data_6CF7
# 
_entry.id   6CF7 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.398 
_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   6CF7         pdb_00006cf7 10.2210/pdb6cf7/pdb 
WWPDB D_1000232653 ?            ?                   
# 
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 2019-02-13 
2 'Structure model' 1 1 2019-03-13 
3 'Structure model' 1 2 2019-03-20 
4 'Structure model' 1 3 2019-03-27 
5 'Structure model' 1 4 2019-04-10 
6 'Structure model' 1 5 2019-12-18 
7 'Structure model' 2 0 2020-07-29 
8 'Structure model' 2 1 2023-10-04 
9 'Structure model' 2 2 2024-11-06 
# 
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 7 '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' 'Data collection'            
2  2 'Structure model' 'Database references'        
3  3 'Structure model' 'Data collection'            
4  3 'Structure model' 'Database references'        
5  4 'Structure model' 'Data collection'            
6  4 'Structure model' 'Database references'        
7  5 'Structure model' 'Author supporting evidence' 
8  5 'Structure model' 'Data collection'            
9  6 'Structure model' 'Author supporting evidence' 
10 7 'Structure model' 'Atomic model'               
11 7 'Structure model' 'Data collection'            
12 7 'Structure model' 'Derived calculations'       
13 7 'Structure model' 'Structure summary'          
14 8 'Structure model' 'Data collection'            
15 8 'Structure model' 'Database references'        
16 8 'Structure model' 'Derived calculations'       
17 8 'Structure model' 'Refinement description'     
18 8 'Structure model' 'Structure summary'          
19 9 '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  2 'Structure model' citation                      
2  3 'Structure model' citation                      
3  3 'Structure model' citation_author               
4  4 'Structure model' citation_author               
5  5 'Structure model' pdbx_audit_support            
6  6 'Structure model' pdbx_audit_support            
7  7 'Structure model' atom_site                     
8  7 'Structure model' atom_site_anisotrop           
9  7 'Structure model' chem_comp                     
10 7 'Structure model' entity                        
11 7 'Structure model' pdbx_branch_scheme            
12 7 'Structure model' pdbx_chem_comp_identifier     
13 7 'Structure model' pdbx_entity_branch            
14 7 'Structure model' pdbx_entity_branch_descriptor 
15 7 'Structure model' pdbx_entity_branch_link       
16 7 'Structure model' pdbx_entity_branch_list       
17 7 'Structure model' pdbx_entity_nonpoly           
18 7 'Structure model' pdbx_nonpoly_scheme           
19 7 'Structure model' pdbx_struct_assembly_gen      
20 7 'Structure model' struct_asym                   
21 7 'Structure model' struct_conn                   
22 7 'Structure model' struct_site                   
23 7 'Structure model' struct_site_gen               
24 8 'Structure model' chem_comp                     
25 8 'Structure model' chem_comp_atom                
26 8 'Structure model' chem_comp_bond                
27 8 'Structure model' database_2                    
28 8 'Structure model' pdbx_initial_refinement_model 
29 8 'Structure model' struct_conn                   
30 9 'Structure model' pdbx_entry_details            
31 9 'Structure model' pdbx_modification_feature     
# 
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  2 'Structure model' '_citation.country'                        
2  2 'Structure model' '_citation.journal_abbrev'                 
3  2 'Structure model' '_citation.journal_id_ASTM'                
4  2 'Structure model' '_citation.journal_id_CSD'                 
5  2 'Structure model' '_citation.journal_id_ISSN'                
6  2 'Structure model' '_citation.pdbx_database_id_DOI'           
7  2 'Structure model' '_citation.title'                          
8  2 'Structure model' '_citation.year'                           
9  3 'Structure model' '_citation.journal_volume'                 
10 3 'Structure model' '_citation.pdbx_database_id_PubMed'        
11 3 'Structure model' '_citation.title'                          
12 4 'Structure model' '_citation_author.identifier_ORCID'        
13 5 'Structure model' '_pdbx_audit_support.funding_organization' 
14 6 'Structure model' '_pdbx_audit_support.funding_organization' 
15 7 'Structure model' '_atom_site.auth_asym_id'                  
16 7 'Structure model' '_atom_site.auth_seq_id'                   
17 7 'Structure model' '_atom_site.label_asym_id'                 
18 7 'Structure model' '_atom_site.label_entity_id'               
19 7 'Structure model' '_atom_site_anisotrop.pdbx_auth_asym_id'   
20 7 'Structure model' '_atom_site_anisotrop.pdbx_auth_seq_id'    
21 7 'Structure model' '_atom_site_anisotrop.pdbx_label_asym_id'  
22 7 'Structure model' '_chem_comp.name'                          
23 7 'Structure model' '_chem_comp.type'                          
24 7 'Structure model' '_pdbx_struct_assembly_gen.asym_id_list'   
25 7 'Structure model' '_struct_conn.pdbx_role'                   
26 7 'Structure model' '_struct_conn.ptnr1_auth_asym_id'          
27 7 'Structure model' '_struct_conn.ptnr1_auth_seq_id'           
28 7 'Structure model' '_struct_conn.ptnr1_label_asym_id'         
29 7 'Structure model' '_struct_conn.ptnr2_auth_asym_id'          
30 7 'Structure model' '_struct_conn.ptnr2_auth_seq_id'           
31 7 'Structure model' '_struct_conn.ptnr2_label_asym_id'         
32 8 'Structure model' '_chem_comp.pdbx_synonyms'                 
33 8 'Structure model' '_database_2.pdbx_DOI'                     
34 8 'Structure model' '_database_2.pdbx_database_accession'      
35 8 'Structure model' '_struct_conn.pdbx_leaving_atom_flag'      
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        6CF7 
_pdbx_database_status.recvd_initial_deposition_date   2018-02-13 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_nmr_data            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Kadam, R.U.'  1 ? 
'Wilson, I.A.' 2 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Science 
_citation.journal_id_ASTM           SCIEAS 
_citation.journal_id_CSD            0038 
_citation.journal_id_ISSN           1095-9203 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            363 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'A small-molecule fusion inhibitor of influenza virus is orally active in mice.' 
_citation.year                      2019 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1126/science.aar6221 
_citation.pdbx_database_id_PubMed   30846569 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'van Dongen, M.J.P.'           1  0000-0002-3026-2402 
primary 'Kadam, R.U.'                  2  0000-0002-1612-9250 
primary 'Juraszek, J.'                 3  0000-0001-7430-2771 
primary 'Lawson, E.'                   4  0000-0002-3015-0232 
primary 'Brandenburg, B.'              5  0000-0002-5025-3802 
primary 'Schmitz, F.'                  6  0000-0003-2303-9517 
primary 'Schepens, W.B.G.'             7  0000-0002-4915-6773 
primary 'Stoops, B.'                   8  0000-0002-1092-2696 
primary 'van Diepen, H.A.'             9  0000-0002-4822-7445 
primary 'Jongeneelen, M.'              10 ?                   
primary 'Tang, C.'                     11 0000-0002-1192-4116 
primary 'Vermond, J.'                  12 0000-0002-5766-8912 
primary 'van Eijgen-Obregoso Real, A.' 13 ?                   
primary 'Blokland, S.'                 14 ?                   
primary 'Garg, D.'                     15 ?                   
primary 'Yu, W.'                       16 ?                   
primary 'Goutier, W.'                  17 0000-0003-2680-5504 
primary 'Lanckacker, E.'               18 0000-0001-7323-7736 
primary 'Klap, J.M.'                   19 0000-0003-1188-3008 
primary 'Peeters, D.C.G.'              20 ?                   
primary 'Wu, J.'                       21 0000-0002-2434-2342 
primary 'Buyck, C.'                    22 0000-0002-5711-1161 
primary 'Jonckers, T.H.M.'             23 ?                   
primary 'Roymans, D.'                  24 0000-0003-1309-415X 
primary 'Roevens, P.'                  25 ?                   
primary 'Vogels, R.'                   26 ?                   
primary 'Koudstaal, W.'                27 ?                   
primary 'Friesen, R.H.E.'              28 ?                   
primary 'Raboisson, P.'                29 ?                   
primary 'Dhanak, D.'                   30 ?                   
primary 'Goudsmit, J.'                 31 ?                   
primary 'Wilson, I.A.'                 32 0000-0002-6469-2419 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man Hemagglutinin 36423.836 1  ? ? ? ? 
2 polymer     man Hemagglutinin 19956.131 1  ? ? ? ? 
3 branched    syn 
;alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose
;
748.682   1  ? ? ? ? 
4 branched    syn 
'beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose' 586.542   1  
? ? ? ? 
5 branched    syn '2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose' 424.401   2  ? ? ? ? 
6 non-polymer syn 2-acetamido-2-deoxy-beta-D-glucopyranose 221.208   1  ? ? ? ? 
7 non-polymer syn 
'N-[2-(2-{4-[(R)-(2-methyl-2H-tetrazol-5-yl)(phenyl)methyl]piperazine-1-carbonyl}pyridin-4-yl)-1,3-benzoxazol-5-yl]acetamide' 
537.572   1  ? ? ? ? 
8 water       nat water 18.015    52 ? ? ? ? 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no 
;DTICIGYHANNSTDTVDTVLEKNVTVTHSVNLLEDSHNGKLCRLKGIAPLQLGNCSVAGWILGNPECELLISRESWSYIV
EKPNPENGTCYPGHFADYEELREQLSSVSSFERFEIFPKESSWPNHTTTGVSASCSHNGESSFYKNLLWLTGKNGLYPNL
SKSYANNKEKEVLVLWGVHHPPNIGDQRALYHKENAYVSVVSSHYSRKFTPEIAKRPKVRDQEGRINYYWTLLEPGDTII
FEANGNLIAPRYAFALSRGFGSGIINSNAPMDECDAKCQTPQGAINSSLPFQNVHPVTIGECPKYVRSAKLRMVTGLRNI
PSIQSR
;
;DTICIGYHANNSTDTVDTVLEKNVTVTHSVNLLEDSHNGKLCRLKGIAPLQLGNCSVAGWILGNPECELLISRESWSYIV
EKPNPENGTCYPGHFADYEELREQLSSVSSFERFEIFPKESSWPNHTTTGVSASCSHNGESSFYKNLLWLTGKNGLYPNL
SKSYANNKEKEVLVLWGVHHPPNIGDQRALYHKENAYVSVVSSHYSRKFTPEIAKRPKVRDQEGRINYYWTLLEPGDTII
FEANGNLIAPRYAFALSRGFGSGIINSNAPMDECDAKCQTPQGAINSSLPFQNVHPVTIGECPKYVRSAKLRMVTGLRNI
PSIQSR
;
A ? 
2 'polypeptide(L)' no no 
;GLFGAIAGFIEGGWTGMVDGWYGYHHQNEQGSGYAADQKSTQNAINGITNKVNSVIEKMNTQFTAVGKEFNKLERRMENL
NKKVDDGFIDIWTYNAELLVLLENERTLDFHDSNVKNLYEKVKSQLKNNAKEIGNGCFEFYHKCNDECMESVKNGTYDYP
KYSEESKLNREKID
;
;GLFGAIAGFIEGGWTGMVDGWYGYHHQNEQGSGYAADQKSTQNAINGITNKVNSVIEKMNTQFTAVGKEFNKLERRMENL
NKKVDDGFIDIWTYNAELLVLLENERTLDFHDSNVKNLYEKVKSQLKNNAKEIGNGCFEFYHKCNDECMESVKNGTYDYP
KYSEESKLNREKID
;
B ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
6 2-acetamido-2-deoxy-beta-D-glucopyranose                                                                                      
NAG 
7 'N-[2-(2-{4-[(R)-(2-methyl-2H-tetrazol-5-yl)(phenyl)methyl]piperazine-1-carbonyl}pyridin-4-yl)-1,3-benzoxazol-5-yl]acetamide' 
EZ7 
8 water                                                                                                                         
HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   ASP n 
1 2   THR n 
1 3   ILE n 
1 4   CYS n 
1 5   ILE n 
1 6   GLY n 
1 7   TYR n 
1 8   HIS n 
1 9   ALA n 
1 10  ASN n 
1 11  ASN n 
1 12  SER n 
1 13  THR n 
1 14  ASP n 
1 15  THR n 
1 16  VAL n 
1 17  ASP n 
1 18  THR n 
1 19  VAL n 
1 20  LEU n 
1 21  GLU n 
1 22  LYS n 
1 23  ASN n 
1 24  VAL n 
1 25  THR n 
1 26  VAL n 
1 27  THR n 
1 28  HIS n 
1 29  SER n 
1 30  VAL n 
1 31  ASN n 
1 32  LEU n 
1 33  LEU n 
1 34  GLU n 
1 35  ASP n 
1 36  SER n 
1 37  HIS n 
1 38  ASN n 
1 39  GLY n 
1 40  LYS n 
1 41  LEU n 
1 42  CYS n 
1 43  ARG n 
1 44  LEU n 
1 45  LYS n 
1 46  GLY n 
1 47  ILE n 
1 48  ALA n 
1 49  PRO n 
1 50  LEU n 
1 51  GLN n 
1 52  LEU n 
1 53  GLY n 
1 54  ASN n 
1 55  CYS n 
1 56  SER n 
1 57  VAL n 
1 58  ALA n 
1 59  GLY n 
1 60  TRP n 
1 61  ILE n 
1 62  LEU n 
1 63  GLY n 
1 64  ASN n 
1 65  PRO n 
1 66  GLU n 
1 67  CYS n 
1 68  GLU n 
1 69  LEU n 
1 70  LEU n 
1 71  ILE n 
1 72  SER n 
1 73  ARG n 
1 74  GLU n 
1 75  SER n 
1 76  TRP n 
1 77  SER n 
1 78  TYR n 
1 79  ILE n 
1 80  VAL n 
1 81  GLU n 
1 82  LYS n 
1 83  PRO n 
1 84  ASN n 
1 85  PRO n 
1 86  GLU n 
1 87  ASN n 
1 88  GLY n 
1 89  THR n 
1 90  CYS n 
1 91  TYR n 
1 92  PRO n 
1 93  GLY n 
1 94  HIS n 
1 95  PHE n 
1 96  ALA n 
1 97  ASP n 
1 98  TYR n 
1 99  GLU n 
1 100 GLU n 
1 101 LEU n 
1 102 ARG n 
1 103 GLU n 
1 104 GLN n 
1 105 LEU n 
1 106 SER n 
1 107 SER n 
1 108 VAL n 
1 109 SER n 
1 110 SER n 
1 111 PHE n 
1 112 GLU n 
1 113 ARG n 
1 114 PHE n 
1 115 GLU n 
1 116 ILE n 
1 117 PHE n 
1 118 PRO n 
1 119 LYS n 
1 120 GLU n 
1 121 SER n 
1 122 SER n 
1 123 TRP n 
1 124 PRO n 
1 125 ASN n 
1 126 HIS n 
1 127 THR n 
1 128 THR n 
1 129 THR n 
1 130 GLY n 
1 131 VAL n 
1 132 SER n 
1 133 ALA n 
1 134 SER n 
1 135 CYS n 
1 136 SER n 
1 137 HIS n 
1 138 ASN n 
1 139 GLY n 
1 140 GLU n 
1 141 SER n 
1 142 SER n 
1 143 PHE n 
1 144 TYR n 
1 145 LYS n 
1 146 ASN n 
1 147 LEU n 
1 148 LEU n 
1 149 TRP n 
1 150 LEU n 
1 151 THR n 
1 152 GLY n 
1 153 LYS n 
1 154 ASN n 
1 155 GLY n 
1 156 LEU n 
1 157 TYR n 
1 158 PRO n 
1 159 ASN n 
1 160 LEU n 
1 161 SER n 
1 162 LYS n 
1 163 SER n 
1 164 TYR n 
1 165 ALA n 
1 166 ASN n 
1 167 ASN n 
1 168 LYS n 
1 169 GLU n 
1 170 LYS n 
1 171 GLU n 
1 172 VAL n 
1 173 LEU n 
1 174 VAL n 
1 175 LEU n 
1 176 TRP n 
1 177 GLY n 
1 178 VAL n 
1 179 HIS n 
1 180 HIS n 
1 181 PRO n 
1 182 PRO n 
1 183 ASN n 
1 184 ILE n 
1 185 GLY n 
1 186 ASP n 
1 187 GLN n 
1 188 ARG n 
1 189 ALA n 
1 190 LEU n 
1 191 TYR n 
1 192 HIS n 
1 193 LYS n 
1 194 GLU n 
1 195 ASN n 
1 196 ALA n 
1 197 TYR n 
1 198 VAL n 
1 199 SER n 
1 200 VAL n 
1 201 VAL n 
1 202 SER n 
1 203 SER n 
1 204 HIS n 
1 205 TYR n 
1 206 SER n 
1 207 ARG n 
1 208 LYS n 
1 209 PHE n 
1 210 THR n 
1 211 PRO n 
1 212 GLU n 
1 213 ILE n 
1 214 ALA n 
1 215 LYS n 
1 216 ARG n 
1 217 PRO n 
1 218 LYS n 
1 219 VAL n 
1 220 ARG n 
1 221 ASP n 
1 222 GLN n 
1 223 GLU n 
1 224 GLY n 
1 225 ARG n 
1 226 ILE n 
1 227 ASN n 
1 228 TYR n 
1 229 TYR n 
1 230 TRP n 
1 231 THR n 
1 232 LEU n 
1 233 LEU n 
1 234 GLU n 
1 235 PRO n 
1 236 GLY n 
1 237 ASP n 
1 238 THR n 
1 239 ILE n 
1 240 ILE n 
1 241 PHE n 
1 242 GLU n 
1 243 ALA n 
1 244 ASN n 
1 245 GLY n 
1 246 ASN n 
1 247 LEU n 
1 248 ILE n 
1 249 ALA n 
1 250 PRO n 
1 251 ARG n 
1 252 TYR n 
1 253 ALA n 
1 254 PHE n 
1 255 ALA n 
1 256 LEU n 
1 257 SER n 
1 258 ARG n 
1 259 GLY n 
1 260 PHE n 
1 261 GLY n 
1 262 SER n 
1 263 GLY n 
1 264 ILE n 
1 265 ILE n 
1 266 ASN n 
1 267 SER n 
1 268 ASN n 
1 269 ALA n 
1 270 PRO n 
1 271 MET n 
1 272 ASP n 
1 273 GLU n 
1 274 CYS n 
1 275 ASP n 
1 276 ALA n 
1 277 LYS n 
1 278 CYS n 
1 279 GLN n 
1 280 THR n 
1 281 PRO n 
1 282 GLN n 
1 283 GLY n 
1 284 ALA n 
1 285 ILE n 
1 286 ASN n 
1 287 SER n 
1 288 SER n 
1 289 LEU n 
1 290 PRO n 
1 291 PHE n 
1 292 GLN n 
1 293 ASN n 
1 294 VAL n 
1 295 HIS n 
1 296 PRO n 
1 297 VAL n 
1 298 THR n 
1 299 ILE n 
1 300 GLY n 
1 301 GLU n 
1 302 CYS n 
1 303 PRO n 
1 304 LYS n 
1 305 TYR n 
1 306 VAL n 
1 307 ARG n 
1 308 SER n 
1 309 ALA n 
1 310 LYS n 
1 311 LEU n 
1 312 ARG n 
1 313 MET n 
1 314 VAL n 
1 315 THR n 
1 316 GLY n 
1 317 LEU n 
1 318 ARG n 
1 319 ASN n 
1 320 ILE n 
1 321 PRO n 
1 322 SER n 
1 323 ILE n 
1 324 GLN n 
1 325 SER n 
1 326 ARG n 
2 1   GLY n 
2 2   LEU n 
2 3   PHE n 
2 4   GLY n 
2 5   ALA n 
2 6   ILE n 
2 7   ALA n 
2 8   GLY n 
2 9   PHE n 
2 10  ILE n 
2 11  GLU n 
2 12  GLY n 
2 13  GLY n 
2 14  TRP n 
2 15  THR n 
2 16  GLY n 
2 17  MET n 
2 18  VAL n 
2 19  ASP n 
2 20  GLY n 
2 21  TRP n 
2 22  TYR n 
2 23  GLY n 
2 24  TYR n 
2 25  HIS n 
2 26  HIS n 
2 27  GLN n 
2 28  ASN n 
2 29  GLU n 
2 30  GLN n 
2 31  GLY n 
2 32  SER n 
2 33  GLY n 
2 34  TYR n 
2 35  ALA n 
2 36  ALA n 
2 37  ASP n 
2 38  GLN n 
2 39  LYS n 
2 40  SER n 
2 41  THR n 
2 42  GLN n 
2 43  ASN n 
2 44  ALA n 
2 45  ILE n 
2 46  ASN n 
2 47  GLY n 
2 48  ILE n 
2 49  THR n 
2 50  ASN n 
2 51  LYS n 
2 52  VAL n 
2 53  ASN n 
2 54  SER n 
2 55  VAL n 
2 56  ILE n 
2 57  GLU n 
2 58  LYS n 
2 59  MET n 
2 60  ASN n 
2 61  THR n 
2 62  GLN n 
2 63  PHE n 
2 64  THR n 
2 65  ALA n 
2 66  VAL n 
2 67  GLY n 
2 68  LYS n 
2 69  GLU n 
2 70  PHE n 
2 71  ASN n 
2 72  LYS n 
2 73  LEU n 
2 74  GLU n 
2 75  ARG n 
2 76  ARG n 
2 77  MET n 
2 78  GLU n 
2 79  ASN n 
2 80  LEU n 
2 81  ASN n 
2 82  LYS n 
2 83  LYS n 
2 84  VAL n 
2 85  ASP n 
2 86  ASP n 
2 87  GLY n 
2 88  PHE n 
2 89  ILE n 
2 90  ASP n 
2 91  ILE n 
2 92  TRP n 
2 93  THR n 
2 94  TYR n 
2 95  ASN n 
2 96  ALA n 
2 97  GLU n 
2 98  LEU n 
2 99  LEU n 
2 100 VAL n 
2 101 LEU n 
2 102 LEU n 
2 103 GLU n 
2 104 ASN n 
2 105 GLU n 
2 106 ARG n 
2 107 THR n 
2 108 LEU n 
2 109 ASP n 
2 110 PHE n 
2 111 HIS n 
2 112 ASP n 
2 113 SER n 
2 114 ASN n 
2 115 VAL n 
2 116 LYS n 
2 117 ASN n 
2 118 LEU n 
2 119 TYR n 
2 120 GLU n 
2 121 LYS n 
2 122 VAL n 
2 123 LYS n 
2 124 SER n 
2 125 GLN n 
2 126 LEU n 
2 127 LYS n 
2 128 ASN n 
2 129 ASN n 
2 130 ALA n 
2 131 LYS n 
2 132 GLU n 
2 133 ILE n 
2 134 GLY n 
2 135 ASN n 
2 136 GLY n 
2 137 CYS n 
2 138 PHE n 
2 139 GLU n 
2 140 PHE n 
2 141 TYR n 
2 142 HIS n 
2 143 LYS n 
2 144 CYS n 
2 145 ASN n 
2 146 ASP n 
2 147 GLU n 
2 148 CYS n 
2 149 MET n 
2 150 GLU n 
2 151 SER n 
2 152 VAL n 
2 153 LYS n 
2 154 ASN n 
2 155 GLY n 
2 156 THR n 
2 157 TYR n 
2 158 ASP n 
2 159 TYR n 
2 160 PRO n 
2 161 LYS n 
2 162 TYR n 
2 163 SER n 
2 164 GLU n 
2 165 GLU n 
2 166 SER n 
2 167 LYS n 
2 168 LEU n 
2 169 ASN n 
2 170 ARG n 
2 171 GLU n 
2 172 LYS n 
2 173 ILE n 
2 174 ASP n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_entity_src_gen.gene_src_species 
_entity_src_gen.gene_src_strain 
_entity_src_gen.gene_src_tissue 
_entity_src_gen.gene_src_tissue_fraction 
_entity_src_gen.gene_src_details 
_entity_src_gen.pdbx_gene_src_fragment 
_entity_src_gen.pdbx_gene_src_scientific_name 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_entity_src_gen.pdbx_gene_src_variant 
_entity_src_gen.pdbx_gene_src_cell_line 
_entity_src_gen.pdbx_gene_src_atcc 
_entity_src_gen.pdbx_gene_src_organ 
_entity_src_gen.pdbx_gene_src_organelle 
_entity_src_gen.pdbx_gene_src_cell 
_entity_src_gen.pdbx_gene_src_cellular_location 
_entity_src_gen.host_org_common_name 
_entity_src_gen.pdbx_host_org_scientific_name 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_entity_src_gen.host_org_genus 
_entity_src_gen.pdbx_host_org_gene 
_entity_src_gen.pdbx_host_org_organ 
_entity_src_gen.host_org_species 
_entity_src_gen.pdbx_host_org_tissue 
_entity_src_gen.pdbx_host_org_tissue_fraction 
_entity_src_gen.pdbx_host_org_strain 
_entity_src_gen.pdbx_host_org_variant 
_entity_src_gen.pdbx_host_org_cell_line 
_entity_src_gen.pdbx_host_org_atcc 
_entity_src_gen.pdbx_host_org_culture_collection 
_entity_src_gen.pdbx_host_org_cell 
_entity_src_gen.pdbx_host_org_organelle 
_entity_src_gen.pdbx_host_org_cellular_location 
_entity_src_gen.pdbx_host_org_vector_type 
_entity_src_gen.pdbx_host_org_vector 
_entity_src_gen.host_org_details 
_entity_src_gen.expression_system_id 
_entity_src_gen.plasmid_name 
_entity_src_gen.plasmid_details 
_entity_src_gen.pdbx_description 
1 1 sample 'Biological sequence' 1 326 'A/Solomon Islands/3/2006(H1N1)' ? HA ? ?                              ? ? ? ? 
'Influenza A virus'                                  464623 ? ? ? ? ? ? ? 'cabbage looper' 'Trichoplusia ni' 7111 ? ? ? ? ? ? ? ? 
? ? ? ? ? ? baculovirus ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 174 ?                                ? HA ? 'A/Hong Kong/65446/2008(H1N1)' ? ? ? ? 
'Influenza A virus (A/Solomon Islands/3/2006(H1N1))' 464623 ? ? ? ? ? ? ? 'cabbage looper' 'Trichoplusia ni' 7111 ? ? ? ? ? ? ? ? 
? ? ? ? ? ? baculovirus ? ? ? ? ? ? 
# 
loop_
_pdbx_entity_branch.entity_id 
_pdbx_entity_branch.type 
3 oligosaccharide 
4 oligosaccharide 
5 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 3 DManpa1-3DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-                                                           
'Glycam Condensed Sequence' GMML       1.0   
2 3 'WURCS=2.0/3,4,3/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5][a1122h-1a_1-5]/1-1-2-3/a4-b1_b4-c1_c3-d1' WURCS PDB2Glycan 1.1.0 
3 3 '[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(3+1)][a-D-Manp]{}}}}}'            LINUCS PDB-CARE   ?     
4 4 DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-                                                                    
'Glycam Condensed Sequence' GMML       1.0   
5 4 'WURCS=2.0/2,3,2/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5]/1-1-2/a4-b1_b4-c1'                        WURCS PDB2Glycan 1.1.0 
6 4 '[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{}}}}'                               LINUCS PDB-CARE   ?     
7 5 DGlcpNAcb1-4DGlcpNAcb1-                                                                             
'Glycam Condensed Sequence' GMML       1.0   
8 5 'WURCS=2.0/1,2,1/[a2122h-1b_1-5_2*NCC/3=O]/1-1/a4-b1'                                               WURCS PDB2Glycan 1.1.0 
9 5 '[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{}}}'                                                  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 3 2 NAG C1 O1 1 NAG O4 HO4 sing ? 
2 3 3 BMA C1 O1 2 NAG O4 HO4 sing ? 
3 3 4 MAN C1 O1 3 BMA O3 HO3 sing ? 
4 4 2 NAG C1 O1 1 NAG O4 HO4 sing ? 
5 4 3 BMA C1 O1 2 NAG O4 HO4 sing ? 
6 5 2 NAG C1 O1 1 NAG 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 
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 
BMA 'D-saccharide, beta linking'  . beta-D-mannopyranose 'beta-D-mannose; D-mannose; mannose' 'C6 H12 O6'      180.156 
CYS 'L-peptide linking'           y CYSTEINE ? 'C3 H7 N O2 S'   121.158 
EZ7 non-polymer                   . 
'N-[2-(2-{4-[(R)-(2-methyl-2H-tetrazol-5-yl)(phenyl)methyl]piperazine-1-carbonyl}pyridin-4-yl)-1,3-benzoxazol-5-yl]acetamide' ? 
'C28 H27 N9 O3'  537.572 
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 
MAN 'D-saccharide, alpha linking' . alpha-D-mannopyranose 'alpha-D-mannose; D-mannose; mannose' 'C6 H12 O6'      180.156 
MET 'L-peptide linking'           y METHIONINE ? 'C5 H11 N O2 S'  149.211 
NAG 'D-saccharide, beta linking'  . 2-acetamido-2-deoxy-beta-D-glucopyranose 
;N-acetyl-beta-D-glucosamine; 2-acetamido-2-deoxy-beta-D-glucose; 2-acetamido-2-deoxy-D-glucose; 2-acetamido-2-deoxy-glucose; N-ACETYL-D-GLUCOSAMINE
;
'C8 H15 N O6'    221.208 
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 
BMA 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DManpb                         
BMA 'COMMON NAME'                         GMML     1.0 b-D-mannopyranose              
BMA 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 b-D-Manp                       
BMA 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 Man                            
MAN 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DManpa                         
MAN 'COMMON NAME'                         GMML     1.0 a-D-mannopyranose              
MAN 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 a-D-Manp                       
MAN 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 Man                            
NAG 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DGlcpNAcb                      
NAG 'COMMON NAME'                         GMML     1.0 N-acetyl-b-D-glucopyranosamine 
NAG 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 b-D-GlcpNAc                    
NAG 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 GlcNAc                         
# 
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   ASP 1   11  11  ASP ASP A . n 
A 1 2   THR 2   12  12  THR THR A . n 
A 1 3   ILE 3   13  13  ILE ILE A . n 
A 1 4   CYS 4   14  14  CYS CYS A . n 
A 1 5   ILE 5   15  15  ILE ILE A . n 
A 1 6   GLY 6   16  16  GLY GLY A . n 
A 1 7   TYR 7   17  17  TYR TYR A . n 
A 1 8   HIS 8   18  18  HIS HIS A . n 
A 1 9   ALA 9   19  19  ALA ALA A . n 
A 1 10  ASN 10  20  20  ASN ASN A . n 
A 1 11  ASN 11  21  21  ASN ASN A . n 
A 1 12  SER 12  22  22  SER SER A . n 
A 1 13  THR 13  23  23  THR THR A . n 
A 1 14  ASP 14  24  24  ASP ASP A . n 
A 1 15  THR 15  25  25  THR THR A . n 
A 1 16  VAL 16  26  26  VAL VAL A . n 
A 1 17  ASP 17  27  27  ASP ASP A . n 
A 1 18  THR 18  28  28  THR THR A . n 
A 1 19  VAL 19  29  29  VAL VAL A . n 
A 1 20  LEU 20  30  30  LEU LEU A . n 
A 1 21  GLU 21  31  31  GLU GLU A . n 
A 1 22  LYS 22  32  32  LYS LYS A . n 
A 1 23  ASN 23  33  33  ASN ASN A . n 
A 1 24  VAL 24  34  34  VAL VAL A . n 
A 1 25  THR 25  35  35  THR THR A . n 
A 1 26  VAL 26  36  36  VAL VAL A . n 
A 1 27  THR 27  37  37  THR THR A . n 
A 1 28  HIS 28  38  38  HIS HIS A . n 
A 1 29  SER 29  39  39  SER SER A . n 
A 1 30  VAL 30  40  40  VAL VAL A . n 
A 1 31  ASN 31  41  41  ASN ASN A . n 
A 1 32  LEU 32  42  42  LEU LEU A . n 
A 1 33  LEU 33  43  43  LEU LEU A . n 
A 1 34  GLU 34  44  44  GLU GLU A . n 
A 1 35  ASP 35  45  45  ASP ASP A . n 
A 1 36  SER 36  46  46  SER SER A . n 
A 1 37  HIS 37  47  47  HIS HIS A . n 
A 1 38  ASN 38  48  48  ASN ASN A . n 
A 1 39  GLY 39  49  49  GLY GLY A . n 
A 1 40  LYS 40  50  50  LYS LYS A . n 
A 1 41  LEU 41  51  51  LEU LEU A . n 
A 1 42  CYS 42  52  52  CYS CYS A . n 
A 1 43  ARG 43  53  53  ARG ARG A . n 
A 1 44  LEU 44  54  54  LEU LEU A . n 
A 1 45  LYS 45  54  54  LYS LYS A A n 
A 1 46  GLY 46  55  55  GLY GLY A . n 
A 1 47  ILE 47  56  56  ILE ILE A . n 
A 1 48  ALA 48  57  57  ALA ALA A . n 
A 1 49  PRO 49  58  58  PRO PRO A . n 
A 1 50  LEU 50  59  59  LEU LEU A . n 
A 1 51  GLN 51  60  60  GLN GLN A . n 
A 1 52  LEU 52  61  61  LEU LEU A . n 
A 1 53  GLY 53  62  62  GLY GLY A . n 
A 1 54  ASN 54  63  63  ASN ASN A . n 
A 1 55  CYS 55  64  64  CYS CYS A . n 
A 1 56  SER 56  65  65  SER SER A . n 
A 1 57  VAL 57  66  66  VAL VAL A . n 
A 1 58  ALA 58  67  67  ALA ALA A . n 
A 1 59  GLY 59  68  68  GLY GLY A . n 
A 1 60  TRP 60  69  69  TRP TRP A . n 
A 1 61  ILE 61  70  70  ILE ILE A . n 
A 1 62  LEU 62  71  71  LEU LEU A . n 
A 1 63  GLY 63  72  72  GLY GLY A . n 
A 1 64  ASN 64  73  73  ASN ASN A . n 
A 1 65  PRO 65  74  74  PRO PRO A . n 
A 1 66  GLU 66  75  75  GLU GLU A . n 
A 1 67  CYS 67  76  76  CYS CYS A . n 
A 1 68  GLU 68  77  77  GLU GLU A . n 
A 1 69  LEU 69  78  78  LEU LEU A . n 
A 1 70  LEU 70  79  79  LEU LEU A . n 
A 1 71  ILE 71  80  80  ILE ILE A . n 
A 1 72  SER 72  81  81  SER SER A . n 
A 1 73  ARG 73  82  82  ARG ARG A . n 
A 1 74  GLU 74  83  83  GLU GLU A . n 
A 1 75  SER 75  83  83  SER SER A A n 
A 1 76  TRP 76  84  84  TRP TRP A . n 
A 1 77  SER 77  85  85  SER SER A . n 
A 1 78  TYR 78  86  86  TYR TYR A . n 
A 1 79  ILE 79  87  87  ILE ILE A . n 
A 1 80  VAL 80  88  88  VAL VAL A . n 
A 1 81  GLU 81  89  89  GLU GLU A . n 
A 1 82  LYS 82  90  90  LYS LYS A . n 
A 1 83  PRO 83  91  91  PRO PRO A . n 
A 1 84  ASN 84  92  92  ASN ASN A . n 
A 1 85  PRO 85  93  93  PRO PRO A . n 
A 1 86  GLU 86  94  94  GLU GLU A . n 
A 1 87  ASN 87  95  95  ASN ASN A . n 
A 1 88  GLY 88  95  95  GLY GLY A A n 
A 1 89  THR 89  96  96  THR THR A . n 
A 1 90  CYS 90  97  97  CYS CYS A . n 
A 1 91  TYR 91  98  98  TYR TYR A . n 
A 1 92  PRO 92  99  99  PRO PRO A . n 
A 1 93  GLY 93  100 100 GLY GLY A . n 
A 1 94  HIS 94  101 101 HIS HIS A . n 
A 1 95  PHE 95  102 102 PHE PHE A . n 
A 1 96  ALA 96  103 103 ALA ALA A . n 
A 1 97  ASP 97  104 104 ASP ASP A . n 
A 1 98  TYR 98  105 105 TYR TYR A . n 
A 1 99  GLU 99  106 106 GLU GLU A . n 
A 1 100 GLU 100 107 107 GLU GLU A . n 
A 1 101 LEU 101 108 108 LEU LEU A . n 
A 1 102 ARG 102 109 109 ARG ARG A . n 
A 1 103 GLU 103 110 110 GLU GLU A . n 
A 1 104 GLN 104 111 111 GLN GLN A . n 
A 1 105 LEU 105 112 112 LEU LEU A . n 
A 1 106 SER 106 113 113 SER SER A . n 
A 1 107 SER 107 114 114 SER SER A . n 
A 1 108 VAL 108 115 115 VAL VAL A . n 
A 1 109 SER 109 116 116 SER SER A . n 
A 1 110 SER 110 117 117 SER SER A . n 
A 1 111 PHE 111 118 118 PHE PHE A . n 
A 1 112 GLU 112 119 119 GLU GLU A . n 
A 1 113 ARG 113 120 120 ARG ARG A . n 
A 1 114 PHE 114 121 121 PHE PHE A . n 
A 1 115 GLU 115 122 122 GLU GLU A . n 
A 1 116 ILE 116 123 123 ILE ILE A . n 
A 1 117 PHE 117 124 124 PHE PHE A . n 
A 1 118 PRO 118 125 125 PRO PRO A . n 
A 1 119 LYS 119 125 125 LYS LYS A A n 
A 1 120 GLU 120 125 125 GLU GLU A B n 
A 1 121 SER 121 125 125 SER SER A C n 
A 1 122 SER 122 126 126 SER SER A . n 
A 1 123 TRP 123 127 127 TRP TRP A . n 
A 1 124 PRO 124 128 128 PRO PRO A . n 
A 1 125 ASN 125 129 129 ASN ASN A . n 
A 1 126 HIS 126 130 130 HIS HIS A . n 
A 1 127 THR 127 131 131 THR THR A . n 
A 1 128 THR 128 132 132 THR THR A . n 
A 1 129 THR 129 133 133 THR THR A . n 
A 1 130 GLY 130 134 134 GLY GLY A . n 
A 1 131 VAL 131 135 135 VAL VAL A . n 
A 1 132 SER 132 136 136 SER SER A . n 
A 1 133 ALA 133 137 137 ALA ALA A . n 
A 1 134 SER 134 138 138 SER SER A . n 
A 1 135 CYS 135 139 139 CYS CYS A . n 
A 1 136 SER 136 140 140 SER SER A . n 
A 1 137 HIS 137 141 141 HIS HIS A . n 
A 1 138 ASN 138 142 142 ASN ASN A . n 
A 1 139 GLY 139 143 143 GLY GLY A . n 
A 1 140 GLU 140 144 144 GLU GLU A . n 
A 1 141 SER 141 145 145 SER SER A . n 
A 1 142 SER 142 146 146 SER SER A . n 
A 1 143 PHE 143 147 147 PHE PHE A . n 
A 1 144 TYR 144 148 148 TYR TYR A . n 
A 1 145 LYS 145 149 149 LYS LYS A . n 
A 1 146 ASN 146 150 150 ASN ASN A . n 
A 1 147 LEU 147 151 151 LEU LEU A . n 
A 1 148 LEU 148 152 152 LEU LEU A . n 
A 1 149 TRP 149 153 153 TRP TRP A . n 
A 1 150 LEU 150 154 154 LEU LEU A . n 
A 1 151 THR 151 155 155 THR THR A . n 
A 1 152 GLY 152 156 156 GLY GLY A . n 
A 1 153 LYS 153 157 157 LYS LYS A . n 
A 1 154 ASN 154 158 158 ASN ASN A . n 
A 1 155 GLY 155 159 159 GLY GLY A . n 
A 1 156 LEU 156 160 160 LEU LEU A . n 
A 1 157 TYR 157 161 161 TYR TYR A . n 
A 1 158 PRO 158 162 162 PRO PRO A . n 
A 1 159 ASN 159 163 163 ASN ASN A . n 
A 1 160 LEU 160 164 164 LEU LEU A . n 
A 1 161 SER 161 165 165 SER SER A . n 
A 1 162 LYS 162 166 166 LYS LYS A . n 
A 1 163 SER 163 167 167 SER SER A . n 
A 1 164 TYR 164 168 168 TYR TYR A . n 
A 1 165 ALA 165 169 169 ALA ALA A . n 
A 1 166 ASN 166 170 170 ASN ASN A . n 
A 1 167 ASN 167 171 171 ASN ASN A . n 
A 1 168 LYS 168 172 172 LYS LYS A . n 
A 1 169 GLU 169 173 173 GLU GLU A . n 
A 1 170 LYS 170 174 174 LYS LYS A . n 
A 1 171 GLU 171 175 175 GLU GLU A . n 
A 1 172 VAL 172 176 176 VAL VAL A . n 
A 1 173 LEU 173 177 177 LEU LEU A . n 
A 1 174 VAL 174 178 178 VAL VAL A . n 
A 1 175 LEU 175 179 179 LEU LEU A . n 
A 1 176 TRP 176 180 180 TRP TRP A . n 
A 1 177 GLY 177 181 181 GLY GLY A . n 
A 1 178 VAL 178 182 182 VAL VAL A . n 
A 1 179 HIS 179 183 183 HIS HIS A . n 
A 1 180 HIS 180 184 184 HIS HIS A . n 
A 1 181 PRO 181 185 185 PRO PRO A . n 
A 1 182 PRO 182 186 186 PRO PRO A . n 
A 1 183 ASN 183 187 187 ASN ASN A . n 
A 1 184 ILE 184 188 188 ILE ILE A . n 
A 1 185 GLY 185 189 189 GLY GLY A . n 
A 1 186 ASP 186 190 190 ASP ASP A . n 
A 1 187 GLN 187 191 191 GLN GLN A . n 
A 1 188 ARG 188 192 192 ARG ARG A . n 
A 1 189 ALA 189 193 193 ALA ALA A . n 
A 1 190 LEU 190 194 194 LEU LEU A . n 
A 1 191 TYR 191 195 195 TYR TYR A . n 
A 1 192 HIS 192 196 196 HIS HIS A . n 
A 1 193 LYS 193 197 197 LYS LYS A . n 
A 1 194 GLU 194 198 198 GLU GLU A . n 
A 1 195 ASN 195 199 199 ASN ASN A . n 
A 1 196 ALA 196 200 200 ALA ALA A . n 
A 1 197 TYR 197 201 201 TYR TYR A . n 
A 1 198 VAL 198 202 202 VAL VAL A . n 
A 1 199 SER 199 203 203 SER SER A . n 
A 1 200 VAL 200 204 204 VAL VAL A . n 
A 1 201 VAL 201 205 205 VAL VAL A . n 
A 1 202 SER 202 206 206 SER SER A . n 
A 1 203 SER 203 207 207 SER SER A . n 
A 1 204 HIS 204 208 208 HIS HIS A . n 
A 1 205 TYR 205 209 209 TYR TYR A . n 
A 1 206 SER 206 210 210 SER SER A . n 
A 1 207 ARG 207 211 211 ARG ARG A . n 
A 1 208 LYS 208 212 212 LYS LYS A . n 
A 1 209 PHE 209 213 213 PHE PHE A . n 
A 1 210 THR 210 214 214 THR THR A . n 
A 1 211 PRO 211 215 215 PRO PRO A . n 
A 1 212 GLU 212 216 216 GLU GLU A . n 
A 1 213 ILE 213 217 217 ILE ILE A . n 
A 1 214 ALA 214 218 218 ALA ALA A . n 
A 1 215 LYS 215 219 219 LYS LYS A . n 
A 1 216 ARG 216 220 220 ARG ARG A . n 
A 1 217 PRO 217 221 221 PRO PRO A . n 
A 1 218 LYS 218 222 222 LYS LYS A . n 
A 1 219 VAL 219 223 223 VAL VAL A . n 
A 1 220 ARG 220 224 224 ARG ARG A . n 
A 1 221 ASP 221 225 225 ASP ASP A . n 
A 1 222 GLN 222 226 226 GLN GLN A . n 
A 1 223 GLU 223 227 227 GLU GLU A . n 
A 1 224 GLY 224 228 228 GLY GLY A . n 
A 1 225 ARG 225 229 229 ARG ARG A . n 
A 1 226 ILE 226 230 230 ILE ILE A . n 
A 1 227 ASN 227 231 231 ASN ASN A . n 
A 1 228 TYR 228 232 232 TYR TYR A . n 
A 1 229 TYR 229 233 233 TYR TYR A . n 
A 1 230 TRP 230 234 234 TRP TRP A . n 
A 1 231 THR 231 235 235 THR THR A . n 
A 1 232 LEU 232 236 236 LEU LEU A . n 
A 1 233 LEU 233 237 237 LEU LEU A . n 
A 1 234 GLU 234 238 238 GLU GLU A . n 
A 1 235 PRO 235 239 239 PRO PRO A . n 
A 1 236 GLY 236 240 240 GLY GLY A . n 
A 1 237 ASP 237 241 241 ASP ASP A . n 
A 1 238 THR 238 242 242 THR THR A . n 
A 1 239 ILE 239 243 243 ILE ILE A . n 
A 1 240 ILE 240 244 244 ILE ILE A . n 
A 1 241 PHE 241 245 245 PHE PHE A . n 
A 1 242 GLU 242 246 246 GLU GLU A . n 
A 1 243 ALA 243 247 247 ALA ALA A . n 
A 1 244 ASN 244 248 248 ASN ASN A . n 
A 1 245 GLY 245 249 249 GLY GLY A . n 
A 1 246 ASN 246 250 250 ASN ASN A . n 
A 1 247 LEU 247 251 251 LEU LEU A . n 
A 1 248 ILE 248 252 252 ILE ILE A . n 
A 1 249 ALA 249 253 253 ALA ALA A . n 
A 1 250 PRO 250 254 254 PRO PRO A . n 
A 1 251 ARG 251 255 255 ARG ARG A . n 
A 1 252 TYR 252 256 256 TYR TYR A . n 
A 1 253 ALA 253 257 257 ALA ALA A . n 
A 1 254 PHE 254 258 258 PHE PHE A . n 
A 1 255 ALA 255 259 259 ALA ALA A . n 
A 1 256 LEU 256 260 260 LEU LEU A . n 
A 1 257 SER 257 261 261 SER SER A . n 
A 1 258 ARG 258 262 262 ARG ARG A . n 
A 1 259 GLY 259 263 263 GLY GLY A . n 
A 1 260 PHE 260 264 264 PHE PHE A . n 
A 1 261 GLY 261 264 264 GLY GLY A A n 
A 1 262 SER 262 265 265 SER SER A . n 
A 1 263 GLY 263 266 266 GLY GLY A . n 
A 1 264 ILE 264 267 267 ILE ILE A . n 
A 1 265 ILE 265 268 268 ILE ILE A . n 
A 1 266 ASN 266 269 269 ASN ASN A . n 
A 1 267 SER 267 270 270 SER SER A . n 
A 1 268 ASN 268 271 271 ASN ASN A . n 
A 1 269 ALA 269 272 272 ALA ALA A . n 
A 1 270 PRO 270 273 273 PRO PRO A . n 
A 1 271 MET 271 274 274 MET MET A . n 
A 1 272 ASP 272 275 275 ASP ASP A . n 
A 1 273 GLU 273 276 276 GLU GLU A . n 
A 1 274 CYS 274 277 277 CYS CYS A . n 
A 1 275 ASP 275 278 278 ASP ASP A . n 
A 1 276 ALA 276 279 279 ALA ALA A . n 
A 1 277 LYS 277 280 280 LYS LYS A . n 
A 1 278 CYS 278 281 281 CYS CYS A . n 
A 1 279 GLN 279 282 282 GLN GLN A . n 
A 1 280 THR 280 283 283 THR THR A . n 
A 1 281 PRO 281 284 284 PRO PRO A . n 
A 1 282 GLN 282 285 285 GLN GLN A . n 
A 1 283 GLY 283 286 286 GLY GLY A . n 
A 1 284 ALA 284 287 287 ALA ALA A . n 
A 1 285 ILE 285 288 288 ILE ILE A . n 
A 1 286 ASN 286 289 289 ASN ASN A . n 
A 1 287 SER 287 290 290 SER SER A . n 
A 1 288 SER 288 291 291 SER SER A . n 
A 1 289 LEU 289 292 292 LEU LEU A . n 
A 1 290 PRO 290 293 293 PRO PRO A . n 
A 1 291 PHE 291 294 294 PHE PHE A . n 
A 1 292 GLN 292 295 295 GLN GLN A . n 
A 1 293 ASN 293 296 296 ASN ASN A . n 
A 1 294 VAL 294 297 297 VAL VAL A . n 
A 1 295 HIS 295 298 298 HIS HIS A . n 
A 1 296 PRO 296 299 299 PRO PRO A . n 
A 1 297 VAL 297 300 300 VAL VAL A . n 
A 1 298 THR 298 301 301 THR THR A . n 
A 1 299 ILE 299 302 302 ILE ILE A . n 
A 1 300 GLY 300 303 303 GLY GLY A . n 
A 1 301 GLU 301 304 304 GLU GLU A . n 
A 1 302 CYS 302 305 305 CYS CYS A . n 
A 1 303 PRO 303 306 306 PRO PRO A . n 
A 1 304 LYS 304 307 307 LYS LYS A . n 
A 1 305 TYR 305 308 308 TYR TYR A . n 
A 1 306 VAL 306 309 309 VAL VAL A . n 
A 1 307 ARG 307 310 310 ARG ARG A . n 
A 1 308 SER 308 311 311 SER SER A . n 
A 1 309 ALA 309 312 312 ALA ALA A . n 
A 1 310 LYS 310 313 313 LYS LYS A . n 
A 1 311 LEU 311 314 314 LEU LEU A . n 
A 1 312 ARG 312 315 315 ARG ARG A . n 
A 1 313 MET 313 316 316 MET MET A . n 
A 1 314 VAL 314 317 317 VAL VAL A . n 
A 1 315 THR 315 318 318 THR THR A . n 
A 1 316 GLY 316 319 319 GLY GLY A . n 
A 1 317 LEU 317 320 320 LEU LEU A . n 
A 1 318 ARG 318 321 321 ARG ARG A . n 
A 1 319 ASN 319 322 322 ASN ASN A . n 
A 1 320 ILE 320 323 323 ILE ILE A . n 
A 1 321 PRO 321 324 324 PRO PRO A . n 
A 1 322 SER 322 325 325 SER SER A . n 
A 1 323 ILE 323 326 ?   ?   ?   A . n 
A 1 324 GLN 324 327 ?   ?   ?   A . n 
A 1 325 SER 325 328 ?   ?   ?   A . n 
A 1 326 ARG 326 329 ?   ?   ?   A . n 
B 2 1   GLY 1   1   1   GLY GLY B . n 
B 2 2   LEU 2   2   2   LEU LEU B . n 
B 2 3   PHE 3   3   3   PHE PHE B . n 
B 2 4   GLY 4   4   4   GLY GLY B . n 
B 2 5   ALA 5   5   5   ALA ALA B . n 
B 2 6   ILE 6   6   6   ILE ILE B . n 
B 2 7   ALA 7   7   7   ALA ALA B . n 
B 2 8   GLY 8   8   8   GLY GLY B . n 
B 2 9   PHE 9   9   9   PHE PHE B . n 
B 2 10  ILE 10  10  10  ILE ILE B . n 
B 2 11  GLU 11  11  11  GLU GLU B . n 
B 2 12  GLY 12  12  12  GLY GLY B . n 
B 2 13  GLY 13  13  13  GLY GLY B . n 
B 2 14  TRP 14  14  14  TRP TRP B . n 
B 2 15  THR 15  15  15  THR THR B . n 
B 2 16  GLY 16  16  16  GLY GLY B . n 
B 2 17  MET 17  17  17  MET MET B . n 
B 2 18  VAL 18  18  18  VAL VAL B . n 
B 2 19  ASP 19  19  19  ASP ASP B . n 
B 2 20  GLY 20  20  20  GLY GLY B . n 
B 2 21  TRP 21  21  21  TRP TRP B . n 
B 2 22  TYR 22  22  22  TYR TYR B . n 
B 2 23  GLY 23  23  23  GLY GLY B . n 
B 2 24  TYR 24  24  24  TYR TYR B . n 
B 2 25  HIS 25  25  25  HIS HIS B . n 
B 2 26  HIS 26  26  26  HIS HIS B . n 
B 2 27  GLN 27  27  27  GLN GLN B . n 
B 2 28  ASN 28  28  28  ASN ASN B . n 
B 2 29  GLU 29  29  29  GLU GLU B . n 
B 2 30  GLN 30  30  30  GLN GLN B . n 
B 2 31  GLY 31  31  31  GLY GLY B . n 
B 2 32  SER 32  32  32  SER SER B . n 
B 2 33  GLY 33  33  33  GLY GLY B . n 
B 2 34  TYR 34  34  34  TYR TYR B . n 
B 2 35  ALA 35  35  35  ALA ALA B . n 
B 2 36  ALA 36  36  36  ALA ALA B . n 
B 2 37  ASP 37  37  37  ASP ASP B . n 
B 2 38  GLN 38  38  38  GLN GLN B . n 
B 2 39  LYS 39  39  39  LYS LYS B . n 
B 2 40  SER 40  40  40  SER SER B . n 
B 2 41  THR 41  41  41  THR THR B . n 
B 2 42  GLN 42  42  42  GLN GLN B . n 
B 2 43  ASN 43  43  43  ASN ASN B . n 
B 2 44  ALA 44  44  44  ALA ALA B . n 
B 2 45  ILE 45  45  45  ILE ILE B . n 
B 2 46  ASN 46  46  46  ASN ASN B . n 
B 2 47  GLY 47  47  47  GLY GLY B . n 
B 2 48  ILE 48  48  48  ILE ILE B . n 
B 2 49  THR 49  49  49  THR THR B . n 
B 2 50  ASN 50  50  50  ASN ASN B . n 
B 2 51  LYS 51  51  51  LYS LYS B . n 
B 2 52  VAL 52  52  52  VAL VAL B . n 
B 2 53  ASN 53  53  53  ASN ASN B . n 
B 2 54  SER 54  54  54  SER SER B . n 
B 2 55  VAL 55  55  55  VAL VAL B . n 
B 2 56  ILE 56  56  56  ILE ILE B . n 
B 2 57  GLU 57  57  57  GLU GLU B . n 
B 2 58  LYS 58  58  58  LYS LYS B . n 
B 2 59  MET 59  59  59  MET MET B . n 
B 2 60  ASN 60  60  60  ASN ASN B . n 
B 2 61  THR 61  61  61  THR THR B . n 
B 2 62  GLN 62  62  62  GLN GLN B . n 
B 2 63  PHE 63  63  63  PHE PHE B . n 
B 2 64  THR 64  64  64  THR THR B . n 
B 2 65  ALA 65  65  65  ALA ALA B . n 
B 2 66  VAL 66  66  66  VAL VAL B . n 
B 2 67  GLY 67  67  67  GLY GLY B . n 
B 2 68  LYS 68  68  68  LYS LYS B . n 
B 2 69  GLU 69  69  69  GLU GLU B . n 
B 2 70  PHE 70  70  70  PHE PHE B . n 
B 2 71  ASN 71  71  71  ASN ASN B . n 
B 2 72  LYS 72  72  72  LYS LYS B . n 
B 2 73  LEU 73  73  73  LEU LEU B . n 
B 2 74  GLU 74  74  74  GLU GLU B . n 
B 2 75  ARG 75  75  75  ARG ARG B . n 
B 2 76  ARG 76  76  76  ARG ARG B . n 
B 2 77  MET 77  77  77  MET MET B . n 
B 2 78  GLU 78  78  78  GLU GLU B . n 
B 2 79  ASN 79  79  79  ASN ASN B . n 
B 2 80  LEU 80  80  80  LEU LEU B . n 
B 2 81  ASN 81  81  81  ASN ASN B . n 
B 2 82  LYS 82  82  82  LYS LYS B . n 
B 2 83  LYS 83  83  83  LYS LYS B . n 
B 2 84  VAL 84  84  84  VAL VAL B . n 
B 2 85  ASP 85  85  85  ASP ASP B . n 
B 2 86  ASP 86  86  86  ASP ASP B . n 
B 2 87  GLY 87  87  87  GLY GLY B . n 
B 2 88  PHE 88  88  88  PHE PHE B . n 
B 2 89  ILE 89  89  89  ILE ILE B . n 
B 2 90  ASP 90  90  90  ASP ASP B . n 
B 2 91  ILE 91  91  91  ILE ILE B . n 
B 2 92  TRP 92  92  92  TRP TRP B . n 
B 2 93  THR 93  93  93  THR THR B . n 
B 2 94  TYR 94  94  94  TYR TYR B . n 
B 2 95  ASN 95  95  95  ASN ASN B . n 
B 2 96  ALA 96  96  96  ALA ALA B . n 
B 2 97  GLU 97  97  97  GLU GLU B . n 
B 2 98  LEU 98  98  98  LEU LEU B . n 
B 2 99  LEU 99  99  99  LEU LEU B . n 
B 2 100 VAL 100 100 100 VAL VAL B . n 
B 2 101 LEU 101 101 101 LEU LEU B . n 
B 2 102 LEU 102 102 102 LEU LEU B . n 
B 2 103 GLU 103 103 103 GLU GLU B . n 
B 2 104 ASN 104 104 104 ASN ASN B . n 
B 2 105 GLU 105 105 105 GLU GLU B . n 
B 2 106 ARG 106 106 106 ARG ARG B . n 
B 2 107 THR 107 107 107 THR THR B . n 
B 2 108 LEU 108 108 108 LEU LEU B . n 
B 2 109 ASP 109 109 109 ASP ASP B . n 
B 2 110 PHE 110 110 110 PHE PHE B . n 
B 2 111 HIS 111 111 111 HIS HIS B . n 
B 2 112 ASP 112 112 112 ASP ASP B . n 
B 2 113 SER 113 113 113 SER SER B . n 
B 2 114 ASN 114 114 114 ASN ASN B . n 
B 2 115 VAL 115 115 115 VAL VAL B . n 
B 2 116 LYS 116 116 116 LYS LYS B . n 
B 2 117 ASN 117 117 117 ASN ASN B . n 
B 2 118 LEU 118 118 118 LEU LEU B . n 
B 2 119 TYR 119 119 119 TYR TYR B . n 
B 2 120 GLU 120 120 120 GLU GLU B . n 
B 2 121 LYS 121 121 121 LYS LYS B . n 
B 2 122 VAL 122 122 122 VAL VAL B . n 
B 2 123 LYS 123 123 123 LYS LYS B . n 
B 2 124 SER 124 124 124 SER SER B . n 
B 2 125 GLN 125 125 125 GLN GLN B . n 
B 2 126 LEU 126 126 126 LEU LEU B . n 
B 2 127 LYS 127 127 127 LYS LYS B . n 
B 2 128 ASN 128 128 128 ASN ASN B . n 
B 2 129 ASN 129 129 129 ASN ASN B . n 
B 2 130 ALA 130 130 130 ALA ALA B . n 
B 2 131 LYS 131 131 131 LYS LYS B . n 
B 2 132 GLU 132 132 132 GLU GLU B . n 
B 2 133 ILE 133 133 133 ILE ILE B . n 
B 2 134 GLY 134 134 134 GLY GLY B . n 
B 2 135 ASN 135 135 135 ASN ASN B . n 
B 2 136 GLY 136 136 136 GLY GLY B . n 
B 2 137 CYS 137 137 137 CYS CYS B . n 
B 2 138 PHE 138 138 138 PHE PHE B . n 
B 2 139 GLU 139 139 139 GLU GLU B . n 
B 2 140 PHE 140 140 140 PHE PHE B . n 
B 2 141 TYR 141 141 141 TYR TYR B . n 
B 2 142 HIS 142 142 142 HIS HIS B . n 
B 2 143 LYS 143 143 143 LYS LYS B . n 
B 2 144 CYS 144 144 144 CYS CYS B . n 
B 2 145 ASN 145 145 145 ASN ASN B . n 
B 2 146 ASP 146 146 146 ASP ASP B . n 
B 2 147 GLU 147 147 147 GLU GLU B . n 
B 2 148 CYS 148 148 148 CYS CYS B . n 
B 2 149 MET 149 149 149 MET MET B . n 
B 2 150 GLU 150 150 150 GLU GLU B . n 
B 2 151 SER 151 151 151 SER SER B . n 
B 2 152 VAL 152 152 152 VAL VAL B . n 
B 2 153 LYS 153 153 153 LYS LYS B . n 
B 2 154 ASN 154 154 154 ASN ASN B . n 
B 2 155 GLY 155 155 155 GLY GLY B . n 
B 2 156 THR 156 156 156 THR THR B . n 
B 2 157 TYR 157 157 157 TYR TYR B . n 
B 2 158 ASP 158 158 158 ASP ASP B . n 
B 2 159 TYR 159 159 159 TYR TYR B . n 
B 2 160 PRO 160 160 160 PRO PRO B . n 
B 2 161 LYS 161 161 161 LYS LYS B . n 
B 2 162 TYR 162 162 162 TYR TYR B . n 
B 2 163 SER 163 163 163 SER SER B . n 
B 2 164 GLU 164 164 164 GLU GLU B . n 
B 2 165 GLU 165 165 165 GLU GLU B . n 
B 2 166 SER 166 166 166 SER SER B . n 
B 2 167 LYS 167 167 167 LYS LYS B . n 
B 2 168 LEU 168 168 168 LEU LEU B . n 
B 2 169 ASN 169 169 169 ASN ASN B . n 
B 2 170 ARG 170 170 170 ARG ARG B . n 
B 2 171 GLU 171 171 171 GLU GLU B . n 
B 2 172 LYS 172 172 ?   ?   ?   B . n 
B 2 173 ILE 173 173 ?   ?   ?   B . n 
B 2 174 ASP 174 174 ?   ?   ?   B . 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 
C 3 NAG 1 C NAG 1 D NAG 2  n 
C 3 NAG 2 C NAG 2 D NAG 3  n 
C 3 BMA 3 C BMA 3 D BMA 4  n 
C 3 MAN 4 C MAN 4 D MAN 5  n 
D 4 NAG 1 D NAG 1 D NAG 6  n 
D 4 NAG 2 D NAG 2 D NAG 7  n 
D 4 BMA 3 D BMA 3 D BMA 8  n 
E 5 NAG 1 E NAG 1 D NAG 9  n 
E 5 NAG 2 E NAG 2 D NAG 10 n 
F 5 NAG 1 F NAG 1 D NAG 11 n 
F 5 NAG 2 F NAG 2 D NAG 12 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 
G 6 NAG 1  412 13 NAG NAG A . 
H 7 EZ7 1  201 1  EZ7 PDB B . 
I 8 HOH 1  501 46 HOH HOH A . 
I 8 HOH 2  502 18 HOH HOH A . 
I 8 HOH 3  503 38 HOH HOH A . 
I 8 HOH 4  504 49 HOH HOH A . 
I 8 HOH 5  505 35 HOH HOH A . 
I 8 HOH 6  506 47 HOH HOH A . 
I 8 HOH 7  507 10 HOH HOH A . 
I 8 HOH 8  508 20 HOH HOH A . 
I 8 HOH 9  509 22 HOH HOH A . 
I 8 HOH 10 510 16 HOH HOH A . 
I 8 HOH 11 511 13 HOH HOH A . 
I 8 HOH 12 512 7  HOH HOH A . 
I 8 HOH 13 513 30 HOH HOH A . 
I 8 HOH 14 514 21 HOH HOH A . 
I 8 HOH 15 515 9  HOH HOH A . 
I 8 HOH 16 516 52 HOH HOH A . 
I 8 HOH 17 517 24 HOH HOH A . 
I 8 HOH 18 518 6  HOH HOH A . 
I 8 HOH 19 519 28 HOH HOH A . 
I 8 HOH 20 520 50 HOH HOH A . 
I 8 HOH 21 521 26 HOH HOH A . 
I 8 HOH 22 522 45 HOH HOH A . 
I 8 HOH 23 523 17 HOH HOH A . 
I 8 HOH 24 524 32 HOH HOH A . 
I 8 HOH 25 525 27 HOH HOH A . 
I 8 HOH 26 526 29 HOH HOH A . 
I 8 HOH 27 527 37 HOH HOH A . 
I 8 HOH 28 528 23 HOH HOH A . 
J 8 HOH 1  301 48 HOH HOH B . 
J 8 HOH 2  302 8  HOH HOH B . 
J 8 HOH 3  303 42 HOH HOH B . 
J 8 HOH 4  304 11 HOH HOH B . 
J 8 HOH 5  305 3  HOH HOH B . 
J 8 HOH 6  306 12 HOH HOH B . 
J 8 HOH 7  307 44 HOH HOH B . 
J 8 HOH 8  308 19 HOH HOH B . 
J 8 HOH 9  309 15 HOH HOH B . 
J 8 HOH 10 310 51 HOH HOH B . 
J 8 HOH 11 311 34 HOH HOH B . 
J 8 HOH 12 312 31 HOH HOH B . 
J 8 HOH 13 313 33 HOH HOH B . 
J 8 HOH 14 314 1  HOH HOH B . 
J 8 HOH 15 315 2  HOH HOH B . 
J 8 HOH 16 316 39 HOH HOH B . 
J 8 HOH 17 317 14 HOH HOH B . 
J 8 HOH 18 318 5  HOH HOH B . 
J 8 HOH 19 319 43 HOH HOH B . 
J 8 HOH 20 320 41 HOH HOH B . 
J 8 HOH 21 321 40 HOH HOH B . 
J 8 HOH 22 322 4  HOH HOH B . 
J 8 HOH 23 323 25 HOH HOH B . 
J 8 HOH 24 324 36 HOH HOH B . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? 1.10_2155 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .         2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .         3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER   ? ? ? .         4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     6CF7 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     161.445 
_cell.length_a_esd                 ? 
_cell.length_b                     161.445 
_cell.length_b_esd                 ? 
_cell.length_c                     161.445 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        24 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
# 
_symmetry.entry_id                         6CF7 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                213 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 41 3 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   6CF7 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                      ? 
_exptl_crystal.density_diffrn              ? 
_exptl_crystal.density_Matthews            3.11 
_exptl_crystal.density_method              ? 
_exptl_crystal.density_percent_sol         60.45 
_exptl_crystal.description                 ? 
_exptl_crystal.F_000                       ? 
_exptl_crystal.id                          1 
_exptl_crystal.preparation                 ? 
_exptl_crystal.size_max                    ? 
_exptl_crystal.size_mid                    ? 
_exptl_crystal.size_min                    ? 
_exptl_crystal.size_rad                    ? 
_exptl_crystal.colour_lustre               ? 
_exptl_crystal.colour_modifier             ? 
_exptl_crystal.colour_primary              ? 
_exptl_crystal.density_meas                ? 
_exptl_crystal.density_meas_esd            ? 
_exptl_crystal.density_meas_gt             ? 
_exptl_crystal.density_meas_lt             ? 
_exptl_crystal.density_meas_temp           ? 
_exptl_crystal.density_meas_temp_esd       ? 
_exptl_crystal.density_meas_temp_gt        ? 
_exptl_crystal.density_meas_temp_lt        ? 
_exptl_crystal.pdbx_crystal_image_url      ? 
_exptl_crystal.pdbx_crystal_image_format   ? 
_exptl_crystal.pdbx_mosaicity              ? 
_exptl_crystal.pdbx_mosaicity_esd          ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp            293.15 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.2M disodium hydrogen phosphate, 20% w/v PEG3350' 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.ambient_environment    ? 
_diffrn.ambient_temp           80 
_diffrn.ambient_temp_details   ? 
_diffrn.ambient_temp_esd       ? 
_diffrn.crystal_id             1 
_diffrn.crystal_support        ? 
_diffrn.crystal_treatment      ? 
_diffrn.details                ? 
_diffrn.id                     1 
_diffrn.ambient_pressure       ? 
_diffrn.ambient_pressure_esd   ? 
_diffrn.ambient_pressure_gt    ? 
_diffrn.ambient_pressure_lt    ? 
_diffrn.ambient_temp_gt        ? 
_diffrn.ambient_temp_lt        ? 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS3 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2016-04-18 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97946 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SSRL BEAMLINE BL12-2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97946 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL12-2 
_diffrn_source.pdbx_synchrotron_site       SSRL 
# 
_reflns.B_iso_Wilson_estimate            59 
_reflns.entry_id                         6CF7 
_reflns.data_reduction_details           ? 
_reflns.data_reduction_method            ? 
_reflns.d_resolution_high                2.719 
_reflns.d_resolution_low                 50 
_reflns.details                          ? 
_reflns.limit_h_max                      ? 
_reflns.limit_h_min                      ? 
_reflns.limit_k_max                      ? 
_reflns.limit_k_min                      ? 
_reflns.limit_l_max                      ? 
_reflns.limit_l_min                      ? 
_reflns.number_all                       ? 
_reflns.number_obs                       19893 
_reflns.observed_criterion               ? 
_reflns.observed_criterion_F_max         ? 
_reflns.observed_criterion_F_min         ? 
_reflns.observed_criterion_I_max         ? 
_reflns.observed_criterion_I_min         ? 
_reflns.observed_criterion_sigma_F       ? 
_reflns.observed_criterion_sigma_I       ? 
_reflns.percent_possible_obs             99.6 
_reflns.R_free_details                   ? 
_reflns.Rmerge_F_all                     ? 
_reflns.Rmerge_F_obs                     ? 
_reflns.Friedel_coverage                 ? 
_reflns.number_gt                        ? 
_reflns.threshold_expression             ? 
_reflns.pdbx_redundancy                  12.4 
_reflns.pdbx_Rmerge_I_obs                ? 
_reflns.pdbx_Rmerge_I_all                ? 
_reflns.pdbx_Rsym_value                  0.10 
_reflns.pdbx_netI_over_av_sigmaI         ? 
_reflns.pdbx_netI_over_sigmaI            22.4 
_reflns.pdbx_res_netI_over_av_sigmaI_2   ? 
_reflns.pdbx_res_netI_over_sigmaI_2      ? 
_reflns.pdbx_chi_squared                 ? 
_reflns.pdbx_scaling_rejects             ? 
_reflns.pdbx_d_res_high_opt              ? 
_reflns.pdbx_d_res_low_opt               ? 
_reflns.pdbx_d_res_opt_method            ? 
_reflns.phase_calculation_details        ? 
_reflns.pdbx_Rrim_I_all                  ? 
_reflns.pdbx_Rpim_I_all                  0.03 
_reflns.pdbx_d_opt                       ? 
_reflns.pdbx_number_measured_all         ? 
_reflns.pdbx_diffrn_id                   1 
_reflns.pdbx_ordinal                     1 
_reflns.pdbx_CC_half                     0.97 
_reflns.pdbx_R_split                     ? 
# 
_reflns_shell.d_res_high                  2.72 
_reflns_shell.d_res_low                   2.77 
_reflns_shell.meanI_over_sigI_all         ? 
_reflns_shell.meanI_over_sigI_obs         2.1 
_reflns_shell.number_measured_all         ? 
_reflns_shell.number_measured_obs         ? 
_reflns_shell.number_possible             ? 
_reflns_shell.number_unique_all           ? 
_reflns_shell.number_unique_obs           967 
_reflns_shell.percent_possible_all        100 
_reflns_shell.percent_possible_obs        ? 
_reflns_shell.Rmerge_F_all                ? 
_reflns_shell.Rmerge_F_obs                ? 
_reflns_shell.Rmerge_I_all                ? 
_reflns_shell.Rmerge_I_obs                ? 
_reflns_shell.meanI_over_sigI_gt          ? 
_reflns_shell.meanI_over_uI_all           ? 
_reflns_shell.meanI_over_uI_gt            ? 
_reflns_shell.number_measured_gt          ? 
_reflns_shell.number_unique_gt            ? 
_reflns_shell.percent_possible_gt         ? 
_reflns_shell.Rmerge_F_gt                 ? 
_reflns_shell.Rmerge_I_gt                 ? 
_reflns_shell.pdbx_redundancy             ? 
_reflns_shell.pdbx_Rsym_value             0.89 
_reflns_shell.pdbx_chi_squared            ? 
_reflns_shell.pdbx_netI_over_sigmaI_all   ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs   ? 
_reflns_shell.pdbx_Rrim_I_all             ? 
_reflns_shell.pdbx_Rpim_I_all             0.24 
_reflns_shell.pdbx_rejects                ? 
_reflns_shell.pdbx_ordinal                1 
_reflns_shell.pdbx_diffrn_id              1 
_reflns_shell.pdbx_CC_half                0.84 
_reflns_shell.pdbx_R_split                ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 6CF7 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.719 
_refine.ls_d_res_low                             44.777 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     19834 
_refine.ls_number_reflns_R_free                  996 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.56 
_refine.ls_percent_reflns_R_free                 5.02 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2273 
_refine.ls_R_factor_R_free                       0.2493 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2261 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.36 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      5W5S 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 25.90 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.39 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        3906 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         199 
_refine_hist.number_atoms_solvent             52 
_refine_hist.number_atoms_total               4157 
_refine_hist.d_res_high                       2.719 
_refine_hist.d_res_low                        44.777 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.004  ? 4220 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.565  ? 5745 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 11.939 ? 2513 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.041  ? 633  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.004  ? 733  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
'X-RAY DIFFRACTION' 2.7192 2.8626  . . 141 2631 100.00 . . . 0.3279 . 0.2807 . . . . . . . . . . 
'X-RAY DIFFRACTION' 2.8626 3.0419  . . 140 2653 100.00 . . . 0.2870 . 0.2674 . . . . . . . . . . 
'X-RAY DIFFRACTION' 3.0419 3.2767  . . 135 2632 100.00 . . . 0.2993 . 0.2742 . . . . . . . . . . 
'X-RAY DIFFRACTION' 3.2767 3.6063  . . 121 2690 100.00 . . . 0.2475 . 0.2414 . . . . . . . . . . 
'X-RAY DIFFRACTION' 3.6063 4.1278  . . 137 2693 100.00 . . . 0.2514 . 0.2184 . . . . . . . . . . 
'X-RAY DIFFRACTION' 4.1278 5.1994  . . 158 2710 99.00  . . . 0.2146 . 0.1925 . . . . . . . . . . 
'X-RAY DIFFRACTION' 5.1994 44.7828 . . 164 2829 98.00  . . . 0.2396 . 0.2164 . . . . . . . . . . 
# 
_struct.entry_id                     6CF7 
_struct.title                        
'Crystal structure of the A/Solomon Islands/3/2006(H1N1) influenza virus hemagglutinin in complex with small molecule JNJ4796' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        6CF7 
_struct_keywords.text            'Glycoprotein, Ectodomain, N-glycosylation, VIRAL PROTEIN' 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN' 
# 
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 5 ? 
G N N 6 ? 
H N N 7 ? 
I N N 8 ? 
J N N 8 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP A7Y8I1_9INFA A7Y8I1 ? 1 
;DTICIGYHANNSTDTVDTVLEKNVTVTHSVNLLEDSHNGKLCLLKGIAPLQLGNCSVAGWILGNPECELLISRESWSYIV
EKPNPENGTCYPGHFADYEELREQLSSVSSFERFEIFPKESSWPNHTTTGVSASCSHNGESSFYKNLLWLTGKNGLYPNL
SKSYANNKEKEVLVLWGVHHPPNIGDQRALYHKENAYVSVVSSHYSRKFTPEIAKRPKVRDQEGRINYYWTLLEPGDTII
FEANGNLIAPRYAFALSRGFGSGIINSNAPMDECDAKCQTPQGAINSSLPFQNVHPVTIGECPKYVRSAKLRMVTGLRNI
PSIQSR
;
18  
2 UNP F2NZB4_9INFA F2NZB4 ? 2 
;GLFGAIAGFIEGGWTGMVDGWYGYHHQNEQGSGYAADQKSTQNAINGITNKVNSVIEKMNTQFTAVGKEFNKLERRMENL
NKKVDDGFIDIWTYNAELLVLLENERTLDFHDSNVKNLYEKVKSQLKNNAKEIGNGCFEFYHKCNDECMESVKNGTYDYP
KYSEESKLNREKID
;
344 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 6CF7 A 1 ? 326 ? A7Y8I1 18  ? 343 ? 11 329 
2 2 6CF7 B 1 ? 174 ? F2NZB4 344 ? 517 ? 1  174 
# 
_struct_ref_seq_dif.align_id                     1 
_struct_ref_seq_dif.pdbx_pdb_id_code             6CF7 
_struct_ref_seq_dif.mon_id                       ARG 
_struct_ref_seq_dif.pdbx_pdb_strand_id           A 
_struct_ref_seq_dif.seq_num                      43 
_struct_ref_seq_dif.pdbx_pdb_ins_code            ? 
_struct_ref_seq_dif.pdbx_seq_db_name             UNP 
_struct_ref_seq_dif.pdbx_seq_db_accession_code   A7Y8I1 
_struct_ref_seq_dif.db_mon_id                    LEU 
_struct_ref_seq_dif.pdbx_seq_db_seq_num          60 
_struct_ref_seq_dif.details                      'engineered mutation' 
_struct_ref_seq_dif.pdbx_auth_seq_num            53 
_struct_ref_seq_dif.pdbx_ordinal                 1 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   hexameric 
_pdbx_struct_assembly.oligomeric_count     6 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 34830 ? 
1 MORE         -78   ? 
1 'SSA (A^2)'  67580 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2,3 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z 1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 
2 'crystal symmetry operation' 5_555 z,x,y 0.0000000000 0.0000000000 1.0000000000 0.0000000000 1.0000000000 0.0000000000 
0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 0.0000000000 
3 'crystal symmetry operation' 9_555 y,z,x 0.0000000000 1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 
1.0000000000 0.0000000000 1.0000000000 0.0000000000 0.0000000000 0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 SER A 56  ? GLY A 63  ? SER A 65  GLY A 72  1 ? 8  
HELX_P HELX_P2 AA2 ASN A 64  ? ILE A 71  ? ASN A 73  ILE A 80  5 ? 8  
HELX_P HELX_P3 AA3 ASP A 97  ? SER A 106 ? ASP A 104 SER A 113 1 ? 10 
HELX_P HELX_P4 AA4 ASN A 183 ? HIS A 192 ? ASN A 187 HIS A 196 1 ? 10 
HELX_P HELX_P5 AA5 ASP B 37  ? LYS B 58  ? ASP B 37  LYS B 58  1 ? 22 
HELX_P HELX_P6 AA6 GLU B 74  ? LYS B 127 ? GLU B 74  LYS B 127 1 ? 54 
HELX_P HELX_P7 AA7 ASN B 145 ? ASN B 154 ? ASN B 145 ASN B 154 1 ? 10 
HELX_P HELX_P8 AA8 TYR B 159 ? LYS B 161 ? TYR B 159 LYS B 161 5 ? 3  
HELX_P HELX_P9 AA9 TYR B 162 ? ARG B 170 ? TYR B 162 ARG B 170 1 ? 9  
# 
_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 4   SG  ? ? ? 1_555 B CYS 137 SG ? ? A CYS 14  B CYS 137 1_555 ? ? ? ? ? ? ? 2.029 ? ?               
disulf2  disulf ?    ? A CYS 42  SG  ? ? ? 1_555 A CYS 274 SG ? ? A CYS 52  A CYS 277 1_555 ? ? ? ? ? ? ? 2.031 ? ?               
disulf3  disulf ?    ? A CYS 55  SG  ? ? ? 1_555 A CYS 67  SG ? ? A CYS 64  A CYS 76  1_555 ? ? ? ? ? ? ? 2.027 ? ?               
disulf4  disulf ?    ? A CYS 90  SG  ? ? ? 1_555 A CYS 135 SG ? ? A CYS 97  A CYS 139 1_555 ? ? ? ? ? ? ? 2.028 ? ?               
disulf5  disulf ?    ? A CYS 278 SG  ? ? ? 1_555 A CYS 302 SG ? ? A CYS 281 A CYS 305 1_555 ? ? ? ? ? ? ? 2.025 ? ?               
disulf6  disulf ?    ? B CYS 144 SG  ? ? ? 1_555 B CYS 148 SG ? ? B CYS 144 B CYS 148 1_555 ? ? ? ? ? ? ? 2.028 ? ?               
covale1  covale one  ? A ASN 11  ND2 ? ? ? 1_555 D NAG .   C1 ? ? A ASN 21  D NAG 1   1_555 ? ? ? ? ? ? ? 1.439 ? N-Glycosylation 
covale2  covale one  ? A ASN 23  ND2 ? ? ? 1_555 F NAG .   C1 ? ? A ASN 33  F NAG 1   1_555 ? ? ? ? ? ? ? 1.438 ? N-Glycosylation 
covale3  covale one  ? A ASN 54  ND2 ? ? ? 1_555 G NAG .   C1 ? ? A ASN 63  A NAG 412 1_555 ? ? ? ? ? ? ? 1.437 ? N-Glycosylation 
covale4  covale one  ? A ASN 87  ND2 ? ? ? 1_555 E NAG .   C1 ? ? A ASN 95  E NAG 1   1_555 ? ? ? ? ? ? ? 1.437 ? N-Glycosylation 
covale5  covale one  ? A ASN 286 ND2 ? ? ? 1_555 C NAG .   C1 ? ? A ASN 289 C NAG 1   1_555 ? ? ? ? ? ? ? 1.436 ? N-Glycosylation 
covale6  covale both ? C NAG .   O4  ? ? ? 1_555 C NAG .   C1 ? ? C NAG 1   C NAG 2   1_555 ? ? ? ? ? ? ? 1.439 ? ?               
covale7  covale both ? C NAG .   O4  ? ? ? 1_555 C BMA .   C1 ? ? C NAG 2   C BMA 3   1_555 ? ? ? ? ? ? ? 1.444 ? ?               
covale8  covale both ? C BMA .   O3  ? ? ? 1_555 C MAN .   C1 ? ? C BMA 3   C MAN 4   1_555 ? ? ? ? ? ? ? 1.453 ? ?               
covale9  covale both ? D NAG .   O4  ? ? ? 1_555 D NAG .   C1 ? ? D NAG 1   D NAG 2   1_555 ? ? ? ? ? ? ? 1.440 ? ?               
covale10 covale both ? D NAG .   O4  ? ? ? 1_555 D BMA .   C1 ? ? D NAG 2   D BMA 3   1_555 ? ? ? ? ? ? ? 1.439 ? ?               
covale11 covale both ? E NAG .   O4  ? ? ? 1_555 E NAG .   C1 ? ? E NAG 1   E NAG 2   1_555 ? ? ? ? ? ? ? 1.441 ? ?               
covale12 covale both ? F NAG .   O4  ? ? ? 1_555 F NAG .   C1 ? ? F NAG 1   F NAG 2   1_555 ? ? ? ? ? ? ? 1.440 ? ?               
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
# 
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  NAG C .   ? ASN A 286 ? NAG C 1   ? 1_555 ASN A 289 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
2  NAG D .   ? ASN A 11  ? NAG D 1   ? 1_555 ASN A 21  ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
3  NAG E .   ? ASN A 87  ? NAG E 1   ? 1_555 ASN A 95  ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
4  NAG F .   ? ASN A 23  ? NAG F 1   ? 1_555 ASN A 33  ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
5  NAG G .   ? ASN A 54  ? NAG A 412 ? 1_555 ASN A 63  ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
6  CYS A 4   ? CYS B 137 ? CYS A 14  ? 1_555 CYS B 137 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
7  CYS A 42  ? CYS A 274 ? CYS A 52  ? 1_555 CYS A 277 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
8  CYS A 55  ? CYS A 67  ? CYS A 64  ? 1_555 CYS A 76  ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
9  CYS A 90  ? CYS A 135 ? CYS A 97  ? 1_555 CYS A 139 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
10 CYS A 278 ? CYS A 302 ? CYS A 281 ? 1_555 CYS A 305 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
11 CYS B 144 ? CYS B 148 ? CYS B 144 ? 1_555 CYS B 148 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 2 ? 
AA3 ? 2 ? 
AA4 ? 3 ? 
AA5 ? 2 ? 
AA6 ? 3 ? 
AA7 ? 5 ? 
AA8 ? 4 ? 
AA9 ? 2 ? 
AB1 ? 4 ? 
AB2 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? parallel      
AA4 2 3 ? parallel      
AA5 1 2 ? parallel      
AA6 1 2 ? parallel      
AA6 2 3 ? parallel      
AA7 1 2 ? anti-parallel 
AA7 2 3 ? anti-parallel 
AA7 3 4 ? anti-parallel 
AA7 4 5 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA8 2 3 ? anti-parallel 
AA8 3 4 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AB1 1 2 ? anti-parallel 
AB1 2 3 ? anti-parallel 
AB1 3 4 ? anti-parallel 
AB2 1 2 ? anti-parallel 
AB2 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 GLY B 31  ? ALA B 36  ? GLY B 31  ALA B 36  
AA1 2 TYR B 22  ? ASN B 28  ? TYR B 22  ASN B 28  
AA1 3 THR A 2   ? TYR A 7   ? THR A 12  TYR A 17  
AA1 4 CYS B 137 ? PHE B 140 ? CYS B 137 PHE B 140 
AA1 5 ALA B 130 ? LYS B 131 ? ALA B 130 LYS B 131 
AA2 1 THR A 15  ? VAL A 16  ? THR A 25  VAL A 26  
AA2 2 VAL A 24  ? THR A 25  ? VAL A 34  THR A 35  
AA3 1 SER A 29  ? ASN A 31  ? SER A 39  ASN A 41  
AA3 2 ARG A 312 ? VAL A 314 ? ARG A 315 VAL A 317 
AA4 1 LEU A 33  ? GLU A 34  ? LEU A 43  GLU A 44  
AA4 2 PHE A 291 ? GLN A 292 ? PHE A 294 GLN A 295 
AA4 3 LYS A 304 ? TYR A 305 ? LYS A 307 TYR A 308 
AA5 1 LEU A 41  ? LEU A 44  ? LEU A 51  LEU A 54  
AA5 2 MET A 271 ? ALA A 276 ? MET A 274 ALA A 279 
AA6 1 LEU A 50  ? GLN A 51  ? LEU A 59  GLN A 60  
AA6 2 ILE A 79  ? GLU A 81  ? ILE A 87  GLU A 89  
AA6 3 ILE A 264 ? ASN A 266 ? ILE A 267 ASN A 269 
AA7 1 VAL A 108 ? GLU A 115 ? VAL A 115 GLU A 122 
AA7 2 TYR A 252 ? ARG A 258 ? TYR A 256 ARG A 262 
AA7 3 GLU A 171 ? HIS A 180 ? GLU A 175 HIS A 184 
AA7 4 LEU A 247 ? PRO A 250 ? LEU A 251 PRO A 254 
AA7 5 LEU A 147 ? TRP A 149 ? LEU A 151 TRP A 153 
AA8 1 VAL A 108 ? GLU A 115 ? VAL A 115 GLU A 122 
AA8 2 TYR A 252 ? ARG A 258 ? TYR A 256 ARG A 262 
AA8 3 GLU A 171 ? HIS A 180 ? GLU A 175 HIS A 184 
AA8 4 ARG A 225 ? LEU A 233 ? ARG A 229 LEU A 237 
AA9 1 SER A 132 ? HIS A 137 ? SER A 136 HIS A 141 
AA9 2 GLU A 140 ? SER A 142 ? GLU A 144 SER A 146 
AB1 1 LEU A 160 ? ALA A 165 ? LEU A 164 ALA A 169 
AB1 2 THR A 238 ? ALA A 243 ? THR A 242 ALA A 247 
AB1 3 VAL A 198 ? VAL A 201 ? VAL A 202 VAL A 205 
AB1 4 SER A 206 ? PHE A 209 ? SER A 210 PHE A 213 
AB2 1 GLY A 283 ? ILE A 285 ? GLY A 286 ILE A 288 
AB2 2 CYS A 278 ? THR A 280 ? CYS A 281 THR A 283 
AB2 3 ILE A 299 ? GLY A 300 ? ILE A 302 GLY A 303 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O GLY B 31  ? O GLY B 31  N ASN B 28  ? N ASN B 28  
AA1 2 3 O GLN B 27  ? O GLN B 27  N THR A 2   ? N THR A 12  
AA1 3 4 N ILE A 3   ? N ILE A 13  O PHE B 138 ? O PHE B 138 
AA1 4 5 O GLU B 139 ? O GLU B 139 N LYS B 131 ? N LYS B 131 
AA2 1 2 N VAL A 16  ? N VAL A 26  O VAL A 24  ? O VAL A 34  
AA3 1 2 N VAL A 30  ? N VAL A 40  O MET A 313 ? O MET A 316 
AA4 1 2 N GLU A 34  ? N GLU A 44  O PHE A 291 ? O PHE A 294 
AA4 2 3 N GLN A 292 ? N GLN A 295 O LYS A 304 ? O LYS A 307 
AA5 1 2 N ARG A 43  ? N ARG A 53  O CYS A 274 ? O CYS A 277 
AA6 1 2 N LEU A 50  ? N LEU A 59  O VAL A 80  ? O VAL A 88  
AA6 2 3 N GLU A 81  ? N GLU A 89  O ILE A 265 ? O ILE A 268 
AA7 1 2 N PHE A 114 ? N PHE A 121 O ALA A 253 ? O ALA A 257 
AA7 2 3 O LEU A 256 ? O LEU A 260 N GLU A 171 ? N GLU A 175 
AA7 3 4 N GLY A 177 ? N GLY A 181 O ILE A 248 ? O ILE A 252 
AA7 4 5 O ALA A 249 ? O ALA A 253 N LEU A 148 ? N LEU A 152 
AA8 1 2 N PHE A 114 ? N PHE A 121 O ALA A 253 ? O ALA A 257 
AA8 2 3 O LEU A 256 ? O LEU A 260 N GLU A 171 ? N GLU A 175 
AA8 3 4 N TRP A 176 ? N TRP A 180 O TYR A 229 ? O TYR A 233 
AA9 1 2 N HIS A 137 ? N HIS A 141 O GLU A 140 ? O GLU A 144 
AB1 1 2 N LEU A 160 ? N LEU A 164 O ALA A 243 ? O ALA A 247 
AB1 2 3 O ILE A 240 ? O ILE A 244 N VAL A 201 ? N VAL A 205 
AB1 3 4 N VAL A 200 ? N VAL A 204 O ARG A 207 ? O ARG A 211 
AB2 1 2 O ILE A 285 ? O ILE A 288 N CYS A 278 ? N CYS A 281 
AB2 2 3 N GLN A 279 ? N GLN A 282 O ILE A 299 ? O ILE A 302 
# 
_pdbx_entry_details.entry_id                   6CF7 
_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 
# 
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 SER A 125 C ? 175.69  -0.93   
2 1 CYS A 139 ? ? -111.17 56.25   
3 1 THR A 155 ? ? -120.42 -163.43 
4 1 ASN A 171 ? ? -101.11 53.80   
5 1 HIS A 196 ? ? 59.19   16.51   
6 1 SER A 206 ? ? -126.76 -161.63 
7 1 ALA B 5   ? ? -90.23  -71.70  
8 1 LYS B 127 ? ? 60.04   -135.69 
# 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         2.2751 
_pdbx_refine_tls.origin_y         27.7487 
_pdbx_refine_tls.origin_z         11.7739 
_pdbx_refine_tls.T[1][1]          0.3627 
_pdbx_refine_tls.T[2][2]          0.3355 
_pdbx_refine_tls.T[3][3]          0.4205 
_pdbx_refine_tls.T[1][2]          0.0322 
_pdbx_refine_tls.T[1][3]          -0.0057 
_pdbx_refine_tls.T[2][3]          0.0008 
_pdbx_refine_tls.L[1][1]          1.7774 
_pdbx_refine_tls.L[2][2]          1.9436 
_pdbx_refine_tls.L[3][3]          1.7766 
_pdbx_refine_tls.L[1][2]          0.3297 
_pdbx_refine_tls.L[1][3]          0.5369 
_pdbx_refine_tls.L[2][3]          0.6311 
_pdbx_refine_tls.S[1][1]          -0.0834 
_pdbx_refine_tls.S[1][2]          0.1028 
_pdbx_refine_tls.S[1][3]          0.3473 
_pdbx_refine_tls.S[2][1]          -0.1970 
_pdbx_refine_tls.S[2][2]          -0.0513 
_pdbx_refine_tls.S[2][3]          0.3527 
_pdbx_refine_tls.S[3][1]          -0.2802 
_pdbx_refine_tls.S[3][2]          -0.2357 
_pdbx_refine_tls.S[3][3]          0.0841 
# 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.refine_tls_id       1 
_pdbx_refine_tls_group.beg_auth_asym_id    ? 
_pdbx_refine_tls_group.beg_auth_seq_id     ? 
_pdbx_refine_tls_group.beg_label_asym_id   ? 
_pdbx_refine_tls_group.beg_label_seq_id    ? 
_pdbx_refine_tls_group.end_auth_asym_id    ? 
_pdbx_refine_tls_group.end_auth_seq_id     ? 
_pdbx_refine_tls_group.end_label_asym_id   ? 
_pdbx_refine_tls_group.end_label_seq_id    ? 
_pdbx_refine_tls_group.selection           ? 
_pdbx_refine_tls_group.selection_details   all 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A ILE 326 ? A ILE 323 
2 1 Y 1 A GLN 327 ? A GLN 324 
3 1 Y 1 A SER 328 ? A SER 325 
4 1 Y 1 A ARG 329 ? A ARG 326 
5 1 Y 1 B LYS 172 ? B LYS 172 
6 1 Y 1 B ILE 173 ? B ILE 173 
7 1 Y 1 B ASP 174 ? B ASP 174 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
BMA C1   C N R 74  
BMA C2   C N S 75  
BMA C3   C N S 76  
BMA C4   C N S 77  
BMA C5   C N R 78  
BMA C6   C N N 79  
BMA O1   O N N 80  
BMA O2   O N N 81  
BMA O3   O N N 82  
BMA O4   O N N 83  
BMA O5   O N N 84  
BMA O6   O N N 85  
BMA H1   H N N 86  
BMA H2   H N N 87  
BMA H3   H N N 88  
BMA H4   H N N 89  
BMA H5   H N N 90  
BMA H61  H N N 91  
BMA H62  H N N 92  
BMA HO1  H N N 93  
BMA HO2  H N N 94  
BMA HO3  H N N 95  
BMA HO4  H N N 96  
BMA HO6  H N N 97  
CYS N    N N N 98  
CYS CA   C N R 99  
CYS C    C N N 100 
CYS O    O N N 101 
CYS CB   C N N 102 
CYS SG   S N N 103 
CYS OXT  O N N 104 
CYS H    H N N 105 
CYS H2   H N N 106 
CYS HA   H N N 107 
CYS HB2  H N N 108 
CYS HB3  H N N 109 
CYS HG   H N N 110 
CYS HXT  H N N 111 
EZ7 C2   C Y N 112 
EZ7 C3   C Y N 113 
EZ7 C4   C Y N 114 
EZ7 C11  C Y N 115 
EZ7 C12  C Y N 116 
EZ7 C16  C Y N 117 
EZ7 C18  C Y N 118 
EZ7 C19  C Y N 119 
EZ7 C60  C N N 120 
EZ7 C58  C N N 121 
EZ7 O59  O N N 122 
EZ7 N7   N N N 123 
EZ7 C1   C Y N 124 
EZ7 O13  O Y N 125 
EZ7 N10  N Y N 126 
EZ7 C9   C Y N 127 
EZ7 C17  C Y N 128 
EZ7 C15  C Y N 129 
EZ7 N14  N Y N 130 
EZ7 C23  C N N 131 
EZ7 O24  O N N 132 
EZ7 N27  N N N 133 
EZ7 C28  C N N 134 
EZ7 C29  C N N 135 
EZ7 C26  C N N 136 
EZ7 C25  C N N 137 
EZ7 N30  N N N 138 
EZ7 C40  C N R 139 
EZ7 C52  C Y N 140 
EZ7 N56  N Y N 141 
EZ7 N53  N Y N 142 
EZ7 N54  N Y N 143 
EZ7 N55  N Y N 144 
EZ7 C57  C N N 145 
EZ7 C44  C Y N 146 
EZ7 C43  C Y N 147 
EZ7 C42  C Y N 148 
EZ7 C41  C Y N 149 
EZ7 C46  C Y N 150 
EZ7 C45  C Y N 151 
EZ7 H1   H N N 152 
EZ7 H2   H N N 153 
EZ7 H3   H N N 154 
EZ7 H4   H N N 155 
EZ7 H5   H N N 156 
EZ7 H6   H N N 157 
EZ7 H7   H N N 158 
EZ7 H8   H N N 159 
EZ7 H9   H N N 160 
EZ7 H10  H N N 161 
EZ7 H11  H N N 162 
EZ7 H12  H N N 163 
EZ7 H13  H N N 164 
EZ7 H14  H N N 165 
EZ7 H15  H N N 166 
EZ7 H16  H N N 167 
EZ7 H17  H N N 168 
EZ7 H18  H N N 169 
EZ7 H20  H N N 170 
EZ7 H21  H N N 171 
EZ7 H22  H N N 172 
EZ7 H23  H N N 173 
EZ7 H24  H N N 174 
EZ7 H25  H N N 175 
EZ7 H26  H N N 176 
EZ7 H27  H N N 177 
EZ7 H28  H N N 178 
GLN N    N N N 179 
GLN CA   C N S 180 
GLN C    C N N 181 
GLN O    O N N 182 
GLN CB   C N N 183 
GLN CG   C N N 184 
GLN CD   C N N 185 
GLN OE1  O N N 186 
GLN NE2  N N N 187 
GLN OXT  O N N 188 
GLN H    H N N 189 
GLN H2   H N N 190 
GLN HA   H N N 191 
GLN HB2  H N N 192 
GLN HB3  H N N 193 
GLN HG2  H N N 194 
GLN HG3  H N N 195 
GLN HE21 H N N 196 
GLN HE22 H N N 197 
GLN HXT  H N N 198 
GLU N    N N N 199 
GLU CA   C N S 200 
GLU C    C N N 201 
GLU O    O N N 202 
GLU CB   C N N 203 
GLU CG   C N N 204 
GLU CD   C N N 205 
GLU OE1  O N N 206 
GLU OE2  O N N 207 
GLU OXT  O N N 208 
GLU H    H N N 209 
GLU H2   H N N 210 
GLU HA   H N N 211 
GLU HB2  H N N 212 
GLU HB3  H N N 213 
GLU HG2  H N N 214 
GLU HG3  H N N 215 
GLU HE2  H N N 216 
GLU HXT  H N N 217 
GLY N    N N N 218 
GLY CA   C N N 219 
GLY C    C N N 220 
GLY O    O N N 221 
GLY OXT  O N N 222 
GLY H    H N N 223 
GLY H2   H N N 224 
GLY HA2  H N N 225 
GLY HA3  H N N 226 
GLY HXT  H N N 227 
HIS N    N N N 228 
HIS CA   C N S 229 
HIS C    C N N 230 
HIS O    O N N 231 
HIS CB   C N N 232 
HIS CG   C Y N 233 
HIS ND1  N Y N 234 
HIS CD2  C Y N 235 
HIS CE1  C Y N 236 
HIS NE2  N Y N 237 
HIS OXT  O N N 238 
HIS H    H N N 239 
HIS H2   H N N 240 
HIS HA   H N N 241 
HIS HB2  H N N 242 
HIS HB3  H N N 243 
HIS HD1  H N N 244 
HIS HD2  H N N 245 
HIS HE1  H N N 246 
HIS HE2  H N N 247 
HIS HXT  H N N 248 
HOH O    O N N 249 
HOH H1   H N N 250 
HOH H2   H N N 251 
ILE N    N N N 252 
ILE CA   C N S 253 
ILE C    C N N 254 
ILE O    O N N 255 
ILE CB   C N S 256 
ILE CG1  C N N 257 
ILE CG2  C N N 258 
ILE CD1  C N N 259 
ILE OXT  O N N 260 
ILE H    H N N 261 
ILE H2   H N N 262 
ILE HA   H N N 263 
ILE HB   H N N 264 
ILE HG12 H N N 265 
ILE HG13 H N N 266 
ILE HG21 H N N 267 
ILE HG22 H N N 268 
ILE HG23 H N N 269 
ILE HD11 H N N 270 
ILE HD12 H N N 271 
ILE HD13 H N N 272 
ILE HXT  H N N 273 
LEU N    N N N 274 
LEU CA   C N S 275 
LEU C    C N N 276 
LEU O    O N N 277 
LEU CB   C N N 278 
LEU CG   C N N 279 
LEU CD1  C N N 280 
LEU CD2  C N N 281 
LEU OXT  O N N 282 
LEU H    H N N 283 
LEU H2   H N N 284 
LEU HA   H N N 285 
LEU HB2  H N N 286 
LEU HB3  H N N 287 
LEU HG   H N N 288 
LEU HD11 H N N 289 
LEU HD12 H N N 290 
LEU HD13 H N N 291 
LEU HD21 H N N 292 
LEU HD22 H N N 293 
LEU HD23 H N N 294 
LEU HXT  H N N 295 
LYS N    N N N 296 
LYS CA   C N S 297 
LYS C    C N N 298 
LYS O    O N N 299 
LYS CB   C N N 300 
LYS CG   C N N 301 
LYS CD   C N N 302 
LYS CE   C N N 303 
LYS NZ   N N N 304 
LYS OXT  O N N 305 
LYS H    H N N 306 
LYS H2   H N N 307 
LYS HA   H N N 308 
LYS HB2  H N N 309 
LYS HB3  H N N 310 
LYS HG2  H N N 311 
LYS HG3  H N N 312 
LYS HD2  H N N 313 
LYS HD3  H N N 314 
LYS HE2  H N N 315 
LYS HE3  H N N 316 
LYS HZ1  H N N 317 
LYS HZ2  H N N 318 
LYS HZ3  H N N 319 
LYS HXT  H N N 320 
MAN C1   C N S 321 
MAN C2   C N S 322 
MAN C3   C N S 323 
MAN C4   C N S 324 
MAN C5   C N R 325 
MAN C6   C N N 326 
MAN O1   O N N 327 
MAN O2   O N N 328 
MAN O3   O N N 329 
MAN O4   O N N 330 
MAN O5   O N N 331 
MAN O6   O N N 332 
MAN H1   H N N 333 
MAN H2   H N N 334 
MAN H3   H N N 335 
MAN H4   H N N 336 
MAN H5   H N N 337 
MAN H61  H N N 338 
MAN H62  H N N 339 
MAN HO1  H N N 340 
MAN HO2  H N N 341 
MAN HO3  H N N 342 
MAN HO4  H N N 343 
MAN HO6  H N N 344 
MET N    N N N 345 
MET CA   C N S 346 
MET C    C N N 347 
MET O    O N N 348 
MET CB   C N N 349 
MET CG   C N N 350 
MET SD   S N N 351 
MET CE   C N N 352 
MET OXT  O N N 353 
MET H    H N N 354 
MET H2   H N N 355 
MET HA   H N N 356 
MET HB2  H N N 357 
MET HB3  H N N 358 
MET HG2  H N N 359 
MET HG3  H N N 360 
MET HE1  H N N 361 
MET HE2  H N N 362 
MET HE3  H N N 363 
MET HXT  H N N 364 
NAG C1   C N R 365 
NAG C2   C N R 366 
NAG C3   C N R 367 
NAG C4   C N S 368 
NAG C5   C N R 369 
NAG C6   C N N 370 
NAG C7   C N N 371 
NAG C8   C N N 372 
NAG N2   N N N 373 
NAG O1   O N N 374 
NAG O3   O N N 375 
NAG O4   O N N 376 
NAG O5   O N N 377 
NAG O6   O N N 378 
NAG O7   O N N 379 
NAG H1   H N N 380 
NAG H2   H N N 381 
NAG H3   H N N 382 
NAG H4   H N N 383 
NAG H5   H N N 384 
NAG H61  H N N 385 
NAG H62  H N N 386 
NAG H81  H N N 387 
NAG H82  H N N 388 
NAG H83  H N N 389 
NAG HN2  H N N 390 
NAG HO1  H N N 391 
NAG HO3  H N N 392 
NAG HO4  H N N 393 
NAG HO6  H N N 394 
PHE N    N N N 395 
PHE CA   C N S 396 
PHE C    C N N 397 
PHE O    O N N 398 
PHE CB   C N N 399 
PHE CG   C Y N 400 
PHE CD1  C Y N 401 
PHE CD2  C Y N 402 
PHE CE1  C Y N 403 
PHE CE2  C Y N 404 
PHE CZ   C Y N 405 
PHE OXT  O N N 406 
PHE H    H N N 407 
PHE H2   H N N 408 
PHE HA   H N N 409 
PHE HB2  H N N 410 
PHE HB3  H N N 411 
PHE HD1  H N N 412 
PHE HD2  H N N 413 
PHE HE1  H N N 414 
PHE HE2  H N N 415 
PHE HZ   H N N 416 
PHE HXT  H N N 417 
PRO N    N N N 418 
PRO CA   C N S 419 
PRO C    C N N 420 
PRO O    O N N 421 
PRO CB   C N N 422 
PRO CG   C N N 423 
PRO CD   C N N 424 
PRO OXT  O N N 425 
PRO H    H N N 426 
PRO HA   H N N 427 
PRO HB2  H N N 428 
PRO HB3  H N N 429 
PRO HG2  H N N 430 
PRO HG3  H N N 431 
PRO HD2  H N N 432 
PRO HD3  H N N 433 
PRO HXT  H N N 434 
SER N    N N N 435 
SER CA   C N S 436 
SER C    C N N 437 
SER O    O N N 438 
SER CB   C N N 439 
SER OG   O N N 440 
SER OXT  O N N 441 
SER H    H N N 442 
SER H2   H N N 443 
SER HA   H N N 444 
SER HB2  H N N 445 
SER HB3  H N N 446 
SER HG   H N N 447 
SER HXT  H N N 448 
THR N    N N N 449 
THR CA   C N S 450 
THR C    C N N 451 
THR O    O N N 452 
THR CB   C N R 453 
THR OG1  O N N 454 
THR CG2  C N N 455 
THR OXT  O N N 456 
THR H    H N N 457 
THR H2   H N N 458 
THR HA   H N N 459 
THR HB   H N N 460 
THR HG1  H N N 461 
THR HG21 H N N 462 
THR HG22 H N N 463 
THR HG23 H N N 464 
THR HXT  H N N 465 
TRP N    N N N 466 
TRP CA   C N S 467 
TRP C    C N N 468 
TRP O    O N N 469 
TRP CB   C N N 470 
TRP CG   C Y N 471 
TRP CD1  C Y N 472 
TRP CD2  C Y N 473 
TRP NE1  N Y N 474 
TRP CE2  C Y N 475 
TRP CE3  C Y N 476 
TRP CZ2  C Y N 477 
TRP CZ3  C Y N 478 
TRP CH2  C Y N 479 
TRP OXT  O N N 480 
TRP H    H N N 481 
TRP H2   H N N 482 
TRP HA   H N N 483 
TRP HB2  H N N 484 
TRP HB3  H N N 485 
TRP HD1  H N N 486 
TRP HE1  H N N 487 
TRP HE3  H N N 488 
TRP HZ2  H N N 489 
TRP HZ3  H N N 490 
TRP HH2  H N N 491 
TRP HXT  H N N 492 
TYR N    N N N 493 
TYR CA   C N S 494 
TYR C    C N N 495 
TYR O    O N N 496 
TYR CB   C N N 497 
TYR CG   C Y N 498 
TYR CD1  C Y N 499 
TYR CD2  C Y N 500 
TYR CE1  C Y N 501 
TYR CE2  C Y N 502 
TYR CZ   C Y N 503 
TYR OH   O N N 504 
TYR OXT  O N N 505 
TYR H    H N N 506 
TYR H2   H N N 507 
TYR HA   H N N 508 
TYR HB2  H N N 509 
TYR HB3  H N N 510 
TYR HD1  H N N 511 
TYR HD2  H N N 512 
TYR HE1  H N N 513 
TYR HE2  H N N 514 
TYR HH   H N N 515 
TYR HXT  H N N 516 
VAL N    N N N 517 
VAL CA   C N S 518 
VAL C    C N N 519 
VAL O    O N N 520 
VAL CB   C N N 521 
VAL CG1  C N N 522 
VAL CG2  C N N 523 
VAL OXT  O N N 524 
VAL H    H N N 525 
VAL H2   H N N 526 
VAL HA   H N N 527 
VAL HB   H N N 528 
VAL HG11 H N N 529 
VAL HG12 H N N 530 
VAL HG13 H N N 531 
VAL HG21 H N N 532 
VAL HG22 H N N 533 
VAL HG23 H N N 534 
VAL HXT  H N N 535 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
BMA C1  C2   sing N N 70  
BMA C1  O1   sing N N 71  
BMA C1  O5   sing N N 72  
BMA C1  H1   sing N N 73  
BMA C2  C3   sing N N 74  
BMA C2  O2   sing N N 75  
BMA C2  H2   sing N N 76  
BMA C3  C4   sing N N 77  
BMA C3  O3   sing N N 78  
BMA C3  H3   sing N N 79  
BMA C4  C5   sing N N 80  
BMA C4  O4   sing N N 81  
BMA C4  H4   sing N N 82  
BMA C5  C6   sing N N 83  
BMA C5  O5   sing N N 84  
BMA C5  H5   sing N N 85  
BMA C6  O6   sing N N 86  
BMA C6  H61  sing N N 87  
BMA C6  H62  sing N N 88  
BMA O1  HO1  sing N N 89  
BMA O2  HO2  sing N N 90  
BMA O3  HO3  sing N N 91  
BMA O4  HO4  sing N N 92  
BMA O6  HO6  sing N N 93  
CYS N   CA   sing N N 94  
CYS N   H    sing N N 95  
CYS N   H2   sing N N 96  
CYS CA  C    sing N N 97  
CYS CA  CB   sing N N 98  
CYS CA  HA   sing N N 99  
CYS C   O    doub N N 100 
CYS C   OXT  sing N N 101 
CYS CB  SG   sing N N 102 
CYS CB  HB2  sing N N 103 
CYS CB  HB3  sing N N 104 
CYS SG  HG   sing N N 105 
CYS OXT HXT  sing N N 106 
EZ7 C60 C58  sing N N 107 
EZ7 N7  C58  sing N N 108 
EZ7 N7  C3   sing N N 109 
EZ7 C2  C3   sing Y N 110 
EZ7 C2  C1   doub Y N 111 
EZ7 C58 O59  doub N N 112 
EZ7 C3  C4   doub Y N 113 
EZ7 C1  C12  sing Y N 114 
EZ7 C4  C11  sing Y N 115 
EZ7 C12 C11  doub Y N 116 
EZ7 C12 O13  sing Y N 117 
EZ7 C11 N10  sing Y N 118 
EZ7 O13 C9   sing Y N 119 
EZ7 N10 C9   doub Y N 120 
EZ7 C9  C17  sing N N 121 
EZ7 C17 C16  sing Y N 122 
EZ7 C17 C18  doub Y N 123 
EZ7 C16 C15  doub Y N 124 
EZ7 C18 C19  sing Y N 125 
EZ7 C15 N14  sing Y N 126 
EZ7 C19 N14  doub Y N 127 
EZ7 C19 C23  sing N N 128 
EZ7 C57 N55  sing N N 129 
EZ7 C26 N27  sing N N 130 
EZ7 C26 C25  sing N N 131 
EZ7 C23 N27  sing N N 132 
EZ7 C23 O24  doub N N 133 
EZ7 N55 N56  sing Y N 134 
EZ7 N55 N54  sing Y N 135 
EZ7 N27 C28  sing N N 136 
EZ7 N56 C52  doub Y N 137 
EZ7 C25 N30  sing N N 138 
EZ7 N54 N53  doub Y N 139 
EZ7 N30 C29  sing N N 140 
EZ7 N30 C40  sing N N 141 
EZ7 C28 C29  sing N N 142 
EZ7 C52 N53  sing Y N 143 
EZ7 C52 C40  sing N N 144 
EZ7 C40 C44  sing N N 145 
EZ7 C45 C44  doub Y N 146 
EZ7 C45 C46  sing Y N 147 
EZ7 C44 C43  sing Y N 148 
EZ7 C46 C41  doub Y N 149 
EZ7 C43 C42  doub Y N 150 
EZ7 C41 C42  sing Y N 151 
EZ7 C2  H1   sing N N 152 
EZ7 C4  H2   sing N N 153 
EZ7 C16 H3   sing N N 154 
EZ7 C18 H4   sing N N 155 
EZ7 C60 H5   sing N N 156 
EZ7 C60 H6   sing N N 157 
EZ7 C60 H7   sing N N 158 
EZ7 N7  H8   sing N N 159 
EZ7 C1  H9   sing N N 160 
EZ7 C15 H10  sing N N 161 
EZ7 C28 H11  sing N N 162 
EZ7 C28 H12  sing N N 163 
EZ7 C29 H13  sing N N 164 
EZ7 C29 H14  sing N N 165 
EZ7 C26 H15  sing N N 166 
EZ7 C26 H16  sing N N 167 
EZ7 C25 H17  sing N N 168 
EZ7 C25 H18  sing N N 169 
EZ7 C40 H20  sing N N 170 
EZ7 C57 H21  sing N N 171 
EZ7 C57 H22  sing N N 172 
EZ7 C57 H23  sing N N 173 
EZ7 C43 H24  sing N N 174 
EZ7 C42 H25  sing N N 175 
EZ7 C41 H26  sing N N 176 
EZ7 C46 H27  sing N N 177 
EZ7 C45 H28  sing N N 178 
GLN N   CA   sing N N 179 
GLN N   H    sing N N 180 
GLN N   H2   sing N N 181 
GLN CA  C    sing N N 182 
GLN CA  CB   sing N N 183 
GLN CA  HA   sing N N 184 
GLN C   O    doub N N 185 
GLN C   OXT  sing N N 186 
GLN CB  CG   sing N N 187 
GLN CB  HB2  sing N N 188 
GLN CB  HB3  sing N N 189 
GLN CG  CD   sing N N 190 
GLN CG  HG2  sing N N 191 
GLN CG  HG3  sing N N 192 
GLN CD  OE1  doub N N 193 
GLN CD  NE2  sing N N 194 
GLN NE2 HE21 sing N N 195 
GLN NE2 HE22 sing N N 196 
GLN OXT HXT  sing N N 197 
GLU N   CA   sing N N 198 
GLU N   H    sing N N 199 
GLU N   H2   sing N N 200 
GLU CA  C    sing N N 201 
GLU CA  CB   sing N N 202 
GLU CA  HA   sing N N 203 
GLU C   O    doub N N 204 
GLU C   OXT  sing N N 205 
GLU CB  CG   sing N N 206 
GLU CB  HB2  sing N N 207 
GLU CB  HB3  sing N N 208 
GLU CG  CD   sing N N 209 
GLU CG  HG2  sing N N 210 
GLU CG  HG3  sing N N 211 
GLU CD  OE1  doub N N 212 
GLU CD  OE2  sing N N 213 
GLU OE2 HE2  sing N N 214 
GLU OXT HXT  sing N N 215 
GLY N   CA   sing N N 216 
GLY N   H    sing N N 217 
GLY N   H2   sing N N 218 
GLY CA  C    sing N N 219 
GLY CA  HA2  sing N N 220 
GLY CA  HA3  sing N N 221 
GLY C   O    doub N N 222 
GLY C   OXT  sing N N 223 
GLY OXT HXT  sing N N 224 
HIS N   CA   sing N N 225 
HIS N   H    sing N N 226 
HIS N   H2   sing N N 227 
HIS CA  C    sing N N 228 
HIS CA  CB   sing N N 229 
HIS CA  HA   sing N N 230 
HIS C   O    doub N N 231 
HIS C   OXT  sing N N 232 
HIS CB  CG   sing N N 233 
HIS CB  HB2  sing N N 234 
HIS CB  HB3  sing N N 235 
HIS CG  ND1  sing Y N 236 
HIS CG  CD2  doub Y N 237 
HIS ND1 CE1  doub Y N 238 
HIS ND1 HD1  sing N N 239 
HIS CD2 NE2  sing Y N 240 
HIS CD2 HD2  sing N N 241 
HIS CE1 NE2  sing Y N 242 
HIS CE1 HE1  sing N N 243 
HIS NE2 HE2  sing N N 244 
HIS OXT HXT  sing N N 245 
HOH O   H1   sing N N 246 
HOH O   H2   sing N N 247 
ILE N   CA   sing N N 248 
ILE N   H    sing N N 249 
ILE N   H2   sing N N 250 
ILE CA  C    sing N N 251 
ILE CA  CB   sing N N 252 
ILE CA  HA   sing N N 253 
ILE C   O    doub N N 254 
ILE C   OXT  sing N N 255 
ILE CB  CG1  sing N N 256 
ILE CB  CG2  sing N N 257 
ILE CB  HB   sing N N 258 
ILE CG1 CD1  sing N N 259 
ILE CG1 HG12 sing N N 260 
ILE CG1 HG13 sing N N 261 
ILE CG2 HG21 sing N N 262 
ILE CG2 HG22 sing N N 263 
ILE CG2 HG23 sing N N 264 
ILE CD1 HD11 sing N N 265 
ILE CD1 HD12 sing N N 266 
ILE CD1 HD13 sing N N 267 
ILE OXT HXT  sing N N 268 
LEU N   CA   sing N N 269 
LEU N   H    sing N N 270 
LEU N   H2   sing N N 271 
LEU CA  C    sing N N 272 
LEU CA  CB   sing N N 273 
LEU CA  HA   sing N N 274 
LEU C   O    doub N N 275 
LEU C   OXT  sing N N 276 
LEU CB  CG   sing N N 277 
LEU CB  HB2  sing N N 278 
LEU CB  HB3  sing N N 279 
LEU CG  CD1  sing N N 280 
LEU CG  CD2  sing N N 281 
LEU CG  HG   sing N N 282 
LEU CD1 HD11 sing N N 283 
LEU CD1 HD12 sing N N 284 
LEU CD1 HD13 sing N N 285 
LEU CD2 HD21 sing N N 286 
LEU CD2 HD22 sing N N 287 
LEU CD2 HD23 sing N N 288 
LEU OXT HXT  sing N N 289 
LYS N   CA   sing N N 290 
LYS N   H    sing N N 291 
LYS N   H2   sing N N 292 
LYS CA  C    sing N N 293 
LYS CA  CB   sing N N 294 
LYS CA  HA   sing N N 295 
LYS C   O    doub N N 296 
LYS C   OXT  sing N N 297 
LYS CB  CG   sing N N 298 
LYS CB  HB2  sing N N 299 
LYS CB  HB3  sing N N 300 
LYS CG  CD   sing N N 301 
LYS CG  HG2  sing N N 302 
LYS CG  HG3  sing N N 303 
LYS CD  CE   sing N N 304 
LYS CD  HD2  sing N N 305 
LYS CD  HD3  sing N N 306 
LYS CE  NZ   sing N N 307 
LYS CE  HE2  sing N N 308 
LYS CE  HE3  sing N N 309 
LYS NZ  HZ1  sing N N 310 
LYS NZ  HZ2  sing N N 311 
LYS NZ  HZ3  sing N N 312 
LYS OXT HXT  sing N N 313 
MAN C1  C2   sing N N 314 
MAN C1  O1   sing N N 315 
MAN C1  O5   sing N N 316 
MAN C1  H1   sing N N 317 
MAN C2  C3   sing N N 318 
MAN C2  O2   sing N N 319 
MAN C2  H2   sing N N 320 
MAN C3  C4   sing N N 321 
MAN C3  O3   sing N N 322 
MAN C3  H3   sing N N 323 
MAN C4  C5   sing N N 324 
MAN C4  O4   sing N N 325 
MAN C4  H4   sing N N 326 
MAN C5  C6   sing N N 327 
MAN C5  O5   sing N N 328 
MAN C5  H5   sing N N 329 
MAN C6  O6   sing N N 330 
MAN C6  H61  sing N N 331 
MAN C6  H62  sing N N 332 
MAN O1  HO1  sing N N 333 
MAN O2  HO2  sing N N 334 
MAN O3  HO3  sing N N 335 
MAN O4  HO4  sing N N 336 
MAN O6  HO6  sing N N 337 
MET N   CA   sing N N 338 
MET N   H    sing N N 339 
MET N   H2   sing N N 340 
MET CA  C    sing N N 341 
MET CA  CB   sing N N 342 
MET CA  HA   sing N N 343 
MET C   O    doub N N 344 
MET C   OXT  sing N N 345 
MET CB  CG   sing N N 346 
MET CB  HB2  sing N N 347 
MET CB  HB3  sing N N 348 
MET CG  SD   sing N N 349 
MET CG  HG2  sing N N 350 
MET CG  HG3  sing N N 351 
MET SD  CE   sing N N 352 
MET CE  HE1  sing N N 353 
MET CE  HE2  sing N N 354 
MET CE  HE3  sing N N 355 
MET OXT HXT  sing N N 356 
NAG C1  C2   sing N N 357 
NAG C1  O1   sing N N 358 
NAG C1  O5   sing N N 359 
NAG C1  H1   sing N N 360 
NAG C2  C3   sing N N 361 
NAG C2  N2   sing N N 362 
NAG C2  H2   sing N N 363 
NAG C3  C4   sing N N 364 
NAG C3  O3   sing N N 365 
NAG C3  H3   sing N N 366 
NAG C4  C5   sing N N 367 
NAG C4  O4   sing N N 368 
NAG C4  H4   sing N N 369 
NAG C5  C6   sing N N 370 
NAG C5  O5   sing N N 371 
NAG C5  H5   sing N N 372 
NAG C6  O6   sing N N 373 
NAG C6  H61  sing N N 374 
NAG C6  H62  sing N N 375 
NAG C7  C8   sing N N 376 
NAG C7  N2   sing N N 377 
NAG C7  O7   doub N N 378 
NAG C8  H81  sing N N 379 
NAG C8  H82  sing N N 380 
NAG C8  H83  sing N N 381 
NAG N2  HN2  sing N N 382 
NAG O1  HO1  sing N N 383 
NAG O3  HO3  sing N N 384 
NAG O4  HO4  sing N N 385 
NAG O6  HO6  sing N N 386 
PHE N   CA   sing N N 387 
PHE N   H    sing N N 388 
PHE N   H2   sing N N 389 
PHE CA  C    sing N N 390 
PHE CA  CB   sing N N 391 
PHE CA  HA   sing N N 392 
PHE C   O    doub N N 393 
PHE C   OXT  sing N N 394 
PHE CB  CG   sing N N 395 
PHE CB  HB2  sing N N 396 
PHE CB  HB3  sing N N 397 
PHE CG  CD1  doub Y N 398 
PHE CG  CD2  sing Y N 399 
PHE CD1 CE1  sing Y N 400 
PHE CD1 HD1  sing N N 401 
PHE CD2 CE2  doub Y N 402 
PHE CD2 HD2  sing N N 403 
PHE CE1 CZ   doub Y N 404 
PHE CE1 HE1  sing N N 405 
PHE CE2 CZ   sing Y N 406 
PHE CE2 HE2  sing N N 407 
PHE CZ  HZ   sing N N 408 
PHE OXT HXT  sing N N 409 
PRO N   CA   sing N N 410 
PRO N   CD   sing N N 411 
PRO N   H    sing N N 412 
PRO CA  C    sing N N 413 
PRO CA  CB   sing N N 414 
PRO CA  HA   sing N N 415 
PRO C   O    doub N N 416 
PRO C   OXT  sing N N 417 
PRO CB  CG   sing N N 418 
PRO CB  HB2  sing N N 419 
PRO CB  HB3  sing N N 420 
PRO CG  CD   sing N N 421 
PRO CG  HG2  sing N N 422 
PRO CG  HG3  sing N N 423 
PRO CD  HD2  sing N N 424 
PRO CD  HD3  sing N N 425 
PRO OXT HXT  sing N N 426 
SER N   CA   sing N N 427 
SER N   H    sing N N 428 
SER N   H2   sing N N 429 
SER CA  C    sing N N 430 
SER CA  CB   sing N N 431 
SER CA  HA   sing N N 432 
SER C   O    doub N N 433 
SER C   OXT  sing N N 434 
SER CB  OG   sing N N 435 
SER CB  HB2  sing N N 436 
SER CB  HB3  sing N N 437 
SER OG  HG   sing N N 438 
SER OXT HXT  sing N N 439 
THR N   CA   sing N N 440 
THR N   H    sing N N 441 
THR N   H2   sing N N 442 
THR CA  C    sing N N 443 
THR CA  CB   sing N N 444 
THR CA  HA   sing N N 445 
THR C   O    doub N N 446 
THR C   OXT  sing N N 447 
THR CB  OG1  sing N N 448 
THR CB  CG2  sing N N 449 
THR CB  HB   sing N N 450 
THR OG1 HG1  sing N N 451 
THR CG2 HG21 sing N N 452 
THR CG2 HG22 sing N N 453 
THR CG2 HG23 sing N N 454 
THR OXT HXT  sing N N 455 
TRP N   CA   sing N N 456 
TRP N   H    sing N N 457 
TRP N   H2   sing N N 458 
TRP CA  C    sing N N 459 
TRP CA  CB   sing N N 460 
TRP CA  HA   sing N N 461 
TRP C   O    doub N N 462 
TRP C   OXT  sing N N 463 
TRP CB  CG   sing N N 464 
TRP CB  HB2  sing N N 465 
TRP CB  HB3  sing N N 466 
TRP CG  CD1  doub Y N 467 
TRP CG  CD2  sing Y N 468 
TRP CD1 NE1  sing Y N 469 
TRP CD1 HD1  sing N N 470 
TRP CD2 CE2  doub Y N 471 
TRP CD2 CE3  sing Y N 472 
TRP NE1 CE2  sing Y N 473 
TRP NE1 HE1  sing N N 474 
TRP CE2 CZ2  sing Y N 475 
TRP CE3 CZ3  doub Y N 476 
TRP CE3 HE3  sing N N 477 
TRP CZ2 CH2  doub Y N 478 
TRP CZ2 HZ2  sing N N 479 
TRP CZ3 CH2  sing Y N 480 
TRP CZ3 HZ3  sing N N 481 
TRP CH2 HH2  sing N N 482 
TRP OXT HXT  sing N N 483 
TYR N   CA   sing N N 484 
TYR N   H    sing N N 485 
TYR N   H2   sing N N 486 
TYR CA  C    sing N N 487 
TYR CA  CB   sing N N 488 
TYR CA  HA   sing N N 489 
TYR C   O    doub N N 490 
TYR C   OXT  sing N N 491 
TYR CB  CG   sing N N 492 
TYR CB  HB2  sing N N 493 
TYR CB  HB3  sing N N 494 
TYR CG  CD1  doub Y N 495 
TYR CG  CD2  sing Y N 496 
TYR CD1 CE1  sing Y N 497 
TYR CD1 HD1  sing N N 498 
TYR CD2 CE2  doub Y N 499 
TYR CD2 HD2  sing N N 500 
TYR CE1 CZ   doub Y N 501 
TYR CE1 HE1  sing N N 502 
TYR CE2 CZ   sing Y N 503 
TYR CE2 HE2  sing N N 504 
TYR CZ  OH   sing N N 505 
TYR OH  HH   sing N N 506 
TYR OXT HXT  sing N N 507 
VAL N   CA   sing N N 508 
VAL N   H    sing N N 509 
VAL N   H2   sing N N 510 
VAL CA  C    sing N N 511 
VAL CA  CB   sing N N 512 
VAL CA  HA   sing N N 513 
VAL C   O    doub N N 514 
VAL C   OXT  sing N N 515 
VAL CB  CG1  sing N N 516 
VAL CB  CG2  sing N N 517 
VAL CB  HB   sing N N 518 
VAL CG1 HG11 sing N N 519 
VAL CG1 HG12 sing N N 520 
VAL CG1 HG13 sing N N 521 
VAL CG2 HG21 sing N N 522 
VAL CG2 HG22 sing N N 523 
VAL CG2 HG23 sing N N 524 
VAL OXT HXT  sing N N 525 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           'R56 AI117675' 
_pdbx_audit_support.ordinal                1 
# 
loop_
_pdbx_entity_branch_list.entity_id 
_pdbx_entity_branch_list.comp_id 
_pdbx_entity_branch_list.num 
_pdbx_entity_branch_list.hetero 
3 NAG 1 n 
3 NAG 2 n 
3 BMA 3 n 
3 MAN 4 n 
4 NAG 1 n 
4 NAG 2 n 
4 BMA 3 n 
5 NAG 1 n 
5 NAG 2 n 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   5W5S 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    6CF7 
_atom_sites.fract_transf_matrix[1][1]   0.006194 
_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]   0.006194 
_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]   0.006194 
_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 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . ASP A 1 1   ? 33.614  63.913  49.533  1.00 111.63 ? 11  ASP A N   1 
ATOM   2    C CA  . ASP A 1 1   ? 33.460  63.601  48.117  1.00 113.79 ? 11  ASP A CA  1 
ATOM   3    C C   . ASP A 1 1   ? 33.631  62.111  47.860  1.00 111.81 ? 11  ASP A C   1 
ATOM   4    O O   . ASP A 1 1   ? 34.634  61.513  48.250  1.00 115.87 ? 11  ASP A O   1 
ATOM   5    C CB  . ASP A 1 1   ? 34.458  64.399  47.279  1.00 116.10 ? 11  ASP A CB  1 
ATOM   6    C CG  . ASP A 1 1   ? 34.112  65.871  47.213  1.00 120.75 ? 11  ASP A CG  1 
ATOM   7    O OD1 . ASP A 1 1   ? 33.391  66.350  48.113  1.00 122.95 ? 11  ASP A OD1 1 
ATOM   8    O OD2 . ASP A 1 1   ? 34.557  66.549  46.263  1.00 123.11 ? 11  ASP A OD2 1 
ATOM   9    N N   . THR A 1 2   ? 32.642  61.515  47.198  1.00 101.89 ? 12  THR A N   1 
ATOM   10   C CA  . THR A 1 2   ? 32.628  60.083  46.943  1.00 94.29  ? 12  THR A CA  1 
ATOM   11   C C   . THR A 1 2   ? 32.048  59.810  45.564  1.00 87.88  ? 12  THR A C   1 
ATOM   12   O O   . THR A 1 2   ? 31.219  60.571  45.057  1.00 89.62  ? 12  THR A O   1 
ATOM   13   C CB  . THR A 1 2   ? 31.807  59.324  47.996  1.00 93.62  ? 12  THR A CB  1 
ATOM   14   O OG1 . THR A 1 2   ? 30.569  60.010  48.221  1.00 90.27  ? 12  THR A OG1 1 
ATOM   15   C CG2 . THR A 1 2   ? 32.573  59.212  49.306  1.00 104.77 ? 12  THR A CG2 1 
ATOM   16   N N   . ILE A 1 3   ? 32.494  58.710  44.965  1.00 85.25  ? 13  ILE A N   1 
ATOM   17   C CA  . ILE A 1 3   ? 31.925  58.194  43.727  1.00 82.49  ? 13  ILE A CA  1 
ATOM   18   C C   . ILE A 1 3   ? 31.687  56.701  43.909  1.00 79.83  ? 13  ILE A C   1 
ATOM   19   O O   . ILE A 1 3   ? 32.475  56.009  44.564  1.00 80.00  ? 13  ILE A O   1 
ATOM   20   C CB  . ILE A 1 3   ? 32.832  58.474  42.507  1.00 82.50  ? 13  ILE A CB  1 
ATOM   21   C CG1 . ILE A 1 3   ? 32.067  58.235  41.204  1.00 80.17  ? 13  ILE A CG1 1 
ATOM   22   C CG2 . ILE A 1 3   ? 34.094  57.621  42.546  1.00 82.11  ? 13  ILE A CG2 1 
ATOM   23   C CD1 . ILE A 1 3   ? 32.887  58.501  39.961  1.00 80.28  ? 13  ILE A CD1 1 
ATOM   24   N N   . CYS A 1 4   ? 30.583  56.211  43.356  1.00 77.54  ? 14  CYS A N   1 
ATOM   25   C CA  . CYS A 1 4   ? 30.191  54.820  43.510  1.00 85.22  ? 14  CYS A CA  1 
ATOM   26   C C   . CYS A 1 4   ? 29.917  54.208  42.145  1.00 72.42  ? 14  CYS A C   1 
ATOM   27   O O   . CYS A 1 4   ? 29.619  54.906  41.173  1.00 72.40  ? 14  CYS A O   1 
ATOM   28   C CB  . CYS A 1 4   ? 28.950  54.681  44.403  1.00 85.83  ? 14  CYS A CB  1 
ATOM   29   S SG  . CYS A 1 4   ? 29.188  55.153  46.133  1.00 95.59  ? 14  CYS A SG  1 
ATOM   30   N N   . ILE A 1 5   ? 30.030  52.885  42.085  1.00 70.33  ? 15  ILE A N   1 
ATOM   31   C CA  . ILE A 1 5   ? 29.674  52.106  40.907  1.00 67.69  ? 15  ILE A CA  1 
ATOM   32   C C   . ILE A 1 5   ? 28.560  51.150  41.306  1.00 65.89  ? 15  ILE A C   1 
ATOM   33   O O   . ILE A 1 5   ? 28.708  50.386  42.267  1.00 65.90  ? 15  ILE A O   1 
ATOM   34   C CB  . ILE A 1 5   ? 30.880  51.336  40.334  1.00 68.24  ? 15  ILE A CB  1 
ATOM   35   C CG1 . ILE A 1 5   ? 31.809  52.271  39.554  1.00 68.35  ? 15  ILE A CG1 1 
ATOM   36   C CG2 . ILE A 1 5   ? 30.411  50.195  39.446  1.00 64.04  ? 15  ILE A CG2 1 
ATOM   37   C CD1 . ILE A 1 5   ? 32.765  53.066  40.417  1.00 71.20  ? 15  ILE A CD1 1 
ATOM   38   N N   . GLY A 1 6   ? 27.445  51.206  40.584  1.00 64.56  ? 16  GLY A N   1 
ATOM   39   C CA  . GLY A 1 6   ? 26.315  50.347  40.880  1.00 64.32  ? 16  GLY A CA  1 
ATOM   40   C C   . GLY A 1 6   ? 25.547  49.943  39.640  1.00 66.00  ? 16  GLY A C   1 
ATOM   41   O O   . GLY A 1 6   ? 26.021  50.153  38.519  1.00 62.88  ? 16  GLY A O   1 
ATOM   42   N N   . TYR A 1 7   ? 24.357  49.374  39.818  1.00 60.03  ? 17  TYR A N   1 
ATOM   43   C CA  . TYR A 1 7   ? 23.594  48.866  38.690  1.00 57.49  ? 17  TYR A CA  1 
ATOM   44   C C   . TYR A 1 7   ? 22.110  49.167  38.869  1.00 57.57  ? 17  TYR A C   1 
ATOM   45   O O   . TYR A 1 7   ? 21.642  49.500  39.962  1.00 58.99  ? 17  TYR A O   1 
ATOM   46   C CB  . TYR A 1 7   ? 23.831  47.364  38.491  1.00 55.36  ? 17  TYR A CB  1 
ATOM   47   C CG  . TYR A 1 7   ? 23.728  46.526  39.743  1.00 55.47  ? 17  TYR A CG  1 
ATOM   48   C CD1 . TYR A 1 7   ? 22.505  46.033  40.171  1.00 54.86  ? 17  TYR A CD1 1 
ATOM   49   C CD2 . TYR A 1 7   ? 24.857  46.212  40.487  1.00 56.34  ? 17  TYR A CD2 1 
ATOM   50   C CE1 . TYR A 1 7   ? 22.405  45.261  41.311  1.00 55.16  ? 17  TYR A CE1 1 
ATOM   51   C CE2 . TYR A 1 7   ? 24.767  45.439  41.631  1.00 56.63  ? 17  TYR A CE2 1 
ATOM   52   C CZ  . TYR A 1 7   ? 23.538  44.966  42.037  1.00 56.05  ? 17  TYR A CZ  1 
ATOM   53   O OH  . TYR A 1 7   ? 23.437  44.197  43.173  1.00 75.22  ? 17  TYR A OH  1 
ATOM   54   N N   . HIS A 1 8   ? 21.379  49.032  37.763  1.00 56.88  ? 18  HIS A N   1 
ATOM   55   C CA  . HIS A 1 8   ? 19.992  49.463  37.658  1.00 56.37  ? 18  HIS A CA  1 
ATOM   56   C C   . HIS A 1 8   ? 19.055  48.540  38.435  1.00 55.63  ? 18  HIS A C   1 
ATOM   57   O O   . HIS A 1 8   ? 19.337  47.361  38.663  1.00 54.28  ? 18  HIS A O   1 
ATOM   58   C CB  . HIS A 1 8   ? 19.573  49.513  36.186  1.00 55.11  ? 18  HIS A CB  1 
ATOM   59   C CG  . HIS A 1 8   ? 18.139  49.887  35.966  1.00 58.18  ? 18  HIS A CG  1 
ATOM   60   N ND1 . HIS A 1 8   ? 17.714  51.195  35.884  1.00 57.25  ? 18  HIS A ND1 1 
ATOM   61   C CD2 . HIS A 1 8   ? 17.034  49.122  35.797  1.00 53.99  ? 18  HIS A CD2 1 
ATOM   62   C CE1 . HIS A 1 8   ? 16.409  51.221  35.681  1.00 57.85  ? 18  HIS A CE1 1 
ATOM   63   N NE2 . HIS A 1 8   ? 15.972  49.976  35.625  1.00 56.08  ? 18  HIS A NE2 1 
ATOM   64   N N   . ALA A 1 9   ? 17.919  49.106  38.839  1.00 58.40  ? 19  ALA A N   1 
ATOM   65   C CA  . ALA A 1 9   ? 16.829  48.358  39.445  1.00 56.28  ? 19  ALA A CA  1 
ATOM   66   C C   . ALA A 1 9   ? 15.521  49.047  39.083  1.00 56.96  ? 19  ALA A C   1 
ATOM   67   O O   . ALA A 1 9   ? 15.505  50.223  38.711  1.00 58.32  ? 19  ALA A O   1 
ATOM   68   C CB  . ALA A 1 9   ? 16.993  48.255  40.965  1.00 57.78  ? 19  ALA A CB  1 
ATOM   69   N N   . ASN A 1 10  ? 14.421  48.306  39.188  1.00 56.15  ? 20  ASN A N   1 
ATOM   70   C CA  . ASN A 1 10  ? 13.105  48.858  38.887  1.00 56.89  ? 20  ASN A CA  1 
ATOM   71   C C   . ASN A 1 10  ? 12.043  48.006  39.571  1.00 56.69  ? 20  ASN A C   1 
ATOM   72   O O   . ASN A 1 10  ? 12.350  47.073  40.317  1.00 59.31  ? 20  ASN A O   1 
ATOM   73   C CB  . ASN A 1 10  ? 12.871  48.952  37.373  1.00 57.59  ? 20  ASN A CB  1 
ATOM   74   C CG  . ASN A 1 10  ? 13.063  47.627  36.663  1.00 58.89  ? 20  ASN A CG  1 
ATOM   75   O OD1 . ASN A 1 10  ? 13.214  46.582  37.295  1.00 70.55  ? 20  ASN A OD1 1 
ATOM   76   N ND2 . ASN A 1 10  ? 13.056  47.665  35.335  1.00 57.77  ? 20  ASN A ND2 1 
ATOM   77   N N   . ASN A 1 11  ? 10.778  48.341  39.308  1.00 57.31  ? 21  ASN A N   1 
ATOM   78   C CA  . ASN A 1 11  ? 9.638   47.628  39.869  1.00 65.24  ? 21  ASN A CA  1 
ATOM   79   C C   . ASN A 1 11  ? 9.179   46.474  38.987  1.00 59.84  ? 21  ASN A C   1 
ATOM   80   O O   . ASN A 1 11  ? 8.024   46.045  39.093  1.00 72.52  ? 21  ASN A O   1 
ATOM   81   C CB  . ASN A 1 11  ? 8.477   48.595  40.108  1.00 80.02  ? 21  ASN A CB  1 
ATOM   82   C CG  . ASN A 1 11  ? 8.013   49.268  38.832  1.00 84.90  ? 21  ASN A CG  1 
ATOM   83   O OD1 . ASN A 1 11  ? 8.753   49.331  37.851  1.00 82.86  ? 21  ASN A OD1 1 
ATOM   84   N ND2 . ASN A 1 11  ? 6.786   49.777  38.837  1.00 103.68 ? 21  ASN A ND2 1 
ATOM   85   N N   . SER A 1 12  ? 10.057  45.966  38.126  1.00 61.81  ? 22  SER A N   1 
ATOM   86   C CA  . SER A 1 12  ? 9.686   44.906  37.200  1.00 50.93  ? 22  SER A CA  1 
ATOM   87   C C   . SER A 1 12  ? 9.419   43.607  37.948  1.00 50.23  ? 22  SER A C   1 
ATOM   88   O O   . SER A 1 12  ? 10.197  43.205  38.818  1.00 51.20  ? 22  SER A O   1 
ATOM   89   C CB  . SER A 1 12  ? 10.791  44.702  36.167  1.00 49.26  ? 22  SER A CB  1 
ATOM   90   O OG  . SER A 1 12  ? 10.542  43.558  35.370  1.00 47.22  ? 22  SER A OG  1 
ATOM   91   N N   . THR A 1 13  ? 8.311   42.953  37.608  1.00 49.61  ? 23  THR A N   1 
ATOM   92   C CA  . THR A 1 13  ? 7.989   41.632  38.126  1.00 51.00  ? 23  THR A CA  1 
ATOM   93   C C   . THR A 1 13  ? 8.330   40.527  37.136  1.00 49.27  ? 23  THR A C   1 
ATOM   94   O O   . THR A 1 13  ? 7.950   39.373  37.355  1.00 46.25  ? 23  THR A O   1 
ATOM   95   C CB  . THR A 1 13  ? 6.508   41.554  38.506  1.00 55.79  ? 23  THR A CB  1 
ATOM   96   O OG1 . THR A 1 13  ? 5.700   41.755  37.339  1.00 61.53  ? 23  THR A OG1 1 
ATOM   97   C CG2 . THR A 1 13  ? 6.167   42.610  39.544  1.00 52.60  ? 23  THR A CG2 1 
ATOM   98   N N   . ASP A 1 14  ? 9.029   40.860  36.051  1.00 47.01  ? 24  ASP A N   1 
ATOM   99   C CA  . ASP A 1 14  ? 9.437   39.859  35.074  1.00 43.90  ? 24  ASP A CA  1 
ATOM   100  C C   . ASP A 1 14  ? 10.326  38.811  35.727  1.00 42.93  ? 24  ASP A C   1 
ATOM   101  O O   . ASP A 1 14  ? 11.311  39.141  36.394  1.00 52.95  ? 24  ASP A O   1 
ATOM   102  C CB  . ASP A 1 14  ? 10.183  40.518  33.914  1.00 48.65  ? 24  ASP A CB  1 
ATOM   103  C CG  . ASP A 1 14  ? 9.280   41.357  33.037  1.00 57.31  ? 24  ASP A CG  1 
ATOM   104  O OD1 . ASP A 1 14  ? 8.047   41.169  33.086  1.00 58.94  ? 24  ASP A OD1 1 
ATOM   105  O OD2 . ASP A 1 14  ? 9.810   42.202  32.285  1.00 53.94  ? 24  ASP A OD2 1 
ATOM   106  N N   . THR A 1 15  ? 9.979   37.545  35.528  1.00 41.39  ? 25  THR A N   1 
ATOM   107  C CA  . THR A 1 15  ? 10.757  36.430  36.043  1.00 40.75  ? 25  THR A CA  1 
ATOM   108  C C   . THR A 1 15  ? 11.184  35.525  34.898  1.00 38.83  ? 25  THR A C   1 
ATOM   109  O O   . THR A 1 15  ? 10.435  35.321  33.938  1.00 39.06  ? 25  THR A O   1 
ATOM   110  C CB  . THR A 1 15  ? 9.963   35.626  37.073  1.00 41.48  ? 25  THR A CB  1 
ATOM   111  O OG1 . THR A 1 15  ? 8.694   35.261  36.518  1.00 50.03  ? 25  THR A OG1 1 
ATOM   112  C CG2 . THR A 1 15  ? 9.746   36.445  38.335  1.00 43.58  ? 25  THR A CG2 1 
ATOM   113  N N   . VAL A 1 16  ? 12.402  34.997  35.000  1.00 41.10  ? 26  VAL A N   1 
ATOM   114  C CA  . VAL A 1 16  ? 12.914  34.014  34.060  1.00 36.67  ? 26  VAL A CA  1 
ATOM   115  C C   . VAL A 1 16  ? 13.518  32.869  34.858  1.00 36.64  ? 26  VAL A C   1 
ATOM   116  O O   . VAL A 1 16  ? 13.774  32.983  36.058  1.00 41.37  ? 26  VAL A O   1 
ATOM   117  C CB  . VAL A 1 16  ? 13.959  34.608  33.090  1.00 36.13  ? 26  VAL A CB  1 
ATOM   118  C CG1 . VAL A 1 16  ? 13.360  35.756  32.300  1.00 36.38  ? 26  VAL A CG1 1 
ATOM   119  C CG2 . VAL A 1 16  ? 15.187  35.066  33.851  1.00 37.05  ? 26  VAL A CG2 1 
ATOM   120  N N   . ASP A 1 17  ? 13.731  31.750  34.176  1.00 35.37  ? 27  ASP A N   1 
ATOM   121  C CA  . ASP A 1 17  ? 14.386  30.596  34.769  1.00 35.34  ? 27  ASP A CA  1 
ATOM   122  C C   . ASP A 1 17  ? 15.842  30.556  34.331  1.00 34.93  ? 27  ASP A C   1 
ATOM   123  O O   . ASP A 1 17  ? 16.168  30.899  33.191  1.00 37.25  ? 27  ASP A O   1 
ATOM   124  C CB  . ASP A 1 17  ? 13.684  29.297  34.372  1.00 34.81  ? 27  ASP A CB  1 
ATOM   125  C CG  . ASP A 1 17  ? 12.325  29.149  35.014  1.00 45.19  ? 27  ASP A CG  1 
ATOM   126  O OD1 . ASP A 1 17  ? 12.124  29.695  36.118  1.00 50.85  ? 27  ASP A OD1 1 
