data_6R71
# 
_entry.id   6R71 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.383 
_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   6R71         pdb_00006r71 10.2210/pdb6r71/pdb 
WWPDB D_1292101533 ?            ?                   
# 
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 2020-04-08 
2 'Structure model' 1 1 2021-10-06 
3 'Structure model' 1 2 2024-01-24 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
loop_
_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 2 'Structure model' 'Derived calculations'   
4 2 'Structure model' 'Structure summary'      
5 3 'Structure model' 'Data collection'        
6 3 'Structure model' 'Refinement description' 
# 
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' database_2                    
2 2 'Structure model' pdbx_contact_author           
3 2 'Structure model' pdbx_database_proc            
4 2 'Structure model' struct_conn                   
5 3 'Structure model' chem_comp_atom                
6 3 'Structure model' chem_comp_bond                
7 3 'Structure model' pdbx_initial_refinement_model 
# 
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' '_database_2.pdbx_DOI'                
2  2 'Structure model' '_database_2.pdbx_database_accession' 
3  2 'Structure model' '_struct_conn.pdbx_dist_value'        
4  2 'Structure model' '_struct_conn.ptnr1_auth_asym_id'     
5  2 'Structure model' '_struct_conn.ptnr1_auth_comp_id'     
6  2 'Structure model' '_struct_conn.ptnr1_auth_seq_id'      
7  2 'Structure model' '_struct_conn.ptnr1_label_asym_id'    
8  2 'Structure model' '_struct_conn.ptnr1_label_atom_id'    
9  2 'Structure model' '_struct_conn.ptnr1_label_comp_id'    
10 2 'Structure model' '_struct_conn.ptnr1_label_seq_id'     
11 2 'Structure model' '_struct_conn.ptnr2_auth_asym_id'     
12 2 'Structure model' '_struct_conn.ptnr2_auth_comp_id'     
13 2 'Structure model' '_struct_conn.ptnr2_auth_seq_id'      
14 2 'Structure model' '_struct_conn.ptnr2_label_asym_id'    
15 2 'Structure model' '_struct_conn.ptnr2_label_atom_id'    
16 2 'Structure model' '_struct_conn.ptnr2_label_comp_id'    
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        6R71 
_pdbx_database_status.recvd_initial_deposition_date   2019-03-28 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_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_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
PDB 'PDB entries for the same citation' 6R6F unspecified 
PDB .                                   6R6Y unspecified 
PDB .                                   6R6J unspecified 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Smirnov, A.'  1 ? 
'Manakova, E.' 2 ? 
'Grazulis, S.' 3 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   FR 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Eur.J.Med.Chem. 
_citation.journal_id_ASTM           EJMCA5 
_citation.journal_id_CSD            0493 
_citation.journal_id_ISSN           0223-5234 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            185 
_citation.language                  ? 
_citation.page_first                111825 
_citation.page_last                 111825 
_citation.title                     
'Halogenated and di-substituted benzenesulfonamides as selective inhibitors of carbonic anhydrase isoforms.' 
_citation.year                      2020 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.ejmech.2019.111825 
_citation.pdbx_database_id_PubMed   31740053 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Zaksauskas, A.'   1  ? 
primary 'Capkauskaite, E.' 2  ? 
primary 'Jezepcikas, L.'   3  ? 
primary 'Linkuviene, V.'   4  ? 
primary 'Paketuryte, V.'   5  ? 
primary 'Smirnov, A.'      6  ? 
primary 'Leitans, J.'      7  ? 
primary 'Kazaks, A.'       8  ? 
primary 'Dvinskis, E.'     9  ? 
primary 'Manakova, E.'     10 ? 
primary 'Grazulis, S.'     11 ? 
primary 'Tars, K.'         12 ? 
primary 'Matulis, D.'      13 ? 
# 
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 'Carbonic anhydrase 12'                                                      29917.318 2   4.2.1.1 ? 
'human carbonic anhydrase XII'                                          ? 
2 non-polymer syn 'ZINC ION'                                                                   65.409    2   ?       ? 
'2-(benzenesulfonyl)-4-chloro-N-(2-hydroxyethyl)-5-sulfamoyl-benzamide' ? 
3 non-polymer syn 1,2-ETHANEDIOL                                                               62.068    1   ?       ? Zn ? 
4 non-polymer syn '4-chloranyl-~{N}-(2-hydroxyethyl)-2-(phenylsulfonyl)-5-sulfamoyl-benzamide' 418.872   2   ?       ? 
1,2-ETHANEDIOL                                                          ? 
5 water       nat water                                                                        18.015    322 ?       ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Carbonate dehydratase XII,Carbonic anhydrase XII,CA-XII,Tumor antigen HOM-RCC-3.1.3' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MSKWTYFGPDGENSWSKKYPSCGGLLQSPIDLHSDILQYDASLTPLEFQGYNLSANKQFLLTNNGHSVKLNLPSDMHIQG
LQSRYSATQLHLHWGNPNDPHGSEHTVSGQHFAAELHIVHYNSDLYPDASTASNKSEGLAVLAVLIEMGSFNPSYDKIFS
HLQHVKYKGQEAFVPGFNIEELLPERTAEYYRYRGSLTTPPCNPTVLWTVFRNPVQISQEQLLALETALYCTHMDDPSPR
EMINNFRQVQKFDERLVYTSFSQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MSKWTYFGPDGENSWSKKYPSCGGLLQSPIDLHSDILQYDASLTPLEFQGYNLSANKQFLLTNNGHSVKLNLPSDMHIQG
LQSRYSATQLHLHWGNPNDPHGSEHTVSGQHFAAELHIVHYNSDLYPDASTASNKSEGLAVLAVLIEMGSFNPSYDKIFS
HLQHVKYKGQEAFVPGFNIEELLPERTAEYYRYRGSLTTPPCNPTVLWTVFRNPVQISQEQLLALETALYCTHMDDPSPR
EMINNFRQVQKFDERLVYTSFSQ
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'ZINC ION'                                                                   ZN  
3 1,2-ETHANEDIOL                                                               EDO 
4 '4-chloranyl-~{N}-(2-hydroxyethyl)-2-(phenylsulfonyl)-5-sulfamoyl-benzamide' JTW 
5 water                                                                        HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   SER n 
1 3   LYS n 
1 4   TRP n 
1 5   THR n 
1 6   TYR n 
1 7   PHE n 
1 8   GLY n 
1 9   PRO n 
1 10  ASP n 
1 11  GLY n 
1 12  GLU n 
1 13  ASN n 
1 14  SER n 
1 15  TRP n 
1 16  SER n 
1 17  LYS n 
1 18  LYS n 
1 19  TYR n 
1 20  PRO n 
1 21  SER n 
1 22  CYS n 
1 23  GLY n 
1 24  GLY n 
1 25  LEU n 
1 26  LEU n 
1 27  GLN n 
1 28  SER n 
1 29  PRO n 
1 30  ILE n 
1 31  ASP n 
1 32  LEU n 
1 33  HIS n 
1 34  SER n 
1 35  ASP n 
1 36  ILE n 
1 37  LEU n 
1 38  GLN n 
1 39  TYR n 
1 40  ASP n 
1 41  ALA n 
1 42  SER n 
1 43  LEU n 
1 44  THR n 
1 45  PRO n 
1 46  LEU n 
1 47  GLU n 
1 48  PHE n 
1 49  GLN n 
1 50  GLY n 
1 51  TYR n 
1 52  ASN n 
1 53  LEU n 
1 54  SER n 
1 55  ALA n 
1 56  ASN n 
1 57  LYS n 
1 58  GLN n 
1 59  PHE n 
1 60  LEU n 
1 61  LEU n 
1 62  THR n 
1 63  ASN n 
1 64  ASN n 
1 65  GLY n 
1 66  HIS n 
1 67  SER n 
1 68  VAL n 
1 69  LYS n 
1 70  LEU n 
1 71  ASN n 
1 72  LEU n 
1 73  PRO n 
1 74  SER n 
1 75  ASP n 
1 76  MET n 
1 77  HIS n 
1 78  ILE n 
1 79  GLN n 
1 80  GLY n 
1 81  LEU n 
1 82  GLN n 
1 83  SER n 
1 84  ARG n 
1 85  TYR n 
1 86  SER n 
1 87  ALA n 
1 88  THR n 
1 89  GLN n 
1 90  LEU n 
1 91  HIS n 
1 92  LEU n 
1 93  HIS n 
1 94  TRP n 
1 95  GLY n 
1 96  ASN n 
1 97  PRO n 
1 98  ASN n 
1 99  ASP n 
1 100 PRO n 
1 101 HIS n 
1 102 GLY n 
1 103 SER n 
1 104 GLU n 
1 105 HIS n 
1 106 THR n 
1 107 VAL n 
1 108 SER n 
1 109 GLY n 
1 110 GLN n 
1 111 HIS n 
1 112 PHE n 
1 113 ALA n 
1 114 ALA n 
1 115 GLU n 
1 116 LEU n 
1 117 HIS n 
1 118 ILE n 
1 119 VAL n 
1 120 HIS n 
1 121 TYR n 
1 122 ASN n 
1 123 SER n 
1 124 ASP n 
1 125 LEU n 
1 126 TYR n 
1 127 PRO n 
1 128 ASP n 
1 129 ALA n 
1 130 SER n 
1 131 THR n 
1 132 ALA n 
1 133 SER n 
1 134 ASN n 
1 135 LYS n 
1 136 SER n 
1 137 GLU n 
1 138 GLY n 
1 139 LEU n 
1 140 ALA n 
1 141 VAL n 
1 142 LEU n 
1 143 ALA n 
1 144 VAL n 
1 145 LEU n 
1 146 ILE n 
1 147 GLU n 
1 148 MET n 
1 149 GLY n 
1 150 SER n 
1 151 PHE n 
1 152 ASN n 
1 153 PRO n 
1 154 SER n 
1 155 TYR n 
1 156 ASP n 
1 157 LYS n 
1 158 ILE n 
1 159 PHE n 
1 160 SER n 
1 161 HIS n 
1 162 LEU n 
1 163 GLN n 
1 164 HIS n 
1 165 VAL n 
1 166 LYS n 
1 167 TYR n 
1 168 LYS n 
1 169 GLY n 
1 170 GLN n 
1 171 GLU n 
1 172 ALA n 
1 173 PHE n 
1 174 VAL n 
1 175 PRO n 
1 176 GLY n 
1 177 PHE n 
1 178 ASN n 
1 179 ILE n 
1 180 GLU n 
1 181 GLU n 
1 182 LEU n 
1 183 LEU n 
1 184 PRO n 
1 185 GLU n 
1 186 ARG n 
1 187 THR n 
1 188 ALA n 
1 189 GLU n 
1 190 TYR n 
1 191 TYR n 
1 192 ARG n 
1 193 TYR n 
1 194 ARG n 
1 195 GLY n 
1 196 SER n 
1 197 LEU n 
1 198 THR n 
1 199 THR n 
1 200 PRO n 
1 201 PRO n 
1 202 CYS n 
1 203 ASN n 
1 204 PRO n 
1 205 THR n 
1 206 VAL n 
1 207 LEU n 
1 208 TRP n 
1 209 THR n 
1 210 VAL n 
1 211 PHE n 
1 212 ARG n 
1 213 ASN n 
1 214 PRO n 
1 215 VAL n 
1 216 GLN n 
1 217 ILE n 
1 218 SER n 
1 219 GLN n 
1 220 GLU n 
1 221 GLN n 
1 222 LEU n 
1 223 LEU n 
1 224 ALA n 
1 225 LEU n 
1 226 GLU n 
1 227 THR n 
1 228 ALA n 
1 229 LEU n 
1 230 TYR n 
1 231 CYS n 
1 232 THR n 
1 233 HIS n 
1 234 MET n 
1 235 ASP n 
1 236 ASP n 
1 237 PRO n 
1 238 SER n 
1 239 PRO n 
1 240 ARG n 
1 241 GLU n 
1 242 MET n 
1 243 ILE n 
1 244 ASN n 
1 245 ASN n 
1 246 PHE n 
1 247 ARG n 
1 248 GLN n 
1 249 VAL n 
1 250 GLN n 
1 251 LYS n 
1 252 PHE n 
1 253 ASP n 
1 254 GLU n 
1 255 ARG n 
1 256 LEU n 
1 257 VAL n 
1 258 TYR n 
1 259 THR n 
1 260 SER n 
1 261 PHE n 
1 262 SER n 
1 263 GLN n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   263 
_entity_src_gen.gene_src_common_name               Human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 CA12 
_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      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_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      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_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               'Rosetta(DE3)' 
_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          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pET21a 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
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 
CYS 'L-peptide linking' y CYSTEINE                                                                     ?                 
'C3 H7 N O2 S'        121.158 
EDO non-polymer         . 1,2-ETHANEDIOL                                                               'ETHYLENE GLYCOL' 
'C2 H6 O2'            62.068  
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 
JTW non-polymer         . '4-chloranyl-~{N}-(2-hydroxyethyl)-2-(phenylsulfonyl)-5-sulfamoyl-benzamide' ?                 
'C15 H15 Cl N2 O6 S2' 418.872 
LEU 'L-peptide linking' y LEUCINE                                                                      ?                 
'C6 H13 N O2'         131.173 
LYS 'L-peptide linking' y LYSINE                                                                       ?                 
'C6 H15 N2 O2 1'      147.195 
MET 'L-peptide linking' y METHIONINE                                                                   ?                 
'C5 H11 N O2 S'       149.211 
PHE 'L-peptide linking' y PHENYLALANINE                                                                ?                 
'C9 H11 N O2'         165.189 
PRO 'L-peptide linking' y PROLINE                                                                      ?                 
'C5 H9 N O2'          115.130 
SER 'L-peptide linking' y SERINE                                                                       ?                 
'C3 H7 N O3'          105.093 
THR 'L-peptide linking' y THREONINE                                                                    ?                 
'C4 H9 N O3'          119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                                                   ?                 
'C11 H12 N2 O2'       204.225 
TYR 'L-peptide linking' y TYROSINE                                                                     ?                 
'C9 H11 N O3'         181.189 
VAL 'L-peptide linking' y VALINE                                                                       ?                 
'C5 H11 N O2'         117.146 
ZN  non-polymer         . 'ZINC ION'                                                                   ?                 'Zn 2' 
65.409  
# 
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   MET 1   1   ?   ?   ?   A . n 
A 1 2   SER 2   2   ?   ?   ?   A . n 
A 1 3   LYS 3   3   3   LYS LYS A . n 
A 1 4   TRP 4   4   4   TRP TRP A . n 
A 1 5   THR 5   5   5   THR THR A . n 
A 1 6   TYR 6   6   6   TYR TYR A . n 
A 1 7   PHE 7   7   7   PHE PHE A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   PRO 9   9   9   PRO PRO A . n 
A 1 10  ASP 10  10  10  ASP ASP A . n 
A 1 11  GLY 11  11  11  GLY GLY A . n 
A 1 12  GLU 12  12  12  GLU GLU A . n 
A 1 13  ASN 13  13  13  ASN ASN A . n 
A 1 14  SER 14  14  14  SER SER A . n 
A 1 15  TRP 15  15  15  TRP TRP A . n 
A 1 16  SER 16  16  16  SER SER A . n 
A 1 17  LYS 17  17  17  LYS LYS A . n 
A 1 18  LYS 18  18  18  LYS LYS A . n 
A 1 19  TYR 19  19  19  TYR TYR A . n 
A 1 20  PRO 20  20  20  PRO PRO A . n 
A 1 21  SER 21  21  21  SER SER A . n 
A 1 22  CYS 22  22  22  CYS CYS A . n 
A 1 23  GLY 23  23  23  GLY GLY A . n 
A 1 24  GLY 24  24  24  GLY GLY A . n 
A 1 25  LEU 25  25  25  LEU LEU A . n 
A 1 26  LEU 26  26  26  LEU LEU A . n 
A 1 27  GLN 27  27  27  GLN GLN A . n 
A 1 28  SER 28  28  28  SER SER A . n 
A 1 29  PRO 29  29  29  PRO PRO A . n 
A 1 30  ILE 30  30  30  ILE ILE A . n 
A 1 31  ASP 31  31  31  ASP ASP A . n 
A 1 32  LEU 32  32  32  LEU LEU A . n 
A 1 33  HIS 33  33  33  HIS HIS A . n 
A 1 34  SER 34  34  34  SER SER A . n 
A 1 35  ASP 35  35  35  ASP ASP A . n 
A 1 36  ILE 36  36  36  ILE ILE A . n 
A 1 37  LEU 37  37  37  LEU LEU A . n 
A 1 38  GLN 38  38  38  GLN GLN A . n 
A 1 39  TYR 39  39  39  TYR TYR A . n 
A 1 40  ASP 40  40  40  ASP ASP A . n 
A 1 41  ALA 41  41  41  ALA ALA A . n 
A 1 42  SER 42  42  42  SER SER A . n 
A 1 43  LEU 43  43  43  LEU LEU A . n 
A 1 44  THR 44  44  44  THR THR A . n 
A 1 45  PRO 45  45  45  PRO PRO A . n 
A 1 46  LEU 46  46  46  LEU LEU A . n 
A 1 47  GLU 47  47  47  GLU GLU A . n 
A 1 48  PHE 48  48  48  PHE PHE A . n 
A 1 49  GLN 49  49  49  GLN GLN A . n 
A 1 50  GLY 50  50  50  GLY GLY A . n 
A 1 51  TYR 51  51  51  TYR TYR A . n 
A 1 52  ASN 52  52  52  ASN ASN A . n 
A 1 53  LEU 53  53  53  LEU LEU A . n 
A 1 54  SER 54  54  54  SER SER A . n 
A 1 55  ALA 55  55  55  ALA ALA A . n 
A 1 56  ASN 56  56  56  ASN ASN A . n 
A 1 57  LYS 57  57  57  LYS LYS A . n 
A 1 58  GLN 58  58  58  GLN GLN A . n 
A 1 59  PHE 59  59  59  PHE PHE A . n 
A 1 60  LEU 60  60  60  LEU LEU A . n 
A 1 61  LEU 61  61  61  LEU LEU A . n 
A 1 62  THR 62  62  62  THR THR A . n 
A 1 63  ASN 63  63  63  ASN ASN A . n 
A 1 64  ASN 64  64  64  ASN ASN A . n 
A 1 65  GLY 65  65  65  GLY GLY A . n 
A 1 66  HIS 66  66  66  HIS HIS A . n 
A 1 67  SER 67  67  67  SER SER A . n 
A 1 68  VAL 68  68  68  VAL VAL A . n 
A 1 69  LYS 69  69  69  LYS LYS A . n 
A 1 70  LEU 70  70  70  LEU LEU A . n 
A 1 71  ASN 71  71  71  ASN ASN A . n 
A 1 72  LEU 72  72  72  LEU LEU A . n 
A 1 73  PRO 73  73  73  PRO PRO A . n 
A 1 74  SER 74  74  74  SER SER A . n 
A 1 75  ASP 75  75  75  ASP ASP A . n 
A 1 76  MET 76  76  76  MET MET A . n 
A 1 77  HIS 77  77  77  HIS HIS A . n 
A 1 78  ILE 78  78  78  ILE ILE A . n 
A 1 79  GLN 79  79  79  GLN GLN A . n 
A 1 80  GLY 80  80  80  GLY GLY A . n 
A 1 81  LEU 81  81  81  LEU LEU A . n 
A 1 82  GLN 82  82  82  GLN GLN A . n 
A 1 83  SER 83  83  83  SER SER A . n 
A 1 84  ARG 84  84  84  ARG ARG A . n 
A 1 85  TYR 85  85  85  TYR TYR A . n 
A 1 86  SER 86  86  86  SER SER A . n 
A 1 87  ALA 87  87  87  ALA ALA A . n 
A 1 88  THR 88  88  88  THR THR A . n 
A 1 89  GLN 89  89  89  GLN GLN A . n 
A 1 90  LEU 90  90  90  LEU LEU A . n 
A 1 91  HIS 91  91  91  HIS HIS A . n 
A 1 92  LEU 92  92  92  LEU LEU A . n 
A 1 93  HIS 93  93  93  HIS HIS A . n 
A 1 94  TRP 94  94  94  TRP TRP A . n 
A 1 95  GLY 95  95  95  GLY GLY A . n 
A 1 96  ASN 96  96  96  ASN ASN A . n 
A 1 97  PRO 97  97  97  PRO PRO A . n 
A 1 98  ASN 98  98  98  ASN ASN A . n 
A 1 99  ASP 99  99  99  ASP ASP A . n 
A 1 100 PRO 100 100 100 PRO PRO A . n 
A 1 101 HIS 101 101 101 HIS HIS A . n 
A 1 102 GLY 102 102 102 GLY GLY A . n 
A 1 103 SER 103 103 103 SER SER A . n 
A 1 104 GLU 104 104 104 GLU GLU A . n 
A 1 105 HIS 105 105 105 HIS HIS A . n 
A 1 106 THR 106 106 106 THR THR A . n 
A 1 107 VAL 107 107 107 VAL VAL A . n 
A 1 108 SER 108 108 108 SER SER A . n 
A 1 109 GLY 109 109 109 GLY GLY A . n 
A 1 110 GLN 110 110 110 GLN GLN A . n 
A 1 111 HIS 111 111 111 HIS HIS A . n 
A 1 112 PHE 112 112 112 PHE PHE A . n 
A 1 113 ALA 113 113 113 ALA ALA A . n 
A 1 114 ALA 114 114 114 ALA ALA A . n 
A 1 115 GLU 115 115 115 GLU GLU A . n 
A 1 116 LEU 116 116 116 LEU LEU A . n 
A 1 117 HIS 117 117 117 HIS HIS A . n 
A 1 118 ILE 118 118 118 ILE ILE A . n 
A 1 119 VAL 119 119 119 VAL VAL A . n 
A 1 120 HIS 120 120 120 HIS HIS A . n 
A 1 121 TYR 121 121 121 TYR TYR A . n 
A 1 122 ASN 122 122 122 ASN ASN A . n 
A 1 123 SER 123 123 123 SER SER A . n 
A 1 124 ASP 124 124 124 ASP ASP A . n 
A 1 125 LEU 125 125 125 LEU LEU A . n 
A 1 126 TYR 126 126 126 TYR TYR A . n 
A 1 127 PRO 127 127 127 PRO PRO A . n 
A 1 128 ASP 128 128 128 ASP ASP A . n 
A 1 129 ALA 129 129 129 ALA ALA A . n 
A 1 130 SER 130 130 130 SER SER A . n 
A 1 131 THR 131 131 131 THR THR A . n 
A 1 132 ALA 132 132 132 ALA ALA A . n 
A 1 133 SER 133 133 133 SER SER A . n 
A 1 134 ASN 134 134 134 ASN ASN A . n 
A 1 135 LYS 135 135 135 LYS LYS A . n 
A 1 136 SER 136 136 136 SER SER A . n 
A 1 137 GLU 137 137 137 GLU GLU A . n 
A 1 138 GLY 138 138 138 GLY GLY A . n 
A 1 139 LEU 139 139 139 LEU LEU A . n 
A 1 140 ALA 140 140 140 ALA ALA A . n 
A 1 141 VAL 141 141 141 VAL VAL A . n 
A 1 142 LEU 142 142 142 LEU LEU A . n 
A 1 143 ALA 143 143 143 ALA ALA A . n 
A 1 144 VAL 144 144 144 VAL VAL A . n 
A 1 145 LEU 145 145 145 LEU LEU A . n 
A 1 146 ILE 146 146 146 ILE ILE A . n 
A 1 147 GLU 147 147 147 GLU GLU A . n 
A 1 148 MET 148 148 148 MET MET A . n 
A 1 149 GLY 149 149 149 GLY GLY A . n 
A 1 150 SER 150 150 150 SER SER A . n 
A 1 151 PHE 151 151 151 PHE PHE A . n 
A 1 152 ASN 152 152 152 ASN ASN A . n 
A 1 153 PRO 153 153 153 PRO PRO A . n 
A 1 154 SER 154 154 154 SER SER A . n 
A 1 155 TYR 155 155 155 TYR TYR A . n 
A 1 156 ASP 156 156 156 ASP ASP A . n 
A 1 157 LYS 157 157 157 LYS LYS A . n 
A 1 158 ILE 158 158 158 ILE ILE A . n 
A 1 159 PHE 159 159 159 PHE PHE A . n 
A 1 160 SER 160 160 160 SER SER A . n 
A 1 161 HIS 161 161 161 HIS HIS A . n 
A 1 162 LEU 162 162 162 LEU LEU A . n 
A 1 163 GLN 163 163 163 GLN GLN A . n 
A 1 164 HIS 164 164 164 HIS HIS A . n 
A 1 165 VAL 165 165 165 VAL VAL A . n 
A 1 166 LYS 166 166 166 LYS LYS A . n 
A 1 167 TYR 167 167 167 TYR TYR A . n 
A 1 168 LYS 168 168 168 LYS LYS A . n 
A 1 169 GLY 169 169 169 GLY GLY A . n 
A 1 170 GLN 170 170 170 GLN GLN A . n 
A 1 171 GLU 171 171 171 GLU GLU A . n 
A 1 172 ALA 172 172 172 ALA ALA A . n 
A 1 173 PHE 173 173 173 PHE PHE A . n 
A 1 174 VAL 174 174 174 VAL VAL A . n 
A 1 175 PRO 175 175 175 PRO PRO A . n 
A 1 176 GLY 176 176 176 GLY GLY A . n 
A 1 177 PHE 177 177 177 PHE PHE A . n 
A 1 178 ASN 178 178 178 ASN ASN A . n 
A 1 179 ILE 179 179 179 ILE ILE A . n 
A 1 180 GLU 180 180 180 GLU GLU A . n 
A 1 181 GLU 181 181 181 GLU GLU A . n 
A 1 182 LEU 182 182 182 LEU LEU A . n 
A 1 183 LEU 183 183 183 LEU LEU A . n 
A 1 184 PRO 184 184 184 PRO PRO A . n 
A 1 185 GLU 185 185 185 GLU GLU A . n 
A 1 186 ARG 186 186 186 ARG ARG A . n 
A 1 187 THR 187 187 187 THR THR A . n 
A 1 188 ALA 188 188 188 ALA ALA A . n 
A 1 189 GLU 189 189 189 GLU GLU A . n 
A 1 190 TYR 190 190 190 TYR TYR A . n 
A 1 191 TYR 191 191 191 TYR TYR A . n 
A 1 192 ARG 192 192 192 ARG ARG A . n 
A 1 193 TYR 193 193 193 TYR TYR A . n 
A 1 194 ARG 194 194 194 ARG ARG A . n 
A 1 195 GLY 195 195 195 GLY GLY A . n 
A 1 196 SER 196 196 196 SER SER A . n 
A 1 197 LEU 197 197 197 LEU LEU A . n 
A 1 198 THR 198 198 198 THR THR A . n 
A 1 199 THR 199 199 199 THR THR A . n 
A 1 200 PRO 200 200 200 PRO PRO A . n 
A 1 201 PRO 201 201 201 PRO PRO A . n 
A 1 202 CYS 202 202 202 CYS CYS A . n 
A 1 203 ASN 203 203 203 ASN ASN A . n 
A 1 204 PRO 204 204 204 PRO PRO A . n 
A 1 205 THR 205 205 205 THR THR A . n 
A 1 206 VAL 206 206 206 VAL VAL A . n 
A 1 207 LEU 207 207 207 LEU LEU A . n 
A 1 208 TRP 208 208 208 TRP TRP A . n 
A 1 209 THR 209 209 209 THR THR A . n 
A 1 210 VAL 210 210 210 VAL VAL A . n 
A 1 211 PHE 211 211 211 PHE PHE A . n 
A 1 212 ARG 212 212 212 ARG ARG A . n 
A 1 213 ASN 213 213 213 ASN ASN A . n 
A 1 214 PRO 214 214 214 PRO PRO A . n 
A 1 215 VAL 215 215 215 VAL VAL A . n 
A 1 216 GLN 216 216 216 GLN GLN A . n 
A 1 217 ILE 217 217 217 ILE ILE A . n 
A 1 218 SER 218 218 218 SER SER A . n 
A 1 219 GLN 219 219 219 GLN GLN A . n 
A 1 220 GLU 220 220 220 GLU GLU A . n 
A 1 221 GLN 221 221 221 GLN GLN A . n 
A 1 222 LEU 222 222 222 LEU LEU A . n 
A 1 223 LEU 223 223 223 LEU LEU A . n 
A 1 224 ALA 224 224 224 ALA ALA A . n 
A 1 225 LEU 225 225 225 LEU LEU A . n 
A 1 226 GLU 226 226 226 GLU GLU A . n 
A 1 227 THR 227 227 227 THR THR A . n 
A 1 228 ALA 228 228 228 ALA ALA A . n 
A 1 229 LEU 229 229 229 LEU LEU A . n 
A 1 230 TYR 230 230 230 TYR TYR A . n 
A 1 231 CYS 231 231 231 CYS CYS A . n 
A 1 232 THR 232 232 232 THR THR A . n 
A 1 233 HIS 233 233 233 HIS HIS A . n 
A 1 234 MET 234 234 234 MET MET A . n 
A 1 235 ASP 235 235 235 ASP ASP A . n 
A 1 236 ASP 236 236 236 ASP ASP A . n 
A 1 237 PRO 237 237 237 PRO PRO A . n 
A 1 238 SER 238 238 238 SER SER A . n 
A 1 239 PRO 239 239 239 PRO PRO A . n 
A 1 240 ARG 240 240 240 ARG ARG A . n 
A 1 241 GLU 241 241 241 GLU GLU A . n 
A 1 242 MET 242 242 242 MET MET A . n 
A 1 243 ILE 243 243 243 ILE ILE A . n 
A 1 244 ASN 244 244 244 ASN ASN A . n 
A 1 245 ASN 245 245 245 ASN ASN A . n 
A 1 246 PHE 246 246 246 PHE PHE A . n 
A 1 247 ARG 247 247 247 ARG ARG A . n 
A 1 248 GLN 248 248 248 GLN GLN A . n 
A 1 249 VAL 249 249 249 VAL VAL A . n 
A 1 250 GLN 250 250 250 GLN GLN A . n 
A 1 251 LYS 251 251 251 LYS LYS A . n 
A 1 252 PHE 252 252 252 PHE PHE A . n 
A 1 253 ASP 253 253 253 ASP ASP A . n 
A 1 254 GLU 254 254 254 GLU GLU A . n 
A 1 255 ARG 255 255 255 ARG ARG A . n 
A 1 256 LEU 256 256 256 LEU LEU A . n 
A 1 257 VAL 257 257 257 VAL VAL A . n 
A 1 258 TYR 258 258 258 TYR TYR A . n 
A 1 259 THR 259 259 259 THR THR A . n 
A 1 260 SER 260 260 260 SER SER A . n 
A 1 261 PHE 261 261 261 PHE PHE A . n 
A 1 262 SER 262 262 262 SER SER A . n 
A 1 263 GLN 263 263 263 GLN GLN A . n 
B 1 1   MET 1   1   ?   ?   ?   B . n 
B 1 2   SER 2   2   ?   ?   ?   B . n 
B 1 3   LYS 3   3   3   LYS LYS B . n 
B 1 4   TRP 4   4   4   TRP TRP B . n 
B 1 5   THR 5   5   5   THR THR B . n 
B 1 6   TYR 6   6   6   TYR TYR B . n 
B 1 7   PHE 7   7   7   PHE PHE B . n 
B 1 8   GLY 8   8   8   GLY GLY B . n 
B 1 9   PRO 9   9   9   PRO PRO B . n 
B 1 10  ASP 10  10  10  ASP ASP B . n 
B 1 11  GLY 11  11  11  GLY GLY B . n 
B 1 12  GLU 12  12  12  GLU GLU B . n 
B 1 13  ASN 13  13  13  ASN ASN B . n 
B 1 14  SER 14  14  14  SER SER B . n 
B 1 15  TRP 15  15  15  TRP TRP B . n 
B 1 16  SER 16  16  16  SER SER B . n 
B 1 17  LYS 17  17  17  LYS LYS B . n 
B 1 18  LYS 18  18  18  LYS LYS B . n 
B 1 19  TYR 19  19  19  TYR TYR B . n 
B 1 20  PRO 20  20  20  PRO PRO B . n 
B 1 21  SER 21  21  21  SER SER B . n 
B 1 22  CYS 22  22  22  CYS CYS B . n 
B 1 23  GLY 23  23  23  GLY GLY B . n 
B 1 24  GLY 24  24  24  GLY GLY B . n 
B 1 25  LEU 25  25  25  LEU LEU B . n 
B 1 26  LEU 26  26  26  LEU LEU B . n 
B 1 27  GLN 27  27  27  GLN GLN B . n 
B 1 28  SER 28  28  28  SER SER B . n 
B 1 29  PRO 29  29  29  PRO PRO B . n 
B 1 30  ILE 30  30  30  ILE ILE B . n 
B 1 31  ASP 31  31  31  ASP ASP B . n 
B 1 32  LEU 32  32  32  LEU LEU B . n 
B 1 33  HIS 33  33  33  HIS HIS B . n 
B 1 34  SER 34  34  34  SER SER B . n 
B 1 35  ASP 35  35  35  ASP ASP B . n 
B 1 36  ILE 36  36  36  ILE ILE B . n 
B 1 37  LEU 37  37  37  LEU LEU B . n 
B 1 38  GLN 38  38  38  GLN GLN B . n 
B 1 39  TYR 39  39  39  TYR TYR B . n 
B 1 40  ASP 40  40  40  ASP ASP B . n 
B 1 41  ALA 41  41  41  ALA ALA B . n 
B 1 42  SER 42  42  42  SER SER B . n 
B 1 43  LEU 43  43  43  LEU LEU B . n 
B 1 44  THR 44  44  44  THR THR B . n 
B 1 45  PRO 45  45  45  PRO PRO B . n 
B 1 46  LEU 46  46  46  LEU LEU B . n 
B 1 47  GLU 47  47  47  GLU GLU B . n 
B 1 48  PHE 48  48  48  PHE PHE B . n 
B 1 49  GLN 49  49  49  GLN GLN B . n 
B 1 50  GLY 50  50  50  GLY GLY B . n 
B 1 51  TYR 51  51  51  TYR TYR B . n 
B 1 52  ASN 52  52  52  ASN ASN B . n 
B 1 53  LEU 53  53  53  LEU LEU B . n 
B 1 54  SER 54  54  54  SER SER B . n 
B 1 55  ALA 55  55  55  ALA ALA B . n 
B 1 56  ASN 56  56  56  ASN ASN B . n 
B 1 57  LYS 57  57  57  LYS LYS B . n 
B 1 58  GLN 58  58  58  GLN GLN B . n 
B 1 59  PHE 59  59  59  PHE PHE B . n 
B 1 60  LEU 60  60  60  LEU LEU B . n 
B 1 61  LEU 61  61  61  LEU LEU B . n 
B 1 62  THR 62  62  62  THR THR B . n 
B 1 63  ASN 63  63  63  ASN ASN B . n 
B 1 64  ASN 64  64  64  ASN ASN B . n 
B 1 65  GLY 65  65  65  GLY GLY B . n 
B 1 66  HIS 66  66  66  HIS HIS B . n 
B 1 67  SER 67  67  67  SER SER B . n 
B 1 68  VAL 68  68  68  VAL VAL B . n 
B 1 69  LYS 69  69  69  LYS LYS B . n 
B 1 70  LEU 70  70  70  LEU LEU B . n 
B 1 71  ASN 71  71  71  ASN ASN B . n 
B 1 72  LEU 72  72  72  LEU LEU B . n 
B 1 73  PRO 73  73  73  PRO PRO B . n 
B 1 74  SER 74  74  74  SER SER B . n 
B 1 75  ASP 75  75  75  ASP ASP B . n 
B 1 76  MET 76  76  76  MET MET B . n 
B 1 77  HIS 77  77  77  HIS HIS B . n 
B 1 78  ILE 78  78  78  ILE ILE B . n 
B 1 79  GLN 79  79  79  GLN GLN B . n 
B 1 80  GLY 80  80  80  GLY GLY B . n 
B 1 81  LEU 81  81  81  LEU LEU B . n 
B 1 82  GLN 82  82  82  GLN GLN B . n 
B 1 83  SER 83  83  83  SER SER B . n 
B 1 84  ARG 84  84  84  ARG ARG B . n 
B 1 85  TYR 85  85  85  TYR TYR B . n 
B 1 86  SER 86  86  86  SER SER B . n 
B 1 87  ALA 87  87  87  ALA ALA B . n 
B 1 88  THR 88  88  88  THR THR B . n 
B 1 89  GLN 89  89  89  GLN GLN B . n 
B 1 90  LEU 90  90  90  LEU LEU B . n 
B 1 91  HIS 91  91  91  HIS HIS B . n 
B 1 92  LEU 92  92  92  LEU LEU B . n 
B 1 93  HIS 93  93  93  HIS HIS B . n 
B 1 94  TRP 94  94  94  TRP TRP B . n 
B 1 95  GLY 95  95  95  GLY GLY B . n 
B 1 96  ASN 96  96  96  ASN ASN B . n 
B 1 97  PRO 97  97  97  PRO PRO B . n 
B 1 98  ASN 98  98  98  ASN ASN B . n 
B 1 99  ASP 99  99  99  ASP ASP B . n 
B 1 100 PRO 100 100 100 PRO PRO B . n 
B 1 101 HIS 101 101 101 HIS HIS B . n 
B 1 102 GLY 102 102 102 GLY GLY B . n 
B 1 103 SER 103 103 103 SER SER B . n 
B 1 104 GLU 104 104 104 GLU GLU B . n 
B 1 105 HIS 105 105 105 HIS HIS B . n 
B 1 106 THR 106 106 106 THR THR B . n 
B 1 107 VAL 107 107 107 VAL VAL B . n 
B 1 108 SER 108 108 108 SER SER B . n 
B 1 109 GLY 109 109 109 GLY GLY B . n 
B 1 110 GLN 110 110 110 GLN GLN B . n 
B 1 111 HIS 111 111 111 HIS HIS B . n 
B 1 112 PHE 112 112 112 PHE PHE B . n 
B 1 113 ALA 113 113 113 ALA ALA B . n 
B 1 114 ALA 114 114 114 ALA ALA B . n 
B 1 115 GLU 115 115 115 GLU GLU B . n 
B 1 116 LEU 116 116 116 LEU LEU B . n 
B 1 117 HIS 117 117 117 HIS HIS B . n 
B 1 118 ILE 118 118 118 ILE ILE B . n 
B 1 119 VAL 119 119 119 VAL VAL B . n 
B 1 120 HIS 120 120 120 HIS HIS B . n 
B 1 121 TYR 121 121 121 TYR TYR B . n 
B 1 122 ASN 122 122 122 ASN ASN B . n 
B 1 123 SER 123 123 123 SER SER B . n 
B 1 124 ASP 124 124 124 ASP ASP B . n 
B 1 125 LEU 125 125 125 LEU LEU B . n 
B 1 126 TYR 126 126 126 TYR TYR B . n 
B 1 127 PRO 127 127 127 PRO PRO B . n 
B 1 128 ASP 128 128 128 ASP ASP B . n 
B 1 129 ALA 129 129 129 ALA ALA B . n 
B 1 130 SER 130 130 130 SER SER B . n 
B 1 131 THR 131 131 131 THR THR B . n 
B 1 132 ALA 132 132 132 ALA ALA B . n 
B 1 133 SER 133 133 133 SER SER B . n 
B 1 134 ASN 134 134 134 ASN ASN B . n 
B 1 135 LYS 135 135 135 LYS LYS B . n 
B 1 136 SER 136 136 136 SER SER B . n 
B 1 137 GLU 137 137 137 GLU GLU B . n 
B 1 138 GLY 138 138 138 GLY GLY B . n 
B 1 139 LEU 139 139 139 LEU LEU B . n 
B 1 140 ALA 140 140 140 ALA ALA B . n 
B 1 141 VAL 141 141 141 VAL VAL B . n 
B 1 142 LEU 142 142 142 LEU LEU B . n 
B 1 143 ALA 143 143 143 ALA ALA B . n 
B 1 144 VAL 144 144 144 VAL VAL B . n 
B 1 145 LEU 145 145 145 LEU LEU B . n 
B 1 146 ILE 146 146 146 ILE ILE B . n 
B 1 147 GLU 147 147 147 GLU GLU B . n 
B 1 148 MET 148 148 148 MET MET B . n 
B 1 149 GLY 149 149 149 GLY GLY B . n 
B 1 150 SER 150 150 150 SER SER B . n 
B 1 151 PHE 151 151 151 PHE PHE B . n 
B 1 152 ASN 152 152 152 ASN ASN B . n 
B 1 153 PRO 153 153 153 PRO PRO B . n 
B 1 154 SER 154 154 154 SER SER B . n 
B 1 155 TYR 155 155 155 TYR TYR B . n 
B 1 156 ASP 156 156 156 ASP ASP B . n 
B 1 157 LYS 157 157 157 LYS LYS B . n 
B 1 158 ILE 158 158 158 ILE ILE B . n 
B 1 159 PHE 159 159 159 PHE PHE B . n 
B 1 160 SER 160 160 160 SER SER B . n 
B 1 161 HIS 161 161 161 HIS HIS B . n 
B 1 162 LEU 162 162 162 LEU LEU B . n 
B 1 163 GLN 163 163 163 GLN GLN B . n 
B 1 164 HIS 164 164 164 HIS HIS B . n 
B 1 165 VAL 165 165 165 VAL VAL B . n 
B 1 166 LYS 166 166 166 LYS LYS B . n 
B 1 167 TYR 167 167 167 TYR TYR B . n 
B 1 168 LYS 168 168 168 LYS LYS B . n 
B 1 169 GLY 169 169 169 GLY GLY B . n 
B 1 170 GLN 170 170 170 GLN GLN B . n 
B 1 171 GLU 171 171 171 GLU GLU B . n 
B 1 172 ALA 172 172 172 ALA ALA B . n 
B 1 173 PHE 173 173 173 PHE PHE B . n 
B 1 174 VAL 174 174 174 VAL VAL B . n 
B 1 175 PRO 175 175 175 PRO PRO B . n 
B 1 176 GLY 176 176 176 GLY GLY B . n 
B 1 177 PHE 177 177 177 PHE PHE B . n 
B 1 178 ASN 178 178 178 ASN ASN B . n 
B 1 179 ILE 179 179 179 ILE ILE B . n 
B 1 180 GLU 180 180 180 GLU GLU B . n 
B 1 181 GLU 181 181 181 GLU GLU B . n 
B 1 182 LEU 182 182 182 LEU LEU B . n 
B 1 183 LEU 183 183 183 LEU LEU B . n 
B 1 184 PRO 184 184 184 PRO PRO B . n 
B 1 185 GLU 185 185 185 GLU GLU B . n 
B 1 186 ARG 186 186 186 ARG ARG B . n 
B 1 187 THR 187 187 187 THR THR B . n 
B 1 188 ALA 188 188 188 ALA ALA B . n 
B 1 189 GLU 189 189 189 GLU GLU B . n 
B 1 190 TYR 190 190 190 TYR TYR B . n 
B 1 191 TYR 191 191 191 TYR TYR B . n 
B 1 192 ARG 192 192 192 ARG ARG B . n 
B 1 193 TYR 193 193 193 TYR TYR B . n 
B 1 194 ARG 194 194 194 ARG ARG B . n 
B 1 195 GLY 195 195 195 GLY GLY B . n 
B 1 196 SER 196 196 196 SER SER B . n 
B 1 197 LEU 197 197 197 LEU LEU B . n 
B 1 198 THR 198 198 198 THR THR B . n 
B 1 199 THR 199 199 199 THR THR B . n 
B 1 200 PRO 200 200 200 PRO PRO B . n 
B 1 201 PRO 201 201 201 PRO PRO B . n 
B 1 202 CYS 202 202 202 CYS CYS B . n 
B 1 203 ASN 203 203 203 ASN ASN B . n 
B 1 204 PRO 204 204 204 PRO PRO B . n 
B 1 205 THR 205 205 205 THR THR B . n 
B 1 206 VAL 206 206 206 VAL VAL B . n 
B 1 207 LEU 207 207 207 LEU LEU B . n 
B 1 208 TRP 208 208 208 TRP TRP B . n 
B 1 209 THR 209 209 209 THR THR B . n 
B 1 210 VAL 210 210 210 VAL VAL B . n 
B 1 211 PHE 211 211 211 PHE PHE B . n 
B 1 212 ARG 212 212 212 ARG ARG B . n 
B 1 213 ASN 213 213 213 ASN ASN B . n 
B 1 214 PRO 214 214 214 PRO PRO B . n 
B 1 215 VAL 215 215 215 VAL VAL B . n 
B 1 216 GLN 216 216 216 GLN GLN B . n 
B 1 217 ILE 217 217 217 ILE ILE B . n 
B 1 218 SER 218 218 218 SER SER B . n 
B 1 219 GLN 219 219 219 GLN GLN B . n 
B 1 220 GLU 220 220 220 GLU GLU B . n 
B 1 221 GLN 221 221 221 GLN GLN B . n 
B 1 222 LEU 222 222 222 LEU LEU B . n 
B 1 223 LEU 223 223 223 LEU LEU B . n 
B 1 224 ALA 224 224 224 ALA ALA B . n 
B 1 225 LEU 225 225 225 LEU LEU B . n 
B 1 226 GLU 226 226 226 GLU GLU B . n 
B 1 227 THR 227 227 227 THR THR B . n 
B 1 228 ALA 228 228 228 ALA ALA B . n 
B 1 229 LEU 229 229 229 LEU LEU B . n 
B 1 230 TYR 230 230 230 TYR TYR B . n 
B 1 231 CYS 231 231 231 CYS CYS B . n 
B 1 232 THR 232 232 232 THR THR B . n 
B 1 233 HIS 233 233 233 HIS HIS B . n 
B 1 234 MET 234 234 234 MET MET B . n 
B 1 235 ASP 235 235 235 ASP ASP B . n 
B 1 236 ASP 236 236 236 ASP ASP B . n 
B 1 237 PRO 237 237 237 PRO PRO B . n 
B 1 238 SER 238 238 238 SER SER B . n 
B 1 239 PRO 239 239 239 PRO PRO B . n 
B 1 240 ARG 240 240 240 ARG ARG B . n 
B 1 241 GLU 241 241 241 GLU GLU B . n 
B 1 242 MET 242 242 242 MET MET B . n 
B 1 243 ILE 243 243 243 ILE ILE B . n 
B 1 244 ASN 244 244 244 ASN ASN B . n 
B 1 245 ASN 245 245 245 ASN ASN B . n 
B 1 246 PHE 246 246 246 PHE PHE B . n 
B 1 247 ARG 247 247 247 ARG ARG B . n 
B 1 248 GLN 248 248 248 GLN GLN B . n 
B 1 249 VAL 249 249 249 VAL VAL B . n 
B 1 250 GLN 250 250 250 GLN GLN B . n 
B 1 251 LYS 251 251 251 LYS LYS B . n 
B 1 252 PHE 252 252 252 PHE PHE B . n 
B 1 253 ASP 253 253 253 ASP ASP B . n 
B 1 254 GLU 254 254 254 GLU GLU B . n 
B 1 255 ARG 255 255 255 ARG ARG B . n 
B 1 256 LEU 256 256 256 LEU LEU B . n 
B 1 257 VAL 257 257 257 VAL VAL B . n 
B 1 258 TYR 258 258 258 TYR TYR B . n 
B 1 259 THR 259 259 259 THR THR B . n 
B 1 260 SER 260 260 260 SER SER B . n 
B 1 261 PHE 261 261 261 PHE PHE B . n 
B 1 262 SER 262 262 262 SER SER B . n 
B 1 263 GLN 263 263 263 GLN GLN B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 ZN  1   301 1   ZN  ZN  A . 
D 3 EDO 1   302 1   EDO EDO A . 
E 4 JTW 1   303 1   JTW EAZ A . 
F 2 ZN  1   301 2   ZN  ZN  B . 
G 4 JTW 1   302 2   JTW EAZ B . 
H 5 HOH 1   401 27  HOH HOH A . 
H 5 HOH 2   402 158 HOH HOH A . 
H 5 HOH 3   403 212 HOH HOH A . 
H 5 HOH 4   404 174 HOH HOH A . 
H 5 HOH 5   405 152 HOH HOH A . 
H 5 HOH 6   406 74  HOH HOH A . 
H 5 HOH 7   407 206 HOH HOH A . 
H 5 HOH 8   408 34  HOH HOH A . 
H 5 HOH 9   409 62  HOH HOH A . 
H 5 HOH 10  410 37  HOH HOH A . 
H 5 HOH 11  411 164 HOH HOH A . 
H 5 HOH 12  412 93  HOH HOH A . 
H 5 HOH 13  413 41  HOH HOH A . 
H 5 HOH 14  414 30  HOH HOH A . 
H 5 HOH 15  415 133 HOH HOH A . 
H 5 HOH 16  416 48  HOH HOH A . 
H 5 HOH 17  417 179 HOH HOH A . 
H 5 HOH 18  418 45  HOH HOH A . 
H 5 HOH 19  419 146 HOH HOH A . 
H 5 HOH 20  420 210 HOH HOH A . 
H 5 HOH 21  421 76  HOH HOH A . 
H 5 HOH 22  422 124 HOH HOH A . 
H 5 HOH 23  423 286 HOH HOH A . 
H 5 HOH 24  424 19  HOH HOH A . 
H 5 HOH 25  425 115 HOH HOH A . 
H 5 HOH 26  426 159 HOH HOH A . 
H 5 HOH 27  427 89  HOH HOH A . 
H 5 HOH 28  428 83  HOH HOH A . 
H 5 HOH 29  429 38  HOH HOH A . 
H 5 HOH 30  430 226 HOH HOH A . 
H 5 HOH 31  431 9   HOH HOH A . 
H 5 HOH 32  432 60  HOH HOH A . 
H 5 HOH 33  433 129 HOH HOH A . 
H 5 HOH 34  434 77  HOH HOH A . 
H 5 HOH 35  435 165 HOH HOH A . 
H 5 HOH 36  436 211 HOH HOH A . 
H 5 HOH 37  437 227 HOH HOH A . 
H 5 HOH 38  438 88  HOH HOH A . 
H 5 HOH 39  439 58  HOH HOH A . 
H 5 HOH 40  440 235 HOH HOH A . 
H 5 HOH 41  441 109 HOH HOH A . 
H 5 HOH 42  442 107 HOH HOH A . 
H 5 HOH 43  443 221 HOH HOH A . 
H 5 HOH 44  444 282 HOH HOH A . 
H 5 HOH 45  445 24  HOH HOH A . 
H 5 HOH 46  446 92  HOH HOH A . 
H 5 HOH 47  447 31  HOH HOH A . 
H 5 HOH 48  448 215 HOH HOH A . 
H 5 HOH 49  449 99  HOH HOH A . 
H 5 HOH 50  450 228 HOH HOH A . 
H 5 HOH 51  451 80  HOH HOH A . 
H 5 HOH 52  452 32  HOH HOH A . 
H 5 HOH 53  453 318 HOH HOH A . 
H 5 HOH 54  454 138 HOH HOH A . 
H 5 HOH 55  455 96  HOH HOH A . 
H 5 HOH 56  456 230 HOH HOH A . 
H 5 HOH 57  457 121 HOH HOH A . 
H 5 HOH 58  458 67  HOH HOH A . 
H 5 HOH 59  459 128 HOH HOH A . 
H 5 HOH 60  460 297 HOH HOH A . 
H 5 HOH 61  461 8   HOH HOH A . 
H 5 HOH 62  462 13  HOH HOH A . 
H 5 HOH 63  463 231 HOH HOH A . 
H 5 HOH 64  464 317 HOH HOH A . 
H 5 HOH 65  465 104 HOH HOH A . 
H 5 HOH 66  466 222 HOH HOH A . 
H 5 HOH 67  467 49  HOH HOH A . 
H 5 HOH 68  468 29  HOH HOH A . 
H 5 HOH 69  469 20  HOH HOH A . 
H 5 HOH 70  470 220 HOH HOH A . 
H 5 HOH 71  471 7   HOH HOH A . 
H 5 HOH 72  472 170 HOH HOH A . 
H 5 HOH 73  473 87  HOH HOH A . 
H 5 HOH 74  474 137 HOH HOH A . 
H 5 HOH 75  475 52  HOH HOH A . 
H 5 HOH 76  476 180 HOH HOH A . 
H 5 HOH 77  477 72  HOH HOH A . 
H 5 HOH 78  478 214 HOH HOH A . 
H 5 HOH 79  479 4   HOH HOH A . 
H 5 HOH 80  480 11  HOH HOH A . 
H 5 HOH 81  481 166 HOH HOH A . 
H 5 HOH 82  482 35  HOH HOH A . 
H 5 HOH 83  483 162 HOH HOH A . 
H 5 HOH 84  484 311 HOH HOH A . 
H 5 HOH 85  485 275 HOH HOH A . 
H 5 HOH 86  486 298 HOH HOH A . 
H 5 HOH 87  487 270 HOH HOH A . 
H 5 HOH 88  488 114 HOH HOH A . 
H 5 HOH 89  489 271 HOH HOH A . 
H 5 HOH 90  490 234 HOH HOH A . 
H 5 HOH 91  491 218 HOH HOH A . 
H 5 HOH 92  492 82  HOH HOH A . 
H 5 HOH 93  493 154 HOH HOH A . 
H 5 HOH 94  494 36  HOH HOH A . 
H 5 HOH 95  495 213 HOH HOH A . 
H 5 HOH 96  496 5   HOH HOH A . 
H 5 HOH 97  497 39  HOH HOH A . 
H 5 HOH 98  498 277 HOH HOH A . 
H 5 HOH 99  499 2   HOH HOH A . 
H 5 HOH 100 500 132 HOH HOH A . 
H 5 HOH 101 501 208 HOH HOH A . 
H 5 HOH 102 502 55  HOH HOH A . 
H 5 HOH 103 503 57  HOH HOH A . 
H 5 HOH 104 504 295 HOH HOH A . 
H 5 HOH 105 505 249 HOH HOH A . 
H 5 HOH 106 506 25  HOH HOH A . 
H 5 HOH 107 507 283 HOH HOH A . 
H 5 HOH 108 508 276 HOH HOH A . 
H 5 HOH 109 509 142 HOH HOH A . 
H 5 HOH 110 510 160 HOH HOH A . 
H 5 HOH 111 511 145 HOH HOH A . 
H 5 HOH 112 512 75  HOH HOH A . 
H 5 HOH 113 513 1   HOH HOH A . 
H 5 HOH 114 514 294 HOH HOH A . 
H 5 HOH 115 515 233 HOH HOH A . 
H 5 HOH 116 516 285 HOH HOH A . 
H 5 HOH 117 517 144 HOH HOH A . 
H 5 HOH 118 518 205 HOH HOH A . 
H 5 HOH 119 519 153 HOH HOH A . 
H 5 HOH 120 520 163 HOH HOH A . 
H 5 HOH 121 521 201 HOH HOH A . 
H 5 HOH 122 522 157 HOH HOH A . 
H 5 HOH 123 523 116 HOH HOH A . 
H 5 HOH 124 524 272 HOH HOH A . 
H 5 HOH 125 525 312 HOH HOH A . 
H 5 HOH 126 526 64  HOH HOH A . 
H 5 HOH 127 527 98  HOH HOH A . 
H 5 HOH 128 528 280 HOH HOH A . 
H 5 HOH 129 529 224 HOH HOH A . 
H 5 HOH 130 530 219 HOH HOH A . 
H 5 HOH 131 531 204 HOH HOH A . 
H 5 HOH 132 532 309 HOH HOH A . 
H 5 HOH 133 533 209 HOH HOH A . 
H 5 HOH 134 534 207 HOH HOH A . 
H 5 HOH 135 535 279 HOH HOH A . 
H 5 HOH 136 536 273 HOH HOH A . 
H 5 HOH 137 537 147 HOH HOH A . 
H 5 HOH 138 538 316 HOH HOH A . 
H 5 HOH 139 539 120 HOH HOH A . 
H 5 HOH 140 540 148 HOH HOH A . 
H 5 HOH 141 541 3   HOH HOH A . 
H 5 HOH 142 542 203 HOH HOH A . 
H 5 HOH 143 543 90  HOH HOH A . 
H 5 HOH 144 544 229 HOH HOH A . 
H 5 HOH 145 545 169 HOH HOH A . 
H 5 HOH 146 546 136 HOH HOH A . 
H 5 HOH 147 547 167 HOH HOH A . 
H 5 HOH 148 548 278 HOH HOH A . 
H 5 HOH 149 549 296 HOH HOH A . 
H 5 HOH 150 550 292 HOH HOH A . 
H 5 HOH 151 551 46  HOH HOH A . 
H 5 HOH 152 552 172 HOH HOH A . 
H 5 HOH 153 553 306 HOH HOH A . 
H 5 HOH 154 554 217 HOH HOH A . 
H 5 HOH 155 555 197 HOH HOH A . 
H 5 HOH 156 556 223 HOH HOH A . 
H 5 HOH 157 557 168 HOH HOH A . 
H 5 HOH 158 558 105 HOH HOH A . 
H 5 HOH 159 559 225 HOH HOH A . 
H 5 HOH 160 560 216 HOH HOH A . 
H 5 HOH 161 561 269 HOH HOH A . 
H 5 HOH 162 562 198 HOH HOH A . 
H 5 HOH 163 563 319 HOH HOH A . 
H 5 HOH 164 564 187 HOH HOH A . 
H 5 HOH 165 565 310 HOH HOH A . 
H 5 HOH 166 566 171 HOH HOH A . 
H 5 HOH 167 567 313 HOH HOH A . 
I 5 HOH 1   401 85  HOH HOH B . 
I 5 HOH 2   402 43  HOH HOH B . 
I 5 HOH 3   403 264 HOH HOH B . 
I 5 HOH 4   404 267 HOH HOH B . 
I 5 HOH 5   405 108 HOH HOH B . 
I 5 HOH 6   406 84  HOH HOH B . 
I 5 HOH 7   407 261 HOH HOH B . 
I 5 HOH 8   408 196 HOH HOH B . 
I 5 HOH 9   409 255 HOH HOH B . 
I 5 HOH 10  410 194 HOH HOH B . 
I 5 HOH 11  411 303 HOH HOH B . 
I 5 HOH 12  412 195 HOH HOH B . 
I 5 HOH 13  413 28  HOH HOH B . 
I 5 HOH 14  414 183 HOH HOH B . 
I 5 HOH 15  415 315 HOH HOH B . 
I 5 HOH 16  416 256 HOH HOH B . 
I 5 HOH 17  417 262 HOH HOH B . 
I 5 HOH 18  418 281 HOH HOH B . 
I 5 HOH 19  419 100 HOH HOH B . 
I 5 HOH 20  420 252 HOH HOH B . 
I 5 HOH 21  421 143 HOH HOH B . 
I 5 HOH 22  422 78  HOH HOH B . 
I 5 HOH 23  423 12  HOH HOH B . 
I 5 HOH 24  424 14  HOH HOH B . 
I 5 HOH 25  425 181 HOH HOH B . 
I 5 HOH 26  426 175 HOH HOH B . 
I 5 HOH 27  427 177 HOH HOH B . 
I 5 HOH 28  428 189 HOH HOH B . 
I 5 HOH 29  429 50  HOH HOH B . 
I 5 HOH 30  430 251 HOH HOH B . 
I 5 HOH 31  431 15  HOH HOH B . 
I 5 HOH 32  432 244 HOH HOH B . 
I 5 HOH 33  433 63  HOH HOH B . 
I 5 HOH 34  434 102 HOH HOH B . 
I 5 HOH 35  435 117 HOH HOH B . 
I 5 HOH 36  436 17  HOH HOH B . 
I 5 HOH 37  437 65  HOH HOH B . 
I 5 HOH 38  438 47  HOH HOH B . 
I 5 HOH 39  439 305 HOH HOH B . 
I 5 HOH 40  440 288 HOH HOH B . 
I 5 HOH 41  441 118 HOH HOH B . 
I 5 HOH 42  442 56  HOH HOH B . 
I 5 HOH 43  443 266 HOH HOH B . 
I 5 HOH 44  444 16  HOH HOH B . 
I 5 HOH 45  445 151 HOH HOH B . 
I 5 HOH 46  446 61  HOH HOH B . 
I 5 HOH 47  447 304 HOH HOH B . 
I 5 HOH 48  448 73  HOH HOH B . 
I 5 HOH 49  449 127 HOH HOH B . 
I 5 HOH 50  450 184 HOH HOH B . 
I 5 HOH 51  451 287 HOH HOH B . 
I 5 HOH 52  452 94  HOH HOH B . 
I 5 HOH 53  453 239 HOH HOH B . 
I 5 HOH 54  454 21  HOH HOH B . 
I 5 HOH 55  455 59  HOH HOH B . 
I 5 HOH 56  456 53  HOH HOH B . 
I 5 HOH 57  457 112 HOH HOH B . 
I 5 HOH 58  458 150 HOH HOH B . 
I 5 HOH 59  459 51  HOH HOH B . 
I 5 HOH 60  460 42  HOH HOH B . 
I 5 HOH 61  461 245 HOH HOH B . 
I 5 HOH 62  462 155 HOH HOH B . 
I 5 HOH 63  463 248 HOH HOH B . 
I 5 HOH 64  464 265 HOH HOH B . 
I 5 HOH 65  465 176 HOH HOH B . 
I 5 HOH 66  466 321 HOH HOH B . 
I 5 HOH 67  467 54  HOH HOH B . 
I 5 HOH 68  468 95  HOH HOH B . 
I 5 HOH 69  469 186 HOH HOH B . 
I 5 HOH 70  470 91  HOH HOH B . 
I 5 HOH 71  471 66  HOH HOH B . 
I 5 HOH 72  472 6   HOH HOH B . 
I 5 HOH 73  473 139 HOH HOH B . 
I 5 HOH 74  474 130 HOH HOH B . 
I 5 HOH 75  475 33  HOH HOH B . 
I 5 HOH 76  476 97  HOH HOH B . 
I 5 HOH 77  477 123 HOH HOH B . 
I 5 HOH 78  478 79  HOH HOH B . 
I 5 HOH 79  479 110 HOH HOH B . 
I 5 HOH 80  480 236 HOH HOH B . 
I 5 HOH 81  481 141 HOH HOH B . 
I 5 HOH 82  482 301 HOH HOH B . 
I 5 HOH 83  483 274 HOH HOH B . 
I 5 HOH 84  484 200 HOH HOH B . 
I 5 HOH 85  485 103 HOH HOH B . 
I 5 HOH 86  486 259 HOH HOH B . 
I 5 HOH 87  487 182 HOH HOH B . 
I 5 HOH 88  488 192 HOH HOH B . 
I 5 HOH 89  489 22  HOH HOH B . 
I 5 HOH 90  490 122 HOH HOH B . 
I 5 HOH 91  491 161 HOH HOH B . 
I 5 HOH 92  492 18  HOH HOH B . 
I 5 HOH 93  493 149 HOH HOH B . 
I 5 HOH 94  494 126 HOH HOH B . 
I 5 HOH 95  495 68  HOH HOH B . 
I 5 HOH 96  496 10  HOH HOH B . 
I 5 HOH 97  497 238 HOH HOH B . 
I 5 HOH 98  498 40  HOH HOH B . 
I 5 HOH 99  499 253 HOH HOH B . 
I 5 HOH 100 500 299 HOH HOH B . 
I 5 HOH 101 501 322 HOH HOH B . 
I 5 HOH 102 502 131 HOH HOH B . 
I 5 HOH 103 503 293 HOH HOH B . 
I 5 HOH 104 504 70  HOH HOH B . 
I 5 HOH 105 505 314 HOH HOH B . 
I 5 HOH 106 506 140 HOH HOH B . 
I 5 HOH 107 507 125 HOH HOH B . 
I 5 HOH 108 508 134 HOH HOH B . 
I 5 HOH 109 509 86  HOH HOH B . 
I 5 HOH 110 510 44  HOH HOH B . 
I 5 HOH 111 511 156 HOH HOH B . 
I 5 HOH 112 512 23  HOH HOH B . 
I 5 HOH 113 513 202 HOH HOH B . 
I 5 HOH 114 514 26  HOH HOH B . 
I 5 HOH 115 515 260 HOH HOH B . 
I 5 HOH 116 516 300 HOH HOH B . 
I 5 HOH 117 517 111 HOH HOH B . 
I 5 HOH 118 518 290 HOH HOH B . 
I 5 HOH 119 519 81  HOH HOH B . 
I 5 HOH 120 520 263 HOH HOH B . 
I 5 HOH 121 521 135 HOH HOH B . 
I 5 HOH 122 522 258 HOH HOH B . 
I 5 HOH 123 523 185 HOH HOH B . 
I 5 HOH 124 524 240 HOH HOH B . 
I 5 HOH 125 525 71  HOH HOH B . 
I 5 HOH 126 526 188 HOH HOH B . 
I 5 HOH 127 527 247 HOH HOH B . 
I 5 HOH 128 528 119 HOH HOH B . 
I 5 HOH 129 529 193 HOH HOH B . 
I 5 HOH 130 530 257 HOH HOH B . 
I 5 HOH 131 531 190 HOH HOH B . 
I 5 HOH 132 532 106 HOH HOH B . 
I 5 HOH 133 533 113 HOH HOH B . 
I 5 HOH 134 534 69  HOH HOH B . 
I 5 HOH 135 535 307 HOH HOH B . 
I 5 HOH 136 536 101 HOH HOH B . 
I 5 HOH 137 537 250 HOH HOH B . 
I 5 HOH 138 538 268 HOH HOH B . 
I 5 HOH 139 539 308 HOH HOH B . 
I 5 HOH 140 540 302 HOH HOH B . 
I 5 HOH 141 541 289 HOH HOH B . 
I 5 HOH 142 542 284 HOH HOH B . 
I 5 HOH 143 543 242 HOH HOH B . 
I 5 HOH 144 544 173 HOH HOH B . 
I 5 HOH 145 545 237 HOH HOH B . 
I 5 HOH 146 546 178 HOH HOH B . 
I 5 HOH 147 547 191 HOH HOH B . 
I 5 HOH 148 548 246 HOH HOH B . 
I 5 HOH 149 549 243 HOH HOH B . 
I 5 HOH 150 550 254 HOH HOH B . 
I 5 HOH 151 551 291 HOH HOH B . 
I 5 HOH 152 552 199 HOH HOH B . 
I 5 HOH 153 553 241 HOH HOH B . 
I 5 HOH 154 554 232 HOH HOH B . 
I 5 HOH 155 555 320 HOH HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A GLN 82  ? CB  ? A GLN 82  CB  
2  1 Y 1 A GLN 82  ? CG  ? A GLN 82  CG  
3  1 Y 1 A GLN 82  ? CD  ? A GLN 82  CD  
4  1 Y 1 A GLN 82  ? OE1 ? A GLN 82  OE1 
5  1 Y 1 A GLN 82  ? NE2 ? A GLN 82  NE2 
6  1 Y 1 A ARG 186 ? CG  ? A ARG 186 CG  
7  1 Y 1 A ARG 186 ? CD  ? A ARG 186 CD  
8  1 Y 1 A ARG 186 ? NE  ? A ARG 186 NE  
9  1 Y 1 A ARG 186 ? CZ  ? A ARG 186 CZ  
10 1 Y 1 A ARG 186 ? NH1 ? A ARG 186 NH1 
11 1 Y 1 A ARG 186 ? NH2 ? A ARG 186 NH2 
12 1 Y 1 B LYS 3   ? CG  ? B LYS 3   CG  
13 1 Y 1 B LYS 3   ? CD  ? B LYS 3   CD  
14 1 Y 1 B LYS 3   ? CE  ? B LYS 3   CE  
15 1 Y 1 B LYS 3   ? NZ  ? B LYS 3   NZ  
16 1 Y 1 B LYS 18  ? CG  ? B LYS 18  CG  
17 1 Y 1 B LYS 18  ? CD  ? B LYS 18  CD  
18 1 Y 1 B LYS 18  ? CE  ? B LYS 18  CE  
19 1 Y 1 B LYS 18  ? NZ  ? B LYS 18  NZ  
20 1 Y 1 B GLN 79  ? CD  ? B GLN 79  CD  
21 1 Y 1 B GLN 79  ? OE1 ? B GLN 79  OE1 
22 1 Y 1 B GLN 79  ? NE2 ? B GLN 79  NE2 
23 1 Y 1 B ARG 194 ? NE  ? B ARG 194 NE  
24 1 Y 1 B ARG 194 ? CZ  ? B ARG 194 CZ  
25 1 Y 1 B ARG 194 ? NH1 ? B ARG 194 NH1 
26 1 Y 1 B ARG 194 ? NH2 ? B ARG 194 NH2 
# 
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        ? ? ? ? ? ? ? ? ? ? ? REFMAC      ? ? ? .    1 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? MOSFLM      ? ? ? .    2 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? 3.10 3 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? SCALA       ? ? ? .    4 
? phasing           ? ? ? ? ? ? ? ? ? ? ? MOLREP      ? ? ? .    5 
? 'model building'  ? ? ? ? ? ? ? ? ? ? ? Coot        ? ? ? .    6 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   105.500 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     6R71 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     45.085 
_cell.length_a_esd                 ? 
_cell.length_b                     70.835 
_cell.length_b_esd                 ? 
_cell.length_c                     74.905 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
# 
_symmetry.entry_id                         6R71 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_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                   6R71 
_exptl.crystals_number            2 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                      ? 
_exptl_crystal.density_diffrn              ? 
_exptl_crystal.density_Matthews            1.93 
_exptl_crystal.density_method              ? 
_exptl_crystal.density_percent_sol         36.15 
_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              7.2 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp            291 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
'Crystallization buffer: 0.1M ammonium citrate (pH 7.2), 0.2 M ammonium sulfate and 26% PEG4000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     CCD 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'MARMOSAIC 225 mm CCD' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2014-11-28 
_diffrn_detector.pdbx_frequency               ? 
# 
_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   0.91000 
_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                        'MAX II BEAMLINE I911-3' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.91000 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   I911-3 
_diffrn_source.pdbx_synchrotron_site       'MAX II' 
# 
_reflns.B_iso_Wilson_estimate            ? 
_reflns.entry_id                         6R71 
_reflns.data_reduction_details           ? 
_reflns.data_reduction_method            ? 
_reflns.d_resolution_high                2.000 
_reflns.d_resolution_low                 37.034 
_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                       29369 
_reflns.observed_criterion               ? 
_reflns.observed_criterion_F_max         ? 
_reflns.observed_criterion_F_min         ? 
_reflns.observed_criterion_I_max         ? 
_reflns.observed_criterion_I_min         ? 
_reflns.observed_criterion_sigma_F       ? 
_reflns.observed_criterion_sigma_I       ? 
_reflns.percent_possible_obs             95.700 
_reflns.R_free_details                   ? 
_reflns.Rmerge_F_all                     ? 
_reflns.Rmerge_F_obs                     ? 
_reflns.Friedel_coverage                 ? 
_reflns.number_gt                        ? 
_reflns.threshold_expression             ? 
_reflns.pdbx_redundancy                  6.300 
_reflns.pdbx_Rmerge_I_obs                ? 
_reflns.pdbx_Rmerge_I_all                ? 
_reflns.pdbx_Rsym_value                  0.102 
_reflns.pdbx_netI_over_av_sigmaI         6.917 
_reflns.pdbx_netI_over_sigmaI            12.100 
_reflns.pdbx_res_netI_over_av_sigmaI_2   ? 
_reflns.pdbx_res_netI_over_sigmaI_2      ? 
_reflns.pdbx_chi_squared                 ? 
_reflns.pdbx_scaling_rejects             ? 
_reflns.pdbx_d_res_high_opt              ? 
_reflns.pdbx_d_res_low_opt               ? 
_reflns.pdbx_d_res_opt_method            ? 
_reflns.phase_calculation_details        ? 
_reflns.pdbx_Rrim_I_all                  0.121 
_reflns.pdbx_Rpim_I_all                  0.047 
_reflns.pdbx_d_opt                       ? 
_reflns.pdbx_number_measured_all         ? 
_reflns.pdbx_diffrn_id                   1 
_reflns.pdbx_ordinal                     1 
_reflns.pdbx_CC_half                     ? 
_reflns.pdbx_R_split                     ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_measured_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.number_unique_obs 
_reflns_shell.percent_possible_all 
_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 
_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 
_reflns_shell.pdbx_rejects 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_R_split 
2.000 2.110  ? 2.2  ? ? ? ? 3987 89.800 ? ? ? ? 0.353 ? ? ? ? ? ? ? ? 6.200 0.353 ? ? ? 0.420 0.163 ? 1  1 ? ? 
2.110 2.240  ? 2.8  ? ? ? ? 3885 92.300 ? ? ? ? 0.273 ? ? ? ? ? ? ? ? 6.100 0.273 ? ? ? 0.323 0.125 ? 2  1 ? ? 
2.240 2.390  ? 3.4  ? ? ? ? 3782 95.500 ? ? ? ? 0.226 ? ? ? ? ? ? ? ? 6.100 0.226 ? ? ? 0.267 0.104 ? 3  1 ? ? 
2.390 2.580  ? 4.4  ? ? ? ? 3597 97.400 ? ? ? ? 0.174 ? ? ? ? ? ? ? ? 6.200 0.174 ? ? ? 0.206 0.080 ? 4  1 ? ? 
2.580 2.830  ? 5.8  ? ? ? ? 3344 97.800 ? ? ? ? 0.131 ? ? ? ? ? ? ? ? 6.400 0.131 ? ? ? 0.156 0.061 ? 5  1 ? ? 
2.830 3.160  ? 7.5  ? ? ? ? 3036 98.300 ? ? ? ? 0.097 ? ? ? ? ? ? ? ? 6.500 0.097 ? ? ? 0.115 0.045 ? 6  1 ? ? 
3.160 3.650  ? 10.1 ? ? ? ? 2685 98.200 ? ? ? ? 0.068 ? ? ? ? ? ? ? ? 6.500 0.068 ? ? ? 0.080 0.031 ? 7  1 ? ? 
3.650 4.470  ? 13.1 ? ? ? ? 2284 98.700 ? ? ? ? 0.050 ? ? ? ? ? ? ? ? 6.500 0.050 ? ? ? 0.058 0.023 ? 8  1 ? ? 
4.470 6.320  ? 13.6 ? ? ? ? 1773 98.700 ? ? ? ? 0.045 ? ? ? ? ? ? ? ? 6.500 0.045 ? ? ? 0.053 0.020 ? 9  1 ? ? 
6.320 37.034 ? 12.0 ? ? ? ? 996  98.400 ? ? ? ? 0.049 ? ? ? ? ? ? ? ? 6.300 0.049 ? ? ? 0.060 0.024 ? 10 1 ? ? 
# 
_refine.aniso_B[1][1]                            0.6000 
_refine.aniso_B[1][2]                            -0.0000 
_refine.aniso_B[1][3]                            -0.2800 
_refine.aniso_B[2][2]                            -0.0700 
_refine.aniso_B[2][3]                            -0.0000 
_refine.aniso_B[3][3]                            -0.3300 
_refine.B_iso_max                                70.370 
_refine.B_iso_mean                               16.2453 
_refine.B_iso_min                                4.070 
_refine.correlation_coeff_Fo_to_Fc               0.9560 
_refine.correlation_coeff_Fo_to_Fc_free          0.9200 
_refine.details                                  
'HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT U VALUES      : REFINED INDIVIDUALLY' 
_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                                 6R71 
_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                            2.0000 
_refine.ls_d_res_low                             36.5000 
_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                     29349 
_refine.ls_number_reflns_R_free                  2943 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    95.2300 
_refine.ls_percent_reflns_R_free                 10.0000 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1584 
_refine.ls_R_factor_R_free                       0.2096 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1528 
_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                          0.000 
_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               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      1JD0 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.2400 
_refine.pdbx_overall_ESU_R_Free                  0.1830 
_refine.pdbx_solvent_vdw_probe_radii             1.4000 
_refine.pdbx_solvent_ion_probe_radii             0.8000 
_refine.pdbx_solvent_shrinkage_radii             0.8000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_R_Cruickshank_DPI             0.2401 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.0000 
_refine_hist.d_res_low                        36.5000 
_refine_hist.number_atoms_solvent             322 
_refine_hist.number_atoms_total               4575 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        4195 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         58 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
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' ? 0.007  0.012  4361 ? r_bond_refined_d       ? ? 
'X-RAY DIFFRACTION' ? 1.517  1.652  5950 ? r_angle_refined_deg    ? ? 
'X-RAY DIFFRACTION' ? 7.279  5.000  522  ? r_dihedral_angle_1_deg ? ? 
'X-RAY DIFFRACTION' ? 38.181 23.947 228  ? r_dihedral_angle_2_deg ? ? 
'X-RAY DIFFRACTION' ? 15.882 15.000 658  ? r_dihedral_angle_3_deg ? ? 
'X-RAY DIFFRACTION' ? 17.326 15.000 13   ? r_dihedral_angle_4_deg ? ? 
'X-RAY DIFFRACTION' ? 0.111  0.200  542  ? r_chiral_restr         ? ? 
'X-RAY DIFFRACTION' ? 0.008  0.020  3452 ? r_gen_planes_refined   ? ? 
'X-RAY DIFFRACTION' ? 1.335  1.425  2091 ? r_mcbond_it            ? ? 
'X-RAY DIFFRACTION' ? 2.177  2.125  2612 ? r_mcangle_it           ? ? 
'X-RAY DIFFRACTION' ? 2.001  1.624  2270 ? r_scbond_it            ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       2.0000 
_refine_ls_shell.d_res_low                        2.0520 
_refine_ls_shell.number_reflns_all                2013 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             225 
_refine_ls_shell.number_reflns_R_work             1788 
_refine_ls_shell.percent_reflns_obs               88.1700 
_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                  0.2380 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.1690 
_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   20 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
# 
_struct.entry_id                     6R71 
_struct.title                        
;Crystal structure of human carbonic anhydrase isozyme XII with 2-(benzenesulfonyl)-4-chloro-N-(2-hydroxyethyl)-5-sulfamoyl-benzamide
;
_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        6R71 
_struct_keywords.text            'drug design, carbonic anhydrase, benzenesulfonamide, metal-binding, lyase' 
_struct_keywords.pdbx_keywords   LYASE 
# 
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 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 2 ? 
G N N 4 ? 
H N N 5 ? 
I N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    CAH12_HUMAN 
_struct_ref.pdbx_db_accession          O43570 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;SKWTYFGPDGENSWSKKYPSCGGLLQSPIDLHSDILQYDASLTPLEFQGYNLSANKQFLLTNNGHSVKLNLPSDMHIQGL
QSRYSATQLHLHWGNPNDPHGSEHTVSGQHFAAELHIVHYNSDLYPDASTASNKSEGLAVLAVLIEMGSFNPSYDKIFSH
LQHVKYKGQEAFVPGFNIEELLPERTAEYYRYRGSLTTPPCNPTVLWTVFRNPVQISQEQLLALETALYCTHMDDPSPRE
MINNFRQVQKFDERLVYTSFSQ
;
_struct_ref.pdbx_align_begin           30 
# 
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 6R71 A 2 ? 263 ? O43570 30 ? 291 ? 2 263 
2 1 6R71 B 2 ? 263 ? O43570 30 ? 291 ? 2 263 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 6R71 MET A 1 ? UNP O43570 ? ? 'initiating methionine' 1 1 
2 6R71 MET B 1 ? UNP O43570 ? ? 'initiating methionine' 1 2 
# 
_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   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
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)' 2290  ? 
1 MORE         2     ? 
1 'SSA (A^2)'  21400 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I 
# 
_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                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_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 14  ? LYS A 18  ? SER A 14  LYS A 18  5 ? 5  
HELX_P HELX_P2  AA2 TYR A 19  ? GLY A 24  ? TYR A 19  GLY A 24  5 ? 6  
HELX_P HELX_P3  AA3 HIS A 33  ? ASP A 35  ? HIS A 33  ASP A 35  5 ? 3  
HELX_P HELX_P4  AA4 ASP A 128 ? SER A 133 ? ASP A 128 SER A 133 1 ? 6  
HELX_P HELX_P5  AA5 ASN A 152 ? SER A 160 ? ASN A 152 SER A 160 1 ? 9  
HELX_P HELX_P6  AA6 HIS A 161 ? VAL A 165 ? HIS A 161 VAL A 165 5 ? 5  
HELX_P HELX_P7  AA7 ASN A 178 ? LEU A 183 ? ASN A 178 LEU A 183 5 ? 6  
HELX_P HELX_P8  AA8 SER A 218 ? ALA A 228 ? SER A 218 ALA A 228 1 ? 11 
HELX_P HELX_P9  AA9 PHE B 7   ? LYS B 18  ? PHE B 7   LYS B 18  5 ? 12 
HELX_P HELX_P10 AB1 TYR B 19  ? GLY B 24  ? TYR B 19  GLY B 24  5 ? 6  
HELX_P HELX_P11 AB2 HIS B 33  ? ASP B 35  ? HIS B 33  ASP B 35  5 ? 3  
HELX_P HELX_P12 AB3 ASP B 128 ? SER B 133 ? ASP B 128 SER B 133 1 ? 6  
HELX_P HELX_P13 AB4 ASN B 152 ? SER B 160 ? ASN B 152 SER B 160 1 ? 9  
HELX_P HELX_P14 AB5 HIS B 161 ? VAL B 165 ? HIS B 161 VAL B 165 5 ? 5  
HELX_P HELX_P15 AB6 ASN B 178 ? LEU B 183 ? ASN B 178 LEU B 183 5 ? 6  
HELX_P HELX_P16 AB7 SER B 218 ? LEU B 229 ? SER B 218 LEU B 229 1 ? 12 
# 
_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 22  SG  ? ? ? 1_555 A CYS 202 SG ? ? A CYS 22  A CYS 202 1_555 ? ? ? ? ? ? ? 2.120 ? ? 
disulf2 disulf ? ? B CYS 22  SG  ? ? ? 1_555 B CYS 202 SG ? ? B CYS 22  B CYS 202 1_555 ? ? ? ? ? ? ? 2.079 ? ? 
metalc1 metalc ? ? A HIS 91  NE2 ? ? ? 1_555 C ZN  .   ZN ? ? A HIS 91  A ZN  301 1_555 ? ? ? ? ? ? ? 2.001 ? ? 
metalc2 metalc ? ? A HIS 93  NE2 ? ? ? 1_555 C ZN  .   ZN ? ? A HIS 93  A ZN  301 1_555 ? ? ? ? ? ? ? 1.997 ? ? 
metalc3 metalc ? ? A HIS 117 ND1 ? ? ? 1_555 C ZN  .   ZN ? ? A HIS 117 A ZN  301 1_555 ? ? ? ? ? ? ? 2.055 ? ? 
metalc4 metalc ? ? C ZN  .   ZN  ? ? ? 1_555 E JTW .   N1 ? ? A ZN  301 A JTW 303 1_555 ? ? ? ? ? ? ? 1.962 ? ? 
metalc5 metalc ? ? B HIS 91  NE2 ? ? ? 1_555 F ZN  .   ZN ? ? B HIS 91  B ZN  301 1_555 ? ? ? ? ? ? ? 2.054 ? ? 
metalc6 metalc ? ? B HIS 93  NE2 ? ? ? 1_555 F ZN  .   ZN ? ? B HIS 93  B ZN  301 1_555 ? ? ? ? ? ? ? 1.996 ? ? 
metalc7 metalc ? ? B HIS 117 ND1 ? ? ? 1_555 F ZN  .   ZN ? ? B HIS 117 B ZN  301 1_555 ? ? ? ? ? ? ? 1.967 ? ? 
metalc8 metalc ? ? F ZN  .   ZN  ? ? ? 1_555 G JTW .   N1 ? ? B ZN  301 B JTW 302 1_555 ? ? ? ? ? ? ? 1.862 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
metalc ? ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  NE2 ? A HIS 91  ? A HIS 91  ? 1_555 ZN ? C ZN . ? A ZN 301 ? 1_555 NE2 ? A HIS 93  ? A HIS 93  ? 1_555 96.9  ? 
2  NE2 ? A HIS 91  ? A HIS 91  ? 1_555 ZN ? C ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS 117 ? A HIS 117 ? 1_555 116.8 ? 
3  NE2 ? A HIS 93  ? A HIS 93  ? 1_555 ZN ? C ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS 117 ? A HIS 117 ? 1_555 93.3  ? 
4  NE2 ? A HIS 91  ? A HIS 91  ? 1_555 ZN ? C ZN . ? A ZN 301 ? 1_555 N1  ? E JTW .   ? A JTW 303 ? 1_555 113.9 ? 
5  NE2 ? A HIS 93  ? A HIS 93  ? 1_555 ZN ? C ZN . ? A ZN 301 ? 1_555 N1  ? E JTW .   ? A JTW 303 ? 1_555 112.3 ? 
6  ND1 ? A HIS 117 ? A HIS 117 ? 1_555 ZN ? C ZN . ? A ZN 301 ? 1_555 N1  ? E JTW .   ? A JTW 303 ? 1_555 118.9 ? 
7  NE2 ? B HIS 91  ? B HIS 91  ? 1_555 ZN ? F ZN . ? B ZN 301 ? 1_555 NE2 ? B HIS 93  ? B HIS 93  ? 1_555 96.3  ? 
8  NE2 ? B HIS 91  ? B HIS 91  ? 1_555 ZN ? F ZN . ? B ZN 301 ? 1_555 ND1 ? B HIS 117 ? B HIS 117 ? 1_555 120.2 ? 
9  NE2 ? B HIS 93  ? B HIS 93  ? 1_555 ZN ? F ZN . ? B ZN 301 ? 1_555 ND1 ? B HIS 117 ? B HIS 117 ? 1_555 102.4 ? 
10 NE2 ? B HIS 91  ? B HIS 91  ? 1_555 ZN ? F ZN . ? B ZN 301 ? 1_555 N1  ? G JTW .   ? B JTW 302 ? 1_555 107.6 ? 
11 NE2 ? B HIS 93  ? B HIS 93  ? 1_555 ZN ? F ZN . ? B ZN 301 ? 1_555 N1  ? G JTW .   ? B JTW 302 ? 1_555 112.3 ? 
12 ND1 ? B HIS 117 ? B HIS 117 ? 1_555 ZN ? F ZN . ? B ZN 301 ? 1_555 N1  ? G JTW .   ? B JTW 302 ? 1_555 116.1 ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 SER 28  A . ? SER 28  A PRO 29  A ? PRO 29  A 1 -0.16 
2 PRO 200 A . ? PRO 200 A PRO 201 A ? PRO 201 A 1 2.94  
3 SER 28  B . ? SER 28  B PRO 29  B ? PRO 29  B 1 4.85  
4 PRO 200 B . ? PRO 200 B PRO 201 B ? PRO 201 B 1 1.82  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2  ? 
AA2 ? 10 ? 
AA3 ? 6  ? 
AA4 ? 2  ? 
AA5 ? 10 ? 
AA6 ? 6  ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2  ? parallel      
AA2 1 2  ? parallel      
AA2 2 3  ? anti-parallel 
AA2 3 4  ? anti-parallel 
AA2 4 5  ? parallel      
AA2 5 6  ? anti-parallel 
AA2 6 7  ? anti-parallel 
AA2 7 8  ? anti-parallel 
AA2 8 9  ? anti-parallel 
AA2 9 10 ? anti-parallel 
AA3 1 2  ? anti-parallel 
AA3 2 3  ? anti-parallel 
AA3 3 4  ? anti-parallel 
AA3 4 5  ? anti-parallel 
AA3 5 6  ? parallel      
AA4 1 2  ? parallel      
AA5 1 2  ? parallel      
AA5 2 3  ? anti-parallel 
AA5 3 4  ? anti-parallel 
AA5 4 5  ? parallel      
AA5 5 6  ? anti-parallel 
AA5 6 7  ? anti-parallel 
AA5 7 8  ? anti-parallel 
AA5 8 9  ? anti-parallel 
AA5 9 10 ? anti-parallel 
AA6 1 2  ? anti-parallel 
AA6 2 3  ? anti-parallel 
AA6 3 4  ? anti-parallel 
AA6 4 5  ? anti-parallel 
AA6 5 6  ? 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  ASP A 31  ? LEU A 32  ? ASP A 31  LEU A 32  
AA1 2  THR A 106 ? VAL A 107 ? THR A 106 VAL A 107 
AA2 1  LEU A 37  ? TYR A 39  ? LEU A 37  TYR A 39  
AA2 2  VAL A 257 ? THR A 259 ? VAL A 257 THR A 259 
AA2 3  TYR A 190 ? GLY A 195 ? TYR A 190 GLY A 195 
AA2 4  VAL A 206 ? PHE A 211 ? VAL A 206 PHE A 211 
AA2 5  LEU A 139 ? MET A 148 ? LEU A 139 MET A 148 
AA2 6  ALA A 114 ? ASN A 122 ? ALA A 114 ASN A 122 
AA2 7  TYR A 85  ? TRP A 94  ? TYR A 85  TRP A 94  
AA2 8  VAL A 68  ? ASN A 71  ? VAL A 68  ASN A 71  
AA2 9  GLN A 58  ? ASN A 63  ? GLN A 58  ASN A 63  
AA2 10 GLU A 171 ? PRO A 175 ? GLU A 171 PRO A 175 
AA3 1  GLU A 47  ? GLN A 49  ? GLU A 47  GLN A 49  
AA3 2  HIS A 77  ? GLN A 79  ? HIS A 77  GLN A 79  
AA3 3  TYR A 85  ? TRP A 94  ? TYR A 85  TRP A 94  
AA3 4  ALA A 114 ? ASN A 122 ? ALA A 114 ASN A 122 
AA3 5  LEU A 139 ? MET A 148 ? LEU A 139 MET A 148 
AA3 6  VAL A 215 ? ILE A 217 ? VAL A 215 ILE A 217 
AA4 1  ASP B 31  ? LEU B 32  ? ASP B 31  LEU B 32  
AA4 2  THR B 106 ? VAL B 107 ? THR B 106 VAL B 107 
AA5 1  LEU B 37  ? TYR B 39  ? LEU B 37  TYR B 39  
AA5 2  VAL B 257 ? THR B 259 ? VAL B 257 THR B 259 
AA5 3  TYR B 190 ? GLY B 195 ? TYR B 190 GLY B 195 
AA5 4  VAL B 206 ? PHE B 211 ? VAL B 206 PHE B 211 
AA5 5  LEU B 139 ? MET B 148 ? LEU B 139 MET B 148 
AA5 6  ALA B 114 ? ASN B 122 ? ALA B 114 ASN B 122 
AA5 7  TYR B 85  ? TRP B 94  ? TYR B 85  TRP B 94  
AA5 8  VAL B 68  ? ASN B 71  ? VAL B 68  ASN B 71  
AA5 9  GLN B 58  ? ASN B 63  ? GLN B 58  ASN B 63  
AA5 10 GLU B 171 ? PRO B 175 ? GLU B 171 PRO B 175 
AA6 1  GLU B 47  ? GLN B 49  ? GLU B 47  GLN B 49  
AA6 2  HIS B 77  ? GLN B 79  ? HIS B 77  GLN B 79  
AA6 3  TYR B 85  ? TRP B 94  ? TYR B 85  TRP B 94  
AA6 4  ALA B 114 ? ASN B 122 ? ALA B 114 ASN B 122 
AA6 5  LEU B 139 ? MET B 148 ? LEU B 139 MET B 148 
AA6 6  VAL B 215 ? ILE B 217 ? VAL B 215 ILE B 217 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2  N LEU A 32  ? N LEU A 32  O THR A 106 ? O THR A 106 
AA2 1 2  N GLN A 38  ? N GLN A 38  O VAL A 257 ? O VAL A 257 
AA2 2 3  O TYR A 258 ? O TYR A 258 N ARG A 192 ? N ARG A 192 
AA2 3 4  N TYR A 191 ? N TYR A 191 O VAL A 210 ? O VAL A 210 
AA2 4 5  O THR A 209 ? O THR A 209 N ALA A 143 ? N ALA A 143 
AA2 5 6  O VAL A 144 ? O VAL A 144 N LEU A 116 ? N LEU A 116 
AA2 6 7  O VAL A 119 ? O VAL A 119 N THR A 88  ? N THR A 88  
AA2 7 8  O LEU A 90  ? O LEU A 90  N LEU A 70  ? N LEU A 70  
AA2 8 9  O ASN A 71  ? O ASN A 71  N LEU A 60  ? N LEU A 60  
AA2 9 10 N LEU A 61  ? N LEU A 61  O ALA A 172 ? O ALA A 172 
AA3 1 2  N GLN A 49  ? N GLN A 49  O HIS A 77  ? O HIS A 77  
AA3 2 3  N ILE A 78  ? N ILE A 78  O TYR A 85  ? O TYR A 85  
AA3 3 4  N THR A 88  ? N THR A 88  O VAL A 119 ? O VAL A 119 
AA3 4 5  N LEU A 116 ? N LEU A 116 O VAL A 144 ? O VAL A 144 
AA3 5 6  N GLU A 147 ? N GLU A 147 O VAL A 215 ? O VAL A 215 
AA4 1 2  N LEU B 32  ? N LEU B 32  O THR B 106 ? O THR B 106 
AA5 1 2  N GLN B 38  ? N GLN B 38  O VAL B 257 ? O VAL B 257 
AA5 2 3  O TYR B 258 ? O TYR B 258 N ARG B 192 ? N ARG B 192 
AA5 3 4  N TYR B 193 ? N TYR B 193 O TRP B 208 ? O TRP B 208 
AA5 4 5  O THR B 209 ? O THR B 209 N ALA B 143 ? N ALA B 143 
AA5 5 6  O VAL B 144 ? O VAL B 144 N LEU B 116 ? N LEU B 116 
AA5 6 7  O VAL B 119 ? O VAL B 119 N THR B 88  ? N THR B 88  
AA5 7 8  O LEU B 90  ? O LEU B 90  N LEU B 70  ? N LEU B 70  
AA5 8 9  O ASN B 71  ? O ASN B 71  N LEU B 60  ? N LEU B 60  
AA5 9 10 N LEU B 61  ? N LEU B 61  O ALA B 172 ? O ALA B 172 
AA6 1 2  N GLN B 49  ? N GLN B 49  O HIS B 77  ? O HIS B 77  
AA6 2 3  N ILE B 78  ? N ILE B 78  O TYR B 85  ? O TYR B 85  
AA6 3 4  N THR B 88  ? N THR B 88  O VAL B 119 ? O VAL B 119 
AA6 4 5  N LEU B 116 ? N LEU B 116 O VAL B 144 ? O VAL B 144 
AA6 5 6  N GLU B 147 ? N GLU B 147 O VAL B 215 ? O VAL B 215 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software A ZN  301 ? 4  'binding site for residue ZN A 301'  
AC2 Software A EDO 302 ? 6  'binding site for residue EDO A 302' 
AC3 Software A JTW 303 ? 14 'binding site for residue JTW A 303' 
AC4 Software B ZN  301 ? 4  'binding site for residue ZN B 301'  
AC5 Software B JTW 302 ? 15 'binding site for residue JTW B 302' 
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1  AC1 4  HIS A 91  ? HIS A 91  . ? 1_555 ? 
