data_6R6Y
# 
_entry.id   6R6Y 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.397 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   6R6Y         pdb_00006r6y 10.2210/pdb6r6y/pdb 
WWPDB D_1292101525 ?            ?                   
# 
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 
4 'Structure model' 1 3 2024-10-09 
# 
_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' 
7 4 'Structure model' 'Structure summary'      
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' 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 
8 4 'Structure model' pdbx_entry_details            
9 4 'Structure model' pdbx_modification_feature     
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1  2 'Structure model' '_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                        6R6Y 
_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_
_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 4    4.2.1.1 ? 
'human carbonic anhydrase XII'                                           ? 
2 non-polymer syn 'ZINC ION'                                                                     65.409    4    ?       ? 
'4-chloro-2-cyclohexylsulfanyl-N-(2-hydroxyethyl)-5-sulfamoyl-benzamide' ? 
3 non-polymer syn 1,2-ETHANEDIOL                                                                 62.068    8    ?       ? Zn ? 
4 non-polymer syn 'DIMETHYL SULFOXIDE'                                                           78.133    2    ?       ? 
1,2-ETHANEDIOL                                                           ? 
5 non-polymer syn '4-chloranyl-2-cyclohexylsulfanyl-~{N}-(2-hydroxyethyl)-5-sulfamoyl-benzamide' 392.921   4    ?       ? ? ? 
6 water       nat water                                                                          18.015    1150 ?       ? ? ? 
# 
_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,C,D 
_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 'DIMETHYL SULFOXIDE'                                                           DMS 
5 '4-chloranyl-2-cyclohexylsulfanyl-~{N}-(2-hydroxyethyl)-5-sulfamoyl-benzamide' EA3 
6 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 BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              Rosetta 
_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 
DMS non-polymer         . 'DIMETHYL SULFOXIDE'                                                           ?                 
'C2 H6 O S'           78.133  
EA3 non-polymer         . '4-chloranyl-2-cyclohexylsulfanyl-~{N}-(2-hydroxyethyl)-5-sulfamoyl-benzamide' ?                 
'C15 H21 Cl N2 O4 S2' 392.921 
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 
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 
C 1 1   MET 1   1   ?   ?   ?   C . n 
C 1 2   SER 2   2   ?   ?   ?   C . n 
C 1 3   LYS 3   3   3   LYS LYS C . n 
C 1 4   TRP 4   4   4   TRP TRP C . n 
C 1 5   THR 5   5   5   THR THR C . n 
C 1 6   TYR 6   6   6   TYR TYR C . n 
C 1 7   PHE 7   7   7   PHE PHE C . n 
C 1 8   GLY 8   8   8   GLY GLY C . n 
C 1 9   PRO 9   9   9   PRO PRO C . n 
C 1 10  ASP 10  10  10  ASP ASP C . n 
C 1 11  GLY 11  11  11  GLY GLY C . n 
C 1 12  GLU 12  12  12  GLU GLU C . n 
C 1 13  ASN 13  13  13  ASN ASN C . n 
C 1 14  SER 14  14  14  SER SER C . n 
C 1 15  TRP 15  15  15  TRP TRP C . n 
C 1 16  SER 16  16  16  SER SER C . n 
C 1 17  LYS 17  17  17  LYS LYS C . n 
C 1 18  LYS 18  18  18  LYS LYS C . n 
C 1 19  TYR 19  19  19  TYR TYR C . n 
C 1 20  PRO 20  20  20  PRO PRO C . n 
C 1 21  SER 21  21  21  SER SER C . n 
C 1 22  CYS 22  22  22  CYS CYS C . n 
C 1 23  GLY 23  23  23  GLY GLY C . n 
C 1 24  GLY 24  24  24  GLY GLY C . n 
C 1 25  LEU 25  25  25  LEU LEU C . n 
C 1 26  LEU 26  26  26  LEU LEU C . n 
C 1 27  GLN 27  27  27  GLN GLN C . n 
C 1 28  SER 28  28  28  SER SER C . n 
C 1 29  PRO 29  29  29  PRO PRO C . n 
C 1 30  ILE 30  30  30  ILE ILE C . n 
C 1 31  ASP 31  31  31  ASP ASP C . n 
C 1 32  LEU 32  32  32  LEU LEU C . n 
C 1 33  HIS 33  33  33  HIS HIS C . n 
C 1 34  SER 34  34  34  SER SER C . n 
C 1 35  ASP 35  35  35  ASP ASP C . n 
C 1 36  ILE 36  36  36  ILE ILE C . n 
C 1 37  LEU 37  37  37  LEU LEU C . n 
C 1 38  GLN 38  38  38  GLN GLN C . n 
C 1 39  TYR 39  39  39  TYR TYR C . n 
C 1 40  ASP 40  40  40  ASP ASP C . n 
C 1 41  ALA 41  41  41  ALA ALA C . n 
C 1 42  SER 42  42  42  SER SER C . n 
C 1 43  LEU 43  43  43  LEU LEU C . n 
C 1 44  THR 44  44  44  THR THR C . n 
C 1 45  PRO 45  45  45  PRO PRO C . n 
C 1 46  LEU 46  46  46  LEU LEU C . n 
C 1 47  GLU 47  47  47  GLU GLU C . n 
C 1 48  PHE 48  48  48  PHE PHE C . n 
C 1 49  GLN 49  49  49  GLN GLN C . n 
C 1 50  GLY 50  50  50  GLY GLY C . n 
C 1 51  TYR 51  51  51  TYR TYR C . n 
C 1 52  ASN 52  52  52  ASN ASN C . n 
C 1 53  LEU 53  53  53  LEU LEU C . n 
C 1 54  SER 54  54  54  SER SER C . n 
C 1 55  ALA 55  55  55  ALA ALA C . n 
C 1 56  ASN 56  56  56  ASN ASN C . n 
C 1 57  LYS 57  57  57  LYS LYS C . n 
C 1 58  GLN 58  58  58  GLN GLN C . n 
C 1 59  PHE 59  59  59  PHE PHE C . n 
C 1 60  LEU 60  60  60  LEU LEU C . n 
C 1 61  LEU 61  61  61  LEU LEU C . n 
C 1 62  THR 62  62  62  THR THR C . n 
C 1 63  ASN 63  63  63  ASN ASN C . n 
C 1 64  ASN 64  64  64  ASN ASN C . n 
C 1 65  GLY 65  65  65  GLY GLY C . n 
C 1 66  HIS 66  66  66  HIS HIS C . n 
C 1 67  SER 67  67  67  SER SER C . n 
C 1 68  VAL 68  68  68  VAL VAL C . n 
C 1 69  LYS 69  69  69  LYS LYS C . n 
C 1 70  LEU 70  70  70  LEU LEU C . n 
C 1 71  ASN 71  71  71  ASN ASN C . n 
C 1 72  LEU 72  72  72  LEU LEU C . n 
C 1 73  PRO 73  73  73  PRO PRO C . n 
C 1 74  SER 74  74  74  SER SER C . n 
C 1 75  ASP 75  75  75  ASP ASP C . n 
C 1 76  MET 76  76  76  MET MET C . n 
C 1 77  HIS 77  77  77  HIS HIS C . n 
C 1 78  ILE 78  78  78  ILE ILE C . n 
C 1 79  GLN 79  79  79  GLN GLN C . n 
C 1 80  GLY 80  80  80  GLY GLY C . n 
C 1 81  LEU 81  81  81  LEU LEU C . n 
C 1 82  GLN 82  82  82  GLN GLN C . n 
C 1 83  SER 83  83  83  SER SER C . n 
C 1 84  ARG 84  84  84  ARG ARG C . n 
C 1 85  TYR 85  85  85  TYR TYR C . n 
C 1 86  SER 86  86  86  SER SER C . n 
C 1 87  ALA 87  87  87  ALA ALA C . n 
C 1 88  THR 88  88  88  THR THR C . n 
C 1 89  GLN 89  89  89  GLN GLN C . n 
C 1 90  LEU 90  90  90  LEU LEU C . n 
C 1 91  HIS 91  91  91  HIS HIS C . n 
C 1 92  LEU 92  92  92  LEU LEU C . n 
C 1 93  HIS 93  93  93  HIS HIS C . n 
C 1 94  TRP 94  94  94  TRP TRP C . n 
C 1 95  GLY 95  95  95  GLY GLY C . n 
C 1 96  ASN 96  96  96  ASN ASN C . n 
C 1 97  PRO 97  97  97  PRO PRO C . n 
C 1 98  ASN 98  98  98  ASN ASN C . n 
C 1 99  ASP 99  99  99  ASP ASP C . n 
C 1 100 PRO 100 100 100 PRO PRO C . n 
C 1 101 HIS 101 101 101 HIS HIS C . n 
C 1 102 GLY 102 102 102 GLY GLY C . n 
C 1 103 SER 103 103 103 SER SER C . n 
C 1 104 GLU 104 104 104 GLU GLU C . n 
C 1 105 HIS 105 105 105 HIS HIS C . n 
C 1 106 THR 106 106 106 THR THR C . n 
C 1 107 VAL 107 107 107 VAL VAL C . n 
C 1 108 SER 108 108 108 SER SER C . n 
C 1 109 GLY 109 109 109 GLY GLY C . n 
C 1 110 GLN 110 110 110 GLN GLN C . n 
C 1 111 HIS 111 111 111 HIS HIS C . n 
C 1 112 PHE 112 112 112 PHE PHE C . n 
C 1 113 ALA 113 113 113 ALA ALA C . n 
C 1 114 ALA 114 114 114 ALA ALA C . n 
C 1 115 GLU 115 115 115 GLU GLU C . n 
C 1 116 LEU 116 116 116 LEU LEU C . n 
C 1 117 HIS 117 117 117 HIS HIS C . n 
C 1 118 ILE 118 118 118 ILE ILE C . n 
C 1 119 VAL 119 119 119 VAL VAL C . n 
C 1 120 HIS 120 120 120 HIS HIS C . n 
C 1 121 TYR 121 121 121 TYR TYR C . n 
C 1 122 ASN 122 122 122 ASN ASN C . n 
C 1 123 SER 123 123 123 SER SER C . n 
C 1 124 ASP 124 124 124 ASP ASP C . n 
C 1 125 LEU 125 125 125 LEU LEU C . n 
C 1 126 TYR 126 126 126 TYR TYR C . n 
C 1 127 PRO 127 127 127 PRO PRO C . n 
C 1 128 ASP 128 128 128 ASP ASP C . n 
C 1 129 ALA 129 129 129 ALA ALA C . n 
C 1 130 SER 130 130 130 SER SER C . n 
C 1 131 THR 131 131 131 THR THR C . n 
C 1 132 ALA 132 132 132 ALA ALA C . n 
C 1 133 SER 133 133 133 SER SER C . n 
C 1 134 ASN 134 134 134 ASN ASN C . n 
C 1 135 LYS 135 135 135 LYS LYS C . n 
C 1 136 SER 136 136 136 SER SER C . n 
C 1 137 GLU 137 137 137 GLU GLU C . n 
C 1 138 GLY 138 138 138 GLY GLY C . n 
C 1 139 LEU 139 139 139 LEU LEU C . n 
C 1 140 ALA 140 140 140 ALA ALA C . n 
C 1 141 VAL 141 141 141 VAL VAL C . n 
C 1 142 LEU 142 142 142 LEU LEU C . n 
C 1 143 ALA 143 143 143 ALA ALA C . n 
C 1 144 VAL 144 144 144 VAL VAL C . n 
C 1 145 LEU 145 145 145 LEU LEU C . n 
C 1 146 ILE 146 146 146 ILE ILE C . n 
C 1 147 GLU 147 147 147 GLU GLU C . n 
C 1 148 MET 148 148 148 MET MET C . n 
C 1 149 GLY 149 149 149 GLY GLY C . n 
C 1 150 SER 150 150 150 SER SER C . n 
C 1 151 PHE 151 151 151 PHE PHE C . n 
C 1 152 ASN 152 152 152 ASN ASN C . n 
C 1 153 PRO 153 153 153 PRO PRO C . n 
C 1 154 SER 154 154 154 SER SER C . n 
C 1 155 TYR 155 155 155 TYR TYR C . n 
C 1 156 ASP 156 156 156 ASP ASP C . n 
C 1 157 LYS 157 157 157 LYS LYS C . n 
C 1 158 ILE 158 158 158 ILE ILE C . n 
C 1 159 PHE 159 159 159 PHE PHE C . n 
C 1 160 SER 160 160 160 SER SER C . n 
C 1 161 HIS 161 161 161 HIS HIS C . n 
C 1 162 LEU 162 162 162 LEU LEU C . n 
C 1 163 GLN 163 163 163 GLN GLN C . n 
C 1 164 HIS 164 164 164 HIS HIS C . n 
C 1 165 VAL 165 165 165 VAL VAL C . n 
C 1 166 LYS 166 166 166 LYS LYS C . n 
C 1 167 TYR 167 167 167 TYR TYR C . n 
C 1 168 LYS 168 168 168 LYS LYS C . n 
C 1 169 GLY 169 169 169 GLY GLY C . n 
C 1 170 GLN 170 170 170 GLN GLN C . n 
C 1 171 GLU 171 171 171 GLU GLU C . n 
C 1 172 ALA 172 172 172 ALA ALA C . n 
C 1 173 PHE 173 173 173 PHE PHE C . n 
C 1 174 VAL 174 174 174 VAL VAL C . n 
C 1 175 PRO 175 175 175 PRO PRO C . n 
C 1 176 GLY 176 176 176 GLY GLY C . n 
C 1 177 PHE 177 177 177 PHE PHE C . n 
C 1 178 ASN 178 178 178 ASN ASN C . n 
C 1 179 ILE 179 179 179 ILE ILE C . n 
C 1 180 GLU 180 180 180 GLU GLU C . n 
C 1 181 GLU 181 181 181 GLU GLU C . n 
C 1 182 LEU 182 182 182 LEU LEU C . n 
C 1 183 LEU 183 183 183 LEU LEU C . n 
C 1 184 PRO 184 184 184 PRO PRO C . n 
C 1 185 GLU 185 185 185 GLU GLU C . n 
C 1 186 ARG 186 186 186 ARG ARG C . n 
C 1 187 THR 187 187 187 THR THR C . n 
C 1 188 ALA 188 188 188 ALA ALA C . n 
C 1 189 GLU 189 189 189 GLU GLU C . n 
C 1 190 TYR 190 190 190 TYR TYR C . n 
C 1 191 TYR 191 191 191 TYR TYR C . n 
C 1 192 ARG 192 192 192 ARG ARG C . n 
C 1 193 TYR 193 193 193 TYR TYR C . n 
C 1 194 ARG 194 194 194 ARG ARG C . n 
C 1 195 GLY 195 195 195 GLY GLY C . n 
C 1 196 SER 196 196 196 SER SER C . n 
C 1 197 LEU 197 197 197 LEU LEU C . n 
C 1 198 THR 198 198 198 THR THR C . n 
C 1 199 THR 199 199 199 THR THR C . n 
C 1 200 PRO 200 200 200 PRO PRO C . n 
C 1 201 PRO 201 201 201 PRO PRO C . n 
C 1 202 CYS 202 202 202 CYS CYS C . n 
C 1 203 ASN 203 203 203 ASN ASN C . n 
C 1 204 PRO 204 204 204 PRO PRO C . n 
C 1 205 THR 205 205 205 THR THR C . n 
C 1 206 VAL 206 206 206 VAL VAL C . n 
C 1 207 LEU 207 207 207 LEU LEU C . n 
C 1 208 TRP 208 208 208 TRP TRP C . n 
C 1 209 THR 209 209 209 THR THR C . n 
C 1 210 VAL 210 210 210 VAL VAL C . n 
C 1 211 PHE 211 211 211 PHE PHE C . n 
C 1 212 ARG 212 212 212 ARG ARG C . n 
C 1 213 ASN 213 213 213 ASN ASN C . n 
C 1 214 PRO 214 214 214 PRO PRO C . n 
C 1 215 VAL 215 215 215 VAL VAL C . n 
C 1 216 GLN 216 216 216 GLN GLN C . n 
C 1 217 ILE 217 217 217 ILE ILE C . n 
C 1 218 SER 218 218 218 SER SER C . n 
C 1 219 GLN 219 219 219 GLN GLN C . n 
C 1 220 GLU 220 220 220 GLU GLU C . n 
C 1 221 GLN 221 221 221 GLN GLN C . n 
C 1 222 LEU 222 222 222 LEU LEU C . n 
C 1 223 LEU 223 223 223 LEU LEU C . n 
C 1 224 ALA 224 224 224 ALA ALA C . n 
C 1 225 LEU 225 225 225 LEU LEU C . n 
C 1 226 GLU 226 226 226 GLU GLU C . n 
C 1 227 THR 227 227 227 THR THR C . n 
C 1 228 ALA 228 228 228 ALA ALA C . n 
C 1 229 LEU 229 229 229 LEU LEU C . n 
C 1 230 TYR 230 230 230 TYR TYR C . n 
C 1 231 CYS 231 231 231 CYS CYS C . n 
C 1 232 THR 232 232 232 THR THR C . n 
C 1 233 HIS 233 233 233 HIS HIS C . n 
C 1 234 MET 234 234 234 MET MET C . n 
C 1 235 ASP 235 235 235 ASP ASP C . n 
C 1 236 ASP 236 236 236 ASP ASP C . n 
C 1 237 PRO 237 237 237 PRO PRO C . n 
C 1 238 SER 238 238 238 SER SER C . n 
C 1 239 PRO 239 239 239 PRO PRO C . n 
C 1 240 ARG 240 240 240 ARG ARG C . n 
C 1 241 GLU 241 241 241 GLU GLU C . n 
C 1 242 MET 242 242 242 MET MET C . n 
C 1 243 ILE 243 243 243 ILE ILE C . n 
C 1 244 ASN 244 244 244 ASN ASN C . n 
C 1 245 ASN 245 245 245 ASN ASN C . n 
C 1 246 PHE 246 246 246 PHE PHE C . n 
C 1 247 ARG 247 247 247 ARG ARG C . n 
C 1 248 GLN 248 248 248 GLN GLN C . n 
C 1 249 VAL 249 249 249 VAL VAL C . n 
C 1 250 GLN 250 250 250 GLN GLN C . n 
C 1 251 LYS 251 251 251 LYS LYS C . n 
C 1 252 PHE 252 252 252 PHE PHE C . n 
C 1 253 ASP 253 253 253 ASP ASP C . n 
C 1 254 GLU 254 254 254 GLU GLU C . n 
C 1 255 ARG 255 255 255 ARG ARG C . n 
C 1 256 LEU 256 256 256 LEU LEU C . n 
C 1 257 VAL 257 257 257 VAL VAL C . n 
C 1 258 TYR 258 258 258 TYR TYR C . n 
C 1 259 THR 259 259 259 THR THR C . n 
C 1 260 SER 260 260 260 SER SER C . n 
C 1 261 PHE 261 261 261 PHE PHE C . n 
C 1 262 SER 262 262 262 SER SER C . n 
C 1 263 GLN 263 263 263 GLN GLN C . n 
D 1 1   MET 1   1   ?   ?   ?   D . n 
D 1 2   SER 2   2   ?   ?   ?   D . n 
D 1 3   LYS 3   3   3   LYS LYS D . n 
D 1 4   TRP 4   4   4   TRP TRP D . n 
D 1 5   THR 5   5   5   THR THR D . n 
D 1 6   TYR 6   6   6   TYR TYR D . n 
D 1 7   PHE 7   7   7   PHE PHE D . n 
D 1 8   GLY 8   8   8   GLY GLY D . n 
D 1 9   PRO 9   9   9   PRO PRO D . n 
D 1 10  ASP 10  10  10  ASP ASP D . n 
D 1 11  GLY 11  11  11  GLY GLY D . n 
D 1 12  GLU 12  12  12  GLU GLU D . n 
D 1 13  ASN 13  13  13  ASN ASN D . n 
D 1 14  SER 14  14  14  SER SER D . n 
D 1 15  TRP 15  15  15  TRP TRP D . n 
D 1 16  SER 16  16  16  SER SER D . n 
D 1 17  LYS 17  17  17  LYS LYS D . n 
D 1 18  LYS 18  18  18  LYS LYS D . n 
D 1 19  TYR 19  19  19  TYR TYR D . n 
D 1 20  PRO 20  20  20  PRO PRO D . n 
D 1 21  SER 21  21  21  SER SER D . n 
D 1 22  CYS 22  22  22  CYS CYS D . n 
D 1 23  GLY 23  23  23  GLY GLY D . n 
D 1 24  GLY 24  24  24  GLY GLY D . n 
D 1 25  LEU 25  25  25  LEU LEU D . n 
D 1 26  LEU 26  26  26  LEU LEU D . n 
D 1 27  GLN 27  27  27  GLN GLN D . n 
D 1 28  SER 28  28  28  SER SER D . n 
D 1 29  PRO 29  29  29  PRO PRO D . n 
D 1 30  ILE 30  30  30  ILE ILE D . n 
D 1 31  ASP 31  31  31  ASP ASP D . n 
D 1 32  LEU 32  32  32  LEU LEU D . n 
D 1 33  HIS 33  33  33  HIS HIS D . n 
D 1 34  SER 34  34  34  SER SER D . n 
D 1 35  ASP 35  35  35  ASP ASP D . n 
D 1 36  ILE 36  36  36  ILE ILE D . n 
D 1 37  LEU 37  37  37  LEU LEU D . n 
D 1 38  GLN 38  38  38  GLN GLN D . n 
D 1 39  TYR 39  39  39  TYR TYR D . n 
D 1 40  ASP 40  40  40  ASP ASP D . n 
D 1 41  ALA 41  41  41  ALA ALA D . n 
D 1 42  SER 42  42  42  SER SER D . n 
D 1 43  LEU 43  43  43  LEU LEU D . n 
D 1 44  THR 44  44  44  THR THR D . n 
D 1 45  PRO 45  45  45  PRO PRO D . n 
D 1 46  LEU 46  46  46  LEU LEU D . n 
D 1 47  GLU 47  47  47  GLU GLU D . n 
D 1 48  PHE 48  48  48  PHE PHE D . n 
D 1 49  GLN 49  49  49  GLN GLN D . n 
D 1 50  GLY 50  50  50  GLY GLY D . n 
D 1 51  TYR 51  51  51  TYR TYR D . n 
D 1 52  ASN 52  52  52  ASN ASN D . n 
D 1 53  LEU 53  53  53  LEU LEU D . n 
D 1 54  SER 54  54  54  SER SER D . n 
D 1 55  ALA 55  55  55  ALA ALA D . n 
D 1 56  ASN 56  56  56  ASN ASN D . n 
D 1 57  LYS 57  57  57  LYS LYS D . n 
D 1 58  GLN 58  58  58  GLN GLN D . n 
D 1 59  PHE 59  59  59  PHE PHE D . n 
D 1 60  LEU 60  60  60  LEU LEU D . n 
D 1 61  LEU 61  61  61  LEU LEU D . n 
D 1 62  THR 62  62  62  THR THR D . n 
D 1 63  ASN 63  63  63  ASN ASN D . n 
D 1 64  ASN 64  64  64  ASN ASN D . n 
D 1 65  GLY 65  65  65  GLY GLY D . n 
D 1 66  HIS 66  66  66  HIS HIS D . n 
D 1 67  SER 67  67  67  SER SER D . n 
D 1 68  VAL 68  68  68  VAL VAL D . n 
D 1 69  LYS 69  69  69  LYS LYS D . n 
D 1 70  LEU 70  70  70  LEU LEU D . n 
D 1 71  ASN 71  71  71  ASN ASN D . n 
D 1 72  LEU 72  72  72  LEU LEU D . n 
D 1 73  PRO 73  73  73  PRO PRO D . n 
D 1 74  SER 74  74  74  SER SER D . n 
D 1 75  ASP 75  75  75  ASP ASP D . n 
D 1 76  MET 76  76  76  MET MET D . n 
D 1 77  HIS 77  77  77  HIS HIS D . n 
D 1 78  ILE 78  78  78  ILE ILE D . n 
D 1 79  GLN 79  79  79  GLN GLN D . n 
D 1 80  GLY 80  80  80  GLY GLY D . n 
D 1 81  LEU 81  81  81  LEU LEU D . n 
D 1 82  GLN 82  82  82  GLN GLN D . n 
D 1 83  SER 83  83  83  SER SER D . n 
D 1 84  ARG 84  84  84  ARG ARG D . n 
D 1 85  TYR 85  85  85  TYR TYR D . n 
D 1 86  SER 86  86  86  SER SER D . n 
D 1 87  ALA 87  87  87  ALA ALA D . n 
D 1 88  THR 88  88  88  THR THR D . n 
D 1 89  GLN 89  89  89  GLN GLN D . n 
D 1 90  LEU 90  90  90  LEU LEU D . n 
D 1 91  HIS 91  91  91  HIS HIS D . n 
D 1 92  LEU 92  92  92  LEU LEU D . n 
D 1 93  HIS 93  93  93  HIS HIS D . n 
D 1 94  TRP 94  94  94  TRP TRP D . n 
D 1 95  GLY 95  95  95  GLY GLY D . n 
D 1 96  ASN 96  96  96  ASN ASN D . n 
D 1 97  PRO 97  97  97  PRO PRO D . n 
D 1 98  ASN 98  98  98  ASN ASN D . n 
D 1 99  ASP 99  99  99  ASP ASP D . n 
D 1 100 PRO 100 100 100 PRO PRO D . n 
D 1 101 HIS 101 101 101 HIS HIS D . n 
D 1 102 GLY 102 102 102 GLY GLY D . n 
D 1 103 SER 103 103 103 SER SER D . n 
D 1 104 GLU 104 104 104 GLU GLU D . n 
D 1 105 HIS 105 105 105 HIS HIS D . n 
D 1 106 THR 106 106 106 THR THR D . n 
D 1 107 VAL 107 107 107 VAL VAL D . n 
D 1 108 SER 108 108 108 SER SER D . n 
D 1 109 GLY 109 109 109 GLY GLY D . n 
D 1 110 GLN 110 110 110 GLN GLN D . n 
D 1 111 HIS 111 111 111 HIS HIS D . n 
D 1 112 PHE 112 112 112 PHE PHE D . n 
D 1 113 ALA 113 113 113 ALA ALA D . n 
D 1 114 ALA 114 114 114 ALA ALA D . n 
D 1 115 GLU 115 115 115 GLU GLU D . n 
D 1 116 LEU 116 116 116 LEU LEU D . n 
D 1 117 HIS 117 117 117 HIS HIS D . n 
D 1 118 ILE 118 118 118 ILE ILE D . n 
D 1 119 VAL 119 119 119 VAL VAL D . n 
D 1 120 HIS 120 120 120 HIS HIS D . n 
D 1 121 TYR 121 121 121 TYR TYR D . n 
D 1 122 ASN 122 122 122 ASN ASN D . n 
D 1 123 SER 123 123 123 SER SER D . n 
D 1 124 ASP 124 124 124 ASP ASP D . n 
D 1 125 LEU 125 125 125 LEU LEU D . n 
D 1 126 TYR 126 126 126 TYR TYR D . n 
D 1 127 PRO 127 127 127 PRO PRO D . n 
D 1 128 ASP 128 128 128 ASP ASP D . n 
D 1 129 ALA 129 129 129 ALA ALA D . n 
D 1 130 SER 130 130 130 SER SER D . n 
D 1 131 THR 131 131 131 THR THR D . n 
D 1 132 ALA 132 132 132 ALA ALA D . n 
D 1 133 SER 133 133 133 SER SER D . n 
D 1 134 ASN 134 134 134 ASN ASN D . n 
D 1 135 LYS 135 135 135 LYS LYS D . n 
D 1 136 SER 136 136 136 SER SER D . n 
D 1 137 GLU 137 137 137 GLU GLU D . n 
D 1 138 GLY 138 138 138 GLY GLY D . n 
D 1 139 LEU 139 139 139 LEU LEU D . n 
D 1 140 ALA 140 140 140 ALA ALA D . n 
D 1 141 VAL 141 141 141 VAL VAL D . n 
D 1 142 LEU 142 142 142 LEU LEU D . n 
D 1 143 ALA 143 143 143 ALA ALA D . n 
D 1 144 VAL 144 144 144 VAL VAL D . n 
D 1 145 LEU 145 145 145 LEU LEU D . n 
D 1 146 ILE 146 146 146 ILE ILE D . n 
D 1 147 GLU 147 147 147 GLU GLU D . n 
D 1 148 MET 148 148 148 MET MET D . n 
D 1 149 GLY 149 149 149 GLY GLY D . n 
D 1 150 SER 150 150 150 SER SER D . n 
D 1 151 PHE 151 151 151 PHE PHE D . n 
D 1 152 ASN 152 152 152 ASN ASN D . n 
D 1 153 PRO 153 153 153 PRO PRO D . n 
D 1 154 SER 154 154 154 SER SER D . n 
D 1 155 TYR 155 155 155 TYR TYR D . n 
D 1 156 ASP 156 156 156 ASP ASP D . n 
D 1 157 LYS 157 157 157 LYS LYS D . n 
D 1 158 ILE 158 158 158 ILE ILE D . n 
D 1 159 PHE 159 159 159 PHE PHE D . n 
D 1 160 SER 160 160 160 SER SER D . n 
D 1 161 HIS 161 161 161 HIS HIS D . n 
D 1 162 LEU 162 162 162 LEU LEU D . n 
D 1 163 GLN 163 163 163 GLN GLN D . n 
D 1 164 HIS 164 164 164 HIS HIS D . n 
D 1 165 VAL 165 165 165 VAL VAL D . n 
D 1 166 LYS 166 166 166 LYS LYS D . n 
D 1 167 TYR 167 167 167 TYR TYR D . n 
D 1 168 LYS 168 168 168 LYS LYS D . n 
D 1 169 GLY 169 169 169 GLY GLY D . n 
D 1 170 GLN 170 170 170 GLN GLN D . n 
D 1 171 GLU 171 171 171 GLU GLU D . n 
D 1 172 ALA 172 172 172 ALA ALA D . n 
D 1 173 PHE 173 173 173 PHE PHE D . n 
D 1 174 VAL 174 174 174 VAL VAL D . n 
D 1 175 PRO 175 175 175 PRO PRO D . n 
D 1 176 GLY 176 176 176 GLY GLY D . n 
D 1 177 PHE 177 177 177 PHE PHE D . n 
D 1 178 ASN 178 178 178 ASN ASN D . n 
D 1 179 ILE 179 179 179 ILE ILE D . n 
D 1 180 GLU 180 180 180 GLU GLU D . n 
D 1 181 GLU 181 181 181 GLU GLU D . n 
D 1 182 LEU 182 182 182 LEU LEU D . n 
D 1 183 LEU 183 183 183 LEU LEU D . n 
D 1 184 PRO 184 184 184 PRO PRO D . n 
D 1 185 GLU 185 185 185 GLU GLU D . n 
D 1 186 ARG 186 186 186 ARG ARG D . n 
D 1 187 THR 187 187 187 THR THR D . n 
D 1 188 ALA 188 188 188 ALA ALA D . n 
D 1 189 GLU 189 189 189 GLU GLU D . n 
D 1 190 TYR 190 190 190 TYR TYR D . n 
D 1 191 TYR 191 191 191 TYR TYR D . n 
D 1 192 ARG 192 192 192 ARG ARG D . n 
D 1 193 TYR 193 193 193 TYR TYR D . n 
D 1 194 ARG 194 194 194 ARG ARG D . n 
D 1 195 GLY 195 195 195 GLY GLY D . n 
D 1 196 SER 196 196 196 SER SER D . n 
D 1 197 LEU 197 197 197 LEU LEU D . n 
D 1 198 THR 198 198 198 THR THR D . n 
D 1 199 THR 199 199 199 THR THR D . n 
D 1 200 PRO 200 200 200 PRO PRO D . n 
D 1 201 PRO 201 201 201 PRO PRO D . n 
D 1 202 CYS 202 202 202 CYS CYS D . n 
D 1 203 ASN 203 203 203 ASN ASN D . n 
D 1 204 PRO 204 204 204 PRO PRO D . n 
D 1 205 THR 205 205 205 THR THR D . n 
D 1 206 VAL 206 206 206 VAL VAL D . n 
D 1 207 LEU 207 207 207 LEU LEU D . n 
D 1 208 TRP 208 208 208 TRP TRP D . n 
D 1 209 THR 209 209 209 THR THR D . n 
D 1 210 VAL 210 210 210 VAL VAL D . n 
D 1 211 PHE 211 211 211 PHE PHE D . n 
D 1 212 ARG 212 212 212 ARG ARG D . n 
D 1 213 ASN 213 213 213 ASN ASN D . n 
D 1 214 PRO 214 214 214 PRO PRO D . n 
D 1 215 VAL 215 215 215 VAL VAL D . n 
D 1 216 GLN 216 216 216 GLN GLN D . n 
D 1 217 ILE 217 217 217 ILE ILE D . n 
D 1 218 SER 218 218 218 SER SER D . n 
D 1 219 GLN 219 219 219 GLN GLN D . n 
D 1 220 GLU 220 220 220 GLU GLU D . n 
D 1 221 GLN 221 221 221 GLN GLN D . n 
D 1 222 LEU 222 222 222 LEU LEU D . n 
D 1 223 LEU 223 223 223 LEU LEU D . n 
D 1 224 ALA 224 224 224 ALA ALA D . n 
D 1 225 LEU 225 225 225 LEU LEU D . n 
D 1 226 GLU 226 226 226 GLU GLU D . n 
D 1 227 THR 227 227 227 THR THR D . n 
D 1 228 ALA 228 228 228 ALA ALA D . n 
D 1 229 LEU 229 229 229 LEU LEU D . n 
D 1 230 TYR 230 230 230 TYR TYR D . n 
D 1 231 CYS 231 231 231 CYS CYS D . n 
D 1 232 THR 232 232 232 THR THR D . n 
D 1 233 HIS 233 233 233 HIS HIS D . n 
D 1 234 MET 234 234 234 MET MET D . n 
D 1 235 ASP 235 235 235 ASP ASP D . n 
D 1 236 ASP 236 236 236 ASP ASP D . n 
D 1 237 PRO 237 237 237 PRO PRO D . n 
D 1 238 SER 238 238 238 SER SER D . n 
D 1 239 PRO 239 239 239 PRO PRO D . n 
D 1 240 ARG 240 240 240 ARG ARG D . n 
D 1 241 GLU 241 241 241 GLU GLU D . n 
D 1 242 MET 242 242 242 MET MET D . n 
D 1 243 ILE 243 243 243 ILE ILE D . n 
D 1 244 ASN 244 244 244 ASN ASN D . n 
D 1 245 ASN 245 245 245 ASN ASN D . n 
D 1 246 PHE 246 246 246 PHE PHE D . n 
D 1 247 ARG 247 247 247 ARG ARG D . n 
D 1 248 GLN 248 248 248 GLN GLN D . n 
D 1 249 VAL 249 249 249 VAL VAL D . n 
D 1 250 GLN 250 250 250 GLN GLN D . n 
D 1 251 LYS 251 251 251 LYS LYS D . n 
D 1 252 PHE 252 252 252 PHE PHE D . n 
D 1 253 ASP 253 253 253 ASP ASP D . n 
D 1 254 GLU 254 254 254 GLU GLU D . n 
D 1 255 ARG 255 255 255 ARG ARG D . n 
D 1 256 LEU 256 256 256 LEU LEU D . n 
D 1 257 VAL 257 257 257 VAL VAL D . n 
D 1 258 TYR 258 258 258 TYR TYR D . n 
D 1 259 THR 259 259 259 THR THR D . n 
D 1 260 SER 260 260 260 SER SER D . n 
D 1 261 PHE 261 261 261 PHE PHE D . n 
D 1 262 SER 262 262 262 SER SER D . n 
D 1 263 GLN 263 263 263 GLN GLN D . 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 
E 2 ZN  1   301 1    ZN  ZN  A . 
F 3 EDO 1   302 3    EDO EDO A . 
G 3 EDO 1   303 6    EDO EDO A . 
H 4 DMS 1   304 8    DMS DMS A . 
I 5 EA3 1   305 1    EA3 EA3 A . 
J 2 ZN  1   301 2    ZN  ZN  B . 
K 3 EDO 1   302 2    EDO EDO B . 
L 3 EDO 1   303 4    EDO EDO B . 
M 3 EDO 1   304 9    EDO EDO B . 
N 5 EA3 1   305 2    EA3 EA3 B . 
O 2 ZN  1   301 3    ZN  ZN  C . 
P 3 EDO 1   302 5    EDO EDO C . 
Q 3 EDO 1   303 10   EDO EDO C . 
R 4 DMS 1   304 11   DMS DMS C . 
S 5 EA3 1   305 3    EA3 EA3 C . 
T 2 ZN  1   301 4    ZN  ZN  D . 
U 3 EDO 1   302 1    EDO EDO D . 
V 5 EA3 1   303 4    EA3 EA3 D . 
W 6 HOH 1   401 699  HOH HOH A . 
W 6 HOH 2   402 944  HOH HOH A . 
W 6 HOH 3   403 855  HOH HOH A . 
W 6 HOH 4   404 959  HOH HOH A . 
W 6 HOH 5   405 205  HOH HOH A . 
W 6 HOH 6   406 382  HOH HOH A . 
W 6 HOH 7   407 591  HOH HOH A . 
W 6 HOH 8   408 1077 HOH HOH A . 
W 6 HOH 9   409 673  HOH HOH A . 
W 6 HOH 10  410 1081 HOH HOH A . 
W 6 HOH 11  411 879  HOH HOH A . 
W 6 HOH 12  412 1078 HOH HOH A . 
W 6 HOH 13  413 640  HOH HOH A . 
W 6 HOH 14  414 876  HOH HOH A . 
W 6 HOH 15  415 195  HOH HOH A . 
W 6 HOH 16  416 455  HOH HOH A . 
W 6 HOH 17  417 663  HOH HOH A . 
W 6 HOH 18  418 822  HOH HOH A . 
W 6 HOH 19  419 249  HOH HOH A . 
W 6 HOH 20  420 865  HOH HOH A . 
W 6 HOH 21  421 334  HOH HOH A . 
W 6 HOH 22  422 6    HOH HOH A . 
W 6 HOH 23  423 601  HOH HOH A . 
W 6 HOH 24  424 610  HOH HOH A . 
W 6 HOH 25  425 679  HOH HOH A . 
W 6 HOH 26  426 936  HOH HOH A . 
W 6 HOH 27  427 176  HOH HOH A . 
W 6 HOH 28  428 1065 HOH HOH A . 
W 6 HOH 29  429 793  HOH HOH A . 
W 6 HOH 30  430 335  HOH HOH A . 
W 6 HOH 31  431 589  HOH HOH A . 
W 6 HOH 32  432 884  HOH HOH A . 
W 6 HOH 33  433 890  HOH HOH A . 
W 6 HOH 34  434 647  HOH HOH A . 
W 6 HOH 35  435 283  HOH HOH A . 
W 6 HOH 36  436 491  HOH HOH A . 
W 6 HOH 37  437 874  HOH HOH A . 
W 6 HOH 38  438 781  HOH HOH A . 
W 6 HOH 39  439 234  HOH HOH A . 
W 6 HOH 40  440 106  HOH HOH A . 
W 6 HOH 41  441 710  HOH HOH A . 
W 6 HOH 42  442 1064 HOH HOH A . 
W 6 HOH 43  443 388  HOH HOH A . 
W 6 HOH 44  444 559  HOH HOH A . 
W 6 HOH 45  445 298  HOH HOH A . 
W 6 HOH 46  446 174  HOH HOH A . 
W 6 HOH 47  447 374  HOH HOH A . 
W 6 HOH 48  448 92   HOH HOH A . 
W 6 HOH 49  449 96   HOH HOH A . 
W 6 HOH 50  450 72   HOH HOH A . 
W 6 HOH 51  451 51   HOH HOH A . 
W 6 HOH 52  452 80   HOH HOH A . 
W 6 HOH 53  453 55   HOH HOH A . 
W 6 HOH 54  454 224  HOH HOH A . 
W 6 HOH 55  455 113  HOH HOH A . 
W 6 HOH 56  456 87   HOH HOH A . 
W 6 HOH 57  457 818  HOH HOH A . 
W 6 HOH 58  458 313  HOH HOH A . 
W 6 HOH 59  459 534  HOH HOH A . 
W 6 HOH 60  460 156  HOH HOH A . 
W 6 HOH 61  461 163  HOH HOH A . 
W 6 HOH 62  462 115  HOH HOH A . 
W 6 HOH 63  463 393  HOH HOH A . 
W 6 HOH 64  464 28   HOH HOH A . 
W 6 HOH 65  465 104  HOH HOH A . 
W 6 HOH 66  466 242  HOH HOH A . 
W 6 HOH 67  467 30   HOH HOH A . 
W 6 HOH 68  468 452  HOH HOH A . 
W 6 HOH 69  469 200  HOH HOH A . 
W 6 HOH 70  470 10   HOH HOH A . 
W 6 HOH 71  471 808  HOH HOH A . 
W 6 HOH 72  472 333  HOH HOH A . 
W 6 HOH 73  473 941  HOH HOH A . 
W 6 HOH 74  474 966  HOH HOH A . 
W 6 HOH 75  475 262  HOH HOH A . 
W 6 HOH 76  476 484  HOH HOH A . 
W 6 HOH 77  477 17   HOH HOH A . 
W 6 HOH 78  478 761  HOH HOH A . 
W 6 HOH 79  479 91   HOH HOH A . 
W 6 HOH 80  480 36   HOH HOH A . 
W 6 HOH 81  481 875  HOH HOH A . 
W 6 HOH 82  482 12   HOH HOH A . 
W 6 HOH 83  483 182  HOH HOH A . 
W 6 HOH 84  484 130  HOH HOH A . 
W 6 HOH 85  485 377  HOH HOH A . 
W 6 HOH 86  486 146  HOH HOH A . 
W 6 HOH 87  487 867  HOH HOH A . 
W 6 HOH 88  488 289  HOH HOH A . 
W 6 HOH 89  489 126  HOH HOH A . 
W 6 HOH 90  490 636  HOH HOH A . 
W 6 HOH 91  491 802  HOH HOH A . 
W 6 HOH 92  492 1068 HOH HOH A . 
W 6 HOH 93  493 186  HOH HOH A . 
W 6 HOH 94  494 1072 HOH HOH A . 
W 6 HOH 95  495 33   HOH HOH A . 
W 6 HOH 96  496 323  HOH HOH A . 
W 6 HOH 97  497 1079 HOH HOH A . 
W 6 HOH 98  498 229  HOH HOH A . 
W 6 HOH 99  499 891  HOH HOH A . 
W 6 HOH 100 500 1063 HOH HOH A . 
W 6 HOH 101 501 1120 HOH HOH A . 
W 6 HOH 102 502 230  HOH HOH A . 
W 6 HOH 103 503 111  HOH HOH A . 
W 6 HOH 104 504 35   HOH HOH A . 
W 6 HOH 105 505 100  HOH HOH A . 
W 6 HOH 106 506 627  HOH HOH A . 
W 6 HOH 107 507 340  HOH HOH A . 
W 6 HOH 108 508 762  HOH HOH A . 
W 6 HOH 109 509 341  HOH HOH A . 
W 6 HOH 110 510 725  HOH HOH A . 
W 6 HOH 111 511 969  HOH HOH A . 
W 6 HOH 112 512 729  HOH HOH A . 
W 6 HOH 113 513 270  HOH HOH A . 
W 6 HOH 114 514 513  HOH HOH A . 
W 6 HOH 115 515 386  HOH HOH A . 
W 6 HOH 116 516 57   HOH HOH A . 
W 6 HOH 117 517 870  HOH HOH A . 
W 6 HOH 118 518 62   HOH HOH A . 
W 6 HOH 119 519 255  HOH HOH A . 
W 6 HOH 120 520 688  HOH HOH A . 
W 6 HOH 121 521 760  HOH HOH A . 
W 6 HOH 122 522 42   HOH HOH A . 
W 6 HOH 123 523 381  HOH HOH A . 
W 6 HOH 124 524 319  HOH HOH A . 
W 6 HOH 125 525 155  HOH HOH A . 
W 6 HOH 126 526 1080 HOH HOH A . 
W 6 HOH 127 527 619  HOH HOH A . 
W 6 HOH 128 528 517  HOH HOH A . 
W 6 HOH 129 529 210  HOH HOH A . 
W 6 HOH 130 530 189  HOH HOH A . 
W 6 HOH 131 531 957  HOH HOH A . 
W 6 HOH 132 532 961  HOH HOH A . 
W 6 HOH 133 533 214  HOH HOH A . 
W 6 HOH 134 534 26   HOH HOH A . 
W 6 HOH 135 535 15   HOH HOH A . 
W 6 HOH 136 536 273  HOH HOH A . 
W 6 HOH 137 537 667  HOH HOH A . 
W 6 HOH 138 538 7    HOH HOH A . 
W 6 HOH 139 539 423  HOH HOH A . 
W 6 HOH 140 540 886  HOH HOH A . 
W 6 HOH 141 541 736  HOH HOH A . 
W 6 HOH 142 542 972  HOH HOH A . 
W 6 HOH 143 543 362  HOH HOH A . 
W 6 HOH 144 544 314  HOH HOH A . 
W 6 HOH 145 545 662  HOH HOH A . 
W 6 HOH 146 546 18   HOH HOH A . 
W 6 HOH 147 547 277  HOH HOH A . 
W 6 HOH 148 548 70   HOH HOH A . 
W 6 HOH 149 549 783  HOH HOH A . 
W 6 HOH 150 550 151  HOH HOH A . 
W 6 HOH 151 551 398  HOH HOH A . 
W 6 HOH 152 552 629  HOH HOH A . 
W 6 HOH 153 553 440  HOH HOH A . 
W 6 HOH 154 554 71   HOH HOH A . 
W 6 HOH 155 555 292  HOH HOH A . 
W 6 HOH 156 556 866  HOH HOH A . 
W 6 HOH 157 557 384  HOH HOH A . 
W 6 HOH 158 558 881  HOH HOH A . 
W 6 HOH 159 559 204  HOH HOH A . 
W 6 HOH 160 560 971  HOH HOH A . 
W 6 HOH 161 561 544  HOH HOH A . 
W 6 HOH 162 562 157  HOH HOH A . 
W 6 HOH 163 563 258  HOH HOH A . 
W 6 HOH 164 564 436  HOH HOH A . 
W 6 HOH 165 565 227  HOH HOH A . 
W 6 HOH 166 566 201  HOH HOH A . 
W 6 HOH 167 567 275  HOH HOH A . 
W 6 HOH 168 568 303  HOH HOH A . 
W 6 HOH 169 569 501  HOH HOH A . 
W 6 HOH 170 570 880  HOH HOH A . 
W 6 HOH 171 571 444  HOH HOH A . 
W 6 HOH 172 572 871  HOH HOH A . 
W 6 HOH 173 573 497  HOH HOH A . 
W 6 HOH 174 574 428  HOH HOH A . 
W 6 HOH 175 575 266  HOH HOH A . 
W 6 HOH 176 576 858  HOH HOH A . 
W 6 HOH 177 577 566  HOH HOH A . 
W 6 HOH 178 578 364  HOH HOH A . 
W 6 HOH 179 579 24   HOH HOH A . 
W 6 HOH 180 580 105  HOH HOH A . 
W 6 HOH 181 581 715  HOH HOH A . 
W 6 HOH 182 582 950  HOH HOH A . 
W 6 HOH 183 583 819  HOH HOH A . 
W 6 HOH 184 584 125  HOH HOH A . 
W 6 HOH 185 585 869  HOH HOH A . 
W 6 HOH 186 586 441  HOH HOH A . 
W 6 HOH 187 587 308  HOH HOH A . 
W 6 HOH 188 588 265  HOH HOH A . 
W 6 HOH 189 589 948  HOH HOH A . 
W 6 HOH 190 590 883  HOH HOH A . 
W 6 HOH 191 591 723  HOH HOH A . 
W 6 HOH 192 592 1066 HOH HOH A . 
W 6 HOH 193 593 703  HOH HOH A . 
W 6 HOH 194 594 738  HOH HOH A . 
W 6 HOH 195 595 1121 HOH HOH A . 
W 6 HOH 196 596 817  HOH HOH A . 
W 6 HOH 197 597 964  HOH HOH A . 
W 6 HOH 198 598 727  HOH HOH A . 
W 6 HOH 199 599 449  HOH HOH A . 
W 6 HOH 200 600 570  HOH HOH A . 
W 6 HOH 201 601 406  HOH HOH A . 
W 6 HOH 202 602 628  HOH HOH A . 
W 6 HOH 203 603 965  HOH HOH A . 
W 6 HOH 204 604 194  HOH HOH A . 
W 6 HOH 205 605 645  HOH HOH A . 
W 6 HOH 206 606 864  HOH HOH A . 
W 6 HOH 207 607 495  HOH HOH A . 
W 6 HOH 208 608 942  HOH HOH A . 
W 6 HOH 209 609 821  HOH HOH A . 
W 6 HOH 210 610 792  HOH HOH A . 
W 6 HOH 211 611 856  HOH HOH A . 
W 6 HOH 212 612 1147 HOH HOH A . 
W 6 HOH 213 613 787  HOH HOH A . 
W 6 HOH 214 614 184  HOH HOH A . 
W 6 HOH 215 615 336  HOH HOH A . 
W 6 HOH 216 616 221  HOH HOH A . 
W 6 HOH 217 617 872  HOH HOH A . 
W 6 HOH 218 618 312  HOH HOH A . 
W 6 HOH 219 619 664  HOH HOH A . 
W 6 HOH 220 620 947  HOH HOH A . 
W 6 HOH 221 621 243  HOH HOH A . 
W 6 HOH 222 622 467  HOH HOH A . 
W 6 HOH 223 623 231  HOH HOH A . 
W 6 HOH 224 624 975  HOH HOH A . 
W 6 HOH 225 625 453  HOH HOH A . 
W 6 HOH 226 626 1071 HOH HOH A . 
W 6 HOH 227 627 958  HOH HOH A . 
W 6 HOH 228 628 1116 HOH HOH A . 
W 6 HOH 229 629 1073 HOH HOH A . 
W 6 HOH 230 630 614  HOH HOH A . 
W 6 HOH 231 631 652  HOH HOH A . 
W 6 HOH 232 632 482  HOH HOH A . 
W 6 HOH 233 633 458  HOH HOH A . 
W 6 HOH 234 634 1085 HOH HOH A . 
W 6 HOH 235 635 757  HOH HOH A . 
W 6 HOH 236 636 857  HOH HOH A . 
W 6 HOH 237 637 873  HOH HOH A . 
W 6 HOH 238 638 397  HOH HOH A . 
W 6 HOH 239 639 960  HOH HOH A . 
W 6 HOH 240 640 878  HOH HOH A . 
W 6 HOH 241 641 943  HOH HOH A . 
W 6 HOH 242 642 602  HOH HOH A . 
W 6 HOH 243 643 877  HOH HOH A . 
W 6 HOH 244 644 1069 HOH HOH A . 
W 6 HOH 245 645 1084 HOH HOH A . 
W 6 HOH 246 646 962  HOH HOH A . 
W 6 HOH 247 647 572  HOH HOH A . 
W 6 HOH 248 648 820  HOH HOH A . 
W 6 HOH 249 649 974  HOH HOH A . 
W 6 HOH 250 650 691  HOH HOH A . 
W 6 HOH 251 651 540  HOH HOH A . 
W 6 HOH 252 652 970  HOH HOH A . 
W 6 HOH 253 653 228  HOH HOH A . 
W 6 HOH 254 654 1126 HOH HOH A . 
W 6 HOH 255 655 940  HOH HOH A . 
W 6 HOH 256 656 1086 HOH HOH A . 
W 6 HOH 257 657 1119 HOH HOH A . 
W 6 HOH 258 658 666  HOH HOH A . 
W 6 HOH 259 659 317  HOH HOH A . 
W 6 HOH 260 660 301  HOH HOH A . 
W 6 HOH 261 661 939  HOH HOH A . 
W 6 HOH 262 662 859  HOH HOH A . 
W 6 HOH 263 663 1061 HOH HOH A . 
W 6 HOH 264 664 1074 HOH HOH A . 
W 6 HOH 265 665 1075 HOH HOH A . 
W 6 HOH 266 666 967  HOH HOH A . 
W 6 HOH 267 667 1125 HOH HOH A . 
W 6 HOH 268 668 1118 HOH HOH A . 
W 6 HOH 269 669 740  HOH HOH A . 
W 6 HOH 270 670 538  HOH HOH A . 
W 6 HOH 271 671 692  HOH HOH A . 
W 6 HOH 272 672 1070 HOH HOH A . 
W 6 HOH 273 673 963  HOH HOH A . 
W 6 HOH 274 674 1117 HOH HOH A . 
W 6 HOH 275 675 378  HOH HOH A . 
W 6 HOH 276 676 595  HOH HOH A . 
W 6 HOH 277 677 887  HOH HOH A . 
W 6 HOH 278 678 937  HOH HOH A . 
W 6 HOH 279 679 889  HOH HOH A . 
W 6 HOH 280 680 938  HOH HOH A . 
W 6 HOH 281 681 524  HOH HOH A . 
W 6 HOH 282 682 769  HOH HOH A . 
W 6 HOH 283 683 542  HOH HOH A . 
W 6 HOH 284 684 885  HOH HOH A . 
W 6 HOH 285 685 1067 HOH HOH A . 
W 6 HOH 286 686 1115 HOH HOH A . 
W 6 HOH 287 687 651  HOH HOH A . 
W 6 HOH 288 688 1114 HOH HOH A . 
W 6 HOH 289 689 949  HOH HOH A . 
X 6 HOH 1   401 360  HOH HOH B . 
X 6 HOH 2   402 956  HOH HOH B . 
X 6 HOH 3   403 483  HOH HOH B . 
X 6 HOH 4   404 1091 HOH HOH B . 
X 6 HOH 5   405 1096 HOH HOH B . 
X 6 HOH 6   406 611  HOH HOH B . 
X 6 HOH 7   407 779  HOH HOH B . 
X 6 HOH 8   408 1060 HOH HOH B . 
X 6 HOH 9   409 520  HOH HOH B . 
X 6 HOH 10  410 1089 HOH HOH B . 
X 6 HOH 11  411 145  HOH HOH B . 
X 6 HOH 12  412 1093 HOH HOH B . 
X 6 HOH 13  413 141  HOH HOH B . 
X 6 HOH 14  414 985  HOH HOH B . 
X 6 HOH 15  415 488  HOH HOH B . 
X 6 HOH 16  416 796  HOH HOH B . 
X 6 HOH 17  417 705  HOH HOH B . 
X 6 HOH 18  418 84   HOH HOH B . 
X 6 HOH 19  419 677  HOH HOH B . 
X 6 HOH 20  420 763  HOH HOH B . 
X 6 HOH 21  421 529  HOH HOH B . 
X 6 HOH 22  422 718  HOH HOH B . 
X 6 HOH 23  423 535  HOH HOH B . 
X 6 HOH 24  424 745  HOH HOH B . 
X 6 HOH 25  425 806  HOH HOH B . 
X 6 HOH 26  426 597  HOH HOH B . 
X 6 HOH 27  427 22   HOH HOH B . 
X 6 HOH 28  428 400  HOH HOH B . 
X 6 HOH 29  429 215  HOH HOH B . 
X 6 HOH 30  430 1087 HOH HOH B . 
X 6 HOH 31  431 416  HOH HOH B . 
X 6 HOH 32  432 1097 HOH HOH B . 
X 6 HOH 33  433 212  HOH HOH B . 
X 6 HOH 34  434 271  HOH HOH B . 
X 6 HOH 35  435 150  HOH HOH B . 
X 6 HOH 36  436 120  HOH HOH B . 
X 6 HOH 37  437 502  HOH HOH B . 
X 6 HOH 38  438 61   HOH HOH B . 
X 6 HOH 39  439 641  HOH HOH B . 
X 6 HOH 40  440 789  HOH HOH B . 
X 6 HOH 41  441 39   HOH HOH B . 
X 6 HOH 42  442 280  HOH HOH B . 
X 6 HOH 43  443 661  HOH HOH B . 
X 6 HOH 44  444 1059 HOH HOH B . 
X 6 HOH 45  445 447  HOH HOH B . 
X 6 HOH 46  446 86   HOH HOH B . 
X 6 HOH 47  447 112  HOH HOH B . 
X 6 HOH 48  448 257  HOH HOH B . 
X 6 HOH 49  449 69   HOH HOH B . 
X 6 HOH 50  450 430  HOH HOH B . 
X 6 HOH 51  451 983  HOH HOH B . 
X 6 HOH 52  452 238  HOH HOH B . 
X 6 HOH 53  453 367  HOH HOH B . 
X 6 HOH 54  454 516  HOH HOH B . 
X 6 HOH 55  455 76   HOH HOH B . 
X 6 HOH 56  456 1058 HOH HOH B . 
X 6 HOH 57  457 460  HOH HOH B . 
X 6 HOH 58  458 165  HOH HOH B . 
X 6 HOH 59  459 515  HOH HOH B . 
X 6 HOH 60  460 790  HOH HOH B . 
X 6 HOH 61  461 53   HOH HOH B . 
X 6 HOH 62  462 435  HOH HOH B . 
X 6 HOH 63  463 206  HOH HOH B . 
X 6 HOH 64  464 823  HOH HOH B . 
X 6 HOH 65  465 77   HOH HOH B . 
X 6 HOH 66  466 429  HOH HOH B . 
X 6 HOH 67  467 103  HOH HOH B . 
X 6 HOH 68  468 550  HOH HOH B . 
X 6 HOH 69  469 604  HOH HOH B . 
X 6 HOH 70  470 149  HOH HOH B . 
X 6 HOH 71  471 191  HOH HOH B . 
X 6 HOH 72  472 643  HOH HOH B . 
X 6 HOH 73  473 134  HOH HOH B . 
X 6 HOH 74  474 707  HOH HOH B . 
X 6 HOH 75  475 346  HOH HOH B . 
X 6 HOH 76  476 984  HOH HOH B . 
X 6 HOH 77  477 895  HOH HOH B . 
X 6 HOH 78  478 795  HOH HOH B . 
X 6 HOH 79  479 40   HOH HOH B . 
X 6 HOH 80  480 97   HOH HOH B . 
X 6 HOH 81  481 747  HOH HOH B . 
X 6 HOH 82  482 320  HOH HOH B . 
X 6 HOH 83  483 724  HOH HOH B . 
X 6 HOH 84  484 286  HOH HOH B . 
X 6 HOH 85  485 712  HOH HOH B . 
X 6 HOH 86  486 290  HOH HOH B . 
X 6 HOH 87  487 75   HOH HOH B . 
X 6 HOH 88  488 668  HOH HOH B . 
X 6 HOH 89  489 64   HOH HOH B . 
X 6 HOH 90  490 764  HOH HOH B . 
X 6 HOH 91  491 425  HOH HOH B . 
X 6 HOH 92  492 188  HOH HOH B . 
X 6 HOH 93  493 814  HOH HOH B . 
X 6 HOH 94  494 202  HOH HOH B . 
X 6 HOH 95  495 598  HOH HOH B . 
X 6 HOH 96  496 93   HOH HOH B . 
X 6 HOH 97  497 987  HOH HOH B . 
X 6 HOH 98  498 129  HOH HOH B . 
X 6 HOH 99  499 264  HOH HOH B . 
X 6 HOH 100 500 946  HOH HOH B . 
X 6 HOH 101 501 153  HOH HOH B . 
X 6 HOH 102 502 477  HOH HOH B . 
X 6 HOH 103 503 284  HOH HOH B . 
X 6 HOH 104 504 85   HOH HOH B . 
X 6 HOH 105 505 476  HOH HOH B . 
X 6 HOH 106 506 1127 HOH HOH B . 
X 6 HOH 107 507 953  HOH HOH B . 
X 6 HOH 108 508 788  HOH HOH B . 
X 6 HOH 109 509 41   HOH HOH B . 
X 6 HOH 110 510 675  HOH HOH B . 
X 6 HOH 111 511 74   HOH HOH B . 
X 6 HOH 112 512 48   HOH HOH B . 
X 6 HOH 113 513 291  HOH HOH B . 
X 6 HOH 114 514 755  HOH HOH B . 
X 6 HOH 115 515 68   HOH HOH B . 
X 6 HOH 116 516 59   HOH HOH B . 
X 6 HOH 117 517 260  HOH HOH B . 
X 6 HOH 118 518 47   HOH HOH B . 
X 6 HOH 119 519 708  HOH HOH B . 
X 6 HOH 120 520 582  HOH HOH B . 
X 6 HOH 121 521 27   HOH HOH B . 
X 6 HOH 122 522 369  HOH HOH B . 
X 6 HOH 123 523 252  HOH HOH B . 
X 6 HOH 124 524 824  HOH HOH B . 
X 6 HOH 125 525 579  HOH HOH B . 
X 6 HOH 126 526 979  HOH HOH B . 
X 6 HOH 127 527 326  HOH HOH B . 
X 6 HOH 128 528 676  HOH HOH B . 
X 6 HOH 129 529 307  HOH HOH B . 
X 6 HOH 130 530 798  HOH HOH B . 
X 6 HOH 131 531 223  HOH HOH B . 
X 6 HOH 132 532 196  HOH HOH B . 
X 6 HOH 133 533 988  HOH HOH B . 
X 6 HOH 134 534 587  HOH HOH B . 
X 6 HOH 135 535 144  HOH HOH B . 
X 6 HOH 136 536 771  HOH HOH B . 
X 6 HOH 137 537 756  HOH HOH B . 
X 6 HOH 138 538 198  HOH HOH B . 
X 6 HOH 139 539 282  HOH HOH B . 
X 6 HOH 140 540 370  HOH HOH B . 
X 6 HOH 141 541 996  HOH HOH B . 
X 6 HOH 142 542 905  HOH HOH B . 
X 6 HOH 143 543 807  HOH HOH B . 
X 6 HOH 144 544 78   HOH HOH B . 
X 6 HOH 145 545 804  HOH HOH B . 
X 6 HOH 146 546 140  HOH HOH B . 
X 6 HOH 147 547 297  HOH HOH B . 
X 6 HOH 148 548 773  HOH HOH B . 
X 6 HOH 149 549 480  HOH HOH B . 
X 6 HOH 150 550 901  HOH HOH B . 
X 6 HOH 151 551 609  HOH HOH B . 
X 6 HOH 152 552 402  HOH HOH B . 
X 6 HOH 153 553 578  HOH HOH B . 
X 6 HOH 154 554 348  HOH HOH B . 
X 6 HOH 155 555 147  HOH HOH B . 
X 6 HOH 156 556 860  HOH HOH B . 
X 6 HOH 157 557 706  HOH HOH B . 
X 6 HOH 158 558 562  HOH HOH B . 
X 6 HOH 159 559 765  HOH HOH B . 
X 6 HOH 160 560 50   HOH HOH B . 
X 6 HOH 161 561 902  HOH HOH B . 
X 6 HOH 162 562 457  HOH HOH B . 
X 6 HOH 163 563 330  HOH HOH B . 
X 6 HOH 164 564 767  HOH HOH B . 
X 6 HOH 165 565 331  HOH HOH B . 
X 6 HOH 166 566 565  HOH HOH B . 
X 6 HOH 167 567 4    HOH HOH B . 
X 6 HOH 168 568 945  HOH HOH B . 
X 6 HOH 169 569 450  HOH HOH B . 
X 6 HOH 170 570 1    HOH HOH B . 
X 6 HOH 171 571 665  HOH HOH B . 
X 6 HOH 172 572 67   HOH HOH B . 
X 6 HOH 173 573 564  HOH HOH B . 
X 6 HOH 174 574 353  HOH HOH B . 
X 6 HOH 175 575 216  HOH HOH B . 
X 6 HOH 176 576 737  HOH HOH B . 
X 6 HOH 177 577 139  HOH HOH B . 
X 6 HOH 178 578 720  HOH HOH B . 
X 6 HOH 179 579 268  HOH HOH B . 
X 6 HOH 180 580 347  HOH HOH B . 
X 6 HOH 181 581 696  HOH HOH B . 
X 6 HOH 182 582 896  HOH HOH B . 
X 6 HOH 183 583 1092 HOH HOH B . 
X 6 HOH 184 584 385  HOH HOH B . 
X 6 HOH 185 585 99   HOH HOH B . 
X 6 HOH 186 586 603  HOH HOH B . 
X 6 HOH 187 587 1095 HOH HOH B . 
X 6 HOH 188 588 427  HOH HOH B . 
X 6 HOH 189 589 315  HOH HOH B . 
X 6 HOH 190 590 351  HOH HOH B . 
X 6 HOH 191 591 649  HOH HOH B . 
X 6 HOH 192 592 512  HOH HOH B . 
X 6 HOH 193 593 816  HOH HOH B . 
X 6 HOH 194 594 826  HOH HOH B . 
X 6 HOH 195 595 815  HOH HOH B . 
X 6 HOH 196 596 554  HOH HOH B . 
X 6 HOH 197 597 166  HOH HOH B . 
X 6 HOH 198 598 669  HOH HOH B . 
X 6 HOH 199 599 185  HOH HOH B . 
X 6 HOH 200 600 658  HOH HOH B . 
X 6 HOH 201 601 511  HOH HOH B . 
X 6 HOH 202 602 537  HOH HOH B . 
X 6 HOH 203 603 994  HOH HOH B . 
X 6 HOH 204 604 305  HOH HOH B . 
X 6 HOH 205 605 162  HOH HOH B . 
X 6 HOH 206 606 171  HOH HOH B . 
X 6 HOH 207 607 521  HOH HOH B . 
X 6 HOH 208 608 466  HOH HOH B . 
X 6 HOH 209 609 349  HOH HOH B . 
X 6 HOH 210 610 812  HOH HOH B . 
X 6 HOH 211 611 541  HOH HOH B . 
X 6 HOH 212 612 1088 HOH HOH B . 
X 6 HOH 213 613 567  HOH HOH B . 
X 6 HOH 214 614 772  HOH HOH B . 
X 6 HOH 215 615 882  HOH HOH B . 
X 6 HOH 216 616 605  HOH HOH B . 
X 6 HOH 217 617 613  HOH HOH B . 
X 6 HOH 218 618 898  HOH HOH B . 
X 6 HOH 219 619 295  HOH HOH B . 
X 6 HOH 220 620 365  HOH HOH B . 
X 6 HOH 221 621 571  HOH HOH B . 
X 6 HOH 222 622 892  HOH HOH B . 
X 6 HOH 223 623 952  HOH HOH B . 
X 6 HOH 224 624 973  HOH HOH B . 
X 6 HOH 225 625 758  HOH HOH B . 
X 6 HOH 226 626 998  HOH HOH B . 
X 6 HOH 227 627 893  HOH HOH B . 
X 6 HOH 228 628 274  HOH HOH B . 
X 6 HOH 229 629 285  HOH HOH B . 
X 6 HOH 230 630 981  HOH HOH B . 
X 6 HOH 231 631 682  HOH HOH B . 
X 6 HOH 232 632 644  HOH HOH B . 
X 6 HOH 233 633 1000 HOH HOH B . 
X 6 HOH 234 634 827  HOH HOH B . 
X 6 HOH 235 635 999  HOH HOH B . 
X 6 HOH 236 636 990  HOH HOH B . 
X 6 HOH 237 637 986  HOH HOH B . 
X 6 HOH 238 638 432  HOH HOH B . 
X 6 HOH 239 639 498  HOH HOH B . 
X 6 HOH 240 640 1122 HOH HOH B . 
X 6 HOH 241 641 404  HOH HOH B . 
X 6 HOH 242 642 1148 HOH HOH B . 
X 6 HOH 243 643 1094 HOH HOH B . 
X 6 HOH 244 644 606  HOH HOH B . 
X 6 HOH 245 645 894  HOH HOH B . 
X 6 HOH 246 646 731  HOH HOH B . 
X 6 HOH 247 647 868  HOH HOH B . 
X 6 HOH 248 648 583  HOH HOH B . 
X 6 HOH 249 649 825  HOH HOH B . 
X 6 HOH 250 650 695  HOH HOH B . 
X 6 HOH 251 651 560  HOH HOH B . 
X 6 HOH 252 652 993  HOH HOH B . 
X 6 HOH 253 653 728  HOH HOH B . 
X 6 HOH 254 654 992  HOH HOH B . 
X 6 HOH 255 655 426  HOH HOH B . 
X 6 HOH 256 656 1098 HOH HOH B . 
X 6 HOH 257 657 897  HOH HOH B . 
X 6 HOH 258 658 586  HOH HOH B . 
X 6 HOH 259 659 240  HOH HOH B . 
X 6 HOH 260 660 951  HOH HOH B . 
X 6 HOH 261 661 343  HOH HOH B . 
X 6 HOH 262 662 685  HOH HOH B . 
X 6 HOH 263 663 684  HOH HOH B . 
X 6 HOH 264 664 433  HOH HOH B . 
X 6 HOH 265 665 403  HOH HOH B . 
X 6 HOH 266 666 1076 HOH HOH B . 
X 6 HOH 267 667 1090 HOH HOH B . 
X 6 HOH 268 668 510  HOH HOH B . 
X 6 HOH 269 669 1123 HOH HOH B . 
X 6 HOH 270 670 372  HOH HOH B . 
X 6 HOH 271 671 722  HOH HOH B . 
X 6 HOH 272 672 545  HOH HOH B . 
X 6 HOH 273 673 500  HOH HOH B . 
X 6 HOH 274 674 533  HOH HOH B . 
X 6 HOH 275 675 469  HOH HOH B . 
X 6 HOH 276 676 431  HOH HOH B . 
X 6 HOH 277 677 1149 HOH HOH B . 
X 6 HOH 278 678 366  HOH HOH B . 
X 6 HOH 279 679 590  HOH HOH B . 
X 6 HOH 280 680 954  HOH HOH B . 
X 6 HOH 281 681 785  HOH HOH B . 
X 6 HOH 282 682 1124 HOH HOH B . 
X 6 HOH 283 683 900  HOH HOH B . 
X 6 HOH 284 684 978  HOH HOH B . 
X 6 HOH 285 685 709  HOH HOH B . 
X 6 HOH 286 686 445  HOH HOH B . 
X 6 HOH 287 687 686  HOH HOH B . 
X 6 HOH 288 688 991  HOH HOH B . 
X 6 HOH 289 689 977  HOH HOH B . 
X 6 HOH 290 690 976  HOH HOH B . 
X 6 HOH 291 691 955  HOH HOH B . 
X 6 HOH 292 692 899  HOH HOH B . 
X 6 HOH 293 693 408  HOH HOH B . 
Y 6 HOH 1   401 680  HOH HOH C . 
Y 6 HOH 2   402 968  HOH HOH C . 
Y 6 HOH 3   403 681  HOH HOH C . 
Y 6 HOH 4   404 1020 HOH HOH C . 
Y 6 HOH 5   405 836  HOH HOH C . 
Y 6 HOH 6   406 638  HOH HOH C . 
Y 6 HOH 7   407 1133 HOH HOH C . 
Y 6 HOH 8   408 434  HOH HOH C . 
Y 6 HOH 9   409 1023 HOH HOH C . 
Y 6 HOH 10  410 833  HOH HOH C . 
Y 6 HOH 11  411 442  HOH HOH C . 
Y 6 HOH 12  412 368  HOH HOH C . 
Y 6 HOH 13  413 199  HOH HOH C . 
Y 6 HOH 14  414 446  HOH HOH C . 
Y 6 HOH 15  415 910  HOH HOH C . 
Y 6 HOH 16  416 108  HOH HOH C . 
Y 6 HOH 17  417 250  HOH HOH C . 
Y 6 HOH 18  418 921  HOH HOH C . 
Y 6 HOH 19  419 179  HOH HOH C . 
Y 6 HOH 20  420 52   HOH HOH C . 
Y 6 HOH 21  421 1104 HOH HOH C . 
Y 6 HOH 22  422 845  HOH HOH C . 
Y 6 HOH 23  423 472  HOH HOH C . 
Y 6 HOH 24  424 383  HOH HOH C . 
Y 6 HOH 25  425 925  HOH HOH C . 
Y 6 HOH 26  426 1134 HOH HOH C . 
Y 6 HOH 27  427 732  HOH HOH C . 
Y 6 HOH 28  428 117  HOH HOH C . 
Y 6 HOH 29  429 226  HOH HOH C . 
Y 6 HOH 30  430 465  HOH HOH C . 
Y 6 HOH 31  431 639  HOH HOH C . 
Y 6 HOH 32  432 1101 HOH HOH C . 
Y 6 HOH 33  433 922  HOH HOH C . 
Y 6 HOH 34  434 219  HOH HOH C . 
Y 6 HOH 35  435 546  HOH HOH C . 
Y 6 HOH 36  436 702  HOH HOH C . 
Y 6 HOH 37  437 830  HOH HOH C . 
Y 6 HOH 38  438 475  HOH HOH C . 
Y 6 HOH 39  439 618  HOH HOH C . 
Y 6 HOH 40  440 923  HOH HOH C . 
Y 6 HOH 41  441 924  HOH HOH C . 
Y 6 HOH 42  442 122  HOH HOH C . 
Y 6 HOH 43  443 777  HOH HOH C . 
Y 6 HOH 44  444 261  HOH HOH C . 
Y 6 HOH 45  445 584  HOH HOH C . 
Y 6 HOH 46  446 592  HOH HOH C . 
Y 6 HOH 47  447 573  HOH HOH C . 
Y 6 HOH 48  448 1132 HOH HOH C . 
Y 6 HOH 49  449 800  HOH HOH C . 
Y 6 HOH 50  450 623  HOH HOH C . 
Y 6 HOH 51  451 784  HOH HOH C . 
Y 6 HOH 52  452 5    HOH HOH C . 
Y 6 HOH 53  453 387  HOH HOH C . 
Y 6 HOH 54  454 518  HOH HOH C . 
Y 6 HOH 55  455 3    HOH HOH C . 
Y 6 HOH 56  456 304  HOH HOH C . 
Y 6 HOH 57  457 485  HOH HOH C . 
Y 6 HOH 58  458 596  HOH HOH C . 
Y 6 HOH 59  459 110  HOH HOH C . 
Y 6 HOH 60  460 838  HOH HOH C . 
Y 6 HOH 61  461 888  HOH HOH C . 
Y 6 HOH 62  462 1102 HOH HOH C . 
Y 6 HOH 63  463 20   HOH HOH C . 
Y 6 HOH 64  464 246  HOH HOH C . 
Y 6 HOH 65  465 287  HOH HOH C . 
Y 6 HOH 66  466 164  HOH HOH C . 
Y 6 HOH 67  467 19   HOH HOH C . 
Y 6 HOH 68  468 102  HOH HOH C . 
Y 6 HOH 69  469 190  HOH HOH C . 
Y 6 HOH 70  470 131  HOH HOH C . 
Y 6 HOH 71  471 563  HOH HOH C . 
Y 6 HOH 72  472 107  HOH HOH C . 
Y 6 HOH 73  473 536  HOH HOH C . 
Y 6 HOH 74  474 778  HOH HOH C . 
Y 6 HOH 75  475 321  HOH HOH C . 
Y 6 HOH 76  476 95   HOH HOH C . 
Y 6 HOH 77  477 531  HOH HOH C . 
Y 6 HOH 78  478 376  HOH HOH C . 
Y 6 HOH 79  479 1013 HOH HOH C . 
Y 6 HOH 80  480 208  HOH HOH C . 
Y 6 HOH 81  481 94   HOH HOH C . 
Y 6 HOH 82  482 527  HOH HOH C . 
Y 6 HOH 83  483 90   HOH HOH C . 
Y 6 HOH 84  484 160  HOH HOH C . 
Y 6 HOH 85  485 744  HOH HOH C . 
Y 6 HOH 86  486 391  HOH HOH C . 
Y 6 HOH 87  487 468  HOH HOH C . 
Y 6 HOH 88  488 399  HOH HOH C . 
Y 6 HOH 89  489 300  HOH HOH C . 
Y 6 HOH 90  490 1008 HOH HOH C . 
Y 6 HOH 91  491 211  HOH HOH C . 
Y 6 HOH 92  492 56   HOH HOH C . 
Y 6 HOH 93  493 915  HOH HOH C . 
Y 6 HOH 94  494 841  HOH HOH C . 
Y 6 HOH 95  495 721  HOH HOH C . 
Y 6 HOH 96  496 548  HOH HOH C . 
Y 6 HOH 97  497 844  HOH HOH C . 
Y 6 HOH 98  498 514  HOH HOH C . 
Y 6 HOH 99  499 752  HOH HOH C . 
Y 6 HOH 100 500 245  HOH HOH C . 
Y 6 HOH 101 501 217  HOH HOH C . 
Y 6 HOH 102 502 443  HOH HOH C . 
Y 6 HOH 103 503 318  HOH HOH C . 
Y 6 HOH 104 504 345  HOH HOH C . 
Y 6 HOH 105 505 259  HOH HOH C . 
Y 6 HOH 106 506 180  HOH HOH C . 
