE A 1 490 ? 35.119 11.525 33.368  1.00 8.48  ? 490  ILE A CB  1 
ATOM   3857 C  CG1 . ILE A 1 490 ? 36.631 11.314 33.400  1.00 5.68  ? 490  ILE A CG1 1 
ATOM   3858 C  CG2 . ILE A 1 490 ? 34.461 10.301 32.730  1.00 6.01  ? 490  ILE A CG2 1 
ATOM   3859 C  CD1 . ILE A 1 490 ? 37.057 10.086 34.148  1.00 7.20  ? 490  ILE A CD1 1 
ATOM   3860 N  N   . HIS A 1 491 ? 34.568 14.581 34.239  1.00 9.17  ? 491  HIS A N   1 
ATOM   3861 C  CA  . HIS A 1 491 ? 35.028 15.745 34.983  1.00 12.32 ? 491  HIS A CA  1 
ATOM   3862 C  C   . HIS A 1 491 ? 34.408 15.821 36.371  1.00 14.27 ? 491  HIS A C   1 
ATOM   3863 O  O   . HIS A 1 491 ? 33.450 15.108 36.671  1.00 16.47 ? 491  HIS A O   1 
ATOM   3864 C  CB  . HIS A 1 491 ? 34.806 17.057 34.204  1.00 9.45  ? 491  HIS A CB  1 
ATOM   3865 C  CG  . HIS A 1 491 ? 33.398 17.274 33.738  1.00 9.70  ? 491  HIS A CG  1 
ATOM   3866 N  ND1 . HIS A 1 491 ? 32.403 17.755 34.562  1.00 8.06  ? 491  HIS A ND1 1 
ATOM   3867 C  CD2 . HIS A 1 491 ? 32.827 17.101 32.521  1.00 9.51  ? 491  HIS A CD2 1 
ATOM   3868 C  CE1 . HIS A 1 491 ? 31.279 17.864 33.874  1.00 12.14 ? 491  HIS A CE1 1 
ATOM   3869 N  NE2 . HIS A 1 491 ? 31.511 17.474 32.633  1.00 10.45 ? 491  HIS A NE2 1 
ATOM   3870 N  N   . ALA A 1 492 ? 34.943 16.708 37.201  1.00 11.47 ? 492  ALA A N   1 
ATOM   3871 C  CA  . ALA A 1 492 ? 34.484 16.885 38.572  1.00 13.38 ? 492  ALA A CA  1 
ATOM   3872 C  C   . ALA A 1 492 ? 32.970 16.940 38.740  1.00 14.42 ? 492  ALA A C   1 
ATOM   3873 O  O   . ALA A 1 492 ? 32.425 16.394 39.695  1.00 18.42 ? 492  ALA A O   1 
ATOM   3874 C  CB  . ALA A 1 492 ? 35.120 18.126 39.172  1.00 10.33 ? 492  ALA A CB  1 
ATOM   3875 N  N   . GLU A 1 493 ? 32.286 17.583 37.802  1.00 17.83 ? 493  GLU A N   1 
ATOM   3876 C  CA  . GLU A 1 493 ? 30.840 17.700 37.890  1.00 19.27 ? 493  GLU A CA  1 
ATOM   3877 C  C   . GLU A 1 493 ? 30.007 16.544 37.329  1.00 20.40 ? 493  GLU A C   1 
ATOM   3878 O  O   . GLU A 1 493 ? 28.776 16.593 37.374  1.00 21.88 ? 493  GLU A O   1 
ATOM   3879 C  CB  . GLU A 1 493 ? 30.384 19.039 37.313  1.00 21.03 ? 493  GLU A CB  1 
ATOM   3880 C  CG  . GLU A 1 493 ? 30.876 20.218 38.143  1.00 27.23 ? 493  GLU A CG  1 
ATOM   3881 C  CD  . GLU A 1 493 ? 30.261 21.545 37.741  1.00 31.11 ? 493  GLU A CD  1 
ATOM   3882 O  OE1 . GLU A 1 493 ? 29.255 21.554 36.996  1.00 32.20 ? 493  GLU A OE1 1 
ATOM   3883 O  OE2 . GLU A 1 493 ? 30.794 22.586 38.185  1.00 34.54 ? 493  GLU A OE2 1 
ATOM   3884 N  N   . SER A 1 494 ? 30.657 15.532 36.757  1.00 17.24 ? 494  SER A N   1 
ATOM   3885 C  CA  . SER A 1 494 ? 29.918 14.375 36.247  1.00 16.21 ? 494  SER A CA  1 
ATOM   3886 C  C   . SER A 1 494 ? 30.117 13.226 37.233  1.00 16.22 ? 494  SER A C   1 
ATOM   3887 O  O   . SER A 1 494 ? 29.712 12.094 36.981  1.00 17.97 ? 494  SER A O   1 
ATOM   3888 C  CB  . SER A 1 494 ? 30.388 13.961 34.843  1.00 14.36 ? 494  SER A CB  1 
ATOM   3889 O  OG  . SER A 1 494 ? 31.718 13.472 34.848  1.00 16.53 ? 494  SER A OG  1 
ATOM   3890 N  N   . LYS A 1 495 ? 30.760 13.533 38.353  1.00 16.90 ? 495  LYS A N   1 
ATOM   3891 C  CA  . LYS A 1 495 ? 31.022 12.548 39.375  1.00 19.45 ? 495  LYS A CA  1 
ATOM   3892 C  C   . LYS A 1 495 ? 29.735 12.282 40.143  1.00 23.22 ? 495  LYS A C   1 
ATOM   3893 O  O   . LYS A 1 495 ? 28.987 13.210 40.468  1.00 24.95 ? 495  LYS A O   1 
ATOM   3894 C  CB  . LYS A 1 495 ? 32.125 13.038 40.311  1.00 18.57 ? 495  LYS A CB  1 
ATOM   3895 C  CG  . LYS A 1 495 ? 32.599 11.986 41.284  1.00 24.65 ? 495  LYS A CG  1 
ATOM   3896 C  CD  . LYS A 1 495 ? 33.491 12.589 42.341  1.00 29.24 ? 495  LYS A CD  1 
ATOM   3897 C  CE  . LYS A 1 495 ? 33.900 11.543 43.354  1.00 33.59 ? 495  LYS A CE  1 
ATOM   3898 N  NZ  . LYS A 1 495 ? 34.567 12.168 44.527  1.00 40.03 ? 495  LYS A NZ  1 
ATOM   3899 N  N   . LEU A 1 496 ? 29.477 11.003 40.392  1.00 24.60 ? 496  LEU A N   1 
ATOM   3900 C  CA  . LEU A 1 496 ? 28.294 10.548 41.105  1.00 22.25 ? 496  LEU A CA  1 
ATOM   3901 C  C   . LEU A 1 496 ? 28.436 10.760 42.607  1.00 24.37 ? 496  LEU A C   1 
ATOM   3902 O  O   . LEU A 1 496 ? 29.562 10.615 43.131  1.00 26.04 ? 496  LEU A O   1 
ATOM   3903 C  CB  . LEU A 1 496 ? 28.072 9.066  40.813  1.00 16.22 ? 496  LEU A CB  1 
ATOM   3904 C  CG  . LEU A 1 496 ? 26.885 8.639  39.954  1.00 16.10 ? 496  LEU A CG  1 
ATOM   3905 C  CD1 . LEU A 1 496 ? 26.391 9.755  39.059  1.00 16.44 ? 496  LEU A CD1 1 
ATOM   3906 C  CD2 . LEU A 1 496 ? 27.303 7.437  39.147  1.00 18.60 ? 496  LEU A CD2 1 
ATOM   3907 O  OXT . LEU A 1 496 ? 27.408 11.053 43.248  1.00 29.23 ? 496  LEU A OXT 1 
HETATM 3908 C  C2  . BGC B 2 .   ? 44.191 34.104 1.291   1.00 61.16 ? 1    BGC B C2  1 
HETATM 3909 C  C3  . BGC B 2 .   ? 43.102 34.811 2.083   1.00 57.74 ? 1    BGC B C3  1 
HETATM 3910 C  C4  . BGC B 2 .   ? 41.780 34.832 1.307   1.00 58.85 ? 1    BGC B C4  1 
HETATM 3911 C  C5  . BGC B 2 .   ? 41.423 33.445 0.728   1.00 63.17 ? 1    BGC B C5  1 
HETATM 3912 C  C6  . BGC B 2 .   ? 40.288 33.519 -0.287  1.00 65.49 ? 1    BGC B C6  1 
HETATM 3913 C  C1  . BGC B 2 .   ? 43.692 32.721 0.915   1.00 63.99 ? 1    BGC B C1  1 
HETATM 3914 O  O1  . BGC B 2 .   ? 44.682 32.028 0.239   1.00 67.67 ? 1    BGC B O1  1 
HETATM 3915 O  O2  . BGC B 2 .   ? 45.370 33.991 2.074   1.00 62.21 ? 1    BGC B O2  1 
HETATM 3916 O  O3  . BGC B 2 .   ? 43.504 36.141 2.370   1.00 52.12 ? 1    BGC B O3  1 
HETATM 3917 O  O4  . BGC B 2 .   ? 40.729 35.241 2.215   1.00 55.65 ? 1    BGC B O4  1 
HETATM 3918 O  O5  . BGC B 2 .   ? 42.555 32.846 0.056   1.00 64.89 ? 1    BGC B O5  1 
HETATM 3919 O  O6  . BGC B 2 .   ? 39.846 32.223 -0.676  1.00 70.02 ? 1    BGC B O6  1 
HETATM 3920 C  C1  . AC1 B 2 .   ? 39.920 36.300 1.798   1.00 49.83 ? 2    AC1 B C1  1 
HETATM 3921 O  O2  . AC1 B 2 .   ? 41.183 37.606 3.394   1.00 43.50 ? 2    AC1 B O2  1 
HETATM 3922 C  C2  . AC1 B 2 .   ? 39.874 37.378 2.893   1.00 47.03 ? 2    AC1 B C2  1 