2  AC1 4  HIS A 93  ? HIS A 93  . ? 1_555 ? 
3  AC1 4  HIS A 117 ? HIS A 117 . ? 1_555 ? 
4  AC1 4  JTW E .   ? JTW A 303 . ? 1_555 ? 
5  AC2 6  PRO A 9   ? PRO A 9   . ? 1_555 ? 
6  AC2 6  SER A 14  ? SER A 14  . ? 1_555 ? 
7  AC2 6  LYS A 17  ? LYS A 17  . ? 1_555 ? 
8  AC2 6  HOH H .   ? HOH A 422 . ? 1_555 ? 
9  AC2 6  PRO B 20  ? PRO B 20  . ? 1_555 ? 
10 AC2 6  GLY B 23  ? GLY B 23  . ? 1_555 ? 
11 AC3 14 HIS A 66  ? HIS A 66  . ? 1_555 ? 
12 AC3 14 GLN A 89  ? GLN A 89  . ? 1_555 ? 
13 AC3 14 HIS A 91  ? HIS A 91  . ? 1_555 ? 
14 AC3 14 HIS A 93  ? HIS A 93  . ? 1_555 ? 
15 AC3 14 HIS A 117 ? HIS A 117 . ? 1_555 ? 
16 AC3 14 SER A 133 ? SER A 133 . ? 1_555 ? 
17 AC3 14 VAL A 141 ? VAL A 141 . ? 1_555 ? 
18 AC3 14 LEU A 197 ? LEU A 197 . ? 1_555 ? 
19 AC3 14 THR A 198 ? THR A 198 . ? 1_555 ? 
20 AC3 14 THR A 199 ? THR A 199 . ? 1_555 ? 
21 AC3 14 TRP A 208 ? TRP A 208 . ? 1_555 ? 
22 AC3 14 ZN  C .   ? ZN  A 301 . ? 1_555 ? 
23 AC3 14 HOH H .   ? HOH A 414 . ? 1_555 ? 
24 AC3 14 HOH H .   ? HOH A 424 . ? 1_555 ? 
25 AC4 4  HIS B 91  ? HIS B 91  . ? 1_555 ? 
26 AC4 4  HIS B 93  ? HIS B 93  . ? 1_555 ? 
27 AC4 4  HIS B 117 ? HIS B 117 . ? 1_555 ? 
28 AC4 4  JTW G .   ? JTW B 302 . ? 1_555 ? 
29 AC5 15 ASN B 64  ? ASN B 64  . ? 1_555 ? 
30 AC5 15 HIS B 66  ? HIS B 66  . ? 1_555 ? 
31 AC5 15 SER B 67  ? SER B 67  . ? 1_555 ? 
32 AC5 15 GLN B 89  ? GLN B 89  . ? 1_555 ? 
33 AC5 15 HIS B 91  ? HIS B 91  . ? 1_555 ? 
34 AC5 15 HIS B 93  ? HIS B 93  . ? 1_555 ? 
35 AC5 15 HIS B 117 ? HIS B 117 . ? 1_555 ? 
36 AC5 15 SER B 133 ? SER B 133 . ? 1_555 ? 
37 AC5 15 VAL B 141 ? VAL B 141 . ? 1_555 ? 
38 AC5 15 LEU B 197 ? LEU B 197 . ? 1_555 ? 
39 AC5 15 THR B 198 ? THR B 198 . ? 1_555 ? 
40 AC5 15 THR B 199 ? THR B 199 . ? 1_555 ? 
41 AC5 15 TRP B 208 ? TRP B 208 . ? 1_555 ? 
42 AC5 15 ZN  F .   ? ZN  B 301 . ? 1_555 ? 
43 AC5 15 HOH I .   ? HOH B 505 . ? 1_555 ? 
# 
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 ASP A 99  ? ? -150.84 78.37 
2 1 ASP B 99  ? ? -150.54 73.55 
3 1 ASN B 245 ? ? -95.29  50.35 
# 
_phasing.method   MR 
# 
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 MET 1 ? A MET 1 
2 1 Y 1 A SER 2 ? A SER 2 
3 1 Y 1 B MET 1 ? B MET 1 
4 1 Y 1 B SER 2 ? B SER 2 
# 
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  
CYS N    N  N N 74  
CYS CA   C  N R 75  
CYS C    C  N N 76  
CYS O    O  N N 77  
CYS CB   C  N N 78  
CYS SG   S  N N 79  
CYS OXT  O  N N 80  
CYS H    H  N N 81  
CYS H2   H  N N 82  
CYS HA   H  N N 83  
CYS HB2  H  N N 84  
CYS HB3  H  N N 85  
CYS HG   H  N N 86  
CYS HXT  H  N N 87  
EDO C1   C  N N 88  
EDO O1   O  N N 89  
EDO C2   C  N N 90  
EDO O2   O  N N 91  
EDO H11  H  N N 92  
EDO H12  H  N N 93  
EDO HO1  H  N N 94  
EDO H21  H  N N 95  
EDO H22  H  N N 96  
EDO HO2  H  N N 97  
GLN N    N  N N 98  
GLN CA   C  N S 99  
GLN C    C  N N 100 
GLN O    O  N N 101 
GLN CB   C  N N 102 
GLN CG   C  N N 103 
GLN CD   C  N N 104 
GLN OE1  O  N N 105 
GLN NE2  N  N N 106 
GLN OXT  O  N N 107 
GLN H    H  N N 108 
GLN H2   H  N N 109 
GLN HA   H  N N 110 
GLN HB2  H  N N 111 
GLN HB3  H  N N 112 
GLN HG2  H  N N 113 
GLN HG3  H  N N 114 
GLN HE21 H  N N 115 
GLN HE22 H  N N 116 
GLN HXT  H  N N 117 
GLU N    N  N N 118 
GLU CA   C  N S 119 
GLU C    C  N N 120 
GLU O    O  N N 121 
GLU CB   C  N N 122 
GLU CG   C  N N 123 
GLU CD   C  N N 124 
GLU OE1  O  N N 125 
GLU OE2  O  N N 126 
GLU OXT  O  N N 127 
GLU H    H  N N 128 
GLU H2   H  N N 129 
GLU HA   H  N N 130 
GLU HB2  H  N N 131 
GLU HB3  H  N N 132 
GLU HG2  H  N N 133 
GLU HG3  H  N N 134 
GLU HE2  H  N N 135 
GLU HXT  H  N N 136 
GLY N    N  N N 137 
GLY CA   C  N N 138 
GLY C    C  N N 139 
GLY O    O  N N 140 
GLY OXT  O  N N 141 
GLY H    H  N N 142 
GLY H2   H  N N 143 
GLY HA2  H  N N 144 
GLY HA3  H  N N 145 
GLY HXT  H  N N 146 
HIS N    N  N N 147 
HIS CA   C  N S 148 
HIS C    C  N N 149 
HIS O    O  N N 150 
HIS CB   C  N N 151 
HIS CG   C  Y N 152 
HIS ND1  N  Y N 153 
HIS CD2  C  Y N 154 
HIS CE1  C  Y N 155 
HIS NE2  N  Y N 156 
HIS OXT  O  N N 157 
HIS H    H  N N 158 
HIS H2   H  N N 159 
HIS HA   H  N N 160 
HIS HB2  H  N N 161 
HIS HB3  H  N N 162 
HIS HD1  H  N N 163 
HIS HD2  H  N N 164 
HIS HE1  H  N N 165 
HIS HE2  H  N N 166 
HIS HXT  H  N N 167 
HOH O    O  N N 168 
HOH H1   H  N N 169 
HOH H2   H  N N 170 
ILE N    N  N N 171 
ILE CA   C  N S 172 
ILE C    C  N N 173 
ILE O    O  N N 174 
ILE CB   C  N S 175 
ILE CG1  C  N N 176 
ILE CG2  C  N N 177 
ILE CD1  C  N N 178 
ILE OXT  O  N N 179 
ILE H    H  N N 180 
ILE H2   H  N N 181 
ILE HA   H  N N 182 
ILE HB   H  N N 183 
ILE HG12 H  N N 184 
ILE HG13 H  N N 185 
ILE HG21 H  N N 186 
ILE HG22 H  N N 187 
ILE HG23 H  N N 188 
ILE HD11 H  N N 189 
ILE HD12 H  N N 190 
ILE HD13 H  N N 191 
ILE HXT  H  N N 192 
JTW C12  C  N N 193 
JTW C21  C  Y N 194 
JTW C22  C  Y N 195 
JTW C23  C  Y N 196 
JTW C5   C  Y N 197 
JTW C6   C  Y N 198 
JTW C8   C  Y N 199 
JTW C9   C  Y N 200 
JTW C10  C  Y N 201 
JTW O20  O  N N 202 
JTW S18  S  N N 203 
JTW O19  O  N N 204 
JTW C25  C  Y N 205 
JTW C26  C  Y N 206 
JTW C24  C  Y N 207 
JTW C7   C  Y N 208 
JTW CL1  CL N N 209 
JTW S2   S  N N 210 
JTW O3   O  N N 211 
JTW O4   O  N N 212 
JTW N1   N  N N 213 
JTW O13  O  N N 214 
JTW N14  N  N N 215 
JTW C15  C  N N 216 
JTW C16  C  N N 217 
JTW O17  O  N N 218 
JTW H1   H  N N 219 
JTW H2   H  N N 220 
JTW H3   H  N N 221 
JTW H4   H  N N 222 
JTW H5   H  N N 223 
JTW H6   H  N N 224 
JTW H7   H  N N 225 
JTW H8   H  N N 226 
JTW H9   H  N N 227 
JTW H10  H  N N 228 
JTW H11  H  N N 229 
JTW H12  H  N N 230 
JTW H13  H  N N 231 
JTW H14  H  N N 232 
JTW H15  H  N N 233 
LEU N    N  N N 234 
LEU CA   C  N S 235 
LEU C    C  N N 236 
LEU O    O  N N 237 
LEU CB   C  N N 238 
LEU CG   C  N N 239 
LEU CD1  C  N N 240 
LEU CD2  C  N N 241 
LEU OXT  O  N N 242 
LEU H    H  N N 243 
LEU H2   H  N N 244 
LEU HA   H  N N 245 
LEU HB2  H  N N 246 
LEU HB3  H  N N 247 
LEU HG   H  N N 248 
LEU HD11 H  N N 249 
LEU HD12 H  N N 250 
LEU HD13 H  N N 251 
LEU HD21 H  N N 252 
LEU HD22 H  N N 253 
LEU HD23 H  N N 254 
LEU HXT  H  N N 255 
LYS N    N  N N 256 
LYS CA   C  N S 257 
LYS C    C  N N 258 
LYS O    O  N N 259 
LYS CB   C  N N 260 
LYS CG   C  N N 261 
LYS CD   C  N N 262 
LYS CE   C  N N 263 
LYS NZ   N  N N 264 
LYS OXT  O  N N 265 
LYS H    H  N N 266 
LYS H2   H  N N 267 
LYS HA   H  N N 268 
LYS HB2  H  N N 269 
LYS HB3  H  N N 270 
LYS HG2  H  N N 271 
LYS HG3  H  N N 272 
LYS HD2  H  N N 273 
LYS HD3  H  N N 274 
LYS HE2  H  N N 275 
LYS HE3  H  N N 276 
LYS HZ1  H  N N 277 
LYS HZ2  H  N N 278 
LYS HZ3  H  N N 279 
LYS HXT  H  N N 280 
MET N    N  N N 281 
MET CA   C  N S 282 
MET C    C  N N 283 
MET O    O  N N 284 
MET CB   C  N N 285 
MET CG   C  N N 286 
MET SD   S  N N 287 
MET CE   C  N N 288 
MET OXT  O  N N 289 
MET H    H  N N 290 
MET H2   H  N N 291 
MET HA   H  N N 292 
MET HB2  H  N N 293 
MET HB3  H  N N 294 
MET HG2  H  N N 295 
MET HG3  H  N N 296 
MET HE1  H  N N 297 
MET HE2  H  N N 298 
MET HE3  H  N N 299 
MET HXT  H  N N 300 
PHE N    N  N N 301 
PHE CA   C  N S 302 
PHE C    C  N N 303 
PHE O    O  N N 304 
PHE CB   C  N N 305 
PHE CG   C  Y N 306 
PHE CD1  C  Y N 307 
PHE CD2  C  Y N 308 
PHE CE1  C  Y N 309 
PHE CE2  C  Y N 310 
PHE CZ   C  Y N 311 
PHE OXT  O  N N 312 
PHE H    H  N N 313 
PHE H2   H  N N 314 
PHE HA   H  N N 315 
PHE HB2  H  N N 316 
PHE HB3  H  N N 317 
PHE HD1  H  N N 318 
PHE HD2  H  N N 319 
PHE HE1  H  N N 320 
PHE HE2  H  N N 321 
PHE HZ   H  N N 322 
PHE HXT  H  N N 323 
PRO N    N  N N 324 
PRO CA   C  N S 325 
PRO C    C  N N 326 
PRO O    O  N N 327 
PRO CB   C  N N 328 
PRO CG   C  N N 329 
PRO CD   C  N N 330 
PRO OXT  O  N N 331 
PRO H    H  N N 332 
PRO HA   H  N N 333 
PRO HB2  H  N N 334 
PRO HB3  H  N N 335 
PRO HG2  H  N N 336 
PRO HG3  H  N N 337 
PRO HD2  H  N N 338 
PRO HD3  H  N N 339 
PRO HXT  H  N N 340 
SER N    N  N N 341 
SER CA   C  N S 342 
SER C    C  N N 343 
SER O    O  N N 344 
SER CB   C  N N 345 
SER OG   O  N N 346 
SER OXT  O  N N 347 
SER H    H  N N 348 
SER H2   H  N N 349 
SER HA   H  N N 350 
SER HB2  H  N N 351 
SER HB3  H  N N 352 
SER HG   H  N N 353 
SER HXT  H  N N 354 
THR N    N  N N 355 
THR CA   C  N S 356 
THR C    C  N N 357 
THR O    O  N N 358 
THR CB   C  N R 359 
THR OG1  O  N N 360 
THR CG2  C  N N 361 
THR OXT  O  N N 362 
THR H    H  N N 363 
THR H2   H  N N 364 
THR HA   H  N N 365 
THR HB   H  N N 366 
THR HG1  H  N N 367 
THR HG21 H  N N 368 
THR HG22 H  N N 369 
THR HG23 H  N N 370 
THR HXT  H  N N 371 
TRP N    N  N N 372 
TRP CA   C  N S 373 
TRP C    C  N N 374 
TRP O    O  N N 375 
TRP CB   C  N N 376 
TRP CG   C  Y N 377 
TRP CD1  C  Y N 378 
TRP CD2  C  Y N 379 
TRP NE1  N  Y N 380 
TRP CE2  C  Y N 381 
TRP CE3  C  Y N 382 
TRP CZ2  C  Y N 383 
TRP CZ3  C  Y N 384 
TRP CH2  C  Y N 385 
TRP OXT  O  N N 386 
TRP H    H  N N 387 
TRP H2   H  N N 388 
TRP HA   H  N N 389 
TRP HB2  H  N N 390 
TRP HB3  H  N N 391 
TRP HD1  H  N N 392 
TRP HE1  H  N N 393 
TRP HE3  H  N N 394 
TRP HZ2  H  N N 395 
TRP HZ3  H  N N 396 
TRP HH2  H  N N 397 
TRP HXT  H  N N 398 
TYR N    N  N N 399 
TYR CA   C  N S 400 
TYR C    C  N N 401 
TYR O    O  N N 402 
TYR CB   C  N N 403 
TYR CG   C  Y N 404 
TYR CD1  C  Y N 405 
TYR CD2  C  Y N 406 
TYR CE1  C  Y N 407 
TYR CE2  C  Y N 408 
TYR CZ   C  Y N 409 
TYR OH   O  N N 410 
TYR OXT  O  N N 411 
TYR H    H  N N 412 
TYR H2   H  N N 413 
TYR HA   H  N N 414 
TYR HB2  H  N N 415 
TYR HB3  H  N N 416 
TYR HD1  H  N N 417 
TYR HD2  H  N N 418 
TYR HE1  H  N N 419 
TYR HE2  H  N N 420 
TYR HH   H  N N 421 
TYR HXT  H  N N 422 
VAL N    N  N N 423 
VAL CA   C  N S 424 
VAL C    C  N N 425 
VAL O    O  N N 426 
VAL CB   C  N N 427 
VAL CG1  C  N N 428 
VAL CG2  C  N N 429 
VAL OXT  O  N N 430 
VAL H    H  N N 431 
VAL H2   H  N N 432 
VAL HA   H  N N 433 
VAL HB   H  N N 434 
VAL HG11 H  N N 435 
VAL HG12 H  N N 436 
VAL HG13 H  N N 437 
VAL HG21 H  N N 438 
VAL HG22 H  N N 439 
VAL HG23 H  N N 440 
VAL HXT  H  N N 441 
ZN  ZN   ZN N N 442 
# 
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  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
EDO C1  O1   sing N N 83  
EDO C1  C2   sing N N 84  
EDO C1  H11  sing N N 85  
EDO C1  H12  sing N N 86  
EDO O1  HO1  sing N N 87  
EDO C2  O2   sing N N 88  
EDO C2  H21  sing N N 89  
EDO C2  H22  sing N N 90  
EDO O2  HO2  sing N N 91  
GLN N   CA   sing N N 92  
GLN N   H    sing N N 93  
GLN N   H2   sing N N 94  
GLN CA  C    sing N N 95  
GLN CA  CB   sing N N 96  
GLN CA  HA   sing N N 97  
GLN C   O    doub N N 98  
GLN C   OXT  sing N N 99  
GLN CB  CG   sing N N 100 
GLN CB  HB2  sing N N 101 
GLN CB  HB3  sing N N 102 
GLN CG  CD   sing N N 103 
GLN CG  HG2  sing N N 104 
GLN CG  HG3  sing N N 105 
GLN CD  OE1  doub N N 106 
GLN CD  NE2  sing N N 107 
GLN NE2 HE21 sing N N 108 
GLN NE2 HE22 sing N N 109 
GLN OXT HXT  sing N N 110 
GLU N   CA   sing N N 111 
GLU N   H    sing N N 112 
GLU N   H2   sing N N 113 
GLU CA  C    sing N N 114 
GLU CA  CB   sing N N 115 
GLU CA  HA   sing N N 116 
GLU C   O    doub N N 117 
GLU C   OXT  sing N N 118 
GLU CB  CG   sing N N 119 
GLU CB  HB2  sing N N 120 
GLU CB  HB3  sing N N 121 
GLU CG  CD   sing N N 122 
GLU CG  HG2  sing N N 123 
GLU CG  HG3  sing N N 124 
GLU CD  OE1  doub N N 125 
GLU CD  OE2  sing N N 126 
GLU OE2 HE2  sing N N 127 
GLU OXT HXT  sing N N 128 
GLY N   CA   sing N N 129 
GLY N   H    sing N N 130 
GLY N   H2   sing N N 131 
GLY CA  C    sing N N 132 
GLY CA  HA2  sing N N 133 
GLY CA  HA3  sing N N 134 
GLY C   O    doub N N 135 
GLY C   OXT  sing N N 136 
GLY OXT HXT  sing N N 137 
HIS N   CA   sing N N 138 
HIS N   H    sing N N 139 
HIS N   H2   sing N N 140 
HIS CA  C    sing N N 141 
HIS CA  CB   sing N N 142 
HIS CA  HA   sing N N 143 
HIS C   O    doub N N 144 
HIS C   OXT  sing N N 145 
HIS CB  CG   sing N N 146 
HIS CB  HB2  sing N N 147 
HIS CB  HB3  sing N N 148 
HIS CG  ND1  sing Y N 149 
HIS CG  CD2  doub Y N 150 
HIS ND1 CE1  doub Y N 151 
HIS ND1 HD1  sing N N 152 
HIS CD2 NE2  sing Y N 153 
HIS CD2 HD2  sing N N 154 
HIS CE1 NE2  sing Y N 155 
HIS CE1 HE1  sing N N 156 
HIS NE2 HE2  sing N N 157 
HIS OXT HXT  sing N N 158 
HOH O   H1   sing N N 159 
HOH O   H2   sing N N 160 
ILE N   CA   sing N N 161 
ILE N   H    sing N N 162 
ILE N   H2   sing N N 163 
ILE CA  C    sing N N 164 
ILE CA  CB   sing N N 165 
ILE CA  HA   sing N N 166 
ILE C   O    doub N N 167 
ILE C   OXT  sing N N 168 
ILE CB  CG1  sing N N 169 
ILE CB  CG2  sing N N 170 
ILE CB  HB   sing N N 171 
ILE CG1 CD1  sing N N 172 
ILE CG1 HG12 sing N N 173 
ILE CG1 HG13 sing N N 174 
ILE CG2 HG21 sing N N 175 
ILE CG2 HG22 sing N N 176 
ILE CG2 HG23 sing N N 177 
ILE CD1 HD11 sing N N 178 
ILE CD1 HD12 sing N N 179 
ILE CD1 HD13 sing N N 180 
ILE OXT HXT  sing N N 181 
JTW C26 C24  doub Y N 182 
JTW C26 C25  sing Y N 183 
JTW C24 C23  sing Y N 184 
JTW C16 C15  sing N N 185 
JTW C16 O17  sing N N 186 
JTW C25 C21  doub Y N 187 
JTW C15 N14  sing N N 188 
JTW O13 C12  doub N N 189 
JTW C23 C22  doub Y N 190 
JTW C21 C22  sing Y N 191 
JTW C21 S18  sing N N 192 
JTW O20 S18  doub N N 193 
JTW N14 C12  sing N N 194 
JTW C12 C9   sing N N 195 
JTW S18 O19  doub N N 196 
JTW S18 C8   sing N N 197 
JTW C9  C8   doub Y N 198 
JTW C9  C10  sing Y N 199 
JTW C8  C7   sing Y N 200 
JTW C10 C5   doub Y N 201 
JTW C7  C6   doub Y N 202 
JTW C5  C6   sing Y N 203 
JTW C5  S2   sing N N 204 
JTW C6  CL1  sing N N 205 
JTW N1  S2   sing N N 206 
JTW S2  O4   doub N N 207 
JTW S2  O3   doub N N 208 
JTW C22 H1   sing N N 209 
JTW C23 H2   sing N N 210 
JTW C10 H3   sing N N 211 
JTW C25 H4   sing N N 212 
JTW C26 H5   sing N N 213 
JTW C24 H6   sing N N 214 
JTW C7  H7   sing N N 215 
JTW N1  H8   sing N N 216 
JTW N1  H9   sing N N 217 
JTW N14 H10  sing N N 218 
JTW C15 H11  sing N N 219 
JTW C15 H12  sing N N 220 
JTW C16 H13  sing N N 221 
JTW C16 H14  sing N N 222 
JTW O17 H15  sing N N 223 
LEU N   CA   sing N N 224 
LEU N   H    sing N N 225 
LEU N   H2   sing N N 226 
LEU CA  C    sing N N 227 
LEU CA  CB   sing N N 228 
LEU CA  HA   sing N N 229 
LEU C   O    doub N N 230 
LEU C   OXT  sing N N 231 
LEU CB  CG   sing N N 232 
LEU CB  HB2  sing N N 233 
LEU CB  HB3  sing N N 234 
LEU CG  CD1  sing N N 235 
LEU CG  CD2  sing N N 236 
LEU CG  HG   sing N N 237 
LEU CD1 HD11 sing N N 238 
LEU CD1 HD12 sing N N 239 
LEU CD1 HD13 sing N N 240 
LEU CD2 HD21 sing N N 241 
LEU CD2 HD22 sing N N 242 
LEU CD2 HD23 sing N N 243 
LEU OXT HXT  sing N N 244 
LYS N   CA   sing N N 245 
LYS N   H    sing N N 246 
LYS N   H2   sing N N 247 
LYS CA  C    sing N N 248 
LYS CA  CB   sing N N 249 
LYS CA  HA   sing N N 250 
LYS C   O    doub N N 251 
LYS C   OXT  sing N N 252 
LYS CB  CG   sing N N 253 
LYS CB  HB2  sing N N 254 
LYS CB  HB3  sing N N 255 
LYS CG  CD   sing N N 256 
LYS CG  HG2  sing N N 257 
LYS CG  HG3  sing N N 258 
LYS CD  CE   sing N N 259 
LYS CD  HD2  sing N N 260 
LYS CD  HD3  sing N N 261 
LYS CE  NZ   sing N N 262 
LYS CE  HE2  sing N N 263 
LYS CE  HE3  sing N N 264 
LYS NZ  HZ1  sing N N 265 
LYS NZ  HZ2  sing N N 266 
LYS NZ  HZ3  sing N N 267 
LYS OXT HXT  sing N N 268 
MET N   CA   sing N N 269 
MET N   H    sing N N 270 
MET N   H2   sing N N 271 
MET CA  C    sing N N 272 
MET CA  CB   sing N N 273 
MET CA  HA   sing N N 274 
MET C   O    doub N N 275 
MET C   OXT  sing N N 276 
MET CB  CG   sing N N 277 
MET CB  HB2  sing N N 278 
MET CB  HB3  sing N N 279 
MET CG  SD   sing N N 280 
MET CG  HG2  sing N N 281 
MET CG  HG3  sing N N 282 
MET SD  CE   sing N N 283 
MET CE  HE1  sing N N 284 
MET CE  HE2  sing N N 285 
MET CE  HE3  sing N N 286 
MET OXT HXT  sing N N 287 
PHE N   CA   sing N N 288 
PHE N   H    sing N N 289 
PHE N   H2   sing N N 290 
PHE CA  C    sing N N 291 
PHE CA  CB   sing N N 292 
PHE CA  HA   sing N N 293 
PHE C   O    doub N N 294 
PHE C   OXT  sing N N 295 
PHE CB  CG   sing N N 296 
PHE CB  HB2  sing N N 297 
PHE CB  HB3  sing N N 298 
PHE CG  CD1  doub Y N 299 
PHE CG  CD2  sing Y N 300 
PHE CD1 CE1  sing Y N 301 
PHE CD1 HD1  sing N N 302 
PHE CD2 CE2  doub Y N 303 
PHE CD2 HD2  sing N N 304 
PHE CE1 CZ   doub Y N 305 
PHE CE1 HE1  sing N N 306 
PHE CE2 CZ   sing Y N 307 
PHE CE2 HE2  sing N N 308 
PHE CZ  HZ   sing N N 309 
PHE OXT HXT  sing N N 310 
PRO N   CA   sing N N 311 
PRO N   CD   sing N N 312 
PRO N   H    sing N N 313 
PRO CA  C    sing N N 314 
PRO CA  CB   sing N N 315 
PRO CA  HA   sing N N 316 
PRO C   O    doub N N 317 
PRO C   OXT  sing N N 318 
PRO CB  CG   sing N N 319 
PRO CB  HB2  sing N N 320 
PRO CB  HB3  sing N N 321 
PRO CG  CD   sing N N 322 
PRO CG  HG2  sing N N 323 
PRO CG  HG3  sing N N 324 
PRO CD  HD2  sing N N 325 
PRO CD  HD3  sing N N 326 
PRO OXT HXT  sing N N 327 
SER N   CA   sing N N 328 
SER N   H    sing N N 329 
SER N   H2   sing N N 330 
SER CA  C    sing N N 331 
SER CA  CB   sing N N 332 
SER CA  HA   sing N N 333 
SER C   O    doub N N 334 
SER C   OXT  sing N N 335 
SER CB  OG   sing N N 336 
SER CB  HB2  sing N N 337 
SER CB  HB3  sing N N 338 
SER OG  HG   sing N N 339 
SER OXT HXT  sing N N 340 
THR N   CA   sing N N 341 
THR N   H    sing N N 342 
THR N   H2   sing N N 343 
THR CA  C    sing N N 344 
THR CA  CB   sing N N 345 
THR CA  HA   sing N N 346 
THR C   O    doub N N 347 
THR C   OXT  sing N N 348 
THR CB  OG1  sing N N 349 
THR CB  CG2  sing N N 350 
THR CB  HB   sing N N 351 
THR OG1 HG1  sing N N 352 
THR CG2 HG21 sing N N 353 
THR CG2 HG22 sing N N 354 
THR CG2 HG23 sing N N 355 
THR OXT HXT  sing N N 356 
TRP N   CA   sing N N 357 
TRP N   H    sing N N 358 
TRP N   H2   sing N N 359 
TRP CA  C    sing N N 360 
TRP CA  CB   sing N N 361 
TRP CA  HA   sing N N 362 
TRP C   O    doub N N 363 
TRP C   OXT  sing N N 364 
TRP CB  CG   sing N N 365 
TRP CB  HB2  sing N N 366 
TRP CB  HB3  sing N N 367 
TRP CG  CD1  doub Y N 368 
TRP CG  CD2  sing Y N 369 
TRP CD1 NE1  sing Y N 370 
TRP CD1 HD1  sing N N 371 
TRP CD2 CE2  doub Y N 372 
TRP CD2 CE3  sing Y N 373 
TRP NE1 CE2  sing Y N 374 
TRP NE1 HE1  sing N N 375 
TRP CE2 CZ2  sing Y N 376 
TRP CE3 CZ3  doub Y N 377 
TRP CE3 HE3  sing N N 378 
TRP CZ2 CH2  doub Y N 379 
TRP CZ2 HZ2  sing N N 380 
TRP CZ3 CH2  sing Y N 381 
TRP CZ3 HZ3  sing N N 382 
TRP CH2 HH2  sing N N 383 
TRP OXT HXT  sing N N 384 
TYR N   CA   sing N N 385 
TYR N   H    sing N N 386 
TYR N   H2   sing N N 387 
TYR CA  C    sing N N 388 
TYR CA  CB   sing N N 389 
TYR CA  HA   sing N N 390 
TYR C   O    doub N N 391 
TYR C   OXT  sing N N 392 
TYR CB  CG   sing N N 393 
TYR CB  HB2  sing N N 394 
TYR CB  HB3  sing N N 395 
TYR CG  CD1  doub Y N 396 
TYR CG  CD2  sing Y N 397 
TYR CD1 CE1  sing Y N 398 
TYR CD1 HD1  sing N N 399 
TYR CD2 CE2  doub Y N 400 
TYR CD2 HD2  sing N N 401 
TYR CE1 CZ   doub Y N 402 
TYR CE1 HE1  sing N N 403 
TYR CE2 CZ   sing Y N 404 
TYR CE2 HE2  sing N N 405 
TYR CZ  OH   sing N N 406 
TYR OH  HH   sing N N 407 
TYR OXT HXT  sing N N 408 
VAL N   CA   sing N N 409 
VAL N   H    sing N N 410 
VAL N   H2   sing N N 411 
VAL CA  C    sing N N 412 
VAL CA  CB   sing N N 413 
VAL CA  HA   sing N N 414 
VAL C   O    doub N N 415 
VAL C   OXT  sing N N 416 
VAL CB  CG1  sing N N 417 
VAL CB  CG2  sing N N 418 
VAL CB  HB   sing N N 419 
VAL CG1 HG11 sing N N 420 
VAL CG1 HG12 sing N N 421 
VAL CG1 HG13 sing N N 422 
VAL CG2 HG21 sing N N 423 
VAL CG2 HG22 sing N N 424 
VAL CG2 HG23 sing N N 425 
VAL OXT HXT  sing N N 426 
# 
_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   1JD0 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    6R71 
_atom_sites.fract_transf_matrix[1][1]   0.022180 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.006152 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.014117 
_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]   0.013854 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
# 
loop_
_atom_type.symbol 
C  
CL 
N  
O  
S  
ZN 
# 
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   . LYS A 1 3   ? 1.760   18.811  -0.436  1.00 36.48 ? 3   LYS A N   1 
ATOM   2    C  CA  . LYS A 1 3   ? 1.012   17.573  -0.013  1.00 33.19 ? 3   LYS A CA  1 
ATOM   3    C  C   . LYS A 1 3   ? 1.296   16.428  -0.989  1.00 28.13 ? 3   LYS A C   1 
ATOM   4    O  O   . LYS A 1 3   ? 1.684   16.658  -2.143  1.00 23.78 ? 3   LYS A O   1 
ATOM   5    C  CB  . LYS A 1 3   ? -0.496  17.839  0.134   1.00 42.85 ? 3   LYS A CB  1 
ATOM   6    C  CG  . LYS A 1 3   ? -1.320  17.947  -1.148  1.00 46.05 ? 3   LYS A CG  1 
ATOM   7    C  CD  . LYS A 1 3   ? -1.847  19.354  -1.444  1.00 60.15 ? 3   LYS A CD  1 
ATOM   8    C  CE  . LYS A 1 3   ? -0.826  20.292  -2.072  1.00 65.42 ? 3   LYS A CE  1 
ATOM   9    N  NZ  . LYS A 1 3   ? -1.410  21.569  -2.558  1.00 63.25 ? 3   LYS A NZ  1 
ATOM   10   N  N   . TRP A 1 4   ? 1.053   15.192  -0.517  1.00 18.83 ? 4   TRP A N   1 
ATOM   11   C  CA  . TRP A 1 4   ? 1.295   14.017  -1.345  1.00 15.18 ? 4   TRP A CA  1 
ATOM   12   C  C   . TRP A 1 4   ? 0.440   12.862  -0.832  1.00 13.49 ? 4   TRP A C   1 
ATOM   13   O  O   . TRP A 1 4   ? 0.091   12.819  0.352   1.00 12.69 ? 4   TRP A O   1 
ATOM   14   C  CB  . TRP A 1 4   ? 2.789   13.688  -1.398  1.00 12.87 ? 4   TRP A CB  1 
ATOM   15   C  CG  . TRP A 1 4   ? 3.393   13.344  -0.066  1.00 12.36 ? 4   TRP A CG  1 
ATOM   16   C  CD1 . TRP A 1 4   ? 3.983   14.206  0.813   1.00 12.54 ? 4   TRP A CD1 1 
ATOM   17   C  CD2 . TRP A 1 4   ? 3.462   12.040  0.547   1.00 11.97 ? 4   TRP A CD2 1 
ATOM   18   N  NE1 . TRP A 1 4   ? 4.440   13.534  1.912   1.00 11.48 ? 4   TRP A NE1 1 
ATOM   19   C  CE2 . TRP A 1 4   ? 4.150   12.198  1.773   1.00 12.32 ? 4   TRP A CE2 1 
ATOM   20   C  CE3 . TRP A 1 4   ? 3.044   10.753  0.172   1.00 11.36 ? 4   TRP A CE3 1 
ATOM   21   C  CZ2 . TRP A 1 4   ? 4.377   11.121  2.639   1.00 11.25 ? 4   TRP A CZ2 1 
ATOM   22   C  CZ3 . TRP A 1 4   ? 3.301   9.686   1.012   1.00 11.13 ? 4   TRP A CZ3 1 
ATOM   23   C  CH2 . TRP A 1 4   ? 3.962   9.872   2.227   1.00 10.78 ? 4   TRP A CH2 1 
ATOM   24   N  N   . THR A 1 5   ? 0.049   11.967  -1.746  1.00 12.44 ? 5   THR A N   1 
ATOM   25   C  CA  . THR A 1 5   ? -0.879  10.901  -1.395  1.00 12.78 ? 5   THR A CA  1 
ATOM   26   C  C   . THR A 1 5   ? -0.500  9.646   -2.175  1.00 11.89 ? 5   THR A C   1 
ATOM   27   O  O   . THR A 1 5   ? 0.516   9.637   -2.876  1.00 11.41 ? 5   THR A O   1 
ATOM   28   C  CB  . THR A 1 5   ? -2.333  11.273  -1.732  1.00 13.26 ? 5   THR A CB  1 
ATOM   29   O  OG1 . THR A 1 5   ? -2.367  11.312  -3.155  1.00 14.33 ? 5   THR A OG1 1 
ATOM   30   C  CG2 . THR A 1 5   ? -2.763  12.632  -1.233  1.00 13.80 ? 5   THR A CG2 1 
ATOM   31   N  N   . TYR A 1 6   ? -1.350  8.617   -2.082  1.00 11.07 ? 6   TYR A N   1 
ATOM   32   C  CA  . TYR A 1 6   ? -1.114  7.394   -2.830  1.00 11.99 ? 6   TYR A CA  1 
ATOM   33   C  C   . TYR A 1 6   ? -2.169  7.219   -3.914  1.00 13.42 ? 6   TYR A C   1 
ATOM   34   O  O   . TYR A 1 6   ? -2.212  6.147   -4.523  1.00 12.96 ? 6   TYR A O   1 
ATOM   35   C  CB  . TYR A 1 6   ? -1.069  6.184   -1.889  1.00 10.78 ? 6   TYR A CB  1 
ATOM   36   C  CG  . TYR A 1 6   ? 0.142   6.165   -0.992  1.00 10.36 ? 6   TYR A CG  1 
ATOM   37   C  CD1 . TYR A 1 6   ? 0.097   6.763   0.255   1.00 10.29 ? 6   TYR A CD1 1 
ATOM   38   C  CD2 . TYR A 1 6   ? 1.315   5.514   -1.364  1.00 10.92 ? 6   TYR A CD2 1 
ATOM   39   C  CE1 . TYR A 1 6   ? 1.193   6.758   1.100   1.00 10.28 ? 6   TYR A CE1 1 
ATOM   40   C  CE2 . TYR A 1 6   ? 2.435   5.502   -0.536  1.00 10.49 ? 6   TYR A CE2 1 
ATOM   41   C  CZ  . TYR A 1 6   ? 2.360   6.132   0.699   1.00 10.65 ? 6   TYR A CZ  1 
ATOM   42   O  OH  . TYR A 1 6   ? 3.407   6.129   1.566   1.00 10.61 ? 6   TYR A OH  1 
ATOM   43   N  N   . PHE A 1 7   ? -3.009  8.254   -4.134  1.00 15.13 ? 7   PHE A N   1 
ATOM   44   C  CA  . PHE A 1 7   ? -4.119  8.163   -5.083  1.00 18.18 ? 7   PHE A CA  1 
ATOM   45   C  C   . PHE A 1 7   ? -4.499  9.543   -5.615  1.00 18.88 ? 7   PHE A C   1 
ATOM   46   O  O   . PHE A 1 7   ? -4.568  10.509  -4.850  1.00 20.22 ? 7   PHE A O   1 
ATOM   47   C  CB  . PHE A 1 7   ? -5.351  7.490   -4.456  1.00 21.81 ? 7   PHE A CB  1 
ATOM   48   C  CG  . PHE A 1 7   ? -6.467  7.204   -5.434  1.00 25.65 ? 7   PHE A CG  1 
ATOM   49   C  CD1 . PHE A 1 7   ? -6.276  6.334   -6.503  1.00 27.34 ? 7   PHE A CD1 1 
ATOM   50   C  CD2 . PHE A 1 7   ? -7.702  7.828   -5.313  1.00 27.18 ? 7   PHE A CD2 1 
ATOM   51   C  CE1 . PHE A 1 7   ? -7.290  6.092   -7.421  1.00 28.90 ? 7   PHE A CE1 1 
ATOM   52   C  CE2 . PHE A 1 7   ? -8.717  7.577   -6.229  1.00 29.94 ? 7   PHE A CE2 1 
ATOM   53   C  CZ  . PHE A 1 7   ? -8.512  6.708   -7.278  1.00 29.14 ? 7   PHE A CZ  1 
ATOM   54   N  N   . GLY A 1 8   ? -4.765  9.620   -6.925  1.00 18.27 ? 8   GLY A N   1 
ATOM   55   C  CA  . GLY A 1 8   ? -5.240  10.856  -7.539  1.00 17.48 ? 8   GLY A CA  1 
ATOM   56   C  C   . GLY A 1 8   ? -4.099  11.758  -8.014  1.00 17.19 ? 8   GLY A C   1 
ATOM   57   O  O   . GLY A 1 8   ? -2.968  11.303  -8.200  1.00 15.28 ? 8   GLY A O   1 
ATOM   58   N  N   . PRO A 1 9   ? -4.356  13.070  -8.219  1.00 17.23 ? 9   PRO A N   1 
ATOM   59   C  CA  . PRO A 1 9   ? -3.376  13.950  -8.851  1.00 16.65 ? 9   PRO A CA  1 
ATOM   60   C  C   . PRO A 1 9   ? -2.049  14.042  -8.092  1.00 16.22 ? 9   PRO A C   1 
ATOM   61   O  O   . PRO A 1 9   ? -1.012  14.291  -8.692  1.00 16.33 ? 9   PRO A O   1 
ATOM   62   C  CB  . PRO A 1 9   ? -4.077  15.322  -8.933  1.00 16.80 ? 9   PRO A CB  1 
ATOM   63   C  CG  . PRO A 1 9   ? -5.547  15.024  -8.715  1.00 17.49 ? 9   PRO A CG  1 
ATOM   64   C  CD  . PRO A 1 9   ? -5.603  13.771  -7.866  1.00 17.63 ? 9   PRO A CD  1 
ATOM   65   N  N   . ASP A 1 10  ? -2.081  13.832  -6.773  1.00 15.95 ? 10  ASP A N   1 
ATOM   66   C  CA  . ASP A 1 10  ? -0.885  13.942  -5.940  1.00 15.68 ? 10  ASP A CA  1 
ATOM   67   C  C   . ASP A 1 10  ? -0.327  12.560  -5.559  1.00 13.47 ? 10  ASP A C   1 
ATOM   68   O  O   . ASP A 1 10  ? 0.445   12.447  -4.607  1.00 12.88 ? 10  ASP A O   1 
ATOM   69   C  CB  . ASP A 1 10  ? -1.208  14.720  -4.661  1.00 17.02 ? 10  ASP A CB  1 
ATOM   70   C  CG  . ASP A 1 10  ? -1.314  16.222  -4.900  1.00 19.82 ? 10  ASP A CG  1 
ATOM   71   O  OD1 . ASP A 1 10  ? -0.636  16.719  -5.826  1.00 21.02 ? 10  ASP A OD1 1 
ATOM   72   O  OD2 . ASP A 1 10  ? -2.059  16.881  -4.154  1.00 18.56 ? 10  ASP A OD2 1 
ATOM   73   N  N   . GLY A 1 11  ? -0.747  11.513  -6.279  1.00 12.54 ? 11  GLY A N   1 
ATOM   74   C  CA  . GLY A 1 11  ? -0.231  10.150  -6.124  1.00 10.57 ? 11  GLY A CA  1 
ATOM   75   C  C   . GLY A 1 11  ? 1.224   9.989   -6.589  1.00 9.87  ? 11  GLY A C   1 
ATOM   76   O  O   . GLY A 1 11  ? 1.867   10.930  -7.046  1.00 9.06  ? 11  GLY A O   1 
ATOM   77   N  N   . GLU A 1 12  ? 1.723   8.749   -6.548  1.00 9.37  ? 12  GLU A N   1 
ATOM   78   C  CA  . GLU A 1 12  ? 3.155   8.484   -6.548  1.00 8.65  ? 12  GLU A CA  1 
ATOM   79   C  C   . GLU A 1 12  ? 3.835   8.871   -7.856  1.00 8.33  ? 12  GLU A C   1 
ATOM   80   O  O   . GLU A 1 12  ? 5.039   9.168   -7.844  1.00 8.10  ? 12  GLU A O   1 
ATOM   81   C  CB  . GLU A 1 12  ? 3.468   7.021   -6.197  1.00 8.61  ? 12  GLU A CB  1 
ATOM   82   C  CG  . GLU A 1 12  ? 2.993   6.029   -7.242  1.00 8.77  ? 12  GLU A CG  1 
ATOM   83   C  CD  . GLU A 1 12  ? 2.938   4.625   -6.664  1.00 8.71  ? 12  GLU A CD  1 
ATOM   84   O  OE1 . GLU A 1 12  ? 3.974   3.958   -6.645  1.00 8.76  ? 12  GLU A OE1 1 
ATOM   85   O  OE2 . GLU A 1 12  ? 1.855   4.209   -6.263  1.00 9.36  ? 12  GLU A OE2 1 
ATOM   86   N  N   . ASN A 1 13  ? 3.096   8.851   -8.975  1.00 8.07  ? 13  ASN A N   1 
ATOM   87   C  CA  . ASN A 1 13  ? 3.725   9.195   -10.248 1.00 8.18  ? 13  ASN A CA  1 
ATOM   88   C  C   . ASN A 1 13  ? 3.965   10.709  -10.290 1.00 8.14  ? 13  ASN A C   1 
ATOM   89   O  O   . ASN A 1 13  ? 4.647   11.187  -11.201 1.00 8.63  ? 13  ASN A O   1 
ATOM   90   C  CB  . ASN A 1 13  ? 2.926   8.752   -11.488 1.00 7.70  ? 13  ASN A CB  1 
ATOM   91   C  CG  . ASN A 1 13  ? 2.801   7.245   -11.689 1.00 8.04  ? 13  ASN A CG  1 
ATOM   92   O  OD1 . ASN A 1 13  ? 3.399   6.450   -10.960 1.00 7.88  ? 13  ASN A OD1 1 
ATOM   93   N  ND2 . ASN A 1 13  ? 2.008   6.838   -12.674 1.00 6.97  ? 13  ASN A ND2 1 
ATOM   94   N  N   . SER A 1 14  ? 3.435   11.440  -9.299  1.00 8.12  ? 14  SER A N   1 
ATOM   95   C  CA  . SER A 1 14  ? 3.453   12.908  -9.262  1.00 8.35  ? 14  SER A CA  1 
ATOM   96   C  C   . SER A 1 14  ? 4.394   13.453  -8.189  1.00 8.42  ? 14  SER A C   1 
ATOM   97   O  O   . SER A 1 14  ? 4.714   14.645  -8.194  1.00 8.46  ? 14  SER A O   1 
ATOM   98   C  CB  . SER A 1 14  ? 2.055   13.510  -9.087  1.00 8.41  ? 14  SER A CB  1 
ATOM   99   O  OG  . SER A 1 14  ? 1.244   13.270  -10.234 1.00 8.65  ? 14  SER A OG  1 
ATOM   100  N  N   . TRP A 1 15  ? 4.827   12.585  -7.262  1.00 8.16  ? 15  TRP A N   1 
ATOM   101  C  CA  . TRP A 1 15  ? 5.675   13.041  -6.174  1.00 8.46  ? 15  TRP A CA  1 
ATOM   102  C  C   . TRP A 1 15  ? 6.866   13.829  -6.723  1.00 9.24  ? 15  TRP A C   1 
ATOM   103  O  O   . TRP A 1 15  ? 7.249   14.870  -6.174  1.00 9.93  ? 15  TRP A O   1 
ATOM   104  C  CB  . TRP A 1 15  ? 6.165   11.858  -5.323  1.00 7.26  ? 15  TRP A CB  1 
ATOM   105  C  CG  . TRP A 1 15  ? 5.111   11.104  -4.571  1.00 7.06  ? 15  TRP A CG  1 
ATOM   106  C  CD1 . TRP A 1 15  ? 3.797   11.447  -4.401  1.00 6.74  ? 15  TRP A CD1 1 
ATOM   107  C  CD2 . TRP A 1 15  ? 5.303   9.862   -3.861  1.00 6.67  ? 15  TRP A CD2 1 
ATOM   108  N  NE1 . TRP A 1 15  ? 3.156   10.484  -3.666  1.00 6.74  ? 15  TRP A NE1 1 
ATOM   109  C  CE2 . TRP A 1 15  ? 4.050   9.502   -3.316  1.00 6.59  ? 15  TRP A CE2 1 
ATOM   110  C  CE3 . TRP A 1 15  ? 6.397   8.993   -3.685  1.00 6.80  ? 15  TRP A CE3 1 
ATOM   111  C  CZ2 . TRP A 1 15  ? 3.871   8.347   -2.552  1.00 6.25  ? 15  TRP A CZ2 1 
ATOM   112  C  CZ3 . TRP A 1 15  ? 6.220   7.828   -2.957  1.00 6.45  ? 15  TRP A CZ3 1 
ATOM   113  C  CH2 . TRP A 1 15  ? 4.975   7.533   -2.384  1.00 6.54  ? 15  TRP A CH2 1 
ATOM   114  N  N   . SER A 1 16  ? 7.463   13.327  -7.810  1.00 9.92  ? 16  SER A N   1 
ATOM   115  C  CA  . SER A 1 16  ? 8.653   13.947  -8.383  1.00 11.25 ? 16  SER A CA  1 
ATOM   116  C  C   . SER A 1 16  ? 8.422   15.424  -8.717  1.00 12.49 ? 16  SER A C   1 
ATOM   117  O  O   . SER A 1 16  ? 9.404   16.157  -8.898  1.00 12.93 ? 16  SER A O   1 
ATOM   118  C  CB  . SER A 1 16  ? 9.115   13.208  -9.620  1.00 11.33 ? 16  SER A CB  1 
ATOM   119  O  OG  . SER A 1 16  ? 8.206   13.447  -10.686 1.00 11.36 ? 16  SER A OG  1 
ATOM   120  N  N   . LYS A 1 17  ? 7.148   15.856  -8.842  1.00 12.79 ? 17  LYS A N   1 
ATOM   121  C  CA  . LYS A 1 17  ? 6.868   17.241  -9.232  1.00 12.93 ? 17  LYS A CA  1 
ATOM   122  C  C   . LYS A 1 17  ? 7.246   18.201  -8.096  1.00 14.30 ? 17  LYS A C   1 
ATOM   123  O  O   . LYS A 1 17  ? 7.549   19.382  -8.328  1.00 14.54 ? 17  LYS A O   1 
ATOM   124  C  CB  . LYS A 1 17  ? 5.396   17.479  -9.596  1.00 12.22 ? 17  LYS A CB  1 
ATOM   125  C  CG  . LYS A 1 17  ? 4.799   16.589  -10.685 1.00 11.74 ? 17  LYS A CG  1 
ATOM   126  C  CD  . LYS A 1 17  ? 3.270   16.613  -10.691 1.00 10.40 ? 17  LYS A CD  1 
ATOM   127  C  CE  . LYS A 1 17  ? 2.707   15.883  -11.894 1.00 10.71 ? 17  LYS A CE  1 
ATOM   128  N  NZ  . LYS A 1 17  ? 1.219   15.909  -11.993 1.00 9.68  ? 17  LYS A NZ  1 
ATOM   129  N  N   . LYS A 1 18  ? 7.194   17.690  -6.858  1.00 13.89 ? 18  LYS A N   1 
ATOM   130  C  CA  . LYS A 1 18  ? 7.503   18.507  -5.702  1.00 13.74 ? 18  LYS A CA  1 
ATOM   131  C  C   . LYS A 1 18  ? 8.800   18.054  -5.037  1.00 14.06 ? 18  LYS A C   1 
ATOM   132  O  O   . LYS A 1 18  ? 9.440   18.861  -4.361  1.00 13.14 ? 18  LYS A O   1 
ATOM   133  C  CB  . LYS A 1 18  ? 6.376   18.450  -4.666  1.00 14.01 ? 18  LYS A CB  1 
ATOM   134  C  CG  . LYS A 1 18  ? 4.963   18.666  -5.194  1.00 15.91 ? 18  LYS A CG  1 
ATOM   135  C  CD  . LYS A 1 18  ? 3.991   18.923  -4.067  1.00 17.28 ? 18  LYS A CD  1 
ATOM   136  C  CE  . LYS A 1 18  ? 2.525   18.864  -4.452  1.00 18.49 ? 18  LYS A CE  1 
ATOM   137  N  NZ  . LYS A 1 18  ? 1.791   19.734  -3.509  1.00 19.48 ? 18  LYS A NZ  1 
ATOM   138  N  N   . TYR A 1 19  ? 9.140   16.767  -5.185  1.00 13.08 ? 19  TYR A N   1 
ATOM   139  C  CA  . TYR A 1 19  ? 10.240  16.144  -4.465  1.00 13.73 ? 19  TYR A CA  1 
ATOM   140  C  C   . TYR A 1 19  ? 11.210  15.514  -5.465  1.00 13.46 ? 19  TYR A C   1 
ATOM   141  O  O   . TYR A 1 19  ? 11.084  14.332  -5.795  1.00 13.45 ? 19  TYR A O   1 
ATOM   142  C  CB  . TYR A 1 19  ? 9.685   15.086  -3.506  1.00 14.13 ? 19  TYR A CB  1 
ATOM   143  C  CG  . TYR A 1 19  ? 8.651   15.617  -2.548  1.00 14.77 ? 19  TYR A CG  1 
ATOM   144  C  CD1 . TYR A 1 19  ? 9.033   16.286  -1.388  1.00 16.20 ? 19  TYR A CD1 1 
ATOM   145  C  CD2 . TYR A 1 19  ? 7.294   15.495  -2.816  1.00 15.44 ? 19  TYR A CD2 1 
ATOM   146  C  CE1 . TYR A 1 19  ? 8.092   16.771  -0.488  1.00 16.86 ? 19  TYR A CE1 1 
ATOM   147  C  CE2 . TYR A 1 19  ? 6.338   15.998  -1.943  1.00 15.61 ? 19  TYR A CE2 1 
ATOM   148  C  CZ  . TYR A 1 19  ? 6.744   16.630  -0.778  1.00 17.52 ? 19  TYR A CZ  1 
ATOM   149  O  OH  . TYR A 1 19  ? 5.805   17.119  0.077   1.00 19.80 ? 19  TYR A OH  1 
ATOM   150  N  N   . PRO A 1 20  ? 12.208  16.288  -5.957  1.00 13.28 ? 20  PRO A N   1 
ATOM   151  C  CA  . PRO A 1 20  ? 13.110  15.827  -7.014  1.00 13.07 ? 20  PRO A CA  1 
ATOM   152  C  C   . PRO A 1 20  ? 13.657  14.410  -6.822  1.00 12.70 ? 20  PRO A C   1 
ATOM   153  O  O   . PRO A 1 20  ? 13.813  13.671  -7.802  1.00 12.22 ? 20  PRO A O   1 
ATOM   154  C  CB  . PRO A 1 20  ? 14.246  16.867  -7.010  1.00 13.75 ? 20  PRO A CB  1 
ATOM   155  C  CG  . PRO A 1 20  ? 13.633  18.134  -6.430  1.00 13.67 ? 20  PRO A CG  1 
ATOM   156  C  CD  . PRO A 1 20  ? 12.472  17.686  -5.559  1.00 13.53 ? 20  PRO A CD  1 
ATOM   157  N  N   . SER A 1 21  ? 13.949  14.025  -5.568  1.00 11.64 ? 21  SER A N   1 
ATOM   158  C  CA  . SER A 1 21  ? 14.572  12.720  -5.358  1.00 11.69 ? 21  SER A CA  1 
ATOM   159  C  C   . SER A 1 21  ? 13.658  11.528  -5.673  1.00 10.78 ? 21  SER A C   1 
ATOM   160  O  O   . SER A 1 21  ? 14.148  10.445  -6.019  1.00 10.74 ? 21  SER A O   1 
ATOM   161  C  CB  . SER A 1 21  ? 15.186  12.615  -3.997  1.00 12.59 ? 21  SER A CB  1 
ATOM   162  O  OG  . SER A 1 21  ? 16.281  13.498  -3.911  1.00 12.65 ? 21  SER A OG  1 
ATOM   163  N  N   . CYS A 1 22  ? 12.331  11.734  -5.618  1.00 10.53 ? 22  CYS A N   1 
ATOM   164  C  CA  . CYS A 1 22  ? 11.379  10.702  -6.002  1.00 10.47 ? 22  CYS A CA  1 
ATOM   165  C  C   . CYS A 1 22  ? 11.516  10.336  -7.473  1.00 11.52 ? 22  CYS A C   1 
ATOM   166  O  O   . CYS A 1 22  ? 11.147  9.234   -7.871  1.00 10.82 ? 22  CYS A O   1 
ATOM   167  C  CB  . CYS A 1 22  ? 9.945   11.137  -5.735  1.00 9.78  ? 22  CYS A CB  1 
ATOM   168  S  SG  . CYS A 1 22  ? 9.690   11.467  -3.972  1.00 9.68  ? 22  CYS A SG  1 
ATOM   169  N  N   . GLY A 1 23  ? 11.997  11.290  -8.285  1.00 13.02 ? 23  GLY A N   1 
ATOM   170  C  CA  . GLY A 1 23  ? 12.268  11.030  -9.697  1.00 14.48 ? 23  GLY A CA  1 
ATOM   171  C  C   . GLY A 1 23  ? 13.724  10.648  -9.966  1.00 15.28 ? 23  GLY A C   1 
ATOM   172  O  O   . GLY A 1 23  ? 14.156  10.578  -11.120 1.00 18.61 ? 23  GLY A O   1 
ATOM   173  N  N   . GLY A 1 24  ? 14.464  10.352  -8.897  1.00 15.30 ? 24  GLY A N   1 
ATOM   174  C  CA  . GLY A 1 24  ? 15.890  10.081  -8.990  1.00 14.66 ? 24  GLY A CA  1 
ATOM   175  C  C   . GLY A 1 24  ? 16.226  8.588   -8.985  1.00 13.94 ? 24  GLY A C   1 
ATOM   176  O  O   . GLY A 1 24  ? 15.371  7.730   -9.193  1.00 13.50 ? 24  GLY A O   1 
ATOM   177  N  N   . LEU A 1 25  ? 17.492  8.291   -8.717  1.00 14.51 ? 25  LEU A N   1 
ATOM   178  C  CA  . LEU A 1 25  ? 17.985  6.918   -8.740  1.00 14.49 ? 25  LEU A CA  1 
ATOM   179  C  C   . LEU A 1 25  ? 17.778  6.236   -7.394  1.00 13.26 ? 25  LEU A C   1 
ATOM   180  O  O   . LEU A 1 25  ? 17.588  6.901   -6.377  1.00 13.11 ? 25  LEU A O   1 
ATOM   181  C  CB  . LEU A 1 25  ? 19.486  6.953   -9.070  1.00 15.46 ? 25  LEU A CB  1 
ATOM   182  C  CG  . LEU A 1 25  ? 19.810  7.400   -10.493 1.00 16.47 ? 25  LEU A CG  1 
ATOM   183  C  CD1 . LEU A 1 25  ? 21.315  7.624   -10.640 1.00 17.60 ? 25  LEU A CD1 1 
ATOM   184  C  CD2 . LEU A 1 25  ? 19.287  6.374   -11.503 1.00 16.26 ? 25  LEU A CD2 1 
ATOM   185  N  N   . LEU A 1 26  ? 17.913  4.903   -7.406  1.00 13.44 ? 26  LEU A N   1 
ATOM   186  C  CA  . LEU A 1 26  ? 18.140  4.085   -6.217  1.00 13.27 ? 26  LEU A CA  1 
ATOM   187  C  C   . LEU A 1 26  ? 16.875  4.102   -5.369  1.00 11.71 ? 26  LEU A C   1 
ATOM   188  O  O   . LEU A 1 26  ? 16.920  4.193   -4.149  1.00 11.35 ? 26  LEU A O   1 
ATOM   189  C  CB  . LEU A 1 26  ? 19.315  4.636   -5.395  1.00 15.07 ? 26  LEU A CB  1 
ATOM   190  C  CG  . LEU A 1 26  ? 20.742  4.472   -5.940  1.00 19.36 ? 26  LEU A CG  1 
ATOM   191  C  CD1 . LEU A 1 26  ? 21.747  4.776   -4.823  1.00 20.36 ? 26  LEU A CD1 1 
ATOM   192  C  CD2 . LEU A 1 26  ? 20.987  3.070   -6.493  1.00 19.56 ? 26  LEU A CD2 1 
ATOM   193  N  N   . GLN A 1 27  ? 15.729  4.028   -6.027  1.00 10.75 ? 27  GLN A N   1 
ATOM   194  C  CA  . GLN A 1 27  ? 14.471  4.149   -5.314  1.00 9.35  ? 27  GLN A CA  1 
ATOM   195  C  C   . GLN A 1 27  ? 14.050  2.817   -4.694  1.00 9.27  ? 27  GLN A C   1 
ATOM   196  O  O   . GLN A 1 27  ? 14.303  1.745   -5.260  1.00 9.54  ? 27  GLN A O   1 
ATOM   197  C  CB  . GLN A 1 27  ? 13.432  4.744   -6.268  1.00 8.88  ? 27  GLN A CB  1 
ATOM   198  C  CG  . GLN A 1 27  ? 13.726  6.186   -6.660  1.00 8.51  ? 27  GLN A CG  1 
ATOM   199  C  CD  . GLN A 1 27  ? 13.581  7.142   -5.506  1.00 8.32  ? 27  GLN A CD  1 
ATOM   200  O  OE1 . GLN A 1 27  ? 12.487  7.510   -5.092  1.00 8.35  ? 27  GLN A OE1 1 
ATOM   201  N  NE2 . GLN A 1 27  ? 14.710  7.515   -4.939  1.00 8.74  ? 27  GLN A NE2 1 
ATOM   202  N  N   . SER A 1 28  ? 13.324  2.908   -3.563  1.00 8.96  ? 28  SER A N   1 
ATOM   203  C  CA  . SER A 1 28  ? 12.662  1.790   -2.897  1.00 8.63  ? 28  SER A CA  1 
ATOM   204  C  C   . SER A 1 28  ? 11.140  1.999   -2.931  1.00 8.58  ? 28  SER A C   1 
ATOM   205  O  O   . SER A 1 28  ? 10.661  3.134   -3.057  1.00 8.37  ? 28  SER A O   1 
ATOM   206  C  CB  . SER A 1 28  ? 13.137  1.656   -1.456  1.00 8.68  ? 28  SER A CB  1 
ATOM   207  O  OG  . SER A 1 28  ? 14.510  1.299   -1.364  1.00 8.39  ? 28  SER A OG  1 
ATOM   208  N  N   . PRO A 1 29  ? 10.310  0.930   -2.817  1.00 8.30  ? 29  PRO A N   1 
ATOM   209  C  CA  . PRO A 1 29  ? 10.793  -0.446  -2.663  1.00 8.08  ? 29  PRO A CA  1 
ATOM   210  C  C   . PRO A 1 29  ? 11.109  -1.153  -3.976  1.00 7.83  ? 29  PRO A C   1 
ATOM   211  O  O   . PRO A 1 29  ? 11.049  -0.552  -5.046  1.00 7.25  ? 29  PRO A O   1 
ATOM   212  C  CB  . PRO A 1 29  ? 9.584   -1.107  -1.975  1.00 8.03  ? 29  PRO A CB  1 
ATOM   213  C  CG  . PRO A 1 29  ? 8.399   -0.451  -2.664  1.00 8.25  ? 29  PRO A CG  1 
ATOM   214  C  CD  . PRO A 1 29  ? 8.837   0.999   -2.838  1.00 8.11  ? 29  PRO A CD  1 
ATOM   215  N  N   . ILE A 1 30  ? 11.449  -2.447  -3.877  1.00 8.35  ? 30  ILE A N   1 
ATOM   216  C  CA  . ILE A 1 30  ? 11.872  -3.246  -5.022  1.00 9.02  ? 30  ILE A CA  1 
ATOM   217  C  C   . ILE A 1 30  ? 11.272  -4.636  -4.869  1.00 8.86  ? 30  ILE A C   1 
ATOM   218  O  O   . ILE A 1 30  ? 10.858  -5.011  -3.764  1.00 8.73  ? 30  ILE A O   1 
ATOM   219  C  CB  . ILE A 1 30  ? 13.417  -3.336  -5.137  1.00 9.12  ? 30  ILE A CB  1 
ATOM   220  C  CG1 . ILE A 1 30  ? 14.035  -3.834  -3.820  1.00 10.03 ? 30  ILE A CG1 1 
ATOM   221  C  CG2 . ILE A 1 30  ? 13.996  -2.007  -5.622  1.00 9.10  ? 30  ILE A CG2 1 
ATOM   222  C  CD1 . ILE A 1 30  ? 15.462  -4.360  -3.868  1.00 10.71 ? 30  ILE A CD1 1 
ATOM   223  N  N   . ASP A 1 31  ? 11.248  -5.374  -5.980  1.00 9.01  ? 31  ASP A N   1 
ATOM   224  C  CA  . ASP A 1 31  ? 10.760  -6.748  -5.997  1.00 9.79  ? 31  ASP A CA  1 
ATOM   225  C  C   . ASP A 1 31  ? 11.930  -7.700  -5.765  1.00 10.57 ? 31  ASP A C   1 
ATOM   226  O  O   . ASP A 1 31  ? 12.891  -7.731  -6.543  1.00 12.06 ? 31  ASP A O   1 
ATOM   227  C  CB  . ASP A 1 31  ? 10.120  -7.122  -7.343  1.00 9.70  ? 31  ASP A CB  1 
ATOM   228  C  CG  . ASP A 1 31  ? 9.715   -8.587  -7.342  1.00 10.28 ? 31  ASP A CG  1 
ATOM   229  O  OD1 . ASP A 1 31  ? 8.968   -8.981  -6.431  1.00 9.90  ? 31  ASP A OD1 1 
ATOM   230  O  OD2 . ASP A 1 31  ? 10.245  -9.349  -8.187  1.00 11.32 ? 31  ASP A OD2 1 
ATOM   231  N  N   . LEU A 1 32  ? 11.816  -8.543  -4.741  1.00 10.31 ? 32  LEU A N   1 
ATOM   232  C  CA  . LEU A 1 32  ? 12.911  -9.435  -4.403  1.00 9.56  ? 32  LEU A CA  1 
ATOM   233  C  C   . LEU A 1 32  ? 12.730  -10.708 -5.221  1.00 9.66  ? 32  LEU A C   1 
ATOM   234  O  O   . LEU A 1 32  ? 11.708  -11.380 -5.085  1.00 9.96  ? 32  LEU A O   1 
ATOM   235  C  CB  . LEU A 1 32  ? 12.886  -9.699  -2.895  1.00 8.96  ? 32  LEU A CB  1 
ATOM   236  C  CG  . LEU A 1 32  ? 13.012  -8.433  -2.046  1.00 9.34  ? 32  LEU A CG  1 
ATOM   237  C  CD1 . LEU A 1 32  ? 12.464  -8.638  -0.629  1.00 9.43  ? 32  LEU A CD1 1 
ATOM   238  C  CD2 . LEU A 1 32  ? 14.451  -7.928  -2.030  1.00 8.51  ? 32  LEU A CD2 1 
ATOM   239  N  N   . HIS A 1 33  ? 13.722  -11.012 -6.067  1.00 9.37  ? 33  HIS A N   1 
ATOM   240  C  CA  . HIS A 1 33  ? 13.653  -12.201 -6.911  1.00 10.56 ? 33  HIS A CA  1 
ATOM   241  C  C   . HIS A 1 33  ? 15.043  -12.646 -7.350  1.00 10.59 ? 33  HIS A C   1 
ATOM   242  O  O   . HIS A 1 33  ? 15.981  -11.844 -7.360  1.00 9.81  ? 33  HIS A O   1 
ATOM   243  C  CB  . HIS A 1 33  ? 12.706  -11.985 -8.096  1.00 10.82 ? 33  HIS A CB  1 
ATOM   244  C  CG  . HIS A 1 33  ? 13.201  -11.001 -9.100  1.00 11.38 ? 33  HIS A CG  1 
ATOM   245  N  ND1 . HIS A 1 33  ? 13.156  -9.639  -8.875  1.00 12.10 ? 33  HIS A ND1 1 
ATOM   246  C  CD2 . HIS A 1 33  ? 13.712  -11.176 -10.341 1.00 11.81 ? 33  HIS A CD2 1 
ATOM   247  C  CE1 . HIS A 1 33  ? 13.625  -9.014  -9.938  1.00 12.67 ? 33  HIS A CE1 1 
ATOM   248  N  NE2 . HIS A 1 33  ? 13.978  -9.936  -10.849 1.00 12.36 ? 33  HIS A NE2 1 
ATOM   249  N  N   . SER A 1 34  ? 15.135  -13.917 -7.776  1.00 11.20 ? 34  SER A N   1 
ATOM   250  C  CA  . SER A 1 34  ? 16.407  -14.627 -7.735  1.00 11.96 ? 34  SER A CA  1 
ATOM   251  C  C   . SER A 1 34  ? 17.439  -13.940 -8.631  1.00 12.07 ? 34  SER A C   1 
ATOM   252  O  O   . SER A 1 34  ? 18.628  -13.909 -8.306  1.00 10.98 ? 34  SER A O   1 
ATOM   253  C  CB  . SER A 1 34  ? 16.235  -16.100 -8.085  1.00 12.40 ? 34  SER A CB  1 
ATOM   254  O  OG  . SER A 1 34  ? 15.787  -16.192 -9.439  1.00 13.53 ? 34  SER A OG  1 
ATOM   255  N  N   . ASP A 1 35  ? 16.985  -13.340 -9.741  1.00 12.41 ? 35  ASP A N   1 
ATOM   256  C  CA  . ASP A 1 35  ? 17.940  -12.841 -10.730 1.00 12.80 ? 35  ASP A CA  1 
ATOM   257  C  C   . ASP A 1 35  ? 18.856  -11.748 -10.175 1.00 12.24 ? 35  ASP A C   1 
ATOM   258  O  O   . ASP A 1 35  ? 19.946  -11.520 -10.702 1.00 12.76 ? 35  ASP A O   1 
ATOM   259  C  CB  . ASP A 1 35  ? 17.224  -12.311 -11.974 1.00 14.02 ? 35  ASP A CB  1 
ATOM   260  C  CG  . ASP A 1 35  ? 16.344  -13.359 -12.633 1.00 15.24 ? 35  ASP A CG  1 
ATOM   261  O  OD1 . ASP A 1 35  ? 15.269  -13.684 -12.051 1.00 13.32 ? 35  ASP A OD1 1 
ATOM   262  O  OD2 . ASP A 1 35  ? 16.754  -13.862 -13.700 1.00 17.33 ? 35  ASP A OD2 1 
ATOM   263  N  N   . ILE A 1 36  ? 18.375  -11.006 -9.175  1.00 11.70 ? 36  ILE A N   1 
ATOM   264  C  CA  . ILE A 1 36  ? 19.038  -9.796  -8.706  1.00 11.60 ? 36  ILE A CA  1 
ATOM   265  C  C   . ILE A 1 36  ? 19.544  -10.010 -7.275  1.00 12.55 ? 36  ILE A C   1 
ATOM   266  O  O   . ILE A 1 36  ? 19.992  -9.070  -6.613  1.00 11.65 ? 36  ILE A O   1 
ATOM   267  C  CB  . ILE A 1 36  ? 18.080  -8.582  -8.839  1.00 11.57 ? 36  ILE A CB  1 
ATOM   268  C  CG1 . ILE A 1 36  ? 16.696  -8.808  -8.210  1.00 11.06 ? 36  ILE A CG1 1 
ATOM   269  C  CG2 . ILE A 1 36  ? 17.922  -8.181  -10.297 1.00 11.15 ? 36  ILE A CG2 1 
ATOM   270  C  CD1 . ILE A 1 36  ? 16.664  -8.693  -6.719  1.00 11.09 ? 36  ILE A CD1 1 
ATOM   271  N  N   . LEU A 1 37  ? 19.489  -11.261 -6.807  1.00 13.17 ? 37  LEU A N   1 
ATOM   272  C  CA  . LEU A 1 37  ? 19.968  -11.627 -5.481  1.00 14.18 ? 37  LEU A CA  1 
ATOM   273  C  C   . LEU A 1 37  ? 21.383  -12.184 -5.564  1.00 15.54 ? 37  LEU A C   1 
ATOM   274  O  O   . LEU A 1 37  ? 21.692  -13.003 -6.443  1.00 16.53 ? 37  LEU A O   1 
ATOM   275  C  CB  . LEU A 1 37  ? 19.085  -12.752 -4.944  1.00 14.95 ? 37  LEU A CB  1 
ATOM   276  C  CG  . LEU A 1 37  ? 17.621  -12.421 -4.668  1.00 13.79 ? 37  LEU A CG  1 
ATOM   277  C  CD1 . LEU A 1 37  ? 16.992  -13.649 -4.033  1.00 14.44 ? 37  LEU A CD1 1 
ATOM   278  C  CD2 . LEU A 1 37  ? 17.496  -11.210 -3.760  1.00 13.58 ? 37  LEU A CD2 1 
ATOM   279  N  N   . GLN A 1 38  ? 22.202  -11.811 -4.578  1.00 16.31 ? 38  GLN A N   1 
ATOM   280  C  CA  . GLN A 1 38  ? 23.528  -12.387 -4.411  1.00 17.51 ? 38  GLN A CA  1 
ATOM   281  C  C   . GLN A 1 38  ? 23.720  -12.793 -2.944  1.00 16.93 ? 38  GLN A C   1 
ATOM   282  O  O   . GLN A 1 38  ? 23.635  -11.967 -2.037  1.00 14.18 ? 38  GLN A O   1 
ATOM   283  C  CB  . GLN A 1 38  ? 24.575  -11.362 -4.841  1.00 19.45 ? 38  GLN A CB  1 
ATOM   284  C  CG  . GLN A 1 38  ? 25.993  -11.779 -4.478  1.00 25.81 ? 38  GLN A CG  1 
ATOM   285  C  CD  . GLN A 1 38  ? 26.989  -11.395 -5.538  1.00 30.13 ? 38  GLN A CD  1 
ATOM   286  O  OE1 . GLN A 1 38  ? 26.991  -11.945 -6.642  1.00 32.19 ? 38  GLN A OE1 1 
ATOM   287  N  NE2 . GLN A 1 38  ? 27.847  -10.442 -5.201  1.00 33.49 ? 38  GLN A NE2 1 
ATOM   288  N  N   . TYR A 1 39  ? 23.995  -14.079 -2.713  1.00 16.24 ? 39  TYR A N   1 
ATOM   289  C  CA  . TYR A 1 39  ? 24.337  -14.515 -1.371  1.00 16.39 ? 39  TYR A CA  1 
ATOM   290  C  C   . TYR A 1 39  ? 25.617  -13.813 -0.921  1.00 16.69 ? 39  TYR A C   1 
ATOM   291  O  O   . TYR A 1 39  ? 26.570  -13.683 -1.684  1.00 16.16 ? 39  TYR A O   1 
ATOM   292  C  CB  . TYR A 1 39  ? 24.500  -16.032 -1.331  1.00 16.79 ? 39  TYR A CB  1 
ATOM   293  C  CG  . TYR A 1 39  ? 25.019  -16.547 -0.017  1.00 18.34 ? 39  TYR A CG  1 
ATOM   294  C  CD1 . TYR A 1 39  ? 24.341  -16.285 1.167   1.00 18.28 ? 39  TYR A CD1 1 
ATOM   295  C  CD2 . TYR A 1 39  ? 26.191  -17.290 0.049   1.00 19.58 ? 39  TYR A CD2 1 
ATOM   296  C  CE1 . TYR A 1 39  ? 24.825  -16.745 2.384   1.00 19.05 ? 39  TYR A CE1 1 
ATOM   297  C  CE2 . TYR A 1 39  ? 26.659  -17.797 1.259   1.00 20.72 ? 39  TYR A CE2 1 
ATOM   298  C  CZ  . TYR A 1 39  ? 25.977  -17.511 2.430   1.00 19.25 ? 39  TYR A CZ  1 
ATOM   299  O  OH  . TYR A 1 39  ? 26.422  -18.000 3.624   1.00 20.73 ? 39  TYR A OH  1 
ATOM   300  N  N   . ASP A 1 40  ? 25.621  -13.313 0.317   1.00 17.05 ? 40  ASP A N   1 
ATOM   301  C  CA  . ASP A 1 40  ? 26.837  -12.746 0.874   1.00 18.39 ? 40  ASP A CA  1 
ATOM   302  C  C   . ASP A 1 40  ? 27.068  -13.350 2.261   1.00 19.88 ? 40  ASP A C   1 
ATOM   303  O  O   . ASP A 1 40  ? 26.377  -12.998 3.218   1.00 16.68 ? 40  ASP A O   1 
ATOM   304  C  CB  . ASP A 1 40  ? 26.822  -11.212 0.845   1.00 17.55 ? 40  ASP A CB  1 
ATOM   305  C  CG  . ASP A 1 40  ? 28.095  -10.559 1.388   1.00 19.52 ? 40  ASP A CG  1 
ATOM   306  O  OD1 . ASP A 1 40  ? 28.918  -11.268 2.014   1.00 18.85 ? 40  ASP A OD1 1 
ATOM   307  O  OD2 . ASP A 1 40  ? 28.242  -9.330  1.224   1.00 18.88 ? 40  ASP A OD2 1 
ATOM   308  N  N   . ALA A 1 41  ? 28.093  -14.218 2.345   1.00 22.30 ? 41  ALA A N   1 
ATOM   309  C  CA  . ALA A 1 41  ? 28.440  -14.981 3.541   1.00 23.11 ? 41  ALA A CA  1 
ATOM   310  C  C   . ALA A 1 41  ? 28.890  -14.047 4.658   1.00 22.78 ? 41  ALA A C   1 
ATOM   311  O  O   . ALA A 1 41  ? 28.830  -14.411 5.825   1.00 23.41 ? 41  ALA A O   1 
ATOM   312  C  CB  . ALA A 1 41  ? 29.513  -16.003 3.228   1.00 23.70 ? 41  ALA A CB  1 
ATOM   313  N  N   . SER A 1 42  ? 29.282  -12.826 4.281   1.00 22.94 ? 42  SER A N   1 
ATOM   314  C  CA  . SER A 1 42  ? 29.772  -11.833 5.221   1.00 22.62 ? 42  SER A CA  1 
ATOM   315  C  C   . SER A 1 42  ? 28.643  -11.200 6.048   1.00 23.18 ? 42  SER A C   1 
ATOM   316  O  O   . SER A 1 42  ? 28.936  -10.528 7.040   1.00 23.87 ? 42  SER A O   1 
ATOM   317  C  CB  . SER A 1 42  ? 30.588  -10.777 4.503   1.00 24.36 ? 42  SER A CB  1 
ATOM   318  O  OG  . SER A 1 42  ? 29.762  -9.709  4.044   1.00 23.99 ? 42  SER A OG  1 
ATOM   319  N  N   . LEU A 1 43  ? 27.367  -11.411 5.667   1.00 18.70 ? 43  LEU A N   1 
ATOM   320  C  CA  . LEU A 1 43  ? 26.265  -10.750 6.351   1.00 16.78 ? 43  LEU A CA  1 
ATOM   321  C  C   . LEU A 1 43  ? 25.854  -11.504 7.619   1.00 16.43 ? 43  LEU A C   1 
ATOM   322  O  O   . LEU A 1 43  ? 25.186  -12.530 7.539   1.00 16.32 ? 43  LEU A O   1 
ATOM   323  C  CB  . LEU A 1 43  ? 25.077  -10.623 5.394   1.00 15.78 ? 43  LEU A CB  1 
ATOM   324  C  CG  . LEU A 1 43  ? 25.274  -9.727  4.169   1.00 15.29 ? 43  LEU A CG  1 
ATOM   325  C  CD1 . LEU A 1 43  ? 24.030  -9.782  3.288   1.00 14.43 ? 43  LEU A CD1 1 
ATOM   326  C  CD2 . LEU A 1 43  ? 25.559  -8.284  4.589   1.00 15.72 ? 43  LEU A CD2 1 
ATOM   327  N  N   . THR A 1 44  ? 26.174  -10.931 8.785   1.00 15.60 ? 44  THR A N   1 
ATOM   328  C  CA  . THR A 1 44  ? 25.984  -11.560 10.086  1.00 16.72 ? 44  THR A CA  1 
ATOM   329  C  C   . THR A 1 44  ? 24.695  -11.063 10.760  1.00 16.42 ? 44  THR A C   1 
ATOM   330  O  O   . THR A 1 44  ? 24.154  -10.026 10.378  1.00 16.22 ? 44  THR A O   1 
ATOM   331  C  CB  . THR A 1 44  ? 27.186  -11.245 10.986  1.00 17.74 ? 44  THR A CB  1 
ATOM   332  O  OG1 . THR A 1 44  ? 27.384  -9.823  10.925  1.00 18.52 ? 44  THR A OG1 1 
ATOM   333  C  CG2 . THR A 1 44  ? 28.441  -11.980 10.555  1.00 18.68 ? 44  THR A CG2 1 
ATOM   334  N  N   . PRO A 1 45  ? 24.179  -11.745 11.812  1.00 17.47 ? 45  PRO A N   1 
ATOM   335  C  CA  . PRO A 1 45  ? 22.908  -11.364 12.425  1.00 18.28 ? 45  PRO A CA  1 
ATOM   336  C  C   . PRO A 1 45  ? 23.001  -10.001 13.106  1.00 17.85 ? 45  PRO A C   1 
ATOM   337  O  O   . PRO A 1 45  ? 24.025  -9.641  13.683  1.00 15.93 ? 45  PRO A O   1 
ATOM   338  C  CB  . PRO A 1 45  ? 22.668  -12.463 13.477  1.00 18.36 ? 45  PRO A CB  1 
ATOM   339  C  CG  . PRO A 1 45  ? 23.490  -13.624 12.959  1.00 18.12 ? 45  PRO A CG  1 
ATOM   340  C  CD  . PRO A 1 45  ? 24.757  -12.930 12.483  1.00 18.26 ? 45  PRO A CD  1 
ATOM   341  N  N   . LEU A 1 46  ? 21.898  -9.264  13.029  1.00 18.04 ? 46  LEU A N   1 
ATOM   342  C  CA  . LEU A 1 46  ? 21.766  -8.027  13.772  1.00 19.68 ? 46  LEU A CA  1 
ATOM   343  C  C   . LEU A 1 46  ? 21.414  -8.344  15.223  1.00 19.79 ? 46  LEU A C   1 
ATOM   344  O  O   . LEU A 1 46  ? 20.801  -9.373  15.506  1.00 20.25 ? 46  LEU A O   1 
ATOM   345  C  CB  . LEU A 1 46  ? 20.696  -7.175  13.087  1.00 18.38 ? 46  LEU A CB  1 
ATOM   346  C  CG  . LEU A 1 46  ? 21.059  -6.770  11.662  1.00 20.16 ? 46  LEU A CG  1 
ATOM   347  C  CD1 . LEU A 1 46  ? 19.958  -5.922  11.046  1.00 20.54 ? 46  LEU A CD1 1 
ATOM   348  C  CD2 . LEU A 1 46  ? 22.404  -6.041  11.643  1.00 21.23 ? 46  LEU A CD2 1 
ATOM   349  N  N   . GLU A 1 47  ? 21.840  -7.447  16.117  1.00 19.99 ? 47  GLU A N   1 
ATOM   350  C  CA  . GLU A 1 47  ? 21.434  -7.454  17.515  1.00 22.14 ? 47  GLU A CA  1 
ATOM   351  C  C   . GLU A 1 47  ? 20.559  -6.228  17.756  1.00 18.96 ? 47  GLU A C   1 
ATOM   352  O  O   . GLU A 1 47  ? 20.844  -5.150  17.239  1.00 19.11 ? 47  GLU A O   1 
ATOM   353  C  CB  . GLU A 1 47  ? 22.667  -7.400  18.421  1.00 25.70 ? 47  GLU A CB  1 
ATOM   354  C  CG  . GLU A 1 47  ? 23.572  -8.610  18.278  1.00 32.20 ? 47  GLU A CG  1 
ATOM   355  C  CD  . GLU A 1 47  ? 23.371  -9.663  19.360  1.00 39.92 ? 47  GLU A CD  1 
ATOM   356  O  OE1 . GLU A 1 47  ? 22.193  -10.017 19.635  1.00 40.47 ? 47  GLU A OE1 1 
ATOM   357  O  OE2 . GLU A 1 47  ? 24.395  -10.111 19.951  1.00 44.55 ? 47  GLU A OE2 1 
ATOM   358  N  N   . PHE A 1 48  ? 19.481  -6.429  18.502  1.00 16.95 ? 48  PHE A N   1 
ATOM   359  C  CA  . PHE A 1 48  ? 18.500  -5.385  18.740  1.00 16.72 ? 48  PHE A CA  1 
ATOM   360  C  C   . PHE A 1 48  ? 18.624  -4.973  20.201  1.00 16.78 ? 48  PHE A C   1 
ATOM   361  O  O   . PHE A 1 48  ? 18.290  -5.768  21.071  1.00 17.83 ? 48  PHE A O   1 
ATOM   362  C  CB  . PHE A 1 48  ? 17.115  -5.915  18.361  1.00 15.62 ? 48  PHE A CB  1 
ATOM   363  C  CG  . PHE A 1 48  ? 17.141  -6.638  17.041  1.00 15.40 ? 48  PHE A CG  1 
ATOM   364  C  CD1 . PHE A 1 48  ? 17.267  -5.925  15.856  1.00 14.59 ? 48  PHE A CD1 1 
ATOM   365  C  CD2 . PHE A 1 48  ? 17.099  -8.025  16.984  1.00 14.33 ? 48  PHE A CD2 1 
ATOM   366  C  CE1 . PHE A 1 48  ? 17.336  -6.587  14.641  1.00 16.45 ? 48  PHE A CE1 1 
ATOM   367  C  CE2 . PHE A 1 48  ? 17.160  -8.684  15.767  1.00 15.01 ? 48  PHE A CE2 1 
ATOM   368  C  CZ  . PHE A 1 48  ? 17.282  -7.975  14.597  1.00 14.76 ? 48  PHE A CZ  1 
ATOM   369  N  N   . GLN A 1 49  ? 19.175  -3.769  20.444  1.00 16.25 ? 49  GLN A N   1 
ATOM   370  C  CA  . GLN A 1 49  ? 19.498  -3.282  21.782  1.00 15.88 ? 49  GLN A CA  1 
ATOM   371  C  C   . GLN A 1 49  ? 18.474  -2.240  22.216  1.00 14.55 ? 49  GLN A C   1 
ATOM   372  O  O   . GLN A 1 49  ? 18.095  -1.366  21.436  1.00 13.89 ? 49  GLN A O   1 
ATOM   373  C  CB  . GLN A 1 49  ? 20.841  -2.540  21.835  1.00 18.48 ? 49  GLN A CB  1 
ATOM   374  C  CG  . GLN A 1 49  ? 22.074  -3.359  21.500  1.00 20.52 ? 49  GLN A CG  1 
ATOM   375  C  CD  . GLN A 1 49  ? 22.109  -4.694  22.197  1.00 25.80 ? 49  GLN A CD  1 
ATOM   376  O  OE1 . GLN A 1 49  ? 22.031  -5.734  21.552  1.00 30.93 ? 49  GLN A OE1 1 
ATOM   377  N  NE2 . GLN A 1 49  ? 22.229  -4.690  23.516  1.00 25.09 ? 49  GLN A NE2 1 
ATOM   378  N  N   . GLY A 1 50  ? 18.040  -2.340  23.478  1.00 14.46 ? 50  GLY A N   1 
ATOM   379  C  CA  . GLY A 1 50  ? 17.091  -1.396  24.054  1.00 13.55 ? 50  GLY A CA  1 
ATOM   380  C  C   . GLY A 1 50  ? 15.701  -1.495  23.427  1.00 13.35 ? 50  GLY A C   1 
ATOM   381  O  O   . GLY A 1 50  ? 14.912  -0.572  23.585  1.00 14.47 ? 50  GLY A O   1 
ATOM   382  N  N   . TYR A 1 51  ? 15.412  -2.595  22.713  1.00 12.11 ? 51  TYR A N   1 
ATOM   383  C  CA  . TYR A 1 51  ? 14.150  -2.762  22.007  1.00 11.82 ? 51  TYR A CA  1 
ATOM   384  C  C   . TYR A 1 51  ? 13.008  -3.048  22.990  1.00 12.11 ? 51  TYR A C   1 
ATOM   385  O  O   . TYR A 1 51  ? 11.842  -2.875  22.668  1.00 10.63 ? 51  TYR A O   1 
ATOM   386  C  CB  . TYR A 1 51  ? 14.252  -3.867  20.947  1.00 10.88 ? 51  TYR A CB  1 
ATOM   387  C  CG  . TYR A 1 51  ? 14.575  -3.394  19.544  1.00 10.00 ? 51  TYR A CG  1 
ATOM   388  C  CD1 . TYR A 1 51  ? 15.676  -2.581  19.291  1.00 9.59  ? 51  TYR A CD1 1 
ATOM   389  C  CD2 . TYR A 1 51  ? 13.842  -3.839  18.448  1.00 9.65  ? 51  TYR A CD2 1 
ATOM   390  C  CE1 . TYR A 1 51  ? 15.983  -2.136  18.013  1.00 9.31  ? 51  TYR A CE1 1 
ATOM   391  C  CE2 . TYR A 1 51  ? 14.147  -3.420  17.150  1.00 9.78  ? 51  TYR A CE2 1 
ATOM   392  C  CZ  . TYR A 1 51  ? 15.211  -2.558  16.937  1.00 9.61  ? 51  TYR A CZ  1 
ATOM   393  O  OH  . TYR A 1 51  ? 15.518  -2.144  15.671  1.00 10.57 ? 51  TYR A OH  1 
ATOM   394  N  N   . ASN A 1 52  ? 13.357  -3.499  24.192  1.00 13.16 ? 52  ASN A N   1 
ATOM   395  C  CA  . ASN A 1 52  ? 12.355  -3.757  25.208  1.00 15.12 ? 52  ASN A CA  1 
ATOM   396  C  C   . ASN A 1 52  ? 12.047  -2.460  25.957  1.00 14.68 ? 52  ASN A C   1 
ATOM   397  O  O   . ASN A 1 52  ? 12.702  -2.183  26.960  1.00 14.59 ? 52  ASN A O   1 
ATOM   398  C  CB  . ASN A 1 52  ? 12.862  -4.824  26.185  1.00 17.55 ? 52  ASN A CB  1 
ATOM   399  C  CG  . ASN A 1 52  ? 11.763  -5.363  27.072  1.00 20.82 ? 52  ASN A CG  1 
ATOM   400  O  OD1 . ASN A 1 52  ? 10.605  -5.377  26.677  1.00 23.08 ? 52  ASN A OD1 1 
ATOM   401  N  ND2 . ASN A 1 52  ? 12.117  -5.823  28.262  1.00 23.93 ? 52  ASN A ND2 1 
ATOM   402  N  N   . LEU A 1 53  ? 11.057  -1.694  25.469  1.00 13.15 ? 53  LEU A N   1 
ATOM   403  C  CA  . LEU A 1 53  ? 10.687  -0.390  26.015  1.00 12.87 ? 53  LEU A CA  1 
ATOM   404  C  C   . LEU A 1 53  ? 9.908   -0.575  27.321  1.00 13.28 ? 53  LEU A C   1 
ATOM   405  O  O   . LEU A 1 53  ? 9.046   -1.451  27.433  1.00 11.91 ? 53  LEU A O   1 
ATOM   406  C  CB  . LEU A 1 53  ? 9.828   0.379   25.002  1.00 12.88 ? 53  LEU A CB  1 
ATOM   407  C  CG  . LEU A 1 53  ? 10.383  0.504   23.575  1.00 13.21 ? 53  LEU A CG  1 
ATOM   408  C  CD1 . LEU A 1 53  ? 9.447   1.328   22.711  1.00 14.21 ? 53  LEU A CD1 1 
ATOM   409  C  CD2 . LEU A 1 53  ? 11.775  1.117   23.581  1.00 13.16 ? 53  LEU A CD2 1 
ATOM   410  N  N   . SER A 1 54  ? 10.216  0.277   28.307  1.00 13.06 ? 54  SER A N   1 
ATOM   411  C  CA  . SER A 1 54  ? 9.603   0.216   29.626  1.00 13.04 ? 54  SER A CA  1 
ATOM   412  C  C   . SER A 1 54  ? 8.108   0.513   29.529  1.00 13.17 ? 54  SER A C   1 
ATOM   413  O  O   . SER A 1 54  ? 7.709   1.536   28.969  1.00 12.04 ? 54  SER A O   1 
ATOM   414  C  CB  . SER A 1 54  ? 10.251  1.220   30.550  1.00 13.45 ? 54  SER A CB  1 
ATOM   415  O  OG  . SER A 1 54  ? 9.654   1.116   31.841  1.00 13.94 ? 54  SER A OG  1 
ATOM   416  N  N   . ALA A 1 55  ? 7.309   -0.353  30.154  1.00 13.24 ? 55  ALA A N   1 
ATOM   417  C  CA  . ALA A 1 55  ? 5.862   -0.188  30.273  1.00 14.58 ? 55  ALA A CA  1 
ATOM   418  C  C   . ALA A 1 55  ? 5.508   1.077   31.052  1.00 14.62 ? 55  ALA A C   1 
ATOM   419  O  O   . ALA A 1 55  ? 4.362   1.516   31.025  1.00 15.33 ? 55  ALA A O   1 
ATOM   420  C  CB  . ALA A 1 55  ? 5.284   -1.417  30.951  1.00 14.46 ? 55  ALA A CB  1 
ATOM   421  N  N   . ASN A 1 56  ? 6.498   1.657   31.749  1.00 14.54 ? 56  ASN A N   1 
ATOM   422  C  CA  . ASN A 1 56  ? 6.285   2.820   32.596  1.00 14.43 ? 56  ASN A CA  1 
ATOM   423  C  C   . ASN A 1 56  ? 6.572   4.103   31.820  1.00 15.67 ? 56  ASN A C   1 
ATOM   424  O  O   . ASN A 1 56  ? 6.373   5.210   32.322  1.00 15.14 ? 56  ASN A O   1 
ATOM   425  C  CB  . ASN A 1 56  ? 7.204   2.808   33.812  1.00 15.05 ? 56  ASN A CB  1 
ATOM   426  C  CG  . ASN A 1 56  ? 6.765   1.807   34.853  1.00 15.69 ? 56  ASN A CG  1 
ATOM   427  O  OD1 . ASN A 1 56  ? 5.585   1.474   34.934  1.00 15.76 ? 56  ASN A OD1 1 
ATOM   428  N  ND2 . ASN A 1 56  ? 7.710   1.307   35.636  1.00 17.06 ? 56  ASN A ND2 1 
ATOM   429  N  N   . LYS A 1 57  ? 7.075   3.945   30.597  1.00 16.19 ? 57  LYS A N   1 
ATOM   430  C  CA  . LYS A 1 57  ? 7.291   5.110   29.755  1.00 16.95 ? 57  LYS A CA  1 
ATOM   431  C  C   . LYS A 1 57  ? 6.250   5.093   28.636  1.00 16.52 ? 57  LYS A C   1 
ATOM   432  O  O   . LYS A 1 57  ? 5.679   4.050   28.355  1.00 15.47 ? 57  LYS A O   1 
ATOM   433  C  CB  . LYS A 1 57  ? 8.694   5.048   29.164  1.00 17.54 ? 57  LYS A CB  1 
ATOM   434  C  CG  . LYS A 1 57  ? 9.838   5.315   30.122  1.00 19.22 ? 57  LYS A CG  1 
ATOM   435  C  CD  . LYS A 1 57  ? 11.096  5.386   29.302  1.00 21.65 ? 57  LYS A CD  1 
ATOM   436  C  CE  . LYS A 1 57  ? 12.067  6.470   29.718  1.00 23.66 ? 57  LYS A CE  1 
ATOM   437  N  NZ  . LYS A 1 57  ? 13.448  5.920   29.652  1.00 24.37 ? 57  LYS A NZ  1 
ATOM   438  N  N   . GLN A 1 58  ? 6.001   6.253   28.027  1.00 16.49 ? 58  GLN A N   1 
ATOM   439  C  CA  . GLN A 1 58  ? 4.988   6.377   26.988  1.00 17.90 ? 58  GLN A CA  1 
ATOM   440  C  C   . GLN A 1 58  ? 5.650   6.834   25.692  1.00 16.46 ? 58  GLN A C   1 
ATOM   441  O  O   . GLN A 1 58  ? 6.615   7.597   25.723  1.00 17.54 ? 58  GLN A O   1 
ATOM   442  C  CB  . GLN A 1 58  ? 4.010   7.487   27.380  1.00 20.91 ? 58  GLN A CB  1 
ATOM   443  C  CG  . GLN A 1 58  ? 3.156   7.145   28.586  1.00 23.16 ? 58  GLN A CG  1 
ATOM   444  C  CD  . GLN A 1 58  ? 2.306   8.331   28.967  1.00 26.66 ? 58  GLN A CD  1 
ATOM   445  O  OE1 . GLN A 1 58  ? 2.810   9.412   29.293  1.00 29.67 ? 58  GLN A OE1 1 
ATOM   446  N  NE2 . GLN A 1 58  ? 0.997   8.130   28.908  1.00 27.80 ? 58  GLN A NE2 1 
ATOM   447  N  N   . PHE A 1 59  ? 5.110   6.368   24.564  1.00 14.24 ? 59  PHE A N   1 
ATOM   448  C  CA  . PHE A 1 59  ? 5.636   6.691   23.244  1.00 12.92 ? 59  PHE A CA  1 
ATOM   449  C  C   . PHE A 1 59  ? 4.507   7.249   22.377  1.00 11.88 ? 59  PHE A C   1 
ATOM   450  O  O   . PHE A 1 59  ? 3.393   6.730   22.381  1.00 11.76 ? 59  PHE A O   1 
ATOM   451  C  CB  . PHE A 1 59  ? 6.382   5.478   22.669  1.00 12.04 ? 59  PHE A CB  1 
ATOM   452  C  CG  . PHE A 1 59  ? 7.484   5.043   23.605  1.00 12.34 ? 59  PHE A CG  1 
ATOM   453  C  CD1 . PHE A 1 59  ? 7.216   4.219   24.695  1.00 12.91 ? 59  PHE A CD1 1 
ATOM   454  C  CD2 . PHE A 1 59  ? 8.758   5.572   23.473  1.00 12.05 ? 59  PHE A CD2 1 
ATOM   455  C  CE1 . PHE A 1 59  ? 8.221   3.881   25.598  1.00 12.72 ? 59  PHE A CE1 1 
ATOM   456  C  CE2 . PHE A 1 59  ? 9.762   5.231   24.372  1.00 13.35 ? 59  PHE A CE2 1 
ATOM   457  C  CZ  . PHE A 1 59  ? 9.493   4.385   25.427  1.00 13.05 ? 59  PHE A CZ  1 
ATOM   458  N  N   . LEU A 1 60  ? 4.812   8.333   21.662  1.00 11.80 ? 60  LEU A N   1 
ATOM   459  C  CA  . LEU A 1 60  ? 3.810   9.083   20.931  1.00 11.74 ? 60  LEU A CA  1 