Y 6 HOH 107 507 158  HOH HOH C . 
Y 6 HOH 108 508 356  HOH HOH C . 
Y 6 HOH 109 509 1099 HOH HOH C . 
Y 6 HOH 110 510 54   HOH HOH C . 
Y 6 HOH 111 511 209  HOH HOH C . 
Y 6 HOH 112 512 593  HOH HOH C . 
Y 6 HOH 113 513 119  HOH HOH C . 
Y 6 HOH 114 514 1033 HOH HOH C . 
Y 6 HOH 115 515 654  HOH HOH C . 
Y 6 HOH 116 516 13   HOH HOH C . 
Y 6 HOH 117 517 306  HOH HOH C . 
Y 6 HOH 118 518 754  HOH HOH C . 
Y 6 HOH 119 519 490  HOH HOH C . 
Y 6 HOH 120 520 914  HOH HOH C . 
Y 6 HOH 121 521 172  HOH HOH C . 
Y 6 HOH 122 522 412  HOH HOH C . 
Y 6 HOH 123 523 401  HOH HOH C . 
Y 6 HOH 124 524 569  HOH HOH C . 
Y 6 HOH 125 525 982  HOH HOH C . 
Y 6 HOH 126 526 45   HOH HOH C . 
Y 6 HOH 127 527 748  HOH HOH C . 
Y 6 HOH 128 528 14   HOH HOH C . 
Y 6 HOH 129 529 837  HOH HOH C . 
Y 6 HOH 130 530 626  HOH HOH C . 
Y 6 HOH 131 531 834  HOH HOH C . 
Y 6 HOH 132 532 133  HOH HOH C . 
Y 6 HOH 133 533 32   HOH HOH C . 
Y 6 HOH 134 534 448  HOH HOH C . 
Y 6 HOH 135 535 617  HOH HOH C . 
Y 6 HOH 136 536 396  HOH HOH C . 
Y 6 HOH 137 537 829  HOH HOH C . 
Y 6 HOH 138 538 862  HOH HOH C . 
Y 6 HOH 139 539 73   HOH HOH C . 
Y 6 HOH 140 540 473  HOH HOH C . 
Y 6 HOH 141 541 768  HOH HOH C . 
Y 6 HOH 142 542 701  HOH HOH C . 
Y 6 HOH 143 543 409  HOH HOH C . 
Y 6 HOH 144 544 233  HOH HOH C . 
Y 6 HOH 145 545 1012 HOH HOH C . 
Y 6 HOH 146 546 704  HOH HOH C . 
Y 6 HOH 147 547 912  HOH HOH C . 
Y 6 HOH 148 548 493  HOH HOH C . 
Y 6 HOH 149 549 421  HOH HOH C . 
Y 6 HOH 150 550 630  HOH HOH C . 
Y 6 HOH 151 551 44   HOH HOH C . 
Y 6 HOH 152 552 213  HOH HOH C . 
Y 6 HOH 153 553 167  HOH HOH C . 
Y 6 HOH 154 554 1105 HOH HOH C . 
Y 6 HOH 155 555 23   HOH HOH C . 
Y 6 HOH 156 556 928  HOH HOH C . 
Y 6 HOH 157 557 1029 HOH HOH C . 
Y 6 HOH 158 558 1108 HOH HOH C . 
Y 6 HOH 159 559 244  HOH HOH C . 
Y 6 HOH 160 560 687  HOH HOH C . 
Y 6 HOH 161 561 241  HOH HOH C . 
Y 6 HOH 162 562 121  HOH HOH C . 
Y 6 HOH 163 563 1128 HOH HOH C . 
Y 6 HOH 164 564 218  HOH HOH C . 
Y 6 HOH 165 565 492  HOH HOH C . 
Y 6 HOH 166 566 786  HOH HOH C . 
Y 6 HOH 167 567 642  HOH HOH C . 
Y 6 HOH 168 568 711  HOH HOH C . 
Y 6 HOH 169 569 168  HOH HOH C . 
Y 6 HOH 170 570 499  HOH HOH C . 
Y 6 HOH 171 571 407  HOH HOH C . 
Y 6 HOH 172 572 913  HOH HOH C . 
Y 6 HOH 173 573 159  HOH HOH C . 
Y 6 HOH 174 574 1017 HOH HOH C . 
Y 6 HOH 175 575 361  HOH HOH C . 
Y 6 HOH 176 576 279  HOH HOH C . 
Y 6 HOH 177 577 101  HOH HOH C . 
Y 6 HOH 178 578 161  HOH HOH C . 
Y 6 HOH 179 579 749  HOH HOH C . 
Y 6 HOH 180 580 328  HOH HOH C . 
Y 6 HOH 181 581 577  HOH HOH C . 
Y 6 HOH 182 582 439  HOH HOH C . 
Y 6 HOH 183 583 236  HOH HOH C . 
Y 6 HOH 184 584 1019 HOH HOH C . 
Y 6 HOH 185 585 357  HOH HOH C . 
Y 6 HOH 186 586 846  HOH HOH C . 
Y 6 HOH 187 587 1082 HOH HOH C . 
Y 6 HOH 188 588 464  HOH HOH C . 
Y 6 HOH 189 589 842  HOH HOH C . 
Y 6 HOH 190 590 780  HOH HOH C . 
Y 6 HOH 191 591 235  HOH HOH C . 
Y 6 HOH 192 592 248  HOH HOH C . 
Y 6 HOH 193 593 523  HOH HOH C . 
Y 6 HOH 194 594 920  HOH HOH C . 
Y 6 HOH 195 595 410  HOH HOH C . 
Y 6 HOH 196 596 803  HOH HOH C . 
Y 6 HOH 197 597 698  HOH HOH C . 
Y 6 HOH 198 598 278  HOH HOH C . 
Y 6 HOH 199 599 813  HOH HOH C . 
Y 6 HOH 200 600 522  HOH HOH C . 
Y 6 HOH 201 601 840  HOH HOH C . 
Y 6 HOH 202 602 549  HOH HOH C . 
Y 6 HOH 203 603 674  HOH HOH C . 
Y 6 HOH 204 604 354  HOH HOH C . 
Y 6 HOH 205 605 615  HOH HOH C . 
Y 6 HOH 206 606 1024 HOH HOH C . 
Y 6 HOH 207 607 607  HOH HOH C . 
Y 6 HOH 208 608 932  HOH HOH C . 
Y 6 HOH 209 609 926  HOH HOH C . 
Y 6 HOH 210 610 997  HOH HOH C . 
Y 6 HOH 211 611 843  HOH HOH C . 
Y 6 HOH 212 612 759  HOH HOH C . 
Y 6 HOH 213 613 417  HOH HOH C . 
Y 6 HOH 214 614 672  HOH HOH C . 
Y 6 HOH 215 615 222  HOH HOH C . 
Y 6 HOH 216 616 995  HOH HOH C . 
Y 6 HOH 217 617 916  HOH HOH C . 
Y 6 HOH 218 618 474  HOH HOH C . 
Y 6 HOH 219 619 309  HOH HOH C . 
Y 6 HOH 220 620 1100 HOH HOH C . 
Y 6 HOH 221 621 861  HOH HOH C . 
Y 6 HOH 222 622 832  HOH HOH C . 
Y 6 HOH 223 623 1032 HOH HOH C . 
Y 6 HOH 224 624 418  HOH HOH C . 
Y 6 HOH 225 625 1026 HOH HOH C . 
Y 6 HOH 226 626 656  HOH HOH C . 
Y 6 HOH 227 627 352  HOH HOH C . 
Y 6 HOH 228 628 1129 HOH HOH C . 
Y 6 HOH 229 629 1015 HOH HOH C . 
Y 6 HOH 230 630 1018 HOH HOH C . 
Y 6 HOH 231 631 1031 HOH HOH C . 
Y 6 HOH 232 632 478  HOH HOH C . 
Y 6 HOH 233 633 839  HOH HOH C . 
Y 6 HOH 234 634 288  HOH HOH C . 
Y 6 HOH 235 635 835  HOH HOH C . 
Y 6 HOH 236 636 847  HOH HOH C . 
Y 6 HOH 237 637 1030 HOH HOH C . 
Y 6 HOH 238 638 1150 HOH HOH C . 
Y 6 HOH 239 639 1016 HOH HOH C . 
Y 6 HOH 240 640 931  HOH HOH C . 
Y 6 HOH 241 641 1021 HOH HOH C . 
Y 6 HOH 242 642 911  HOH HOH C . 
Y 6 HOH 243 643 625  HOH HOH C . 
Y 6 HOH 244 644 863  HOH HOH C . 
Y 6 HOH 245 645 927  HOH HOH C . 
Y 6 HOH 246 646 933  HOH HOH C . 
Y 6 HOH 247 647 1009 HOH HOH C . 
Y 6 HOH 248 648 1083 HOH HOH C . 
Y 6 HOH 249 649 909  HOH HOH C . 
Y 6 HOH 250 650 481  HOH HOH C . 
Y 6 HOH 251 651 1131 HOH HOH C . 
Y 6 HOH 252 652 766  HOH HOH C . 
Y 6 HOH 253 653 1107 HOH HOH C . 
Y 6 HOH 254 654 907  HOH HOH C . 
Y 6 HOH 255 655 743  HOH HOH C . 
Y 6 HOH 256 656 650  HOH HOH C . 
Y 6 HOH 257 657 670  HOH HOH C . 
Y 6 HOH 258 658 918  HOH HOH C . 
Y 6 HOH 259 659 831  HOH HOH C . 
Y 6 HOH 260 660 694  HOH HOH C . 
Y 6 HOH 261 661 689  HOH HOH C . 
Y 6 HOH 262 662 1106 HOH HOH C . 
Y 6 HOH 263 663 908  HOH HOH C . 
Y 6 HOH 264 664 109  HOH HOH C . 
Y 6 HOH 265 665 359  HOH HOH C . 
Y 6 HOH 266 666 1028 HOH HOH C . 
Y 6 HOH 267 667 1011 HOH HOH C . 
Y 6 HOH 268 668 594  HOH HOH C . 
Y 6 HOH 269 669 934  HOH HOH C . 
Y 6 HOH 270 670 1025 HOH HOH C . 
Y 6 HOH 271 671 1014 HOH HOH C . 
Y 6 HOH 272 672 929  HOH HOH C . 
Y 6 HOH 273 673 917  HOH HOH C . 
Y 6 HOH 274 674 462  HOH HOH C . 
Y 6 HOH 275 675 1010 HOH HOH C . 
Z 6 HOH 1   401 1004 HOH HOH D . 
Z 6 HOH 2   402 254  HOH HOH D . 
Z 6 HOH 3   403 371  HOH HOH D . 
Z 6 HOH 4   404 801  HOH HOH D . 
Z 6 HOH 5   405 1041 HOH HOH D . 
Z 6 HOH 6   406 322  HOH HOH D . 
Z 6 HOH 7   407 503  HOH HOH D . 
Z 6 HOH 8   408 558  HOH HOH D . 
Z 6 HOH 9   409 853  HOH HOH D . 
Z 6 HOH 10  410 1007 HOH HOH D . 
Z 6 HOH 11  411 775  HOH HOH D . 
Z 6 HOH 12  412 714  HOH HOH D . 
Z 6 HOH 13  413 379  HOH HOH D . 
Z 6 HOH 14  414 657  HOH HOH D . 
Z 6 HOH 15  415 414  HOH HOH D . 
Z 6 HOH 16  416 734  HOH HOH D . 
Z 6 HOH 17  417 276  HOH HOH D . 
Z 6 HOH 18  418 671  HOH HOH D . 
Z 6 HOH 19  419 1111 HOH HOH D . 
Z 6 HOH 20  420 989  HOH HOH D . 
Z 6 HOH 21  421 9    HOH HOH D . 
Z 6 HOH 22  422 575  HOH HOH D . 
Z 6 HOH 23  423 716  HOH HOH D . 
Z 6 HOH 24  424 588  HOH HOH D . 
Z 6 HOH 25  425 1112 HOH HOH D . 
Z 6 HOH 26  426 730  HOH HOH D . 
Z 6 HOH 27  427 422  HOH HOH D . 
Z 6 HOH 28  428 183  HOH HOH D . 
Z 6 HOH 29  429 98   HOH HOH D . 
Z 6 HOH 30  430 380  HOH HOH D . 
Z 6 HOH 31  431 338  HOH HOH D . 
Z 6 HOH 32  432 187  HOH HOH D . 
Z 6 HOH 33  433 424  HOH HOH D . 
Z 6 HOH 34  434 848  HOH HOH D . 
Z 6 HOH 35  435 903  HOH HOH D . 
Z 6 HOH 36  436 1110 HOH HOH D . 
Z 6 HOH 37  437 169  HOH HOH D . 
Z 6 HOH 38  438 293  HOH HOH D . 
Z 6 HOH 39  439 89   HOH HOH D . 
Z 6 HOH 40  440 63   HOH HOH D . 
Z 6 HOH 41  441 487  HOH HOH D . 
Z 6 HOH 42  442 294  HOH HOH D . 
Z 6 HOH 43  443 1003 HOH HOH D . 
Z 6 HOH 44  444 919  HOH HOH D . 
Z 6 HOH 45  445 906  HOH HOH D . 
Z 6 HOH 46  446 733  HOH HOH D . 
Z 6 HOH 47  447 1055 HOH HOH D . 
Z 6 HOH 48  448 272  HOH HOH D . 
Z 6 HOH 49  449 247  HOH HOH D . 
Z 6 HOH 50  450 302  HOH HOH D . 
Z 6 HOH 51  451 616  HOH HOH D . 
Z 6 HOH 52  452 809  HOH HOH D . 
Z 6 HOH 53  453 1145 HOH HOH D . 
Z 6 HOH 54  454 580  HOH HOH D . 
Z 6 HOH 55  455 11   HOH HOH D . 
Z 6 HOH 56  456 263  HOH HOH D . 
Z 6 HOH 57  457 1130 HOH HOH D . 
Z 6 HOH 58  458 405  HOH HOH D . 
Z 6 HOH 59  459 82   HOH HOH D . 
Z 6 HOH 60  460 123  HOH HOH D . 
Z 6 HOH 61  461 38   HOH HOH D . 
Z 6 HOH 62  462 420  HOH HOH D . 
Z 6 HOH 63  463 143  HOH HOH D . 
Z 6 HOH 64  464 678  HOH HOH D . 
Z 6 HOH 65  465 142  HOH HOH D . 
Z 6 HOH 66  466 116  HOH HOH D . 
Z 6 HOH 67  467 31   HOH HOH D . 
Z 6 HOH 68  468 316  HOH HOH D . 
Z 6 HOH 69  469 170  HOH HOH D . 
Z 6 HOH 70  470 329  HOH HOH D . 
Z 6 HOH 71  471 173  HOH HOH D . 
Z 6 HOH 72  472 193  HOH HOH D . 
Z 6 HOH 73  473 132  HOH HOH D . 
Z 6 HOH 74  474 136  HOH HOH D . 
Z 6 HOH 75  475 29   HOH HOH D . 
Z 6 HOH 76  476 791  HOH HOH D . 
Z 6 HOH 77  477 904  HOH HOH D . 
Z 6 HOH 78  478 350  HOH HOH D . 
Z 6 HOH 79  479 137  HOH HOH D . 
Z 6 HOH 80  480 66   HOH HOH D . 
Z 6 HOH 81  481 543  HOH HOH D . 
Z 6 HOH 82  482 547  HOH HOH D . 
Z 6 HOH 83  483 128  HOH HOH D . 
Z 6 HOH 84  484 2    HOH HOH D . 
Z 6 HOH 85  485 504  HOH HOH D . 
Z 6 HOH 86  486 203  HOH HOH D . 
Z 6 HOH 87  487 413  HOH HOH D . 
Z 6 HOH 88  488 525  HOH HOH D . 
Z 6 HOH 89  489 25   HOH HOH D . 
Z 6 HOH 90  490 34   HOH HOH D . 
Z 6 HOH 91  491 37   HOH HOH D . 
Z 6 HOH 92  492 646  HOH HOH D . 
Z 6 HOH 93  493 1062 HOH HOH D . 
Z 6 HOH 94  494 88   HOH HOH D . 
Z 6 HOH 95  495 479  HOH HOH D . 
Z 6 HOH 96  496 220  HOH HOH D . 
Z 6 HOH 97  497 719  HOH HOH D . 
Z 6 HOH 98  498 395  HOH HOH D . 
Z 6 HOH 99  499 49   HOH HOH D . 
Z 6 HOH 100 500 81   HOH HOH D . 
Z 6 HOH 101 501 46   HOH HOH D . 
Z 6 HOH 102 502 60   HOH HOH D . 
Z 6 HOH 103 503 620  HOH HOH D . 
Z 6 HOH 104 504 127  HOH HOH D . 
Z 6 HOH 105 505 648  HOH HOH D . 
Z 6 HOH 106 506 1109 HOH HOH D . 
Z 6 HOH 107 507 79   HOH HOH D . 
Z 6 HOH 108 508 509  HOH HOH D . 
Z 6 HOH 109 509 631  HOH HOH D . 
Z 6 HOH 110 510 327  HOH HOH D . 
Z 6 HOH 111 511 634  HOH HOH D . 
Z 6 HOH 112 512 8    HOH HOH D . 
Z 6 HOH 113 513 181  HOH HOH D . 
Z 6 HOH 114 514 373  HOH HOH D . 
Z 6 HOH 115 515 810  HOH HOH D . 
Z 6 HOH 116 516 849  HOH HOH D . 
Z 6 HOH 117 517 805  HOH HOH D . 
Z 6 HOH 118 518 811  HOH HOH D . 
Z 6 HOH 119 519 197  HOH HOH D . 
Z 6 HOH 120 520 324  HOH HOH D . 
Z 6 HOH 121 521 438  HOH HOH D . 
Z 6 HOH 122 522 1053 HOH HOH D . 
Z 6 HOH 123 523 124  HOH HOH D . 
Z 6 HOH 124 524 600  HOH HOH D . 
Z 6 HOH 125 525 135  HOH HOH D . 
Z 6 HOH 126 526 1143 HOH HOH D . 
Z 6 HOH 127 527 1049 HOH HOH D . 
Z 6 HOH 128 528 256  HOH HOH D . 
Z 6 HOH 129 529 154  HOH HOH D . 
Z 6 HOH 130 530 454  HOH HOH D . 
Z 6 HOH 131 531 735  HOH HOH D . 
Z 6 HOH 132 532 556  HOH HOH D . 
Z 6 HOH 133 533 653  HOH HOH D . 
Z 6 HOH 134 534 114  HOH HOH D . 
Z 6 HOH 135 535 552  HOH HOH D . 
Z 6 HOH 136 536 58   HOH HOH D . 
Z 6 HOH 137 537 337  HOH HOH D . 
Z 6 HOH 138 538 178  HOH HOH D . 
Z 6 HOH 139 539 1035 HOH HOH D . 
Z 6 HOH 140 540 505  HOH HOH D . 
Z 6 HOH 141 541 232  HOH HOH D . 
Z 6 HOH 142 542 461  HOH HOH D . 
Z 6 HOH 143 543 530  HOH HOH D . 
Z 6 HOH 144 544 342  HOH HOH D . 
Z 6 HOH 145 545 175  HOH HOH D . 
Z 6 HOH 146 546 1037 HOH HOH D . 
Z 6 HOH 147 547 612  HOH HOH D . 
Z 6 HOH 148 548 269  HOH HOH D . 
Z 6 HOH 149 549 794  HOH HOH D . 
Z 6 HOH 150 550 486  HOH HOH D . 
Z 6 HOH 151 551 507  HOH HOH D . 
Z 6 HOH 152 552 344  HOH HOH D . 
Z 6 HOH 153 553 83   HOH HOH D . 
Z 6 HOH 154 554 355  HOH HOH D . 
Z 6 HOH 155 555 459  HOH HOH D . 
Z 6 HOH 156 556 471  HOH HOH D . 
Z 6 HOH 157 557 310  HOH HOH D . 
Z 6 HOH 158 558 118  HOH HOH D . 
Z 6 HOH 159 559 519  HOH HOH D . 
Z 6 HOH 160 560 21   HOH HOH D . 
Z 6 HOH 161 561 1135 HOH HOH D . 
Z 6 HOH 162 562 299  HOH HOH D . 
Z 6 HOH 163 563 489  HOH HOH D . 
Z 6 HOH 164 564 411  HOH HOH D . 
Z 6 HOH 165 565 1022 HOH HOH D . 
Z 6 HOH 166 566 624  HOH HOH D . 
Z 6 HOH 167 567 608  HOH HOH D . 
Z 6 HOH 168 568 16   HOH HOH D . 
Z 6 HOH 169 569 660  HOH HOH D . 
Z 6 HOH 170 570 1006 HOH HOH D . 
Z 6 HOH 171 571 363  HOH HOH D . 
Z 6 HOH 172 572 1034 HOH HOH D . 
Z 6 HOH 173 573 637  HOH HOH D . 
Z 6 HOH 174 574 599  HOH HOH D . 
Z 6 HOH 175 575 568  HOH HOH D . 
Z 6 HOH 176 576 267  HOH HOH D . 
Z 6 HOH 177 577 65   HOH HOH D . 
Z 6 HOH 178 578 138  HOH HOH D . 
Z 6 HOH 179 579 585  HOH HOH D . 
Z 6 HOH 180 580 392  HOH HOH D . 
Z 6 HOH 181 581 508  HOH HOH D . 
Z 6 HOH 182 582 935  HOH HOH D . 
Z 6 HOH 183 583 43   HOH HOH D . 
Z 6 HOH 184 584 1142 HOH HOH D . 
Z 6 HOH 185 585 375  HOH HOH D . 
Z 6 HOH 186 586 470  HOH HOH D . 
Z 6 HOH 187 587 390  HOH HOH D . 
Z 6 HOH 188 588 1044 HOH HOH D . 
Z 6 HOH 189 589 463  HOH HOH D . 
Z 6 HOH 190 590 311  HOH HOH D . 
Z 6 HOH 191 591 553  HOH HOH D . 
Z 6 HOH 192 592 697  HOH HOH D . 
Z 6 HOH 193 593 332  HOH HOH D . 
Z 6 HOH 194 594 551  HOH HOH D . 
Z 6 HOH 195 595 774  HOH HOH D . 
Z 6 HOH 196 596 152  HOH HOH D . 
Z 6 HOH 197 597 632  HOH HOH D . 
Z 6 HOH 198 598 237  HOH HOH D . 
Z 6 HOH 199 599 1047 HOH HOH D . 
Z 6 HOH 200 600 207  HOH HOH D . 
Z 6 HOH 201 601 854  HOH HOH D . 
Z 6 HOH 202 602 296  HOH HOH D . 
Z 6 HOH 203 603 532  HOH HOH D . 
Z 6 HOH 204 604 742  HOH HOH D . 
Z 6 HOH 205 605 1137 HOH HOH D . 
Z 6 HOH 206 606 557  HOH HOH D . 
Z 6 HOH 207 607 177  HOH HOH D . 
Z 6 HOH 208 608 358  HOH HOH D . 
Z 6 HOH 209 609 1054 HOH HOH D . 
Z 6 HOH 210 610 633  HOH HOH D . 
Z 6 HOH 211 611 770  HOH HOH D . 
Z 6 HOH 212 612 1140 HOH HOH D . 
Z 6 HOH 213 613 980  HOH HOH D . 
Z 6 HOH 214 614 389  HOH HOH D . 
Z 6 HOH 215 615 1050 HOH HOH D . 
Z 6 HOH 216 616 325  HOH HOH D . 
Z 6 HOH 217 617 1042 HOH HOH D . 
Z 6 HOH 218 618 713  HOH HOH D . 
Z 6 HOH 219 619 1043 HOH HOH D . 
Z 6 HOH 220 620 225  HOH HOH D . 
Z 6 HOH 221 621 739  HOH HOH D . 
Z 6 HOH 222 622 1141 HOH HOH D . 
Z 6 HOH 223 623 1139 HOH HOH D . 
Z 6 HOH 224 624 576  HOH HOH D . 
Z 6 HOH 225 625 700  HOH HOH D . 
Z 6 HOH 226 626 1146 HOH HOH D . 
Z 6 HOH 227 627 415  HOH HOH D . 
Z 6 HOH 228 628 750  HOH HOH D . 
Z 6 HOH 229 629 852  HOH HOH D . 
Z 6 HOH 230 630 850  HOH HOH D . 
Z 6 HOH 231 631 239  HOH HOH D . 
Z 6 HOH 232 632 506  HOH HOH D . 
Z 6 HOH 233 633 621  HOH HOH D . 
Z 6 HOH 234 634 437  HOH HOH D . 
Z 6 HOH 235 635 930  HOH HOH D . 
Z 6 HOH 236 636 526  HOH HOH D . 
Z 6 HOH 237 637 419  HOH HOH D . 
Z 6 HOH 238 638 1136 HOH HOH D . 
Z 6 HOH 239 639 797  HOH HOH D . 
Z 6 HOH 240 640 828  HOH HOH D . 
Z 6 HOH 241 641 561  HOH HOH D . 
Z 6 HOH 242 642 1138 HOH HOH D . 
Z 6 HOH 243 643 1005 HOH HOH D . 
Z 6 HOH 244 644 281  HOH HOH D . 
Z 6 HOH 245 645 148  HOH HOH D . 
Z 6 HOH 246 646 622  HOH HOH D . 
Z 6 HOH 247 647 1045 HOH HOH D . 
Z 6 HOH 248 648 782  HOH HOH D . 
Z 6 HOH 249 649 635  HOH HOH D . 
Z 6 HOH 250 650 339  HOH HOH D . 
Z 6 HOH 251 651 1036 HOH HOH D . 
Z 6 HOH 252 652 1027 HOH HOH D . 
Z 6 HOH 253 653 1144 HOH HOH D . 
Z 6 HOH 254 654 659  HOH HOH D . 
Z 6 HOH 255 655 1039 HOH HOH D . 
Z 6 HOH 256 656 693  HOH HOH D . 
Z 6 HOH 257 657 1052 HOH HOH D . 
Z 6 HOH 258 658 717  HOH HOH D . 
Z 6 HOH 259 659 1103 HOH HOH D . 
Z 6 HOH 260 660 555  HOH HOH D . 
Z 6 HOH 261 661 1046 HOH HOH D . 
Z 6 HOH 262 662 253  HOH HOH D . 
Z 6 HOH 263 663 851  HOH HOH D . 
Z 6 HOH 264 664 451  HOH HOH D . 
Z 6 HOH 265 665 746  HOH HOH D . 
Z 6 HOH 266 666 1057 HOH HOH D . 
Z 6 HOH 267 667 1048 HOH HOH D . 
Z 6 HOH 268 668 1040 HOH HOH D . 
Z 6 HOH 269 669 528  HOH HOH D . 
Z 6 HOH 270 670 456  HOH HOH D . 
Z 6 HOH 271 671 1056 HOH HOH D . 
Z 6 HOH 272 672 690  HOH HOH D . 
Z 6 HOH 273 673 753  HOH HOH D . 
Z 6 HOH 274 674 581  HOH HOH D . 
Z 6 HOH 275 675 1038 HOH HOH D . 
Z 6 HOH 276 676 655  HOH HOH D . 
Z 6 HOH 277 677 394  HOH HOH D . 
Z 6 HOH 278 678 574  HOH HOH D . 
Z 6 HOH 279 679 751  HOH HOH D . 
Z 6 HOH 280 680 494  HOH HOH D . 
Z 6 HOH 281 681 192  HOH HOH D . 
Z 6 HOH 282 682 1113 HOH HOH D . 
Z 6 HOH 283 683 496  HOH HOH D . 
Z 6 HOH 284 684 539  HOH HOH D . 
Z 6 HOH 285 685 799  HOH HOH D . 
Z 6 HOH 286 686 741  HOH HOH D . 
Z 6 HOH 287 687 251  HOH HOH D . 
Z 6 HOH 288 688 1051 HOH HOH D . 
Z 6 HOH 289 689 776  HOH HOH D . 
Z 6 HOH 290 690 683  HOH HOH D . 
Z 6 HOH 291 691 726  HOH HOH D . 
Z 6 HOH 292 692 1001 HOH HOH D . 
Z 6 HOH 293 693 1002 HOH HOH D . 
# 
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 extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? 3.10 2 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? XDS         ? ? ? .    3 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? SCALA       ? ? ? .    4 
? phasing           ? ? ? ? ? ? ? ? ? ? ? MOLREP      ? ? ? .    5 
? 'model building'  ? ? ? ? ? ? ? ? ? ? ? Coot        ? ? ? .    6 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   108.650 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     6R6Y 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     77.335 
_cell.length_a_esd                 ? 
_cell.length_b                     74.192 
_cell.length_b_esd                 ? 
_cell.length_c                     91.634 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_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                         6R6Y 
_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                   6R6Y 
_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            2.08 
_exptl_crystal.density_method              ? 
_exptl_crystal.density_percent_sol         40.90 
_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                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2014-01-08 
_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   0.97552 
_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                        'PETRA III, EMBL c/o DESY BEAMLINE P14 (MX2)' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97552 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   'P14 (MX2)' 
_diffrn_source.pdbx_synchrotron_site       'PETRA III, EMBL c/o DESY' 
# 
_reflns.B_iso_Wilson_estimate            ? 
_reflns.entry_id                         6R6Y 
_reflns.data_reduction_details           ? 
_reflns.data_reduction_method            ? 
_reflns.d_resolution_high                1.380 
_reflns.d_resolution_low                 74.192 
_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                       198797 
_reflns.number_obs                       198797 
_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             98.800 
_reflns.R_free_details                   ? 
_reflns.Rmerge_F_all                     ? 
_reflns.Rmerge_F_obs                     ? 
_reflns.Friedel_coverage                 ? 
_reflns.number_gt                        ? 
_reflns.threshold_expression             ? 
_reflns.pdbx_redundancy                  6.900 
_reflns.pdbx_Rmerge_I_obs                ? 
_reflns.pdbx_Rmerge_I_all                ? 
_reflns.pdbx_Rsym_value                  0.049 
_reflns.pdbx_netI_over_av_sigmaI         7.250 
_reflns.pdbx_netI_over_sigmaI            18.100 
_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                  0.059 
_reflns.pdbx_Rpim_I_all                  0.022 
_reflns.pdbx_d_opt                       ? 
_reflns.pdbx_number_measured_all         1363773 
_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 
1.380 1.450  ? 2.1  ? ? ? ? 29001 98.800 ? ? ? ? 0.343 ? ? ? ? ? ? ? ? 6.700 0.343 ? ? ? 0.406 0.156 ? 1  1 ? ? 
1.450 1.540  ? 3.1  ? ? ? ? 27346 98.800 ? ? ? ? 0.224 ? ? ? ? ? ? ? ? 6.800 0.224 ? ? ? 0.266 0.102 ? 2  1 ? ? 
1.540 1.650  ? 4.8  ? ? ? ? 25744 98.700 ? ? ? ? 0.149 ? ? ? ? ? ? ? ? 6.800 0.149 ? ? ? 0.179 0.069 ? 3  1 ? ? 
1.650 1.780  ? 7.1  ? ? ? ? 23882 98.700 ? ? ? ? 0.100 ? ? ? ? ? ? ? ? 6.800 0.100 ? ? ? 0.121 0.046 ? 4  1 ? ? 
1.780 1.950  ? 10.0 ? ? ? ? 21958 98.100 ? ? ? ? 0.067 ? ? ? ? ? ? ? ? 6.800 0.067 ? ? ? 0.082 0.031 ? 5  1 ? ? 
1.950 2.180  ? 12.6 ? ? ? ? 20021 99.000 ? ? ? ? 0.050 ? ? ? ? ? ? ? ? 7.000 0.050 ? ? ? 0.061 0.023 ? 6  1 ? ? 
2.180 2.520  ? 14.0 ? ? ? ? 17727 99.400 ? ? ? ? 0.043 ? ? ? ? ? ? ? ? 7.000 0.043 ? ? ? 0.053 0.020 ? 7  1 ? ? 
2.520 3.090  ? 14.7 ? ? ? ? 15065 99.400 ? ? ? ? 0.038 ? ? ? ? ? ? ? ? 7.000 0.038 ? ? ? 0.046 0.018 ? 8  1 ? ? 
3.090 4.360  ? 15.3 ? ? ? ? 11624 99.000 ? ? ? ? 0.033 ? ? ? ? ? ? ? ? 7.000 0.033 ? ? ? 0.039 0.015 ? 9  1 ? ? 
4.360 74.192 ? 11.6 ? ? ? ? 6429  98.500 ? ? ? ? 0.032 ? ? ? ? ? ? ? ? 6.800 0.032 ? ? ? 0.039 0.015 ? 10 1 ? ? 
# 
_refine.aniso_B[1][1]                            -0.2700 
_refine.aniso_B[1][2]                            0.0000 
_refine.aniso_B[1][3]                            0.1600 
_refine.aniso_B[2][2]                            -0.0600 
_refine.aniso_B[2][3]                            0.0000 
_refine.aniso_B[3][3]                            0.1900 
_refine.B_iso_max                                64.890 
_refine.B_iso_mean                               17.0663 
_refine.B_iso_min                                5.400 
_refine.correlation_coeff_Fo_to_Fc               0.9730 
_refine.correlation_coeff_Fo_to_Fc_free          0.9650 
_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                                 6R6Y 
_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                            1.3800 
_refine.ls_d_res_low                             73.2800 
_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                     198753 
_refine.ls_number_reflns_R_free                  19765 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.7300 
_refine.ls_percent_reflns_R_free                 9.9000 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1641 
_refine.ls_R_factor_R_free                       0.1873 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1616 
_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                       0.0620 
_refine.pdbx_overall_ESU_R_Free                  0.0630 
_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             0.0618 
_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                       1.3800 
_refine_hist.d_res_low                        73.2800 
_refine_hist.number_atoms_solvent             1150 
_refine_hist.number_atoms_total               9680 
_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        8390 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         140 
_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' ? 0.013  0.012  9027  ? r_bond_refined_d       ? ? 
'X-RAY DIFFRACTION' ? 1.943  1.652  12317 ? r_angle_refined_deg    ? ? 
'X-RAY DIFFRACTION' ? 7.079  5.000  1090  ? r_dihedral_angle_1_deg ? ? 
'X-RAY DIFFRACTION' ? 35.480 23.504 488   ? r_dihedral_angle_2_deg ? ? 
'X-RAY DIFFRACTION' ? 12.525 15.000 1407  ? r_dihedral_angle_3_deg ? ? 
'X-RAY DIFFRACTION' ? 14.093 15.000 36    ? r_dihedral_angle_4_deg ? ? 
'X-RAY DIFFRACTION' ? 0.119  0.200  1112  ? r_chiral_restr         ? ? 
'X-RAY DIFFRACTION' ? 0.013  0.020  7186  ? r_gen_planes_refined   ? ? 
'X-RAY DIFFRACTION' ? 1.556  1.368  4300  ? r_mcbond_it            ? ? 
'X-RAY DIFFRACTION' ? 2.298  2.048  5410  ? r_mcangle_it           ? ? 
'X-RAY DIFFRACTION' ? 2.858  1.655  4727  ? r_scbond_it            ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.3800 
_refine_ls_shell.d_res_low                        1.4160 
_refine_ls_shell.number_reflns_all                14695 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             1481 
_refine_ls_shell.number_reflns_R_work             13214 
_refine_ls_shell.percent_reflns_obs               98.7000 
_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                  0.2210 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.1940 
_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                     6R6Y 
_struct.title                        
;Crystal structure of human carbonic anhydrase isozyme XII with 4-chloro-2-cyclohexylsulfanyl-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        6R6Y 
_struct_keywords.text            
'drug design, carbonic anhydrase, benzenesulfonamide, metal-binding, lyase-lyase inhibitor complex, 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 1 ? 
D N N 1 ? 
E N N 2 ? 
F N N 3 ? 
G N N 3 ? 
H N N 4 ? 
I N N 5 ? 
J N N 2 ? 
K N N 3 ? 
L N N 3 ? 
M N N 3 ? 
N N N 5 ? 
O N N 2 ? 
P N N 3 ? 
Q N N 3 ? 
R N N 4 ? 
S N N 5 ? 
T N N 2 ? 
U N N 3 ? 
V N N 5 ? 
W N N 6 ? 
X N N 6 ? 
Y N N 6 ? 
Z N N 6 ? 
# 
_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 6R6Y A 2 ? 263 ? O43570 30 ? 291 ? 2 263 
2 1 6R6Y B 2 ? 263 ? O43570 30 ? 291 ? 2 263 
3 1 6R6Y C 2 ? 263 ? O43570 30 ? 291 ? 2 263 
4 1 6R6Y D 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 6R6Y MET A 1 ? UNP O43570 ? ? 'initiating methionine' 1 1 
2 6R6Y MET B 1 ? UNP O43570 ? ? 'initiating methionine' 1 2 
3 6R6Y MET C 1 ? UNP O43570 ? ? 'initiating methionine' 1 3 
4 6R6Y MET D 1 ? UNP O43570 ? ? 'initiating methionine' 1 4 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? dimeric 2 
2 author_defined_assembly ? dimeric 2 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,B,E,F,G,H,I,J,K,L,M,N,W,X 
2 1 C,D,O,P,Q,R,S,T,U,V,Y,Z     
# 
loop_
_pdbx_struct_assembly_auth_evidence.id 
_pdbx_struct_assembly_auth_evidence.assembly_id 
_pdbx_struct_assembly_auth_evidence.experimental_support 
_pdbx_struct_assembly_auth_evidence.details 
1 1 none ? 
2 2 none ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
_struct_biol.id        1 
_struct_biol.details   'The asymmetric unit contains two dimers:' 
# 
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 PHE A 7   ? ASN A 13  ? PHE A 7   ASN A 13  5 ? 7  
HELX_P HELX_P2  AA2 SER A 14  ? TYR A 19  ? SER A 14  TYR A 19  1 ? 6  
HELX_P HELX_P3  AA3 PRO A 20  ? GLY A 24  ? PRO A 20  GLY A 24  5 ? 5  
HELX_P HELX_P4  AA4 HIS A 33  ? ASP A 35  ? HIS A 33  ASP A 35  5 ? 3  
HELX_P HELX_P5  AA5 ASP A 128 ? SER A 133 ? ASP A 128 SER A 133 1 ? 6  
HELX_P HELX_P6  AA6 ASN A 152 ? SER A 160 ? ASN A 152 SER A 160 1 ? 9  
HELX_P HELX_P7  AA7 HIS A 161 ? LYS A 166 ? HIS A 161 LYS A 166 5 ? 6  
HELX_P HELX_P8  AA8 ASN A 178 ? LEU A 183 ? ASN A 178 LEU A 183 5 ? 6  
HELX_P HELX_P9  AA9 SER A 218 ? ALA A 228 ? SER A 218 ALA A 228 1 ? 11 
HELX_P HELX_P10 AB1 GLY B 11  ? LYS B 18  ? GLY B 11  LYS B 18  5 ? 8  
HELX_P HELX_P11 AB2 TYR B 19  ? GLY B 24  ? TYR B 19  GLY B 24  5 ? 6  
HELX_P HELX_P12 AB3 HIS B 33  ? ASP B 35  ? HIS B 33  ASP B 35  5 ? 3  
HELX_P HELX_P13 AB4 ASP B 128 ? SER B 133 ? ASP B 128 SER B 133 1 ? 6  
HELX_P HELX_P14 AB5 ASN B 152 ? SER B 160 ? ASN B 152 SER B 160 1 ? 9  
HELX_P HELX_P15 AB6 HIS B 161 ? VAL B 165 ? HIS B 161 VAL B 165 5 ? 5  
HELX_P HELX_P16 AB7 ASN B 178 ? LEU B 183 ? ASN B 178 LEU B 183 5 ? 6  
HELX_P HELX_P17 AB8 SER B 218 ? LEU B 229 ? SER B 218 LEU B 229 1 ? 12 
HELX_P HELX_P18 AB9 GLY C 11  ? ASN C 13  ? GLY C 11  ASN C 13  5 ? 3  
HELX_P HELX_P19 AC1 SER C 14  ? TYR C 19  ? SER C 14  TYR C 19  1 ? 6  
HELX_P HELX_P20 AC2 PRO C 20  ? GLY C 24  ? PRO C 20  GLY C 24  5 ? 5  
HELX_P HELX_P21 AC3 HIS C 33  ? ASP C 35  ? HIS C 33  ASP C 35  5 ? 3  
HELX_P HELX_P22 AC4 ASP C 128 ? SER C 133 ? ASP C 128 SER C 133 1 ? 6  
HELX_P HELX_P23 AC5 ASN C 152 ? SER C 160 ? ASN C 152 SER C 160 1 ? 9  
HELX_P HELX_P24 AC6 HIS C 161 ? VAL C 165 ? HIS C 161 VAL C 165 5 ? 5  
HELX_P HELX_P25 AC7 ASN C 178 ? LEU C 183 ? ASN C 178 LEU C 183 5 ? 6  
HELX_P HELX_P26 AC8 SER C 218 ? ALA C 228 ? SER C 218 ALA C 228 1 ? 11 
HELX_P HELX_P27 AC9 GLY D 11  ? LYS D 18  ? GLY D 11  LYS D 18  5 ? 8  
HELX_P HELX_P28 AD1 TYR D 19  ? GLY D 24  ? TYR D 19  GLY D 24  5 ? 6  
HELX_P HELX_P29 AD2 HIS D 33  ? ASP D 35  ? HIS D 33  ASP D 35  5 ? 3  
HELX_P HELX_P30 AD3 ASP D 128 ? SER D 133 ? ASP D 128 SER D 133 1 ? 6  
HELX_P HELX_P31 AD4 TYR D 155 ? SER D 160 ? TYR D 155 SER D 160 1 ? 6  
HELX_P HELX_P32 AD5 HIS D 161 ? VAL D 165 ? HIS D 161 VAL D 165 5 ? 5  
HELX_P HELX_P33 AD6 ASN D 178 ? LEU D 183 ? ASN D 178 LEU D 183 5 ? 6  
HELX_P HELX_P34 AD7 SER D 218 ? LEU D 229 ? SER D 218 LEU D 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 ? ? ? ? ? ? ? 2.067 ? ? 
disulf2  disulf ? ? B CYS 22  SG  ? ? ? 1_555 B CYS 202 SG ? ? B CYS 22  B CYS 202 1_555 ? ? ? ? ? ? ? 2.042 ? ? 
disulf3  disulf ? ? C CYS 22  SG  ? ? ? 1_555 C CYS 202 SG ? ? C CYS 22  C CYS 202 1_555 ? ? ? ? ? ? ? 2.063 ? ? 
disulf4  disulf ? ? D CYS 22  SG  ? ? ? 1_555 D CYS 202 SG ? ? D CYS 22  D CYS 202 1_555 ? ? ? ? ? ? ? 2.033 ? ? 
metalc1  metalc ? ? A HIS 91  NE2 ? ? ? 1_555 E ZN  .   ZN ? ? A HIS 91  A ZN  301 1_555 ? ? ? ? ? ? ? 2.011 ? ? 
metalc2  metalc ? ? A HIS 93  NE2 ? ? ? 1_555 E ZN  .   ZN ? ? A HIS 93  A ZN  301 1_555 ? ? ? ? ? ? ? 2.022 ? ? 
metalc3  metalc ? ? A HIS 117 ND1 ? ? ? 1_555 E ZN  .   ZN ? ? A HIS 117 A ZN  301 1_555 ? ? ? ? ? ? ? 2.011 ? ? 
metalc4  metalc ? ? E ZN  .   ZN  ? ? ? 1_555 I EA3 .   N1 ? ? A ZN  301 A EA3 305 1_555 ? ? ? ? ? ? ? 1.939 ? ? 
metalc5  metalc ? ? B HIS 91  NE2 ? ? ? 1_555 J ZN  .   ZN ? ? B HIS 91  B ZN  301 1_555 ? ? ? ? ? ? ? 1.998 ? ? 
metalc6  metalc ? ? B HIS 93  NE2 ? ? ? 1_555 J ZN  .   ZN ? ? B HIS 93  B ZN  301 1_555 ? ? ? ? ? ? ? 2.037 ? ? 
metalc7  metalc ? ? B HIS 117 ND1 ? ? ? 1_555 J ZN  .   ZN ? ? B HIS 117 B ZN  301 1_555 ? ? ? ? ? ? ? 1.995 ? ? 
metalc8  metalc ? ? J ZN  .   ZN  ? ? ? 1_555 N EA3 .   N1 ? ? B ZN  301 B EA3 305 1_555 ? ? ? ? ? ? ? 1.894 ? ? 
metalc9  metalc ? ? C HIS 91  NE2 ? ? ? 1_555 O ZN  .   ZN ? ? C HIS 91  C ZN  301 1_555 ? ? ? ? ? ? ? 1.994 ? ? 
metalc10 metalc ? ? C HIS 93  NE2 ? ? ? 1_555 O ZN  .   ZN ? ? C HIS 93  C ZN  301 1_555 ? ? ? ? ? ? ? 2.046 ? ? 
metalc11 metalc ? ? C HIS 117 ND1 ? ? ? 1_555 O ZN  .   ZN ? ? C HIS 117 C ZN  301 1_555 ? ? ? ? ? ? ? 1.996 ? ? 
metalc12 metalc ? ? O ZN  .   ZN  ? ? ? 1_555 S EA3 .   N1 ? ? C ZN  301 C EA3 305 1_555 ? ? ? ? ? ? ? 1.936 ? ? 
metalc13 metalc ? ? D HIS 91  NE2 ? ? ? 1_555 T ZN  .   ZN ? ? D HIS 91  D ZN  301 1_555 ? ? ? ? ? ? ? 2.034 ? ? 
metalc14 metalc ? ? D HIS 93  NE2 ? ? ? 1_555 T ZN  .   ZN ? ? D HIS 93  D ZN  301 1_555 ? ? ? ? ? ? ? 2.025 ? ? 
metalc15 metalc ? ? D HIS 117 ND1 ? ? ? 1_555 T ZN  .   ZN ? ? D HIS 117 D ZN  301 1_555 ? ? ? ? ? ? ? 1.993 ? ? 
metalc16 metalc ? ? T ZN  .   ZN  ? ? ? 1_555 V EA3 .   N1 ? ? D ZN  301 D EA3 303 1_555 ? ? ? ? ? ? ? 1.948 ? ? 
# 
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 ? E ZN . ? A ZN 301 ? 1_555 NE2 ? A HIS 93  ? A HIS 93  ? 1_555 101.7 ? 
2  NE2 ? A HIS 91  ? A HIS 91  ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS 117 ? A HIS 117 ? 1_555 111.9 ? 
3  NE2 ? A HIS 93  ? A HIS 93  ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS 117 ? A HIS 117 ? 1_555 99.5  ? 
4  NE2 ? A HIS 91  ? A HIS 91  ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 N1  ? I EA3 .   ? A EA3 305 ? 1_555 109.9 ? 
5  NE2 ? A HIS 93  ? A HIS 93  ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 N1  ? I EA3 .   ? A EA3 305 ? 1_555 117.8 ? 
6  ND1 ? A HIS 117 ? A HIS 117 ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 N1  ? I EA3 .   ? A EA3 305 ? 1_555 115.1 ? 
7  NE2 ? B HIS 91  ? B HIS 91  ? 1_555 ZN ? J ZN . ? B ZN 301 ? 1_555 NE2 ? B HIS 93  ? B HIS 93  ? 1_555 103.4 ? 
8  NE2 ? B HIS 91  ? B HIS 91  ? 1_555 ZN ? J ZN . ? B ZN 301 ? 1_555 ND1 ? B HIS 117 ? B HIS 117 ? 1_555 112.6 ? 
9  NE2 ? B HIS 93  ? B HIS 93  ? 1_555 ZN ? J ZN . ? B ZN 301 ? 1_555 ND1 ? B HIS 117 ? B HIS 117 ? 1_555 99.7  ? 
10 NE2 ? B HIS 91  ? B HIS 91  ? 1_555 ZN ? J ZN . ? B ZN 301 ? 1_555 N1  ? N EA3 .   ? B EA3 305 ? 1_555 110.4 ? 
11 NE2 ? B HIS 93  ? B HIS 93  ? 1_555 ZN ? J ZN . ? B ZN 301 ? 1_555 N1  ? N EA3 .   ? B EA3 305 ? 1_555 115.6 ? 
12 ND1 ? B HIS 117 ? B HIS 117 ? 1_555 ZN ? J ZN . ? B ZN 301 ? 1_555 N1  ? N EA3 .   ? B EA3 305 ? 1_555 114.4 ? 
13 NE2 ? C HIS 91  ? C HIS 91  ? 1_555 ZN ? O ZN . ? C ZN 301 ? 1_555 NE2 ? C HIS 93  ? C HIS 93  ? 1_555 101.1 ? 
14 NE2 ? C HIS 91  ? C HIS 91  ? 1_555 ZN ? O ZN . ? C ZN 301 ? 1_555 ND1 ? C HIS 117 ? C HIS 117 ? 1_555 113.3 ? 
15 NE2 ? C HIS 93  ? C HIS 93  ? 1_555 ZN ? O ZN . ? C ZN 301 ? 1_555 ND1 ? C HIS 117 ? C HIS 117 ? 1_555 100.6 ? 
16 NE2 ? C HIS 91  ? C HIS 91  ? 1_555 ZN ? O ZN . ? C ZN 301 ? 1_555 N1  ? S EA3 .   ? C EA3 305 ? 1_555 111.1 ? 
17 NE2 ? C HIS 93  ? C HIS 93  ? 1_555 ZN ? O ZN . ? C ZN 301 ? 1_555 N1  ? S EA3 .   ? C EA3 305 ? 1_555 116.4 ? 
18 ND1 ? C HIS 117 ? C HIS 117 ? 1_555 ZN ? O ZN . ? C ZN 301 ? 1_555 N1  ? S EA3 .   ? C EA3 305 ? 1_555 113.5 ? 
19 NE2 ? D HIS 91  ? D HIS 91  ? 1_555 ZN ? T ZN . ? D ZN 301 ? 1_555 NE2 ? D HIS 93  ? D HIS 93  ? 1_555 103.9 ? 
20 NE2 ? D HIS 91  ? D HIS 91  ? 1_555 ZN ? T ZN . ? D ZN 301 ? 1_555 ND1 ? D HIS 117 ? D HIS 117 ? 1_555 113.4 ? 
21 NE2 ? D HIS 93  ? D HIS 93  ? 1_555 ZN ? T ZN . ? D ZN 301 ? 1_555 ND1 ? D HIS 117 ? D HIS 117 ? 1_555 99.0  ? 
22 NE2 ? D HIS 91  ? D HIS 91  ? 1_555 ZN ? T ZN . ? D ZN 301 ? 1_555 N1  ? V EA3 .   ? D EA3 303 ? 1_555 109.2 ? 
23 NE2 ? D HIS 93  ? D HIS 93  ? 1_555 ZN ? T ZN . ? D ZN 301 ? 1_555 N1  ? V EA3 .   ? D EA3 303 ? 1_555 114.9 ? 
24 ND1 ? D HIS 117 ? D HIS 117 ? 1_555 ZN ? T ZN . ? D ZN 301 ? 1_555 N1  ? V EA3 .   ? D EA3 303 ? 1_555 115.6 ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 CYS A 22 ? CYS A 202 ? CYS A 22 ? 1_555 CYS A 202 ? 1_555 SG SG . . . None 'Disulfide bridge' 
2 CYS B 22 ? CYS B 202 ? CYS B 22 ? 1_555 CYS B 202 ? 1_555 SG SG . . . None 'Disulfide bridge' 
3 CYS C 22 ? CYS C 202 ? CYS C 22 ? 1_555 CYS C 202 ? 1_555 SG SG . . . None 'Disulfide bridge' 
4 CYS D 22 ? CYS D 202 ? CYS D 22 ? 1_555 CYS D 202 ? 1_555 SG SG . . . None 'Disulfide bridge' 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1  SER 28  A . ? SER 28  A PRO 29  A ? PRO 29  A 1 1.96  
2  PRO 200 A . ? PRO 200 A PRO 201 A ? PRO 201 A 1 4.29  
3  SER 28  B . ? SER 28  B PRO 29  B ? PRO 29  B 1 -1.37 
4  PRO 200 B . ? PRO 200 B PRO 201 B ? PRO 201 B 1 8.18  
5  PRO 200 B . ? PRO 200 B PRO 201 B ? PRO 201 B 1 -1.24 
6  GLY 8   C . ? GLY 8   C PRO 9   C ? PRO 9   C 1 7.22  
7  SER 28  C . ? SER 28  C PRO 29  C ? PRO 29  C 1 1.55  
8  PRO 200 C . ? PRO 200 C PRO 201 C ? PRO 201 C 1 1.24  
9  SER 28  D . ? SER 28  D PRO 29  D ? PRO 29  D 1 -2.00 
10 PRO 200 D . ? PRO 200 D PRO 201 D ? PRO 201 D 1 2.04  
# 
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  ? 
AA7 ? 2  ? 
AA8 ? 10 ? 
AA9 ? 6  ? 
AB1 ? 2  ? 
AB2 ? 10 ? 
AB3 ? 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      
AA7 1 2  ? parallel      
AA8 1 2  ? parallel      
AA8 2 3  ? anti-parallel 
AA8 3 4  ? anti-parallel 
AA8 4 5  ? parallel      
AA8 5 6  ? anti-parallel 
AA8 6 7  ? anti-parallel 
AA8 7 8  ? anti-parallel 
AA8 8 9  ? anti-parallel 
AA8 9 10 ? anti-parallel 
AA9 1 2  ? anti-parallel 
AA9 2 3  ? anti-parallel 
AA9 3 4  ? anti-parallel 
AA9 4 5  ? anti-parallel 
AA9 5 6  ? parallel      
AB1 1 2  ? parallel      
AB2 1 2  ? parallel      
AB2 2 3  ? anti-parallel 
AB2 3 4  ? anti-parallel 
AB2 4 5  ? parallel      
AB2 5 6  ? anti-parallel 
AB2 6 7  ? anti-parallel 
AB2 7 8  ? anti-parallel 
AB2 8 9  ? anti-parallel 
AB2 9 10 ? anti-parallel 
AB3 1 2  ? anti-parallel 
AB3 2 3  ? anti-parallel 
AB3 3 4  ? anti-parallel 
AB3 4 5  ? anti-parallel 
AB3 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 
AA7 1  ASP C 31  ? LEU C 32  ? ASP C 31  LEU C 32  
AA7 2  THR C 106 ? VAL C 107 ? THR C 106 VAL C 107 
AA8 1  LEU C 37  ? TYR C 39  ? LEU C 37  TYR C 39  
AA8 2  VAL C 257 ? THR C 259 ? VAL C 257 THR C 259 
AA8 3  TYR C 190 ? GLY C 195 ? TYR C 190 GLY C 195 
AA8 4  VAL C 206 ? PHE C 211 ? VAL C 206 PHE C 211 
AA8 5  LEU C 139 ? MET C 148 ? LEU C 139 MET C 148 
AA8 6  ALA C 114 ? ASN C 122 ? ALA C 114 ASN C 122 
AA8 7  TYR C 85  ? TRP C 94  ? TYR C 85  TRP C 94  
AA8 8  VAL C 68  ? ASN C 71  ? VAL C 68  ASN C 71  
AA8 9  GLN C 58  ? ASN C 63  ? GLN C 58  ASN C 63  
AA8 10 GLU C 171 ? PRO C 175 ? GLU C 171 PRO C 175 
AA9 1  GLU C 47  ? GLN C 49  ? GLU C 47  GLN C 49  
AA9 2  HIS C 77  ? GLN C 79  ? HIS C 77  GLN C 79  
AA9 3  TYR C 85  ? TRP C 94  ? TYR C 85  TRP C 94  
AA9 4  ALA C 114 ? ASN C 122 ? ALA C 114 ASN C 122 
AA9 5  LEU C 139 ? MET C 148 ? LEU C 139 MET C 148 
AA9 6  VAL C 215 ? ILE C 217 ? VAL C 215 ILE C 217 
AB1 1  ASP D 31  ? LEU D 32  ? ASP D 31  LEU D 32  
AB1 2  THR D 106 ? VAL D 107 ? THR D 106 VAL D 107 
AB2 1  LEU D 37  ? TYR D 39  ? LEU D 37  TYR D 39  
AB2 2  VAL D 257 ? THR D 259 ? VAL D 257 THR D 259 
AB2 3  TYR D 190 ? GLY D 195 ? TYR D 190 GLY D 195 
AB2 4  VAL D 206 ? PHE D 211 ? VAL D 206 PHE D 211 
AB2 5  LEU D 139 ? MET D 148 ? LEU D 139 MET D 148 
AB2 6  ALA D 114 ? ASN D 122 ? ALA D 114 ASN D 122 
AB2 7  TYR D 85  ? TRP D 94  ? TYR D 85  TRP D 94  
AB2 8  VAL D 68  ? ASN D 71  ? VAL D 68  ASN D 71  
AB2 9  GLN D 58  ? ASN D 63  ? GLN D 58  ASN D 63  
AB2 10 GLU D 171 ? PRO D 175 ? GLU D 171 PRO D 175 
AB3 1  GLU D 47  ? GLN D 49  ? GLU D 47  GLN D 49  
AB3 2  HIS D 77  ? GLN D 79  ? HIS D 77  GLN D 79  
AB3 3  TYR D 85  ? TRP D 94  ? TYR D 85  TRP D 94  
AB3 4  ALA D 114 ? ASN D 122 ? ALA D 114 ASN D 122 
AB3 5  LEU D 139 ? MET D 148 ? LEU D 139 MET D 148 
AB3 6  VAL D 215 ? ILE D 217 ? VAL D 215 ILE D 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 GLY A 195 ? N GLY A 195 O VAL A 206 ? O VAL A 206 
AA2 4 5  O THR A 209 ? O THR A 209 N ALA A 143 ? N ALA A 143 
AA2 5 6  O ILE A 146 ? O ILE A 146 N ALA A 114 ? N ALA A 114 
AA2 6 7  O VAL A 119 ? O VAL A 119 N GLN A 89  ? N GLN A 89  
AA2 7 8  O LEU A 90  ? O LEU A 90  N LEU A 70  ? N LEU A 70  
AA2 8 9  O LYS A 69  ? O LYS A 69  N THR A 62  ? N THR A 62  
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 GLN A 89  ? N GLN A 89  O VAL A 119 ? O VAL A 119 
AA3 4 5  N ALA A 114 ? N ALA A 114 O ILE A 146 ? O ILE A 146 
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 191 ? N TYR B 191 O VAL B 210 ? O VAL B 210 
AA5 4 5  O THR B 209 ? O THR B 209 N ALA B 143 ? N ALA B 143 
AA5 5 6  O LEU B 142 ? O LEU B 142 N ILE B 118 ? N ILE B 118 
AA5 6 7  O VAL B 119 ? O VAL B 119 N GLN B 89  ? N GLN B 89  
AA5 7 8  O LEU B 90  ? O LEU B 90  N LEU B 70  ? N LEU B 70  
AA5 8 9  O LYS B 69  ? O LYS B 69  N THR B 62  ? N THR B 62  
AA5 9 10 N LEU B 61  ? N LEU B 61  O ALA B 172 ? O ALA B 172 
AA6 1 2  N GLU B 47  ? N GLU B 47  O GLN B 79  ? O GLN B 79  
AA6 2 3  N ILE B 78  ? N ILE B 78  O TYR B 85  ? O TYR B 85  
AA6 3 4  N GLN B 89  ? N GLN B 89  O VAL B 119 ? O VAL B 119 
AA6 4 5  N ILE B 118 ? N ILE B 118 O LEU B 142 ? O LEU B 142 
AA6 5 6  N GLU B 147 ? N GLU B 147 O VAL B 215 ? O VAL B 215 
AA7 1 2  N LEU C 32  ? N LEU C 32  O THR C 106 ? O THR C 106 
AA8 1 2  N GLN C 38  ? N GLN C 38  O THR C 259 ? O THR C 259 
AA8 2 3  O TYR C 258 ? O TYR C 258 N ARG C 192 ? N ARG C 192 
AA8 3 4  N GLY C 195 ? N GLY C 195 O VAL C 206 ? O VAL C 206 
AA8 4 5  O THR C 209 ? O THR C 209 N ALA C 143 ? N ALA C 143 
AA8 5 6  O LEU C 142 ? O LEU C 142 N ILE C 118 ? N ILE C 118 
AA8 6 7  O VAL C 119 ? O VAL C 119 N GLN C 89  ? N GLN C 89  
AA8 7 8  O LEU C 90  ? O LEU C 90  N LEU C 70  ? N LEU C 70  
AA8 8 9  O ASN C 71  ? O ASN C 71  N LEU C 60  ? N LEU C 60  
AA8 9 10 N LEU C 61  ? N LEU C 61  O ALA C 172 ? O ALA C 172 
AA9 1 2  N GLU C 47  ? N GLU C 47  O GLN C 79  ? O GLN C 79  
AA9 2 3  N ILE C 78  ? N ILE C 78  O TYR C 85  ? O TYR C 85  
AA9 3 4  N GLN C 89  ? N GLN C 89  O VAL C 119 ? O VAL C 119 
AA9 4 5  N ILE C 118 ? N ILE C 118 O LEU C 142 ? O LEU C 142 
AA9 5 6  N GLU C 147 ? N GLU C 147 O VAL C 215 ? O VAL C 215 
AB1 1 2  N LEU D 32  ? N LEU D 32  O THR D 106 ? O THR D 106 
AB2 1 2  N GLN D 38  ? N GLN D 38  O VAL D 257 ? O VAL D 257 
AB2 2 3  O TYR D 258 ? O TYR D 258 N ARG D 192 ? N ARG D 192 
AB2 3 4  N GLY D 195 ? N GLY D 195 O VAL D 206 ? O VAL D 206 
AB2 4 5  O THR D 209 ? O THR D 209 N ALA D 143 ? N ALA D 143 
AB2 5 6  O ILE D 146 ? O ILE D 146 N ALA D 114 ? N ALA D 114 
AB2 6 7  O VAL D 119 ? O VAL D 119 N GLN D 89  ? N GLN D 89  
AB2 7 8  O LEU D 90  ? O LEU D 90  N LEU D 70  ? N LEU D 70  
AB2 8 9  O ASN D 71  ? O ASN D 71  N LEU D 60  ? N LEU D 60  
AB2 9 10 N LEU D 61  ? N LEU D 61  O ALA D 172 ? O ALA D 172 
AB3 1 2  N GLN D 49  ? N GLN D 49  O HIS D 77  ? O HIS D 77  
AB3 2 3  N ILE D 78  ? N ILE D 78  O TYR D 85  ? O TYR D 85  
AB3 3 4  N GLN D 89  ? N GLN D 89  O VAL D 119 ? O VAL D 119 
AB3 4 5  N ALA D 114 ? N ALA D 114 O ILE D 146 ? O ILE D 146 
AB3 5 6  N GLU D 147 ? N GLU D 147 O VAL D 215 ? O VAL D 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 ? 4  'binding site for residue EDO A 302' 
AC3 Software A EDO 303 ? 6  'binding site for residue EDO A 303' 
AC4 Software A DMS 304 ? 7  'binding site for residue DMS A 304' 
AC5 Software A EA3 305 ? 15 'binding site for residue EA3 A 305' 
AC6 Software B ZN  301 ? 4  'binding site for residue ZN B 301'  
AC7 Software B EDO 302 ? 5  'binding site for residue EDO B 302' 
AC8 Software B EDO 303 ? 6  'binding site for residue EDO B 303' 
AC9 Software B EDO 304 ? 7  'binding site for residue EDO B 304' 
AD1 Software B EA3 305 ? 18 'binding site for residue EA3 B 305' 
AD2 Software C ZN  301 ? 4  'binding site for residue ZN C 301'  
AD3 Software C EDO 302 ? 6  'binding site for residue EDO C 302' 
AD4 Software C EDO 303 ? 9  'binding site for residue EDO C 303' 
AD5 Software C DMS 304 ? 5  'binding site for residue DMS C 304' 
AD6 Software C EA3 305 ? 15 'binding site for residue EA3 C 305' 
AD7 Software D ZN  301 ? 4  'binding site for residue ZN D 301'  
AD8 Software D EDO 302 ? 6  'binding site for residue EDO D 302' 
AD9 Software D EA3 303 ? 15 'binding site for residue EA3 D 303' 
# 
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  EA3 I .   ? EA3 A 305 . ? 1_555 ? 