HETATM 3923 C  C4A . AC1 B 2 .   ? 33.584 37.507 2.990   1.00 40.79 ? 2    AC1 B C4A 1 
HETATM 3924 C  C3  . AC1 B 2 .   ? 38.976 36.973 4.057   1.00 46.75 ? 2    AC1 B C3  1 
HETATM 3925 O  O3  . AC1 B 2 .   ? 38.836 38.080 4.938   1.00 46.56 ? 2    AC1 B O3  1 
HETATM 3926 C  C4  . AC1 B 2 .   ? 37.607 36.525 3.543   1.00 45.37 ? 2    AC1 B C4  1 
HETATM 3927 N  N4A . AC1 B 2 .   ? 36.678 36.086 4.572   1.00 43.84 ? 2    AC1 B N4A 1 
HETATM 3928 C  C5  . AC1 B 2 .   ? 37.812 35.393 2.540   1.00 45.19 ? 2    AC1 B C5  1 
HETATM 3929 O  O5  . AC1 B 2 .   ? 38.604 35.873 1.438   1.00 48.25 ? 2    AC1 B O5  1 
HETATM 3930 C  C6  . AC1 B 2 .   ? 36.477 34.862 2.029   1.00 42.09 ? 2    AC1 B C6  1 
HETATM 3931 C  C1B . AC1 B 2 .   ? 35.873 37.197 5.060   1.00 42.42 ? 2    AC1 B C1B 1 
HETATM 3932 C  C2B . AC1 B 2 .   ? 34.407 36.811 5.281   1.00 40.96 ? 2    AC1 B C2B 1 
HETATM 3933 O  O2B . AC1 B 2 .   ? 34.308 35.769 6.236   1.00 41.48 ? 2    AC1 B O2B 1 
HETATM 3934 C  C3B . AC1 B 2 .   ? 33.775 36.341 3.974   1.00 40.58 ? 2    AC1 B C3B 1 
HETATM 3935 O  O3B . AC1 B 2 .   ? 32.522 35.733 4.264   1.00 38.27 ? 2    AC1 B O3B 1 
HETATM 3936 O  O4  . AC1 B 2 .   ? 33.627 37.005 1.595   1.00 38.95 ? 2    AC1 B O4  1 
HETATM 3937 C  C5B . AC1 B 2 .   ? 34.647 38.582 3.197   1.00 39.54 ? 2    AC1 B C5B 1 
HETATM 3938 C  C7B . AC1 B 2 .   ? 35.800 38.461 4.179   1.00 40.54 ? 2    AC1 B C7B 1 
HETATM 3939 C  C6B . AC1 B 2 .   ? 34.509 39.862 2.405   1.00 40.03 ? 2    AC1 B C6B 1 
HETATM 3940 O  O6B . AC1 B 2 .   ? 33.781 40.684 3.308   1.00 39.55 ? 2    AC1 B O6B 1 
HETATM 3941 C  C1  . GLC B 2 .   ? 32.395 36.567 1.089   1.00 35.59 ? 3    GLC B C1  1 
HETATM 3942 C  C2  . GLC B 2 .   ? 32.609 35.521 -0.021  1.00 36.92 ? 3    GLC B C2  1 
HETATM 3943 C  C3  . GLC B 2 .   ? 32.982 36.177 -1.352  1.00 37.01 ? 3    GLC B C3  1 
HETATM 3944 C  C4  . GLC B 2 .   ? 31.926 37.222 -1.690  1.00 37.05 ? 3    GLC B C4  1 
HETATM 3945 C  C5  . GLC B 2 .   ? 31.959 38.263 -0.586  1.00 35.58 ? 3    GLC B C5  1 
HETATM 3946 C  C6  . GLC B 2 .   ? 31.031 39.435 -0.841  1.00 34.98 ? 3    GLC B C6  1 
HETATM 3947 O  O2  . GLC B 2 .   ? 33.631 34.608 0.357   1.00 36.05 ? 3    GLC B O2  1 
HETATM 3948 O  O3  . GLC B 2 .   ? 33.051 35.188 -2.369  1.00 37.76 ? 3    GLC B O3  1 
HETATM 3949 O  O4  . GLC B 2 .   ? 32.182 37.831 -2.974  1.00 36.11 ? 3    GLC B O4  1 
HETATM 3950 O  O5  . GLC B 2 .   ? 31.562 37.646 0.658   1.00 35.83 ? 3    GLC B O5  1 
HETATM 3951 O  O6  . GLC B 2 .   ? 29.674 39.025 -0.833  1.00 32.87 ? 3    GLC B O6  1 
HETATM 3952 C  C1  . AC1 B 2 .   ? 31.045 37.961 -3.786  1.00 39.98 ? 4    AC1 B C1  1 
HETATM 3953 O  O2  . AC1 B 2 .   ? 31.414 35.702 -4.583  1.00 40.38 ? 4    AC1 B O2  1 
HETATM 3954 C  C2  . AC1 B 2 .   ? 31.153 37.034 -5.000  1.00 41.36 ? 4    AC1 B C2  1 
HETATM 3955 C  C4A . AC1 B 2 .   ? 34.523 41.747 -9.974  1.00 57.46 ? 4    AC1 B C4A 1 
HETATM 3956 C  C3  . AC1 B 2 .   ? 32.279 37.512 -5.904  1.00 42.48 ? 4    AC1 B C3  1 
HETATM 3957 O  O3  . AC1 B 2 .   ? 32.351 36.680 -7.053  1.00 42.18 ? 4    AC1 B O3  1 
HETATM 3958 C  C4  . AC1 B 2 .   ? 32.022 38.963 -6.313  1.00 43.56 ? 4    AC1 B C4  1 
HETATM 3959 N  N4A . AC1 B 2 .   ? 33.194 39.426 -7.038  1.00 47.93 ? 4    AC1 B N4A 1 
HETATM 3960 C  C5  . AC1 B 2 .   ? 31.855 39.843 -5.071  1.00 40.86 ? 4    AC1 B C5  1 
HETATM 3961 O  O5  . AC1 B 2 .   ? 30.826 39.303 -4.215  1.00 42.16 ? 4    AC1 B O5  1 
HETATM 3962 C  C6  . AC1 B 2 .   ? 31.476 41.263 -5.487  1.00 38.12 ? 4    AC1 B C6  1 
HETATM 3963 C  C1B . AC1 B 2 .   ? 32.849 39.623 -8.438  1.00 53.17 ? 4    AC1 B C1B 1 
HETATM 3964 C  C2B . AC1 B 2 .   ? 34.101 39.365 -9.279  1.00 56.55 ? 4    AC1 B C2B 1 
HETATM 3965 O  O2B . AC1 B 2 .   ? 34.759 38.194 -8.812  1.00 59.49 ? 4    AC1 B O2B 1 
HETATM 3966 C  C3B . AC1 B 2 .   ? 35.059 40.557 -9.180  1.00 57.79 ? 4    AC1 B C3B 1 
HETATM 3967 O  O3B . AC1 B 2 .   ? 36.348 40.196 -9.663  1.00 57.94 ? 4    AC1 B O3B 1 
HETATM 3968 O  O4  . AC1 B 2 .   ? 35.462 42.814 -9.917  1.00 57.70 ? 4    AC1 B O4  1 
HETATM 3969 C  C5B . AC1 B 2 .   ? 33.143 42.099 -9.416  1.00 56.92 ? 4    AC1 B C5B 1 
HETATM 3970 C  C7B . AC1 B 2 .   ? 32.310 41.046 -8.692  1.00 54.53 ? 4    AC1 B C7B 1 
HETATM 3971 C  C6B . AC1 B 2 .   ? 32.542 43.491 -9.559  1.00 57.44 ? 4    AC1 B C6B 1 
HETATM 3972 O  O6B . AC1 B 2 .   ? 32.352 44.070 -8.273  1.00 58.19 ? 4    AC1 B O6B 1 
HETATM 3973 C  C2  . BGC C 3 .   ? 54.087 17.121 12.530  1.00 66.33 ? 996  BGC A C2  1 
HETATM 3974 C  C3  . BGC C 3 .   ? 54.035 18.635 12.280  1.00 66.43 ? 996  BGC A C3  1 
HETATM 3975 C  C4  . BGC C 3 .   ? 53.981 19.394 13.629  1.00 66.90 ? 996  BGC A C4  1 
HETATM 3976 C  C5  . BGC C 3 .   ? 55.101 18.928 14.559  1.00 68.00 ? 996  BGC A C5  1 
HETATM 3977 C  C6  . BGC C 3 .   ? 55.008 19.539 15.953  1.00 68.35 ? 996  BGC A C6  1 
HETATM 3978 C  C1  . BGC C 3 .   ? 55.253 16.804 13.470  1.00 66.54 ? 996  BGC A C1  1 
HETATM 3979 O  O1  . BGC C 3 .   ? 55.316 15.442 13.720  1.00 64.67 ? 996  BGC A O1  1 
HETATM 3980 O  O2  . BGC C 3 .   ? 54.262 16.424 11.300  1.00 66.42 ? 996  BGC A O2  1 
HETATM 3981 O  O3  . BGC C 3 .   ? 52.897 18.967 11.491  1.00 63.72 ? 996  BGC A O3  1 
HETATM 3982 O  O4  . BGC C 3 .   ? 54.065 20.789 13.392  1.00 66.54 ? 996  BGC A O4  1 
HETATM 3983 O  O5  . BGC C 3 .   ? 55.071 17.485 14.714  1.00 67.46 ? 996  BGC A O5  1 
HETATM 3984 O  O6  . BGC C 3 .   ? 55.967 18.967 16.836  1.00 69.61 ? 996  BGC A O6  1 
HETATM 3985 CL CL  . CL  D 4 .   ? 36.212 33.985 11.485  1.00 8.96  ? 498  CL  A CL  1 
HETATM 3986 CA CA  . CA  E 5 .   ? 41.149 47.568 2.426   1.00 11.64 ? 500  CA  A CA  1 
HETATM 3987 O  O   . HOH F 6 .   ? 23.068 35.778 13.029  1.00 9.52  ? 997  HOH A O   1 
HETATM 3988 O  O   . HOH F 6 .   ? 20.172 40.426 5.386   1.00 17.11 ? 998  HOH A O   1 
HETATM 3989 O  O   . HOH F 6 .   ? 22.128 26.052 13.699  1.00 8.78  ? 999  HOH A O   1 