ATOM   127  O OD2 . ASP A 1 17  ? 11.453  28.485  34.413  1.00 53.07  ? 27  ASP A OD2 1 
ATOM   128  N N   . THR A 1 18  ? 16.714  30.146  35.245  1.00 35.70  ? 28  THR A N   1 
ATOM   129  C CA  . THR A 1 18  ? 18.129  29.984  34.957  1.00 35.57  ? 28  THR A CA  1 
ATOM   130  C C   . THR A 1 18  ? 18.548  28.573  35.342  1.00 35.55  ? 28  THR A C   1 
ATOM   131  O O   . THR A 1 18  ? 17.778  27.813  35.932  1.00 49.60  ? 28  THR A O   1 
ATOM   132  C CB  . THR A 1 18  ? 18.980  31.028  35.694  1.00 36.89  ? 28  THR A CB  1 
ATOM   133  O OG1 . THR A 1 18  ? 18.789  30.900  37.108  1.00 40.68  ? 28  THR A OG1 1 
ATOM   134  C CG2 . THR A 1 18  ? 18.586  32.431  35.260  1.00 37.06  ? 28  THR A CG2 1 
ATOM   135  N N   . VAL A 1 19  ? 19.783  28.216  34.988  1.00 36.24  ? 29  VAL A N   1 
ATOM   136  C CA  . VAL A 1 19  ? 20.243  26.860  35.262  1.00 37.10  ? 29  VAL A CA  1 
ATOM   137  C C   . VAL A 1 19  ? 20.517  26.676  36.750  1.00 37.11  ? 29  VAL A C   1 
ATOM   138  O O   . VAL A 1 19  ? 20.360  25.572  37.283  1.00 43.12  ? 29  VAL A O   1 
ATOM   139  C CB  . VAL A 1 19  ? 21.475  26.527  34.396  1.00 36.92  ? 29  VAL A CB  1 
ATOM   140  C CG1 . VAL A 1 19  ? 22.669  27.371  34.800  1.00 57.54  ? 29  VAL A CG1 1 
ATOM   141  C CG2 . VAL A 1 19  ? 21.808  25.048  34.481  1.00 36.90  ? 29  VAL A CG2 1 
ATOM   142  N N   . LEU A 1 20  ? 20.900  27.744  37.452  1.00 38.20  ? 30  LEU A N   1 
ATOM   143  C CA  . LEU A 1 20  ? 21.185  27.660  38.877  1.00 39.91  ? 30  LEU A CA  1 
ATOM   144  C C   . LEU A 1 20  ? 20.006  28.047  39.758  1.00 45.86  ? 30  LEU A C   1 
ATOM   145  O O   . LEU A 1 20  ? 20.007  27.703  40.944  1.00 48.05  ? 30  LEU A O   1 
ATOM   146  C CB  . LEU A 1 20  ? 22.379  28.554  39.238  1.00 40.99  ? 30  LEU A CB  1 
ATOM   147  C CG  . LEU A 1 20  ? 23.723  28.239  38.581  1.00 45.54  ? 30  LEU A CG  1 
ATOM   148  C CD1 . LEU A 1 20  ? 24.742  29.301  38.946  1.00 41.99  ? 30  LEU A CD1 1 
ATOM   149  C CD2 . LEU A 1 20  ? 24.212  26.862  38.992  1.00 41.26  ? 30  LEU A CD2 1 
ATOM   150  N N   . GLU A 1 21  ? 19.008  28.744  39.218  1.00 39.94  ? 31  GLU A N   1 
ATOM   151  C CA  . GLU A 1 21  ? 17.938  29.283  40.047  1.00 40.93  ? 31  GLU A CA  1 
ATOM   152  C C   . GLU A 1 21  ? 16.697  29.495  39.194  1.00 45.67  ? 31  GLU A C   1 
ATOM   153  O O   . GLU A 1 21  ? 16.779  30.096  38.118  1.00 42.36  ? 31  GLU A O   1 
ATOM   154  C CB  . GLU A 1 21  ? 18.376  30.602  40.698  1.00 42.25  ? 31  GLU A CB  1 
ATOM   155  C CG  . GLU A 1 21  ? 17.384  31.190  41.692  1.00 43.66  ? 31  GLU A CG  1 
ATOM   156  C CD  . GLU A 1 21  ? 17.783  32.582  42.156  1.00 53.98  ? 31  GLU A CD  1 
ATOM   157  O OE1 . GLU A 1 21  ? 16.914  33.306  42.687  1.00 59.82  ? 31  GLU A OE1 1 
ATOM   158  O OE2 . GLU A 1 21  ? 18.963  32.959  41.984  1.00 50.02  ? 31  GLU A OE2 1 
ATOM   159  N N   . LYS A 1 22  ? 15.561  29.002  39.673  1.00 53.63  ? 32  LYS A N   1 
ATOM   160  C CA  . LYS A 1 22  ? 14.278  29.260  39.039  1.00 55.36  ? 32  LYS A CA  1 
ATOM   161  C C   . LYS A 1 22  ? 13.661  30.542  39.589  1.00 59.30  ? 32  LYS A C   1 
ATOM   162  O O   . LYS A 1 22  ? 13.986  30.996  40.689  1.00 64.77  ? 32  LYS A O   1 
ATOM   163  C CB  . LYS A 1 22  ? 13.313  28.096  39.262  1.00 55.24  ? 32  LYS A CB  1 
ATOM   164  C CG  . LYS A 1 22  ? 13.682  26.804  38.561  1.00 50.36  ? 32  LYS A CG  1 
ATOM   165  C CD  . LYS A 1 22  ? 12.493  25.858  38.566  1.00 52.39  ? 32  LYS A CD  1 
ATOM   166  C CE  . LYS A 1 22  ? 12.780  24.574  37.809  1.00 57.12  ? 32  LYS A CE  1 
ATOM   167  N NZ  . LYS A 1 22  ? 13.584  23.620  38.618  1.00 68.86  ? 32  LYS A NZ  1 
ATOM   168  N N   . ASN A 1 23  ? 12.760  31.126  38.795  1.00 47.99  ? 33  ASN A N   1 
ATOM   169  C CA  . ASN A 1 23  ? 11.934  32.258  39.221  1.00 49.40  ? 33  ASN A CA  1 
ATOM   170  C C   . ASN A 1 23  ? 12.791  33.450  39.648  1.00 43.02  ? 33  ASN A C   1 
ATOM   171  O O   . ASN A 1 23  ? 12.607  34.024  40.723  1.00 47.54  ? 33  ASN A O   1 
ATOM   172  C CB  . ASN A 1 23  ? 10.980  31.840  40.345  1.00 53.32  ? 33  ASN A CB  1 
ATOM   173  C CG  . ASN A 1 23  ? 9.808   32.790  40.506  1.00 65.95  ? 33  ASN A CG  1 
ATOM   174  O OD1 . ASN A 1 23  ? 9.314   33.358  39.532  1.00 63.38  ? 33  ASN A OD1 1 
ATOM   175  N ND2 . ASN A 1 23  ? 9.357   32.968  41.746  1.00 82.10  ? 33  ASN A ND2 1 
ATOM   176  N N   . VAL A 1 24  ? 13.736  33.824  38.792  1.00 41.36  ? 34  VAL A N   1 
ATOM   177  C CA  . VAL A 1 24  ? 14.617  34.958  39.051  1.00 42.28  ? 34  VAL A CA  1 
ATOM   178  C C   . VAL A 1 24  ? 13.940  36.220  38.533  1.00 45.02  ? 34  VAL A C   1 
ATOM   179  O O   . VAL A 1 24  ? 13.666  36.341  37.335  1.00 41.42  ? 34  VAL A O   1 
ATOM   180  C CB  . VAL A 1 24  ? 15.991  34.761  38.393  1.00 41.35  ? 34  VAL A CB  1 
ATOM   181  C CG1 . VAL A 1 24  ? 16.842  36.015  38.555  1.00 42.40  ? 34  VAL A CG1 1 
ATOM   182  C CG2 . VAL A 1 24  ? 16.696  33.552  38.984  1.00 41.33  ? 34  VAL A CG2 1 
ATOM   183  N N   . THR A 1 25  ? 13.674  37.161  39.435  1.00 44.40  ? 35  THR A N   1 
ATOM   184  C CA  . THR A 1 25  ? 13.068  38.432  39.061  1.00 45.10  ? 35  THR A CA  1 
ATOM   185  C C   . THR A 1 25  ? 14.117  39.304  38.381  1.00 44.94  ? 35  THR A C   1 
ATOM   186  O O   . THR A 1 25  ? 15.186  39.553  38.947  1.00 45.68  ? 35  THR A O   1 
ATOM   187  C CB  . THR A 1 25  ? 12.494  39.128  40.292  1.00 47.29  ? 35  THR A CB  1 
ATOM   188  O OG1 . THR A 1 25  ? 11.576  38.247  40.954  1.00 47.60  ? 35  THR A OG1 1 
ATOM   189  C CG2 . THR A 1 25  ? 11.772  40.405  39.898  1.00 48.18  ? 35  THR A CG2 1 
ATOM   190  N N   . VAL A 1 26  ? 13.817  39.763  37.167  1.00 44.12  ? 36  VAL A N   1 
ATOM   191  C CA  . VAL A 1 26  ? 14.783  40.491  36.357  1.00 43.92  ? 36  VAL A CA  1 
ATOM   192  C C   . VAL A 1 26  ? 14.218  41.859  35.994  1.00 45.04  ? 36  VAL A C   1 
ATOM   193  O O   . VAL A 1 26  ? 13.018  42.117  36.107  1.00 45.64  ? 36  VAL A O   1 
ATOM   194  C CB  . VAL A 1 26  ? 15.178  39.707  35.090  1.00 41.97  ? 36  VAL A CB  1 
ATOM   195  C CG1 . VAL A 1 26  ? 15.908  38.426  35.470  1.00 41.14  ? 36  VAL A CG1 1 
ATOM   196  C CG2 . VAL A 1 26  ? 13.950  39.395  34.255  1.00 42.52  ? 36  VAL A CG2 1 
ATOM   197  N N   . THR A 1 27  ? 15.112  42.746  35.549  1.00 45.54  ? 37  THR A N   1 
ATOM   198  C CA  . THR A 1 27  ? 14.715  44.121  35.264  1.00 46.92  ? 37  THR A CA  1 
ATOM   199  C C   . THR A 1 27  ? 14.076  44.248  33.888  1.00 46.02  ? 37  THR A C   1 
ATOM   200  O O   . THR A 1 27  ? 13.098  44.986  33.721  1.00 46.96  ? 37  THR A O   1 
ATOM   201  C CB  . THR A 1 27  ? 15.921  45.056  35.368  1.00 48.09  ? 37  THR A CB  1 
ATOM   202  O OG1 . THR A 1 27  ? 16.819  44.808  34.279  1.00 46.91  ? 37  THR A OG1 1 
ATOM   203  C CG2 . THR A 1 27  ? 16.654  44.839  36.679  1.00 48.97  ? 37  THR A CG2 1 
ATOM   204  N N   . HIS A 1 28  ? 14.616  43.548  32.892  1.00 51.51  ? 38  HIS A N   1 
ATOM   205  C CA  . HIS A 1 28  ? 14.105  43.605  31.532  1.00 43.56  ? 38  HIS A CA  1 
ATOM   206  C C   . HIS A 1 28  ? 14.161  42.214  30.922  1.00 51.97  ? 38  HIS A C   1 
ATOM   207  O O   . HIS A 1 28  ? 15.088  41.448  31.197  1.00 51.47  ? 38  HIS A O   1 
ATOM   208  C CB  . HIS A 1 28  ? 14.907  44.596  30.678  1.00 44.23  ? 38  HIS A CB  1 
ATOM   209  C CG  . HIS A 1 28  ? 15.012  45.967  31.276  1.00 48.78  ? 38  HIS A CG  1 
ATOM   210  N ND1 . HIS A 1 28  ? 15.937  46.290  32.246  1.00 47.39  ? 38  HIS A ND1 1 
ATOM   211  C CD2 . HIS A 1 28  ? 14.305  47.098  31.042  1.00 47.85  ? 38  HIS A CD2 1 
ATOM   212  C CE1 . HIS A 1 28  ? 15.797  47.560  32.582  1.00 49.37  ? 38  HIS A CE1 1 
ATOM   213  N NE2 . HIS A 1 28  ? 14.814  48.073  31.866  1.00 51.07  ? 38  HIS A NE2 1 
ATOM   214  N N   . SER A 1 29  ? 13.165  41.892  30.099  1.00 40.76  ? 39  SER A N   1 
ATOM   215  C CA  . SER A 1 29  ? 13.097  40.584  29.465  1.00 38.97  ? 39  SER A CA  1 
ATOM   216  C C   . SER A 1 29  ? 12.261  40.692  28.199  1.00 38.53  ? 39  SER A C   1 
ATOM   217  O O   . SER A 1 29  ? 11.506  41.648  28.011  1.00 39.95  ? 39  SER A O   1 
ATOM   218  C CB  . SER A 1 29  ? 12.513  39.533  30.412  1.00 38.51  ? 39  SER A CB  1 
ATOM   219  O OG  . SER A 1 29  ? 11.211  39.887  30.824  1.00 47.02  ? 39  SER A OG  1 
ATOM   220  N N   . VAL A 1 30  ? 12.408  39.693  27.331  1.00 37.04  ? 40  VAL A N   1 
ATOM   221  C CA  . VAL A 1 30  ? 11.646  39.605  26.091  1.00 36.55  ? 40  VAL A CA  1 
ATOM   222  C C   . VAL A 1 30  ? 11.037  38.213  25.991  1.00 35.20  ? 40  VAL A C   1 
ATOM   223  O O   . VAL A 1 30  ? 11.736  37.208  26.162  1.00 34.19  ? 40  VAL A O   1 
ATOM   224  C CB  . VAL A 1 30  ? 12.516  39.916  24.856  1.00 36.35  ? 40  VAL A CB  1 
ATOM   225  C CG1 . VAL A 1 30  ? 13.843  39.171  24.923  1.00 35.49  ? 40  VAL A CG1 1 
ATOM   226  C CG2 . VAL A 1 30  ? 11.769  39.573  23.574  1.00 35.73  ? 40  VAL A CG2 1 
ATOM   227  N N   . ASN A 1 31  ? 9.734   38.157  25.738  1.00 42.67  ? 41  ASN A N   1 
ATOM   228  C CA  . ASN A 1 31  ? 9.054   36.886  25.539  1.00 35.92  ? 41  ASN A CA  1 
ATOM   229  C C   . ASN A 1 31  ? 9.254   36.415  24.104  1.00 33.26  ? 41  ASN A C   1 
ATOM   230  O O   . ASN A 1 31  ? 9.035   37.175  23.157  1.00 36.39  ? 41  ASN A O   1 
ATOM   231  C CB  . ASN A 1 31  ? 7.565   37.023  25.855  1.00 38.84  ? 41  ASN A CB  1 
ATOM   232  C CG  . ASN A 1 31  ? 6.764   35.819  25.411  1.00 40.14  ? 41  ASN A CG  1 
ATOM   233  O OD1 . ASN A 1 31  ? 6.797   34.765  26.049  1.00 50.89  ? 41  ASN A OD1 1 
ATOM   234  N ND2 . ASN A 1 31  ? 6.034   35.969  24.312  1.00 40.92  ? 41  ASN A ND2 1 
ATOM   235  N N   . LEU A 1 32  ? 9.679   35.165  23.946  1.00 38.80  ? 42  LEU A N   1 
ATOM   236  C CA  . LEU A 1 32  ? 9.921   34.585  22.632  1.00 31.11  ? 42  LEU A CA  1 
ATOM   237  C C   . LEU A 1 32  ? 8.826   33.623  22.196  1.00 33.56  ? 42  LEU A C   1 
ATOM   238  O O   . LEU A 1 32  ? 8.962   32.991  21.146  1.00 37.73  ? 42  LEU A O   1 
ATOM   239  C CB  . LEU A 1 32  ? 11.270  33.860  22.616  1.00 30.30  ? 42  LEU A CB  1 
ATOM   240  C CG  . LEU A 1 32  ? 12.519  34.718  22.811  1.00 30.90  ? 42  LEU A CG  1 
ATOM   241  C CD1 . LEU A 1 32  ? 13.761  33.851  22.773  1.00 30.19  ? 42  LEU A CD1 1 
ATOM   242  C CD2 . LEU A 1 32  ? 12.599  35.814  21.759  1.00 31.63  ? 42  LEU A CD2 1 
ATOM   243  N N   . LEU A 1 33  ? 7.746   33.505  22.965  1.00 33.06  ? 43  LEU A N   1 
ATOM   244  C CA  . LEU A 1 33  ? 6.720   32.492  22.743  1.00 30.52  ? 43  LEU A CA  1 
ATOM   245  C C   . LEU A 1 33  ? 5.393   33.179  22.445  1.00 31.51  ? 43  LEU A C   1 
ATOM   246  O O   . LEU A 1 33  ? 4.825   33.849  23.312  1.00 32.58  ? 43  LEU A O   1 
ATOM   247  C CB  . LEU A 1 33  ? 6.601   31.572  23.956  1.00 30.34  ? 43  LEU A CB  1 
ATOM   248  C CG  . LEU A 1 33  ? 5.576   30.444  23.875  1.00 30.06  ? 43  LEU A CG  1 
ATOM   249  C CD1 . LEU A 1 33  ? 5.879   29.544  22.697  1.00 28.99  ? 43  LEU A CD1 1 
ATOM   250  C CD2 . LEU A 1 33  ? 5.575   29.661  25.172  1.00 30.38  ? 43  LEU A CD2 1 
ATOM   251  N N   . GLU A 1 34  ? 4.901   33.007  21.224  1.00 31.84  ? 44  GLU A N   1 
ATOM   252  C CA  . GLU A 1 34  ? 3.609   33.553  20.833  1.00 32.36  ? 44  GLU A CA  1 
ATOM   253  C C   . GLU A 1 34  ? 2.508   32.578  21.231  1.00 32.34  ? 44  GLU A C   1 
ATOM   254  O O   . GLU A 1 34  ? 2.541   31.404  20.850  1.00 31.39  ? 44  GLU A O   1 
ATOM   255  C CB  . GLU A 1 34  ? 3.571   33.816  19.331  1.00 32.37  ? 44  GLU A CB  1 
ATOM   256  C CG  . GLU A 1 34  ? 2.265   34.431  18.859  1.00 33.64  ? 44  GLU A CG  1 
ATOM   257  C CD  . GLU A 1 34  ? 2.001   35.779  19.496  1.00 40.96  ? 44  GLU A CD  1 
ATOM   258  O OE1 . GLU A 1 34  ? 2.883   36.660  19.417  1.00 44.68  ? 44  GLU A OE1 1 
ATOM   259  O OE2 . GLU A 1 34  ? 0.918   35.955  20.090  1.00 55.24  ? 44  GLU A OE2 1 
ATOM   260  N N   . ASP A 1 35  ? 1.536   33.059  21.997  1.00 33.56  ? 45  ASP A N   1 
ATOM   261  C CA  . ASP A 1 35  ? 0.415   32.233  22.411  1.00 33.89  ? 45  ASP A CA  1 
ATOM   262  C C   . ASP A 1 35  ? -0.924  32.783  21.955  1.00 35.24  ? 45  ASP A C   1 
ATOM   263  O O   . ASP A 1 35  ? -1.955  32.164  22.232  1.00 44.82  ? 45  ASP A O   1 
ATOM   264  C CB  . ASP A 1 35  ? 0.405   32.063  23.937  1.00 37.21  ? 45  ASP A CB  1 
ATOM   265  C CG  . ASP A 1 35  ? 0.147   33.368  24.674  1.00 49.98  ? 45  ASP A CG  1 
ATOM   266  O OD1 . ASP A 1 35  ? 0.460   34.446  24.124  1.00 53.68  ? 45  ASP A OD1 1 
ATOM   267  O OD2 . ASP A 1 35  ? -0.364  33.314  25.812  1.00 56.30  ? 45  ASP A OD2 1 
ATOM   268  N N   . SER A 1 36  ? -0.942  33.910  21.256  1.00 35.98  ? 46  SER A N   1 
ATOM   269  C CA  . SER A 1 36  ? -2.181  34.575  20.893  1.00 37.56  ? 46  SER A CA  1 
ATOM   270  C C   . SER A 1 36  ? -2.525  34.334  19.429  1.00 37.37  ? 46  SER A C   1 
ATOM   271  O O   . SER A 1 36  ? -1.649  34.197  18.570  1.00 36.77  ? 46  SER A O   1 
ATOM   272  C CB  . SER A 1 36  ? -2.090  36.077  21.167  1.00 39.93  ? 46  SER A CB  1 
ATOM   273  O OG  . SER A 1 36  ? -2.023  36.332  22.558  1.00 70.82  ? 46  SER A OG  1 
ATOM   274  N N   . HIS A 1 37  ? -3.826  34.285  19.159  1.00 38.54  ? 47  HIS A N   1 
ATOM   275  C CA  . HIS A 1 37  ? -4.350  34.167  17.808  1.00 38.81  ? 47  HIS A CA  1 
ATOM   276  C C   . HIS A 1 37  ? -5.720  34.826  17.789  1.00 43.98  ? 47  HIS A C   1 
ATOM   277  O O   . HIS A 1 37  ? -6.337  35.038  18.835  1.00 49.88  ? 47  HIS A O   1 
ATOM   278  C CB  . HIS A 1 37  ? -4.437  32.705  17.361  1.00 37.58  ? 47  HIS A CB  1 
ATOM   279  C CG  . HIS A 1 37  ? -5.391  31.889  18.173  1.00 38.00  ? 47  HIS A CG  1 
ATOM   280  N ND1 . HIS A 1 37  ? -6.718  31.742  17.834  1.00 39.32  ? 47  HIS A ND1 1 
ATOM   281  C CD2 . HIS A 1 37  ? -5.217  31.193  19.321  1.00 37.47  ? 47  HIS A CD2 1 
ATOM   282  C CE1 . HIS A 1 37  ? -7.319  30.982  18.732  1.00 39.58  ? 47  HIS A CE1 1 
ATOM   283  N NE2 . HIS A 1 37  ? -6.430  30.635  19.644  1.00 38.48  ? 47  HIS A NE2 1 
ATOM   284  N N   . ASN A 1 38  ? -6.195  35.148  16.592  1.00 41.68  ? 48  ASN A N   1 
ATOM   285  C CA  . ASN A 1 38  ? -7.452  35.870  16.460  1.00 43.88  ? 48  ASN A CA  1 
ATOM   286  C C   . ASN A 1 38  ? -8.668  34.957  16.386  1.00 44.45  ? 48  ASN A C   1 
ATOM   287  O O   . ASN A 1 38  ? -9.797  35.459  16.351  1.00 46.43  ? 48  ASN A O   1 
ATOM   288  C CB  . ASN A 1 38  ? -7.413  36.794  15.236  1.00 44.86  ? 48  ASN A CB  1 
ATOM   289  C CG  . ASN A 1 38  ? -7.214  36.047  13.934  1.00 43.96  ? 48  ASN A CG  1 
ATOM   290  O OD1 . ASN A 1 38  ? -7.222  34.817  13.896  1.00 51.66  ? 48  ASN A OD1 1 
ATOM   291  N ND2 . ASN A 1 38  ? -7.039  36.794  12.851  1.00 44.78  ? 48  ASN A ND2 1 
ATOM   292  N N   . GLY A 1 39  ? -8.468  33.642  16.363  1.00 42.93  ? 49  GLY A N   1 
ATOM   293  C CA  . GLY A 1 39  ? -9.589  32.717  16.362  1.00 43.54  ? 49  GLY A CA  1 
ATOM   294  C C   . GLY A 1 39  ? -10.434 32.768  15.112  1.00 44.69  ? 49  GLY A C   1 
ATOM   295  O O   . GLY A 1 39  ? -11.614 32.404  15.152  1.00 46.00  ? 49  GLY A O   1 
ATOM   296  N N   . LYS A 1 40  ? -9.864  33.216  13.997  1.00 44.40  ? 50  LYS A N   1 
ATOM   297  C CA  . LYS A 1 40  ? -10.607 33.375  12.758  1.00 45.70  ? 50  LYS A CA  1 
ATOM   298  C C   . LYS A 1 40  ? -9.783  32.845  11.594  1.00 44.34  ? 50  LYS A C   1 
ATOM   299  O O   . LYS A 1 40  ? -8.550  32.834  11.640  1.00 42.78  ? 50  LYS A O   1 
ATOM   300  C CB  . LYS A 1 40  ? -10.970 34.846  12.498  1.00 47.71  ? 50  LYS A CB  1 
ATOM   301  C CG  . LYS A 1 40  ? -11.753 35.507  13.621  1.00 49.33  ? 50  LYS A CG  1 
ATOM   302  C CD  . LYS A 1 40  ? -11.850 37.010  13.412  1.00 54.92  ? 50  LYS A CD  1 
ATOM   303  C CE  . LYS A 1 40  ? -12.470 37.689  14.621  1.00 65.30  ? 50  LYS A CE  1 
ATOM   304  N NZ  . LYS A 1 40  ? -12.445 39.175  14.509  1.00 88.29  ? 50  LYS A NZ  1 
ATOM   305  N N   . LEU A 1 41  ? -10.478 32.406  10.548  1.00 45.11  ? 51  LEU A N   1 
ATOM   306  C CA  . LEU A 1 41  ? -9.840  32.021  9.297   1.00 44.34  ? 51  LEU A CA  1 
ATOM   307  C C   . LEU A 1 41  ? -9.692  33.262  8.428   1.00 45.67  ? 51  LEU A C   1 
ATOM   308  O O   . LEU A 1 41  ? -10.687 33.909  8.085   1.00 58.10  ? 51  LEU A O   1 
ATOM   309  C CB  . LEU A 1 41  ? -10.656 30.948  8.580   1.00 46.43  ? 51  LEU A CB  1 
ATOM   310  C CG  . LEU A 1 41  ? -10.977 29.698  9.398   1.00 55.27  ? 51  LEU A CG  1 
ATOM   311  C CD1 . LEU A 1 41  ? -11.758 28.715  8.549   1.00 54.94  ? 51  LEU A CD1 1 
ATOM   312  C CD2 . LEU A 1 41  ? -9.712  29.056  9.948   1.00 42.44  ? 51  LEU A CD2 1 
ATOM   313  N N   . CYS A 1 42  ? -8.455  33.590  8.075   1.00 44.65  ? 52  CYS A N   1 
ATOM   314  C CA  . CYS A 1 42  ? -8.132  34.824  7.376   1.00 45.90  ? 52  CYS A CA  1 
ATOM   315  C C   . CYS A 1 42  ? -7.544  34.526  6.004   1.00 45.69  ? 52  CYS A C   1 
ATOM   316  O O   . CYS A 1 42  ? -7.229  33.383  5.663   1.00 44.36  ? 52  CYS A O   1 
ATOM   317  C CB  . CYS A 1 42  ? -7.148  35.673  8.188   1.00 45.31  ? 52  CYS A CB  1 
ATOM   318  S SG  . CYS A 1 42  ? -7.749  36.112  9.822   1.00 53.54  ? 52  CYS A SG  1 
ATOM   319  N N   . ARG A 1 43  ? -7.399  35.587  5.216   1.00 47.20  ? 53  ARG A N   1 
ATOM   320  C CA  . ARG A 1 43  ? -6.721  35.484  3.935   1.00 47.25  ? 53  ARG A CA  1 
ATOM   321  C C   . ARG A 1 43  ? -5.220  35.331  4.147   1.00 45.41  ? 53  ARG A C   1 
ATOM   322  O O   . ARG A 1 43  ? -4.649  35.853  5.109   1.00 48.91  ? 53  ARG A O   1 
ATOM   323  C CB  . ARG A 1 43  ? -7.004  36.720  3.084   1.00 49.77  ? 53  ARG A CB  1 
ATOM   324  C CG  . ARG A 1 43  ? -8.472  37.091  2.997   1.00 55.04  ? 53  ARG A CG  1 
ATOM   325  C CD  . ARG A 1 43  ? -8.645  38.486  2.422   1.00 61.09  ? 53  ARG A CD  1 
ATOM   326  N NE  . ARG A 1 43  ? -10.049 38.871  2.327   1.00 72.38  ? 53  ARG A NE  1 
ATOM   327  C CZ  . ARG A 1 43  ? -10.805 38.672  1.252   1.00 85.95  ? 53  ARG A CZ  1 
ATOM   328  N NH1 . ARG A 1 43  ? -10.290 38.090  0.178   1.00 82.45  ? 53  ARG A NH1 1 
ATOM   329  N NH2 . ARG A 1 43  ? -12.074 39.057  1.251   1.00 80.96  ? 53  ARG A NH2 1 
ATOM   330  N N   . LEU A 1 44  ? -4.579  34.602  3.240   1.00 52.75  ? 54  LEU A N   1 
ATOM   331  C CA  . LEU A 1 44  ? -3.133  34.402  3.274   1.00 53.91  ? 54  LEU A CA  1 
ATOM   332  C C   . LEU A 1 44  ? -2.517  35.296  2.204   1.00 65.33  ? 54  LEU A C   1 
ATOM   333  O O   . LEU A 1 44  ? -2.583  34.991  1.010   1.00 61.95  ? 54  LEU A O   1 
ATOM   334  C CB  . LEU A 1 44  ? -2.779  32.936  3.056   1.00 52.24  ? 54  LEU A CB  1 
ATOM   335  C CG  . LEU A 1 44  ? -1.301  32.580  3.220   1.00 63.37  ? 54  LEU A CG  1 
ATOM   336  C CD1 . LEU A 1 44  ? -0.870  32.740  4.671   1.00 63.80  ? 54  LEU A CD1 1 
ATOM   337  C CD2 . LEU A 1 44  ? -1.033  31.169  2.723   1.00 74.56  ? 54  LEU A CD2 1 
ATOM   338  N N   . LYS A 1 45  A -1.919  36.406  2.644   1.00 67.88  ? 54  LYS A N   1 
ATOM   339  C CA  . LYS A 1 45  A -1.308  37.392  1.752   1.00 68.44  ? 54  LYS A CA  1 
ATOM   340  C C   . LYS A 1 45  A -2.323  37.907  0.731   1.00 73.66  ? 54  LYS A C   1 
ATOM   341  O O   . LYS A 1 45  A -2.038  38.025  -0.462  1.00 76.59  ? 54  LYS A O   1 
ATOM   342  C CB  . LYS A 1 45  A -0.070  36.816  1.059   1.00 72.15  ? 54  LYS A CB  1 
ATOM   343  C CG  . LYS A 1 45  A 0.968   36.252  2.019   1.00 76.95  ? 54  LYS A CG  1 
ATOM   344  C CD  . LYS A 1 45  A 2.141   35.641  1.274   1.00 88.53  ? 54  LYS A CD  1 
ATOM   345  C CE  . LYS A 1 45  A 3.088   34.922  2.222   1.00 106.47 ? 54  LYS A CE  1 
ATOM   346  N NZ  . LYS A 1 45  A 3.640   35.827  3.272   1.00 107.40 ? 54  LYS A NZ  1 
ATOM   347  N N   . GLY A 1 46  ? -3.525  38.210  1.217   1.00 81.98  ? 55  GLY A N   1 
ATOM   348  C CA  . GLY A 1 46  ? -4.593  38.736  0.399   1.00 78.16  ? 55  GLY A CA  1 
ATOM   349  C C   . GLY A 1 46  ? -5.487  37.691  -0.239  1.00 81.34  ? 55  GLY A C   1 
ATOM   350  O O   . GLY A 1 46  ? -6.658  37.976  -0.511  1.00 91.33  ? 55  GLY A O   1 
ATOM   351  N N   . ILE A 1 47  ? -4.972  36.489  -0.483  1.00 71.45  ? 56  ILE A N   1 
ATOM   352  C CA  . ILE A 1 47  ? -5.742  35.459  -1.171  1.00 68.95  ? 56  ILE A CA  1 
ATOM   353  C C   . ILE A 1 47  ? -6.603  34.711  -0.161  1.00 63.21  ? 56  ILE A C   1 
ATOM   354  O O   . ILE A 1 47  ? -6.108  34.222  0.861   1.00 64.43  ? 56  ILE A O   1 
ATOM   355  C CB  . ILE A 1 47  ? -4.814  34.504  -1.937  1.00 69.70  ? 56  ILE A CB  1 
ATOM   356  C CG1 . ILE A 1 47  ? -4.063  35.271  -3.028  1.00 78.49  ? 56  ILE A CG1 1 
ATOM   357  C CG2 . ILE A 1 47  ? -5.609  33.366  -2.548  1.00 67.58  ? 56  ILE A CG2 1 
ATOM   358  C CD1 . ILE A 1 47  ? -3.193  34.401  -3.914  1.00 86.58  ? 56  ILE A CD1 1 
ATOM   359  N N   . ALA A 1 48  ? -7.897  34.623  -0.450  1.00 58.15  ? 57  ALA A N   1 
ATOM   360  C CA  . ALA A 1 48  ? -8.863  34.000  0.438   1.00 55.48  ? 57  ALA A CA  1 
ATOM   361  C C   . ALA A 1 48  ? -8.799  32.479  0.332   1.00 57.59  ? 57  ALA A C   1 
ATOM   362  O O   . ALA A 1 48  ? -8.346  31.935  -0.677  1.00 56.12  ? 57  ALA A O   1 
ATOM   363  C CB  . ALA A 1 48  ? -10.268 34.491  0.102   1.00 57.17  ? 57  ALA A CB  1 
ATOM   364  N N   . PRO A 1 49  ? -9.238  31.763  1.374   1.00 50.26  ? 58  PRO A N   1 
ATOM   365  C CA  . PRO A 1 49  ? -9.240  30.297  1.304   1.00 48.78  ? 58  PRO A CA  1 
ATOM   366  C C   . PRO A 1 49  ? -10.512 29.732  0.694   1.00 48.34  ? 58  PRO A C   1 
ATOM   367  O O   . PRO A 1 49  ? -11.375 30.478  0.220   1.00 53.35  ? 58  PRO A O   1 
ATOM   368  C CB  . PRO A 1 49  ? -9.098  29.884  2.771   1.00 45.15  ? 58  PRO A CB  1 
ATOM   369  C CG  . PRO A 1 49  ? -9.783  30.974  3.514   1.00 46.38  ? 58  PRO A CG  1 
ATOM   370  C CD  . PRO A 1 49  ? -9.547  32.248  2.732   1.00 50.12  ? 58  PRO A CD  1 
ATOM   371  N N   . LEU A 1 50  ? -10.634 28.409  0.709   1.00 47.37  ? 59  LEU A N   1 
ATOM   372  C CA  . LEU A 1 50  ? -11.793 27.701  0.175   1.00 48.72  ? 59  LEU A CA  1 
ATOM   373  C C   . LEU A 1 50  ? -12.512 27.020  1.335   1.00 48.22  ? 59  LEU A C   1 
ATOM   374  O O   . LEU A 1 50  ? -12.083 25.965  1.810   1.00 49.65  ? 59  LEU A O   1 
ATOM   375  C CB  . LEU A 1 50  ? -11.368 26.693  -0.888  1.00 49.34  ? 59  LEU A CB  1 
ATOM   376  C CG  . LEU A 1 50  ? -12.444 25.735  -1.405  1.00 49.53  ? 59  LEU A CG  1 
ATOM   377  C CD1 . LEU A 1 50  ? -13.535 26.491  -2.140  1.00 52.20  ? 59  LEU A CD1 1 
ATOM   378  C CD2 . LEU A 1 50  ? -11.835 24.672  -2.299  1.00 48.91  ? 59  LEU A CD2 1 
ATOM   379  N N   . GLN A 1 51  ? -13.602 27.631  1.795   1.00 53.27  ? 60  GLN A N   1 
ATOM   380  C CA  . GLN A 1 51  ? -14.434 27.030  2.830   1.00 54.87  ? 60  GLN A CA  1 
ATOM   381  C C   . GLN A 1 51  ? -15.389 26.029  2.193   1.00 54.74  ? 60  GLN A C   1 
ATOM   382  O O   . GLN A 1 51  ? -16.176 26.388  1.311   1.00 70.90  ? 60  GLN A O   1 
ATOM   383  C CB  . GLN A 1 51  ? -15.209 28.102  3.594   1.00 61.12  ? 60  GLN A CB  1 
ATOM   384  C CG  . GLN A 1 51  ? -14.403 28.812  4.669   1.00 67.18  ? 60  GLN A CG  1 
ATOM   385  C CD  . GLN A 1 51  ? -15.260 29.710  5.541   1.00 87.75  ? 60  GLN A CD  1 
ATOM   386  O OE1 . GLN A 1 51  ? -16.059 30.503  5.042   1.00 99.91  ? 60  GLN A OE1 1 
ATOM   387  N NE2 . GLN A 1 51  ? -15.103 29.584  6.854   1.00 88.54  ? 60  GLN A NE2 1 
ATOM   388  N N   . LEU A 1 52  ? -15.321 24.774  2.638   1.00 51.23  ? 61  LEU A N   1 
ATOM   389  C CA  . LEU A 1 52  ? -16.158 23.729  2.066   1.00 63.02  ? 61  LEU A CA  1 
ATOM   390  C C   . LEU A 1 52  ? -17.550 23.681  2.682   1.00 60.40  ? 61  LEU A C   1 
ATOM   391  O O   . LEU A 1 52  ? -18.442 23.049  2.106   1.00 66.54  ? 61  LEU A O   1 
ATOM   392  C CB  . LEU A 1 52  ? -15.483 22.364  2.226   1.00 49.03  ? 61  LEU A CB  1 
ATOM   393  C CG  . LEU A 1 52  ? -14.140 22.169  1.520   1.00 47.47  ? 61  LEU A CG  1 
ATOM   394  C CD1 . LEU A 1 52  ? -13.660 20.732  1.653   1.00 46.13  ? 61  LEU A CD1 1 
ATOM   395  C CD2 . LEU A 1 52  ? -14.235 22.569  0.060   1.00 48.87  ? 61  LEU A CD2 1 
ATOM   396  N N   . GLY A 1 53  ? -17.758 24.334  3.824   1.00 52.67  ? 62  GLY A N   1 
ATOM   397  C CA  . GLY A 1 53  ? -19.058 24.265  4.472   1.00 54.50  ? 62  GLY A CA  1 
ATOM   398  C C   . GLY A 1 53  ? -19.344 22.861  4.968   1.00 66.70  ? 62  GLY A C   1 
ATOM   399  O O   . GLY A 1 53  ? -18.474 22.180  5.520   1.00 63.78  ? 62  GLY A O   1 
ATOM   400  N N   . ASN A 1 54  ? -20.580 22.410  4.758   1.00 69.46  ? 63  ASN A N   1 
ATOM   401  C CA  . ASN A 1 54  ? -20.988 21.063  5.138   1.00 66.28  ? 63  ASN A CA  1 
ATOM   402  C C   . ASN A 1 54  ? -20.556 20.006  4.130   1.00 56.81  ? 63  ASN A C   1 
ATOM   403  O O   . ASN A 1 54  ? -21.047 18.874  4.194   1.00 60.58  ? 63  ASN A O   1 
ATOM   404  C CB  . ASN A 1 54  ? -22.506 20.999  5.317   1.00 79.70  ? 63  ASN A CB  1 
ATOM   405  C CG  . ASN A 1 54  ? -23.024 22.034  6.290   1.00 98.89  ? 63  ASN A CG  1 
ATOM   406  O OD1 . ASN A 1 54  ? -22.321 22.449  7.212   1.00 105.71 ? 63  ASN A OD1 1 
ATOM   407  N ND2 . ASN A 1 54  ? -24.265 22.460  6.086   1.00 115.92 ? 63  ASN A ND2 1 
ATOM   408  N N   . CYS A 1 55  ? -19.659 20.344  3.211   1.00 54.37  ? 64  CYS A N   1 
ATOM   409  C CA  . CYS A 1 55  ? -19.235 19.453  2.141   1.00 53.93  ? 64  CYS A CA  1 
ATOM   410  C C   . CYS A 1 55  ? -17.839 18.916  2.425   1.00 51.30  ? 64  CYS A C   1 
ATOM   411  O O   . CYS A 1 55  ? -16.970 19.645  2.913   1.00 49.86  ? 64  CYS A O   1 
ATOM   412  C CB  . CYS A 1 55  ? -19.254 20.186  0.797   1.00 58.13  ? 64  CYS A CB  1 
ATOM   413  S SG  . CYS A 1 55  ? -20.895 20.778  0.332   1.00 69.72  ? 64  CYS A SG  1 
ATOM   414  N N   . SER A 1 56  ? -17.631 17.637  2.124   1.00 50.84  ? 65  SER A N   1 
ATOM   415  C CA  . SER A 1 56  ? -16.318 17.030  2.249   1.00 48.62  ? 65  SER A CA  1 
ATOM   416  C C   . SER A 1 56  ? -15.516 17.273  0.975   1.00 52.05  ? 65  SER A C   1 
ATOM   417  O O   . SER A 1 56  ? -15.996 17.873  0.011   1.00 49.75  ? 65  SER A O   1 
ATOM   418  C CB  . SER A 1 56  ? -16.438 15.536  2.542   1.00 50.60  ? 65  SER A CB  1 
ATOM   419  O OG  . SER A 1 56  ? -16.843 14.819  1.392   1.00 53.75  ? 65  SER A OG  1 
ATOM   420  N N   . VAL A 1 57  ? -14.268 16.803  0.970   1.00 48.03  ? 66  VAL A N   1 
ATOM   421  C CA  . VAL A 1 57  ? -13.455 16.886  -0.239  1.00 46.19  ? 66  VAL A CA  1 
ATOM   422  C C   . VAL A 1 57  ? -14.074 16.048  -1.348  1.00 52.48  ? 66  VAL A C   1 
ATOM   423  O O   . VAL A 1 57  ? -14.121 16.465  -2.513  1.00 48.84  ? 66  VAL A O   1 
ATOM   424  C CB  . VAL A 1 57  ? -12.007 16.460  0.063   1.00 45.42  ? 66  VAL A CB  1 
ATOM   425  C CG1 . VAL A 1 57  ? -11.219 16.291  -1.226  1.00 44.09  ? 66  VAL A CG1 1 
ATOM   426  C CG2 . VAL A 1 57  ? -11.335 17.483  0.966   1.00 42.74  ? 66  VAL A CG2 1 
ATOM   427  N N   . ALA A 1 58  ? -14.577 14.860  -1.002  1.00 62.79  ? 67  ALA A N   1 
ATOM   428  C CA  . ALA A 1 58  ? -15.245 14.016  -1.987  1.00 57.60  ? 67  ALA A CA  1 
ATOM   429  C C   . ALA A 1 58  ? -16.511 14.684  -2.511  1.00 57.45  ? 67  ALA A C   1 
ATOM   430  O O   . ALA A 1 58  ? -16.771 14.689  -3.719  1.00 56.35  ? 67  ALA A O   1 
ATOM   431  C CB  . ALA A 1 58  ? -15.567 12.652  -1.375  1.00 60.14  ? 67  ALA A CB  1 
ATOM   432  N N   . GLY A 1 59  ? -17.316 15.250  -1.611  1.00 55.04  ? 68  GLY A N   1 
ATOM   433  C CA  . GLY A 1 59  ? -18.525 15.929  -2.047  1.00 54.84  ? 68  GLY A CA  1 
ATOM   434  C C   . GLY A 1 59  ? -18.233 17.159  -2.886  1.00 55.31  ? 68  GLY A C   1 
ATOM   435  O O   . GLY A 1 59  ? -18.946 17.451  -3.849  1.00 57.38  ? 68  GLY A O   1 
ATOM   436  N N   . TRP A 1 60  ? -17.176 17.893  -2.533  1.00 53.54  ? 69  TRP A N   1 
ATOM   437  C CA  . TRP A 1 60  ? -16.805 19.080  -3.298  1.00 54.01  ? 69  TRP A CA  1 
ATOM   438  C C   . TRP A 1 60  ? -16.298 18.712  -4.686  1.00 55.32  ? 69  TRP A C   1 
ATOM   439  O O   . TRP A 1 60  ? -16.651 19.365  -5.675  1.00 56.25  ? 69  TRP A O   1 
ATOM   440  C CB  . TRP A 1 60  ? -15.753 19.883  -2.531  1.00 53.48  ? 69  TRP A CB  1 
ATOM   441  C CG  . TRP A 1 60  ? -14.894 20.772  -3.388  1.00 51.97  ? 69  TRP A CG  1 
ATOM   442  C CD1 . TRP A 1 60  ? -15.318 21.747  -4.244  1.00 53.86  ? 69  TRP A CD1 1 
ATOM   443  C CD2 . TRP A 1 60  ? -13.461 20.783  -3.447  1.00 53.16  ? 69  TRP A CD2 1 
ATOM   444  N NE1 . TRP A 1 60  ? -14.241 22.351  -4.844  1.00 53.30  ? 69  TRP A NE1 1 
ATOM   445  C CE2 . TRP A 1 60  ? -13.089 21.780  -4.371  1.00 56.57  ? 69  TRP A CE2 1 
ATOM   446  C CE3 . TRP A 1 60  ? -12.458 20.043  -2.813  1.00 51.67  ? 69  TRP A CE3 1 
ATOM   447  C CZ2 . TRP A 1 60  ? -11.758 22.056  -4.676  1.00 49.79  ? 69  TRP A CZ2 1 
ATOM   448  C CZ3 . TRP A 1 60  ? -11.137 20.319  -3.117  1.00 46.70  ? 69  TRP A CZ3 1 
ATOM   449  C CH2 . TRP A 1 60  ? -10.799 21.317  -4.039  1.00 47.64  ? 69  TRP A CH2 1 
ATOM   450  N N   . ILE A 1 61  ? -15.481 17.662  -4.785  1.00 58.63  ? 70  ILE A N   1 
ATOM   451  C CA  . ILE A 1 61  ? -14.853 17.340  -6.060  1.00 55.19  ? 70  ILE A CA  1 
ATOM   452  C C   . ILE A 1 61  ? -15.751 16.496  -6.957  1.00 60.17  ? 70  ILE A C   1 
ATOM   453  O O   . ILE A 1 61  ? -15.543 16.470  -8.177  1.00 57.67  ? 70  ILE A O   1 
ATOM   454  C CB  . ILE A 1 61  ? -13.503 16.641  -5.823  1.00 51.31  ? 70  ILE A CB  1 
ATOM   455  C CG1 . ILE A 1 61  ? -12.531 16.964  -6.956  1.00 51.89  ? 70  ILE A CG1 1 
ATOM   456  C CG2 . ILE A 1 61  ? -13.688 15.138  -5.680  1.00 51.14  ? 70  ILE A CG2 1 
ATOM   457  C CD1 . ILE A 1 61  ? -12.226 18.440  -7.084  1.00 55.72  ? 70  ILE A CD1 1 
ATOM   458  N N   . LEU A 1 62  ? -16.749 15.813  -6.397  1.00 58.25  ? 71  LEU A N   1 
ATOM   459  C CA  . LEU A 1 62  ? -17.676 15.020  -7.195  1.00 58.29  ? 71  LEU A CA  1 
ATOM   460  C C   . LEU A 1 62  ? -18.888 15.811  -7.665  1.00 60.82  ? 71  LEU A C   1 
ATOM   461  O O   . LEU A 1 62  ? -19.642 15.314  -8.508  1.00 62.89  ? 71  LEU A O   1 
ATOM   462  C CB  . LEU A 1 62  ? -18.152 13.797  -6.404  1.00 58.03  ? 71  LEU A CB  1 
ATOM   463  C CG  . LEU A 1 62  ? -17.173 12.631  -6.278  1.00 60.68  ? 71  LEU A CG  1 
ATOM   464  C CD1 . LEU A 1 62  ? -17.757 11.547  -5.389  1.00 56.40  ? 71  LEU A CD1 1 
ATOM   465  C CD2 . LEU A 1 62  ? -16.818 12.075  -7.649  1.00 57.35  ? 71  LEU A CD2 1 
ATOM   466  N N   . GLY A 1 63  ? -19.096 17.016  -7.145  1.00 60.85  ? 72  GLY A N   1 
ATOM   467  C CA  . GLY A 1 63  ? -20.245 17.807  -7.535  1.00 63.40  ? 72  GLY A CA  1 
ATOM   468  C C   . GLY A 1 63  ? -21.506 17.412  -6.798  1.00 64.61  ? 72  GLY A C   1 
ATOM   469  O O   . GLY A 1 63  ? -22.541 17.158  -7.419  1.00 69.49  ? 72  GLY A O   1 
ATOM   470  N N   . ASN A 1 64  ? -21.428 17.344  -5.473  1.00 66.13  ? 73  ASN A N   1 
ATOM   471  C CA  . ASN A 1 64  ? -22.610 17.056  -4.679  1.00 64.35  ? 73  ASN A CA  1 
ATOM   472  C C   . ASN A 1 64  ? -23.625 18.186  -4.845  1.00 66.74  ? 73  ASN A C   1 
ATOM   473  O O   . ASN A 1 64  ? -23.247 19.361  -4.872  1.00 66.49  ? 73  ASN A O   1 
ATOM   474  C CB  . ASN A 1 64  ? -22.236 16.886  -3.206  1.00 62.45  ? 73  ASN A CB  1 
ATOM   475  C CG  . ASN A 1 64  ? -23.383 16.359  -2.365  1.00 63.64  ? 73  ASN A CG  1 
ATOM   476  O OD1 . ASN A 1 64  ? -24.340 17.078  -2.077  1.00 65.42  ? 73  ASN A OD1 1 
ATOM   477  N ND2 . ASN A 1 64  ? -23.286 15.099  -1.955  1.00 62.93  ? 73  ASN A ND2 1 
ATOM   478  N N   . PRO A 1 65  ? -24.914 17.862  -4.979  1.00 71.93  ? 74  PRO A N   1 
ATOM   479  C CA  . PRO A 1 65  ? -25.910 18.913  -5.249  1.00 72.15  ? 74  PRO A CA  1 
ATOM   480  C C   . PRO A 1 65  ? -25.983 19.989  -4.179  1.00 78.71  ? 74  PRO A C   1 
ATOM   481  O O   . PRO A 1 65  ? -26.282 21.146  -4.501  1.00 83.69  ? 74  PRO A O   1 
ATOM   482  C CB  . PRO A 1 65  ? -27.223 18.124  -5.348  1.00 77.95  ? 74  PRO A CB  1 
ATOM   483  C CG  . PRO A 1 65  ? -26.802 16.754  -5.768  1.00 73.46  ? 74  PRO A CG  1 
ATOM   484  C CD  . PRO A 1 65  ? -25.494 16.512  -5.075  1.00 74.34  ? 74  PRO A CD  1 
ATOM   485  N N   . GLU A 1 66  ? -25.717 19.653  -2.920  1.00 93.67  ? 75  GLU A N   1 
ATOM   486  C CA  . GLU A 1 66  ? -25.719 20.639  -1.847  1.00 97.80  ? 75  GLU A CA  1 
ATOM   487  C C   . GLU A 1 66  ? -24.424 21.442  -1.773  1.00 87.91  ? 75  GLU A C   1 
ATOM   488  O O   . GLU A 1 66  ? -24.230 22.191  -0.810  1.00 83.57  ? 75  GLU A O   1 
ATOM   489  C CB  . GLU A 1 66  ? -25.982 19.953  -0.504  1.00 101.07 ? 75  GLU A CB  1 
ATOM   490  C CG  . GLU A 1 66  ? -27.373 19.346  -0.366  1.00 98.94  ? 75  GLU A CG  1 
ATOM   491  C CD  . GLU A 1 66  ? -28.443 20.372  -0.028  1.00 105.17 ? 75  GLU A CD  1 
ATOM   492  O OE1 . GLU A 1 66  ? -28.590 21.363  -0.773  1.00 103.40 ? 75  GLU A OE1 1 
ATOM   493  O OE2 . GLU A 1 66  ? -29.136 20.186  0.994   1.00 110.03 ? 75  GLU A OE2 1 
ATOM   494  N N   . CYS A 1 67  ? -23.540 21.313  -2.765  1.00 75.32  ? 76  CYS A N   1 
ATOM   495  C CA  . CYS A 1 67  ? -22.259 22.010  -2.764  1.00 79.63  ? 76  CYS A CA  1 
ATOM   496  C C   . CYS A 1 67  ? -22.100 22.922  -3.976  1.00 79.04  ? 76  CYS A C   1 
ATOM   497  O O   . CYS A 1 67  ? -20.975 23.305  -4.315  1.00 83.63  ? 76  CYS A O   1 
ATOM   498  C CB  . CYS A 1 67  ? -21.109 21.001  -2.693  1.00 77.27  ? 76  CYS A CB  1 
ATOM   499  S SG  . CYS A 1 67  ? -21.317 19.772  -1.376  1.00 74.74  ? 76  CYS A SG  1 
ATOM   500  N N   . GLU A 1 68  ? -23.208 23.291  -4.627  1.00 86.25  ? 77  GLU A N   1 
ATOM   501  C CA  . GLU A 1 68  ? -23.142 24.158  -5.799  1.00 90.56  ? 77  GLU A CA  1 
ATOM   502  C C   . GLU A 1 68  ? -22.488 25.499  -5.498  1.00 82.71  ? 77  GLU A C   1 
ATOM   503  O O   . GLU A 1 68  ? -21.960 26.138  -6.415  1.00 80.14  ? 77  GLU A O   1 
ATOM   504  C CB  . GLU A 1 68  ? -24.544 24.393  -6.365  1.00 102.63 ? 77  GLU A CB  1 
ATOM   505  C CG  . GLU A 1 68  ? -25.208 23.156  -6.940  1.00 109.35 ? 77  GLU A CG  1 
ATOM   506  C CD  . GLU A 1 68  ? -26.556 23.465  -7.560  1.00 129.24 ? 77  GLU A CD  1 
ATOM   507  O OE1 . GLU A 1 68  ? -26.924 24.658  -7.617  1.00 134.85 ? 77  GLU A OE1 1 
ATOM   508  O OE2 . GLU A 1 68  ? -27.248 22.518  -7.989  1.00 130.88 ? 77  GLU A OE2 1 
ATOM   509  N N   . LEU A 1 69  ? -22.510 25.939  -4.238  1.00 68.33  ? 78  LEU A N   1 
ATOM   510  C CA  . LEU A 1 69  ? -21.873 27.199  -3.876  1.00 72.45  ? 78  LEU A CA  1 
ATOM   511  C C   . LEU A 1 69  ? -20.362 27.152  -4.051  1.00 80.93  ? 78  LEU A C   1 
ATOM   512  O O   . LEU A 1 69  ? -19.723 28.207  -4.121  1.00 87.25  ? 78  LEU A O   1 
ATOM   513  C CB  . LEU A 1 69  ? -22.208 27.559  -2.429  1.00 81.15  ? 78  LEU A CB  1 
ATOM   514  C CG  . LEU A 1 69  ? -23.679 27.480  -2.018  1.00 78.12  ? 78  LEU A CG  1 
ATOM   515  C CD1 . LEU A 1 69  ? -23.839 27.854  -0.551  1.00 80.19  ? 78  LEU A CD1 1 
ATOM   516  C CD2 . LEU A 1 69  ? -24.534 28.371  -2.904  1.00 79.90  ? 78  LEU A CD2 1 
ATOM   517  N N   . LEU A 1 70  ? -19.779 25.958  -4.125  1.00 75.26  ? 79  LEU A N   1 
ATOM   518  C CA  . LEU A 1 70  ? -18.335 25.790  -4.193  1.00 64.28  ? 79  LEU A CA  1 
ATOM   519  C C   . LEU A 1 70  ? -17.812 25.693  -5.619  1.00 61.50  ? 79  LEU A C   1 
ATOM   520  O O   . LEU A 1 70  ? -16.594 25.624  -5.813  1.00 66.57  ? 79  LEU A O   1 
ATOM   521  C CB  . LEU A 1 70  ? -17.918 24.542  -3.408  1.00 58.55  ? 79  LEU A CB  1 
ATOM   522  C CG  . LEU A 1 70  ? -17.708 24.640  -1.894  1.00 61.11  ? 79  LEU A CG  1 
ATOM   523  C CD1 . LEU A 1 70  ? -18.855 25.348  -1.181  1.00 70.29  ? 79  LEU A CD1 1 
ATOM   524  C CD2 . LEU A 1 70  ? -17.519 23.246  -1.327  1.00 58.56  ? 79  LEU A CD2 1 
ATOM   525  N N   . ILE A 1 71  ? -18.695 25.689  -6.618  1.00 72.22  ? 80  ILE A N   1 
ATOM   526  C CA  . ILE A 1 71  ? -18.248 25.542  -7.998  1.00 76.73  ? 80  ILE A CA  1 
ATOM   527  C C   . ILE A 1 71  ? -17.570 26.813  -8.494  1.00 78.15  ? 80  ILE A C   1 
ATOM   528  O O   . ILE A 1 71  ? -16.619 26.751  -9.283  1.00 75.92  ? 80  ILE A O   1 
ATOM   529  C CB  . ILE A 1 71  ? -19.435 25.150  -8.895  1.00 91.00  ? 80  ILE A CB  1 
ATOM   530  C CG1 . ILE A 1 71  ? -20.185 23.962  -8.290  1.00 95.35  ? 80  ILE A CG1 1 
ATOM   531  C CG2 . ILE A 1 71  ? -18.954 24.814  -10.296 1.00 99.41  ? 80  ILE A CG2 1 
ATOM   532  C CD1 . ILE A 1 71  ? -21.419 23.561  -9.062  1.00 101.67 ? 80  ILE A CD1 1 
ATOM   533  N N   . SER A 1 72  ? -18.031 27.982  -8.041  1.00 89.10  ? 81  SER A N   1 
ATOM   534  C CA  . SER A 1 72  ? -17.488 29.242  -8.535  1.00 89.13  ? 81  SER A CA  1 
ATOM   535  C C   . SER A 1 72  ? -16.076 29.516  -8.033  1.00 83.43  ? 81  SER A C   1 
ATOM   536  O O   . SER A 1 72  ? -15.387 30.371  -8.599  1.00 84.55  ? 81  SER A O   1 
ATOM   537  C CB  . SER A 1 72  ? -18.410 30.399  -8.146  1.00 92.82  ? 81  SER A CB  1 
ATOM   538  O OG  . SER A 1 72  ? -18.590 30.464  -6.743  1.00 97.48  ? 81  SER A OG  1 
ATOM   539  N N   . ARG A 1 73  ? -15.629 28.813  -6.997  1.00 69.94  ? 82  ARG A N   1 
ATOM   540  C CA  . ARG A 1 73  ? -14.293 29.023  -6.451  1.00 69.63  ? 82  ARG A CA  1 
ATOM   541  C C   . ARG A 1 73  ? -13.278 28.221  -7.256  1.00 72.88  ? 82  ARG A C   1 
ATOM   542  O O   . ARG A 1 73  ? -13.356 26.989  -7.313  1.00 74.78  ? 82  ARG A O   1 
ATOM   543  C CB  . ARG A 1 73  ? -14.248 28.618  -4.980  1.00 68.52  ? 82  ARG A CB  1 
ATOM   544  C CG  . ARG A 1 73  ? -15.168 29.425  -4.077  1.00 71.77  ? 82  ARG A CG  1 
ATOM   545  C CD  . ARG A 1 73  ? -14.776 30.891  -4.063  1.00 76.52  ? 82  ARG A CD  1 
ATOM   546  N NE  . ARG A 1 73  ? -13.351 31.072  -3.797  1.00 70.36  ? 82  ARG A NE  1 
ATOM   547  C CZ  . ARG A 1 73  ? -12.812 31.083  -2.583  1.00 64.15  ? 82  ARG A CZ  1 
ATOM   548  N NH1 . ARG A 1 73  ? -13.579 30.917  -1.515  1.00 63.20  ? 82  ARG A NH1 1 
ATOM   549  N NH2 . ARG A 1 73  ? -11.506 31.256  -2.436  1.00 66.25  ? 82  ARG A NH2 1 
ATOM   550  N N   . GLU A 1 74  ? -12.324 28.917  -7.877  1.00 74.44  ? 83  GLU A N   1 
ATOM   551  C CA  . GLU A 1 74  ? -11.273 28.263  -8.644  1.00 65.80  ? 83  GLU A CA  1 
ATOM   552  C C   . GLU A 1 74  ? -9.877  28.743  -8.268  1.00 67.13  ? 83  GLU A C   1 
ATOM   553  O O   . GLU A 1 74  ? -8.923  28.444  -8.991  1.00 70.60  ? 83  GLU A O   1 
ATOM   554  C CB  . GLU A 1 74  ? -11.499 28.459  -10.146 1.00 64.97  ? 83  GLU A CB  1 
ATOM   555  C CG  . GLU A 1 74  ? -12.704 27.712  -10.680 1.00 81.97  ? 83  GLU A CG  1 
ATOM   556  C CD  . GLU A 1 74  ? -12.753 27.691  -12.191 1.00 84.96  ? 83  GLU A CD  1 
ATOM   557  O OE1 . GLU A 1 74  ? -12.057 28.514  -12.822 1.00 92.48  ? 83  GLU A OE1 1 
ATOM   558  O OE2 . GLU A 1 74  ? -13.485 26.845  -12.746 1.00 78.66  ? 83  GLU A OE2 1 
ATOM   559  N N   . SER A 1 75  A -9.729  29.475  -7.166  1.00 66.78  ? 83  SER A N   1 
ATOM   560  C CA  . SER A 1 75  A -8.413  29.870  -6.685  1.00 62.79  ? 83  SER A CA  1 
ATOM   561  C C   . SER A 1 75  A -8.510  30.149  -5.193  1.00 64.61  ? 83  SER A C   1 
ATOM   562  O O   . SER A 1 75  A -9.479  30.759  -4.735  1.00 75.10  ? 83  SER A O   1 
ATOM   563  C CB  . SER A 1 75  A -7.881  31.103  -7.425  1.00 63.64  ? 83  SER A CB  1 
ATOM   564  O OG  . SER A 1 75  A -8.478  32.292  -6.943  1.00 68.46  ? 83  SER A OG  1 
ATOM   565  N N   . TRP A 1 76  ? -7.503  29.704  -4.445  1.00 53.17  ? 84  TRP A N   1 
ATOM   566  C CA  . TRP A 1 76  ? -7.522  29.840  -2.996  1.00 55.32  ? 84  TRP A CA  1 
ATOM   567  C C   . TRP A 1 76  ? -6.107  29.702  -2.461  1.00 48.92  ? 84  TRP A C   1 
ATOM   568  O O   . TRP A 1 76  ? -5.222  29.158  -3.126  1.00 50.28  ? 84  TRP A O   1 
ATOM   569  C CB  . TRP A 1 76  ? -8.434  28.794  -2.351  1.00 54.52  ? 84  TRP A CB  1 
ATOM   570  C CG  . TRP A 1 76  ? -8.073  27.403  -2.753  1.00 54.22  ? 84  TRP A CG  1 
ATOM   571  C CD1 . TRP A 1 76  ? -7.162  26.584  -2.152  1.00 51.42  ? 84  TRP A CD1 1 
ATOM   572  C CD2 . TRP A 1 76  ? -8.599  26.670  -3.865  1.00 48.17  ? 84  TRP A CD2 1 
ATOM   573  N NE1 . TRP A 1 76  ? -7.095  25.385  -2.816  1.00 46.17  ? 84  TRP A NE1 1 
ATOM   574  C CE2 . TRP A 1 76  ? -7.969  25.412  -3.871  1.00 46.65  ? 84  TRP A CE2 1 
ATOM   575  C CE3 . TRP A 1 76  ? -9.547  26.954  -4.852  1.00 50.51  ? 84  TRP A CE3 1 
ATOM   576  C CZ2 . TRP A 1 76  ? -8.254  24.439  -4.826  1.00 49.78  ? 84  TRP A CZ2 1 
ATOM   577  C CZ3 . TRP A 1 76  ? -9.829  25.989  -5.799  1.00 51.22  ? 84  TRP A CZ3 1 
ATOM   578  C CH2 . TRP A 1 76  ? -9.185  24.746  -5.779  1.00 49.66  ? 84  TRP A CH2 1 
ATOM   579  N N   . SER A 1 77  ? -5.911  30.195  -1.240  1.00 56.99  ? 85  SER A N   1 
ATOM   580  C CA  . SER A 1 77  ? -4.634  30.053  -0.555  1.00 53.55  ? 85  SER A CA  1 
ATOM   581  C C   . SER A 1 77  ? -4.532  28.752  0.228   1.00 49.77  ? 85  SER A C   1 
ATOM   582  O O   . SER A 1 77  ? -3.424  28.233  0.408   1.00 51.76  ? 85  SER A O   1 
ATOM   583  C CB  . SER A 1 77  ? -4.405  31.240  0.383   1.00 54.94  ? 85  SER A CB  1 
ATOM   584  O OG  . SER A 1 77  ? -5.525  31.446  1.225   1.00 57.37  ? 85  SER A OG  1 
ATOM   585  N N   . TYR A 1 78  ? -5.655  28.215  0.692   1.00 43.06  ? 86  TYR A N   1 
ATOM   586  C CA  . TYR A 1 78  ? -5.691  26.928  1.381   1.00 40.44  ? 86  TYR A CA  1 
ATOM   587  C C   . TYR A 1 78  ? -7.146  26.479  1.457   1.00 41.48  ? 86  TYR A C   1 
ATOM   588  O O   . TYR A 1 78  ? -8.063  27.216  1.083   1.00 43.24  ? 86  TYR A O   1 
ATOM   589  C CB  . TYR A 1 78  ? -5.047  27.009  2.767   1.00 38.83  ? 86  TYR A CB  1 
ATOM   590  C CG  . TYR A 1 78  ? -5.695  28.004  3.705   1.00 43.80  ? 86  TYR A CG  1 
ATOM   591  C CD1 . TYR A 1 78  ? -5.389  29.357  3.638   1.00 40.22  ? 86  TYR A CD1 1 
ATOM   592  C CD2 . TYR A 1 78  ? -6.604  27.587  4.668   1.00 39.40  ? 86  TYR A CD2 1 
ATOM   593  C CE1 . TYR A 1 78  ? -5.978  30.268  4.497   1.00 40.93  ? 86  TYR A CE1 1 
ATOM   594  C CE2 . TYR A 1 78  ? -7.196  28.490  5.530   1.00 40.14  ? 86  TYR A CE2 1 
ATOM   595  C CZ  . TYR A 1 78  ? -6.880  29.828  5.441   1.00 40.89  ? 86  TYR A CZ  1 
ATOM   596  O OH  . TYR A 1 78  ? -7.467  30.730  6.298   1.00 51.29  ? 86  TYR A OH  1 
ATOM   597  N N   . ILE A 1 79  ? -7.351  25.263  1.956   1.00 40.55  ? 87  ILE A N   1 
ATOM   598  C CA  . ILE A 1 79  ? -8.660  24.620  1.963   1.00 41.55  ? 87  ILE A CA  1 
ATOM   599  C C   . ILE A 1 79  ? -9.052  24.306  3.400   1.00 42.00  ? 87  ILE A C   1 
ATOM   600  O O   . ILE A 1 79  ? -8.263  23.725  4.154   1.00 46.27  ? 87  ILE A O   1 
ATOM   601  C CB  . ILE A 1 79  ? -8.663  23.345  1.102   1.00 41.54  ? 87  ILE A CB  1 
ATOM   602  C CG1 . ILE A 1 79  ? -8.326  23.694  -0.348  1.00 43.59  ? 87  ILE A CG1 1 
ATOM   603  C CG2 . ILE A 1 79  ? -10.010 22.643  1.184   1.00 42.65  ? 87  ILE A CG2 1 
ATOM   604  C CD1 . ILE A 1 79  ? -8.222  22.497  -1.263  1.00 49.47  ? 87  ILE A CD1 1 
ATOM   605  N N   . VAL A 1 80  ? -10.272 24.687  3.770   1.00 42.22  ? 88  VAL A N   1 
ATOM   606  C CA  . VAL A 1 80  ? -10.834 24.408  5.085   1.00 42.01  ? 88  VAL A CA  1 
ATOM   607  C C   . VAL A 1 80  ? -11.976 23.420  4.909   1.00 43.07  ? 88  VAL A C   1 
ATOM   608  O O   . VAL A 1 80  ? -12.924 23.680  4.158   1.00 44.87  ? 88  VAL A O   1 
ATOM   609  C CB  . VAL A 1 80  ? -11.325 25.686  5.783   1.00 44.28  ? 88  VAL A CB  1 
ATOM   610  C CG1 . VAL A 1 80  ? -11.904 25.346  7.151   1.00 42.94  ? 88  VAL A CG1 1 
ATOM   611  C CG2 . VAL A 1 80  ? -10.197 26.696  5.907   1.00 42.13  ? 88  VAL A CG2 1 
ATOM   612  N N   . GLU A 1 81  ? -11.884 22.290  5.599   1.00 42.11  ? 89  GLU A N   1 
ATOM   613  C CA  . GLU A 1 81  ? -12.943 21.297  5.656   1.00 43.12  ? 89  GLU A CA  1 
ATOM   614  C C   . GLU A 1 81  ? -13.381 21.141  7.103   1.00 61.18  ? 89  GLU A C   1 
ATOM   615  O O   . GLU A 1 81  ? -12.544 21.110  8.009   1.00 67.25  ? 89  GLU A O   1 
ATOM   616  C CB  . GLU A 1 81  ? -12.467 19.950  5.089   1.00 42.32  ? 89  GLU A CB  1 
ATOM   617  C CG  . GLU A 1 81  ? -13.310 18.756  5.506   1.00 42.98  ? 89  GLU A CG  1 
ATOM   618  C CD  . GLU A 1 81  ? -12.806 17.448  4.925   1.00 43.95  ? 89  GLU A CD  1 
ATOM   619  O OE1 . GLU A 1 81  ? -13.188 17.117  3.784   1.00 43.34  ? 89  GLU A OE1 1 
ATOM   620  O OE2 . GLU A 1 81  ? -12.023 16.753  5.608   1.00 56.57  ? 89  GLU A OE2 1 
ATOM   621  N N   . LYS A 1 82  ? -14.691 21.068  7.325   1.00 65.37  ? 90  LYS A N   1 
ATOM   622  C CA  . LYS A 1 82  ? -15.188 20.880  8.677   1.00 67.89  ? 90  LYS A CA  1 
ATOM   623  C C   . LYS A 1 82  ? -14.707 19.534  9.223   1.00 67.11  ? 90  LYS A C   1 
ATOM   624  O O   . LYS A 1 82  ? -14.503 18.586  8.458   1.00 58.55  ? 90  LYS A O   1 
ATOM   625  C CB  . LYS A 1 82  ? -16.712 20.961  8.705   1.00 80.25  ? 90  LYS A CB  1 
ATOM   626  C CG  . LYS A 1 82  ? -17.246 22.342  8.353   1.00 89.09  ? 90  LYS A CG  1 
ATOM   627  C CD  . LYS A 1 82  ? -16.565 23.425  9.176   1.00 92.35  ? 90  LYS A CD  1 
ATOM   628  C CE  . LYS A 1 82  ? -16.784 24.804  8.575   1.00 89.75  ? 90  LYS A CE  1 
ATOM   629  N NZ  . LYS A 1 82  ? -18.228 25.140  8.468   1.00 84.13  ? 90  LYS A NZ  1 
ATOM   630  N N   . PRO A 1 83  ? -14.496 19.435  10.543  1.00 80.85  ? 91  PRO A N   1 
ATOM   631  C CA  . PRO A 1 83  ? -13.893 18.208  11.103  1.00 85.34  ? 91  PRO A CA  1 
ATOM   632  C C   . PRO A 1 83  ? -14.549 16.920  10.639  1.00 83.67  ? 91  PRO A C   1 
ATOM   633  O O   . PRO A 1 83  ? -13.850 15.968  10.269  1.00 88.75  ? 91  PRO A O   1 
ATOM   634  C CB  . PRO A 1 83  ? -14.037 18.422  12.615  1.00 89.42  ? 91  PRO A CB  1 
ATOM   635  C CG  . PRO A 1 83  ? -14.006 19.894  12.778  1.00 88.14  ? 91  PRO A CG  1 
ATOM   636  C CD  . PRO A 1 83  ? -14.722 20.457  11.579  1.00 84.22  ? 91  PRO A CD  1 
ATOM   637  N N   . ASN A 1 84  ? -15.874 16.865  10.647  1.00 82.40  ? 92  ASN A N   1 
ATOM   638  C CA  . ASN A 1 84  ? -16.603 15.741  10.067  1.00 98.01  ? 92  ASN A CA  1 
ATOM   639  C C   . ASN A 1 84  ? -17.686 16.314  9.167   1.00 99.25  ? 92  ASN A C   1 
ATOM   640  O O   . ASN A 1 84  ? -18.724 16.785  9.660   1.00 105.48 ? 92  ASN A O   1 
ATOM   641  C CB  . ASN A 1 84  ? -17.196 14.837  11.134  1.00 103.47 ? 92  ASN A CB  1 
ATOM   642  C CG  . ASN A 1 84  ? -17.558 13.473  10.585  1.00 121.34 ? 92  ASN A CG  1 
ATOM   643  O OD1 . ASN A 1 84  ? -16.783 12.522  10.691  1.00 122.98 ? 92  ASN A OD1 1 
ATOM   644  N ND2 . ASN A 1 84  ? -18.734 13.374  9.974   1.00 124.17 ? 92  ASN A ND2 1 
ATOM   645  N N   . PRO A 1 85  ? -17.474 16.305  7.854   1.00 83.02  ? 93  PRO A N   1 
ATOM   646  C CA  . PRO A 1 85  ? -18.452 16.911  6.947   1.00 69.89  ? 93  PRO A CA  1 
ATOM   647  C C   . PRO A 1 85  ? -19.719 16.077  6.853   1.00 69.52  ? 93  PRO A C   1 
ATOM   648  O O   . PRO A 1 85  ? -19.756 14.899  7.212   1.00 68.82  ? 93  PRO A O   1 
ATOM   649  C CB  . PRO A 1 85  ? -17.714 16.954  5.605   1.00 67.80  ? 93  PRO A CB  1 
ATOM   650  C CG  . PRO A 1 85  ? -16.259 16.748  5.951   1.00 72.11  ? 93  PRO A CG  1 
ATOM   651  C CD  . PRO A 1 85  ? -16.271 15.853  7.141   1.00 74.80  ? 93  PRO A CD  1 
ATOM   652  N N   . GLU A 1 86  ? -20.773 16.714  6.348   1.00 73.73  ? 94  GLU A N   1 
ATOM   653  C CA  . GLU A 1 86  ? -22.090 16.098  6.261   1.00 82.15  ? 94  GLU A CA  1 
ATOM   654  C C   . GLU A 1 86  ? -22.389 15.542  4.875   1.00 76.51  ? 94  GLU A C   1 
ATOM   655  O O   . GLU A 1 86  ? -22.879 14.418  4.751   1.00 79.69  ? 94  GLU A O   1 
ATOM   656  C CB  . GLU A 1 86  ? -23.166 17.117  6.655   1.00 95.41  ? 94  GLU A CB  1 
ATOM   657  C CG  . GLU A 1 86  ? -22.923 17.788  7.998   1.00 104.66 ? 94  GLU A CG  1 
ATOM   658  C CD  . GLU A 1 86  ? -23.026 16.820  9.161   1.00 114.16 ? 94  GLU A CD  1 
ATOM   659  O OE1 . GLU A 1 86  ? -23.748 15.809  9.034   1.00 115.87 ? 94  GLU A OE1 1 
ATOM   660  O OE2 . GLU A 1 86  ? -22.382 17.069  10.203  1.00 108.22 ? 94  GLU A OE2 1 
ATOM   661  N N   . ASN A 1 87  ? -22.101 16.307  3.829   1.00 60.51  ? 95  ASN A N   1 
ATOM   662  C CA  . ASN A 1 87  ? -22.482 15.968  2.461   1.00 58.78  ? 95  ASN A CA  1 
ATOM   663  C C   . ASN A 1 87  ? -21.240 15.506  1.697   1.00 56.86  ? 95  ASN A C   1 
ATOM   664  O O   . ASN A 1 87  ? -20.495 16.314  1.142   1.00 55.96  ? 95  ASN A O   1 
ATOM   665  C CB  . ASN A 1 87  ? -23.153 17.167  1.792   1.00 61.17  ? 95  ASN A CB  1 
ATOM   666  C CG  . ASN A 1 87  ? -24.470 17.532  2.450   1.00 65.52  ? 95  ASN A CG  1 
ATOM   667  O OD1 . ASN A 1 87  ? -24.691 18.677  2.848   1.00 69.57  ? 95  ASN A OD1 1 
ATOM   668  N ND2 . ASN A 1 87  ? -25.351 16.546  2.572   1.00 70.30  ? 95  ASN A ND2 1 
ATOM   669  N N   . GLY A 1 88  A -21.029 14.192  1.673   1.00 56.40  ? 95  GLY A N   1 
ATOM   670  C CA  . GLY A 1 88  A -19.936 13.604  0.924   1.00 54.92  ? 95  GLY A CA  1 
ATOM   671  C C   . GLY A 1 88  A -20.414 12.771  -0.248  1.00 56.48  ? 95  GLY A C   1 
ATOM   672  O O   . GLY A 1 88  A -20.983 13.307  -1.203  1.00 58.49  ? 95  GLY A O   1 
ATOM   673  N N   . THR A 1 89  ? -20.190 11.460  -0.191  1.00 59.98  ? 96  THR A N   1 
ATOM   674  C CA  . THR A 1 89  ? -20.689 10.544  -1.216  1.00 57.79  ? 96  THR A CA  1 
ATOM   675  C C   . THR A 1 89  ? -22.149 10.239  -0.910  1.00 66.04  ? 96  THR A C   1 
ATOM   676  O O   . THR A 1 89  ? -22.457 9.377   -0.083  1.00 63.87  ? 96  THR A O   1 
ATOM   677  C CB  . THR A 1 89  ? -19.857 9.268   -1.261  1.00 56.67  ? 96  THR A CB  1 
ATOM   678  O OG1 . THR A 1 89  ? -19.800 8.684   0.046   1.00 73.48  ? 96  THR A OG1 1 
ATOM   679  C CG2 . THR A 1 89  ? -18.449 9.573   -1.736  1.00 54.67  ? 96  THR A CG2 1 
ATOM   680  N N   . CYS A 1 90  ? -23.055 10.950  -1.583  1.00 62.20  ? 97  CYS A N   1 
ATOM   681  C CA  . CYS A 1 90  ? -24.475 10.798  -1.288  1.00 64.70  ? 97  CYS A CA  1 
ATOM   682  C C   . CYS A 1 90  ? -24.989 9.427   -1.716  1.00 66.19  ? 97  CYS A C   1 
ATOM   683  O O   . CYS A 1 90  ? -25.840 8.840   -1.038  1.00 76.83  ? 97  CYS A O   1 
ATOM   684  C CB  . CYS A 1 90  ? -25.268 11.922  -1.953  1.00 66.62  ? 97  CYS A CB  1 
ATOM   685  S SG  . CYS A 1 90  ? -24.939 12.139  -3.708  1.00 67.28  ? 97  CYS A SG  1 
ATOM   686  N N   . TYR A 1 91  ? -24.486 8.899   -2.832  1.00 66.10  ? 98  TYR A N   1 
ATOM   687  C CA  . TYR A 1 91  ? -24.760 7.515   -3.197  1.00 67.23  ? 98  TYR A CA  1 
ATOM   688  C C   . TYR A 1 91  ? -23.646 6.636   -2.648  1.00 65.01  ? 98  TYR A C   1 
ATOM   689  O O   . TYR A 1 91  ? -22.475 6.862   -2.984  1.00 63.05  ? 98  TYR A O   1 
ATOM   690  C CB  . TYR A 1 91  ? -24.864 7.354   -4.705  1.00 68.64  ? 98  TYR A CB  1 
ATOM   691  C CG  . TYR A 1 91  ? -25.775 6.222   -5.139  1.00 71.10  ? 98  TYR A CG  1 
ATOM   692  C CD1 . TYR A 1 91  ? -25.335 4.905   -5.133  1.00 78.82  ? 98  TYR A CD1 1 
ATOM   693  C CD2 . TYR A 1 91  ? -27.076 6.473   -5.554  1.00 80.87  ? 98  TYR A CD2 1 
ATOM   694  C CE1 . TYR A 1 91  ? -26.166 3.869   -5.529  1.00 73.11  ? 98  TYR A CE1 1 
ATOM   695  C CE2 . TYR A 1 91  ? -27.913 5.446   -5.951  1.00 76.35  ? 98  TYR A CE2 1 
ATOM   696  C CZ  . TYR A 1 91  ? -27.453 4.145   -5.936  1.00 75.90  ? 98  TYR A CZ  1 
ATOM   697  O OH  . TYR A 1 91  ? -28.284 3.120   -6.331  1.00 94.30  ? 98  TYR A OH  1 
ATOM   698  N N   . PRO A 1 92  ? -23.951 5.643   -1.813  1.00 70.59  ? 99  PRO A N   1 
ATOM   699  C CA  . PRO A 1 92  ? -22.894 4.935   -1.084  1.00 68.51  ? 99  PRO A CA  1 
ATOM   700  C C   . PRO A 1 92  ? -21.947 4.189   -2.011  1.00 67.03  ? 99  PRO A C   1 
ATOM   701  O O   . PRO A 1 92  ? -22.281 3.824   -3.141  1.00 83.05  ? 99  PRO A O   1 
ATOM   702  C CB  . PRO A 1 92  ? -23.671 3.965   -0.184  1.00 74.65  ? 99  PRO A CB  1 
ATOM   703  C CG  . PRO A 1 92  ? -24.992 3.795   -0.860  1.00 85.51  ? 99  PRO A CG  1 
ATOM   704  C CD  . PRO A 1 92  ? -25.291 5.121   -1.497  1.00 79.60  ? 99  PRO A CD  1 
ATOM   705  N N   . GLY A 1 93  ? -20.747 3.966   -1.505  1.00 60.30  ? 100 GLY A N   1 
ATOM   706  C CA  . GLY A 1 93  ? -19.719 3.280   -2.257  1.00 59.48  ? 100 GLY A CA  1 
ATOM   707  C C   . GLY A 1 93  ? -18.367 3.527   -1.631  1.00 56.81  ? 100 GLY A C   1 
ATOM   708  O O   . GLY A 1 93  ? -18.242 4.198   -0.608  1.00 55.61  ? 100 GLY A O   1 
ATOM   709  N N   . HIS A 1 94  ? -17.352 2.961   -2.273  1.00 56.05  ? 101 HIS A N   1 
ATOM   710  C CA  . HIS A 1 94  ? -15.975 3.125   -1.836  1.00 53.69  ? 101 HIS A CA  1 
ATOM   711  C C   . HIS A 1 94  ? -15.254 4.077   -2.776  1.00 58.75  ? 101 HIS A C   1 
ATOM   712  O O   . HIS A 1 94  ? -15.280 3.894   -3.997  1.00 53.95  ? 101 HIS A O   1 
ATOM   713  C CB  . HIS A 1 94  ? -15.246 1.783   -1.782  1.00 53.52  ? 101 HIS A CB  1 
ATOM   714  C CG  . HIS A 1 94  ? -13.792 1.903   -1.445  1.00 63.85  ? 101 HIS A CG  1 
ATOM   715  N ND1 . HIS A 1 94  ? -13.341 2.466   -0.271  1.00 58.71  ? 101 HIS A ND1 1 
ATOM   716  C CD2 . HIS A 1 94  ? -12.685 1.541   -2.136  1.00 61.14  ? 101 HIS A CD2 1 
ATOM   717  C CE1 . HIS A 1 94  ? -12.021 2.440   -0.250  1.00 60.05  ? 101 HIS A CE1 1 
ATOM   718  N NE2 . HIS A 1 94  ? -11.598 1.884   -1.371  1.00 60.51  ? 101 HIS A NE2 1 
ATOM   719  N N   . PHE A 1 95  ? -14.621 5.093   -2.200  1.00 51.07  ? 102 PHE A N   1 
ATOM   720  C CA  . PHE A 1 95  ? -13.814 6.046   -2.952  1.00 50.18  ? 102 PHE A CA  1 
ATOM   721  C C   . PHE A 1 95  ? -12.374 5.544   -2.940  1.00 48.64  ? 102 PHE A C   1 
ATOM   722  O O   . PHE A 1 95  ? -11.712 5.571   -1.898  1.00 51.07  ? 102 PHE A O   1 
ATOM   723  C CB  . PHE A 1 95  ? -13.936 7.438   -2.339  1.00 49.31  ? 102 PHE A CB  1 
ATOM   724  C CG  . PHE A 1 95  ? -13.547 8.552   -3.265  1.00 49.21  ? 102 PHE A CG  1 
ATOM   725  C CD1 . PHE A 1 95  ? -12.356 8.511   -3.969  1.00 59.75  ? 102 PHE A CD1 1 
ATOM   726  C CD2 . PHE A 1 95  ? -14.373 9.648   -3.425  1.00 50.13  ? 102 PHE A CD2 1 
ATOM   727  C CE1 . PHE A 1 95  ? -12.000 9.535   -4.813  1.00 48.50  ? 102 PHE A CE1 1 
ATOM   728  C CE2 . PHE A 1 95  ? -14.023 10.677  -4.270  1.00 50.24  ? 102 PHE A CE2 1 
ATOM   729  C CZ  . PHE A 1 95  ? -12.834 10.619  -4.966  1.00 49.43  ? 102 PHE A CZ  1 
ATOM   730  N N   . ALA A 1 96  ? -11.893 5.086   -4.093  1.00 49.27  ? 103 ALA A N   1 
ATOM   731  C CA  . ALA A 1 96  ? -10.566 4.492   -4.169  1.00 48.19  ? 103 ALA A CA  1 
ATOM   732  C C   . ALA A 1 96  ? -9.490  5.556   -4.003  1.00 52.86  ? 103 ALA A C   1 
ATOM   733  O O   . ALA A 1 96  ? -9.509  6.586   -4.685  1.00 46.62  ? 103 ALA A O   1 
ATOM   734  C CB  . ALA A 1 96  ? -10.387 3.764   -5.498  1.00 49.61  ? 103 ALA A CB  1 
ATOM   735  N N   . ASP A 1 97  ? -8.550  5.300   -3.093  1.00 50.02  ? 104 ASP A N   1 
ATOM   736  C CA  . ASP A 1 97  ? -7.402  6.177   -2.859  1.00 49.52  ? 104 ASP A CA  1 
ATOM   737  C C   . ASP A 1 97  ? -7.851  7.604   -2.551  1.00 45.52  ? 104 ASP A C   1 
ATOM   738  O O   . ASP A 1 97  ? -7.341  8.583   -3.101  1.00 47.44  ? 104 ASP A O   1 
ATOM   739  C CB  . ASP A 1 97  ? -6.439  6.139   -4.046  1.00 43.45  ? 104 ASP A CB  1 
ATOM   740  C CG  . ASP A 1 97  ? -5.920  4.745   -4.325  1.00 43.98  ? 104 ASP A CG  1 
ATOM   741  O OD1 . ASP A 1 97  ? -5.077  4.255   -3.544  1.00 43.61  ? 104 ASP A OD1 1 
ATOM   742  O OD2 . ASP A 1 97  ? -6.351  4.138   -5.327  1.00 45.60  ? 104 ASP A OD2 1 
ATOM   743  N N   . TYR A 1 98  ? -8.828  7.708   -1.651  1.00 42.90  ? 105 TYR A N   1 
ATOM   744  C CA  . TYR A 1 98  ? -9.381  9.006   -1.283  1.00 42.74  ? 105 TYR A CA  1 
ATOM   745  C C   . TYR A 1 98  ? -8.328  9.895   -0.633  1.00 40.95  ? 105 TYR A C   1 
ATOM   746  O O   . TYR A 1 98  ? -8.204  11.078  -0.974  1.00 47.16  ? 105 TYR A O   1 
ATOM   747  C CB  . TYR A 1 98  ? -10.573 8.791   -0.351  1.00 43.39  ? 105 TYR A CB  1 
ATOM   748  C CG  . TYR A 1 98  ? -11.225 10.047  0.166   1.00 43.43  ? 105 TYR A CG  1 
ATOM   749  C CD1 . TYR A 1 98  ? -11.659 11.034  -0.703  1.00 44.33  ? 105 TYR A CD1 1 
ATOM   750  C CD2 . TYR A 1 98  ? -11.432 10.230  1.525   1.00 42.76  ? 105 TYR A CD2 1 
ATOM   751  C CE1 . TYR A 1 98  ? -12.264 12.180  -0.233  1.00 44.55  ? 105 TYR A CE1 1 
ATOM   752  C CE2 . TYR A 1 98  ? -12.037 11.370  2.006   1.00 45.32  ? 105 TYR A CE2 1 
ATOM   753  C CZ  . TYR A 1 98  ? -12.452 12.343  1.121   1.00 52.48  ? 105 TYR A CZ  1 
ATOM   754  O OH  . TYR A 1 98  ? -13.057 13.484  1.594   1.00 51.89  ? 105 TYR A OH  1 
ATOM   755  N N   . GLU A 1 99  ? -7.546  9.331   0.288   1.00 50.78  ? 106 GLU A N   1 
ATOM   756  C CA  . GLU A 1 99  ? -6.531  10.103  0.992   1.00 38.09  ? 106 GLU A CA  1 
ATOM   757  C C   . GLU A 1 99  ? -5.430  10.578  0.054   1.00 37.69  ? 106 GLU A C   1 
ATOM   758  O O   . GLU A 1 99  ? -4.916  11.690  0.222   1.00 36.92  ? 106 GLU A O   1 
ATOM   759  C CB  . GLU A 1 99  ? -5.954  9.264   2.132   1.00 37.13  ? 106 GLU A CB  1 
ATOM   760  C CG  . GLU A 1 99  ? -6.985  8.803   3.160   1.00 37.63  ? 106 GLU A CG  1 
ATOM   761  C CD  . GLU A 1 99  ? -7.828  7.625   2.689   1.00 39.45  ? 106 GLU A CD  1 
ATOM   762  O OE1 . GLU A 1 99  ? -7.308  6.775   1.933   1.00 43.34  ? 106 GLU A OE1 1 
ATOM   763  O OE2 . GLU A 1 99  ? -9.014  7.549   3.074   1.00 41.04  ? 106 GLU A OE2 1 
ATOM   764  N N   . GLU A 1 100 ? -5.057  9.759   -0.931  1.00 38.36  ? 107 GLU A N   1 
ATOM   765  C CA  . GLU A 1 100 ? -4.070  10.186  -1.914  1.00 38.33  ? 107 GLU A CA  1 
ATOM   766  C C   . GLU A 1 100 ? -4.595  11.343  -2.750  1.00 39.20  ? 107 GLU A C   1 
ATOM   767  O O   . GLU A 1 100 ? -3.838  12.254  -3.099  1.00 38.85  ? 107 GLU A O   1 
ATOM   768  C CB  . GLU A 1 100 ? -3.675  9.009   -2.806  1.00 39.17  ? 107 GLU A CB  1 
ATOM   769  C CG  . GLU A 1 100 ? -2.744  8.018   -2.140  1.00 38.33  ? 107 GLU A CG  1 
ATOM   770  C CD  . GLU A 1 100 ? -1.395  8.629   -1.823  1.00 40.49  ? 107 GLU A CD  1 
ATOM   771  O OE1 . GLU A 1 100 ? -0.845  9.331   -2.695  1.00 41.61  ? 107 GLU A OE1 1 
ATOM   772  O OE2 . GLU A 1 100 ? -0.888  8.420   -0.701  1.00 46.38  ? 107 GLU A OE2 1 
ATOM   773  N N   . LEU A 1 101 ? -5.888  11.322  -3.085  1.00 40.57  ? 108 LEU A N   1 
ATOM   774  C CA  . LEU A 1 101 ? -6.473  12.439  -3.818  1.00 41.56  ? 108 LEU A CA  1 
ATOM   775  C C   . LEU A 1 101 ? -6.486  13.700  -2.967  1.00 42.69  ? 108 LEU A C   1 
ATOM   776  O O   . LEU A 1 101 ? -6.223  14.800  -3.468  1.00 45.23  ? 108 LEU A O   1 
ATOM   777  C CB  . LEU A 1 101 ? -7.885  12.083  -4.279  1.00 43.60  ? 108 LEU A CB  1 
ATOM   778  C CG  . LEU A 1 101 ? -8.567  13.161  -5.117  1.00 44.72  ? 108 LEU A CG  1 
ATOM   779  C CD1 . LEU A 1 101 ? -7.716  13.492  -6.330  1.00 45.23  ? 108 LEU A CD1 1 
ATOM   780  C CD2 . LEU A 1 101 ? -9.954  12.718  -5.544  1.00 46.57  ? 108 LEU A CD2 1 
ATOM   781  N N   . ARG A 1 102 ? -6.791  13.559  -1.674  1.00 41.20  ? 109 ARG A N   1 
ATOM   782  C CA  . ARG A 1 102 ? -6.680  14.692  -0.759  1.00 40.10  ? 109 ARG A CA  1 
ATOM   783  C C   . ARG A 1 102 ? -5.266  15.263  -0.766  1.00 39.94  ? 109 ARG A C   1 
ATOM   784  O O   . ARG A 1 102 ? -5.073  16.484  -0.840  1.00 39.08  ? 109 ARG A O   1 
ATOM   785  C CB  . ARG A 1 102 ? -7.080  14.261  0.653   1.00 39.15  ? 109 ARG A CB  1 
ATOM   786  C CG  . ARG A 1 102 ? -8.528  13.827  0.787   1.00 40.40  ? 109 ARG A CG  1 
ATOM   787  C CD  . ARG A 1 102 ? -8.823  13.357  2.204   1.00 56.08  ? 109 ARG A CD  1 
ATOM   788  N NE  . ARG A 1 102 ? -8.461  14.362  3.199   1.00 47.64  ? 109 ARG A NE  1 
ATOM   789  C CZ  . ARG A 1 102 ? -9.316  15.224  3.739   1.00 53.86  ? 109 ARG A CZ  1 
ATOM   790  N NH1 . ARG A 1 102 ? -10.592 15.204  3.383   1.00 58.48  ? 109 ARG A NH1 1 
ATOM   791  N NH2 . ARG A 1 102 ? -8.897  16.103  4.638   1.00 56.19  ? 109 ARG A NH2 1 
ATOM   792  N N   . GLU A 1 103 ? -4.261  14.387  -0.696  1.00 39.76  ? 110 GLU A N   1 
ATOM   793  C CA  . GLU A 1 103 ? -2.879  14.853  -0.696  1.00 39.55  ? 110 GLU A CA  1 
ATOM   794  C C   . GLU A 1 103 ? -2.533  15.559  -2.001  1.00 36.81  ? 110 GLU A C   1 
ATOM   795  O O   . GLU A 1 103 ? -1.811  16.562  -2.001  1.00 38.65  ? 110 GLU A O   1 
ATOM   796  C CB  . GLU A 1 103 ? -1.928  13.682  -0.451  1.00 37.98  ? 110 GLU A CB  1 
ATOM   797  C CG  . GLU A 1 103 ? -0.499  14.092  -0.122  1.00 49.06  ? 110 GLU A CG  1 
ATOM   798  C CD  . GLU A 1 103 ? -0.331  14.552  1.317   1.00 47.69  ? 110 GLU A CD  1 
ATOM   799  O OE1 . GLU A 1 103 ? -1.328  14.564  2.071   1.00 51.85  ? 110 GLU A OE1 1 
ATOM   800  O OE2 . GLU A 1 103 ? 0.806   14.900  1.696   1.00 50.39  ? 110 GLU A OE2 1 
ATOM   801  N N   . GLN A 1 104 ? -3.039  15.046  -3.126  1.00 38.20  ? 111 GLN A N   1 
ATOM   802  C CA  . GLN A 1 104 ? -2.817  15.701  -4.412  1.00 39.42  ? 111 GLN A CA  1 
ATOM   803  C C   . GLN A 1 104 ? -3.428  17.095  -4.430  1.00 40.02  ? 111 GLN A C   1 
ATOM   804  O O   . GLN A 1 104 ? -2.790  18.062  -4.859  1.00 42.26  ? 111 GLN A O   1 
ATOM   805  C CB  . GLN A 1 104 ? -3.405  14.852  -5.538  1.00 41.00  ? 111 GLN A CB  1 
ATOM   806  C CG  . GLN A 1 104 ? -2.722  13.517  -5.742  1.00 49.71  ? 111 GLN A CG  1 
ATOM   807  C CD  . GLN A 1 104 ? -1.412  13.645  -6.483  1.00 40.89  ? 111 GLN A CD  1 
ATOM   808  O OE1 . GLN A 1 104 ? -1.056  14.725  -6.953  1.00 41.28  ? 111 GLN A OE1 1 
ATOM   809  N NE2 . GLN A 1 104 ? -0.687  12.539  -6.598  1.00 44.27  ? 111 GLN A NE2 1 
ATOM   810  N N   . LEU A 1 105 ? -4.675  17.214  -3.970  1.00 40.45  ? 112 LEU A N   1 
ATOM   811  C CA  . LEU A 1 105 ? -5.341  18.509  -3.950  1.00 41.23  ? 112 LEU A CA  1 
ATOM   812  C C   . LEU A 1 105 ? -4.732  19.461  -2.929  1.00 39.95  ? 112 LEU A C   1 
ATOM   813  O O   . LEU A 1 105 ? -4.968  20.670  -3.015  1.00 40.62  ? 112 LEU A O   1 
ATOM   814  C CB  . LEU A 1 105 ? -6.833  18.328  -3.669  1.00 42.17  ? 112 LEU A CB  1 
ATOM   815  C CG  . LEU A 1 105 ? -7.653  17.666  -4.778  1.00 51.93  ? 112 LEU A CG  1 
ATOM   816  C CD1 . LEU A 1 105 ? -9.043  17.300  -4.281  1.00 44.69  ? 112 LEU A CD1 1 
ATOM   817  C CD2 . LEU A 1 105 ? -7.743  18.584  -5.988  1.00 45.60  ? 112 LEU A CD2 1 
ATOM   818  N N   . SER A 1 106 ? -3.957  18.949  -1.970  1.00 38.27  ? 113 SER A N   1 
ATOM   819  C CA  . SER A 1 106 ? -3.314  19.827  -0.997  1.00 45.94  ? 113 SER A CA  1 
ATOM   820  C C   . SER A 1 106 ? -2.256  20.726  -1.623  1.00 40.15  ? 113 SER A C   1 
ATOM   821  O O   . SER A 1 106 ? -1.903  21.747  -1.025  1.00 47.48  ? 113 SER A O   1 
ATOM   822  C CB  . SER A 1 106 ? -2.684  19.006  0.127   1.00 39.31  ? 113 SER A CB  1 
ATOM   823  O OG  . SER A 1 106 ? -3.669  18.556  1.036   1.00 44.75  ? 113 SER A OG  1 
ATOM   824  N N   . SER A 1 107 ? -1.740  20.375  -2.800  1.00 42.52  ? 114 SER A N   1 
ATOM   825  C CA  . SER A 1 107 ? -0.719  21.164  -3.478  1.00 46.22  ? 114 SER A CA  1 
ATOM   826  C C   . SER A 1 107 ? -1.260  21.839  -4.735  1.00 51.05  ? 114 SER A C   1 
ATOM   827  O O   . SER A 1 107 ? -0.512  22.101  -5.679  1.00 55.86  ? 114 SER A O   1 
ATOM   828  C CB  . SER A 1 107 ? 0.489   20.295  -3.821  1.00 51.87  ? 114 SER A CB  1 
ATOM   829  O OG  . SER A 1 107 ? 0.124   19.230  -4.676  1.00 54.04  ? 114 SER A OG  1 
ATOM   830  N N   . VAL A 1 108 ? -2.557  22.126  -4.759  1.00 48.82  ? 115 VAL A N   1 
ATOM   831  C CA  . VAL A 1 108 ? -3.213  22.756  -5.898  1.00 45.82  ? 115 VAL A CA  1 
ATOM   832  C C   . VAL A 1 108 ? -3.555  24.189  -5.520  1.00 46.26  ? 115 VAL A C   1 
ATOM   833  O O   . VAL A 1 108 ? -4.162  24.433  -4.469  1.00 43.35  ? 115 VAL A O   1 
ATOM   834  C CB  . VAL A 1 108 ? -4.471  21.979  -6.322  1.00 45.13  ? 115 VAL A CB  1 
ATOM   835  C CG1 . VAL A 1 108 ? -5.206  22.722  -7.419  1.00 46.84  ? 115 VAL A CG1 1 
ATOM   836  C CG2 . VAL A 1 108 ? -4.098  20.576  -6.777  1.00 46.98  ? 115 VAL A CG2 1 
ATOM   837  N N   . SER A 1 109 ? -3.159  25.136  -6.371  1.00 47.42  ? 116 SER A N   1 
ATOM   838  C CA  . SER A 1 109 ? -3.433  26.547  -6.135  1.00 53.49  ? 116 SER A CA  1 
ATOM   839  C C   . SER A 1 109 ? -4.648  27.053  -6.895  1.00 57.75  ? 116 SER A C   1 
ATOM   840  O O   . SER A 1 109 ? -5.250  28.048  -6.477  1.00 64.54  ? 116 SER A O   1 
ATOM   841  C CB  . SER A 1 109 ? -2.213  27.395  -6.513  1.00 61.27  ? 116 SER A CB  1 
ATOM   842  O OG  . SER A 1 109 ? -1.837  27.164  -7.858  1.00 69.43  ? 116 SER A OG  1 
ATOM   843  N N   . SER A 1 110 ? -5.019  26.389  -7.983  1.00 49.76  ? 117 SER A N   1 
ATOM   844  C CA  . SER A 1 110 ? -6.165  26.779  -8.790  1.00 52.14  ? 117 SER A CA  1 
ATOM   845  C C   . SER A 1 110 ? -6.423  25.680  -9.806  1.00 53.00  ? 117 SER A C   1 
ATOM   846  O O   . SER A 1 110 ? -5.537  24.877  -10.108 1.00 52.15  ? 117 SER A O   1 
ATOM   847  C CB  . SER A 1 110 ? -5.923  28.114  -9.500  1.00 66.38  ? 117 SER A CB  1 
ATOM   848  O OG  . SER A 1 110 ? -4.851  28.011  -10.413 1.00 76.48  ? 117 SER A OG  1 
ATOM   849  N N   . PHE A 1 111 ? -7.642  25.654  -10.339 1.00 56.92  ? 118 PHE A N   1 
ATOM   850  C CA  . PHE A 1 111 ? -7.908  24.763  -11.456 1.00 59.32  ? 118 PHE A CA  1 
ATOM   851  C C   . PHE A 1 111 ? -8.983  25.353  -12.358 1.00 67.57  ? 118 PHE A C   1 
ATOM   852  O O   . PHE A 1 111 ? -9.654  26.332  -12.017 1.00 63.28  ? 118 PHE A O   1 
ATOM   853  C CB  . PHE A 1 111 ? -8.274  23.341  -10.987 1.00 60.94  ? 118 PHE A CB  1 
ATOM   854  C CG  . PHE A 1 111 ? -9.432  23.264  -10.022 1.00 55.28  ? 118 PHE A CG  1 
ATOM   855  C CD1 . PHE A 1 111 ? -10.417 24.236  -9.982  1.00 58.76  ? 118 PHE A CD1 1 
ATOM   856  C CD2 . PHE A 1 111 ? -9.529  22.193  -9.152  1.00 52.83  ? 118 PHE A CD2 1 
ATOM   857  C CE1 . PHE A 1 111 ? -11.466 24.148  -9.104  1.00 57.33  ? 118 PHE A CE1 1 
ATOM   858  C CE2 . PHE A 1 111 ? -10.578 22.100  -8.266  1.00 52.72  ? 118 PHE A CE2 1 
ATOM   859  C CZ  . PHE A 1 111 ? -11.548 23.080  -8.243  1.00 64.03  ? 118 PHE A CZ  1 
ATOM   860  N N   . GLU A 1 112 ? -9.126  24.735  -13.526 1.00 69.16  ? 119 GLU A N   1 
ATOM   861  C CA  . GLU A 1 112 ? -10.103 25.118  -14.532 1.00 75.20  ? 119 GLU A CA  1 
ATOM   862  C C   . GLU A 1 112 ? -11.128 24.002  -14.651 1.00 72.74  ? 119 GLU A C   1 
ATOM   863  O O   . GLU A 1 112 ? -10.779 22.870  -15.005 1.00 63.55  ? 119 GLU A O   1 
ATOM   864  C CB  . GLU A 1 112 ? -9.427  25.359  -15.879 1.00 92.19  ? 119 GLU A CB  1 
ATOM   865  C CG  . GLU A 1 112 ? -8.204  26.248  -15.830 1.00 107.84 ? 119 GLU A CG  1 
ATOM   866  C CD  . GLU A 1 112 ? -7.299  26.042  -17.030 1.00 118.27 ? 119 GLU A CD  1 
ATOM   867  O OE1 . GLU A 1 112 ? -7.811  25.670  -18.107 1.00 116.38 ? 119 GLU A OE1 1 
ATOM   868  O OE2 . GLU A 1 112 ? -6.072  26.235  -16.890 1.00 115.87 ? 119 GLU A OE2 1 
ATOM   869  N N   . ARG A 1 113 ? -12.385 24.319  -14.368 1.00 70.00  ? 120 ARG A N   1 
ATOM   870  C CA  . ARG A 1 113 ? -13.458 23.344  -14.488 1.00 67.58  ? 120 ARG A CA  1 
ATOM   871  C C   . ARG A 1 113 ? -14.075 23.423  -15.879 1.00 77.35  ? 120 ARG A C   1 
ATOM   872  O O   . ARG A 1 113 ? -14.454 24.505  -16.338 1.00 82.99  ? 120 ARG A O   1 
ATOM   873  C CB  . ARG A 1 113 ? -14.523 23.572  -13.417 1.00 65.82  ? 120 ARG A CB  1 
ATOM   874  C CG  . ARG A 1 113 ? -15.699 22.620  -13.499 1.00 66.89  ? 120 ARG A CG  1 
ATOM   875  C CD  . ARG A 1 113 ? -16.646 22.834  -12.335 1.00 66.57  ? 120 ARG A CD  1 
ATOM   876  N NE  . ARG A 1 113 ? -17.879 22.063  -12.464 1.00 70.25  ? 120 ARG A NE  1 
ATOM   877  C CZ  . ARG A 1 113 ? -18.994 22.525  -13.021 1.00 85.54  ? 120 ARG A CZ  1 
ATOM   878  N NH1 . ARG A 1 113 ? -19.032 23.757  -13.510 1.00 83.59  ? 120 ARG A NH1 1 
ATOM   879  N NH2 . ARG A 1 113 ? -20.071 21.754  -13.092 1.00 92.98  ? 120 ARG A NH2 1 
ATOM   880  N N   . PHE A 1 114 ? -14.165 22.276  -16.547 1.00 69.76  ? 121 PHE A N   1 
ATOM   881  C CA  . PHE A 1 114 ? -14.716 22.205  -17.892 1.00 73.34  ? 121 PHE A CA  1 
ATOM   882  C C   . PHE A 1 114 ? -15.366 20.843  -18.073 1.00 76.74  ? 121 PHE A C   1 
ATOM   883  O O   . PHE A 1 114 ? -14.871 19.839  -17.555 1.00 71.05  ? 121 PHE A O   1 
ATOM   884  C CB  . PHE A 1 114 ? -13.632 22.427  -18.954 1.00 76.67  ? 121 PHE A CB  1 
ATOM   885  C CG  . PHE A 1 114 ? -12.581 21.352  -18.984 1.00 76.51  ? 121 PHE A CG  1 
ATOM   886  C CD1 . PHE A 1 114 ? -11.506 21.389  -18.113 1.00 86.02  ? 121 PHE A CD1 1 
ATOM   887  C CD2 . PHE A 1 114 ? -12.667 20.307  -19.890 1.00 74.98  ? 121 PHE A CD2 1 
ATOM   888  C CE1 . PHE A 1 114 ? -10.538 20.401  -18.141 1.00 77.72  ? 121 PHE A CE1 1 
ATOM   889  C CE2 . PHE A 1 114 ? -11.703 19.318  -19.923 1.00 83.02  ? 121 PHE A CE2 1 
ATOM   890  C CZ  . PHE A 1 114 ? -10.637 19.365  -19.047 1.00 73.19  ? 121 PHE A CZ  1 
ATOM   891  N N   . GLU A 1 115 ? -16.477 20.813  -18.806 1.00 75.99  ? 122 GLU A N   1 
ATOM   892  C CA  . GLU A 1 115 ? -17.178 19.558  -19.055 1.00 83.65  ? 122 GLU A CA  1 
ATOM   893  C C   . GLU A 1 115 ? -16.443 18.790  -20.146 1.00 80.99  ? 122 GLU A C   1 
ATOM   894  O O   . GLU A 1 115 ? -16.454 19.184  -21.317 1.00 84.98  ? 122 GLU A O   1 
ATOM   895  C CB  . GLU A 1 115 ? -18.639 19.808  -19.423 1.00 79.64  ? 122 GLU A CB  1 
ATOM   896  C CG  . GLU A 1 115 ? -18.886 20.929  -20.410 1.00 92.05  ? 122 GLU A CG  1 
ATOM   897  C CD  . GLU A 1 115 ? -20.355 21.059  -20.763 1.00 95.41  ? 122 GLU A CD  1 
ATOM   898  O OE1 . GLU A 1 115 ? -21.162 20.253  -20.252 1.00 85.96  ? 122 GLU A OE1 1 
ATOM   899  O OE2 . GLU A 1 115 ? -20.705 21.965  -21.549 1.00 94.70  ? 122 GLU A OE2 1 
ATOM   900  N N   . ILE A 1 116 ? -15.797 17.690  -19.757 1.00 79.57  ? 123 ILE A N   1 
ATOM   901  C CA  . ILE A 1 116 ? -14.989 16.928  -20.701 1.00 84.23  ? 123 ILE A CA  1 
ATOM   902  C C   . ILE A 1 116 ? -15.881 16.132  -21.648 1.00 90.41  ? 123 ILE A C   1 
ATOM   903  O O   . ILE A 1 116 ? -15.570 15.977  -22.835 1.00 88.54  ? 123 ILE A O   1 
ATOM   904  C CB  . ILE A 1 116 ? -13.998 16.028  -19.935 1.00 79.89  ? 123 ILE A CB  1 
ATOM   905  C CG1 . ILE A 1 116 ? -13.111 15.244  -20.902 1.00 96.11  ? 123 ILE A CG1 1 
ATOM   906  C CG2 . ILE A 1 116 ? -14.733 15.090  -18.980 1.00 74.44  ? 123 ILE A CG2 1 
ATOM   907  C CD1 . ILE A 1 116 ? -12.119 14.346  -20.201 1.00 72.09  ? 123 ILE A CD1 1 
ATOM   908  N N   . PHE A 1 117 ? -17.009 15.630  -21.144 1.00 99.99  ? 124 PHE A N   1 
ATOM   909  C CA  . PHE A 1 117 ? -17.988 14.884  -21.935 1.00 90.19  ? 124 PHE A CA  1 
ATOM   910  C C   . PHE A 1 117 ? -19.344 15.527  -21.683 1.00 84.45  ? 124 PHE A C   1 
ATOM   911  O O   . PHE A 1 117 ? -20.040 15.176  -20.719 1.00 82.24  ? 124 PHE A O   1 
ATOM   912  C CB  . PHE A 1 117 ? -17.993 13.401  -21.565 1.00 93.82  ? 124 PHE A CB  1 
ATOM   913  C CG  . PHE A 1 117 ? -16.711 12.687  -21.893 1.00 97.31  ? 124 PHE A CG  1 
ATOM   914  C CD1 . PHE A 1 117 ? -16.026 12.968  -23.063 1.00 109.12 ? 124 PHE A CD1 1 
ATOM   915  C CD2 . PHE A 1 117 ? -16.191 11.737  -21.029 1.00 84.76  ? 124 PHE A CD2 1 
ATOM   916  C CE1 . PHE A 1 117 ? -14.846 12.315  -23.366 1.00 105.24 ? 124 PHE A CE1 1 
ATOM   917  C CE2 . PHE A 1 117 ? -15.011 11.080  -21.328 1.00 81.63  ? 124 PHE A CE2 1 
ATOM   918  C CZ  . PHE A 1 117 ? -14.339 11.370  -22.497 1.00 85.39  ? 124 PHE A CZ  1 
ATOM   919  N N   . PRO A 1 118 ? -19.638 16.542  -22.491 1.00 87.32  ? 125 PRO A N   1 
ATOM   920  C CA  . PRO A 1 118 ? -20.844 17.345  -22.432 1.00 88.68  ? 125 PRO A CA  1 
ATOM   921  C C   . PRO A 1 118 ? -21.982 16.386  -22.419 1.00 88.90  ? 125 PRO A C   1 
ATOM   922  O O   . PRO A 1 118 ? -21.951 15.428  -23.143 1.00 89.90  ? 125 PRO A O   1 
ATOM   923  C CB  . PRO A 1 118 ? -20.781 18.130  -23.717 1.00 90.42  ? 125 PRO A CB  1 
ATOM   924  C CG  . PRO A 1 118 ? -19.336 18.230  -24.018 1.00 89.33  ? 125 PRO A CG  1 
ATOM   925  C CD  . PRO A 1 118 ? -18.809 16.897  -23.645 1.00 87.34  ? 125 PRO A CD  1 
ATOM   926  N N   . LYS A 1 119 A -22.979 16.661  -21.604 1.00 91.82  ? 125 LYS A N   1 
ATOM   927  C CA  . LYS A 1 119 A -24.118 15.781  -21.420 1.00 95.53  ? 125 LYS A CA  1 
ATOM   928  C C   . LYS A 1 119 A -25.103 15.677  -22.570 1.00 104.39 ? 125 LYS A C   1 
ATOM   929  O O   . LYS A 1 119 A -25.922 14.783  -22.617 1.00 99.64  ? 125 LYS A O   1 
ATOM   930  C CB  . LYS A 1 119 A -24.866 16.210  -20.171 1.00 96.85  ? 125 LYS A CB  1 
ATOM   931  C CG  . LYS A 1 119 A -26.351 15.991  -20.239 1.00 99.61  ? 125 LYS A CG  1 
ATOM   932  C CD  . LYS A 1 119 A -27.025 16.504  -18.990 1.00 98.07  ? 125 LYS A CD  1 
ATOM   933  C CE  . LYS A 1 119 A -28.103 15.552  -18.532 1.00 94.29  ? 125 LYS A CE  1 
ATOM   934  N NZ  . LYS A 1 119 A -28.649 15.914  -17.207 1.00 105.32 ? 125 LYS A NZ  1 
ATOM   935  N N   . GLU A 1 120 B -25.024 16.596  -23.503 1.00 113.68 ? 125 GLU A N   1 
ATOM   936  C CA  . GLU A 1 120 B -25.922 16.574  -24.603 1.00 123.87 ? 125 GLU A CA  1 
ATOM   937  C C   . GLU A 1 120 B -25.134 16.764  -25.867 1.00 119.95 ? 125 GLU A C   1 
ATOM   938  O O   . GLU A 1 120 B -25.292 17.799  -26.489 1.00 120.53 ? 125 GLU A O   1 
ATOM   939  C CB  . GLU A 1 120 B -26.925 17.707  -24.430 1.00 133.69 ? 125 GLU A CB  1 
ATOM   940  C CG  . GLU A 1 120 B -28.199 17.305  -23.720 1.00 139.81 ? 125 GLU A CG  1 
ATOM   941  C CD  . GLU A 1 120 B -28.379 17.979  -22.379 1.00 141.97 ? 125 GLU A CD  1 
ATOM   942  O OE1 . GLU A 1 120 B -27.729 19.007  -22.121 1.00 142.07 ? 125 GLU A OE1 1 
ATOM   943  O OE2 . GLU A 1 120 B -29.185 17.474  -21.581 1.00 143.26 ? 125 GLU A OE2 1 
ATOM   944  N N   . SER A 1 121 C -24.301 15.766  -26.203 1.00 111.65 ? 125 SER A N   1 
ATOM   945  C CA  . SER A 1 121 C -23.429 15.694  -27.398 1.00 112.62 ? 125 SER A CA  1 
ATOM   946  C C   . SER A 1 121 C -22.559 14.457  -27.373 1.00 104.67 ? 125 SER A C   1 
ATOM   947  O O   . SER A 1 121 C -21.773 14.254  -28.290 1.00 114.06 ? 125 SER A O   1 
ATOM   948  C CB  . SER A 1 121 C -22.429 16.873  -27.504 1.00 122.63 ? 125 SER A CB  1 
ATOM   949  O OG  . SER A 1 121 C -21.259 16.562  -28.249 1.00 126.12 ? 125 SER A OG  1 
ATOM   950  N N   . SER A 1 122 ? -22.653 13.639  -26.343 1.00 97.02  ? 126 SER A N   1 
ATOM   951  C CA  . SER A 1 122 ? -21.713 12.540  -26.270 1.00 95.52  ? 126 SER A CA  1 
ATOM   952  C C   . SER A 1 122 ? -22.259 11.153  -26.378 1.00 103.72 ? 126 SER A C   1 
ATOM   953  O O   . SER A 1 122 ? -21.643 10.287  -26.968 1.00 112.02 ? 126 SER A O   1 
ATOM   954  C CB  . SER A 1 122 ? -20.905 12.655  -24.982 1.00 92.72  ? 126 SER A CB  1 
ATOM   955  O OG  . SER A 1 122 ? -19.605 13.106  -25.265 1.00 90.37  ? 126 SER A OG  1 
ATOM   956  N N   . TRP A 1 123 ? -23.413 10.942  -25.795 1.00 97.66  ? 127 TRP A N   1 
ATOM   957  C CA  . TRP A 1 123 ? -24.033 9.619   -25.784 1.00 102.29 ? 127 TRP A CA  1 
ATOM   958  C C   . TRP A 1 123 ? -25.400 9.730   -26.445 1.00 101.50 ? 127 TRP A C   1 
ATOM   959  O O   . TRP A 1 123 ? -26.433 9.769   -25.763 1.00 101.92 ? 127 TRP A O   1 
ATOM   960  C CB  . TRP A 1 123 ? -24.150 9.078   -24.358 1.00 104.13 ? 127 TRP A CB  1 
ATOM   961  C CG  . TRP A 1 123 ? -23.096 9.612   -23.440 1.00 95.70  ? 127 TRP A CG  1 
ATOM   962  C CD1 . TRP A 1 123 ? -23.214 10.667  -22.582 1.00 98.63  ? 127 TRP A CD1 1 
ATOM   963  C CD2 . TRP A 1 123 ? -21.756 9.128   -23.299 1.00 88.93  ? 127 TRP A CD2 1 
ATOM   964  N NE1 . TRP A 1 123 ? -22.032 10.865  -21.911 1.00 86.75  ? 127 TRP A NE1 1 
ATOM   965  C CE2 . TRP A 1 123 ? -21.121 9.933   -22.334 1.00 86.07  ? 127 TRP A CE2 1 
ATOM   966  C CE3 . TRP A 1 123 ? -21.033 8.090   -23.894 1.00 89.02  ? 127 TRP A CE3 1 
ATOM   967  C CZ2 . TRP A 1 123 ? -19.797 9.732   -21.950 1.00 83.32  ? 127 TRP A CZ2 1 
ATOM   968  C CZ3 . TRP A 1 123 ? -19.720 7.892   -23.511 1.00 86.33  ? 127 TRP A CZ3 1 
ATOM   969  C CH2 . TRP A 1 123 ? -19.115 8.709   -22.550 1.00 83.52  ? 127 TRP A CH2 1 
ATOM   970  N N   . PRO A 1 124 ? -25.445 9.789   -27.779 1.00 124.08 ? 128 PRO A N   1 
ATOM   971  C CA  . PRO A 1 124 ? -26.745 9.879   -28.459 1.00 125.09 ? 128 PRO A CA  1 
ATOM   972  C C   . PRO A 1 124 ? -27.569 8.611   -28.344 1.00 127.06 ? 128 PRO A C   1 
ATOM   973  O O   . PRO A 1 124 ? -28.794 8.673   -28.501 1.00 138.39 ? 128 PRO A O   1 
ATOM   974  C CB  . PRO A 1 124 ? -26.359 10.164  -29.916 1.00 130.79 ? 128 PRO A CB  1 
ATOM   975  C CG  . PRO A 1 124 ? -25.015 9.530   -30.063 1.00 126.64 ? 128 PRO A CG  1 
ATOM   976  C CD  . PRO A 1 124 ? -24.324 9.715   -28.733 1.00 122.15 ? 128 PRO A CD  1 
ATOM   977  N N   . ASN A 1 125 ? -26.942 7.470   -28.070 1.00 118.60 ? 129 ASN A N   1 
ATOM   978  C CA  . ASN A 1 125 ? -27.640 6.200   -27.944 1.00 118.38 ? 129 ASN A CA  1 
ATOM   979  C C   . ASN A 1 125 ? -27.862 5.789   -26.496 1.00 110.97 ? 129 ASN A C   1 
ATOM   980  O O   . ASN A 1 125 ? -28.329 4.674   -26.248 1.00 112.76 ? 129 ASN A O   1 
ATOM   981  C CB  . ASN A 1 125 ? -26.860 5.102   -28.674 1.00 118.55 ? 129 ASN A CB  1 
ATOM   982  C CG  . ASN A 1 125 ? -26.442 5.513   -30.072 1.00 126.68 ? 129 ASN A CG  1 
ATOM   983  O OD1 . ASN A 1 125 ? -27.234 6.073   -30.831 1.00 127.32 ? 129 ASN A OD1 1 
ATOM   984  N ND2 . ASN A 1 125 ? -25.187 5.245   -30.416 1.00 123.77 ? 129 ASN A ND2 1 
ATOM   985  N N   . HIS A 1 126 ? -27.540 6.655   -25.538 1.00 114.96 ? 130 HIS A N   1 
ATOM   986  C CA  . HIS A 1 126 ? -27.689 6.351   -24.125 1.00 101.04 ? 130 HIS A CA  1 
ATOM   987  C C   . HIS A 1 126 ? -28.506 7.441   -23.447 1.00 101.22 ? 130 HIS A C   1 
ATOM   988  O O   . HIS A 1 126 ? -28.604 8.569   -23.934 1.00 102.32 ? 130 HIS A O   1 
ATOM   989  C CB  . HIS A 1 126 ? -26.330 6.218   -23.427 1.00 97.17  ? 130 HIS A CB  1 
ATOM   990  C CG  . HIS A 1 126 ? -25.394 5.265   -24.101 1.00 96.95  ? 130 HIS A CG  1 
ATOM   991  N ND1 . HIS A 1 126 ? -24.597 5.630   -25.164 1.00 97.62  ? 130 HIS A ND1 1 
ATOM   992  C CD2 . HIS A 1 126 ? -25.123 3.961   -23.858 1.00 96.32  ? 130 HIS A CD2 1 
ATOM   993  C CE1 . HIS A 1 126 ? -23.876 4.592   -25.548 1.00 97.39  ? 130 HIS A CE1 1 
ATOM   994  N NE2 . HIS A 1 126 ? -24.177 3.566   -24.772 1.00 96.59  ? 130 HIS A NE2 1 
ATOM   995  N N   . THR A 1 127 ? -29.094 7.085   -22.309 1.00 100.28 ? 131 THR A N   1 
ATOM   996  C CA  . THR A 1 127 ? -29.828 8.036   -21.488 1.00 100.23 ? 131 THR A CA  1 
ATOM   997  C C   . THR A 1 127 ? -28.893 8.653   -20.457 1.00 98.47  ? 131 THR A C   1 
ATOM   998  O O   . THR A 1 127 ? -28.099 7.954   -19.822 1.00 93.85  ? 131 THR A O   1 
ATOM   999  C CB  . THR A 1 127 ? -31.004 7.354   -20.788 1.00 101.52 ? 131 THR A CB  1 
ATOM   1000 O OG1 . THR A 1 127 ? -31.872 6.774   -21.769 1.00 111.47 ? 131 THR A OG1 1 
ATOM   1001 C CG2 . THR A 1 127 ? -31.794 8.358   -19.961 1.00 101.77 ? 131 THR A CG2 1 
ATOM   1002 N N   . THR A 1 128 ? -28.989 9.972   -20.298 1.00 96.43  ? 132 THR A N   1 
ATOM   1003 C CA  . THR A 1 128 ? -28.116 10.724  -19.407 1.00 93.19  ? 132 THR A CA  1 
ATOM   1004 C C   . THR A 1 128 ? -28.908 11.449  -18.323 1.00 93.06  ? 132 THR A C   1 
ATOM   1005 O O   . THR A 1 128 ? -28.506 12.520  -17.864 1.00 91.64  ? 132 THR A O   1 
ATOM   1006 C CB  . THR A 1 128 ? -27.271 11.721  -20.200 1.00 93.01  ? 132 THR A CB  1 
ATOM   1007 O OG1 . THR A 1 128 ? -28.118 12.741  -20.742 1.00 95.91  ? 132 THR A OG1 1 
ATOM   1008 C CG2 . THR A 1 128 ? -26.545 11.020  -21.341 1.00 93.59  ? 132 THR A CG2 1 
ATOM   1009 N N   . THR A 1 129 ? -30.036 10.877  -17.898 1.00 96.04  ? 133 THR A N   1 
ATOM   1010 C CA  . THR A 1 129 ? -30.931 11.540  -16.957 1.00 97.98  ? 133 THR A CA  1 
ATOM   1011 C C   . THR A 1 129 ? -31.112 10.770  -15.654 1.00 96.91  ? 133 THR A C   1 
ATOM   1012 O O   . THR A 1 129 ? -32.012 11.105  -14.874 1.00 110.27 ? 133 THR A O   1 
ATOM   1013 C CB  . THR A 1 129 ? -32.301 11.777  -17.601 1.00 102.68 ? 133 THR A CB  1 
ATOM   1014 O OG1 . THR A 1 129 ? -32.941 10.518  -17.838 1.00 103.83 ? 133 THR A OG1 1 
ATOM   1015 C CG2 . THR A 1 129 ? -32.150 12.521  -18.920 1.00 103.01 ? 133 THR A CG2 1 
ATOM   1016 N N   . GLY A 1 130 ? -30.294 9.753   -15.397 1.00 91.38  ? 134 GLY A N   1 
ATOM   1017 C CA  . GLY A 1 130 ? -30.421 8.981   -14.176 1.00 89.98  ? 134 GLY A CA  1 
ATOM   1018 C C   . GLY A 1 130 ? -30.207 9.803   -12.922 1.00 87.83  ? 134 GLY A C   1 
ATOM   1019 O O   . GLY A 1 130 ? -29.214 10.527  -12.808 1.00 85.55  ? 134 GLY A O   1 
ATOM   1020 N N   . VAL A 1 131 ? -31.141 9.709   -11.975 1.00 88.70  ? 135 VAL A N   1 
ATOM   1021 C CA  . VAL A 1 131 ? -31.050 10.404  -10.696 1.00 86.96  ? 135 VAL A CA  1 
ATOM   1022 C C   . VAL A 1 131 ? -31.420 9.428   -9.588  1.00 86.60  ? 135 VAL A C   1 
ATOM   1023 O O   . VAL A 1 131 ? -31.926 8.332   -9.834  1.00 92.28  ? 135 VAL A O   1 
ATOM   1024 C CB  . VAL A 1 131 ? -31.957 11.652  -10.633 1.00 88.98  ? 135 VAL A CB  1 
ATOM   1025 C CG1 . VAL A 1 131 ? -31.448 12.732  -11.574 1.00 89.05  ? 135 VAL A CG1 1 
ATOM   1026 C CG2 . VAL A 1 131 ? -33.394 11.282  -10.963 1.00 92.71  ? 135 VAL A CG2 1 
ATOM   1027 N N   . SER A 1 132 ? -31.162 9.844   -8.351  1.00 84.70  ? 136 SER A N   1 
ATOM   1028 C CA  . SER A 1 132 ? -31.443 9.023   -7.185  1.00 84.29  ? 136 SER A CA  1 
ATOM   1029 C C   . SER A 1 132 ? -32.035 9.888   -6.084  1.00 93.25  ? 136 SER A C   1 
ATOM   1030 O O   . SER A 1 132 ? -31.745 11.084  -5.986  1.00 88.82  ? 136 SER A O   1 
ATOM   1031 C CB  . SER A 1 132 ? -30.182 8.317   -6.671  1.00 81.08  ? 136 SER A CB  1 
ATOM   1032 O OG  . SER A 1 132 ? -30.475 7.511   -5.544  1.00 81.80  ? 136 SER A OG  1 
ATOM   1033 N N   . ALA A 1 133 ? -32.881 9.265   -5.261  1.00 108.78 ? 137 ALA A N   1 
ATOM   1034 C CA  . ALA A 1 133 ? -33.414 9.939   -4.085  1.00 110.12 ? 137 ALA A CA  1 
ATOM   1035 C C   . ALA A 1 133 ? -32.379 10.050  -2.975  1.00 107.00 ? 137 ALA A C   1 
ATOM   1036 O O   . ALA A 1 133 ? -32.514 10.911  -2.099  1.00 103.47 ? 137 ALA A O   1 
ATOM   1037 C CB  . ALA A 1 133 ? -34.656 9.210   -3.573  1.00 109.12 ? 137 ALA A CB  1 
ATOM   1038 N N   . SER A 1 134 ? -31.353 9.196   -2.992  1.00 99.96  ? 138 SER A N   1 
ATOM   1039 C CA  . SER A 1 134 ? -30.268 9.307   -2.026  1.00 96.40  ? 138 SER A CA  1 
ATOM   1040 C C   . SER A 1 134 ? -29.410 10.542  -2.263  1.00 91.28  ? 138 SER A C   1 
ATOM   1041 O O   . SER A 1 134 ? -28.760 11.022  -1.329  1.00 86.28  ? 138 SER A O   1 
ATOM   1042 C CB  . SER A 1 134 ? -29.399 8.050   -2.069  1.00 95.14  ? 138 SER A CB  1 
ATOM   1043 O OG  . SER A 1 134 ? -29.018 7.745   -3.398  1.00 95.34  ? 138 SER A OG  1 
ATOM   1044 N N   . CYS A 1 135 ? -29.388 11.063  -3.489  1.00 85.13  ? 139 CYS A N   1 
ATOM   1045 C CA  . CYS A 1 135 ? -28.692 12.309  -3.779  1.00 75.07  ? 139 CYS A CA  1 
ATOM   1046 C C   . CYS A 1 135 ? -29.703 13.398  -4.106  1.00 83.95  ? 139 CYS A C   1 
ATOM   1047 O O   . CYS A 1 135 ? -29.638 14.013  -5.175  1.00 83.23  ? 139 CYS A O   1 
ATOM   1048 C CB  . CYS A 1 135 ? -27.710 12.126  -4.938  1.00 74.51  ? 139 CYS A CB  1 
ATOM   1049 S SG  . CYS A 1 135 ? -26.349 10.987  -4.602  1.00 86.60  ? 139 CYS A SG  1 
ATOM   1050 N N   . SER A 1 136 ? -30.636 13.643  -3.192  1.00 111.68 ? 140 SER A N   1 
ATOM   1051 C CA  . SER A 1 136 ? -31.736 14.558  -3.448  1.00 126.60 ? 140 SER A CA  1 
ATOM   1052 C C   . SER A 1 136 ? -31.291 16.011  -3.308  1.00 120.49 ? 140 SER A C   1 
ATOM   1053 O O   . SER A 1 136 ? -30.301 16.331  -2.645  1.00 116.59 ? 140 SER A O   1 
ATOM   1054 C CB  . SER A 1 136 ? -32.900 14.280  -2.497  1.00 131.59 ? 140 SER A CB  1 
ATOM   1055 O OG  . SER A 1 136 ? -33.406 12.969  -2.675  1.00 135.21 ? 140 SER A OG  1 
ATOM   1056 N N   . HIS A 1 137 ? -32.053 16.896  -3.948  1.00 123.04 ? 141 HIS A N   1 
ATOM   1057 C CA  . HIS A 1 137 ? -31.826 18.333  -3.868  1.00 121.28 ? 141 HIS A CA  1 
ATOM   1058 C C   . HIS A 1 137 ? -33.170 19.035  -3.986  1.00 127.63 ? 141 HIS A C   1 
ATOM   1059 O O   . HIS A 1 137 ? -33.918 18.781  -4.936  1.00 139.34 ? 141 HIS A O   1 
ATOM   1060 C CB  . HIS A 1 137 ? -30.872 18.809  -4.969  1.00 115.41 ? 141 HIS A CB  1 
ATOM   1061 C CG  . HIS A 1 137 ? -30.575 20.275  -4.919  1.00 119.04 ? 141 HIS A CG  1 
ATOM   1062 N ND1 . HIS A 1 137 ? -30.092 20.898  -3.788  1.00 108.50 ? 141 HIS A ND1 1 
ATOM   1063 C CD2 . HIS A 1 137 ? -30.692 21.241  -5.860  1.00 125.84 ? 141 HIS A CD2 1 
ATOM   1064 C CE1 . HIS A 1 137 ? -29.925 22.185  -4.035  1.00 109.17 ? 141 HIS A CE1 1 
ATOM   1065 N NE2 . HIS A 1 137 ? -30.281 22.420  -5.285  1.00 121.28 ? 141 HIS A NE2 1 
ATOM   1066 N N   . ASN A 1 138 ? -33.469 19.908  -3.021  1.00 121.01 ? 142 ASN A N   1 
ATOM   1067 C CA  . ASN A 1 138 ? -34.763 20.591  -2.942  1.00 129.83 ? 142 ASN A CA  1 
ATOM   1068 C C   . ASN A 1 138 ? -35.913 19.588  -2.864  1.00 131.10 ? 142 ASN A C   1 
ATOM   1069 O O   . ASN A 1 138 ? -36.979 19.790  -3.449  1.00 129.18 ? 142 ASN A O   1 
ATOM   1070 C CB  . ASN A 1 138 ? -34.958 21.558  -4.113  1.00 134.24 ? 142 ASN A CB  1 
ATOM   1071 C CG  . ASN A 1 138 ? -34.076 22.786  -4.008  1.00 138.07 ? 142 ASN A CG  1 
ATOM   1072 O OD1 . ASN A 1 138 ? -33.752 23.238  -2.910  1.00 138.77 ? 142 ASN A OD1 1 
ATOM   1073 N ND2 . ASN A 1 138 ? -33.684 23.334  -5.153  1.00 136.61 ? 142 ASN A ND2 1 
ATOM   1074 N N   . GLY A 1 139 ? -35.692 18.494  -2.134  1.00 137.28 ? 143 GLY A N   1 
ATOM   1075 C CA  . GLY A 1 139 ? -36.707 17.484  -1.920  1.00 139.21 ? 143 GLY A CA  1 
ATOM   1076 C C   . GLY A 1 139 ? -36.881 16.482  -3.039  1.00 137.70 ? 143 GLY A C   1 
ATOM   1077 O O   . GLY A 1 139 ? -37.540 15.455  -2.828  1.00 140.55 ? 143 GLY A O   1 
ATOM   1078 N N   . GLU A 1 140 ? -36.314 16.733  -4.214  1.00 134.09 ? 144 GLU A N   1 
ATOM   1079 C CA  . GLU A 1 140 ? -36.481 15.873  -5.375  1.00 137.79 ? 144 GLU A CA  1 
ATOM   1080 C C   . GLU A 1 140 ? -35.185 15.129  -5.670  1.00 123.25 ? 144 GLU A C   1 
ATOM   1081 O O   . GLU A 1 140 ? -34.092 15.601  -5.347  1.00 122.69 ? 144 GLU A O   1 
ATOM   1082 C CB  . GLU A 1 140 ? -36.906 16.692  -6.598  1.00 151.69 ? 144 GLU A CB  1 
ATOM   1083 C CG  . GLU A 1 140 ? -38.141 17.551  -6.361  1.00 163.89 ? 144 GLU A CG  1 
ATOM   1084 C CD  . GLU A 1 140 ? -38.287 18.668  -7.378  1.00 169.17 ? 144 GLU A CD  1 
ATOM   1085 O OE1 . GLU A 1 140 ? -37.448 18.751  -8.300  1.00 167.89 ? 144 GLU A OE1 1 
ATOM   1086 O OE2 . GLU A 1 140 ? -39.238 19.469  -7.250  1.00 169.53 ? 144 GLU A OE2 1 
ATOM   1087 N N   . SER A 1 141 ? -35.322 13.956  -6.288  1.00 109.77 ? 145 SER A N   1 
ATOM   1088 C CA  . SER A 1 141 ? -34.164 13.139  -6.626  1.00 94.22  ? 145 SER A CA  1 
ATOM   1089 C C   . SER A 1 141 ? -33.225 13.896  -7.558  1.00 92.79  ? 145 SER A C   1 
ATOM   1090 O O   . SER A 1 141 ? -33.652 14.709  -8.382  1.00 90.99  ? 145 SER A O   1 
ATOM   1091 C CB  . SER A 1 141 ? -34.611 11.831  -7.284  1.00 97.99  ? 145 SER A CB  1 
ATOM   1092 O OG  . SER A 1 141 ? -35.429 11.071  -6.412  1.00 106.58 ? 145 SER A OG  1 
ATOM   1093 N N   . SER A 1 142 ? -31.931 13.626  -7.419  1.00 102.61 ? 146 SER A N   1 
ATOM   1094 C CA  . SER A 1 142 ? -30.922 14.309  -8.222  1.00 100.53 ? 146 SER A CA  1 
ATOM   1095 C C   . SER A 1 142 ? -29.662 13.449  -8.252  1.00 100.15 ? 146 SER A C   1 
ATOM   1096 O O   . SER A 1 142 ? -29.681 12.277  -7.860  1.00 109.34 ? 146 SER A O   1 
ATOM   1097 C CB  . SER A 1 142 ? -30.644 15.714  -7.678  1.00 99.41  ? 146 SER A CB  1 
ATOM   1098 O OG  . SER A 1 142 ? -29.759 16.418  -8.530  1.00 95.53  ? 146 SER A OG  1 
ATOM   1099 N N   . PHE A 1 143 ? -28.561 14.038  -8.714  1.00 84.02  ? 147 PHE A N   1 
ATOM   1100 C CA  . PHE A 1 143 ? -27.323 13.299  -8.917  1.00 78.06  ? 147 PHE A CA  1 
ATOM   1101 C C   . PHE A 1 143 ? -26.166 14.289  -8.952  1.00 79.40  ? 147 PHE A C   1 
ATOM   1102 O O   . PHE A 1 143 ? -26.366 15.506  -8.953  1.00 82.52  ? 147 PHE A O   1 
ATOM   1103 C CB  . PHE A 1 143 ? -27.391 12.468  -10.204 1.00 84.19  ? 147 PHE A CB  1 
ATOM   1104 C CG  . PHE A 1 143 ? -26.309 11.436  -10.323 1.00 76.54  ? 147 PHE A CG  1 
ATOM   1105 C CD1 . PHE A 1 143 ? -26.287 10.338  -9.481  1.00 75.55  ? 147 PHE A CD1 1 
ATOM   1106 C CD2 . PHE A 1 143 ? -25.320 11.557  -11.285 1.00 75.80  ? 147 PHE A CD2 1 
ATOM   1107 C CE1 . PHE A 1 143 ? -25.294 9.385   -9.589  1.00 75.18  ? 147 PHE A CE1 1 
ATOM   1108 C CE2 . PHE A 1 143 ? -24.326 10.606  -11.399 1.00 74.08  ? 147 PHE A CE2 1 
ATOM   1109 C CZ  . PHE A 1 143 ? -24.313 9.518   -10.551 1.00 73.09  ? 147 PHE A CZ  1 
ATOM   1110 N N   . TYR A 1 144 ? -24.949 13.747  -8.976  1.00 77.37  ? 148 TYR A N   1 
ATOM   1111 C CA  . TYR A 1 144 ? -23.751 14.576  -9.008  1.00 72.70  ? 148 TYR A CA  1 
ATOM   1112 C C   . TYR A 1 144 ? -23.718 15.431  -10.269 1.00 75.36  ? 148 TYR A C   1 
ATOM   1113 O O   . TYR A 1 144 ? -24.159 15.015  -11.344 1.00 90.30  ? 148 TYR A O   1 
ATOM   1114 C CB  . TYR A 1 144 ? -22.492 13.707  -8.945  1.00 67.96  ? 148 TYR A CB  1 
ATOM   1115 C CG  . TYR A 1 144 ? -22.415 12.804  -7.735  1.00 66.40  ? 148 TYR A CG  1 
ATOM   1116 C CD1 . TYR A 1 144 ? -21.991 13.290  -6.506  1.00 64.40  ? 148 TYR A CD1 1 
ATOM   1117 C CD2 . TYR A 1 144 ? -22.754 11.462  -7.826  1.00 67.08  ? 148 TYR A CD2 1 
ATOM   1118 C CE1 . TYR A 1 144 ? -21.916 12.466  -5.400  1.00 63.16  ? 148 TYR A CE1 1 
ATOM   1119 C CE2 . TYR A 1 144 ? -22.683 10.631  -6.726  1.00 65.86  ? 148 TYR A CE2 1 
ATOM   1120 C CZ  . TYR A 1 144 ? -22.263 11.137  -5.516  1.00 63.92  ? 148 TYR A CZ  1 
ATOM   1121 O OH  . TYR A 1 144 ? -22.191 10.314  -4.416  1.00 62.89  ? 148 TYR A OH  1 
ATOM   1122 N N   . LYS A 1 145 ? -23.179 16.639  -10.130 1.00 71.23  ? 149 LYS A N   1 
ATOM   1123 C CA  . LYS A 1 145 ? -23.082 17.571  -11.244 1.00 77.90  ? 149 LYS A CA  1 
ATOM   1124 C C   . LYS A 1 145 ? -21.822 17.371  -12.075 1.00 71.64  ? 149 LYS A C   1 
ATOM   1125 O O   . LYS A 1 145 ? -21.726 17.930  -13.172 1.00 86.72  ? 149 LYS A O   1 
ATOM   1126 C CB  . LYS A 1 145 ? -23.138 19.014  -10.731 1.00 82.21  ? 149 LYS A CB  1 
ATOM   1127 C CG  . LYS A 1 145 ? -23.577 20.026  -11.779 1.00 104.13 ? 149 LYS A CG  1 
ATOM   1128 C CD  . LYS A 1 145 ? -23.662 21.430  -11.206 1.00 107.50 ? 149 LYS A CD  1 
ATOM   1129 C CE  . LYS A 1 145 ? -24.135 22.420  -12.257 1.00 104.01 ? 149 LYS A CE  1 
ATOM   1130 N NZ  . LYS A 1 145 ? -24.226 23.805  -11.718 1.00 94.67  ? 149 LYS A NZ  1 
ATOM   1131 N N   . ASN A 1 146 ? -20.860 16.593  -11.585 1.00 69.08  ? 150 ASN A N   1 
ATOM   1132 C CA  . ASN A 1 146 ? -19.649 16.288  -12.333 1.00 68.07  ? 150 ASN A CA  1 
ATOM   1133 C C   . ASN A 1 146 ? -19.636 14.870  -12.883 1.00 68.48  ? 150 ASN A C   1 
ATOM   1134 O O   . ASN A 1 146 ? -18.650 14.473  -13.513 1.00 67.80  ? 150 ASN A O   1 
ATOM   1135 C CB  . ASN A 1 146 ? -18.412 16.514  -11.457 1.00 65.00  ? 150 ASN A CB  1 
ATOM   1136 C CG  . ASN A 1 146 ? -18.221 17.969  -11.087 1.00 64.67  ? 150 ASN A CG  1 
ATOM   1137 O OD1 . ASN A 1 146 ? -18.617 18.869  -11.829 1.00 66.66  ? 150 ASN A OD1 1 
ATOM   1138 N ND2 . ASN A 1 146 ? -17.610 18.210  -9.933  1.00 62.30  ? 150 ASN A ND2 1 
ATOM   1139 N N   . LEU A 1 147 ? -20.697 14.099  -12.660 1.00 82.19  ? 151 LEU A N   1 
ATOM   1140 C CA  . LEU A 1 147 ? -20.820 12.756  -13.203 1.00 74.51  ? 151 LEU A CA  1 
ATOM   1141 C C   . LEU A 1 147 ? -22.130 12.642  -13.969 1.00 73.76  ? 151 LEU A C   1 
ATOM   1142 O O   . LEU A 1 147 ? -23.019 13.488  -13.850 1.00 75.23  ? 151 LEU A O   1 
ATOM   1143 C CB  . LEU A 1 147 ? -20.756 11.691  -12.100 1.00 74.94  ? 151 LEU A CB  1 
ATOM   1144 C CG  . LEU A 1 147 ? -19.450 11.623  -11.307 1.00 65.69  ? 151 LEU A CG  1 
ATOM   1145 C CD1 . LEU A 1 147 ? -19.554 10.582  -10.209 1.00 64.50  ? 151 LEU A CD1 1 
ATOM   1146 C CD2 . LEU A 1 147 ? -18.276 11.322  -12.226 1.00 72.90  ? 151 LEU A CD2 1 
ATOM   1147 N N   . LEU A 1 148 ? -22.239 11.576  -14.758 1.00 77.99  ? 152 LEU A N   1 
ATOM   1148 C CA  . LEU A 1 148 ? -23.394 11.361  -15.625 1.00 78.29  ? 152 LEU A CA  1 
ATOM   1149 C C   . LEU A 1 148 ? -23.771 9.889   -15.545 1.00 78.82  ? 152 LEU A C   1 
ATOM   1150 O O   . LEU A 1 148 ? -23.011 9.027   -15.997 1.00 78.22  ? 152 LEU A O   1 
ATOM   1151 C CB  . LEU A 1 148 ? -23.082 11.775  -17.064 1.00 81.20  ? 152 LEU A CB  1 
ATOM   1152 C CG  . LEU A 1 148 ? -24.265 12.080  -17.982 1.00 83.65  ? 152 LEU A CG  1 
ATOM   1153 C CD1 . LEU A 1 148 ? -25.139 13.163  -17.373 1.00 84.41  ? 152 LEU A CD1 1 
ATOM   1154 C CD2 . LEU A 1 148 ? -23.769 12.498  -19.357 1.00 90.93  ? 152 LEU A CD2 1 
ATOM   1155 N N   . TRP A 1 149 ? -24.937 9.599   -14.970 1.00 80.08  ? 153 TRP A N   1 
ATOM   1156 C CA  . TRP A 1 149 ? -25.394 8.221   -14.803 1.00 80.80  ? 153 TRP A CA  1 
ATOM   1157 C C   . TRP A 1 149 ? -26.044 7.763   -16.103 1.00 87.48  ? 153 TRP A C   1 
ATOM   1158 O O   . TRP A 1 149 ? -27.213 8.057   -16.365 1.00 98.24  ? 153 TRP A O   1 
ATOM   1159 C CB  . TRP A 1 149 ? -26.361 8.114   -13.629 1.00 81.01  ? 153 TRP A CB  1 
ATOM   1160 C CG  . TRP A 1 149 ? -26.626 6.703   -13.181 1.00 81.18  ? 153 TRP A CG  1 
ATOM   1161 C CD1 . TRP A 1 149 ? -26.412 5.557   -13.894 1.00 81.99  ? 153 TRP A CD1 1 
ATOM   1162 C CD2 . TRP A 1 149 ? -27.142 6.293   -11.911 1.00 80.68  ? 153 TRP A CD2 1 
ATOM   1163 N NE1 . TRP A 1 149 ? -26.771 4.462   -13.147 1.00 82.05  ? 153 TRP A NE1 1 
ATOM   1164 C CE2 . TRP A 1 149 ? -27.221 4.887   -11.925 1.00 81.27  ? 153 TRP A CE2 1 
ATOM   1165 C CE3 . TRP A 1 149 ? -27.548 6.979   -10.764 1.00 80.01  ? 153 TRP A CE3 1 
ATOM   1166 C CZ2 . TRP A 1 149 ? -27.689 4.155   -10.837 1.00 81.19  ? 153 TRP A CZ2 1 
ATOM   1167 C CZ3 . TRP A 1 149 ? -28.012 6.251   -9.685  1.00 83.26  ? 153 TRP A CZ3 1 
ATOM   1168 C CH2 . TRP A 1 149 ? -28.078 4.854   -9.729  1.00 87.90  ? 153 TRP A CH2 1 
ATOM   1169 N N   . LEU A 1 150 ? -25.288 7.031   -16.917 1.00 83.91  ? 154 LEU A N   1 
ATOM   1170 C CA  . LEU A 1 150 ? -25.796 6.523   -18.185 1.00 86.92  ? 154 LEU A CA  1 
ATOM   1171 C C   . LEU A 1 150 ? -26.723 5.342   -17.930 1.00 95.78  ? 154 LEU A C   1 
ATOM   1172 O O   . LEU A 1 150 ? -26.303 4.329   -17.360 1.00 93.08  ? 154 LEU A O   1 
ATOM   1173 C CB  . LEU A 1 150 ? -24.644 6.115   -19.098 1.00 86.41  ? 154 LEU A CB  1 
ATOM   1174 C CG  . LEU A 1 150 ? -23.614 7.200   -19.412 1.00 84.97  ? 154 LEU A CG  1 
ATOM   1175 C CD1 . LEU A 1 150 ? -22.617 6.705   -20.444 1.00 85.17  ? 154 LEU A CD1 1 
ATOM   1176 C CD2 . LEU A 1 150 ? -24.297 8.471   -19.886 1.00 91.43  ? 154 LEU A CD2 1 
ATOM   1177 N N   . THR A 1 151 ? -27.981 5.471   -18.353 1.00 106.11 ? 155 THR A N   1 
ATOM   1178 C CA  . THR A 1 151 ? -28.954 4.397   -18.192 1.00 95.00  ? 155 THR A CA  1 
ATOM   1179 C C   . THR A 1 151 ? -29.480 3.971   -19.561 1.00 101.20 ? 155 THR A C   1 
ATOM   1180 O O   . THR A 1 151 ? -28.875 4.303   -20.583 1.00 97.30  ? 155 THR A O   1 
ATOM   1181 C CB  . THR A 1 151 ? -30.095 4.837   -17.272 1.00 99.75  ? 155 THR A CB  1 
ATOM   1182 O OG1 . THR A 1 151 ? -29.570 5.673   -16.233 1.00 116.09 ? 155 THR A OG1 1 
ATOM   1183 C CG2 . THR A 1 151 ? -30.760 3.621   -16.630 1.00 99.17  ? 155 THR A CG2 1 
ATOM   1184 N N   . GLY A 1 152 ? -30.603 3.253   -19.604 1.00 122.92 ? 156 GLY A N   1 
ATOM   1185 C CA  . GLY A 1 152 ? -31.080 2.694   -20.855 1.00 121.11 ? 156 GLY A CA  1 
ATOM   1186 C C   . GLY A 1 152 ? -31.793 3.713   -21.729 1.00 125.44 ? 156 GLY A C   1 
ATOM   1187 O O   . GLY A 1 152 ? -32.519 4.584   -21.254 1.00 124.64 ? 156 GLY A O   1 
ATOM   1188 N N   . LYS A 1 153 ? -31.588 3.582   -23.041 1.00 136.94 ? 157 LYS A N   1 
ATOM   1189 C CA  . LYS A 1 153 ? -32.169 4.482   -24.035 1.00 145.66 ? 157 LYS A CA  1 
ATOM   1190 C C   . LYS A 1 153 ? -32.864 3.647   -25.103 1.00 147.65 ? 157 LYS A C   1 
ATOM   1191 O O   . LYS A 1 153 ? -32.205 2.904   -25.838 1.00 150.55 ? 157 LYS A O   1 
ATOM   1192 C CB  . LYS A 1 153 ? -31.096 5.376   -24.657 1.00 147.69 ? 157 LYS A CB  1 
ATOM   1193 C CG  . LYS A 1 153 ? -31.527 6.111   -25.923 1.00 148.19 ? 157 LYS A CG  1 
ATOM   1194 C CD  . LYS A 1 153 ? -32.402 7.315   -25.615 1.00 148.68 ? 157 LYS A CD  1 
ATOM   1195 C CE  . LYS A 1 153 ? -32.662 8.130   -26.874 1.00 155.81 ? 157 LYS A CE  1 
ATOM   1196 N NZ  . LYS A 1 153 ? -33.452 9.365   -26.612 1.00 157.18 ? 157 LYS A NZ  1 
ATOM   1197 N N   . ASN A 1 154 ? -34.190 3.775   -25.185 1.00 139.27 ? 158 ASN A N   1 
ATOM   1198 C CA  . ASN A 1 154 ? -35.006 3.051   -26.163 1.00 140.49 ? 158 ASN A CA  1 
ATOM   1199 C C   . ASN A 1 154 ? -34.824 1.537   -26.059 1.00 137.75 ? 158 ASN A C   1 
ATOM   1200 O O   . ASN A 1 154 ? -35.018 0.809   -27.035 1.00 131.37 ? 158 ASN A O   1 
ATOM   1201 C CB  . ASN A 1 154 ? -34.721 3.531   -27.591 1.00 134.21 ? 158 ASN A CB  1 
ATOM   1202 C CG  . ASN A 1 154 ? -35.269 4.922   -27.858 1.00 132.62 ? 158 ASN A CG  1 
ATOM   1203 O OD1 . ASN A 1 154 ? -36.361 5.268   -27.407 1.00 137.84 ? 158 ASN A OD1 1 
ATOM   1204 N ND2 . ASN A 1 154 ? -34.509 5.728   -28.591 1.00 128.17 ? 158 ASN A ND2 1 
ATOM   1205 N N   . GLY A 1 155 ? -34.452 1.052   -24.877 1.00 139.33 ? 159 GLY A N   1 
ATOM   1206 C CA  . GLY A 1 155 ? -34.361 -0.374  -24.635 1.00 132.17 ? 159 GLY A CA  1 
ATOM   1207 C C   . GLY A 1 155 ? -33.050 -1.028  -25.007 1.00 135.06 ? 159 GLY A C   1 
ATOM   1208 O O   . GLY A 1 155 ? -33.010 -2.256  -25.146 1.00 125.30 ? 159 GLY A O   1 
ATOM   1209 N N   . LEU A 1 156 ? -31.976 -0.258  -25.169 1.00 147.78 ? 160 LEU A N   1 
ATOM   1210 C CA  . LEU A 1 156 ? -30.682 -0.827  -25.514 1.00 148.03 ? 160 LEU A CA  1 
ATOM   1211 C C   . LEU A 1 156 ? -29.574 -0.000  -24.880 1.00 136.11 ? 160 LEU A C   1 
ATOM   1212 O O   . LEU A 1 156 ? -29.726 1.203   -24.650 1.00 138.17 ? 160 LEU A O   1 
ATOM   1213 C CB  . LEU A 1 156 ? -30.475 -0.899  -27.033 1.00 151.47 ? 160 LEU A CB  1 
ATOM   1214 C CG  . LEU A 1 156 ? -31.166 -2.043  -27.778 1.00 156.90 ? 160 LEU A CG  1 
ATOM   1215 C CD1 . LEU A 1 156 ? -30.913 -1.946  -29.273 1.00 164.37 ? 160 LEU A CD1 1 
ATOM   1216 C CD2 . LEU A 1 156 ? -30.701 -3.389  -27.241 1.00 153.67 ? 160 LEU A CD2 1 
ATOM   1217 N N   . TYR A 1 157 ? -28.453 -0.666  -24.602 1.00 121.35 ? 161 TYR A N   1 
ATOM   1218 C CA  . TYR A 1 157 ? -27.255 -0.033  -24.055 1.00 102.04 ? 161 TYR A CA  1 
ATOM   1219 C C   . TYR A 1 157 ? -26.094 -0.402  -24.967 1.00 101.86 ? 161 TYR A C   1 
ATOM   1220 O O   . TYR A 1 157 ? -25.390 -1.391  -24.724 1.00 100.70 ? 161 TYR A O   1 
ATOM   1221 C CB  . TYR A 1 157 ? -26.999 -0.477  -22.616 1.00 99.38  ? 161 TYR A CB  1 
ATOM   1222 C CG  . TYR A 1 157 ? -26.103 0.456   -21.829 1.00 109.35 ? 161 TYR A CG  1 
ATOM   1223 C CD1 . TYR A 1 157 ? -24.760 0.599   -22.150 1.00 101.60 ? 161 TYR A CD1 1 
ATOM   1224 C CD2 . TYR A 1 157 ? -26.600 1.183   -20.756 1.00 107.35 ? 161 TYR A CD2 1 
ATOM   1225 C CE1 . TYR A 1 157 ? -23.940 1.447   -21.433 1.00 90.72  ? 161 TYR A CE1 1 
ATOM   1226 C CE2 . TYR A 1 157 ? -25.786 2.033   -20.031 1.00 98.42  ? 161 TYR A CE2 1 
ATOM   1227 C CZ  . TYR A 1 157 ? -24.456 2.161   -20.373 1.00 95.98  ? 161 TYR A CZ  1 
ATOM   1228 O OH  . TYR A 1 157 ? -23.638 3.005   -19.656 1.00 96.26  ? 161 TYR A OH  1 
ATOM   1229 N N   . PRO A 1 158 ? -25.863 0.368   -26.028 1.00 103.18 ? 162 PRO A N   1 
ATOM   1230 C CA  . PRO A 1 158 ? -24.823 0.005   -26.998 1.00 103.55 ? 162 PRO A CA  1 
ATOM   1231 C C   . PRO A 1 158 ? -23.427 0.078   -26.394 1.00 99.98  ? 162 PRO A C   1 
ATOM   1232 O O   . PRO A 1 158 ? -23.208 0.580   -25.290 1.00 97.16  ? 162 PRO A O   1 
ATOM   1233 C CB  . PRO A 1 158 ? -24.997 1.040   -28.115 1.00 105.75 ? 162 PRO A CB  1 
ATOM   1234 C CG  . PRO A 1 158 ? -26.384 1.572   -27.937 1.00 107.56 ? 162 PRO A CG  1 
ATOM   1235 C CD  . PRO A 1 158 ? -26.640 1.538   -26.465 1.00 104.96 ? 162 PRO A CD  1 
ATOM   1236 N N   . ASN A 1 159 ? -22.469 -0.445  -27.157 1.00 107.35 ? 163 ASN A N   1 
ATOM   1237 C CA  . ASN A 1 159 ? -21.064 -0.434  -26.764 1.00 98.32  ? 163 ASN A CA  1 
ATOM   1238 C C   . ASN A 1 159 ? -20.497 0.960   -27.001 1.00 103.13 ? 163 ASN A C   1 
ATOM   1239 O O   . ASN A 1 159 ? -20.342 1.388   -28.150 1.00 98.50  ? 163 ASN A O   1 
ATOM   1240 C CB  . ASN A 1 159 ? -20.283 -1.483  -27.550 1.00 101.77 ? 163 ASN A CB  1 
ATOM   1241 C CG  . ASN A 1 159 ? -20.742 -2.896  -27.254 1.00 109.43 ? 163 ASN A CG  1 
ATOM   1242 O OD1 . ASN A 1 159 ? -21.746 -3.105  -26.573 1.00 111.20 ? 163 ASN A OD1 1 
ATOM   1243 N ND2 . ASN A 1 159 ? -20.008 -3.877  -27.769 1.00 107.28 ? 163 ASN A ND2 1 
ATOM   1244 N N   . LEU A 1 160 ? -20.187 1.669   -25.920 1.00 105.15 ? 164 LEU A N   1 
ATOM   1245 C CA  . LEU A 1 160 ? -19.624 3.008   -26.006 1.00 101.97 ? 164 LEU A CA  1 
ATOM   1246 C C   . LEU A 1 160 ? -18.112 2.949   -25.835 1.00 97.64  ? 164 LEU A C   1 
ATOM   1247 O O   . LEU A 1 160 ? -17.596 2.161   -25.035 1.00 96.63  ? 164 LEU A O   1 
ATOM   1248 C CB  . LEU A 1 160 ? -20.246 3.935   -24.956 1.00 95.11  ? 164 LEU A CB  1 
ATOM   1249 C CG  . LEU A 1 160 ? -20.052 3.636   -23.467 1.00 91.54  ? 164 LEU A CG  1 
ATOM   1250 C CD1 . LEU A 1 160 ? -18.869 4.410   -22.896 1.00 84.57  ? 164 LEU A CD1 1 
ATOM   1251 C CD2 . LEU A 1 160 ? -21.323 3.946   -22.691 1.00 87.88  ? 164 LEU A CD2 1 
ATOM   1252 N N   . SER A 1 161 ? -17.406 3.786   -26.597 1.00 99.00  ? 165 SER A N   1 
ATOM   1253 C CA  . SER A 1 161 ? -15.944 3.836   -26.550 1.00 96.30  ? 165 SER A CA  1 
ATOM   1254 C C   . SER A 1 161 ? -15.521 5.263   -26.905 1.00 93.96  ? 165 SER A C   1 
ATOM   1255 O O   . SER A 1 161 ? -15.374 5.606   -28.080 1.00 100.41 ? 165 SER A O   1 
ATOM   1256 C CB  . SER A 1 161 ? -15.321 2.815   -27.491 1.00 100.96 ? 165 SER A CB  1 
ATOM   1257 O OG  . SER A 1 161 ? -13.913 2.962   -27.542 1.00 103.55 ? 165 SER A OG  1 
ATOM   1258 N N   . LYS A 1 162 ? -15.329 6.082   -25.878 1.00 94.92  ? 166 LYS A N   1 
ATOM   1259 C CA  . LYS A 1 162 ? -14.904 7.463   -26.044 1.00 99.40  ? 166 LYS A CA  1 
ATOM   1260 C C   . LYS A 1 162 ? -13.481 7.639   -25.531 1.00 92.72  ? 166 LYS A C   1 
ATOM   1261 O O   . LYS A 1 162 ? -12.909 6.755   -24.890 1.00 96.16  ? 166 LYS A O   1 
ATOM   1262 C CB  . LYS A 1 162 ? -15.861 8.421   -25.323 1.00 93.89  ? 166 LYS A CB  1 
ATOM   1263 C CG  . LYS A 1 162 ? -17.232 8.531   -25.975 1.00 107.81 ? 166 LYS A CG  1 
ATOM   1264 C CD  . LYS A 1 162 ? -17.131 9.051   -27.403 1.00 111.68 ? 166 LYS A CD  1 
ATOM   1265 C CE  . LYS A 1 162 ? -18.501 9.135   -28.063 1.00 113.66 ? 166 LYS A CE  1 
ATOM   1266 N NZ  . LYS A 1 162 ? -18.421 9.607   -29.474 1.00 110.65 ? 166 LYS A NZ  1 
ATOM   1267 N N   . SER A 1 163 ? -12.909 8.802   -25.829 1.00 82.72  ? 167 SER A N   1 
ATOM   1268 C CA  . SER A 1 163 ? -11.539 9.104   -25.439 1.00 81.84  ? 167 SER A CA  1 