ATOM   460  C  C   . LEU A 1 60  ? 3.477   8.347   19.635  1.00 11.11 ? 60  LEU A C   1 
ATOM   461  O  O   . LEU A 1 60  ? 4.352   8.035   18.816  1.00 9.97  ? 60  LEU A O   1 
ATOM   462  C  CB  . LEU A 1 60  ? 4.352   10.477  20.600  1.00 13.55 ? 60  LEU A CB  1 
ATOM   463  C  CG  . LEU A 1 60  ? 3.351   11.372  19.877  1.00 14.44 ? 60  LEU A CG  1 
ATOM   464  C  CD1 . LEU A 1 60  ? 2.277   11.843  20.859  1.00 15.85 ? 60  LEU A CD1 1 
ATOM   465  C  CD2 . LEU A 1 60  ? 4.047   12.570  19.239  1.00 16.05 ? 60  LEU A CD2 1 
ATOM   466  N  N   . LEU A 1 61  ? 2.186   8.073   19.496  1.00 11.11 ? 61  LEU A N   1 
ATOM   467  C  CA  . LEU A 1 61  ? 1.621   7.530   18.274  1.00 11.03 ? 61  LEU A CA  1 
ATOM   468  C  C   . LEU A 1 61  ? 0.867   8.660   17.594  1.00 11.60 ? 61  LEU A C   1 
ATOM   469  O  O   . LEU A 1 61  ? 0.064   9.330   18.242  1.00 12.27 ? 61  LEU A O   1 
ATOM   470  C  CB  . LEU A 1 61  ? 0.681   6.377   18.637  1.00 10.47 ? 61  LEU A CB  1 
ATOM   471  C  CG  . LEU A 1 61  ? 0.222   5.534   17.446  1.00 10.58 ? 61  LEU A CG  1 
ATOM   472  C  CD1 . LEU A 1 61  ? 1.342   4.588   17.032  1.00 9.96  ? 61  LEU A CD1 1 
ATOM   473  C  CD2 . LEU A 1 61  ? -1.032  4.749   17.788  1.00 10.97 ? 61  LEU A CD2 1 
ATOM   474  N  N   . THR A 1 62  ? 1.150   8.851   16.304  1.00 12.65 ? 62  THR A N   1 
ATOM   475  C  CA  . THR A 1 62  ? 0.553   9.926   15.533  1.00 12.73 ? 62  THR A CA  1 
ATOM   476  C  C   . THR A 1 62  ? 0.033   9.398   14.201  1.00 11.83 ? 62  THR A C   1 
ATOM   477  O  O   . THR A 1 62  ? 0.708   8.651   13.490  1.00 11.38 ? 62  THR A O   1 
ATOM   478  C  CB  . THR A 1 62  ? 1.607   10.975  15.146  1.00 13.47 ? 62  THR A CB  1 
ATOM   479  O  OG1 . THR A 1 62  ? 2.346   11.359  16.296  1.00 15.56 ? 62  THR A OG1 1 
ATOM   480  C  CG2 . THR A 1 62  ? 1.031   12.224  14.515  1.00 13.78 ? 62  THR A CG2 1 
ATOM   481  N  N   . ASN A 1 63  ? -1.161  9.878   13.834  1.00 11.29 ? 63  ASN A N   1 
ATOM   482  C  CA  . ASN A 1 63  ? -1.588  9.847   12.451  1.00 10.37 ? 63  ASN A CA  1 
ATOM   483  C  C   . ASN A 1 63  ? -0.937  11.040  11.736  1.00 10.19 ? 63  ASN A C   1 
ATOM   484  O  O   . ASN A 1 63  ? -1.327  12.189  11.960  1.00 9.09  ? 63  ASN A O   1 
ATOM   485  C  CB  . ASN A 1 63  ? -3.123  9.774   12.402  1.00 9.63  ? 63  ASN A CB  1 
ATOM   486  C  CG  . ASN A 1 63  ? -3.707  9.731   11.007  1.00 10.00 ? 63  ASN A CG  1 
ATOM   487  O  OD1 . ASN A 1 63  ? -3.081  10.183  10.036  1.00 9.67  ? 63  ASN A OD1 1 
ATOM   488  N  ND2 . ASN A 1 63  ? -4.946  9.261   10.912  1.00 9.83  ? 63  ASN A ND2 1 
ATOM   489  N  N   . ASN A 1 64  ? 0.040   10.776  10.843  1.00 10.36 ? 64  ASN A N   1 
ATOM   490  C  CA  . ASN A 1 64  ? 0.690   11.890  10.163  1.00 10.39 ? 64  ASN A CA  1 
ATOM   491  C  C   . ASN A 1 64  ? 0.021   12.172  8.828   1.00 10.48 ? 64  ASN A C   1 
ATOM   492  O  O   . ASN A 1 64  ? 0.547   12.942  8.033   1.00 10.30 ? 64  ASN A O   1 
ATOM   493  C  CB  . ASN A 1 64  ? 2.197   11.734  9.976   1.00 10.29 ? 64  ASN A CB  1 
ATOM   494  C  CG  . ASN A 1 64  ? 2.575   10.481  9.203   1.00 10.39 ? 64  ASN A CG  1 
ATOM   495  O  OD1 . ASN A 1 64  ? 1.796   9.972   8.400   1.00 9.80  ? 64  ASN A OD1 1 
ATOM   496  N  ND2 . ASN A 1 64  ? 3.777   9.978   9.442   1.00 10.50 ? 64  ASN A ND2 1 
ATOM   497  N  N   . GLY A 1 65  ? -1.084  11.468  8.557   1.00 11.31 ? 65  GLY A N   1 
ATOM   498  C  CA  . GLY A 1 65  ? -1.785  11.600  7.294   1.00 11.48 ? 65  GLY A CA  1 
ATOM   499  C  C   . GLY A 1 65  ? -1.285  10.616  6.229   1.00 12.87 ? 65  GLY A C   1 
ATOM   500  O  O   . GLY A 1 65  ? -1.917  10.461  5.176   1.00 12.77 ? 65  GLY A O   1 
ATOM   501  N  N   . HIS A 1 66  ? -0.141  9.972   6.483   1.00 11.26 ? 66  HIS A N   1 
ATOM   502  C  CA  . HIS A 1 66  ? 0.426   9.084   5.479   1.00 10.87 ? 66  HIS A CA  1 
ATOM   503  C  C   . HIS A 1 66  ? 0.509   7.659   6.014   1.00 10.11 ? 66  HIS A C   1 
ATOM   504  O  O   . HIS A 1 66  ? 0.521   6.684   5.253   1.00 10.51 ? 66  HIS A O   1 
ATOM   505  C  CB  . HIS A 1 66  ? 1.809   9.622   5.062   1.00 11.82 ? 66  HIS A CB  1 
ATOM   506  C  CG  . HIS A 1 66  ? 1.727   11.004  4.519   1.00 12.00 ? 66  HIS A CG  1 
ATOM   507  N  ND1 . HIS A 1 66  ? 1.132   11.267  3.293   1.00 12.39 ? 66  HIS A ND1 1 
ATOM   508  C  CD2 . HIS A 1 66  ? 2.125   12.190  5.023   1.00 11.86 ? 66  HIS A CD2 1 
ATOM   509  C  CE1 . HIS A 1 66  ? 1.151   12.567  3.067   1.00 12.07 ? 66  HIS A CE1 1 
ATOM   510  N  NE2 . HIS A 1 66  ? 1.775   13.144  4.104   1.00 12.51 ? 66  HIS A NE2 1 
ATOM   511  N  N   . SER A 1 67  ? 0.578   7.547   7.337   1.00 9.05  ? 67  SER A N   1 
ATOM   512  C  CA  . SER A 1 67  ? 0.689   6.268   8.018   1.00 8.51  ? 67  SER A CA  1 
ATOM   513  C  C   . SER A 1 67  ? 0.367   6.527   9.482   1.00 8.43  ? 67  SER A C   1 
ATOM   514  O  O   . SER A 1 67  ? 0.059   7.656   9.859   1.00 8.33  ? 67  SER A O   1 
ATOM   515  C  CB  . SER A 1 67  ? 2.090   5.671   7.830   1.00 8.38  ? 67  SER A CB  1 
ATOM   516  O  OG  . SER A 1 67  ? 2.214   4.393   8.459   1.00 8.14  ? 67  SER A OG  1 
ATOM   517  N  N   . VAL A 1 68  ? 0.359   5.476   10.291  1.00 8.66  ? 68  VAL A N   1 
ATOM   518  C  CA  . VAL A 1 68  ? 0.397   5.695   11.718  1.00 9.57  ? 68  VAL A CA  1 
ATOM   519  C  C   . VAL A 1 68  ? 1.840   5.422   12.129  1.00 10.30 ? 68  VAL A C   1 
ATOM   520  O  O   . VAL A 1 68  ? 2.382   4.395   11.755  1.00 10.14 ? 68  VAL A O   1 
ATOM   521  C  CB  . VAL A 1 68  ? -0.612  4.804   12.473  1.00 8.83  ? 68  VAL A CB  1 
ATOM   522  C  CG1 . VAL A 1 68  ? -0.366  3.314   12.267  1.00 8.67  ? 68  VAL A CG1 1 
ATOM   523  C  CG2 . VAL A 1 68  ? -0.615  5.111   13.954  1.00 9.62  ? 68  VAL A CG2 1 
ATOM   524  N  N   . LYS A 1 69  ? 2.431   6.357   12.882  1.00 11.22 ? 69  LYS A N   1 
ATOM   525  C  CA  . LYS A 1 69  ? 3.818   6.293   13.297  1.00 12.30 ? 69  LYS A CA  1 
ATOM   526  C  C   . LYS A 1 69  ? 3.911   6.301   14.816  1.00 11.45 ? 69  LYS A C   1 
ATOM   527  O  O   . LYS A 1 69  ? 3.278   7.121   15.476  1.00 12.62 ? 69  LYS A O   1 
ATOM   528  C  CB  . LYS A 1 69  ? 4.641   7.408   12.639  1.00 14.27 ? 69  LYS A CB  1 
ATOM   529  C  CG  . LYS A 1 69  ? 5.654   8.121   13.510  1.00 17.82 ? 69  LYS A CG  1 
ATOM   530  C  CD  . LYS A 1 69  ? 6.215   9.385   12.880  1.00 20.13 ? 69  LYS A CD  1 
ATOM   531  C  CE  . LYS A 1 69  ? 6.097   10.588  13.794  1.00 20.61 ? 69  LYS A CE  1 
ATOM   532  N  NZ  . LYS A 1 69  ? 6.416   11.820  13.034  1.00 23.62 ? 69  LYS A NZ  1 
ATOM   533  N  N   . LEU A 1 70  ? 4.757   5.405   15.330  1.00 10.42 ? 70  LEU A N   1 
ATOM   534  C  CA  . LEU A 1 70  ? 5.149   5.394   16.728  1.00 10.54 ? 70  LEU A CA  1 
ATOM   535  C  C   . LEU A 1 70  ? 6.568   5.962   16.875  1.00 10.71 ? 70  LEU A C   1 
ATOM   536  O  O   . LEU A 1 70  ? 7.508   5.456   16.286  1.00 10.28 ? 70  LEU A O   1 
ATOM   537  C  CB  . LEU A 1 70  ? 5.079   3.952   17.232  1.00 10.09 ? 70  LEU A CB  1 
ATOM   538  C  CG  . LEU A 1 70  ? 5.423   3.776   18.713  1.00 10.19 ? 70  LEU A CG  1 
ATOM   539  C  CD1 . LEU A 1 70  ? 4.416   4.545   19.578  1.00 9.83  ? 70  LEU A CD1 1 
ATOM   540  C  CD2 . LEU A 1 70  ? 5.462   2.297   19.065  1.00 9.09  ? 70  LEU A CD2 1 
ATOM   541  N  N   . ASN A 1 71  ? 6.726   7.021   17.678  1.00 11.42 ? 71  ASN A N   1 
ATOM   542  C  CA  . ASN A 1 71  ? 8.046   7.526   18.039  1.00 12.16 ? 71  ASN A CA  1 
ATOM   543  C  C   . ASN A 1 71  ? 8.834   6.507   18.877  1.00 11.80 ? 71  ASN A C   1 
ATOM   544  O  O   . ASN A 1 71  ? 8.314   5.864   19.783  1.00 12.85 ? 71  ASN A O   1 
ATOM   545  C  CB  . ASN A 1 71  ? 7.987   8.864   18.778  1.00 12.13 ? 71  ASN A CB  1 
ATOM   546  C  CG  . ASN A 1 71  ? 7.783   10.070  17.886  1.00 14.00 ? 71  ASN A CG  1 
ATOM   547  O  OD1 . ASN A 1 71  ? 7.701   9.947   16.671  1.00 13.97 ? 71  ASN A OD1 1 
ATOM   548  N  ND2 . ASN A 1 71  ? 7.700   11.246  18.492  1.00 15.22 ? 71  ASN A ND2 1 
ATOM   549  N  N   . LEU A 1 72  ? 10.130  6.397   18.597  1.00 11.13 ? 72  LEU A N   1 
ATOM   550  C  CA  . LEU A 1 72  ? 10.971  5.486   19.353  1.00 11.06 ? 72  LEU A CA  1 
ATOM   551  C  C   . LEU A 1 72  ? 12.145  6.278   19.920  1.00 11.35 ? 72  LEU A C   1 
ATOM   552  O  O   . LEU A 1 72  ? 12.545  7.288   19.339  1.00 12.09 ? 72  LEU A O   1 
ATOM   553  C  CB  . LEU A 1 72  ? 11.440  4.353   18.439  1.00 10.46 ? 72  LEU A CB  1 
ATOM   554  C  CG  . LEU A 1 72  ? 10.328  3.499   17.832  1.00 9.70  ? 72  LEU A CG  1 
ATOM   555  C  CD1 . LEU A 1 72  ? 10.901  2.604   16.739  1.00 8.87  ? 72  LEU A CD1 1 
ATOM   556  C  CD2 . LEU A 1 72  ? 9.660   2.677   18.926  1.00 8.72  ? 72  LEU A CD2 1 
ATOM   557  N  N   . PRO A 1 73  ? 12.682  5.870   21.088  1.00 11.68 ? 73  PRO A N   1 
ATOM   558  C  CA  . PRO A 1 73  ? 13.761  6.611   21.742  1.00 12.01 ? 73  PRO A CA  1 
ATOM   559  C  C   . PRO A 1 73  ? 15.111  6.192   21.154  1.00 12.63 ? 73  PRO A C   1 
ATOM   560  O  O   . PRO A 1 73  ? 15.302  5.048   20.718  1.00 12.95 ? 73  PRO A O   1 
ATOM   561  C  CB  . PRO A 1 73  ? 13.593  6.117   23.188  1.00 11.53 ? 73  PRO A CB  1 
ATOM   562  C  CG  . PRO A 1 73  ? 13.241  4.650   23.009  1.00 10.68 ? 73  PRO A CG  1 
ATOM   563  C  CD  . PRO A 1 73  ? 12.308  4.642   21.819  1.00 11.03 ? 73  PRO A CD  1 
ATOM   564  N  N   . SER A 1 74  ? 16.053  7.129   21.139  1.00 14.27 ? 74  SER A N   1 
ATOM   565  C  CA  . SER A 1 74  ? 17.364  6.881   20.549  1.00 17.20 ? 74  SER A CA  1 
ATOM   566  C  C   . SER A 1 74  ? 18.231  5.916   21.376  1.00 18.41 ? 74  SER A C   1 
ATOM   567  O  O   . SER A 1 74  ? 19.308  5.525   20.916  1.00 18.79 ? 74  SER A O   1 
ATOM   568  C  CB  . SER A 1 74  ? 18.074  8.167   20.328  1.00 18.85 ? 74  SER A CB  1 
ATOM   569  O  OG  . SER A 1 74  ? 18.385  8.730   21.582  1.00 22.74 ? 74  SER A OG  1 
ATOM   570  N  N   . ASP A 1 75  ? 17.781  5.519   22.580  1.00 17.18 ? 75  ASP A N   1 
ATOM   571  C  CA  . ASP A 1 75  ? 18.508  4.498   23.326  1.00 19.64 ? 75  ASP A CA  1 
ATOM   572  C  C   . ASP A 1 75  ? 18.171  3.108   22.776  1.00 18.43 ? 75  ASP A C   1 
ATOM   573  O  O   . ASP A 1 75  ? 18.718  2.095   23.192  1.00 18.76 ? 75  ASP A O   1 
ATOM   574  C  CB  . ASP A 1 75  ? 18.424  4.692   24.844  1.00 22.83 ? 75  ASP A CB  1 
ATOM   575  C  CG  . ASP A 1 75  ? 17.030  4.587   25.436  1.00 28.06 ? 75  ASP A CG  1 
ATOM   576  O  OD1 . ASP A 1 75  ? 16.177  3.898   24.852  1.00 28.54 ? 75  ASP A OD1 1 
ATOM   577  O  OD2 . ASP A 1 75  ? 16.805  5.206   26.489  1.00 34.09 ? 75  ASP A OD2 1 
ATOM   578  N  N   . MET A 1 76  ? 17.294  3.075   21.780  1.00 16.66 ? 76  MET A N   1 
ATOM   579  C  CA  . MET A 1 76  ? 16.979  1.835   21.093  1.00 15.00 ? 76  MET A CA  1 
ATOM   580  C  C   . MET A 1 76  ? 17.866  1.785   19.857  1.00 13.96 ? 76  MET A C   1 
ATOM   581  O  O   . MET A 1 76  ? 17.962  2.777   19.140  1.00 13.22 ? 76  MET A O   1 
ATOM   582  C  CB  . MET A 1 76  ? 15.502  1.916   20.704  1.00 14.72 ? 76  MET A CB  1 
ATOM   583  C  CG  . MET A 1 76  ? 15.008  0.750   19.945  1.00 15.43 ? 76  MET A CG  1 
ATOM   584  S  SD  . MET A 1 76  ? 13.212  0.857   19.837  1.00 16.03 ? 76  MET A SD  1 
ATOM   585  C  CE  . MET A 1 76  ? 13.022  -0.152  18.368  1.00 13.77 ? 76  MET A CE  1 
ATOM   586  N  N   . HIS A 1 77  ? 18.616  0.692   19.656  1.00 14.57 ? 77  HIS A N   1 
ATOM   587  C  CA  . HIS A 1 77  ? 19.573  0.720   18.555  1.00 15.32 ? 77  HIS A CA  1 
ATOM   588  C  C   . HIS A 1 77  ? 19.905  -0.682  18.057  1.00 16.10 ? 77  HIS A C   1 
ATOM   589  O  O   . HIS A 1 77  ? 19.739  -1.685  18.763  1.00 16.48 ? 77  HIS A O   1 
ATOM   590  C  CB  . HIS A 1 77  ? 20.840  1.520   18.901  1.00 17.12 ? 77  HIS A CB  1 
ATOM   591  C  CG  . HIS A 1 77  ? 21.617  0.973   20.057  1.00 18.57 ? 77  HIS A CG  1 
ATOM   592  N  ND1 . HIS A 1 77  ? 21.180  1.094   21.379  1.00 20.75 ? 77  HIS A ND1 1 
ATOM   593  C  CD2 . HIS A 1 77  ? 22.789  0.308   20.108  1.00 19.09 ? 77  HIS A CD2 1 
ATOM   594  C  CE1 . HIS A 1 77  ? 22.059  0.523   22.191  1.00 20.02 ? 77  HIS A CE1 1 
ATOM   595  N  NE2 . HIS A 1 77  ? 23.058  0.041   21.436  1.00 21.94 ? 77  HIS A NE2 1 
ATOM   596  N  N   . ILE A 1 78  ? 20.353  -0.728  16.806  1.00 17.04 ? 78  ILE A N   1 
ATOM   597  C  CA  . ILE A 1 78  ? 20.780  -1.996  16.255  1.00 19.36 ? 78  ILE A CA  1 
ATOM   598  C  C   . ILE A 1 78  ? 22.306  -2.072  16.255  1.00 20.15 ? 78  ILE A C   1 
ATOM   599  O  O   . ILE A 1 78  ? 22.994  -1.071  16.046  1.00 19.70 ? 78  ILE A O   1 
ATOM   600  C  CB  . ILE A 1 78  ? 20.107  -2.297  14.899  1.00 21.70 ? 78  ILE A CB  1 
ATOM   601  C  CG1 . ILE A 1 78  ? 20.383  -1.257  13.819  1.00 22.59 ? 78  ILE A CG1 1 
ATOM   602  C  CG2 . ILE A 1 78  ? 18.606  -2.451  15.091  1.00 24.73 ? 78  ILE A CG2 1 
ATOM   603  C  CD1 . ILE A 1 78  ? 19.283  -1.212  12.773  1.00 21.76 ? 78  ILE A CD1 1 
ATOM   604  N  N   . GLN A 1 79  ? 22.797  -3.283  16.517  1.00 20.78 ? 79  GLN A N   1 
ATOM   605  C  CA  . GLN A 1 79  ? 24.217  -3.577  16.550  1.00 24.41 ? 79  GLN A CA  1 
ATOM   606  C  C   . GLN A 1 79  ? 24.486  -4.582  15.438  1.00 24.37 ? 79  GLN A C   1 
ATOM   607  O  O   . GLN A 1 79  ? 23.667  -5.465  15.189  1.00 22.01 ? 79  GLN A O   1 
ATOM   608  C  CB  . GLN A 1 79  ? 24.585  -4.160  17.918  1.00 28.41 ? 79  GLN A CB  1 
ATOM   609  C  CG  . GLN A 1 79  ? 25.749  -3.456  18.602  1.00 32.94 ? 79  GLN A CG  1 
ATOM   610  C  CD  . GLN A 1 79  ? 25.918  -3.871  20.047  1.00 35.89 ? 79  GLN A CD  1 
ATOM   611  O  OE1 . GLN A 1 79  ? 25.730  -5.032  20.416  1.00 37.03 ? 79  GLN A OE1 1 
ATOM   612  N  NE2 . GLN A 1 79  ? 26.304  -2.918  20.880  1.00 37.44 ? 79  GLN A NE2 1 
ATOM   613  N  N   . GLY A 1 80  ? 25.615  -4.411  14.743  1.00 24.82 ? 80  GLY A N   1 
ATOM   614  C  CA  . GLY A 1 80  ? 25.965  -5.342  13.689  1.00 25.25 ? 80  GLY A CA  1 
ATOM   615  C  C   . GLY A 1 80  ? 26.268  -4.644  12.368  1.00 27.51 ? 80  GLY A C   1 
ATOM   616  O  O   . GLY A 1 80  ? 26.876  -5.255  11.487  1.00 28.33 ? 80  GLY A O   1 
ATOM   617  N  N   . LEU A 1 81  ? 25.827  -3.381  12.234  1.00 24.27 ? 81  LEU A N   1 
ATOM   618  C  CA  . LEU A 1 81  ? 26.200  -2.575  11.082  1.00 25.17 ? 81  LEU A CA  1 
ATOM   619  C  C   . LEU A 1 81  ? 27.516  -1.848  11.370  1.00 27.55 ? 81  LEU A C   1 
ATOM   620  O  O   . LEU A 1 81  ? 28.070  -1.925  12.467  1.00 26.29 ? 81  LEU A O   1 
ATOM   621  C  CB  . LEU A 1 81  ? 25.053  -1.618  10.715  1.00 23.47 ? 81  LEU A CB  1 
ATOM   622  C  CG  . LEU A 1 81  ? 23.705  -2.291  10.458  1.00 21.60 ? 81  LEU A CG  1 
ATOM   623  C  CD1 . LEU A 1 81  ? 22.587  -1.265  10.358  1.00 21.78 ? 81  LEU A CD1 1 
ATOM   624  C  CD2 . LEU A 1 81  ? 23.749  -3.156  9.199   1.00 22.44 ? 81  LEU A CD2 1 
ATOM   625  N  N   . GLN A 1 82  ? 28.024  -1.117  10.382  1.00 32.69 ? 82  GLN A N   1 
ATOM   626  C  CA  . GLN A 1 82  ? 29.361  -0.565  10.542  1.00 38.62 ? 82  GLN A CA  1 
ATOM   627  C  C   . GLN A 1 82  ? 29.360  0.511   11.634  1.00 36.32 ? 82  GLN A C   1 
ATOM   628  O  O   . GLN A 1 82  ? 30.418  0.910   12.120  1.00 37.19 ? 82  GLN A O   1 
ATOM   629  N  N   . SER A 1 83  ? 28.157  0.940   12.037  1.00 29.37 ? 83  SER A N   1 
ATOM   630  C  CA  . SER A 1 83  ? 27.962  2.111   12.872  1.00 24.57 ? 83  SER A CA  1 
ATOM   631  C  C   . SER A 1 83  ? 26.751  1.872   13.765  1.00 22.39 ? 83  SER A C   1 
ATOM   632  O  O   . SER A 1 83  ? 25.888  1.044   13.454  1.00 18.51 ? 83  SER A O   1 
ATOM   633  C  CB  . SER A 1 83  ? 27.757  3.334   11.996  1.00 25.20 ? 83  SER A CB  1 
ATOM   634  O  OG  . SER A 1 83  ? 28.980  3.989   11.705  1.00 24.94 ? 83  SER A OG  1 
ATOM   635  N  N   . ARG A 1 84  ? 26.668  2.614   14.875  1.00 21.72 ? 84  ARG A N   1 
ATOM   636  C  CA  . ARG A 1 84  ? 25.445  2.528   15.655  1.00 18.64 ? 84  ARG A CA  1 
ATOM   637  C  C   . ARG A 1 84  ? 24.327  3.209   14.862  1.00 17.20 ? 84  ARG A C   1 
ATOM   638  O  O   . ARG A 1 84  ? 24.478  4.358   14.428  1.00 16.08 ? 84  ARG A O   1 
ATOM   639  C  CB  . ARG A 1 84  ? 25.593  3.139   17.052  1.00 19.61 ? 84  ARG A CB  1 
ATOM   640  C  CG  . ARG A 1 84  ? 24.255  3.369   17.749  1.00 20.23 ? 84  ARG A CG  1 
ATOM   641  C  CD  . ARG A 1 84  ? 24.385  3.467   19.251  1.00 20.62 ? 84  ARG A CD  1 
ATOM   642  N  NE  . ARG A 1 84  ? 23.180  4.017   19.865  1.00 21.59 ? 84  ARG A NE  1 
ATOM   643  C  CZ  . ARG A 1 84  ? 22.948  3.981   21.169  1.00 21.75 ? 84  ARG A CZ  1 
ATOM   644  N  NH1 . ARG A 1 84  ? 23.825  3.391   21.966  1.00 19.72 ? 84  ARG A NH1 1 
ATOM   645  N  NH2 . ARG A 1 84  ? 21.837  4.502   21.660  1.00 22.43 ? 84  ARG A NH2 1 
ATOM   646  N  N   . TYR A 1 85  ? 23.216  2.477   14.692  1.00 14.13 ? 85  TYR A N   1 
ATOM   647  C  CA  . TYR A 1 85  ? 21.995  3.050   14.165  1.00 13.46 ? 85  TYR A CA  1 
ATOM   648  C  C   . TYR A 1 85  ? 20.952  3.078   15.282  1.00 13.42 ? 85  TYR A C   1 
ATOM   649  O  O   . TYR A 1 85  ? 20.587  2.036   15.804  1.00 13.73 ? 85  TYR A O   1 
ATOM   650  C  CB  . TYR A 1 85  ? 21.537  2.272   12.935  1.00 13.57 ? 85  TYR A CB  1 
ATOM   651  C  CG  . TYR A 1 85  ? 22.322  2.567   11.684  1.00 13.67 ? 85  TYR A CG  1 
ATOM   652  C  CD1 . TYR A 1 85  ? 23.449  1.821   11.352  1.00 15.04 ? 85  TYR A CD1 1 
ATOM   653  C  CD2 . TYR A 1 85  ? 21.915  3.559   10.809  1.00 13.80 ? 85  TYR A CD2 1 
ATOM   654  C  CE1 . TYR A 1 85  ? 24.157  2.049   10.178  1.00 15.53 ? 85  TYR A CE1 1 
ATOM   655  C  CE2 . TYR A 1 85  ? 22.621  3.814   9.641   1.00 14.93 ? 85  TYR A CE2 1 
ATOM   656  C  CZ  . TYR A 1 85  ? 23.752  3.074   9.335   1.00 15.29 ? 85  TYR A CZ  1 
ATOM   657  O  OH  . TYR A 1 85  ? 24.448  3.342   8.191   1.00 17.05 ? 85  TYR A OH  1 
ATOM   658  N  N   . SER A 1 86  ? 20.491  4.282   15.637  1.00 11.79 ? 86  SER A N   1 
ATOM   659  C  CA  . SER A 1 86  ? 19.537  4.462   16.712  1.00 11.66 ? 86  SER A CA  1 
ATOM   660  C  C   . SER A 1 86  ? 18.154  4.648   16.104  1.00 10.91 ? 86  SER A C   1 
ATOM   661  O  O   . SER A 1 86  ? 18.018  5.309   15.077  1.00 10.94 ? 86  SER A O   1 
ATOM   662  C  CB  . SER A 1 86  ? 19.899  5.673   17.557  1.00 11.53 ? 86  SER A CB  1 
ATOM   663  O  OG  . SER A 1 86  ? 21.211  5.512   18.067  1.00 13.92 ? 86  SER A OG  1 
ATOM   664  N  N   . ALA A 1 87  ? 17.146  4.151   16.815  1.00 10.71 ? 87  ALA A N   1 
ATOM   665  C  CA  . ALA A 1 87  ? 15.774  4.185   16.342  1.00 10.67 ? 87  ALA A CA  1 
ATOM   666  C  C   . ALA A 1 87  ? 15.246  5.613   16.421  1.00 11.00 ? 87  ALA A C   1 
ATOM   667  O  O   . ALA A 1 87  ? 15.641  6.406   17.298  1.00 10.38 ? 87  ALA A O   1 
ATOM   668  C  CB  . ALA A 1 87  ? 14.921  3.233   17.143  1.00 10.53 ? 87  ALA A CB  1 
ATOM   669  N  N   . THR A 1 88  ? 14.336  5.907   15.491  1.00 10.89 ? 88  THR A N   1 
ATOM   670  C  CA  . THR A 1 88  ? 13.644  7.180   15.457  1.00 10.99 ? 88  THR A CA  1 
ATOM   671  C  C   . THR A 1 88  ? 12.135  6.947   15.517  1.00 10.18 ? 88  THR A C   1 
ATOM   672  O  O   . THR A 1 88  ? 11.425  7.650   16.256  1.00 9.65  ? 88  THR A O   1 
ATOM   673  C  CB  . THR A 1 88  ? 14.157  8.056   14.301  1.00 12.78 ? 88  THR A CB  1 
ATOM   674  O  OG1 . THR A 1 88  ? 13.412  9.269   14.368  1.00 17.10 ? 88  THR A OG1 1 
ATOM   675  C  CG2 . THR A 1 88  ? 13.892  7.466   12.933  1.00 12.33 ? 88  THR A CG2 1 
ATOM   676  N  N   . GLN A 1 89  ? 11.637  5.965   14.742  1.00 8.87  ? 89  GLN A N   1 
ATOM   677  C  CA  . GLN A 1 89  ? 10.195  5.730   14.680  1.00 8.50  ? 89  GLN A CA  1 
ATOM   678  C  C   . GLN A 1 89  ? 9.912   4.415   13.963  1.00 7.87  ? 89  GLN A C   1 
ATOM   679  O  O   . GLN A 1 89  ? 10.761  3.900   13.236  1.00 7.53  ? 89  GLN A O   1 
ATOM   680  C  CB  . GLN A 1 89  ? 9.443   6.900   14.021  1.00 8.83  ? 89  GLN A CB  1 
ATOM   681  C  CG  . GLN A 1 89  ? 9.974   7.319   12.655  1.00 9.60  ? 89  GLN A CG  1 
ATOM   682  C  CD  . GLN A 1 89  ? 9.115   6.867   11.501  1.00 10.39 ? 89  GLN A CD  1 
ATOM   683  O  OE1 . GLN A 1 89  ? 8.568   5.763   11.482  1.00 11.75 ? 89  GLN A OE1 1 
ATOM   684  N  NE2 . GLN A 1 89  ? 9.015   7.711   10.493  1.00 10.06 ? 89  GLN A NE2 1 
ATOM   685  N  N   . LEU A 1 90  ? 8.694   3.899   14.140  1.00 7.37  ? 90  LEU A N   1 
ATOM   686  C  CA  . LEU A 1 90  ? 8.243   2.818   13.262  1.00 6.82  ? 90  LEU A CA  1 
ATOM   687  C  C   . LEU A 1 90  ? 6.858   3.185   12.704  1.00 6.53  ? 90  LEU A C   1 
ATOM   688  O  O   . LEU A 1 90  ? 6.189   4.063   13.239  1.00 6.02  ? 90  LEU A O   1 
ATOM   689  C  CB  . LEU A 1 90  ? 8.278   1.481   14.028  1.00 6.20  ? 90  LEU A CB  1 
ATOM   690  C  CG  . LEU A 1 90  ? 7.365   1.361   15.259  1.00 6.34  ? 90  LEU A CG  1 
ATOM   691  C  CD1 . LEU A 1 90  ? 5.880   1.228   14.872  1.00 5.78  ? 90  LEU A CD1 1 
ATOM   692  C  CD2 . LEU A 1 90  ? 7.770   0.200   16.155  1.00 5.98  ? 90  LEU A CD2 1 
ATOM   693  N  N   . HIS A 1 91  ? 6.469   2.561   11.578  1.00 6.46  ? 91  HIS A N   1 
ATOM   694  C  CA  . HIS A 1 91  ? 5.195   2.857   10.937  1.00 6.67  ? 91  HIS A CA  1 
ATOM   695  C  C   . HIS A 1 91  ? 4.866   1.700   10.005  1.00 6.80  ? 91  HIS A C   1 
ATOM   696  O  O   . HIS A 1 91  ? 5.651   0.756   9.867   1.00 7.21  ? 91  HIS A O   1 
ATOM   697  C  CB  . HIS A 1 91  ? 5.251   4.208   10.177  1.00 6.45  ? 91  HIS A CB  1 
ATOM   698  C  CG  . HIS A 1 91  ? 6.195   4.155   9.024   1.00 6.41  ? 91  HIS A CG  1 
ATOM   699  N  ND1 . HIS A 1 91  ? 7.497   4.546   9.128   1.00 6.51  ? 91  HIS A ND1 1 
ATOM   700  C  CD2 . HIS A 1 91  ? 6.058   3.645   7.779   1.00 6.76  ? 91  HIS A CD2 1 
ATOM   701  C  CE1 . HIS A 1 91  ? 8.129   4.342   7.985   1.00 7.01  ? 91  HIS A CE1 1 
ATOM   702  N  NE2 . HIS A 1 91  ? 7.273   3.749   7.147   1.00 7.02  ? 91  HIS A NE2 1 
ATOM   703  N  N   . LEU A 1 92  ? 3.713   1.792   9.347   1.00 6.93  ? 92  LEU A N   1 
ATOM   704  C  CA  . LEU A 1 92  ? 3.264   0.670   8.554   1.00 7.34  ? 92  LEU A CA  1 
ATOM   705  C  C   . LEU A 1 92  ? 2.772   1.142   7.191   1.00 7.47  ? 92  LEU A C   1 
ATOM   706  O  O   . LEU A 1 92  ? 2.470   2.326   6.991   1.00 8.11  ? 92  LEU A O   1 
ATOM   707  C  CB  . LEU A 1 92  ? 2.168   -0.083  9.326   1.00 7.41  ? 92  LEU A CB  1 
ATOM   708  C  CG  . LEU A 1 92  ? 2.637   -0.800  10.593  1.00 7.94  ? 92  LEU A CG  1 
ATOM   709  C  CD1 . LEU A 1 92  ? 2.170   -0.037  11.817  1.00 7.97  ? 92  LEU A CD1 1 
ATOM   710  C  CD2 . LEU A 1 92  ? 2.118   -2.245  10.642  1.00 7.75  ? 92  LEU A CD2 1 
ATOM   711  N  N   . HIS A 1 93  ? 2.673   0.171   6.281   1.00 7.31  ? 93  HIS A N   1 
ATOM   712  C  CA  . HIS A 1 93  ? 2.092   0.329   4.954   1.00 7.89  ? 93  HIS A CA  1 
ATOM   713  C  C   . HIS A 1 93  ? 1.131   -0.836  4.755   1.00 8.11  ? 93  HIS A C   1 
ATOM   714  O  O   . HIS A 1 93  ? 1.445   -1.940  5.191   1.00 8.11  ? 93  HIS A O   1 
ATOM   715  C  CB  . HIS A 1 93  ? 3.196   0.282   3.887   1.00 7.21  ? 93  HIS A CB  1 
ATOM   716  C  CG  . HIS A 1 93  ? 4.275   1.294   4.111   1.00 7.09  ? 93  HIS A CG  1 
ATOM   717  N  ND1 . HIS A 1 93  ? 4.277   2.523   3.466   1.00 6.61  ? 93  HIS A ND1 1 
ATOM   718  C  CD2 . HIS A 1 93  ? 5.366   1.280   4.907   1.00 6.81  ? 93  HIS A CD2 1 
ATOM   719  C  CE1 . HIS A 1 93  ? 5.315   3.234   3.860   1.00 6.60  ? 93  HIS A CE1 1 
ATOM   720  N  NE2 . HIS A 1 93  ? 6.006   2.495   4.743   1.00 6.72  ? 93  HIS A NE2 1 
ATOM   721  N  N   . TRP A 1 94  ? -0.026  -0.590  4.128   1.00 8.36  ? 94  TRP A N   1 
ATOM   722  C  CA  . TRP A 1 94  ? -1.022  -1.643  3.997   1.00 8.70  ? 94  TRP A CA  1 
ATOM   723  C  C   . TRP A 1 94  ? -1.890  -1.408  2.761   1.00 9.37  ? 94  TRP A C   1 
ATOM   724  O  O   . TRP A 1 94  ? -1.771  -0.374  2.092   1.00 8.87  ? 94  TRP A O   1 
ATOM   725  C  CB  . TRP A 1 94  ? -1.856  -1.758  5.288   1.00 9.19  ? 94  TRP A CB  1 
ATOM   726  C  CG  . TRP A 1 94  ? -2.578  -0.501  5.673   1.00 9.22  ? 94  TRP A CG  1 
ATOM   727  C  CD1 . TRP A 1 94  ? -3.810  -0.098  5.238   1.00 9.38  ? 94  TRP A CD1 1 
ATOM   728  C  CD2 . TRP A 1 94  ? -2.080  0.550   6.512   1.00 9.13  ? 94  TRP A CD2 1 
ATOM   729  N  NE1 . TRP A 1 94  ? -4.111  1.130   5.764   1.00 9.14  ? 94  TRP A NE1 1 
ATOM   730  C  CE2 . TRP A 1 94  ? -3.080  1.544   6.564   1.00 9.37  ? 94  TRP A CE2 1 
ATOM   731  C  CE3 . TRP A 1 94  ? -0.896  0.745   7.233   1.00 9.47  ? 94  TRP A CE3 1 
ATOM   732  C  CZ2 . TRP A 1 94  ? -2.934  2.703   7.325   1.00 9.44  ? 94  TRP A CZ2 1 
ATOM   733  C  CZ3 . TRP A 1 94  ? -0.752  1.887   7.998   1.00 9.63  ? 94  TRP A CZ3 1 
ATOM   734  C  CH2 . TRP A 1 94  ? -1.765  2.847   8.043   1.00 9.98  ? 94  TRP A CH2 1 
ATOM   735  N  N   . GLY A 1 95  ? -2.777  -2.379  2.484   1.00 10.42 ? 95  GLY A N   1 
ATOM   736  C  CA  . GLY A 1 95  ? -3.707  -2.285  1.368   1.00 11.17 ? 95  GLY A CA  1 
ATOM   737  C  C   . GLY A 1 95  ? -5.089  -1.770  1.781   1.00 11.17 ? 95  GLY A C   1 
ATOM   738  O  O   . GLY A 1 95  ? -5.222  -0.690  2.381   1.00 9.33  ? 95  GLY A O   1 
ATOM   739  N  N   . ASN A 1 96  ? -6.118  -2.532  1.390   1.00 11.42 ? 96  ASN A N   1 
ATOM   740  C  CA  . ASN A 1 96  ? -7.495  -2.182  1.721   1.00 13.37 ? 96  ASN A CA  1 
ATOM   741  C  C   . ASN A 1 96  ? -8.342  -3.446  1.905   1.00 14.66 ? 96  ASN A C   1 
ATOM   742  O  O   . ASN A 1 96  ? -7.936  -4.546  1.510   1.00 14.61 ? 96  ASN A O   1 
ATOM   743  C  CB  . ASN A 1 96  ? -8.100  -1.221  0.690   1.00 14.53 ? 96  ASN A CB  1 
ATOM   744  C  CG  . ASN A 1 96  ? -8.500  -1.901  -0.610  1.00 16.60 ? 96  ASN A CG  1 
ATOM   745  O  OD1 . ASN A 1 96  ? -9.634  -2.375  -0.752  1.00 16.03 ? 96  ASN A OD1 1 
ATOM   746  N  ND2 . ASN A 1 96  ? -7.578  -1.941  -1.564  1.00 16.26 ? 96  ASN A ND2 1 
ATOM   747  N  N   . PRO A 1 97  ? -9.562  -3.338  2.483   1.00 16.60 ? 97  PRO A N   1 
ATOM   748  C  CA  . PRO A 1 97  ? -10.399 -4.522  2.711   1.00 18.22 ? 97  PRO A CA  1 
ATOM   749  C  C   . PRO A 1 97  ? -10.645 -5.390  1.473   1.00 19.60 ? 97  PRO A C   1 
ATOM   750  O  O   . PRO A 1 97  ? -10.794 -6.602  1.594   1.00 19.83 ? 97  PRO A O   1 
ATOM   751  C  CB  . PRO A 1 97  ? -11.693 -3.921  3.275   1.00 18.04 ? 97  PRO A CB  1 
ATOM   752  C  CG  . PRO A 1 97  ? -11.237 -2.628  3.923   1.00 16.69 ? 97  PRO A CG  1 
ATOM   753  C  CD  . PRO A 1 97  ? -10.185 -2.094  2.977   1.00 15.94 ? 97  PRO A CD  1 
ATOM   754  N  N   . ASN A 1 98  ? -10.662 -4.759  0.293   1.00 19.72 ? 98  ASN A N   1 
ATOM   755  C  CA  . ASN A 1 98  ? -10.954 -5.423  -0.968  1.00 23.40 ? 98  ASN A CA  1 
ATOM   756  C  C   . ASN A 1 98  ? -9.671  -5.978  -1.589  1.00 23.71 ? 98  ASN A C   1 
ATOM   757  O  O   . ASN A 1 98  ? -9.728  -6.786  -2.515  1.00 26.34 ? 98  ASN A O   1 
ATOM   758  C  CB  . ASN A 1 98  ? -11.630 -4.484  -1.979  1.00 26.10 ? 98  ASN A CB  1 
ATOM   759  C  CG  . ASN A 1 98  ? -13.085 -4.154  -1.682  1.00 29.22 ? 98  ASN A CG  1 
ATOM   760  O  OD1 . ASN A 1 98  ? -13.762 -4.849  -0.925  1.00 32.01 ? 98  ASN A OD1 1 
ATOM   761  N  ND2 . ASN A 1 98  ? -13.590 -3.095  -2.294  1.00 31.22 ? 98  ASN A ND2 1 
ATOM   762  N  N   . ASP A 1 99  ? -8.511  -5.541  -1.089  1.00 21.11 ? 99  ASP A N   1 
ATOM   763  C  CA  . ASP A 1 99  ? -7.242  -6.050  -1.586  1.00 18.66 ? 99  ASP A CA  1 
ATOM   764  C  C   . ASP A 1 99  ? -6.217  -5.985  -0.458  1.00 16.35 ? 99  ASP A C   1 
ATOM   765  O  O   . ASP A 1 99  ? -5.422  -5.050  -0.411  1.00 15.71 ? 99  ASP A O   1 
ATOM   766  C  CB  . ASP A 1 99  ? -6.780  -5.299  -2.841  1.00 19.98 ? 99  ASP A CB  1 
ATOM   767  C  CG  . ASP A 1 99  ? -5.456  -5.810  -3.425  1.00 22.40 ? 99  ASP A CG  1 
ATOM   768  O  OD1 . ASP A 1 99  ? -5.065  -6.968  -3.121  1.00 20.71 ? 99  ASP A OD1 1 
ATOM   769  O  OD2 . ASP A 1 99  ? -4.789  -5.021  -4.138  1.00 23.87 ? 99  ASP A OD2 1 
ATOM   770  N  N   . PRO A 1 100 ? -6.240  -6.936  0.507   1.00 14.60 ? 100 PRO A N   1 
ATOM   771  C  CA  . PRO A 1 100 ? -5.377  -6.844  1.680   1.00 13.48 ? 100 PRO A CA  1 
ATOM   772  C  C   . PRO A 1 100 ? -3.952  -7.324  1.417   1.00 12.58 ? 100 PRO A C   1 
ATOM   773  O  O   . PRO A 1 100 ? -3.469  -8.227  2.102   1.00 11.96 ? 100 PRO A O   1 
ATOM   774  C  CB  . PRO A 1 100 ? -6.120  -7.737  2.689   1.00 13.52 ? 100 PRO A CB  1 
ATOM   775  C  CG  . PRO A 1 100 ? -6.749  -8.821  1.826   1.00 13.30 ? 100 PRO A CG  1 
ATOM   776  C  CD  . PRO A 1 100 ? -7.170  -8.087  0.574   1.00 14.04 ? 100 PRO A CD  1 
ATOM   777  N  N   . HIS A 1 101 ? -3.304  -6.709  0.417   1.00 11.78 ? 101 HIS A N   1 
ATOM   778  C  CA  . HIS A 1 101 ? -1.942  -7.043  0.029   1.00 11.84 ? 101 HIS A CA  1 
ATOM   779  C  C   . HIS A 1 101 ? -1.196  -5.756  -0.299  1.00 11.45 ? 101 HIS A C   1 
ATOM   780  O  O   . HIS A 1 101 ? -0.939  -5.453  -1.468  1.00 12.16 ? 101 HIS A O   1 
ATOM   781  C  CB  . HIS A 1 101 ? -1.925  -7.978  -1.185  1.00 12.63 ? 101 HIS A CB  1 
ATOM   782  C  CG  . HIS A 1 101 ? -2.849  -9.137  -1.067  1.00 13.56 ? 101 HIS A CG  1 
ATOM   783  N  ND1 . HIS A 1 101 ? -2.485  -10.300 -0.426  1.00 14.50 ? 101 HIS A ND1 1 
ATOM   784  C  CD2 . HIS A 1 101 ? -4.118  -9.304  -1.491  1.00 15.14 ? 101 HIS A CD2 1 
ATOM   785  C  CE1 . HIS A 1 101 ? -3.492  -11.148 -0.452  1.00 15.43 ? 101 HIS A CE1 1 
ATOM   786  N  NE2 . HIS A 1 101 ? -4.512  -10.559 -1.098  1.00 15.82 ? 101 HIS A NE2 1 
ATOM   787  N  N   . GLY A 1 102 ? -0.852  -5.014  0.746   1.00 10.30 ? 102 GLY A N   1 
ATOM   788  C  CA  . GLY A 1 102 ? -0.266  -3.693  0.580   1.00 10.21 ? 102 GLY A CA  1 
ATOM   789  C  C   . GLY A 1 102 ? 1.156   -3.588  1.149   1.00 10.04 ? 102 GLY A C   1 
ATOM   790  O  O   . GLY A 1 102 ? 1.566   -2.493  1.524   1.00 10.21 ? 102 GLY A O   1 
ATOM   791  N  N   . SER A 1 103 ? 1.917   -4.700  1.176   1.00 8.99  ? 103 SER A N   1 
ATOM   792  C  CA  . SER A 1 103 ? 3.336   -4.591  1.485   1.00 8.46  ? 103 SER A CA  1 
ATOM   793  C  C   . SER A 1 103 ? 4.004   -3.711  0.431   1.00 8.31  ? 103 SER A C   1 
ATOM   794  O  O   . SER A 1 103 ? 3.507   -3.588  -0.680  1.00 8.99  ? 103 SER A O   1 
ATOM   795  C  CB  . SER A 1 103 ? 4.037   -5.953  1.579   1.00 8.12  ? 103 SER A CB  1 
ATOM   796  O  OG  . SER A 1 103 ? 4.277   -6.531  0.298   1.00 7.67  ? 103 SER A OG  1 
ATOM   797  N  N   . GLU A 1 104 ? 5.174   -3.151  0.740   1.00 8.74  ? 104 GLU A N   1 
ATOM   798  C  CA  . GLU A 1 104 ? 5.815   -2.324  -0.272  1.00 8.77  ? 104 GLU A CA  1 
ATOM   799  C  C   . GLU A 1 104 ? 6.817   -3.187  -1.022  1.00 8.61  ? 104 GLU A C   1 
ATOM   800  O  O   . GLU A 1 104 ? 6.829   -3.237  -2.254  1.00 7.91  ? 104 GLU A O   1 
ATOM   801  C  CB  . GLU A 1 104 ? 6.516   -1.132  0.363   1.00 9.04  ? 104 GLU A CB  1 
ATOM   802  C  CG  . GLU A 1 104 ? 5.582   -0.203  1.133   1.00 8.77  ? 104 GLU A CG  1 
ATOM   803  C  CD  . GLU A 1 104 ? 6.156   1.201   1.134   1.00 8.95  ? 104 GLU A CD  1 
ATOM   804  O  OE1 . GLU A 1 104 ? 7.106   1.414   1.874   1.00 9.08  ? 104 GLU A OE1 1 
ATOM   805  O  OE2 . GLU A 1 104 ? 5.679   2.071   0.359   1.00 9.31  ? 104 GLU A OE2 1 
ATOM   806  N  N   . HIS A 1 105 ? 7.646   -3.908  -0.269  1.00 8.40  ? 105 HIS A N   1 
ATOM   807  C  CA  . HIS A 1 105 ? 8.483   -4.861  -0.963  1.00 8.33  ? 105 HIS A CA  1 
ATOM   808  C  C   . HIS A 1 105 ? 7.607   -6.043  -1.356  1.00 8.72  ? 105 HIS A C   1 
ATOM   809  O  O   . HIS A 1 105 ? 6.656   -6.398  -0.646  1.00 8.07  ? 105 HIS A O   1 
ATOM   810  C  CB  . HIS A 1 105 ? 9.693   -5.276  -0.106  1.00 8.57  ? 105 HIS A CB  1 
ATOM   811  C  CG  . HIS A 1 105 ? 10.664  -4.167  0.138   1.00 8.39  ? 105 HIS A CG  1 
ATOM   812  N  ND1 . HIS A 1 105 ? 10.586  -3.376  1.235   1.00 8.47  ? 105 HIS A ND1 1 
ATOM   813  C  CD2 . HIS A 1 105 ? 11.747  -3.745  -0.556  1.00 8.66  ? 105 HIS A CD2 1 
ATOM   814  C  CE1 . HIS A 1 105 ? 11.570  -2.498  1.232   1.00 8.50  ? 105 HIS A CE1 1 
ATOM   815  N  NE2 . HIS A 1 105 ? 12.298  -2.702  0.133   1.00 8.57  ? 105 HIS A NE2 1 
ATOM   816  N  N   . THR A 1 106 ? 7.977   -6.656  -2.487  1.00 8.95  ? 106 THR A N   1 
ATOM   817  C  CA  . THR A 1 106 ? 7.318   -7.846  -2.976  1.00 8.95  ? 106 THR A CA  1 
ATOM   818  C  C   . THR A 1 106 ? 8.388   -8.921  -3.180  1.00 9.28  ? 106 THR A C   1 
ATOM   819  O  O   . THR A 1 106 ? 9.579   -8.622  -3.230  1.00 8.56  ? 106 THR A O   1 
ATOM   820  C  CB  . THR A 1 106 ? 6.517   -7.508  -4.237  1.00 8.95  ? 106 THR A CB  1 
ATOM   821  O  OG1 . THR A 1 106 ? 7.501   -7.138  -5.191  1.00 8.30  ? 106 THR A OG1 1 
ATOM   822  C  CG2 . THR A 1 106 ? 5.584   -6.322  -4.081  1.00 9.39  ? 106 THR A CG2 1 
ATOM   823  N  N   . VAL A 1 107 ? 7.949   -10.178 -3.227  1.00 9.73  ? 107 VAL A N   1 
ATOM   824  C  CA  . VAL A 1 107 ? 8.824   -11.331 -3.389  1.00 11.45 ? 107 VAL A CA  1 
ATOM   825  C  C   . VAL A 1 107 ? 8.223   -12.155 -4.527  1.00 11.48 ? 107 VAL A C   1 
ATOM   826  O  O   . VAL A 1 107 ? 7.058   -12.517 -4.458  1.00 11.63 ? 107 VAL A O   1 
ATOM   827  C  CB  . VAL A 1 107 ? 8.887   -12.140 -2.069  1.00 12.73 ? 107 VAL A CB  1 
ATOM   828  C  CG1 . VAL A 1 107 ? 9.690   -13.438 -2.208  1.00 13.63 ? 107 VAL A CG1 1 
ATOM   829  C  CG2 . VAL A 1 107 ? 9.461   -11.308 -0.915  1.00 13.12 ? 107 VAL A CG2 1 
ATOM   830  N  N   . SER A 1 108 ? 8.971   -12.348 -5.621  1.00 12.93 ? 108 SER A N   1 
ATOM   831  C  CA  . SER A 1 108 ? 8.447   -12.966 -6.835  1.00 12.44 ? 108 SER A CA  1 
ATOM   832  C  C   . SER A 1 108 ? 7.189   -12.260 -7.311  1.00 12.20 ? 108 SER A C   1 
ATOM   833  O  O   . SER A 1 108 ? 6.270   -12.920 -7.803  1.00 11.66 ? 108 SER A O   1 
ATOM   834  C  CB  . SER A 1 108 ? 8.079   -14.410 -6.634  1.00 13.46 ? 108 SER A CB  1 
ATOM   835  O  OG  . SER A 1 108 ? 9.212   -15.217 -6.666  1.00 14.15 ? 108 SER A OG  1 
ATOM   836  N  N   . GLY A 1 109 ? 7.158   -10.934 -7.164  1.00 11.08 ? 109 GLY A N   1 
ATOM   837  C  CA  . GLY A 1 109 ? 6.031   -10.163 -7.651  1.00 10.42 ? 109 GLY A CA  1 
ATOM   838  C  C   . GLY A 1 109 ? 4.808   -10.209 -6.728  1.00 9.99  ? 109 GLY A C   1 
ATOM   839  O  O   . GLY A 1 109 ? 3.762   -9.664  -7.078  1.00 9.39  ? 109 GLY A O   1 
ATOM   840  N  N   . GLN A 1 110 ? 4.920   -10.879 -5.576  1.00 9.72  ? 110 GLN A N   1 
ATOM   841  C  CA  . GLN A 1 110 ? 3.779   -11.093 -4.689  1.00 9.61  ? 110 GLN A CA  1 
ATOM   842  C  C   . GLN A 1 110 ? 3.853   -10.086 -3.536  1.00 8.75  ? 110 GLN A C   1 
ATOM   843  O  O   . GLN A 1 110 ? 4.898   -9.940  -2.925  1.00 8.61  ? 110 GLN A O   1 
ATOM   844  C  CB  . GLN A 1 110 ? 3.817   -12.514 -4.108  1.00 10.13 ? 110 GLN A CB  1 
ATOM   845  C  CG  . GLN A 1 110 ? 4.046   -13.623 -5.142  1.00 11.02 ? 110 GLN A CG  1 
ATOM   846  C  CD  . GLN A 1 110 ? 3.096   -13.525 -6.318  1.00 12.06 ? 110 GLN A CD  1 
ATOM   847  O  OE1 . GLN A 1 110 ? 1.878   -13.641 -6.165  1.00 12.49 ? 110 GLN A OE1 1 
ATOM   848  N  NE2 . GLN A 1 110 ? 3.649   -13.321 -7.510  1.00 11.39 ? 110 GLN A NE2 1 
ATOM   849  N  N   . HIS A 1 111 ? 2.750   -9.399  -3.249  1.00 8.84  ? 111 HIS A N   1 
ATOM   850  C  CA  . HIS A 1 111 ? 2.637   -8.588  -2.047  1.00 9.74  ? 111 HIS A CA  1 
ATOM   851  C  C   . HIS A 1 111 ? 2.299   -9.461  -0.834  1.00 9.94  ? 111 HIS A C   1 
ATOM   852  O  O   . HIS A 1 111 ? 1.564   -10.431 -0.947  1.00 10.76 ? 111 HIS A O   1 
ATOM   853  C  CB  . HIS A 1 111 ? 1.514   -7.550  -2.205  1.00 9.82  ? 111 HIS A CB  1 
ATOM   854  C  CG  . HIS A 1 111 ? 1.836   -6.475  -3.183  1.00 9.19  ? 111 HIS A CG  1 
ATOM   855  N  ND1 . HIS A 1 111 ? 2.462   -5.327  -2.802  1.00 9.73  ? 111 HIS A ND1 1 
ATOM   856  C  CD2 . HIS A 1 111 ? 1.634   -6.373  -4.510  1.00 9.07  ? 111 HIS A CD2 1 
ATOM   857  C  CE1 . HIS A 1 111 ? 2.614   -4.526  -3.841  1.00 9.42  ? 111 HIS A CE1 1 
ATOM   858  N  NE2 . HIS A 1 111 ? 2.158   -5.159  -4.904  1.00 9.17  ? 111 HIS A NE2 1 
ATOM   859  N  N   . PHE A 1 112 ? 2.845   -9.096  0.326   1.00 10.04 ? 112 PHE A N   1 
ATOM   860  C  CA  . PHE A 1 112 ? 2.367   -9.567  1.611   1.00 9.75  ? 112 PHE A CA  1 
ATOM   861  C  C   . PHE A 1 112 ? 1.259   -8.623  2.061   1.00 8.90  ? 112 PHE A C   1 
ATOM   862  O  O   . PHE A 1 112 ? 1.031   -7.607  1.412   1.00 8.60  ? 112 PHE A O   1 
ATOM   863  C  CB  . PHE A 1 112 ? 3.550   -9.706  2.574   1.00 11.47 ? 112 PHE A CB  1 
ATOM   864  C  CG  . PHE A 1 112 ? 4.475   -10.846 2.217   1.00 12.84 ? 112 PHE A CG  1 
ATOM   865  C  CD1 . PHE A 1 112 ? 5.442   -10.705 1.223   1.00 13.78 ? 112 PHE A CD1 1 
ATOM   866  C  CD2 . PHE A 1 112 ? 4.384   -12.065 2.875   1.00 13.17 ? 112 PHE A CD2 1 
ATOM   867  C  CE1 . PHE A 1 112 ? 6.273   -11.770 0.874   1.00 15.17 ? 112 PHE A CE1 1 
ATOM   868  C  CE2 . PHE A 1 112 ? 5.195   -13.140 2.516   1.00 14.24 ? 112 PHE A CE2 1 
ATOM   869  C  CZ  . PHE A 1 112 ? 6.149   -12.991 1.526   1.00 14.34 ? 112 PHE A CZ  1 
ATOM   870  N  N   . ALA A 1 113 ? 0.540   -8.964  3.136   1.00 8.22  ? 113 ALA A N   1 
ATOM   871  C  CA  . ALA A 1 113 ? -0.627  -8.171  3.523   1.00 8.37  ? 113 ALA A CA  1 
ATOM   872  C  C   . ALA A 1 113 ? -0.213  -6.750  3.894   1.00 8.41  ? 113 ALA A C   1 
ATOM   873  O  O   . ALA A 1 113 ? -0.901  -5.785  3.553   1.00 8.64  ? 113 ALA A O   1 
ATOM   874  C  CB  . ALA A 1 113 ? -1.322  -8.803  4.723   1.00 8.40  ? 113 ALA A CB  1 
ATOM   875  N  N   . ALA A 1 114 ? 0.894   -6.642  4.641   1.00 8.28  ? 114 ALA A N   1 
ATOM   876  C  CA  . ALA A 1 114 ? 1.330   -5.339  5.111   1.00 8.62  ? 114 ALA A CA  1 
ATOM   877  C  C   . ALA A 1 114 ? 2.832   -5.381  5.326   1.00 8.26  ? 114 ALA A C   1 
ATOM   878  O  O   . ALA A 1 114 ? 3.481   -6.383  5.021   1.00 8.73  ? 114 ALA A O   1 
ATOM   879  C  CB  . ALA A 1 114 ? 0.566   -4.922  6.359   1.00 8.17  ? 114 ALA A CB  1 
ATOM   880  N  N   . GLU A 1 115 ? 3.351   -4.265  5.829   1.00 8.00  ? 115 GLU A N   1 
ATOM   881  C  CA  . GLU A 1 115 ? 4.780   -4.114  6.036   1.00 8.01  ? 115 GLU A CA  1 
ATOM   882  C  C   . GLU A 1 115 ? 5.013   -3.117  7.176   1.00 7.73  ? 115 GLU A C   1 
ATOM   883  O  O   . GLU A 1 115 ? 4.479   -2.008  7.167   1.00 7.44  ? 115 GLU A O   1 
ATOM   884  C  CB  . GLU A 1 115 ? 5.460   -3.679  4.738   1.00 7.54  ? 115 GLU A CB  1 
ATOM   885  C  CG  . GLU A 1 115 ? 6.985   -3.791  4.784   1.00 7.78  ? 115 GLU A CG  1 
ATOM   886  C  CD  . GLU A 1 115 ? 7.650   -3.684  3.417   1.00 7.74  ? 115 GLU A CD  1 
ATOM   887  O  OE1 . GLU A 1 115 ? 8.839   -3.318  3.365   1.00 7.61  ? 115 GLU A OE1 1 
ATOM   888  O  OE2 . GLU A 1 115 ? 6.993   -4.015  2.415   1.00 7.82  ? 115 GLU A OE2 1 
ATOM   889  N  N   . LEU A 1 116 ? 5.855   -3.520  8.125   1.00 7.76  ? 116 LEU A N   1 
ATOM   890  C  CA  . LEU A 1 116 ? 6.334   -2.619  9.169   1.00 7.42  ? 116 LEU A CA  1 
ATOM   891  C  C   . LEU A 1 116 ? 7.751   -2.138  8.833   1.00 7.32  ? 116 LEU A C   1 
ATOM   892  O  O   . LEU A 1 116 ? 8.635   -2.933  8.497   1.00 7.16  ? 116 LEU A O   1 
ATOM   893  C  CB  . LEU A 1 116 ? 6.335   -3.390  10.490  1.00 7.28  ? 116 LEU A CB  1 
ATOM   894  C  CG  . LEU A 1 116 ? 7.045   -2.732  11.679  1.00 7.42  ? 116 LEU A CG  1 
ATOM   895  C  CD1 . LEU A 1 116 ? 6.046   -1.819  12.389  1.00 7.10  ? 116 LEU A CD1 1 
ATOM   896  C  CD2 . LEU A 1 116 ? 7.555   -3.824  12.638  1.00 7.20  ? 116 LEU A CD2 1 
ATOM   897  N  N   . HIS A 1 117 ? 7.955   -0.823  8.966   1.00 7.18  ? 117 HIS A N   1 
ATOM   898  C  CA  . HIS A 1 117 ? 9.267   -0.220  8.867   1.00 6.97  ? 117 HIS A CA  1 
ATOM   899  C  C   . HIS A 1 117 ? 9.707   0.290   10.232  1.00 7.33  ? 117 HIS A C   1 
ATOM   900  O  O   . HIS A 1 117 ? 8.943   0.998   10.876  1.00 7.25  ? 117 HIS A O   1 
ATOM   901  C  CB  . HIS A 1 117 ? 9.267   0.874   7.795   1.00 6.39  ? 117 HIS A CB  1 
ATOM   902  C  CG  . HIS A 1 117 ? 9.083   0.308   6.429   1.00 6.19  ? 117 HIS A CG  1 
ATOM   903  N  ND1 . HIS A 1 117 ? 8.462   1.009   5.410   1.00 5.99  ? 117 HIS A ND1 1 
ATOM   904  C  CD2 . HIS A 1 117 ? 9.366   -0.923  5.936   1.00 5.78  ? 117 HIS A CD2 1 
ATOM   905  C  CE1 . HIS A 1 117 ? 8.434   0.255   4.317   1.00 5.85  ? 117 HIS A CE1 1 
ATOM   906  N  NE2 . HIS A 1 117 ? 8.958   -0.944  4.624   1.00 5.68  ? 117 HIS A NE2 1 
ATOM   907  N  N   . ILE A 1 118 ? 10.926  -0.091  10.666  1.00 7.72  ? 118 ILE A N   1 
ATOM   908  C  CA  . ILE A 1 118 ? 11.519  0.515   11.862  1.00 8.13  ? 118 ILE A CA  1 
ATOM   909  C  C   . ILE A 1 118 ? 12.716  1.355   11.407  1.00 8.12  ? 118 ILE A C   1 
ATOM   910  O  O   . ILE A 1 118 ? 13.725  0.825   10.966  1.00 7.75  ? 118 ILE A O   1 
ATOM   911  C  CB  . ILE A 1 118 ? 11.923  -0.499  12.966  1.00 7.93  ? 118 ILE A CB  1 
ATOM   912  C  CG1 . ILE A 1 118 ? 10.877  -1.573  13.253  1.00 8.75  ? 118 ILE A CG1 1 
ATOM   913  C  CG2 . ILE A 1 118 ? 12.299  0.219   14.251  1.00 8.31  ? 118 ILE A CG2 1 
ATOM   914  C  CD1 . ILE A 1 118 ? 11.434  -2.720  14.071  1.00 8.59  ? 118 ILE A CD1 1 
ATOM   915  N  N   . VAL A 1 119 ? 12.566  2.680   11.494  1.00 8.61  ? 119 VAL A N   1 
ATOM   916  C  CA  . VAL A 1 119 ? 13.542  3.632   10.986  1.00 8.43  ? 119 VAL A CA  1 
ATOM   917  C  C   . VAL A 1 119 ? 14.575  3.962   12.068  1.00 8.61  ? 119 VAL A C   1 
ATOM   918  O  O   . VAL A 1 119 ? 14.248  4.233   13.219  1.00 7.92  ? 119 VAL A O   1 
ATOM   919  C  CB  . VAL A 1 119 ? 12.846  4.905   10.476  1.00 8.59  ? 119 VAL A CB  1 
ATOM   920  C  CG1 . VAL A 1 119 ? 13.813  5.852   9.777   1.00 8.13  ? 119 VAL A CG1 1 
ATOM   921  C  CG2 . VAL A 1 119 ? 11.677  4.567   9.561   1.00 8.66  ? 119 VAL A CG2 1 
ATOM   922  N  N   . HIS A 1 120 ? 15.844  3.931   11.644  1.00 8.89  ? 120 HIS A N   1 
ATOM   923  C  CA  . HIS A 1 120 ? 16.969  4.274   12.485  1.00 9.53  ? 120 HIS A CA  1 
ATOM   924  C  C   . HIS A 1 120 ? 17.834  5.243   11.693  1.00 10.68 ? 120 HIS A C   1 
ATOM   925  O  O   . HIS A 1 120 ? 17.812  5.239   10.453  1.00 11.13 ? 120 HIS A O   1 
ATOM   926  C  CB  . HIS A 1 120 ? 17.812  3.023   12.792  1.00 9.13  ? 120 HIS A CB  1 
ATOM   927  C  CG  . HIS A 1 120 ? 17.100  1.882   13.437  1.00 9.04  ? 120 HIS A CG  1 
ATOM   928  N  ND1 . HIS A 1 120 ? 16.109  1.180   12.796  1.00 8.79  ? 120 HIS A ND1 1 
ATOM   929  C  CD2 . HIS A 1 120 ? 17.254  1.307   14.658  1.00 8.84  ? 120 HIS A CD2 1 
ATOM   930  C  CE1 . HIS A 1 120 ? 15.670  0.226   13.602  1.00 9.08  ? 120 HIS A CE1 1 
ATOM   931  N  NE2 . HIS A 1 120 ? 16.338  0.298   14.752  1.00 8.69  ? 120 HIS A NE2 1 
ATOM   932  N  N   . TYR A 1 121 ? 18.624  6.055   12.413  1.00 12.03 ? 121 TYR A N   1 
ATOM   933  C  CA  . TYR A 1 121 ? 19.597  6.905   11.745  1.00 13.12 ? 121 TYR A CA  1 
ATOM   934  C  C   . TYR A 1 121 ? 20.974  6.611   12.335  1.00 13.30 ? 121 TYR A C   1 
ATOM   935  O  O   . TYR A 1 121 ? 21.110  6.218   13.498  1.00 12.03 ? 121 TYR A O   1 
ATOM   936  C  CB  . TYR A 1 121 ? 19.171  8.379   11.855  1.00 14.36 ? 121 TYR A CB  1 
ATOM   937  C  CG  . TYR A 1 121 ? 19.368  8.921   13.243  1.00 15.13 ? 121 TYR A CG  1 
ATOM   938  C  CD1 . TYR A 1 121 ? 18.429  8.648   14.216  1.00 15.63 ? 121 TYR A CD1 1 
ATOM   939  C  CD2 . TYR A 1 121 ? 20.501  9.645   13.603  1.00 16.74 ? 121 TYR A CD2 1 
ATOM   940  C  CE1 . TYR A 1 121 ? 18.591  9.085   15.516  1.00 16.13 ? 121 TYR A CE1 1 
ATOM   941  C  CE2 . TYR A 1 121 ? 20.685  10.089  14.911  1.00 16.91 ? 121 TYR A CE2 1 
ATOM   942  C  CZ  . TYR A 1 121 ? 19.724  9.791   15.865  1.00 18.16 ? 121 TYR A CZ  1 
ATOM   943  O  OH  . TYR A 1 121 ? 19.814  10.176  17.167  1.00 20.45 ? 121 TYR A OH  1 
ATOM   944  N  N   . ASN A 1 122 ? 22.009  6.818   11.517  1.00 14.30 ? 122 ASN A N   1 
ATOM   945  C  CA  . ASN A 1 122 ? 23.367  6.607   11.979  1.00 15.40 ? 122 ASN A CA  1 
ATOM   946  C  C   . ASN A 1 122 ? 23.708  7.713   12.980  1.00 14.94 ? 122 ASN A C   1 
ATOM   947  O  O   . ASN A 1 122 ? 24.065  8.821   12.586  1.00 15.32 ? 122 ASN A O   1 
ATOM   948  C  CB  . ASN A 1 122 ? 24.342  6.564   10.800  1.00 17.37 ? 122 ASN A CB  1 
ATOM   949  C  CG  . ASN A 1 122 ? 25.795  6.355   11.205  1.00 17.88 ? 122 ASN A CG  1 
ATOM   950  O  OD1 . ASN A 1 122 ? 26.207  6.752   12.288  1.00 17.61 ? 122 ASN A OD1 1 
ATOM   951  N  ND2 . ASN A 1 122 ? 26.583  5.734   10.341  1.00 17.56 ? 122 ASN A ND2 1 
ATOM   952  N  N   . SER A 1 123 ? 23.598  7.397   14.275  1.00 14.42 ? 123 SER A N   1 
ATOM   953  C  CA  . SER A 1 123 ? 23.760  8.391   15.326  1.00 15.50 ? 123 SER A CA  1 
ATOM   954  C  C   . SER A 1 123 ? 25.232  8.624   15.660  1.00 16.88 ? 123 SER A C   1 
ATOM   955  O  O   . SER A 1 123 ? 25.551  9.575   16.376  1.00 16.52 ? 123 SER A O   1 
ATOM   956  C  CB  . SER A 1 123 ? 22.975  8.031   16.575  1.00 13.72 ? 123 SER A CB  1 
ATOM   957  O  OG  . SER A 1 123 ? 23.347  6.746   17.052  1.00 13.64 ? 123 SER A OG  1 
ATOM   958  N  N   . ASP A 1 124 ? 26.088  7.696   15.215  1.00 19.67 ? 124 ASP A N   1 
ATOM   959  C  CA  . ASP A 1 124 ? 27.537  7.823   15.295  1.00 22.59 ? 124 ASP A CA  1 
ATOM   960  C  C   . ASP A 1 124 ? 27.996  9.019   14.468  1.00 24.61 ? 124 ASP A C   1 
ATOM   961  O  O   . ASP A 1 124 ? 28.919  9.699   14.902  1.00 26.80 ? 124 ASP A O   1 
ATOM   962  C  CB  . ASP A 1 124 ? 28.274  6.528   14.896  1.00 22.03 ? 124 ASP A CB  1 
ATOM   963  C  CG  . ASP A 1 124 ? 28.238  5.458   15.973  1.00 23.26 ? 124 ASP A CG  1 
ATOM   964  O  OD1 . ASP A 1 124 ? 27.903  5.798   17.123  1.00 23.99 ? 124 ASP A OD1 1 
ATOM   965  O  OD2 . ASP A 1 124 ? 28.535  4.288   15.661  1.00 24.57 ? 124 ASP A OD2 1 
ATOM   966  N  N   . LEU A 1 125 ? 27.352  9.268   13.304  1.00 24.87 ? 125 LEU A N   1 
ATOM   967  C  CA  . LEU A 1 125 ? 27.843  10.251  12.343  1.00 25.02 ? 125 LEU A CA  1 
ATOM   968  C  C   . LEU A 1 125 ? 27.021  11.540  12.390  1.00 23.19 ? 125 LEU A C   1 
ATOM   969  O  O   . LEU A 1 125 ? 27.535  12.607  12.084  1.00 23.56 ? 125 LEU A O   1 
ATOM   970  C  CB  . LEU A 1 125 ? 27.866  9.708   10.904  1.00 25.01 ? 125 LEU A CB  1 
ATOM   971  C  CG  . LEU A 1 125 ? 28.575  8.388   10.585  1.00 26.08 ? 125 LEU A CG  1 
ATOM   972  C  CD1 . LEU A 1 125 ? 28.634  8.169   9.078   1.00 26.33 ? 125 LEU A CD1 1 
ATOM   973  C  CD2 . LEU A 1 125 ? 29.966  8.275   11.192  1.00 25.46 ? 125 LEU A CD2 1 
ATOM   974  N  N   . TYR A 1 126 ? 25.748  11.445  12.780  1.00 26.08 ? 126 TYR A N   1 
ATOM   975  C  CA  . TYR A 1 126 ? 24.777  12.505  12.537  1.00 24.54 ? 126 TYR A CA  1 
ATOM   976  C  C   . TYR A 1 126 ? 24.033  12.876  13.824  1.00 24.06 ? 126 TYR A C   1 
ATOM   977  O  O   . TYR A 1 126 ? 23.737  12.009  14.637  1.00 22.09 ? 126 TYR A O   1 
ATOM   978  C  CB  . TYR A 1 126 ? 23.865  12.116  11.362  1.00 26.36 ? 126 TYR A CB  1 
ATOM   979  C  CG  . TYR A 1 126 ? 24.621  11.790  10.096  1.00 24.01 ? 126 TYR A CG  1 
ATOM   980  C  CD1 . TYR A 1 126 ? 25.333  12.770  9.430   1.00 25.26 ? 126 TYR A CD1 1 
ATOM   981  C  CD2 . TYR A 1 126 ? 24.666  10.500  9.588   1.00 24.81 ? 126 TYR A CD2 1 
ATOM   982  C  CE1 . TYR A 1 126 ? 26.075  12.477  8.295   1.00 27.64 ? 126 TYR A CE1 1 
ATOM   983  C  CE2 . TYR A 1 126 ? 25.395  10.187  8.450   1.00 26.78 ? 126 TYR A CE2 1 
ATOM   984  C  CZ  . TYR A 1 126 ? 26.107  11.185  7.802   1.00 28.95 ? 126 TYR A CZ  1 
ATOM   985  O  OH  . TYR A 1 126 ? 26.850  10.916  6.687   1.00 30.95 ? 126 TYR A OH  1 
ATOM   986  N  N   . PRO A 1 127 ? 23.702  14.171  14.061  1.00 24.81 ? 127 PRO A N   1 
ATOM   987  C  CA  . PRO A 1 127 ? 22.934  14.562  15.246  1.00 26.28 ? 127 PRO A CA  1 
ATOM   988  C  C   . PRO A 1 127 ? 21.453  14.167  15.249  1.00 27.41 ? 127 PRO A C   1 
ATOM   989  O  O   . PRO A 1 127 ? 20.810  14.229  16.289  1.00 26.77 ? 127 PRO A O   1 
ATOM   990  C  CB  . PRO A 1 127 ? 23.096  16.096  15.298  1.00 26.41 ? 127 PRO A CB  1 
ATOM   991  C  CG  . PRO A 1 127 ? 23.369  16.509  13.874  1.00 23.91 ? 127 PRO A CG  1 
ATOM   992  C  CD  . PRO A 1 127 ? 24.097  15.334  13.249  1.00 25.04 ? 127 PRO A CD  1 
ATOM   993  N  N   . ASP A 1 128 ? 20.902  13.782  14.089  1.00 25.98 ? 128 ASP A N   1 
ATOM   994  C  CA  . ASP A 1 128 ? 19.479  13.489  13.997  1.00 27.82 ? 128 ASP A CA  1 
ATOM   995  C  C   . ASP A 1 128 ? 19.157  12.886  12.637  1.00 24.69 ? 128 ASP A C   1 
ATOM   996  O  O   . ASP A 1 128 ? 19.960  12.977  11.717  1.00 22.46 ? 128 ASP A O   1 
ATOM   997  C  CB  . ASP A 1 128 ? 18.614  14.723  14.295  1.00 31.40 ? 128 ASP A CB  1 
ATOM   998  C  CG  . ASP A 1 128 ? 18.817  15.878  13.333  1.00 36.04 ? 128 ASP A CG  1 
ATOM   999  O  OD1 . ASP A 1 128 ? 18.333  15.793  12.185  1.00 38.61 ? 128 ASP A OD1 1 
ATOM   1000 O  OD2 . ASP A 1 128 ? 19.469  16.848  13.736  1.00 42.56 ? 128 ASP A OD2 1 
ATOM   1001 N  N   . ALA A 1 129 ? 17.959  12.303  12.539  1.00 24.02 ? 129 ALA A N   1 
ATOM   1002 C  CA  . ALA A 1 129 ? 17.473  11.639  11.339  1.00 24.16 ? 129 ALA A CA  1 
ATOM   1003 C  C   . ALA A 1 129 ? 17.417  12.564  10.119  1.00 23.99 ? 129 ALA A C   1 
ATOM   1004 O  O   . ALA A 1 129 ? 17.729  12.131  9.004   1.00 23.33 ? 129 ALA A O   1 
ATOM   1005 C  CB  . ALA A 1 129 ? 16.132  10.995  11.619  1.00 25.06 ? 129 ALA A CB  1 
ATOM   1006 N  N   . SER A 1 130 ? 17.006  13.829  10.297  1.00 26.32 ? 130 SER A N   1 
ATOM   1007 C  CA  . SER A 1 130 ? 16.900  14.704  9.126   1.00 24.51 ? 130 SER A CA  1 
ATOM   1008 C  C   . SER A 1 130 ? 18.266  14.923  8.478   1.00 25.86 ? 130 SER A C   1 
ATOM   1009 O  O   . SER A 1 130 ? 18.398  14.785  7.252   1.00 24.43 ? 130 SER A O   1 
ATOM   1010 C  CB  . SER A 1 130 ? 16.138  15.998  9.367   1.00 26.80 ? 130 SER A CB  1 
ATOM   1011 O  OG  . SER A 1 130 ? 16.348  16.506  10.670  1.00 26.20 ? 130 SER A OG  1 
ATOM   1012 N  N   . THR A 1 131 ? 19.278  15.221  9.307   1.00 23.23 ? 131 THR A N   1 
ATOM   1013 C  CA  . THR A 1 131 ? 20.649  15.312  8.825   1.00 23.64 ? 131 THR A CA  1 
ATOM   1014 C  C   . THR A 1 131 ? 21.075  14.011  8.150   1.00 24.35 ? 131 THR A C   1 
ATOM   1015 O  O   . THR A 1 131 ? 21.639  14.041  7.051   1.00 24.15 ? 131 THR A O   1 
ATOM   1016 C  CB  . THR A 1 131 ? 21.602  15.717  9.959   1.00 25.04 ? 131 THR A CB  1 
ATOM   1017 O  OG1 . THR A 1 131 ? 21.129  16.987  10.403  1.00 23.17 ? 131 THR A OG1 1 
ATOM   1018 C  CG2 . THR A 1 131 ? 23.048  15.851  9.527   1.00 24.29 ? 131 THR A CG2 1 
ATOM   1019 N  N   . ALA A 1 132 ? 20.813  12.867  8.811   1.00 21.05 ? 132 ALA A N   1 
ATOM   1020 C  CA  . ALA A 1 132 ? 21.275  11.585  8.290   1.00 20.76 ? 132 ALA A CA  1 
ATOM   1021 C  C   . ALA A 1 132 ? 20.654  11.329  6.913   1.00 19.54 ? 132 ALA A C   1 
ATOM   1022 O  O   . ALA A 1 132 ? 21.270  10.711  6.046   1.00 20.49 ? 132 ALA A O   1 
ATOM   1023 C  CB  . ALA A 1 132 ? 20.932  10.475  9.263   1.00 18.94 ? 132 ALA A CB  1 
ATOM   1024 N  N   . SER A 1 133 ? 19.426  11.817  6.723   1.00 19.89 ? 133 SER A N   1 
ATOM   1025 C  CA  . SER A 1 133 ? 18.617  11.430  5.579   1.00 19.95 ? 133 SER A CA  1 
ATOM   1026 C  C   . SER A 1 133 ? 19.158  12.021  4.282   1.00 21.28 ? 133 SER A C   1 
ATOM   1027 O  O   . SER A 1 133 ? 18.698  11.627  3.215   1.00 21.69 ? 133 SER A O   1 
ATOM   1028 C  CB  . SER A 1 133 ? 17.170  11.765  5.783   1.00 19.13 ? 133 SER A CB  1 
ATOM   1029 O  OG  . SER A 1 133 ? 16.961  13.163  5.766   1.00 18.81 ? 133 SER A OG  1 
ATOM   1030 N  N   . ASN A 1 134 ? 20.153  12.917  4.391   1.00 20.34 ? 134 ASN A N   1 
ATOM   1031 C  CA  . ASN A 1 134 ? 20.786  13.554  3.245   1.00 21.89 ? 134 ASN A CA  1 
ATOM   1032 C  C   . ASN A 1 134 ? 22.108  12.877  2.880   1.00 23.79 ? 134 ASN A C   1 
ATOM   1033 O  O   . ASN A 1 134 ? 22.758  13.255  1.902   1.00 23.36 ? 134 ASN A O   1 
ATOM   1034 C  CB  . ASN A 1 134 ? 20.977  15.050  3.500   1.00 22.11 ? 134 ASN A CB  1 
ATOM   1035 C  CG  . ASN A 1 134 ? 19.675  15.798  3.345   1.00 23.33 ? 134 ASN A CG  1 
ATOM   1036 O  OD1 . ASN A 1 134 ? 19.374  16.726  4.104   1.00 24.28 ? 134 ASN A OD1 1 
ATOM   1037 N  ND2 . ASN A 1 134 ? 18.884  15.380  2.367   1.00 21.91 ? 134 ASN A ND2 1 
ATOM   1038 N  N   . LYS A 1 135 ? 22.514  11.864  3.657   1.00 24.71 ? 135 LYS A N   1 
ATOM   1039 C  CA  . LYS A 1 135 ? 23.796  11.222  3.416   1.00 23.62 ? 135 LYS A CA  1 
ATOM   1040 C  C   . LYS A 1 135 ? 23.589  9.738   3.163   1.00 23.63 ? 135 LYS A C   1 
ATOM   1041 O  O   . LYS A 1 135 ? 22.705  9.135   3.768   1.00 21.69 ? 135 LYS A O   1 
ATOM   1042 C  CB  . LYS A 1 135 ? 24.729  11.370  4.620   1.00 26.67 ? 135 LYS A CB  1 
ATOM   1043 C  CG  . LYS A 1 135 ? 25.171  12.789  4.956   1.00 28.84 ? 135 LYS A CG  1 
ATOM   1044 C  CD  . LYS A 1 135 ? 24.064  13.661  5.513   1.00 31.78 ? 135 LYS A CD  1 
ATOM   1045 C  CE  . LYS A 1 135 ? 24.580  14.981  6.052   1.00 32.06 ? 135 LYS A CE  1 
ATOM   1046 N  NZ  . LYS A 1 135 ? 23.597  16.082  5.933   1.00 31.72 ? 135 LYS A NZ  1 
ATOM   1047 N  N   . SER A 1 136 ? 24.456  9.186   2.299   1.00 22.06 ? 136 SER A N   1 
ATOM   1048 C  CA  . SER A 1 136 ? 24.478  7.790   1.896   1.00 26.57 ? 136 SER A CA  1 
ATOM   1049 C  C   . SER A 1 136 ? 24.570  6.903   3.139   1.00 24.68 ? 136 SER A C   1 
ATOM   1050 O  O   . SER A 1 136 ? 25.445  7.096   3.971   1.00 22.74 ? 136 SER A O   1 
ATOM   1051 C  CB  . SER A 1 136 ? 25.656  7.553   0.960   1.00 28.81 ? 136 SER A CB  1 
ATOM   1052 O  OG  . SER A 1 136 ? 25.634  6.237   0.412   1.00 33.07 ? 136 SER A OG  1 
ATOM   1053 N  N   . GLU A 1 137 ? 23.638  5.956   3.284   1.00 24.90 ? 137 GLU A N   1 
ATOM   1054 C  CA  . GLU A 1 137 ? 23.665  5.029   4.410   1.00 25.04 ? 137 GLU A CA  1 
ATOM   1055 C  C   . GLU A 1 137 ? 23.350  5.744   5.725   1.00 21.64 ? 137 GLU A C   1 
ATOM   1056 O  O   . GLU A 1 137 ? 23.468  5.126   6.783   1.00 22.76 ? 137 GLU A O   1 
ATOM   1057 C  CB  . GLU A 1 137 ? 25.030  4.350   4.583   1.00 28.45 ? 137 GLU A CB  1 
ATOM   1058 C  CG  . GLU A 1 137 ? 25.674  3.842   3.305   1.00 35.43 ? 137 GLU A CG  1 
ATOM   1059 C  CD  . GLU A 1 137 ? 25.032  2.578   2.775   1.00 40.24 ? 137 GLU A CD  1 
ATOM   1060 O  OE1 . GLU A 1 137 ? 25.770  1.618   2.455   1.00 36.13 ? 137 GLU A OE1 1 
ATOM   1061 O  OE2 . GLU A 1 137 ? 23.782  2.567   2.689   1.00 51.81 ? 137 GLU A OE2 1 
ATOM   1062 N  N   . GLY A 1 138 ? 22.931  7.016   5.652   1.00 17.53 ? 138 GLY A N   1 
ATOM   1063 C  CA  . GLY A 1 138 ? 22.498  7.791   6.810   1.00 14.37 ? 138 GLY A CA  1 
ATOM   1064 C  C   . GLY A 1 138 ? 21.369  7.113   7.604   1.00 12.66 ? 138 GLY A C   1 
ATOM   1065 O  O   . GLY A 1 138 ? 21.307  7.231   8.815   1.00 11.58 ? 138 GLY A O   1 
ATOM   1066 N  N   . LEU A 1 139 ? 20.434  6.453   6.923   1.00 11.01 ? 139 LEU A N   1 
ATOM   1067 C  CA  . LEU A 1 139 ? 19.346  5.788   7.623   1.00 10.28 ? 139 LEU A CA  1 
ATOM   1068 C  C   . LEU A 1 139 ? 19.463  4.285   7.398   1.00 9.19  ? 139 LEU A C   1 
ATOM   1069 O  O   . LEU A 1 139 ? 19.958  3.862   6.373   1.00 9.23  ? 139 LEU A O   1 
ATOM   1070 C  CB  . LEU A 1 139 ? 18.002  6.307   7.098   1.00 10.31 ? 139 LEU A CB  1 
ATOM   1071 C  CG  . LEU A 1 139 ? 17.791  7.829   7.132   1.00 10.80 ? 139 LEU A CG  1 
ATOM   1072 C  CD1 . LEU A 1 139 ? 16.490  8.218   6.439   1.00 10.62 ? 139 LEU A CD1 1 
ATOM   1073 C  CD2 . LEU A 1 139 ? 17.805  8.382   8.554   1.00 10.55 ? 139 LEU A CD2 1 
ATOM   1074 N  N   . ALA A 1 140 ? 19.007  3.496   8.372   1.00 8.86  ? 140 ALA A N   1 
ATOM   1075 C  CA  . ALA A 1 140 ? 18.858  2.059   8.232   1.00 8.19  ? 140 ALA A CA  1 
ATOM   1076 C  C   . ALA A 1 140 ? 17.428  1.739   8.630   1.00 8.17  ? 140 ALA A C   1 
ATOM   1077 O  O   . ALA A 1 140 ? 16.973  2.165   9.698   1.00 8.78  ? 140 ALA A O   1 
ATOM   1078 C  CB  . ALA A 1 140 ? 19.841  1.313   9.131   1.00 7.95  ? 140 ALA A CB  1 
ATOM   1079 N  N   . VAL A 1 141 ? 16.716  1.033   7.747   1.00 7.93  ? 141 VAL A N   1 
ATOM   1080 C  CA  . VAL A 1 141 ? 15.344  0.649   8.032   1.00 7.55  ? 141 VAL A CA  1 
ATOM   1081 C  C   . VAL A 1 141 ? 15.269  -0.870  8.114   1.00 7.43  ? 141 VAL A C   1 
ATOM   1082 O  O   . VAL A 1 141 ? 15.865  -1.566  7.300   1.00 6.95  ? 141 VAL A O   1 
ATOM   1083 C  CB  . VAL A 1 141 ? 14.351  1.179   6.983   1.00 7.45  ? 141 VAL A CB  1 
ATOM   1084 C  CG1 . VAL A 1 141 ? 12.920  0.741   7.327   1.00 7.42  ? 141 VAL A CG1 1 
ATOM   1085 C  CG2 . VAL A 1 141 ? 14.415  2.686   6.908   1.00 7.48  ? 141 VAL A CG2 1 
ATOM   1086 N  N   . LEU A 1 142 ? 14.567  -1.361  9.136   1.00 7.61  ? 142 LEU A N   1 
ATOM   1087 C  CA  . LEU A 1 142 ? 14.241  -2.782  9.206   1.00 7.85  ? 142 LEU A CA  1 
ATOM   1088 C  C   . LEU A 1 142 ? 12.811  -2.931  8.692   1.00 8.20  ? 142 LEU A C   1 
ATOM   1089 O  O   . LEU A 1 142 ? 11.922  -2.208  9.127   1.00 8.40  ? 142 LEU A O   1 
ATOM   1090 C  CB  . LEU A 1 142 ? 14.342  -3.311  10.646  1.00 7.82  ? 142 LEU A CB  1 
ATOM   1091 C  CG  . LEU A 1 142 ? 15.657  -3.101  11.419  1.00 8.22  ? 142 LEU A CG  1 
ATOM   1092 C  CD1 . LEU A 1 142 ? 15.580  -3.765  12.784  1.00 8.41  ? 142 LEU A CD1 1 
ATOM   1093 C  CD2 . LEU A 1 142 ? 16.880  -3.621  10.663  1.00 8.26  ? 142 LEU A CD2 1 
ATOM   1094 N  N   . ALA A 1 143 ? 12.605  -3.839  7.732   1.00 8.41  ? 143 ALA A N   1 
ATOM   1095 C  CA  . ALA A 1 143 ? 11.281  -4.071  7.190   1.00 8.24  ? 143 ALA A CA  1 
ATOM   1096 C  C   . ALA A 1 143 ? 10.821  -5.477  7.567   1.00 8.30  ? 143 ALA A C   1 
ATOM   1097 O  O   . ALA A 1 143 ? 11.524  -6.467  7.323   1.00 8.62  ? 143 ALA A O   1 
ATOM   1098 C  CB  . ALA A 1 143 ? 11.284  -3.872  5.687   1.00 8.13  ? 143 ALA A CB  1 
ATOM   1099 N  N   . VAL A 1 144 ? 9.622   -5.547  8.137   1.00 8.14  ? 144 VAL A N   1 
ATOM   1100 C  CA  . VAL A 1 144 ? 9.017   -6.813  8.524   1.00 8.63  ? 144 VAL A CA  1 
ATOM   1101 C  C   . VAL A 1 144 ? 7.787   -7.009  7.645   1.00 8.71  ? 144 VAL A C   1 
ATOM   1102 O  O   . VAL A 1 144 ? 6.920   -6.145  7.599   1.00 8.25  ? 144 VAL A O   1 
ATOM   1103 C  CB  . VAL A 1 144 ? 8.660   -6.831  10.027  1.00 9.03  ? 144 VAL A CB  1 
ATOM   1104 C  CG1 . VAL A 1 144 ? 7.943   -8.116  10.394  1.00 9.02  ? 144 VAL A CG1 1 
ATOM   1105 C  CG2 . VAL A 1 144 ? 9.889   -6.678  10.922  1.00 8.54  ? 144 VAL A CG2 1 
ATOM   1106 N  N   . LEU A 1 145 ? 7.759   -8.107  6.877   1.00 9.18  ? 145 LEU A N   1 
ATOM   1107 C  CA  . LEU A 1 145 ? 6.599   -8.394  6.053   1.00 8.69  ? 145 LEU A CA  1 
ATOM   1108 C  C   . LEU A 1 145 ? 5.531   -9.065  6.911   1.00 9.18  ? 145 LEU A C   1 
ATOM   1109 O  O   . LEU A 1 145 ? 5.829   -9.946  7.739   1.00 8.89  ? 145 LEU A O   1 
ATOM   1110 C  CB  . LEU A 1 145 ? 7.002   -9.332  4.913   1.00 9.19  ? 145 LEU A CB  1 
ATOM   1111 C  CG  . LEU A 1 145 ? 8.036   -8.812  3.919   1.00 8.59  ? 145 LEU A CG  1 
ATOM   1112 C  CD1 . LEU A 1 145 ? 8.582   -9.986  3.125   1.00 8.93  ? 145 LEU A CD1 1 
ATOM   1113 C  CD2 . LEU A 1 145 ? 7.412   -7.770  2.985   1.00 9.00  ? 145 LEU A CD2 1 
ATOM   1114 N  N   . ILE A 1 146 ? 4.288   -8.657  6.664   1.00 9.13  ? 146 ILE A N   1 
ATOM   1115 C  CA  . ILE A 1 146 ? 3.162   -9.037  7.498   1.00 9.47  ? 146 ILE A CA  1 
ATOM   1116 C  C   . ILE A 1 146 ? 2.159   -9.808  6.637   1.00 10.21 ? 146 ILE A C   1 
ATOM   1117 O  O   . ILE A 1 146 ? 1.727   -9.319  5.594   1.00 10.01 ? 146 ILE A O   1 
ATOM   1118 C  CB  . ILE A 1 146 ? 2.544   -7.791  8.143   1.00 9.24  ? 146 ILE A CB  1 
ATOM   1119 C  CG1 . ILE A 1 146 ? 3.554   -7.038  9.028   1.00 9.28  ? 146 ILE A CG1 1 
ATOM   1120 C  CG2 . ILE A 1 146 ? 1.282   -8.190  8.896   1.00 9.58  ? 146 ILE A CG2 1 
ATOM   1121 C  CD1 . ILE A 1 146 ? 3.040   -5.708  9.590   1.00 8.19  ? 146 ILE A CD1 1 
ATOM   1122 N  N   . GLU A 1 147 ? 1.840   -11.041 7.051   1.00 11.37 ? 147 GLU A N   1 
ATOM   1123 C  CA  . GLU A 1 147 ? 0.833   -11.819 6.350   1.00 12.60 ? 147 GLU A CA  1 
ATOM   1124 C  C   . GLU A 1 147 ? -0.352  -12.067 7.283   1.00 12.13 ? 147 GLU A C   1 
ATOM   1125 O  O   . GLU A 1 147 ? -0.208  -12.073 8.504   1.00 10.92 ? 147 GLU A O   1 
ATOM   1126 C  CB  . GLU A 1 147 ? 1.426   -13.091 5.734   1.00 15.32 ? 147 GLU A CB  1 
ATOM   1127 C  CG  . GLU A 1 147 ? 2.223   -13.927 6.697   1.00 20.14 ? 147 GLU A CG  1 
ATOM   1128 C  CD  . GLU A 1 147 ? 2.579   -15.348 6.265   1.00 23.81 ? 147 GLU A CD  1 
ATOM   1129 O  OE1 . GLU A 1 147 ? 2.419   -15.655 5.060   1.00 23.75 ? 147 GLU A OE1 1 
ATOM   1130 O  OE2 . GLU A 1 147 ? 3.022   -16.156 7.158   1.00 24.89 ? 147 GLU A OE2 1 
ATOM   1131 N  N   . MET A 1 148 ? -1.532  -12.246 6.687   1.00 11.71 ? 148 MET A N   1 
ATOM   1132 C  CA  . MET A 1 148 ? -2.713  -12.609 7.441   1.00 12.57 ? 148 MET A CA  1 
ATOM   1133 C  C   . MET A 1 148 ? -2.455  -13.981 8.068   1.00 12.93 ? 148 MET A C   1 
ATOM   1134 O  O   . MET A 1 148 ? -1.904  -14.883 7.432   1.00 12.47 ? 148 MET A O   1 
ATOM   1135 C  CB  . MET A 1 148 ? -3.940  -12.664 6.519   1.00 13.72 ? 148 MET A CB  1 
ATOM   1136 C  CG  . MET A 1 148 ? -5.241  -13.004 7.242   1.00 14.76 ? 148 MET A CG  1 
ATOM   1137 S  SD  . MET A 1 148 ? -6.601  -13.145 6.060   1.00 18.95 ? 148 MET A SD  1 
ATOM   1138 C  CE  . MET A 1 148 ? -6.519  -11.503 5.332   1.00 15.16 ? 148 MET A CE  1 
ATOM   1139 N  N   . GLY A 1 149 ? -2.772  -14.089 9.357   1.00 11.97 ? 149 GLY A N   1 
ATOM   1140 C  CA  . GLY A 1 149 ? -2.432  -15.286 10.100  1.00 11.18 ? 149 GLY A CA  1 
ATOM   1141 C  C   . GLY A 1 149 ? -3.089  -15.290 11.474  1.00 10.41 ? 149 GLY A C   1 
ATOM   1142 O  O   . GLY A 1 149 ? -4.250  -14.905 11.619  1.00 11.12 ? 149 GLY A O   1 