HETATM 3990 O  O   . HOH F 6 .   ? 30.904 28.393 27.418  1.00 13.63 ? 1000 HOH A O   1 
HETATM 3991 O  O   . HOH F 6 .   ? 43.132 49.958 6.315   1.00 25.24 ? 1001 HOH A O   1 
HETATM 3992 O  O   . HOH F 6 .   ? 28.188 47.053 26.005  1.00 10.60 ? 1002 HOH A O   1 
HETATM 3993 O  O   . HOH F 6 .   ? 38.989 21.250 10.696  1.00 8.40  ? 1003 HOH A O   1 
HETATM 3994 O  O   . HOH F 6 .   ? 26.494 41.313 25.145  1.00 14.47 ? 1004 HOH A O   1 
HETATM 3995 O  O   . HOH F 6 .   ? 41.997 24.358 22.187  1.00 9.01  ? 1005 HOH A O   1 
HETATM 3996 O  O   . HOH F 6 .   ? 31.531 48.999 6.104   1.00 8.81  ? 1006 HOH A O   1 
HETATM 3997 O  O   . HOH F 6 .   ? 23.631 41.812 6.626   1.00 16.54 ? 1007 HOH A O   1 
HETATM 3998 O  O   . HOH F 6 .   ? 29.957 22.244 10.919  1.00 8.04  ? 1008 HOH A O   1 
HETATM 3999 O  O   . HOH F 6 .   ? 18.561 32.064 1.698   1.00 21.19 ? 1009 HOH A O   1 
HETATM 4000 O  O   . HOH F 6 .   ? 33.377 28.933 13.822  1.00 13.83 ? 1010 HOH A O   1 
HETATM 4001 O  O   . HOH F 6 .   ? 26.229 35.492 5.969   1.00 8.15  ? 1011 HOH A O   1 
HETATM 4002 O  O   . HOH F 6 .   ? 41.059 27.212 12.752  1.00 24.95 ? 1012 HOH A O   1 
HETATM 4003 O  O   . HOH F 6 .   ? 27.181 8.595  31.074  1.00 15.84 ? 1013 HOH A O   1 
HETATM 4004 O  O   . HOH F 6 .   ? 38.135 29.296 26.140  1.00 15.15 ? 1014 HOH A O   1 
HETATM 4005 O  O   . HOH F 6 .   ? 35.287 44.059 6.585   1.00 3.64  ? 1015 HOH A O   1 
HETATM 4006 O  O   . HOH F 6 .   ? 39.521 49.133 3.032   1.00 10.99 ? 1016 HOH A O   1 
HETATM 4007 O  O   . HOH F 6 .   ? 32.316 30.731 12.102  1.00 3.55  ? 1017 HOH A O   1 
HETATM 4008 O  O   . HOH F 6 .   ? 23.222 28.413 11.602  1.00 8.82  ? 1018 HOH A O   1 
HETATM 4009 O  O   . HOH F 6 .   ? 25.746 26.381 6.924   1.00 14.62 ? 1019 HOH A O   1 
HETATM 4010 O  O   . HOH F 6 .   ? 19.497 43.932 11.570  1.00 9.46  ? 1020 HOH A O   1 
HETATM 4011 O  O   . HOH F 6 .   ? 33.144 33.491 11.343  1.00 8.74  ? 1021 HOH A O   1 
HETATM 4012 O  O   . HOH F 6 .   ? 29.113 36.299 11.851  1.00 10.90 ? 1022 HOH A O   1 
HETATM 4013 O  O   . HOH F 6 .   ? 41.685 46.054 0.850   1.00 7.43  ? 1023 HOH A O   1 
HETATM 4014 O  O   . HOH F 6 .   ? 31.606 7.694  24.716  1.00 16.38 ? 1024 HOH A O   1 
HETATM 4015 O  O   . HOH F 6 .   ? 47.863 32.717 12.052  1.00 13.02 ? 1025 HOH A O   1 
HETATM 4016 O  O   . HOH F 6 .   ? 45.303 32.845 10.882  1.00 4.57  ? 1026 HOH A O   1 
HETATM 4017 O  O   . HOH F 6 .   ? 37.727 45.459 -0.719  1.00 11.61 ? 1027 HOH A O   1 
HETATM 4018 O  O   . HOH F 6 .   ? 28.720 44.892 10.570  1.00 12.11 ? 1028 HOH A O   1 
HETATM 4019 O  O   . HOH F 6 .   ? 27.269 35.731 8.406   1.00 12.03 ? 1029 HOH A O   1 
HETATM 4020 O  O   . HOH F 6 .   ? 14.088 38.669 14.159  1.00 23.58 ? 1030 HOH A O   1 
HETATM 4021 O  O   . HOH F 6 .   ? 23.579 54.253 1.001   1.00 14.52 ? 1031 HOH A O   1 
HETATM 4022 O  O   . HOH F 6 .   ? 16.066 37.298 29.114  1.00 16.78 ? 1032 HOH A O   1 
HETATM 4023 O  O   . HOH F 6 .   ? 22.115 36.211 3.516   1.00 14.09 ? 1033 HOH A O   1 
HETATM 4024 O  O   . HOH F 6 .   ? 32.947 26.388 27.206  1.00 10.42 ? 1034 HOH A O   1 
HETATM 4025 O  O   . HOH F 6 .   ? 42.033 49.162 3.808   1.00 10.48 ? 1035 HOH A O   1 
HETATM 4026 O  O   . HOH F 6 .   ? 37.508 24.606 3.077   1.00 22.79 ? 1036 HOH A O   1 
HETATM 4027 O  O   . HOH F 6 .   ? 25.822 27.377 1.416   1.00 12.76 ? 1037 HOH A O   1 
HETATM 4028 O  O   . HOH F 6 .   ? 28.778 35.129 29.293  1.00 15.99 ? 1038 HOH A O   1 
HETATM 4029 O  O   . HOH F 6 .   ? 26.281 44.106 5.542   1.00 13.85 ? 1039 HOH A O   1 
HETATM 4030 O  O   . HOH F 6 .   ? 16.486 31.940 12.604  1.00 13.86 ? 1040 HOH A O   1 
HETATM 4031 O  O   . HOH F 6 .   ? 40.859 50.210 -3.853  1.00 13.67 ? 1041 HOH A O   1 
HETATM 4032 O  O   . HOH F 6 .   ? 37.937 50.632 -4.181  1.00 18.98 ? 1042 HOH A O   1 
HETATM 4033 O  O   . HOH F 6 .   ? 20.687 38.439 3.722   1.00 17.17 ? 1043 HOH A O   1 
HETATM 4034 O  O   . HOH F 6 .   ? 27.646 55.739 11.162  1.00 17.53 ? 1044 HOH A O   1 
HETATM 4035 O  O   . HOH F 6 .   ? 30.802 22.747 0.218   1.00 20.44 ? 1045 HOH A O   1 
HETATM 4036 O  O   . HOH F 6 .   ? 13.210 29.451 17.781  1.00 25.31 ? 1046 HOH A O   1 
HETATM 4037 O  O   . HOH F 6 .   ? 26.391 22.708 28.390  1.00 24.62 ? 1047 HOH A O   1 
HETATM 4038 O  O   . HOH F 6 .   ? 50.021 31.907 13.839  1.00 25.79 ? 1048 HOH A O   1 
HETATM 4039 O  O   . HOH F 6 .   ? 54.899 33.586 -0.104  1.00 25.63 ? 1049 HOH A O   1 
HETATM 4040 O  O   . HOH F 6 .   ? 37.164 33.037 6.900   1.00 9.51  ? 1050 HOH A O   1 
HETATM 4041 O  O   . HOH F 6 .   ? 43.616 51.210 3.092   1.00 17.34 ? 1051 HOH A O   1 
HETATM 4042 O  O   . HOH F 6 .   ? 19.270 51.340 12.275  1.00 25.11 ? 1052 HOH A O   1 
HETATM 4043 O  O   . HOH F 6 .   ? 44.834 14.990 34.885  1.00 17.09 ? 1053 HOH A O   1 
HETATM 4044 O  O   . HOH F 6 .   ? 34.529 25.242 15.697  1.00 14.10 ? 1054 HOH A O   1 
HETATM 4045 O  O   . HOH F 6 .   ? 32.751 11.152 17.608  1.00 22.18 ? 1055 HOH A O   1 
HETATM 4046 O  O   . HOH F 6 .   ? 44.261 10.906 14.211  1.00 16.00 ? 1056 HOH A O   1 
HETATM 4047 O  O   . HOH F 6 .   ? 14.014 36.911 6.796   1.00 19.69 ? 1057 HOH A O   1 
HETATM 4048 O  O   . HOH F 6 .   ? 39.529 26.181 10.460  1.00 16.92 ? 1058 HOH A O   1 
HETATM 4049 O  O   . HOH F 6 .   ? 23.957 54.438 7.839   1.00 13.01 ? 1059 HOH A O   1 
HETATM 4050 O  O   . HOH F 6 .   ? 40.666 49.767 -6.530  1.00 23.35 ? 1060 HOH A O   1 
HETATM 4051 O  O   . HOH F 6 .   ? 32.432 23.688 16.260  1.00 14.23 ? 1061 HOH A O   1 
HETATM 4052 O  O   . HOH F 6 .   ? 14.266 39.889 19.656  1.00 24.31 ? 1062 HOH A O   1 
HETATM 4053 O  O   . HOH F 6 .   ? 41.512 26.781 8.629   1.00 41.42 ? 1063 HOH A O   1 
HETATM 4054 O  O   . HOH F 6 .   ? 48.414 49.094 -4.443  1.00 20.65 ? 1064 HOH A O   1 
HETATM 4055 O  O   . HOH F 6 .   ? 48.919 45.510 16.340  1.00 23.99 ? 1065 HOH A O   1 