ATOM   1269 C C   . SER A 1 163 ? -11.373 10.615  -25.383 1.00 81.50  ? 167 SER A C   1 
ATOM   1270 O O   . SER A 1 163 ? -12.208 11.372  -25.884 1.00 82.22  ? 167 SER A O   1 
ATOM   1271 C CB  . SER A 1 163 ? -10.532 8.473   -26.405 1.00 81.77  ? 167 SER A CB  1 
ATOM   1272 O OG  . SER A 1 163 ? -10.819 8.827   -27.745 1.00 85.07  ? 167 SER A OG  1 
ATOM   1273 N N   . TYR A 1 164 ? -10.278 11.046  -24.761 1.00 77.90  ? 168 TYR A N   1 
ATOM   1274 C CA  . TYR A 1 164 ? -9.988  12.467  -24.629 1.00 77.49  ? 168 TYR A CA  1 
ATOM   1275 C C   . TYR A 1 164 ? -8.483  12.681  -24.644 1.00 82.97  ? 168 TYR A C   1 
ATOM   1276 O O   . TYR A 1 164 ? -7.744  11.967  -23.959 1.00 82.46  ? 168 TYR A O   1 
ATOM   1277 C CB  . TYR A 1 164 ? -10.591 13.039  -23.341 1.00 75.36  ? 168 TYR A CB  1 
ATOM   1278 C CG  . TYR A 1 164 ? -10.127 14.444  -23.024 1.00 76.09  ? 168 TYR A CG  1 
ATOM   1279 C CD1 . TYR A 1 164 ? -10.687 15.542  -23.662 1.00 76.72  ? 168 TYR A CD1 1 
ATOM   1280 C CD2 . TYR A 1 164 ? -9.132  14.671  -22.081 1.00 73.85  ? 168 TYR A CD2 1 
ATOM   1281 C CE1 . TYR A 1 164 ? -10.266 16.826  -23.375 1.00 78.98  ? 168 TYR A CE1 1 
ATOM   1282 C CE2 . TYR A 1 164 ? -8.705  15.951  -21.787 1.00 73.56  ? 168 TYR A CE2 1 
ATOM   1283 C CZ  . TYR A 1 164 ? -9.276  17.025  -22.437 1.00 82.08  ? 168 TYR A CZ  1 
ATOM   1284 O OH  . TYR A 1 164 ? -8.854  18.303  -22.149 1.00 87.65  ? 168 TYR A OH  1 
ATOM   1285 N N   . ALA A 1 165 ? -8.041  13.662  -25.425 1.00 95.41  ? 169 ALA A N   1 
ATOM   1286 C CA  . ALA A 1 165 ? -6.645  14.068  -25.473 1.00 98.70  ? 169 ALA A CA  1 
ATOM   1287 C C   . ALA A 1 165 ? -6.459  15.339  -24.656 1.00 98.32  ? 169 ALA A C   1 
ATOM   1288 O O   . ALA A 1 165 ? -7.327  16.217  -24.649 1.00 101.52 ? 169 ALA A O   1 
ATOM   1289 C CB  . ALA A 1 165 ? -6.185  14.294  -26.913 1.00 94.03  ? 169 ALA A CB  1 
ATOM   1290 N N   . ASN A 1 166 ? -5.321  15.435  -23.974 1.00 91.96  ? 170 ASN A N   1 
ATOM   1291 C CA  . ASN A 1 166 ? -5.065  16.530  -23.040 1.00 90.96  ? 170 ASN A CA  1 
ATOM   1292 C C   . ASN A 1 166 ? -4.667  17.775  -23.823 1.00 95.06  ? 170 ASN A C   1 
ATOM   1293 O O   . ASN A 1 166 ? -3.495  17.998  -24.132 1.00 98.79  ? 170 ASN A O   1 
ATOM   1294 C CB  . ASN A 1 166 ? -3.988  16.133  -22.038 1.00 92.71  ? 170 ASN A CB  1 
ATOM   1295 C CG  . ASN A 1 166 ? -3.989  17.011  -20.805 1.00 94.25  ? 170 ASN A CG  1 
ATOM   1296 O OD1 . ASN A 1 166 ? -4.396  18.172  -20.853 1.00 95.89  ? 170 ASN A OD1 1 
ATOM   1297 N ND2 . ASN A 1 166 ? -3.534  16.458  -19.686 1.00 92.13  ? 170 ASN A ND2 1 
ATOM   1298 N N   . ASN A 1 167 ? -5.656  18.602  -24.142 1.00 92.73  ? 171 ASN A N   1 
ATOM   1299 C CA  . ASN A 1 167 ? -5.430  19.887  -24.806 1.00 92.29  ? 171 ASN A CA  1 
ATOM   1300 C C   . ASN A 1 167 ? -5.496  21.039  -23.811 1.00 88.26  ? 171 ASN A C   1 
ATOM   1301 O O   . ASN A 1 167 ? -6.245  21.998  -23.991 1.00 94.40  ? 171 ASN A O   1 
ATOM   1302 C CB  . ASN A 1 167 ? -6.439  20.082  -25.931 1.00 104.62 ? 171 ASN A CB  1 
ATOM   1303 C CG  . ASN A 1 167 ? -6.234  19.108  -27.073 1.00 121.20 ? 171 ASN A CG  1 
ATOM   1304 O OD1 . ASN A 1 167 ? -5.109  18.709  -27.369 1.00 129.68 ? 171 ASN A OD1 1 
ATOM   1305 N ND2 . ASN A 1 167 ? -7.326  18.721  -27.723 1.00 115.93 ? 171 ASN A ND2 1 
ATOM   1306 N N   . LYS A 1 168 ? -4.707  20.955  -22.739 1.00 76.31  ? 172 LYS A N   1 
ATOM   1307 C CA  . LYS A 1 168 ? -4.736  21.974  -21.697 1.00 82.39  ? 172 LYS A CA  1 
ATOM   1308 C C   . LYS A 1 168 ? -3.370  22.360  -21.151 1.00 85.24  ? 172 LYS A C   1 
ATOM   1309 O O   . LYS A 1 168 ? -3.302  23.309  -20.364 1.00 91.78  ? 172 LYS A O   1 
ATOM   1310 C CB  . LYS A 1 168 ? -5.620  21.514  -20.529 1.00 77.83  ? 172 LYS A CB  1 
ATOM   1311 C CG  . LYS A 1 168 ? -7.112  21.561  -20.816 1.00 77.87  ? 172 LYS A CG  1 
ATOM   1312 C CD  . LYS A 1 168 ? -7.604  22.994  -20.928 1.00 92.27  ? 172 LYS A CD  1 
ATOM   1313 C CE  . LYS A 1 168 ? -9.112  23.043  -21.101 1.00 91.81  ? 172 LYS A CE  1 
ATOM   1314 N NZ  . LYS A 1 168 ? -9.614  24.442  -21.184 1.00 96.13  ? 172 LYS A NZ  1 
ATOM   1315 N N   . GLU A 1 169 ? -2.292  21.666  -21.522 1.00 90.62  ? 173 GLU A N   1 
ATOM   1316 C CA  . GLU A 1 169 ? -0.926  21.985  -21.107 1.00 92.52  ? 173 GLU A CA  1 
ATOM   1317 C C   . GLU A 1 169 ? -0.717  21.852  -19.601 1.00 83.29  ? 173 GLU A C   1 
ATOM   1318 O O   . GLU A 1 169 ? 0.277   22.352  -19.064 1.00 77.24  ? 173 GLU A O   1 
ATOM   1319 C CB  . GLU A 1 169 ? -0.517  23.387  -21.573 1.00 98.60  ? 173 GLU A CB  1 
ATOM   1320 C CG  . GLU A 1 169 ? -0.545  23.569  -23.078 1.00 102.30 ? 173 GLU A CG  1 
ATOM   1321 C CD  . GLU A 1 169 ? -0.179  24.975  -23.497 1.00 107.36 ? 173 GLU A CD  1 
ATOM   1322 O OE1 . GLU A 1 169 ? -0.096  25.854  -22.614 1.00 110.32 ? 173 GLU A OE1 1 
ATOM   1323 O OE2 . GLU A 1 169 ? 0.027   25.202  -24.708 1.00 102.13 ? 173 GLU A OE2 1 
ATOM   1324 N N   . LYS A 1 170 ? -1.635  21.184  -18.905 1.00 83.55  ? 174 LYS A N   1 
ATOM   1325 C CA  . LYS A 1 170 ? -1.525  20.960  -17.470 1.00 76.98  ? 174 LYS A CA  1 
ATOM   1326 C C   . LYS A 1 170 ? -2.081  19.581  -17.143 1.00 74.88  ? 174 LYS A C   1 
ATOM   1327 O O   . LYS A 1 170 ? -2.666  18.906  -17.994 1.00 81.20  ? 174 LYS A O   1 
ATOM   1328 C CB  . LYS A 1 170 ? -2.267  22.039  -16.668 1.00 81.55  ? 174 LYS A CB  1 
ATOM   1329 C CG  . LYS A 1 170 ? -1.674  23.434  -16.781 1.00 92.65  ? 174 LYS A CG  1 
ATOM   1330 C CD  . LYS A 1 170 ? -2.574  24.474  -16.134 1.00 105.13 ? 174 LYS A CD  1 
ATOM   1331 C CE  . LYS A 1 170 ? -2.028  25.880  -16.336 1.00 116.02 ? 174 LYS A CE  1 
ATOM   1332 N NZ  . LYS A 1 170 ? -2.935  26.922  -15.777 1.00 119.44 ? 174 LYS A NZ  1 
ATOM   1333 N N   . GLU A 1 171 ? -1.888  19.163  -15.895 1.00 77.79  ? 175 GLU A N   1 
ATOM   1334 C CA  . GLU A 1 171 ? -2.472  17.913  -15.426 1.00 71.31  ? 175 GLU A CA  1 
ATOM   1335 C C   . GLU A 1 171 ? -3.990  18.029  -15.373 1.00 66.52  ? 175 GLU A C   1 
ATOM   1336 O O   . GLU A 1 171 ? -4.535  19.049  -14.943 1.00 73.08  ? 175 GLU A O   1 
ATOM   1337 C CB  . GLU A 1 171 ? -1.929  17.553  -14.043 1.00 74.16  ? 175 GLU A CB  1 
ATOM   1338 C CG  . GLU A 1 171 ? -0.523  16.986  -14.042 1.00 79.68  ? 175 GLU A CG  1 
ATOM   1339 C CD  . GLU A 1 171 ? -0.052  16.612  -12.650 1.00 84.86  ? 175 GLU A CD  1 
ATOM   1340 O OE1 . GLU A 1 171 ? -0.360  17.358  -11.696 1.00 77.80  ? 175 GLU A OE1 1 
ATOM   1341 O OE2 . GLU A 1 171 ? 0.616   15.566  -12.508 1.00 82.19  ? 175 GLU A OE2 1 
ATOM   1342 N N   . VAL A 1 172 ? -4.676  16.977  -15.811 1.00 56.98  ? 176 VAL A N   1 
ATOM   1343 C CA  . VAL A 1 172 ? -6.134  16.963  -15.870 1.00 58.23  ? 176 VAL A CA  1 
ATOM   1344 C C   . VAL A 1 172 ? -6.645  15.856  -14.960 1.00 56.66  ? 176 VAL A C   1 
ATOM   1345 O O   . VAL A 1 172 ? -6.375  14.674  -15.199 1.00 56.64  ? 176 VAL A O   1 
ATOM   1346 C CB  . VAL A 1 172 ? -6.647  16.777  -17.306 1.00 61.00  ? 176 VAL A CB  1 
ATOM   1347 C CG1 . VAL A 1 172 ? -8.142  16.507  -17.303 1.00 62.13  ? 176 VAL A CG1 1 
ATOM   1348 C CG2 . VAL A 1 172 ? -6.330  18.009  -18.141 1.00 62.72  ? 176 VAL A CG2 1 
ATOM   1349 N N   . LEU A 1 173 ? -7.395  16.236  -13.930 1.00 55.66  ? 177 LEU A N   1 
ATOM   1350 C CA  . LEU A 1 173 ? -7.973  15.277  -12.997 1.00 54.50  ? 177 LEU A CA  1 
ATOM   1351 C C   . LEU A 1 173 ? -9.281  14.742  -13.566 1.00 56.48  ? 177 LEU A C   1 
ATOM   1352 O O   . LEU A 1 173 ? -10.209 15.513  -13.829 1.00 64.92  ? 177 LEU A O   1 
ATOM   1353 C CB  . LEU A 1 173 ? -8.208  15.925  -11.634 1.00 52.78  ? 177 LEU A CB  1 
ATOM   1354 C CG  . LEU A 1 173 ? -9.033  15.098  -10.646 1.00 52.00  ? 177 LEU A CG  1 
ATOM   1355 C CD1 . LEU A 1 173 ? -8.314  13.807  -10.286 1.00 50.70  ? 177 LEU A CD1 1 
ATOM   1356 C CD2 . LEU A 1 173 ? -9.347  15.909  -9.402  1.00 50.75  ? 177 LEU A CD2 1 
ATOM   1357 N N   . VAL A 1 174 ? -9.358  13.426  -13.747 1.00 57.85  ? 178 VAL A N   1 
ATOM   1358 C CA  . VAL A 1 174 ? -10.548 12.772  -14.279 1.00 58.62  ? 178 VAL A CA  1 
ATOM   1359 C C   . VAL A 1 174 ? -11.133 11.865  -13.205 1.00 57.55  ? 178 VAL A C   1 
ATOM   1360 O O   . VAL A 1 174 ? -10.403 11.123  -12.540 1.00 60.43  ? 178 VAL A O   1 
ATOM   1361 C CB  . VAL A 1 174 ? -10.229 11.977  -15.561 1.00 60.33  ? 178 VAL A CB  1 
ATOM   1362 C CG1 . VAL A 1 174 ? -11.497 11.372  -16.145 1.00 62.56  ? 178 VAL A CG1 1 
ATOM   1363 C CG2 . VAL A 1 174 ? -9.549  12.873  -16.581 1.00 61.44  ? 178 VAL A CG2 1 
ATOM   1364 N N   . LEU A 1 175 ? -12.452 11.932  -13.036 1.00 58.73  ? 179 LEU A N   1 
ATOM   1365 C CA  . LEU A 1 175 ? -13.166 11.103  -12.077 1.00 58.19  ? 179 LEU A CA  1 
ATOM   1366 C C   . LEU A 1 175 ? -14.287 10.355  -12.781 1.00 60.57  ? 179 LEU A C   1 
ATOM   1367 O O   . LEU A 1 175 ? -14.878 10.852  -13.741 1.00 63.35  ? 179 LEU A O   1 
ATOM   1368 C CB  . LEU A 1 175 ? -13.751 11.934  -10.927 1.00 57.30  ? 179 LEU A CB  1 
ATOM   1369 C CG  . LEU A 1 175 ? -12.782 12.766  -10.085 1.00 66.75  ? 179 LEU A CG  1 
ATOM   1370 C CD1 . LEU A 1 175 ? -12.682 14.186  -10.619 1.00 55.72  ? 179 LEU A CD1 1 
ATOM   1371 C CD2 . LEU A 1 175 ? -13.205 12.763  -8.625  1.00 53.71  ? 179 LEU A CD2 1 
ATOM   1372 N N   . TRP A 1 176 ? -14.578 9.153   -12.291 1.00 60.38  ? 180 TRP A N   1 
ATOM   1373 C CA  . TRP A 1 176 ? -15.672 8.354   -12.823 1.00 62.64  ? 180 TRP A CA  1 
ATOM   1374 C C   . TRP A 1 176 ? -16.120 7.377   -11.745 1.00 61.98  ? 180 TRP A C   1 
ATOM   1375 O O   . TRP A 1 176 ? -15.541 7.312   -10.659 1.00 73.31  ? 180 TRP A O   1 
ATOM   1376 C CB  . TRP A 1 176 ? -15.260 7.615   -14.101 1.00 64.09  ? 180 TRP A CB  1 
ATOM   1377 C CG  . TRP A 1 176 ? -14.251 6.540   -13.873 1.00 62.79  ? 180 TRP A CG  1 
ATOM   1378 C CD1 . TRP A 1 176 ? -14.494 5.205   -13.727 1.00 63.30  ? 180 TRP A CD1 1 
ATOM   1379 C CD2 . TRP A 1 176 ? -12.833 6.704   -13.762 1.00 60.95  ? 180 TRP A CD2 1 
ATOM   1380 N NE1 . TRP A 1 176 ? -13.315 4.528   -13.534 1.00 61.92  ? 180 TRP A NE1 1 
ATOM   1381 C CE2 . TRP A 1 176 ? -12.280 5.426   -13.550 1.00 60.45  ? 180 TRP A CE2 1 
ATOM   1382 C CE3 . TRP A 1 176 ? -11.977 7.807   -13.822 1.00 59.82  ? 180 TRP A CE3 1 
ATOM   1383 C CZ2 . TRP A 1 176 ? -10.911 5.221   -13.398 1.00 58.90  ? 180 TRP A CZ2 1 
ATOM   1384 C CZ3 . TRP A 1 176 ? -10.618 7.601   -13.670 1.00 58.26  ? 180 TRP A CZ3 1 
ATOM   1385 C CH2 . TRP A 1 176 ? -10.099 6.319   -13.460 1.00 57.81  ? 180 TRP A CH2 1 
ATOM   1386 N N   . GLY A 1 177 ? -17.164 6.609   -12.064 1.00 64.02  ? 181 GLY A N   1 
ATOM   1387 C CA  . GLY A 1 177 ? -17.718 5.665   -11.119 1.00 63.89  ? 181 GLY A CA  1 
ATOM   1388 C C   . GLY A 1 177 ? -18.094 4.360   -11.791 1.00 65.76  ? 181 GLY A C   1 
ATOM   1389 O O   . GLY A 1 177 ? -18.166 4.261   -13.017 1.00 67.50  ? 181 GLY A O   1 
ATOM   1390 N N   . VAL A 1 178 ? -18.327 3.353   -10.954 1.00 71.60  ? 182 VAL A N   1 
ATOM   1391 C CA  . VAL A 1 178 ? -18.762 2.032   -11.392 1.00 67.34  ? 182 VAL A CA  1 
ATOM   1392 C C   . VAL A 1 178 ? -19.933 1.616   -10.514 1.00 70.14  ? 182 VAL A C   1 
ATOM   1393 O O   . VAL A 1 178 ? -19.804 1.568   -9.285  1.00 69.56  ? 182 VAL A O   1 
ATOM   1394 C CB  . VAL A 1 178 ? -17.633 0.992   -11.319 1.00 72.36  ? 182 VAL A CB  1 
ATOM   1395 C CG1 . VAL A 1 178 ? -18.174 -0.393  -11.634 1.00 70.74  ? 182 VAL A CG1 1 
ATOM   1396 C CG2 . VAL A 1 178 ? -16.514 1.357   -12.279 1.00 70.08  ? 182 VAL A CG2 1 
ATOM   1397 N N   . HIS A 1 179 ? -21.065 1.313   -11.141 1.00 78.17  ? 183 HIS A N   1 
ATOM   1398 C CA  . HIS A 1 179 ? -22.287 0.989   -10.420 1.00 72.32  ? 183 HIS A CA  1 
ATOM   1399 C C   . HIS A 1 179 ? -22.358 -0.503  -10.122 1.00 73.06  ? 183 HIS A C   1 
ATOM   1400 O O   . HIS A 1 179 ? -22.026 -1.337  -10.969 1.00 74.04  ? 183 HIS A O   1 
ATOM   1401 C CB  . HIS A 1 179 ? -23.513 1.418   -11.226 1.00 75.08  ? 183 HIS A CB  1 
ATOM   1402 C CG  . HIS A 1 179 ? -24.800 1.310   -10.471 1.00 81.75  ? 183 HIS A CG  1 
ATOM   1403 N ND1 . HIS A 1 179 ? -25.986 0.945   -11.071 1.00 85.65  ? 183 HIS A ND1 1 
ATOM   1404 C CD2 . HIS A 1 179 ? -25.089 1.526   -9.166  1.00 84.24  ? 183 HIS A CD2 1 
ATOM   1405 C CE1 . HIS A 1 179 ? -26.950 0.936   -10.167 1.00 88.59  ? 183 HIS A CE1 1 
ATOM   1406 N NE2 . HIS A 1 179 ? -26.432 1.286   -9.003  1.00 90.77  ? 183 HIS A NE2 1 
ATOM   1407 N N   . HIS A 1 180 ? -22.797 -0.830  -8.909  1.00 74.90  ? 184 HIS A N   1 
ATOM   1408 C CA  . HIS A 1 180 ? -22.960 -2.212  -8.461  1.00 79.56  ? 184 HIS A CA  1 
ATOM   1409 C C   . HIS A 1 180 ? -24.366 -2.377  -7.902  1.00 84.68  ? 184 HIS A C   1 
ATOM   1410 O O   . HIS A 1 180 ? -24.615 -2.049  -6.727  1.00 81.64  ? 184 HIS A O   1 
ATOM   1411 C CB  . HIS A 1 180 ? -21.913 -2.581  -7.418  1.00 80.53  ? 184 HIS A CB  1 
ATOM   1412 C CG  . HIS A 1 180 ? -20.504 -2.424  -7.898  1.00 75.10  ? 184 HIS A CG  1 
ATOM   1413 N ND1 . HIS A 1 180 ? -19.705 -3.498  -8.226  1.00 69.24  ? 184 HIS A ND1 1 
ATOM   1414 C CD2 . HIS A 1 180 ? -19.753 -1.318  -8.112  1.00 67.41  ? 184 HIS A CD2 1 
ATOM   1415 C CE1 . HIS A 1 180 ? -18.522 -3.061  -8.618  1.00 67.50  ? 184 HIS A CE1 1 
ATOM   1416 N NE2 . HIS A 1 180 ? -18.525 -1.742  -8.558  1.00 66.35  ? 184 HIS A NE2 1 
ATOM   1417 N N   . PRO A 1 181 ? -25.305 -2.874  -8.701  1.00 80.55  ? 185 PRO A N   1 
ATOM   1418 C CA  . PRO A 1 181 ? -26.696 -2.977  -8.253  1.00 81.63  ? 185 PRO A CA  1 
ATOM   1419 C C   . PRO A 1 181 ? -26.860 -4.074  -7.218  1.00 93.55  ? 185 PRO A C   1 
ATOM   1420 O O   . PRO A 1 181 ? -25.987 -4.943  -7.071  1.00 92.12  ? 185 PRO A O   1 
ATOM   1421 C CB  . PRO A 1 181 ? -27.460 -3.311  -9.546  1.00 83.86  ? 185 PRO A CB  1 
ATOM   1422 C CG  . PRO A 1 181 ? -26.522 -2.965  -10.660 1.00 82.90  ? 185 PRO A CG  1 
ATOM   1423 C CD  . PRO A 1 181 ? -25.158 -3.235  -10.119 1.00 80.79  ? 185 PRO A CD  1 
ATOM   1424 N N   . PRO A 1 182 ? -27.970 -4.068  -6.478  1.00 101.53 ? 186 PRO A N   1 
ATOM   1425 C CA  . PRO A 1 182 ? -28.164 -5.068  -5.419  1.00 101.98 ? 186 PRO A CA  1 
ATOM   1426 C C   . PRO A 1 182 ? -28.522 -6.453  -5.938  1.00 107.61 ? 186 PRO A C   1 
ATOM   1427 O O   . PRO A 1 182 ? -27.978 -7.456  -5.468  1.00 121.46 ? 186 PRO A O   1 
ATOM   1428 C CB  . PRO A 1 182 ? -29.311 -4.475  -4.594  1.00 96.75  ? 186 PRO A CB  1 
ATOM   1429 C CG  . PRO A 1 182 ? -30.059 -3.615  -5.560  1.00 96.22  ? 186 PRO A CG  1 
ATOM   1430 C CD  . PRO A 1 182 ? -29.021 -3.036  -6.468  1.00 96.89  ? 186 PRO A CD  1 
ATOM   1431 N N   . ASN A 1 183 ? -29.441 -6.526  -6.895  1.00 89.16  ? 187 ASN A N   1 
ATOM   1432 C CA  . ASN A 1 183 ? -29.919 -7.796  -7.422  1.00 99.17  ? 187 ASN A CA  1 
ATOM   1433 C C   . ASN A 1 183 ? -29.797 -7.796  -8.942  1.00 108.43 ? 187 ASN A C   1 
ATOM   1434 O O   . ASN A 1 183 ? -29.409 -6.800  -9.561  1.00 110.67 ? 187 ASN A O   1 
ATOM   1435 C CB  . ASN A 1 183 ? -31.366 -8.072  -6.991  1.00 101.98 ? 187 ASN A CB  1 
ATOM   1436 C CG  . ASN A 1 183 ? -32.320 -6.970  -7.404  1.00 101.67 ? 187 ASN A CG  1 
ATOM   1437 O OD1 . ASN A 1 183 ? -32.715 -6.877  -8.566  1.00 99.88  ? 187 ASN A OD1 1 
ATOM   1438 N ND2 . ASN A 1 183 ? -32.706 -6.135  -6.447  1.00 104.18 ? 187 ASN A ND2 1 
ATOM   1439 N N   . ILE A 1 184 ? -30.137 -8.938  -9.542  1.00 115.57 ? 188 ILE A N   1 
ATOM   1440 C CA  . ILE A 1 184 ? -30.035 -9.092  -10.989 1.00 121.08 ? 188 ILE A CA  1 
ATOM   1441 C C   . ILE A 1 184 ? -31.172 -8.369  -11.702 1.00 129.13 ? 188 ILE A C   1 
ATOM   1442 O O   . ILE A 1 184 ? -31.002 -7.901  -12.837 1.00 125.02 ? 188 ILE A O   1 
ATOM   1443 C CB  . ILE A 1 184 ? -30.011 -10.586 -11.354 1.00 119.50 ? 188 ILE A CB  1 
ATOM   1444 C CG1 . ILE A 1 184 ? -29.065 -11.350 -10.426 1.00 115.61 ? 188 ILE A CG1 1 
ATOM   1445 C CG2 . ILE A 1 184 ? -29.601 -10.776 -12.804 1.00 115.17 ? 188 ILE A CG2 1 
ATOM   1446 C CD1 . ILE A 1 184 ? -29.050 -12.842 -10.675 1.00 122.13 ? 188 ILE A CD1 1 
ATOM   1447 N N   . GLY A 1 185 ? -32.340 -8.270  -11.063 1.00 132.62 ? 189 GLY A N   1 
ATOM   1448 C CA  . GLY A 1 185 ? -33.471 -7.615  -11.700 1.00 130.08 ? 189 GLY A CA  1 
ATOM   1449 C C   . GLY A 1 185 ? -33.213 -6.150  -11.993 1.00 131.94 ? 189 GLY A C   1 
ATOM   1450 O O   . GLY A 1 185 ? -33.542 -5.656  -13.074 1.00 130.17 ? 189 GLY A O   1 
ATOM   1451 N N   . ASP A 1 186 ? -32.622 -5.433  -11.034 1.00 127.01 ? 190 ASP A N   1 
ATOM   1452 C CA  . ASP A 1 186 ? -32.275 -4.037  -11.274 1.00 115.53 ? 190 ASP A CA  1 
ATOM   1453 C C   . ASP A 1 186 ? -31.090 -3.910  -12.225 1.00 102.49 ? 190 ASP A C   1 
ATOM   1454 O O   . ASP A 1 186 ? -30.998 -2.928  -12.970 1.00 99.54  ? 190 ASP A O   1 
ATOM   1455 C CB  . ASP A 1 186 ? -31.981 -3.332  -9.949  1.00 113.41 ? 190 ASP A CB  1 
ATOM   1456 C CG  . ASP A 1 186 ? -33.214 -3.204  -9.072  1.00 124.97 ? 190 ASP A CG  1 
ATOM   1457 O OD1 . ASP A 1 186 ? -33.928 -2.186  -9.194  1.00 135.01 ? 190 ASP A OD1 1 
ATOM   1458 O OD2 . ASP A 1 186 ? -33.469 -4.120  -8.262  1.00 124.75 ? 190 ASP A OD2 1 
ATOM   1459 N N   . GLN A 1 187 ? -30.185 -4.891  -12.219 1.00 93.51  ? 191 GLN A N   1 
ATOM   1460 C CA  . GLN A 1 187 ? -29.061 -4.886  -13.151 1.00 92.24  ? 191 GLN A CA  1 
ATOM   1461 C C   . GLN A 1 187 ? -29.548 -4.946  -14.594 1.00 95.01  ? 191 GLN A C   1 
ATOM   1462 O O   . GLN A 1 187 ? -29.316 -4.020  -15.384 1.00 94.79  ? 191 GLN A O   1 
ATOM   1463 C CB  . GLN A 1 187 ? -28.127 -6.058  -12.844 1.00 91.08  ? 191 GLN A CB  1 
ATOM   1464 C CG  . GLN A 1 187 ? -27.139 -6.381  -13.955 1.00 90.79  ? 191 GLN A CG  1 
ATOM   1465 C CD  . GLN A 1 187 ? -26.177 -5.245  -14.235 1.00 96.09  ? 191 GLN A CD  1 
ATOM   1466 O OE1 . GLN A 1 187 ? -25.686 -4.590  -13.315 1.00 92.57  ? 191 GLN A OE1 1 
ATOM   1467 N NE2 . GLN A 1 187 ? -25.904 -5.002  -15.512 1.00 98.18  ? 191 GLN A NE2 1 
ATOM   1468 N N   . ARG A 1 188 ? -30.226 -6.040  -14.957 1.00 111.58 ? 192 ARG A N   1 
ATOM   1469 C CA  . ARG A 1 188 ? -30.776 -6.154  -16.303 1.00 104.18 ? 192 ARG A CA  1 
ATOM   1470 C C   . ARG A 1 188 ? -31.778 -5.046  -16.590 1.00 102.36 ? 192 ARG A C   1 
ATOM   1471 O O   . ARG A 1 188 ? -31.876 -4.575  -17.728 1.00 103.76 ? 192 ARG A O   1 
ATOM   1472 C CB  . ARG A 1 188 ? -31.442 -7.517  -16.491 1.00 112.43 ? 192 ARG A CB  1 
ATOM   1473 C CG  . ARG A 1 188 ? -30.520 -8.710  -16.336 1.00 117.46 ? 192 ARG A CG  1 
ATOM   1474 C CD  . ARG A 1 188 ? -31.305 -10.001 -16.490 1.00 120.37 ? 192 ARG A CD  1 
ATOM   1475 N NE  . ARG A 1 188 ? -30.495 -11.182 -16.208 1.00 120.80 ? 192 ARG A NE  1 
ATOM   1476 C CZ  . ARG A 1 188 ? -30.989 -12.408 -16.072 1.00 117.78 ? 192 ARG A CZ  1 
ATOM   1477 N NH1 . ARG A 1 188 ? -32.293 -12.615 -16.189 1.00 112.04 ? 192 ARG A NH1 1 
ATOM   1478 N NH2 . ARG A 1 188 ? -30.180 -13.426 -15.813 1.00 123.37 ? 192 ARG A NH2 1 
ATOM   1479 N N   . ALA A 1 189 ? -32.524 -4.614  -15.571 1.00 102.30 ? 193 ALA A N   1 
ATOM   1480 C CA  . ALA A 1 189 ? -33.518 -3.567  -15.755 1.00 103.95 ? 193 ALA A CA  1 
ATOM   1481 C C   . ALA A 1 189 ? -32.887 -2.214  -16.053 1.00 109.01 ? 193 ALA A C   1 
ATOM   1482 O O   . ALA A 1 189 ? -33.547 -1.357  -16.650 1.00 103.72 ? 193 ALA A O   1 
ATOM   1483 C CB  . ALA A 1 189 ? -34.406 -3.465  -14.514 1.00 104.37 ? 193 ALA A CB  1 
ATOM   1484 N N   . LEU A 1 190 ? -31.633 -2.003  -15.657 1.00 117.28 ? 194 LEU A N   1 
ATOM   1485 C CA  . LEU A 1 190 ? -30.974 -0.720  -15.861 1.00 116.57 ? 194 LEU A CA  1 
ATOM   1486 C C   . LEU A 1 190 ? -30.011 -0.706  -17.039 1.00 110.23 ? 194 LEU A C   1 
ATOM   1487 O O   . LEU A 1 190 ? -29.887 0.329   -17.702 1.00 107.87 ? 194 LEU A O   1 
ATOM   1488 C CB  . LEU A 1 190 ? -30.218 -0.302  -14.595 1.00 113.35 ? 194 LEU A CB  1 
ATOM   1489 C CG  . LEU A 1 190 ? -31.066 0.236   -13.440 1.00 114.73 ? 194 LEU A CG  1 
ATOM   1490 C CD1 . LEU A 1 190 ? -30.185 0.619   -12.263 1.00 108.40 ? 194 LEU A CD1 1 
ATOM   1491 C CD2 . LEU A 1 190 ? -31.902 1.421   -13.894 1.00 118.05 ? 194 LEU A CD2 1 
ATOM   1492 N N   . TYR A 1 191 ? -29.325 -1.813  -17.324 1.00 95.88  ? 195 TYR A N   1 
ATOM   1493 C CA  . TYR A 1 191 ? -28.302 -1.811  -18.361 1.00 95.38  ? 195 TYR A CA  1 
ATOM   1494 C C   . TYR A 1 191 ? -28.525 -2.839  -19.461 1.00 104.73 ? 195 TYR A C   1 
ATOM   1495 O O   . TYR A 1 191 ? -27.664 -2.974  -20.339 1.00 98.03  ? 195 TYR A O   1 
ATOM   1496 C CB  . TYR A 1 191 ? -26.918 -2.018  -17.732 1.00 96.30  ? 195 TYR A CB  1 
ATOM   1497 C CG  . TYR A 1 191 ? -26.594 -0.984  -16.678 1.00 89.12  ? 195 TYR A CG  1 
ATOM   1498 C CD1 . TYR A 1 191 ? -26.245 0.312   -17.035 1.00 88.24  ? 195 TYR A CD1 1 
ATOM   1499 C CD2 . TYR A 1 191 ? -26.649 -1.300  -15.328 1.00 87.55  ? 195 TYR A CD2 1 
ATOM   1500 C CE1 . TYR A 1 191 ? -25.955 1.264   -16.075 1.00 93.27  ? 195 TYR A CE1 1 
ATOM   1501 C CE2 . TYR A 1 191 ? -26.360 -0.355  -14.361 1.00 92.80  ? 195 TYR A CE2 1 
ATOM   1502 C CZ  . TYR A 1 191 ? -26.012 0.924   -14.740 1.00 87.50  ? 195 TYR A CZ  1 
ATOM   1503 O OH  . TYR A 1 191 ? -25.724 1.865   -13.779 1.00 81.96  ? 195 TYR A OH  1 
ATOM   1504 N N   . HIS A 1 192 ? -29.644 -3.565  -19.441 1.00 110.57 ? 196 HIS A N   1 
ATOM   1505 C CA  . HIS A 1 192 ? -30.039 -4.486  -20.507 1.00 107.79 ? 196 HIS A CA  1 
ATOM   1506 C C   . HIS A 1 192 ? -29.014 -5.588  -20.753 1.00 107.83 ? 196 HIS A C   1 
ATOM   1507 O O   . HIS A 1 192 ? -29.044 -6.240  -21.801 1.00 114.08 ? 196 HIS A O   1 
ATOM   1508 C CB  . HIS A 1 192 ? -30.312 -3.738  -21.817 1.00 114.65 ? 196 HIS A CB  1 
ATOM   1509 C CG  . HIS A 1 192 ? -31.297 -2.621  -21.682 1.00 123.47 ? 196 HIS A CG  1 
ATOM   1510 N ND1 . HIS A 1 192 ? -32.592 -2.819  -21.253 1.00 127.16 ? 196 HIS A ND1 1 
ATOM   1511 C CD2 . HIS A 1 192 ? -31.180 -1.295  -21.926 1.00 123.76 ? 196 HIS A CD2 1 
ATOM   1512 C CE1 . HIS A 1 192 ? -33.229 -1.662  -21.236 1.00 127.91 ? 196 HIS A CE1 1 
ATOM   1513 N NE2 . HIS A 1 192 ? -32.395 -0.721  -21.640 1.00 127.22 ? 196 HIS A NE2 1 
ATOM   1514 N N   . LYS A 1 193 ? -28.096 -5.809  -19.816 1.00 112.26 ? 197 LYS A N   1 
ATOM   1515 C CA  . LYS A 1 193 ? -27.071 -6.828  -19.970 1.00 114.06 ? 197 LYS A CA  1 
ATOM   1516 C C   . LYS A 1 193 ? -26.885 -7.555  -18.648 1.00 119.71 ? 197 LYS A C   1 
ATOM   1517 O O   . LYS A 1 193 ? -27.241 -7.050  -17.581 1.00 116.84 ? 197 LYS A O   1 
ATOM   1518 C CB  . LYS A 1 193 ? -25.738 -6.229  -20.440 1.00 102.41 ? 197 LYS A CB  1 
ATOM   1519 C CG  . LYS A 1 193 ? -25.801 -5.554  -21.799 1.00 99.11  ? 197 LYS A CG  1 
ATOM   1520 C CD  . LYS A 1 193 ? -24.445 -5.013  -22.203 1.00 96.97  ? 197 LYS A CD  1 
ATOM   1521 C CE  . LYS A 1 193 ? -24.529 -4.229  -23.500 1.00 98.81  ? 197 LYS A CE  1 
ATOM   1522 N NZ  . LYS A 1 193 ? -24.930 -5.088  -24.646 1.00 123.23 ? 197 LYS A NZ  1 
ATOM   1523 N N   . GLU A 1 194 ? -26.311 -8.753  -18.732 1.00 129.30 ? 198 GLU A N   1 
ATOM   1524 C CA  . GLU A 1 194 ? -26.082 -9.582  -17.556 1.00 130.05 ? 198 GLU A CA  1 
ATOM   1525 C C   . GLU A 1 194 ? -24.624 -9.613  -17.121 1.00 124.12 ? 198 GLU A C   1 
ATOM   1526 O O   . GLU A 1 194 ? -24.350 -9.779  -15.928 1.00 121.78 ? 198 GLU A O   1 
ATOM   1527 C CB  . GLU A 1 194 ? -26.569 -11.013 -17.820 1.00 148.08 ? 198 GLU A CB  1 
ATOM   1528 C CG  . GLU A 1 194 ? -26.616 -11.901 -16.586 1.00 153.33 ? 198 GLU A CG  1 
ATOM   1529 C CD  . GLU A 1 194 ? -27.229 -13.262 -16.868 1.00 158.73 ? 198 GLU A CD  1 
ATOM   1530 O OE1 . GLU A 1 194 ? -27.757 -13.460 -17.983 1.00 160.93 ? 198 GLU A OE1 1 
ATOM   1531 O OE2 . GLU A 1 194 ? -27.185 -14.133 -15.973 1.00 159.76 ? 198 GLU A OE2 1 
ATOM   1532 N N   . ASN A 1 195 ? -23.685 -9.445  -18.053 1.00 126.16 ? 199 ASN A N   1 
ATOM   1533 C CA  . ASN A 1 195 ? -22.250 -9.457  -17.760 1.00 123.77 ? 199 ASN A CA  1 
ATOM   1534 C C   . ASN A 1 195 ? -21.628 -8.247  -18.452 1.00 116.68 ? 199 ASN A C   1 
ATOM   1535 O O   . ASN A 1 195 ? -21.177 -8.341  -19.596 1.00 117.31 ? 199 ASN A O   1 
ATOM   1536 C CB  . ASN A 1 195 ? -21.608 -10.765 -18.220 1.00 133.51 ? 199 ASN A CB  1 
ATOM   1537 C CG  . ASN A 1 195 ? -22.308 -11.989 -17.658 1.00 139.17 ? 199 ASN A CG  1 
ATOM   1538 O OD1 . ASN A 1 195 ? -22.658 -12.031 -16.478 1.00 139.63 ? 199 ASN A OD1 1 
ATOM   1539 N ND2 . ASN A 1 195 ? -22.522 -12.989 -18.505 1.00 139.00 ? 199 ASN A ND2 1 
ATOM   1540 N N   . ALA A 1 196 ? -21.602 -7.115  -17.756 1.00 87.15  ? 200 ALA A N   1 
ATOM   1541 C CA  . ALA A 1 196 ? -21.073 -5.876  -18.302 1.00 85.99  ? 200 ALA A CA  1 
ATOM   1542 C C   . ALA A 1 196 ? -19.615 -5.695  -17.889 1.00 83.08  ? 200 ALA A C   1 
ATOM   1543 O O   . ALA A 1 196 ? -19.041 -6.499  -17.151 1.00 81.93  ? 200 ALA A O   1 
ATOM   1544 C CB  . ALA A 1 196 ? -21.923 -4.686  -17.853 1.00 85.57  ? 200 ALA A CB  1 
ATOM   1545 N N   . TYR A 1 197 ? -19.009 -4.614  -18.377 1.00 85.23  ? 201 TYR A N   1 
ATOM   1546 C CA  . TYR A 1 197 ? -17.615 -4.325  -18.078 1.00 85.48  ? 201 TYR A CA  1 
ATOM   1547 C C   . TYR A 1 197 ? -17.366 -2.837  -18.262 1.00 86.21  ? 201 TYR A C   1 
ATOM   1548 O O   . TYR A 1 197 ? -18.032 -2.178  -19.064 1.00 88.19  ? 201 TYR A O   1 
ATOM   1549 C CB  . TYR A 1 197 ? -16.667 -5.130  -18.975 1.00 89.54  ? 201 TYR A CB  1 
ATOM   1550 C CG  . TYR A 1 197 ? -16.485 -4.546  -20.362 1.00 98.36  ? 201 TYR A CG  1 
ATOM   1551 C CD1 . TYR A 1 197 ? -17.447 -4.729  -21.347 1.00 110.58 ? 201 TYR A CD1 1 
ATOM   1552 C CD2 . TYR A 1 197 ? -15.348 -3.816  -20.687 1.00 97.08  ? 201 TYR A CD2 1 
ATOM   1553 C CE1 . TYR A 1 197 ? -17.285 -4.197  -22.616 1.00 108.99 ? 201 TYR A CE1 1 
ATOM   1554 C CE2 . TYR A 1 197 ? -15.177 -3.280  -21.953 1.00 97.19  ? 201 TYR A CE2 1 
ATOM   1555 C CZ  . TYR A 1 197 ? -16.148 -3.474  -22.913 1.00 101.22 ? 201 TYR A CZ  1 
ATOM   1556 O OH  . TYR A 1 197 ? -15.983 -2.944  -24.172 1.00 109.77 ? 201 TYR A OH  1 
ATOM   1557 N N   . VAL A 1 198 ? -16.403 -2.316  -17.504 1.00 84.28  ? 202 VAL A N   1 
ATOM   1558 C CA  . VAL A 1 198 ? -15.891 -0.967  -17.709 1.00 74.16  ? 202 VAL A CA  1 
ATOM   1559 C C   . VAL A 1 198 ? -14.381 -1.065  -17.860 1.00 72.70  ? 202 VAL A C   1 
ATOM   1560 O O   . VAL A 1 198 ? -13.733 -1.863  -17.178 1.00 77.71  ? 202 VAL A O   1 
ATOM   1561 C CB  . VAL A 1 198 ? -16.276 -0.017  -16.554 1.00 72.23  ? 202 VAL A CB  1 
ATOM   1562 C CG1 . VAL A 1 198 ? -15.825 1.402   -16.858 1.00 71.31  ? 202 VAL A CG1 1 
ATOM   1563 C CG2 . VAL A 1 198 ? -17.777 -0.050  -16.319 1.00 74.43  ? 202 VAL A CG2 1 
ATOM   1564 N N   . SER A 1 199 ? -13.823 -0.278  -18.775 1.00 85.22  ? 203 SER A N   1 
ATOM   1565 C CA  . SER A 1 199 ? -12.396 -0.332  -19.065 1.00 81.15  ? 203 SER A CA  1 
ATOM   1566 C C   . SER A 1 199 ? -11.880 1.085   -19.233 1.00 77.22  ? 203 SER A C   1 
ATOM   1567 O O   . SER A 1 199 ? -12.338 1.810   -20.122 1.00 91.63  ? 203 SER A O   1 
ATOM   1568 C CB  . SER A 1 199 ? -12.119 -1.161  -20.324 1.00 90.35  ? 203 SER A CB  1 
ATOM   1569 O OG  . SER A 1 199 ? -10.737 -1.168  -20.635 1.00 103.04 ? 203 SER A OG  1 
ATOM   1570 N N   . VAL A 1 200 ? -10.937 1.479   -18.382 1.00 70.56  ? 204 VAL A N   1 
ATOM   1571 C CA  . VAL A 1 200 ? -10.306 2.792   -18.459 1.00 67.35  ? 204 VAL A CA  1 
ATOM   1572 C C   . VAL A 1 200 ? -8.819  2.568   -18.682 1.00 72.34  ? 204 VAL A C   1 
ATOM   1573 O O   . VAL A 1 200 ? -8.170  1.862   -17.899 1.00 67.50  ? 204 VAL A O   1 
ATOM   1574 C CB  . VAL A 1 200 ? -10.552 3.627   -17.192 1.00 65.06  ? 204 VAL A CB  1 
ATOM   1575 C CG1 . VAL A 1 200 ? -10.022 5.041   -17.383 1.00 64.33  ? 204 VAL A CG1 1 
ATOM   1576 C CG2 . VAL A 1 200 ? -12.030 3.641   -16.840 1.00 65.92  ? 204 VAL A CG2 1 
ATOM   1577 N N   . VAL A 1 201 ? -8.277  3.158   -19.746 1.00 81.16  ? 205 VAL A N   1 
ATOM   1578 C CA  . VAL A 1 201 ? -6.870  2.969   -20.084 1.00 80.20  ? 205 VAL A CA  1 
ATOM   1579 C C   . VAL A 1 201 ? -6.250  4.301   -20.485 1.00 75.07  ? 205 VAL A C   1 
ATOM   1580 O O   . VAL A 1 201 ? -6.875  5.097   -21.198 1.00 81.44  ? 205 VAL A O   1 
ATOM   1581 C CB  . VAL A 1 201 ? -6.683  1.922   -21.204 1.00 82.72  ? 205 VAL A CB  1 
ATOM   1582 C CG1 . VAL A 1 201 ? -6.808  0.514   -20.641 1.00 82.17  ? 205 VAL A CG1 1 
ATOM   1583 C CG2 . VAL A 1 201 ? -7.696  2.146   -22.319 1.00 94.78  ? 205 VAL A CG2 1 
ATOM   1584 N N   . SER A 1 202 ? -5.033  4.539   -20.029 1.00 77.32  ? 206 SER A N   1 
ATOM   1585 C CA  . SER A 1 202 ? -4.241  5.681   -20.475 1.00 85.08  ? 206 SER A CA  1 
ATOM   1586 C C   . SER A 1 202 ? -2.896  5.135   -20.948 1.00 106.02 ? 206 SER A C   1 
ATOM   1587 O O   . SER A 1 202 ? -2.739  3.941   -21.229 1.00 115.61 ? 206 SER A O   1 
ATOM   1588 C CB  . SER A 1 202 ? -4.091  6.729   -19.366 1.00 76.32  ? 206 SER A CB  1 
ATOM   1589 O OG  . SER A 1 202 ? -3.084  6.351   -18.447 1.00 76.52  ? 206 SER A OG  1 
ATOM   1590 N N   . SER A 1 203 ? -1.896  6.015   -21.039 1.00 129.59 ? 207 SER A N   1 
ATOM   1591 C CA  . SER A 1 203 ? -0.566  5.561   -21.427 1.00 142.04 ? 207 SER A CA  1 
ATOM   1592 C C   . SER A 1 203 ? 0.088   4.741   -20.323 1.00 150.17 ? 207 SER A C   1 
ATOM   1593 O O   . SER A 1 203 ? 0.831   3.795   -20.611 1.00 151.86 ? 207 SER A O   1 
ATOM   1594 C CB  . SER A 1 203 ? 0.314   6.755   -21.798 1.00 141.52 ? 207 SER A CB  1 
ATOM   1595 O OG  . SER A 1 203 ? 0.440   7.658   -20.714 1.00 138.73 ? 207 SER A OG  1 
ATOM   1596 N N   . HIS A 1 204 ? -0.178  5.080   -19.060 1.00 151.38 ? 208 HIS A N   1 
ATOM   1597 C CA  . HIS A 1 204 ? 0.387   4.356   -17.932 1.00 151.53 ? 208 HIS A CA  1 
ATOM   1598 C C   . HIS A 1 204 ? -0.643  3.942   -16.889 1.00 138.96 ? 208 HIS A C   1 
ATOM   1599 O O   . HIS A 1 204 ? -0.282  3.223   -15.949 1.00 142.32 ? 208 HIS A O   1 
ATOM   1600 C CB  . HIS A 1 204 ? 1.488   5.189   -17.258 1.00 157.30 ? 208 HIS A CB  1 
ATOM   1601 C CG  . HIS A 1 204 ? 2.639   5.508   -18.162 1.00 163.87 ? 208 HIS A CG  1 
ATOM   1602 N ND1 . HIS A 1 204 ? 3.496   4.542   -18.645 1.00 166.09 ? 208 HIS A ND1 1 
ATOM   1603 C CD2 . HIS A 1 204 ? 3.074   6.685   -18.673 1.00 165.91 ? 208 HIS A CD2 1 
ATOM   1604 C CE1 . HIS A 1 204 ? 4.408   5.110   -19.414 1.00 167.75 ? 208 HIS A CE1 1 
ATOM   1605 N NE2 . HIS A 1 204 ? 4.175   6.410   -19.447 1.00 167.72 ? 208 HIS A NE2 1 
ATOM   1606 N N   . TYR A 1 205 ? -1.898  4.365   -17.016 1.00 110.22 ? 209 TYR A N   1 
ATOM   1607 C CA  . TYR A 1 205 ? -2.988  3.866   -16.190 1.00 78.58  ? 209 TYR A CA  1 
ATOM   1608 C C   . TYR A 1 205 ? -3.821  2.882   -16.998 1.00 75.75  ? 209 TYR A C   1 
ATOM   1609 O O   . TYR A 1 205 ? -4.113  3.119   -18.174 1.00 86.42  ? 209 TYR A O   1 
ATOM   1610 C CB  . TYR A 1 205 ? -3.874  5.009   -15.686 1.00 79.81  ? 209 TYR A CB  1 
ATOM   1611 C CG  . TYR A 1 205 ? -5.029  4.564   -14.810 1.00 74.38  ? 209 TYR A CG  1 
ATOM   1612 C CD1 . TYR A 1 205 ? -6.263  4.234   -15.361 1.00 74.41  ? 209 TYR A CD1 1 
ATOM   1613 C CD2 . TYR A 1 205 ? -4.888  4.484   -13.432 1.00 73.41  ? 209 TYR A CD2 1 
ATOM   1614 C CE1 . TYR A 1 205 ? -7.319  3.830   -14.563 1.00 70.61  ? 209 TYR A CE1 1 
ATOM   1615 C CE2 . TYR A 1 205 ? -5.938  4.083   -12.626 1.00 69.90  ? 209 TYR A CE2 1 
ATOM   1616 C CZ  . TYR A 1 205 ? -7.151  3.757   -13.197 1.00 73.71  ? 209 TYR A CZ  1 
ATOM   1617 O OH  . TYR A 1 205 ? -8.198  3.357   -12.399 1.00 66.63  ? 209 TYR A OH  1 
ATOM   1618 N N   . SER A 1 206 ? -4.210  1.782   -16.360 1.00 64.24  ? 210 SER A N   1 
ATOM   1619 C CA  . SER A 1 206 ? -4.968  0.733   -17.037 1.00 67.83  ? 210 SER A CA  1 
ATOM   1620 C C   . SER A 1 206 ? -5.706  -0.081  -15.989 1.00 72.17  ? 210 SER A C   1 
ATOM   1621 O O   . SER A 1 206 ? -5.068  -0.735  -15.157 1.00 74.51  ? 210 SER A O   1 
ATOM   1622 C CB  . SER A 1 206 ? -4.042  -0.161  -17.862 1.00 71.54  ? 210 SER A CB  1 
ATOM   1623 O OG  . SER A 1 206 ? -4.746  -1.263  -18.409 1.00 84.46  ? 210 SER A OG  1 
ATOM   1624 N N   . ARG A 1 207 ? -7.036  -0.048  -16.024 1.00 78.67  ? 211 ARG A N   1 
ATOM   1625 C CA  . ARG A 1 207 ? -7.817  -0.845  -15.092 1.00 74.78  ? 211 ARG A CA  1 
ATOM   1626 C C   . ARG A 1 207 ? -9.148  -1.227  -15.726 1.00 80.16  ? 211 ARG A C   1 
ATOM   1627 O O   . ARG A 1 207 ? -9.698  -0.496  -16.559 1.00 71.78  ? 211 ARG A O   1 
ATOM   1628 C CB  . ARG A 1 207 ? -8.046  -0.110  -13.766 1.00 72.10  ? 211 ARG A CB  1 
ATOM   1629 C CG  . ARG A 1 207 ? -8.550  -1.017  -12.654 1.00 75.33  ? 211 ARG A CG  1 
ATOM   1630 C CD  . ARG A 1 207 ? -8.518  -0.337  -11.301 1.00 88.88  ? 211 ARG A CD  1 
ATOM   1631 N NE  . ARG A 1 207 ? -9.182  -1.146  -10.282 1.00 89.77  ? 211 ARG A NE  1 
ATOM   1632 C CZ  . ARG A 1 207 ? -9.315  -0.784  -9.011  1.00 93.87  ? 211 ARG A CZ  1 
ATOM   1633 N NH1 . ARG A 1 207 ? -8.829  0.379   -8.598  1.00 80.56  ? 211 ARG A NH1 1 
ATOM   1634 N NH2 . ARG A 1 207 ? -9.935  -1.583  -8.153  1.00 101.27 ? 211 ARG A NH2 1 
ATOM   1635 N N   . LYS A 1 208 ? -9.653  -2.388  -15.309 1.00 86.26  ? 212 LYS A N   1 
ATOM   1636 C CA  . LYS A 1 208 ? -10.890 -2.971  -15.807 1.00 85.10  ? 212 LYS A CA  1 
ATOM   1637 C C   . LYS A 1 208 ? -11.769 -3.340  -14.621 1.00 84.59  ? 212 LYS A C   1 
ATOM   1638 O O   . LYS A 1 208 ? -11.339 -4.083  -13.733 1.00 87.24  ? 212 LYS A O   1 
ATOM   1639 C CB  . LYS A 1 208 ? -10.596 -4.207  -16.663 1.00 88.32  ? 212 LYS A CB  1 
ATOM   1640 C CG  . LYS A 1 208 ? -11.814 -4.866  -17.280 1.00 94.28  ? 212 LYS A CG  1 
ATOM   1641 C CD  . LYS A 1 208 ? -11.424 -6.172  -17.955 1.00 92.62  ? 212 LYS A CD  1 
ATOM   1642 C CE  . LYS A 1 208 ? -12.591 -6.787  -18.704 1.00 98.12  ? 212 LYS A CE  1 
ATOM   1643 N NZ  . LYS A 1 208 ? -12.998 -5.957  -19.870 1.00 113.26 ? 212 LYS A NZ  1 
ATOM   1644 N N   . PHE A 1 209 ? -12.993 -2.820  -14.607 1.00 72.18  ? 213 PHE A N   1 
ATOM   1645 C CA  . PHE A 1 209 ? -13.936 -3.016  -13.516 1.00 72.29  ? 213 PHE A CA  1 
ATOM   1646 C C   . PHE A 1 209 ? -15.074 -3.930  -13.954 1.00 74.79  ? 213 PHE A C   1 
ATOM   1647 O O   . PHE A 1 209 ? -15.625 -3.776  -15.053 1.00 72.00  ? 213 PHE A O   1 
ATOM   1648 C CB  . PHE A 1 209 ? -14.506 -1.678  -13.035 1.00 66.23  ? 213 PHE A CB  1 
ATOM   1649 C CG  . PHE A 1 209 ? -13.460 -0.630  -12.768 1.00 66.42  ? 213 PHE A CG  1 
ATOM   1650 C CD1 . PHE A 1 209 ? -12.853 -0.535  -11.528 1.00 66.35  ? 213 PHE A CD1 1 
ATOM   1651 C CD2 . PHE A 1 209 ? -13.090 0.265   -13.758 1.00 64.24  ? 213 PHE A CD2 1 
ATOM   1652 C CE1 . PHE A 1 209 ? -11.894 0.428   -11.285 1.00 72.81  ? 213 PHE A CE1 1 
ATOM   1653 C CE2 . PHE A 1 209 ? -12.132 1.230   -13.518 1.00 63.86  ? 213 PHE A CE2 1 
ATOM   1654 C CZ  . PHE A 1 209 ? -11.534 1.311   -12.281 1.00 73.04  ? 213 PHE A CZ  1 
ATOM   1655 N N   . THR A 1 210 ? -15.421 -4.874  -13.079 1.00 81.07  ? 214 THR A N   1 
ATOM   1656 C CA  . THR A 1 210 ? -16.519 -5.806  -13.258 1.00 87.28  ? 214 THR A CA  1 
ATOM   1657 C C   . THR A 1 210 ? -17.557 -5.579  -12.167 1.00 88.07  ? 214 THR A C   1 
ATOM   1658 O O   . THR A 1 210 ? -17.195 -5.503  -10.984 1.00 94.55  ? 214 THR A O   1 
ATOM   1659 C CB  . THR A 1 210 ? -16.022 -7.264  -13.203 1.00 92.70  ? 214 THR A CB  1 
ATOM   1660 O OG1 . THR A 1 210 ? -14.951 -7.447  -14.137 1.00 99.45  ? 214 THR A OG1 1 
ATOM   1661 C CG2 . THR A 1 210 ? -17.150 -8.233  -13.532 1.00 93.61  ? 214 THR A CG2 1 
ATOM   1662 N N   . PRO A 1 211 ? -18.841 -5.460  -12.509 1.00 77.90  ? 215 PRO A N   1 
ATOM   1663 C CA  . PRO A 1 211 ? -19.863 -5.236  -11.476 1.00 77.51  ? 215 PRO A CA  1 
ATOM   1664 C C   . PRO A 1 211 ? -20.037 -6.466  -10.596 1.00 79.91  ? 215 PRO A C   1 
ATOM   1665 O O   . PRO A 1 211 ? -20.109 -7.594  -11.087 1.00 90.63  ? 215 PRO A O   1 
ATOM   1666 C CB  . PRO A 1 211 ? -21.131 -4.936  -12.288 1.00 85.85  ? 215 PRO A CB  1 
ATOM   1667 C CG  . PRO A 1 211 ? -20.636 -4.540  -13.645 1.00 91.61  ? 215 PRO A CG  1 
ATOM   1668 C CD  . PRO A 1 211 ? -19.400 -5.352  -13.866 1.00 92.10  ? 215 PRO A CD  1 
ATOM   1669 N N   . GLU A 1 212 ? -20.118 -6.235  -9.288  1.00 84.23  ? 216 GLU A N   1 
ATOM   1670 C CA  . GLU A 1 212 ? -20.335 -7.287  -8.301  1.00 87.87  ? 216 GLU A CA  1 
ATOM   1671 C C   . GLU A 1 212 ? -21.743 -7.124  -7.742  1.00 96.43  ? 216 GLU A C   1 
ATOM   1672 O O   . GLU A 1 212 ? -22.039 -6.129  -7.072  1.00 100.04 ? 216 GLU A O   1 
ATOM   1673 C CB  . GLU A 1 212 ? -19.292 -7.217  -7.188  1.00 90.88  ? 216 GLU A CB  1 
ATOM   1674 C CG  . GLU A 1 212 ? -17.878 -6.985  -7.676  1.00 96.26  ? 216 GLU A CG  1 
ATOM   1675 C CD  . GLU A 1 212 ? -16.898 -6.774  -6.540  1.00 106.65 ? 216 GLU A CD  1 
ATOM   1676 O OE1 . GLU A 1 212 ? -17.135 -7.316  -5.440  1.00 110.03 ? 216 GLU A OE1 1 
ATOM   1677 O OE2 . GLU A 1 212 ? -15.894 -6.059  -6.744  1.00 111.79 ? 216 GLU A OE2 1 
ATOM   1678 N N   . ILE A 1 213 ? -22.603 -8.099  -8.013  1.00 99.91  ? 217 ILE A N   1 
ATOM   1679 C CA  . ILE A 1 213 ? -23.999 -8.057  -7.597  1.00 101.28 ? 217 ILE A CA  1 
ATOM   1680 C C   . ILE A 1 213 ? -24.146 -8.880  -6.325  1.00 111.47 ? 217 ILE A C   1 
ATOM   1681 O O   . ILE A 1 213 ? -23.842 -10.080 -6.312  1.00 114.13 ? 217 ILE A O   1 
ATOM   1682 C CB  . ILE A 1 213 ? -24.932 -8.574  -8.704  1.00 102.71 ? 217 ILE A CB  1 
ATOM   1683 C CG1 . ILE A 1 213 ? -25.059 -7.546  -9.832  1.00 104.45 ? 217 ILE A CG1 1 
ATOM   1684 C CG2 . ILE A 1 213 ? -26.300 -8.908  -8.135  1.00 107.01 ? 217 ILE A CG2 1 
ATOM   1685 C CD1 . ILE A 1 213 ? -23.951 -7.610  -10.866 1.00 109.15 ? 217 ILE A CD1 1 
ATOM   1686 N N   . ALA A 1 214 ? -24.611 -8.237  -5.256  1.00 113.23 ? 218 ALA A N   1 
ATOM   1687 C CA  . ALA A 1 214 ? -24.806 -8.909  -3.979  1.00 119.08 ? 218 ALA A CA  1 
ATOM   1688 C C   . ALA A 1 214 ? -25.748 -8.077  -3.123  1.00 121.93 ? 218 ALA A C   1 
ATOM   1689 O O   . ALA A 1 214 ? -25.964 -6.889  -3.378  1.00 114.66 ? 218 ALA A O   1 
ATOM   1690 C CB  . ALA A 1 214 ? -23.477 -9.139  -3.252  1.00 110.41 ? 218 ALA A CB  1 
ATOM   1691 N N   . LYS A 1 215 ? -26.306 -8.720  -2.100  1.00 139.36 ? 219 LYS A N   1 
ATOM   1692 C CA  . LYS A 1 215 ? -27.207 -8.050  -1.171  1.00 141.55 ? 219 LYS A CA  1 
ATOM   1693 C C   . LYS A 1 215 ? -26.386 -7.292  -0.135  1.00 134.15 ? 219 LYS A C   1 
ATOM   1694 O O   . LYS A 1 215 ? -25.620 -7.897  0.623   1.00 138.65 ? 219 LYS A O   1 
ATOM   1695 C CB  . LYS A 1 215 ? -28.131 -9.062  -0.499  1.00 148.15 ? 219 LYS A CB  1 
ATOM   1696 C CG  . LYS A 1 215 ? -28.946 -9.900  -1.471  1.00 151.81 ? 219 LYS A CG  1 
ATOM   1697 C CD  . LYS A 1 215 ? -29.846 -10.879 -0.736  1.00 153.29 ? 219 LYS A CD  1 
ATOM   1698 C CE  . LYS A 1 215 ? -30.661 -11.714 -1.709  1.00 156.17 ? 219 LYS A CE  1 
ATOM   1699 N NZ  . LYS A 1 215 ? -31.582 -12.648 -1.005  1.00 161.42 ? 219 LYS A NZ  1 
ATOM   1700 N N   . ARG A 1 216 ? -26.546 -5.971  -0.102  1.00 122.39 ? 220 ARG A N   1 
ATOM   1701 C CA  . ARG A 1 216 ? -25.742 -5.126  0.763   1.00 101.51 ? 220 ARG A CA  1 
ATOM   1702 C C   . ARG A 1 216 ? -26.627 -4.337  1.722   1.00 95.10  ? 220 ARG A C   1 
ATOM   1703 O O   . ARG A 1 216 ? -27.798 -4.083  1.424   1.00 99.18  ? 220 ARG A O   1 
ATOM   1704 C CB  . ARG A 1 216 ? -24.887 -4.159  -0.065  1.00 93.71  ? 220 ARG A CB  1 
ATOM   1705 C CG  . ARG A 1 216 ? -23.867 -4.856  -0.948  1.00 96.38  ? 220 ARG A CG  1 
ATOM   1706 C CD  . ARG A 1 216 ? -23.029 -3.859  -1.724  1.00 110.02 ? 220 ARG A CD  1 
ATOM   1707 N NE  . ARG A 1 216 ? -22.004 -4.516  -2.530  1.00 116.88 ? 220 ARG A NE  1 
ATOM   1708 C CZ  . ARG A 1 216 ? -22.208 -4.987  -3.755  1.00 105.33 ? 220 ARG A CZ  1 
ATOM   1709 N NH1 . ARG A 1 216 ? -23.404 -4.876  -4.318  1.00 88.82  ? 220 ARG A NH1 1 
ATOM   1710 N NH2 . ARG A 1 216 ? -21.218 -5.570  -4.418  1.00 102.71 ? 220 ARG A NH2 1 
ATOM   1711 N N   . PRO A 1 217 ? -26.101 -3.951  2.885   1.00 88.40  ? 221 PRO A N   1 
ATOM   1712 C CA  . PRO A 1 217 ? -26.907 -3.178  3.836   1.00 89.24  ? 221 PRO A CA  1 
ATOM   1713 C C   . PRO A 1 217 ? -27.323 -1.832  3.261   1.00 98.33  ? 221 PRO A C   1 
ATOM   1714 O O   . PRO A 1 217 ? -26.640 -1.249  2.416   1.00 100.77 ? 221 PRO A O   1 
ATOM   1715 C CB  . PRO A 1 217 ? -25.971 -3.004  5.038   1.00 88.13  ? 221 PRO A CB  1 
ATOM   1716 C CG  . PRO A 1 217 ? -24.994 -4.124  4.922   1.00 88.65  ? 221 PRO A CG  1 
ATOM   1717 C CD  . PRO A 1 217 ? -24.794 -4.327  3.451   1.00 91.74  ? 221 PRO A CD  1 
ATOM   1718 N N   . LYS A 1 218 ? -28.463 -1.341  3.739   1.00 108.32 ? 222 LYS A N   1 
ATOM   1719 C CA  . LYS A 1 218 ? -28.983 -0.059  3.285   1.00 108.22 ? 222 LYS A CA  1 
ATOM   1720 C C   . LYS A 1 218 ? -28.120 1.082   3.807   1.00 106.05 ? 222 LYS A C   1 
ATOM   1721 O O   . LYS A 1 218 ? -27.836 1.163   5.006   1.00 101.06 ? 222 LYS A O   1 
ATOM   1722 C CB  . LYS A 1 218 ? -30.426 0.121   3.755   1.00 111.57 ? 222 LYS A CB  1 
ATOM   1723 C CG  . LYS A 1 218 ? -31.429 -0.816  3.107   1.00 119.52 ? 222 LYS A CG  1 
ATOM   1724 C CD  . LYS A 1 218 ? -31.989 -0.222  1.826   1.00 123.88 ? 222 LYS A CD  1 
ATOM   1725 C CE  . LYS A 1 218 ? -33.194 -1.011  1.339   1.00 121.18 ? 222 LYS A CE  1 
ATOM   1726 N NZ  . LYS A 1 218 ? -33.764 -0.448  0.084   1.00 123.67 ? 222 LYS A NZ  1 
ATOM   1727 N N   . VAL A 1 219 ? -27.700 1.962   2.903   1.00 105.75 ? 223 VAL A N   1 
ATOM   1728 C CA  . VAL A 1 219 ? -27.016 3.202   3.255   1.00 101.99 ? 223 VAL A CA  1 
ATOM   1729 C C   . VAL A 1 219 ? -27.718 4.320   2.501   1.00 107.97 ? 223 VAL A C   1 
ATOM   1730 O O   . VAL A 1 219 ? -27.637 4.387   1.268   1.00 120.11 ? 223 VAL A O   1 
ATOM   1731 C CB  . VAL A 1 219 ? -25.519 3.171   2.917   1.00 88.24  ? 223 VAL A CB  1 
ATOM   1732 C CG1 . VAL A 1 219 ? -24.878 4.508   3.254   1.00 82.54  ? 223 VAL A CG1 1 
ATOM   1733 C CG2 . VAL A 1 219 ? -24.823 2.044   3.664   1.00 88.28  ? 223 VAL A CG2 1 
ATOM   1734 N N   . ARG A 1 220 ? -28.411 5.192   3.236   1.00 95.62  ? 224 ARG A N   1 
ATOM   1735 C CA  . ARG A 1 220 ? -29.204 6.272   2.648   1.00 85.44  ? 224 ARG A CA  1 
ATOM   1736 C C   . ARG A 1 220 ? -30.254 5.712   1.689   1.00 88.35  ? 224 ARG A C   1 
ATOM   1737 O O   . ARG A 1 220 ? -30.421 6.187   0.563   1.00 84.38  ? 224 ARG A O   1 
ATOM   1738 C CB  . ARG A 1 220 ? -28.308 7.302   1.954   1.00 88.75  ? 224 ARG A CB  1 
ATOM   1739 C CG  . ARG A 1 220 ? -27.315 7.979   2.887   1.00 94.03  ? 224 ARG A CG  1 
ATOM   1740 C CD  . ARG A 1 220 ? -26.407 8.939   2.137   1.00 81.02  ? 224 ARG A CD  1 
ATOM   1741 N NE  . ARG A 1 220 ? -27.164 9.935   1.382   1.00 84.78  ? 224 ARG A NE  1 
ATOM   1742 C CZ  . ARG A 1 220 ? -27.612 11.078  1.891   1.00 80.44  ? 224 ARG A CZ  1 
ATOM   1743 N NH1 . ARG A 1 220 ? -28.291 11.924  1.129   1.00 75.24  ? 224 ARG A NH1 1 
ATOM   1744 N NH2 . ARG A 1 220 ? -27.383 11.373  3.163   1.00 68.30  ? 224 ARG A NH2 1 
ATOM   1745 N N   . ASP A 1 221 ? -30.960 4.678   2.154   1.00 93.66  ? 225 ASP A N   1 
ATOM   1746 C CA  . ASP A 1 221 ? -32.037 4.035   1.400   1.00 106.06 ? 225 ASP A CA  1 
ATOM   1747 C C   . ASP A 1 221 ? -31.536 3.509   0.054   1.00 105.92 ? 225 ASP A C   1 
ATOM   1748 O O   . ASP A 1 221 ? -32.160 3.706   -0.991  1.00 111.50 ? 225 ASP A O   1 
ATOM   1749 C CB  . ASP A 1 221 ? -33.223 4.988   1.214   1.00 104.92 ? 225 ASP A CB  1 
ATOM   1750 C CG  . ASP A 1 221 ? -34.469 4.280   0.717   1.00 109.54 ? 225 ASP A CG  1 
ATOM   1751 O OD1 . ASP A 1 221 ? -34.663 3.100   1.076   1.00 112.24 ? 225 ASP A OD1 1 
ATOM   1752 O OD2 . ASP A 1 221 ? -35.251 4.899   -0.036  1.00 109.09 ? 225 ASP A OD2 1 
ATOM   1753 N N   . GLN A 1 222 ? -30.389 2.831   0.085   1.00 96.90  ? 226 GLN A N   1 
ATOM   1754 C CA  . GLN A 1 222 ? -29.817 2.249   -1.123  1.00 89.82  ? 226 GLN A CA  1 
ATOM   1755 C C   . GLN A 1 222 ? -29.104 0.951   -0.775  1.00 87.99  ? 226 GLN A C   1 
ATOM   1756 O O   . GLN A 1 222 ? -28.308 0.913   0.167   1.00 80.96  ? 226 GLN A O   1 
ATOM   1757 C CB  . GLN A 1 222 ? -28.839 3.215   -1.807  1.00 84.06  ? 226 GLN A CB  1 
ATOM   1758 C CG  . GLN A 1 222 ? -29.495 4.345   -2.583  1.00 89.08  ? 226 GLN A CG  1 
ATOM   1759 C CD  . GLN A 1 222 ? -30.400 3.850   -3.696  1.00 100.82 ? 226 GLN A CD  1 
ATOM   1760 O OE1 . GLN A 1 222 ? -30.186 2.776   -4.259  1.00 105.66 ? 226 GLN A OE1 1 
ATOM   1761 N NE2 . GLN A 1 222 ? -31.424 4.635   -4.016  1.00 104.15 ? 226 GLN A NE2 1 
ATOM   1762 N N   . GLU A 1 223 ? -29.392 -0.103  -1.540  1.00 99.91  ? 227 GLU A N   1 
ATOM   1763 C CA  . GLU A 1 223 ? -28.681 -1.369  -1.414  1.00 107.52 ? 227 GLU A CA  1 
ATOM   1764 C C   . GLU A 1 223 ? -27.550 -1.519  -2.420  1.00 107.20 ? 227 GLU A C   1 
ATOM   1765 O O   . GLU A 1 223 ? -26.610 -2.279  -2.162  1.00 103.33 ? 227 GLU A O   1 
ATOM   1766 C CB  . GLU A 1 223 ? -29.649 -2.548  -1.573  1.00 119.01 ? 227 GLU A CB  1 
ATOM   1767 C CG  . GLU A 1 223 ? -30.581 -2.752  -0.393  1.00 128.02 ? 227 GLU A CG  1 
ATOM   1768 C CD  . GLU A 1 223 ? -31.505 -3.940  -0.577  1.00 133.73 ? 227 GLU A CD  1 
ATOM   1769 O OE1 . GLU A 1 223 ? -31.335 -4.684  -1.566  1.00 133.65 ? 227 GLU A OE1 1 
ATOM   1770 O OE2 . GLU A 1 223 ? -32.405 -4.129  0.268   1.00 137.79 ? 227 GLU A OE2 1 
ATOM   1771 N N   . GLY A 1 224 ? -27.620 -0.825  -3.555  1.00 77.39  ? 228 GLY A N   1 
ATOM   1772 C CA  . GLY A 1 224 ? -26.517 -0.825  -4.488  1.00 75.81  ? 228 GLY A CA  1 
ATOM   1773 C C   . GLY A 1 224 ? -25.448 0.182   -4.114  1.00 78.98  ? 228 GLY A C   1 
ATOM   1774 O O   . GLY A 1 224 ? -25.665 1.106   -3.331  1.00 72.02  ? 228 GLY A O   1 
ATOM   1775 N N   . ARG A 1 225 ? -24.265 -0.008  -4.686  1.00 76.65  ? 229 ARG A N   1 
ATOM   1776 C CA  . ARG A 1 225 ? -23.127 0.858   -4.425  1.00 71.73  ? 229 ARG A CA  1 
ATOM   1777 C C   . ARG A 1 225 ? -22.651 1.498   -5.721  1.00 68.04  ? 229 ARG A C   1 
ATOM   1778 O O   . ARG A 1 225 ? -23.069 1.127   -6.819  1.00 69.95  ? 229 ARG A O   1 
ATOM   1779 C CB  . ARG A 1 225 ? -21.978 0.082   -3.769  1.00 66.30  ? 229 ARG A CB  1 
ATOM   1780 C CG  . ARG A 1 225 ? -22.282 -0.440  -2.378  1.00 66.28  ? 229 ARG A CG  1 
ATOM   1781 C CD  . ARG A 1 225 ? -22.469 0.689   -1.381  1.00 65.19  ? 229 ARG A CD  1 
ATOM   1782 N NE  . ARG A 1 225 ? -22.713 0.176   -0.036  1.00 65.28  ? 229 ARG A NE  1 
ATOM   1783 C CZ  . ARG A 1 225 ? -23.916 -0.127  0.438   1.00 67.47  ? 229 ARG A CZ  1 
ATOM   1784 N NH1 . ARG A 1 225 ? -24.988 0.034   -0.325  1.00 69.73  ? 229 ARG A NH1 1 
ATOM   1785 N NH2 . ARG A 1 225 ? -24.049 -0.591  1.673   1.00 69.76  ? 229 ARG A NH2 1 
ATOM   1786 N N   . ILE A 1 226 ? -21.771 2.484   -5.574  1.00 65.83  ? 230 ILE A N   1 
ATOM   1787 C CA  . ILE A 1 226 ? -21.063 3.095   -6.693  1.00 65.31  ? 230 ILE A CA  1 
ATOM   1788 C C   . ILE A 1 226 ? -19.626 3.302   -6.239  1.00 62.48  ? 230 ILE A C   1 
ATOM   1789 O O   . ILE A 1 226 ? -19.356 4.178   -5.411  1.00 60.88  ? 230 ILE A O   1 
ATOM   1790 C CB  . ILE A 1 226 ? -21.683 4.427   -7.143  1.00 66.13  ? 230 ILE A CB  1 
ATOM   1791 C CG1 . ILE A 1 226 ? -23.059 4.199   -7.769  1.00 69.21  ? 230 ILE A CG1 1 
ATOM   1792 C CG2 . ILE A 1 226 ? -20.767 5.133   -8.134  1.00 65.32  ? 230 ILE A CG2 1 
ATOM   1793 C CD1 . ILE A 1 226 ? -23.702 5.459   -8.302  1.00 70.39  ? 230 ILE A CD1 1 
ATOM   1794 N N   . ASN A 1 227 ? -18.709 2.491   -6.756  1.00 67.82  ? 231 ASN A N   1 
ATOM   1795 C CA  . ASN A 1 227 ? -17.300 2.668   -6.443  1.00 59.55  ? 231 ASN A CA  1 
ATOM   1796 C C   . ASN A 1 227 ? -16.735 3.812   -7.272  1.00 58.96  ? 231 ASN A C   1 
ATOM   1797 O O   . ASN A 1 227 ? -16.871 3.829   -8.499  1.00 60.41  ? 231 ASN A O   1 
ATOM   1798 C CB  . ASN A 1 227 ? -16.522 1.379   -6.703  1.00 61.82  ? 231 ASN A CB  1 
ATOM   1799 C CG  . ASN A 1 227 ? -16.778 0.325   -5.648  1.00 66.64  ? 231 ASN A CG  1 
ATOM   1800 O OD1 . ASN A 1 227 ? -17.176 0.638   -4.526  1.00 65.05  ? 231 ASN A OD1 1 
ATOM   1801 N ND2 . ASN A 1 227 ? -16.546 -0.935  -6.001  1.00 71.59  ? 231 ASN A ND2 1 
ATOM   1802 N N   . TYR A 1 228 ? -16.110 4.772   -6.599  1.00 56.98  ? 232 TYR A N   1 
ATOM   1803 C CA  . TYR A 1 228 ? -15.586 5.966   -7.245  1.00 56.43  ? 232 TYR A CA  1 
ATOM   1804 C C   . TYR A 1 228 ? -14.097 5.807   -7.522  1.00 54.88  ? 232 TYR A C   1 
ATOM   1805 O O   . TYR A 1 228 ? -13.353 5.269   -6.697  1.00 53.34  ? 232 TYR A O   1 
ATOM   1806 C CB  . TYR A 1 228 ? -15.837 7.202   -6.379  1.00 55.46  ? 232 TYR A CB  1 
ATOM   1807 C CG  . TYR A 1 228 ? -17.293 7.396   -6.023  1.00 57.09  ? 232 TYR A CG  1 
ATOM   1808 C CD1 . TYR A 1 228 ? -18.166 8.021   -6.903  1.00 59.07  ? 232 TYR A CD1 1 
ATOM   1809 C CD2 . TYR A 1 228 ? -17.798 6.945   -4.811  1.00 56.86  ? 232 TYR A CD2 1 
ATOM   1810 C CE1 . TYR A 1 228 ? -19.501 8.197   -6.585  1.00 60.77  ? 232 TYR A CE1 1 
ATOM   1811 C CE2 . TYR A 1 228 ? -19.132 7.118   -4.482  1.00 58.55  ? 232 TYR A CE2 1 
ATOM   1812 C CZ  . TYR A 1 228 ? -19.980 7.743   -5.373  1.00 63.12  ? 232 TYR A CZ  1 
ATOM   1813 O OH  . TYR A 1 228 ? -21.308 7.916   -5.053  1.00 62.37  ? 232 TYR A OH  1 
ATOM   1814 N N   . TYR A 1 229 ? -13.672 6.279   -8.693  1.00 55.47  ? 233 TYR A N   1 
ATOM   1815 C CA  . TYR A 1 229 ? -12.289 6.158   -9.127  1.00 54.42  ? 233 TYR A CA  1 
ATOM   1816 C C   . TYR A 1 229 ? -11.859 7.457   -9.792  1.00 54.32  ? 233 TYR A C   1 
ATOM   1817 O O   . TYR A 1 229 ? -12.682 8.222   -10.299 1.00 55.67  ? 233 TYR A O   1 
ATOM   1818 C CB  . TYR A 1 229 ? -12.107 4.973   -10.085 1.00 55.84  ? 233 TYR A CB  1 
ATOM   1819 C CG  . TYR A 1 229 ? -12.557 3.652   -9.504  1.00 56.25  ? 233 TYR A CG  1 
ATOM   1820 C CD1 . TYR A 1 229 ? -11.724 2.921   -8.669  1.00 54.95  ? 233 TYR A CD1 1 
ATOM   1821 C CD2 . TYR A 1 229 ? -13.817 3.142   -9.783  1.00 58.28  ? 233 TYR A CD2 1 
ATOM   1822 C CE1 . TYR A 1 229 ? -12.131 1.717   -8.129  1.00 60.06  ? 233 TYR A CE1 1 
ATOM   1823 C CE2 . TYR A 1 229 ? -14.232 1.938   -9.250  1.00 58.84  ? 233 TYR A CE2 1 
ATOM   1824 C CZ  . TYR A 1 229 ? -13.387 1.230   -8.423  1.00 60.13  ? 233 TYR A CZ  1 
ATOM   1825 O OH  . TYR A 1 229 ? -13.797 0.029   -7.890  1.00 66.16  ? 233 TYR A OH  1 
ATOM   1826 N N   . TRP A 1 230 ? -10.551 7.699   -9.784  1.00 52.87  ? 234 TRP A N   1 
ATOM   1827 C CA  . TRP A 1 230 ? -9.998  8.929   -10.327 1.00 52.71  ? 234 TRP A CA  1 
ATOM   1828 C C   . TRP A 1 230 ? -8.606  8.653   -10.872 1.00 52.18  ? 234 TRP A C   1 
ATOM   1829 O O   . TRP A 1 230 ? -8.001  7.617   -10.586 1.00 51.54  ? 234 TRP A O   1 
ATOM   1830 C CB  . TRP A 1 230 ? -9.944  10.032  -9.264  1.00 51.10  ? 234 TRP A CB  1 
ATOM   1831 C CG  . TRP A 1 230 ? -9.083  9.680   -8.089  1.00 48.90  ? 234 TRP A CG  1 
ATOM   1832 C CD1 . TRP A 1 230 ? -9.465  9.007   -6.966  1.00 48.13  ? 234 TRP A CD1 1 
ATOM   1833 C CD2 . TRP A 1 230 ? -7.689  9.972   -7.928  1.00 51.18  ? 234 TRP A CD2 1 
ATOM   1834 N NE1 . TRP A 1 230 ? -8.396  8.865   -6.115  1.00 46.23  ? 234 TRP A NE1 1 
ATOM   1835 C CE2 . TRP A 1 230 ? -7.294  9.448   -6.682  1.00 45.72  ? 234 TRP A CE2 1 
ATOM   1836 C CE3 . TRP A 1 230 ? -6.737  10.626  -8.715  1.00 47.43  ? 234 TRP A CE3 1 
ATOM   1837 C CZ2 . TRP A 1 230 ? -5.990  9.558   -6.205  1.00 48.61  ? 234 TRP A CZ2 1 
ATOM   1838 C CZ3 . TRP A 1 230 ? -5.444  10.734  -8.240  1.00 45.82  ? 234 TRP A CZ3 1 
ATOM   1839 C CH2 . TRP A 1 230 ? -5.082  10.203  -6.997  1.00 44.17  ? 234 TRP A CH2 1 
ATOM   1840 N N   . THR A 1 231 ? -8.103  9.598   -11.663 1.00 52.64  ? 235 THR A N   1 
ATOM   1841 C CA  . THR A 1 231 ? -6.757  9.497   -12.206 1.00 52.32  ? 235 THR A CA  1 
ATOM   1842 C C   . THR A 1 231 ? -6.295  10.873  -12.654 1.00 52.44  ? 235 THR A C   1 
ATOM   1843 O O   . THR A 1 231 ? -7.103  11.761  -12.949 1.00 53.85  ? 235 THR A O   1 
ATOM   1844 C CB  . THR A 1 231 ? -6.680  8.511   -13.377 1.00 55.60  ? 235 THR A CB  1 
ATOM   1845 O OG1 . THR A 1 231 ? -5.315  8.363   -13.785 1.00 58.43  ? 235 THR A OG1 1 
ATOM   1846 C CG2 . THR A 1 231 ? -7.497  9.015   -14.556 1.00 63.14  ? 235 THR A CG2 1 
ATOM   1847 N N   . LEU A 1 232 ? -4.976  11.034  -12.694 1.00 51.55  ? 236 LEU A N   1 
ATOM   1848 C CA  . LEU A 1 232 ? -4.339  12.232  -13.219 1.00 51.87  ? 236 LEU A CA  1 
ATOM   1849 C C   . LEU A 1 232 ? -3.861  11.962  -14.637 1.00 55.05  ? 236 LEU A C   1 
ATOM   1850 O O   . LEU A 1 232 ? -3.219  10.939  -14.898 1.00 60.07  ? 236 LEU A O   1 
ATOM   1851 C CB  . LEU A 1 232 ? -3.162  12.667  -12.347 1.00 50.21  ? 236 LEU A CB  1 
ATOM   1852 C CG  . LEU A 1 232 ? -3.492  13.266  -10.982 1.00 47.99  ? 236 LEU A CG  1 
ATOM   1853 C CD1 . LEU A 1 232 ? -2.220  13.772  -10.326 1.00 46.95  ? 236 LEU A CD1 1 
ATOM   1854 C CD2 . LEU A 1 232 ? -4.513  14.381  -11.122 1.00 48.90  ? 236 LEU A CD2 1 
ATOM   1855 N N   . LEU A 1 233 ? -4.171  12.880  -15.545 1.00 65.80  ? 237 LEU A N   1 
ATOM   1856 C CA  . LEU A 1 233 ? -3.824  12.760  -16.954 1.00 66.09  ? 237 LEU A CA  1 
ATOM   1857 C C   . LEU A 1 233 ? -2.743  13.787  -17.259 1.00 66.75  ? 237 LEU A C   1 
ATOM   1858 O O   . LEU A 1 233 ? -2.979  14.997  -17.148 1.00 67.68  ? 237 LEU A O   1 
ATOM   1859 C CB  . LEU A 1 233 ? -5.054  12.963  -17.835 1.00 64.82  ? 237 LEU A CB  1 
ATOM   1860 C CG  . LEU A 1 233 ? -4.906  12.541  -19.294 1.00 75.80  ? 237 LEU A CG  1 
ATOM   1861 C CD1 . LEU A 1 233 ? -4.593  11.055  -19.385 1.00 78.43  ? 237 LEU A CD1 1 
ATOM   1862 C CD2 . LEU A 1 233 ? -6.164  12.876  -20.076 1.00 65.12  ? 237 LEU A CD2 1 
ATOM   1863 N N   . GLU A 1 234 ? -1.562  13.297  -17.627 1.00 73.41  ? 238 GLU A N   1 
ATOM   1864 C CA  . GLU A 1 234 ? -0.445  14.172  -17.935 1.00 77.80  ? 238 GLU A CA  1 
ATOM   1865 C C   . GLU A 1 234 ? -0.756  15.000  -19.183 1.00 83.24  ? 238 GLU A C   1 
ATOM   1866 O O   . GLU A 1 234 ? -1.576  14.599  -20.015 1.00 73.27  ? 238 GLU A O   1 
ATOM   1867 C CB  . GLU A 1 234 ? 0.823   13.351  -18.162 1.00 89.19  ? 238 GLU A CB  1 
ATOM   1868 C CG  . GLU A 1 234 ? 1.147   12.361  -17.053 1.00 93.83  ? 238 GLU A CG  1 
ATOM   1869 C CD  . GLU A 1 234 ? 2.028   12.957  -15.973 1.00 96.98  ? 238 GLU A CD  1 
ATOM   1870 O OE1 . GLU A 1 234 ? 2.103   14.201  -15.876 1.00 96.37  ? 238 GLU A OE1 1 
ATOM   1871 O OE2 . GLU A 1 234 ? 2.654   12.178  -15.224 1.00 103.78 ? 238 GLU A OE2 1 
ATOM   1872 N N   . PRO A 1 235 ? -0.126  16.164  -19.335 1.00 86.60  ? 239 PRO A N   1 
ATOM   1873 C CA  . PRO A 1 235 ? -0.305  16.944  -20.569 1.00 81.71  ? 239 PRO A CA  1 
ATOM   1874 C C   . PRO A 1 235 ? 0.156   16.156  -21.785 1.00 87.81  ? 239 PRO A C   1 
ATOM   1875 O O   . PRO A 1 235 ? 1.317   15.753  -21.885 1.00 86.26  ? 239 PRO A O   1 
ATOM   1876 C CB  . PRO A 1 235 ? 0.564   18.184  -20.330 1.00 83.31  ? 239 PRO A CB  1 
ATOM   1877 C CG  . PRO A 1 235 ? 0.662   18.298  -18.846 1.00 88.48  ? 239 PRO A CG  1 
ATOM   1878 C CD  . PRO A 1 235 ? 0.668   16.890  -18.331 1.00 76.06  ? 239 PRO A CD  1 
ATOM   1879 N N   . GLY A 1 236 ? -0.774  15.930  -22.712 1.00 95.09  ? 240 GLY A N   1 
ATOM   1880 C CA  . GLY A 1 236 ? -0.490  15.239  -23.950 1.00 84.17  ? 240 GLY A CA  1 
ATOM   1881 C C   . GLY A 1 236 ? -0.982  13.809  -24.015 1.00 83.76  ? 240 GLY A C   1 
ATOM   1882 O O   . GLY A 1 236 ? -0.979  13.220  -25.103 1.00 82.12  ? 240 GLY A O   1 
ATOM   1883 N N   . ASP A 1 237 ? -1.402  13.235  -22.894 1.00 87.01  ? 241 ASP A N   1 
ATOM   1884 C CA  . ASP A 1 237 ? -1.860  11.856  -22.869 1.00 85.23  ? 241 ASP A CA  1 
ATOM   1885 C C   . ASP A 1 237 ? -3.344  11.779  -23.214 1.00 78.06  ? 241 ASP A C   1 
ATOM   1886 O O   . ASP A 1 237 ? -4.097  12.743  -23.059 1.00 76.62  ? 241 ASP A O   1 
ATOM   1887 C CB  . ASP A 1 237 ? -1.597  11.229  -21.498 1.00 93.41  ? 241 ASP A CB  1 
ATOM   1888 C CG  . ASP A 1 237 ? -1.801  9.728   -21.495 1.00 98.99  ? 241 ASP A CG  1 
ATOM   1889 O OD1 . ASP A 1 237 ? -1.836  9.129   -22.591 1.00 97.56  ? 241 ASP A OD1 1 
ATOM   1890 O OD2 . ASP A 1 237 ? -1.920  9.144   -20.397 1.00 100.23 ? 241 ASP A OD2 1 
ATOM   1891 N N   . THR A 1 238 ? -3.756  10.610  -23.695 1.00 73.07  ? 242 THR A N   1 
ATOM   1892 C CA  . THR A 1 238 ? -5.133  10.354  -24.091 1.00 78.78  ? 242 THR A CA  1 
ATOM   1893 C C   . THR A 1 238 ? -5.709  9.257   -23.208 1.00 80.50  ? 242 THR A C   1 
ATOM   1894 O O   . THR A 1 238 ? -5.085  8.205   -23.033 1.00 82.80  ? 242 THR A O   1 
ATOM   1895 C CB  . THR A 1 238 ? -5.214  9.947   -25.565 1.00 76.75  ? 242 THR A CB  1 
ATOM   1896 O OG1 . THR A 1 238 ? -4.686  10.999  -26.381 1.00 78.68  ? 242 THR A OG1 1 
ATOM   1897 C CG2 . THR A 1 238 ? -6.655  9.670   -25.969 1.00 77.77  ? 242 THR A CG2 1 
ATOM   1898 N N   . ILE A 1 239 ? -6.893  9.505   -22.653 1.00 80.53  ? 243 ILE A N   1 
ATOM   1899 C CA  . ILE A 1 239 ? -7.580  8.543   -21.801 1.00 75.52  ? 243 ILE A CA  1 
ATOM   1900 C C   . ILE A 1 239 ? -8.751  7.959   -22.579 1.00 79.34  ? 243 ILE A C   1 
ATOM   1901 O O   . ILE A 1 239 ? -9.472  8.681   -23.278 1.00 74.09  ? 243 ILE A O   1 
ATOM   1902 C CB  . ILE A 1 239 ? -8.045  9.180   -20.475 1.00 74.14  ? 243 ILE A CB  1 
ATOM   1903 C CG1 . ILE A 1 239 ? -8.733  8.138   -19.591 1.00 68.53  ? 243 ILE A CG1 1 
ATOM   1904 C CG2 . ILE A 1 239 ? -8.954  10.378  -20.727 1.00 75.05  ? 243 ILE A CG2 1 
ATOM   1905 C CD1 . ILE A 1 239 ? -9.016  8.617   -18.187 1.00 63.92  ? 243 ILE A CD1 1 
ATOM   1906 N N   . ILE A 1 240 ? -8.929  6.645   -22.468 1.00 79.18  ? 244 ILE A N   1 
ATOM   1907 C CA  . ILE A 1 240 ? -9.916  5.908   -23.245 1.00 81.58  ? 244 ILE A CA  1 
ATOM   1908 C C   . ILE A 1 240 ? -10.850 5.185   -22.286 1.00 77.42  ? 244 ILE A C   1 
ATOM   1909 O O   . ILE A 1 240 ? -10.399 4.406   -21.432 1.00 72.16  ? 244 ILE A O   1 
ATOM   1910 C CB  . ILE A 1 240 ? -9.258  4.917   -24.216 1.00 80.04  ? 244 ILE A CB  1 
ATOM   1911 C CG1 . ILE A 1 240 ? -8.331  5.653   -25.184 1.00 81.56  ? 244 ILE A CG1 1 
ATOM   1912 C CG2 . ILE A 1 240 ? -10.320 4.141   -24.979 1.00 82.38  ? 244 ILE A CG2 1 
ATOM   1913 C CD1 . ILE A 1 240 ? -7.656  4.747   -26.189 1.00 94.23  ? 244 ILE A CD1 1 
ATOM   1914 N N   . PHE A 1 241 ? -12.146 5.454   -22.430 1.00 75.73  ? 245 PHE A N   1 
ATOM   1915 C CA  . PHE A 1 241 ? -13.216 4.756   -21.732 1.00 75.35  ? 245 PHE A CA  1 
ATOM   1916 C C   . PHE A 1 241 ? -13.937 3.841   -22.714 1.00 78.32  ? 245 PHE A C   1 
ATOM   1917 O O   . PHE A 1 241 ? -14.390 4.294   -23.771 1.00 81.56  ? 245 PHE A O   1 
ATOM   1918 C CB  . PHE A 1 241 ? -14.220 5.743   -21.130 1.00 75.03  ? 245 PHE A CB  1 
ATOM   1919 C CG  . PHE A 1 241 ? -13.694 6.521   -19.959 1.00 72.09  ? 245 PHE A CG  1 
ATOM   1920 C CD1 . PHE A 1 241 ? -12.889 7.632   -20.149 1.00 71.35  ? 245 PHE A CD1 1 
ATOM   1921 C CD2 . PHE A 1 241 ? -14.029 6.157   -18.666 1.00 70.26  ? 245 PHE A CD2 1 
ATOM   1922 C CE1 . PHE A 1 241 ? -12.415 8.354   -19.070 1.00 72.65  ? 245 PHE A CE1 1 
ATOM   1923 C CE2 . PHE A 1 241 ? -13.557 6.874   -17.584 1.00 67.71  ? 245 PHE A CE2 1 
ATOM   1924 C CZ  . PHE A 1 241 ? -12.749 7.973   -17.786 1.00 66.94  ? 245 PHE A CZ  1 
ATOM   1925 N N   . GLU A 1 242 ? -14.044 2.562   -22.363 1.00 80.36  ? 246 GLU A N   1 
ATOM   1926 C CA  . GLU A 1 242 ? -14.853 1.609   -23.112 1.00 93.51  ? 246 GLU A CA  1 
ATOM   1927 C C   . GLU A 1 242 ? -15.791 0.910   -22.142 1.00 98.38  ? 246 GLU A C   1 
ATOM   1928 O O   . GLU A 1 242 ? -15.339 0.339   -21.146 1.00 97.94  ? 246 GLU A O   1 
ATOM   1929 C CB  . GLU A 1 242 ? -13.987 0.579   -23.842 1.00 100.13 ? 246 GLU A CB  1 
ATOM   1930 C CG  . GLU A 1 242 ? -13.129 1.160   -24.945 1.00 103.26 ? 246 GLU A CG  1 
ATOM   1931 C CD  . GLU A 1 242 ? -12.376 0.094   -25.711 1.00 106.33 ? 246 GLU A CD  1 
ATOM   1932 O OE1 . GLU A 1 242 ? -12.331 -1.062  -25.241 1.00 104.79 ? 246 GLU A OE1 1 
ATOM   1933 O OE2 . GLU A 1 242 ? -11.833 0.412   -26.789 1.00 111.54 ? 246 GLU A OE2 1 
ATOM   1934 N N   . ALA A 1 243 ? -17.090 0.951   -22.430 1.00 82.71  ? 247 ALA A N   1 
ATOM   1935 C CA  . ALA A 1 243 ? -18.062 0.379   -21.512 1.00 82.57  ? 247 ALA A CA  1 
ATOM   1936 C C   . ALA A 1 243 ? -19.300 -0.072  -22.270 1.00 104.00 ? 247 ALA A C   1 
ATOM   1937 O O   . ALA A 1 243 ? -19.621 0.451   -23.341 1.00 101.01 ? 247 ALA A O   1 
ATOM   1938 C CB  . ALA A 1 243 ? -18.455 1.379   -20.419 1.00 80.63  ? 247 ALA A CB  1 
ATOM   1939 N N   . ASN A 1 244 ? -19.990 -1.060  -21.695 1.00 105.90 ? 248 ASN A N   1 
ATOM   1940 C CA  . ASN A 1 244 ? -21.288 -1.502  -22.185 1.00 104.19 ? 248 ASN A CA  1 
ATOM   1941 C C   . ASN A 1 244 ? -22.337 -1.497  -21.081 1.00 104.77 ? 248 ASN A C   1 
ATOM   1942 O O   . ASN A 1 244 ? -23.406 -2.091  -21.254 1.00 108.09 ? 248 ASN A O   1 
ATOM   1943 C CB  . ASN A 1 244 ? -21.187 -2.899  -22.810 1.00 105.32 ? 248 ASN A CB  1 
ATOM   1944 C CG  . ASN A 1 244 ? -20.826 -3.968  -21.797 1.00 104.91 ? 248 ASN A CG  1 
ATOM   1945 O OD1 . ASN A 1 244 ? -20.295 -3.675  -20.727 1.00 110.80 ? 248 ASN A OD1 1 
ATOM   1946 N ND2 . ASN A 1 244 ? -21.109 -5.221  -22.135 1.00 106.43 ? 248 ASN A ND2 1 
ATOM   1947 N N   . GLY A 1 245 ? -22.060 -0.851  -19.960 1.00 95.57  ? 249 GLY A N   1 
ATOM   1948 C CA  . GLY A 1 245 ? -22.994 -0.791  -18.857 1.00 92.86  ? 249 GLY A CA  1 
ATOM   1949 C C   . GLY A 1 245 ? -22.282 -0.534  -17.552 1.00 84.26  ? 249 GLY A C   1 
ATOM   1950 O O   . GLY A 1 245 ? -21.078 -0.756  -17.411 1.00 91.00  ? 249 GLY A O   1 
ATOM   1951 N N   . ASN A 1 246 ? -23.055 -0.034  -16.585 1.00 85.65  ? 250 ASN A N   1 
ATOM   1952 C CA  . ASN A 1 246 ? -22.591 0.184   -15.213 1.00 86.06  ? 250 ASN A CA  1 
ATOM   1953 C C   . ASN A 1 246 ? -21.471 1.218   -15.136 1.00 85.90  ? 250 ASN A C   1 
ATOM   1954 O O   . ASN A 1 246 ? -20.669 1.209   -14.199 1.00 81.65  ? 250 ASN A O   1 
ATOM   1955 C CB  . ASN A 1 246 ? -22.147 -1.130  -14.565 1.00 92.08  ? 250 ASN A CB  1 
ATOM   1956 C CG  . ASN A 1 246 ? -23.256 -2.159  -14.521 1.00 99.51  ? 250 ASN A CG  1 
ATOM   1957 O OD1 . ASN A 1 246 ? -23.506 -2.862  -15.500 1.00 104.43 ? 250 ASN A OD1 1 
ATOM   1958 N ND2 . ASN A 1 246 ? -23.931 -2.252  -13.381 1.00 102.72 ? 250 ASN A ND2 1 
ATOM   1959 N N   . LEU A 1 247 ? -21.414 2.126   -16.106 1.00 94.83  ? 251 LEU A N   1 
ATOM   1960 C CA  . LEU A 1 247 ? -20.426 3.197   -16.120 1.00 75.67  ? 251 LEU A CA  1 
ATOM   1961 C C   . LEU A 1 247 ? -21.086 4.508   -15.711 1.00 75.59  ? 251 LEU A C   1 
ATOM   1962 O O   . LEU A 1 247 ? -21.990 4.993   -16.399 1.00 77.90  ? 251 LEU A O   1 
ATOM   1963 C CB  . LEU A 1 247 ? -19.786 3.344   -17.500 1.00 76.78  ? 251 LEU A CB  1 
ATOM   1964 C CG  . LEU A 1 247 ? -18.968 4.631   -17.674 1.00 75.40  ? 251 LEU A CG  1 
ATOM   1965 C CD1 . LEU A 1 247 ? -17.723 4.609   -16.797 1.00 72.26  ? 251 LEU A CD1 1 
ATOM   1966 C CD2 . LEU A 1 247 ? -18.603 4.867   -19.131 1.00 77.23  ? 251 LEU A CD2 1 
ATOM   1967 N N   . ILE A 1 248 ? -20.634 5.075   -14.596 1.00 84.95  ? 252 ILE A N   1 
ATOM   1968 C CA  . ILE A 1 248 ? -20.990 6.436   -14.213 1.00 72.69  ? 252 ILE A CA  1 
ATOM   1969 C C   . ILE A 1 248 ? -19.994 7.346   -14.924 1.00 71.95  ? 252 ILE A C   1 
ATOM   1970 O O   . ILE A 1 248 ? -18.896 7.596   -14.426 1.00 69.53  ? 252 ILE A O   1 
ATOM   1971 C CB  . ILE A 1 248 ? -20.962 6.629   -12.697 1.00 70.53  ? 252 ILE A CB  1 
ATOM   1972 C CG1 . ILE A 1 248 ? -21.771 5.535   -12.001 1.00 71.26  ? 252 ILE A CG1 1 
ATOM   1973 C CG2 . ILE A 1 248 ? -21.502 8.004   -12.327 1.00 70.62  ? 252 ILE A CG2 1 
ATOM   1974 C CD1 . ILE A 1 248 ? -23.221 5.472   -12.431 1.00 74.28  ? 252 ILE A CD1 1 
ATOM   1975 N N   . ALA A 1 249 ? -20.381 7.832   -16.100 1.00 80.05  ? 253 ALA A N   1 
ATOM   1976 C CA  . ALA A 1 249 ? -19.453 8.515   -16.983 1.00 74.13  ? 253 ALA A CA  1 
ATOM   1977 C C   . ALA A 1 249 ? -18.994 9.846   -16.387 1.00 72.39  ? 253 ALA A C   1 
ATOM   1978 O O   . ALA A 1 249 ? -19.705 10.460  -15.586 1.00 72.18  ? 253 ALA A O   1 
ATOM   1979 C CB  . ALA A 1 249 ? -20.099 8.756   -18.345 1.00 77.32  ? 253 ALA A CB  1 
ATOM   1980 N N   . PRO A 1 250 ? -17.799 10.305  -16.756 1.00 71.25  ? 254 PRO A N   1 
ATOM   1981 C CA  . PRO A 1 250 ? -17.361 11.640  -16.334 1.00 69.97  ? 254 PRO A CA  1 
ATOM   1982 C C   . PRO A 1 250 ? -18.092 12.729  -17.099 1.00 72.35  ? 254 PRO A C   1 
ATOM   1983 O O   . PRO A 1 250 ? -18.347 12.608  -18.300 1.00 79.01  ? 254 PRO A O   1 
ATOM   1984 C CB  . PRO A 1 250 ? -15.863 11.647  -16.662 1.00 68.50  ? 254 PRO A CB  1 
ATOM   1985 C CG  . PRO A 1 250 ? -15.494 10.210  -16.867 1.00 68.37  ? 254 PRO A CG  1 
ATOM   1986 C CD  . PRO A 1 250 ? -16.717 9.553   -17.413 1.00 84.87  ? 254 PRO A CD  1 
ATOM   1987 N N   . ARG A 1 251 ? -18.421 13.807  -16.392 1.00 71.81  ? 255 ARG A N   1 
ATOM   1988 C CA  . ARG A 1 251 ? -19.030 14.980  -17.003 1.00 73.98  ? 255 ARG A CA  1 
ATOM   1989 C C   . ARG A 1 251 ? -18.066 16.159  -17.035 1.00 72.95  ? 255 ARG A C   1 
ATOM   1990 O O   . ARG A 1 251 ? -17.746 16.661  -18.114 1.00 74.53  ? 255 ARG A O   1 
ATOM   1991 C CB  . ARG A 1 251 ? -20.324 15.348  -16.265 1.00 74.84  ? 255 ARG A CB  1 
ATOM   1992 C CG  . ARG A 1 251 ? -21.053 16.543  -16.849 1.00 77.35  ? 255 ARG A CG  1 
ATOM   1993 C CD  . ARG A 1 251 ? -22.550 16.303  -16.912 1.00 80.16  ? 255 ARG A CD  1 
ATOM   1994 N NE  . ARG A 1 251 ? -23.319 17.523  -16.679 1.00 81.29  ? 255 ARG A NE  1 
ATOM   1995 C CZ  . ARG A 1 251 ? -23.503 18.482  -17.581 1.00 83.56  ? 255 ARG A CZ  1 
ATOM   1996 N NH1 . ARG A 1 251 ? -22.966 18.378  -18.788 1.00 90.77  ? 255 ARG A NH1 1 
ATOM   1997 N NH2 . ARG A 1 251 ? -24.221 19.552  -17.270 1.00 84.88  ? 255 ARG A NH2 1 
ATOM   1998 N N   . TYR A 1 252 ? -17.579 16.603  -15.878 1.00 70.46  ? 256 TYR A N   1 
ATOM   1999 C CA  . TYR A 1 252 ? -16.626 17.699  -15.782 1.00 69.35  ? 256 TYR A CA  1 
ATOM   2000 C C   . TYR A 1 252 ? -15.267 17.195  -15.312 1.00 66.58  ? 256 TYR A C   1 
ATOM   2001 O O   . TYR A 1 252 ? -15.172 16.214  -14.568 1.00 64.95  ? 256 TYR A O   1 
ATOM   2002 C CB  . TYR A 1 252 ? -17.119 18.784  -14.819 1.00 75.71  ? 256 TYR A CB  1 
ATOM   2003 C CG  . TYR A 1 252 ? -18.240 19.633  -15.365 1.00 73.10  ? 256 TYR A CG  1 
ATOM   2004 C CD1 . TYR A 1 252 ? -19.552 19.193  -15.317 1.00 76.37  ? 256 TYR A CD1 1 
ATOM   2005 C CD2 . TYR A 1 252 ? -17.986 20.880  -15.919 1.00 76.52  ? 256 TYR A CD2 1 
ATOM   2006 C CE1 . TYR A 1 252 ? -20.583 19.964  -15.815 1.00 76.38  ? 256 TYR A CE1 1 
ATOM   2007 C CE2 . TYR A 1 252 ? -19.010 21.661  -16.418 1.00 81.93  ? 256 TYR A CE2 1 
ATOM   2008 C CZ  . TYR A 1 252 ? -20.307 21.197  -16.363 1.00 84.35  ? 256 TYR A CZ  1 
ATOM   2009 O OH  . TYR A 1 252 ? -21.332 21.969  -16.857 1.00 83.16  ? 256 TYR A OH  1 
ATOM   2010 N N   . ALA A 1 253 ? -14.215 17.889  -15.743 1.00 66.21  ? 257 ALA A N   1 
ATOM   2011 C CA  . ALA A 1 253 ? -12.846 17.589  -15.350 1.00 63.81  ? 257 ALA A CA  1 
ATOM   2012 C C   . ALA A 1 253 ? -12.171 18.863  -14.856 1.00 66.42  ? 257 ALA A C   1 
ATOM   2013 O O   . ALA A 1 253 ? -12.735 19.958  -14.922 1.00 80.10  ? 257 ALA A O   1 
ATOM   2014 C CB  . ALA A 1 253 ? -12.051 16.973  -16.508 1.00 64.67  ? 257 ALA A CB  1 
ATOM   2015 N N   . PHE A 1 254 ? -10.941 18.713  -14.363 1.00 60.50  ? 258 PHE A N   1 
ATOM   2016 C CA  . PHE A 1 254 ? -10.208 19.810  -13.740 1.00 59.19  ? 258 PHE A CA  1 
ATOM   2017 C C   . PHE A 1 254 ? -8.776  19.845  -14.250 1.00 68.69  ? 258 PHE A C   1 
ATOM   2018 O O   . PHE A 1 254 ? -8.051  18.851  -14.144 1.00 57.39  ? 258 PHE A O   1 
ATOM   2019 C CB  . PHE A 1 254 ? -10.205 19.676  -12.215 1.00 56.74  ? 258 PHE A CB  1 
ATOM   2020 C CG  . PHE A 1 254 ? -11.574 19.633  -11.607 1.00 57.29  ? 258 PHE A CG  1 
ATOM   2021 C CD1 . PHE A 1 254 ? -12.243 18.430  -11.465 1.00 57.38  ? 258 PHE A CD1 1 
ATOM   2022 C CD2 . PHE A 1 254 ? -12.191 20.793  -11.175 1.00 57.90  ? 258 PHE A CD2 1 
ATOM   2023 C CE1 . PHE A 1 254 ? -13.502 18.384  -10.907 1.00 58.08  ? 258 PHE A CE1 1 
ATOM   2024 C CE2 . PHE A 1 254 ? -13.453 20.753  -10.615 1.00 58.61  ? 258 PHE A CE2 1 
ATOM   2025 C CZ  . PHE A 1 254 ? -14.108 19.547  -10.480 1.00 58.70  ? 258 PHE A CZ  1 
ATOM   2026 N N   . ALA A 1 255 ? -8.370  20.997  -14.781 1.00 69.53  ? 259 ALA A N   1 
ATOM   2027 C CA  . ALA A 1 255 ? -6.990  21.228  -15.197 1.00 68.71  ? 259 ALA A CA  1 
ATOM   2028 C C   . ALA A 1 255 ? -6.241  21.865  -14.032 1.00 67.06  ? 259 ALA A C   1 
ATOM   2029 O O   . ALA A 1 255 ? -6.519  23.007  -13.658 1.00 70.70  ? 259 ALA A O   1 
ATOM   2030 C CB  . ALA A 1 255 ? -6.941  22.112  -16.439 1.00 71.48  ? 259 ALA A CB  1 
ATOM   2031 N N   . LEU A 1 256 ? -5.283  21.133  -13.471 1.00 57.99  ? 260 LEU A N   1 
ATOM   2032 C CA  . LEU A 1 256 ? -4.671  21.499  -12.202 1.00 52.72  ? 260 LEU A CA  1 
ATOM   2033 C C   . LEU A 1 256 ? -3.470  22.415  -12.393 1.00 62.38  ? 260 LEU A C   1 
ATOM   2034 O O   . LEU A 1 256 ? -2.662  22.226  -13.307 1.00 59.10  ? 260 LEU A O   1 
ATOM   2035 C CB  . LEU A 1 256 ? -4.244  20.243  -11.443 1.00 50.66  ? 260 LEU A CB  1 
ATOM   2036 C CG  . LEU A 1 256 ? -5.344  19.201  -11.239 1.00 50.74  ? 260 LEU A CG  1 
ATOM   2037 C CD1 . LEU A 1 256 ? -4.803  17.990  -10.505 1.00 48.87  ? 260 LEU A CD1 1 
ATOM   2038 C CD2 . LEU A 1 256 ? -6.523  19.805  -10.492 1.00 50.80  ? 260 LEU A CD2 1 
ATOM   2039 N N   . SER A 1 257 ? -3.359  23.405  -11.510 1.00 71.43  ? 261 SER A N   1 
ATOM   2040 C CA  . SER A 1 257 ? -2.203  24.293  -11.434 1.00 62.94  ? 261 SER A CA  1 
ATOM   2041 C C   . SER A 1 257 ? -1.577  24.121  -10.056 1.00 65.91  ? 261 SER A C   1 
ATOM   2042 O O   . SER A 1 257 ? -2.197  24.455  -9.040  1.00 63.93  ? 261 SER A O   1 
ATOM   2043 C CB  . SER A 1 257 ? -2.603  25.746  -11.686 1.00 58.58  ? 261 SER A CB  1 
ATOM   2044 O OG  . SER A 1 257 ? -3.126  25.907  -12.993 1.00 60.77  ? 261 SER A OG  1 
ATOM   2045 N N   . ARG A 1 258 ? -0.355  23.598  -10.024 1.00 79.00  ? 262 ARG A N   1 
ATOM   2046 C CA  . ARG A 1 258 ? 0.302   23.301  -8.762  1.00 68.56  ? 262 ARG A CA  1 
ATOM   2047 C C   . ARG A 1 258 ? 0.712   24.584  -8.043  1.00 69.74  ? 262 ARG A C   1 
ATOM   2048 O O   . ARG A 1 258 ? 0.833   25.658  -8.640  1.00 76.97  ? 262 ARG A O   1 
ATOM   2049 C CB  . ARG A 1 258 ? 1.526   22.414  -8.992  1.00 71.79  ? 262 ARG A CB  1 
ATOM   2050 C CG  . ARG A 1 258 ? 1.199   21.055  -9.587  1.00 75.27  ? 262 ARG A CG  1 
ATOM   2051 C CD  . ARG A 1 258 ? 0.424   20.189  -8.607  1.00 74.39  ? 262 ARG A CD  1 
ATOM   2052 N NE  . ARG A 1 258 ? 0.138   18.869  -9.164  1.00 80.85  ? 262 ARG A NE  1 
ATOM   2053 C CZ  . ARG A 1 258 ? -0.456  17.885  -8.496  1.00 65.97  ? 262 ARG A CZ  1 
ATOM   2054 N NH1 . ARG A 1 258 ? -0.829  18.064  -7.237  1.00 60.90  ? 262 ARG A NH1 1 
ATOM   2055 N NH2 . ARG A 1 258 ? -0.673  16.719  -9.088  1.00 61.92  ? 262 ARG A NH2 1 
ATOM   2056 N N   . GLY A 1 259 ? 0.923   24.456  -6.737  1.00 71.93  ? 263 GLY A N   1 
ATOM   2057 C CA  . GLY A 1 259 ? 1.327   25.577  -5.912  1.00 69.79  ? 263 GLY A CA  1 
ATOM   2058 C C   . GLY A 1 259 ? 1.699   25.146  -4.511  1.00 72.85  ? 263 GLY A C   1 
ATOM   2059 O O   . GLY A 1 259 ? 1.043   24.278  -3.927  1.00 74.19  ? 263 GLY A O   1 
ATOM   2060 N N   . PHE A 1 260 ? 2.753   25.740  -3.963  1.00 75.60  ? 264 PHE A N   1 
ATOM   2061 C CA  . PHE A 1 260 ? 3.219   25.405  -2.628  1.00 73.79  ? 264 PHE A CA  1 
ATOM   2062 C C   . PHE A 1 260 ? 2.598   26.338  -1.595  1.00 68.84  ? 264 PHE A C   1 
ATOM   2063 O O   . PHE A 1 260 ? 2.178   27.456  -1.902  1.00 70.48  ? 264 PHE A O   1 
ATOM   2064 C CB  . PHE A 1 260 ? 4.745   25.482  -2.554  1.00 76.33  ? 264 PHE A CB  1 
ATOM   2065 C CG  . PHE A 1 260 ? 5.443   24.832  -3.717  1.00 94.77  ? 264 PHE A CG  1 
ATOM   2066 C CD1 . PHE A 1 260 ? 5.740   23.479  -3.701  1.00 100.37 ? 264 PHE A CD1 1 
ATOM   2067 C CD2 . PHE A 1 260 ? 5.806   25.578  -4.827  1.00 103.03 ? 264 PHE A CD2 1 
ATOM   2068 C CE1 . PHE A 1 260 ? 6.381   22.883  -4.772  1.00 99.21  ? 264 PHE A CE1 1 
ATOM   2069 C CE2 . PHE A 1 260 ? 6.446   24.988  -5.900  1.00 103.05 ? 264 PHE A CE2 1 
ATOM   2070 C CZ  . PHE A 1 260 ? 6.734   23.639  -5.872  1.00 102.61 ? 264 PHE A CZ  1 
ATOM   2071 N N   . GLY A 1 261 A 2.548   25.861  -0.352  1.00 57.74  ? 264 GLY A N   1 
ATOM   2072 C CA  . GLY A 1 261 A 2.029   26.642  0.747   1.00 59.58  ? 264 GLY A CA  1 
ATOM   2073 C C   . GLY A 1 261 A 0.572   26.405  1.073   1.00 55.54  ? 264 GLY A C   1 
ATOM   2074 O O   . GLY A 1 261 A 0.101   26.885  2.111   1.00 71.76  ? 264 GLY A O   1 
ATOM   2075 N N   . SER A 1 262 ? -0.154  25.687  0.225   1.00 54.08  ? 265 SER A N   1 
ATOM   2076 C CA  . SER A 1 262 ? -1.554  25.386  0.461   1.00 45.78  ? 265 SER A CA  1 
ATOM   2077 C C   . SER A 1 262 ? -1.693  24.054  1.191   1.00 42.45  ? 265 SER A C   1 
ATOM   2078 O O   . SER A 1 262 ? -0.735  23.294  1.344   1.00 43.86  ? 265 SER A O   1 
ATOM   2079 C CB  . SER A 1 262 ? -2.322  25.359  -0.860  1.00 51.18  ? 265 SER A CB  1 
ATOM   2080 O OG  . SER A 1 262 ? -3.704  25.140  -0.642  1.00 56.88  ? 265 SER A OG  1 
ATOM   2081 N N   . GLY A 1 263 ? -2.906  23.777  1.649   1.00 41.80  ? 266 GLY A N   1 
ATOM   2082 C CA  . GLY A 1 263 ? -3.160  22.545  2.372   1.00 35.84  ? 266 GLY A CA  1 
ATOM   2083 C C   . GLY A 1 263 ? -4.607  22.476  2.804   1.00 40.78  ? 266 GLY A C   1 
ATOM   2084 O O   . GLY A 1 263 ? -5.385  23.417  2.616   1.00 45.32  ? 266 GLY A O   1 
ATOM   2085 N N   . ILE A 1 264 ? -4.954  21.334  3.389   1.00 42.20  ? 267 ILE A N   1 
ATOM   2086 C CA  . ILE A 1 264 ? -6.303  21.052  3.868   1.00 43.88  ? 267 ILE A CA  1 
ATOM   2087 C C   . ILE A 1 264 ? -6.253  21.014  5.389   1.00 48.34  ? 267 ILE A C   1 
ATOM   2088 O O   . ILE A 1 264 ? -5.459  20.264  5.970   1.00 50.23  ? 267 ILE A O   1 
ATOM   2089 C CB  . ILE A 1 264 ? -6.838  19.730  3.296   1.00 41.64  ? 267 ILE A CB  1 
ATOM   2090 C CG1 . ILE A 1 264 ? -6.938  19.809  1.772   1.00 49.52  ? 267 ILE A CG1 1 
ATOM   2091 C CG2 . ILE A 1 264 ? -8.178  19.368  3.920   1.00 37.69  ? 267 ILE A CG2 1 
ATOM   2092 C CD1 . ILE A 1 264 ? -7.346  18.506  1.121   1.00 44.52  ? 267 ILE A CD1 1 
ATOM   2093 N N   . ILE A 1 265 ? -7.086  21.826  6.038   1.00 36.16  ? 268 ILE A N   1 
ATOM   2094 C CA  . ILE A 1 265 ? -7.136  21.860  7.493   1.00 35.60  ? 268 ILE A CA  1 
ATOM   2095 C C   . ILE A 1 265 ? -8.571  21.655  7.956   1.00 38.47  ? 268 ILE A C   1 
ATOM   2096 O O   . ILE A 1 265 ? -9.528  21.980  7.248   1.00 44.78  ? 268 ILE A O   1 
ATOM   2097 C CB  . ILE A 1 265 ? -6.565  23.176  8.073   1.00 35.27  ? 268 ILE A CB  1 
ATOM   2098 C CG1 . ILE A 1 265 ? -7.396  24.378  7.627   1.00 36.84  ? 268 ILE A CG1 1 
ATOM   2099 C CG2 . ILE A 1 265 ? -5.111  23.352  7.669   1.00 52.53  ? 268 ILE A CG2 1 
ATOM   2100 C CD1 . ILE A 1 265 ? -6.947  25.679  8.250   1.00 36.78  ? 268 ILE A CD1 1 
ATOM   2101 N N   . ASN A 1 266 ? -8.711  21.095  9.154   1.00 40.14  ? 269 ASN A N   1 
ATOM   2102 C CA  . ASN A 1 266 ? -10.000 20.947  9.817   1.00 42.41  ? 269 ASN A CA  1 
ATOM   2103 C C   . ASN A 1 266 ? -10.127 22.043  10.867  1.00 39.76  ? 269 ASN A C   1 
ATOM   2104 O O   . ASN A 1 266 ? -9.288  22.141  11.769  1.00 52.92  ? 269 ASN A O   1 
ATOM   2105 C CB  . ASN A 1 266 ? -10.135 19.570  10.466  1.00 50.88  ? 269 ASN A CB  1 
ATOM   2106 C CG  . ASN A 1 266 ? -9.981  18.438  9.474   1.00 62.13  ? 269 ASN A CG  1 
ATOM   2107 O OD1 . ASN A 1 266 ? -10.508 18.491  8.363   1.00 62.64  ? 269 ASN A OD1 1 
ATOM   2108 N ND2 . ASN A 1 266 ? -9.251  17.403  9.872   1.00 73.52  ? 269 ASN A ND2 1 
ATOM   2109 N N   . SER A 1 267 ? -11.170 22.860  10.752  1.00 39.76  ? 270 SER A N   1 
ATOM   2110 C CA  . SER A 1 267 ? -11.333 23.980  11.666  1.00 40.30  ? 270 SER A CA  1 
ATOM   2111 C C   . SER A 1 267 ? -12.798 24.379  11.732  1.00 42.49  ? 270 SER A C   1 
ATOM   2112 O O   . SER A 1 267 ? -13.529 24.284  10.743  1.00 43.63  ? 270 SER A O   1 
ATOM   2113 C CB  . SER A 1 267 ? -10.477 25.176  11.235  1.00 39.80  ? 270 SER A CB  1 
ATOM   2114 O OG  . SER A 1 267 ? -10.749 26.313  12.036  1.00 44.04  ? 270 SER A OG  1 
ATOM   2115 N N   . ASN A 1 268 ? -13.215 24.823  12.916  1.00 57.93  ? 271 ASN A N   1 
ATOM   2116 C CA  . ASN A 1 268 ? -14.535 25.400  13.126  1.00 53.51  ? 271 ASN A CA  1 
ATOM   2117 C C   . ASN A 1 268 ? -14.496 26.915  13.266  1.00 53.01  ? 271 ASN A C   1 
ATOM   2118 O O   . ASN A 1 268 ? -15.538 27.528  13.514  1.00 59.84  ? 271 ASN A O   1 
ATOM   2119 C CB  . ASN A 1 268 ? -15.192 24.790  14.368  1.00 63.66  ? 271 ASN A CB  1 
ATOM   2120 C CG  . ASN A 1 268 ? -15.738 23.398  14.117  1.00 71.78  ? 271 ASN A CG  1 
ATOM   2121 O OD1 . ASN A 1 268 ? -16.192 23.083  13.016  1.00 78.66  ? 271 ASN A OD1 1 
ATOM   2122 N ND2 . ASN A 1 268 ? -15.701 22.555  15.145  1.00 80.29  ? 271 ASN A ND2 1 
ATOM   2123 N N   . ALA A 1 269 ? -13.324 27.530  13.120  1.00 44.86  ? 272 ALA A N   1 
ATOM   2124 C CA  . ALA A 1 269 ? -13.225 28.975  13.218  1.00 49.45  ? 272 ALA A CA  1 
ATOM   2125 C C   . ALA A 1 269 ? -13.935 29.636  12.037  1.00 47.36  ? 272 ALA A C   1 
ATOM   2126 O O   . ALA A 1 269 ? -13.915 29.116  10.920  1.00 49.50  ? 272 ALA A O   1 
ATOM   2127 C CB  . ALA A 1 269 ? -11.763 29.411  13.258  1.00 43.88  ? 272 ALA A CB  1 
ATOM   2128 N N   . PRO A 1 270 ? -14.582 30.776  12.262  1.00 50.15  ? 273 PRO A N   1 
ATOM   2129 C CA  . PRO A 1 270 ? -15.301 31.443  11.174  1.00 51.13  ? 273 PRO A CA  1 
ATOM   2130 C C   . PRO A 1 270 ? -14.376 32.251  10.280  1.00 50.62  ? 273 PRO A C   1 
ATOM   2131 O O   . PRO A 1 270 ? -13.349 32.779  10.711  1.00 51.73  ? 273 PRO A O   1 
ATOM   2132 C CB  . PRO A 1 270 ? -16.283 32.368  11.909  1.00 53.45  ? 273 PRO A CB  1 
ATOM   2133 C CG  . PRO A 1 270 ? -16.208 31.978  13.364  1.00 52.81  ? 273 PRO A CG  1 
ATOM   2134 C CD  . PRO A 1 270 ? -14.846 31.411  13.560  1.00 50.07  ? 273 PRO A CD  1 
ATOM   2135 N N   . MET A 1 271 ? -14.766 32.344  9.012   1.00 60.34  ? 274 MET A N   1 
ATOM   2136 C CA  . MET A 1 271 ? -14.079 33.218  8.074   1.00 62.32  ? 274 MET A CA  1 
ATOM   2137 C C   . MET A 1 271 ? -14.350 34.679  8.421   1.00 60.24  ? 274 MET A C   1 
ATOM   2138 O O   . MET A 1 271 ? -15.427 35.035  8.905   1.00 71.34  ? 274 MET A O   1 
ATOM   2139 C CB  . MET A 1 271 ? -14.535 32.917  6.645   1.00 72.84  ? 274 MET A CB  1 
ATOM   2140 C CG  . MET A 1 271 ? -13.956 33.828  5.574   1.00 85.74  ? 274 MET A CG  1 
ATOM   2141 S SD  . MET A 1 271 ? -12.209 33.535  5.243   1.00 82.12  ? 274 MET A SD  1 
ATOM   2142 C CE  . MET A 1 271 ? -11.875 34.841  4.063   1.00 85.61  ? 274 MET A CE  1 
ATOM   2143 N N   . ASP A 1 272 ? -13.354 35.528  8.179   1.00 61.43  ? 275 ASP A N   1 
ATOM   2144 C CA  . ASP A 1 272 ? -13.495 36.954  8.433   1.00 69.02  ? 275 ASP A CA  1 
ATOM   2145 C C   . ASP A 1 272 ? -12.662 37.727  7.421   1.00 76.87  ? 275 ASP A C   1 
ATOM   2146 O O   . ASP A 1 272 ? -11.796 37.169  6.742   1.00 72.29  ? 275 ASP A O   1 
ATOM   2147 C CB  . ASP A 1 272 ? -13.076 37.314  9.864   1.00 78.16  ? 275 ASP A CB  1 
ATOM   2148 C CG  . ASP A 1 272 ? -13.570 38.684  10.287  1.00 91.63  ? 275 ASP A CG  1 
ATOM   2149 O OD1 . ASP A 1 272 ? -14.724 38.781  10.753  1.00 86.42  ? 275 ASP A OD1 1 
ATOM   2150 O OD2 . ASP A 1 272 ? -12.808 39.663  10.144  1.00 99.35  ? 275 ASP A OD2 1 
ATOM   2151 N N   . GLU A 1 273 ? -12.936 39.029  7.329   1.00 95.25  ? 276 GLU A N   1 
ATOM   2152 C CA  . GLU A 1 273 ? -12.231 39.916  6.405   1.00 101.84 ? 276 GLU A CA  1 
ATOM   2153 C C   . GLU A 1 273 ? -10.897 40.368  7.008   1.00 98.86  ? 276 GLU A C   1 
ATOM   2154 O O   . GLU A 1 273 ? -10.610 41.554  7.168   1.00 114.09 ? 276 GLU A O   1 
ATOM   2155 C CB  . GLU A 1 273 ? -13.114 41.104  6.041   1.00 108.47 ? 276 GLU A CB  1 
ATOM   2156 C CG  . GLU A 1 273 ? -13.814 41.749  7.231   1.00 119.26 ? 276 GLU A CG  1 
ATOM   2157 C CD  . GLU A 1 273 ? -14.768 42.856  6.819   1.00 128.45 ? 276 GLU A CD  1 
ATOM   2158 O OE1 . GLU A 1 273 ? -14.735 43.263  5.638   1.00 133.20 ? 276 GLU A OE1 1 
ATOM   2159 O OE2 . GLU A 1 273 ? -15.552 43.318  7.675   1.00 123.53 ? 276 GLU A OE2 1 
ATOM   2160 N N   . CYS A 1 274 ? -10.074 39.380  7.346   1.00 73.21  ? 277 CYS A N   1 
ATOM   2161 C CA  . CYS A 1 274 ? -8.750  39.607  7.899   1.00 66.36  ? 277 CYS A CA  1 
ATOM   2162 C C   . CYS A 1 274 ? -7.696  39.030  6.966   1.00 58.65  ? 277 CYS A C   1 
ATOM   2163 O O   . CYS A 1 274 ? -7.955  38.103  6.194   1.00 67.00  ? 277 CYS A O   1 
ATOM   2164 C CB  . CYS A 1 274 ? -8.615  38.985  9.294   1.00 65.21  ? 277 CYS A CB  1 
ATOM   2165 S SG  . CYS A 1 274 ? -9.329  37.332  9.446   1.00 71.50  ? 277 CYS A SG  1 
ATOM   2166 N N   . ASP A 1 275 ? -6.500  39.599  7.041   1.00 62.91  ? 278 ASP A N   1 
ATOM   2167 C CA  . ASP A 1 275 ? -5.365  39.142  6.256   1.00 62.28  ? 278 ASP A CA  1 
ATOM   2168 C C   . ASP A 1 275 ? -4.198  38.864  7.188   1.00 59.90  ? 278 ASP A C   1 
ATOM   2169 O O   . ASP A 1 275 ? -3.932  39.637  8.113   1.00 60.42  ? 278 ASP A O   1 
ATOM   2170 C CB  . ASP A 1 275 ? -4.958  40.173  5.198   1.00 67.47  ? 278 ASP A CB  1 
ATOM   2171 C CG  . ASP A 1 275 ? -3.972  39.615  4.196   1.00 74.02  ? 278 ASP A CG  1 
ATOM   2172 O OD1 . ASP A 1 275 ? -4.167  38.464  3.756   1.00 83.35  ? 278 ASP A OD1 1 
ATOM   2173 O OD2 . ASP A 1 275 ? -2.999  40.319  3.856   1.00 84.22  ? 278 ASP A OD2 1 
ATOM   2174 N N   . ALA A 1 276 ? -3.508  37.753  6.947   1.00 46.06  ? 279 ALA A N   1 
ATOM   2175 C CA  . ALA A 1 276 ? -2.382  37.366  7.781   1.00 48.30  ? 279 ALA A CA  1 
ATOM   2176 C C   . ALA A 1 276 ? -1.377  36.600  6.937   1.00 43.42  ? 279 ALA A C   1 
ATOM   2177 O O   . ALA A 1 276 ? -1.672  36.157  5.825   1.00 46.76  ? 279 ALA A O   1 
ATOM   2178 C CB  . ALA A 1 276 ? -2.832  36.527  8.981   1.00 47.34  ? 279 ALA A CB  1 
ATOM   2179 N N   . LYS A 1 277 ? -0.173  36.456  7.483   1.00 47.59  ? 280 LYS A N   1 
ATOM   2180 C CA  . LYS A 1 277 ? 0.874   35.658  6.866   1.00 52.09  ? 280 LYS A CA  1 
ATOM   2181 C C   . LYS A 1 277 ? 0.953   34.251  7.440   1.00 44.49  ? 280 LYS A C   1 
ATOM   2182 O O   . LYS A 1 277 ? 1.715   33.430  6.922   1.00 42.41  ? 280 LYS A O   1 
ATOM   2183 C CB  . LYS A 1 277 ? 2.230   36.358  7.026   1.00 64.41  ? 280 LYS A CB  1 
ATOM   2184 C CG  . LYS A 1 277 ? 2.242   37.790  6.506   1.00 88.17  ? 280 LYS A CG  1 
ATOM   2185 C CD  . LYS A 1 277 ? 3.574   38.478  6.764   1.00 94.41  ? 280 LYS A CD  1 
ATOM   2186 C CE  . LYS A 1 277 ? 3.562   39.913  6.256   1.00 88.77  ? 280 LYS A CE  1 
ATOM   2187 N NZ  . LYS A 1 277 ? 4.857   40.605  6.505   1.00 98.60  ? 280 LYS A NZ  1 
ATOM   2188 N N   . CYS A 1 278 ? 0.175   33.954  8.479   1.00 38.19  ? 281 CYS A N   1 
ATOM   2189 C CA  . CYS A 1 278 ? 0.234   32.681  9.184   1.00 36.04  ? 281 CYS A CA  1 
ATOM   2190 C C   . CYS A 1 278 ? -1.166  32.283  9.627   1.00 35.70  ? 281 CYS A C   1 
ATOM   2191 O O   . CYS A 1 278 ? -1.851  33.060  10.299  1.00 39.95  ? 281 CYS A O   1 
ATOM   2192 C CB  . CYS A 1 278 ? 1.161   32.771  10.402  1.00 43.96  ? 281 CYS A CB  1 
ATOM   2193 S SG  . CYS A 1 278 ? 1.081   31.327  11.475  1.00 49.08  ? 281 CYS A SG  1 
ATOM   2194 N N   . GLN A 1 279 ? -1.579  31.070  9.265   1.00 35.15  ? 282 GLN A N   1 
ATOM   2195 C CA  . GLN A 1 279 ? -2.907  30.565  9.582   1.00 35.68  ? 282 GLN A CA  1 
ATOM   2196 C C   . GLN A 1 279 ? -2.807  29.193  10.235  1.00 34.34  ? 282 GLN A C   1 
ATOM   2197 O O   . GLN A 1 279 ? -2.072  28.320  9.762   1.00 33.32  ? 282 GLN A O   1 
ATOM   2198 C CB  . GLN A 1 279 ? -3.783  30.472  8.326   1.00 36.90  ? 282 GLN A CB  1 
ATOM   2199 C CG  . GLN A 1 279 ? -5.218  30.052  8.601   1.00 37.78  ? 282 GLN A CG  1 
ATOM   2200 C CD  . GLN A 1 279 ? -6.012  31.128  9.316   1.00 39.16  ? 282 GLN A CD  1 
ATOM   2201 O OE1 . GLN A 1 279 ? -5.914  32.307  8.984   1.00 40.22  ? 282 GLN A OE1 1 
ATOM   2202 N NE2 . GLN A 1 279 ? -6.795  30.727  10.309  1.00 44.93  ? 282 GLN A NE2 1 
ATOM   2203 N N   . THR A 1 280 ? -3.546  29.010  11.323  1.00 34.53  ? 283 THR A N   1 
ATOM   2204 C CA  . THR A 1 280 ? -3.643  27.749  12.035  1.00 33.63  ? 283 THR A CA  1 
ATOM   2205 C C   . THR A 1 280 ? -5.117  27.389  12.210  1.00 34.77  ? 283 THR A C   1 
ATOM   2206 O O   . THR A 1 280 ? -5.984  28.259  12.118  1.00 36.20  ? 283 THR A O   1 
ATOM   2207 C CB  . THR A 1 280 ? -2.959  27.820  13.410  1.00 32.84  ? 283 THR A CB  1 
ATOM   2208 O OG1 . THR A 1 280 ? -3.801  28.518  14.336  1.00 33.92  ? 283 THR A OG1 1 
ATOM   2209 C CG2 . THR A 1 280 ? -1.619  28.533  13.309  1.00 32.17  ? 283 THR A CG2 1 
ATOM   2210 N N   . PRO A 1 281 ? -5.421  26.110  12.449  1.00 34.32  ? 284 PRO A N   1 
ATOM   2211 C CA  . PRO A 1 281 ? -6.828  25.737  12.693  1.00 35.56  ? 284 PRO A CA  1 
ATOM   2212 C C   . PRO A 1 281 ? -7.465  26.477  13.855  1.00 36.54  ? 284 PRO A C   1 
ATOM   2213 O O   . PRO A 1 281 ? -8.688  26.663  13.863  1.00 48.55  ? 284 PRO A O   1 
ATOM   2214 C CB  . PRO A 1 281 ? -6.743  24.229  12.965  1.00 34.75  ? 284 PRO A CB  1 
ATOM   2215 C CG  . PRO A 1 281 ? -5.522  23.789  12.254  1.00 33.40  ? 284 PRO A CG  1 
ATOM   2216 C CD  . PRO A 1 281 ? -4.550  24.929  12.339  1.00 32.92  ? 284 PRO A CD  1 
ATOM   2217 N N   . GLN A 1 282 ? -6.675  26.900  14.844  1.00 38.28  ? 285 GLN A N   1 
ATOM   2218 C CA  . GLN A 1 282 ? -7.225  27.699  15.933  1.00 38.88  ? 285 GLN A CA  1 
ATOM   2219 C C   . GLN A 1 282 ? -7.492  29.131  15.497  1.00 38.14  ? 285 GLN A C   1 
ATOM   2220 O O   . GLN A 1 282 ? -8.414  29.773  16.009  1.00 39.70  ? 285 GLN A O   1 
ATOM   2221 C CB  . GLN A 1 282 ? -6.275  27.682  17.130  1.00 43.63  ? 285 GLN A CB  1 
ATOM   2222 C CG  . GLN A 1 282 ? -6.072  26.314  17.739  1.00 41.95  ? 285 GLN A CG  1 
ATOM   2223 C CD  . GLN A 1 282 ? -7.318  25.793  18.422  1.00 48.40  ? 285 GLN A CD  1 
ATOM   2224 O OE1 . GLN A 1 282 ? -7.988  26.520  19.154  1.00 51.41  ? 285 GLN A OE1 1 
ATOM   2225 N NE2 . GLN A 1 282 ? -7.639  24.527  18.180  1.00 59.35  ? 285 GLN A NE2 1 
ATOM   2226 N N   . GLY A 1 283 ? -6.705  29.644  14.566  1.00 37.61  ? 286 GLY A N   1 
ATOM   2227 C CA  . GLY A 1 283 ? -6.851  31.014  14.125  1.00 38.83  ? 286 GLY A CA  1 
ATOM   2228 C C   . GLY A 1 283 ? -5.575  31.501  13.476  1.00 37.91  ? 286 GLY A C   1 
ATOM   2229 O O   . GLY A 1 283 ? -4.576  30.787  13.392  1.00 36.35  ? 286 GLY A O   1 
ATOM   2230 N N   . ALA A 1 284 ? -5.637  32.744  13.009  1.00 39.11  ? 287 ALA A N   1 
ATOM   2231 C CA  . ALA A 1 284 ? -4.490  33.360  12.362  1.00 38.65  ? 287 ALA A CA  1 
ATOM   2232 C C   . ALA A 1 284 ? -3.527  33.920  13.401  1.00 38.03  ? 287 ALA A C   1 
ATOM   2233 O O   . ALA A 1 284 ? -3.932  34.388  14.469  1.00 38.69  ? 287 ALA A O   1 
ATOM   2234 C CB  . ALA A 1 284 ? -4.937  34.469  11.411  1.00 40.42  ? 287 ALA A CB  1 
ATOM   2235 N N   . ILE A 1 285 ? -2.239  33.865  13.077  1.00 36.89  ? 288 ILE A N   1 
ATOM   2236 C CA  . ILE A 1 285 ? -1.178  34.348  13.952  1.00 36.29  ? 288 ILE A CA  1 
ATOM   2237 C C   . ILE A 1 285 ? -0.536  35.562  13.299  1.00 39.62  ? 288 ILE A C   1 
ATOM   2238 O O   . ILE A 1 285 ? -0.147  35.513  12.126  1.00 49.14  ? 288 ILE A O   1 
ATOM   2239 C CB  . ILE A 1 285 ? -0.136  33.253  14.237  1.00 34.44  ? 288 ILE A CB  1 
ATOM   2240 C CG1 . ILE A 1 285 ? -0.772  32.106  15.023  1.00 33.85  ? 288 ILE A CG1 1 
ATOM   2241 C CG2 . ILE A 1 285 ? 1.057   33.826  14.991  1.00 34.00  ? 288 ILE A CG2 1 
ATOM   2242 C CD1 . ILE A 1 285 ? 0.198   31.017  15.409  1.00 32.26  ? 288 ILE A CD1 1 
ATOM   2243 N N   . ASN A 1 286 ? -0.437  36.649  14.056  1.00 38.02  ? 289 ASN A N   1 
ATOM   2244 C CA  . ASN A 1 286 ? 0.193   37.893  13.624  1.00 39.03  ? 289 ASN A CA  1 
ATOM   2245 C C   . ASN A 1 286 ? 1.339   38.154  14.599  1.00 38.30  ? 289 ASN A C   1 
ATOM   2246 O O   . ASN A 1 286 ? 1.151   38.764  15.654  1.00 38.95  ? 289 ASN A O   1 
ATOM   2247 C CB  . ASN A 1 286 ? -0.833  39.027  13.586  1.00 41.16  ? 289 ASN A CB  1 
ATOM   2248 C CG  . ASN A 1 286 ? -0.201  40.400  13.602  1.00 50.00  ? 289 ASN A CG  1 
ATOM   2249 O OD1 . ASN A 1 286 ? 0.515   40.784  12.676  1.00 49.82  ? 289 ASN A OD1 1 
ATOM   2250 N ND2 . ASN A 1 286 ? -0.476  41.157  14.656  1.00 49.80  ? 289 ASN A ND2 1 
ATOM   2251 N N   . SER A 1 287 ? 2.529   37.671  14.251  1.00 37.07  ? 290 SER A N   1 
ATOM   2252 C CA  . SER A 1 287 ? 3.652   37.709  15.176  1.00 36.28  ? 290 SER A CA  1 
ATOM   2253 C C   . SER A 1 287 ? 4.953   37.646  14.394  1.00 36.48  ? 290 SER A C   1 
ATOM   2254 O O   . SER A 1 287 ? 4.993   37.186  13.250  1.00 41.98  ? 290 SER A O   1 
ATOM   2255 C CB  . SER A 1 287 ? 3.573   36.556  16.185  1.00 35.97  ? 290 SER A CB  1 
ATOM   2256 O OG  . SER A 1 287 ? 4.699   36.531  17.044  1.00 34.26  ? 290 SER A OG  1 
ATOM   2257 N N   . SER A 1 288 ? 6.020   38.127  15.030  1.00 45.17  ? 291 SER A N   1 
ATOM   2258 C CA  . SER A 1 288 ? 7.374   37.977  14.513  1.00 48.62  ? 291 SER A CA  1 
ATOM   2259 C C   . SER A 1 288 ? 8.261   37.196  15.473  1.00 40.51  ? 291 SER A C   1 
ATOM   2260 O O   . SER A 1 288 ? 9.489   37.212  15.324  1.00 42.25  ? 291 SER A O   1 
ATOM   2261 C CB  . SER A 1 288 ? 7.990   39.346  14.211  1.00 58.43  ? 291 SER A CB  1 
ATOM   2262 O OG  . SER A 1 288 ? 7.927   40.195  15.342  1.00 72.36  ? 291 SER A OG  1 
ATOM   2263 N N   . LEU A 1 289 ? 7.670   36.513  16.452  1.00 34.04  ? 292 LEU A N   1 
ATOM   2264 C CA  . LEU A 1 289 ? 8.399   35.722  17.427  1.00 32.04  ? 292 LEU A CA  1 
ATOM   2265 C C   . LEU A 1 289 ? 8.808   34.376  16.830  1.00 30.77  ? 292 LEU A C   1 
ATOM   2266 O O   . LEU A 1 289 ? 8.145   33.862  15.926  1.00 30.60  ? 292 LEU A O   1 
ATOM   2267 C CB  . LEU A 1 289 ? 7.547   35.501  18.673  1.00 32.05  ? 292 LEU A CB  1 
ATOM   2268 C CG  . LEU A 1 289 ? 7.189   36.767  19.454  1.00 33.41  ? 292 LEU A CG  1 
ATOM   2269 C CD1 . LEU A 1 289 ? 6.341   36.435  20.672  1.00 36.28  ? 292 LEU A CD1 1 
ATOM   2270 C CD2 . LEU A 1 289 ? 8.449   37.517  19.860  1.00 36.06  ? 292 LEU A CD2 1 
ATOM   2271 N N   . PRO A 1 290 ? 9.906   33.788  17.314  1.00 30.02  ? 293 PRO A N   1 
ATOM   2272 C CA  . PRO A 1 290 ? 10.387  32.535  16.715  1.00 29.01  ? 293 PRO A CA  1 
ATOM   2273 C C   . PRO A 1 290 ? 9.618   31.295  17.142  1.00 28.20  ? 293 PRO A C   1 
ATOM   2274 O O   . PRO A 1 290 ? 9.741   30.261  16.474  1.00 37.54  ? 293 PRO A O   1 
ATOM   2275 C CB  . PRO A 1 290 ? 11.847  32.465  17.184  1.00 28.79  ? 293 PRO A CB  1 
ATOM   2276 C CG  . PRO A 1 290 ? 11.847  33.198  18.479  1.00 29.29  ? 293 PRO A CG  1 
ATOM   2277 C CD  . PRO A 1 290 ? 10.834  34.302  18.338  1.00 30.27  ? 293 PRO A CD  1 
ATOM   2278 N N   . PHE A 1 291 ? 8.829   31.355  18.212  1.00 28.37  ? 294 PHE A N   1 
ATOM   2279 C CA  . PHE A 1 291 ? 8.133   30.184  18.723  1.00 27.80  ? 294 PHE A CA  1 
ATOM   2280 C C   . PHE A 1 291 ? 6.657   30.497  18.931  1.00 28.47  ? 294 PHE A C   1 
ATOM   2281 O O   . PHE A 1 291 ? 6.263   31.649  19.118  1.00 29.41  ? 294 PHE A O   1 
ATOM   2282 C CB  . PHE A 1 291 ? 8.751   29.695  20.041  1.00 27.50  ? 294 PHE A CB  1 
ATOM   2283 C CG  . PHE A 1 291 ? 10.212  29.358  19.940  1.00 27.02  ? 294 PHE A CG  1 
ATOM   2284 C CD1 . PHE A 1 291 ? 10.627  28.220  19.273  1.00 26.30  ? 294 PHE A CD1 1 
ATOM   2285 C CD2 . PHE A 1 291 ? 11.168  30.174  20.520  1.00 39.49  ? 294 PHE A CD2 1 
ATOM   2286 C CE1 . PHE A 1 291 ? 11.965  27.904  19.181  1.00 26.05  ? 294 PHE A CE1 1 
ATOM   2287 C CE2 . PHE A 1 291 ? 12.511  29.865  20.430  1.00 27.17  ? 294 PHE A CE2 1 
ATOM   2288 C CZ  . PHE A 1 291 ? 12.910  28.730  19.760  1.00 31.92  ? 294 PHE A CZ  1 
ATOM   2289 N N   . GLN A 1 292 ? 5.840   29.446  18.897  1.00 28.13  ? 295 GLN A N   1 
ATOM   2290 C CA  . GLN A 1 292 ? 4.413   29.560  19.163  1.00 28.86  ? 295 GLN A CA  1 
ATOM   2291 C C   . GLN A 1 292 ? 3.905   28.242  19.727  1.00 28.47  ? 295 GLN A C   1 
ATOM   2292 O O   . GLN A 1 292 ? 4.387   27.175  19.343  1.00 27.65  ? 295 GLN A O   1 
ATOM   2293 C CB  . GLN A 1 292 ? 3.631   29.939  17.896  1.00 32.13  ? 295 GLN A CB  1 
ATOM   2294 C CG  . GLN A 1 292 ? 3.843   29.005  16.710  1.00 30.55  ? 295 GLN A CG  1 
ATOM   2295 C CD  . GLN A 1 292 ? 2.755   27.951  16.571  1.00 32.50  ? 295 GLN A CD  1 
ATOM   2296 O OE1 . GLN A 1 292 ? 1.841   27.865  17.390  1.00 33.05  ? 295 GLN A OE1 1 
ATOM   2297 N NE2 . GLN A 1 292 ? 2.851   27.145  15.522  1.00 37.46  ? 295 GLN A NE2 1 
ATOM   2298 N N   . ASN A 1 293 ? 2.944   28.321  20.649  1.00 29.24  ? 296 ASN A N   1 
ATOM   2299 C CA  . ASN A 1 293 ? 2.295   27.139  21.206  1.00 29.21  ? 296 ASN A CA  1 
ATOM   2300 C C   . ASN A 1 293 ? 0.809   27.095  20.863  1.00 30.07  ? 296 ASN A C   1 
ATOM   2301 O O   . ASN A 1 293 ? 0.017   26.470  21.573  1.00 44.68  ? 296 ASN A O   1 
ATOM   2302 C CB  . ASN A 1 293 ? 2.500   27.064  22.719  1.00 29.56  ? 296 ASN A CB  1 
ATOM   2303 C CG  . ASN A 1 293 ? 1.942   28.266  23.460  1.00 30.76  ? 296 ASN A CG  1 
ATOM   2304 O OD1 . ASN A 1 293 ? 1.217   29.085  22.900  1.00 36.34  ? 296 ASN A OD1 1 
ATOM   2305 N ND2 . ASN A 1 293 ? 2.278   28.370  24.740  1.00 31.17  ? 296 ASN A ND2 1 
ATOM   2306 N N   . VAL A 1 294 ? 0.422   27.757  19.774  1.00 30.39  ? 297 VAL A N   1 
ATOM   2307 C CA  . VAL A 1 294 ? -0.984  27.821  19.397  1.00 31.41  ? 297 VAL A CA  1 
ATOM   2308 C C   . VAL A 1 294 ? -1.438  26.511  18.767  1.00 33.46  ? 297 VAL A C   1 
ATOM   2309 O O   . VAL A 1 294 ? -2.411  25.898  19.217  1.00 42.83  ? 297 VAL A O   1 
ATOM   2310 C CB  . VAL A 1 294 ? -1.224  29.014  18.456  1.00 32.11  ? 297 VAL A CB  1 
ATOM   2311 C CG1 . VAL A 1 294 ? -2.677  29.071  18.018  1.00 33.32  ? 297 VAL A CG1 1 
ATOM   2312 C CG2 . VAL A 1 294 ? -0.807  30.312  19.132  1.00 32.69  ? 297 VAL A CG2 1 
ATOM   2313 N N   . HIS A 1 295 ? -0.748  26.061  17.721  1.00 30.10  ? 298 HIS A N   1 
ATOM   2314 C CA  . HIS A 1 295 ? -1.133  24.838  17.025  1.00 29.83  ? 298 HIS A CA  1 
ATOM   2315 C C   . HIS A 1 295 ? 0.004   24.350  16.134  1.00 28.76  ? 298 HIS A C   1 
ATOM   2316 O O   . HIS A 1 295 ? 0.714   25.163  15.532  1.00 28.57  ? 298 HIS A O   1 
ATOM   2317 C CB  . HIS A 1 295 ? -2.397  25.068  16.193  1.00 30.88  ? 298 HIS A CB  1 
ATOM   2318 C CG  . HIS A 1 295 ? -3.180  23.821  15.924  1.00 34.72  ? 298 HIS A CG  1 
ATOM   2319 N ND1 . HIS A 1 295 ? -2.870  22.953  14.900  1.00 34.26  ? 298 HIS A ND1 1 
ATOM   2320 C CD2 . HIS A 1 295 ? -4.266  23.300  16.543  1.00 33.66  ? 298 HIS A CD2 1 
ATOM   2321 C CE1 . HIS A 1 295 ? -3.728  21.949  14.902  1.00 32.83  ? 298 HIS A CE1 1 
ATOM   2322 N NE2 . HIS A 1 295 ? -4.585  22.136  15.888  1.00 34.46  ? 298 HIS A NE2 1 
ATOM   2323 N N   . PRO A 1 296 ? 0.211   23.033  16.025  1.00 37.18  ? 299 PRO A N   1 
ATOM   2324 C CA  . PRO A 1 296 ? 1.278   22.527  15.142  1.00 27.37  ? 299 PRO A CA  1 
ATOM   2325 C C   . PRO A 1 296 ? 0.955   22.598  13.661  1.00 27.67  ? 299 PRO A C   1 
ATOM   2326 O O   . PRO A 1 296 ? 1.888   22.624  12.849  1.00 33.18  ? 299 PRO A O   1 
ATOM   2327 C CB  . PRO A 1 296 ? 1.444   21.069  15.593  1.00 26.97  ? 299 PRO A CB  1 
ATOM   2328 C CG  . PRO A 1 296 ? 0.144   20.716  16.214  1.00 27.77  ? 299 PRO A CG  1 
ATOM   2329 C CD  . PRO A 1 296 ? -0.379  21.966  16.854  1.00 28.41  ? 299 PRO A CD  1 
ATOM   2330 N N   . VAL A 1 297 ? -0.318  22.610  13.284  1.00 33.49  ? 300 VAL A N   1 
ATOM   2331 C CA  . VAL A 1 297 ? -0.704  22.732  11.883  1.00 31.44  ? 300 VAL A CA  1 
ATOM   2332 C C   . VAL A 1 297 ? -0.637  24.201  11.492  1.00 32.15  ? 300 VAL A C   1 
ATOM   2333 O O   . VAL A 1 297 ? -1.332  25.041  12.073  1.00 42.52  ? 300 VAL A O   1 
ATOM   2334 C CB  . VAL A 1 297 ? -2.106  22.155  11.643  1.00 30.45  ? 300 VAL A CB  1 
ATOM   2335 C CG1 . VAL A 1 297 ? -2.523  22.358  10.199  1.00 30.66  ? 300 VAL A CG1 1 
ATOM   2336 C CG2 . VAL A 1 297 ? -2.128  20.681  11.999  1.00 29.55  ? 300 VAL A CG2 1 
ATOM   2337 N N   . THR A 1 298 ? 0.209   24.515  10.516  1.00 30.23  ? 301 THR A N   1 
ATOM   2338 C CA  . THR A 1 298 ? 0.451   25.887  10.103  1.00 34.65  ? 301 THR A CA  1 
ATOM   2339 C C   . THR A 1 298 ? 0.374   25.993  8.587   1.00 36.71  ? 301 THR A C   1 
ATOM   2340 O O   . THR A 1 298 ? 0.634   25.029  7.863   1.00 43.77  ? 301 THR A O   1 
ATOM   2341 C CB  . THR A 1 298 ? 1.822   26.390  10.588  1.00 39.42  ? 301 THR A CB  1 
ATOM   2342 O OG1 . THR A 1 298 ? 2.859   25.539  10.083  1.00 51.78  ? 301 THR A OG1 1 
ATOM   2343 C CG2 . THR A 1 298 ? 1.879   26.407  12.109  1.00 31.77  ? 301 THR A CG2 1 
ATOM   2344 N N   . ILE A 1 299 ? 0.008   27.182  8.119   1.00 31.81  ? 302 ILE A N   1 
ATOM   2345 C CA  . ILE A 1 299 ? -0.043  27.497  6.697   1.00 32.76  ? 302 ILE A CA  1 
ATOM   2346 C C   . ILE A 1 299 ? 0.509   28.903  6.515   1.00 33.46  ? 302 ILE A C   1 
ATOM   2347 O O   . ILE A 1 299 ? 0.125   29.824  7.243   1.00 33.96  ? 302 ILE A O   1 
ATOM   2348 C CB  . ILE A 1 299 ? -1.475  27.385  6.133   1.00 45.92  ? 302 ILE A CB  1 
ATOM   2349 C CG1 . ILE A 1 299 ? -1.893  25.916  6.039   1.00 44.06  ? 302 ILE A CG1 1 
ATOM   2350 C CG2 . ILE A 1 299 ? -1.581  28.066  4.777   1.00 35.34  ? 302 ILE A CG2 1 
ATOM   2351 C CD1 . ILE A 1 299 ? -3.313  25.716  5.589   1.00 53.16  ? 302 ILE A CD1 1 
ATOM   2352 N N   . GLY A 1 300 ? 1.421   29.064  5.561   1.00 35.95  ? 303 GLY A N   1 
ATOM   2353 C CA  . GLY A 1 300 ? 2.059   30.345  5.338   1.00 42.52  ? 303 GLY A CA  1 
ATOM   2354 C C   . GLY A 1 300 ? 3.428   30.434  5.979   1.00 43.42  ? 303 GLY A C   1 
ATOM   2355 O O   . GLY A 1 300 ? 4.194   29.466  5.963   1.00 43.30  ? 303 GLY A O   1 
ATOM   2356 N N   . GLU A 1 301 ? 3.747   31.590  6.547   1.00 51.86  ? 304 GLU A N   1 
ATOM   2357 C CA  . GLU A 1 301 ? 5.024   31.825  7.216   1.00 50.63  ? 304 GLU A CA  1 
ATOM   2358 C C   . GLU A 1 301 ? 4.726   32.001  8.701   1.00 48.64  ? 304 GLU A C   1 
ATOM   2359 O O   . GLU A 1 301 ? 4.273   33.066  9.131   1.00 54.97  ? 304 GLU A O   1 
ATOM   2360 C CB  . GLU A 1 301 ? 5.728   33.039  6.619   1.00 60.73  ? 304 GLU A CB  1 
ATOM   2361 C CG  . GLU A 1 301 ? 5.764   33.024  5.098   1.00 66.87  ? 304 GLU A CG  1 
ATOM   2362 C CD  . GLU A 1 301 ? 6.557   34.175  4.516   1.00 70.91  ? 304 GLU A CD  1 
ATOM   2363 O OE1 . GLU A 1 301 ? 7.803   34.102  4.525   1.00 70.37  ? 304 GLU A OE1 1 
ATOM   2364 O OE2 . GLU A 1 301 ? 5.933   35.154  4.057   1.00 77.62  ? 304 GLU A OE2 1 
ATOM   2365 N N   . CYS A 1 302 ? 4.976   30.954  9.477   1.00 31.21  ? 305 CYS A N   1 
ATOM   2366 C CA  . CYS A 1 302 ? 4.580   30.875  10.872  1.00 30.72  ? 305 CYS A CA  1 
ATOM   2367 C C   . CYS A 1 302 ? 5.792   30.703  11.778  1.00 29.81  ? 305 CYS A C   1 
ATOM   2368 O O   . CYS A 1 302 ? 6.879   30.334  11.319  1.00 38.52  ? 305 CYS A O   1 
ATOM   2369 C CB  . CYS A 1 302 ? 3.616   29.701  11.099  1.00 34.41  ? 305 CYS A CB  1 
ATOM   2370 S SG  . CYS A 1 302 ? 1.973   29.879  10.376  1.00 44.48  ? 305 CYS A SG  1 
ATOM   2371 N N   . PRO A 1 303 ? 5.640   30.969  13.072  1.00 34.48  ? 306 PRO A N   1 
ATOM   2372 C CA  . PRO A 1 303 ? 6.673   30.569  14.030  1.00 28.81  ? 306 PRO A CA  1 
ATOM   2373 C C   . PRO A 1 303 ? 6.694   29.060  14.217  1.00 28.49  ? 306 PRO A C   1 
ATOM   2374 O O   . PRO A 1 303 ? 5.745   28.347  13.887  1.00 45.68  ? 306 PRO A O   1 
ATOM   2375 C CB  . PRO A 1 303 ? 6.260   31.281  15.324  1.00 31.50  ? 306 PRO A CB  1 
ATOM   2376 C CG  . PRO A 1 303 ? 5.338   32.364  14.896  1.00 30.46  ? 306 PRO A CG  1 
ATOM   2377 C CD  . PRO A 1 303 ? 4.625   31.837  13.692  1.00 30.58  ? 306 PRO A CD  1 
ATOM   2378 N N   . LYS A 1 304 ? 7.805   28.577  14.764  1.00 27.80  ? 307 LYS A N   1 
ATOM   2379 C CA  . LYS A 1 304 ? 7.984   27.150  14.999  1.00 26.51  ? 307 LYS A CA  1 
ATOM   2380 C C   . LYS A 1 304 ? 7.200   26.719  16.233  1.00 28.21  ? 307 LYS A C   1 
ATOM   2381 O O   . LYS A 1 304 ? 7.335   27.319  17.304  1.00 44.27  ? 307 LYS A O   1 
ATOM   2382 C CB  . LYS A 1 304 ? 9.467   26.827  15.172  1.00 28.46  ? 307 LYS A CB  1 
ATOM   2383 C CG  . LYS A 1 304 ? 9.749   25.409  15.634  1.00 37.41  ? 307 LYS A CG  1 
ATOM   2384 C CD  . LYS A 1 304 ? 9.532   24.401  14.519  1.00 47.80  ? 307 LYS A CD  1 
ATOM   2385 C CE  . LYS A 1 304 ? 10.636  24.478  13.479  1.00 47.91  ? 307 LYS A CE  1 
ATOM   2386 N NZ  . LYS A 1 304 ? 10.462  23.430  12.437  1.00 49.35  ? 307 LYS A NZ  1 
ATOM   2387 N N   . TYR A 1 305 ? 6.395   25.668  16.086  1.00 26.00  ? 308 TYR A N   1 
ATOM   2388 C CA  . TYR A 1 305 ? 5.541   25.212  17.174  1.00 26.13  ? 308 TYR A CA  1 
ATOM   2389 C C   . TYR A 1 305 ? 6.347   24.488  18.245  1.00 25.68  ? 308 TYR A C   1 
ATOM   2390 O O   . TYR A 1 305 ? 7.174   23.625  17.937  1.00 30.41  ? 308 TYR A O   1 
ATOM   2391 C CB  . TYR A 1 305 ? 4.444   24.287  16.654  1.00 26.24  ? 308 TYR A CB  1 
ATOM   2392 C CG  . TYR A 1 305 ? 3.619   23.694  17.771  1.00 26.53  ? 308 TYR A CG  1 
ATOM   2393 C CD1 . TYR A 1 305 ? 2.643   24.448  18.407  1.00 37.62  ? 308 TYR A CD1 1 
ATOM   2394 C CD2 . TYR A 1 305 ? 3.829   22.390  18.206  1.00 26.17  ? 308 TYR A CD2 1 
ATOM   2395 C CE1 . TYR A 1 305 ? 1.892   23.922  19.435  1.00 27.82  ? 308 TYR A CE1 1 
ATOM   2396 C CE2 . TYR A 1 305 ? 3.081   21.855  19.237  1.00 26.64  ? 308 TYR A CE2 1 
ATOM   2397 C CZ  . TYR A 1 305 ? 2.113   22.628  19.847  1.00 27.47  ? 308 TYR A CZ  1 
ATOM   2398 O OH  . TYR A 1 305 ? 1.360   22.109  20.873  1.00 39.38  ? 308 TYR A OH  1 
ATOM   2399 N N   . VAL A 1 306 ? 6.085   24.830  19.508  1.00 26.06  ? 309 VAL A N   1 
ATOM   2400 C CA  . VAL A 1 306 ? 6.677   24.155  20.657  1.00 25.92  ? 309 VAL A CA  1 
ATOM   2401 C C   . VAL A 1 306 ? 5.584   23.912  21.692  1.00 26.56  ? 309 VAL A C   1 
ATOM   2402 O O   . VAL A 1 306 ? 4.550   24.580  21.702  1.00 29.37  ? 309 VAL A O   1 
ATOM   2403 C CB  . VAL A 1 306 ? 7.842   24.968  21.274  1.00 32.56  ? 309 VAL A CB  1 
ATOM   2404 C CG1 . VAL A 1 306 ? 8.956   25.155  20.257  1.00 25.50  ? 309 VAL A CG1 1 
ATOM   2405 C CG2 . VAL A 1 306 ? 7.345   26.314  21.764  1.00 26.67  ? 309 VAL A CG2 1 
ATOM   2406 N N   . ARG A 1 307 ? 5.817   22.933  22.567  1.00 26.58  ? 310 ARG A N   1 
ATOM   2407 C CA  . ARG A 1 307 ? 4.864   22.587  23.618  1.00 29.82  ? 310 ARG A CA  1 
ATOM   2408 C C   . ARG A 1 307 ? 5.035   23.425  24.877  1.00 28.06  ? 310 ARG A C   1 
ATOM   2409 O O   . ARG A 1 307 ? 4.400   23.129  25.894  1.00 43.82  ? 310 ARG A O   1 
ATOM   2410 C CB  . ARG A 1 307 ? 4.981   21.108  23.998  1.00 27.35  ? 310 ARG A CB  1 