ATOM   1143 N  N   . SER A 1 150 ? -2.308  -15.711 12.470  1.00 10.65 ? 150 SER A N   1 
ATOM   1144 C  CA  . SER A 1 150 ? -2.721  -15.788 13.863  1.00 10.83 ? 150 SER A CA  1 
ATOM   1145 C  C   . SER A 1 150 ? -2.873  -14.383 14.434  1.00 11.47 ? 150 SER A C   1 
ATOM   1146 O  O   . SER A 1 150 ? -2.168  -13.479 14.004  1.00 10.86 ? 150 SER A O   1 
ATOM   1147 C  CB  . SER A 1 150 ? -1.686  -16.571 14.638  1.00 11.56 ? 150 SER A CB  1 
ATOM   1148 O  OG  . SER A 1 150 ? -1.679  -17.946 14.226  1.00 11.97 ? 150 SER A OG  1 
ATOM   1149 N  N   . PHE A 1 151 ? -3.804  -14.210 15.380  1.00 11.58 ? 151 PHE A N   1 
ATOM   1150 C  CA  . PHE A 1 151 ? -3.824  -13.012 16.207  1.00 12.40 ? 151 PHE A CA  1 
ATOM   1151 C  C   . PHE A 1 151 ? -2.434  -12.779 16.814  1.00 11.76 ? 151 PHE A C   1 
ATOM   1152 O  O   . PHE A 1 151 ? -1.857  -13.685 17.406  1.00 11.91 ? 151 PHE A O   1 
ATOM   1153 C  CB  . PHE A 1 151 ? -4.872  -13.120 17.325  1.00 12.51 ? 151 PHE A CB  1 
ATOM   1154 C  CG  . PHE A 1 151 ? -4.876  -11.918 18.248  1.00 13.13 ? 151 PHE A CG  1 
ATOM   1155 C  CD1 . PHE A 1 151 ? -5.463  -10.719 17.855  1.00 12.37 ? 151 PHE A CD1 1 
ATOM   1156 C  CD2 . PHE A 1 151 ? -4.241  -11.972 19.486  1.00 13.50 ? 151 PHE A CD2 1 
ATOM   1157 C  CE1 . PHE A 1 151 ? -5.464  -9.618  18.702  1.00 13.31 ? 151 PHE A CE1 1 
ATOM   1158 C  CE2 . PHE A 1 151 ? -4.214  -10.861 20.325  1.00 13.61 ? 151 PHE A CE2 1 
ATOM   1159 C  CZ  . PHE A 1 151 ? -4.813  -9.682  19.930  1.00 13.41 ? 151 PHE A CZ  1 
ATOM   1160 N  N   . ASN A 1 152 ? -1.932  -11.540 16.699  1.00 11.99 ? 152 ASN A N   1 
ATOM   1161 C  CA  . ASN A 1 152 ? -0.617  -11.143 17.182  1.00 12.05 ? 152 ASN A CA  1 
ATOM   1162 C  C   . ASN A 1 152 ? -0.800  -10.128 18.313  1.00 11.97 ? 152 ASN A C   1 
ATOM   1163 O  O   . ASN A 1 152 ? -1.109  -8.964  18.065  1.00 11.87 ? 152 ASN A O   1 
ATOM   1164 C  CB  . ASN A 1 152 ? 0.290   -10.601 16.058  1.00 11.93 ? 152 ASN A CB  1 
ATOM   1165 C  CG  . ASN A 1 152 ? 1.757   -10.608 16.441  1.00 12.65 ? 152 ASN A CG  1 
ATOM   1166 O  OD1 . ASN A 1 152 ? 2.097   -10.218 17.561  1.00 12.77 ? 152 ASN A OD1 1 
ATOM   1167 N  ND2 . ASN A 1 152 ? 2.613   -11.139 15.571  1.00 11.34 ? 152 ASN A ND2 1 
ATOM   1168 N  N   . PRO A 1 153 ? -0.614  -10.556 19.580  1.00 12.18 ? 153 PRO A N   1 
ATOM   1169 C  CA  . PRO A 1 153 ? -0.765  -9.674  20.743  1.00 12.31 ? 153 PRO A CA  1 
ATOM   1170 C  C   . PRO A 1 153 ? 0.198   -8.493  20.809  1.00 13.07 ? 153 PRO A C   1 
ATOM   1171 O  O   . PRO A 1 153 ? -0.145  -7.416  21.327  1.00 12.63 ? 153 PRO A O   1 
ATOM   1172 C  CB  . PRO A 1 153 ? -0.557  -10.618 21.940  1.00 12.88 ? 153 PRO A CB  1 
ATOM   1173 C  CG  . PRO A 1 153 ? -0.830  -12.011 21.391  1.00 12.84 ? 153 PRO A CG  1 
ATOM   1174 C  CD  . PRO A 1 153 ? -0.364  -11.964 19.952  1.00 12.04 ? 153 PRO A CD  1 
ATOM   1175 N  N   . SER A 1 154 ? 1.406   -8.702  20.274  1.00 12.69 ? 154 SER A N   1 
ATOM   1176 C  CA  . SER A 1 154 ? 2.425   -7.663  20.213  1.00 12.59 ? 154 SER A CA  1 
ATOM   1177 C  C   . SER A 1 154 ? 2.014   -6.532  19.274  1.00 12.59 ? 154 SER A C   1 
ATOM   1178 O  O   . SER A 1 154 ? 2.191   -5.364  19.610  1.00 12.42 ? 154 SER A O   1 
ATOM   1179 C  CB  . SER A 1 154 ? 3.734   -8.241  19.799  1.00 12.42 ? 154 SER A CB  1 
ATOM   1180 O  OG  . SER A 1 154 ? 4.057   -9.291  20.692  1.00 13.07 ? 154 SER A OG  1 
ATOM   1181 N  N   . TYR A 1 155 ? 1.521   -6.883  18.077  1.00 11.52 ? 155 TYR A N   1 
ATOM   1182 C  CA  . TYR A 1 155 ? 1.030   -5.871  17.148  1.00 11.04 ? 155 TYR A CA  1 
ATOM   1183 C  C   . TYR A 1 155 ? -0.226  -5.193  17.694  1.00 11.73 ? 155 TYR A C   1 
ATOM   1184 O  O   . TYR A 1 155 ? -0.457  -4.006  17.436  1.00 10.89 ? 155 TYR A O   1 
ATOM   1185 C  CB  . TYR A 1 155 ? 0.805   -6.465  15.751  1.00 10.67 ? 155 TYR A CB  1 
ATOM   1186 C  CG  . TYR A 1 155 ? 2.070   -6.501  14.924  1.00 10.49 ? 155 TYR A CG  1 
ATOM   1187 C  CD1 . TYR A 1 155 ? 2.966   -7.556  15.029  1.00 10.20 ? 155 TYR A CD1 1 
ATOM   1188 C  CD2 . TYR A 1 155 ? 2.396   -5.463  14.064  1.00 10.44 ? 155 TYR A CD2 1 
ATOM   1189 C  CE1 . TYR A 1 155 ? 4.142   -7.588  14.296  1.00 10.42 ? 155 TYR A CE1 1 
ATOM   1190 C  CE2 . TYR A 1 155 ? 3.567   -5.486  13.312  1.00 10.05 ? 155 TYR A CE2 1 
ATOM   1191 C  CZ  . TYR A 1 155 ? 4.448   -6.547  13.430  1.00 10.25 ? 155 TYR A CZ  1 
ATOM   1192 O  OH  . TYR A 1 155 ? 5.602   -6.586  12.694  1.00 9.23  ? 155 TYR A OH  1 
ATOM   1193 N  N   . ASP A 1 156 ? -1.014  -5.927  18.496  1.00 11.88 ? 156 ASP A N   1 
ATOM   1194 C  CA  . ASP A 1 156 ? -2.178  -5.291  19.088  1.00 12.80 ? 156 ASP A CA  1 
ATOM   1195 C  C   . ASP A 1 156 ? -1.767  -4.169  20.043  1.00 14.04 ? 156 ASP A C   1 
ATOM   1196 O  O   . ASP A 1 156 ? -2.566  -3.264  20.290  1.00 12.93 ? 156 ASP A O   1 
ATOM   1197 C  CB  . ASP A 1 156 ? -3.170  -6.289  19.683  1.00 13.84 ? 156 ASP A CB  1 
ATOM   1198 C  CG  . ASP A 1 156 ? -4.573  -6.071  19.123  1.00 15.74 ? 156 ASP A CG  1 
ATOM   1199 O  OD1 . ASP A 1 156 ? -4.700  -5.877  17.865  1.00 14.77 ? 156 ASP A OD1 1 
ATOM   1200 O  OD2 . ASP A 1 156 ? -5.535  -6.098  19.933  1.00 16.28 ? 156 ASP A OD2 1 
ATOM   1201 N  N   . LYS A 1 157 ? -0.512  -4.192  20.525  1.00 13.84 ? 157 LYS A N   1 
ATOM   1202 C  CA  . LYS A 1 157 ? -0.046  -3.112  21.388  1.00 15.45 ? 157 LYS A CA  1 
ATOM   1203 C  C   . LYS A 1 157 ? -0.067  -1.770  20.648  1.00 14.43 ? 157 LYS A C   1 
ATOM   1204 O  O   . LYS A 1 157 ? -0.082  -0.723  21.287  1.00 13.51 ? 157 LYS A O   1 
ATOM   1205 C  CB  . LYS A 1 157 ? 1.376   -3.394  21.877  1.00 17.28 ? 157 LYS A CB  1 
ATOM   1206 C  CG  . LYS A 1 157 ? 1.552   -4.708  22.633  1.00 20.44 ? 157 LYS A CG  1 
ATOM   1207 C  CD  . LYS A 1 157 ? 1.624   -4.549  24.125  1.00 22.78 ? 157 LYS A CD  1 
ATOM   1208 C  CE  . LYS A 1 157 ? 1.591   -5.867  24.867  1.00 26.86 ? 157 LYS A CE  1 
ATOM   1209 N  NZ  . LYS A 1 157 ? 0.816   -5.726  26.121  1.00 29.98 ? 157 LYS A NZ  1 
ATOM   1210 N  N   . ILE A 1 158 ? 0.013   -1.812  19.310  1.00 13.01 ? 158 ILE A N   1 
ATOM   1211 C  CA  . ILE A 1 158 ? -0.122  -0.636  18.463  1.00 11.37 ? 158 ILE A CA  1 
ATOM   1212 C  C   . ILE A 1 158 ? -1.596  -0.510  18.100  1.00 10.54 ? 158 ILE A C   1 
ATOM   1213 O  O   . ILE A 1 158 ? -2.210  0.547   18.265  1.00 10.53 ? 158 ILE A O   1 
ATOM   1214 C  CB  . ILE A 1 158 ? 0.743   -0.767  17.181  1.00 11.37 ? 158 ILE A CB  1 
ATOM   1215 C  CG1 . ILE A 1 158 ? 2.229   -0.913  17.529  1.00 10.94 ? 158 ILE A CG1 1 
ATOM   1216 C  CG2 . ILE A 1 158 ? 0.446   0.375   16.180  1.00 10.89 ? 158 ILE A CG2 1 
ATOM   1217 C  CD1 . ILE A 1 158 ? 3.175   -1.102  16.356  1.00 11.32 ? 158 ILE A CD1 1 
ATOM   1218 N  N   . PHE A 1 159 ? -2.169  -1.613  17.600  1.00 10.72 ? 159 PHE A N   1 
ATOM   1219 C  CA  . PHE A 1 159 ? -3.455  -1.553  16.923  1.00 11.00 ? 159 PHE A CA  1 
ATOM   1220 C  C   . PHE A 1 159 ? -4.595  -1.141  17.855  1.00 11.01 ? 159 PHE A C   1 
ATOM   1221 O  O   . PHE A 1 159 ? -5.564  -0.542  17.407  1.00 11.84 ? 159 PHE A O   1 
ATOM   1222 C  CB  . PHE A 1 159 ? -3.772  -2.869  16.202  1.00 10.85 ? 159 PHE A CB  1 
ATOM   1223 C  CG  . PHE A 1 159 ? -2.818  -3.245  15.089  1.00 10.40 ? 159 PHE A CG  1 
ATOM   1224 C  CD1 . PHE A 1 159 ? -2.112  -2.279  14.385  1.00 9.67  ? 159 PHE A CD1 1 
ATOM   1225 C  CD2 . PHE A 1 159 ? -2.664  -4.576  14.716  1.00 10.00 ? 159 PHE A CD2 1 
ATOM   1226 C  CE1 . PHE A 1 159 ? -1.251  -2.628  13.356  1.00 9.72  ? 159 PHE A CE1 1 
ATOM   1227 C  CE2 . PHE A 1 159 ? -1.821  -4.920  13.668  1.00 9.74  ? 159 PHE A CE2 1 
ATOM   1228 C  CZ  . PHE A 1 159 ? -1.113  -3.952  12.989  1.00 9.75  ? 159 PHE A CZ  1 
ATOM   1229 N  N   . SER A 1 160 ? -4.507  -1.506  19.134  1.00 11.55 ? 160 SER A N   1 
ATOM   1230 C  CA  . SER A 1 160 ? -5.555  -1.194  20.084  1.00 11.56 ? 160 SER A CA  1 
ATOM   1231 C  C   . SER A 1 160 ? -5.707  0.319   20.248  1.00 11.79 ? 160 SER A C   1 
ATOM   1232 O  O   . SER A 1 160 ? -6.683  0.751   20.857  1.00 12.19 ? 160 SER A O   1 
ATOM   1233 C  CB  . SER A 1 160 ? -5.256  -1.841  21.413  1.00 11.68 ? 160 SER A CB  1 
ATOM   1234 O  OG  . SER A 1 160 ? -3.998  -1.404  21.875  1.00 12.02 ? 160 SER A OG  1 
ATOM   1235 N  N   . HIS A 1 161 ? -4.740  1.123   19.744  1.00 11.59 ? 161 HIS A N   1 
ATOM   1236 C  CA  . HIS A 1 161 ? -4.754  2.571   19.933  1.00 11.70 ? 161 HIS A CA  1 
ATOM   1237 C  C   . HIS A 1 161 ? -5.236  3.323   18.682  1.00 12.51 ? 161 HIS A C   1 
ATOM   1238 O  O   . HIS A 1 161 ? -5.358  4.564   18.728  1.00 11.94 ? 161 HIS A O   1 
ATOM   1239 C  CB  . HIS A 1 161 ? -3.368  3.115   20.379  1.00 11.85 ? 161 HIS A CB  1 
ATOM   1240 C  CG  . HIS A 1 161 ? -2.906  2.663   21.722  1.00 12.87 ? 161 HIS A CG  1 
ATOM   1241 N  ND1 . HIS A 1 161 ? -3.127  3.401   22.875  1.00 13.69 ? 161 HIS A ND1 1 
ATOM   1242 C  CD2 . HIS A 1 161 ? -2.251  1.549   22.110  1.00 12.98 ? 161 HIS A CD2 1 
ATOM   1243 C  CE1 . HIS A 1 161 ? -2.629  2.762   23.911  1.00 13.75 ? 161 HIS A CE1 1 
ATOM   1244 N  NE2 . HIS A 1 161 ? -2.089  1.616   23.469  1.00 14.50 ? 161 HIS A NE2 1 
ATOM   1245 N  N   . LEU A 1 162 ? -5.493  2.583   17.576  1.00 12.44 ? 162 LEU A N   1 
ATOM   1246 C  CA  . LEU A 1 162 ? -5.854  3.158   16.281  1.00 12.96 ? 162 LEU A CA  1 
ATOM   1247 C  C   . LEU A 1 162 ? -7.064  4.074   16.418  1.00 13.83 ? 162 LEU A C   1 
ATOM   1248 O  O   . LEU A 1 162 ? -7.096  5.150   15.829  1.00 12.69 ? 162 LEU A O   1 
ATOM   1249 C  CB  . LEU A 1 162 ? -6.165  2.055   15.260  1.00 12.51 ? 162 LEU A CB  1 
ATOM   1250 C  CG  . LEU A 1 162 ? -4.969  1.222   14.780  1.00 13.08 ? 162 LEU A CG  1 
ATOM   1251 C  CD1 . LEU A 1 162 ? -5.380  0.282   13.655  1.00 13.57 ? 162 LEU A CD1 1 
ATOM   1252 C  CD2 . LEU A 1 162 ? -3.824  2.101   14.324  1.00 13.27 ? 162 LEU A CD2 1 
ATOM   1253 N  N   . GLN A 1 163 ? -8.047  3.658   17.217  1.00 15.09 ? 163 GLN A N   1 
ATOM   1254 C  CA  . GLN A 1 163 ? -9.275  4.436   17.352  1.00 17.93 ? 163 GLN A CA  1 
ATOM   1255 C  C   . GLN A 1 163 ? -9.059  5.799   18.024  1.00 18.16 ? 163 GLN A C   1 
ATOM   1256 O  O   . GLN A 1 163 ? -9.992  6.593   18.094  1.00 19.24 ? 163 GLN A O   1 
ATOM   1257 C  CB  . GLN A 1 163 ? -10.405 3.640   18.020  1.00 21.15 ? 163 GLN A CB  1 
ATOM   1258 C  CG  . GLN A 1 163 ? -10.817 2.362   17.276  1.00 24.48 ? 163 GLN A CG  1 
ATOM   1259 C  CD  . GLN A 1 163 ? -11.282 2.502   15.846  1.00 25.70 ? 163 GLN A CD  1 
ATOM   1260 O  OE1 . GLN A 1 163 ? -11.102 1.593   15.035  1.00 30.40 ? 163 GLN A OE1 1 
ATOM   1261 N  NE2 . GLN A 1 163 ? -11.897 3.625   15.518  1.00 24.86 ? 163 GLN A NE2 1 
ATOM   1262 N  N   . HIS A 1 164 ? -7.852  6.104   18.510  1.00 17.77 ? 164 HIS A N   1 
ATOM   1263 C  CA  . HIS A 1 164 ? -7.618  7.431   19.064  1.00 17.30 ? 164 HIS A CA  1 
ATOM   1264 C  C   . HIS A 1 164 ? -6.736  8.266   18.134  1.00 15.16 ? 164 HIS A C   1 
ATOM   1265 O  O   . HIS A 1 164 ? -6.330  9.361   18.502  1.00 14.44 ? 164 HIS A O   1 
ATOM   1266 C  CB  . HIS A 1 164 ? -6.995  7.357   20.473  1.00 19.68 ? 164 HIS A CB  1 
ATOM   1267 C  CG  . HIS A 1 164 ? -7.811  6.619   21.485  1.00 24.25 ? 164 HIS A CG  1 
ATOM   1268 N  ND1 . HIS A 1 164 ? -9.117  6.979   21.808  1.00 27.33 ? 164 HIS A ND1 1 
ATOM   1269 C  CD2 . HIS A 1 164 ? -7.505  5.581   22.291  1.00 26.00 ? 164 HIS A CD2 1 
ATOM   1270 C  CE1 . HIS A 1 164 ? -9.589  6.169   22.740  1.00 25.46 ? 164 HIS A CE1 1 
ATOM   1271 N  NE2 . HIS A 1 164 ? -8.618  5.308   23.050  1.00 28.85 ? 164 HIS A NE2 1 
ATOM   1272 N  N   . VAL A 1 165 ? -6.406  7.746   16.945  1.00 13.29 ? 165 VAL A N   1 
ATOM   1273 C  CA  . VAL A 1 165 ? -5.563  8.490   16.014  1.00 13.11 ? 165 VAL A CA  1 
ATOM   1274 C  C   . VAL A 1 165 ? -6.198  8.411   14.626  1.00 12.17 ? 165 VAL A C   1 
ATOM   1275 O  O   . VAL A 1 165 ? -5.509  8.303   13.628  1.00 11.72 ? 165 VAL A O   1 
ATOM   1276 C  CB  . VAL A 1 165 ? -4.084  8.012   16.005  1.00 13.65 ? 165 VAL A CB  1 
ATOM   1277 C  CG1 . VAL A 1 165 ? -3.339  8.311   17.310  1.00 14.69 ? 165 VAL A CG1 1 
ATOM   1278 C  CG2 . VAL A 1 165 ? -3.932  6.539   15.637  1.00 13.07 ? 165 VAL A CG2 1 
ATOM   1279 N  N   . LYS A 1 166 ? -7.529  8.442   14.585  1.00 13.87 ? 166 LYS A N   1 
ATOM   1280 C  CA  . LYS A 1 166 ? -8.325  8.222   13.383  1.00 14.12 ? 166 LYS A CA  1 
ATOM   1281 C  C   . LYS A 1 166 ? -8.014  9.237   12.277  1.00 14.71 ? 166 LYS A C   1 
ATOM   1282 O  O   . LYS A 1 166 ? -8.032  8.883   11.084  1.00 12.92 ? 166 LYS A O   1 
ATOM   1283 C  CB  . LYS A 1 166 ? -9.813  8.223   13.741  1.00 14.68 ? 166 LYS A CB  1 
ATOM   1284 C  CG  . LYS A 1 166 ? -10.268 7.019   14.569  1.00 15.48 ? 166 LYS A CG  1 
ATOM   1285 C  CD  . LYS A 1 166 ? -11.787 6.867   14.662  1.00 15.31 ? 166 LYS A CD  1 
ATOM   1286 C  CE  . LYS A 1 166 ? -12.412 6.537   13.321  1.00 15.75 ? 166 LYS A CE  1 
ATOM   1287 N  NZ  . LYS A 1 166 ? -12.109 5.144   12.893  1.00 15.31 ? 166 LYS A NZ  1 
ATOM   1288 N  N   . TYR A 1 167 ? -7.746  10.497  12.667  1.00 15.25 ? 167 TYR A N   1 
ATOM   1289 C  CA  . TYR A 1 167 ? -7.537  11.580  11.709  1.00 15.95 ? 167 TYR A CA  1 
ATOM   1290 C  C   . TYR A 1 167 ? -6.126  12.146  11.747  1.00 13.67 ? 167 TYR A C   1 
ATOM   1291 O  O   . TYR A 1 167 ? -5.438  12.074  12.760  1.00 11.79 ? 167 TYR A O   1 
ATOM   1292 C  CB  . TYR A 1 167 ? -8.557  12.701  11.895  1.00 18.44 ? 167 TYR A CB  1 
ATOM   1293 C  CG  . TYR A 1 167 ? -9.945  12.140  11.989  1.00 22.32 ? 167 TYR A CG  1 
ATOM   1294 C  CD1 . TYR A 1 167 ? -10.620 11.669  10.872  1.00 24.53 ? 167 TYR A CD1 1 
ATOM   1295 C  CD2 . TYR A 1 167 ? -10.549 12.018  13.224  1.00 23.96 ? 167 TYR A CD2 1 
ATOM   1296 C  CE1 . TYR A 1 167 ? -11.890 11.120  10.987  1.00 28.12 ? 167 TYR A CE1 1 
ATOM   1297 C  CE2 . TYR A 1 167 ? -11.814 11.481  13.354  1.00 27.70 ? 167 TYR A CE2 1 
ATOM   1298 C  CZ  . TYR A 1 167 ? -12.484 11.033  12.234  1.00 29.54 ? 167 TYR A CZ  1 
ATOM   1299 O  OH  . TYR A 1 167 ? -13.730 10.510  12.427  1.00 37.30 ? 167 TYR A OH  1 
ATOM   1300 N  N   . LYS A 1 168 ? -5.728  12.705  10.601  1.00 12.35 ? 168 LYS A N   1 
ATOM   1301 C  CA  . LYS A 1 168 ? -4.430  13.352  10.460  1.00 11.96 ? 168 LYS A CA  1 
ATOM   1302 C  C   . LYS A 1 168 ? -4.225  14.384  11.567  1.00 10.79 ? 168 LYS A C   1 
ATOM   1303 O  O   . LYS A 1 168 ? -5.098  15.202  11.856  1.00 9.84  ? 168 LYS A O   1 
ATOM   1304 C  CB  . LYS A 1 168 ? -4.248  13.980  9.075   1.00 12.82 ? 168 LYS A CB  1 
ATOM   1305 C  CG  . LYS A 1 168 ? -2.901  14.666  8.873   1.00 13.52 ? 168 LYS A CG  1 
ATOM   1306 C  CD  . LYS A 1 168 ? -2.851  15.508  7.617   1.00 15.37 ? 168 LYS A CD  1 
ATOM   1307 C  CE  . LYS A 1 168 ? -1.452  15.909  7.182   1.00 17.32 ? 168 LYS A CE  1 
ATOM   1308 N  NZ  . LYS A 1 168 ? -1.436  16.088  5.710   1.00 19.68 ? 168 LYS A NZ  1 
ATOM   1309 N  N   . GLY A 1 169 ? -3.052  14.300  12.192  1.00 10.28 ? 169 GLY A N   1 
ATOM   1310 C  CA  . GLY A 1 169 ? -2.662  15.219  13.243  1.00 10.43 ? 169 GLY A CA  1 
ATOM   1311 C  C   . GLY A 1 169 ? -3.086  14.726  14.624  1.00 10.67 ? 169 GLY A C   1 
ATOM   1312 O  O   . GLY A 1 169 ? -2.688  15.333  15.602  1.00 10.08 ? 169 GLY A O   1 
ATOM   1313 N  N   . GLN A 1 170 ? -3.887  13.641  14.700  1.00 10.79 ? 170 GLN A N   1 
ATOM   1314 C  CA  . GLN A 1 170 ? -4.313  13.142  16.004  1.00 12.82 ? 170 GLN A CA  1 
ATOM   1315 C  C   . GLN A 1 170 ? -3.206  12.279  16.599  1.00 12.28 ? 170 GLN A C   1 
ATOM   1316 O  O   . GLN A 1 170 ? -2.480  11.632  15.853  1.00 11.44 ? 170 GLN A O   1 
ATOM   1317 C  CB  . GLN A 1 170 ? -5.629  12.375  15.904  1.00 13.63 ? 170 GLN A CB  1 
ATOM   1318 C  CG  . GLN A 1 170 ? -6.765  13.257  15.424  1.00 15.37 ? 170 GLN A CG  1 
ATOM   1319 C  CD  . GLN A 1 170 ? -8.098  12.658  15.774  1.00 17.55 ? 170 GLN A CD  1 
ATOM   1320 O  OE1 . GLN A 1 170 ? -8.344  11.464  15.561  1.00 16.51 ? 170 GLN A OE1 1 
ATOM   1321 N  NE2 . GLN A 1 170 ? -8.963  13.508  16.313  1.00 18.28 ? 170 GLN A NE2 1 
ATOM   1322 N  N   . GLU A 1 171 ? -3.069  12.304  17.935  1.00 13.04 ? 171 GLU A N   1 
ATOM   1323 C  CA  . GLU A 1 171 ? -1.923  11.706  18.618  1.00 14.14 ? 171 GLU A CA  1 
ATOM   1324 C  C   . GLU A 1 171 ? -2.395  10.965  19.873  1.00 14.62 ? 171 GLU A C   1 
ATOM   1325 O  O   . GLU A 1 171 ? -3.391  11.350  20.490  1.00 14.55 ? 171 GLU A O   1 
ATOM   1326 C  CB  . GLU A 1 171 ? -0.914  12.776  19.063  1.00 15.33 ? 171 GLU A CB  1 
ATOM   1327 C  CG  . GLU A 1 171 ? -0.181  13.471  17.923  1.00 16.41 ? 171 GLU A CG  1 
ATOM   1328 C  CD  . GLU A 1 171 ? 0.772   14.584  18.335  1.00 18.92 ? 171 GLU A CD  1 
ATOM   1329 O  OE1 . GLU A 1 171 ? 1.473   15.113  17.451  1.00 20.34 ? 171 GLU A OE1 1 
ATOM   1330 O  OE2 . GLU A 1 171 ? 0.831   14.910  19.533  1.00 20.44 ? 171 GLU A OE2 1 
ATOM   1331 N  N   . ALA A 1 172 ? -1.634  9.936   20.276  1.00 13.83 ? 172 ALA A N   1 
ATOM   1332 C  CA  . ALA A 1 172 ? -1.942  9.181   21.481  1.00 14.61 ? 172 ALA A CA  1 
ATOM   1333 C  C   . ALA A 1 172 ? -0.652  8.596   22.048  1.00 14.68 ? 172 ALA A C   1 
ATOM   1334 O  O   . ALA A 1 172 ? 0.345   8.468   21.348  1.00 15.39 ? 172 ALA A O   1 
ATOM   1335 C  CB  . ALA A 1 172 ? -2.946  8.097   21.168  1.00 14.37 ? 172 ALA A CB  1 
ATOM   1336 N  N   . PHE A 1 173 ? -0.676  8.261   23.332  1.00 14.56 ? 173 PHE A N   1 
ATOM   1337 C  CA  . PHE A 1 173 ? 0.488   7.704   23.995  1.00 16.64 ? 173 PHE A CA  1 
ATOM   1338 C  C   . PHE A 1 173 ? 0.365   6.193   24.068  1.00 14.93 ? 173 PHE A C   1 
ATOM   1339 O  O   . PHE A 1 173 ? -0.675  5.681   24.439  1.00 15.41 ? 173 PHE A O   1 
ATOM   1340 C  CB  . PHE A 1 173 ? 0.601   8.250   25.416  1.00 17.41 ? 173 PHE A CB  1 
ATOM   1341 C  CG  . PHE A 1 173 ? 1.108   9.662   25.407  1.00 19.38 ? 173 PHE A CG  1 
ATOM   1342 C  CD1 . PHE A 1 173 ? 2.317   9.966   24.790  1.00 20.63 ? 173 PHE A CD1 1 
ATOM   1343 C  CD2 . PHE A 1 173 ? 0.383   10.675  26.011  1.00 21.12 ? 173 PHE A CD2 1 
ATOM   1344 C  CE1 . PHE A 1 173 ? 2.793   11.267  24.764  1.00 22.52 ? 173 PHE A CE1 1 
ATOM   1345 C  CE2 . PHE A 1 173 ? 0.853   11.979  25.978  1.00 24.42 ? 173 PHE A CE2 1 
ATOM   1346 C  CZ  . PHE A 1 173 ? 2.056   12.268  25.356  1.00 24.77 ? 173 PHE A CZ  1 
ATOM   1347 N  N   . VAL A 1 174 ? 1.439   5.496   23.720  1.00 13.49 ? 174 VAL A N   1 
ATOM   1348 C  CA  . VAL A 1 174 ? 1.406   4.051   23.857  1.00 13.45 ? 174 VAL A CA  1 
ATOM   1349 C  C   . VAL A 1 174 ? 2.458   3.697   24.904  1.00 12.85 ? 174 VAL A C   1 
ATOM   1350 O  O   . VAL A 1 174 ? 3.599   4.159   24.794  1.00 12.47 ? 174 VAL A O   1 
ATOM   1351 C  CB  . VAL A 1 174 ? 1.661   3.368   22.493  1.00 13.71 ? 174 VAL A CB  1 
ATOM   1352 C  CG1 . VAL A 1 174 ? 1.769   1.850   22.585  1.00 12.63 ? 174 VAL A CG1 1 
ATOM   1353 C  CG2 . VAL A 1 174 ? 0.643   3.797   21.433  1.00 13.64 ? 174 VAL A CG2 1 
ATOM   1354 N  N   . PRO A 1 175 ? 2.119   2.895   25.946  1.00 12.72 ? 175 PRO A N   1 
ATOM   1355 C  CA  . PRO A 1 175 ? 3.121   2.463   26.923  1.00 11.99 ? 175 PRO A CA  1 
ATOM   1356 C  C   . PRO A 1 175 ? 4.121   1.544   26.215  1.00 11.79 ? 175 PRO A C   1 
ATOM   1357 O  O   . PRO A 1 175 ? 3.778   0.814   25.267  1.00 10.13 ? 175 PRO A O   1 
ATOM   1358 C  CB  . PRO A 1 175 ? 2.308   1.714   27.995  1.00 12.95 ? 175 PRO A CB  1 
ATOM   1359 C  CG  . PRO A 1 175 ? 0.855   2.155   27.756  1.00 13.39 ? 175 PRO A CG  1 
ATOM   1360 C  CD  . PRO A 1 175 ? 0.779   2.357   26.249  1.00 12.78 ? 175 PRO A CD  1 
ATOM   1361 N  N   . GLY A 1 176 ? 5.380   1.640   26.657  1.00 11.42 ? 176 GLY A N   1 
ATOM   1362 C  CA  . GLY A 1 176 ? 6.437   0.855   26.047  1.00 10.48 ? 176 GLY A CA  1 
ATOM   1363 C  C   . GLY A 1 176 ? 6.096   -0.629  26.134  1.00 10.66 ? 176 GLY A C   1 
ATOM   1364 O  O   . GLY A 1 176 ? 5.440   -1.057  27.074  1.00 9.91  ? 176 GLY A O   1 
ATOM   1365 N  N   . PHE A 1 177 ? 6.541   -1.377  25.124  1.00 10.85 ? 177 PHE A N   1 
ATOM   1366 C  CA  . PHE A 1 177 ? 6.483   -2.826  25.070  1.00 10.99 ? 177 PHE A CA  1 
ATOM   1367 C  C   . PHE A 1 177 ? 7.698   -3.264  24.267  1.00 10.91 ? 177 PHE A C   1 
ATOM   1368 O  O   . PHE A 1 177 ? 8.448   -2.422  23.782  1.00 10.63 ? 177 PHE A O   1 
ATOM   1369 C  CB  . PHE A 1 177 ? 5.204   -3.315  24.379  1.00 10.75 ? 177 PHE A CB  1 
ATOM   1370 C  CG  . PHE A 1 177 ? 5.053   -2.868  22.937  1.00 10.80 ? 177 PHE A CG  1 
ATOM   1371 C  CD1 . PHE A 1 177 ? 4.606   -1.591  22.638  1.00 10.42 ? 177 PHE A CD1 1 
ATOM   1372 C  CD2 . PHE A 1 177 ? 5.339   -3.722  21.879  1.00 10.40 ? 177 PHE A CD2 1 
ATOM   1373 C  CE1 . PHE A 1 177 ? 4.431   -1.185  21.317  1.00 11.08 ? 177 PHE A CE1 1 
ATOM   1374 C  CE2 . PHE A 1 177 ? 5.162   -3.313  20.561  1.00 10.91 ? 177 PHE A CE2 1 
ATOM   1375 C  CZ  . PHE A 1 177 ? 4.708   -2.043  20.277  1.00 10.41 ? 177 PHE A CZ  1 
ATOM   1376 N  N   . ASN A 1 178 ? 7.859   -4.580  24.129  1.00 11.44 ? 178 ASN A N   1 
ATOM   1377 C  CA  . ASN A 1 178 ? 9.040   -5.141  23.500  1.00 12.04 ? 178 ASN A CA  1 
ATOM   1378 C  C   . ASN A 1 178 ? 8.905   -5.101  21.979  1.00 11.32 ? 178 ASN A C   1 
ATOM   1379 O  O   . ASN A 1 178 ? 8.168   -5.898  21.393  1.00 11.41 ? 178 ASN A O   1 
ATOM   1380 C  CB  . ASN A 1 178 ? 9.366   -6.526  24.051  1.00 12.37 ? 178 ASN A CB  1 
ATOM   1381 C  CG  . ASN A 1 178 ? 10.704  -7.030  23.563  1.00 13.36 ? 178 ASN A CG  1 
ATOM   1382 O  OD1 . ASN A 1 178 ? 11.451  -6.301  22.900  1.00 12.79 ? 178 ASN A OD1 1 
ATOM   1383 N  ND2 . ASN A 1 178 ? 11.010  -8.276  23.898  1.00 13.29 ? 178 ASN A ND2 1 
ATOM   1384 N  N   . ILE A 1 179 ? 9.643   -4.177  21.354  1.00 10.57 ? 179 ILE A N   1 
ATOM   1385 C  CA  . ILE A 1 179 ? 9.557   -4.027  19.909  1.00 12.06 ? 179 ILE A CA  1 
ATOM   1386 C  C   . ILE A 1 179 ? 10.151  -5.266  19.243  1.00 12.49 ? 179 ILE A C   1 
ATOM   1387 O  O   . ILE A 1 179 ? 9.854   -5.560  18.093  1.00 13.01 ? 179 ILE A O   1 
ATOM   1388 C  CB  . ILE A 1 179 ? 10.277  -2.762  19.413  1.00 11.57 ? 179 ILE A CB  1 
ATOM   1389 C  CG1 . ILE A 1 179 ? 9.811   -1.481  20.125  1.00 12.23 ? 179 ILE A CG1 1 
ATOM   1390 C  CG2 . ILE A 1 179 ? 10.220  -2.688  17.886  1.00 12.39 ? 179 ILE A CG2 1 
ATOM   1391 C  CD1 . ILE A 1 179 ? 8.321   -1.140  20.033  1.00 12.06 ? 179 ILE A CD1 1 
ATOM   1392 N  N   . GLU A 1 180 ? 11.007  -5.983  19.964  1.00 13.04 ? 180 GLU A N   1 
ATOM   1393 C  CA  . GLU A 1 180 ? 11.545  -7.220  19.426  1.00 14.75 ? 180 GLU A CA  1 
ATOM   1394 C  C   . GLU A 1 180 ? 10.422  -8.188  19.073  1.00 13.79 ? 180 GLU A C   1 
ATOM   1395 O  O   . GLU A 1 180 ? 10.558  -8.945  18.128  1.00 13.77 ? 180 GLU A O   1 
ATOM   1396 C  CB  . GLU A 1 180 ? 12.541  -7.861  20.389  1.00 15.62 ? 180 GLU A CB  1 
ATOM   1397 C  CG  . GLU A 1 180 ? 13.958  -7.710  19.903  1.00 19.96 ? 180 GLU A CG  1 
ATOM   1398 C  CD  . GLU A 1 180 ? 14.947  -8.668  20.541  1.00 20.39 ? 180 GLU A CD  1 
ATOM   1399 O  OE1 . GLU A 1 180 ? 15.213  -9.710  19.928  1.00 20.21 ? 180 GLU A OE1 1 
ATOM   1400 O  OE2 . GLU A 1 180 ? 15.427  -8.364  21.650  1.00 21.80 ? 180 GLU A OE2 1 
ATOM   1401 N  N   . GLU A 1 181 ? 9.315   -8.144  19.827  1.00 14.04 ? 181 GLU A N   1 
ATOM   1402 C  CA  . GLU A 1 181 ? 8.193   -9.054  19.607  1.00 14.68 ? 181 GLU A CA  1 
ATOM   1403 C  C   . GLU A 1 181 ? 7.516   -8.779  18.251  1.00 13.81 ? 181 GLU A C   1 
ATOM   1404 O  O   . GLU A 1 181 ? 6.700   -9.566  17.786  1.00 12.72 ? 181 GLU A O   1 
ATOM   1405 C  CB  . GLU A 1 181 ? 7.184   -8.956  20.755  1.00 16.08 ? 181 GLU A CB  1 
ATOM   1406 C  CG  . GLU A 1 181 ? 7.738   -9.261  22.147  1.00 21.54 ? 181 GLU A CG  1 
ATOM   1407 C  CD  . GLU A 1 181 ? 6.789   -9.014  23.332  1.00 25.91 ? 181 GLU A CD  1 
ATOM   1408 O  OE1 . GLU A 1 181 ? 5.767   -8.280  23.182  1.00 29.48 ? 181 GLU A OE1 1 
ATOM   1409 O  OE2 . GLU A 1 181 ? 7.061   -9.550  24.420  1.00 29.66 ? 181 GLU A OE2 1 
ATOM   1410 N  N   . LEU A 1 182 ? 7.840   -7.655  17.606  1.00 13.21 ? 182 LEU A N   1 
ATOM   1411 C  CA  . LEU A 1 182 ? 7.255   -7.365  16.300  1.00 12.10 ? 182 LEU A CA  1 
ATOM   1412 C  C   . LEU A 1 182 ? 8.103   -7.947  15.168  1.00 12.50 ? 182 LEU A C   1 
ATOM   1413 O  O   . LEU A 1 182 ? 7.721   -7.850  13.999  1.00 13.07 ? 182 LEU A O   1 
ATOM   1414 C  CB  . LEU A 1 182 ? 7.142   -5.844  16.131  1.00 11.40 ? 182 LEU A CB  1 
ATOM   1415 C  CG  . LEU A 1 182 ? 6.276   -5.106  17.153  1.00 10.95 ? 182 LEU A CG  1 
ATOM   1416 C  CD1 . LEU A 1 182 ? 6.253   -3.612  16.798  1.00 11.17 ? 182 LEU A CD1 1 
ATOM   1417 C  CD2 . LEU A 1 182 ? 4.867   -5.686  17.201  1.00 10.18 ? 182 LEU A CD2 1 
ATOM   1418 N  N   . LEU A 1 183 ? 9.295   -8.458  15.500  1.00 12.45 ? 183 LEU A N   1 
ATOM   1419 C  CA  . LEU A 1 183 ? 10.190  -8.987  14.487  1.00 12.08 ? 183 LEU A CA  1 
ATOM   1420 C  C   . LEU A 1 183 ? 9.892   -10.472 14.314  1.00 12.83 ? 183 LEU A C   1 
ATOM   1421 O  O   . LEU A 1 183 ? 9.334   -11.105 15.206  1.00 10.85 ? 183 LEU A O   1 
ATOM   1422 C  CB  . LEU A 1 183 ? 11.640  -8.788  14.937  1.00 12.62 ? 183 LEU A CB  1 
ATOM   1423 C  CG  . LEU A 1 183 ? 12.165  -7.346  15.057  1.00 13.30 ? 183 LEU A CG  1 
ATOM   1424 C  CD1 . LEU A 1 183 ? 13.668  -7.349  15.313  1.00 13.95 ? 183 LEU A CD1 1 
ATOM   1425 C  CD2 . LEU A 1 183 ? 11.856  -6.508  13.824  1.00 13.30 ? 183 LEU A CD2 1 
ATOM   1426 N  N   . PRO A 1 184 ? 10.244  -11.057 13.150  1.00 13.47 ? 184 PRO A N   1 
ATOM   1427 C  CA  . PRO A 1 184 ? 9.961   -12.463 12.887  1.00 16.13 ? 184 PRO A CA  1 
ATOM   1428 C  C   . PRO A 1 184 ? 10.910  -13.432 13.568  1.00 20.59 ? 184 PRO A C   1 
ATOM   1429 O  O   . PRO A 1 184 ? 11.835  -13.039 14.300  1.00 19.95 ? 184 PRO A O   1 
ATOM   1430 C  CB  . PRO A 1 184 ? 10.258  -12.638 11.398  1.00 15.17 ? 184 PRO A CB  1 
ATOM   1431 C  CG  . PRO A 1 184 ? 11.187  -11.498 11.048  1.00 14.93 ? 184 PRO A CG  1 
ATOM   1432 C  CD  . PRO A 1 184 ? 10.877  -10.376 12.014  1.00 13.73 ? 184 PRO A CD  1 
ATOM   1433 N  N   . GLU A 1 185 ? 10.624  -14.697 13.247  1.00 25.62 ? 185 GLU A N   1 
ATOM   1434 C  CA  . GLU A 1 185 ? 11.494  -15.853 13.354  1.00 30.31 ? 185 GLU A CA  1 
ATOM   1435 C  C   . GLU A 1 185 ? 12.815  -15.616 12.617  1.00 31.45 ? 185 GLU A C   1 
ATOM   1436 O  O   . GLU A 1 185 ? 12.853  -15.134 11.475  1.00 31.46 ? 185 GLU A O   1 
ATOM   1437 C  CB  . GLU A 1 185 ? 10.751  -17.041 12.744  1.00 32.09 ? 185 GLU A CB  1 
ATOM   1438 C  CG  . GLU A 1 185 ? 11.494  -18.349 12.921  1.00 39.75 ? 185 GLU A CG  1 
ATOM   1439 C  CD  . GLU A 1 185 ? 10.718  -19.593 12.529  1.00 42.03 ? 185 GLU A CD  1 
ATOM   1440 O  OE1 . GLU A 1 185 ? 10.252  -19.663 11.366  1.00 42.62 ? 185 GLU A OE1 1 
ATOM   1441 O  OE2 . GLU A 1 185 ? 10.591  -20.492 13.394  1.00 43.49 ? 185 GLU A OE2 1 
ATOM   1442 N  N   . ARG A 1 186 ? 13.910  -15.989 13.282  1.00 29.62 ? 186 ARG A N   1 
ATOM   1443 C  CA  . ARG A 1 186 ? 15.171  -16.195 12.593  1.00 30.33 ? 186 ARG A CA  1 
ATOM   1444 C  C   . ARG A 1 186 ? 15.540  -14.924 11.832  1.00 27.45 ? 186 ARG A C   1 
ATOM   1445 O  O   . ARG A 1 186 ? 15.724  -14.946 10.609  1.00 30.63 ? 186 ARG A O   1 
ATOM   1446 C  CB  . ARG A 1 186 ? 15.095  -17.431 11.688  1.00 36.68 ? 186 ARG A CB  1 
ATOM   1447 N  N   . THR A 1 187 ? 15.693  -13.837 12.588  1.00 18.63 ? 187 THR A N   1 
ATOM   1448 C  CA  . THR A 1 187 ? 16.073  -12.560 12.023  1.00 16.20 ? 187 THR A CA  1 
ATOM   1449 C  C   . THR A 1 187 ? 17.400  -12.687 11.290  1.00 15.25 ? 187 THR A C   1 
ATOM   1450 O  O   . THR A 1 187 ? 17.790  -11.742 10.615  1.00 14.75 ? 187 THR A O   1 
ATOM   1451 C  CB  . THR A 1 187 ? 16.180  -11.500 13.129  1.00 15.30 ? 187 THR A CB  1 
ATOM   1452 O  OG1 . THR A 1 187 ? 16.928  -12.051 14.210  1.00 12.81 ? 187 THR A OG1 1 
ATOM   1453 C  CG2 . THR A 1 187 ? 14.821  -11.083 13.635  1.00 15.76 ? 187 THR A CG2 1 
ATOM   1454 N  N   . ALA A 1 188 ? 18.111  -13.824 11.460  1.00 14.65 ? 188 ALA A N   1 
ATOM   1455 C  CA  . ALA A 1 188 ? 19.468  -13.936 10.933  1.00 14.24 ? 188 ALA A CA  1 
ATOM   1456 C  C   . ALA A 1 188 ? 19.428  -13.929 9.406   1.00 13.39 ? 188 ALA A C   1 
ATOM   1457 O  O   . ALA A 1 188 ? 20.423  -13.653 8.747   1.00 13.18 ? 188 ALA A O   1 
ATOM   1458 C  CB  . ALA A 1 188 ? 20.172  -15.183 11.440  1.00 13.91 ? 188 ALA A CB  1 
ATOM   1459 N  N   . GLU A 1 189 ? 18.253  -14.242 8.866   1.00 13.60 ? 189 GLU A N   1 
ATOM   1460 C  CA  . GLU A 1 189 ? 18.036  -14.388 7.447   1.00 14.18 ? 189 GLU A CA  1 
ATOM   1461 C  C   . GLU A 1 189 ? 17.360  -13.126 6.926   1.00 12.24 ? 189 GLU A C   1 
ATOM   1462 O  O   . GLU A 1 189 ? 16.230  -12.834 7.313   1.00 11.29 ? 189 GLU A O   1 
ATOM   1463 C  CB  . GLU A 1 189 ? 17.181  -15.632 7.213   1.00 17.19 ? 189 GLU A CB  1 
ATOM   1464 C  CG  . GLU A 1 189 ? 17.832  -16.875 7.782   1.00 22.52 ? 189 GLU A CG  1 
ATOM   1465 C  CD  . GLU A 1 189 ? 17.329  -18.120 7.094   1.00 26.13 ? 189 GLU A CD  1 
ATOM   1466 O  OE1 . GLU A 1 189 ? 16.115  -18.240 6.950   1.00 29.53 ? 189 GLU A OE1 1 
ATOM   1467 O  OE2 . GLU A 1 189 ? 18.159  -18.944 6.678   1.00 37.31 ? 189 GLU A OE2 1 
ATOM   1468 N  N   . TYR A 1 190 ? 18.054  -12.382 6.052   1.00 10.97 ? 190 TYR A N   1 
ATOM   1469 C  CA  . TYR A 1 190 ? 17.464  -11.150 5.543   1.00 10.16 ? 190 TYR A CA  1 
ATOM   1470 C  C   . TYR A 1 190 ? 18.050  -10.798 4.182   1.00 10.83 ? 190 TYR A C   1 
ATOM   1471 O  O   . TYR A 1 190 ? 19.087  -11.330 3.790   1.00 10.63 ? 190 TYR A O   1 
ATOM   1472 C  CB  . TYR A 1 190 ? 17.753  -9.984  6.489   1.00 10.02 ? 190 TYR A CB  1 
ATOM   1473 C  CG  . TYR A 1 190 ? 19.218  -9.800  6.833   1.00 9.72  ? 190 TYR A CG  1 
ATOM   1474 C  CD1 . TYR A 1 190 ? 20.083  -9.097  6.007   1.00 9.47  ? 190 TYR A CD1 1 
ATOM   1475 C  CD2 . TYR A 1 190 ? 19.726  -10.310 8.011   1.00 9.48  ? 190 TYR A CD2 1 
ATOM   1476 C  CE1 . TYR A 1 190 ? 21.420  -8.905  6.332   1.00 10.02 ? 190 TYR A CE1 1 
ATOM   1477 C  CE2 . TYR A 1 190 ? 21.052  -10.113 8.362   1.00 10.28 ? 190 TYR A CE2 1 
ATOM   1478 C  CZ  . TYR A 1 190 ? 21.909  -9.427  7.517   1.00 9.93  ? 190 TYR A CZ  1 
ATOM   1479 O  OH  . TYR A 1 190 ? 23.213  -9.267  7.890   1.00 10.34 ? 190 TYR A OH  1 
ATOM   1480 N  N   . TYR A 1 191 ? 17.366  -9.868  3.499   1.00 10.98 ? 191 TYR A N   1 
ATOM   1481 C  CA  . TYR A 1 191 ? 17.826  -9.188  2.300   1.00 11.02 ? 191 TYR A CA  1 
ATOM   1482 C  C   . TYR A 1 191 ? 18.389  -7.823  2.695   1.00 11.51 ? 191 TYR A C   1 
ATOM   1483 O  O   . TYR A 1 191 ? 17.843  -7.163  3.585   1.00 10.39 ? 191 TYR A O   1 
ATOM   1484 C  CB  . TYR A 1 191 ? 16.651  -8.976  1.344   1.00 11.52 ? 191 TYR A CB  1 
ATOM   1485 C  CG  . TYR A 1 191 ? 15.770  -10.173 1.055   1.00 12.09 ? 191 TYR A CG  1 
ATOM   1486 C  CD1 . TYR A 1 191 ? 14.635  -10.420 1.822   1.00 12.34 ? 191 TYR A CD1 1 
ATOM   1487 C  CD2 . TYR A 1 191 ? 15.999  -10.985 -0.049  1.00 11.91 ? 191 TYR A CD2 1 
ATOM   1488 C  CE1 . TYR A 1 191 ? 13.778  -11.477 1.529   1.00 13.51 ? 191 TYR A CE1 1 
ATOM   1489 C  CE2 . TYR A 1 191 ? 15.160  -12.051 -0.347  1.00 12.82 ? 191 TYR A CE2 1 
ATOM   1490 C  CZ  . TYR A 1 191 ? 14.052  -12.300 0.451   1.00 13.11 ? 191 TYR A CZ  1 
ATOM   1491 O  OH  . TYR A 1 191 ? 13.204  -13.322 0.165   1.00 16.15 ? 191 TYR A OH  1 
ATOM   1492 N  N   . ARG A 1 192 ? 19.480  -7.425  2.013   1.00 11.18 ? 192 ARG A N   1 
ATOM   1493 C  CA  . ARG A 1 192 ? 20.234  -6.210  2.293   1.00 11.03 ? 192 ARG A CA  1 
ATOM   1494 C  C   . ARG A 1 192 ? 20.580  -5.493  0.981   1.00 10.85 ? 192 ARG A C   1 
ATOM   1495 O  O   . ARG A 1 192 ? 21.144  -6.096  0.072   1.00 9.89  ? 192 ARG A O   1 
ATOM   1496 C  CB  . ARG A 1 192 ? 21.485  -6.573  3.110   1.00 11.21 ? 192 ARG A CB  1 
ATOM   1497 C  CG  . ARG A 1 192 ? 22.494  -5.442  3.227   1.00 11.25 ? 192 ARG A CG  1 
ATOM   1498 C  CD  . ARG A 1 192 ? 22.026  -4.255  4.051   1.00 11.49 ? 192 ARG A CD  1 
ATOM   1499 N  NE  . ARG A 1 192 ? 21.448  -4.693  5.310   1.00 11.85 ? 192 ARG A NE  1 
ATOM   1500 C  CZ  . ARG A 1 192 ? 22.154  -5.169  6.331   1.00 12.54 ? 192 ARG A CZ  1 
ATOM   1501 N  NH1 . ARG A 1 192 ? 21.560  -5.552  7.452   1.00 11.87 ? 192 ARG A NH1 1 
ATOM   1502 N  NH2 . ARG A 1 192 ? 23.466  -5.242  6.225   1.00 14.05 ? 192 ARG A NH2 1 
ATOM   1503 N  N   . TYR A 1 193 ? 20.249  -4.190  0.892   1.00 10.40 ? 193 TYR A N   1 
ATOM   1504 C  CA  . TYR A 1 193 ? 20.392  -3.453  -0.355  1.00 10.43 ? 193 TYR A CA  1 
ATOM   1505 C  C   . TYR A 1 193 ? 20.369  -1.950  -0.077  1.00 10.80 ? 193 TYR A C   1 
ATOM   1506 O  O   . TYR A 1 193 ? 19.914  -1.519  0.996   1.00 10.61 ? 193 TYR A O   1 
ATOM   1507 C  CB  . TYR A 1 193 ? 19.332  -3.928  -1.363  1.00 10.00 ? 193 TYR A CB  1 
ATOM   1508 C  CG  . TYR A 1 193 ? 17.981  -3.258  -1.263  1.00 9.15  ? 193 TYR A CG  1 
ATOM   1509 C  CD1 . TYR A 1 193 ? 17.722  -2.089  -1.962  1.00 9.28  ? 193 TYR A CD1 1 
ATOM   1510 C  CD2 . TYR A 1 193 ? 16.958  -3.774  -0.491  1.00 9.28  ? 193 TYR A CD2 1 
ATOM   1511 C  CE1 . TYR A 1 193 ? 16.496  -1.444  -1.896  1.00 8.42  ? 193 TYR A CE1 1 
ATOM   1512 C  CE2 . TYR A 1 193 ? 15.722  -3.127  -0.385  1.00 8.44  ? 193 TYR A CE2 1 
ATOM   1513 C  CZ  . TYR A 1 193 ? 15.491  -1.960  -1.094  1.00 8.36  ? 193 TYR A CZ  1 
ATOM   1514 O  OH  . TYR A 1 193 ? 14.276  -1.332  -1.054  1.00 7.63  ? 193 TYR A OH  1 
ATOM   1515 N  N   A ARG A 1 194 ? 20.893  -1.152  -1.020  0.50 11.06 ? 194 ARG A N   1 
ATOM   1516 N  N   B ARG A 1 194 ? 20.850  -1.164  -1.048  0.50 10.99 ? 194 ARG A N   1 
ATOM   1517 C  CA  A ARG A 1 194 ? 20.826  0.296   -0.882  0.50 11.48 ? 194 ARG A CA  1 
ATOM   1518 C  CA  B ARG A 1 194 ? 20.832  0.285   -0.937  0.50 11.38 ? 194 ARG A CA  1 
ATOM   1519 C  C   A ARG A 1 194 ? 19.629  0.847   -1.653  0.50 11.10 ? 194 ARG A C   1 
ATOM   1520 C  C   B ARG A 1 194 ? 19.612  0.843   -1.667  0.50 11.04 ? 194 ARG A C   1 
ATOM   1521 O  O   A ARG A 1 194 ? 19.440  0.545   -2.832  0.50 11.08 ? 194 ARG A O   1 
ATOM   1522 O  O   B ARG A 1 194 ? 19.398  0.550   -2.844  0.50 11.00 ? 194 ARG A O   1 
ATOM   1523 C  CB  A ARG A 1 194 ? 22.100  1.018   -1.331  0.50 12.82 ? 194 ARG A CB  1 
ATOM   1524 C  CB  B ARG A 1 194 ? 22.053  0.902   -1.614  0.50 12.62 ? 194 ARG A CB  1 
ATOM   1525 C  CG  A ARG A 1 194 ? 23.160  0.139   -1.979  0.50 15.05 ? 194 ARG A CG  1 
ATOM   1526 C  CG  B ARG A 1 194 ? 23.388  0.594   -0.955  0.50 14.65 ? 194 ARG A CG  1 
ATOM   1527 C  CD  A ARG A 1 194 ? 24.328  -0.076  -1.028  0.50 16.74 ? 194 ARG A CD  1 
ATOM   1528 C  CD  B ARG A 1 194 ? 24.350  1.628   -1.526  0.50 16.01 ? 194 ARG A CD  1 
ATOM   1529 N  NE  A ARG A 1 194 ? 24.620  -1.491  -0.830  0.50 18.57 ? 194 ARG A NE  1 
ATOM   1530 N  NE  B ARG A 1 194 ? 25.735  1.231   -1.411  0.50 18.03 ? 194 ARG A NE  1 
ATOM   1531 C  CZ  A ARG A 1 194 ? 25.086  -1.994  0.303   0.50 19.01 ? 194 ARG A CZ  1 
ATOM   1532 N  NH1 A ARG A 1 194 ? 25.313  -3.291  0.413   0.50 19.62 ? 194 ARG A NH1 1 
ATOM   1533 N  NH2 A ARG A 1 194 ? 25.294  -1.200  1.333   0.50 19.28 ? 194 ARG A NH2 1 
ATOM   1534 N  N   . GLY A 1 195 ? 18.841  1.681   -0.973  1.00 10.21 ? 195 GLY A N   1 
ATOM   1535 C  CA  . GLY A 1 195 ? 17.692  2.317   -1.586  1.00 9.98  ? 195 GLY A CA  1 
ATOM   1536 C  C   . GLY A 1 195 ? 17.367  3.672   -0.958  1.00 9.55  ? 195 GLY A C   1 
ATOM   1537 O  O   . GLY A 1 195 ? 18.266  4.396   -0.536  1.00 9.35  ? 195 GLY A O   1 
ATOM   1538 N  N   . SER A 1 196 ? 16.059  3.979   -0.911  1.00 8.94  ? 196 SER A N   1 
ATOM   1539 C  CA  . SER A 1 196 ? 15.553  5.307   -0.607  1.00 8.53  ? 196 SER A CA  1 
ATOM   1540 C  C   . SER A 1 196 ? 14.448  5.196   0.431   1.00 9.00  ? 196 SER A C   1 
ATOM   1541 O  O   . SER A 1 196 ? 13.926  4.094   0.663   1.00 8.27  ? 196 SER A O   1 
ATOM   1542 C  CB  . SER A 1 196 ? 15.004  5.962   -1.861  1.00 7.63  ? 196 SER A CB  1 
ATOM   1543 O  OG  . SER A 1 196 ? 13.785  5.343   -2.277  1.00 6.81  ? 196 SER A OG  1 
ATOM   1544 N  N   . LEU A 1 197 ? 14.087  6.356   1.018   1.00 9.33  ? 197 LEU A N   1 
ATOM   1545 C  CA  . LEU A 1 197 ? 12.783  6.455   1.651   1.00 9.53  ? 197 LEU A CA  1 
ATOM   1546 C  C   . LEU A 1 197 ? 11.763  6.024   0.604   1.00 9.45  ? 197 LEU A C   1 
ATOM   1547 O  O   . LEU A 1 197 ? 11.896  6.427   -0.551  1.00 9.49  ? 197 LEU A O   1 
ATOM   1548 C  CB  . LEU A 1 197 ? 12.410  7.893   2.025   1.00 10.43 ? 197 LEU A CB  1 
ATOM   1549 C  CG  . LEU A 1 197 ? 13.280  8.751   2.939   1.00 11.80 ? 197 LEU A CG  1 
ATOM   1550 C  CD1 . LEU A 1 197 ? 12.426  9.506   3.937   1.00 12.24 ? 197 LEU A CD1 1 
ATOM   1551 C  CD2 . LEU A 1 197 ? 14.436  8.060   3.585   1.00 11.54 ? 197 LEU A CD2 1 
ATOM   1552 N  N   . THR A 1 198 ? 10.727  5.268   1.014   1.00 8.84  ? 198 THR A N   1 
ATOM   1553 C  CA  . THR A 1 198 ? 9.684   4.889   0.078   1.00 8.37  ? 198 THR A CA  1 
ATOM   1554 C  C   . THR A 1 198 ? 8.617   5.975   0.002   1.00 8.23  ? 198 THR A C   1 
ATOM   1555 O  O   . THR A 1 198 ? 7.672   5.865   -0.782  1.00 7.58  ? 198 THR A O   1 
ATOM   1556 C  CB  . THR A 1 198 ? 9.036   3.551   0.419   1.00 8.63  ? 198 THR A CB  1 
ATOM   1557 O  OG1 . THR A 1 198 ? 8.359   3.746   1.663   1.00 8.68  ? 198 THR A OG1 1 
ATOM   1558 C  CG2 . THR A 1 198 ? 10.020  2.396   0.465   1.00 8.62  ? 198 THR A CG2 1 
ATOM   1559 N  N   . THR A 1 199 ? 8.776   7.031   0.813   1.00 7.92  ? 199 THR A N   1 
ATOM   1560 C  CA  . THR A 1 199 ? 7.853   8.160   0.754   1.00 7.88  ? 199 THR A CA  1 
ATOM   1561 C  C   . THR A 1 199 ? 8.630   9.418   0.393   1.00 8.01  ? 199 THR A C   1 
ATOM   1562 O  O   . THR A 1 199 ? 9.843   9.471   0.591   1.00 7.70  ? 199 THR A O   1 
ATOM   1563 C  CB  . THR A 1 199 ? 7.267   8.431   2.147   1.00 7.82  ? 199 THR A CB  1 
ATOM   1564 O  OG1 . THR A 1 199 ? 8.355   8.787   3.008   1.00 7.90  ? 199 THR A OG1 1 
ATOM   1565 C  CG2 . THR A 1 199 ? 6.570   7.212   2.724   1.00 7.84  ? 199 THR A CG2 1 
ATOM   1566 N  N   . PRO A 1 200 ? 7.981   10.517  -0.068  1.00 8.39  ? 200 PRO A N   1 
ATOM   1567 C  CA  . PRO A 1 200 ? 8.684   11.790  -0.176  1.00 8.78  ? 200 PRO A CA  1 
ATOM   1568 C  C   . PRO A 1 200 ? 9.372   12.073  1.161   1.00 9.63  ? 200 PRO A C   1 
ATOM   1569 O  O   . PRO A 1 200 ? 8.839   11.785  2.233   1.00 8.90  ? 200 PRO A O   1 
ATOM   1570 C  CB  . PRO A 1 200 ? 7.547   12.793  -0.460  1.00 8.80  ? 200 PRO A CB  1 
ATOM   1571 C  CG  . PRO A 1 200 ? 6.539   11.977  -1.208  1.00 8.85  ? 200 PRO A CG  1 
ATOM   1572 C  CD  . PRO A 1 200 ? 6.589   10.609  -0.533  1.00 8.54  ? 200 PRO A CD  1 
ATOM   1573 N  N   . PRO A 1 201 ? 10.574  12.674  1.155   1.00 10.28 ? 201 PRO A N   1 
ATOM   1574 C  CA  . PRO A 1 201 ? 11.214  13.121  -0.079  1.00 10.16 ? 201 PRO A CA  1 
ATOM   1575 C  C   . PRO A 1 201 ? 12.039  12.118  -0.885  1.00 10.24 ? 201 PRO A C   1 
ATOM   1576 O  O   . PRO A 1 201 ? 12.745  12.562  -1.789  1.00 10.09 ? 201 PRO A O   1 
ATOM   1577 C  CB  . PRO A 1 201 ? 12.098  14.278  0.424   1.00 10.28 ? 201 PRO A CB  1 
ATOM   1578 C  CG  . PRO A 1 201 ? 12.494  13.855  1.833   1.00 11.47 ? 201 PRO A CG  1 
ATOM   1579 C  CD  . PRO A 1 201 ? 11.272  13.135  2.371   1.00 10.73 ? 201 PRO A CD  1 
ATOM   1580 N  N   . CYS A 1 202 ? 11.941  10.806  -0.571  1.00 10.15 ? 202 CYS A N   1 
ATOM   1581 C  CA  . CYS A 1 202 ? 12.475  9.700   -1.367  1.00 10.54 ? 202 CYS A CA  1 
ATOM   1582 C  C   . CYS A 1 202 ? 14.007  9.752   -1.463  1.00 11.59 ? 202 CYS A C   1 
ATOM   1583 O  O   . CYS A 1 202 ? 14.586  9.183   -2.388  1.00 11.18 ? 202 CYS A O   1 
ATOM   1584 C  CB  . CYS A 1 202 ? 11.926  9.682   -2.792  1.00 11.22 ? 202 CYS A CB  1 
ATOM   1585 S  SG  . CYS A 1 202 ? 10.110  9.674   -2.922  1.00 10.88 ? 202 CYS A SG  1 
ATOM   1586 N  N   . ASN A 1 203 ? 14.682  10.373  -0.481  1.00 11.99 ? 203 ASN A N   1 
ATOM   1587 C  CA  . ASN A 1 203 ? 16.139  10.473  -0.531  1.00 13.08 ? 203 ASN A CA  1 
ATOM   1588 C  C   . ASN A 1 203 ? 16.764  9.098   -0.686  1.00 12.23 ? 203 ASN A C   1 
ATOM   1589 O  O   . ASN A 1 203 ? 16.384  8.185   0.025   1.00 12.42 ? 203 ASN A O   1 
ATOM   1590 C  CB  . ASN A 1 203 ? 16.735  11.125  0.712   1.00 14.72 ? 203 ASN A CB  1 
ATOM   1591 C  CG  . ASN A 1 203 ? 16.182  12.512  0.948   1.00 19.29 ? 203 ASN A CG  1 
ATOM   1592 O  OD1 . ASN A 1 203 ? 15.850  13.221  -0.008  1.00 21.58 ? 203 ASN A OD1 1 
ATOM   1593 N  ND2 . ASN A 1 203 ? 16.105  12.915  2.205   1.00 19.97 ? 203 ASN A ND2 1 
ATOM   1594 N  N   . PRO A 1 204 ? 17.763  8.910   -1.580  1.00 12.23 ? 204 PRO A N   1 
ATOM   1595 C  CA  . PRO A 1 204 ? 18.327  7.577   -1.797  1.00 12.05 ? 204 PRO A CA  1 
ATOM   1596 C  C   . PRO A 1 204 ? 19.398  7.302   -0.735  1.00 12.43 ? 204 PRO A C   1 
ATOM   1597 O  O   . PRO A 1 204 ? 20.552  7.078   -1.046  1.00 11.97 ? 204 PRO A O   1 
ATOM   1598 C  CB  . PRO A 1 204 ? 18.907  7.731   -3.225  1.00 13.08 ? 204 PRO A CB  1 
ATOM   1599 C  CG  . PRO A 1 204 ? 19.382  9.194   -3.275  1.00 12.45 ? 204 PRO A CG  1 
ATOM   1600 C  CD  . PRO A 1 204 ? 18.307  9.934   -2.503  1.00 11.70 ? 204 PRO A CD  1 
ATOM   1601 N  N   . THR A 1 205 ? 19.013  7.319   0.543   1.00 12.46 ? 205 THR A N   1 
ATOM   1602 C  CA  . THR A 1 205 ? 20.021  7.364   1.591   1.00 12.13 ? 205 THR A CA  1 
ATOM   1603 C  C   . THR A 1 205 ? 19.743  6.310   2.661   1.00 12.42 ? 205 THR A C   1 
ATOM   1604 O  O   . THR A 1 205 ? 20.159  6.482   3.811   1.00 12.50 ? 205 THR A O   1 
ATOM   1605 C  CB  . THR A 1 205 ? 20.008  8.734   2.273   1.00 12.07 ? 205 THR A CB  1 
ATOM   1606 O  OG1 . THR A 1 205 ? 18.656  8.857   2.709   1.00 12.97 ? 205 THR A OG1 1 
ATOM   1607 C  CG2 . THR A 1 205 ? 20.330  9.877   1.337   1.00 12.55 ? 205 THR A CG2 1 
ATOM   1608 N  N   . VAL A 1 206 ? 19.075  5.208   2.268   1.00 11.97 ? 206 VAL A N   1 
ATOM   1609 C  CA  . VAL A 1 206 ? 18.630  4.203   3.222   1.00 11.15 ? 206 VAL A CA  1 
ATOM   1610 C  C   . VAL A 1 206 ? 19.391  2.916   2.942   1.00 10.74 ? 206 VAL A C   1 
ATOM   1611 O  O   . VAL A 1 206 ? 19.459  2.464   1.802   1.00 10.83 ? 206 VAL A O   1 
ATOM   1612 C  CB  . VAL A 1 206 ? 17.102  3.939   3.168   1.00 11.13 ? 206 VAL A CB  1 
ATOM   1613 C  CG1 . VAL A 1 206 ? 16.697  2.739   4.048   1.00 10.21 ? 206 VAL A CG1 1 
ATOM   1614 C  CG2 . VAL A 1 206 ? 16.293  5.161   3.563   1.00 10.83 ? 206 VAL A CG2 1 
ATOM   1615 N  N   . LEU A 1 207 ? 19.917  2.316   4.010   1.00 9.92  ? 207 LEU A N   1 
ATOM   1616 C  CA  . LEU A 1 207 ? 20.394  0.947   3.960   1.00 9.51  ? 207 LEU A CA  1 
ATOM   1617 C  C   . LEU A 1 207 ? 19.270  0.067   4.502   1.00 9.14  ? 207 LEU A C   1 
ATOM   1618 O  O   . LEU A 1 207 ? 18.878  0.197   5.666   1.00 8.29  ? 207 LEU A O   1 
ATOM   1619 C  CB  . LEU A 1 207 ? 21.685  0.817   4.779   1.00 10.32 ? 207 LEU A CB  1 
ATOM   1620 C  CG  . LEU A 1 207 ? 22.217  -0.605  4.939   1.00 12.15 ? 207 LEU A CG  1 
ATOM   1621 C  CD1 . LEU A 1 207 ? 22.788  -1.086  3.618   1.00 13.36 ? 207 LEU A CD1 1 
ATOM   1622 C  CD2 . LEU A 1 207 ? 23.278  -0.672  6.033   1.00 12.12 ? 207 LEU A CD2 1 
ATOM   1623 N  N   . TRP A 1 208 ? 18.736  -0.782  3.611   1.00 8.24  ? 208 TRP A N   1 
ATOM   1624 C  CA  . TRP A 1 208 ? 17.532  -1.568  3.854   1.00 8.45  ? 208 TRP A CA  1 
ATOM   1625 C  C   . TRP A 1 208 ? 17.908  -2.973  4.302   1.00 8.52  ? 208 TRP A C   1 
ATOM   1626 O  O   . TRP A 1 208 ? 18.767  -3.617  3.693   1.00 8.13  ? 208 TRP A O   1 
ATOM   1627 C  CB  . TRP A 1 208 ? 16.696  -1.660  2.567   1.00 8.27  ? 208 TRP A CB  1 
ATOM   1628 C  CG  . TRP A 1 208 ? 15.796  -0.479  2.328   1.00 8.16  ? 208 TRP A CG  1 
ATOM   1629 C  CD1 . TRP A 1 208 ? 15.999  0.563   1.464   1.00 7.73  ? 208 TRP A CD1 1 
ATOM   1630 C  CD2 . TRP A 1 208 ? 14.523  -0.241  2.951   1.00 8.00  ? 208 TRP A CD2 1 
ATOM   1631 N  NE1 . TRP A 1 208 ? 14.949  1.437   1.512   1.00 7.64  ? 208 TRP A NE1 1 
ATOM   1632 C  CE2 . TRP A 1 208 ? 14.032  0.982   2.424   1.00 7.79  ? 208 TRP A CE2 1 
ATOM   1633 C  CE3 . TRP A 1 208 ? 13.755  -0.944  3.894   1.00 7.91  ? 208 TRP A CE3 1 
ATOM   1634 C  CZ2 . TRP A 1 208 ? 12.813  1.524   2.822   1.00 7.68  ? 208 TRP A CZ2 1 
ATOM   1635 C  CZ3 . TRP A 1 208 ? 12.549  -0.407  4.281   1.00 7.71  ? 208 TRP A CZ3 1 
ATOM   1636 C  CH2 . TRP A 1 208 ? 12.092  0.807   3.761   1.00 7.87  ? 208 TRP A CH2 1 
ATOM   1637 N  N   . THR A 1 209 ? 17.190  -3.451  5.326   1.00 8.76  ? 209 THR A N   1 
ATOM   1638 C  CA  . THR A 1 209 ? 17.195  -4.850  5.725   1.00 8.54  ? 209 THR A CA  1 
ATOM   1639 C  C   . THR A 1 209 ? 15.735  -5.302  5.728   1.00 9.05  ? 209 THR A C   1 
ATOM   1640 O  O   . THR A 1 209 ? 14.920  -4.772  6.480   1.00 9.38  ? 209 THR A O   1 
ATOM   1641 C  CB  . THR A 1 209 ? 17.772  -5.035  7.137   1.00 8.15  ? 209 THR A CB  1 
ATOM   1642 O  OG1 . THR A 1 209 ? 19.077  -4.478  7.151   1.00 8.10  ? 209 THR A OG1 1 
ATOM   1643 C  CG2 . THR A 1 209 ? 17.898  -6.486  7.572   1.00 8.30  ? 209 THR A CG2 1 
ATOM   1644 N  N   . VAL A 1 210 ? 15.416  -6.271  4.868   1.00 8.46  ? 210 VAL A N   1 
ATOM   1645 C  CA  . VAL A 1 210 ? 14.092  -6.868  4.859   1.00 8.09  ? 210 VAL A CA  1 
ATOM   1646 C  C   . VAL A 1 210 ? 14.259  -8.297  5.367   1.00 8.25  ? 210 VAL A C   1 
ATOM   1647 O  O   . VAL A 1 210 ? 15.007  -9.084  4.784   1.00 7.12  ? 210 VAL A O   1 
ATOM   1648 C  CB  . VAL A 1 210 ? 13.520  -6.852  3.424   1.00 7.98  ? 210 VAL A CB  1 
ATOM   1649 C  CG1 . VAL A 1 210 ? 12.120  -7.429  3.342   1.00 8.18  ? 210 VAL A CG1 1 
ATOM   1650 C  CG2 . VAL A 1 210 ? 13.553  -5.453  2.818   1.00 8.41  ? 210 VAL A CG2 1 
ATOM   1651 N  N   . PHE A 1 211 ? 13.537  -8.639  6.438   1.00 8.56  ? 211 PHE A N   1 
ATOM   1652 C  CA  . PHE A 1 211 ? 13.665  -9.980  6.973   1.00 9.48  ? 211 PHE A CA  1 
ATOM   1653 C  C   . PHE A 1 211 ? 13.044  -10.974 5.993   1.00 10.26 ? 211 PHE A C   1 
ATOM   1654 O  O   . PHE A 1 211 ? 12.014  -10.687 5.370   1.00 10.44 ? 211 PHE A O   1 
ATOM   1655 C  CB  . PHE A 1 211 ? 13.139  -10.052 8.415   1.00 9.38  ? 211 PHE A CB  1 
ATOM   1656 C  CG  . PHE A 1 211 ? 13.929  -9.220  9.397   1.00 9.68  ? 211 PHE A CG  1 
ATOM   1657 C  CD1 . PHE A 1 211 ? 15.187  -9.632  9.833   1.00 10.14 ? 211 PHE A CD1 1 
ATOM   1658 C  CD2 . PHE A 1 211 ? 13.436  -8.009  9.862   1.00 9.91  ? 211 PHE A CD2 1 
ATOM   1659 C  CE1 . PHE A 1 211 ? 15.933  -8.866  10.726  1.00 10.40 ? 211 PHE A CE1 1 
ATOM   1660 C  CE2 . PHE A 1 211 ? 14.169  -7.246  10.768  1.00 10.29 ? 211 PHE A CE2 1 
ATOM   1661 C  CZ  . PHE A 1 211 ? 15.428  -7.656  11.175  1.00 10.22 ? 211 PHE A CZ  1 
ATOM   1662 N  N   . ARG A 1 212 ? 13.653  -12.162 5.902   1.00 10.80 ? 212 ARG A N   1 
ATOM   1663 C  CA  . ARG A 1 212 ? 13.149  -13.214 5.025   1.00 11.97 ? 212 ARG A CA  1 
ATOM   1664 C  C   . ARG A 1 212 ? 11.786  -13.727 5.480   1.00 10.88 ? 212 ARG A C   1 
ATOM   1665 O  O   . ARG A 1 212 ? 10.918  -14.020 4.670   1.00 10.50 ? 212 ARG A O   1 
ATOM   1666 C  CB  . ARG A 1 212 ? 14.091  -14.420 5.032   1.00 13.99 ? 212 ARG A CB  1 
ATOM   1667 C  CG  . ARG A 1 212 ? 13.709  -15.464 3.991   1.00 16.14 ? 212 ARG A CG  1 
ATOM   1668 C  CD  . ARG A 1 212 ? 14.469  -16.746 4.269   1.00 19.55 ? 212 ARG A CD  1 
ATOM   1669 N  NE  . ARG A 1 212 ? 14.527  -17.371 2.954   1.00 21.82 ? 212 ARG A NE  1 
ATOM   1670 C  CZ  . ARG A 1 212 ? 15.246  -18.434 2.636   1.00 22.80 ? 212 ARG A CZ  1 
ATOM   1671 N  NH1 . ARG A 1 212 ? 15.991  -19.029 3.557   1.00 21.99 ? 212 ARG A NH1 1 
ATOM   1672 N  NH2 . ARG A 1 212 ? 15.219  -18.883 1.386   1.00 22.13 ? 212 ARG A NH2 1 
ATOM   1673 N  N   . ASN A 1 213 ? 11.641  -13.910 6.792   1.00 11.88 ? 213 ASN A N   1 
ATOM   1674 C  CA  . ASN A 1 213 ? 10.474  -14.562 7.366   1.00 11.22 ? 213 ASN A CA  1 
ATOM   1675 C  C   . ASN A 1 213 ? 9.432   -13.502 7.711   1.00 10.30 ? 213 ASN A C   1 
ATOM   1676 O  O   . ASN A 1 213 ? 9.769   -12.517 8.372   1.00 9.05  ? 213 ASN A O   1 
ATOM   1677 C  CB  . ASN A 1 213 ? 10.860  -15.381 8.607   1.00 11.82 ? 213 ASN A CB  1 
ATOM   1678 C  CG  . ASN A 1 213 ? 11.813  -16.511 8.271   1.00 12.79 ? 213 ASN A CG  1 
ATOM   1679 O  OD1 . ASN A 1 213 ? 11.619  -17.202 7.281   1.00 13.37 ? 213 ASN A OD1 1 
ATOM   1680 N  ND2 . ASN A 1 213 ? 12.879  -16.656 9.037   1.00 13.71 ? 213 ASN A ND2 1 
ATOM   1681 N  N   . PRO A 1 214 ? 8.149   -13.711 7.322   1.00 10.36 ? 214 PRO A N   1 
ATOM   1682 C  CA  . PRO A 1 214 ? 7.052   -12.806 7.677   1.00 10.38 ? 214 PRO A CA  1 
ATOM   1683 C  C   . PRO A 1 214 ? 6.590   -13.038 9.114   1.00 10.03 ? 214 PRO A C   1 
ATOM   1684 O  O   . PRO A 1 214 ? 6.888   -14.065 9.706   1.00 9.63  ? 214 PRO A O   1 
ATOM   1685 C  CB  . PRO A 1 214 ? 5.888   -13.219 6.747   1.00 10.63 ? 214 PRO A CB  1 
ATOM   1686 C  CG  . PRO A 1 214 ? 6.173   -14.672 6.405   1.00 11.11 ? 214 PRO A CG  1 
ATOM   1687 C  CD  . PRO A 1 214 ? 7.683   -14.853 6.511   1.00 11.19 ? 214 PRO A CD  1 
ATOM   1688 N  N   . VAL A 1 215 ? 5.832   -12.083 9.654   1.00 9.31  ? 215 VAL A N   1 
ATOM   1689 C  CA  . VAL A 1 215 ? 5.076   -12.303 10.876  1.00 9.30  ? 215 VAL A CA  1 
ATOM   1690 C  C   . VAL A 1 215 ? 3.613   -12.413 10.477  1.00 9.02  ? 215 VAL A C   1 
ATOM   1691 O  O   . VAL A 1 215 ? 3.258   -12.125 9.331   1.00 9.14  ? 215 VAL A O   1 
ATOM   1692 C  CB  . VAL A 1 215 ? 5.281   -11.162 11.898  1.00 9.35  ? 215 VAL A CB  1 
ATOM   1693 C  CG1 . VAL A 1 215 ? 6.718   -11.079 12.434  1.00 9.18  ? 215 VAL A CG1 1 
ATOM   1694 C  CG2 . VAL A 1 215 ? 4.815   -9.823  11.354  1.00 9.35  ? 215 VAL A CG2 1 
ATOM   1695 N  N   . GLN A 1 216 ? 2.765   -12.726 11.454  1.00 8.95  ? 216 GLN A N   1 
ATOM   1696 C  CA  . GLN A 1 216 ? 1.341   -12.849 11.219  1.00 9.62  ? 216 GLN A CA  1 
ATOM   1697 C  C   . GLN A 1 216 ? 0.573   -11.902 12.133  1.00 9.66  ? 216 GLN A C   1 
ATOM   1698 O  O   . GLN A 1 216 ? 0.927   -11.780 13.298  1.00 9.64  ? 216 GLN A O   1 
ATOM   1699 C  CB  . GLN A 1 216 ? 0.922   -14.264 11.586  1.00 10.24 ? 216 GLN A CB  1 
ATOM   1700 C  CG  . GLN A 1 216 ? 1.472   -15.325 10.643  1.00 12.06 ? 216 GLN A CG  1 
ATOM   1701 C  CD  . GLN A 1 216 ? 1.166   -16.699 11.196  1.00 14.18 ? 216 GLN A CD  1 
ATOM   1702 O  OE1 . GLN A 1 216 ? 0.068   -16.956 11.711  1.00 15.01 ? 216 GLN A OE1 1 
ATOM   1703 N  NE2 . GLN A 1 216 ? 2.145   -17.584 11.105  1.00 14.89 ? 216 GLN A NE2 1 
ATOM   1704 N  N   . ILE A 1 217 ? -0.487  -11.288 11.595  1.00 9.48  ? 217 ILE A N   1 
ATOM   1705 C  CA  . ILE A 1 217 ? -1.576  -10.668 12.347  1.00 9.68  ? 217 ILE A CA  1 
ATOM   1706 C  C   . ILE A 1 217 ? -2.897  -11.216 11.813  1.00 10.79 ? 217 ILE A C   1 
ATOM   1707 O  O   . ILE A 1 217 ? -2.960  -11.628 10.650  1.00 10.98 ? 217 ILE A O   1 
ATOM   1708 C  CB  . ILE A 1 217 ? -1.533  -9.130  12.227  1.00 9.13  ? 217 ILE A CB  1 
ATOM   1709 C  CG1 . ILE A 1 217 ? -1.817  -8.633  10.808  1.00 9.15  ? 217 ILE A CG1 1 
ATOM   1710 C  CG2 . ILE A 1 217 ? -0.202  -8.621  12.746  1.00 9.76  ? 217 ILE A CG2 1 
ATOM   1711 C  CD1 . ILE A 1 217 ? -1.881  -7.127  10.670  1.00 9.47  ? 217 ILE A CD1 1 
ATOM   1712 N  N   . SER A 1 218 ? -3.953  -11.185 12.648  1.00 10.94 ? 218 SER A N   1 
ATOM   1713 C  CA  . SER A 1 218 ? -5.229  -11.785 12.277  1.00 11.19 ? 218 SER A CA  1 
ATOM   1714 C  C   . SER A 1 218 ? -5.973  -10.927 11.249  1.00 12.02 ? 218 SER A C   1 
ATOM   1715 O  O   . SER A 1 218 ? -5.667  -9.749  11.046  1.00 10.44 ? 218 SER A O   1 
ATOM   1716 C  CB  . SER A 1 218 ? -6.079  -12.050 13.490  1.00 10.64 ? 218 SER A CB  1 
ATOM   1717 O  OG  . SER A 1 218 ? -6.537  -10.830 14.038  1.00 10.88 ? 218 SER A OG  1 
ATOM   1718 N  N   . GLN A 1 219 ? -6.964  -11.545 10.594  1.00 13.33 ? 219 GLN A N   1 
ATOM   1719 C  CA  . GLN A 1 219 ? -7.860  -10.834 9.695   1.00 15.12 ? 219 GLN A CA  1 
ATOM   1720 C  C   . GLN A 1 219 ? -8.490  -9.637  10.418  1.00 14.09 ? 219 GLN A C   1 
ATOM   1721 O  O   . GLN A 1 219 ? -8.543  -8.544  9.857   1.00 13.59 ? 219 GLN A O   1 
ATOM   1722 C  CB  . GLN A 1 219 ? -8.839  -11.801 9.006   1.00 20.05 ? 219 GLN A CB  1 
ATOM   1723 C  CG  . GLN A 1 219 ? -10.076 -11.158 8.367   1.00 24.61 ? 219 GLN A CG  1 
ATOM   1724 C  CD  . GLN A 1 219 ? -9.893  -10.138 7.258   1.00 32.70 ? 219 GLN A CD  1 
ATOM   1725 O  OE1 . GLN A 1 219 ? -10.870 -9.636  6.684   1.00 34.57 ? 219 GLN A OE1 1 
ATOM   1726 N  NE2 . GLN A 1 219 ? -8.649  -9.788  6.949   1.00 35.27 ? 219 GLN A NE2 1 
ATOM   1727 N  N   . GLU A 1 220 ? -8.929  -9.830  11.669  1.00 13.85 ? 220 GLU A N   1 
ATOM   1728 C  CA  . GLU A 1 220 ? -9.522  -8.750  12.454  1.00 14.48 ? 220 GLU A CA  1 
ATOM   1729 C  C   . GLU A 1 220 ? -8.534  -7.587  12.628  1.00 13.64 ? 220 GLU A C   1 
ATOM   1730 O  O   . GLU A 1 220 ? -8.920  -6.419  12.509  1.00 13.70 ? 220 GLU A O   1 
ATOM   1731 C  CB  . GLU A 1 220 ? -10.057 -9.273  13.789  1.00 17.97 ? 220 GLU A CB  1 
ATOM   1732 C  CG  . GLU A 1 220 ? -11.217 -10.249 13.642  1.00 21.34 ? 220 GLU A CG  1 
ATOM   1733 C  CD  . GLU A 1 220 ? -10.842 -11.727 13.529  1.00 25.92 ? 220 GLU A CD  1 
ATOM   1734 O  OE1 . GLU A 1 220 ? -9.636  -12.066 13.306  1.00 23.06 ? 220 GLU A OE1 1 
ATOM   1735 O  OE2 . GLU A 1 220 ? -11.768 -12.558 13.688  1.00 30.68 ? 220 GLU A OE2 1 
ATOM   1736 N  N   . GLN A 1 221 ? -7.260  -7.902  12.906  1.00 12.11 ? 221 GLN A N   1 
ATOM   1737 C  CA  . GLN A 1 221 ? -6.238  -6.874  13.115  1.00 12.24 ? 221 GLN A CA  1 
ATOM   1738 C  C   . GLN A 1 221 ? -5.925  -6.153  11.807  1.00 12.03 ? 221 GLN A C   1 
ATOM   1739 O  O   . GLN A 1 221 ? -5.733  -4.947  11.793  1.00 12.16 ? 221 GLN A O   1 
ATOM   1740 C  CB  . GLN A 1 221 ? -4.937  -7.434  13.690  1.00 11.30 ? 221 GLN A CB  1 
ATOM   1741 C  CG  . GLN A 1 221 ? -5.048  -7.896  15.139  1.00 11.34 ? 221 GLN A CG  1 
ATOM   1742 C  CD  . GLN A 1 221 ? -3.758  -8.522  15.616  1.00 11.01 ? 221 GLN A CD  1 
ATOM   1743 O  OE1 . GLN A 1 221 ? -3.375  -9.627  15.204  1.00 10.73 ? 221 GLN A OE1 1 
ATOM   1744 N  NE2 . GLN A 1 221 ? -3.054  -7.793  16.468  1.00 10.86 ? 221 GLN A NE2 1 
ATOM   1745 N  N   . LEU A 1 222 ? -5.835  -6.905  10.711  1.00 11.79 ? 222 LEU A N   1 
ATOM   1746 C  CA  . LEU A 1 222 ? -5.595  -6.322  9.402   1.00 12.35 ? 222 LEU A CA  1 
ATOM   1747 C  C   . LEU A 1 222 ? -6.768  -5.409  9.050   1.00 12.71 ? 222 LEU A C   1 
ATOM   1748 O  O   . LEU A 1 222 ? -6.566  -4.292  8.573   1.00 11.82 ? 222 LEU A O   1 
ATOM   1749 C  CB  . LEU A 1 222 ? -5.452  -7.482  8.404   1.00 12.96 ? 222 LEU A CB  1 
ATOM   1750 C  CG  . LEU A 1 222 ? -4.790  -7.186  7.058   1.00 14.71 ? 222 LEU A CG  1 
ATOM   1751 C  CD1 . LEU A 1 222 ? -3.464  -6.431  7.202   1.00 13.08 ? 222 LEU A CD1 1 
ATOM   1752 C  CD2 . LEU A 1 222 ? -4.561  -8.494  6.295   1.00 15.62 ? 222 LEU A CD2 1 
ATOM   1753 N  N   . LEU A 1 223 ? -8.000  -5.871  9.302   1.00 13.42 ? 223 LEU A N   1 
ATOM   1754 C  CA  . LEU A 1 223 ? -9.157  -5.048  8.963   1.00 15.41 ? 223 LEU A CA  1 
ATOM   1755 C  C   . LEU A 1 223 ? -9.115  -3.722  9.722   1.00 14.09 ? 223 LEU A C   1 
ATOM   1756 O  O   . LEU A 1 223 ? -9.399  -2.667  9.139   1.00 12.95 ? 223 LEU A O   1 
ATOM   1757 C  CB  . LEU A 1 223 ? -10.473 -5.798  9.217   1.00 17.10 ? 223 LEU A CB  1 
ATOM   1758 C  CG  . LEU A 1 223 ? -11.711 -5.171  8.564   1.00 19.16 ? 223 LEU A CG  1 
ATOM   1759 C  CD1 . LEU A 1 223 ? -11.669 -5.298  7.056   1.00 18.14 ? 223 LEU A CD1 1 
ATOM   1760 C  CD2 . LEU A 1 223 ? -12.987 -5.801  9.106   1.00 20.37 ? 223 LEU A CD2 1 
ATOM   1761 N  N   . ALA A 1 224 ? -8.773  -3.804  11.016  1.00 12.05 ? 224 ALA A N   1 
ATOM   1762 C  CA  . ALA A 1 224 ? -8.741  -2.635  11.870  1.00 11.54 ? 224 ALA A CA  1 
ATOM   1763 C  C   . ALA A 1 224 ? -7.761  -1.618  11.287  1.00 11.72 ? 224 ALA A C   1 
ATOM   1764 O  O   . ALA A 1 224 ? -8.089  -0.434  11.179  1.00 10.93 ? 224 ALA A O   1 
ATOM   1765 C  CB  . ALA A 1 224 ? -8.362  -3.037  13.273  1.00 11.20 ? 224 ALA A CB  1 
ATOM   1766 N  N   . LEU A 1 225 ? -6.579  -2.107  10.865  1.00 11.30 ? 225 LEU A N   1 
ATOM   1767 C  CA  . LEU A 1 225 ? -5.543  -1.269  10.278  1.00 11.62 ? 225 LEU A CA  1 
ATOM   1768 C  C   . LEU A 1 225 ? -6.023  -0.631  8.969   1.00 12.45 ? 225 LEU A C   1 
ATOM   1769 O  O   . LEU A 1 225 ? -5.746  0.544   8.707   1.00 13.12 ? 225 LEU A O   1 
ATOM   1770 C  CB  . LEU A 1 225 ? -4.281  -2.110  10.070  1.00 10.73 ? 225 LEU A CB  1 
ATOM   1771 C  CG  . LEU A 1 225 ? -3.040  -1.357  9.563   1.00 10.82 ? 225 LEU A CG  1 
ATOM   1772 C  CD1 . LEU A 1 225 ? -2.542  -0.289  10.557  1.00 10.07 ? 225 LEU A CD1 1 
ATOM   1773 C  CD2 . LEU A 1 225 ? -1.926  -2.359  9.254   1.00 9.58  ? 225 LEU A CD2 1 
ATOM   1774 N  N   . GLU A 1 226 ? -6.752  -1.403  8.155   1.00 12.33 ? 226 GLU A N   1 
ATOM   1775 C  CA  . GLU A 1 226 ? -7.184  -0.918  6.855   1.00 13.00 ? 226 GLU A CA  1 
ATOM   1776 C  C   . GLU A 1 226 ? -8.426  -0.021  6.977   1.00 12.72 ? 226 GLU A C   1 
ATOM   1777 O  O   . GLU A 1 226 ? -8.784  0.648   6.006   1.00 12.71 ? 226 GLU A O   1 
ATOM   1778 C  CB  . GLU A 1 226 ? -7.508  -2.097  5.925   1.00 13.04 ? 226 GLU A CB  1 
ATOM   1779 C  CG  . GLU A 1 226 ? -6.314  -2.972  5.564   1.00 13.26 ? 226 GLU A CG  1 
ATOM   1780 C  CD  . GLU A 1 226 ? -6.743  -4.367  5.146   1.00 14.46 ? 226 GLU A CD  1 
ATOM   1781 O  OE1 . GLU A 1 226 ? -7.941  -4.663  5.312   1.00 14.11 ? 226 GLU A OE1 1 
ATOM   1782 O  OE2 . GLU A 1 226 ? -5.879  -5.152  4.657   1.00 13.90 ? 226 GLU A OE2 1 
ATOM   1783 N  N   . THR A 1 227 ? -9.112  -0.016  8.124   1.00 11.85 ? 227 THR A N   1 
ATOM   1784 C  CA  . THR A 1 227 ? -10.338 0.777   8.154   1.00 12.82 ? 227 THR A CA  1 
ATOM   1785 C  C   . THR A 1 227 ? -10.344 1.870   9.228   1.00 13.37 ? 227 THR A C   1 
ATOM   1786 O  O   . THR A 1 227 ? -11.210 2.746   9.177   1.00 12.90 ? 227 THR A O   1 
ATOM   1787 C  CB  . THR A 1 227 ? -11.605 -0.087  8.275   1.00 12.20 ? 227 THR A CB  1 
ATOM   1788 O  OG1 . THR A 1 227 ? -11.576 -0.751  9.535   1.00 11.42 ? 227 THR A OG1 1 
ATOM   1789 C  CG2 . THR A 1 227 ? -11.742 -1.106  7.165   1.00 12.71 ? 227 THR A CG2 1 
ATOM   1790 N  N   . ALA A 1 228 ? -9.397  1.855   10.181  1.00 13.24 ? 228 ALA A N   1 
ATOM   1791 C  CA  . ALA A 1 228 ? -9.500  2.796   11.290  1.00 13.86 ? 228 ALA A CA  1 
ATOM   1792 C  C   . ALA A 1 228 ? -9.093  4.231   10.919  1.00 14.18 ? 228 ALA A C   1 
ATOM   1793 O  O   . ALA A 1 228 ? -9.523  5.180   11.592  1.00 14.93 ? 228 ALA A O   1 
ATOM   1794 C  CB  . ALA A 1 228 ? -8.785  2.290   12.528  1.00 14.42 ? 228 ALA A CB  1 
ATOM   1795 N  N   . LEU A 1 229 ? -8.270  4.410   9.868   1.00 12.98 ? 229 LEU A N   1 
ATOM   1796 C  CA  . LEU A 1 229 ? -7.554  5.671   9.744   1.00 12.73 ? 229 LEU A CA  1 
ATOM   1797 C  C   . LEU A 1 229 ? -7.945  6.424   8.479   1.00 12.37 ? 229 LEU A C   1 
ATOM   1798 O  O   . LEU A 1 229 ? -8.344  5.835   7.469   1.00 11.30 ? 229 LEU A O   1 
ATOM   1799 C  CB  . LEU A 1 229 ? -6.042  5.410   9.759   1.00 13.55 ? 229 LEU A CB  1 
ATOM   1800 C  CG  . LEU A 1 229 ? -5.489  4.644   10.965  1.00 13.92 ? 229 LEU A CG  1 
ATOM   1801 C  CD1 . LEU A 1 229 ? -3.967  4.447   10.829  1.00 14.03 ? 229 LEU A CD1 1 
ATOM   1802 C  CD2 . LEU A 1 229 ? -5.837  5.355   12.279  1.00 14.00 ? 229 LEU A CD2 1 
ATOM   1803 N  N   . TYR A 1 230 ? -7.772  7.750   8.565   1.00 12.61 ? 230 TYR A N   1 
ATOM   1804 C  CA  . TYR A 1 230 ? -8.013  8.704   7.501   1.00 12.66 ? 230 TYR A CA  1 
ATOM   1805 C  C   . TYR A 1 230 ? -6.736  9.488   7.259   1.00 12.27 ? 230 TYR A C   1 
ATOM   1806 O  O   . TYR A 1 230 ? -6.057  9.834   8.215   1.00 12.00 ? 230 TYR A O   1 
ATOM   1807 C  CB  . TYR A 1 230 ? -9.203  9.610   7.837   1.00 14.45 ? 230 TYR A CB  1 
ATOM   1808 C  CG  . TYR A 1 230 ? -10.496 8.832   7.833   1.00 17.36 ? 230 TYR A CG  1 
ATOM   1809 C  CD1 . TYR A 1 230 ? -10.880 8.084   8.934   1.00 18.05 ? 230 TYR A CD1 1 
ATOM   1810 C  CD2 . TYR A 1 230 ? -11.271 8.766   6.688   1.00 17.99 ? 230 TYR A CD2 1 
ATOM   1811 C  CE1 . TYR A 1 230 ? -12.031 7.310   8.907   1.00 21.38 ? 230 TYR A CE1 1 
ATOM   1812 C  CE2 . TYR A 1 230 ? -12.439 8.024   6.654   1.00 21.08 ? 230 TYR A CE2 1 
ATOM   1813 C  CZ  . TYR A 1 230 ? -12.811 7.288   7.762   1.00 22.52 ? 230 TYR A CZ  1 
ATOM   1814 O  OH  . TYR A 1 230 ? -13.947 6.538   7.716   1.00 28.68 ? 230 TYR A OH  1 
ATOM   1815 N  N   . CYS A 1 231 ? -6.439  9.766   5.979   1.00 12.49 ? 231 CYS A N   1 
ATOM   1816 C  CA  . CYS A 1 231 ? -5.320  10.590  5.560   1.00 12.66 ? 231 CYS A CA  1 
ATOM   1817 C  C   . CYS A 1 231 ? -5.604  12.059  5.876   1.00 12.26 ? 231 CYS A C   1 
ATOM   1818 O  O   . CYS A 1 231 ? -4.702  12.876  5.863   1.00 12.30 ? 231 CYS A O   1 
ATOM   1819 C  CB  . CYS A 1 231 ? -5.212  10.559  4.044   1.00 15.39 ? 231 CYS A CB  1 
ATOM   1820 S  SG  . CYS A 1 231 ? -4.590  8.998   3.387   1.00 23.69 ? 231 CYS A SG  1 
ATOM   1821 N  N   . THR A 1 232 ? -6.872  12.402  6.119   1.00 12.02 ? 232 THR A N   1 
ATOM   1822 C  CA  . THR A 1 232 ? -7.263  13.798  6.173   1.00 13.06 ? 232 THR A CA  1 
ATOM   1823 C  C   . THR A 1 232 ? -7.507  14.211  7.619   1.00 12.82 ? 232 THR A C   1 
ATOM   1824 O  O   . THR A 1 232 ? -7.735  13.351  8.472   1.00 11.31 ? 232 THR A O   1 
ATOM   1825 C  CB  . THR A 1 232 ? -8.534  14.023  5.353   1.00 13.98 ? 232 THR A CB  1 