HETATM 4056 O  O   . HOH F 6 .   ? 32.264 49.436 31.174  1.00 22.52 ? 1066 HOH A O   1 
HETATM 4057 O  O   . HOH F 6 .   ? 39.337 25.152 37.881  1.00 42.45 ? 1067 HOH A O   1 
HETATM 4058 O  O   . HOH F 6 .   ? 33.262 11.054 9.788   1.00 27.49 ? 1068 HOH A O   1 
HETATM 4059 O  O   . HOH F 6 .   ? 38.968 25.314 29.999  1.00 36.92 ? 1069 HOH A O   1 
HETATM 4060 O  O   . HOH F 6 .   ? 44.665 53.147 4.670   1.00 12.81 ? 1070 HOH A O   1 
HETATM 4061 O  O   . HOH F 6 .   ? 47.167 9.507  31.601  1.00 18.31 ? 1071 HOH A O   1 
HETATM 4062 O  O   . HOH F 6 .   ? 49.754 20.589 24.159  1.00 23.09 ? 1072 HOH A O   1 
HETATM 4063 O  O   . HOH F 6 .   ? 48.692 51.103 -2.535  1.00 18.63 ? 1073 HOH A O   1 
HETATM 4064 O  O   . HOH F 6 .   ? 31.793 8.697  43.334  1.00 41.48 ? 1074 HOH A O   1 
HETATM 4065 O  O   . HOH F 6 .   ? 19.396 31.029 -0.728  1.00 16.36 ? 1075 HOH A O   1 
HETATM 4066 O  O   . HOH F 6 .   ? 15.077 39.804 30.055  1.00 38.50 ? 1076 HOH A O   1 
HETATM 4067 O  O   . HOH F 6 .   ? 49.855 38.416 2.603   1.00 20.07 ? 1077 HOH A O   1 
HETATM 4068 O  O   . HOH F 6 .   ? 33.876 23.634 -3.033  1.00 49.00 ? 1078 HOH A O   1 
HETATM 4069 O  O   . HOH F 6 .   ? 27.447 58.954 12.319  1.00 47.17 ? 1079 HOH A O   1 
HETATM 4070 O  O   . HOH F 6 .   ? 25.842 56.109 9.105   1.00 27.59 ? 1080 HOH A O   1 
HETATM 4071 O  O   . HOH F 6 .   ? 26.092 52.988 27.786  1.00 24.20 ? 1081 HOH A O   1 
HETATM 4072 O  O   . HOH F 6 .   ? 38.303 4.675  16.124  1.00 31.52 ? 1082 HOH A O   1 
HETATM 4073 O  O   . HOH F 6 .   ? 25.673 54.636 12.869  1.00 24.34 ? 1083 HOH A O   1 
HETATM 4074 O  O   . HOH F 6 .   ? 32.868 5.607  23.589  1.00 22.35 ? 1084 HOH A O   1 
HETATM 4075 O  O   . HOH F 6 .   ? 27.723 56.571 18.008  1.00 24.57 ? 1085 HOH A O   1 
HETATM 4076 O  O   . HOH F 6 .   ? 44.889 3.460  12.718  1.00 44.91 ? 1086 HOH A O   1 
HETATM 4077 O  O   . HOH F 6 .   ? 48.719 45.643 -12.505 1.00 48.85 ? 1087 HOH A O   1 
HETATM 4078 O  O   . HOH F 6 .   ? 52.679 34.436 6.754   1.00 23.14 ? 1088 HOH A O   1 
HETATM 4079 O  O   . HOH F 6 .   ? 41.789 59.294 13.850  1.00 41.10 ? 1089 HOH A O   1 
HETATM 4080 O  O   . HOH F 6 .   ? 20.541 19.313 16.603  1.00 28.05 ? 1090 HOH A O   1 
HETATM 4081 O  O   . HOH F 6 .   ? 35.830 20.233 4.292   1.00 42.09 ? 1091 HOH A O   1 
HETATM 4082 O  O   . HOH F 6 .   ? 19.973 31.146 32.515  1.00 41.12 ? 1092 HOH A O   1 
HETATM 4083 O  O   . HOH F 6 .   ? 18.674 27.246 1.924   1.00 32.05 ? 1093 HOH A O   1 
HETATM 4084 O  O   . HOH F 6 .   ? 52.644 24.089 22.870  1.00 33.43 ? 1094 HOH A O   1 
HETATM 4085 O  O   . HOH F 6 .   ? 30.355 57.589 18.442  1.00 20.04 ? 1095 HOH A O   1 
HETATM 4086 O  O   . HOH F 6 .   ? 41.804 37.643 6.514   1.00 13.45 ? 1096 HOH A O   1 
HETATM 4087 O  O   . HOH F 6 .   ? 28.280 8.057  22.322  1.00 31.14 ? 1097 HOH A O   1 
HETATM 4088 O  O   . HOH F 6 .   ? 51.108 48.206 -4.781  1.00 35.79 ? 1098 HOH A O   1 
HETATM 4089 O  O   . HOH F 6 .   ? 26.178 16.268 0.692   1.00 54.98 ? 1099 HOH A O   1 
HETATM 4090 O  O   . HOH F 6 .   ? 11.404 36.764 29.282  1.00 61.19 ? 1100 HOH A O   1 
HETATM 4091 O  O   . HOH F 6 .   ? 42.195 27.877 28.990  1.00 49.46 ? 1101 HOH A O   1 
HETATM 4092 O  O   . HOH F 6 .   ? 19.184 19.640 14.208  1.00 28.13 ? 1102 HOH A O   1 
HETATM 4093 O  O   . HOH F 6 .   ? 29.020 25.786 33.417  1.00 40.24 ? 1103 HOH A O   1 
HETATM 4094 O  O   . HOH F 6 .   ? 49.721 50.108 10.198  1.00 8.65  ? 1104 HOH A O   1 
HETATM 4095 O  O   . HOH F 6 .   ? 26.649 60.485 -0.940  1.00 34.20 ? 1105 HOH A O   1 
HETATM 4096 O  O   . HOH F 6 .   ? 39.689 30.600 27.900  1.00 28.12 ? 1106 HOH A O   1 
HETATM 4097 O  O   . HOH F 6 .   ? 51.407 46.423 13.360  1.00 59.64 ? 1107 HOH A O   1 
HETATM 4098 O  O   . HOH F 6 .   ? 38.516 44.566 -9.060  1.00 49.07 ? 1108 HOH A O   1 
HETATM 4099 O  O   . HOH F 6 .   ? 28.216 51.810 26.576  1.00 9.54  ? 1109 HOH A O   1 
HETATM 4100 O  O   . HOH F 6 .   ? 38.186 43.116 26.257  1.00 16.04 ? 1110 HOH A O   1 
HETATM 4101 O  O   . HOH F 6 .   ? 15.335 49.226 12.132  1.00 30.58 ? 1111 HOH A O   1 
HETATM 4102 O  O   . HOH F 6 .   ? 33.798 16.017 42.137  1.00 36.08 ? 1112 HOH A O   1 
HETATM 4103 O  O   . HOH F 6 .   ? 14.766 24.348 4.678   1.00 50.85 ? 1113 HOH A O   1 
HETATM 4104 O  O   . HOH F 6 .   ? 15.464 41.195 2.194   1.00 22.06 ? 1114 HOH A O   1 
HETATM 4105 O  O   . HOH F 6 .   ? 38.266 11.658 6.041   1.00 22.24 ? 1115 HOH A O   1 
HETATM 4106 O  O   . HOH F 6 .   ? 17.360 23.626 27.728  1.00 48.25 ? 1116 HOH A O   1 
HETATM 4107 O  O   . HOH F 6 .   ? 38.423 30.833 5.821   1.00 29.68 ? 1117 HOH A O   1 
HETATM 4108 O  O   . HOH F 6 .   ? 15.178 24.069 24.262  1.00 29.06 ? 1118 HOH A O   1 
HETATM 4109 O  O   . HOH F 6 .   ? 42.981 27.185 31.423  1.00 34.90 ? 1119 HOH A O   1 
HETATM 4110 O  O   . HOH F 6 .   ? 18.787 58.811 -1.645  1.00 41.88 ? 1120 HOH A O   1 
HETATM 4111 O  O   . HOH F 6 .   ? 44.802 0.433  24.640  1.00 65.80 ? 1121 HOH A O   1 
HETATM 4112 O  O   . HOH F 6 .   ? 20.575 19.163 23.910  1.00 45.34 ? 1122 HOH A O   1 
HETATM 4113 O  O   . HOH F 6 .   ? 11.966 41.937 10.948  1.00 47.26 ? 1123 HOH A O   1 
HETATM 4114 O  O   . HOH F 6 .   ? 18.600 24.792 2.962   1.00 35.78 ? 1124 HOH A O   1 
HETATM 4115 O  O   . HOH F 6 .   ? 22.752 53.215 20.929  1.00 17.09 ? 1125 HOH A O   1 
HETATM 4116 O  O   . HOH F 6 .   ? 35.534 2.474  29.285  1.00 21.18 ? 1126 HOH A O   1 
HETATM 4117 O  O   . HOH F 6 .   ? 32.554 4.808  43.615  1.00 33.64 ? 1127 HOH A O   1 
HETATM 4118 O  O   . HOH F 6 .   ? 40.092 10.085 7.312   1.00 37.88 ? 1128 HOH A O   1 
HETATM 4119 O  O   . HOH F 6 .   ? 25.678 20.278 29.637  1.00 38.00 ? 1129 HOH A O   1 
HETATM 4120 O  O   . HOH F 6 .   ? 30.472 60.194 -4.934  1.00 38.48 ? 1130 HOH A O   1 
HETATM 4121 O  O   . HOH F 6 .   ? 13.325 38.490 2.557   1.00 25.63 ? 1131 HOH A O   1 
HETATM 4122 O  O   . HOH F 6 .   ? 32.907 2.895  24.460  1.00 32.38 ? 1132 HOH A O   1 