ATOM   2411 C CG  . ARG A 1 307 ? 4.749   20.131  22.873  1.00 30.67  ? 310 ARG A CG  1 
ATOM   2412 C CD  . ARG A 1 307 ? 4.539   18.733  23.426  1.00 28.84  ? 310 ARG A CD  1 
ATOM   2413 N NE  . ARG A 1 307 ? 5.047   17.705  22.523  1.00 36.05  ? 310 ARG A NE  1 
ATOM   2414 C CZ  . ARG A 1 307 ? 4.346   17.150  21.542  1.00 45.54  ? 310 ARG A CZ  1 
ATOM   2415 N NH1 . ARG A 1 307 ? 3.093   17.521  21.322  1.00 45.87  ? 310 ARG A NH1 1 
ATOM   2416 N NH2 . ARG A 1 307 ? 4.903   16.224  20.777  1.00 52.71  ? 310 ARG A NH2 1 
ATOM   2417 N N   . SER A 1 308 ? 5.871   24.454  24.834  1.00 28.48  ? 311 SER A N   1 
ATOM   2418 C CA  . SER A 1 308 ? 6.206   25.208  26.030  1.00 28.57  ? 311 SER A CA  1 
ATOM   2419 C C   . SER A 1 308 ? 5.088   26.170  26.414  1.00 29.58  ? 311 SER A C   1 
ATOM   2420 O O   . SER A 1 308 ? 4.334   26.658  25.568  1.00 29.66  ? 311 SER A O   1 
ATOM   2421 C CB  . SER A 1 308 ? 7.505   25.980  25.817  1.00 28.19  ? 311 SER A CB  1 
ATOM   2422 O OG  . SER A 1 308 ? 8.525   25.107  25.374  1.00 29.57  ? 311 SER A OG  1 
ATOM   2423 N N   . ALA A 1 309 ? 4.992   26.437  27.714  1.00 30.54  ? 312 ALA A N   1 
ATOM   2424 C CA  . ALA A 1 309 ? 4.063   27.417  28.256  1.00 31.75  ? 312 ALA A CA  1 
ATOM   2425 C C   . ALA A 1 309 ? 4.703   28.779  28.484  1.00 35.84  ? 312 ALA A C   1 
ATOM   2426 O O   . ALA A 1 309 ? 3.979   29.767  28.642  1.00 41.79  ? 312 ALA A O   1 
ATOM   2427 C CB  . ALA A 1 309 ? 3.471   26.911  29.576  1.00 32.90  ? 312 ALA A CB  1 
ATOM   2428 N N   . LYS A 1 310 ? 6.033   28.855  28.499  1.00 31.49  ? 313 LYS A N   1 
ATOM   2429 C CA  . LYS A 1 310 ? 6.733   30.096  28.804  1.00 33.29  ? 313 LYS A CA  1 
ATOM   2430 C C   . LYS A 1 310 ? 8.157   30.000  28.278  1.00 33.52  ? 313 LYS A C   1 
ATOM   2431 O O   . LYS A 1 310 ? 8.879   29.056  28.613  1.00 46.13  ? 313 LYS A O   1 
ATOM   2432 C CB  . LYS A 1 310 ? 6.728   30.362  30.314  1.00 38.04  ? 313 LYS A CB  1 
ATOM   2433 C CG  . LYS A 1 310 ? 7.436   31.638  30.734  1.00 60.62  ? 313 LYS A CG  1 
ATOM   2434 C CD  . LYS A 1 310 ? 7.382   31.818  32.245  1.00 62.53  ? 313 LYS A CD  1 
ATOM   2435 C CE  . LYS A 1 310 ? 8.141   33.059  32.691  1.00 60.25  ? 313 LYS A CE  1 
ATOM   2436 N NZ  . LYS A 1 310 ? 8.131   33.213  34.173  1.00 71.10  ? 313 LYS A NZ  1 
ATOM   2437 N N   . LEU A 1 311 ? 8.557   30.979  27.447  1.00 33.64  ? 314 LEU A N   1 
ATOM   2438 C CA  . LEU A 1 311 ? 9.916   31.073  26.898  1.00 30.31  ? 314 LEU A CA  1 
ATOM   2439 C C   . LEU A 1 311 ? 10.342  32.541  26.957  1.00 31.14  ? 314 LEU A C   1 
ATOM   2440 O O   . LEU A 1 311 ? 10.337  33.256  25.952  1.00 32.61  ? 314 LEU A O   1 
ATOM   2441 C CB  . LEU A 1 311 ? 9.994   30.526  25.473  1.00 29.29  ? 314 LEU A CB  1 
ATOM   2442 C CG  . LEU A 1 311 ? 10.246  29.024  25.324  1.00 43.39  ? 314 LEU A CG  1 
ATOM   2443 C CD1 . LEU A 1 311 ? 10.284  28.633  23.858  1.00 31.99  ? 314 LEU A CD1 1 
ATOM   2444 C CD2 . LEU A 1 311 ? 11.536  28.626  26.021  1.00 38.14  ? 314 LEU A CD2 1 
ATOM   2445 N N   . ARG A 1 312 ? 10.719  32.990  28.150  1.00 32.01  ? 315 ARG A N   1 
ATOM   2446 C CA  . ARG A 1 312 ? 11.108  34.373  28.385  1.00 33.04  ? 315 ARG A CA  1 
ATOM   2447 C C   . ARG A 1 312 ? 12.619  34.455  28.552  1.00 33.60  ? 315 ARG A C   1 
ATOM   2448 O O   . ARG A 1 312 ? 13.196  33.752  29.388  1.00 32.92  ? 315 ARG A O   1 
ATOM   2449 C CB  . ARG A 1 312 ? 10.399  34.943  29.616  1.00 35.42  ? 315 ARG A CB  1 
ATOM   2450 C CG  . ARG A 1 312 ? 10.743  36.392  29.910  1.00 47.14  ? 315 ARG A CG  1 
ATOM   2451 C CD  . ARG A 1 312 ? 9.776   37.004  30.911  1.00 42.60  ? 315 ARG A CD  1 
ATOM   2452 N NE  . ARG A 1 312 ? 8.440   37.151  30.344  1.00 42.75  ? 315 ARG A NE  1 
ATOM   2453 C CZ  . ARG A 1 312 ? 8.047   38.188  29.612  1.00 43.63  ? 315 ARG A CZ  1 
ATOM   2454 N NH1 . ARG A 1 312 ? 8.891   39.176  29.357  1.00 38.43  ? 315 ARG A NH1 1 
ATOM   2455 N NH2 . ARG A 1 312 ? 6.811   38.235  29.135  1.00 53.75  ? 315 ARG A NH2 1 
ATOM   2456 N N   . MET A 1 313 ? 13.248  35.316  27.759  1.00 36.47  ? 316 MET A N   1 
ATOM   2457 C CA  . MET A 1 313 ? 14.693  35.488  27.744  1.00 33.78  ? 316 MET A CA  1 
ATOM   2458 C C   . MET A 1 313 ? 15.053  36.810  28.407  1.00 44.20  ? 316 MET A C   1 
ATOM   2459 O O   . MET A 1 313 ? 14.521  37.860  28.035  1.00 45.67  ? 316 MET A O   1 
ATOM   2460 C CB  . MET A 1 313 ? 15.217  35.446  26.309  1.00 32.59  ? 316 MET A CB  1 
ATOM   2461 C CG  . MET A 1 313 ? 16.718  35.579  26.180  1.00 48.97  ? 316 MET A CG  1 
ATOM   2462 S SD  . MET A 1 313 ? 17.283  35.102  24.538  1.00 38.67  ? 316 MET A SD  1 
ATOM   2463 C CE  . MET A 1 313 ? 16.928  33.351  24.566  1.00 42.43  ? 316 MET A CE  1 
ATOM   2464 N N   . VAL A 1 314 ? 15.956  36.759  29.381  1.00 44.89  ? 317 VAL A N   1 
ATOM   2465 C CA  . VAL A 1 314 ? 16.333  37.954  30.128  1.00 40.80  ? 317 VAL A CA  1 
ATOM   2466 C C   . VAL A 1 314 ? 17.278  38.803  29.288  1.00 44.16  ? 317 VAL A C   1 
ATOM   2467 O O   . VAL A 1 314 ? 18.222  38.290  28.675  1.00 40.13  ? 317 VAL A O   1 
ATOM   2468 C CB  . VAL A 1 314 ? 16.967  37.578  31.478  1.00 37.30  ? 317 VAL A CB  1 
ATOM   2469 C CG1 . VAL A 1 314 ? 18.119  36.611  31.288  1.00 36.54  ? 317 VAL A CG1 1 
ATOM   2470 C CG2 . VAL A 1 314 ? 17.439  38.825  32.218  1.00 38.98  ? 317 VAL A CG2 1 
ATOM   2471 N N   . THR A 1 315 ? 17.008  40.104  29.240  1.00 38.36  ? 318 THR A N   1 
ATOM   2472 C CA  . THR A 1 315 ? 17.902  41.084  28.639  1.00 39.23  ? 318 THR A CA  1 
ATOM   2473 C C   . THR A 1 315 ? 18.562  41.983  29.668  1.00 40.84  ? 318 THR A C   1 
ATOM   2474 O O   . THR A 1 315 ? 19.711  42.381  29.488  1.00 41.47  ? 318 THR A O   1 
ATOM   2475 C CB  . THR A 1 315 ? 17.141  41.956  27.638  1.00 39.65  ? 318 THR A CB  1 
ATOM   2476 O OG1 . THR A 1 315 ? 16.030  42.577  28.296  1.00 42.34  ? 318 THR A OG1 1 
ATOM   2477 C CG2 . THR A 1 315 ? 16.635  41.117  26.481  1.00 38.21  ? 318 THR A CG2 1 
ATOM   2478 N N   . GLY A 1 316 ? 17.857  42.306  30.742  1.00 41.66  ? 319 GLY A N   1 
ATOM   2479 C CA  . GLY A 1 316 ? 18.370  43.155  31.794  1.00 43.35  ? 319 GLY A CA  1 
ATOM   2480 C C   . GLY A 1 316 ? 19.116  42.386  32.860  1.00 43.32  ? 319 GLY A C   1 
ATOM   2481 O O   . GLY A 1 316 ? 19.759  41.365  32.596  1.00 42.18  ? 319 GLY A O   1 
ATOM   2482 N N   . LEU A 1 317 ? 19.021  42.882  34.087  1.00 53.70  ? 320 LEU A N   1 
ATOM   2483 C CA  . LEU A 1 317 ? 19.774  42.374  35.222  1.00 54.15  ? 320 LEU A CA  1 
ATOM   2484 C C   . LEU A 1 317 ? 18.840  41.680  36.203  1.00 53.46  ? 320 LEU A C   1 
ATOM   2485 O O   . LEU A 1 317 ? 17.616  41.724  36.071  1.00 55.78  ? 320 LEU A O   1 
ATOM   2486 C CB  . LEU A 1 317 ? 20.521  43.511  35.931  1.00 65.73  ? 320 LEU A CB  1 
ATOM   2487 C CG  . LEU A 1 317 ? 21.722  44.203  35.282  1.00 55.63  ? 320 LEU A CG  1 
ATOM   2488 C CD1 . LEU A 1 317 ? 21.373  44.924  33.990  1.00 57.87  ? 320 LEU A CD1 1 
ATOM   2489 C CD2 . LEU A 1 317 ? 22.307  45.180  36.270  1.00 54.58  ? 320 LEU A CD2 1 
ATOM   2490 N N   . ARG A 1 318 ? 19.439  41.035  37.202  1.00 56.26  ? 321 ARG A N   1 
ATOM   2491 C CA  . ARG A 1 318 ? 18.669  40.542  38.336  1.00 53.85  ? 321 ARG A CA  1 
ATOM   2492 C C   . ARG A 1 318 ? 18.155  41.732  39.136  1.00 53.28  ? 321 ARG A C   1 
ATOM   2493 O O   . ARG A 1 318 ? 18.945  42.534  39.643  1.00 53.57  ? 321 ARG A O   1 
ATOM   2494 C CB  . ARG A 1 318 ? 19.523  39.626  39.210  1.00 51.48  ? 321 ARG A CB  1 
ATOM   2495 C CG  . ARG A 1 318 ? 18.748  38.977  40.350  1.00 73.94  ? 321 ARG A CG  1 
ATOM   2496 C CD  . ARG A 1 318 ? 19.562  37.909  41.063  1.00 72.87  ? 321 ARG A CD  1 
ATOM   2497 N NE  . ARG A 1 318 ? 20.315  37.077  40.130  1.00 61.86  ? 321 ARG A NE  1 
ATOM   2498 C CZ  . ARG A 1 318 ? 20.481  35.766  40.264  1.00 64.13  ? 321 ARG A CZ  1 
ATOM   2499 N NH1 . ARG A 1 318 ? 19.931  35.126  41.286  1.00 65.85  ? 321 ARG A NH1 1 
ATOM   2500 N NH2 . ARG A 1 318 ? 21.187  35.092  39.366  1.00 62.92  ? 321 ARG A NH2 1 
ATOM   2501 N N   . ASN A 1 319 ? 16.834  41.856  39.236  1.00 49.45  ? 322 ASN A N   1 
ATOM   2502 C CA  . ASN A 1 319 ? 16.206  43.025  39.848  1.00 50.11  ? 322 ASN A CA  1 
ATOM   2503 C C   . ASN A 1 319 ? 16.350  42.925  41.361  1.00 51.85  ? 322 ASN A C   1 
ATOM   2504 O O   . ASN A 1 319 ? 15.643  42.157  42.017  1.00 51.82  ? 322 ASN A O   1 
ATOM   2505 C CB  . ASN A 1 319 ? 14.743  43.120  39.433  1.00 53.54  ? 322 ASN A CB  1 
ATOM   2506 C CG  . ASN A 1 319 ? 14.152  44.488  39.694  1.00 51.80  ? 322 ASN A CG  1 
ATOM   2507 O OD1 . ASN A 1 319 ? 14.877  45.476  39.807  1.00 53.01  ? 322 ASN A OD1 1 
ATOM   2508 N ND2 . ASN A 1 319 ? 12.829  44.556  39.786  1.00 58.96  ? 322 ASN A ND2 1 
ATOM   2509 N N   . ILE A 1 320 ? 17.270  43.707  41.919  1.00 53.28  ? 323 ILE A N   1 
ATOM   2510 C CA  . ILE A 1 320 ? 17.524  43.716  43.358  1.00 67.04  ? 323 ILE A CA  1 
ATOM   2511 C C   . ILE A 1 320 ? 17.300  45.128  43.890  1.00 73.96  ? 323 ILE A C   1 
ATOM   2512 O O   . ILE A 1 320 ? 18.273  45.859  44.127  1.00 76.73  ? 323 ILE A O   1 
ATOM   2513 C CB  . ILE A 1 320 ? 18.945  43.226  43.676  1.00 57.44  ? 323 ILE A CB  1 
ATOM   2514 C CG1 . ILE A 1 320 ? 19.289  41.999  42.832  1.00 55.43  ? 323 ILE A CG1 1 
ATOM   2515 C CG2 . ILE A 1 320 ? 19.077  42.904  45.157  1.00 68.79  ? 323 ILE A CG2 1 
ATOM   2516 C CD1 . ILE A 1 320 ? 20.717  41.535  42.985  1.00 52.79  ? 323 ILE A CD1 1 
ATOM   2517 N N   . PRO A 1 321 ? 16.051  45.557  44.089  1.00 84.83  ? 324 PRO A N   1 
ATOM   2518 C CA  . PRO A 1 321 ? 15.807  46.935  44.528  1.00 85.45  ? 324 PRO A CA  1 
ATOM   2519 C C   . PRO A 1 321 ? 15.522  47.059  46.018  1.00 86.20  ? 324 PRO A C   1 
ATOM   2520 O O   . PRO A 1 321 ? 15.109  46.090  46.663  1.00 94.75  ? 324 PRO A O   1 
ATOM   2521 C CB  . PRO A 1 321 ? 14.586  47.342  43.694  1.00 84.27  ? 324 PRO A CB  1 
ATOM   2522 C CG  . PRO A 1 321 ? 13.887  46.019  43.347  1.00 84.69  ? 324 PRO A CG  1 
ATOM   2523 C CD  . PRO A 1 321 ? 14.793  44.874  43.751  1.00 87.78  ? 324 PRO A CD  1 
ATOM   2524 N N   . SER A 1 322 ? 15.736  48.258  46.558  1.00 101.38 ? 325 SER A N   1 
ATOM   2525 C CA  . SER A 1 322 ? 15.451  48.587  47.958  1.00 106.88 ? 325 SER A CA  1 
ATOM   2526 C C   . SER A 1 322 ? 15.950  47.527  48.939  1.00 109.67 ? 325 SER A C   1 
ATOM   2527 O O   . SER A 1 322 ? 16.992  47.694  49.573  1.00 109.44 ? 325 SER A O   1 
ATOM   2528 C CB  . SER A 1 322 ? 13.948  48.813  48.157  1.00 101.97 ? 325 SER A CB  1 
ATOM   2529 O OG  . SER A 1 322 ? 13.201  47.642  47.881  1.00 101.60 ? 325 SER A OG  1 
ATOM   2530 N N   . GLY B 2 1   ? 26.808  35.630  41.777  1.00 49.29  ? 1   GLY B N   1 
ATOM   2531 C CA  . GLY B 2 1   ? 27.307  35.930  40.449  1.00 48.22  ? 1   GLY B CA  1 
ATOM   2532 C C   . GLY B 2 1   ? 28.691  35.361  40.213  1.00 48.59  ? 1   GLY B C   1 
ATOM   2533 O O   . GLY B 2 1   ? 29.460  35.190  41.153  1.00 50.16  ? 1   GLY B O   1 
ATOM   2534 N N   . LEU B 2 2   ? 29.006  35.068  38.948  1.00 47.61  ? 2   LEU B N   1 
ATOM   2535 C CA  . LEU B 2 2   ? 30.296  34.459  38.631  1.00 55.99  ? 2   LEU B CA  1 
ATOM   2536 C C   . LEU B 2 2   ? 31.455  35.397  38.942  1.00 49.57  ? 2   LEU B C   1 
ATOM   2537 O O   . LEU B 2 2   ? 32.537  34.946  39.338  1.00 50.76  ? 2   LEU B O   1 
ATOM   2538 C CB  . LEU B 2 2   ? 30.342  34.040  37.163  1.00 55.84  ? 2   LEU B CB  1 
ATOM   2539 C CG  . LEU B 2 2   ? 29.696  32.710  36.780  1.00 44.50  ? 2   LEU B CG  1 
ATOM   2540 C CD1 . LEU B 2 2   ? 30.104  32.335  35.368  1.00 43.44  ? 2   LEU B CD1 1 
ATOM   2541 C CD2 . LEU B 2 2   ? 30.081  31.620  37.760  1.00 45.31  ? 2   LEU B CD2 1 
ATOM   2542 N N   . PHE B 2 3   ? 31.251  36.701  38.769  1.00 50.02  ? 3   PHE B N   1 
ATOM   2543 C CA  . PHE B 2 3   ? 32.311  37.689  38.904  1.00 56.95  ? 3   PHE B CA  1 
ATOM   2544 C C   . PHE B 2 3   ? 32.190  38.505  40.184  1.00 53.61  ? 3   PHE B C   1 
ATOM   2545 O O   . PHE B 2 3   ? 32.869  39.527  40.324  1.00 55.19  ? 3   PHE B O   1 
ATOM   2546 C CB  . PHE B 2 3   ? 32.324  38.601  37.676  1.00 51.36  ? 3   PHE B CB  1 
ATOM   2547 C CG  . PHE B 2 3   ? 32.633  37.878  36.402  1.00 50.01  ? 3   PHE B CG  1 
ATOM   2548 C CD1 . PHE B 2 3   ? 31.628  37.264  35.673  1.00 52.06  ? 3   PHE B CD1 1 
ATOM   2549 C CD2 . PHE B 2 3   ? 33.934  37.792  35.945  1.00 50.93  ? 3   PHE B CD2 1 
ATOM   2550 C CE1 . PHE B 2 3   ? 31.919  36.586  34.501  1.00 46.88  ? 3   PHE B CE1 1 
ATOM   2551 C CE2 . PHE B 2 3   ? 34.228  37.118  34.775  1.00 57.71  ? 3   PHE B CE2 1 
ATOM   2552 C CZ  . PHE B 2 3   ? 33.220  36.515  34.053  1.00 47.85  ? 3   PHE B CZ  1 
ATOM   2553 N N   . GLY B 2 4   ? 31.338  38.078  41.114  1.00 53.53  ? 4   GLY B N   1 
ATOM   2554 C CA  . GLY B 2 4   ? 31.273  38.650  42.445  1.00 55.42  ? 4   GLY B CA  1 
ATOM   2555 C C   . GLY B 2 4   ? 30.851  40.098  42.544  1.00 56.53  ? 4   GLY B C   1 
ATOM   2556 O O   . GLY B 2 4   ? 30.931  40.670  43.633  1.00 58.17  ? 4   GLY B O   1 
ATOM   2557 N N   . ALA B 2 5   ? 30.395  40.717  41.459  1.00 61.60  ? 5   ALA B N   1 
ATOM   2558 C CA  . ALA B 2 5   ? 29.977  42.123  41.517  1.00 57.98  ? 5   ALA B CA  1 
ATOM   2559 C C   . ALA B 2 5   ? 28.495  42.226  41.858  1.00 55.60  ? 5   ALA B C   1 
ATOM   2560 O O   . ALA B 2 5   ? 28.132  42.628  42.969  1.00 57.08  ? 5   ALA B O   1 
ATOM   2561 C CB  . ALA B 2 5   ? 30.298  42.830  40.200  1.00 55.74  ? 5   ALA B CB  1 
ATOM   2562 N N   . ILE B 2 6   ? 27.629  41.865  40.912  1.00 53.62  ? 6   ILE B N   1 
ATOM   2563 C CA  . ILE B 2 6   ? 26.192  41.925  41.145  1.00 53.07  ? 6   ILE B CA  1 
ATOM   2564 C C   . ILE B 2 6   ? 25.812  40.886  42.189  1.00 58.01  ? 6   ILE B C   1 
ATOM   2565 O O   . ILE B 2 6   ? 26.194  39.713  42.087  1.00 52.19  ? 6   ILE B O   1 
ATOM   2566 C CB  . ILE B 2 6   ? 25.428  41.719  39.830  1.00 51.02  ? 6   ILE B CB  1 
ATOM   2567 C CG1 . ILE B 2 6   ? 25.761  42.850  38.854  1.00 51.33  ? 6   ILE B CG1 1 
ATOM   2568 C CG2 . ILE B 2 6   ? 23.928  41.639  40.084  1.00 50.49  ? 6   ILE B CG2 1 
ATOM   2569 C CD1 . ILE B 2 6   ? 25.042  42.755  37.529  1.00 49.60  ? 6   ILE B CD1 1 
ATOM   2570 N N   . ALA B 2 7   ? 25.066  41.320  43.209  1.00 54.39  ? 7   ALA B N   1 
ATOM   2571 C CA  . ALA B 2 7   ? 24.755  40.503  44.382  1.00 55.06  ? 7   ALA B CA  1 
ATOM   2572 C C   . ALA B 2 7   ? 26.023  39.974  45.047  1.00 56.15  ? 7   ALA B C   1 
ATOM   2573 O O   . ALA B 2 7   ? 26.008  38.924  45.695  1.00 56.23  ? 7   ALA B O   1 
ATOM   2574 C CB  . ALA B 2 7   ? 23.807  39.351  44.035  1.00 53.23  ? 7   ALA B CB  1 
ATOM   2575 N N   . GLY B 2 8   ? 27.126  40.703  44.887  1.00 60.96  ? 8   GLY B N   1 
ATOM   2576 C CA  . GLY B 2 8   ? 28.386  40.357  45.511  1.00 61.99  ? 8   GLY B CA  1 
ATOM   2577 C C   . GLY B 2 8   ? 28.868  41.454  46.436  1.00 63.96  ? 8   GLY B C   1 
ATOM   2578 O O   . GLY B 2 8   ? 28.167  41.812  47.387  1.00 63.47  ? 8   GLY B O   1 
ATOM   2579 N N   . PHE B 2 9   ? 30.057  42.008  46.174  1.00 68.43  ? 9   PHE B N   1 
ATOM   2580 C CA  . PHE B 2 9   ? 30.532  43.101  47.011  1.00 64.55  ? 9   PHE B CA  1 
ATOM   2581 C C   . PHE B 2 9   ? 29.714  44.369  46.803  1.00 67.08  ? 9   PHE B C   1 
ATOM   2582 O O   . PHE B 2 9   ? 29.751  45.260  47.656  1.00 82.20  ? 9   PHE B O   1 
ATOM   2583 C CB  . PHE B 2 9   ? 32.029  43.362  46.783  1.00 65.68  ? 9   PHE B CB  1 
ATOM   2584 C CG  . PHE B 2 9   ? 32.391  43.774  45.380  1.00 64.49  ? 9   PHE B CG  1 
ATOM   2585 C CD1 . PHE B 2 9   ? 32.271  45.093  44.974  1.00 65.22  ? 9   PHE B CD1 1 
ATOM   2586 C CD2 . PHE B 2 9   ? 32.903  42.850  44.485  1.00 62.91  ? 9   PHE B CD2 1 
ATOM   2587 C CE1 . PHE B 2 9   ? 32.621  45.475  43.693  1.00 64.37  ? 9   PHE B CE1 1 
ATOM   2588 C CE2 . PHE B 2 9   ? 33.255  43.226  43.203  1.00 62.04  ? 9   PHE B CE2 1 
ATOM   2589 C CZ  . PHE B 2 9   ? 33.114  44.541  42.807  1.00 62.79  ? 9   PHE B CZ  1 
ATOM   2590 N N   . ILE B 2 10  ? 28.976  44.463  45.702  1.00 62.97  ? 10  ILE B N   1 
ATOM   2591 C CA  . ILE B 2 10  ? 27.922  45.456  45.532  1.00 63.14  ? 10  ILE B CA  1 
ATOM   2592 C C   . ILE B 2 10  ? 26.606  44.743  45.820  1.00 63.89  ? 10  ILE B C   1 
ATOM   2593 O O   . ILE B 2 10  ? 26.192  43.856  45.067  1.00 75.63  ? 10  ILE B O   1 
ATOM   2594 C CB  . ILE B 2 10  ? 27.936  46.071  44.128  1.00 62.03  ? 10  ILE B CB  1 
ATOM   2595 C CG1 . ILE B 2 10  ? 29.308  46.677  43.829  1.00 63.27  ? 10  ILE B CG1 1 
ATOM   2596 C CG2 . ILE B 2 10  ? 26.854  47.129  44.003  1.00 62.50  ? 10  ILE B CG2 1 
ATOM   2597 C CD1 . ILE B 2 10  ? 29.429  47.259  42.442  1.00 62.44  ? 10  ILE B CD1 1 
ATOM   2598 N N   . GLU B 2 11  ? 25.945  45.129  46.912  1.00 67.04  ? 11  GLU B N   1 
ATOM   2599 C CA  . GLU B 2 11  ? 24.883  44.298  47.470  1.00 64.47  ? 11  GLU B CA  1 
ATOM   2600 C C   . GLU B 2 11  ? 23.554  44.461  46.736  1.00 61.68  ? 11  GLU B C   1 
ATOM   2601 O O   . GLU B 2 11  ? 22.826  43.480  46.555  1.00 60.16  ? 11  GLU B O   1 
ATOM   2602 C CB  . GLU B 2 11  ? 24.708  44.606  48.958  1.00 83.81  ? 11  GLU B CB  1 
ATOM   2603 C CG  . GLU B 2 11  ? 25.835  44.079  49.835  1.00 99.65  ? 11  GLU B CG  1 
ATOM   2604 C CD  . GLU B 2 11  ? 25.689  44.486  51.289  1.00 104.49 ? 11  GLU B CD  1 
ATOM   2605 O OE1 . GLU B 2 11  ? 25.310  45.647  51.552  1.00 106.85 ? 11  GLU B OE1 1 
ATOM   2606 O OE2 . GLU B 2 11  ? 25.949  43.641  52.172  1.00 110.74 ? 11  GLU B OE2 1 
ATOM   2607 N N   . GLY B 2 12  ? 23.210  45.678  46.315  1.00 62.30  ? 12  GLY B N   1 
ATOM   2608 C CA  . GLY B 2 12  ? 21.895  45.936  45.763  1.00 63.64  ? 12  GLY B CA  1 
ATOM   2609 C C   . GLY B 2 12  ? 21.947  46.818  44.532  1.00 67.81  ? 12  GLY B C   1 
ATOM   2610 O O   . GLY B 2 12  ? 23.017  47.230  44.080  1.00 72.75  ? 12  GLY B O   1 
ATOM   2611 N N   . GLY B 2 13  ? 20.759  47.102  43.998  1.00 62.14  ? 13  GLY B N   1 
ATOM   2612 C CA  . GLY B 2 13  ? 20.621  47.939  42.822  1.00 59.82  ? 13  GLY B CA  1 
ATOM   2613 C C   . GLY B 2 13  ? 20.032  49.303  43.118  1.00 69.65  ? 13  GLY B C   1 
ATOM   2614 O O   . GLY B 2 13  ? 19.457  49.522  44.189  1.00 66.11  ? 13  GLY B O   1 
ATOM   2615 N N   . TRP B 2 14  ? 20.160  50.228  42.170  1.00 72.64  ? 14  TRP B N   1 
ATOM   2616 C CA  . TRP B 2 14  ? 19.716  51.607  42.343  1.00 64.35  ? 14  TRP B CA  1 
ATOM   2617 C C   . TRP B 2 14  ? 18.486  51.852  41.478  1.00 63.65  ? 14  TRP B C   1 
ATOM   2618 O O   . TRP B 2 14  ? 18.590  51.927  40.249  1.00 65.33  ? 14  TRP B O   1 
ATOM   2619 C CB  . TRP B 2 14  ? 20.831  52.585  41.979  1.00 65.62  ? 14  TRP B CB  1 
ATOM   2620 C CG  . TRP B 2 14  ? 22.036  52.486  42.855  1.00 77.77  ? 14  TRP B CG  1 
ATOM   2621 C CD1 . TRP B 2 14  ? 22.088  52.003  44.129  1.00 76.94  ? 14  TRP B CD1 1 
ATOM   2622 C CD2 . TRP B 2 14  ? 23.372  52.875  42.517  1.00 67.32  ? 14  TRP B CD2 1 
ATOM   2623 N NE1 . TRP B 2 14  ? 23.374  52.071  44.608  1.00 72.30  ? 14  TRP B NE1 1 
ATOM   2624 C CE2 . TRP B 2 14  ? 24.181  52.601  43.636  1.00 68.45  ? 14  TRP B CE2 1 
ATOM   2625 C CE3 . TRP B 2 14  ? 23.961  53.428  41.376  1.00 67.17  ? 14  TRP B CE3 1 
ATOM   2626 C CZ2 . TRP B 2 14  ? 25.548  52.862  43.649  1.00 69.42  ? 14  TRP B CZ2 1 
ATOM   2627 C CZ3 . TRP B 2 14  ? 25.316  53.687  41.390  1.00 68.15  ? 14  TRP B CZ3 1 
ATOM   2628 C CH2 . TRP B 2 14  ? 26.096  53.405  42.520  1.00 69.25  ? 14  TRP B CH2 1 
ATOM   2629 N N   . THR B 2 15  ? 17.325  51.989  42.120  1.00 64.59  ? 15  THR B N   1 
ATOM   2630 C CA  . THR B 2 15  ? 16.128  52.396  41.395  1.00 64.49  ? 15  THR B CA  1 
ATOM   2631 C C   . THR B 2 15  ? 16.216  53.835  40.904  1.00 66.32  ? 15  THR B C   1 
ATOM   2632 O O   . THR B 2 15  ? 15.520  54.194  39.948  1.00 66.01  ? 15  THR B O   1 
ATOM   2633 C CB  . THR B 2 15  ? 14.886  52.238  42.273  1.00 65.43  ? 15  THR B CB  1 
ATOM   2634 O OG1 . THR B 2 15  ? 15.083  52.933  43.510  1.00 68.02  ? 15  THR B OG1 1 
ATOM   2635 C CG2 . THR B 2 15  ? 14.607  50.772  42.554  1.00 63.54  ? 15  THR B CG2 1 
ATOM   2636 N N   . GLY B 2 16  ? 17.051  54.663  41.534  1.00 70.57  ? 16  GLY B N   1 
ATOM   2637 C CA  . GLY B 2 16  ? 17.183  56.059  41.153  1.00 78.09  ? 16  GLY B CA  1 
ATOM   2638 C C   . GLY B 2 16  ? 17.891  56.292  39.834  1.00 75.94  ? 16  GLY B C   1 
ATOM   2639 O O   . GLY B 2 16  ? 17.824  57.408  39.306  1.00 78.23  ? 16  GLY B O   1 
ATOM   2640 N N   . MET B 2 17  ? 18.569  55.282  39.297  1.00 67.29  ? 17  MET B N   1 
ATOM   2641 C CA  . MET B 2 17  ? 19.224  55.374  37.996  1.00 70.65  ? 17  MET B CA  1 
ATOM   2642 C C   . MET B 2 17  ? 18.294  54.759  36.956  1.00 64.14  ? 17  MET B C   1 
ATOM   2643 O O   . MET B 2 17  ? 18.054  53.548  36.970  1.00 71.74  ? 17  MET B O   1 
ATOM   2644 C CB  . MET B 2 17  ? 20.579  54.672  38.018  1.00 65.15  ? 17  MET B CB  1 
ATOM   2645 C CG  . MET B 2 17  ? 21.332  54.752  36.705  1.00 74.22  ? 17  MET B CG  1 
ATOM   2646 S SD  . MET B 2 17  ? 22.985  54.047  36.816  1.00 76.90  ? 17  MET B SD  1 
ATOM   2647 C CE  . MET B 2 17  ? 22.613  52.374  37.332  1.00 77.60  ? 17  MET B CE  1 
ATOM   2648 N N   . VAL B 2 18  ? 17.773  55.594  36.056  1.00 70.90  ? 18  VAL B N   1 
ATOM   2649 C CA  . VAL B 2 18  ? 16.712  55.203  35.140  1.00 75.61  ? 18  VAL B CA  1 
ATOM   2650 C C   . VAL B 2 18  ? 17.118  55.353  33.679  1.00 74.68  ? 18  VAL B C   1 
ATOM   2651 O O   . VAL B 2 18  ? 16.274  55.227  32.794  1.00 76.35  ? 18  VAL B O   1 
ATOM   2652 C CB  . VAL B 2 18  ? 15.421  55.997  35.420  1.00 78.20  ? 18  VAL B CB  1 
ATOM   2653 C CG1 . VAL B 2 18  ? 14.972  55.803  36.858  1.00 73.40  ? 18  VAL B CG1 1 
ATOM   2654 C CG2 . VAL B 2 18  ? 15.635  57.472  35.111  1.00 68.16  ? 18  VAL B CG2 1 
ATOM   2655 N N   . ASP B 2 19  ? 18.393  55.624  33.402  1.00 73.43  ? 19  ASP B N   1 
ATOM   2656 C CA  . ASP B 2 19  ? 18.842  55.853  32.033  1.00 73.71  ? 19  ASP B CA  1 
ATOM   2657 C C   . ASP B 2 19  ? 19.864  54.828  31.558  1.00 70.73  ? 19  ASP B C   1 
ATOM   2658 O O   . ASP B 2 19  ? 20.456  55.015  30.488  1.00 72.30  ? 19  ASP B O   1 
ATOM   2659 C CB  . ASP B 2 19  ? 19.419  57.265  31.892  1.00 79.34  ? 19  ASP B CB  1 
ATOM   2660 C CG  . ASP B 2 19  ? 20.534  57.541  32.878  1.00 89.39  ? 19  ASP B CG  1 
ATOM   2661 O OD1 . ASP B 2 19  ? 20.557  56.885  33.938  1.00 101.93 ? 19  ASP B OD1 1 
ATOM   2662 O OD2 . ASP B 2 19  ? 21.385  58.413  32.596  1.00 81.00  ? 19  ASP B OD2 1 
ATOM   2663 N N   . GLY B 2 20  ? 20.086  53.756  32.307  1.00 71.22  ? 20  GLY B N   1 
ATOM   2664 C CA  . GLY B 2 20  ? 21.056  52.763  31.882  1.00 57.76  ? 20  GLY B CA  1 
ATOM   2665 C C   . GLY B 2 20  ? 21.130  51.619  32.866  1.00 56.42  ? 20  GLY B C   1 
ATOM   2666 O O   . GLY B 2 20  ? 20.431  51.592  33.884  1.00 56.82  ? 20  GLY B O   1 
ATOM   2667 N N   . TRP B 2 21  ? 22.004  50.667  32.543  1.00 54.98  ? 21  TRP B N   1 
ATOM   2668 C CA  . TRP B 2 21  ? 22.180  49.459  33.343  1.00 53.67  ? 21  TRP B CA  1 
ATOM   2669 C C   . TRP B 2 21  ? 23.290  49.629  34.375  1.00 55.00  ? 21  TRP B C   1 
ATOM   2670 O O   . TRP B 2 21  ? 23.063  49.461  35.576  1.00 55.52  ? 21  TRP B O   1 
ATOM   2671 C CB  . TRP B 2 21  ? 22.481  48.266  32.430  1.00 53.76  ? 21  TRP B CB  1 
ATOM   2672 C CG  . TRP B 2 21  ? 21.271  47.644  31.810  1.00 49.84  ? 21  TRP B CG  1 
ATOM   2673 C CD1 . TRP B 2 21  ? 20.015  47.587  32.339  1.00 58.40  ? 21  TRP B CD1 1 
ATOM   2674 C CD2 . TRP B 2 21  ? 21.201  46.987  30.540  1.00 48.24  ? 21  TRP B CD2 1 
ATOM   2675 N NE1 . TRP B 2 21  ? 19.170  46.931  31.479  1.00 48.12  ? 21  TRP B NE1 1 
ATOM   2676 C CE2 . TRP B 2 21  ? 19.873  46.555  30.366  1.00 47.17  ? 21  TRP B CE2 1 
ATOM   2677 C CE3 . TRP B 2 21  ? 22.134  46.723  29.532  1.00 47.75  ? 21  TRP B CE3 1 
ATOM   2678 C CZ2 . TRP B 2 21  ? 19.452  45.873  29.226  1.00 45.86  ? 21  TRP B CZ2 1 
ATOM   2679 C CZ3 . TRP B 2 21  ? 21.716  46.046  28.402  1.00 46.22  ? 21  TRP B CZ3 1 
ATOM   2680 C CH2 . TRP B 2 21  ? 20.386  45.629  28.257  1.00 45.16  ? 21  TRP B CH2 1 
ATOM   2681 N N   . TYR B 2 22  ? 24.495  49.949  33.917  1.00 55.71  ? 22  TYR B N   1 
ATOM   2682 C CA  . TYR B 2 22  ? 25.647  50.149  34.784  1.00 66.94  ? 22  TYR B CA  1 
ATOM   2683 C C   . TYR B 2 22  ? 25.980  51.634  34.824  1.00 62.97  ? 22  TYR B C   1 
ATOM   2684 O O   . TYR B 2 22  ? 26.057  52.283  33.774  1.00 67.55  ? 22  TYR B O   1 
ATOM   2685 C CB  . TYR B 2 22  ? 26.850  49.344  34.289  1.00 58.83  ? 22  TYR B CB  1 
ATOM   2686 C CG  . TYR B 2 22  ? 26.477  48.120  33.478  1.00 53.87  ? 22  TYR B CG  1 
ATOM   2687 C CD1 . TYR B 2 22  ? 25.808  47.052  34.061  1.00 52.40  ? 22  TYR B CD1 1 
ATOM   2688 C CD2 . TYR B 2 22  ? 26.807  48.027  32.132  1.00 53.19  ? 22  TYR B CD2 1 
ATOM   2689 C CE1 . TYR B 2 22  ? 25.471  45.932  33.327  1.00 50.28  ? 22  TYR B CE1 1 
ATOM   2690 C CE2 . TYR B 2 22  ? 26.474  46.909  31.389  1.00 51.07  ? 22  TYR B CE2 1 
ATOM   2691 C CZ  . TYR B 2 22  ? 25.806  45.864  31.993  1.00 49.60  ? 22  TYR B CZ  1 
ATOM   2692 O OH  . TYR B 2 22  ? 25.468  44.745  31.267  1.00 47.62  ? 22  TYR B OH  1 
ATOM   2693 N N   . GLY B 2 23  ? 26.178  52.171  36.023  1.00 63.12  ? 23  GLY B N   1 
ATOM   2694 C CA  . GLY B 2 23  ? 26.401  53.594  36.146  1.00 63.97  ? 23  GLY B CA  1 
ATOM   2695 C C   . GLY B 2 23  ? 27.137  53.978  37.413  1.00 65.97  ? 23  GLY B C   1 
ATOM   2696 O O   . GLY B 2 23  ? 27.733  53.140  38.095  1.00 67.92  ? 23  GLY B O   1 
ATOM   2697 N N   . TYR B 2 24  ? 27.076  55.271  37.714  1.00 75.36  ? 24  TYR B N   1 
ATOM   2698 C CA  . TYR B 2 24  ? 27.832  55.909  38.779  1.00 70.82  ? 24  TYR B CA  1 
ATOM   2699 C C   . TYR B 2 24  ? 26.885  56.582  39.767  1.00 73.36  ? 24  TYR B C   1 
ATOM   2700 O O   . TYR B 2 24  ? 25.665  56.598  39.593  1.00 81.54  ? 24  TYR B O   1 
ATOM   2701 C CB  . TYR B 2 24  ? 28.805  56.947  38.215  1.00 72.85  ? 24  TYR B CB  1 
ATOM   2702 C CG  . TYR B 2 24  ? 29.769  56.436  37.170  1.00 71.81  ? 24  TYR B CG  1 
ATOM   2703 C CD1 . TYR B 2 24  ? 30.910  55.736  37.534  1.00 71.69  ? 24  TYR B CD1 1 
ATOM   2704 C CD2 . TYR B 2 24  ? 29.558  56.685  35.820  1.00 71.20  ? 24  TYR B CD2 1 
ATOM   2705 C CE1 . TYR B 2 24  ? 31.803  55.279  36.583  1.00 70.97  ? 24  TYR B CE1 1 
ATOM   2706 C CE2 . TYR B 2 24  ? 30.447  56.234  34.861  1.00 70.47  ? 24  TYR B CE2 1 
ATOM   2707 C CZ  . TYR B 2 24  ? 31.567  55.531  35.248  1.00 74.50  ? 24  TYR B CZ  1 
ATOM   2708 O OH  . TYR B 2 24  ? 32.454  55.078  34.298  1.00 81.95  ? 24  TYR B OH  1 
ATOM   2709 N N   . HIS B 2 25  ? 27.480  57.164  40.811  1.00 92.11  ? 25  HIS B N   1 
ATOM   2710 C CA  . HIS B 2 25  ? 26.734  57.967  41.780  1.00 97.94  ? 25  HIS B CA  1 
ATOM   2711 C C   . HIS B 2 25  ? 27.750  58.864  42.486  1.00 98.60  ? 25  HIS B C   1 
ATOM   2712 O O   . HIS B 2 25  ? 28.514  58.388  43.330  1.00 97.59  ? 25  HIS B O   1 
ATOM   2713 C CB  . HIS B 2 25  ? 25.981  57.092  42.767  1.00 99.85  ? 25  HIS B CB  1 
ATOM   2714 C CG  . HIS B 2 25  ? 25.483  57.828  43.969  1.00 111.69 ? 25  HIS B CG  1 
ATOM   2715 N ND1 . HIS B 2 25  ? 24.371  58.642  43.940  1.00 111.74 ? 25  HIS B ND1 1 
ATOM   2716 C CD2 . HIS B 2 25  ? 25.951  57.876  45.239  1.00 115.65 ? 25  HIS B CD2 1 
ATOM   2717 C CE1 . HIS B 2 25  ? 24.173  59.155  45.141  1.00 109.21 ? 25  HIS B CE1 1 
ATOM   2718 N NE2 . HIS B 2 25  ? 25.118  58.706  45.947  1.00 112.83 ? 25  HIS B NE2 1 
ATOM   2719 N N   . HIS B 2 26  ? 27.747  60.148  42.141  1.00 95.04  ? 26  HIS B N   1 
ATOM   2720 C CA  . HIS B 2 26  ? 28.741  61.077  42.656  1.00 84.72  ? 26  HIS B CA  1 
ATOM   2721 C C   . HIS B 2 26  ? 28.112  62.028  43.665  1.00 97.98  ? 26  HIS B C   1 
ATOM   2722 O O   . HIS B 2 26  ? 26.949  62.418  43.535  1.00 88.90  ? 26  HIS B O   1 
ATOM   2723 C CB  . HIS B 2 26  ? 29.398  61.875  41.521  1.00 87.42  ? 26  HIS B CB  1 
ATOM   2724 C CG  . HIS B 2 26  ? 28.514  62.924  40.923  1.00 89.78  ? 26  HIS B CG  1 
ATOM   2725 N ND1 . HIS B 2 26  ? 28.373  64.179  41.474  1.00 100.20 ? 26  HIS B ND1 1 
ATOM   2726 C CD2 . HIS B 2 26  ? 27.731  62.908  39.818  1.00 97.80  ? 26  HIS B CD2 1 
ATOM   2727 C CE1 . HIS B 2 26  ? 27.539  64.890  40.737  1.00 96.33  ? 26  HIS B CE1 1 
ATOM   2728 N NE2 . HIS B 2 26  ? 27.136  64.143  39.725  1.00 88.96  ? 26  HIS B NE2 1 
ATOM   2729 N N   . GLN B 2 27  ? 28.896  62.393  44.678  1.00 114.95 ? 27  GLN B N   1 
ATOM   2730 C CA  . GLN B 2 27  ? 28.457  63.331  45.711  1.00 119.37 ? 27  GLN B CA  1 
ATOM   2731 C C   . GLN B 2 27  ? 29.653  64.201  46.082  1.00 117.75 ? 27  GLN B C   1 
ATOM   2732 O O   . GLN B 2 27  ? 30.551  63.753  46.799  1.00 120.18 ? 27  GLN B O   1 
ATOM   2733 C CB  . GLN B 2 27  ? 27.907  62.602  46.932  1.00 119.89 ? 27  GLN B CB  1 
ATOM   2734 C CG  . GLN B 2 27  ? 27.468  63.541  48.045  1.00 130.52 ? 27  GLN B CG  1 
ATOM   2735 C CD  . GLN B 2 27  ? 27.385  62.862  49.396  1.00 132.00 ? 27  GLN B CD  1 
ATOM   2736 O OE1 . GLN B 2 27  ? 27.673  61.673  49.527  1.00 124.44 ? 27  GLN B OE1 1 
ATOM   2737 N NE2 . GLN B 2 27  ? 26.994  63.620  50.415  1.00 132.09 ? 27  GLN B NE2 1 
ATOM   2738 N N   . ASN B 2 28  ? 29.661  65.436  45.596  1.00 109.46 ? 28  ASN B N   1 
ATOM   2739 C CA  . ASN B 2 28  ? 30.706  66.399  45.906  1.00 100.87 ? 28  ASN B CA  1 
ATOM   2740 C C   . ASN B 2 28  ? 30.073  67.672  46.469  1.00 123.04 ? 28  ASN B C   1 
ATOM   2741 O O   . ASN B 2 28  ? 28.870  67.724  46.748  1.00 120.50 ? 28  ASN B O   1 
ATOM   2742 C CB  . ASN B 2 28  ? 31.566  66.686  44.670  1.00 100.78 ? 28  ASN B CB  1 
ATOM   2743 C CG  . ASN B 2 28  ? 30.753  67.170  43.478  1.00 100.14 ? 28  ASN B CG  1 
ATOM   2744 O OD1 . ASN B 2 28  ? 29.594  67.561  43.609  1.00 100.45 ? 28  ASN B OD1 1 
ATOM   2745 N ND2 . ASN B 2 28  ? 31.369  67.149  42.301  1.00 99.43  ? 28  ASN B ND2 1 
ATOM   2746 N N   . GLU B 2 29  ? 30.901  68.709  46.623  1.00 129.71 ? 29  GLU B N   1 
ATOM   2747 C CA  . GLU B 2 29  ? 30.418  69.975  47.165  1.00 133.94 ? 29  GLU B CA  1 
ATOM   2748 C C   . GLU B 2 29  ? 29.292  70.551  46.314  1.00 133.12 ? 29  GLU B C   1 
ATOM   2749 O O   . GLU B 2 29  ? 28.367  71.184  46.839  1.00 138.74 ? 29  GLU B O   1 
ATOM   2750 C CB  . GLU B 2 29  ? 31.577  70.968  47.273  1.00 147.34 ? 29  GLU B CB  1 
ATOM   2751 C CG  . GLU B 2 29  ? 31.193  72.333  47.822  1.00 152.04 ? 29  GLU B CG  1 
ATOM   2752 C CD  . GLU B 2 29  ? 30.772  72.288  49.278  1.00 156.76 ? 29  GLU B CD  1 
ATOM   2753 O OE1 . GLU B 2 29  ? 31.152  71.331  49.984  1.00 156.31 ? 29  GLU B OE1 1 
ATOM   2754 O OE2 . GLU B 2 29  ? 30.057  73.213  49.718  1.00 159.80 ? 29  GLU B OE2 1 
ATOM   2755 N N   . GLN B 2 30  ? 29.346  70.335  44.998  1.00 118.67 ? 30  GLN B N   1 
ATOM   2756 C CA  . GLN B 2 30  ? 28.319  70.861  44.108  1.00 118.51 ? 30  GLN B CA  1 
ATOM   2757 C C   . GLN B 2 30  ? 27.024  70.063  44.164  1.00 124.08 ? 30  GLN B C   1 
ATOM   2758 O O   . GLN B 2 30  ? 26.018  70.505  43.597  1.00 117.63 ? 30  GLN B O   1 
ATOM   2759 C CB  . GLN B 2 30  ? 28.833  70.897  42.668  1.00 118.20 ? 30  GLN B CB  1 
ATOM   2760 C CG  . GLN B 2 30  ? 30.207  71.536  42.512  1.00 116.39 ? 30  GLN B CG  1 
ATOM   2761 C CD  . GLN B 2 30  ? 30.565  71.797  41.062  1.00 119.75 ? 30  GLN B CD  1 
ATOM   2762 O OE1 . GLN B 2 30  ? 31.658  71.459  40.609  1.00 112.96 ? 30  GLN B OE1 1 
ATOM   2763 N NE2 . GLN B 2 30  ? 29.644  72.409  40.327  1.00 127.94 ? 30  GLN B NE2 1 
ATOM   2764 N N   . GLY B 2 31  ? 27.017  68.914  44.827  1.00 129.58 ? 31  GLY B N   1 
ATOM   2765 C CA  . GLY B 2 31  ? 25.831  68.097  44.938  1.00 124.99 ? 31  GLY B CA  1 
ATOM   2766 C C   . GLY B 2 31  ? 26.107  66.664  44.549  1.00 118.54 ? 31  GLY B C   1 
ATOM   2767 O O   . GLY B 2 31  ? 27.238  66.269  44.271  1.00 117.20 ? 31  GLY B O   1 
ATOM   2768 N N   . SER B 2 32  ? 25.041  65.877  44.532  1.00 104.61 ? 32  SER B N   1 
ATOM   2769 C CA  . SER B 2 32  ? 25.106  64.459  44.221  1.00 102.17 ? 32  SER B CA  1 
ATOM   2770 C C   . SER B 2 32  ? 24.218  64.154  43.020  1.00 102.33 ? 32  SER B C   1 
ATOM   2771 O O   . SER B 2 32  ? 23.515  65.015  42.501  1.00 93.28  ? 32  SER B O   1 
ATOM   2772 C CB  . SER B 2 32  ? 24.692  63.623  45.432  1.00 93.82  ? 32  SER B CB  1 
ATOM   2773 O OG  . SER B 2 32  ? 23.414  64.022  45.890  1.00 94.17  ? 32  SER B OG  1 
ATOM   2774 N N   . GLY B 2 33  ? 24.259  62.909  42.581  1.00 101.45 ? 33  GLY B N   1 
ATOM   2775 C CA  . GLY B 2 33  ? 23.450  62.482  41.460  1.00 105.52 ? 33  GLY B CA  1 
ATOM   2776 C C   . GLY B 2 33  ? 23.893  61.153  40.892  1.00 94.86  ? 33  GLY B C   1 
ATOM   2777 O O   . GLY B 2 33  ? 25.027  60.690  41.079  1.00 97.05  ? 33  GLY B O   1 
ATOM   2778 N N   . TYR B 2 34  ? 22.953  60.520  40.195  1.00 93.06  ? 34  TYR B N   1 
ATOM   2779 C CA  . TYR B 2 34  ? 23.186  59.301  39.439  1.00 77.88  ? 34  TYR B CA  1 
ATOM   2780 C C   . TYR B 2 34  ? 23.411  59.634  37.970  1.00 75.17  ? 34  TYR B C   1 
ATOM   2781 O O   . TYR B 2 34  ? 22.881  60.619  37.452  1.00 82.38  ? 34  TYR B O   1 
ATOM   2782 C CB  . TYR B 2 34  ? 22.002  58.342  39.558  1.00 73.56  ? 34  TYR B CB  1 
ATOM   2783 C CG  . TYR B 2 34  ? 21.733  57.780  40.941  1.00 76.58  ? 34  TYR B CG  1 
ATOM   2784 C CD1 . TYR B 2 34  ? 22.487  56.728  41.445  1.00 73.44  ? 34  TYR B CD1 1 
ATOM   2785 C CD2 . TYR B 2 34  ? 20.689  58.267  41.721  1.00 75.28  ? 34  TYR B CD2 1 
ATOM   2786 C CE1 . TYR B 2 34  ? 22.229  56.195  42.694  1.00 76.81  ? 34  TYR B CE1 1 
ATOM   2787 C CE2 . TYR B 2 34  ? 20.425  57.739  42.971  1.00 75.86  ? 34  TYR B CE2 1 
ATOM   2788 C CZ  . TYR B 2 34  ? 21.198  56.704  43.452  1.00 84.51  ? 34  TYR B CZ  1 
ATOM   2789 O OH  . TYR B 2 34  ? 20.942  56.175  44.695  1.00 80.03  ? 34  TYR B OH  1 
ATOM   2790 N N   . ALA B 2 35  ? 24.198  58.798  37.298  1.00 73.27  ? 35  ALA B N   1 
ATOM   2791 C CA  . ALA B 2 35  ? 24.422  58.954  35.867  1.00 72.66  ? 35  ALA B CA  1 
ATOM   2792 C C   . ALA B 2 35  ? 24.950  57.642  35.314  1.00 75.10  ? 35  ALA B C   1 
ATOM   2793 O O   . ALA B 2 35  ? 25.943  57.111  35.819  1.00 85.18  ? 35  ALA B O   1 
ATOM   2794 C CB  . ALA B 2 35  ? 25.404  60.091  35.579  1.00 75.21  ? 35  ALA B CB  1 
ATOM   2795 N N   . ALA B 2 36  ? 24.300  57.138  34.269  1.00 68.08  ? 36  ALA B N   1 
ATOM   2796 C CA  . ALA B 2 36  ? 24.658  55.850  33.696  1.00 65.50  ? 36  ALA B CA  1 
ATOM   2797 C C   . ALA B 2 36  ? 25.848  55.984  32.756  1.00 67.85  ? 36  ALA B C   1 
ATOM   2798 O O   . ALA B 2 36  ? 25.890  56.890  31.916  1.00 71.98  ? 36  ALA B O   1 
ATOM   2799 C CB  . ALA B 2 36  ? 23.465  55.257  32.949  1.00 65.23  ? 36  ALA B CB  1 
ATOM   2800 N N   . ASP B 2 37  ? 26.811  55.075  32.892  1.00 74.10  ? 37  ASP B N   1 
ATOM   2801 C CA  . ASP B 2 37  ? 27.922  55.006  31.951  1.00 76.10  ? 37  ASP B CA  1 
ATOM   2802 C C   . ASP B 2 37  ? 27.413  54.495  30.609  1.00 74.00  ? 37  ASP B C   1 
ATOM   2803 O O   . ASP B 2 37  ? 26.906  53.373  30.516  1.00 81.24  ? 37  ASP B O   1 
ATOM   2804 C CB  . ASP B 2 37  ? 29.025  54.101  32.490  1.00 76.11  ? 37  ASP B CB  1 
ATOM   2805 C CG  . ASP B 2 37  ? 30.254  54.089  31.603  1.00 84.13  ? 37  ASP B CG  1 
ATOM   2806 O OD1 . ASP B 2 37  ? 30.472  55.081  30.877  1.00 89.45  ? 37  ASP B OD1 1 
ATOM   2807 O OD2 . ASP B 2 37  ? 31.003  53.091  31.631  1.00 85.77  ? 37  ASP B OD2 1 
ATOM   2808 N N   . GLN B 2 38  ? 27.555  55.317  29.569  1.00 68.47  ? 38  GLN B N   1 
ATOM   2809 C CA  . GLN B 2 38  ? 26.922  55.022  28.289  1.00 71.04  ? 38  GLN B CA  1 
ATOM   2810 C C   . GLN B 2 38  ? 27.726  54.038  27.448  1.00 70.60  ? 38  GLN B C   1 
ATOM   2811 O O   . GLN B 2 38  ? 27.146  53.316  26.628  1.00 76.32  ? 38  GLN B O   1 
ATOM   2812 C CB  . GLN B 2 38  ? 26.702  56.321  27.515  1.00 82.89  ? 38  GLN B CB  1 
ATOM   2813 C CG  . GLN B 2 38  ? 25.893  57.351  28.285  1.00 105.60 ? 38  GLN B CG  1 
ATOM   2814 C CD  . GLN B 2 38  ? 26.261  58.778  27.925  1.00 123.91 ? 38  GLN B CD  1 
ATOM   2815 O OE1 . GLN B 2 38  ? 26.918  59.029  26.914  1.00 127.37 ? 38  GLN B OE1 1 
ATOM   2816 N NE2 . GLN B 2 38  ? 25.845  59.722  28.762  1.00 122.93 ? 38  GLN B NE2 1 
ATOM   2817 N N   . LYS B 2 39  ? 29.046  53.989  27.631  1.00 73.62  ? 39  LYS B N   1 
ATOM   2818 C CA  . LYS B 2 39  ? 29.867  53.087  26.830  1.00 78.20  ? 39  LYS B CA  1 
ATOM   2819 C C   . LYS B 2 39  ? 29.612  51.631  27.204  1.00 71.85  ? 39  LYS B C   1 
ATOM   2820 O O   . LYS B 2 39  ? 29.321  50.798  26.337  1.00 74.61  ? 39  LYS B O   1 
ATOM   2821 C CB  . LYS B 2 39  ? 31.347  53.438  26.993  1.00 78.99  ? 39  LYS B CB  1 
ATOM   2822 C CG  . LYS B 2 39  ? 32.275  52.606  26.121  1.00 87.77  ? 39  LYS B CG  1 
ATOM   2823 C CD  . LYS B 2 39  ? 33.703  53.126  26.166  1.00 96.63  ? 39  LYS B CD  1 
ATOM   2824 C CE  . LYS B 2 39  ? 34.311  52.974  27.550  1.00 108.92 ? 39  LYS B CE  1 
ATOM   2825 N NZ  . LYS B 2 39  ? 35.720  53.457  27.582  1.00 106.80 ? 39  LYS B NZ  1 
ATOM   2826 N N   . SER B 2 40  ? 29.712  51.308  28.495  1.00 67.88  ? 40  SER B N   1 
ATOM   2827 C CA  . SER B 2 40  ? 29.507  49.931  28.936  1.00 63.23  ? 40  SER B CA  1 
ATOM   2828 C C   . SER B 2 40  ? 28.069  49.487  28.693  1.00 56.99  ? 40  SER B C   1 
ATOM   2829 O O   . SER B 2 40  ? 27.821  48.396  28.160  1.00 58.66  ? 40  SER B O   1 
ATOM   2830 C CB  . SER B 2 40  ? 29.874  49.798  30.415  1.00 64.04  ? 40  SER B CB  1 
ATOM   2831 O OG  . SER B 2 40  ? 29.134  50.710  31.207  1.00 69.16  ? 40  SER B OG  1 
ATOM   2832 N N   . THR B 2 41  ? 27.106  50.326  29.083  1.00 56.67  ? 41  THR B N   1 
ATOM   2833 C CA  . THR B 2 41  ? 25.702  50.018  28.835  1.00 57.10  ? 41  THR B CA  1 
ATOM   2834 C C   . THR B 2 41  ? 25.442  49.786  27.352  1.00 53.14  ? 41  THR B C   1 
ATOM   2835 O O   . THR B 2 41  ? 24.758  48.825  26.978  1.00 51.19  ? 41  THR B O   1 
ATOM   2836 C CB  . THR B 2 41  ? 24.818  51.146  29.368  1.00 55.52  ? 41  THR B CB  1 
ATOM   2837 O OG1 . THR B 2 41  ? 24.857  51.146  30.800  1.00 56.10  ? 41  THR B OG1 1 
ATOM   2838 C CG2 . THR B 2 41  ? 23.381  50.975  28.907  1.00 54.39  ? 41  THR B CG2 1 
ATOM   2839 N N   . GLN B 2 42  ? 26.001  50.639  26.490  1.00 54.66  ? 42  GLN B N   1 
ATOM   2840 C CA  . GLN B 2 42  ? 25.784  50.473  25.057  1.00 54.07  ? 42  GLN B CA  1 
ATOM   2841 C C   . GLN B 2 42  ? 26.416  49.186  24.540  1.00 52.42  ? 42  GLN B C   1 
ATOM   2842 O O   . GLN B 2 42  ? 25.846  48.517  23.671  1.00 50.98  ? 42  GLN B O   1 
ATOM   2843 C CB  . GLN B 2 42  ? 26.328  51.679  24.296  1.00 56.45  ? 42  GLN B CB  1 
ATOM   2844 C CG  . GLN B 2 42  ? 25.974  51.656  22.823  1.00 59.35  ? 42  GLN B CG  1 
ATOM   2845 C CD  . GLN B 2 42  ? 24.479  51.572  22.598  1.00 62.33  ? 42  GLN B CD  1 
ATOM   2846 O OE1 . GLN B 2 42  ? 23.698  52.210  23.305  1.00 73.65  ? 42  GLN B OE1 1 
ATOM   2847 N NE2 . GLN B 2 42  ? 24.070  50.776  21.618  1.00 55.96  ? 42  GLN B NE2 1 
ATOM   2848 N N   . ASN B 2 43  ? 27.598  48.829  25.051  1.00 52.75  ? 43  ASN B N   1 
ATOM   2849 C CA  . ASN B 2 43  ? 28.207  47.561  24.660  1.00 51.32  ? 43  ASN B CA  1 
ATOM   2850 C C   . ASN B 2 43  ? 27.320  46.386  25.047  1.00 49.02  ? 43  ASN B C   1 
ATOM   2851 O O   . ASN B 2 43  ? 27.132  45.452  24.257  1.00 47.55  ? 43  ASN B O   1 
ATOM   2852 C CB  . ASN B 2 43  ? 29.590  47.421  25.295  1.00 52.44  ? 43  ASN B CB  1 
ATOM   2853 C CG  . ASN B 2 43  ? 30.643  48.253  24.588  1.00 80.99  ? 43  ASN B CG  1 
ATOM   2854 O OD1 . ASN B 2 43  ? 30.570  48.466  23.377  1.00 78.02  ? 43  ASN B OD1 1 
ATOM   2855 N ND2 . ASN B 2 43  ? 31.632  48.726  25.342  1.00 82.91  ? 43  ASN B ND2 1 
ATOM   2856 N N   . ALA B 2 44  ? 26.758  46.420  26.258  1.00 48.85  ? 44  ALA B N   1 
ATOM   2857 C CA  . ALA B 2 44  ? 25.859  45.353  26.684  1.00 46.91  ? 44  ALA B CA  1 
ATOM   2858 C C   . ALA B 2 44  ? 24.622  45.288  25.796  1.00 45.88  ? 44  ALA B C   1 
ATOM   2859 O O   . ALA B 2 44  ? 24.163  44.197  25.432  1.00 44.15  ? 44  ALA B O   1 
ATOM   2860 C CB  . ALA B 2 44  ? 25.466  45.558  28.146  1.00 47.34  ? 44  ALA B CB  1 
ATOM   2861 N N   . ILE B 2 45  ? 24.072  46.450  25.433  1.00 47.08  ? 45  ILE B N   1 
ATOM   2862 C CA  . ILE B 2 45  ? 22.901  46.484  24.562  1.00 46.40  ? 45  ILE B CA  1 
ATOM   2863 C C   . ILE B 2 45  ? 23.225  45.877  23.203  1.00 45.61  ? 45  ILE B C   1 
ATOM   2864 O O   . ILE B 2 45  ? 22.426  45.119  22.641  1.00 44.51  ? 45  ILE B O   1 
ATOM   2865 C CB  . ILE B 2 45  ? 22.377  47.926  24.426  1.00 51.61  ? 45  ILE B CB  1 
ATOM   2866 C CG1 . ILE B 2 45  ? 21.872  48.443  25.773  1.00 48.99  ? 45  ILE B CG1 1 
ATOM   2867 C CG2 . ILE B 2 45  ? 21.280  47.999  23.381  1.00 47.81  ? 45  ILE B CG2 1 
ATOM   2868 C CD1 . ILE B 2 45  ? 21.459  49.893  25.744  1.00 51.08  ? 45  ILE B CD1 1 
ATOM   2869 N N   . ASN B 2 46  ? 24.398  46.200  22.653  1.00 46.69  ? 46  ASN B N   1 
ATOM   2870 C CA  . ASN B 2 46  ? 24.788  45.643  21.361  1.00 47.73  ? 46  ASN B CA  1 
ATOM   2871 C C   . ASN B 2 46  ? 24.952  44.130  21.443  1.00 44.28  ? 46  ASN B C   1 
ATOM   2872 O O   . ASN B 2 46  ? 24.450  43.391  20.587  1.00 43.09  ? 46  ASN B O   1 
ATOM   2873 C CB  . ASN B 2 46  ? 26.082  46.296  20.875  1.00 48.03  ? 46  ASN B CB  1 
ATOM   2874 C CG  . ASN B 2 46  ? 25.927  47.781  20.620  1.00 55.79  ? 46  ASN B CG  1 
ATOM   2875 O OD1 . ASN B 2 46  ? 24.816  48.283  20.467  1.00 61.18  ? 46  ASN B OD1 1 
ATOM   2876 N ND2 . ASN B 2 46  ? 27.049  48.493  20.570  1.00 57.69  ? 46  ASN B ND2 1 
ATOM   2877 N N   . GLY B 2 47  ? 25.647  43.650  22.476  1.00 44.10  ? 47  GLY B N   1 
ATOM   2878 C CA  . GLY B 2 47  ? 25.890  42.220  22.589  1.00 42.54  ? 47  GLY B CA  1 
ATOM   2879 C C   . GLY B 2 47  ? 24.615  41.423  22.785  1.00 40.79  ? 47  GLY B C   1 
ATOM   2880 O O   . GLY B 2 47  ? 24.413  40.381  22.154  1.00 39.50  ? 47  GLY B O   1 
ATOM   2881 N N   . ILE B 2 48  ? 23.731  41.907  23.658  1.00 40.89  ? 48  ILE B N   1 
ATOM   2882 C CA  . ILE B 2 48  ? 22.488  41.189  23.922  1.00 39.45  ? 48  ILE B CA  1 
ATOM   2883 C C   . ILE B 2 48  ? 21.548  41.280  22.724  1.00 38.99  ? 48  ILE B C   1 
ATOM   2884 O O   . ILE B 2 48  ? 20.843  40.316  22.394  1.00 39.80  ? 48  ILE B O   1 
ATOM   2885 C CB  . ILE B 2 48  ? 21.841  41.723  25.211  1.00 39.98  ? 48  ILE B CB  1 
ATOM   2886 C CG1 . ILE B 2 48  ? 22.738  41.416  26.407  1.00 40.35  ? 48  ILE B CG1 1 
ATOM   2887 C CG2 . ILE B 2 48  ? 20.463  41.126  25.414  1.00 43.20  ? 48  ILE B CG2 1 
ATOM   2888 C CD1 . ILE B 2 48  ? 22.265  42.044  27.686  1.00 54.64  ? 48  ILE B CD1 1 
ATOM   2889 N N   . THR B 2 49  ? 21.528  42.432  22.049  1.00 40.29  ? 49  THR B N   1 
ATOM   2890 C CA  . THR B 2 49  ? 20.750  42.559  20.821  1.00 40.13  ? 49  THR B CA  1 
ATOM   2891 C C   . THR B 2 49  ? 21.209  41.541  19.786  1.00 39.18  ? 49  THR B C   1 
ATOM   2892 O O   . THR B 2 49  ? 20.388  40.877  19.140  1.00 38.12  ? 49  THR B O   1 
ATOM   2893 C CB  . THR B 2 49  ? 20.870  43.981  20.266  1.00 42.03  ? 49  THR B CB  1 
ATOM   2894 O OG1 . THR B 2 49  ? 20.244  44.904  21.165  1.00 42.97  ? 49  THR B OG1 1 
ATOM   2895 C CG2 . THR B 2 49  ? 20.201  44.078  18.899  1.00 42.08  ? 49  THR B CG2 1 
ATOM   2896 N N   . ASN B 2 50  ? 22.526  41.398  19.623  1.00 39.67  ? 50  ASN B N   1 
ATOM   2897 C CA  . ASN B 2 50  ? 23.050  40.418  18.679  1.00 38.97  ? 50  ASN B CA  1 
ATOM   2898 C C   . ASN B 2 50  ? 22.769  38.992  19.134  1.00 37.21  ? 50  ASN B C   1 
ATOM   2899 O O   . ASN B 2 50  ? 22.609  38.098  18.297  1.00 45.32  ? 50  ASN B O   1 
ATOM   2900 C CB  . ASN B 2 50  ? 24.551  40.631  18.483  1.00 44.01  ? 50  ASN B CB  1 
ATOM   2901 C CG  . ASN B 2 50  ? 25.121  39.775  17.373  1.00 60.28  ? 50  ASN B CG  1 
ATOM   2902 O OD1 . ASN B 2 50  ? 25.058  40.139  16.197  1.00 70.03  ? 50  ASN B OD1 1 
ATOM   2903 N ND2 . ASN B 2 50  ? 25.693  38.634  17.740  1.00 66.18  ? 50  ASN B ND2 1 
ATOM   2904 N N   . LYS B 2 51  ? 22.707  38.756  20.445  1.00 36.82  ? 51  LYS B N   1 
ATOM   2905 C CA  . LYS B 2 51  ? 22.395  37.417  20.937  1.00 36.98  ? 51  LYS B CA  1 
ATOM   2906 C C   . LYS B 2 51  ? 20.958  37.030  20.606  1.00 48.39  ? 51  LYS B C   1 
ATOM   2907 O O   . LYS B 2 51  ? 20.711  35.977  20.003  1.00 49.84  ? 51  LYS B O   1 
ATOM   2908 C CB  . LYS B 2 51  ? 22.642  37.336  22.443  1.00 35.69  ? 51  LYS B CB  1 
ATOM   2909 C CG  . LYS B 2 51  ? 21.985  36.133  23.086  1.00 41.08  ? 51  LYS B CG  1 
ATOM   2910 C CD  . LYS B 2 51  ? 22.144  36.132  24.592  1.00 38.46  ? 51  LYS B CD  1 
ATOM   2911 C CE  . LYS B 2 51  ? 23.430  35.455  25.010  1.00 40.66  ? 51  LYS B CE  1 
ATOM   2912 N NZ  . LYS B 2 51  ? 23.369  35.038  26.435  1.00 41.90  ? 51  LYS B NZ  1 
ATOM   2913 N N   . VAL B 2 52  ? 19.994  37.869  21.000  1.00 36.16  ? 52  VAL B N   1 
ATOM   2914 C CA  . VAL B 2 52  ? 18.595  37.593  20.678  1.00 33.93  ? 52  VAL B CA  1 
ATOM   2915 C C   . VAL B 2 52  ? 18.406  37.492  19.170  1.00 33.81  ? 52  VAL B C   1 
ATOM   2916 O O   . VAL B 2 52  ? 17.683  36.616  18.675  1.00 36.00  ? 52  VAL B O   1 
ATOM   2917 C CB  . VAL B 2 52  ? 17.680  38.671  21.289  1.00 40.44  ? 52  VAL B CB  1 
ATOM   2918 C CG1 . VAL B 2 52  ? 16.224  38.395  20.936  1.00 34.18  ? 52  VAL B CG1 1 
ATOM   2919 C CG2 . VAL B 2 52  ? 17.867  38.733  22.794  1.00 35.01  ? 52  VAL B CG2 1 
ATOM   2920 N N   . ASN B 2 53  ? 19.057  38.384  18.417  1.00 35.18  ? 53  ASN B N   1 
ATOM   2921 C CA  . ASN B 2 53  ? 18.976  38.319  16.962  1.00 35.15  ? 53  ASN B CA  1 
ATOM   2922 C C   . ASN B 2 53  ? 19.491  36.986  16.441  1.00 36.28  ? 53  ASN B C   1 
ATOM   2923 O O   . ASN B 2 53  ? 18.890  36.395  15.541  1.00 38.87  ? 53  ASN B O   1 
ATOM   2924 C CB  . ASN B 2 53  ? 19.756  39.473  16.333  1.00 36.84  ? 53  ASN B CB  1 
ATOM   2925 C CG  . ASN B 2 53  ? 18.953  40.753  16.270  1.00 38.02  ? 53  ASN B CG  1 
ATOM   2926 O OD1 . ASN B 2 53  ? 17.731  40.742  16.417  1.00 37.59  ? 53  ASN B OD1 1 
ATOM   2927 N ND2 . ASN B 2 53  ? 19.635  41.865  16.034  1.00 39.69  ? 53  ASN B ND2 1 
ATOM   2928 N N   . SER B 2 54  ? 20.601  36.495  16.994  1.00 41.16  ? 54  SER B N   1 
ATOM   2929 C CA  . SER B 2 54  ? 21.131  35.206  16.561  1.00 38.96  ? 54  SER B CA  1 
ATOM   2930 C C   . SER B 2 54  ? 20.157  34.080  16.876  1.00 41.00  ? 54  SER B C   1 
ATOM   2931 O O   . SER B 2 54  ? 19.971  33.162  16.066  1.00 57.23  ? 54  SER B O   1 
ATOM   2932 C CB  . SER B 2 54  ? 22.483  34.944  17.225  1.00 40.66  ? 54  SER B CB  1 
ATOM   2933 O OG  . SER B 2 54  ? 23.449  35.896  16.814  1.00 47.20  ? 54  SER B OG  1 
ATOM   2934 N N   . VAL B 2 55  ? 19.521  34.138  18.048  1.00 37.82  ? 55  VAL B N   1 
ATOM   2935 C CA  . VAL B 2 55  ? 18.552  33.112  18.422  1.00 35.40  ? 55  VAL B CA  1 
ATOM   2936 C C   . VAL B 2 55  ? 17.391  33.091  17.436  1.00 39.78  ? 55  VAL B C   1 
ATOM   2937 O O   . VAL B 2 55  ? 16.962  32.026  16.977  1.00 47.66  ? 55  VAL B O   1 
ATOM   2938 C CB  . VAL B 2 55  ? 18.065  33.336  19.865  1.00 37.91  ? 55  VAL B CB  1 
ATOM   2939 C CG1 . VAL B 2 55  ? 16.949  32.358  20.213  1.00 39.78  ? 55  VAL B CG1 1 
ATOM   2940 C CG2 . VAL B 2 55  ? 19.224  33.200  20.839  1.00 30.61  ? 55  VAL B CG2 1 
ATOM   2941 N N   . ILE B 2 56  ? 16.873  34.270  17.086  1.00 36.31  ? 56  ILE B N   1 
ATOM   2942 C CA  . ILE B 2 56  ? 15.757  34.329  16.146  1.00 33.42  ? 56  ILE B CA  1 
ATOM   2943 C C   . ILE B 2 56  ? 16.199  33.898  14.750  1.00 40.43  ? 56  ILE B C   1 
ATOM   2944 O O   . ILE B 2 56  ? 15.454  33.225  14.027  1.00 39.25  ? 56  ILE B O   1 
ATOM   2945 C CB  . ILE B 2 56  ? 15.144  35.742  16.144  1.00 35.76  ? 56  ILE B CB  1 
ATOM   2946 C CG1 . ILE B 2 56  ? 14.587  36.073  17.530  1.00 31.85  ? 56  ILE B CG1 1 
ATOM   2947 C CG2 . ILE B 2 56  ? 14.062  35.861  15.082  1.00 32.07  ? 56  ILE B CG2 1 
ATOM   2948 C CD1 . ILE B 2 56  ? 13.995  37.452  17.638  1.00 34.19  ? 56  ILE B CD1 1 
ATOM   2949 N N   . GLU B 2 57  ? 17.422  34.262  14.356  1.00 43.82  ? 57  GLU B N   1 
ATOM   2950 C CA  . GLU B 2 57  ? 17.904  33.943  13.016  1.00 46.82  ? 57  GLU B CA  1 
ATOM   2951 C C   . GLU B 2 57  ? 18.116  32.447  12.841  1.00 44.85  ? 57  GLU B C   1 
ATOM   2952 O O   . GLU B 2 57  ? 17.876  31.904  11.757  1.00 48.02  ? 57  GLU B O   1 
ATOM   2953 C CB  . GLU B 2 57  ? 19.199  34.699  12.728  1.00 61.06  ? 57  GLU B CB  1 
ATOM   2954 C CG  . GLU B 2 57  ? 19.015  36.179  12.458  1.00 82.21  ? 57  GLU B CG  1 
ATOM   2955 C CD  . GLU B 2 57  ? 20.324  36.942  12.514  1.00 81.58  ? 57  GLU B CD  1 
ATOM   2956 O OE1 . GLU B 2 57  ? 21.388  36.293  12.590  1.00 84.53  ? 57  GLU B OE1 1 
ATOM   2957 O OE2 . GLU B 2 57  ? 20.288  38.190  12.488  1.00 78.75  ? 57  GLU B OE2 1 
ATOM   2958 N N   . LYS B 2 58  ? 18.574  31.762  13.890  1.00 51.54  ? 58  LYS B N   1 
ATOM   2959 C CA  . LYS B 2 58  ? 18.741  30.318  13.784  1.00 42.21  ? 58  LYS B CA  1 
ATOM   2960 C C   . LYS B 2 58  ? 17.415  29.570  13.778  1.00 47.36  ? 58  LYS B C   1 
ATOM   2961 O O   . LYS B 2 58  ? 17.411  28.361  13.526  1.00 48.14  ? 58  LYS B O   1 
ATOM   2962 C CB  . LYS B 2 58  ? 19.621  29.800  14.920  1.00 39.57  ? 58  LYS B CB  1 
ATOM   2963 C CG  . LYS B 2 58  ? 21.024  30.378  14.917  1.00 40.83  ? 58  LYS B CG  1 
ATOM   2964 C CD  . LYS B 2 58  ? 21.676  30.238  13.554  1.00 36.13  ? 58  LYS B CD  1 
ATOM   2965 C CE  . LYS B 2 58  ? 23.031  30.920  13.527  1.00 42.61  ? 58  LYS B CE  1 
ATOM   2966 N NZ  . LYS B 2 58  ? 23.668  30.849  12.184  1.00 49.17  ? 58  LYS B NZ  1 
ATOM   2967 N N   . MET B 2 59  ? 16.301  30.245  14.052  1.00 61.85  ? 59  MET B N   1 
ATOM   2968 C CA  . MET B 2 59  ? 14.973  29.639  13.974  1.00 52.97  ? 59  MET B CA  1 
ATOM   2969 C C   . MET B 2 59  ? 14.356  30.079  12.649  1.00 59.90  ? 59  MET B C   1 
ATOM   2970 O O   . MET B 2 59  ? 13.711  31.124  12.557  1.00 76.28  ? 59  MET B O   1 
ATOM   2971 C CB  . MET B 2 59  ? 14.112  30.039  15.167  1.00 56.02  ? 59  MET B CB  1 
ATOM   2972 C CG  . MET B 2 59  ? 14.621  29.538  16.507  1.00 53.41  ? 59  MET B CG  1 
ATOM   2973 S SD  . MET B 2 59  ? 14.890  27.756  16.534  1.00 58.56  ? 59  MET B SD  1 
ATOM   2974 C CE  . MET B 2 59  ? 13.289  27.147  16.012  1.00 70.01  ? 59  MET B CE  1 
ATOM   2975 N N   . ASN B 2 60  ? 14.570  29.272  11.614  1.00 59.46  ? 60  ASN B N   1 
ATOM   2976 C CA  . ASN B 2 60  ? 14.074  29.603  10.288  1.00 62.97  ? 60  ASN B CA  1 
ATOM   2977 C C   . ASN B 2 60  ? 12.553  29.486  10.236  1.00 76.19  ? 60  ASN B C   1 
ATOM   2978 O O   . ASN B 2 60  ? 11.929  28.759  11.015  1.00 80.76  ? 60  ASN B O   1 
ATOM   2979 C CB  . ASN B 2 60  ? 14.707  28.693  9.236   1.00 72.36  ? 60  ASN B CB  1 
ATOM   2980 C CG  . ASN B 2 60  ? 16.214  28.839  9.170   1.00 77.44  ? 60  ASN B CG  1 
ATOM   2981 O OD1 . ASN B 2 60  ? 16.949  27.859  9.287   1.00 89.45  ? 60  ASN B OD1 1 
ATOM   2982 N ND2 . ASN B 2 60  ? 16.682  30.068  8.984   1.00 81.85  ? 60  ASN B ND2 1 
ATOM   2983 N N   . THR B 2 61  ? 11.962  30.216  9.292   1.00 76.34  ? 61  THR B N   1 
ATOM   2984 C CA  . THR B 2 61  ? 10.510  30.289  9.188   1.00 69.71  ? 61  THR B CA  1 
ATOM   2985 C C   . THR B 2 61  ? 9.908   28.914  8.928   1.00 63.13  ? 61  THR B C   1 
ATOM   2986 O O   . THR B 2 61  ? 10.317  28.206  8.003   1.00 74.31  ? 61  THR B O   1 
ATOM   2987 C CB  . THR B 2 61  ? 10.110  31.253  8.069   1.00 71.07  ? 61  THR B CB  1 
ATOM   2988 O OG1 . THR B 2 61  ? 10.529  32.581  8.404   1.00 83.52  ? 61  THR B OG1 1 
ATOM   2989 C CG2 . THR B 2 61  ? 8.604   31.237  7.865   1.00 69.46  ? 61  THR B CG2 1 
ATOM   2990 N N   . GLN B 2 62  ? 8.935   28.539  9.754   1.00 52.05  ? 62  GLN B N   1 
ATOM   2991 C CA  . GLN B 2 62  ? 8.182   27.308  9.545   1.00 45.79  ? 62  GLN B CA  1 
ATOM   2992 C C   . GLN B 2 62  ? 7.118   27.543  8.482   1.00 48.35  ? 62  GLN B C   1 
ATOM   2993 O O   . GLN B 2 62  ? 6.203   28.350  8.680   1.00 55.97  ? 62  GLN B O   1 
ATOM   2994 C CB  . GLN B 2 62  ? 7.539   26.846  10.850  1.00 49.92  ? 62  GLN B CB  1 
ATOM   2995 C CG  . GLN B 2 62  ? 6.549   25.706  10.678  1.00 58.58  ? 62  GLN B CG  1 
ATOM   2996 C CD  . GLN B 2 62  ? 7.224   24.385  10.374  1.00 68.81  ? 62  GLN B CD  1 
ATOM   2997 O OE1 . GLN B 2 62  ? 8.261   24.057  10.949  1.00 76.74  ? 62  GLN B OE1 1 
ATOM   2998 N NE2 . GLN B 2 62  ? 6.637   23.617  9.463   1.00 74.64  ? 62  GLN B NE2 1 
ATOM   2999 N N   . PHE B 2 63  ? 7.230   26.839  7.360   1.00 45.18  ? 63  PHE B N   1 
ATOM   3000 C CA  . PHE B 2 63  ? 6.281   26.989  6.269   1.00 45.03  ? 63  PHE B CA  1 
ATOM   3001 C C   . PHE B 2 63  ? 5.164   25.953  6.410   1.00 46.91  ? 63  PHE B C   1 
ATOM   3002 O O   . PHE B 2 63  ? 5.036   25.282  7.437   1.00 53.60  ? 63  PHE B O   1 
ATOM   3003 C CB  . PHE B 2 63  ? 7.009   26.907  4.929   1.00 46.25  ? 63  PHE B CB  1 
ATOM   3004 C CG  . PHE B 2 63  ? 7.885   28.098  4.648   1.00 54.25  ? 63  PHE B CG  1 
ATOM   3005 C CD1 . PHE B 2 63  ? 7.337   29.281  4.180   1.00 52.63  ? 63  PHE B CD1 1 
ATOM   3006 C CD2 . PHE B 2 63  ? 9.252   28.040  4.865   1.00 44.45  ? 63  PHE B CD2 1 
ATOM   3007 C CE1 . PHE B 2 63  ? 8.136   30.382  3.927   1.00 51.71  ? 63  PHE B CE1 1 
ATOM   3008 C CE2 . PHE B 2 63  ? 10.056  29.138  4.614   1.00 44.77  ? 63  PHE B CE2 1 
ATOM   3009 C CZ  . PHE B 2 63  ? 9.495   30.310  4.144   1.00 46.92  ? 63  PHE B CZ  1 
ATOM   3010 N N   . THR B 2 64  ? 4.343   25.818  5.371   1.00 42.72  ? 64  THR B N   1 
ATOM   3011 C CA  . THR B 2 64  ? 3.109   25.048  5.474   1.00 38.87  ? 64  THR B CA  1 
ATOM   3012 C C   . THR B 2 64  ? 3.386   23.583  5.782   1.00 36.45  ? 64  THR B C   1 
ATOM   3013 O O   . THR B 2 64  ? 4.172   22.923  5.095   1.00 42.87  ? 64  THR B O   1 
ATOM   3014 C CB  . THR B 2 64  ? 2.308   25.169  4.180   1.00 45.28  ? 64  THR B CB  1 
ATOM   3015 O OG1 . THR B 2 64  ? 1.941   26.537  3.973   1.00 49.56  ? 64  THR B OG1 1 
ATOM   3016 C CG2 . THR B 2 64  ? 1.051   24.315  4.250   1.00 46.78  ? 64  THR B CG2 1 
ATOM   3017 N N   . ALA B 2 65  ? 2.727   23.077  6.822   1.00 44.71  ? 65  ALA B N   1 
ATOM   3018 C CA  . ALA B 2 65  ? 2.842   21.674  7.211   1.00 46.32  ? 65  ALA B CA  1 
ATOM   3019 C C   . ALA B 2 65  ? 1.542   21.276  7.891   1.00 42.38  ? 65  ALA B C   1 
ATOM   3020 O O   . ALA B 2 65  ? 1.307   21.649  9.043   1.00 47.04  ? 65  ALA B O   1 
ATOM   3021 C CB  . ALA B 2 65  ? 4.037   21.450  8.134   1.00 47.40  ? 65  ALA B CB  1 
ATOM   3022 N N   . VAL B 2 66  ? 0.703   20.527  7.185   1.00 37.41  ? 66  VAL B N   1 
ATOM   3023 C CA  . VAL B 2 66  ? -0.599  20.132  7.691   1.00 40.38  ? 66  VAL B CA  1 
ATOM   3024 C C   . VAL B 2 66  ? -0.603  18.626  7.935   1.00 39.49  ? 66  VAL B C   1 
ATOM   3025 O O   . VAL B 2 66  ? 0.312   17.904  7.542   1.00 42.76  ? 66  VAL B O   1 
ATOM   3026 C CB  . VAL B 2 66  ? -1.740  20.547  6.741   1.00 41.90  ? 66  VAL B CB  1 
ATOM   3027 C CG1 . VAL B 2 66  ? -1.670  22.035  6.460   1.00 42.75  ? 66  VAL B CG1 1 
ATOM   3028 C CG2 . VAL B 2 66  ? -1.674  19.753  5.448   1.00 47.35  ? 66  VAL B CG2 1 
ATOM   3029 N N   . GLY B 2 67  ? -1.652  18.158  8.601   1.00 38.66  ? 67  GLY B N   1 
ATOM   3030 C CA  . GLY B 2 67  ? -1.813  16.747  8.862   1.00 39.66  ? 67  GLY B CA  1 
ATOM   3031 C C   . GLY B 2 67  ? -2.133  15.972  7.601   1.00 43.64  ? 67  GLY B C   1 
ATOM   3032 O O   . GLY B 2 67  ? -2.288  16.516  6.508   1.00 42.24  ? 67  GLY B O   1 
ATOM   3033 N N   . LYS B 2 68  ? -2.228  14.656  7.766   1.00 47.26  ? 68  LYS B N   1 
ATOM   3034 C CA  . LYS B 2 68  ? -2.526  13.755  6.665   1.00 45.04  ? 68  LYS B CA  1 
ATOM   3035 C C   . LYS B 2 68  ? -3.607  12.772  7.086   1.00 41.28  ? 68  LYS B C   1 
ATOM   3036 O O   . LYS B 2 68  ? -3.762  12.464  8.270   1.00 45.91  ? 68  LYS B O   1 
ATOM   3037 C CB  . LYS B 2 68  ? -1.279  12.991  6.206   1.00 48.64  ? 68  LYS B CB  1 
ATOM   3038 C CG  . LYS B 2 68  ? -0.139  13.885  5.758   1.00 43.15  ? 68  LYS B CG  1 
ATOM   3039 C CD  . LYS B 2 68  ? 1.032   13.073  5.240   1.00 44.35  ? 68  LYS B CD  1 
ATOM   3040 C CE  . LYS B 2 68  ? 2.147   13.981  4.756   1.00 45.65  ? 68  LYS B CE  1 
ATOM   3041 N NZ  . LYS B 2 68  ? 3.260   13.197  4.161   1.00 75.42  ? 68  LYS B NZ  1 
ATOM   3042 N N   . GLU B 2 69  ? -4.350  12.282  6.099   1.00 33.00  ? 69  GLU B N   1 
ATOM   3043 C CA  . GLU B 2 69  ? -5.404  11.306  6.319   1.00 34.03  ? 69  GLU B CA  1 
ATOM   3044 C C   . GLU B 2 69  ? -4.921  9.914   5.936   1.00 34.19  ? 69  GLU B C   1 
ATOM   3045 O O   . GLU B 2 69  ? -4.072  9.749   5.056   1.00 33.93  ? 69  GLU B O   1 
ATOM   3046 C CB  . GLU B 2 69  ? -6.657  11.662  5.517   1.00 45.48  ? 69  GLU B CB  1 
ATOM   3047 C CG  . GLU B 2 69  ? -7.311  12.964  5.936   1.00 59.82  ? 69  GLU B CG  1 
ATOM   3048 C CD  . GLU B 2 69  ? -7.915  12.894  7.325   1.00 73.10  ? 69  GLU B CD  1 
ATOM   3049 O OE1 . GLU B 2 69  ? -8.352  11.798  7.734   1.00 87.78  ? 69  GLU B OE1 1 
ATOM   3050 O OE2 . GLU B 2 69  ? -7.950  13.938  8.010   1.00 75.63  ? 69  GLU B OE2 1 
ATOM   3051 N N   . PHE B 2 70  ? -5.474  8.912   6.617   1.00 39.21  ? 70  PHE B N   1 
ATOM   3052 C CA  . PHE B 2 70  ? -5.125  7.516   6.402   1.00 35.18  ? 70  PHE B CA  1 
ATOM   3053 C C   . PHE B 2 70  ? -6.375  6.669   6.564   1.00 36.64  ? 70  PHE B C   1 
ATOM   3054 O O   . PHE B 2 70  ? -7.163  6.888   7.488   1.00 43.86  ? 70  PHE B O   1 
ATOM   3055 C CB  . PHE B 2 70  ? -4.047  7.048   7.388   1.00 34.26  ? 70  PHE B CB  1 
ATOM   3056 C CG  . PHE B 2 70  ? -2.830  7.925   7.417   1.00 34.63  ? 70  PHE B CG  1 
ATOM   3057 C CD1 . PHE B 2 70  ? -1.767  7.684   6.567   1.00 36.04  ? 70  PHE B CD1 1 
ATOM   3058 C CD2 . PHE B 2 70  ? -2.750  8.998   8.293   1.00 32.13  ? 70  PHE B CD2 1 
ATOM   3059 C CE1 . PHE B 2 70  ? -0.649  8.493   6.593   1.00 33.32  ? 70  PHE B CE1 1 
ATOM   3060 C CE2 . PHE B 2 70  ? -1.634  9.808   8.320   1.00 31.57  ? 70  PHE B CE2 1 
ATOM   3061 C CZ  . PHE B 2 70  ? -0.583  9.555   7.468   1.00 32.05  ? 70  PHE B CZ  1 
ATOM   3062 N N   . ASN B 2 71  ? -6.556  5.702   5.669   1.00 45.26  ? 71  ASN B N   1 
ATOM   3063 C CA  . ASN B 2 71  ? -7.734  4.855   5.745   1.00 50.30  ? 71  ASN B CA  1 
ATOM   3064 C C   . ASN B 2 71  ? -7.541  3.773   6.807   1.00 52.09  ? 71  ASN B C   1 
ATOM   3065 O O   . ASN B 2 71  ? -6.514  3.702   7.489   1.00 49.87  ? 71  ASN B O   1 
ATOM   3066 C CB  . ASN B 2 71  ? -8.053  4.253   4.379   1.00 50.28  ? 71  ASN B CB  1 
ATOM   3067 C CG  . ASN B 2 71  ? -6.908  3.450   3.813   1.00 48.44  ? 71  ASN B CG  1 
ATOM   3068 O OD1 . ASN B 2 71  ? -6.682  2.308   4.208   1.00 46.71  ? 71  ASN B OD1 1 
ATOM   3069 N ND2 . ASN B 2 71  ? -6.185  4.038   2.870   1.00 71.86  ? 71  ASN B ND2 1 
ATOM   3070 N N   . LYS B 2 72  ? -8.550  2.908   6.942   1.00 64.16  ? 72  LYS B N   1 
ATOM   3071 C CA  . LYS B 2 72  ? -8.589  1.951   8.041   1.00 61.29  ? 72  LYS B CA  1 
ATOM   3072 C C   . LYS B 2 72  ? -7.489  0.900   7.959   1.00 51.73  ? 72  LYS B C   1 
ATOM   3073 O O   . LYS B 2 72  ? -7.198  0.251   8.968   1.00 51.12  ? 72  LYS B O   1 
ATOM   3074 C CB  . LYS B 2 72  ? -9.956  1.271   8.084   1.00 70.48  ? 72  LYS B CB  1 
ATOM   3075 C CG  . LYS B 2 72  ? -11.116 2.243   8.161   1.00 79.00  ? 72  LYS B CG  1 
ATOM   3076 C CD  . LYS B 2 72  ? -12.448 1.522   8.087   1.00 98.06  ? 72  LYS B CD  1 
ATOM   3077 C CE  . LYS B 2 72  ? -13.603 2.508   8.104   1.00 97.71  ? 72  LYS B CE  1 
ATOM   3078 N NZ  . LYS B 2 72  ? -14.922 1.823   8.016   1.00 98.29  ? 72  LYS B NZ  1 
ATOM   3079 N N   . LEU B 2 73  ? -6.873  0.713   6.792   1.00 41.18  ? 73  LEU B N   1 
ATOM   3080 C CA  . LEU B 2 73  ? -5.806  -0.264  6.625   1.00 41.16  ? 73  LEU B CA  1 
ATOM   3081 C C   . LEU B 2 73  ? -4.424  0.380   6.572   1.00 39.50  ? 73  LEU B C   1 
ATOM   3082 O O   . LEU B 2 73  ? -3.482  -0.235  6.061   1.00 55.08  ? 73  LEU B O   1 
ATOM   3083 C CB  . LEU B 2 73  ? -6.046  -1.103  5.368   1.00 42.48  ? 73  LEU B CB  1 
ATOM   3084 C CG  . LEU B 2 73  ? -7.138  -2.173  5.448   1.00 44.92  ? 73  LEU B CG  1 
ATOM   3085 C CD1 . LEU B 2 73  ? -7.273  -2.912  4.123   1.00 47.18  ? 73  LEU B CD1 1 
ATOM   3086 C CD2 . LEU B 2 73  ? -6.848  -3.149  6.577   1.00 44.96  ? 73  LEU B CD2 1 
ATOM   3087 N N   . GLU B 2 74  ? -4.281  1.597   7.091   1.00 38.21  ? 74  GLU B N   1 
ATOM   3088 C CA  . GLU B 2 74  ? -3.008  2.311   7.104   1.00 36.72  ? 74  GLU B CA  1 
ATOM   3089 C C   . GLU B 2 74  ? -2.688  2.823   8.500   1.00 35.80  ? 74  GLU B C   1 
ATOM   3090 O O   . GLU B 2 74  ? -2.273  3.971   8.684   1.00 37.40  ? 74  GLU B O   1 
ATOM   3091 C CB  . GLU B 2 74  ? -3.015  3.454   6.093   1.00 36.14  ? 74  GLU B CB  1 
ATOM   3092 C CG  . GLU B 2 74  ? -3.025  2.988   4.651   1.00 37.45  ? 74  GLU B CG  1 
ATOM   3093 C CD  . GLU B 2 74  ? -3.185  4.131   3.672   1.00 39.27  ? 74  GLU B CD  1 
ATOM   3094 O OE1 . GLU B 2 74  ? -3.812  5.144   4.045   1.00 39.73  ? 74  GLU B OE1 1 
ATOM   3095 O OE2 . GLU B 2 74  ? -2.687  4.016   2.531   1.00 41.30  ? 74  GLU B OE2 1 
ATOM   3096 N N   . ARG B 2 75  ? -2.865  1.966   9.509   1.00 36.47  ? 75  ARG B N   1 
ATOM   3097 C CA  . ARG B 2 75  ? -2.635  2.385   10.887  1.00 35.87  ? 75  ARG B CA  1 
ATOM   3098 C C   . ARG B 2 75  ? -1.145  2.491   11.191  1.00 34.81  ? 75  ARG B C   1 
ATOM   3099 O O   . ARG B 2 75  ? -0.723  3.357   11.966  1.00 33.84  ? 75  ARG B O   1 
ATOM   3100 C CB  . ARG B 2 75  ? -3.312  1.409   11.848  1.00 37.20  ? 75  ARG B CB  1 
ATOM   3101 C CG  . ARG B 2 75  ? -3.356  1.896   13.281  1.00 42.01  ? 75  ARG B CG  1 
ATOM   3102 C CD  . ARG B 2 75  ? -4.279  3.095   13.415  1.00 62.24  ? 75  ARG B CD  1 
ATOM   3103 N NE  . ARG B 2 75  ? -4.435  3.526   14.801  1.00 78.13  ? 75  ARG B NE  1 
ATOM   3104 C CZ  . ARG B 2 75  ? -5.330  3.020   15.645  1.00 88.22  ? 75  ARG B CZ  1 
ATOM   3105 N NH1 . ARG B 2 75  ? -5.404  3.475   16.888  1.00 94.06  ? 75  ARG B NH1 1 
ATOM   3106 N NH2 . ARG B 2 75  ? -6.149  2.055   15.246  1.00 67.74  ? 75  ARG B NH2 1 
ATOM   3107 N N   . ARG B 2 76  ? -0.333  1.610   10.600  1.00 39.03  ? 76  ARG B N   1 
ATOM   3108 C CA  . ARG B 2 76  ? 1.112   1.697   10.789  1.00 34.30  ? 76  ARG B CA  1 
ATOM   3109 C C   . ARG B 2 76  ? 1.672   2.990   10.207  1.00 33.00  ? 76  ARG B C   1 
ATOM   3110 O O   . ARG B 2 76  ? 2.517   3.646   10.829  1.00 36.21  ? 76  ARG B O   1 
ATOM   3111 C CB  . ARG B 2 76  ? 1.802   0.490   10.156  1.00 35.16  ? 76  ARG B CB  1 
ATOM   3112 C CG  . ARG B 2 76  ? 1.558   -0.823  10.884  1.00 47.16  ? 76  ARG B CG  1 
ATOM   3113 C CD  . ARG B 2 76  ? 2.064   -1.999  10.074  1.00 37.63  ? 76  ARG B CD  1 
ATOM   3114 N NE  . ARG B 2 76  ? 1.423   -2.048  8.767   1.00 38.08  ? 76  ARG B NE  1 
ATOM   3115 C CZ  . ARG B 2 76  ? 1.982   -2.563  7.679   1.00 38.62  ? 76  ARG B CZ  1 
ATOM   3116 N NH1 . ARG B 2 76  ? 3.204   -3.072  7.737   1.00 38.79  ? 76  ARG B NH1 1 
ATOM   3117 N NH2 . ARG B 2 76  ? 1.320   -2.557  6.533   1.00 39.14  ? 76  ARG B NH2 1 
ATOM   3118 N N   . MET B 2 77  ? 1.214   3.373   9.014   1.00 33.07  ? 77  MET B N   1 
ATOM   3119 C CA  . MET B 2 77  ? 1.709   4.597   8.396   1.00 32.08  ? 77  MET B CA  1 
ATOM   3120 C C   . MET B 2 77  ? 1.191   5.828   9.128   1.00 31.32  ? 77  MET B C   1 
ATOM   3121 O O   . MET B 2 77  ? 1.906   6.830   9.257   1.00 35.98  ? 77  MET B O   1 
ATOM   3122 C CB  . MET B 2 77  ? 1.312   4.641   6.921   1.00 39.93  ? 77  MET B CB  1 
ATOM   3123 C CG  . MET B 2 77  ? 2.107   5.641   6.103   1.00 49.06  ? 77  MET B CG  1 
ATOM   3124 S SD  . MET B 2 77  ? 1.394   5.944   4.476   1.00 63.06  ? 77  MET B SD  1 
ATOM   3125 C CE  . MET B 2 77  ? 1.378   4.288   3.796   1.00 86.03  ? 77  MET B CE  1 
ATOM   3126 N N   . GLU B 2 78  ? -0.053  5.776   9.604   1.00 31.89  ? 78  GLU B N   1 
ATOM   3127 C CA  . GLU B 2 78  ? -0.575  6.861   10.424  1.00 31.41  ? 78  GLU B CA  1 
ATOM   3128 C C   . GLU B 2 78  ? 0.251   7.032   11.691  1.00 35.73  ? 78  GLU B C   1 
ATOM   3129 O O   . GLU B 2 78  ? 0.596   8.158   12.074  1.00 32.14  ? 78  GLU B O   1 
ATOM   3130 C CB  . GLU B 2 78  ? -2.036  6.594   10.773  1.00 32.46  ? 78  GLU B CB  1 
ATOM   3131 C CG  . GLU B 2 78  ? -2.680  7.715   11.554  1.00 36.42  ? 78  GLU B CG  1 
ATOM   3132 C CD  . GLU B 2 78  ? -4.103  7.405   11.951  1.00 46.06  ? 78  GLU B CD  1 
ATOM   3133 O OE1 . GLU B 2 78  ? -4.580  7.999   12.939  1.00 61.53  ? 78  GLU B OE1 1 
ATOM   3134 O OE2 . GLU B 2 78  ? -4.743  6.570   11.280  1.00 55.66  ? 78  GLU B OE2 1 
ATOM   3135 N N   . ASN B 2 79  ? 0.586   5.922   12.350  1.00 31.23  ? 79  ASN B N   1 
ATOM   3136 C CA  . ASN B 2 79  ? 1.376   5.997   13.570  1.00 30.80  ? 79  ASN B CA  1 
ATOM   3137 C C   . ASN B 2 79  ? 2.813   6.413   13.290  1.00 29.86  ? 79  ASN B C   1 
ATOM   3138 O O   . ASN B 2 79  ? 3.457   7.012   14.156  1.00 36.06  ? 79  ASN B O   1 
ATOM   3139 C CB  . ASN B 2 79  ? 1.333   4.658   14.301  1.00 31.85  ? 79  ASN B CB  1 
ATOM   3140 C CG  . ASN B 2 79  ? -0.001  4.406   14.966  1.00 32.86  ? 79  ASN B CG  1 
ATOM   3141 O OD1 . ASN B 2 79  ? -0.709  5.343   15.336  1.00 35.02  ? 79  ASN B OD1 1 
ATOM   3142 N ND2 . ASN B 2 79  ? -0.354  3.136   15.125  1.00 34.12  ? 79  ASN B ND2 1 
ATOM   3143 N N   . LEU B 2 80  ? 3.333   6.108   12.098  1.00 29.88  ? 80  LEU B N   1 
ATOM   3144 C CA  . LEU B 2 80  ? 4.662   6.583   11.730  1.00 29.16  ? 80  LEU B CA  1 
ATOM   3145 C C   . LEU B 2 80  ? 4.660   8.090   11.500  1.00 28.28  ? 80  LEU B C   1 
ATOM   3146 O O   . LEU B 2 80  ? 5.564   8.795   11.961  1.00 29.40  ? 80  LEU B O   1 
ATOM   3147 C CB  . LEU B 2 80  ? 5.158   5.846   10.485  1.00 29.66  ? 80  LEU B CB  1 
ATOM   3148 C CG  . LEU B 2 80  ? 6.511   6.272   9.912   1.00 29.21  ? 80  LEU B CG  1 
ATOM   3149 C CD1 . LEU B 2 80  ? 7.615   6.082   10.937  1.00 29.01  ? 80  LEU B CD1 1 
ATOM   3150 C CD2 . LEU B 2 80  ? 6.824   5.500   8.640   1.00 29.99  ? 80  LEU B CD2 1 
ATOM   3151 N N   . ASN B 2 81  ? 3.654   8.594   10.782  1.00 28.43  ? 81  ASN B N   1 
ATOM   3152 C CA  . ASN B 2 81  ? 3.497   10.036  10.607  1.00 37.99  ? 81  ASN B CA  1 
ATOM   3153 C C   . ASN B 2 81  ? 3.390   10.738  11.958  1.00 27.40  ? 81  ASN B C   1 
ATOM   3154 O O   . ASN B 2 81  ? 4.057   11.752  12.207  1.00 27.72  ? 81  ASN B O   1 
ATOM   3155 C CB  . ASN B 2 81  ? 2.261   10.301  9.743   1.00 28.39  ? 81  ASN B CB  1 
ATOM   3156 C CG  . ASN B 2 81  ? 2.165   11.734  9.271   1.00 28.04  ? 81  ASN B CG  1 
ATOM   3157 O OD1 . ASN B 2 81  ? 2.972   12.188  8.462   1.00 28.52  ? 81  ASN B OD1 1 
ATOM   3158 N ND2 . ASN B 2 81  ? 1.156   12.448  9.754   1.00 36.82  ? 81  ASN B ND2 1 
ATOM   3159 N N   . LYS B 2 82  ? 2.627   10.211  12.879  1.00 40.43  ? 82  LYS B N   1 
ATOM   3160 C CA  . LYS B 2 82  ? 2.525   10.792  14.191  1.00 31.21  ? 82  LYS B CA  1 
ATOM   3161 C C   . LYS B 2 82  ? 3.836   10.773  14.970  1.00 31.42  ? 82  LYS B C   1 
ATOM   3162 O O   . LYS B 2 82  ? 4.150   11.672  15.681  1.00 28.04  ? 82  LYS B O   1 
ATOM   3163 C CB  . LYS B 2 82  ? 1.501   10.017  14.963  1.00 30.00  ? 82  LYS B CB  1 
ATOM   3164 C CG  . LYS B 2 82  ? 0.955   10.766  16.134  1.00 30.00  ? 82  LYS B CG  1 
ATOM   3165 C CD  . LYS B 2 82  ? -0.026  9.934   16.897  1.00 30.00  ? 82  LYS B CD  1 
ATOM   3166 C CE  . LYS B 2 82  ? -0.367  10.603  18.209  1.00 30.00  ? 82  LYS B CE  1 
ATOM   3167 N NZ  . LYS B 2 82  ? -0.566  9.621   19.302  1.00 30.00  ? 82  LYS B NZ  1 
ATOM   3168 N N   . LYS B 2 83  ? 4.583   9.705   14.837  1.00 27.45  ? 83  LYS B N   1 
ATOM   3169 C CA  . LYS B 2 83  ? 5.858   9.543   15.464  1.00 27.17  ? 83  LYS B CA  1 
ATOM   3170 C C   . LYS B 2 83  ? 6.820   10.558  14.940  1.00 26.39  ? 83  LYS B C   1 
ATOM   3171 O O   . LYS B 2 83  ? 7.613   11.053  15.649  1.00 27.45  ? 83  LYS B O   1 
ATOM   3172 C CB  . LYS B 2 83  ? 6.371   8.142   15.173  1.00 27.80  ? 83  LYS B CB  1 
ATOM   3173 C CG  . LYS B 2 83  ? 7.705   7.787   15.751  1.00 27.75  ? 83  LYS B CG  1 
ATOM   3174 C CD  . LYS B 2 83  ? 7.810   6.315   15.903  1.00 28.70  ? 83  LYS B CD  1 
ATOM   3175 C CE  . LYS B 2 83  ? 8.822   5.666   14.992  1.00 30.30  ? 83  LYS B CE  1 
ATOM   3176 N NZ  . LYS B 2 83  ? 8.444   4.308   14.564  1.00 30.09  ? 83  LYS B NZ  1 
ATOM   3177 N N   . VAL B 2 84  ? 6.784   10.823  13.661  1.00 26.26  ? 84  VAL B N   1 
ATOM   3178 C CA  . VAL B 2 84  ? 7.668   11.840  13.094  1.00 25.73  ? 84  VAL B CA  1 
ATOM   3179 C C   . VAL B 2 84  ? 7.302   13.220  13.630  1.00 25.29  ? 84  VAL B C   1 
ATOM   3180 O O   . VAL B 2 84  ? 8.153   13.955  14.150  1.00 24.92  ? 84  VAL B O   1 
ATOM   3181 C CB  . VAL B 2 84  ? 7.610   11.804  11.557  1.00 25.95  ? 84  VAL B CB  1 
ATOM   3182 C CG1 . VAL B 2 84  ? 8.359   12.986  10.970  1.00 25.59  ? 84  VAL B CG1 1 
ATOM   3183 C CG2 . VAL B 2 84  ? 8.178   10.498  11.036  1.00 26.49  ? 84  VAL B CG2 1 
ATOM   3184 N N   . ASP B 2 85  ? 6.021   13.588  13.510  1.00 25.47  ? 85  ASP B N   1 
ATOM   3185 C CA  . ASP B 2 85  ? 5.586   14.908  13.961  1.00 25.26  ? 85  ASP B CA  1 
ATOM   3186 C C   . ASP B 2 85  ? 5.892   15.115  15.442  1.00 25.13  ? 85  ASP B C   1 
ATOM   3187 O O   . ASP B 2 85  ? 6.508   16.119  15.830  1.00 24.80  ? 85  ASP B O   1 
ATOM   3188 C CB  . ASP B 2 85  ? 4.093   15.090  13.683  1.00 25.75  ? 85  ASP B CB  1 
ATOM   3189 C CG  . ASP B 2 85  ? 3.784   15.204  12.202  1.00 28.57  ? 85  ASP B CG  1 
ATOM   3190 O OD1 . ASP B 2 85  ? 4.705   15.514  11.418  1.00 30.68  ? 85  ASP B OD1 1 
ATOM   3191 O OD2 . ASP B 2 85  ? 2.616   14.989  11.818  1.00 35.13  ? 85  ASP B OD2 1 
ATOM   3192 N N   . ASP B 2 86  ? 5.480   14.161  16.283  1.00 25.53  ? 86  ASP B N   1 
ATOM   3193 C CA  . ASP B 2 86  ? 5.712   14.280  17.718  1.00 25.64  ? 86  ASP B CA  1 
ATOM   3194 C C   . ASP B 2 86  ? 7.198   14.336  18.039  1.00 33.63  ? 86  ASP B C   1 
ATOM   3195 O O   . ASP B 2 86  ? 7.619   15.091  18.921  1.00 25.17  ? 86  ASP B O   1 
ATOM   3196 C CB  . ASP B 2 86  ? 5.048   13.117  18.456  1.00 26.37  ? 86  ASP B CB  1 
ATOM   3197 C CG  . ASP B 2 86  ? 3.550   13.290  18.586  1.00 40.56  ? 86  ASP B CG  1 
ATOM   3198 O OD1 . ASP B 2 86  ? 3.047   14.390  18.272  1.00 29.28  ? 86  ASP B OD1 1 
ATOM   3199 O OD2 . ASP B 2 86  ? 2.875   12.331  19.017  1.00 36.10  ? 86  ASP B OD2 1 
ATOM   3200 N N   . GLY B 2 87  ? 8.009   13.543  17.334  1.00 25.23  ? 87  GLY B N   1 
ATOM   3201 C CA  . GLY B 2 87  ? 9.439   13.550  17.596  1.00 25.08  ? 87  GLY B CA  1 
ATOM   3202 C C   . GLY B 2 87  ? 10.075  14.897  17.311  1.00 24.61  ? 87  GLY B C   1 
ATOM   3203 O O   . GLY B 2 87  ? 10.817  15.437  18.140  1.00 24.56  ? 87  GLY B O   1 
ATOM   3204 N N   . PHE B 2 88  ? 9.785   15.464  16.135  1.00 24.40  ? 88  PHE B N   1 
ATOM   3205 C CA  . PHE B 2 88  ? 10.344  16.771  15.799  1.00 24.14  ? 88  PHE B CA  1 
ATOM   3206 C C   . PHE B 2 88  ? 9.868   17.843  16.776  1.00 24.08  ? 88  PHE B C   1 
ATOM   3207 O O   . PHE B 2 88  ? 10.651  18.711  17.189  1.00 32.02  ? 88  PHE B O   1 
ATOM   3208 C CB  . PHE B 2 88  ? 9.985   17.145  14.360  1.00 24.16  ? 88  PHE B CB  1 
ATOM   3209 C CG  . PHE B 2 88  ? 10.774  16.398  13.323  1.00 24.35  ? 88  PHE B CG  1 
ATOM   3210 C CD1 . PHE B 2 88  ? 12.072  15.988  13.582  1.00 24.44  ? 88  PHE B CD1 1 
ATOM   3211 C CD2 . PHE B 2 88  ? 10.221  16.105  12.088  1.00 31.71  ? 88  PHE B CD2 1 
ATOM   3212 C CE1 . PHE B 2 88  ? 12.802  15.299  12.628  1.00 28.89  ? 88  PHE B CE1 1 
ATOM   3213 C CE2 . PHE B 2 88  ? 10.947  15.415  11.130  1.00 27.92  ? 88  PHE B CE2 1 
ATOM   3214 C CZ  . PHE B 2 88  ? 12.236  15.011  11.402  1.00 25.61  ? 88  PHE B CZ  1 
ATOM   3215 N N   . ILE B 2 89  ? 8.593   17.788  17.173  1.00 24.27  ? 89  ILE B N   1 
ATOM   3216 C CA  . ILE B 2 89  ? 8.077   18.753  18.144  1.00 24.42  ? 89  ILE B CA  1 
ATOM   3217 C C   . ILE B 2 89  ? 8.827   18.633  19.470  1.00 24.53  ? 89  ILE B C   1 
ATOM   3218 O O   . ILE B 2 89  ? 9.201   19.639  20.086  1.00 37.17  ? 89  ILE B O   1 
ATOM   3219 C CB  . ILE B 2 89  ? 6.561   18.566  18.334  1.00 24.84  ? 89  ILE B CB  1 
ATOM   3220 C CG1 . ILE B 2 89  ? 5.805   19.037  17.089  1.00 24.90  ? 89  ILE B CG1 1 
ATOM   3221 C CG2 . ILE B 2 89  ? 6.082   19.319  19.557  1.00 25.77  ? 89  ILE B CG2 1 
ATOM   3222 C CD1 . ILE B 2 89  ? 4.318   18.788  17.154  1.00 25.46  ? 89  ILE B CD1 1 
ATOM   3223 N N   . ASP B 2 90  ? 9.054   17.399  19.929  1.00 24.72  ? 90  ASP B N   1 
ATOM   3224 C CA  . ASP B 2 90  ? 9.777   17.196  21.183  1.00 25.02  ? 90  ASP B CA  1 
ATOM   3225 C C   . ASP B 2 90  ? 11.188  17.759  21.105  1.00 24.80  ? 90  ASP B C   1 
ATOM   3226 O O   . ASP B 2 90  ? 11.659  18.418  22.042  1.00 38.32  ? 90  ASP B O   1 
ATOM   3227 C CB  . ASP B 2 90  ? 9.829   15.709  21.535  1.00 25.44  ? 90  ASP B CB  1 
ATOM   3228 C CG  . ASP B 2 90  ? 8.477   15.150  21.909  1.00 36.90  ? 90  ASP B CG  1 
ATOM   3229 O OD1 . ASP B 2 90  ? 7.582   15.944  22.262  1.00 36.89  ? 90  ASP B OD1 1 
ATOM   3230 O OD2 . ASP B 2 90  ? 8.310   13.915  21.856  1.00 50.64  ? 90  ASP B OD2 1 
ATOM   3231 N N   . ILE B 2 91  ? 11.883  17.500  19.998  1.00 26.83  ? 91  ILE B N   1 
ATOM   3232 C CA  . ILE B 2 91  ? 13.252  17.982  19.868  1.00 24.52  ? 91  ILE B CA  1 
ATOM   3233 C C   . ILE B 2 91  ? 13.292  19.506  19.854  1.00 24.40  ? 91  ILE B C   1 
ATOM   3234 O O   . ILE B 2 91  ? 14.130  20.120  20.525  1.00 24.62  ? 91  ILE B O   1 
ATOM   3235 C CB  . ILE B 2 91  ? 13.906  17.369  18.619  1.00 24.46  ? 91  ILE B CB  1 
ATOM   3236 C CG1 . ILE B 2 91  ? 14.132  15.870  18.830  1.00 28.56  ? 91  ILE B CG1 1 
ATOM   3237 C CG2 . ILE B 2 91  ? 15.212  18.073  18.296  1.00 24.58  ? 91  ILE B CG2 1 
ATOM   3238 C CD1 . ILE B 2 91  ? 14.620  15.142  17.601  1.00 38.92  ? 91  ILE B CD1 1 
ATOM   3239 N N   . TRP B 2 92  ? 12.377  20.145  19.120  1.00 27.43  ? 92  TRP B N   1 
ATOM   3240 C CA  . TRP B 2 92  ? 12.398  21.604  19.055  1.00 32.66  ? 92  TRP B CA  1 
ATOM   3241 C C   . TRP B 2 92  ? 12.014  22.231  20.392  1.00 24.58  ? 92  TRP B C   1 
ATOM   3242 O O   . TRP B 2 92  ? 12.558  23.276  20.774  1.00 24.82  ? 92  TRP B O   1 
ATOM   3243 C CB  . TRP B 2 92  ? 11.482  22.091  17.933  1.00 24.22  ? 92  TRP B CB  1 
ATOM   3244 C CG  . TRP B 2 92  ? 12.113  21.944  16.585  1.00 24.52  ? 92  TRP B CG  1 
ATOM   3245 C CD1 . TRP B 2 92  ? 11.695  21.143  15.565  1.00 27.99  ? 92  TRP B CD1 1 
ATOM   3246 C CD2 . TRP B 2 92  ? 13.298  22.600  16.122  1.00 38.28  ? 92  TRP B CD2 1 
ATOM   3247 N NE1 . TRP B 2 92  ? 12.538  21.270  14.491  1.00 30.86  ? 92  TRP B NE1 1 
ATOM   3248 C CE2 . TRP B 2 92  ? 13.532  22.157  14.807  1.00 30.78  ? 92  TRP B CE2 1 
ATOM   3249 C CE3 . TRP B 2 92  ? 14.181  23.524  16.690  1.00 24.65  ? 92  TRP B CE3 1 
ATOM   3250 C CZ2 . TRP B 2 92  ? 14.612  22.604  14.049  1.00 33.29  ? 92  TRP B CZ2 1 
ATOM   3251 C CZ3 . TRP B 2 92  ? 15.251  23.966  15.939  1.00 31.67  ? 92  TRP B CZ3 1 
ATOM   3252 C CH2 . TRP B 2 92  ? 15.458  23.507  14.631  1.00 29.95  ? 92  TRP B CH2 1 
ATOM   3253 N N   . THR B 2 93  ? 11.086  21.604  21.118  1.00 24.72  ? 93  THR B N   1 
ATOM   3254 C CA  . THR B 2 93  ? 10.745  22.067  22.460  1.00 25.20  ? 93  THR B CA  1 
ATOM   3255 C C   . THR B 2 93  ? 11.959  22.008  23.381  1.00 25.46  ? 93  THR B C   1 
ATOM   3256 O O   . THR B 2 93  ? 12.306  22.995  24.045  1.00 25.82  ? 93  THR B O   1 
ATOM   3257 C CB  . THR B 2 93  ? 9.599   21.221  23.019  1.00 25.50  ? 93  THR B CB  1 
ATOM   3258 O OG1 . THR B 2 93  ? 8.463   21.324  22.153  1.00 31.26  ? 93  THR B OG1 1 
ATOM   3259 C CG2 . THR B 2 93  ? 9.214   21.680  24.413  1.00 26.21  ? 93  THR B CG2 1 
ATOM   3260 N N   . TYR B 2 94  ? 12.624  20.851  23.417  1.00 25.41  ? 94  TYR B N   1 
ATOM   3261 C CA  . TYR B 2 94  ? 13.835  20.691  24.215  1.00 25.80  ? 94  TYR B CA  1 
ATOM   3262 C C   . TYR B 2 94  ? 14.875  21.753  23.866  1.00 25.79  ? 94  TYR B C   1 
ATOM   3263 O O   . TYR B 2 94  ? 15.441  22.403  24.755  1.00 31.25  ? 94  TYR B O   1 
ATOM   3264 C CB  . TYR B 2 94  ? 14.390  19.280  24.004  1.00 25.84  ? 94  TYR B CB  1 
ATOM   3265 C CG  . TYR B 2 94  ? 15.754  19.036  24.602  1.00 26.36  ? 94  TYR B CG  1 
ATOM   3266 C CD1 . TYR B 2 94  ? 15.893  18.635  25.924  1.00 27.10  ? 94  TYR B CD1 1 
ATOM   3267 C CD2 . TYR B 2 94  ? 16.904  19.192  23.840  1.00 27.53  ? 94  TYR B CD2 1 
ATOM   3268 C CE1 . TYR B 2 94  ? 17.139  18.408  26.473  1.00 27.74  ? 94  TYR B CE1 1 
ATOM   3269 C CE2 . TYR B 2 94  ? 18.154  18.970  24.380  1.00 26.92  ? 94  TYR B CE2 1 
ATOM   3270 C CZ  . TYR B 2 94  ? 18.265  18.577  25.695  1.00 28.34  ? 94  TYR B CZ  1 
ATOM   3271 O OH  . TYR B 2 94  ? 19.509  18.356  26.234  1.00 30.34  ? 94  TYR B OH  1 
ATOM   3272 N N   . ASN B 2 95  ? 15.126  21.948  22.567  1.00 25.37  ? 95  ASN B N   1 
ATOM   3273 C CA  . ASN B 2 95  ? 16.109  22.933  22.120  1.00 25.53  ? 95  ASN B CA  1 
ATOM   3274 C C   . ASN B 2 95  ? 15.769  24.327  22.625  1.00 25.82  ? 95  ASN B C   1 
ATOM   3275 O O   . ASN B 2 95  ? 16.628  25.031  23.172  1.00 51.98  ? 95  ASN B O   1 
ATOM   3276 C CB  . ASN B 2 95  ? 16.187  22.940  20.593  1.00 25.20  ? 95  ASN B CB  1 
ATOM   3277 C CG  . ASN B 2 95  ? 16.889  21.724  20.036  1.00 28.78  ? 95  ASN B CG  1 
ATOM   3278 O OD1 . ASN B 2 95  ? 17.323  20.842  20.778  1.00 30.19  ? 95  ASN B OD1 1 
ATOM   3279 N ND2 . ASN B 2 95  ? 17.001  21.667  18.715  1.00 32.64  ? 95  ASN B ND2 1 
ATOM   3280 N N   . ALA B 2 96  ? 14.517  24.750  22.433  1.00 31.75  ? 96  ALA B N   1 
ATOM   3281 C CA  . ALA B 2 96  ? 14.120  26.097  22.830  1.00 26.11  ? 96  ALA B CA  1 
ATOM   3282 C C   . ALA B 2 96  ? 14.273  26.297  24.334  1.00 29.84  ? 96  ALA B C   1 
ATOM   3283 O O   . ALA B 2 96  ? 14.924  27.251  24.784  1.00 33.55  ? 96  ALA B O   1 
ATOM   3284 C CB  . ALA B 2 96  ? 12.682  26.366  22.391  1.00 26.02  ? 96  ALA B CB  1 
ATOM   3285 N N   . GLU B 2 97  ? 13.690  25.396  25.129  1.00 26.75  ? 97  GLU B N   1 
ATOM   3286 C CA  . GLU B 2 97  ? 13.713  25.580  26.577  1.00 27.51  ? 97  GLU B CA  1 
ATOM   3287 C C   . GLU B 2 97  ? 15.135  25.544  27.126  1.00 27.89  ? 97  GLU B C   1 
ATOM   3288 O O   . GLU B 2 97  ? 15.523  26.406  27.928  1.00 47.68  ? 97  GLU B O   1 
ATOM   3289 C CB  . GLU B 2 97  ? 12.841  24.521  27.249  1.00 27.66  ? 97  GLU B CB  1 
ATOM   3290 C CG  . GLU B 2 97  ? 11.370  24.646  26.886  1.00 33.58  ? 97  GLU B CG  1 
ATOM   3291 C CD  . GLU B 2 97  ? 10.472  23.762  27.722  1.00 43.93  ? 97  GLU B CD  1 
ATOM   3292 O OE1 . GLU B 2 97  ? 10.993  22.873  28.424  1.00 54.63  ? 97  GLU B OE1 1 
ATOM   3293 O OE2 . GLU B 2 97  ? 9.242   23.962  27.679  1.00 47.36  ? 97  GLU B OE2 1 
ATOM   3294 N N   . LEU B 2 98  ? 15.934  24.571  26.685  1.00 27.56  ? 98  LEU B N   1 
ATOM   3295 C CA  . LEU B 2 98  ? 17.302  24.457  27.178  1.00 28.08  ? 98  LEU B CA  1 
ATOM   3296 C C   . LEU B 2 98  ? 18.132  25.674  26.782  1.00 28.83  ? 98  LEU B C   1 
ATOM   3297 O O   . LEU B 2 98  ? 18.873  26.232  27.606  1.00 42.02  ? 98  LEU B O   1 
ATOM   3298 C CB  . LEU B 2 98  ? 17.932  23.172  26.646  1.00 30.37  ? 98  LEU B CB  1 
ATOM   3299 C CG  . LEU B 2 98  ? 19.291  22.817  27.235  1.00 46.42  ? 98  LEU B CG  1 
ATOM   3300 C CD1 . LEU B 2 98  ? 19.153  22.473  28.710  1.00 35.82  ? 98  LEU B CD1 1 
ATOM   3301 C CD2 . LEU B 2 98  ? 19.911  21.669  26.462  1.00 47.47  ? 98  LEU B CD2 1 
ATOM   3302 N N   . LEU B 2 99  ? 18.019  26.096  25.520  1.00 27.81  ? 99  LEU B N   1 
ATOM   3303 C CA  . LEU B 2 99  ? 18.728  27.285  25.059  1.00 28.19  ? 99  LEU B CA  1 
ATOM   3304 C C   . LEU B 2 99  ? 18.385  28.498  25.915  1.00 39.44  ? 99  LEU B C   1 
ATOM   3305 O O   . LEU B 2 99  ? 19.275  29.244  26.341  1.00 39.68  ? 99  LEU B O   1 
ATOM   3306 C CB  . LEU B 2 99  ? 18.393  27.550  23.591  1.00 27.68  ? 99  LEU B CB  1 
ATOM   3307 C CG  . LEU B 2 99  ? 19.025  28.788  22.954  1.00 35.86  ? 99  LEU B CG  1 
ATOM   3308 C CD1 . LEU B 2 99  ? 20.539  28.668  22.947  1.00 34.26  ? 99  LEU B CD1 1 
ATOM   3309 C CD2 . LEU B 2 99  ? 18.495  29.004  21.546  1.00 27.85  ? 99  LEU B CD2 1 
ATOM   3310 N N   . VAL B 2 100 ? 17.092  28.701  26.191  1.00 28.73  ? 100 VAL B N   1 
ATOM   3311 C CA  . VAL B 2 100 ? 16.686  29.866  26.974  1.00 29.53  ? 100 VAL B CA  1 
ATOM   3312 C C   . VAL B 2 100 ? 17.248  29.789  28.390  1.00 32.27  ? 100 VAL B C   1 
ATOM   3313 O O   . VAL B 2 100 ? 17.745  30.786  28.926  1.00 40.88  ? 100 VAL B O   1 
ATOM   3314 C CB  . VAL B 2 100 ? 15.154  30.012  26.968  1.00 29.40  ? 100 VAL B CB  1 
ATOM   3315 C CG1 . VAL B 2 100 ? 14.708  30.993  28.037  1.00 30.43  ? 100 VAL B CG1 1 
ATOM   3316 C CG2 . VAL B 2 100 ? 14.685  30.489  25.605  1.00 28.98  ? 100 VAL B CG2 1 
ATOM   3317 N N   . LEU B 2 101 ? 17.192  28.610  29.015  1.00 30.22  ? 101 LEU B N   1 
ATOM   3318 C CA  . LEU B 2 101 ? 17.796  28.444  30.338  1.00 31.97  ? 101 LEU B CA  1 
ATOM   3319 C C   . LEU B 2 101 ? 19.264  28.862  30.336  1.00 34.68  ? 101 LEU B C   1 
ATOM   3320 O O   . LEU B 2 101 ? 19.671  29.811  31.032  1.00 46.27  ? 101 LEU B O   1 
ATOM   3321 C CB  . LEU B 2 101 ? 17.672  26.988  30.789  1.00 31.01  ? 101 LEU B CB  1 
ATOM   3322 C CG  . LEU B 2 101 ? 16.527  26.556  31.698  1.00 31.99  ? 101 LEU B CG  1 
ATOM   3323 C CD1 . LEU B 2 101 ? 16.784  25.148  32.205  1.00 34.52  ? 101 LEU B CD1 1 
ATOM   3324 C CD2 . LEU B 2 101 ? 16.383  27.511  32.852  1.00 41.36  ? 101 LEU B CD2 1 
ATOM   3325 N N   . LEU B 2 102 ? 20.074  28.161  29.538  1.00 31.20  ? 102 LEU B N   1 
ATOM   3326 C CA  . LEU B 2 102 ? 21.519  28.344  29.595  1.00 31.89  ? 102 LEU B CA  1 
ATOM   3327 C C   . LEU B 2 102 ? 21.915  29.771  29.232  1.00 33.38  ? 102 LEU B C   1 
ATOM   3328 O O   . LEU B 2 102 ? 22.731  30.396  29.923  1.00 54.14  ? 102 LEU B O   1 
ATOM   3329 C CB  . LEU B 2 102 ? 22.201  27.330  28.677  1.00 31.36  ? 102 LEU B CB  1 
ATOM   3330 C CG  . LEU B 2 102 ? 21.829  25.872  28.969  1.00 33.46  ? 102 LEU B CG  1 
ATOM   3331 C CD1 . LEU B 2 102 ? 22.510  24.924  27.996  1.00 30.64  ? 102 LEU B CD1 1 
ATOM   3332 C CD2 . LEU B 2 102 ? 22.160  25.502  30.407  1.00 32.03  ? 102 LEU B CD2 1 
ATOM   3333 N N   . GLU B 2 103 ? 21.330  30.317  28.164  1.00 31.77  ? 103 GLU B N   1 
ATOM   3334 C CA  . GLU B 2 103 ? 21.712  31.663  27.755  1.00 38.92  ? 103 GLU B CA  1 
ATOM   3335 C C   . GLU B 2 103 ? 21.152  32.738  28.679  1.00 33.22  ? 103 GLU B C   1 
ATOM   3336 O O   . GLU B 2 103 ? 21.696  33.848  28.711  1.00 41.56  ? 103 GLU B O   1 
ATOM   3337 C CB  . GLU B 2 103 ? 21.293  31.913  26.309  1.00 32.21  ? 103 GLU B CB  1 
ATOM   3338 C CG  . GLU B 2 103 ? 22.130  31.123  25.317  1.00 34.05  ? 103 GLU B CG  1 
ATOM   3339 C CD  . GLU B 2 103 ? 23.624  31.245  25.586  1.00 40.12  ? 103 GLU B CD  1 
ATOM   3340 O OE1 . GLU B 2 103 ? 24.125  32.385  25.694  1.00 48.36  ? 103 GLU B OE1 1 
ATOM   3341 O OE2 . GLU B 2 103 ? 24.298  30.199  25.698  1.00 40.43  ? 103 GLU B OE2 1 
ATOM   3342 N N   . ASN B 2 104 ? 20.089  32.443  29.431  1.00 33.06  ? 104 ASN B N   1 
ATOM   3343 C CA  . ASN B 2 104 ? 19.690  33.340  30.513  1.00 34.12  ? 104 ASN B CA  1 
ATOM   3344 C C   . ASN B 2 104 ? 20.782  33.418  31.570  1.00 35.23  ? 104 ASN B C   1 
ATOM   3345 O O   . ASN B 2 104 ? 21.206  34.515  31.974  1.00 40.77  ? 104 ASN B O   1 
ATOM   3346 C CB  . ASN B 2 104 ? 18.374  32.876  31.137  1.00 33.90  ? 104 ASN B CB  1 
ATOM   3347 C CG  . ASN B 2 104 ? 17.166  33.299  30.332  1.00 33.39  ? 104 ASN B CG  1 
ATOM   3348 O OD1 . ASN B 2 104 ? 17.267  34.126  29.426  1.00 33.39  ? 104 ASN B OD1 1 
ATOM   3349 N ND2 . ASN B 2 104 ? 16.009  32.738  30.663  1.00 33.12  ? 104 ASN B ND2 1 
ATOM   3350 N N   . GLU B 2 105 ? 21.262  32.254  32.022  1.00 35.08  ? 105 GLU B N   1 
ATOM   3351 C CA  . GLU B 2 105 ? 22.361  32.247  32.983  1.00 36.26  ? 105 GLU B CA  1 
ATOM   3352 C C   . GLU B 2 105 ? 23.562  33.021  32.450  1.00 36.86  ? 105 GLU B C   1 
ATOM   3353 O O   . GLU B 2 105 ? 24.134  33.867  33.151  1.00 45.34  ? 105 GLU B O   1 
ATOM   3354 C CB  . GLU B 2 105 ? 22.755  30.812  33.324  1.00 36.04  ? 105 GLU B CB  1 
ATOM   3355 C CG  . GLU B 2 105 ? 23.839  30.708  34.377  1.00 37.42  ? 105 GLU B CG  1 
ATOM   3356 C CD  . GLU B 2 105 ? 23.299  30.870  35.785  1.00 57.26  ? 105 GLU B CD  1 
ATOM   3357 O OE1 . GLU B 2 105 ? 22.206  30.337  36.069  1.00 47.50  ? 105 GLU B OE1 1 
ATOM   3358 O OE2 . GLU B 2 105 ? 23.963  31.535  36.608  1.00 49.03  ? 105 GLU B OE2 1 
ATOM   3359 N N   . ARG B 2 106 ? 23.948  32.759  31.197  1.00 36.06  ? 106 ARG B N   1 
ATOM   3360 C CA  . ARG B 2 106 ? 25.114  33.435  30.638  1.00 36.79  ? 106 ARG B CA  1 
ATOM   3361 C C   . ARG B 2 106 ? 24.880  34.928  30.450  1.00 37.48  ? 106 ARG B C   1 
ATOM   3362 O O   . ARG B 2 106 ? 25.842  35.702  30.441  1.00 40.85  ? 106 ARG B O   1 
ATOM   3363 C CB  . ARG B 2 106 ? 25.516  32.792  29.313  1.00 35.95  ? 106 ARG B CB  1 
ATOM   3364 C CG  . ARG B 2 106 ? 26.390  31.563  29.476  1.00 35.99  ? 106 ARG B CG  1 
ATOM   3365 C CD  . ARG B 2 106 ? 27.014  31.139  28.163  1.00 53.56  ? 106 ARG B CD  1 
ATOM   3366 N NE  . ARG B 2 106 ? 27.936  32.136  27.629  1.00 41.94  ? 106 ARG B NE  1 
ATOM   3367 C CZ  . ARG B 2 106 ? 29.187  32.297  28.045  1.00 39.30  ? 106 ARG B CZ  1 
ATOM   3368 N NH1 . ARG B 2 106 ? 29.668  31.535  29.015  1.00 38.45  ? 106 ARG B NH1 1 
ATOM   3369 N NH2 . ARG B 2 106 ? 29.954  33.223  27.493  1.00 43.55  ? 106 ARG B NH2 1 
ATOM   3370 N N   . THR B 2 107 ? 23.626  35.354  30.293  1.00 37.92  ? 107 THR B N   1 
ATOM   3371 C CA  . THR B 2 107 ? 23.351  36.782  30.187  1.00 37.85  ? 107 THR B CA  1 
ATOM   3372 C C   . THR B 2 107 ? 23.547  37.474  31.531  1.00 39.29  ? 107 THR B C   1 
ATOM   3373 O O   . THR B 2 107 ? 24.199  38.527  31.613  1.00 40.57  ? 107 THR B O   1 
ATOM   3374 C CB  . THR B 2 107 ? 21.936  37.011  29.661  1.00 37.08  ? 107 THR B CB  1 
ATOM   3375 O OG1 . THR B 2 107 ? 21.828  36.482  28.335  1.00 35.95  ? 107 THR B OG1 1 
ATOM   3376 C CG2 . THR B 2 107 ? 21.618  38.497  29.626  1.00 38.21  ? 107 THR B CG2 1 
ATOM   3377 N N   . LEU B 2 108 ? 22.999  36.891  32.603  1.00 42.52  ? 108 LEU B N   1 
ATOM   3378 C CA  . LEU B 2 108 ? 23.232  37.467  33.926  1.00 40.79  ? 108 LEU B CA  1 
ATOM   3379 C C   . LEU B 2 108 ? 24.719  37.476  34.269  1.00 41.83  ? 108 LEU B C   1 
ATOM   3380 O O   . LEU B 2 108 ? 25.238  38.466  34.807  1.00 43.34  ? 108 LEU B O   1 
ATOM   3381 C CB  . LEU B 2 108 ? 22.430  36.706  34.979  1.00 40.70  ? 108 LEU B CB  1 
ATOM   3382 C CG  . LEU B 2 108 ? 20.912  36.810  34.819  1.00 40.09  ? 108 LEU B CG  1 
ATOM   3383 C CD1 . LEU B 2 108 ? 20.202  36.065  35.933  1.00 40.31  ? 108 LEU B CD1 1 
ATOM   3384 C CD2 . LEU B 2 108 ? 20.474  38.263  34.786  1.00 41.09  ? 108 LEU B CD2 1 
ATOM   3385 N N   . ASP B 2 109 ? 25.427  36.391  33.943  1.00 41.17  ? 109 ASP B N   1 
ATOM   3386 C CA  . ASP B 2 109 ? 26.875  36.376  34.133  1.00 42.24  ? 109 ASP B CA  1 
ATOM   3387 C C   . ASP B 2 109 ? 27.548  37.477  33.321  1.00 45.99  ? 109 ASP B C   1 
ATOM   3388 O O   . ASP B 2 109 ? 28.526  38.084  33.774  1.00 44.48  ? 109 ASP B O   1 
ATOM   3389 C CB  . ASP B 2 109 ? 27.444  35.011  33.752  1.00 43.36  ? 109 ASP B CB  1 
ATOM   3390 C CG  . ASP B 2 109 ? 26.998  33.912  34.689  1.00 48.46  ? 109 ASP B CG  1 
ATOM   3391 O OD1 . ASP B 2 109 ? 26.601  34.224  35.831  1.00 61.66  ? 109 ASP B OD1 1 
ATOM   3392 O OD2 . ASP B 2 109 ? 27.050  32.733  34.286  1.00 46.49  ? 109 ASP B OD2 1 
ATOM   3393 N N   . PHE B 2 110 ? 27.036  37.747  32.120  1.00 42.00  ? 110 PHE B N   1 
ATOM   3394 C CA  . PHE B 2 110 ? 27.604  38.801  31.287  1.00 42.81  ? 110 PHE B CA  1 
ATOM   3395 C C   . PHE B 2 110 ? 27.469  40.164  31.958  1.00 44.33  ? 110 PHE B C   1 
ATOM   3396 O O   . PHE B 2 110 ? 28.420  40.955  31.980  1.00 49.31  ? 110 PHE B O   1 
ATOM   3397 C CB  . PHE B 2 110 ? 26.929  38.789  29.915  1.00 41.59  ? 110 PHE B CB  1 
ATOM   3398 C CG  . PHE B 2 110 ? 27.377  39.893  29.004  1.00 42.53  ? 110 PHE B CG  1 
ATOM   3399 C CD1 . PHE B 2 110 ? 28.687  39.959  28.563  1.00 43.45  ? 110 PHE B CD1 1 
ATOM   3400 C CD2 . PHE B 2 110 ? 26.477  40.853  28.569  1.00 42.66  ? 110 PHE B CD2 1 
ATOM   3401 C CE1 . PHE B 2 110 ? 29.096  40.971  27.717  1.00 44.51  ? 110 PHE B CE1 1 
ATOM   3402 C CE2 . PHE B 2 110 ? 26.879  41.865  27.722  1.00 43.72  ? 110 PHE B CE2 1 
ATOM   3403 C CZ  . PHE B 2 110 ? 28.191  41.925  27.296  1.00 44.65  ? 110 PHE B CZ  1 
ATOM   3404 N N   . HIS B 2 111 ? 26.291  40.453  32.520  1.00 44.14  ? 111 HIS B N   1 
ATOM   3405 C CA  . HIS B 2 111 ? 26.116  41.715  33.237  1.00 45.75  ? 111 HIS B CA  1 
ATOM   3406 C C   . HIS B 2 111 ? 27.058  41.800  34.432  1.00 47.27  ? 111 HIS B C   1 
ATOM   3407 O O   . HIS B 2 111 ? 27.694  42.838  34.668  1.00 52.42  ? 111 HIS B O   1 
ATOM   3408 C CB  . HIS B 2 111 ? 24.668  41.871  33.695  1.00 45.39  ? 111 HIS B CB  1 
ATOM   3409 C CG  . HIS B 2 111 ? 23.695  42.070  32.577  1.00 44.36  ? 111 HIS B CG  1 
ATOM   3410 N ND1 . HIS B 2 111 ? 23.699  43.191  31.775  1.00 45.11  ? 111 HIS B ND1 1 
ATOM   3411 C CD2 . HIS B 2 111 ? 22.675  41.296  32.137  1.00 42.80  ? 111 HIS B CD2 1 
ATOM   3412 C CE1 . HIS B 2 111 ? 22.728  43.096  30.886  1.00 44.06  ? 111 HIS B CE1 1 
ATOM   3413 N NE2 . HIS B 2 111 ? 22.091  41.957  31.084  1.00 42.63  ? 111 HIS B NE2 1 
ATOM   3414 N N   . ASP B 2 112 ? 27.149  40.713  35.206  1.00 46.84  ? 112 ASP B N   1 
ATOM   3415 C CA  . ASP B 2 112 ? 28.065  40.680  36.343  1.00 48.37  ? 112 ASP B CA  1 
ATOM   3416 C C   . ASP B 2 112 ? 29.491  41.005  35.908  1.00 49.40  ? 112 ASP B C   1 
ATOM   3417 O O   . ASP B 2 112 ? 30.197  41.781  36.569  1.00 52.75  ? 112 ASP B O   1 
ATOM   3418 C CB  . ASP B 2 112 ? 27.998  39.305  37.010  1.00 47.68  ? 112 ASP B CB  1 
ATOM   3419 C CG  . ASP B 2 112 ? 28.522  39.315  38.429  1.00 49.39  ? 112 ASP B CG  1 
ATOM   3420 O OD1 . ASP B 2 112 ? 28.485  40.381  39.076  1.00 50.91  ? 112 ASP B OD1 1 
ATOM   3421 O OD2 . ASP B 2 112 ? 28.963  38.247  38.903  1.00 49.34  ? 112 ASP B OD2 1 
ATOM   3422 N N   . SER B 2 113 ? 29.921  40.440  34.779  1.00 48.37  ? 113 SER B N   1 
ATOM   3423 C CA  . SER B 2 113 ? 31.257  40.725  34.268  1.00 49.45  ? 113 SER B CA  1 
ATOM   3424 C C   . SER B 2 113 ? 31.401  42.188  33.875  1.00 50.76  ? 113 SER B C   1 
ATOM   3425 O O   . SER B 2 113 ? 32.453  42.797  34.101  1.00 52.54  ? 113 SER B O   1 
ATOM   3426 C CB  . SER B 2 113 ? 31.568  39.826  33.074  1.00 48.14  ? 113 SER B CB  1 
ATOM   3427 O OG  . SER B 2 113 ? 32.699  40.308  32.373  1.00 49.29  ? 113 SER B OG  1 
ATOM   3428 N N   . ASN B 2 114 ? 30.358  42.770  33.277  1.00 50.05  ? 114 ASN B N   1 
ATOM   3429 C CA  . ASN B 2 114 ? 30.442  44.175  32.887  1.00 51.45  ? 114 ASN B CA  1 
ATOM   3430 C C   . ASN B 2 114 ? 30.600  45.079  34.105  1.00 53.38  ? 114 ASN B C   1 
ATOM   3431 O O   . ASN B 2 114 ? 31.397  46.027  34.086  1.00 55.23  ? 114 ASN B O   1 
ATOM   3432 C CB  . ASN B 2 114 ? 29.212  44.569  32.071  1.00 50.43  ? 114 ASN B CB  1 
ATOM   3433 C CG  . ASN B 2 114 ? 29.211  43.948  30.691  1.00 49.01  ? 114 ASN B CG  1 
ATOM   3434 O OD1 . ASN B 2 114 ? 30.262  43.581  30.163  1.00 52.72  ? 114 ASN B OD1 1 
ATOM   3435 N ND2 . ASN B 2 114 ? 28.032  43.833  30.094  1.00 47.68  ? 114 ASN B ND2 1 
ATOM   3436 N N   . VAL B 2 115 ? 29.862  44.793  35.179  1.00 55.46  ? 115 VAL B N   1 
ATOM   3437 C CA  . VAL B 2 115 ? 29.978  45.603  36.389  1.00 55.10  ? 115 VAL B CA  1 
ATOM   3438 C C   . VAL B 2 115 ? 31.361  45.441  37.012  1.00 56.56  ? 115 VAL B C   1 
ATOM   3439 O O   . VAL B 2 115 ? 32.020  46.428  37.363  1.00 58.63  ? 115 VAL B O   1 
ATOM   3440 C CB  . VAL B 2 115 ? 28.862  45.246  37.385  1.00 54.62  ? 115 VAL B CB  1 
ATOM   3441 C CG1 . VAL B 2 115 ? 29.052  46.005  38.687  1.00 56.81  ? 115 VAL B CG1 1 
ATOM   3442 C CG2 . VAL B 2 115 ? 27.506  45.558  36.784  1.00 53.55  ? 115 VAL B CG2 1 
ATOM   3443 N N   . LYS B 2 116 ? 31.822  44.192  37.155  1.00 55.68  ? 116 LYS B N   1 
ATOM   3444 C CA  . LYS B 2 116 ? 33.158  43.957  37.700  1.00 57.15  ? 116 LYS B CA  1 
ATOM   3445 C C   . LYS B 2 116 ? 34.223  44.697  36.898  1.00 58.40  ? 116 LYS B C   1 
ATOM   3446 O O   . LYS B 2 116 ? 35.112  45.341  37.470  1.00 60.54  ? 116 LYS B O   1 
ATOM   3447 C CB  . LYS B 2 116 ? 33.451  42.454  37.730  1.00 55.92  ? 116 LYS B CB  1 
ATOM   3448 C CG  . LYS B 2 116 ? 34.850  42.072  38.210  1.00 57.44  ? 116 LYS B CG  1 
ATOM   3449 C CD  . LYS B 2 116 ? 35.062  42.408  39.679  1.00 64.35  ? 116 LYS B CD  1 
ATOM   3450 C CE  . LYS B 2 116 ? 36.442  41.975  40.153  1.00 60.97  ? 116 LYS B CE  1 
ATOM   3451 N NZ  . LYS B 2 116 ? 36.636  40.500  40.083  1.00 81.35  ? 116 LYS B NZ  1 
ATOM   3452 N N   . ASN B 2 117 ? 34.128  44.642  35.568  1.00 61.99  ? 117 ASN B N   1 
ATOM   3453 C CA  . ASN B 2 117 ? 35.128  45.286  34.725  1.00 63.87  ? 117 ASN B CA  1 
ATOM   3454 C C   . ASN B 2 117 ? 35.068  46.802  34.846  1.00 60.38  ? 117 ASN B C   1 
ATOM   3455 O O   . ASN B 2 117 ? 36.108  47.469  34.817  1.00 62.40  ? 117 ASN B O   1 
ATOM   3456 C CB  . ASN B 2 117 ? 34.941  44.862  33.269  1.00 56.96  ? 117 ASN B CB  1 
ATOM   3457 C CG  . ASN B 2 117 ? 35.329  43.419  33.026  1.00 55.66  ? 117 ASN B CG  1 
ATOM   3458 O OD1 . ASN B 2 117 ? 36.073  42.822  33.804  1.00 60.72  ? 117 ASN B OD1 1 
ATOM   3459 N ND2 . ASN B 2 117 ? 34.831  42.853  31.933  1.00 56.74  ? 117 ASN B ND2 1 
ATOM   3460 N N   . LEU B 2 118 ? 33.865  47.367  34.967  1.00 59.88  ? 118 LEU B N   1 
ATOM   3461 C CA  . LEU B 2 118 ? 33.751  48.813  35.138  1.00 61.80  ? 118 LEU B CA  1 
ATOM   3462 C C   . LEU B 2 118 ? 34.386  49.254  36.452  1.00 63.94  ? 118 LEU B C   1 
ATOM   3463 O O   . LEU B 2 118 ? 35.160  50.222  36.495  1.00 66.16  ? 118 LEU B O   1 
ATOM   3464 C CB  . LEU B 2 118 ? 32.281  49.229  35.076  1.00 60.90  ? 118 LEU B CB  1 
ATOM   3465 C CG  . LEU B 2 118 ? 31.979  50.719  35.230  1.00 62.88  ? 118 LEU B CG  1 
ATOM   3466 C CD1 . LEU B 2 118 ? 32.627  51.520  34.115  1.00 65.22  ? 118 LEU B CD1 1 
ATOM   3467 C CD2 . LEU B 2 118 ? 30.482  50.954  35.254  1.00 61.95  ? 118 LEU B CD2 1 
ATOM   3468 N N   . TYR B 2 119 ? 34.072  48.541  37.537  1.00 63.45  ? 119 TYR B N   1 
ATOM   3469 C CA  . TYR B 2 119 ? 34.682  48.834  38.831  1.00 65.53  ? 119 TYR B CA  1 
ATOM   3470 C C   . TYR B 2 119 ? 36.202  48.755  38.753  1.00 67.56  ? 119 TYR B C   1 
ATOM   3471 O O   . TYR B 2 119 ? 36.908  49.622  39.282  1.00 74.01  ? 119 TYR B O   1 
ATOM   3472 C CB  . TYR B 2 119 ? 34.142  47.870  39.887  1.00 64.65  ? 119 TYR B CB  1 
ATOM   3473 C CG  . TYR B 2 119 ? 34.764  48.028  41.256  1.00 66.80  ? 119 TYR B CG  1 
ATOM   3474 C CD1 . TYR B 2 119 ? 34.312  48.999  42.137  1.00 70.53  ? 119 TYR B CD1 1 
ATOM   3475 C CD2 . TYR B 2 119 ? 35.794  47.194  41.674  1.00 67.30  ? 119 TYR B CD2 1 
ATOM   3476 C CE1 . TYR B 2 119 ? 34.873  49.145  43.392  1.00 75.21  ? 119 TYR B CE1 1 
ATOM   3477 C CE2 . TYR B 2 119 ? 36.362  47.333  42.927  1.00 69.42  ? 119 TYR B CE2 1 
ATOM   3478 C CZ  . TYR B 2 119 ? 35.898  48.310  43.782  1.00 76.99  ? 119 TYR B CZ  1 
ATOM   3479 O OH  . TYR B 2 119 ? 36.456  48.455  45.031  1.00 73.31  ? 119 TYR B OH  1 
ATOM   3480 N N   . GLU B 2 120 ? 36.725  47.719  38.089  1.00 65.75  ? 120 GLU B N   1 
ATOM   3481 C CA  . GLU B 2 120 ? 38.174  47.600  37.956  1.00 67.27  ? 120 GLU B CA  1 
ATOM   3482 C C   . GLU B 2 120 ? 38.758  48.730  37.117  1.00 68.85  ? 120 GLU B C   1 
ATOM   3483 O O   . GLU B 2 120 ? 39.898  49.148  37.350  1.00 78.89  ? 120 GLU B O   1 
ATOM   3484 C CB  . GLU B 2 120 ? 38.542  46.244  37.353  1.00 65.63  ? 120 GLU B CB  1 
ATOM   3485 C CG  . GLU B 2 120 ? 38.182  45.056  38.227  1.00 64.50  ? 120 GLU B CG  1 
ATOM   3486 C CD  . GLU B 2 120 ? 38.909  45.062  39.559  1.00 93.00  ? 120 GLU B CD  1 
ATOM   3487 O OE1 . GLU B 2 120 ? 40.046  45.578  39.624  1.00 90.90  ? 120 GLU B OE1 1 
ATOM   3488 O OE2 . GLU B 2 120 ? 38.339  44.550  40.544  1.00 91.89  ? 120 GLU B OE2 1 
ATOM   3489 N N   . LYS B 2 121 ? 38.000  49.232  36.140  1.00 67.89  ? 121 LYS B N   1 
ATOM   3490 C CA  . LYS B 2 121 ? 38.462  50.378  35.362  1.00 69.60  ? 121 LYS B CA  1 
ATOM   3491 C C   . LYS B 2 121 ? 38.602  51.613  36.241  1.00 75.88  ? 121 LYS B C   1 
ATOM   3492 O O   . LYS B 2 121 ? 39.653  52.267  36.256  1.00 74.51  ? 121 LYS B O   1 
ATOM   3493 C CB  . LYS B 2 121 ? 37.498  50.658  34.209  1.00 68.14  ? 121 LYS B CB  1 
ATOM   3494 C CG  . LYS B 2 121 ? 37.538  49.651  33.080  1.00 72.49  ? 121 LYS B CG  1 
ATOM   3495 C CD  . LYS B 2 121 ? 36.484  49.988  32.033  1.00 91.12  ? 121 LYS B CD  1 
ATOM   3496 C CE  . LYS B 2 121 ? 36.331  48.881  31.002  1.00 101.79 ? 121 LYS B CE  1 
ATOM   3497 N NZ  . LYS B 2 121 ? 35.185  49.146  30.086  1.00 96.14  ? 121 LYS B NZ  1 
ATOM   3498 N N   . VAL B 2 122 ? 37.540  51.952  36.979  1.00 74.14  ? 122 VAL B N   1 
ATOM   3499 C CA  . VAL B 2 122 ? 37.579  53.139  37.831  1.00 74.27  ? 122 VAL B CA  1 
ATOM   3500 C C   . VAL B 2 122 ? 38.678  53.010  38.879  1.00 76.20  ? 122 VAL B C   1 
ATOM   3501 O O   . VAL B 2 122 ? 39.413  53.968  39.152  1.00 78.86  ? 122 VAL B O   1 
ATOM   3502 C CB  . VAL B 2 122 ? 36.200  53.379  38.475  1.00 73.52  ? 122 VAL B CB  1 
ATOM   3503 C CG1 . VAL B 2 122 ? 36.270  54.513  39.487  1.00 76.56  ? 122 VAL B CG1 1 
ATOM   3504 C CG2 . VAL B 2 122 ? 35.169  53.686  37.402  1.00 72.10  ? 122 VAL B CG2 1 
ATOM   3505 N N   . LYS B 2 123 ? 38.813  51.824  39.475  1.00 75.06  ? 123 LYS B N   1 
ATOM   3506 C CA  . LYS B 2 123 ? 39.883  51.590  40.441  1.00 76.92  ? 123 LYS B CA  1 
ATOM   3507 C C   . LYS B 2 123 ? 41.252  51.815  39.810  1.00 78.60  ? 123 LYS B C   1 
ATOM   3508 O O   . LYS B 2 123 ? 42.102  52.521  40.370  1.00 81.32  ? 123 LYS B O   1 
ATOM   3509 C CB  . LYS B 2 123 ? 39.769  50.172  40.998  1.00 85.32  ? 123 LYS B CB  1 
ATOM   3510 C CG  . LYS B 2 123 ? 40.905  49.754  41.908  1.00 77.12  ? 123 LYS B CG  1 
ATOM   3511 C CD  . LYS B 2 123 ? 40.755  48.298  42.304  1.00 75.44  ? 123 LYS B CD  1 
ATOM   3512 C CE  . LYS B 2 123 ? 41.821  47.874  43.295  1.00 77.46  ? 123 LYS B CE  1 
ATOM   3513 N NZ  . LYS B 2 123 ? 41.612  46.472  43.751  1.00 80.59  ? 123 LYS B NZ  1 
ATOM   3514 N N   . SER B 2 124 ? 41.476  51.228  38.631  1.00 77.14  ? 124 SER B N   1 
ATOM   3515 C CA  . SER B 2 124 ? 42.736  51.419  37.922  1.00 81.10  ? 124 SER B CA  1 
ATOM   3516 C C   . SER B 2 124 ? 42.975  52.877  37.553  1.00 93.61  ? 124 SER B C   1 
ATOM   3517 O O   . SER B 2 124 ? 44.126  53.269  37.333  1.00 87.01  ? 124 SER B O   1 
ATOM   3518 C CB  . SER B 2 124 ? 42.763  50.557  36.661  1.00 79.02  ? 124 SER B CB  1 
ATOM   3519 O OG  . SER B 2 124 ? 41.752  50.964  35.756  1.00 87.69  ? 124 SER B OG  1 
ATOM   3520 N N   . GLN B 2 125 ? 41.917  53.684  37.469  1.00 97.85  ? 125 GLN B N   1 
ATOM   3521 C CA  . GLN B 2 125 ? 42.101  55.111  37.230  1.00 91.92  ? 125 GLN B CA  1 
ATOM   3522 C C   . GLN B 2 125 ? 42.498  55.844  38.504  1.00 91.13  ? 125 GLN B C   1 
ATOM   3523 O O   . GLN B 2 125 ? 43.439  56.645  38.501  1.00 93.75  ? 125 GLN B O   1 
ATOM   3524 C CB  . GLN B 2 125 ? 40.826  55.720  36.652  1.00 95.43  ? 125 GLN B CB  1 
ATOM   3525 C CG  . GLN B 2 125 ? 40.671  55.528  35.166  1.00 104.97 ? 125 GLN B CG  1 
ATOM   3526 C CD  . GLN B 2 125 ? 39.918  56.669  34.527  1.00 95.81  ? 125 GLN B CD  1 
ATOM   3527 O OE1 . GLN B 2 125 ? 40.479  57.431  33.742  1.00 100.78 ? 125 GLN B OE1 1 
ATOM   3528 N NE2 . GLN B 2 125 ? 38.642  56.803  34.869  1.00 88.95  ? 125 GLN B NE2 1 
ATOM   3529 N N   . LEU B 2 126 ? 41.788  55.584  39.604  1.00 88.10  ? 126 LEU B N   1 
ATOM   3530 C CA  . LEU B 2 126 ? 41.993  56.371  40.814  1.00 87.68  ? 126 LEU B CA  1 
ATOM   3531 C C   . LEU B 2 126 ? 43.307  56.018  41.499  1.00 89.59  ? 126 LEU B C   1 
ATOM   3532 O O   . LEU B 2 126 ? 44.001  56.907  42.007  1.00 94.22  ? 126 LEU B O   1 
ATOM   3533 C CB  . LEU B 2 126 ? 40.817  56.176  41.770  1.00 86.54  ? 126 LEU B CB  1 
ATOM   3534 C CG  . LEU B 2 126 ? 39.449  56.588  41.222  1.00 84.96  ? 126 LEU B CG  1 
ATOM   3535 C CD1 . LEU B 2 126 ? 38.390  56.509  42.309  1.00 84.51  ? 126 LEU B CD1 1 
ATOM   3536 C CD2 . LEU B 2 126 ? 39.504  57.983  40.615  1.00 86.99  ? 126 LEU B CD2 1 
ATOM   3537 N N   . LYS B 2 127 ? 43.664  54.738  41.525  1.00 107.89 ? 127 LYS B N   1 
ATOM   3538 C CA  . LYS B 2 127 ? 44.889  54.267  42.203  1.00 100.24 ? 127 LYS B CA  1 
ATOM   3539 C C   . LYS B 2 127 ? 44.766  54.647  43.683  1.00 99.43  ? 127 LYS B C   1 
ATOM   3540 O O   . LYS B 2 127 ? 43.692  54.471  44.278  1.00 101.28 ? 127 LYS B O   1 
ATOM   3541 C CB  . LYS B 2 127 ? 46.123  54.805  41.500  1.00 96.14  ? 127 LYS B CB  1 
ATOM   3542 C CG  . LYS B 2 127 ? 46.196  54.479  40.018  1.00 95.53  ? 127 LYS B CG  1 
ATOM   3543 C CD  . LYS B 2 127 ? 47.382  55.168  39.362  1.00 100.31 ? 127 LYS B CD  1 
ATOM   3544 C CE  . LYS B 2 127 ? 47.387  54.950  37.858  1.00 105.38 ? 127 LYS B CE  1 
ATOM   3545 N NZ  . LYS B 2 127 ? 48.496  55.692  37.199  1.00 110.00 ? 127 LYS B NZ  1 
ATOM   3546 N N   . ASN B 2 128 ? 45.820  55.179  44.304  1.00 103.98 ? 128 ASN B N   1 
ATOM   3547 C CA  . ASN B 2 128 ? 45.819  55.464  45.733  1.00 102.87 ? 128 ASN B CA  1 
ATOM   3548 C C   . ASN B 2 128 ? 45.365  56.884  46.060  1.00 98.68  ? 128 ASN B C   1 
ATOM   3549 O O   . ASN B 2 128 ? 45.583  57.349  47.185  1.00 101.07 ? 128 ASN B O   1 
ATOM   3550 C CB  . ASN B 2 128 ? 47.208  55.210  46.324  1.00 99.30  ? 128 ASN B CB  1 
ATOM   3551 C CG  . ASN B 2 128 ? 48.250  56.173  45.801  1.00 102.05 ? 128 ASN B CG  1 
ATOM   3552 O OD1 . ASN B 2 128 ? 48.134  56.690  44.691  1.00 101.54 ? 128 ASN B OD1 1 
ATOM   3553 N ND2 . ASN B 2 128 ? 49.280  56.419  46.602  1.00 109.87 ? 128 ASN B ND2 1 