5   AC2 4  ASP A 156 ? ASP A 156 . ? 1_555 ? 
6   AC2 4  PHE A 159 ? PHE A 159 . ? 1_555 ? 
7   AC2 4  SER A 160 ? SER A 160 . ? 1_555 ? 
8   AC2 4  HOH W .   ? HOH A 520 . ? 1_555 ? 
9   AC3 6  ASN A 71  ? ASN A 71  . ? 1_555 ? 
10  AC3 6  LEU A 72  ? LEU A 72  . ? 1_555 ? 
11  AC3 6  THR A 88  ? THR A 88  . ? 1_555 ? 
12  AC3 6  HOH W .   ? HOH A 437 . ? 1_555 ? 
13  AC3 6  HOH W .   ? HOH A 488 . ? 1_555 ? 
14  AC3 6  HOH W .   ? HOH A 489 . ? 1_555 ? 
15  AC4 7  GLN A 110 ? GLN A 110 . ? 1_555 ? 
16  AC4 7  HIS A 111 ? HIS A 111 . ? 1_555 ? 
17  AC4 7  PHE A 112 ? PHE A 112 . ? 1_555 ? 
18  AC4 7  HOH W .   ? HOH A 401 . ? 1_555 ? 
19  AC4 7  HOH W .   ? HOH A 410 . ? 1_555 ? 
20  AC4 7  HOH W .   ? HOH A 547 . ? 1_555 ? 
21  AC4 7  HOH W .   ? HOH A 595 . ? 1_555 ? 
22  AC5 15 GLN A 89  ? GLN A 89  . ? 1_555 ? 
23  AC5 15 HIS A 91  ? HIS A 91  . ? 1_555 ? 
24  AC5 15 HIS A 93  ? HIS A 93  . ? 1_555 ? 
25  AC5 15 HIS A 117 ? HIS A 117 . ? 1_555 ? 
26  AC5 15 ALA A 129 ? ALA A 129 . ? 1_555 ? 
27  AC5 15 SER A 130 ? SER A 130 . ? 1_555 ? 
28  AC5 15 VAL A 141 ? VAL A 141 . ? 1_555 ? 
29  AC5 15 LEU A 197 ? LEU A 197 . ? 1_555 ? 
30  AC5 15 THR A 198 ? THR A 198 . ? 1_555 ? 
31  AC5 15 THR A 199 ? THR A 199 . ? 1_555 ? 
32  AC5 15 TRP A 208 ? TRP A 208 . ? 1_555 ? 
33  AC5 15 ZN  E .   ? ZN  A 301 . ? 1_555 ? 
34  AC5 15 HOH W .   ? HOH A 533 . ? 1_555 ? 
35  AC5 15 HOH W .   ? HOH A 576 . ? 1_555 ? 
36  AC5 15 HOH W .   ? HOH A 611 . ? 1_555 ? 
37  AC6 4  HIS B 91  ? HIS B 91  . ? 1_555 ? 
38  AC6 4  HIS B 93  ? HIS B 93  . ? 1_555 ? 
39  AC6 4  HIS B 117 ? HIS B 117 . ? 1_555 ? 
40  AC6 4  EA3 N .   ? EA3 B 305 . ? 1_555 ? 
41  AC7 5  ASP B 156 ? ASP B 156 . ? 1_555 ? 
42  AC7 5  SER B 160 ? SER B 160 . ? 1_555 ? 
43  AC7 5  GLN B 221 ? GLN B 221 . ? 1_555 ? 
44  AC7 5  ALA B 224 ? ALA B 224 . ? 1_555 ? 
45  AC7 5  HOH X .   ? HOH B 459 . ? 1_555 ? 
46  AC8 6  THR B 44  ? THR B 44  . ? 1_555 ? 
47  AC8 6  LEU B 46  ? LEU B 46  . ? 1_555 ? 
48  AC8 6  GLY B 80  ? GLY B 80  . ? 1_555 ? 
49  AC8 6  TYR B 190 ? TYR B 190 . ? 1_555 ? 
50  AC8 6  ARG B 192 ? ARG B 192 . ? 1_555 ? 
51  AC8 6  HOH X .   ? HOH B 414 . ? 1_555 ? 
52  AC9 7  ALA B 55  ? ALA B 55  . ? 1_555 ? 
53  AC9 7  LYS B 157 ? LYS B 157 . ? 1_555 ? 
54  AC9 7  GLY B 176 ? GLY B 176 . ? 1_555 ? 
55  AC9 7  PHE B 177 ? PHE B 177 . ? 1_555 ? 
56  AC9 7  HOH X .   ? HOH B 466 . ? 1_555 ? 
57  AC9 7  HOH X .   ? HOH B 470 . ? 1_555 ? 
58  AC9 7  HOH X .   ? HOH B 510 . ? 1_555 ? 
59  AD1 18 TRP B 4   ? TRP B 4   . ? 1_555 ? 
60  AD1 18 HIS B 66  ? HIS B 66  . ? 1_555 ? 
61  AD1 18 GLN B 89  ? GLN B 89  . ? 1_555 ? 
62  AD1 18 HIS B 91  ? HIS B 91  . ? 1_555 ? 
63  AD1 18 HIS B 93  ? HIS B 93  . ? 1_555 ? 
64  AD1 18 HIS B 117 ? HIS B 117 . ? 1_555 ? 
65  AD1 18 ALA B 129 ? ALA B 129 . ? 1_555 ? 
66  AD1 18 SER B 130 ? SER B 130 . ? 1_555 ? 
67  AD1 18 VAL B 141 ? VAL B 141 . ? 1_555 ? 
68  AD1 18 LEU B 197 ? LEU B 197 . ? 1_555 ? 
69  AD1 18 THR B 198 ? THR B 198 . ? 1_555 ? 
70  AD1 18 THR B 199 ? THR B 199 . ? 1_555 ? 
71  AD1 18 TRP B 208 ? TRP B 208 . ? 1_555 ? 
72  AD1 18 ZN  J .   ? ZN  B 301 . ? 1_555 ? 
73  AD1 18 HOH X .   ? HOH B 536 . ? 1_555 ? 
74  AD1 18 HOH X .   ? HOH B 540 . ? 1_555 ? 
75  AD1 18 HOH X .   ? HOH B 571 . ? 1_555 ? 
76  AD1 18 HOH X .   ? HOH B 576 . ? 1_555 ? 
77  AD2 4  HIS C 91  ? HIS C 91  . ? 1_555 ? 
78  AD2 4  HIS C 93  ? HIS C 93  . ? 1_555 ? 
79  AD2 4  HIS C 117 ? HIS C 117 . ? 1_555 ? 
80  AD2 4  EA3 S .   ? EA3 C 305 . ? 1_555 ? 
81  AD3 6  ASN C 71  ? ASN C 71  . ? 1_555 ? 
82  AD3 6  LEU C 72  ? LEU C 72  . ? 1_555 ? 
83  AD3 6  THR C 88  ? THR C 88  . ? 1_555 ? 
84  AD3 6  HOH Y .   ? HOH C 429 . ? 1_555 ? 
85  AD3 6  HOH Y .   ? HOH C 488 . ? 1_555 ? 
86  AD3 6  HOH Y .   ? HOH C 536 . ? 1_555 ? 
87  AD4 9  SER C 42  ? SER C 42  . ? 1_555 ? 
88  AD4 9  THR C 44  ? THR C 44  . ? 1_555 ? 
89  AD4 9  LEU C 46  ? LEU C 46  . ? 1_555 ? 
90  AD4 9  GLY C 80  ? GLY C 80  . ? 1_555 ? 
91  AD4 9  LEU C 81  ? LEU C 81  . ? 1_555 ? 
92  AD4 9  TYR C 190 ? TYR C 190 . ? 1_555 ? 
93  AD4 9  ARG C 192 ? ARG C 192 . ? 1_555 ? 
94  AD4 9  HOH Y .   ? HOH C 443 . ? 1_555 ? 
95  AD4 9  HOH Y .   ? HOH C 471 . ? 1_555 ? 
96  AD5 5  GLN C 110 ? GLN C 110 . ? 1_555 ? 
97  AD5 5  HIS C 111 ? HIS C 111 . ? 1_555 ? 
98  AD5 5  PHE C 112 ? PHE C 112 . ? 1_555 ? 
99  AD5 5  HOH Y .   ? HOH C 401 . ? 1_555 ? 
100 AD5 5  HOH Y .   ? HOH C 542 . ? 1_555 ? 
101 AD6 15 TRP C 4   ? TRP C 4   . ? 1_555 ? 
102 AD6 15 GLN C 89  ? GLN C 89  . ? 1_555 ? 
103 AD6 15 HIS C 91  ? HIS C 91  . ? 1_555 ? 
104 AD6 15 HIS C 93  ? HIS C 93  . ? 1_555 ? 
105 AD6 15 HIS C 117 ? HIS C 117 . ? 1_555 ? 
106 AD6 15 ALA C 129 ? ALA C 129 . ? 1_555 ? 
107 AD6 15 SER C 130 ? SER C 130 . ? 1_555 ? 
108 AD6 15 SER C 133 ? SER C 133 . ? 1_555 ? 
109 AD6 15 VAL C 141 ? VAL C 141 . ? 1_555 ? 
110 AD6 15 LEU C 197 ? LEU C 197 . ? 1_555 ? 
111 AD6 15 THR C 198 ? THR C 198 . ? 1_555 ? 
112 AD6 15 THR C 199 ? THR C 199 . ? 1_555 ? 
113 AD6 15 TRP C 208 ? TRP C 208 . ? 1_555 ? 
114 AD6 15 ZN  O .   ? ZN  C 301 . ? 1_555 ? 
115 AD6 15 HOH Y .   ? HOH C 549 . ? 1_555 ? 
116 AD7 4  HIS D 91  ? HIS D 91  . ? 1_555 ? 
117 AD7 4  HIS D 93  ? HIS D 93  . ? 1_555 ? 
118 AD7 4  HIS D 117 ? HIS D 117 . ? 1_555 ? 
119 AD7 4  EA3 V .   ? EA3 D 303 . ? 1_555 ? 
120 AD8 6  SER D 42  ? SER D 42  . ? 1_555 ? 
121 AD8 6  THR D 44  ? THR D 44  . ? 1_555 ? 
122 AD8 6  LEU D 46  ? LEU D 46  . ? 1_555 ? 
123 AD8 6  GLY D 80  ? GLY D 80  . ? 1_555 ? 
124 AD8 6  TYR D 190 ? TYR D 190 . ? 1_555 ? 
125 AD8 6  ARG D 192 ? ARG D 192 . ? 1_555 ? 
126 AD9 15 TRP D 4   ? TRP D 4   . ? 1_555 ? 
127 AD9 15 GLN D 89  ? GLN D 89  . ? 1_555 ? 
128 AD9 15 HIS D 91  ? HIS D 91  . ? 1_555 ? 
129 AD9 15 HIS D 93  ? HIS D 93  . ? 1_555 ? 
130 AD9 15 HIS D 117 ? HIS D 117 . ? 1_555 ? 
131 AD9 15 ALA D 129 ? ALA D 129 . ? 1_555 ? 
132 AD9 15 SER D 130 ? SER D 130 . ? 1_555 ? 
133 AD9 15 VAL D 141 ? VAL D 141 . ? 1_555 ? 
134 AD9 15 LEU D 197 ? LEU D 197 . ? 1_555 ? 
135 AD9 15 THR D 198 ? THR D 198 . ? 1_555 ? 
136 AD9 15 THR D 199 ? THR D 199 . ? 1_555 ? 
137 AD9 15 TRP D 208 ? TRP D 208 . ? 1_555 ? 
138 AD9 15 ZN  T .   ? ZN  D 301 . ? 1_555 ? 
139 AD9 15 HOH Z .   ? HOH D 447 . ? 1_555 ? 
140 AD9 15 HOH Z .   ? HOH D 535 . ? 1_555 ? 
# 
_pdbx_entry_details.entry_id                   6R6Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASN A 245 ? ? -96.03  52.35 
2 1 ASP B 99  ? ? -151.93 85.48 
3 1 GLU B 137 ? ? 43.29   29.33 
4 1 ASN B 245 ? ? -95.68  56.23 
5 1 ASN C 245 ? ? -96.58  51.04 
6 1 ASP D 99  ? ? -151.48 81.04 
7 1 ASN D 245 ? ? -97.60  54.69 
8 1 GLU D 254 ? ? 77.50   -0.84 
# 
_phasing.method   MR 
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      C 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       675 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   7.17 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
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 
5 1 Y 1 C MET 1 ? C MET 1 
6 1 Y 1 C SER 2 ? C SER 2 
7 1 Y 1 D MET 1 ? D MET 1 
8 1 Y 1 D SER 2 ? D 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  
DMS S    S  N N 88  
DMS O    O  N N 89  
DMS C1   C  N N 90  
DMS C2   C  N N 91  
DMS H11  H  N N 92  
DMS H12  H  N N 93  
DMS H13  H  N N 94  
DMS H21  H  N N 95  
DMS H22  H  N N 96  
DMS H23  H  N N 97  
EA3 O13  O  N N 98  
EA3 C12  C  N N 99  
EA3 N14  N  N N 100 
EA3 C15  C  N N 101 
EA3 C16  C  N N 102 
EA3 O17  O  N N 103 
EA3 C9   C  Y N 104 
EA3 C10  C  Y N 105 
EA3 C3   C  Y N 106 
EA3 S2   S  N N 107 
EA3 O4   O  N N 108 
EA3 O5   O  N N 109 
EA3 N1   N  N N 110 
EA3 C8   C  Y N 111 
EA3 C7   C  Y N 112 
EA3 C6   C  Y N 113 
EA3 CL1  CL N N 114 
EA3 S18  S  N N 115 
EA3 C19  C  N N 116 
EA3 C24  C  N N 117 
EA3 C23  C  N N 118 
EA3 C22  C  N N 119 
EA3 C21  C  N N 120 
EA3 C20  C  N N 121 
EA3 H1   H  N N 122 
EA3 H2   H  N N 123 
EA3 H3   H  N N 124 
EA3 H4   H  N N 125 
EA3 H5   H  N N 126 
EA3 H6   H  N N 127 
EA3 H7   H  N N 128 
EA3 H8   H  N N 129 
EA3 H9   H  N N 130 
EA3 H10  H  N N 131 
EA3 H11  H  N N 132 
EA3 H12  H  N N 133 
EA3 H13  H  N N 134 
EA3 H14  H  N N 135 
EA3 H15  H  N N 136 
EA3 H16  H  N N 137 
EA3 H17  H  N N 138 
EA3 H18  H  N N 139 
EA3 H19  H  N N 140 
EA3 H20  H  N N 141 
EA3 H21  H  N N 142 
EDO C1   C  N N 143 
EDO O1   O  N N 144 
EDO C2   C  N N 145 
EDO O2   O  N N 146 
EDO H11  H  N N 147 
EDO H12  H  N N 148 
EDO HO1  H  N N 149 
EDO H21  H  N N 150 
EDO H22  H  N N 151 
EDO HO2  H  N N 152 
GLN N    N  N N 153 
GLN CA   C  N S 154 
GLN C    C  N N 155 
GLN O    O  N N 156 
GLN CB   C  N N 157 
GLN CG   C  N N 158 
GLN CD   C  N N 159 
GLN OE1  O  N N 160 
GLN NE2  N  N N 161 
GLN OXT  O  N N 162 
GLN H    H  N N 163 
GLN H2   H  N N 164 
GLN HA   H  N N 165 
GLN HB2  H  N N 166 
GLN HB3  H  N N 167 
GLN HG2  H  N N 168 
GLN HG3  H  N N 169 
GLN HE21 H  N N 170 
GLN HE22 H  N N 171 
GLN HXT  H  N N 172 
GLU N    N  N N 173 
GLU CA   C  N S 174 
GLU C    C  N N 175 
GLU O    O  N N 176 
GLU CB   C  N N 177 
GLU CG   C  N N 178 
GLU CD   C  N N 179 
GLU OE1  O  N N 180 
GLU OE2  O  N N 181 
GLU OXT  O  N N 182 
GLU H    H  N N 183 
GLU H2   H  N N 184 
GLU HA   H  N N 185 
GLU HB2  H  N N 186 
GLU HB3  H  N N 187 
GLU HG2  H  N N 188 
GLU HG3  H  N N 189 
GLU HE2  H  N N 190 
GLU HXT  H  N N 191 
GLY N    N  N N 192 
GLY CA   C  N N 193 
GLY C    C  N N 194 
GLY O    O  N N 195 
GLY OXT  O  N N 196 
GLY H    H  N N 197 
GLY H2   H  N N 198 
GLY HA2  H  N N 199 
GLY HA3  H  N N 200 
GLY HXT  H  N N 201 
HIS N    N  N N 202 
HIS CA   C  N S 203 
HIS C    C  N N 204 
HIS O    O  N N 205 
HIS CB   C  N N 206 
HIS CG   C  Y N 207 
HIS ND1  N  Y N 208 
HIS CD2  C  Y N 209 
HIS CE1  C  Y N 210 
HIS NE2  N  Y N 211 
HIS OXT  O  N N 212 
HIS H    H  N N 213 
HIS H2   H  N N 214 
HIS HA   H  N N 215 
HIS HB2  H  N N 216 
HIS HB3  H  N N 217 
HIS HD1  H  N N 218 
HIS HD2  H  N N 219 
HIS HE1  H  N N 220 
HIS HE2  H  N N 221 
HIS HXT  H  N N 222 
HOH O    O  N N 223 
HOH H1   H  N N 224 
HOH H2   H  N N 225 
ILE N    N  N N 226 
ILE CA   C  N S 227 
ILE C    C  N N 228 
ILE O    O  N N 229 
ILE CB   C  N S 230 
ILE CG1  C  N N 231 
ILE CG2  C  N N 232 
ILE CD1  C  N N 233 
ILE OXT  O  N N 234 
ILE H    H  N N 235 
ILE H2   H  N N 236 
ILE HA   H  N N 237 
ILE HB   H  N N 238 
ILE HG12 H  N N 239 
ILE HG13 H  N N 240 
ILE HG21 H  N N 241 
ILE HG22 H  N N 242 
ILE HG23 H  N N 243 
ILE HD11 H  N N 244 
ILE HD12 H  N N 245 
ILE HD13 H  N N 246 
ILE HXT  H  N N 247 
LEU N    N  N N 248 
LEU CA   C  N S 249 
LEU C    C  N N 250 
LEU O    O  N N 251 
LEU CB   C  N N 252 
LEU CG   C  N N 253 
LEU CD1  C  N N 254 
LEU CD2  C  N N 255 
LEU OXT  O  N N 256 
LEU H    H  N N 257 
LEU H2   H  N N 258 
LEU HA   H  N N 259 
LEU HB2  H  N N 260 
LEU HB3  H  N N 261 
LEU HG   H  N N 262 
LEU HD11 H  N N 263 
LEU HD12 H  N N 264 
LEU HD13 H  N N 265 
LEU HD21 H  N N 266 
LEU HD22 H  N N 267 
LEU HD23 H  N N 268 
LEU HXT  H  N N 269 
LYS N    N  N N 270 
LYS CA   C  N S 271 
LYS C    C  N N 272 
LYS O    O  N N 273 
LYS CB   C  N N 274 
LYS CG   C  N N 275 
LYS CD   C  N N 276 
LYS CE   C  N N 277 
LYS NZ   N  N N 278 
LYS OXT  O  N N 279 
LYS H    H  N N 280 
LYS H2   H  N N 281 
LYS HA   H  N N 282 
LYS HB2  H  N N 283 
LYS HB3  H  N N 284 
LYS HG2  H  N N 285 
LYS HG3  H  N N 286 
LYS HD2  H  N N 287 
LYS HD3  H  N N 288 
LYS HE2  H  N N 289 
LYS HE3  H  N N 290 
LYS HZ1  H  N N 291 
LYS HZ2  H  N N 292 
LYS HZ3  H  N N 293 
LYS HXT  H  N N 294 
MET N    N  N N 295 
MET CA   C  N S 296 
MET C    C  N N 297 
MET O    O  N N 298 
MET CB   C  N N 299 
MET CG   C  N N 300 
MET SD   S  N N 301 
MET CE   C  N N 302 
MET OXT  O  N N 303 
MET H    H  N N 304 
MET H2   H  N N 305 
MET HA   H  N N 306 
MET HB2  H  N N 307 
MET HB3  H  N N 308 
MET HG2  H  N N 309 
MET HG3  H  N N 310 
MET HE1  H  N N 311 
MET HE2  H  N N 312 
MET HE3  H  N N 313 
MET HXT  H  N N 314 
PHE N    N  N N 315 
PHE CA   C  N S 316 
PHE C    C  N N 317 
PHE O    O  N N 318 
PHE CB   C  N N 319 
PHE CG   C  Y N 320 
PHE CD1  C  Y N 321 
PHE CD2  C  Y N 322 
PHE CE1  C  Y N 323 
PHE CE2  C  Y N 324 
PHE CZ   C  Y N 325 
PHE OXT  O  N N 326 
PHE H    H  N N 327 
PHE H2   H  N N 328 
PHE HA   H  N N 329 
PHE HB2  H  N N 330 
PHE HB3  H  N N 331 
PHE HD1  H  N N 332 
PHE HD2  H  N N 333 
PHE HE1  H  N N 334 
PHE HE2  H  N N 335 
PHE HZ   H  N N 336 
PHE HXT  H  N N 337 
PRO N    N  N N 338 
PRO CA   C  N S 339 
PRO C    C  N N 340 
PRO O    O  N N 341 
PRO CB   C  N N 342 
PRO CG   C  N N 343 
PRO CD   C  N N 344 
PRO OXT  O  N N 345 
PRO H    H  N N 346 
PRO HA   H  N N 347 
PRO HB2  H  N N 348 
PRO HB3  H  N N 349 
PRO HG2  H  N N 350 
PRO HG3  H  N N 351 
PRO HD2  H  N N 352 
PRO HD3  H  N N 353 
PRO HXT  H  N N 354 
SER N    N  N N 355 
SER CA   C  N S 356 
SER C    C  N N 357 
SER O    O  N N 358 
SER CB   C  N N 359 
SER OG   O  N N 360 
SER OXT  O  N N 361 
SER H    H  N N 362 
SER H2   H  N N 363 
SER HA   H  N N 364 
SER HB2  H  N N 365 
SER HB3  H  N N 366 
SER HG   H  N N 367 
SER HXT  H  N N 368 
THR N    N  N N 369 
THR CA   C  N S 370 
THR C    C  N N 371 
THR O    O  N N 372 
THR CB   C  N R 373 
THR OG1  O  N N 374 
THR CG2  C  N N 375 
THR OXT  O  N N 376 
THR H    H  N N 377 
THR H2   H  N N 378 
THR HA   H  N N 379 
THR HB   H  N N 380 
THR HG1  H  N N 381 
THR HG21 H  N N 382 
THR HG22 H  N N 383 
THR HG23 H  N N 384 
THR HXT  H  N N 385 
TRP N    N  N N 386 
TRP CA   C  N S 387 
TRP C    C  N N 388 
TRP O    O  N N 389 
TRP CB   C  N N 390 
TRP CG   C  Y N 391 
TRP CD1  C  Y N 392 
TRP CD2  C  Y N 393 
TRP NE1  N  Y N 394 
TRP CE2  C  Y N 395 
TRP CE3  C  Y N 396 
TRP CZ2  C  Y N 397 
TRP CZ3  C  Y N 398 
TRP CH2  C  Y N 399 
TRP OXT  O  N N 400 
TRP H    H  N N 401 
TRP H2   H  N N 402 
TRP HA   H  N N 403 
TRP HB2  H  N N 404 
TRP HB3  H  N N 405 
TRP HD1  H  N N 406 
TRP HE1  H  N N 407 
TRP HE3  H  N N 408 
TRP HZ2  H  N N 409 
TRP HZ3  H  N N 410 
TRP HH2  H  N N 411 
TRP HXT  H  N N 412 
TYR N    N  N N 413 
TYR CA   C  N S 414 
TYR C    C  N N 415 
TYR O    O  N N 416 
TYR CB   C  N N 417 
TYR CG   C  Y N 418 
TYR CD1  C  Y N 419 
TYR CD2  C  Y N 420 
TYR CE1  C  Y N 421 
TYR CE2  C  Y N 422 
TYR CZ   C  Y N 423 
TYR OH   O  N N 424 
TYR OXT  O  N N 425 
TYR H    H  N N 426 
TYR H2   H  N N 427 
TYR HA   H  N N 428 
TYR HB2  H  N N 429 
TYR HB3  H  N N 430 
TYR HD1  H  N N 431 
TYR HD2  H  N N 432 
TYR HE1  H  N N 433 
TYR HE2  H  N N 434 
TYR HH   H  N N 435 
TYR HXT  H  N N 436 
VAL N    N  N N 437 
VAL CA   C  N S 438 
VAL C    C  N N 439 
VAL O    O  N N 440 
VAL CB   C  N N 441 
VAL CG1  C  N N 442 
VAL CG2  C  N N 443 
VAL OXT  O  N N 444 
VAL H    H  N N 445 
VAL H2   H  N N 446 
VAL HA   H  N N 447 
VAL HB   H  N N 448 
VAL HG11 H  N N 449 
VAL HG12 H  N N 450 
VAL HG13 H  N N 451 
VAL HG21 H  N N 452 
VAL HG22 H  N N 453 
VAL HG23 H  N N 454 
VAL HXT  H  N N 455 
ZN  ZN   ZN N N 456 
# 
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  
DMS S   O    doub N N 83  
DMS S   C1   sing N N 84  
DMS S   C2   sing N N 85  
DMS C1  H11  sing N N 86  
DMS C1  H12  sing N N 87  
DMS C1  H13  sing N N 88  
DMS C2  H21  sing N N 89  
DMS C2  H22  sing N N 90  
DMS C2  H23  sing N N 91  
EA3 C16 O17  sing N N 92  
EA3 C16 C15  sing N N 93  
EA3 C15 N14  sing N N 94  
EA3 O13 C12  doub N N 95  
EA3 C20 C21  sing N N 96  
EA3 C20 C19  sing N N 97  
EA3 C21 C22  sing N N 98  
EA3 C12 N14  sing N N 99  
EA3 C12 C9   sing N N 100 
EA3 C19 S18  sing N N 101 
EA3 C19 C24  sing N N 102 
EA3 S18 C8   sing N N 103 
EA3 C22 C23  sing N N 104 
EA3 C9  C8   doub Y N 105 
EA3 C9  C10  sing Y N 106 
EA3 C8  C7   sing Y N 107 
EA3 C24 C23  sing N N 108 
EA3 C10 C3   doub Y N 109 
EA3 C7  C6   doub Y N 110 
EA3 C3  C6   sing Y N 111 
EA3 C3  S2   sing N N 112 
EA3 C6  CL1  sing N N 113 
EA3 N1  S2   sing N N 114 
EA3 O4  S2   doub N N 115 
EA3 S2  O5   doub N N 116 
EA3 N14 H1   sing N N 117 
EA3 C15 H2   sing N N 118 
EA3 C15 H3   sing N N 119 
EA3 C16 H4   sing N N 120 
EA3 C16 H5   sing N N 121 
EA3 O17 H6   sing N N 122 
EA3 C10 H7   sing N N 123 
EA3 N1  H8   sing N N 124 
EA3 N1  H9   sing N N 125 
EA3 C7  H10  sing N N 126 
EA3 C19 H11  sing N N 127 
EA3 C24 H12  sing N N 128 
EA3 C24 H13  sing N N 129 
EA3 C23 H14  sing N N 130 
EA3 C23 H15  sing N N 131 
EA3 C22 H16  sing N N 132 
EA3 C22 H17  sing N N 133 
EA3 C21 H18  sing N N 134 
EA3 C21 H19  sing N N 135 
EA3 C20 H20  sing N N 136 
EA3 C20 H21  sing N N 137 
EDO C1  O1   sing N N 138 
EDO C1  C2   sing N N 139 
EDO C1  H11  sing N N 140 
EDO C1  H12  sing N N 141 
EDO O1  HO1  sing N N 142 
EDO C2  O2   sing N N 143 
EDO C2  H21  sing N N 144 
EDO C2  H22  sing N N 145 
EDO O2  HO2  sing N N 146 
GLN N   CA   sing N N 147 
GLN N   H    sing N N 148 
GLN N   H2   sing N N 149 
GLN CA  C    sing N N 150 
GLN CA  CB   sing N N 151 
GLN CA  HA   sing N N 152 
GLN C   O    doub N N 153 
GLN C   OXT  sing N N 154 
GLN CB  CG   sing N N 155 
GLN CB  HB2  sing N N 156 
GLN CB  HB3  sing N N 157 
GLN CG  CD   sing N N 158 
GLN CG  HG2  sing N N 159 
GLN CG  HG3  sing N N 160 
GLN CD  OE1  doub N N 161 
GLN CD  NE2  sing N N 162 
GLN NE2 HE21 sing N N 163 
GLN NE2 HE22 sing N N 164 
GLN OXT HXT  sing N N 165 
GLU N   CA   sing N N 166 
GLU N   H    sing N N 167 
GLU N   H2   sing N N 168 
GLU CA  C    sing N N 169 
GLU CA  CB   sing N N 170 
GLU CA  HA   sing N N 171 
GLU C   O    doub N N 172 
GLU C   OXT  sing N N 173 
GLU CB  CG   sing N N 174 
GLU CB  HB2  sing N N 175 
GLU CB  HB3  sing N N 176 
GLU CG  CD   sing N N 177 
GLU CG  HG2  sing N N 178 
GLU CG  HG3  sing N N 179 
GLU CD  OE1  doub N N 180 
GLU CD  OE2  sing N N 181 
GLU OE2 HE2  sing N N 182 
GLU OXT HXT  sing N N 183 
GLY N   CA   sing N N 184 
GLY N   H    sing N N 185 
GLY N   H2   sing N N 186 
GLY CA  C    sing N N 187 
GLY CA  HA2  sing N N 188 
GLY CA  HA3  sing N N 189 
GLY C   O    doub N N 190 
GLY C   OXT  sing N N 191 
GLY OXT HXT  sing N N 192 
HIS N   CA   sing N N 193 
HIS N   H    sing N N 194 
HIS N   H2   sing N N 195 
HIS CA  C    sing N N 196 
HIS CA  CB   sing N N 197 
HIS CA  HA   sing N N 198 
HIS C   O    doub N N 199 
HIS C   OXT  sing N N 200 
HIS CB  CG   sing N N 201 
HIS CB  HB2  sing N N 202 
HIS CB  HB3  sing N N 203 
HIS CG  ND1  sing Y N 204 
HIS CG  CD2  doub Y N 205 
HIS ND1 CE1  doub Y N 206 
HIS ND1 HD1  sing N N 207 
HIS CD2 NE2  sing Y N 208 
HIS CD2 HD2  sing N N 209 
HIS CE1 NE2  sing Y N 210 
HIS CE1 HE1  sing N N 211 
HIS NE2 HE2  sing N N 212 
HIS OXT HXT  sing N N 213 
HOH O   H1   sing N N 214 
HOH O   H2   sing N N 215 
ILE N   CA   sing N N 216 
ILE N   H    sing N N 217 
ILE N   H2   sing N N 218 
ILE CA  C    sing N N 219 
ILE CA  CB   sing N N 220 
ILE CA  HA   sing N N 221 
ILE C   O    doub N N 222 
ILE C   OXT  sing N N 223 
ILE CB  CG1  sing N N 224 
ILE CB  CG2  sing N N 225 
ILE CB  HB   sing N N 226 
ILE CG1 CD1  sing N N 227 
ILE CG1 HG12 sing N N 228 
ILE CG1 HG13 sing N N 229 
ILE CG2 HG21 sing N N 230 
ILE CG2 HG22 sing N N 231 
ILE CG2 HG23 sing N N 232 
ILE CD1 HD11 sing N N 233 
ILE CD1 HD12 sing N N 234 
ILE CD1 HD13 sing N N 235 
ILE OXT HXT  sing N N 236 
LEU N   CA   sing N N 237 
LEU N   H    sing N N 238 
LEU N   H2   sing N N 239 
LEU CA  C    sing N N 240 
LEU CA  CB   sing N N 241 
LEU CA  HA   sing N N 242 
LEU C   O    doub N N 243 
LEU C   OXT  sing N N 244 
LEU CB  CG   sing N N 245 
LEU CB  HB2  sing N N 246 
LEU CB  HB3  sing N N 247 
LEU CG  CD1  sing N N 248 
LEU CG  CD2  sing N N 249 
LEU CG  HG   sing N N 250 
LEU CD1 HD11 sing N N 251 
LEU CD1 HD12 sing N N 252 
LEU CD1 HD13 sing N N 253 
LEU CD2 HD21 sing N N 254 
LEU CD2 HD22 sing N N 255 
LEU CD2 HD23 sing N N 256 
LEU OXT HXT  sing N N 257 
LYS N   CA   sing N N 258 
LYS N   H    sing N N 259 
LYS N   H2   sing N N 260 
LYS CA  C    sing N N 261 
LYS CA  CB   sing N N 262 
LYS CA  HA   sing N N 263 
LYS C   O    doub N N 264 
LYS C   OXT  sing N N 265 
LYS CB  CG   sing N N 266 
LYS CB  HB2  sing N N 267 
LYS CB  HB3  sing N N 268 
LYS CG  CD   sing N N 269 
LYS CG  HG2  sing N N 270 
LYS CG  HG3  sing N N 271 
LYS CD  CE   sing N N 272 
LYS CD  HD2  sing N N 273 
LYS CD  HD3  sing N N 274 
LYS CE  NZ   sing N N 275 
LYS CE  HE2  sing N N 276 
LYS CE  HE3  sing N N 277 
LYS NZ  HZ1  sing N N 278 
LYS NZ  HZ2  sing N N 279 
LYS NZ  HZ3  sing N N 280 
LYS OXT HXT  sing N N 281 
MET N   CA   sing N N 282 
MET N   H    sing N N 283 
MET N   H2   sing N N 284 
MET CA  C    sing N N 285 
MET CA  CB   sing N N 286 
MET CA  HA   sing N N 287 
MET C   O    doub N N 288 
MET C   OXT  sing N N 289 
MET CB  CG   sing N N 290 
MET CB  HB2  sing N N 291 
MET CB  HB3  sing N N 292 
MET CG  SD   sing N N 293 
MET CG  HG2  sing N N 294 
MET CG  HG3  sing N N 295 
MET SD  CE   sing N N 296 
MET CE  HE1  sing N N 297 
MET CE  HE2  sing N N 298 
MET CE  HE3  sing N N 299 
MET OXT HXT  sing N N 300 
PHE N   CA   sing N N 301 
PHE N   H    sing N N 302 
PHE N   H2   sing N N 303 
PHE CA  C    sing N N 304 
PHE CA  CB   sing N N 305 
PHE CA  HA   sing N N 306 
PHE C   O    doub N N 307 
PHE C   OXT  sing N N 308 
PHE CB  CG   sing N N 309 
PHE CB  HB2  sing N N 310 
PHE CB  HB3  sing N N 311 
PHE CG  CD1  doub Y N 312 
PHE CG  CD2  sing Y N 313 
PHE CD1 CE1  sing Y N 314 
PHE CD1 HD1  sing N N 315 
PHE CD2 CE2  doub Y N 316 
PHE CD2 HD2  sing N N 317 
PHE CE1 CZ   doub Y N 318 
PHE CE1 HE1  sing N N 319 
PHE CE2 CZ   sing Y N 320 
PHE CE2 HE2  sing N N 321 
PHE CZ  HZ   sing N N 322 
PHE OXT HXT  sing N N 323 
PRO N   CA   sing N N 324 
PRO N   CD   sing N N 325 
PRO N   H    sing N N 326 
PRO CA  C    sing N N 327 
PRO CA  CB   sing N N 328 
PRO CA  HA   sing N N 329 
PRO C   O    doub N N 330 
PRO C   OXT  sing N N 331 
PRO CB  CG   sing N N 332 
PRO CB  HB2  sing N N 333 
PRO CB  HB3  sing N N 334 
PRO CG  CD   sing N N 335 
PRO CG  HG2  sing N N 336 
PRO CG  HG3  sing N N 337 
PRO CD  HD2  sing N N 338 
PRO CD  HD3  sing N N 339 
PRO OXT HXT  sing N N 340 
SER N   CA   sing N N 341 
SER N   H    sing N N 342 
SER N   H2   sing N N 343 
SER CA  C    sing N N 344 
SER CA  CB   sing N N 345 
SER CA  HA   sing N N 346 
SER C   O    doub N N 347 
SER C   OXT  sing N N 348 
SER CB  OG   sing N N 349 
SER CB  HB2  sing N N 350 
SER CB  HB3  sing N N 351 
SER OG  HG   sing N N 352 
SER OXT HXT  sing N N 353 
THR N   CA   sing N N 354 
THR N   H    sing N N 355 
THR N   H2   sing N N 356 
THR CA  C    sing N N 357 
THR CA  CB   sing N N 358 
THR CA  HA   sing N N 359 
THR C   O    doub N N 360 
THR C   OXT  sing N N 361 
THR CB  OG1  sing N N 362 
THR CB  CG2  sing N N 363 
THR CB  HB   sing N N 364 
THR OG1 HG1  sing N N 365 
THR CG2 HG21 sing N N 366 
THR CG2 HG22 sing N N 367 
THR CG2 HG23 sing N N 368 
THR OXT HXT  sing N N 369 
TRP N   CA   sing N N 370 
TRP N   H    sing N N 371 
TRP N   H2   sing N N 372 
TRP CA  C    sing N N 373 
TRP CA  CB   sing N N 374 
TRP CA  HA   sing N N 375 
TRP C   O    doub N N 376 
TRP C   OXT  sing N N 377 
TRP CB  CG   sing N N 378 
TRP CB  HB2  sing N N 379 
TRP CB  HB3  sing N N 380 
TRP CG  CD1  doub Y N 381 
TRP CG  CD2  sing Y N 382 
TRP CD1 NE1  sing Y N 383 
TRP CD1 HD1  sing N N 384 
TRP CD2 CE2  doub Y N 385 
TRP CD2 CE3  sing Y N 386 
TRP NE1 CE2  sing Y N 387 
TRP NE1 HE1  sing N N 388 
TRP CE2 CZ2  sing Y N 389 
TRP CE3 CZ3  doub Y N 390 
TRP CE3 HE3  sing N N 391 
TRP CZ2 CH2  doub Y N 392 
TRP CZ2 HZ2  sing N N 393 
TRP CZ3 CH2  sing Y N 394 
TRP CZ3 HZ3  sing N N 395 
TRP CH2 HH2  sing N N 396 
TRP OXT HXT  sing N N 397 
TYR N   CA   sing N N 398 
TYR N   H    sing N N 399 
TYR N   H2   sing N N 400 
TYR CA  C    sing N N 401 
TYR CA  CB   sing N N 402 
TYR CA  HA   sing N N 403 
TYR C   O    doub N N 404 
TYR C   OXT  sing N N 405 
TYR CB  CG   sing N N 406 
TYR CB  HB2  sing N N 407 
TYR CB  HB3  sing N N 408 
TYR CG  CD1  doub Y N 409 
TYR CG  CD2  sing Y N 410 
TYR CD1 CE1  sing Y N 411 
TYR CD1 HD1  sing N N 412 
TYR CD2 CE2  doub Y N 413 
TYR CD2 HD2  sing N N 414 
TYR CE1 CZ   doub Y N 415 
TYR CE1 HE1  sing N N 416 
TYR CE2 CZ   sing Y N 417 
TYR CE2 HE2  sing N N 418 
TYR CZ  OH   sing N N 419 
TYR OH  HH   sing N N 420 
TYR OXT HXT  sing N N 421 
VAL N   CA   sing N N 422 
VAL N   H    sing N N 423 
VAL N   H2   sing N N 424 
VAL CA  C    sing N N 425 
VAL CA  CB   sing N N 426 
VAL CA  HA   sing N N 427 
VAL C   O    doub N N 428 
VAL C   OXT  sing N N 429 
VAL CB  CG1  sing N N 430 
VAL CB  CG2  sing N N 431 
VAL CB  HB   sing N N 432 
VAL CG1 HG11 sing N N 433 
VAL CG1 HG12 sing N N 434 
VAL CG1 HG13 sing N N 435 
VAL CG2 HG21 sing N N 436 
VAL CG2 HG22 sing N N 437 
VAL CG2 HG23 sing N N 438 
VAL OXT HXT  sing N N 439 
# 
_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                    6R6Y 
_atom_sites.fract_transf_matrix[1][1]   0.012931 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.004363 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.013479 
_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]   0.011518 
_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   A LYS A 1 3   ? 18.840  15.762  18.522  0.50 21.67 ? 3   LYS A N   1 
ATOM   2    N  N   B LYS A 1 3   ? 17.638  16.306  19.716  0.50 25.76 ? 3   LYS A N   1 
ATOM   3    C  CA  A LYS A 1 3   ? 17.863  16.364  17.588  0.50 20.27 ? 3   LYS A CA  1 
ATOM   4    C  CA  B LYS A 1 3   ? 17.372  16.174  18.270  0.50 25.05 ? 3   LYS A CA  1 
ATOM   5    C  C   A LYS A 1 3   ? 17.025  15.297  16.887  0.50 17.97 ? 3   LYS A C   1 
ATOM   6    C  C   B LYS A 1 3   ? 16.618  14.870  18.043  0.50 22.68 ? 3   LYS A C   1 
ATOM   7    O  O   A LYS A 1 3   ? 16.252  15.655  16.009  0.50 18.90 ? 3   LYS A O   1 
ATOM   8    O  O   B LYS A 1 3   ? 15.733  14.537  18.824  0.50 22.95 ? 3   LYS A O   1 
ATOM   9    C  CB  A LYS A 1 3   ? 18.572  17.088  16.446  0.50 21.21 ? 3   LYS A CB  1 
ATOM   10   C  CB  B LYS A 1 3   ? 18.666  16.274  17.453  0.50 25.89 ? 3   LYS A CB  1 
ATOM   11   C  CG  A LYS A 1 3   ? 19.386  16.146  15.574  0.50 21.35 ? 3   LYS A CG  1 
ATOM   12   C  CG  B LYS A 1 3   ? 19.769  15.286  17.817  0.50 28.26 ? 3   LYS A CG  1 
ATOM   13   C  CD  A LYS A 1 3   ? 20.730  15.850  16.236  0.50 25.76 ? 3   LYS A CD  1 
ATOM   14   C  CD  B LYS A 1 3   ? 21.157  15.858  17.590  0.50 28.67 ? 3   LYS A CD  1 
ATOM   15   C  CE  A LYS A 1 3   ? 21.461  17.130  16.596  0.50 26.89 ? 3   LYS A CE  1 
ATOM   16   C  CE  B LYS A 1 3   ? 21.224  17.311  18.012  0.50 29.06 ? 3   LYS A CE  1 
ATOM   17   N  NZ  A LYS A 1 3   ? 22.919  17.017  16.338  0.50 30.04 ? 3   LYS A NZ  1 
ATOM   18   N  NZ  B LYS A 1 3   ? 22.209  18.083  17.218  0.50 27.92 ? 3   LYS A NZ  1 
ATOM   19   N  N   A TRP A 1 4   ? 17.248  14.008  17.182  0.50 14.07 ? 4   TRP A N   1 
ATOM   20   N  N   B TRP A 1 4   ? 17.039  14.107  17.028  0.50 17.39 ? 4   TRP A N   1 
ATOM   21   C  CA  A TRP A 1 4   ? 16.338  12.996  16.653  0.50 12.92 ? 4   TRP A CA  1 
ATOM   22   C  CA  B TRP A 1 4   ? 16.230  13.004  16.524  0.50 14.26 ? 4   TRP A CA  1 
ATOM   23   C  C   A TRP A 1 4   ? 16.228  11.814  17.609  0.50 13.22 ? 4   TRP A C   1 
ATOM   24   C  C   B TRP A 1 4   ? 16.225  11.847  17.518  0.50 14.22 ? 4   TRP A C   1 
ATOM   25   O  O   A TRP A 1 4   ? 17.145  11.520  18.383  0.50 12.63 ? 4   TRP A O   1 
ATOM   26   O  O   B TRP A 1 4   ? 17.218  11.627  18.229  0.50 14.57 ? 4   TRP A O   1 
ATOM   27   C  CB  A TRP A 1 4   ? 16.775  12.561  15.253  0.50 12.13 ? 4   TRP A CB  1 
ATOM   28   C  CB  B TRP A 1 4   ? 16.729  12.561  15.146  0.50 13.38 ? 4   TRP A CB  1 
ATOM   29   C  CG  A TRP A 1 4   ? 18.123  11.906  15.195  0.50 11.31 ? 4   TRP A CG  1 
ATOM   30   C  CG  B TRP A 1 4   ? 18.087  11.925  15.127  0.50 12.35 ? 4   TRP A CG  1 
ATOM   31   C  CD1 A TRP A 1 4   ? 19.330  12.504  15.004  0.50 12.14 ? 4   TRP A CD1 1 
ATOM   32   C  CD1 B TRP A 1 4   ? 19.284  12.543  14.935  0.50 13.17 ? 4   TRP A CD1 1 
ATOM   33   C  CD2 A TRP A 1 4   ? 18.398  10.493  15.275  0.50 10.81 ? 4   TRP A CD2 1 
ATOM   34   C  CD2 B TRP A 1 4   ? 18.384  10.517  15.225  0.50 11.75 ? 4   TRP A CD2 1 
ATOM   35   N  NE1 A TRP A 1 4   ? 20.332  11.580  14.969  0.50 12.61 ? 4   TRP A NE1 1 
ATOM   36   N  NE1 B TRP A 1 4   ? 20.302  11.634  14.932  0.50 13.41 ? 4   TRP A NE1 1 
ATOM   37   C  CE2 A TRP A 1 4   ? 19.792  10.323  15.132  0.50 10.63 ? 4   TRP A CE2 1 
ATOM   38   C  CE2 B TRP A 1 4   ? 19.781  10.370  15.103  0.50 11.59 ? 4   TRP A CE2 1 
ATOM   39   C  CE3 A TRP A 1 4   ? 17.600  9.355   15.447  0.50 10.25 ? 4   TRP A CE3 1 
ATOM   40   C  CE3 B TRP A 1 4   ? 17.605  9.366   15.400  0.50 11.08 ? 4   TRP A CE3 1 
ATOM   41   C  CZ2 A TRP A 1 4   ? 20.401  9.069   15.157  0.50 10.89 ? 4   TRP A CZ2 1 
ATOM   42   C  CZ2 B TRP A 1 4   ? 20.413  9.129   15.158  0.50 11.71 ? 4   TRP A CZ2 1 
ATOM   43   C  CZ3 A TRP A 1 4   ? 18.194  8.110   15.470  0.50 10.16 ? 4   TRP A CZ3 1 
ATOM   44   C  CZ3 B TRP A 1 4   ? 18.222  8.134   15.449  0.50 10.95 ? 4   TRP A CZ3 1 
ATOM   45   C  CH2 A TRP A 1 4   ? 19.576  7.980   15.340  0.50 10.27 ? 4   TRP A CH2 1 
ATOM   46   C  CH2 B TRP A 1 4   ? 19.606  8.026   15.343  0.50 11.07 ? 4   TRP A CH2 1 
ATOM   47   N  N   . THR A 1 5   ? 15.127  11.076  17.495  1.00 12.69 ? 5   THR A N   1 
ATOM   48   C  CA  . THR A 1 5   ? 14.895  9.947   18.391  1.00 13.19 ? 5   THR A CA  1 
ATOM   49   C  C   . THR A 1 5   ? 14.161  8.860   17.634  1.00 12.77 ? 5   THR A C   1 
ATOM   50   O  O   . THR A 1 5   ? 13.890  8.952   16.445  1.00 11.79 ? 5   THR A O   1 
ATOM   51   C  CB  . THR A 1 5   ? 13.958  10.341  19.559  1.00 15.08 ? 5   THR A CB  1 
ATOM   52   O  OG1 . THR A 1 5   ? 12.674  10.592  18.972  1.00 17.41 ? 5   THR A OG1 1 
ATOM   53   C  CG2 . THR A 1 5   ? 14.387  11.592  20.309  1.00 17.25 ? 5   THR A CG2 1 
ATOM   54   N  N   . TYR A 1 6   ? 13.841  7.769   18.335  1.00 13.61 ? 6   TYR A N   1 
ATOM   55   C  CA  . TYR A 1 6   ? 13.005  6.742   17.739  1.00 13.63 ? 6   TYR A CA  1 
ATOM   56   C  C   . TYR A 1 6   ? 11.570  6.747   18.271  1.00 14.27 ? 6   TYR A C   1 
ATOM   57   O  O   . TYR A 1 6   ? 10.839  5.762   18.236  1.00 14.80 ? 6   TYR A O   1 
ATOM   58   C  CB  . TYR A 1 6   ? 13.576  5.332   17.935  1.00 12.84 ? 6   TYR A CB  1 
ATOM   59   C  CG  . TYR A 1 6   ? 14.854  5.067   17.173  1.00 11.44 ? 6   TYR A CG  1 
ATOM   60   C  CD1 . TYR A 1 6   ? 16.099  5.319   17.742  1.00 11.67 ? 6   TYR A CD1 1 
ATOM   61   C  CD2 . TYR A 1 6   ? 14.816  4.538   15.897  1.00 11.13 ? 6   TYR A CD2 1 
ATOM   62   C  CE1 . TYR A 1 6   ? 17.279  5.072   17.070  1.00 11.60 ? 6   TYR A CE1 1 
ATOM   63   C  CE2 . TYR A 1 6   ? 15.978  4.273   15.203  1.00 9.90  ? 6   TYR A CE2 1 
ATOM   64   C  CZ  . TYR A 1 6   ? 17.195  4.565   15.785  1.00 10.05 ? 6   TYR A CZ  1 
ATOM   65   O  OH  . TYR A 1 6   ? 18.314  4.263   15.094  1.00 11.41 ? 6   TYR A OH  1 
ATOM   66   N  N   . PHE A 1 7   ? 11.102  7.897   18.776  1.00 21.30 ? 7   PHE A N   1 
ATOM   67   C  CA  . PHE A 1 7   ? 9.801   7.915   19.431  1.00 27.24 ? 7   PHE A CA  1 
ATOM   68   C  C   . PHE A 1 7   ? 9.412   9.368   19.630  1.00 32.71 ? 7   PHE A C   1 
ATOM   69   O  O   . PHE A 1 7   ? 10.256  10.251  19.493  1.00 35.20 ? 7   PHE A O   1 
ATOM   70   C  CB  . PHE A 1 7   ? 9.888   7.311   20.835  1.00 33.27 ? 7   PHE A CB  1 
ATOM   71   C  CG  . PHE A 1 7   ? 10.453  8.318   21.804  1.00 36.13 ? 7   PHE A CG  1 
ATOM   72   C  CD1 . PHE A 1 7   ? 11.824  8.453   21.973  1.00 38.86 ? 7   PHE A CD1 1 
ATOM   73   C  CD2 . PHE A 1 7   ? 9.614   9.195   22.489  1.00 43.54 ? 7   PHE A CD2 1 
ATOM   74   C  CE1 . PHE A 1 7   ? 12.344  9.421   22.821  1.00 42.87 ? 7   PHE A CE1 1 
ATOM   75   C  CE2 . PHE A 1 7   ? 10.137  10.167  23.332  1.00 45.88 ? 7   PHE A CE2 1 
ATOM   76   C  CZ  . PHE A 1 7   ? 11.502  10.282  23.492  1.00 42.14 ? 7   PHE A CZ  1 
ATOM   77   N  N   . GLY A 1 8   ? 8.151   9.581   20.005  1.00 28.22 ? 8   GLY A N   1 
ATOM   78   C  CA  . GLY A 1 8   ? 7.607   10.894  20.331  1.00 28.60 ? 8   GLY A CA  1 
ATOM   79   C  C   . GLY A 1 8   ? 7.551   11.725  19.060  1.00 31.40 ? 8   GLY A C   1 
ATOM   80   O  O   . GLY A 1 8   ? 7.444   11.158  17.954  1.00 31.68 ? 8   GLY A O   1 
ATOM   81   N  N   . PRO A 1 9   ? 7.614   13.067  19.160  1.00 24.33 ? 9   PRO A N   1 
ATOM   82   C  CA  . PRO A 1 9   ? 7.498   13.879  17.961  1.00 24.20 ? 9   PRO A CA  1 
ATOM   83   C  C   . PRO A 1 9   ? 8.808   14.064  17.209  1.00 20.71 ? 9   PRO A C   1 
ATOM   84   O  O   . PRO A 1 9   ? 8.741   14.592  16.132  1.00 19.08 ? 9   PRO A O   1 
ATOM   85   C  CB  . PRO A 1 9   ? 6.930   15.203  18.496  1.00 28.88 ? 9   PRO A CB  1 
ATOM   86   C  CG  . PRO A 1 9   ? 7.589   15.302  19.851  1.00 25.86 ? 9   PRO A CG  1 
ATOM   87   C  CD  . PRO A 1 9   ? 7.641   13.882  20.399  1.00 27.40 ? 9   PRO A CD  1 
ATOM   88   N  N   . ASP A 1 10  ? 9.959   13.582  17.735  1.00 19.92 ? 10  ASP A N   1 
ATOM   89   C  CA  . ASP A 1 10  ? 11.204  13.683  16.989  1.00 17.37 ? 10  ASP A CA  1 
ATOM   90   C  C   . ASP A 1 10  ? 11.655  12.338  16.400  1.00 15.32 ? 10  ASP A C   1 
ATOM   91   O  O   . ASP A 1 10  ? 12.815  12.214  15.978  1.00 13.19 ? 10  ASP A O   1 
ATOM   92   C  CB  . ASP A 1 10  ? 12.323  14.320  17.832  1.00 20.83 ? 10  ASP A CB  1 
ATOM   93   C  CG  . ASP A 1 10  ? 12.014  15.760  18.228  1.00 27.78 ? 10  ASP A CG  1 
ATOM   94   O  OD1 . ASP A 1 10  ? 11.509  16.528  17.365  1.00 29.58 ? 10  ASP A OD1 1 
ATOM   95   O  OD2 . ASP A 1 10  ? 12.239  16.085  19.412  1.00 36.58 ? 10  ASP A OD2 1 
ATOM   96   N  N   . GLY A 1 11  ? 10.702  11.412  16.361  1.00 14.98 ? 11  GLY A N   1 
ATOM   97   C  CA  . GLY A 1 11  ? 10.875  10.048  15.864  1.00 12.38 ? 11  GLY A CA  1 
ATOM   98   C  C   . GLY A 1 11  ? 10.899  9.998   14.338  1.00 10.62 ? 11  GLY A C   1 
ATOM   99   O  O   . GLY A 1 11  ? 10.954  11.009  13.603  1.00 11.18 ? 11  GLY A O   1 
ATOM   100  N  N   . GLU A 1 12  ? 10.927  8.750   13.826  1.00 9.67  ? 12  GLU A N   1 
ATOM   101  C  CA  . GLU A 1 12  ? 11.371  8.525   12.470  1.00 8.91  ? 12  GLU A CA  1 
ATOM   102  C  C   . GLU A 1 12  ? 10.500  9.208   11.411  1.00 8.92  ? 12  GLU A C   1 
ATOM   103  O  O   . GLU A 1 12  ? 11.012  9.517   10.338  1.00 9.21  ? 12  GLU A O   1 
ATOM   104  C  CB  . GLU A 1 12  ? 11.560  7.022   12.199  1.00 8.98  ? 12  GLU A CB  1 
ATOM   105  C  CG  . GLU A 1 12  ? 10.249  6.249   12.151  1.00 9.34  ? 12  GLU A CG  1 
ATOM   106  C  CD  . GLU A 1 12  ? 10.560  4.761   12.282  1.00 9.13  ? 12  GLU A CD  1 
ATOM   107  O  OE1 . GLU A 1 12  ? 10.817  4.125   11.279  1.00 9.28  ? 12  GLU A OE1 1 
ATOM   108  O  OE2 . GLU A 1 12  ? 10.524  4.323   13.465  1.00 11.21 ? 12  GLU A OE2 1 
ATOM   109  N  N   . ASN A 1 13  ? 9.191   9.367   11.674  1.00 8.87  ? 13  ASN A N   1 
ATOM   110  C  CA  . ASN A 1 13  ? 8.349   10.026  10.668  1.00 8.73  ? 13  ASN A CA  1 
ATOM   111  C  C   . ASN A 1 13  ? 8.691   11.508  10.484  1.00 9.68  ? 13  ASN A C   1 
ATOM   112  O  O   . ASN A 1 13  ? 8.291   12.055  9.464   1.00 9.88  ? 13  ASN A O   1 
ATOM   113  C  CB  . ASN A 1 13  ? 6.852   9.909   10.960  1.00 8.94  ? 13  ASN A CB  1 
ATOM   114  C  CG  . ASN A 1 13  ? 6.386   8.476   10.807  1.00 9.00  ? 13  ASN A CG  1 
ATOM   115  O  OD1 . ASN A 1 13  ? 7.088   7.578   10.313  1.00 10.35 ? 13  ASN A OD1 1 
ATOM   116  N  ND2 . ASN A 1 13  ? 5.191   8.240   11.290  1.00 9.12  ? 13  ASN A ND2 1 
ATOM   117  N  N   . SER A 1 14  ? 9.420   12.060  11.456  1.00 9.13  ? 14  SER A N   1 
ATOM   118  C  CA  . SER A 1 14  ? 9.792   13.495  11.457  1.00 9.26  ? 14  SER A CA  1 
ATOM   119  C  C   . SER A 1 14  ? 11.254  13.692  11.059  1.00 10.36 ? 14  SER A C   1 
ATOM   120  O  O   . SER A 1 14  ? 11.648  14.845  10.893  1.00 10.72 ? 14  SER A O   1 
ATOM   121  C  CB  . SER A 1 14  ? 9.578   14.140  12.808  1.00 12.06 ? 14  SER A CB  1 
ATOM   122  O  OG  . SER A 1 14  ? 8.168   14.157  13.022  1.00 16.53 ? 14  SER A OG  1 
ATOM   123  N  N   . TRP A 1 15  ? 12.048  12.624  10.873  1.00 8.79  ? 15  TRP A N   1 
ATOM   124  C  CA  . TRP A 1 15  ? 13.467  12.829  10.544  1.00 8.62  ? 15  TRP A CA  1 
ATOM   125  C  C   . TRP A 1 15  ? 13.642  13.661  9.273   1.00 9.56  ? 15  TRP A C   1 
ATOM   126  O  O   . TRP A 1 15  ? 14.587  14.460  9.198   1.00 9.20  ? 15  TRP A O   1 
ATOM   127  C  CB  . TRP A 1 15  ? 14.145  11.482  10.335  1.00 8.16  ? 15  TRP A CB  1 
ATOM   128  C  CG  . TRP A 1 15  ? 14.301  10.638  11.568  1.00 8.83  ? 15  TRP A CG  1 
ATOM   129  C  CD1 . TRP A 1 15  ? 14.054  10.942  12.861  1.00 8.38  ? 15  TRP A CD1 1 
ATOM   130  C  CD2 . TRP A 1 15  ? 14.727  9.257   11.562  1.00 7.80  ? 15  TRP A CD2 1 
ATOM   131  N  NE1 . TRP A 1 15  ? 14.364  9.875   13.678  1.00 8.37  ? 15  TRP A NE1 1 
ATOM   132  C  CE2 . TRP A 1 15  ? 14.821  8.844   12.901  1.00 7.49  ? 15  TRP A CE2 1 
ATOM   133  C  CE3 . TRP A 1 15  ? 15.179  8.413   10.544  1.00 8.08  ? 15  TRP A CE3 1 
ATOM   134  C  CZ2 . TRP A 1 15  ? 15.220  7.534   13.225  1.00 7.45  ? 15  TRP A CZ2 1 
ATOM   135  C  CZ3 . TRP A 1 15  ? 15.609  7.143   10.869  1.00 8.11  ? 15  TRP A CZ3 1 
ATOM   136  C  CH2 . TRP A 1 15  ? 15.621  6.727   12.185  1.00 7.88  ? 15  TRP A CH2 1 
ATOM   137  N  N   . SER A 1 16  ? 12.738  13.540  8.306   1.00 8.88  ? 16  SER A N   1 
ATOM   138  C  CA  . SER A 1 16  ? 12.912  14.195  7.022   1.00 9.29  ? 16  SER A CA  1 
ATOM   139  C  C   . SER A 1 16  ? 12.818  15.720  7.121   1.00 9.66  ? 16  SER A C   1 
ATOM   140  O  O   . SER A 1 16  ? 13.252  16.373  6.144   1.00 9.31  ? 16  SER A O   1 
ATOM   141  C  CB  . SER A 1 16  ? 11.914  13.685  6.034   1.00 9.81  ? 16  SER A CB  1 
ATOM   142  O  OG  . SER A 1 16  ? 10.592  14.081  6.454   1.00 11.74 ? 16  SER A OG  1 
ATOM   143  N  N   A LYS A 1 17  ? 12.271  16.233  8.217   0.50 9.43  ? 17  LYS A N   1 
ATOM   144  N  N   B LYS A 1 17  ? 12.304  16.210  8.252   0.50 9.49  ? 17  LYS A N   1 
ATOM   145  C  CA  A LYS A 1 17  ? 12.252  17.695  8.328   0.50 10.08 ? 17  LYS A CA  1 
ATOM   146  C  CA  B LYS A 1 17  ? 12.207  17.666  8.349   0.50 10.38 ? 17  LYS A CA  1 
ATOM   147  C  C   A LYS A 1 17  ? 13.695  18.221  8.286   0.50 9.49  ? 17  LYS A C   1 
ATOM   148  C  C   B LYS A 1 17  ? 13.582  18.316  8.487   0.50 10.22 ? 17  LYS A C   1 
ATOM   149  O  O   A LYS A 1 17  ? 14.084  19.053  7.428   0.50 8.68  ? 17  LYS A O   1 
ATOM   150  O  O   B LYS A 1 17  ? 13.767  19.408  8.019   0.50 10.30 ? 17  LYS A O   1 
ATOM   151  C  CB  A LYS A 1 17  ? 11.519  18.091  9.605   0.50 10.69 ? 17  LYS A CB  1 
ATOM   152  C  CB  B LYS A 1 17  ? 11.413  18.170  9.537   0.50 10.95 ? 17  LYS A CB  1 
ATOM   153  C  CG  A LYS A 1 17  ? 10.056  17.670  9.663   0.50 12.74 ? 17  LYS A CG  1 
ATOM   154  C  CG  B LYS A 1 17  ? 11.416  19.696  9.570   0.50 11.83 ? 17  LYS A CG  1 
ATOM   155  C  CD  A LYS A 1 17  ? 9.447   17.846  11.027  0.50 13.89 ? 17  LYS A CD  1 
ATOM   156  C  CD  B LYS A 1 17  ? 10.515  20.232  10.642  0.50 14.16 ? 17  LYS A CD  1 
ATOM   157  C  CE  A LYS A 1 17  ? 8.090   17.163  11.157  0.50 15.04 ? 17  LYS A CE  1 
ATOM   158  C  CE  B LYS A 1 17  ? 9.039   19.975  10.418  0.50 15.78 ? 17  LYS A CE  1 
ATOM   159  N  NZ  A LYS A 1 17  ? 7.521   17.350  12.521  0.50 16.15 ? 17  LYS A NZ  1 
ATOM   160  N  NZ  B LYS A 1 17  ? 8.240   20.250  11.641  0.50 15.94 ? 17  LYS A NZ  1 
ATOM   161  N  N   . LYS A 1 18  ? 14.505  17.736  9.257   1.00 10.18 ? 18  LYS A N   1 
ATOM   162  C  CA  . LYS A 1 18  ? 15.861  18.256  9.382   1.00 11.64 ? 18  LYS A CA  1 
ATOM   163  C  C   . LYS A 1 18  ? 16.856  17.486  8.508   1.00 12.67 ? 18  LYS A C   1 
ATOM   164  O  O   . LYS A 1 18  ? 17.952  17.981  8.183   1.00 13.88 ? 18  LYS A O   1 
ATOM   165  C  CB  . LYS A 1 18  ? 16.309  18.160  10.837  1.00 14.76 ? 18  LYS A CB  1 
ATOM   166  C  CG  . LYS A 1 18  ? 17.751  18.557  11.135  1.00 21.89 ? 18  LYS A CG  1 
ATOM   167  C  CD  . LYS A 1 18  ? 18.119  18.423  12.617  1.00 28.08 ? 18  LYS A CD  1 
ATOM   168  C  CE  . LYS A 1 18  ? 19.541  18.891  12.858  1.00 31.23 ? 18  LYS A CE  1 
ATOM   169  N  NZ  . LYS A 1 18  ? 19.858  19.022  14.303  1.00 42.20 ? 18  LYS A NZ  1 
ATOM   170  N  N   . TYR A 1 19  ? 16.537  16.259  8.083   1.00 10.34 ? 19  TYR A N   1 
ATOM   171  C  CA  . TYR A 1 19  ? 17.422  15.400  7.325   1.00 9.93  ? 19  TYR A CA  1 
ATOM   172  C  C   . TYR A 1 19  ? 16.733  14.958  6.037   1.00 10.44 ? 19  TYR A C   1 
ATOM   173  O  O   . TYR A 1 19  ? 16.072  13.890  5.998   1.00 9.08  ? 19  TYR A O   1 
ATOM   174  C  CB  . TYR A 1 19  ? 17.800  14.185  8.183   1.00 10.33 ? 19  TYR A CB  1 
ATOM   175  C  CG  . TYR A 1 19  ? 18.472  14.549  9.480   1.00 10.76 ? 19  TYR A CG  1 
ATOM   176  C  CD1 . TYR A 1 19  ? 19.834  14.861  9.505   1.00 10.85 ? 19  TYR A CD1 1 
ATOM   177  C  CD2 . TYR A 1 19  ? 17.764  14.586  10.660  1.00 10.26 ? 19  TYR A CD2 1 
ATOM   178  C  CE1 . TYR A 1 19  ? 20.451  15.173  10.713  1.00 12.76 ? 19  TYR A CE1 1 
ATOM   179  C  CE2 . TYR A 1 19  ? 18.368  14.896  11.866  1.00 11.99 ? 19  TYR A CE2 1 
ATOM   180  C  CZ  . TYR A 1 19  ? 19.720  15.170  11.882  1.00 12.71 ? 19  TYR A CZ  1 
ATOM   181  O  OH  . TYR A 1 19  ? 20.334  15.486  13.086  1.00 17.31 ? 19  TYR A OH  1 
ATOM   182  N  N   . PRO A 1 20  ? 16.734  15.776  4.971   1.00 9.35  ? 20  PRO A N   1 
ATOM   183  C  CA  . PRO A 1 20  ? 15.828  15.547  3.863   1.00 9.07  ? 20  PRO A CA  1 
ATOM   184  C  C   . PRO A 1 20  ? 16.035  14.198  3.193   1.00 9.85  ? 20  PRO A C   1 
ATOM   185  O  O   . PRO A 1 20  ? 15.124  13.643  2.576   1.00 9.91  ? 20  PRO A O   1 
ATOM   186  C  CB  . PRO A 1 20  ? 16.122  16.695  2.896   1.00 11.44 ? 20  PRO A CB  1 
ATOM   187  C  CG  . PRO A 1 20  ? 16.758  17.755  3.788   1.00 13.11 ? 20  PRO A CG  1 
ATOM   188  C  CD  . PRO A 1 20  ? 17.470  17.071  4.933   1.00 10.18 ? 20  PRO A CD  1 
ATOM   189  N  N   . SER A 1 21  ? 17.254  13.640  3.282   1.00 9.41  ? 21  SER A N   1 
ATOM   190  C  CA  . SER A 1 21  ? 17.470  12.331  2.647   1.00 9.65  ? 21  SER A CA  1 
ATOM   191  C  C   . SER A 1 21  ? 16.594  11.235  3.288   1.00 9.21  ? 21  SER A C   1 
ATOM   192  O  O   . SER A 1 21  ? 16.390  10.227  2.618   1.00 8.48  ? 21  SER A O   1 
ATOM   193  C  CB  . SER A 1 21  ? 18.977  11.920  2.671   1.00 10.01 ? 21  SER A CB  1 
ATOM   194  O  OG  . SER A 1 21  ? 19.702  12.759  1.753   1.00 12.94 ? 21  SER A OG  1 
ATOM   195  N  N   . CYS A 1 22  ? 16.159  11.428  4.542   1.00 9.04  ? 22  CYS A N   1 
ATOM   196  C  CA  . CYS A 1 22  ? 15.319  10.423  5.177   1.00 9.52  ? 22  CYS A CA  1 
ATOM   197  C  C   . CYS A 1 22  ? 13.977  10.268  4.459   1.00 9.46  ? 22  CYS A C   1 
ATOM   198  O  O   . CYS A 1 22  ? 13.305  9.267   4.680   1.00 10.07 ? 22  CYS A O   1 
ATOM   199  C  CB  . CYS A 1 22  ? 15.120  10.730  6.644   1.00 9.96  ? 22  CYS A CB  1 
ATOM   200  S  SG  . CYS A 1 22  ? 16.681  10.793  7.564   1.00 9.97  ? 22  CYS A SG  1 
ATOM   201  N  N   . GLY A 1 23  ? 13.620  11.238  3.603   1.00 10.10 ? 23  GLY A N   1 
ATOM   202  C  CA  . GLY A 1 23  ? 12.425  11.147  2.753   1.00 10.20 ? 23  GLY A CA  1 
ATOM   203  C  C   . GLY A 1 23  ? 12.728  10.935  1.297   1.00 9.72  ? 23  GLY A C   1 
ATOM   204  O  O   . GLY A 1 23  ? 11.818  11.021  0.466   1.00 10.35 ? 23  GLY A O   1 
ATOM   205  N  N   . GLY A 1 24  ? 13.963  10.596  0.958   1.00 9.20  ? 24  GLY A N   1 
ATOM   206  C  CA  . GLY A 1 24  ? 14.380  10.438  -0.425  1.00 10.66 ? 24  GLY A CA  1 
ATOM   207  C  C   . GLY A 1 24  ? 14.468  8.979   -0.851  1.00 9.95  ? 24  GLY A C   1 
ATOM   208  O  O   . GLY A 1 24  ? 13.787  8.150   -0.242  1.00 12.18 ? 24  GLY A O   1 
ATOM   209  N  N   . LEU A 1 25  ? 15.251  8.721   -1.898  1.00 11.36 ? 25  LEU A N   1 
ATOM   210  C  CA  . LEU A 1 25  ? 15.361  7.406   -2.503  1.00 12.16 ? 25  LEU A CA  1 
ATOM   211  C  C   . LEU A 1 25  ? 16.288  6.500   -1.693  1.00 12.55 ? 25  LEU A C   1 
ATOM   212  O  O   . LEU A 1 25  ? 17.059  6.958   -0.835  1.00 12.01 ? 25  LEU A O   1 
ATOM   213  C  CB  . LEU A 1 25  ? 15.978  7.633   -3.880  1.00 16.43 ? 25  LEU A CB  1 
ATOM   214  C  CG  . LEU A 1 25  ? 15.185  8.551   -4.815  1.00 19.93 ? 25  LEU A CG  1 
ATOM   215  C  CD1 . LEU A 1 25  ? 15.832  8.594   -6.187  1.00 27.45 ? 25  LEU A CD1 1 
ATOM   216  C  CD2 . LEU A 1 25  ? 13.767  8.035   -4.930  1.00 21.01 ? 25  LEU A CD2 1 
ATOM   217  N  N   . LEU A 1 26  ? 16.169  5.217   -2.036  1.00 13.49 ? 26  LEU A N   1 
ATOM   218  C  CA  . LEU A 1 26  ? 17.085  4.152   -1.663  1.00 12.82 ? 26  LEU A CA  1 
ATOM   219  C  C   . LEU A 1 26  ? 17.094  3.946   -0.136  1.00 11.36 ? 26  LEU A C   1 
ATOM   220  O  O   . LEU A 1 26  ? 18.129  3.609   0.430   1.00 12.32 ? 26  LEU A O   1 
ATOM   221  C  CB  . LEU A 1 26  ? 18.514  4.380   -2.193  1.00 16.18 ? 26  LEU A CB  1 
ATOM   222  C  CG  . LEU A 1 26  ? 18.633  4.457   -3.723  1.00 21.53 ? 26  LEU A CG  1 
ATOM   223  C  CD1 . LEU A 1 26  ? 20.104  4.616   -4.152  1.00 23.89 ? 26  LEU A CD1 1 
ATOM   224  C  CD2 . LEU A 1 26  ? 18.005  3.255   -4.387  1.00 22.77 ? 26  LEU A CD2 1 
ATOM   225  N  N   . GLN A 1 27  ? 16.006  4.187   0.592   1.00 9.35  ? 27  GLN A N   1 
ATOM   226  C  CA  . GLN A 1 27  ? 16.049  4.096   2.043   1.00 8.48  ? 27  GLN A CA  1 
ATOM   227  C  C   . GLN A 1 27  ? 16.071  2.658   2.518   1.00 7.93  ? 27  GLN A C   1 
ATOM   228  O  O   . GLN A 1 27  ? 15.463  1.726   1.980   1.00 10.55 ? 27  GLN A O   1 
ATOM   229  C  CB  . GLN A 1 27  ? 14.880  4.848   2.668   1.00 8.49  ? 27  GLN A CB  1 
ATOM   230  C  CG  . GLN A 1 27  ? 14.939  6.345   2.349   1.00 7.72  ? 27  GLN A CG  1 
ATOM   231  C  CD  . GLN A 1 27  ? 16.104  6.967   3.049   1.00 7.86  ? 27  GLN A CD  1 
ATOM   232  O  OE1 . GLN A 1 27  ? 16.119  7.138   4.259   1.00 7.98  ? 27  GLN A OE1 1 
ATOM   233  N  NE2 . GLN A 1 27  ? 17.156  7.235   2.272   1.00 8.39  ? 27  GLN A NE2 1 
ATOM   234  N  N   . SER A 1 28  ? 16.790  2.484   3.624   1.00 7.57  ? 28  SER A N   1 
ATOM   235  C  CA  . SER A 1 28  ? 16.919  1.222   4.369   1.00 7.09  ? 28  SER A CA  1 
ATOM   236  C  C   . SER A 1 28  ? 16.344  1.421   5.758   1.00 7.57  ? 28  SER A C   1 
ATOM   237  O  O   . SER A 1 28  ? 16.268  2.547   6.277   1.00 7.67  ? 28  SER A O   1 
ATOM   238  C  CB  . SER A 1 28  ? 18.406  0.942   4.511   1.00 8.02  ? 28  SER A CB  1 
ATOM   239  O  OG  . SER A 1 28  ? 18.966  0.643   3.237   1.00 7.78  ? 28  SER A OG  1 
ATOM   240  N  N   . PRO A 1 29  ? 15.962  0.353   6.487   1.00 7.36  ? 29  PRO A N   1 
ATOM   241  C  CA  . PRO A 1 29  ? 16.082  -1.047  6.082   1.00 6.98  ? 29  PRO A CA  1 
ATOM   242  C  C   . PRO A 1 29  ? 14.833  -1.477  5.309   1.00 7.03  ? 29  PRO A C   1 
ATOM   243  O  O   . PRO A 1 29  ? 13.910  -0.685  5.110   1.00 8.28  ? 29  PRO A O   1 
ATOM   244  C  CB  . PRO A 1 29  ? 16.101  -1.772  7.460   1.00 7.23  ? 29  PRO A CB  1 
ATOM   245  C  CG  . PRO A 1 29  ? 15.118  -0.952  8.267   1.00 6.90  ? 29  PRO A CG  1 
ATOM   246  C  CD  . PRO A 1 29  ? 15.427  0.494   7.844   1.00 6.81  ? 29  PRO A CD  1 
ATOM   247  N  N   . ILE A 1 30  ? 14.837  -2.729  4.850   1.00 7.94  ? 30  ILE A N   1 
ATOM   248  C  CA  . ILE A 1 30  ? 13.811  -3.298  3.981   1.00 8.16  ? 30  ILE A CA  1 
ATOM   249  C  C   . ILE A 1 30  ? 13.577  -4.731  4.442   1.00 9.19  ? 30  ILE A C   1 
ATOM   250  O  O   . ILE A 1 30  ? 14.354  -5.316  5.237   1.00 9.64  ? 30  ILE A O   1 
ATOM   251  C  CB  . ILE A 1 30  ? 14.273  -3.328  2.507   1.00 9.93  ? 30  ILE A CB  1 
ATOM   252  C  CG1 . ILE A 1 30  ? 15.521  -4.213  2.313   1.00 10.72 ? 30  ILE A CG1 1 
ATOM   253  C  CG2 . ILE A 1 30  ? 14.509  -1.884  2.017   1.00 11.52 ? 30  ILE A CG2 1 
ATOM   254  C  CD1 . ILE A 1 30  ? 15.822  -4.423  0.834   1.00 12.36 ? 30  ILE A CD1 1 
ATOM   255  N  N   . ASP A 1 31  ? 12.420  -5.232  4.012   1.00 9.35  ? 31  ASP A N   1 
ATOM   256  C  CA  . ASP A 1 31  ? 12.064  -6.611  4.230   1.00 9.63  ? 31  ASP A CA  1 
ATOM   257  C  C   . ASP A 1 31  ? 12.681  -7.450  3.125   1.00 10.57 ? 31  ASP A C   1 
ATOM   258  O  O   . ASP A 1 31  ? 12.507  -7.214  1.927   1.00 12.38 ? 31  ASP A O   1 
ATOM   259  C  CB  . ASP A 1 31  ? 10.545  -6.753  4.163   1.00 10.45 ? 31  ASP A CB  1 
ATOM   260  C  CG  . ASP A 1 31  ? 10.086  -8.181  4.402   1.00 12.29 ? 31  ASP A CG  1 