HETATM 4123 O  O   . HOH F 6 .   ? 15.675 19.291 9.831   1.00 42.02 ? 1133 HOH A O   1 
HETATM 4124 O  O   . HOH F 6 .   ? 48.018 48.059 16.442  1.00 31.74 ? 1134 HOH A O   1 
HETATM 4125 O  O   . HOH F 6 .   ? 21.799 17.804 13.291  1.00 65.80 ? 1135 HOH A O   1 
HETATM 4126 O  O   . HOH F 6 .   ? 49.069 8.894  9.700   1.00 45.28 ? 1136 HOH A O   1 
HETATM 4127 O  O   . HOH F 6 .   ? 43.691 32.075 26.177  1.00 35.14 ? 1137 HOH A O   1 
HETATM 4128 O  O   . HOH F 6 .   ? 28.028 17.699 33.843  1.00 42.49 ? 1138 HOH A O   1 
HETATM 4129 O  O   . HOH F 6 .   ? 17.197 31.179 31.227  1.00 33.72 ? 1139 HOH A O   1 
HETATM 4130 O  O   . HOH F 6 .   ? 38.051 5.188  44.300  1.00 34.99 ? 1140 HOH A O   1 
HETATM 4131 O  O   . HOH F 6 .   ? 33.580 0.951  22.760  1.00 25.19 ? 1141 HOH A O   1 
HETATM 4132 O  O   . HOH F 6 .   ? 36.295 15.134 40.972  1.00 28.13 ? 1142 HOH A O   1 
HETATM 4133 O  O   . HOH F 6 .   ? 9.461  29.679 9.161   1.00 39.54 ? 1143 HOH A O   1 
HETATM 4134 O  O   . HOH F 6 .   ? 23.552 16.774 7.672   1.00 43.43 ? 1144 HOH A O   1 
HETATM 4135 O  O   . HOH F 6 .   ? 56.930 40.713 0.447   1.00 60.07 ? 1145 HOH A O   1 
HETATM 4136 O  O   . HOH F 6 .   ? 48.437 24.263 30.595  1.00 18.42 ? 1146 HOH A O   1 
HETATM 4137 O  O   . HOH F 6 .   ? 51.903 34.921 13.278  1.00 48.01 ? 1147 HOH A O   1 
HETATM 4138 O  O   . HOH F 6 .   ? 40.361 21.532 42.020  1.00 48.22 ? 1148 HOH A O   1 
HETATM 4139 O  O   . HOH F 6 .   ? 30.602 10.747 10.103  1.00 36.03 ? 1149 HOH A O   1 
HETATM 4140 O  O   . HOH F 6 .   ? 51.076 37.351 24.330  1.00 27.67 ? 1150 HOH A O   1 
HETATM 4141 O  O   . HOH F 6 .   ? 48.323 32.555 4.507   1.00 50.73 ? 1151 HOH A O   1 
HETATM 4142 O  O   . HOH F 6 .   ? 48.465 7.065  32.369  1.00 33.85 ? 1152 HOH A O   1 
HETATM 4143 O  O   . HOH F 6 .   ? 40.553 39.587 -4.742  1.00 27.82 ? 1153 HOH A O   1 
HETATM 4144 O  O   . HOH F 6 .   ? 35.530 -0.902 31.908  1.00 36.72 ? 1154 HOH A O   1 
HETATM 4145 O  O   . HOH F 6 .   ? 37.902 17.306 41.365  1.00 36.02 ? 1155 HOH A O   1 
HETATM 4146 O  O   . HOH F 6 .   ? 50.710 26.543 23.683  1.00 37.32 ? 1156 HOH A O   1 
HETATM 4147 O  O   . HOH F 6 .   ? 30.035 22.895 16.407  1.00 32.71 ? 1157 HOH A O   1 
HETATM 4148 O  O   . HOH F 6 .   ? 53.284 19.173 25.972  1.00 40.36 ? 1158 HOH A O   1 
HETATM 4149 O  O   . HOH F 6 .   ? 47.955 6.719  11.515  1.00 32.42 ? 1159 HOH A O   1 
HETATM 4150 O  O   . HOH F 6 .   ? 54.813 11.854 9.932   1.00 48.62 ? 1160 HOH A O   1 
HETATM 4151 O  O   . HOH F 6 .   ? 43.052 21.353 -0.108  1.00 44.47 ? 1161 HOH A O   1 
HETATM 4152 O  O   . HOH F 6 .   ? 46.457 16.108 38.761  1.00 54.32 ? 1162 HOH A O   1 
HETATM 4153 O  O   . HOH F 6 .   ? 30.858 58.857 20.848  1.00 12.14 ? 1163 HOH A O   1 
HETATM 4154 O  O   . HOH F 6 .   ? 13.193 39.101 5.197   1.00 27.63 ? 1164 HOH A O   1 
HETATM 4155 O  O   . HOH F 6 .   ? 25.077 6.730  23.966  1.00 46.80 ? 1165 HOH A O   1 
HETATM 4156 O  O   . HOH F 6 .   ? 47.532 0.423  20.768  1.00 22.37 ? 1166 HOH A O   1 
HETATM 4157 O  O   . HOH F 6 .   ? 36.566 38.065 30.488  1.00 17.90 ? 1167 HOH A O   1 
HETATM 4158 O  O   . HOH F 6 .   ? 38.000 1.507  35.871  1.00 17.18 ? 1168 HOH A O   1 
HETATM 4159 O  O   . HOH F 6 .   ? 44.031 10.713 42.176  1.00 41.71 ? 1169 HOH A O   1 
HETATM 4160 O  O   . HOH F 6 .   ? 15.156 31.358 -7.578  1.00 27.75 ? 1170 HOH A O   1 
HETATM 4161 O  O   . HOH F 6 .   ? 11.673 20.167 9.974   1.00 31.88 ? 1171 HOH A O   1 
HETATM 4162 O  O   . HOH F 6 .   ? 20.028 48.335 -6.082  1.00 24.66 ? 1172 HOH A O   1 
HETATM 4163 O  O   . HOH F 6 .   ? 49.853 6.251  38.112  1.00 49.31 ? 1173 HOH A O   1 
HETATM 4164 O  O   . HOH F 6 .   ? 35.388 1.849  32.321  1.00 41.89 ? 1174 HOH A O   1 
HETATM 4165 O  O   . HOH F 6 .   ? 49.442 18.675 4.566   1.00 38.36 ? 1175 HOH A O   1 
HETATM 4166 O  O   . HOH F 6 .   ? 25.382 15.750 32.348  1.00 37.56 ? 1176 HOH A O   1 
HETATM 4167 O  O   . HOH F 6 .   ? 31.542 61.947 2.194   1.00 33.08 ? 1177 HOH A O   1 
HETATM 4168 O  O   . HOH F 6 .   ? 13.165 48.879 14.234  1.00 25.53 ? 1178 HOH A O   1 
HETATM 4169 O  O   . HOH F 6 .   ? 31.429 21.226 2.343   1.00 34.97 ? 1179 HOH A O   1 
HETATM 4170 O  O   . HOH F 6 .   ? 25.667 15.669 9.758   1.00 36.80 ? 1180 HOH A O   1 
HETATM 4171 O  O   . HOH F 6 .   ? 29.689 31.220 -3.784  1.00 33.05 ? 1181 HOH A O   1 
HETATM 4172 O  O   . HOH F 6 .   ? 33.198 18.370 5.439   1.00 36.83 ? 1182 HOH A O   1 
HETATM 4173 O  O   . HOH F 6 .   ? 53.046 34.310 16.285  1.00 49.84 ? 1183 HOH A O   1 
HETATM 4174 O  O   . HOH F 6 .   ? 25.606 13.518 17.781  1.00 56.52 ? 1184 HOH A O   1 
HETATM 4175 O  O   . HOH F 6 .   ? 49.050 35.794 -4.458  1.00 30.35 ? 1185 HOH A O   1 
HETATM 4176 O  O   . HOH F 6 .   ? 41.277 9.565  45.445  1.00 30.47 ? 1186 HOH A O   1 
HETATM 4177 O  O   . HOH F 6 .   ? 24.826 52.938 30.901  1.00 46.49 ? 1187 HOH A O   1 
HETATM 4178 O  O   . HOH F 6 .   ? 37.471 56.788 -5.221  1.00 44.18 ? 1188 HOH A O   1 
HETATM 4179 O  O   . HOH F 6 .   ? 37.002 31.930 -0.881  1.00 63.40 ? 1189 HOH A O   1 
HETATM 4180 O  O   . HOH F 6 .   ? 9.636  24.701 17.905  1.00 48.61 ? 1190 HOH A O   1 
HETATM 4181 O  O   . HOH F 6 .   ? 26.221 60.277 9.886   1.00 51.81 ? 1191 HOH A O   1 
HETATM 4182 O  O   . HOH F 6 .   ? 46.642 54.258 14.847  1.00 40.95 ? 1192 HOH A O   1 
HETATM 4183 O  O   . HOH F 6 .   ? 15.001 45.618 24.688  1.00 67.75 ? 1193 HOH A O   1 
HETATM 4184 O  O   . HOH F 6 .   ? 40.431 57.623 -4.359  1.00 63.82 ? 1194 HOH A O   1 
HETATM 4185 O  O   . HOH F 6 .   ? 20.229 44.896 -5.983  1.00 44.14 ? 1195 HOH A O   1 
HETATM 4186 O  O   . HOH F 6 .   ? 49.840 49.777 14.739  1.00 49.16 ? 1196 HOH A O   1 
HETATM 4187 O  O   . HOH F 6 .   ? 39.405 58.840 20.863  1.00 32.66 ? 1197 HOH A O   1 
HETATM 4188 O  O   . HOH F 6 .   ? 53.066 41.828 -8.710  1.00 47.18 ? 1198 HOH A O   1 
HETATM 4189 O  O   . HOH F 6 .   ? 12.237 36.861 9.096   1.00 63.78 ? 1199 HOH A O   1 