ATOM   1826 O  OG1 . THR A 1 232 ? -9.402  12.918  5.613   1.00 16.24 ? 232 THR A OG1 1 
ATOM   1827 C  CG2 . THR A 1 232 ? -8.278  14.143  3.866   1.00 14.37 ? 232 THR A CG2 1 
ATOM   1828 N  N   . HIS A 1 233 ? -7.461  15.533  7.863   1.00 11.89 ? 233 HIS A N   1 
ATOM   1829 C  CA  . HIS A 1 233 ? -7.860  16.094  9.139   1.00 12.67 ? 233 HIS A CA  1 
ATOM   1830 C  C   . HIS A 1 233 ? -9.333  15.797  9.356   1.00 13.02 ? 233 HIS A C   1 
ATOM   1831 O  O   . HIS A 1 233 ? -10.101 15.563  8.404   1.00 11.90 ? 233 HIS A O   1 
ATOM   1832 C  CB  . HIS A 1 233 ? -7.643  17.618  9.197   1.00 13.57 ? 233 HIS A CB  1 
ATOM   1833 C  CG  . HIS A 1 233 ? -6.220  18.042  9.073   1.00 15.64 ? 233 HIS A CG  1 
ATOM   1834 N  ND1 . HIS A 1 233 ? -5.277  17.788  10.065  1.00 16.89 ? 233 HIS A ND1 1 
ATOM   1835 C  CD2 . HIS A 1 233 ? -5.568  18.690  8.085   1.00 16.39 ? 233 HIS A CD2 1 
ATOM   1836 C  CE1 . HIS A 1 233 ? -4.102  18.256  9.678   1.00 16.50 ? 233 HIS A CE1 1 
ATOM   1837 N  NE2 . HIS A 1 233 ? -4.253  18.809  8.468   1.00 16.75 ? 233 HIS A NE2 1 
ATOM   1838 N  N   . MET A 1 234 ? -9.716  15.839  10.622  1.00 13.01 ? 234 MET A N   1 
ATOM   1839 C  CA  . MET A 1 234 ? -11.090 15.510  10.924  1.00 15.54 ? 234 MET A CA  1 
ATOM   1840 C  C   . MET A 1 234 ? -12.002 16.537  10.252  1.00 15.13 ? 234 MET A C   1 
ATOM   1841 O  O   . MET A 1 234 ? -13.100 16.182  9.865   1.00 15.61 ? 234 MET A O   1 
ATOM   1842 C  CB  . MET A 1 234 ? -11.326 15.485  12.440  1.00 18.05 ? 234 MET A CB  1 
ATOM   1843 C  CG  . MET A 1 234 ? -12.742 15.020  12.833  1.00 23.84 ? 234 MET A CG  1 
ATOM   1844 S  SD  . MET A 1 234 ? -13.042 14.946  14.644  1.00 29.00 ? 234 MET A SD  1 
ATOM   1845 C  CE  . MET A 1 234 ? -11.665 15.918  15.270  1.00 25.78 ? 234 MET A CE  1 
ATOM   1846 N  N   . ASP A 1 235 ? -11.561 17.796  10.094  1.00 13.83 ? 235 ASP A N   1 
ATOM   1847 C  CA  . ASP A 1 235 ? -12.468 18.805  9.566   1.00 14.15 ? 235 ASP A CA  1 
ATOM   1848 C  C   . ASP A 1 235 ? -12.397 18.959  8.039   1.00 14.74 ? 235 ASP A C   1 
ATOM   1849 O  O   . ASP A 1 235 ? -12.926 19.943  7.517   1.00 14.01 ? 235 ASP A O   1 
ATOM   1850 C  CB  . ASP A 1 235 ? -12.291 20.147  10.280  1.00 12.89 ? 235 ASP A CB  1 
ATOM   1851 C  CG  . ASP A 1 235 ? -10.931 20.757  10.045  1.00 13.53 ? 235 ASP A CG  1 
ATOM   1852 O  OD1 . ASP A 1 235 ? -10.089 20.082  9.413   1.00 13.04 ? 235 ASP A OD1 1 
ATOM   1853 O  OD2 . ASP A 1 235 ? -10.716 21.910  10.494  1.00 14.04 ? 235 ASP A OD2 1 
ATOM   1854 N  N   . ASP A 1 236 ? -11.723 18.028  7.338   1.00 14.74 ? 236 ASP A N   1 
ATOM   1855 C  CA  . ASP A 1 236 ? -11.510 18.130  5.897   1.00 15.44 ? 236 ASP A CA  1 
ATOM   1856 C  C   . ASP A 1 236 ? -12.848 18.030  5.160   1.00 15.19 ? 236 ASP A C   1 
ATOM   1857 O  O   . ASP A 1 236 ? -13.648 17.132  5.426   1.00 13.77 ? 236 ASP A O   1 
ATOM   1858 C  CB  . ASP A 1 236 ? -10.521 17.095  5.344   1.00 15.82 ? 236 ASP A CB  1 
ATOM   1859 C  CG  . ASP A 1 236 ? -9.949  17.470  3.975   1.00 17.68 ? 236 ASP A CG  1 
ATOM   1860 O  OD1 . ASP A 1 236 ? -10.714 17.439  2.951   1.00 18.55 ? 236 ASP A OD1 1 
ATOM   1861 O  OD2 . ASP A 1 236 ? -8.745  17.816  3.929   1.00 18.08 ? 236 ASP A OD2 1 
ATOM   1862 N  N   . PRO A 1 237 ? -13.140 18.948  4.215   1.00 15.05 ? 237 PRO A N   1 
ATOM   1863 C  CA  . PRO A 1 237 ? -14.366 18.860  3.422   1.00 16.94 ? 237 PRO A CA  1 
ATOM   1864 C  C   . PRO A 1 237 ? -14.459 17.630  2.513   1.00 19.24 ? 237 PRO A C   1 
ATOM   1865 O  O   . PRO A 1 237 ? -15.554 17.267  2.093   1.00 20.66 ? 237 PRO A O   1 
ATOM   1866 C  CB  . PRO A 1 237 ? -14.319 20.119  2.538   1.00 16.48 ? 237 PRO A CB  1 
ATOM   1867 C  CG  . PRO A 1 237 ? -13.387 21.065  3.279   1.00 15.81 ? 237 PRO A CG  1 
ATOM   1868 C  CD  . PRO A 1 237 ? -12.349 20.148  3.900   1.00 16.09 ? 237 PRO A CD  1 
ATOM   1869 N  N   . SER A 1 238 ? -13.321 17.018  2.165   1.00 20.21 ? 238 SER A N   1 
ATOM   1870 C  CA  . SER A 1 238 ? -13.357 15.771  1.404   1.00 22.90 ? 238 SER A CA  1 
ATOM   1871 C  C   . SER A 1 238 ? -12.444 14.719  2.035   1.00 23.27 ? 238 SER A C   1 
ATOM   1872 O  O   . SER A 1 238 ? -11.268 14.618  1.677   1.00 22.82 ? 238 SER A O   1 
ATOM   1873 C  CB  . SER A 1 238 ? -13.034 15.987  -0.050  1.00 23.17 ? 238 SER A CB  1 
ATOM   1874 O  OG  . SER A 1 238 ? -11.745 16.548  -0.199  1.00 26.01 ? 238 SER A OG  1 
ATOM   1875 N  N   . PRO A 1 239 ? -12.986 13.897  2.963   1.00 23.70 ? 239 PRO A N   1 
ATOM   1876 C  CA  . PRO A 1 239 ? -12.198 12.918  3.710   1.00 26.03 ? 239 PRO A CA  1 
ATOM   1877 C  C   . PRO A 1 239 ? -11.647 11.866  2.748   1.00 28.22 ? 239 PRO A C   1 
ATOM   1878 O  O   . PRO A 1 239 ? -12.176 11.664  1.652   1.00 26.35 ? 239 PRO A O   1 
ATOM   1879 C  CB  . PRO A 1 239 ? -13.225 12.212  4.621   1.00 26.17 ? 239 PRO A CB  1 
ATOM   1880 C  CG  . PRO A 1 239 ? -14.417 13.134  4.648   1.00 26.20 ? 239 PRO A CG  1 
ATOM   1881 C  CD  . PRO A 1 239 ? -14.415 13.819  3.295   1.00 24.73 ? 239 PRO A CD  1 
ATOM   1882 N  N   . ARG A 1 240 ? -10.565 11.210  3.170   1.00 27.35 ? 240 ARG A N   1 
ATOM   1883 C  CA  . ARG A 1 240 ? -9.958  10.173  2.359   1.00 26.02 ? 240 ARG A CA  1 
ATOM   1884 C  C   . ARG A 1 240 ? -9.450  9.104   3.316   1.00 23.80 ? 240 ARG A C   1 
ATOM   1885 O  O   . ARG A 1 240 ? -8.743  9.427   4.281   1.00 20.76 ? 240 ARG A O   1 
ATOM   1886 C  CB  . ARG A 1 240 ? -8.865  10.763  1.465   1.00 31.21 ? 240 ARG A CB  1 
ATOM   1887 C  CG  . ARG A 1 240 ? -9.272  12.043  0.744   1.00 38.67 ? 240 ARG A CG  1 
ATOM   1888 C  CD  . ARG A 1 240 ? -9.777  11.877  -0.684  1.00 45.83 ? 240 ARG A CD  1 
ATOM   1889 N  NE  . ARG A 1 240 ? -8.757  11.287  -1.544  1.00 51.33 ? 240 ARG A NE  1 
ATOM   1890 C  CZ  . ARG A 1 240 ? -7.527  11.771  -1.710  1.00 50.11 ? 240 ARG A CZ  1 
ATOM   1891 N  NH1 . ARG A 1 240 ? -7.149  12.864  -1.066  1.00 50.94 ? 240 ARG A NH1 1 
ATOM   1892 N  NH2 . ARG A 1 240 ? -6.677  11.150  -2.508  1.00 45.27 ? 240 ARG A NH2 1 
ATOM   1893 N  N   . GLU A 1 241 ? -9.885  7.857   3.071   1.00 19.06 ? 241 GLU A N   1 
ATOM   1894 C  CA  . GLU A 1 241 ? -9.449  6.740   3.885   1.00 18.51 ? 241 GLU A CA  1 
ATOM   1895 C  C   . GLU A 1 241 ? -7.950  6.535   3.663   1.00 15.68 ? 241 GLU A C   1 
ATOM   1896 O  O   . GLU A 1 241 ? -7.408  6.757   2.572   1.00 13.45 ? 241 GLU A O   1 
ATOM   1897 C  CB  . GLU A 1 241 ? -10.239 5.462   3.608   1.00 20.78 ? 241 GLU A CB  1 
ATOM   1898 C  CG  . GLU A 1 241 ? -11.738 5.599   3.771   1.00 27.54 ? 241 GLU A CG  1 
ATOM   1899 C  CD  . GLU A 1 241 ? -12.481 4.410   3.175   1.00 32.17 ? 241 GLU A CD  1 
ATOM   1900 O  OE1 . GLU A 1 241 ? -12.244 4.097   1.983   1.00 36.59 ? 241 GLU A OE1 1 
ATOM   1901 O  OE2 . GLU A 1 241 ? -13.252 3.766   3.912   1.00 34.25 ? 241 GLU A OE2 1 
ATOM   1902 N  N   . MET A 1 242 ? -7.282  6.156   4.748   1.00 13.42 ? 242 MET A N   1 
ATOM   1903 C  CA  . MET A 1 242 ? -5.885  5.794   4.649   1.00 11.67 ? 242 MET A CA  1 
ATOM   1904 C  C   . MET A 1 242 ? -5.803  4.307   4.321   1.00 11.21 ? 242 MET A C   1 
ATOM   1905 O  O   . MET A 1 242 ? -5.809  3.464   5.226   1.00 10.15 ? 242 MET A O   1 
ATOM   1906 C  CB  . MET A 1 242 ? -5.154  6.070   5.964   1.00 10.72 ? 242 MET A CB  1 
ATOM   1907 C  CG  . MET A 1 242 ? -3.646  6.074   5.762   1.00 10.05 ? 242 MET A CG  1 
ATOM   1908 S  SD  . MET A 1 242 ? -2.807  6.182   7.371   1.00 10.21 ? 242 MET A SD  1 
ATOM   1909 C  CE  . MET A 1 242 ? -3.027  7.921   7.741   1.00 9.53  ? 242 MET A CE  1 
ATOM   1910 N  N   . ILE A 1 243 ? -5.785  4.034   3.005   1.00 11.05 ? 243 ILE A N   1 
ATOM   1911 C  CA  . ILE A 1 243 ? -5.663  2.709   2.411   1.00 11.02 ? 243 ILE A CA  1 
ATOM   1912 C  C   . ILE A 1 243 ? -4.594  2.754   1.322   1.00 10.78 ? 243 ILE A C   1 
ATOM   1913 O  O   . ILE A 1 243 ? -4.241  3.836   0.803   1.00 11.09 ? 243 ILE A O   1 
ATOM   1914 C  CB  . ILE A 1 243 ? -7.019  2.247   1.844   1.00 11.47 ? 243 ILE A CB  1 
ATOM   1915 C  CG1 . ILE A 1 243 ? -7.608  3.252   0.833   1.00 12.09 ? 243 ILE A CG1 1 
ATOM   1916 C  CG2 . ILE A 1 243 ? -7.966  1.918   2.997   1.00 11.45 ? 243 ILE A CG2 1 
ATOM   1917 C  CD1 . ILE A 1 243 ? -8.929  2.850   0.154   1.00 11.17 ? 243 ILE A CD1 1 
ATOM   1918 N  N   . ASN A 1 244 ? -4.054  1.573   1.016   1.00 9.38  ? 244 ASN A N   1 
ATOM   1919 C  CA  . ASN A 1 244 ? -3.149  1.401   -0.109  1.00 9.05  ? 244 ASN A CA  1 
ATOM   1920 C  C   . ASN A 1 244 ? -2.017  2.419   -0.005  1.00 8.55  ? 244 ASN A C   1 
ATOM   1921 O  O   . ASN A 1 244 ? -1.659  3.028   -1.014  1.00 7.93  ? 244 ASN A O   1 
ATOM   1922 C  CB  . ASN A 1 244 ? -3.892  1.586   -1.442  1.00 9.40  ? 244 ASN A CB  1 
ATOM   1923 C  CG  . ASN A 1 244 ? -5.060  0.631   -1.573  1.00 10.35 ? 244 ASN A CG  1 
ATOM   1924 O  OD1 . ASN A 1 244 ? -5.009  -0.499  -1.082  1.00 10.01 ? 244 ASN A OD1 1 
ATOM   1925 N  ND2 . ASN A 1 244 ? -6.135  1.101   -2.195  1.00 10.82 ? 244 ASN A ND2 1 
ATOM   1926 N  N   . ASN A 1 245 ? -1.475  2.599   1.213   1.00 7.57  ? 245 ASN A N   1 
ATOM   1927 C  CA  . ASN A 1 245 ? -0.379  3.527   1.434   1.00 7.33  ? 245 ASN A CA  1 
ATOM   1928 C  C   . ASN A 1 245 ? 0.960   2.821   1.217   1.00 7.53  ? 245 ASN A C   1 
ATOM   1929 O  O   . ASN A 1 245 ? 1.834   2.854   2.084   1.00 7.72  ? 245 ASN A O   1 
ATOM   1930 C  CB  . ASN A 1 245 ? -0.472  4.239   2.794   1.00 6.89  ? 245 ASN A CB  1 
ATOM   1931 C  CG  . ASN A 1 245 ? -0.421  3.286   3.973   1.00 6.52  ? 245 ASN A CG  1 
ATOM   1932 O  OD1 . ASN A 1 245 ? -0.595  2.090   3.802   1.00 6.45  ? 245 ASN A OD1 1 
ATOM   1933 N  ND2 . ASN A 1 245 ? -0.211  3.802   5.169   1.00 6.65  ? 245 ASN A ND2 1 
ATOM   1934 N  N   . PHE A 1 246 ? 1.103   2.175   0.057   1.00 7.38  ? 246 PHE A N   1 
ATOM   1935 C  CA  . PHE A 1 246 ? 2.372   1.600   -0.355  1.00 7.32  ? 246 PHE A CA  1 
ATOM   1936 C  C   . PHE A 1 246 ? 2.718   2.140   -1.732  1.00 6.97  ? 246 PHE A C   1 
ATOM   1937 O  O   . PHE A 1 246 ? 1.814   2.436   -2.522  1.00 6.41  ? 246 PHE A O   1 
ATOM   1938 C  CB  . PHE A 1 246 ? 2.307   0.068   -0.434  1.00 7.42  ? 246 PHE A CB  1 
ATOM   1939 C  CG  . PHE A 1 246 ? 1.238   -0.451  -1.364  1.00 7.76  ? 246 PHE A CG  1 
ATOM   1940 C  CD1 . PHE A 1 246 ? -0.087  -0.541  -0.940  1.00 7.65  ? 246 PHE A CD1 1 
ATOM   1941 C  CD2 . PHE A 1 246 ? 1.561   -0.819  -2.663  1.00 7.57  ? 246 PHE A CD2 1 
ATOM   1942 C  CE1 . PHE A 1 246 ? -1.079  -1.010  -1.791  1.00 8.06  ? 246 PHE A CE1 1 
ATOM   1943 C  CE2 . PHE A 1 246 ? 0.577   -1.325  -3.508  1.00 8.10  ? 246 PHE A CE2 1 
ATOM   1944 C  CZ  . PHE A 1 246 ? -0.742  -1.397  -3.081  1.00 8.00  ? 246 PHE A CZ  1 
ATOM   1945 N  N   . ARG A 1 247 ? 4.028   2.269   -1.977  1.00 6.99  ? 247 ARG A N   1 
ATOM   1946 C  CA  . ARG A 1 247 ? 4.572   2.680   -3.257  1.00 7.55  ? 247 ARG A CA  1 
ATOM   1947 C  C   . ARG A 1 247 ? 4.732   1.440   -4.140  1.00 7.75  ? 247 ARG A C   1 
ATOM   1948 O  O   . ARG A 1 247 ? 5.101   0.379   -3.624  1.00 7.57  ? 247 ARG A O   1 
ATOM   1949 C  CB  . ARG A 1 247 ? 5.967   3.276   -3.024  1.00 7.58  ? 247 ARG A CB  1 
ATOM   1950 C  CG  . ARG A 1 247 ? 6.389   4.260   -4.098  1.00 7.88  ? 247 ARG A CG  1 
ATOM   1951 C  CD  . ARG A 1 247 ? 7.836   4.655   -3.948  1.00 7.71  ? 247 ARG A CD  1 
ATOM   1952 N  NE  . ARG A 1 247 ? 8.191   5.720   -4.878  1.00 7.78  ? 247 ARG A NE  1 
ATOM   1953 C  CZ  . ARG A 1 247 ? 9.411   6.244   -5.006  1.00 7.90  ? 247 ARG A CZ  1 
ATOM   1954 N  NH1 . ARG A 1 247 ? 10.435  5.816   -4.272  1.00 7.73  ? 247 ARG A NH1 1 
ATOM   1955 N  NH2 . ARG A 1 247 ? 9.599   7.213   -5.877  1.00 8.23  ? 247 ARG A NH2 1 
ATOM   1956 N  N   . GLN A 1 248 ? 4.513   1.592   -5.466  1.00 7.65  ? 248 GLN A N   1 
ATOM   1957 C  CA  . GLN A 1 248 ? 4.874   0.534   -6.403  1.00 7.51  ? 248 GLN A CA  1 
ATOM   1958 C  C   . GLN A 1 248 ? 6.379   0.266   -6.351  1.00 7.45  ? 248 GLN A C   1 
ATOM   1959 O  O   . GLN A 1 248 ? 7.178   1.155   -6.021  1.00 7.06  ? 248 GLN A O   1 
ATOM   1960 C  CB  . GLN A 1 248 ? 4.448   0.897   -7.832  1.00 8.12  ? 248 GLN A CB  1 
ATOM   1961 C  CG  . GLN A 1 248 ? 2.927   1.014   -7.976  1.00 8.14  ? 248 GLN A CG  1 
ATOM   1962 C  CD  . GLN A 1 248 ? 2.240   -0.317  -7.745  1.00 8.04  ? 248 GLN A CD  1 
ATOM   1963 O  OE1 . GLN A 1 248 ? 2.160   -1.162  -8.656  1.00 8.19  ? 248 GLN A OE1 1 
ATOM   1964 N  NE2 . GLN A 1 248 ? 1.687   -0.490  -6.560  1.00 6.86  ? 248 GLN A NE2 1 
ATOM   1965 N  N   . VAL A 1 249 ? 6.777   -0.970  -6.717  1.00 7.09  ? 249 VAL A N   1 
ATOM   1966 C  CA  . VAL A 1 249 ? 8.192   -1.282  -6.767  1.00 6.77  ? 249 VAL A CA  1 
ATOM   1967 C  C   . VAL A 1 249 ? 8.841   -0.503  -7.916  1.00 6.78  ? 249 VAL A C   1 
ATOM   1968 O  O   . VAL A 1 249 ? 8.171   -0.010  -8.819  1.00 6.55  ? 249 VAL A O   1 
ATOM   1969 C  CB  . VAL A 1 249 ? 8.490   -2.797  -6.835  1.00 6.68  ? 249 VAL A CB  1 
ATOM   1970 C  CG1 . VAL A 1 249 ? 8.111   -3.540  -5.552  1.00 6.64  ? 249 VAL A CG1 1 
ATOM   1971 C  CG2 . VAL A 1 249 ? 7.940   -3.469  -8.093  1.00 6.82  ? 249 VAL A CG2 1 
ATOM   1972 N  N   . GLN A 1 250 ? 10.169  -0.420  -7.847  1.00 6.70  ? 250 GLN A N   1 
ATOM   1973 C  CA  . GLN A 1 250 ? 10.958  0.561   -8.561  1.00 7.43  ? 250 GLN A CA  1 
ATOM   1974 C  C   . GLN A 1 250 ? 12.001  -0.181  -9.393  1.00 8.47  ? 250 GLN A C   1 
ATOM   1975 O  O   . GLN A 1 250 ? 12.430  -1.281  -9.002  1.00 8.42  ? 250 GLN A O   1 
ATOM   1976 C  CB  . GLN A 1 250 ? 11.654  1.473   -7.544  1.00 7.01  ? 250 GLN A CB  1 
ATOM   1977 C  CG  . GLN A 1 250 ? 10.692  2.231   -6.621  1.00 6.53  ? 250 GLN A CG  1 
ATOM   1978 C  CD  . GLN A 1 250 ? 9.972   3.341   -7.354  1.00 6.56  ? 250 GLN A CD  1 
ATOM   1979 O  OE1 . GLN A 1 250 ? 10.579  4.198   -7.993  1.00 6.56  ? 250 GLN A OE1 1 
ATOM   1980 N  NE2 . GLN A 1 250 ? 8.653   3.320   -7.307  1.00 6.26  ? 250 GLN A NE2 1 
ATOM   1981 N  N   . LYS A 1 251 ? 12.422  0.459   -10.497 1.00 8.72  ? 251 LYS A N   1 
ATOM   1982 C  CA  . LYS A 1 251 ? 13.520  -0.022  -11.325 1.00 9.92  ? 251 LYS A CA  1 
ATOM   1983 C  C   . LYS A 1 251 ? 14.736  -0.306  -10.444 1.00 10.34 ? 251 LYS A C   1 
ATOM   1984 O  O   . LYS A 1 251 ? 14.957  0.406   -9.480  1.00 9.56  ? 251 LYS A O   1 
ATOM   1985 C  CB  . LYS A 1 251 ? 13.901  1.034   -12.367 1.00 10.22 ? 251 LYS A CB  1 
ATOM   1986 C  CG  . LYS A 1 251 ? 12.969  1.183   -13.573 1.00 10.42 ? 251 LYS A CG  1 
ATOM   1987 C  CD  . LYS A 1 251 ? 12.924  -0.037  -14.486 1.00 10.52 ? 251 LYS A CD  1 
ATOM   1988 C  CE  . LYS A 1 251 ? 12.094  0.188   -15.736 1.00 10.16 ? 251 LYS A CE  1 
ATOM   1989 N  NZ  . LYS A 1 251 ? 10.632  0.267   -15.444 1.00 9.38  ? 251 LYS A NZ  1 
ATOM   1990 N  N   . PHE A 1 252 ? 15.540  -1.316  -10.818 1.00 11.40 ? 252 PHE A N   1 
ATOM   1991 C  CA  . PHE A 1 252 ? 16.742  -1.674  -10.069 1.00 12.69 ? 252 PHE A CA  1 
ATOM   1992 C  C   . PHE A 1 252 ? 17.886  -0.661  -10.165 1.00 13.12 ? 252 PHE A C   1 
ATOM   1993 O  O   . PHE A 1 252 ? 18.583  -0.466  -9.171  1.00 13.17 ? 252 PHE A O   1 
ATOM   1994 C  CB  . PHE A 1 252 ? 17.185  -3.111  -10.367 1.00 13.01 ? 252 PHE A CB  1 
ATOM   1995 C  CG  . PHE A 1 252 ? 16.402  -4.079  -9.521  1.00 14.26 ? 252 PHE A CG  1 
ATOM   1996 C  CD1 . PHE A 1 252 ? 16.764  -4.311  -8.198  1.00 14.79 ? 252 PHE A CD1 1 
ATOM   1997 C  CD2 . PHE A 1 252 ? 15.243  -4.673  -10.014 1.00 15.16 ? 252 PHE A CD2 1 
ATOM   1998 C  CE1 . PHE A 1 252 ? 16.024  -5.180  -7.403  1.00 14.73 ? 252 PHE A CE1 1 
ATOM   1999 C  CE2 . PHE A 1 252 ? 14.490  -5.517  -9.204  1.00 15.30 ? 252 PHE A CE2 1 
ATOM   2000 C  CZ  . PHE A 1 252 ? 14.887  -5.771  -7.905  1.00 14.29 ? 252 PHE A CZ  1 
ATOM   2001 N  N   . ASP A 1 253 ? 18.125  -0.068  -11.347 1.00 14.18 ? 253 ASP A N   1 
ATOM   2002 C  CA  . ASP A 1 253 ? 19.193  0.922   -11.525 1.00 15.47 ? 253 ASP A CA  1 
ATOM   2003 C  C   . ASP A 1 253 ? 20.540  0.245   -11.251 1.00 17.17 ? 253 ASP A C   1 
ATOM   2004 O  O   . ASP A 1 253 ? 21.412  0.823   -10.600 1.00 16.37 ? 253 ASP A O   1 
ATOM   2005 C  CB  . ASP A 1 253 ? 19.007  2.177   -10.636 1.00 16.24 ? 253 ASP A CB  1 
ATOM   2006 C  CG  . ASP A 1 253 ? 17.799  3.071   -10.946 1.00 17.79 ? 253 ASP A CG  1 
ATOM   2007 O  OD1 . ASP A 1 253 ? 17.288  3.026   -12.089 1.00 16.56 ? 253 ASP A OD1 1 
ATOM   2008 O  OD2 . ASP A 1 253 ? 17.353  3.827   -10.030 1.00 18.67 ? 253 ASP A OD2 1 
ATOM   2009 N  N   . GLU A 1 254 ? 20.672  -1.012  -11.715 1.00 19.35 ? 254 GLU A N   1 
ATOM   2010 C  CA  . GLU A 1 254 ? 21.902  -1.797  -11.717 1.00 21.14 ? 254 GLU A CA  1 
ATOM   2011 C  C   . GLU A 1 254 ? 22.276  -2.289  -10.311 1.00 20.68 ? 254 GLU A C   1 
ATOM   2012 O  O   . GLU A 1 254 ? 23.409  -2.725  -10.106 1.00 18.48 ? 254 GLU A O   1 
ATOM   2013 C  CB  . GLU A 1 254 ? 23.057  -0.996  -12.325 1.00 26.07 ? 254 GLU A CB  1 
ATOM   2014 C  CG  . GLU A 1 254 ? 23.085  -0.919  -13.844 1.00 29.75 ? 254 GLU A CG  1 
ATOM   2015 C  CD  . GLU A 1 254 ? 24.246  -0.036  -14.302 1.00 37.60 ? 254 GLU A CD  1 
ATOM   2016 O  OE1 . GLU A 1 254 ? 24.063  1.211   -14.349 1.00 38.29 ? 254 GLU A OE1 1 
ATOM   2017 O  OE2 . GLU A 1 254 ? 25.357  -0.583  -14.558 1.00 39.76 ? 254 GLU A OE2 1 
ATOM   2018 N  N   . ARG A 1 255 ? 21.340  -2.235  -9.342  1.00 17.98 ? 255 ARG A N   1 
ATOM   2019 C  CA  . ARG A 1 255 ? 21.656  -2.709  -7.999  1.00 17.63 ? 255 ARG A CA  1 
ATOM   2020 C  C   . ARG A 1 255 ? 21.512  -4.227  -7.939  1.00 16.95 ? 255 ARG A C   1 
ATOM   2021 O  O   . ARG A 1 255 ? 20.669  -4.788  -8.642  1.00 18.61 ? 255 ARG A O   1 
ATOM   2022 C  CB  . ARG A 1 255 ? 20.687  -2.156  -6.945  1.00 15.97 ? 255 ARG A CB  1 
ATOM   2023 C  CG  . ARG A 1 255 ? 20.923  -0.703  -6.558  1.00 16.03 ? 255 ARG A CG  1 
ATOM   2024 C  CD  . ARG A 1 255 ? 19.715  -0.224  -5.761  1.00 15.95 ? 255 ARG A CD  1 
ATOM   2025 N  NE  . ARG A 1 255 ? 18.497  -0.010  -6.555  1.00 15.28 ? 255 ARG A NE  1 
ATOM   2026 C  CZ  . ARG A 1 255 ? 17.358  0.484   -6.075  1.00 13.99 ? 255 ARG A CZ  1 
ATOM   2027 N  NH1 . ARG A 1 255 ? 17.242  0.784   -4.788  1.00 14.06 ? 255 ARG A NH1 1 
ATOM   2028 N  NH2 . ARG A 1 255 ? 16.342  0.671   -6.888  1.00 12.01 ? 255 ARG A NH2 1 
ATOM   2029 N  N   . LEU A 1 256 ? 22.304  -4.842  -7.050  1.00 16.27 ? 256 LEU A N   1 
ATOM   2030 C  CA  . LEU A 1 256 ? 22.065  -6.179  -6.529  1.00 17.29 ? 256 LEU A CA  1 
ATOM   2031 C  C   . LEU A 1 256 ? 21.486  -6.081  -5.110  1.00 17.42 ? 256 LEU A C   1 
ATOM   2032 O  O   . LEU A 1 256 ? 21.648  -5.083  -4.395  1.00 15.44 ? 256 LEU A O   1 
ATOM   2033 C  CB  . LEU A 1 256 ? 23.397  -6.941  -6.492  1.00 20.33 ? 256 LEU A CB  1 
ATOM   2034 C  CG  . LEU A 1 256 ? 23.750  -7.871  -7.665  1.00 23.46 ? 256 LEU A CG  1 
ATOM   2035 C  CD1 . LEU A 1 256 ? 22.867  -7.691  -8.897  1.00 22.52 ? 256 LEU A CD1 1 
ATOM   2036 C  CD2 . LEU A 1 256 ? 25.226  -7.771  -8.021  1.00 22.71 ? 256 LEU A CD2 1 
ATOM   2037 N  N   . VAL A 1 257 ? 20.763  -7.134  -4.721  1.00 15.14 ? 257 VAL A N   1 
ATOM   2038 C  CA  . VAL A 1 257 ? 20.315  -7.309  -3.353  1.00 14.72 ? 257 VAL A CA  1 
ATOM   2039 C  C   . VAL A 1 257 ? 21.144  -8.459  -2.789  1.00 14.49 ? 257 VAL A C   1 
ATOM   2040 O  O   . VAL A 1 257 ? 21.268  -9.504  -3.437  1.00 13.76 ? 257 VAL A O   1 
ATOM   2041 C  CB  . VAL A 1 257 ? 18.801  -7.624  -3.300  1.00 14.27 ? 257 VAL A CB  1 
ATOM   2042 C  CG1 . VAL A 1 257 ? 18.290  -7.796  -1.875  1.00 14.35 ? 257 VAL A CG1 1 
ATOM   2043 C  CG2 . VAL A 1 257 ? 17.975  -6.565  -4.016  1.00 13.62 ? 257 VAL A CG2 1 
ATOM   2044 N  N   . TYR A 1 258 ? 21.674  -8.268  -1.574  1.00 13.92 ? 258 TYR A N   1 
ATOM   2045 C  CA  . TYR A 1 258 ? 22.506  -9.281  -0.938  1.00 13.99 ? 258 TYR A CA  1 
ATOM   2046 C  C   . TYR A 1 258 ? 21.687  -10.043 0.086   1.00 13.68 ? 258 TYR A C   1 
ATOM   2047 O  O   . TYR A 1 258 ? 20.806  -9.478  0.721   1.00 13.88 ? 258 TYR A O   1 
ATOM   2048 C  CB  . TYR A 1 258 ? 23.765  -8.614  -0.385  1.00 15.32 ? 258 TYR A CB  1 
ATOM   2049 C  CG  . TYR A 1 258 ? 24.495  -7.879  -1.476  1.00 16.44 ? 258 TYR A CG  1 
ATOM   2050 C  CD1 . TYR A 1 258 ? 24.190  -6.559  -1.763  1.00 18.68 ? 258 TYR A CD1 1 
ATOM   2051 C  CD2 . TYR A 1 258 ? 25.389  -8.540  -2.306  1.00 18.23 ? 258 TYR A CD2 1 
ATOM   2052 C  CE1 . TYR A 1 258 ? 24.807  -5.896  -2.810  1.00 20.48 ? 258 TYR A CE1 1 
ATOM   2053 C  CE2 . TYR A 1 258 ? 26.041  -7.888  -3.342  1.00 19.51 ? 258 TYR A CE2 1 
ATOM   2054 C  CZ  . TYR A 1 258 ? 25.745  -6.559  -3.585  1.00 21.05 ? 258 TYR A CZ  1 
ATOM   2055 O  OH  . TYR A 1 258 ? 26.340  -5.890  -4.606  1.00 24.01 ? 258 TYR A OH  1 
ATOM   2056 N  N   . THR A 1 259 ? 21.955  -11.342 0.219   1.00 13.26 ? 259 THR A N   1 
ATOM   2057 C  CA  . THR A 1 259 ? 21.155  -12.130 1.138   1.00 12.64 ? 259 THR A CA  1 
ATOM   2058 C  C   . THR A 1 259 ? 22.099  -12.778 2.142   1.00 12.52 ? 259 THR A C   1 
ATOM   2059 O  O   . THR A 1 259 ? 23.220  -13.115 1.768   1.00 11.25 ? 259 THR A O   1 
ATOM   2060 C  CB  . THR A 1 259 ? 20.263  -13.133 0.395   1.00 12.98 ? 259 THR A CB  1 
ATOM   2061 O  OG1 . THR A 1 259 ? 21.113  -14.059 -0.285  1.00 12.74 ? 259 THR A OG1 1 
ATOM   2062 C  CG2 . THR A 1 259 ? 19.310  -12.439 -0.559  1.00 12.55 ? 259 THR A CG2 1 
ATOM   2063 N  N   . SER A 1 260 ? 21.617  -12.943 3.386   1.00 11.59 ? 260 SER A N   1 
ATOM   2064 C  CA  . SER A 1 260 ? 22.386  -13.595 4.428   1.00 12.77 ? 260 SER A CA  1 
ATOM   2065 C  C   . SER A 1 260 ? 22.123  -15.103 4.405   1.00 14.51 ? 260 SER A C   1 
ATOM   2066 O  O   . SER A 1 260 ? 22.711  -15.842 5.197   1.00 16.10 ? 260 SER A O   1 
ATOM   2067 C  CB  . SER A 1 260 ? 22.052  -13.003 5.785   1.00 11.33 ? 260 SER A CB  1 
ATOM   2068 O  OG  . SER A 1 260 ? 20.721  -13.326 6.131   1.00 10.68 ? 260 SER A OG  1 
ATOM   2069 N  N   . PHE A 1 261 ? 21.231  -15.552 3.516   1.00 15.31 ? 261 PHE A N   1 
ATOM   2070 C  CA  . PHE A 1 261 ? 20.888  -16.964 3.367   1.00 17.94 ? 261 PHE A CA  1 
ATOM   2071 C  C   . PHE A 1 261 ? 21.025  -17.352 1.889   1.00 18.32 ? 261 PHE A C   1 
ATOM   2072 O  O   . PHE A 1 261 ? 21.069  -16.481 1.011   1.00 16.55 ? 261 PHE A O   1 
ATOM   2073 C  CB  . PHE A 1 261 ? 19.452  -17.220 3.855   1.00 17.52 ? 261 PHE A CB  1 
ATOM   2074 C  CG  . PHE A 1 261 ? 18.450  -16.430 3.049   1.00 18.26 ? 261 PHE A CG  1 
ATOM   2075 C  CD1 . PHE A 1 261 ? 17.929  -16.932 1.861   1.00 17.68 ? 261 PHE A CD1 1 
ATOM   2076 C  CD2 . PHE A 1 261 ? 18.138  -15.124 3.405   1.00 17.41 ? 261 PHE A CD2 1 
ATOM   2077 C  CE1 . PHE A 1 261 ? 17.066  -16.163 1.086   1.00 19.01 ? 261 PHE A CE1 1 
ATOM   2078 C  CE2 . PHE A 1 261 ? 17.267  -14.364 2.636   1.00 16.61 ? 261 PHE A CE2 1 
ATOM   2079 C  CZ  . PHE A 1 261 ? 16.732  -14.879 1.481   1.00 17.60 ? 261 PHE A CZ  1 
ATOM   2080 N  N   . SER A 1 262 ? 21.061  -18.665 1.620   1.00 21.24 ? 262 SER A N   1 
ATOM   2081 C  CA  . SER A 1 262 ? 21.249  -19.178 0.262   1.00 29.37 ? 262 SER A CA  1 
ATOM   2082 C  C   . SER A 1 262 ? 19.968  -19.787 -0.317  1.00 33.77 ? 262 SER A C   1 
ATOM   2083 O  O   . SER A 1 262 ? 19.295  -20.606 0.309   1.00 39.82 ? 262 SER A O   1 
ATOM   2084 C  CB  . SER A 1 262 ? 22.441  -20.102 0.147   1.00 30.49 ? 262 SER A CB  1 
ATOM   2085 O  OG  . SER A 1 262 ? 22.370  -21.105 1.149   1.00 28.53 ? 262 SER A OG  1 
ATOM   2086 N  N   . GLN A 1 263 ? 19.687  -19.376 -1.561  1.00 44.21 ? 263 GLN A N   1 
ATOM   2087 C  CA  . GLN A 1 263 ? 18.371  -19.347 -2.184  1.00 48.08 ? 263 GLN A CA  1 
ATOM   2088 C  C   . GLN A 1 263 ? 18.352  -20.334 -3.356  1.00 52.86 ? 263 GLN A C   1 
ATOM   2089 O  O   . GLN A 1 263 ? 17.565  -21.284 -3.395  1.00 56.99 ? 263 GLN A O   1 
ATOM   2090 C  CB  . GLN A 1 263 ? 18.066  -17.953 -2.761  1.00 43.30 ? 263 GLN A CB  1 
ATOM   2091 C  CG  . GLN A 1 263 ? 18.873  -16.797 -2.170  1.00 41.87 ? 263 GLN A CG  1 
ATOM   2092 C  CD  . GLN A 1 263 ? 20.140  -16.409 -2.908  1.00 42.77 ? 263 GLN A CD  1 
ATOM   2093 O  OE1 . GLN A 1 263 ? 20.859  -17.229 -3.487  1.00 39.75 ? 263 GLN A OE1 1 
ATOM   2094 N  NE2 . GLN A 1 263 ? 20.453  -15.125 -2.870  1.00 43.25 ? 263 GLN A NE2 1 
ATOM   2095 O  OXT . GLN A 1 263 ? 19.148  -20.175 -4.285  1.00 49.34 ? 263 GLN A OXT 1 
ATOM   2096 N  N   . LYS B 1 3   ? 12.484  15.438  -24.038 1.00 38.68 ? 3   LYS B N   1 
ATOM   2097 C  CA  . LYS B 1 3   ? 12.995  14.046  -23.839 1.00 38.39 ? 3   LYS B CA  1 
ATOM   2098 C  C   . LYS B 1 3   ? 12.333  13.408  -22.620 1.00 35.06 ? 3   LYS B C   1 
ATOM   2099 O  O   . LYS B 1 3   ? 11.821  14.082  -21.720 1.00 36.98 ? 3   LYS B O   1 
ATOM   2100 C  CB  . LYS B 1 3   ? 14.521  13.971  -23.684 1.00 42.84 ? 3   LYS B CB  1 
ATOM   2101 N  N   . TRP B 1 4   ? 12.345  12.078  -22.651 1.00 24.00 ? 4   TRP B N   1 
ATOM   2102 C  CA  . TRP B 1 4   ? 11.975  11.226  -21.542 1.00 19.04 ? 4   TRP B CA  1 
ATOM   2103 C  C   . TRP B 1 4   ? 12.753  9.940   -21.760 1.00 16.59 ? 4   TRP B C   1 
ATOM   2104 O  O   . TRP B 1 4   ? 13.130  9.670   -22.894 1.00 16.99 ? 4   TRP B O   1 
ATOM   2105 C  CB  . TRP B 1 4   ? 10.458  10.993  -21.538 1.00 14.78 ? 4   TRP B CB  1 
ATOM   2106 C  CG  . TRP B 1 4   ? 9.917   10.369  -22.792 1.00 13.54 ? 4   TRP B CG  1 
ATOM   2107 C  CD1 . TRP B 1 4   ? 9.502   11.012  -23.926 1.00 13.01 ? 4   TRP B CD1 1 
ATOM   2108 C  CD2 . TRP B 1 4   ? 9.734   8.959   -23.042 1.00 13.02 ? 4   TRP B CD2 1 
ATOM   2109 N  NE1 . TRP B 1 4   ? 9.068   10.101  -24.855 1.00 12.22 ? 4   TRP B NE1 1 
ATOM   2110 C  CE2 . TRP B 1 4   ? 9.190   8.835   -24.337 1.00 12.49 ? 4   TRP B CE2 1 
ATOM   2111 C  CE3 . TRP B 1 4   ? 9.956   7.792   -22.293 1.00 12.75 ? 4   TRP B CE3 1 
ATOM   2112 C  CZ2 . TRP B 1 4   ? 8.892   7.597   -24.907 1.00 12.03 ? 4   TRP B CZ2 1 
ATOM   2113 C  CZ3 . TRP B 1 4   ? 9.629   6.572   -22.849 1.00 12.28 ? 4   TRP B CZ3 1 
ATOM   2114 C  CH2 . TRP B 1 4   ? 9.104   6.471   -24.142 1.00 11.54 ? 4   TRP B CH2 1 
ATOM   2115 N  N   . THR B 1 5   ? 12.976  9.177   -20.685 1.00 17.27 ? 5   THR B N   1 
ATOM   2116 C  CA  . THR B 1 5   ? 13.756  7.950   -20.696 1.00 16.90 ? 5   THR B CA  1 
ATOM   2117 C  C   . THR B 1 5   ? 13.156  6.984   -19.675 1.00 17.39 ? 5   THR B C   1 
ATOM   2118 O  O   . THR B 1 5   ? 12.162  7.289   -19.024 1.00 17.80 ? 5   THR B O   1 
ATOM   2119 C  CB  . THR B 1 5   ? 15.222  8.236   -20.329 1.00 16.73 ? 5   THR B CB  1 
ATOM   2120 O  OG1 . THR B 1 5   ? 15.233  8.593   -18.954 1.00 15.75 ? 5   THR B OG1 1 
ATOM   2121 C  CG2 . THR B 1 5   ? 15.840  9.396   -21.082 1.00 17.29 ? 5   THR B CG2 1 
ATOM   2122 N  N   . TYR B 1 6   ? 13.817  5.842   -19.486 1.00 17.58 ? 6   TYR B N   1 
ATOM   2123 C  CA  . TYR B 1 6   ? 13.412  4.850   -18.506 1.00 18.79 ? 6   TYR B CA  1 
ATOM   2124 C  C   . TYR B 1 6   ? 14.429  4.761   -17.372 1.00 22.18 ? 6   TYR B C   1 
ATOM   2125 O  O   . TYR B 1 6   ? 14.523  3.727   -16.711 1.00 24.92 ? 6   TYR B O   1 
ATOM   2126 C  CB  . TYR B 1 6   ? 13.320  3.472   -19.161 1.00 16.44 ? 6   TYR B CB  1 
ATOM   2127 C  CG  . TYR B 1 6   ? 12.176  3.316   -20.131 1.00 15.68 ? 6   TYR B CG  1 
ATOM   2128 C  CD1 . TYR B 1 6   ? 10.924  2.921   -19.688 1.00 15.32 ? 6   TYR B CD1 1 
ATOM   2129 C  CD2 . TYR B 1 6   ? 12.341  3.544   -21.493 1.00 14.73 ? 6   TYR B CD2 1 
ATOM   2130 C  CE1 . TYR B 1 6   ? 9.867   2.756   -20.565 1.00 14.61 ? 6   TYR B CE1 1 
ATOM   2131 C  CE2 . TYR B 1 6   ? 11.294  3.361   -22.384 1.00 14.60 ? 6   TYR B CE2 1 
ATOM   2132 C  CZ  . TYR B 1 6   ? 10.053  2.962   -21.915 1.00 14.38 ? 6   TYR B CZ  1 
ATOM   2133 O  OH  . TYR B 1 6   ? 8.983   2.774   -22.748 1.00 14.93 ? 6   TYR B OH  1 
ATOM   2134 N  N   . PHE B 1 7   ? 15.207  5.827   -17.160 1.00 25.80 ? 7   PHE B N   1 
ATOM   2135 C  CA  . PHE B 1 7   ? 16.162  5.829   -16.062 1.00 31.43 ? 7   PHE B CA  1 
ATOM   2136 C  C   . PHE B 1 7   ? 16.665  7.238   -15.761 1.00 31.71 ? 7   PHE B C   1 
ATOM   2137 O  O   . PHE B 1 7   ? 16.673  8.117   -16.626 1.00 30.34 ? 7   PHE B O   1 
ATOM   2138 C  CB  . PHE B 1 7   ? 17.302  4.837   -16.322 1.00 41.82 ? 7   PHE B CB  1 
ATOM   2139 C  CG  . PHE B 1 7   ? 18.370  5.258   -17.302 1.00 50.62 ? 7   PHE B CG  1 
ATOM   2140 C  CD1 . PHE B 1 7   ? 18.211  6.366   -18.124 1.00 54.26 ? 7   PHE B CD1 1 
ATOM   2141 C  CD2 . PHE B 1 7   ? 19.536  4.511   -17.419 1.00 59.73 ? 7   PHE B CD2 1 
ATOM   2142 C  CE1 . PHE B 1 7   ? 19.199  6.737   -19.023 1.00 58.50 ? 7   PHE B CE1 1 
ATOM   2143 C  CE2 . PHE B 1 7   ? 20.524  4.872   -18.323 1.00 64.85 ? 7   PHE B CE2 1 
ATOM   2144 C  CZ  . PHE B 1 7   ? 20.349  5.983   -19.121 1.00 66.97 ? 7   PHE B CZ  1 
ATOM   2145 N  N   . GLY B 1 8   ? 17.103  7.437   -14.520 1.00 30.01 ? 8   GLY B N   1 
ATOM   2146 C  CA  . GLY B 1 8   ? 17.774  8.679   -14.175 1.00 30.49 ? 8   GLY B CA  1 
ATOM   2147 C  C   . GLY B 1 8   ? 16.724  9.759   -13.953 1.00 30.53 ? 8   GLY B C   1 
ATOM   2148 O  O   . GLY B 1 8   ? 15.552  9.426   -13.771 1.00 33.62 ? 8   GLY B O   1 
ATOM   2149 N  N   . PRO B 1 9   ? 17.091  11.060  -13.989 1.00 29.64 ? 9   PRO B N   1 
ATOM   2150 C  CA  . PRO B 1 9   ? 16.140  12.138  -13.688 1.00 27.67 ? 9   PRO B CA  1 
ATOM   2151 C  C   . PRO B 1 9   ? 14.937  12.244  -14.626 1.00 25.08 ? 9   PRO B C   1 
ATOM   2152 O  O   . PRO B 1 9   ? 13.902  12.782  -14.249 1.00 26.30 ? 9   PRO B O   1 
ATOM   2153 C  CB  . PRO B 1 9   ? 16.981  13.428  -13.799 1.00 29.43 ? 9   PRO B CB  1 
ATOM   2154 C  CG  . PRO B 1 9   ? 18.433  12.965  -13.746 1.00 31.01 ? 9   PRO B CG  1 
ATOM   2155 C  CD  . PRO B 1 9   ? 18.442  11.559  -14.312 1.00 29.72 ? 9   PRO B CD  1 
ATOM   2156 N  N   . ASP B 1 10  ? 15.056  11.725  -15.853 1.00 22.52 ? 10  ASP B N   1 
ATOM   2157 C  CA  . ASP B 1 10  ? 14.002  11.923  -16.837 1.00 20.17 ? 10  ASP B CA  1 
ATOM   2158 C  C   . ASP B 1 10  ? 13.186  10.644  -17.002 1.00 17.66 ? 10  ASP B C   1 
ATOM   2159 O  O   . ASP B 1 10  ? 12.497  10.472  -18.015 1.00 15.89 ? 10  ASP B O   1 
ATOM   2160 C  CB  . ASP B 1 10  ? 14.592  12.395  -18.168 1.00 22.37 ? 10  ASP B CB  1 
ATOM   2161 C  CG  . ASP B 1 10  ? 15.082  13.833  -18.109 1.00 26.17 ? 10  ASP B CG  1 
ATOM   2162 O  OD1 . ASP B 1 10  ? 14.426  14.661  -17.432 1.00 27.63 ? 10  ASP B OD1 1 
ATOM   2163 O  OD2 . ASP B 1 10  ? 16.115  14.112  -18.725 1.00 28.08 ? 10  ASP B OD2 1 
ATOM   2164 N  N   . GLY B 1 11  ? 13.297  9.763   -15.999 1.00 15.56 ? 11  GLY B N   1 
ATOM   2165 C  CA  . GLY B 1 11  ? 12.709  8.432   -16.025 1.00 12.58 ? 11  GLY B CA  1 
ATOM   2166 C  C   . GLY B 1 11  ? 11.235  8.517   -15.664 1.00 10.74 ? 11  GLY B C   1 
ATOM   2167 O  O   . GLY B 1 11  ? 10.704  9.614   -15.486 1.00 10.15 ? 11  GLY B O   1 
ATOM   2168 N  N   . GLU B 1 12  ? 10.610  7.347   -15.521 1.00 9.69  ? 12  GLU B N   1 
ATOM   2169 C  CA  . GLU B 1 12  ? 9.160   7.209   -15.470 1.00 8.82  ? 12  GLU B CA  1 
ATOM   2170 C  C   . GLU B 1 12  ? 8.534   7.952   -14.289 1.00 8.38  ? 12  GLU B C   1 
ATOM   2171 O  O   . GLU B 1 12  ? 7.393   8.375   -14.414 1.00 8.48  ? 12  GLU B O   1 
ATOM   2172 C  CB  . GLU B 1 12  ? 8.728   5.739   -15.530 1.00 8.76  ? 12  GLU B CB  1 
ATOM   2173 C  CG  . GLU B 1 12  ? 9.051   4.945   -14.268 1.00 8.97  ? 12  GLU B CG  1 
ATOM   2174 C  CD  . GLU B 1 12  ? 9.002   3.445   -14.538 1.00 9.66  ? 12  GLU B CD  1 
ATOM   2175 O  OE1 . GLU B 1 12  ? 7.927   2.867   -14.505 1.00 9.23  ? 12  GLU B OE1 1 
ATOM   2176 O  OE2 . GLU B 1 12  ? 10.043  2.878   -14.859 1.00 10.70 ? 12  GLU B OE2 1 
ATOM   2177 N  N   . ASN B 1 13  ? 9.252   8.115   -13.165 1.00 8.45  ? 13  ASN B N   1 
ATOM   2178 C  CA  . ASN B 1 13  ? 8.688   8.818   -12.022 1.00 8.62  ? 13  ASN B CA  1 
ATOM   2179 C  C   . ASN B 1 13  ? 8.568   10.320  -12.317 1.00 9.09  ? 13  ASN B C   1 
ATOM   2180 O  O   . ASN B 1 13  ? 7.826   11.000  -11.628 1.00 8.65  ? 13  ASN B O   1 
ATOM   2181 C  CB  . ASN B 1 13  ? 9.449   8.535   -10.727 1.00 9.03  ? 13  ASN B CB  1 
ATOM   2182 C  CG  . ASN B 1 13  ? 9.307   7.106   -10.216 1.00 9.49  ? 13  ASN B CG  1 
ATOM   2183 O  OD1 . ASN B 1 13  ? 8.474   6.332   -10.701 1.00 10.03 ? 13  ASN B OD1 1 
ATOM   2184 N  ND2 . ASN B 1 13  ? 10.059  6.766   -9.184  1.00 9.67  ? 13  ASN B ND2 1 
ATOM   2185 N  N   . SER B 1 14  ? 9.250   10.805  -13.371 1.00 9.37  ? 14  SER B N   1 
ATOM   2186 C  CA  . SER B 1 14  ? 9.355   12.219  -13.713 1.00 9.97  ? 14  SER B CA  1 
ATOM   2187 C  C   . SER B 1 14  ? 8.496   12.591  -14.927 1.00 9.95  ? 14  SER B C   1 
ATOM   2188 O  O   . SER B 1 14  ? 8.367   13.773  -15.241 1.00 10.03 ? 14  SER B O   1 
ATOM   2189 C  CB  . SER B 1 14  ? 10.806  12.618  -13.953 1.00 10.52 ? 14  SER B CB  1 
ATOM   2190 O  OG  . SER B 1 14  ? 11.563  12.557  -12.739 1.00 11.88 ? 14  SER B OG  1 
ATOM   2191 N  N   . TRP B 1 15  ? 7.960   11.590  -15.641 1.00 9.91  ? 15  TRP B N   1 
ATOM   2192 C  CA  . TRP B 1 15  ? 7.180   11.821  -16.857 1.00 9.68  ? 15  TRP B CA  1 
ATOM   2193 C  C   . TRP B 1 15  ? 6.027   12.802  -16.635 1.00 9.90  ? 15  TRP B C   1 
ATOM   2194 O  O   . TRP B 1 15  ? 5.695   13.600  -17.535 1.00 10.07 ? 15  TRP B O   1 
ATOM   2195 C  CB  . TRP B 1 15  ? 6.632   10.503  -17.443 1.00 9.79  ? 15  TRP B CB  1 
ATOM   2196 C  CG  . TRP B 1 15  ? 7.629   9.533   -18.004 1.00 9.67  ? 15  TRP B CG  1 
ATOM   2197 C  CD1 . TRP B 1 15  ? 8.964   9.729   -18.243 1.00 10.30 ? 15  TRP B CD1 1 
ATOM   2198 C  CD2 . TRP B 1 15  ? 7.338   8.194   -18.459 1.00 9.54  ? 15  TRP B CD2 1 
ATOM   2199 N  NE1 . TRP B 1 15  ? 9.525   8.590   -18.772 1.00 9.54  ? 15  TRP B NE1 1 
ATOM   2200 C  CE2 . TRP B 1 15  ? 8.558   7.628   -18.890 1.00 9.85  ? 15  TRP B CE2 1 
ATOM   2201 C  CE3 . TRP B 1 15  ? 6.176   7.415   -18.498 1.00 9.40  ? 15  TRP B CE3 1 
ATOM   2202 C  CZ2 . TRP B 1 15  ? 8.635   6.333   -19.415 1.00 10.27 ? 15  TRP B CZ2 1 
ATOM   2203 C  CZ3 . TRP B 1 15  ? 6.250   6.133   -19.003 1.00 9.57  ? 15  TRP B CZ3 1 
ATOM   2204 C  CH2 . TRP B 1 15  ? 7.466   5.604   -19.448 1.00 10.46 ? 15  TRP B CH2 1 
ATOM   2205 N  N   . SER B 1 16  ? 5.384   12.711  -15.464 1.00 8.99  ? 16  SER B N   1 
ATOM   2206 C  CA  . SER B 1 16  ? 4.157   13.452  -15.224 1.00 9.40  ? 16  SER B CA  1 
ATOM   2207 C  C   . SER B 1 16  ? 4.406   14.968  -15.220 1.00 10.31 ? 16  SER B C   1 
ATOM   2208 O  O   . SER B 1 16  ? 3.467   15.742  -15.340 1.00 11.23 ? 16  SER B O   1 
ATOM   2209 C  CB  . SER B 1 16  ? 3.586   13.025  -13.909 1.00 9.31  ? 16  SER B CB  1 
ATOM   2210 O  OG  . SER B 1 16  ? 4.553   13.288  -12.888 1.00 8.97  ? 16  SER B OG  1 
ATOM   2211 N  N   . LYS B 1 17  ? 5.654   15.400  -15.049 1.00 11.18 ? 17  LYS B N   1 
ATOM   2212 C  CA  . LYS B 1 17  ? 5.971   16.818  -14.937 1.00 12.98 ? 17  LYS B CA  1 
ATOM   2213 C  C   . LYS B 1 17  ? 5.551   17.548  -16.214 1.00 13.01 ? 17  LYS B C   1 
ATOM   2214 O  O   . LYS B 1 17  ? 4.961   18.637  -16.163 1.00 11.88 ? 17  LYS B O   1 
ATOM   2215 C  CB  . LYS B 1 17  ? 7.490   16.994  -14.787 1.00 14.91 ? 17  LYS B CB  1 
ATOM   2216 C  CG  . LYS B 1 17  ? 8.086   16.565  -13.451 1.00 17.15 ? 17  LYS B CG  1 
ATOM   2217 C  CD  . LYS B 1 17  ? 9.610   16.789  -13.381 1.00 20.96 ? 17  LYS B CD  1 
ATOM   2218 C  CE  . LYS B 1 17  ? 10.267  16.079  -12.213 1.00 21.40 ? 17  LYS B CE  1 
ATOM   2219 N  NZ  . LYS B 1 17  ? 11.707  15.825  -12.452 1.00 23.94 ? 17  LYS B NZ  1 
ATOM   2220 N  N   . LYS B 1 18  ? 5.860   16.916  -17.354 1.00 12.85 ? 18  LYS B N   1 
ATOM   2221 C  CA  . LYS B 1 18  ? 5.689   17.497  -18.682 1.00 13.58 ? 18  LYS B CA  1 
ATOM   2222 C  C   . LYS B 1 18  ? 4.538   16.819  -19.432 1.00 13.30 ? 18  LYS B C   1 
ATOM   2223 O  O   . LYS B 1 18  ? 3.995   17.388  -20.386 1.00 11.49 ? 18  LYS B O   1 
ATOM   2224 C  CB  . LYS B 1 18  ? 7.013   17.423  -19.458 1.00 13.56 ? 18  LYS B CB  1 
ATOM   2225 N  N   . TYR B 1 19  ? 4.180   15.597  -18.997 1.00 13.41 ? 19  TYR B N   1 
ATOM   2226 C  CA  . TYR B 1 19  ? 3.109   14.829  -19.608 1.00 12.58 ? 19  TYR B CA  1 
ATOM   2227 C  C   . TYR B 1 19  ? 2.079   14.469  -18.537 1.00 13.53 ? 19  TYR B C   1 
ATOM   2228 O  O   . TYR B 1 19  ? 2.067   13.355  -17.993 1.00 13.32 ? 19  TYR B O   1 
ATOM   2229 C  CB  . TYR B 1 19  ? 3.674   13.578  -20.296 1.00 12.61 ? 19  TYR B CB  1 
ATOM   2230 C  CG  . TYR B 1 19  ? 4.726   13.833  -21.348 1.00 13.13 ? 19  TYR B CG  1 
ATOM   2231 C  CD1 . TYR B 1 19  ? 6.078   13.756  -21.045 1.00 13.49 ? 19  TYR B CD1 1 
ATOM   2232 C  CD2 . TYR B 1 19  ? 4.374   14.089  -22.666 1.00 13.21 ? 19  TYR B CD2 1 
ATOM   2233 C  CE1 . TYR B 1 19  ? 7.051   13.966  -22.012 1.00 13.27 ? 19  TYR B CE1 1 
ATOM   2234 C  CE2 . TYR B 1 19  ? 5.334   14.298  -23.649 1.00 13.98 ? 19  TYR B CE2 1 
ATOM   2235 C  CZ  . TYR B 1 19  ? 6.675   14.235  -23.318 1.00 14.15 ? 19  TYR B CZ  1 
ATOM   2236 O  OH  . TYR B 1 19  ? 7.617   14.431  -24.286 1.00 14.81 ? 19  TYR B OH  1 
ATOM   2237 N  N   . PRO B 1 20  ? 1.177   15.403  -18.183 1.00 13.93 ? 20  PRO B N   1 
ATOM   2238 C  CA  . PRO B 1 20  ? 0.333   15.227  -17.000 1.00 14.17 ? 20  PRO B CA  1 
ATOM   2239 C  C   . PRO B 1 20  ? -0.451  13.915  -16.907 1.00 13.83 ? 20  PRO B C   1 
ATOM   2240 O  O   . PRO B 1 20  ? -0.526  13.339  -15.816 1.00 14.18 ? 20  PRO B O   1 
ATOM   2241 C  CB  . PRO B 1 20  ? -0.541  16.499  -16.955 1.00 14.28 ? 20  PRO B CB  1 
ATOM   2242 C  CG  . PRO B 1 20  ? 0.198   17.514  -17.827 1.00 15.18 ? 20  PRO B CG  1 
ATOM   2243 C  CD  . PRO B 1 20  ? 1.000   16.715  -18.835 1.00 14.74 ? 20  PRO B CD  1 
ATOM   2244 N  N   . SER B 1 21  ? -0.968  13.406  -18.043 1.00 12.29 ? 21  SER B N   1 
ATOM   2245 C  CA  . SER B 1 21  ? -1.682  12.128  -18.062 1.00 12.07 ? 21  SER B CA  1 
ATOM   2246 C  C   . SER B 1 21  ? -0.910  10.990  -17.391 1.00 11.29 ? 21  SER B C   1 
ATOM   2247 O  O   . SER B 1 21  ? -1.513  10.015  -16.947 1.00 12.22 ? 21  SER B O   1 
ATOM   2248 C  CB  . SER B 1 21  ? -2.089  11.718  -19.466 1.00 11.70 ? 21  SER B CB  1 
ATOM   2249 O  OG  . SER B 1 21  ? -3.193  12.496  -19.898 1.00 11.39 ? 21  SER B OG  1 
ATOM   2250 N  N   . CYS B 1 22  ? 0.416   11.073  -17.380 1.00 10.49 ? 22  CYS B N   1 
ATOM   2251 C  CA  . CYS B 1 22  ? 1.238   10.001  -16.827 1.00 10.58 ? 22  CYS B CA  1 
ATOM   2252 C  C   . CYS B 1 22  ? 1.027   9.881   -15.314 1.00 10.25 ? 22  CYS B C   1 
ATOM   2253 O  O   . CYS B 1 22  ? 1.362   8.856   -14.725 1.00 9.86  ? 22  CYS B O   1 
ATOM   2254 C  CB  . CYS B 1 22  ? 2.725   10.223  -17.132 1.00 9.63  ? 22  CYS B CB  1 
ATOM   2255 S  SG  . CYS B 1 22  ? 3.158   10.164  -18.900 1.00 9.24  ? 22  CYS B SG  1 
ATOM   2256 N  N   . GLY B 1 23  ? 0.508   10.943  -14.679 1.00 11.11 ? 23  GLY B N   1 
ATOM   2257 C  CA  . GLY B 1 23  ? 0.157   10.896  -13.266 1.00 11.27 ? 23  GLY B CA  1 
ATOM   2258 C  C   . GLY B 1 23  ? -1.357  10.845  -13.054 1.00 12.66 ? 23  GLY B C   1 
ATOM   2259 O  O   . GLY B 1 23  ? -1.829  11.010  -11.933 1.00 13.49 ? 23  GLY B O   1 
ATOM   2260 N  N   . GLY B 1 24  ? -2.118  10.602  -14.130 1.00 13.01 ? 24  GLY B N   1 
ATOM   2261 C  CA  . GLY B 1 24  ? -3.572  10.618  -14.090 1.00 14.60 ? 24  GLY B CA  1 
ATOM   2262 C  C   . GLY B 1 24  ? -4.141  9.231   -13.800 1.00 17.14 ? 24  GLY B C   1 
ATOM   2263 O  O   . GLY B 1 24  ? -3.434  8.352   -13.287 1.00 15.88 ? 24  GLY B O   1 
ATOM   2264 N  N   . LEU B 1 25  ? -5.422  9.044   -14.130 1.00 18.58 ? 25  LEU B N   1 
ATOM   2265 C  CA  . LEU B 1 25  ? -6.056  7.746   -13.927 1.00 22.24 ? 25  LEU B CA  1 
ATOM   2266 C  C   . LEU B 1 25  ? -5.858  6.841   -15.149 1.00 21.42 ? 25  LEU B C   1 
ATOM   2267 O  O   . LEU B 1 25  ? -5.349  7.275   -16.197 1.00 20.98 ? 25  LEU B O   1 
ATOM   2268 C  CB  . LEU B 1 25  ? -7.545  7.926   -13.594 1.00 25.95 ? 25  LEU B CB  1 
ATOM   2269 C  CG  . LEU B 1 25  ? -7.881  9.018   -12.570 1.00 28.41 ? 25  LEU B CG  1 
ATOM   2270 C  CD1 . LEU B 1 25  ? -9.308  9.529   -12.756 1.00 29.37 ? 25  LEU B CD1 1 
ATOM   2271 C  CD2 . LEU B 1 25  ? -7.630  8.572   -11.128 1.00 27.40 ? 25  LEU B CD2 1 
ATOM   2272 N  N   . LEU B 1 26  ? -6.285  5.575   -14.976 1.00 18.74 ? 26  LEU B N   1 
ATOM   2273 C  CA  . LEU B 1 26  ? -6.320  4.523   -15.982 1.00 17.69 ? 26  LEU B CA  1 
ATOM   2274 C  C   . LEU B 1 26  ? -4.917  4.250   -16.544 1.00 14.63 ? 26  LEU B C   1 
ATOM   2275 O  O   . LEU B 1 26  ? -4.815  3.965   -17.739 1.00 13.81 ? 26  LEU B O   1 
ATOM   2276 C  CB  . LEU B 1 26  ? -7.269  4.861   -17.146 1.00 17.54 ? 26  LEU B CB  1 
ATOM   2277 C  CG  . LEU B 1 26  ? -8.778  4.624   -17.006 1.00 20.20 ? 26  LEU B CG  1 
ATOM   2278 C  CD1 . LEU B 1 26  ? -9.446  4.564   -18.389 1.00 18.57 ? 26  LEU B CD1 1 
ATOM   2279 C  CD2 . LEU B 1 26  ? -9.126  3.393   -16.206 1.00 18.64 ? 26  LEU B CD2 1 
ATOM   2280 N  N   . GLN B 1 27  ? -3.874  4.226   -15.699 1.00 11.07 ? 27  GLN B N   1 
ATOM   2281 C  CA  . GLN B 1 27  ? -2.538  3.984   -16.234 1.00 10.05 ? 27  GLN B CA  1 
ATOM   2282 C  C   . GLN B 1 27  ? -2.256  2.491   -16.495 1.00 9.57  ? 27  GLN B C   1 
ATOM   2283 O  O   . GLN B 1 27  ? -2.617  1.592   -15.713 1.00 7.96  ? 27  GLN B O   1 
ATOM   2284 C  CB  . GLN B 1 27  ? -1.447  4.661   -15.405 1.00 9.89  ? 27  GLN B CB  1 
ATOM   2285 C  CG  . GLN B 1 27  ? -1.504  6.196   -15.406 1.00 9.70  ? 27  GLN B CG  1 
ATOM   2286 C  CD  . GLN B 1 27  ? -1.156  6.805   -16.751 1.00 9.61  ? 27  GLN B CD  1 
ATOM   2287 O  OE1 . GLN B 1 27  ? 0.005   6.878   -17.149 1.00 9.74  ? 27  GLN B OE1 1 
ATOM   2288 N  NE2 . GLN B 1 27  ? -2.170  7.214   -17.486 1.00 9.26  ? 27  GLN B NE2 1 
ATOM   2289 N  N   . SER B 1 28  ? -1.537  2.255   -17.609 1.00 9.12  ? 28  SER B N   1 
ATOM   2290 C  CA  . SER B 1 28  ? -0.999  0.948   -17.985 1.00 9.26  ? 28  SER B CA  1 
ATOM   2291 C  C   . SER B 1 28  ? 0.528   0.977   -17.896 1.00 9.40  ? 28  SER B C   1 
ATOM   2292 O  O   . SER B 1 28  ? 1.133   2.047   -18.066 1.00 10.12 ? 28  SER B O   1 
ATOM   2293 C  CB  . SER B 1 28  ? -1.426  0.597   -19.393 1.00 8.87  ? 28  SER B CB  1 
ATOM   2294 O  OG  . SER B 1 28  ? -2.841  0.469   -19.505 1.00 8.70  ? 28  SER B OG  1 
ATOM   2295 N  N   . PRO B 1 29  ? 1.235   -0.167  -17.722 1.00 9.34  ? 29  PRO B N   1 
ATOM   2296 C  CA  . PRO B 1 29  ? 0.638   -1.508  -17.708 1.00 9.44  ? 29  PRO B CA  1 
ATOM   2297 C  C   . PRO B 1 29  ? 0.175   -1.875  -16.296 1.00 9.60  ? 29  PRO B C   1 
ATOM   2298 O  O   . PRO B 1 29  ? 0.355   -1.091  -15.381 1.00 9.08  ? 29  PRO B O   1 
ATOM   2299 C  CB  . PRO B 1 29  ? 1.852   -2.374  -18.062 1.00 9.26  ? 29  PRO B CB  1 
ATOM   2300 C  CG  . PRO B 1 29  ? 3.002   -1.688  -17.350 1.00 9.30  ? 29  PRO B CG  1 
ATOM   2301 C  CD  . PRO B 1 29  ? 2.698   -0.211  -17.547 1.00 9.39  ? 29  PRO B CD  1 
ATOM   2302 N  N   . ILE B 1 30  ? -0.435  -3.064  -16.133 1.00 10.07 ? 30  ILE B N   1 
ATOM   2303 C  CA  . ILE B 1 30  ? -0.986  -3.503  -14.860 1.00 10.09 ? 30  ILE B CA  1 
ATOM   2304 C  C   . ILE B 1 30  ? -0.585  -4.960  -14.643 1.00 10.46 ? 30  ILE B C   1 
ATOM   2305 O  O   . ILE B 1 30  ? -0.128  -5.634  -15.570 1.00 9.08  ? 30  ILE B O   1 
ATOM   2306 C  CB  . ILE B 1 30  ? -2.524  -3.345  -14.827 1.00 10.67 ? 30  ILE B CB  1 
ATOM   2307 C  CG1 . ILE B 1 30  ? -3.223  -4.172  -15.914 1.00 10.81 ? 30  ILE B CG1 1 
ATOM   2308 C  CG2 . ILE B 1 30  ? -2.928  -1.872  -14.854 1.00 11.15 ? 30  ILE B CG2 1 
ATOM   2309 C  CD1 . ILE B 1 30  ? -4.730  -4.201  -15.776 1.00 11.10 ? 30  ILE B CD1 1 
ATOM   2310 N  N   . ASP B 1 31  ? -0.770  -5.420  -13.403 1.00 11.46 ? 31  ASP B N   1 
ATOM   2311 C  CA  . ASP B 1 31  ? -0.689  -6.835  -13.063 1.00 11.90 ? 31  ASP B CA  1 
ATOM   2312 C  C   . ASP B 1 31  ? -2.023  -7.505  -13.401 1.00 12.50 ? 31  ASP B C   1 
ATOM   2313 O  O   . ASP B 1 31  ? -3.068  -7.128  -12.860 1.00 12.77 ? 31  ASP B O   1 
ATOM   2314 C  CB  . ASP B 1 31  ? -0.327  -7.036  -11.592 1.00 12.72 ? 31  ASP B CB  1 
ATOM   2315 C  CG  . ASP B 1 31  ? -0.207  -8.506  -11.189 1.00 13.71 ? 31  ASP B CG  1 
ATOM   2316 O  OD1 . ASP B 1 31  ? 0.255   -9.328  -12.022 1.00 13.58 ? 31  ASP B OD1 1 
ATOM   2317 O  OD2 . ASP B 1 31  ? -0.599  -8.827  -10.056 1.00 13.68 ? 31  ASP B OD2 1 
ATOM   2318 N  N   . LEU B 1 32  ? -1.979  -8.478  -14.319 1.00 11.84 ? 32  LEU B N   1 
ATOM   2319 C  CA  . LEU B 1 32  ? -3.141  -9.309  -14.621 1.00 13.07 ? 32  LEU B CA  1 
ATOM   2320 C  C   . LEU B 1 32  ? -3.216  -10.473 -13.631 1.00 15.19 ? 32  LEU B C   1 
ATOM   2321 O  O   . LEU B 1 32  ? -2.531  -11.483 -13.797 1.00 14.77 ? 32  LEU B O   1 
ATOM   2322 C  CB  . LEU B 1 32  ? -2.993  -9.815  -16.057 1.00 11.97 ? 32  LEU B CB  1 
ATOM   2323 C  CG  . LEU B 1 32  ? -2.651  -8.715  -17.064 1.00 11.83 ? 32  LEU B CG  1 
ATOM   2324 C  CD1 . LEU B 1 32  ? -2.333  -9.285  -18.462 1.00 11.06 ? 32  LEU B CD1 1 
ATOM   2325 C  CD2 . LEU B 1 32  ? -3.786  -7.697  -17.117 1.00 10.74 ? 32  LEU B CD2 1 
ATOM   2326 N  N   . HIS B 1 33  ? -4.025  -10.329 -12.577 1.00 19.39 ? 33  HIS B N   1 
ATOM   2327 C  CA  . HIS B 1 33  ? -3.995  -11.368 -11.562 1.00 23.18 ? 33  HIS B CA  1 
ATOM   2328 C  C   . HIS B 1 33  ? -5.382  -11.937 -11.316 1.00 25.92 ? 33  HIS B C   1 
ATOM   2329 O  O   . HIS B 1 33  ? -6.396  -11.273 -11.535 1.00 22.25 ? 33  HIS B O   1 
ATOM   2330 C  CB  . HIS B 1 33  ? -3.230  -10.936 -10.303 1.00 28.14 ? 33  HIS B CB  1 
ATOM   2331 C  CG  . HIS B 1 33  ? -3.987  -10.035 -9.385  1.00 31.76 ? 33  HIS B CG  1 
ATOM   2332 N  ND1 . HIS B 1 33  ? -3.898  -8.651  -9.462  1.00 36.97 ? 33  HIS B ND1 1 
ATOM   2333 C  CD2 . HIS B 1 33  ? -4.811  -10.306 -8.350  1.00 34.13 ? 33  HIS B CD2 1 
ATOM   2334 C  CE1 . HIS B 1 33  ? -4.646  -8.100  -8.521  1.00 38.39 ? 33  HIS B CE1 1 
ATOM   2335 N  NE2 . HIS B 1 33  ? -5.221  -9.100  -7.822  1.00 40.57 ? 33  HIS B NE2 1 
ATOM   2336 N  N   . SER B 1 34  ? -5.387  -13.176 -10.822 1.00 28.37 ? 34  SER B N   1 
ATOM   2337 C  CA  . SER B 1 34  ? -6.564  -14.030 -10.772 1.00 31.61 ? 34  SER B CA  1 
ATOM   2338 C  C   . SER B 1 34  ? -7.791  -13.267 -10.272 1.00 31.19 ? 34  SER B C   1 
ATOM   2339 O  O   . SER B 1 34  ? -8.865  -13.365 -10.868 1.00 33.43 ? 34  SER B O   1 
ATOM   2340 C  CB  . SER B 1 34  ? -6.266  -15.278 -9.959  1.00 33.43 ? 34  SER B CB  1 
ATOM   2341 O  OG  . SER B 1 34  ? -7.438  -15.735 -9.293  1.00 39.28 ? 34  SER B OG  1 
ATOM   2342 N  N   . ASP B 1 35  ? -7.591  -12.465 -9.216  1.00 32.20 ? 35  ASP B N   1 
ATOM   2343 C  CA  . ASP B 1 35  ? -8.636  -11.858 -8.403  1.00 33.56 ? 35  ASP B CA  1 
ATOM   2344 C  C   . ASP B 1 35  ? -9.394  -10.764 -9.142  1.00 33.00 ? 35  ASP B C   1 
ATOM   2345 O  O   . ASP B 1 35  ? -10.517 -10.448 -8.759  1.00 34.35 ? 35  ASP B O   1 
ATOM   2346 C  CB  . ASP B 1 35  ? -8.048  -11.175 -7.167  1.00 39.25 ? 35  ASP B CB  1 
ATOM   2347 C  CG  . ASP B 1 35  ? -7.970  -12.081 -5.951  1.00 43.59 ? 35  ASP B CG  1 
ATOM   2348 O  OD1 . ASP B 1 35  ? -9.018  -12.253 -5.288  1.00 46.67 ? 35  ASP B OD1 1 
ATOM   2349 O  OD2 . ASP B 1 35  ? -6.867  -12.608 -5.678  1.00 44.45 ? 35  ASP B OD2 1 
ATOM   2350 N  N   . ILE B 1 36  ? -8.770  -10.147 -10.152 1.00 29.17 ? 36  ILE B N   1 
ATOM   2351 C  CA  . ILE B 1 36  ? -9.411  -9.041  -10.844 1.00 26.87 ? 36  ILE B CA  1 
ATOM   2352 C  C   . ILE B 1 36  ? -9.847  -9.476  -12.242 1.00 24.83 ? 36  ILE B C   1 
ATOM   2353 O  O   . ILE B 1 36  ? -10.241 -8.634  -13.041 1.00 24.58 ? 36  ILE B O   1 
ATOM   2354 C  CB  . ILE B 1 36  ? -8.503  -7.787  -10.889 1.00 27.34 ? 36  ILE B CB  1 
ATOM   2355 C  CG1 . ILE B 1 36  ? -7.190  -8.059  -11.627 1.00 24.91 ? 36  ILE B CG1 1 
ATOM   2356 C  CG2 . ILE B 1 36  ? -8.283  -7.244  -9.483  1.00 26.65 ? 36  ILE B CG2 1 
ATOM   2357 C  CD1 . ILE B 1 36  ? -6.492  -6.819  -12.130 1.00 27.96 ? 36  ILE B CD1 1 
ATOM   2358 N  N   . LEU B 1 37  ? -9.746  -10.779 -12.540 1.00 22.80 ? 37  LEU B N   1 
ATOM   2359 C  CA  . LEU B 1 37  ? -10.170 -11.278 -13.835 1.00 21.79 ? 37  LEU B CA  1 
ATOM   2360 C  C   . LEU B 1 37  ? -11.657 -11.620 -13.808 1.00 23.97 ? 37  LEU B C   1 
ATOM   2361 O  O   . LEU B 1 37  ? -12.144 -12.251 -12.867 1.00 23.24 ? 37  LEU B O   1 
ATOM   2362 C  CB  . LEU B 1 37  ? -9.348  -12.515 -14.197 1.00 19.83 ? 37  LEU B CB  1 
ATOM   2363 C  CG  . LEU B 1 37  ? -7.836  -12.313 -14.182 1.00 19.54 ? 37  LEU B CG  1 
ATOM   2364 C  CD1 . LEU B 1 37  ? -7.129  -13.588 -14.618 1.00 20.71 ? 37  LEU B CD1 1 
ATOM   2365 C  CD2 . LEU B 1 37  ? -7.433  -11.134 -15.049 1.00 19.22 ? 37  LEU B CD2 1 
ATOM   2366 N  N   . GLN B 1 38  ? -12.373 -11.223 -14.864 1.00 20.22 ? 38  GLN B N   1 
ATOM   2367 C  CA  . GLN B 1 38  ? -13.778 -11.591 -14.941 1.00 21.13 ? 38  GLN B CA  1 
ATOM   2368 C  C   . GLN B 1 38  ? -14.073 -12.085 -16.347 1.00 17.41 ? 38  GLN B C   1 
ATOM   2369 O  O   . GLN B 1 38  ? -13.850 -11.376 -17.314 1.00 15.40 ? 38  GLN B O   1 
ATOM   2370 C  CB  . GLN B 1 38  ? -14.723 -10.442 -14.579 1.00 21.92 ? 38  GLN B CB  1 
ATOM   2371 C  CG  . GLN B 1 38  ? -16.195 -10.813 -14.765 1.00 26.74 ? 38  GLN B CG  1 
ATOM   2372 C  CD  . GLN B 1 38  ? -17.146 -9.743  -14.281 1.00 31.29 ? 38  GLN B CD  1 
ATOM   2373 O  OE1 . GLN B 1 38  ? -17.158 -9.375  -13.103 1.00 32.86 ? 38  GLN B OE1 1 
ATOM   2374 N  NE2 . GLN B 1 38  ? -17.957 -9.233  -15.196 1.00 32.06 ? 38  GLN B NE2 1 
ATOM   2375 N  N   . TYR B 1 39  ? -14.575 -13.310 -16.436 1.00 16.28 ? 39  TYR B N   1 
ATOM   2376 C  CA  . TYR B 1 39  ? -14.882 -13.868 -17.738 1.00 16.55 ? 39  TYR B CA  1 
ATOM   2377 C  C   . TYR B 1 39  ? -16.008 -13.059 -18.374 1.00 16.10 ? 39  TYR B C   1 
ATOM   2378 O  O   . TYR B 1 39  ? -16.975 -12.700 -17.690 1.00 15.88 ? 39  TYR B O   1 
ATOM   2379 C  CB  . TYR B 1 39  ? -15.199 -15.358 -17.625 1.00 17.50 ? 39  TYR B CB  1 
ATOM   2380 C  CG  . TYR B 1 39  ? -15.830 -15.928 -18.867 1.00 18.51 ? 39  TYR B CG  1 
ATOM   2381 C  CD1 . TYR B 1 39  ? -15.121 -16.026 -20.047 1.00 19.10 ? 39  TYR B CD1 1 
ATOM   2382 C  CD2 . TYR B 1 39  ? -17.157 -16.328 -18.874 1.00 20.39 ? 39  TYR B CD2 1 
ATOM   2383 C  CE1 . TYR B 1 39  ? -15.696 -16.537 -21.202 1.00 20.01 ? 39  TYR B CE1 1 
ATOM   2384 C  CE2 . TYR B 1 39  ? -17.748 -16.850 -20.012 1.00 20.81 ? 39  TYR B CE2 1 
ATOM   2385 C  CZ  . TYR B 1 39  ? -17.017 -16.955 -21.181 1.00 21.27 ? 39  TYR B CZ  1 
ATOM   2386 O  OH  . TYR B 1 39  ? -17.595 -17.490 -22.302 1.00 21.70 ? 39  TYR B OH  1 
ATOM   2387 N  N   . ASP B 1 40  ? -15.840 -12.760 -19.674 1.00 15.38 ? 40  ASP B N   1 
ATOM   2388 C  CA  . ASP B 1 40  ? -16.799 -12.018 -20.491 1.00 16.66 ? 40  ASP B CA  1 
ATOM   2389 C  C   . ASP B 1 40  ? -17.055 -12.803 -21.786 1.00 16.12 ? 40  ASP B C   1 
ATOM   2390 O  O   . ASP B 1 40  ? -16.266 -12.778 -22.737 1.00 14.63 ? 40  ASP B O   1 
ATOM   2391 C  CB  . ASP B 1 40  ? -16.304 -10.580 -20.701 1.00 17.82 ? 40  ASP B CB  1 
ATOM   2392 C  CG  . ASP B 1 40  ? -17.283 -9.621  -21.373 1.00 22.26 ? 40  ASP B CG  1 
ATOM   2393 O  OD1 . ASP B 1 40  ? -18.182 -10.090 -22.132 1.00 20.45 ? 40  ASP B OD1 1 
ATOM   2394 O  OD2 . ASP B 1 40  ? -17.137 -8.381  -21.131 1.00 26.31 ? 40  ASP B OD2 1 
ATOM   2395 N  N   . ALA B 1 41  ? -18.167 -13.539 -21.803 1.00 16.60 ? 41  ALA B N   1 
ATOM   2396 C  CA  . ALA B 1 41  ? -18.529 -14.412 -22.912 1.00 17.93 ? 41  ALA B CA  1 
ATOM   2397 C  C   . ALA B 1 41  ? -18.754 -13.608 -24.191 1.00 18.98 ? 41  ALA B C   1 
ATOM   2398 O  O   . ALA B 1 41  ? -18.824 -14.168 -25.276 1.00 20.64 ? 41  ALA B O   1 
ATOM   2399 C  CB  . ALA B 1 41  ? -19.749 -15.232 -22.549 1.00 20.72 ? 41  ALA B CB  1 
ATOM   2400 N  N   . SER B 1 42  ? -18.826 -12.284 -24.079 1.00 19.80 ? 42  SER B N   1 
ATOM   2401 C  CA  . SER B 1 42  ? -19.088 -11.475 -25.256 1.00 20.91 ? 42  SER B CA  1 
ATOM   2402 C  C   . SER B 1 42  ? -17.786 -11.089 -25.971 1.00 23.10 ? 42  SER B C   1 
ATOM   2403 O  O   . SER B 1 42  ? -17.820 -10.559 -27.078 1.00 23.26 ? 42  SER B O   1 
ATOM   2404 C  CB  . SER B 1 42  ? -19.916 -10.282 -24.891 1.00 21.80 ? 42  SER B CB  1 
ATOM   2405 O  OG  . SER B 1 42  ? -19.081 -9.197  -24.515 1.00 20.08 ? 42  SER B OG  1 
ATOM   2406 N  N   . LEU B 1 43  ? -16.634 -11.362 -25.346 1.00 21.83 ? 43  LEU B N   1 
ATOM   2407 C  CA  . LEU B 1 43  ? -15.348 -11.160 -26.001 1.00 19.63 ? 43  LEU B CA  1 
ATOM   2408 C  C   . LEU B 1 43  ? -15.113 -12.290 -26.997 1.00 19.55 ? 43  LEU B C   1 
ATOM   2409 O  O   . LEU B 1 43  ? -14.602 -13.359 -26.631 1.00 17.38 ? 43  LEU B O   1 
ATOM   2410 C  CB  . LEU B 1 43  ? -14.254 -11.140 -24.932 1.00 19.37 ? 43  LEU B CB  1 
ATOM   2411 C  CG  . LEU B 1 43  ? -14.373 -9.986  -23.938 1.00 19.73 ? 43  LEU B CG  1 
ATOM   2412 C  CD1 . LEU B 1 43  ? -13.246 -10.013 -22.905 1.00 17.72 ? 43  LEU B CD1 1 
ATOM   2413 C  CD2 . LEU B 1 43  ? -14.423 -8.641  -24.671 1.00 19.72 ? 43  LEU B CD2 1 
ATOM   2414 N  N   . THR B 1 44  ? -15.458 -12.011 -28.263 1.00 18.35 ? 44  THR B N   1 
ATOM   2415 C  CA  . THR B 1 44  ? -15.297 -12.972 -29.343 1.00 19.52 ? 44  THR B CA  1 
ATOM   2416 C  C   . THR B 1 44  ? -13.905 -12.831 -29.962 1.00 17.74 ? 44  THR B C   1 
ATOM   2417 O  O   . THR B 1 44  ? -13.147 -11.919 -29.613 1.00 16.46 ? 44  THR B O   1 
ATOM   2418 C  CB  . THR B 1 44  ? -16.468 -12.942 -30.345 1.00 22.11 ? 44  THR B CB  1 
ATOM   2419 O  OG1 . THR B 1 44  ? -16.798 -11.592 -30.647 1.00 23.78 ? 44  THR B OG1 1 
ATOM   2420 C  CG2 . THR B 1 44  ? -17.718 -13.615 -29.825 1.00 24.92 ? 44  THR B CG2 1 
ATOM   2421 N  N   . PRO B 1 45  ? -13.500 -13.791 -30.824 1.00 15.97 ? 45  PRO B N   1 
ATOM   2422 C  CA  . PRO B 1 45  ? -12.195 -13.743 -31.472 1.00 16.25 ? 45  PRO B CA  1 
ATOM   2423 C  C   . PRO B 1 45  ? -12.102 -12.505 -32.355 1.00 16.11 ? 45  PRO B C   1 
ATOM   2424 O  O   . PRO B 1 45  ? -13.038 -12.196 -33.075 1.00 15.72 ? 45  PRO B O   1 
ATOM   2425 C  CB  . PRO B 1 45  ? -12.176 -15.054 -32.269 1.00 16.38 ? 45  PRO B CB  1 
ATOM   2426 C  CG  . PRO B 1 45  ? -13.090 -15.955 -31.458 1.00 16.43 ? 45  PRO B CG  1 
ATOM   2427 C  CD  . PRO B 1 45  ? -14.235 -15.026 -31.136 1.00 16.28 ? 45  PRO B CD  1 
ATOM   2428 N  N   . LEU B 1 46  ? -10.986 -11.777 -32.242 1.00 16.55 ? 46  LEU B N   1 
ATOM   2429 C  CA  . LEU B 1 46  ? -10.685 -10.678 -33.147 1.00 17.93 ? 46  LEU B CA  1 
ATOM   2430 C  C   . LEU B 1 46  ? -10.258 -11.275 -34.486 1.00 20.15 ? 46  LEU B C   1 
ATOM   2431 O  O   . LEU B 1 46  ? -9.759  -12.403 -34.551 1.00 21.88 ? 46  LEU B O   1 
ATOM   2432 C  CB  . LEU B 1 46  ? -9.567  -9.830  -32.538 1.00 17.01 ? 46  LEU B CB  1 
ATOM   2433 C  CG  . LEU B 1 46  ? -9.968  -8.994  -31.321 1.00 17.79 ? 46  LEU B CG  1 
ATOM   2434 C  CD1 . LEU B 1 46  ? -8.740  -8.391  -30.647 1.00 17.20 ? 46  LEU B CD1 1 
ATOM   2435 C  CD2 . LEU B 1 46  ? -10.934 -7.893  -31.732 1.00 17.55 ? 46  LEU B CD2 1 
ATOM   2436 N  N   . GLU B 1 47  ? -10.490 -10.526 -35.563 1.00 20.21 ? 47  GLU B N   1 
ATOM   2437 C  CA  . GLU B 1 47  ? -9.960  -10.923 -36.854 1.00 21.77 ? 47  GLU B CA  1 
ATOM   2438 C  C   . GLU B 1 47  ? -8.905  -9.899  -37.251 1.00 19.46 ? 47  GLU B C   1 
ATOM   2439 O  O   . GLU B 1 47  ? -9.071  -8.704  -36.990 1.00 18.50 ? 47  GLU B O   1 
ATOM   2440 C  CB  . GLU B 1 47  ? -11.091 -11.050 -37.880 1.00 26.56 ? 47  GLU B CB  1 
ATOM   2441 C  CG  . GLU B 1 47  ? -11.986 -12.243 -37.608 1.00 31.83 ? 47  GLU B CG  1 
ATOM   2442 C  CD  . GLU B 1 47  ? -13.349 -12.167 -38.268 1.00 41.29 ? 47  GLU B CD  1 
ATOM   2443 O  OE1 . GLU B 1 47  ? -14.171 -13.064 -38.001 1.00 44.43 ? 47  GLU B OE1 1 
ATOM   2444 O  OE2 . GLU B 1 47  ? -13.586 -11.206 -39.045 1.00 49.00 ? 47  GLU B OE2 1 
ATOM   2445 N  N   . PHE B 1 48  ? -7.828  -10.410 -37.848 1.00 16.65 ? 48  PHE B N   1 
ATOM   2446 C  CA  . PHE B 1 48  ? -6.684  -9.637  -38.295 1.00 17.39 ? 48  PHE B CA  1 
ATOM   2447 C  C   . PHE B 1 48  ? -6.706  -9.579  -39.817 1.00 18.35 ? 48  PHE B C   1 
ATOM   2448 O  O   . PHE B 1 48  ? -6.563  -10.594 -40.500 1.00 18.83 ? 48  PHE B O   1 
ATOM   2449 C  CB  . PHE B 1 48  ? -5.397  -10.170 -37.668 1.00 15.73 ? 48  PHE B CB  1 
ATOM   2450 C  CG  . PHE B 1 48  ? -5.588  -10.516 -36.213 1.00 16.59 ? 48  PHE B CG  1 
ATOM   2451 C  CD1 . PHE B 1 48  ? -5.675  -9.515  -35.246 1.00 16.05 ? 48  PHE B CD1 1 
ATOM   2452 C  CD2 . PHE B 1 48  ? -5.736  -11.841 -35.819 1.00 16.61 ? 48  PHE B CD2 1 
ATOM   2453 C  CE1 . PHE B 1 48  ? -5.891  -9.839  -33.911 1.00 16.69 ? 48  PHE B CE1 1 
ATOM   2454 C  CE2 . PHE B 1 48  ? -5.941  -12.162 -34.483 1.00 16.42 ? 48  PHE B CE2 1 
ATOM   2455 C  CZ  . PHE B 1 48  ? -6.023  -11.166 -33.531 1.00 16.72 ? 48  PHE B CZ  1 
ATOM   2456 N  N   . GLN B 1 49  ? -6.949  -8.380  -40.322 1.00 16.46 ? 49  GLN B N   1 
ATOM   2457 C  CA  . GLN B 1 49  ? -7.201  -8.209  -41.738 1.00 18.45 ? 49  GLN B CA  1 
ATOM   2458 C  C   . GLN B 1 49  ? -6.017  -7.460  -42.344 1.00 17.33 ? 49  GLN B C   1 
ATOM   2459 O  O   . GLN B 1 49  ? -5.534  -6.459  -41.797 1.00 17.84 ? 49  GLN B O   1 
ATOM   2460 C  CB  . GLN B 1 49  ? -8.582  -7.574  -41.934 1.00 23.51 ? 49  GLN B CB  1 
ATOM   2461 C  CG  . GLN B 1 49  ? -9.626  -8.444  -42.648 1.00 31.59 ? 49  GLN B CG  1 
ATOM   2462 C  CD  . GLN B 1 49  ? -10.401 -9.486  -41.868 1.00 33.09 ? 49  GLN B CD  1 
ATOM   2463 O  OE1 . GLN B 1 49  ? -11.525 -9.252  -41.414 1.00 35.37 ? 49  GLN B OE1 1 
ATOM   2464 N  NE2 . GLN B 1 49  ? -9.837  -10.680 -41.757 1.00 36.21 ? 49  GLN B NE2 1 
ATOM   2465 N  N   . GLY B 1 50  ? -5.491  -8.029  -43.428 1.00 15.37 ? 50  GLY B N   1 
ATOM   2466 C  CA  . GLY B 1 50  ? -4.459  -7.372  -44.201 1.00 15.40 ? 50  GLY B CA  1 
ATOM   2467 C  C   . GLY B 1 50  ? -3.092  -7.534  -43.542 1.00 14.90 ? 50  GLY B C   1 
ATOM   2468 O  O   . GLY B 1 50  ? -2.187  -6.767  -43.859 1.00 13.38 ? 50  GLY B O   1 
ATOM   2469 N  N   . TYR B 1 51  ? -2.953  -8.540  -42.650 1.00 14.21 ? 51  TYR B N   1 
ATOM   2470 C  CA  . TYR B 1 51  ? -1.719  -8.725  -41.888 1.00 14.02 ? 51  TYR B CA  1 
ATOM   2471 C  C   . TYR B 1 51  ? -0.639  -9.376  -42.760 1.00 15.05 ? 51  TYR B C   1 
ATOM   2472 O  O   . TYR B 1 51  ? 0.554   -9.292  -42.456 1.00 14.65 ? 51  TYR B O   1 
ATOM   2473 C  CB  . TYR B 1 51  ? -1.970  -9.513  -40.598 1.00 13.78 ? 51  TYR B CB  1 
ATOM   2474 C  CG  . TYR B 1 51  ? -2.303  -8.694  -39.372 1.00 12.92 ? 51  TYR B CG  1 
ATOM   2475 C  CD1 . TYR B 1 51  ? -3.261  -7.681  -39.411 1.00 12.73 ? 51  TYR B CD1 1 
ATOM   2476 C  CD2 . TYR B 1 51  ? -1.677  -8.937  -38.157 1.00 12.83 ? 51  TYR B CD2 1 
ATOM   2477 C  CE1 . TYR B 1 51  ? -3.566  -6.910  -38.292 1.00 11.78 ? 51  TYR B CE1 1 
ATOM   2478 C  CE2 . TYR B 1 51  ? -1.950  -8.158  -37.032 1.00 12.10 ? 51  TYR B CE2 1 
ATOM   2479 C  CZ  . TYR B 1 51  ? -2.924  -7.165  -37.090 1.00 12.18 ? 51  TYR B CZ  1 
ATOM   2480 O  OH  . TYR B 1 51  ? -3.208  -6.391  -35.991 1.00 11.89 ? 51  TYR B OH  1 
ATOM   2481 N  N   . ASN B 1 52  ? -1.076  -10.049 -43.830 1.00 16.78 ? 52  ASN B N   1 
ATOM   2482 C  CA  . ASN B 1 52  ? -0.185  -10.754 -44.745 1.00 18.59 ? 52  ASN B CA  1 
ATOM   2483 C  C   . ASN B 1 52  ? 0.460   -9.750  -45.700 1.00 19.73 ? 52  ASN B C   1 
ATOM   2484 O  O   . ASN B 1 52  ? -0.097  -9.455  -46.756 1.00 19.47 ? 52  ASN B O   1 
ATOM   2485 C  CB  . ASN B 1 52  ? -0.934  -11.867 -45.481 1.00 19.30 ? 52  ASN B CB  1 
ATOM   2486 C  CG  . ASN B 1 52  ? -0.007  -12.783 -46.246 1.00 21.54 ? 52  ASN B CG  1 
ATOM   2487 O  OD1 . ASN B 1 52  ? 1.200   -12.770 -46.019 1.00 22.91 ? 52  ASN B OD1 1 
ATOM   2488 N  ND2 . ASN B 1 52  ? -0.554  -13.529 -47.196 1.00 21.48 ? 52  ASN B ND2 1 
ATOM   2489 N  N   . LEU B 1 53  ? 1.625   -9.217  -45.304 1.00 18.61 ? 53  LEU B N   1 
ATOM   2490 C  CA  . LEU B 1 53  ? 2.299   -8.150  -46.032 1.00 21.06 ? 53  LEU B CA  1 
ATOM   2491 C  C   . LEU B 1 53  ? 3.154   -8.763  -47.138 1.00 22.73 ? 53  LEU B C   1 
ATOM   2492 O  O   . LEU B 1 53  ? 3.828   -9.763  -46.916 1.00 22.75 ? 53  LEU B O   1 
ATOM   2493 C  CB  . LEU B 1 53  ? 3.183   -7.341  -45.066 1.00 18.56 ? 53  LEU B CB  1 
ATOM   2494 C  CG  . LEU B 1 53  ? 2.457   -6.708  -43.877 1.00 18.58 ? 53  LEU B CG  1 
ATOM   2495 C  CD1 . LEU B 1 53  ? 3.435   -5.980  -42.965 1.00 18.29 ? 53  LEU B CD1 1 
ATOM   2496 C  CD2 . LEU B 1 53  ? 1.381   -5.750  -44.351 1.00 18.53 ? 53  LEU B CD2 1 
ATOM   2497 N  N   . SER B 1 54  ? 3.146   -8.119  -48.309 1.00 24.64 ? 54  SER B N   1 
ATOM   2498 C  CA  . SER B 1 54  ? 3.863   -8.615  -49.471 1.00 24.07 ? 54  SER B CA  1 
ATOM   2499 C  C   . SER B 1 54  ? 5.366   -8.609  -49.209 1.00 23.43 ? 54  SER B C   1 
ATOM   2500 O  O   . SER B 1 54  ? 5.921   -7.595  -48.797 1.00 20.86 ? 54  SER B O   1 
ATOM   2501 C  CB  . SER B 1 54  ? 3.522   -7.801  -50.689 1.00 24.98 ? 54  SER B CB  1 
ATOM   2502 O  OG  . SER B 1 54  ? 4.471   -8.057  -51.711 1.00 23.96 ? 54  SER B OG  1 
ATOM   2503 N  N   . ALA B 1 55  ? 6.012   -9.743  -49.509 1.00 21.57 ? 55  ALA B N   1 
ATOM   2504 C  CA  . ALA B 1 55  ? 7.458   -9.848  -49.442 1.00 22.69 ? 55  ALA B CA  1 
ATOM   2505 C  C   . ALA B 1 55  ? 8.143   -8.977  -50.505 1.00 22.54 ? 55  ALA B C   1 
ATOM   2506 O  O   . ALA B 1 55  ? 9.350   -8.756  -50.439 1.00 21.89 ? 55  ALA B O   1 
ATOM   2507 C  CB  . ALA B 1 55  ? 7.846   -11.307 -49.523 1.00 26.56 ? 55  ALA B CB  1 
ATOM   2508 N  N   . ASN B 1 56  ? 7.364   -8.400  -51.434 1.00 22.26 ? 56  ASN B N   1 