ATOM   261  O  OD1 . ASP A 1 31  ? 10.651  -8.882  5.275   1.00 11.63 ? 31  ASP A OD1 1 
ATOM   262  O  OD2 . ASP A 1 31  ? 9.119   -8.568  3.746   1.00 16.30 ? 31  ASP A OD2 1 
ATOM   263  N  N   . LEU A 1 32  ? 13.448  -8.449  3.501   1.00 10.42 ? 32  LEU A N   1 
ATOM   264  C  CA  . LEU A 1 32  ? 14.090  -9.362  2.572   1.00 11.47 ? 32  LEU A CA  1 
ATOM   265  C  C   . LEU A 1 32  ? 13.164  -10.552 2.373   1.00 13.05 ? 32  LEU A C   1 
ATOM   266  O  O   . LEU A 1 32  ? 12.997  -11.365 3.259   1.00 13.87 ? 32  LEU A O   1 
ATOM   267  C  CB  . LEU A 1 32  ? 15.435  -9.795  3.200   1.00 12.57 ? 32  LEU A CB  1 
ATOM   268  C  CG  . LEU A 1 32  ? 16.355  -8.626  3.620   1.00 11.17 ? 32  LEU A CG  1 
ATOM   269  C  CD1 . LEU A 1 32  ? 17.591  -9.083  4.382   1.00 13.97 ? 32  LEU A CD1 1 
ATOM   270  C  CD2 . LEU A 1 32  ? 16.764  -7.836  2.385   1.00 14.81 ? 32  LEU A CD2 1 
ATOM   271  N  N   . HIS A 1 33  ? 12.453  -10.577 1.246   1.00 16.12 ? 33  HIS A N   1 
ATOM   272  C  CA  . HIS A 1 33  ? 11.471  -11.651 1.105   1.00 17.19 ? 33  HIS A CA  1 
ATOM   273  C  C   . HIS A 1 33  ? 11.606  -12.204 -0.293  1.00 19.41 ? 33  HIS A C   1 
ATOM   274  O  O   . HIS A 1 33  ? 12.073  -11.492 -1.167  1.00 18.63 ? 33  HIS A O   1 
ATOM   275  C  CB  . HIS A 1 33  ? 10.064  -11.117 1.427   1.00 19.88 ? 33  HIS A CB  1 
ATOM   276  C  CG  . HIS A 1 33  ? 9.598   -10.020 0.526   1.00 21.10 ? 33  HIS A CG  1 
ATOM   277  N  ND1 . HIS A 1 33  ? 9.964   -8.700  0.698   1.00 23.11 ? 33  HIS A ND1 1 
ATOM   278  C  CD2 . HIS A 1 33  ? 8.792   -10.066 -0.566  1.00 24.84 ? 33  HIS A CD2 1 
ATOM   279  C  CE1 . HIS A 1 33  ? 9.394   -7.969  -0.263  1.00 26.47 ? 33  HIS A CE1 1 
ATOM   280  N  NE2 . HIS A 1 33  ? 8.705   -8.790  -1.061  1.00 26.54 ? 33  HIS A NE2 1 
ATOM   281  N  N   . SER A 1 34  ? 11.086  -13.418 -0.486  1.00 20.76 ? 34  SER A N   1 
ATOM   282  C  CA  . SER A 1 34  ? 11.477  -14.277 -1.587  1.00 24.84 ? 34  SER A CA  1 
ATOM   283  C  C   . SER A 1 34  ? 11.136  -13.654 -2.944  1.00 25.57 ? 34  SER A C   1 
ATOM   284  O  O   . SER A 1 34  ? 11.904  -13.829 -3.883  1.00 28.13 ? 34  SER A O   1 
ATOM   285  C  CB  . SER A 1 34  ? 10.895  -15.660 -1.415  1.00 30.07 ? 34  SER A CB  1 
ATOM   286  O  OG  . SER A 1 34  ? 9.489   -15.579 -1.524  1.00 38.29 ? 34  SER A OG  1 
ATOM   287  N  N   . ASP A 1 35  ? 10.039  -12.886 -3.038  1.00 26.10 ? 35  ASP A N   1 
ATOM   288  C  CA  . ASP A 1 35  ? 9.610   -12.360 -4.331  1.00 30.63 ? 35  ASP A CA  1 
ATOM   289  C  C   . ASP A 1 35  ? 10.630  -11.382 -4.913  1.00 28.78 ? 35  ASP A C   1 
ATOM   290  O  O   . ASP A 1 35  ? 10.638  -11.174 -6.126  1.00 29.85 ? 35  ASP A O   1 
ATOM   291  C  CB  . ASP A 1 35  ? 8.214   -11.719 -4.279  1.00 34.58 ? 35  ASP A CB  1 
ATOM   292  C  CG  . ASP A 1 35  ? 7.066   -12.723 -4.322  1.00 46.04 ? 35  ASP A CG  1 
ATOM   293  O  OD1 . ASP A 1 35  ? 7.273   -13.851 -4.850  1.00 46.35 ? 35  ASP A OD1 1 
ATOM   294  O  OD2 . ASP A 1 35  ? 5.966   -12.381 -3.812  1.00 46.45 ? 35  ASP A OD2 1 
ATOM   295  N  N   . ILE A 1 36  ? 11.469  -10.755 -4.057  1.00 22.88 ? 36  ILE A N   1 
ATOM   296  C  CA  . ILE A 1 36  ? 12.370  -9.710  -4.534  1.00 21.21 ? 36  ILE A CA  1 
ATOM   297  C  C   . ILE A 1 36  ? 13.800  -10.227 -4.520  1.00 19.76 ? 36  ILE A C   1 
ATOM   298  O  O   . ILE A 1 36  ? 14.715  -9.430  -4.720  1.00 21.05 ? 36  ILE A O   1 
ATOM   299  C  CB  . ILE A 1 36  ? 12.260  -8.385  -3.750  1.00 20.80 ? 36  ILE A CB  1 
ATOM   300  C  CG1 . ILE A 1 36  ? 12.549  -8.633  -2.259  1.00 22.27 ? 36  ILE A CG1 1 
ATOM   301  C  CG2 . ILE A 1 36  ? 10.958  -7.631  -4.020  1.00 21.91 ? 36  ILE A CG2 1 
ATOM   302  C  CD1 . ILE A 1 36  ? 12.899  -7.399  -1.500  1.00 23.42 ? 36  ILE A CD1 1 
ATOM   303  N  N   . LEU A 1 37  ? 14.009  -11.513 -4.240  1.00 17.83 ? 37  LEU A N   1 
ATOM   304  C  CA  . LEU A 1 37  ? 15.382  -12.032 -4.191  1.00 18.94 ? 37  LEU A CA  1 
ATOM   305  C  C   . LEU A 1 37  ? 15.825  -12.552 -5.549  1.00 22.04 ? 37  LEU A C   1 
ATOM   306  O  O   . LEU A 1 37  ? 15.059  -13.218 -6.245  1.00 24.91 ? 37  LEU A O   1 
ATOM   307  C  CB  . LEU A 1 37  ? 15.478  -13.172 -3.174  1.00 17.87 ? 37  LEU A CB  1 
ATOM   308  C  CG  . LEU A 1 37  ? 15.079  -12.861 -1.726  1.00 20.04 ? 37  LEU A CG  1 
ATOM   309  C  CD1 . LEU A 1 37  ? 15.357  -14.077 -0.845  1.00 21.45 ? 37  LEU A CD1 1 
ATOM   310  C  CD2 . LEU A 1 37  ? 15.804  -11.641 -1.178  1.00 18.37 ? 37  LEU A CD2 1 
ATOM   311  N  N   . GLN A 1 38  ? 17.083  -12.330 -5.899  1.00 18.79 ? 38  GLN A N   1 
ATOM   312  C  CA  . GLN A 1 38  ? 17.604  -12.901 -7.143  1.00 21.41 ? 38  GLN A CA  1 
ATOM   313  C  C   . GLN A 1 38  ? 19.043  -13.346 -6.942  1.00 19.37 ? 38  GLN A C   1 
ATOM   314  O  O   . GLN A 1 38  ? 19.908  -12.528 -6.571  1.00 15.68 ? 38  GLN A O   1 
ATOM   315  C  CB  . GLN A 1 38  ? 17.560  -11.889 -8.287  1.00 23.32 ? 38  GLN A CB  1 
ATOM   316  C  CG  . GLN A 1 38  ? 17.954  -12.523 -9.621  1.00 27.54 ? 38  GLN A CG  1 
ATOM   317  C  CD  . GLN A 1 38  ? 17.866  -11.523 -10.749 1.00 32.65 ? 38  GLN A CD  1 
ATOM   318  O  OE1 . GLN A 1 38  ? 16.780  -11.091 -11.135 1.00 33.61 ? 38  GLN A OE1 1 
ATOM   319  N  NE2 . GLN A 1 38  ? 19.020  -11.111 -11.247 1.00 32.59 ? 38  GLN A NE2 1 
ATOM   320  N  N   . TYR A 1 39  ? 19.329  -14.627 -7.178  1.00 19.27 ? 39  TYR A N   1 
ATOM   321  C  CA  . TYR A 1 39  ? 20.675  -15.144 -7.147  1.00 17.96 ? 39  TYR A CA  1 
ATOM   322  C  C   . TYR A 1 39  ? 21.543  -14.388 -8.152  1.00 19.71 ? 39  TYR A C   1 
ATOM   323  O  O   . TYR A 1 39  ? 21.137  -14.146 -9.294  1.00 21.28 ? 39  TYR A O   1 
ATOM   324  C  CB  . TYR A 1 39  ? 20.655  -16.636 -7.523  1.00 17.30 ? 39  TYR A CB  1 
ATOM   325  C  CG  . TYR A 1 39  ? 22.019  -17.251 -7.594  1.00 21.18 ? 39  TYR A CG  1 
ATOM   326  C  CD1 . TYR A 1 39  ? 22.865  -17.240 -6.496  1.00 20.28 ? 39  TYR A CD1 1 
ATOM   327  C  CD2 . TYR A 1 39  ? 22.485  -17.848 -8.762  1.00 22.48 ? 39  TYR A CD2 1 
ATOM   328  C  CE1 . TYR A 1 39  ? 24.137  -17.792 -6.544  1.00 22.52 ? 39  TYR A CE1 1 
ATOM   329  C  CE2 . TYR A 1 39  ? 23.767  -18.369 -8.838  1.00 26.16 ? 39  TYR A CE2 1 
ATOM   330  C  CZ  . TYR A 1 39  ? 24.584  -18.382 -7.718  1.00 25.34 ? 39  TYR A CZ  1 
ATOM   331  O  OH  . TYR A 1 39  ? 25.842  -18.905 -7.798  1.00 32.38 ? 39  TYR A OH  1 
ATOM   332  N  N   . ASP A 1 40  ? 22.747  -14.018 -7.718  1.00 17.46 ? 40  ASP A N   1 
ATOM   333  C  CA  . ASP A 1 40  ? 23.714  -13.396 -8.592  1.00 18.95 ? 40  ASP A CA  1 
ATOM   334  C  C   . ASP A 1 40  ? 25.051  -14.077 -8.314  1.00 22.34 ? 40  ASP A C   1 
ATOM   335  O  O   . ASP A 1 40  ? 25.620  -13.931 -7.243  1.00 17.74 ? 40  ASP A O   1 
ATOM   336  C  CB  . ASP A 1 40  ? 23.741  -11.892 -8.323  1.00 19.51 ? 40  ASP A CB  1 
ATOM   337  C  CG  . ASP A 1 40  ? 24.740  -11.162 -9.216  1.00 21.87 ? 40  ASP A CG  1 
ATOM   338  O  OD1 . ASP A 1 40  ? 25.600  -11.835 -9.767  1.00 25.60 ? 40  ASP A OD1 1 
ATOM   339  O  OD2 . ASP A 1 40  ? 24.637  -9.911  -9.309  1.00 30.65 ? 40  ASP A OD2 1 
ATOM   340  N  N   . ALA A 1 41  ? 25.539  -14.867 -9.290  1.00 25.01 ? 41  ALA A N   1 
ATOM   341  C  CA  . ALA A 1 41  ? 26.795  -15.599 -9.155  1.00 26.31 ? 41  ALA A CA  1 
ATOM   342  C  C   . ALA A 1 41  ? 28.017  -14.675 -9.067  1.00 24.85 ? 41  ALA A C   1 
ATOM   343  O  O   . ALA A 1 41  ? 29.088  -15.127 -8.686  1.00 31.37 ? 41  ALA A O   1 
ATOM   344  C  CB  . ALA A 1 41  ? 26.953  -16.601 -10.290 1.00 30.50 ? 41  ALA A CB  1 
ATOM   345  N  N   . SER A 1 42  ? 27.868  -13.375 -9.371  1.00 26.88 ? 42  SER A N   1 
ATOM   346  C  CA  . SER A 1 42  ? 28.940  -12.397 -9.185  1.00 27.03 ? 42  SER A CA  1 
ATOM   347  C  C   . SER A 1 42  ? 29.256  -12.132 -7.704  1.00 28.90 ? 42  SER A C   1 
ATOM   348  O  O   . SER A 1 42  ? 30.228  -11.443 -7.358  1.00 28.36 ? 42  SER A O   1 
ATOM   349  C  CB  . SER A 1 42  ? 28.597  -11.110 -9.909  1.00 28.92 ? 42  SER A CB  1 
ATOM   350  O  OG  . SER A 1 42  ? 28.348  -10.041 -9.003  1.00 36.46 ? 42  SER A OG  1 
ATOM   351  N  N   . LEU A 1 43  ? 28.405  -12.621 -6.802  1.00 21.01 ? 43  LEU A N   1 
ATOM   352  C  CA  . LEU A 1 43  ? 28.564  -12.278 -5.386  1.00 20.00 ? 43  LEU A CA  1 
ATOM   353  C  C   . LEU A 1 43  ? 29.454  -13.296 -4.681  1.00 19.32 ? 43  LEU A C   1 
ATOM   354  O  O   . LEU A 1 43  ? 28.994  -14.228 -4.027  1.00 21.16 ? 43  LEU A O   1 
ATOM   355  C  CB  . LEU A 1 43  ? 27.177  -12.170 -4.743  1.00 16.06 ? 43  LEU A CB  1 
ATOM   356  C  CG  . LEU A 1 43  ? 26.316  -11.015 -5.251  1.00 15.89 ? 43  LEU A CG  1 
ATOM   357  C  CD1 . LEU A 1 43  ? 24.947  -11.013 -4.586  1.00 14.39 ? 43  LEU A CD1 1 
ATOM   358  C  CD2 . LEU A 1 43  ? 26.990  -9.644  -5.121  1.00 15.69 ? 43  LEU A CD2 1 
ATOM   359  N  N   . THR A 1 44  ? 30.756  -13.065 -4.772  1.00 19.36 ? 44  THR A N   1 
ATOM   360  C  CA  . THR A 1 44  ? 31.755  -13.967 -4.230  1.00 20.27 ? 44  THR A CA  1 
ATOM   361  C  C   . THR A 1 44  ? 31.981  -13.664 -2.745  1.00 18.94 ? 44  THR A C   1 
ATOM   362  O  O   . THR A 1 44  ? 31.501  -12.644 -2.237  1.00 17.68 ? 44  THR A O   1 
ATOM   363  C  CB  . THR A 1 44  ? 33.036  -13.816 -5.066  1.00 23.19 ? 44  THR A CB  1 
ATOM   364  O  OG1 . THR A 1 44  ? 33.401  -12.452 -4.908  1.00 26.89 ? 44  THR A OG1 1 
ATOM   365  C  CG2 . THR A 1 44  ? 32.768  -14.001 -6.542  1.00 28.40 ? 44  THR A CG2 1 
ATOM   366  N  N   . PRO A 1 45  ? 32.665  -14.543 -1.993  1.00 18.85 ? 45  PRO A N   1 
ATOM   367  C  CA  . PRO A 1 45  ? 32.889  -14.302 -0.566  1.00 17.98 ? 45  PRO A CA  1 
ATOM   368  C  C   . PRO A 1 45  ? 33.742  -13.074 -0.312  1.00 19.80 ? 45  PRO A C   1 
ATOM   369  O  O   . PRO A 1 45  ? 34.694  -12.779 -1.042  1.00 23.68 ? 45  PRO A O   1 
ATOM   370  C  CB  . PRO A 1 45  ? 33.587  -15.578 -0.079  1.00 21.31 ? 45  PRO A CB  1 
ATOM   371  C  CG  . PRO A 1 45  ? 33.201  -16.623 -1.116  1.00 21.05 ? 45  PRO A CG  1 
ATOM   372  C  CD  . PRO A 1 45  ? 33.160  -15.876 -2.425  1.00 20.78 ? 45  PRO A CD  1 
ATOM   373  N  N   . LEU A 1 46  ? 33.365  -12.316 0.710   1.00 15.76 ? 46  LEU A N   1 
ATOM   374  C  CA  . LEU A 1 46  ? 34.206  -11.236 1.176   1.00 15.38 ? 46  LEU A CA  1 
ATOM   375  C  C   . LEU A 1 46  ? 35.317  -11.780 2.063   1.00 14.32 ? 46  LEU A C   1 
ATOM   376  O  O   . LEU A 1 46  ? 35.140  -12.836 2.681   1.00 18.82 ? 46  LEU A O   1 
ATOM   377  C  CB  . LEU A 1 46  ? 33.364  -10.260 2.007   1.00 15.47 ? 46  LEU A CB  1 
ATOM   378  C  CG  . LEU A 1 46  ? 32.249  -9.528  1.262   1.00 15.93 ? 46  LEU A CG  1 
ATOM   379  C  CD1 . LEU A 1 46  ? 31.465  -8.634  2.209   1.00 17.05 ? 46  LEU A CD1 1 
ATOM   380  C  CD2 . LEU A 1 46  ? 32.811  -8.741  0.077   1.00 18.97 ? 46  LEU A CD2 1 
ATOM   381  N  N   . GLU A 1 47  ? 36.384  -11.009 2.152   1.00 14.96 ? 47  GLU A N   1 
ATOM   382  C  CA  . GLU A 1 47  ? 37.420  -11.384 3.080   1.00 16.22 ? 47  GLU A CA  1 
ATOM   383  C  C   . GLU A 1 47  ? 37.554  -10.271 4.108   1.00 14.72 ? 47  GLU A C   1 
ATOM   384  O  O   . GLU A 1 47  ? 37.537  -9.075  3.774   1.00 16.81 ? 47  GLU A O   1 
ATOM   385  C  CB  . GLU A 1 47  ? 38.754  -11.564 2.355   1.00 20.70 ? 47  GLU A CB  1 
ATOM   386  C  CG  . GLU A 1 47  ? 38.760  -12.733 1.385   1.00 30.57 ? 47  GLU A CG  1 
ATOM   387  C  CD  . GLU A 1 47  ? 39.983  -12.742 0.473   1.00 42.95 ? 47  GLU A CD  1 
ATOM   388  O  OE1 . GLU A 1 47  ? 39.796  -12.673 -0.769  1.00 47.44 ? 47  GLU A OE1 1 
ATOM   389  O  OE2 . GLU A 1 47  ? 41.130  -12.797 1.005   1.00 45.61 ? 47  GLU A OE2 1 
ATOM   390  N  N   . PHE A 1 48  ? 37.738  -10.663 5.378   1.00 14.73 ? 48  PHE A N   1 
ATOM   391  C  CA  . PHE A 1 48  ? 37.737  -9.729  6.469   1.00 14.18 ? 48  PHE A CA  1 
ATOM   392  C  C   . PHE A 1 48  ? 39.172  -9.629  6.942   1.00 15.31 ? 48  PHE A C   1 
ATOM   393  O  O   . PHE A 1 48  ? 39.685  -10.602 7.505   1.00 19.05 ? 48  PHE A O   1 
ATOM   394  C  CB  . PHE A 1 48  ? 36.763  -10.220 7.544   1.00 15.18 ? 48  PHE A CB  1 
ATOM   395  C  CG  . PHE A 1 48  ? 35.424  -10.603 6.966   1.00 13.94 ? 48  PHE A CG  1 
ATOM   396  C  CD1 . PHE A 1 48  ? 34.550  -9.628  6.489   1.00 14.64 ? 48  PHE A CD1 1 
ATOM   397  C  CD2 . PHE A 1 48  ? 35.059  -11.938 6.796   1.00 15.23 ? 48  PHE A CD2 1 
ATOM   398  C  CE1 . PHE A 1 48  ? 33.333  -9.980  5.892   1.00 13.57 ? 48  PHE A CE1 1 
ATOM   399  C  CE2 . PHE A 1 48  ? 33.856  -12.287 6.194   1.00 14.51 ? 48  PHE A CE2 1 
ATOM   400  C  CZ  . PHE A 1 48  ? 33.012  -11.296 5.710   1.00 13.52 ? 48  PHE A CZ  1 
ATOM   401  N  N   . GLN A 1 49  ? 39.803  -8.511  6.656   1.00 13.32 ? 49  GLN A N   1 
ATOM   402  C  CA  . GLN A 1 49  ? 41.243  -8.393  6.853   1.00 13.37 ? 49  GLN A CA  1 
ATOM   403  C  C   . GLN A 1 49  ? 41.478  -7.410  7.976   1.00 12.68 ? 49  GLN A C   1 
ATOM   404  O  O   . GLN A 1 49  ? 40.862  -6.347  8.104   1.00 12.76 ? 49  GLN A O   1 
ATOM   405  C  CB  . GLN A 1 49  ? 41.830  -7.743  5.598   1.00 15.45 ? 49  GLN A CB  1 
ATOM   406  C  CG  . GLN A 1 49  ? 41.684  -8.661  4.386   1.00 20.68 ? 49  GLN A CG  1 
ATOM   407  C  CD  . GLN A 1 49  ? 42.724  -8.583  3.289   1.00 25.70 ? 49  GLN A CD  1 
ATOM   408  O  OE1 . GLN A 1 49  ? 43.060  -9.605  2.677   1.00 31.36 ? 49  GLN A OE1 1 
ATOM   409  N  NE2 . GLN A 1 49  ? 43.201  -7.376  3.005   1.00 28.44 ? 49  GLN A NE2 1 
ATOM   410  N  N   . GLY A 1 50  ? 42.440  -7.724  8.860   1.00 14.07 ? 50  GLY A N   1 
ATOM   411  C  CA  . GLY A 1 50  ? 42.705  -6.875  9.998   1.00 13.48 ? 50  GLY A CA  1 
ATOM   412  C  C   . GLY A 1 50  ? 41.596  -6.849  11.067  1.00 12.40 ? 50  GLY A C   1 
ATOM   413  O  O   . GLY A 1 50  ? 41.606  -5.986  11.916  1.00 14.68 ? 50  GLY A O   1 
ATOM   414  N  N   . TYR A 1 51  ? 40.733  -7.866  11.049  1.00 13.03 ? 51  TYR A N   1 
ATOM   415  C  CA  . TYR A 1 51  ? 39.649  -7.992  12.033  1.00 13.49 ? 51  TYR A CA  1 
ATOM   416  C  C   . TYR A 1 51  ? 40.157  -8.509  13.372  1.00 14.00 ? 51  TYR A C   1 
ATOM   417  O  O   . TYR A 1 51  ? 39.473  -8.336  14.369  1.00 13.16 ? 51  TYR A O   1 
ATOM   418  C  CB  . TYR A 1 51  ? 38.533  -8.868  11.457  1.00 12.42 ? 51  TYR A CB  1 
ATOM   419  C  CG  . TYR A 1 51  ? 37.482  -8.143  10.628  1.00 11.79 ? 51  TYR A CG  1 
ATOM   420  C  CD1 . TYR A 1 51  ? 37.829  -7.264  9.589   1.00 12.26 ? 51  TYR A CD1 1 
ATOM   421  C  CD2 . TYR A 1 51  ? 36.121  -8.363  10.888  1.00 10.77 ? 51  TYR A CD2 1 
ATOM   422  C  CE1 . TYR A 1 51  ? 36.851  -6.650  8.798   1.00 11.84 ? 51  TYR A CE1 1 
ATOM   423  C  CE2 . TYR A 1 51  ? 35.150  -7.757  10.091  1.00 11.25 ? 51  TYR A CE2 1 
ATOM   424  C  CZ  . TYR A 1 51  ? 35.516  -6.863  9.113   1.00 12.01 ? 51  TYR A CZ  1 
ATOM   425  O  OH  . TYR A 1 51  ? 34.491  -6.236  8.420   1.00 12.89 ? 51  TYR A OH  1 
ATOM   426  N  N   . ASN A 1 52  ? 41.311  -9.203  13.370  1.00 15.39 ? 52  ASN A N   1 
ATOM   427  C  CA  . ASN A 1 52  ? 41.843  -9.737  14.618  1.00 15.89 ? 52  ASN A CA  1 
ATOM   428  C  C   . ASN A 1 52  ? 42.583  -8.625  15.368  1.00 16.09 ? 52  ASN A C   1 
ATOM   429  O  O   . ASN A 1 52  ? 43.816  -8.513  15.222  1.00 21.55 ? 52  ASN A O   1 
ATOM   430  C  CB  . ASN A 1 52  ? 42.735  -10.947 14.346  1.00 16.77 ? 52  ASN A CB  1 
ATOM   431  C  CG  . ASN A 1 52  ? 43.071  -11.711 15.614  1.00 21.97 ? 52  ASN A CG  1 
ATOM   432  O  OD1 . ASN A 1 52  ? 42.482  -11.498 16.675  1.00 20.02 ? 52  ASN A OD1 1 
ATOM   433  N  ND2 . ASN A 1 52  ? 44.065  -12.579 15.507  1.00 27.97 ? 52  ASN A ND2 1 
ATOM   434  N  N   . LEU A 1 53  ? 41.866  -7.795  16.120  1.00 15.38 ? 53  LEU A N   1 
ATOM   435  C  CA  . LEU A 1 53  ? 42.437  -6.577  16.664  1.00 16.06 ? 53  LEU A CA  1 
ATOM   436  C  C   . LEU A 1 53  ? 43.423  -6.937  17.768  1.00 20.63 ? 53  LEU A C   1 
ATOM   437  O  O   . LEU A 1 53  ? 43.139  -7.770  18.609  1.00 19.45 ? 53  LEU A O   1 
ATOM   438  C  CB  . LEU A 1 53  ? 41.363  -5.649  17.248  1.00 15.72 ? 53  LEU A CB  1 
ATOM   439  C  CG  . LEU A 1 53  ? 40.279  -5.200  16.253  1.00 14.65 ? 53  LEU A CG  1 
ATOM   440  C  CD1 . LEU A 1 53  ? 39.251  -4.305  16.935  1.00 16.48 ? 53  LEU A CD1 1 
ATOM   441  C  CD2 . LEU A 1 53  ? 40.896  -4.590  14.992  1.00 17.86 ? 53  LEU A CD2 1 
ATOM   442  N  N   . SER A 1 54  ? 44.543  -6.218  17.762  1.00 21.05 ? 54  SER A N   1 
ATOM   443  C  CA  . SER A 1 54  ? 45.578  -6.337  18.771  1.00 22.37 ? 54  SER A CA  1 
ATOM   444  C  C   . SER A 1 54  ? 44.961  -6.313  20.161  1.00 21.98 ? 54  SER A C   1 
ATOM   445  O  O   . SER A 1 54  ? 44.348  -5.325  20.545  1.00 20.41 ? 54  SER A O   1 
ATOM   446  C  CB  . SER A 1 54  ? 46.531  -5.195  18.620  1.00 20.83 ? 54  SER A CB  1 
ATOM   447  O  OG  . SER A 1 54  ? 47.610  -5.402  19.541  1.00 24.99 ? 54  SER A OG  1 
ATOM   448  N  N   . ALA A 1 55  ? 45.192  -7.375  20.940  1.00 25.32 ? 55  ALA A N   1 
ATOM   449  C  CA  . ALA A 1 55  ? 44.787  -7.373  22.338  1.00 27.09 ? 55  ALA A CA  1 
ATOM   450  C  C   . ALA A 1 55  ? 45.633  -6.410  23.172  1.00 27.40 ? 55  ALA A C   1 
ATOM   451  O  O   . ALA A 1 55  ? 45.378  -6.280  24.348  1.00 27.65 ? 55  ALA A O   1 
ATOM   452  C  CB  . ALA A 1 55  ? 44.882  -8.772  22.894  1.00 34.76 ? 55  ALA A CB  1 
ATOM   453  N  N   . ASN A 1 56  ? 46.623  -5.741  22.566  1.00 28.40 ? 56  ASN A N   1 
ATOM   454  C  CA  . ASN A 1 56  ? 47.438  -4.747  23.259  1.00 29.26 ? 56  ASN A CA  1 
ATOM   455  C  C   . ASN A 1 56  ? 46.947  -3.333  22.949  1.00 31.18 ? 56  ASN A C   1 
ATOM   456  O  O   . ASN A 1 56  ? 47.534  -2.345  23.379  1.00 31.46 ? 56  ASN A O   1 
ATOM   457  C  CB  . ASN A 1 56  ? 48.919  -4.878  22.868  1.00 27.82 ? 56  ASN A CB  1 
ATOM   458  C  CG  . ASN A 1 56  ? 49.530  -6.177  23.345  1.00 32.62 ? 56  ASN A CG  1 
ATOM   459  O  OD1 . ASN A 1 56  ? 49.232  -6.650  24.443  1.00 33.49 ? 56  ASN A OD1 1 
ATOM   460  N  ND2 . ASN A 1 56  ? 50.365  -6.779  22.513  1.00 34.21 ? 56  ASN A ND2 1 
ATOM   461  N  N   . LYS A 1 57  ? 45.872  -3.232  22.151  1.00 23.58 ? 57  LYS A N   1 
ATOM   462  C  CA  . LYS A 1 57  ? 45.303  -1.937  21.820  1.00 21.60 ? 57  LYS A CA  1 
ATOM   463  C  C   . LYS A 1 57  ? 43.919  -1.839  22.461  1.00 18.80 ? 57  LYS A C   1 
ATOM   464  O  O   . LYS A 1 57  ? 43.317  -2.859  22.756  1.00 20.42 ? 57  LYS A O   1 
ATOM   465  C  CB  . LYS A 1 57  ? 45.132  -1.850  20.296  1.00 22.19 ? 57  LYS A CB  1 
ATOM   466  C  CG  . LYS A 1 57  ? 46.331  -1.312  19.530  1.00 27.47 ? 57  LYS A CG  1 
ATOM   467  C  CD  . LYS A 1 57  ? 45.979  -1.040  18.053  1.00 26.47 ? 57  LYS A CD  1 
ATOM   468  C  CE  . LYS A 1 57  ? 45.093  0.165   17.826  1.00 24.08 ? 57  LYS A CE  1 
ATOM   469  N  NZ  . LYS A 1 57  ? 45.214  0.690   16.434  1.00 30.61 ? 57  LYS A NZ  1 
ATOM   470  N  N   . GLN A 1 58  ? 43.501  -0.612  22.736  1.00 18.85 ? 58  GLN A N   1 
ATOM   471  C  CA  . GLN A 1 58  ? 42.164  -0.372  23.278  1.00 18.02 ? 58  GLN A CA  1 
ATOM   472  C  C   . GLN A 1 58  ? 41.315  0.407   22.297  1.00 18.60 ? 58  GLN A C   1 
ATOM   473  O  O   . GLN A 1 58  ? 41.775  1.352   21.649  1.00 20.66 ? 58  GLN A O   1 
ATOM   474  C  CB  . GLN A 1 58  ? 42.234  0.315   24.639  1.00 19.88 ? 58  GLN A CB  1 
ATOM   475  C  CG  . GLN A 1 58  ? 42.828  -0.631  25.647  1.00 21.56 ? 58  GLN A CG  1 
ATOM   476  C  CD  . GLN A 1 58  ? 43.113  0.016   26.971  1.00 23.73 ? 58  GLN A CD  1 
ATOM   477  O  OE1 . GLN A 1 58  ? 43.640  -0.653  27.858  1.00 25.46 ? 58  GLN A OE1 1 
ATOM   478  N  NE2 . GLN A 1 58  ? 42.805  1.300   27.068  1.00 22.10 ? 58  GLN A NE2 1 
ATOM   479  N  N   . PHE A 1 59  ? 40.034  -0.001  22.259  1.00 17.55 ? 59  PHE A N   1 
ATOM   480  C  CA  . PHE A 1 59  ? 39.086  0.581   21.317  1.00 16.90 ? 59  PHE A CA  1 
ATOM   481  C  C   . PHE A 1 59  ? 37.945  1.241   22.072  1.00 15.62 ? 59  PHE A C   1 
ATOM   482  O  O   . PHE A 1 59  ? 37.461  0.667   23.044  1.00 15.47 ? 59  PHE A O   1 
ATOM   483  C  CB  . PHE A 1 59  ? 38.627  -0.489  20.331  1.00 14.81 ? 59  PHE A CB  1 
ATOM   484  C  CG  . PHE A 1 59  ? 39.806  -1.019  19.549  1.00 16.08 ? 59  PHE A CG  1 
ATOM   485  C  CD1 . PHE A 1 59  ? 40.243  -0.415  18.382  1.00 16.52 ? 59  PHE A CD1 1 
ATOM   486  C  CD2 . PHE A 1 59  ? 40.569  -2.050  20.079  1.00 16.61 ? 59  PHE A CD2 1 
ATOM   487  C  CE1 . PHE A 1 59  ? 41.372  -0.889  17.710  1.00 18.10 ? 59  PHE A CE1 1 
ATOM   488  C  CE2 . PHE A 1 59  ? 41.699  -2.506  19.394  1.00 14.27 ? 59  PHE A CE2 1 
ATOM   489  C  CZ  . PHE A 1 59  ? 42.092  -1.937  18.213  1.00 17.17 ? 59  PHE A CZ  1 
ATOM   490  N  N   . LEU A 1 60  ? 37.566  2.428   21.641  1.00 15.77 ? 60  LEU A N   1 
ATOM   491  C  CA  . LEU A 1 60  ? 36.666  3.268   22.426  1.00 16.53 ? 60  LEU A CA  1 
ATOM   492  C  C   . LEU A 1 60  ? 35.207  2.834   22.216  1.00 16.87 ? 60  LEU A C   1 
ATOM   493  O  O   . LEU A 1 60  ? 34.709  2.818   21.078  1.00 14.83 ? 60  LEU A O   1 
ATOM   494  C  CB  . LEU A 1 60  ? 36.844  4.722   22.018  1.00 17.91 ? 60  LEU A CB  1 
ATOM   495  C  CG  . LEU A 1 60  ? 36.060  5.726   22.837  1.00 20.76 ? 60  LEU A CG  1 
ATOM   496  C  CD1 . LEU A 1 60  ? 36.641  5.834   24.254  1.00 22.62 ? 60  LEU A CD1 1 
ATOM   497  C  CD2 . LEU A 1 60  ? 36.042  7.084   22.148  1.00 22.99 ? 60  LEU A CD2 1 
ATOM   498  N  N   . LEU A 1 61  ? 34.509  2.464   23.277  1.00 14.39 ? 61  LEU A N   1 
ATOM   499  C  CA  . LEU A 1 61  ? 33.069  2.184   23.273  1.00 13.72 ? 61  LEU A CA  1 
ATOM   500  C  C   . LEU A 1 61  ? 32.351  3.407   23.805  1.00 14.51 ? 61  LEU A C   1 
ATOM   501  O  O   . LEU A 1 61  ? 32.759  3.950   24.830  1.00 16.08 ? 61  LEU A O   1 
ATOM   502  C  CB  . LEU A 1 61  ? 32.844  0.988   24.196  1.00 15.97 ? 61  LEU A CB  1 
ATOM   503  C  CG  . LEU A 1 61  ? 31.446  0.340   24.186  1.00 15.77 ? 61  LEU A CG  1 
ATOM   504  C  CD1 . LEU A 1 61  ? 31.224  -0.474  22.907  1.00 15.18 ? 61  LEU A CD1 1 
ATOM   505  C  CD2 . LEU A 1 61  ? 31.284  -0.601  25.364  1.00 17.48 ? 61  LEU A CD2 1 
ATOM   506  N  N   A THR A 1 62  ? 31.308  3.863   23.101  0.50 14.44 ? 62  THR A N   1 
ATOM   507  N  N   B THR A 1 62  ? 31.285  3.855   23.128  0.50 14.58 ? 62  THR A N   1 
ATOM   508  C  CA  A THR A 1 62  ? 30.546  5.027   23.504  0.50 14.26 ? 62  THR A CA  1 
ATOM   509  C  CA  B THR A 1 62  ? 30.549  5.008   23.603  0.50 14.47 ? 62  THR A CA  1 
ATOM   510  C  C   A THR A 1 62  ? 29.057  4.659   23.560  0.50 13.68 ? 62  THR A C   1 
ATOM   511  C  C   B THR A 1 62  ? 29.043  4.819   23.460  0.50 14.20 ? 62  THR A C   1 
ATOM   512  O  O   A THR A 1 62  ? 28.576  3.800   22.806  0.50 13.59 ? 62  THR A O   1 
ATOM   513  O  O   B THR A 1 62  ? 28.536  4.317   22.451  0.50 13.61 ? 62  THR A O   1 
ATOM   514  C  CB  A THR A 1 62  ? 30.823  6.235   22.578  0.50 16.79 ? 62  THR A CB  1 
ATOM   515  C  CB  B THR A 1 62  ? 30.888  6.290   22.829  0.50 17.07 ? 62  THR A CB  1 
ATOM   516  O  OG1 A THR A 1 62  ? 32.210  6.548   22.375  0.50 18.90 ? 62  THR A OG1 1 
ATOM   517  O  OG1 B THR A 1 62  ? 30.694  5.992   21.445  0.50 17.81 ? 62  THR A OG1 1 
ATOM   518  C  CG2 A THR A 1 62  ? 30.106  7.499   22.994  0.50 17.27 ? 62  THR A CG2 1 
ATOM   519  C  CG2 B THR A 1 62  ? 32.299  6.783   23.068  0.50 19.90 ? 62  THR A CG2 1 
ATOM   520  N  N   . ASN A 1 63  ? 28.335  5.345   24.447  1.00 13.38 ? 63  ASN A N   1 
ATOM   521  C  CA  . ASN A 1 63  ? 26.893  5.509   24.323  1.00 12.78 ? 63  ASN A CA  1 
ATOM   522  C  C   . ASN A 1 63  ? 26.658  6.883   23.710  1.00 13.61 ? 63  ASN A C   1 
ATOM   523  O  O   . ASN A 1 63  ? 26.968  7.928   24.292  1.00 14.51 ? 63  ASN A O   1 
ATOM   524  C  CB  . ASN A 1 63  ? 26.256  5.461   25.698  1.00 12.88 ? 63  ASN A CB  1 
ATOM   525  C  CG  . ASN A 1 63  ? 24.772  5.694   25.734  1.00 13.14 ? 63  ASN A CG  1 
ATOM   526  O  OD1 . ASN A 1 63  ? 24.218  6.356   24.865  1.00 13.74 ? 63  ASN A OD1 1 
ATOM   527  N  ND2 . ASN A 1 63  ? 24.159  5.183   26.792  1.00 13.74 ? 63  ASN A ND2 1 
ATOM   528  N  N   . ASN A 1 64  ? 26.136  6.929   22.468  1.00 13.96 ? 64  ASN A N   1 
ATOM   529  C  CA  . ASN A 1 64  ? 25.949  8.213   21.789  1.00 14.85 ? 64  ASN A CA  1 
ATOM   530  C  C   . ASN A 1 64  ? 24.497  8.674   21.826  1.00 15.14 ? 64  ASN A C   1 
ATOM   531  O  O   . ASN A 1 64  ? 24.112  9.593   21.111  1.00 17.50 ? 64  ASN A O   1 
ATOM   532  C  CB  . ASN A 1 64  ? 26.403  8.167   20.321  1.00 16.72 ? 64  ASN A CB  1 
ATOM   533  C  CG  . ASN A 1 64  ? 25.676  7.103   19.515  1.00 17.10 ? 64  ASN A CG  1 
ATOM   534  O  OD1 . ASN A 1 64  ? 24.613  6.624   19.909  1.00 15.63 ? 64  ASN A OD1 1 
ATOM   535  N  ND2 . ASN A 1 64  ? 26.224  6.732   18.359  1.00 18.14 ? 64  ASN A ND2 1 
ATOM   536  N  N   . GLY A 1 65  ? 23.696  8.058   22.691  1.00 14.02 ? 65  GLY A N   1 
ATOM   537  C  CA  . GLY A 1 65  ? 22.307  8.400   22.884  1.00 16.55 ? 65  GLY A CA  1 
ATOM   538  C  C   . GLY A 1 65  ? 21.407  7.761   21.833  1.00 16.60 ? 65  GLY A C   1 
ATOM   539  O  O   . GLY A 1 65  ? 20.197  7.914   21.961  1.00 19.37 ? 65  GLY A O   1 
ATOM   540  N  N   . HIS A 1 66  ? 21.959  7.011   20.869  1.00 14.19 ? 66  HIS A N   1 
ATOM   541  C  CA  . HIS A 1 66  ? 21.173  6.340   19.833  1.00 12.71 ? 66  HIS A CA  1 
ATOM   542  C  C   . HIS A 1 66  ? 21.465  4.850   19.808  1.00 12.60 ? 66  HIS A C   1 
ATOM   543  O  O   . HIS A 1 66  ? 20.621  4.080   19.339  1.00 13.58 ? 66  HIS A O   1 
ATOM   544  C  CB  . HIS A 1 66  ? 21.418  6.950   18.440  1.00 14.04 ? 66  HIS A CB  1 
ATOM   545  C  CG  . HIS A 1 66  ? 21.166  8.428   18.378  1.00 15.21 ? 66  HIS A CG  1 
ATOM   546  N  ND1 . HIS A 1 66  ? 19.880  8.995   18.501  1.00 16.89 ? 66  HIS A ND1 1 
ATOM   547  C  CD2 . HIS A 1 66  ? 22.030  9.445   18.172  1.00 16.60 ? 66  HIS A CD2 1 
ATOM   548  C  CE1 . HIS A 1 66  ? 19.985  10.322  18.403  1.00 15.99 ? 66  HIS A CE1 1 
ATOM   549  N  NE2 . HIS A 1 66  ? 21.294  10.609  18.220  1.00 15.57 ? 66  HIS A NE2 1 
ATOM   550  N  N   . SER A 1 67  ? 22.661  4.449   20.248  1.00 11.93 ? 67  SER A N   1 
ATOM   551  C  CA  . SER A 1 67  ? 23.116  3.068   20.266  1.00 11.90 ? 67  SER A CA  1 
ATOM   552  C  C   . SER A 1 67  ? 24.346  3.015   21.159  1.00 12.34 ? 67  SER A C   1 
ATOM   553  O  O   . SER A 1 67  ? 24.731  4.034   21.746  1.00 13.65 ? 67  SER A O   1 
ATOM   554  C  CB  . SER A 1 67  ? 23.473  2.629   18.821  1.00 11.89 ? 67  SER A CB  1 
ATOM   555  O  OG  . SER A 1 67  ? 23.795  1.236   18.797  1.00 12.75 ? 67  SER A OG  1 
ATOM   556  N  N   . VAL A 1 68  ? 24.919  1.827   21.229  1.00 11.45 ? 68  VAL A N   1 
ATOM   557  C  CA  . VAL A 1 68  ? 26.274  1.718   21.745  1.00 12.44 ? 68  VAL A CA  1 
ATOM   558  C  C   . VAL A 1 68  ? 27.168  1.470   20.529  1.00 12.97 ? 68  VAL A C   1 
ATOM   559  O  O   . VAL A 1 68  ? 26.859  0.628   19.689  1.00 12.88 ? 68  VAL A O   1 
ATOM   560  C  CB  . VAL A 1 68  ? 26.347  0.618   22.834  1.00 15.12 ? 68  VAL A CB  1 
ATOM   561  C  CG1 . VAL A 1 68  ? 25.862  -0.719  22.382  1.00 16.21 ? 68  VAL A CG1 1 
ATOM   562  C  CG2 . VAL A 1 68  ? 27.777  0.427   23.303  1.00 17.01 ? 68  VAL A CG2 1 
ATOM   563  N  N   A LYS A 1 69  ? 28.313  2.140   20.530  0.50 11.70 ? 69  LYS A N   1 
ATOM   564  N  N   B LYS A 1 69  ? 28.240  2.269   20.415  0.50 13.11 ? 69  LYS A N   1 
ATOM   565  C  CA  A LYS A 1 69  ? 29.167  2.164   19.358  0.50 10.94 ? 69  LYS A CA  1 
ATOM   566  C  CA  B LYS A 1 69  ? 29.144  2.128   19.276  0.50 12.80 ? 69  LYS A CA  1 
ATOM   567  C  C   A LYS A 1 69  ? 30.581  1.810   19.793  0.50 11.94 ? 69  LYS A C   1 
ATOM   568  C  C   B LYS A 1 69  ? 30.575  1.869   19.735  0.50 13.26 ? 69  LYS A C   1 
ATOM   569  O  O   A LYS A 1 69  ? 31.042  2.343   20.795  0.50 13.61 ? 69  LYS A O   1 
ATOM   570  O  O   B LYS A 1 69  ? 31.034  2.527   20.673  0.50 14.37 ? 69  LYS A O   1 
ATOM   571  C  CB  A LYS A 1 69  ? 29.167  3.569   18.778  0.50 11.40 ? 69  LYS A CB  1 
ATOM   572  C  CB  B LYS A 1 69  ? 29.054  3.291   18.284  0.50 16.32 ? 69  LYS A CB  1 
ATOM   573  C  CG  A LYS A 1 69  ? 30.023  3.671   17.530  0.50 12.36 ? 69  LYS A CG  1 
ATOM   574  C  CG  B LYS A 1 69  ? 29.585  4.640   18.736  0.50 18.09 ? 69  LYS A CG  1 
ATOM   575  C  CD  A LYS A 1 69  ? 30.048  5.033   16.878  0.50 13.66 ? 69  LYS A CD  1 
ATOM   576  C  CD  B LYS A 1 69  ? 29.877  5.569   17.579  0.50 20.94 ? 69  LYS A CD  1 
ATOM   577  C  CE  A LYS A 1 69  ? 30.526  6.188   17.723  0.50 18.37 ? 69  LYS A CE  1 
ATOM   578  C  CE  B LYS A 1 69  ? 30.429  6.900   18.058  0.50 24.77 ? 69  LYS A CE  1 
ATOM   579  N  NZ  A LYS A 1 69  ? 30.352  7.457   16.958  0.50 20.31 ? 69  LYS A NZ  1 
ATOM   580  N  NZ  B LYS A 1 69  ? 31.174  7.590   16.970  0.50 25.26 ? 69  LYS A NZ  1 
ATOM   581  N  N   . LEU A 1 70  ? 31.259  0.970   19.005  1.00 10.84 ? 70  LEU A N   1 
ATOM   582  C  CA  . LEU A 1 70  ? 32.675  0.663   19.224  1.00 11.46 ? 70  LEU A CA  1 
ATOM   583  C  C   . LEU A 1 70  ? 33.444  1.221   18.048  1.00 11.44 ? 70  LEU A C   1 
ATOM   584  O  O   . LEU A 1 70  ? 33.147  0.929   16.887  1.00 11.33 ? 70  LEU A O   1 
ATOM   585  C  CB  . LEU A 1 70  ? 32.851  -0.833  19.330  1.00 12.11 ? 70  LEU A CB  1 
ATOM   586  C  CG  . LEU A 1 70  ? 34.324  -1.300  19.493  1.00 12.46 ? 70  LEU A CG  1 
ATOM   587  C  CD1 . LEU A 1 70  ? 34.893  -0.899  20.856  1.00 12.61 ? 70  LEU A CD1 1 
ATOM   588  C  CD2 . LEU A 1 70  ? 34.373  -2.793  19.377  1.00 13.63 ? 70  LEU A CD2 1 
ATOM   589  N  N   . ASN A 1 71  ? 34.409  2.115   18.311  1.00 11.43 ? 71  ASN A N   1 
ATOM   590  C  CA  . ASN A 1 71  ? 35.253  2.639   17.254  1.00 11.85 ? 71  ASN A CA  1 
ATOM   591  C  C   . ASN A 1 71  ? 36.221  1.565   16.794  1.00 13.83 ? 71  ASN A C   1 
ATOM   592  O  O   . ASN A 1 71  ? 36.717  0.756   17.581  1.00 13.93 ? 71  ASN A O   1 
ATOM   593  C  CB  . ASN A 1 71  ? 36.039  3.853   17.715  1.00 14.76 ? 71  ASN A CB  1 
ATOM   594  C  CG  . ASN A 1 71  ? 35.185  5.101   17.817  1.00 18.43 ? 71  ASN A CG  1 
ATOM   595  O  OD1 . ASN A 1 71  ? 33.994  5.142   17.465  1.00 23.42 ? 71  ASN A OD1 1 
ATOM   596  N  ND2 . ASN A 1 71  ? 35.794  6.172   18.285  1.00 23.24 ? 71  ASN A ND2 1 
ATOM   597  N  N   . LEU A 1 72  ? 36.463  1.520   15.484  1.00 11.57 ? 72  LEU A N   1 
ATOM   598  C  CA  . LEU A 1 72  ? 37.292  0.495   14.876  1.00 12.26 ? 72  LEU A CA  1 
ATOM   599  C  C   . LEU A 1 72  ? 38.405  1.174   14.091  1.00 12.77 ? 72  LEU A C   1 
ATOM   600  O  O   . LEU A 1 72  ? 38.227  2.289   13.590  1.00 14.43 ? 72  LEU A O   1 
ATOM   601  C  CB  . LEU A 1 72  ? 36.448  -0.382  13.941  1.00 10.74 ? 72  LEU A CB  1 
ATOM   602  C  CG  . LEU A 1 72  ? 35.370  -1.189  14.638  1.00 10.94 ? 72  LEU A CG  1 
ATOM   603  C  CD1 . LEU A 1 72  ? 34.454  -1.846  13.584  1.00 10.76 ? 72  LEU A CD1 1 
ATOM   604  C  CD2 . LEU A 1 72  ? 35.916  -2.271  15.568  1.00 12.64 ? 72  LEU A CD2 1 
ATOM   605  N  N   . PRO A 1 73  ? 39.576  0.483   13.936  1.00 13.12 ? 73  PRO A N   1 
ATOM   606  C  CA  . PRO A 1 73  ? 40.713  1.119   13.282  1.00 14.16 ? 73  PRO A CA  1 
ATOM   607  C  C   . PRO A 1 73  ? 40.627  0.956   11.770  1.00 14.42 ? 73  PRO A C   1 
ATOM   608  O  O   . PRO A 1 73  ? 40.121  -0.043  11.234  1.00 14.82 ? 73  PRO A O   1 
ATOM   609  C  CB  . PRO A 1 73  ? 41.869  0.340   13.933  1.00 13.17 ? 73  PRO A CB  1 
ATOM   610  C  CG  . PRO A 1 73  ? 41.352  -1.065  14.060  1.00 12.05 ? 73  PRO A CG  1 
ATOM   611  C  CD  . PRO A 1 73  ? 39.866  -0.869  14.415  1.00 12.24 ? 73  PRO A CD  1 
ATOM   612  N  N   . SER A 1 74  ? 41.209  1.941   11.097  1.00 16.89 ? 74  SER A N   1 
ATOM   613  C  CA  . SER A 1 74  ? 41.099  1.921   9.649   1.00 17.79 ? 74  SER A CA  1 
ATOM   614  C  C   . SER A 1 74  ? 41.995  0.870   8.972   1.00 18.93 ? 74  SER A C   1 
ATOM   615  O  O   . SER A 1 74  ? 41.863  0.639   7.773   1.00 19.56 ? 74  SER A O   1 
ATOM   616  C  CB  . SER A 1 74  ? 41.351  3.259   9.099   1.00 20.40 ? 74  SER A CB  1 
ATOM   617  O  OG  . SER A 1 74  ? 42.691  3.605   9.359   1.00 24.03 ? 74  SER A OG  1 
ATOM   618  N  N   . ASP A 1 75  ? 42.916  0.182   9.681   1.00 16.14 ? 75  ASP A N   1 
ATOM   619  C  CA  . ASP A 1 75  ? 43.597  -0.954  9.059   1.00 17.81 ? 75  ASP A CA  1 
ATOM   620  C  C   . ASP A 1 75  ? 42.695  -2.185  8.907   1.00 15.13 ? 75  ASP A C   1 
ATOM   621  O  O   . ASP A 1 75  ? 43.021  -3.184  8.257   1.00 18.18 ? 75  ASP A O   1 
ATOM   622  C  CB  . ASP A 1 75  ? 44.919  -1.273  9.775   1.00 19.88 ? 75  ASP A CB  1 
ATOM   623  C  CG  . ASP A 1 75  ? 44.695  -1.718  11.198  1.00 21.49 ? 75  ASP A CG  1 
ATOM   624  O  OD1 . ASP A 1 75  ? 44.335  -0.857  12.007  1.00 25.00 ? 75  ASP A OD1 1 
ATOM   625  O  OD2 . ASP A 1 75  ? 44.966  -2.910  11.479  1.00 26.41 ? 75  ASP A OD2 1 
ATOM   626  N  N   . MET A 1 76  ? 41.518  -2.172  9.561   1.00 13.31 ? 76  MET A N   1 
ATOM   627  C  CA  . MET A 1 76  ? 40.579  -3.237  9.391   1.00 13.62 ? 76  MET A CA  1 
ATOM   628  C  C   . MET A 1 76  ? 39.758  -2.934  8.131   1.00 12.22 ? 76  MET A C   1 
ATOM   629  O  O   . MET A 1 76  ? 39.358  -1.777  7.955   1.00 13.86 ? 76  MET A O   1 
ATOM   630  C  CB  . MET A 1 76  ? 39.720  -3.111  10.638  1.00 16.82 ? 76  MET A CB  1 
ATOM   631  C  CG  . MET A 1 76  ? 38.625  -4.050  10.680  1.00 15.20 ? 76  MET A CG  1 
ATOM   632  S  SD  . MET A 1 76  ? 37.826  -3.984  12.349  1.00 15.04 ? 76  MET A SD  1 
ATOM   633  C  CE  . MET A 1 76  ? 36.234  -4.697  11.920  1.00 15.53 ? 76  MET A CE  1 
ATOM   634  N  N   . HIS A 1 77  ? 39.649  -3.916  7.266   1.00 11.58 ? 77  HIS A N   1 
ATOM   635  C  CA  . HIS A 1 77  ? 38.910  -3.664  6.016   1.00 12.04 ? 77  HIS A CA  1 
ATOM   636  C  C   . HIS A 1 77  ? 38.330  -4.906  5.399   1.00 11.53 ? 77  HIS A C   1 
ATOM   637  O  O   . HIS A 1 77  ? 38.663  -6.040  5.730   1.00 13.40 ? 77  HIS A O   1 
ATOM   638  C  CB  . HIS A 1 77  ? 39.773  -2.923  4.964   1.00 14.81 ? 77  HIS A CB  1 
ATOM   639  C  CG  . HIS A 1 77  ? 40.974  -3.703  4.547   1.00 16.17 ? 77  HIS A CG  1 
ATOM   640  N  ND1 . HIS A 1 77  ? 42.177  -3.495  5.157   1.00 18.17 ? 77  HIS A ND1 1 
ATOM   641  C  CD2 . HIS A 1 77  ? 41.161  -4.661  3.623   1.00 18.14 ? 77  HIS A CD2 1 
ATOM   642  C  CE1 . HIS A 1 77  ? 43.083  -4.278  4.623   1.00 17.53 ? 77  HIS A CE1 1 
ATOM   643  N  NE2 . HIS A 1 77  ? 42.507  -5.003  3.666   1.00 20.28 ? 77  HIS A NE2 1 
ATOM   644  N  N   . ILE A 1 78  ? 37.377  -4.654  4.480   1.00 11.74 ? 78  ILE A N   1 
ATOM   645  C  CA  . ILE A 1 78  ? 36.775  -5.659  3.601   1.00 12.84 ? 78  ILE A CA  1 
ATOM   646  C  C   . ILE A 1 78  ? 37.557  -5.679  2.307   1.00 13.00 ? 78  ILE A C   1 
ATOM   647  O  O   . ILE A 1 78  ? 37.789  -4.618  1.741   1.00 13.39 ? 78  ILE A O   1 
ATOM   648  C  CB  . ILE A 1 78  ? 35.282  -5.323  3.325   1.00 13.87 ? 78  ILE A CB  1 
ATOM   649  C  CG1 . ILE A 1 78  ? 34.444  -5.348  4.599   1.00 16.43 ? 78  ILE A CG1 1 
ATOM   650  C  CG2 . ILE A 1 78  ? 34.728  -6.255  2.255   1.00 17.63 ? 78  ILE A CG2 1 
ATOM   651  C  CD1 . ILE A 1 78  ? 33.102  -4.605  4.369   1.00 16.18 ? 78  ILE A CD1 1 
ATOM   652  N  N   . GLN A 1 79  ? 37.962  -6.878  1.910   1.00 13.80 ? 79  GLN A N   1 
ATOM   653  C  CA  . GLN A 1 79  ? 38.467  -7.123  0.573   1.00 16.60 ? 79  GLN A CA  1 
ATOM   654  C  C   . GLN A 1 79  ? 37.403  -7.925  -0.202  1.00 15.79 ? 79  GLN A C   1 
ATOM   655  O  O   . GLN A 1 79  ? 36.747  -8.835  0.350   1.00 16.64 ? 79  GLN A O   1 
ATOM   656  C  CB  . GLN A 1 79  ? 39.772  -7.926  0.759   1.00 19.25 ? 79  GLN A CB  1 
ATOM   657  C  CG  . GLN A 1 79  ? 40.391  -8.388  -0.561  1.00 26.18 ? 79  GLN A CG  1 
ATOM   658  C  CD  . GLN A 1 79  ? 41.423  -7.398  -1.046  1.00 39.45 ? 79  GLN A CD  1 
ATOM   659  O  OE1 . GLN A 1 79  ? 41.928  -6.567  -0.283  1.00 45.38 ? 79  GLN A OE1 1 
ATOM   660  N  NE2 . GLN A 1 79  ? 41.761  -7.484  -2.327  1.00 42.52 ? 79  GLN A NE2 1 
ATOM   661  N  N   . GLY A 1 80  ? 37.315  -7.662  -1.510  1.00 17.38 ? 80  GLY A N   1 
ATOM   662  C  CA  . GLY A 1 80  ? 36.414  -8.389  -2.396  1.00 16.67 ? 80  GLY A CA  1 
ATOM   663  C  C   . GLY A 1 80  ? 35.432  -7.478  -3.120  1.00 16.57 ? 80  GLY A C   1 
ATOM   664  O  O   . GLY A 1 80  ? 34.797  -7.902  -4.079  1.00 19.52 ? 80  GLY A O   1 
ATOM   665  N  N   . LEU A 1 81  ? 35.252  -6.234  -2.664  1.00 14.56 ? 81  LEU A N   1 
ATOM   666  C  CA  . LEU A 1 81  ? 34.451  -5.248  -3.376  1.00 16.74 ? 81  LEU A CA  1 
ATOM   667  C  C   . LEU A 1 81  ? 35.421  -4.551  -4.341  1.00 16.71 ? 81  LEU A C   1 
ATOM   668  O  O   . LEU A 1 81  ? 36.627  -4.814  -4.380  1.00 19.27 ? 81  LEU A O   1 
ATOM   669  C  CB  . LEU A 1 81  ? 33.764  -4.289  -2.393  1.00 15.68 ? 81  LEU A CB  1 
ATOM   670  C  CG  . LEU A 1 81  ? 32.813  -4.950  -1.380  1.00 15.74 ? 81  LEU A CG  1 
ATOM   671  C  CD1 . LEU A 1 81  ? 32.374  -3.983  -0.268  1.00 17.21 ? 81  LEU A CD1 1 
ATOM   672  C  CD2 . LEU A 1 81  ? 31.585  -5.542  -2.093  1.00 17.80 ? 81  LEU A CD2 1 
ATOM   673  N  N   . GLN A 1 82  ? 34.886  -3.662  -5.164  1.00 20.68 ? 82  GLN A N   1 
ATOM   674  C  CA  . GLN A 1 82  ? 35.761  -3.111  -6.186  1.00 19.43 ? 82  GLN A CA  1 
ATOM   675  C  C   . GLN A 1 82  ? 36.816  -2.186  -5.572  1.00 17.70 ? 82  GLN A C   1 
ATOM   676  O  O   . GLN A 1 82  ? 37.972  -2.134  -6.060  1.00 18.52 ? 82  GLN A O   1 
ATOM   677  C  CB  . GLN A 1 82  ? 34.918  -2.339  -7.186  1.00 23.90 ? 82  GLN A CB  1 
ATOM   678  C  CG  . GLN A 1 82  ? 35.798  -1.600  -8.167  1.00 28.98 ? 82  GLN A CG  1 
ATOM   679  C  CD  . GLN A 1 82  ? 34.988  -0.996  -9.282  1.00 35.06 ? 82  GLN A CD  1 
ATOM   680  O  OE1 . GLN A 1 82  ? 34.920  0.222   -9.399  1.00 28.80 ? 82  GLN A OE1 1 
ATOM   681  N  NE2 . GLN A 1 82  ? 34.400  -1.852  -10.106 1.00 38.06 ? 82  GLN A NE2 1 
ATOM   682  N  N   . SER A 1 83  ? 36.380  -1.442  -4.534  1.00 15.92 ? 83  SER A N   1 
ATOM   683  C  CA  . SER A 1 83  ? 37.280  -0.603  -3.760  1.00 13.35 ? 83  SER A CA  1 
ATOM   684  C  C   . SER A 1 83  ? 37.451  -1.283  -2.408  1.00 12.85 ? 83  SER A C   1 
ATOM   685  O  O   . SER A 1 83  ? 36.596  -2.074  -1.987  1.00 11.95 ? 83  SER A O   1 
ATOM   686  C  CB  . SER A 1 83  ? 36.687  0.742   -3.491  1.00 13.21 ? 83  SER A CB  1 
ATOM   687  O  OG  . SER A 1 83  ? 36.480  1.498   -4.700  1.00 14.10 ? 83  SER A OG  1 
ATOM   688  N  N   . ARG A 1 84  ? 38.553  -0.923  -1.735  1.00 11.75 ? 84  ARG A N   1 
ATOM   689  C  CA  . ARG A 1 84  ? 38.703  -1.281  -0.332  1.00 11.31 ? 84  ARG A CA  1 
ATOM   690  C  C   . ARG A 1 84  ? 37.737  -0.456  0.491   1.00 10.38 ? 84  ARG A C   1 
ATOM   691  O  O   . ARG A 1 84  ? 37.676  0.752   0.351   1.00 10.28 ? 84  ARG A O   1 
ATOM   692  C  CB  . ARG A 1 84  ? 40.143  -0.970  0.104   1.00 10.03 ? 84  ARG A CB  1 
ATOM   693  C  CG  . ARG A 1 84  ? 40.350  -1.371  1.564   1.00 10.31 ? 84  ARG A CG  1 
ATOM   694  C  CD  . ARG A 1 84  ? 41.780  -1.126  2.078   1.00 11.66 ? 84  ARG A CD  1 
ATOM   695  N  NE  . ARG A 1 84  ? 42.695  -2.193  1.698   1.00 11.78 ? 84  ARG A NE  1 
ATOM   696  C  CZ  . ARG A 1 84  ? 43.991  -2.211  1.983   1.00 12.69 ? 84  ARG A CZ  1 
ATOM   697  N  NH1 . ARG A 1 84  ? 44.534  -1.212  2.658   1.00 14.66 ? 84  ARG A NH1 1 
ATOM   698  N  NH2 . ARG A 1 84  ? 44.741  -3.226  1.594   1.00 15.22 ? 84  ARG A NH2 1 
ATOM   699  N  N   . TYR A 1 85  ? 37.054  -1.152  1.439   1.00 9.88  ? 85  TYR A N   1 
ATOM   700  C  CA  . TYR A 1 85  ? 36.270  -0.437  2.444   1.00 10.38 ? 85  TYR A CA  1 
ATOM   701  C  C   . TYR A 1 85  ? 36.863  -0.654  3.839   1.00 10.19 ? 85  TYR A C   1 
ATOM   702  O  O   . TYR A 1 85  ? 36.996  -1.811  4.263   1.00 11.36 ? 85  TYR A O   1 
ATOM   703  C  CB  . TYR A 1 85  ? 34.798  -0.897  2.403   1.00 11.35 ? 85  TYR A CB  1 
ATOM   704  C  CG  . TYR A 1 85  ? 34.059  -0.366  1.193   1.00 8.86  ? 85  TYR A CG  1 
ATOM   705  C  CD1 . TYR A 1 85  ? 34.177  -0.945  -0.065  1.00 10.17 ? 85  TYR A CD1 1 
ATOM   706  C  CD2 . TYR A 1 85  ? 33.225  0.733   1.360   1.00 9.52  ? 85  TYR A CD2 1 
ATOM   707  C  CE1 . TYR A 1 85  ? 33.530  -0.374  -1.172  1.00 10.50 ? 85  TYR A CE1 1 
ATOM   708  C  CE2 . TYR A 1 85  ? 32.529  1.263   0.269   1.00 9.34  ? 85  TYR A CE2 1 
ATOM   709  C  CZ  . TYR A 1 85  ? 32.738  0.738   -0.989  1.00 10.43 ? 85  TYR A CZ  1 
ATOM   710  O  OH  . TYR A 1 85  ? 32.040  1.266   -2.070  1.00 15.17 ? 85  TYR A OH  1 
ATOM   711  N  N   . SER A 1 86  ? 37.233  0.428   4.517   1.00 9.61  ? 86  SER A N   1 
ATOM   712  C  CA  . SER A 1 86  ? 37.937  0.346   5.795   1.00 9.80  ? 86  SER A CA  1 
ATOM   713  C  C   . SER A 1 86  ? 36.923  0.567   6.901   1.00 10.10 ? 86  SER A C   1 
ATOM   714  O  O   . SER A 1 86  ? 36.023  1.378   6.764   1.00 9.63  ? 86  SER A O   1 
ATOM   715  C  CB  . SER A 1 86  ? 39.015  1.396   5.883   1.00 10.88 ? 86  SER A CB  1 
ATOM   716  O  OG  . SER A 1 86  ? 40.016  1.098   4.887   1.00 12.92 ? 86  SER A OG  1 
ATOM   717  N  N   . ALA A 1 87  ? 37.108  -0.144  8.009   1.00 9.91  ? 87  ALA A N   1 
ATOM   718  C  CA  . ALA A 1 87  ? 36.165  -0.042  9.116   1.00 9.53  ? 87  ALA A CA  1 
ATOM   719  C  C   . ALA A 1 87  ? 36.251  1.314   9.782   1.00 9.38  ? 87  ALA A C   1 
ATOM   720  O  O   . ALA A 1 87  ? 37.315  1.939   9.858   1.00 11.45 ? 87  ALA A O   1 
ATOM   721  C  CB  . ALA A 1 87  ? 36.407  -1.154  10.100  1.00 11.77 ? 87  ALA A CB  1 
ATOM   722  N  N   . THR A 1 88  ? 35.149  1.758   10.375  1.00 9.35  ? 88  THR A N   1 
ATOM   723  C  CA  . THR A 1 88  ? 35.102  2.958   11.198  1.00 9.92  ? 88  THR A CA  1 
ATOM   724  C  C   . THR A 1 88  ? 34.442  2.663   12.537  1.00 10.05 ? 88  THR A C   1 
ATOM   725  O  O   . THR A 1 88  ? 34.898  3.195   13.540  1.00 10.15 ? 88  THR A O   1 
ATOM   726  C  CB  . THR A 1 88  ? 34.487  4.104   10.394  1.00 11.10 ? 88  THR A CB  1 
ATOM   727  O  OG1 . THR A 1 88  ? 34.418  5.243   11.239  1.00 13.89 ? 88  THR A OG1 1 
ATOM   728  C  CG2 . THR A 1 88  ? 33.064  3.892   9.934   1.00 12.21 ? 88  THR A CG2 1 
ATOM   729  N  N   . GLN A 1 89  ? 33.366  1.858   12.572  1.00 9.65  ? 89  GLN A N   1 
ATOM   730  C  CA  . GLN A 1 89  ? 32.701  1.622   13.845  1.00 9.59  ? 89  GLN A CA  1 
ATOM   731  C  C   . GLN A 1 89  ? 31.708  0.490   13.673  1.00 8.90  ? 89  GLN A C   1 
ATOM   732  O  O   . GLN A 1 89  ? 31.333  0.146   12.566  1.00 9.70  ? 89  GLN A O   1 
ATOM   733  C  CB  . GLN A 1 89  ? 31.989  2.859   14.371  1.00 10.08 ? 89  GLN A CB  1 
ATOM   734  C  CG  . GLN A 1 89  ? 31.044  3.495   13.363  1.00 11.20 ? 89  GLN A CG  1 
ATOM   735  C  CD  . GLN A 1 89  ? 29.582  3.379   13.759  1.00 10.97 ? 89  GLN A CD  1 
ATOM   736  O  OE1 . GLN A 1 89  ? 29.124  2.290   14.108  1.00 10.87 ? 89  GLN A OE1 1 
ATOM   737  N  NE2 . GLN A 1 89  ? 28.828  4.441   13.597  1.00 13.81 ? 89  GLN A NE2 1 
ATOM   738  N  N   . LEU A 1 90  ? 31.351  -0.127  14.796  1.00 8.72  ? 90  LEU A N   1 
ATOM   739  C  CA  . LEU A 1 90  ? 30.202  -1.015  14.872  1.00 8.63  ? 90  LEU A CA  1 
ATOM   740  C  C   . LEU A 1 90  ? 29.225  -0.541  15.928  1.00 8.43  ? 90  LEU A C   1 
ATOM   741  O  O   . LEU A 1 90  ? 29.591  0.132   16.854  1.00 9.28  ? 90  LEU A O   1 
ATOM   742  C  CB  . LEU A 1 90  ? 30.621  -2.499  14.976  1.00 8.92  ? 90  LEU A CB  1 
ATOM   743  C  CG  . LEU A 1 90  ? 31.378  -2.955  16.244  1.00 9.05  ? 90  LEU A CG  1 
ATOM   744  C  CD1 . LEU A 1 90  ? 30.443  -3.050  17.482  1.00 11.13 ? 90  LEU A CD1 1 
ATOM   745  C  CD2 . LEU A 1 90  ? 32.035  -4.313  15.948  1.00 11.10 ? 90  LEU A CD2 1 
ATOM   746  N  N   . HIS A 1 91  ? 27.962  -0.951  15.761  1.00 8.68  ? 91  HIS A N   1 
ATOM   747  C  CA  . HIS A 1 91  ? 26.939  -0.617  16.726  1.00 8.38  ? 91  HIS A CA  1 
ATOM   748  C  C   . HIS A 1 91  ? 25.773  -1.587  16.568  1.00 7.63  ? 91  HIS A C   1 
ATOM   749  O  O   . HIS A 1 91  ? 25.786  -2.441  15.687  1.00 7.63  ? 91  HIS A O   1 
ATOM   750  C  CB  . HIS A 1 91  ? 26.496  0.837   16.540  1.00 9.28  ? 91  HIS A CB  1 
ATOM   751  C  CG  . HIS A 1 91  ? 25.843  0.997   15.200  1.00 8.37  ? 91  HIS A CG  1 
ATOM   752  N  ND1 . HIS A 1 91  ? 26.542  1.428   14.094  1.00 8.94  ? 91  HIS A ND1 1 
ATOM   753  C  CD2 . HIS A 1 91  ? 24.588  0.708   14.782  1.00 8.59  ? 91  HIS A CD2 1 
ATOM   754  C  CE1 . HIS A 1 91  ? 25.753  1.395   13.012  1.00 8.29  ? 91  HIS A CE1 1 
ATOM   755  N  NE2 . HIS A 1 91  ? 24.515  0.930   13.403  1.00 7.50  ? 91  HIS A NE2 1 
ATOM   756  N  N   . LEU A 1 92  ? 24.771  -1.461  17.462  1.00 8.33  ? 92  LEU A N   1 
ATOM   757  C  CA  . LEU A 1 92  ? 23.682  -2.418  17.458  1.00 8.27  ? 92  LEU A CA  1 
ATOM   758  C  C   . LEU A 1 92  ? 22.317  -1.736  17.495  1.00 7.73  ? 92  LEU A C   1 
ATOM   759  O  O   . LEU A 1 92  ? 22.173  -0.557  17.794  1.00 8.24  ? 92  LEU A O   1 
ATOM   760  C  CB  . LEU A 1 92  ? 23.798  -3.332  18.692  1.00 11.35 ? 92  LEU A CB  1 
ATOM   761  C  CG  . LEU A 1 92  ? 24.978  -4.314  18.609  1.00 9.79  ? 92  LEU A CG  1 
ATOM   762  C  CD1 . LEU A 1 92  ? 26.045  -3.883  19.586  1.00 16.00 ? 92  LEU A CD1 1 
ATOM   763  C  CD2 . LEU A 1 92  ? 24.516  -5.737  18.880  1.00 13.57 ? 92  LEU A CD2 1 
ATOM   764  N  N   . HIS A 1 93  ? 21.294  -2.522  17.115  1.00 7.00  ? 93  HIS A N   1 
ATOM   765  C  CA  . HIS A 1 93  ? 19.886  -2.081  17.210  1.00 7.88  ? 93  HIS A CA  1 
ATOM   766  C  C   . HIS A 1 93  ? 19.104  -3.201  17.868  1.00 7.68  ? 93  HIS A C   1 
ATOM   767  O  O   . HIS A 1 93  ? 19.390  -4.380  17.624  1.00 8.40  ? 93  HIS A O   1 
ATOM   768  C  CB  . HIS A 1 93  ? 19.339  -1.902  15.764  1.00 7.81  ? 93  HIS A CB  1 
ATOM   769  C  CG  . HIS A 1 93  ? 20.074  -0.871  14.977  1.00 7.01  ? 93  HIS A CG  1 
ATOM   770  N  ND1 . HIS A 1 93  ? 19.727  0.455   14.941  1.00 7.78  ? 93  HIS A ND1 1 
ATOM   771  C  CD2 . HIS A 1 93  ? 21.142  -1.000  14.161  1.00 6.93  ? 93  HIS A CD2 1 
ATOM   772  C  CE1 . HIS A 1 93  ? 20.598  1.089   14.134  1.00 7.58  ? 93  HIS A CE1 1 
ATOM   773  N  NE2 . HIS A 1 93  ? 21.479  0.231   13.668  1.00 7.77  ? 93  HIS A NE2 1 
ATOM   774  N  N   . TRP A 1 94  ? 18.122  -2.825  18.693  1.00 8.69  ? 94  TRP A N   1 
ATOM   775  C  CA  . TRP A 1 94  ? 17.387  -3.852  19.432  1.00 7.97  ? 94  TRP A CA  1 
ATOM   776  C  C   . TRP A 1 94  ? 15.999  -3.320  19.791  1.00 9.04  ? 94  TRP A C   1 
ATOM   777  O  O   . TRP A 1 94  ? 15.682  -2.149  19.567  1.00 8.46  ? 94  TRP A O   1 
ATOM   778  C  CB  . TRP A 1 94  ? 18.135  -4.252  20.731  1.00 8.24  ? 94  TRP A CB  1 
ATOM   779  C  CG  . TRP A 1 94  ? 18.458  -3.108  21.657  1.00 8.46  ? 94  TRP A CG  1 
ATOM   780  C  CD1 . TRP A 1 94  ? 17.643  -2.602  22.643  1.00 9.54  ? 94  TRP A CD1 1 
ATOM   781  C  CD2 . TRP A 1 94  ? 19.635  -2.271  21.644  1.00 8.88  ? 94  TRP A CD2 1 
ATOM   782  N  NE1 . TRP A 1 94  ? 18.236  -1.519  23.273  1.00 9.48  ? 94  TRP A NE1 1 
ATOM   783  C  CE2 . TRP A 1 94  ? 19.494  -1.335  22.698  1.00 9.41  ? 94  TRP A CE2 1 
ATOM   784  C  CE3 . TRP A 1 94  ? 20.813  -2.241  20.871  1.00 9.21  ? 94  TRP A CE3 1 
ATOM   785  C  CZ2 . TRP A 1 94  ? 20.448  -0.374  22.993  1.00 9.17  ? 94  TRP A CZ2 1 
ATOM   786  C  CZ3 . TRP A 1 94  ? 21.748  -1.256  21.151  1.00 9.43  ? 94  TRP A CZ3 1 
ATOM   787  C  CH2 . TRP A 1 94  ? 21.589  -0.344  22.194  1.00 9.44  ? 94  TRP A CH2 1 
ATOM   788  N  N   . GLY A 1 95  ? 15.213  -4.228  20.350  1.00 8.85  ? 95  GLY A N   1 
ATOM   789  C  CA  . GLY A 1 95  ? 13.824  -3.958  20.739  1.00 9.64  ? 95  GLY A CA  1 
ATOM   790  C  C   . GLY A 1 95  ? 13.698  -3.639  22.232  1.00 9.26  ? 95  GLY A C   1 
ATOM   791  O  O   . GLY A 1 95  ? 14.347  -2.752  22.779  1.00 9.54  ? 95  GLY A O   1 
ATOM   792  N  N   . ASN A 1 96  ? 12.852  -4.429  22.926  1.00 10.91 ? 96  ASN A N   1 
ATOM   793  C  CA  . ASN A 1 96  ? 12.695  -4.212  24.362  1.00 11.25 ? 96  ASN A CA  1 
ATOM   794  C  C   . ASN A 1 96  ? 12.214  -5.526  24.958  1.00 11.96 ? 96  ASN A C   1 
ATOM   795  O  O   . ASN A 1 96  ? 11.754  -6.417  24.248  1.00 10.83 ? 96  ASN A O   1 
ATOM   796  C  CB  . ASN A 1 96  ? 11.755  -3.048  24.646  1.00 13.53 ? 96  ASN A CB  1 
ATOM   797  C  CG  . ASN A 1 96  ? 10.316  -3.390  24.347  1.00 15.79 ? 96  ASN A CG  1 
ATOM   798  O  OD1 . ASN A 1 96  ? 9.634   -3.938  25.236  1.00 19.80 ? 96  ASN A OD1 1 
ATOM   799  N  ND2 . ASN A 1 96  ? 9.819   -3.148  23.155  1.00 16.99 ? 96  ASN A ND2 1 