ATOM   3554 N N   . ASN B 2 129 ? 44.742  57.582  45.113  1.00 97.86  ? 129 ASN B N   1 
ATOM   3555 C CA  . ASN B 2 129 ? 44.156  58.887  45.392  1.00 99.55  ? 129 ASN B CA  1 
ATOM   3556 C C   . ASN B 2 129 ? 42.780  58.785  46.035  1.00 98.05  ? 129 ASN B C   1 
ATOM   3557 O O   . ASN B 2 129 ? 42.126  59.815  46.233  1.00 99.23  ? 129 ASN B O   1 
ATOM   3558 C CB  . ASN B 2 129 ? 44.069  59.714  44.107  1.00 99.62  ? 129 ASN B CB  1 
ATOM   3559 C CG  . ASN B 2 129 ? 45.429  60.152  43.607  1.00 107.31 ? 129 ASN B CG  1 
ATOM   3560 O OD1 . ASN B 2 129 ? 46.458  59.650  44.058  1.00 110.97 ? 129 ASN B OD1 1 
ATOM   3561 N ND2 . ASN B 2 129 ? 45.443  61.095  42.672  1.00 103.05 ? 129 ASN B ND2 1 
ATOM   3562 N N   . ALA B 2 130 ? 42.333  57.575  46.358  1.00 95.67  ? 130 ALA B N   1 
ATOM   3563 C CA  . ALA B 2 130 ? 41.053  57.347  47.009  1.00 94.31  ? 130 ALA B CA  1 
ATOM   3564 C C   . ALA B 2 130 ? 41.090  55.964  47.636  1.00 92.83  ? 130 ALA B C   1 
ATOM   3565 O O   . ALA B 2 130 ? 41.798  55.074  47.156  1.00 91.77  ? 130 ALA B O   1 
ATOM   3566 C CB  . ALA B 2 130 ? 39.885  57.463  46.024  1.00 92.45  ? 130 ALA B CB  1 
ATOM   3567 N N   . LYS B 2 131 ? 40.333  55.789  48.712  1.00 92.95  ? 131 LYS B N   1 
ATOM   3568 C CA  . LYS B 2 131 ? 40.313  54.513  49.406  1.00 91.86  ? 131 LYS B CA  1 
ATOM   3569 C C   . LYS B 2 131 ? 39.059  53.729  49.041  1.00 100.00 ? 131 LYS B C   1 
ATOM   3570 O O   . LYS B 2 131 ? 38.013  54.300  48.716  1.00 89.10  ? 131 LYS B O   1 
ATOM   3571 C CB  . LYS B 2 131 ? 40.403  54.699  50.923  1.00 96.74  ? 131 LYS B CB  1 
ATOM   3572 C CG  . LYS B 2 131 ? 39.081  54.886  51.642  1.00 98.33  ? 131 LYS B CG  1 
ATOM   3573 C CD  . LYS B 2 131 ? 39.304  54.867  53.145  1.00 103.83 ? 131 LYS B CD  1 
ATOM   3574 C CE  . LYS B 2 131 ? 38.003  54.975  53.914  1.00 105.49 ? 131 LYS B CE  1 
ATOM   3575 N NZ  . LYS B 2 131 ? 38.236  54.928  55.383  1.00 109.21 ? 131 LYS B NZ  1 
ATOM   3576 N N   . GLU B 2 132 ? 39.185  52.403  49.088  1.00 98.81  ? 132 GLU B N   1 
ATOM   3577 C CA  . GLU B 2 132 ? 38.115  51.501  48.667  1.00 97.54  ? 132 GLU B CA  1 
ATOM   3578 C C   . GLU B 2 132 ? 37.240  51.149  49.865  1.00 104.71 ? 132 GLU B C   1 
ATOM   3579 O O   . GLU B 2 132 ? 37.420  50.129  50.534  1.00 110.44 ? 132 GLU B O   1 
ATOM   3580 C CB  . GLU B 2 132 ? 38.695  50.249  48.022  1.00 98.92  ? 132 GLU B CB  1 
ATOM   3581 C CG  . GLU B 2 132 ? 39.000  50.383  46.545  1.00 98.87  ? 132 GLU B CG  1 
ATOM   3582 C CD  . GLU B 2 132 ? 39.365  49.056  45.913  1.00 107.44 ? 132 GLU B CD  1 
ATOM   3583 O OE1 . GLU B 2 132 ? 40.141  48.296  46.530  1.00 108.04 ? 132 GLU B OE1 1 
ATOM   3584 O OE2 . GLU B 2 132 ? 38.863  48.765  44.808  1.00 113.65 ? 132 GLU B OE2 1 
ATOM   3585 N N   . ILE B 2 133 ? 36.264  52.020  50.134  1.00 113.11 ? 133 ILE B N   1 
ATOM   3586 C CA  . ILE B 2 133 ? 35.203  51.637  51.049  1.00 115.64 ? 133 ILE B CA  1 
ATOM   3587 C C   . ILE B 2 133 ? 34.389  50.517  50.404  1.00 116.89 ? 133 ILE B C   1 
ATOM   3588 O O   . ILE B 2 133 ? 34.405  50.318  49.182  1.00 128.43 ? 133 ILE B O   1 
ATOM   3589 C CB  . ILE B 2 133 ? 34.304  52.828  51.418  1.00 122.59 ? 133 ILE B CB  1 
ATOM   3590 C CG1 . ILE B 2 133 ? 33.897  53.603  50.164  1.00 124.98 ? 133 ILE B CG1 1 
ATOM   3591 C CG2 . ILE B 2 133 ? 34.997  53.732  52.424  1.00 119.89 ? 133 ILE B CG2 1 
ATOM   3592 C CD1 . ILE B 2 133 ? 33.082  54.845  50.457  1.00 125.99 ? 133 ILE B CD1 1 
ATOM   3593 N N   . GLY B 2 134 ? 33.671  49.775  51.241  1.00 118.59 ? 134 GLY B N   1 
ATOM   3594 C CA  . GLY B 2 134 ? 32.886  48.652  50.766  1.00 122.25 ? 134 GLY B CA  1 
ATOM   3595 C C   . GLY B 2 134 ? 31.782  49.042  49.803  1.00 113.82 ? 134 GLY B C   1 
ATOM   3596 O O   . GLY B 2 134 ? 31.609  50.224  49.485  1.00 117.80 ? 134 GLY B O   1 
ATOM   3597 N N   . ASN B 2 135 ? 31.039  48.046  49.321  1.00 93.85  ? 135 ASN B N   1 
ATOM   3598 C CA  . ASN B 2 135 ? 29.882  48.240  48.449  1.00 85.36  ? 135 ASN B CA  1 
ATOM   3599 C C   . ASN B 2 135 ? 30.257  48.857  47.105  1.00 74.76  ? 135 ASN B C   1 
ATOM   3600 O O   . ASN B 2 135 ? 29.395  49.400  46.407  1.00 70.21  ? 135 ASN B O   1 
ATOM   3601 C CB  . ASN B 2 135 ? 28.805  49.084  49.140  1.00 99.33  ? 135 ASN B CB  1 
ATOM   3602 C CG  . ASN B 2 135 ? 27.405  48.563  48.888  1.00 97.89  ? 135 ASN B CG  1 
ATOM   3603 O OD1 . ASN B 2 135 ? 27.093  48.085  47.798  1.00 95.64  ? 135 ASN B OD1 1 
ATOM   3604 N ND2 . ASN B 2 135 ? 26.552  48.647  49.904  1.00 96.96  ? 135 ASN B ND2 1 
ATOM   3605 N N   . GLY B 2 136 ? 31.530  48.787  46.725  1.00 83.01  ? 136 GLY B N   1 
ATOM   3606 C CA  . GLY B 2 136 ? 31.948  49.265  45.422  1.00 80.74  ? 136 GLY B CA  1 
ATOM   3607 C C   . GLY B 2 136 ? 32.040  50.767  45.273  1.00 80.96  ? 136 GLY B C   1 
ATOM   3608 O O   . GLY B 2 136 ? 31.899  51.279  44.158  1.00 77.31  ? 136 GLY B O   1 
ATOM   3609 N N   . CYS B 2 137 ? 32.275  51.493  46.361  1.00 77.94  ? 137 CYS B N   1 
ATOM   3610 C CA  . CYS B 2 137 ? 32.431  52.938  46.319  1.00 90.07  ? 137 CYS B CA  1 
ATOM   3611 C C   . CYS B 2 137 ? 33.881  53.321  46.582  1.00 79.34  ? 137 CYS B C   1 
ATOM   3612 O O   . CYS B 2 137 ? 34.666  52.544  47.133  1.00 84.70  ? 137 CYS B O   1 
ATOM   3613 C CB  . CYS B 2 137 ? 31.522  53.627  47.342  1.00 85.07  ? 137 CYS B CB  1 
ATOM   3614 S SG  . CYS B 2 137 ? 29.752  53.433  47.050  1.00 90.55  ? 137 CYS B SG  1 
ATOM   3615 N N   . PHE B 2 138 ? 34.229  54.539  46.178  1.00 81.04  ? 138 PHE B N   1 
ATOM   3616 C CA  . PHE B 2 138 ? 35.553  55.100  46.407  1.00 86.64  ? 138 PHE B CA  1 
ATOM   3617 C C   . PHE B 2 138 ? 35.414  56.395  47.190  1.00 87.06  ? 138 PHE B C   1 
ATOM   3618 O O   . PHE B 2 138 ? 34.647  57.281  46.798  1.00 86.75  ? 138 PHE B O   1 
ATOM   3619 C CB  . PHE B 2 138 ? 36.285  55.366  45.088  1.00 91.95  ? 138 PHE B CB  1 
ATOM   3620 C CG  . PHE B 2 138 ? 36.541  54.134  44.272  1.00 80.50  ? 138 PHE B CG  1 
ATOM   3621 C CD1 . PHE B 2 138 ? 37.670  53.361  44.492  1.00 80.82  ? 138 PHE B CD1 1 
ATOM   3622 C CD2 . PHE B 2 138 ? 35.663  53.757  43.270  1.00 84.92  ? 138 PHE B CD2 1 
ATOM   3623 C CE1 . PHE B 2 138 ? 37.911  52.230  43.735  1.00 78.58  ? 138 PHE B CE1 1 
ATOM   3624 C CE2 . PHE B 2 138 ? 35.898  52.627  42.510  1.00 75.63  ? 138 PHE B CE2 1 
ATOM   3625 C CZ  . PHE B 2 138 ? 37.024  51.863  42.743  1.00 75.98  ? 138 PHE B CZ  1 
ATOM   3626 N N   . GLU B 2 139 ? 36.153  56.505  48.290  1.00 102.44 ? 139 GLU B N   1 
ATOM   3627 C CA  . GLU B 2 139 ? 36.187  57.726  49.084  1.00 93.03  ? 139 GLU B CA  1 
ATOM   3628 C C   . GLU B 2 139 ? 37.414  58.531  48.679  1.00 94.11  ? 139 GLU B C   1 
ATOM   3629 O O   . GLU B 2 139 ? 38.549  58.088  48.888  1.00 94.87  ? 139 GLU B O   1 
ATOM   3630 C CB  . GLU B 2 139 ? 36.207  57.415  50.579  1.00 101.19 ? 139 GLU B CB  1 
ATOM   3631 C CG  . GLU B 2 139 ? 35.706  58.562  51.444  1.00 112.50 ? 139 GLU B CG  1 
ATOM   3632 C CD  . GLU B 2 139 ? 35.707  58.223  52.921  1.00 123.17 ? 139 GLU B CD  1 
ATOM   3633 O OE1 . GLU B 2 139 ? 36.789  57.907  53.458  1.00 123.99 ? 139 GLU B OE1 1 
ATOM   3634 O OE2 . GLU B 2 139 ? 34.624  58.267  53.542  1.00 127.72 ? 139 GLU B OE2 1 
ATOM   3635 N N   . PHE B 2 140 ? 37.182  59.706  48.100  1.00 95.24  ? 140 PHE B N   1 
ATOM   3636 C CA  . PHE B 2 140 ? 38.268  60.516  47.569  1.00 101.51 ? 140 PHE B CA  1 
ATOM   3637 C C   . PHE B 2 140 ? 39.129  61.090  48.688  1.00 113.44 ? 140 PHE B C   1 
ATOM   3638 O O   . PHE B 2 140 ? 38.624  61.520  49.729  1.00 109.88 ? 140 PHE B O   1 
ATOM   3639 C CB  . PHE B 2 140 ? 37.713  61.655  46.715  1.00 106.85 ? 140 PHE B CB  1 
ATOM   3640 C CG  . PHE B 2 140 ? 37.192  61.215  45.380  1.00 98.70  ? 140 PHE B CG  1 
ATOM   3641 C CD1 . PHE B 2 140 ? 38.060  60.992  44.325  1.00 103.21 ? 140 PHE B CD1 1 
ATOM   3642 C CD2 . PHE B 2 140 ? 35.835  61.033  45.175  1.00 96.18  ? 140 PHE B CD2 1 
ATOM   3643 C CE1 . PHE B 2 140 ? 37.585  60.589  43.093  1.00 100.32 ? 140 PHE B CE1 1 
ATOM   3644 C CE2 . PHE B 2 140 ? 35.355  60.632  43.944  1.00 93.53  ? 140 PHE B CE2 1 
ATOM   3645 C CZ  . PHE B 2 140 ? 36.231  60.410  42.902  1.00 94.87  ? 140 PHE B CZ  1 
ATOM   3646 N N   . TYR B 2 141 ? 40.440  61.096  48.461  1.00 114.65 ? 141 TYR B N   1 
ATOM   3647 C CA  . TYR B 2 141 ? 41.395  61.736  49.353  1.00 114.14 ? 141 TYR B CA  1 
ATOM   3648 C C   . TYR B 2 141 ? 41.681  63.181  48.966  1.00 117.00 ? 141 TYR B C   1 
ATOM   3649 O O   . TYR B 2 141 ? 42.583  63.797  49.542  1.00 123.45 ? 141 TYR B O   1 
ATOM   3650 C CB  . TYR B 2 141 ? 42.706  60.945  49.383  1.00 115.45 ? 141 TYR B CB  1 
ATOM   3651 C CG  . TYR B 2 141 ? 42.701  59.766  50.327  1.00 116.63 ? 141 TYR B CG  1 
ATOM   3652 C CD1 . TYR B 2 141 ? 41.869  59.743  51.438  1.00 119.14 ? 141 TYR B CD1 1 
ATOM   3653 C CD2 . TYR B 2 141 ? 43.536  58.678  50.111  1.00 118.72 ? 141 TYR B CD2 1 
ATOM   3654 C CE1 . TYR B 2 141 ? 41.866  58.667  52.305  1.00 124.39 ? 141 TYR B CE1 1 
ATOM   3655 C CE2 . TYR B 2 141 ? 43.539  57.598  50.971  1.00 119.77 ? 141 TYR B CE2 1 
ATOM   3656 C CZ  . TYR B 2 141 ? 42.704  57.597  52.066  1.00 123.57 ? 141 TYR B CZ  1 
ATOM   3657 O OH  . TYR B 2 141 ? 42.706  56.522  52.925  1.00 122.65 ? 141 TYR B OH  1 
ATOM   3658 N N   . HIS B 2 142 ? 40.943  63.733  48.005  1.00 110.87 ? 142 HIS B N   1 
ATOM   3659 C CA  . HIS B 2 142 ? 41.179  65.089  47.535  1.00 109.95 ? 142 HIS B CA  1 
ATOM   3660 C C   . HIS B 2 142 ? 39.857  65.686  47.069  1.00 115.00 ? 142 HIS B C   1 
ATOM   3661 O O   . HIS B 2 142 ? 38.806  65.042  47.125  1.00 106.51 ? 142 HIS B O   1 
ATOM   3662 C CB  . HIS B 2 142 ? 42.227  65.108  46.418  1.00 110.12 ? 142 HIS B CB  1 
ATOM   3663 C CG  . HIS B 2 142 ? 41.811  64.364  45.187  1.00 110.80 ? 142 HIS B CG  1 
ATOM   3664 N ND1 . HIS B 2 142 ? 40.970  64.904  44.239  1.00 108.25 ? 142 HIS B ND1 1 
ATOM   3665 C CD2 . HIS B 2 142 ? 42.118  63.119  44.751  1.00 112.37 ? 142 HIS B CD2 1 
ATOM   3666 C CE1 . HIS B 2 142 ? 40.778  64.026  43.271  1.00 105.21 ? 142 HIS B CE1 1 
ATOM   3667 N NE2 . HIS B 2 142 ? 41.463  62.934  43.557  1.00 101.68 ? 142 HIS B NE2 1 
ATOM   3668 N N   . LYS B 2 143 ? 39.919  66.931  46.605  1.00 125.79 ? 143 LYS B N   1 
ATOM   3669 C CA  . LYS B 2 143 ? 38.739  67.609  46.091  1.00 129.49 ? 143 LYS B CA  1 
ATOM   3670 C C   . LYS B 2 143 ? 38.455  67.172  44.661  1.00 122.23 ? 143 LYS B C   1 
ATOM   3671 O O   . LYS B 2 143 ? 39.371  66.999  43.852  1.00 123.63 ? 143 LYS B O   1 
ATOM   3672 C CB  . LYS B 2 143 ? 38.920  69.126  46.150  1.00 140.91 ? 143 LYS B CB  1 
ATOM   3673 C CG  . LYS B 2 143 ? 38.774  69.714  47.544  1.00 148.04 ? 143 LYS B CG  1 
ATOM   3674 C CD  . LYS B 2 143 ? 37.388  69.440  48.112  1.00 150.28 ? 143 LYS B CD  1 
ATOM   3675 C CE  . LYS B 2 143 ? 36.299  70.045  47.237  1.00 153.10 ? 143 LYS B CE  1 
ATOM   3676 N NZ  . LYS B 2 143 ? 34.936  69.677  47.711  1.00 157.94 ? 143 LYS B NZ  1 
ATOM   3677 N N   . CYS B 2 144 ? 37.171  66.999  44.352  1.00 111.48 ? 144 CYS B N   1 
ATOM   3678 C CA  . CYS B 2 144 ? 36.736  66.507  43.045  1.00 106.69 ? 144 CYS B CA  1 
ATOM   3679 C C   . CYS B 2 144 ? 35.419  67.194  42.700  1.00 117.03 ? 144 CYS B C   1 
ATOM   3680 O O   . CYS B 2 144 ? 34.351  66.751  43.133  1.00 109.37 ? 144 CYS B O   1 
ATOM   3681 C CB  . CYS B 2 144 ? 36.590  64.989  43.058  1.00 107.60 ? 144 CYS B CB  1 
ATOM   3682 S SG  . CYS B 2 144 ? 36.153  64.235  41.473  1.00 105.46 ? 144 CYS B SG  1 
ATOM   3683 N N   . ASN B 2 145 ? 35.496  68.272  41.925  1.00 130.76 ? 145 ASN B N   1 
ATOM   3684 C CA  . ASN B 2 145 ? 34.303  68.980  41.481  1.00 130.34 ? 145 ASN B CA  1 
ATOM   3685 C C   . ASN B 2 145 ? 33.665  68.214  40.321  1.00 123.98 ? 145 ASN B C   1 
ATOM   3686 O O   . ASN B 2 145 ? 34.067  67.097  39.986  1.00 115.75 ? 145 ASN B O   1 
ATOM   3687 C CB  . ASN B 2 145 ? 34.647  70.419  41.103  1.00 132.58 ? 145 ASN B CB  1 
ATOM   3688 C CG  . ASN B 2 145 ? 35.726  70.502  40.041  1.00 136.22 ? 145 ASN B CG  1 
ATOM   3689 O OD1 . ASN B 2 145 ? 36.690  69.737  40.060  1.00 132.83 ? 145 ASN B OD1 1 
ATOM   3690 N ND2 . ASN B 2 145 ? 35.570  71.434  39.108  1.00 142.87 ? 145 ASN B ND2 1 
ATOM   3691 N N   . ASP B 2 146 ? 32.650  68.816  39.694  1.00 122.95 ? 146 ASP B N   1 
ATOM   3692 C CA  . ASP B 2 146 ? 31.983  68.164  38.572  1.00 104.74 ? 146 ASP B CA  1 
ATOM   3693 C C   . ASP B 2 146 ? 32.944  67.910  37.420  1.00 102.76 ? 146 ASP B C   1 
ATOM   3694 O O   . ASP B 2 146 ? 32.805  66.912  36.704  1.00 109.41 ? 146 ASP B O   1 
ATOM   3695 C CB  . ASP B 2 146 ? 30.798  69.009  38.105  1.00 108.40 ? 146 ASP B CB  1 
ATOM   3696 C CG  . ASP B 2 146 ? 29.747  69.181  39.184  1.00 115.27 ? 146 ASP B CG  1 
ATOM   3697 O OD1 . ASP B 2 146 ? 30.015  68.793  40.341  1.00 110.59 ? 146 ASP B OD1 1 
ATOM   3698 O OD2 . ASP B 2 146 ? 28.659  69.712  38.879  1.00 119.10 ? 146 ASP B OD2 1 
ATOM   3699 N N   . GLU B 2 147 ? 33.924  68.794  37.228  1.00 109.16 ? 147 GLU B N   1 
ATOM   3700 C CA  . GLU B 2 147 ? 34.953  68.568  36.218  1.00 112.30 ? 147 GLU B CA  1 
ATOM   3701 C C   . GLU B 2 147 ? 35.711  67.272  36.489  1.00 104.58 ? 147 GLU B C   1 
ATOM   3702 O O   . GLU B 2 147 ? 35.912  66.454  35.583  1.00 101.39 ? 147 GLU B O   1 
ATOM   3703 C CB  . GLU B 2 147 ? 35.907  69.763  36.186  1.00 123.26 ? 147 GLU B CB  1 
ATOM   3704 C CG  . GLU B 2 147 ? 37.227  69.517  35.478  1.00 121.41 ? 147 GLU B CG  1 
ATOM   3705 C CD  . GLU B 2 147 ? 38.178  70.692  35.614  1.00 139.56 ? 147 GLU B CD  1 
ATOM   3706 O OE1 . GLU B 2 147 ? 37.722  71.782  36.021  1.00 139.27 ? 147 GLU B OE1 1 
ATOM   3707 O OE2 . GLU B 2 147 ? 39.381  70.526  35.322  1.00 146.98 ? 147 GLU B OE2 1 
ATOM   3708 N N   . CYS B 2 148 ? 36.125  67.063  37.740  1.00 102.05 ? 148 CYS B N   1 
ATOM   3709 C CA  . CYS B 2 148 ? 36.877  65.861  38.086  1.00 101.52 ? 148 CYS B CA  1 
ATOM   3710 C C   . CYS B 2 148 ? 35.994  64.619  38.042  1.00 110.02 ? 148 CYS B C   1 
ATOM   3711 O O   . CYS B 2 148 ? 36.431  63.557  37.581  1.00 100.38 ? 148 CYS B O   1 
ATOM   3712 C CB  . CYS B 2 148 ? 37.510  66.025  39.467  1.00 105.15 ? 148 CYS B CB  1 
ATOM   3713 S SG  . CYS B 2 148 ? 37.813  64.474  40.333  1.00 101.35 ? 148 CYS B SG  1 
ATOM   3714 N N   . MET B 2 149 ? 34.755  64.729  38.529  1.00 110.34 ? 149 MET B N   1 
ATOM   3715 C CA  . MET B 2 149 ? 33.827  63.604  38.460  1.00 95.85  ? 149 MET B CA  1 
ATOM   3716 C C   . MET B 2 149 ? 33.616  63.162  37.018  1.00 95.78  ? 149 MET B C   1 
ATOM   3717 O O   . MET B 2 149 ? 33.765  61.978  36.687  1.00 99.79  ? 149 MET B O   1 
ATOM   3718 C CB  . MET B 2 149 ? 32.495  63.983  39.107  1.00 98.11  ? 149 MET B CB  1 
ATOM   3719 C CG  . MET B 2 149 ? 32.561  64.198  40.611  1.00 104.20 ? 149 MET B CG  1 
ATOM   3720 S SD  . MET B 2 149 ? 32.918  62.682  41.518  1.00 89.98  ? 149 MET B SD  1 
ATOM   3721 C CE  . MET B 2 149 ? 32.580  63.200  43.198  1.00 92.36  ? 149 MET B CE  1 
ATOM   3722 N N   . GLU B 2 150 ? 33.275  64.107  36.139  1.00 89.55  ? 150 GLU B N   1 
ATOM   3723 C CA  . GLU B 2 150 ? 33.125  63.780  34.727  1.00 87.97  ? 150 GLU B CA  1 
ATOM   3724 C C   . GLU B 2 150 ? 34.436  63.320  34.105  1.00 87.93  ? 150 GLU B C   1 
ATOM   3725 O O   . GLU B 2 150 ? 34.411  62.620  33.088  1.00 92.11  ? 150 GLU B O   1 
ATOM   3726 C CB  . GLU B 2 150 ? 32.571  64.980  33.956  1.00 89.87  ? 150 GLU B CB  1 
ATOM   3727 C CG  . GLU B 2 150 ? 31.206  65.451  34.433  1.00 91.71  ? 150 GLU B CG  1 
ATOM   3728 C CD  . GLU B 2 150 ? 30.155  64.359  34.394  1.00 103.95 ? 150 GLU B CD  1 
ATOM   3729 O OE1 . GLU B 2 150 ? 30.197  63.515  33.473  1.00 109.38 ? 150 GLU B OE1 1 
ATOM   3730 O OE2 . GLU B 2 150 ? 29.286  64.343  35.291  1.00 108.75 ? 150 GLU B OE2 1 
ATOM   3731 N N   . SER B 2 151 ? 35.578  63.697  34.687  1.00 95.00  ? 151 SER B N   1 
ATOM   3732 C CA  . SER B 2 151 ? 36.846  63.140  34.227  1.00 96.03  ? 151 SER B CA  1 
ATOM   3733 C C   . SER B 2 151 ? 36.970  61.669  34.601  1.00 99.39  ? 151 SER B C   1 
ATOM   3734 O O   . SER B 2 151 ? 37.557  60.885  33.846  1.00 95.42  ? 151 SER B O   1 
ATOM   3735 C CB  . SER B 2 151 ? 38.020  63.929  34.805  1.00 94.69  ? 151 SER B CB  1 
ATOM   3736 O OG  . SER B 2 151 ? 38.264  63.566  36.152  1.00 96.87  ? 151 SER B OG  1 
ATOM   3737 N N   . VAL B 2 152 ? 36.431  61.279  35.757  1.00 100.57 ? 152 VAL B N   1 
ATOM   3738 C CA  . VAL B 2 152 ? 36.454  59.872  36.144  1.00 87.22  ? 152 VAL B CA  1 
ATOM   3739 C C   . VAL B 2 152 ? 35.469  59.072  35.301  1.00 80.74  ? 152 VAL B C   1 
ATOM   3740 O O   . VAL B 2 152 ? 35.743  57.927  34.923  1.00 78.64  ? 152 VAL B O   1 
ATOM   3741 C CB  . VAL B 2 152 ? 36.158  59.724  37.648  1.00 84.14  ? 152 VAL B CB  1 
ATOM   3742 C CG1 . VAL B 2 152 ? 36.137  58.255  38.045  1.00 81.57  ? 152 VAL B CG1 1 
ATOM   3743 C CG2 . VAL B 2 152 ? 37.184  60.487  38.466  1.00 87.33  ? 152 VAL B CG2 1 
ATOM   3744 N N   . LYS B 2 153 ? 34.313  59.662  34.988  1.00 90.46  ? 153 LYS B N   1 
ATOM   3745 C CA  . LYS B 2 153 ? 33.280  58.928  34.264  1.00 84.54  ? 153 LYS B CA  1 
ATOM   3746 C C   . LYS B 2 153 ? 33.752  58.528  32.870  1.00 86.00  ? 153 LYS B C   1 
ATOM   3747 O O   . LYS B 2 153 ? 33.706  57.348  32.504  1.00 99.80  ? 153 LYS B O   1 
ATOM   3748 C CB  . LYS B 2 153 ? 32.003  59.762  34.185  1.00 85.24  ? 153 LYS B CB  1 
ATOM   3749 C CG  . LYS B 2 153 ? 31.302  59.931  35.518  1.00 83.61  ? 153 LYS B CG  1 
ATOM   3750 C CD  . LYS B 2 153 ? 30.037  60.752  35.370  1.00 82.77  ? 153 LYS B CD  1 
ATOM   3751 C CE  . LYS B 2 153 ? 29.322  60.899  36.698  1.00 83.30  ? 153 LYS B CE  1 
ATOM   3752 N NZ  . LYS B 2 153 ? 28.126  61.771  36.567  1.00 84.86  ? 153 LYS B NZ  1 
ATOM   3753 N N   . ASN B 2 154 ? 34.214  59.494  32.078  1.00 95.87  ? 154 ASN B N   1 
ATOM   3754 C CA  . ASN B 2 154 ? 34.639  59.210  30.712  1.00 98.31  ? 154 ASN B CA  1 
ATOM   3755 C C   . ASN B 2 154 ? 36.037  58.604  30.632  1.00 99.99  ? 154 ASN B C   1 
ATOM   3756 O O   . ASN B 2 154 ? 36.598  58.527  29.535  1.00 106.26 ? 154 ASN B O   1 
ATOM   3757 C CB  . ASN B 2 154 ? 34.567  60.480  29.857  1.00 106.82 ? 154 ASN B CB  1 
ATOM   3758 C CG  . ASN B 2 154 ? 35.431  61.605  30.395  1.00 127.55 ? 154 ASN B CG  1 
ATOM   3759 O OD1 . ASN B 2 154 ? 36.217  61.418  31.323  1.00 138.87 ? 154 ASN B OD1 1 
ATOM   3760 N ND2 . ASN B 2 154 ? 35.290  62.788  29.806  1.00 138.17 ? 154 ASN B ND2 1 
ATOM   3761 N N   . GLY B 2 155 ? 36.610  58.183  31.757  1.00 78.81  ? 155 GLY B N   1 
ATOM   3762 C CA  . GLY B 2 155 ? 37.893  57.509  31.750  1.00 79.08  ? 155 GLY B CA  1 
ATOM   3763 C C   . GLY B 2 155 ? 39.060  58.387  31.351  1.00 88.55  ? 155 GLY B C   1 
ATOM   3764 O O   . GLY B 2 155 ? 39.893  57.985  30.534  1.00 91.83  ? 155 GLY B O   1 
ATOM   3765 N N   . THR B 2 156 ? 39.139  59.586  31.926  1.00 89.58  ? 156 THR B N   1 
ATOM   3766 C CA  . THR B 2 156 ? 40.231  60.517  31.652  1.00 97.49  ? 156 THR B CA  1 
ATOM   3767 C C   . THR B 2 156 ? 40.719  61.162  32.944  1.00 90.40  ? 156 THR B C   1 
ATOM   3768 O O   . THR B 2 156 ? 41.009  62.362  32.988  1.00 93.34  ? 156 THR B O   1 
ATOM   3769 C CB  . THR B 2 156 ? 39.811  61.590  30.646  1.00 101.62 ? 156 THR B CB  1 
ATOM   3770 O OG1 . THR B 2 156 ? 38.586  62.199  31.073  1.00 102.53 ? 156 THR B OG1 1 
ATOM   3771 C CG2 . THR B 2 156 ? 39.622  60.991  29.256  1.00 96.91  ? 156 THR B CG2 1 
ATOM   3772 N N   . TYR B 2 157 ? 40.821  60.374  34.012  1.00 90.77  ? 157 TYR B N   1 
ATOM   3773 C CA  . TYR B 2 157 ? 41.255  60.906  35.297  1.00 91.54  ? 157 TYR B CA  1 
ATOM   3774 C C   . TYR B 2 157 ? 42.756  61.163  35.294  1.00 99.70  ? 157 TYR B C   1 
ATOM   3775 O O   . TYR B 2 157 ? 43.534  60.409  34.703  1.00 101.39 ? 157 TYR B O   1 
ATOM   3776 C CB  . TYR B 2 157 ? 40.888  59.943  36.428  1.00 89.68  ? 157 TYR B CB  1 
ATOM   3777 C CG  . TYR B 2 157 ? 41.405  60.356  37.792  1.00 100.17 ? 157 TYR B CG  1 
ATOM   3778 C CD1 . TYR B 2 157 ? 40.778  61.358  38.523  1.00 100.76 ? 157 TYR B CD1 1 
ATOM   3779 C CD2 . TYR B 2 157 ? 42.515  59.736  38.353  1.00 110.73 ? 157 TYR B CD2 1 
ATOM   3780 C CE1 . TYR B 2 157 ? 41.247  61.735  39.771  1.00 104.44 ? 157 TYR B CE1 1 
ATOM   3781 C CE2 . TYR B 2 157 ? 42.991  60.107  39.601  1.00 114.58 ? 157 TYR B CE2 1 
ATOM   3782 C CZ  . TYR B 2 157 ? 42.353  61.106  40.305  1.00 112.55 ? 157 TYR B CZ  1 
ATOM   3783 O OH  . TYR B 2 157 ? 42.821  61.478  41.545  1.00 121.66 ? 157 TYR B OH  1 
ATOM   3784 N N   . ASP B 2 158 ? 43.161  62.236  35.968  1.00 109.83 ? 158 ASP B N   1 
ATOM   3785 C CA  . ASP B 2 158 ? 44.558  62.647  36.035  1.00 115.82 ? 158 ASP B CA  1 
ATOM   3786 C C   . ASP B 2 158 ? 45.105  62.279  37.411  1.00 121.16 ? 158 ASP B C   1 
ATOM   3787 O O   . ASP B 2 158 ? 44.711  62.870  38.422  1.00 108.58 ? 158 ASP B O   1 
ATOM   3788 C CB  . ASP B 2 158 ? 44.692  64.144  35.769  1.00 111.14 ? 158 ASP B CB  1 
ATOM   3789 C CG  . ASP B 2 158 ? 46.096  64.542  35.371  1.00 111.12 ? 158 ASP B CG  1 
ATOM   3790 O OD1 . ASP B 2 158 ? 47.059  63.963  35.915  1.00 111.41 ? 158 ASP B OD1 1 
ATOM   3791 O OD2 . ASP B 2 158 ? 46.237  65.431  34.507  1.00 108.76 ? 158 ASP B OD2 1 
ATOM   3792 N N   . TYR B 2 159 ? 46.016  61.310  37.446  1.00 129.51 ? 159 TYR B N   1 
ATOM   3793 C CA  . TYR B 2 159 ? 46.558  60.825  38.710  1.00 129.44 ? 159 TYR B CA  1 
ATOM   3794 C C   . TYR B 2 159 ? 47.575  61.794  39.315  1.00 133.85 ? 159 TYR B C   1 
ATOM   3795 O O   . TYR B 2 159 ? 47.434  62.150  40.492  1.00 146.98 ? 159 TYR B O   1 
ATOM   3796 C CB  . TYR B 2 159 ? 47.170  59.431  38.533  1.00 124.78 ? 159 TYR B CB  1 
ATOM   3797 C CG  . TYR B 2 159 ? 48.028  58.987  39.695  1.00 128.89 ? 159 TYR B CG  1 
ATOM   3798 C CD1 . TYR B 2 159 ? 47.455  58.590  40.896  1.00 125.84 ? 159 TYR B CD1 1 
ATOM   3799 C CD2 . TYR B 2 159 ? 49.412  58.962  39.590  1.00 133.47 ? 159 TYR B CD2 1 
ATOM   3800 C CE1 . TYR B 2 159 ? 48.239  58.183  41.961  1.00 127.39 ? 159 TYR B CE1 1 
ATOM   3801 C CE2 . TYR B 2 159 ? 50.204  58.557  40.650  1.00 132.66 ? 159 TYR B CE2 1 
ATOM   3802 C CZ  . TYR B 2 159 ? 49.612  58.169  41.833  1.00 128.84 ? 159 TYR B CZ  1 
ATOM   3803 O OH  . TYR B 2 159 ? 50.396  57.765  42.889  1.00 127.63 ? 159 TYR B OH  1 
ATOM   3804 N N   . PRO B 2 160 ? 48.606  62.246  38.583  1.00 129.33 ? 160 PRO B N   1 
ATOM   3805 C CA  . PRO B 2 160 ? 49.579  63.159  39.208  1.00 133.57 ? 160 PRO B CA  1 
ATOM   3806 C C   . PRO B 2 160 ? 48.998  64.508  39.595  1.00 129.72 ? 160 PRO B C   1 
ATOM   3807 O O   . PRO B 2 160 ? 49.569  65.178  40.464  1.00 138.58 ? 160 PRO B O   1 
ATOM   3808 C CB  . PRO B 2 160 ? 50.666  63.315  38.133  1.00 134.38 ? 160 PRO B CB  1 
ATOM   3809 C CG  . PRO B 2 160 ? 50.492  62.146  37.235  1.00 133.43 ? 160 PRO B CG  1 
ATOM   3810 C CD  . PRO B 2 160 ? 49.022  61.892  37.213  1.00 122.61 ? 160 PRO B CD  1 
ATOM   3811 N N   . LYS B 2 161 ? 47.886  64.927  38.989  1.00 129.87 ? 161 LYS B N   1 
ATOM   3812 C CA  . LYS B 2 161 ? 47.297  66.224  39.302  1.00 125.13 ? 161 LYS B CA  1 
ATOM   3813 C C   . LYS B 2 161 ? 46.748  66.298  40.723  1.00 124.95 ? 161 LYS B C   1 
ATOM   3814 O O   . LYS B 2 161 ? 46.398  67.393  41.176  1.00 145.98 ? 161 LYS B O   1 
ATOM   3815 C CB  . LYS B 2 161 ? 46.190  66.547  38.295  1.00 117.64 ? 161 LYS B CB  1 
ATOM   3816 C CG  . LYS B 2 161 ? 45.833  68.023  38.204  1.00 117.71 ? 161 LYS B CG  1 
ATOM   3817 C CD  . LYS B 2 161 ? 44.641  68.252  37.291  1.00 113.97 ? 161 LYS B CD  1 
ATOM   3818 C CE  . LYS B 2 161 ? 44.222  69.714  37.291  1.00 125.04 ? 161 LYS B CE  1 
ATOM   3819 N NZ  . LYS B 2 161 ? 43.006  69.943  36.462  1.00 117.55 ? 161 LYS B NZ  1 
ATOM   3820 N N   . TYR B 2 162 ? 46.671  65.173  41.439  1.00 112.44 ? 162 TYR B N   1 
ATOM   3821 C CA  . TYR B 2 162 ? 46.193  65.187  42.816  1.00 112.76 ? 162 TYR B CA  1 
ATOM   3822 C C   . TYR B 2 162 ? 47.055  64.345  43.750  1.00 113.17 ? 162 TYR B C   1 
ATOM   3823 O O   . TYR B 2 162 ? 46.635  64.088  44.887  1.00 112.98 ? 162 TYR B O   1 
ATOM   3824 C CB  . TYR B 2 162 ? 44.742  64.699  42.891  1.00 111.26 ? 162 TYR B CB  1 
ATOM   3825 C CG  . TYR B 2 162 ? 43.777  65.489  42.037  1.00 111.31 ? 162 TYR B CG  1 
ATOM   3826 C CD1 . TYR B 2 162 ? 43.226  66.678  42.496  1.00 111.28 ? 162 TYR B CD1 1 
ATOM   3827 C CD2 . TYR B 2 162 ? 43.411  65.042  40.775  1.00 113.95 ? 162 TYR B CD2 1 
ATOM   3828 C CE1 . TYR B 2 162 ? 42.341  67.402  41.719  1.00 112.86 ? 162 TYR B CE1 1 
ATOM   3829 C CE2 . TYR B 2 162 ? 42.526  65.759  39.990  1.00 110.92 ? 162 TYR B CE2 1 
ATOM   3830 C CZ  . TYR B 2 162 ? 41.994  66.938  40.468  1.00 114.49 ? 162 TYR B CZ  1 
ATOM   3831 O OH  . TYR B 2 162 ? 41.113  67.656  39.691  1.00 108.59 ? 162 TYR B OH  1 
ATOM   3832 N N   . SER B 2 163 ? 48.239  63.907  43.316  1.00 134.10 ? 163 SER B N   1 
ATOM   3833 C CA  . SER B 2 163 ? 49.058  63.040  44.157  1.00 139.65 ? 163 SER B CA  1 
ATOM   3834 C C   . SER B 2 163 ? 49.571  63.778  45.387  1.00 147.55 ? 163 SER B C   1 
ATOM   3835 O O   . SER B 2 163 ? 49.651  63.198  46.476  1.00 159.62 ? 163 SER B O   1 
ATOM   3836 C CB  . SER B 2 163 ? 50.222  62.471  43.347  1.00 141.31 ? 163 SER B CB  1 
ATOM   3837 O OG  . SER B 2 163 ? 51.060  63.508  42.870  1.00 160.42 ? 163 SER B OG  1 
ATOM   3838 N N   . GLU B 2 164 ? 49.929  65.055  45.234  1.00 129.80 ? 164 GLU B N   1 
ATOM   3839 C CA  . GLU B 2 164 ? 50.363  65.844  46.383  1.00 131.79 ? 164 GLU B CA  1 
ATOM   3840 C C   . GLU B 2 164 ? 49.235  65.981  47.398  1.00 123.90 ? 164 GLU B C   1 
ATOM   3841 O O   . GLU B 2 164 ? 49.416  65.710  48.591  1.00 124.94 ? 164 GLU B O   1 
ATOM   3842 C CB  . GLU B 2 164 ? 50.841  67.222  45.923  1.00 143.75 ? 164 GLU B CB  1 
ATOM   3843 C CG  . GLU B 2 164 ? 51.453  67.246  44.530  1.00 147.94 ? 164 GLU B CG  1 
ATOM   3844 C CD  . GLU B 2 164 ? 52.796  66.549  44.465  1.00 146.85 ? 164 GLU B CD  1 
ATOM   3845 O OE1 . GLU B 2 164 ? 53.497  66.505  45.497  1.00 139.68 ? 164 GLU B OE1 1 
ATOM   3846 O OE2 . GLU B 2 164 ? 53.149  66.043  43.379  1.00 146.76 ? 164 GLU B OE2 1 
ATOM   3847 N N   . GLU B 2 165 ? 48.055  66.390  46.929  1.00 122.26 ? 165 GLU B N   1 
ATOM   3848 C CA  . GLU B 2 165 ? 46.909  66.586  47.811  1.00 121.75 ? 165 GLU B CA  1 
ATOM   3849 C C   . GLU B 2 165 ? 46.536  65.294  48.529  1.00 131.57 ? 165 GLU B C   1 
ATOM   3850 O O   . GLU B 2 165 ? 46.317  65.285  49.747  1.00 138.07 ? 165 GLU B O   1 
ATOM   3851 C CB  . GLU B 2 165 ? 45.733  67.115  46.992  1.00 120.19 ? 165 GLU B CB  1 
ATOM   3852 C CG  . GLU B 2 165 ? 44.625  67.764  47.789  1.00 120.84 ? 165 GLU B CG  1 
ATOM   3853 C CD  . GLU B 2 165 ? 43.637  68.480  46.893  1.00 120.10 ? 165 GLU B CD  1 
ATOM   3854 O OE1 . GLU B 2 165 ? 43.938  68.635  45.690  1.00 119.67 ? 165 GLU B OE1 1 
ATOM   3855 O OE2 . GLU B 2 165 ? 42.563  68.885  47.384  1.00 120.10 ? 165 GLU B OE2 1 
ATOM   3856 N N   . SER B 2 166 ? 46.469  64.186  47.786  1.00 118.21 ? 166 SER B N   1 
ATOM   3857 C CA  . SER B 2 166 ? 46.080  62.915  48.388  1.00 113.44 ? 166 SER B CA  1 
ATOM   3858 C C   . SER B 2 166 ? 47.141  62.411  49.359  1.00 120.48 ? 166 SER B C   1 
ATOM   3859 O O   . SER B 2 166 ? 46.810  61.860  50.415  1.00 115.06 ? 166 SER B O   1 
ATOM   3860 C CB  . SER B 2 166 ? 45.810  61.882  47.296  1.00 120.93 ? 166 SER B CB  1 
ATOM   3861 O OG  . SER B 2 166 ? 44.767  62.314  46.438  1.00 109.74 ? 166 SER B OG  1 
ATOM   3862 N N   . LYS B 2 167 ? 48.421  62.590  49.024  1.00 143.91 ? 167 LYS B N   1 
ATOM   3863 C CA  . LYS B 2 167 ? 49.482  62.169  49.933  1.00 148.56 ? 167 LYS B CA  1 
ATOM   3864 C C   . LYS B 2 167 ? 49.492  63.008  51.204  1.00 149.51 ? 167 LYS B C   1 
ATOM   3865 O O   . LYS B 2 167 ? 49.854  62.507  52.275  1.00 150.48 ? 167 LYS B O   1 
ATOM   3866 C CB  . LYS B 2 167 ? 50.838  62.241  49.232  1.00 148.61 ? 167 LYS B CB  1 
ATOM   3867 C CG  . LYS B 2 167 ? 51.951  61.495  49.955  1.00 147.89 ? 167 LYS B CG  1 
ATOM   3868 C CD  . LYS B 2 167 ? 53.196  61.383  49.088  1.00 149.24 ? 167 LYS B CD  1 
ATOM   3869 C CE  . LYS B 2 167 ? 54.253  60.508  49.745  1.00 153.22 ? 167 LYS B CE  1 
ATOM   3870 N NZ  . LYS B 2 167 ? 55.442  60.313  48.868  1.00 154.52 ? 167 LYS B NZ  1 
ATOM   3871 N N   . LEU B 2 168 ? 49.092  64.278  51.111  1.00 150.12 ? 168 LEU B N   1 
ATOM   3872 C CA  . LEU B 2 168 ? 48.970  65.099  52.312  1.00 162.04 ? 168 LEU B CA  1 
ATOM   3873 C C   . LEU B 2 168 ? 47.784  64.654  53.159  1.00 151.71 ? 168 LEU B C   1 
ATOM   3874 O O   . LEU B 2 168 ? 47.893  64.523  54.384  1.00 154.24 ? 168 LEU B O   1 
ATOM   3875 C CB  . LEU B 2 168 ? 48.832  66.574  51.932  1.00 167.52 ? 168 LEU B CB  1 
ATOM   3876 C CG  . LEU B 2 168 ? 50.055  67.261  51.323  1.00 168.34 ? 168 LEU B CG  1 
ATOM   3877 C CD1 . LEU B 2 168 ? 49.739  68.716  51.014  1.00 168.82 ? 168 LEU B CD1 1 
ATOM   3878 C CD2 . LEU B 2 168 ? 51.251  67.154  52.253  1.00 170.64 ? 168 LEU B CD2 1 
ATOM   3879 N N   . ASN B 2 169 ? 46.636  64.414  52.518  1.00 139.35 ? 169 ASN B N   1 
ATOM   3880 C CA  . ASN B 2 169 ? 45.438  64.055  53.272  1.00 133.97 ? 169 ASN B CA  1 
ATOM   3881 C C   . ASN B 2 169 ? 45.539  62.661  53.875  1.00 128.41 ? 169 ASN B C   1 
ATOM   3882 O O   . ASN B 2 169 ? 44.909  62.385  54.904  1.00 125.14 ? 169 ASN B O   1 
ATOM   3883 C CB  . ASN B 2 169 ? 44.203  64.159  52.381  1.00 127.96 ? 169 ASN B CB  1 
ATOM   3884 C CG  . ASN B 2 169 ? 43.863  65.593  52.034  1.00 130.90 ? 169 ASN B CG  1 
ATOM   3885 O OD1 . ASN B 2 169 ? 43.079  66.241  52.727  1.00 133.98 ? 169 ASN B OD1 1 
ATOM   3886 N ND2 . ASN B 2 169 ? 44.453  66.098  50.957  1.00 128.96 ? 169 ASN B ND2 1 
ATOM   3887 N N   . ARG B 2 170 ? 46.318  61.772  53.260  1.00 131.95 ? 170 ARG B N   1 
ATOM   3888 C CA  . ARG B 2 170 ? 46.495  60.445  53.832  1.00 127.79 ? 170 ARG B CA  1 
ATOM   3889 C C   . ARG B 2 170 ? 47.302  60.475  55.120  1.00 134.78 ? 170 ARG B C   1 
ATOM   3890 O O   . ARG B 2 170 ? 47.365  59.451  55.810  1.00 134.78 ? 170 ARG B O   1 
ATOM   3891 C CB  . ARG B 2 170 ? 47.161  59.517  52.815  1.00 124.92 ? 170 ARG B CB  1 
ATOM   3892 C CG  . ARG B 2 170 ? 46.511  58.147  52.724  1.00 122.11 ? 170 ARG B CG  1 
ATOM   3893 C CD  . ARG B 2 170 ? 47.230  57.245  51.738  1.00 116.36 ? 170 ARG B CD  1 
ATOM   3894 N NE  . ARG B 2 170 ? 47.457  57.908  50.458  1.00 118.40 ? 170 ARG B NE  1 
ATOM   3895 C CZ  . ARG B 2 170 ? 48.644  58.008  49.872  1.00 122.83 ? 170 ARG B CZ  1 
ATOM   3896 N NH1 . ARG B 2 170 ? 49.712  57.471  50.443  1.00 124.89 ? 170 ARG B NH1 1 
ATOM   3897 N NH2 . ARG B 2 170 ? 48.760  58.632  48.708  1.00 115.19 ? 170 ARG B NH2 1 
ATOM   3898 N N   . GLU B 2 171 ? 47.907  61.615  55.448  1.00 138.11 ? 171 GLU B N   1 
ATOM   3899 C CA  . GLU B 2 171 ? 48.670  61.827  56.675  1.00 132.89 ? 171 GLU B CA  1 
ATOM   3900 C C   . GLU B 2 171 ? 49.608  60.664  56.984  1.00 136.66 ? 171 GLU B C   1 
ATOM   3901 O O   . GLU B 2 171 ? 50.243  60.115  56.082  1.00 135.94 ? 171 GLU B O   1 
ATOM   3902 C CB  . GLU B 2 171 ? 47.723  62.075  57.856  1.00 129.02 ? 171 GLU B CB  1 
ATOM   3903 C CG  . GLU B 2 171 ? 47.253  60.816  58.568  1.00 131.38 ? 171 GLU B CG  1 
ATOM   3904 C CD  . GLU B 2 171 ? 45.769  60.837  58.872  1.00 132.93 ? 171 GLU B CD  1 
ATOM   3905 O OE1 . GLU B 2 171 ? 45.198  61.942  58.987  1.00 126.17 ? 171 GLU B OE1 1 
ATOM   3906 O OE2 . GLU B 2 171 ? 45.170  59.746  58.987  1.00 124.16 ? 171 GLU B OE2 1 
HETATM 3907 C C1  . NAG C 3 .   ? 0.066   42.482  14.764  1.00 52.49  ? 1   NAG C C1  1 
HETATM 3908 C C2  . NAG C 3 .   ? -0.759  43.379  15.676  1.00 57.67  ? 1   NAG C C2  1 
HETATM 3909 C C3  . NAG C 3 .   ? -0.201  44.800  15.664  1.00 57.42  ? 1   NAG C C3  1 
HETATM 3910 C C4  . NAG C 3 .   ? 1.294   44.794  15.965  1.00 58.38  ? 1   NAG C C4  1 
HETATM 3911 C C5  . NAG C 3 .   ? 2.026   43.786  15.077  1.00 57.94  ? 1   NAG C C5  1 
HETATM 3912 C C6  . NAG C 3 .   ? 3.476   43.599  15.460  1.00 58.09  ? 1   NAG C C6  1 
HETATM 3913 C C7  . NAG C 3 .   ? -2.644  43.745  14.114  1.00 59.43  ? 1   NAG C C7  1 
HETATM 3914 C C8  . NAG C 3 .   ? -4.130  43.651  13.944  1.00 51.74  ? 1   NAG C C8  1 
HETATM 3915 N N2  . NAG C 3 .   ? -2.168  43.368  15.309  1.00 60.56  ? 1   NAG C N2  1 
HETATM 3916 O O3  . NAG C 3 .   ? -0.887  45.587  16.630  1.00 56.43  ? 1   NAG C O3  1 
HETATM 3917 O O4  . NAG C 3 .   ? 1.819   46.092  15.712  1.00 67.04  ? 1   NAG C O4  1 
HETATM 3918 O O5  . NAG C 3 .   ? 1.411   42.494  15.180  1.00 57.95  ? 1   NAG C O5  1 
HETATM 3919 O O6  . NAG C 3 .   ? 3.609   43.372  16.856  1.00 56.58  ? 1   NAG C O6  1 
HETATM 3920 O O7  . NAG C 3 .   ? -1.914  44.148  13.211  1.00 65.97  ? 1   NAG C O7  1 
HETATM 3921 C C1  . NAG C 3 .   ? 2.525   46.599  16.859  1.00 66.29  ? 2   NAG C C1  1 
HETATM 3922 C C2  . NAG C 3 .   ? 3.546   47.610  16.354  1.00 72.79  ? 2   NAG C C2  1 
HETATM 3923 C C3  . NAG C 3 .   ? 4.326   48.204  17.522  1.00 75.81  ? 2   NAG C C3  1 
HETATM 3924 C C4  . NAG C 3 .   ? 3.371   48.768  18.565  1.00 82.60  ? 2   NAG C C4  1 
HETATM 3925 C C5  . NAG C 3 .   ? 2.354   47.706  18.974  1.00 69.84  ? 2   NAG C C5  1 
HETATM 3926 C C6  . NAG C 3 .   ? 1.295   48.229  19.918  1.00 64.79  ? 2   NAG C C6  1 
HETATM 3927 C C7  . NAG C 3 .   ? 4.464   47.315  14.095  1.00 86.44  ? 2   NAG C C7  1 
HETATM 3928 C C8  . NAG C 3 .   ? 5.462   46.583  13.251  1.00 86.49  ? 2   NAG C C8  1 
HETATM 3929 N N2  . NAG C 3 .   ? 4.449   46.996  15.394  1.00 83.40  ? 2   NAG C N2  1 
HETATM 3930 O O3  . NAG C 3 .   ? 5.190   49.227  17.039  1.00 78.49  ? 2   NAG C O3  1 
HETATM 3931 O O4  . NAG C 3 .   ? 4.101   49.184  19.714  1.00 83.19  ? 2   NAG C O4  1 
HETATM 3932 O O5  . NAG C 3 .   ? 1.668   47.217  17.812  1.00 72.98  ? 2   NAG C O5  1 
HETATM 3933 O O6  . NAG C 3 .   ? 0.320   48.997  19.227  1.00 74.46  ? 2   NAG C O6  1 
HETATM 3934 O O7  . NAG C 3 .   ? 3.707   48.157  13.624  1.00 81.30  ? 2   NAG C O7  1 
HETATM 3935 C C1  . BMA C 3 .   ? 4.162   50.626  19.763  1.00 81.78  ? 3   BMA C C1  1 
HETATM 3936 C C2  . BMA C 3 .   ? 4.315   51.045  21.224  1.00 76.39  ? 3   BMA C C2  1 
HETATM 3937 C C3  . BMA C 3 .   ? 4.679   52.542  21.423  1.00 80.30  ? 3   BMA C C3  1 
HETATM 3938 C C4  . BMA C 3 .   ? 5.455   53.183  20.227  1.00 83.44  ? 3   BMA C C4  1 
HETATM 3939 C C5  . BMA C 3 .   ? 5.120   52.560  18.847  1.00 93.91  ? 3   BMA C C5  1 
HETATM 3940 C C6  . BMA C 3 .   ? 6.122   52.962  17.772  1.00 95.66  ? 3   BMA C C6  1 
HETATM 3941 O O2  . BMA C 3 .   ? 5.350   50.301  21.852  1.00 69.07  ? 3   BMA C O2  1 
HETATM 3942 O O3  . BMA C 3 .   ? 5.517   52.674  22.579  1.00 92.79  ? 3   BMA C O3  1 
HETATM 3943 O O4  . BMA C 3 .   ? 5.225   54.590  20.177  1.00 75.55  ? 3   BMA C O4  1 
HETATM 3944 O O5  . BMA C 3 .   ? 5.175   51.144  18.961  1.00 89.39  ? 3   BMA C O5  1 
HETATM 3945 O O6  . BMA C 3 .   ? 7.303   52.189  17.964  1.00 99.50  ? 3   BMA C O6  1 
HETATM 3946 C C1  . MAN C 3 .   ? 4.820   53.102  23.780  1.00 84.80  ? 4   MAN C C1  1 
HETATM 3947 C C2  . MAN C 3 .   ? 4.067   51.882  24.455  1.00 86.69  ? 4   MAN C C2  1 
HETATM 3948 C C3  . MAN C 3 .   ? 2.855   52.324  25.252  1.00 103.59 ? 4   MAN C C3  1 
HETATM 3949 C C4  . MAN C 3 .   ? 3.112   53.709  25.795  1.00 104.07 ? 4   MAN C C4  1 
HETATM 3950 C C5  . MAN C 3 .   ? 3.112   54.697  24.625  1.00 100.16 ? 4   MAN C C5  1 
HETATM 3951 C C6  . MAN C 3 .   ? 3.421   56.121  25.068  1.00 95.19  ? 4   MAN C C6  1 
HETATM 3952 O O2  . MAN C 3 .   ? 4.918   51.210  25.391  1.00 91.29  ? 4   MAN C O2  1 
HETATM 3953 O O3  . MAN C 3 .   ? 2.534   51.401  26.302  1.00 99.32  ? 4   MAN C O3  1 
HETATM 3954 O O4  . MAN C 3 .   ? 2.092   54.068  26.707  1.00 108.64 ? 4   MAN C O4  1 
HETATM 3955 O O5  . MAN C 3 .   ? 4.080   54.301  23.575  1.00 92.62  ? 4   MAN C O5  1 
HETATM 3956 O O6  . MAN C 3 .   ? 3.611   56.912  23.912  1.00 90.53  ? 4   MAN C O6  1 
HETATM 3957 C C1  . NAG D 4 .   ? 6.275   50.432  37.662  1.00 123.08 ? 1   NAG D C1  1 
HETATM 3958 C C2  . NAG D 4 .   ? 4.792   50.174  37.437  1.00 129.92 ? 1   NAG D C2  1 
HETATM 3959 C C3  . NAG D 4 .   ? 4.345   50.798  36.119  1.00 130.30 ? 1   NAG D C3  1 
HETATM 3960 C C4  . NAG D 4 .   ? 4.743   52.268  36.049  1.00 133.86 ? 1   NAG D C4  1 
HETATM 3961 C C5  . NAG D 4 .   ? 6.221   52.456  36.397  1.00 129.12 ? 1   NAG D C5  1 
HETATM 3962 C C6  . NAG D 4 .   ? 6.614   53.909  36.533  1.00 130.94 ? 1   NAG D C6  1 
HETATM 3963 C C7  . NAG D 4 .   ? 3.512   48.210  38.165  1.00 134.39 ? 1   NAG D C7  1 
HETATM 3964 C C8  . NAG D 4 .   ? 3.359   46.722  38.059  1.00 127.45 ? 1   NAG D C8  1 
HETATM 3965 N N2  . NAG D 4 .   ? 4.505   48.749  37.451  1.00 135.05 ? 1   NAG D N2  1 
HETATM 3966 O O3  . NAG D 4 .   ? 2.932   50.676  35.997  1.00 128.92 ? 1   NAG D O3  1 
HETATM 3967 O O4  . NAG D 4 .   ? 4.522   52.745  34.726  1.00 142.29 ? 1   NAG D O4  1 
HETATM 3968 O O5  . NAG D 4 .   ? 6.522   51.830  37.653  1.00 129.32 ? 1   NAG D O5  1 
HETATM 3969 O O6  . NAG D 4 .   ? 8.025   54.076  36.503  1.00 128.93 ? 1   NAG D O6  1 
HETATM 3970 O O7  . NAG D 4 .   ? 2.770   48.892  38.865  1.00 130.79 ? 1   NAG D O7  1 
HETATM 3971 C C1  . NAG D 4 .   ? 3.528   53.787  34.726  1.00 150.80 ? 2   NAG D C1  1 
HETATM 3972 C C2  . NAG D 4 .   ? 3.456   54.414  33.343  1.00 153.02 ? 2   NAG D C2  1 
HETATM 3973 C C3  . NAG D 4 .   ? 2.468   55.576  33.345  1.00 158.16 ? 2   NAG D C3  1 
HETATM 3974 C C4  . NAG D 4 .   ? 1.116   55.136  33.899  1.00 160.00 ? 2   NAG D C4  1 
HETATM 3975 C C5  . NAG D 4 .   ? 1.285   54.405  35.232  1.00 155.34 ? 2   NAG D C5  1 
HETATM 3976 C C6  . NAG D 4 .   ? 0.002   53.784  35.734  1.00 153.34 ? 2   NAG D C6  1 
HETATM 3977 C C7  . NAG D 4 .   ? 5.228   54.631  31.660  1.00 145.23 ? 2   NAG D C7  1 
HETATM 3978 C C8  . NAG D 4 .   ? 6.599   55.161  31.364  1.00 139.09 ? 2   NAG D C8  1 
HETATM 3979 N N2  . NAG D 4 .   ? 4.766   54.857  32.895  1.00 150.50 ? 2   NAG D N2  1 
HETATM 3980 O O3  . NAG D 4 .   ? 2.345   56.048  32.007  1.00 154.13 ? 2   NAG D O3  1 
HETATM 3981 O O4  . NAG D 4 .   ? 0.284   56.266  34.148  1.00 167.53 ? 2   NAG D O4  1 
HETATM 3982 O O5  . NAG D 4 .   ? 2.240   53.340  35.110  1.00 150.10 ? 2   NAG D O5  1 
HETATM 3983 O O6  . NAG D 4 .   ? 0.240   52.922  36.839  1.00 151.23 ? 2   NAG D O6  1 
HETATM 3984 O O7  . NAG D 4 .   ? 4.569   54.026  30.820  1.00 145.78 ? 2   NAG D O7  1 
HETATM 3985 C C1  . BMA D 4 .   ? -0.368  56.756  32.962  1.00 167.50 ? 3   BMA D C1  1 
HETATM 3986 C C2  . BMA D 4 .   ? -1.839  57.101  33.265  1.00 167.99 ? 3   BMA D C2  1 
HETATM 3987 C C3  . BMA D 4 .   ? -2.468  57.853  32.080  1.00 165.02 ? 3   BMA D C3  1 
HETATM 3988 C C4  . BMA D 4 .   ? -1.555  58.983  31.580  1.00 171.13 ? 3   BMA D C4  1 
HETATM 3989 C C5  . BMA D 4 .   ? -0.183  58.403  31.235  1.00 169.93 ? 3   BMA D C5  1 
HETATM 3990 C C6  . BMA D 4 .   ? 0.795   59.447  30.720  1.00 168.19 ? 3   BMA D C6  1 
HETATM 3991 O O2  . BMA D 4 .   ? -1.933  57.956  34.394  1.00 169.51 ? 3   BMA D O2  1 
HETATM 3992 O O3  . BMA D 4 .   ? -3.753  58.371  32.403  1.00 159.80 ? 3   BMA D O3  1 
HETATM 3993 O O4  . BMA D 4 .   ? -2.116  59.591  30.431  1.00 170.92 ? 3   BMA D O4  1 
HETATM 3994 O O5  . BMA D 4 .   ? 0.357   57.850  32.434  1.00 170.07 ? 3   BMA D O5  1 
HETATM 3995 O O6  . BMA D 4 .   ? 1.257   60.213  31.827  1.00 167.52 ? 3   BMA D O6  1 
HETATM 3996 C C1  . NAG E 5 .   ? -26.654 16.672  3.164   1.00 69.78  ? 1   NAG E C1  1 
HETATM 3997 C C2  . NAG E 5 .   ? -27.540 15.522  2.675   1.00 76.89  ? 1   NAG E C2  1 
HETATM 3998 C C3  . NAG E 5 .   ? -28.900 15.561  3.364   1.00 86.65  ? 1   NAG E C3  1 
HETATM 3999 C C4  . NAG E 5 .   ? -28.722 15.571  4.875   1.00 87.76  ? 1   NAG E C4  1 
HETATM 4000 C C5  . NAG E 5 .   ? -27.839 16.748  5.274   1.00 78.24  ? 1   NAG E C5  1 
HETATM 4001 C C6  . NAG E 5 .   ? -27.543 16.789  6.754   1.00 79.60  ? 1   NAG E C6  1 
HETATM 4002 C C7  . NAG E 5 .   ? -26.856 14.964  0.384   1.00 84.98  ? 1   NAG E C7  1 
HETATM 4003 C C8  . NAG E 5 .   ? -27.174 15.107  -1.073  1.00 90.30  ? 1   NAG E C8  1 
HETATM 4004 N N2  . NAG E 5 .   ? -27.700 15.563  1.230   1.00 83.64  ? 1   NAG E N2  1 
HETATM 4005 O O3  . NAG E 5 .   ? -29.660 14.426  2.967   1.00 100.66 ? 1   NAG E O3  1 
HETATM 4006 O O4  . NAG E 5 .   ? -29.984 15.665  5.527   1.00 108.35 ? 1   NAG E O4  1 
HETATM 4007 O O5  . NAG E 5 .   ? -26.575 16.648  4.601   1.00 69.57  ? 1   NAG E O5  1 
HETATM 4008 O O6  . NAG E 5 .   ? -26.512 17.721  7.051   1.00 90.03  ? 1   NAG E O6  1 
HETATM 4009 O O7  . NAG E 5 .   ? -25.877 14.339  0.778   1.00 84.97  ? 1   NAG E O7  1 
HETATM 4010 C C1  . NAG E 5 .   ? -30.303 14.374  6.082   1.00 117.02 ? 2   NAG E C1  1 
HETATM 4011 C C2  . NAG E 5 .   ? -31.304 14.524  7.225   1.00 119.35 ? 2   NAG E C2  1 
HETATM 4012 C C3  . NAG E 5 .   ? -31.643 13.157  7.812   1.00 124.04 ? 2   NAG E C3  1 
HETATM 4013 C C4  . NAG E 5 .   ? -32.108 12.207  6.716   1.00 130.61 ? 2   NAG E C4  1 
HETATM 4014 C C5  . NAG E 5 .   ? -31.078 12.155  5.591   1.00 126.33 ? 2   NAG E C5  1 
HETATM 4015 C C6  . NAG E 5 .   ? -31.533 11.328  4.411   1.00 132.34 ? 2   NAG E C6  1 
HETATM 4016 C C7  . NAG E 5 .   ? -30.936 16.738  8.220   1.00 111.28 ? 2   NAG E C7  1 
HETATM 4017 C C8  . NAG E 5 .   ? -30.344 17.497  9.368   1.00 100.68 ? 2   NAG E C8  1 
HETATM 4018 N N2  . NAG E 5 .   ? -30.790 15.409  8.258   1.00 117.18 ? 2   NAG E N2  1 
HETATM 4019 O O3  . NAG E 5 .   ? -32.661 13.301  8.795   1.00 127.62 ? 2   NAG E O3  1 
HETATM 4020 O O4  . NAG E 5 .   ? -32.288 10.901  7.251   1.00 133.85 ? 2   NAG E O4  1 
HETATM 4021 O O5  . NAG E 5 .   ? -30.829 13.479  5.097   1.00 126.25 ? 2   NAG E O5  1 
HETATM 4022 O O6  . NAG E 5 .   ? -31.425 9.936   4.678   1.00 134.34 ? 2   NAG E O6  1 
HETATM 4023 O O7  . NAG E 5 .   ? -31.519 17.301  7.299   1.00 106.80 ? 2   NAG E O7  1 
HETATM 4024 C C1  . NAG F 5 .   ? 8.247   33.835  42.038  1.00 87.23  ? 1   NAG F C1  1 
HETATM 4025 C C2  . NAG F 5 .   ? 7.008   33.030  42.405  1.00 97.57  ? 1   NAG F C2  1 
HETATM 4026 C C3  . NAG F 5 .   ? 5.826   33.963  42.643  1.00 96.60  ? 1   NAG F C3  1 
HETATM 4027 C C4  . NAG F 5 .   ? 6.185   35.020  43.680  1.00 102.13 ? 1   NAG F C4  1 
HETATM 4028 C C5  . NAG F 5 .   ? 7.477   35.736  43.286  1.00 98.37  ? 1   NAG F C5  1 
HETATM 4029 C C6  . NAG F 5 .   ? 7.970   36.697  44.344  1.00 100.10 ? 1   NAG F C6  1 
HETATM 4030 C C7  . NAG F 5 .   ? 6.583   30.746  41.617  1.00 92.58  ? 1   NAG F C7  1 
HETATM 4031 C C8  . NAG F 5 .   ? 6.255   29.883  40.436  1.00 73.44  ? 1   NAG F C8  1 
HETATM 4032 N N2  . NAG F 5 .   ? 6.693   32.056  41.373  1.00 94.61  ? 1   NAG F N2  1 
HETATM 4033 O O3  . NAG F 5 .   ? 4.707   33.201  43.084  1.00 82.55  ? 1   NAG F O3  1 
HETATM 4034 O O4  . NAG F 5 .   ? 5.135   35.975  43.778  1.00 122.66 ? 1   NAG F O4  1 
HETATM 4035 O O5  . NAG F 5 .   ? 8.528   34.781  43.072  1.00 93.31  ? 1   NAG F O5  1 
HETATM 4036 O O6  . NAG F 5 .   ? 9.386   36.811  44.328  1.00 100.33 ? 1   NAG F O6  1 
HETATM 4037 O O7  . NAG F 5 .   ? 6.737   30.279  42.742  1.00 104.10 ? 1   NAG F O7  1 
HETATM 4038 C C1  . NAG F 5 .   ? 4.438   35.807  45.027  1.00 143.40 ? 2   NAG F C1  1 
HETATM 4039 C C2  . NAG F 5 .   ? 3.302   36.820  45.107  1.00 149.06 ? 2   NAG F C2  1 
HETATM 4040 C C3  . NAG F 5 .   ? 2.560   36.673  46.430  1.00 152.49 ? 2   NAG F C3  1 
HETATM 4041 C C4  . NAG F 5 .   ? 2.094   35.235  46.617  1.00 156.90 ? 2   NAG F C4  1 
HETATM 4042 C C5  . NAG F 5 .   ? 3.267   34.269  46.458  1.00 153.56 ? 2   NAG F C5  1 
HETATM 4043 C C6  . NAG F 5 .   ? 2.844   32.818  46.487  1.00 148.19 ? 2   NAG F C6  1 
HETATM 4044 C C7  . NAG F 5 .   ? 3.179   39.090  44.184  1.00 154.88 ? 2   NAG F C7  1 
HETATM 4045 C C8  . NAG F 5 .   ? 3.823   40.442  44.127  1.00 156.89 ? 2   NAG F C8  1 
HETATM 4046 N N2  . NAG F 5 .   ? 3.795   38.178  44.944  1.00 152.21 ? 2   NAG F N2  1 
HETATM 4047 O O3  . NAG F 5 .   ? 1.443   37.554  46.446  1.00 150.35 ? 2   NAG F O3  1 
HETATM 4048 O O4  . NAG F 5 .   ? 1.526   35.074  47.912  1.00 159.68 ? 2   NAG F O4  1 
HETATM 4049 O O5  . NAG F 5 .   ? 3.916   34.485  45.196  1.00 150.16 ? 2   NAG F O5  1 
HETATM 4050 O O6  . NAG F 5 .   ? 3.785   32.014  47.186  1.00 144.46 ? 2   NAG F O6  1 
HETATM 4051 O O7  . NAG F 5 .   ? 2.147   38.835  43.570  1.00 153.97 ? 2   NAG F O7  1 
HETATM 4052 C C1  . NAG G 6 .   ? -24.892 23.442  6.927   1.00 132.86 ? 412 NAG A C1  1 
HETATM 4053 C C2  . NAG G 6 .   ? -26.271 23.838  6.406   1.00 146.60 ? 412 NAG A C2  1 
HETATM 4054 C C3  . NAG G 6 .   ? -26.883 24.915  7.298   1.00 154.70 ? 412 NAG A C3  1 
HETATM 4055 C C4  . NAG G 6 .   ? -26.881 24.467  8.754   1.00 152.89 ? 412 NAG A C4  1 
HETATM 4056 C C5  . NAG G 6 .   ? -25.481 24.029  9.174   1.00 146.75 ? 412 NAG A C5  1 
HETATM 4057 C C6  . NAG G 6 .   ? -25.437 23.446  10.567  1.00 150.44 ? 412 NAG A C6  1 
HETATM 4058 C C7  . NAG G 6 .   ? -26.298 23.472  3.978   1.00 153.57 ? 412 NAG A C7  1 
HETATM 4059 C C8  . NAG G 6 .   ? -26.202 24.115  2.627   1.00 156.10 ? 412 NAG A C8  1 
HETATM 4060 N N2  . NAG G 6 .   ? -26.199 24.296  5.027   1.00 151.49 ? 412 NAG A N2  1 
HETATM 4061 O O3  . NAG G 6 .   ? -28.215 25.181  6.875   1.00 158.61 ? 412 NAG A O3  1 
HETATM 4062 O O4  . NAG G 6 .   ? -27.306 25.536  9.591   1.00 154.33 ? 412 NAG A O4  1 
HETATM 4063 O O5  . NAG G 6 .   ? -24.997 23.012  8.284   1.00 134.40 ? 412 NAG A O5  1 
HETATM 4064 O O6  . NAG G 6 .   ? -24.590 24.204  11.420  1.00 150.47 ? 412 NAG A O6  1 
HETATM 4065 O O7  . NAG G 6 .   ? -26.454 22.263  4.114   1.00 152.56 ? 412 NAG A O7  1 
HETATM 4066 C C2  . EZ7 H 7 .   ? 15.330  41.053  18.622  1.00 39.08  ? 201 EZ7 B C2  1 
HETATM 4067 C C3  . EZ7 H 7 .   ? 14.049  41.132  19.140  1.00 46.42  ? 201 EZ7 B C3  1 
HETATM 4068 C C4  . EZ7 H 7 .   ? 13.884  41.748  20.380  1.00 42.85  ? 201 EZ7 B C4  1 
HETATM 4069 C C11 . EZ7 H 7 .   ? 14.940  42.233  21.038  1.00 45.62  ? 201 EZ7 B C11 1 
HETATM 4070 C C12 . EZ7 H 7 .   ? 16.168  42.144  20.521  1.00 43.00  ? 201 EZ7 B C12 1 
HETATM 4071 C C16 . EZ7 H 7 .   ? 18.321  43.708  23.451  1.00 45.25  ? 201 EZ7 B C16 1 
HETATM 4072 C C18 . EZ7 H 7 .   ? 16.217  44.382  24.402  1.00 42.69  ? 201 EZ7 B C18 1 
HETATM 4073 C C19 . EZ7 H 7 .   ? 16.896  45.022  25.446  1.00 42.79  ? 201 EZ7 B C19 1 
HETATM 4074 C C60 . EZ7 H 7 .   ? 10.918  39.769  17.742  1.00 35.75  ? 201 EZ7 B C60 1 
HETATM 4075 C C58 . EZ7 H 7 .   ? 11.818  40.384  18.811  1.00 41.15  ? 201 EZ7 B C58 1 
HETATM 4076 O O59 . EZ7 H 7 .   ? 11.371  40.622  19.932  1.00 52.09  ? 201 EZ7 B O59 1 
HETATM 4077 N N7  . EZ7 H 7 .   ? 13.075  40.608  18.380  1.00 46.04  ? 201 EZ7 B N7  1 
HETATM 4078 C C1  . EZ7 H 7 .   ? 16.387  41.574  19.345  1.00 38.68  ? 201 EZ7 B C1  1 
HETATM 4079 O O13 . EZ7 H 7 .   ? 17.019  42.696  21.364  1.00 45.83  ? 201 EZ7 B O13 1 
HETATM 4080 N N10 . EZ7 H 7 .   ? 15.060  42.854  22.213  1.00 49.95  ? 201 EZ7 B N10 1 
HETATM 4081 C C9  . EZ7 H 7 .   ? 16.353  43.120  22.370  1.00 46.91  ? 201 EZ7 B C9  1 
HETATM 4082 C C17 . EZ7 H 7 .   ? 16.934  43.730  23.399  1.00 43.14  ? 201 EZ7 B C17 1 
HETATM 4083 C C15 . EZ7 H 7 .   ? 18.977  44.332  24.502  1.00 42.03  ? 201 EZ7 B C15 1 
HETATM 4084 N N14 . EZ7 H 7 .   ? 18.238  44.971  25.495  1.00 43.87  ? 201 EZ7 B N14 1 
HETATM 4085 C C23 . EZ7 H 7 .   ? 16.211  45.664  26.485  1.00 44.93  ? 201 EZ7 B C23 1 
HETATM 4086 O O24 . EZ7 H 7 .   ? 15.454  44.980  27.169  1.00 46.09  ? 201 EZ7 B O24 1 
HETATM 4087 N N27 . EZ7 H 7 .   ? 16.452  46.961  26.792  1.00 45.77  ? 201 EZ7 B N27 1 
HETATM 4088 C C28 . EZ7 H 7 .   ? 15.756  47.594  27.932  1.00 47.04  ? 201 EZ7 B C28 1 
HETATM 4089 C C29 . EZ7 H 7 .   ? 16.725  48.460  28.743  1.00 48.69  ? 201 EZ7 B C29 1 
HETATM 4090 C C26 . EZ7 H 7 .   ? 17.364  47.828  26.007  1.00 50.75  ? 201 EZ7 B C26 1 
HETATM 4091 C C25 . EZ7 H 7 .   ? 18.213  48.727  26.909  1.00 52.06  ? 201 EZ7 B C25 1 
HETATM 4092 N N30 . EZ7 H 7 .   ? 17.421  49.459  27.912  1.00 54.08  ? 201 EZ7 B N30 1 
HETATM 4093 C C40 . EZ7 H 7 .   ? 18.329  50.279  28.750  1.00 56.55  ? 201 EZ7 B C40 1 
HETATM 4094 C C52 . EZ7 H 7 .   ? 18.966  51.433  27.980  1.00 59.42  ? 201 EZ7 B C52 1 
HETATM 4095 N N56 . EZ7 H 7 .   ? 18.497  52.023  26.906  1.00 58.42  ? 201 EZ7 B N56 1 
HETATM 4096 N N53 . EZ7 H 7 .   ? 20.096  52.031  28.288  1.00 64.32  ? 201 EZ7 B N53 1 
HETATM 4097 N N54 . EZ7 H 7 .   ? 20.236  52.815  27.514  1.00 58.96  ? 201 EZ7 B N54 1 
HETATM 4098 N N55 . EZ7 H 7 .   ? 19.283  52.825  26.673  1.00 61.85  ? 201 EZ7 B N55 1 
HETATM 4099 C C57 . EZ7 H 7 .   ? 19.246  53.773  25.555  1.00 60.23  ? 201 EZ7 B C57 1 
HETATM 4100 C C44 . EZ7 H 7 .   ? 17.703  50.800  29.881  1.00 65.92  ? 201 EZ7 B C44 1 
HETATM 4101 C C43 . EZ7 H 7 .   ? 18.176  50.432  31.134  1.00 65.47  ? 201 EZ7 B C43 1 
HETATM 4102 C C42 . EZ7 H 7 .   ? 17.569  50.933  32.276  1.00 71.37  ? 201 EZ7 B C42 1 
HETATM 4103 C C41 . EZ7 H 7 .   ? 16.495  51.809  32.168  1.00 74.97  ? 201 EZ7 B C41 1 
HETATM 4104 C C46 . EZ7 H 7 .   ? 16.023  52.187  30.916  1.00 77.20  ? 201 EZ7 B C46 1 
HETATM 4105 C C45 . EZ7 H 7 .   ? 16.631  51.685  29.770  1.00 75.16  ? 201 EZ7 B C45 1 
HETATM 4106 O O   . HOH I 8 .   ? -10.224 25.387  -18.619 1.00 100.08 ? 501 HOH A O   1 
HETATM 4107 O O   . HOH I 8 .   ? -4.055  4.786   -1.294  1.00 40.02  ? 502 HOH A O   1 
HETATM 4108 O O   . HOH I 8 .   ? -11.416 31.919  -6.038  1.00 58.66  ? 503 HOH A O   1 
HETATM 4109 O O   . HOH I 8 .   ? -25.821 20.516  -8.942  1.00 79.64  ? 504 HOH A O   1 
HETATM 4110 O O   . HOH I 8 .   ? 19.150  35.859  28.195  1.00 41.02  ? 505 HOH A O   1 
HETATM 4111 O O   . HOH I 8 .   ? 2.869   36.415  11.793  1.00 42.78  ? 506 HOH A O   1 
HETATM 4112 O O   . HOH I 8 .   ? 6.181   24.315  13.655  1.00 31.10  ? 507 HOH A O   1 
HETATM 4113 O O   . HOH I 8 .   ? -5.469  6.744   -0.242  1.00 39.28  ? 508 HOH A O   1 
HETATM 4114 O O   . HOH I 8 .   ? -14.447 5.358   0.640   1.00 51.88  ? 509 HOH A O   1 
HETATM 4115 O O   . HOH I 8 .   ? -2.380  29.404  22.861  1.00 35.83  ? 510 HOH A O   1 
HETATM 4116 O O   . HOH I 8 .   ? -4.318  12.861  2.777   1.00 42.42  ? 511 HOH A O   1 
HETATM 4117 O O   . HOH I 8 .   ? -1.210  36.554  16.838  1.00 60.78  ? 512 HOH A O   1 
HETATM 4118 O O   . HOH I 8 .   ? 10.267  26.744  29.671  1.00 41.10  ? 513 HOH A O   1 
HETATM 4119 O O   . HOH I 8 .   ? -10.868 5.659   1.846   1.00 62.54  ? 514 HOH A O   1 
HETATM 4120 O O   . HOH I 8 .   ? -0.834  40.187  5.813   1.00 46.49  ? 515 HOH A O   1 
HETATM 4121 O O   . HOH I 8 .   ? -15.374 29.574  0.376   1.00 63.15  ? 516 HOH A O   1 
HETATM 4122 O O   . HOH I 8 .   ? -31.261 5.920   -11.885 1.00 89.40  ? 517 HOH A O   1 
HETATM 4123 O O   . HOH I 8 .   ? 7.612   34.523  12.679  1.00 51.27  ? 518 HOH A O   1 
HETATM 4124 O O   . HOH I 8 .   ? 11.832  31.136  31.005  1.00 51.20  ? 519 HOH A O   1 
HETATM 4125 O O   . HOH I 8 .   ? 0.426   46.500  12.583  1.00 51.21  ? 520 HOH A O   1 
HETATM 4126 O O   . HOH I 8 .   ? -3.020  8.480   -11.293 1.00 52.60  ? 521 HOH A O   1 
HETATM 4127 O O   . HOH I 8 .   ? -27.525 20.282  -16.786 1.00 90.86  ? 522 HOH A O   1 
HETATM 4128 O O   . HOH I 8 .   ? -8.090  2.158   -1.754  1.00 56.01  ? 523 HOH A O   1 
HETATM 4129 O O   . HOH I 8 .   ? 7.274   25.470  30.341  1.00 56.37  ? 524 HOH A O   1 
HETATM 4130 O O   . HOH I 8 .   ? -22.032 24.393  2.111   1.00 61.26  ? 525 HOH A O   1 
HETATM 4131 O O   . HOH I 8 .   ? 3.702   32.914  26.723  1.00 43.51  ? 526 HOH A O   1 
HETATM 4132 O O   . HOH I 8 .   ? -16.257 37.019  5.649   1.00 64.42  ? 527 HOH A O   1 
HETATM 4133 O O   . HOH I 8 .   ? -15.593 9.544   1.370   1.00 48.43  ? 528 HOH A O   1 
HETATM 4134 O O   . HOH J 8 .   ? -3.891  5.854   15.161  1.00 47.75  ? 301 HOH B O   1 
HETATM 4135 O O   . HOH J 8 .   ? 12.256  32.978  13.220  1.00 69.95  ? 302 HOH B O   1 
HETATM 4136 O O   . HOH J 8 .   ? -5.957  4.375   10.372  1.00 44.94  ? 303 HOH B O   1 
HETATM 4137 O O   . HOH J 8 .   ? 1.179   15.422  9.520   1.00 27.69  ? 304 HOH B O   1 
HETATM 4138 O O   . HOH J 8 .   ? 34.562  54.739  32.563  1.00 71.23  ? 305 HOH B O   1 
HETATM 4139 O O   . HOH J 8 .   ? -1.909  13.853  10.407  1.00 48.67  ? 306 HOH B O   1 
HETATM 4140 O O   . HOH J 8 .   ? 21.398  31.859  38.263  1.00 41.09  ? 307 HOH B O   1 
HETATM 4141 O O   . HOH J 8 .   ? -6.491  9.258   9.306   1.00 49.24  ? 308 HOH B O   1 
HETATM 4142 O O   . HOH J 8 .   ? 0.184   1.183   7.283   1.00 35.75  ? 309 HOH B O   1 
HETATM 4143 O O   . HOH J 8 .   ? 0.506   16.845  4.653   1.00 54.46  ? 310 HOH B O   1 
HETATM 4144 O O   . HOH J 8 .   ? 3.192   7.182   17.224  1.00 41.66  ? 311 HOH B O   1 
HETATM 4145 O O   . HOH J 8 .   ? 13.423  27.430  29.943  1.00 48.04  ? 312 HOH B O   1 
HETATM 4146 O O   . HOH J 8 .   ? 7.922   10.466  18.689  1.00 33.97  ? 313 HOH B O   1 
HETATM 4147 O O   . HOH J 8 .   ? 22.127  60.905  34.374  1.00 84.55  ? 314 HOH B O   1 
HETATM 4148 O O   . HOH J 8 .   ? 23.399  55.723  46.683  1.00 77.15  ? 315 HOH B O   1 
HETATM 4149 O O   . HOH J 8 .   ? -10.111 11.074  5.148   1.00 51.96  ? 316 HOH B O   1 
HETATM 4150 O O   . HOH J 8 .   ? -1.110  11.106  11.625  1.00 52.23  ? 317 HOH B O   1 
HETATM 4151 O O   . HOH J 8 .   ? 24.152  44.257  17.452  1.00 44.64  ? 318 HOH B O   1 
HETATM 4152 O O   . HOH J 8 .   ? 4.078   9.291   18.750  1.00 45.69  ? 319 HOH B O   1 
HETATM 4153 O O   . HOH J 8 .   ? -9.431  0.664   2.624   1.00 69.11  ? 320 HOH B O   1 
HETATM 4154 O O   . HOH J 8 .   ? -11.062 2.969   4.308   1.00 66.02  ? 321 HOH B O   1 
HETATM 4155 O O   . HOH J 8 .   ? 17.426  55.606  28.528  1.00 68.04  ? 322 HOH B O   1 
HETATM 4156 O O   . HOH J 8 .   ? 1.012   16.733  16.113  1.00 44.84  ? 323 HOH B O   1 
HETATM 4157 O O   . HOH J 8 .   ? 36.155  43.755  45.999  1.00 77.35  ? 324 HOH B O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . ASP A 1   ? 1.6008 1.0574 1.5831 -0.2379 -0.2797 -0.5540 11  ASP A N   
2    C CA  . ASP A 1   ? 1.6190 1.0773 1.6270 -0.2394 -0.2698 -0.5296 11  ASP A CA  
3    C C   . ASP A 1   ? 1.5803 1.0793 1.5889 -0.2347 -0.2677 -0.5151 11  ASP A C   
4    O O   . ASP A 1   ? 1.6204 1.1493 1.6327 -0.2439 -0.2786 -0.5157 11  ASP A O   
5    C CB  . ASP A 1   ? 1.6412 1.0878 1.6824 -0.2627 -0.2747 -0.5201 11  ASP A CB  
6    C CG  . ASP A 1   ? 1.7148 1.1151 1.7581 -0.2662 -0.2740 -0.5292 11  ASP A CG  
7    O OD1 . ASP A 1   ? 1.7570 1.1384 1.7763 -0.2533 -0.2742 -0.5486 11  ASP A OD1 
8    O OD2 . ASP A 1   ? 1.7423 1.1249 1.8104 -0.2821 -0.2730 -0.5169 11  ASP A OD2 
9    N N   . THR A 2   ? 1.4551 0.9551 1.4611 -0.2200 -0.2542 -0.5024 12  THR A N   
10   C CA  . THR A 2   ? 1.3477 0.8829 1.3519 -0.2132 -0.2509 -0.4892 12  THR A CA  
11   C C   . THR A 2   ? 1.2617 0.7925 1.2847 -0.2093 -0.2378 -0.4678 12  THR A C   
12   O O   . THR A 2   ? 1.2933 0.7932 1.3188 -0.2035 -0.2292 -0.4658 12  THR A O   
13   C CB  . THR A 2   ? 1.3478 0.8948 1.3145 -0.1946 -0.2480 -0.5006 12  THR A CB  
14   O OG1 . THR A 2   ? 1.3206 0.8384 1.2709 -0.1804 -0.2379 -0.5108 12  THR A OG1 
15   C CG2 . THR A 2   ? 1.4907 1.0524 1.4376 -0.1998 -0.2626 -0.5173 12  THR A CG2 
16   N N   . ILE A 3   ? 1.2138 0.7757 1.2498 -0.2120 -0.2369 -0.4520 13  ILE A N   
17   C CA  . ILE A 3   ? 1.1736 0.7372 1.2234 -0.2068 -0.2245 -0.4317 13  ILE A CA  
18   C C   . ILE A 3   ? 1.1330 0.7300 1.1701 -0.1949 -0.2221 -0.4267 13  ILE A C   
19   O O   . ILE A 3   ? 1.1275 0.7524 1.1598 -0.1984 -0.2323 -0.4311 13  ILE A O   
20   C CB  . ILE A 3   ? 1.1614 0.7265 1.2466 -0.2267 -0.2244 -0.4142 13  ILE A CB  
21   C CG1 . ILE A 3   ? 1.1314 0.6876 1.2273 -0.2212 -0.2107 -0.3942 13  ILE A CG1 
22   C CG2 . ILE A 3   ? 1.1378 0.7430 1.2389 -0.2385 -0.2331 -0.4098 13  ILE A CG2 
23   C CD1 . ILE A 3   ? 1.1222 0.6791 1.2492 -0.2413 -0.2085 -0.3758 13  ILE A CD1 
24   N N   . CYS A 4   ? 1.1073 0.7007 1.1382 -0.1803 -0.2094 -0.4177 14  CYS A N   
25   C CA  . CYS A 4   ? 1.2003 0.8213 1.2166 -0.1680 -0.2057 -0.4130 14  CYS A CA  
26   C C   . CYS A 4   ? 1.0290 0.6568 1.0658 -0.1671 -0.1957 -0.3919 14  CYS A C   
27   O O   . CYS A 4   ? 1.0304 0.6359 1.0844 -0.1708 -0.1890 -0.3820 14  CYS A O   
28   C CB  . CYS A 4   ? 1.2223 0.8353 1.2036 -0.1490 -0.1988 -0.4260 14  CYS A CB  
29   S SG  . CYS A 4   ? 1.3576 0.9673 1.3070 -0.1485 -0.2093 -0.4513 14  CYS A SG  
30   N N   . ILE A 5   ? 0.9936 0.6516 1.0271 -0.1623 -0.1955 -0.3847 15  ILE A N   
31   C CA  . ILE A 5   ? 0.9518 0.6196 1.0003 -0.1591 -0.1857 -0.3663 15  ILE A CA  
32   C C   . ILE A 5   ? 0.9356 0.6113 0.9567 -0.1401 -0.1781 -0.3685 15  ILE A C   
33   O O   . ILE A 5   ? 0.9369 0.6315 0.9355 -0.1348 -0.1841 -0.3764 15  ILE A O   
34   C CB  . ILE A 5   ? 0.9400 0.6391 1.0139 -0.1717 -0.1915 -0.3548 15  ILE A CB  
35   C CG1 . ILE A 5   ? 0.9335 0.6244 1.0392 -0.1918 -0.1934 -0.3478 15  ILE A CG1 
36   C CG2 . ILE A 5   ? 0.8794 0.5946 0.9592 -0.1643 -0.1821 -0.3397 15  ILE A CG2 
37   C CD1 . ILE A 5   ? 0.9697 0.6587 1.0768 -0.2036 -0.2063 -0.3616 15  ILE A CD1 
38   N N   . GLY A 6   ? 0.9234 0.5842 0.9454 -0.1301 -0.1652 -0.3612 16  GLY A N   
39   C CA  . GLY A 6   ? 0.9257 0.5942 0.9240 -0.1128 -0.1561 -0.3629 16  GLY A CA  
40   C C   . GLY A 6   ? 0.9429 0.6117 0.9529 -0.1063 -0.1418 -0.3422 16  GLY A C   
41   O O   . GLY A 6   ? 0.8957 0.5619 0.9316 -0.1164 -0.1404 -0.3261 16  GLY A O   
42   N N   . TYR A 7   ? 0.8725 0.5459 0.8624 -0.0902 -0.1299 -0.3406 17  TYR A N   
43   C CA  . TYR A 7   ? 0.8359 0.5141 0.8342 -0.0831 -0.1162 -0.3192 17  TYR A CA  
44   C C   . TYR A 7   ? 0.8457 0.5097 0.8320 -0.0668 -0.1055 -0.3271 17  TYR A C   
45   O O   . TYR A 7   ? 0.8723 0.5297 0.8394 -0.0597 -0.1065 -0.3486 17  TYR A O   
46   C CB  . TYR A 7   ? 0.8002 0.5119 0.7914 -0.0816 -0.1118 -0.3021 17  TYR A CB  
47   C CG  . TYR A 7   ? 0.8061 0.5350 0.7665 -0.0750 -0.1140 -0.3121 17  TYR A CG  
48   C CD1 . TYR A 7   ? 0.8050 0.5374 0.7422 -0.0613 -0.1025 -0.3145 17  TYR A CD1 
49   C CD2 . TYR A 7   ? 0.8146 0.5570 0.7691 -0.0832 -0.1279 -0.3186 17  TYR A CD2 
50   C CE1 . TYR A 7   ? 0.8145 0.5611 0.7202 -0.0571 -0.1038 -0.3221 17  TYR A CE1 
51   C CE2 . TYR A 7   ? 0.8245 0.5801 0.7471 -0.0776 -0.1312 -0.3262 17  TYR A CE2 
52   C CZ  . TYR A 7   ? 0.8253 0.5821 0.7221 -0.0651 -0.1186 -0.3273 17  TYR A CZ  
53   O OH  . TYR A 7   ? 1.0759 0.8442 0.9378 -0.0611 -0.1211 -0.3334 17  TYR A OH  
54   N N   . HIS A 8   ? 0.8338 0.4952 0.8323 -0.0610 -0.0954 -0.3099 18  HIS A N   
55   C CA  . HIS A 8   ? 0.8328 0.4795 0.8295 -0.0459 -0.0864 -0.3154 18  HIS A CA  
56   C C   . HIS A 8   ? 0.8244 0.4927 0.7967 -0.0328 -0.0759 -0.3213 18  HIS A C   
57   O O   . HIS A 8   ? 0.8031 0.4976 0.7616 -0.0347 -0.0734 -0.3123 18  HIS A O   
58   C CB  . HIS A 8   ? 0.8126 0.4521 0.8294 -0.0446 -0.0806 -0.2932 18  HIS A CB  
59   C CG  . HIS A 8   ? 0.8549 0.4819 0.8736 -0.0281 -0.0726 -0.2970 18  HIS A CG  
60   N ND1 . HIS A 8   ? 0.8506 0.4440 0.8808 -0.0235 -0.0774 -0.3085 18  HIS A ND1 
61   C CD2 . HIS A 8   ? 0.7980 0.4423 0.8109 -0.0150 -0.0609 -0.2913 18  HIS A CD2 
62   C CE1 . HIS A 8   ? 0.8579 0.4498 0.8903 -0.0071 -0.0693 -0.3102 18  HIS A CE1 
63   N NE2 . HIS A 8   ? 0.8282 0.4518 0.8506 -0.0023 -0.0589 -0.3000 18  HIS A NE2 
64   N N   . ALA A 9   ? 0.8649 0.5214 0.8327 -0.0196 -0.0696 -0.3370 19  ALA A N   
65   C CA  . ALA A 9   ? 0.8379 0.5140 0.7864 -0.0071 -0.0568 -0.3428 19  ALA A CA  
66   C C   . ALA A 9   ? 0.8466 0.5090 0.8085 0.0075  -0.0489 -0.3498 19  ALA A C   
67   O O   . ALA A 9   ? 0.8675 0.5010 0.8475 0.0089  -0.0556 -0.3563 19  ALA A O   
68   C CB  . ALA A 9   ? 0.8645 0.5478 0.7832 -0.0074 -0.0585 -0.3649 19  ALA A CB  
69   N N   . ASN A 10  ? 0.8322 0.5151 0.7862 0.0184  -0.0351 -0.3483 20  ASN A N   
70   C CA  . ASN A 10  ? 0.8391 0.5146 0.8079 0.0339  -0.0272 -0.3561 20  ASN A CA  
71   C C   . ASN A 10  ? 0.8327 0.5366 0.7848 0.0430  -0.0114 -0.3633 20  ASN A C   
72   O O   . ASN A 10  ? 0.8676 0.5920 0.7938 0.0368  -0.0074 -0.3623 20  ASN A O   
73   C CB  . ASN A 10  ? 0.8421 0.5088 0.8374 0.0356  -0.0288 -0.3335 20  ASN A CB  
74   C CG  . ASN A 10  ? 0.8512 0.5429 0.8433 0.0295  -0.0238 -0.3076 20  ASN A CG  
75   O OD1 . ASN A 10  ? 0.9977 0.7136 0.9693 0.0259  -0.0181 -0.3061 20  ASN A OD1 
76   N ND2 . ASN A 10  ? 0.8332 0.5174 0.8445 0.0283  -0.0263 -0.2871 20  ASN A ND2 
77   N N   . ASN A 11  ? 0.8351 0.5398 0.8027 0.0577  -0.0027 -0.3703 21  ASN A N   
78   C CA  . ASN A 11  ? 0.9296 0.6624 0.8868 0.0664  0.0140  -0.3781 21  ASN A CA  
79   C C   . ASN A 11  ? 0.8516 0.6070 0.8152 0.0659  0.0217  -0.3532 21  ASN A C   
80   O O   . ASN A 11  ? 1.0042 0.7804 0.9708 0.0748  0.0353  -0.3574 21  ASN A O   
81   C CB  . ASN A 11  ? 1.1137 0.8413 1.0855 0.0821  0.0199  -0.3952 21  ASN A CB  
82   C CG  . ASN A 11  ? 1.1698 0.8798 1.1761 0.0911  0.0135  -0.3848 21  ASN A CG  
83   O OD1 . ASN A 11  ? 1.1461 0.8381 1.1642 0.0843  0.0022  -0.3694 21  ASN A OD1 
84   N ND2 . ASN A 11  ? 1.4006 1.1159 1.4227 0.1060  0.0203  -0.3927 21  ASN A ND2 
85   N N   . SER A 12  ? 0.8763 0.6291 0.8431 0.0554  0.0137  -0.3288 22  SER A N   
86   C CA  . SER A 12  ? 0.7300 0.5014 0.7037 0.0547  0.0195  -0.3056 22  SER A CA  
87   C C   . SER A 12  ? 0.7199 0.5202 0.6685 0.0510  0.0312  -0.3035 22  SER A C   
88   O O   . SER A 12  ? 0.7397 0.5434 0.6625 0.0421  0.0288  -0.3066 22  SER A O   
89   C CB  . SER A 12  ? 0.7096 0.4714 0.6908 0.0437  0.0085  -0.2824 22  SER A CB  
90   O OG  . SER A 12  ? 0.6765 0.4575 0.6600 0.0420  0.0140  -0.2612 22  SER A OG  
91   N N   . THR A 13  ? 0.7030 0.5232 0.6588 0.0573  0.0432  -0.2980 23  THR A N   
92   C CA  . THR A 13  ? 0.7191 0.5654 0.6533 0.0523  0.0546  -0.2918 23  THR A CA  
93   C C   . THR A 13  ? 0.6933 0.5480 0.6309 0.0455  0.0524  -0.2648 23  THR A C   
94   O O   . THR A 13  ? 0.6529 0.5275 0.5768 0.0418  0.0615  -0.2568 23  THR A O   
95   C CB  . THR A 13  ? 0.7714 0.6375 0.7110 0.0621  0.0710  -0.3051 23  THR A CB  
96   O OG1 . THR A 13  ? 0.8326 0.7004 0.8049 0.0713  0.0714  -0.2974 23  THR A OG1 
97   C CG2 . THR A 13  ? 0.7345 0.5943 0.6697 0.0695  0.0745  -0.3343 23  THR A CG2 
98   N N   . ASP A 14  ? 0.6639 0.5033 0.6189 0.0433  0.0408  -0.2511 24  ASP A N   
99   C CA  . ASP A 14  ? 0.6209 0.4678 0.5792 0.0369  0.0385  -0.2272 24  ASP A CA  
100  C C   . ASP A 14  ? 0.6144 0.4702 0.5465 0.0264  0.0369  -0.2204 24  ASP A C   
101  O O   . ASP A 14  ? 0.7487 0.5951 0.6680 0.0208  0.0286  -0.2271 24  ASP A O   
102  C CB  . ASP A 14  ? 0.6809 0.5088 0.6588 0.0346  0.0266  -0.2159 24  ASP A CB  
103  C CG  . ASP A 14  ? 0.7855 0.6035 0.7887 0.0449  0.0264  -0.2165 24  ASP A CG  
104  O OD1 . ASP A 14  ? 0.7993 0.6308 0.8093 0.0541  0.0356  -0.2218 24  ASP A OD1 
105  O OD2 . ASP A 14  ? 0.7454 0.5421 0.7620 0.0434  0.0165  -0.2113 24  ASP A OD2 
106  N N   . THR A 15  ? 0.5917 0.4647 0.5164 0.0239  0.0436  -0.2073 25  THR A N   
107  C CA  . THR A 15  ? 0.5892 0.4692 0.4900 0.0151  0.0409  -0.1984 25  THR A CA  
108  C C   . THR A 15  ? 0.5599 0.4444 0.4709 0.0115  0.0372  -0.1771 25  THR A C   
109  O O   . THR A 15  ? 0.5552 0.4453 0.4835 0.0154  0.0422  -0.1689 25  THR A O   
110  C CB  . THR A 15  ? 0.6017 0.4964 0.4778 0.0142  0.0528  -0.2033 25  THR A CB  
111  O OG1 . THR A 15  ? 0.7008 0.6090 0.5911 0.0190  0.0648  -0.1996 25  THR A OG1 
112  C CG2 . THR A 15  ? 0.6349 0.5260 0.4949 0.0163  0.0562  -0.2256 25  THR A CG2 
113  N N   . VAL A 16  ? 0.5926 0.4751 0.4938 0.0044  0.0277  -0.1694 26  VAL A N   
114  C CA  . VAL A 16  ? 0.5323 0.4206 0.4404 0.0010  0.0243  -0.1512 26  VAL A CA  
115  C C   . VAL A 16  ? 0.5383 0.4322 0.4217 -0.0042 0.0206  -0.1463 26  VAL A C   
116  O O   . VAL A 16  ? 0.6064 0.4977 0.4679 -0.0061 0.0179  -0.1561 26  VAL A O   
117  C CB  . VAL A 16  ? 0.5215 0.4013 0.4500 -0.0019 0.0145  -0.1455 26  VAL A CB  
118  C CG1 . VAL A 16  ? 0.5208 0.3909 0.4708 0.0028  0.0167  -0.1485 26  VAL A CG1 
119  C CG2 . VAL A 16  ? 0.5379 0.4109 0.4590 -0.0073 0.0036  -0.1534 26  VAL A CG2 
120  N N   . ASP A 17  ? 0.5191 0.4197 0.4052 -0.0059 0.0196  -0.1312 27  ASP A N   
121  C CA  . ASP A 17  ? 0.5247 0.4280 0.3903 -0.0099 0.0137  -0.1242 27  ASP A CA  
122  C C   . ASP A 17  ? 0.5162 0.4180 0.3931 -0.0124 0.0003  -0.1196 27  ASP A C   
123  O O   . ASP A 17  ? 0.5372 0.4398 0.4385 -0.0122 -0.0007 -0.1149 27  ASP A O   
124  C CB  . ASP A 17  ? 0.5170 0.4276 0.3781 -0.0101 0.0206  -0.1116 27  ASP A CB  
125  C CG  . ASP A 17  ? 0.6516 0.5668 0.4985 -0.0097 0.0340  -0.1162 27  ASP A CG  
126  O OD1 . ASP A 17  ? 0.7298 0.6429 0.5593 -0.0103 0.0365  -0.1284 27  ASP A OD1 
127  O OD2 . ASP A 17  ? 0.7467 0.6691 0.6004 -0.0094 0.0423  -0.1086 27  ASP A OD2 
128  N N   . THR A 18  ? 0.5324 0.4328 0.3914 -0.0150 -0.0100 -0.1212 28  THR A N   
129  C CA  . THR A 18  ? 0.5261 0.4287 0.3968 -0.0171 -0.0234 -0.1179 28  THR A CA  
130  C C   . THR A 18  ? 0.5304 0.4357 0.3846 -0.0168 -0.0305 -0.1085 28  THR A C   
131  O O   . THR A 18  ? 0.7172 0.6199 0.5476 -0.0166 -0.0253 -0.1045 28  THR A O   
132  C CB  . THR A 18  ? 0.5447 0.4424 0.4147 -0.0200 -0.0334 -0.1311 28  THR A CB  
133  O OG1 . THR A 18  ? 0.6050 0.4980 0.4428 -0.0205 -0.0363 -0.1387 28  THR A OG1 
134  C CG2 . THR A 18  ? 0.5431 0.4344 0.4305 -0.0202 -0.0275 -0.1400 28  THR A CG2 
135  N N   . VAL A 19  ? 0.5329 0.4432 0.4009 -0.0171 -0.0424 -0.1049 29  VAL A N   
136  C CA  . VAL A 19  ? 0.5475 0.4587 0.4033 -0.0151 -0.0511 -0.0959 29  VAL A CA  
137  C C   . VAL A 19  ? 0.5607 0.4646 0.3845 -0.0162 -0.0615 -0.1002 29  VAL A C   
138  O O   . VAL A 19  ? 0.6465 0.5450 0.4469 -0.0153 -0.0652 -0.0920 29  VAL A O   
139  C CB  . VAL A 19  ? 0.5327 0.4540 0.4162 -0.0137 -0.0605 -0.0923 29  VAL A CB  
140  C CG1 . VAL A 19  ? 0.7886 0.7142 0.6833 -0.0163 -0.0728 -0.1026 29  VAL A CG1 
141  C CG2 . VAL A 19  ? 0.5354 0.4564 0.4103 -0.0096 -0.0686 -0.0825 29  VAL A CG2 
142  N N   . LEU A 20  ? 0.5765 0.4784 0.3966 -0.0187 -0.0668 -0.1130 30  LEU A N   
143  C CA  . LEU A 20  ? 0.6113 0.5063 0.3987 -0.0201 -0.0775 -0.1185 30  LEU A CA  
144  C C   . LEU A 20  ? 0.6993 0.5867 0.4566 -0.0223 -0.0655 -0.1250 30  LEU A C   
145  O O   . LEU A 20  ? 0.7409 0.6216 0.4630 -0.0241 -0.0715 -0.1265 30  LEU A O   
146  C CB  . LEU A 20  ? 0.6201 0.5181 0.4192 -0.0221 -0.0922 -0.1306 30  LEU A CB  
147  C CG  . LEU A 20  ? 0.6640 0.5731 0.4931 -0.0208 -0.1059 -0.1273 30  LEU A CG  
148  C CD1 . LEU A 20  ? 0.6133 0.5264 0.4559 -0.0247 -0.1180 -0.1411 30  LEU A CD1 
149  C CD2 . LEU A 20  ? 0.6152 0.5236 0.4290 -0.0164 -0.1191 -0.1173 30  LEU A CD2 
150  N N   . GLU A 21  ? 0.6197 0.5085 0.3896 -0.0220 -0.0491 -0.1293 31  GLU A N   
151  C CA  . GLU A 21  ? 0.6411 0.5259 0.3880 -0.0232 -0.0372 -0.1393 31  GLU A CA  
152  C C   . GLU A 21  ? 0.6940 0.5831 0.4583 -0.0210 -0.0189 -0.1376 31  GLU A C   
153  O O   . GLU A 21  ? 0.6404 0.5321 0.4369 -0.0188 -0.0170 -0.1376 31  GLU A O   
154  C CB  . GLU A 21  ? 0.6597 0.5402 0.4056 -0.0244 -0.0431 -0.1574 31  GLU A CB  
155  C CG  . GLU A 21  ? 0.6874 0.5642 0.4074 -0.0250 -0.0319 -0.1711 31  GLU A CG  
156  C CD  . GLU A 21  ? 0.8185 0.6895 0.5429 -0.0253 -0.0374 -0.1905 31  GLU A CD  
157  O OE1 . GLU A 21  ? 0.8968 0.7654 0.6108 -0.0240 -0.0263 -0.2046 31  GLU A OE1 
158  O OE2 . GLU A 21  ? 0.7638 0.6332 0.5037 -0.0270 -0.0526 -0.1927 31  GLU A OE2 
159  N N   . LYS A 22  ? 0.8014 0.6919 0.5443 -0.0221 -0.0060 -0.1359 32  LYS A N   
160  C CA  . LYS A 22  ? 0.8160 0.7129 0.5745 -0.0197 0.0111  -0.1370 32  LYS A CA  
161  C C   . LYS A 22  ? 0.8664 0.7627 0.6241 -0.0176 0.0192  -0.1558 32  LYS A C   
162  O O   . LYS A 22  ? 0.9450 0.8363 0.6797 -0.0195 0.0147  -0.1676 32  LYS A O   
163  C CB  . LYS A 22  ? 0.8195 0.7206 0.5590 -0.0229 0.0222  -0.1269 32  LYS A CB  
164  C CG  . LYS A 22  ? 0.7564 0.6567 0.5005 -0.0240 0.0164  -0.1086 32  LYS A CG  
165  C CD  . LYS A 22  ? 0.7843 0.6889 0.5174 -0.0278 0.0301  -0.1002 32  LYS A CD  
166  C CE  . LYS A 22  ? 0.8432 0.7449 0.5822 -0.0285 0.0245  -0.0831 32  LYS A CE  
167  N NZ  . LYS A 22  ? 1.0057 0.8957 0.7151 -0.0318 0.0115  -0.0744 32  LYS A NZ  
168  N N   . ASN A 23  ? 0.7130 0.6142 0.4963 -0.0131 0.0302  -0.1592 33  ASN A N   
169  C CA  . ASN A 23  ? 0.7296 0.6314 0.5159 -0.0090 0.0398  -0.1774 33  ASN A CA  
170  C C   . ASN A 23  ? 0.6521 0.5425 0.4401 -0.0082 0.0290  -0.1919 33  ASN A C   
171  O O   . ASN A 23  ? 0.7168 0.6045 0.4850 -0.0083 0.0313  -0.2081 33  ASN A O   
172  C CB  . ASN A 23  ? 0.7869 0.6962 0.5429 -0.0118 0.0531  -0.1839 33  ASN A CB  
173  C CG  . ASN A 23  ? 0.9408 0.8569 0.7081 -0.0059 0.0674  -0.2013 33  ASN A CG  
174  O OD1 . ASN A 23  ? 0.8966 0.8147 0.6969 0.0008  0.0704  -0.2023 33  ASN A OD1 
175  N ND2 . ASN A 23  ? 1.1533 1.0731 0.8929 -0.0079 0.0760  -0.2155 33  ASN A ND2 
176  N N   . VAL A 24  ? 0.6254 0.5093 0.4368 -0.0083 0.0174  -0.1865 34  VAL A N   
177  C CA  . VAL A 24  ? 0.6387 0.5113 0.4564 -0.0091 0.0062  -0.1990 34  VAL A CA  
178  C C   . VAL A 24  ? 0.6676 0.5332 0.5096 -0.0032 0.0121  -0.2098 34  VAL A C   
179  O O   . VAL A 24  ? 0.6133 0.4788 0.4816 -0.0004 0.0145  -0.2004 34  VAL A O   
180  C CB  . VAL A 24  ? 0.6226 0.4932 0.4554 -0.0135 -0.0083 -0.1883 34  VAL A CB  
181  C CG1 . VAL A 24  ? 0.6359 0.4951 0.4798 -0.0159 -0.0190 -0.2012 34  VAL A CG1 
182  C CG2 . VAL A 24  ? 0.6282 0.5043 0.4379 -0.0175 -0.0166 -0.1793 34  VAL A CG2 
183  N N   . THR A 25  ? 0.6654 0.5240 0.4976 -0.0010 0.0135  -0.2297 35  THR A N   
184  C CA  . THR A 25  ? 0.6701 0.5187 0.5248 0.0059  0.0171  -0.2422 35  THR A CA  
185  C C   . THR A 25  ? 0.6659 0.4988 0.5427 0.0025  0.0036  -0.2407 35  THR A C   
186  O O   . THR A 25  ? 0.6805 0.5070 0.5482 -0.0038 -0.0080 -0.2464 35  THR A O   
187  C CB  . THR A 25  ? 0.7047 0.5507 0.5412 0.0096  0.0229  -0.2660 35  THR A CB  
188  O OG1 . THR A 25  ? 0.7107 0.5734 0.5246 0.0103  0.0368  -0.2663 35  THR A OG1 
189  C CG2 . THR A 25  ? 0.7112 0.5462 0.5730 0.0187  0.0264  -0.2798 35  THR A CG2 
190  N N   . VAL A 26  ? 0.6482 0.4748 0.5533 0.0059  0.0047  -0.2328 36  VAL A N   
191  C CA  . VAL A 26  ? 0.6435 0.4557 0.5696 0.0007  -0.0064 -0.2275 36  VAL A CA  
192  C C   . VAL A 26  ? 0.6578 0.4506 0.6030 0.0069  -0.0064 -0.2378 36  VAL A C   
193  O O   . VAL A 26  ? 0.6643 0.4579 0.6121 0.0169  0.0026  -0.2461 36  VAL A O   
194  C CB  . VAL A 26  ? 0.6114 0.4317 0.5517 -0.0032 -0.0072 -0.2047 36  VAL A CB  
195  C CG1 . VAL A 26  ? 0.6010 0.4373 0.5247 -0.0089 -0.0101 -0.1959 36  VAL A CG1 
196  C CG2 . VAL A 26  ? 0.6128 0.4392 0.5636 0.0046  0.0033  -0.1961 36  VAL A CG2 
197  N N   . THR A 27  ? 0.6652 0.4400 0.6250 0.0005  -0.0170 -0.2374 37  THR A N   
198  C CA  . THR A 27  ? 0.6852 0.4358 0.6617 0.0054  -0.0197 -0.2472 37  THR A CA  
199  C C   . THR A 27  ? 0.6686 0.4139 0.6660 0.0102  -0.0168 -0.2316 37  THR A C   
200  O O   . THR A 27  ? 0.6809 0.4142 0.6890 0.0208  -0.0144 -0.2392 37  THR A O   
201  C CB  . THR A 27  ? 0.7044 0.4355 0.6874 -0.0051 -0.0326 -0.2528 37  THR A CB  
202  O OG1 . THR A 27  ? 0.6845 0.4168 0.6813 -0.0155 -0.0372 -0.2329 37  THR A OG1 
203  C CG2 . THR A 27  ? 0.7202 0.4584 0.6819 -0.0106 -0.0378 -0.2669 37  THR A CG2 
204  N N   . HIS A 28  ? 0.7333 0.4873 0.7367 0.0031  -0.0176 -0.2107 38  HIS A N   
205  C CA  . HIS A 28  ? 0.6287 0.3779 0.6484 0.0062  -0.0158 -0.1945 38  HIS A CA  
206  C C   . HIS A 28  ? 0.7285 0.5018 0.7442 0.0036  -0.0101 -0.1769 38  HIS A C   
207  O O   . HIS A 28  ? 0.7208 0.5072 0.7275 -0.0047 -0.0118 -0.1727 38  HIS A O   
208  C CB  . HIS A 28  ? 0.6402 0.3655 0.6747 -0.0027 -0.0250 -0.1869 38  HIS A CB  
209  C CG  . HIS A 28  ? 0.7055 0.4038 0.7443 -0.0021 -0.0323 -0.2041 38  HIS A CG  
210  N ND1 . HIS A 28  ? 0.6915 0.3861 0.7229 -0.0101 -0.0383 -0.2176 38  HIS A ND1 
211  C CD2 . HIS A 28  ? 0.6985 0.3709 0.7487 0.0061  -0.0357 -0.2106 38  HIS A CD2 
212  C CE1 . HIS A 28  ? 0.7236 0.3910 0.7612 -0.0076 -0.0444 -0.2322 38  HIS A CE1 
213  N NE2 . HIS A 28  ? 0.7462 0.3989 0.7955 0.0026  -0.0430 -0.2282 38  HIS A NE2 
214  N N   . SER A 29  ? 0.5824 0.3609 0.6055 0.0111  -0.0045 -0.1675 39  SER A N   
215  C CA  . SER A 29  ? 0.5537 0.3532 0.5736 0.0094  0.0008  -0.1518 39  SER A CA  
216  C C   . SER A 29  ? 0.5450 0.3408 0.5783 0.0151  0.0022  -0.1398 39  SER A C   
217  O O   . SER A 29  ? 0.5647 0.3450 0.6085 0.0232  0.0001  -0.1453 39  SER A O   
218  C CB  . SER A 29  ? 0.5462 0.3668 0.5504 0.0135  0.0089  -0.1580 39  SER A CB  
219  O OG  . SER A 29  ? 0.6527 0.4743 0.6595 0.0246  0.0153  -0.1696 39  SER A OG  
220  N N   . VAL A 30  ? 0.5216 0.3314 0.5543 0.0115  0.0047  -0.1239 40  VAL A N   
221  C CA  . VAL A 30  ? 0.5124 0.3217 0.5547 0.0161  0.0055  -0.1115 40  VAL A CA  
222  C C   . VAL A 30  ? 0.4890 0.3227 0.5259 0.0188  0.0130  -0.1060 40  VAL A C   
223  O O   . VAL A 30  ? 0.4749 0.3220 0.5022 0.0122  0.0150  -0.1013 40  VAL A O   
224  C CB  . VAL A 30  ? 0.5120 0.3099 0.5592 0.0067  0.0001  -0.0960 40  VAL A CB  
225  C CG1 . VAL A 30  ? 0.4992 0.3094 0.5399 -0.0050 0.0006  -0.0910 40  VAL A CG1 
226  C CG2 . VAL A 30  ? 0.5017 0.3026 0.5535 0.0107  0.0010  -0.0820 40  VAL A CG2 
227  N N   . ASN A 31  ? 0.5794 0.4184 0.6236 0.0286  0.0164  -0.1072 41  ASN A N   
228  C CA  . ASN A 31  ? 0.4876 0.3484 0.5290 0.0304  0.0232  -0.1017 41  ASN A CA  
229  C C   . ASN A 31  ? 0.4522 0.3144 0.4970 0.0267  0.0203  -0.0845 41  ASN A C   
230  O O   . ASN A 31  ? 0.4934 0.3420 0.5472 0.0292  0.0147  -0.0781 41  ASN A O   
231  C CB  . ASN A 31  ? 0.5185 0.3878 0.5694 0.0416  0.0282  -0.1114 41  ASN A CB  
232  C CG  . ASN A 31  ? 0.5276 0.4179 0.5797 0.0426  0.0341  -0.1042 41  ASN A CG  
233  O OD1 . ASN A 31  ? 0.6626 0.5681 0.7030 0.0382  0.0409  -0.1050 41  ASN A OD1 
234  N ND2 . ASN A 31  ? 0.5330 0.4231 0.5988 0.0481  0.0304  -0.0970 41  ASN A ND2 
235  N N   . LEU A 32  ? 0.5203 0.3973 0.5565 0.0209  0.0237  -0.0770 42  LEU A N   
236  C CA  . LEU A 32  ? 0.4214 0.3020 0.4587 0.0170  0.0221  -0.0625 42  LEU A CA  
237  C C   . LEU A 32  ? 0.4466 0.3426 0.4861 0.0216  0.0261  -0.0588 42  LEU A C   
238  O O   . LEU A 32  ? 0.4981 0.3988 0.5367 0.0187  0.0251  -0.0481 42  LEU A O   
239  C CB  . LEU A 32  ? 0.4122 0.2981 0.4410 0.0075  0.0221  -0.0574 42  LEU A CB  
240  C CG  . LEU A 32  ? 0.4238 0.2974 0.4530 0.0005  0.0175  -0.0592 42  LEU A CG  
241  C CD1 . LEU A 32  ? 0.4127 0.2971 0.4373 -0.0075 0.0176  -0.0552 42  LEU A CD1 
242  C CD2 . LEU A 32  ? 0.4362 0.2927 0.4728 -0.0015 0.0130  -0.0519 42  LEU A CD2 
243  N N   . LEU A 33  ? 0.4360 0.3410 0.4790 0.0281  0.0309  -0.0683 43  LEU A N   
244  C CA  . LEU A 33  ? 0.3970 0.3195 0.4430 0.0306  0.0358  -0.0664 43  LEU A CA  
245  C C   . LEU A 33  ? 0.4035 0.3276 0.4663 0.0406  0.0346  -0.0712 43  LEU A C   
246  O O   . LEU A 33  ? 0.4149 0.3391 0.4840 0.0467  0.0374  -0.0838 43  LEU A O   
247  C CB  . LEU A 33  ? 0.3942 0.3295 0.4293 0.0275  0.0439  -0.0730 43  LEU A CB  
248  C CG  . LEU A 33  ? 0.3839 0.3371 0.4212 0.0275  0.0500  -0.0713 43  LEU A CG  
249  C CD1 . LEU A 33  ? 0.3700 0.3254 0.4061 0.0234  0.0465  -0.0586 43  LEU A CD1 
250  C CD2 . LEU A 33  ? 0.3902 0.3514 0.4127 0.0227  0.0579  -0.0768 43  LEU A CD2 
251  N N   . GLU A 34  ? 0.4045 0.3306 0.4748 0.0428  0.0299  -0.0620 44  GLU A N   
252  C CA  . GLU A 34  ? 0.4037 0.3335 0.4922 0.0532  0.0267  -0.0657 44  GLU A CA  
253  C C   . GLU A 34  ? 0.3929 0.3474 0.4886 0.0546  0.0346  -0.0715 44  GLU A C   
254  O O   . GLU A 34  ? 0.3793 0.3446 0.4686 0.0482  0.0371  -0.0644 44  GLU A O   
255  C CB  . GLU A 34  ? 0.4062 0.3264 0.4975 0.0545  0.0165  -0.0528 44  GLU A CB  
256  C CG  . GLU A 34  ? 0.4150 0.3374 0.5259 0.0665  0.0099  -0.0559 44  GLU A CG  
257  C CD  . GLU A 34  ? 0.5085 0.4171 0.6307 0.0759  0.0068  -0.0667 44  GLU A CD  
258  O OE1 . GLU A 34  ? 0.5661 0.4509 0.6807 0.0735  0.0017  -0.0632 44  GLU A OE1 
259  O OE2 . GLU A 34  ? 0.6791 0.6012 0.8187 0.0854  0.0100  -0.0796 44  GLU A OE2 
260  N N   . ASP A 35  ? 0.4006 0.3643 0.5104 0.0625  0.0390  -0.0850 45  ASP A N   
261  C CA  . ASP A 35  ? 0.3929 0.3823 0.5124 0.0629  0.0479  -0.0915 45  ASP A CA  
262  C C   . ASP A 35  ? 0.3973 0.3976 0.5440 0.0747  0.0440  -0.0979 45  ASP A C   
263  O O   . ASP A 35  ? 0.5062 0.5309 0.6658 0.0751  0.0514  -0.1044 45  ASP A O   
264  C CB  . ASP A 35  ? 0.4349 0.4329 0.5459 0.0597  0.0605  -0.1040 45  ASP A CB  
265  C CG  . ASP A 35  ? 0.5957 0.5873 0.7161 0.0694  0.0611  -0.1191 45  ASP A CG  
266  O OD1 . ASP A 35  ? 0.6470 0.6189 0.7738 0.0761  0.0505  -0.1176 45  ASP A OD1 
267  O OD2 . ASP A 35  ? 0.6711 0.6766 0.7915 0.0697  0.0723  -0.1327 45  ASP A OD2 
268  N N   . SER A 36  ? 0.4092 0.3923 0.5656 0.0840  0.0321  -0.0960 46  SER A N   
269  C CA  . SER A 36  ? 0.4172 0.4085 0.6012 0.0977  0.0260  -0.1033 46  SER A CA  
270  C C   . SER A 36  ? 0.4132 0.4038 0.6029 0.0995  0.0135  -0.0900 46  SER A C   
271  O O   . SER A 36  ? 0.4173 0.3907 0.5890 0.0929  0.0066  -0.0751 46  SER A O   
272  C CB  . SER A 36  ? 0.4516 0.4216 0.6438 0.1089  0.0192  -0.1115 46  SER A CB  
273  O OG  . SER A 36  ? 0.8420 0.8167 1.0321 0.1091  0.0308  -0.1275 46  SER A OG  
274  N N   . HIS A 37  ? 0.4127 0.4236 0.6281 0.1085  0.0108  -0.0964 47  HIS A N   
275  C CA  . HIS A 37  ? 0.4129 0.4249 0.6367 0.1124  -0.0031 -0.0862 47  HIS A CA  
276  C C   . HIS A 37  ? 0.4619 0.4888 0.7203 0.1285  -0.0094 -0.0984 47  HIS A C   
277  O O   . HIS A 37  ? 0.5250 0.5691 0.8013 0.1340  0.0008  -0.1154 47  HIS A O   
278  C CB  . HIS A 37  ? 0.3939 0.4243 0.6099 0.1008  0.0013  -0.0789 47  HIS A CB  
279  C CG  . HIS A 37  ? 0.3825 0.4457 0.6156 0.0983  0.0144  -0.0912 47  HIS A CG  
280  N ND1 . HIS A 37  ? 0.3811 0.4693 0.6434 0.1053  0.0107  -0.0980 47  HIS A ND1 
281  C CD2 . HIS A 37  ? 0.3746 0.4498 0.5994 0.0889  0.0311  -0.0979 47  HIS A CD2 
282  C CE1 . HIS A 37  ? 0.3721 0.4874 0.6442 0.0991  0.0260  -0.1084 47  HIS A CE1 
283  N NE2 . HIS A 37  ? 0.3692 0.4759 0.6171 0.0890  0.0385  -0.1079 47  HIS A NE2 
284  N N   . ASN A 38  ? 0.4316 0.4527 0.6992 0.1364  -0.0266 -0.0901 48  ASN A N   
285  C CA  . ASN A 38  ? 0.4439 0.4768 0.7464 0.1539  -0.0364 -0.1009 48  ASN A CA  
286  C C   . ASN A 38  ? 0.4294 0.5018 0.7575 0.1543  -0.0328 -0.1088 48  ASN A C   
287  O O   . ASN A 38  ? 0.4376 0.5267 0.7998 0.1690  -0.0397 -0.1202 48  ASN A O   
288  C CB  . ASN A 38  ? 0.4667 0.4711 0.7669 0.1637  -0.0593 -0.0881 48  ASN A CB  
289  C CG  . ASN A 38  ? 0.4621 0.4638 0.7444 0.1551  -0.0691 -0.0702 48  ASN A CG  
290  O OD1 . ASN A 38  ? 0.5548 0.5775 0.8307 0.1434  -0.0598 -0.0687 48  ASN A OD1 
291  N ND2 . ASN A 38  ? 0.4850 0.4592 0.7575 0.1608  -0.0882 -0.0565 48  ASN A ND2 
292  N N   . GLY A 39  ? 0.4096 0.4974 0.7241 0.1387  -0.0228 -0.1035 49  GLY A N   
293  C CA  . GLY A 39  ? 0.3968 0.5221 0.7354 0.1363  -0.0180 -0.1112 49  GLY A CA  
294  C C   . GLY A 39  ? 0.4026 0.5354 0.7599 0.1449  -0.0375 -0.1065 49  GLY A C   
295  O O   . GLY A 39  ? 0.3974 0.5636 0.7869 0.1486  -0.0370 -0.1173 49  GLY A O   
296  N N   . LYS A 40  ? 0.4153 0.5187 0.7530 0.1476  -0.0550 -0.0908 50  LYS A N   
297  C CA  . LYS A 40  ? 0.4265 0.5325 0.7773 0.1565  -0.0764 -0.0849 50  LYS A CA  
298  C C   . LYS A 40  ? 0.4282 0.5134 0.7433 0.1456  -0.0851 -0.0654 50  LYS A C   
299  O O   . LYS A 40  ? 0.4276 0.4880 0.7099 0.1360  -0.0788 -0.0555 50  LYS A O   
300  C CB  . LYS A 40  ? 0.4527 0.5403 0.8197 0.1765  -0.0939 -0.0867 50  LYS A CB  
301  C CG  . LYS A 40  ? 0.4549 0.5611 0.8583 0.1897  -0.0861 -0.1080 50  LYS A CG  
302  C CD  . LYS A 40  ? 0.5316 0.6103 0.9450 0.2089  -0.1034 -0.1087 50  LYS A CD  
303  C CE  . LYS A 40  ? 0.6467 0.7414 1.0932 0.2219  -0.0933 -0.1318 50  LYS A CE  
304  N NZ  . LYS A 40  ? 0.9459 1.0085 1.4002 0.2404  -0.1097 -0.1332 50  LYS A NZ  
305  N N   . LEU A 41  ? 0.4315 0.5286 0.7540 0.1472  -0.0996 -0.0612 51  LEU A N   
306  C CA  . LEU A 41  ? 0.4391 0.5170 0.7287 0.1391  -0.1106 -0.0438 51  LEU A CA  
307  C C   . LEU A 41  ? 0.4698 0.5165 0.7492 0.1508  -0.1316 -0.0322 51  LEU A C   
308  O O   . LEU A 41  ? 0.6166 0.6691 0.9219 0.1662  -0.1486 -0.0362 51  LEU A O   
309  C CB  . LEU A 41  ? 0.4533 0.5577 0.7532 0.1345  -0.1171 -0.0453 51  LEU A CB  
310  C CG  . LEU A 41  ? 0.5504 0.6861 0.8637 0.1225  -0.0980 -0.0567 51  LEU A CG  
311  C CD1 . LEU A 41  ? 0.5357 0.6935 0.8584 0.1175  -0.1073 -0.0573 51  LEU A CD1 
312  C CD2 . LEU A 41  ? 0.4033 0.5246 0.6845 0.1072  -0.0796 -0.0514 51  LEU A CD2 
313  N N   . CYS A 42  ? 0.4801 0.4938 0.7227 0.1433  -0.1309 -0.0179 52  CYS A N   
314  C CA  . CYS A 42  ? 0.5126 0.4910 0.7404 0.1514  -0.1480 -0.0051 52  CYS A CA  
315  C C   . CYS A 42  ? 0.5282 0.4887 0.7189 0.1421  -0.1585 0.0135  52  CYS A C   
316  O O   . CYS A 42  ? 0.5123 0.4857 0.6873 0.1292  -0.1508 0.0154  52  CYS A O   
317  C CB  . CYS A 42  ? 0.5173 0.4699 0.7342 0.1499  -0.1378 -0.0044 52  CYS A CB  
318  S SG  . CYS A 42  ? 0.6027 0.5735 0.8580 0.1607  -0.1248 -0.0272 52  CYS A SG  
319  N N   . ARG A 43  ? 0.5629 0.4918 0.7386 0.1486  -0.1765 0.0270  53  ARG A N   
320  C CA  . ARG A 43  ? 0.5843 0.4917 0.7194 0.1388  -0.1853 0.0459  53  ARG A CA  
321  C C   . ARG A 43  ? 0.5771 0.4677 0.6805 0.1223  -0.1673 0.0532  53  ARG A C   
322  O O   . ARG A 43  ? 0.6229 0.5038 0.7318 0.1217  -0.1557 0.0487  53  ARG A O   
323  C CB  . ARG A 43  ? 0.6297 0.5054 0.7561 0.1499  -0.2100 0.0596  53  ARG A CB  
324  C CG  . ARG A 43  ? 0.6793 0.5694 0.8425 0.1696  -0.2299 0.0511  53  ARG A CG  
325  C CD  . ARG A 43  ? 0.7705 0.6231 0.9274 0.1825  -0.2536 0.0638  53  ARG A CD  
326  N NE  . ARG A 43  ? 0.8962 0.7629 1.0911 0.2034  -0.2746 0.0549  53  ARG A NE  
327  C CZ  . ARG A 43  ? 1.0670 0.9392 1.2594 0.2091  -0.2970 0.0615  53  ARG A CZ  
328  N NH1 . ARG A 43  ? 1.0393 0.9032 1.1902 0.1950  -0.3004 0.0768  53  ARG A NH1 
329  N NH2 . ARG A 43  ? 0.9857 0.8728 1.2175 0.2293  -0.3163 0.0517  53  ARG A NH2 
330  N N   . LEU A 44  ? 0.6814 0.5702 0.7527 0.1090  -0.1651 0.0634  54  LEU A N   
331  C CA  . LEU A 44  ? 0.7104 0.5861 0.7520 0.0931  -0.1490 0.0704  54  LEU A CA  
332  C C   . LEU A 44  ? 0.8778 0.7190 0.8855 0.0887  -0.1605 0.0901  54  LEU A C   
333  O O   . LEU A 44  ? 0.8442 0.6822 0.8273 0.0845  -0.1704 0.1004  54  LEU A O   
334  C CB  . LEU A 44  ? 0.6853 0.5839 0.7156 0.0810  -0.1365 0.0662  54  LEU A CB  
335  C CG  . LEU A 44  ? 0.8367 0.7283 0.8429 0.0659  -0.1184 0.0698  54  LEU A CG  
336  C CD1 . LEU A 44  ? 0.8348 0.7297 0.8597 0.0661  -0.1031 0.0595  54  LEU A CD1 
337  C CD2 . LEU A 44  ? 0.9765 0.8871 0.9692 0.0560  -0.1107 0.0668  54  LEU A CD2 
338  N N   . LYS A 45  A 0.9198 0.7343 0.9249 0.0890  -0.1591 0.0953  54  LYS A N   
339  C CA  . LYS A 45  A 0.9497 0.7274 0.9233 0.0835  -0.1692 0.1150  54  LYS A CA  
340  C C   . LYS A 45  A 1.0217 0.7864 0.9906 0.0948  -0.1953 0.1251  54  LYS A C   
341  O O   . LYS A 45  A 1.0763 0.8236 1.0101 0.0873  -0.2046 0.1419  54  LYS A O   
342  C CB  . LYS A 45  A 1.0098 0.7852 0.9464 0.0639  -0.1564 0.1250  54  LYS A CB  
343  C CG  . LYS A 45  A 1.0643 0.8535 1.0061 0.0535  -0.1325 0.1150  54  LYS A CG  
344  C CD  . LYS A 45  A 1.2214 1.0121 1.1304 0.0357  -0.1204 0.1230  54  LYS A CD  
345  C CE  . LYS A 45  A 1.4396 1.2483 1.3575 0.0274  -0.0986 0.1113  54  LYS A CE  
346  N NZ  . LYS A 45  A 1.4518 1.2458 1.3830 0.0273  -0.0927 0.1087  54  LYS A NZ  
347  N N   . GLY A 46  ? 1.1119 0.8863 1.1168 0.1131  -0.2074 0.1143  55  GLY A N   
348  C CA  . GLY A 46  ? 1.0656 0.8301 1.0740 0.1271  -0.2342 0.1212  55  GLY A CA  
349  C C   . GLY A 46  ? 1.0937 0.8891 1.1077 0.1300  -0.2424 0.1161  55  GLY A C   
350  O O   . GLY A 46  ? 1.2114 1.0121 1.2467 0.1460  -0.2632 0.1133  55  GLY A O   
351  N N   . ILE A 47  ? 0.9672 0.7831 0.9642 0.1155  -0.2274 0.1137  56  ILE A N   
352  C CA  . ILE A 47  ? 0.9262 0.7689 0.9248 0.1162  -0.2354 0.1090  56  ILE A CA  
353  C C   . ILE A 47  ? 0.8254 0.7066 0.8696 0.1235  -0.2271 0.0872  56  ILE A C   
354  O O   . ILE A 47  ? 0.8324 0.7273 0.8885 0.1172  -0.2049 0.0764  56  ILE A O   
355  C CB  . ILE A 47  ? 0.9479 0.7935 0.9071 0.0976  -0.2237 0.1154  56  ILE A CB  
356  C CG1 . ILE A 47  ? 1.0868 0.8961 0.9994 0.0895  -0.2324 0.1376  56  ILE A CG1 
357  C CG2 . ILE A 47  ? 0.9102 0.7842 0.8732 0.0978  -0.2309 0.1078  56  ILE A CG2 
358  C CD1 . ILE A 47  ? 1.2015 1.0143 1.0736 0.0720  -0.2219 0.1435  56  ILE A CD1 
359  N N   . ALA A 48  ? 0.7469 0.6459 0.8166 0.1364  -0.2453 0.0808  57  ALA A N   
360  C CA  . ALA A 48  ? 0.6851 0.6221 0.8009 0.1435  -0.2392 0.0604  57  ALA A CA  
361  C C   . ALA A 48  ? 0.7037 0.6692 0.8152 0.1302  -0.2264 0.0526  57  ALA A C   
362  O O   . ALA A 48  ? 0.6989 0.6577 0.7756 0.1198  -0.2297 0.0618  57  ALA A O   
363  C CB  . ALA A 48  ? 0.6927 0.6399 0.8397 0.1621  -0.2646 0.0561  57  ALA A CB  
364  N N   . PRO A 49  ? 0.5893 0.5858 0.7345 0.1296  -0.2112 0.0352  58  PRO A N   
365  C CA  . PRO A 49  ? 0.5630 0.5843 0.7059 0.1169  -0.2002 0.0277  58  PRO A CA  
366  C C   . PRO A 49  ? 0.5415 0.5891 0.7061 0.1218  -0.2170 0.0205  58  PRO A C   
367  O O   . PRO A 49  ? 0.6002 0.6470 0.7797 0.1357  -0.2391 0.0224  58  PRO A O   
368  C CB  . PRO A 49  ? 0.5033 0.5418 0.6704 0.1131  -0.1763 0.0141  58  PRO A CB  
369  C CG  . PRO A 49  ? 0.5073 0.5474 0.7076 0.1288  -0.1811 0.0076  58  PRO A CG  
370  C CD  . PRO A 49  ? 0.5723 0.5786 0.7534 0.1380  -0.2000 0.0225  58  PRO A CD  
371  N N   . LEU A 50  ? 0.5207 0.5912 0.6881 0.1105  -0.2077 0.0120  59  LEU A N   
372  C CA  . LEU A 50  ? 0.5214 0.6195 0.7102 0.1119  -0.2217 0.0035  59  LEU A CA  
373  C C   . LEU A 50  ? 0.4892 0.6215 0.7214 0.1099  -0.2067 -0.0142 59  LEU A C   
374  O O   . LEU A 50  ? 0.5064 0.6469 0.7333 0.0961  -0.1881 -0.0193 59  LEU A O   
375  C CB  . LEU A 50  ? 0.5421 0.6366 0.6960 0.0990  -0.2249 0.0080  59  LEU A CB  
376  C CG  . LEU A 50  ? 0.5284 0.6518 0.7019 0.0967  -0.2369 -0.0024 59  LEU A CG  
377  C CD1 . LEU A 50  ? 0.5548 0.6837 0.7448 0.1115  -0.2658 -0.0007 59  LEU A CD1 
378  C CD2 . LEU A 50  ? 0.5350 0.6521 0.6712 0.0826  -0.2355 0.0001  59  LEU A CD2 
379  N N   . GLN A 51  ? 0.5324 0.6843 0.8073 0.1235  -0.2146 -0.0234 60  GLN A N   
380  C CA  . GLN A 51  ? 0.5260 0.7143 0.8444 0.1212  -0.2011 -0.0407 60  GLN A CA  
381  C C   . GLN A 51  ? 0.5089 0.7260 0.8450 0.1157  -0.2120 -0.0485 60  GLN A C   
382  O O   . GLN A 51  ? 0.7078 0.9314 1.0549 0.1259  -0.2367 -0.0478 60  GLN A O   
383  C CB  . GLN A 51  ? 0.5876 0.7880 0.9468 0.1383  -0.2037 -0.0496 60  GLN A CB  
384  C CG  . GLN A 51  ? 0.6727 0.8548 1.0250 0.1403  -0.1853 -0.0488 60  GLN A CG  
385  C CD  . GLN A 51  ? 0.9127 1.1121 1.3094 0.1563  -0.1850 -0.0620 60  GLN A CD  
386  O OE1 . GLN A 51  ? 1.0582 1.2608 1.4771 0.1729  -0.2065 -0.0634 60  GLN A OE1 
387  N NE2 . GLN A 51  ? 0.9146 1.1253 1.3243 0.1518  -0.1609 -0.0723 60  GLN A NE2 
388  N N   . LEU A 52  ? 0.4582 0.6914 0.7968 0.0996  -0.1949 -0.0558 61  LEU A N   
389  C CA  . LEU A 52  ? 0.5939 0.8527 0.9480 0.0916  -0.2039 -0.0638 61  LEU A CA  
390  C C   . LEU A 52  ? 0.5275 0.8282 0.9392 0.0961  -0.2045 -0.0801 61  LEU A C   
391  O O   . LEU A 52  ? 0.5903 0.9154 1.0225 0.0927  -0.2174 -0.0874 61  LEU A O   
392  C CB  . LEU A 52  ? 0.4255 0.6805 0.7571 0.0717  -0.1866 -0.0645 61  LEU A CB  
393  C CG  . LEU A 52  ? 0.4357 0.6551 0.7130 0.0654  -0.1854 -0.0513 61  LEU A CG  
394  C CD1 . LEU A 52  ? 0.4236 0.6431 0.6862 0.0474  -0.1710 -0.0550 61  LEU A CD1 
395  C CD2 . LEU A 52  ? 0.4650 0.6719 0.7197 0.0721  -0.2112 -0.0430 61  LEU A CD2 
396  N N   . GLY A 53  ? 0.4172 0.7282 0.8560 0.1034  -0.1908 -0.0869 62  GLY A N   
397  C CA  . GLY A 53  ? 0.4071 0.7615 0.9020 0.1067  -0.1881 -0.1039 62  GLY A CA  
398  C C   . GLY A 53  ? 0.5497 0.9282 1.0563 0.0859  -0.1707 -0.1127 62  GLY A C   
399  O O   . GLY A 53  ? 0.5271 0.8898 1.0063 0.0715  -0.1505 -0.1084 62  GLY A O   
400  N N   . ASN A 54  ? 0.5579 0.9747 1.1065 0.0841  -0.1795 -0.1251 63  ASN A N   
401  C CA  . ASN A 54  ? 0.5048 0.9457 1.0680 0.0631  -0.1654 -0.1336 63  ASN A CA  
402  C C   . ASN A 54  ? 0.4018 0.8255 0.9314 0.0494  -0.1749 -0.1267 63  ASN A C   
403  O O   . ASN A 54  ? 0.4379 0.8814 0.9823 0.0327  -0.1697 -0.1343 63  ASN A O   
404  C CB  . ASN A 54  ? 0.6373 1.1288 1.2621 0.0652  -0.1706 -0.1509 63  ASN A CB  
405  C CG  . ASN A 54  ? 0.8608 1.3735 1.5232 0.0799  -0.1612 -0.1608 63  ASN A CG  
406  O OD1 . ASN A 54  ? 0.9583 1.4541 1.6042 0.0811  -0.1417 -0.1577 63  ASN A OD1 
407  N ND2 . ASN A 54  ? 1.0464 1.5973 1.7608 0.0918  -0.1757 -0.1740 63  ASN A ND2 
408  N N   . CYS A 55  ? 0.3978 0.7853 0.8827 0.0555  -0.1882 -0.1132 64  CYS A N   
409  C CA  . CYS A 55  ? 0.4092 0.7799 0.8601 0.0449  -0.1989 -0.1078 64  CYS A CA  
410  C C   . CYS A 55  ? 0.4028 0.7393 0.8072 0.0338  -0.1804 -0.0983 64  CYS A C   
411  O O   . CYS A 55  ? 0.3987 0.7128 0.7828 0.0403  -0.1700 -0.0900 64  CYS A O   
412  C CB  . CYS A 55  ? 0.4734 0.8297 0.9054 0.0590  -0.2281 -0.0998 64  CYS A CB  
413  S SG  . CYS A 55  ? 0.5889 0.9845 1.0756 0.0739  -0.2551 -0.1110 64  CYS A SG  
414  N N   . SER A 56  ? 0.4030 0.7360 0.7926 0.0172  -0.1770 -0.1003 65  SER A N   
415  C CA  . SER A 56  ? 0.3999 0.7010 0.7463 0.0075  -0.1625 -0.0924 65  SER A CA  
416  C C   . SER A 56  ? 0.4674 0.7402 0.7700 0.0130  -0.1779 -0.0826 65  SER A C   
417  O O   . SER A 56  ? 0.4370 0.7134 0.7400 0.0231  -0.2001 -0.0809 65  SER A O   
418  C CB  . SER A 56  ? 0.4215 0.7288 0.7721 -0.0123 -0.1518 -0.0996 65  SER A CB  
419  O OG  . SER A 56  ? 0.4616 0.7727 0.8078 -0.0178 -0.1699 -0.1041 65  SER A OG  
420  N N   . VAL A 57  ? 0.4388 0.6837 0.7025 0.0060  -0.1661 -0.0762 66  VAL A N   
421  C CA  . VAL A 57  ? 0.4381 0.6583 0.6586 0.0084  -0.1776 -0.0683 66  VAL A CA  
422  C C   . VAL A 57  ? 0.5153 0.7447 0.7338 0.0022  -0.1953 -0.0754 66  VAL A C   
423  O O   . VAL A 57  ? 0.4783 0.7011 0.6765 0.0088  -0.2148 -0.0713 66  VAL A O   
424  C CB  . VAL A 57  ? 0.4493 0.6422 0.6341 0.0018  -0.1595 -0.0625 66  VAL A CB  
425  C CG1 . VAL A 57  ? 0.4538 0.6259 0.5956 0.0012  -0.1691 -0.0575 66  VAL A CG1 
426  C CG2 . VAL A 57  ? 0.4201 0.6017 0.6023 0.0096  -0.1462 -0.0544 66  VAL A CG2 
427  N N   . ALA A 58  ? 0.6344 0.8784 0.8729 -0.0112 -0.1895 -0.0862 67  ALA A N   
428  C CA  . ALA A 58  ? 0.5645 0.8189 0.8053 -0.0183 -0.2067 -0.0951 67  ALA A CA  
429  C C   . ALA A 58  ? 0.5437 0.8243 0.8147 -0.0089 -0.2293 -0.0989 67  ALA A C   
430  O O   . ALA A 58  ? 0.5352 0.8147 0.7910 -0.0059 -0.2513 -0.0995 67  ALA A O   
431  C CB  . ALA A 58  ? 0.5870 0.8509 0.8472 -0.0356 -0.1949 -0.1056 67  ALA A CB  
432  N N   . GLY A 59  ? 0.4907 0.7957 0.8048 -0.0036 -0.2248 -0.1021 68  GLY A N   
433  C CA  . GLY A 59  ? 0.4680 0.7998 0.8158 0.0073  -0.2466 -0.1067 68  GLY A CA  
434  C C   . GLY A 59  ? 0.4881 0.8025 0.8108 0.0248  -0.2651 -0.0951 68  GLY A C   
435  O O   . GLY A 59  ? 0.5094 0.8336 0.8371 0.0322  -0.2911 -0.0965 68  GLY A O   
436  N N   . TRP A 60  ? 0.4842 0.7715 0.7786 0.0311  -0.2527 -0.0831 69  TRP A N   
437  C CA  . TRP A 60  ? 0.5064 0.7725 0.7734 0.0458  -0.2687 -0.0702 69  TRP A CA  
438  C C   . TRP A 60  ? 0.5455 0.7914 0.7650 0.0417  -0.2836 -0.0647 69  TRP A C   
439  O O   . TRP A 60  ? 0.5627 0.8045 0.7702 0.0515  -0.3081 -0.0589 69  TRP A O   
440  C CB  . TRP A 60  ? 0.5136 0.7557 0.7627 0.0507  -0.2500 -0.0595 69  TRP A CB  
441  C CG  . TRP A 60  ? 0.5204 0.7300 0.7242 0.0584  -0.2599 -0.0438 69  TRP A CG  
442  C CD1 . TRP A 60  ? 0.5485 0.7520 0.7459 0.0716  -0.2847 -0.0360 69  TRP A CD1 
443  C CD2 . TRP A 60  ? 0.5606 0.7395 0.7195 0.0528  -0.2450 -0.0336 69  TRP A CD2 
444  N NE1 . TRP A 60  ? 0.5689 0.7384 0.7178 0.0729  -0.2853 -0.0207 69  TRP A NE1 
445  C CE2 . TRP A 60  ? 0.6225 0.7783 0.7487 0.0614  -0.2605 -0.0196 69  TRP A CE2 
446  C CE3 . TRP A 60  ? 0.5501 0.7191 0.6940 0.0413  -0.2206 -0.0349 69  TRP A CE3 
447  C CZ2 . TRP A 60  ? 0.5618 0.6876 0.6424 0.0575  -0.2507 -0.0076 69  TRP A CZ2 
448  C CZ3 . TRP A 60  ? 0.5110 0.6514 0.6120 0.0392  -0.2122 -0.0240 69  TRP A CZ3 
449  C CH2 . TRP A 60  ? 0.5398 0.6601 0.6102 0.0466  -0.2263 -0.0108 69  TRP A CH2 
450  N N   . ILE A 61  ? 0.6011 0.8340 0.7927 0.0277  -0.2698 -0.0668 70  ILE A N   
451  C CA  . ILE A 61  ? 0.5806 0.7930 0.7233 0.0238  -0.2804 -0.0625 70  ILE A CA  
452  C C   . ILE A 61  ? 0.6356 0.8654 0.7853 0.0180  -0.3006 -0.0739 70  ILE A C   
453  O O   . ILE A 61  ? 0.6206 0.8379 0.7328 0.0182  -0.3168 -0.0707 70  ILE A O   
454  C CB  . ILE A 61  ? 0.5501 0.7402 0.6593 0.0132  -0.2572 -0.0609 70  ILE A CB  
455  C CG1 . ILE A 61  ? 0.5848 0.7483 0.6386 0.0145  -0.2630 -0.0507 70  ILE A CG1 
456  C CG2 . ILE A 61  ? 0.5411 0.7412 0.6607 -0.0013 -0.2501 -0.0751 70  ILE A CG2 
457  C CD1 . ILE A 61  ? 0.6432 0.7914 0.6825 0.0268  -0.2687 -0.0346 70  ILE A CD1 
458  N N   . LEU A 62  ? 0.5862 0.8450 0.7821 0.0119  -0.3000 -0.0874 71  LEU A N   
459  C CA  . LEU A 62  ? 0.5764 0.8542 0.7842 0.0055  -0.3201 -0.0996 71  LEU A CA  
460  C C   . LEU A 62  ? 0.5911 0.8918 0.8280 0.0181  -0.3476 -0.1006 71  LEU A C   
461  O O   . LEU A 62  ? 0.6107 0.9259 0.8530 0.0148  -0.3693 -0.1094 71  LEU A O   
462  C CB  . LEU A 62  ? 0.5546 0.8521 0.7981 -0.0100 -0.3061 -0.1140 71  LEU A CB  
463  C CG  . LEU A 62  ? 0.6049 0.8809 0.8196 -0.0247 -0.2874 -0.1172 71  LEU A CG  
464  C CD1 . LEU A 62  ? 0.5317 0.8261 0.7853 -0.0397 -0.2747 -0.1294 71  LEU A CD1 
465  C CD2 . LEU A 62  ? 0.5821 0.8425 0.7543 -0.0285 -0.3028 -0.1203 71  LEU A CD2 
466  N N   . GLY A 63  ? 0.5839 0.8880 0.8403 0.0329  -0.3485 -0.0928 72  GLY A N   
467  C CA  . GLY A 63  ? 0.5986 0.9242 0.8861 0.0470  -0.3754 -0.0943 72  GLY A CA  
468  C C   . GLY A 63  ? 0.5775 0.9462 0.9313 0.0442  -0.3748 -0.1105 72  GLY A C   
469  O O   . GLY A 63  ? 0.6226 1.0165 1.0012 0.0448  -0.3982 -0.1201 72  GLY A O   
470  N N   . ASN A 64  ? 0.5837 0.9623 0.9665 0.0403  -0.3480 -0.1141 73  ASN A N   
471  C CA  . ASN A 64  ? 0.5257 0.9471 0.9724 0.0370  -0.3441 -0.1291 73  ASN A CA  
472  C C   . ASN A 64  ? 0.5353 0.9801 1.0204 0.0572  -0.3668 -0.1310 73  ASN A C   
473  O O   . ASN A 64  ? 0.5435 0.9688 1.0138 0.0740  -0.3718 -0.1194 73  ASN A O   
474  C CB  . ASN A 64  ? 0.4952 0.9192 0.9584 0.0296  -0.3100 -0.1307 73  ASN A CB  
475  C CG  . ASN A 64  ? 0.4751 0.9432 0.9997 0.0208  -0.3012 -0.1468 73  ASN A CG  
476  O OD1 . ASN A 64  ? 0.4719 0.9709 1.0428 0.0328  -0.3093 -0.1536 73  ASN A OD1 
477  N ND2 . ASN A 64  ? 0.4647 0.9360 0.9904 -0.0005 -0.2842 -0.1532 73  ASN A ND2 
478  N N   . PRO A 65  ? 0.5705 1.0564 1.1060 0.0561  -0.3820 -0.1458 74  PRO A N   
479  C CA  . PRO A 65  ? 0.5605 1.0597 1.1212 0.0749  -0.3983 -0.1444 74  PRO A CA  
480  C C   . PRO A 65  ? 0.6319 1.1372 1.2217 0.0898  -0.3846 -0.1434 74  PRO A C   
481  O O   . PRO A 65  ? 0.6977 1.1944 1.2878 0.1094  -0.3995 -0.1364 74  PRO A O   
482  C CB  . PRO A 65  ? 0.6079 1.1446 1.2094 0.0643  -0.4008 -0.1587 74  PRO A CB  
483  C CG  . PRO A 65  ? 0.5614 1.0913 1.1386 0.0425  -0.3986 -0.1631 74  PRO A CG  
484  C CD  . PRO A 65  ? 0.5880 1.0957 1.1409 0.0355  -0.3784 -0.1589 74  PRO A CD  
485  N N   . GLU A 66  ? 0.8094 1.3276 1.4220 0.0808  -0.3566 -0.1504 75  GLU A N   
486  C CA  . GLU A 66  ? 0.8519 1.3750 1.4892 0.0940  -0.3413 -0.1507 75  GLU A CA  
487  C C   . GLU A 66  ? 0.7566 1.2358 1.3477 0.1032  -0.3366 -0.1345 75  GLU A C   
488  O O   . GLU A 66  ? 0.6980 1.1752 1.3022 0.1119  -0.3203 -0.1343 75  GLU A O   
489  C CB  . GLU A 66  ? 0.8710 1.4237 1.5456 0.0789  -0.3100 -0.1637 75  GLU A CB  
490  C CG  . GLU A 66  ? 0.8157 1.4089 1.5349 0.0695  -0.3070 -0.1776 75  GLU A CG  
491  C CD  . GLU A 66  ? 0.8736 1.4894 1.6329 0.0874  -0.3096 -0.1836 75  GLU A CD  
492  O OE1 . GLU A 66  ? 0.8593 1.4604 1.6090 0.1074  -0.3328 -0.1767 75  GLU A OE1 
493  O OE2 . GLU A 66  ? 0.9115 1.5587 1.7103 0.0809  -0.2880 -0.1953 75  GLU A OE2 
494  N N   . CYS A 67  ? 0.6293 1.0705 1.1620 0.1002  -0.3471 -0.1204 76  CYS A N   
495  C CA  . CYS A 67  ? 0.7161 1.1118 1.1977 0.1052  -0.3388 -0.1031 76  CYS A CA  
496  C C   . CYS A 67  ? 0.7284 1.0973 1.1773 0.1204  -0.3689 -0.0891 76  CYS A C   
497  O O   . CYS A 67  ? 0.8174 1.1461 1.2141 0.1203  -0.3654 -0.0733 76  CYS A O   
498  C CB  . CYS A 67  ? 0.7095 1.0808 1.1457 0.0853  -0.3170 -0.0978 76  CYS A CB  
499  S SG  . CYS A 67  ? 0.6574 1.0561 1.1263 0.0650  -0.2847 -0.1123 76  CYS A SG  
500  N N   . GLU A 68  ? 0.8025 1.1932 1.2814 0.1331  -0.3988 -0.0944 77  GLU A N   
501  C CA  . GLU A 68  ? 0.8776 1.2407 1.3227 0.1470  -0.4282 -0.0797 77  GLU A CA  
502  C C   . GLU A 68  ? 0.7945 1.1252 1.2231 0.1628  -0.4277 -0.0658 77  GLU A C   
503  O O   . GLU A 68  ? 0.7899 1.0840 1.1712 0.1685  -0.4442 -0.0484 77  GLU A O   
504  C CB  . GLU A 68  ? 1.0129 1.3988 1.4877 0.1553  -0.4469 -0.0859 77  GLU A CB  
505  C CG  . GLU A 68  ? 1.0864 1.4984 1.5699 0.1401  -0.4530 -0.0971 77  GLU A CG  
506  C CD  . GLU A 68  ? 1.3222 1.7551 1.8332 0.1495  -0.4738 -0.1019 77  GLU A CD  
507  O OE1 . GLU A 68  ? 1.3934 1.8174 1.9128 0.1683  -0.4848 -0.0957 77  GLU A OE1 
508  O OE2 . GLU A 68  ? 1.3303 1.7877 1.8548 0.1380  -0.4795 -0.1122 77  GLU A OE2 
509  N N   . LEU A 69  ? 0.5975 0.9384 1.0602 0.1680  -0.4065 -0.0725 78  LEU A N   
510  C CA  . LEU A 69  ? 0.6657 0.9739 1.1129 0.1816  -0.4033 -0.0604 78  LEU A CA  
511  C C   . LEU A 69  ? 0.8095 1.0734 1.1920 0.1696  -0.3873 -0.0433 78  LEU A C   
512  O O   . LEU A 69  ? 0.9098 1.1387 1.2664 0.1789  -0.3906 -0.0291 78  LEU A O   
513  C CB  . LEU A 69  ? 0.7519 1.0828 1.2487 0.1878  -0.3813 -0.0740 78  LEU A CB  
514  C CG  . LEU A 69  ? 0.6780 1.0545 1.2359 0.1933  -0.3819 -0.0928 78  LEU A CG  
515  C CD1 . LEU A 69  ? 0.6847 1.0797 1.2827 0.1978  -0.3565 -0.1055 78  LEU A CD1 
516  C CD2 . LEU A 69  ? 0.7023 1.0712 1.2625 0.2094  -0.4084 -0.0877 78  LEU A CD2 
517  N N   . LEU A 70  ? 0.7459 1.0105 1.1032 0.1491  -0.3702 -0.0449 79  LEU A N   
518  C CA  . LEU A 70  ? 0.6374 0.8658 0.9391 0.1370  -0.3519 -0.0318 79  LEU A CA  
519  C C   . LEU A 70  ? 0.6298 0.8311 0.8758 0.1325  -0.3700 -0.0178 79  LEU A C   
520  O O   . LEU A 70  ? 0.7199 0.8914 0.9182 0.1231  -0.3565 -0.0065 79  LEU A O   
521  C CB  . LEU A 70  ? 0.5590 0.8013 0.8642 0.1180  -0.3222 -0.0419 79  LEU A CB  
522  C CG  . LEU A 70  ? 0.5795 0.8307 0.9118 0.1166  -0.2938 -0.0490 79  LEU A CG  
523  C CD1 . LEU A 70  ? 0.6669 0.9470 1.0570 0.1318  -0.2991 -0.0605 79  LEU A CD1 
524  C CD2 . LEU A 70  ? 0.5407 0.8076 0.8768 0.0972  -0.2710 -0.0588 79  LEU A CD2 
525  N N   . ILE A 71  ? 0.7604 0.9725 1.0112 0.1390  -0.4001 -0.0188 80  ILE A N   
526  C CA  . ILE A 71  ? 0.8441 1.0320 1.0392 0.1338  -0.4175 -0.0064 80  ILE A CA  
527  C C   . ILE A 71  ? 0.8896 1.0359 1.0438 0.1432  -0.4279 0.0150  80  ILE A C   
528  O O   . ILE A 71  ? 0.8904 1.0074 0.9869 0.1339  -0.4264 0.0283  80  ILE A O   
529  C CB  . ILE A 71  ? 1.0108 1.2234 1.2232 0.1378  -0.4482 -0.0145 80  ILE A CB  
530  C CG1 . ILE A 71  ? 1.0358 1.2913 1.2959 0.1279  -0.4372 -0.0363 80  ILE A CG1 
531  C CG2 . ILE A 71  ? 1.1453 1.3352 1.2967 0.1296  -0.4637 -0.0041 80  ILE A CG2 
532  C CD1 . ILE A 71  ? 1.0976 1.3823 1.3831 0.1311  -0.4668 -0.0467 80  ILE A CD1 
533  N N   . SER A 72  ? 1.0200 1.1624 1.2031 0.1611  -0.4380 0.0182  81  SER A N   
534  C CA  . SER A 72  ? 1.0466 1.1470 1.1930 0.1704  -0.4511 0.0392  81  SER A CA  
535  C C   . SER A 72  ? 0.9960 1.0658 1.1080 0.1605  -0.4229 0.0498  81  SER A C   
536  O O   . SER A 72  ? 1.0373 1.0687 1.1064 0.1618  -0.4302 0.0691  81  SER A O   
537  C CB  . SER A 72  ? 1.0773 1.1814 1.2679 0.1932  -0.4697 0.0378  81  SER A CB  
538  O OG  . SER A 72  ? 1.1125 1.2381 1.3531 0.1974  -0.4476 0.0232  81  SER A OG  
539  N N   . ARG A 73  ? 0.8143 0.8998 0.9434 0.1499  -0.3917 0.0382  82  ARG A N   
540  C CA  . ARG A 73  ? 0.8283 0.8883 0.9290 0.1406  -0.3651 0.0464  82  ARG A CA  
541  C C   . ARG A 73  ? 0.8923 0.9382 0.9388 0.1226  -0.3557 0.0534  82  ARG A C   
542  O O   . ARG A 73  ? 0.9081 0.9757 0.9575 0.1116  -0.3470 0.0414  82  ARG A O   
543  C CB  . ARG A 73  ? 0.7934 0.8756 0.9343 0.1377  -0.3372 0.0311  82  ARG A CB  
544  C CG  . ARG A 73  ? 0.8116 0.9092 1.0062 0.1549  -0.3421 0.0221  82  ARG A CG  
545  C CD  . ARG A 73  ? 0.8879 0.9501 1.0695 0.1673  -0.3506 0.0365  82  ARG A CD  
546  N NE  . ARG A 73  ? 0.8329 0.8651 0.9755 0.1557  -0.3290 0.0474  82  ARG A NE  
547  C CZ  . ARG A 73  ? 0.7485 0.7831 0.9056 0.1520  -0.3032 0.0405  82  ARG A CZ  
548  N NH1 . ARG A 73  ? 0.7096 0.7748 0.9169 0.1584  -0.2943 0.0229  82  ARG A NH1 
549  N NH2 . ARG A 73  ? 0.7959 0.8038 0.9174 0.1415  -0.2861 0.0507  82  ARG A NH2 
550  N N   . GLU A 74  ? 0.9405 0.9498 0.9379 0.1193  -0.3569 0.0721  83  GLU A N   
551  C CA  . GLU A 74  ? 0.8533 0.8490 0.7980 0.1025  -0.3461 0.0785  83  GLU A CA  
552  C C   . GLU A 74  ? 0.8884 0.8574 0.8048 0.0943  -0.3233 0.0895  83  GLU A C   
553  O O   . GLU A 74  ? 0.9529 0.9070 0.8225 0.0815  -0.3154 0.0973  83  GLU A O   
554  C CB  . GLU A 74  ? 0.8620 0.8425 0.7642 0.1028  -0.3730 0.0909  83  GLU A CB  
555  C CG  . GLU A 74  ? 1.0610 1.0699 0.9834 0.1066  -0.3942 0.0785  83  GLU A CG  
556  C CD  . GLU A 74  ? 1.1206 1.1147 0.9926 0.1034  -0.4176 0.0893  83  GLU A CD  
557  O OE1 . GLU A 74  ? 1.2428 1.2029 1.0682 0.1016  -0.4221 0.1090  83  GLU A OE1 
558  O OE2 . GLU A 74  ? 1.0314 1.0479 0.9094 0.1017  -0.4313 0.0780  83  GLU A OE2 
559  N N   . SER A 75  A 0.8765 0.8403 0.8205 0.1010  -0.3125 0.0891  83  SER A N   
560  C CA  . SER A 75  A 0.8403 0.7822 0.7632 0.0925  -0.2900 0.0971  83  SER A CA  
561  C C   . SER A 75  A 0.8450 0.7971 0.8126 0.0990  -0.2747 0.0867  83  SER A C   
562  O O   . SER A 75  A 0.9632 0.9226 0.9678 0.1138  -0.2873 0.0821  83  SER A O   
563  C CB  . SER A 75  A 0.8771 0.7801 0.7608 0.0933  -0.3019 0.1192  83  SER A CB  