ATOM   2509 C  CA  . ASN B 1 56  ? 7.888   -7.509  -52.465 1.00 22.83 ? 56  ASN B CA  1 
ATOM   2510 C  C   . ASN B 1 56  ? 7.946   -6.054  -51.985 1.00 22.11 ? 56  ASN B C   1 
ATOM   2511 O  O   . ASN B 1 56  ? 8.496   -5.190  -52.674 1.00 21.38 ? 56  ASN B O   1 
ATOM   2512 C  CB  . ASN B 1 56  ? 7.053   -7.595  -53.744 1.00 24.30 ? 56  ASN B CB  1 
ATOM   2513 C  CG  . ASN B 1 56  ? 7.286   -8.884  -54.505 1.00 28.11 ? 56  ASN B CG  1 
ATOM   2514 O  OD1 . ASN B 1 56  ? 8.398   -9.406  -54.532 1.00 26.08 ? 56  ASN B OD1 1 
ATOM   2515 N  ND2 . ASN B 1 56  ? 6.241   -9.409  -55.126 1.00 30.03 ? 56  ASN B ND2 1 
ATOM   2516 N  N   . LYS B 1 57  ? 7.390   -5.797  -50.792 1.00 20.48 ? 57  LYS B N   1 
ATOM   2517 C  CA  . LYS B 1 57  ? 7.248   -4.457  -50.243 1.00 20.97 ? 57  LYS B CA  1 
ATOM   2518 C  C   . LYS B 1 57  ? 8.164   -4.332  -49.028 1.00 18.88 ? 57  LYS B C   1 
ATOM   2519 O  O   . LYS B 1 57  ? 8.393   -5.328  -48.340 1.00 18.62 ? 57  LYS B O   1 
ATOM   2520 C  CB  . LYS B 1 57  ? 5.780   -4.257  -49.834 1.00 24.01 ? 57  LYS B CB  1 
ATOM   2521 C  CG  . LYS B 1 57  ? 5.237   -2.844  -49.947 1.00 30.61 ? 57  LYS B CG  1 
ATOM   2522 C  CD  . LYS B 1 57  ? 5.596   -1.941  -48.777 1.00 32.24 ? 57  LYS B CD  1 
ATOM   2523 C  CE  . LYS B 1 57  ? 5.360   -0.462  -49.024 1.00 34.85 ? 57  LYS B CE  1 
ATOM   2524 N  NZ  . LYS B 1 57  ? 5.215   0.288   -47.750 1.00 32.18 ? 57  LYS B NZ  1 
ATOM   2525 N  N   . GLN B 1 58  ? 8.652   -3.111  -48.783 1.00 17.48 ? 58  GLN B N   1 
ATOM   2526 C  CA  . GLN B 1 58  ? 9.569   -2.778  -47.703 1.00 19.01 ? 58  GLN B CA  1 
ATOM   2527 C  C   . GLN B 1 58  ? 8.834   -1.979  -46.622 1.00 18.42 ? 58  GLN B C   1 
ATOM   2528 O  O   . GLN B 1 58  ? 8.055   -1.078  -46.930 1.00 16.79 ? 58  GLN B O   1 
ATOM   2529 C  CB  . GLN B 1 58  ? 10.686  -1.858  -48.204 1.00 21.57 ? 58  GLN B CB  1 
ATOM   2530 C  CG  . GLN B 1 58  ? 11.434  -2.349  -49.439 1.00 25.17 ? 58  GLN B CG  1 
ATOM   2531 C  CD  . GLN B 1 58  ? 12.023  -3.727  -49.275 1.00 29.04 ? 58  GLN B CD  1 
ATOM   2532 O  OE1 . GLN B 1 58  ? 12.051  -4.521  -50.218 1.00 38.58 ? 58  GLN B OE1 1 
ATOM   2533 N  NE2 . GLN B 1 58  ? 12.490  -4.045  -48.079 1.00 29.89 ? 58  GLN B NE2 1 
ATOM   2534 N  N   . PHE B 1 59  ? 9.120   -2.305  -45.352 1.00 15.70 ? 59  PHE B N   1 
ATOM   2535 C  CA  . PHE B 1 59  ? 8.535   -1.615  -44.213 1.00 14.77 ? 59  PHE B CA  1 
ATOM   2536 C  C   . PHE B 1 59  ? 9.654   -1.081  -43.328 1.00 14.34 ? 59  PHE B C   1 
ATOM   2537 O  O   . PHE B 1 59  ? 10.625  -1.791  -43.046 1.00 14.23 ? 59  PHE B O   1 
ATOM   2538 C  CB  . PHE B 1 59  ? 7.548   -2.522  -43.473 1.00 14.77 ? 59  PHE B CB  1 
ATOM   2539 C  CG  . PHE B 1 59  ? 6.454   -2.968  -44.401 1.00 15.35 ? 59  PHE B CG  1 
ATOM   2540 C  CD1 . PHE B 1 59  ? 6.619   -4.092  -45.194 1.00 14.76 ? 59  PHE B CD1 1 
ATOM   2541 C  CD2 . PHE B 1 59  ? 5.312   -2.195  -44.565 1.00 15.16 ? 59  PHE B CD2 1 
ATOM   2542 C  CE1 . PHE B 1 59  ? 5.640   -4.457  -46.107 1.00 14.98 ? 59  PHE B CE1 1 
ATOM   2543 C  CE2 . PHE B 1 59  ? 4.324   -2.590  -45.451 1.00 15.78 ? 59  PHE B CE2 1 
ATOM   2544 C  CZ  . PHE B 1 59  ? 4.489   -3.717  -46.226 1.00 15.05 ? 59  PHE B CZ  1 
ATOM   2545 N  N   . LEU B 1 60  ? 9.472   0.172   -42.891 1.00 13.35 ? 60  LEU B N   1 
ATOM   2546 C  CA  . LEU B 1 60  ? 10.506  0.951   -42.221 1.00 12.51 ? 60  LEU B CA  1 
ATOM   2547 C  C   . LEU B 1 60  ? 10.648  0.516   -40.771 1.00 11.86 ? 60  LEU B C   1 
ATOM   2548 O  O   . LEU B 1 60  ? 9.703   0.645   -40.002 1.00 9.79  ? 60  LEU B O   1 
ATOM   2549 C  CB  . LEU B 1 60  ? 10.123  2.432   -42.272 1.00 12.77 ? 60  LEU B CB  1 
ATOM   2550 C  CG  . LEU B 1 60  ? 11.233  3.411   -41.882 1.00 13.06 ? 60  LEU B CG  1 
ATOM   2551 C  CD1 . LEU B 1 60  ? 12.348  3.359   -42.927 1.00 13.90 ? 60  LEU B CD1 1 
ATOM   2552 C  CD2 . LEU B 1 60  ? 10.656  4.824   -41.804 1.00 13.16 ? 60  LEU B CD2 1 
ATOM   2553 N  N   . LEU B 1 61  ? 11.859  0.045   -40.426 1.00 11.80 ? 61  LEU B N   1 
ATOM   2554 C  CA  . LEU B 1 61  ? 12.233  -0.212  -39.044 1.00 12.70 ? 61  LEU B CA  1 
ATOM   2555 C  C   . LEU B 1 61  ? 13.095  0.943   -38.552 1.00 13.31 ? 61  LEU B C   1 
ATOM   2556 O  O   . LEU B 1 61  ? 14.057  1.332   -39.225 1.00 12.54 ? 61  LEU B O   1 
ATOM   2557 C  CB  . LEU B 1 61  ? 13.016  -1.528  -38.994 1.00 12.02 ? 61  LEU B CB  1 
ATOM   2558 C  CG  . LEU B 1 61  ? 13.284  -2.136  -37.623 1.00 11.10 ? 61  LEU B CG  1 
ATOM   2559 C  CD1 . LEU B 1 61  ? 12.001  -2.718  -37.063 1.00 11.07 ? 61  LEU B CD1 1 
ATOM   2560 C  CD2 . LEU B 1 61  ? 14.336  -3.241  -37.780 1.00 11.20 ? 61  LEU B CD2 1 
ATOM   2561 N  N   . THR B 1 62  ? 12.768  1.442   -37.349 1.00 14.35 ? 62  THR B N   1 
ATOM   2562 C  CA  . THR B 1 62  ? 13.455  2.599   -36.790 1.00 14.54 ? 62  THR B CA  1 
ATOM   2563 C  C   . THR B 1 62  ? 13.871  2.306   -35.355 1.00 14.61 ? 62  THR B C   1 
ATOM   2564 O  O   . THR B 1 62  ? 13.076  1.779   -34.584 1.00 14.90 ? 62  THR B O   1 
ATOM   2565 C  CB  . THR B 1 62  ? 12.531  3.821   -36.714 1.00 14.56 ? 62  THR B CB  1 
ATOM   2566 O  OG1 . THR B 1 62  ? 12.197  4.151   -38.046 1.00 17.42 ? 62  THR B OG1 1 
ATOM   2567 C  CG2 . THR B 1 62  ? 13.202  5.071   -36.182 1.00 17.41 ? 62  THR B CG2 1 
ATOM   2568 N  N   . ASN B 1 63  ? 15.093  2.716   -34.990 1.00 14.40 ? 63  ASN B N   1 
ATOM   2569 C  CA  . ASN B 1 63  ? 15.428  2.900   -33.587 1.00 13.91 ? 63  ASN B CA  1 
ATOM   2570 C  C   . ASN B 1 63  ? 15.016  4.325   -33.208 1.00 14.27 ? 63  ASN B C   1 
ATOM   2571 O  O   . ASN B 1 63  ? 15.600  5.295   -33.701 1.00 14.31 ? 63  ASN B O   1 
ATOM   2572 C  CB  . ASN B 1 63  ? 16.914  2.633   -33.357 1.00 12.75 ? 63  ASN B CB  1 
ATOM   2573 C  CG  . ASN B 1 63  ? 17.408  2.857   -31.944 1.00 12.58 ? 63  ASN B CG  1 
ATOM   2574 O  OD1 . ASN B 1 63  ? 16.843  3.639   -31.184 1.00 13.39 ? 63  ASN B OD1 1 
ATOM   2575 N  ND2 . ASN B 1 63  ? 18.500  2.199   -31.596 1.00 12.20 ? 63  ASN B ND2 1 
ATOM   2576 N  N   . ASN B 1 64  ? 14.010  4.477   -32.332 1.00 14.59 ? 64  ASN B N   1 
ATOM   2577 C  CA  . ASN B 1 64  ? 13.562  5.843   -32.060 1.00 14.62 ? 64  ASN B CA  1 
ATOM   2578 C  C   . ASN B 1 64  ? 14.145  6.349   -30.738 1.00 14.39 ? 64  ASN B C   1 
ATOM   2579 O  O   . ASN B 1 64  ? 13.726  7.387   -30.213 1.00 13.85 ? 64  ASN B O   1 
ATOM   2580 C  CB  . ASN B 1 64  ? 12.035  5.998   -32.131 1.00 15.43 ? 64  ASN B CB  1 
ATOM   2581 C  CG  . ASN B 1 64  ? 11.323  5.087   -31.152 1.00 15.68 ? 64  ASN B CG  1 
ATOM   2582 O  OD1 . ASN B 1 64  ? 11.934  4.630   -30.183 1.00 16.86 ? 64  ASN B OD1 1 
ATOM   2583 N  ND2 . ASN B 1 64  ? 10.039  4.834   -31.384 1.00 14.90 ? 64  ASN B ND2 1 
ATOM   2584 N  N   . GLY B 1 65  ? 15.094  5.593   -30.185 1.00 13.41 ? 65  GLY B N   1 
ATOM   2585 C  CA  . GLY B 1 65  ? 15.667  5.955   -28.897 1.00 13.64 ? 65  GLY B CA  1 
ATOM   2586 C  C   . GLY B 1 65  ? 14.878  5.453   -27.685 1.00 13.94 ? 65  GLY B C   1 
ATOM   2587 O  O   . GLY B 1 65  ? 15.396  5.563   -26.572 1.00 14.17 ? 65  GLY B O   1 
ATOM   2588 N  N   . HIS B 1 66  ? 13.645  4.940   -27.890 1.00 13.27 ? 66  HIS B N   1 
ATOM   2589 C  CA  . HIS B 1 66  ? 12.850  4.334   -26.821 1.00 12.29 ? 66  HIS B CA  1 
ATOM   2590 C  C   . HIS B 1 66  ? 12.602  2.841   -27.067 1.00 12.26 ? 66  HIS B C   1 
ATOM   2591 O  O   . HIS B 1 66  ? 12.514  2.062   -26.124 1.00 11.58 ? 66  HIS B O   1 
ATOM   2592 C  CB  . HIS B 1 66  ? 11.520  5.083   -26.620 1.00 12.56 ? 66  HIS B CB  1 
ATOM   2593 C  CG  . HIS B 1 66  ? 11.666  6.560   -26.415 1.00 12.35 ? 66  HIS B CG  1 
ATOM   2594 N  ND1 . HIS B 1 66  ? 12.263  7.107   -25.279 1.00 13.69 ? 66  HIS B ND1 1 
ATOM   2595 C  CD2 . HIS B 1 66  ? 11.298  7.597   -27.185 1.00 12.29 ? 66  HIS B CD2 1 
ATOM   2596 C  CE1 . HIS B 1 66  ? 12.277  8.425   -25.378 1.00 13.85 ? 66  HIS B CE1 1 
ATOM   2597 N  NE2 . HIS B 1 66  ? 11.656  8.750   -26.540 1.00 13.22 ? 66  HIS B NE2 1 
ATOM   2598 N  N   . SER B 1 67  ? 12.454  2.435   -28.338 1.00 12.11 ? 67  SER B N   1 
ATOM   2599 C  CA  . SER B 1 67  ? 12.245  1.038   -28.677 1.00 12.01 ? 67  SER B CA  1 
ATOM   2600 C  C   . SER B 1 67  ? 12.813  0.825   -30.077 1.00 13.16 ? 67  SER B C   1 
ATOM   2601 O  O   . SER B 1 67  ? 13.428  1.737   -30.639 1.00 14.12 ? 67  SER B O   1 
ATOM   2602 C  CB  . SER B 1 67  ? 10.774  0.687   -28.645 1.00 11.65 ? 67  SER B CB  1 
ATOM   2603 O  OG  . SER B 1 67  ? 10.591  -0.724  -28.724 1.00 12.54 ? 67  SER B OG  1 
ATOM   2604 N  N   . VAL B 1 68  ? 12.606  -0.370  -30.625 1.00 12.05 ? 68  VAL B N   1 
ATOM   2605 C  CA  . VAL B 1 68  ? 12.718  -0.558  -32.068 1.00 12.68 ? 68  VAL B CA  1 
ATOM   2606 C  C   . VAL B 1 68  ? 11.288  -0.690  -32.588 1.00 13.04 ? 68  VAL B C   1 
ATOM   2607 O  O   . VAL B 1 68  ? 10.484  -1.416  -31.997 1.00 11.93 ? 68  VAL B O   1 
ATOM   2608 C  CB  . VAL B 1 68  ? 13.567  -1.798  -32.413 1.00 12.54 ? 68  VAL B CB  1 
ATOM   2609 C  CG1 . VAL B 1 68  ? 13.107  -3.046  -31.658 1.00 11.48 ? 68  VAL B CG1 1 
ATOM   2610 C  CG2 . VAL B 1 68  ? 13.612  -2.060  -33.920 1.00 12.02 ? 68  VAL B CG2 1 
ATOM   2611 N  N   . LYS B 1 69  ? 10.985  0.043   -33.666 1.00 12.57 ? 69  LYS B N   1 
ATOM   2612 C  CA  . LYS B 1 69  ? 9.623   0.180   -34.143 1.00 12.67 ? 69  LYS B CA  1 
ATOM   2613 C  C   . LYS B 1 69  ? 9.598   -0.176  -35.632 1.00 12.46 ? 69  LYS B C   1 
ATOM   2614 O  O   . LYS B 1 69  ? 10.459  0.266   -36.394 1.00 12.06 ? 69  LYS B O   1 
ATOM   2615 C  CB  . LYS B 1 69  ? 9.176   1.633   -33.930 1.00 13.29 ? 69  LYS B CB  1 
ATOM   2616 C  CG  . LYS B 1 69  ? 7.858   2.019   -34.588 1.00 15.02 ? 69  LYS B CG  1 
ATOM   2617 C  CD  . LYS B 1 69  ? 7.469   3.471   -34.363 1.00 15.41 ? 69  LYS B CD  1 
ATOM   2618 C  CE  . LYS B 1 69  ? 8.042   4.415   -35.398 1.00 18.02 ? 69  LYS B CE  1 
ATOM   2619 N  NZ  . LYS B 1 69  ? 7.440   5.763   -35.219 1.00 18.81 ? 69  LYS B NZ  1 
ATOM   2620 N  N   . LEU B 1 70  ? 8.601   -0.977  -36.021 1.00 11.16 ? 70  LEU B N   1 
ATOM   2621 C  CA  . LEU B 1 70  ? 8.335   -1.300  -37.412 1.00 11.11 ? 70  LEU B CA  1 
ATOM   2622 C  C   . LEU B 1 70  ? 7.088   -0.519  -37.816 1.00 11.79 ? 70  LEU B C   1 
ATOM   2623 O  O   . LEU B 1 70  ? 6.034   -0.714  -37.205 1.00 11.61 ? 70  LEU B O   1 
ATOM   2624 C  CB  . LEU B 1 70  ? 8.091   -2.811  -37.527 1.00 9.93  ? 70  LEU B CB  1 
ATOM   2625 C  CG  . LEU B 1 70  ? 7.708   -3.316  -38.923 1.00 9.78  ? 70  LEU B CG  1 
ATOM   2626 C  CD1 . LEU B 1 70  ? 8.802   -3.001  -39.944 1.00 9.21  ? 70  LEU B CD1 1 
ATOM   2627 C  CD2 . LEU B 1 70  ? 7.419   -4.807  -38.908 1.00 10.14 ? 70  LEU B CD2 1 
ATOM   2628 N  N   . ASN B 1 71  ? 7.226   0.384   -38.796 1.00 12.37 ? 71  ASN B N   1 
ATOM   2629 C  CA  . ASN B 1 71  ? 6.082   1.108   -39.334 1.00 13.61 ? 71  ASN B CA  1 
ATOM   2630 C  C   . ASN B 1 71  ? 5.179   0.112   -40.069 1.00 13.04 ? 71  ASN B C   1 
ATOM   2631 O  O   . ASN B 1 71  ? 5.664   -0.818  -40.706 1.00 11.93 ? 71  ASN B O   1 
ATOM   2632 C  CB  . ASN B 1 71  ? 6.493   2.365   -40.118 1.00 16.12 ? 71  ASN B CB  1 
ATOM   2633 C  CG  . ASN B 1 71  ? 7.008   3.460   -39.196 1.00 19.74 ? 71  ASN B CG  1 
ATOM   2634 O  OD1 . ASN B 1 71  ? 6.436   3.740   -38.144 1.00 20.85 ? 71  ASN B OD1 1 
ATOM   2635 N  ND2 . ASN B 1 71  ? 8.125   4.067   -39.553 1.00 25.26 ? 71  ASN B ND2 1 
ATOM   2636 N  N   . LEU B 1 72  ? 3.859   0.239   -39.887 1.00 12.78 ? 72  LEU B N   1 
ATOM   2637 C  CA  . LEU B 1 72  ? 2.939   -0.712  -40.493 1.00 12.36 ? 72  LEU B CA  1 
ATOM   2638 C  C   . LEU B 1 72  ? 1.914   0.057   -41.327 1.00 12.40 ? 72  LEU B C   1 
ATOM   2639 O  O   . LEU B 1 72  ? 1.627   1.220   -41.026 1.00 12.70 ? 72  LEU B O   1 
ATOM   2640 C  CB  . LEU B 1 72  ? 2.245   -1.514  -39.389 1.00 11.66 ? 72  LEU B CB  1 
ATOM   2641 C  CG  . LEU B 1 72  ? 3.111   -2.477  -38.565 1.00 11.77 ? 72  LEU B CG  1 
ATOM   2642 C  CD1 . LEU B 1 72  ? 2.340   -2.999  -37.343 1.00 11.43 ? 72  LEU B CD1 1 
ATOM   2643 C  CD2 . LEU B 1 72  ? 3.618   -3.642  -39.414 1.00 11.82 ? 72  LEU B CD2 1 
ATOM   2644 N  N   . PRO B 1 73  ? 1.363   -0.554  -42.405 1.00 12.15 ? 73  PRO B N   1 
ATOM   2645 C  CA  . PRO B 1 73  ? 0.401   0.129   -43.264 1.00 12.66 ? 73  PRO B CA  1 
ATOM   2646 C  C   . PRO B 1 73  ? -0.996  0.104   -42.662 1.00 13.36 ? 73  PRO B C   1 
ATOM   2647 O  O   . PRO B 1 73  ? -1.383  -0.875  -42.005 1.00 11.79 ? 73  PRO B O   1 
ATOM   2648 C  CB  . PRO B 1 73  ? 0.480   -0.676  -44.574 1.00 12.22 ? 73  PRO B CB  1 
ATOM   2649 C  CG  . PRO B 1 73  ? 0.806   -2.083  -44.136 1.00 12.83 ? 73  PRO B CG  1 
ATOM   2650 C  CD  . PRO B 1 73  ? 1.686   -1.906  -42.909 1.00 12.77 ? 73  PRO B CD  1 
ATOM   2651 N  N   . SER B 1 74  ? -1.760  1.171   -42.956 1.00 13.65 ? 74  SER B N   1 
ATOM   2652 C  CA  . SER B 1 74  ? -3.090  1.323   -42.390 1.00 13.89 ? 74  SER B CA  1 
ATOM   2653 C  C   . SER B 1 74  ? -4.114  0.400   -43.061 1.00 15.49 ? 74  SER B C   1 
ATOM   2654 O  O   . SER B 1 74  ? -5.276  0.384   -42.675 1.00 15.27 ? 74  SER B O   1 
ATOM   2655 C  CB  . SER B 1 74  ? -3.512  2.762   -42.382 1.00 13.45 ? 74  SER B CB  1 
ATOM   2656 O  OG  . SER B 1 74  ? -3.637  3.230   -43.702 1.00 12.10 ? 74  SER B OG  1 
ATOM   2657 N  N   . ASP B 1 75  ? -3.683  -0.428  -44.014 1.00 17.19 ? 75  ASP B N   1 
ATOM   2658 C  CA  . ASP B 1 75  ? -4.614  -1.425  -44.522 1.00 19.83 ? 75  ASP B CA  1 
ATOM   2659 C  C   . ASP B 1 75  ? -4.682  -2.663  -43.609 1.00 18.48 ? 75  ASP B C   1 
ATOM   2660 O  O   . ASP B 1 75  ? -5.554  -3.525  -43.785 1.00 16.69 ? 75  ASP B O   1 
ATOM   2661 C  CB  . ASP B 1 75  ? -4.409  -1.720  -46.008 1.00 24.46 ? 75  ASP B CB  1 
ATOM   2662 C  CG  . ASP B 1 75  ? -2.966  -1.736  -46.468 1.00 27.67 ? 75  ASP B CG  1 
ATOM   2663 O  OD1 . ASP B 1 75  ? -2.251  -2.676  -46.077 1.00 32.02 ? 75  ASP B OD1 1 
ATOM   2664 O  OD2 . ASP B 1 75  ? -2.587  -0.825  -47.235 1.00 24.45 ? 75  ASP B OD2 1 
ATOM   2665 N  N   . MET B 1 76  ? -3.729  -2.787  -42.672 1.00 15.05 ? 76  MET B N   1 
ATOM   2666 C  CA  . MET B 1 76  ? -3.899  -3.764  -41.607 1.00 15.04 ? 76  MET B CA  1 
ATOM   2667 C  C   . MET B 1 76  ? -4.909  -3.203  -40.622 1.00 13.89 ? 76  MET B C   1 
ATOM   2668 O  O   . MET B 1 76  ? -4.757  -2.063  -40.179 1.00 12.77 ? 76  MET B O   1 
ATOM   2669 C  CB  . MET B 1 76  ? -2.598  -3.982  -40.827 1.00 15.01 ? 76  MET B CB  1 
ATOM   2670 C  CG  . MET B 1 76  ? -1.504  -4.584  -41.653 1.00 14.77 ? 76  MET B CG  1 
ATOM   2671 S  SD  . MET B 1 76  ? 0.035   -4.698  -40.711 1.00 15.95 ? 76  MET B SD  1 
ATOM   2672 C  CE  . MET B 1 76  ? -0.503  -5.438  -39.168 1.00 14.38 ? 76  MET B CE  1 
ATOM   2673 N  N   . HIS B 1 77  ? -5.870  -4.036  -40.225 1.00 14.44 ? 77  HIS B N   1 
ATOM   2674 C  CA  . HIS B 1 77  ? -6.846  -3.594  -39.238 1.00 16.26 ? 77  HIS B CA  1 
ATOM   2675 C  C   . HIS B 1 77  ? -7.352  -4.768  -38.414 1.00 15.74 ? 77  HIS B C   1 
ATOM   2676 O  O   . HIS B 1 77  ? -7.172  -5.932  -38.777 1.00 15.55 ? 77  HIS B O   1 
ATOM   2677 C  CB  . HIS B 1 77  ? -8.020  -2.834  -39.877 1.00 20.10 ? 77  HIS B CB  1 
ATOM   2678 C  CG  . HIS B 1 77  ? -8.672  -3.542  -41.012 1.00 22.33 ? 77  HIS B CG  1 
ATOM   2679 N  ND1 . HIS B 1 77  ? -8.358  -3.264  -42.321 1.00 24.92 ? 77  HIS B ND1 1 
ATOM   2680 C  CD2 . HIS B 1 77  ? -9.636  -4.489  -41.052 1.00 25.72 ? 77  HIS B CD2 1 
ATOM   2681 C  CE1 . HIS B 1 77  ? -9.072  -4.036  -43.122 1.00 25.08 ? 77  HIS B CE1 1 
ATOM   2682 N  NE2 . HIS B 1 77  ? -9.881  -4.783  -42.374 1.00 24.06 ? 77  HIS B NE2 1 
ATOM   2683 N  N   . ILE B 1 78  ? -7.936  -4.413  -37.271 1.00 15.53 ? 78  ILE B N   1 
ATOM   2684 C  CA  . ILE B 1 78  ? -8.598  -5.361  -36.400 1.00 14.51 ? 78  ILE B CA  1 
ATOM   2685 C  C   . ILE B 1 78  ? -10.076 -5.247  -36.715 1.00 15.40 ? 78  ILE B C   1 
ATOM   2686 O  O   . ILE B 1 78  ? -10.581 -4.132  -36.805 1.00 13.81 ? 78  ILE B O   1 
ATOM   2687 C  CB  . ILE B 1 78  ? -8.375  -4.981  -34.921 1.00 14.73 ? 78  ILE B CB  1 
ATOM   2688 C  CG1 . ILE B 1 78  ? -6.901  -5.035  -34.507 1.00 12.51 ? 78  ILE B CG1 1 
ATOM   2689 C  CG2 . ILE B 1 78  ? -9.274  -5.847  -34.042 1.00 13.08 ? 78  ILE B CG2 1 
ATOM   2690 C  CD1 . ILE B 1 78  ? -6.623  -4.351  -33.190 1.00 12.71 ? 78  ILE B CD1 1 
ATOM   2691 N  N   . GLN B 1 79  ? -10.745 -6.399  -36.840 1.00 16.86 ? 79  GLN B N   1 
ATOM   2692 C  CA  . GLN B 1 79  ? -12.189 -6.457  -36.986 1.00 21.34 ? 79  GLN B CA  1 
ATOM   2693 C  C   . GLN B 1 79  ? -12.711 -7.153  -35.734 1.00 20.09 ? 79  GLN B C   1 
ATOM   2694 O  O   . GLN B 1 79  ? -12.135 -8.165  -35.321 1.00 20.77 ? 79  GLN B O   1 
ATOM   2695 C  CB  . GLN B 1 79  ? -12.525 -7.179  -38.301 1.00 25.65 ? 79  GLN B CB  1 
ATOM   2696 C  CG  . GLN B 1 79  ? -14.004 -7.277  -38.666 1.00 33.56 ? 79  GLN B CG  1 
ATOM   2697 N  N   . GLY B 1 80  ? -13.737 -6.562  -35.103 1.00 18.37 ? 80  GLY B N   1 
ATOM   2698 C  CA  . GLY B 1 80  ? -14.388 -7.145  -33.935 1.00 17.05 ? 80  GLY B CA  1 
ATOM   2699 C  C   . GLY B 1 80  ? -14.565 -6.160  -32.773 1.00 16.94 ? 80  GLY B C   1 
ATOM   2700 O  O   . GLY B 1 80  ? -15.260 -6.454  -31.811 1.00 15.42 ? 80  GLY B O   1 
ATOM   2701 N  N   . LEU B 1 81  ? -13.920 -4.992  -32.831 1.00 16.90 ? 81  LEU B N   1 
ATOM   2702 C  CA  . LEU B 1 81  ? -14.128 -3.988  -31.793 1.00 16.96 ? 81  LEU B CA  1 
ATOM   2703 C  C   . LEU B 1 81  ? -15.257 -3.040  -32.210 1.00 17.62 ? 81  LEU B C   1 
ATOM   2704 O  O   . LEU B 1 81  ? -15.762 -3.139  -33.324 1.00 15.37 ? 81  LEU B O   1 
ATOM   2705 C  CB  . LEU B 1 81  ? -12.806 -3.245  -31.554 1.00 16.21 ? 81  LEU B CB  1 
ATOM   2706 C  CG  . LEU B 1 81  ? -11.656 -4.148  -31.097 1.00 15.69 ? 81  LEU B CG  1 
ATOM   2707 C  CD1 . LEU B 1 81  ? -10.321 -3.419  -31.117 1.00 15.31 ? 81  LEU B CD1 1 
ATOM   2708 C  CD2 . LEU B 1 81  ? -11.939 -4.746  -29.714 1.00 15.70 ? 81  LEU B CD2 1 
ATOM   2709 N  N   . GLN B 1 82  ? -15.609 -2.096  -31.328 1.00 18.94 ? 82  GLN B N   1 
ATOM   2710 C  CA  . GLN B 1 82  ? -16.689 -1.149  -31.588 1.00 21.67 ? 82  GLN B CA  1 
ATOM   2711 C  C   . GLN B 1 82  ? -16.395 -0.316  -32.834 1.00 18.83 ? 82  GLN B C   1 
ATOM   2712 O  O   . GLN B 1 82  ? -17.306 -0.034  -33.606 1.00 17.88 ? 82  GLN B O   1 
ATOM   2713 C  CB  . GLN B 1 82  ? -17.014 -0.259  -30.378 1.00 26.93 ? 82  GLN B CB  1 
ATOM   2714 C  CG  . GLN B 1 82  ? -15.827 0.054   -29.470 1.00 37.26 ? 82  GLN B CG  1 
ATOM   2715 C  CD  . GLN B 1 82  ? -15.142 1.385   -29.697 1.00 42.93 ? 82  GLN B CD  1 
ATOM   2716 O  OE1 . GLN B 1 82  ? -15.734 2.461   -29.540 1.00 53.49 ? 82  GLN B OE1 1 
ATOM   2717 N  NE2 . GLN B 1 82  ? -13.859 1.326   -30.024 1.00 39.78 ? 82  GLN B NE2 1 
ATOM   2718 N  N   . SER B 1 83  ? -15.126 0.068   -33.005 1.00 16.27 ? 83  SER B N   1 
ATOM   2719 C  CA  . SER B 1 83  ? -14.679 0.820   -34.155 1.00 15.38 ? 83  SER B CA  1 
ATOM   2720 C  C   . SER B 1 83  ? -13.694 -0.049  -34.924 1.00 15.10 ? 83  SER B C   1 
ATOM   2721 O  O   . SER B 1 83  ? -13.137 -0.998  -34.389 1.00 12.30 ? 83  SER B O   1 
ATOM   2722 C  CB  . SER B 1 83  ? -13.990 2.113   -33.752 1.00 16.51 ? 83  SER B CB  1 
ATOM   2723 O  OG  . SER B 1 83  ? -14.905 3.115   -33.332 1.00 18.25 ? 83  SER B OG  1 
ATOM   2724 N  N   . ARG B 1 84  ? -13.447 0.358   -36.168 1.00 15.01 ? 84  ARG B N   1 
ATOM   2725 C  CA  . ARG B 1 84  ? -12.324 -0.156  -36.921 1.00 15.58 ? 84  ARG B CA  1 
ATOM   2726 C  C   . ARG B 1 84  ? -11.040 0.452   -36.358 1.00 14.00 ? 84  ARG B C   1 
ATOM   2727 O  O   . ARG B 1 84  ? -10.948 1.667   -36.207 1.00 13.43 ? 84  ARG B O   1 
ATOM   2728 C  CB  . ARG B 1 84  ? -12.598 0.131   -38.398 1.00 17.28 ? 84  ARG B CB  1 
ATOM   2729 C  CG  . ARG B 1 84  ? -11.360 0.425   -39.221 1.00 22.32 ? 84  ARG B CG  1 
ATOM   2730 C  CD  . ARG B 1 84  ? -10.768 -0.786  -39.885 1.00 23.06 ? 84  ARG B CD  1 
ATOM   2731 N  NE  . ARG B 1 84  ? -11.442 -1.190  -41.108 1.00 26.72 ? 84  ARG B NE  1 
ATOM   2732 C  CZ  . ARG B 1 84  ? -12.364 -2.134  -41.145 1.00 26.57 ? 84  ARG B CZ  1 
ATOM   2733 N  NH1 . ARG B 1 84  ? -12.717 -2.730  -40.014 1.00 29.26 ? 84  ARG B NH1 1 
ATOM   2734 N  NH2 . ARG B 1 84  ? -12.920 -2.470  -42.297 1.00 23.53 ? 84  ARG B NH2 1 
ATOM   2735 N  N   . TYR B 1 85  ? -10.055 -0.408  -36.052 1.00 12.79 ? 85  TYR B N   1 
ATOM   2736 C  CA  . TYR B 1 85  ? -8.736  0.069   -35.686 1.00 12.23 ? 85  TYR B CA  1 
ATOM   2737 C  C   . TYR B 1 85  ? -7.724  -0.435  -36.705 1.00 11.76 ? 85  TYR B C   1 
ATOM   2738 O  O   . TYR B 1 85  ? -7.628  -1.634  -36.918 1.00 12.23 ? 85  TYR B O   1 
ATOM   2739 C  CB  . TYR B 1 85  ? -8.352  -0.391  -34.281 1.00 12.23 ? 85  TYR B CB  1 
ATOM   2740 C  CG  . TYR B 1 85  ? -9.139  0.274   -33.186 1.00 12.11 ? 85  TYR B CG  1 
ATOM   2741 C  CD1 . TYR B 1 85  ? -10.379 -0.220  -32.811 1.00 11.22 ? 85  TYR B CD1 1 
ATOM   2742 C  CD2 . TYR B 1 85  ? -8.655  1.420   -32.557 1.00 12.33 ? 85  TYR B CD2 1 
ATOM   2743 C  CE1 . TYR B 1 85  ? -11.113 0.403   -31.818 1.00 11.54 ? 85  TYR B CE1 1 
ATOM   2744 C  CE2 . TYR B 1 85  ? -9.369  2.046   -31.548 1.00 11.92 ? 85  TYR B CE2 1 
ATOM   2745 C  CZ  . TYR B 1 85  ? -10.607 1.531   -31.191 1.00 12.45 ? 85  TYR B CZ  1 
ATOM   2746 O  OH  . TYR B 1 85  ? -11.335 2.137   -30.223 1.00 12.92 ? 85  TYR B OH  1 
ATOM   2747 N  N   . SER B 1 86  ? -6.978  0.519   -37.283 1.00 11.38 ? 86  SER B N   1 
ATOM   2748 C  CA  . SER B 1 86  ? -5.990  0.338   -38.327 1.00 11.38 ? 86  SER B CA  1 
ATOM   2749 C  C   . SER B 1 86  ? -4.590  0.474   -37.733 1.00 11.17 ? 86  SER B C   1 
ATOM   2750 O  O   . SER B 1 86  ? -4.349  1.366   -36.924 1.00 11.61 ? 86  SER B O   1 
ATOM   2751 C  CB  . SER B 1 86  ? -6.217  1.372   -39.419 1.00 11.46 ? 86  SER B CB  1 
ATOM   2752 O  OG  . SER B 1 86  ? -7.463  1.110   -40.063 1.00 12.46 ? 86  SER B OG  1 
ATOM   2753 N  N   . ALA B 1 87  ? -3.661  -0.388  -38.177 1.00 10.53 ? 87  ALA B N   1 
ATOM   2754 C  CA  . ALA B 1 87  ? -2.318  -0.440  -37.626 1.00 10.09 ? 87  ALA B CA  1 
ATOM   2755 C  C   . ALA B 1 87  ? -1.518  0.824   -37.963 1.00 10.37 ? 87  ALA B C   1 
ATOM   2756 O  O   . ALA B 1 87  ? -1.653  1.415   -39.041 1.00 9.29  ? 87  ALA B O   1 
ATOM   2757 C  CB  . ALA B 1 87  ? -1.613  -1.663  -38.141 1.00 10.25 ? 87  ALA B CB  1 
ATOM   2758 N  N   . THR B 1 88  ? -0.607  1.185   -37.056 1.00 10.51 ? 88  THR B N   1 
ATOM   2759 C  CA  . THR B 1 88  ? 0.350   2.228   -37.389 1.00 11.84 ? 88  THR B CA  1 
ATOM   2760 C  C   . THR B 1 88  ? 1.783   1.697   -37.282 1.00 11.26 ? 88  THR B C   1 
ATOM   2761 O  O   . THR B 1 88  ? 2.612   2.061   -38.108 1.00 10.87 ? 88  THR B O   1 
ATOM   2762 C  CB  . THR B 1 88  ? 0.083   3.525   -36.603 1.00 13.43 ? 88  THR B CB  1 
ATOM   2763 O  OG1 . THR B 1 88  ? 0.952   4.553   -37.102 1.00 17.29 ? 88  THR B OG1 1 
ATOM   2764 C  CG2 . THR B 1 88  ? 0.363   3.373   -35.132 1.00 14.00 ? 88  THR B CG2 1 
ATOM   2765 N  N   . GLN B 1 89  ? 2.061   0.857   -36.266 1.00 9.75  ? 89  GLN B N   1 
ATOM   2766 C  CA  . GLN B 1 89  ? 3.406   0.383   -35.993 1.00 9.32  ? 89  GLN B CA  1 
ATOM   2767 C  C   . GLN B 1 89  ? 3.350   -0.773  -34.995 1.00 8.81  ? 89  GLN B C   1 
ATOM   2768 O  O   . GLN B 1 89  ? 2.329   -0.957  -34.325 1.00 8.87  ? 89  GLN B O   1 
ATOM   2769 C  CB  . GLN B 1 89  ? 4.303   1.533   -35.493 1.00 8.88  ? 89  GLN B CB  1 
ATOM   2770 C  CG  . GLN B 1 89  ? 3.689   2.391   -34.394 1.00 8.94  ? 89  GLN B CG  1 
ATOM   2771 C  CD  . GLN B 1 89  ? 4.265   2.099   -33.028 1.00 9.05  ? 89  GLN B CD  1 
ATOM   2772 O  OE1 . GLN B 1 89  ? 4.657   0.965   -32.715 1.00 9.18  ? 89  GLN B OE1 1 
ATOM   2773 N  NE2 . GLN B 1 89  ? 4.403   3.142   -32.221 1.00 9.09  ? 89  GLN B NE2 1 
ATOM   2774 N  N   . LEU B 1 90  ? 4.456   -1.523  -34.891 1.00 8.14  ? 90  LEU B N   1 
ATOM   2775 C  CA  . LEU B 1 90  ? 4.666   -2.378  -33.737 1.00 8.00  ? 90  LEU B CA  1 
ATOM   2776 C  C   . LEU B 1 90  ? 6.034   -2.045  -33.142 1.00 8.04  ? 90  LEU B C   1 
ATOM   2777 O  O   . LEU B 1 90  ? 6.881   -1.462  -33.819 1.00 7.82  ? 90  LEU B O   1 
ATOM   2778 C  CB  . LEU B 1 90  ? 4.450   -3.860  -34.103 1.00 7.85  ? 90  LEU B CB  1 
ATOM   2779 C  CG  . LEU B 1 90  ? 5.289   -4.463  -35.244 1.00 8.15  ? 90  LEU B CG  1 
ATOM   2780 C  CD1 . LEU B 1 90  ? 6.722   -4.657  -34.772 1.00 7.85  ? 90  LEU B CD1 1 
ATOM   2781 C  CD2 . LEU B 1 90  ? 4.721   -5.820  -35.732 1.00 7.68  ? 90  LEU B CD2 1 
ATOM   2782 N  N   . HIS B 1 91  ? 6.243   -2.426  -31.878 1.00 7.63  ? 91  HIS B N   1 
ATOM   2783 C  CA  . HIS B 1 91  ? 7.476   -2.159  -31.156 1.00 7.93  ? 91  HIS B CA  1 
ATOM   2784 C  C   . HIS B 1 91  ? 7.546   -3.134  -29.984 1.00 7.91  ? 91  HIS B C   1 
ATOM   2785 O  O   . HIS B 1 91  ? 6.602   -3.898  -29.774 1.00 8.16  ? 91  HIS B O   1 
ATOM   2786 C  CB  . HIS B 1 91  ? 7.554   -0.686  -30.700 1.00 7.48  ? 91  HIS B CB  1 
ATOM   2787 C  CG  . HIS B 1 91  ? 6.514   -0.347  -29.688 1.00 7.70  ? 91  HIS B CG  1 
ATOM   2788 N  ND1 . HIS B 1 91  ? 5.259   0.144   -30.048 1.00 7.67  ? 91  HIS B ND1 1 
ATOM   2789 C  CD2 . HIS B 1 91  ? 6.504   -0.491  -28.333 1.00 7.77  ? 91  HIS B CD2 1 
ATOM   2790 C  CE1 . HIS B 1 91  ? 4.552   0.370   -28.938 1.00 7.69  ? 91  HIS B CE1 1 
ATOM   2791 N  NE2 . HIS B 1 91  ? 5.280   -0.050  -27.877 1.00 7.78  ? 91  HIS B NE2 1 
ATOM   2792 N  N   . LEU B 1 92  ? 8.641   -3.097  -29.221 1.00 7.81  ? 92  LEU B N   1 
ATOM   2793 C  CA  . LEU B 1 92  ? 8.815   -4.075  -28.157 1.00 8.51  ? 92  LEU B CA  1 
ATOM   2794 C  C   . LEU B 1 92  ? 9.361   -3.437  -26.883 1.00 8.50  ? 92  LEU B C   1 
ATOM   2795 O  O   . LEU B 1 92  ? 9.926   -2.344  -26.914 1.00 9.72  ? 92  LEU B O   1 
ATOM   2796 C  CB  . LEU B 1 92  ? 9.744   -5.208  -28.606 1.00 8.68  ? 92  LEU B CB  1 
ATOM   2797 C  CG  . LEU B 1 92  ? 9.232   -6.049  -29.762 1.00 8.95  ? 92  LEU B CG  1 
ATOM   2798 C  CD1 . LEU B 1 92  ? 9.897   -5.614  -31.061 1.00 10.02 ? 92  LEU B CD1 1 
ATOM   2799 C  CD2 . LEU B 1 92  ? 9.525   -7.515  -29.490 1.00 9.10  ? 92  LEU B CD2 1 
ATOM   2800 N  N   . HIS B 1 93  ? 9.227   -4.184  -25.783 1.00 8.19  ? 93  HIS B N   1 
ATOM   2801 C  CA  . HIS B 1 93  ? 9.700   -3.778  -24.470 1.00 8.12  ? 93  HIS B CA  1 
ATOM   2802 C  C   . HIS B 1 93  ? 10.445  -4.975  -23.889 1.00 8.46  ? 93  HIS B C   1 
ATOM   2803 O  O   . HIS B 1 93  ? 9.935   -6.094  -23.942 1.00 7.97  ? 93  HIS B O   1 
ATOM   2804 C  CB  . HIS B 1 93  ? 8.515   -3.354  -23.585 1.00 7.90  ? 93  HIS B CB  1 
ATOM   2805 C  CG  . HIS B 1 93  ? 7.694   -2.238  -24.133 1.00 7.84  ? 93  HIS B CG  1 
ATOM   2806 N  ND1 . HIS B 1 93  ? 7.979   -0.905  -23.857 1.00 8.23  ? 93  HIS B ND1 1 
ATOM   2807 C  CD2 . HIS B 1 93  ? 6.605   -2.223  -24.937 1.00 7.73  ? 93  HIS B CD2 1 
ATOM   2808 C  CE1 . HIS B 1 93  ? 7.106   -0.121  -24.475 1.00 7.89  ? 93  HIS B CE1 1 
ATOM   2809 N  NE2 . HIS B 1 93  ? 6.255   -0.893  -25.148 1.00 7.55  ? 93  HIS B NE2 1 
ATOM   2810 N  N   . TRP B 1 94  ? 11.632  -4.727  -23.334 1.00 8.93  ? 94  TRP B N   1 
ATOM   2811 C  CA  . TRP B 1 94  ? 12.448  -5.817  -22.816 1.00 9.65  ? 94  TRP B CA  1 
ATOM   2812 C  C   . TRP B 1 94  ? 13.238  -5.360  -21.580 1.00 9.85  ? 94  TRP B C   1 
ATOM   2813 O  O   . TRP B 1 94  ? 13.261  -4.182  -21.234 1.00 10.02 ? 94  TRP B O   1 
ATOM   2814 C  CB  . TRP B 1 94  ? 13.345  -6.338  -23.949 1.00 9.47  ? 94  TRP B CB  1 
ATOM   2815 C  CG  . TRP B 1 94  ? 14.295  -5.320  -24.506 1.00 9.78  ? 94  TRP B CG  1 
ATOM   2816 C  CD1 . TRP B 1 94  ? 15.554  -5.024  -24.043 1.00 9.71  ? 94  TRP B CD1 1 
ATOM   2817 C  CD2 . TRP B 1 94  ? 14.088  -4.490  -25.673 1.00 9.55  ? 94  TRP B CD2 1 
ATOM   2818 N  NE1 . TRP B 1 94  ? 16.112  -4.030  -24.812 1.00 9.21  ? 94  TRP B NE1 1 
ATOM   2819 C  CE2 . TRP B 1 94  ? 15.248  -3.696  -25.827 1.00 9.32  ? 94  TRP B CE2 1 
ATOM   2820 C  CE3 . TRP B 1 94  ? 13.036  -4.336  -26.590 1.00 9.57  ? 94  TRP B CE3 1 
ATOM   2821 C  CZ2 . TRP B 1 94  ? 15.400  -2.793  -26.881 1.00 8.99  ? 94  TRP B CZ2 1 
ATOM   2822 C  CZ3 . TRP B 1 94  ? 13.168  -3.416  -27.614 1.00 9.93  ? 94  TRP B CZ3 1 
ATOM   2823 C  CH2 . TRP B 1 94  ? 14.343  -2.671  -27.762 1.00 9.61  ? 94  TRP B CH2 1 
ATOM   2824 N  N   . GLY B 1 95  ? 13.904  -6.308  -20.914 1.00 10.52 ? 95  GLY B N   1 
ATOM   2825 C  CA  . GLY B 1 95  ? 14.690  -6.008  -19.724 1.00 11.13 ? 95  GLY B CA  1 
ATOM   2826 C  C   . GLY B 1 95  ? 16.175  -5.917  -20.044 1.00 10.97 ? 95  GLY B C   1 
ATOM   2827 O  O   . GLY B 1 95  ? 16.595  -5.046  -20.805 1.00 11.18 ? 95  GLY B O   1 
ATOM   2828 N  N   . ASN B 1 96  ? 16.964  -6.814  -19.443 1.00 11.45 ? 96  ASN B N   1 
ATOM   2829 C  CA  . ASN B 1 96  ? 18.406  -6.805  -19.674 1.00 11.82 ? 96  ASN B CA  1 
ATOM   2830 C  C   . ASN B 1 96  ? 18.971  -8.186  -19.353 1.00 11.39 ? 96  ASN B C   1 
ATOM   2831 O  O   . ASN B 1 96  ? 18.322  -8.971  -18.655 1.00 11.14 ? 96  ASN B O   1 
ATOM   2832 C  CB  . ASN B 1 96  ? 19.099  -5.663  -18.925 1.00 11.76 ? 96  ASN B CB  1 
ATOM   2833 C  CG  . ASN B 1 96  ? 19.250  -5.950  -17.447 1.00 12.65 ? 96  ASN B CG  1 
ATOM   2834 O  OD1 . ASN B 1 96  ? 20.200  -6.613  -17.030 1.00 12.85 ? 96  ASN B OD1 1 
ATOM   2835 N  ND2 . ASN B 1 96  ? 18.303  -5.493  -16.647 1.00 12.88 ? 96  ASN B ND2 1 
ATOM   2836 N  N   . PRO B 1 97  ? 20.164  -8.557  -19.872 1.00 12.04 ? 97  PRO B N   1 
ATOM   2837 C  CA  . PRO B 1 97  ? 20.669  -9.914  -19.675 1.00 12.83 ? 97  PRO B CA  1 
ATOM   2838 C  C   . PRO B 1 97  ? 20.830  -10.325 -18.206 1.00 12.92 ? 97  PRO B C   1 
ATOM   2839 O  O   . PRO B 1 97  ? 20.718  -11.507 -17.915 1.00 12.68 ? 97  PRO B O   1 
ATOM   2840 C  CB  . PRO B 1 97  ? 21.996  -9.923  -20.455 1.00 12.92 ? 97  PRO B CB  1 
ATOM   2841 C  CG  . PRO B 1 97  ? 21.842  -8.794  -21.457 1.00 12.50 ? 97  PRO B CG  1 
ATOM   2842 C  CD  . PRO B 1 97  ? 21.090  -7.735  -20.682 1.00 11.92 ? 97  PRO B CD  1 
ATOM   2843 N  N   . ASN B 1 98  ? 21.010  -9.359  -17.290 1.00 13.49 ? 98  ASN B N   1 
ATOM   2844 C  CA  . ASN B 1 98  ? 21.125  -9.655  -15.861 1.00 14.95 ? 98  ASN B CA  1 
ATOM   2845 C  C   . ASN B 1 98  ? 19.751  -9.922  -15.244 1.00 14.86 ? 98  ASN B C   1 
ATOM   2846 O  O   . ASN B 1 98  ? 19.673  -10.491 -14.164 1.00 15.98 ? 98  ASN B O   1 
ATOM   2847 C  CB  . ASN B 1 98  ? 21.777  -8.518  -15.058 1.00 16.95 ? 98  ASN B CB  1 
ATOM   2848 C  CG  . ASN B 1 98  ? 23.200  -8.210  -15.488 1.00 19.57 ? 98  ASN B CG  1 
ATOM   2849 O  OD1 . ASN B 1 98  ? 24.041  -9.105  -15.555 1.00 18.67 ? 98  ASN B OD1 1 
ATOM   2850 N  ND2 . ASN B 1 98  ? 23.472  -6.944  -15.790 1.00 20.25 ? 98  ASN B ND2 1 
ATOM   2851 N  N   . ASP B 1 99  ? 18.681  -9.443  -15.890 1.00 13.09 ? 99  ASP B N   1 
ATOM   2852 C  CA  . ASP B 1 99  ? 17.332  -9.522  -15.359 1.00 12.68 ? 99  ASP B CA  1 
ATOM   2853 C  C   . ASP B 1 99  ? 16.387  -9.593  -16.556 1.00 12.32 ? 99  ASP B C   1 
ATOM   2854 O  O   . ASP B 1 99  ? 15.737  -8.607  -16.902 1.00 11.93 ? 99  ASP B O   1 
ATOM   2855 C  CB  . ASP B 1 99  ? 17.025  -8.390  -14.369 1.00 13.54 ? 99  ASP B CB  1 
ATOM   2856 C  CG  . ASP B 1 99  ? 15.822  -8.655  -13.472 1.00 13.65 ? 99  ASP B CG  1 
ATOM   2857 O  OD1 . ASP B 1 99  ? 15.461  -9.808  -13.310 1.00 12.78 ? 99  ASP B OD1 1 
ATOM   2858 O  OD2 . ASP B 1 99  ? 15.250  -7.691  -12.941 1.00 16.69 ? 99  ASP B OD2 1 
ATOM   2859 N  N   . PRO B 1 100 ? 16.338  -10.759 -17.247 1.00 11.55 ? 100 PRO B N   1 
ATOM   2860 C  CA  . PRO B 1 100 ? 15.691  -10.855 -18.561 1.00 11.64 ? 100 PRO B CA  1 
ATOM   2861 C  C   . PRO B 1 100 ? 14.178  -11.029 -18.403 1.00 11.86 ? 100 PRO B C   1 
ATOM   2862 O  O   . PRO B 1 100 ? 13.599  -12.005 -18.867 1.00 10.78 ? 100 PRO B O   1 
ATOM   2863 C  CB  . PRO B 1 100 ? 16.380  -12.115 -19.135 1.00 11.59 ? 100 PRO B CB  1 
ATOM   2864 C  CG  . PRO B 1 100 ? 16.544  -13.007 -17.928 1.00 11.30 ? 100 PRO B CG  1 
ATOM   2865 C  CD  . PRO B 1 100 ? 16.911  -12.045 -16.803 1.00 10.78 ? 100 PRO B CD  1 
ATOM   2866 N  N   . HIS B 1 101 ? 13.551  -10.068 -17.719 1.00 13.04 ? 101 HIS B N   1 
ATOM   2867 C  CA  . HIS B 1 101 ? 12.123  -10.141 -17.458 1.00 13.88 ? 101 HIS B CA  1 
ATOM   2868 C  C   . HIS B 1 101 ? 11.555  -8.731  -17.612 1.00 13.35 ? 101 HIS B C   1 
ATOM   2869 O  O   . HIS B 1 101 ? 11.254  -8.062  -16.637 1.00 14.33 ? 101 HIS B O   1 
ATOM   2870 C  CB  . HIS B 1 101 ? 11.841  -10.732 -16.060 1.00 14.41 ? 101 HIS B CB  1 
ATOM   2871 C  CG  . HIS B 1 101 ? 12.649  -11.939 -15.723 1.00 15.32 ? 101 HIS B CG  1 
ATOM   2872 N  ND1 . HIS B 1 101 ? 12.253  -13.223 -16.066 1.00 15.67 ? 101 HIS B ND1 1 
ATOM   2873 C  CD2 . HIS B 1 101 ? 13.832  -12.069 -15.091 1.00 16.20 ? 101 HIS B CD2 1 
ATOM   2874 C  CE1 . HIS B 1 101 ? 13.161  -14.097 -15.650 1.00 16.50 ? 101 HIS B CE1 1 
ATOM   2875 N  NE2 . HIS B 1 101 ? 14.142  -13.417 -15.052 1.00 17.20 ? 101 HIS B NE2 1 
ATOM   2876 N  N   . GLY B 1 102 ? 11.397  -8.289  -18.855 1.00 12.98 ? 102 GLY B N   1 
ATOM   2877 C  CA  . GLY B 1 102 ? 11.082  -6.892  -19.095 1.00 11.70 ? 102 GLY B CA  1 
ATOM   2878 C  C   . GLY B 1 102 ? 9.769   -6.696  -19.850 1.00 10.55 ? 102 GLY B C   1 
ATOM   2879 O  O   . GLY B 1 102 ? 9.587   -5.676  -20.499 1.00 10.29 ? 102 GLY B O   1 
ATOM   2880 N  N   . SER B 1 103 ? 8.848   -7.653  -19.748 1.00 10.14 ? 103 SER B N   1 
ATOM   2881 C  CA  . SER B 1 103 ? 7.482   -7.385  -20.184 1.00 10.52 ? 103 SER B CA  1 
ATOM   2882 C  C   . SER B 1 103 ? 6.903   -6.199  -19.399 1.00 10.63 ? 103 SER B C   1 
ATOM   2883 O  O   . SER B 1 103 ? 7.357   -5.875  -18.294 1.00 11.14 ? 103 SER B O   1 
ATOM   2884 C  CB  . SER B 1 103 ? 6.591   -8.625  -20.120 1.00 10.41 ? 103 SER B CB  1 
ATOM   2885 O  OG  . SER B 1 103 ? 6.258   -8.958  -18.775 1.00 10.54 ? 103 SER B OG  1 
ATOM   2886 N  N   . GLU B 1 104 ? 5.926   -5.521  -20.001 1.00 9.65  ? 104 GLU B N   1 
ATOM   2887 C  CA  . GLU B 1 104 ? 5.231   -4.454  -19.295 1.00 9.20  ? 104 GLU B CA  1 
ATOM   2888 C  C   . GLU B 1 104 ? 4.150   -5.042  -18.392 1.00 8.59  ? 104 GLU B C   1 
ATOM   2889 O  O   . GLU B 1 104 ? 4.104   -4.749  -17.205 1.00 7.95  ? 104 GLU B O   1 
ATOM   2890 C  CB  . GLU B 1 104 ? 4.682   -3.454  -20.305 1.00 9.19  ? 104 GLU B CB  1 
ATOM   2891 C  CG  . GLU B 1 104 ? 5.792   -2.804  -21.113 1.00 9.66  ? 104 GLU B CG  1 
ATOM   2892 C  CD  . GLU B 1 104 ? 5.515   -1.346  -21.446 1.00 10.49 ? 104 GLU B CD  1 
ATOM   2893 O  OE1 . GLU B 1 104 ? 4.582   -1.095  -22.252 1.00 10.84 ? 104 GLU B OE1 1 
ATOM   2894 O  OE2 . GLU B 1 104 ? 6.184   -0.467  -20.865 1.00 10.70 ? 104 GLU B OE2 1 
ATOM   2895 N  N   . HIS B 1 105 ? 3.273   -5.856  -18.982 1.00 8.54  ? 105 HIS B N   1 
ATOM   2896 C  CA  . HIS B 1 105 ? 2.216   -6.509  -18.233 1.00 8.79  ? 105 HIS B CA  1 
ATOM   2897 C  C   . HIS B 1 105 ? 2.817   -7.660  -17.442 1.00 9.08  ? 105 HIS B C   1 
ATOM   2898 O  O   . HIS B 1 105 ? 3.796   -8.274  -17.878 1.00 9.03  ? 105 HIS B O   1 
ATOM   2899 C  CB  . HIS B 1 105 ? 1.118   -7.001  -19.186 1.00 9.10  ? 105 HIS B CB  1 
ATOM   2900 C  CG  . HIS B 1 105 ? 0.267   -5.876  -19.647 1.00 9.12  ? 105 HIS B CG  1 
ATOM   2901 N  ND1 . HIS B 1 105 ? 0.597   -5.109  -20.751 1.00 9.32  ? 105 HIS B ND1 1 
ATOM   2902 C  CD2 . HIS B 1 105 ? -0.818  -5.299  -19.078 1.00 9.57  ? 105 HIS B CD2 1 
ATOM   2903 C  CE1 . HIS B 1 105 ? -0.287  -4.143  -20.899 1.00 9.95  ? 105 HIS B CE1 1 
ATOM   2904 N  NE2 . HIS B 1 105 ? -1.163  -4.221  -19.861 1.00 10.08 ? 105 HIS B NE2 1 
ATOM   2905 N  N   . THR B 1 106 ? 2.226   -7.923  -16.271 1.00 9.44  ? 106 THR B N   1 
ATOM   2906 C  CA  . THR B 1 106 ? 2.612   -9.081  -15.491 1.00 9.32  ? 106 THR B CA  1 
ATOM   2907 C  C   . THR B 1 106 ? 1.378   -9.952  -15.320 1.00 10.04 ? 106 THR B C   1 
ATOM   2908 O  O   . THR B 1 106 ? 0.256   -9.468  -15.452 1.00 9.71  ? 106 THR B O   1 
ATOM   2909 C  CB  . THR B 1 106 ? 3.260   -8.722  -14.153 1.00 9.16  ? 106 THR B CB  1 
ATOM   2910 O  OG1 . THR B 1 106 ? 2.316   -8.013  -13.355 1.00 9.19  ? 106 THR B OG1 1 
ATOM   2911 C  CG2 . THR B 1 106 ? 4.527   -7.904  -14.266 1.00 8.68  ? 106 THR B CG2 1 
ATOM   2912 N  N   . VAL B 1 107 ? 1.626   -11.243 -15.076 1.00 10.40 ? 107 VAL B N   1 
ATOM   2913 C  CA  . VAL B 1 107 ? 0.576   -12.224 -14.880 1.00 11.60 ? 107 VAL B CA  1 
ATOM   2914 C  C   . VAL B 1 107 ? 0.780   -12.798 -13.485 1.00 11.99 ? 107 VAL B C   1 
ATOM   2915 O  O   . VAL B 1 107 ? 1.805   -13.407 -13.226 1.00 10.85 ? 107 VAL B O   1 
ATOM   2916 C  CB  . VAL B 1 107 ? 0.595   -13.318 -15.973 1.00 11.87 ? 107 VAL B CB  1 
ATOM   2917 C  CG1 . VAL B 1 107 ? -0.467  -14.381 -15.729 1.00 11.80 ? 107 VAL B CG1 1 
ATOM   2918 C  CG2 . VAL B 1 107 ? 0.419   -12.728 -17.363 1.00 11.31 ? 107 VAL B CG2 1 
ATOM   2919 N  N   . SER B 1 108 ? -0.196  -12.535 -12.606 1.00 12.58 ? 108 SER B N   1 
ATOM   2920 C  CA  . SER B 1 108 ? -0.139  -12.911 -11.203 1.00 13.53 ? 108 SER B CA  1 
ATOM   2921 C  C   . SER B 1 108 ? 1.239   -12.555 -10.648 1.00 12.14 ? 108 SER B C   1 
ATOM   2922 O  O   . SER B 1 108 ? 1.927   -13.386 -10.067 1.00 11.03 ? 108 SER B O   1 
ATOM   2923 C  CB  . SER B 1 108 ? -0.542  -14.356 -11.009 1.00 15.73 ? 108 SER B CB  1 
ATOM   2924 O  OG  . SER B 1 108 ? -1.958  -14.451 -11.055 1.00 19.57 ? 108 SER B OG  1 
ATOM   2925 N  N   . GLY B 1 109 ? 1.648   -11.310 -10.920 1.00 11.51 ? 109 GLY B N   1 
ATOM   2926 C  CA  . GLY B 1 109 ? 2.867   -10.753 -10.370 1.00 11.52 ? 109 GLY B CA  1 
ATOM   2927 C  C   . GLY B 1 109 ? 4.150   -11.081 -11.147 1.00 12.02 ? 109 GLY B C   1 
ATOM   2928 O  O   . GLY B 1 109 ? 5.200   -10.519 -10.816 1.00 11.28 ? 109 GLY B O   1 
ATOM   2929 N  N   . GLN B 1 110 ? 4.084   -11.929 -12.194 1.00 10.87 ? 110 GLN B N   1 
ATOM   2930 C  CA  . GLN B 1 110 ? 5.313   -12.345 -12.864 1.00 10.77 ? 110 GLN B CA  1 
ATOM   2931 C  C   . GLN B 1 110 ? 5.438   -11.685 -14.238 1.00 10.14 ? 110 GLN B C   1 
ATOM   2932 O  O   . GLN B 1 110 ? 4.480   -11.698 -15.003 1.00 8.45  ? 110 GLN B O   1 
ATOM   2933 C  CB  . GLN B 1 110 ? 5.356   -13.865 -13.063 1.00 12.21 ? 110 GLN B CB  1 
ATOM   2934 C  CG  . GLN B 1 110 ? 5.398   -14.612 -11.742 1.00 13.14 ? 110 GLN B CG  1 
ATOM   2935 C  CD  . GLN B 1 110 ? 6.836   -14.881 -11.384 1.00 15.47 ? 110 GLN B CD  1 
ATOM   2936 O  OE1 . GLN B 1 110 ? 7.515   -15.668 -12.053 1.00 17.99 ? 110 GLN B OE1 1 
ATOM   2937 N  NE2 . GLN B 1 110 ? 7.320   -14.222 -10.339 1.00 14.28 ? 110 GLN B NE2 1 
ATOM   2938 N  N   . HIS B 1 111 ? 6.636   -11.147 -14.521 1.00 9.31  ? 111 HIS B N   1 
ATOM   2939 C  CA  . HIS B 1 111 ? 6.953   -10.630 -15.841 1.00 9.63  ? 111 HIS B CA  1 
ATOM   2940 C  C   . HIS B 1 111 ? 7.274   -11.803 -16.760 1.00 10.27 ? 111 HIS B C   1 
ATOM   2941 O  O   . HIS B 1 111 ? 7.760   -12.841 -16.292 1.00 10.04 ? 111 HIS B O   1 
ATOM   2942 C  CB  . HIS B 1 111 ? 8.191   -9.734  -15.794 1.00 9.32  ? 111 HIS B CB  1 
ATOM   2943 C  CG  . HIS B 1 111 ? 8.003   -8.429  -15.087 1.00 9.21  ? 111 HIS B CG  1 
ATOM   2944 N  ND1 . HIS B 1 111 ? 7.887   -7.218  -15.784 1.00 9.28  ? 111 HIS B ND1 1 
ATOM   2945 C  CD2 . HIS B 1 111 ? 7.957   -8.118  -13.766 1.00 9.03  ? 111 HIS B CD2 1 
ATOM   2946 C  CE1 . HIS B 1 111 ? 7.757   -6.218  -14.916 1.00 8.96  ? 111 HIS B CE1 1 
ATOM   2947 N  NE2 . HIS B 1 111 ? 7.811   -6.746  -13.671 1.00 8.95  ? 111 HIS B NE2 1 
ATOM   2948 N  N   . PHE B 1 112 ? 7.007   -11.612 -18.056 1.00 10.01 ? 112 PHE B N   1 
ATOM   2949 C  CA  . PHE B 1 112 ? 7.596   -12.415 -19.117 1.00 9.82  ? 112 PHE B CA  1 
ATOM   2950 C  C   . PHE B 1 112 ? 8.910   -11.763 -19.545 1.00 9.62  ? 112 PHE B C   1 
ATOM   2951 O  O   . PHE B 1 112 ? 9.256   -10.694 -19.061 1.00 9.71  ? 112 PHE B O   1 
ATOM   2952 C  CB  . PHE B 1 112 ? 6.593   -12.568 -20.264 1.00 10.34 ? 112 PHE B CB  1 
ATOM   2953 C  CG  . PHE B 1 112 ? 5.480   -13.542 -19.975 1.00 10.92 ? 112 PHE B CG  1 
ATOM   2954 C  CD1 . PHE B 1 112 ? 4.408   -13.180 -19.175 1.00 11.15 ? 112 PHE B CD1 1 
ATOM   2955 C  CD2 . PHE B 1 112 ? 5.528   -14.837 -20.469 1.00 10.79 ? 112 PHE B CD2 1 
ATOM   2956 C  CE1 . PHE B 1 112 ? 3.403   -14.098 -18.885 1.00 11.29 ? 112 PHE B CE1 1 
ATOM   2957 C  CE2 . PHE B 1 112 ? 4.537   -15.755 -20.158 1.00 11.24 ? 112 PHE B CE2 1 
ATOM   2958 C  CZ  . PHE B 1 112 ? 3.464   -15.376 -19.389 1.00 11.33 ? 112 PHE B CZ  1 
ATOM   2959 N  N   . ALA B 1 113 ? 9.654   -12.413 -20.451 1.00 9.86  ? 113 ALA B N   1 
ATOM   2960 C  CA  . ALA B 1 113 ? 10.953  -11.908 -20.874 1.00 9.54  ? 113 ALA B CA  1 
ATOM   2961 C  C   . ALA B 1 113 ? 10.796  -10.536 -21.546 1.00 9.63  ? 113 ALA B C   1 
ATOM   2962 O  O   . ALA B 1 113 ? 11.558  -9.614  -21.259 1.00 9.59  ? 113 ALA B O   1 
ATOM   2963 C  CB  . ALA B 1 113 ? 11.612  -12.905 -21.795 1.00 9.24  ? 113 ALA B CB  1 
ATOM   2964 N  N   . ALA B 1 114 ? 9.791   -10.408 -22.424 1.00 8.97  ? 114 ALA B N   1 
ATOM   2965 C  CA  . ALA B 1 114 ? 9.607   -9.199  -23.217 1.00 9.21  ? 114 ALA B CA  1 
ATOM   2966 C  C   . ALA B 1 114 ? 8.152   -9.117  -23.654 1.00 9.13  ? 114 ALA B C   1 
ATOM   2967 O  O   . ALA B 1 114 ? 7.349   -9.992  -23.321 1.00 9.23  ? 114 ALA B O   1 
ATOM   2968 C  CB  . ALA B 1 114 ? 10.541  -9.178  -24.422 1.00 8.73  ? 114 ALA B CB  1 
ATOM   2969 N  N   . GLU B 1 115 ? 7.836   -8.058  -24.415 1.00 9.00  ? 115 GLU B N   1 
ATOM   2970 C  CA  . GLU B 1 115 ? 6.465   -7.845  -24.816 1.00 9.05  ? 115 GLU B CA  1 
ATOM   2971 C  C   . GLU B 1 115 ? 6.471   -7.064  -26.124 1.00 8.82  ? 115 GLU B C   1 
ATOM   2972 O  O   . GLU B 1 115 ? 7.153   -6.052  -26.236 1.00 8.25  ? 115 GLU B O   1 
ATOM   2973 C  CB  . GLU B 1 115 ? 5.690   -7.161  -23.681 1.00 8.48  ? 115 GLU B CB  1 
ATOM   2974 C  CG  . GLU B 1 115 ? 4.199   -6.950  -23.942 1.00 8.57  ? 115 GLU B CG  1 
ATOM   2975 C  CD  . GLU B 1 115 ? 3.457   -6.473  -22.691 1.00 8.69  ? 115 GLU B CD  1 
ATOM   2976 O  OE1 . GLU B 1 115 ? 2.361   -5.874  -22.826 1.00 8.46  ? 115 GLU B OE1 1 
ATOM   2977 O  OE2 . GLU B 1 115 ? 4.008   -6.656  -21.562 1.00 8.68  ? 115 GLU B OE2 1 
ATOM   2978 N  N   . LEU B 1 116 ? 5.651   -7.545  -27.069 1.00 9.01  ? 116 LEU B N   1 
ATOM   2979 C  CA  . LEU B 1 116 ? 5.395   -6.883  -28.341 1.00 9.39  ? 116 LEU B CA  1 
ATOM   2980 C  C   . LEU B 1 116 ? 4.052   -6.158  -28.326 1.00 8.93  ? 116 LEU B C   1 
ATOM   2981 O  O   . LEU B 1 116 ? 3.032   -6.688  -27.887 1.00 8.85  ? 116 LEU B O   1 
ATOM   2982 C  CB  . LEU B 1 116 ? 5.374   -7.955  -29.441 1.00 10.21 ? 116 LEU B CB  1 
ATOM   2983 C  CG  . LEU B 1 116 ? 5.066   -7.448  -30.849 1.00 10.92 ? 116 LEU B CG  1 
ATOM   2984 C  CD1 . LEU B 1 116 ? 6.361   -7.164  -31.593 1.00 12.42 ? 116 LEU B CD1 1 
ATOM   2985 C  CD2 . LEU B 1 116 ? 4.274   -8.502  -31.610 1.00 11.63 ? 116 LEU B CD2 1 
ATOM   2986 N  N   . HIS B 1 117 ? 4.036   -4.979  -28.940 1.00 8.63  ? 117 HIS B N   1 
ATOM   2987 C  CA  . HIS B 1 117 ? 2.835   -4.169  -29.003 1.00 8.68  ? 117 HIS B CA  1 
ATOM   2988 C  C   . HIS B 1 117 ? 2.572   -3.812  -30.465 1.00 8.89  ? 117 HIS B C   1 
ATOM   2989 O  O   . HIS B 1 117 ? 3.447   -3.258  -31.131 1.00 9.03  ? 117 HIS B O   1 
ATOM   2990 C  CB  . HIS B 1 117 ? 3.032   -2.881  -28.170 1.00 8.12  ? 117 HIS B CB  1 
ATOM   2991 C  CG  . HIS B 1 117 ? 3.000   -3.106  -26.694 1.00 7.92  ? 117 HIS B CG  1 
ATOM   2992 N  ND1 . HIS B 1 117 ? 3.523   -2.195  -25.764 1.00 8.19  ? 117 HIS B ND1 1 
ATOM   2993 C  CD2 . HIS B 1 117 ? 2.520   -4.138  -25.976 1.00 7.61  ? 117 HIS B CD2 1 
ATOM   2994 C  CE1 . HIS B 1 117 ? 3.345   -2.671  -24.537 1.00 7.65  ? 117 HIS B CE1 1 
ATOM   2995 N  NE2 . HIS B 1 117 ? 2.735   -3.859  -24.646 1.00 7.44  ? 117 HIS B NE2 1 
ATOM   2996 N  N   . ILE B 1 118 ? 1.361   -4.119  -30.940 1.00 8.78  ? 118 ILE B N   1 
ATOM   2997 C  CA  . ILE B 1 118 ? 0.956   -3.694  -32.268 1.00 8.35  ? 118 ILE B CA  1 
ATOM   2998 C  C   . ILE B 1 118 ? -0.051  -2.563  -32.067 1.00 8.29  ? 118 ILE B C   1 
ATOM   2999 O  O   . ILE B 1 118 ? -1.162  -2.787  -31.574 1.00 8.02  ? 118 ILE B O   1 
ATOM   3000 C  CB  . ILE B 1 118 ? 0.374   -4.871  -33.102 1.00 8.09  ? 118 ILE B CB  1 
ATOM   3001 C  CG1 . ILE B 1 118 ? 1.247   -6.131  -33.031 1.00 7.97  ? 118 ILE B CG1 1 
ATOM   3002 C  CG2 . ILE B 1 118 ? 0.160   -4.417  -34.531 1.00 7.70  ? 118 ILE B CG2 1 
ATOM   3003 C  CD1 . ILE B 1 118 ? 0.809   -7.281  -33.943 1.00 8.09  ? 118 ILE B CD1 1 
ATOM   3004 N  N   . VAL B 1 119 ? 0.355   -1.352  -32.458 1.00 7.91  ? 119 VAL B N   1 
ATOM   3005 C  CA  . VAL B 1 119 ? -0.426  -0.161  -32.169 1.00 7.95  ? 119 VAL B CA  1 
ATOM   3006 C  C   . VAL B 1 119 ? -1.335  0.124   -33.361 1.00 7.96  ? 119 VAL B C   1 
ATOM   3007 O  O   . VAL B 1 119 ? -0.865  0.146   -34.491 1.00 7.41  ? 119 VAL B O   1 
ATOM   3008 C  CB  . VAL B 1 119 ? 0.500   1.046   -31.918 1.00 7.87  ? 119 VAL B CB  1 
ATOM   3009 C  CG1 . VAL B 1 119 ? -0.288  2.310   -31.644 1.00 7.86  ? 119 VAL B CG1 1 
ATOM   3010 C  CG2 . VAL B 1 119 ? 1.483   0.772   -30.805 1.00 8.26  ? 119 VAL B CG2 1 
ATOM   3011 N  N   . HIS B 1 120 ? -2.632  0.329   -33.074 1.00 8.49  ? 120 HIS B N   1 
ATOM   3012 C  CA  . HIS B 1 120 ? -3.660  0.670   -34.046 1.00 8.63  ? 120 HIS B CA  1 
ATOM   3013 C  C   . HIS B 1 120 ? -4.408  1.899   -33.547 1.00 8.66  ? 120 HIS B C   1 
ATOM   3014 O  O   . HIS B 1 120 ? -4.393  2.155   -32.334 1.00 8.42  ? 120 HIS B O   1 
ATOM   3015 C  CB  . HIS B 1 120 ? -4.691  -0.454  -34.130 1.00 8.74  ? 120 HIS B CB  1 
ATOM   3016 C  CG  . HIS B 1 120 ? -4.149  -1.775  -34.532 1.00 8.86  ? 120 HIS B CG  1 
ATOM   3017 N  ND1 . HIS B 1 120 ? -3.425  -2.570  -33.662 1.00 9.24  ? 120 HIS B ND1 1 
ATOM   3018 C  CD2 . HIS B 1 120 ? -4.338  -2.501  -35.658 1.00 9.42  ? 120 HIS B CD2 1 
ATOM   3019 C  CE1 . HIS B 1 120 ? -3.132  -3.716  -34.258 1.00 9.23  ? 120 HIS B CE1 1 
ATOM   3020 N  NE2 . HIS B 1 120 ? -3.674  -3.695  -35.500 1.00 9.38  ? 120 HIS B NE2 1 
ATOM   3021 N  N   . TYR B 1 121 ? -5.020  2.644   -34.487 1.00 8.33  ? 121 TYR B N   1 
ATOM   3022 C  CA  . TYR B 1 121 ? -5.761  3.856   -34.153 1.00 9.15  ? 121 TYR B CA  1 
ATOM   3023 C  C   . TYR B 1 121 ? -7.173  3.768   -34.720 1.00 9.30  ? 121 TYR B C   1 
ATOM   3024 O  O   . TYR B 1 121 ? -7.424  2.998   -35.649 1.00 9.33  ? 121 TYR B O   1 
ATOM   3025 C  CB  . TYR B 1 121 ? -5.051  5.119   -34.666 1.00 9.08  ? 121 TYR B CB  1 
ATOM   3026 C  CG  . TYR B 1 121 ? -4.966  5.195   -36.168 1.00 9.55  ? 121 TYR B CG  1 
ATOM   3027 C  CD1 . TYR B 1 121 ? -4.004  4.491   -36.868 1.00 9.83  ? 121 TYR B CD1 1 
ATOM   3028 C  CD2 . TYR B 1 121 ? -5.853  5.969   -36.891 1.00 9.94  ? 121 TYR B CD2 1 
ATOM   3029 C  CE1 . TYR B 1 121 ? -3.954  4.511   -38.251 1.00 9.61  ? 121 TYR B CE1 1 
ATOM   3030 C  CE2 . TYR B 1 121 ? -5.800  6.024   -38.277 1.00 10.08 ? 121 TYR B CE2 1 
ATOM   3031 C  CZ  . TYR B 1 121 ? -4.845  5.297   -38.957 1.00 9.84  ? 121 TYR B CZ  1 
ATOM   3032 O  OH  . TYR B 1 121 ? -4.812  5.341   -40.318 1.00 9.66  ? 121 TYR B OH  1 
ATOM   3033 N  N   . ASN B 1 122 ? -8.094  4.513   -34.103 1.00 10.17 ? 122 ASN B N   1 
ATOM   3034 C  CA  . ASN B 1 122 ? -9.481  4.514   -34.531 1.00 11.31 ? 122 ASN B CA  1 
ATOM   3035 C  C   . ASN B 1 122 ? -9.560  5.264   -35.861 1.00 11.49 ? 122 ASN B C   1 
ATOM   3036 O  O   . ASN B 1 122 ? -9.544  6.501   -35.881 1.00 10.51 ? 122 ASN B O   1 
ATOM   3037 C  CB  . ASN B 1 122 ? -10.419 5.074   -33.450 1.00 12.19 ? 122 ASN B CB  1 
ATOM   3038 C  CG  . ASN B 1 122 ? -11.872 5.092   -33.881 1.00 14.08 ? 122 ASN B CG  1 
ATOM   3039 O  OD1 . ASN B 1 122 ? -12.185 4.977   -35.068 1.00 13.67 ? 122 ASN B OD1 1 
ATOM   3040 N  ND2 . ASN B 1 122 ? -12.777 5.237   -32.923 1.00 15.56 ? 122 ASN B ND2 1 
ATOM   3041 N  N   . SER B 1 123 ? -9.623  4.496   -36.965 1.00 10.96 ? 123 SER B N   1 
ATOM   3042 C  CA  . SER B 1 123 ? -9.559  5.097   -38.292 1.00 11.97 ? 123 SER B CA  1 
ATOM   3043 C  C   . SER B 1 123 ? -10.951 5.515   -38.780 1.00 12.39 ? 123 SER B C   1 
ATOM   3044 O  O   . SER B 1 123 ? -11.059 6.227   -39.777 1.00 11.60 ? 123 SER B O   1 
ATOM   3045 C  CB  . SER B 1 123 ? -8.833  4.226   -39.299 1.00 11.74 ? 123 SER B CB  1 
ATOM   3046 O  OG  . SER B 1 123 ? -9.346  2.888   -39.309 1.00 11.31 ? 123 SER B OG  1 
ATOM   3047 N  N   . ASP B 1 124 ? -12.004 5.056   -38.073 1.00 12.39 ? 124 ASP B N   1 
ATOM   3048 C  CA  . ASP B 1 124 ? -13.349 5.565   -38.289 1.00 12.93 ? 124 ASP B CA  1 
ATOM   3049 C  C   . ASP B 1 124 ? -13.388 7.078   -38.036 1.00 13.63 ? 124 ASP B C   1 
ATOM   3050 O  O   . ASP B 1 124 ? -14.031 7.791   -38.796 1.00 13.51 ? 124 ASP B O   1 
ATOM   3051 C  CB  . ASP B 1 124 ? -14.398 4.753   -37.529 1.00 12.42 ? 124 ASP B CB  1 
ATOM   3052 C  CG  . ASP B 1 124 ? -14.508 3.315   -38.011 1.00 12.89 ? 124 ASP B CG  1 
ATOM   3053 O  OD1 . ASP B 1 124 ? -14.211 3.060   -39.212 1.00 12.20 ? 124 ASP B OD1 1 
ATOM   3054 O  OD2 . ASP B 1 124 ? -14.879 2.457   -37.193 1.00 12.63 ? 124 ASP B OD2 1 
ATOM   3055 N  N   . LEU B 1 125 ? -12.643 7.568   -37.032 1.00 12.94 ? 125 LEU B N   1 
ATOM   3056 C  CA  . LEU B 1 125 ? -12.731 8.955   -36.589 1.00 14.50 ? 125 LEU B CA  1 
ATOM   3057 C  C   . LEU B 1 125 ? -11.477 9.787   -36.881 1.00 15.19 ? 125 LEU B C   1 
ATOM   3058 O  O   . LEU B 1 125 ? -11.602 10.982  -37.155 1.00 14.69 ? 125 LEU B O   1 
ATOM   3059 C  CB  . LEU B 1 125 ? -13.023 8.968   -35.085 1.00 16.09 ? 125 LEU B CB  1 
ATOM   3060 C  CG  . LEU B 1 125 ? -14.477 8.684   -34.712 1.00 16.25 ? 125 LEU B CG  1 
ATOM   3061 C  CD1 . LEU B 1 125 ? -14.641 8.771   -33.204 1.00 16.40 ? 125 LEU B CD1 1 
ATOM   3062 C  CD2 . LEU B 1 125 ? -15.390 9.688   -35.404 1.00 18.09 ? 125 LEU B CD2 1 
ATOM   3063 N  N   . TYR B 1 126 ? -10.279 9.180   -36.821 1.00 14.99 ? 126 TYR B N   1 
ATOM   3064 C  CA  . TYR B 1 126 ? -9.040  9.954   -36.849 1.00 15.87 ? 126 TYR B CA  1 
ATOM   3065 C  C   . TYR B 1 126 ? -8.187  9.573   -38.053 1.00 15.97 ? 126 TYR B C   1 
ATOM   3066 O  O   . TYR B 1 126 ? -8.271  8.446   -38.527 1.00 17.18 ? 126 TYR B O   1 
ATOM   3067 C  CB  . TYR B 1 126 ? -8.319  9.814   -35.508 1.00 15.46 ? 126 TYR B CB  1 
ATOM   3068 C  CG  . TYR B 1 126 ? -9.271  10.165  -34.402 1.00 16.08 ? 126 TYR B CG  1 
ATOM   3069 C  CD1 . TYR B 1 126 ? -9.797  11.444  -34.323 1.00 15.80 ? 126 TYR B CD1 1 
ATOM   3070 C  CD2 . TYR B 1 126 ? -9.732  9.196   -33.522 1.00 16.23 ? 126 TYR B CD2 1 
ATOM   3071 C  CE1 . TYR B 1 126 ? -10.731 11.767  -33.355 1.00 16.06 ? 126 TYR B CE1 1 
ATOM   3072 C  CE2 . TYR B 1 126 ? -10.656 9.504   -32.538 1.00 16.34 ? 126 TYR B CE2 1 
ATOM   3073 C  CZ  . TYR B 1 126 ? -11.143 10.797  -32.455 1.00 16.26 ? 126 TYR B CZ  1 
ATOM   3074 O  OH  . TYR B 1 126 ? -12.045 11.100  -31.492 1.00 16.29 ? 126 TYR B OH  1 
ATOM   3075 N  N   . PRO B 1 127 ? -7.354  10.487  -38.600 1.00 16.33 ? 127 PRO B N   1 
ATOM   3076 C  CA  . PRO B 1 127 ? -6.469  10.131  -39.714 1.00 16.99 ? 127 PRO B CA  1 
ATOM   3077 C  C   . PRO B 1 127 ? -5.213  9.343   -39.337 1.00 17.01 ? 127 PRO B C   1 
ATOM   3078 O  O   . PRO B 1 127 ? -4.618  8.686   -40.199 1.00 16.27 ? 127 PRO B O   1 
ATOM   3079 C  CB  . PRO B 1 127 ? -6.126  11.478  -40.380 1.00 16.98 ? 127 PRO B CB  1 
ATOM   3080 C  CG  . PRO B 1 127 ? -6.434  12.540  -39.353 1.00 16.88 ? 127 PRO B CG  1 
ATOM   3081 C  CD  . PRO B 1 127 ? -7.297  11.918  -38.266 1.00 17.04 ? 127 PRO B CD  1 
ATOM   3082 N  N   . ASP B 1 128 ? -4.814  9.414   -38.056 1.00 16.38 ? 128 ASP B N   1 
ATOM   3083 C  CA  . ASP B 1 128 ? -3.590  8.768   -37.596 1.00 17.06 ? 128 ASP B CA  1 
ATOM   3084 C  C   . ASP B 1 128 ? -3.614  8.582   -36.076 1.00 15.85 ? 128 ASP B C   1 
ATOM   3085 O  O   . ASP B 1 128 ? -4.482  9.127   -35.397 1.00 14.03 ? 128 ASP B O   1 
ATOM   3086 C  CB  . ASP B 1 128 ? -2.343  9.541   -38.059 1.00 20.42 ? 128 ASP B CB  1 
ATOM   3087 C  CG  . ASP B 1 128 ? -2.459  11.049  -37.895 1.00 21.72 ? 128 ASP B CG  1 
ATOM   3088 O  OD1 . ASP B 1 128 ? -2.772  11.502  -36.768 1.00 21.81 ? 128 ASP B OD1 1 
ATOM   3089 O  OD2 . ASP B 1 128 ? -2.273  11.751  -38.900 1.00 24.57 ? 128 ASP B OD2 1 
ATOM   3090 N  N   . ALA B 1 129 ? -2.603  7.860   -35.560 1.00 15.23 ? 129 ALA B N   1 
ATOM   3091 C  CA  . ALA B 1 129 ? -2.487  7.542   -34.140 1.00 15.14 ? 129 ALA B CA  1 
ATOM   3092 C  C   . ALA B 1 129 ? -2.255  8.807   -33.310 1.00 14.53 ? 129 ALA B C   1 
ATOM   3093 O  O   . ALA B 1 129 ? -2.840  8.987   -32.238 1.00 13.78 ? 129 ALA B O   1 
ATOM   3094 C  CB  . ALA B 1 129 ? -1.393  6.522   -33.915 1.00 13.17 ? 129 ALA B CB  1 
ATOM   3095 N  N   . SER B 1 130 ? -1.392  9.681   -33.833 1.00 14.55 ? 130 SER B N   1 
ATOM   3096 C  CA  . SER B 1 130 ? -1.060  10.923  -33.162 1.00 14.55 ? 130 SER B CA  1 
ATOM   3097 C  C   . SER B 1 130 ? -2.329  11.739  -32.887 1.00 15.41 ? 130 SER B C   1 
ATOM   3098 O  O   . SER B 1 130 ? -2.534  12.220  -31.763 1.00 14.70 ? 130 SER B O   1 
ATOM   3099 C  CB  . SER B 1 130 ? 0.016   11.666  -33.945 1.00 15.85 ? 130 SER B CB  1 
ATOM   3100 O  OG  . SER B 1 130 ? -0.057  13.054  -33.685 1.00 17.69 ? 130 SER B OG  1 
ATOM   3101 N  N   . THR B 1 131 ? -3.215  11.853  -33.887 1.00 13.75 ? 131 THR B N   1 
ATOM   3102 C  CA  . THR B 1 131 ? -4.475  12.563  -33.683 1.00 14.63 ? 131 THR B CA  1 
ATOM   3103 C  C   . THR B 1 131 ? -5.411  11.800  -32.744 1.00 13.97 ? 131 THR B C   1 
ATOM   3104 O  O   . THR B 1 131 ? -6.079  12.408  -31.903 1.00 14.04 ? 131 THR B O   1 
ATOM   3105 C  CB  . THR B 1 131 ? -5.188  12.846  -35.015 1.00 16.08 ? 131 THR B CB  1 
ATOM   3106 O  OG1 . THR B 1 131 ? -4.252  13.534  -35.849 1.00 17.21 ? 131 THR B OG1 1 
ATOM   3107 C  CG2 . THR B 1 131 ? -6.463  13.642  -34.846 1.00 14.68 ? 131 THR B CG2 1 
ATOM   3108 N  N   . ALA B 1 132 ? -5.477  10.471  -32.919 1.00 12.63 ? 132 ALA B N   1 
ATOM   3109 C  CA  . ALA B 1 132 ? -6.359  9.610   -32.155 1.00 12.84 ? 132 ALA B CA  1 
ATOM   3110 C  C   . ALA B 1 132 ? -5.955  9.539   -30.677 1.00 13.24 ? 132 ALA B C   1 
ATOM   3111 O  O   . ALA B 1 132 ? -6.794  9.237   -29.822 1.00 13.28 ? 132 ALA B O   1 
ATOM   3112 C  CB  . ALA B 1 132 ? -6.335  8.228   -32.778 1.00 12.85 ? 132 ALA B CB  1 
ATOM   3113 N  N   . SER B 1 133 ? -4.677  9.823   -30.392 1.00 13.27 ? 133 SER B N   1 
ATOM   3114 C  CA  . SER B 1 133 ? -4.003  9.412   -29.165 1.00 14.16 ? 133 SER B CA  1 
ATOM   3115 C  C   . SER B 1 133 ? -4.541  10.153  -27.941 1.00 15.71 ? 133 SER B C   1 
ATOM   3116 O  O   . SER B 1 133 ? -4.413  9.649   -26.825 1.00 15.19 ? 133 SER B O   1 
ATOM   3117 C  CB  . SER B 1 133 ? -2.481  9.506   -29.267 1.00 13.60 ? 133 SER B CB  1 
ATOM   3118 O  OG  . SER B 1 133 ? -2.043  10.851  -29.310 1.00 13.52 ? 133 SER B OG  1 
ATOM   3119 N  N   . ASN B 1 134 ? -5.135  11.337  -28.142 1.00 16.10 ? 134 ASN B N   1 
ATOM   3120 C  CA  . ASN B 1 134 ? -5.699  12.046  -26.998 1.00 17.93 ? 134 ASN B CA  1 
ATOM   3121 C  C   . ASN B 1 134 ? -7.227  11.947  -26.974 1.00 17.65 ? 134 ASN B C   1 
ATOM   3122 O  O   . ASN B 1 134 ? -7.879  12.656  -26.213 1.00 18.10 ? 134 ASN B O   1 
ATOM   3123 C  CB  . ASN B 1 134 ? -5.078  13.441  -26.781 1.00 20.50 ? 134 ASN B CB  1 
ATOM   3124 C  CG  . ASN B 1 134 ? -5.485  14.474  -27.811 1.00 23.70 ? 134 ASN B CG  1 
ATOM   3125 O  OD1 . ASN B 1 134 ? -5.189  15.666  -27.660 1.00 24.20 ? 134 ASN B OD1 1 
ATOM   3126 N  ND2 . ASN B 1 134 ? -6.185  14.037  -28.846 1.00 22.54 ? 134 ASN B ND2 1 
ATOM   3127 N  N   . LYS B 1 135 ? -7.806  11.043  -27.772 1.00 17.27 ? 135 LYS B N   1 
ATOM   3128 C  CA  . LYS B 1 135 ? -9.263  10.964  -27.874 1.00 17.25 ? 135 LYS B CA  1 
ATOM   3129 C  C   . LYS B 1 135 ? -9.766  9.649   -27.274 1.00 17.57 ? 135 LYS B C   1 
ATOM   3130 O  O   . LYS B 1 135 ? -9.082  8.624   -27.335 1.00 15.33 ? 135 LYS B O   1 
ATOM   3131 C  CB  . LYS B 1 135 ? -9.700  11.193  -29.325 1.00 16.83 ? 135 LYS B CB  1 
ATOM   3132 C  CG  . LYS B 1 135 ? -9.585  12.643  -29.805 1.00 17.40 ? 135 LYS B CG  1 
ATOM   3133 C  CD  . LYS B 1 135 ? -10.712 13.540  -29.332 0.01 17.21 ? 135 LYS B CD  1 
ATOM   3134 C  CE  . LYS B 1 135 ? -10.582 14.964  -29.830 0.01 17.22 ? 135 LYS B CE  1 
ATOM   3135 N  NZ  . LYS B 1 135 ? -11.701 15.815  -29.360 0.01 17.20 ? 135 LYS B NZ  1 
ATOM   3136 N  N   . SER B 1 136 ? -10.959 9.703   -26.677 1.00 17.48 ? 136 SER B N   1 
ATOM   3137 C  CA  . SER B 1 136 ? -11.527 8.540   -26.015 1.00 19.98 ? 136 SER B CA  1 
ATOM   3138 C  C   . SER B 1 136 ? -11.537 7.368   -26.997 1.00 19.11 ? 136 SER B C   1 
ATOM   3139 O  O   . SER B 1 136 ? -11.935 7.535   -28.142 1.00 17.94 ? 136 SER B O   1 
ATOM   3140 C  CB  . SER B 1 136 ? -12.909 8.874   -25.518 1.00 23.18 ? 136 SER B CB  1 
ATOM   3141 O  OG  . SER B 1 136 ? -13.394 7.852   -24.670 1.00 28.37 ? 136 SER B OG  1 
ATOM   3142 N  N   . GLU B 1 137 ? -11.024 6.214   -26.561 1.00 19.35 ? 137 GLU B N   1 
ATOM   3143 C  CA  . GLU B 1 137 ? -10.975 5.001   -27.368 1.00 20.22 ? 137 GLU B CA  1 
ATOM   3144 C  C   . GLU B 1 137 ? -10.242 5.268   -28.683 1.00 17.69 ? 137 GLU B C   1 
ATOM   3145 O  O   . GLU B 1 137 ? -10.557 4.660   -29.711 1.00 17.38 ? 137 GLU B O   1 
ATOM   3146 C  CB  . GLU B 1 137 ? -12.386 4.485   -27.673 1.00 24.84 ? 137 GLU B CB  1 
ATOM   3147 C  CG  . GLU B 1 137 ? -13.299 4.450   -26.467 1.00 31.71 ? 137 GLU B CG  1 
ATOM   3148 C  CD  . GLU B 1 137 ? -13.814 3.093   -26.029 1.00 38.78 ? 137 GLU B CD  1 
ATOM   3149 O  OE1 . GLU B 1 137 ? -14.908 2.708   -26.504 1.00 38.59 ? 137 GLU B OE1 1 
ATOM   3150 O  OE2 . GLU B 1 137 ? -13.141 2.445   -25.176 1.00 46.98 ? 137 GLU B OE2 1 
ATOM   3151 N  N   . GLY B 1 138 ? -9.267  6.185   -28.660 1.00 13.91 ? 138 GLY B N   1 
ATOM   3152 C  CA  . GLY B 1 138 ? -8.566  6.529   -29.887 1.00 12.16 ? 138 GLY B CA  1 
ATOM   3153 C  C   . GLY B 1 138 ? -7.633  5.423   -30.393 1.00 11.03 ? 138 GLY B C   1 
ATOM   3154 O  O   . GLY B 1 138 ? -7.341  5.360   -31.590 1.00 10.57 ? 138 GLY B O   1 
ATOM   3155 N  N   . LEU B 1 139 ? -7.184  4.537   -29.487 1.00 10.17 ? 139 LEU B N   1 
ATOM   3156 C  CA  . LEU B 1 139 ? -6.158  3.550   -29.817 1.00 9.72  ? 139 LEU B CA  1 
ATOM   3157 C  C   . LEU B 1 139 ? -6.535  2.161   -29.302 1.00 9.40  ? 139 LEU B C   1 
ATOM   3158 O  O   . LEU B 1 139 ? -7.266  2.018   -28.326 1.00 9.59  ? 139 LEU B O   1 
ATOM   3159 C  CB  . LEU B 1 139 ? -4.821  3.958   -29.176 1.00 9.02  ? 139 LEU B CB  1 
ATOM   3160 C  CG  . LEU B 1 139 ? -4.287  5.336   -29.526 1.00 8.80  ? 139 LEU B CG  1 
ATOM   3161 C  CD1 . LEU B 1 139 ? -3.147  5.714   -28.585 1.00 9.07  ? 139 LEU B CD1 1 
ATOM   3162 C  CD2 . LEU B 1 139 ? -3.831  5.390   -30.976 1.00 8.72  ? 139 LEU B CD2 1 
ATOM   3163 N  N   . ALA B 1 140 ? -5.960  1.143   -29.944 1.00 9.04  ? 140 ALA B N   1 
ATOM   3164 C  CA  . ALA B 1 140 ? -6.106  -0.253  -29.550 1.00 8.90  ? 140 ALA B CA  1 
ATOM   3165 C  C   . ALA B 1 140 ? -4.756  -0.934  -29.789 1.00 8.67  ? 140 ALA B C   1 
ATOM   3166 O  O   . ALA B 1 140 ? -4.186  -0.781  -30.869 1.00 7.73  ? 140 ALA B O   1 
ATOM   3167 C  CB  . ALA B 1 140 ? -7.232  -0.898  -30.349 1.00 8.56  ? 140 ALA B CB  1 
ATOM   3168 N  N   . VAL B 1 141 ? -4.217  -1.598  -28.746 1.00 8.98  ? 141 VAL B N   1 
ATOM   3169 C  CA  . VAL B 1 141 ? -2.924  -2.262  -28.846 1.00 8.76  ? 141 VAL B CA  1 
ATOM   3170 C  C   . VAL B 1 141 ? -3.134  -3.768  -28.667 1.00 8.53  ? 141 VAL B C   1 
ATOM   3171 O  O   . VAL B 1 141 ? -3.854  -4.178  -27.767 1.00 7.85  ? 141 VAL B O   1 
ATOM   3172 C  CB  . VAL B 1 141 ? -1.928  -1.732  -27.787 1.00 9.34  ? 141 VAL B CB  1 
ATOM   3173 C  CG1 . VAL B 1 141 ? -0.600  -2.476  -27.824 1.00 8.89  ? 141 VAL B CG1 1 
ATOM   3174 C  CG2 . VAL B 1 141 ? -1.679  -0.235  -27.907 1.00 8.89  ? 141 VAL B CG2 1 
ATOM   3175 N  N   . LEU B 1 142 ? -2.490  -4.576  -29.526 1.00 7.83  ? 142 LEU B N   1 
ATOM   3176 C  CA  . LEU B 1 142 ? -2.383  -6.006  -29.274 1.00 7.61  ? 142 LEU B CA  1 
ATOM   3177 C  C   . LEU B 1 142 ? -1.029  -6.232  -28.624 1.00 7.92  ? 142 LEU B C   1 
ATOM   3178 O  O   . LEU B 1 142 ? 0.006   -5.777  -29.132 1.00 7.85  ? 142 LEU B O   1 
ATOM   3179 C  CB  . LEU B 1 142 ? -2.476  -6.791  -30.590 1.00 7.39  ? 142 LEU B CB  1 
ATOM   3180 C  CG  . LEU B 1 142 ? -3.706  -6.515  -31.456 1.00 7.31  ? 142 LEU B CG  1 
ATOM   3181 C  CD1 . LEU B 1 142 ? -3.539  -7.206  -32.807 1.00 7.22  ? 142 LEU B CD1 1 
ATOM   3182 C  CD2 . LEU B 1 142 ? -4.970  -7.008  -30.739 1.00 7.19  ? 142 LEU B CD2 1 
ATOM   3183 N  N   . ALA B 1 143 ? -1.064  -6.927  -27.489 1.00 8.35  ? 143 ALA B N   1 
ATOM   3184 C  CA  . ALA B 1 143 ? 0.132   -7.147  -26.704 1.00 8.44  ? 143 ALA B CA  1 
ATOM   3185 C  C   . ALA B 1 143 ? 0.410   -8.644  -26.695 1.00 8.90  ? 143 ALA B C   1 
ATOM   3186 O  O   . ALA B 1 143 ? -0.481  -9.436  -26.427 1.00 9.09  ? 143 ALA B O   1 
ATOM   3187 C  CB  . ALA B 1 143 ? -0.049  -6.582  -25.317 1.00 8.50  ? 143 ALA B CB  1 
ATOM   3188 N  N   . VAL B 1 144 ? 1.642   -9.013  -27.059 1.00 9.37  ? 144 VAL B N   1 
ATOM   3189 C  CA  . VAL B 1 144 ? 2.047   -10.408 -27.091 1.00 9.61  ? 144 VAL B CA  1 
ATOM   3190 C  C   . VAL B 1 144 ? 3.175   -10.562 -26.084 1.00 9.67  ? 144 VAL B C   1 
ATOM   3191 O  O   . VAL B 1 144 ? 4.151   -9.808  -26.167 1.00 8.80  ? 144 VAL B O   1 