HETATM 4190 O  O   . HOH F 6 .   ? 52.932 46.057 6.272   1.00 49.43 ? 1200 HOH A O   1 
HETATM 4191 O  O   . HOH F 6 .   ? 27.220 55.976 20.539  1.00 30.39 ? 1201 HOH A O   1 
HETATM 4192 O  O   . HOH F 6 .   ? 35.390 14.260 3.970   1.00 56.17 ? 1202 HOH A O   1 
HETATM 4193 O  O   . HOH F 6 .   ? 38.959 63.065 6.740   1.00 31.97 ? 1203 HOH A O   1 
HETATM 4194 O  O   . HOH F 6 .   ? 52.992 43.173 5.838   1.00 47.38 ? 1204 HOH A O   1 
HETATM 4195 O  O   . HOH F 6 .   ? 42.260 29.713 26.979  1.00 35.25 ? 1205 HOH A O   1 
HETATM 4196 O  O   . HOH F 6 .   ? 22.766 17.322 10.292  1.00 54.43 ? 1206 HOH A O   1 
HETATM 4197 O  O   . HOH F 6 .   ? 34.845 8.127  10.524  1.00 44.33 ? 1207 HOH A O   1 
HETATM 4198 O  O   . HOH F 6 .   ? 21.510 11.330 27.822  1.00 32.20 ? 1208 HOH A O   1 
HETATM 4199 O  O   . HOH F 6 .   ? 35.604 17.211 2.823   1.00 53.89 ? 1209 HOH A O   1 
HETATM 4200 O  O   . HOH F 6 .   ? 27.616 55.141 27.569  1.00 28.26 ? 1210 HOH A O   1 
HETATM 4201 O  O   . HOH F 6 .   ? 33.529 8.973  45.908  1.00 59.67 ? 1211 HOH A O   1 
HETATM 4202 O  O   . HOH F 6 .   ? 47.026 54.340 3.859   1.00 44.17 ? 1212 HOH A O   1 
HETATM 4203 O  O   . HOH F 6 .   ? 49.522 9.954  33.346  1.00 64.73 ? 1213 HOH A O   1 
HETATM 4204 O  O   . HOH F 6 .   ? 34.905 56.870 23.336  1.00 32.81 ? 1214 HOH A O   1 
HETATM 4205 O  O   . HOH F 6 .   ? 43.001 -4.828 28.799  1.00 28.41 ? 1215 HOH A O   1 
HETATM 4206 O  O   . HOH F 6 .   ? 52.965 33.193 10.398  1.00 63.86 ? 1216 HOH A O   1 
HETATM 4207 O  O   . HOH F 6 .   ? 32.605 53.171 32.136  1.00 11.68 ? 1217 HOH A O   1 
HETATM 4208 O  O   . HOH F 6 .   ? 14.917 41.618 4.917   1.00 54.74 ? 1218 HOH A O   1 
HETATM 4209 O  O   . HOH F 6 .   ? 48.661 9.167  6.135   1.00 39.68 ? 1219 HOH A O   1 
HETATM 4210 O  O   . HOH F 6 .   ? 37.943 15.095 1.115   1.00 50.17 ? 1220 HOH A O   1 
HETATM 4211 O  O   . HOH F 6 .   ? 28.026 58.426 21.308  1.00 25.59 ? 1221 HOH A O   1 
HETATM 4212 O  O   . HOH F 6 .   ? 22.935 14.782 20.401  1.00 48.75 ? 1222 HOH A O   1 
HETATM 4213 O  O   . HOH F 6 .   ? 13.225 33.344 -6.575  1.00 36.00 ? 1223 HOH A O   1 
HETATM 4214 O  O   . HOH F 6 .   ? 50.278 1.323  24.530  1.00 66.78 ? 1224 HOH A O   1 
HETATM 4215 O  O   . HOH F 6 .   A 39.514 27.019 2.259   1.00 31.83 ? 1225 HOH A O   1 
HETATM 4216 O  O   . HOH F 6 .   A 49.076 52.416 8.754   1.00 51.88 ? 1226 HOH A O   1 
HETATM 4217 O  O   . HOH F 6 .   A 18.899 56.304 0.838   1.00 20.42 ? 1227 HOH A O   1 
HETATM 4218 O  O   . HOH F 6 .   A 35.286 28.118 -3.212  1.00 61.02 ? 1228 HOH A O   1 
HETATM 4219 O  O   . HOH F 6 .   A 45.243 59.849 8.872   1.00 53.77 ? 1229 HOH A O   1 
HETATM 4220 O  O   . HOH F 6 .   A 48.747 35.921 5.344   1.00 48.49 ? 1230 HOH A O   1 
HETATM 4221 O  O   . HOH F 6 .   A 19.154 57.708 3.157   1.00 56.05 ? 1231 HOH A O   1 
HETATM 4222 O  O   . HOH F 6 .   A 27.106 42.664 -5.895  1.00 32.65 ? 1232 HOH A O   1 
HETATM 4223 O  O   . HOH F 6 .   A 46.075 31.231 2.978   1.00 41.88 ? 1233 HOH A O   1 
HETATM 4224 O  O   . HOH F 6 .   A 42.444 24.154 -1.389  1.00 39.48 ? 1234 HOH A O   1 
HETATM 4225 O  O   . HOH F 6 .   A 15.838 35.991 -6.100  1.00 62.22 ? 1235 HOH A O   1 
HETATM 4226 O  O   . HOH F 6 .   A 41.108 37.570 -2.935  1.00 54.25 ? 1236 HOH A O   1 
HETATM 4227 O  O   . HOH F 6 .   A 54.098 41.509 -6.060  1.00 22.84 ? 1237 HOH A O   1 
HETATM 4228 O  O   . HOH F 6 .   A 38.378 35.914 -1.323  1.00 44.69 ? 1238 HOH A O   1 
HETATM 4229 O  O   . HOH F 6 .   A 30.660 33.224 -5.790  1.00 47.86 ? 1239 HOH A O   1 
HETATM 4230 O  O   . HOH F 6 .   A 18.823 28.964 -10.721 1.00 52.91 ? 1240 HOH A O   1 
HETATM 4231 O  O   . HOH F 6 .   B 29.744 6.179  44.117  1.00 53.06 ? 1241 HOH A O   1 
HETATM 4232 O  O   . HOH F 6 .   B 23.443 52.794 12.879  1.00 26.97 ? 1242 HOH A O   1 
HETATM 4233 O  O   . HOH F 6 .   B 40.799 -4.495 17.737  1.00 38.09 ? 1243 HOH A O   1 
HETATM 4234 O  O   . HOH F 6 .   B 34.450 -1.337 24.458  1.00 30.19 ? 1244 HOH A O   1 
HETATM 4235 O  O   . HOH F 6 .   B 41.634 62.483 7.606   1.00 47.82 ? 1245 HOH A O   1 
HETATM 4236 O  O   . HOH F 6 .   B 50.311 29.382 3.276   1.00 59.52 ? 1246 HOH A O   1 
HETATM 4237 O  O   . HOH F 6 .   B 11.279 28.895 -1.339  1.00 46.03 ? 1247 HOH A O   1 
HETATM 4238 O  O   . HOH F 6 .   B 14.405 37.068 -2.396  1.00 30.36 ? 1248 HOH A O   1 
HETATM 4239 O  O   . HOH F 6 .   B 14.792 34.404 -3.400  1.00 29.47 ? 1249 HOH A O   1 
HETATM 4240 O  O   . HOH F 6 .   B 15.899 32.418 -1.873  1.00 54.23 ? 1250 HOH A O   1 
HETATM 4241 O  O   . HOH F 6 .   B 17.458 29.484 -1.904  1.00 24.74 ? 1251 HOH A O   1 
HETATM 4242 O  O   . HOH F 6 .   B 15.487 26.119 2.437   1.00 53.24 ? 1252 HOH A O   1 
HETATM 4243 O  O   . HOH F 6 .   B 30.046 5.776  21.560  1.00 44.88 ? 1253 HOH A O   1 
HETATM 4244 O  O   . HOH F 6 .   B 42.353 42.651 27.783  1.00 18.89 ? 1254 HOH A O   1 
HETATM 4245 O  O   . HOH F 6 .   B 43.354 40.053 29.023  1.00 49.32 ? 1255 HOH A O   1 
HETATM 4246 O  O   . HOH F 6 .   B 44.697 37.707 26.555  1.00 48.90 ? 1256 HOH A O   1 
HETATM 4247 O  O   . HOH F 6 .   B 46.165 39.499 27.923  1.00 37.04 ? 1257 HOH A O   1 
HETATM 4248 O  O   . HOH F 6 .   B 42.308 37.492 28.163  1.00 59.64 ? 1258 HOH A O   1 
HETATM 4249 O  O   . HOH F 6 .   B 31.252 40.015 32.112  1.00 29.43 ? 1259 HOH A O   1 
HETATM 4250 O  O   . HOH F 6 .   B 31.181 38.331 35.162  1.00 43.41 ? 1260 HOH A O   1 
HETATM 4251 O  O   . HOH F 6 .   B 27.507 28.296 33.868  1.00 30.87 ? 1261 HOH A O   1 
HETATM 4252 O  O   . HOH F 6 .   B 10.845 27.849 22.664  1.00 67.21 ? 1262 HOH A O   1 
HETATM 4253 O  O   . HOH F 6 .   B 24.170 43.103 -6.818  1.00 52.98 ? 1263 HOH A O   1 
HETATM 4254 O  O   . HOH F 6 .   B 11.460 40.817 19.249  1.00 51.31 ? 1264 HOH A O   1 
HETATM 4255 O  O   . HOH F 6 .   B 13.557 41.803 28.486  1.00 56.41 ? 1265 HOH A O   1 
HETATM 4256 O  O   . HOH F 6 .   B 33.947 62.961 3.101   1.00 58.63 ? 1266 HOH A O   1 