564  O OG  . SER A 75  A 0.9335 0.8240 0.8439 0.1091  -0.3156 0.1235  83  SER A OG  
565  N N   . TRP A 76  ? 0.7011 0.6543 0.6650 0.0882  -0.2480 0.0824  84  TRP A N   
566  C CA  . TRP A 76  ? 0.7121 0.6759 0.7139 0.0924  -0.2317 0.0717  84  TRP A CA  
567  C C   . TRP A 76  ? 0.6416 0.5935 0.6236 0.0802  -0.2068 0.0742  84  TRP A C   
568  O O   . TRP A 76  ? 0.6728 0.6180 0.6197 0.0678  -0.1991 0.0793  84  TRP A O   
569  C CB  . TRP A 76  ? 0.6765 0.6770 0.7179 0.0937  -0.2268 0.0528  84  TRP A CB  
570  C CG  . TRP A 76  ? 0.6741 0.6877 0.6983 0.0799  -0.2172 0.0470  84  TRP A CG  
571  C CD1 . TRP A 76  ? 0.6398 0.6568 0.6573 0.0683  -0.1937 0.0415  84  TRP A CD1 
572  C CD2 . TRP A 76  ? 0.5986 0.6219 0.6096 0.0768  -0.2322 0.0455  84  TRP A CD2 
573  N NE1 . TRP A 76  ? 0.5749 0.6023 0.5770 0.0587  -0.1928 0.0363  84  TRP A NE1 
574  C CE2 . TRP A 76  ? 0.5812 0.6128 0.5786 0.0632  -0.2158 0.0382  84  TRP A CE2 
575  C CE3 . TRP A 76  ? 0.6281 0.6534 0.6376 0.0846  -0.2590 0.0490  84  TRP A CE3 
576  C CZ2 . TRP A 76  ? 0.6226 0.6640 0.6049 0.0569  -0.2245 0.0335  84  TRP A CZ2 
577  C CZ3 . TRP A 76  ? 0.6389 0.6751 0.6324 0.0777  -0.2680 0.0448  84  TRP A CZ3 
578  C CH2 . TRP A 76  ? 0.6210 0.6649 0.6009 0.0638  -0.2504 0.0366  84  TRP A CH2 
579  N N   . SER A 77  ? 0.7361 0.6870 0.7422 0.0841  -0.1944 0.0692  85  SER A N   
580  C CA  . SER A 77  ? 0.6992 0.6423 0.6933 0.0737  -0.1713 0.0694  85  SER A CA  
581  C C   . SER A 77  ? 0.6374 0.6061 0.6475 0.0667  -0.1531 0.0546  85  SER A C   
582  O O   . SER A 77  ? 0.6697 0.6349 0.6619 0.0558  -0.1366 0.0548  85  SER A O   
583  C CB  . SER A 77  ? 0.7171 0.6442 0.7261 0.0806  -0.1676 0.0712  85  SER A CB  
584  O OG  . SER A 77  ? 0.7282 0.6724 0.7792 0.0935  -0.1719 0.0590  85  SER A OG  
585  N N   . TYR A 78  ? 0.5327 0.5268 0.5764 0.0724  -0.1562 0.0420  86  TYR A N   
586  C CA  . TYR A 78  ? 0.4871 0.5041 0.5453 0.0649  -0.1409 0.0290  86  TYR A CA  
587  C C   . TYR A 78  ? 0.4800 0.5239 0.5721 0.0710  -0.1509 0.0180  86  TYR A C   
588  O O   . TYR A 78  ? 0.4966 0.5425 0.6037 0.0823  -0.1689 0.0194  86  TYR A O   
589  C CB  . TYR A 78  ? 0.4631 0.4794 0.5327 0.0626  -0.1209 0.0239  86  TYR A CB  
590  C CG  . TYR A 78  ? 0.5153 0.5339 0.6151 0.0743  -0.1224 0.0193  86  TYR A CG  
591  C CD1 . TYR A 78  ? 0.4800 0.4750 0.5730 0.0816  -0.1293 0.0281  86  TYR A CD1 
592  C CD2 . TYR A 78  ? 0.4394 0.4834 0.5743 0.0775  -0.1163 0.0055  86  TYR A CD2 
593  C CE1 . TYR A 78  ? 0.4792 0.4754 0.6006 0.0934  -0.1309 0.0221  86  TYR A CE1 
594  C CE2 . TYR A 78  ? 0.4380 0.4862 0.6009 0.0886  -0.1164 -0.0007 86  TYR A CE2 
595  C CZ  . TYR A 78  ? 0.4577 0.4817 0.6142 0.0973  -0.1241 0.0069  86  TYR A CZ  
596  O OH  . TYR A 78  ? 0.5789 0.6060 0.7640 0.1094  -0.1245 -0.0011 86  TYR A OH  
597  N N   . ILE A 79  ? 0.4569 0.5214 0.5623 0.0631  -0.1397 0.0070  87  ILE A N   
598  C CA  . ILE A 79  ? 0.4500 0.5424 0.5865 0.0648  -0.1472 -0.0041 87  ILE A CA  
599  C C   . ILE A 79  ? 0.4383 0.5500 0.6077 0.0636  -0.1308 -0.0158 87  ILE A C   
600  O O   . ILE A 79  ? 0.4966 0.6044 0.6571 0.0546  -0.1125 -0.0174 87  ILE A O   
601  C CB  . ILE A 79  ? 0.4528 0.5520 0.5735 0.0542  -0.1505 -0.0068 87  ILE A CB  
602  C CG1 . ILE A 79  ? 0.4965 0.5777 0.5819 0.0553  -0.1669 0.0043  87  ILE A CG1 
603  C CG2 . ILE A 79  ? 0.4452 0.5744 0.6008 0.0540  -0.1575 -0.0190 87  ILE A CG2 
604  C CD1 . ILE A 79  ? 0.5763 0.6617 0.6414 0.0453  -0.1701 0.0008  87  ILE A CD1 
605  N N   . VAL A 80  ? 0.4213 0.5545 0.6285 0.0726  -0.1376 -0.0241 88  VAL A N   
606  C CA  . VAL A 80  ? 0.3999 0.5559 0.6404 0.0712  -0.1223 -0.0364 88  VAL A CA  
607  C C   . VAL A 80  ? 0.3941 0.5808 0.6615 0.0658  -0.1266 -0.0469 88  VAL A C   
608  O O   . VAL A 80  ? 0.4066 0.6065 0.6916 0.0736  -0.1456 -0.0492 88  VAL A O   
609  C CB  . VAL A 80  ? 0.4188 0.5782 0.6855 0.0858  -0.1238 -0.0402 88  VAL A CB  
610  C CG1 . VAL A 80  ? 0.3824 0.5677 0.6813 0.0829  -0.1058 -0.0541 88  VAL A CG1 
611  C CG2 . VAL A 80  ? 0.4113 0.5381 0.6514 0.0901  -0.1210 -0.0298 88  VAL A CG2 
612  N N   . GLU A 81  ? 0.3775 0.5747 0.6480 0.0522  -0.1100 -0.0529 89  GLU A N   
613  C CA  . GLU A 81  ? 0.3711 0.5978 0.6696 0.0441  -0.1102 -0.0636 89  GLU A CA  
614  C C   . GLU A 81  ? 0.5838 0.8307 0.9102 0.0399  -0.0905 -0.0732 89  GLU A C   
615  O O   . GLU A 81  ? 0.6706 0.9036 0.9809 0.0354  -0.0733 -0.0705 89  GLU A O   
616  C CB  . GLU A 81  ? 0.3717 0.5904 0.6460 0.0293  -0.1088 -0.0619 89  GLU A CB  
617  C CG  . GLU A 81  ? 0.3631 0.6070 0.6628 0.0162  -0.1021 -0.0724 89  GLU A CG  
618  C CD  . GLU A 81  ? 0.3876 0.6194 0.6628 0.0024  -0.1020 -0.0713 89  GLU A CD  
619  O OE1 . GLU A 81  ? 0.3799 0.6150 0.6518 0.0019  -0.1190 -0.0727 89  GLU A OE1 
620  O OE2 . GLU A 81  ? 0.5574 0.7757 0.8162 -0.0074 -0.0859 -0.0694 89  GLU A OE2 
621  N N   . LYS A 82  ? 0.6117 0.8923 0.9796 0.0413  -0.0932 -0.0846 90  LYS A N   
622  C CA  . LYS A 82  ? 0.6273 0.9304 1.0218 0.0356  -0.0732 -0.0946 90  LYS A CA  
623  C C   . LYS A 82  ? 0.6250 0.9227 1.0021 0.0157  -0.0562 -0.0933 90  LYS A C   
624  O O   . LYS A 82  ? 0.5247 0.8142 0.8859 0.0061  -0.0629 -0.0899 90  LYS A O   
625  C CB  . LYS A 82  ? 0.7535 1.0975 1.1981 0.0394  -0.0792 -0.1081 90  LYS A CB  
626  C CG  . LYS A 82  ? 0.8560 1.2062 1.3226 0.0611  -0.0954 -0.1109 90  LYS A CG  
627  C CD  . LYS A 82  ? 0.9071 1.2387 1.3630 0.0716  -0.0852 -0.1085 90  LYS A CD  
628  C CE  . LYS A 82  ? 0.8740 1.1970 1.3390 0.0934  -0.1055 -0.1066 90  LYS A CE  
629  N NZ  . LYS A 82  ? 0.7731 1.1338 1.2896 0.1043  -0.1167 -0.1204 90  LYS A NZ  
630  N N   . PRO A 83  ? 0.7979 1.0980 1.1759 0.0094  -0.0349 -0.0959 91  PRO A N   
631  C CA  . PRO A 83  ? 0.8662 1.1543 1.2221 -0.0087 -0.0201 -0.0922 91  PRO A CA  
632  C C   . PRO A 83  ? 0.8368 1.1385 1.2037 -0.0237 -0.0235 -0.0957 91  PRO A C   
633  O O   . PRO A 83  ? 0.9173 1.1975 1.2571 -0.0337 -0.0243 -0.0897 91  PRO A O   
634  C CB  . PRO A 83  ? 0.9106 1.2101 1.2768 -0.0122 0.0013  -0.0974 91  PRO A CB  
635  C CG  . PRO A 83  ? 0.8918 1.1911 1.2662 0.0064  -0.0022 -0.0997 91  PRO A CG  
636  C CD  . PRO A 83  ? 0.8314 1.1418 1.2268 0.0191  -0.0242 -0.1020 91  PRO A CD  
637  N N   . ASN A 84  ? 0.7954 1.1325 1.2028 -0.0255 -0.0258 -0.1064 92  ASN A N   
638  C CA  . ASN A 84  ? 0.9833 1.3353 1.4054 -0.0392 -0.0324 -0.1110 92  ASN A CA  
639  C C   . ASN A 84  ? 0.9784 1.3578 1.4349 -0.0280 -0.0521 -0.1189 92  ASN A C   
640  O O   . ASN A 84  ? 1.0322 1.4460 1.5296 -0.0241 -0.0485 -0.1295 92  ASN A O   
641  C CB  . ASN A 84  ? 1.0401 1.4114 1.4800 -0.0584 -0.0129 -0.1167 92  ASN A CB  
642  C CG  . ASN A 84  ? 1.2651 1.6382 1.7073 -0.0762 -0.0180 -0.1182 92  ASN A CG  
643  O OD1 . ASN A 84  ? 1.3051 1.6508 1.7170 -0.0883 -0.0126 -0.1111 92  ASN A OD1 
644  N ND2 . ASN A 84  ? 1.2780 1.6829 1.7572 -0.0774 -0.0298 -0.1280 92  ASN A ND2 
645  N N   . PRO A 85  ? 0.7826 1.1484 1.2236 -0.0221 -0.0734 -0.1146 93  PRO A N   
646  C CA  . PRO A 85  ? 0.5989 0.9876 1.0690 -0.0098 -0.0954 -0.1208 93  PRO A CA  
647  C C   . PRO A 85  ? 0.5687 0.9940 1.0788 -0.0221 -0.0984 -0.1330 93  PRO A C   
648  O O   . PRO A 85  ? 0.5599 0.9867 1.0684 -0.0418 -0.0868 -0.1348 93  PRO A O   
649  C CB  . PRO A 85  ? 0.5948 0.9539 1.0274 -0.0039 -0.1152 -0.1113 93  PRO A CB  
650  C CG  . PRO A 85  ? 0.6769 0.9987 1.0642 -0.0082 -0.1014 -0.1004 93  PRO A CG  
651  C CD  . PRO A 85  ? 0.7066 1.0347 1.1009 -0.0246 -0.0787 -0.1039 93  PRO A CD  
652  N N   . GLU A 86  ? 0.5997 1.0546 1.1473 -0.0102 -0.1153 -0.1413 94  GLU A N   
653  C CA  . GLU A 86  ? 0.6771 1.1733 1.2710 -0.0200 -0.1197 -0.1548 94  GLU A CA  
654  C C   . GLU A 86  ? 0.6074 1.1028 1.1968 -0.0225 -0.1452 -0.1556 94  GLU A C   
655  O O   . GLU A 86  ? 0.6389 1.1480 1.2410 -0.0407 -0.1444 -0.1620 94  GLU A O   
656  C CB  . GLU A 86  ? 0.8148 1.3503 1.4601 -0.0050 -0.1223 -0.1665 94  GLU A CB  
657  C CG  . GLU A 86  ? 0.9295 1.4672 1.5798 -0.0005 -0.0982 -0.1678 94  GLU A CG  
658  C CD  . GLU A 86  ? 1.0437 1.5938 1.6999 -0.0234 -0.0698 -0.1718 94  GLU A CD  
659  O OE1 . GLU A 86  ? 1.0505 1.6235 1.7286 -0.0410 -0.0691 -0.1784 94  GLU A OE1 
660  O OE2 . GLU A 86  ? 0.9794 1.5154 1.6171 -0.0246 -0.0487 -0.1679 94  GLU A OE2 
661  N N   . ASN A 87  ? 0.4170 0.8954 0.9869 -0.0053 -0.1681 -0.1491 95  ASN A N   
662  C CA  . ASN A 87  ? 0.3957 0.8759 0.9619 -0.0047 -0.1954 -0.1507 95  ASN A CA  
663  C C   . ASN A 87  ? 0.4060 0.8419 0.9124 -0.0091 -0.1990 -0.1387 95  ASN A C   
664  O O   . ASN A 87  ? 0.4149 0.8236 0.8877 0.0048  -0.2083 -0.1278 95  ASN A O   
665  C CB  . ASN A 87  ? 0.4139 0.9086 1.0019 0.0179  -0.2205 -0.1523 95  ASN A CB  
666  C CG  . ASN A 87  ? 0.4310 0.9745 1.0840 0.0227  -0.2187 -0.1672 95  ASN A CG  
667  O OD1 . ASN A 87  ? 0.4731 1.0246 1.1457 0.0409  -0.2196 -0.1684 95  ASN A OD1 
668  N ND2 . ASN A 87  ? 0.4689 1.0457 1.1566 0.0058  -0.2158 -0.1796 95  ASN A ND2 
669  N N   . GLY A 88  A 0.4067 0.8357 0.9007 -0.0288 -0.1913 -0.1412 95  GLY A N   
670  C CA  . GLY A 88  A 0.4179 0.8091 0.8598 -0.0338 -0.1945 -0.1333 95  GLY A CA  
671  C C   . GLY A 88  A 0.4365 0.8330 0.8763 -0.0417 -0.2154 -0.1404 95  GLY A C   
672  O O   . GLY A 88  A 0.4562 0.8637 0.9025 -0.0307 -0.2399 -0.1422 95  GLY A O   
673  N N   . THR A 89  ? 0.4875 0.8745 0.9171 -0.0605 -0.2071 -0.1446 96  THR A N   
674  C CA  . THR A 89  ? 0.4578 0.8503 0.8878 -0.0704 -0.2257 -0.1537 96  THR A CA  
675  C C   . THR A 89  ? 0.5284 0.9647 1.0163 -0.0792 -0.2301 -0.1669 96  THR A C   
676  O O   . THR A 89  ? 0.4904 0.9366 0.9997 -0.0971 -0.2133 -0.1724 96  THR A O   
677  C CB  . THR A 89  ? 0.4643 0.8271 0.8617 -0.0864 -0.2155 -0.1539 96  THR A CB  
678  O OG1 . THR A 89  ? 0.6717 1.0355 1.0847 -0.1001 -0.1905 -0.1539 96  THR A OG1 
679  C CG2 . THR A 89  ? 0.4702 0.7942 0.8128 -0.0770 -0.2136 -0.1430 96  THR A CG2 
680  N N   . CYS A 90  ? 0.4622 0.9250 0.9759 -0.0670 -0.2531 -0.1719 97  CYS A N   
681  C CA  . CYS A 90  ? 0.4580 0.9678 1.0325 -0.0732 -0.2579 -0.1855 97  CYS A CA  
682  C C   . CYS A 90  ? 0.4706 0.9888 1.0556 -0.0948 -0.2645 -0.1969 97  CYS A C   
683  O O   . CYS A 90  ? 0.5807 1.1290 1.2096 -0.1106 -0.2544 -0.2068 97  CYS A O   
684  C CB  . CYS A 90  ? 0.4658 1.0003 1.0650 -0.0525 -0.2838 -0.1880 97  CYS A CB  
685  S SG  . CYS A 90  ? 0.4973 1.0078 1.0514 -0.0410 -0.3185 -0.1832 97  CYS A SG  
686  N N   . TYR A 91  ? 0.4914 0.9834 1.0366 -0.0969 -0.2807 -0.1964 98  TYR A N   
687  C CA  . TYR A 91  ? 0.5055 0.9962 1.0526 -0.1184 -0.2847 -0.2070 98  TYR A CA  
688  C C   . TYR A 91  ? 0.5026 0.9545 1.0129 -0.1313 -0.2616 -0.2008 98  TYR A C   
689  O O   . TYR A 91  ? 0.5063 0.9221 0.9671 -0.1219 -0.2593 -0.1910 98  TYR A O   
690  C CB  . TYR A 91  ? 0.5331 1.0173 1.0575 -0.1141 -0.3154 -0.2122 98  TYR A CB  
691  C CG  . TYR A 91  ? 0.5529 1.0513 1.0972 -0.1326 -0.3244 -0.2246 98  TYR A CG  
692  C CD1 . TYR A 91  ? 0.6643 1.1397 1.1909 -0.1526 -0.3166 -0.2302 98  TYR A CD1 
693  C CD2 . TYR A 91  ? 0.6555 1.1854 1.2318 -0.1293 -0.3386 -0.2287 98  TYR A CD2 
694  C CE1 . TYR A 91  ? 0.5850 1.0680 1.1250 -0.1695 -0.3229 -0.2391 98  TYR A CE1 
695  C CE2 . TYR A 91  ? 0.5899 1.1301 1.1808 -0.1464 -0.3450 -0.2380 98  TYR A CE2 
696  C CZ  . TYR A 91  ? 0.5984 1.1147 1.1708 -0.1668 -0.3371 -0.2430 98  TYR A CZ  
697  O OH  . TYR A 91  ? 0.8240 1.3486 1.4105 -0.1842 -0.3439 -0.2521 98  TYR A OH  
698  N N   . PRO A 92  ? 0.5639 1.0215 1.0966 -0.1527 -0.2446 -0.2059 99  PRO A N   
699  C CA  . PRO A 92  ? 0.5606 0.9812 1.0613 -0.1629 -0.2214 -0.1981 99  PRO A CA  
700  C C   . PRO A 92  ? 0.5717 0.9521 1.0231 -0.1646 -0.2302 -0.1983 99  PRO A C   
701  O O   . PRO A 92  ? 0.7755 1.1581 1.2218 -0.1660 -0.2525 -0.2077 99  PRO A O   
702  C CB  . PRO A 92  ? 0.6197 1.0582 1.1585 -0.1876 -0.2069 -0.2050 99  PRO A CB  
703  C CG  . PRO A 92  ? 0.7300 1.2074 1.3116 -0.1938 -0.2278 -0.2195 99  PRO A CG  
704  C CD  . PRO A 92  ? 0.6457 1.1441 1.2346 -0.1693 -0.2462 -0.2188 99  PRO A CD  
705  N N   . GLY A 93  ? 0.5104 0.8549 0.9257 -0.1641 -0.2125 -0.1888 100 GLY A N   
706  C CA  . GLY A 93  ? 0.5284 0.8343 0.8972 -0.1643 -0.2172 -0.1894 100 GLY A CA  
707  C C   . GLY A 93  ? 0.5170 0.7908 0.8505 -0.1563 -0.1980 -0.1766 100 GLY A C   
708  O O   . GLY A 93  ? 0.4962 0.7765 0.8401 -0.1516 -0.1817 -0.1673 100 GLY A O   
709  N N   . HIS A 94  ? 0.5322 0.7726 0.8247 -0.1548 -0.2005 -0.1776 101 HIS A N   
710  C CA  . HIS A 94  ? 0.5243 0.7338 0.7819 -0.1467 -0.1846 -0.1672 101 HIS A CA  
711  C C   . HIS A 94  ? 0.6020 0.8042 0.8261 -0.1281 -0.1937 -0.1625 101 HIS A C   
712  O O   . HIS A 94  ? 0.5483 0.7474 0.7539 -0.1258 -0.2110 -0.1701 101 HIS A O   
713  C CB  . HIS A 94  ? 0.5402 0.7163 0.7769 -0.1580 -0.1786 -0.1719 101 HIS A CB  
714  C CG  . HIS A 94  ? 0.6929 0.8385 0.8947 -0.1485 -0.1647 -0.1630 101 HIS A CG  
715  N ND1 . HIS A 94  ? 0.6276 0.7710 0.8322 -0.1444 -0.1467 -0.1506 101 HIS A ND1 
716  C CD2 . HIS A 94  ? 0.6801 0.7984 0.8447 -0.1422 -0.1665 -0.1659 101 HIS A CD2 
717  C CE1 . HIS A 94  ? 0.6646 0.7805 0.8364 -0.1362 -0.1389 -0.1458 101 HIS A CE1 
718  N NE2 . HIS A 94  ? 0.6833 0.7845 0.8315 -0.1346 -0.1501 -0.1551 101 HIS A NE2 
719  N N   . PHE A 95  ? 0.5088 0.7077 0.7239 -0.1158 -0.1819 -0.1500 102 PHE A N   
720  C CA  . PHE A 95  ? 0.5120 0.7007 0.6937 -0.0996 -0.1871 -0.1430 102 PHE A CA  
721  C C   . PHE A 95  ? 0.5160 0.6717 0.6604 -0.0986 -0.1750 -0.1407 102 PHE A C   
722  O O   . PHE A 95  ? 0.5509 0.6950 0.6946 -0.0986 -0.1571 -0.1334 102 PHE A O   
723  C CB  . PHE A 95  ? 0.4920 0.6948 0.6867 -0.0873 -0.1818 -0.1316 102 PHE A CB  
724  C CG  . PHE A 95  ? 0.5006 0.6998 0.6693 -0.0719 -0.1933 -0.1247 102 PHE A CG  
725  C CD1 . PHE A 95  ? 0.6573 0.8311 0.7820 -0.0676 -0.1920 -0.1218 102 PHE A CD1 
726  C CD2 . PHE A 95  ? 0.4984 0.7194 0.6870 -0.0620 -0.2054 -0.1212 102 PHE A CD2 
727  C CE1 . PHE A 95  ? 0.5248 0.6943 0.6235 -0.0556 -0.2016 -0.1141 102 PHE A CE1 
728  C CE2 . PHE A 95  ? 0.5108 0.7248 0.6734 -0.0487 -0.2170 -0.1131 102 PHE A CE2 
729  C CZ  . PHE A 95  ? 0.5246 0.7124 0.6409 -0.0464 -0.2146 -0.1089 102 PHE A CZ  
730  N N   . ALA A 96  ? 0.5388 0.6804 0.6527 -0.0976 -0.1850 -0.1479 103 ALA A N   
731  C CA  . ALA A 96  ? 0.5454 0.6583 0.6272 -0.0967 -0.1744 -0.1490 103 ALA A CA  
732  C C   . ALA A 96  ? 0.6149 0.7195 0.6741 -0.0837 -0.1638 -0.1364 103 ALA A C   
733  O O   . ALA A 96  ? 0.5376 0.6499 0.5837 -0.0744 -0.1721 -0.1307 103 ALA A O   
734  C CB  . ALA A 96  ? 0.5755 0.6784 0.6311 -0.0987 -0.1878 -0.1622 103 ALA A CB  
735  N N   . ASP A 97  ? 0.5861 0.6739 0.6406 -0.0837 -0.1464 -0.1318 104 ASP A N   
736  C CA  . ASP A 97  ? 0.5897 0.6681 0.6238 -0.0730 -0.1350 -0.1212 104 ASP A CA  
737  C C   . ASP A 97  ? 0.5295 0.6246 0.5756 -0.0651 -0.1360 -0.1094 104 ASP A C   
738  O O   . ASP A 97  ? 0.5612 0.6547 0.5868 -0.0558 -0.1380 -0.1023 104 ASP A O   
739  C CB  . ASP A 97  ? 0.5295 0.5955 0.5258 -0.0676 -0.1382 -0.1254 104 ASP A CB  
740  C CG  . ASP A 97  ? 0.5458 0.5942 0.5310 -0.0735 -0.1366 -0.1389 104 ASP A CG  
741  O OD1 . ASP A 97  ? 0.5463 0.5793 0.5313 -0.0736 -0.1234 -0.1381 104 ASP A OD1 
742  O OD2 . ASP A 97  ? 0.5689 0.6182 0.5455 -0.0775 -0.1495 -0.1507 104 ASP A OD2 
743  N N   . TYR A 98  ? 0.4796 0.5906 0.5600 -0.0693 -0.1343 -0.1079 105 TYR A N   
744  C CA  . TYR A 98  ? 0.4660 0.5943 0.5636 -0.0613 -0.1357 -0.0991 105 TYR A CA  
745  C C   . TYR A 98  ? 0.4518 0.5684 0.5358 -0.0527 -0.1219 -0.0878 105 TYR A C   
746  O O   . TYR A 98  ? 0.5323 0.6514 0.6080 -0.0427 -0.1263 -0.0801 105 TYR A O   
747  C CB  . TYR A 98  ? 0.4537 0.6027 0.5923 -0.0688 -0.1334 -0.1022 105 TYR A CB  
748  C CG  . TYR A 98  ? 0.4397 0.6086 0.6017 -0.0602 -0.1336 -0.0959 105 TYR A CG  
749  C CD1 . TYR A 98  ? 0.4481 0.6274 0.6089 -0.0495 -0.1497 -0.0935 105 TYR A CD1 
750  C CD2 . TYR A 98  ? 0.4210 0.5977 0.6061 -0.0627 -0.1184 -0.0930 105 TYR A CD2 
751  C CE1 . TYR A 98  ? 0.4376 0.6336 0.6217 -0.0403 -0.1510 -0.0889 105 TYR A CE1 
752  C CE2 . TYR A 98  ? 0.4396 0.6349 0.6474 -0.0540 -0.1182 -0.0895 105 TYR A CE2 
753  C CZ  . TYR A 98  ? 0.5269 0.7316 0.7356 -0.0423 -0.1348 -0.0878 105 TYR A CZ  
754  O OH  . TYR A 98  ? 0.5056 0.7273 0.7386 -0.0322 -0.1358 -0.0853 105 TYR A OH  
755  N N   . GLU A 99  ? 0.5820 0.6845 0.6628 -0.0568 -0.1063 -0.0867 106 GLU A N   
756  C CA  . GLU A 99  ? 0.4284 0.5205 0.4983 -0.0497 -0.0933 -0.0771 106 GLU A CA  
757  C C   . GLU A 99  ? 0.4388 0.5179 0.4754 -0.0424 -0.0950 -0.0737 106 GLU A C   
758  O O   . GLU A 99  ? 0.4323 0.5092 0.4614 -0.0347 -0.0909 -0.0645 106 GLU A O   
759  C CB  . GLU A 99  ? 0.4196 0.4988 0.4923 -0.0562 -0.0787 -0.0773 106 GLU A CB  
760  C CG  . GLU A 99  ? 0.4120 0.5031 0.5147 -0.0656 -0.0742 -0.0792 106 GLU A CG  
761  C CD  . GLU A 99  ? 0.4299 0.5251 0.5437 -0.0770 -0.0828 -0.0892 106 GLU A CD  
762  O OE1 . GLU A 99  ? 0.4905 0.5703 0.5857 -0.0793 -0.0878 -0.0954 106 GLU A OE1 
763  O OE2 . GLU A 99  ? 0.4342 0.5486 0.5764 -0.0839 -0.0845 -0.0919 106 GLU A OE2 
764  N N   . GLU A 100 ? 0.4569 0.5274 0.4733 -0.0454 -0.1004 -0.0814 107 GLU A N   
765  C CA  . GLU A 100 ? 0.4704 0.5317 0.4542 -0.0398 -0.1012 -0.0793 107 GLU A CA  
766  C C   . GLU A 100 ? 0.4810 0.5513 0.4573 -0.0338 -0.1137 -0.0726 107 GLU A C   
767  O O   . GLU A 100 ? 0.4856 0.5494 0.4410 -0.0283 -0.1110 -0.0641 107 GLU A O   
768  C CB  . GLU A 100 ? 0.4904 0.5427 0.4553 -0.0443 -0.1045 -0.0916 107 GLU A CB  
769  C CG  . GLU A 100 ? 0.4851 0.5223 0.4489 -0.0469 -0.0919 -0.0968 107 GLU A CG  
770  C CD  . GLU A 100 ? 0.5201 0.5492 0.4693 -0.0405 -0.0789 -0.0899 107 GLU A CD  
771  O OE1 . GLU A 100 ? 0.5415 0.5714 0.4680 -0.0363 -0.0797 -0.0869 107 GLU A OE1 
772  O OE2 . GLU A 100 ? 0.5934 0.6154 0.5535 -0.0405 -0.0682 -0.0871 107 GLU A OE2 
773  N N   . LEU A 101 ? 0.4877 0.5725 0.4811 -0.0353 -0.1283 -0.0760 108 LEU A N   
774  C CA  . LEU A 101 ? 0.4991 0.5919 0.4880 -0.0284 -0.1428 -0.0689 108 LEU A CA  
775  C C   . LEU A 101 ? 0.5079 0.6029 0.5112 -0.0207 -0.1373 -0.0573 108 LEU A C   
776  O O   . LEU A 101 ? 0.5475 0.6370 0.5340 -0.0137 -0.1426 -0.0474 108 LEU A O   
777  C CB  . LEU A 101 ? 0.5124 0.6226 0.5216 -0.0311 -0.1606 -0.0766 108 LEU A CB  
778  C CG  . LEU A 101 ? 0.5254 0.6435 0.5302 -0.0230 -0.1795 -0.0700 108 LEU A CG  
779  C CD1 . LEU A 101 ? 0.5525 0.6550 0.5113 -0.0207 -0.1842 -0.0650 108 LEU A CD1 
780  C CD2 . LEU A 101 ? 0.5344 0.6723 0.5628 -0.0258 -0.1980 -0.0793 108 LEU A CD2 
781  N N   . ARG A 102 ? 0.4768 0.5787 0.5098 -0.0225 -0.1268 -0.0584 109 ARG A N   
782  C CA  . ARG A 102 ? 0.4586 0.5610 0.5039 -0.0154 -0.1193 -0.0494 109 ARG A CA  
783  C C   . ARG A 102 ? 0.4723 0.5558 0.4895 -0.0122 -0.1089 -0.0409 109 ARG A C   
784  O O   . ARG A 102 ? 0.4650 0.5438 0.4760 -0.0050 -0.1111 -0.0313 109 ARG A O   
785  C CB  . ARG A 102 ? 0.4334 0.5449 0.5094 -0.0199 -0.1070 -0.0533 109 ARG A CB  
786  C CG  . ARG A 102 ? 0.4307 0.5646 0.5397 -0.0241 -0.1151 -0.0614 109 ARG A CG  
787  C CD  . ARG A 102 ? 0.6182 0.7598 0.7528 -0.0308 -0.1002 -0.0645 109 ARG A CD  
788  N NE  . ARG A 102 ? 0.5103 0.6499 0.6501 -0.0238 -0.0891 -0.0577 109 ARG A NE  
789  C CZ  . ARG A 102 ? 0.5742 0.7313 0.7411 -0.0178 -0.0901 -0.0578 109 ARG A CZ  
790  N NH1 . ARG A 102 ? 0.6162 0.7961 0.8099 -0.0176 -0.1019 -0.0642 109 ARG A NH1 
791  N NH2 . ARG A 102 ? 0.6045 0.7572 0.7732 -0.0117 -0.0797 -0.0528 109 ARG A NH2 
792  N N   . GLU A 103 ? 0.4790 0.5514 0.4802 -0.0177 -0.0980 -0.0448 110 GLU A N   
793  C CA  . GLU A 103 ? 0.4891 0.5468 0.4667 -0.0155 -0.0874 -0.0383 110 GLU A CA  
794  C C   . GLU A 103 ? 0.4663 0.5181 0.4143 -0.0127 -0.0960 -0.0323 110 GLU A C   
795  O O   . GLU A 103 ? 0.4968 0.5400 0.4317 -0.0093 -0.0915 -0.0226 110 GLU A O   
796  C CB  . GLU A 103 ? 0.4750 0.5241 0.4439 -0.0209 -0.0760 -0.0457 110 GLU A CB  
797  C CG  . GLU A 103 ? 0.6241 0.6620 0.5781 -0.0189 -0.0629 -0.0406 110 GLU A CG  
798  C CD  . GLU A 103 ? 0.6008 0.6378 0.5734 -0.0170 -0.0529 -0.0356 110 GLU A CD  
799  O OE1 . GLU A 103 ? 0.6428 0.6883 0.6391 -0.0174 -0.0547 -0.0362 110 GLU A OE1 
800  O OE2 . GLU A 103 ? 0.6406 0.6697 0.6043 -0.0155 -0.0430 -0.0319 110 GLU A OE2 
801  N N   . GLN A 104 ? 0.4868 0.5423 0.4225 -0.0150 -0.1086 -0.0379 111 GLN A N   
802  C CA  . GLN A 104 ? 0.5148 0.5644 0.4188 -0.0133 -0.1181 -0.0315 111 GLN A CA  
803  C C   . GLN A 104 ? 0.5204 0.5701 0.4301 -0.0060 -0.1287 -0.0191 111 GLN A C   
804  O O   . GLN A 104 ? 0.5603 0.5984 0.4470 -0.0040 -0.1282 -0.0079 111 GLN A O   
805  C CB  . GLN A 104 ? 0.5371 0.5919 0.4286 -0.0171 -0.1316 -0.0411 111 GLN A CB  
806  C CG  . GLN A 104 ? 0.6524 0.7036 0.5328 -0.0234 -0.1227 -0.0542 111 GLN A CG  
807  C CD  . GLN A 104 ? 0.5562 0.5972 0.4003 -0.0246 -0.1136 -0.0526 111 GLN A CD  
808  O OE1 . GLN A 104 ? 0.5697 0.6056 0.3934 -0.0224 -0.1147 -0.0407 111 GLN A OE1 
809  N NE2 . GLN A 104 ? 0.6027 0.6404 0.4389 -0.0283 -0.1044 -0.0649 111 GLN A NE2 
810  N N   . LEU A 105 ? 0.5109 0.5737 0.4524 -0.0023 -0.1386 -0.0214 112 LEU A N   
811  C CA  . LEU A 105 ? 0.5171 0.5807 0.4687 0.0065  -0.1502 -0.0115 112 LEU A CA  
812  C C   . LEU A 105 ? 0.5010 0.5558 0.4609 0.0108  -0.1376 -0.0033 112 LEU A C   
813  O O   . LEU A 105 ? 0.5115 0.5599 0.4718 0.0182  -0.1459 0.0066  112 LEU A O   
814  C CB  . LEU A 105 ? 0.5100 0.5939 0.4984 0.0098  -0.1629 -0.0186 112 LEU A CB  
815  C CG  . LEU A 105 ? 0.6322 0.7258 0.6152 0.0072  -0.1812 -0.0256 112 LEU A CG  
816  C CD1 . LEU A 105 ? 0.5180 0.6357 0.5444 0.0081  -0.1895 -0.0353 112 LEU A CD1 
817  C CD2 . LEU A 105 ? 0.5648 0.6486 0.5192 0.0130  -0.1996 -0.0151 112 LEU A CD2 
818  N N   . SER A 106 ? 0.4783 0.5314 0.4445 0.0064  -0.1189 -0.0073 113 SER A N   
819  C CA  . SER A 106 ? 0.5763 0.6208 0.5485 0.0097  -0.1072 -0.0005 113 SER A CA  
820  C C   . SER A 106 ? 0.5194 0.5458 0.4602 0.0098  -0.1054 0.0111  113 SER A C   
821  O O   . SER A 106 ? 0.6137 0.6313 0.5589 0.0136  -0.1010 0.0185  113 SER A O   
822  C CB  . SER A 106 ? 0.4881 0.5343 0.4712 0.0047  -0.0893 -0.0074 113 SER A CB  
823  O OG  . SER A 106 ? 0.5413 0.6023 0.5566 0.0047  -0.0884 -0.0148 113 SER A OG  
824  N N   . SER A 107 ? 0.5619 0.5827 0.4709 0.0048  -0.1082 0.0123  114 SER A N   
825  C CA  . SER A 107 ? 0.6248 0.6298 0.5015 0.0024  -0.1051 0.0234  114 SER A CA  
826  C C   . SER A 107 ? 0.6961 0.6941 0.5495 0.0044  -0.1234 0.0328  114 SER A C   
827  O O   . SER A 107 ? 0.7724 0.7596 0.5904 -0.0008 -0.1223 0.0400  114 SER A O   
828  C CB  . SER A 107 ? 0.7038 0.7079 0.5590 -0.0057 -0.0908 0.0176  114 SER A CB  
829  O OG  . SER A 107 ? 0.7326 0.7442 0.5766 -0.0089 -0.0971 0.0080  114 SER A OG  
830  N N   . VAL A 108 ? 0.6592 0.6638 0.5321 0.0119  -0.1406 0.0329  115 VAL A N   
831  C CA  . VAL A 108 ? 0.6298 0.6278 0.4835 0.0155  -0.1617 0.0418  115 VAL A CA  
832  C C   . VAL A 108 ? 0.6356 0.6215 0.5006 0.0246  -0.1702 0.0539  115 VAL A C   
833  O O   . VAL A 108 ? 0.5834 0.5778 0.4858 0.0318  -0.1694 0.0493  115 VAL A O   
834  C CB  . VAL A 108 ? 0.6103 0.6258 0.4787 0.0179  -0.1781 0.0316  115 VAL A CB  
835  C CG1 . VAL A 108 ? 0.6401 0.6487 0.4910 0.0234  -0.2026 0.0414  115 VAL A CG1 
836  C CG2 . VAL A 108 ? 0.6357 0.6593 0.4899 0.0087  -0.1707 0.0192  115 VAL A CG2 
837  N N   . SER A 109 ? 0.6683 0.6334 0.5002 0.0238  -0.1781 0.0693  116 SER A N   
838  C CA  . SER A 109 ? 0.7486 0.6967 0.5871 0.0324  -0.1883 0.0821  116 SER A CA  
839  C C   . SER A 109 ? 0.8030 0.7490 0.6422 0.0421  -0.2161 0.0877  116 SER A C   
840  O O   . SER A 109 ? 0.8844 0.8230 0.7448 0.0533  -0.2274 0.0930  116 SER A O   
841  C CB  . SER A 109 ? 0.8675 0.7902 0.6702 0.0249  -0.1800 0.0975  116 SER A CB  
842  O OG  . SER A 109 ? 0.9883 0.9036 0.7462 0.0163  -0.1847 0.1044  116 SER A OG  
843  N N   . SER A 110 ? 0.7070 0.6594 0.5244 0.0388  -0.2282 0.0857  117 SER A N   
844  C CA  . SER A 110 ? 0.7378 0.6895 0.5537 0.0477  -0.2569 0.0906  117 SER A CA  
845  C C   . SER A 110 ? 0.7517 0.7162 0.5460 0.0410  -0.2644 0.0827  117 SER A C   
846  O O   . SER A 110 ? 0.7488 0.7147 0.5180 0.0293  -0.2482 0.0780  117 SER A O   
847  C CB  . SER A 110 ? 0.9397 0.8599 0.7226 0.0503  -0.2709 0.1121  117 SER A CB  
848  O OG  . SER A 110 ? 1.0903 0.9948 0.8207 0.0367  -0.2623 0.1216  117 SER A OG  
849  N N   . PHE A 111 ? 0.7943 0.7687 0.5997 0.0491  -0.2898 0.0803  118 PHE A N   
850  C CA  . PHE A 111 ? 0.8307 0.8134 0.6097 0.0429  -0.3010 0.0744  118 PHE A CA  
851  C C   . PHE A 111 ? 0.9389 0.9178 0.7109 0.0525  -0.3346 0.0822  118 PHE A C   
852  O O   . PHE A 111 ? 0.8779 0.8519 0.6744 0.0655  -0.3495 0.0894  118 PHE A O   
853  C CB  . PHE A 111 ? 0.8315 0.8430 0.6409 0.0383  -0.2916 0.0526  118 PHE A CB  
854  C CG  . PHE A 111 ? 0.7323 0.7671 0.6009 0.0477  -0.2975 0.0418  118 PHE A CG  
855  C CD1 . PHE A 111 ? 0.7683 0.8040 0.6602 0.0616  -0.3191 0.0478  118 PHE A CD1 
856  C CD2 . PHE A 111 ? 0.6834 0.7394 0.5845 0.0424  -0.2809 0.0251  118 PHE A CD2 
857  C CE1 . PHE A 111 ? 0.7232 0.7839 0.6710 0.0698  -0.3227 0.0362  118 PHE A CE1 
858  C CE2 . PHE A 111 ? 0.6567 0.7358 0.6108 0.0490  -0.2841 0.0151  118 PHE A CE2 
859  C CZ  . PHE A 111 ? 0.7904 0.8736 0.7688 0.0627  -0.3042 0.0199  118 PHE A CZ  
860  N N   . GLU A 112 ? 0.9697 0.9506 0.7073 0.0464  -0.3471 0.0800  119 GLU A N   
861  C CA  . GLU A 112 ? 1.0515 1.0297 0.7759 0.0540  -0.3809 0.0864  119 GLU A CA  
862  C C   . GLU A 112 ? 1.0003 1.0097 0.7537 0.0545  -0.3926 0.0664  119 GLU A C   
863  O O   . GLU A 112 ? 0.8863 0.9052 0.6231 0.0431  -0.3823 0.0540  119 GLU A O   
864  C CB  . GLU A 112 ? 1.2984 1.2518 0.9527 0.0452  -0.3876 0.1011  119 GLU A CB  
865  C CG  . GLU A 112 ? 1.5177 1.4417 1.1379 0.0392  -0.3704 0.1195  119 GLU A CG  
866  C CD  . GLU A 112 ? 1.6776 1.5860 1.2300 0.0248  -0.3651 0.1274  119 GLU A CD  
867  O OE1 . GLU A 112 ? 1.6627 1.5735 1.1857 0.0233  -0.3853 0.1259  119 GLU A OE1 
868  O OE2 . GLU A 112 ? 1.6594 1.5548 1.1884 0.0145  -0.3403 0.1339  119 GLU A OE2 
869  N N   . ARG A 113 ? 0.9455 0.9711 0.7431 0.0677  -0.4141 0.0623  120 ARG A N   
870  C CA  . ARG A 113 ? 0.8938 0.9508 0.7233 0.0679  -0.4275 0.0436  120 ARG A CA  
871  C C   . ARG A 113 ? 1.0300 1.0828 0.8263 0.0703  -0.4608 0.0484  120 ARG A C   
872  O O   . ARG A 113 ? 1.1105 1.1473 0.8954 0.0815  -0.4845 0.0640  120 ARG A O   
873  C CB  . ARG A 113 ? 0.8397 0.9220 0.7391 0.0799  -0.4319 0.0342  120 ARG A CB  
874  C CG  . ARG A 113 ? 0.8288 0.9462 0.7666 0.0794  -0.4460 0.0148  120 ARG A CG  
875  C CD  . ARG A 113 ? 0.7920 0.9369 0.8003 0.0894  -0.4447 0.0047  120 ARG A CD  
876  N NE  . ARG A 113 ? 0.8134 0.9938 0.8621 0.0893  -0.4611 -0.0128 120 ARG A NE  
877  C CZ  . ARG A 113 ? 0.9960 1.1897 1.0643 0.1015  -0.4939 -0.0133 120 ARG A CZ  
878  N NH1 . ARG A 113 ? 0.9855 1.1565 1.0342 0.1145  -0.5096 0.0040  120 ARG A NH1 
879  N NH2 . ARG A 113 ? 1.0658 1.2939 1.1731 0.0988  -0.5037 -0.0304 120 ARG A NH2 
880  N N   . PHE A 114 ? 0.9353 1.0006 0.7148 0.0599  -0.4634 0.0348  121 PHE A N   
881  C CA  . PHE A 114 ? 0.9930 1.0559 0.7376 0.0602  -0.4938 0.0369  121 PHE A CA  
882  C C   . PHE A 114 ? 1.0192 1.1115 0.7852 0.0527  -0.4978 0.0134  121 PHE A C   
883  O O   . PHE A 114 ? 0.9409 1.0421 0.7164 0.0419  -0.4736 -0.0007 121 PHE A O   
884  C CB  . PHE A 114 ? 1.0703 1.1032 0.7395 0.0506  -0.4869 0.0514  121 PHE A CB  
885  C CG  . PHE A 114 ? 1.0778 1.1099 0.7192 0.0349  -0.4610 0.0400  121 PHE A CG  
886  C CD1 . PHE A 114 ? 1.1993 1.2235 0.8456 0.0298  -0.4273 0.0421  121 PHE A CD1 
887  C CD2 . PHE A 114 ? 1.0650 1.1054 0.6786 0.0256  -0.4678 0.0261  121 PHE A CD2 
888  C CE1 . PHE A 114 ? 1.1006 1.1259 0.7264 0.0167  -0.4015 0.0306  121 PHE A CE1 
889  C CE2 . PHE A 114 ? 1.1739 1.2143 0.7662 0.0123  -0.4412 0.0139  121 PHE A CE2 
890  C CZ  . PHE A 114 ? 1.0495 1.0826 0.6487 0.0084  -0.4082 0.0163  121 PHE A CZ  
891  N N   . GLU A 115 ? 1.0002 1.1084 0.7786 0.0570  -0.5190 0.0097  122 GLU A N   
892  C CA  . GLU A 115 ? 1.0811 1.2168 0.8803 0.0490  -0.5244 -0.0122 122 GLU A CA  
893  C C   . GLU A 115 ? 1.0723 1.1951 0.8100 0.0355  -0.5200 -0.0160 122 GLU A C   
894  O O   . GLU A 115 ? 1.1414 1.2522 0.8352 0.0358  -0.5319 -0.0058 122 GLU A O   
895  C CB  . GLU A 115 ? 1.0103 1.1689 0.8466 0.0581  -0.5485 -0.0153 122 GLU A CB  
896  C CG  . GLU A 115 ? 1.1843 1.3251 0.9882 0.0677  -0.5676 0.0041  122 GLU A CG  
897  C CD  . GLU A 115 ? 1.2056 1.3713 1.0484 0.0765  -0.5920 -0.0015 122 GLU A CD  
898  O OE1 . GLU A 115 ? 1.0579 1.2557 0.9523 0.0738  -0.5925 -0.0205 122 GLU A OE1 
899  O OE2 . GLU A 115 ? 1.2076 1.3607 1.0298 0.0857  -0.6104 0.0132  122 GLU A OE2 
900  N N   . ILE A 116 ? 1.0543 1.1798 0.7890 0.0238  -0.5022 -0.0315 123 ILE A N   
901  C CA  . ILE A 116 ? 1.1366 1.2497 0.8142 0.0113  -0.4942 -0.0376 123 ILE A CA  
902  C C   . ILE A 116 ? 1.2086 1.3400 0.8866 0.0064  -0.5108 -0.0519 123 ILE A C   
903  O O   . ILE A 116 ? 1.2054 1.3272 0.8314 0.0009  -0.5144 -0.0507 123 ILE A O   
904  C CB  . ILE A 116 ? 1.0823 1.1917 0.7613 0.0016  -0.4662 -0.0500 123 ILE A CB  
905  C CG1 . ILE A 116 ? 1.3119 1.4083 0.9317 -0.0102 -0.4573 -0.0583 123 ILE A CG1 
906  C CG2 . ILE A 116 ? 0.9828 1.1189 0.7268 -0.0012 -0.4607 -0.0694 123 ILE A CG2 
907  C CD1 . ILE A 116 ? 1.0057 1.1003 0.6330 -0.0190 -0.4227 -0.0703 123 ILE A CD1 
908  N N   . PHE A 117 ? 1.3010 1.4601 1.0379 0.0077  -0.5205 -0.0658 124 PHE A N   
909  C CA  . PHE A 117 ? 1.1673 1.3463 0.9131 0.0027  -0.5376 -0.0799 124 PHE A CA  
910  C C   . PHE A 117 ? 1.0698 1.2708 0.8683 0.0141  -0.5575 -0.0761 124 PHE A C   
911  O O   . PHE A 117 ? 1.0136 1.2381 0.8732 0.0144  -0.5550 -0.0871 124 PHE A O   
912  C CB  . PHE A 117 ? 1.2019 1.3938 0.9692 -0.0106 -0.5266 -0.1043 124 PHE A CB  
913  C CG  . PHE A 117 ? 1.2699 1.4410 0.9866 -0.0210 -0.5078 -0.1111 124 PHE A CG  
914  C CD1 . PHE A 117 ? 1.4476 1.6002 1.0985 -0.0228 -0.5084 -0.1028 124 PHE A CD1 
915  C CD2 . PHE A 117 ? 1.1045 1.2754 0.8404 -0.0289 -0.4885 -0.1262 124 PHE A CD2 
916  C CE1 . PHE A 117 ? 1.4186 1.5548 1.0250 -0.0319 -0.4892 -0.1107 124 PHE A CE1 
917  C CE2 . PHE A 117 ? 1.0861 1.2381 0.7774 -0.0370 -0.4709 -0.1338 124 PHE A CE2 
918  C CZ  . PHE A 117 ? 1.1605 1.2962 0.7879 -0.0384 -0.4707 -0.1266 124 PHE A CZ  
919  N N   . PRO A 118 ? 1.1153 1.3100 0.8924 0.0234  -0.5766 -0.0608 125 PRO A N   
920  C CA  . PRO A 118 ? 1.1096 1.3230 0.9367 0.0367  -0.5952 -0.0562 125 PRO A CA  
921  C C   . PRO A 118 ? 1.0842 1.3323 0.9615 0.0319  -0.6060 -0.0763 125 PRO A C   
922  O O   . PRO A 118 ? 1.1005 1.3546 0.9609 0.0194  -0.6082 -0.0904 125 PRO A O   
923  C CB  . PRO A 118 ? 1.1528 1.3486 0.9342 0.0448  -0.6144 -0.0376 125 PRO A CB  
924  C CG  . PRO A 118 ? 1.1724 1.3361 0.8855 0.0383  -0.5991 -0.0265 125 PRO A CG  
925  C CD  . PRO A 118 ? 1.1480 1.3165 0.8539 0.0229  -0.5803 -0.0459 125 PRO A CD  
926  N N   . LYS A 119 A 1.0923 1.3635 1.0329 0.0416  -0.6118 -0.0779 125 LYS A N   
927  C CA  . LYS A 119 A 1.1092 1.4160 1.1043 0.0367  -0.6202 -0.0964 125 LYS A CA  
928  C C   . LYS A 119 A 1.2260 1.5399 1.2006 0.0354  -0.6454 -0.0989 125 LYS A C   
929  O O   . LYS A 119 A 1.1557 1.4876 1.1427 0.0231  -0.6492 -0.1162 125 LYS A O   
930  C CB  . LYS A 119 A 1.0954 1.4257 1.1588 0.0491  -0.6212 -0.0961 125 LYS A CB  
931  C CG  . LYS A 119 A 1.0961 1.4657 1.2227 0.0424  -0.6236 -0.1156 125 LYS A CG  
932  C CD  . LYS A 119 A 1.0472 1.4399 1.2389 0.0550  -0.6207 -0.1153 125 LYS A CD  
933  C CE  . LYS A 119 A 0.9646 1.3981 1.2200 0.0466  -0.6199 -0.1346 125 LYS A CE  
934  N NZ  . LYS A 119 A 1.0752 1.5327 1.3937 0.0578  -0.6124 -0.1359 125 LYS A NZ  
935  N N   . GLU A 120 B 1.3594 1.6580 1.3020 0.0475  -0.6632 -0.0816 125 GLU A N   
936  C CA  . GLU A 120 B 1.4956 1.7984 1.4124 0.0469  -0.6882 -0.0821 125 GLU A CA  
937  C C   . GLU A 120 B 1.4839 1.7527 1.3209 0.0467  -0.6915 -0.0659 125 GLU A C   
938  O O   . GLU A 120 B 1.5048 1.7531 1.3216 0.0591  -0.6967 -0.0456 125 GLU A O   
939  C CB  . GLU A 120 B 1.5989 1.9213 1.5592 0.0624  -0.7119 -0.0778 125 GLU A CB  
940  C CG  . GLU A 120 B 1.6375 2.0000 1.6747 0.0604  -0.7126 -0.0965 125 GLU A CG  
941  C CD  . GLU A 120 B 1.6447 2.0157 1.7337 0.0666  -0.6929 -0.0969 125 GLU A CD  
942  O OE1 . GLU A 120 B 1.6607 2.0069 1.7304 0.0762  -0.6840 -0.0810 125 GLU A OE1 
943  O OE2 . GLU A 120 B 1.6306 2.0334 1.7793 0.0613  -0.6858 -0.1130 125 GLU A OE2 
944  N N   . SER A 121 C 1.3960 1.6585 1.1876 0.0322  -0.6876 -0.0751 125 SER A N   
945  C CA  . SER A 121 C 1.3937 1.6768 1.2087 0.0170  -0.6813 -0.0993 125 SER A CA  
946  C C   . SER A 121 C 1.3179 1.5816 1.0774 0.0025  -0.6636 -0.1064 125 SER A C   
947  O O   . SER A 121 C 1.4566 1.7123 1.1650 -0.0030 -0.6726 -0.1074 125 SER A O   
948  C CB  . SER A 121 C 1.5065 1.8142 1.3385 0.0152  -0.7073 -0.1100 125 SER A CB  
949  O OG  . SER A 121 C 1.5362 1.8624 1.3935 -0.0004 -0.7011 -0.1331 125 SER A OG  
950  N N   . SER A 122 ? 1.2199 1.4765 0.9897 -0.0033 -0.6381 -0.1119 126 SER A N   
951  C CA  . SER A 122 ? 1.2198 1.4618 0.9478 -0.0174 -0.6200 -0.1232 126 SER A CA  
952  C C   . SER A 122 ? 1.3100 1.5701 1.0610 -0.0315 -0.6216 -0.1480 126 SER A C   
953  O O   . SER A 122 ? 1.4315 1.6802 1.1444 -0.0432 -0.6116 -0.1598 126 SER A O   
954  C CB  . SER A 122 ? 1.1887 1.4151 0.9191 -0.0178 -0.5929 -0.1200 126 SER A CB  
955  O OG  . SER A 122 ? 1.1749 1.3809 0.8781 -0.0067 -0.5898 -0.0971 126 SER A OG  
956  N N   . TRP A 123 ? 1.2034 1.4911 1.0160 -0.0310 -0.6332 -0.1564 127 TRP A N   
957  C CA  . TRP A 123 ? 1.2466 1.5520 1.0881 -0.0454 -0.6346 -0.1792 127 TRP A CA  
958  C C   . TRP A 123 ? 1.2206 1.5505 1.0854 -0.0428 -0.6627 -0.1820 127 TRP A C   
959  O O   . TRP A 123 ? 1.1964 1.5524 1.1239 -0.0402 -0.6688 -0.1860 127 TRP A O   
960  C CB  . TRP A 123 ? 1.2462 1.5632 1.1469 -0.0504 -0.6163 -0.1885 127 TRP A CB  
961  C CG  . TRP A 123 ? 1.1475 1.4465 1.0422 -0.0444 -0.5944 -0.1775 127 TRP A CG  
962  C CD1 . TRP A 123 ? 1.1731 1.4765 1.0981 -0.0312 -0.5916 -0.1633 127 TRP A CD1 
963  C CD2 . TRP A 123 ? 1.0832 1.3567 0.9390 -0.0510 -0.5724 -0.1805 127 TRP A CD2 
964  N NE1 . TRP A 123 ? 1.0356 1.3179 0.9425 -0.0299 -0.5699 -0.1568 127 TRP A NE1 
965  C CE2 . TRP A 123 ? 1.0471 1.3112 0.9118 -0.0418 -0.5578 -0.1671 127 TRP A CE2 
966  C CE3 . TRP A 123 ? 1.1031 1.3610 0.9184 -0.0633 -0.5635 -0.1942 127 TRP A CE3 
967  C CZ2 . TRP A 123 ? 1.0303 1.2709 0.8648 -0.0448 -0.5354 -0.1665 127 TRP A CZ2 
968  C CZ3 . TRP A 123 ? 1.0863 1.3210 0.8728 -0.0655 -0.5404 -0.1941 127 TRP A CZ3 
969  C CH2 . TRP A 123 ? 1.0502 1.2768 0.8463 -0.0564 -0.5269 -0.1802 127 TRP A CH2 
970  N N   . PRO A 124 ? 1.5250 1.8487 1.3408 -0.0435 -0.6800 -0.1804 128 PRO A N   
971  C CA  . PRO A 124 ? 1.5232 1.8702 1.3594 -0.0409 -0.7085 -0.1835 128 PRO A CA  
972  C C   . PRO A 124 ? 1.5272 1.8967 1.4039 -0.0557 -0.7120 -0.2065 128 PRO A C   
973  O O   . PRO A 124 ? 1.6490 2.0445 1.5646 -0.0534 -0.7325 -0.2104 128 PRO A O   
974  C CB  . PRO A 124 ? 1.6249 1.9554 1.3891 -0.0401 -0.7224 -0.1764 128 PRO A CB  
975  C CG  . PRO A 124 ? 1.5973 1.9032 1.3112 -0.0506 -0.6989 -0.1820 128 PRO A CG  
976  C CD  . PRO A 124 ? 1.5347 1.8318 1.2746 -0.0476 -0.6736 -0.1772 128 PRO A CD  
977  N N   . ASN A 125 ? 1.4258 1.7853 1.2954 -0.0707 -0.6927 -0.2217 129 ASN A N   
978  C CA  . ASN A 125 ? 1.4056 1.7816 1.3108 -0.0865 -0.6941 -0.2433 129 ASN A CA  
979  C C   . ASN A 125 ? 1.2866 1.6747 1.2552 -0.0913 -0.6757 -0.2493 129 ASN A C   
980  O O   . ASN A 125 ? 1.2958 1.6941 1.2945 -0.1062 -0.6726 -0.2665 129 ASN A O   
981  C CB  . ASN A 125 ? 1.4315 1.7865 1.2864 -0.1011 -0.6862 -0.2581 129 ASN A CB  
982  C CG  . ASN A 125 ? 1.5623 1.9035 1.3474 -0.0974 -0.6994 -0.2518 129 ASN A CG  
983  O OD1 . ASN A 125 ? 1.5672 1.9221 1.3484 -0.0909 -0.7244 -0.2458 129 ASN A OD1 
984  N ND2 . ASN A 125 ? 1.5527 1.8675 1.2824 -0.1015 -0.6823 -0.2533 129 ASN A ND2 
985  N N   . HIS A 126 ? 1.3309 1.7175 1.3195 -0.0797 -0.6632 -0.2354 130 HIS A N   
986  C CA  . HIS A 126 ? 1.1316 1.5298 1.1777 -0.0838 -0.6441 -0.2398 130 HIS A CA  
987  C C   . HIS A 126 ? 1.1090 1.5313 1.2054 -0.0691 -0.6506 -0.2283 130 HIS A C   
988  O O   . HIS A 126 ? 1.1295 1.5498 1.2083 -0.0534 -0.6653 -0.2134 130 HIS A O   
989  C CB  . HIS A 126 ? 1.0994 1.4706 1.1222 -0.0853 -0.6170 -0.2366 130 HIS A CB  
990  C CG  . HIS A 126 ? 1.1231 1.4680 1.0927 -0.0969 -0.6089 -0.2472 130 HIS A CG  
991  N ND1 . HIS A 126 ? 1.1611 1.4843 1.0636 -0.0922 -0.6135 -0.2407 130 HIS A ND1 
992  C CD2 . HIS A 126 ? 1.1164 1.4528 1.0903 -0.1128 -0.5957 -0.2643 130 HIS A CD2 
993  C CE1 . HIS A 126 ? 1.1757 1.4801 1.0445 -0.1043 -0.6029 -0.2545 130 HIS A CE1 
994  N NE2 . HIS A 126 ? 1.1495 1.4600 1.0607 -0.1164 -0.5927 -0.2690 130 HIS A NE2 
995  N N   . THR A 127 ? 1.0690 1.5134 1.2280 -0.0748 -0.6388 -0.2355 131 THR A N   
996  C CA  . THR A 127 ? 1.0425 1.5113 1.2546 -0.0618 -0.6400 -0.2272 131 THR A CA  
997  C C   . THR A 127 ? 1.0255 1.4790 1.2370 -0.0538 -0.6175 -0.2161 131 THR A C   
998  O O   . THR A 127 ? 0.9736 1.4127 1.1794 -0.0645 -0.5955 -0.2213 131 THR A O   
999  C CB  . THR A 127 ? 1.0240 1.5281 1.3052 -0.0729 -0.6377 -0.2412 131 THR A CB  
1000 O OG1 . THR A 127 ? 1.1451 1.6634 1.4267 -0.0807 -0.6597 -0.2519 131 THR A OG1 
1001 C CG2 . THR A 127 ? 0.9994 1.5312 1.3362 -0.0587 -0.6380 -0.2342 131 THR A CG2 
1002 N N   . THR A 128 ? 0.9971 1.4525 1.2144 -0.0348 -0.6237 -0.2008 132 THR A N   
1003 C CA  . THR A 128 ? 0.9624 1.4022 1.1762 -0.0252 -0.6053 -0.1886 132 THR A CA  
1004 C C   . THR A 128 ? 0.9302 1.3973 1.2083 -0.0149 -0.6007 -0.1862 132 THR A C   
1005 O O   . THR A 128 ? 0.9160 1.3736 1.1923 0.0000  -0.5959 -0.1728 132 THR A O   
1006 C CB  . THR A 128 ? 0.9909 1.4000 1.1432 -0.0118 -0.6140 -0.1707 132 THR A CB  
1007 O OG1 . THR A 128 ? 1.0208 1.4409 1.1823 0.0038  -0.6375 -0.1612 132 THR A OG1 
1008 C CG2 . THR A 128 ? 1.0277 1.4129 1.1154 -0.0221 -0.6181 -0.1742 132 THR A CG2 
1009 N N   . THR A 129 ? 0.9374 1.4389 1.2727 -0.0231 -0.6011 -0.1996 133 THR A N   
1010 C CA  . THR A 129 ? 0.9308 1.4629 1.3291 -0.0136 -0.5974 -0.1995 133 THR A CA  
1011 C C   . THR A 129 ? 0.8943 1.4460 1.3417 -0.0280 -0.5715 -0.2108 133 THR A C   
1012 O O   . THR A 129 ? 1.0340 1.6172 1.5386 -0.0240 -0.5667 -0.2144 133 THR A O   
1013 C CB  . THR A 129 ? 0.9704 1.5316 1.3991 -0.0077 -0.6226 -0.2041 133 THR A CB  
1014 O OG1 . THR A 129 ? 0.9728 1.5524 1.4198 -0.0273 -0.6250 -0.2204 133 THR A OG1 
1015 C CG2 . THR A 129 ? 0.9984 1.5393 1.3764 0.0057  -0.6490 -0.1922 133 THR A CG2 
1016 N N   . GLY A 130 ? 0.8374 1.3711 1.2637 -0.0449 -0.5543 -0.2164 134 GLY A N   
1017 C CA  . GLY A 130 ? 0.8006 1.3492 1.2690 -0.0602 -0.5294 -0.2256 134 GLY A CA  
1018 C C   . GLY A 130 ? 0.7613 1.3170 1.2587 -0.0501 -0.5100 -0.2185 134 GLY A C   
1019 O O   . GLY A 130 ? 0.7514 1.2822 1.2167 -0.0384 -0.5051 -0.2070 134 GLY A O   
1020 N N   . VAL A 131 ? 0.7408 1.3308 1.2985 -0.0548 -0.4984 -0.2257 135 VAL A N   
1021 C CA  . VAL A 131 ? 0.7044 1.3053 1.2944 -0.0471 -0.4776 -0.2215 135 VAL A CA  
1022 C C   . VAL A 131 ? 0.6793 1.3005 1.3105 -0.0681 -0.4527 -0.2318 135 VAL A C   
1023 O O   . VAL A 131 ? 0.7450 1.3750 1.3861 -0.0867 -0.4545 -0.2418 135 VAL A O   
1024 C CB  . VAL A 131 ? 0.7102 1.3359 1.3349 -0.0261 -0.4892 -0.2179 135 VAL A CB  
1025 C CG1 . VAL A 131 ? 0.7345 1.3340 1.3150 -0.0051 -0.5106 -0.2043 135 VAL A CG1 
1026 C CG2 . VAL A 131 ? 0.7309 1.3932 1.3986 -0.0316 -0.5025 -0.2293 135 VAL A CG2 
1027 N N   . SER A 132 ? 0.6457 1.2730 1.2994 -0.0654 -0.4292 -0.2288 136 SER A N   
1028 C CA  . SER A 132 ? 0.6229 1.2674 1.3123 -0.0851 -0.4028 -0.2362 136 SER A CA  
1029 C C   . SER A 132 ? 0.7110 1.3849 1.4470 -0.0751 -0.3876 -0.2359 136 SER A C   
1030 O O   . SER A 132 ? 0.6582 1.3273 1.3893 -0.0536 -0.3908 -0.2283 136 SER A O   
1031 C CB  . SER A 132 ? 0.6038 1.2163 1.2607 -0.0982 -0.3829 -0.2334 136 SER A CB  
1032 O OG  . SER A 132 ? 0.5976 1.2242 1.2863 -0.1183 -0.3574 -0.2389 136 SER A OG  
1033 N N   . ALA A 133 ? 0.8831 1.5868 1.6635 -0.0914 -0.3705 -0.2446 137 ALA A N   
1034 C CA  . ALA A 133 ? 0.8762 1.6082 1.6997 -0.0852 -0.3510 -0.2460 137 ALA A CA  
1035 C C   . ALA A 133 ? 0.8474 1.5612 1.6568 -0.0877 -0.3237 -0.2398 137 ALA A C   
1036 O O   . ALA A 133 ? 0.7903 1.5187 1.6224 -0.0762 -0.3096 -0.2387 137 ALA A O   
1037 C CB  . ALA A 133 ? 0.8344 1.6045 1.7072 -0.1033 -0.3407 -0.2569 137 ALA A CB  
1038 N N   . SER A 134 ? 0.7812 1.4632 1.5536 -0.1023 -0.3160 -0.2365 138 SER A N   
1039 C CA  . SER A 134 ? 0.7487 1.4104 1.5035 -0.1040 -0.2924 -0.2301 138 SER A CA  
1040 C C   . SER A 134 ? 0.6995 1.3413 1.4276 -0.0792 -0.3011 -0.2208 138 SER A C   
1041 O O   . SER A 134 ? 0.6390 1.2742 1.3651 -0.0747 -0.2819 -0.2161 138 SER A O   
1042 C CB  . SER A 134 ? 0.7541 1.3850 1.4758 -0.1253 -0.2845 -0.2296 138 SER A CB  
1043 O OG  . SER A 134 ? 0.7767 1.3842 1.4616 -0.1227 -0.3093 -0.2296 138 SER A OG  
1044 N N   . CYS A 135 ? 0.6327 1.2637 1.3384 -0.0637 -0.3294 -0.2174 139 CYS A N   
1045 C CA  . CYS A 135 ? 0.5200 1.1318 1.2006 -0.0398 -0.3399 -0.2071 139 CYS A CA  
1046 C C   . CYS A 135 ? 0.6157 1.2500 1.3241 -0.0194 -0.3567 -0.2073 139 CYS A C   
1047 O O   . CYS A 135 ? 0.6197 1.2396 1.3032 -0.0042 -0.3821 -0.2009 139 CYS A O   
1048 C CB  . CYS A 135 ? 0.5444 1.1189 1.1679 -0.0376 -0.3586 -0.2003 139 CYS A CB  
1049 S SG  . CYS A 135 ? 0.7206 1.2630 1.3067 -0.0574 -0.3404 -0.2002 139 CYS A SG  
1050 N N   . SER A 136 ? 0.9389 1.6074 1.6971 -0.0190 -0.3423 -0.2145 140 SER A N   
1051 C CA  . SER A 136 ? 1.1085 1.8021 1.8997 -0.0012 -0.3573 -0.2176 140 SER A CA  
1052 C C   . SER A 136 ? 1.0393 1.7178 1.8209 0.0247  -0.3616 -0.2086 140 SER A C   
1053 O O   . SER A 136 ? 1.0028 1.6613 1.7658 0.0273  -0.3458 -0.2023 140 SER A O   
1054 C CB  . SER A 136 ? 1.1385 1.8748 1.9863 -0.0105 -0.3391 -0.2298 140 SER A CB  
1055 O OG  . SER A 136 ? 1.1764 1.9263 2.0347 -0.0346 -0.3370 -0.2375 140 SER A OG  
1056 N N   . HIS A 137 ? 1.0642 1.7517 1.8592 0.0438  -0.3841 -0.2081 141 HIS A N   
1057 C CA  . HIS A 137 ? 1.0482 1.7216 1.8385 0.0692  -0.3909 -0.2001 141 HIS A CA  
1058 C C   . HIS A 137 ? 1.1038 1.8073 1.9383 0.0841  -0.4039 -0.2076 141 HIS A C   
1059 O O   . HIS A 137 ? 1.2466 1.9613 2.0865 0.0838  -0.4264 -0.2104 141 HIS A O   
1060 C CB  . HIS A 137 ? 1.0072 1.6377 1.7401 0.0799  -0.4134 -0.1846 141 HIS A CB  
1061 C CG  . HIS A 137 ? 1.0629 1.6732 1.7867 0.1046  -0.4209 -0.1744 141 HIS A CG  
1062 N ND1 . HIS A 137 ? 0.9275 1.5336 1.6613 0.1112  -0.3993 -0.1736 141 HIS A ND1 
1063 C CD2 . HIS A 137 ? 1.1620 1.7532 1.8662 0.1235  -0.4476 -0.1644 141 HIS A CD2 
1064 C CE1 . HIS A 137 ? 0.9473 1.5318 1.6690 0.1332  -0.4126 -0.1639 141 HIS A CE1 
1065 N NE2 . HIS A 137 ? 1.1101 1.6845 1.8134 0.1409  -0.4419 -0.1576 141 HIS A NE2 
1066 N N   . ASN A 138 ? 1.0052 1.7219 1.8708 0.0970  -0.3899 -0.2118 142 ASN A N   
1067 C CA  . ASN A 138 ? 1.0906 1.8387 2.0038 0.1114  -0.3984 -0.2215 142 ASN A CA  
1068 C C   . ASN A 138 ? 1.0784 1.8696 2.0334 0.0941  -0.3943 -0.2360 142 ASN A C   
1069 O O   . ASN A 138 ? 1.0373 1.8510 2.0199 0.1020  -0.4139 -0.2423 142 ASN A O   
1070 C CB  . ASN A 138 ? 1.1584 1.8875 2.0547 0.1337  -0.4328 -0.2127 142 ASN A CB  
1071 C CG  . ASN A 138 ? 1.2292 1.9207 2.0961 0.1534  -0.4354 -0.1998 142 ASN A CG  
1072 O OD1 . ASN A 138 ? 1.2340 1.9255 2.1129 0.1573  -0.4128 -0.2023 142 ASN A OD1 
1073 N ND2 . ASN A 138 ? 1.2354 1.8935 2.0617 0.1652  -0.4628 -0.1856 142 ASN A ND2 
1074 N N   . GLY A 139 ? 1.1517 1.9534 2.1109 0.0699  -0.3688 -0.2409 143 GLY A N   
1075 C CA  . GLY A 139 ? 1.1505 1.9907 2.1480 0.0503  -0.3608 -0.2537 143 GLY A CA  
1076 C C   . GLY A 139 ? 1.1376 1.9751 2.1192 0.0358  -0.3808 -0.2534 143 GLY A C   
1077 O O   . GLY A 139 ? 1.1565 2.0203 2.1635 0.0148  -0.3717 -0.2627 143 GLY A O   
1078 N N   . GLU A 140 ? 1.1167 1.9225 2.0557 0.0454  -0.4071 -0.2429 144 GLU A N   
1079 C CA  . GLU A 140 ? 1.1714 1.9727 2.0913 0.0338  -0.4285 -0.2430 144 GLU A CA  
1080 C C   . GLU A 140 ? 1.0181 1.7813 1.8834 0.0199  -0.4241 -0.2344 144 GLU A C   
1081 O O   . GLU A 140 ? 1.0312 1.7651 1.8653 0.0269  -0.4150 -0.2247 144 GLU A O   
1082 C CB  . GLU A 140 ? 1.3528 2.1478 2.2627 0.0547  -0.4638 -0.2383 144 GLU A CB  
1083 C CG  . GLU A 140 ? 1.4783 2.3078 2.4410 0.0718  -0.4708 -0.2468 144 GLU A CG  
1084 C CD  . GLU A 140 ? 1.5563 2.3689 2.5023 0.0972  -0.5030 -0.2383 144 GLU A CD  
1085 O OE1 . GLU A 140 ? 1.5709 2.3456 2.4624 0.1002  -0.5196 -0.2252 144 GLU A OE1 
1086 O OE2 . GLU A 140 ? 1.5395 2.3759 2.5259 0.1139  -0.5114 -0.2446 144 GLU A OE2 
1087 N N   . SER A 141 ? 0.8507 1.6146 1.7056 0.0003  -0.4310 -0.2388 145 SER A N   
1088 C CA  . SER A 141 ? 0.6821 1.4109 1.4867 -0.0139 -0.4277 -0.2331 145 SER A CA  
1089 C C   . SER A 141 ? 0.6950 1.3852 1.4455 0.0034  -0.4475 -0.2196 145 SER A C   
1090 O O   . SER A 141 ? 0.6738 1.3635 1.4200 0.0212  -0.4722 -0.2155 145 SER A O   
1091 C CB  . SER A 141 ? 0.7279 1.4638 1.5314 -0.0356 -0.4362 -0.2414 145 SER A CB  
1092 O OG  . SER A 141 ? 0.8101 1.5789 1.6606 -0.0541 -0.4168 -0.2524 145 SER A OG  
1093 N N   . SER A 142 ? 0.8446 1.5014 1.5526 -0.0024 -0.4363 -0.2124 146 SER A N   
1094 C CA  . SER A 142 ? 0.8494 1.4677 1.5024 0.0119  -0.4516 -0.1988 146 SER A CA  
1095 C C   . SER A 142 ? 0.8699 1.4571 1.4781 -0.0033 -0.4403 -0.1962 146 SER A C   
1096 O O   . SER A 142 ? 0.9807 1.5747 1.5989 -0.0245 -0.4258 -0.2052 146 SER A O   
1097 C CB  . SER A 142 ? 0.8360 1.4473 1.4938 0.0342  -0.4480 -0.1894 146 SER A CB  
1098 O OG  . SER A 142 ? 0.8172 1.3909 1.4214 0.0474  -0.4646 -0.1749 146 SER A OG  
1099 N N   . PHE A 143 ? 0.6942 1.2459 1.2525 0.0075  -0.4469 -0.1836 147 PHE A N   
1100 C CA  . PHE A 143 ? 0.6451 1.1651 1.1557 -0.0045 -0.4395 -0.1812 147 PHE A CA  
1101 C C   . PHE A 143 ? 0.6863 1.1740 1.1564 0.0108  -0.4397 -0.1663 147 PHE A C   
1102 O O   . PHE A 143 ? 0.7240 1.2112 1.2000 0.0299  -0.4481 -0.1573 147 PHE A O   
1103 C CB  . PHE A 143 ? 0.7376 1.2469 1.2144 -0.0142 -0.4583 -0.1852 147 PHE A CB  
1104 C CG  . PHE A 143 ? 0.6631 1.1453 1.0999 -0.0300 -0.4479 -0.1879 147 PHE A CG  
1105 C CD1 . PHE A 143 ? 0.6401 1.1302 1.1001 -0.0495 -0.4269 -0.1984 147 PHE A CD1 
1106 C CD2 . PHE A 143 ? 0.6858 1.1336 1.0607 -0.0257 -0.4586 -0.1801 147 PHE A CD2 
1107 C CE1 . PHE A 143 ? 0.6566 1.1196 1.0805 -0.0631 -0.4179 -0.2016 147 PHE A CE1 
1108 C CE2 . PHE A 143 ? 0.6843 1.1075 1.0230 -0.0392 -0.4486 -0.1844 147 PHE A CE2 
1109 C CZ  . PHE A 143 ? 0.6609 1.0911 1.0250 -0.0572 -0.4288 -0.1956 147 PHE A CZ  
1110 N N   . TYR A 144 ? 0.6837 1.1432 1.1126 0.0019  -0.4302 -0.1639 148 TYR A N   
1111 C CA  . TYR A 144 ? 0.6497 1.0764 1.0361 0.0135  -0.4281 -0.1494 148 TYR A CA  
1112 C C   . TYR A 144 ? 0.7031 1.1108 1.0494 0.0281  -0.4545 -0.1373 148 TYR A C   
1113 O O   . TYR A 144 ? 0.8982 1.3063 1.2267 0.0241  -0.4720 -0.1401 148 TYR A O   
1114 C CB  . TYR A 144 ? 0.6167 1.0102 0.9553 -0.0011 -0.4049 -0.1463 148 TYR A CB  
1115 C CG  . TYR A 144 ? 0.5847 0.9871 0.9511 -0.0171 -0.3752 -0.1543 148 TYR A CG  
1116 C CD1 . TYR A 144 ? 0.5563 0.9553 0.9354 -0.0138 -0.3494 -0.1475 148 TYR A CD1 
1117 C CD2 . TYR A 144 ? 0.5864 0.9984 0.9639 -0.0360 -0.3738 -0.1682 148 TYR A CD2 
1118 C CE1 . TYR A 144 ? 0.5313 0.9367 0.9318 -0.0289 -0.3231 -0.1535 148 TYR A CE1 
1119 C CE2 . TYR A 144 ? 0.5619 0.9786 0.9619 -0.0515 -0.3475 -0.1738 148 TYR A CE2 
1120 C CZ  . TYR A 144 ? 0.5349 0.9484 0.9453 -0.0479 -0.3223 -0.1659 148 TYR A CZ  
1121 O OH  . TYR A 144 ? 0.5146 0.9312 0.9437 -0.0638 -0.2969 -0.1702 148 TYR A OH  
1122 N N   . LYS A 145 ? 0.6624 1.0514 0.9925 0.0443  -0.4560 -0.1227 149 LYS A N   
1123 C CA  . LYS A 145 ? 0.7683 1.1344 1.0573 0.0577  -0.4781 -0.1077 149 LYS A CA  
1124 C C   . LYS A 145 ? 0.7252 1.0535 0.9432 0.0524  -0.4801 -0.0983 149 LYS A C   
1125 O O   . LYS A 145 ? 0.9369 1.2454 1.1128 0.0590  -0.4978 -0.0865 149 LYS A O   
1126 C CB  . LYS A 145 ? 0.8197 1.1802 1.1238 0.0773  -0.4791 -0.0956 149 LYS A CB  
1127 C CG  . LYS A 145 ? 1.1089 1.4561 1.3914 0.0922  -0.5042 -0.0827 149 LYS A CG  
1128 C CD  . LYS A 145 ? 1.1480 1.4877 1.4486 0.1113  -0.5043 -0.0722 149 LYS A CD  
1129 C CE  . LYS A 145 ? 1.1159 1.4404 1.3956 0.1256  -0.5301 -0.0592 149 LYS A CE  
1130 N NZ  . LYS A 145 ? 0.9956 1.3092 1.2924 0.1444  -0.5309 -0.0495 149 LYS A NZ  
1131 N N   . ASN A 146 ? 0.7043 1.0180 0.9025 0.0384  -0.4511 -0.1003 150 ASN A N   
1132 C CA  . ASN A 146 ? 0.7252 1.0043 0.8568 0.0312  -0.4442 -0.0927 150 ASN A CA  
1133 C C   . ASN A 146 ? 0.7338 1.0166 0.8516 0.0146  -0.4446 -0.1078 150 ASN A C   
1134 O O   . ASN A 146 ? 0.7515 1.0085 0.8161 0.0078  -0.4377 -0.1051 150 ASN A O   
1135 C CB  . ASN A 146 ? 0.6999 0.9557 0.8141 0.0293  -0.4113 -0.0830 150 ASN A CB  
1136 C CG  . ASN A 146 ? 0.6994 0.9432 0.8146 0.0451  -0.4117 -0.0667 150 ASN A CG  
1137 O OD1 . ASN A 146 ? 0.7300 0.9687 0.8340 0.0574  -0.4371 -0.0574 150 ASN A OD1 
1138 N ND2 . ASN A 146 ? 0.6672 0.9049 0.7950 0.0449  -0.3845 -0.0631 150 ASN A ND2 
1139 N N   . LEU A 147 ? 0.8812 1.1955 1.0463 0.0075  -0.4521 -0.1246 151 LEU A N   
1140 C CA  . LEU A 147 ? 0.7855 1.1036 0.9418 -0.0084 -0.4558 -0.1404 151 LEU A CA  
1141 C C   . LEU A 147 ? 0.7604 1.1032 0.9389 -0.0077 -0.4820 -0.1480 151 LEU A C   
1142 O O   . LEU A 147 ? 0.7620 1.1233 0.9731 0.0042  -0.4924 -0.1428 151 LEU A O   
1143 C CB  . LEU A 147 ? 0.7769 1.1041 0.9664 -0.0236 -0.4288 -0.1519 151 LEU A CB  
1144 C CG  . LEU A 147 ? 0.6766 0.9769 0.8424 -0.0266 -0.3957 -0.1434 151 LEU A CG  
1145 C CD1 . LEU A 147 ? 0.6464 0.9566 0.8476 -0.0413 -0.3731 -0.1541 151 LEU A CD1 
1146 C CD2 . LEU A 147 ? 0.8007 1.0681 0.9010 -0.0296 -0.3932 -0.1398 151 LEU A CD2 
1147 N N   . LEU A 148 ? 0.8211 1.1619 0.9801 -0.0207 -0.4876 -0.1594 152 LEU A N   
1148 C CA  . LEU A 148 ? 0.8147 1.1745 0.9856 -0.0223 -0.5084 -0.1652 152 LEU A CA  
1149 C C   . LEU A 148 ? 0.8110 1.1824 1.0013 -0.0418 -0.5024 -0.1841 152 LEU A C   
1150 O O   . LEU A 148 ? 0.8234 1.1737 0.9750 -0.0524 -0.4971 -0.1909 152 LEU A O   
1151 C CB  . LEU A 148 ? 0.8788 1.2175 0.9889 -0.0164 -0.5273 -0.1562 152 LEU A CB  
1152 C CG  . LEU A 148 ? 0.9008 1.2574 1.0203 -0.0111 -0.5532 -0.1559 152 LEU A CG  
1153 C CD1 . LEU A 148 ? 0.8869 1.2647 1.0554 0.0042  -0.5597 -0.1482 152 LEU A CD1 
1154 C CD2 . LEU A 148 ? 1.0235 1.3553 1.0759 -0.0065 -0.5686 -0.1454 152 LEU A CD2 
1155 N N   . TRP A 149 ? 0.7963 1.2002 1.0461 -0.0468 -0.5024 -0.1928 153 TRP A N   
1156 C CA  . TRP A 149 ? 0.7938 1.2090 1.0670 -0.0667 -0.4961 -0.2095 153 TRP A CA  
1157 C C   . TRP A 149 ? 0.8832 1.3022 1.1385 -0.0713 -0.5188 -0.2164 153 TRP A C   
1158 O O   . TRP A 149 ? 0.9999 1.4456 1.2872 -0.0675 -0.5346 -0.2179 153 TRP A O   
1159 C CB  . TRP A 149 ? 0.7622 1.2109 1.1049 -0.0718 -0.4848 -0.2150 153 TRP A CB  
1160 C CG  . TRP A 149 ? 0.7546 1.2094 1.1204 -0.0943 -0.4720 -0.2295 153 TRP A CG  
1161 C CD1 . TRP A 149 ? 0.7796 1.2180 1.1176 -0.1088 -0.4760 -0.2398 153 TRP A CD1 
1162 C CD2 . TRP A 149 ? 0.7232 1.1998 1.1427 -0.1054 -0.4524 -0.2347 153 TRP A CD2 
1163 N NE1 . TRP A 149 ? 0.7664 1.2130 1.1380 -0.1281 -0.4612 -0.2503 153 TRP A NE1 
1164 C CE2 . TRP A 149 ? 0.7322 1.2025 1.1531 -0.1271 -0.4461 -0.2468 153 TRP A CE2 
1165 C CE3 . TRP A 149 ? 0.6915 1.1916 1.1567 -0.0994 -0.4388 -0.2303 153 TRP A CE3 
1166 C CZ2 . TRP A 149 ? 0.7116 1.1970 1.1762 -0.1438 -0.4270 -0.2527 153 TRP A CZ2 
1167 C CZ3 . TRP A 149 ? 0.7126 1.2302 1.2208 -0.1160 -0.4186 -0.2372 153 TRP A CZ3 
1168 C CH2 . TRP A 149 ? 0.7743 1.2840 1.2813 -0.1385 -0.4130 -0.2475 153 TRP A CH2 
1169 N N   . LEU A 150 ? 0.8636 1.2566 1.0679 -0.0794 -0.5200 -0.2216 154 LEU A N   
1170 C CA  . LEU A 150 ? 0.9089 1.3031 1.0907 -0.0850 -0.5404 -0.2294 154 LEU A CA  
1171 C C   . LEU A 150 ? 1.0001 1.4146 1.2246 -0.1029 -0.5394 -0.2459 154 LEU A C   
1172 O O   . LEU A 150 ? 0.9677 1.3715 1.1975 -0.1174 -0.5218 -0.2552 154 LEU A O   
1173 C CB  . LEU A 150 ? 0.9368 1.2969 1.0497 -0.0880 -0.5393 -0.2308 154 LEU A CB  
1174 C CG  . LEU A 150 ? 0.9426 1.2795 1.0063 -0.0730 -0.5382 -0.2141 154 LEU A CG  
1175 C CD1 . LEU A 150 ? 0.9772 1.2852 0.9736 -0.0779 -0.5374 -0.2178 154 LEU A CD1 
1176 C CD2 . LEU A 150 ? 1.0192 1.3687 1.0861 -0.0569 -0.5587 -0.1998 154 LEU A CD2 
1177 N N   . THR A 151 ? 1.1113 1.5540 1.3661 -0.1021 -0.5585 -0.2493 155 THR A N   
1178 C CA  . THR A 151 ? 0.9500 1.4138 1.2457 -0.1197 -0.5596 -0.2644 155 THR A CA  
1179 C C   . THR A 151 ? 1.0361 1.5015 1.3075 -0.1241 -0.5841 -0.2725 155 THR A C   
1180 O O   . THR A 151 ? 1.0121 1.4567 1.2281 -0.1164 -0.5953 -0.2676 155 THR A O   
1181 C CB  . THR A 151 ? 0.9744 1.4765 1.3390 -0.1173 -0.5574 -0.2635 155 THR A CB  
1182 O OG1 . THR A 151 ? 1.1778 1.6780 1.5551 -0.1062 -0.5399 -0.2523 155 THR A OG1 
1183 C CG2 . THR A 151 ? 0.9473 1.4654 1.3554 -0.1393 -0.5462 -0.2773 155 THR A CG2 
1184 N N   . GLY A 152 ? 1.2897 1.7800 1.6008 -0.1369 -0.5922 -0.2846 156 GLY A N   
1185 C CA  . GLY A 152 ? 1.2739 1.7650 1.5628 -0.1437 -0.6144 -0.2944 156 GLY A CA  
1186 C C   . GLY A 152 ? 1.3241 1.8328 1.6093 -0.1277 -0.6413 -0.2870 156 GLY A C   
1187 O O   . GLY A 152 ? 1.2915 1.8262 1.6182 -0.1161 -0.6459 -0.2798 156 GLY A O   
1188 N N   . LYS A 153 ? 1.4919 1.9858 1.7256 -0.1273 -0.6594 -0.2893 157 LYS A N   
1189 C CA  . LYS A 153 ? 1.6032 2.1085 1.8228 -0.1131 -0.6869 -0.2817 157 LYS A CA  
1190 C C   . LYS A 153 ? 1.6287 2.1424 1.8390 -0.1253 -0.7078 -0.2961 157 LYS A C   
1191 O O   . LYS A 153 ? 1.6898 2.1792 1.8511 -0.1349 -0.7073 -0.3039 157 LYS A O   
1192 C CB  . LYS A 153 ? 1.6602 2.1359 1.8155 -0.0984 -0.6887 -0.2663 157 LYS A CB  
1193 C CG  . LYS A 153 ? 1.6759 2.1549 1.7999 -0.0870 -0.7178 -0.2590 157 LYS A CG  
1194 C CD  . LYS A 153 ? 1.6603 2.1633 1.8254 -0.0691 -0.7312 -0.2470 157 LYS A CD  
1195 C CE  . LYS A 153 ? 1.7648 2.2643 1.8911 -0.0564 -0.7595 -0.2369 157 LYS A CE  
1196 N NZ  . LYS A 153 ? 1.7635 2.2820 1.9267 -0.0369 -0.7734 -0.2245 157 LYS A NZ  
1197 N N   . ASN A 154 ? 1.4950 2.0436 1.7529 -0.1246 -0.7261 -0.3005 158 ASN A N   
1198 C CA  . ASN A 154 ? 1.5066 2.0681 1.7631 -0.1357 -0.7485 -0.3143 158 ASN A CA  
1199 C C   . ASN A 154 ? 1.4757 2.0265 1.7316 -0.1596 -0.7363 -0.3322 158 ASN A C   
1200 O O   . ASN A 154 ? 1.4049 1.9512 1.6354 -0.1700 -0.7512 -0.3441 158 ASN A O   
1201 C CB  . ASN A 154 ? 1.4533 1.9994 1.6465 -0.1263 -0.7714 -0.3086 158 ASN A CB  
1202 C CG  . ASN A 154 ? 1.4254 1.9868 1.6268 -0.1045 -0.7911 -0.2930 158 ASN A CG  
1203 O OD1 . ASN A 154 ? 1.4607 2.0552 1.7214 -0.0995 -0.7999 -0.2938 158 ASN A OD1 
1204 N ND2 . ASN A 154 ? 1.3969 1.9340 1.5388 -0.0915 -0.7977 -0.2787 158 ASN A ND2 
1205 N N   . GLY A 155 ? 1.4885 2.0339 1.7716 -0.1684 -0.7095 -0.3342 159 GLY A N   
1206 C CA  . GLY A 155 ? 1.3991 1.9340 1.6887 -0.1912 -0.6972 -0.3501 159 GLY A CA  
1207 C C   . GLY A 155 ? 1.4701 1.9626 1.6992 -0.1969 -0.6846 -0.3542 159 GLY A C   
1208 O O   . GLY A 155 ? 1.3520 1.8321 1.5767 -0.2151 -0.6806 -0.3693 159 GLY A O   
1209 N N   . LEU A 156 ? 1.6542 2.1237 1.8371 -0.1822 -0.6779 -0.3417 160 LEU A N   
1210 C CA  . LEU A 156 ? 1.6896 2.1201 1.8150 -0.1864 -0.6646 -0.3459 160 LEU A CA  
1211 C C   . LEU A 156 ? 1.5511 1.9636 1.6568 -0.1726 -0.6455 -0.3305 160 LEU A C   
1212 O O   . LEU A 156 ? 1.5695 1.9949 1.6855 -0.1565 -0.6498 -0.3150 160 LEU A O   
1213 C CB  . LEU A 156 ? 1.7572 2.1752 1.8227 -0.1852 -0.6838 -0.3509 160 LEU A CB  
1214 C CG  . LEU A 156 ? 1.8239 2.2465 1.8910 -0.2024 -0.6985 -0.3704 160 LEU A CG  
1215 C CD1 . LEU A 156 ? 1.9433 2.3546 1.9476 -0.1992 -0.7171 -0.3736 160 LEU A CD1 
1216 C CD2 . LEU A 156 ? 1.7884 2.1892 1.8611 -0.2201 -0.6785 -0.3851 160 LEU A CD2 
1217 N N   . TYR A 157 ? 1.3838 1.7654 1.4614 -0.1789 -0.6247 -0.3353 161 TYR A N   
1218 C CA  . TYR A 157 ? 1.1543 1.5151 1.2075 -0.1677 -0.6054 -0.3228 161 TYR A CA  
1219 C C   . TYR A 157 ? 1.1862 1.5139 1.1702 -0.1683 -0.6013 -0.3280 161 TYR A C   
1220 O O   . TYR A 157 ? 1.1830 1.4877 1.1554 -0.1784 -0.5849 -0.3392 161 TYR A O   
1221 C CB  . TYR A 157 ? 1.1082 1.4658 1.2019 -0.1745 -0.5808 -0.3236 161 TYR A CB  
1222 C CG  . TYR A 157 ? 1.2398 1.5878 1.3270 -0.1608 -0.5641 -0.3080 161 TYR A CG  
1223 C CD1 . TYR A 157 ? 1.1705 1.4878 1.2020 -0.1546 -0.5535 -0.3045 161 TYR A CD1 
1224 C CD2 . TYR A 157 ? 1.1904 1.5609 1.3276 -0.1544 -0.5582 -0.2977 161 TYR A CD2 
1225 C CE1 . TYR A 157 ? 1.0376 1.3462 1.0633 -0.1427 -0.5388 -0.2905 161 TYR A CE1 
1226 C CE2 . TYR A 157 ? 1.0822 1.4436 1.2136 -0.1422 -0.5435 -0.2841 161 TYR A CE2 
1227 C CZ  . TYR A 157 ? 1.0805 1.4105 1.1560 -0.1366 -0.5344 -0.2803 161 TYR A CZ  
1228 O OH  . TYR A 157 ? 1.0891 1.4099 1.1586 -0.1250 -0.5203 -0.2669 161 TYR A OH  
1229 N N   . PRO A 158 ? 1.2198 1.5442 1.1565 -0.1578 -0.6152 -0.3201 162 PRO A N   
1230 C CA  . PRO A 158 ? 1.2563 1.5526 1.1255 -0.1597 -0.6112 -0.3262 162 PRO A CA  
1231 C C   . PRO A 158 ? 1.2281 1.4980 1.0729 -0.1554 -0.5851 -0.3215 162 PRO A C   
1232 O O   . PRO A 158 ? 1.1818 1.4541 1.0559 -0.1490 -0.5717 -0.3108 162 PRO A O   
1233 C CB  . PRO A 158 ? 1.2949 1.5982 1.1250 -0.1484 -0.6316 -0.3144 162 PRO A CB  
1234 C CG  . PRO A 158 ? 1.2899 1.6260 1.1711 -0.1442 -0.6520 -0.3087 162 PRO A CG  
1235 C CD  . PRO A 158 ? 1.2326 1.5797 1.1758 -0.1449 -0.6367 -0.3064 162 PRO A CD  
1236 N N   . ASN A 159 ? 1.3480 1.5931 1.1379 -0.1590 -0.5776 -0.3304 163 ASN A N   
1237 C CA  . ASN A 159 ? 1.2522 1.4714 1.0122 -0.1549 -0.5533 -0.3280 163 ASN A CA  
1238 C C   . ASN A 159 ? 1.3245 1.5429 1.0509 -0.1400 -0.5532 -0.3072 163 ASN A C   
1239 O O   . ASN A 159 ? 1.2828 1.4991 0.9606 -0.1371 -0.5638 -0.3036 163 ASN A O   
1240 C CB  . ASN A 159 ? 1.3192 1.5141 1.0337 -0.1637 -0.5454 -0.3461 163 ASN A CB  
1241 C CG  . ASN A 159 ? 1.4071 1.5972 1.1536 -0.1783 -0.5439 -0.3661 163 ASN A CG  
1242 O OD1 . ASN A 159 ? 1.4052 1.6133 1.2066 -0.1838 -0.5505 -0.3666 163 ASN A OD1 
1243 N ND2 . ASN A 159 ? 1.3993 1.5649 1.1118 -0.1850 -0.5347 -0.3829 163 ASN A ND2 
1244 N N   . LEU A 160 ? 1.3416 1.5610 1.0928 -0.1313 -0.5410 -0.2934 164 LEU A N   
1245 C CA  . LEU A 160 ? 1.3118 1.5279 1.0348 -0.1173 -0.5396 -0.2726 164 LEU A CA  
1246 C C   . LEU A 160 ? 1.2788 1.4690 0.9622 -0.1155 -0.5152 -0.2721 164 LEU A C   
1247 O O   . LEU A 160 ? 1.2637 1.4428 0.9650 -0.1206 -0.4971 -0.2824 164 LEU A O   
1248 C CB  . LEU A 160 ? 1.2019 1.4355 0.9762 -0.1077 -0.5427 -0.2571 164 LEU A CB  
1249 C CG  . LEU A 160 ? 1.1408 1.3745 0.9630 -0.1093 -0.5236 -0.2589 164 LEU A CG  
1250 C CD1 . LEU A 160 ? 1.0653 1.2820 0.8659 -0.0995 -0.5056 -0.2452 164 LEU A CD1 
1251 C CD2 . LEU A 160 ? 1.0629 1.3253 0.9510 -0.1078 -0.5336 -0.2550 164 LEU A CD2 
1252 N N   . SER A 161 ? 1.3170 1.4980 0.9466 -0.1085 -0.5146 -0.2599 165 SER A N   
1253 C CA  . SER A 161 ? 1.3040 1.4628 0.8921 -0.1066 -0.4912 -0.2586 165 SER A CA  
1254 C C   . SER A 161 ? 1.2869 1.4434 0.8397 -0.0956 -0.4931 -0.2351 165 SER A C   
1255 O O   . SER A 161 ? 1.3853 1.5403 0.8893 -0.0957 -0.5006 -0.2311 165 SER A O   
1256 C CB  . SER A 161 ? 1.3821 1.5271 0.9267 -0.1164 -0.4839 -0.2777 165 SER A CB  
1257 O OG  . SER A 161 ? 1.4350 1.5614 0.9380 -0.1140 -0.4613 -0.2760 165 SER A OG  
1258 N N   . LYS A 162 ? 1.2911 1.4467 0.8687 -0.0865 -0.4861 -0.2196 166 LYS A N   
1259 C CA  . LYS A 162 ? 1.3596 1.5089 0.9084 -0.0759 -0.4865 -0.1957 166 LYS A CA  
1260 C C   . LYS A 162 ? 1.2896 1.4195 0.8138 -0.0741 -0.4602 -0.1914 166 LYS A C   
1261 O O   . LYS A 162 ? 1.3310 1.4540 0.8686 -0.0790 -0.4428 -0.2062 166 LYS A O   
1262 C CB  . LYS A 162 ? 1.2695 1.4325 0.8654 -0.0659 -0.5012 -0.1795 166 LYS A CB  
1263 C CG  . LYS A 162 ? 1.4330 1.6160 1.0472 -0.0650 -0.5287 -0.1797 166 LYS A CG  
1264 C CD  . LYS A 162 ? 1.5033 1.6810 1.0590 -0.0634 -0.5411 -0.1711 166 LYS A CD  
1265 C CE  . LYS A 162 ? 1.5156 1.7133 1.0895 -0.0621 -0.5698 -0.1721 166 LYS A CE  
1266 N NZ  . LYS A 162 ? 1.4986 1.6913 1.0142 -0.0608 -0.5828 -0.1641 166 LYS A NZ  
1267 N N   . SER A 163 ? 1.1782 1.2985 0.6665 -0.0671 -0.4573 -0.1705 167 SER A N   
1268 C CA  . SER A 163 ? 1.1821 1.2844 0.6430 -0.0658 -0.4325 -0.1641 167 SER A CA  
1269 C C   . SER A 163 ? 1.1857 1.2798 0.6312 -0.0567 -0.4356 -0.1357 167 SER A C   
1270 O O   . SER A 163 ? 1.1925 1.2930 0.6383 -0.0513 -0.4565 -0.1223 167 SER A O   
1271 C CB  . SER A 163 ? 1.2020 1.2961 0.6087 -0.0733 -0.4169 -0.1769 167 SER A CB  
1272 O OG  . SER A 163 ? 1.2559 1.3549 0.6214 -0.0742 -0.4303 -0.1720 167 SER A OG  
1273 N N   . TYR A 164 ? 1.1495 1.2281 0.5822 -0.0552 -0.4145 -0.1264 168 TYR A N   
1274 C CA  . TYR A 164 ? 1.1533 1.2200 0.5711 -0.0483 -0.4142 -0.0989 168 TYR A CA  
1275 C C   . TYR A 164 ? 1.2425 1.2917 0.6181 -0.0527 -0.3867 -0.0933 168 TYR A C   
1276 O O   . TYR A 164 ? 1.2331 1.2799 0.6203 -0.0565 -0.3657 -0.1063 168 TYR A O   
1277 C CB  . TYR A 164 ? 1.1066 1.1768 0.5798 -0.0400 -0.4213 -0.0892 168 TYR A CB  
1278 C CG  . TYR A 164 ? 1.1254 1.1797 0.5859 -0.0335 -0.4172 -0.0623 168 TYR A CG  
1279 C CD1 . TYR A 164 ? 1.1387 1.1899 0.5865 -0.0267 -0.4349 -0.0424 168 TYR A CD1 
1280 C CD2 . TYR A 164 ? 1.0951 1.1421 0.5687 -0.0340 -0.3870 -0.0561 168 TYR A CD2 
1281 C CE1 . TYR A 164 ? 1.1765 1.2105 0.6138 -0.0212 -0.4312 -0.0179 168 TYR A CE1 
1282 C CE2 . TYR A 164 ? 1.0989 1.1318 0.5644 -0.0290 -0.3814 -0.0320 168 TYR A CE2 
1283 C CZ  . TYR A 164 ? 1.2180 1.2408 0.6600 -0.0232 -0.4073 -0.0129 168 TYR A CZ  
1284 O OH  . TYR A 164 ? 1.2970 1.3025 0.7307 -0.0187 -0.4025 0.0111  168 TYR A OH  
1285 N N   . ALA A 165 ? 1.4183 1.4571 0.7497 -0.0520 -0.3848 -0.0738 169 ALA A N   
1286 C CA  . ALA A 165 ? 1.4775 1.5016 0.7710 -0.0567 -0.3580 -0.0647 169 ALA A CA  
1287 C C   . ALA A 165 ? 1.4731 1.4837 0.7789 -0.0520 -0.3558 -0.0389 169 ALA A C   
1288 O O   . ALA A 165 ? 1.5092 1.5183 0.8299 -0.0440 -0.3769 -0.0226 169 ALA A O   
1289 C CB  . ALA A 165 ? 1.4389 1.4599 0.6741 -0.0602 -0.3543 -0.0607 169 ALA A CB  
1290 N N   . ASN A 166 ? 1.3953 1.3985 0.7002 -0.0561 -0.3284 -0.0361 170 ASN A N   
1291 C CA  . ASN A 166 ? 1.3769 1.3717 0.7075 -0.0508 -0.3193 -0.0148 170 ASN A CA  
1292 C C   . ASN A 166 ? 1.4536 1.4281 0.7302 -0.0539 -0.3241 0.0107  170 ASN A C   
1293 O O   . ASN A 166 ? 1.5147 1.4818 0.7572 -0.0619 -0.3003 0.0160  170 ASN A O   
1294 C CB  . ASN A 166 ? 1.3886 1.3875 0.7467 -0.0531 -0.2852 -0.0225 170 ASN A CB  
1295 C CG  . ASN A 166 ? 1.3947 1.3899 0.7965 -0.0461 -0.2785 -0.0068 170 ASN A CG  
1296 O OD1 . ASN A 166 ? 1.4210 1.4047 0.8177 -0.0414 -0.2932 0.0143  170 ASN A OD1 
1297 N ND2 . ASN A 166 ? 1.3510 1.3546 0.7951 -0.0451 -0.2571 -0.0174 170 ASN A ND2 
1298 N N   . ASN A 167 ? 1.4232 1.3938 0.7062 -0.0453 -0.3495 0.0260  171 ASN A N   
1299 C CA  . ASN A 167 ? 1.4349 1.3875 0.6842 -0.0446 -0.3519 0.0520  171 ASN A CA  
1300 C C   . ASN A 167 ? 1.3795 1.3175 0.6566 -0.0379 -0.3548 0.0726  171 ASN A C   
1301 O O   . ASN A 167 ? 1.4580 1.3869 0.7418 -0.0290 -0.3753 0.0894  171 ASN A O   
1302 C CB  . ASN A 167 ? 1.5952 1.5509 0.8289 -0.0393 -0.3785 0.0557  171 ASN A CB  
1303 C CG  . ASN A 167 ? 1.8139 1.7808 1.0104 -0.0465 -0.3743 0.0379  171 ASN A CG  
1304 O OD1 . ASN A 167 ? 1.9320 1.8977 1.0974 -0.0557 -0.3489 0.0310  171 ASN A OD1 
1305 N ND2 . ASN A 167 ? 1.7413 1.7208 0.9428 -0.0419 -0.3990 0.0293  171 ASN A ND2 
1306 N N   . LYS A 168 ? 1.2230 1.1587 0.5179 -0.0416 -0.3338 0.0707  172 LYS A N   
1307 C CA  . LYS A 168 ? 1.2905 1.2169 0.6231 -0.0337 -0.3310 0.0866  172 LYS A CA  
1308 C C   . LYS A 168 ? 1.3311 1.2490 0.6587 -0.0414 -0.2984 0.0938  172 LYS A C   
1309 O O   . LYS A 168 ? 1.4095 1.3162 0.7615 -0.0361 -0.2960 0.1083  172 LYS A O   
1310 C CB  . LYS A 168 ? 1.2018 1.1483 0.6069 -0.0224 -0.3356 0.0724  172 LYS A CB  
1311 C CG  . LYS A 168 ? 1.1934 1.1476 0.6175 -0.0119 -0.3710 0.0708  172 LYS A CG  
1312 C CD  . LYS A 168 ? 1.3845 1.3182 0.8030 -0.0026 -0.3932 0.0956  172 LYS A CD  
1313 C CE  . LYS A 168 ? 1.3634 1.3106 0.8143 0.0101  -0.4253 0.0917  172 LYS A CE  
1314 N NZ  . LYS A 168 ? 1.4214 1.3521 0.8791 0.0215  -0.4412 0.1132  172 LYS A NZ  
1315 N N   . GLU A 169 ? 1.4068 1.3305 0.7060 -0.0531 -0.2736 0.0830  173 GLU A N   
1316 C CA  . GLU A 169 ? 1.4345 1.3533 0.7274 -0.0616 -0.2423 0.0884  173 GLU A CA  
1317 C C   . GLU A 169 ? 1.2936 1.2222 0.6489 -0.0551 -0.2260 0.0811  173 GLU A C   
1318 O O   . GLU A 169 ? 1.2177 1.1405 0.5767 -0.0598 -0.2043 0.0886  173 GLU A O   
1319 C CB  . GLU A 169 ? 1.5340 1.4259 0.7865 -0.0673 -0.2452 0.1171  173 GLU A CB  
1320 C CG  . GLU A 169 ? 1.6023 1.4864 0.7980 -0.0735 -0.2537 0.1246  173 GLU A CG  
1321 C CD  . GLU A 169 ? 1.6826 1.5425 0.8541 -0.0767 -0.2526 0.1519  173 GLU A CD  
1322 O OE1 . GLU A 169 ? 1.7174 1.5625 0.9118 -0.0738 -0.2527 0.1664  173 GLU A OE1 
1323 O OE2 . GLU A 169 ? 1.6322 1.4868 0.7615 -0.0824 -0.2516 0.1586  173 GLU A OE2 
1324 N N   . LYS A 170 ? 1.2756 1.2194 0.6794 -0.0453 -0.2359 0.0665  174 LYS A N   
1325 C CA  . LYS A 170 ? 1.1699 1.1238 0.6310 -0.0395 -0.2214 0.0586  174 LYS A CA  
1326 C C   . LYS A 170 ? 1.1256 1.1006 0.6190 -0.0367 -0.2225 0.0342  174 LYS A C   
1327 O O   . LYS A 170 ? 1.2094 1.1907 0.6850 -0.0380 -0.2373 0.0240  174 LYS A O   
1328 C CB  . LYS A 170 ? 1.2192 1.1645 0.7146 -0.0289 -0.2352 0.0735  174 LYS A CB  
1329 C CG  . LYS A 170 ? 1.3761 1.2974 0.8466 -0.0315 -0.2328 0.0977  174 LYS A CG  
1330 C CD  . LYS A 170 ? 1.5267 1.4381 1.0295 -0.0190 -0.2513 0.1105  174 LYS A CD  
1331 C CE  . LYS A 170 ? 1.6835 1.5664 1.1584 -0.0220 -0.2518 0.1353  174 LYS A CE  
1332 N NZ  . LYS A 170 ? 1.7206 1.5915 1.2258 -0.0084 -0.2720 0.1469  174 LYS A NZ  
1333 N N   . GLU A 171 ? 1.1437 1.1282 0.6837 -0.0335 -0.2072 0.0250  175 GLU A N   
1334 C CA  . GLU A 171 ? 1.0442 1.0459 0.6193 -0.0313 -0.2084 0.0040  175 GLU A CA  
1335 C C   . GLU A 171 ? 0.9723 0.9812 0.5741 -0.0235 -0.2353 0.0042  175 GLU A C   
1336 O O   . GLU A 171 ? 1.0509 1.0549 0.6709 -0.0160 -0.2458 0.0182  175 GLU A O   
1337 C CB  . GLU A 171 ? 1.0645 1.0721 0.6813 -0.0299 -0.1868 -0.0027 175 GLU A CB  
1338 C CG  . GLU A 171 ? 1.1398 1.1471 0.7403 -0.0367 -0.1613 -0.0109 175 GLU A CG  
1339 C CD  . GLU A 171 ? 1.1900 1.2023 0.8320 -0.0344 -0.1433 -0.0171 175 GLU A CD  
1340 O OE1 . GLU A 171 ? 1.0917 1.1017 0.7626 -0.0292 -0.1442 -0.0068 175 GLU A OE1 
1341 O OE2 . GLU A 171 ? 1.1534 1.1711 0.7985 -0.0374 -0.1290 -0.0326 175 GLU A OE2 
1342 N N   . VAL A 172 ? 0.8460 0.8671 0.4519 -0.0250 -0.2466 -0.0126 176 VAL A N   
1343 C CA  . VAL A 172 ? 0.8495 0.8814 0.4815 -0.0189 -0.2730 -0.0151 176 VAL A CA  
1344 C C   . VAL A 172 ? 0.8076 0.8568 0.4886 -0.0194 -0.2676 -0.0336 176 VAL A C   
1345 O O   . VAL A 172 ? 0.8079 0.8615 0.4827 -0.0261 -0.2606 -0.0507 176 VAL A O   
1346 C CB  . VAL A 172 ? 0.8984 0.9293 0.4900 -0.0214 -0.2960 -0.0176 176 VAL A CB  
1347 C CG1 . VAL A 172 ? 0.8959 0.9430 0.5217 -0.0160 -0.3223 -0.0252 176 VAL A CG1 
1348 C CG2 . VAL A 172 ? 0.9422 0.9540 0.4868 -0.0206 -0.3049 0.0043  176 VAL A CG2 
1349 N N   . LEU A 173 ? 0.7759 0.8343 0.5048 -0.0127 -0.2710 -0.0305 177 LEU A N   
1350 C CA  . LEU A 173 ? 0.7396 0.8147 0.5162 -0.0143 -0.2660 -0.0458 177 LEU A CA  
1351 C C   . LEU A 173 ? 0.7546 0.8457 0.5456 -0.0146 -0.2909 -0.0566 177 LEU A C   
1352 O O   . LEU A 173 ? 0.8562 0.9533 0.6571 -0.0072 -0.3125 -0.0490 177 LEU A O   
1353 C CB  . LEU A 173 ? 0.7016 0.7816 0.5221 -0.0079 -0.2573 -0.0386 177 LEU A CB  
1354 C CG  . LEU A 173 ? 0.6682 0.7674 0.5400 -0.0099 -0.2547 -0.0520 177 LEU A CG  
1355 C CD1 . LEU A 173 ? 0.6530 0.7495 0.5239 -0.0193 -0.2356 -0.0654 177 LEU A CD1 
1356 C CD2 . LEU A 173 ? 0.6374 0.7425 0.5483 -0.0027 -0.2479 -0.0443 177 LEU A CD2 
1357 N N   . VAL A 174 ? 0.7689 0.8664 0.5626 -0.0228 -0.2888 -0.0748 178 VAL A N   
1358 C CA  . VAL A 174 ? 0.7685 0.8817 0.5771 -0.0253 -0.3115 -0.0877 178 VAL A CA  
1359 C C   . VAL A 174 ? 0.7324 0.8610 0.5933 -0.0302 -0.3038 -0.1007 178 VAL A C   
1360 O O   . VAL A 174 ? 0.7693 0.8912 0.6355 -0.0359 -0.2822 -0.1072 178 VAL A O   
1361 C CB  . VAL A 174 ? 0.8075 0.9138 0.5709 -0.0324 -0.3187 -0.0993 178 VAL A CB  
1362 C CG1 . VAL A 174 ? 0.8253 0.9479 0.6038 -0.0351 -0.3448 -0.1126 178 VAL A CG1 
1363 C CG2 . VAL A 174 ? 0.8457 0.9358 0.5530 -0.0295 -0.3228 -0.0852 178 VAL A CG2 
1364 N N   . LEU A 175 ? 0.7275 0.8768 0.6272 -0.0282 -0.3219 -0.1044 179 LEU A N   
1365 C CA  . LEU A 175 ? 0.6979 0.8647 0.6484 -0.0346 -0.3163 -0.1164 179 LEU A CA  
1366 C C   . LEU A 175 ? 0.7178 0.9018 0.6819 -0.0405 -0.3395 -0.1314 179 LEU A C   
1367 O O   . LEU A 175 ? 0.7556 0.9454 0.7061 -0.0353 -0.3642 -0.1292 179 LEU A O   
1368 C CB  . LEU A 175 ? 0.6665 0.8478 0.6627 -0.0274 -0.3118 -0.1078 179 LEU A CB  
1369 C CG  . LEU A 175 ? 0.7932 0.9599 0.7831 -0.0213 -0.2903 -0.0935 179 LEU A CG  
1370 C CD1 . LEU A 175 ? 0.6636 0.8219 0.6316 -0.0091 -0.3022 -0.0770 179 LEU A CD1 
1371 C CD2 . LEU A 175 ? 0.6067 0.7878 0.6463 -0.0218 -0.2758 -0.0946 179 LEU A CD2 
1372 N N   . TRP A 176 ? 0.7042 0.8951 0.6950 -0.0520 -0.3324 -0.1463 180 TRP A N   
1373 C CA  . TRP A 176 ? 0.7204 0.9289 0.7308 -0.0598 -0.3530 -0.1622 180 TRP A CA  
1374 C C   . TRP A 176 ? 0.6930 0.9124 0.7498 -0.0716 -0.3400 -0.1727 180 TRP A C   
1375 O O   . TRP A 176 ? 0.8353 1.0467 0.9036 -0.0731 -0.3161 -0.1673 180 TRP A O   
1376 C CB  . TRP A 176 ? 0.7591 0.9531 0.7230 -0.0652 -0.3633 -0.1733 180 TRP A CB  
1377 C CG  . TRP A 176 ? 0.7553 0.9288 0.7017 -0.0739 -0.3421 -0.1826 180 TRP A CG  
1378 C CD1 . TRP A 176 ? 0.7565 0.9294 0.7194 -0.0865 -0.3403 -0.2001 180 TRP A CD1 
1379 C CD2 . TRP A 176 ? 0.7515 0.9018 0.6625 -0.0703 -0.3204 -0.1753 180 TRP A CD2 
1380 N NE1 . TRP A 176 ? 0.7546 0.9039 0.6941 -0.0895 -0.3198 -0.2042 180 TRP A NE1 
1381 C CE2 . TRP A 176 ? 0.7504 0.8875 0.6591 -0.0796 -0.3071 -0.1897 180 TRP A CE2 
1382 C CE3 . TRP A 176 ? 0.7504 0.8899 0.6327 -0.0605 -0.3114 -0.1584 180 TRP A CE3 
1383 C CZ2 . TRP A 176 ? 0.7471 0.8629 0.6278 -0.0779 -0.2856 -0.1884 180 TRP A CZ2 
1384 C CZ3 . TRP A 176 ? 0.7464 0.8661 0.6011 -0.0606 -0.2891 -0.1571 180 TRP A CZ3 
1385 C CH2 . TRP A 176 ? 0.7441 0.8534 0.5991 -0.0686 -0.2767 -0.1724 180 TRP A CH2 
1386 N N   . GLY A 177 ? 0.7043 0.9416 0.7867 -0.0810 -0.3566 -0.1875 181 GLY A N   
1387 C CA  . GLY A 177 ? 0.6839 0.9325 0.8110 -0.0946 -0.3463 -0.1974 181 GLY A CA  
1388 C C   . GLY A 177 ? 0.7088 0.9558 0.8339 -0.1088 -0.3584 -0.2165 181 GLY A C   
1389 O O   . GLY A 177 ? 0.7419 0.9858 0.8371 -0.1072 -0.3786 -0.2236 181 GLY A O   
1390 N N   . VAL A 178 ? 0.7723 1.0200 0.9283 -0.1233 -0.3458 -0.2247 182 VAL A N   
1391 C CA  . VAL A 178 ? 0.7170 0.9624 0.8792 -0.1392 -0.3555 -0.2435 182 VAL A CA  
1392 C C   . VAL A 178 ? 0.7235 0.9957 0.9458 -0.1527 -0.3544 -0.2487 182 VAL A C   
1393 O O   . VAL A 178 ? 0.7085 0.9802 0.9542 -0.1571 -0.3324 -0.2412 182 VAL A O   
1394 C CB  . VAL A 178 ? 0.8028 1.0125 0.9340 -0.1458 -0.3392 -0.2493 182 VAL A CB  
1395 C CG1 . VAL A 178 ? 0.7792 0.9854 0.9231 -0.1634 -0.3491 -0.2691 182 VAL A CG1 
1396 C CG2 . VAL A 178 ? 0.8007 0.9883 0.8738 -0.1337 -0.3403 -0.2469 182 VAL A CG2 
1397 N N   . HIS A 179 ? 0.8097 1.1051 1.0552 -0.1598 -0.3766 -0.2605 183 HIS A N   
1398 C CA  . HIS A 179 ? 0.7079 1.0313 1.0087 -0.1724 -0.3730 -0.2625 183 HIS A CA  
1399 C C   . HIS A 179 ? 0.7202 1.0273 1.0286 -0.1939 -0.3635 -0.2728 183 HIS A C   
1400 O O   . HIS A 179 ? 0.7509 1.0348 1.0273 -0.1990 -0.3708 -0.2823 183 HIS A O   
1401 C CB  . HIS A 179 ? 0.7275 1.0803 1.0451 -0.1684 -0.3948 -0.2637 183 HIS A CB  
1402 C CG  . HIS A 179 ? 0.7806 1.1680 1.1575 -0.1784 -0.3908 -0.2649 183 HIS A CG  
1403 N ND1 . HIS A 179 ? 0.8156 1.2247 1.2139 -0.1858 -0.4064 -0.2722 183 HIS A ND1 
1404 C CD2 . HIS A 179 ? 0.7924 1.1974 1.2108 -0.1826 -0.3721 -0.2600 183 HIS A CD2 
1405 C CE1 . HIS A 179 ? 0.8252 1.2645 1.2765 -0.1941 -0.3973 -0.2719 183 HIS A CE1 
1406 N NE2 . HIS A 179 ? 0.8494 1.2867 1.3129 -0.1924 -0.3759 -0.2645 183 HIS A NE2 
1407 N N   . HIS A 180 ? 0.7259 1.0443 1.0756 -0.2066 -0.3466 -0.2706 184 HIS A N   
1408 C CA  . HIS A 180 ? 0.7865 1.0891 1.1473 -0.2286 -0.3364 -0.2774 184 HIS A CA  
1409 C C   . HIS A 180 ? 0.8224 1.1595 1.2357 -0.2423 -0.3345 -0.2774 184 HIS A C   
1410 O O   . HIS A 180 ? 0.7675 1.1212 1.2133 -0.2460 -0.3173 -0.2699 184 HIS A O   
1411 C CB  . HIS A 180 ? 0.8111 1.0856 1.1633 -0.2332 -0.3140 -0.2729 184 HIS A CB  
1412 C CG  . HIS A 180 ? 0.7706 1.0115 1.0715 -0.2191 -0.3127 -0.2718 184 HIS A CG  
1413 N ND1 . HIS A 180 ? 0.7195 0.9224 0.9891 -0.2252 -0.3105 -0.2802 184 HIS A ND1 
1414 C CD2 . HIS A 180 ? 0.6842 0.9216 0.9555 -0.1983 -0.3095 -0.2599 184 HIS A CD2 
1415 C CE1 . HIS A 180 ? 0.7198 0.9003 0.9444 -0.2085 -0.3054 -0.2743 184 HIS A CE1 
1416 N NE2 . HIS A 180 ? 0.6989 0.8993 0.9229 -0.1929 -0.3045 -0.2614 184 HIS A NE2 
1417 N N   . PRO A 181 ? 0.7628 1.1125 1.1853 -0.2502 -0.3511 -0.2860 185 PRO A N   
1418 C CA  . PRO A 181 ? 0.7473 1.1335 1.2208 -0.2624 -0.3507 -0.2868 185 PRO A CA  
1419 C C   . PRO A 181 ? 0.8950 1.2704 1.3889 -0.2863 -0.3314 -0.2866 185 PRO A C   
1420 O O   . PRO A 181 ? 0.8993 1.2352 1.3656 -0.2944 -0.3231 -0.2880 185 PRO A O   
1421 C CB  . PRO A 181 ? 0.7740 1.1697 1.2426 -0.2643 -0.3756 -0.2972 185 PRO A CB  
1422 C CG  . PRO A 181 ? 0.7874 1.1591 1.2033 -0.2477 -0.3895 -0.2990 185 PRO A CG  
1423 C CD  . PRO A 181 ? 0.7832 1.1176 1.1689 -0.2465 -0.3718 -0.2955 185 PRO A CD  
1424 N N   . PRO A 182 ? 0.9694 1.3779 1.5106 -0.2978 -0.3236 -0.2844 186 PRO A N   
1425 C CA  . PRO A 182 ? 0.9723 1.3706 1.5317 -0.3219 -0.3040 -0.2817 186 PRO A CA  
1426 C C   . PRO A 182 ? 1.0521 1.4308 1.6056 -0.3426 -0.3128 -0.2909 186 PRO A C   
1427 O O   . PRO A 182 ? 1.2447 1.5874 1.7828 -0.3575 -0.3015 -0.2895 186 PRO A O   
1428 C CB  . PRO A 182 ? 0.8731 1.3186 1.4842 -0.3254 -0.2945 -0.2771 186 PRO A CB  
1429 C CG  . PRO A 182 ? 0.8507 1.3303 1.4751 -0.3091 -0.3168 -0.2825 186 PRO A CG  
1430 C CD  . PRO A 182 ? 0.8818 1.3383 1.4611 -0.2876 -0.3303 -0.2827 186 PRO A CD  
1431 N N   . ASN A 183 ? 0.8071 1.2080 1.3727 -0.3437 -0.3335 -0.3002 187 ASN A N   
1432 C CA  . ASN A 183 ? 0.9390 1.3258 1.5030 -0.3639 -0.3433 -0.3101 187 ASN A CA  
1433 C C   . ASN A 183 ? 1.0691 1.4484 1.6023 -0.3528 -0.3688 -0.3214 187 ASN A C   
1434 O O   . ASN A 183 ? 1.1014 1.4878 1.6158 -0.3304 -0.3788 -0.3203 187 ASN A O   
1435 C CB  . ASN A 183 ? 0.9449 1.3696 1.5603 -0.3823 -0.3421 -0.3110 187 ASN A CB  
1436 C CG  . ASN A 183 ? 0.9138 1.3890 1.5602 -0.3677 -0.3553 -0.3129 187 ASN A CG  
1437 O OD1 . ASN A 183 ? 0.8902 1.3751 1.5299 -0.3611 -0.3786 -0.3219 187 ASN A OD1 
1438 N ND2 . ASN A 183 ? 0.9237 1.4307 1.6039 -0.3625 -0.3404 -0.3045 187 ASN A ND2 
1439 N N   . ILE A 184 ? 1.1669 1.5305 1.6936 -0.3695 -0.3792 -0.3321 188 ILE A N   
1440 C CA  . ILE A 184 ? 1.2505 1.6046 1.7454 -0.3617 -0.4024 -0.3442 188 ILE A CA  
1441 C C   . ILE A 184 ? 1.3289 1.7283 1.8492 -0.3547 -0.4225 -0.3479 188 ILE A C   
1442 O O   . ILE A 184 ? 1.2859 1.6860 1.7784 -0.3392 -0.4414 -0.3529 188 ILE A O   
1443 C CB  . ILE A 184 ? 1.2467 1.5675 1.7263 -0.3823 -0.4061 -0.3554 188 ILE A CB  
1444 C CG1 . ILE A 184 ? 1.2169 1.4950 1.6809 -0.3917 -0.3849 -0.3499 188 ILE A CG1 
1445 C CG2 . ILE A 184 ? 1.2123 1.5149 1.6489 -0.3726 -0.4263 -0.3682 188 ILE A CG2 
1446 C CD1 . ILE A 184 ? 1.3158 1.5581 1.7665 -0.4123 -0.3875 -0.3601 188 ILE A CD1 
1447 N N   . GLY A 185 ? 1.3431 1.7807 1.9152 -0.3657 -0.4189 -0.3454 189 GLY A N   
1448 C CA  . GLY A 185 ? 1.2867 1.7685 1.8871 -0.3588 -0.4383 -0.3494 189 GLY A CA  
1449 C C   . GLY A 185 ? 1.3072 1.8067 1.8992 -0.3305 -0.4452 -0.3424 189 GLY A C   
1450 O O   . GLY A 185 ? 1.2840 1.7967 1.8653 -0.3180 -0.4682 -0.3470 189 GLY A O   
1451 N N   . ASP A 186 ? 1.2439 1.7425 1.8394 -0.3204 -0.4261 -0.3308 190 ASP A N   
1452 C CA  . ASP A 186 ? 1.0982 1.6086 1.6827 -0.2935 -0.4320 -0.3233 190 ASP A CA  
1453 C C   . ASP A 186 ? 0.9655 1.4393 1.4894 -0.2795 -0.4418 -0.3240 190 ASP A C   
1454 O O   . ASP A 186 ? 0.9313 1.4133 1.4375 -0.2593 -0.4573 -0.3208 190 ASP A O   
1455 C CB  . ASP A 186 ? 1.0611 1.5808 1.6671 -0.2876 -0.4081 -0.3115 190 ASP A CB  
1456 C CG  . ASP A 186 ? 1.1733 1.7358 1.8393 -0.2972 -0.3988 -0.3106 190 ASP A CG  
1457 O OD1 . ASP A 186 ? 1.2794 1.8781 1.9723 -0.2822 -0.4079 -0.3092 190 ASP A OD1 
1458 O OD2 . ASP A 186 ? 1.1649 1.7243 1.8506 -0.3198 -0.3823 -0.3112 190 ASP A OD2 
1459 N N   . GLN A 187 ? 0.8765 1.3092 1.3672 -0.2899 -0.4330 -0.3279 191 GLN A N   
1460 C CA  . GLN A 187 ? 0.8914 1.2894 1.3239 -0.2781 -0.4409 -0.3305 191 GLN A CA  
1461 C C   . GLN A 187 ? 0.9309 1.3353 1.3439 -0.2747 -0.4677 -0.3400 191 GLN A C   
1462 O O   . GLN A 187 ? 0.9353 1.3439 1.3223 -0.2559 -0.4816 -0.3363 191 GLN A O   
1463 C CB  . GLN A 187 ? 0.8999 1.2542 1.3065 -0.2912 -0.4263 -0.3351 191 GLN A CB  
1464 C CG  . GLN A 187 ? 0.9273 1.2464 1.2759 -0.2834 -0.4356 -0.3428 191 GLN A CG  
1465 C CD  . GLN A 187 ? 1.0080 1.3208 1.3221 -0.2600 -0.4357 -0.3343 191 GLN A CD  
1466 O OE1 . GLN A 187 ? 0.9601 1.2742 1.2831 -0.2523 -0.4203 -0.3233 191 GLN A OE1 
1467 N NE2 . GLN A 187 ? 1.0505 1.3562 1.3237 -0.2494 -0.4529 -0.3392 191 GLN A NE2 
1468 N N   . ARG A 188 ? 1.1373 1.5412 1.5610 -0.2937 -0.4755 -0.3519 192 ARG A N   
1469 C CA  . ARG A 188 ? 1.0463 1.4581 1.4540 -0.2924 -0.5014 -0.3620 192 ARG A CA  
1470 C C   . ARG A 188 ? 0.9991 1.4544 1.4355 -0.2799 -0.5178 -0.3570 192 ARG A C   
1471 O O   . ARG A 188 ? 1.0243 1.4837 1.4343 -0.2682 -0.5392 -0.3590 192 ARG A O   
1472 C CB  . ARG A 188 ? 1.1475 1.5545 1.5697 -0.3167 -0.5060 -0.3756 192 ARG A CB  
1473 C CG  . ARG A 188 ? 1.2364 1.5974 1.6290 -0.3292 -0.4928 -0.3821 192 ARG A CG  
1474 C CD  . ARG A 188 ? 1.2681 1.6262 1.6792 -0.3538 -0.4986 -0.3948 192 ARG A CD  
1475 N NE  . ARG A 188 ? 1.2963 1.6091 1.6844 -0.3665 -0.4852 -0.4004 192 ARG A NE  
1476 C CZ  . ARG A 188 ? 1.2570 1.5582 1.6601 -0.3899 -0.4849 -0.4092 192 ARG A CZ  
1477 N NH1 . ARG A 188 ? 1.1605 1.4941 1.6025 -0.4039 -0.4967 -0.4138 192 ARG A NH1 
1478 N NH2 . ARG A 188 ? 1.3503 1.6071 1.7301 -0.3990 -0.4729 -0.4135 192 ARG A NH2 
1479 N N   . ALA A 189 ? 0.9700 1.4575 1.4593 -0.2819 -0.5079 -0.3503 193 ALA A N   
1480 C CA  . ALA A 189 ? 0.9660 1.4958 1.4878 -0.2691 -0.5225 -0.3463 193 ALA A CA  
1481 C C   . ALA A 189 ? 1.0400 1.5673 1.5345 -0.2424 -0.5278 -0.3348 193 ALA A C   
1482 O O   . ALA A 189 ? 0.9617 1.5141 1.4651 -0.2286 -0.5472 -0.3323 193 ALA A O   
1483 C CB  . ALA A 189 ? 0.9388 1.5029 1.5238 -0.2778 -0.5072 -0.3429 193 ALA A CB  
1484 N N   . LEU A 190 ? 1.1659 1.6629 1.6275 -0.2351 -0.5118 -0.3274 194 LEU A N   
1485 C CA  . LEU A 190 ? 1.1671 1.6596 1.6022 -0.2111 -0.5151 -0.3153 194 LEU A CA  
1486 C C   . LEU A 190 ? 1.1199 1.5796 1.4886 -0.2027 -0.5266 -0.3161 194 LEU A C   
1487 O O   . LEU A 190 ? 1.0967 1.5595 1.4422 -0.1843 -0.5408 -0.3080 194 LEU A O   
1488 C CB  . LEU A 190 ? 1.1262 1.6104 1.5701 -0.2066 -0.4894 -0.3052 194 LEU A CB  
1489 C CG  . LEU A 190 ? 1.1115 1.6320 1.6158 -0.2062 -0.4778 -0.3001 194 LEU A CG  
1490 C CD1 . LEU A 190 ? 1.0352 1.5434 1.5402 -0.2020 -0.4525 -0.2906 194 LEU A CD1 
1491 C CD2 . LEU A 190 ? 1.1364 1.6889 1.6601 -0.1878 -0.4969 -0.2955 194 LEU A CD2 
1492 N N   . TYR A 191 ? 0.9595 1.3875 1.2961 -0.2154 -0.5207 -0.3255 195 TYR A N   
1493 C CA  . TYR A 191 ? 0.9851 1.3816 1.2573 -0.2075 -0.5274 -0.3269 195 TYR A CA  
1494 C C   . TYR A 191 ? 1.1156 1.5006 1.3630 -0.2196 -0.5420 -0.3422 195 TYR A C   
1495 O O   . TYR A 191 ? 1.0581 1.4163 1.2504 -0.2150 -0.5456 -0.3455 195 TYR A O   
1496 C CB  . TYR A 191 ? 1.0173 1.3798 1.2620 -0.2062 -0.5044 -0.3236 195 TYR A CB  
1497 C CG  . TYR A 191 ? 0.9168 1.2882 1.1812 -0.1939 -0.4901 -0.3089 195 TYR A CG  
1498 C CD1 . TYR A 191 ? 0.9120 1.2865 1.1541 -0.1736 -0.4977 -0.2965 195 TYR A CD1 
1499 C CD2 . TYR A 191 ? 0.8820 1.2580 1.1864 -0.2033 -0.4692 -0.3070 195 TYR A CD2 
1500 C CE1 . TYR A 191 ? 0.9672 1.3490 1.2275 -0.1623 -0.4852 -0.2836 195 TYR A CE1 
1501 C CE2 . TYR A 191 ? 0.9397 1.3246 1.2618 -0.1923 -0.4558 -0.2945 195 TYR A CE2 
1502 C CZ  . TYR A 191 ? 0.8787 1.2665 1.1795 -0.1715 -0.4642 -0.2834 195 TYR A CZ  
1503 O OH  . TYR A 191 ? 0.8000 1.1955 1.1186 -0.1606 -0.4514 -0.2716 195 TYR A OH  
1504 N N   . HIS A 192 ? 1.1701 1.5751 1.4560 -0.2353 -0.5498 -0.3520 196 HIS A N   
1505 C CA  . HIS A 192 ? 1.1430 1.5419 1.4108 -0.2471 -0.5665 -0.3671 196 HIS A CA  
1506 C C   . HIS A 192 ? 1.1713 1.5281 1.3977 -0.2565 -0.5558 -0.3777 196 HIS A C   
1507 O O   . HIS A 192 ? 1.2644 1.6092 1.4608 -0.2625 -0.5691 -0.3903 196 HIS A O   
1508 C CB  . HIS A 192 ? 1.2365 1.6461 1.4737 -0.2339 -0.5921 -0.3658 196 HIS A CB  
1509 C CG  . HIS A 192 ? 1.3226 1.7710 1.5976 -0.2222 -0.6051 -0.3556 196 HIS A CG  
1510 N ND1 . HIS A 192 ? 1.3380 1.8212 1.6724 -0.2317 -0.6108 -0.3599 196 HIS A ND1 
1511 C CD2 . HIS A 192 ? 1.3276 1.7850 1.5899 -0.2014 -0.6134 -0.3417 196 HIS A CD2 
1512 C CE1 . HIS A 192 ? 1.3299 1.8425 1.6877 -0.2162 -0.6220 -0.3499 196 HIS A CE1 
1513 N NE2 . HIS A 192 ? 1.3409 1.8373 1.6555 -0.1975 -0.6243 -0.3384 196 HIS A NE2 
1514 N N   . LYS A 193 ? 1.2359 1.5697 1.4596 -0.2573 -0.5321 -0.3734 197 LYS A N   
1515 C CA  . LYS A 193 ? 1.2849 1.5775 1.4715 -0.2641 -0.5208 -0.3833 197 LYS A CA  
1516 C C   . LYS A 193 ? 1.3502 1.6301 1.5681 -0.2771 -0.4984 -0.3822 197 LYS A C   
1517 O O   . LYS A 193 ? 1.2937 1.5937 1.5520 -0.2769 -0.4881 -0.3712 197 LYS A O   
1518 C CB  . LYS A 193 ? 1.1640 1.4325 1.2947 -0.2468 -0.5154 -0.3783 197 LYS A CB  
1519 C CG  . LYS A 193 ? 1.1330 1.4089 1.2240 -0.2353 -0.5362 -0.3783 197 LYS A CG  
1520 C CD  . LYS A 193 ? 1.1326 1.3840 1.1677 -0.2205 -0.5280 -0.3729 197 LYS A CD  
1521 C CE  . LYS A 193 ? 1.1668 1.4265 1.1611 -0.2097 -0.5477 -0.3697 197 LYS A CE  
1522 N NZ  . LYS A 193 ? 1.4849 1.7400 1.4571 -0.2201 -0.5636 -0.3864 197 LYS A NZ  
1523 N N   . GLU A 194 ? 1.4899 1.7352 1.6876 -0.2882 -0.4909 -0.3936 198 GLU A N   
1524 C CA  . GLU A 194 ? 1.4977 1.7244 1.7191 -0.3018 -0.4708 -0.3928 198 GLU A CA  
1525 C C   . GLU A 194 ? 1.4449 1.6365 1.6344 -0.2924 -0.4519 -0.3891 198 GLU A C   
1526 O O   . GLU A 194 ? 1.4110 1.5939 1.6222 -0.2975 -0.4336 -0.3813 198 GLU A O   
1527 C CB  . GLU A 194 ? 1.7293 1.9402 1.9571 -0.3230 -0.4757 -0.4079 198 GLU A CB  
1528 C CG  . GLU A 194 ? 1.7909 1.9860 2.0490 -0.3408 -0.4576 -0.4054 198 GLU A CG  
1529 C CD  . GLU A 194 ? 1.8610 2.0424 2.1277 -0.3629 -0.4645 -0.4194 198 GLU A CD  
1530 O OE1 . GLU A 194 ? 1.8897 2.0798 2.1452 -0.3648 -0.4841 -0.4314 198 GLU A OE1 
1531 O OE2 . GLU A 194 ? 1.8751 2.0361 2.1588 -0.3788 -0.4506 -0.4181 198 GLU A OE2 
1532 N N   . ASN A 195 ? 1.4944 1.6663 1.6327 -0.2791 -0.4556 -0.3942 199 ASN A N   
1533 C CA  . ASN A 195 ? 1.4858 1.6256 1.5914 -0.2687 -0.4384 -0.3921 199 ASN A CA  
1534 C C   . ASN A 195 ? 1.4057 1.5533 1.4744 -0.2482 -0.4432 -0.3853 199 ASN A C   
1535 O O   . ASN A 195 ? 1.4324 1.5681 1.4568 -0.2424 -0.4514 -0.3942 199 ASN A O   
1536 C CB  . ASN A 195 ? 1.6317 1.7327 1.7086 -0.2758 -0.4351 -0.4084 199 ASN A CB  
1537 C CG  . ASN A 195 ? 1.6953 1.7868 1.8058 -0.2974 -0.4331 -0.4149 199 ASN A CG  
1538 O OD1 . ASN A 195 ? 1.6862 1.7841 1.8351 -0.3063 -0.4222 -0.4050 199 ASN A OD1 
1539 N ND2 . ASN A 195 ? 1.7034 1.7794 1.7986 -0.3069 -0.4435 -0.4315 199 ASN A ND2 
1540 N N   . ALA A 196 ? 1.0195 1.1865 1.1051 -0.2380 -0.4377 -0.3694 200 ALA A N   
1541 C CA  . ALA A 196 ? 1.0130 1.1878 1.0665 -0.2192 -0.4422 -0.3602 200 ALA A CA  
1542 C C   . ALA A 196 ? 0.9946 1.1431 1.0189 -0.2088 -0.4232 -0.3562 200 ALA A C   
1543 O O   . ALA A 196 ? 0.9856 1.1107 1.0167 -0.2150 -0.4073 -0.3602 200 ALA A O   
1544 C CB  . ALA A 196 ? 0.9836 1.1951 1.0724 -0.2128 -0.4490 -0.3455 200 ALA A CB  
1545 N N   . TYR A 197 ? 1.0319 1.1838 1.0228 -0.1928 -0.4253 -0.3475 201 TYR A N   
1546 C CA  . TYR A 197 ? 1.0523 1.1824 1.0132 -0.1820 -0.4081 -0.3435 201 TYR A CA  
1547 C C   . TYR A 197 ? 1.0624 1.2074 1.0057 -0.1662 -0.4118 -0.3278 201 TYR A C   
1548 O O   . TYR A 197 ? 1.0842 1.2478 1.0189 -0.1622 -0.4296 -0.3233 201 TYR A O   
1549 C CB  . TYR A 197 ? 1.1296 1.2304 1.0423 -0.1815 -0.4038 -0.3581 201 TYR A CB  
1550 C CG  . TYR A 197 ? 1.2562 1.3610 1.1200 -0.1734 -0.4161 -0.3588 201 TYR A CG  
1551 C CD1 . TYR A 197 ? 1.4082 1.5259 1.2676 -0.1797 -0.4364 -0.3652 201 TYR A CD1 
1552 C CD2 . TYR A 197 ? 1.2574 1.3528 1.0782 -0.1604 -0.4069 -0.3526 201 TYR A CD2 
1553 C CE1 . TYR A 197 ? 1.4028 1.5232 1.2150 -0.1734 -0.4476 -0.3648 201 TYR A CE1 
1554 C CE2 . TYR A 197 ? 1.2738 1.3718 1.0471 -0.1549 -0.4168 -0.3517 201 TYR A CE2 
1555 C CZ  . TYR A 197 ? 1.3225 1.4325 1.0910 -0.1614 -0.4373 -0.3575 201 TYR A CZ  
1556 O OH  . TYR A 197 ? 1.4465 1.5585 1.1658 -0.1569 -0.4473 -0.3559 201 TYR A OH  
1557 N N   . VAL A 198 ? 1.0428 1.1786 0.9808 -0.1573 -0.3956 -0.3191 202 VAL A N   
1558 C CA  . VAL A 198 ? 0.9212 1.0633 0.8333 -0.1421 -0.3965 -0.3046 202 VAL A CA  
1559 C C   . VAL A 198 ? 0.9260 1.0421 0.7941 -0.1351 -0.3798 -0.3076 202 VAL A C   
1560 O O   . VAL A 198 ? 0.9928 1.0907 0.8693 -0.1390 -0.3637 -0.3152 202 VAL A O   
1561 C CB  . VAL A 198 ? 0.8764 1.0381 0.8299 -0.1369 -0.3933 -0.2892 202 VAL A CB  
1562 C CG1 . VAL A 198 ? 0.8728 1.0388 0.7980 -0.1211 -0.3967 -0.2731 202 VAL A CG1 
1563 C CG2 . VAL A 198 ? 0.8784 1.0681 0.8815 -0.1447 -0.4065 -0.2885 202 VAL A CG2 
1564 N N   . SER A 199 ? 1.1010 1.2150 0.9218 -0.1253 -0.3833 -0.3016 203 SER A N   
1565 C CA  . SER A 199 ? 1.0715 1.1643 0.8476 -0.1190 -0.3668 -0.3051 203 SER A CA  
1566 C C   . SER A 199 ? 1.0295 1.1270 0.7777 -0.1069 -0.3642 -0.2854 203 SER A C   
1567 O O   . SER A 199 ? 1.2165 1.3237 0.9412 -0.1036 -0.3816 -0.2785 203 SER A O   
1568 C CB  . SER A 199 ? 1.2059 1.2854 0.9416 -0.1238 -0.3694 -0.3210 203 SER A CB  
1569 O OG  . SER A 199 ? 1.3863 1.4487 1.0802 -0.1173 -0.3518 -0.3247 203 SER A OG  
1570 N N   . VAL A 200 ? 0.9469 1.0355 0.6986 -0.1012 -0.3392 -0.2721 204 VAL A N   
1571 C CA  . VAL A 200 ? 0.9145 1.0036 0.6408 -0.0911 -0.3309 -0.2510 204 VAL A CA  
1572 C C   . VAL A 200 ? 0.9962 1.0674 0.6849 -0.0882 -0.3084 -0.2551 204 VAL A C   
1573 O O   . VAL A 200 ? 0.9328 0.9930 0.6391 -0.0894 -0.2897 -0.2612 204 VAL A O   
1574 C CB  . VAL A 200 ? 0.8689 0.9668 0.6363 -0.0865 -0.3217 -0.2306 204 VAL A CB  
1575 C CG1 . VAL A 200 ? 0.8688 0.9661 0.6093 -0.0767 -0.3174 -0.2090 204 VAL A CG1 
1576 C CG2 . VAL A 200 ? 0.8576 0.9760 0.6710 -0.0904 -0.3410 -0.2308 204 VAL A CG2 
1577 N N   . VAL A 201 ? 1.1260 1.1945 0.7633 -0.0845 -0.3105 -0.2518 205 VAL A N   
1578 C CA  . VAL A 201 ? 1.1305 1.1861 0.7307 -0.0823 -0.2889 -0.2574 205 VAL A CA  
1579 C C   . VAL A 201 ? 1.0774 1.1337 0.6413 -0.0768 -0.2826 -0.2366 205 VAL A C   
1580 O O   . VAL A 201 ? 1.1632 1.2256 0.7056 -0.0759 -0.3015 -0.2260 205 VAL A O   
1581 C CB  . VAL A 201 ? 1.1761 1.2251 0.7419 -0.0871 -0.2951 -0.2838 205 VAL A CB  
1582 C CG1 . VAL A 201 ? 1.1606 1.2012 0.7604 -0.0920 -0.2922 -0.3049 205 VAL A CG1 
1583 C CG2 . VAL A 201 ? 1.3338 1.3916 0.8756 -0.0903 -0.3238 -0.2864 205 VAL A CG2 
1584 N N   . SER A 202 ? 1.1103 1.1597 0.6679 -0.0733 -0.2572 -0.2306 206 SER A N   
1585 C CA  . SER A 202 ? 1.2219 1.2699 0.7409 -0.0703 -0.2475 -0.2133 206 SER A CA  
1586 C C   . SER A 202 ? 1.4999 1.5416 0.9866 -0.0711 -0.2258 -0.2279 206 SER A C   
1587 O O   . SER A 202 ? 1.6231 1.6613 1.1084 -0.0734 -0.2242 -0.2523 206 SER A O   
1588 C CB  . SER A 202 ? 1.1010 1.1500 0.6487 -0.0652 -0.2374 -0.1892 206 SER A CB  
1589 O OG  . SER A 202 ? 1.0984 1.1425 0.6664 -0.0634 -0.2124 -0.1924 206 SER A OG  
1590 N N   . SER A 203 ? 1.8071 1.8477 1.2688 -0.0694 -0.2085 -0.2138 207 SER A N   
1591 C CA  . SER A 203 ? 1.9742 2.0128 1.4097 -0.0700 -0.1856 -0.2276 207 SER A CA  
1592 C C   . SER A 203 ? 2.0645 2.0998 1.5416 -0.0662 -0.1675 -0.2385 207 SER A C   
1593 O O   . SER A 203 ? 2.0894 2.1224 1.5580 -0.0656 -0.1558 -0.2606 207 SER A O   
1594 C CB  . SER A 203 ? 1.9790 2.0190 1.3789 -0.0709 -0.1715 -0.2087 207 SER A CB  
1595 O OG  . SER A 203 ? 1.9338 1.9728 1.3646 -0.0674 -0.1642 -0.1863 207 SER A OG  
1596 N N   . HIS A 204 ? 2.0653 2.0997 1.5866 -0.0631 -0.1656 -0.2239 208 HIS A N   
1597 C CA  . HIS A 204 ? 2.0560 2.0855 1.6162 -0.0595 -0.1504 -0.2313 208 HIS A CA  
1598 C C   . HIS A 204 ? 1.8817 1.9085 1.4899 -0.0599 -0.1618 -0.2290 208 HIS A C   
1599 O O   . HIS A 204 ? 1.9162 1.9361 1.5553 -0.0580 -0.1518 -0.2355 208 HIS A O   
1600 C CB  . HIS A 204 ? 2.1269 2.1580 1.6917 -0.0558 -0.1288 -0.2158 208 HIS A CB  
1601 C CG  . HIS A 204 ? 2.2227 2.2582 1.7454 -0.0567 -0.1132 -0.2194 208 HIS A CG  
1602 N ND1 . HIS A 204 ? 2.2550 2.2909 1.7646 -0.0556 -0.1010 -0.2434 208 HIS A ND1 
1603 C CD2 . HIS A 204 ? 2.2576 2.2977 1.7486 -0.0592 -0.1072 -0.2024 208 HIS A CD2 
1604 C CE1 . HIS A 204 ? 2.2861 2.3294 1.7584 -0.0577 -0.0869 -0.2416 208 HIS A CE1 
1605 N NE2 . HIS A 204 ? 2.2894 2.3344 1.7487 -0.0608 -0.0903 -0.2161 208 HIS A NE2 
1606 N N   . TYR A 205 ? 1.5134 1.5457 1.1289 -0.0626 -0.1824 -0.2200 209 TYR A N   
1607 C CA  . TYR A 205 ? 1.0976 1.1308 0.7572 -0.0650 -0.1942 -0.2212 209 TYR A CA  
1608 C C   . TYR A 205 ? 1.0639 1.0968 0.7174 -0.0708 -0.2131 -0.2413 209 TYR A C   
1609 O O   . TYR A 205 ? 1.2093 1.2466 0.8276 -0.0725 -0.2264 -0.2449 209 TYR A O   
1610 C CB  . TYR A 205 ? 1.1033 1.1462 0.7829 -0.0635 -0.2042 -0.1991 209 TYR A CB  
1611 C CG  . TYR A 205 ? 1.0170 1.0650 0.7440 -0.0668 -0.2146 -0.2002 209 TYR A CG  
1612 C CD1 . TYR A 205 ? 1.0124 1.0688 0.7461 -0.0717 -0.2375 -0.2080 209 TYR A CD1 
1613 C CD2 . TYR A 205 ? 0.9930 1.0386 0.7576 -0.0660 -0.2014 -0.1934 209 TYR A CD2 
1614 C CE1 . TYR A 205 ? 0.9467 1.0105 0.7257 -0.0763 -0.2455 -0.2095 209 TYR A CE1 
1615 C CE2 . TYR A 205 ? 0.9327 0.9841 0.7391 -0.0707 -0.2089 -0.1941 209 TYR A CE2 
1616 C CZ  . TYR A 205 ? 0.9749 1.0363 0.7895 -0.0762 -0.2303 -0.2023 209 TYR A CZ  
1617 O OH  . TYR A 205 ? 0.8679 0.9378 0.7260 -0.0823 -0.2365 -0.2036 209 TYR A OH  
1618 N N   . SER A 206 ? 0.9090 0.9357 0.5960 -0.0747 -0.2148 -0.2541 210 SER A N   
1619 C CA  . SER A 206 ? 0.9558 0.9802 0.6413 -0.0815 -0.2322 -0.2751 210 SER A CA  
1620 C C   . SER A 206 ? 0.9959 1.0162 0.7300 -0.0875 -0.2356 -0.2788 210 SER A C   
1621 O O   . SER A 206 ? 1.0240 1.0310 0.7761 -0.0867 -0.2208 -0.2825 210 SER A O   
1622 C CB  . SER A 206 ? 1.0175 1.0302 0.6705 -0.0807 -0.2248 -0.2980 210 SER A CB  
1623 O OG  . SER A 206 ? 1.1823 1.1899 0.8370 -0.0875 -0.2412 -0.3201 210 SER A OG  
1624 N N   . ARG A 207 ? 1.0672 1.0992 0.8226 -0.0937 -0.2552 -0.2775 211 ARG A N   
1625 C CA  . ARG A 207 ? 1.0034 1.0335 0.8045 -0.1020 -0.2585 -0.2815 211 ARG A CA  
1626 C C   . ARG A 207 ? 1.0644 1.1058 0.8756 -0.1109 -0.2835 -0.2924 211 ARG A C   
1627 O O   . ARG A 207 ? 0.9590 1.0154 0.7529 -0.1089 -0.2996 -0.2885 211 ARG A O   
1628 C CB  . ARG A 207 ? 0.9547 0.9930 0.7917 -0.1003 -0.2486 -0.2601 211 ARG A CB  
1629 C CG  . ARG A 207 ? 0.9834 1.0155 0.8632 -0.1096 -0.2452 -0.2634 211 ARG A CG  
1630 C CD  . ARG A 207 ? 1.1437 1.1811 1.0522 -0.1071 -0.2310 -0.2435 211 ARG A CD  
1631 N NE  . ARG A 207 ? 1.1429 1.1771 1.0910 -0.1182 -0.2293 -0.2453 211 ARG A NE  
1632 C CZ  . ARG A 207 ? 1.1840 1.2224 1.1604 -0.1192 -0.2175 -0.2307 211 ARG A CZ  
1633 N NH1 . ARG A 207 ? 1.0146 1.0603 0.9859 -0.1090 -0.2071 -0.2141 211 ARG A NH1 
1634 N NH2 . ARG A 207 ? 1.2681 1.3029 1.2768 -0.1312 -0.2159 -0.2328 211 ARG A NH2 
1635 N N   . LYS A 208 ? 1.1348 1.1681 0.9746 -0.1212 -0.2874 -0.3059 212 LYS A N   
1636 C CA  . LYS A 208 ? 1.1118 1.1543 0.9672 -0.1321 -0.3102 -0.3193 212 LYS A CA  
1637 C C   . LYS A 208 ? 1.0855 1.1339 0.9944 -0.1426 -0.3093 -0.3142 212 LYS A C   
1638 O O   . LYS A 208 ? 1.1197 1.1497 1.0452 -0.1468 -0.2947 -0.3154 212 LYS A O   
1639 C CB  . LYS A 208 ? 1.1667 1.1902 0.9990 -0.1371 -0.3161 -0.3451 212 LYS A CB  
1640 C CG  . LYS A 208 ? 1.2359 1.2657 1.0807 -0.1492 -0.3338 -0.3532 212 LYS A CG  
1641 C CD  . LYS A 208 ? 1.2297 1.2349 1.0544 -0.1540 -0.3314 -0.3725 212 LYS A CD  
1642 C CE  . LYS A 208 ? 1.2949 1.3068 1.1266 -0.1660 -0.3499 -0.3815 212 LYS A CE  
1643 N NZ  . LYS A 208 ? 1.4901 1.5212 1.2920 -0.1620 -0.3651 -0.3782 212 LYS A NZ  
1644 N N   . PHE A 209 ? 0.9109 0.9852 0.8463 -0.1468 -0.3248 -0.3084 213 PHE A N   
1645 C CA  . PHE A 209 ? 0.8908 0.9775 0.8785 -0.1573 -0.3234 -0.3028 213 PHE A CA  
1646 C C   . PHE A 209 ? 0.9126 1.0068 0.9221 -0.1724 -0.3430 -0.3199 213 PHE A C   
1647 O O   . PHE A 209 ? 0.8790 0.9845 0.8722 -0.1715 -0.3594 -0.3237 213 PHE A O   
1648 C CB  . PHE A 209 ? 0.7977 0.9121 0.8068 -0.1503 -0.3239 -0.2829 213 PHE A CB  
1649 C CG  . PHE A 209 ? 0.8101 0.9185 0.7949 -0.1353 -0.3074 -0.2653 213 PHE A CG  
1650 C CD1 . PHE A 209 ? 0.8076 0.9065 0.8070 -0.1338 -0.2845 -0.2533 213 PHE A CD1 
1651 C CD2 . PHE A 209 ? 0.7943 0.9059 0.7405 -0.1238 -0.3152 -0.2605 213 PHE A CD2 
1652 C CE1 . PHE A 209 ? 0.8979 0.9920 0.8765 -0.1209 -0.2701 -0.2380 213 PHE A CE1 
1653 C CE2 . PHE A 209 ? 0.7987 0.9044 0.7234 -0.1119 -0.2999 -0.2442 213 PHE A CE2 
1654 C CZ  . PHE A 209 ? 0.9118 1.0093 0.8541 -0.1103 -0.2775 -0.2336 213 PHE A CZ  
1655 N N   . THR A 210 ? 0.9839 1.0693 1.0270 -0.1864 -0.3354 -0.3230 214 THR A N   
1656 C CA  . THR A 210 ? 1.0532 1.1429 1.1204 -0.2027 -0.3446 -0.3310 214 THR A CA  
1657 C C   . THR A 210 ? 1.0370 1.1515 1.1576 -0.2130 -0.3418 -0.3212 214 THR A C   
1658 O O   . THR A 210 ? 1.1146 1.2236 1.2542 -0.2148 -0.3259 -0.3131 214 THR A O   
1659 C CB  . THR A 210 ? 1.1369 1.1905 1.1948 -0.2124 -0.3370 -0.3434 214 THR A CB  
1660 O OG1 . THR A 210 ? 1.2457 1.2775 1.2553 -0.2013 -0.3362 -0.3531 214 THR A OG1 
1661 C CG2 . THR A 210 ? 1.1406 1.1975 1.2187 -0.2297 -0.3483 -0.3526 214 THR A CG2 
1662 N N   . PRO A 211 ? 0.8904 1.0333 1.0362 -0.2200 -0.3560 -0.3218 215 PRO A N   
1663 C CA  . PRO A 211 ? 0.8589 1.0290 1.0572 -0.2298 -0.3515 -0.3134 215 PRO A CA  
1664 C C   . PRO A 211 ? 0.8876 1.0396 1.1091 -0.2495 -0.3390 -0.3162 215 PRO A C   
1665 O O   . PRO A 211 ? 1.0341 1.1650 1.2445 -0.2602 -0.3437 -0.3275 215 PRO A O   
1666 C CB  . PRO A 211 ? 0.9485 1.1508 1.1626 -0.2316 -0.3718 -0.3163 215 PRO A CB  
1667 C CG  . PRO A 211 ? 1.0397 1.2349 1.2061 -0.2176 -0.3863 -0.3209 215 PRO A CG  
1668 C CD  . PRO A 211 ? 1.0726 1.2275 1.1993 -0.2172 -0.3767 -0.3292 215 PRO A CD  
1669 N N   . GLU A 212 ? 0.9295 1.0889 1.1821 -0.2547 -0.3230 -0.3054 216 GLU A N   
1670 C CA  . GLU A 212 ? 0.9734 1.1167 1.2487 -0.2745 -0.3095 -0.3041 216 GLU A CA  
1671 C C   . GLU A 212 ? 1.0530 1.2340 1.3770 -0.2878 -0.3094 -0.2992 216 GLU A C   
1672 O O   . GLU A 212 ? 1.0807 1.2908 1.4296 -0.2820 -0.3025 -0.2893 216 GLU A O   
1673 C CB  . GLU A 212 ? 1.0209 1.1413 1.2908 -0.2716 -0.2894 -0.2949 216 GLU A CB  
1674 C CG  . GLU A 212 ? 1.1128 1.2062 1.3385 -0.2536 -0.2886 -0.2980 216 GLU A CG  
1675 C CD  . GLU A 212 ? 1.2541 1.3274 1.4708 -0.2473 -0.2649 -0.2819 216 GLU A CD  
1676 O OE1 . GLU A 212 ? 1.2919 1.3571 1.5316 -0.2619 -0.2523 -0.2752 216 GLU A OE1 
1677 O OE2 . GLU A 212 ? 1.3323 1.3979 1.5175 -0.2282 -0.2586 -0.2748 216 GLU A OE2 
1678 N N   . ILE A 213 ? 1.0923 1.2733 1.4304 -0.3056 -0.3165 -0.3066 217 ILE A N   
1679 C CA  . ILE A 213 ? 1.0820 1.2999 1.4663 -0.3196 -0.3174 -0.3039 217 ILE A CA  
1680 C C   . ILE A 213 ? 1.2086 1.4125 1.6141 -0.3406 -0.2983 -0.2968 217 ILE A C   
1681 O O   . ILE A 213 ? 1.2597 1.4270 1.6500 -0.3540 -0.2964 -0.3012 217 ILE A O   
1682 C CB  . ILE A 213 ? 1.0950 1.3247 1.4829 -0.3272 -0.3382 -0.3163 217 ILE A CB  
1683 C CG1 . ILE A 213 ? 1.1137 1.3669 1.4879 -0.3071 -0.3573 -0.3197 217 ILE A CG1 
1684 C CG2 . ILE A 213 ? 1.1235 1.3829 1.5594 -0.3471 -0.3362 -0.3145 217 ILE A CG2 
1685 C CD1 . ILE A 213 ? 1.2015 1.4236 1.5221 -0.2931 -0.3656 -0.3268 217 ILE A CD1 
1686 N N   . ALA A 214 ? 1.2104 1.4423 1.6494 -0.3434 -0.2840 -0.2855 218 ALA A N   
1687 C CA  . ALA A 214 ? 1.2815 1.5034 1.7397 -0.3638 -0.2645 -0.2764 218 ALA A CA  
1688 C C   . ALA A 214 ? 1.2875 1.5562 1.7892 -0.3663 -0.2536 -0.2677 218 ALA A C   
1689 O O   . ALA A 214 ? 1.1804 1.4828 1.6933 -0.3486 -0.2588 -0.2674 218 ALA A O   
1690 C CB  . ALA A 214 ? 1.1951 1.3750 1.6249 -0.3606 -0.2487 -0.2690 218 ALA A CB  
1691 N N   . LYS A 215 ? 1.5003 1.7697 2.0251 -0.3882 -0.2385 -0.2605 219 LYS A N   
1692 C CA  . LYS A 215 ? 1.4998 1.8126 2.0658 -0.3925 -0.2246 -0.2526 219 LYS A CA  
1693 C C   . LYS A 215 ? 1.4101 1.7185 1.9684 -0.3825 -0.2039 -0.2409 219 LYS A C   
1694 O O   . LYS A 215 ? 1.4861 1.7576 2.0243 -0.3914 -0.1896 -0.2329 219 LYS A O   
1695 C CB  . LYS A 215 ? 1.5741 1.8893 2.1654 -0.4210 -0.2160 -0.2489 219 LYS A CB  
1696 C CG  . LYS A 215 ? 1.6170 1.9346 2.2164 -0.4336 -0.2360 -0.2607 219 LYS A CG  
1697 C CD  . LYS A 215 ? 1.6263 1.9460 2.2519 -0.4629 -0.2268 -0.2558 219 LYS A CD  
1698 C CE  . LYS A 215 ? 1.6591 1.9814 2.2933 -0.4764 -0.2472 -0.2681 219 LYS A CE  
1699 N NZ  . LYS A 215 ? 1.7151 2.0412 2.3771 -0.5059 -0.2391 -0.2629 219 LYS A NZ  
1700 N N   . ARG A 216 ? 1.2438 1.5887 1.8176 -0.3637 -0.2032 -0.2399 220 ARG A N   
1701 C CA  . ARG A 216 ? 0.9830 1.3257 1.5483 -0.3517 -0.1856 -0.2305 220 ARG A CA  
1702 C C   . ARG A 216 ? 0.8737 1.2613 1.4782 -0.3526 -0.1697 -0.2246 220 ARG A C   
1703 O O   . ARG A 216 ? 0.9011 1.3278 1.5395 -0.3535 -0.1776 -0.2301 220 ARG A O   
1704 C CB  . ARG A 216 ? 0.8932 1.2327 1.4345 -0.3251 -0.1988 -0.2343 220 ARG A CB  
1705 C CG  . ARG A 216 ? 0.9563 1.2507 1.4549 -0.3217 -0.2116 -0.2404 220 ARG A CG  
1706 C CD  . ARG A 216 ? 1.1380 1.4308 1.6116 -0.2960 -0.2233 -0.2430 220 ARG A CD  
1707 N NE  . ARG A 216 ? 1.2532 1.5035 1.6842 -0.2920 -0.2332 -0.2494 220 ARG A NE  
1708 C CZ  . ARG A 216 ? 1.1143 1.3578 1.5301 -0.2909 -0.2534 -0.2601 220 ARG A CZ  
1709 N NH1 . ARG A 216 ? 0.8862 1.1621 1.3264 -0.2941 -0.2670 -0.2651 220 ARG A NH1 
1710 N NH2 . ARG A 216 ? 1.1073 1.3120 1.4831 -0.2863 -0.2597 -0.2664 220 ARG A NH2 
1711 N N   . PRO A 217 ? 0.7919 1.1748 1.3921 -0.3522 -0.1469 -0.2141 221 PRO A N   
1712 C CA  . PRO A 217 ? 0.7769 1.2019 1.4118 -0.3519 -0.1300 -0.2096 221 PRO A CA  
1713 C C   . PRO A 217 ? 0.8719 1.3369 1.5274 -0.3276 -0.1422 -0.2159 221 PRO A C   
1714 O O   . PRO A 217 ? 0.9128 1.3681 1.5479 -0.3081 -0.1580 -0.2193 221 PRO A O   
1715 C CB  . PRO A 217 ? 0.7771 1.1802 1.3911 -0.3530 -0.1058 -0.1976 221 PRO A CB  
1716 C CG  . PRO A 217 ? 0.8146 1.1632 1.3907 -0.3639 -0.1075 -0.1943 221 PRO A CG  
1717 C CD  . PRO A 217 ? 0.8617 1.1990 1.4251 -0.3543 -0.1345 -0.2061 221 PRO A CD  
1718 N N   . LYS A 218 ? 0.9702 1.4794 1.6659 -0.3285 -0.1349 -0.2171 222 LYS A N   
1719 C CA  . LYS A 218 ? 0.9484 1.4960 1.6676 -0.3052 -0.1463 -0.2226 222 LYS A CA  
1720 C C   . LYS A 218 ? 0.9261 1.4712 1.6322 -0.2853 -0.1360 -0.2168 222 LYS A C   
1721 O O   . LYS A 218 ? 0.8644 1.4065 1.5688 -0.2916 -0.1113 -0.2094 222 LYS A O   
1722 C CB  . LYS A 218 ? 0.9591 1.5539 1.7262 -0.3117 -0.1392 -0.2263 222 LYS A CB  
1723 C CG  . LYS A 218 ? 1.0496 1.6552 1.8364 -0.3286 -0.1531 -0.2336 222 LYS A CG  
1724 C CD  . LYS A 218 ? 1.0927 1.7211 1.8929 -0.3108 -0.1818 -0.2433 222 LYS A CD  
1725 C CE  . LYS A 218 ? 1.0420 1.6915 1.8709 -0.3275 -0.1933 -0.2513 222 LYS A CE  
1726 N NZ  . LYS A 218 ? 1.0626 1.7336 1.9027 -0.3104 -0.2222 -0.2604 222 LYS A NZ  
1727 N N   . VAL A 219 ? 0.9260 1.4710 1.6208 -0.2617 -0.1555 -0.2198 223 VAL A N   
1728 C CA  . VAL A 219 ? 0.8802 1.4275 1.5675 -0.2402 -0.1499 -0.2153 223 VAL A CA  
1729 C C   . VAL A 219 ? 0.9379 1.5169 1.6475 -0.2173 -0.1700 -0.2204 223 VAL A C   
1730 O O   . VAL A 219 ? 1.0990 1.6702 1.7943 -0.2075 -0.1956 -0.2241 223 VAL A O   
1731 C CB  . VAL A 219 ? 0.7368 1.2400 1.3760 -0.2326 -0.1535 -0.2098 223 VAL A CB  
1732 C CG1 . VAL A 219 ? 0.6716 1.1707 1.2938 -0.2073 -0.1471 -0.1999 223 VAL A CG1 
1733 C CG2 . VAL A 219 ? 0.7591 1.2244 1.3709 -0.2528 -0.1342 -0.2022 223 VAL A CG2 
1734 N N   . ARG A 220 ? 0.7592 1.3722 1.5015 -0.2086 -0.1586 -0.2208 224 ARG A N   
1735 C CA  . ARG A 220 ? 0.6115 1.2553 1.3795 -0.1867 -0.1764 -0.2256 224 ARG A CA  
1736 C C   . ARG A 220 ? 0.6365 1.2973 1.4231 -0.1933 -0.1971 -0.2335 224 ARG A C   
1737 O O   . ARG A 220 ? 0.5869 1.2500 1.3690 -0.1775 -0.2235 -0.2361 224 ARG A O   
1738 C CB  . ARG A 220 ? 0.6684 1.2943 1.4094 -0.1612 -0.1933 -0.2215 224 ARG A CB  
1739 C CG  . ARG A 220 ? 0.7448 1.3571 1.4710 -0.1530 -0.1742 -0.2143 224 ARG A CG  
1740 C CD  . ARG A 220 ? 0.5982 1.1877 1.2924 -0.1288 -0.1916 -0.2080 224 ARG A CD  
1741 N NE  . ARG A 220 ? 0.6310 1.2437 1.3464 -0.1078 -0.2147 -0.2115 224 ARG A NE  
1742 C CZ  . ARG A 220 ? 0.5605 1.1947 1.3011 -0.0904 -0.2104 -0.2115 224 ARG A CZ  
1743 N NH1 . ARG A 220 ? 0.4856 1.1338 1.2395 -0.0711 -0.2328 -0.2129 224 ARG A NH1 
1744 N NH2 . ARG A 220 ? 0.4016 1.0414 1.1521 -0.0923 -0.1839 -0.2101 224 ARG A NH2 
1745 N N   . ASP A 221 ? 0.6937 1.3653 1.4998 -0.2177 -0.1850 -0.2366 225 ASP A N   
1746 C CA  . ASP A 221 ? 0.8370 1.5274 1.6653 -0.2279 -0.2016 -0.2447 225 ASP A CA  
1747 C C   . ASP A 221 ? 0.8561 1.5176 1.6507 -0.2272 -0.2276 -0.2466 225 ASP A C   
1748 O O   . ASP A 221 ? 0.9195 1.5949 1.7223 -0.2185 -0.2522 -0.2525 225 ASP A O   
1749 C CB  . ASP A 221 ? 0.7937 1.5287 1.6643 -0.2116 -0.2116 -0.2512 225 ASP A CB  
1750 C CG  . ASP A 221 ? 0.8330 1.5942 1.7349 -0.2257 -0.2232 -0.2600 225 ASP A CG  
1751 O OD1 . ASP A 221 ? 0.8684 1.6237 1.7726 -0.2520 -0.2119 -0.2605 225 ASP A OD1 
1752 O OD2 . ASP A 221 ? 0.8116 1.5981 1.7353 -0.2106 -0.2443 -0.2661 225 ASP A OD2 
1753 N N   . GLN A 222 ? 0.7690 1.3890 1.5237 -0.2361 -0.2219 -0.2420 226 GLN A N   
1754 C CA  . GLN A 222 ? 0.7017 1.2908 1.4201 -0.2365 -0.2436 -0.2448 226 GLN A CA  
1755 C C   . GLN A 222 ? 0.6997 1.2513 1.3923 -0.2589 -0.2309 -0.2429 226 GLN A C   
1756 O O   . GLN A 222 ? 0.6212 1.1543 1.3006 -0.2629 -0.2098 -0.2357 226 GLN A O   
1757 C CB  . GLN A 222 ? 0.6462 1.2170 1.3307 -0.2116 -0.2577 -0.2409 226 GLN A CB  
1758 C CG  . GLN A 222 ? 0.6962 1.2932 1.3951 -0.1888 -0.2796 -0.2426 226 GLN A CG  
1759 C CD  . GLN A 222 ? 0.8384 1.4473 1.5450 -0.1935 -0.3035 -0.2509 226 GLN A CD  
1760 O OE1 . GLN A 222 ? 0.9143 1.5011 1.5992 -0.2085 -0.3100 -0.2552 226 GLN A OE1 