ATOM   3192 C  CB  . VAL B 1 144 ? 2.507   -10.856 -28.492 1.00 9.60  ? 144 VAL B CB  1 
ATOM   3193 C  CG1 . VAL B 1 144 ? 2.977   -12.316 -28.451 1.00 9.70  ? 144 VAL B CG1 1 
ATOM   3194 C  CG2 . VAL B 1 144 ? 1.435   -10.636 -29.572 1.00 9.11  ? 144 VAL B CG2 1 
ATOM   3195 N  N   . LEU B 1 145 ? 2.986   -11.495 -25.127 1.00 10.03 ? 145 LEU B N   1 
ATOM   3196 C  CA  . LEU B 1 145 ? 3.963   -11.809 -24.085 1.00 10.37 ? 145 LEU B CA  1 
ATOM   3197 C  C   . LEU B 1 145 ? 4.958   -12.826 -24.631 1.00 11.81 ? 145 LEU B C   1 
ATOM   3198 O  O   . LEU B 1 145 ? 4.561   -13.774 -25.331 1.00 11.26 ? 145 LEU B O   1 
ATOM   3199 C  CB  . LEU B 1 145 ? 3.258   -12.394 -22.858 1.00 10.25 ? 145 LEU B CB  1 
ATOM   3200 C  CG  . LEU B 1 145 ? 2.179   -11.519 -22.207 1.00 9.92  ? 145 LEU B CG  1 
ATOM   3201 C  CD1 . LEU B 1 145 ? 1.387   -12.365 -21.224 1.00 10.51 ? 145 LEU B CD1 1 
ATOM   3202 C  CD2 . LEU B 1 145 ? 2.778   -10.323 -21.478 1.00 9.78  ? 145 LEU B CD2 1 
ATOM   3203 N  N   . ILE B 1 146 ? 6.246   -12.595 -24.327 1.00 12.18 ? 146 ILE B N   1 
ATOM   3204 C  CA  . ILE B 1 146 ? 7.335   -13.335 -24.953 1.00 12.96 ? 146 ILE B CA  1 
ATOM   3205 C  C   . ILE B 1 146 ? 8.155   -14.024 -23.867 1.00 13.61 ? 146 ILE B C   1 
ATOM   3206 O  O   . ILE B 1 146 ? 8.545   -13.373 -22.910 1.00 13.81 ? 146 ILE B O   1 
ATOM   3207 C  CB  . ILE B 1 146 ? 8.205   -12.380 -25.789 1.00 13.04 ? 146 ILE B CB  1 
ATOM   3208 C  CG1 . ILE B 1 146 ? 7.385   -11.704 -26.897 1.00 12.30 ? 146 ILE B CG1 1 
ATOM   3209 C  CG2 . ILE B 1 146 ? 9.444   -13.099 -26.333 1.00 13.26 ? 146 ILE B CG2 1 
ATOM   3210 C  CD1 . ILE B 1 146 ? 8.085   -10.533 -27.565 1.00 12.91 ? 146 ILE B CD1 1 
ATOM   3211 N  N   . GLU B 1 147 ? 8.377   -15.340 -24.018 1.00 14.13 ? 147 GLU B N   1 
ATOM   3212 C  CA  . GLU B 1 147 ? 9.239   -16.083 -23.113 1.00 16.46 ? 147 GLU B CA  1 
ATOM   3213 C  C   . GLU B 1 147 ? 10.359  -16.746 -23.925 1.00 18.26 ? 147 GLU B C   1 
ATOM   3214 O  O   . GLU B 1 147 ? 10.304  -16.837 -25.153 1.00 17.66 ? 147 GLU B O   1 
ATOM   3215 C  CB  . GLU B 1 147 ? 8.456   -17.087 -22.248 1.00 16.76 ? 147 GLU B CB  1 
ATOM   3216 C  CG  . GLU B 1 147 ? 8.038   -18.383 -22.960 1.00 17.68 ? 147 GLU B CG  1 
ATOM   3217 C  CD  . GLU B 1 147 ? 6.977   -19.288 -22.319 1.00 19.10 ? 147 GLU B CD  1 
ATOM   3218 O  OE1 . GLU B 1 147 ? 6.576   -19.018 -21.186 1.00 20.65 ? 147 GLU B OE1 1 
ATOM   3219 O  OE2 . GLU B 1 147 ? 6.539   -20.277 -22.956 1.00 19.15 ? 147 GLU B OE2 1 
ATOM   3220 N  N   . MET B 1 148 ? 11.383  -17.205 -23.207 1.00 19.16 ? 148 MET B N   1 
ATOM   3221 C  CA  . MET B 1 148 ? 12.507  -17.907 -23.783 1.00 22.35 ? 148 MET B CA  1 
ATOM   3222 C  C   . MET B 1 148 ? 12.064  -19.335 -24.077 1.00 20.86 ? 148 MET B C   1 
ATOM   3223 O  O   . MET B 1 148 ? 11.426  -19.955 -23.230 1.00 20.66 ? 148 MET B O   1 
ATOM   3224 C  CB  . MET B 1 148 ? 13.619  -17.912 -22.733 1.00 28.31 ? 148 MET B CB  1 
ATOM   3225 C  CG  . MET B 1 148 ? 14.991  -18.310 -23.231 1.00 37.37 ? 148 MET B CG  1 
ATOM   3226 S  SD  . MET B 1 148 ? 16.236  -17.603 -22.100 1.00 50.63 ? 148 MET B SD  1 
ATOM   3227 C  CE  . MET B 1 148 ? 15.495  -17.997 -20.516 1.00 42.09 ? 148 MET B CE  1 
ATOM   3228 N  N   . GLY B 1 149 ? 12.360  -19.821 -25.292 1.00 18.35 ? 149 GLY B N   1 
ATOM   3229 C  CA  . GLY B 1 149 ? 12.144  -21.218 -25.630 1.00 18.03 ? 149 GLY B CA  1 
ATOM   3230 C  C   . GLY B 1 149 ? 12.784  -21.550 -26.974 1.00 18.20 ? 149 GLY B C   1 
ATOM   3231 O  O   . GLY B 1 149 ? 13.923  -21.152 -27.223 1.00 17.86 ? 149 GLY B O   1 
ATOM   3232 N  N   . SER B 1 150 ? 12.028  -22.210 -27.860 1.00 17.14 ? 150 SER B N   1 
ATOM   3233 C  CA  . SER B 1 150 ? 12.583  -22.560 -29.160 1.00 17.04 ? 150 SER B CA  1 
ATOM   3234 C  C   . SER B 1 150 ? 12.755  -21.318 -30.032 1.00 16.45 ? 150 SER B C   1 
ATOM   3235 O  O   . SER B 1 150 ? 12.084  -20.308 -29.836 1.00 16.10 ? 150 SER B O   1 
ATOM   3236 C  CB  . SER B 1 150 ? 11.754  -23.610 -29.842 1.00 19.15 ? 150 SER B CB  1 
ATOM   3237 O  OG  . SER B 1 150 ? 10.381  -23.271 -29.752 1.00 24.07 ? 150 SER B OG  1 
ATOM   3238 N  N   . PHE B 1 151 ? 13.696  -21.397 -30.976 1.00 15.92 ? 151 PHE B N   1 
ATOM   3239 C  CA  . PHE B 1 151 ? 13.937  -20.358 -31.963 1.00 15.66 ? 151 PHE B CA  1 
ATOM   3240 C  C   . PHE B 1 151 ? 12.640  -20.039 -32.716 1.00 15.63 ? 151 PHE B C   1 
ATOM   3241 O  O   . PHE B 1 151 ? 11.822  -20.933 -32.979 1.00 14.97 ? 151 PHE B O   1 
ATOM   3242 C  CB  . PHE B 1 151 ? 15.072  -20.807 -32.889 1.00 15.46 ? 151 PHE B CB  1 
ATOM   3243 C  CG  . PHE B 1 151 ? 15.264  -19.947 -34.115 1.00 16.13 ? 151 PHE B CG  1 
ATOM   3244 C  CD1 . PHE B 1 151 ? 16.011  -18.782 -34.060 1.00 16.27 ? 151 PHE B CD1 1 
ATOM   3245 C  CD2 . PHE B 1 151 ? 14.654  -20.281 -35.318 1.00 16.01 ? 151 PHE B CD2 1 
ATOM   3246 C  CE1 . PHE B 1 151 ? 16.156  -17.983 -35.188 1.00 16.10 ? 151 PHE B CE1 1 
ATOM   3247 C  CE2 . PHE B 1 151 ? 14.827  -19.498 -36.447 1.00 15.94 ? 151 PHE B CE2 1 
ATOM   3248 C  CZ  . PHE B 1 151 ? 15.569  -18.345 -36.379 1.00 15.44 ? 151 PHE B CZ  1 
ATOM   3249 N  N   . ASN B 1 152 ? 12.444  -18.745 -33.025 1.00 14.48 ? 152 ASN B N   1 
ATOM   3250 C  CA  . ASN B 1 152 ? 11.225  -18.305 -33.677 1.00 13.81 ? 152 ASN B CA  1 
ATOM   3251 C  C   . ASN B 1 152 ? 11.599  -17.658 -35.005 1.00 13.60 ? 152 ASN B C   1 
ATOM   3252 O  O   . ASN B 1 152 ? 12.116  -16.537 -35.011 1.00 13.67 ? 152 ASN B O   1 
ATOM   3253 C  CB  . ASN B 1 152 ? 10.404  -17.396 -32.753 1.00 14.78 ? 152 ASN B CB  1 
ATOM   3254 C  CG  . ASN B 1 152 ? 9.022   -17.080 -33.276 1.00 14.64 ? 152 ASN B CG  1 
ATOM   3255 O  OD1 . ASN B 1 152 ? 8.865   -16.710 -34.439 1.00 14.86 ? 152 ASN B OD1 1 
ATOM   3256 N  ND2 . ASN B 1 152 ? 8.015   -17.232 -32.430 1.00 14.53 ? 152 ASN B ND2 1 
ATOM   3257 N  N   . PRO B 1 153 ? 11.373  -18.345 -36.163 1.00 14.22 ? 153 PRO B N   1 
ATOM   3258 C  CA  . PRO B 1 153 ? 11.729  -17.798 -37.474 1.00 14.05 ? 153 PRO B CA  1 
ATOM   3259 C  C   . PRO B 1 153 ? 10.991  -16.501 -37.786 1.00 13.96 ? 153 PRO B C   1 
ATOM   3260 O  O   . PRO B 1 153 ? 11.517  -15.637 -38.461 1.00 14.74 ? 153 PRO B O   1 
ATOM   3261 C  CB  . PRO B 1 153 ? 11.305  -18.892 -38.471 1.00 13.12 ? 153 PRO B CB  1 
ATOM   3262 C  CG  . PRO B 1 153 ? 11.230  -20.154 -37.661 1.00 13.49 ? 153 PRO B CG  1 
ATOM   3263 C  CD  . PRO B 1 153 ? 10.805  -19.706 -36.278 1.00 13.40 ? 153 PRO B CD  1 
ATOM   3264 N  N   . SER B 1 154 ? 9.744   -16.395 -37.337 1.00 14.96 ? 154 SER B N   1 
ATOM   3265 C  CA  . SER B 1 154 ? 8.904   -15.251 -37.663 1.00 14.68 ? 154 SER B CA  1 
ATOM   3266 C  C   . SER B 1 154 ? 9.446   -14.004 -36.972 1.00 14.81 ? 154 SER B C   1 
ATOM   3267 O  O   . SER B 1 154 ? 9.527   -12.956 -37.608 1.00 14.84 ? 154 SER B O   1 
ATOM   3268 C  CB  . SER B 1 154 ? 7.488   -15.483 -37.221 1.00 15.71 ? 154 SER B CB  1 
ATOM   3269 O  OG  . SER B 1 154 ? 6.911   -16.557 -37.936 1.00 16.60 ? 154 SER B OG  1 
ATOM   3270 N  N   . TYR B 1 155 ? 9.739   -14.116 -35.656 1.00 14.12 ? 155 TYR B N   1 
ATOM   3271 C  CA  . TYR B 1 155 ? 10.357  -13.025 -34.914 1.00 13.57 ? 155 TYR B CA  1 
ATOM   3272 C  C   . TYR B 1 155 ? 11.713  -12.679 -35.511 1.00 13.51 ? 155 TYR B C   1 
ATOM   3273 O  O   . TYR B 1 155 ? 12.070  -11.508 -35.578 1.00 13.32 ? 155 TYR B O   1 
ATOM   3274 C  CB  . TYR B 1 155 ? 10.416  -13.308 -33.408 1.00 12.21 ? 155 TYR B CB  1 
ATOM   3275 C  CG  . TYR B 1 155 ? 9.124   -12.905 -32.732 1.00 11.16 ? 155 TYR B CG  1 
ATOM   3276 C  CD1 . TYR B 1 155 ? 8.026   -13.749 -32.745 1.00 10.54 ? 155 TYR B CD1 1 
ATOM   3277 C  CD2 . TYR B 1 155 ? 8.977   -11.648 -32.159 1.00 10.75 ? 155 TYR B CD2 1 
ATOM   3278 C  CE1 . TYR B 1 155 ? 6.815   -13.372 -32.184 1.00 10.44 ? 155 TYR B CE1 1 
ATOM   3279 C  CE2 . TYR B 1 155 ? 7.793   -11.276 -31.538 1.00 10.21 ? 155 TYR B CE2 1 
ATOM   3280 C  CZ  . TYR B 1 155 ? 6.705   -12.133 -31.573 1.00 10.52 ? 155 TYR B CZ  1 
ATOM   3281 O  OH  . TYR B 1 155 ? 5.527   -11.764 -30.999 1.00 10.73 ? 155 TYR B OH  1 
ATOM   3282 N  N   . ASP B 1 156 ? 12.424  -13.694 -36.011 1.00 13.95 ? 156 ASP B N   1 
ATOM   3283 C  CA  . ASP B 1 156 ? 13.725  -13.409 -36.600 1.00 15.67 ? 156 ASP B CA  1 
ATOM   3284 C  C   . ASP B 1 156 ? 13.608  -12.533 -37.855 1.00 15.44 ? 156 ASP B C   1 
ATOM   3285 O  O   . ASP B 1 156 ? 14.600  -11.940 -38.271 1.00 14.42 ? 156 ASP B O   1 
ATOM   3286 C  CB  . ASP B 1 156 ? 14.564  -14.662 -36.821 1.00 16.34 ? 156 ASP B CB  1 
ATOM   3287 C  CG  . ASP B 1 156 ? 16.007  -14.437 -36.386 1.00 19.68 ? 156 ASP B CG  1 
ATOM   3288 O  OD1 . ASP B 1 156 ? 16.234  -14.035 -35.193 1.00 18.31 ? 156 ASP B OD1 1 
ATOM   3289 O  OD2 . ASP B 1 156 ? 16.892  -14.624 -37.237 1.00 19.72 ? 156 ASP B OD2 1 
ATOM   3290 N  N   . LYS B 1 157 ? 12.409  -12.441 -38.456 1.00 16.15 ? 157 LYS B N   1 
ATOM   3291 C  CA  . LYS B 1 157 ? 12.229  -11.574 -39.617 1.00 17.04 ? 157 LYS B CA  1 
ATOM   3292 C  C   . LYS B 1 157 ? 12.428  -10.113 -39.205 1.00 17.72 ? 157 LYS B C   1 
ATOM   3293 O  O   . LYS B 1 157 ? 12.752  -9.259  -40.035 1.00 18.42 ? 157 LYS B O   1 
ATOM   3294 C  CB  . LYS B 1 157 ? 10.881  -11.850 -40.298 1.00 18.54 ? 157 LYS B CB  1 
ATOM   3295 C  CG  . LYS B 1 157 ? 10.781  -13.257 -40.880 1.00 20.14 ? 157 LYS B CG  1 
ATOM   3296 C  CD  . LYS B 1 157 ? 9.448   -13.618 -41.517 1.00 22.11 ? 157 LYS B CD  1 
ATOM   3297 C  CE  . LYS B 1 157 ? 9.414   -15.074 -41.969 1.00 24.38 ? 157 LYS B CE  1 
ATOM   3298 N  NZ  . LYS B 1 157 ? 8.070   -15.528 -42.413 1.00 26.66 ? 157 LYS B NZ  1 
ATOM   3299 N  N   . ILE B 1 158 ? 12.250  -9.831  -37.908 1.00 15.31 ? 158 ILE B N   1 
ATOM   3300 C  CA  . ILE B 1 158 ? 12.570  -8.509  -37.393 1.00 13.90 ? 158 ILE B CA  1 
ATOM   3301 C  C   . ILE B 1 158 ? 13.995  -8.504  -36.844 1.00 13.71 ? 158 ILE B C   1 
ATOM   3302 O  O   . ILE B 1 158 ? 14.766  -7.587  -37.138 1.00 13.10 ? 158 ILE B O   1 
ATOM   3303 C  CB  . ILE B 1 158 ? 11.530  -8.043  -36.344 1.00 13.03 ? 158 ILE B CB  1 
ATOM   3304 C  CG1 . ILE B 1 158 ? 10.115  -7.958  -36.927 1.00 12.88 ? 158 ILE B CG1 1 
ATOM   3305 C  CG2 . ILE B 1 158 ? 11.940  -6.716  -35.750 1.00 13.19 ? 158 ILE B CG2 1 
ATOM   3306 C  CD1 . ILE B 1 158 ? 9.027   -7.774  -35.885 1.00 13.90 ? 158 ILE B CD1 1 
ATOM   3307 N  N   . PHE B 1 159 ? 14.329  -9.516  -36.019 1.00 13.11 ? 159 PHE B N   1 
ATOM   3308 C  CA  . PHE B 1 159 ? 15.496  -9.409  -35.157 1.00 13.63 ? 159 PHE B CA  1 
ATOM   3309 C  C   . PHE B 1 159 ? 16.765  -9.498  -35.999 1.00 13.03 ? 159 PHE B C   1 
ATOM   3310 O  O   . PHE B 1 159 ? 17.799  -8.940  -35.632 1.00 11.09 ? 159 PHE B O   1 
ATOM   3311 C  CB  . PHE B 1 159 ? 15.488  -10.516 -34.090 1.00 15.01 ? 159 PHE B CB  1 
ATOM   3312 C  CG  . PHE B 1 159 ? 14.387  -10.445 -33.055 1.00 16.28 ? 159 PHE B CG  1 
ATOM   3313 C  CD1 . PHE B 1 159 ? 13.714  -9.262  -32.801 1.00 17.11 ? 159 PHE B CD1 1 
ATOM   3314 C  CD2 . PHE B 1 159 ? 14.047  -11.562 -32.310 1.00 17.03 ? 159 PHE B CD2 1 
ATOM   3315 C  CE1 . PHE B 1 159 ? 12.738  -9.203  -31.812 1.00 18.47 ? 159 PHE B CE1 1 
ATOM   3316 C  CE2 . PHE B 1 159 ? 13.065  -11.507 -31.333 1.00 17.34 ? 159 PHE B CE2 1 
ATOM   3317 C  CZ  . PHE B 1 159 ? 12.410  -10.324 -31.090 1.00 17.39 ? 159 PHE B CZ  1 
ATOM   3318 N  N   . SER B 1 160 ? 16.675  -10.212 -37.134 1.00 12.96 ? 160 SER B N   1 
ATOM   3319 C  CA  . SER B 1 160 ? 17.784  -10.258 -38.073 1.00 13.33 ? 160 SER B CA  1 
ATOM   3320 C  C   . SER B 1 160 ? 18.153  -8.856  -38.578 1.00 14.27 ? 160 SER B C   1 
ATOM   3321 O  O   . SER B 1 160 ? 19.206  -8.692  -39.187 1.00 13.98 ? 160 SER B O   1 
ATOM   3322 C  CB  . SER B 1 160 ? 17.473  -11.193 -39.222 1.00 13.05 ? 160 SER B CB  1 
ATOM   3323 O  OG  . SER B 1 160 ? 16.392  -10.674 -40.000 1.00 12.59 ? 160 SER B OG  1 
ATOM   3324 N  N   . HIS B 1 161 ? 17.313  -7.836  -38.312 1.00 14.94 ? 161 HIS B N   1 
ATOM   3325 C  CA  . HIS B 1 161 ? 17.580  -6.480  -38.777 1.00 14.54 ? 161 HIS B CA  1 
ATOM   3326 C  C   . HIS B 1 161 ? 18.026  -5.552  -37.644 1.00 15.15 ? 161 HIS B C   1 
ATOM   3327 O  O   . HIS B 1 161 ? 18.318  -4.372  -37.881 1.00 13.64 ? 161 HIS B O   1 
ATOM   3328 C  CB  . HIS B 1 161 ? 16.354  -5.912  -39.527 1.00 14.84 ? 161 HIS B CB  1 
ATOM   3329 C  CG  . HIS B 1 161 ? 16.119  -6.536  -40.866 1.00 16.06 ? 161 HIS B CG  1 
ATOM   3330 N  ND1 . HIS B 1 161 ? 16.923  -6.248  -41.969 1.00 15.67 ? 161 HIS B ND1 1 
ATOM   3331 C  CD2 . HIS B 1 161 ? 15.203  -7.442  -41.286 1.00 16.55 ? 161 HIS B CD2 1 
ATOM   3332 C  CE1 . HIS B 1 161 ? 16.479  -6.914  -43.018 1.00 16.63 ? 161 HIS B CE1 1 
ATOM   3333 N  NE2 . HIS B 1 161 ? 15.424  -7.655  -42.626 1.00 17.35 ? 161 HIS B NE2 1 
ATOM   3334 N  N   . LEU B 1 162 ? 18.091  -6.067  -36.411 1.00 15.39 ? 162 LEU B N   1 
ATOM   3335 C  CA  . LEU B 1 162 ? 18.403  -5.196  -35.281 1.00 15.58 ? 162 LEU B CA  1 
ATOM   3336 C  C   . LEU B 1 162 ? 19.747  -4.515  -35.511 1.00 15.99 ? 162 LEU B C   1 
ATOM   3337 O  O   . LEU B 1 162 ? 19.955  -3.361  -35.112 1.00 14.93 ? 162 LEU B O   1 
ATOM   3338 C  CB  . LEU B 1 162 ? 18.487  -6.024  -33.991 1.00 15.02 ? 162 LEU B CB  1 
ATOM   3339 C  CG  . LEU B 1 162 ? 17.165  -6.489  -33.390 1.00 14.52 ? 162 LEU B CG  1 
ATOM   3340 C  CD1 . LEU B 1 162 ? 17.454  -7.604  -32.388 1.00 14.28 ? 162 LEU B CD1 1 
ATOM   3341 C  CD2 . LEU B 1 162 ? 16.474  -5.329  -32.695 1.00 14.66 ? 162 LEU B CD2 1 
ATOM   3342 N  N   . GLN B 1 163 ? 20.648  -5.289  -36.124 1.00 16.48 ? 163 GLN B N   1 
ATOM   3343 C  CA  . GLN B 1 163 ? 22.018  -4.908  -36.420 1.00 19.15 ? 163 GLN B CA  1 
ATOM   3344 C  C   . GLN B 1 163 ? 22.050  -3.661  -37.300 1.00 17.91 ? 163 GLN B C   1 
ATOM   3345 O  O   . GLN B 1 163 ? 23.068  -2.985  -37.360 1.00 18.23 ? 163 GLN B O   1 
ATOM   3346 C  CB  . GLN B 1 163 ? 22.759  -6.086  -37.064 1.00 22.27 ? 163 GLN B CB  1 
ATOM   3347 C  CG  . GLN B 1 163 ? 22.047  -6.670  -38.288 1.00 25.14 ? 163 GLN B CG  1 
ATOM   3348 C  CD  . GLN B 1 163 ? 22.795  -7.804  -38.956 1.00 30.39 ? 163 GLN B CD  1 
ATOM   3349 O  OE1 . GLN B 1 163 ? 24.031  -7.866  -38.953 1.00 30.55 ? 163 GLN B OE1 1 
ATOM   3350 N  NE2 . GLN B 1 163 ? 22.038  -8.711  -39.564 1.00 31.54 ? 163 GLN B NE2 1 
ATOM   3351 N  N   . HIS B 1 164 ? 20.937  -3.331  -37.965 1.00 17.22 ? 164 HIS B N   1 
ATOM   3352 C  CA  . HIS B 1 164 ? 20.964  -2.187  -38.863 1.00 16.31 ? 164 HIS B CA  1 
ATOM   3353 C  C   . HIS B 1 164 ? 20.280  -0.961  -38.261 1.00 16.44 ? 164 HIS B C   1 
ATOM   3354 O  O   . HIS B 1 164 ? 20.105  0.036   -38.963 1.00 16.41 ? 164 HIS B O   1 
ATOM   3355 C  CB  . HIS B 1 164 ? 20.385  -2.493  -40.244 1.00 18.84 ? 164 HIS B CB  1 
ATOM   3356 C  CG  . HIS B 1 164 ? 21.088  -3.581  -40.972 1.00 22.18 ? 164 HIS B CG  1 
ATOM   3357 N  ND1 . HIS B 1 164 ? 20.411  -4.460  -41.795 1.00 25.47 ? 164 HIS B ND1 1 
ATOM   3358 C  CD2 . HIS B 1 164 ? 22.385  -3.951  -40.983 1.00 23.41 ? 164 HIS B CD2 1 
ATOM   3359 C  CE1 . HIS B 1 164 ? 21.266  -5.329  -42.294 1.00 27.06 ? 164 HIS B CE1 1 
ATOM   3360 N  NE2 . HIS B 1 164 ? 22.490  -5.031  -41.810 1.00 25.97 ? 164 HIS B NE2 1 
ATOM   3361 N  N   . VAL B 1 165 ? 19.917  -1.021  -36.974 1.00 14.83 ? 165 VAL B N   1 
ATOM   3362 C  CA  . VAL B 1 165 ? 19.282  0.109   -36.301 1.00 14.09 ? 165 VAL B CA  1 
ATOM   3363 C  C   . VAL B 1 165 ? 19.876  0.257   -34.896 1.00 14.70 ? 165 VAL B C   1 
ATOM   3364 O  O   . VAL B 1 165 ? 19.164  0.560   -33.943 1.00 14.75 ? 165 VAL B O   1 
ATOM   3365 C  CB  . VAL B 1 165 ? 17.744  -0.038  -36.258 1.00 13.52 ? 165 VAL B CB  1 
ATOM   3366 C  CG1 . VAL B 1 165 ? 17.119  0.126   -37.658 1.00 12.00 ? 165 VAL B CG1 1 
ATOM   3367 C  CG2 . VAL B 1 165 ? 17.326  -1.368  -35.618 1.00 11.63 ? 165 VAL B CG2 1 
ATOM   3368 N  N   . LYS B 1 166 ? 21.203  0.136   -34.803 1.00 14.51 ? 166 LYS B N   1 
ATOM   3369 C  CA  . LYS B 1 166 ? 21.937  0.140   -33.545 1.00 16.09 ? 166 LYS B CA  1 
ATOM   3370 C  C   . LYS B 1 166 ? 21.756  1.432   -32.741 1.00 16.08 ? 166 LYS B C   1 
ATOM   3371 O  O   . LYS B 1 166 ? 21.815  1.415   -31.516 1.00 15.49 ? 166 LYS B O   1 
ATOM   3372 C  CB  . LYS B 1 166 ? 23.410  -0.184  -33.812 1.00 18.41 ? 166 LYS B CB  1 
ATOM   3373 C  CG  . LYS B 1 166 ? 23.738  -1.668  -33.661 1.00 21.51 ? 166 LYS B CG  1 
ATOM   3374 C  CD  . LYS B 1 166 ? 25.044  -2.139  -34.249 1.00 23.40 ? 166 LYS B CD  1 
ATOM   3375 C  CE  . LYS B 1 166 ? 25.618  -3.321  -33.498 1.00 27.40 ? 166 LYS B CE  1 
ATOM   3376 N  NZ  . LYS B 1 166 ? 24.576  -4.143  -32.821 1.00 29.07 ? 166 LYS B NZ  1 
ATOM   3377 N  N   . TYR B 1 167 ? 21.516  2.558   -33.418 1.00 15.41 ? 167 TYR B N   1 
ATOM   3378 C  CA  . TYR B 1 167 ? 21.520  3.836   -32.725 1.00 15.20 ? 167 TYR B CA  1 
ATOM   3379 C  C   . TYR B 1 167 ? 20.255  4.624   -33.022 1.00 15.09 ? 167 TYR B C   1 
ATOM   3380 O  O   . TYR B 1 167 ? 19.646  4.449   -34.067 1.00 13.14 ? 167 TYR B O   1 
ATOM   3381 C  CB  . TYR B 1 167 ? 22.702  4.686   -33.185 1.00 15.28 ? 167 TYR B CB  1 
ATOM   3382 C  CG  . TYR B 1 167 ? 24.052  4.157   -32.774 1.00 15.36 ? 167 TYR B CG  1 
ATOM   3383 C  CD1 . TYR B 1 167 ? 24.768  3.295   -33.591 1.00 16.16 ? 167 TYR B CD1 1 
ATOM   3384 C  CD2 . TYR B 1 167 ? 24.617  4.543   -31.573 1.00 14.97 ? 167 TYR B CD2 1 
ATOM   3385 C  CE1 . TYR B 1 167 ? 26.033  2.848   -33.235 1.00 16.60 ? 167 TYR B CE1 1 
ATOM   3386 C  CE2 . TYR B 1 167 ? 25.868  4.094   -31.192 1.00 15.91 ? 167 TYR B CE2 1 
ATOM   3387 C  CZ  . TYR B 1 167 ? 26.578  3.245   -32.023 1.00 16.02 ? 167 TYR B CZ  1 
ATOM   3388 O  OH  . TYR B 1 167 ? 27.812  2.830   -31.633 1.00 14.85 ? 167 TYR B OH  1 
ATOM   3389 N  N   . LYS B 1 168 ? 19.899  5.501   -32.071 1.00 14.93 ? 168 LYS B N   1 
ATOM   3390 C  CA  . LYS B 1 168 ? 18.772  6.403   -32.222 1.00 15.38 ? 168 LYS B CA  1 
ATOM   3391 C  C   . LYS B 1 168 ? 18.868  7.097   -33.581 1.00 14.83 ? 168 LYS B C   1 
ATOM   3392 O  O   . LYS B 1 168 ? 19.907  7.653   -33.909 1.00 14.18 ? 168 LYS B O   1 
ATOM   3393 C  CB  . LYS B 1 168 ? 18.830  7.459   -31.111 1.00 15.43 ? 168 LYS B CB  1 
ATOM   3394 C  CG  . LYS B 1 168 ? 17.800  8.556   -31.264 1.00 16.31 ? 168 LYS B CG  1 
ATOM   3395 C  CD  . LYS B 1 168 ? 17.487  9.206   -29.956 1.00 17.44 ? 168 LYS B CD  1 
ATOM   3396 C  CE  . LYS B 1 168 ? 16.042  9.647   -29.993 1.00 18.50 ? 168 LYS B CE  1 
ATOM   3397 N  NZ  . LYS B 1 168 ? 15.918  11.003  -29.433 1.00 17.41 ? 168 LYS B NZ  1 
ATOM   3398 N  N   . GLY B 1 169 ? 17.799  7.010   -34.377 1.00 14.45 ? 169 GLY B N   1 
ATOM   3399 C  CA  . GLY B 1 169 ? 17.710  7.746   -35.624 1.00 15.93 ? 169 GLY B CA  1 
ATOM   3400 C  C   . GLY B 1 169 ? 17.912  6.838   -36.832 1.00 16.08 ? 169 GLY B C   1 
ATOM   3401 O  O   . GLY B 1 169 ? 17.569  7.204   -37.951 1.00 16.17 ? 169 GLY B O   1 
ATOM   3402 N  N   . GLN B 1 170 ? 18.451  5.640   -36.603 1.00 16.39 ? 170 GLN B N   1 
ATOM   3403 C  CA  . GLN B 1 170 ? 18.759  4.781   -37.733 1.00 16.95 ? 170 GLN B CA  1 
ATOM   3404 C  C   . GLN B 1 170 ? 17.486  4.107   -38.233 1.00 17.50 ? 170 GLN B C   1 
ATOM   3405 O  O   . GLN B 1 170 ? 16.556  3.894   -37.457 1.00 17.63 ? 170 GLN B O   1 
ATOM   3406 C  CB  . GLN B 1 170 ? 19.883  3.807   -37.378 1.00 17.01 ? 170 GLN B CB  1 
ATOM   3407 C  CG  . GLN B 1 170 ? 21.215  4.519   -37.215 1.00 16.96 ? 170 GLN B CG  1 
ATOM   3408 C  CD  . GLN B 1 170 ? 22.348  3.539   -37.063 1.00 17.06 ? 170 GLN B CD  1 
ATOM   3409 O  OE1 . GLN B 1 170 ? 22.380  2.744   -36.134 1.00 17.04 ? 170 GLN B OE1 1 
ATOM   3410 N  NE2 . GLN B 1 170 ? 23.291  3.582   -37.989 1.00 18.86 ? 170 GLN B NE2 1 
ATOM   3411 N  N   . GLU B 1 171 ? 17.444  3.816   -39.543 1.00 18.05 ? 171 GLU B N   1 
ATOM   3412 C  CA  . GLU B 1 171 ? 16.307  3.168   -40.189 1.00 18.34 ? 171 GLU B CA  1 
ATOM   3413 C  C   . GLU B 1 171 ? 16.839  2.031   -41.050 1.00 18.02 ? 171 GLU B C   1 
ATOM   3414 O  O   . GLU B 1 171 ? 17.923  2.155   -41.618 1.00 17.93 ? 171 GLU B O   1 
ATOM   3415 C  CB  . GLU B 1 171 ? 15.555  4.128   -41.120 1.00 20.26 ? 171 GLU B CB  1 
ATOM   3416 C  CG  . GLU B 1 171 ? 15.260  5.488   -40.514 1.00 22.49 ? 171 GLU B CG  1 
ATOM   3417 C  CD  . GLU B 1 171 ? 14.667  6.518   -41.466 1.00 25.30 ? 171 GLU B CD  1 
ATOM   3418 O  OE1 . GLU B 1 171 ? 13.867  7.337   -41.007 1.00 26.78 ? 171 GLU B OE1 1 
ATOM   3419 O  OE2 . GLU B 1 171 ? 14.988  6.485   -42.679 1.00 29.47 ? 171 GLU B OE2 1 
ATOM   3420 N  N   . ALA B 1 172 ? 16.097  0.918   -41.088 1.00 16.47 ? 172 ALA B N   1 
ATOM   3421 C  CA  . ALA B 1 172 ? 16.341  -0.157  -42.033 1.00 17.16 ? 172 ALA B CA  1 
ATOM   3422 C  C   . ALA B 1 172 ? 15.026  -0.519  -42.728 1.00 17.67 ? 172 ALA B C   1 
ATOM   3423 O  O   . ALA B 1 172 ? 13.950  -0.143  -42.262 1.00 18.69 ? 172 ALA B O   1 
ATOM   3424 C  CB  . ALA B 1 172 ? 16.921  -1.345  -41.299 1.00 16.74 ? 172 ALA B CB  1 
ATOM   3425 N  N   . PHE B 1 173 ? 15.121  -1.241  -43.845 1.00 16.87 ? 173 PHE B N   1 
ATOM   3426 C  CA  . PHE B 1 173 ? 13.959  -1.822  -44.500 1.00 16.72 ? 173 PHE B CA  1 
ATOM   3427 C  C   . PHE B 1 173 ? 13.785  -3.285  -44.092 1.00 17.14 ? 173 PHE B C   1 
ATOM   3428 O  O   . PHE B 1 173 ? 14.750  -4.047  -44.053 1.00 16.93 ? 173 PHE B O   1 
ATOM   3429 C  CB  . PHE B 1 173 ? 14.090  -1.733  -46.020 1.00 15.99 ? 173 PHE B CB  1 
ATOM   3430 C  CG  . PHE B 1 173 ? 13.799  -0.366  -46.587 1.00 16.84 ? 173 PHE B CG  1 
ATOM   3431 C  CD1 . PHE B 1 173 ? 12.787  0.423   -46.067 1.00 17.03 ? 173 PHE B CD1 1 
ATOM   3432 C  CD2 . PHE B 1 173 ? 14.511  0.124   -47.673 1.00 17.36 ? 173 PHE B CD2 1 
ATOM   3433 C  CE1 . PHE B 1 173 ? 12.537  1.689   -46.581 1.00 18.94 ? 173 PHE B CE1 1 
ATOM   3434 C  CE2 . PHE B 1 173 ? 14.246  1.383   -48.198 1.00 17.47 ? 173 PHE B CE2 1 
ATOM   3435 C  CZ  . PHE B 1 173 ? 13.255  2.166   -47.656 1.00 18.13 ? 173 PHE B CZ  1 
ATOM   3436 N  N   . VAL B 1 174 ? 12.535  -3.657  -43.797 1.00 15.56 ? 174 VAL B N   1 
ATOM   3437 C  CA  . VAL B 1 174 ? 12.164  -5.030  -43.493 1.00 15.92 ? 174 VAL B CA  1 
ATOM   3438 C  C   . VAL B 1 174 ? 11.173  -5.476  -44.560 1.00 16.02 ? 174 VAL B C   1 
ATOM   3439 O  O   . VAL B 1 174 ? 10.061  -4.949  -44.648 1.00 15.08 ? 174 VAL B O   1 
ATOM   3440 C  CB  . VAL B 1 174 ? 11.511  -5.153  -42.105 1.00 16.41 ? 174 VAL B CB  1 
ATOM   3441 C  CG1 . VAL B 1 174 ? 10.929  -6.544  -41.861 1.00 17.06 ? 174 VAL B CG1 1 
ATOM   3442 C  CG2 . VAL B 1 174 ? 12.487  -4.793  -41.002 1.00 17.28 ? 174 VAL B CG2 1 
ATOM   3443 N  N   . PRO B 1 175 ? 11.549  -6.474  -45.379 1.00 15.55 ? 175 PRO B N   1 
ATOM   3444 C  CA  . PRO B 1 175 ? 10.615  -7.062  -46.334 1.00 15.71 ? 175 PRO B CA  1 
ATOM   3445 C  C   . PRO B 1 175 ? 9.361   -7.543  -45.599 1.00 15.51 ? 175 PRO B C   1 
ATOM   3446 O  O   . PRO B 1 175 ? 9.465   -8.101  -44.505 1.00 14.62 ? 175 PRO B O   1 
ATOM   3447 C  CB  . PRO B 1 175 ? 11.363  -8.256  -46.949 1.00 15.46 ? 175 PRO B CB  1 
ATOM   3448 C  CG  . PRO B 1 175 ? 12.767  -8.269  -46.340 1.00 16.22 ? 175 PRO B CG  1 
ATOM   3449 C  CD  . PRO B 1 175 ? 12.885  -7.090  -45.398 1.00 16.07 ? 175 PRO B CD  1 
ATOM   3450 N  N   . GLY B 1 176 ? 8.192   -7.260  -46.186 1.00 14.00 ? 176 GLY B N   1 
ATOM   3451 C  CA  . GLY B 1 176 ? 6.910   -7.695  -45.653 1.00 14.60 ? 176 GLY B CA  1 
ATOM   3452 C  C   . GLY B 1 176 ? 6.863   -9.203  -45.397 1.00 15.37 ? 176 GLY B C   1 
ATOM   3453 O  O   . GLY B 1 176 ? 7.366   -9.999  -46.185 1.00 15.33 ? 176 GLY B O   1 
ATOM   3454 N  N   . PHE B 1 177 ? 6.271   -9.575  -44.263 1.00 14.90 ? 177 PHE B N   1 
ATOM   3455 C  CA  . PHE B 1 177 ? 5.907   -10.952 -43.976 1.00 15.30 ? 177 PHE B CA  1 
ATOM   3456 C  C   . PHE B 1 177 ? 4.512   -10.957 -43.352 1.00 14.72 ? 177 PHE B C   1 
ATOM   3457 O  O   . PHE B 1 177 ? 3.926   -9.906  -43.123 1.00 14.88 ? 177 PHE B O   1 
ATOM   3458 C  CB  . PHE B 1 177 ? 6.918   -11.607 -43.038 1.00 14.69 ? 177 PHE B CB  1 
ATOM   3459 C  CG  . PHE B 1 177 ? 7.103   -10.943 -41.696 1.00 14.65 ? 177 PHE B CG  1 
ATOM   3460 C  CD1 . PHE B 1 177 ? 7.879   -9.789  -41.567 1.00 14.97 ? 177 PHE B CD1 1 
ATOM   3461 C  CD2 . PHE B 1 177 ? 6.533   -11.490 -40.557 1.00 14.59 ? 177 PHE B CD2 1 
ATOM   3462 C  CE1 . PHE B 1 177 ? 8.070   -9.197  -40.322 1.00 15.45 ? 177 PHE B CE1 1 
ATOM   3463 C  CE2 . PHE B 1 177 ? 6.707   -10.883 -39.321 1.00 15.76 ? 177 PHE B CE2 1 
ATOM   3464 C  CZ  . PHE B 1 177 ? 7.479   -9.745  -39.206 1.00 15.48 ? 177 PHE B CZ  1 
ATOM   3465 N  N   . ASN B 1 178 ? 3.975   -12.145 -43.098 1.00 14.68 ? 178 ASN B N   1 
ATOM   3466 C  CA  . ASN B 1 178 ? 2.676   -12.226 -42.449 1.00 15.33 ? 178 ASN B CA  1 
ATOM   3467 C  C   . ASN B 1 178 ? 2.805   -11.838 -40.979 1.00 14.61 ? 178 ASN B C   1 
ATOM   3468 O  O   . ASN B 1 178 ? 3.339   -12.610 -40.184 1.00 14.44 ? 178 ASN B O   1 
ATOM   3469 C  CB  . ASN B 1 178 ? 2.104   -13.638 -42.555 1.00 16.95 ? 178 ASN B CB  1 
ATOM   3470 C  CG  . ASN B 1 178 ? 0.660   -13.724 -42.108 1.00 17.63 ? 178 ASN B CG  1 
ATOM   3471 O  OD1 . ASN B 1 178 ? 0.102   -12.768 -41.594 1.00 17.67 ? 178 ASN B OD1 1 
ATOM   3472 N  ND2 . ASN B 1 178 ? 0.055   -14.883 -42.292 1.00 19.88 ? 178 ASN B ND2 1 
ATOM   3473 N  N   . ILE B 1 179 ? 2.224   -10.691 -40.611 1.00 14.24 ? 179 ILE B N   1 
ATOM   3474 C  CA  . ILE B 1 179 ? 2.363   -10.195 -39.249 1.00 13.64 ? 179 ILE B CA  1 
ATOM   3475 C  C   . ILE B 1 179 ? 1.696   -11.147 -38.257 1.00 14.15 ? 179 ILE B C   1 
ATOM   3476 O  O   . ILE B 1 179 ? 2.132   -11.242 -37.118 1.00 14.23 ? 179 ILE B O   1 
ATOM   3477 C  CB  . ILE B 1 179 ? 1.871   -8.738  -39.122 1.00 12.94 ? 179 ILE B CB  1 
ATOM   3478 C  CG1 . ILE B 1 179 ? 2.684   -7.811  -40.037 1.00 13.09 ? 179 ILE B CG1 1 
ATOM   3479 C  CG2 . ILE B 1 179 ? 1.941   -8.270  -37.671 1.00 12.77 ? 179 ILE B CG2 1 
ATOM   3480 C  CD1 . ILE B 1 179 ? 4.205   -7.810  -39.787 1.00 11.87 ? 179 ILE B CD1 1 
ATOM   3481 N  N   . GLU B 1 180 ? 0.671   -11.884 -38.697 1.00 15.75 ? 180 GLU B N   1 
ATOM   3482 C  CA  . GLU B 1 180 ? -0.040  -12.818 -37.831 1.00 16.63 ? 180 GLU B CA  1 
ATOM   3483 C  C   . GLU B 1 180 ? 0.872   -13.884 -37.237 1.00 15.90 ? 180 GLU B C   1 
ATOM   3484 O  O   . GLU B 1 180 ? 0.561   -14.448 -36.183 1.00 15.21 ? 180 GLU B O   1 
ATOM   3485 C  CB  . GLU B 1 180 ? -1.137  -13.547 -38.597 1.00 20.13 ? 180 GLU B CB  1 
ATOM   3486 C  CG  . GLU B 1 180 ? -2.466  -12.843 -38.500 1.00 22.30 ? 180 GLU B CG  1 
ATOM   3487 C  CD  . GLU B 1 180 ? -3.617  -13.745 -38.888 1.00 25.53 ? 180 GLU B CD  1 
ATOM   3488 O  OE1 . GLU B 1 180 ? -4.089  -14.526 -38.028 1.00 25.52 ? 180 GLU B OE1 1 
ATOM   3489 O  OE2 . GLU B 1 180 ? -4.030  -13.654 -40.055 1.00 29.08 ? 180 GLU B OE2 1 
ATOM   3490 N  N   . GLU B 1 181 ? 1.986   -14.154 -37.927 1.00 15.35 ? 181 GLU B N   1 
ATOM   3491 C  CA  . GLU B 1 181 ? 2.988   -15.105 -37.481 1.00 15.11 ? 181 GLU B CA  1 
ATOM   3492 C  C   . GLU B 1 181 ? 3.587   -14.671 -36.150 1.00 13.57 ? 181 GLU B C   1 
ATOM   3493 O  O   . GLU B 1 181 ? 4.181   -15.490 -35.455 1.00 12.21 ? 181 GLU B O   1 
ATOM   3494 C  CB  . GLU B 1 181 ? 4.133   -15.151 -38.484 1.00 17.08 ? 181 GLU B CB  1 
ATOM   3495 C  CG  . GLU B 1 181 ? 3.785   -15.878 -39.767 1.00 19.61 ? 181 GLU B CG  1 
ATOM   3496 C  CD  . GLU B 1 181 ? 4.937   -15.934 -40.771 1.00 22.69 ? 181 GLU B CD  1 
ATOM   3497 O  OE1 . GLU B 1 181 ? 6.114   -15.818 -40.339 1.00 20.93 ? 181 GLU B OE1 1 
ATOM   3498 O  OE2 . GLU B 1 181 ? 4.654   -16.085 -41.993 1.00 23.41 ? 181 GLU B OE2 1 
ATOM   3499 N  N   . LEU B 1 182 ? 3.434   -13.381 -35.816 1.00 12.28 ? 182 LEU B N   1 
ATOM   3500 C  CA  . LEU B 1 182 ? 3.985   -12.850 -34.580 1.00 12.59 ? 182 LEU B CA  1 
ATOM   3501 C  C   . LEU B 1 182 ? 3.025   -13.083 -33.414 1.00 12.55 ? 182 LEU B C   1 
ATOM   3502 O  O   . LEU B 1 182 ? 3.404   -12.898 -32.262 1.00 12.37 ? 182 LEU B O   1 
ATOM   3503 C  CB  . LEU B 1 182 ? 4.297   -11.355 -34.746 1.00 12.59 ? 182 LEU B CB  1 
ATOM   3504 C  CG  . LEU B 1 182 ? 5.351   -10.978 -35.789 1.00 12.21 ? 182 LEU B CG  1 
ATOM   3505 C  CD1 . LEU B 1 182 ? 5.573   -9.476  -35.788 1.00 12.03 ? 182 LEU B CD1 1 
ATOM   3506 C  CD2 . LEU B 1 182 ? 6.654   -11.711 -35.535 1.00 11.35 ? 182 LEU B CD2 1 
ATOM   3507 N  N   . LEU B 1 183 ? 1.776   -13.452 -33.711 1.00 12.54 ? 183 LEU B N   1 
ATOM   3508 C  CA  . LEU B 1 183 ? 0.799   -13.618 -32.647 1.00 13.14 ? 183 LEU B CA  1 
ATOM   3509 C  C   . LEU B 1 183 ? 0.904   -15.029 -32.082 1.00 13.46 ? 183 LEU B C   1 
ATOM   3510 O  O   . LEU B 1 183 ? 1.273   -15.961 -32.805 1.00 12.62 ? 183 LEU B O   1 
ATOM   3511 C  CB  . LEU B 1 183 ? -0.611  -13.377 -33.192 1.00 13.88 ? 183 LEU B CB  1 
ATOM   3512 C  CG  . LEU B 1 183 ? -0.823  -12.024 -33.870 1.00 13.75 ? 183 LEU B CG  1 
ATOM   3513 C  CD1 . LEU B 1 183 ? -2.289  -11.860 -34.226 1.00 15.29 ? 183 LEU B CD1 1 
ATOM   3514 C  CD2 . LEU B 1 183 ? -0.357  -10.868 -32.981 1.00 12.84 ? 183 LEU B CD2 1 
ATOM   3515 N  N   . PRO B 1 184 ? 0.574   -15.238 -30.788 1.00 13.25 ? 184 PRO B N   1 
ATOM   3516 C  CA  . PRO B 1 184 ? 0.706   -16.559 -30.190 1.00 14.21 ? 184 PRO B CA  1 
ATOM   3517 C  C   . PRO B 1 184 ? -0.422  -17.446 -30.681 1.00 17.03 ? 184 PRO B C   1 
ATOM   3518 O  O   . PRO B 1 184 ? -1.314  -16.998 -31.402 1.00 18.04 ? 184 PRO B O   1 
ATOM   3519 C  CB  . PRO B 1 184 ? 0.509   -16.278 -28.701 1.00 13.52 ? 184 PRO B CB  1 
ATOM   3520 C  CG  . PRO B 1 184 ? -0.430  -15.098 -28.676 1.00 12.53 ? 184 PRO B CG  1 
ATOM   3521 C  CD  . PRO B 1 184 ? 0.036   -14.247 -29.841 1.00 13.46 ? 184 PRO B CD  1 
ATOM   3522 N  N   . GLU B 1 185 ? -0.351  -18.713 -30.281 1.00 18.68 ? 185 GLU B N   1 
ATOM   3523 C  CA  . GLU B 1 185 ? -1.440  -19.652 -30.453 1.00 20.25 ? 185 GLU B CA  1 
ATOM   3524 C  C   . GLU B 1 185 ? -2.686  -19.192 -29.689 1.00 19.62 ? 185 GLU B C   1 
ATOM   3525 O  O   . GLU B 1 185 ? -2.604  -18.452 -28.696 1.00 17.75 ? 185 GLU B O   1 
ATOM   3526 C  CB  . GLU B 1 185 ? -0.947  -21.015 -29.965 1.00 23.31 ? 185 GLU B CB  1 
ATOM   3527 C  CG  . GLU B 1 185 ? -1.541  -22.155 -30.753 1.00 29.96 ? 185 GLU B CG  1 
ATOM   3528 C  CD  . GLU B 1 185 ? -0.932  -23.511 -30.442 1.00 32.97 ? 185 GLU B CD  1 
ATOM   3529 O  OE1 . GLU B 1 185 ? -0.204  -23.612 -29.427 1.00 35.14 ? 185 GLU B OE1 1 
ATOM   3530 O  OE2 . GLU B 1 185 ? -1.173  -24.448 -31.229 1.00 34.09 ? 185 GLU B OE2 1 
ATOM   3531 N  N   . ARG B 1 186 ? -3.842  -19.674 -30.164 1.00 18.20 ? 186 ARG B N   1 
ATOM   3532 C  CA  . ARG B 1 186 ? -5.154  -19.414 -29.580 1.00 19.41 ? 186 ARG B CA  1 
ATOM   3533 C  C   . ARG B 1 186 ? -5.364  -17.935 -29.255 1.00 17.57 ? 186 ARG B C   1 
ATOM   3534 O  O   . ARG B 1 186 ? -5.639  -17.599 -28.102 1.00 16.73 ? 186 ARG B O   1 
ATOM   3535 C  CB  . ARG B 1 186 ? -5.380  -20.293 -28.348 1.00 22.02 ? 186 ARG B CB  1 
ATOM   3536 C  CG  . ARG B 1 186 ? -5.616  -21.753 -28.699 1.00 26.21 ? 186 ARG B CG  1 
ATOM   3537 C  CD  . ARG B 1 186 ? -4.934  -22.673 -27.712 1.00 29.91 ? 186 ARG B CD  1 
ATOM   3538 N  NE  . ARG B 1 186 ? -5.698  -22.962 -26.504 1.00 32.89 ? 186 ARG B NE  1 
ATOM   3539 C  CZ  . ARG B 1 186 ? -6.366  -24.089 -26.279 1.00 37.08 ? 186 ARG B CZ  1 
ATOM   3540 N  NH1 . ARG B 1 186 ? -6.995  -24.260 -25.127 1.00 35.09 ? 186 ARG B NH1 1 
ATOM   3541 N  NH2 . ARG B 1 186 ? -6.393  -25.043 -27.197 1.00 40.43 ? 186 ARG B NH2 1 
ATOM   3542 N  N   . THR B 1 187 ? -5.323  -17.075 -30.289 1.00 14.95 ? 187 THR B N   1 
ATOM   3543 C  CA  . THR B 1 187 ? -5.522  -15.636 -30.121 1.00 14.36 ? 187 THR B CA  1 
ATOM   3544 C  C   . THR B 1 187 ? -6.933  -15.373 -29.605 1.00 14.13 ? 187 THR B C   1 
ATOM   3545 O  O   . THR B 1 187 ? -7.227  -14.290 -29.091 1.00 14.48 ? 187 THR B O   1 
ATOM   3546 C  CB  . THR B 1 187 ? -5.230  -14.841 -31.403 1.00 13.92 ? 187 THR B CB  1 
ATOM   3547 O  OG1 . THR B 1 187 ? -5.967  -15.400 -32.489 1.00 13.61 ? 187 THR B OG1 1 
ATOM   3548 C  CG2 . THR B 1 187 ? -3.770  -14.852 -31.789 1.00 13.75 ? 187 THR B CG2 1 
ATOM   3549 N  N   . ALA B 1 188 ? -7.774  -16.410 -29.650 1.00 14.42 ? 188 ALA B N   1 
ATOM   3550 C  CA  . ALA B 1 188 ? -9.129  -16.298 -29.132 1.00 14.47 ? 188 ALA B CA  1 
ATOM   3551 C  C   . ALA B 1 188 ? -9.101  -16.068 -27.622 1.00 12.84 ? 188 ALA B C   1 
ATOM   3552 O  O   . ALA B 1 188 ? -10.052 -15.531 -27.091 1.00 12.24 ? 188 ALA B O   1 
ATOM   3553 C  CB  . ALA B 1 188 ? -9.943  -17.530 -29.483 1.00 15.93 ? 188 ALA B CB  1 
ATOM   3554 N  N   . GLU B 1 189 ? -8.003  -16.447 -26.947 1.00 12.43 ? 189 GLU B N   1 
ATOM   3555 C  CA  . GLU B 1 189 ? -7.878  -16.281 -25.503 1.00 12.51 ? 189 GLU B CA  1 
ATOM   3556 C  C   . GLU B 1 189 ? -7.127  -14.979 -25.181 1.00 12.07 ? 189 GLU B C   1 
ATOM   3557 O  O   . GLU B 1 189 ? -5.948  -14.838 -25.522 1.00 11.33 ? 189 GLU B O   1 
ATOM   3558 C  CB  . GLU B 1 189 ? -7.085  -17.453 -24.916 1.00 13.73 ? 189 GLU B CB  1 
ATOM   3559 C  CG  . GLU B 1 189 ? -7.781  -18.802 -25.074 1.00 15.74 ? 189 GLU B CG  1 
ATOM   3560 C  CD  . GLU B 1 189 ? -7.042  -19.931 -24.372 1.00 18.89 ? 189 GLU B CD  1 
ATOM   3561 O  OE1 . GLU B 1 189 ? -5.796  -20.026 -24.504 1.00 22.26 ? 189 GLU B OE1 1 
ATOM   3562 O  OE2 . GLU B 1 189 ? -7.695  -20.692 -23.670 1.00 21.55 ? 189 GLU B OE2 1 
ATOM   3563 N  N   . TYR B 1 190 ? -7.796  -14.037 -24.502 1.00 11.07 ? 190 TYR B N   1 
ATOM   3564 C  CA  . TYR B 1 190 ? -7.152  -12.761 -24.236 1.00 10.97 ? 190 TYR B CA  1 
ATOM   3565 C  C   . TYR B 1 190 ? -7.736  -12.054 -23.019 1.00 10.95 ? 190 TYR B C   1 
ATOM   3566 O  O   . TYR B 1 190 ? -8.839  -12.349 -22.560 1.00 10.84 ? 190 TYR B O   1 
ATOM   3567 C  CB  . TYR B 1 190 ? -7.200  -11.852 -25.467 1.00 10.91 ? 190 TYR B CB  1 
ATOM   3568 C  CG  . TYR B 1 190 ? -8.576  -11.544 -25.999 1.00 11.25 ? 190 TYR B CG  1 
ATOM   3569 C  CD1 . TYR B 1 190 ? -9.302  -10.462 -25.524 1.00 11.11 ? 190 TYR B CD1 1 
ATOM   3570 C  CD2 . TYR B 1 190 ? -9.123  -12.292 -27.039 1.00 11.17 ? 190 TYR B CD2 1 
ATOM   3571 C  CE1 . TYR B 1 190 ? -10.546 -10.134 -26.063 1.00 12.02 ? 190 TYR B CE1 1 
ATOM   3572 C  CE2 . TYR B 1 190 ? -10.360 -11.978 -27.576 1.00 11.06 ? 190 TYR B CE2 1 
ATOM   3573 C  CZ  . TYR B 1 190 ? -11.080 -10.899 -27.087 1.00 11.23 ? 190 TYR B CZ  1 
ATOM   3574 O  OH  . TYR B 1 190 ? -12.302 -10.584 -27.622 1.00 11.56 ? 190 TYR B OH  1 
ATOM   3575 N  N   . TYR B 1 191 ? -6.938  -11.112 -22.512 1.00 10.39 ? 191 TYR B N   1 
ATOM   3576 C  CA  . TYR B 1 191 ? -7.356  -10.172 -21.502 1.00 9.62  ? 191 TYR B CA  1 
ATOM   3577 C  C   . TYR B 1 191 ? -7.703  -8.867  -22.199 1.00 9.69  ? 191 TYR B C   1 
ATOM   3578 O  O   . TYR B 1 191 ? -7.076  -8.469  -23.188 1.00 9.45  ? 191 TYR B O   1 
ATOM   3579 C  CB  . TYR B 1 191 ? -6.213  -9.877  -20.516 1.00 9.85  ? 191 TYR B CB  1 
ATOM   3580 C  CG  . TYR B 1 191 ? -5.541  -11.047 -19.836 1.00 9.81  ? 191 TYR B CG  1 
ATOM   3581 C  CD1 . TYR B 1 191 ? -5.998  -11.541 -18.616 1.00 10.18 ? 191 TYR B CD1 1 
ATOM   3582 C  CD2 . TYR B 1 191 ? -4.411  -11.639 -20.390 1.00 9.63  ? 191 TYR B CD2 1 
ATOM   3583 C  CE1 . TYR B 1 191 ? -5.356  -12.598 -17.973 1.00 9.75  ? 191 TYR B CE1 1 
ATOM   3584 C  CE2 . TYR B 1 191 ? -3.767  -12.700 -19.771 1.00 10.15 ? 191 TYR B CE2 1 
ATOM   3585 C  CZ  . TYR B 1 191 ? -4.239  -13.178 -18.556 1.00 10.11 ? 191 TYR B CZ  1 
ATOM   3586 O  OH  . TYR B 1 191 ? -3.592  -14.226 -17.962 1.00 10.32 ? 191 TYR B OH  1 
ATOM   3587 N  N   . ARG B 1 192 ? -8.688  -8.173  -21.637 1.00 10.13 ? 192 ARG B N   1 
ATOM   3588 C  CA  . ARG B 1 192 ? -9.171  -6.942  -22.226 1.00 10.16 ? 192 ARG B CA  1 
ATOM   3589 C  C   . ARG B 1 192 ? -9.385  -5.943  -21.099 1.00 10.22 ? 192 ARG B C   1 
ATOM   3590 O  O   . ARG B 1 192 ? -10.056 -6.245  -20.099 1.00 9.88  ? 192 ARG B O   1 
ATOM   3591 C  CB  . ARG B 1 192 ? -10.482 -7.210  -22.976 1.00 10.51 ? 192 ARG B CB  1 
ATOM   3592 C  CG  . ARG B 1 192 ? -11.258 -5.944  -23.325 1.00 11.90 ? 192 ARG B CG  1 
ATOM   3593 C  CD  . ARG B 1 192 ? -10.561 -5.044  -24.351 1.00 11.69 ? 192 ARG B CD  1 
ATOM   3594 N  NE  . ARG B 1 192 ? -10.059 -5.827  -25.474 1.00 11.87 ? 192 ARG B NE  1 
ATOM   3595 C  CZ  . ARG B 1 192 ? -10.838 -6.342  -26.422 1.00 12.67 ? 192 ARG B CZ  1 
ATOM   3596 N  NH1 . ARG B 1 192 ? -10.321 -7.058  -27.408 1.00 12.06 ? 192 ARG B NH1 1 
ATOM   3597 N  NH2 . ARG B 1 192 ? -12.148 -6.161  -26.368 1.00 12.87 ? 192 ARG B NH2 1 
ATOM   3598 N  N   . TYR B 1 193 ? -8.814  -4.746  -21.262 1.00 10.31 ? 193 TYR B N   1 
ATOM   3599 C  CA  . TYR B 1 193 ? -9.135  -3.680  -20.318 1.00 10.43 ? 193 TYR B CA  1 
ATOM   3600 C  C   . TYR B 1 193 ? -8.878  -2.319  -20.978 1.00 11.44 ? 193 TYR B C   1 
ATOM   3601 O  O   . TYR B 1 193 ? -8.136  -2.218  -21.961 1.00 10.41 ? 193 TYR B O   1 
ATOM   3602 C  CB  . TYR B 1 193 ? -8.388  -3.907  -18.993 1.00 10.46 ? 193 TYR B CB  1 
ATOM   3603 C  CG  . TYR B 1 193 ? -6.936  -3.503  -19.032 1.00 10.53 ? 193 TYR B CG  1 
ATOM   3604 C  CD1 . TYR B 1 193 ? -5.981  -4.353  -19.563 1.00 10.41 ? 193 TYR B CD1 1 
ATOM   3605 C  CD2 . TYR B 1 193 ? -6.533  -2.240  -18.620 1.00 10.86 ? 193 TYR B CD2 1 
ATOM   3606 C  CE1 . TYR B 1 193 ? -4.648  -3.985  -19.648 1.00 10.73 ? 193 TYR B CE1 1 
ATOM   3607 C  CE2 . TYR B 1 193 ? -5.206  -1.856  -18.685 1.00 10.69 ? 193 TYR B CE2 1 
ATOM   3608 C  CZ  . TYR B 1 193 ? -4.269  -2.726  -19.219 1.00 10.68 ? 193 TYR B CZ  1 
ATOM   3609 O  OH  . TYR B 1 193 ? -2.972  -2.349  -19.319 1.00 10.51 ? 193 TYR B OH  1 
ATOM   3610 N  N   . ARG B 1 194 ? -9.519  -1.275  -20.424 1.00 13.12 ? 194 ARG B N   1 
ATOM   3611 C  CA  . ARG B 1 194 ? -9.278  0.113   -20.808 1.00 13.99 ? 194 ARG B CA  1 
ATOM   3612 C  C   . ARG B 1 194 ? -8.086  0.635   -20.009 1.00 13.39 ? 194 ARG B C   1 
ATOM   3613 O  O   . ARG B 1 194 ? -8.094  0.599   -18.773 1.00 14.25 ? 194 ARG B O   1 
ATOM   3614 C  CB  . ARG B 1 194 ? -10.535 0.960   -20.554 1.00 15.89 ? 194 ARG B CB  1 
ATOM   3615 C  CG  . ARG B 1 194 ? -11.687 0.707   -21.521 1.00 18.41 ? 194 ARG B CG  1 
ATOM   3616 C  CD  . ARG B 1 194 ? -12.862 1.659   -21.291 1.00 20.59 ? 194 ARG B CD  1 
ATOM   3617 N  N   . GLY B 1 195 ? -7.064  1.125   -20.718 1.00 12.52 ? 195 GLY B N   1 
ATOM   3618 C  CA  . GLY B 1 195 ? -5.917  1.733   -20.060 1.00 11.44 ? 195 GLY B CA  1 
ATOM   3619 C  C   . GLY B 1 195 ? -5.274  2.867   -20.872 1.00 10.98 ? 195 GLY B C   1 
ATOM   3620 O  O   . GLY B 1 195 ? -5.947  3.653   -21.541 1.00 11.19 ? 195 GLY B O   1 
ATOM   3621 N  N   . SER B 1 196 ? -3.948  2.954   -20.795 1.00 9.76  ? 196 SER B N   1 
ATOM   3622 C  CA  . SER B 1 196 ? -3.238  4.111   -21.316 1.00 8.97  ? 196 SER B CA  1 
ATOM   3623 C  C   . SER B 1 196 ? -2.094  3.655   -22.213 1.00 8.50  ? 196 SER B C   1 
ATOM   3624 O  O   . SER B 1 196 ? -1.771  2.469   -22.238 1.00 7.21  ? 196 SER B O   1 
ATOM   3625 C  CB  . SER B 1 196 ? -2.717  4.984   -20.196 1.00 9.19  ? 196 SER B CB  1 
ATOM   3626 O  OG  . SER B 1 196 ? -1.603  4.374   -19.550 1.00 9.97  ? 196 SER B OG  1 
ATOM   3627 N  N   . LEU B 1 197 ? -1.534  4.615   -22.969 1.00 8.58  ? 197 LEU B N   1 
ATOM   3628 C  CA  . LEU B 1 197 ? -0.196  4.455   -23.515 1.00 9.02  ? 197 LEU B CA  1 
ATOM   3629 C  C   . LEU B 1 197 ? 0.707   4.169   -22.327 1.00 9.18  ? 197 LEU B C   1 
ATOM   3630 O  O   . LEU B 1 197 ? 0.544   4.817   -21.289 1.00 9.80  ? 197 LEU B O   1 
ATOM   3631 C  CB  . LEU B 1 197 ? 0.276   5.725   -24.232 1.00 8.91  ? 197 LEU B CB  1 
ATOM   3632 C  CG  . LEU B 1 197 ? -0.270  5.989   -25.640 1.00 9.33  ? 197 LEU B CG  1 
ATOM   3633 C  CD1 . LEU B 1 197 ? -1.563  6.803   -25.590 1.00 8.52  ? 197 LEU B CD1 1 
ATOM   3634 C  CD2 . LEU B 1 197 ? 0.756   6.795   -26.422 1.00 9.80  ? 197 LEU B CD2 1 
ATOM   3635 N  N   . THR B 1 198 ? 1.639   3.219   -22.507 1.00 8.58  ? 198 THR B N   1 
ATOM   3636 C  CA  . THR B 1 198 ? 2.642   2.948   -21.491 1.00 8.37  ? 198 THR B CA  1 
ATOM   3637 C  C   . THR B 1 198 ? 3.858   3.868   -21.613 1.00 8.14  ? 198 THR B C   1 
ATOM   3638 O  O   . THR B 1 198 ? 4.783   3.708   -20.822 1.00 8.88  ? 198 THR B O   1 
ATOM   3639 C  CB  . THR B 1 198 ? 3.083   1.483   -21.473 1.00 7.66  ? 198 THR B CB  1 
ATOM   3640 O  OG1 . THR B 1 198 ? 3.837   1.191   -22.650 1.00 7.93  ? 198 THR B OG1 1 
ATOM   3641 C  CG2 . THR B 1 198 ? 1.914   0.537   -21.349 1.00 7.48  ? 198 THR B CG2 1 
ATOM   3642 N  N   . THR B 1 199 ? 3.874   4.762   -22.604 1.00 7.71  ? 199 THR B N   1 
ATOM   3643 C  CA  . THR B 1 199 ? 4.941   5.733   -22.782 1.00 8.01  ? 199 THR B CA  1 
ATOM   3644 C  C   . THR B 1 199 ? 4.298   7.113   -22.744 1.00 8.38  ? 199 THR B C   1 
ATOM   3645 O  O   . THR B 1 199 ? 3.117   7.220   -23.060 1.00 8.94  ? 199 THR B O   1 
ATOM   3646 C  CB  . THR B 1 199 ? 5.594   5.622   -24.174 1.00 8.09  ? 199 THR B CB  1 
ATOM   3647 O  OG1 . THR B 1 199 ? 4.607   5.645   -25.218 1.00 7.85  ? 199 THR B OG1 1 
ATOM   3648 C  CG2 . THR B 1 199 ? 6.398   4.351   -24.356 1.00 8.60  ? 199 THR B CG2 1 
ATOM   3649 N  N   . PRO B 1 200 ? 5.030   8.219   -22.459 1.00 8.32  ? 200 PRO B N   1 
ATOM   3650 C  CA  . PRO B 1 200 ? 4.473   9.564   -22.664 1.00 8.65  ? 200 PRO B CA  1 
ATOM   3651 C  C   . PRO B 1 200 ? 3.826   9.668   -24.045 1.00 9.28  ? 200 PRO B C   1 
ATOM   3652 O  O   . PRO B 1 200 ? 4.328   9.099   -25.013 1.00 9.27  ? 200 PRO B O   1 
ATOM   3653 C  CB  . PRO B 1 200 ? 5.726   10.457  -22.595 1.00 8.55  ? 200 PRO B CB  1 
ATOM   3654 C  CG  . PRO B 1 200 ? 6.619   9.736   -21.617 1.00 8.01  ? 200 PRO B CG  1 
ATOM   3655 C  CD  . PRO B 1 200 ? 6.420   8.263   -21.970 1.00 8.23  ? 200 PRO B CD  1 
ATOM   3656 N  N   . PRO B 1 201 ? 2.714   10.421  -24.204 1.00 9.43  ? 201 PRO B N   1 
ATOM   3657 C  CA  . PRO B 1 201 ? 2.111   11.184  -23.112 1.00 9.11  ? 201 PRO B CA  1 
ATOM   3658 C  C   . PRO B 1 201 ? 1.148   10.448  -22.185 1.00 8.73  ? 201 PRO B C   1 
ATOM   3659 O  O   . PRO B 1 201 ? 0.466   11.110  -21.433 1.00 8.55  ? 201 PRO B O   1 
ATOM   3660 C  CB  . PRO B 1 201 ? 1.384   12.326  -23.841 1.00 9.54  ? 201 PRO B CB  1 
ATOM   3661 C  CG  . PRO B 1 201 ? 1.880   12.220  -25.267 1.00 9.66  ? 201 PRO B CG  1 
ATOM   3662 C  CD  . PRO B 1 201 ? 2.090   10.736  -25.494 1.00 9.92  ? 201 PRO B CD  1 
ATOM   3663 N  N   . CYS B 1 202 ? 1.089   9.106   -22.251 1.00 8.46  ? 202 CYS B N   1 
ATOM   3664 C  CA  . CYS B 1 202 ? 0.365   8.272   -21.290 1.00 8.55  ? 202 CYS B CA  1 
ATOM   3665 C  C   . CYS B 1 202 ? -1.145  8.522   -21.298 1.00 8.55  ? 202 CYS B C   1 
ATOM   3666 O  O   . CYS B 1 202 ? -1.813  8.241   -20.310 1.00 7.88  ? 202 CYS B O   1 
ATOM   3667 C  CB  . CYS B 1 202 ? 0.830   8.500   -19.850 1.00 8.58  ? 202 CYS B CB  1 
ATOM   3668 S  SG  . CYS B 1 202 ? 2.609   8.264   -19.542 1.00 8.35  ? 202 CYS B SG  1 
ATOM   3669 N  N   . ASN B 1 203 ? -1.696  9.068   -22.394 1.00 9.14  ? 203 ASN B N   1 
ATOM   3670 C  CA  . ASN B 1 203 ? -3.128  9.326   -22.480 1.00 9.11  ? 203 ASN B CA  1 
ATOM   3671 C  C   . ASN B 1 203 ? -3.944  8.077   -22.179 1.00 9.31  ? 203 ASN B C   1 
ATOM   3672 O  O   . ASN B 1 203 ? -3.609  6.992   -22.648 1.00 9.20  ? 203 ASN B O   1 
ATOM   3673 C  CB  . ASN B 1 203 ? -3.517  9.787   -23.880 1.00 9.35  ? 203 ASN B CB  1 
ATOM   3674 C  CG  . ASN B 1 203 ? -2.632  10.937  -24.294 1.00 10.04 ? 203 ASN B CG  1 
ATOM   3675 O  OD1 . ASN B 1 203 ? -1.476  10.727  -24.672 1.00 10.02 ? 203 ASN B OD1 1 
ATOM   3676 N  ND2 . ASN B 1 203 ? -3.156  12.138  -24.152 1.00 9.39  ? 203 ASN B ND2 1 
ATOM   3677 N  N   . PRO B 1 204 ? -5.040  8.190   -21.389 1.00 10.06 ? 204 PRO B N   1 
ATOM   3678 C  CA  . PRO B 1 204 ? -5.845  7.021   -21.020 1.00 10.17 ? 204 PRO B CA  1 
ATOM   3679 C  C   . PRO B 1 204 ? -6.859  6.618   -22.086 1.00 10.65 ? 204 PRO B C   1 
ATOM   3680 O  O   . PRO B 1 204 ? -8.057  6.614   -21.817 1.00 11.51 ? 204 PRO B O   1 
ATOM   3681 C  CB  . PRO B 1 204 ? -6.584  7.539   -19.767 1.00 10.60 ? 204 PRO B CB  1 
ATOM   3682 C  CG  . PRO B 1 204 ? -6.801  9.038   -20.054 1.00 10.09 ? 204 PRO B CG  1 
ATOM   3683 C  CD  . PRO B 1 204 ? -5.472  9.422   -20.687 1.00 10.59 ? 204 PRO B CD  1 
ATOM   3684 N  N   . THR B 1 205 ? -6.363  6.291   -23.293 1.00 9.86  ? 205 THR B N   1 
ATOM   3685 C  CA  . THR B 1 205 ? -7.162  6.269   -24.500 1.00 9.02  ? 205 THR B CA  1 
ATOM   3686 C  C   . THR B 1 205 ? -6.941  4.939   -25.225 1.00 9.45  ? 205 THR B C   1 
ATOM   3687 O  O   . THR B 1 205 ? -7.220  4.818   -26.421 1.00 8.72  ? 205 THR B O   1 
ATOM   3688 C  CB  . THR B 1 205 ? -6.756  7.462   -25.374 1.00 8.86  ? 205 THR B CB  1 
ATOM   3689 O  OG1 . THR B 1 205 ? -5.339  7.320   -25.609 1.00 8.62  ? 205 THR B OG1 1 
ATOM   3690 C  CG2 . THR B 1 205 ? -7.046  8.803   -24.725 1.00 8.58  ? 205 THR B CG2 1 
ATOM   3691 N  N   . VAL B 1 206 ? -6.430  3.926   -24.505 1.00 9.81  ? 206 VAL B N   1 
ATOM   3692 C  CA  . VAL B 1 206 ? -6.083  2.679   -25.188 1.00 10.78 ? 206 VAL B CA  1 
ATOM   3693 C  C   . VAL B 1 206 ? -6.993  1.542   -24.751 1.00 11.28 ? 206 VAL B C   1 
ATOM   3694 O  O   . VAL B 1 206 ? -7.207  1.340   -23.564 1.00 11.77 ? 206 VAL B O   1 
ATOM   3695 C  CB  . VAL B 1 206 ? -4.617  2.261   -25.007 1.00 10.67 ? 206 VAL B CB  1 
ATOM   3696 C  CG1 . VAL B 1 206 ? -4.370  0.877   -25.639 1.00 9.76  ? 206 VAL B CG1 1 
ATOM   3697 C  CG2 . VAL B 1 206 ? -3.701  3.313   -25.609 1.00 10.84 ? 206 VAL B CG2 1 
ATOM   3698 N  N   . LEU B 1 207 ? -7.505  0.810   -25.741 1.00 11.48 ? 207 LEU B N   1 
ATOM   3699 C  CA  . LEU B 1 207 ? -8.200  -0.438  -25.501 1.00 12.33 ? 207 LEU B CA  1 
ATOM   3700 C  C   . LEU B 1 207 ? -7.151  -1.538  -25.582 1.00 11.82 ? 207 LEU B C   1 
ATOM   3701 O  O   . LEU B 1 207 ? -6.598  -1.759  -26.663 1.00 11.54 ? 207 LEU B O   1 
ATOM   3702 C  CB  . LEU B 1 207 ? -9.187  -0.613  -26.653 1.00 15.79 ? 207 LEU B CB  1 
ATOM   3703 C  CG  . LEU B 1 207 ? -10.642 -0.863  -26.279 1.00 19.54 ? 207 LEU B CG  1 
ATOM   3704 C  CD1 . LEU B 1 207 ? -11.072 0.065   -25.147 1.00 21.82 ? 207 LEU B CD1 1 
ATOM   3705 C  CD2 . LEU B 1 207 ? -11.521 -0.659  -27.513 1.00 19.64 ? 207 LEU B CD2 1 
ATOM   3706 N  N   . TRP B 1 208 ? -6.844  -2.167  -24.439 1.00 10.42 ? 208 TRP B N   1 
ATOM   3707 C  CA  . TRP B 1 208 ? -5.789  -3.174  -24.393 1.00 9.90  ? 208 TRP B CA  1 
ATOM   3708 C  C   . TRP B 1 208 ? -6.361  -4.565  -24.661 1.00 9.81  ? 208 TRP B C   1 
ATOM   3709 O  O   . TRP B 1 208 ? -7.354  -4.954  -24.067 1.00 8.92  ? 208 TRP B O   1 
ATOM   3710 C  CB  . TRP B 1 208 ? -5.010  -3.158  -23.055 1.00 8.97  ? 208 TRP B CB  1 
ATOM   3711 C  CG  . TRP B 1 208 ? -3.994  -2.054  -22.949 1.00 8.60  ? 208 TRP B CG  1 
ATOM   3712 C  CD1 . TRP B 1 208 ? -4.204  -0.810  -22.422 1.00 8.18  ? 208 TRP B CD1 1 
ATOM   3713 C  CD2 . TRP B 1 208 ? -2.643  -2.045  -23.465 1.00 8.30  ? 208 TRP B CD2 1 
ATOM   3714 N  NE1 . TRP B 1 208 ? -3.078  -0.041  -22.556 1.00 8.40  ? 208 TRP B NE1 1 
ATOM   3715 C  CE2 . TRP B 1 208 ? -2.106  -0.767  -23.197 1.00 8.23  ? 208 TRP B CE2 1 
ATOM   3716 C  CE3 . TRP B 1 208 ? -1.838  -2.981  -24.137 1.00 8.72  ? 208 TRP B CE3 1 
ATOM   3717 C  CZ2 . TRP B 1 208 ? -0.802  -0.419  -23.540 1.00 8.49  ? 208 TRP B CZ2 1 
ATOM   3718 C  CZ3 . TRP B 1 208 ? -0.550  -2.632  -24.486 1.00 8.31  ? 208 TRP B CZ3 1 
ATOM   3719 C  CH2 . TRP B 1 208 ? -0.045  -1.358  -24.212 1.00 8.25  ? 208 TRP B CH2 1 
ATOM   3720 N  N   . THR B 1 209 ? -5.684  -5.311  -25.542 1.00 10.36 ? 209 THR B N   1 
ATOM   3721 C  CA  . THR B 1 209 ? -5.868  -6.750  -25.644 1.00 10.07 ? 209 THR B CA  1 
ATOM   3722 C  C   . THR B 1 209 ? -4.511  -7.437  -25.476 1.00 11.08 ? 209 THR B C   1 
ATOM   3723 O  O   . THR B 1 209 ? -3.577  -7.220  -26.262 1.00 11.40 ? 209 THR B O   1 
ATOM   3724 C  CB  . THR B 1 209 ? -6.383  -7.123  -27.037 1.00 9.96  ? 209 THR B CB  1 
ATOM   3725 O  OG1 . THR B 1 209 ? -7.598  -6.410  -27.262 1.00 9.27  ? 209 THR B OG1 1 
ATOM   3726 C  CG2 . THR B 1 209 ? -6.617  -8.618  -27.168 1.00 10.02 ? 209 THR B CG2 1 
ATOM   3727 N  N   . VAL B 1 210 ? -4.409  -8.268  -24.439 1.00 10.87 ? 210 VAL B N   1 
ATOM   3728 C  CA  . VAL B 1 210 ? -3.199  -9.021  -24.181 1.00 10.54 ? 210 VAL B CA  1 
ATOM   3729 C  C   . VAL B 1 210 ? -3.542  -10.486 -24.360 1.00 10.62 ? 210 VAL B C   1 
ATOM   3730 O  O   . VAL B 1 210 ? -4.379  -10.989 -23.615 1.00 10.12 ? 210 VAL B O   1 
ATOM   3731 C  CB  . VAL B 1 210 ? -2.723  -8.807  -22.736 1.00 10.49 ? 210 VAL B CB  1 
ATOM   3732 C  CG1 . VAL B 1 210 ? -1.369  -9.463  -22.535 1.00 10.75 ? 210 VAL B CG1 1 
ATOM   3733 C  CG2 . VAL B 1 210 ? -2.677  -7.330  -22.380 1.00 10.58 ? 210 VAL B CG2 1 
ATOM   3734 N  N   . PHE B 1 211 ? -2.850  -11.146 -25.300 1.00 10.46 ? 211 PHE B N   1 
ATOM   3735 C  CA  . PHE B 1 211 ? -3.113  -12.550 -25.571 1.00 10.86 ? 211 PHE B CA  1 
ATOM   3736 C  C   . PHE B 1 211 ? -2.703  -13.371 -24.354 1.00 11.16 ? 211 PHE B C   1 
ATOM   3737 O  O   . PHE B 1 211 ? -1.707  -13.077 -23.706 1.00 10.30 ? 211 PHE B O   1 
ATOM   3738 C  CB  . PHE B 1 211 ? -2.486  -12.987 -26.897 1.00 10.67 ? 211 PHE B CB  1 
ATOM   3739 C  CG  . PHE B 1 211 ? -3.072  -12.249 -28.078 1.00 11.05 ? 211 PHE B CG  1 
ATOM   3740 C  CD1 . PHE B 1 211 ? -4.405  -12.432 -28.441 1.00 11.11 ? 211 PHE B CD1 1 
ATOM   3741 C  CD2 . PHE B 1 211 ? -2.322  -11.311 -28.782 1.00 10.52 ? 211 PHE B CD2 1 
ATOM   3742 C  CE1 . PHE B 1 211 ? -4.955  -11.723 -29.506 1.00 11.02 ? 211 PHE B CE1 1 
ATOM   3743 C  CE2 . PHE B 1 211 ? -2.875  -10.608 -29.847 1.00 10.46 ? 211 PHE B CE2 1 
ATOM   3744 C  CZ  . PHE B 1 211 ? -4.188  -10.811 -30.212 1.00 10.27 ? 211 PHE B CZ  1 
ATOM   3745 N  N   . ARG B 1 212 ? -3.498  -14.395 -24.045 1.00 11.99 ? 212 ARG B N   1 
ATOM   3746 C  CA  . ARG B 1 212 ? -3.269  -15.184 -22.843 1.00 13.20 ? 212 ARG B CA  1 
ATOM   3747 C  C   . ARG B 1 212 ? -1.942  -15.943 -22.965 1.00 12.82 ? 212 ARG B C   1 
ATOM   3748 O  O   . ARG B 1 212 ? -1.202  -16.075 -21.987 1.00 12.02 ? 212 ARG B O   1 
ATOM   3749 C  CB  . ARG B 1 212 ? -4.421  -16.185 -22.646 1.00 14.64 ? 212 ARG B CB  1 
ATOM   3750 C  CG  . ARG B 1 212 ? -4.321  -16.973 -21.344 1.00 15.76 ? 212 ARG B CG  1 
ATOM   3751 C  CD  . ARG B 1 212 ? -4.962  -18.342 -21.335 1.00 17.55 ? 212 ARG B CD  1 
ATOM   3752 N  NE  . ARG B 1 212 ? -5.218  -18.751 -19.962 1.00 18.79 ? 212 ARG B NE  1 
ATOM   3753 C  CZ  . ARG B 1 212 ? -6.175  -19.606 -19.585 1.00 18.95 ? 212 ARG B CZ  1 
ATOM   3754 N  NH1 . ARG B 1 212 ? -6.949  -20.193 -20.491 1.00 18.46 ? 212 ARG B NH1 1 
ATOM   3755 N  NH2 . ARG B 1 212 ? -6.327  -19.877 -18.298 1.00 17.01 ? 212 ARG B NH2 1 
ATOM   3756 N  N   . ASN B 1 213 ? -1.670  -16.461 -24.171 1.00 12.58 ? 213 ASN B N   1 
ATOM   3757 C  CA  . ASN B 1 213 ? -0.537  -17.344 -24.395 1.00 12.72 ? 213 ASN B CA  1 
ATOM   3758 C  C   . ASN B 1 213 ? 0.657   -16.559 -24.919 1.00 12.75 ? 213 ASN B C   1 
ATOM   3759 O  O   . ASN B 1 213 ? 0.507   -15.709 -25.799 1.00 13.65 ? 213 ASN B O   1 
ATOM   3760 C  CB  . ASN B 1 213 ? -0.909  -18.491 -25.337 1.00 12.88 ? 213 ASN B CB  1 
ATOM   3761 C  CG  . ASN B 1 213 ? -2.094  -19.252 -24.784 1.00 13.38 ? 213 ASN B CG  1 
ATOM   3762 O  OD1 . ASN B 1 213 ? -2.056  -19.669 -23.632 1.00 14.11 ? 213 ASN B OD1 1 
ATOM   3763 N  ND2 . ASN B 1 213 ? -3.160  -19.371 -25.553 1.00 12.73 ? 213 ASN B ND2 1 
ATOM   3764 N  N   . PRO B 1 214 ? 1.863   -16.817 -24.360 1.00 12.89 ? 214 PRO B N   1 
ATOM   3765 C  CA  . PRO B 1 214 ? 3.096   -16.199 -24.836 1.00 11.86 ? 214 PRO B CA  1 
ATOM   3766 C  C   . PRO B 1 214 ? 3.611   -16.916 -26.081 1.00 12.45 ? 214 PRO B C   1 
ATOM   3767 O  O   . PRO B 1 214 ? 3.220   -18.057 -26.367 1.00 11.64 ? 214 PRO B O   1 
ATOM   3768 C  CB  . PRO B 1 214 ? 4.084   -16.534 -23.713 1.00 12.65 ? 214 PRO B CB  1 
ATOM   3769 C  CG  . PRO B 1 214 ? 3.595   -17.874 -23.186 1.00 12.50 ? 214 PRO B CG  1 
ATOM   3770 C  CD  . PRO B 1 214 ? 2.087   -17.765 -23.247 1.00 12.52 ? 214 PRO B CD  1 
ATOM   3771 N  N   . VAL B 1 215 ? 4.476   -16.214 -26.825 1.00 11.78 ? 215 VAL B N   1 
ATOM   3772 C  CA  . VAL B 1 215 ? 5.255   -16.850 -27.870 1.00 12.65 ? 215 VAL B CA  1 
ATOM   3773 C  C   . VAL B 1 215 ? 6.600   -17.147 -27.224 1.00 13.30 ? 215 VAL B C   1 
ATOM   3774 O  O   . VAL B 1 215 ? 6.927   -16.583 -26.175 1.00 12.89 ? 215 VAL B O   1 
ATOM   3775 C  CB  . VAL B 1 215 ? 5.406   -15.963 -29.125 1.00 12.26 ? 215 VAL B CB  1 
ATOM   3776 C  CG1 . VAL B 1 215 ? 4.059   -15.697 -29.796 1.00 12.30 ? 215 VAL B CG1 1 
ATOM   3777 C  CG2 . VAL B 1 215 ? 6.075   -14.630 -28.786 1.00 12.19 ? 215 VAL B CG2 1 
ATOM   3778 N  N   . GLN B 1 216 ? 7.368   -18.015 -27.875 1.00 13.18 ? 216 GLN B N   1 
ATOM   3779 C  CA  . GLN B 1 216 ? 8.732   -18.283 -27.456 1.00 14.44 ? 216 GLN B CA  1 
ATOM   3780 C  C   . GLN B 1 216 ? 9.686   -17.744 -28.511 1.00 13.59 ? 216 GLN B C   1 
ATOM   3781 O  O   . GLN B 1 216 ? 9.385   -17.767 -29.709 1.00 12.20 ? 216 GLN B O   1 
ATOM   3782 C  CB  . GLN B 1 216 ? 8.989   -19.790 -27.392 1.00 15.90 ? 216 GLN B CB  1 
ATOM   3783 C  CG  . GLN B 1 216 ? 8.116   -20.490 -26.372 1.00 19.44 ? 216 GLN B CG  1 
ATOM   3784 C  CD  . GLN B 1 216 ? 8.372   -21.976 -26.311 1.00 23.41 ? 216 GLN B CD  1 
ATOM   3785 O  OE1 . GLN B 1 216 ? 9.285   -22.520 -26.950 1.00 23.58 ? 216 GLN B OE1 1 
ATOM   3786 N  NE2 . GLN B 1 216 ? 7.554   -22.647 -25.512 1.00 26.14 ? 216 GLN B NE2 1 
ATOM   3787 N  N   . ILE B 1 217 ? 10.818  -17.227 -28.020 1.00 13.91 ? 217 ILE B N   1 
ATOM   3788 C  CA  . ILE B 1 217 ? 11.985  -16.954 -28.836 1.00 14.35 ? 217 ILE B CA  1 
ATOM   3789 C  C   . ILE B 1 217 ? 13.166  -17.613 -28.144 1.00 14.92 ? 217 ILE B C   1 
ATOM   3790 O  O   . ILE B 1 217 ? 13.099  -17.908 -26.957 1.00 16.96 ? 217 ILE B O   1 
ATOM   3791 C  CB  . ILE B 1 217 ? 12.164  -15.430 -29.010 1.00 13.55 ? 217 ILE B CB  1 
ATOM   3792 C  CG1 . ILE B 1 217 ? 12.568  -14.726 -27.702 1.00 12.88 ? 217 ILE B CG1 1 
ATOM   3793 C  CG2 . ILE B 1 217 ? 10.904  -14.827 -29.615 1.00 13.43 ? 217 ILE B CG2 1 
ATOM   3794 C  CD1 . ILE B 1 217 ? 12.876  -13.226 -27.883 1.00 11.52 ? 217 ILE B CD1 1 
ATOM   3795 N  N   . SER B 1 218 ? 14.259  -17.819 -28.867 1.00 15.41 ? 218 SER B N   1 
ATOM   3796 C  CA  . SER B 1 218 ? 15.400  -18.487 -28.265 1.00 15.93 ? 218 SER B CA  1 
ATOM   3797 C  C   . SER B 1 218 ? 16.192  -17.551 -27.349 1.00 16.89 ? 218 SER B C   1 
ATOM   3798 O  O   . SER B 1 218 ? 16.083  -16.318 -27.423 1.00 14.02 ? 218 SER B O   1 
ATOM   3799 C  CB  . SER B 1 218 ? 16.289  -19.069 -29.328 1.00 16.36 ? 218 SER B CB  1 
ATOM   3800 O  OG  . SER B 1 218 ? 17.026  -18.024 -29.935 1.00 15.75 ? 218 SER B OG  1 
ATOM   3801 N  N   . GLN B 1 219 ? 17.043  -18.159 -26.496 1.00 17.43 ? 219 GLN B N   1 
ATOM   3802 C  CA  . GLN B 1 219 ? 17.874  -17.346 -25.624 1.00 18.65 ? 219 GLN B CA  1 
ATOM   3803 C  C   . GLN B 1 219 ? 18.721  -16.389 -26.460 1.00 18.43 ? 219 GLN B C   1 
ATOM   3804 O  O   . GLN B 1 219 ? 18.820  -15.198 -26.116 1.00 18.17 ? 219 GLN B O   1 
ATOM   3805 C  CB  . GLN B 1 219 ? 18.704  -18.175 -24.639 1.00 20.86 ? 219 GLN B CB  1 
ATOM   3806 C  CG  . GLN B 1 219 ? 19.826  -17.365 -23.988 1.00 26.35 ? 219 GLN B CG  1 
ATOM   3807 C  CD  . GLN B 1 219 ? 19.478  -16.414 -22.857 1.00 31.55 ? 219 GLN B CD  1 
ATOM   3808 O  OE1 . GLN B 1 219 ? 19.802  -16.676 -21.697 1.00 36.23 ? 219 GLN B OE1 1 
ATOM   3809 N  NE2 . GLN B 1 219 ? 18.857  -15.280 -23.165 1.00 28.51 ? 219 GLN B NE2 1 
ATOM   3810 N  N   . GLU B 1 220 ? 19.321  -16.904 -27.549 1.00 17.08 ? 220 GLU B N   1 
ATOM   3811 C  CA  . GLU B 1 220 ? 20.137  -16.069 -28.428 1.00 19.55 ? 220 GLU B CA  1 
ATOM   3812 C  C   . GLU B 1 220 ? 19.297  -14.905 -28.986 1.00 17.41 ? 220 GLU B C   1 
ATOM   3813 O  O   . GLU B 1 220 ? 19.729  -13.751 -28.992 1.00 18.46 ? 220 GLU B O   1 
ATOM   3814 C  CB  . GLU B 1 220 ? 20.750  -16.893 -29.576 1.00 23.54 ? 220 GLU B CB  1 
ATOM   3815 C  CG  . GLU B 1 220 ? 21.510  -18.164 -29.152 1.00 26.58 ? 220 GLU B CG  1 
ATOM   3816 C  CD  . GLU B 1 220 ? 20.777  -19.260 -28.370 1.00 30.55 ? 220 GLU B CD  1 
ATOM   3817 O  OE1 . GLU B 1 220 ? 19.592  -19.559 -28.675 1.00 27.28 ? 220 GLU B OE1 1 
ATOM   3818 O  OE2 . GLU B 1 220 ? 21.394  -19.808 -27.417 1.00 33.38 ? 220 GLU B OE2 1 
ATOM   3819 N  N   . GLN B 1 221 ? 18.095  -15.204 -29.481 1.00 14.52 ? 221 GLN B N   1 
ATOM   3820 C  CA  . GLN B 1 221 ? 17.191  -14.143 -29.917 1.00 14.48 ? 221 GLN B CA  1 
ATOM   3821 C  C   . GLN B 1 221 ? 16.953  -13.089 -28.823 1.00 13.04 ? 221 GLN B C   1 
ATOM   3822 O  O   . GLN B 1 221 ? 16.970  -11.890 -29.099 1.00 13.36 ? 221 GLN B O   1 
ATOM   3823 C  CB  . GLN B 1 221 ? 15.864  -14.696 -30.433 1.00 13.04 ? 221 GLN B CB  1 
ATOM   3824 C  CG  . GLN B 1 221 ? 15.984  -15.281 -31.844 1.00 13.05 ? 221 GLN B CG  1 
ATOM   3825 C  CD  . GLN B 1 221 ? 14.683  -15.866 -32.313 1.00 12.26 ? 221 GLN B CD  1 
ATOM   3826 O  OE1 . GLN B 1 221 ? 14.077  -16.668 -31.626 1.00 12.73 ? 221 GLN B OE1 1 
ATOM   3827 N  NE2 . GLN B 1 221 ? 14.245  -15.485 -33.504 1.00 12.94 ? 221 GLN B NE2 1 
ATOM   3828 N  N   . LEU B 1 222 ? 16.660  -13.533 -27.600 1.00 12.68 ? 222 LEU B N   1 
ATOM   3829 C  CA  . LEU B 1 222 ? 16.334  -12.587 -26.553 1.00 13.35 ? 222 LEU B CA  1 
ATOM   3830 C  C   . LEU B 1 222 ? 17.565  -11.743 -26.232 1.00 13.41 ? 222 LEU B C   1 
ATOM   3831 O  O   . LEU B 1 222 ? 17.472  -10.536 -26.075 1.00 12.64 ? 222 LEU B O   1 
ATOM   3832 C  CB  . LEU B 1 222 ? 15.795  -13.319 -25.318 1.00 13.99 ? 222 LEU B CB  1 
ATOM   3833 C  CG  . LEU B 1 222 ? 15.557  -12.433 -24.090 1.00 15.62 ? 222 LEU B CG  1 
ATOM   3834 C  CD1 . LEU B 1 222 ? 14.516  -11.351 -24.383 1.00 14.86 ? 222 LEU B CD1 1 
ATOM   3835 C  CD2 . LEU B 1 222 ? 15.124  -13.274 -22.885 1.00 16.26 ? 222 LEU B CD2 1 
ATOM   3836 N  N   . LEU B 1 223 ? 18.717  -12.404 -26.146 1.00 14.18 ? 223 LEU B N   1 
ATOM   3837 C  CA  . LEU B 1 223 ? 20.003  -11.772 -25.902 1.00 15.18 ? 223 LEU B CA  1 
ATOM   3838 C  C   . LEU B 1 223 ? 20.224  -10.684 -26.944 1.00 15.17 ? 223 LEU B C   1 
ATOM   3839 O  O   . LEU B 1 223 ? 20.728  -9.611  -26.608 1.00 14.80 ? 223 LEU B O   1 
ATOM   3840 C  CB  . LEU B 1 223 ? 21.059  -12.857 -26.104 1.00 16.27 ? 223 LEU B CB  1 
ATOM   3841 C  CG  . LEU B 1 223 ? 22.101  -13.065 -25.014 1.00 19.31 ? 223 LEU B CG  1 
ATOM   3842 C  CD1 . LEU B 1 223 ? 21.594  -12.630 -23.644 1.00 17.90 ? 223 LEU B CD1 1 
ATOM   3843 C  CD2 . LEU B 1 223 ? 22.509  -14.539 -25.004 1.00 18.84 ? 223 LEU B CD2 1 
ATOM   3844 N  N   . ALA B 1 224 ? 19.884  -10.993 -28.211 1.00 14.64 ? 224 ALA B N   1 
ATOM   3845 C  CA  . ALA B 1 224 ? 20.081  -10.025 -29.285 1.00 14.24 ? 224 ALA B CA  1 
ATOM   3846 C  C   . ALA B 1 224 ? 19.173  -8.816  -29.089 1.00 14.18 ? 224 ALA B C   1 
ATOM   3847 O  O   . ALA B 1 224 ? 19.603  -7.680  -29.267 1.00 15.16 ? 224 ALA B O   1 
ATOM   3848 C  CB  . ALA B 1 224 ? 19.835  -10.655 -30.639 1.00 14.13 ? 224 ALA B CB  1 
ATOM   3849 N  N   . LEU B 1 225 ? 17.898  -9.051  -28.763 1.00 13.62 ? 225 LEU B N   1 
ATOM   3850 C  CA  . LEU B 1 225 ? 17.006  -7.928  -28.551 1.00 13.47 ? 225 LEU B CA  1 
ATOM   3851 C  C   . LEU B 1 225 ? 17.540  -7.046  -27.421 1.00 13.57 ? 225 LEU B C   1 
ATOM   3852 O  O   . LEU B 1 225 ? 17.595  -5.828  -27.560 1.00 13.22 ? 225 LEU B O   1 
ATOM   3853 C  CB  . LEU B 1 225 ? 15.592  -8.459  -28.290 1.00 14.56 ? 225 LEU B CB  1 
ATOM   3854 C  CG  . LEU B 1 225 ? 14.500  -7.433  -27.998 1.00 14.85 ? 225 LEU B CG  1 
ATOM   3855 C  CD1 . LEU B 1 225 ? 14.279  -6.504  -29.188 1.00 15.15 ? 225 LEU B CD1 1 
ATOM   3856 C  CD2 . LEU B 1 225 ? 13.191  -8.150  -27.672 1.00 15.61 ? 225 LEU B CD2 1 
ATOM   3857 N  N   . GLU B 1 226 ? 17.969  -7.681  -26.322 1.00 13.62 ? 226 GLU B N   1 
ATOM   3858 C  CA  . GLU B 1 226 ? 18.425  -7.003  -25.121 1.00 13.28 ? 226 GLU B CA  1 
ATOM   3859 C  C   . GLU B 1 226 ? 19.722  -6.227  -25.342 1.00 14.44 ? 226 GLU B C   1 
ATOM   3860 O  O   . GLU B 1 226 ? 19.983  -5.271  -24.617 1.00 15.32 ? 226 GLU B O   1 
ATOM   3861 C  CB  . GLU B 1 226 ? 18.705  -8.015  -24.007 1.00 12.32 ? 226 GLU B CB  1 
ATOM   3862 C  CG  . GLU B 1 226 ? 17.432  -8.645  -23.453 1.00 11.51 ? 226 GLU B CG  1 
ATOM   3863 C  CD  . GLU B 1 226 ? 17.677  -9.838  -22.550 1.00 11.45 ? 226 GLU B CD  1 
ATOM   3864 O  OE1 . GLU B 1 226 ? 18.810  -10.384 -22.531 1.00 10.95 ? 226 GLU B OE1 1 
ATOM   3865 O  OE2 . GLU B 1 226 ? 16.747  -10.209 -21.865 1.00 11.80 ? 226 GLU B OE2 1 
ATOM   3866 N  N   . THR B 1 227 ? 20.582  -6.672  -26.263 1.00 14.41 ? 227 THR B N   1 
ATOM   3867 C  CA  . THR B 1 227 ? 21.908  -6.075  -26.285 1.00 14.67 ? 227 THR B CA  1 
ATOM   3868 C  C   . THR B 1 227 ? 22.218  -5.372  -27.606 1.00 16.54 ? 227 THR B C   1 
ATOM   3869 O  O   . THR B 1 227 ? 23.249  -4.726  -27.716 1.00 17.68 ? 227 THR B O   1 
ATOM   3870 C  CB  . THR B 1 227 ? 22.980  -7.116  -25.952 1.00 14.44 ? 227 THR B CB  1 
ATOM   3871 O  OG1 . THR B 1 227 ? 22.906  -8.100  -26.987 1.00 13.51 ? 227 THR B OG1 1 
ATOM   3872 C  CG2 . THR B 1 227 ? 22.731  -7.778  -24.613 1.00 14.61 ? 227 THR B CG2 1 
ATOM   3873 N  N   . ALA B 1 228 ? 21.344  -5.478  -28.612 1.00 17.90 ? 228 ALA B N   1 
ATOM   3874 C  CA  . ALA B 1 228 ? 21.707  -4.946  -29.923 1.00 16.14 ? 228 ALA B CA  1 