ATOM   800  N  N   . PRO A 1 97  ? 12.293  -5.697  26.297  1.00 12.25 ? 97  PRO A N   1 
ATOM   801  C  CA  . PRO A 1 97  ? 11.952  -6.996  26.870  1.00 12.77 ? 97  PRO A CA  1 
ATOM   802  C  C   . PRO A 1 97  ? 10.518  -7.455  26.633  1.00 12.20 ? 97  PRO A C   1 
ATOM   803  O  O   . PRO A 1 97  ? 10.284  -8.635  26.595  1.00 14.17 ? 97  PRO A O   1 
ATOM   804  C  CB  . PRO A 1 97  ? 12.251  -6.798  28.368  1.00 14.13 ? 97  PRO A CB  1 
ATOM   805  C  CG  . PRO A 1 97  ? 13.315  -5.712  28.385  1.00 14.89 ? 97  PRO A CG  1 
ATOM   806  C  CD  . PRO A 1 97  ? 12.851  -4.757  27.298  1.00 14.14 ? 97  PRO A CD  1 
ATOM   807  N  N   . ASN A 1 98  ? 9.585   -6.539  26.480  1.00 12.57 ? 98  ASN A N   1 
ATOM   808  C  CA  . ASN A 1 98  ? 8.202   -6.944  26.193  1.00 14.62 ? 98  ASN A CA  1 
ATOM   809  C  C   . ASN A 1 98  ? 7.940   -7.281  24.722  1.00 15.11 ? 98  ASN A C   1 
ATOM   810  O  O   . ASN A 1 98  ? 6.901   -7.880  24.373  1.00 18.10 ? 98  ASN A O   1 
ATOM   811  C  CB  . ASN A 1 98  ? 7.236   -5.806  26.565  1.00 16.89 ? 98  ASN A CB  1 
ATOM   812  C  CG  . ASN A 1 98  ? 7.140   -5.611  28.062  1.00 24.71 ? 98  ASN A CG  1 
ATOM   813  O  OD1 . ASN A 1 98  ? 7.133   -6.585  28.814  1.00 28.34 ? 98  ASN A OD1 1 
ATOM   814  N  ND2 . ASN A 1 98  ? 6.974   -4.373  28.493  1.00 30.29 ? 98  ASN A ND2 1 
ATOM   815  N  N   . ASP A 1 99  ? 8.841   -6.834  23.837  1.00 12.93 ? 99  ASP A N   1 
ATOM   816  C  CA  . ASP A 1 99  ? 8.735   -7.125  22.413  1.00 13.30 ? 99  ASP A CA  1 
ATOM   817  C  C   . ASP A 1 99  ? 10.156  -7.251  21.856  1.00 12.17 ? 99  ASP A C   1 
ATOM   818  O  O   . ASP A 1 99  ? 10.672  -6.318  21.244  1.00 12.47 ? 99  ASP A O   1 
ATOM   819  C  CB  . ASP A 1 99  ? 7.805   -6.109  21.723  1.00 15.11 ? 99  ASP A CB  1 
ATOM   820  C  CG  . ASP A 1 99  ? 7.302   -6.488  20.349  1.00 17.71 ? 99  ASP A CG  1 
ATOM   821  O  OD1 . ASP A 1 99  ? 7.703   -7.521  19.845  1.00 16.91 ? 99  ASP A OD1 1 
ATOM   822  O  OD2 . ASP A 1 99  ? 6.483   -5.714  19.839  1.00 21.97 ? 99  ASP A OD2 1 
ATOM   823  N  N   . PRO A 1 100 ? 10.842  -8.371  22.114  1.00 10.93 ? 100 PRO A N   1 
ATOM   824  C  CA  . PRO A 1 100 ? 12.298  -8.461  21.916  1.00 11.43 ? 100 PRO A CA  1 
ATOM   825  C  C   . PRO A 1 100 ? 12.606  -8.827  20.460  1.00 12.43 ? 100 PRO A C   1 
ATOM   826  O  O   . PRO A 1 100 ? 13.188  -9.862  20.147  1.00 11.98 ? 100 PRO A O   1 
ATOM   827  C  CB  . PRO A 1 100 ? 12.698  -9.582  22.892  1.00 11.91 ? 100 PRO A CB  1 
ATOM   828  C  CG  . PRO A 1 100 ? 11.492  -10.485 22.878  1.00 12.14 ? 100 PRO A CG  1 
ATOM   829  C  CD  . PRO A 1 100 ? 10.308  -9.543  22.861  1.00 12.27 ? 100 PRO A CD  1 
ATOM   830  N  N   . HIS A 1 101 ? 12.195  -7.945  19.559  1.00 11.66 ? 101 HIS A N   1 
ATOM   831  C  CA  . HIS A 1 101 ? 12.303  -8.234  18.112  1.00 12.14 ? 101 HIS A CA  1 
ATOM   832  C  C   . HIS A 1 101 ? 12.640  -6.954  17.370  1.00 13.65 ? 101 HIS A C   1 
ATOM   833  O  O   . HIS A 1 101 ? 11.837  -6.418  16.588  1.00 16.21 ? 101 HIS A O   1 
ATOM   834  C  CB  . HIS A 1 101 ? 10.979  -8.781  17.524  1.00 15.01 ? 101 HIS A CB  1 
ATOM   835  C  CG  . HIS A 1 101 ? 10.416  -9.910  18.310  1.00 15.53 ? 101 HIS A CG  1 
ATOM   836  N  ND1 . HIS A 1 101 ? 10.939  -11.196 18.284  1.00 16.12 ? 101 HIS A ND1 1 
ATOM   837  C  CD2 . HIS A 1 101 ? 9.404   -9.906  19.210  1.00 15.55 ? 101 HIS A CD2 1 
ATOM   838  C  CE1 . HIS A 1 101 ? 10.243  -11.931 19.155  1.00 16.49 ? 101 HIS A CE1 1 
ATOM   839  N  NE2 . HIS A 1 101 ? 9.325   -11.160 19.726  1.00 15.73 ? 101 HIS A NE2 1 
ATOM   840  N  N   . GLY A 1 102 ? 13.865  -6.499  17.587  1.00 9.88  ? 102 GLY A N   1 
ATOM   841  C  CA  . GLY A 1 102 ? 14.301  -5.182  17.179  1.00 10.21 ? 102 GLY A CA  1 
ATOM   842  C  C   . GLY A 1 102 ? 15.417  -5.148  16.133  1.00 8.90  ? 102 GLY A C   1 
ATOM   843  O  O   . GLY A 1 102 ? 16.091  -4.120  16.058  1.00 10.03 ? 102 GLY A O   1 
ATOM   844  N  N   . SER A 1 103 ? 15.549  -6.178  15.303  1.00 8.79  ? 103 SER A N   1 
ATOM   845  C  CA  . SER A 1 103 ? 16.378  -6.001  14.119  1.00 8.30  ? 103 SER A CA  1 
ATOM   846  C  C   . SER A 1 103 ? 15.797  -4.909  13.208  1.00 8.88  ? 103 SER A C   1 
ATOM   847  O  O   . SER A 1 103 ? 14.602  -4.567  13.285  1.00 9.94  ? 103 SER A O   1 
ATOM   848  C  CB  . SER A 1 103 ? 16.549  -7.297  13.369  1.00 8.87  ? 103 SER A CB  1 
ATOM   849  O  OG  . SER A 1 103 ? 15.311  -7.710  12.756  1.00 9.42  ? 103 SER A OG  1 
ATOM   850  N  N   . GLU A 1 104 ? 16.643  -4.377  12.336  1.00 8.10  ? 104 GLU A N   1 
ATOM   851  C  CA  . GLU A 1 104 ? 16.182  -3.386  11.350  1.00 7.91  ? 104 GLU A CA  1 
ATOM   852  C  C   . GLU A 1 104 ? 15.696  -4.097  10.091  1.00 8.31  ? 104 GLU A C   1 
ATOM   853  O  O   . GLU A 1 104 ? 14.555  -3.889  9.657   1.00 7.85  ? 104 GLU A O   1 
ATOM   854  C  CB  . GLU A 1 104 ? 17.334  -2.431  11.042  1.00 8.76  ? 104 GLU A CB  1 
ATOM   855  C  CG  . GLU A 1 104 ? 17.852  -1.723  12.276  1.00 8.49  ? 104 GLU A CG  1 
ATOM   856  C  CD  . GLU A 1 104 ? 18.222  -0.301  11.958  1.00 8.38  ? 104 GLU A CD  1 
ATOM   857  O  OE1 . GLU A 1 104 ? 19.291  -0.112  11.388  1.00 8.92  ? 104 GLU A OE1 1 
ATOM   858  O  OE2 . GLU A 1 104 ? 17.421  0.607   12.222  1.00 9.87  ? 104 GLU A OE2 1 
ATOM   859  N  N   . HIS A 1 105 ? 16.545  -4.905  9.455   1.00 7.29  ? 105 HIS A N   1 
ATOM   860  C  CA  . HIS A 1 105 ? 16.075  -5.731  8.359   1.00 7.74  ? 105 HIS A CA  1 
ATOM   861  C  C   . HIS A 1 105 ? 15.158  -6.808  8.923   1.00 7.67  ? 105 HIS A C   1 
ATOM   862  O  O   . HIS A 1 105 ? 15.326  -7.305  10.054  1.00 8.84  ? 105 HIS A O   1 
ATOM   863  C  CB  . HIS A 1 105 ? 17.276  -6.361  7.638   1.00 7.78  ? 105 HIS A CB  1 
ATOM   864  C  CG  . HIS A 1 105 ? 18.008  -5.303  6.888   1.00 8.12  ? 105 HIS A CG  1 
ATOM   865  N  ND1 . HIS A 1 105 ? 19.084  -4.600  7.427   1.00 8.12  ? 105 HIS A ND1 1 
ATOM   866  C  CD2 . HIS A 1 105 ? 17.781  -4.777  5.670   1.00 7.89  ? 105 HIS A CD2 1 
ATOM   867  C  CE1 . HIS A 1 105 ? 19.500  -3.689  6.571   1.00 8.22  ? 105 HIS A CE1 1 
ATOM   868  N  NE2 . HIS A 1 105 ? 18.729  -3.791  5.460   1.00 8.39  ? 105 HIS A NE2 1 
ATOM   869  N  N   . THR A 1 106 ? 14.199  -7.196  8.093   1.00 7.59  ? 106 THR A N   1 
ATOM   870  C  CA  . THR A 1 106 ? 13.354  -8.354  8.372   1.00 8.49  ? 106 THR A CA  1 
ATOM   871  C  C   . THR A 1 106 ? 13.543  -9.359  7.257   1.00 8.97  ? 106 THR A C   1 
ATOM   872  O  O   . THR A 1 106 ? 14.007  -9.044  6.183   1.00 9.13  ? 106 THR A O   1 
ATOM   873  C  CB  . THR A 1 106 ? 11.878  -7.967  8.540   1.00 9.57  ? 106 THR A CB  1 
ATOM   874  O  OG1 . THR A 1 106 ? 11.457  -7.322  7.317   1.00 10.06 ? 106 THR A OG1 1 
ATOM   875  C  CG2 . THR A 1 106 ? 11.724  -6.978  9.666   1.00 10.52 ? 106 THR A CG2 1 
ATOM   876  N  N   . VAL A 1 107 ? 13.193  -10.628 7.553   1.00 10.05 ? 107 VAL A N   1 
ATOM   877  C  CA  . VAL A 1 107 ? 13.264  -11.711 6.592   1.00 10.48 ? 107 VAL A CA  1 
ATOM   878  C  C   . VAL A 1 107 ? 11.874  -12.340 6.520   1.00 9.95  ? 107 VAL A C   1 
ATOM   879  O  O   . VAL A 1 107 ? 11.345  -12.805 7.506   1.00 10.32 ? 107 VAL A O   1 
ATOM   880  C  CB  . VAL A 1 107 ? 14.328  -12.761 6.949   1.00 11.40 ? 107 VAL A CB  1 
ATOM   881  C  CG1 . VAL A 1 107 ? 14.334  -13.923 5.966   1.00 11.61 ? 107 VAL A CG1 1 
ATOM   882  C  CG2 . VAL A 1 107 ? 15.755  -12.186 7.029   1.00 13.65 ? 107 VAL A CG2 1 
ATOM   883  N  N   . SER A 1 108 ? 11.267  -12.276 5.330   1.00 10.78 ? 108 SER A N   1 
ATOM   884  C  CA  . SER A 1 108 ? 9.904   -12.771 5.092   1.00 11.92 ? 108 SER A CA  1 
ATOM   885  C  C   . SER A 1 108 ? 8.976   -12.181 6.141   1.00 12.64 ? 108 SER A C   1 
ATOM   886  O  O   . SER A 1 108 ? 8.105   -12.879 6.705   1.00 12.58 ? 108 SER A O   1 
ATOM   887  C  CB  . SER A 1 108 ? 9.887   -14.289 5.188   1.00 13.50 ? 108 SER A CB  1 
ATOM   888  O  OG  . SER A 1 108 ? 10.745  -14.853 4.201   1.00 17.42 ? 108 SER A OG  1 
ATOM   889  N  N   . GLY A 1 109 ? 9.177   -10.885 6.418   1.00 10.32 ? 109 GLY A N   1 
ATOM   890  C  CA  . GLY A 1 109 ? 8.308   -10.108 7.286   1.00 11.37 ? 109 GLY A CA  1 
ATOM   891  C  C   . GLY A 1 109 ? 8.662   -10.221 8.775   1.00 13.01 ? 109 GLY A C   1 
ATOM   892  O  O   . GLY A 1 109 ? 8.034   -9.568  9.607   1.00 15.46 ? 109 GLY A O   1 
ATOM   893  N  N   . GLN A 1 110 ? 9.627   -11.076 9.133   1.00 11.57 ? 110 GLN A N   1 
ATOM   894  C  CA  . GLN A 1 110 ? 9.982   -11.325 10.526  1.00 10.99 ? 110 GLN A CA  1 
ATOM   895  C  C   . GLN A 1 110 ? 11.234  -10.597 11.029  1.00 10.12 ? 110 GLN A C   1 
ATOM   896  O  O   . GLN A 1 110 ? 12.242  -10.597 10.341  1.00 9.54  ? 110 GLN A O   1 
ATOM   897  C  CB  . GLN A 1 110 ? 10.242  -12.819 10.728  1.00 12.40 ? 110 GLN A CB  1 
ATOM   898  C  CG  . GLN A 1 110 ? 9.168   -13.739 10.146  1.00 14.21 ? 110 GLN A CG  1 
ATOM   899  C  CD  . GLN A 1 110 ? 7.784   -13.324 10.614  1.00 15.34 ? 110 GLN A CD  1 
ATOM   900  O  OE1 . GLN A 1 110 ? 7.448   -13.294 11.791  1.00 16.20 ? 110 GLN A OE1 1 
ATOM   901  N  NE2 . GLN A 1 110 ? 6.933   -12.996 9.665   1.00 17.26 ? 110 GLN A NE2 1 
ATOM   902  N  N   . HIS A 1 111 ? 11.092  -9.931  12.168  1.00 10.68 ? 111 HIS A N   1 
ATOM   903  C  CA  . HIS A 1 111 ? 12.225  -9.351  12.836  1.00 10.96 ? 111 HIS A CA  1 
ATOM   904  C  C   . HIS A 1 111 ? 12.991  -10.413 13.581  1.00 12.15 ? 111 HIS A C   1 
ATOM   905  O  O   . HIS A 1 111 ? 12.441  -11.419 14.042  1.00 14.48 ? 111 HIS A O   1 
ATOM   906  C  CB  . HIS A 1 111 ? 11.796  -8.391  13.949  1.00 12.62 ? 111 HIS A CB  1 
ATOM   907  C  CG  . HIS A 1 111 ? 11.389  -7.056  13.439  1.00 11.30 ? 111 HIS A CG  1 
ATOM   908  N  ND1 . HIS A 1 111 ? 10.126  -6.703  12.960  1.00 14.54 ? 111 HIS A ND1 1 
ATOM   909  C  CD2 . HIS A 1 111 ? 12.183  -5.994  13.262  1.00 10.58 ? 111 HIS A CD2 1 
ATOM   910  C  CE1 . HIS A 1 111 ? 10.124  -5.442  12.525  1.00 13.73 ? 111 HIS A CE1 1 
ATOM   911  N  NE2 . HIS A 1 111 ? 11.434  -5.009  12.666  1.00 13.73 ? 111 HIS A NE2 1 
ATOM   912  N  N   . PHE A 1 112 ? 14.283  -10.236 13.622  1.00 9.84  ? 112 PHE A N   1 
ATOM   913  C  CA  . PHE A 1 112 ? 15.141  -10.929 14.567  1.00 10.28 ? 112 PHE A CA  1 
ATOM   914  C  C   . PHE A 1 112 ? 15.240  -10.109 15.837  1.00 9.46  ? 112 PHE A C   1 
ATOM   915  O  O   . PHE A 1 112 ? 14.719  -8.975  15.927  1.00 9.86  ? 112 PHE A O   1 
ATOM   916  C  CB  . PHE A 1 112 ? 16.528  -11.143 13.961  1.00 10.60 ? 112 PHE A CB  1 
ATOM   917  C  CG  . PHE A 1 112 ? 16.522  -12.245 12.934  1.00 12.17 ? 112 PHE A CG  1 
ATOM   918  C  CD1 . PHE A 1 112 ? 15.959  -12.066 11.660  1.00 14.54 ? 112 PHE A CD1 1 
ATOM   919  C  CD2 . PHE A 1 112 ? 16.935  -13.531 13.283  1.00 13.77 ? 112 PHE A CD2 1 
ATOM   920  C  CE1 . PHE A 1 112 ? 15.903  -13.140 10.768  1.00 17.63 ? 112 PHE A CE1 1 
ATOM   921  C  CE2 . PHE A 1 112 ? 16.922  -14.581 12.381  1.00 15.90 ? 112 PHE A CE2 1 
ATOM   922  C  CZ  . PHE A 1 112 ? 16.369  -14.391 11.150  1.00 15.96 ? 112 PHE A CZ  1 
ATOM   923  N  N   . ALA A 1 113 ? 15.888  -10.657 16.872  1.00 9.26  ? 113 ALA A N   1 
ATOM   924  C  CA  . ALA A 1 113 ? 15.930  -10.024 18.181  1.00 9.38  ? 113 ALA A CA  1 
ATOM   925  C  C   . ALA A 1 113 ? 16.679  -8.698  18.099  1.00 8.86  ? 113 ALA A C   1 
ATOM   926  O  O   . ALA A 1 113 ? 16.298  -7.744  18.759  1.00 9.31  ? 113 ALA A O   1 
ATOM   927  C  CB  . ALA A 1 113 ? 16.568  -10.919 19.268  1.00 10.03 ? 113 ALA A CB  1 
ATOM   928  N  N   . ALA A 1 114 ? 17.801  -8.660  17.355  1.00 8.78  ? 114 ALA A N   1 
ATOM   929  C  CA  . ALA A 1 114 ? 18.671  -7.479  17.293  1.00 8.12  ? 114 ALA A CA  1 
ATOM   930  C  C   . ALA A 1 114 ? 19.495  -7.581  16.019  1.00 7.36  ? 114 ALA A C   1 
ATOM   931  O  O   . ALA A 1 114 ? 19.404  -8.594  15.303  1.00 8.22  ? 114 ALA A O   1 
ATOM   932  C  CB  . ALA A 1 114 ? 19.569  -7.459  18.547  1.00 9.72  ? 114 ALA A CB  1 
ATOM   933  N  N   . GLU A 1 115 ? 20.275  -6.512  15.797  1.00 8.04  ? 115 GLU A N   1 
ATOM   934  C  CA  . GLU A 1 115 ? 21.096  -6.544  14.589  1.00 8.05  ? 115 GLU A CA  1 
ATOM   935  C  C   . GLU A 1 115 ? 22.372  -5.769  14.879  1.00 7.99  ? 115 GLU A C   1 
ATOM   936  O  O   . GLU A 1 115 ? 22.314  -4.678  15.480  1.00 9.01  ? 115 GLU A O   1 
ATOM   937  C  CB  . GLU A 1 115 ? 20.281  -5.921  13.445  1.00 8.12  ? 115 GLU A CB  1 
ATOM   938  C  CG  . GLU A 1 115 ? 20.926  -5.949  12.056  1.00 8.40  ? 115 GLU A CG  1 
ATOM   939  C  CD  . GLU A 1 115 ? 19.989  -5.541  10.923  1.00 8.53  ? 115 GLU A CD  1 
ATOM   940  O  OE1 . GLU A 1 115 ? 18.770  -5.762  11.091  1.00 9.32  ? 115 GLU A OE1 1 
ATOM   941  O  OE2 . GLU A 1 115 ? 20.429  -5.052  9.895   1.00 8.52  ? 115 GLU A OE2 1 
ATOM   942  N  N   . LEU A 1 116 ? 23.509  -6.300  14.404  1.00 7.17  ? 116 LEU A N   1 
ATOM   943  C  CA  . LEU A 1 116 ? 24.827  -5.682  14.519  1.00 7.99  ? 116 LEU A CA  1 
ATOM   944  C  C   . LEU A 1 116 ? 25.159  -5.096  13.141  1.00 6.89  ? 116 LEU A C   1 
ATOM   945  O  O   . LEU A 1 116 ? 25.005  -5.767  12.121  1.00 6.97  ? 116 LEU A O   1 
ATOM   946  C  CB  . LEU A 1 116 ? 25.889  -6.729  14.925  1.00 8.69  ? 116 LEU A CB  1 
ATOM   947  C  CG  . LEU A 1 116 ? 27.363  -6.278  14.785  1.00 9.44  ? 116 LEU A CG  1 
ATOM   948  C  CD1 . LEU A 1 116 ? 27.717  -5.305  15.890  1.00 12.48 ? 116 LEU A CD1 1 
ATOM   949  C  CD2 . LEU A 1 116 ? 28.273  -7.528  14.755  1.00 10.78 ? 116 LEU A CD2 1 
ATOM   950  N  N   . HIS A 1 117 ? 25.666  -3.852  13.151  1.00 6.78  ? 117 HIS A N   1 
ATOM   951  C  CA  . HIS A 1 117 ? 26.157  -3.210  11.932  1.00 6.81  ? 117 HIS A CA  1 
ATOM   952  C  C   . HIS A 1 117 ? 27.614  -2.857  12.074  1.00 7.02  ? 117 HIS A C   1 
ATOM   953  O  O   . HIS A 1 117 ? 27.988  -2.202  13.041  1.00 7.63  ? 117 HIS A O   1 
ATOM   954  C  CB  . HIS A 1 117 ? 25.397  -1.911  11.647  1.00 7.35  ? 117 HIS A CB  1 
ATOM   955  C  CG  . HIS A 1 117 ? 23.993  -2.193  11.271  1.00 7.09  ? 117 HIS A CG  1 
ATOM   956  N  ND1 . HIS A 1 117 ? 22.968  -1.262  11.427  1.00 6.90  ? 117 HIS A ND1 1 
ATOM   957  C  CD2 . HIS A 1 117 ? 23.441  -3.295  10.723  1.00 7.13  ? 117 HIS A CD2 1 
ATOM   958  C  CE1 . HIS A 1 117 ? 21.860  -1.795  10.999  1.00 7.18  ? 117 HIS A CE1 1 
ATOM   959  N  NE2 . HIS A 1 117 ? 22.088  -3.046  10.574  1.00 6.78  ? 117 HIS A NE2 1 
ATOM   960  N  N   . ILE A 1 118 ? 28.441  -3.343  11.135  1.00 8.18  ? 118 ILE A N   1 
ATOM   961  C  CA  . ILE A 1 118 ? 29.862  -2.981  11.128  1.00 7.81  ? 118 ILE A CA  1 
ATOM   962  C  C   . ILE A 1 118 ? 30.022  -2.044  9.932   1.00 7.50  ? 118 ILE A C   1 
ATOM   963  O  O   . ILE A 1 118 ? 29.875  -2.467  8.756   1.00 7.77  ? 118 ILE A O   1 
ATOM   964  C  CB  . ILE A 1 118 ? 30.773  -4.200  10.965  1.00 8.59  ? 118 ILE A CB  1 
ATOM   965  C  CG1 . ILE A 1 118 ? 30.423  -5.271  12.004  1.00 8.95  ? 118 ILE A CG1 1 
ATOM   966  C  CG2 . ILE A 1 118 ? 32.232  -3.745  11.152  1.00 9.43  ? 118 ILE A CG2 1 
ATOM   967  C  CD1 . ILE A 1 118 ? 31.264  -6.543  11.889  1.00 11.23 ? 118 ILE A CD1 1 
ATOM   968  N  N   . VAL A 1 119 ? 30.241  -0.784  10.212  1.00 8.01  ? 119 VAL A N   1 
ATOM   969  C  CA  . VAL A 1 119 ? 30.251  0.279   9.206   1.00 8.56  ? 119 VAL A CA  1 
ATOM   970  C  C   . VAL A 1 119 ? 31.658  0.448   8.647   1.00 8.20  ? 119 VAL A C   1 
ATOM   971  O  O   . VAL A 1 119 ? 32.617  0.605   9.428   1.00 9.25  ? 119 VAL A O   1 
ATOM   972  C  CB  . VAL A 1 119 ? 29.779  1.624   9.809   1.00 8.43  ? 119 VAL A CB  1 
ATOM   973  C  CG1 . VAL A 1 119 ? 29.660  2.724   8.741   1.00 10.44 ? 119 VAL A CG1 1 
ATOM   974  C  CG2 . VAL A 1 119 ? 28.419  1.461   10.535  1.00 9.45  ? 119 VAL A CG2 1 
ATOM   975  N  N   . HIS A 1 120 ? 31.743  0.498   7.322   1.00 8.19  ? 120 HIS A N   1 
ATOM   976  C  CA  . HIS A 1 120 ? 33.003  0.705   6.601   1.00 8.25  ? 120 HIS A CA  1 
ATOM   977  C  C   . HIS A 1 120 ? 32.830  1.866   5.621   1.00 8.36  ? 120 HIS A C   1 
ATOM   978  O  O   . HIS A 1 120 ? 31.720  2.149   5.167   1.00 8.42  ? 120 HIS A O   1 
ATOM   979  C  CB  . HIS A 1 120 ? 33.444  -0.546  5.851   1.00 8.31  ? 120 HIS A CB  1 
ATOM   980  C  CG  . HIS A 1 120 ? 33.602  -1.788  6.631   1.00 8.61  ? 120 HIS A CG  1 
ATOM   981  N  ND1 . HIS A 1 120 ? 32.546  -2.491  7.244   1.00 8.59  ? 120 HIS A ND1 1 
ATOM   982  C  CD2 . HIS A 1 120 ? 34.715  -2.520  6.876   1.00 9.27  ? 120 HIS A CD2 1 
ATOM   983  C  CE1 . HIS A 1 120 ? 33.031  -3.608  7.779   1.00 9.11  ? 120 HIS A CE1 1 
ATOM   984  N  NE2 . HIS A 1 120 ? 34.364  -3.667  7.588   1.00 10.26 ? 120 HIS A NE2 1 
ATOM   985  N  N   . TYR A 1 121 ? 33.935  2.502   5.250   1.00 9.56  ? 121 TYR A N   1 
ATOM   986  C  CA  . TYR A 1 121 ? 33.912  3.563   4.245   1.00 9.03  ? 121 TYR A CA  1 
ATOM   987  C  C   . TYR A 1 121 ? 34.902  3.250   3.126   1.00 10.19 ? 121 TYR A C   1 
ATOM   988  O  O   . TYR A 1 121 ? 35.910  2.585   3.345   1.00 10.17 ? 121 TYR A O   1 
ATOM   989  C  CB  . TYR A 1 121 ? 34.198  4.955   4.852   1.00 11.00 ? 121 TYR A CB  1 
ATOM   990  C  CG  . TYR A 1 121 ? 35.614  5.203   5.316   1.00 11.70 ? 121 TYR A CG  1 
ATOM   991  C  CD1 . TYR A 1 121 ? 36.055  4.655   6.508   1.00 12.67 ? 121 TYR A CD1 1 
ATOM   992  C  CD2 . TYR A 1 121 ? 36.544  5.896   4.538   1.00 12.44 ? 121 TYR A CD2 1 
ATOM   993  C  CE1 . TYR A 1 121 ? 37.373  4.780   6.930   1.00 14.33 ? 121 TYR A CE1 1 
ATOM   994  C  CE2 . TYR A 1 121 ? 37.885  6.013   4.934   1.00 13.78 ? 121 TYR A CE2 1 
ATOM   995  C  CZ  . TYR A 1 121 ? 38.271  5.477   6.146   1.00 15.10 ? 121 TYR A CZ  1 
ATOM   996  O  OH  . TYR A 1 121 ? 39.577  5.608   6.619   1.00 18.23 ? 121 TYR A OH  1 
ATOM   997  N  N   . ASN A 1 122 ? 34.667  3.877   1.975   1.00 9.76  ? 122 ASN A N   1 
ATOM   998  C  CA  . ASN A 1 122 ? 35.510  3.663   0.793   1.00 10.58 ? 122 ASN A CA  1 
ATOM   999  C  C   . ASN A 1 122 ? 36.785  4.500   0.908   1.00 11.16 ? 122 ASN A C   1 
ATOM   1000 O  O   . ASN A 1 122 ? 36.814  5.684   0.643   1.00 10.64 ? 122 ASN A O   1 
ATOM   1001 C  CB  . ASN A 1 122 ? 34.783  4.124   -0.462  1.00 10.73 ? 122 ASN A CB  1 
ATOM   1002 C  CG  . ASN A 1 122 ? 35.504  3.695   -1.712  1.00 11.15 ? 122 ASN A CG  1 
ATOM   1003 O  OD1 . ASN A 1 122 ? 36.760  3.646   -1.742  1.00 10.96 ? 122 ASN A OD1 1 
ATOM   1004 N  ND2 . ASN A 1 122 ? 34.736  3.374   -2.767  1.00 12.89 ? 122 ASN A ND2 1 
ATOM   1005 N  N   . SER A 1 123 ? 37.856  3.844   1.406   1.00 10.57 ? 123 SER A N   1 
ATOM   1006 C  CA  . SER A 1 123 ? 39.092  4.543   1.723   1.00 12.16 ? 123 SER A CA  1 
ATOM   1007 C  C   . SER A 1 123 ? 39.932  4.698   0.466   1.00 12.02 ? 123 SER A C   1 
ATOM   1008 O  O   . SER A 1 123 ? 40.913  5.441   0.508   1.00 13.58 ? 123 SER A O   1 
ATOM   1009 C  CB  . SER A 1 123 ? 39.806  3.734   2.817   1.00 11.47 ? 123 SER A CB  1 
ATOM   1010 O  OG  . SER A 1 123 ? 39.889  2.366   2.514   1.00 11.96 ? 123 SER A OG  1 
ATOM   1011 N  N   . ASP A 1 124 ? 39.626  3.970   -0.599  1.00 10.97 ? 124 ASP A N   1 
ATOM   1012 C  CA  . ASP A 1 124 ? 40.328  4.198   -1.868  1.00 12.14 ? 124 ASP A CA  1 
ATOM   1013 C  C   . ASP A 1 124 ? 39.910  5.531   -2.470  1.00 14.10 ? 124 ASP A C   1 
ATOM   1014 O  O   . ASP A 1 124 ? 40.727  6.197   -3.120  1.00 15.82 ? 124 ASP A O   1 
ATOM   1015 C  CB  . ASP A 1 124 ? 40.019  3.110   -2.872  1.00 12.31 ? 124 ASP A CB  1 
ATOM   1016 C  CG  . ASP A 1 124 ? 40.696  1.796   -2.593  1.00 11.02 ? 124 ASP A CG  1 
ATOM   1017 O  OD1 . ASP A 1 124 ? 41.731  1.836   -1.850  1.00 12.93 ? 124 ASP A OD1 1 
ATOM   1018 O  OD2 . ASP A 1 124 ? 40.260  0.787   -3.079  1.00 11.77 ? 124 ASP A OD2 1 
ATOM   1019 N  N   . LEU A 1 125 ? 38.645  5.946   -2.274  1.00 12.27 ? 125 LEU A N   1 
ATOM   1020 C  CA  . LEU A 1 125 ? 38.174  7.181   -2.913  1.00 13.78 ? 125 LEU A CA  1 
ATOM   1021 C  C   . LEU A 1 125 ? 38.149  8.350   -1.935  1.00 13.81 ? 125 LEU A C   1 
ATOM   1022 O  O   . LEU A 1 125 ? 38.177  9.509   -2.404  1.00 15.82 ? 125 LEU A O   1 
ATOM   1023 C  CB  . LEU A 1 125 ? 36.762  6.981   -3.501  1.00 13.94 ? 125 LEU A CB  1 
ATOM   1024 C  CG  . LEU A 1 125 ? 36.656  5.840   -4.509  1.00 17.48 ? 125 LEU A CG  1 
ATOM   1025 C  CD1 . LEU A 1 125 ? 35.230  5.766   -5.059  1.00 18.69 ? 125 LEU A CD1 1 
ATOM   1026 C  CD2 . LEU A 1 125 ? 37.660  6.031   -5.651  1.00 22.94 ? 125 LEU A CD2 1 
ATOM   1027 N  N   . TYR A 1 126 ? 38.004  8.091   -0.614  1.00 12.10 ? 126 TYR A N   1 
ATOM   1028 C  CA  . TYR A 1 126 ? 37.727  9.163   0.333   1.00 12.61 ? 126 TYR A CA  1 
ATOM   1029 C  C   . TYR A 1 126 ? 38.661  9.047   1.532   1.00 14.82 ? 126 TYR A C   1 
ATOM   1030 O  O   . TYR A 1 126 ? 39.109  7.968   1.905   1.00 15.73 ? 126 TYR A O   1 
ATOM   1031 C  CB  . TYR A 1 126 ? 36.261  9.120   0.801   1.00 13.29 ? 126 TYR A CB  1 
ATOM   1032 C  CG  . TYR A 1 126 ? 35.326  9.146   -0.363  1.00 13.93 ? 126 TYR A CG  1 
ATOM   1033 C  CD1 . TYR A 1 126 ? 35.245  10.242  -1.231  1.00 14.77 ? 126 TYR A CD1 1 
ATOM   1034 C  CD2 . TYR A 1 126 ? 34.550  8.015   -0.638  1.00 13.97 ? 126 TYR A CD2 1 
ATOM   1035 C  CE1 . TYR A 1 126 ? 34.419  10.160  -2.351  1.00 16.02 ? 126 TYR A CE1 1 
ATOM   1036 C  CE2 . TYR A 1 126 ? 33.719  7.935   -1.748  1.00 13.72 ? 126 TYR A CE2 1 
ATOM   1037 C  CZ  . TYR A 1 126 ? 33.662  9.027   -2.622  1.00 15.56 ? 126 TYR A CZ  1 
ATOM   1038 O  OH  . TYR A 1 126 ? 32.856  8.983   -3.752  1.00 16.16 ? 126 TYR A OH  1 
ATOM   1039 N  N   . PRO A 1 127 ? 39.006  10.184  2.174   1.00 16.88 ? 127 PRO A N   1 
ATOM   1040 C  CA  . PRO A 1 127 ? 39.995  10.186  3.252   1.00 16.89 ? 127 PRO A CA  1 
ATOM   1041 C  C   . PRO A 1 127 ? 39.532  9.709   4.613   1.00 18.50 ? 127 PRO A C   1 
ATOM   1042 O  O   . PRO A 1 127 ? 40.359  9.324   5.438   1.00 22.45 ? 127 PRO A O   1 
ATOM   1043 C  CB  . PRO A 1 127 ? 40.445  11.650  3.350   1.00 19.80 ? 127 PRO A CB  1 
ATOM   1044 C  CG  . PRO A 1 127 ? 39.223  12.404  2.857   1.00 18.66 ? 127 PRO A CG  1 
ATOM   1045 C  CD  . PRO A 1 127 ? 38.683  11.544  1.730   1.00 17.00 ? 127 PRO A CD  1 
ATOM   1046 N  N   . ASP A 1 128 ? 38.207  9.729   4.845   1.00 16.59 ? 128 ASP A N   1 
ATOM   1047 C  CA  . ASP A 1 128 ? 37.668  9.365   6.135   1.00 17.52 ? 128 ASP A CA  1 
ATOM   1048 C  C   . ASP A 1 128 ? 36.175  9.121   5.981   1.00 18.00 ? 128 ASP A C   1 
ATOM   1049 O  O   . ASP A 1 128 ? 35.595  9.451   4.943   1.00 17.98 ? 128 ASP A O   1 
ATOM   1050 C  CB  . ASP A 1 128 ? 37.987  10.420  7.195   1.00 21.49 ? 128 ASP A CB  1 
ATOM   1051 C  CG  . ASP A 1 128 ? 37.618  11.806  6.729   1.00 25.82 ? 128 ASP A CG  1 
ATOM   1052 O  OD1 . ASP A 1 128 ? 36.452  12.014  6.422   1.00 22.51 ? 128 ASP A OD1 1 
ATOM   1053 O  OD2 . ASP A 1 128 ? 38.514  12.677  6.711   1.00 35.41 ? 128 ASP A OD2 1 
ATOM   1054 N  N   . ALA A 1 129 ? 35.581  8.515   7.010   1.00 16.80 ? 129 ALA A N   1 
ATOM   1055 C  CA  . ALA A 1 129 ? 34.212  8.054   6.910   1.00 15.54 ? 129 ALA A CA  1 
ATOM   1056 C  C   . ALA A 1 129 ? 33.234  9.209   6.765   1.00 18.96 ? 129 ALA A C   1 
ATOM   1057 O  O   . ALA A 1 129 ? 32.261  9.117   6.032   1.00 17.51 ? 129 ALA A O   1 
ATOM   1058 C  CB  . ALA A 1 129 ? 33.890  7.187   8.107   1.00 16.37 ? 129 ALA A CB  1 
ATOM   1059 N  N   . SER A 1 130 ? 33.469  10.278  7.540   1.00 20.23 ? 130 SER A N   1 
ATOM   1060 C  CA  . SER A 1 130 ? 32.586  11.439  7.460   1.00 20.12 ? 130 SER A CA  1 
ATOM   1061 C  C   . SER A 1 130 ? 32.518  11.991  6.024   1.00 18.65 ? 130 SER A C   1 
ATOM   1062 O  O   . SER A 1 130 ? 31.453  12.211  5.455   1.00 18.43 ? 130 SER A O   1 
ATOM   1063 C  CB  . SER A 1 130 ? 33.071  12.473  8.461   1.00 25.87 ? 130 SER A CB  1 
ATOM   1064 O  OG  . SER A 1 130 ? 32.316  13.679  8.368   1.00 31.36 ? 130 SER A OG  1 
ATOM   1065 N  N   . THR A 1 131 ? 33.675  12.166  5.400   1.00 18.33 ? 131 THR A N   1 
ATOM   1066 C  CA  . THR A 1 131 ? 33.675  12.704  4.051   1.00 18.92 ? 131 THR A CA  1 
ATOM   1067 C  C   . THR A 1 131 ? 32.960  11.730  3.110   1.00 16.62 ? 131 THR A C   1 
ATOM   1068 O  O   . THR A 1 131 ? 32.280  12.152  2.176   1.00 17.18 ? 131 THR A O   1 
ATOM   1069 C  CB  . THR A 1 131 ? 35.094  12.937  3.510   1.00 20.79 ? 131 THR A CB  1 
ATOM   1070 O  OG1 . THR A 1 131 ? 35.736  13.847  4.407   1.00 23.94 ? 131 THR A OG1 1 
ATOM   1071 C  CG2 . THR A 1 131 ? 35.137  13.553  2.127   1.00 19.44 ? 131 THR A CG2 1 
ATOM   1072 N  N   . ALA A 1 132 ? 33.201  10.402  3.280   1.00 15.73 ? 132 ALA A N   1 
ATOM   1073 C  CA  . ALA A 1 132 ? 32.607  9.400   2.399   1.00 14.17 ? 132 ALA A CA  1 
ATOM   1074 C  C   . ALA A 1 132 ? 31.083  9.330   2.513   1.00 14.49 ? 132 ALA A C   1 
ATOM   1075 O  O   . ALA A 1 132 ? 30.471  8.879   1.571   1.00 13.31 ? 132 ALA A O   1 
ATOM   1076 C  CB  . ALA A 1 132 ? 33.154  8.007   2.737   1.00 13.50 ? 132 ALA A CB  1 
ATOM   1077 N  N   . SER A 1 133 ? 30.562  9.636   3.685   1.00 14.25 ? 133 SER A N   1 
ATOM   1078 C  CA  . SER A 1 133 ? 29.199  9.241   4.041   1.00 15.88 ? 133 SER A CA  1 
ATOM   1079 C  C   . SER A 1 133 ? 28.136  9.824   3.109   1.00 16.56 ? 133 SER A C   1 
ATOM   1080 O  O   . SER A 1 133 ? 27.027  9.291   3.032   1.00 16.33 ? 133 SER A O   1 
ATOM   1081 C  CB  . SER A 1 133 ? 28.888  9.608   5.446   1.00 16.50 ? 133 SER A CB  1 
ATOM   1082 O  OG  . SER A 1 133 ? 28.830  11.040  5.581   1.00 19.10 ? 133 SER A OG  1 
ATOM   1083 N  N   . ASN A 1 134 ? 28.416  10.943  2.427   1.00 15.93 ? 134 ASN A N   1 
ATOM   1084 C  CA  . ASN A 1 134 ? 27.455  11.590  1.542   1.00 16.99 ? 134 ASN A CA  1 
ATOM   1085 C  C   . ASN A 1 134 ? 27.867  11.488  0.077   1.00 18.72 ? 134 ASN A C   1 
ATOM   1086 O  O   . ASN A 1 134 ? 27.356  12.195  -0.786  1.00 21.40 ? 134 ASN A O   1 
ATOM   1087 C  CB  . ASN A 1 134 ? 27.035  12.997  2.014   1.00 21.16 ? 134 ASN A CB  1 
ATOM   1088 C  CG  . ASN A 1 134 ? 28.116  14.031  1.751   1.00 24.65 ? 134 ASN A CG  1 
ATOM   1089 O  OD1 . ASN A 1 134 ? 29.295  13.685  1.671   1.00 25.32 ? 134 ASN A OD1 1 
ATOM   1090 N  ND2 . ASN A 1 134 ? 27.734  15.305  1.654   1.00 29.63 ? 134 ASN A ND2 1 
ATOM   1091 N  N   . LYS A 1 135 ? 28.793  10.593  -0.222  1.00 15.39 ? 135 LYS A N   1 
ATOM   1092 C  CA  . LYS A 1 135 ? 29.330  10.506  -1.553  1.00 16.25 ? 135 LYS A CA  1 
ATOM   1093 C  C   . LYS A 1 135 ? 29.072  9.167   -2.197  1.00 18.33 ? 135 LYS A C   1 
ATOM   1094 O  O   . LYS A 1 135 ? 28.817  8.162   -1.514  1.00 15.56 ? 135 LYS A O   1 
ATOM   1095 C  CB  . LYS A 1 135 ? 30.824  10.857  -1.502  1.00 18.43 ? 135 LYS A CB  1 
ATOM   1096 C  CG  . LYS A 1 135 ? 31.027  12.322  -1.092  1.00 21.31 ? 135 LYS A CG  1 
ATOM   1097 C  CD  . LYS A 1 135 ? 32.441  12.823  -1.227  1.00 24.28 ? 135 LYS A CD  1 
ATOM   1098 C  CE  . LYS A 1 135 ? 32.610  14.216  -0.655  1.00 21.80 ? 135 LYS A CE  1 
ATOM   1099 N  NZ  . LYS A 1 135 ? 31.923  14.407  0.651   1.00 23.87 ? 135 LYS A NZ  1 
ATOM   1100 N  N   . SER A 1 136 ? 29.195  9.161   -3.514  1.00 19.46 ? 136 SER A N   1 
ATOM   1101 C  CA  . SER A 1 136 ? 29.006  7.985   -4.337  1.00 21.10 ? 136 SER A CA  1 
ATOM   1102 C  C   . SER A 1 136 ? 29.902  6.843   -3.859  1.00 17.44 ? 136 SER A C   1 
ATOM   1103 O  O   . SER A 1 136 ? 31.113  6.983   -3.697  1.00 16.39 ? 136 SER A O   1 
ATOM   1104 C  CB  . SER A 1 136 ? 29.357  8.350   -5.757  1.00 22.43 ? 136 SER A CB  1 
ATOM   1105 O  OG  . SER A 1 136 ? 28.932  7.344   -6.654  1.00 35.66 ? 136 SER A OG  1 
ATOM   1106 N  N   . GLU A 1 137 ? 29.293  5.672   -3.648  1.00 17.31 ? 137 GLU A N   1 
ATOM   1107 C  CA  . GLU A 1 137 ? 30.069  4.498   -3.256  1.00 16.94 ? 137 GLU A CA  1 
ATOM   1108 C  C   . GLU A 1 137 ? 30.731  4.719   -1.901  1.00 15.74 ? 137 GLU A C   1 
ATOM   1109 O  O   . GLU A 1 137 ? 31.745  4.093   -1.597  1.00 15.80 ? 137 GLU A O   1 
ATOM   1110 C  CB  . GLU A 1 137 ? 31.088  4.117   -4.321  1.00 21.50 ? 137 GLU A CB  1 
ATOM   1111 C  CG  . GLU A 1 137 ? 30.414  3.992   -5.678  1.00 25.27 ? 137 GLU A CG  1 
ATOM   1112 C  CD  . GLU A 1 137 ? 30.988  2.943   -6.602  1.00 38.77 ? 137 GLU A CD  1 
ATOM   1113 O  OE1 . GLU A 1 137 ? 32.224  2.750   -6.563  1.00 43.67 ? 137 GLU A OE1 1 
ATOM   1114 O  OE2 . GLU A 1 137 ? 30.187  2.311   -7.347  1.00 48.31 ? 137 GLU A OE2 1 
ATOM   1115 N  N   . GLY A 1 138 ? 30.116  5.524   -1.029  1.00 11.82 ? 138 GLY A N   1 
ATOM   1116 C  CA  . GLY A 1 138 ? 30.862  5.988   0.099   1.00 12.14 ? 138 GLY A CA  1 
ATOM   1117 C  C   . GLY A 1 138 ? 30.989  4.937   1.200   1.00 10.47 ? 138 GLY A C   1 
ATOM   1118 O  O   . GLY A 1 138 ? 32.034  4.874   1.855   1.00 10.72 ? 138 GLY A O   1 
ATOM   1119 N  N   . LEU A 1 139 ? 29.926  4.174   1.497   1.00 10.52 ? 139 LEU A N   1 
ATOM   1120 C  CA  . LEU A 1 139 ? 29.886  3.328   2.682   1.00 8.89  ? 139 LEU A CA  1 
ATOM   1121 C  C   . LEU A 1 139 ? 29.511  1.893   2.317   1.00 8.91  ? 139 LEU A C   1 
ATOM   1122 O  O   . LEU A 1 139 ? 28.797  1.628   1.352   1.00 9.43  ? 139 LEU A O   1 
ATOM   1123 C  CB  . LEU A 1 139 ? 28.890  3.884   3.702   1.00 8.84  ? 139 LEU A CB  1 
ATOM   1124 C  CG  . LEU A 1 139 ? 29.120  5.300   4.198   1.00 9.08  ? 139 LEU A CG  1 
ATOM   1125 C  CD1 . LEU A 1 139 ? 27.956  5.697   5.090   1.00 11.02 ? 139 LEU A CD1 1 
ATOM   1126 C  CD2 . LEU A 1 139 ? 30.423  5.418   4.964   1.00 10.83 ? 139 LEU A CD2 1 
ATOM   1127 N  N   . ALA A 1 140 ? 29.914  0.958   3.179   1.00 8.30  ? 140 ALA A N   1 
ATOM   1128 C  CA  . ALA A 1 140 ? 29.504  -0.425  3.106   1.00 8.35  ? 140 ALA A CA  1 
ATOM   1129 C  C   . ALA A 1 140 ? 29.272  -0.902  4.533   1.00 8.32  ? 140 ALA A C   1 
ATOM   1130 O  O   . ALA A 1 140 ? 30.143  -0.707  5.381   1.00 9.48  ? 140 ALA A O   1 
ATOM   1131 C  CB  . ALA A 1 140 ? 30.509  -1.243  2.349   1.00 9.07  ? 140 ALA A CB  1 
ATOM   1132 N  N   . VAL A 1 141 ? 28.145  -1.555  4.752   1.00 8.23  ? 141 VAL A N   1 
ATOM   1133 C  CA  . VAL A 1 141 ? 27.819  -2.017  6.109   1.00 8.32  ? 141 VAL A CA  1 
ATOM   1134 C  C   . VAL A 1 141 ? 27.638  -3.523  6.025   1.00 8.11  ? 141 VAL A C   1 
ATOM   1135 O  O   . VAL A 1 141 ? 27.025  -4.067  5.095   1.00 8.53  ? 141 VAL A O   1 
ATOM   1136 C  CB  . VAL A 1 141 ? 26.553  -1.349  6.657   1.00 8.21  ? 141 VAL A CB  1 
ATOM   1137 C  CG1 . VAL A 1 141 ? 26.200  -1.908  8.037   1.00 9.48  ? 141 VAL A CG1 1 
ATOM   1138 C  CG2 . VAL A 1 141 ? 26.792  0.154   6.756   1.00 10.43 ? 141 VAL A CG2 1 
ATOM   1139 N  N   . LEU A 1 142 ? 28.212  -4.242  7.009   1.00 7.67  ? 142 LEU A N   1 
ATOM   1140 C  CA  . LEU A 1 142 ? 27.930  -5.657  7.199   1.00 7.99  ? 142 LEU A CA  1 
ATOM   1141 C  C   . LEU A 1 142 ? 26.906  -5.731  8.317   1.00 8.24  ? 142 LEU A C   1 
ATOM   1142 O  O   . LEU A 1 142 ? 27.099  -5.158  9.405   1.00 9.40  ? 142 LEU A O   1 
ATOM   1143 C  CB  . LEU A 1 142 ? 29.198  -6.398  7.669   1.00 8.89  ? 142 LEU A CB  1 
ATOM   1144 C  CG  . LEU A 1 142 ? 30.418  -6.278  6.761   1.00 9.22  ? 142 LEU A CG  1 
ATOM   1145 C  CD1 . LEU A 1 142 ? 31.518  -7.151  7.383   1.00 10.75 ? 142 LEU A CD1 1 
ATOM   1146 C  CD2 . LEU A 1 142 ? 30.067  -6.752  5.349   1.00 9.47  ? 142 LEU A CD2 1 
ATOM   1147 N  N   . ALA A 1 143 ? 25.820  -6.456  8.039   1.00 7.57  ? 143 ALA A N   1 
ATOM   1148 C  CA  . ALA A 1 143 ? 24.756  -6.615  9.038   1.00 6.83  ? 143 ALA A CA  1 
ATOM   1149 C  C   . ALA A 1 143 ? 24.652  -8.084  9.451   1.00 7.14  ? 143 ALA A C   1 
ATOM   1150 O  O   . ALA A 1 143 ? 24.581  -8.987  8.601   1.00 7.82  ? 143 ALA A O   1 
ATOM   1151 C  CB  . ALA A 1 143 ? 23.443  -6.161  8.429   1.00 7.72  ? 143 ALA A CB  1 
ATOM   1152 N  N   . VAL A 1 144 ? 24.623  -8.265  10.791  1.00 6.89  ? 144 VAL A N   1 
ATOM   1153 C  CA  . VAL A 1 144 ? 24.440  -9.602  11.327  1.00 7.94  ? 144 VAL A CA  1 
ATOM   1154 C  C   . VAL A 1 144 ? 23.124  -9.588  12.113  1.00 6.99  ? 144 VAL A C   1 
ATOM   1155 O  O   . VAL A 1 144 ? 22.929  -8.764  13.035  1.00 8.10  ? 144 VAL A O   1 
ATOM   1156 C  CB  . VAL A 1 144 ? 25.595  -9.911  12.308  1.00 8.12  ? 144 VAL A CB  1 
ATOM   1157 C  CG1 . VAL A 1 144 ? 25.424  -11.309 12.916  1.00 10.79 ? 144 VAL A CG1 1 
ATOM   1158 C  CG2 . VAL A 1 144 ? 26.955  -9.829  11.587  1.00 8.37  ? 144 VAL A CG2 1 
ATOM   1159 N  N   . LEU A 1 145 ? 22.284  -10.547 11.770  1.00 8.84  ? 145 LEU A N   1 
ATOM   1160 C  CA  . LEU A 1 145 ? 21.026  -10.741 12.488  1.00 8.61  ? 145 LEU A CA  1 
ATOM   1161 C  C   . LEU A 1 145 ? 21.309  -11.542 13.756  1.00 9.48  ? 145 LEU A C   1 
ATOM   1162 O  O   . LEU A 1 145 ? 22.059  -12.512 13.693  1.00 9.31  ? 145 LEU A O   1 
ATOM   1163 C  CB  . LEU A 1 145 ? 20.037  -11.446 11.559  1.00 9.72  ? 145 LEU A CB  1 
ATOM   1164 C  CG  . LEU A 1 145 ? 19.738  -10.680 10.267  1.00 11.13 ? 145 LEU A CG  1 
ATOM   1165 C  CD1 . LEU A 1 145 ? 19.024  -11.578 9.262   1.00 13.13 ? 145 LEU A CD1 1 
ATOM   1166 C  CD2 . LEU A 1 145 ? 18.909  -9.419  10.572  1.00 12.66 ? 145 LEU A CD2 1 
ATOM   1167 N  N   . ILE A 1 146 ? 20.652  -11.182 14.855  1.00 8.52  ? 146 ILE A N   1 
ATOM   1168 C  CA  . ILE A 1 146 ? 20.901  -11.786 16.165  1.00 9.63  ? 146 ILE A CA  1 
ATOM   1169 C  C   . ILE A 1 146 ? 19.597  -12.365 16.692  1.00 9.71  ? 146 ILE A C   1 
ATOM   1170 O  O   . ILE A 1 146 ? 18.563  -11.707 16.702  1.00 10.06 ? 146 ILE A O   1 
ATOM   1171 C  CB  . ILE A 1 146 ? 21.440  -10.725 17.133  1.00 9.63  ? 146 ILE A CB  1 
ATOM   1172 C  CG1 . ILE A 1 146 ? 22.765  -10.138 16.613  1.00 9.73  ? 146 ILE A CG1 1 
ATOM   1173 C  CG2 . ILE A 1 146 ? 21.664  -11.331 18.535  1.00 10.30 ? 146 ILE A CG2 1 
ATOM   1174 C  CD1 . ILE A 1 146 ? 23.167  -8.868  17.362  1.00 10.51 ? 146 ILE A CD1 1 
ATOM   1175 N  N   . GLU A 1 147 ? 19.665  -13.632 17.163  1.00 10.40 ? 147 GLU A N   1 
ATOM   1176 C  CA  . GLU A 1 147 ? 18.521  -14.246 17.819  1.00 11.18 ? 147 GLU A CA  1 
ATOM   1177 C  C   . GLU A 1 147 ? 18.942  -14.817 19.164  1.00 12.00 ? 147 GLU A C   1 
ATOM   1178 O  O   . GLU A 1 147 ? 20.130  -15.014 19.443  1.00 11.59 ? 147 GLU A O   1 
ATOM   1179 C  CB  . GLU A 1 147 ? 17.908  -15.373 16.997  1.00 13.90 ? 147 GLU A CB  1 
ATOM   1180 C  CG  . GLU A 1 147 ? 18.838  -16.534 16.714  1.00 13.58 ? 147 GLU A CG  1 
ATOM   1181 C  CD  . GLU A 1 147 ? 18.414  -17.552 15.669  1.00 16.28 ? 147 GLU A CD  1 
ATOM   1182 O  OE1 . GLU A 1 147 ? 17.390  -17.337 14.981  1.00 19.25 ? 147 GLU A OE1 1 
ATOM   1183 O  OE2 . GLU A 1 147 ? 19.141  -18.576 15.504  1.00 20.55 ? 147 GLU A OE2 1 
ATOM   1184 N  N   . MET A 1 148 ? 17.930  -15.074 20.011  1.00 13.89 ? 148 MET A N   1 
ATOM   1185 C  CA  . MET A 1 148 ? 18.240  -15.730 21.265  1.00 14.99 ? 148 MET A CA  1 
ATOM   1186 C  C   . MET A 1 148 ? 18.627  -17.199 21.043  1.00 14.75 ? 148 MET A C   1 
ATOM   1187 O  O   . MET A 1 148 ? 18.063  -17.901 20.199  1.00 16.23 ? 148 MET A O   1 
ATOM   1188 C  CB  . MET A 1 148 ? 16.989  -15.684 22.138  1.00 17.63 ? 148 MET A CB  1 
ATOM   1189 C  CG  . MET A 1 148 ? 17.302  -16.083 23.581  1.00 21.13 ? 148 MET A CG  1 
ATOM   1190 S  SD  . MET A 1 148 ? 15.991  -15.815 24.855  1.00 29.23 ? 148 MET A SD  1 
ATOM   1191 C  CE  . MET A 1 148 ? 15.857  -14.035 24.917  1.00 22.47 ? 148 MET A CE  1 
ATOM   1192 N  N   . GLY A 1 149 ? 19.593  -17.667 21.855  1.00 14.18 ? 149 GLY A N   1 
ATOM   1193 C  CA  . GLY A 1 149 ? 20.021  -19.062 21.829  1.00 15.02 ? 149 GLY A CA  1 
ATOM   1194 C  C   . GLY A 1 149 ? 21.103  -19.272 22.877  1.00 15.10 ? 149 GLY A C   1 
ATOM   1195 O  O   . GLY A 1 149 ? 20.941  -18.808 23.991  1.00 15.86 ? 149 GLY A O   1 
ATOM   1196 N  N   . SER A 1 150 ? 22.184  -19.950 22.477  1.00 16.43 ? 150 SER A N   1 
ATOM   1197 C  CA  . SER A 1 150 ? 23.250  -20.174 23.425  1.00 17.31 ? 150 SER A CA  1 
ATOM   1198 C  C   . SER A 1 150 ? 24.033  -18.895 23.735  1.00 16.82 ? 150 SER A C   1 
ATOM   1199 O  O   . SER A 1 150 ? 24.165  -17.969 22.917  1.00 14.60 ? 150 SER A O   1 
ATOM   1200 C  CB  . SER A 1 150 ? 24.172  -21.258 22.960  1.00 22.49 ? 150 SER A CB  1 
ATOM   1201 O  OG  . SER A 1 150 ? 24.737  -20.876 21.747  1.00 27.17 ? 150 SER A OG  1 
ATOM   1202 N  N   . PHE A 1 151 ? 24.608  -18.853 24.924  1.00 15.67 ? 151 PHE A N   1 
ATOM   1203 C  CA  . PHE A 1 151 ? 25.566  -17.841 25.317  1.00 14.89 ? 151 PHE A CA  1 
ATOM   1204 C  C   . PHE A 1 151 ? 26.658  -17.684 24.257  1.00 14.45 ? 151 PHE A C   1 
ATOM   1205 O  O   . PHE A 1 151 ? 27.225  -18.666 23.770  1.00 16.57 ? 151 PHE A O   1 
ATOM   1206 C  CB  . PHE A 1 151 ? 26.159  -18.192 26.690  1.00 14.56 ? 151 PHE A CB  1 
ATOM   1207 C  CG  . PHE A 1 151 ? 27.134  -17.172 27.178  1.00 14.66 ? 151 PHE A CG  1 
ATOM   1208 C  CD1 . PHE A 1 151 ? 26.685  -15.965 27.703  1.00 17.27 ? 151 PHE A CD1 1 
ATOM   1209 C  CD2 . PHE A 1 151 ? 28.507  -17.394 27.121  1.00 15.67 ? 151 PHE A CD2 1 
ATOM   1210 C  CE1 . PHE A 1 151 ? 27.578  -15.003 28.121  1.00 16.77 ? 151 PHE A CE1 1 
ATOM   1211 C  CE2 . PHE A 1 151 ? 29.395  -16.430 27.575  1.00 15.52 ? 151 PHE A CE2 1 
ATOM   1212 C  CZ  . PHE A 1 151 ? 28.936  -15.223 28.062  1.00 16.14 ? 151 PHE A CZ  1 
ATOM   1213 N  N   . ASN A 1 152 ? 27.014  -16.436 23.979  1.00 13.62 ? 152 ASN A N   1 
ATOM   1214 C  CA  . ASN A 1 152 ? 28.010  -16.113 22.969  1.00 13.19 ? 152 ASN A CA  1 
ATOM   1215 C  C   . ASN A 1 152 ? 29.179  -15.371 23.611  1.00 14.13 ? 152 ASN A C   1 
ATOM   1216 O  O   . ASN A 1 152 ? 29.094  -14.205 23.937  1.00 14.12 ? 152 ASN A O   1 
ATOM   1217 C  CB  . ASN A 1 152 ? 27.342  -15.265 21.879  1.00 12.43 ? 152 ASN A CB  1 
ATOM   1218 C  CG  . ASN A 1 152 ? 28.226  -15.182 20.656  1.00 13.03 ? 152 ASN A CG  1 
ATOM   1219 O  OD1 . ASN A 1 152 ? 29.396  -14.794 20.753  1.00 13.78 ? 152 ASN A OD1 1 
ATOM   1220 N  ND2 . ASN A 1 152 ? 27.628  -15.396 19.513  1.00 13.17 ? 152 ASN A ND2 1 
ATOM   1221 N  N   . PRO A 1 153 ? 30.321  -16.058 23.901  1.00 15.19 ? 153 PRO A N   1 
ATOM   1222 C  CA  . PRO A 1 153 ? 31.445  -15.359 24.521  1.00 14.95 ? 153 PRO A CA  1 
ATOM   1223 C  C   . PRO A 1 153 ? 31.997  -14.157 23.757  1.00 15.35 ? 153 PRO A C   1 
ATOM   1224 O  O   . PRO A 1 153 ? 32.496  -13.200 24.330  1.00 17.46 ? 153 PRO A O   1 
ATOM   1225 C  CB  . PRO A 1 153 ? 32.500  -16.493 24.598  1.00 17.20 ? 153 PRO A CB  1 
ATOM   1226 C  CG  . PRO A 1 153 ? 31.749  -17.780 24.575  1.00 19.50 ? 153 PRO A CG  1 
ATOM   1227 C  CD  . PRO A 1 153 ? 30.517  -17.521 23.715  1.00 15.74 ? 153 PRO A CD  1 
ATOM   1228 N  N   . SER A 1 154 ? 31.895  -14.245 22.425  1.00 14.44 ? 154 SER A N   1 
ATOM   1229 C  CA  . SER A 1 154 ? 32.493  -13.173 21.653  1.00 13.87 ? 154 SER A CA  1 
ATOM   1230 C  C   . SER A 1 154 ? 31.652  -11.908 21.787  1.00 12.16 ? 154 SER A C   1 
ATOM   1231 O  O   . SER A 1 154 ? 32.196  -10.857 21.970  1.00 13.44 ? 154 SER A O   1 
ATOM   1232 C  CB  . SER A 1 154 ? 32.628  -13.558 20.203  1.00 15.75 ? 154 SER A CB  1 
ATOM   1233 O  OG  . SER A 1 154 ? 33.438  -14.746 20.028  1.00 20.22 ? 154 SER A OG  1 
ATOM   1234 N  N   . TYR A 1 155 ? 30.313  -12.040 21.714  1.00 12.14 ? 155 TYR A N   1 
ATOM   1235 C  CA  . TYR A 1 155 ? 29.515  -10.832 21.939  1.00 13.06 ? 155 TYR A CA  1 
ATOM   1236 C  C   . TYR A 1 155 ? 29.681  -10.298 23.347  1.00 13.04 ? 155 TYR A C   1 
ATOM   1237 O  O   . TYR A 1 155 ? 29.606  -9.082  23.552  1.00 13.84 ? 155 TYR A O   1 
ATOM   1238 C  CB  . TYR A 1 155 ? 28.036  -11.065 21.615  1.00 12.01 ? 155 TYR A CB  1 
ATOM   1239 C  CG  . TYR A 1 155 ? 27.754  -10.911 20.122  1.00 12.38 ? 155 TYR A CG  1 
ATOM   1240 C  CD1 . TYR A 1 155 ? 28.064  -11.910 19.213  1.00 12.47 ? 155 TYR A CD1 1 
ATOM   1241 C  CD2 . TYR A 1 155 ? 27.155  -9.750  19.633  1.00 12.22 ? 155 TYR A CD2 1 
ATOM   1242 C  CE1 . TYR A 1 155 ? 27.869  -11.777 17.838  1.00 11.04 ? 155 TYR A CE1 1 
ATOM   1243 C  CE2 . TYR A 1 155 ? 26.981  -9.584  18.264  1.00 10.71 ? 155 TYR A CE2 1 
ATOM   1244 C  CZ  . TYR A 1 155 ? 27.321  -10.584 17.387  1.00 9.87  ? 155 TYR A CZ  1 
ATOM   1245 O  OH  . TYR A 1 155 ? 27.085  -10.346 16.054  1.00 11.17 ? 155 TYR A OH  1 
ATOM   1246 N  N   . ASP A 1 156 ? 30.007  -11.200 24.304  1.00 12.39 ? 156 ASP A N   1 
ATOM   1247 C  CA  . ASP A 1 156 ? 30.195  -10.737 25.665  1.00 14.70 ? 156 ASP A CA  1 
ATOM   1248 C  C   . ASP A 1 156 ? 31.460  -9.890  25.804  1.00 15.49 ? 156 ASP A C   1 
ATOM   1249 O  O   . ASP A 1 156 ? 31.533  -9.115  26.734  1.00 17.32 ? 156 ASP A O   1 
ATOM   1250 C  CB  . ASP A 1 156 ? 30.114  -11.900 26.650  1.00 17.64 ? 156 ASP A CB  1 
ATOM   1251 C  CG  . ASP A 1 156 ? 29.133  -11.543 27.762  1.00 19.12 ? 156 ASP A CG  1 
ATOM   1252 O  OD1 . ASP A 1 156 ? 27.977  -11.068 27.469  1.00 17.65 ? 156 ASP A OD1 1 
ATOM   1253 O  OD2 . ASP A 1 156 ? 29.545  -11.694 28.945  1.00 23.74 ? 156 ASP A OD2 1 
ATOM   1254 N  N   . LYS A 1 157 ? 32.388  -9.970  24.836  1.00 14.01 ? 157 LYS A N   1 
ATOM   1255 C  CA  . LYS A 1 157 ? 33.530  -9.071  24.835  1.00 16.73 ? 157 LYS A CA  1 
ATOM   1256 C  C   . LYS A 1 157 ? 33.098  -7.625  24.667  1.00 15.62 ? 157 LYS A C   1 
ATOM   1257 O  O   . LYS A 1 157 ? 33.818  -6.708  25.106  1.00 17.07 ? 157 LYS A O   1 
ATOM   1258 C  CB  . LYS A 1 157 ? 34.581  -9.480  23.797  1.00 17.68 ? 157 LYS A CB  1 
ATOM   1259 C  CG  . LYS A 1 157 ? 35.187  -10.830 24.135  1.00 19.90 ? 157 LYS A CG  1 
ATOM   1260 C  CD  . LYS A 1 157 ? 36.103  -11.380 23.055  1.00 19.49 ? 157 LYS A CD  1 
ATOM   1261 C  CE  . LYS A 1 157 ? 36.417  -12.849 23.265  1.00 21.06 ? 157 LYS A CE  1 
ATOM   1262 N  NZ  . LYS A 1 157 ? 37.404  -13.362 22.278  1.00 21.78 ? 157 LYS A NZ  1 
ATOM   1263 N  N   . ILE A 1 158 ? 31.912  -7.410  24.080  1.00 15.43 ? 158 ILE A N   1 
ATOM   1264 C  CA  . ILE A 1 158 ? 31.340  -6.061  24.063  1.00 15.66 ? 158 ILE A CA  1 
ATOM   1265 C  C   . ILE A 1 158 ? 30.379  -5.894  25.254  1.00 14.89 ? 158 ILE A C   1 
ATOM   1266 O  O   . ILE A 1 158 ? 30.462  -4.901  25.987  1.00 15.37 ? 158 ILE A O   1 
ATOM   1267 C  CB  . ILE A 1 158 ? 30.580  -5.788  22.742  1.00 16.81 ? 158 ILE A CB  1 
ATOM   1268 C  CG1 . ILE A 1 158 ? 31.536  -5.824  21.558  1.00 19.53 ? 158 ILE A CG1 1 
ATOM   1269 C  CG2 . ILE A 1 158 ? 29.822  -4.448  22.790  1.00 17.28 ? 158 ILE A CG2 1 
ATOM   1270 C  CD1 . ILE A 1 158 ? 30.806  -5.799  20.224  1.00 19.76 ? 158 ILE A CD1 1 
ATOM   1271 N  N   . PHE A 1 159 ? 29.457  -6.842  25.443  1.00 13.00 ? 159 PHE A N   1 
ATOM   1272 C  CA  . PHE A 1 159 ? 28.371  -6.646  26.406  1.00 14.77 ? 159 PHE A CA  1 
ATOM   1273 C  C   . PHE A 1 159 ? 28.881  -6.545  27.852  1.00 15.25 ? 159 PHE A C   1 
ATOM   1274 O  O   . PHE A 1 159 ? 28.252  -5.847  28.629  1.00 16.67 ? 159 PHE A O   1 
ATOM   1275 C  CB  . PHE A 1 159 ? 27.340  -7.765  26.338  1.00 13.48 ? 159 PHE A CB  1 
ATOM   1276 C  CG  . PHE A 1 159 ? 26.602  -7.883  25.013  1.00 14.74 ? 159 PHE A CG  1 
ATOM   1277 C  CD1 . PHE A 1 159 ? 26.527  -6.836  24.094  1.00 15.42 ? 159 PHE A CD1 1 
ATOM   1278 C  CD2 . PHE A 1 159 ? 25.973  -9.075  24.699  1.00 15.78 ? 159 PHE A CD2 1 
ATOM   1279 C  CE1 . PHE A 1 159 ? 25.807  -6.998  22.906  1.00 16.41 ? 159 PHE A CE1 1 
ATOM   1280 C  CE2 . PHE A 1 159 ? 25.309  -9.246  23.496  1.00 17.42 ? 159 PHE A CE2 1 
ATOM   1281 C  CZ  . PHE A 1 159 ? 25.220  -8.192  22.603  1.00 15.70 ? 159 PHE A CZ  1 
ATOM   1282 N  N   . SER A 1 160 ? 30.074  -7.106  28.155  1.00 15.86 ? 160 SER A N   1 
ATOM   1283 C  CA  . SER A 1 160 ? 30.593  -7.000  29.523  1.00 18.50 ? 160 SER A CA  1 
ATOM   1284 C  C   . SER A 1 160 ? 30.965  -5.567  29.900  1.00 21.35 ? 160 SER A C   1 
ATOM   1285 O  O   . SER A 1 160 ? 31.147  -5.278  31.091  1.00 22.01 ? 160 SER A O   1 
ATOM   1286 C  CB  . SER A 1 160 ? 31.747  -7.948  29.708  1.00 18.13 ? 160 SER A CB  1 
ATOM   1287 O  OG  . SER A 1 160 ? 32.859  -7.512  28.947  1.00 21.59 ? 160 SER A OG  1 
ATOM   1288 N  N   . HIS A 1 161 ? 31.095  -4.666  28.904  1.00 17.57 ? 161 HIS A N   1 
ATOM   1289 C  CA  . HIS A 1 161 ? 31.398  -3.273  29.145  1.00 16.89 ? 161 HIS A CA  1 
ATOM   1290 C  C   . HIS A 1 161 ? 30.171  -2.356  29.204  1.00 17.41 ? 161 HIS A C   1 
ATOM   1291 O  O   . HIS A 1 161 ? 30.348  -1.152  29.434  1.00 17.40 ? 161 HIS A O   1 
ATOM   1292 C  CB  . HIS A 1 161 ? 32.421  -2.725  28.141  1.00 18.16 ? 161 HIS A CB  1 
ATOM   1293 C  CG  . HIS A 1 161 ? 33.699  -3.490  28.152  1.00 18.58 ? 161 HIS A CG  1 
ATOM   1294 N  ND1 . HIS A 1 161 ? 34.789  -3.094  28.932  1.00 22.80 ? 161 HIS A ND1 1 
ATOM   1295 C  CD2 . HIS A 1 161 ? 34.095  -4.585  27.464  1.00 20.41 ? 161 HIS A CD2 1 
ATOM   1296 C  CE1 . HIS A 1 161 ? 35.791  -3.940  28.739  1.00 22.60 ? 161 HIS A CE1 1 
ATOM   1297 N  NE2 . HIS A 1 161 ? 35.397  -4.867  27.839  1.00 22.23 ? 161 HIS A NE2 1 
ATOM   1298 N  N   . LEU A 1 162 ? 28.956  -2.899  28.971  1.00 15.97 ? 162 LEU A N   1 
ATOM   1299 C  CA  . LEU A 1 162 ? 27.800  -2.018  28.850  1.00 16.46 ? 162 LEU A CA  1 
ATOM   1300 C  C   . LEU A 1 162 ? 27.536  -1.222  30.128  1.00 17.44 ? 162 LEU A C   1 
ATOM   1301 O  O   . LEU A 1 162 ? 27.084  -0.082  30.028  1.00 16.10 ? 162 LEU A O   1 
ATOM   1302 C  CB  . LEU A 1 162 ? 26.535  -2.816  28.523  1.00 16.87 ? 162 LEU A CB  1 
ATOM   1303 C  CG  . LEU A 1 162 ? 26.463  -3.438  27.127  1.00 17.23 ? 162 LEU A CG  1 
ATOM   1304 C  CD1 . LEU A 1 162 ? 25.237  -4.334  26.995  1.00 18.14 ? 162 LEU A CD1 1 
ATOM   1305 C  CD2 . LEU A 1 162 ? 26.471  -2.362  26.048  1.00 21.13 ? 162 LEU A CD2 1 
ATOM   1306 N  N   . GLN A 1 163 ? 27.820  -1.803  31.311  1.00 20.71 ? 163 GLN A N   1 
ATOM   1307 C  CA  . GLN A 1 163 ? 27.514  -1.047  32.531  1.00 25.09 ? 163 GLN A CA  1 
ATOM   1308 C  C   . GLN A 1 163 ? 28.326  0.243   32.605  1.00 24.33 ? 163 GLN A C   1 
ATOM   1309 O  O   . GLN A 1 163 ? 27.844  1.228   33.173  1.00 30.02 ? 163 GLN A O   1 
ATOM   1310 C  CB  . GLN A 1 163 ? 27.483  -1.866  33.828  1.00 34.30 ? 163 GLN A CB  1 
ATOM   1311 C  CG  . GLN A 1 163 ? 28.380  -3.099  33.850  1.00 42.42 ? 163 GLN A CG  1 
ATOM   1312 C  CD  . GLN A 1 163 ? 29.873  -2.860  33.887  1.00 47.58 ? 163 GLN A CD  1 
ATOM   1313 O  OE1 . GLN A 1 163 ? 30.502  -2.612  32.858  1.00 45.68 ? 163 GLN A OE1 1 
ATOM   1314 N  NE2 . GLN A 1 163 ? 30.463  -3.004  35.070  1.00 45.18 ? 163 GLN A NE2 1 
ATOM   1315 N  N   . HIS A 1 164 ? 29.477  0.281   31.925  1.00 18.33 ? 164 HIS A N   1 
ATOM   1316 C  CA  . HIS A 1 164 ? 30.305  1.482   32.008  1.00 19.02 ? 164 HIS A CA  1 
ATOM   1317 C  C   . HIS A 1 164 ? 29.883  2.552   31.006  1.00 18.10 ? 164 HIS A C   1 
ATOM   1318 O  O   . HIS A 1 164 ? 30.467  3.627   30.980  1.00 20.30 ? 164 HIS A O   1 
ATOM   1319 C  CB  . HIS A 1 164 ? 31.797  1.178   31.782  1.00 20.94 ? 164 HIS A CB  1 
ATOM   1320 C  CG  . HIS A 1 164 ? 32.429  0.318   32.829  1.00 19.64 ? 164 HIS A CG  1 
ATOM   1321 N  ND1 . HIS A 1 164 ? 32.301  0.551   34.171  1.00 21.22 ? 164 HIS A ND1 1 
ATOM   1322 C  CD2 . HIS A 1 164 ? 33.255  -0.736  32.707  1.00 24.50 ? 164 HIS A CD2 1 
ATOM   1323 C  CE1 . HIS A 1 164 ? 32.959  -0.384  34.835  1.00 20.31 ? 164 HIS A CE1 1 
ATOM   1324 N  NE2 . HIS A 1 164 ? 33.548  -1.176  33.973  1.00 29.47 ? 164 HIS A NE2 1 
ATOM   1325 N  N   . VAL A 1 165 ? 28.940  2.233   30.090  1.00 15.39 ? 165 VAL A N   1 
ATOM   1326 C  CA  . VAL A 1 165 ? 28.451  3.230   29.147  1.00 15.48 ? 165 VAL A CA  1 
ATOM   1327 C  C   . VAL A 1 165 ? 26.939  3.344   29.232  1.00 15.20 ? 165 VAL A C   1 
ATOM   1328 O  O   . VAL A 1 165 ? 26.242  3.590   28.245  1.00 14.89 ? 165 VAL A O   1 
ATOM   1329 C  CB  . VAL A 1 165 ? 28.901  2.908   27.700  1.00 14.92 ? 165 VAL A CB  1 
ATOM   1330 C  CG1 . VAL A 1 165 ? 30.435  3.033   27.533  1.00 16.89 ? 165 VAL A CG1 1 
ATOM   1331 C  CG2 . VAL A 1 165 ? 28.449  1.543   27.220  1.00 15.18 ? 165 VAL A CG2 1 
ATOM   1332 N  N   . LYS A 1 166 ? 26.421  3.302   30.470  1.00 16.44 ? 166 LYS A N   1 
ATOM   1333 C  CA  . LYS A 1 166 ? 24.994  3.322   30.730  1.00 17.06 ? 166 LYS A CA  1 
ATOM   1334 C  C   . LYS A 1 166 ? 24.327  4.575   30.159  1.00 15.35 ? 166 LYS A C   1 
ATOM   1335 O  O   . LYS A 1 166 ? 23.218  4.478   29.649  1.00 17.34 ? 166 LYS A O   1 
ATOM   1336 C  CB  . LYS A 1 166 ? 24.794  3.273   32.250  1.00 20.77 ? 166 LYS A CB  1 
ATOM   1337 C  CG  . LYS A 1 166 ? 23.383  3.061   32.775  1.00 27.23 ? 166 LYS A CG  1 
ATOM   1338 C  CD  . LYS A 1 166 ? 23.387  2.602   34.246  1.00 31.45 ? 166 LYS A CD  1 
ATOM   1339 C  CE  . LYS A 1 166 ? 24.060  1.251   34.428  1.00 38.28 ? 166 LYS A CE  1 