1761 N NE2 . GLN A 222 ? 0.8587 1.5019 1.5965 -0.1805 -0.3169 -0.2537 226 GLN A NE2 
1762 N N   . GLU A 223 ? 0.8573 1.3965 1.5421 -0.2732 -0.2445 -0.2494 227 GLU A N   
1763 C CA  . GLU A 223 ? 0.9771 1.4749 1.6334 -0.2924 -0.2373 -0.2487 227 GLU A CA  
1764 C C   . GLU A 223 ? 1.0019 1.4612 1.6100 -0.2820 -0.2530 -0.2512 227 GLU A C   
1765 O O   . GLU A 223 ? 0.9756 1.3958 1.5547 -0.2910 -0.2438 -0.2490 227 GLU A O   
1766 C CB  . GLU A 223 ? 1.1142 1.6176 1.7900 -0.3163 -0.2412 -0.2547 227 GLU A CB  
1767 C CG  . GLU A 223 ? 1.2055 1.7368 1.9220 -0.3334 -0.2203 -0.2509 227 GLU A CG  
1768 C CD  . GLU A 223 ? 1.2704 1.8055 2.0051 -0.3582 -0.2250 -0.2563 227 GLU A CD  
1769 O OE1 . GLU A 223 ? 1.2845 1.7960 1.9977 -0.3631 -0.2434 -0.2631 227 GLU A OE1 
1770 O OE2 . GLU A 223 ? 1.3012 1.8629 2.0713 -0.3731 -0.2102 -0.2541 227 GLU A OE2 
1771 N N   . GLY A 224 ? 0.6248 1.0931 1.2225 -0.2634 -0.2761 -0.2555 228 GLY A N   
1772 C CA  . GLY A 224 ? 0.6324 1.0664 1.1817 -0.2518 -0.2894 -0.2571 228 GLY A CA  
1773 C C   . GLY A 224 ? 0.6827 1.1064 1.2120 -0.2333 -0.2813 -0.2489 228 GLY A C   
1774 O O   . GLY A 224 ? 0.5783 1.0259 1.1322 -0.2249 -0.2704 -0.2426 228 GLY A O   
1775 N N   . ARG A 225 ? 0.6805 1.0678 1.1642 -0.2269 -0.2865 -0.2497 229 ARG A N   
1776 C CA  . ARG A 225 ? 0.6343 1.0035 1.0878 -0.2089 -0.2771 -0.2386 229 ARG A CA  
1777 C C   . ARG A 225 ? 0.6037 0.9627 1.0187 -0.1896 -0.2981 -0.2385 229 ARG A C   
1778 O O   . ARG A 225 ? 0.6280 0.9914 1.0383 -0.1921 -0.3214 -0.2504 229 ARG A O   
1779 C CB  . ARG A 225 ? 0.5908 0.9167 1.0117 -0.2163 -0.2556 -0.2317 229 ARG A CB  
1780 C CG  . ARG A 225 ? 0.5795 0.9095 1.0294 -0.2343 -0.2325 -0.2276 229 ARG A CG  
1781 C CD  . ARG A 225 ? 0.5503 0.9049 1.0216 -0.2244 -0.2167 -0.2166 229 ARG A CD  
1782 N NE  . ARG A 225 ? 0.5430 0.9004 1.0368 -0.2425 -0.1932 -0.2123 229 ARG A NE  
1783 C CZ  . ARG A 225 ? 0.5431 0.9354 1.0853 -0.2600 -0.1901 -0.2193 229 ARG A CZ  
1784 N NH1 . ARG A 225 ? 0.5508 0.9764 1.1223 -0.2593 -0.2091 -0.2295 229 ARG A NH1 
1785 N NH2 . ARG A 225 ? 0.5675 0.9592 1.1239 -0.2773 -0.1670 -0.2138 229 ARG A NH2 
1786 N N   . ILE A 226 ? 0.5899 0.9350 0.9762 -0.1710 -0.2895 -0.2247 230 ILE A N   
1787 C CA  . ILE A 226 ? 0.6043 0.9323 0.9450 -0.1537 -0.3040 -0.2211 230 ILE A CA  
1788 C C   . ILE A 226 ? 0.5936 0.8866 0.8938 -0.1458 -0.2829 -0.2085 230 ILE A C   
1789 O O   . ILE A 226 ? 0.5700 0.8667 0.8765 -0.1365 -0.2683 -0.1961 230 ILE A O   
1790 C CB  . ILE A 226 ? 0.6012 0.9567 0.9549 -0.1362 -0.3212 -0.2165 230 ILE A CB  
1791 C CG1 . ILE A 226 ? 0.6160 1.0063 1.0074 -0.1425 -0.3463 -0.2305 230 ILE A CG1 
1792 C CG2 . ILE A 226 ? 0.6166 0.9484 0.9167 -0.1193 -0.3312 -0.2085 230 ILE A CG2 
1793 C CD1 . ILE A 226 ? 0.6182 1.0341 1.0223 -0.1241 -0.3674 -0.2267 230 ILE A CD1 
1794 N N   . ASN A 227 ? 0.6853 0.9454 0.9461 -0.1495 -0.2814 -0.2127 231 ASN A N   
1795 C CA  . ASN A 227 ? 0.6038 0.8324 0.8263 -0.1412 -0.2633 -0.2023 231 ASN A CA  
1796 C C   . ASN A 227 ? 0.6090 0.8338 0.7972 -0.1225 -0.2719 -0.1940 231 ASN A C   
1797 O O   . ASN A 227 ? 0.6346 0.8597 0.8011 -0.1191 -0.2919 -0.2006 231 ASN A O   
1798 C CB  . ASN A 227 ? 0.6525 0.8485 0.8480 -0.1508 -0.2588 -0.2113 231 ASN A CB  
1799 C CG  . ASN A 227 ? 0.7065 0.8963 0.9291 -0.1685 -0.2451 -0.2144 231 ASN A CG  
1800 O OD1 . ASN A 227 ? 0.6715 0.8758 0.9242 -0.1722 -0.2318 -0.2061 231 ASN A OD1 
1801 N ND2 . ASN A 227 ? 0.7808 0.9477 0.9915 -0.1799 -0.2482 -0.2263 231 ASN A ND2 
1802 N N   . TYR A 228 ? 0.5875 0.8079 0.7694 -0.1112 -0.2572 -0.1793 232 TYR A N   
1803 C CA  . TYR A 228 ? 0.5920 0.8081 0.7440 -0.0945 -0.2635 -0.1689 232 TYR A CA  
1804 C C   . TYR A 228 ? 0.5989 0.7828 0.7033 -0.0906 -0.2514 -0.1651 232 TYR A C   
1805 O O   . TYR A 228 ? 0.5856 0.7529 0.6881 -0.0952 -0.2318 -0.1636 232 TYR A O   
1806 C CB  . TYR A 228 ? 0.5666 0.7981 0.7425 -0.0842 -0.2562 -0.1560 232 TYR A CB  
1807 C CG  . TYR A 228 ? 0.5584 0.8252 0.7857 -0.0869 -0.2660 -0.1610 232 TYR A CG  
1808 C CD1 . TYR A 228 ? 0.5736 0.8608 0.8101 -0.0791 -0.2910 -0.1633 232 TYR A CD1 
1809 C CD2 . TYR A 228 ? 0.5376 0.8183 0.8045 -0.0977 -0.2505 -0.1637 232 TYR A CD2 
1810 C CE1 . TYR A 228 ? 0.5660 0.8889 0.8538 -0.0807 -0.3004 -0.1694 232 TYR A CE1 
1811 C CE2 . TYR A 228 ? 0.5305 0.8473 0.8471 -0.1009 -0.2578 -0.1697 232 TYR A CE2 
1812 C CZ  . TYR A 228 ? 0.5769 0.9158 0.9057 -0.0919 -0.2829 -0.1732 232 TYR A CZ  
1813 O OH  . TYR A 228 ? 0.5365 0.9144 0.9188 -0.0942 -0.2907 -0.1806 232 TYR A OH  
1814 N N   . TYR A 229 ? 0.6219 0.7978 0.6880 -0.0823 -0.2634 -0.1635 233 TYR A N   
1815 C CA  . TYR A 229 ? 0.6326 0.7821 0.6529 -0.0788 -0.2529 -0.1617 233 TYR A CA  
1816 C C   . TYR A 229 ? 0.6424 0.7894 0.6322 -0.0660 -0.2585 -0.1486 233 TYR A C   
1817 O O   . TYR A 229 ? 0.6525 0.8146 0.6482 -0.0604 -0.2770 -0.1445 233 TYR A O   
1818 C CB  . TYR A 229 ? 0.6624 0.8001 0.6590 -0.0868 -0.2610 -0.1785 233 TYR A CB  
1819 C CG  . TYR A 229 ? 0.6584 0.7949 0.6838 -0.1007 -0.2575 -0.1914 233 TYR A CG  
1820 C CD1 . TYR A 229 ? 0.6486 0.7651 0.6742 -0.1050 -0.2376 -0.1922 233 TYR A CD1 
1821 C CD2 . TYR A 229 ? 0.6690 0.8235 0.7220 -0.1099 -0.2750 -0.2023 233 TYR A CD2 
1822 C CE1 . TYR A 229 ? 0.7069 0.8184 0.7567 -0.1185 -0.2351 -0.2023 233 TYR A CE1 
1823 C CE2 . TYR A 229 ? 0.6683 0.8200 0.7473 -0.1245 -0.2716 -0.2133 233 TYR A CE2 
1824 C CZ  . TYR A 229 ? 0.6932 0.8219 0.7694 -0.1289 -0.2515 -0.2127 233 TYR A CZ  
1825 O OH  . TYR A 229 ? 0.7639 0.8860 0.8638 -0.1443 -0.2488 -0.2221 233 TYR A OH  
1826 N N   . TRP A 230 ? 0.6413 0.7686 0.5988 -0.0616 -0.2427 -0.1420 234 TRP A N   
1827 C CA  . TRP A 230 ? 0.6515 0.7731 0.5780 -0.0515 -0.2446 -0.1280 234 TRP A CA  
1828 C C   . TRP A 230 ? 0.6663 0.7674 0.5488 -0.0517 -0.2319 -0.1297 234 TRP A C   
1829 O O   . TRP A 230 ? 0.6617 0.7530 0.5434 -0.0573 -0.2193 -0.1403 234 TRP A O   
1830 C CB  . TRP A 230 ? 0.6226 0.7479 0.5710 -0.0439 -0.2342 -0.1124 234 TRP A CB  
1831 C CG  . TRP A 230 ? 0.5948 0.7099 0.5533 -0.0463 -0.2097 -0.1110 234 TRP A CG  
1832 C CD1 . TRP A 230 ? 0.5712 0.6921 0.5655 -0.0526 -0.2002 -0.1159 234 TRP A CD1 
1833 C CD2 . TRP A 230 ? 0.6385 0.7360 0.5701 -0.0430 -0.1922 -0.1041 234 TRP A CD2 
1834 N NE1 . TRP A 230 ? 0.5535 0.6599 0.5430 -0.0526 -0.1793 -0.1120 234 TRP A NE1 
1835 C CE2 . TRP A 230 ? 0.5636 0.6567 0.5169 -0.0464 -0.1743 -0.1053 234 TRP A CE2 
1836 C CE3 . TRP A 230 ? 0.6084 0.6940 0.4997 -0.0384 -0.1900 -0.0968 234 TRP A CE3 
1837 C CZ2 . TRP A 230 ? 0.6101 0.6885 0.5483 -0.0440 -0.1559 -0.1004 234 TRP A CZ2 
1838 C CZ3 . TRP A 230 ? 0.5967 0.6694 0.4749 -0.0372 -0.1700 -0.0923 234 TRP A CZ3 
1839 C CH2 . TRP A 230 ? 0.5687 0.6383 0.4712 -0.0393 -0.1539 -0.0946 234 TRP A CH2 
1840 N N   . THR A 231 ? 0.6862 0.7811 0.5326 -0.0456 -0.2355 -0.1192 235 THR A N   
1841 C CA  . THR A 231 ? 0.7015 0.7805 0.5060 -0.0459 -0.2219 -0.1199 235 THR A CA  
1842 C C   . THR A 231 ? 0.7145 0.7880 0.4901 -0.0395 -0.2226 -0.1019 235 THR A C   
1843 O O   . THR A 231 ? 0.7295 0.8091 0.5075 -0.0349 -0.2398 -0.0916 235 THR A O   
1844 C CB  . THR A 231 ? 0.7541 0.8296 0.5288 -0.0516 -0.2302 -0.1369 235 THR A CB  
1845 O OG1 . THR A 231 ? 0.8063 0.8690 0.5449 -0.0516 -0.2136 -0.1395 235 THR A OG1 
1846 C CG2 . THR A 231 ? 0.8548 0.9369 0.6072 -0.0504 -0.2550 -0.1346 235 THR A CG2 
1847 N N   . LEU A 232 ? 0.7158 0.7775 0.4652 -0.0395 -0.2039 -0.0983 236 LEU A N   
1848 C CA  . LEU A 232 ? 0.7337 0.7874 0.4495 -0.0363 -0.2018 -0.0820 236 LEU A CA  
1849 C C   . LEU A 232 ? 0.7927 0.8411 0.4578 -0.0407 -0.2055 -0.0882 236 LEU A C   
1850 O O   . LEU A 232 ? 0.8608 0.9074 0.5142 -0.0449 -0.1949 -0.1043 236 LEU A O   
1851 C CB  . LEU A 232 ? 0.7137 0.7600 0.4339 -0.0349 -0.1780 -0.0738 236 LEU A CB  
1852 C CG  . LEU A 232 ? 0.6708 0.7200 0.4324 -0.0300 -0.1733 -0.0640 236 LEU A CG  
1853 C CD1 . LEU A 232 ? 0.6619 0.7026 0.4195 -0.0291 -0.1516 -0.0558 236 LEU A CD1 
1854 C CD2 . LEU A 232 ? 0.6787 0.7314 0.4479 -0.0242 -0.1921 -0.0506 236 LEU A CD2 
1855 N N   . LEU A 233 ? 0.9402 0.9854 0.5745 -0.0393 -0.2206 -0.0758 237 LEU A N   
1856 C CA  . LEU A 233 ? 0.9633 1.0036 0.5443 -0.0440 -0.2261 -0.0795 237 LEU A CA  
1857 C C   . LEU A 233 ? 0.9874 1.0164 0.5325 -0.0452 -0.2125 -0.0628 237 LEU A C   
1858 O O   . LEU A 233 ? 1.0019 1.0243 0.5452 -0.0415 -0.2199 -0.0426 237 LEU A O   
1859 C CB  . LEU A 233 ? 0.9498 0.9940 0.5191 -0.0427 -0.2563 -0.0779 237 LEU A CB  
1860 C CG  . LEU A 233 ? 1.1077 1.1488 0.6236 -0.0485 -0.2652 -0.0870 237 LEU A CG  
1861 C CD1 . LEU A 233 ? 1.1383 1.1841 0.6576 -0.0537 -0.2555 -0.1131 237 LEU A CD1 
1862 C CD2 . LEU A 233 ? 0.9743 1.0191 0.4808 -0.0462 -0.2977 -0.0829 237 LEU A CD2 
1863 N N   . GLU A 234 ? 1.0813 1.1081 0.5997 -0.0506 -0.1925 -0.0719 238 GLU A N   
1864 C CA  . GLU A 234 ? 1.1509 1.1695 0.6357 -0.0541 -0.1766 -0.0580 238 GLU A CA  
1865 C C   . GLU A 234 ? 1.2394 1.2496 0.6739 -0.0573 -0.1932 -0.0440 238 GLU A C   
1866 O O   . GLU A 234 ? 1.1180 1.1307 0.5351 -0.0579 -0.2136 -0.0512 238 GLU A O   
1867 C CB  . GLU A 234 ? 1.2994 1.3217 0.7678 -0.0592 -0.1525 -0.0743 238 GLU A CB  
1868 C CG  . GLU A 234 ? 1.3412 1.3695 0.8546 -0.0558 -0.1385 -0.0901 238 GLU A CG  
1869 C CD  . GLU A 234 ? 1.3738 1.4003 0.9106 -0.0538 -0.1189 -0.0793 238 GLU A CD  
1870 O OE1 . GLU A 234 ? 1.3707 1.3911 0.8999 -0.0540 -0.1197 -0.0585 238 GLU A OE1 
1871 O OE2 . GLU A 234 ? 1.4502 1.4804 1.0127 -0.0520 -0.1038 -0.0919 238 GLU A OE2 
1872 N N   . PRO A 235 ? 1.2937 1.2930 0.7036 -0.0601 -0.1860 -0.0234 239 PRO A N   
1873 C CA  . PRO A 235 ? 1.2537 1.2417 0.6091 -0.0647 -0.2005 -0.0085 239 PRO A CA  
1874 C C   . PRO A 235 ? 1.3458 1.3382 0.6525 -0.0730 -0.1957 -0.0238 239 PRO A C   
1875 O O   . PRO A 235 ? 1.3290 1.3264 0.6220 -0.0791 -0.1704 -0.0335 239 PRO A O   
1876 C CB  . PRO A 235 ? 1.2828 1.2577 0.6249 -0.0683 -0.1863 0.0140  239 PRO A CB  
1877 C CG  . PRO A 235 ? 1.3278 1.3064 0.7276 -0.0615 -0.1756 0.0145  239 PRO A CG  
1878 C CD  . PRO A 235 ? 1.1542 1.1490 0.5866 -0.0592 -0.1669 -0.0112 239 PRO A CD  
1879 N N   . GLY A 236 ? 1.4466 1.4383 0.7281 -0.0729 -0.2207 -0.0273 240 GLY A N   
1880 C CA  . GLY A 236 ? 1.3242 1.3190 0.5550 -0.0806 -0.2200 -0.0420 240 GLY A CA  
1881 C C   . GLY A 236 ? 1.3082 1.3160 0.5582 -0.0785 -0.2261 -0.0709 240 GLY A C   
1882 O O   . GLY A 236 ? 1.2998 1.3101 0.5105 -0.0829 -0.2306 -0.0846 240 GLY A O   
1883 N N   . ASP A 237 ? 1.3269 1.3422 0.6369 -0.0717 -0.2256 -0.0806 241 ASP A N   
1884 C CA  . ASP A 237 ? 1.2939 1.3190 0.6255 -0.0709 -0.2308 -0.1074 241 ASP A CA  
1885 C C   . ASP A 237 ? 1.1994 1.2273 0.5393 -0.0679 -0.2643 -0.1082 241 ASP A C   
1886 O O   . ASP A 237 ? 1.1791 1.2037 0.5283 -0.0633 -0.2822 -0.0886 241 ASP A O   
1887 C CB  . ASP A 237 ? 1.3762 1.4067 0.7663 -0.0666 -0.2143 -0.1168 241 ASP A CB  
1888 C CG  . ASP A 237 ? 1.4389 1.4756 0.8465 -0.0674 -0.2149 -0.1453 241 ASP A CG  
1889 O OD1 . ASP A 237 ? 1.4331 1.4705 0.8033 -0.0718 -0.2218 -0.1607 241 ASP A OD1 
1890 O OD2 . ASP A 237 ? 1.4373 1.4767 0.8943 -0.0642 -0.2087 -0.1523 241 ASP A OD2 
1891 N N   . THR A 238 ? 1.1347 1.1690 0.4726 -0.0704 -0.2733 -0.1323 242 THR A N   
1892 C CA  . THR A 238 ? 1.2022 1.2421 0.5490 -0.0690 -0.3051 -0.1377 242 THR A CA  
1893 C C   . THR A 238 ? 1.2016 1.2508 0.6063 -0.0677 -0.3060 -0.1566 242 THR A C   
1894 O O   . THR A 238 ? 1.2287 1.2778 0.6396 -0.0707 -0.2890 -0.1767 242 THR A O   
1895 C CB  . THR A 238 ? 1.1932 1.2346 0.4885 -0.0736 -0.3157 -0.1495 242 THR A CB  
1896 O OG1 . THR A 238 ? 1.2346 1.2701 0.4847 -0.0730 -0.3102 -0.1295 242 THR A OG1 
1897 C CG2 . THR A 238 ? 1.1951 1.2488 0.5110 -0.0718 -0.3455 -0.1549 242 THR A CG2 
1898 N N   . ILE A 239 ? 1.1851 1.2423 0.6325 -0.0635 -0.3257 -0.1502 243 ILE A N   
1899 C CA  . ILE A 239 ? 1.0996 1.1666 0.6031 -0.0640 -0.3282 -0.1658 243 ILE A CA  
1900 C C   . ILE A 239 ? 1.1456 1.2214 0.6477 -0.0671 -0.3578 -0.1800 243 ILE A C   
1901 O O   . ILE A 239 ? 1.0843 1.1631 0.5676 -0.0646 -0.3823 -0.1695 243 ILE A O   
1902 C CB  . ILE A 239 ? 1.0617 1.1348 0.6206 -0.0580 -0.3254 -0.1505 243 ILE A CB  
1903 C CG1 . ILE A 239 ? 0.9687 1.0521 0.5831 -0.0609 -0.3260 -0.1664 243 ILE A CG1 
1904 C CG2 . ILE A 239 ? 1.0716 1.1491 0.6309 -0.0517 -0.3494 -0.1312 243 ILE A CG2 
1905 C CD1 . ILE A 239 ? 0.8907 0.9803 0.5579 -0.0563 -0.3171 -0.1542 243 ILE A CD1 
1906 N N   . ILE A 240 ? 1.1360 1.2149 0.6576 -0.0728 -0.3566 -0.2041 244 ILE A N   
1907 C CA  . ILE A 240 ? 1.1638 1.2509 0.6851 -0.0784 -0.3802 -0.2205 244 ILE A CA  
1908 C C   . ILE A 240 ? 1.0863 1.1843 0.6710 -0.0809 -0.3872 -0.2310 244 ILE A C   
1909 O O   . ILE A 240 ? 1.0123 1.1052 0.6243 -0.0836 -0.3683 -0.2409 244 ILE A O   
1910 C CB  . ILE A 240 ? 1.1599 1.2389 0.6422 -0.0862 -0.3700 -0.2401 244 ILE A CB  
1911 C CG1 . ILE A 240 ? 1.2023 1.2744 0.6222 -0.0854 -0.3608 -0.2296 244 ILE A CG1 
1912 C CG2 . ILE A 240 ? 1.1842 1.2721 0.6739 -0.0943 -0.3893 -0.2535 244 ILE A CG2 
1913 C CD1 . ILE A 240 ? 1.3786 1.4436 0.7581 -0.0936 -0.3497 -0.2489 244 ILE A CD1 
1914 N N   . PHE A 241 ? 1.0503 1.1647 0.6622 -0.0813 -0.4096 -0.2258 245 PHE A N   
1915 C CA  . PHE A 241 ? 1.0211 1.1501 0.6919 -0.0865 -0.4180 -0.2360 245 PHE A CA  
1916 C C   . PHE A 241 ? 1.0589 1.1933 0.7237 -0.0963 -0.4317 -0.2517 245 PHE A C   
1917 O O   . PHE A 241 ? 1.1068 1.2475 0.7445 -0.0955 -0.4482 -0.2461 245 PHE A O   
1918 C CB  . PHE A 241 ? 0.9971 1.1444 0.7092 -0.0795 -0.4326 -0.2197 245 PHE A CB  
1919 C CG  . PHE A 241 ? 0.9542 1.0982 0.6867 -0.0718 -0.4160 -0.2042 245 PHE A CG  
1920 C CD1 . PHE A 241 ? 0.9608 1.0927 0.6573 -0.0636 -0.4074 -0.1844 245 PHE A CD1 
1921 C CD2 . PHE A 241 ? 0.9089 1.0621 0.6986 -0.0746 -0.4033 -0.2059 245 PHE A CD2 
1922 C CE1 . PHE A 241 ? 0.9710 1.0999 0.6897 -0.0578 -0.3871 -0.1680 245 PHE A CE1 
1923 C CE2 . PHE A 241 ? 0.8708 1.0214 0.6804 -0.0685 -0.3827 -0.1894 245 PHE A CE2 
1924 C CZ  . PHE A 241 ? 0.8767 1.0152 0.6515 -0.0598 -0.3751 -0.1710 245 PHE A CZ  
1925 N N   . GLU A 242 ? 1.0776 1.2086 0.7672 -0.1057 -0.4253 -0.2709 246 GLU A N   
1926 C CA  . GLU A 242 ? 1.2412 1.3771 0.9346 -0.1162 -0.4389 -0.2866 246 GLU A CA  
1927 C C   . GLU A 242 ? 1.2779 1.4253 1.0346 -0.1237 -0.4416 -0.2939 246 GLU A C   
1928 O O   . GLU A 242 ? 1.2674 1.4053 1.0484 -0.1265 -0.4249 -0.2994 246 GLU A O   
1929 C CB  . GLU A 242 ? 1.3455 1.4606 0.9985 -0.1225 -0.4277 -0.3048 246 GLU A CB  
1930 C CG  . GLU A 242 ? 1.4096 1.5158 0.9978 -0.1181 -0.4244 -0.2997 246 GLU A CG  
1931 C CD  . GLU A 242 ? 1.4668 1.5548 1.0184 -0.1247 -0.4137 -0.3198 246 GLU A CD  
1932 O OE1 . GLU A 242 ? 1.4422 1.5201 1.0190 -0.1304 -0.4063 -0.3365 246 GLU A OE1 
1933 O OE2 . GLU A 242 ? 1.5525 1.6354 1.0501 -0.1244 -0.4126 -0.3186 246 GLU A OE2 
1934 N N   . ALA A 243 ? 1.0635 1.2319 0.8470 -0.1277 -0.4619 -0.2938 247 ALA A N   
1935 C CA  . ALA A 243 ? 1.0362 1.2194 0.8816 -0.1360 -0.4638 -0.2992 247 ALA A CA  
1936 C C   . ALA A 243 ? 1.2974 1.4974 1.1565 -0.1445 -0.4853 -0.3079 247 ALA A C   
1937 O O   . ALA A 243 ? 1.2669 1.4742 1.0969 -0.1404 -0.5024 -0.3040 247 ALA A O   
1938 C CB  . ALA A 243 ? 0.9915 1.1929 0.8794 -0.1280 -0.4623 -0.2829 247 ALA A CB  
1939 N N   . ASN A 244 ? 1.3050 1.5106 1.2080 -0.1572 -0.4840 -0.3193 248 ASN A N   
1940 C CA  . ASN A 244 ? 1.2686 1.4940 1.1964 -0.1666 -0.5035 -0.3274 248 ASN A CA  
1941 C C   . ASN A 244 ? 1.2449 1.4953 1.2405 -0.1720 -0.5034 -0.3240 248 ASN A C   
1942 O O   . ASN A 244 ? 1.2719 1.5382 1.2969 -0.1831 -0.5153 -0.3329 248 ASN A O   
1943 C CB  . ASN A 244 ? 1.2948 1.5019 1.2048 -0.1803 -0.5037 -0.3478 248 ASN A CB  
1944 C CG  . ASN A 244 ? 1.2868 1.4765 1.2228 -0.1906 -0.4845 -0.3567 248 ASN A CG  
1945 O OD1 . ASN A 244 ? 1.3572 1.5423 1.3104 -0.1863 -0.4677 -0.3481 248 ASN A OD1 
1946 N ND2 . ASN A 244 ? 1.3090 1.4875 1.2471 -0.2045 -0.4874 -0.3738 248 ASN A ND2 
1947 N N   . GLY A 245 ? 1.1185 1.3734 1.1392 -0.1652 -0.4896 -0.3120 249 GLY A N   
1948 C CA  . GLY A 245 ? 1.0548 1.3345 1.1388 -0.1704 -0.4864 -0.3085 249 GLY A CA  
1949 C C   . GLY A 245 ? 0.9428 1.2149 1.0439 -0.1672 -0.4639 -0.3004 249 GLY A C   
1950 O O   . GLY A 245 ? 1.0480 1.2925 1.1171 -0.1649 -0.4493 -0.3013 249 GLY A O   
1951 N N   . ASN A 246 ? 0.9342 1.2328 1.0874 -0.1669 -0.4609 -0.2928 250 ASN A N   
1952 C CA  . ASN A 246 ? 0.9314 1.2283 1.1102 -0.1662 -0.4394 -0.2856 250 ASN A CA  
1953 C C   . ASN A 246 ? 0.9452 1.2281 1.0904 -0.1491 -0.4330 -0.2735 250 ASN A C   
1954 O O   . ASN A 246 ? 0.8948 1.1648 1.0429 -0.1487 -0.4140 -0.2700 250 ASN A O   
1955 C CB  . ASN A 246 ? 1.0130 1.2877 1.1978 -0.1825 -0.4218 -0.2955 250 ASN A CB  
1956 C CG  . ASN A 246 ? 1.0913 1.3783 1.3111 -0.2011 -0.4266 -0.3060 250 ASN A CG  
1957 O OD1 . ASN A 246 ? 1.1626 1.4421 1.3632 -0.2077 -0.4396 -0.3171 250 ASN A OD1 
1958 N ND2 . ASN A 246 ? 1.1087 1.4148 1.3794 -0.2105 -0.4156 -0.3025 250 ASN A ND2 
1959 N N   . LEU A 247 ? 1.0686 1.3534 1.1811 -0.1355 -0.4488 -0.2662 251 LEU A N   
1960 C CA  . LEU A 247 ? 0.8416 1.1134 0.9202 -0.1197 -0.4446 -0.2528 251 LEU A CA  
1961 C C   . LEU A 247 ? 0.8222 1.1187 0.9310 -0.1067 -0.4521 -0.2383 251 LEU A C   
1962 O O   . LEU A 247 ? 0.8436 1.1578 0.9585 -0.1016 -0.4717 -0.2353 251 LEU A O   
1963 C CB  . LEU A 247 ? 0.8834 1.1358 0.8980 -0.1139 -0.4551 -0.2527 251 LEU A CB  
1964 C CG  . LEU A 247 ? 0.8814 1.1235 0.8598 -0.0976 -0.4546 -0.2358 251 LEU A CG  
1965 C CD1 . LEU A 247 ? 0.8517 1.0740 0.8200 -0.0957 -0.4318 -0.2337 251 LEU A CD1 
1966 C CD2 . LEU A 247 ? 0.9292 1.1579 0.8471 -0.0935 -0.4670 -0.2338 251 LEU A CD2 
1967 N N   . ILE A 248 ? 0.9344 1.2313 1.0621 -0.1010 -0.4367 -0.2299 252 ILE A N   
1968 C CA  . ILE A 248 ? 0.7668 1.0804 0.9148 -0.0858 -0.4418 -0.2152 252 ILE A CA  
1969 C C   . ILE A 248 ? 0.7845 1.0744 0.8751 -0.0719 -0.4468 -0.2025 252 ILE A C   
1970 O O   . ILE A 248 ? 0.7688 1.0365 0.8364 -0.0687 -0.4228 -0.1919 252 ILE A O   
1971 C CB  . ILE A 248 ? 0.7215 1.0450 0.9132 -0.0866 -0.4192 -0.2105 252 ILE A CB  
1972 C CG1 . ILE A 248 ? 0.7077 1.0506 0.9494 -0.1045 -0.4131 -0.2250 252 ILE A CG1 
1973 C CG2 . ILE A 248 ? 0.7071 1.0506 0.9254 -0.0706 -0.4256 -0.1978 252 ILE A CG2 
1974 C CD1 . ILE A 248 ? 0.7248 1.0974 1.0003 -0.1075 -0.4294 -0.2296 252 ILE A CD1 
1975 N N   . ALA A 249 ? 0.8959 1.1864 0.9593 -0.0652 -0.4673 -0.1973 253 ALA A N   
1976 C CA  . ALA A 249 ? 0.8501 1.1155 0.8508 -0.0561 -0.4719 -0.1859 253 ALA A CA  
1977 C C   . ALA A 249 ? 0.8303 1.0898 0.8302 -0.0413 -0.4672 -0.1672 253 ALA A C   
1978 O O   . ALA A 249 ? 0.8047 1.0846 0.8531 -0.0346 -0.4682 -0.1622 253 ALA A O   
1979 C CB  . ALA A 249 ? 0.8977 1.1672 0.8728 -0.0533 -0.4954 -0.1836 253 ALA A CB  
1980 N N   . PRO A 250 ? 0.8434 1.0745 0.7892 -0.0371 -0.4554 -0.1549 254 PRO A N   
1981 C CA  . PRO A 250 ? 0.8324 1.0538 0.7723 -0.0241 -0.4478 -0.1336 254 PRO A CA  
1982 C C   . PRO A 250 ? 0.8632 1.0902 0.7955 -0.0114 -0.4790 -0.1227 254 PRO A C   
1983 O O   . PRO A 250 ? 0.9595 1.1835 0.8590 -0.0131 -0.4957 -0.1237 254 PRO A O   
1984 C CB  . PRO A 250 ? 0.8437 1.0339 0.7251 -0.0265 -0.4274 -0.1262 254 PRO A CB  
1985 C CG  . PRO A 250 ? 0.8470 1.0330 0.7176 -0.0401 -0.4176 -0.1454 254 PRO A CG  
1986 C CD  . PRO A 250 ? 1.0417 1.2487 0.9342 -0.0453 -0.4439 -0.1613 254 PRO A CD  
1987 N N   . ARG A 251 ? 0.8438 1.0775 0.8072 0.0008  -0.4791 -0.1099 255 ARG A N   
1988 C CA  . ARG A 251 ? 0.8729 1.1071 0.8308 0.0146  -0.5026 -0.0957 255 ARG A CA  
1989 C C   . ARG A 251 ? 0.8830 1.0878 0.8009 0.0241  -0.4985 -0.0743 255 ARG A C   
1990 O O   . ARG A 251 ? 0.9270 1.1120 0.7929 0.0262  -0.5080 -0.0619 255 ARG A O   
1991 C CB  . ARG A 251 ? 0.8499 1.1160 0.8778 0.0225  -0.5098 -0.0991 255 ARG A CB  
1992 C CG  . ARG A 251 ? 0.8811 1.1481 0.9097 0.0377  -0.5309 -0.0850 255 ARG A CG  
1993 C CD  . ARG A 251 ? 0.8876 1.1895 0.9686 0.0391  -0.5458 -0.0963 255 ARG A CD  
1994 N NE  . ARG A 251 ? 0.8883 1.1992 1.0011 0.0567  -0.5576 -0.0862 255 ARG A NE  
1995 C CZ  . ARG A 251 ? 0.9316 1.2277 1.0157 0.0683  -0.5771 -0.0714 255 ARG A CZ  
1996 N NH1 . ARG A 251 ? 1.0514 1.3245 1.0728 0.0635  -0.5862 -0.0642 255 ARG A NH1 
1997 N NH2 . ARG A 251 ? 0.9344 1.2383 1.0522 0.0847  -0.5868 -0.0643 255 ARG A NH2 
1998 N N   . TYR A 252 ? 0.8452 1.0458 0.7861 0.0274  -0.4736 -0.0674 256 TYR A N   
1999 C CA  . TYR A 252 ? 0.8516 1.0240 0.7594 0.0342  -0.4626 -0.0468 256 TYR A CA  
2000 C C   . TYR A 252 ? 0.8304 0.9854 0.7139 0.0236  -0.4278 -0.0469 256 TYR A C   
2001 O O   . TYR A 252 ? 0.7970 0.9637 0.7073 0.0148  -0.4086 -0.0608 256 TYR A O   
2002 C CB  . TYR A 252 ? 0.9144 1.0943 0.8680 0.0483  -0.4631 -0.0382 256 TYR A CB  
2003 C CG  . TYR A 252 ? 0.8730 1.0623 0.8423 0.0629  -0.4986 -0.0329 256 TYR A CG  
2004 C CD1 . TYR A 252 ? 0.8863 1.1096 0.9056 0.0643  -0.5119 -0.0475 256 TYR A CD1 
2005 C CD2 . TYR A 252 ? 0.9363 1.0995 0.8718 0.0736  -0.5106 -0.0120 256 TYR A CD2 
2006 C CE1 . TYR A 252 ? 0.8782 1.1101 0.9140 0.0764  -0.5325 -0.0417 256 TYR A CE1 
2007 C CE2 . TYR A 252 ? 0.9974 1.1670 0.9486 0.0858  -0.5315 -0.0057 256 TYR A CE2 
2008 C CZ  . TYR A 252 ? 0.9996 1.2040 1.0012 0.0877  -0.5429 -0.0210 256 TYR A CZ  
2009 O OH  . TYR A 252 ? 0.9767 1.1881 0.9949 0.1005  -0.5644 -0.0155 256 TYR A OH  
2010 N N   . ALA A 253 ? 0.8520 0.9786 0.6850 0.0245  -0.4203 -0.0307 257 ALA A N   
2011 C CA  . ALA A 253 ? 0.8352 0.9452 0.6439 0.0161  -0.3885 -0.0290 257 ALA A CA  
2012 C C   . ALA A 253 ? 0.8775 0.9681 0.6783 0.0234  -0.3777 -0.0093 257 ALA A C   
2013 O O   . ALA A 253 ? 1.0493 1.1360 0.8581 0.0348  -0.3958 0.0033  257 ALA A O   
2014 C CB  . ALA A 253 ? 0.8709 0.9665 0.6197 0.0060  -0.3866 -0.0322 257 ALA A CB  
2015 N N   . PHE A 254 ? 0.8118 0.8894 0.5973 0.0168  -0.3488 -0.0071 258 PHE A N   
2016 C CA  . PHE A 254 ? 0.8021 0.8624 0.5845 0.0217  -0.3349 0.0092  258 PHE A CA  
2017 C C   . PHE A 254 ? 0.9473 0.9859 0.6768 0.0128  -0.3168 0.0168  258 PHE A C   
2018 O O   . PHE A 254 ? 0.8057 0.8473 0.5273 0.0036  -0.2974 0.0049  258 PHE A O   
2019 C CB  . PHE A 254 ? 0.7501 0.8222 0.5836 0.0235  -0.3146 0.0029  258 PHE A CB  
2020 C CG  . PHE A 254 ? 0.7304 0.8272 0.6193 0.0310  -0.3281 -0.0057 258 PHE A CG  
2021 C CD1 . PHE A 254 ? 0.7147 0.8344 0.6309 0.0247  -0.3294 -0.0240 258 PHE A CD1 
2022 C CD2 . PHE A 254 ? 0.7290 0.8267 0.6442 0.0441  -0.3393 0.0036  258 PHE A CD2 
2023 C CE1 . PHE A 254 ? 0.6974 0.8429 0.6664 0.0301  -0.3403 -0.0325 258 PHE A CE1 
2024 C CE2 . PHE A 254 ? 0.7112 0.8353 0.6802 0.0512  -0.3505 -0.0061 258 PHE A CE2 
2025 C CZ  . PHE A 254 ? 0.6949 0.8443 0.6912 0.0436  -0.3505 -0.0241 258 PHE A CZ  
2026 N N   . ALA A 255 ? 0.9768 0.9934 0.6715 0.0156  -0.3230 0.0364  259 ALA A N   
2027 C CA  . ALA A 255 ? 0.9891 0.9858 0.6359 0.0066  -0.3044 0.0457  259 ALA A CA  
2028 C C   . ALA A 255 ? 0.9635 0.9524 0.6320 0.0083  -0.2823 0.0531  259 ALA A C   
2029 O O   . ALA A 255 ? 1.0091 0.9872 0.6901 0.0167  -0.2904 0.0670  259 ALA A O   
2030 C CB  . ALA A 255 ? 1.0488 1.0245 0.6427 0.0062  -0.3228 0.0639  259 ALA A CB  
2031 N N   . LEU A 256 ? 0.8457 0.8393 0.5183 0.0008  -0.2556 0.0433  260 LEU A N   
2032 C CA  . LEU A 256 ? 0.7702 0.7616 0.4713 0.0023  -0.2350 0.0458  260 LEU A CA  
2033 C C   . LEU A 256 ? 0.9110 0.8809 0.5781 -0.0026 -0.2219 0.0619  260 LEU A C   
2034 O O   . LEU A 256 ? 0.8867 0.8493 0.5097 -0.0119 -0.2152 0.0641  260 LEU A O   
2035 C CB  . LEU A 256 ? 0.7315 0.7378 0.4556 -0.0028 -0.2144 0.0276  260 LEU A CB  
2036 C CG  . LEU A 256 ? 0.7147 0.7416 0.4716 -0.0011 -0.2245 0.0108  260 LEU A CG  
2037 C CD1 . LEU A 256 ? 0.6822 0.7179 0.4567 -0.0071 -0.2038 -0.0049 260 LEU A CD1 
2038 C CD2 . LEU A 256 ? 0.6977 0.7340 0.4985 0.0091  -0.2378 0.0134  260 LEU A CD2 
2039 N N   . SER A 257 ? 1.0216 0.9822 0.7103 0.0029  -0.2177 0.0721  261 SER A N   
2040 C CA  . SER A 257 ? 0.9280 0.8692 0.5941 -0.0025 -0.2032 0.0864  261 SER A CA  
2041 C C   . SER A 257 ? 0.9518 0.8998 0.6528 -0.0024 -0.1808 0.0791  261 SER A C   
2042 O O   . SER A 257 ? 0.9120 0.8644 0.6529 0.0065  -0.1838 0.0773  261 SER A O   
2043 C CB  . SER A 257 ? 0.8835 0.8024 0.5397 0.0038  -0.2211 0.1066  261 SER A CB  
2044 O OG  . SER A 257 ? 0.9263 0.8368 0.5457 0.0034  -0.2430 0.1148  261 SER A OG  
2045 N N   . ARG A 258 ? 1.1219 1.0717 0.8079 -0.0120 -0.1587 0.0741  262 ARG A N   
2046 C CA  . ARG A 258 ? 0.9771 0.9341 0.6937 -0.0123 -0.1383 0.0662  262 ARG A CA  
2047 C C   . ARG A 258 ? 0.9942 0.9357 0.7197 -0.0102 -0.1337 0.0796  262 ARG A C   
2048 O O   . ARG A 258 ? 1.1005 1.0230 0.8012 -0.0116 -0.1416 0.0960  262 ARG A O   
2049 C CB  . ARG A 258 ? 1.0218 0.9853 0.7205 -0.0221 -0.1178 0.0568  262 ARG A CB  
2050 C CG  . ARG A 258 ? 1.0632 1.0409 0.7559 -0.0239 -0.1206 0.0406  262 ARG A CG  
2051 C CD  . ARG A 258 ? 1.0331 1.0250 0.7685 -0.0181 -0.1222 0.0267  262 ARG A CD  
2052 N NE  . ARG A 258 ? 1.1129 1.1158 0.8432 -0.0209 -0.1252 0.0109  262 ARG A NE  
2053 C CZ  . ARG A 258 ? 0.9102 0.9247 0.6718 -0.0189 -0.1257 -0.0026 262 ARG A CZ  
2054 N NH1 . ARG A 258 ? 0.8321 0.8504 0.6314 -0.0142 -0.1225 -0.0021 262 ARG A NH1 
2055 N NH2 . ARG A 258 ? 0.8589 0.8805 0.6132 -0.0223 -0.1292 -0.0169 262 ARG A NH2 
2056 N N   . GLY A 259 ? 1.0081 0.9564 0.7684 -0.0071 -0.1214 0.0726  263 GLY A N   
2057 C CA  . GLY A 259 ? 0.9814 0.9165 0.7539 -0.0050 -0.1160 0.0821  263 GLY A CA  
2058 C C   . GLY A 259 ? 1.0053 0.9511 0.8114 -0.0035 -0.1001 0.0711  263 GLY A C   
2059 O O   . GLY A 259 ? 1.0084 0.9702 0.8404 0.0007  -0.1005 0.0586  263 GLY A O   
2060 N N   . PHE A 260 ? 1.0435 0.9803 0.8485 -0.0078 -0.0865 0.0760  264 PHE A N   
2061 C CA  . PHE A 260 ? 1.0086 0.9537 0.8415 -0.0068 -0.0721 0.0668  264 PHE A CA  
2062 C C   . PHE A 260 ? 0.9390 0.8776 0.7992 0.0019  -0.0775 0.0696  264 PHE A C   
2063 O O   . PHE A 260 ? 0.9666 0.8897 0.8218 0.0059  -0.0895 0.0808  264 PHE A O   
2064 C CB  . PHE A 260 ? 1.0464 0.9882 0.8658 -0.0163 -0.0545 0.0684  264 PHE A CB  
2065 C CG  . PHE A 260 ? 1.2886 1.2351 1.0773 -0.0251 -0.0486 0.0669  264 PHE A CG  
2066 C CD1 . PHE A 260 ? 1.3527 1.3154 1.1453 -0.0265 -0.0402 0.0523  264 PHE A CD1 
2067 C CD2 . PHE A 260 ? 1.4087 1.3424 1.1634 -0.0322 -0.0514 0.0799  264 PHE A CD2 
2068 C CE1 . PHE A 260 ? 1.3455 1.3134 1.1106 -0.0337 -0.0343 0.0487  264 PHE A CE1 
2069 C CE2 . PHE A 260 ? 1.4169 1.3567 1.1419 -0.0408 -0.0446 0.0774  264 PHE A CE2 
2070 C CZ  . PHE A 260 ? 1.4033 1.3611 1.1343 -0.0410 -0.0358 0.0609  264 PHE A CZ  
2071 N N   . GLY A 261 A 0.7851 0.7349 0.6737 0.0050  -0.0686 0.0590  264 GLY A N   
2072 C CA  . GLY A 261 A 0.8007 0.7471 0.7159 0.0129  -0.0707 0.0585  264 GLY A CA  
2073 C C   . GLY A 261 A 0.7367 0.6959 0.6778 0.0222  -0.0815 0.0516  264 GLY A C   
2074 O O   . GLY A 261 A 0.9330 0.8942 0.8995 0.0289  -0.0807 0.0477  264 GLY A O   
2075 N N   . SER A 262 ? 0.7165 0.6856 0.6527 0.0223  -0.0912 0.0488  265 SER A N   
2076 C CA  . SER A 262 ? 0.5972 0.5820 0.5602 0.0298  -0.1016 0.0412  265 SER A CA  
2077 C C   . SER A 262 ? 0.5430 0.5466 0.5234 0.0258  -0.0908 0.0278  265 SER A C   
2078 O O   . SER A 262 ? 0.5649 0.5680 0.5338 0.0182  -0.0779 0.0247  265 SER A O   
2079 C CB  . SER A 262 ? 0.6700 0.6554 0.6194 0.0319  -0.1203 0.0454  265 SER A CB  
2080 O OG  . SER A 262 ? 0.7264 0.7291 0.7056 0.0394  -0.1316 0.0375  265 SER A OG  
2081 N N   . GLY A 263 ? 0.5196 0.5397 0.5289 0.0308  -0.0963 0.0199  266 GLY A N   
2082 C CA  . GLY A 263 ? 0.4330 0.4695 0.4592 0.0258  -0.0868 0.0084  266 GLY A CA  
2083 C C   . GLY A 263 ? 0.4778 0.5339 0.5377 0.0311  -0.0939 0.0008  266 GLY A C   
2084 O O   . GLY A 263 ? 0.5304 0.5882 0.6032 0.0403  -0.1061 0.0034  266 GLY A O   
2085 N N   . ILE A 264 ? 0.4859 0.5567 0.5608 0.0248  -0.0860 -0.0089 267 ILE A N   
2086 C CA  . ILE A 264 ? 0.4883 0.5818 0.5972 0.0265  -0.0895 -0.0178 267 ILE A CA  
2087 C C   . ILE A 264 ? 0.5368 0.6362 0.6639 0.0250  -0.0730 -0.0227 267 ILE A C   
2088 O O   . ILE A 264 ? 0.5664 0.6594 0.6826 0.0170  -0.0597 -0.0236 267 ILE A O   
2089 C CB  . ILE A 264 ? 0.4551 0.5609 0.5662 0.0183  -0.0940 -0.0249 267 ILE A CB  
2090 C CG1 . ILE A 264 ? 0.5634 0.6640 0.6542 0.0201  -0.1115 -0.0209 267 ILE A CG1 
2091 C CG2 . ILE A 264 ? 0.3839 0.5154 0.5328 0.0174  -0.0947 -0.0347 267 ILE A CG2 
2092 C CD1 . ILE A 264 ? 0.4976 0.6075 0.5867 0.0116  -0.1168 -0.0287 267 ILE A CD1 
2093 N N   . ILE A 265 ? 0.3696 0.4808 0.5237 0.0330  -0.0741 -0.0263 268 ILE A N   
2094 C CA  . ILE A 265 ? 0.3544 0.4730 0.5251 0.0317  -0.0583 -0.0320 268 ILE A CA  
2095 C C   . ILE A 265 ? 0.3690 0.5163 0.5765 0.0326  -0.0588 -0.0425 268 ILE A C   
2096 O O   . ILE A 265 ? 0.4386 0.5990 0.6639 0.0393  -0.0735 -0.0449 268 ILE A O   
2097 C CB  . ILE A 265 ? 0.3563 0.4605 0.5234 0.0404  -0.0548 -0.0280 268 ILE A CB  
2098 C CG1 . ILE A 265 ? 0.3692 0.4768 0.5537 0.0540  -0.0696 -0.0277 268 ILE A CG1 
2099 C CG2 . ILE A 265 ? 0.5948 0.6731 0.7278 0.0375  -0.0527 -0.0181 268 ILE A CG2 
2100 C CD1 . ILE A 265 ? 0.3735 0.4662 0.5578 0.0627  -0.0667 -0.0254 268 ILE A CD1 
2101 N N   . ASN A 266 ? 0.3827 0.5407 0.6017 0.0253  -0.0427 -0.0487 269 ASN A N   
2102 C CA  . ASN A 266 ? 0.3897 0.5772 0.6446 0.0244  -0.0384 -0.0595 269 ASN A CA  
2103 C C   . ASN A 266 ? 0.3499 0.5416 0.6192 0.0335  -0.0300 -0.0639 269 ASN A C   
2104 O O   . ASN A 266 ? 0.5265 0.7047 0.7797 0.0306  -0.0168 -0.0619 269 ASN A O   
2105 C CB  . ASN A 266 ? 0.4934 0.6899 0.7498 0.0083  -0.0252 -0.0634 269 ASN A CB  
2106 C CG  . ASN A 266 ? 0.6427 0.8331 0.8850 -0.0008 -0.0333 -0.0608 269 ASN A CG  
2107 O OD1 . ASN A 266 ? 0.6450 0.8417 0.8933 0.0031  -0.0493 -0.0614 269 ASN A OD1 
2108 N ND2 . ASN A 266 ? 0.7979 0.9748 1.0206 -0.0125 -0.0232 -0.0582 269 ASN A ND2 
2109 N N   . SER A 267 ? 0.3335 0.5437 0.6336 0.0451  -0.0385 -0.0708 270 SER A N   
2110 C CA  . SER A 267 ? 0.3341 0.5476 0.6494 0.0558  -0.0321 -0.0768 270 SER A CA  
2111 C C   . SER A 267 ? 0.3361 0.5825 0.6957 0.0647  -0.0374 -0.0893 270 SER A C   
2112 O O   . SER A 267 ? 0.3416 0.5997 0.7165 0.0687  -0.0539 -0.0899 270 SER A O   
2113 C CB  . SER A 267 ? 0.3444 0.5283 0.6396 0.0675  -0.0417 -0.0679 270 SER A CB  
2114 O OG  . SER A 267 ? 0.3912 0.5778 0.7044 0.0793  -0.0381 -0.0754 270 SER A OG  
2115 N N   . ASN A 268 ? 0.5194 0.7818 0.8999 0.0680  -0.0233 -0.1004 271 ASN A N   
2116 C CA  . ASN A 268 ? 0.4375 0.7322 0.8632 0.0791  -0.0264 -0.1146 271 ASN A CA  
2117 C C   . ASN A 268 ? 0.4321 0.7154 0.8666 0.0989  -0.0337 -0.1178 271 ASN A C   
2118 O O   . ASN A 268 ? 0.4970 0.8059 0.9708 0.1110  -0.0363 -0.1313 271 ASN A O   
2119 C CB  . ASN A 268 ? 0.5485 0.8745 0.9957 0.0683  -0.0039 -0.1276 271 ASN A CB  
2120 C CG  . ASN A 268 ? 0.6421 0.9884 1.0968 0.0510  -0.0007 -0.1280 271 ASN A CG  
2121 O OD1 . ASN A 268 ? 0.7240 1.0765 1.1883 0.0519  -0.0178 -0.1257 271 ASN A OD1 
2122 N ND2 . ASN A 268 ? 0.7486 1.1041 1.1979 0.0345  0.0207  -0.1308 271 ASN A ND2 
2123 N N   . ALA A 269 ? 0.3525 0.5986 0.7533 0.1023  -0.0371 -0.1066 272 ALA A N   
2124 C CA  . ALA A 269 ? 0.4139 0.6442 0.8209 0.1200  -0.0452 -0.1086 272 ALA A CA  
2125 C C   . ALA A 269 ? 0.3811 0.6116 0.8066 0.1352  -0.0709 -0.1063 272 ALA A C   
2126 O O   . ALA A 269 ? 0.4139 0.6396 0.8272 0.1309  -0.0847 -0.0961 272 ALA A O   
2127 C CB  . ALA A 269 ? 0.3706 0.5604 0.7364 0.1174  -0.0435 -0.0959 272 ALA A CB  
2128 N N   . PRO A 270 ? 0.4050 0.6407 0.8598 0.1537  -0.0785 -0.1161 273 PRO A N   
2129 C CA  . PRO A 270 ? 0.4114 0.6462 0.8851 0.1698  -0.1051 -0.1138 273 PRO A CA  
2130 C C   . PRO A 270 ? 0.4319 0.6210 0.8703 0.1754  -0.1224 -0.0956 273 PRO A C   
2131 O O   . PRO A 270 ? 0.4645 0.6241 0.8768 0.1735  -0.1147 -0.0897 273 PRO A O   
2132 C CB  . PRO A 270 ? 0.4182 0.6750 0.9377 0.1881  -0.1047 -0.1328 273 PRO A CB  
2133 C CG  . PRO A 270 ? 0.4017 0.6778 0.9270 0.1784  -0.0754 -0.1463 273 PRO A CG  
2134 C CD  . PRO A 270 ? 0.3928 0.6404 0.8691 0.1608  -0.0630 -0.1323 273 PRO A CD  
2135 N N   . MET A 271 ? 0.5569 0.7411 0.9946 0.1815  -0.1464 -0.0866 274 MET A N   
2136 C CA  . MET A 271 ? 0.6062 0.7483 1.0133 0.1880  -0.1655 -0.0691 274 MET A CA  
2137 C C   . MET A 271 ? 0.5784 0.7051 1.0054 0.2083  -0.1752 -0.0743 274 MET A C   
2138 O O   . MET A 271 ? 0.6951 0.8487 1.1668 0.2225  -0.1776 -0.0912 274 MET A O   
2139 C CB  . MET A 271 ? 0.7414 0.8839 1.1421 0.1895  -0.1895 -0.0590 274 MET A CB  
2140 C CG  . MET A 271 ? 0.9300 1.0298 1.2979 0.1959  -0.2112 -0.0397 274 MET A CG  
2141 S SD  . MET A 271 ? 0.9174 0.9792 1.2235 0.1763  -0.1991 -0.0204 274 MET A SD  
2142 C CE  . MET A 271 ? 0.9862 1.0022 1.2644 0.1867  -0.2264 0.0000  274 MET A CE  
2143 N N   . ASP A 272 ? 0.6187 0.7020 1.0132 0.2094  -0.1805 -0.0603 275 ASP A N   
2144 C CA  . ASP A 272 ? 0.7177 0.7784 1.1263 0.2279  -0.1916 -0.0633 275 ASP A CA  
2145 C C   . ASP A 272 ? 0.8465 0.8583 1.2159 0.2281  -0.2096 -0.0407 275 ASP A C   
2146 O O   . ASP A 272 ? 0.8071 0.8035 1.1363 0.2120  -0.2076 -0.0245 275 ASP A O   
2147 C CB  . ASP A 272 ? 0.8311 0.8917 1.2471 0.2274  -0.1690 -0.0768 275 ASP A CB  
2148 C CG  . ASP A 272 ? 0.9962 1.0447 1.4405 0.2493  -0.1794 -0.0875 275 ASP A CG  
2149 O OD1 . ASP A 272 ? 0.9040 0.9859 1.3938 0.2631  -0.1798 -0.1068 275 ASP A OD1 
2150 O OD2 . ASP A 272 ? 1.1157 1.1214 1.5377 0.2527  -0.1872 -0.0771 275 ASP A OD2 
2151 N N   . GLU A 273 ? 1.0835 1.0706 1.4650 0.2462  -0.2272 -0.0400 276 GLU A N   
2152 C CA  . GLU A 273 ? 1.1954 1.1327 1.5414 0.2472  -0.2458 -0.0181 276 GLU A CA  
2153 C C   . GLU A 273 ? 1.1782 1.0833 1.4946 0.2358  -0.2296 -0.0121 276 GLU A C   
2154 O O   . GLU A 273 ? 1.3834 1.2539 1.6976 0.2446  -0.2378 -0.0090 276 GLU A O   
2155 C CB  . GLU A 273 ? 1.2760 1.1977 1.6478 0.2716  -0.2733 -0.0193 276 GLU A CB  
2156 C CG  . GLU A 273 ? 1.3913 1.3293 1.8107 0.2895  -0.2673 -0.0436 276 GLU A CG  
2157 C CD  . GLU A 273 ? 1.5058 1.4331 1.9417 0.3062  -0.2878 -0.0451 276 GLU A CD  
2158 O OE1 . GLU A 273 ? 1.5840 1.4826 1.9943 0.3068  -0.3101 -0.0254 276 GLU A OE1 
2159 O OE2 . GLU A 273 ? 1.4248 1.3725 1.8965 0.3173  -0.2805 -0.0660 276 GLU A OE2 
2160 N N   . CYS A 274 ? 0.8567 0.7735 1.1512 0.2159  -0.2070 -0.0111 277 CYS A N   
2161 C CA  . CYS A 274 ? 0.7876 0.6798 1.0541 0.2027  -0.1906 -0.0058 277 CYS A CA  
2162 C C   . CYS A 274 ? 0.7105 0.5865 0.9315 0.1836  -0.1888 0.0144  277 CYS A C   
2163 O O   . CYS A 274 ? 0.8133 0.7068 1.0256 0.1775  -0.1921 0.0195  277 CYS A O   
2164 C CB  . CYS A 274 ? 0.7586 0.6790 1.0403 0.1966  -0.1641 -0.0244 277 CYS A CB  
2165 S SG  . CYS A 274 ? 0.8156 0.7880 1.1130 0.1883  -0.1510 -0.0349 277 CYS A SG  
2166 N N   . ASP A 275 ? 0.7849 0.6278 0.9777 0.1741  -0.1833 0.0250  278 ASP A N   
2167 C CA  . ASP A 275 ? 0.7960 0.6239 0.9465 0.1553  -0.1785 0.0427  278 ASP A CA  
2168 C C   . ASP A 275 ? 0.7696 0.5974 0.9089 0.1413  -0.1552 0.0382  278 ASP A C   
2169 O O   . ASP A 275 ? 0.7768 0.5920 0.9268 0.1453  -0.1500 0.0305  278 ASP A O   
2170 C CB  . ASP A 275 ? 0.8852 0.6701 1.0081 0.1551  -0.1972 0.0637  278 ASP A CB  
2171 C CG  . ASP A 275 ? 0.9858 0.7610 1.0657 0.1361  -0.1933 0.0815  278 ASP A CG  
2172 O OD1 . ASP A 275 ? 1.0969 0.8987 1.1714 0.1301  -0.1893 0.0801  278 ASP A OD1 
2173 O OD2 . ASP A 275 ? 1.1353 0.8770 1.1876 0.1266  -0.1937 0.0961  278 ASP A OD2 
2174 N N   . ALA A 276 ? 0.5967 0.4385 0.7151 0.1254  -0.1422 0.0423  279 ALA A N   
2175 C CA  . ALA A 276 ? 0.6277 0.4717 0.7356 0.1123  -0.1215 0.0383  279 ALA A CA  
2176 C C   . ALA A 276 ? 0.5778 0.4196 0.6522 0.0953  -0.1155 0.0512  279 ALA A C   
2177 O O   . ALA A 276 ? 0.6235 0.4685 0.6845 0.0935  -0.1248 0.0601  279 ALA A O   
2178 C CB  . ALA A 276 ? 0.5961 0.4739 0.7286 0.1140  -0.1060 0.0192  279 ALA A CB  
2179 N N   . LYS A 277 ? 0.6365 0.4737 0.6980 0.0832  -0.1001 0.0511  280 LYS A N   
2180 C CA  . LYS A 277 ? 0.7018 0.5415 0.7359 0.0674  -0.0912 0.0597  280 LYS A CA  
2181 C C   . LYS A 277 ? 0.5932 0.4635 0.6336 0.0623  -0.0765 0.0485  280 LYS A C   
2182 O O   . LYS A 277 ? 0.5715 0.4475 0.5925 0.0510  -0.0694 0.0532  280 LYS A O   
2183 C CB  . LYS A 277 ? 0.8713 0.6877 0.8883 0.0565  -0.0843 0.0669  280 LYS A CB  
2184 C CG  . LYS A 277 ? 1.1867 0.9679 1.1956 0.0595  -0.0984 0.0792  280 LYS A CG  
2185 C CD  . LYS A 277 ? 1.2775 1.0370 1.2727 0.0471  -0.0906 0.0850  280 LYS A CD  
2186 C CE  . LYS A 277 ? 1.2218 0.9427 1.2084 0.0490  -0.1053 0.0981  280 LYS A CE  
2187 N NZ  . LYS A 277 ? 1.3573 1.0570 1.3321 0.0351  -0.0976 0.1036  280 LYS A NZ  
2188 N N   . CYS A 278 ? 0.4984 0.3879 0.5649 0.0701  -0.0718 0.0338  281 CYS A N   
2189 C CA  . CYS A 278 ? 0.4607 0.3757 0.5331 0.0648  -0.0578 0.0237  281 CYS A CA  
2190 C C   . CYS A 278 ? 0.4394 0.3780 0.5391 0.0743  -0.0597 0.0119  281 CYS A C   
2191 O O   . CYS A 278 ? 0.4860 0.4248 0.6071 0.0850  -0.0624 0.0038  281 CYS A O   
2192 C CB  . CYS A 278 ? 0.5620 0.4741 0.6340 0.0596  -0.0439 0.0172  281 CYS A CB  
2193 S SG  . CYS A 278 ? 0.6149 0.5549 0.6950 0.0548  -0.0285 0.0048  281 CYS A SG  
2194 N N   . GLN A 279 ? 0.4253 0.3845 0.5256 0.0701  -0.0579 0.0100  282 GLN A N   
2195 C CA  . GLN A 279 ? 0.4148 0.3994 0.5416 0.0765  -0.0592 -0.0008 282 GLN A CA  
2196 C C   . GLN A 279 ? 0.3907 0.3956 0.5185 0.0670  -0.0447 -0.0080 282 GLN A C   
2197 O O   . GLN A 279 ? 0.3851 0.3881 0.4928 0.0572  -0.0410 -0.0027 282 GLN A O   
2198 C CB  . GLN A 279 ? 0.4277 0.4172 0.5572 0.0814  -0.0758 0.0043  282 GLN A CB  
2199 C CG  . GLN A 279 ? 0.4186 0.4366 0.5803 0.0883  -0.0787 -0.0075 282 GLN A CG  
2200 C CD  . GLN A 279 ? 0.4256 0.4463 0.6160 0.1024  -0.0823 -0.0164 282 GLN A CD  
2201 O OE1 . GLN A 279 ? 0.4472 0.4459 0.6351 0.1112  -0.0938 -0.0105 282 GLN A OE1 
2202 N NE2 . GLN A 279 ? 0.4808 0.5280 0.6984 0.1043  -0.0722 -0.0310 282 GLN A NE2 
2203 N N   . THR A 280 ? 0.3793 0.4026 0.5299 0.0700  -0.0366 -0.0203 283 THR A N   
2204 C CA  . THR A 280 ? 0.3609 0.4028 0.5141 0.0610  -0.0235 -0.0269 283 THR A CA  
2205 C C   . THR A 280 ? 0.3564 0.4255 0.5391 0.0651  -0.0247 -0.0368 283 THR A C   
2206 O O   . THR A 280 ? 0.3654 0.4402 0.5698 0.0767  -0.0331 -0.0414 283 THR A O   
2207 C CB  . THR A 280 ? 0.3536 0.3918 0.5021 0.0574  -0.0089 -0.0323 283 THR A CB  
2208 O OG1 . THR A 280 ? 0.3560 0.4049 0.5278 0.0658  -0.0053 -0.0436 283 THR A OG1 
2209 C CG2 . THR A 280 ? 0.3610 0.3735 0.4879 0.0558  -0.0096 -0.0244 283 THR A CG2 
2210 N N   . PRO A 281 ? 0.3441 0.4304 0.5294 0.0555  -0.0168 -0.0405 284 PRO A N   
2211 C CA  . PRO A 281 ? 0.3401 0.4552 0.5558 0.0571  -0.0160 -0.0507 284 PRO A CA  
2212 C C   . PRO A 281 ? 0.3404 0.4685 0.5796 0.0643  -0.0077 -0.0626 284 PRO A C   
2213 O O   . PRO A 281 ? 0.4744 0.6258 0.7444 0.0709  -0.0110 -0.0717 284 PRO A O   
2214 C CB  . PRO A 281 ? 0.3292 0.4538 0.5374 0.0425  -0.0059 -0.0513 284 PRO A CB  
2215 C CG  . PRO A 281 ? 0.3300 0.4322 0.5068 0.0366  -0.0091 -0.0405 284 PRO A CG  
2216 C CD  . PRO A 281 ? 0.3363 0.4163 0.4984 0.0429  -0.0104 -0.0352 284 PRO A CD  
2217 N N   . GLN A 282 ? 0.3709 0.4863 0.5974 0.0635  0.0030  -0.0639 285 GLN A N   
2218 C CA  . GLN A 282 ? 0.3683 0.4943 0.6147 0.0712  0.0109  -0.0765 285 GLN A CA  
2219 C C   . GLN A 282 ? 0.3578 0.4735 0.6178 0.0876  -0.0025 -0.0780 285 GLN A C   
2220 O O   . GLN A 282 ? 0.3629 0.4946 0.6509 0.0978  -0.0012 -0.0907 285 GLN A O   
2221 C CB  . GLN A 282 ? 0.4392 0.5536 0.6651 0.0647  0.0253  -0.0779 285 GLN A CB  
2222 C CG  . GLN A 282 ? 0.4194 0.5424 0.6322 0.0495  0.0384  -0.0769 285 GLN A CG  
2223 C CD  . GLN A 282 ? 0.4828 0.6369 0.7194 0.0459  0.0491  -0.0882 285 GLN A CD  
2224 O OE1 . GLN A 282 ? 0.5096 0.6779 0.7658 0.0532  0.0553  -0.1004 285 GLN A OE1 
2225 N NE2 . GLN A 282 ? 0.6179 0.7832 0.8539 0.0341  0.0519  -0.0849 285 GLN A NE2 
2226 N N   . GLY A 283 ? 0.3665 0.4555 0.6072 0.0900  -0.0151 -0.0656 286 GLY A N   
2227 C CA  . GLY A 283 ? 0.3845 0.4573 0.6336 0.1043  -0.0290 -0.0645 286 GLY A CA  
2228 C C   . GLY A 283 ? 0.3945 0.4333 0.6127 0.1012  -0.0359 -0.0498 286 GLY A C   
2229 O O   . GLY A 283 ? 0.3859 0.4165 0.5787 0.0888  -0.0293 -0.0420 286 GLY A O   
2230 N N   . ALA A 284 ? 0.4151 0.4341 0.6370 0.1126  -0.0496 -0.0463 287 ALA A N   
2231 C CA  . ALA A 284 ? 0.4295 0.4153 0.6236 0.1090  -0.0564 -0.0319 287 ALA A CA  
2232 C C   . ALA A 284 ? 0.4302 0.4002 0.6145 0.1059  -0.0456 -0.0356 287 ALA A C   
2233 O O   . ALA A 284 ? 0.4304 0.4072 0.6324 0.1127  -0.0391 -0.0493 287 ALA A O   
2234 C CB  . ALA A 284 ? 0.4563 0.4235 0.6558 0.1213  -0.0768 -0.0247 287 ALA A CB  
2235 N N   . ILE A 285 ? 0.4317 0.3819 0.5881 0.0952  -0.0436 -0.0241 288 ILE A N   
2236 C CA  . ILE A 285 ? 0.4331 0.3676 0.5783 0.0903  -0.0349 -0.0264 288 ILE A CA  
2237 C C   . ILE A 285 ? 0.4900 0.3917 0.6236 0.0918  -0.0462 -0.0156 288 ILE A C   
2238 O O   . ILE A 285 ? 0.6202 0.5100 0.7367 0.0867  -0.0541 -0.0011 288 ILE A O   
2239 C CB  . ILE A 285 ? 0.4143 0.3549 0.5395 0.0757  -0.0224 -0.0233 288 ILE A CB  
2240 C CG1 . ILE A 285 ? 0.3940 0.3629 0.5293 0.0734  -0.0111 -0.0336 288 ILE A CG1 
2241 C CG2 . ILE A 285 ? 0.4186 0.3417 0.5316 0.0704  -0.0164 -0.0243 288 ILE A CG2 
2242 C CD1 . ILE A 285 ? 0.3787 0.3515 0.4954 0.0607  -0.0003 -0.0313 288 ILE A CD1 
2243 N N   . ASN A 286 ? 0.4722 0.3585 0.6139 0.0981  -0.0467 -0.0229 289 ASN A N   
2244 C CA  . ASN A 286 ? 0.4997 0.3515 0.6317 0.0986  -0.0568 -0.0138 289 ASN A CA  
2245 C C   . ASN A 286 ? 0.4970 0.3387 0.6193 0.0900  -0.0462 -0.0187 289 ASN A C   
2246 O O   . ASN A 286 ? 0.5019 0.3411 0.6368 0.0966  -0.0430 -0.0325 289 ASN A O   
2247 C CB  . ASN A 286 ? 0.5234 0.3634 0.6772 0.1158  -0.0703 -0.0193 289 ASN A CB  
2248 C CG  . ASN A 286 ? 0.6500 0.4524 0.7974 0.1170  -0.0783 -0.0149 289 ASN A CG  
2249 O OD1 . ASN A 286 ? 0.6628 0.4403 0.7896 0.1089  -0.0859 0.0021  289 ASN A OD1 
2250 N ND2 . ASN A 286 ? 0.6432 0.4409 0.8080 0.1264  -0.0764 -0.0308 289 ASN A ND2 
2251 N N   . SER A 287 ? 0.4902 0.3277 0.5906 0.0754  -0.0409 -0.0085 290 SER A N   
2252 C CA  . SER A 287 ? 0.4842 0.3177 0.5764 0.0663  -0.0309 -0.0135 290 SER A CA  
2253 C C   . SER A 287 ? 0.4981 0.3189 0.5691 0.0519  -0.0305 0.0010  290 SER A C   
2254 O O   . SER A 287 ? 0.5708 0.3936 0.6308 0.0476  -0.0338 0.0132  290 SER A O   
2255 C CB  . SER A 287 ? 0.4700 0.3316 0.5650 0.0639  -0.0176 -0.0249 290 SER A CB  
2256 O OG  . SER A 287 ? 0.4527 0.3107 0.5381 0.0552  -0.0098 -0.0290 290 SER A OG  
2257 N N   . SER A 288 ? 0.6139 0.4229 0.6796 0.0442  -0.0263 -0.0016 291 SER A N   
2258 C CA  . SER A 288 ? 0.6650 0.4682 0.7142 0.0292  -0.0228 0.0088  291 SER A CA  
2259 C C   . SER A 288 ? 0.5575 0.3774 0.6044 0.0219  -0.0116 0.0004  291 SER A C   
2260 O O   . SER A 288 ? 0.5836 0.3998 0.6218 0.0101  -0.0084 0.0052  291 SER A O   
2261 C CB  . SER A 288 ? 0.8013 0.5726 0.8462 0.0242  -0.0299 0.0160  291 SER A CB  
2262 O OG  . SER A 288 ? 0.9778 0.7374 1.0341 0.0296  -0.0310 0.0032  291 SER A OG  
2263 N N   . LEU A 289 ? 0.4667 0.3054 0.5214 0.0283  -0.0060 -0.0119 292 LEU A N   
2264 C CA  . LEU A 289 ? 0.4378 0.2911 0.4886 0.0227  0.0028  -0.0195 292 LEU A CA  
2265 C C   . LEU A 289 ? 0.4187 0.2898 0.4608 0.0162  0.0076  -0.0127 292 LEU A C   
2266 O O   . LEU A 289 ? 0.4146 0.2923 0.4558 0.0187  0.0057  -0.0064 292 LEU A O   
2267 C CB  . LEU A 289 ? 0.4312 0.2963 0.4904 0.0311  0.0073  -0.0340 292 LEU A CB  
2268 C CG  . LEU A 289 ? 0.4504 0.3002 0.5188 0.0383  0.0040  -0.0448 292 LEU A CG  
2269 C CD1 . LEU A 289 ? 0.4793 0.3450 0.5542 0.0456  0.0108  -0.0600 292 LEU A CD1 
2270 C CD2 . LEU A 289 ? 0.4916 0.3244 0.5541 0.0301  0.0025  -0.0459 292 LEU A CD2 
2271 N N   . PRO A 290 ? 0.4087 0.2871 0.4448 0.0085  0.0129  -0.0147 293 PRO A N   
2272 C CA  . PRO A 290 ? 0.3933 0.2868 0.4223 0.0031  0.0167  -0.0093 293 PRO A CA  
2273 C C   . PRO A 290 ? 0.3770 0.2877 0.4066 0.0076  0.0206  -0.0140 293 PRO A C   
2274 O O   . PRO A 290 ? 0.4934 0.4144 0.5183 0.0050  0.0223  -0.0095 293 PRO A O   
2275 C CB  . PRO A 290 ? 0.3912 0.2858 0.4171 -0.0054 0.0195  -0.0113 293 PRO A CB  
2276 C CG  . PRO A 290 ? 0.3985 0.2856 0.4286 -0.0028 0.0186  -0.0214 293 PRO A CG  
2277 C CD  . PRO A 290 ? 0.4138 0.2861 0.4500 0.0042  0.0140  -0.0220 293 PRO A CD  
2278 N N   . PHE A 291 ? 0.3763 0.2904 0.4113 0.0136  0.0225  -0.0232 294 PHE A N   
2279 C CA  . PHE A 291 ? 0.3640 0.2938 0.3986 0.0155  0.0273  -0.0273 294 PHE A CA  
2280 C C   . PHE A 291 ? 0.3672 0.3017 0.4129 0.0237  0.0275  -0.0327 294 PHE A C   
2281 O O   . PHE A 291 ? 0.3795 0.3046 0.4333 0.0294  0.0244  -0.0369 294 PHE A O   
2282 C CB  . PHE A 291 ? 0.3612 0.2948 0.3887 0.0125  0.0318  -0.0342 294 PHE A CB  
2283 C CG  . PHE A 291 ? 0.3581 0.2899 0.3785 0.0056  0.0307  -0.0307 294 PHE A CG  
2284 C CD1 . PHE A 291 ? 0.3478 0.2876 0.3640 0.0024  0.0314  -0.0251 294 PHE A CD1 
2285 C CD2 . PHE A 291 ? 0.5192 0.4424 0.5387 0.0027  0.0288  -0.0344 294 PHE A CD2 
2286 C CE1 . PHE A 291 ? 0.3453 0.2863 0.3584 -0.0027 0.0305  -0.0236 294 PHE A CE1 
2287 C CE2 . PHE A 291 ? 0.3636 0.2885 0.3803 -0.0035 0.0275  -0.0323 294 PHE A CE2 
2288 C CZ  . PHE A 291 ? 0.4212 0.3559 0.4355 -0.0057 0.0286  -0.0271 294 PHE A CZ  
2289 N N   . GLN A 292 ? 0.3572 0.3067 0.4051 0.0243  0.0308  -0.0332 295 GLN A N   
2290 C CA  . GLN A 292 ? 0.3585 0.3183 0.4199 0.0310  0.0324  -0.0397 295 GLN A CA  
2291 C C   . GLN A 292 ? 0.3489 0.3250 0.4080 0.0271  0.0398  -0.0425 295 GLN A C   
2292 O O   . GLN A 292 ? 0.3408 0.3192 0.3906 0.0211  0.0402  -0.0364 295 GLN A O   
2293 C CB  . GLN A 292 ? 0.3965 0.3559 0.4684 0.0365  0.0245  -0.0343 295 GLN A CB  
2294 C CG  . GLN A 292 ? 0.3778 0.3408 0.4423 0.0315  0.0215  -0.0245 295 GLN A CG  
2295 C CD  . GLN A 292 ? 0.3938 0.3750 0.4661 0.0317  0.0235  -0.0267 295 GLN A CD  
2296 O OE1 . GLN A 292 ? 0.3929 0.3862 0.4767 0.0345  0.0284  -0.0351 295 GLN A OE1 
2297 N NE2 . GLN A 292 ? 0.4577 0.4418 0.5239 0.0279  0.0200  -0.0198 295 GLN A NE2 
2298 N N   . ASN A 293 ? 0.3521 0.3391 0.4196 0.0302  0.0461  -0.0520 296 ASN A N   
2299 C CA  . ASN A 293 ? 0.3469 0.3496 0.4131 0.0251  0.0540  -0.0543 296 ASN A CA  
2300 C C   . ASN A 293 ? 0.3452 0.3652 0.4320 0.0295  0.0551  -0.0586 296 ASN A C   
2301 O O   . ASN A 293 ? 0.5237 0.5593 0.6145 0.0260  0.0639  -0.0642 296 ASN A O   
2302 C CB  . ASN A 293 ? 0.3548 0.3585 0.4098 0.0218  0.0628  -0.0618 296 ASN A CB  
2303 C CG  . ASN A 293 ? 0.3661 0.3716 0.4312 0.0292  0.0660  -0.0739 296 ASN A CG  
2304 O OD1 . ASN A 293 ? 0.4297 0.4377 0.5136 0.0377  0.0620  -0.0774 296 ASN A OD1 
2305 N ND2 . ASN A 293 ? 0.3762 0.3800 0.4282 0.0265  0.0725  -0.0811 296 ASN A ND2 
2306 N N   . VAL A 294 ? 0.3456 0.3634 0.4455 0.0366  0.0459  -0.0559 297 VAL A N   
2307 C CA  . VAL A 294 ? 0.3452 0.3803 0.4679 0.0424  0.0445  -0.0608 297 VAL A CA  
2308 C C   . VAL A 294 ? 0.3666 0.4144 0.4903 0.0354  0.0444  -0.0557 297 VAL A C   
2309 O O   . VAL A 294 ? 0.4748 0.5422 0.6104 0.0325  0.0514  -0.0617 297 VAL A O   
2310 C CB  . VAL A 294 ? 0.3531 0.3788 0.4880 0.0531  0.0322  -0.0588 297 VAL A CB  
2311 C CG1 . VAL A 294 ? 0.3535 0.3984 0.5143 0.0604  0.0283  -0.0641 297 VAL A CG1 
2312 C CG2 . VAL A 294 ? 0.3655 0.3764 0.5003 0.0596  0.0320  -0.0648 297 VAL A CG2 
2313 N N   . HIS A 295 ? 0.3316 0.3690 0.4432 0.0320  0.0371  -0.0454 298 HIS A N   
2314 C CA  . HIS A 295 ? 0.3249 0.3718 0.4367 0.0258  0.0356  -0.0415 298 HIS A CA  
2315 C C   . HIS A 295 ? 0.3226 0.3549 0.4151 0.0214  0.0303  -0.0318 298 HIS A C   
2316 O O   . HIS A 295 ? 0.3272 0.3458 0.4127 0.0250  0.0241  -0.0269 298 HIS A O   
2317 C CB  . HIS A 295 ? 0.3261 0.3873 0.4599 0.0319  0.0279  -0.0438 298 HIS A CB  
2318 C CG  . HIS A 295 ? 0.3667 0.4445 0.5079 0.0247  0.0294  -0.0448 298 HIS A CG  
2319 N ND1 . HIS A 295 ? 0.3659 0.4392 0.4966 0.0195  0.0231  -0.0380 298 HIS A ND1 
2320 C CD2 . HIS A 295 ? 0.3403 0.4395 0.4990 0.0211  0.0368  -0.0525 298 HIS A CD2 
2321 C CE1 . HIS A 295 ? 0.3389 0.4282 0.4802 0.0131  0.0255  -0.0414 298 HIS A CE1 
2322 N NE2 . HIS A 295 ? 0.3483 0.4540 0.5070 0.0133  0.0341  -0.0496 298 HIS A NE2 
2323 N N   . PRO A 296 ? 0.4315 0.4660 0.5151 0.0133  0.0328  -0.0294 299 PRO A N   
2324 C CA  . PRO A 296 ? 0.3167 0.3394 0.3838 0.0100  0.0283  -0.0224 299 PRO A CA  
2325 C C   . PRO A 296 ? 0.3195 0.3433 0.3884 0.0125  0.0185  -0.0184 299 PRO A C   
2326 O O   . PRO A 296 ? 0.3974 0.4109 0.4523 0.0115  0.0149  -0.0130 299 PRO A O   
2327 C CB  . PRO A 296 ? 0.3137 0.3380 0.3732 0.0017  0.0335  -0.0228 299 PRO A CB  
2328 C CG  . PRO A 296 ? 0.3138 0.3533 0.3880 -0.0008 0.0384  -0.0281 299 PRO A CG  
2329 C CD  . PRO A 296 ? 0.3158 0.3613 0.4023 0.0060  0.0410  -0.0333 299 PRO A CD  
2330 N N   . VAL A 297 ? 0.3835 0.4205 0.4686 0.0152  0.0140  -0.0213 300 VAL A N   
2331 C CA  . VAL A 297 ? 0.3571 0.3949 0.4427 0.0180  0.0027  -0.0176 300 VAL A CA  
2332 C C   . VAL A 297 ? 0.3688 0.3972 0.4555 0.0265  -0.0044 -0.0137 300 VAL A C   
2333 O O   . VAL A 297 ? 0.4930 0.5261 0.5964 0.0333  -0.0047 -0.0182 300 VAL A O   
2334 C CB  . VAL A 297 ? 0.3319 0.3887 0.4365 0.0175  -0.0009 -0.0227 300 VAL A CB  
2335 C CG1 . VAL A 297 ? 0.3347 0.3920 0.4384 0.0212  -0.0148 -0.0190 300 VAL A CG1 
2336 C CG2 . VAL A 297 ? 0.3197 0.3818 0.4213 0.0075  0.0057  -0.0254 300 VAL A CG2 
2337 N N   . THR A 298 ? 0.3550 0.3696 0.4239 0.0257  -0.0098 -0.0058 301 THR A N   
2338 C CA  . THR A 298 ? 0.4169 0.4175 0.4822 0.0315  -0.0166 0.0002  301 THR A CA  
2339 C C   . THR A 298 ? 0.4489 0.4441 0.5018 0.0318  -0.0280 0.0082  301 THR A C   
2340 O O   . THR A 298 ? 0.5412 0.5400 0.5818 0.0259  -0.0281 0.0094  301 THR A O   
2341 C CB  . THR A 298 ? 0.4868 0.4722 0.5387 0.0281  -0.0097 0.0033  301 THR A CB  
2342 O OG1 . THR A 298 ? 0.6500 0.6333 0.6841 0.0202  -0.0058 0.0066  301 THR A OG1 
2343 C CG2 . THR A 298 ? 0.3854 0.3747 0.4470 0.0284  0.0000  -0.0047 301 THR A CG2 
2344 N N   . ILE A 299 ? 0.3895 0.3746 0.4445 0.0388  -0.0383 0.0135  302 ILE A N   
2345 C CA  . ILE A 299 ? 0.4099 0.3858 0.4491 0.0393  -0.0507 0.0231  302 ILE A CA  
2346 C C   . ILE A 299 ? 0.4295 0.3825 0.4592 0.0418  -0.0552 0.0323  302 ILE A C   
2347 O O   . ILE A 299 ? 0.4322 0.3799 0.4781 0.0494  -0.0571 0.0294  302 ILE A O   
2348 C CB  . ILE A 299 ? 0.5673 0.5558 0.6217 0.0464  -0.0640 0.0207  302 ILE A CB  
2349 C CG1 . ILE A 299 ? 0.5356 0.5440 0.5944 0.0407  -0.0605 0.0133  302 ILE A CG1 
2350 C CG2 . ILE A 299 ? 0.4438 0.4181 0.4810 0.0490  -0.0797 0.0321  302 ILE A CG2 
2351 C CD1 . ILE A 299 ? 0.6392 0.6638 0.7170 0.0464  -0.0729 0.0090  302 ILE A CD1 
2352 N N   . GLY A 300 ? 0.4744 0.4136 0.4778 0.0348  -0.0563 0.0427  303 GLY A N   
2353 C CA  . GLY A 300 ? 0.5695 0.4850 0.5611 0.0340  -0.0596 0.0528  303 GLY A CA  
2354 C C   . GLY A 300 ? 0.5854 0.4947 0.5698 0.0255  -0.0458 0.0525  303 GLY A C   
2355 O O   . GLY A 300 ? 0.5832 0.5028 0.5592 0.0177  -0.0357 0.0494  303 GLY A O   
2356 N N   . GLU A 301 ? 0.6963 0.5888 0.6853 0.0273  -0.0462 0.0547  304 GLU A N   
2357 C CA  . GLU A 301 ? 0.6841 0.5705 0.6691 0.0194  -0.0348 0.0538  304 GLU A CA  
2358 C C   . GLU A 301 ? 0.6498 0.5412 0.6571 0.0258  -0.0302 0.0419  304 GLU A C   
2359 O O   . GLU A 301 ? 0.7306 0.6091 0.7488 0.0331  -0.0362 0.0409  304 GLU A O   
2360 C CB  . GLU A 301 ? 0.8257 0.6867 0.7951 0.0138  -0.0390 0.0664  304 GLU A CB  
2361 C CG  . GLU A 301 ? 0.9139 0.7679 0.8589 0.0085  -0.0456 0.0794  304 GLU A CG  
2362 C CD  . GLU A 301 ? 0.9798 0.8079 0.9064 -0.0001 -0.0479 0.0933  304 GLU A CD  
2363 O OE1 . GLU A 301 ? 0.9759 0.8047 0.8930 -0.0122 -0.0363 0.0948  304 GLU A OE1 
2364 O OE2 . GLU A 301 ? 1.0733 0.8801 0.9957 0.0051  -0.0616 0.1027  304 GLU A OE2 
2365 N N   . CYS A 302 ? 0.4213 0.3304 0.4343 0.0233  -0.0198 0.0326  305 CYS A N   
2366 C CA  . CYS A 302 ? 0.4063 0.3238 0.4370 0.0285  -0.0145 0.0208  305 CYS A CA  
2367 C C   . CYS A 302 ? 0.3963 0.3133 0.4230 0.0216  -0.0043 0.0168  305 CYS A C   
2368 O O   . CYS A 302 ? 0.5112 0.4275 0.5249 0.0130  -0.0002 0.0214  305 CYS A O   
2369 C CB  . CYS A 302 ? 0.4423 0.3815 0.4834 0.0315  -0.0124 0.0134  305 CYS A CB  
2370 S SG  . CYS A 302 ? 0.5630 0.5092 0.6179 0.0414  -0.0249 0.0136  305 CYS A SG  
2371 N N   . PRO A 303 ? 0.4511 0.3697 0.4892 0.0253  -0.0002 0.0074  306 PRO A N   
2372 C CA  . PRO A 303 ? 0.3796 0.3012 0.4138 0.0193  0.0084  0.0023  306 PRO A CA  
2373 C C   . PRO A 303 ? 0.3708 0.3096 0.4023 0.0163  0.0143  -0.0008 306 PRO A C   
2374 O O   . PRO A 303 ? 0.5835 0.5331 0.6191 0.0190  0.0131  -0.0016 306 PRO A O   
2375 C CB  . PRO A 303 ? 0.4110 0.3296 0.4564 0.0252  0.0100  -0.0076 306 PRO A CB  
2376 C CG  . PRO A 303 ? 0.3981 0.3063 0.4530 0.0336  0.0015  -0.0063 306 PRO A CG  
2377 C CD  . PRO A 303 ? 0.3977 0.3128 0.4516 0.0352  -0.0041 0.0008  306 PRO A CD  
2378 N N   . LYS A 304 ? 0.3636 0.3040 0.3888 0.0105  0.0198  -0.0027 307 LYS A N   
2379 C CA  . LYS A 304 ? 0.3444 0.2969 0.3659 0.0077  0.0243  -0.0052 307 LYS A CA  
2380 C C   . LYS A 304 ? 0.3616 0.3213 0.3889 0.0106  0.0280  -0.0129 307 LYS A C   
2381 O O   . LYS A 304 ? 0.5658 0.5215 0.5949 0.0119  0.0301  -0.0183 307 LYS A O   
2382 C CB  . LYS A 304 ? 0.3718 0.3234 0.3863 0.0018  0.0273  -0.0050 307 LYS A CB  
2383 C CG  . LYS A 304 ? 0.4832 0.4438 0.4944 0.0003  0.0304  -0.0084 307 LYS A CG  
2384 C CD  . LYS A 304 ? 0.6139 0.5808 0.6215 -0.0008 0.0297  -0.0054 307 LYS A CD  
2385 C CE  . LYS A 304 ? 0.6172 0.5839 0.6192 -0.0048 0.0300  -0.0017 307 LYS A CE  
2386 N NZ  . LYS A 304 ? 0.6349 0.6081 0.6319 -0.0055 0.0296  -0.0010 307 LYS A NZ  
2387 N N   . TYR A 305 ? 0.3295 0.2996 0.3587 0.0107  0.0292  -0.0137 308 TYR A N   
2388 C CA  . TYR A 305 ? 0.3267 0.3051 0.3610 0.0116  0.0340  -0.0201 308 TYR A CA  
2389 C C   . TYR A 305 ? 0.3249 0.3018 0.3491 0.0071  0.0385  -0.0224 308 TYR A C   
2390 O O   . TYR A 305 ? 0.3879 0.3633 0.4042 0.0035  0.0377  -0.0192 308 TYR A O   
2391 C CB  . TYR A 305 ? 0.3223 0.3121 0.3626 0.0111  0.0336  -0.0199 308 TYR A CB  
2392 C CG  . TYR A 305 ? 0.3213 0.3208 0.3659 0.0093  0.0403  -0.0257 308 TYR A CG  
2393 C CD1 . TYR A 305 ? 0.4553 0.4619 0.5124 0.0137  0.0433  -0.0323 308 TYR A CD1 
2394 C CD2 . TYR A 305 ? 0.3193 0.3201 0.3551 0.0028  0.0440  -0.0249 308 TYR A CD2 
2395 C CE1 . TYR A 305 ? 0.3265 0.3440 0.3866 0.0106  0.0514  -0.0380 308 TYR A CE1 
2396 C CE2 . TYR A 305 ? 0.3224 0.3306 0.3593 -0.0008 0.0509  -0.0289 308 TYR A CE2 
2397 C CZ  . TYR A 305 ? 0.3257 0.3436 0.3745 0.0025  0.0554  -0.0355 308 TYR A CZ  
2398 O OH  . TYR A 305 ? 0.4732 0.5007 0.5224 -0.0025 0.0642  -0.0398 308 TYR A OH  
2399 N N   . VAL A 306 ? 0.3296 0.3070 0.3537 0.0079  0.0429  -0.0284 309 VAL A N   
2400 C CA  . VAL A 306 ? 0.3324 0.3078 0.3444 0.0038  0.0463  -0.0303 309 VAL A CA  
2401 C C   . VAL A 306 ? 0.3378 0.3212 0.3503 0.0029  0.0533  -0.0358 309 VAL A C   
2402 O O   . VAL A 306 ? 0.3669 0.3575 0.3916 0.0069  0.0558  -0.0406 309 VAL A O   
2403 C CB  . VAL A 306 ? 0.4216 0.3877 0.4276 0.0041  0.0443  -0.0326 309 VAL A CB  
2404 C CG1 . VAL A 306 ? 0.3337 0.2947 0.3404 0.0031  0.0392  -0.0274 309 VAL A CG1 
2405 C CG2 . VAL A 306 ? 0.3457 0.3093 0.3585 0.0085  0.0455  -0.0392 309 VAL A CG2 
2406 N N   . ARG A 307 ? 0.3429 0.3250 0.3420 -0.0025 0.0563  -0.0350 310 ARG A N   
2407 C CA  . ARG A 307 ? 0.3826 0.3722 0.3781 -0.0060 0.0646  -0.0392 310 ARG A CA  
2408 C C   . ARG A 307 ? 0.3638 0.3510 0.3512 -0.0048 0.0685  -0.0466 310 ARG A C   
2409 O O   . ARG A 307 ? 0.5641 0.5570 0.5436 -0.0088 0.0764  -0.0503 310 ARG A O   
2410 C CB  . ARG A 307 ? 0.3572 0.3434 0.3385 -0.0136 0.0657  -0.0335 310 ARG A CB  
2411 C CG  . ARG A 307 ? 0.3966 0.3842 0.3844 -0.0157 0.0623  -0.0279 310 ARG A CG  
2412 C CD  . ARG A 307 ? 0.3789 0.3625 0.3543 -0.0241 0.0648  -0.0235 310 ARG A CD  
2413 N NE  . ARG A 307 ? 0.4731 0.4492 0.4474 -0.0251 0.0579  -0.0180 310 ARG A NE  
2414 C CZ  . ARG A 307 ? 0.5876 0.5695 0.5730 -0.0268 0.0570  -0.0171 310 ARG A CZ  
2415 N NH1 . ARG A 307 ? 0.5821 0.5787 0.5822 -0.0276 0.0617  -0.0206 310 ARG A NH1 
2416 N NH2 . ARG A 307 ? 0.6822 0.6558 0.6649 -0.0271 0.0507  -0.0137 310 ARG A NH2 
2417 N N   . SER A 308 ? 0.3716 0.3506 0.3598 -0.0003 0.0634  -0.0490 311 SER A N   
2418 C CA  . SER A 308 ? 0.3775 0.3521 0.3560 0.0004  0.0655  -0.0568 311 SER A CA  
2419 C C   . SER A 308 ? 0.3837 0.3667 0.3737 0.0052  0.0721  -0.0673 311 SER A C   
2420 O O   . SER A 308 ? 0.3762 0.3651 0.3856 0.0105  0.0715  -0.0683 311 SER A O   
2421 C CB  . SER A 308 ? 0.3768 0.3397 0.3545 0.0025  0.0572  -0.0565 311 SER A CB  
2422 O OG  . SER A 308 ? 0.3979 0.3563 0.3693 -0.0007 0.0513  -0.0483 311 SER A OG  
2423 N N   . ALA A 309 ? 0.3996 0.3834 0.3772 0.0038  0.0781  -0.0757 312 ALA A N   
2424 C CA  . ALA A 309 ? 0.4091 0.4009 0.3966 0.0092  0.0851  -0.0887 312 ALA A CA  
2425 C C   . ALA A 309 ? 0.4643 0.4438 0.4538 0.0152  0.0796  -0.0968 312 ALA A C   
2426 O O   . ALA A 309 ? 0.5338 0.5170 0.5370 0.0223  0.0827  -0.1079 312 ALA A O   
2427 C CB  . ALA A 309 ? 0.4258 0.4272 0.3971 0.0033  0.0968  -0.0950 312 ALA A CB  
2428 N N   . LYS A 310 ? 0.4177 0.3831 0.3959 0.0126  0.0712  -0.0922 313 LYS A N   
2429 C CA  . LYS A 310 ? 0.4444 0.3972 0.4233 0.0160  0.0657  -0.0999 313 LYS A CA  
2430 C C   . LYS A 310 ? 0.4523 0.3938 0.4274 0.0122  0.0555  -0.0910 313 LYS A C   
2431 O O   . LYS A 310 ? 0.6170 0.5585 0.5771 0.0066  0.0534  -0.0852 313 LYS A O   
2432 C CB  . LYS A 310 ? 0.5104 0.4633 0.4716 0.0146  0.0709  -0.1123 313 LYS A CB  
2433 C CG  . LYS A 310 ? 0.8011 0.7401 0.7621 0.0176  0.0648  -0.1224 313 LYS A CG  
2434 C CD  . LYS A 310 ? 0.8317 0.7718 0.7722 0.0159  0.0701  -0.1357 313 LYS A CD  
2435 C CE  . LYS A 310 ? 0.8081 0.7333 0.7478 0.0181  0.0629  -0.1468 313 LYS A CE  
2436 N NZ  . LYS A 310 ? 0.9530 0.8791 0.8695 0.0162  0.0674  -0.1606 313 LYS A NZ  
2437 N N   . LEU A 311 ? 0.4525 0.3841 0.4417 0.0152  0.0491  -0.0898 314 LEU A N   
2438 C CA  . LEU A 311 ? 0.4133 0.3360 0.4022 0.0108  0.0407  -0.0828 314 LEU A CA  
2439 C C   . LEU A 311 ? 0.4261 0.3346 0.4225 0.0124  0.0357  -0.0898 314 LEU A C   
2440 O O   . LEU A 311 ? 0.4430 0.3435 0.4526 0.0140  0.0321  -0.0852 314 LEU A O   
2441 C CB  . LEU A 311 ? 0.3963 0.3221 0.3943 0.0097  0.0387  -0.0702 314 LEU A CB  
2442 C CG  . LEU A 311 ? 0.5747 0.5096 0.5641 0.0058  0.0397  -0.0623 314 LEU A CG  
2443 C CD1 . LEU A 311 ? 0.4265 0.3639 0.4252 0.0054  0.0379  -0.0521 314 LEU A CD1 
2444 C CD2 . LEU A 311 ? 0.5131 0.4454 0.4908 0.0012  0.0351  -0.0626 314 LEU A CD2 
2445 N N   . ARG A 312 ? 0.4420 0.3458 0.4283 0.0114  0.0350  -0.1007 315 ARG A N   
2446 C CA  . ARG A 312 ? 0.4580 0.3469 0.4503 0.0124  0.0300  -0.1096 315 ARG A CA  
2447 C C   . ARG A 312 ? 0.4686 0.3518 0.4562 0.0046  0.0221  -0.1080 315 ARG A C   
2448 O O   . ARG A 312 ? 0.4628 0.3521 0.4358 0.0011  0.0209  -0.1099 315 ARG A O   
2449 C CB  . ARG A 312 ? 0.4908 0.3786 0.4764 0.0174  0.0345  -0.1262 315 ARG A CB  
2450 C CG  . ARG A 312 ? 0.6431 0.5131 0.6349 0.0191  0.0288  -0.1374 315 ARG A CG  
2451 C CD  . ARG A 312 ? 0.5863 0.4565 0.5757 0.0266  0.0348  -0.1552 315 ARG A CD  
2452 N NE  . ARG A 312 ? 0.5809 0.4571 0.5864 0.0358  0.0405  -0.1558 315 ARG A NE  
2453 C CZ  . ARG A 312 ? 0.5901 0.4528 0.6148 0.0427  0.0357  -0.1569 315 ARG A CZ  
2454 N NH1 . ARG A 312 ? 0.5300 0.3710 0.5590 0.0400  0.0263  -0.1570 315 ARG A NH1 
2455 N NH2 . ARG A 312 ? 0.7104 0.5811 0.7506 0.0519  0.0397  -0.1578 315 ARG A NH2 
2456 N N   . MET A 313 ? 0.5047 0.3761 0.5049 0.0016  0.0165  -0.1044 316 MET A N   
2457 C CA  . MET A 313 ? 0.4713 0.3396 0.4728 -0.0070 0.0095  -0.1028 316 MET A CA  
2458 C C   . MET A 313 ? 0.6078 0.4599 0.6115 -0.0086 0.0043  -0.1150 316 MET A C   
2459 O O   . MET A 313 ? 0.6283 0.4655 0.6415 -0.0053 0.0037  -0.1175 316 MET A O   
2460 C CB  . MET A 313 ? 0.4521 0.3204 0.4658 -0.0119 0.0083  -0.0891 316 MET A CB  
2461 C CG  . MET A 313 ? 0.6576 0.5269 0.6763 -0.0217 0.0027  -0.0874 316 MET A CG  
2462 S SD  . MET A 313 ? 0.5210 0.3982 0.5499 -0.0276 0.0049  -0.0715 316 MET A SD  
2463 C CE  . MET A 313 ? 0.5652 0.4619 0.5850 -0.0223 0.0090  -0.0670 316 MET A CE  
2464 N N   . VAL A 314 ? 0.6189 0.4728 0.6140 -0.0133 -0.0008 -0.1229 317 VAL A N   
2465 C CA  . VAL A 314 ? 0.5719 0.4108 0.5676 -0.0154 -0.0066 -0.1366 317 VAL A CA  
2466 C C   . VAL A 314 ? 0.6127 0.4403 0.6250 -0.0242 -0.0126 -0.1314 317 VAL A C   
2467 O O   . VAL A 314 ? 0.5562 0.3937 0.5748 -0.0316 -0.0145 -0.1218 317 VAL A O   
2468 C CB  . VAL A 314 ? 0.5310 0.3763 0.5099 -0.0179 -0.0113 -0.1470 317 VAL A CB  
2469 C CG1 . VAL A 314 ? 0.5166 0.3760 0.4959 -0.0243 -0.0164 -0.1381 317 VAL A CG1 
2470 C CG2 . VAL A 314 ? 0.5572 0.3867 0.5370 -0.0211 -0.0185 -0.1623 317 VAL A CG2 
2471 N N   . THR A 315 ? 0.5437 0.3501 0.5635 -0.0236 -0.0152 -0.1381 318 THR A N   
2472 C CA  . THR A 315 ? 0.5553 0.3464 0.5888 -0.0337 -0.0214 -0.1350 318 THR A CA  
2473 C C   . THR A 315 ? 0.5802 0.3589 0.6128 -0.0387 -0.0293 -0.1510 318 THR A C   
2474 O O   . THR A 315 ? 0.5860 0.3619 0.6279 -0.0507 -0.0352 -0.1498 318 THR A O   
2475 C CB  . THR A 315 ? 0.5641 0.3350 0.6075 -0.0305 -0.0204 -0.1279 318 THR A CB  
2476 O OG1 . THR A 315 ? 0.6033 0.3617 0.6438 -0.0188 -0.0199 -0.1410 318 THR A OG1 
2477 C CG2 . THR A 315 ? 0.5415 0.3242 0.5861 -0.0276 -0.0143 -0.1113 318 THR A CG2 
2478 N N   . GLY A 316 ? 0.5962 0.3688 0.6181 -0.0303 -0.0291 -0.1669 319 GLY A N   
2479 C CA  . GLY A 316 ? 0.6229 0.3831 0.6412 -0.0339 -0.0367 -0.1846 319 GLY A CA  
2480 C C   . GLY A 316 ? 0.6214 0.3994 0.6251 -0.0374 -0.0406 -0.1918 319 GLY A C   
2481 O O   . GLY A 316 ? 0.6007 0.3981 0.6039 -0.0416 -0.0409 -0.1810 319 GLY A O   
2482 N N   . LEU A 317 ? 0.7596 0.5303 0.7504 -0.0350 -0.0444 -0.2107 320 LEU A N   
2483 C CA  . LEU A 317 ? 0.7669 0.5496 0.7411 -0.0387 -0.0512 -0.2198 320 LEU A CA  
2484 C C   . LEU A 317 ? 0.7636 0.5560 0.7118 -0.0291 -0.0442 -0.2272 320 LEU A C   
2485 O O   . LEU A 317 ? 0.7944 0.5846 0.7405 -0.0198 -0.0339 -0.2282 320 LEU A O   
2486 C CB  . LEU A 317 ? 0.9182 0.6846 0.8947 -0.0458 -0.0623 -0.2370 320 LEU A CB  
2487 C CG  . LEU A 317 ? 0.7851 0.5436 0.7850 -0.0595 -0.0714 -0.2330 320 LEU A CG  
2488 C CD1 . LEU A 317 ? 0.8123 0.5538 0.8327 -0.0611 -0.0667 -0.2215 320 LEU A CD1 
2489 C CD2 . LEU A 317 ? 0.7776 0.5217 0.7745 -0.0653 -0.0826 -0.2534 320 LEU A CD2 
2490 N N   . ARG A 318 ? 0.8020 0.6056 0.7302 -0.0319 -0.0502 -0.2322 321 ARG A N   
2491 C CA  . ARG A 318 ? 0.7794 0.5889 0.6780 -0.0255 -0.0447 -0.2417 321 ARG A CA  
2492 C C   . ARG A 318 ? 0.7798 0.5729 0.6716 -0.0218 -0.0440 -0.2641 321 ARG A C   
2493 O O   . ARG A 318 ? 0.7870 0.5689 0.6795 -0.0275 -0.0552 -0.2771 321 ARG A O   
2494 C CB  . ARG A 318 ? 0.7525 0.5745 0.6291 -0.0300 -0.0539 -0.2408 321 ARG A CB  
2495 C CG  . ARG A 318 ? 1.0467 0.8748 0.8880 -0.0252 -0.0474 -0.2472 321 ARG A CG  
2496 C CD  . ARG A 318 ? 1.0372 0.8760 0.8556 -0.0292 -0.0577 -0.2414 321 ARG A CD  
2497 N NE  . ARG A 318 ? 0.8880 0.7371 0.7252 -0.0319 -0.0628 -0.2227 321 ARG A NE  
2498 C CZ  . ARG A 318 ? 0.9180 0.7780 0.7406 -0.0312 -0.0649 -0.2099 321 ARG A CZ  
2499 N NH1 . ARG A 318 ? 0.9514 0.8122 0.7385 -0.0294 -0.0619 -0.2118 321 ARG A NH1 
2500 N NH2 . ARG A 318 ? 0.8928 0.7620 0.7358 -0.0327 -0.0695 -0.1953 321 ARG A NH2 
2501 N N   . ASN A 319 ? 0.7331 0.5255 0.6203 -0.0122 -0.0312 -0.2699 322 ASN A N   
2502 C CA  . ASN A 319 ? 0.7471 0.5240 0.6327 -0.0063 -0.0289 -0.2922 322 ASN A CA  
2503 C C   . ASN A 319 ? 0.7791 0.5596 0.6314 -0.0076 -0.0310 -0.3101 322 ASN A C   
2504 O O   . ASN A 319 ? 0.7820 0.5767 0.6101 -0.0040 -0.0210 -0.3115 322 ASN A O   
2505 C CB  . ASN A 319 ? 0.7868 0.5659 0.6815 0.0053  -0.0144 -0.2929 322 ASN A CB  
2506 C CG  . ASN A 319 ? 0.7679 0.5276 0.6726 0.0130  -0.0137 -0.3142 322 ASN A CG  
2507 O OD1 . ASN A 319 ? 0.7876 0.5271 0.6996 0.0087  -0.0250 -0.3240 322 ASN A OD1 
2508 N ND2 . ASN A 319 ? 0.8559 0.6217 0.7627 0.0245  -0.0008 -0.3222 322 ASN A ND2 
2509 N N   . ILE A 320 ? 0.8024 0.5698 0.6523 -0.0137 -0.0443 -0.3238 323 ILE A N   
2510 C CA  . ILE A 320 ? 0.9872 0.7560 0.8040 -0.0158 -0.0490 -0.3421 323 ILE A CA  
2511 C C   . ILE A 320 ? 1.0809 0.8290 0.9005 -0.0125 -0.0514 -0.3684 323 ILE A C   
2512 O O   . ILE A 320 ? 1.1187 0.8531 0.9434 -0.0199 -0.0660 -0.3780 323 ILE A O   
2513 C CB  . ILE A 320 ? 0.8666 0.6409 0.6749 -0.0265 -0.0658 -0.3359 323 ILE A CB  
2514 C CG1 . ILE A 320 ? 0.8327 0.6235 0.6498 -0.0290 -0.0653 -0.3093 323 ILE A CG1 
2515 C CG2 . ILE A 320 ? 1.0225 0.8018 0.7893 -0.0280 -0.0700 -0.3501 323 ILE A CG2 
2516 C CD1 . ILE A 320 ? 0.7971 0.5950 0.6138 -0.0381 -0.0824 -0.3028 323 ILE A CD1 
2517 N N   . PRO A 321 ? 1.2198 0.9652 1.0381 -0.0017 -0.0377 -0.3817 324 PRO A N   
2518 C CA  . PRO A 321 ? 1.2329 0.9566 1.0571 0.0031  -0.0402 -0.4079 324 PRO A CA  
2519 C C   . PRO A 321 ? 1.2531 0.9811 1.0409 0.0048  -0.0360 -0.4269 324 PRO A C   
2520 O O   . PRO A 321 ? 1.3646 1.1124 1.1230 0.0053  -0.0268 -0.4263 324 PRO A O   
2521 C CB  . PRO A 321 ? 1.2107 0.9302 1.0610 0.0155  -0.0278 -0.4065 324 PRO A CB  
2522 C CG  . PRO A 321 ? 1.2093 0.9555 1.0530 0.0183  -0.0139 -0.3869 324 PRO A CG  
2523 C CD  . PRO A 321 ? 1.2518 1.0132 1.0704 0.0073  -0.0198 -0.3731 324 PRO A CD  
2524 N N   . SER A 322 ? 1.4517 1.1603 1.2401 0.0046  -0.0421 -0.4413 325 SER A N   
2525 C CA  . SER A 322 ? 1.5324 1.2411 1.2876 0.0063  -0.0380 -0.4594 325 SER A CA  
2526 C C   . SER A 322 ? 1.5759 1.3015 1.2896 -0.0015 -0.0408 -0.4581 325 SER A C   
2527 O O   . SER A 322 ? 1.5803 1.2995 1.2785 -0.0108 -0.0558 -0.4626 325 SER A O   
2528 C CB  . SER A 322 ? 1.4680 1.1831 1.2234 0.0201  -0.0184 -0.4683 325 SER A CB  
2529 O OG  . SER A 322 ? 1.4571 1.1964 1.2068 0.0235  -0.0045 -0.4573 325 SER A OG  
2530 N N   . GLY B 1   ? 0.7091 0.5984 0.5652 -0.0533 -0.1517 -0.2255 1   GLY B N   
2531 C CA  . GLY B 1   ? 0.6784 0.5762 0.5776 -0.0575 -0.1473 -0.2190 1   GLY B CA  
2532 C C   . GLY B 1   ? 0.6685 0.5859 0.5917 -0.0599 -0.1626 -0.2152 1   GLY B C   
2533 O O   . GLY B 1   ? 0.6904 0.6125 0.6030 -0.0605 -0.1808 -0.2229 1   GLY B O   
2534 N N   . LEU B 2   ? 0.6411 0.5710 0.5969 -0.0610 -0.1556 -0.2042 2   LEU B N   
2535 C CA  . LEU B 2   ? 0.7309 0.6830 0.7135 -0.0622 -0.1683 -0.2012 2   LEU B CA  
2536 C C   . LEU B 2   ? 0.6395 0.5991 0.6450 -0.0723 -0.1824 -0.2156 2   LEU B C   
2537 O O   . LEU B 2   ? 0.6451 0.6218 0.6617 -0.0720 -0.1999 -0.2192 2   LEU B O   
2538 C CB  . LEU B 2   ? 0.7149 0.6793 0.7272 -0.0621 -0.1552 -0.1882 2   LEU B CB  
2539 C CG  . LEU B 2   ? 0.5751 0.5414 0.5743 -0.0517 -0.1478 -0.1735 2   LEU B CG  
2540 C CD1 . LEU B 2   ? 0.5448 0.5278 0.5779 -0.0528 -0.1390 -0.1643 2   LEU B CD1 
2541 C CD2 . LEU B 2   ? 0.5911 0.5612 0.5694 -0.0439 -0.1643 -0.1725 2   LEU B CD2 
2542 N N   . PHE B 3   ? 0.6465 0.5933 0.6607 -0.0811 -0.1761 -0.2240 3   PHE B N   
2543 C CA  . PHE B 3   ? 0.7238 0.6761 0.7638 -0.0933 -0.1874 -0.2371 3   PHE B CA  
2544 C C   . PHE B 3   ? 0.6955 0.6308 0.7105 -0.0957 -0.1985 -0.2546 3   PHE B C   
2545 O O   . PHE B 3   ? 0.7100 0.6435 0.7436 -0.1068 -0.2064 -0.2672 3   PHE B O   
2546 C CB  . PHE B 3   ? 0.6436 0.5927 0.7150 -0.1038 -0.1734 -0.2335 3   PHE B CB  
2547 C CG  . PHE B 3   ? 0.6111 0.5800 0.7090 -0.1035 -0.1636 -0.2187 3   PHE B CG  
2548 C CD1 . PHE B 3   ? 0.6428 0.6060 0.7292 -0.0952 -0.1475 -0.2044 3   PHE B CD1 
2549 C CD2 . PHE B 3   ? 0.6019 0.5968 0.7367 -0.1116 -0.1704 -0.2202 3   PHE B CD2 
2550 C CE1 . PHE B 3   ? 0.5637 0.5449 0.6727 -0.0949 -0.1387 -0.1921 3   PHE B CE1 
2551 C CE2 . PHE B 3   ? 0.6731 0.6878 0.8317 -0.1112 -0.1602 -0.2083 3   PHE B CE2 
2552 C CZ  . PHE B 3   ? 0.5556 0.5624 0.6999 -0.1027 -0.1445 -0.1943 3   PHE B CZ  
2553 N N   . GLY B 4   ? 0.7129 0.6354 0.6855 -0.0863 -0.1987 -0.2559 4   GLY B N   
2554 C CA  . GLY B 4   ? 0.7511 0.6604 0.6944 -0.0874 -0.2104 -0.2731 4   GLY B CA  
2555 C C   . GLY B 4   ? 0.7717 0.6598 0.7164 -0.0943 -0.2046 -0.2875 4   GLY B C   
2556 O O   . GLY B 4   ? 0.8030 0.6808 0.7266 -0.0963 -0.2156 -0.3047 4   GLY B O   
2557 N N   . ALA B 5   ? 0.8313 0.7108 0.7987 -0.0977 -0.1886 -0.2816 5   ALA B N   
2558 C CA  . ALA B 5   ? 0.7925 0.6481 0.7625 -0.1034 -0.1842 -0.2950 5   ALA B CA  
2559 C C   . ALA B 5   ? 0.7792 0.6159 0.7175 -0.0930 -0.1701 -0.2972 5   ALA B C   
2560 O O   . ALA B 5   ? 0.8115 0.6360 0.7213 -0.0904 -0.1746 -0.3136 5   ALA B O   
2561 C CB  . ALA B 5   ? 0.7514 0.6049 0.7616 -0.1134 -0.1763 -0.2875 5   ALA B CB  
2562 N N   . ILE B 6   ? 0.7528 0.5883 0.6961 -0.0870 -0.1528 -0.2818 6   ILE B N   
2563 C CA  . ILE B 6   ? 0.7588 0.5802 0.6773 -0.0769 -0.1384 -0.2836 6   ILE B CA  
2564 C C   . ILE B 6   ? 0.8315 0.6612 0.7113 -0.0690 -0.1401 -0.2840 6   ILE B C   
2565 O O   . ILE B 6   ? 0.7533 0.5999 0.6299 -0.0669 -0.1437 -0.2706 6   ILE B O   
2566 C CB  . ILE B 6   ? 0.7274 0.5482 0.6629 -0.0729 -0.1215 -0.2662 6   ILE B CB  
2567 C CG1 . ILE B 6   ? 0.7245 0.5327 0.6933 -0.0817 -0.1204 -0.2656 6   ILE B CG1 
2568 C CG2 . ILE B 6   ? 0.7316 0.5430 0.6440 -0.0617 -0.1071 -0.2679 6   ILE B CG2 
2569 C CD1 . ILE B 6   ? 0.6984 0.5037 0.6824 -0.0785 -0.1055 -0.2487 6   ILE B CD1 
2570 N N   . ALA B 7   ? 0.8000 0.6170 0.6496 -0.0649 -0.1375 -0.2998 7   ALA B N   
2571 C CA  . ALA B 7   ? 0.8209 0.6430 0.6281 -0.0599 -0.1400 -0.3029 7   ALA B CA  
2572 C C   . ALA B 7   ? 0.8334 0.6669 0.6329 -0.0648 -0.1614 -0.3037 7   ALA B C   
2573 O O   . ALA B 7   ? 0.8418 0.6830 0.6117 -0.0611 -0.1659 -0.2971 7   ALA B O   
2574 C CB  . ALA B 7   ? 0.7995 0.6298 0.5933 -0.0522 -0.1249 -0.2852 7   ALA B CB  
2575 N N   . GLY B 8   ? 0.8851 0.7193 0.7118 -0.0734 -0.1754 -0.3117 8   GLY B N   
2576 C CA  . GLY B 8   ? 0.8947 0.7410 0.7198 -0.0782 -0.1978 -0.3154 8   GLY B CA  
2577 C C   . GLY B 8   ? 0.9257 0.7610 0.7434 -0.0850 -0.2118 -0.3394 8   GLY B C   
2578 O O   . GLY B 8   ? 0.9357 0.7576 0.7181 -0.0818 -0.2090 -0.3537 8   GLY B O   
2579 N N   . PHE B 9   ? 0.9690 0.8107 0.8202 -0.0949 -0.2264 -0.3452 9   PHE B N   
2580 C CA  . PHE B 9   ? 0.9253 0.7553 0.7720 -0.1026 -0.2404 -0.3690 9   PHE B CA  
2581 C C   . PHE B 9   ? 0.9640 0.7692 0.8154 -0.1039 -0.2267 -0.3809 9   PHE B C   
2582 O O   . PHE B 9   ? 1.1646 0.9571 1.0015 -0.1074 -0.2296 -0.3951 9   PHE B O   
2583 C CB  . PHE B 9   ? 0.9219 0.7675 0.8061 -0.1142 -0.2582 -0.3704 9   PHE B CB  
2584 C CG  . PHE B 9   ? 0.8889 0.7384 0.8231 -0.1222 -0.2507 -0.3618 9   PHE B CG  
2585 C CD1 . PHE B 9   ? 0.8980 0.7282 0.8520 -0.1309 -0.2435 -0.3693 9   PHE B CD1 
2586 C CD2 . PHE B 9   ? 0.8525 0.7255 0.8125 -0.1214 -0.2485 -0.3425 9   PHE B CD2 
2587 C CE1 . PHE B 9   ? 0.8723 0.7045 0.8691 -0.1400 -0.2370 -0.3605 9   PHE B CE1 
2588 C CE2 . PHE B 9   ? 0.8254 0.7036 0.8284 -0.1299 -0.2393 -0.3331 9   PHE B CE2 
2589 C CZ  . PHE B 9   ? 0.8360 0.6935 0.8562 -0.1398 -0.2334 -0.3413 9   PHE B CZ  
2590 N N   . ILE B 10  ? 0.9076 0.7069 0.7782 -0.1007 -0.2080 -0.3684 10  ILE B N   
2591 C CA  . ILE B 10  ? 0.9183 0.6932 0.7874 -0.0974 -0.1937 -0.3777 10  ILE B CA  
2592 C C   . ILE B 10  ? 0.9388 0.7141 0.7747 -0.0840 -0.1773 -0.3724 10  ILE B C   
2593 O O   . ILE B 10  ? 1.0818 0.8686 0.9232 -0.0788 -0.1658 -0.3519 10  ILE B O   
2594 C CB  . ILE B 10  ? 0.8929 0.6599 0.8039 -0.1027 -0.1846 -0.3665 10  ILE B CB  
2595 C CG1 . ILE B 10  ? 0.8964 0.6665 0.8411 -0.1184 -0.1998 -0.3701 10  ILE B CG1 
2596 C CG2 . ILE B 10  ? 0.9087 0.6479 0.8182 -0.0978 -0.1727 -0.3769 10  ILE B CG2 
2597 C CD1 . ILE B 10  ? 0.8754 0.6380 0.8590 -0.1263 -0.1912 -0.3574 10  ILE B CD1 
2598 N N   . GLU B 11  ? 0.9940 0.7576 0.7957 -0.0791 -0.1756 -0.3918 11  GLU B N   
2599 C CA  . GLU B 11  ? 0.9721 0.7415 0.7361 -0.0689 -0.1626 -0.3884 11  GLU B CA  
2600 C C   . GLU B 11  ? 0.9360 0.6985 0.7091 -0.0601 -0.1401 -0.3826 11  GLU B C   
2601 O O   . GLU B 11  ? 0.9172 0.6914 0.6773 -0.0536 -0.1274 -0.3679 11  GLU B O   
2602 C CB  . GLU B 11  ? 1.2332 0.9962 0.9551 -0.0682 -0.1669 -0.4087 11  GLU B CB  
2603 C CG  . GLU B 11  ? 1.4366 1.2109 1.1387 -0.0748 -0.1871 -0.4080 11  GLU B CG  
2604 C CD  . GLU B 11  ? 1.5141 1.2813 1.1749 -0.0762 -0.1888 -0.4236 11  GLU B CD  
2605 O OE1 . GLU B 11  ? 1.5485 1.2994 1.2120 -0.0767 -0.1821 -0.4386 11  GLU B OE1 
2606 O OE2 . GLU B 11  ? 1.6020 1.3790 1.2267 -0.0767 -0.1972 -0.4204 11  GLU B OE2 
2607 N N   . GLY B 12  ? 0.9428 0.6860 0.7383 -0.0596 -0.1357 -0.3940 12  GLY B N   
2608 C CA  . GLY B 12  ? 0.9599 0.6956 0.7626 -0.0496 -0.1165 -0.3923 12  GLY B CA  
2609 C C   . GLY B 12  ? 1.0041 0.7240 0.8484 -0.0518 -0.1152 -0.3863 12  GLY B C   
2610 O O   . GLY B 12  ? 1.0603 0.7756 0.9283 -0.0626 -0.1276 -0.3829 12  GLY B O   
2611 N N   . GLY B 13  ? 0.9321 0.6441 0.7848 -0.0418 -0.1000 -0.3849 13  GLY B N   
2612 C CA  . GLY B 13  ? 0.8970 0.5910 0.7850 -0.0422 -0.0981 -0.3780 13  GLY B CA  
2613 C C   . GLY B 13  ? 1.0288 0.6959 0.9215 -0.0367 -0.0971 -0.3983 13  GLY B C   
2614 O O   . GLY B 13  ? 0.9923 0.6597 0.8600 -0.0300 -0.0918 -0.4136 13  GLY B O   
2615 N N   . TRP B 14  ? 1.0639 0.7095 0.9864 -0.0399 -0.0998 -0.3918 14  TRP B N   
2616 C CA  . TRP B 14  ? 0.9658 0.5847 0.8945 -0.0356 -0.0992 -0.4027 14  TRP B CA  
2617 C C   . TRP B 14  ? 0.9548 0.5642 0.8995 -0.0224 -0.0879 -0.3962 14  TRP B C   
2618 O O   . TRP B 14  ? 0.9709 0.5713 0.9401 -0.0255 -0.0892 -0.3797 14  TRP B O   
2619 C CB  . TRP B 14  ? 0.9822 0.5806 0.9306 -0.0504 -0.1124 -0.3999 14  TRP B CB  
2620 C CG  . TRP B 14  ? 1.1371 0.7448 1.0731 -0.0631 -0.1248 -0.4078 14  TRP B CG  
2621 C CD1 . TRP B 14  ? 1.1318 0.7550 1.0367 -0.0608 -0.1262 -0.4213 14  TRP B CD1 
2622 C CD2 . TRP B 14  ? 0.9999 0.6032 0.9545 -0.0806 -0.1378 -0.4021 14  TRP B CD2 
2623 N NE1 . TRP B 14  ? 1.0719 0.6999 0.9752 -0.0748 -0.1407 -0.4244 14  TRP B NE1 
2624 C CE2 . TRP B 14  ? 1.0160 0.6336 0.9513 -0.0871 -0.1477 -0.4134 14  TRP B CE2 
2625 C CE3 . TRP B 14  ? 0.9925 0.5820 0.9777 -0.0922 -0.1416 -0.3881 14  TRP B CE3 
2626 C CZ2 . TRP B 14  ? 1.0228 0.6433 0.9717 -0.1039 -0.1615 -0.4120 14  TRP B CZ2 
2627 C CZ3 . TRP B 14  ? 0.9997 0.5923 0.9974 -0.1100 -0.1537 -0.3866 14  TRP B CZ3 
2628 C CH2 . TRP B 14  ? 1.0137 0.6227 0.9949 -0.1153 -0.1637 -0.3990 14  TRP B CH2 
2629 N N   . THR B 15  ? 0.9703 0.5825 0.9014 -0.0079 -0.0769 -0.4091 15  THR B N   
2630 C CA  . THR B 15  ? 0.9663 0.5690 0.9151 0.0059  -0.0679 -0.4054 15  THR B CA  
2631 C C   . THR B 15  ? 0.9939 0.5625 0.9634 0.0053  -0.0756 -0.4057 15  THR B C   
2632 O O   . THR B 15  ? 0.9873 0.5436 0.9770 0.0133  -0.0729 -0.3960 15  THR B O   
2633 C CB  . THR B 15  ? 0.9792 0.5961 0.9105 0.0210  -0.0540 -0.4207 15  THR B CB  
2634 O OG1 . THR B 15  ? 1.0210 0.6305 0.9329 0.0199  -0.0568 -0.4407 15  THR B OG1 
2635 C CG2 . THR B 15  ? 0.9508 0.6003 0.8631 0.0221  -0.0442 -0.4166 15  THR B CG2 
2636 N N   . GLY B 16  ? 1.0548 0.6075 1.0190 -0.0044 -0.0856 -0.4162 16  GLY B N   
2637 C CA  . GLY B 16  ? 1.1558 0.6743 1.1371 -0.0064 -0.0932 -0.4173 16  GLY B CA  
2638 C C   . GLY B 16  ? 1.1260 0.6283 1.1310 -0.0186 -0.1009 -0.3957 16  GLY B C   
2639 O O   . GLY B 16  ? 1.1601 0.6322 1.1800 -0.0191 -0.1058 -0.3925 16  GLY B O   
2640 N N   . MET B 17  ? 1.0093 0.5303 1.0173 -0.0288 -0.1020 -0.3807 17  MET B N   
2641 C CA  . MET B 17  ? 1.0484 0.5580 1.0780 -0.0413 -0.1072 -0.3588 17  MET B CA  
2642 C C   . MET B 17  ? 0.9608 0.4760 1.0001 -0.0305 -0.0988 -0.3431 17  MET B C   
2643 O O   . MET B 17  ? 1.0502 0.5929 1.0828 -0.0263 -0.0922 -0.3400 17  MET B O   
2644 C CB  . MET B 17  ? 0.9724 0.5007 1.0022 -0.0595 -0.1137 -0.3527 17  MET B CB  
2645 C CG  . MET B 17  ? 1.0827 0.6025 1.1348 -0.0747 -0.1175 -0.3305 17  MET B CG  
2646 S SD  . MET B 17  ? 1.1065 0.6516 1.1637 -0.0962 -0.1255 -0.3262 17  MET B SD  
2647 C CE  . MET B 17  ? 1.1082 0.6918 1.1485 -0.0853 -0.1194 -0.3297 17  MET B CE  
2648 N N   . VAL B 18  ? 1.0502 0.5389 1.1046 -0.0260 -0.0999 -0.3330 18  VAL B N   
2649 C CA  . VAL B 18  ? 1.1063 0.5971 1.1696 -0.0128 -0.0932 -0.3203 18  VAL B CA  
2650 C C   . VAL B 18  ? 1.0947 0.5688 1.1741 -0.0235 -0.0976 -0.2948 18  VAL B C   
2651 O O   . VAL B 18  ? 1.1146 0.5842 1.2020 -0.0134 -0.0945 -0.2822 18  VAL B O   
2652 C CB  . VAL B 18  ? 1.1430 0.6203 1.2080 0.0069  -0.0899 -0.3319 18  VAL B CB  
2653 C CG1 . VAL B 18  ? 1.0817 0.5780 1.1290 0.0167  -0.0833 -0.3567 18  VAL B CG1 
2654 C CG2 . VAL B 18  ? 1.0256 0.4640 1.1001 0.0030  -0.0993 -0.3305 18  VAL B CG2 
2655 N N   . ASP B 19  ? 1.0801 0.5458 1.1641 -0.0442 -0.1046 -0.2866 19  ASP B N   
2656 C CA  . ASP B 19  ? 1.0849 0.5340 1.1818 -0.0570 -0.1076 -0.2619 19  ASP B CA  
2657 C C   . ASP B 19  ? 1.0377 0.5107 1.1392 -0.0737 -0.1064 -0.2491 19  ASP B C   
2658 O O   . ASP B 19  ? 1.0578 0.5202 1.1692 -0.0885 -0.1081 -0.2290 19  ASP B O   
2659 C CB  . ASP B 19  ? 1.1661 0.5805 1.2680 -0.0689 -0.1157 -0.2602 19  ASP B CB  
2660 C CG  . ASP B 19  ? 1.2930 0.7125 1.3911 -0.0832 -0.1208 -0.2753 19  ASP B CG  
2661 O OD1 . ASP B 19  ? 1.4468 0.8915 1.5344 -0.0777 -0.1190 -0.2924 19  ASP B OD1 
2662 O OD2 . ASP B 19  ? 1.1914 0.5900 1.2960 -0.1002 -0.1268 -0.2698 19  ASP B OD2 
2663 N N   . GLY B 20  ? 1.0351 0.5445 1.1264 -0.0717 -0.1016 -0.2569 20  GLY B N   
2664 C CA  . GLY B 20  ? 0.8537 0.3951 0.9458 -0.0854 -0.0977 -0.2407 20  GLY B CA  
2665 C C   . GLY B 20  ? 0.8293 0.4079 0.9064 -0.0794 -0.0935 -0.2505 20  GLY B C   
2666 O O   . GLY B 20  ? 0.8383 0.4186 0.9021 -0.0660 -0.0924 -0.2692 20  GLY B O   
2667 N N   . TRP B 21  ? 0.8007 0.4088 0.8795 -0.0897 -0.0911 -0.2374 21  TRP B N   
2668 C CA  . TRP B 21  ? 0.7772 0.4202 0.8417 -0.0851 -0.0883 -0.2423 21  TRP B CA  
2669 C C   . TRP B 21  ? 0.7927 0.4417 0.8554 -0.0958 -0.0991 -0.2585 21  TRP B C   
2670 O O   . TRP B 21  ? 0.8033 0.4578 0.8483 -0.0883 -0.1018 -0.2765 21  TRP B O   
2671 C CB  . TRP B 21  ? 0.7676 0.4394 0.8357 -0.0882 -0.0809 -0.2203 21  TRP B CB  
2672 C CG  . TRP B 21  ? 0.7181 0.3955 0.7799 -0.0740 -0.0702 -0.2085 21  TRP B CG  
2673 C CD1 . TRP B 21  ? 0.8318 0.5057 0.8814 -0.0574 -0.0654 -0.2179 21  TRP B CD1 
2674 C CD2 . TRP B 21  ? 0.6918 0.3808 0.7601 -0.0757 -0.0629 -0.1861 21  TRP B CD2 
2675 N NE1 . TRP B 21  ? 0.6985 0.3816 0.7482 -0.0490 -0.0564 -0.2025 21  TRP B NE1 
2676 C CE2 . TRP B 21  ? 0.6804 0.3717 0.7402 -0.0597 -0.0552 -0.1829 21  TRP B CE2 
2677 C CE3 . TRP B 21  ? 0.6782 0.3772 0.7588 -0.0895 -0.0618 -0.1696 21  TRP B CE3 
2678 C CZ2 . TRP B 21  ? 0.6595 0.3611 0.7218 -0.0571 -0.0478 -0.1637 21  TRP B CZ2 
2679 C CZ3 . TRP B 21  ? 0.6552 0.3644 0.7366 -0.0866 -0.0534 -0.1508 21  TRP B CZ3 
2680 C CH2 . TRP B 21  ? 0.6448 0.3543 0.7166 -0.0705 -0.0472 -0.1480 21  TRP B CH2 
2681 N N   . TYR B 22  ? 0.7956 0.4450 0.8762 -0.1139 -0.1052 -0.2525 22  TYR B N   
2682 C CA  . TYR B 22  ? 0.9344 0.5910 1.0182 -0.1258 -0.1171 -0.2671 22  TYR B CA  
2683 C C   . TYR B 22  ? 0.8915 0.5128 0.9881 -0.1372 -0.1259 -0.2778 22  TYR B C   
2684 O O   . TYR B 22  ? 0.9508 0.5525 1.0634 -0.1463 -0.1238 -0.2644 22  TYR B O   
2685 C CB  . TYR B 22  ? 0.8162 0.5043 0.9148 -0.1387 -0.1178 -0.2542 22  TYR B CB  
2686 C CG  . TYR B 22  ? 0.7462 0.4587 0.8420 -0.1310 -0.1061 -0.2343 22  TYR B CG  
2687 C CD1 . TYR B 22  ? 0.7286 0.4590 0.8032 -0.1155 -0.1020 -0.2357 22  TYR B CD1 
2688 C CD2 . TYR B 22  ? 0.7302 0.4474 0.8434 -0.1402 -0.0991 -0.2143 22  TYR B CD2 
2689 C CE1 . TYR B 22  ? 0.6956 0.4465 0.7682 -0.1090 -0.0921 -0.2184 22  TYR B CE1 
2690 C CE2 . TYR B 22  ? 0.6972 0.4360 0.8072 -0.1331 -0.0889 -0.1978 22  TYR B CE2 
2691 C CZ  . TYR B 22  ? 0.6796 0.4347 0.7703 -0.1173 -0.0859 -0.2002 22  TYR B CZ  
2692 O OH  . TYR B 22  ? 0.6488 0.4237 0.7368 -0.1107 -0.0765 -0.1845 22  TYR B OH  
2693 N N   . GLY B 23  ? 0.8994 0.5111 0.9876 -0.1373 -0.1363 -0.3016 23  GLY B N   
2694 C CA  . GLY B 23  ? 0.9189 0.4989 1.0128 -0.1455 -0.1422 -0.3087 23  GLY B CA  
2695 C C   . GLY B 23  ? 0.9459 0.5306 1.0302 -0.1510 -0.1526 -0.3277 23  GLY B C   
2696 O O   . GLY B 23  ? 0.9631 0.5765 1.0410 -0.1522 -0.1580 -0.3343 23  GLY B O   
2697 N N   . TYR B 24  ? 1.0753 0.6301 1.1579 -0.1538 -0.1561 -0.3362 24  TYR B N   
2698 C CA  . TYR B 24  ? 1.0207 0.5730 1.0971 -0.1620 -0.1666 -0.3534 24  TYR B CA  
2699 C C   . TYR B 24  ? 1.0674 0.5988 1.1212 -0.1468 -0.1658 -0.3725 24  TYR B C   
2700 O O   . TYR B 24  ? 1.1776 0.6973 1.2233 -0.1303 -0.1570 -0.3721 24  TYR B O   
2701 C CB  . TYR B 24  ? 1.0450 0.5800 1.1429 -0.1832 -0.1719 -0.3470 24  TYR B CB  
2702 C CG  . TYR B 24  ? 1.0169 0.5722 1.1394 -0.2004 -0.1708 -0.3281 24  TYR B CG  
2703 C CD1 . TYR B 24  ? 1.0008 0.5910 1.1322 -0.2109 -0.1778 -0.3308 24  TYR B CD1 
2704 C CD2 . TYR B 24  ? 1.0094 0.5495 1.1464 -0.2064 -0.1628 -0.3077 24  TYR B CD2 
2705 C CE1 . TYR B 24  ? 0.9760 0.5880 1.1325 -0.2264 -0.1756 -0.3149 24  TYR B CE1 
2706 C CE2 . TYR B 24  ? 0.9862 0.5465 1.1450 -0.2231 -0.1600 -0.2909 24  TYR B CE2 
2707 C CZ  . TYR B 24  ? 1.0212 0.6186 1.1910 -0.2330 -0.1659 -0.2952 24  TYR B CZ  
2708 O OH  . TYR B 24  ? 1.0996 0.7207 1.2935 -0.2491 -0.1619 -0.2797 24  TYR B OH  
2709 N N   . HIS B 25  ? 1.3090 0.8368 1.3539 -0.1530 -0.1752 -0.3897 25  HIS B N   
2710 C CA  . HIS B 25  ? 1.3966 0.9031 1.4216 -0.1415 -0.1750 -0.4096 25  HIS B CA  
2711 C C   . HIS B 25  ? 1.4078 0.9044 1.4343 -0.1565 -0.1872 -0.4228 25  HIS B C   
2712 O O   . HIS B 25  ? 1.3907 0.9098 1.4076 -0.1622 -0.1955 -0.4319 25  HIS B O   
2713 C CB  . HIS B 25  ? 1.4236 0.9501 1.4202 -0.1245 -0.1703 -0.4216 25  HIS B CB  
2714 C CG  . HIS B 25  ? 1.5860 1.0976 1.5602 -0.1161 -0.1712 -0.4447 25  HIS B CG  
2715 N ND1 . HIS B 25  ? 1.5960 1.0819 1.5678 -0.1028 -0.1637 -0.4516 25  HIS B ND1 
2716 C CD2 . HIS B 25  ? 1.6406 1.1599 1.5938 -0.1190 -0.1790 -0.4626 25  HIS B CD2 
2717 C CE1 . HIS B 25  ? 1.5732 1.0522 1.5240 -0.0979 -0.1658 -0.4736 25  HIS B CE1 
2718 N NE2 . HIS B 25  ? 1.6170 1.1153 1.5548 -0.1081 -0.1750 -0.4804 25  HIS B NE2 
2719 N N   . HIS B 26  ? 1.3703 0.8327 1.4080 -0.1627 -0.1888 -0.4238 26  HIS B N   
2720 C CA  . HIS B 26  ? 1.2422 0.6923 1.2846 -0.1792 -0.2001 -0.4349 26  HIS B CA  
2721 C C   . HIS B 26  ? 1.4248 0.8493 1.4486 -0.1691 -0.2018 -0.4575 26  HIS B C   
2722 O O   . HIS B 26  ? 1.3185 0.7227 1.3366 -0.1530 -0.1939 -0.4601 26  HIS B O   
2723 C CB  . HIS B 26  ? 1.2742 0.7037 1.3435 -0.1980 -0.2016 -0.4190 26  HIS B CB  
2724 C CG  . HIS B 26  ? 1.3167 0.7052 1.3894 -0.1912 -0.1963 -0.4153 26  HIS B CG  
2725 N ND1 . HIS B 26  ? 1.4614 0.8168 1.5292 -0.1913 -0.2013 -0.4310 26  HIS B ND1 
2726 C CD2 . HIS B 26  ? 1.4202 0.7950 1.5007 -0.1837 -0.1875 -0.3976 26  HIS B CD2 
2727 C CE1 . HIS B 26  ? 1.4213 0.7444 1.4945 -0.1835 -0.1960 -0.4231 26  HIS B CE1 
2728 N NE2 . HIS B 26  ? 1.3217 0.6560 1.4022 -0.1788 -0.1879 -0.4025 26  HIS B NE2 
2729 N N   . GLN B 27  ? 1.6418 1.0688 1.6571 -0.1786 -0.2126 -0.4746 27  GLN B N   
2730 C CA  . GLN B 27  ? 1.7116 1.1150 1.7088 -0.1715 -0.2154 -0.4981 27  GLN B CA  
2731 C C   . GLN B 27  ? 1.6919 1.0842 1.6979 -0.1921 -0.2287 -0.5072 27  GLN B C   
2732 O O   . GLN B 27  ? 1.7168 1.1332 1.7164 -0.2014 -0.2382 -0.5143 27  GLN B O   
2733 C CB  . GLN B 27  ? 1.7218 1.1462 1.6871 -0.1564 -0.2131 -0.5145 27  GLN B CB  
2734 C CG  . GLN B 27  ? 1.8706 1.2727 1.8157 -0.1494 -0.2152 -0.5401 27  GLN B CG  
2735 C CD  . GLN B 27  ? 1.8930 1.3182 1.8042 -0.1426 -0.2166 -0.5569 27  GLN B CD  
2736 O OE1 . GLN B 27  ? 1.7895 1.2470 1.6918 -0.1430 -0.2170 -0.5490 27  GLN B OE1 
2737 N NE2 . GLN B 27  ? 1.9065 1.3146 1.7976 -0.1366 -0.2175 -0.5801 27  GLN B NE2 
2738 N N   . ASN B 28  ? 1.5943 0.9499 1.6147 -0.1993 -0.2300 -0.5067 28  ASN B N   
2739 C CA  . ASN B 28  ? 1.4879 0.8277 1.5172 -0.2193 -0.2419 -0.5159 28  ASN B CA  
2740 C C   . ASN B 28  ? 1.7852 1.0851 1.8046 -0.2118 -0.2432 -0.5353 28  ASN B C   
2741 O O   . ASN B 28  ? 1.7613 1.0511 1.7660 -0.1904 -0.2353 -0.5434 28  ASN B O   
2742 C CB  . ASN B 28  ? 1.4787 0.8126 1.5380 -0.2408 -0.2429 -0.4945 28  ASN B CB  
2743 C CG  . ASN B 28  ? 1.4768 0.7808 1.5475 -0.2351 -0.2331 -0.4775 28  ASN B CG  
2744 O OD1 . ASN B 28  ? 1.4919 0.7735 1.5515 -0.2160 -0.2277 -0.4843 28  ASN B OD1 
2745 N ND2 . ASN B 28  ? 1.4602 0.7646 1.5530 -0.2520 -0.2309 -0.4552 28  ASN B ND2 
2746 N N   . GLU B 29  ? 1.8738 1.1516 1.9028 -0.2298 -0.2531 -0.5431 29  GLU B N   
2747 C CA  . GLU B 29  ? 1.9432 1.1813 1.9645 -0.2245 -0.2558 -0.5626 29  GLU B CA  
2748 C C   . GLU B 29  ? 1.9412 1.1467 1.9699 -0.2103 -0.2464 -0.5533 29  GLU B C   
2749 O O   . GLU B 29  ? 2.0241 1.2064 2.0409 -0.1936 -0.2442 -0.5699 29  GLU B O   
2750 C CB  . GLU B 29  ? 2.1150 1.3341 2.1493 -0.2492 -0.2680 -0.5688 29  GLU B CB  
2751 C CG  . GLU B 29  ? 2.1911 1.3667 2.2189 -0.2459 -0.2722 -0.5896 29  GLU B CG  
2752 C CD  . GLU B 29  ? 2.2583 1.4405 2.2572 -0.2316 -0.2751 -0.6179 29  GLU B CD  
2753 O OE1 . GLU B 29  ? 2.2451 1.4646 2.2294 -0.2316 -0.2779 -0.6229 29  GLU B OE1 
2754 O OE2 . GLU B 29  ? 2.3105 1.4603 2.3008 -0.2204 -0.2746 -0.6353 29  GLU B OE2 
2755 N N   . GLN B 30  ? 1.7523 0.9561 1.8004 -0.2164 -0.2411 -0.5269 30  GLN B N   
2756 C CA  . GLN B 30  ? 1.7580 0.9310 1.8137 -0.2035 -0.2336 -0.5156 30  GLN B CA  
2757 C C   . GLN B 30  ? 1.8272 1.0165 1.8709 -0.1765 -0.2229 -0.5153 30  GLN B C   
2758 O O   . GLN B 30  ? 1.7519 0.9172 1.8002 -0.1617 -0.2174 -0.5098 30  GLN B O   
2759 C CB  . GLN B 30  ? 1.7492 0.9146 1.8272 -0.2205 -0.2314 -0.4868 30  GLN B CB  
2760 C CG  . GLN B 30  ? 1.7248 0.8809 1.8167 -0.2503 -0.2400 -0.4843 30  GLN B CG  
2761 C CD  . GLN B 30  ? 1.7658 0.9065 1.8775 -0.2668 -0.2359 -0.4566 30  GLN B CD  
2762 O OE1 . GLN B 30  ? 1.6689 0.8293 1.7937 -0.2894 -0.2368 -0.4443 30  GLN B OE1 
2763 N NE2 . GLN B 30  ? 1.8806 0.9863 1.9943 -0.2555 -0.2313 -0.4467 30  GLN B NE2 
2764 N N   . GLY B 31  ? 1.8886 1.1176 1.9173 -0.1700 -0.2202 -0.5208 31  GLY B N   
2765 C CA  . GLY B 31  ? 1.8285 1.0757 1.8448 -0.1462 -0.2093 -0.5211 31  GLY B CA  
2766 C C   . GLY B 31  ? 1.7332 1.0209 1.7499 -0.1484 -0.2047 -0.5044 31  GLY B C   
2767 O O   . GLY B 31  ? 1.7075 1.0119 1.7337 -0.1675 -0.2104 -0.4941 31  GLY B O   
2768 N N   . SER B 32  ? 1.5544 0.8587 1.5614 -0.1284 -0.1942 -0.5024 32  SER B N   
2769 C CA  . SER B 32  ? 1.5117 0.8536 1.5165 -0.1271 -0.1888 -0.4882 32  SER B CA  
2770 C C   . SER B 32  ? 1.5108 0.8488 1.5285 -0.1160 -0.1790 -0.4681 32  SER B C   
2771 O O   . SER B 32  ? 1.4032 0.7108 1.4301 -0.1081 -0.1770 -0.4657 32  SER B O   
2772 C CB  . SER B 32  ? 1.4059 0.7760 1.3829 -0.1146 -0.1851 -0.5050 32  SER B CB  
2773 O OG  . SER B 32  ? 1.4184 0.7760 1.3835 -0.0940 -0.1768 -0.5193 32  SER B OG  
2774 N N   . GLY B 33  ? 1.4891 0.8580 1.5074 -0.1153 -0.1739 -0.4535 33  GLY B N   
2775 C CA  . GLY B 33  ? 1.5370 0.9060 1.5662 -0.1053 -0.1650 -0.4343 33  GLY B CA  
2776 C C   . GLY B 33  ? 1.3896 0.7918 1.4230 -0.1114 -0.1620 -0.4170 33  GLY B C   
2777 O O   . GLY B 33  ? 1.4101 0.8318 1.4453 -0.1272 -0.1683 -0.4150 33  GLY B O   
2778 N N   . TYR B 34  ? 1.3635 0.7730 1.3995 -0.0978 -0.1526 -0.4049 34  TYR B N   
2779 C CA  . TYR B 34  ? 1.1601 0.5965 1.2024 -0.1015 -0.1485 -0.3863 34  TYR B CA  
2780 C C   . TYR B 34  ? 1.1244 0.5432 1.1886 -0.1116 -0.1483 -0.3624 34  TYR B C   
2781 O O   . TYR B 34  ? 1.2242 0.6107 1.2953 -0.1076 -0.1483 -0.3583 34  TYR B O   
2782 C CB  . TYR B 34  ? 1.1026 0.5589 1.1334 -0.0811 -0.1377 -0.3874 34  TYR B CB  
2783 C CG  . TYR B 34  ? 1.1420 0.6204 1.1473 -0.0719 -0.1353 -0.4078 34  TYR B CG  
2784 C CD1 . TYR B 34  ? 1.0957 0.6046 1.0900 -0.0794 -0.1382 -0.4085 34  TYR B CD1 
2785 C CD2 . TYR B 34  ? 1.1330 0.6026 1.1245 -0.0554 -0.1298 -0.4257 34  TYR B CD2 
2786 C CE1 . TYR B 34  ? 1.1413 0.6688 1.1083 -0.0717 -0.1362 -0.4251 34  TYR B CE1 
2787 C CE2 . TYR B 34  ? 1.1423 0.6323 1.1077 -0.0483 -0.1261 -0.4432 34  TYR B CE2 
2788 C CZ  . TYR B 34  ? 1.2473 0.7651 1.1988 -0.0569 -0.1295 -0.4421 34  TYR B CZ  
2789 O OH  . TYR B 34  ? 1.1942 0.7304 1.1159 -0.0507 -0.1262 -0.4578 34  TYR B OH  
2790 N N   . ALA B 35  ? 1.0898 0.5301 1.1640 -0.1247 -0.1482 -0.3462 35  ALA B N   
2791 C CA  . ALA B 35  ? 1.0802 0.5082 1.1725 -0.1354 -0.1462 -0.3219 35  ALA B CA  
2792 C C   . ALA B 35  ? 1.0973 0.5596 1.1964 -0.1425 -0.1427 -0.3078 35  ALA B C   
2793 O O   . ALA B 35  ? 1.2160 0.7038 1.3166 -0.1535 -0.1473 -0.3132 35  ALA B O   
2794 C CB  . ALA B 35  ? 1.1168 0.5203 1.2206 -0.1565 -0.1532 -0.3182 35  ALA B CB  
2795 N N   . ALA B 36  ? 1.0066 0.4694 1.1109 -0.1360 -0.1354 -0.2901 36  ALA B N   
2796 C CA  . ALA B 36  ? 0.9612 0.4557 1.0720 -0.1405 -0.1311 -0.2772 36  ALA B CA  
2797 C C   . ALA B 36  ? 0.9838 0.4807 1.1134 -0.1646 -0.1324 -0.2598 36  ALA B C   
2798 O O   . ALA B 36  ? 1.0433 0.5119 1.1797 -0.1737 -0.1320 -0.2467 36  ALA B O   
2799 C CB  . ALA B 36  ? 0.9585 0.4527 1.0671 -0.1241 -0.1226 -0.2656 36  ALA B CB  
2800 N N   . ASP B 37  ? 1.0487 0.5804 1.1862 -0.1751 -0.1335 -0.2596 37  ASP B N   
2801 C CA  . ASP B 37  ? 1.0637 0.6064 1.2214 -0.1975 -0.1321 -0.2431 37  ASP B CA  
2802 C C   . ASP B 37  ? 1.0354 0.5775 1.1987 -0.1961 -0.1226 -0.2205 37  ASP B C   
2803 O O   . ASP B 37  ? 1.1213 0.6913 1.2741 -0.1818 -0.1144 -0.2140 37  ASP B O   
2804 C CB  . ASP B 37  ? 1.0468 0.6311 1.2138 -0.2062 -0.1362 -0.2504 37  ASP B CB  
2805 C CG  . ASP B 37  ? 1.1350 0.7354 1.3261 -0.2300 -0.1339 -0.2361 37  ASP B CG  
2806 O OD1 . ASP B 37  ? 1.2089 0.7838 1.4061 -0.2441 -0.1318 -0.2249 37  ASP B OD1 
2807 O OD2 . ASP B 37  ? 1.1388 0.7786 1.3414 -0.2345 -0.1335 -0.2356 37  ASP B OD2 
2808 N N   . GLN B 38  ? 0.9717 0.4888 1.1412 -0.2091 -0.1199 -0.2030 38  GLN B N   
2809 C CA  . GLN B 38  ? 1.0070 0.5170 1.1753 -0.2061 -0.1113 -0.1802 38  GLN B CA  
2810 C C   . GLN B 38  ? 0.9855 0.5353 1.1616 -0.2180 -0.1010 -0.1626 38  GLN B C   
2811 O O   . GLN B 38  ? 1.0567 0.6187 1.2245 -0.2090 -0.0914 -0.1461 38  GLN B O   
2812 C CB  . GLN B 38  ? 1.1725 0.6389 1.3380 -0.2138 -0.1122 -0.1671 38  GLN B CB  
2813 C CG  . GLN B 38  ? 1.4752 0.9080 1.6289 -0.1988 -0.1188 -0.1821 38  GLN B CG  
2814 C CD  . GLN B 38  ? 1.7192 1.1148 1.8739 -0.2133 -0.1221 -0.1762 38  GLN B CD  
2815 O OE1 . GLN B 38  ? 1.7628 1.1532 1.9236 -0.2332 -0.1179 -0.1570 38  GLN B OE1 
2816 N NE2 . GLN B 38  ? 1.7176 1.0875 1.8657 -0.2038 -0.1288 -0.1930 38  GLN B NE2 
2817 N N   . LYS B 39  ? 1.0108 0.5825 1.2041 -0.2376 -0.1031 -0.1669 39  LYS B N   
2818 C CA  . LYS B 39  ? 1.0520 0.6634 1.2560 -0.2489 -0.0929 -0.1523 39  LYS B CA  
2819 C C   . LYS B 39  ? 0.9607 0.6132 1.1562 -0.2304 -0.0882 -0.1552 39  LYS B C   
2820 O O   . LYS B 39  ? 0.9913 0.6619 1.1818 -0.2251 -0.0774 -0.1392 39  LYS B O   
2821 C CB  . LYS B 39  ? 1.0487 0.6753 1.2772 -0.2742 -0.0969 -0.1586 39  LYS B CB  
2822 C CG  . LYS B 39  ? 1.1407 0.8094 1.3846 -0.2873 -0.0856 -0.1452 39  LYS B CG  
2823 C CD  . LYS B 39  ? 1.2394 0.9208 1.5113 -0.3147 -0.0888 -0.1507 39  LYS B CD  
2824 C CE  . LYS B 39  ? 1.3852 1.0857 1.6674 -0.3119 -0.1025 -0.1755 39  LYS B CE  
2825 N NZ  . LYS B 39  ? 1.3450 1.0640 1.6488 -0.3357 -0.1049 -0.1784 39  LYS B NZ  
2826 N N   . SER B 40  ? 0.9070 0.5729 1.0992 -0.2209 -0.0967 -0.1755 40  SER B N   
2827 C CA  . SER B 40  ? 0.8394 0.5413 1.0218 -0.2044 -0.0937 -0.1780 40  SER B CA  
2828 C C   . SER B 40  ? 0.7708 0.4629 0.9317 -0.1831 -0.0866 -0.1706 40  SER B C   
2829 O O   . SER B 40  ? 0.7854 0.5020 0.9414 -0.1752 -0.0778 -0.1589 40  SER B O   
2830 C CB  . SER B 40  ? 0.8471 0.5598 1.0262 -0.1997 -0.1059 -0.2009 40  SER B CB  
2831 O OG  . SER B 40  ? 0.9279 0.6058 1.0938 -0.1921 -0.1130 -0.2157 40  SER B OG  
2832 N N   . THR B 41  ? 0.7822 0.4392 0.9317 -0.1735 -0.0906 -0.1783 41  THR B N   
2833 C CA  . THR B 41  ? 0.7964 0.4440 0.9293 -0.1537 -0.0842 -0.1724 41  THR B CA  
2834 C C   . THR B 41  ? 0.7456 0.3928 0.8806 -0.1568 -0.0745 -0.1482 41  THR B C   
2835 O O   . THR B 41  ? 0.7183 0.3829 0.8439 -0.1440 -0.0668 -0.1395 41  THR B O   
2836 C CB  . THR B 41  ? 0.7918 0.3998 0.9180 -0.1448 -0.0906 -0.1852 41  THR B CB  
2837 O OG1 . THR B 41  ? 0.8001 0.4129 0.9184 -0.1381 -0.0977 -0.2088 41  THR B OG1 
2838 C CG2 . THR B 41  ? 0.7848 0.3821 0.8996 -0.1260 -0.0842 -0.1775 41  THR B CG2 
2839 N N   . GLN B 42  ? 0.7676 0.3952 0.9138 -0.1748 -0.0749 -0.1371 42  GLN B N   
2840 C CA  . GLN B 42  ? 0.7615 0.3869 0.9061 -0.1792 -0.0660 -0.1136 42  GLN B CA  
2841 C C   . GLN B 42  ? 0.7246 0.3939 0.8731 -0.1829 -0.0564 -0.1044 42  GLN B C   
2842 O O   . GLN B 42  ? 0.7062 0.3845 0.8463 -0.1757 -0.0482 -0.0899 42  GLN B O   
2843 C CB  . GLN B 42  ? 0.7991 0.3931 0.9524 -0.2002 -0.0683 -0.1032 42  GLN B CB  
2844 C CG  . GLN B 42  ? 0.8414 0.4261 0.9876 -0.2044 -0.0603 -0.0784 42  GLN B CG  
2845 C CD  . GLN B 42  ? 0.8903 0.4573 1.0206 -0.1819 -0.0610 -0.0738 42  GLN B CD  
2846 O OE1 . GLN B 42  ? 1.0435 0.5842 1.1706 -0.1687 -0.0693 -0.0861 42  GLN B OE1 
2847 N NE2 . GLN B 42  ? 0.8073 0.3901 0.9288 -0.1771 -0.0524 -0.0573 42  GLN B NE2 
2848 N N   . ASN B 43  ? 0.7148 0.4120 0.8774 -0.1936 -0.0582 -0.1134 43  ASN B N   
2849 C CA  . ASN B 43  ? 0.6804 0.4204 0.8489 -0.1946 -0.0503 -0.1075 43  ASN B CA  
2850 C C   . ASN B 43  ? 0.6509 0.4079 0.8038 -0.1721 -0.0479 -0.1097 43  ASN B C   
2851 O O   . ASN B 43  ? 0.6269 0.4035 0.7762 -0.1675 -0.0390 -0.0978 43  ASN B O   
2852 C CB  . ASN B 43  ? 0.6790 0.4457 0.8676 -0.2075 -0.0554 -0.1197 43  ASN B CB  
2853 C CG  . ASN B 43  ? 1.0354 0.7982 1.2437 -0.2334 -0.0531 -0.1134 43  ASN B CG  
2854 O OD1 . ASN B 43  ? 1.0009 0.7557 1.2078 -0.2427 -0.0436 -0.0958 43  ASN B OD1 
2855 N ND2 . ASN B 43  ? 1.0518 0.8206 1.2778 -0.2461 -0.0619 -0.1276 43  ASN B ND2 
2856 N N   . ALA B 44  ? 0.6546 0.4041 0.7973 -0.1586 -0.0554 -0.1253 44  ALA B N   
2857 C CA  . ALA B 44  ? 0.6308 0.3943 0.7573 -0.1388 -0.0526 -0.1273 44  ALA B CA  
2858 C C   . ALA B 44  ? 0.6262 0.3755 0.7415 -0.1284 -0.0451 -0.1138 44  ALA B C   
2859 O O   . ALA B 44  ? 0.6001 0.3689 0.7083 -0.1188 -0.0385 -0.1063 44  ALA B O   
2860 C CB  . ALA B 44  ? 0.6425 0.3980 0.7581 -0.1285 -0.0610 -0.1468 44  ALA B CB  
2861 N N   . ILE B 45  ? 0.6532 0.3679 0.7677 -0.1301 -0.0473 -0.1108 45  ILE B N   
2862 C CA  . ILE B 45  ? 0.6527 0.3524 0.7580 -0.1200 -0.0426 -0.0980 45  ILE B CA  
2863 C C   . ILE B 45  ? 0.6369 0.3521 0.7439 -0.1280 -0.0340 -0.0784 45  ILE B C   
2864 O O   . ILE B 45  ? 0.6230 0.3472 0.7210 -0.1171 -0.0284 -0.0696 45  ILE B O   
2865 C CB  . ILE B 45  ? 0.7328 0.3897 0.8387 -0.1209 -0.0491 -0.0985 45  ILE B CB  
2866 C CG1 . ILE B 45  ? 0.7052 0.3483 0.8079 -0.1096 -0.0564 -0.1202 45  ILE B CG1 
2867 C CG2 . ILE B 45  ? 0.6923 0.3337 0.7906 -0.1118 -0.0461 -0.0832 45  ILE B CG2 
2868 C CD1 . ILE B 45  ? 0.7452 0.3447 0.8509 -0.1100 -0.0642 -0.1238 45  ILE B CD1 
2869 N N   . ASN B 46  ? 0.6455 0.3647 0.7640 -0.1476 -0.0325 -0.0721 46  ASN B N   
2870 C CA  . ASN B 46  ? 0.6528 0.3886 0.7721 -0.1566 -0.0229 -0.0549 46  ASN B CA  
2871 C C   . ASN B 46  ? 0.5961 0.3714 0.7151 -0.1482 -0.0170 -0.0567 46  ASN B C   
2872 O O   . ASN B 46  ? 0.5805 0.3657 0.6911 -0.1423 -0.0100 -0.0454 46  ASN B O   
2873 C CB  . ASN B 46  ? 0.6518 0.3877 0.7854 -0.1808 -0.0212 -0.0502 46  ASN B CB  
2874 C CG  . ASN B 46  ? 0.7649 0.4576 0.8973 -0.1911 -0.0268 -0.0451 46  ASN B CG  
2875 O OD1 . ASN B 46  ? 0.8473 0.5099 0.9674 -0.1799 -0.0309 -0.0409 46  ASN B OD1 
2876 N ND2 . ASN B 46  ? 0.7854 0.4747 0.9320 -0.2128 -0.0276 -0.0458 46  ASN B ND2 
2877 N N   . GLY B 47  ? 0.5838 0.3806 0.7112 -0.1473 -0.0209 -0.0710 47  GLY B N   
2878 C CA  . GLY B 47  ? 0.5523 0.3840 0.6802 -0.1396 -0.0171 -0.0726 47  GLY B CA  
2879 C C   . GLY B 47  ? 0.5358 0.3675 0.6466 -0.1202 -0.0155 -0.0717 47  GLY B C   
2880 O O   . GLY B 47  ? 0.5146 0.3645 0.6215 -0.1148 -0.0090 -0.0640 47  GLY B O   
2881 N N   . ILE B 48  ? 0.5468 0.3585 0.6481 -0.1098 -0.0211 -0.0805 48  ILE B N   
2882 C CA  . ILE B 48  ? 0.5330 0.3463 0.6197 -0.0924 -0.0189 -0.0810 48  ILE B CA  
2883 C C   . ILE B 48  ? 0.5328 0.3346 0.6140 -0.0886 -0.0134 -0.0666 48  ILE B C   
2884 O O   . ILE B 48  ? 0.5414 0.3557 0.6150 -0.0788 -0.0087 -0.0614 48  ILE B O   
2885 C CB  . ILE B 48  ? 0.5474 0.3453 0.6265 -0.0833 -0.0251 -0.0962 48  ILE B CB  
2886 C CG1 . ILE B 48  ? 0.5467 0.3592 0.6272 -0.0860 -0.0313 -0.1100 48  ILE B CG1 
2887 C CG2 . ILE B 48  ? 0.5922 0.3911 0.6583 -0.0668 -0.0212 -0.0965 48  ILE B CG2 
2888 C CD1 . ILE B 48  ? 0.7359 0.5330 0.8073 -0.0795 -0.0374 -0.1264 48  ILE B CD1 
2889 N N   . THR B 49  ? 0.5568 0.3333 0.6409 -0.0966 -0.0151 -0.0595 49  THR B N   
2890 C CA  . THR B 49  ? 0.5610 0.3254 0.6385 -0.0944 -0.0117 -0.0442 49  THR B CA  
2891 C C   . THR B 49  ? 0.5409 0.3301 0.6174 -0.0996 -0.0034 -0.0324 49  THR B C   
2892 O O   . THR B 49  ? 0.5286 0.3233 0.5965 -0.0909 0.0002  -0.0247 49  THR B O   
2893 C CB  . THR B 49  ? 0.5953 0.3266 0.6751 -0.1048 -0.0160 -0.0371 49  THR B CB  
2894 O OG1 . THR B 49  ? 0.6154 0.3213 0.6959 -0.0967 -0.0240 -0.0490 49  THR B OG1 
2895 C CG2 . THR B 49  ? 0.6030 0.3221 0.6736 -0.1042 -0.0137 -0.0190 49  THR B CG2 
2896 N N   . ASN B 50  ? 0.5383 0.3440 0.6248 -0.1139 -0.0004 -0.0323 50  ASN B N   
2897 C CA  . ASN B 50  ? 0.5206 0.3523 0.6079 -0.1187 0.0082  -0.0238 50  ASN B CA  
2898 C C   . ASN B 50  ? 0.4907 0.3478 0.5753 -0.1052 0.0099  -0.0299 50  ASN B C   
2899 O O   . ASN B 50  ? 0.5900 0.4620 0.6700 -0.1026 0.0161  -0.0225 50  ASN B O   
2900 C CB  . ASN B 50  ? 0.5744 0.4208 0.6771 -0.1369 0.0114  -0.0247 50  ASN B CB  
2901 C CG  . ASN B 50  ? 0.7713 0.6436 0.8757 -0.1431 0.0217  -0.0164 50  ASN B CG  
2902 O OD1 . ASN B 50  ? 0.9000 0.7637 0.9970 -0.1521 0.0277  -0.0030 50  ASN B OD1 
2903 N ND2 . ASN B 50  ? 0.8325 0.7360 0.9460 -0.1382 0.0235  -0.0247 50  ASN B ND2 
2904 N N   . LYS B 51  ? 0.4841 0.3450 0.5700 -0.0971 0.0041  -0.0431 51  LYS B N   
2905 C CA  . LYS B 51  ? 0.4812 0.3621 0.5620 -0.0850 0.0049  -0.0476 51  LYS B CA  
2906 C C   . LYS B 51  ? 0.6327 0.5059 0.7002 -0.0725 0.0073  -0.0420 51  LYS B C   
2907 O O   . LYS B 51  ? 0.6474 0.5354 0.7109 -0.0681 0.0121  -0.0365 51  LYS B O   
2908 C CB  . LYS B 51  ? 0.4637 0.3475 0.5449 -0.0805 -0.0024 -0.0620 51  LYS B CB  
2909 C CG  . LYS B 51  ? 0.5319 0.4270 0.6021 -0.0672 -0.0024 -0.0654 51  LYS B CG  
2910 C CD  . LYS B 51  ? 0.5003 0.3951 0.5657 -0.0634 -0.0099 -0.0786 51  LYS B CD  
2911 C CE  . LYS B 51  ? 0.5183 0.4341 0.5925 -0.0674 -0.0147 -0.0834 51  LYS B CE  
2912 N NZ  . LYS B 51  ? 0.5374 0.4547 0.5999 -0.0606 -0.0222 -0.0937 51  LYS B NZ  
2913 N N   . VAL B 52  ? 0.4869 0.3379 0.5491 -0.0665 0.0038  -0.0446 52  VAL B N   
2914 C CA  . VAL B 52  ? 0.4634 0.3088 0.5169 -0.0547 0.0055  -0.0404 52  VAL B CA  
2915 C C   . VAL B 52  ? 0.4632 0.3077 0.5140 -0.0582 0.0095  -0.0256 52  VAL B C   
2916 O O   . VAL B 52  ? 0.4896 0.3439 0.5345 -0.0510 0.0126  -0.0209 52  VAL B O   
2917 C CB  . VAL B 52  ? 0.5541 0.3760 0.6064 -0.0478 0.0007  -0.0470 52  VAL B CB  
2918 C CG1 . VAL B 52  ? 0.4773 0.2968 0.5246 -0.0353 0.0023  -0.0435 52  VAL B CG1 
2919 C CG2 . VAL B 52  ? 0.4850 0.3088 0.5366 -0.0447 -0.0025 -0.0627 52  VAL B CG2 
2920 N N   . ASN B 53  ? 0.4836 0.3158 0.5374 -0.0704 0.0093  -0.0179 53  ASN B N   
2921 C CA  . ASN B 53  ? 0.4857 0.3167 0.5333 -0.0757 0.0133  -0.0032 53  ASN B CA  
2922 C C   . ASN B 53  ? 0.4907 0.3503 0.5376 -0.0771 0.0204  -0.0013 53  ASN B C   
2923 O O   . ASN B 53  ? 0.5248 0.3890 0.5630 -0.0731 0.0233  0.0065  53  ASN B O   
2924 C CB  . ASN B 53  ? 0.5121 0.3259 0.5616 -0.0914 0.0129  0.0047  53  ASN B CB  
2925 C CG  . ASN B 53  ? 0.5399 0.3191 0.5855 -0.0887 0.0053  0.0089  53  ASN B CG  
2926 O OD1 . ASN B 53  ? 0.5388 0.3092 0.5803 -0.0745 0.0011  0.0076  53  ASN B OD1 
2927 N ND2 . ASN B 53  ? 0.5669 0.3261 0.6150 -0.1026 0.0032  0.0136  53  ASN B ND2 
2928 N N   . SER B 54  ? 0.5427 0.4216 0.5994 -0.0821 0.0224  -0.0091 54  SER B N   
2929 C CA  . SER B 54  ? 0.5054 0.4112 0.5639 -0.0818 0.0283  -0.0093 54  SER B CA  
2930 C C   . SER B 54  ? 0.5312 0.4443 0.5824 -0.0674 0.0275  -0.0120 54  SER B C   
2931 O O   . SER B 54  ? 0.7343 0.6594 0.7806 -0.0649 0.0319  -0.0076 54  SER B O   
2932 C CB  . SER B 54  ? 0.5157 0.4403 0.5891 -0.0880 0.0281  -0.0187 54  SER B CB  
2933 O OG  . SER B 54  ? 0.5964 0.5182 0.6789 -0.1036 0.0303  -0.0159 54  SER B OG  
2934 N N   . VAL B 55  ? 0.4938 0.3997 0.5435 -0.0585 0.0224  -0.0198 55  VAL B N   
2935 C CA  . VAL B 55  ? 0.4634 0.3756 0.5060 -0.0466 0.0224  -0.0222 55  VAL B CA  
2936 C C   . VAL B 55  ? 0.5238 0.4288 0.5587 -0.0421 0.0240  -0.0134 55  VAL B C   
2937 O O   . VAL B 55  ? 0.6214 0.5377 0.6518 -0.0375 0.0266  -0.0110 55  VAL B O   
2938 C CB  . VAL B 55  ? 0.4981 0.4033 0.5389 -0.0398 0.0179  -0.0321 55  VAL B CB  
2939 C CG1 . VAL B 55  ? 0.5228 0.4334 0.5555 -0.0294 0.0193  -0.0334 55  VAL B CG1 
2940 C CG2 . VAL B 55  ? 0.4010 0.3148 0.4472 -0.0438 0.0145  -0.0408 55  VAL B CG2 
2941 N N   . ILE B 56  ? 0.4869 0.3722 0.5206 -0.0431 0.0213  -0.0087 56  ILE B N   
2942 C CA  . ILE B 56  ? 0.4551 0.3328 0.4820 -0.0381 0.0205  -0.0002 56  ILE B CA  
2943 C C   . ILE B 56  ? 0.5434 0.4288 0.5641 -0.0452 0.0247  0.0100  56  ILE B C   
2944 O O   . ILE B 56  ? 0.5289 0.4197 0.5429 -0.0403 0.0253  0.0144  56  ILE B O   
2945 C CB  . ILE B 56  ? 0.4929 0.3452 0.5206 -0.0364 0.0146  0.0021  56  ILE B CB  
2946 C CG1 . ILE B 56  ? 0.4432 0.2903 0.4766 -0.0278 0.0116  -0.0104 56  ILE B CG1 
2947 C CG2 . ILE B 56  ? 0.4510 0.2950 0.4725 -0.0311 0.0115  0.0119  56  ILE B CG2 
2948 C CD1 . ILE B 56  ? 0.4803 0.3021 0.5169 -0.0243 0.0052  -0.0110 56  ILE B CD1 
2949 N N   . GLU B 57  ? 0.5849 0.4724 0.6078 -0.0574 0.0280  0.0128  57  GLU B N   
2950 C CA  . GLU B 57  ? 0.6224 0.5181 0.6382 -0.0656 0.0337  0.0218  57  GLU B CA  
2951 C C   . GLU B 57  ? 0.5893 0.5095 0.6054 -0.0616 0.0386  0.0171  57  GLU B C   
2952 O O   . GLU B 57  ? 0.6306 0.5568 0.6371 -0.0621 0.0418  0.0228  57  GLU B O   
2953 C CB  . GLU B 57  ? 0.8016 0.6965 0.8219 -0.0810 0.0377  0.0246  57  GLU B CB  
2954 C CG  . GLU B 57  ? 1.0804 0.9469 1.0961 -0.0878 0.0333  0.0333  57  GLU B CG  
2955 C CD  . GLU B 57  ? 1.0699 0.9356 1.0941 -0.1040 0.0368  0.0335  57  GLU B CD  
2956 O OE1 . GLU B 57  ? 1.0958 0.9863 1.1298 -0.1099 0.0434  0.0275  57  GLU B OE1 