HETATM 4257 O  O   . HOH F 6 .   B 36.406 64.023 4.222   1.00 59.00 ? 1267 HOH A O   1 
HETATM 4258 O  O   . HOH F 6 .   B 50.559 42.491 -9.593  1.00 64.86 ? 1268 HOH A O   1 
HETATM 4259 O  O   . HOH F 6 .   B 48.674 52.971 2.243   1.00 33.34 ? 1269 HOH A O   1 
HETATM 4260 O  O   . HOH F 6 .   B 23.604 54.057 26.328  1.00 42.82 ? 1270 HOH A O   1 
HETATM 4261 O  O   . HOH F 6 .   B 23.759 56.287 28.164  1.00 33.66 ? 1271 HOH A O   1 
HETATM 4262 O  O   . HOH F 6 .   B 36.697 55.838 25.151  1.00 53.21 ? 1272 HOH A O   1 
HETATM 4263 O  O   . HOH F 6 .   B 14.968 17.264 11.625  1.00 54.30 ? 1273 HOH A O   1 
HETATM 4264 O  O   . HOH F 6 .   B 52.776 7.716  26.749  1.00 32.49 ? 1274 HOH A O   1 
HETATM 4265 O  O   . HOH F 6 .   B 54.490 10.044 18.428  1.00 50.73 ? 1275 HOH A O   1 
HETATM 4266 O  O   . HOH F 6 .   B 48.718 17.830 37.741  1.00 64.08 ? 1276 HOH A O   1 
HETATM 4267 O  O   . HOH F 6 .   B 48.606 13.183 38.259  1.00 63.03 ? 1277 HOH A O   1 
HETATM 4268 O  O   . HOH F 6 .   B 29.564 1.615  31.615  1.00 34.03 ? 1278 HOH A O   1 
HETATM 4269 O  O   . HOH F 6 .   B 32.279 19.793 41.960  1.00 54.96 ? 1279 HOH A O   1 
HETATM 4270 O  O   . HOH F 6 .   B 35.881 15.377 44.367  1.00 61.35 ? 1280 HOH A O   1 
HETATM 4271 O  O   . HOH F 6 .   B 28.085 32.067 35.175  1.00 59.71 ? 1281 HOH A O   1 
HETATM 4272 O  O   . HOH F 6 .   B 28.053 60.768 -3.307  1.00 41.18 ? 1282 HOH A O   1 
HETATM 4273 O  O   . HOH F 6 .   B 10.365 21.537 12.051  1.00 61.49 ? 1283 HOH A O   1 
HETATM 4274 O  O   . HOH F 6 .   B 38.457 58.203 23.721  1.00 59.44 ? 1284 HOH A O   1 
HETATM 4275 O  O   . HOH F 6 .   B 34.621 1.737  34.863  1.00 39.22 ? 1285 HOH A O   1 
HETATM 4276 O  O   . HOH F 6 .   B 38.370 45.555 29.706  1.00 25.75 ? 1286 HOH A O   1 
HETATM 4277 O  O   . HOH F 6 .   B 52.736 30.249 0.552   1.00 40.36 ? 1287 HOH A O   1 
HETATM 4278 O  O   . HOH F 6 .   B 53.281 35.746 -0.832  1.00 38.24 ? 1288 HOH A O   1 
HETATM 4279 O  O   . HOH F 6 .   B 54.794 16.533 18.326  1.00 29.19 ? 1289 HOH A O   1 
HETATM 4280 O  O   . HOH F 6 .   B 56.966 40.338 3.446   1.00 58.51 ? 1290 HOH A O   1 
HETATM 4281 O  O   . HOH F 6 .   B 11.634 32.816 -4.220  1.00 49.57 ? 1291 HOH A O   1 
HETATM 4282 O  O   . HOH F 6 .   B 16.640 21.976 25.535  1.00 42.61 ? 1292 HOH A O   1 
HETATM 4283 O  O   . HOH F 6 .   B 42.179 47.752 21.210  1.00 41.15 ? 1293 HOH A O   1 
HETATM 4284 O  O   . HOH F 6 .   B 39.120 48.085 22.546  1.00 50.93 ? 1294 HOH A O   1 
HETATM 4285 O  O   . HOH F 6 .   B 41.560 50.340 22.263  1.00 48.67 ? 1295 HOH A O   1 
HETATM 4286 O  O   . HOH F 6 .   B 29.537 50.525 36.974  1.00 64.01 ? 1296 HOH A O   1 
HETATM 4287 O  O   . HOH F 6 .   B 38.090 53.676 29.316  1.00 69.40 ? 1297 HOH A O   1 
HETATM 4288 O  O   . HOH F 6 .   B 48.982 19.847 7.369   1.00 55.80 ? 1298 HOH A O   1 
HETATM 4289 O  O   . HOH F 6 .   B 49.159 18.812 10.370  1.00 50.93 ? 1299 HOH A O   1 
HETATM 4290 O  O   . HOH F 6 .   B 28.107 4.286  23.526  1.00 49.18 ? 1300 HOH A O   1 
HETATM 4291 O  O   . HOH F 6 .   B 15.987 53.389 -8.542  1.00 57.77 ? 1301 HOH A O   1 
HETATM 4292 O  O   . HOH F 6 .   B 45.824 13.865 0.865   1.00 63.46 ? 1302 HOH A O   1 
HETATM 4293 O  O   . HOH F 6 .   B 33.541 41.377 32.801  0.81 44.39 ? 1303 HOH A O   1 
HETATM 4294 O  O   . HOH F 6 .   B 33.816 57.336 -9.294  0.60 39.81 ? 1304 HOH A O   1 
HETATM 4295 O  O   . HOH F 6 .   B 55.958 41.422 -4.180  1.00 40.70 ? 1305 HOH A O   1 
HETATM 4296 O  O   . HOH F 6 .   B 15.317 36.202 31.509  1.00 62.23 ? 1306 HOH A O   1 
HETATM 4297 O  O   . HOH F 6 .   B 52.166 46.222 9.080   1.00 45.34 ? 1307 HOH A O   1 
HETATM 4298 O  O   . HOH F 6 .   B 23.385 55.504 23.561  1.00 65.87 ? 1308 HOH A O   1 
HETATM 4299 O  O   . HOH F 6 .   B 21.310 53.045 23.570  1.00 34.79 ? 1309 HOH A O   1 
HETATM 4300 O  O   . HOH F 6 .   B 12.562 37.839 -0.415  1.00 52.99 ? 1310 HOH A O   1 
HETATM 4301 O  O   . HOH F 6 .   B 41.008 32.682 26.922  1.00 64.02 ? 1311 HOH A O   1 
HETATM 4302 O  O   . HOH F 6 .   B 9.382  44.101 15.412  1.00 62.86 ? 1312 HOH A O   1 
HETATM 4303 O  O   . HOH F 6 .   B 14.762 51.383 17.817  1.00 40.67 ? 1313 HOH A O   1 
HETATM 4304 O  O   . HOH F 6 .   B 55.943 35.401 6.409   1.00 49.67 ? 1314 HOH A O   1 
HETATM 4305 O  O   . HOH F 6 .   B 50.684 41.534 22.336  1.00 24.91 ? 1315 HOH A O   1 
HETATM 4306 O  O   . HOH F 6 .   B 32.418 17.179 20.827  1.00 49.20 ? 1316 HOH A O   1 
HETATM 4307 O  O   . HOH F 6 .   B 21.254 13.042 25.255  1.00 60.86 ? 1317 HOH A O   1 
HETATM 4308 O  O   . HOH F 6 .   B 51.595 1.301  21.939  1.00 63.88 ? 1318 HOH A O   1 
HETATM 4309 O  O   . HOH F 6 .   B 30.323 10.457 47.028  1.00 66.97 ? 1319 HOH A O   1 
HETATM 4310 O  O   . HOH F 6 .   B 30.236 2.073  41.000  1.00 46.72 ? 1320 HOH A O   1 
HETATM 4311 O  O   . HOH F 6 .   B 40.727 34.382 29.038  1.00 55.53 ? 1321 HOH A O   1 
HETATM 4312 O  O   . HOH F 6 .   B 24.216 4.817  37.314  1.00 42.31 ? 1322 HOH A O   1 
HETATM 4313 O  O   . HOH F 6 .   B 50.342 2.208  27.619  1.00 55.67 ? 1323 HOH A O   1 
HETATM 4314 O  O   . HOH F 6 .   B 47.396 33.737 -0.968  1.00 68.90 ? 1324 HOH A O   1 
HETATM 4315 O  O   . HOH F 6 .   B 9.605  41.121 16.895  1.00 65.56 ? 1325 HOH A O   1 
HETATM 4316 O  O   . HOH F 6 .   B 19.518 48.438 25.120  1.00 61.87 ? 1326 HOH A O   1 
HETATM 4317 O  O   . HOH F 6 .   B 42.304 51.682 -9.072  1.00 47.17 ? 1327 HOH A O   1 
HETATM 4318 O  O   . HOH F 6 .   B 32.297 50.366 -11.440 1.00 53.99 ? 1328 HOH A O   1 
HETATM 4319 O  O   . HOH F 6 .   B 27.967 47.947 36.647  1.00 63.85 ? 1329 HOH A O   1 
HETATM 4320 O  O   . HOH F 6 .   B 18.376 47.711 30.950  1.00 65.23 ? 1330 HOH A O   1 
HETATM 4321 O  O   . HOH F 6 .   B 52.651 25.601 9.416   1.00 53.40 ? 1331 HOH A O   1 
HETATM 4322 O  O   . HOH F 6 .   B 54.825 30.142 18.685  1.00 45.06 ? 1332 HOH A O   1 