ATOM   1340 N  NZ  . LYS A 1 166 ? 23.354  0.151   33.715  1.00 43.44 ? 166 LYS A NZ  1 
ATOM   1341 N  N   . TYR A 1 167 ? 24.954  5.759   30.333  1.00 14.58 ? 167 TYR A N   1 
ATOM   1342 C  CA  . TYR A 1 167 ? 24.321  7.014   29.953  1.00 14.16 ? 167 TYR A CA  1 
ATOM   1343 C  C   . TYR A 1 167 ? 24.980  7.695   28.754  1.00 14.51 ? 167 TYR A C   1 
ATOM   1344 O  O   . TYR A 1 167 ? 26.156  7.466   28.406  1.00 14.75 ? 167 TYR A O   1 
ATOM   1345 C  CB  . TYR A 1 167 ? 24.354  8.016   31.117  1.00 15.00 ? 167 TYR A CB  1 
ATOM   1346 C  CG  . TYR A 1 167 ? 23.647  7.525   32.355  1.00 15.96 ? 167 TYR A CG  1 
ATOM   1347 C  CD1 . TYR A 1 167 ? 22.270  7.537   32.425  1.00 17.16 ? 167 TYR A CD1 1 
ATOM   1348 C  CD2 . TYR A 1 167 ? 24.370  7.023   33.435  1.00 17.40 ? 167 TYR A CD2 1 
ATOM   1349 C  CE1 . TYR A 1 167 ? 21.608  7.047   33.547  1.00 19.20 ? 167 TYR A CE1 1 
ATOM   1350 C  CE2 . TYR A 1 167 ? 23.725  6.534   34.566  1.00 20.04 ? 167 TYR A CE2 1 
ATOM   1351 C  CZ  . TYR A 1 167 ? 22.343  6.573   34.621  1.00 22.05 ? 167 TYR A CZ  1 
ATOM   1352 O  OH  . TYR A 1 167 ? 21.715  6.091   35.741  1.00 23.14 ? 167 TYR A OH  1 
ATOM   1353 N  N   . LYS A 1 168 ? 24.165  8.520   28.096  1.00 15.96 ? 168 LYS A N   1 
ATOM   1354 C  CA  . LYS A 1 168 ? 24.649  9.263   26.944  1.00 16.64 ? 168 LYS A CA  1 
ATOM   1355 C  C   . LYS A 1 168 ? 25.941  10.009  27.260  1.00 18.39 ? 168 LYS A C   1 
ATOM   1356 O  O   . LYS A 1 168 ? 26.045  10.652  28.307  1.00 17.00 ? 168 LYS A O   1 
ATOM   1357 C  CB  . LYS A 1 168 ? 23.560  10.224  26.473  1.00 16.63 ? 168 LYS A CB  1 
ATOM   1358 C  CG  . LYS A 1 168 ? 23.922  10.912  25.163  1.00 17.87 ? 168 LYS A CG  1 
ATOM   1359 C  CD  . LYS A 1 168 ? 22.853  11.874  24.680  1.00 20.93 ? 168 LYS A CD  1 
ATOM   1360 C  CE  . LYS A 1 168 ? 23.305  12.546  23.398  1.00 25.61 ? 168 LYS A CE  1 
ATOM   1361 N  NZ  . LYS A 1 168 ? 22.260  13.408  22.792  1.00 29.07 ? 168 LYS A NZ  1 
ATOM   1362 N  N   . GLY A 1 169 ? 26.933  9.886   26.364  1.00 17.79 ? 169 GLY A N   1 
ATOM   1363 C  CA  . GLY A 1 169 ? 28.193  10.579  26.554  1.00 19.33 ? 169 GLY A CA  1 
ATOM   1364 C  C   . GLY A 1 169 ? 29.239  9.748   27.280  1.00 19.38 ? 169 GLY A C   1 
ATOM   1365 O  O   . GLY A 1 169 ? 30.418  10.075  27.246  1.00 23.74 ? 169 GLY A O   1 
ATOM   1366 N  N   . GLN A 1 170 ? 28.849  8.656   27.931  1.00 16.75 ? 170 GLN A N   1 
ATOM   1367 C  CA  . GLN A 1 170 ? 29.871  7.900   28.633  1.00 15.59 ? 170 GLN A CA  1 
ATOM   1368 C  C   . GLN A 1 170 ? 30.654  7.004   27.680  1.00 17.47 ? 170 GLN A C   1 
ATOM   1369 O  O   . GLN A 1 170 ? 30.181  6.704   26.574  1.00 17.14 ? 170 GLN A O   1 
ATOM   1370 C  CB  . GLN A 1 170 ? 29.187  7.068   29.709  1.00 16.12 ? 170 GLN A CB  1 
ATOM   1371 C  CG  . GLN A 1 170 ? 28.648  7.936   30.826  1.00 16.03 ? 170 GLN A CG  1 
ATOM   1372 C  CD  . GLN A 1 170 ? 28.095  7.104   31.956  1.00 16.84 ? 170 GLN A CD  1 
ATOM   1373 O  OE1 . GLN A 1 170 ? 27.505  6.040   31.776  1.00 17.01 ? 170 GLN A OE1 1 
ATOM   1374 N  NE2 . GLN A 1 170 ? 28.260  7.599   33.187  1.00 16.55 ? 170 GLN A NE2 1 
ATOM   1375 N  N   A GLU A 1 171 ? 31.847  6.557   28.098  0.50 16.17 ? 171 GLU A N   1 
ATOM   1376 N  N   B GLU A 1 171 ? 31.840  6.579   28.130  0.50 15.42 ? 171 GLU A N   1 
ATOM   1377 C  CA  A GLU A 1 171 ? 32.839  5.955   27.215  0.50 17.95 ? 171 GLU A CA  1 
ATOM   1378 C  CA  B GLU A 1 171 ? 32.773  5.827   27.313  0.50 16.17 ? 171 GLU A CA  1 
ATOM   1379 C  C   A GLU A 1 171 ? 33.678  4.970   28.012  0.50 15.24 ? 171 GLU A C   1 
ATOM   1380 C  C   B GLU A 1 171 ? 33.470  4.762   28.137  0.50 15.56 ? 171 GLU A C   1 
ATOM   1381 O  O   A GLU A 1 171 ? 33.923  5.241   29.206  0.50 15.94 ? 171 GLU A O   1 
ATOM   1382 O  O   B GLU A 1 171 ? 33.452  4.749   29.390  0.50 12.82 ? 171 GLU A O   1 
ATOM   1383 C  CB  A GLU A 1 171 ? 33.771  7.037   26.652  0.50 20.59 ? 171 GLU A CB  1 
ATOM   1384 C  CB  B GLU A 1 171 ? 33.789  6.727   26.594  0.50 17.49 ? 171 GLU A CB  1 
ATOM   1385 C  CG  A GLU A 1 171 ? 33.158  7.890   25.556  0.50 22.23 ? 171 GLU A CG  1 
ATOM   1386 C  CG  B GLU A 1 171 ? 34.790  7.393   27.524  0.50 17.90 ? 171 GLU A CG  1 
ATOM   1387 C  CD  A GLU A 1 171 ? 33.924  9.120   25.064  0.50 24.29 ? 171 GLU A CD  1 
ATOM   1388 C  CD  B GLU A 1 171 ? 35.883  8.262   26.906  0.50 20.54 ? 171 GLU A CD  1 
ATOM   1389 O  OE1 A GLU A 1 171 ? 35.089  9.315   25.480  0.50 25.82 ? 171 GLU A OE1 1 
ATOM   1390 O  OE1 B GLU A 1 171 ? 35.634  8.903   25.852  0.50 21.71 ? 171 GLU A OE1 1 
ATOM   1391 O  OE2 A GLU A 1 171 ? 33.352  9.891   24.266  0.50 25.65 ? 171 GLU A OE2 1 
ATOM   1392 O  OE2 B GLU A 1 171 ? 36.999  8.297   27.495  0.50 17.38 ? 171 GLU A OE2 1 
ATOM   1393 N  N   . ALA A 1 172 ? 34.040  3.827   27.402  1.00 16.20 ? 172 ALA A N   1 
ATOM   1394 C  CA  . ALA A 1 172 ? 34.793  2.754   28.019  1.00 15.92 ? 172 ALA A CA  1 
ATOM   1395 C  C   . ALA A 1 172 ? 35.798  2.263   26.994  1.00 18.00 ? 172 ALA A C   1 
ATOM   1396 O  O   . ALA A 1 172 ? 35.616  2.463   25.791  1.00 19.14 ? 172 ALA A O   1 
ATOM   1397 C  CB  . ALA A 1 172 ? 33.867  1.646   28.460  1.00 19.30 ? 172 ALA A CB  1 
ATOM   1398 N  N   . PHE A 1 173 ? 36.863  1.632   27.454  1.00 18.69 ? 173 PHE A N   1 
ATOM   1399 C  CA  . PHE A 1 173 ? 37.864  1.070   26.579  1.00 20.66 ? 173 PHE A CA  1 
ATOM   1400 C  C   . PHE A 1 173 ? 37.693  -0.444  26.532  1.00 21.77 ? 173 PHE A C   1 
ATOM   1401 O  O   . PHE A 1 173 ? 37.554  -1.113  27.564  1.00 22.37 ? 173 PHE A O   1 
ATOM   1402 C  CB  . PHE A 1 173 ? 39.228  1.569   27.069  1.00 21.60 ? 173 PHE A CB  1 
ATOM   1403 C  CG  . PHE A 1 173 ? 39.520  2.969   26.584  1.00 23.19 ? 173 PHE A CG  1 
ATOM   1404 C  CD1 . PHE A 1 173 ? 39.808  3.215   25.243  1.00 29.10 ? 173 PHE A CD1 1 
ATOM   1405 C  CD2 . PHE A 1 173 ? 39.461  4.056   27.441  1.00 29.88 ? 173 PHE A CD2 1 
ATOM   1406 C  CE1 . PHE A 1 173 ? 40.082  4.498   24.786  1.00 29.08 ? 173 PHE A CE1 1 
ATOM   1407 C  CE2 . PHE A 1 173 ? 39.728  5.338   26.983  1.00 30.76 ? 173 PHE A CE2 1 
ATOM   1408 C  CZ  . PHE A 1 173 ? 40.046  5.562   25.663  1.00 29.70 ? 173 PHE A CZ  1 
ATOM   1409 N  N   . VAL A 1 174 ? 37.668  -0.987  25.304  1.00 16.51 ? 174 VAL A N   1 
ATOM   1410 C  CA  . VAL A 1 174 ? 37.551  -2.398  25.056  1.00 18.50 ? 174 VAL A CA  1 
ATOM   1411 C  C   . VAL A 1 174 ? 38.865  -2.921  24.496  1.00 18.91 ? 174 VAL A C   1 
ATOM   1412 O  O   . VAL A 1 174 ? 39.313  -2.437  23.459  1.00 19.57 ? 174 VAL A O   1 
ATOM   1413 C  CB  . VAL A 1 174 ? 36.397  -2.641  24.068  1.00 16.05 ? 174 VAL A CB  1 
ATOM   1414 C  CG1 . VAL A 1 174 ? 36.263  -4.125  23.916  1.00 18.76 ? 174 VAL A CG1 1 
ATOM   1415 C  CG2 . VAL A 1 174 ? 35.110  -2.027  24.630  1.00 18.49 ? 174 VAL A CG2 1 
ATOM   1416 N  N   . PRO A 1 175 ? 39.487  -3.955  25.106  1.00 18.13 ? 175 PRO A N   1 
ATOM   1417 C  CA  . PRO A 1 175 ? 40.723  -4.515  24.559  1.00 19.04 ? 175 PRO A CA  1 
ATOM   1418 C  C   . PRO A 1 175 ? 40.416  -5.139  23.205  1.00 18.22 ? 175 PRO A C   1 
ATOM   1419 O  O   . PRO A 1 175 ? 39.361  -5.743  23.055  1.00 18.04 ? 175 PRO A O   1 
ATOM   1420 C  CB  . PRO A 1 175 ? 41.091  -5.637  25.538  1.00 21.64 ? 175 PRO A CB  1 
ATOM   1421 C  CG  . PRO A 1 175 ? 40.385  -5.237  26.818  1.00 23.28 ? 175 PRO A CG  1 
ATOM   1422 C  CD  . PRO A 1 175 ? 39.097  -4.527  26.403  1.00 19.56 ? 175 PRO A CD  1 
ATOM   1423 N  N   . GLY A 1 176 ? 41.372  -5.052  22.281  1.00 18.88 ? 176 GLY A N   1 
ATOM   1424 C  CA  . GLY A 1 176 ? 41.161  -5.678  20.991  1.00 17.41 ? 176 GLY A CA  1 
ATOM   1425 C  C   . GLY A 1 176 ? 40.779  -7.148  21.106  1.00 18.01 ? 176 GLY A C   1 
ATOM   1426 O  O   . GLY A 1 176 ? 41.331  -7.905  21.929  1.00 19.87 ? 176 GLY A O   1 
ATOM   1427 N  N   . PHE A 1 177 ? 39.866  -7.603  20.238  1.00 15.98 ? 177 PHE A N   1 
ATOM   1428 C  CA  . PHE A 1 177 ? 39.539  -8.994  20.032  1.00 14.57 ? 177 PHE A CA  1 
ATOM   1429 C  C   . PHE A 1 177 ? 39.220  -9.210  18.551  1.00 13.24 ? 177 PHE A C   1 
ATOM   1430 O  O   . PHE A 1 177 ? 39.242  -8.236  17.805  1.00 14.86 ? 177 PHE A O   1 
ATOM   1431 C  CB  . PHE A 1 177 ? 38.392  -9.462  20.943  1.00 16.49 ? 177 PHE A CB  1 
ATOM   1432 C  CG  . PHE A 1 177 ? 37.029  -8.876  20.634  1.00 15.65 ? 177 PHE A CG  1 
ATOM   1433 C  CD1 . PHE A 1 177 ? 36.699  -7.597  21.058  1.00 15.59 ? 177 PHE A CD1 1 
ATOM   1434 C  CD2 . PHE A 1 177 ? 36.099  -9.592  19.889  1.00 15.26 ? 177 PHE A CD2 1 
ATOM   1435 C  CE1 . PHE A 1 177 ? 35.445  -7.040  20.745  1.00 15.73 ? 177 PHE A CE1 1 
ATOM   1436 C  CE2 . PHE A 1 177 ? 34.866  -9.030  19.580  1.00 16.13 ? 177 PHE A CE2 1 
ATOM   1437 C  CZ  . PHE A 1 177 ? 34.531  -7.773  20.016  1.00 15.63 ? 177 PHE A CZ  1 
ATOM   1438 N  N   . ASN A 1 178 ? 39.046  -10.470 18.177  1.00 14.52 ? 178 ASN A N   1 
ATOM   1439 C  CA  . ASN A 1 178 ? 38.819  -10.804 16.779  1.00 14.65 ? 178 ASN A CA  1 
ATOM   1440 C  C   . ASN A 1 178 ? 37.348  -10.513 16.426  1.00 15.35 ? 178 ASN A C   1 
ATOM   1441 O  O   . ASN A 1 178 ? 36.425  -11.288 16.727  1.00 13.87 ? 178 ASN A O   1 
ATOM   1442 C  CB  . ASN A 1 178 ? 39.226  -12.247 16.460  1.00 16.80 ? 178 ASN A CB  1 
ATOM   1443 C  CG  . ASN A 1 178 ? 39.008  -12.640 15.025  1.00 17.41 ? 178 ASN A CG  1 
ATOM   1444 O  OD1 . ASN A 1 178 ? 38.737  -11.805 14.162  1.00 16.75 ? 178 ASN A OD1 1 
ATOM   1445 N  ND2 . ASN A 1 178 ? 39.102  -13.919 14.749  1.00 21.87 ? 178 ASN A ND2 1 
ATOM   1446 N  N   . ILE A 1 179 ? 37.133  -9.383  15.736  1.00 12.54 ? 179 ILE A N   1 
ATOM   1447 C  CA  . ILE A 1 179 ? 35.779  -8.974  15.345  1.00 12.18 ? 179 ILE A CA  1 
ATOM   1448 C  C   . ILE A 1 179 ? 35.108  -10.014 14.444  1.00 12.21 ? 179 ILE A C   1 
ATOM   1449 O  O   . ILE A 1 179 ? 33.863  -10.086 14.382  1.00 11.54 ? 179 ILE A O   1 
ATOM   1450 C  CB  . ILE A 1 179 ? 35.831  -7.600  14.658  1.00 11.14 ? 179 ILE A CB  1 
ATOM   1451 C  CG1 . ILE A 1 179 ? 36.458  -6.519  15.533  1.00 12.32 ? 179 ILE A CG1 1 
ATOM   1452 C  CG2 . ILE A 1 179 ? 34.425  -7.188  14.198  1.00 12.49 ? 179 ILE A CG2 1 
ATOM   1453 C  CD1 . ILE A 1 179 ? 35.841  -6.361  16.919  1.00 14.60 ? 179 ILE A CD1 1 
ATOM   1454 N  N   . GLU A 1 180 ? 35.879  -10.834 13.718  1.00 12.63 ? 180 GLU A N   1 
ATOM   1455 C  CA  . GLU A 1 180 ? 35.248  -11.826 12.869  1.00 13.08 ? 180 GLU A CA  1 
ATOM   1456 C  C   . GLU A 1 180 ? 34.452  -12.842 13.700  1.00 13.76 ? 180 GLU A C   1 
ATOM   1457 O  O   . GLU A 1 180 ? 33.585  -13.508 13.144  1.00 14.56 ? 180 GLU A O   1 
ATOM   1458 C  CB  . GLU A 1 180 ? 36.289  -12.549 12.013  1.00 15.59 ? 180 GLU A CB  1 
ATOM   1459 C  CG  . GLU A 1 180 ? 35.728  -13.242 10.784  1.00 19.55 ? 180 GLU A CG  1 
ATOM   1460 C  CD  . GLU A 1 180 ? 36.759  -13.774 9.805   1.00 20.35 ? 180 GLU A CD  1 
ATOM   1461 O  OE1 . GLU A 1 180 ? 37.948  -13.484 9.996   1.00 22.54 ? 180 GLU A OE1 1 
ATOM   1462 O  OE2 . GLU A 1 180 ? 36.336  -14.533 8.919   1.00 25.14 ? 180 GLU A OE2 1 
ATOM   1463 N  N   . GLU A 1 181 ? 34.771  -12.951 14.998  1.00 12.98 ? 181 GLU A N   1 
ATOM   1464 C  CA  . GLU A 1 181 ? 34.013  -13.828 15.889  1.00 14.25 ? 181 GLU A CA  1 
ATOM   1465 C  C   . GLU A 1 181 ? 32.549  -13.382 16.055  1.00 12.43 ? 181 GLU A C   1 
ATOM   1466 O  O   . GLU A 1 181 ? 31.710  -14.195 16.425  1.00 14.02 ? 181 GLU A O   1 
ATOM   1467 C  CB  . GLU A 1 181 ? 34.608  -13.813 17.287  1.00 15.59 ? 181 GLU A CB  1 
ATOM   1468 C  CG  . GLU A 1 181 ? 35.988  -14.452 17.409  1.00 17.84 ? 181 GLU A CG  1 
ATOM   1469 C  CD  . GLU A 1 181 ? 36.658  -14.236 18.752  1.00 21.22 ? 181 GLU A CD  1 
ATOM   1470 O  OE1 . GLU A 1 181 ? 35.981  -13.794 19.765  1.00 21.34 ? 181 GLU A OE1 1 
ATOM   1471 O  OE2 . GLU A 1 181 ? 37.877  -14.490 18.780  1.00 21.45 ? 181 GLU A OE2 1 
ATOM   1472 N  N   . LEU A 1 182 ? 32.246  -12.117 15.710  1.00 11.75 ? 182 LEU A N   1 
ATOM   1473 C  CA  . LEU A 1 182 ? 30.858  -11.631 15.754  1.00 10.61 ? 182 LEU A CA  1 
ATOM   1474 C  C   . LEU A 1 182 ? 30.058  -11.999 14.511  1.00 11.12 ? 182 LEU A C   1 
ATOM   1475 O  O   . LEU A 1 182 ? 28.838  -11.818 14.500  1.00 11.31 ? 182 LEU A O   1 
ATOM   1476 C  CB  . LEU A 1 182 ? 30.862  -10.108 15.867  1.00 10.18 ? 182 LEU A CB  1 
ATOM   1477 C  CG  . LEU A 1 182 ? 31.658  -9.542  17.048  1.00 10.02 ? 182 LEU A CG  1 
ATOM   1478 C  CD1 . LEU A 1 182 ? 31.563  -8.021  17.066  1.00 11.47 ? 182 LEU A CD1 1 
ATOM   1479 C  CD2 . LEU A 1 182 ? 31.148  -10.053 18.392  1.00 12.75 ? 182 LEU A CD2 1 
ATOM   1480 N  N   . LEU A 1 183 ? 30.712  -12.495 13.458  1.00 10.52 ? 183 LEU A N   1 
ATOM   1481 C  CA  . LEU A 1 183 ? 30.032  -12.865 12.237  1.00 11.66 ? 183 LEU A CA  1 
ATOM   1482 C  C   . LEU A 1 183 ? 29.451  -14.248 12.340  1.00 12.47 ? 183 LEU A C   1 
ATOM   1483 O  O   . LEU A 1 183 ? 30.007  -15.093 13.056  1.00 13.60 ? 183 LEU A O   1 
ATOM   1484 C  CB  . LEU A 1 183 ? 31.009  -12.772 11.057  1.00 12.57 ? 183 LEU A CB  1 
ATOM   1485 C  CG  . LEU A 1 183 ? 31.664  -11.401 10.874  1.00 12.75 ? 183 LEU A CG  1 
ATOM   1486 C  CD1 . LEU A 1 183 ? 32.515  -11.398 9.610   1.00 15.79 ? 183 LEU A CD1 1 
ATOM   1487 C  CD2 . LEU A 1 183 ? 30.626  -10.294 10.754  1.00 13.61 ? 183 LEU A CD2 1 
ATOM   1488 N  N   . PRO A 1 184 ? 28.407  -14.560 11.594  1.00 10.95 ? 184 PRO A N   1 
ATOM   1489 C  CA  . PRO A 1 184 ? 27.768  -15.860 11.637  1.00 12.71 ? 184 PRO A CA  1 
ATOM   1490 C  C   . PRO A 1 184 ? 28.520  -16.883 10.813  1.00 12.85 ? 184 PRO A C   1 
ATOM   1491 O  O   . PRO A 1 184 ? 29.572  -16.612 10.200  1.00 14.31 ? 184 PRO A O   1 
ATOM   1492 C  CB  . PRO A 1 184 ? 26.354  -15.543 11.061  1.00 13.05 ? 184 PRO A CB  1 
ATOM   1493 C  CG  . PRO A 1 184 ? 26.677  -14.466 10.000  1.00 12.75 ? 184 PRO A CG  1 
ATOM   1494 C  CD  . PRO A 1 184 ? 27.732  -13.624 10.659  1.00 11.73 ? 184 PRO A CD  1 
ATOM   1495 N  N   . GLU A 1 185 ? 27.940  -18.086 10.877  1.00 15.95 ? 185 GLU A N   1 
ATOM   1496 C  CA  . GLU A 1 185 ? 28.373  -19.201 10.054  1.00 17.14 ? 185 GLU A CA  1 
ATOM   1497 C  C   . GLU A 1 185 ? 28.070  -18.903 8.593   1.00 18.14 ? 185 GLU A C   1 
ATOM   1498 O  O   . GLU A 1 185 ? 27.127  -18.175 8.264   1.00 17.32 ? 185 GLU A O   1 
ATOM   1499 C  CB  . GLU A 1 185 ? 27.514  -20.432 10.407  1.00 21.26 ? 185 GLU A CB  1 
ATOM   1500 C  CG  . GLU A 1 185 ? 27.847  -20.984 11.788  1.00 29.58 ? 185 GLU A CG  1 
ATOM   1501 C  CD  . GLU A 1 185 ? 29.348  -21.164 11.906  1.00 38.00 ? 185 GLU A CD  1 
ATOM   1502 O  OE1 . GLU A 1 185 ? 29.848  -22.147 11.328  1.00 43.48 ? 185 GLU A OE1 1 
ATOM   1503 O  OE2 . GLU A 1 185 ? 30.022  -20.300 12.517  1.00 38.72 ? 185 GLU A OE2 1 
ATOM   1504 N  N   . ARG A 1 186 ? 28.968  -19.371 7.718   1.00 17.21 ? 186 ARG A N   1 
ATOM   1505 C  CA  . ARG A 1 186 ? 28.820  -19.335 6.284   1.00 18.00 ? 186 ARG A CA  1 
ATOM   1506 C  C   . ARG A 1 186 ? 28.591  -17.890 5.837   1.00 14.59 ? 186 ARG A C   1 
ATOM   1507 O  O   . ARG A 1 186 ? 27.626  -17.561 5.155   1.00 15.15 ? 186 ARG A O   1 
ATOM   1508 C  CB  . ARG A 1 186 ? 27.726  -20.294 5.807   1.00 20.20 ? 186 ARG A CB  1 
ATOM   1509 C  CG  . ARG A 1 186 ? 28.001  -21.724 6.263   1.00 24.82 ? 186 ARG A CG  1 
ATOM   1510 C  CD  . ARG A 1 186 ? 27.178  -22.802 5.579   1.00 23.91 ? 186 ARG A CD  1 
ATOM   1511 N  NE  . ARG A 1 186 ? 25.745  -22.572 5.623   1.00 28.46 ? 186 ARG A NE  1 
ATOM   1512 C  CZ  . ARG A 1 186 ? 24.973  -22.669 6.694   1.00 30.65 ? 186 ARG A CZ  1 
ATOM   1513 N  NH1 . ARG A 1 186 ? 25.500  -23.017 7.860   1.00 31.18 ? 186 ARG A NH1 1 
ATOM   1514 N  NH2 . ARG A 1 186 ? 23.676  -22.433 6.580   1.00 33.23 ? 186 ARG A NH2 1 
ATOM   1515 N  N   . THR A 1 187 ? 29.585  -17.091 6.129   1.00 13.48 ? 187 THR A N   1 
ATOM   1516 C  CA  . THR A 1 187 ? 29.534  -15.713 5.652   1.00 14.05 ? 187 THR A CA  1 
ATOM   1517 C  C   . THR A 1 187 ? 29.531  -15.594 4.131   1.00 13.96 ? 187 THR A C   1 
ATOM   1518 O  O   . THR A 1 187 ? 29.184  -14.524 3.640   1.00 14.05 ? 187 THR A O   1 
ATOM   1519 C  CB  . THR A 1 187 ? 30.634  -14.835 6.238   1.00 13.99 ? 187 THR A CB  1 
ATOM   1520 O  OG1 . THR A 1 187 ? 31.848  -15.521 6.012   1.00 16.58 ? 187 THR A OG1 1 
ATOM   1521 C  CG2 . THR A 1 187 ? 30.501  -14.550 7.724   1.00 14.49 ? 187 THR A CG2 1 
ATOM   1522 N  N   . ALA A 1 188 ? 29.834  -16.684 3.398   1.00 14.77 ? 188 ALA A N   1 
ATOM   1523 C  CA  . ALA A 1 188 ? 29.644  -16.685 1.948   1.00 15.98 ? 188 ALA A CA  1 
ATOM   1524 C  C   . ALA A 1 188 ? 28.192  -16.429 1.523   1.00 14.27 ? 188 ALA A C   1 
ATOM   1525 O  O   . ALA A 1 188 ? 27.962  -16.037 0.375   1.00 14.31 ? 188 ALA A O   1 
ATOM   1526 C  CB  . ALA A 1 188 ? 30.155  -18.001 1.336   1.00 16.35 ? 188 ALA A CB  1 
ATOM   1527 N  N   . GLU A 1 189 ? 27.237  -16.679 2.437   1.00 13.64 ? 189 GLU A N   1 
ATOM   1528 C  CA  . GLU A 1 189 ? 25.812  -16.607 2.141   1.00 12.40 ? 189 GLU A CA  1 
ATOM   1529 C  C   . GLU A 1 189 ? 25.323  -15.246 2.645   1.00 11.28 ? 189 GLU A C   1 
ATOM   1530 O  O   . GLU A 1 189 ? 25.284  -15.012 3.847   1.00 11.19 ? 189 GLU A O   1 
ATOM   1531 C  CB  . GLU A 1 189 ? 25.061  -17.752 2.824   1.00 16.31 ? 189 GLU A CB  1 
ATOM   1532 C  CG  . GLU A 1 189 ? 25.437  -19.160 2.331   1.00 19.85 ? 189 GLU A CG  1 
ATOM   1533 C  CD  . GLU A 1 189 ? 24.920  -20.336 3.145   1.00 24.63 ? 189 GLU A CD  1 
ATOM   1534 O  OE1 . GLU A 1 189 ? 24.112  -20.138 4.080   1.00 24.77 ? 189 GLU A OE1 1 
ATOM   1535 O  OE2 . GLU A 1 189 ? 25.413  -21.483 2.893   1.00 28.63 ? 189 GLU A OE2 1 
ATOM   1536 N  N   . TYR A 1 190 ? 24.907  -14.393 1.712   1.00 9.97  ? 190 TYR A N   1 
ATOM   1537 C  CA  . TYR A 1 190 ? 24.460  -13.046 2.075   1.00 10.33 ? 190 TYR A CA  1 
ATOM   1538 C  C   . TYR A 1 190 ? 23.468  -12.467 1.072   1.00 10.36 ? 190 TYR A C   1 
ATOM   1539 O  O   . TYR A 1 190 ? 23.402  -12.855 -0.107  1.00 10.61 ? 190 TYR A O   1 
ATOM   1540 C  CB  . TYR A 1 190 ? 25.649  -12.096 2.332   1.00 9.92  ? 190 TYR A CB  1 
ATOM   1541 C  CG  . TYR A 1 190 ? 26.569  -11.962 1.144   1.00 11.19 ? 190 TYR A CG  1 
ATOM   1542 C  CD1 . TYR A 1 190 ? 26.283  -11.065 0.132   1.00 11.20 ? 190 TYR A CD1 1 
ATOM   1543 C  CD2 . TYR A 1 190 ? 27.734  -12.706 1.046   1.00 12.15 ? 190 TYR A CD2 1 
ATOM   1544 C  CE1 . TYR A 1 190 ? 27.128  -10.890 -0.966  1.00 12.34 ? 190 TYR A CE1 1 
ATOM   1545 C  CE2 . TYR A 1 190 ? 28.610  -12.525 -0.029  1.00 12.12 ? 190 TYR A CE2 1 
ATOM   1546 C  CZ  . TYR A 1 190 ? 28.315  -11.611 -1.015  1.00 11.28 ? 190 TYR A CZ  1 
ATOM   1547 O  OH  . TYR A 1 190 ? 29.145  -11.348 -2.101  1.00 13.56 ? 190 TYR A OH  1 
ATOM   1548 N  N   . TYR A 1 191 ? 22.720  -11.461 1.534   1.00 9.34  ? 191 TYR A N   1 
ATOM   1549 C  CA  . TYR A 1 191 ? 21.906  -10.567 0.743   1.00 9.18  ? 191 TYR A CA  1 
ATOM   1550 C  C   . TYR A 1 191 ? 22.687  -9.291  0.452   1.00 9.98  ? 191 TYR A C   1 
ATOM   1551 O  O   . TYR A 1 191 ? 23.446  -8.829  1.324   1.00 10.20 ? 191 TYR A O   1 
ATOM   1552 C  CB  . TYR A 1 191 ? 20.627  -10.176 1.498   1.00 9.85  ? 191 TYR A CB  1 
ATOM   1553 C  CG  . TYR A 1 191 ? 19.829  -11.311 2.096   1.00 9.47  ? 191 TYR A CG  1 
ATOM   1554 C  CD1 . TYR A 1 191 ? 18.763  -11.845 1.374   1.00 10.72 ? 191 TYR A CD1 1 
ATOM   1555 C  CD2 . TYR A 1 191 ? 20.027  -11.736 3.408   1.00 10.25 ? 191 TYR A CD2 1 
ATOM   1556 C  CE1 . TYR A 1 191 ? 17.984  -12.858 1.938   1.00 11.29 ? 191 TYR A CE1 1 
ATOM   1557 C  CE2 . TYR A 1 191 ? 19.242  -12.715 3.986   1.00 10.84 ? 191 TYR A CE2 1 
ATOM   1558 C  CZ  . TYR A 1 191 ? 18.221  -13.258 3.242   1.00 11.94 ? 191 TYR A CZ  1 
ATOM   1559 O  OH  . TYR A 1 191 ? 17.449  -14.255 3.807   1.00 14.14 ? 191 TYR A OH  1 
ATOM   1560 N  N   . ARG A 1 192 ? 22.493  -8.713  -0.709  1.00 10.52 ? 192 ARG A N   1 
ATOM   1561 C  CA  . ARG A 1 192 ? 23.247  -7.516  -1.115  1.00 8.94  ? 192 ARG A CA  1 
ATOM   1562 C  C   . ARG A 1 192 ? 22.287  -6.571  -1.837  1.00 8.97  ? 192 ARG A C   1 
ATOM   1563 O  O   . ARG A 1 192 ? 21.563  -6.979  -2.743  1.00 10.28 ? 192 ARG A O   1 
ATOM   1564 C  CB  . ARG A 1 192 ? 24.312  -7.936  -2.127  1.00 10.39 ? 192 ARG A CB  1 
ATOM   1565 C  CG  . ARG A 1 192 ? 24.993  -6.801  -2.880  1.00 11.22 ? 192 ARG A CG  1 
ATOM   1566 C  CD  . ARG A 1 192 ? 25.819  -5.840  -2.042  1.00 11.33 ? 192 ARG A CD  1 
ATOM   1567 N  NE  . ARG A 1 192 ? 26.788  -6.487  -1.166  1.00 12.41 ? 192 ARG A NE  1 
ATOM   1568 C  CZ  . ARG A 1 192 ? 27.896  -7.098  -1.599  1.00 12.86 ? 192 ARG A CZ  1 
ATOM   1569 N  NH1 . ARG A 1 192 ? 28.214  -7.027  -2.895  1.00 14.39 ? 192 ARG A NH1 1 
ATOM   1570 N  NH2 . ARG A 1 192 ? 28.734  -7.681  -0.752  1.00 13.11 ? 192 ARG A NH2 1 
ATOM   1571 N  N   . TYR A 1 193 ? 22.286  -5.299  -1.427  1.00 8.66  ? 193 TYR A N   1 
ATOM   1572 C  CA  . TYR A 1 193 ? 21.470  -4.283  -2.077  1.00 8.95  ? 193 TYR A CA  1 
ATOM   1573 C  C   . TYR A 1 193 ? 22.076  -2.927  -1.808  1.00 9.23  ? 193 TYR A C   1 
ATOM   1574 O  O   . TYR A 1 193 ? 22.754  -2.709  -0.796  1.00 9.71  ? 193 TYR A O   1 
ATOM   1575 C  CB  . TYR A 1 193 ? 19.976  -4.373  -1.730  1.00 9.19  ? 193 TYR A CB  1 
ATOM   1576 C  CG  . TYR A 1 193 ? 19.599  -3.827  -0.373  1.00 7.76  ? 193 TYR A CG  1 
ATOM   1577 C  CD1 . TYR A 1 193 ? 19.802  -4.547  0.795   1.00 8.49  ? 193 TYR A CD1 1 
ATOM   1578 C  CD2 . TYR A 1 193 ? 19.079  -2.556  -0.276  1.00 8.99  ? 193 TYR A CD2 1 
ATOM   1579 C  CE1 . TYR A 1 193 ? 19.500  -4.026  2.039   1.00 8.21  ? 193 TYR A CE1 1 
ATOM   1580 C  CE2 . TYR A 1 193 ? 18.750  -2.016  0.948   1.00 8.83  ? 193 TYR A CE2 1 
ATOM   1581 C  CZ  . TYR A 1 193 ? 18.983  -2.737  2.109   1.00 8.00  ? 193 TYR A CZ  1 
ATOM   1582 O  OH  . TYR A 1 193 ? 18.688  -2.162  3.307   1.00 8.29  ? 193 TYR A OH  1 
ATOM   1583 N  N   . ARG A 1 194 ? 21.714  -1.960  -2.659  1.00 9.91  ? 194 ARG A N   1 
ATOM   1584 C  CA  . ARG A 1 194 ? 22.127  -0.573  -2.442  1.00 10.06 ? 194 ARG A CA  1 
ATOM   1585 C  C   . ARG A 1 194 ? 21.039  0.158   -1.675  1.00 9.20  ? 194 ARG A C   1 
ATOM   1586 O  O   . ARG A 1 194 ? 19.838  0.134   -2.000  1.00 10.32 ? 194 ARG A O   1 
ATOM   1587 C  CB  . ARG A 1 194 ? 22.260  0.140   -3.802  1.00 12.59 ? 194 ARG A CB  1 
ATOM   1588 C  CG  . ARG A 1 194 ? 23.407  -0.468  -4.591  1.00 18.04 ? 194 ARG A CG  1 
ATOM   1589 C  CD  . ARG A 1 194 ? 24.720  0.153   -4.181  1.00 29.12 ? 194 ARG A CD  1 
ATOM   1590 N  NE  . ARG A 1 194 ? 25.081  0.942   -5.354  1.00 44.97 ? 194 ARG A NE  1 
ATOM   1591 C  CZ  . ARG A 1 194 ? 26.312  1.333   -5.663  1.00 43.48 ? 194 ARG A CZ  1 
ATOM   1592 N  NH1 . ARG A 1 194 ? 27.328  1.027   -4.873  1.00 42.71 ? 194 ARG A NH1 1 
ATOM   1593 N  NH2 . ARG A 1 194 ? 26.510  2.023   -6.775  1.00 50.18 ? 194 ARG A NH2 1 
ATOM   1594 N  N   . GLY A 1 195 ? 21.429  0.752   -0.552  1.00 8.87  ? 195 GLY A N   1 
ATOM   1595 C  CA  . GLY A 1 195 ? 20.508  1.441   0.324   1.00 9.28  ? 195 GLY A CA  1 
ATOM   1596 C  C   . GLY A 1 195 ? 21.121  2.635   0.994   1.00 8.66  ? 195 GLY A C   1 
ATOM   1597 O  O   . GLY A 1 195 ? 21.947  3.381   0.432   1.00 9.26  ? 195 GLY A O   1 
ATOM   1598 N  N   . SER A 1 196 ? 20.677  2.849   2.230   1.00 7.93  ? 196 SER A N   1 
ATOM   1599 C  CA  . SER A 1 196 ? 20.948  4.094   2.919   1.00 7.61  ? 196 SER A CA  1 
ATOM   1600 C  C   . SER A 1 196 ? 21.414  3.831   4.353   1.00 7.61  ? 196 SER A C   1 
ATOM   1601 O  O   . SER A 1 196 ? 21.281  2.712   4.874   1.00 7.26  ? 196 SER A O   1 
ATOM   1602 C  CB  . SER A 1 196 ? 19.752  5.027   2.978   1.00 8.23  ? 196 SER A CB  1 
ATOM   1603 O  OG  . SER A 1 196 ? 18.790  4.575   3.951   1.00 7.77  ? 196 SER A OG  1 
ATOM   1604 N  N   . LEU A 1 197 ? 21.937  4.861   4.999   1.00 7.59  ? 197 LEU A N   1 
ATOM   1605 C  CA  . LEU A 1 197 ? 21.969  4.873   6.444   1.00 7.86  ? 197 LEU A CA  1 
ATOM   1606 C  C   . LEU A 1 197 ? 20.548  4.634   6.964   1.00 7.58  ? 197 LEU A C   1 
ATOM   1607 O  O   . LEU A 1 197 ? 19.595  5.219   6.434   1.00 8.30  ? 197 LEU A O   1 
ATOM   1608 C  CB  . LEU A 1 197 ? 22.484  6.211   7.008   1.00 10.71 ? 197 LEU A CB  1 
ATOM   1609 C  CG  . LEU A 1 197 ? 23.999  6.431   7.124   1.00 11.74 ? 197 LEU A CG  1 
ATOM   1610 C  CD1 . LEU A 1 197 ? 24.600  6.685   5.766   1.00 14.72 ? 197 LEU A CD1 1 
ATOM   1611 C  CD2 . LEU A 1 197 ? 24.244  7.633   8.021   1.00 13.92 ? 197 LEU A CD2 1 
ATOM   1612 N  N   . THR A 1 198 ? 20.423  3.878   8.054   1.00 7.13  ? 198 THR A N   1 
ATOM   1613 C  CA  . THR A 1 198 ? 19.106  3.686   8.655   1.00 7.57  ? 198 THR A CA  1 
ATOM   1614 C  C   . THR A 1 198 ? 18.857  4.703   9.771   1.00 7.85  ? 198 THR A C   1 
ATOM   1615 O  O   . THR A 1 198 ? 17.796  4.657   10.413  1.00 8.24  ? 198 THR A O   1 
ATOM   1616 C  CB  . THR A 1 198 ? 18.954  2.286   9.253   1.00 7.35  ? 198 THR A CB  1 
ATOM   1617 O  OG1 . THR A 1 198 ? 19.857  2.211   10.361  1.00 7.87  ? 198 THR A OG1 1 
ATOM   1618 C  CG2 . THR A 1 198 ? 19.203  1.170   8.270   1.00 8.04  ? 198 THR A CG2 1 
ATOM   1619 N  N   . THR A 1 199 ? 19.823  5.599   9.996   1.00 7.92  ? 199 THR A N   1 
ATOM   1620 C  CA  . THR A 1 199 ? 19.653  6.690   10.923  1.00 8.01  ? 199 THR A CA  1 
ATOM   1621 C  C   . THR A 1 199 ? 19.840  7.976   10.135  1.00 8.47  ? 199 THR A C   1 
ATOM   1622 O  O   . THR A 1 199 ? 20.513  7.960   9.111   1.00 8.99  ? 199 THR A O   1 
ATOM   1623 C  CB  . THR A 1 199 ? 20.695  6.690   12.051  1.00 8.15  ? 199 THR A CB  1 
ATOM   1624 O  OG1 . THR A 1 199 ? 22.003  6.896   11.518  1.00 9.70  ? 199 THR A OG1 1 
ATOM   1625 C  CG2 . THR A 1 199 ? 20.664  5.365   12.799  1.00 9.99  ? 199 THR A CG2 1 
ATOM   1626 N  N   . PRO A 1 200 ? 19.418  9.119   10.681  1.00 7.97  ? 200 PRO A N   1 
ATOM   1627 C  CA  . PRO A 1 200 ? 19.802  10.396  10.096  1.00 8.62  ? 200 PRO A CA  1 
ATOM   1628 C  C   . PRO A 1 200 ? 21.318  10.435  9.979   1.00 10.75 ? 200 PRO A C   1 
ATOM   1629 O  O   . PRO A 1 200 ? 22.021  9.905   10.850  1.00 11.27 ? 200 PRO A O   1 
ATOM   1630 C  CB  . PRO A 1 200 ? 19.341  11.392  11.164  1.00 9.17  ? 200 PRO A CB  1 
ATOM   1631 C  CG  . PRO A 1 200 ? 18.071  10.754  11.653  1.00 7.95  ? 200 PRO A CG  1 
ATOM   1632 C  CD  . PRO A 1 200 ? 18.484  9.281   11.793  1.00 8.02  ? 200 PRO A CD  1 
ATOM   1633 N  N   . PRO A 1 201 ? 21.867  11.037  8.916   1.00 9.81  ? 201 PRO A N   1 
ATOM   1634 C  CA  . PRO A 1 201 ? 21.111  11.756  7.874   1.00 10.38 ? 201 PRO A CA  1 
ATOM   1635 C  C   . PRO A 1 201 ? 20.491  10.952  6.740   1.00 9.20  ? 201 PRO A C   1 
ATOM   1636 O  O   . PRO A 1 201 ? 20.040  11.496  5.756   1.00 10.60 ? 201 PRO A O   1 
ATOM   1637 C  CB  . PRO A 1 201 ? 22.143  12.753  7.285   1.00 11.17 ? 201 PRO A CB  1 
ATOM   1638 C  CG  . PRO A 1 201 ? 23.328  12.687  8.191   1.00 13.73 ? 201 PRO A CG  1 
ATOM   1639 C  CD  . PRO A 1 201 ? 23.313  11.294  8.828   1.00 9.97  ? 201 PRO A CD  1 
ATOM   1640 N  N   . CYS A 1 202 ? 20.530  9.605   6.821   1.00 8.76  ? 202 CYS A N   1 
ATOM   1641 C  CA  . CYS A 1 202 ? 19.843  8.683   5.904   1.00 8.20  ? 202 CYS A CA  1 
ATOM   1642 C  C   . CYS A 1 202 ? 20.387  8.761   4.480   1.00 8.54  ? 202 CYS A C   1 
ATOM   1643 O  O   . CYS A 1 202 ? 19.691  8.512   3.527   1.00 9.33  ? 202 CYS A O   1 
ATOM   1644 C  CB  . CYS A 1 202 ? 18.332  8.990   5.824   1.00 9.21  ? 202 CYS A CB  1 
ATOM   1645 S  SG  . CYS A 1 202 ? 17.461  8.885   7.407   1.00 9.11  ? 202 CYS A SG  1 
ATOM   1646 N  N   . ASN A 1 203 ? 21.664  9.114   4.351   1.00 9.60  ? 203 ASN A N   1 
ATOM   1647 C  CA  . ASN A 1 203 ? 22.228  9.276   3.017   1.00 10.46 ? 203 ASN A CA  1 
ATOM   1648 C  C   . ASN A 1 203 ? 22.141  7.985   2.242   1.00 9.48  ? 203 ASN A C   1 
ATOM   1649 O  O   . ASN A 1 203 ? 22.428  6.895   2.801   1.00 9.16  ? 203 ASN A O   1 
ATOM   1650 C  CB  . ASN A 1 203 ? 23.732  9.638   3.082   1.00 13.33 ? 203 ASN A CB  1 
ATOM   1651 C  CG  . ASN A 1 203 ? 23.920  10.821  4.004   1.00 15.13 ? 203 ASN A CG  1 
ATOM   1652 O  OD1 . ASN A 1 203 ? 23.979  10.649  5.225   1.00 18.38 ? 203 ASN A OD1 1 
ATOM   1653 N  ND2 . ASN A 1 203 ? 23.899  12.031  3.457   1.00 21.41 ? 203 ASN A ND2 1 
ATOM   1654 N  N   . PRO A 1 204 ? 21.805  8.014   0.924   1.00 9.34  ? 204 PRO A N   1 
ATOM   1655 C  CA  . PRO A 1 204 ? 21.613  6.807   0.133   1.00 9.70  ? 204 PRO A CA  1 
ATOM   1656 C  C   . PRO A 1 204 ? 22.928  6.336   -0.453  1.00 9.96  ? 204 PRO A C   1 
ATOM   1657 O  O   . PRO A 1 204 ? 23.064  6.163   -1.674  1.00 12.35 ? 204 PRO A O   1 
ATOM   1658 C  CB  . PRO A 1 204 ? 20.650  7.242   -1.002  1.00 10.52 ? 204 PRO A CB  1 
ATOM   1659 C  CG  . PRO A 1 204 ? 21.053  8.719   -1.193  1.00 11.95 ? 204 PRO A CG  1 
ATOM   1660 C  CD  . PRO A 1 204 ? 21.327  9.252   0.211   1.00 9.93  ? 204 PRO A CD  1 
ATOM   1661 N  N   . THR A 1 205 ? 23.877  6.070   0.454   1.00 9.71  ? 205 THR A N   1 
ATOM   1662 C  CA  . THR A 1 205 ? 25.242  5.831   -0.006  1.00 10.33 ? 205 THR A CA  1 
ATOM   1663 C  C   . THR A 1 205 ? 25.821  4.534   0.570   1.00 9.98  ? 205 THR A C   1 
ATOM   1664 O  O   . THR A 1 205 ? 27.032  4.356   0.602   1.00 10.22 ? 205 THR A O   1 
ATOM   1665 C  CB  . THR A 1 205 ? 26.099  6.968   0.552   1.00 10.27 ? 205 THR A CB  1 
ATOM   1666 O  OG1 . THR A 1 205 ? 25.910  7.035   1.960   1.00 11.24 ? 205 THR A OG1 1 
ATOM   1667 C  CG2 . THR A 1 205 ? 25.806  8.333   -0.086  1.00 12.71 ? 205 THR A CG2 1 
ATOM   1668 N  N   . VAL A 1 206 ? 24.956  3.604   0.984   1.00 9.35  ? 206 VAL A N   1 
ATOM   1669 C  CA  . VAL A 1 206 ? 25.411  2.377   1.650   1.00 9.06  ? 206 VAL A CA  1 
ATOM   1670 C  C   . VAL A 1 206 ? 25.217  1.173   0.776   1.00 9.62  ? 206 VAL A C   1 
ATOM   1671 O  O   . VAL A 1 206 ? 24.094  0.882   0.341   1.00 9.81  ? 206 VAL A O   1 
ATOM   1672 C  CB  . VAL A 1 206 ? 24.644  2.142   2.975   1.00 8.17  ? 206 VAL A CB  1 
ATOM   1673 C  CG1 . VAL A 1 206 ? 25.103  0.797   3.541   1.00 8.08  ? 206 VAL A CG1 1 
ATOM   1674 C  CG2 . VAL A 1 206 ? 24.894  3.277   3.971   1.00 8.82  ? 206 VAL A CG2 1 
ATOM   1675 N  N   . LEU A 1 207 ? 26.276  0.421   0.586   1.00 8.64  ? 207 LEU A N   1 
ATOM   1676 C  CA  . LEU A 1 207 ? 26.195  -0.905  0.008   1.00 8.68  ? 207 LEU A CA  1 
ATOM   1677 C  C   . LEU A 1 207 ? 25.984  -1.890  1.158   1.00 9.01  ? 207 LEU A C   1 
ATOM   1678 O  O   . LEU A 1 207 ? 26.852  -2.060  2.029   1.00 9.29  ? 207 LEU A O   1 
ATOM   1679 C  CB  . LEU A 1 207 ? 27.460  -1.243  -0.783  1.00 11.15 ? 207 LEU A CB  1 
ATOM   1680 C  CG  . LEU A 1 207 ? 27.326  -2.559  -1.541  1.00 12.47 ? 207 LEU A CG  1 
ATOM   1681 C  CD1 . LEU A 1 207 ? 26.351  -2.399  -2.725  1.00 15.61 ? 207 LEU A CD1 1 
ATOM   1682 C  CD2 . LEU A 1 207 ? 28.683  -3.015  -2.034  1.00 18.76 ? 207 LEU A CD2 1 
ATOM   1683 N  N   . TRP A 1 208 ? 24.787  -2.480  1.213   1.00 8.04  ? 208 TRP A N   1 
ATOM   1684 C  CA  . TRP A 1 208 ? 24.407  -3.377  2.311   1.00 7.62  ? 208 TRP A CA  1 
ATOM   1685 C  C   . TRP A 1 208 ? 24.782  -4.807  2.008   1.00 7.96  ? 208 TRP A C   1 
ATOM   1686 O  O   . TRP A 1 208 ? 24.517  -5.310  0.908   1.00 8.64  ? 208 TRP A O   1 
ATOM   1687 C  CB  . TRP A 1 208 ? 22.873  -3.328  2.570   1.00 8.03  ? 208 TRP A CB  1 
ATOM   1688 C  CG  . TRP A 1 208 ? 22.519  -2.132  3.380   1.00 7.88  ? 208 TRP A CG  1 
ATOM   1689 C  CD1 . TRP A 1 208 ? 22.067  -0.910  2.930   1.00 7.87  ? 208 TRP A CD1 1 
ATOM   1690 C  CD2 . TRP A 1 208 ? 22.634  -1.968  4.806   1.00 7.26  ? 208 TRP A CD2 1 
ATOM   1691 N  NE1 . TRP A 1 208 ? 21.916  -0.016  3.956   1.00 8.02  ? 208 TRP A NE1 1 
ATOM   1692 C  CE2 . TRP A 1 208 ? 22.243  -0.650  5.138   1.00 7.39  ? 208 TRP A CE2 1 
ATOM   1693 C  CE3 . TRP A 1 208 ? 23.029  -2.826  5.839   1.00 7.87  ? 208 TRP A CE3 1 
ATOM   1694 C  CZ2 . TRP A 1 208 ? 22.241  -0.163  6.441   1.00 8.00  ? 208 TRP A CZ2 1 
ATOM   1695 C  CZ3 . TRP A 1 208 ? 23.017  -2.351  7.126   1.00 8.22  ? 208 TRP A CZ3 1 
ATOM   1696 C  CH2 . TRP A 1 208 ? 22.670  -1.027  7.419   1.00 7.82  ? 208 TRP A CH2 1 
ATOM   1697 N  N   . THR A 1 209 ? 25.383  -5.477  3.015   1.00 7.11  ? 209 THR A N   1 
ATOM   1698 C  CA  . THR A 1 209 ? 25.578  -6.912  3.003   1.00 8.45  ? 209 THR A CA  1 
ATOM   1699 C  C   . THR A 1 209 ? 24.912  -7.434  4.272   1.00 8.15  ? 209 THR A C   1 
ATOM   1700 O  O   . THR A 1 209 ? 25.430  -7.128  5.345   1.00 9.03  ? 209 THR A O   1 
ATOM   1701 C  CB  . THR A 1 209 ? 27.067  -7.293  2.955   1.00 8.81  ? 209 THR A CB  1 
ATOM   1702 O  OG1 . THR A 1 209 ? 27.615  -6.750  1.744   1.00 9.55  ? 209 THR A OG1 1 
ATOM   1703 C  CG2 . THR A 1 209 ? 27.304  -8.800  2.926   1.00 9.48  ? 209 THR A CG2 1 
ATOM   1704 N  N   . VAL A 1 210 ? 23.841  -8.231  4.095   1.00 7.95  ? 210 VAL A N   1 
ATOM   1705 C  CA  . VAL A 1 210 ? 23.203  -8.792  5.274   1.00 7.91  ? 210 VAL A CA  1 
ATOM   1706 C  C   . VAL A 1 210 ? 23.442  -10.292 5.226   1.00 7.97  ? 210 VAL A C   1 
ATOM   1707 O  O   . VAL A 1 210 ? 23.029  -10.952 4.288   1.00 8.42  ? 210 VAL A O   1 
ATOM   1708 C  CB  . VAL A 1 210 ? 21.686  -8.483  5.287   1.00 7.62  ? 210 VAL A CB  1 
ATOM   1709 C  CG1 . VAL A 1 210 ? 21.078  -9.075  6.554   1.00 8.62  ? 210 VAL A CG1 1 
ATOM   1710 C  CG2 . VAL A 1 210 ? 21.390  -7.006  5.143   1.00 8.62  ? 210 VAL A CG2 1 
ATOM   1711 N  N   . PHE A 1 211 ? 24.162  -10.821 6.230   1.00 8.09  ? 211 PHE A N   1 
ATOM   1712 C  CA  . PHE A 1 211 ? 24.413  -12.260 6.195   1.00 8.82  ? 211 PHE A CA  1 
ATOM   1713 C  C   . PHE A 1 211 ? 23.133  -13.068 6.319   1.00 9.02  ? 211 PHE A C   1 
ATOM   1714 O  O   . PHE A 1 211 ? 22.220  -12.713 7.064   1.00 9.82  ? 211 PHE A O   1 
ATOM   1715 C  CB  . PHE A 1 211 ? 25.448  -12.625 7.261   1.00 8.90  ? 211 PHE A CB  1 
ATOM   1716 C  CG  . PHE A 1 211 ? 26.789  -11.974 7.009   1.00 8.25  ? 211 PHE A CG  1 
ATOM   1717 C  CD1 . PHE A 1 211 ? 27.562  -12.388 5.923   1.00 9.43  ? 211 PHE A CD1 1 
ATOM   1718 C  CD2 . PHE A 1 211 ? 27.257  -10.915 7.794   1.00 9.50  ? 211 PHE A CD2 1 
ATOM   1719 C  CE1 . PHE A 1 211 ? 28.772  -11.762 5.627   1.00 12.22 ? 211 PHE A CE1 1 
ATOM   1720 C  CE2 . PHE A 1 211 ? 28.492  -10.333 7.515   1.00 10.61 ? 211 PHE A CE2 1 
ATOM   1721 C  CZ  . PHE A 1 211 ? 29.218  -10.721 6.426   1.00 10.81 ? 211 PHE A CZ  1 
ATOM   1722 N  N   A ARG A 1 212 ? 23.092  -14.189 5.593   0.50 9.48  ? 212 ARG A N   1 
ATOM   1723 N  N   B ARG A 1 212 ? 23.073  -14.194 5.593   0.50 9.47  ? 212 ARG A N   1 
ATOM   1724 C  CA  A ARG A 1 212 ? 21.904  -15.021 5.575   0.50 10.12 ? 212 ARG A CA  1 
ATOM   1725 C  CA  B ARG A 1 212 ? 21.867  -15.008 5.590   0.50 10.11 ? 212 ARG A CA  1 
ATOM   1726 C  C   A ARG A 1 212 ? 21.632  -15.638 6.948   0.50 10.16 ? 212 ARG A C   1 
ATOM   1727 C  C   B ARG A 1 212 ? 21.622  -15.634 6.964   0.50 10.18 ? 212 ARG A C   1 
ATOM   1728 O  O   A ARG A 1 212 ? 20.467  -15.703 7.363   0.50 11.49 ? 212 ARG A O   1 
ATOM   1729 O  O   B ARG A 1 212 ? 20.467  -15.688 7.405   0.50 11.51 ? 212 ARG A O   1 
ATOM   1730 C  CB  A ARG A 1 212 ? 22.087  -16.159 4.578   0.50 10.88 ? 212 ARG A CB  1 
ATOM   1731 C  CB  B ARG A 1 212 ? 21.940  -16.118 4.540   0.50 10.85 ? 212 ARG A CB  1 
ATOM   1732 C  CG  A ARG A 1 212 ? 20.926  -17.136 4.586   0.50 12.73 ? 212 ARG A CG  1 
ATOM   1733 C  CG  B ARG A 1 212 ? 20.600  -16.780 4.252   0.50 12.37 ? 212 ARG A CG  1 
ATOM   1734 C  CD  A ARG A 1 212 ? 21.323  -18.364 3.791   0.50 14.42 ? 212 ARG A CD  1 
ATOM   1735 C  CD  B ARG A 1 212 ? 20.890  -18.078 3.523   0.50 14.58 ? 212 ARG A CD  1 
ATOM   1736 N  NE  A ARG A 1 212 ? 20.194  -19.277 3.612   0.50 14.91 ? 212 ARG A NE  1 
ATOM   1737 N  NE  B ARG A 1 212 ? 19.644  -18.674 3.048   0.50 17.11 ? 212 ARG A NE  1 
ATOM   1738 C  CZ  A ARG A 1 212 ? 19.882  -20.312 4.401   0.50 17.61 ? 212 ARG A CZ  1 
ATOM   1739 C  CZ  B ARG A 1 212 ? 19.574  -19.736 2.236   0.50 18.89 ? 212 ARG A CZ  1 
ATOM   1740 N  NH1 A ARG A 1 212 ? 20.607  -20.596 5.468   0.50 16.99 ? 212 ARG A NH1 1 
ATOM   1741 N  NH1 B ARG A 1 212 ? 20.686  -20.318 1.832   0.50 20.22 ? 212 ARG A NH1 1 
ATOM   1742 N  NH2 A ARG A 1 212 ? 18.828  -21.055 4.119   0.50 19.04 ? 212 ARG A NH2 1 
ATOM   1743 N  NH2 B ARG A 1 212 ? 18.391  -20.190 1.846   0.50 21.05 ? 212 ARG A NH2 1 
ATOM   1744 N  N   . ASN A 1 213 ? 22.697  -16.060 7.645   1.00 9.63  ? 213 ASN A N   1 
ATOM   1745 C  CA  . ASN A 1 213 ? 22.514  -16.838 8.874   1.00 10.50 ? 213 ASN A CA  1 
ATOM   1746 C  C   . ASN A 1 213 ? 22.628  -15.907 10.078  1.00 10.89 ? 213 ASN A C   1 
ATOM   1747 O  O   . ASN A 1 213 ? 23.562  -15.101 10.133  1.00 11.09 ? 213 ASN A O   1 
ATOM   1748 C  CB  . ASN A 1 213 ? 23.577  -17.957 8.910   1.00 12.98 ? 213 ASN A CB  1 
ATOM   1749 C  CG  . ASN A 1 213 ? 23.473  -18.877 7.713   1.00 14.44 ? 213 ASN A CG  1 
ATOM   1750 O  OD1 . ASN A 1 213 ? 24.450  -19.100 7.002   1.00 18.37 ? 213 ASN A OD1 1 
ATOM   1751 N  ND2 . ASN A 1 213 ? 22.279  -19.265 7.396   1.00 15.71 ? 213 ASN A ND2 1 
ATOM   1752 N  N   . PRO A 1 214 ? 21.770  -16.067 11.109  1.00 10.96 ? 214 PRO A N   1 
ATOM   1753 C  CA  . PRO A 1 214 ? 21.912  -15.271 12.304  1.00 11.74 ? 214 PRO A CA  1 
ATOM   1754 C  C   . PRO A 1 214 ? 22.980  -15.852 13.240  1.00 11.58 ? 214 PRO A C   1 
ATOM   1755 O  O   . PRO A 1 214 ? 23.390  -17.016 13.100  1.00 13.12 ? 214 PRO A O   1 
ATOM   1756 C  CB  . PRO A 1 214 ? 20.537  -15.412 12.958  1.00 13.07 ? 214 PRO A CB  1 
ATOM   1757 C  CG  . PRO A 1 214 ? 20.106  -16.846 12.581  1.00 15.03 ? 214 PRO A CG  1 
ATOM   1758 C  CD  . PRO A 1 214 ? 20.605  -16.974 11.152  1.00 13.78 ? 214 PRO A CD  1 
ATOM   1759 N  N   . VAL A 1 215 ? 23.390  -15.039 14.207  1.00 10.47 ? 215 VAL A N   1 
ATOM   1760 C  CA  . VAL A 1 215 ? 24.136  -15.519 15.370  1.00 10.98 ? 215 VAL A CA  1 
ATOM   1761 C  C   . VAL A 1 215 ? 23.174  -15.639 16.542  1.00 11.47 ? 215 VAL A C   1 
ATOM   1762 O  O   . VAL A 1 215 ? 22.072  -15.096 16.535  1.00 11.60 ? 215 VAL A O   1 
ATOM   1763 C  CB  . VAL A 1 215 ? 25.297  -14.600 15.758  1.00 11.50 ? 215 VAL A CB  1 
ATOM   1764 C  CG1 . VAL A 1 215 ? 26.321  -14.474 14.640  1.00 12.64 ? 215 VAL A CG1 1 
ATOM   1765 C  CG2 . VAL A 1 215 ? 24.854  -13.229 16.168  1.00 11.84 ? 215 VAL A CG2 1 
ATOM   1766 N  N   A GLN A 1 216 ? 23.697  -16.275 17.600  0.50 11.60 ? 216 GLN A N   1 
ATOM   1767 N  N   B GLN A 1 216 ? 23.503  -16.468 17.528  0.50 11.45 ? 216 GLN A N   1 
ATOM   1768 C  CA  A GLN A 1 216 ? 22.967  -16.469 18.844  0.50 12.03 ? 216 GLN A CA  1 
ATOM   1769 C  CA  B GLN A 1 216 ? 22.699  -16.596 18.745  0.50 12.04 ? 216 GLN A CA  1 
ATOM   1770 C  C   A GLN A 1 216 ? 23.637  -15.725 19.985  0.50 11.57 ? 216 GLN A C   1 
ATOM   1771 C  C   B GLN A 1 216 ? 23.450  -15.988 19.935  0.50 11.91 ? 216 GLN A C   1 
ATOM   1772 O  O   A GLN A 1 216 ? 24.858  -15.645 20.137  0.50 10.36 ? 216 GLN A O   1 
ATOM   1773 O  O   B GLN A 1 216 ? 24.641  -16.246 20.042  0.50 10.75 ? 216 GLN A O   1 
ATOM   1774 C  CB  A GLN A 1 216 ? 22.759  -17.952 19.199  0.50 13.15 ? 216 GLN A CB  1 
ATOM   1775 C  CB  B GLN A 1 216 ? 22.496  -18.096 19.018  0.50 12.92 ? 216 GLN A CB  1 
ATOM   1776 C  CG  A GLN A 1 216 ? 21.729  -18.611 18.288  0.50 14.60 ? 216 GLN A CG  1 
ATOM   1777 C  CG  B GLN A 1 216 ? 21.831  -18.851 17.864  0.50 14.46 ? 216 GLN A CG  1 
ATOM   1778 C  CD  A GLN A 1 216 ? 21.386  -20.049 18.575  0.50 16.48 ? 216 GLN A CD  1 
ATOM   1779 C  CD  B GLN A 1 216 ? 22.713  -19.143 16.669  0.50 15.69 ? 216 GLN A CD  1 
ATOM   1780 O  OE1 A GLN A 1 216 ? 21.840  -20.624 19.562  0.50 17.06 ? 216 GLN A OE1 1 
ATOM   1781 O  OE1 B GLN A 1 216 ? 23.884  -19.449 16.805  0.50 17.82 ? 216 GLN A OE1 1 
ATOM   1782 N  NE2 A GLN A 1 216 ? 20.502  -20.587 17.742  0.50 18.88 ? 216 GLN A NE2 1 
ATOM   1783 N  NE2 B GLN A 1 216 ? 22.163  -19.094 15.453  0.50 15.61 ? 216 GLN A NE2 1 
ATOM   1784 N  N   . ILE A 1 217 ? 22.763  -15.238 20.848  1.00 11.82 ? 217 ILE A N   1 
ATOM   1785 C  CA  . ILE A 1 217 ? 23.218  -14.773 22.156  1.00 12.49 ? 217 ILE A CA  1 
ATOM   1786 C  C   . ILE A 1 217 ? 22.201  -15.286 23.191  1.00 12.46 ? 217 ILE A C   1 
ATOM   1787 O  O   . ILE A 1 217 ? 21.069  -15.618 22.843  1.00 12.38 ? 217 ILE A O   1 
ATOM   1788 C  CB  . ILE A 1 217 ? 23.376  -13.233 22.217  1.00 11.23 ? 217 ILE A CB  1 
ATOM   1789 C  CG1 . ILE A 1 217 ? 22.034  -12.484 22.077  1.00 11.96 ? 217 ILE A CG1 1 
ATOM   1790 C  CG2 . ILE A 1 217 ? 24.371  -12.760 21.155  1.00 12.43 ? 217 ILE A CG2 1 
ATOM   1791 C  CD1 . ILE A 1 217 ? 22.118  -10.983 22.231  1.00 11.99 ? 217 ILE A CD1 1 
ATOM   1792 N  N   . SER A 1 218 ? 22.628  -15.353 24.458  1.00 12.38 ? 218 SER A N   1 
ATOM   1793 C  CA  . SER A 1 218 ? 21.701  -15.933 25.418  1.00 13.03 ? 218 SER A CA  1 
ATOM   1794 C  C   . SER A 1 218 ? 20.567  -14.975 25.748  1.00 13.76 ? 218 SER A C   1 
ATOM   1795 O  O   . SER A 1 218 ? 20.632  -13.751 25.567  1.00 12.20 ? 218 SER A O   1 
ATOM   1796 C  CB  . SER A 1 218 ? 22.432  -16.315 26.674  1.00 13.65 ? 218 SER A CB  1 
ATOM   1797 O  OG  . SER A 1 218 ? 22.848  -15.167 27.399  1.00 14.02 ? 218 SER A OG  1 
ATOM   1798 N  N   . GLN A 1 219 ? 19.543  -15.549 26.395  1.00 15.67 ? 219 GLN A N   1 
ATOM   1799 C  CA  . GLN A 1 219 ? 18.482  -14.737 26.982  1.00 16.29 ? 219 GLN A CA  1 
ATOM   1800 C  C   . GLN A 1 219 ? 19.005  -13.626 27.896  1.00 14.73 ? 219 GLN A C   1 
ATOM   1801 O  O   . GLN A 1 219 ? 18.538  -12.502 27.799  1.00 14.47 ? 219 GLN A O   1 
ATOM   1802 C  CB  . GLN A 1 219 ? 17.565  -15.728 27.718  1.00 21.68 ? 219 GLN A CB  1 
ATOM   1803 C  CG  . GLN A 1 219 ? 16.542  -15.087 28.643  1.00 30.83 ? 219 GLN A CG  1 
ATOM   1804 C  CD  . GLN A 1 219 ? 16.008  -16.124 29.600  1.00 39.73 ? 219 GLN A CD  1 
ATOM   1805 O  OE1 . GLN A 1 219 ? 15.671  -17.245 29.209  1.00 44.59 ? 219 GLN A OE1 1 
ATOM   1806 N  NE2 . GLN A 1 219 ? 15.956  -15.760 30.872  1.00 43.55 ? 219 GLN A NE2 1 
ATOM   1807 N  N   . GLU A 1 220 ? 19.978  -13.905 28.727  1.00 12.69 ? 220 GLU A N   1 
ATOM   1808 C  CA  . GLU A 1 220 ? 20.543  -12.936 29.628  1.00 14.16 ? 220 GLU A CA  1 
ATOM   1809 C  C   . GLU A 1 220 ? 21.319  -11.855 28.876  1.00 12.92 ? 220 GLU A C   1 
ATOM   1810 O  O   . GLU A 1 220 ? 21.227  -10.691 29.249  1.00 12.35 ? 220 GLU A O   1 
ATOM   1811 C  CB  . GLU A 1 220 ? 21.386  -13.577 30.737  1.00 15.51 ? 220 GLU A CB  1 
ATOM   1812 C  CG  . GLU A 1 220 ? 20.592  -14.585 31.604  1.00 19.17 ? 220 GLU A CG  1 
ATOM   1813 C  CD  . GLU A 1 220 ? 20.269  -15.971 31.020  1.00 26.20 ? 220 GLU A CD  1 
ATOM   1814 O  OE1 . GLU A 1 220 ? 20.816  -16.397 29.919  1.00 24.26 ? 220 GLU A OE1 1 
ATOM   1815 O  OE2 . GLU A 1 220 ? 19.387  -16.653 31.633  1.00 31.23 ? 220 GLU A OE2 1 
ATOM   1816 N  N   . GLN A 1 221 ? 22.060  -12.266 27.821  1.00 13.47 ? 221 GLN A N   1 
ATOM   1817 C  CA  . GLN A 1 221 ? 22.799  -11.273 27.060  1.00 11.62 ? 221 GLN A CA  1 
ATOM   1818 C  C   . GLN A 1 221 ? 21.825  -10.314 26.365  1.00 12.47 ? 221 GLN A C   1 
ATOM   1819 O  O   . GLN A 1 221 ? 22.067  -9.117  26.354  1.00 11.20 ? 221 GLN A O   1 
ATOM   1820 C  CB  . GLN A 1 221 ? 23.675  -11.955 26.011  1.00 12.15 ? 221 GLN A CB  1 
ATOM   1821 C  CG  . GLN A 1 221 ? 24.871  -12.685 26.636  1.00 12.65 ? 221 GLN A CG  1 
ATOM   1822 C  CD  . GLN A 1 221 ? 25.706  -13.371 25.582  1.00 11.75 ? 221 GLN A CD  1 
ATOM   1823 O  OE1 . GLN A 1 221 ? 25.293  -14.278 24.905  1.00 12.75 ? 221 GLN A OE1 1 
ATOM   1824 N  NE2 . GLN A 1 221 ? 26.945  -12.903 25.479  1.00 13.54 ? 221 GLN A NE2 1 
ATOM   1825 N  N   . LEU A 1 222 ? 20.755  -10.855 25.790  1.00 10.36 ? 222 LEU A N   1 
ATOM   1826 C  CA  . LEU A 1 222 ? 19.810  -10.013 25.053  1.00 11.33 ? 222 LEU A CA  1 
ATOM   1827 C  C   . LEU A 1 222 ? 19.130  -9.059  26.025  1.00 11.98 ? 222 LEU A C   1 
ATOM   1828 O  O   . LEU A 1 222 ? 18.961  -7.888  25.744  1.00 11.36 ? 222 LEU A O   1 
ATOM   1829 C  CB  . LEU A 1 222 ? 18.798  -10.894 24.331  1.00 11.34 ? 222 LEU A CB  1 
ATOM   1830 C  CG  . LEU A 1 222 ? 17.657  -10.136 23.645  1.00 11.71 ? 222 LEU A CG  1 
ATOM   1831 C  CD1 . LEU A 1 222 ? 18.213  -9.213  22.533  1.00 12.47 ? 222 LEU A CD1 1 
ATOM   1832 C  CD2 . LEU A 1 222 ? 16.649  -11.112 23.043  1.00 14.07 ? 222 LEU A CD2 1 
ATOM   1833 N  N   . LEU A 1 223 ? 18.795  -9.578  27.240  1.00 12.04 ? 223 LEU A N   1 
ATOM   1834 C  CA  . LEU A 1 223 ? 18.144  -8.732  28.218  1.00 12.94 ? 223 LEU A CA  1 
ATOM   1835 C  C   . LEU A 1 223 ? 19.100  -7.638  28.662  1.00 12.08 ? 223 LEU A C   1 
ATOM   1836 O  O   . LEU A 1 223 ? 18.659  -6.508  28.860  1.00 13.22 ? 223 LEU A O   1 
ATOM   1837 C  CB  . LEU A 1 223 ? 17.781  -9.585  29.442  1.00 14.84 ? 223 LEU A CB  1 
ATOM   1838 C  CG  . LEU A 1 223 ? 16.961  -8.845  30.477  1.00 16.94 ? 223 LEU A CG  1 
ATOM   1839 C  CD1 . LEU A 1 223 ? 15.589  -8.441  29.885  1.00 17.37 ? 223 LEU A CD1 1 
ATOM   1840 C  CD2 . LEU A 1 223 ? 16.789  -9.787  31.658  1.00 18.65 ? 223 LEU A CD2 1 
ATOM   1841 N  N   . ALA A 1 224 ? 20.405  -7.951  28.809  1.00 12.27 ? 224 ALA A N   1 
ATOM   1842 C  CA  . ALA A 1 224 ? 21.386  -6.946  29.178  1.00 13.16 ? 224 ALA A CA  1 
ATOM   1843 C  C   . ALA A 1 224 ? 21.434  -5.803  28.163  1.00 13.96 ? 224 ALA A C   1 
ATOM   1844 O  O   . ALA A 1 224 ? 21.419  -4.630  28.504  1.00 14.04 ? 224 ALA A O   1 
ATOM   1845 C  CB  . ALA A 1 224 ? 22.767  -7.536  29.414  1.00 14.71 ? 224 ALA A CB  1 
ATOM   1846 N  N   . LEU A 1 225 ? 21.567  -6.186  26.883  1.00 11.89 ? 225 LEU A N   1 
ATOM   1847 C  CA  . LEU A 1 225 ? 21.563  -5.193  25.803  1.00 12.39 ? 225 LEU A CA  1 
ATOM   1848 C  C   . LEU A 1 225 ? 20.315  -4.319  25.868  1.00 12.57 ? 225 LEU A C   1 
ATOM   1849 O  O   . LEU A 1 225 ? 20.408  -3.106  25.685  1.00 14.63 ? 225 LEU A O   1 
ATOM   1850 C  CB  . LEU A 1 225 ? 21.623  -5.933  24.472  1.00 11.90 ? 225 LEU A CB  1 
ATOM   1851 C  CG  . LEU A 1 225 ? 21.726  -4.982  23.285  1.00 12.39 ? 225 LEU A CG  1 
ATOM   1852 C  CD1 . LEU A 1 225 ? 23.006  -4.142  23.323  1.00 13.86 ? 225 LEU A CD1 1 
ATOM   1853 C  CD2 . LEU A 1 225 ? 21.727  -5.804  22.022  1.00 12.37 ? 225 LEU A CD2 1 
ATOM   1854 N  N   . GLU A 1 226 ? 19.153  -4.962  26.110  1.00 11.36 ? 226 GLU A N   1 
ATOM   1855 C  CA  . GLU A 1 226 ? 17.892  -4.223  26.130  1.00 12.30 ? 226 GLU A CA  1 
ATOM   1856 C  C   . GLU A 1 226 ? 17.670  -3.319  27.343  1.00 13.93 ? 226 GLU A C   1 
ATOM   1857 O  O   . GLU A 1 226 ? 16.821  -2.423  27.305  1.00 15.36 ? 226 GLU A O   1 
ATOM   1858 C  CB  . GLU A 1 226 ? 16.712  -5.177  26.056  1.00 12.22 ? 226 GLU A CB  1 
ATOM   1859 C  CG  . GLU A 1 226 ? 16.630  -5.962  24.751  1.00 11.40 ? 226 GLU A CG  1 
ATOM   1860 C  CD  . GLU A 1 226 ? 15.699  -7.159  24.799  1.00 12.38 ? 226 GLU A CD  1 
ATOM   1861 O  OE1 . GLU A 1 226 ? 15.433  -7.638  25.951  1.00 13.74 ? 226 GLU A OE1 1 
ATOM   1862 O  OE2 . GLU A 1 226 ? 15.269  -7.630  23.767  1.00 13.56 ? 226 GLU A OE2 1 
ATOM   1863 N  N   . THR A 1 227 ? 18.399  -3.574  28.435  1.00 13.78 ? 227 THR A N   1 
ATOM   1864 C  CA  . THR A 1 227 ? 18.066  -2.924  29.702  1.00 14.54 ? 227 THR A CA  1 
ATOM   1865 C  C   . THR A 1 227 ? 19.240  -2.131  30.259  1.00 16.39 ? 227 THR A C   1 
ATOM   1866 O  O   . THR A 1 227 ? 19.053  -1.468  31.284  1.00 18.03 ? 227 THR A O   1 
ATOM   1867 C  CB  . THR A 1 227 ? 17.606  -3.930  30.769  1.00 15.15 ? 227 THR A CB  1 
ATOM   1868 O  OG1 . THR A 1 227 ? 18.659  -4.848  31.053  1.00 16.26 ? 227 THR A OG1 1 
ATOM   1869 C  CG2 . THR A 1 227 ? 16.316  -4.618  30.368  1.00 16.47 ? 227 THR A CG2 1 
ATOM   1870 N  N   . ALA A 1 228 ? 20.448  -2.220  29.675  1.00 14.59 ? 228 ALA A N   1 
ATOM   1871 C  CA  . ALA A 1 228 ? 21.645  -1.653  30.297  1.00 15.95 ? 228 ALA A CA  1 
ATOM   1872 C  C   . ALA A 1 228 ? 21.788  -0.151  30.054  1.00 16.38 ? 228 ALA A C   1 
ATOM   1873 O  O   . ALA A 1 228 ? 22.472  0.525   30.842  1.00 17.54 ? 228 ALA A O   1 
ATOM   1874 C  CB  . ALA A 1 228 ? 22.890  -2.469  29.938  1.00 18.32 ? 228 ALA A CB  1 
ATOM   1875 N  N   . LEU A 1 229 ? 21.159  0.393   28.987  1.00 14.08 ? 229 LEU A N   1 
ATOM   1876 C  CA  . LEU A 1 229 ? 21.521  1.712   28.485  1.00 15.51 ? 229 LEU A CA  1 
ATOM   1877 C  C   . LEU A 1 229 ? 20.347  2.653   28.534  1.00 14.75 ? 229 LEU A C   1 
ATOM   1878 O  O   . LEU A 1 229 ? 19.181  2.279   28.398  1.00 13.66 ? 229 LEU A O   1 
ATOM   1879 C  CB  . LEU A 1 229 ? 22.073  1.649   27.059  1.00 15.11 ? 229 LEU A CB  1 