ATOM   3875 C  C   . ALA B 1 228 ? 21.718  -3.419  -29.953 1.00 15.78 ? 228 ALA B C   1 
ATOM   3876 O  O   . ALA B 1 228 ? 22.489  -2.854  -30.730 1.00 15.36 ? 228 ALA B O   1 
ATOM   3877 C  CB  . ALA B 1 228 ? 20.813  -5.488  -31.004 1.00 16.25 ? 228 ALA B CB  1 
ATOM   3878 N  N   . LEU B 1 229 ? 20.849  -2.742  -29.179 1.00 14.46 ? 229 LEU B N   1 
ATOM   3879 C  CA  . LEU B 1 229 ? 20.597  -1.338  -29.507 1.00 14.16 ? 229 LEU B CA  1 
ATOM   3880 C  C   . LEU B 1 229 ? 21.079  -0.379  -28.419 1.00 13.68 ? 229 LEU B C   1 
ATOM   3881 O  O   . LEU B 1 229 ? 21.149  -0.736  -27.253 1.00 11.70 ? 229 LEU B O   1 
ATOM   3882 C  CB  . LEU B 1 229 ? 19.100  -1.098  -29.734 1.00 13.79 ? 229 LEU B CB  1 
ATOM   3883 C  CG  . LEU B 1 229 ? 18.340  -2.090  -30.614 1.00 14.04 ? 229 LEU B CG  1 
ATOM   3884 C  CD1 . LEU B 1 229 ? 16.916  -1.585  -30.750 1.00 14.19 ? 229 LEU B CD1 1 
ATOM   3885 C  CD2 . LEU B 1 229 ? 18.989  -2.236  -31.984 1.00 13.47 ? 229 LEU B CD2 1 
ATOM   3886 N  N   . TYR B 1 230 ? 21.385  0.852   -28.847 1.00 15.69 ? 230 TYR B N   1 
ATOM   3887 C  CA  . TYR B 1 230 ? 21.674  1.993   -27.990 1.00 16.77 ? 230 TYR B CA  1 
ATOM   3888 C  C   . TYR B 1 230 ? 20.493  2.952   -28.074 1.00 17.35 ? 230 TYR B C   1 
ATOM   3889 O  O   . TYR B 1 230 ? 19.794  2.966   -29.084 1.00 16.75 ? 230 TYR B O   1 
ATOM   3890 C  CB  . TYR B 1 230 ? 22.942  2.724   -28.445 1.00 19.72 ? 230 TYR B CB  1 
ATOM   3891 C  CG  . TYR B 1 230 ? 24.261  2.184   -27.947 1.00 21.66 ? 230 TYR B CG  1 
ATOM   3892 C  CD1 . TYR B 1 230 ? 24.418  0.854   -27.587 1.00 23.89 ? 230 TYR B CD1 1 
ATOM   3893 C  CD2 . TYR B 1 230 ? 25.369  3.011   -27.847 1.00 23.60 ? 230 TYR B CD2 1 
ATOM   3894 C  CE1 . TYR B 1 230 ? 25.619  0.364   -27.105 1.00 23.88 ? 230 TYR B CE1 1 
ATOM   3895 C  CE2 . TYR B 1 230 ? 26.585  2.535   -27.382 1.00 24.78 ? 230 TYR B CE2 1 
ATOM   3896 C  CZ  . TYR B 1 230 ? 26.710  1.206   -27.014 1.00 25.04 ? 230 TYR B CZ  1 
ATOM   3897 O  OH  . TYR B 1 230 ? 27.912  0.736   -26.560 1.00 30.30 ? 230 TYR B OH  1 
ATOM   3898 N  N   . CYS B 1 231 ? 20.207  3.694   -27.025 1.00 17.47 ? 231 CYS B N   1 
ATOM   3899 C  CA  . CYS B 1 231 ? 19.071  4.615   -27.133 1.00 20.08 ? 231 CYS B CA  1 
ATOM   3900 C  C   . CYS B 1 231 ? 19.590  6.009   -27.461 1.00 17.15 ? 231 CYS B C   1 
ATOM   3901 O  O   . CYS B 1 231 ? 18.789  6.863   -27.566 1.00 16.79 ? 231 CYS B O   1 
ATOM   3902 C  CB  . CYS B 1 231 ? 18.210  4.580   -25.887 1.00 26.42 ? 231 CYS B CB  1 
ATOM   3903 S  SG  . CYS B 1 231 ? 19.121  5.010   -24.401 1.00 40.23 ? 231 CYS B SG  1 
ATOM   3904 N  N   . THR B 1 232 ? 20.878  6.138   -27.733 1.00 16.88 ? 232 THR B N   1 
ATOM   3905 C  CA  . THR B 1 232 ? 21.460  7.431   -28.023 1.00 16.38 ? 232 THR B CA  1 
ATOM   3906 C  C   . THR B 1 232 ? 21.767  7.532   -29.518 1.00 15.54 ? 232 THR B C   1 
ATOM   3907 O  O   . THR B 1 232 ? 21.989  6.517   -30.173 1.00 14.96 ? 232 THR B O   1 
ATOM   3908 C  CB  . THR B 1 232 ? 22.689  7.605   -27.117 1.00 16.76 ? 232 THR B CB  1 
ATOM   3909 O  OG1 . THR B 1 232 ? 23.352  6.335   -27.076 1.00 15.63 ? 232 THR B OG1 1 
ATOM   3910 C  CG2 . THR B 1 232 ? 22.315  8.010   -25.710 1.00 17.53 ? 232 THR B CG2 1 
ATOM   3911 N  N   . HIS B 1 233 ? 21.761  8.765   -30.047 1.00 15.65 ? 233 HIS B N   1 
ATOM   3912 C  CA  . HIS B 1 233 ? 22.372  9.049   -31.337 1.00 18.09 ? 233 HIS B CA  1 
ATOM   3913 C  C   . HIS B 1 233 ? 23.847  8.660   -31.285 1.00 18.38 ? 233 HIS B C   1 
ATOM   3914 O  O   . HIS B 1 233 ? 24.512  8.744   -30.242 1.00 18.63 ? 233 HIS B O   1 
ATOM   3915 C  CB  . HIS B 1 233 ? 22.279  10.549  -31.708 1.00 19.56 ? 233 HIS B CB  1 
ATOM   3916 C  CG  . HIS B 1 233 ? 20.894  11.026  -31.963 1.00 20.63 ? 233 HIS B CG  1 
ATOM   3917 N  ND1 . HIS B 1 233 ? 20.180  10.660  -33.087 1.00 22.81 ? 233 HIS B ND1 1 
ATOM   3918 C  CD2 . HIS B 1 233 ? 20.085  11.837  -31.251 1.00 23.26 ? 233 HIS B CD2 1 
ATOM   3919 C  CE1 . HIS B 1 233 ? 18.978  11.206  -33.040 1.00 21.36 ? 233 HIS B CE1 1 
ATOM   3920 N  NE2 . HIS B 1 233 ? 18.901  11.945  -31.931 1.00 22.56 ? 233 HIS B NE2 1 
ATOM   3921 N  N   . MET B 1 234 ? 24.363  8.273   -32.444 1.00 18.58 ? 234 MET B N   1 
ATOM   3922 C  CA  . MET B 1 234 ? 25.730  7.805   -32.591 1.00 20.85 ? 234 MET B CA  1 
ATOM   3923 C  C   . MET B 1 234 ? 26.712  8.858   -32.073 1.00 21.88 ? 234 MET B C   1 
ATOM   3924 O  O   . MET B 1 234 ? 27.730  8.505   -31.475 1.00 20.94 ? 234 MET B O   1 
ATOM   3925 C  CB  . MET B 1 234 ? 26.011  7.569   -34.079 1.00 22.00 ? 234 MET B CB  1 
ATOM   3926 C  CG  . MET B 1 234 ? 26.521  6.203   -34.411 1.00 24.16 ? 234 MET B CG  1 
ATOM   3927 S  SD  . MET B 1 234 ? 26.826  6.063   -36.208 1.00 27.45 ? 234 MET B SD  1 
ATOM   3928 C  CE  . MET B 1 234 ? 25.550  7.122   -36.888 1.00 24.12 ? 234 MET B CE  1 
ATOM   3929 N  N   . ASP B 1 235 ? 26.411  10.149  -32.304 1.00 22.09 ? 235 ASP B N   1 
ATOM   3930 C  CA  . ASP B 1 235 ? 27.370  11.189  -31.950 1.00 26.59 ? 235 ASP B CA  1 
ATOM   3931 C  C   . ASP B 1 235 ? 27.208  11.653  -30.497 1.00 27.00 ? 235 ASP B C   1 
ATOM   3932 O  O   . ASP B 1 235 ? 27.866  12.602  -30.095 1.00 26.36 ? 235 ASP B O   1 
ATOM   3933 C  CB  . ASP B 1 235 ? 27.371  12.369  -32.929 1.00 28.78 ? 235 ASP B CB  1 
ATOM   3934 C  CG  . ASP B 1 235 ? 26.121  13.236  -32.878 1.00 32.75 ? 235 ASP B CG  1 
ATOM   3935 O  OD1 . ASP B 1 235 ? 25.264  12.978  -32.018 1.00 34.92 ? 235 ASP B OD1 1 
ATOM   3936 O  OD2 . ASP B 1 235 ? 26.018  14.170  -33.698 1.00 31.47 ? 235 ASP B OD2 1 
ATOM   3937 N  N   . ASP B 1 236 ? 26.364  10.977  -29.705 1.00 24.44 ? 236 ASP B N   1 
ATOM   3938 C  CA  . ASP B 1 236 ? 26.077  11.421  -28.344 1.00 23.08 ? 236 ASP B CA  1 
ATOM   3939 C  C   . ASP B 1 236 ? 27.296  11.176  -27.450 1.00 20.94 ? 236 ASP B C   1 
ATOM   3940 O  O   . ASP B 1 236 ? 27.792  10.057  -27.369 1.00 20.60 ? 236 ASP B O   1 
ATOM   3941 C  CB  . ASP B 1 236 ? 24.802  10.751  -27.813 1.00 23.35 ? 236 ASP B CB  1 
ATOM   3942 C  CG  . ASP B 1 236 ? 24.232  11.333  -26.519 1.00 24.07 ? 236 ASP B CG  1 
ATOM   3943 O  OD1 . ASP B 1 236 ? 25.001  11.522  -25.546 1.00 24.62 ? 236 ASP B OD1 1 
ATOM   3944 O  OD2 . ASP B 1 236 ? 23.010  11.546  -26.476 1.00 23.48 ? 236 ASP B OD2 1 
ATOM   3945 N  N   . PRO B 1 237 ? 27.794  12.195  -26.708 1.00 22.69 ? 237 PRO B N   1 
ATOM   3946 C  CA  . PRO B 1 237 ? 28.949  12.019  -25.818 1.00 22.38 ? 237 PRO B CA  1 
ATOM   3947 C  C   . PRO B 1 237 ? 28.723  11.122  -24.605 1.00 22.80 ? 237 PRO B C   1 
ATOM   3948 O  O   . PRO B 1 237 ? 29.679  10.706  -23.955 1.00 23.47 ? 237 PRO B O   1 
ATOM   3949 C  CB  . PRO B 1 237 ? 29.201  13.442  -25.314 1.00 23.84 ? 237 PRO B CB  1 
ATOM   3950 C  CG  . PRO B 1 237 ? 27.830  14.069  -25.333 1.00 23.36 ? 237 PRO B CG  1 
ATOM   3951 C  CD  . PRO B 1 237 ? 27.257  13.571  -26.645 1.00 22.68 ? 237 PRO B CD  1 
ATOM   3952 N  N   . SER B 1 238 ? 27.460  10.818  -24.278 1.00 23.90 ? 238 SER B N   1 
ATOM   3953 C  CA  . SER B 1 238 ? 27.238  9.808   -23.253 1.00 26.08 ? 238 SER B CA  1 
ATOM   3954 C  C   . SER B 1 238 ? 26.314  8.711   -23.777 1.00 24.93 ? 238 SER B C   1 
ATOM   3955 O  O   . SER B 1 238 ? 25.104  8.789   -23.630 1.00 26.71 ? 238 SER B O   1 
ATOM   3956 C  CB  . SER B 1 238 ? 26.784  10.410  -21.937 1.00 28.22 ? 238 SER B CB  1 
ATOM   3957 O  OG  . SER B 1 238 ? 25.769  11.370  -22.156 1.00 29.26 ? 238 SER B OG  1 
ATOM   3958 N  N   . PRO B 1 239 ? 26.863  7.687   -24.466 1.00 26.59 ? 239 PRO B N   1 
ATOM   3959 C  CA  . PRO B 1 239 ? 26.051  6.624   -25.065 1.00 24.58 ? 239 PRO B CA  1 
ATOM   3960 C  C   . PRO B 1 239 ? 25.405  5.737   -24.007 1.00 25.51 ? 239 PRO B C   1 
ATOM   3961 O  O   . PRO B 1 239 ? 26.001  5.468   -22.958 1.00 23.83 ? 239 PRO B O   1 
ATOM   3962 C  CB  . PRO B 1 239 ? 27.073  5.853   -25.915 1.00 24.51 ? 239 PRO B CB  1 
ATOM   3963 C  CG  . PRO B 1 239 ? 28.373  6.090   -25.197 1.00 25.64 ? 239 PRO B CG  1 
ATOM   3964 C  CD  . PRO B 1 239 ? 28.296  7.536   -24.760 1.00 24.64 ? 239 PRO B CD  1 
ATOM   3965 N  N   . ARG B 1 240 ? 24.158  5.328   -24.285 1.00 23.72 ? 240 ARG B N   1 
ATOM   3966 C  CA  . ARG B 1 240 ? 23.375  4.508   -23.374 1.00 23.26 ? 240 ARG B CA  1 
ATOM   3967 C  C   . ARG B 1 240 ? 22.806  3.324   -24.145 1.00 20.30 ? 240 ARG B C   1 
ATOM   3968 O  O   . ARG B 1 240 ? 22.232  3.516   -25.206 1.00 17.35 ? 240 ARG B O   1 
ATOM   3969 C  CB  . ARG B 1 240 ? 22.284  5.345   -22.702 1.00 26.10 ? 240 ARG B CB  1 
ATOM   3970 C  CG  . ARG B 1 240 ? 22.838  6.448   -21.812 1.00 35.99 ? 240 ARG B CG  1 
ATOM   3971 C  CD  . ARG B 1 240 ? 21.830  7.393   -21.186 1.00 40.52 ? 240 ARG B CD  1 
ATOM   3972 N  NE  . ARG B 1 240 ? 21.381  8.518   -22.008 1.00 49.81 ? 240 ARG B NE  1 
ATOM   3973 C  CZ  . ARG B 1 240 ? 20.155  8.659   -22.534 1.00 52.65 ? 240 ARG B CZ  1 
ATOM   3974 N  NH1 . ARG B 1 240 ? 19.225  7.735   -22.343 1.00 54.71 ? 240 ARG B NH1 1 
ATOM   3975 N  NH2 . ARG B 1 240 ? 19.862  9.728   -23.259 1.00 50.62 ? 240 ARG B NH2 1 
ATOM   3976 N  N   . GLU B 1 241 ? 23.023  2.112   -23.616 1.00 19.08 ? 241 GLU B N   1 
ATOM   3977 C  CA  . GLU B 1 241 ? 22.397  0.885   -24.079 1.00 18.61 ? 241 GLU B CA  1 
ATOM   3978 C  C   . GLU B 1 241 ? 20.879  1.026   -23.947 1.00 17.31 ? 241 GLU B C   1 
ATOM   3979 O  O   . GLU B 1 241 ? 20.377  1.656   -23.020 1.00 17.38 ? 241 GLU B O   1 
ATOM   3980 C  CB  . GLU B 1 241 ? 22.852  -0.288  -23.206 1.00 20.94 ? 241 GLU B CB  1 
ATOM   3981 C  CG  . GLU B 1 241 ? 24.291  -0.726  -23.454 1.00 24.64 ? 241 GLU B CG  1 
ATOM   3982 C  CD  . GLU B 1 241 ? 24.881  -1.544  -22.314 1.00 28.69 ? 241 GLU B CD  1 
ATOM   3983 O  OE1 . GLU B 1 241 ? 24.171  -1.752  -21.312 1.00 32.29 ? 241 GLU B OE1 1 
ATOM   3984 O  OE2 . GLU B 1 241 ? 26.037  -1.991  -22.429 1.00 30.83 ? 241 GLU B OE2 1 
ATOM   3985 N  N   . MET B 1 242 ? 20.138  0.469   -24.907 1.00 14.87 ? 242 MET B N   1 
ATOM   3986 C  CA  . MET B 1 242 ? 18.697  0.470   -24.787 1.00 13.13 ? 242 MET B CA  1 
ATOM   3987 C  C   . MET B 1 242 ? 18.309  -0.843  -24.131 1.00 12.79 ? 242 MET B C   1 
ATOM   3988 O  O   . MET B 1 242 ? 18.231  -1.885  -24.787 1.00 12.93 ? 242 MET B O   1 
ATOM   3989 C  CB  . MET B 1 242 ? 17.998  0.595   -26.150 1.00 13.26 ? 242 MET B CB  1 
ATOM   3990 C  CG  . MET B 1 242 ? 16.466  0.640   -26.041 1.00 12.45 ? 242 MET B CG  1 
ATOM   3991 S  SD  . MET B 1 242 ? 15.689  0.570   -27.672 1.00 12.37 ? 242 MET B SD  1 
ATOM   3992 C  CE  . MET B 1 242 ? 16.203  2.128   -28.396 1.00 12.43 ? 242 MET B CE  1 
ATOM   3993 N  N   . ILE B 1 243 ? 18.087  -0.766  -22.818 1.00 11.89 ? 243 ILE B N   1 
ATOM   3994 C  CA  . ILE B 1 243 ? 17.675  -1.894  -22.005 1.00 11.52 ? 243 ILE B CA  1 
ATOM   3995 C  C   . ILE B 1 243 ? 16.625  -1.381  -21.020 1.00 10.50 ? 243 ILE B C   1 
ATOM   3996 O  O   . ILE B 1 243 ? 16.532  -0.165  -20.764 1.00 8.66  ? 243 ILE B O   1 
ATOM   3997 C  CB  . ILE B 1 243 ? 18.891  -2.452  -21.232 1.00 12.50 ? 243 ILE B CB  1 
ATOM   3998 C  CG1 . ILE B 1 243 ? 19.597  -1.359  -20.411 1.00 12.42 ? 243 ILE B CG1 1 
ATOM   3999 C  CG2 . ILE B 1 243 ? 19.846  -3.205  -22.151 1.00 12.43 ? 243 ILE B CG2 1 
ATOM   4000 C  CD1 . ILE B 1 243 ? 20.534  -1.917  -19.336 1.00 15.14 ? 243 ILE B CD1 1 
ATOM   4001 N  N   . ASN B 1 244 ? 15.873  -2.331  -20.446 1.00 9.61  ? 244 ASN B N   1 
ATOM   4002 C  CA  . ASN B 1 244 ? 14.901  -2.002  -19.407 1.00 9.63  ? 244 ASN B CA  1 
ATOM   4003 C  C   . ASN B 1 244 ? 13.920  -0.936  -19.891 1.00 9.27  ? 244 ASN B C   1 
ATOM   4004 O  O   . ASN B 1 244 ? 13.595  -0.019  -19.137 1.00 8.85  ? 244 ASN B O   1 
ATOM   4005 C  CB  . ASN B 1 244 ? 15.606  -1.479  -18.145 1.00 10.08 ? 244 ASN B CB  1 
ATOM   4006 C  CG  . ASN B 1 244 ? 16.569  -2.502  -17.574 1.00 10.66 ? 244 ASN B CG  1 
ATOM   4007 O  OD1 . ASN B 1 244 ? 16.358  -3.710  -17.716 1.00 10.90 ? 244 ASN B OD1 1 
ATOM   4008 N  ND2 . ASN B 1 244 ? 17.661  -2.034  -16.984 1.00 10.95 ? 244 ASN B ND2 1 
ATOM   4009 N  N   . ASN B 1 245 ? 13.461  -1.041  -21.143 1.00 8.63  ? 245 ASN B N   1 
ATOM   4010 C  CA  . ASN B 1 245 ? 12.656  0.020   -21.737 1.00 8.60  ? 245 ASN B CA  1 
ATOM   4011 C  C   . ASN B 1 245 ? 11.174  -0.324  -21.559 1.00 8.79  ? 245 ASN B C   1 
ATOM   4012 O  O   . ASN B 1 245 ? 10.430  -0.359  -22.541 1.00 8.44  ? 245 ASN B O   1 
ATOM   4013 C  CB  . ASN B 1 245 ? 13.018  0.245   -23.211 1.00 8.90  ? 245 ASN B CB  1 
ATOM   4014 C  CG  . ASN B 1 245 ? 12.799  -0.987  -24.071 1.00 9.13  ? 245 ASN B CG  1 
ATOM   4015 O  OD1 . ASN B 1 245 ? 12.821  -2.109  -23.558 1.00 8.19  ? 245 ASN B OD1 1 
ATOM   4016 N  ND2 . ASN B 1 245 ? 12.588  -0.791  -25.380 1.00 9.34  ? 245 ASN B ND2 1 
ATOM   4017 N  N   . PHE B 1 246 ? 10.788  -0.661  -20.302 1.00 8.34  ? 246 PHE B N   1 
ATOM   4018 C  CA  . PHE B 1 246 ? 9.432   -1.040  -19.951 1.00 8.21  ? 246 PHE B CA  1 
ATOM   4019 C  C   . PHE B 1 246 ? 8.985   -0.198  -18.761 1.00 8.02  ? 246 PHE B C   1 
ATOM   4020 O  O   . PHE B 1 246 ? 9.805   0.242   -17.973 1.00 8.46  ? 246 PHE B O   1 
ATOM   4021 C  CB  . PHE B 1 246 ? 9.319   -2.537  -19.608 1.00 8.11  ? 246 PHE B CB  1 
ATOM   4022 C  CG  . PHE B 1 246 ? 10.103  -2.950  -18.393 1.00 8.24  ? 246 PHE B CG  1 
ATOM   4023 C  CD1 . PHE B 1 246 ? 11.470  -3.214  -18.492 1.00 8.34  ? 246 PHE B CD1 1 
ATOM   4024 C  CD2 . PHE B 1 246 ? 9.508   -3.015  -17.137 1.00 7.97  ? 246 PHE B CD2 1 
ATOM   4025 C  CE1 . PHE B 1 246 ? 12.200  -3.593  -17.368 1.00 8.66  ? 246 PHE B CE1 1 
ATOM   4026 C  CE2 . PHE B 1 246 ? 10.242  -3.393  -16.016 1.00 7.73  ? 246 PHE B CE2 1 
ATOM   4027 C  CZ  . PHE B 1 246 ? 11.586  -3.682  -16.132 1.00 8.12  ? 246 PHE B CZ  1 
ATOM   4028 N  N   . ARG B 1 247 ? 7.676   0.031   -18.635 1.00 8.34  ? 247 ARG B N   1 
ATOM   4029 C  CA  . ARG B 1 247 ? 7.175   0.821   -17.513 1.00 8.07  ? 247 ARG B CA  1 
ATOM   4030 C  C   . ARG B 1 247 ? 6.835   -0.138  -16.382 1.00 8.15  ? 247 ARG B C   1 
ATOM   4031 O  O   . ARG B 1 247 ? 6.351   -1.245  -16.665 1.00 8.26  ? 247 ARG B O   1 
ATOM   4032 C  CB  . ARG B 1 247 ? 5.914   1.582   -17.893 1.00 7.44  ? 247 ARG B CB  1 
ATOM   4033 C  CG  . ARG B 1 247 ? 5.614   2.759   -16.966 1.00 7.49  ? 247 ARG B CG  1 
ATOM   4034 C  CD  . ARG B 1 247 ? 4.195   3.246   -17.242 1.00 7.45  ? 247 ARG B CD  1 
ATOM   4035 N  NE  . ARG B 1 247 ? 3.933   4.535   -16.612 1.00 7.14  ? 247 ARG B NE  1 
ATOM   4036 C  CZ  . ARG B 1 247 ? 2.807   5.239   -16.720 1.00 6.74  ? 247 ARG B CZ  1 
ATOM   4037 N  NH1 . ARG B 1 247 ? 1.797   4.801   -17.467 1.00 6.38  ? 247 ARG B NH1 1 
ATOM   4038 N  NH2 . ARG B 1 247 ? 2.726   6.390   -16.079 1.00 6.31  ? 247 ARG B NH2 1 
ATOM   4039 N  N   . GLN B 1 248 ? 7.109   0.298   -15.134 1.00 8.07  ? 248 GLN B N   1 
ATOM   4040 C  CA  . GLN B 1 248 ? 6.735   -0.413  -13.923 1.00 8.64  ? 248 GLN B CA  1 
ATOM   4041 C  C   . GLN B 1 248 ? 5.215   -0.542  -13.961 1.00 8.71  ? 248 GLN B C   1 
ATOM   4042 O  O   . GLN B 1 248 ? 4.548   0.268   -14.605 1.00 8.81  ? 248 GLN B O   1 
ATOM   4043 C  CB  . GLN B 1 248 ? 7.196   0.331   -12.651 1.00 9.02  ? 248 GLN B CB  1 
ATOM   4044 C  CG  . GLN B 1 248 ? 8.706   0.350   -12.369 1.00 9.32  ? 248 GLN B CG  1 
ATOM   4045 C  CD  . GLN B 1 248 ? 9.354   -1.017  -12.241 1.00 10.36 ? 248 GLN B CD  1 
ATOM   4046 O  OE1 . GLN B 1 248 ? 9.328   -1.669  -11.176 1.00 11.27 ? 248 GLN B OE1 1 
ATOM   4047 N  NE2 . GLN B 1 248 ? 9.946   -1.471  -13.334 1.00 9.00  ? 248 GLN B NE2 1 
ATOM   4048 N  N   . VAL B 1 249 ? 4.672   -1.564  -13.276 1.00 8.68  ? 249 VAL B N   1 
ATOM   4049 C  CA  . VAL B 1 249 ? 3.232   -1.793  -13.303 1.00 8.36  ? 249 VAL B CA  1 
ATOM   4050 C  C   . VAL B 1 249 ? 2.557   -0.741  -12.428 1.00 8.49  ? 249 VAL B C   1 
ATOM   4051 O  O   . VAL B 1 249 ? 3.156   -0.241  -11.470 1.00 7.72  ? 249 VAL B O   1 
ATOM   4052 C  CB  . VAL B 1 249 ? 2.803   -3.211  -12.837 1.00 8.51  ? 249 VAL B CB  1 
ATOM   4053 C  CG1 . VAL B 1 249 ? 3.250   -4.299  -13.804 1.00 8.46  ? 249 VAL B CG1 1 
ATOM   4054 C  CG2 . VAL B 1 249 ? 3.337   -3.508  -11.450 1.00 8.79  ? 249 VAL B CG2 1 
ATOM   4055 N  N   . GLN B 1 250 ? 1.289   -0.462  -12.768 1.00 8.21  ? 250 GLN B N   1 
ATOM   4056 C  CA  . GLN B 1 250 ? 0.583   0.650   -12.161 1.00 9.31  ? 250 GLN B CA  1 
ATOM   4057 C  C   . GLN B 1 250 ? -0.467  0.096   -11.201 1.00 9.87  ? 250 GLN B C   1 
ATOM   4058 O  O   . GLN B 1 250 ? -0.957  -1.014  -11.408 1.00 10.06 ? 250 GLN B O   1 
ATOM   4059 C  CB  . GLN B 1 250 ? -0.075  1.499   -13.255 1.00 8.29  ? 250 GLN B CB  1 
ATOM   4060 C  CG  . GLN B 1 250 ? 0.917   1.990   -14.318 1.00 8.82  ? 250 GLN B CG  1 
ATOM   4061 C  CD  . GLN B 1 250 ? 1.841   3.069   -13.796 1.00 8.53  ? 250 GLN B CD  1 
ATOM   4062 O  OE1 . GLN B 1 250 ? 1.419   4.152   -13.375 1.00 8.60  ? 250 GLN B OE1 1 
ATOM   4063 N  NE2 . GLN B 1 250 ? 3.125   2.816   -13.889 1.00 8.35  ? 250 GLN B NE2 1 
ATOM   4064 N  N   . LYS B 1 251 ? -0.821  0.875   -10.172 1.00 10.99 ? 251 LYS B N   1 
ATOM   4065 C  CA  . LYS B 1 251 ? -1.940  0.471   -9.321  1.00 12.87 ? 251 LYS B CA  1 
ATOM   4066 C  C   . LYS B 1 251 ? -3.221  0.475   -10.141 1.00 15.19 ? 251 LYS B C   1 
ATOM   4067 O  O   . LYS B 1 251 ? -3.440  1.372   -10.957 1.00 14.87 ? 251 LYS B O   1 
ATOM   4068 C  CB  . LYS B 1 251 ? -2.127  1.378   -8.100  1.00 11.64 ? 251 LYS B CB  1 
ATOM   4069 C  CG  . LYS B 1 251 ? -0.986  1.303   -7.087  1.00 10.93 ? 251 LYS B CG  1 
ATOM   4070 C  CD  . LYS B 1 251 ? -1.183  2.240   -5.921  1.00 10.42 ? 251 LYS B CD  1 
ATOM   4071 C  CE  . LYS B 1 251 ? -0.244  2.008   -4.751  1.00 10.29 ? 251 LYS B CE  1 
ATOM   4072 N  NZ  . LYS B 1 251 ? 1.187   1.957   -5.146  1.00 8.63  ? 251 LYS B NZ  1 
ATOM   4073 N  N   . PHE B 1 252 ? -4.056  -0.534  -9.904  1.00 18.79 ? 252 PHE B N   1 
ATOM   4074 C  CA  . PHE B 1 252 ? -5.232  -0.747  -10.730 1.00 26.01 ? 252 PHE B CA  1 
ATOM   4075 C  C   . PHE B 1 252 ? -6.365  -1.111  -9.788  1.00 31.70 ? 252 PHE B C   1 
ATOM   4076 O  O   . PHE B 1 252 ? -6.641  -2.288  -9.581  1.00 35.01 ? 252 PHE B O   1 
ATOM   4077 C  CB  . PHE B 1 252 ? -4.957  -1.851  -11.759 1.00 26.43 ? 252 PHE B CB  1 
ATOM   4078 C  CG  . PHE B 1 252 ? -6.006  -2.060  -12.826 1.00 27.08 ? 252 PHE B CG  1 
ATOM   4079 C  CD1 . PHE B 1 252 ? -6.166  -1.150  -13.864 1.00 28.87 ? 252 PHE B CD1 1 
ATOM   4080 C  CD2 . PHE B 1 252 ? -6.812  -3.190  -12.820 1.00 29.78 ? 252 PHE B CD2 1 
ATOM   4081 C  CE1 . PHE B 1 252 ? -7.112  -1.355  -14.861 1.00 30.56 ? 252 PHE B CE1 1 
ATOM   4082 C  CE2 . PHE B 1 252 ? -7.768  -3.398  -13.810 1.00 29.14 ? 252 PHE B CE2 1 
ATOM   4083 C  CZ  . PHE B 1 252 ? -7.914  -2.481  -14.829 1.00 32.75 ? 252 PHE B CZ  1 
ATOM   4084 N  N   . ASP B 1 253 ? -6.961  -0.085  -9.180  1.00 39.12 ? 253 ASP B N   1 
ATOM   4085 C  CA  . ASP B 1 253 ? -7.752  -0.279  -7.974  1.00 45.85 ? 253 ASP B CA  1 
ATOM   4086 C  C   . ASP B 1 253 ? -9.240  -0.368  -8.318  1.00 43.64 ? 253 ASP B C   1 
ATOM   4087 O  O   . ASP B 1 253 ? -9.760  0.462   -9.063  1.00 36.66 ? 253 ASP B O   1 
ATOM   4088 C  CB  . ASP B 1 253 ? -7.383  0.723   -6.872  1.00 54.23 ? 253 ASP B CB  1 
ATOM   4089 C  CG  . ASP B 1 253 ? -6.992  2.109   -7.365  1.00 61.79 ? 253 ASP B CG  1 
ATOM   4090 O  OD1 . ASP B 1 253 ? -7.512  2.535   -8.419  1.00 64.59 ? 253 ASP B OD1 1 
ATOM   4091 O  OD2 . ASP B 1 253 ? -6.163  2.754   -6.687  1.00 70.37 ? 253 ASP B OD2 1 
ATOM   4092 N  N   . GLU B 1 254 ? -9.888  -1.416  -7.782  1.00 46.93 ? 254 GLU B N   1 
ATOM   4093 C  CA  . GLU B 1 254 ? -11.306 -1.713  -7.950  1.00 49.66 ? 254 GLU B CA  1 
ATOM   4094 C  C   . GLU B 1 254 ? -11.725 -1.572  -9.421  1.00 49.06 ? 254 GLU B C   1 
ATOM   4095 O  O   . GLU B 1 254 ? -12.825 -1.111  -9.744  1.00 47.01 ? 254 GLU B O   1 
ATOM   4096 C  CB  . GLU B 1 254 ? -12.158 -0.940  -6.932  1.00 53.94 ? 254 GLU B CB  1 
ATOM   4097 C  CG  . GLU B 1 254 ? -11.895 0.559   -6.901  1.00 57.61 ? 254 GLU B CG  1 
ATOM   4098 C  CD  . GLU B 1 254 ? -12.943 1.404   -6.195  1.00 63.32 ? 254 GLU B CD  1 
ATOM   4099 O  OE1 . GLU B 1 254 ? -12.901 2.644   -6.357  1.00 63.08 ? 254 GLU B OE1 1 
ATOM   4100 O  OE2 . GLU B 1 254 ? -13.799 0.825   -5.487  1.00 69.08 ? 254 GLU B OE2 1 
ATOM   4101 N  N   . ARG B 1 255 ? -10.809 -1.952  -10.318 1.00 43.45 ? 255 ARG B N   1 
ATOM   4102 C  CA  . ARG B 1 255 ? -11.117 -2.115  -11.729 1.00 38.88 ? 255 ARG B CA  1 
ATOM   4103 C  C   . ARG B 1 255 ? -10.971 -3.592  -12.072 1.00 31.96 ? 255 ARG B C   1 
ATOM   4104 O  O   . ARG B 1 255 ? -10.259 -4.320  -11.389 1.00 30.17 ? 255 ARG B O   1 
ATOM   4105 C  CB  . ARG B 1 255 ? -10.206 -1.251  -12.604 1.00 39.75 ? 255 ARG B CB  1 
ATOM   4106 C  CG  . ARG B 1 255 ? -10.766 0.120   -12.948 1.00 43.96 ? 255 ARG B CG  1 
ATOM   4107 C  CD  . ARG B 1 255 ? -9.635  1.036   -13.380 1.00 48.34 ? 255 ARG B CD  1 
ATOM   4108 N  NE  . ARG B 1 255 ? -8.917  1.502   -12.196 1.00 55.11 ? 255 ARG B NE  1 
ATOM   4109 C  CZ  . ARG B 1 255 ? -7.655  1.937   -12.149 1.00 54.00 ? 255 ARG B CZ  1 
ATOM   4110 N  NH1 . ARG B 1 255 ? -6.910  1.988   -13.241 1.00 53.83 ? 255 ARG B NH1 1 
ATOM   4111 N  NH2 . ARG B 1 255 ? -7.146  2.332   -10.995 1.00 52.22 ? 255 ARG B NH2 1 
ATOM   4112 N  N   . LEU B 1 256 ? -11.667 -4.014  -13.127 1.00 28.38 ? 256 LEU B N   1 
ATOM   4113 C  CA  . LEU B 1 256 ? -11.631 -5.399  -13.563 1.00 29.67 ? 256 LEU B CA  1 
ATOM   4114 C  C   . LEU B 1 256 ? -10.864 -5.510  -14.879 1.00 26.21 ? 256 LEU B C   1 
ATOM   4115 O  O   . LEU B 1 256 ? -10.857 -4.595  -15.708 1.00 25.78 ? 256 LEU B O   1 
ATOM   4116 C  CB  . LEU B 1 256 ? -13.069 -5.903  -13.739 1.00 31.10 ? 256 LEU B CB  1 
ATOM   4117 C  CG  . LEU B 1 256 ? -13.718 -6.596  -12.539 1.00 34.41 ? 256 LEU B CG  1 
ATOM   4118 C  CD1 . LEU B 1 256 ? -13.064 -6.222  -11.218 1.00 37.44 ? 256 LEU B CD1 1 
ATOM   4119 C  CD2 . LEU B 1 256 ? -15.207 -6.297  -12.497 1.00 34.96 ? 256 LEU B CD2 1 
ATOM   4120 N  N   . VAL B 1 257 ? -10.238 -6.674  -15.059 1.00 23.74 ? 257 VAL B N   1 
ATOM   4121 C  CA  . VAL B 1 257 ? -9.751  -7.089  -16.362 1.00 21.83 ? 257 VAL B CA  1 
ATOM   4122 C  C   . VAL B 1 257 ? -10.663 -8.211  -16.829 1.00 20.60 ? 257 VAL B C   1 
ATOM   4123 O  O   . VAL B 1 257 ? -10.880 -9.175  -16.099 1.00 20.97 ? 257 VAL B O   1 
ATOM   4124 C  CB  . VAL B 1 257 ? -8.289  -7.561  -16.286 1.00 22.04 ? 257 VAL B CB  1 
ATOM   4125 C  CG1 . VAL B 1 257 ? -7.766  -7.958  -17.657 1.00 21.89 ? 257 VAL B CG1 1 
ATOM   4126 C  CG2 . VAL B 1 257 ? -7.399  -6.513  -15.634 1.00 21.59 ? 257 VAL B CG2 1 
ATOM   4127 N  N   . TYR B 1 258 ? -11.197 -8.046  -18.035 1.00 18.07 ? 258 TYR B N   1 
ATOM   4128 C  CA  . TYR B 1 258 ? -12.084 -9.030  -18.627 1.00 17.81 ? 258 TYR B CA  1 
ATOM   4129 C  C   . TYR B 1 258 ? -11.255 -10.036 -19.406 1.00 15.73 ? 258 TYR B C   1 
ATOM   4130 O  O   . TYR B 1 258 ? -10.240 -9.673  -19.994 1.00 14.65 ? 258 TYR B O   1 
ATOM   4131 C  CB  . TYR B 1 258 ? -13.166 -8.314  -19.439 1.00 18.54 ? 258 TYR B CB  1 
ATOM   4132 C  CG  . TYR B 1 258 ? -13.824 -7.246  -18.604 1.00 20.95 ? 258 TYR B CG  1 
ATOM   4133 C  CD1 . TYR B 1 258 ? -13.318 -5.952  -18.568 1.00 22.17 ? 258 TYR B CD1 1 
ATOM   4134 C  CD2 . TYR B 1 258 ? -14.891 -7.563  -17.772 1.00 21.55 ? 258 TYR B CD2 1 
ATOM   4135 C  CE1 . TYR B 1 258 ? -13.888 -4.984  -17.753 1.00 25.40 ? 258 TYR B CE1 1 
ATOM   4136 C  CE2 . TYR B 1 258 ? -15.486 -6.601  -16.970 1.00 24.41 ? 258 TYR B CE2 1 
ATOM   4137 C  CZ  . TYR B 1 258 ? -14.980 -5.315  -16.962 1.00 25.75 ? 258 TYR B CZ  1 
ATOM   4138 O  OH  . TYR B 1 258 ? -15.575 -4.390  -16.164 1.00 31.25 ? 258 TYR B OH  1 
ATOM   4139 N  N   . THR B 1 259 ? -11.715 -11.298 -19.386 1.00 14.86 ? 259 THR B N   1 
ATOM   4140 C  CA  . THR B 1 259 ? -11.024 -12.376 -20.064 1.00 13.26 ? 259 THR B CA  1 
ATOM   4141 C  C   . THR B 1 259 ? -11.974 -13.054 -21.051 1.00 12.75 ? 259 THR B C   1 
ATOM   4142 O  O   . THR B 1 259 ? -13.158 -13.238 -20.784 1.00 12.20 ? 259 THR B O   1 
ATOM   4143 C  CB  . THR B 1 259 ? -10.471 -13.386 -19.053 1.00 13.33 ? 259 THR B CB  1 
ATOM   4144 O  OG1 . THR B 1 259 ? -11.583 -13.966 -18.359 1.00 13.06 ? 259 THR B OG1 1 
ATOM   4145 C  CG2 . THR B 1 259 ? -9.499  -12.767 -18.076 1.00 12.59 ? 259 THR B CG2 1 
ATOM   4146 N  N   . SER B 1 260 ? -11.429 -13.487 -22.182 1.00 11.88 ? 260 SER B N   1 
ATOM   4147 C  CA  . SER B 1 260 ? -12.256 -14.177 -23.157 1.00 12.65 ? 260 SER B CA  1 
ATOM   4148 C  C   . SER B 1 260 ? -12.388 -15.666 -22.817 1.00 12.99 ? 260 SER B C   1 
ATOM   4149 O  O   . SER B 1 260 ? -13.169 -16.395 -23.442 1.00 12.84 ? 260 SER B O   1 
ATOM   4150 C  CB  . SER B 1 260 ? -11.752 -13.926 -24.560 1.00 11.40 ? 260 SER B CB  1 
ATOM   4151 O  OG  . SER B 1 260 ? -10.481 -14.513 -24.764 1.00 11.03 ? 260 SER B OG  1 
ATOM   4152 N  N   . PHE B 1 261 ? -11.624 -16.115 -21.814 1.00 13.36 ? 261 PHE B N   1 
ATOM   4153 C  CA  . PHE B 1 261 ? -11.589 -17.503 -21.368 1.00 14.78 ? 261 PHE B CA  1 
ATOM   4154 C  C   . PHE B 1 261 ? -12.077 -17.545 -19.927 1.00 16.69 ? 261 PHE B C   1 
ATOM   4155 O  O   . PHE B 1 261 ? -11.865 -16.568 -19.198 1.00 17.19 ? 261 PHE B O   1 
ATOM   4156 C  CB  . PHE B 1 261 ? -10.150 -18.038 -21.358 1.00 13.49 ? 261 PHE B CB  1 
ATOM   4157 C  CG  . PHE B 1 261 ? -9.142  -17.097 -20.730 1.00 12.48 ? 261 PHE B CG  1 
ATOM   4158 C  CD1 . PHE B 1 261 ? -8.654  -16.004 -21.445 1.00 12.10 ? 261 PHE B CD1 1 
ATOM   4159 C  CD2 . PHE B 1 261 ? -8.733  -17.259 -19.410 1.00 12.05 ? 261 PHE B CD2 1 
ATOM   4160 C  CE1 . PHE B 1 261 ? -7.756  -15.120 -20.867 1.00 11.22 ? 261 PHE B CE1 1 
ATOM   4161 C  CE2 . PHE B 1 261 ? -7.840  -16.366 -18.831 1.00 11.56 ? 261 PHE B CE2 1 
ATOM   4162 C  CZ  . PHE B 1 261 ? -7.342  -15.318 -19.571 1.00 11.08 ? 261 PHE B CZ  1 
ATOM   4163 N  N   . SER B 1 262 ? -12.705 -18.670 -19.520 1.00 17.73 ? 262 SER B N   1 
ATOM   4164 C  CA  . SER B 1 262 ? -13.256 -18.758 -18.173 1.00 20.98 ? 262 SER B CA  1 
ATOM   4165 C  C   . SER B 1 262 ? -12.331 -19.505 -17.217 1.00 22.33 ? 262 SER B C   1 
ATOM   4166 O  O   . SER B 1 262 ? -12.468 -19.357 -16.002 1.00 28.91 ? 262 SER B O   1 
ATOM   4167 C  CB  . SER B 1 262 ? -14.688 -19.292 -18.139 1.00 22.49 ? 262 SER B CB  1 
ATOM   4168 O  OG  . SER B 1 262 ? -14.764 -20.572 -18.742 1.00 24.12 ? 262 SER B OG  1 
ATOM   4169 N  N   . GLN B 1 263 ? -11.384 -20.277 -17.760 1.00 21.65 ? 263 GLN B N   1 
ATOM   4170 C  CA  . GLN B 1 263 ? -10.389 -20.981 -16.964 1.00 23.35 ? 263 GLN B CA  1 
ATOM   4171 C  C   . GLN B 1 263 ? -9.089  -21.099 -17.778 1.00 22.67 ? 263 GLN B C   1 
ATOM   4172 O  O   . GLN B 1 263 ? -9.187  -20.894 -19.031 1.00 25.22 ? 263 GLN B O   1 
ATOM   4173 C  CB  . GLN B 1 263 ? -10.916 -22.363 -16.559 1.00 22.11 ? 263 GLN B CB  1 
ATOM   4174 C  CG  . GLN B 1 263 ? -11.421 -23.198 -17.730 1.00 23.55 ? 263 GLN B CG  1 
ATOM   4175 C  CD  . GLN B 1 263 ? -11.761 -24.595 -17.268 1.00 25.68 ? 263 GLN B CD  1 
ATOM   4176 O  OE1 . GLN B 1 263 ? -12.113 -24.799 -16.106 1.00 28.17 ? 263 GLN B OE1 1 
ATOM   4177 N  NE2 . GLN B 1 263 ? -11.655 -25.566 -18.169 1.00 22.52 ? 263 GLN B NE2 1 
HETATM 4178 ZN ZN  . ZN  C 2 .   ? 7.835   2.966   5.393   1.00 8.94  ? 301 ZN  A ZN  1 
HETATM 4179 C  C1  . EDO D 3 .   ? -1.427  14.481  -13.429 1.00 22.68 ? 302 EDO A C1  1 
HETATM 4180 O  O1  . EDO D 3 .   ? -0.074  14.082  -13.269 1.00 17.65 ? 302 EDO A O1  1 
HETATM 4181 C  C2  . EDO D 3 .   ? -2.256  14.668  -12.218 1.00 22.42 ? 302 EDO A C2  1 
HETATM 4182 O  O2  . EDO D 3 .   ? -1.497  15.108  -11.113 1.00 23.48 ? 302 EDO A O2  1 
HETATM 4183 C  C12 . JTW E 4 .   ? 7.981   8.542   6.833   1.00 16.24 ? 303 JTW A C12 1 
HETATM 4184 C  C21 . JTW E 4 .   ? 11.955  11.052  7.447   1.00 22.04 ? 303 JTW A C21 1 
HETATM 4185 C  C22 . JTW E 4 .   ? 13.279  10.998  7.875   1.00 25.49 ? 303 JTW A C22 1 
HETATM 4186 C  C23 . JTW E 4 .   ? 14.180  11.930  7.372   1.00 26.24 ? 303 JTW A C23 1 
HETATM 4187 C  C5  . JTW E 4 .   ? 10.488  6.069   5.687   1.00 10.57 ? 303 JTW A C5  1 
HETATM 4188 C  C6  . JTW E 4 .   ? 11.683  6.508   6.202   1.00 11.63 ? 303 JTW A C6  1 
HETATM 4189 C  C8  . JTW E 4 .   ? 10.540  8.372   7.169   1.00 16.30 ? 303 JTW A C8  1 
HETATM 4190 C  C9  . JTW E 4 .   ? 9.322   7.949   6.634   1.00 14.67 ? 303 JTW A C9  1 
HETATM 4191 C  C10 . JTW E 4 .   ? 9.302   6.754   5.908   1.00 12.44 ? 303 JTW A C10 1 
HETATM 4192 O  O20 . JTW E 4 .   ? 9.430   10.634  8.187   1.00 23.19 ? 303 JTW A O20 1 
HETATM 4193 S  S18 . JTW E 4 .   ? 10.785  9.873   8.082   1.00 20.32 ? 303 JTW A S18 1 
HETATM 4194 O  O19 . JTW E 4 .   ? 11.086  9.541   9.569   1.00 22.42 ? 303 JTW A O19 1 
HETATM 4195 C  C25 . JTW E 4 .   ? 11.505  12.021  6.534   1.00 24.71 ? 303 JTW A C25 1 
HETATM 4196 C  C26 . JTW E 4 .   ? 12.398  12.956  6.017   1.00 25.27 ? 303 JTW A C26 1 
HETATM 4197 C  C24 . JTW E 4 .   ? 13.733  12.892  6.452   1.00 27.61 ? 303 JTW A C24 1 
HETATM 4198 C  C7  . JTW E 4 .   ? 11.720  7.679   6.932   1.00 13.75 ? 303 JTW A C7  1 
HETATM 4199 CL CL1 . JTW E 4 .   ? 13.205  5.682   5.965   1.00 10.98 ? 303 JTW A CL1 1 
HETATM 4200 S  S2  . JTW E 4 .   ? 10.352  4.534   4.792   1.00 9.30  ? 303 JTW A S2  1 
HETATM 4201 O  O3  . JTW E 4 .   ? 11.348  4.385   3.689   1.00 8.75  ? 303 JTW A O3  1 
HETATM 4202 O  O4  . JTW E 4 .   ? 10.630  3.497   5.876   1.00 8.21  ? 303 JTW A O4  1 
HETATM 4203 N  N1  . JTW E 4 .   ? 8.741   4.241   4.209   1.00 9.19  ? 303 JTW A N1  1 
HETATM 4204 O  O13 . JTW E 4 .   ? 7.541   8.432   7.980   1.00 15.98 ? 303 JTW A O13 1 
HETATM 4205 N  N14 . JTW E 4 .   ? 7.263   9.031   5.795   1.00 15.50 ? 303 JTW A N14 1 
HETATM 4206 C  C15 . JTW E 4 .   ? 5.913   9.513   5.956   1.00 20.69 ? 303 JTW A C15 1 
HETATM 4207 C  C16 . JTW E 4 .   ? 4.862   8.380   5.741   1.00 25.62 ? 303 JTW A C16 1 
HETATM 4208 O  O17 . JTW E 4 .   ? 5.110   6.958   5.994   1.00 29.90 ? 303 JTW A O17 1 
HETATM 4209 ZN ZN  . ZN  F 2 .   ? 4.506   -0.512  -26.031 1.00 8.79  ? 301 ZN  B ZN  1 
HETATM 4210 C  C12 . JTW G 4 .   ? 5.334   4.343   -28.802 1.00 16.36 ? 302 JTW B C12 1 
HETATM 4211 C  C21 . JTW G 4 .   ? 2.421   7.458   -30.002 1.00 18.44 ? 302 JTW B C21 1 
HETATM 4212 C  C22 . JTW G 4 .   ? 1.159   7.960   -30.296 1.00 19.47 ? 302 JTW B C22 1 
HETATM 4213 C  C23 . JTW G 4 .   ? 0.874   9.250   -29.831 1.00 20.39 ? 302 JTW B C23 1 
HETATM 4214 C  C5  . JTW G 4 .   ? 2.350   2.691   -27.320 1.00 12.02 ? 302 JTW B C5  1 
HETATM 4215 C  C6  . JTW G 4 .   ? 1.249   3.229   -27.968 1.00 12.12 ? 302 JTW B C6  1 
HETATM 4216 C  C8  . JTW G 4 .   ? 2.762   4.567   -29.234 1.00 14.91 ? 302 JTW B C8  1 
HETATM 4217 C  C9  . JTW G 4 .   ? 3.889   4.018   -28.562 1.00 14.84 ? 302 JTW B C9  1 
HETATM 4218 C  C10 . JTW G 4 .   ? 3.667   3.063   -27.582 1.00 12.53 ? 302 JTW B C10 1 
HETATM 4219 O  O20 . JTW G 4 .   ? 4.296   5.886   -31.056 1.00 16.27 ? 302 JTW B O20 1 
HETATM 4220 S  S18 . JTW G 4 .   ? 2.863   5.835   -30.512 1.00 18.32 ? 302 JTW B S18 1 
HETATM 4221 O  O19 . JTW G 4 .   ? 1.964   5.434   -31.665 1.00 18.97 ? 302 JTW B O19 1 
HETATM 4222 C  C25 . JTW G 4 .   ? 3.377   8.162   -29.284 1.00 19.08 ? 302 JTW B C25 1 
HETATM 4223 C  C26 . JTW G 4 .   ? 3.056   9.459   -28.838 1.00 20.82 ? 302 JTW B C26 1 
HETATM 4224 C  C24 . JTW G 4 .   ? 1.804   9.996   -29.128 1.00 18.92 ? 302 JTW B C24 1 
HETATM 4225 C  C7  . JTW G 4 .   ? 1.467   4.189   -28.944 1.00 13.14 ? 302 JTW B C7  1 
HETATM 4226 CL CL1 . JTW G 4 .   ? -0.404  2.747   -27.594 1.00 10.90 ? 302 JTW B CL1 1 
HETATM 4227 S  S2  . JTW G 4 .   ? 2.151   1.412   -26.091 1.00 11.71 ? 302 JTW B S2  1 
HETATM 4228 O  O3  . JTW G 4 .   ? 1.220   1.761   -24.905 1.00 10.89 ? 302 JTW B O3  1 
HETATM 4229 O  O4  . JTW G 4 .   ? 1.785   0.196   -26.921 1.00 10.99 ? 302 JTW B O4  1 
HETATM 4230 N  N1  . JTW G 4 .   ? 3.696   1.025   -25.360 1.00 11.54 ? 302 JTW B N1  1 
HETATM 4231 O  O13 . JTW G 4 .   ? 5.895   3.782   -29.753 1.00 16.60 ? 302 JTW B O13 1 
HETATM 4232 N  N14 . JTW G 4 .   ? 5.997   5.197   -27.970 1.00 17.49 ? 302 JTW B N14 1 
HETATM 4233 C  C15 . JTW G 4 .   ? 7.410   5.459   -28.190 1.00 24.06 ? 302 JTW B C15 1 
HETATM 4234 C  C16 . JTW G 4 .   ? 8.197   4.217   -27.756 1.00 28.63 ? 302 JTW B C16 1 
HETATM 4235 O  O17 . JTW G 4 .   ? 8.441   3.316   -28.828 1.00 36.91 ? 302 JTW B O17 1 
HETATM 4236 O  O   . HOH H 5 .   ? 9.001   -9.832  25.486  1.00 17.54 ? 401 HOH A O   1 
HETATM 4237 O  O   . HOH H 5 .   ? 14.193  -7.045  23.140  1.00 15.17 ? 402 HOH A O   1 
HETATM 4238 O  O   . HOH H 5 .   ? 3.294   -11.449 20.079  1.00 30.79 ? 403 HOH A O   1 
HETATM 4239 O  O   . HOH H 5 .   ? -11.054 13.518  7.243   1.00 12.84 ? 404 HOH A O   1 
HETATM 4240 O  O   . HOH H 5 .   ? 16.345  15.894  -3.713  1.00 25.81 ? 405 HOH A O   1 
HETATM 4241 O  O   . HOH H 5 .   ? 25.137  -1.171  14.097  1.00 25.24 ? 406 HOH A O   1 
HETATM 4242 O  O   . HOH H 5 .   ? 26.154  -8.622  13.018  1.00 30.48 ? 407 HOH A O   1 
HETATM 4243 O  O   . HOH H 5 .   ? -3.620  -4.842  3.708   1.00 10.06 ? 408 HOH A O   1 
HETATM 4244 O  O   . HOH H 5 .   ? 5.460   4.554   0.439   1.00 7.25  ? 409 HOH A O   1 
HETATM 4245 O  O   . HOH H 5 .   ? 7.094   2.105   -9.600  1.00 10.06 ? 410 HOH A O   1 
HETATM 4246 O  O   . HOH H 5 .   ? 5.392   11.928  10.757  1.00 17.43 ? 411 HOH A O   1 
HETATM 4247 O  O   . HOH H 5 .   ? -12.084 0.210   11.798  1.00 14.95 ? 412 HOH A O   1 
HETATM 4248 O  O   . HOH H 5 .   ? -9.531  9.667   16.863  1.00 15.93 ? 413 HOH A O   1 
HETATM 4249 O  O   . HOH H 5 .   ? 3.209   6.373   4.078   1.00 11.14 ? 414 HOH A O   1 
HETATM 4250 O  O   . HOH H 5 .   ? 11.205  -13.690 1.679   1.00 14.83 ? 415 HOH A O   1 
HETATM 4251 O  O   . HOH H 5 .   ? -1.880  -7.157  23.210  1.00 18.70 ? 416 HOH A O   1 
HETATM 4252 O  O   . HOH H 5 .   ? 23.034  -5.365  25.869  1.00 19.02 ? 417 HOH A O   1 
HETATM 4253 O  O   . HOH H 5 .   ? 3.074   16.956  18.300  1.00 20.17 ? 418 HOH A O   1 
HETATM 4254 O  O   . HOH H 5 .   ? 12.949  7.450   -10.053 1.00 13.99 ? 419 HOH A O   1 
HETATM 4255 O  O   . HOH H 5 .   ? 7.444   -12.820 15.667  1.00 18.26 ? 420 HOH A O   1 
HETATM 4256 O  O   . HOH H 5 .   ? -8.614  -7.162  5.140   1.00 14.68 ? 421 HOH A O   1 
HETATM 4257 O  O   . HOH H 5 .   ? 0.419   16.372  -9.296  1.00 21.65 ? 422 HOH A O   1 
HETATM 4258 O  O   . HOH H 5 .   ? 15.992  5.186   -12.744 1.00 27.17 ? 423 HOH A O   1 
HETATM 4259 O  O   . HOH H 5 .   ? 5.218   7.481   8.670   1.00 12.10 ? 424 HOH A O   1 
HETATM 4260 O  O   . HOH H 5 .   ? 29.105  -3.313  14.412  1.00 27.10 ? 425 HOH A O   1 
HETATM 4261 O  O   . HOH H 5 .   ? 8.333   -3.872  28.078  1.00 18.60 ? 426 HOH A O   1 
HETATM 4262 O  O   . HOH H 5 .   ? 21.162  -12.595 -12.747 1.00 21.28 ? 427 HOH A O   1 
HETATM 4263 O  O   . HOH H 5 .   ? -8.244  -11.716 15.809  1.00 14.02 ? 428 HOH A O   1 
HETATM 4264 O  O   . HOH H 5 .   ? 6.035   4.564   -8.142  1.00 9.18  ? 429 HOH A O   1 
HETATM 4265 O  O   . HOH H 5 .   ? 2.907   21.170  -0.526  1.00 26.14 ? 430 HOH A O   1 
HETATM 4266 O  O   . HOH H 5 .   ? 4.917   -2.221  -3.935  1.00 5.50  ? 431 HOH A O   1 
HETATM 4267 O  O   . HOH H 5 .   ? 6.970   20.868  -10.430 1.00 13.75 ? 432 HOH A O   1 
HETATM 4268 O  O   . HOH H 5 .   ? 19.598  -10.371 12.001  1.00 15.87 ? 433 HOH A O   1 
HETATM 4269 O  O   . HOH H 5 .   ? -4.351  13.157  -4.723  1.00 12.89 ? 434 HOH A O   1 
HETATM 4270 O  O   . HOH H 5 .   ? 25.761  6.685   18.432  1.00 20.33 ? 435 HOH A O   1 
HETATM 4271 O  O   . HOH H 5 .   ? 11.115  -11.507 17.655  1.00 26.78 ? 436 HOH A O   1 
HETATM 4272 O  O   . HOH H 5 .   ? -5.959  -7.484  22.169  1.00 23.77 ? 437 HOH A O   1 
HETATM 4273 O  O   . HOH H 5 .   ? 12.650  4.635   -9.624  1.00 11.76 ? 438 HOH A O   1 
HETATM 4274 O  O   . HOH H 5 .   ? 5.261   -10.851 15.827  1.00 23.44 ? 439 HOH A O   1 
HETATM 4275 O  O   . HOH H 5 .   ? -2.006  -15.377 19.475  1.00 25.31 ? 440 HOH A O   1 
HETATM 4276 O  O   . HOH H 5 .   ? 15.302  1.320   25.444  1.00 24.10 ? 441 HOH A O   1 
HETATM 4277 O  O   . HOH H 5 .   ? 22.956  -13.262 9.540   1.00 15.74 ? 442 HOH A O   1 
HETATM 4278 O  O   . HOH H 5 .   ? -3.974  -8.623  -4.934  1.00 28.66 ? 443 HOH A O   1 
HETATM 4279 O  O   . HOH H 5 .   ? -7.915  -7.071  19.143  1.00 29.11 ? 444 HOH A O   1 
HETATM 4280 O  O   . HOH H 5 .   ? 11.761  -3.820  -8.416  1.00 8.89  ? 445 HOH A O   1 
HETATM 4281 O  O   . HOH H 5 .   ? 1.676   -0.867  25.241  1.00 19.09 ? 446 HOH A O   1 
HETATM 4282 O  O   . HOH H 5 .   ? -6.727  17.329  5.643   1.00 21.89 ? 447 HOH A O   1 
HETATM 4283 O  O   . HOH H 5 .   ? 15.016  8.807   18.356  1.00 20.18 ? 448 HOH A O   1 
HETATM 4284 O  O   . HOH H 5 .   ? 10.388  -8.416  -10.717 1.00 26.15 ? 449 HOH A O   1 
HETATM 4285 O  O   . HOH H 5 .   ? -4.796  5.509   23.153  1.00 20.95 ? 450 HOH A O   1 
HETATM 4286 O  O   . HOH H 5 .   ? 0.147   6.273   -5.838  1.00 13.68 ? 451 HOH A O   1 
HETATM 4287 O  O   . HOH H 5 .   ? -6.955  2.831   7.906   1.00 14.21 ? 452 HOH A O   1 
HETATM 4288 O  O   . HOH H 5 .   ? -10.102 18.745  12.169  1.00 34.74 ? 453 HOH A O   1 
HETATM 4289 O  O   . HOH H 5 .   ? 19.554  -11.383 14.186  1.00 14.29 ? 454 HOH A O   1 
HETATM 4290 O  O   . HOH H 5 .   ? -1.067  17.509  15.486  1.00 19.63 ? 455 HOH A O   1 
HETATM 4291 O  O   . HOH H 5 .   ? -6.770  11.053  20.587  1.00 23.36 ? 456 HOH A O   1 
HETATM 4292 O  O   . HOH H 5 .   ? 2.967   3.973   -9.915  1.00 8.23  ? 457 HOH A O   1 
HETATM 4293 O  O   . HOH H 5 .   ? -11.469 -5.652  13.099  1.00 19.63 ? 458 HOH A O   1 
HETATM 4294 O  O   . HOH H 5 .   ? -2.100  22.087  0.034   1.00 21.43 ? 459 HOH A O   1 
HETATM 4295 O  O   . HOH H 5 .   ? -13.528 -11.705 15.596  1.00 32.96 ? 460 HOH A O   1 
HETATM 4296 O  O   . HOH H 5 .   ? 22.082  -2.658  -3.211  1.00 12.42 ? 461 HOH A O   1 
HETATM 4297 O  O   . HOH H 5 .   ? 6.993   10.704  -8.983  1.00 7.32  ? 462 HOH A O   1 
HETATM 4298 O  O   . HOH H 5 .   ? -13.167 3.992   10.650  1.00 20.26 ? 463 HOH A O   1 
HETATM 4299 O  O   . HOH H 5 .   ? 16.366  7.287   24.769  1.00 34.25 ? 464 HOH A O   1 
HETATM 4300 O  O   . HOH H 5 .   ? 29.700  -14.644 8.419   1.00 41.31 ? 465 HOH A O   1 
HETATM 4301 O  O   . HOH H 5 .   ? 3.186   -7.306  -8.388  1.00 24.86 ? 466 HOH A O   1 
HETATM 4302 O  O   . HOH H 5 .   ? 7.176   7.269   -7.201  1.00 12.54 ? 467 HOH A O   1 
HETATM 4303 O  O   . HOH H 5 .   ? 18.739  -1.784  7.665   1.00 8.12  ? 468 HOH A O   1 
HETATM 4304 O  O   . HOH H 5 .   ? -7.983  0.646   18.020  1.00 22.73 ? 469 HOH A O   1 
HETATM 4305 O  O   . HOH H 5 .   ? -2.027  -5.207  -4.065  1.00 19.77 ? 470 HOH A O   1 
HETATM 4306 O  O   . HOH H 5 .   ? 9.798   -10.053 7.102   1.00 7.47  ? 471 HOH A O   1 
HETATM 4307 O  O   . HOH H 5 .   ? -6.888  -4.747  16.589  1.00 24.82 ? 472 HOH A O   1 
HETATM 4308 O  O   . HOH H 5 .   ? 24.301  -6.849  8.706   1.00 13.36 ? 473 HOH A O   1 
HETATM 4309 O  O   . HOH H 5 .   ? 10.666  18.611  -9.192  1.00 33.05 ? 474 HOH A O   1 
HETATM 4310 O  O   . HOH H 5 .   ? 16.548  -5.148  23.141  1.00 14.72 ? 475 HOH A O   1 
HETATM 4311 O  O   . HOH H 5 .   ? 25.806  -10.144 22.342  1.00 28.34 ? 476 HOH A O   1 
HETATM 4312 O  O   . HOH H 5 .   ? -0.637  -0.595  24.340  1.00 17.01 ? 477 HOH A O   1 
HETATM 4313 O  O   . HOH H 5 .   ? 9.186   8.071   26.689  1.00 26.46 ? 478 HOH A O   1 
HETATM 4314 O  O   . HOH H 5 .   ? 14.879  3.128   -8.862  1.00 11.64 ? 479 HOH A O   1 
HETATM 4315 O  O   . HOH H 5 .   ? 13.115  15.074  -2.958  1.00 4.07  ? 480 HOH A O   1 
HETATM 4316 O  O   . HOH H 5 .   ? 26.583  -0.233  20.140  1.00 29.31 ? 481 HOH A O   1 
HETATM 4317 O  O   . HOH H 5 .   ? 17.028  9.591   -5.801  1.00 9.62  ? 482 HOH A O   1 
HETATM 4318 O  O   . HOH H 5 .   ? -2.278  13.788  4.330   1.00 19.89 ? 483 HOH A O   1 
HETATM 4319 O  O   . HOH H 5 .   ? 15.132  14.918  3.935   1.00 33.58 ? 484 HOH A O   1 
HETATM 4320 O  O   . HOH H 5 .   ? 24.888  -15.779 -4.778  1.00 28.53 ? 485 HOH A O   1 
HETATM 4321 O  O   . HOH H 5 .   ? 17.054  -0.700  -13.879 1.00 22.56 ? 486 HOH A O   1 
HETATM 4322 O  O   . HOH H 5 .   ? -3.436  8.231   -0.222  1.00 26.43 ? 487 HOH A O   1 
HETATM 4323 O  O   . HOH H 5 .   ? -9.526  3.530   6.350   1.00 17.41 ? 488 HOH A O   1 
HETATM 4324 O  O   . HOH H 5 .   ? -3.328  6.372   1.647   1.00 28.40 ? 489 HOH A O   1 
HETATM 4325 O  O   . HOH H 5 .   ? 25.628  -14.818 5.936   1.00 26.66 ? 490 HOH A O   1 
HETATM 4326 O  O   . HOH H 5 .   ? 28.370  4.274   19.471  1.00 35.08 ? 491 HOH A O   1 
HETATM 4327 O  O   . HOH H 5 .   ? 11.417  3.001   -11.277 1.00 12.26 ? 492 HOH A O   1 
HETATM 4328 O  O   . HOH H 5 .   ? -8.973  24.054  9.826   1.00 22.55 ? 493 HOH A O   1 
HETATM 4329 O  O   . HOH H 5 .   ? -12.444 3.498   6.728   1.00 24.51 ? 494 HOH A O   1 
HETATM 4330 O  O   . HOH H 5 .   ? 3.812   -14.082 13.728  1.00 16.89 ? 495 HOH A O   1 
HETATM 4331 O  O   . HOH H 5 .   ? -4.010  -10.958 2.723   1.00 19.78 ? 496 HOH A O   1 
HETATM 4332 O  O   . HOH H 5 .   ? -9.691  18.679  0.591   1.00 30.48 ? 497 HOH A O   1 
HETATM 4333 O  O   . HOH H 5 .   ? 3.113   4.070   30.758  1.00 35.56 ? 498 HOH A O   1 
HETATM 4334 O  O   . HOH H 5 .   ? -1.748  -12.230 3.828   1.00 12.76 ? 499 HOH A O   1 
HETATM 4335 O  O   . HOH H 5 .   ? -7.645  16.033  12.919  1.00 17.35 ? 500 HOH A O   1 
HETATM 4336 O  O   . HOH H 5 .   ? 27.560  -5.062  -0.033  1.00 26.33 ? 501 HOH A O   1 
HETATM 4337 O  O   . HOH H 5 .   ? 29.715  -14.841 0.026   1.00 34.37 ? 502 HOH A O   1 
HETATM 4338 O  O   . HOH H 5 .   ? 6.084   -6.374  25.570  1.00 22.97 ? 503 HOH A O   1 
HETATM 4339 O  O   . HOH H 5 .   ? 22.325  4.793   0.955   1.00 35.00 ? 504 HOH A O   1 
HETATM 4340 O  O   . HOH H 5 .   ? 18.420  -4.188  25.720  1.00 27.20 ? 505 HOH A O   1 
HETATM 4341 O  O   . HOH H 5 .   ? 0.214   8.732   -9.528  1.00 15.16 ? 506 HOH A O   1 
HETATM 4342 O  O   . HOH H 5 .   ? 1.420   -15.946 -7.946  1.00 40.32 ? 507 HOH A O   1 
HETATM 4343 O  O   . HOH H 5 .   ? 12.441  2.195   28.036  1.00 28.52 ? 508 HOH A O   1 
HETATM 4344 O  O   . HOH H 5 .   ? -4.671  -2.073  -4.284  1.00 41.32 ? 509 HOH A O   1 
HETATM 4345 O  O   . HOH H 5 .   ? 3.612   6.264   32.273  1.00 21.91 ? 510 HOH A O   1 
HETATM 4346 O  O   . HOH H 5 .   ? -4.861  14.315  19.161  1.00 22.13 ? 511 HOH A O   1 
HETATM 4347 O  O   . HOH H 5 .   ? 0.421   -9.650  -5.079  1.00 15.22 ? 512 HOH A O   1 
HETATM 4348 O  O   . HOH H 5 .   ? 14.729  -2.889  -13.216 1.00 14.18 ? 513 HOH A O   1 
HETATM 4349 O  O   . HOH H 5 .   ? 29.953  -8.524  10.141  1.00 27.89 ? 514 HOH A O   1 
HETATM 4350 O  O   . HOH H 5 .   ? 13.649  -13.404 8.952   1.00 15.23 ? 515 HOH A O   1 
HETATM 4351 O  O   . HOH H 5 .   ? 1.813   -2.993  26.840  1.00 41.48 ? 516 HOH A O   1 
HETATM 4352 O  O   . HOH H 5 .   ? 18.972  -9.123  19.715  1.00 17.97 ? 517 HOH A O   1 
HETATM 4353 O  O   . HOH H 5 .   ? 28.468  -11.197 -2.365  1.00 31.13 ? 518 HOH A O   1 
HETATM 4354 O  O   . HOH H 5 .   ? 5.860   -5.980  -7.431  1.00 19.80 ? 519 HOH A O   1 
HETATM 4355 O  O   . HOH H 5 .   ? -1.641  7.403   3.285   1.00 18.57 ? 520 HOH A O   1 
HETATM 4356 O  O   . HOH H 5 .   ? 20.229  -5.305  -11.576 1.00 25.25 ? 521 HOH A O   1 
HETATM 4357 O  O   . HOH H 5 .   ? 17.895  -15.735 13.783  1.00 25.12 ? 522 HOH A O   1 
HETATM 4358 O  O   . HOH H 5 .   ? -6.280  4.073   -2.895  1.00 21.00 ? 523 HOH A O   1 
HETATM 4359 O  O   . HOH H 5 .   ? -7.711  7.370   -0.430  1.00 38.57 ? 524 HOH A O   1 
HETATM 4360 O  O   . HOH H 5 .   ? 15.900  16.027  1.925   1.00 39.40 ? 525 HOH A O   1 
HETATM 4361 O  O   . HOH H 5 .   ? 4.561   -3.114  -6.575  1.00 14.94 ? 526 HOH A O   1 
HETATM 4362 O  O   . HOH H 5 .   ? 7.448   9.843   22.263  1.00 18.37 ? 527 HOH A O   1 
HETATM 4363 O  O   . HOH H 5 .   ? 4.779   -16.798 9.627   1.00 33.88 ? 528 HOH A O   1 
HETATM 4364 O  O   . HOH H 5 .   ? -9.018  0.609   -3.230  1.00 34.21 ? 529 HOH A O   1 
HETATM 4365 O  O   . HOH H 5 .   ? 22.849  11.633  17.603  1.00 34.49 ? 530 HOH A O   1 
HETATM 4366 O  O   . HOH H 5 .   ? -9.382  23.301  12.994  1.00 35.13 ? 531 HOH A O   1 
HETATM 4367 O  O   . HOH H 5 .   ? 4.032   13.866  12.700  1.00 30.58 ? 532 HOH A O   1 
HETATM 4368 O  O   . HOH H 5 .   ? 19.181  -11.177 17.543  1.00 38.12 ? 533 HOH A O   1 
HETATM 4369 O  O   . HOH H 5 .   ? 25.582  -4.019  4.181   1.00 18.96 ? 534 HOH A O   1 
HETATM 4370 O  O   . HOH H 5 .   ? -11.386 0.977   4.185   1.00 32.81 ? 535 HOH A O   1 
HETATM 4371 O  O   . HOH H 5 .   ? -12.121 7.658   0.788   1.00 31.80 ? 536 HOH A O   1 
HETATM 4372 O  O   . HOH H 5 .   ? -5.223  6.001   -1.362  1.00 30.31 ? 537 HOH A O   1 
HETATM 4373 O  O   . HOH H 5 .   ? -1.792  9.863   2.001   1.00 32.10 ? 538 HOH A O   1 
HETATM 4374 O  O   . HOH H 5 .   ? 18.076  11.798  -6.037  1.00 18.47 ? 539 HOH A O   1 
HETATM 4375 O  O   . HOH H 5 .   ? -5.533  11.931  -11.047 1.00 26.37 ? 540 HOH A O   1 
HETATM 4376 O  O   . HOH H 5 .   ? 24.704  -3.076  -5.621  1.00 22.18 ? 541 HOH A O   1 
HETATM 4377 O  O   . HOH H 5 .   ? 22.992  3.722   -10.918 1.00 43.86 ? 542 HOH A O   1 
HETATM 4378 O  O   . HOH H 5 .   ? 0.162   16.281  2.795   1.00 36.62 ? 543 HOH A O   1 
HETATM 4379 O  O   . HOH H 5 .   ? -9.641  2.779   21.131  1.00 35.37 ? 544 HOH A O   1 
HETATM 4380 O  O   . HOH H 5 .   ? 6.084   -14.957 -2.297  1.00 35.14 ? 545 HOH A O   1 
HETATM 4381 O  O   . HOH H 5 .   ? 29.381  -3.009  19.431  1.00 41.40 ? 546 HOH A O   1 
HETATM 4382 O  O   . HOH H 5 .   ? 26.296  9.045   19.686  1.00 33.46 ? 547 HOH A O   1 
HETATM 4383 O  O   . HOH H 5 .   ? 8.710   -2.198  32.745  1.00 31.24 ? 548 HOH A O   1 
HETATM 4384 O  O   . HOH H 5 .   ? -2.840  -4.486  23.557  1.00 27.92 ? 549 HOH A O   1 
HETATM 4385 O  O   . HOH H 5 .   ? 8.204   -22.375 10.436  1.00 29.97 ? 550 HOH A O   1 
HETATM 4386 O  O   . HOH H 5 .   ? 11.626  -11.345 22.165  1.00 40.90 ? 551 HOH A O   1 
HETATM 4387 O  O   . HOH H 5 .   ? -1.841  17.815  11.186  1.00 22.07 ? 552 HOH A O   1 
HETATM 4388 O  O   . HOH H 5 .   ? -0.110  18.257  18.275  1.00 33.80 ? 553 HOH A O   1 
HETATM 4389 O  O   . HOH H 5 .   ? 25.958  6.308   21.394  1.00 29.01 ? 554 HOH A O   1 
HETATM 4390 O  O   . HOH H 5 .   ? -1.555  7.316   -7.939  1.00 25.15 ? 555 HOH A O   1 
HETATM 4391 O  O   . HOH H 5 .   ? -13.423 -0.940  0.878   1.00 33.12 ? 556 HOH A O   1 
HETATM 4392 O  O   . HOH H 5 .   ? 16.021  11.810  15.831  1.00 30.92 ? 557 HOH A O   1 
HETATM 4393 O  O   . HOH H 5 .   ? -10.623 2.820   25.274  1.00 40.42 ? 558 HOH A O   1 
HETATM 4394 O  O   . HOH H 5 .   ? -5.743  -12.767 1.962   1.00 29.90 ? 559 HOH A O   1 
HETATM 4395 O  O   . HOH H 5 .   ? 22.312  8.723   20.659  1.00 31.93 ? 560 HOH A O   1 
HETATM 4396 O  O   . HOH H 5 .   ? 1.837   18.174  3.589   1.00 32.74 ? 561 HOH A O   1 
HETATM 4397 O  O   . HOH H 5 .   ? 14.287  16.844  -1.683  1.00 26.30 ? 562 HOH A O   1 
HETATM 4398 O  O   . HOH H 5 .   ? 20.898  4.225   -14.223 1.00 35.99 ? 563 HOH A O   1 
HETATM 4399 O  O   . HOH H 5 .   ? -5.259  18.878  16.078  1.00 22.91 ? 564 HOH A O   1 
HETATM 4400 O  O   . HOH H 5 .   ? 5.095   14.236  6.936   1.00 38.09 ? 565 HOH A O   1 
HETATM 4401 O  O   . HOH H 5 .   ? -4.051  -8.651  23.433  1.00 29.08 ? 566 HOH A O   1 
HETATM 4402 O  O   . HOH H 5 .   ? 14.436  17.699  0.706   1.00 33.19 ? 567 HOH A O   1 
HETATM 4403 O  O   . HOH I 5 .   ? 6.781   1.847   -21.492 1.00 15.26 ? 401 HOH B O   1 
HETATM 4404 O  O   . HOH I 5 .   ? -1.207  -3.474  -11.259 1.00 7.24  ? 402 HOH B O   1 
HETATM 4405 O  O   . HOH I 5 .   ? 19.920  0.693   -41.453 1.00 30.98 ? 403 HOH B O   1 
HETATM 4406 O  O   . HOH I 5 .   ? -2.479  -12.879 -41.830 1.00 33.64 ? 404 HOH B O   1 
HETATM 4407 O  O   . HOH I 5 .   ? 25.320  6.659   -28.565 1.00 15.98 ? 405 HOH B O   1 
HETATM 4408 O  O   . HOH I 5 .   ? -4.406  1.699   -13.982 1.00 22.62 ? 406 HOH B O   1 
HETATM 4409 O  O   . HOH I 5 .   ? 12.634  -23.267 -33.361 1.00 37.50 ? 407 HOH B O   1 
HETATM 4410 O  O   . HOH I 5 .   ? 18.768  -12.743 -21.688 1.00 9.86  ? 408 HOH B O   1 
HETATM 4411 O  O   . HOH I 5 .   ? -7.204  14.542  -31.212 1.00 31.20 ? 409 HOH B O   1 
HETATM 4412 O  O   . HOH I 5 .   ? 0.658   -16.886 -35.548 1.00 22.66 ? 410 HOH B O   1 
HETATM 4413 O  O   . HOH I 5 .   ? 16.034  -14.806 -39.604 1.00 32.51 ? 411 HOH B O   1 
HETATM 4414 O  O   . HOH I 5 .   ? -2.766  14.900  -20.579 1.00 26.63 ? 412 HOH B O   1 
HETATM 4415 O  O   . HOH I 5 .   ? -0.536  11.412  -9.779  1.00 16.66 ? 413 HOH B O   1 
HETATM 4416 O  O   . HOH I 5 .   ? 9.083   -11.838 -45.785 1.00 34.05 ? 414 HOH B O   1 
HETATM 4417 O  O   . HOH I 5 .   ? -1.175  11.978  -27.190 1.00 23.09 ? 415 HOH B O   1 
HETATM 4418 O  O   . HOH I 5 .   ? -12.940 9.408   -29.794 1.00 27.32 ? 416 HOH B O   1 
HETATM 4419 O  O   . HOH I 5 .   ? 20.264  -8.231  -35.966 1.00 28.39 ? 417 HOH B O   1 
HETATM 4420 O  O   . HOH I 5 .   ? 10.976  -9.156  -54.621 1.00 35.34 ? 418 HOH B O   1 
HETATM 4421 O  O   . HOH I 5 .   ? 10.926  -10.135 -43.832 1.00 15.69 ? 419 HOH B O   1 
HETATM 4422 O  O   . HOH I 5 .   ? -7.850  -0.718  -42.388 1.00 30.18 ? 420 HOH B O   1 
HETATM 4423 O  O   . HOH I 5 .   ? 3.208   -7.222  -11.046 1.00 21.46 ? 421 HOH B O   1 
HETATM 4424 O  O   . HOH I 5 .   ? 20.424  -13.441 -19.633 1.00 20.42 ? 422 HOH B O   1 
HETATM 4425 O  O   . HOH I 5 .   ? 11.964  4.468   -15.615 1.00 10.80 ? 423 HOH B O   1 
HETATM 4426 O  O   . HOH I 5 .   ? 14.332  -8.864  -21.223 1.00 10.73 ? 424 HOH B O   1 
HETATM 4427 O  O   . HOH I 5 .   ? 5.464   -14.552 -43.944 1.00 28.30 ? 425 HOH B O   1 
HETATM 4428 O  O   . HOH I 5 .   ? 15.648  5.234   -21.245 1.00 31.23 ? 426 HOH B O   1 
HETATM 4429 O  O   . HOH I 5 .   ? 5.920   3.841   -13.139 1.00 12.85 ? 427 HOH B O   1 
HETATM 4430 O  O   . HOH I 5 .   ? -5.189  12.140  -18.240 1.00 21.46 ? 428 HOH B O   1 
HETATM 4431 O  O   . HOH I 5 .   ? 17.244  10.498  -17.556 1.00 29.35 ? 429 HOH B O   1 
HETATM 4432 O  O   . HOH I 5 .   ? 2.389   3.749   -40.115 1.00 21.43 ? 430 HOH B O   1 
HETATM 4433 O  O   . HOH I 5 .   ? -12.865 -8.213  -28.649 1.00 15.54 ? 431 HOH B O   1 
HETATM 4434 O  O   . HOH I 5 .   ? -8.808  -14.366 -36.053 1.00 24.13 ? 432 HOH B O   1 
HETATM 4435 O  O   . HOH I 5 .   ? 10.079  -14.108 -17.293 1.00 14.96 ? 433 HOH B O   1 
HETATM 4436 O  O   . HOH I 5 .   ? 13.095  -16.088 -40.540 1.00 28.14 ? 434 HOH B O   1 
HETATM 4437 O  O   . HOH I 5 .   ? 12.603  15.627  -14.940 1.00 19.10 ? 435 HOH B O   1 
HETATM 4438 O  O   . HOH I 5 .   ? 6.122   -3.708  -15.706 1.00 7.41  ? 436 HOH B O   1 
HETATM 4439 O  O   . HOH I 5 .   ? 9.525   2.516   -25.333 1.00 16.32 ? 437 HOH B O   1 
HETATM 4440 O  O   . HOH I 5 .   ? -12.525 -3.511  -34.992 1.00 12.78 ? 438 HOH B O   1 
HETATM 4441 O  O   . HOH I 5 .   ? -4.270  -21.058 -32.394 1.00 29.01 ? 439 HOH B O   1 
HETATM 4442 O  O   . HOH I 5 .   ? -3.548  -1.835  -7.640  1.00 26.80 ? 440 HOH B O   1 
HETATM 4443 O  O   . HOH I 5 .   ? -4.323  16.247  -25.203 1.00 26.72 ? 441 HOH B O   1 
HETATM 4444 O  O   . HOH I 5 .   ? 5.270   -16.395 -33.189 1.00 14.67 ? 442 HOH B O   1 
HETATM 4445 O  O   . HOH I 5 .   ? 21.243  10.787  -28.374 1.00 18.11 ? 443 HOH B O   1 
HETATM 4446 O  O   . HOH I 5 .   ? 0.777   -13.006 -25.253 1.00 7.12  ? 444 HOH B O   1 
HETATM 4447 O  O   . HOH I 5 .   ? 4.160   20.060  -20.615 1.00 23.47 ? 445 HOH B O   1 
HETATM 4448 O  O   . HOH I 5 .   ? 4.467   2.094   -11.169 1.00 5.28  ? 446 HOH B O   1 
HETATM 4449 O  O   . HOH I 5 .   ? 3.720   -12.457 -46.935 1.00 28.54 ? 447 HOH B O   1 
HETATM 4450 O  O   . HOH I 5 .   ? 7.267   1.514   -43.682 1.00 17.46 ? 448 HOH B O   1 
HETATM 4451 O  O   . HOH I 5 .   ? 13.199  -9.855  -42.630 1.00 17.32 ? 449 HOH B O   1 
HETATM 4452 O  O   . HOH I 5 .   ? -11.954 3.056   -40.694 1.00 8.13  ? 450 HOH B O   1 
HETATM 4453 O  O   . HOH I 5 .   ? -3.762  -5.125  -11.180 1.00 29.76 ? 451 HOH B O   1 
HETATM 4454 O  O   . HOH I 5 .   ? 5.383   6.584   -14.683 1.00 14.01 ? 452 HOH B O   1 
HETATM 4455 O  O   . HOH I 5 .   ? -8.801  -13.054 -30.917 1.00 20.61 ? 453 HOH B O   1 
HETATM 4456 O  O   . HOH I 5 .   ? 8.964   6.947   -33.316 1.00 23.13 ? 454 HOH B O   1 
HETATM 4457 O  O   . HOH I 5 .   ? 18.950  -3.509  -27.193 1.00 12.18 ? 455 HOH B O   1 
HETATM 4458 O  O   . HOH I 5 .   ? -8.576  -14.658 -32.621 1.00 20.26 ? 456 HOH B O   1 
HETATM 4459 O  O   . HOH I 5 .   ? 6.078   6.117   -11.969 1.00 35.20 ? 457 HOH B O   1 
HETATM 4460 O  O   . HOH I 5 .   ? 8.872   15.116  -17.558 1.00 18.25 ? 458 HOH B O   1 
HETATM 4461 O  O   . HOH I 5 .   ? 21.440  -2.754  -25.441 1.00 14.43 ? 459 HOH B O   1 
HETATM 4462 O  O   . HOH I 5 .   ? -1.449  -15.396 -19.354 1.00 15.30 ? 460 HOH B O   1 
HETATM 4463 O  O   . HOH I 5 .   ? -1.643  -17.679 -34.029 1.00 31.11 ? 461 HOH B O   1 
HETATM 4464 O  O   . HOH I 5 .   ? 15.950  -5.160  -13.705 1.00 26.47 ? 462 HOH B O   1 
HETATM 4465 O  O   . HOH I 5 .   ? -15.270 -4.444  -35.906 1.00 24.89 ? 463 HOH B O   1 
HETATM 4466 O  O   . HOH I 5 .   ? 22.455  7.834   -34.891 1.00 21.76 ? 464 HOH B O   1 
HETATM 4467 O  O   . HOH I 5 .   ? 8.807   3.656   -11.197 1.00 10.70 ? 465 HOH B O   1 
HETATM 4468 O  O   . HOH I 5 .   ? 18.936  -19.103 -31.580 1.00 34.32 ? 466 HOH B O   1 
HETATM 4469 O  O   . HOH I 5 .   ? 11.651  -16.504 -20.563 1.00 12.36 ? 467 HOH B O   1 
HETATM 4470 O  O   . HOH I 5 .   ? -4.541  -10.774 -42.390 1.00 15.11 ? 468 HOH B O   1 
HETATM 4471 O  O   . HOH I 5 .   ? 12.052  -7.863  -14.005 1.00 27.85 ? 469 HOH B O   1 
HETATM 4472 O  O   . HOH I 5 .   ? 2.351   -16.106 -13.426 1.00 16.87 ? 470 HOH B O   1 
HETATM 4473 O  O   . HOH I 5 .   ? 0.317   13.797  -20.810 1.00 10.57 ? 471 HOH B O   1 
HETATM 4474 O  O   . HOH I 5 .   ? -6.812  -3.920  -28.382 1.00 6.25  ? 472 HOH B O   1 
HETATM 4475 O  O   . HOH I 5 .   ? -1.019  7.997   -11.972 1.00 12.31 ? 473 HOH B O   1 
HETATM 4476 O  O   . HOH I 5 .   ? -0.084  -10.370 -7.809  1.00 38.40 ? 474 HOH B O   1 
HETATM 4477 O  O   . HOH I 5 .   ? 5.493   10.283  -13.735 1.00 9.34  ? 475 HOH B O   1 
HETATM 4478 O  O   . HOH I 5 .   ? -0.742  5.077   -11.894 1.00 11.78 ? 476 HOH B O   1 
HETATM 4479 O  O   . HOH I 5 .   ? -0.932  6.513   -37.740 1.00 20.92 ? 477 HOH B O   1 
HETATM 4480 O  O   . HOH I 5 .   ? -9.652  0.143   -16.489 1.00 37.16 ? 478 HOH B O   1 
HETATM 4481 O  O   . HOH I 5 .   ? 6.170   -19.360 -30.022 1.00 16.62 ? 479 HOH B O   1 
HETATM 4482 O  O   . HOH I 5 .   ? -7.752  4.913   -12.666 1.00 24.06 ? 480 HOH B O   1 
HETATM 4483 O  O   . HOH I 5 .   ? -3.331  -13.155 -47.489 1.00 32.01 ? 481 HOH B O   1 
HETATM 4484 O  O   . HOH I 5 .   ? -0.302  3.454   -43.734 1.00 31.31 ? 482 HOH B O   1 
HETATM 4485 O  O   . HOH I 5 .   ? -3.815  5.200   -13.050 1.00 37.92 ? 483 HOH B O   1 
HETATM 4486 O  O   . HOH I 5 .   ? 18.128  0.734   -16.676 1.00 20.52 ? 484 HOH B O   1 
HETATM 4487 O  O   . HOH I 5 .   ? 12.012  7.707   -12.708 1.00 24.13 ? 485 HOH B O   1 
HETATM 4488 O  O   . HOH I 5 .   ? 16.914  -20.978 -26.316 1.00 27.27 ? 486 HOH B O   1 
HETATM 4489 O  O   . HOH I 5 .   ? 2.126   -17.148 -42.683 1.00 31.00 ? 487 HOH B O   1 
HETATM 4490 O  O   . HOH I 5 .   ? 1.927   -19.361 -28.711 1.00 17.25 ? 488 HOH B O   1 
HETATM 4491 O  O   . HOH I 5 .   ? -4.348  9.683   -17.339 1.00 7.20  ? 489 HOH B O   1 
HETATM 4492 O  O   . HOH I 5 .   ? -12.251 12.242  -26.598 1.00 28.33 ? 490 HOH B O   1 
HETATM 4493 O  O   . HOH I 5 .   ? -7.352  -26.674 -29.342 1.00 22.90 ? 491 HOH B O   1 
HETATM 4494 O  O   . HOH I 5 .   ? 18.542  -13.143 -33.749 1.00 21.70 ? 492 HOH B O   1 
HETATM 4495 O  O   . HOH I 5 .   ? 13.505  14.141  -10.976 1.00 29.51 ? 493 HOH B O   1 
HETATM 4496 O  O   . HOH I 5 .   ? -12.735 -14.899 -28.177 1.00 17.65 ? 494 HOH B O   1 
HETATM 4497 O  O   . HOH I 5 .   ? 15.287  -23.778 -30.675 1.00 28.89 ? 495 HOH B O   1 
HETATM 4498 O  O   . HOH I 5 .   ? 23.178  -0.106  -37.201 1.00 22.78 ? 496 HOH B O   1 
HETATM 4499 O  O   . HOH I 5 .   ? -13.056 -20.561 -21.677 1.00 26.35 ? 497 HOH B O   1 
HETATM 4500 O  O   . HOH I 5 .   ? 13.728  -14.847 -19.415 1.00 16.84 ? 498 HOH B O   1 
HETATM 4501 O  O   . HOH I 5 .   ? -0.382  3.515   -40.586 1.00 19.09 ? 499 HOH B O   1 
HETATM 4502 O  O   . HOH I 5 .   ? -6.707  -10.363 -44.658 1.00 30.74 ? 500 HOH B O   1 
HETATM 4503 O  O   . HOH I 5 .   ? 22.713  10.732  -23.339 1.00 35.66 ? 501 HOH B O   1 
HETATM 4504 O  O   . HOH I 5 .   ? 4.026   -21.331 -21.940 1.00 19.92 ? 502 HOH B O   1 
HETATM 4505 O  O   . HOH I 5 .   ? 23.729  -11.587 -14.070 1.00 32.94 ? 503 HOH B O   1 
HETATM 4506 O  O   . HOH I 5 .   ? 6.588   -3.653  -12.615 1.00 16.30 ? 504 HOH B O   1 
HETATM 4507 O  O   . HOH I 5 .   ? 6.019   8.101   -27.167 1.00 43.41 ? 505 HOH B O   1 
HETATM 4508 O  O   . HOH I 5 .   ? -1.150  -7.036  -7.812  1.00 27.79 ? 506 HOH B O   1 
HETATM 4509 O  O   . HOH I 5 .   ? 0.407   3.534   -9.984  1.00 14.61 ? 507 HOH B O   1 
HETATM 4510 O  O   . HOH I 5 .   ? 10.716  12.817  -17.919 1.00 21.45 ? 508 HOH B O   1 
HETATM 4511 O  O   . HOH I 5 .   ? 7.860   -17.459 -19.037 1.00 12.89 ? 509 HOH B O   1 
HETATM 4512 O  O   . HOH I 5 .   ? -3.305  -16.379 -26.706 1.00 13.70 ? 510 HOH B O   1 
HETATM 4513 O  O   . HOH I 5 .   ? 10.265  -4.445  -10.749 1.00 24.34 ? 511 HOH B O   1 
HETATM 4514 O  O   . HOH I 5 .   ? 17.395  -0.205  -45.454 1.00 27.88 ? 512 HOH B O   1 
HETATM 4515 O  O   . HOH I 5 .   ? 22.717  -4.088  -15.430 1.00 25.07 ? 513 HOH B O   1 
HETATM 4516 O  O   . HOH I 5 .   ? -11.596 -1.898  -18.380 1.00 14.84 ? 514 HOH B O   1 
HETATM 4517 O  O   . HOH I 5 .   ? 9.436   -20.594 -31.182 1.00 24.83 ? 515 HOH B O   1 
HETATM 4518 O  O   . HOH I 5 .   ? 1.191   -15.071 -49.088 1.00 29.75 ? 516 HOH B O   1 
HETATM 4519 O  O   . HOH I 5 .   ? 20.496  -2.226  -15.984 1.00 27.12 ? 517 HOH B O   1 
HETATM 4520 O  O   . HOH I 5 .   ? -7.590  2.773   -42.580 1.00 37.91 ? 518 HOH B O   1 
HETATM 4521 O  O   . HOH I 5 .   ? 12.514  7.210   -44.280 1.00 27.52 ? 519 HOH B O   1 
HETATM 4522 O  O   . HOH I 5 .   ? 18.636  -4.380  -44.265 1.00 42.70 ? 520 HOH B O   1 
HETATM 4523 O  O   . HOH I 5 .   ? -6.019  12.510  -23.037 1.00 19.90 ? 521 HOH B O   1 
HETATM 4524 O  O   . HOH I 5 .   ? 9.110   -22.635 -22.818 1.00 42.58 ? 522 HOH B O   1 
HETATM 4525 O  O   . HOH I 5 .   ? 9.278   -15.363 -19.537 1.00 13.49 ? 523 HOH B O   1 
HETATM 4526 O  O   . HOH I 5 .   ? -4.944  -17.708 -16.548 1.00 30.10 ? 524 HOH B O   1 
HETATM 4527 O  O   . HOH I 5 .   ? 24.747  10.691  -34.877 1.00 32.16 ? 525 HOH B O   1 
HETATM 4528 O  O   . HOH I 5 .   ? 0.543   9.063   -36.218 1.00 30.46 ? 526 HOH B O   1 
HETATM 4529 O  O   . HOH I 5 .   ? -3.878  -10.518 -45.167 1.00 24.64 ? 527 HOH B O   1 
HETATM 4530 O  O   . HOH I 5 .   ? 15.415  -4.966  -47.345 1.00 34.35 ? 528 HOH B O   1 
HETATM 4531 O  O   . HOH I 5 .   ? 3.384   -18.251 -32.306 1.00 24.64 ? 529 HOH B O   1 
HETATM 4532 O  O   . HOH I 5 .   ? -6.879  17.482  -29.652 1.00 29.98 ? 530 HOH B O   1 
HETATM 4533 O  O   . HOH I 5 .   ? 6.851   -18.883 -35.635 1.00 36.19 ? 531 HOH B O   1 
HETATM 4534 O  O   . HOH I 5 .   ? 18.438  -4.939  -13.502 1.00 19.74 ? 532 HOH B O   1 
HETATM 4535 O  O   . HOH I 5 .   ? -7.616  -18.847 -31.729 1.00 23.02 ? 533 HOH B O   1 
HETATM 4536 O  O   . HOH I 5 .   ? -5.461  -18.667 -33.118 1.00 22.85 ? 534 HOH B O   1 
HETATM 4537 O  O   . HOH I 5 .   ? 8.651   -20.319 -33.566 1.00 28.33 ? 535 HOH B O   1 
HETATM 4538 O  O   . HOH I 5 .   ? 27.012  7.467   -20.547 1.00 37.90 ? 536 HOH B O   1 
HETATM 4539 O  O   . HOH I 5 .   ? 11.478  -3.303  -53.265 1.00 34.98 ? 537 HOH B O   1 
HETATM 4540 O  O   . HOH I 5 .   ? 25.601  -1.733  -30.231 1.00 23.09 ? 538 HOH B O   1 
HETATM 4541 O  O   . HOH I 5 .   ? 8.611   -18.755 -41.717 1.00 35.53 ? 539 HOH B O   1 
HETATM 4542 O  O   . HOH I 5 .   ? 1.651   13.023  -36.640 1.00 46.27 ? 540 HOH B O   1 
HETATM 4543 O  O   . HOH I 5 .   ? 13.286  11.748  -26.136 1.00 42.99 ? 541 HOH B O   1 
HETATM 4544 O  O   . HOH I 5 .   ? 18.891  4.635   -43.821 1.00 38.93 ? 542 HOH B O   1 
HETATM 4545 O  O   . HOH I 5 .   ? -11.719 -18.846 -25.407 1.00 29.19 ? 543 HOH B O   1 
HETATM 4546 O  O   . HOH I 5 .   ? 0.989   -21.152 -22.633 1.00 31.99 ? 544 HOH B O   1 
HETATM 4547 O  O   . HOH I 5 .   ? -10.902 -15.901 -15.414 1.00 32.35 ? 545 HOH B O   1 
HETATM 4548 O  O   . HOH I 5 .   ? -20.424 -12.807 -18.765 1.00 29.22 ? 546 HOH B O   1 
HETATM 4549 O  O   . HOH I 5 .   ? 16.792  2.696   -45.027 1.00 20.46 ? 547 HOH B O   1 
HETATM 4550 O  O   . HOH I 5 .   ? 0.490   -17.660 -38.188 1.00 28.18 ? 548 HOH B O   1 
HETATM 4551 O  O   . HOH I 5 .   ? -9.373  -17.168 -33.146 1.00 29.78 ? 549 HOH B O   1 
HETATM 4552 O  O   . HOH I 5 .   ? 14.965  -16.465 -17.440 1.00 30.84 ? 550 HOH B O   1 
HETATM 4553 O  O   . HOH I 5 .   ? -10.177 10.607  -22.895 1.00 32.69 ? 551 HOH B O   1 
HETATM 4554 O  O   . HOH I 5 .   ? 13.302  5.083   -13.109 1.00 27.90 ? 552 HOH B O   1 
HETATM 4555 O  O   . HOH I 5 .   ? -13.557 -17.306 -28.106 1.00 24.23 ? 553 HOH B O   1 
HETATM 4556 O  O   . HOH I 5 .   ? -0.727  -17.680 -13.417 1.00 29.39 ? 554 HOH B O   1 
HETATM 4557 O  O   . HOH I 5 .   ? 7.293   4.511   -43.724 1.00 39.55 ? 555 HOH B O   1 
# 