2957 O OE2 . GLU B 57  ? 1.0432 0.8833 1.0656 -0.1106 0.0323  0.0393  57  GLU B OE2 
2958 N N   . LYS B 58  ? 0.6664 0.5997 0.6923 -0.0576 0.0385  0.0066  58  LYS B N   
2959 C CA  . LYS B 58  ? 0.5413 0.4943 0.5680 -0.0527 0.0415  0.0020  58  LYS B CA  
2960 C C   . LYS B 58  ? 0.6101 0.5607 0.6288 -0.0421 0.0389  0.0026  58  LYS B C   
2961 O O   . LYS B 58  ? 0.6161 0.5796 0.6335 -0.0383 0.0409  -0.0001 58  LYS B O   
2962 C CB  . LYS B 58  ? 0.5000 0.4651 0.5384 -0.0511 0.0400  -0.0083 58  LYS B CB  
2963 C CG  . LYS B 58  ? 0.5093 0.4824 0.5597 -0.0619 0.0424  -0.0108 58  LYS B CG  
2964 C CD  . LYS B 58  ? 0.4459 0.4312 0.4959 -0.0705 0.0508  -0.0060 58  LYS B CD  
2965 C CE  . LYS B 58  ? 0.5201 0.5147 0.5841 -0.0833 0.0544  -0.0082 58  LYS B CE  
2966 N NZ  . LYS B 58  ? 0.5993 0.6072 0.6619 -0.0934 0.0647  -0.0036 58  LYS B NZ  
2967 N N   . MET B 59  ? 0.7999 0.7350 0.8152 -0.0372 0.0344  0.0050  59  MET B N   
2968 C CA  . MET B 59  ? 0.6892 0.6238 0.6996 -0.0283 0.0322  0.0055  59  MET B CA  
2969 C C   . MET B 59  ? 0.7824 0.7093 0.7841 -0.0297 0.0308  0.0154  59  MET B C   
2970 O O   . MET B 59  ? 0.9955 0.9065 0.9962 -0.0282 0.0261  0.0198  59  MET B O   
2971 C CB  . MET B 59  ? 0.7292 0.6556 0.7437 -0.0212 0.0285  0.0001  59  MET B CB  
2972 C CG  . MET B 59  ? 0.6926 0.6257 0.7110 -0.0197 0.0291  -0.0090 59  MET B CG  
2973 S SD  . MET B 59  ? 0.7530 0.7030 0.7691 -0.0175 0.0314  -0.0117 59  MET B SD  
2974 C CE  . MET B 59  ? 0.8994 0.8497 0.9109 -0.0114 0.0313  -0.0086 59  MET B CE  
2975 N N   . ASN B 60  ? 0.7757 0.7131 0.7703 -0.0323 0.0342  0.0183  60  ASN B N   
2976 C CA  . ASN B 60  ? 0.8265 0.7573 0.8089 -0.0346 0.0324  0.0280  60  ASN B CA  
2977 C C   . ASN B 60  ? 0.9959 0.9217 0.9773 -0.0251 0.0256  0.0290  60  ASN B C   
2978 O O   . ASN B 60  ? 1.0489 0.9819 1.0377 -0.0181 0.0249  0.0219  60  ASN B O   
2979 C CB  . ASN B 60  ? 0.9433 0.8885 0.9173 -0.0396 0.0384  0.0286  60  ASN B CB  
2980 C CG  . ASN B 60  ? 1.0036 0.9574 0.9814 -0.0493 0.0460  0.0268  60  ASN B CG  
2981 O OD1 . ASN B 60  ? 1.1480 1.1189 1.1317 -0.0490 0.0509  0.0190  60  ASN B OD1 
2982 N ND2 . ASN B 60  ? 1.0640 1.0061 1.0398 -0.0579 0.0465  0.0336  60  ASN B ND2 
2983 N N   . THR B 61  ? 1.0050 0.9186 0.9771 -0.0255 0.0202  0.0385  61  THR B N   
2984 C CA  . THR B 61  ? 0.9218 0.8309 0.8960 -0.0162 0.0119  0.0395  61  THR B CA  
2985 C C   . THR B 61  ? 0.8331 0.7586 0.8068 -0.0122 0.0126  0.0348  61  THR B C   
2986 O O   . THR B 61  ? 0.9759 0.9091 0.9384 -0.0169 0.0155  0.0366  61  THR B O   
2987 C CB  . THR B 61  ? 0.9488 0.8411 0.9106 -0.0177 0.0043  0.0518  61  THR B CB  
2988 O OG1 . THR B 61  ? 1.1122 0.9852 1.0759 -0.0209 0.0022  0.0561  61  THR B OG1 
2989 C CG2 . THR B 61  ? 0.9274 0.8183 0.8936 -0.0070 -0.0057 0.0521  61  THR B CG2 
2990 N N   . GLN B 62  ? 0.6869 0.6178 0.6729 -0.0043 0.0105  0.0279  62  GLN B N   
2991 C CA  . GLN B 62  ? 0.6026 0.5471 0.5901 -0.0012 0.0099  0.0237  62  GLN B CA  
2992 C C   . GLN B 62  ? 0.6375 0.5792 0.6205 0.0024  0.0008  0.0294  62  GLN B C   
2993 O O   . GLN B 62  ? 0.7330 0.6684 0.7250 0.0089  -0.0061 0.0306  62  GLN B O   
2994 C CB  . GLN B 62  ? 0.6478 0.5995 0.6496 0.0040  0.0121  0.0148  62  GLN B CB  
2995 C CG  . GLN B 62  ? 0.7520 0.7160 0.7577 0.0064  0.0107  0.0110  62  GLN B CG  
2996 C CD  . GLN B 62  ? 0.8816 0.8532 0.8796 0.0017  0.0150  0.0086  62  GLN B CD  
2997 O OE1 . GLN B 62  ? 0.9826 0.9544 0.9789 -0.0012 0.0206  0.0059  62  GLN B OE1 
2998 N NE2 . GLN B 62  ? 0.9549 0.9324 0.9489 0.0015  0.0115  0.0087  62  GLN B NE2 
2999 N N   . PHE B 63  ? 0.5999 0.5469 0.5698 -0.0013 0.0000  0.0322  63  PHE B N   
3000 C CA  . PHE B 63  ? 0.6011 0.5460 0.5638 0.0015  -0.0101 0.0377  63  PHE B CA  
3001 C C   . PHE B 63  ? 0.6165 0.5756 0.5904 0.0062  -0.0133 0.0302  63  PHE B C   
3002 O O   . PHE B 63  ? 0.6939 0.6618 0.6810 0.0074  -0.0076 0.0220  63  PHE B O   
3003 C CB  . PHE B 63  ? 0.6254 0.5673 0.5646 -0.0061 -0.0095 0.0448  63  PHE B CB  
3004 C CG  . PHE B 63  ? 0.7357 0.6620 0.6635 -0.0120 -0.0078 0.0544  63  PHE B CG  
3005 C CD1 . PHE B 63  ? 0.7229 0.6320 0.6449 -0.0098 -0.0182 0.0648  63  PHE B CD1 
3006 C CD2 . PHE B 63  ? 0.6118 0.5406 0.5364 -0.0201 0.0034  0.0530  63  PHE B CD2 
3007 C CE1 . PHE B 63  ? 0.7207 0.6126 0.6314 -0.0167 -0.0169 0.0746  63  PHE B CE1 
3008 C CE2 . PHE B 63  ? 0.6234 0.5386 0.5390 -0.0275 0.0054  0.0619  63  PHE B CE2 
3009 C CZ  . PHE B 63  ? 0.6599 0.5554 0.5676 -0.0265 -0.0045 0.0731  63  PHE B CZ  
3010 N N   . THR B 64  ? 0.5648 0.5258 0.5325 0.0081  -0.0229 0.0333  64  THR B N   
3011 C CA  . THR B 64  ? 0.5068 0.4812 0.4887 0.0125  -0.0281 0.0266  64  THR B CA  
3012 C C   . THR B 64  ? 0.4719 0.4579 0.4552 0.0080  -0.0202 0.0180  64  THR B C   
3013 O O   . THR B 64  ? 0.5585 0.5446 0.5257 0.0027  -0.0167 0.0178  64  THR B O   
3014 C CB  . THR B 64  ? 0.5913 0.5652 0.5639 0.0146  -0.0415 0.0316  64  THR B CB  
3015 O OG1 . THR B 64  ? 0.6498 0.6105 0.6229 0.0202  -0.0510 0.0400  64  THR B OG1 
3016 C CG2 . THR B 64  ? 0.5991 0.5894 0.5888 0.0179  -0.0471 0.0236  64  THR B CG2 
3017 N N   . ALA B 65  ? 0.5671 0.5624 0.5694 0.0101  -0.0172 0.0107  65  ALA B N   
3018 C CA  . ALA B 65  ? 0.5841 0.5873 0.5886 0.0057  -0.0111 0.0035  65  ALA B CA  
3019 C C   . ALA B 65  ? 0.5234 0.5384 0.5485 0.0076  -0.0126 -0.0023 65  ALA B C   
3020 O O   . ALA B 65  ? 0.5774 0.5945 0.6155 0.0096  -0.0074 -0.0047 65  ALA B O   
3021 C CB  . ALA B 65  ? 0.6004 0.5989 0.6019 0.0029  -0.0006 0.0018  65  ALA B CB  
3022 N N   . VAL B 66  ? 0.4565 0.4803 0.4847 0.0062  -0.0191 -0.0053 66  VAL B N   
3023 C CA  . VAL B 66  ? 0.4821 0.5201 0.5321 0.0065  -0.0208 -0.0111 66  VAL B CA  
3024 C C   . VAL B 66  ? 0.4696 0.5113 0.5196 -0.0012 -0.0161 -0.0168 66  VAL B C   
3025 O O   . VAL B 66  ? 0.5192 0.5526 0.5529 -0.0049 -0.0139 -0.0169 66  VAL B O   
3026 C CB  . VAL B 66  ? 0.4956 0.5421 0.5542 0.0110  -0.0343 -0.0106 66  VAL B CB  
3027 C CG1 . VAL B 66  ? 0.5101 0.5480 0.5663 0.0190  -0.0406 -0.0037 66  VAL B CG1 
3028 C CG2 . VAL B 66  ? 0.5701 0.6159 0.6130 0.0071  -0.0419 -0.0108 66  VAL B CG2 
3029 N N   . GLY B 67  ? 0.4485 0.5027 0.5177 -0.0038 -0.0143 -0.0220 67  GLY B N   
3030 C CA  . GLY B 67  ? 0.4601 0.5162 0.5307 -0.0123 -0.0107 -0.0266 67  GLY B CA  
3031 C C   . GLY B 67  ? 0.5115 0.5695 0.5770 -0.0153 -0.0203 -0.0294 67  GLY B C   
3032 O O   . GLY B 67  ? 0.4952 0.5546 0.5552 -0.0108 -0.0301 -0.0275 67  GLY B O   
3033 N N   . LYS B 68  ? 0.5578 0.6143 0.6238 -0.0233 -0.0181 -0.0339 68  LYS B N   
3034 C CA  . LYS B 68  ? 0.5309 0.5880 0.5922 -0.0273 -0.0268 -0.0386 68  LYS B CA  
3035 C C   . LYS B 68  ? 0.4740 0.5406 0.5538 -0.0363 -0.0268 -0.0443 68  LYS B C   
3036 O O   . LYS B 68  ? 0.5295 0.5964 0.6183 -0.0414 -0.0174 -0.0438 68  LYS B O   
3037 C CB  . LYS B 68  ? 0.5894 0.6301 0.6285 -0.0285 -0.0250 -0.0398 68  LYS B CB  
3038 C CG  . LYS B 68  ? 0.5284 0.5616 0.5496 -0.0217 -0.0234 -0.0348 68  LYS B CG  
3039 C CD  . LYS B 68  ? 0.5536 0.5751 0.5564 -0.0226 -0.0212 -0.0384 68  LYS B CD  
3040 C CE  . LYS B 68  ? 0.5768 0.5941 0.5634 -0.0176 -0.0184 -0.0337 68  LYS B CE  
3041 N NZ  . LYS B 68  ? 0.9614 0.9715 0.9325 -0.0181 -0.0156 -0.0392 68  LYS B NZ  
3042 N N   . GLU B 69  ? 0.3652 0.4393 0.4495 -0.0393 -0.0374 -0.0495 69  GLU B N   
3043 C CA  . GLU B 69  ? 0.3688 0.4526 0.4717 -0.0495 -0.0388 -0.0556 69  GLU B CA  
3044 C C   . GLU B 69  ? 0.3806 0.4484 0.4700 -0.0570 -0.0402 -0.0603 69  GLU B C   
3045 O O   . GLU B 69  ? 0.3883 0.4441 0.4568 -0.0529 -0.0444 -0.0616 69  GLU B O   
3046 C CB  . GLU B 69  ? 0.5007 0.6054 0.6218 -0.0483 -0.0513 -0.0599 69  GLU B CB  
3047 C CG  . GLU B 69  ? 0.6703 0.7921 0.8105 -0.0402 -0.0512 -0.0571 69  GLU B CG  
3048 C CD  . GLU B 69  ? 0.8270 0.9607 0.9898 -0.0459 -0.0387 -0.0584 69  GLU B CD  
3049 O OE1 . GLU B 69  ? 1.0091 1.1455 1.1807 -0.0583 -0.0343 -0.0624 69  GLU B OE1 
3050 O OE2 . GLU B 69  ? 0.8543 0.9941 1.0251 -0.0386 -0.0330 -0.0557 69  GLU B OE2 
3051 N N   . PHE B 70  ? 0.4403 0.5076 0.5420 -0.0683 -0.0362 -0.0632 70  PHE B N   
3052 C CA  . PHE B 70  ? 0.3985 0.4479 0.4903 -0.0763 -0.0379 -0.0679 70  PHE B CA  
3053 C C   . PHE B 70  ? 0.4066 0.4658 0.5198 -0.0899 -0.0405 -0.0730 70  PHE B C   
3054 O O   . PHE B 70  ? 0.4868 0.5602 0.6194 -0.0958 -0.0334 -0.0706 70  PHE B O   
3055 C CB  . PHE B 70  ? 0.3987 0.4262 0.4768 -0.0771 -0.0278 -0.0630 70  PHE B CB  
3056 C CG  . PHE B 70  ? 0.4111 0.4320 0.4727 -0.0651 -0.0239 -0.0579 70  PHE B CG  
3057 C CD1 . PHE B 70  ? 0.4396 0.4478 0.4821 -0.0589 -0.0274 -0.0611 70  PHE B CD1 
3058 C CD2 . PHE B 70  ? 0.3755 0.4039 0.4415 -0.0605 -0.0162 -0.0511 70  PHE B CD2 
3059 C CE1 . PHE B 70  ? 0.4107 0.4150 0.4402 -0.0495 -0.0231 -0.0568 70  PHE B CE1 
3060 C CE2 . PHE B 70  ? 0.3751 0.3971 0.4272 -0.0508 -0.0130 -0.0468 70  PHE B CE2 
3061 C CZ  . PHE B 70  ? 0.3909 0.4015 0.4254 -0.0459 -0.0163 -0.0493 70  PHE B CZ  
3062 N N   . ASN B 71  ? 0.5191 0.5715 0.6289 -0.0954 -0.0501 -0.0810 71  ASN B N   
3063 C CA  . ASN B 71  ? 0.5730 0.6344 0.7040 -0.1099 -0.0536 -0.0867 71  ASN B CA  
3064 C C   . ASN B 71  ? 0.6027 0.6441 0.7322 -0.1222 -0.0444 -0.0836 71  ASN B C   
3065 O O   . ASN B 71  ? 0.5869 0.6085 0.6994 -0.1182 -0.0366 -0.0772 71  ASN B O   
3066 C CB  . ASN B 71  ? 0.5736 0.6350 0.7018 -0.1118 -0.0686 -0.0973 71  ASN B CB  
3067 C CG  . ASN B 71  ? 0.5686 0.6019 0.6701 -0.1087 -0.0713 -0.1015 71  ASN B CG  
3068 O OD1 . ASN B 71  ? 0.5545 0.5671 0.6530 -0.1174 -0.0690 -0.1036 71  ASN B OD1 
3069 N ND2 . ASN B 71  ? 0.8722 0.9043 0.9539 -0.0964 -0.0761 -0.1029 71  ASN B ND2 
3070 N N   . LYS B 72  ? 0.7480 0.7943 0.8956 -0.1379 -0.0462 -0.0879 72  LYS B N   
3071 C CA  . LYS B 72  ? 0.7172 0.7463 0.8653 -0.1524 -0.0371 -0.0831 72  LYS B CA  
3072 C C   . LYS B 72  ? 0.6168 0.6080 0.7405 -0.1520 -0.0398 -0.0831 72  LYS B C   
3073 O O   . LYS B 72  ? 0.6183 0.5888 0.7352 -0.1602 -0.0324 -0.0760 72  LYS B O   
3074 C CB  . LYS B 72  ? 0.8199 0.8639 0.9942 -0.1709 -0.0389 -0.0882 72  LYS B CB  
3075 C CG  . LYS B 72  ? 0.9045 0.9891 1.1081 -0.1710 -0.0370 -0.0902 72  LYS B CG  
3076 C CD  . LYS B 72  ? 1.1304 1.2326 1.3629 -0.1898 -0.0398 -0.0971 72  LYS B CD  
3077 C CE  . LYS B 72  ? 1.1004 1.2462 1.3660 -0.1879 -0.0391 -0.1010 72  LYS B CE  
3078 N NZ  . LYS B 72  ? 1.0897 1.2572 1.3875 -0.2068 -0.0419 -0.1090 72  LYS B NZ  
3079 N N   . LEU B 73  ? 0.4909 0.4725 0.6010 -0.1426 -0.0503 -0.0912 73  LEU B N   
3080 C CA  . LEU B 73  ? 0.5090 0.4566 0.5985 -0.1400 -0.0535 -0.0939 73  LEU B CA  
3081 C C   . LEU B 73  ? 0.4974 0.4368 0.5665 -0.1225 -0.0501 -0.0908 73  LEU B C   
3082 O O   . LEU B 73  ? 0.7069 0.6253 0.7605 -0.1159 -0.0546 -0.0968 73  LEU B O   
3083 C CB  . LEU B 73  ? 0.5282 0.4692 0.6167 -0.1429 -0.0668 -0.1079 73  LEU B CB  
3084 C CG  . LEU B 73  ? 0.5549 0.4917 0.6603 -0.1624 -0.0716 -0.1126 73  LEU B CG  
3085 C CD1 . LEU B 73  ? 0.5869 0.5170 0.6889 -0.1634 -0.0860 -0.1282 73  LEU B CD1 
3086 C CD2 . LEU B 73  ? 0.5671 0.4734 0.6678 -0.1731 -0.0653 -0.1048 73  LEU B CD2 
3087 N N   . GLU B 74  ? 0.4751 0.4313 0.5455 -0.1150 -0.0422 -0.0825 74  GLU B N   
3088 C CA  . GLU B 74  ? 0.4634 0.4146 0.5171 -0.1000 -0.0384 -0.0789 74  GLU B CA  
3089 C C   . GLU B 74  ? 0.4526 0.4019 0.5056 -0.0994 -0.0272 -0.0673 74  GLU B C   
3090 O O   . GLU B 74  ? 0.4699 0.4309 0.5201 -0.0899 -0.0224 -0.0626 74  GLU B O   
3091 C CB  . GLU B 74  ? 0.4495 0.4222 0.5015 -0.0895 -0.0421 -0.0816 74  GLU B CB  
3092 C CG  . GLU B 74  ? 0.4690 0.4405 0.5133 -0.0877 -0.0531 -0.0933 74  GLU B CG  
3093 C CD  . GLU B 74  ? 0.4864 0.4786 0.5271 -0.0794 -0.0578 -0.0940 74  GLU B CD  
3094 O OE1 . GLU B 74  ? 0.4818 0.4928 0.5348 -0.0782 -0.0555 -0.0872 74  GLU B OE1 
3095 O OE2 . GLU B 74  ? 0.5185 0.5075 0.5432 -0.0739 -0.0639 -0.1015 74  GLU B OE2 
3096 N N   . ARG B 75  ? 0.4664 0.3992 0.5202 -0.1104 -0.0234 -0.0623 75  ARG B N   
3097 C CA  . ARG B 75  ? 0.4606 0.3911 0.5111 -0.1116 -0.0130 -0.0513 75  ARG B CA  
3098 C C   . ARG B 75  ? 0.4594 0.3716 0.4914 -0.0993 -0.0123 -0.0480 75  ARG B C   
3099 O O   . ARG B 75  ? 0.4466 0.3646 0.4745 -0.0938 -0.0053 -0.0412 75  ARG B O   
3100 C CB  . ARG B 75  ? 0.4807 0.3983 0.5346 -0.1288 -0.0093 -0.0460 75  ARG B CB  
3101 C CG  . ARG B 75  ? 0.5419 0.4620 0.5923 -0.1328 0.0025  -0.0351 75  ARG B CG  
3102 C CD  . ARG B 75  ? 0.7804 0.7359 0.8485 -0.1326 0.0097  -0.0357 75  ARG B CD  
3103 N NE  . ARG B 75  ? 0.9812 0.9410 1.0463 -0.1377 0.0221  -0.0272 75  ARG B NE  
3104 C CZ  . ARG B 75  ? 1.1061 1.0686 1.1773 -0.1547 0.0301  -0.0232 75  ARG B CZ  
3105 N NH1 . ARG B 75  ? 1.1806 1.1477 1.2457 -0.1586 0.0421  -0.0163 75  ARG B NH1 
3106 N NH2 . ARG B 75  ? 0.8435 0.8042 0.9261 -0.1689 0.0266  -0.0266 75  ARG B NH2 
3107 N N   . ARG B 76  ? 0.5233 0.4141 0.5455 -0.0946 -0.0197 -0.0539 76  ARG B N   
3108 C CA  . ARG B 76  ? 0.4726 0.3495 0.4812 -0.0819 -0.0198 -0.0528 76  ARG B CA  
3109 C C   . ARG B 76  ? 0.4495 0.3473 0.4569 -0.0694 -0.0172 -0.0546 76  ARG B C   
3110 O O   . ARG B 76  ? 0.4921 0.3900 0.4936 -0.0619 -0.0126 -0.0493 76  ARG B O   
3111 C CB  . ARG B 76  ? 0.4939 0.3465 0.4957 -0.0784 -0.0285 -0.0616 76  ARG B CB  
3112 C CG  . ARG B 76  ? 0.6564 0.4797 0.6558 -0.0892 -0.0322 -0.0579 76  ARG B CG  
3113 C CD  . ARG B 76  ? 0.5446 0.3448 0.5404 -0.0854 -0.0423 -0.0693 76  ARG B CD  
3114 N NE  . ARG B 76  ? 0.5433 0.3578 0.5458 -0.0874 -0.0465 -0.0815 76  ARG B NE  
3115 C CZ  . ARG B 76  ? 0.5538 0.3613 0.5524 -0.0793 -0.0533 -0.0954 76  ARG B CZ  
3116 N NH1 . ARG B 76  ? 0.5648 0.3529 0.5560 -0.0679 -0.0561 -0.0996 76  ARG B NH1 
3117 N NH2 . ARG B 76  ? 0.5545 0.3759 0.5569 -0.0822 -0.0575 -0.1059 76  ARG B NH2 
3118 N N   . MET B 77  ? 0.4434 0.3579 0.4553 -0.0676 -0.0207 -0.0618 77  MET B N   
3119 C CA  . MET B 77  ? 0.4262 0.3580 0.4346 -0.0572 -0.0187 -0.0622 77  MET B CA  
3120 C C   . MET B 77  ? 0.4083 0.3574 0.4242 -0.0577 -0.0121 -0.0535 77  MET B C   
3121 O O   . MET B 77  ? 0.4669 0.4220 0.4781 -0.0495 -0.0081 -0.0499 77  MET B O   
3122 C CB  . MET B 77  ? 0.5222 0.4650 0.5299 -0.0560 -0.0254 -0.0712 77  MET B CB  
3123 C CG  . MET B 77  ? 0.6376 0.5912 0.6353 -0.0456 -0.0242 -0.0722 77  MET B CG  
3124 S SD  . MET B 77  ? 0.8111 0.7800 0.8050 -0.0457 -0.0325 -0.0795 77  MET B SD  
3125 C CE  . MET B 77  ? 1.1088 1.0612 1.0986 -0.0502 -0.0400 -0.0932 77  MET B CE  
3126 N N   . GLU B 78  ? 0.4084 0.3663 0.4372 -0.0674 -0.0107 -0.0510 78  GLU B N   
3127 C CA  . GLU B 78  ? 0.3940 0.3679 0.4315 -0.0676 -0.0036 -0.0445 78  GLU B CA  
3128 C C   . GLU B 78  ? 0.4556 0.4180 0.4841 -0.0655 0.0037  -0.0373 78  GLU B C   
3129 O O   . GLU B 78  ? 0.4075 0.3785 0.4351 -0.0589 0.0083  -0.0337 78  GLU B O   
3130 C CB  . GLU B 78  ? 0.3973 0.3838 0.4521 -0.0794 -0.0022 -0.0448 78  GLU B CB  
3131 C CG  . GLU B 78  ? 0.4369 0.4432 0.5037 -0.0789 0.0055  -0.0407 78  GLU B CG  
3132 C CD  . GLU B 78  ? 0.5472 0.5691 0.6339 -0.0912 0.0085  -0.0423 78  GLU B CD  
3133 O OE1 . GLU B 78  ? 0.7362 0.7705 0.8313 -0.0935 0.0178  -0.0392 78  GLU B OE1 
3134 O OE2 . GLU B 78  ? 0.6657 0.6887 0.7603 -0.0989 0.0020  -0.0475 78  GLU B OE2 
3135 N N   . ASN B 79  ? 0.4081 0.3494 0.4290 -0.0712 0.0037  -0.0352 79  ASN B N   
3136 C CA  . ASN B 79  ? 0.4105 0.3392 0.4206 -0.0695 0.0085  -0.0280 79  ASN B CA  
3137 C C   . ASN B 79  ? 0.4037 0.3268 0.4042 -0.0565 0.0064  -0.0293 79  ASN B C   
3138 O O   . ASN B 79  ? 0.4847 0.4063 0.4793 -0.0524 0.0103  -0.0243 79  ASN B O   
3139 C CB  . ASN B 79  ? 0.4342 0.3389 0.4370 -0.0792 0.0071  -0.0243 79  ASN B CB  
3140 C CG  . ASN B 79  ? 0.4420 0.3535 0.4530 -0.0942 0.0129  -0.0205 79  ASN B CG  
3141 O OD1 . ASN B 79  ? 0.4588 0.3924 0.4792 -0.0959 0.0203  -0.0193 79  ASN B OD1 
3142 N ND2 . ASN B 79  ? 0.4651 0.3578 0.4736 -0.1056 0.0099  -0.0192 79  ASN B ND2 
3143 N N   . LEU B 80  ? 0.4050 0.3262 0.4040 -0.0505 0.0005  -0.0367 80  LEU B N   
3144 C CA  . LEU B 80  ? 0.3980 0.3191 0.3906 -0.0391 0.0000  -0.0390 80  LEU B CA  
3145 C C   . LEU B 80  ? 0.3794 0.3202 0.3749 -0.0343 0.0044  -0.0368 80  LEU B C   
3146 O O   . LEU B 80  ? 0.3945 0.3362 0.3864 -0.0285 0.0075  -0.0340 80  LEU B O   
3147 C CB  . LEU B 80  ? 0.4070 0.3230 0.3969 -0.0348 -0.0059 -0.0489 80  LEU B CB  
3148 C CG  . LEU B 80  ? 0.4017 0.3215 0.3867 -0.0240 -0.0050 -0.0535 80  LEU B CG  
3149 C CD1 . LEU B 80  ? 0.4040 0.3118 0.3864 -0.0188 -0.0045 -0.0504 80  LEU B CD1 
3150 C CD2 . LEU B 80  ? 0.4135 0.3305 0.3954 -0.0209 -0.0096 -0.0651 80  LEU B CD2 
3151 N N   . ASN B 81  ? 0.3740 0.3297 0.3764 -0.0368 0.0035  -0.0382 81  ASN B N   
3152 C CA  . ASN B 81  ? 0.4886 0.4602 0.4944 -0.0326 0.0062  -0.0351 81  ASN B CA  
3153 C C   . ASN B 81  ? 0.3528 0.3263 0.3618 -0.0333 0.0126  -0.0289 81  ASN B C   
3154 O O   . ASN B 81  ? 0.3569 0.3333 0.3632 -0.0276 0.0155  -0.0262 81  ASN B O   
3155 C CB  . ASN B 81  ? 0.3595 0.3451 0.3740 -0.0354 0.0020  -0.0374 81  ASN B CB  
3156 C CG  . ASN B 81  ? 0.3503 0.3487 0.3663 -0.0295 0.0018  -0.0345 81  ASN B CG  
3157 O OD1 . ASN B 81  ? 0.3600 0.3577 0.3660 -0.0243 0.0004  -0.0348 81  ASN B OD1 
3158 N ND2 . ASN B 81  ? 0.4534 0.4634 0.4822 -0.0306 0.0031  -0.0320 81  ASN B ND2 
3159 N N   . LYS B 82  ? 0.5169 0.4885 0.5307 -0.0412 0.0153  -0.0269 82  LYS B N   
3160 C CA  . LYS B 82  ? 0.3998 0.3724 0.4137 -0.0432 0.0223  -0.0220 82  LYS B CA  
3161 C C   . LYS B 82  ? 0.4114 0.3701 0.4125 -0.0385 0.0231  -0.0191 82  LYS B C   
3162 O O   . LYS B 82  ? 0.3679 0.3304 0.3672 -0.0348 0.0271  -0.0167 82  LYS B O   
3168 N N   . LYS B 83  ? 0.3691 0.3116 0.3623 -0.0382 0.0185  -0.0201 83  LYS B N   
3169 C CA  . LYS B 83  ? 0.3730 0.3030 0.3564 -0.0330 0.0173  -0.0180 83  LYS B CA  
3170 C C   . LYS B 83  ? 0.3597 0.2987 0.3442 -0.0240 0.0176  -0.0202 83  LYS B C   
3171 O O   . LYS B 83  ? 0.3748 0.3125 0.3556 -0.0206 0.0192  -0.0178 83  LYS B O   
3172 C CB  . LYS B 83  ? 0.3891 0.3001 0.3670 -0.0327 0.0106  -0.0202 83  LYS B CB  
3173 C CG  . LYS B 83  ? 0.3951 0.2937 0.3655 -0.0258 0.0071  -0.0190 83  LYS B CG  
3174 C CD  . LYS B 83  ? 0.4163 0.2923 0.3817 -0.0259 -0.0005 -0.0200 83  LYS B CD  
3175 C CE  . LYS B 83  ? 0.4345 0.3110 0.4059 -0.0223 -0.0045 -0.0295 83  LYS B CE  
3176 N NZ  . LYS B 83  ? 0.4411 0.2932 0.4088 -0.0212 -0.0128 -0.0318 83  LYS B NZ  
3177 N N   . VAL B 84  ? 0.3536 0.3018 0.3423 -0.0210 0.0161  -0.0246 84  VAL B N   
3178 C CA  . VAL B 84  ? 0.3440 0.3008 0.3328 -0.0147 0.0173  -0.0258 84  VAL B CA  
3179 C C   . VAL B 84  ? 0.3344 0.3000 0.3264 -0.0145 0.0215  -0.0215 84  VAL B C   
3180 O O   . VAL B 84  ? 0.3303 0.2958 0.3207 -0.0113 0.0234  -0.0200 84  VAL B O   
3181 C CB  . VAL B 84  ? 0.3445 0.3082 0.3331 -0.0132 0.0151  -0.0306 84  VAL B CB  
3182 C CG1 . VAL B 84  ? 0.3376 0.3103 0.3246 -0.0092 0.0177  -0.0298 84  VAL B CG1 
3183 C CG2 . VAL B 84  ? 0.3555 0.3102 0.3409 -0.0117 0.0114  -0.0372 84  VAL B CG2 
3184 N N   . ASP B 85  ? 0.3320 0.3056 0.3303 -0.0177 0.0225  -0.0204 85  ASP B N   
3185 C CA  . ASP B 85  ? 0.3249 0.3066 0.3284 -0.0162 0.0258  -0.0179 85  ASP B CA  
3186 C C   . ASP B 85  ? 0.3260 0.3026 0.3262 -0.0170 0.0300  -0.0159 85  ASP B C   
3187 O O   . ASP B 85  ? 0.3221 0.2991 0.3212 -0.0135 0.0316  -0.0152 85  ASP B O   
3188 C CB  . ASP B 85  ? 0.3239 0.3163 0.3380 -0.0189 0.0254  -0.0186 85  ASP B CB  
3189 C CG  . ASP B 85  ? 0.3571 0.3554 0.3730 -0.0170 0.0196  -0.0200 85  ASP B CG  
3190 O OD1 . ASP B 85  ? 0.3874 0.3829 0.3954 -0.0136 0.0178  -0.0196 85  ASP B OD1 
3191 O OD2 . ASP B 85  ? 0.4344 0.4411 0.4592 -0.0196 0.0168  -0.0217 85  ASP B OD2 
3192 N N   . ASP B 86  ? 0.3343 0.3048 0.3311 -0.0225 0.0316  -0.0150 86  ASP B N   
3193 C CA  . ASP B 86  ? 0.3399 0.3048 0.3294 -0.0243 0.0353  -0.0127 86  ASP B CA  
3194 C C   . ASP B 86  ? 0.4471 0.4026 0.4282 -0.0195 0.0321  -0.0121 86  ASP B C   
3195 O O   . ASP B 86  ? 0.3414 0.2965 0.3185 -0.0179 0.0340  -0.0116 86  ASP B O   
3196 C CB  . ASP B 86  ? 0.3535 0.3110 0.3376 -0.0327 0.0371  -0.0103 86  ASP B CB  
3197 C CG  . ASP B 86  ? 0.5252 0.4961 0.5197 -0.0388 0.0429  -0.0114 86  ASP B CG  
3198 O OD1 . ASP B 86  ? 0.3738 0.3590 0.3797 -0.0347 0.0450  -0.0144 86  ASP B OD1 
3199 O OD2 . ASP B 86  ? 0.4707 0.4378 0.4631 -0.0477 0.0452  -0.0095 86  ASP B OD2 
3200 N N   . GLY B 87  ? 0.3434 0.2925 0.3228 -0.0169 0.0269  -0.0135 87  GLY B N   
3201 C CA  . GLY B 87  ? 0.3447 0.2882 0.3202 -0.0118 0.0233  -0.0143 87  GLY B CA  
3202 C C   . GLY B 87  ? 0.3338 0.2869 0.3143 -0.0078 0.0251  -0.0157 87  GLY B C   
3203 O O   . GLY B 87  ? 0.3346 0.2860 0.3125 -0.0061 0.0247  -0.0155 87  GLY B O   
3204 N N   . PHE B 88  ? 0.3260 0.2882 0.3128 -0.0070 0.0266  -0.0169 88  PHE B N   
3205 C CA  . PHE B 88  ? 0.3194 0.2881 0.3097 -0.0048 0.0282  -0.0169 88  PHE B CA  
3206 C C   . PHE B 88  ? 0.3183 0.2874 0.3093 -0.0054 0.0310  -0.0154 88  PHE B C   
3207 O O   . PHE B 88  ? 0.4189 0.3876 0.4103 -0.0041 0.0312  -0.0159 88  PHE B O   
3208 C CB  . PHE B 88  ? 0.3165 0.2921 0.3096 -0.0047 0.0284  -0.0168 88  PHE B CB  
3209 C CG  . PHE B 88  ? 0.3189 0.2961 0.3102 -0.0035 0.0271  -0.0202 88  PHE B CG  
3210 C CD1 . PHE B 88  ? 0.3202 0.2963 0.3122 -0.0011 0.0265  -0.0235 88  PHE B CD1 
3211 C CD2 . PHE B 88  ? 0.4115 0.3924 0.4009 -0.0044 0.0261  -0.0213 88  PHE B CD2 
3212 C CE1 . PHE B 88  ? 0.3752 0.3550 0.3676 0.0009  0.0262  -0.0286 88  PHE B CE1 
3213 C CE2 . PHE B 88  ? 0.3636 0.3468 0.3502 -0.0032 0.0258  -0.0261 88  PHE B CE2 
3214 C CZ  . PHE B 88  ? 0.3336 0.3168 0.3225 -0.0004 0.0265  -0.0302 88  PHE B CZ  
3215 N N   . ILE B 89  ? 0.3197 0.2904 0.3120 -0.0077 0.0333  -0.0147 89  ILE B N   
3216 C CA  . ILE B 89  ? 0.3207 0.2930 0.3143 -0.0077 0.0368  -0.0154 89  ILE B CA  
3217 C C   . ILE B 89  ? 0.3276 0.2928 0.3118 -0.0084 0.0370  -0.0159 89  ILE B C   
3218 O O   . ILE B 89  ? 0.4880 0.4527 0.4717 -0.0068 0.0378  -0.0178 89  ILE B O   
3219 C CB  . ILE B 89  ? 0.3220 0.3008 0.3209 -0.0103 0.0403  -0.0161 89  ILE B CB  
3220 C CG1 . ILE B 89  ? 0.3165 0.3033 0.3261 -0.0080 0.0383  -0.0161 89  ILE B CG1 
3221 C CG2 . ILE B 89  ? 0.3331 0.3141 0.3318 -0.0104 0.0455  -0.0187 89  ILE B CG2 
3222 C CD1 . ILE B 89  ? 0.3171 0.3137 0.3364 -0.0104 0.0406  -0.0179 89  ILE B CD1 
3223 N N   . ASP B 90  ? 0.3352 0.2933 0.3109 -0.0108 0.0350  -0.0143 90  ASP B N   
3224 C CA  . ASP B 90  ? 0.3456 0.2953 0.3098 -0.0113 0.0330  -0.0138 90  ASP B CA  
3225 C C   . ASP B 90  ? 0.3422 0.2916 0.3086 -0.0070 0.0284  -0.0158 90  ASP B C   
3226 O O   . ASP B 90  ? 0.5157 0.4632 0.4773 -0.0066 0.0276  -0.0174 90  ASP B O   
3227 C CB  . ASP B 90  ? 0.3578 0.2967 0.3121 -0.0141 0.0296  -0.0103 90  ASP B CB  
3228 C CG  . ASP B 90  ? 0.5044 0.4429 0.4547 -0.0211 0.0350  -0.0079 90  ASP B CG  
3229 O OD1 . ASP B 90  ? 0.5002 0.4478 0.4538 -0.0231 0.0419  -0.0098 90  ASP B OD1 
3230 O OD2 . ASP B 90  ? 0.6833 0.6124 0.6283 -0.0247 0.0324  -0.0046 90  ASP B OD2 
3231 N N   . ILE B 91  ? 0.3643 0.3168 0.3384 -0.0044 0.0256  -0.0165 91  ILE B N   
3232 C CA  . ILE B 91  ? 0.3323 0.2878 0.3115 -0.0015 0.0223  -0.0191 91  ILE B CA  
3233 C C   . ILE B 91  ? 0.3275 0.2878 0.3119 -0.0022 0.0254  -0.0204 91  ILE B C   
3234 O O   . ILE B 91  ? 0.3304 0.2902 0.3150 -0.0019 0.0230  -0.0227 91  ILE B O   
3235 C CB  . ILE B 91  ? 0.3274 0.2878 0.3142 0.0008  0.0209  -0.0209 91  ILE B CB  
3236 C CG1 . ILE B 91  ? 0.3835 0.3357 0.3659 0.0029  0.0156  -0.0211 91  ILE B CG1 
3237 C CG2 . ILE B 91  ? 0.3233 0.2917 0.3189 0.0022  0.0201  -0.0241 91  ILE B CG2 
3238 C CD1 . ILE B 91  ? 0.5108 0.4676 0.5004 0.0059  0.0147  -0.0248 91  ILE B CD1 
3239 N N   . TRP B 92  ? 0.3633 0.3270 0.3520 -0.0030 0.0294  -0.0191 92  TRP B N   
3240 C CA  . TRP B 92  ? 0.4276 0.3922 0.4211 -0.0033 0.0311  -0.0198 92  TRP B CA  
3241 C C   . TRP B 92  ? 0.3282 0.2885 0.3172 -0.0033 0.0321  -0.0226 92  TRP B C   
3242 O O   . TRP B 92  ? 0.3313 0.2894 0.3224 -0.0034 0.0311  -0.0252 92  TRP B O   
3243 C CB  . TRP B 92  ? 0.3182 0.2855 0.3166 -0.0030 0.0331  -0.0171 92  TRP B CB  
3244 C CG  . TRP B 92  ? 0.3200 0.2912 0.3206 -0.0039 0.0325  -0.0149 92  TRP B CG  
3245 C CD1 . TRP B 92  ? 0.3631 0.3379 0.3625 -0.0039 0.0324  -0.0136 92  TRP B CD1 
3246 C CD2 . TRP B 92  ? 0.4926 0.4656 0.4961 -0.0060 0.0327  -0.0147 92  TRP B CD2 
3247 N NE1 . TRP B 92  ? 0.3980 0.3768 0.3977 -0.0054 0.0331  -0.0128 92  TRP B NE1 
3248 C CE2 . TRP B 92  ? 0.3961 0.3745 0.3988 -0.0072 0.0338  -0.0131 92  TRP B CE2 
3249 C CE3 . TRP B 92  ? 0.3195 0.2906 0.3264 -0.0080 0.0323  -0.0163 92  TRP B CE3 
3250 C CZ2 . TRP B 92  ? 0.4256 0.4089 0.4305 -0.0107 0.0360  -0.0127 92  TRP B CZ2 
3251 C CZ3 . TRP B 92  ? 0.4056 0.3811 0.4167 -0.0118 0.0336  -0.0156 92  TRP B CZ3 
3252 C CH2 . TRP B 92  ? 0.3820 0.3642 0.3919 -0.0134 0.0362  -0.0136 92  TRP B CH2 
3253 N N   . THR B 93  ? 0.3325 0.2918 0.3148 -0.0039 0.0344  -0.0227 93  THR B N   
3254 C CA  . THR B 93  ? 0.3420 0.2985 0.3170 -0.0045 0.0366  -0.0264 93  THR B CA  
3255 C C   . THR B 93  ? 0.3499 0.3011 0.3162 -0.0050 0.0316  -0.0282 93  THR B C   
3256 O O   . THR B 93  ? 0.3556 0.3047 0.3208 -0.0047 0.0308  -0.0328 93  THR B O   
3257 C CB  . THR B 93  ? 0.3476 0.3055 0.3157 -0.0071 0.0413  -0.0254 93  THR B CB  
3258 O OG1 . THR B 93  ? 0.4144 0.3796 0.3936 -0.0065 0.0448  -0.0249 93  THR B OG1 
3259 C CG2 . THR B 93  ? 0.3604 0.3169 0.3184 -0.0085 0.0453  -0.0300 93  THR B CG2 
3260 N N   . TYR B 94  ? 0.3520 0.3005 0.3130 -0.0052 0.0269  -0.0253 94  TYR B N   
3261 C CA  . TYR B 94  ? 0.3604 0.3048 0.3151 -0.0044 0.0197  -0.0268 94  TYR B CA  
3262 C C   . TYR B 94  ? 0.3548 0.3037 0.3214 -0.0036 0.0170  -0.0307 94  TYR B C   
3263 O O   . TYR B 94  ? 0.4259 0.3726 0.3887 -0.0042 0.0135  -0.0349 94  TYR B O   
3264 C CB  . TYR B 94  ? 0.3629 0.3039 0.3150 -0.0029 0.0139  -0.0233 94  TYR B CB  
3265 C CG  . TYR B 94  ? 0.3707 0.3094 0.3212 -0.0003 0.0042  -0.0251 94  TYR B CG  
3266 C CD1 . TYR B 94  ? 0.3893 0.3184 0.3221 -0.0009 -0.0015 -0.0239 94  TYR B CD1 
3267 C CD2 . TYR B 94  ? 0.3773 0.3245 0.3440 0.0024  0.0005  -0.0282 94  TYR B CD2 
3268 C CE1 . TYR B 94  ? 0.3982 0.3256 0.3302 0.0024  -0.0126 -0.0257 94  TYR B CE1 
3269 C CE2 . TYR B 94  ? 0.3685 0.3167 0.3376 0.0054  -0.0091 -0.0311 94  TYR B CE2 
3270 C CZ  . TYR B 94  ? 0.3955 0.3334 0.3478 0.0059  -0.0167 -0.0298 94  TYR B CZ  
3271 O OH  . TYR B 94  ? 0.4194 0.3585 0.3748 0.0097  -0.0284 -0.0328 94  TYR B OH  
3272 N N   . ASN B 95  ? 0.3430 0.2981 0.3230 -0.0033 0.0188  -0.0294 95  ASN B N   
3273 C CA  . ASN B 95  ? 0.3395 0.2993 0.3311 -0.0047 0.0176  -0.0320 95  ASN B CA  
3274 C C   . ASN B 95  ? 0.3449 0.3000 0.3363 -0.0065 0.0193  -0.0351 95  ASN B C   
3275 O O   . ASN B 95  ? 0.6756 0.6299 0.6697 -0.0083 0.0155  -0.0394 95  ASN B O   
3276 C CB  . ASN B 95  ? 0.3299 0.2961 0.3315 -0.0056 0.0212  -0.0290 95  ASN B CB  
3277 C CG  . ASN B 95  ? 0.3719 0.3444 0.3771 -0.0035 0.0190  -0.0291 95  ASN B CG  
3278 O OD1 . ASN B 95  ? 0.3917 0.3623 0.3931 -0.0007 0.0135  -0.0306 95  ASN B OD1 
3279 N ND2 . ASN B 95  ? 0.4164 0.3956 0.4281 -0.0045 0.0228  -0.0276 95  ASN B ND2 
3280 N N   . ALA B 96  ? 0.4215 0.3735 0.4114 -0.0057 0.0244  -0.0339 96  ALA B N   
3281 C CA  . ALA B 96  ? 0.3514 0.2977 0.3432 -0.0058 0.0258  -0.0379 96  ALA B CA  
3282 C C   . ALA B 96  ? 0.4034 0.3455 0.3848 -0.0058 0.0237  -0.0445 96  ALA B C   
3283 O O   . ALA B 96  ? 0.4510 0.3890 0.4348 -0.0074 0.0204  -0.0497 96  ALA B O   
3284 C CB  . ALA B 96  ? 0.3496 0.2953 0.3437 -0.0031 0.0307  -0.0364 96  ALA B CB  
3285 N N   . GLU B 97  ? 0.3685 0.3109 0.3370 -0.0050 0.0252  -0.0445 97  GLU B N   
3286 C CA  . GLU B 97  ? 0.3843 0.3224 0.3384 -0.0056 0.0240  -0.0505 97  GLU B CA  
3287 C C   . GLU B 97  ? 0.3907 0.3272 0.3417 -0.0070 0.0149  -0.0528 97  GLU B C   
3288 O O   . GLU B 97  ? 0.6439 0.5764 0.5912 -0.0080 0.0118  -0.0600 97  GLU B O   
3289 C CB  . GLU B 97  ? 0.3913 0.3297 0.3299 -0.0064 0.0281  -0.0481 97  GLU B CB  
3290 C CG  . GLU B 97  ? 0.4629 0.4060 0.4069 -0.0054 0.0373  -0.0482 97  GLU B CG  
3291 C CD  . GLU B 97  ? 0.5987 0.5432 0.5273 -0.0084 0.0432  -0.0471 97  GLU B CD  
3292 O OE1 . GLU B 97  ? 0.7416 0.6807 0.6534 -0.0113 0.0392  -0.0436 97  GLU B OE1 
3293 O OE2 . GLU B 97  ? 0.6382 0.5894 0.5719 -0.0082 0.0515  -0.0497 97  GLU B OE2 
3294 N N   . LEU B 98  ? 0.3844 0.3244 0.3385 -0.0067 0.0098  -0.0478 98  LEU B N   
3295 C CA  . LEU B 98  ? 0.3904 0.3316 0.3451 -0.0070 -0.0001 -0.0505 98  LEU B CA  
3296 C C   . LEU B 98  ? 0.3932 0.3378 0.3643 -0.0096 -0.0019 -0.0554 98  LEU B C   
3297 O O   . LEU B 98  ? 0.5613 0.5044 0.5307 -0.0112 -0.0086 -0.0617 98  LEU B O   
3298 C CB  . LEU B 98  ? 0.4164 0.3619 0.3755 -0.0046 -0.0048 -0.0454 98  LEU B CB  
3299 C CG  . LEU B 98  ? 0.6185 0.5664 0.5790 -0.0031 -0.0168 -0.0482 98  LEU B CG  
3300 C CD1 . LEU B 98  ? 0.4954 0.4334 0.4320 -0.0028 -0.0232 -0.0488 98  LEU B CD1 
3301 C CD2 . LEU B 98  ? 0.6262 0.5800 0.5973 0.0008  -0.0205 -0.0449 98  LEU B CD2 
3302 N N   . LEU B 99  ? 0.3741 0.3223 0.3601 -0.0108 0.0035  -0.0523 99  LEU B N   
3303 C CA  . LEU B 99  ? 0.3738 0.3230 0.3743 -0.0153 0.0029  -0.0552 99  LEU B CA  
3304 C C   . LEU B 99  ? 0.5214 0.4604 0.5168 -0.0166 0.0023  -0.0621 99  LEU B C   
3305 O O   . LEU B 99  ? 0.5229 0.4609 0.5238 -0.0205 -0.0032 -0.0680 99  LEU B O   
3306 C CB  . LEU B 99  ? 0.3631 0.3144 0.3742 -0.0168 0.0096  -0.0490 99  LEU B CB  
3307 C CG  . LEU B 99  ? 0.4630 0.4127 0.4870 -0.0232 0.0102  -0.0493 99  LEU B CG  
3308 C CD1 . LEU B 99  ? 0.4348 0.3960 0.4709 -0.0277 0.0057  -0.0525 99  LEU B CD1 
3309 C CD2 . LEU B 99  ? 0.3604 0.3092 0.3886 -0.0246 0.0165  -0.0415 99  LEU B CD2 
3310 N N   . VAL B 100 ? 0.3911 0.3234 0.3773 -0.0134 0.0078  -0.0627 100 VAL B N   
3311 C CA  . VAL B 100 ? 0.4057 0.3282 0.3880 -0.0133 0.0080  -0.0711 100 VAL B CA  
3312 C C   . VAL B 100 ? 0.4454 0.3665 0.4141 -0.0141 0.0016  -0.0792 100 VAL B C   
3313 O O   . VAL B 100 ? 0.5559 0.4710 0.5265 -0.0167 -0.0028 -0.0874 100 VAL B O   
3314 C CB  . VAL B 100 ? 0.4066 0.3258 0.3845 -0.0086 0.0159  -0.0715 100 VAL B CB  
3315 C CG1 . VAL B 100 ? 0.4246 0.3356 0.3959 -0.0070 0.0164  -0.0830 100 VAL B CG1 
3316 C CG2 . VAL B 100 ? 0.3971 0.3146 0.3894 -0.0078 0.0192  -0.0652 100 VAL B CG2 
3317 N N   . LEU B 101 ? 0.4232 0.3482 0.3769 -0.0124 0.0000  -0.0767 101 LEU B N   
3318 C CA  . LEU B 101 ? 0.4516 0.3743 0.3890 -0.0133 -0.0080 -0.0827 101 LEU B CA  
3319 C C   . LEU B 101 ? 0.4805 0.4066 0.4305 -0.0167 -0.0185 -0.0865 101 LEU B C   
3320 O O   . LEU B 101 ? 0.6293 0.5506 0.5779 -0.0193 -0.0233 -0.0960 101 LEU B O   
3321 C CB  . LEU B 101 ? 0.4444 0.3689 0.3648 -0.0116 -0.0100 -0.0761 101 LEU B CB  
3322 C CG  . LEU B 101 ? 0.4666 0.3864 0.3627 -0.0111 -0.0035 -0.0763 101 LEU B CG  
3323 C CD1 . LEU B 101 ? 0.5052 0.4230 0.3834 -0.0111 -0.0093 -0.0687 101 LEU B CD1 
3324 C CD2 . LEU B 101 ? 0.5917 0.5061 0.4738 -0.0124 -0.0037 -0.0879 101 LEU B CD2 
3325 N N   . LEU B 102 ? 0.4287 0.3642 0.3926 -0.0168 -0.0218 -0.0803 102 LEU B N   
3326 C CA  . LEU B 102 ? 0.4301 0.3734 0.4080 -0.0198 -0.0319 -0.0843 102 LEU B CA  
3327 C C   . LEU B 102 ? 0.4442 0.3856 0.4386 -0.0261 -0.0309 -0.0900 102 LEU B C   
3328 O O   . LEU B 102 ? 0.7061 0.6474 0.7034 -0.0299 -0.0394 -0.0984 102 LEU B O   
3329 C CB  . LEU B 102 ? 0.4143 0.3703 0.4070 -0.0180 -0.0333 -0.0778 102 LEU B CB  
3330 C CG  . LEU B 102 ? 0.4465 0.4010 0.4237 -0.0119 -0.0354 -0.0716 102 LEU B CG  
3331 C CD1 . LEU B 102 ? 0.4012 0.3675 0.3954 -0.0091 -0.0368 -0.0672 102 LEU B CD1 
3332 C CD2 . LEU B 102 ? 0.4370 0.3858 0.3943 -0.0101 -0.0471 -0.0751 102 LEU B CD2 
3333 N N   . GLU B 103 ? 0.4215 0.3597 0.4258 -0.0277 -0.0214 -0.0853 103 GLU B N   
3334 C CA  . GLU B 103 ? 0.5090 0.4418 0.5278 -0.0346 -0.0209 -0.0888 103 GLU B CA  
3335 C C   . GLU B 103 ? 0.4455 0.3627 0.4542 -0.0346 -0.0222 -0.0982 103 GLU B C   
3336 O O   . GLU B 103 ? 0.5499 0.4605 0.5688 -0.0409 -0.0256 -0.1039 103 GLU B O   
3337 C CB  . GLU B 103 ? 0.4207 0.3526 0.4505 -0.0365 -0.0119 -0.0797 103 GLU B CB  
3338 C CG  . GLU B 103 ? 0.4340 0.3825 0.4774 -0.0389 -0.0105 -0.0734 103 GLU B CG  
3339 C CD  . GLU B 103 ? 0.5017 0.4626 0.5603 -0.0450 -0.0180 -0.0793 103 GLU B CD  
3340 O OE1 . GLU B 103 ? 0.6046 0.5604 0.6725 -0.0530 -0.0202 -0.0840 103 GLU B OE1 
3341 O OE2 . GLU B 103 ? 0.4992 0.4749 0.5621 -0.0417 -0.0223 -0.0798 103 GLU B OE2 
3342 N N   . ASN B 104 ? 0.4518 0.3632 0.4411 -0.0282 -0.0191 -0.1006 104 ASN B N   
3343 C CA  . ASN B 104 ? 0.4730 0.3725 0.4508 -0.0275 -0.0208 -0.1126 104 ASN B CA  
3344 C C   . ASN B 104 ? 0.4883 0.3899 0.4605 -0.0312 -0.0325 -0.1216 104 ASN B C   
3345 O O   . ASN B 104 ? 0.5596 0.4529 0.5366 -0.0356 -0.0376 -0.1316 104 ASN B O   
3346 C CB  . ASN B 104 ? 0.4777 0.3749 0.4356 -0.0207 -0.0137 -0.1139 104 ASN B CB  
3347 C CG  . ASN B 104 ? 0.4703 0.3625 0.4359 -0.0167 -0.0038 -0.1106 104 ASN B CG  
3348 O OD1 . ASN B 104 ? 0.4669 0.3526 0.4492 -0.0187 -0.0034 -0.1081 104 ASN B OD1 
3349 N ND2 . ASN B 104 ? 0.4701 0.3651 0.4233 -0.0114 0.0038  -0.1102 104 ASN B ND2 
3350 N N   . GLU B 105 ? 0.4862 0.3980 0.4486 -0.0294 -0.0383 -0.1183 105 GLU B N   
3351 C CA  . GLU B 105 ? 0.5014 0.4167 0.4595 -0.0321 -0.0518 -0.1262 105 GLU B CA  
3352 C C   . GLU B 105 ? 0.4983 0.4189 0.4832 -0.0398 -0.0579 -0.1296 105 GLU B C   
3353 O O   . GLU B 105 ? 0.6070 0.5231 0.5928 -0.0445 -0.0662 -0.1407 105 GLU B O   
3354 C CB  . GLU B 105 ? 0.4991 0.4238 0.4463 -0.0282 -0.0584 -0.1197 105 GLU B CB  
3355 C CG  . GLU B 105 ? 0.5177 0.4458 0.4582 -0.0296 -0.0747 -0.1272 105 GLU B CG  
3356 C CD  . GLU B 105 ? 0.7838 0.7005 0.6912 -0.0284 -0.0778 -0.1350 105 GLU B CD  
3357 O OE1 . GLU B 105 ? 0.6697 0.5804 0.5548 -0.0248 -0.0690 -0.1305 105 GLU B OE1 
3358 O OE2 . GLU B 105 ? 0.6816 0.5962 0.5851 -0.0318 -0.0887 -0.1464 105 GLU B OE2 
3359 N N   . ARG B 106 ? 0.4777 0.4083 0.4843 -0.0420 -0.0534 -0.1206 106 ARG B N   
3360 C CA  . ARG B 106 ? 0.4755 0.4140 0.5085 -0.0511 -0.0573 -0.1231 106 ARG B CA  
3361 C C   . ARG B 106 ? 0.4873 0.4098 0.5271 -0.0581 -0.0541 -0.1281 106 ARG B C   
3362 O O   . ARG B 106 ? 0.5236 0.4480 0.5803 -0.0674 -0.0599 -0.1339 106 ARG B O   
3363 C CB  . ARG B 106 ? 0.4533 0.4069 0.5056 -0.0523 -0.0511 -0.1127 106 ARG B CB  
3364 C CG  . ARG B 106 ? 0.4457 0.4183 0.5036 -0.0482 -0.0590 -0.1118 106 ARG B CG  
3365 C CD  . ARG B 106 ? 0.6544 0.6445 0.7361 -0.0509 -0.0529 -0.1055 106 ARG B CD  
3366 N NE  . ARG B 106 ? 0.4964 0.4942 0.6028 -0.0629 -0.0520 -0.1091 106 ARG B NE  
3367 C CZ  . ARG B 106 ? 0.4518 0.4648 0.5767 -0.0681 -0.0620 -0.1176 106 ARG B CZ  
3368 N NH1 . ARG B 106 ? 0.4398 0.4608 0.5604 -0.0610 -0.0753 -0.1232 106 ARG B NH1 
3369 N NH2 . ARG B 106 ? 0.4956 0.5155 0.6436 -0.0809 -0.0593 -0.1202 106 ARG B NH2 
3370 N N   . THR B 107 ? 0.5019 0.4085 0.5305 -0.0538 -0.0455 -0.1262 107 THR B N   
3371 C CA  . THR B 107 ? 0.5054 0.3931 0.5395 -0.0586 -0.0441 -0.1316 107 THR B CA  
3372 C C   . THR B 107 ? 0.5304 0.4084 0.5541 -0.0596 -0.0532 -0.1475 107 THR B C   
3373 O O   . THR B 107 ? 0.5454 0.4149 0.5813 -0.0683 -0.0588 -0.1548 107 THR B O   
3374 C CB  . THR B 107 ? 0.5024 0.3770 0.5295 -0.0517 -0.0339 -0.1261 107 THR B CB  
3375 O OG1 . THR B 107 ? 0.4823 0.3647 0.5190 -0.0522 -0.0266 -0.1118 107 THR B OG1 
3376 C CG2 . THR B 107 ? 0.5225 0.3744 0.5550 -0.0549 -0.0343 -0.1325 107 THR B CG2 
3377 N N   . LEU B 108 ? 0.5790 0.4576 0.5789 -0.0518 -0.0547 -0.1531 108 LEU B N   
3378 C CA  . LEU B 108 ? 0.5643 0.4351 0.5506 -0.0529 -0.0638 -0.1691 108 LEU B CA  
3379 C C   . LEU B 108 ? 0.5698 0.4516 0.5678 -0.0610 -0.0775 -0.1742 108 LEU B C   
3380 O O   . LEU B 108 ? 0.5905 0.4635 0.5927 -0.0674 -0.0856 -0.1867 108 LEU B O   
3381 C CB  . LEU B 108 ? 0.5730 0.4448 0.5287 -0.0443 -0.0621 -0.1725 108 LEU B CB  
3382 C CG  . LEU B 108 ? 0.5714 0.4345 0.5171 -0.0367 -0.0485 -0.1712 108 LEU B CG  
3383 C CD1 . LEU B 108 ? 0.5836 0.4496 0.4984 -0.0308 -0.0459 -0.1752 108 LEU B CD1 
3384 C CD2 . LEU B 108 ? 0.5876 0.4322 0.5415 -0.0372 -0.0465 -0.1821 108 LEU B CD2 
3385 N N   . ASP B 109 ? 0.5525 0.4538 0.5579 -0.0606 -0.0809 -0.1655 109 ASP B N   
3386 C CA  . ASP B 109 ? 0.5554 0.4711 0.5782 -0.0678 -0.0940 -0.1703 109 ASP B CA  
3387 C C   . ASP B 109 ? 0.5937 0.5077 0.6458 -0.0799 -0.0928 -0.1717 109 ASP B C   
3388 O O   . ASP B 109 ? 0.5694 0.4867 0.6340 -0.0885 -0.1038 -0.1820 109 ASP B O   
3389 C CB  . ASP B 109 ? 0.5601 0.4973 0.5900 -0.0636 -0.0965 -0.1605 109 ASP B CB  
3390 C CG  . ASP B 109 ? 0.6347 0.5718 0.6349 -0.0536 -0.1013 -0.1590 109 ASP B CG  
3391 O OD1 . ASP B 109 ? 0.8142 0.7394 0.7891 -0.0520 -0.1060 -0.1680 109 ASP B OD1 
3392 O OD2 . ASP B 109 ? 0.6058 0.5538 0.6068 -0.0479 -0.1002 -0.1489 109 ASP B OD2 
3393 N N   . PHE B 110 ? 0.5416 0.4499 0.6043 -0.0817 -0.0800 -0.1612 110 PHE B N   
3394 C CA  . PHE B 110 ? 0.5452 0.4488 0.6324 -0.0947 -0.0777 -0.1601 110 PHE B CA  
3395 C C   . PHE B 110 ? 0.5736 0.4536 0.6573 -0.1000 -0.0831 -0.1730 110 PHE B C   
3396 O O   . PHE B 110 ? 0.6306 0.5103 0.7327 -0.1126 -0.0898 -0.1795 110 PHE B O   
3397 C CB  . PHE B 110 ? 0.5297 0.4284 0.6220 -0.0943 -0.0636 -0.1452 110 PHE B CB  
3398 C CG  . PHE B 110 ? 0.5381 0.4274 0.6504 -0.1083 -0.0601 -0.1415 110 PHE B CG  
3399 C CD1 . PHE B 110 ? 0.5354 0.4431 0.6724 -0.1213 -0.0624 -0.1412 110 PHE B CD1 
3400 C CD2 . PHE B 110 ? 0.5507 0.4129 0.6575 -0.1086 -0.0547 -0.1380 110 PHE B CD2 
3401 C CE1 . PHE B 110 ? 0.5464 0.4447 0.7000 -0.1363 -0.0581 -0.1366 110 PHE B CE1 
3402 C CE2 . PHE B 110 ? 0.5630 0.4128 0.6853 -0.1223 -0.0522 -0.1328 110 PHE B CE2 
3403 C CZ  . PHE B 110 ? 0.5614 0.4289 0.7060 -0.1372 -0.0533 -0.1315 110 PHE B CZ  
3404 N N   . HIS B 111 ? 0.5851 0.4457 0.6465 -0.0907 -0.0801 -0.1779 111 HIS B N   
3405 C CA  . HIS B 111 ? 0.6148 0.4520 0.6716 -0.0939 -0.0855 -0.1926 111 HIS B CA  
3406 C C   . HIS B 111 ? 0.6327 0.4770 0.6864 -0.0984 -0.1004 -0.2080 111 HIS B C   
3407 O O   . HIS B 111 ? 0.6974 0.5312 0.7631 -0.1090 -0.1082 -0.2185 111 HIS B O   
3408 C CB  . HIS B 111 ? 0.6235 0.4436 0.6574 -0.0813 -0.0789 -0.1971 111 HIS B CB  
3409 C CG  . HIS B 111 ? 0.6124 0.4215 0.6515 -0.0770 -0.0670 -0.1847 111 HIS B CG  
3410 N ND1 . HIS B 111 ? 0.6233 0.4123 0.6784 -0.0841 -0.0658 -0.1815 111 HIS B ND1 
3411 C CD2 . HIS B 111 ? 0.5939 0.4085 0.6239 -0.0666 -0.0569 -0.1746 111 HIS B CD2 
3412 C CE1 . HIS B 111 ? 0.6123 0.3950 0.6669 -0.0774 -0.0563 -0.1698 111 HIS B CE1 
3413 N NE2 . HIS B 111 ? 0.5934 0.3924 0.6340 -0.0668 -0.0507 -0.1660 111 HIS B NE2 
3414 N N   . ASP B 112 ? 0.6276 0.4883 0.6640 -0.0908 -0.1054 -0.2094 112 ASP B N   
3415 C CA  . ASP B 112 ? 0.6460 0.5147 0.6771 -0.0942 -0.1215 -0.2229 112 ASP B CA  
3416 C C   . ASP B 112 ? 0.6433 0.5264 0.7074 -0.1079 -0.1302 -0.2240 112 ASP B C   
3417 O O   . ASP B 112 ? 0.6851 0.5640 0.7553 -0.1164 -0.1423 -0.2384 112 ASP B O   
3418 C CB  . ASP B 112 ? 0.6394 0.5239 0.6483 -0.0842 -0.1257 -0.2193 112 ASP B CB  
3419 C CG  . ASP B 112 ? 0.6670 0.5526 0.6569 -0.0843 -0.1422 -0.2343 112 ASP B CG  
3420 O OD1 . ASP B 112 ? 0.6936 0.5632 0.6776 -0.0887 -0.1471 -0.2498 112 ASP B OD1 
3421 O OD2 . ASP B 112 ? 0.6647 0.5657 0.6443 -0.0796 -0.1511 -0.2308 112 ASP B OD2 
3422 N N   . SER B 113 ? 0.6169 0.5176 0.7033 -0.1108 -0.1235 -0.2099 113 SER B N   
3423 C CA  . SER B 113 ? 0.6134 0.5316 0.7340 -0.1248 -0.1289 -0.2108 113 SER B CA  
3424 C C   . SER B 113 ? 0.6313 0.5296 0.7677 -0.1391 -0.1268 -0.2152 113 SER B C   
3425 O O   . SER B 113 ? 0.6449 0.5495 0.8020 -0.1522 -0.1367 -0.2247 113 SER B O   
3426 C CB  . SER B 113 ? 0.5830 0.5240 0.7222 -0.1244 -0.1193 -0.1953 113 SER B CB  
3427 O OG  . SER B 113 ? 0.5810 0.5370 0.7549 -0.1399 -0.1195 -0.1954 113 SER B OG  
3428 N N   . ASN B 114 ? 0.6334 0.5069 0.7613 -0.1370 -0.1149 -0.2083 114 ASN B N   
3429 C CA  . ASN B 114 ? 0.6548 0.5042 0.7958 -0.1502 -0.1139 -0.2112 114 ASN B CA  
3430 C C   . ASN B 114 ? 0.6876 0.5196 0.8209 -0.1533 -0.1272 -0.2315 114 ASN B C   
3431 O O   . ASN B 114 ? 0.7068 0.5318 0.8597 -0.1689 -0.1339 -0.2387 114 ASN B O   
3432 C CB  . ASN B 114 ? 0.6534 0.4780 0.7846 -0.1445 -0.1008 -0.2000 114 ASN B CB  
3433 C CG  . ASN B 114 ? 0.6271 0.4658 0.7693 -0.1462 -0.0883 -0.1803 114 ASN B CG  
3434 O OD1 . ASN B 114 ? 0.6590 0.5219 0.8224 -0.1564 -0.0879 -0.1755 114 ASN B OD1 
3435 N ND2 . ASN B 114 ? 0.6195 0.4443 0.7481 -0.1363 -0.0781 -0.1698 114 ASN B ND2 
3436 N N   . VAL B 115 ? 0.7259 0.5511 0.8302 -0.1395 -0.1310 -0.2415 115 VAL B N   
3437 C CA  . VAL B 115 ? 0.7303 0.5396 0.8236 -0.1415 -0.1436 -0.2626 115 VAL B CA  
3438 C C   . VAL B 115 ? 0.7370 0.5682 0.8439 -0.1514 -0.1597 -0.2726 115 VAL B C   
3439 O O   . VAL B 115 ? 0.7622 0.5834 0.8820 -0.1640 -0.1699 -0.2859 115 VAL B O   
3440 C CB  . VAL B 115 ? 0.7395 0.5398 0.7962 -0.1249 -0.1420 -0.2708 115 VAL B CB  
3441 C CG1 . VAL B 115 ? 0.7765 0.5631 0.8190 -0.1269 -0.1553 -0.2942 115 VAL B CG1 
3442 C CG2 . VAL B 115 ? 0.7356 0.5150 0.7842 -0.1157 -0.1272 -0.2637 115 VAL B CG2 
3443 N N   . LYS B 116 ? 0.7163 0.5773 0.8218 -0.1456 -0.1634 -0.2667 116 LYS B N   
3444 C CA  . LYS B 116 ? 0.7215 0.6066 0.8432 -0.1533 -0.1802 -0.2757 116 LYS B CA  
3445 C C   . LYS B 116 ? 0.7212 0.6141 0.8837 -0.1726 -0.1811 -0.2750 116 LYS B C   
3446 O O   . LYS B 116 ? 0.7427 0.6382 0.9195 -0.1843 -0.1953 -0.2897 116 LYS B O   
3447 C CB  . LYS B 116 ? 0.6972 0.6120 0.8154 -0.1429 -0.1827 -0.2663 116 LYS B CB  
3448 C CG  . LYS B 116 ? 0.7002 0.6436 0.8388 -0.1485 -0.2012 -0.2743 116 LYS B CG  
3449 C CD  . LYS B 116 ? 0.7976 0.7331 0.9143 -0.1476 -0.2204 -0.2933 116 LYS B CD  
3450 C CE  . LYS B 116 ? 0.7378 0.7032 0.8755 -0.1519 -0.2409 -0.3010 116 LYS B CE  
3451 N NZ  . LYS B 116 ? 0.9889 0.9784 1.1236 -0.1390 -0.2439 -0.2895 116 LYS B NZ  
3452 N N   . ASN B 117 ? 0.7593 0.6557 0.9402 -0.1773 -0.1656 -0.2583 117 ASN B N   
3453 C CA  . ASN B 117 ? 0.7675 0.6731 0.9861 -0.1973 -0.1638 -0.2557 117 ASN B CA  
3454 C C   . ASN B 117 ? 0.7330 0.6056 0.9555 -0.2110 -0.1665 -0.2650 117 ASN B C   
3455 O O   . ASN B 117 ? 0.7473 0.6264 0.9973 -0.2294 -0.1739 -0.2724 117 ASN B O   
3456 C CB  . ASN B 117 ? 0.6729 0.5876 0.9039 -0.1988 -0.1454 -0.2351 117 ASN B CB  
3457 C CG  . ASN B 117 ? 0.6421 0.5933 0.8794 -0.1892 -0.1439 -0.2277 117 ASN B CG  
3458 O OD1 . ASN B 117 ? 0.6965 0.6711 0.9394 -0.1857 -0.1580 -0.2373 117 ASN B OD1 
3459 N ND2 . ASN B 117 ? 0.6547 0.6102 0.8911 -0.1845 -0.1280 -0.2109 117 ASN B ND2 
3460 N N   . LEU B 118 ? 0.7469 0.5840 0.9442 -0.2027 -0.1609 -0.2653 118 LEU B N   
3461 C CA  . LEU B 118 ? 0.7822 0.5839 0.9820 -0.2137 -0.1650 -0.2755 118 LEU B CA  
3462 C C   . LEU B 118 ? 0.8101 0.6113 1.0081 -0.2182 -0.1840 -0.2991 118 LEU B C   
3463 O O   . LEU B 118 ? 0.8355 0.6297 1.0487 -0.2343 -0.1891 -0.3032 118 LEU B O   
3464 C CB  . LEU B 118 ? 0.7913 0.5576 0.9650 -0.2001 -0.1561 -0.2730 118 LEU B CB  
3465 C CG  . LEU B 118 ? 0.8302 0.5544 1.0043 -0.2078 -0.1602 -0.2836 118 LEU B CG  
3466 C CD1 . LEU B 118 ? 0.8538 0.5677 1.0566 -0.2292 -0.1562 -0.2720 118 LEU B CD1 
3467 C CD2 . LEU B 118 ? 0.8365 0.5316 0.9857 -0.1902 -0.1522 -0.2828 118 LEU B CD2 
3468 N N   . TYR B 119 ? 0.8099 0.6200 0.9810 -0.2026 -0.1918 -0.3089 119 TYR B N   
3469 C CA  . TYR B 119 ? 0.8384 0.6518 0.9995 -0.2044 -0.2086 -0.3271 119 TYR B CA  
3470 C C   . TYR B 119 ? 0.8434 0.6879 1.0357 -0.2194 -0.2181 -0.3268 119 TYR B C   
3471 O O   . TYR B 119 ? 0.9251 0.7645 1.1227 -0.2305 -0.2270 -0.3361 119 TYR B O   
3472 C CB  . TYR B 119 ? 0.8360 0.6576 0.9628 -0.1862 -0.2153 -0.3352 119 TYR B CB  
3473 C CG  . TYR B 119 ? 0.8669 0.6945 0.9769 -0.1864 -0.2318 -0.3504 119 TYR B CG  
3474 C CD1 . TYR B 119 ? 0.9315 0.7314 1.0170 -0.1850 -0.2339 -0.3642 119 TYR B CD1 
3475 C CD2 . TYR B 119 ? 0.8593 0.7201 0.9775 -0.1873 -0.2455 -0.3511 119 TYR B CD2 
3476 C CE1 . TYR B 119 ? 0.9948 0.7999 1.0632 -0.1859 -0.2488 -0.3783 119 TYR B CE1 
3477 C CE2 . TYR B 119 ? 0.8902 0.7557 0.9917 -0.1874 -0.2616 -0.3642 119 TYR B CE2 
3478 C CZ  . TYR B 119 ? 1.0040 0.8414 1.0797 -0.1874 -0.2629 -0.3777 119 TYR B CZ  
3479 O OH  . TYR B 119 ? 0.9619 0.8038 1.0196 -0.1883 -0.2787 -0.3910 119 TYR B OH  
3480 N N   . GLU B 120 ? 0.8019 0.6799 1.0164 -0.2197 -0.2161 -0.3170 120 GLU B N   
3481 C CA  . GLU B 120 ? 0.7987 0.7105 1.0467 -0.2328 -0.2238 -0.3168 120 GLU B CA  
3482 C C   . GLU B 120 ? 0.8123 0.7155 1.0883 -0.2544 -0.2161 -0.3112 120 GLU B C   
3483 O O   . GLU B 120 ? 0.9271 0.8466 1.2240 -0.2679 -0.2245 -0.3165 120 GLU B O   
3484 C CB  . GLU B 120 ? 0.7590 0.7087 1.0260 -0.2269 -0.2215 -0.3077 120 GLU B CB  
3485 C CG  . GLU B 120 ? 0.7505 0.7111 0.9890 -0.2064 -0.2312 -0.3107 120 GLU B CG  
3486 C CD  . GLU B 120 ? 1.1115 1.0818 1.3402 -0.2048 -0.2526 -0.3253 120 GLU B CD  
3487 O OE1 . GLU B 120 ? 1.0709 1.0569 1.3261 -0.2182 -0.2597 -0.3296 120 GLU B OE1 
3488 O OE2 . GLU B 120 ? 1.1125 1.0745 1.3043 -0.1902 -0.2611 -0.3310 120 GLU B OE2 
3489 N N   . LYS B 121 ? 0.8087 0.6862 1.0846 -0.2584 -0.2005 -0.3000 121 LYS B N   
3490 C CA  . LYS B 121 ? 0.8286 0.6914 1.1245 -0.2794 -0.1934 -0.2930 121 LYS B CA  
3491 C C   . LYS B 121 ? 0.9215 0.7563 1.2053 -0.2862 -0.2035 -0.3061 121 LYS B C   
3492 O O   . LYS B 121 ? 0.8947 0.7375 1.1991 -0.3043 -0.2086 -0.3088 121 LYS B O   
3493 C CB  . LYS B 121 ? 0.8205 0.6562 1.1123 -0.2799 -0.1764 -0.2773 121 LYS B CB  
3494 C CG  . LYS B 121 ? 0.8606 0.7235 1.1703 -0.2796 -0.1635 -0.2624 121 LYS B CG  
3495 C CD  . LYS B 121 ? 1.1106 0.9425 1.4091 -0.2782 -0.1478 -0.2460 121 LYS B CD  
3496 C CE  . LYS B 121 ? 1.2364 1.0948 1.5362 -0.2708 -0.1323 -0.2268 121 LYS B CE  
3497 N NZ  . LYS B 121 ? 1.1814 1.0092 1.4621 -0.2652 -0.1183 -0.2097 121 LYS B NZ  
3498 N N   . VAL B 122 ? 0.9212 0.7237 1.1719 -0.2721 -0.2060 -0.3149 122 VAL B N   
3499 C CA  . VAL B 122 ? 0.9369 0.7108 1.1741 -0.2772 -0.2147 -0.3288 122 VAL B CA  
3500 C C   . VAL B 122 ? 0.9510 0.7509 1.1935 -0.2818 -0.2315 -0.3430 122 VAL B C   
3501 O O   . VAL B 122 ? 0.9839 0.7760 1.2365 -0.2974 -0.2383 -0.3501 122 VAL B O   
3502 C CB  . VAL B 122 ? 0.9508 0.6911 1.1515 -0.2584 -0.2130 -0.3371 122 VAL B CB  
3503 C CG1 . VAL B 122 ? 1.0029 0.7175 1.1886 -0.2619 -0.2226 -0.3542 122 VAL B CG1 
3504 C CG2 . VAL B 122 ? 0.9428 0.6550 1.1415 -0.2550 -0.1978 -0.3229 122 VAL B CG2 
3505 N N   . LYS B 123 ? 0.9289 0.7588 1.1641 -0.2686 -0.2391 -0.3470 123 LYS B N   
3506 C CA  . LYS B 123 ? 0.9419 0.7986 1.1822 -0.2717 -0.2564 -0.3589 123 LYS B CA  
3507 C C   . LYS B 123 ? 0.9400 0.8238 1.2226 -0.2922 -0.2579 -0.3540 123 LYS B C   
3508 O O   . LYS B 123 ? 0.9708 0.8566 1.2625 -0.3047 -0.2690 -0.3642 123 LYS B O   
3509 C CB  . LYS B 123 ? 1.0439 0.9278 1.2698 -0.2535 -0.2635 -0.3599 123 LYS B CB  
3510 C CG  . LYS B 123 ? 0.9276 0.8423 1.1603 -0.2548 -0.2825 -0.3694 123 LYS B CG  
3511 C CD  . LYS B 123 ? 0.9031 0.8420 1.1213 -0.2365 -0.2889 -0.3669 123 LYS B CD  
3512 C CE  . LYS B 123 ? 0.9187 0.8849 1.1394 -0.2355 -0.3098 -0.3759 123 LYS B CE  
3513 N NZ  . LYS B 123 ? 0.9589 0.9431 1.1599 -0.2169 -0.3175 -0.3724 123 LYS B NZ  
3514 N N   . SER B 124 ? 0.9055 0.8112 1.2144 -0.2963 -0.2461 -0.3388 124 SER B N   
3515 C CA  . SER B 124 ? 0.9326 0.8665 1.2824 -0.3163 -0.2443 -0.3331 124 SER B CA  
3516 C C   . SER B 124 ? 1.0977 1.0031 1.4557 -0.3380 -0.2399 -0.3321 124 SER B C   
3517 O O   . SER B 124 ? 0.9977 0.9231 1.3851 -0.3567 -0.2427 -0.3324 124 SER B O   
3518 C CB  . SER B 124 ? 0.8904 0.8495 1.2625 -0.3160 -0.2291 -0.3167 124 SER B CB  
3519 O OG  . SER B 124 ? 1.0148 0.9415 1.3756 -0.3171 -0.2126 -0.3044 124 SER B OG  
3520 N N   . GLN B 125 ? 1.1752 1.0343 1.5083 -0.3357 -0.2333 -0.3307 125 GLN B N   
3521 C CA  . GLN B 125 ? 1.1097 0.9365 1.4465 -0.3551 -0.2313 -0.3307 125 GLN B CA  
3522 C C   . GLN B 125 ? 1.1070 0.9226 1.4329 -0.3581 -0.2480 -0.3504 125 GLN B C   
3523 O O   . GLN B 125 ? 1.1333 0.9504 1.4783 -0.3787 -0.2529 -0.3537 125 GLN B O   
3524 C CB  . GLN B 125 ? 1.1769 0.9571 1.4919 -0.3501 -0.2189 -0.3219 125 GLN B CB  
3525 C CG  . GLN B 125 ? 1.2920 1.0742 1.6221 -0.3578 -0.2017 -0.3002 125 GLN B CG  
3526 C CD  . GLN B 125 ? 1.1970 0.9292 1.5141 -0.3646 -0.1928 -0.2912 125 GLN B CD  
3527 O OE1 . GLN B 125 ? 1.2580 0.9810 1.5901 -0.3867 -0.1870 -0.2810 125 GLN B OE1 
3528 N NE2 . GLN B 125 ? 1.1307 0.8299 1.4190 -0.3455 -0.1918 -0.2950 125 GLN B NE2 
3529 N N   . LEU B 126 ? 1.0829 0.8874 1.3772 -0.3386 -0.2565 -0.3636 126 LEU B N   
3530 C CA  . LEU B 126 ? 1.0884 0.8762 1.3668 -0.3407 -0.2708 -0.3827 126 LEU B CA  
3531 C C   . LEU B 126 ? 1.0934 0.9202 1.3903 -0.3481 -0.2870 -0.3923 126 LEU B C   
3532 O O   . LEU B 126 ? 1.1523 0.9721 1.4556 -0.3626 -0.2969 -0.4033 126 LEU B O   
3533 C CB  . LEU B 126 ? 1.0950 0.8610 1.3320 -0.3179 -0.2734 -0.3937 126 LEU B CB  
3534 C CG  . LEU B 126 ? 1.0944 0.8211 1.3127 -0.3083 -0.2588 -0.3868 126 LEU B CG  
3535 C CD1 . LEU B 126 ? 1.1082 0.8160 1.2867 -0.2875 -0.2618 -0.4009 126 LEU B CD1 
3536 C CD2 . LEU B 126 ? 1.1285 0.8196 1.3571 -0.3257 -0.2535 -0.3835 126 LEU B CD2 
3537 N N   . LYS B 127 ? 1.3087 1.1759 1.6147 -0.3380 -0.2905 -0.3884 127 LYS B N   
3538 C CA  . LYS B 127 ? 1.1927 1.0994 1.5164 -0.3415 -0.3073 -0.3971 127 LYS B CA  
3539 C C   . LYS B 127 ? 1.1983 1.0890 1.4905 -0.3348 -0.3238 -0.4165 127 LYS B C   
3540 O O   . LYS B 127 ? 1.2420 1.1101 1.4961 -0.3177 -0.3229 -0.4213 127 LYS B O   
3541 C CB  . LYS B 127 ? 1.1199 1.0466 1.4865 -0.3661 -0.3061 -0.3927 127 LYS B CB  
3542 C CG  . LYS B 127 ? 1.0981 1.0392 1.4923 -0.3737 -0.2877 -0.3733 127 LYS B CG  
3543 C CD  . LYS B 127 ? 1.1403 1.0975 1.5733 -0.4007 -0.2853 -0.3694 127 LYS B CD  
3544 C CE  . LYS B 127 ? 1.1936 1.1613 1.6493 -0.4098 -0.2651 -0.3495 127 LYS B CE  
3545 N NZ  . LYS B 127 ? 1.2361 1.2171 1.7264 -0.4379 -0.2612 -0.3447 127 LYS B NZ  
3546 N N   . ASN B 128 ? 1.2475 1.1496 1.5537 -0.3483 -0.3385 -0.4282 128 ASN B N   
3547 C CA  . ASN B 128 ? 1.2467 1.1381 1.5236 -0.3427 -0.3554 -0.4470 128 ASN B CA  
3548 C C   . ASN B 128 ? 1.2147 1.0605 1.4741 -0.3519 -0.3538 -0.4579 128 ASN B C   
3549 O O   . ASN B 128 ? 1.2538 1.0912 1.4953 -0.3529 -0.3681 -0.4751 128 ASN B O   
3550 C CB  . ASN B 128 ? 1.1812 1.1105 1.4812 -0.3507 -0.3745 -0.4551 128 ASN B CB  
3551 C CG  . ASN B 128 ? 1.2013 1.1361 1.5400 -0.3769 -0.3749 -0.4558 128 ASN B CG  
3552 O OD1 . ASN B 128 ? 1.1926 1.1152 1.5501 -0.3896 -0.3590 -0.4443 128 ASN B OD1 
3553 N ND2 . ASN B 128 ? 1.2906 1.2435 1.6405 -0.3860 -0.3933 -0.4690 128 ASN B ND2 
3554 N N   . ASN B 129 ? 1.2130 1.0287 1.4766 -0.3583 -0.3373 -0.4485 129 ASN B N   
3555 C CA  . ASN B 129 ? 1.2563 1.0249 1.5011 -0.3635 -0.3349 -0.4582 129 ASN B CA  
3556 C C   . ASN B 129 ? 1.2613 1.0016 1.4625 -0.3413 -0.3308 -0.4653 129 ASN B C   
3557 O O   . ASN B 129 ? 1.2953 0.9952 1.4796 -0.3419 -0.3271 -0.4734 129 ASN B O   
3558 C CB  . ASN B 129 ? 1.2578 1.0033 1.5240 -0.3797 -0.3199 -0.4443 129 ASN B CB  
3559 C CG  . ASN B 129 ? 1.3352 1.1013 1.6409 -0.4060 -0.3238 -0.4407 129 ASN B CG  
3560 O OD1 . ASN B 129 ? 1.3628 1.1674 1.6860 -0.4103 -0.3365 -0.4463 129 ASN B OD1 
3561 N ND2 . ASN B 129 ? 1.2852 1.0255 1.6047 -0.4239 -0.3130 -0.4311 129 ASN B ND2 
3562 N N   . ALA B 130 ? 1.2304 0.9911 1.4136 -0.3221 -0.3311 -0.4625 130 ALA B N   
3563 C CA  . ALA B 130 ? 1.2343 0.9737 1.3753 -0.3012 -0.3267 -0.4689 130 ALA B CA  
3564 C C   . ALA B 130 ? 1.2102 0.9821 1.3346 -0.2859 -0.3342 -0.4683 130 ALA B C   
3565 O O   . ALA B 130 ? 1.1771 0.9841 1.3257 -0.2877 -0.3371 -0.4573 130 ALA B O   
3566 C CB  . ALA B 130 ? 1.2203 0.9343 1.3581 -0.2933 -0.3072 -0.4562 130 ALA B CB  
3567 N N   . LYS B 131 ? 1.2298 0.9897 1.3121 -0.2711 -0.3373 -0.4801 131 LYS B N   
3568 C CA  . LYS B 131 ? 1.2149 1.0010 1.2745 -0.2570 -0.3452 -0.4794 131 LYS B CA  
3569 C C   . LYS B 131 ? 1.3271 1.1069 1.3654 -0.2392 -0.3301 -0.4692 131 LYS B C   
3570 O O   . LYS B 131 ? 1.2027 0.9526 1.2301 -0.2342 -0.3157 -0.4696 131 LYS B O   
3571 C CB  . LYS B 131 ? 1.2902 1.0716 1.3138 -0.2539 -0.3597 -0.4984 131 LYS B CB  
3572 C CG  . LYS B 131 ? 1.3353 1.0883 1.3125 -0.2398 -0.3509 -0.5081 131 LYS B CG  
3573 C CD  . LYS B 131 ? 1.4165 1.1717 1.3571 -0.2376 -0.3661 -0.5252 131 LYS B CD  
3574 C CE  . LYS B 131 ? 1.4615 1.1923 1.3541 -0.2239 -0.3561 -0.5355 131 LYS B CE  
3575 N NZ  . LYS B 131 ? 1.5206 1.2542 1.3748 -0.2231 -0.3704 -0.5516 131 LYS B NZ  
3576 N N   . GLU B 132 ? 1.3042 1.1127 1.3374 -0.2294 -0.3340 -0.4601 132 GLU B N   
3577 C CA  . GLU B 132 ? 1.2941 1.1016 1.3105 -0.2136 -0.3206 -0.4488 132 GLU B CA  
3578 C C   . GLU B 132 ? 1.4058 1.2027 1.3699 -0.1993 -0.3216 -0.4586 132 GLU B C   
3579 O O   . GLU B 132 ? 1.4790 1.2954 1.4216 -0.1915 -0.3313 -0.4569 132 GLU B O   
3580 C CB  . GLU B 132 ? 1.2922 1.1347 1.3314 -0.2108 -0.3236 -0.4332 132 GLU B CB  
3581 C CG  . GLU B 132 ? 1.2744 1.1238 1.3585 -0.2204 -0.3128 -0.4192 132 GLU B CG  
3582 C CD  . GLU B 132 ? 1.3656 1.2484 1.4681 -0.2145 -0.3132 -0.4047 132 GLU B CD  
3583 O OE1 . GLU B 132 ? 1.3646 1.2740 1.4663 -0.2113 -0.3289 -0.4063 132 GLU B OE1 
3584 O OE2 . GLU B 132 ? 1.4398 1.3216 1.5569 -0.2124 -0.2984 -0.3918 132 GLU B OE2 
3585 N N   . ILE B 133 ? 1.5301 1.2950 1.4728 -0.1959 -0.3110 -0.4687 133 ILE B N   
3586 C CA  . ILE B 133 ? 1.5814 1.3365 1.4757 -0.1815 -0.3057 -0.4758 133 ILE B CA  
3587 C C   . ILE B 133 ? 1.5963 1.3604 1.4846 -0.1687 -0.2932 -0.4602 133 ILE B C   
3588 O O   . ILE B 133 ? 1.7300 1.4993 1.6507 -0.1702 -0.2854 -0.4461 133 ILE B O   
3589 C CB  . ILE B 133 ? 1.6869 1.4074 1.5635 -0.1796 -0.2955 -0.4908 133 ILE B CB  
3590 C CG1 . ILE B 133 ? 1.7130 1.4136 1.6222 -0.1827 -0.2820 -0.4835 133 ILE B CG1 
3591 C CG2 . ILE B 133 ? 1.6584 1.3705 1.5263 -0.1897 -0.3096 -0.5093 133 ILE B CG2 
3592 C CD1 . ILE B 133 ? 1.7416 1.4070 1.6385 -0.1803 -0.2736 -0.4979 133 ILE B CD1 
3593 N N   . GLY B 134 ? 1.6316 1.3976 1.4767 -0.1568 -0.2910 -0.4626 134 GLY B N   
3594 C CA  . GLY B 134 ? 1.6787 1.4533 1.5132 -0.1448 -0.2802 -0.4487 134 GLY B CA  
3595 C C   . GLY B 134 ? 1.5740 1.3302 1.4203 -0.1392 -0.2597 -0.4441 134 GLY B C   
3596 O O   . GLY B 134 ? 1.6262 1.3609 1.4888 -0.1441 -0.2541 -0.4511 134 GLY B O   
3597 N N   . ASN B 135 ? 1.3212 1.0852 1.1595 -0.1287 -0.2493 -0.4318 135 ASN B N   
3598 C CA  . ASN B 135 ? 1.2161 0.9653 1.0620 -0.1212 -0.2298 -0.4267 135 ASN B CA  
3599 C C   . ASN B 135 ? 1.0678 0.8113 0.9614 -0.1297 -0.2266 -0.4178 135 ASN B C   
3600 O O   . ASN B 135 ? 1.0132 0.7381 0.9165 -0.1257 -0.2125 -0.4157 135 ASN B O   
3601 C CB  . ASN B 135 ? 1.4099 1.1352 1.2290 -0.1146 -0.2185 -0.4421 135 ASN B CB  
3602 C CG  . ASN B 135 ? 1.3983 1.1205 1.2003 -0.1007 -0.1999 -0.4377 135 ASN B CG  
3603 O OD1 . ASN B 135 ? 1.3611 1.0882 1.1844 -0.0974 -0.1920 -0.4237 135 ASN B OD1 
3604 N ND2 . ASN B 135 ? 1.4017 1.1170 1.1654 -0.0931 -0.1922 -0.4501 135 ASN B ND2 
3605 N N   . GLY B 136 ? 1.1570 0.9166 1.0804 -0.1416 -0.2391 -0.4120 136 GLY B N   
3606 C CA  . GLY B 136 ? 1.1145 0.8717 1.0816 -0.1517 -0.2349 -0.4016 136 GLY B CA  
3607 C C   . GLY B 136 ? 1.1212 0.8518 1.1032 -0.1615 -0.2333 -0.4094 136 GLY B C   
3608 O O   . GLY B 136 ? 1.0701 0.7884 1.0789 -0.1668 -0.2245 -0.3999 136 GLY B O   
3609 N N   . CYS B 137 ? 1.0923 0.8124 1.0566 -0.1645 -0.2419 -0.4261 137 CYS B N   
3610 C CA  . CYS B 137 ? 1.2507 0.9441 1.2275 -0.1744 -0.2424 -0.4350 137 CYS B CA  
3611 C C   . CYS B 137 ? 1.1040 0.8096 1.1008 -0.1913 -0.2585 -0.4393 137 CYS B C   
3612 O O   . CYS B 137 ? 1.1641 0.8970 1.1571 -0.1928 -0.2709 -0.4401 137 CYS B O   
3613 C CB  . CYS B 137 ? 1.2068 0.8758 1.1495 -0.1650 -0.2388 -0.4529 137 CYS B CB  
3614 S SG  . CYS B 137 ? 1.2881 0.9411 1.2115 -0.1454 -0.2185 -0.4505 137 CYS B SG  
3615 N N   . PHE B 138 ? 1.1253 0.8100 1.1438 -0.2042 -0.2586 -0.4419 138 PHE B N   
3616 C CA  . PHE B 138 ? 1.1868 0.8795 1.2257 -0.2221 -0.2726 -0.4475 138 PHE B CA  
3617 C C   . PHE B 138 ? 1.2070 0.8691 1.2317 -0.2260 -0.2766 -0.4659 138 PHE B C   
3618 O O   . PHE B 138 ? 1.2139 0.8436 1.2384 -0.2240 -0.2667 -0.4670 138 PHE B O   
3619 C CB  . PHE B 138 ? 1.2379 0.9360 1.3199 -0.2382 -0.2691 -0.4320 138 PHE B CB  
3620 C CG  . PHE B 138 ? 1.0762 0.8063 1.1762 -0.2359 -0.2653 -0.4148 138 PHE B CG  
3621 C CD1 . PHE B 138 ? 1.0629 0.8302 1.1776 -0.2413 -0.2773 -0.4135 138 PHE B CD1 
3622 C CD2 . PHE B 138 ? 1.1334 0.8566 1.2366 -0.2280 -0.2500 -0.4004 138 PHE B CD2 
3623 C CE1 . PHE B 138 ? 1.0187 0.8157 1.1515 -0.2383 -0.2738 -0.3987 138 PHE B CE1 
3624 C CE2 . PHE B 138 ? 1.0004 0.7527 1.1203 -0.2261 -0.2463 -0.3856 138 PHE B CE2 
3625 C CZ  . PHE B 138 ? 0.9876 0.7768 1.1224 -0.2311 -0.2579 -0.3850 138 PHE B CZ  
3626 N N   . GLU B 139 ? 1.4025 1.0742 1.4154 -0.2312 -0.2918 -0.4805 139 GLU B N   
3627 C CA  . GLU B 139 ? 1.2963 0.9412 1.2973 -0.2369 -0.2976 -0.4995 139 GLU B CA  
3628 C C   . GLU B 139 ? 1.2983 0.9434 1.3342 -0.2591 -0.3068 -0.4990 139 GLU B C   
3629 O O   . GLU B 139 ? 1.2930 0.9679 1.3437 -0.2687 -0.3196 -0.4983 139 GLU B O   
3630 C CB  . GLU B 139 ? 1.4094 1.0626 1.3728 -0.2300 -0.3086 -0.5167 139 GLU B CB  
3631 C CG  . GLU B 139 ? 1.5714 1.1920 1.5112 -0.2287 -0.3089 -0.5377 139 GLU B CG  
3632 C CD  . GLU B 139 ? 1.7171 1.3462 1.6164 -0.2228 -0.3187 -0.5543 139 GLU B CD  
3633 O OE1 . GLU B 139 ? 1.7192 1.3708 1.6212 -0.2318 -0.3353 -0.5574 139 GLU B OE1 
3634 O OE2 . GLU B 139 ? 1.7913 1.4054 1.6561 -0.2091 -0.3096 -0.5641 139 GLU B OE2 
3635 N N   . PHE B 140 ? 1.3191 0.9313 1.3685 -0.2670 -0.3002 -0.4991 140 PHE B N   
3636 C CA  . PHE B 140 ? 1.3882 0.9975 1.4711 -0.2898 -0.3061 -0.4964 140 PHE B CA  
3637 C C   . PHE B 140 ? 1.5408 1.1517 1.6178 -0.3004 -0.3232 -0.5160 140 PHE B C   
3638 O O   . PHE B 140 ? 1.5121 1.1044 1.5586 -0.2923 -0.3270 -0.5343 140 PHE B O   
3639 C CB  . PHE B 140 ? 1.4658 1.0345 1.5593 -0.2951 -0.2950 -0.4911 140 PHE B CB  
3640 C CG  . PHE B 140 ? 1.3575 0.9264 1.4663 -0.2914 -0.2801 -0.4687 140 PHE B CG  
3641 C CD1 . PHE B 140 ? 1.3971 0.9849 1.5393 -0.3079 -0.2781 -0.4513 140 PHE B CD1 
3642 C CD2 . PHE B 140 ? 1.3379 0.8890 1.4276 -0.2718 -0.2677 -0.4653 140 PHE B CD2 
3643 C CE1 . PHE B 140 ? 1.3566 0.9442 1.5110 -0.3052 -0.2643 -0.4307 140 PHE B CE1 
3644 C CE2 . PHE B 140 ? 1.2998 0.8507 1.4031 -0.2686 -0.2548 -0.4447 140 PHE B CE2 
3645 C CZ  . PHE B 140 ? 1.3005 0.8689 1.4351 -0.2855 -0.2532 -0.4273 140 PHE B CZ  
3646 N N   . TYR B 141 ? 1.5383 1.1726 1.6453 -0.3191 -0.3333 -0.5126 141 TYR B N   
3647 C CA  . TYR B 141 ? 1.5306 1.1669 1.6393 -0.3329 -0.3501 -0.5298 141 TYR B CA  
3648 C C   . TYR B 141 ? 1.5722 1.1751 1.6983 -0.3516 -0.3492 -0.5339 141 TYR B C   
3649 O O   . TYR B 141 ? 1.6507 1.2551 1.7846 -0.3668 -0.3629 -0.5469 141 TYR B O   
3650 C CB  . TYR B 141 ? 1.5236 1.2062 1.6570 -0.3427 -0.3628 -0.5250 141 TYR B CB  
3651 C CG  . TYR B 141 ? 1.5368 1.2487 1.6457 -0.3269 -0.3725 -0.5297 141 TYR B CG  
3652 C CD1 . TYR B 141 ? 1.5890 1.2846 1.6534 -0.3116 -0.3746 -0.5443 141 TYR B CD1 
3653 C CD2 . TYR B 141 ? 1.5419 1.2974 1.6714 -0.3275 -0.3795 -0.5194 141 TYR B CD2 
3654 C CE1 . TYR B 141 ? 1.6559 1.3762 1.6943 -0.2986 -0.3835 -0.5472 141 TYR B CE1 
3655 C CE2 . TYR B 141 ? 1.5551 1.3348 1.6607 -0.3130 -0.3895 -0.5225 141 TYR B CE2 
3656 C CZ  . TYR B 141 ? 1.6251 1.3863 1.6838 -0.2993 -0.3915 -0.5358 141 TYR B CZ  
3657 O OH  . TYR B 141 ? 1.6151 1.3986 1.6466 -0.2862 -0.4014 -0.5374 141 TYR B OH  
3658 N N   . HIS B 142 ? 1.5027 1.0750 1.6347 -0.3512 -0.3343 -0.5230 142 HIS B N   
3659 C CA  . HIS B 142 ? 1.4974 1.0350 1.6452 -0.3693 -0.3328 -0.5243 142 HIS B CA  
3660 C C   . HIS B 142 ? 1.5806 1.0752 1.7138 -0.3568 -0.3186 -0.5208 142 HIS B C   
3661 O O   . HIS B 142 ? 1.4799 0.9746 1.5926 -0.3349 -0.3100 -0.5181 142 HIS B O   
3662 C CB  . HIS B 142 ? 1.4802 1.0359 1.6680 -0.3925 -0.3307 -0.5066 142 HIS B CB  
3663 C CG  . HIS B 142 ? 1.4810 1.0477 1.6811 -0.3871 -0.3153 -0.4827 142 HIS B CG  
3664 N ND1 . HIS B 142 ? 1.4606 0.9924 1.6599 -0.3854 -0.3009 -0.4702 142 HIS B ND1 
3665 C CD2 . HIS B 142 ? 1.4827 1.0910 1.6957 -0.3828 -0.3127 -0.4694 142 HIS B CD2 
3666 C CE1 . HIS B 142 ? 1.4119 0.9636 1.6222 -0.3810 -0.2899 -0.4501 142 HIS B CE1 
3667 N NE2 . HIS B 142 ? 1.3486 0.9468 1.5679 -0.3794 -0.2964 -0.4496 142 HIS B NE2 
3668 N N   . LYS B 143 ? 1.7259 1.1834 1.8702 -0.3709 -0.3164 -0.5208 143 LYS B N   
3669 C CA  . LYS B 143 ? 1.7905 1.2049 1.9247 -0.3600 -0.3044 -0.5167 143 LYS B CA  
3670 C C   . LYS B 143 ? 1.6917 1.1094 1.8430 -0.3607 -0.2902 -0.4898 143 LYS B C   
3671 O O   . LYS B 143 ? 1.6944 1.1308 1.8721 -0.3801 -0.2892 -0.4748 143 LYS B O   
3672 C CB  . LYS B 143 ? 1.9483 1.3191 2.0868 -0.3746 -0.3085 -0.5268 143 LYS B CB  
3673 C CG  . LYS B 143 ? 2.0516 1.4069 2.1665 -0.3680 -0.3195 -0.5552 143 LYS B CG  
3674 C CD  . LYS B 143 ? 2.0939 1.4381 2.1778 -0.3388 -0.3127 -0.5646 143 LYS B CD  
3675 C CE  . LYS B 143 ? 2.1422 1.4475 2.2274 -0.3288 -0.2996 -0.5543 143 LYS B CE  
3676 N NZ  . LYS B 143 ? 2.2141 1.5144 2.2726 -0.3000 -0.2916 -0.5621 143 LYS B NZ  
3677 N N   . CYS B 144 ? 1.5665 0.9666 1.7025 -0.3396 -0.2791 -0.4843 144 CYS B N   
3678 C CA  . CYS B 144 ? 1.5011 0.9037 1.6488 -0.3368 -0.2656 -0.4594 144 CYS B CA  
3679 C C   . CYS B 144 ? 1.6509 1.0101 1.7858 -0.3211 -0.2566 -0.4578 144 CYS B C   
3680 O O   . CYS B 144 ? 1.5607 0.9199 1.6752 -0.2971 -0.2522 -0.4641 144 CYS B O   
3681 C CB  . CYS B 144 ? 1.4996 0.9454 1.6434 -0.3233 -0.2624 -0.4520 144 CYS B CB  
3682 S SG  . CYS B 144 ? 1.4646 0.9191 1.6232 -0.3207 -0.2466 -0.4221 144 CYS B SG  
3683 N N   . ASN B 145 ? 1.8328 1.1557 1.9799 -0.3347 -0.2539 -0.4493 145 ASN B N   
3684 C CA  . ASN B 145 ? 1.8444 1.1249 1.9829 -0.3203 -0.2464 -0.4457 145 ASN B CA  
3685 C C   . ASN B 145 ? 1.7595 1.0486 1.9027 -0.3113 -0.2340 -0.4214 145 ASN B C   
3686 O O   . ASN B 145 ? 1.6398 0.9679 1.7903 -0.3139 -0.2308 -0.4100 145 ASN B O   
3687 C CB  . ASN B 145 ? 1.8840 1.1207 2.0326 -0.3384 -0.2492 -0.4453 145 ASN B CB  
3688 C CG  . ASN B 145 ? 1.9199 1.1637 2.0921 -0.3671 -0.2465 -0.4249 145 ASN B CG  
3689 O OD1 . ASN B 145 ? 1.8594 1.1442 2.0434 -0.3801 -0.2487 -0.4214 145 ASN B OD1 
3690 N ND2 . ASN B 145 ? 2.0148 1.2193 2.1941 -0.3771 -0.2413 -0.4113 145 ASN B ND2 
3691 N N   . ASP B 146 ? 1.7599 1.0124 1.8993 -0.2999 -0.2273 -0.4135 146 ASP B N   
3692 C CA  . ASP B 146 ? 1.5266 0.7839 1.6693 -0.2909 -0.2162 -0.3904 146 ASP B CA  
3693 C C   . ASP B 146 ? 1.4902 0.7613 1.6529 -0.3154 -0.2117 -0.3670 146 ASP B C   
3694 O O   . ASP B 146 ? 1.5647 0.8611 1.7314 -0.3118 -0.2039 -0.3503 146 ASP B O   
3695 C CB  . ASP B 146 ? 1.5898 0.8024 1.7264 -0.2758 -0.2122 -0.3864 146 ASP B CB  
3696 C CG  . ASP B 146 ? 1.6861 0.8893 1.8044 -0.2498 -0.2145 -0.4093 146 ASP B CG  
3697 O OD1 . ASP B 146 ? 1.6225 0.8489 1.7304 -0.2463 -0.2196 -0.4292 146 ASP B OD1 
3698 O OD2 . ASP B 146 ? 1.7459 0.9193 1.8601 -0.2330 -0.2111 -0.4076 146 ASP B OD2 
3699 N N   . GLU B 147 ? 1.5722 0.8279 1.7474 -0.3410 -0.2157 -0.3660 147 GLU B N   
3700 C CA  . GLU B 147 ? 1.5998 0.8729 1.7943 -0.3670 -0.2104 -0.3460 147 GLU B CA  
3701 C C   . GLU B 147 ? 1.4804 0.8100 1.6833 -0.3704 -0.2117 -0.3465 147 GLU B C   
3702 O O   . GLU B 147 ? 1.4282 0.7830 1.6412 -0.3753 -0.2032 -0.3275 147 GLU B O   
3703 C CB  . GLU B 147 ? 1.7429 0.9919 1.9485 -0.3944 -0.2152 -0.3493 147 GLU B CB  
3704 C CG  . GLU B 147 ? 1.7032 0.9799 1.9301 -0.4247 -0.2115 -0.3354 147 GLU B CG  
3705 C CD  . GLU B 147 ? 1.9368 1.1918 2.1742 -0.4520 -0.2169 -0.3422 147 GLU B CD  
3706 O OE1 . GLU B 147 ? 1.9510 1.1617 2.1789 -0.4477 -0.2221 -0.3534 147 GLU B OE1 
3707 O OE2 . GLU B 147 ? 2.0153 1.2981 2.2712 -0.4778 -0.2161 -0.3368 147 GLU B OE2 
3708 N N   . CYS B 148 ? 1.4429 0.7930 1.6416 -0.3671 -0.2226 -0.3684 148 CYS B N   
3709 C CA  . CYS B 148 ? 1.4157 0.8189 1.6228 -0.3691 -0.2260 -0.3702 148 CYS B CA  
3710 C C   . CYS B 148 ? 1.5195 0.9454 1.7154 -0.3446 -0.2199 -0.3652 148 CYS B C   
3711 O O   . CYS B 148 ? 1.3807 0.8448 1.5886 -0.3474 -0.2162 -0.3536 148 CYS B O   
3712 C CB  . CYS B 148 ? 1.4590 0.8746 1.6616 -0.3712 -0.2405 -0.3950 148 CYS B CB  
3713 S SG  . CYS B 148 ? 1.3934 0.8657 1.5919 -0.3578 -0.2469 -0.4036 148 CYS B SG  
3714 N N   . MET B 149 ? 1.5381 0.9421 1.7120 -0.3204 -0.2187 -0.3743 149 MET B N   
3715 C CA  . MET B 149 ? 1.3523 0.7749 1.5147 -0.2975 -0.2119 -0.3695 149 MET B CA  
3716 C C   . MET B 149 ? 1.3465 0.7719 1.5210 -0.3008 -0.2001 -0.3432 149 MET B C   
3717 O O   . MET B 149 ? 1.3834 0.8445 1.5637 -0.2979 -0.1961 -0.3339 149 MET B O   
3718 C CB  . MET B 149 ? 1.3979 0.7929 1.5368 -0.2730 -0.2108 -0.3831 149 MET B CB  
3719 C CG  . MET B 149 ? 1.4799 0.8774 1.6018 -0.2662 -0.2207 -0.4099 149 MET B CG  
3720 S SD  . MET B 149 ? 1.2857 0.7358 1.3972 -0.2580 -0.2252 -0.4181 149 MET B SD  
3721 C CE  . MET B 149 ? 1.3291 0.7677 1.4124 -0.2465 -0.2340 -0.4488 149 MET B CE  
3722 N N   . GLU B 150 ? 1.2793 0.6664 1.4568 -0.3071 -0.1948 -0.3308 150 GLU B N   
3723 C CA  . GLU B 150 ? 1.2562 0.6433 1.4430 -0.3126 -0.1838 -0.3049 150 GLU B CA  
3724 C C   . GLU B 150 ? 1.2375 0.6575 1.4459 -0.3376 -0.1815 -0.2926 150 GLU B C   
3725 O O   . GLU B 150 ? 1.2826 0.7188 1.4984 -0.3402 -0.1720 -0.2732 150 GLU B O   
3726 C CB  . GLU B 150 ? 1.2978 0.6349 1.4818 -0.3156 -0.1800 -0.2941 150 GLU B CB  
3727 C CG  . GLU B 150 ? 1.3376 0.6430 1.5038 -0.2894 -0.1816 -0.3048 150 GLU B CG  
3728 C CD  . GLU B 150 ? 1.4896 0.8141 1.6459 -0.2645 -0.1760 -0.3019 150 GLU B CD  
3729 O OE1 . GLU B 150 ? 1.5495 0.8941 1.7123 -0.2672 -0.1684 -0.2829 150 GLU B OE1 
3730 O OE2 . GLU B 150 ? 1.5567 0.8768 1.6985 -0.2426 -0.1785 -0.3193 150 GLU B OE2 
3731 N N   . SER B 151 ? 1.3195 0.7511 1.5388 -0.3560 -0.1897 -0.3039 151 SER B N   
3732 C CA  . SER B 151 ? 1.3118 0.7829 1.5540 -0.3777 -0.1882 -0.2951 151 SER B CA  
3733 C C   . SER B 151 ? 1.3368 0.8571 1.5826 -0.3647 -0.1897 -0.2982 151 SER B C   
3734 O O   . SER B 151 ? 1.2696 0.8232 1.5328 -0.3740 -0.1834 -0.2844 151 SER B O   
3735 C CB  . SER B 151 ? 1.2904 0.7627 1.5446 -0.4000 -0.1979 -0.3075 151 SER B CB  
3736 O OG  . SER B 151 ? 1.3126 0.8063 1.5618 -0.3898 -0.2107 -0.3298 151 SER B OG  
3737 N N   . VAL B 152 ? 1.3556 0.8811 1.5843 -0.3435 -0.1975 -0.3164 152 VAL B N   
3738 C CA  . VAL B 152 ? 1.1723 0.7407 1.4008 -0.3298 -0.1989 -0.3194 152 VAL B CA  
3739 C C   . VAL B 152 ? 1.0917 0.6615 1.3144 -0.3146 -0.1869 -0.3036 152 VAL B C   
3740 O O   . VAL B 152 ? 1.0494 0.6559 1.2827 -0.3128 -0.1831 -0.2954 152 VAL B O   
3741 C CB  . VAL B 152 ? 1.1392 0.7108 1.3468 -0.3131 -0.2102 -0.3430 152 VAL B CB  
3742 C CG1 . VAL B 152 ? 1.0941 0.7071 1.2980 -0.2986 -0.2118 -0.3449 152 VAL B CG1 
3743 C CG2 . VAL B 152 ? 1.1776 0.7492 1.3914 -0.3289 -0.2229 -0.3585 152 VAL B CG2 
3744 N N   . LYS B 153 ? 1.2332 0.7637 1.4400 -0.3032 -0.1813 -0.2995 153 LYS B N   
3745 C CA  . LYS B 153 ? 1.1607 0.6910 1.3605 -0.2870 -0.1711 -0.2859 153 LYS B CA  
3746 C C   . LYS B 153 ? 1.1681 0.7128 1.3867 -0.3022 -0.1610 -0.2622 153 LYS B C   
3747 O O   . LYS B 153 ? 1.3305 0.9068 1.5547 -0.2960 -0.1558 -0.2546 153 LYS B O   
3748 C CB  . LYS B 153 ? 1.1906 0.6756 1.3726 -0.2723 -0.1682 -0.2863 153 LYS B CB  
3749 C CG  . LYS B 153 ? 1.1799 0.6558 1.3411 -0.2528 -0.1749 -0.3095 153 LYS B CG  
3750 C CD  . LYS B 153 ? 1.1876 0.6218 1.3354 -0.2375 -0.1714 -0.3100 153 LYS B CD  
3751 C CE  . LYS B 153 ? 1.2030 0.6316 1.3304 -0.2182 -0.1760 -0.3340 153 LYS B CE  
3752 N NZ  . LYS B 153 ? 1.2387 0.6286 1.3570 -0.2030 -0.1729 -0.3360 153 LYS B NZ  
3753 N N   . ASN B 154 ? 1.2976 0.8198 1.5253 -0.3227 -0.1575 -0.2504 154 ASN B N   
3754 C CA  . ASN B 154 ? 1.3198 0.8534 1.5620 -0.3387 -0.1462 -0.2272 154 ASN B CA  
3755 C C   . ASN B 154 ? 1.3172 0.8977 1.5840 -0.3575 -0.1464 -0.2267 154 ASN B C   
3756 O O   . ASN B 154 ? 1.3884 0.9802 1.6690 -0.3755 -0.1366 -0.2090 154 ASN B O   
3757 C CB  . ASN B 154 ? 1.4431 0.9334 1.6823 -0.3541 -0.1411 -0.2137 154 ASN B CB  
3758 C CG  . ASN B 154 ? 1.7087 1.1837 1.9540 -0.3731 -0.1487 -0.2250 154 ASN B CG  
3759 O OD1 . ASN B 154 ? 1.8406 1.3412 2.0947 -0.3774 -0.1578 -0.2415 154 ASN B OD1 
3760 N ND2 . ASN B 154 ? 1.8589 1.2914 2.0995 -0.3845 -0.1453 -0.2161 154 ASN B ND2 
3761 N N   . GLY B 155 ? 1.0379 0.6465 1.3100 -0.3534 -0.1573 -0.2455 155 GLY B N   
3762 C CA  . GLY B 155 ? 1.0166 0.6738 1.3142 -0.3671 -0.1590 -0.2464 155 GLY B CA  
3763 C C   . GLY B 155 ? 1.1302 0.7875 1.4466 -0.3965 -0.1589 -0.2420 155 GLY B C   
3764 O O   . GLY B 155 ? 1.1540 0.8425 1.4926 -0.4125 -0.1513 -0.2298 155 GLY B O   
3765 N N   . THR B 156 ? 1.1573 0.7808 1.4655 -0.4043 -0.1667 -0.2524 156 THR B N   
3766 C CA  . THR B 156 ? 1.2534 0.8732 1.5777 -0.4335 -0.1677 -0.2501 156 THR B CA  
3767 C C   . THR B 156 ? 1.1659 0.7799 1.4891 -0.4360 -0.1835 -0.2729 156 THR B C   
3768 O O   . THR B 156 ? 1.2139 0.7966 1.5359 -0.4527 -0.1861 -0.2758 156 THR B O   
3769 C CB  . THR B 156 ? 1.3248 0.8975 1.6388 -0.4469 -0.1573 -0.2339 156 THR B CB  
3770 O OG1 . THR B 156 ? 1.3603 0.8863 1.6490 -0.4276 -0.1603 -0.2406 156 THR B OG1 
3771 C CG2 . THR B 156 ? 1.2602 0.8440 1.5777 -0.4511 -0.1413 -0.2095 156 THR B CG2 
3772 N N   . TYR B 157 ? 1.1611 0.8043 1.4835 -0.4198 -0.1943 -0.2894 157 TYR B N   
3773 C CA  . TYR B 157 ? 1.1734 0.8128 1.4919 -0.4207 -0.2100 -0.3116 157 TYR B CA  
3774 C C   . TYR B 157 ? 1.2577 0.9255 1.6050 -0.4467 -0.2158 -0.3138 157 TYR B C   
3775 O O   . TYR B 157 ? 1.2566 0.9669 1.6288 -0.4552 -0.2114 -0.3041 157 TYR B O   
3776 C CB  . TYR B 157 ? 1.1469 0.8086 1.4518 -0.3956 -0.2196 -0.3272 157 TYR B CB  
3777 C CG  . TYR B 157 ? 1.2810 0.9444 1.5804 -0.3963 -0.2365 -0.3501 157 TYR B CG  
3778 C CD1 . TYR B 157 ? 1.3105 0.9312 1.5866 -0.3910 -0.2418 -0.3639 157 TYR B CD1 
3779 C CD2 . TYR B 157 ? 1.3939 1.1018 1.7114 -0.4014 -0.2475 -0.3582 157 TYR B CD2 
3780 C CE1 . TYR B 157 ? 1.3588 0.9810 1.6283 -0.3921 -0.2570 -0.3852 157 TYR B CE1 
3781 C CE2 . TYR B 157 ? 1.4444 1.1536 1.7553 -0.4022 -0.2637 -0.3787 157 TYR B CE2 
3782 C CZ  . TYR B 157 ? 1.4414 1.1074 1.7274 -0.3981 -0.2682 -0.3922 157 TYR B CZ  
3783 O OH  . TYR B 157 ? 1.5591 1.2262 1.8371 -0.3994 -0.2841 -0.4130 157 TYR B OH  
3784 N N   . ASP B 158 ? 1.3942 1.0396 1.7392 -0.4589 -0.2258 -0.3274 158 ASP B N   
3785 C CA  . ASP B 158 ? 1.4538 1.1215 1.8255 -0.4850 -0.2326 -0.3311 158 ASP B CA  
3786 C C   . ASP B 158 ? 1.5117 1.2065 1.8852 -0.4765 -0.2507 -0.3532 158 ASP B C   
3787 O O   . ASP B 158 ? 1.3686 1.0360 1.7209 -0.4684 -0.2608 -0.3706 158 ASP B O   
3788 C CB  . ASP B 158 ? 1.4107 1.0330 1.7792 -0.5075 -0.2312 -0.3301 158 ASP B CB  
3789 C CG  . ASP B 158 ? 1.3926 1.0379 1.7914 -0.5395 -0.2325 -0.3259 158 ASP B CG  
3790 O OD1 . ASP B 158 ? 1.3738 1.0651 1.7943 -0.5423 -0.2427 -0.3351 158 ASP B OD1 
3791 O OD2 . ASP B 158 ? 1.3714 0.9889 1.7721 -0.5620 -0.2233 -0.3132 158 ASP B OD2 
3792 N N   . TYR B 159 ? 1.5913 1.3400 1.9897 -0.4779 -0.2547 -0.3528 159 TYR B N   
3793 C CA  . TYR B 159 ? 1.5802 1.3579 1.9799 -0.4684 -0.2724 -0.3722 159 TYR B CA  
3794 C C   . TYR B 159 ? 1.6324 1.4078 2.0453 -0.4900 -0.2856 -0.3857 159 TYR B C   
3795 O O   . TYR B 159 ? 1.8101 1.5706 2.2039 -0.4824 -0.2994 -0.4048 159 TYR B O   
3796 C CB  . TYR B 159 ? 1.4943 1.3298 1.9170 -0.4605 -0.2729 -0.3672 159 TYR B CB  
3797 C CG  . TYR B 159 ? 1.5320 1.4021 1.9632 -0.4561 -0.2923 -0.3848 159 TYR B CG  
3798 C CD1 . TYR B 159 ? 1.5055 1.3693 1.9066 -0.4338 -0.3045 -0.3996 159 TYR B CD1 
3799 C CD2 . TYR B 159 ? 1.5643 1.4739 2.0329 -0.4743 -0.2985 -0.3862 159 TYR B CD2 
3800 C CE1 . TYR B 159 ? 1.5136 1.4074 1.9194 -0.4299 -0.3231 -0.4145 159 TYR B CE1 
3801 C CE2 . TYR B 159 ? 1.5410 1.4820 2.0177 -0.4696 -0.3175 -0.4019 159 TYR B CE2 
3802 C CZ  . TYR B 159 ? 1.5065 1.4384 1.9506 -0.4474 -0.3302 -0.4157 159 TYR B CZ  
3803 O OH  . TYR B 159 ? 1.4795 1.4411 1.9288 -0.4428 -0.3499 -0.4303 159 TYR B OH  
3804 N N   . PRO B 160 ? 1.5599 1.3499 2.0040 -0.5175 -0.2820 -0.3772 160 PRO B N   
3805 C CA  . PRO B 160 ? 1.6098 1.3984 2.0669 -0.5386 -0.2955 -0.3911 160 PRO B CA  
3806 C C   . PRO B 160 ? 1.5894 1.3187 2.0208 -0.5448 -0.2978 -0.4002 160 PRO B C   
3807 O O   . PRO B 160 ? 1.7029 1.4266 2.1359 -0.5547 -0.3122 -0.4174 160 PRO B O   
3808 C CB  . PRO B 160 ? 1.5984 1.4139 2.0936 -0.5669 -0.2872 -0.3761 160 PRO B CB  
3809 C CG  . PRO B 160 ? 1.5716 1.4200 2.0783 -0.5558 -0.2738 -0.3591 160 PRO B CG  
3810 C CD  . PRO B 160 ? 1.4582 1.2718 1.9286 -0.5313 -0.2663 -0.3555 160 PRO B CD  
3811 N N   . LYS B 161 ? 1.6136 1.2986 2.0223 -0.5386 -0.2846 -0.3899 161 LYS B N   
3812 C CA  . LYS B 161 ? 1.5804 1.2076 1.9665 -0.5427 -0.2860 -0.3986 161 LYS B CA  
3813 C C   . LYS B 161 ? 1.5917 1.2045 1.9512 -0.5215 -0.3000 -0.4221 161 LYS B C   
3814 O O   . LYS B 161 ? 1.8782 1.4470 2.2214 -0.5248 -0.3039 -0.4338 161 LYS B O   
3815 C CB  . LYS B 161 ? 1.5049 1.0909 1.8741 -0.5376 -0.2687 -0.3813 161 LYS B CB  
3816 C CG  . LYS B 161 ? 1.5299 1.0567 1.8858 -0.5500 -0.2669 -0.3844 161 LYS B CG  
3817 C CD  . LYS B 161 ? 1.5019 0.9888 1.8397 -0.5397 -0.2513 -0.3682 161 LYS B CD  
3818 C CE  . LYS B 161 ? 1.6667 1.0928 1.9912 -0.5481 -0.2506 -0.3730 161 LYS B CE  
3819 N NZ  . LYS B 161 ? 1.5909 0.9774 1.8982 -0.5348 -0.2371 -0.3581 161 LYS B NZ  
3820 N N   . TYR B 162 ? 1.4236 1.0714 1.7772 -0.5003 -0.3074 -0.4296 162 TYR B N   
3821 C CA  . TYR B 162 ? 1.4407 1.0776 1.7661 -0.4814 -0.3204 -0.4515 162 TYR B CA  
3822 C C   . TYR B 162 ? 1.4271 1.1118 1.7610 -0.4771 -0.3366 -0.4636 162 TYR B C   
3823 O O   . TYR B 162 ? 1.4343 1.1168 1.7416 -0.4590 -0.3468 -0.4797 162 TYR B O   
3824 C CB  . TYR B 162 ? 1.4388 1.0560 1.7327 -0.4525 -0.3119 -0.4493 162 TYR B CB  
3825 C CG  . TYR B 162 ? 1.4588 1.0279 1.7426 -0.4524 -0.2972 -0.4381 162 TYR B CG  
3826 C CD1 . TYR B 162 ? 1.4809 1.0014 1.7460 -0.4521 -0.2996 -0.4508 162 TYR B CD1 
3827 C CD2 . TYR B 162 ? 1.4883 1.0605 1.7810 -0.4519 -0.2814 -0.4152 162 TYR B CD2 
3828 C CE1 . TYR B 162 ? 1.5185 0.9944 1.7752 -0.4504 -0.2873 -0.4405 162 TYR B CE1 
3829 C CE2 . TYR B 162 ? 1.4681 0.9957 1.7506 -0.4512 -0.2691 -0.4043 162 TYR B CE2 
3830 C CZ  . TYR B 162 ? 1.5351 1.0146 1.8002 -0.4500 -0.2724 -0.4168 162 TYR B CZ  
3831 O OH  . TYR B 162 ? 1.4783 0.9130 1.7344 -0.4477 -0.2612 -0.4059 162 TYR B OH  
3832 N N   . SER B 163 ? 1.6660 1.3941 2.0353 -0.4928 -0.3392 -0.4563 163 SER B N   
3833 C CA  . SER B 163 ? 1.7172 1.4924 2.0965 -0.4867 -0.3551 -0.4667 163 SER B CA  
3834 C C   . SER B 163 ? 1.8230 1.5891 2.1939 -0.4939 -0.3741 -0.4896 163 SER B C   
3835 O O   . SER B 163 ? 1.9751 1.7593 2.3306 -0.4792 -0.3885 -0.5032 163 SER B O   
3836 C CB  . SER B 163 ? 1.7073 1.5315 2.1305 -0.5020 -0.3528 -0.4541 163 SER B CB  
3837 O OG  . SER B 163 ? 1.9433 1.7602 2.3918 -0.5322 -0.3520 -0.4524 163 SER B OG  
3838 N N   . GLU B 164 ? 1.6051 1.3424 1.9844 -0.5171 -0.3747 -0.4940 164 GLU B N   
3839 C CA  . GLU B 164 ? 1.6375 1.3620 2.0078 -0.5247 -0.3923 -0.5167 164 GLU B CA  
3840 C C   . GLU B 164 ? 1.5639 1.2548 1.8889 -0.5017 -0.3961 -0.5320 164 GLU B C   
3841 O O   . GLU B 164 ? 1.5784 1.2819 1.8869 -0.4922 -0.4120 -0.5493 164 GLU B O   
3842 C CB  . GLU B 164 ? 1.7938 1.4880 2.1800 -0.5542 -0.3901 -0.5171 164 GLU B CB  
3843 C CG  . GLU B 164 ? 1.8298 1.5398 2.2515 -0.5761 -0.3767 -0.4953 164 GLU B CG  
3844 C CD  . GLU B 164 ? 1.7829 1.5533 2.2435 -0.5877 -0.3851 -0.4932 164 GLU B CD  
3845 O OE1 . GLU B 164 ? 1.6837 1.4750 2.1486 -0.5886 -0.4041 -0.5109 164 GLU B OE1 
3846 O OE2 . GLU B 164 ? 1.7639 1.5613 2.2509 -0.5954 -0.3728 -0.4741 164 GLU B OE2 
3847 N N   . GLU B 165 ? 1.5642 1.2130 1.8682 -0.4923 -0.3813 -0.5256 165 GLU B N   
3848 C CA  . GLU B 165 ? 1.5825 1.1984 1.8449 -0.4705 -0.3824 -0.5399 165 GLU B CA  
3849 C C   . GLU B 165 ? 1.7039 1.3501 1.9451 -0.4454 -0.3871 -0.5429 165 GLU B C   
3850 O O   . GLU B 165 ? 1.7972 1.4391 2.0098 -0.4342 -0.3986 -0.5616 165 GLU B O   
3851 C CB  . GLU B 165 ? 1.5816 1.1532 1.8318 -0.4638 -0.3643 -0.5290 165 GLU B CB  
3852 C CG  . GLU B 165 ? 1.6165 1.1450 1.8300 -0.4473 -0.3645 -0.5456 165 GLU B CG  
3853 C CD  . GLU B 165 ? 1.6237 1.1070 1.8326 -0.4445 -0.3484 -0.5348 165 GLU B CD  
3854 O OE1 . GLU B 165 ? 1.6107 1.0924 1.8439 -0.4597 -0.3386 -0.5153 165 GLU B OE1 
3855 O OE2 . GLU B 165 ? 1.6442 1.0941 1.8248 -0.4270 -0.3455 -0.5456 165 GLU B OE2 
3856 N N   . SER B 166 ? 1.5206 1.1971 1.7740 -0.4370 -0.3784 -0.5246 166 SER B N   
3857 C CA  . SER B 166 ? 1.4581 1.1613 1.6906 -0.4135 -0.3820 -0.5256 166 SER B CA  
3858 C C   . SER B 166 ? 1.5329 1.2741 1.7706 -0.4160 -0.4025 -0.5375 166 SER B C   
3859 O O   . SER B 166 ? 1.4727 1.2199 1.6792 -0.3993 -0.4117 -0.5484 166 SER B O   
3860 C CB  . SER B 166 ? 1.5407 1.2664 1.7879 -0.4054 -0.3679 -0.5031 166 SER B CB  
3861 O OG  . SER B 166 ? 1.4133 1.1034 1.6529 -0.4014 -0.3500 -0.4921 166 SER B OG  
3862 N N   . LYS B 167 ? 1.8081 1.5755 2.0844 -0.4372 -0.4098 -0.5353 167 LYS B N   
3863 C CA  . LYS B 167 ? 1.8520 1.6559 2.1365 -0.4401 -0.4307 -0.5469 167 LYS B CA  
3864 C C   . LYS B 167 ? 1.8811 1.6609 2.1388 -0.4426 -0.4457 -0.5706 167 LYS B C   
3865 O O   . LYS B 167 ? 1.8915 1.6919 2.1341 -0.4348 -0.4627 -0.5826 167 LYS B O   
3866 C CB  . LYS B 167 ? 1.8244 1.6625 2.1597 -0.4630 -0.4340 -0.5397 167 LYS B CB  
3867 C CG  . LYS B 167 ? 1.7941 1.6801 2.1451 -0.4622 -0.4542 -0.5471 167 LYS B CG  
3868 C CD  . LYS B 167 ? 1.7801 1.7055 2.1850 -0.4818 -0.4537 -0.5372 167 LYS B CD  
3869 C CE  . LYS B 167 ? 1.8075 1.7836 2.2305 -0.4773 -0.4735 -0.5434 167 LYS B CE  
3870 N NZ  . LYS B 167 ? 1.7914 1.8102 2.2694 -0.4943 -0.4715 -0.5338 167 LYS B NZ  
3871 N N   . LEU B 168 ? 1.9061 1.6413 2.1564 -0.4532 -0.4399 -0.5777 168 LEU B N   
3872 C CA  . LEU B 168 ? 2.0754 1.7839 2.2973 -0.4540 -0.4525 -0.6013 168 LEU B CA  
3873 C C   . LEU B 168 ? 1.9664 1.6589 2.1391 -0.4278 -0.4505 -0.6095 168 LEU B C   
3874 O O   . LEU B 168 ? 2.0056 1.7033 2.1517 -0.4214 -0.4654 -0.6265 168 LEU B O   
3875 C CB  . LEU B 168 ? 2.1579 1.8211 2.3860 -0.4716 -0.4462 -0.6064 168 LEU B CB  
3876 C CG  . LEU B 168 ? 2.1508 1.8235 2.4219 -0.5018 -0.4504 -0.6030 168 LEU B CG  
3877 C CD1 . LEU B 168 ? 2.1747 1.7954 2.4441 -0.5170 -0.4437 -0.6080 168 LEU B CD1 
3878 C CD2 . LEU B 168 ? 2.1651 1.8707 2.4476 -0.5119 -0.4731 -0.6181 168 LEU B CD2 
3879 N N   . ASN B 169 ? 1.8205 1.4940 1.9800 -0.4131 -0.4319 -0.5973 169 ASN B N   
3880 C CA  . ASN B 169 ? 1.7732 1.4303 1.8866 -0.3893 -0.4276 -0.6050 169 ASN B CA  
3881 C C   . ASN B 169 ? 1.6955 1.3910 1.7925 -0.3738 -0.4357 -0.6023 169 ASN B C   
3882 O O   . ASN B 169 ? 1.6703 1.3589 1.7256 -0.3587 -0.4394 -0.6141 169 ASN B O   
3883 C CB  . ASN B 169 ? 1.7087 1.3374 1.8157 -0.3780 -0.4059 -0.5923 169 ASN B CB  
3884 C CG  . ASN B 169 ? 1.7601 1.3422 1.8714 -0.3886 -0.3991 -0.5982 169 ASN B CG  
3885 O OD1 . ASN B 169 ? 1.8199 1.3691 1.9015 -0.3797 -0.3981 -0.6141 169 ASN B OD1 
3886 N ND2 . ASN B 169 ? 1.7244 1.3032 1.8724 -0.4080 -0.3943 -0.5853 169 ASN B ND2 
3887 N N   . ARG B 170 ? 1.7167 1.4521 1.8448 -0.3772 -0.4382 -0.5869 170 ARG B N   
3888 C CA  . ARG B 170 ? 1.6567 1.4280 1.7708 -0.3627 -0.4477 -0.5839 170 ARG B CA  
3889 C C   . ARG B 170 ? 1.7447 1.5307 1.8454 -0.3667 -0.4710 -0.6017 170 ARG B C   
3890 O O   . ARG B 170 ? 1.7438 1.5536 1.8236 -0.3537 -0.4809 -0.6015 170 ARG B O   
3891 C CB  . ARG B 170 ? 1.5940 1.4043 1.7479 -0.3650 -0.4448 -0.5638 170 ARG B CB  
3892 C CG  . ARG B 170 ? 1.5587 1.3865 1.6944 -0.3433 -0.4389 -0.5511 170 ARG B CG  
3893 C CD  . ARG B 170 ? 1.4590 1.3262 1.6359 -0.3455 -0.4367 -0.5329 170 ARG B CD  
3894 N NE  . ARG B 170 ? 1.4741 1.3348 1.6897 -0.3619 -0.4228 -0.5224 170 ARG B NE  
3895 C CZ  . ARG B 170 ? 1.5058 1.3944 1.7667 -0.3793 -0.4270 -0.5176 170 ARG B CZ  
3896 N NH1 . ARG B 170 ? 1.5144 1.4405 1.7903 -0.3810 -0.4454 -0.5229 170 ARG B NH1 
3897 N NH2 . ARG B 170 ? 1.4021 1.2816 1.6929 -0.3951 -0.4127 -0.5070 170 ARG B NH2 
3898 N N   . GLU B 171 ? 1.7883 1.5597 1.8995 -0.3847 -0.4801 -0.6165 171 GLU B N   
3899 C CA  . GLU B 171 ? 1.7230 1.5043 1.8218 -0.3907 -0.5027 -0.6356 171 GLU B CA  
3900 C C   . GLU B 171 ? 1.7504 1.5804 1.8615 -0.3868 -0.5193 -0.6299 171 GLU B C   
3901 O O   . GLU B 171 ? 1.7177 1.5780 1.8694 -0.3911 -0.5169 -0.6143 171 GLU B O   
3902 C CB  . GLU B 171 ? 1.7026 1.4546 1.7451 -0.3778 -0.5041 -0.6529 171 GLU B CB  
3903 C CG  . GLU B 171 ? 1.7391 1.5093 1.7435 -0.3570 -0.5076 -0.6495 171 GLU B CG  
3904 C CD  . GLU B 171 ? 1.7847 1.5231 1.7430 -0.3401 -0.4915 -0.6529 171 GLU B CD  
3905 O OE1 . GLU B 171 ? 1.7153 1.4164 1.6624 -0.3438 -0.4838 -0.6656 171 GLU B OE1 
3906 O OE2 . GLU B 171 ? 1.6776 1.4283 1.6116 -0.3232 -0.4863 -0.6429 171 GLU B OE2 
3907 C C1  . NAG C .   ? 0.6909 0.4514 0.8521 0.1280  -0.0844 -0.0289 1   NAG C C1  
3908 C C2  . NAG C .   ? 0.7487 0.5058 0.9368 0.1454  -0.0876 -0.0484 1   NAG C C2  
3909 C C3  . NAG C .   ? 0.7617 0.4748 0.9454 0.1470  -0.0985 -0.0452 1   NAG C C3  
3910 C C4  . NAG C .   ? 0.7864 0.4856 0.9461 0.1277  -0.0893 -0.0393 1   NAG C C4  
3911 C C5  . NAG C .   ? 0.7852 0.4950 0.9212 0.1109  -0.0843 -0.0207 1   NAG C C5  
3912 C C6  . NAG C .   ? 0.7950 0.5002 0.9121 0.0924  -0.0734 -0.0176 1   NAG C C6  
3913 C C7  . NAG C .   ? 0.7626 0.5197 0.9760 0.1694  -0.1155 -0.0396 1   NAG C C7  
3914 C C8  . NAG C .   ? 0.6472 0.4273 0.8914 0.1878  -0.1241 -0.0493 1   NAG C C8  
3915 N N2  . NAG C .   ? 0.7718 0.5445 0.9848 0.1625  -0.0971 -0.0537 1   NAG C N2  
3916 O O3  . NAG C .   ? 0.7416 0.4523 0.9503 0.1632  -0.0997 -0.0665 1   NAG C O3  
3917 O O4  . NAG C .   ? 0.9125 0.5682 1.0665 0.1266  -0.1012 -0.0324 1   NAG C O4  
3918 O O5  . NAG C .   ? 0.7702 0.5195 0.9121 0.1124  -0.0751 -0.0259 1   NAG C O5  
3919 O O6  . NAG C .   ? 0.7676 0.4893 0.8928 0.0933  -0.0613 -0.0369 1   NAG C O6  
3920 O O7  . NAG C .   ? 0.8634 0.5899 1.0532 0.1607  -0.1249 -0.0201 1   NAG C O7  
3921 C C1  . NAG C .   ? 0.9060 0.5520 1.0606 0.1222  -0.0936 -0.0464 2   NAG C C1  
3922 C C2  . NAG C .   ? 1.0081 0.6107 1.1469 0.1105  -0.1027 -0.0321 2   NAG C C2  
3923 C C3  . NAG C .   ? 1.0501 0.6404 1.1899 0.1051  -0.0967 -0.0471 2   NAG C C3  
3924 C C4  . NAG C .   ? 1.1274 0.7196 1.2915 0.1249  -0.0981 -0.0721 2   NAG C C4  
3925 C C5  . NAG C .   ? 0.9462 0.5838 1.1237 0.1356  -0.0878 -0.0843 2   NAG C C5  
3926 C C6  . NAG C .   ? 0.8713 0.5156 1.0748 0.1558  -0.0879 -0.1096 2   NAG C C6  
3927 C C7  . NAG C .   ? 1.2003 0.7823 1.3016 0.0880  -0.1112 0.0109  2   NAG C C7  
3928 C C8  . NAG C .   ? 1.2067 0.7966 1.2831 0.0677  -0.1038 0.0292  2   NAG C C8  
3929 N N2  . NAG C .   ? 1.1501 0.7543 1.2646 0.0918  -0.0994 -0.0106 2   NAG C N2  
3930 O O3  . NAG C .   ? 1.1020 0.6501 1.2301 0.0941  -0.1062 -0.0342 2   NAG C O3  
3931 O O4  . NAG C .   ? 1.1378 0.7227 1.3003 0.1191  -0.0913 -0.0879 2   NAG C O4  
3932 O O5  . NAG C .   ? 0.9824 0.6293 1.1612 0.1400  -0.0950 -0.0689 2   NAG C O5  
3933 O O6  . NAG C .   ? 0.9937 0.6199 1.2154 0.1734  -0.1047 -0.1074 2   NAG C O6  
3934 O O7  . NAG C .   ? 1.1413 0.6980 1.2500 0.1008  -0.1274 0.0150  2   NAG C O7  
3935 C C1  . BMA C .   ? 1.1325 0.6731 1.3017 0.1246  -0.1050 -0.0916 3   BMA C C1  
3936 C C2  . BMA C .   ? 1.0613 0.6029 1.2384 0.1285  -0.0981 -0.1184 3   BMA C C2  
3937 C C3  . BMA C .   ? 1.1259 0.6183 1.3070 0.1299  -0.1112 -0.1240 3   BMA C C3  
3938 C C4  . BMA C .   ? 1.1841 0.6354 1.3508 0.1155  -0.1242 -0.0969 3   BMA C C4  
3939 C C5  . BMA C .   ? 1.3167 0.7763 1.4749 0.1137  -0.1282 -0.0714 3   BMA C C5  
3940 C C6  . BMA C .   ? 1.3568 0.7838 1.4939 0.0936  -0.1353 -0.0444 3   BMA C C6  
3941 O O2  . BMA C .   ? 0.9670 0.5291 1.1282 0.1111  -0.0843 -0.1203 3   BMA C O2  
3942 O O3  . BMA C .   ? 1.2856 0.7791 1.4608 0.1203  -0.1027 -0.1406 3   BMA C O3  
3943 O O4  . BMA C .   ? 1.0944 0.5106 1.2655 0.1219  -0.1362 -0.0982 3   BMA C O4  
3944 O O5  . BMA C .   ? 1.2457 0.7531 1.3977 0.1080  -0.1125 -0.0709 3   BMA C O5  
3945 O O6  . BMA C .   ? 1.4033 0.8525 1.5249 0.0721  -0.1207 -0.0401 3   BMA C O6  
3946 C C1  . MAN C .   ? 1.1771 0.6783 1.3668 0.1364  -0.0990 -0.1697 4   MAN C C1  
3947 C C2  . MAN C .   ? 1.1820 0.7344 1.3773 0.1448  -0.0830 -0.1839 4   MAN C C2  
3948 C C3  . MAN C .   ? 1.3851 0.9513 1.5996 0.1656  -0.0801 -0.2082 4   MAN C C3  
3949 C C4  . MAN C .   ? 1.4016 0.9378 1.6149 0.1666  -0.0866 -0.2181 4   MAN C C4  
3950 C C5  . MAN C .   ? 1.3643 0.8616 1.5798 0.1674  -0.1044 -0.1976 4   MAN C C5  
3951 C C6  . MAN C .   ? 1.3130 0.7762 1.5274 0.1672  -0.1120 -0.2057 4   MAN C C6  
3952 O O2  . MAN C .   ? 1.2387 0.8126 1.4175 0.1305  -0.0694 -0.1917 4   MAN C O2  
3953 O O3  . MAN C .   ? 1.3176 0.9237 1.5325 0.1682  -0.0630 -0.2277 4   MAN C O3  
3954 O O4  . MAN C .   ? 1.4486 1.0036 1.6758 0.1831  -0.0806 -0.2417 4   MAN C O4  
3955 O O5  . MAN C .   ? 1.2796 0.7595 1.4800 0.1496  -0.1098 -0.1712 4   MAN C O5  
3956 O O6  . MAN C .   ? 1.2675 0.6933 1.4791 0.1636  -0.1276 -0.1831 4   MAN C O6  
3957 C C1  . NAG D .   ? 1.6418 1.3401 1.6948 0.1157  0.0128  -0.3826 1   NAG D C1  
3958 C C2  . NAG D .   ? 1.7142 1.4369 1.7851 0.1308  0.0241  -0.3850 1   NAG D C2  
3959 C C3  . NAG D .   ? 1.7152 1.4189 1.8167 0.1403  0.0133  -0.3718 1   NAG D C3  
3960 C C4  . NAG D .   ? 1.7709 1.4359 1.8793 0.1424  -0.0010 -0.3756 1   NAG D C4  
3961 C C5  . NAG D .   ? 1.7246 1.3683 1.8129 0.1254  -0.0092 -0.3743 1   NAG D C5  
3962 C C6  . NAG D .   ? 1.7584 1.3658 1.8510 0.1257  -0.0214 -0.3810 1   NAG D C6  
3963 C C7  . NAG D .   ? 1.7534 1.5422 1.8105 0.1320  0.0535  -0.3894 1   NAG D C7  
3964 C C8  . NAG D .   ? 1.6589 1.4779 1.7058 0.1249  0.0653  -0.3799 1   NAG D C8  
3965 N N2  . NAG D .   ? 1.7710 1.5273 1.8330 0.1267  0.0370  -0.3790 1   NAG D N2  
3966 O O3  . NAG D .   ? 1.6835 1.4109 1.8040 0.1553  0.0223  -0.3766 1   NAG D O3  
3967 O O4  . NAG D .   ? 1.8771 1.5209 2.0084 0.1479  -0.0128 -0.3587 1   NAG D O4  
3968 O O5  . NAG D .   ? 1.7287 1.3941 1.7906 0.1186  0.0010  -0.3884 1   NAG D O5  
3969 O O6  . NAG D .   ? 1.7441 1.3303 1.8246 0.1084  -0.0314 -0.3743 1   NAG D O6  
3970 O O7  . NAG D .   ? 1.7050 1.4985 1.7659 0.1414  0.0590  -0.4058 1   NAG D O7  
3971 C C1  . NAG D .   ? 1.9812 1.6165 2.1320 0.1644  -0.0158 -0.3684 2   NAG D C1  
3972 C C2  . NAG D .   ? 2.0126 1.6188 2.1826 0.1684  -0.0313 -0.3489 2   NAG D C2  
3973 C C3  . NAG D .   ? 2.0750 1.6692 2.2654 0.1860  -0.0368 -0.3592 2   NAG D C3  
3974 C C4  . NAG D .   ? 2.0808 1.7150 2.2835 0.2009  -0.0228 -0.3750 2   NAG D C4  
3975 C C5  . NAG D .   ? 2.0191 1.6829 2.2002 0.1940  -0.0056 -0.3923 2   NAG D C5  
3976 C C6  . NAG D .   ? 1.9761 1.6831 2.1670 0.2049  0.0106  -0.4049 2   NAG D C6  
3977 C C7  . NAG D .   ? 1.9329 1.4887 2.0965 0.1454  -0.0527 -0.3113 2   NAG D C7  
3978 C C8  . NAG D .   ? 1.8699 1.3919 2.0228 0.1275  -0.0634 -0.3001 2   NAG D C8  
3979 N N2  . NAG D .   ? 1.9957 1.5668 2.1557 0.1529  -0.0437 -0.3355 2   NAG D N2  
3980 O O3  . NAG D .   ? 2.0272 1.5960 2.2330 0.1896  -0.0516 -0.3388 2   NAG D O3  
3981 O O4  . NAG D .   ? 2.1734 1.7979 2.3939 0.2168  -0.0270 -0.3895 2   NAG D O4  
3982 O O5  . NAG D .   ? 1.9572 1.6278 2.1182 0.1775  -0.0026 -0.3797 2   NAG D O5  
3983 O O6  . NAG D .   ? 1.9486 1.6826 2.1146 0.1954  0.0267  -0.4156 2   NAG D O6  
3984 O O7  . NAG D .   ? 1.9316 1.5010 2.1065 0.1520  -0.0519 -0.2990 2   NAG D O7  
3985 C C1  . BMA D .   ? 2.1698 1.7799 2.4147 0.2283  -0.0402 -0.3759 3   BMA D C1  
3986 C C2  . BMA D .   ? 2.1599 1.7931 2.4300 0.2487  -0.0355 -0.3930 3   BMA D C2  
3987 C C3  . BMA D .   ? 2.1212 1.7327 2.4160 0.2618  -0.0530 -0.3802 3   BMA D C3  
3988 C C4  . BMA D .   ? 2.2190 1.7768 2.5063 0.2560  -0.0711 -0.3690 3   BMA D C4  
3989 C C5  . BMA D .   ? 2.2170 1.7600 2.4794 0.2343  -0.0722 -0.3504 3   BMA D C5  
3990 C C6  . BMA D .   ? 2.2149 1.7067 2.4688 0.2249  -0.0885 -0.3376 3   BMA D C6  
3991 O O2  . BMA D .   ? 2.1819 1.8094 2.4493 0.2540  -0.0316 -0.4172 3   BMA D O2  
3992 O O3  . BMA D .   ? 2.0409 1.6695 2.3612 0.2813  -0.0512 -0.3981 3   BMA D O3  
3993 O O4  . BMA D .   ? 2.2168 1.7541 2.5232 0.2668  -0.0877 -0.3544 3   BMA D O4  
3994 O O5  . BMA D .   ? 2.2187 1.7814 2.4616 0.2243  -0.0573 -0.3661 3   BMA D O5  
3995 O O6  . BMA D .   ? 2.2142 1.6920 2.4588 0.2221  -0.0863 -0.3577 3   BMA D O6  
3996 C C1  . NAG E .   ? 0.4239 1.0519 1.1756 0.0059  -0.2120 -0.1956 1   NAG E C1  
3997 C C2  . NAG E .   ? 0.5026 1.1495 1.2693 -0.0127 -0.2176 -0.2027 1   NAG E C2  
3998 C C3  . NAG E .   ? 0.5966 1.2840 1.4118 -0.0157 -0.2053 -0.2136 1   NAG E C3  
3999 C C4  . NAG E .   ? 0.6040 1.3003 1.4301 -0.0239 -0.1712 -0.2161 1   NAG E C4  
4000 C C5  . NAG E .   ? 0.4956 1.1719 1.3051 -0.0038 -0.1677 -0.2100 1   NAG E C5  
4001 C C6  . NAG E .   ? 0.5099 1.1912 1.3235 -0.0114 -0.1343 -0.2120 1   NAG E C6  
4002 C C7  . NAG E .   ? 0.6368 1.2450 1.3472 -0.0113 -0.2625 -0.1939 1   NAG E C7  
4003 C C8  . NAG E .   ? 0.7124 1.3127 1.4061 -0.0021 -0.2951 -0.1913 1   NAG E C8  
4004 N N2  . NAG E .   ? 0.5969 1.2335 1.3475 -0.0046 -0.2498 -0.1997 1   NAG E N2  
4005 O O3  . NAG E .   ? 0.7641 1.4678 1.5927 -0.0352 -0.2091 -0.2196 1   NAG E O3  
4006 O O4  . NAG E .   ? 0.8378 1.5719 1.7069 -0.0260 -0.1593 -0.2266 1   NAG E O4  
4007 O O5  . NAG E .   ? 0.4126 1.0519 1.1790 -0.0020 -0.1799 -0.1993 1   NAG E O5  
4008 O O6  . NAG E .   ? 0.6573 1.3143 1.4489 0.0045  -0.1318 -0.2054 1   NAG E O6  
4009 O O7  . NAG E .   ? 0.6573 1.2378 1.3333 -0.0242 -0.2444 -0.1874 1   NAG E O7  
4010 C C1  . NAG E .   ? 0.9411 1.6875 1.8176 -0.0546 -0.1398 -0.2300 2   NAG E C1  
4011 C C2  . NAG E .   ? 0.9464 1.7282 1.8603 -0.0593 -0.1162 -0.2393 2   NAG E C2  
4012 C C3  . NAG E .   ? 1.0009 1.7926 1.9195 -0.0906 -0.0959 -0.2407 2   NAG E C3  
4013 C C4  . NAG E .   ? 1.0821 1.8759 2.0045 -0.1029 -0.1167 -0.2419 2   NAG E C4  
4014 C C5  . NAG E .   ? 1.0528 1.8103 1.9370 -0.0958 -0.1404 -0.2339 2   NAG E C5  
4015 C C6  . NAG E .   ? 1.1286 1.8864 2.0132 -0.1050 -0.1638 -0.2362 2   NAG E C6  
4016 C C7  . NAG E .   ? 0.8431 1.6228 1.7623 -0.0213 -0.1058 -0.2414 2   NAG E C7  
4017 C C8  . NAG E .   ? 0.7147 1.4863 1.6244 -0.0134 -0.0834 -0.2410 2   NAG E C8  
4018 N N2  . NAG E .   ? 0.9227 1.6990 1.8306 -0.0479 -0.0969 -0.2384 2   NAG E N2  
4019 O O3  . NAG E .   ? 1.0228 1.8498 1.9764 -0.0950 -0.0755 -0.2497 2   NAG E O3  
4020 O O4  . NAG E .   ? 1.1227 1.9184 2.0445 -0.1330 -0.0985 -0.2414 2   NAG E O4  
4021 O O5  . NAG E .   ? 1.0551 1.8063 1.9355 -0.0664 -0.1581 -0.2320 2   NAG E O5  
4022 O O6  . NAG E .   ? 1.1601 1.9092 2.0352 -0.1340 -0.1509 -0.2352 2   NAG E O6  
4023 O O7  . NAG E .   ? 0.7786 1.5659 1.7135 -0.0046 -0.1313 -0.2440 2   NAG E O7  
4024 C C1  . NAG F .   ? 1.2123 1.1406 0.9614 -0.0017 0.0904  -0.2349 1   NAG F C1  
4025 C C2  . NAG F .   ? 1.3409 1.2881 1.0784 -0.0054 0.1097  -0.2333 1   NAG F C2  
4026 C C3  . NAG F .   ? 1.3190 1.2789 1.0725 0.0026  0.1252  -0.2553 1   NAG F C3  
4027 C C4  . NAG F .   ? 1.3978 1.3488 1.1338 0.0053  0.1227  -0.2783 1   NAG F C4  
4028 C C5  . NAG F .   ? 1.3545 1.2830 1.1002 0.0078  0.1015  -0.2773 1   NAG F C5  
4029 C C6  . NAG F .   ? 1.3867 1.3042 1.1124 0.0087  0.0965  -0.2992 1   NAG F C6  
4030 C C7  . NAG F .   ? 1.2755 1.2342 1.0080 -0.0168 0.1153  -0.1977 1   NAG F C7  
4031 C C8  . NAG F .   ? 1.0235 0.9877 0.7792 -0.0175 0.1158  -0.1795 1   NAG F C8  
4032 N N2  . NAG F .   ? 1.2951 1.2492 1.0503 -0.0073 0.1113  -0.2131 1   NAG F N2  
4033 O O3  . NAG F .   ? 1.1379 1.1186 0.8800 -0.0027 0.1444  -0.2551 1   NAG F O3  
4034 O O4  . NAG F .   ? 1.6474 1.6087 1.4043 0.0151  0.1355  -0.3003 1   NAG F O4  
4035 O O5  . NAG F .   ? 1.2976 1.2185 1.0291 -0.0004 0.0883  -0.2559 1   NAG F O5  
4036 O O6  . NAG F .   ? 1.3980 1.2978 1.1164 0.0045  0.0762  -0.2929 1   NAG F O6  
4037 O O7  . NAG F .   ? 1.4350 1.3919 1.1286 -0.0248 0.1178  -0.1984 1   NAG F O7  
4038 C C1  . NAG F .   ? 1.9152 1.8917 1.6416 0.0107  0.1528  -0.3152 2   NAG F C1  
4039 C C2  . NAG F .   ? 1.9735 1.9636 1.7264 0.0227  0.1669  -0.3406 2   NAG F C2  
4040 C C3  . NAG F .   ? 2.0212 2.0291 1.7437 0.0180  0.1854  -0.3546 2   NAG F C3  
4041 C C4  . NAG F .   ? 2.0785 2.1039 1.7790 0.0043  0.1986  -0.3369 2   NAG F C4  
4042 C C5  . NAG F .   ? 2.0513 2.0586 1.7247 -0.0070 0.1830  -0.3127 2   NAG F C5  
4043 C C6  . NAG F .   ? 1.9853 2.0045 1.6405 -0.0202 0.1930  -0.2916 2   NAG F C6  
4044 C C7  . NAG F .   ? 2.0334 2.0038 1.8474 0.0474  0.1542  -0.3670 2   NAG F C7  
4045 C C8  . NAG F .   ? 2.0632 2.0081 1.8899 0.0561  0.1395  -0.3821 2   NAG F C8  
4046 N N2  . NAG F .   ? 2.0137 1.9843 1.7852 0.0335  0.1542  -0.3568 2   NAG F N2  
4047 O O3  . NAG F .   ? 1.9788 2.0002 1.7334 0.0308  0.1952  -0.3703 2   NAG F O3  
4048 O O4  . NAG F .   ? 2.1196 2.1574 1.7899 -0.0013 0.2117  -0.3423 2   NAG F O4  
4049 O O5  . NAG F .   ? 2.0017 1.9941 1.7095 -0.0001 0.1649  -0.2995 2   NAG F O5  
4050 O O6  . NAG F .   ? 1.9589 1.9626 1.5674 -0.0321 0.1830  -0.2771 2   NAG F O6  
4051 O O7  . NAG F .   ? 2.0066 1.9958 1.8479 0.0524  0.1648  -0.3640 2   NAG F O7  
4052 C C1  . NAG G .   ? 1.2386 1.8144 1.9951 0.1077  -0.1689 -0.1866 412 NAG A C1  
4053 C C2  . NAG G .   ? 1.3910 1.9938 2.1854 0.1193  -0.1869 -0.1956 412 NAG A C2  
4054 C C3  . NAG G .   ? 1.4804 2.0954 2.3021 0.1349  -0.1760 -0.2058 412 NAG A C3  
4055 C C4  . NAG G .   ? 1.4469 2.0821 2.2800 0.1200  -0.1401 -0.2157 412 NAG A C4  
4056 C C5  . NAG G .   ? 1.3896 1.9996 2.1867 0.1086  -0.1254 -0.2065 412 NAG A C5  
4057 C C6  . NAG G .   ? 1.4291 2.0563 2.2308 0.0908  -0.0902 -0.2142 412 NAG A C6  
4058 C C7  . NAG G .   ? 1.4971 2.0770 2.2610 0.1231  -0.2381 -0.1805 412 NAG A C7  
4059 C C8  . NAG G .   ? 1.5460 2.0994 2.2857 0.1387  -0.2718 -0.1686 412 NAG A C8  
4060 N N2  . NAG G .   ? 1.4666 2.0468 2.2427 0.1330  -0.2206 -0.1849 412 NAG A N2  
4061 O O3  . NAG G .   ? 1.5099 2.1506 2.3660 0.1435  -0.1901 -0.2146 412 NAG A O3  
4062 O O4  . NAG G .   ? 1.4564 2.0985 2.3089 0.1354  -0.1302 -0.2253 412 NAG A O4  
4063 O O5  . NAG G .   ? 1.2458 1.8429 2.0179 0.0940  -0.1364 -0.1964 412 NAG A O5  
4064 O O6  . NAG G .   ? 1.4418 2.0489 2.2263 0.0991  -0.0758 -0.2130 412 NAG A O6  
4065 O O7  . NAG G .   ? 1.4763 2.0744 2.2459 0.1018  -0.2270 -0.1855 412 NAG A O7  
4066 C C2  . EZ7 H .   ? 0.5595 0.3172 0.6082 -0.0396 -0.0087 -0.0192 201 EZ7 B C2  
4067 C C3  . EZ7 H .   ? 0.6528 0.4069 0.7039 -0.0241 -0.0113 -0.0272 201 EZ7 B C3  
4068 C C4  . EZ7 H .   ? 0.6087 0.3542 0.6653 -0.0186 -0.0140 -0.0431 201 EZ7 B C4  
4069 C C11 . EZ7 H .   ? 0.6451 0.3847 0.7036 -0.0283 -0.0153 -0.0500 201 EZ7 B C11 
4070 C C12 . EZ7 H .   ? 0.6108 0.3544 0.6688 -0.0435 -0.0136 -0.0417 201 EZ7 B C12 
4071 C C16 . EZ7 H .   ? 0.6404 0.3685 0.7104 -0.0598 -0.0241 -0.0790 201 EZ7 B C16 
4072 C C18 . EZ7 H .   ? 0.6158 0.3233 0.6827 -0.0337 -0.0272 -0.0962 201 EZ7 B C18 
4073 C C19 . EZ7 H .   ? 0.6196 0.3184 0.6880 -0.0389 -0.0319 -0.1112 201 EZ7 B C19 
4074 C C60 . EZ7 H .   ? 0.5109 0.2858 0.5614 0.0046  -0.0120 -0.0168 201 EZ7 B C60 
4075 C C58 . EZ7 H .   ? 0.5814 0.3478 0.6343 -0.0013 -0.0114 -0.0274 201 EZ7 B C58 
4076 O O59 . EZ7 H .   ? 0.7179 0.4847 0.7765 0.0067  -0.0112 -0.0422 201 EZ7 B O59 
4077 N N7  . EZ7 H .   ? 0.6468 0.4074 0.6952 -0.0159 -0.0109 -0.0197 201 EZ7 B N7  
4078 C C1  . EZ7 H .   ? 0.5543 0.3075 0.6080 -0.0493 -0.0097 -0.0268 201 EZ7 B C1  
4079 O O13 . EZ7 H .   ? 0.6471 0.3849 0.7095 -0.0509 -0.0164 -0.0518 201 EZ7 B O13 
4080 N N10 . EZ7 H .   ? 0.7018 0.4324 0.7636 -0.0263 -0.0184 -0.0657 201 EZ7 B N10 
4081 C C9  . EZ7 H .   ? 0.6633 0.3924 0.7268 -0.0405 -0.0196 -0.0661 201 EZ7 B C9  
4082 C C17 . EZ7 H .   ? 0.6172 0.3382 0.6836 -0.0444 -0.0236 -0.0799 201 EZ7 B C17 
4083 C C15 . EZ7 H .   ? 0.6009 0.3216 0.6744 -0.0648 -0.0295 -0.0937 201 EZ7 B C15 
4084 N N14 . EZ7 H .   ? 0.6301 0.3354 0.7013 -0.0542 -0.0335 -0.1097 201 EZ7 B N14 
4085 C C23 . EZ7 H .   ? 0.6511 0.3372 0.7187 -0.0283 -0.0348 -0.1296 201 EZ7 B C23 
4086 O O24 . EZ7 H .   ? 0.6623 0.3658 0.7231 -0.0170 -0.0296 -0.1384 201 EZ7 B O24 
4087 N N27 . EZ7 H .   ? 0.6697 0.3262 0.7430 -0.0315 -0.0427 -0.1387 201 EZ7 B N27 
4088 C C28 . EZ7 H .   ? 0.6901 0.3351 0.7623 -0.0197 -0.0452 -0.1607 201 EZ7 B C28 
4089 C C29 . EZ7 H .   ? 0.7161 0.3444 0.7895 -0.0300 -0.0529 -0.1749 201 EZ7 B C29 
4090 C C26 . EZ7 H .   ? 0.7379 0.3714 0.8189 -0.0472 -0.0488 -0.1279 201 EZ7 B C26 
4091 C C25 . EZ7 H .   ? 0.7588 0.3759 0.8434 -0.0566 -0.0562 -0.1434 201 EZ7 B C25 
4092 N N30 . EZ7 H .   ? 0.7905 0.3901 0.8741 -0.0433 -0.0603 -0.1644 201 EZ7 B N30 
4093 C C40 . EZ7 H .   ? 0.8261 0.4103 0.9123 -0.0538 -0.0682 -0.1797 201 EZ7 B C40 
4094 C C52 . EZ7 H .   ? 0.8702 0.4203 0.9672 -0.0684 -0.0761 -0.1704 201 EZ7 B C52 
4095 N N56 . EZ7 H .   ? 0.8645 0.3890 0.9660 -0.0676 -0.0783 -0.1552 201 EZ7 B N56 
4096 N N53 . EZ7 H .   ? 0.9337 0.4736 1.0366 -0.0852 -0.0824 -0.1758 201 EZ7 B N53 
4097 N N54 . EZ7 H .   ? 0.8726 0.3855 0.9820 -0.0933 -0.0865 -0.1650 201 EZ7 B N54 
4098 N N55 . EZ7 H .   ? 0.9134 0.4157 1.0210 -0.0827 -0.0844 -0.1520 201 EZ7 B N55 
4099 C C57 . EZ7 H .   ? 0.9038 0.3689 1.0158 -0.0904 -0.0899 -0.1348 201 EZ7 B C57 
4100 C C44 . EZ7 H .   ? 0.9495 0.5232 1.0319 -0.0416 -0.0710 -0.2031 201 EZ7 B C44 
4101 C C43 . EZ7 H .   ? 0.9411 0.5325 1.0138 -0.0432 -0.0712 -0.2207 201 EZ7 B C43 
4102 C C42 . EZ7 H .   ? 1.0211 0.6033 1.0872 -0.0317 -0.0728 -0.2451 201 EZ7 B C42 
4103 C C41 . EZ7 H .   ? 1.0731 0.6295 1.1460 -0.0178 -0.0742 -0.2530 201 EZ7 B C41 
4104 C C46 . EZ7 H .   ? 1.1034 0.6414 1.1884 -0.0152 -0.0756 -0.2350 201 EZ7 B C46 
4105 C C45 . EZ7 H .   ? 1.0740 0.6199 1.1619 -0.0278 -0.0741 -0.2095 201 EZ7 B C45 
4106 O O   . HOH I .   ? 1.0029 1.4647 1.3348 0.1023  -0.6706 -0.1139 501 HOH A O   
4107 O O   . HOH I .   ? 0.4990 0.5216 0.5001 -0.0694 -0.0976 -0.1198 502 HOH A O   
4108 O O   . HOH I .   ? 0.7517 0.7055 0.7715 0.1401  -0.3439 0.0911  503 HOH A O   
4109 O O   . HOH I .   ? 0.7143 1.1471 1.1646 0.1048  -0.4756 -0.1109 504 HOH A O   
4110 O O   . HOH I .   ? 0.5566 0.4306 0.5712 -0.0338 -0.0126 -0.1061 505 HOH A O   
4111 O O   . HOH I .   ? 0.5707 0.4136 0.6410 0.0623  -0.0478 0.0188  506 HOH A O   
4112 O O   . HOH I .   ? 0.3942 0.3715 0.4160 0.0073  0.0229  -0.0050 507 HOH A O   
4113 O O   . HOH I .   ? 0.4670 0.5225 0.5030 -0.0664 -0.0969 -0.1014 508 HOH A O   
4114 O O   . HOH I .   ? 0.5073 0.7088 0.7550 -0.1229 -0.1417 -0.1350 509 HOH A O   
4115 O O   . HOH I .   ? 0.3860 0.4454 0.5299 0.0529  0.0707  -0.0991 510 HOH A O   
4116 O O   . HOH I .   ? 0.4950 0.5697 0.5470 -0.0298 -0.0661 -0.0517 511 HOH A O   
4117 O O   . HOH I .   ? 0.7398 0.6581 0.9113 0.1063  -0.0237 -0.0587 512 HOH A O   
4118 O O   . HOH I .   ? 0.5663 0.5061 0.4893 -0.0042 0.0476  -0.0731 513 HOH A O   
4119 O O   . HOH I .   ? 0.6920 0.8225 0.8618 -0.1060 -0.1071 -0.1127 514 HOH A O   
4120 O O   . HOH I .   ? 0.6586 0.4009 0.7069 0.1041  -0.1516 0.0830  515 HOH A O   
4121 O O   . HOH I .   ? 0.6477 0.7969 0.9548 0.1593  -0.2714 -0.0179 516 HOH A O   
4122 O O   . HOH I .   ? 0.7508 1.3339 1.3120 -0.1191 -0.4770 -0.2555 517 HOH A O   
4123 O O   . HOH I .   ? 0.6885 0.5454 0.7142 0.0168  -0.0104 0.0224  518 HOH A O   
4124 O O   . HOH I .   ? 0.6992 0.6130 0.6333 0.0016  0.0347  -0.1078 519 HOH A O   
4125 O O   . HOH I .   ? 0.7254 0.3505 0.8700 0.1398  -0.1402 0.0088  520 HOH A O   
4126 O O   . HOH I .   ? 0.7267 0.7740 0.4981 -0.0466 -0.1613 -0.1282 521 HOH A O   
4127 O O   . HOH I .   ? 0.9388 1.3188 1.1946 0.1079  -0.6177 -0.0823 522 HOH A O   
4128 O O   . HOH I .   ? 0.6716 0.7172 0.7394 -0.1083 -0.1315 -0.1474 523 HOH A O   
4129 O O   . HOH I .   ? 0.7550 0.7167 0.6703 -0.0087 0.0722  -0.0741 524 HOH A O   
4130 O O   . HOH I .   ? 0.4452 0.8637 1.0187 0.1288  -0.2579 -0.1198 525 HOH A O   
4131 O O   . HOH I .   ? 0.5476 0.5054 0.5999 0.0452  0.0637  -0.1148 526 HOH A O   
4132 O O   . HOH I .   ? 0.6318 0.7248 1.0912 0.2593  -0.2624 -0.0576 527 HOH A O   
4133 O O   . HOH I .   ? 0.4267 0.6905 0.7229 -0.0813 -0.1445 -0.1189 528 HOH A O   
4134 O O   . HOH J .   ? 0.5868 0.5746 0.6528 -0.1161 0.0298  -0.0262 301 HOH B O   
4135 O O   . HOH J .   ? 0.9230 0.8045 0.9304 -0.0187 0.0154  0.0205  302 HOH B O   
4136 O O   . HOH J .   ? 0.5284 0.5427 0.6363 -0.1212 -0.0095 -0.0575 303 HOH B O   
4137 O O   . HOH J .   ? 0.3321 0.3552 0.3649 -0.0172 0.0027  -0.0240 304 HOH B O   
4138 O O   . HOH J .   ? 0.9319 0.5974 1.1772 -0.2891 -0.1540 -0.2537 305 HOH B O   
4139 O O   . HOH J .   ? 0.5759 0.6249 0.6483 -0.0327 0.0025  -0.0330 306 HOH B O   
4140 O O   . HOH J .   ? 0.6093 0.5011 0.4507 -0.0273 -0.0692 -0.1559 307 HOH B O   
4141 O O   . HOH J .   ? 0.5513 0.6357 0.6838 -0.0791 -0.0136 -0.0567 308 HOH B O   
4142 O O   . HOH J .   ? 0.4817 0.3790 0.4978 -0.0801 -0.0377 -0.0818 309 HOH B O   
4143 O O   . HOH J .   ? 0.6784 0.7095 0.6814 -0.0084 -0.0295 -0.0196 310 HOH B O   
4144 O O   . HOH J .   ? 0.5646 0.4743 0.5442 -0.0640 0.0223  -0.0082 311 HOH B O   
4145 O O   . HOH J .   ? 0.6593 0.5853 0.5807 -0.0066 0.0245  -0.0747 312 HOH B O   
4146 O O   . HOH J .   ? 0.4728 0.3855 0.4325 -0.0266 0.0194  -0.0073 313 HOH B O   
4147 O O   . HOH J .   ? 1.2543 0.6052 1.3529 -0.1096 -0.1417 -0.3061 314 HOH B O   
4148 O O   . HOH J .   ? 1.1610 0.7220 1.0482 -0.0782 -0.1522 -0.4754 315 HOH B O   
4149 O O   . HOH J .   ? 0.5401 0.7022 0.7318 -0.0618 -0.0688 -0.0765 316 HOH B O   
4150 O O   . HOH J .   ? 0.6361 0.6562 0.6922 -0.0498 0.0106  -0.0334 317 HOH B O   
4151 O O   . HOH J .   ? 0.6156 0.3710 0.7097 -0.1631 0.0023  -0.0042 318 HOH B O   
4152 O O   . HOH J .   ? 0.6142 0.5370 0.5850 -0.0541 0.0312  -0.0039 319 HOH B O   
4153 O O   . HOH J .   ? 0.8166 0.8538 0.9556 -0.1460 -0.0967 -0.1283 320 HOH B O   
4154 O O   . HOH J .   ? 0.7394 0.8395 0.9293 -0.1437 -0.0804 -0.1120 321 HOH B O   
4155 O O   . HOH J .   ? 1.0166 0.4375 1.1310 -0.0492 -0.1044 -0.2024 322 HOH B O   
4156 O O   . HOH J .   ? 0.5449 0.5678 0.5910 -0.0228 0.0399  -0.0221 323 HOH B O   
4157 O O   . HOH J .   ? 1.0118 0.9183 1.0090 -0.1454 -0.2979 -0.3674 324 HOH B O   
# 