ATOM   1880 C  CG  . LEU A 1 229 ? 23.138  0.579   26.798  1.00 16.13 ? 229 LEU A CG  1 
ATOM   1881 C  CD1 . LEU A 1 229 ? 23.574  0.707   25.339  1.00 18.91 ? 229 LEU A CD1 1 
ATOM   1882 C  CD2 . LEU A 1 229 ? 24.351  0.782   27.712  1.00 17.11 ? 229 LEU A CD2 1 
ATOM   1883 N  N   . TYR A 1 230 ? 20.692  3.916   28.718  1.00 15.79 ? 230 TYR A N   1 
ATOM   1884 C  CA  . TYR A 1 230 ? 19.769  5.037   28.630  1.00 16.54 ? 230 TYR A CA  1 
ATOM   1885 C  C   . TYR A 1 230 ? 20.160  5.977   27.494  1.00 15.96 ? 230 TYR A C   1 
ATOM   1886 O  O   . TYR A 1 230 ? 21.334  6.119   27.151  1.00 17.48 ? 230 TYR A O   1 
ATOM   1887 C  CB  . TYR A 1 230 ? 19.837  5.826   29.948  1.00 18.71 ? 230 TYR A CB  1 
ATOM   1888 C  CG  . TYR A 1 230 ? 19.272  5.136   31.170  1.00 25.20 ? 230 TYR A CG  1 
ATOM   1889 C  CD1 . TYR A 1 230 ? 20.012  4.199   31.879  1.00 27.32 ? 230 TYR A CD1 1 
ATOM   1890 C  CD2 . TYR A 1 230 ? 18.016  5.463   31.649  1.00 28.75 ? 230 TYR A CD2 1 
ATOM   1891 C  CE1 . TYR A 1 230 ? 19.508  3.587   33.023  1.00 36.32 ? 230 TYR A CE1 1 
ATOM   1892 C  CE2 . TYR A 1 230 ? 17.484  4.854   32.782  1.00 31.76 ? 230 TYR A CE2 1 
ATOM   1893 C  CZ  . TYR A 1 230 ? 18.239  3.922   33.477  1.00 35.56 ? 230 TYR A CZ  1 
ATOM   1894 O  OH  . TYR A 1 230 ? 17.701  3.346   34.601  1.00 42.70 ? 230 TYR A OH  1 
ATOM   1895 N  N   . CYS A 1 231 ? 19.183  6.648   26.900  1.00 18.04 ? 231 CYS A N   1 
ATOM   1896 C  CA  . CYS A 1 231 ? 19.548  7.534   25.821  1.00 18.30 ? 231 CYS A CA  1 
ATOM   1897 C  C   . CYS A 1 231 ? 19.742  8.953   26.336  1.00 18.16 ? 231 CYS A C   1 
ATOM   1898 O  O   . CYS A 1 231 ? 20.185  9.822   25.592  1.00 18.74 ? 231 CYS A O   1 
ATOM   1899 C  CB  . CYS A 1 231 ? 18.609  7.390   24.647  1.00 24.09 ? 231 CYS A CB  1 
ATOM   1900 S  SG  . CYS A 1 231 ? 16.879  7.670   25.045  1.00 30.14 ? 231 CYS A SG  1 
ATOM   1901 N  N   . THR A 1 232 ? 19.570  9.107   27.668  1.00 17.09 ? 232 THR A N   1 
ATOM   1902 C  CA  . THR A 1 232 ? 19.740  10.402  28.316  1.00 17.82 ? 232 THR A CA  1 
ATOM   1903 C  C   . THR A 1 232 ? 21.073  10.493  29.060  1.00 15.97 ? 232 THR A C   1 
ATOM   1904 O  O   . THR A 1 232 ? 21.684  9.486   29.423  1.00 16.81 ? 232 THR A O   1 
ATOM   1905 C  CB  . THR A 1 232 ? 18.553  10.620  29.267  1.00 17.77 ? 232 THR A CB  1 
ATOM   1906 O  OG1 . THR A 1 232 ? 18.308  9.408   29.981  1.00 18.45 ? 232 THR A OG1 1 
ATOM   1907 C  CG2 . THR A 1 232 ? 17.311  11.046  28.524  1.00 20.43 ? 232 THR A CG2 1 
ATOM   1908 N  N   . HIS A 1 233 ? 21.531  11.742  29.301  1.00 17.82 ? 233 HIS A N   1 
ATOM   1909 C  CA  . HIS A 1 233 ? 22.705  11.976  30.130  1.00 18.99 ? 233 HIS A CA  1 
ATOM   1910 C  C   . HIS A 1 233 ? 22.412  11.579  31.581  1.00 17.97 ? 233 HIS A C   1 
ATOM   1911 O  O   . HIS A 1 233 ? 21.257  11.588  32.018  1.00 19.05 ? 233 HIS A O   1 
ATOM   1912 C  CB  . HIS A 1 233 ? 23.153  13.450  30.086  1.00 20.19 ? 233 HIS A CB  1 
ATOM   1913 C  CG  . HIS A 1 233 ? 23.694  13.837  28.748  1.00 23.03 ? 233 HIS A CG  1 
ATOM   1914 N  ND1 . HIS A 1 233 ? 22.945  14.581  27.840  1.00 31.10 ? 233 HIS A ND1 1 
ATOM   1915 C  CD2 . HIS A 1 233 ? 24.906  13.647  28.176  1.00 25.94 ? 233 HIS A CD2 1 
ATOM   1916 C  CE1 . HIS A 1 233 ? 23.660  14.797  26.753  1.00 25.73 ? 233 HIS A CE1 1 
ATOM   1917 N  NE2 . HIS A 1 233 ? 24.853  14.241  26.927  1.00 24.61 ? 233 HIS A NE2 1 
ATOM   1918 N  N   . MET A 1 234 ? 23.484  11.237  32.300  1.00 18.82 ? 234 MET A N   1 
ATOM   1919 C  CA  . MET A 1 234 ? 23.375  10.774  33.686  1.00 20.61 ? 234 MET A CA  1 
ATOM   1920 C  C   . MET A 1 234 ? 22.551  11.740  34.540  1.00 23.14 ? 234 MET A C   1 
ATOM   1921 O  O   . MET A 1 234 ? 21.820  11.283  35.410  1.00 22.70 ? 234 MET A O   1 
ATOM   1922 C  CB  . MET A 1 234 ? 24.765  10.595  34.297  1.00 22.95 ? 234 MET A CB  1 
ATOM   1923 C  CG  . MET A 1 234 ? 24.753  9.873   35.652  1.00 22.60 ? 234 MET A CG  1 
ATOM   1924 S  SD  . MET A 1 234 ? 26.444  9.460   36.200  1.00 34.10 ? 234 MET A SD  1 
ATOM   1925 C  CE  . MET A 1 234 ? 27.118  11.120  36.187  1.00 35.72 ? 234 MET A CE  1 
ATOM   1926 N  N   . ASP A 1 235 ? 22.693  13.052  34.331  1.00 23.65 ? 235 ASP A N   1 
ATOM   1927 C  CA  . ASP A 1 235 ? 22.072  13.988  35.262  1.00 28.05 ? 235 ASP A CA  1 
ATOM   1928 C  C   . ASP A 1 235 ? 20.702  14.463  34.777  1.00 27.51 ? 235 ASP A C   1 
ATOM   1929 O  O   . ASP A 1 235 ? 20.101  15.355  35.383  1.00 26.60 ? 235 ASP A O   1 
ATOM   1930 C  CB  . ASP A 1 235 ? 23.039  15.111  35.649  1.00 35.19 ? 235 ASP A CB  1 
ATOM   1931 C  CG  . ASP A 1 235 ? 23.318  16.076  34.509  1.00 42.61 ? 235 ASP A CG  1 
ATOM   1932 O  OD1 . ASP A 1 235 ? 22.468  16.168  33.591  1.00 47.74 ? 235 ASP A OD1 1 
ATOM   1933 O  OD2 . ASP A 1 235 ? 24.375  16.746  34.551  1.00 52.06 ? 235 ASP A OD2 1 
ATOM   1934 N  N   . ASP A 1 236 ? 20.167  13.866  33.701  1.00 24.26 ? 236 ASP A N   1 
ATOM   1935 C  CA  . ASP A 1 236 ? 18.855  14.242  33.206  1.00 21.68 ? 236 ASP A CA  1 
ATOM   1936 C  C   . ASP A 1 236 ? 17.793  13.900  34.247  1.00 24.19 ? 236 ASP A C   1 
ATOM   1937 O  O   . ASP A 1 236 ? 17.674  12.748  34.676  1.00 21.71 ? 236 ASP A O   1 
ATOM   1938 C  CB  . ASP A 1 236 ? 18.511  13.465  31.931  1.00 23.08 ? 236 ASP A CB  1 
ATOM   1939 C  CG  . ASP A 1 236 ? 17.372  14.070  31.136  1.00 26.84 ? 236 ASP A CG  1 
ATOM   1940 O  OD1 . ASP A 1 236 ? 16.317  14.397  31.740  1.00 28.79 ? 236 ASP A OD1 1 
ATOM   1941 O  OD2 . ASP A 1 236 ? 17.533  14.179  29.891  1.00 24.30 ? 236 ASP A OD2 1 
ATOM   1942 N  N   . PRO A 1 237 ? 16.948  14.852  34.704  1.00 23.50 ? 237 PRO A N   1 
ATOM   1943 C  CA  . PRO A 1 237 ? 15.936  14.495  35.698  1.00 23.90 ? 237 PRO A CA  1 
ATOM   1944 C  C   . PRO A 1 237 ? 14.778  13.653  35.151  1.00 25.74 ? 237 PRO A C   1 
ATOM   1945 O  O   . PRO A 1 237 ? 13.912  13.210  35.904  1.00 24.93 ? 237 PRO A O   1 
ATOM   1946 C  CB  . PRO A 1 237 ? 15.446  15.886  36.156  1.00 24.81 ? 237 PRO A CB  1 
ATOM   1947 C  CG  . PRO A 1 237 ? 15.556  16.712  34.879  1.00 26.80 ? 237 PRO A CG  1 
ATOM   1948 C  CD  . PRO A 1 237 ? 16.901  16.284  34.319  1.00 24.24 ? 237 PRO A CD  1 
ATOM   1949 N  N   . SER A 1 238 ? 14.745  13.428  33.825  1.00 25.57 ? 238 SER A N   1 
ATOM   1950 C  CA  . SER A 1 238 ? 13.755  12.544  33.216  1.00 26.03 ? 238 SER A CA  1 
ATOM   1951 C  C   . SER A 1 238 ? 14.453  11.492  32.345  1.00 23.45 ? 238 SER A C   1 
ATOM   1952 O  O   . SER A 1 238 ? 14.470  11.605  31.117  1.00 22.10 ? 238 SER A O   1 
ATOM   1953 C  CB  . SER A 1 238 ? 12.743  13.315  32.401  1.00 29.60 ? 238 SER A CB  1 
ATOM   1954 O  OG  . SER A 1 238 ? 12.165  14.356  33.180  1.00 37.33 ? 238 SER A OG  1 
ATOM   1955 N  N   . PRO A 1 239 ? 15.020  10.442  32.974  1.00 22.48 ? 239 PRO A N   1 
ATOM   1956 C  CA  . PRO A 1 239 ? 15.778  9.411   32.257  1.00 20.57 ? 239 PRO A CA  1 
ATOM   1957 C  C   . PRO A 1 239 ? 14.865  8.635   31.315  1.00 23.59 ? 239 PRO A C   1 
ATOM   1958 O  O   . PRO A 1 239 ? 13.676  8.430   31.580  1.00 22.80 ? 239 PRO A O   1 
ATOM   1959 C  CB  . PRO A 1 239 ? 16.296  8.517   33.379  1.00 21.94 ? 239 PRO A CB  1 
ATOM   1960 C  CG  . PRO A 1 239 ? 15.299  8.752   34.521  1.00 24.70 ? 239 PRO A CG  1 
ATOM   1961 C  CD  . PRO A 1 239 ? 15.007  10.234  34.436  1.00 22.90 ? 239 PRO A CD  1 
ATOM   1962 N  N   . ARG A 1 240 ? 15.458  8.173   30.210  1.00 21.21 ? 240 ARG A N   1 
ATOM   1963 C  CA  . ARG A 1 240 ? 14.744  7.364   29.235  1.00 22.21 ? 240 ARG A CA  1 
ATOM   1964 C  C   . ARG A 1 240 ? 15.626  6.174   28.878  1.00 21.00 ? 240 ARG A C   1 
ATOM   1965 O  O   . ARG A 1 240 ? 16.792  6.339   28.548  1.00 20.13 ? 240 ARG A O   1 
ATOM   1966 C  CB  . ARG A 1 240 ? 14.397  8.188   27.997  1.00 23.71 ? 240 ARG A CB  1 
ATOM   1967 C  CG  . ARG A 1 240 ? 13.511  7.463   26.996  1.00 26.77 ? 240 ARG A CG  1 
ATOM   1968 C  CD  . ARG A 1 240 ? 13.149  8.467   25.913  0.01 25.35 ? 240 ARG A CD  1 
ATOM   1969 N  NE  . ARG A 1 240 ? 13.296  9.859   26.332  0.01 25.33 ? 240 ARG A NE  1 
ATOM   1970 C  CZ  . ARG A 1 240 ? 14.215  10.700  25.863  0.01 25.22 ? 240 ARG A CZ  1 
ATOM   1971 N  NH1 . ARG A 1 240 ? 15.070  10.297  24.938  0.01 25.09 ? 240 ARG A NH1 1 
ATOM   1972 N  NH2 . ARG A 1 240 ? 14.275  11.939  26.318  0.01 25.07 ? 240 ARG A NH2 1 
ATOM   1973 N  N   . GLU A 1 241 ? 15.049  4.983   28.935  1.00 19.01 ? 241 GLU A N   1 
ATOM   1974 C  CA  . GLU A 1 241 ? 15.746  3.751   28.579  1.00 18.70 ? 241 GLU A CA  1 
ATOM   1975 C  C   . GLU A 1 241 ? 15.935  3.690   27.060  1.00 18.09 ? 241 GLU A C   1 
ATOM   1976 O  O   . GLU A 1 241 ? 15.048  4.103   26.312  1.00 20.38 ? 241 GLU A O   1 
ATOM   1977 C  CB  . GLU A 1 241 ? 14.919  2.559   29.053  1.00 21.56 ? 241 GLU A CB  1 
ATOM   1978 C  CG  . GLU A 1 241 ? 14.682  2.483   30.560  1.00 27.41 ? 241 GLU A CG  1 
ATOM   1979 C  CD  . GLU A 1 241 ? 13.591  1.458   30.896  1.00 35.81 ? 241 GLU A CD  1 
ATOM   1980 O  OE1 . GLU A 1 241 ? 12.708  1.211   30.022  1.00 45.53 ? 241 GLU A OE1 1 
ATOM   1981 O  OE2 . GLU A 1 241 ? 13.614  0.898   32.016  1.00 39.17 ? 241 GLU A OE2 1 
ATOM   1982 N  N   . MET A 1 242 ? 17.132  3.239   26.636  1.00 15.34 ? 242 MET A N   1 
ATOM   1983 C  CA  . MET A 1 242 ? 17.436  3.085   25.223  1.00 13.50 ? 242 MET A CA  1 
ATOM   1984 C  C   . MET A 1 242 ? 16.918  1.728   24.774  1.00 11.88 ? 242 MET A C   1 
ATOM   1985 O  O   . MET A 1 242 ? 17.535  0.682   25.028  1.00 12.58 ? 242 MET A O   1 
ATOM   1986 C  CB  . MET A 1 242 ? 18.949  3.155   24.990  1.00 14.30 ? 242 MET A CB  1 
ATOM   1987 C  CG  . MET A 1 242 ? 19.295  3.184   23.495  1.00 12.74 ? 242 MET A CG  1 
ATOM   1988 S  SD  . MET A 1 242 ? 21.079  3.110   23.198  1.00 14.46 ? 242 MET A SD  1 
ATOM   1989 C  CE  . MET A 1 242 ? 21.554  4.733   23.803  1.00 15.60 ? 242 MET A CE  1 
ATOM   1990 N  N   . ILE A 1 243 ? 15.745  1.780   24.132  1.00 10.66 ? 243 ILE A N   1 
ATOM   1991 C  CA  . ILE A 1 243 ? 15.077  0.598   23.611  1.00 11.38 ? 243 ILE A CA  1 
ATOM   1992 C  C   . ILE A 1 243 ? 14.506  0.930   22.231  1.00 11.36 ? 243 ILE A C   1 
ATOM   1993 O  O   . ILE A 1 243 ? 14.308  2.104   21.896  1.00 11.30 ? 243 ILE A O   1 
ATOM   1994 C  CB  . ILE A 1 243 ? 13.907  0.166   24.521  1.00 13.14 ? 243 ILE A CB  1 
ATOM   1995 C  CG1 . ILE A 1 243 ? 12.955  1.319   24.873  1.00 13.84 ? 243 ILE A CG1 1 
ATOM   1996 C  CG2 . ILE A 1 243 ? 14.470  -0.504  25.786  1.00 14.40 ? 243 ILE A CG2 1 
ATOM   1997 C  CD1 . ILE A 1 243 ? 11.750  0.898   25.750  1.00 15.48 ? 243 ILE A CD1 1 
ATOM   1998 N  N   . ASN A 1 244 ? 14.142  -0.094  21.461  1.00 9.72  ? 244 ASN A N   1 
ATOM   1999 C  CA  . ASN A 1 244 ? 13.414  0.083   20.212  1.00 10.39 ? 244 ASN A CA  1 
ATOM   2000 C  C   . ASN A 1 244 ? 14.133  1.098   19.324  1.00 9.94  ? 244 ASN A C   1 
ATOM   2001 O  O   . ASN A 1 244 ? 13.524  1.925   18.645  1.00 9.91  ? 244 ASN A O   1 
ATOM   2002 C  CB  . ASN A 1 244 ? 11.951  0.471   20.444  1.00 11.40 ? 244 ASN A CB  1 
ATOM   2003 C  CG  . ASN A 1 244 ? 11.266  -0.467  21.400  1.00 12.15 ? 244 ASN A CG  1 
ATOM   2004 O  OD1 . ASN A 1 244 ? 11.468  -1.668  21.299  1.00 14.03 ? 244 ASN A OD1 1 
ATOM   2005 N  ND2 . ASN A 1 244 ? 10.423  0.159   22.244  1.00 14.41 ? 244 ASN A ND2 1 
ATOM   2006 N  N   . ASN A 1 245 ? 15.465  0.954   19.214  1.00 9.00  ? 245 ASN A N   1 
ATOM   2007 C  CA  . ASN A 1 245 ? 16.295  1.888   18.446  1.00 9.05  ? 245 ASN A CA  1 
ATOM   2008 C  C   . ASN A 1 245 ? 16.519  1.329   17.050  1.00 8.17  ? 245 ASN A C   1 
ATOM   2009 O  O   . ASN A 1 245 ? 17.656  1.263   16.579  1.00 9.16  ? 245 ASN A O   1 
ATOM   2010 C  CB  . ASN A 1 245 ? 17.584  2.214   19.168  1.00 9.57  ? 245 ASN A CB  1 
ATOM   2011 C  CG  . ASN A 1 245 ? 18.453  1.014   19.451  1.00 9.28  ? 245 ASN A CG  1 
ATOM   2012 O  OD1 . ASN A 1 245 ? 18.033  -0.128  19.371  1.00 10.68 ? 245 ASN A OD1 1 
ATOM   2013 N  ND2 . ASN A 1 245 ? 19.723  1.267   19.759  1.00 11.67 ? 245 ASN A ND2 1 
ATOM   2014 N  N   . PHE A 1 246 ? 15.449  0.956   16.340  1.00 7.86  ? 246 PHE A N   1 
ATOM   2015 C  CA  . PHE A 1 246 ? 15.493  0.437   14.973  1.00 8.37  ? 246 PHE A CA  1 
ATOM   2016 C  C   . PHE A 1 246 ? 14.510  1.277   14.176  1.00 7.93  ? 246 PHE A C   1 
ATOM   2017 O  O   . PHE A 1 246 ? 13.490  1.746   14.721  1.00 8.41  ? 246 PHE A O   1 
ATOM   2018 C  CB  . PHE A 1 246 ? 15.122  -1.061  14.879  1.00 9.18  ? 246 PHE A CB  1 
ATOM   2019 C  CG  . PHE A 1 246 ? 13.768  -1.396  15.449  1.00 8.43  ? 246 PHE A CG  1 
ATOM   2020 C  CD1 . PHE A 1 246 ? 13.561  -1.642  16.802  1.00 9.14  ? 246 PHE A CD1 1 
ATOM   2021 C  CD2 . PHE A 1 246 ? 12.673  -1.510  14.605  1.00 8.96  ? 246 PHE A CD2 1 
ATOM   2022 C  CE1 . PHE A 1 246 ? 12.297  -1.933  17.297  1.00 9.76  ? 246 PHE A CE1 1 
ATOM   2023 C  CE2 . PHE A 1 246 ? 11.397  -1.772  15.088  1.00 10.46 ? 246 PHE A CE2 1 
ATOM   2024 C  CZ  . PHE A 1 246 ? 11.195  -2.024  16.439  1.00 9.81  ? 246 PHE A CZ  1 
ATOM   2025 N  N   . ARG A 1 247 ? 14.801  1.409   12.907  1.00 7.82  ? 247 ARG A N   1 
ATOM   2026 C  CA  . ARG A 1 247 ? 13.880  2.112   11.985  1.00 7.77  ? 247 ARG A CA  1 
ATOM   2027 C  C   . ARG A 1 247 ? 12.904  1.088   11.412  1.00 7.68  ? 247 ARG A C   1 
ATOM   2028 O  O   . ARG A 1 247 ? 13.286  -0.056  11.151  1.00 8.56  ? 247 ARG A O   1 
ATOM   2029 C  CB  . ARG A 1 247 ? 14.685  2.788   10.876  1.00 8.16  ? 247 ARG A CB  1 
ATOM   2030 C  CG  . ARG A 1 247 ? 13.914  3.757   10.001  1.00 7.53  ? 247 ARG A CG  1 
ATOM   2031 C  CD  . ARG A 1 247 ? 14.753  4.194   8.801   1.00 7.48  ? 247 ARG A CD  1 
ATOM   2032 N  NE  . ARG A 1 247 ? 14.113  5.348   8.167   1.00 6.96  ? 247 ARG A NE  1 
ATOM   2033 C  CZ  . ARG A 1 247 ? 14.626  5.956   7.092   1.00 7.26  ? 247 ARG A CZ  1 
ATOM   2034 N  NH1 . ARG A 1 247 ? 15.623  5.420   6.419   1.00 8.51  ? 247 ARG A NH1 1 
ATOM   2035 N  NH2 . ARG A 1 247 ? 14.062  7.089   6.648   1.00 8.04  ? 247 ARG A NH2 1 
ATOM   2036 N  N   . GLN A 1 248 ? 11.637  1.467   11.207  1.00 7.50  ? 248 GLN A N   1 
ATOM   2037 C  CA  . GLN A 1 248 ? 10.715  0.608   10.470  1.00 6.94  ? 248 GLN A CA  1 
ATOM   2038 C  C   . GLN A 1 248 ? 11.203  0.318   9.055   1.00 7.30  ? 248 GLN A C   1 
ATOM   2039 O  O   . GLN A 1 248 ? 11.902  1.142   8.449   1.00 7.58  ? 248 GLN A O   1 
ATOM   2040 C  CB  . GLN A 1 248 ? 9.326   1.276   10.371  1.00 7.88  ? 248 GLN A CB  1 
ATOM   2041 C  CG  . GLN A 1 248 ? 8.674   1.607   11.703  1.00 8.13  ? 248 GLN A CG  1 
ATOM   2042 C  CD  . GLN A 1 248 ? 8.311   0.396   12.514  1.00 8.90  ? 248 GLN A CD  1 
ATOM   2043 O  OE1 . GLN A 1 248 ? 9.063   -0.059  13.365  1.00 10.30 ? 248 GLN A OE1 1 
ATOM   2044 N  NE2 . GLN A 1 248 ? 7.178   -0.223  12.174  1.00 10.94 ? 248 GLN A NE2 1 
ATOM   2045 N  N   . VAL A 1 249 ? 10.795  -0.804  8.477   1.00 7.46  ? 249 VAL A N   1 
ATOM   2046 C  CA  . VAL A 1 249 ? 11.134  -1.114  7.106   1.00 8.22  ? 249 VAL A CA  1 
ATOM   2047 C  C   . VAL A 1 249 ? 10.522  -0.073  6.150   1.00 8.20  ? 249 VAL A C   1 
ATOM   2048 O  O   . VAL A 1 249 ? 9.398   0.422   6.360   1.00 8.97  ? 249 VAL A O   1 
ATOM   2049 C  CB  . VAL A 1 249 ? 10.809  -2.555  6.684   1.00 9.20  ? 249 VAL A CB  1 
ATOM   2050 C  CG1 . VAL A 1 249 ? 11.693  -3.554  7.462   1.00 10.57 ? 249 VAL A CG1 1 
ATOM   2051 C  CG2 . VAL A 1 249 ? 9.324   -2.830  6.803   1.00 12.09 ? 249 VAL A CG2 1 
ATOM   2052 N  N   . GLN A 1 250 ? 11.227  0.130   5.057   1.00 8.24  ? 250 GLN A N   1 
ATOM   2053 C  CA  . GLN A 1 250 ? 10.852  1.123   4.060   1.00 8.42  ? 250 GLN A CA  1 
ATOM   2054 C  C   . GLN A 1 250 ? 10.274  0.423   2.840   1.00 9.91  ? 250 GLN A C   1 
ATOM   2055 O  O   . GLN A 1 250 ? 10.615  -0.720  2.540   1.00 11.42 ? 250 GLN A O   1 
ATOM   2056 C  CB  . GLN A 1 250 ? 12.130  1.848   3.601   1.00 8.57  ? 250 GLN A CB  1 
ATOM   2057 C  CG  . GLN A 1 250 ? 12.968  2.444   4.755   1.00 8.27  ? 250 GLN A CG  1 
ATOM   2058 C  CD  . GLN A 1 250 ? 12.232  3.567   5.428   1.00 8.10  ? 250 GLN A CD  1 
ATOM   2059 O  OE1 . GLN A 1 250 ? 11.939  4.595   4.782   1.00 9.60  ? 250 GLN A OE1 1 
ATOM   2060 N  NE2 . GLN A 1 250 ? 11.875  3.395   6.674   1.00 6.96  ? 250 GLN A NE2 1 
ATOM   2061 N  N   . LYS A 1 251 ? 9.436   1.156   2.080   1.00 9.30  ? 251 LYS A N   1 
ATOM   2062 C  CA  . LYS A 1 251 ? 8.991   0.565   0.817   1.00 12.34 ? 251 LYS A CA  1 
ATOM   2063 C  C   . LYS A 1 251 ? 10.185  0.302   -0.101  1.00 12.81 ? 251 LYS A C   1 
ATOM   2064 O  O   . LYS A 1 251 ? 11.155  1.089   -0.123  1.00 12.59 ? 251 LYS A O   1 
ATOM   2065 C  CB  . LYS A 1 251 ? 7.996   1.481   0.096   1.00 11.60 ? 251 LYS A CB  1 
ATOM   2066 C  CG  . LYS A 1 251 ? 6.645   1.489   0.822   1.00 12.48 ? 251 LYS A CG  1 
ATOM   2067 C  CD  . LYS A 1 251 ? 5.666   2.385   0.167   1.00 13.35 ? 251 LYS A CD  1 
ATOM   2068 C  CE  . LYS A 1 251 ? 4.212   2.186   0.614   1.00 10.29 ? 251 LYS A CE  1 
ATOM   2069 N  NZ  . LYS A 1 251 ? 4.012   2.168   2.079   1.00 10.07 ? 251 LYS A NZ  1 
ATOM   2070 N  N   . PHE A 1 252 ? 10.090  -0.757  -0.905  1.00 13.69 ? 252 PHE A N   1 
ATOM   2071 C  CA  . PHE A 1 252 ? 11.159  -1.179  -1.805  1.00 14.96 ? 252 PHE A CA  1 
ATOM   2072 C  C   . PHE A 1 252 ? 10.474  -1.771  -3.032  1.00 22.22 ? 252 PHE A C   1 
ATOM   2073 O  O   . PHE A 1 252 ? 10.150  -2.951  -3.003  1.00 25.39 ? 252 PHE A O   1 
ATOM   2074 C  CB  . PHE A 1 252 ? 11.971  -2.263  -1.081  1.00 16.13 ? 252 PHE A CB  1 
ATOM   2075 C  CG  . PHE A 1 252 ? 13.254  -2.713  -1.763  1.00 16.59 ? 252 PHE A CG  1 
ATOM   2076 C  CD1 . PHE A 1 252 ? 14.427  -1.980  -1.675  1.00 16.35 ? 252 PHE A CD1 1 
ATOM   2077 C  CD2 . PHE A 1 252 ? 13.291  -3.933  -2.429  1.00 18.36 ? 252 PHE A CD2 1 
ATOM   2078 C  CE1 . PHE A 1 252 ? 15.583  -2.453  -2.302  1.00 16.92 ? 252 PHE A CE1 1 
ATOM   2079 C  CE2 . PHE A 1 252 ? 14.463  -4.398  -3.025  1.00 19.09 ? 252 PHE A CE2 1 
ATOM   2080 C  CZ  . PHE A 1 252 ? 15.613  -3.659  -2.933  1.00 17.80 ? 252 PHE A CZ  1 
ATOM   2081 N  N   . ASP A 1 253 ? 10.179  -0.952  -4.050  1.00 28.28 ? 253 ASP A N   1 
ATOM   2082 C  CA  . ASP A 1 253 ? 9.376   -1.411  -5.198  1.00 26.26 ? 253 ASP A CA  1 
ATOM   2083 C  C   . ASP A 1 253 ? 10.194  -1.355  -6.483  1.00 24.12 ? 253 ASP A C   1 
ATOM   2084 O  O   . ASP A 1 253 ? 11.020  -0.462  -6.681  1.00 23.60 ? 253 ASP A O   1 
ATOM   2085 C  CB  . ASP A 1 253 ? 8.007   -0.714  -5.323  1.00 31.62 ? 253 ASP A CB  1 
ATOM   2086 C  CG  . ASP A 1 253 ? 6.969   -1.415  -6.220  1.00 44.53 ? 253 ASP A CG  1 
ATOM   2087 O  OD1 . ASP A 1 253 ? 6.856   -2.688  -6.147  1.00 42.36 ? 253 ASP A OD1 1 
ATOM   2088 O  OD2 . ASP A 1 253 ? 6.242   -0.687  -6.990  1.00 42.77 ? 253 ASP A OD2 1 
ATOM   2089 N  N   A GLU A 1 254 ? 9.958   -2.340  -7.359  0.50 25.78 ? 254 GLU A N   1 
ATOM   2090 N  N   B GLU A 1 254 ? 9.953   -2.383  -7.313  0.50 25.89 ? 254 GLU A N   1 
ATOM   2091 C  CA  A GLU A 1 254 ? 10.625  -2.384  -8.652  0.50 26.79 ? 254 GLU A CA  1 
ATOM   2092 C  CA  B GLU A 1 254 ? 10.543  -2.570  -8.632  0.50 27.16 ? 254 GLU A CA  1 
ATOM   2093 C  C   A GLU A 1 254 ? 12.130  -2.523  -8.445  0.50 26.59 ? 254 GLU A C   1 
ATOM   2094 C  C   B GLU A 1 254 ? 12.060  -2.714  -8.534  0.50 26.52 ? 254 GLU A C   1 
ATOM   2095 O  O   A GLU A 1 254 ? 12.913  -1.940  -9.187  0.50 27.92 ? 254 GLU A O   1 
ATOM   2096 O  O   B GLU A 1 254 ? 12.775  -2.362  -9.462  0.50 26.10 ? 254 GLU A O   1 
ATOM   2097 C  CB  A GLU A 1 254 ? 10.331  -1.107  -9.442  0.50 29.07 ? 254 GLU A CB  1 
ATOM   2098 C  CB  B GLU A 1 254 ? 10.068  -1.488  -9.602  0.50 30.06 ? 254 GLU A CB  1 
ATOM   2099 C  CG  A GLU A 1 254 ? 8.849   -0.871  -9.677  0.50 30.49 ? 254 GLU A CG  1 
ATOM   2100 C  CG  B GLU A 1 254 ? 8.602   -1.637  -9.973  0.50 31.66 ? 254 GLU A CG  1 
ATOM   2101 C  CD  A GLU A 1 254 ? 8.594   0.155   -10.763 0.50 33.56 ? 254 GLU A CD  1 
ATOM   2102 C  CD  B GLU A 1 254 ? 8.256   -2.988  -10.576 0.50 33.60 ? 254 GLU A CD  1 
ATOM   2103 O  OE1 A GLU A 1 254 ? 9.465   1.018   -10.945 0.50 36.46 ? 254 GLU A OE1 1 
ATOM   2104 O  OE1 B GLU A 1 254 ? 9.109   -3.567  -11.284 0.50 38.44 ? 254 GLU A OE1 1 
ATOM   2105 O  OE2 A GLU A 1 254 ? 7.536   0.076   -11.424 0.50 36.89 ? 254 GLU A OE2 1 
ATOM   2106 O  OE2 B GLU A 1 254 ? 7.143   -3.465  -10.326 0.50 32.81 ? 254 GLU A OE2 1 
ATOM   2107 N  N   . ARG A 1 255 ? 12.524  -3.281  -7.417  1.00 26.36 ? 255 ARG A N   1 
ATOM   2108 C  CA  . ARG A 1 255 ? 13.949  -3.471  -7.148  1.00 23.36 ? 255 ARG A CA  1 
ATOM   2109 C  C   . ARG A 1 255 ? 14.187  -4.875  -6.617  1.00 23.62 ? 255 ARG A C   1 
ATOM   2110 O  O   . ARG A 1 255 ? 13.291  -5.518  -6.065  1.00 27.21 ? 255 ARG A O   1 
ATOM   2111 C  CB  . ARG A 1 255 ? 14.435  -2.454  -6.121  1.00 19.69 ? 255 ARG A CB  1 
ATOM   2112 C  CG  . ARG A 1 255 ? 14.364  -1.008  -6.597  1.00 21.13 ? 255 ARG A CG  1 
ATOM   2113 C  CD  . ARG A 1 255 ? 14.940  -0.071  -5.540  1.00 21.55 ? 255 ARG A CD  1 
ATOM   2114 N  NE  . ARG A 1 255 ? 16.313  -0.480  -5.331  1.00 23.52 ? 255 ARG A NE  1 
ATOM   2115 C  CZ  . ARG A 1 255 ? 17.002  -0.161  -4.245  1.00 22.24 ? 255 ARG A CZ  1 
ATOM   2116 N  NH1 . ARG A 1 255 ? 16.395  0.523   -3.284  1.00 23.22 ? 255 ARG A NH1 1 
ATOM   2117 N  NH2 . ARG A 1 255 ? 18.247  -0.597  -4.116  1.00 16.09 ? 255 ARG A NH2 1 
ATOM   2118 N  N   . LEU A 1 256 ? 15.421  -5.345  -6.808  1.00 21.37 ? 256 LEU A N   1 
ATOM   2119 C  CA  . LEU A 1 256 ? 15.799  -6.646  -6.298  1.00 20.18 ? 256 LEU A CA  1 
ATOM   2120 C  C   . LEU A 1 256 ? 16.813  -6.526  -5.145  1.00 17.83 ? 256 LEU A C   1 
ATOM   2121 O  O   . LEU A 1 256 ? 17.524  -5.528  -4.989  1.00 19.81 ? 256 LEU A O   1 
ATOM   2122 C  CB  . LEU A 1 256 ? 16.379  -7.481  -7.449  1.00 22.76 ? 256 LEU A CB  1 
ATOM   2123 C  CG  . LEU A 1 256 ? 15.438  -7.797  -8.618  1.00 24.84 ? 256 LEU A CG  1 
ATOM   2124 C  CD1 . LEU A 1 256 ? 16.213  -8.378  -9.780  1.00 25.62 ? 256 LEU A CD1 1 
ATOM   2125 C  CD2 . LEU A 1 256 ? 14.336  -8.773  -8.186  1.00 30.76 ? 256 LEU A CD2 1 
ATOM   2126 N  N   . VAL A 1 257 ? 16.809  -7.575  -4.327  1.00 18.19 ? 257 VAL A N   1 
ATOM   2127 C  CA  . VAL A 1 257 ? 17.929  -7.870  -3.459  1.00 15.41 ? 257 VAL A CA  1 
ATOM   2128 C  C   . VAL A 1 257 ? 18.643  -9.089  -4.016  1.00 14.19 ? 257 VAL A C   1 
ATOM   2129 O  O   . VAL A 1 257 ? 18.018  -10.129 -4.306  1.00 16.04 ? 257 VAL A O   1 
ATOM   2130 C  CB  . VAL A 1 257 ? 17.434  -8.169  -2.035  1.00 15.17 ? 257 VAL A CB  1 
ATOM   2131 C  CG1 . VAL A 1 257 ? 18.509  -8.691  -1.066  1.00 15.24 ? 257 VAL A CG1 1 
ATOM   2132 C  CG2 . VAL A 1 257 ? 16.664  -6.998  -1.464  1.00 17.41 ? 257 VAL A CG2 1 
ATOM   2133 N  N   . TYR A 1 258 ? 19.924  -8.925  -4.216  1.00 13.16 ? 258 TYR A N   1 
ATOM   2134 C  CA  . TYR A 1 258 ? 20.710  -9.973  -4.823  1.00 13.90 ? 258 TYR A CA  1 
ATOM   2135 C  C   . TYR A 1 258 ? 21.180  -10.892 -3.720  1.00 13.90 ? 258 TYR A C   1 
ATOM   2136 O  O   . TYR A 1 258 ? 21.456  -10.432 -2.601  1.00 14.09 ? 258 TYR A O   1 
ATOM   2137 C  CB  . TYR A 1 258 ? 21.823  -9.378  -5.683  1.00 14.22 ? 258 TYR A CB  1 
ATOM   2138 C  CG  . TYR A 1 258 ? 21.249  -8.451  -6.725  1.00 18.09 ? 258 TYR A CG  1 
ATOM   2139 C  CD1 . TYR A 1 258 ? 20.735  -8.961  -7.913  1.00 20.19 ? 258 TYR A CD1 1 
ATOM   2140 C  CD2 . TYR A 1 258 ? 21.106  -7.091  -6.467  1.00 19.05 ? 258 TYR A CD2 1 
ATOM   2141 C  CE1 . TYR A 1 258 ? 20.169  -8.116  -8.859  1.00 24.55 ? 258 TYR A CE1 1 
ATOM   2142 C  CE2 . TYR A 1 258 ? 20.482  -6.249  -7.373  1.00 23.29 ? 258 TYR A CE2 1 
ATOM   2143 C  CZ  . TYR A 1 258 ? 20.053  -6.761  -8.584  1.00 24.30 ? 258 TYR A CZ  1 
ATOM   2144 O  OH  . TYR A 1 258 ? 19.464  -5.867  -9.435  1.00 28.65 ? 258 TYR A OH  1 
ATOM   2145 N  N   . THR A 1 259 ? 21.215  -12.196 -4.001  1.00 13.09 ? 259 THR A N   1 
ATOM   2146 C  CA  . THR A 1 259 ? 21.692  -13.178 -3.024  1.00 13.27 ? 259 THR A CA  1 
ATOM   2147 C  C   . THR A 1 259 ? 22.909  -13.905 -3.578  1.00 13.29 ? 259 THR A C   1 
ATOM   2148 O  O   . THR A 1 259 ? 23.007  -14.214 -4.791  1.00 14.42 ? 259 THR A O   1 
ATOM   2149 C  CB  . THR A 1 259 ? 20.581  -14.145 -2.579  1.00 14.26 ? 259 THR A CB  1 
ATOM   2150 O  OG1 . THR A 1 259 ? 20.127  -14.738 -3.802  1.00 18.08 ? 259 THR A OG1 1 
ATOM   2151 C  CG2 . THR A 1 259 ? 19.417  -13.411 -1.965  1.00 14.16 ? 259 THR A CG2 1 
ATOM   2152 N  N   . SER A 1 260 ? 23.826  -14.266 -2.698  1.00 13.45 ? 260 SER A N   1 
ATOM   2153 C  CA  . SER A 1 260 ? 24.980  -15.068 -3.072  1.00 15.17 ? 260 SER A CA  1 
ATOM   2154 C  C   . SER A 1 260 ? 24.671  -16.559 -3.040  1.00 16.23 ? 260 SER A C   1 
ATOM   2155 O  O   . SER A 1 260 ? 25.559  -17.357 -3.324  1.00 18.83 ? 260 SER A O   1 
ATOM   2156 C  CB  . SER A 1 260 ? 26.146  -14.795 -2.206  1.00 15.67 ? 260 SER A CB  1 
ATOM   2157 O  OG  . SER A 1 260 ? 25.844  -15.179 -0.873  1.00 14.52 ? 260 SER A OG  1 
ATOM   2158 N  N   . PHE A 1 261 ? 23.468  -16.897 -2.615  1.00 16.08 ? 261 PHE A N   1 
ATOM   2159 C  CA  . PHE A 1 261 ? 23.044  -18.277 -2.504  1.00 18.79 ? 261 PHE A CA  1 
ATOM   2160 C  C   . PHE A 1 261 ? 21.784  -18.438 -3.338  1.00 20.26 ? 261 PHE A C   1 
ATOM   2161 O  O   . PHE A 1 261 ? 20.955  -17.536 -3.499  1.00 20.59 ? 261 PHE A O   1 
ATOM   2162 C  CB  . PHE A 1 261 ? 22.806  -18.595 -1.021  1.00 17.06 ? 261 PHE A CB  1 
ATOM   2163 C  CG  . PHE A 1 261 ? 21.808  -17.676 -0.368  1.00 17.38 ? 261 PHE A CG  1 
ATOM   2164 C  CD1 . PHE A 1 261 ? 20.443  -17.951 -0.336  1.00 17.36 ? 261 PHE A CD1 1 
ATOM   2165 C  CD2 . PHE A 1 261 ? 22.240  -16.488 0.193   1.00 14.46 ? 261 PHE A CD2 1 
ATOM   2166 C  CE1 . PHE A 1 261 ? 19.531  -17.097 0.271   1.00 17.81 ? 261 PHE A CE1 1 
ATOM   2167 C  CE2 . PHE A 1 261 ? 21.339  -15.640 0.815   1.00 15.41 ? 261 PHE A CE2 1 
ATOM   2168 C  CZ  . PHE A 1 261 ? 19.999  -15.940 0.870   1.00 17.56 ? 261 PHE A CZ  1 
ATOM   2169 N  N   . SER A 1 262 ? 21.634  -19.635 -3.908  1.00 26.72 ? 262 SER A N   1 
ATOM   2170 C  CA  . SER A 1 262 ? 20.346  -19.958 -4.482  1.00 28.54 ? 262 SER A CA  1 
ATOM   2171 C  C   . SER A 1 262 ? 19.720  -20.982 -3.547  1.00 37.62 ? 262 SER A C   1 
ATOM   2172 O  O   . SER A 1 262 ? 18.593  -20.792 -3.120  1.00 34.23 ? 262 SER A O   1 
ATOM   2173 C  CB  . SER A 1 262 ? 20.474  -20.480 -5.890  1.00 35.91 ? 262 SER A CB  1 
ATOM   2174 O  OG  . SER A 1 262 ? 21.457  -21.496 -5.930  1.00 38.94 ? 262 SER A OG  1 
ATOM   2175 N  N   . GLN A 1 263 ? 20.529  -21.987 -3.162  1.00 42.25 ? 263 GLN A N   1 
ATOM   2176 C  CA  . GLN A 1 263 ? 20.116  -23.129 -2.346  1.00 48.38 ? 263 GLN A CA  1 
ATOM   2177 C  C   . GLN A 1 263 ? 19.144  -22.703 -1.219  1.00 51.82 ? 263 GLN A C   1 
ATOM   2178 O  O   . GLN A 1 263 ? 19.335  -21.610 -0.612  1.00 38.84 ? 263 GLN A O   1 
ATOM   2179 C  CB  . GLN A 1 263 ? 21.319  -23.966 -1.857  1.00 50.12 ? 263 GLN A CB  1 
ATOM   2180 C  CG  . GLN A 1 263 ? 22.134  -24.638 -2.970  1.00 47.41 ? 263 GLN A CG  1 
ATOM   2181 C  CD  . GLN A 1 263 ? 22.433  -26.117 -2.812  1.00 47.46 ? 263 GLN A CD  1 
ATOM   2182 O  OE1 . GLN A 1 263 ? 23.425  -26.538 -2.205  1.00 44.05 ? 263 GLN A OE1 1 
ATOM   2183 N  NE2 . GLN A 1 263 ? 21.600  -26.938 -3.430  1.00 31.69 ? 263 GLN A NE2 1 
ATOM   2184 N  N   . LYS B 1 3   ? -0.773  17.742  -1.920  1.00 38.16 ? 3   LYS B N   1 
ATOM   2185 C  CA  . LYS B 1 3   ? -0.471  16.725  -2.962  1.00 30.96 ? 3   LYS B CA  1 
ATOM   2186 C  C   . LYS B 1 3   ? 0.415   15.632  -2.351  1.00 27.94 ? 3   LYS B C   1 
ATOM   2187 O  O   . LYS B 1 3   ? 1.338   15.115  -3.002  1.00 26.51 ? 3   LYS B O   1 
ATOM   2188 C  CB  . LYS B 1 3   ? 0.170   17.370  -4.192  1.00 37.18 ? 3   LYS B CB  1 
ATOM   2189 C  CG  . LYS B 1 3   ? 1.574   17.904  -3.957  1.00 41.15 ? 3   LYS B CG  1 
ATOM   2190 C  CD  . LYS B 1 3   ? 1.675   19.307  -3.412  1.00 44.75 ? 3   LYS B CD  1 
ATOM   2191 C  CE  . LYS B 1 3   ? 2.966   19.983  -3.832  1.00 42.04 ? 3   LYS B CE  1 
ATOM   2192 N  NZ  . LYS B 1 3   ? 4.150   19.075  -3.781  1.00 40.59 ? 3   LYS B NZ  1 
ATOM   2193 N  N   . TRP B 1 4   ? 0.128   15.279  -1.082  1.00 15.29 ? 4   TRP B N   1 
ATOM   2194 C  CA  . TRP B 1 4   ? 0.793   14.140  -0.474  1.00 13.83 ? 4   TRP B CA  1 
ATOM   2195 C  C   . TRP B 1 4   ? 0.544   12.927  -1.354  1.00 12.86 ? 4   TRP B C   1 
ATOM   2196 O  O   . TRP B 1 4   ? -0.487  12.847  -2.033  1.00 14.23 ? 4   TRP B O   1 
ATOM   2197 C  CB  . TRP B 1 4   ? 0.268   13.929  0.955   1.00 11.43 ? 4   TRP B CB  1 
ATOM   2198 C  CG  . TRP B 1 4   ? -1.186  13.586  1.144   1.00 11.77 ? 4   TRP B CG  1 
ATOM   2199 C  CD1 . TRP B 1 4   ? -2.211  14.445  1.404   1.00 11.26 ? 4   TRP B CD1 1 
ATOM   2200 C  CD2 . TRP B 1 4   ? -1.785  12.267  1.148   1.00 10.32 ? 4   TRP B CD2 1 
ATOM   2201 N  NE1 . TRP B 1 4   ? -3.407  13.781  1.496   1.00 12.18 ? 4   TRP B NE1 1 
ATOM   2202 C  CE2 . TRP B 1 4   ? -3.168  12.432  1.400   1.00 10.84 ? 4   TRP B CE2 1 
ATOM   2203 C  CE3 . TRP B 1 4   ? -1.263  10.965  0.991   1.00 9.80  ? 4   TRP B CE3 1 
ATOM   2204 C  CZ2 . TRP B 1 4   ? -4.058  11.353  1.488   1.00 10.85 ? 4   TRP B CZ2 1 
ATOM   2205 C  CZ3 . TRP B 1 4   ? -2.125  9.883   1.101   1.00 9.14  ? 4   TRP B CZ3 1 
ATOM   2206 C  CH2 . TRP B 1 4   ? -3.487  10.104  1.312   1.00 10.04 ? 4   TRP B CH2 1 
ATOM   2207 N  N   . THR B 1 5   ? 1.480   11.980  -1.317  1.00 11.32 ? 5   THR B N   1 
ATOM   2208 C  CA  . THR B 1 5   ? 1.394   10.782  -2.144  1.00 11.42 ? 5   THR B CA  1 
ATOM   2209 C  C   . THR B 1 5   ? 1.847   9.593   -1.278  1.00 10.98 ? 5   THR B C   1 
ATOM   2210 O  O   . THR B 1 5   ? 2.281   9.755   -0.114  1.00 10.41 ? 5   THR B O   1 
ATOM   2211 C  CB  . THR B 1 5   ? 2.333   10.885  -3.386  1.00 12.47 ? 5   THR B CB  1 
ATOM   2212 O  OG1 . THR B 1 5   ? 3.657   10.865  -2.838  1.00 14.77 ? 5   THR B OG1 1 
ATOM   2213 C  CG2 . THR B 1 5   ? 2.112   12.135  -4.233  1.00 15.29 ? 5   THR B CG2 1 
ATOM   2214 N  N   . TYR B 1 6   ? 1.968   8.451   -1.939  1.00 11.10 ? 6   TYR B N   1 
ATOM   2215 C  CA  . TYR B 1 6   ? 2.603   7.280   -1.358  1.00 11.32 ? 6   TYR B CA  1 
ATOM   2216 C  C   . TYR B 1 6   ? 3.970   6.934   -1.948  1.00 12.44 ? 6   TYR B C   1 
ATOM   2217 O  O   . TYR B 1 6   ? 4.533   5.881   -1.655  1.00 12.45 ? 6   TYR B O   1 
ATOM   2218 C  CB  . TYR B 1 6   ? 1.687   6.073   -1.466  1.00 10.58 ? 6   TYR B CB  1 
ATOM   2219 C  CG  . TYR B 1 6   ? 0.442   6.168   -0.625  1.00 9.42  ? 6   TYR B CG  1 
ATOM   2220 C  CD1 . TYR B 1 6   ? -0.734  6.705   -1.107  1.00 9.24  ? 6   TYR B CD1 1 
ATOM   2221 C  CD2 . TYR B 1 6   ? 0.463   5.657   0.666   1.00 9.17  ? 6   TYR B CD2 1 
ATOM   2222 C  CE1 . TYR B 1 6   ? -1.884  6.731   -0.322  1.00 9.50  ? 6   TYR B CE1 1 
ATOM   2223 C  CE2 . TYR B 1 6   ? -0.659  5.672   1.473   1.00 8.50  ? 6   TYR B CE2 1 
ATOM   2224 C  CZ  . TYR B 1 6   ? -1.829  6.226   0.979   1.00 7.91  ? 6   TYR B CZ  1 
ATOM   2225 O  OH  . TYR B 1 6   ? -3.008  6.203   1.643   1.00 8.65  ? 6   TYR B OH  1 
ATOM   2226 N  N   . PHE B 1 7   ? 4.517   7.812   -2.798  1.00 14.47 ? 7   PHE B N   1 
ATOM   2227 C  CA  . PHE B 1 7   ? 5.786   7.477   -3.421  1.00 18.32 ? 7   PHE B CA  1 
ATOM   2228 C  C   . PHE B 1 7   ? 6.506   8.756   -3.797  1.00 18.60 ? 7   PHE B C   1 
ATOM   2229 O  O   . PHE B 1 7   ? 5.873   9.603   -4.415  1.00 20.21 ? 7   PHE B O   1 
ATOM   2230 C  CB  . PHE B 1 7   ? 5.589   6.691   -4.723  1.00 23.90 ? 7   PHE B CB  1 
ATOM   2231 C  CG  . PHE B 1 7   ? 6.880   6.368   -5.439  1.00 29.06 ? 7   PHE B CG  1 
ATOM   2232 C  CD1 . PHE B 1 7   ? 7.754   5.386   -4.956  1.00 32.38 ? 7   PHE B CD1 1 
ATOM   2233 C  CD2 . PHE B 1 7   ? 7.271   7.098   -6.562  1.00 34.86 ? 7   PHE B CD2 1 
ATOM   2234 C  CE1 . PHE B 1 7   ? 8.962   5.111   -5.591  1.00 33.51 ? 7   PHE B CE1 1 
ATOM   2235 C  CE2 . PHE B 1 7   ? 8.469   6.813   -7.207  1.00 39.54 ? 7   PHE B CE2 1 
ATOM   2236 C  CZ  . PHE B 1 7   ? 9.312   5.827   -6.720  1.00 40.29 ? 7   PHE B CZ  1 
ATOM   2237 N  N   . GLY B 1 8   ? 7.824   8.791   -3.573  1.00 20.10 ? 8   GLY B N   1 
ATOM   2238 C  CA  . GLY B 1 8   ? 8.638   9.921   -4.000  1.00 18.58 ? 8   GLY B CA  1 
ATOM   2239 C  C   . GLY B 1 8   ? 8.697   11.018  -2.944  1.00 19.33 ? 8   GLY B C   1 
ATOM   2240 O  O   . GLY B 1 8   ? 8.422   10.795  -1.759  1.00 17.82 ? 8   GLY B O   1 
ATOM   2241 N  N   A PRO B 1 9   ? 9.032   12.283  -3.279  0.50 17.86 ? 9   PRO B N   1 
ATOM   2242 N  N   B PRO B 1 9   ? 9.091   12.225  -3.386  0.50 18.90 ? 9   PRO B N   1 
ATOM   2243 C  CA  A PRO B 1 9   ? 9.325   13.301  -2.260  0.50 17.14 ? 9   PRO B CA  1 
ATOM   2244 C  CA  B PRO B 1 9   ? 9.297   13.371  -2.509  0.50 18.18 ? 9   PRO B CA  1 
ATOM   2245 C  C   A PRO B 1 9   ? 8.149   13.752  -1.408  0.50 16.15 ? 9   PRO B C   1 
ATOM   2246 C  C   B PRO B 1 9   ? 8.221   13.603  -1.467  0.50 16.43 ? 9   PRO B C   1 
ATOM   2247 O  O   A PRO B 1 9   ? 8.304   14.448  -0.397  0.50 15.87 ? 9   PRO B O   1 
ATOM   2248 O  O   B PRO B 1 9   ? 8.573   13.955  -0.347  0.50 17.32 ? 9   PRO B O   1 
ATOM   2249 C  CB  A PRO B 1 9   ? 9.804   14.526  -3.061  0.50 17.62 ? 9   PRO B CB  1 
ATOM   2250 C  CB  B PRO B 1 9   ? 9.446   14.572  -3.462  0.50 19.89 ? 9   PRO B CB  1 
ATOM   2251 C  CG  A PRO B 1 9   ? 10.143  13.946  -4.397  0.50 15.73 ? 9   PRO B CG  1 
ATOM   2252 C  CG  B PRO B 1 9   ? 9.015   14.015  -4.793  0.50 18.66 ? 9   PRO B CG  1 
ATOM   2253 C  CD  A PRO B 1 9   ? 9.185   12.804  -4.643  0.50 18.57 ? 9   PRO B CD  1 
ATOM   2254 C  CD  B PRO B 1 9   ? 9.403   12.550  -4.785  0.50 19.46 ? 9   PRO B CD  1 
ATOM   2255 N  N   . ASP B 1 10  ? 6.950   13.398  -1.867  1.00 15.21 ? 10  ASP B N   1 
ATOM   2256 C  CA  . ASP B 1 10  ? 5.780   13.759  -1.103  1.00 15.55 ? 10  ASP B CA  1 
ATOM   2257 C  C   . ASP B 1 10  ? 5.171   12.531  -0.403  1.00 12.78 ? 10  ASP B C   1 
ATOM   2258 O  O   . ASP B 1 10  ? 4.053   12.633  0.091   1.00 12.18 ? 10  ASP B O   1 
ATOM   2259 C  CB  . ASP B 1 10  ? 4.778   14.536  -1.967  1.00 18.66 ? 10  ASP B CB  1 
ATOM   2260 C  CG  . ASP B 1 10  ? 5.387   15.838  -2.496  1.00 23.83 ? 10  ASP B CG  1 
ATOM   2261 O  OD1 . ASP B 1 10  ? 5.983   16.565  -1.697  1.00 26.25 ? 10  ASP B OD1 1 
ATOM   2262 O  OD2 . ASP B 1 10  ? 5.301   16.074  -3.712  1.00 28.30 ? 10  ASP B OD2 1 
ATOM   2263 N  N   . GLY B 1 11  ? 5.964   11.449  -0.385  1.00 12.68 ? 11  GLY B N   1 
ATOM   2264 C  CA  . GLY B 1 11  ? 5.554   10.165  0.202   1.00 10.38 ? 11  GLY B CA  1 
ATOM   2265 C  C   . GLY B 1 11  ? 5.569   10.201  1.736   1.00 8.98  ? 11  GLY B C   1 
ATOM   2266 O  O   . GLY B 1 11  ? 5.778   11.223  2.392   1.00 8.55  ? 11  GLY B O   1 
ATOM   2267 N  N   . GLU B 1 12  ? 5.339   9.018   2.337   1.00 8.67  ? 12  GLU B N   1 
ATOM   2268 C  CA  . GLU B 1 12  ? 4.922   8.954   3.717   1.00 7.87  ? 12  GLU B CA  1 
ATOM   2269 C  C   . GLU B 1 12  ? 5.958   9.413   4.740   1.00 7.65  ? 12  GLU B C   1 
ATOM   2270 O  O   . GLU B 1 12  ? 5.588   9.869   5.804   1.00 7.97  ? 12  GLU B O   1 
ATOM   2271 C  CB  . GLU B 1 12  ? 4.487   7.527   4.087   1.00 8.63  ? 12  GLU B CB  1 
ATOM   2272 C  CG  . GLU B 1 12  ? 5.615   6.497   4.186   1.00 9.09  ? 12  GLU B CG  1 
ATOM   2273 C  CD  . GLU B 1 12  ? 4.975   5.123   4.128   1.00 8.64  ? 12  GLU B CD  1 
ATOM   2274 O  OE1 . GLU B 1 12  ? 4.611   4.647   5.209   1.00 8.73  ? 12  GLU B OE1 1 
ATOM   2275 O  OE2 . GLU B 1 12  ? 4.921   4.582   3.001   1.00 10.16 ? 12  GLU B OE2 1 
ATOM   2276 N  N   . ASN B 1 13  ? 7.270   9.343   4.388   1.00 8.29  ? 13  ASN B N   1 
ATOM   2277 C  CA  . ASN B 1 13  ? 8.266   9.842   5.337   1.00 8.65  ? 13  ASN B CA  1 
ATOM   2278 C  C   . ASN B 1 13  ? 8.300   11.371  5.391   1.00 9.24  ? 13  ASN B C   1 
ATOM   2279 O  O   . ASN B 1 13  ? 8.883   11.915  6.326   1.00 9.59  ? 13  ASN B O   1 
ATOM   2280 C  CB  . ASN B 1 13  ? 9.679   9.339   4.994   1.00 9.30  ? 13  ASN B CB  1 
ATOM   2281 C  CG  . ASN B 1 13  ? 9.830   7.850   5.256   1.00 8.94  ? 13  ASN B CG  1 
ATOM   2282 O  OD1 . ASN B 1 13  ? 8.920   7.178   5.737   1.00 9.60  ? 13  ASN B OD1 1 
ATOM   2283 N  ND2 . ASN B 1 13  ? 10.994  7.353   4.943   1.00 9.40  ? 13  ASN B ND2 1 
ATOM   2284 N  N   . SER B 1 14  ? 7.565   12.005  4.468   1.00 8.99  ? 14  SER B N   1 
ATOM   2285 C  CA  . SER B 1 14  ? 7.523   13.468  4.415   1.00 8.69  ? 14  SER B CA  1 
ATOM   2286 C  C   . SER B 1 14  ? 6.188   14.024  4.852   1.00 8.88  ? 14  SER B C   1 
ATOM   2287 O  O   . SER B 1 14  ? 6.044   15.250  4.973   1.00 8.90  ? 14  SER B O   1 
ATOM   2288 C  CB  . SER B 1 14  ? 7.800   13.938  3.037   1.00 8.94  ? 14  SER B CB  1 
ATOM   2289 O  OG  . SER B 1 14  ? 9.170   13.659  2.676   1.00 9.79  ? 14  SER B OG  1 
ATOM   2290 N  N   . TRP B 1 15  ? 5.171   13.196  5.107   1.00 8.09  ? 15  TRP B N   1 
ATOM   2291 C  CA  . TRP B 1 15  ? 3.848   13.725  5.432   1.00 7.80  ? 15  TRP B CA  1 
ATOM   2292 C  C   . TRP B 1 15  ? 3.908   14.624  6.647   1.00 9.15  ? 15  TRP B C   1 
ATOM   2293 O  O   . TRP B 1 15  ? 3.206   15.664  6.677   1.00 9.44  ? 15  TRP B O   1 
ATOM   2294 C  CB  . TRP B 1 15  ? 2.890   12.579  5.759   1.00 7.82  ? 15  TRP B CB  1 
ATOM   2295 C  CG  . TRP B 1 15  ? 2.496   11.705  4.626   1.00 8.07  ? 15  TRP B CG  1 
ATOM   2296 C  CD1 . TRP B 1 15  ? 2.775   11.877  3.310   1.00 8.59  ? 15  TRP B CD1 1 
ATOM   2297 C  CD2 . TRP B 1 15  ? 1.737   10.464  4.735   1.00 7.44  ? 15  TRP B CD2 1 
ATOM   2298 N  NE1 . TRP B 1 15  ? 2.232   10.835  2.562   1.00 8.10  ? 15  TRP B NE1 1 
ATOM   2299 C  CE2 . TRP B 1 15  ? 1.580   9.962   3.420   1.00 7.57  ? 15  TRP B CE2 1 
ATOM   2300 C  CE3 . TRP B 1 15  ? 1.151   9.774   5.829   1.00 7.93  ? 15  TRP B CE3 1 
ATOM   2301 C  CZ2 . TRP B 1 15  ? 0.858   8.779   3.147   1.00 7.91  ? 15  TRP B CZ2 1 
ATOM   2302 C  CZ3 . TRP B 1 15  ? 0.446   8.616   5.542   1.00 8.18  ? 15  TRP B CZ3 1 
ATOM   2303 C  CH2 . TRP B 1 15  ? 0.361   8.110   4.243   1.00 7.81  ? 15  TRP B CH2 1 
ATOM   2304 N  N   . SER B 1 16  ? 4.748   14.338  7.633   1.00 8.54  ? 16  SER B N   1 
ATOM   2305 C  CA  . SER B 1 16  ? 4.843   15.113  8.865   1.00 9.27  ? 16  SER B CA  1 
ATOM   2306 C  C   . SER B 1 16  ? 5.303   16.566  8.647   1.00 9.92  ? 16  SER B C   1 
ATOM   2307 O  O   . SER B 1 16  ? 5.096   17.394  9.542   1.00 11.71 ? 16  SER B O   1 
ATOM   2308 C  CB  . SER B 1 16  ? 5.752   14.430  9.870   1.00 11.12 ? 16  SER B CB  1 
ATOM   2309 O  OG  . SER B 1 16  ? 7.076   14.519  9.371   1.00 14.20 ? 16  SER B OG  1 
ATOM   2310 N  N   . LYS B 1 17  ? 5.937   16.826  7.492   1.00 9.79  ? 17  LYS B N   1 
ATOM   2311 C  CA  . LYS B 1 17  ? 6.383   18.186  7.168   1.00 10.30 ? 17  LYS B CA  1 
ATOM   2312 C  C   . LYS B 1 17  ? 5.174   19.106  7.105   1.00 11.76 ? 17  LYS B C   1 
ATOM   2313 O  O   . LYS B 1 17  ? 5.301   20.332  7.346   1.00 11.94 ? 17  LYS B O   1 
ATOM   2314 C  CB  . LYS B 1 17  ? 7.147   18.227  5.853   1.00 10.10 ? 17  LYS B CB  1 
ATOM   2315 C  CG  . LYS B 1 17  ? 8.434   17.397  5.826   1.00 11.07 ? 17  LYS B CG  1 
ATOM   2316 C  CD  . LYS B 1 17  ? 9.043   17.447  4.451   1.00 10.62 ? 17  LYS B CD  1 
ATOM   2317 C  CE  . LYS B 1 17  ? 10.191  16.464  4.272   1.00 10.42 ? 17  LYS B CE  1 
ATOM   2318 N  NZ  . LYS B 1 17  ? 10.841  16.566  2.966   1.00 10.98 ? 17  LYS B NZ  1 
ATOM   2319 N  N   . LYS B 1 18  ? 4.050   18.614  6.568   1.00 10.70 ? 18  LYS B N   1 
ATOM   2320 C  CA  . LYS B 1 18  ? 2.830   19.403  6.359   1.00 11.49 ? 18  LYS B CA  1 
ATOM   2321 C  C   . LYS B 1 18  ? 1.734   19.040  7.366   1.00 11.65 ? 18  LYS B C   1 
ATOM   2322 O  O   . LYS B 1 18  ? 0.820   19.825  7.590   1.00 13.21 ? 18  LYS B O   1 
ATOM   2323 C  CB  . LYS B 1 18  ? 2.326   19.195  4.941   1.00 12.58 ? 18  LYS B CB  1 
ATOM   2324 C  CG  . LYS B 1 18  ? 3.253   19.806  3.895   1.00 16.78 ? 18  LYS B CG  1 
ATOM   2325 C  CD  . LYS B 1 18  ? 2.761   19.536  2.478   1.00 20.25 ? 18  LYS B CD  1 
ATOM   2326 C  CE  . LYS B 1 18  ? 3.575   20.250  1.415   1.00 26.22 ? 18  LYS B CE  1 
ATOM   2327 N  NZ  . LYS B 1 18  ? 2.831   20.223  0.132   1.00 31.31 ? 18  LYS B NZ  1 
ATOM   2328 N  N   . TYR B 1 19  ? 1.758   17.806  7.915   1.00 9.87  ? 19  TYR B N   1 
ATOM   2329 C  CA  . TYR B 1 19  ? 0.669   17.252  8.700   1.00 10.64 ? 19  TYR B CA  1 
ATOM   2330 C  C   . TYR B 1 19  ? 1.269   16.783  10.000  1.00 10.85 ? 19  TYR B C   1 
ATOM   2331 O  O   . TYR B 1 19  ? 1.704   15.629  10.106  1.00 10.29 ? 19  TYR B O   1 
ATOM   2332 C  CB  . TYR B 1 19  ? 0.014   16.104  7.927   1.00 10.35 ? 19  TYR B CB  1 
ATOM   2333 C  CG  . TYR B 1 19  ? -0.590  16.524  6.628   1.00 10.40 ? 19  TYR B CG  1 
ATOM   2334 C  CD1 . TYR B 1 19  ? -1.797  17.202  6.620   1.00 11.79 ? 19  TYR B CD1 1 
ATOM   2335 C  CD2 . TYR B 1 19  ? 0.056   16.323  5.424   1.00 11.00 ? 19  TYR B CD2 1 
ATOM   2336 C  CE1 . TYR B 1 19  ? -2.360  17.534  5.409   1.00 12.44 ? 19  TYR B CE1 1 
ATOM   2337 C  CE2 . TYR B 1 19  ? -0.465  16.745  4.222   1.00 12.34 ? 19  TYR B CE2 1 
ATOM   2338 C  CZ  . TYR B 1 19  ? -1.713  17.334  4.220   1.00 14.07 ? 19  TYR B CZ  1 
ATOM   2339 O  OH  . TYR B 1 19  ? -2.208  17.703  2.981   1.00 17.13 ? 19  TYR B OH  1 
ATOM   2340 N  N   . PRO B 1 20  ? 1.441   17.644  11.013  1.00 10.82 ? 20  PRO B N   1 
ATOM   2341 C  CA  . PRO B 1 20  ? 2.213   17.284  12.188  1.00 12.70 ? 20  PRO B CA  1 
ATOM   2342 C  C   . PRO B 1 20  ? 1.738   16.011  12.882  1.00 10.65 ? 20  PRO B C   1 
ATOM   2343 O  O   . PRO B 1 20  ? 2.576   15.335  13.503  1.00 11.85 ? 20  PRO B O   1 
ATOM   2344 C  CB  . PRO B 1 20  ? 2.061   18.487  13.150  1.00 14.52 ? 20  PRO B CB  1 
ATOM   2345 C  CG  . PRO B 1 20  ? 1.777   19.609  12.206  1.00 15.71 ? 20  PRO B CG  1 
ATOM   2346 C  CD  . PRO B 1 20  ? 0.965   19.058  11.050  1.00 12.92 ? 20  PRO B CD  1 
ATOM   2347 N  N   . SER B 1 21  ? 0.434   15.701  12.879  1.00 9.75  ? 21  SER B N   1 
ATOM   2348 C  CA  . SER B 1 21  ? 0.007   14.505  13.606  1.00 9.91  ? 21  SER B CA  1 
ATOM   2349 C  C   . SER B 1 21  ? 0.563   13.227  12.944  1.00 9.72  ? 21  SER B C   1 
ATOM   2350 O  O   . SER B 1 21  ? 0.641   12.205  13.641  1.00 9.65  ? 21  SER B O   1 
ATOM   2351 C  CB  . SER B 1 21  ? -1.500  14.389  13.633  1.00 11.57 ? 21  SER B CB  1 
ATOM   2352 O  OG  . SER B 1 21  ? -2.030  15.450  14.427  1.00 13.21 ? 21  SER B OG  1 
ATOM   2353 N  N   . CYS B 1 22  ? 0.995   13.270  11.682  1.00 8.77  ? 22  CYS B N   1 
ATOM   2354 C  CA  . CYS B 1 22  ? 1.607   12.095  11.052  1.00 9.17  ? 22  CYS B CA  1 
ATOM   2355 C  C   . CYS B 1 22  ? 2.903   11.723  11.758  1.00 10.44 ? 22  CYS B C   1 
ATOM   2356 O  O   . CYS B 1 22  ? 3.381   10.614  11.524  1.00 10.64 ? 22  CYS B O   1 
ATOM   2357 C  CB  . CYS B 1 22  ? 1.784   12.307  9.543   1.00 8.69  ? 22  CYS B CB  1 
ATOM   2358 S  SG  . CYS B 1 22  ? 0.225   12.599  8.670   1.00 9.75  ? 22  CYS B SG  1 
ATOM   2359 N  N   . GLY B 1 23  ? 3.504   12.657  12.530  1.00 10.72 ? 23  GLY B N   1 
ATOM   2360 C  CA  . GLY B 1 23  ? 4.717   12.423  13.307  1.00 11.19 ? 23  GLY B CA  1 
ATOM   2361 C  C   . GLY B 1 23  ? 4.423   12.317  14.776  1.00 11.12 ? 23  GLY B C   1 
ATOM   2362 O  O   . GLY B 1 23  ? 5.379   12.324  15.576  1.00 13.54 ? 23  GLY B O   1 
ATOM   2363 N  N   . GLY B 1 24  ? 3.160   12.195  15.129  1.00 12.06 ? 24  GLY B N   1 
ATOM   2364 C  CA  . GLY B 1 24  ? 2.759   12.178  16.515  1.00 13.16 ? 24  GLY B CA  1 
ATOM   2365 C  C   . GLY B 1 24  ? 2.566   10.758  17.019  1.00 15.17 ? 24  GLY B C   1 
ATOM   2366 O  O   . GLY B 1 24  ? 3.079   9.804   16.457  1.00 17.31 ? 24  GLY B O   1 
ATOM   2367 N  N   . LEU B 1 25  ? 1.872   10.688  18.117  1.00 18.80 ? 25  LEU B N   1 
ATOM   2368 C  CA  . LEU B 1 25  ? 1.712   9.349   18.677  1.00 19.74 ? 25  LEU B CA  1 
ATOM   2369 C  C   . LEU B 1 25  ? 0.431   8.718   18.115  1.00 18.18 ? 25  LEU B C   1 
ATOM   2370 O  O   . LEU B 1 25  ? -0.368  9.328   17.382  1.00 16.00 ? 25  LEU B O   1 
ATOM   2371 C  CB  . LEU B 1 25  ? 1.765   9.420   20.211  1.00 25.38 ? 25  LEU B CB  1 
ATOM   2372 C  CG  . LEU B 1 25  ? 3.073   9.942   20.839  1.00 24.70 ? 25  LEU B CG  1 
ATOM   2373 C  CD1 . LEU B 1 25  ? 2.854   10.276  22.300  1.00 28.99 ? 25  LEU B CD1 1 
ATOM   2374 C  CD2 . LEU B 1 25  ? 4.234   8.960   20.679  1.00 29.95 ? 25  LEU B CD2 1 
ATOM   2375 N  N   . LEU B 1 26  ? 0.260   7.455   18.509  1.00 17.24 ? 26  LEU B N   1 
ATOM   2376 C  CA  . LEU B 1 26  ? -0.916  6.643   18.288  1.00 16.73 ? 26  LEU B CA  1 
ATOM   2377 C  C   . LEU B 1 26  ? -1.140  6.432   16.794  1.00 11.19 ? 26  LEU B C   1 
ATOM   2378 O  O   . LEU B 1 26  ? -2.295  6.320   16.378  1.00 11.87 ? 26  LEU B O   1 
ATOM   2379 C  CB  . LEU B 1 26  ? -2.167  7.227   18.946  1.00 17.19 ? 26  LEU B CB  1 
ATOM   2380 C  CG  . LEU B 1 26  ? -2.149  7.374   20.484  1.00 23.28 ? 26  LEU B CG  1 
ATOM   2381 C  CD1 . LEU B 1 26  ? -3.255  8.307   20.943  1.00 30.22 ? 26  LEU B CD1 1 
ATOM   2382 C  CD2 . LEU B 1 26  ? -2.315  6.035   21.155  1.00 25.26 ? 26  LEU B CD2 1 
ATOM   2383 N  N   . GLN B 1 27  ? -0.085  6.219   16.011  1.00 10.59 ? 27  GLN B N   1 
ATOM   2384 C  CA  . GLN B 1 27  ? -0.262  6.130   14.565  1.00 9.61  ? 27  GLN B CA  1 
ATOM   2385 C  C   . GLN B 1 27  ? -0.618  4.717   14.117  1.00 8.74  ? 27  GLN B C   1 
ATOM   2386 O  O   . GLN B 1 27  ? -0.223  3.688   14.712  1.00 9.84  ? 27  GLN B O   1 
ATOM   2387 C  CB  . GLN B 1 27  ? 0.978   6.628   13.829  1.00 8.75  ? 27  GLN B CB  1 
ATOM   2388 C  CG  . GLN B 1 27  ? 1.218   8.126   14.065  1.00 9.45  ? 27  GLN B CG  1 
ATOM   2389 C  CD  . GLN B 1 27  ? 0.145   8.955   13.391  1.00 7.84  ? 27  GLN B CD  1 
ATOM   2390 O  OE1 . GLN B 1 27  ? 0.149   9.074   12.159  1.00 9.26  ? 27  GLN B OE1 1 
ATOM   2391 N  NE2 . GLN B 1 27  ? -0.799  9.483   14.150  1.00 9.12  ? 27  GLN B NE2 1 
ATOM   2392 N  N   . SER B 1 28  ? -1.418  4.689   13.061  1.00 7.71  ? 28  SER B N   1 
ATOM   2393 C  CA  . SER B 1 28  ? -1.794  3.465   12.376  1.00 6.99  ? 28  SER B CA  1 
ATOM   2394 C  C   . SER B 1 28  ? -1.238  3.443   10.970  1.00 8.13  ? 28  SER B C   1 
ATOM   2395 O  O   . SER B 1 28  ? -0.970  4.523   10.397  1.00 8.52  ? 28  SER B O   1 
ATOM   2396 C  CB  . SER B 1 28  ? -3.307  3.438   12.315  1.00 7.93  ? 28  SER B CB  1 
ATOM   2397 O  OG  . SER B 1 28  ? -3.831  3.310   13.624  1.00 7.93  ? 28  SER B OG  1 
ATOM   2398 N  N   . PRO B 1 29  ? -1.112  2.323   10.270  1.00 6.84  ? 29  PRO B N   1 
ATOM   2399 C  CA  . PRO B 1 29  ? -1.468  0.976   10.785  1.00 7.83  ? 29  PRO B CA  1 
ATOM   2400 C  C   . PRO B 1 29  ? -0.330  0.356   11.569  1.00 7.66  ? 29  PRO B C   1 
ATOM   2401 O  O   . PRO B 1 29  ? 0.718   0.973   11.755  1.00 8.13  ? 29  PRO B O   1 
ATOM   2402 C  CB  . PRO B 1 29  ? -1.680  0.246   9.433   1.00 7.70  ? 29  PRO B CB  1 
ATOM   2403 C  CG  . PRO B 1 29  ? -0.530  0.791   8.558   1.00 7.73  ? 29  PRO B CG  1 
ATOM   2404 C  CD  . PRO B 1 29  ? -0.642  2.268   8.872   1.00 8.12  ? 29  PRO B CD  1 
ATOM   2405 N  N   . ILE B 1 30  ? -0.560  -0.878  12.039  1.00 7.61  ? 30  ILE B N   1 
ATOM   2406 C  CA  . ILE B 1 30  ? 0.410   -1.589  12.883  1.00 7.74  ? 30  ILE B CA  1 
ATOM   2407 C  C   . ILE B 1 30  ? 0.420   -3.043  12.445  1.00 7.98  ? 30  ILE B C   1 
ATOM   2408 O  O   . ILE B 1 30  ? -0.459  -3.535  11.755  1.00 8.11  ? 30  ILE B O   1 
ATOM   2409 C  CB  . ILE B 1 30  ? 0.081   -1.461  14.388  1.00 8.49  ? 30  ILE B CB  1 
ATOM   2410 C  CG1 . ILE B 1 30  ? -1.328  -2.027  14.688  1.00 9.44  ? 30  ILE B CG1 1 
ATOM   2411 C  CG2 . ILE B 1 30  ? 0.290   -0.002  14.858  1.00 10.22 ? 30  ILE B CG2 1 
ATOM   2412 C  CD1 . ILE B 1 30  ? -1.617  -2.154  16.172  1.00 11.35 ? 30  ILE B CD1 1 
ATOM   2413 N  N   . ASP B 1 31  ? 1.515   -3.703  12.859  1.00 8.22  ? 31  ASP B N   1 
ATOM   2414 C  CA  . ASP B 1 31  ? 1.666   -5.135  12.716  1.00 9.06  ? 31  ASP B CA  1 
ATOM   2415 C  C   . ASP B 1 31  ? 1.045   -5.829  13.920  1.00 10.27 ? 31  ASP B C   1 
ATOM   2416 O  O   . ASP B 1 31  ? 1.429   -5.608  15.055  1.00 11.80 ? 31  ASP B O   1 
ATOM   2417 C  CB  . ASP B 1 31  ? 3.144   -5.512  12.629  1.00 9.98  ? 31  ASP B CB  1 
ATOM   2418 C  CG  . ASP B 1 31  ? 3.267   -7.037  12.493  1.00 11.32 ? 31  ASP B CG  1 