HETATM 4323 O  O   . HOH F 6 .   B 57.247 21.619 21.536  1.00 56.54 ? 1333 HOH A O   1 
HETATM 4324 O  O   . HOH F 6 .   B 56.935 24.715 14.234  1.00 43.25 ? 1334 HOH A O   1 
HETATM 4325 O  O   . HOH F 6 .   B 13.895 30.547 -2.791  1.00 46.11 ? 1335 HOH A O   1 
HETATM 4326 O  O   . HOH F 6 .   B 51.479 15.732 34.252  1.00 41.02 ? 1336 HOH A O   1 
HETATM 4327 O  O   . HOH F 6 .   B 51.592 15.228 30.775  1.00 61.22 ? 1337 HOH A O   1 
HETATM 4328 O  O   . HOH F 6 .   B 34.594 2.606  12.458  1.00 50.18 ? 1338 HOH A O   1 
HETATM 4329 O  O   . HOH F 6 .   B 39.546 27.827 29.378  1.00 33.76 ? 1339 HOH A O   1 
HETATM 4330 O  O   . HOH F 6 .   B 27.922 3.766  40.826  1.00 54.23 ? 1340 HOH A O   1 
HETATM 4331 O  O   . HOH F 6 .   B 10.516 35.952 21.105  1.00 59.75 ? 1341 HOH A O   1 
HETATM 4332 O  O   . HOH F 6 .   B 27.833 33.032 -7.634  1.00 69.08 ? 1342 HOH A O   1 
HETATM 4333 O  O   . HOH F 6 .   B 33.482 -2.490 26.975  1.00 65.02 ? 1343 HOH A O   1 
HETATM 4334 O  O   . HOH F 6 .   B 8.267  26.336 11.016  1.00 48.51 ? 1344 HOH A O   1 
HETATM 4335 O  O   . HOH F 6 .   B 44.427 21.090 3.542   1.00 61.61 ? 1345 HOH A O   1 
HETATM 4336 O  O   . HOH F 6 .   B 36.788 33.045 30.087  1.00 63.52 ? 1346 HOH A O   1 
HETATM 4337 O  O   . HOH F 6 .   B 16.018 49.997 -7.860  1.00 46.16 ? 1347 HOH A O   1 
HETATM 4338 O  O   . HOH F 6 .   B 46.851 21.346 6.037   1.00 56.94 ? 1348 HOH A O   1 
HETATM 4339 O  O   . HOH F 6 .   B 51.598 21.273 9.093   1.00 39.63 ? 1349 HOH A O   1 
HETATM 4340 O  O   . HOH F 6 .   B 29.840 43.448 -7.797  1.00 37.62 ? 1350 HOH A O   1 
HETATM 4341 O  O   . HOH F 6 .   B 27.131 19.011 31.723  1.00 49.86 ? 1351 HOH A O   1 
HETATM 4342 O  O   . HOH F 6 .   B 17.846 19.942 11.256  1.00 31.45 ? 1352 HOH A O   1 
HETATM 4343 O  O   . HOH F 6 .   B 54.368 14.573 8.368   1.00 44.93 ? 1353 HOH A O   1 
HETATM 4344 O  O   . HOH F 6 .   B 35.119 36.140 31.899  1.00 56.07 ? 1354 HOH A O   1 
HETATM 4345 O  O   . HOH F 6 .   B 36.879 23.301 0.241   1.00 61.55 ? 1355 HOH A O   1 
HETATM 4346 O  O   . HOH F 6 .   B 21.581 40.725 -8.280  1.00 45.16 ? 1356 HOH A O   1 
HETATM 4347 O  O   . HOH F 6 .   B 47.134 54.145 7.256   1.00 54.22 ? 1357 HOH A O   1 
HETATM 4348 O  O   . HOH F 6 .   B 51.624 38.933 21.994  1.00 45.27 ? 1358 HOH A O   1 
HETATM 4349 O  O   . HOH F 6 .   B 28.121 40.205 -6.378  1.00 58.00 ? 1359 HOH A O   1 
HETATM 4350 O  O   . HOH F 6 .   B 42.011 49.084 24.521  1.00 49.92 ? 1360 HOH A O   1 
HETATM 4351 O  O   . HOH F 6 .   B 47.050 16.807 2.286   1.00 66.54 ? 1361 HOH A O   1 
HETATM 4352 O  O   . HOH F 6 .   B 14.477 45.626 -1.461  1.00 68.27 ? 1362 HOH A O   1 
HETATM 4353 O  O   . HOH F 6 .   B 12.076 21.452 6.536   1.00 57.17 ? 1363 HOH A O   1 
HETATM 4354 O  O   . HOH F 6 .   B 23.674 5.520  41.713  1.00 59.41 ? 1364 HOH A O   1 
HETATM 4355 O  O   . HOH F 6 .   B 56.607 13.746 12.334  1.00 54.32 ? 1365 HOH A O   1 
HETATM 4356 O  O   . HOH F 6 .   B 58.292 13.343 10.176  1.00 47.52 ? 1366 HOH A O   1 
HETATM 4357 O  O   . HOH F 6 .   B 53.226 22.167 11.470  1.00 38.01 ? 1367 HOH A O   1 
HETATM 4358 O  O   . HOH F 6 .   B 19.668 33.096 -10.522 1.00 31.73 ? 1368 HOH A O   1 
HETATM 4359 O  O   . HOH F 6 .   B 19.660 31.116 -7.705  1.00 38.99 ? 1369 HOH A O   1 
HETATM 4360 O  O   . HOH F 6 .   B 23.212 29.723 -9.473  1.00 65.31 ? 1370 HOH A O   1 
HETATM 4361 O  O   . HOH F 6 .   B 25.977 30.896 -9.338  1.00 56.94 ? 1371 HOH A O   1 
HETATM 4362 O  O   . HOH F 6 .   B 27.127 26.005 -11.860 1.00 47.63 ? 1372 HOH A O   1 
HETATM 4363 O  O   . HOH F 6 .   B 25.245 26.284 -9.662  1.00 60.84 ? 1373 HOH A O   1 
HETATM 4364 O  O   . HOH F 6 .   B 20.454 26.927 -9.423  1.00 55.89 ? 1374 HOH A O   1 
HETATM 4365 O  O   . HOH F 6 .   B 45.916 47.190 25.123  1.00 53.89 ? 1375 HOH A O   1 
HETATM 4366 O  O   . HOH F 6 .   B 40.225 33.272 32.167  1.00 62.38 ? 1376 HOH A O   1 
HETATM 4367 O  O   . HOH F 6 .   B 9.141  34.148 18.218  1.00 57.54 ? 1377 HOH A O   1 
HETATM 4368 O  O   . HOH F 6 .   B 10.366 32.643 16.159  1.00 48.80 ? 1378 HOH A O   1 
HETATM 4369 O  O   . HOH F 6 .   B 12.293 24.619 24.277  1.00 57.80 ? 1379 HOH A O   1 
HETATM 4370 O  O   . HOH F 6 .   B 34.713 61.379 -8.207  1.00 61.52 ? 1380 HOH A O   1 
HETATM 4371 O  O   . HOH F 6 .   B 39.719 51.063 -8.863  1.00 41.25 ? 1381 HOH A O   1 
HETATM 4372 O  O   . HOH F 6 .   B 4.900  21.180 9.545   1.00 68.81 ? 1382 HOH A O   1 
HETATM 4373 O  O   . HOH F 6 .   B 46.525 57.650 12.807  1.00 64.83 ? 1383 HOH A O   1 
HETATM 4374 O  O   . HOH F 6 .   B 19.383 51.842 25.476  1.00 59.96 ? 1384 HOH A O   1 
HETATM 4375 O  O   . HOH F 6 .   B 17.720 50.637 30.704  1.00 61.61 ? 1385 HOH A O   1 
HETATM 4376 O  O   . HOH F 6 .   B 29.310 42.730 36.158  1.00 59.47 ? 1386 HOH A O   1 
HETATM 4377 O  O   . HOH F 6 .   B 34.433 30.695 -3.421  1.00 65.83 ? 1387 HOH A O   1 
HETATM 4378 O  O   . HOH F 6 .   B 33.396 26.277 -2.457  1.00 48.73 ? 1388 HOH A O   1 
HETATM 4379 O  O   . HOH F 6 .   B 32.403 16.127 3.499   1.00 52.07 ? 1389 HOH A O   1 
HETATM 4380 O  O   . HOH F 6 .   B 33.757 15.776 1.131   1.00 58.18 ? 1390 HOH A O   1 
HETATM 4381 O  O   . HOH F 6 .   B 32.637 14.074 -1.607  1.00 65.54 ? 1391 HOH A O   1 
HETATM 4382 O  O   . HOH F 6 .   B 46.882 28.020 27.094  1.00 45.92 ? 1392 HOH A O   1 
HETATM 4383 O  O   . HOH F 6 .   B 7.235  23.651 12.444  1.00 61.05 ? 1393 HOH A O   1 
HETATM 4384 O  O   . HOH F 6 .   B 6.131  26.000 13.131  1.00 60.58 ? 1394 HOH A O   1 
HETATM 4385 O  O   . HOH F 6 .   B 6.095  26.091 15.768  1.00 56.81 ? 1395 HOH A O   1 
HETATM 4386 O  O   . HOH F 6 .   B 14.356 18.886 27.252  1.00 61.18 ? 1396 HOH A O   1 
HETATM 4387 O  O   . HOH F 6 .   B 46.440 17.743 41.374  1.00 64.79 ? 1397 HOH A O   1 
HETATM 4388 O  O   . HOH F 6 .   B 33.019 1.262  26.981  1.00 50.63 ? 1398 HOH A O   1 
HETATM 4389 O  O   . HOH F 6 .   B 27.434 9.982  45.851  1.00 57.89 ? 1399 HOH A O   1 
# 