ATOM   2419 O  OD1 . ASP B 1 31  ? 2.729   -7.654  11.553  1.00 12.12 ? 31  ASP B OD1 1 
ATOM   2420 O  OD2 . ASP B 1 31  ? 3.967   -7.619  13.360  1.00 15.83 ? 31  ASP B OD2 1 
ATOM   2421 N  N   . LEU B 1 32  ? 0.121   -6.708  13.618  1.00 10.12 ? 32  LEU B N   1 
ATOM   2422 C  CA  . LEU B 1 32  ? -0.585  -7.453  14.658  1.00 10.85 ? 32  LEU B CA  1 
ATOM   2423 C  C   . LEU B 1 32  ? 0.180   -8.734  14.942  1.00 12.10 ? 32  LEU B C   1 
ATOM   2424 O  O   . LEU B 1 32  ? 0.168   -9.626  14.113  1.00 13.46 ? 32  LEU B O   1 
ATOM   2425 C  CB  . LEU B 1 32  ? -2.004  -7.781  14.190  1.00 11.49 ? 32  LEU B CB  1 
ATOM   2426 C  CG  . LEU B 1 32  ? -2.809  -6.548  13.778  1.00 13.73 ? 32  LEU B CG  1 
ATOM   2427 C  CD1 . LEU B 1 32  ? -4.090  -6.928  13.023  1.00 13.64 ? 32  LEU B CD1 1 
ATOM   2428 C  CD2 . LEU B 1 32  ? -3.140  -5.659  14.965  1.00 15.69 ? 32  LEU B CD2 1 
ATOM   2429 N  N   . HIS B 1 33  ? 0.899   -8.793  16.085  1.00 11.26 ? 33  HIS B N   1 
ATOM   2430 C  CA  . HIS B 1 33  ? 1.716   -9.974  16.362  1.00 12.36 ? 33  HIS B CA  1 
ATOM   2431 C  C   . HIS B 1 33  ? 1.578   -10.276 17.850  1.00 10.66 ? 33  HIS B C   1 
ATOM   2432 O  O   . HIS B 1 33  ? 1.273   -9.433  18.676  1.00 11.44 ? 33  HIS B O   1 
ATOM   2433 C  CB  . HIS B 1 33  ? 3.213   -9.735  15.975  1.00 14.03 ? 33  HIS B CB  1 
ATOM   2434 C  CG  . HIS B 1 33  ? 3.886   -8.591  16.685  1.00 14.89 ? 33  HIS B CG  1 
ATOM   2435 N  ND1 . HIS B 1 33  ? 3.628   -7.263  16.398  1.00 17.96 ? 33  HIS B ND1 1 
ATOM   2436 C  CD2 . HIS B 1 33  ? 4.825   -8.554  17.681  1.00 15.13 ? 33  HIS B CD2 1 
ATOM   2437 C  CE1 . HIS B 1 33  ? 4.330   -6.452  17.185  1.00 20.66 ? 33  HIS B CE1 1 
ATOM   2438 N  NE2 . HIS B 1 33  ? 5.075   -7.247  17.977  1.00 17.29 ? 33  HIS B NE2 1 
ATOM   2439 N  N   . SER B 1 34  ? 1.959   -11.527 18.181  1.00 12.89 ? 34  SER B N   1 
ATOM   2440 C  CA  . SER B 1 34  ? 1.624   -12.113 19.482  1.00 13.61 ? 34  SER B CA  1 
ATOM   2441 C  C   . SER B 1 34  ? 2.109   -11.268 20.658  1.00 12.19 ? 34  SER B C   1 
ATOM   2442 O  O   . SER B 1 34  ? 1.412   -11.137 21.668  1.00 12.58 ? 34  SER B O   1 
ATOM   2443 C  CB  . SER B 1 34  ? 2.149   -13.513 19.552  1.00 15.94 ? 34  SER B CB  1 
ATOM   2444 O  OG  . SER B 1 34  ? 3.574   -13.475 19.563  1.00 19.53 ? 34  SER B OG  1 
ATOM   2445 N  N   . ASP B 1 35  ? 3.306   -10.666 20.620  1.00 12.73 ? 35  ASP B N   1 
ATOM   2446 C  CA  . ASP B 1 35  ? 3.860   -10.046 21.810  1.00 13.91 ? 35  ASP B CA  1 
ATOM   2447 C  C   . ASP B 1 35  ? 3.028   -8.864  22.285  1.00 14.66 ? 35  ASP B C   1 
ATOM   2448 O  O   . ASP B 1 35  ? 3.126   -8.427  23.444  1.00 16.80 ? 35  ASP B O   1 
ATOM   2449 C  CB  . ASP B 1 35  ? 5.274   -9.473  21.563  1.00 16.10 ? 35  ASP B CB  1 
ATOM   2450 C  CG  . ASP B 1 35  ? 6.191   -10.491 20.928  1.00 19.00 ? 35  ASP B CG  1 
ATOM   2451 O  OD1 . ASP B 1 35  ? 5.894   -10.907 19.783  1.00 18.55 ? 35  ASP B OD1 1 
ATOM   2452 O  OD2 . ASP B 1 35  ? 7.182   -10.924 21.602  1.00 18.20 ? 35  ASP B OD2 1 
ATOM   2453 N  N   . ILE B 1 36  ? 2.157   -8.310  21.408  1.00 12.73 ? 36  ILE B N   1 
ATOM   2454 C  CA  . ILE B 1 36  ? 1.435   -7.099  21.771  1.00 14.50 ? 36  ILE B CA  1 
ATOM   2455 C  C   . ILE B 1 36  ? -0.079  -7.359  21.825  1.00 13.26 ? 36  ILE B C   1 
ATOM   2456 O  O   . ILE B 1 36  ? -0.830  -6.401  21.980  1.00 14.46 ? 36  ILE B O   1 
ATOM   2457 C  CB  . ILE B 1 36  ? 1.744   -5.859  20.876  1.00 16.08 ? 36  ILE B CB  1 
ATOM   2458 C  CG1 . ILE B 1 36  ? 1.703   -6.163  19.381  1.00 18.89 ? 36  ILE B CG1 1 
ATOM   2459 C  CG2 . ILE B 1 36  ? 3.136   -5.338  21.183  1.00 19.20 ? 36  ILE B CG2 1 
ATOM   2460 C  CD1 . ILE B 1 36  ? 0.358   -6.337  18.815  1.00 19.47 ? 36  ILE B CD1 1 
ATOM   2461 N  N   . LEU B 1 37  ? -0.486  -8.616  21.703  1.00 12.81 ? 37  LEU B N   1 
ATOM   2462 C  CA  . LEU B 1 37  ? -1.906  -8.990  21.732  1.00 13.76 ? 37  LEU B CA  1 
ATOM   2463 C  C   . LEU B 1 37  ? -2.298  -9.355  23.151  1.00 15.22 ? 37  LEU B C   1 
ATOM   2464 O  O   . LEU B 1 37  ? -1.558  -10.062 23.825  1.00 16.54 ? 37  LEU B O   1 
ATOM   2465 C  CB  . LEU B 1 37  ? -2.181  -10.182 20.816  1.00 14.90 ? 37  LEU B CB  1 
ATOM   2466 C  CG  . LEU B 1 37  ? -1.913  -9.932  19.330  1.00 14.10 ? 37  LEU B CG  1 
ATOM   2467 C  CD1 . LEU B 1 37  ? -2.166  -11.203 18.542  1.00 16.78 ? 37  LEU B CD1 1 
ATOM   2468 C  CD2 . LEU B 1 37  ? -2.744  -8.755  18.772  1.00 13.60 ? 37  LEU B CD2 1 
ATOM   2469 N  N   . GLN B 1 38  ? -3.523  -9.040  23.532  1.00 12.36 ? 38  GLN B N   1 
ATOM   2470 C  CA  . GLN B 1 38  ? -4.039  -9.505  24.825  1.00 14.12 ? 38  GLN B CA  1 
ATOM   2471 C  C   . GLN B 1 38  ? -5.545  -9.656  24.718  1.00 14.16 ? 38  GLN B C   1 
ATOM   2472 O  O   . GLN B 1 38  ? -6.260  -8.737  24.315  1.00 11.87 ? 38  GLN B O   1 
ATOM   2473 C  CB  . GLN B 1 38  ? -3.798  -8.468  25.909  1.00 17.70 ? 38  GLN B CB  1 
ATOM   2474 C  CG  . GLN B 1 38  ? -4.206  -8.926  27.312  1.00 20.51 ? 38  GLN B CG  1 
ATOM   2475 C  CD  . GLN B 1 38  ? -3.693  -7.924  28.315  1.00 25.99 ? 38  GLN B CD  1 
ATOM   2476 O  OE1 . GLN B 1 38  ? -2.484  -7.811  28.519  1.00 33.54 ? 38  GLN B OE1 1 
ATOM   2477 N  NE2 . GLN B 1 38  ? -4.599  -7.163  28.899  1.00 28.80 ? 38  GLN B NE2 1 
ATOM   2478 N  N   . TYR B 1 39  ? -6.026  -10.817 25.103  1.00 12.52 ? 39  TYR B N   1 
ATOM   2479 C  CA  . TYR B 1 39  ? -7.434  -11.131 25.097  1.00 12.06 ? 39  TYR B CA  1 
ATOM   2480 C  C   . TYR B 1 39  ? -8.159  -10.203 26.076  1.00 11.72 ? 39  TYR B C   1 
ATOM   2481 O  O   . TYR B 1 39  ? -7.698  -9.920  27.198  1.00 13.67 ? 39  TYR B O   1 
ATOM   2482 C  CB  . TYR B 1 39  ? -7.588  -12.573 25.585  1.00 12.41 ? 39  TYR B CB  1 
ATOM   2483 C  CG  . TYR B 1 39  ? -9.017  -12.988 25.757  1.00 12.12 ? 39  TYR B CG  1 
ATOM   2484 C  CD1 . TYR B 1 39  ? -9.925  -12.927 24.720  1.00 12.55 ? 39  TYR B CD1 1 
ATOM   2485 C  CD2 . TYR B 1 39  ? -9.503  -13.414 26.996  1.00 14.35 ? 39  TYR B CD2 1 
ATOM   2486 C  CE1 . TYR B 1 39  ? -11.252 -13.308 24.838  1.00 13.92 ? 39  TYR B CE1 1 
ATOM   2487 C  CE2 . TYR B 1 39  ? -10.816 -13.818 27.128  1.00 15.07 ? 39  TYR B CE2 1 
ATOM   2488 C  CZ  . TYR B 1 39  ? -11.711 -13.744 26.077  1.00 14.31 ? 39  TYR B CZ  1 
ATOM   2489 O  OH  . TYR B 1 39  ? -13.021 -14.076 26.235  1.00 18.01 ? 39  TYR B OH  1 
ATOM   2490 N  N   . ASP B 1 40  ? -9.334  -9.724  25.655  1.00 11.33 ? 40  ASP B N   1 
ATOM   2491 C  CA  . ASP B 1 40  ? -10.154 -8.880  26.504  1.00 13.51 ? 40  ASP B CA  1 
ATOM   2492 C  C   . ASP B 1 40  ? -11.569 -9.382  26.402  1.00 13.64 ? 40  ASP B C   1 
ATOM   2493 O  O   . ASP B 1 40  ? -12.228 -9.172  25.391  1.00 11.92 ? 40  ASP B O   1 
ATOM   2494 C  CB  . ASP B 1 40  ? -10.013 -7.411  26.078  1.00 13.73 ? 40  ASP B CB  1 
ATOM   2495 C  CG  . ASP B 1 40  ? -10.807 -6.439  26.913  1.00 15.92 ? 40  ASP B CG  1 
ATOM   2496 O  OD1 . ASP B 1 40  ? -11.635 -6.883  27.700  1.00 16.30 ? 40  ASP B OD1 1 
ATOM   2497 O  OD2 . ASP B 1 40  ? -10.635 -5.230  26.679  1.00 19.48 ? 40  ASP B OD2 1 
ATOM   2498 N  N   . ALA B 1 41  ? -12.097 -9.996  27.474  1.00 14.77 ? 41  ALA B N   1 
ATOM   2499 C  CA  . ALA B 1 41  ? -13.406 -10.618 27.428  1.00 15.78 ? 41  ALA B CA  1 
ATOM   2500 C  C   . ALA B 1 41  ? -14.533 -9.597  27.324  1.00 15.25 ? 41  ALA B C   1 
ATOM   2501 O  O   . ALA B 1 41  ? -15.659 -9.955  26.984  1.00 16.99 ? 41  ALA B O   1 
ATOM   2502 C  CB  . ALA B 1 41  ? -13.545 -11.505 28.664  1.00 16.63 ? 41  ALA B CB  1 
ATOM   2503 N  N   . SER B 1 42  ? -14.213 -8.316  27.538  1.00 16.00 ? 42  SER B N   1 
ATOM   2504 C  CA  . SER B 1 42  ? -15.230 -7.272  27.403  1.00 16.46 ? 42  SER B CA  1 
ATOM   2505 C  C   . SER B 1 42  ? -15.481 -6.849  25.950  1.00 17.22 ? 42  SER B C   1 
ATOM   2506 O  O   . SER B 1 42  ? -16.371 -6.042  25.660  1.00 18.18 ? 42  SER B O   1 
ATOM   2507 C  CB  . SER B 1 42  ? -14.897 -6.054  28.246  1.00 21.34 ? 42  SER B CB  1 
ATOM   2508 O  OG  . SER B 1 42  ? -13.852 -5.273  27.674  1.00 26.13 ? 42  SER B OG  1 
ATOM   2509 N  N   . LEU B 1 43  ? -14.736 -7.416  25.011  1.00 13.66 ? 43  LEU B N   1 
ATOM   2510 C  CA  . LEU B 1 43  ? -14.933 -7.085  23.600  1.00 13.64 ? 43  LEU B CA  1 
ATOM   2511 C  C   . LEU B 1 43  ? -16.030 -7.954  23.019  1.00 13.54 ? 43  LEU B C   1 
ATOM   2512 O  O   . LEU B 1 43  ? -15.775 -8.971  22.387  1.00 14.58 ? 43  LEU B O   1 
ATOM   2513 C  CB  . LEU B 1 43  ? -13.624 -7.250  22.845  1.00 12.48 ? 43  LEU B CB  1 
ATOM   2514 C  CG  . LEU B 1 43  ? -12.553 -6.235  23.228  1.00 11.91 ? 43  LEU B CG  1 
ATOM   2515 C  CD1 . LEU B 1 43  ? -11.276 -6.508  22.469  1.00 13.17 ? 43  LEU B CD1 1 
ATOM   2516 C  CD2 . LEU B 1 43  ? -12.946 -4.792  22.939  1.00 13.08 ? 43  LEU B CD2 1 
ATOM   2517 N  N   . THR B 1 44  ? -17.275 -7.520  23.261  1.00 14.70 ? 44  THR B N   1 
ATOM   2518 C  CA  . THR B 1 44  ? -18.447 -8.244  22.840  1.00 16.43 ? 44  THR B CA  1 
ATOM   2519 C  C   . THR B 1 44  ? -18.752 -7.964  21.373  1.00 13.25 ? 44  THR B C   1 
ATOM   2520 O  O   . THR B 1 44  ? -18.127 -7.074  20.755  1.00 13.06 ? 44  THR B O   1 
ATOM   2521 C  CB  . THR B 1 44  ? -19.609 -7.838  23.768  1.00 17.07 ? 44  THR B CB  1 
ATOM   2522 O  OG1 . THR B 1 44  ? -19.613 -6.426  23.872  1.00 20.97 ? 44  THR B OG1 1 
ATOM   2523 C  CG2 . THR B 1 44  ? -19.374 -8.306  25.196  1.00 20.39 ? 44  THR B CG2 1 
ATOM   2524 N  N   . PRO B 1 45  ? -19.649 -8.721  20.721  1.00 13.95 ? 45  PRO B N   1 
ATOM   2525 C  CA  . PRO B 1 45  ? -19.865 -8.571  19.273  1.00 13.81 ? 45  PRO B CA  1 
ATOM   2526 C  C   . PRO B 1 45  ? -20.510 -7.240  18.886  1.00 13.62 ? 45  PRO B C   1 
ATOM   2527 O  O   . PRO B 1 45  ? -21.287 -6.619  19.627  1.00 16.38 ? 45  PRO B O   1 
ATOM   2528 C  CB  . PRO B 1 45  ? -20.772 -9.741  18.904  1.00 17.35 ? 45  PRO B CB  1 
ATOM   2529 C  CG  . PRO B 1 45  ? -20.476 -10.768 20.023  1.00 16.43 ? 45  PRO B CG  1 
ATOM   2530 C  CD  . PRO B 1 45  ? -20.355 -9.905  21.267  1.00 14.82 ? 45  PRO B CD  1 
ATOM   2531 N  N   . LEU B 1 46  ? -20.064 -6.712  17.738  1.00 12.29 ? 46  LEU B N   1 
ATOM   2532 C  CA  . LEU B 1 46  ? -20.741 -5.532  17.206  1.00 12.98 ? 46  LEU B CA  1 
ATOM   2533 C  C   . LEU B 1 46  ? -21.949 -6.006  16.416  1.00 13.35 ? 46  LEU B C   1 
ATOM   2534 O  O   . LEU B 1 46  ? -21.992 -7.105  15.900  1.00 14.41 ? 46  LEU B O   1 
ATOM   2535 C  CB  . LEU B 1 46  ? -19.781 -4.817  16.246  1.00 13.89 ? 46  LEU B CB  1 
ATOM   2536 C  CG  . LEU B 1 46  ? -18.528 -4.237  16.873  1.00 16.11 ? 46  LEU B CG  1 
ATOM   2537 C  CD1 . LEU B 1 46  ? -17.683 -3.597  15.782  1.00 18.03 ? 46  LEU B CD1 1 
ATOM   2538 C  CD2 . LEU B 1 46  ? -18.870 -3.213  17.932  1.00 19.76 ? 46  LEU B CD2 1 
ATOM   2539 N  N   . GLU B 1 47  ? -22.926 -5.116  16.345  1.00 15.35 ? 47  GLU B N   1 
ATOM   2540 C  CA  . GLU B 1 47  ? -24.001 -5.377  15.395  1.00 15.96 ? 47  GLU B CA  1 
ATOM   2541 C  C   . GLU B 1 47  ? -24.003 -4.270  14.326  1.00 14.24 ? 47  GLU B C   1 
ATOM   2542 O  O   . GLU B 1 47  ? -23.709 -3.097  14.635  1.00 16.79 ? 47  GLU B O   1 
ATOM   2543 C  CB  . GLU B 1 47  ? -25.371 -5.401  16.090  1.00 20.85 ? 47  GLU B CB  1 
ATOM   2544 C  CG  . GLU B 1 47  ? -25.485 -6.485  17.165  1.00 25.06 ? 47  GLU B CG  1 
ATOM   2545 C  CD  . GLU B 1 47  ? -26.833 -6.544  17.879  1.00 35.36 ? 47  GLU B CD  1 
ATOM   2546 O  OE1 . GLU B 1 47  ? -27.205 -5.552  18.545  1.00 39.96 ? 47  GLU B OE1 1 
ATOM   2547 O  OE2 . GLU B 1 47  ? -27.523 -7.580  17.752  1.00 43.10 ? 47  GLU B OE2 1 
ATOM   2548 N  N   . PHE B 1 48  ? -24.295 -4.712  13.116  1.00 15.14 ? 48  PHE B N   1 
ATOM   2549 C  CA  . PHE B 1 48  ? -24.225 -3.854  11.939  1.00 14.05 ? 48  PHE B CA  1 
ATOM   2550 C  C   . PHE B 1 48  ? -25.644 -3.531  11.486  1.00 16.83 ? 48  PHE B C   1 
ATOM   2551 O  O   . PHE B 1 48  ? -26.330 -4.443  11.026  1.00 18.60 ? 48  PHE B O   1 
ATOM   2552 C  CB  . PHE B 1 48  ? -23.415 -4.530  10.828  1.00 16.31 ? 48  PHE B CB  1 
ATOM   2553 C  CG  . PHE B 1 48  ? -22.117 -5.069  11.368  1.00 15.31 ? 48  PHE B CG  1 
ATOM   2554 C  CD1 . PHE B 1 48  ? -21.082 -4.217  11.686  1.00 14.07 ? 48  PHE B CD1 1 
ATOM   2555 C  CD2 . PHE B 1 48  ? -21.953 -6.440  11.599  1.00 16.04 ? 48  PHE B CD2 1 
ATOM   2556 C  CE1 . PHE B 1 48  ? -19.914 -4.707  12.284  1.00 15.13 ? 48  PHE B CE1 1 
ATOM   2557 C  CE2 . PHE B 1 48  ? -20.778 -6.918  12.166  1.00 17.37 ? 48  PHE B CE2 1 
ATOM   2558 C  CZ  . PHE B 1 48  ? -19.759 -6.059  12.486  1.00 15.60 ? 48  PHE B CZ  1 
ATOM   2559 N  N   . GLN B 1 49  ? -26.052 -2.273  11.718  1.00 13.47 ? 49  GLN B N   1 
ATOM   2560 C  CA  . GLN B 1 49  ? -27.448 -1.901  11.534  1.00 14.19 ? 49  GLN B CA  1 
ATOM   2561 C  C   . GLN B 1 49  ? -27.576 -1.018  10.304  1.00 12.35 ? 49  GLN B C   1 
ATOM   2562 O  O   . GLN B 1 49  ? -26.810 -0.079  10.127  1.00 12.58 ? 49  GLN B O   1 
ATOM   2563 C  CB  . GLN B 1 49  ? -27.944 -1.107  12.746  1.00 17.48 ? 49  GLN B CB  1 
ATOM   2564 C  CG  . GLN B 1 49  ? -27.635 -1.767  14.083  1.00 25.64 ? 49  GLN B CG  1 
ATOM   2565 C  CD  . GLN B 1 49  ? -28.655 -2.747  14.607  1.00 39.73 ? 49  GLN B CD  1 
ATOM   2566 O  OE1 . GLN B 1 49  ? -28.543 -3.221  15.743  1.00 46.02 ? 49  GLN B OE1 1 
ATOM   2567 N  NE2 . GLN B 1 49  ? -29.668 -3.042  13.803  1.00 37.55 ? 49  GLN B NE2 1 
ATOM   2568 N  N   . GLY B 1 50  ? -28.567 -1.291  9.458   1.00 11.91 ? 50  GLY B N   1 
ATOM   2569 C  CA  . GLY B 1 50  ? -28.787 -0.442  8.293   1.00 11.94 ? 50  GLY B CA  1 
ATOM   2570 C  C   . GLY B 1 50  ? -27.722 -0.641  7.226   1.00 12.14 ? 50  GLY B C   1 
ATOM   2571 O  O   . GLY B 1 50  ? -27.661 0.161   6.287   1.00 13.85 ? 50  GLY B O   1 
ATOM   2572 N  N   . TYR B 1 51  ? -26.974 -1.745  7.296   1.00 10.63 ? 51  TYR B N   1 
ATOM   2573 C  CA  . TYR B 1 51  ? -25.992 -2.056  6.257   1.00 10.18 ? 51  TYR B CA  1 
ATOM   2574 C  C   . TYR B 1 51  ? -26.581 -2.578  4.955   1.00 10.19 ? 51  TYR B C   1 
ATOM   2575 O  O   . TYR B 1 51  ? -25.935 -2.590  3.928   1.00 9.44  ? 51  TYR B O   1 
ATOM   2576 C  CB  . TYR B 1 51  ? -24.975 -3.088  6.808   1.00 10.07 ? 51  TYR B CB  1 
ATOM   2577 C  CG  . TYR B 1 51  ? -23.783 -2.534  7.558   1.00 9.20  ? 51  TYR B CG  1 
ATOM   2578 C  CD1 . TYR B 1 51  ? -23.895 -1.577  8.550   1.00 9.49  ? 51  TYR B CD1 1 
ATOM   2579 C  CD2 . TYR B 1 51  ? -22.496 -3.009  7.254   1.00 9.68  ? 51  TYR B CD2 1 
ATOM   2580 C  CE1 . TYR B 1 51  ? -22.826 -1.037  9.246   1.00 10.62 ? 51  TYR B CE1 1 
ATOM   2581 C  CE2 . TYR B 1 51  ? -21.409 -2.488  7.951   1.00 10.17 ? 51  TYR B CE2 1 
ATOM   2582 C  CZ  . TYR B 1 51  ? -21.560 -1.474  8.877   1.00 10.69 ? 51  TYR B CZ  1 
ATOM   2583 O  OH  . TYR B 1 51  ? -20.446 -0.963  9.501   1.00 12.05 ? 51  TYR B OH  1 
ATOM   2584 N  N   . ASN B 1 52  ? -27.849 -3.075  5.012   1.00 10.91 ? 52  ASN B N   1 
ATOM   2585 C  CA  . ASN B 1 52  ? -28.477 -3.624  3.824   1.00 10.85 ? 52  ASN B CA  1 
ATOM   2586 C  C   . ASN B 1 52  ? -29.093 -2.504  2.988   1.00 13.39 ? 52  ASN B C   1 
ATOM   2587 O  O   . ASN B 1 52  ? -30.245 -2.116  3.217   1.00 14.93 ? 52  ASN B O   1 
ATOM   2588 C  CB  . ASN B 1 52  ? -29.517 -4.695  4.217   1.00 13.26 ? 52  ASN B CB  1 
ATOM   2589 C  CG  . ASN B 1 52  ? -30.109 -5.382  3.036   1.00 18.41 ? 52  ASN B CG  1 
ATOM   2590 O  OD1 . ASN B 1 52  ? -29.665 -5.208  1.915   1.00 23.16 ? 52  ASN B OD1 1 
ATOM   2591 N  ND2 . ASN B 1 52  ? -31.147 -6.179  3.299   1.00 22.36 ? 52  ASN B ND2 1 
ATOM   2592 N  N   . LEU B 1 53  ? -28.275 -1.864  2.148   1.00 11.65 ? 53  LEU B N   1 
ATOM   2593 C  CA  . LEU B 1 53  ? -28.746 -0.675  1.435   1.00 11.05 ? 53  LEU B CA  1 
ATOM   2594 C  C   . LEU B 1 53  ? -29.665 -1.113  0.281   1.00 9.78  ? 53  LEU B C   1 
ATOM   2595 O  O   . LEU B 1 53  ? -29.401 -2.076  -0.434  1.00 11.76 ? 53  LEU B O   1 
ATOM   2596 C  CB  . LEU B 1 53  ? -27.564 0.095   0.849   1.00 10.78 ? 53  LEU B CB  1 
ATOM   2597 C  CG  . LEU B 1 53  ? -26.457 0.470   1.832   1.00 12.65 ? 53  LEU B CG  1 
ATOM   2598 C  CD1 . LEU B 1 53  ? -25.339 1.169   1.053   1.00 13.76 ? 53  LEU B CD1 1 
ATOM   2599 C  CD2 . LEU B 1 53  ? -26.986 1.330   2.958   1.00 14.11 ? 53  LEU B CD2 1 
ATOM   2600 N  N   . SER B 1 54  ? -30.713 -0.289  0.098   1.00 10.14 ? 54  SER B N   1 
ATOM   2601 C  CA  . SER B 1 54  ? -31.663 -0.652  -0.935  1.00 11.72 ? 54  SER B CA  1 
ATOM   2602 C  C   . SER B 1 54  ? -30.979 -0.657  -2.310  1.00 10.71 ? 54  SER B C   1 
ATOM   2603 O  O   . SER B 1 54  ? -30.436 0.360   -2.729  1.00 10.30 ? 54  SER B O   1 
ATOM   2604 C  CB  . SER B 1 54  ? -32.778 0.325   -0.907  1.00 11.75 ? 54  SER B CB  1 
ATOM   2605 O  OG  . SER B 1 54  ? -33.671 -0.028  -1.966  1.00 12.66 ? 54  SER B OG  1 
ATOM   2606 N  N   . ALA B 1 55  ? -31.260 -1.692  -3.121  1.00 11.63 ? 55  ALA B N   1 
ATOM   2607 C  CA  . ALA B 1 55  ? -30.789 -1.763  -4.504  1.00 13.08 ? 55  ALA B CA  1 
ATOM   2608 C  C   . ALA B 1 55  ? -31.488 -0.739  -5.387  1.00 12.20 ? 55  ALA B C   1 
ATOM   2609 O  O   . ALA B 1 55  ? -31.030 -0.480  -6.507  1.00 14.07 ? 55  ALA B O   1 
ATOM   2610 C  CB  . ALA B 1 55  ? -30.944 -3.160  -5.089  1.00 15.63 ? 55  ALA B CB  1 
ATOM   2611 N  N   . ASN B 1 56  ? -32.584 -0.164  -4.907  1.00 11.48 ? 56  ASN B N   1 
ATOM   2612 C  CA  . ASN B 1 56  ? -33.262 0.836   -5.727  1.00 11.99 ? 56  ASN B CA  1 
ATOM   2613 C  C   . ASN B 1 56  ? -32.752 2.235   -5.435  1.00 12.20 ? 56  ASN B C   1 
ATOM   2614 O  O   . ASN B 1 56  ? -33.108 3.221   -6.134  1.00 14.76 ? 56  ASN B O   1 
ATOM   2615 C  CB  . ASN B 1 56  ? -34.778 0.811   -5.495  1.00 12.27 ? 56  ASN B CB  1 
ATOM   2616 C  CG  . ASN B 1 56  ? -35.414 -0.456  -5.988  1.00 14.61 ? 56  ASN B CG  1 
ATOM   2617 O  OD1 . ASN B 1 56  ? -34.854 -1.237  -6.737  1.00 16.23 ? 56  ASN B OD1 1 
ATOM   2618 N  ND2 . ASN B 1 56  ? -36.649 -0.631  -5.593  1.00 18.02 ? 56  ASN B ND2 1 
ATOM   2619 N  N   . LYS B 1 57  ? -31.872 2.380   -4.429  1.00 11.44 ? 57  LYS B N   1 
ATOM   2620 C  CA  . LYS B 1 57  ? -31.180 3.628   -4.177  1.00 11.16 ? 57  LYS B CA  1 
ATOM   2621 C  C   . LYS B 1 57  ? -29.757 3.545   -4.709  1.00 11.11 ? 57  LYS B C   1 
ATOM   2622 O  O   . LYS B 1 57  ? -29.348 2.485   -5.171  1.00 10.92 ? 57  LYS B O   1 
ATOM   2623 C  CB  . LYS B 1 57  ? -31.104 3.867   -2.672  1.00 11.92 ? 57  LYS B CB  1 
ATOM   2624 C  CG  . LYS B 1 57  ? -32.433 4.350   -2.063  1.00 15.31 ? 57  LYS B CG  1 
ATOM   2625 C  CD  . LYS B 1 57  ? -32.278 4.608   -0.594  1.00 20.61 ? 57  LYS B CD  1 
ATOM   2626 C  CE  . LYS B 1 57  ? -33.374 5.466   -0.025  1.00 26.17 ? 57  LYS B CE  1 
ATOM   2627 N  NZ  . LYS B 1 57  ? -33.040 5.811   1.383   1.00 29.14 ? 57  LYS B NZ  1 
ATOM   2628 N  N   . GLN B 1 58  ? -29.126 4.700   -4.837  1.00 10.72 ? 58  GLN B N   1 
ATOM   2629 C  CA  . GLN B 1 58  ? -27.762 4.742   -5.347  1.00 11.03 ? 58  GLN B CA  1 
ATOM   2630 C  C   . GLN B 1 58  ? -26.886 5.625   -4.483  1.00 9.98  ? 58  GLN B C   1 
ATOM   2631 O  O   . GLN B 1 58  ? -27.304 6.573   -3.864  1.00 11.23 ? 58  GLN B O   1 
ATOM   2632 C  CB  . GLN B 1 58  ? -27.703 5.105   -6.820  1.00 16.55 ? 58  GLN B CB  1 
ATOM   2633 C  CG  . GLN B 1 58  ? -28.323 6.427   -7.140  1.00 17.98 ? 58  GLN B CG  1 
ATOM   2634 C  CD  . GLN B 1 58  ? -28.670 6.544   -8.612  1.00 23.30 ? 58  GLN B CD  1 
ATOM   2635 O  OE1 . GLN B 1 58  ? -28.453 5.647   -9.455  1.00 22.83 ? 58  GLN B OE1 1 
ATOM   2636 N  NE2 . GLN B 1 58  ? -29.217 7.706   -8.918  1.00 25.95 ? 58  GLN B NE2 1 
ATOM   2637 N  N   . PHE B 1 59  ? -25.606 5.261   -4.468  1.00 9.42  ? 59  PHE B N   1 
ATOM   2638 C  CA  . PHE B 1 59  ? -24.625 5.791   -3.544  1.00 8.99  ? 59  PHE B CA  1 
ATOM   2639 C  C   . PHE B 1 59  ? -23.409 6.246   -4.346  1.00 8.13  ? 59  PHE B C   1 
ATOM   2640 O  O   . PHE B 1 59  ? -23.018 5.598   -5.310  1.00 9.13  ? 59  PHE B O   1 
ATOM   2641 C  CB  . PHE B 1 59  ? -24.257 4.699   -2.517  1.00 10.60 ? 59  PHE B CB  1 
ATOM   2642 C  CG  . PHE B 1 59  ? -25.506 4.321   -1.763  1.00 10.01 ? 59  PHE B CG  1 
ATOM   2643 C  CD1 . PHE B 1 59  ? -26.388 3.341   -2.233  1.00 9.66  ? 59  PHE B CD1 1 
ATOM   2644 C  CD2 . PHE B 1 59  ? -25.834 5.053   -0.633  1.00 10.84 ? 59  PHE B CD2 1 
ATOM   2645 C  CE1 . PHE B 1 59  ? -27.590 3.129   -1.535  1.00 10.23 ? 59  PHE B CE1 1 
ATOM   2646 C  CE2 . PHE B 1 59  ? -27.059 4.839   0.026   1.00 11.18 ? 59  PHE B CE2 1 
ATOM   2647 C  CZ  . PHE B 1 59  ? -27.887 3.831   -0.411  1.00 10.67 ? 59  PHE B CZ  1 
ATOM   2648 N  N   . LEU B 1 60  ? -22.862 7.381   -3.951  1.00 8.99  ? 60  LEU B N   1 
ATOM   2649 C  CA  . LEU B 1 60  ? -21.834 8.004   -4.770  1.00 9.39  ? 60  LEU B CA  1 
ATOM   2650 C  C   . LEU B 1 60  ? -20.459 7.381   -4.522  1.00 9.75  ? 60  LEU B C   1 
ATOM   2651 O  O   . LEU B 1 60  ? -19.981 7.374   -3.386  1.00 10.53 ? 60  LEU B O   1 
ATOM   2652 C  CB  . LEU B 1 60  ? -21.838 9.472   -4.354  1.00 11.52 ? 60  LEU B CB  1 
ATOM   2653 C  CG  . LEU B 1 60  ? -20.990 10.376  -5.226  1.00 15.21 ? 60  LEU B CG  1 
ATOM   2654 C  CD1 . LEU B 1 60  ? -21.700 10.634  -6.528  1.00 16.99 ? 60  LEU B CD1 1 
ATOM   2655 C  CD2 . LEU B 1 60  ? -20.755 11.724  -4.511  1.00 19.32 ? 60  LEU B CD2 1 
ATOM   2656 N  N   . LEU B 1 61  ? -19.836 6.928   -5.598  1.00 9.98  ? 61  LEU B N   1 
ATOM   2657 C  CA  . LEU B 1 61  ? -18.456 6.449   -5.663  1.00 9.81  ? 61  LEU B CA  1 
ATOM   2658 C  C   . LEU B 1 61  ? -17.577 7.555   -6.214  1.00 11.11 ? 61  LEU B C   1 
ATOM   2659 O  O   . LEU B 1 61  ? -17.946 8.190   -7.213  1.00 12.23 ? 61  LEU B O   1 
ATOM   2660 C  CB  . LEU B 1 61  ? -18.475 5.220   -6.564  1.00 10.54 ? 61  LEU B CB  1 
ATOM   2661 C  CG  . LEU B 1 61  ? -17.166 4.418   -6.587  1.00 10.26 ? 61  LEU B CG  1 
ATOM   2662 C  CD1 . LEU B 1 61  ? -16.974 3.645   -5.275  1.00 12.18 ? 61  LEU B CD1 1 
ATOM   2663 C  CD2 . LEU B 1 61  ? -17.120 3.446   -7.790  1.00 11.57 ? 61  LEU B CD2 1 
ATOM   2664 N  N   . THR B 1 62  ? -16.438 7.827   -5.573  1.00 11.41 ? 62  THR B N   1 
ATOM   2665 C  CA  . THR B 1 62  ? -15.592 8.927   -6.042  1.00 11.85 ? 62  THR B CA  1 
ATOM   2666 C  C   . THR B 1 62  ? -14.140 8.477   -5.972  1.00 11.46 ? 62  THR B C   1 
ATOM   2667 O  O   . THR B 1 62  ? -13.697 7.814   -5.029  1.00 12.35 ? 62  THR B O   1 
ATOM   2668 C  CB  . THR B 1 62  ? -15.745 10.181  -5.191  1.00 15.82 ? 62  THR B CB  1 
ATOM   2669 O  OG1 . THR B 1 62  ? -17.060 10.602  -4.793  1.00 20.31 ? 62  THR B OG1 1 
ATOM   2670 C  CG2 . THR B 1 62  ? -15.146 11.401  -5.858  1.00 18.07 ? 62  THR B CG2 1 
ATOM   2671 N  N   . ASN B 1 63  ? -13.360 8.916   -6.948  1.00 10.00 ? 63  ASN B N   1 
ATOM   2672 C  CA  . ASN B 1 63  ? -11.910 8.861   -6.891  1.00 10.30 ? 63  ASN B CA  1 
ATOM   2673 C  C   . ASN B 1 63  ? -11.452 10.148  -6.253  1.00 10.50 ? 63  ASN B C   1 
ATOM   2674 O  O   . ASN B 1 63  ? -11.643 11.240  -6.817  1.00 9.92  ? 63  ASN B O   1 
ATOM   2675 C  CB  . ASN B 1 63  ? -11.374 8.775   -8.324  1.00 11.17 ? 63  ASN B CB  1 
ATOM   2676 C  CG  . ASN B 1 63  ? -9.871  8.777   -8.403  1.00 9.91  ? 63  ASN B CG  1 
ATOM   2677 O  OD1 . ASN B 1 63  ? -9.196  9.341   -7.533  1.00 10.88 ? 63  ASN B OD1 1 
ATOM   2678 N  ND2 . ASN B 1 63  ? -9.333  8.122   -9.427  1.00 10.50 ? 63  ASN B ND2 1 
ATOM   2679 N  N   . ASN B 1 64  ? -10.880 10.069  -5.040  1.00 10.43 ? 64  ASN B N   1 
ATOM   2680 C  CA  . ASN B 1 64  ? -10.505 11.293  -4.322  1.00 11.41 ? 64  ASN B CA  1 
ATOM   2681 C  C   . ASN B 1 64  ? -9.014  11.612  -4.501  1.00 12.34 ? 64  ASN B C   1 
ATOM   2682 O  O   . ASN B 1 64  ? -8.481  12.495  -3.808  1.00 13.52 ? 64  ASN B O   1 
ATOM   2683 C  CB  . ASN B 1 64  ? -10.879 11.213  -2.832  1.00 11.41 ? 64  ASN B CB  1 
ATOM   2684 C  CG  . ASN B 1 64  ? -10.180 10.099  -2.118  1.00 12.70 ? 64  ASN B CG  1 
ATOM   2685 O  OD1 . ASN B 1 64  ? -9.199  9.529   -2.608  1.00 11.94 ? 64  ASN B OD1 1 
ATOM   2686 N  ND2 . ASN B 1 64  ? -10.640 9.783   -0.911  1.00 14.64 ? 64  ASN B ND2 1 
ATOM   2687 N  N   . GLY B 1 65  ? -8.366  10.957  -5.462  1.00 10.92 ? 65  GLY B N   1 
ATOM   2688 C  CA  . GLY B 1 65  ? -6.950  11.209  -5.680  1.00 12.70 ? 65  GLY B CA  1 
ATOM   2689 C  C   . GLY B 1 65  ? -6.048  10.350  -4.799  1.00 12.72 ? 65  GLY B C   1 
ATOM   2690 O  O   . GLY B 1 65  ? -4.843  10.411  -5.018  1.00 14.27 ? 65  GLY B O   1 
ATOM   2691 N  N   . HIS B 1 66  ? -6.596  9.559   -3.854  1.00 11.17 ? 66  HIS B N   1 
ATOM   2692 C  CA  . HIS B 1 66  ? -5.791  8.743   -2.949  1.00 12.50 ? 66  HIS B CA  1 
ATOM   2693 C  C   . HIS B 1 66  ? -6.344  7.339   -2.790  1.00 10.76 ? 66  HIS B C   1 
ATOM   2694 O  O   . HIS B 1 66  ? -5.597  6.432   -2.417  1.00 11.35 ? 66  HIS B O   1 
ATOM   2695 C  CB  . HIS B 1 66  ? -5.742  9.386   -1.579  1.00 13.14 ? 66  HIS B CB  1 
ATOM   2696 C  CG  . HIS B 1 66  ? -5.197  10.781  -1.654  1.00 12.89 ? 66  HIS B CG  1 
ATOM   2697 N  ND1 . HIS B 1 66  ? -3.861  11.081  -1.839  1.00 14.78 ? 66  HIS B ND1 1 
ATOM   2698 C  CD2 . HIS B 1 66  ? -5.808  11.946  -1.488  1.00 13.81 ? 66  HIS B CD2 1 
ATOM   2699 C  CE1 . HIS B 1 66  ? -3.693  12.409  -1.850  1.00 13.98 ? 66  HIS B CE1 1 
ATOM   2700 N  NE2 . HIS B 1 66  ? -4.891  12.944  -1.612  1.00 14.43 ? 66  HIS B NE2 1 
ATOM   2701 N  N   . SER B 1 67  ? -7.631  7.150   -3.085  1.00 10.38 ? 67  SER B N   1 
ATOM   2702 C  CA  . SER B 1 67  ? -8.301  5.861   -3.047  1.00 9.27  ? 67  SER B CA  1 
ATOM   2703 C  C   . SER B 1 67  ? -9.565  5.990   -3.885  1.00 9.70  ? 67  SER B C   1 
ATOM   2704 O  O   . SER B 1 67  ? -9.814  7.042   -4.479  1.00 11.04 ? 67  SER B O   1 
ATOM   2705 C  CB  . SER B 1 67  ? -8.619  5.498   -1.589  1.00 11.16 ? 67  SER B CB  1 
ATOM   2706 O  OG  . SER B 1 67  ? -9.152  4.150   -1.501  1.00 11.14 ? 67  SER B OG  1 
ATOM   2707 N  N   . VAL B 1 68  ? -10.347 4.928   -3.880  1.00 10.67 ? 68  VAL B N   1 
ATOM   2708 C  CA  . VAL B 1 68  ? -11.695 5.016   -4.382  1.00 10.74 ? 68  VAL B CA  1 
ATOM   2709 C  C   . VAL B 1 68  ? -12.569 4.922   -3.119  1.00 9.81  ? 68  VAL B C   1 
ATOM   2710 O  O   . VAL B 1 68  ? -12.387 3.999   -2.308  1.00 10.73 ? 68  VAL B O   1 
ATOM   2711 C  CB  . VAL B 1 68  ? -11.937 3.927   -5.445  1.00 11.33 ? 68  VAL B CB  1 
ATOM   2712 C  CG1 . VAL B 1 68  ? -11.732 2.511   -4.966  1.00 13.05 ? 68  VAL B CG1 1 
ATOM   2713 C  CG2 . VAL B 1 68  ? -13.355 4.070   -6.009  1.00 14.57 ? 68  VAL B CG2 1 
ATOM   2714 N  N   . LYS B 1 69  ? -13.555 5.814   -3.025  1.00 10.34 ? 69  LYS B N   1 
ATOM   2715 C  CA  . LYS B 1 69  ? -14.437 5.850   -1.848  1.00 10.00 ? 69  LYS B CA  1 
ATOM   2716 C  C   . LYS B 1 69  ? -15.895 5.754   -2.254  1.00 8.99  ? 69  LYS B C   1 
ATOM   2717 O  O   . LYS B 1 69  ? -16.340 6.388   -3.222  1.00 10.50 ? 69  LYS B O   1 
ATOM   2718 C  CB  . LYS B 1 69  ? -14.090 7.040   -0.968  1.00 15.71 ? 69  LYS B CB  1 
ATOM   2719 C  CG  . LYS B 1 69  ? -14.545 8.402   -1.374  1.00 18.39 ? 69  LYS B CG  1 
ATOM   2720 C  CD  . LYS B 1 69  ? -14.764 9.262   -0.104  1.00 18.86 ? 69  LYS B CD  1 
ATOM   2721 C  CE  . LYS B 1 69  ? -15.297 10.525  -0.682  1.00 24.13 ? 69  LYS B CE  1 
ATOM   2722 N  NZ  . LYS B 1 69  ? -15.127 11.639  0.271   1.00 28.46 ? 69  LYS B NZ  1 
ATOM   2723 N  N   . LEU B 1 70  ? -16.665 5.026   -1.451  1.00 7.82  ? 70  LEU B N   1 
ATOM   2724 C  CA  . LEU B 1 70  ? -18.123 4.995   -1.590  1.00 7.76  ? 70  LEU B CA  1 
ATOM   2725 C  C   . LEU B 1 70  ? -18.671 5.761   -0.399  1.00 7.63  ? 70  LEU B C   1 
ATOM   2726 O  O   . LEU B 1 70  ? -18.437 5.378   0.751   1.00 8.35  ? 70  LEU B O   1 
ATOM   2727 C  CB  . LEU B 1 70  ? -18.557 3.540   -1.527  1.00 8.57  ? 70  LEU B CB  1 
ATOM   2728 C  CG  . LEU B 1 70  ? -20.059 3.320   -1.779  1.00 8.55  ? 70  LEU B CG  1 
ATOM   2729 C  CD1 . LEU B 1 70  ? -20.491 3.731   -3.176  1.00 11.02 ? 70  LEU B CD1 1 
ATOM   2730 C  CD2 . LEU B 1 70  ? -20.426 1.871   -1.467  1.00 10.97 ? 70  LEU B CD2 1 
ATOM   2731 N  N   . ASN B 1 71  ? -19.548 6.746   -0.633  1.00 8.46  ? 71  ASN B N   1 
ATOM   2732 C  CA  . ASN B 1 71  ? -20.275 7.459   0.417   1.00 9.80  ? 71  ASN B CA  1 
ATOM   2733 C  C   . ASN B 1 71  ? -21.391 6.579   0.948   1.00 10.14 ? 71  ASN B C   1 
ATOM   2734 O  O   . ASN B 1 71  ? -22.039 5.841   0.200   1.00 11.88 ? 71  ASN B O   1 
ATOM   2735 C  CB  . ASN B 1 71  ? -20.852 8.792   -0.103  1.00 12.22 ? 71  ASN B CB  1 
ATOM   2736 C  CG  . ASN B 1 71  ? -19.821 9.869   -0.373  1.00 14.87 ? 71  ASN B CG  1 
ATOM   2737 O  OD1 . ASN B 1 71  ? -18.649 9.745   -0.028  1.00 17.51 ? 71  ASN B OD1 1 
ATOM   2738 N  ND2 . ASN B 1 71  ? -20.305 11.026  -0.837  1.00 18.99 ? 71  ASN B ND2 1 
ATOM   2739 N  N   . LEU B 1 72  ? -21.522 6.608   2.266   1.00 9.50  ? 72  LEU B N   1 
ATOM   2740 C  CA  . LEU B 1 72  ? -22.503 5.785   2.943   1.00 9.61  ? 72  LEU B CA  1 
ATOM   2741 C  C   . LEU B 1 72  ? -23.484 6.666   3.734   1.00 10.09 ? 72  LEU B C   1 
ATOM   2742 O  O   . LEU B 1 72  ? -23.139 7.749   4.190   1.00 11.95 ? 72  LEU B O   1 
ATOM   2743 C  CB  . LEU B 1 72  ? -21.733 4.867   3.912   1.00 9.33  ? 72  LEU B CB  1 
ATOM   2744 C  CG  . LEU B 1 72  ? -20.818 3.857   3.218   1.00 9.33  ? 72  LEU B CG  1 
ATOM   2745 C  CD1 . LEU B 1 72  ? -19.945 3.138   4.246   1.00 8.69  ? 72  LEU B CD1 1 
ATOM   2746 C  CD2 . LEU B 1 72  ? -21.578 2.859   2.365   1.00 10.16 ? 72  LEU B CD2 1 
ATOM   2747 N  N   . PRO B 1 73  ? -24.725 6.172   3.928   1.00 10.60 ? 73  PRO B N   1 
ATOM   2748 C  CA  . PRO B 1 73  ? -25.741 6.980   4.610   1.00 11.90 ? 73  PRO B CA  1 
ATOM   2749 C  C   . PRO B 1 73  ? -25.594 6.899   6.124   1.00 13.48 ? 73  PRO B C   1 
ATOM   2750 O  O   . PRO B 1 73  ? -25.116 5.895   6.640   1.00 13.49 ? 73  PRO B O   1 
ATOM   2751 C  CB  . PRO B 1 73  ? -27.013 6.303   4.148   1.00 12.23 ? 73  PRO B CB  1 
ATOM   2752 C  CG  . PRO B 1 73  ? -26.646 4.826   3.938   1.00 11.68 ? 73  PRO B CG  1 
ATOM   2753 C  CD  . PRO B 1 73  ? -25.235 4.899   3.372   1.00 10.61 ? 73  PRO B CD  1 
ATOM   2754 N  N   . SER B 1 74  ? -26.011 7.956   6.809   1.00 17.66 ? 74  SER B N   1 
ATOM   2755 C  CA  . SER B 1 74  ? -25.794 8.005   8.244   1.00 16.96 ? 74  SER B CA  1 
ATOM   2756 C  C   . SER B 1 74  ? -26.778 7.108   9.001   1.00 16.31 ? 74  SER B C   1 
ATOM   2757 O  O   . SER B 1 74  ? -26.537 6.903   10.204  1.00 18.18 ? 74  SER B O   1 
ATOM   2758 C  CB  . SER B 1 74  ? -25.854 9.417   8.755   1.00 22.43 ? 74  SER B CB  1 
ATOM   2759 O  OG  . SER B 1 74  ? -27.125 9.969   8.423   1.00 24.30 ? 74  SER B OG  1 
ATOM   2760 N  N   . ASP B 1 75  ? -27.763 6.513   8.308   1.00 15.38 ? 75  ASP B N   1 
ATOM   2761 C  CA  . ASP B 1 75  ? -28.639 5.534   8.947   1.00 17.66 ? 75  ASP B CA  1 
ATOM   2762 C  C   . ASP B 1 75  ? -27.941 4.190   9.147   1.00 17.53 ? 75  ASP B C   1 
ATOM   2763 O  O   . ASP B 1 75  ? -28.452 3.300   9.827   1.00 19.98 ? 75  ASP B O   1 
ATOM   2764 C  CB  . ASP B 1 75  ? -30.024 5.456   8.290   1.00 21.84 ? 75  ASP B CB  1 
ATOM   2765 C  CG  . ASP B 1 75  ? -30.190 5.437   6.784   1.00 28.47 ? 75  ASP B CG  1 
ATOM   2766 O  OD1 . ASP B 1 75  ? -29.266 4.991   6.052   1.00 28.72 ? 75  ASP B OD1 1 
ATOM   2767 O  OD2 . ASP B 1 75  ? -31.317 5.815   6.338   1.00 38.24 ? 75  ASP B OD2 1 
ATOM   2768 N  N   . MET B 1 76  ? -26.769 4.119   8.469   1.00 13.51 ? 76  MET B N   1 
ATOM   2769 C  CA  . MET B 1 76  ? -26.011 2.887   8.655   1.00 12.89 ? 76  MET B CA  1 
ATOM   2770 C  C   . MET B 1 76  ? -25.174 3.052   9.915   1.00 12.31 ? 76  MET B C   1 
ATOM   2771 O  O   . MET B 1 76  ? -24.487 4.077   10.081  1.00 12.81 ? 76  MET B O   1 
ATOM   2772 C  CB  . MET B 1 76  ? -25.162 2.750   7.401   1.00 15.75 ? 76  MET B CB  1 
ATOM   2773 C  CG  . MET B 1 76  ? -24.351 1.570   7.352   1.00 16.61 ? 76  MET B CG  1 
ATOM   2774 S  SD  . MET B 1 76  ? -23.654 1.584   5.615   1.00 15.18 ? 76  MET B SD  1 
ATOM   2775 C  CE  . MET B 1 76  ? -22.280 0.561   6.095   1.00 14.63 ? 76  MET B CE  1 
ATOM   2776 N  N   . HIS B 1 77  ? -25.216 2.111   10.897  1.00 11.98 ? 77  HIS B N   1 
ATOM   2777 C  CA  . HIS B 1 77  ? -24.404 2.348   12.084  1.00 13.56 ? 77  HIS B CA  1 
ATOM   2778 C  C   . HIS B 1 77  ? -23.946 1.063   12.727  1.00 13.23 ? 77  HIS B C   1 
ATOM   2779 O  O   . HIS B 1 77  ? -24.410 -0.012  12.396  1.00 13.40 ? 77  HIS B O   1 
ATOM   2780 C  CB  . HIS B 1 77  ? -25.115 3.265   13.091  1.00 19.99 ? 77  HIS B CB  1 
ATOM   2781 C  CG  . HIS B 1 77  ? -26.420 2.747   13.548  1.00 22.76 ? 77  HIS B CG  1 
ATOM   2782 N  ND1 . HIS B 1 77  ? -27.603 2.943   12.841  1.00 24.29 ? 77  HIS B ND1 1 
ATOM   2783 C  CD2 . HIS B 1 77  ? -26.749 2.116   14.698  1.00 26.01 ? 77  HIS B CD2 1 
ATOM   2784 C  CE1 . HIS B 1 77  ? -28.598 2.390   13.530  1.00 26.13 ? 77  HIS B CE1 1 
ATOM   2785 N  NE2 . HIS B 1 77  ? -28.101 1.890   14.669  1.00 27.75 ? 77  HIS B NE2 1 
ATOM   2786 N  N   A ILE B 1 78  ? -22.975 1.235   13.614  0.50 12.99 ? 78  ILE B N   1 
ATOM   2787 N  N   B ILE B 1 78  ? -22.997 1.253   13.644  0.50 13.50 ? 78  ILE B N   1 
ATOM   2788 C  CA  A ILE B 1 78  ? -22.544 0.111   14.421  0.50 14.52 ? 78  ILE B CA  1 
ATOM   2789 C  CA  B ILE B 1 78  ? -22.464 0.183   14.474  0.50 15.73 ? 78  ILE B CA  1 
ATOM   2790 C  C   A ILE B 1 78  ? -23.246 0.286   15.755  0.50 15.64 ? 78  ILE B C   1 
ATOM   2791 C  C   B ILE B 1 78  ? -23.158 0.289   15.820  0.50 16.91 ? 78  ILE B C   1 
ATOM   2792 O  O   A ILE B 1 78  ? -23.303 1.395   16.280  0.50 16.55 ? 78  ILE B O   1 
ATOM   2793 O  O   B ILE B 1 78  ? -23.140 1.375   16.403  0.50 17.96 ? 78  ILE B O   1 
ATOM   2794 C  CB  A ILE B 1 78  ? -21.012 0.112   14.625  0.50 14.35 ? 78  ILE B CB  1 
ATOM   2795 C  CB  B ILE B 1 78  ? -20.936 0.348   14.654  0.50 16.51 ? 78  ILE B CB  1 
ATOM   2796 C  CG1 A ILE B 1 78  ? -20.140 0.137   13.373  0.50 16.71 ? 78  ILE B CG1 1 
ATOM   2797 C  CG1 B ILE B 1 78  ? -20.151 -0.025  13.402  0.50 19.56 ? 78  ILE B CG1 1 
ATOM   2798 C  CG2 A ILE B 1 78  ? -20.597 -0.968  15.626  0.50 15.97 ? 78  ILE B CG2 1 
ATOM   2799 C  CG2 B ILE B 1 78  ? -20.449 -0.417  15.890  0.50 16.47 ? 78  ILE B CG2 1 
ATOM   2800 C  CD1 A ILE B 1 78  ? -18.732 0.626   13.666  0.50 12.84 ? 78  ILE B CD1 1 
ATOM   2801 C  CD1 B ILE B 1 78  ? -20.840 -1.042  12.575  0.50 17.52 ? 78  ILE B CD1 1 
ATOM   2802 N  N   . GLN B 1 79  ? -23.708 -0.845  16.283  1.00 16.17 ? 79  GLN B N   1 
ATOM   2803 C  CA  . GLN B 1 79  ? -24.195 -0.920  17.656  1.00 18.77 ? 79  GLN B CA  1 
ATOM   2804 C  C   . GLN B 1 79  ? -23.210 -1.792  18.450  1.00 18.69 ? 79  GLN B C   1 
ATOM   2805 O  O   . GLN B 1 79  ? -22.781 -2.866  18.002  1.00 17.96 ? 79  GLN B O   1 
ATOM   2806 C  CB  . GLN B 1 79  ? -25.592 -1.542  17.716  1.00 21.17 ? 79  GLN B CB  1 
ATOM   2807 C  CG  . GLN B 1 79  ? -26.133 -1.451  19.141  1.00 31.92 ? 79  GLN B CG  1 
ATOM   2808 C  CD  . GLN B 1 79  ? -27.582 -1.839  19.243  1.00 35.22 ? 79  GLN B CD  1 
ATOM   2809 O  OE1 . GLN B 1 79  ? -28.464 -1.095  18.814  1.00 40.39 ? 79  GLN B OE1 1 
ATOM   2810 N  NE2 . GLN B 1 79  ? -27.830 -3.011  19.810  1.00 35.04 ? 79  GLN B NE2 1 
ATOM   2811 N  N   . GLY B 1 80  ? -22.897 -1.334  19.654  1.00 18.82 ? 80  GLY B N   1 
ATOM   2812 C  CA  . GLY B 1 80  ? -22.087 -2.128  20.582  1.00 19.15 ? 80  GLY B CA  1 
ATOM   2813 C  C   . GLY B 1 80  ? -20.890 -1.377  21.146  1.00 20.79 ? 80  GLY B C   1 
ATOM   2814 O  O   . GLY B 1 80  ? -20.323 -1.800  22.158  1.00 21.69 ? 80  GLY B O   1 
ATOM   2815 N  N   . LEU B 1 81  ? -20.524 -0.243  20.534  1.00 18.88 ? 81  LEU B N   1 
ATOM   2816 C  CA  . LEU B 1 81  ? -19.553 0.656   21.138  1.00 17.89 ? 81  LEU B CA  1 
ATOM   2817 C  C   . LEU B 1 81  ? -20.245 1.521   22.188  1.00 21.18 ? 81  LEU B C   1 
ATOM   2818 O  O   . LEU B 1 81  ? -21.426 1.360   22.442  1.00 20.74 ? 81  LEU B O   1 
ATOM   2819 C  CB  . LEU B 1 81  ? -18.834 1.466   20.051  1.00 18.47 ? 81  LEU B CB  1 
ATOM   2820 C  CG  . LEU B 1 81  ? -18.141 0.563   19.029  1.00 19.99 ? 81  LEU B CG  1 
ATOM   2821 C  CD1 . LEU B 1 81  ? -17.668 1.378   17.838  1.00 19.01 ? 81  LEU B CD1 1 
ATOM   2822 C  CD2 . LEU B 1 81  ? -16.964 -0.131  19.693  1.00 18.93 ? 81  LEU B CD2 1 
ATOM   2823 N  N   . GLN B 1 82  ? -19.525 2.420   22.841  1.00 24.29 ? 82  GLN B N   1 
ATOM   2824 C  CA  . GLN B 1 82  ? -20.184 3.108   23.948  1.00 26.83 ? 82  GLN B CA  1 
ATOM   2825 C  C   . GLN B 1 82  ? -21.048 4.272   23.471  1.00 28.31 ? 82  GLN B C   1 
ATOM   2826 O  O   . GLN B 1 82  ? -21.796 4.845   24.259  1.00 28.42 ? 82  GLN B O   1 
ATOM   2827 C  CB  . GLN B 1 82  ? -19.164 3.565   24.984  1.00 27.53 ? 82  GLN B CB  1 
ATOM   2828 C  CG  . GLN B 1 82  ? -18.793 2.434   25.943  1.00 30.74 ? 82  GLN B CG  1 
ATOM   2829 C  CD  . GLN B 1 82  ? -17.599 2.794   26.790  1.00 34.05 ? 82  GLN B CD  1 
ATOM   2830 O  OE1 . GLN B 1 82  ? -17.653 2.790   28.022  1.00 35.34 ? 82  GLN B OE1 1 
ATOM   2831 N  NE2 . GLN B 1 82  ? -16.506 3.128   26.123  1.00 31.76 ? 82  GLN B NE2 1 
ATOM   2832 N  N   . SER B 1 83  ? -20.884 4.653   22.201  1.00 22.42 ? 83  SER B N   1 
ATOM   2833 C  CA  . SER B 1 83  ? -21.762 5.588   21.511  1.00 19.33 ? 83  SER B CA  1 
ATOM   2834 C  C   . SER B 1 83  ? -22.158 4.897   20.218  1.00 19.11 ? 83  SER B C   1 
ATOM   2835 O  O   . SER B 1 83  ? -21.495 3.945   19.802  1.00 16.36 ? 83  SER B O   1 
ATOM   2836 C  CB  . SER B 1 83  ? -21.022 6.856   21.176  1.00 22.08 ? 83  SER B CB  1 
ATOM   2837 O  OG  . SER B 1 83  ? -20.667 7.582   22.352  1.00 26.41 ? 83  SER B OG  1 
ATOM   2838 N  N   A ARG B 1 84  ? -23.202 5.450   19.588  0.50 17.63 ? 84  ARG B N   1 
ATOM   2839 N  N   B ARG B 1 84  ? -23.281 5.304   19.628  0.50 18.31 ? 84  ARG B N   1 
ATOM   2840 C  CA  A ARG B 1 84  ? -23.570 5.096   18.229  0.50 16.89 ? 84  ARG B CA  1 
ATOM   2841 C  CA  B ARG B 1 84  ? -23.526 4.820   18.284  0.50 17.30 ? 84  ARG B CA  1 
ATOM   2842 C  C   A ARG B 1 84  ? -22.526 5.685   17.274  0.50 15.99 ? 84  ARG B C   1 
ATOM   2843 C  C   B ARG B 1 84  ? -22.585 5.573   17.331  0.50 16.96 ? 84  ARG B C   1 
ATOM   2844 O  O   A ARG B 1 84  ? -22.173 6.867   17.329  0.50 15.50 ? 84  ARG B O   1 
ATOM   2845 O  O   B ARG B 1 84  ? -22.325 6.761   17.471  0.50 17.02 ? 84  ARG B O   1 
ATOM   2846 C  CB  A ARG B 1 84  ? -24.969 5.617   17.898  0.50 17.89 ? 84  ARG B CB  1 
ATOM   2847 C  CB  B ARG B 1 84  ? -25.003 4.912   17.915  0.50 18.13 ? 84  ARG B CB  1 
ATOM   2848 C  CG  A ARG B 1 84  ? -25.184 5.826   16.409  0.50 19.15 ? 84  ARG B CG  1 
ATOM   2849 C  CG  B ARG B 1 84  ? -25.188 5.186   16.429  0.50 21.45 ? 84  ARG B CG  1 
ATOM   2850 C  CD  A ARG B 1 84  ? -26.648 5.982   16.024  0.50 20.45 ? 84  ARG B CD  1 
ATOM   2851 C  CD  B ARG B 1 84  ? -26.501 5.873   16.138  0.50 23.24 ? 84  ARG B CD  1 
ATOM   2852 N  NE  A ARG B 1 84  ? -26.722 5.922   14.577  0.50 19.54 ? 84  ARG B NE  1 
ATOM   2853 N  NE  B ARG B 1 84  ? -27.551 4.915   16.390  0.50 22.46 ? 84  ARG B NE  1 
ATOM   2854 C  CZ  A ARG B 1 84  ? -27.836 5.813   13.889  0.50 20.31 ? 84  ARG B CZ  1 
ATOM   2855 C  CZ  B ARG B 1 84  ? -28.834 5.168   16.178  0.50 22.69 ? 84  ARG B CZ  1 
ATOM   2856 N  NH1 A ARG B 1 84  ? -28.992 5.740   14.525  0.50 21.03 ? 84  ARG B NH1 1 
ATOM   2857 N  NH1 B ARG B 1 84  ? -29.219 6.360   15.758  0.50 25.12 ? 84  ARG B NH1 1 
ATOM   2858 N  NH2 A ARG B 1 84  ? -27.781 5.765   12.574  0.50 16.89 ? 84  ARG B NH2 1 
ATOM   2859 N  NH2 B ARG B 1 84  ? -29.725 4.234   16.437  0.50 21.21 ? 84  ARG B NH2 1 
ATOM   2860 N  N   . TYR B 1 85  ? -22.035 4.821   16.376  1.00 13.60 ? 85  TYR B N   1 
ATOM   2861 C  CA  . TYR B 1 85  ? -21.167 5.340   15.322  1.00 12.18 ? 85  TYR B CA  1 
ATOM   2862 C  C   . TYR B 1 85  ? -21.875 5.115   14.011  1.00 12.09 ? 85  TYR B C   1 
ATOM   2863 O  O   . TYR B 1 85  ? -22.255 4.007   13.716  1.00 14.93 ? 85  TYR B O   1 
ATOM   2864 C  CB  . TYR B 1 85  ? -19.802 4.620   15.340  1.00 12.12 ? 85  TYR B CB  1 
ATOM   2865 C  CG  . TYR B 1 85  ? -18.870 5.101   16.422  1.00 11.84 ? 85  TYR B CG  1 
ATOM   2866 C  CD1 . TYR B 1 85  ? -19.044 4.631   17.716  1.00 13.57 ? 85  TYR B CD1 1 
ATOM   2867 C  CD2 . TYR B 1 85  ? -17.855 6.024   16.204  1.00 11.06 ? 85  TYR B CD2 1 
ATOM   2868 C  CE1 . TYR B 1 85  ? -18.224 5.074   18.749  1.00 13.42 ? 85  TYR B CE1 1 
ATOM   2869 C  CE2 . TYR B 1 85  ? -16.997 6.414   17.214  1.00 12.70 ? 85  TYR B CE2 1 
ATOM   2870 C  CZ  . TYR B 1 85  ? -17.193 5.951   18.494  1.00 14.00 ? 85  TYR B CZ  1 
ATOM   2871 O  OH  . TYR B 1 85  ? -16.366 6.348   19.518  1.00 18.08 ? 85  TYR B OH  1 
ATOM   2872 N  N   . SER B 1 86  ? -21.996 6.181   13.220  1.00 10.99 ? 86  SER B N   1 
ATOM   2873 C  CA  . SER B 1 86  ? -22.711 6.136   11.958  1.00 11.19 ? 86  SER B CA  1 
ATOM   2874 C  C   . SER B 1 86  ? -21.688 6.116   10.805  1.00 9.40  ? 86  SER B C   1 
ATOM   2875 O  O   . SER B 1 86  ? -20.654 6.808   10.872  1.00 9.77  ? 86  SER B O   1 
ATOM   2876 C  CB  . SER B 1 86  ? -23.587 7.369   11.814  1.00 14.71 ? 86  SER B CB  1 
ATOM   2877 O  OG  . SER B 1 86  ? -24.691 7.286   12.752  1.00 17.00 ? 86  SER B OG  1 
ATOM   2878 N  N   . ALA B 1 87  ? -22.049 5.379   9.765   1.00 9.85  ? 87  ALA B N   1 
ATOM   2879 C  CA  . ALA B 1 87  ? -21.127 5.286   8.626   1.00 8.76  ? 87  ALA B CA  1 
ATOM   2880 C  C   . ALA B 1 87  ? -21.032 6.612   7.902   1.00 10.08 ? 87  ALA B C   1 
ATOM   2881 O  O   . ALA B 1 87  ? -22.006 7.387   7.857   1.00 11.98 ? 87  ALA B O   1 
ATOM   2882 C  CB  . ALA B 1 87  ? -21.624 4.234   7.699   1.00 11.00 ? 87  ALA B CB  1 
ATOM   2883 N  N   . THR B 1 88  ? -19.860 6.849   7.294   1.00 9.28  ? 88  THR B N   1 
ATOM   2884 C  CA  . THR B 1 88  ? -19.695 7.996   6.403   1.00 9.41  ? 88  THR B CA  1 
ATOM   2885 C  C   . THR B 1 88  ? -19.163 7.557   5.037   1.00 8.78  ? 88  THR B C   1 
ATOM   2886 O  O   . THR B 1 88  ? -19.583 8.067   4.017   1.00 8.79  ? 88  THR B O   1 
ATOM   2887 C  CB  . THR B 1 88  ? -18.878 9.114   7.059   1.00 11.41 ? 88  THR B CB  1 
ATOM   2888 O  OG1 . THR B 1 88  ? -18.803 10.237  6.154   1.00 14.92 ? 88  THR B OG1 1 
ATOM   2889 C  CG2 . THR B 1 88  ? -17.486 8.694   7.484   1.00 11.37 ? 88  THR B CG2 1 
ATOM   2890 N  N   . GLN B 1 89  ? -18.238 6.586   4.988   1.00 7.34  ? 89  GLN B N   1 
ATOM   2891 C  CA  . GLN B 1 89  ? -17.706 6.186   3.688   1.00 7.13  ? 89  GLN B CA  1 
ATOM   2892 C  C   . GLN B 1 89  ? -16.887 4.916   3.863   1.00 6.22  ? 89  GLN B C   1 
ATOM   2893 O  O   . GLN B 1 89  ? -16.519 4.599   4.999   1.00 6.84  ? 89  GLN B O   1 
ATOM   2894 C  CB  . GLN B 1 89  ? -16.762 7.258   3.059   1.00 8.67  ? 89  GLN B CB  1 
ATOM   2895 C  CG  . GLN B 1 89  ? -15.688 7.736   4.042   1.00 9.91  ? 89  GLN B CG  1 
ATOM   2896 C  CD  . GLN B 1 89  ? -14.301 7.406   3.578   1.00 9.94  ? 89  GLN B CD  1 
ATOM   2897 O  OE1 . GLN B 1 89  ? -14.012 6.267   3.239   1.00 9.71  ? 89  GLN B OE1 1 
ATOM   2898 N  NE2 . GLN B 1 89  ? -13.394 8.355   3.648   1.00 11.81 ? 89  GLN B NE2 1 
ATOM   2899 N  N   . LEU B 1 90  ? -16.710 4.200   2.771   1.00 6.06  ? 90  LEU B N   1 
ATOM   2900 C  CA  . LEU B 1 90  ? -15.738 3.108   2.775   1.00 6.54  ? 90  LEU B CA  1 
ATOM   2901 C  C   . LEU B 1 90  ? -14.737 3.350   1.653   1.00 6.53  ? 90  LEU B C   1 
ATOM   2902 O  O   . LEU B 1 90  ? -15.031 4.030   0.682   1.00 6.83  ? 90  LEU B O   1 
ATOM   2903 C  CB  . LEU B 1 90  ? -16.389 1.708   2.764   1.00 6.95  ? 90  LEU B CB  1 
ATOM   2904 C  CG  . LEU B 1 90  ? -17.321 1.406   1.596   1.00 6.95  ? 90  LEU B CG  1 
ATOM   2905 C  CD1 . LEU B 1 90  ? -16.565 1.078   0.307   1.00 8.50  ? 90  LEU B CD1 1 
ATOM   2906 C  CD2 . LEU B 1 90  ? -18.181 0.189   1.943   1.00 7.89  ? 90  LEU B CD2 1 
ATOM   2907 N  N   . HIS B 1 91  ? -13.543 2.744   1.742   1.00 6.01  ? 91  HIS B N   1 
ATOM   2908 C  CA  . HIS B 1 91  ? -12.527 2.871   0.707   1.00 6.37  ? 91  HIS B CA  1 
ATOM   2909 C  C   . HIS B 1 91  ? -11.563 1.718   0.857   1.00 5.74  ? 91  HIS B C   1 
ATOM   2910 O  O   . HIS B 1 91  ? -11.658 0.937   1.810   1.00 6.13  ? 91  HIS B O   1 
ATOM   2911 C  CB  . HIS B 1 91  ? -11.827 4.230   0.817   1.00 6.25  ? 91  HIS B CB  1 
ATOM   2912 C  CG  . HIS B 1 91  ? -11.102 4.381   2.110   1.00 5.40  ? 91  HIS B CG  1 
ATOM   2913 N  ND1 . HIS B 1 91  ? -11.631 4.974   3.224   1.00 6.76  ? 91  HIS B ND1 1 
ATOM   2914 C  CD2 . HIS B 1 91  ? -9.876  3.902   2.483   1.00 6.34  ? 91  HIS B CD2 1 
ATOM   2915 C  CE1 . HIS B 1 91  ? -10.787 4.857   4.265   1.00 6.35  ? 91  HIS B CE1 1 
ATOM   2916 N  NE2 . HIS B 1 91  ? -9.683  4.166   3.820   1.00 5.95  ? 91  HIS B NE2 1 
ATOM   2917 N  N   . LEU B 1 92  ? -10.602 1.633   -0.072  1.00 6.56  ? 92  LEU B N   1 
ATOM   2918 C  CA  . LEU B 1 92  ? -9.656  0.498   -0.039  1.00 6.55  ? 92  LEU B CA  1 
ATOM   2919 C  C   . LEU B 1 92  ? -8.206  0.974   -0.137  1.00 6.53  ? 92  LEU B C   1 
ATOM   2920 O  O   . LEU B 1 92  ? -7.899  2.120   -0.505  1.00 7.01  ? 92  LEU B O   1 
ATOM   2921 C  CB  . LEU B 1 92  ? -9.979  -0.469  -1.173  1.00 8.08  ? 92  LEU B CB  1 
ATOM   2922 C  CG  . LEU B 1 92  ? -11.360 -1.131  -1.062  1.00 8.60  ? 92  LEU B CG  1 
ATOM   2923 C  CD1 . LEU B 1 92  ? -12.352 -0.475  -1.949  1.00 12.62 ? 92  LEU B CD1 1 
ATOM   2924 C  CD2 . LEU B 1 92  ? -11.232 -2.606  -1.334  1.00 11.34 ? 92  LEU B CD2 1 
ATOM   2925 N  N   . HIS B 1 93  ? -7.315  0.055   0.164   1.00 6.56  ? 93  HIS B N   1 
ATOM   2926 C  CA  . HIS B 1 93  ? -5.875  0.224   -0.039  1.00 6.54  ? 93  HIS B CA  1 
ATOM   2927 C  C   . HIS B 1 93  ? -5.381  -1.023  -0.715  1.00 6.89  ? 93  HIS B C   1 
ATOM   2928 O  O   . HIS B 1 93  ? -5.832  -2.134  -0.383  1.00 6.91  ? 93  HIS B O   1 
ATOM   2929 C  CB  . HIS B 1 93  ? -5.164  0.359   1.308   1.00 7.58  ? 93  HIS B CB  1 
ATOM   2930 C  CG  . HIS B 1 93  ? -5.690  1.518   2.100   1.00 6.21  ? 93  HIS B CG  1 
ATOM   2931 N  ND1 . HIS B 1 93  ? -5.091  2.791   2.111   1.00 6.52  ? 93  HIS B ND1 1 
ATOM   2932 C  CD2 . HIS B 1 93  ? -6.738  1.640   2.991   1.00 5.81  ? 93  HIS B CD2 1 
ATOM   2933 C  CE1 . HIS B 1 93  ? -5.777  3.631   2.892   1.00 6.73  ? 93  HIS B CE1 1 
ATOM   2934 N  NE2 . HIS B 1 93  ? -6.779  2.959   3.452   1.00 6.18  ? 93  HIS B NE2 1 
ATOM   2935 N  N   . TRP B 1 94  ? -4.419  -0.891  -1.627  1.00 6.52  ? 94  TRP B N   1 
ATOM   2936 C  CA  . TRP B 1 94  ? -3.947  -2.035  -2.408  1.00 6.61  ? 94  TRP B CA  1 
ATOM   2937 C  C   . TRP B 1 94  ? -2.513  -1.785  -2.872  1.00 7.14  ? 94  TRP B C   1 
ATOM   2938 O  O   . TRP B 1 94  ? -1.893  -0.732  -2.651  1.00 7.35  ? 94  TRP B O   1 
ATOM   2939 C  CB  . TRP B 1 94  ? -4.879  -2.279  -3.579  1.00 7.50  ? 94  TRP B CB  1 
ATOM   2940 C  CG  . TRP B 1 94  ? -5.013  -1.095  -4.517  1.00 7.45  ? 94  TRP B CG  1 
ATOM   2941 C  CD1 . TRP B 1 94  ? -4.208  -0.755  -5.574  1.00 8.34  ? 94  TRP B CD1 1 
ATOM   2942 C  CD2 . TRP B 1 94  ? -6.017  -0.051  -4.455  1.00 7.44  ? 94  TRP B CD2 1 
ATOM   2943 N  NE1 . TRP B 1 94  ? -4.656  0.395   -6.195  1.00 8.68  ? 94  TRP B NE1 1 
ATOM   2944 C  CE2 . TRP B 1 94  ? -5.782  0.840   -5.526  1.00 7.52  ? 94  TRP B CE2 1 
ATOM   2945 C  CE3 . TRP B 1 94  ? -7.102  0.224   -3.619  1.00 7.64  ? 94  TRP B CE3 1 
ATOM   2946 C  CZ2 . TRP B 1 94  ? -6.583  1.956   -5.778  1.00 8.12  ? 94  TRP B CZ2 1 
ATOM   2947 C  CZ3 . TRP B 1 94  ? -7.857  1.371   -3.827  1.00 7.50  ? 94  TRP B CZ3 1 
ATOM   2948 C  CH2 . TRP B 1 94  ? -7.611  2.203   -4.924  1.00 7.98  ? 94  TRP B CH2 1 
ATOM   2949 N  N   . GLY B 1 95  ? -2.002  -2.836  -3.538  1.00 7.25  ? 95  GLY B N   1 
ATOM   2950 C  CA  . GLY B 1 95  ? -0.620  -2.855  -4.022  1.00 8.88  ? 95  GLY B CA  1 
ATOM   2951 C  C   . GLY B 1 95  ? -0.542  -2.514  -5.508  1.00 8.72  ? 95  GLY B C   1 
ATOM   2952 O  O   . GLY B 1 95  ? -1.021  -1.488  -5.971  1.00 8.81  ? 95  GLY B O   1 
ATOM   2953 N  N   . ASN B 1 96  ? 0.002   -3.449  -6.315  1.00 10.05 ? 96  ASN B N   1 
ATOM   2954 C  CA  . ASN B 1 96  ? 0.162   -3.157  -7.726  1.00 11.32 ? 96  ASN B CA  1 
ATOM   2955 C  C   . ASN B 1 96  ? 0.169   -4.467  -8.470  1.00 12.00 ? 96  ASN B C   1 
ATOM   2956 O  O   . ASN B 1 96  ? 0.255   -5.516  -7.885  1.00 11.06 ? 96  ASN B O   1 
ATOM   2957 C  CB  . ASN B 1 96  ? 1.457   -2.363  -7.950  1.00 12.75 ? 96  ASN B CB  1 
ATOM   2958 C  CG  . ASN B 1 96  ? 2.740   -3.139  -7.664  1.00 14.26 ? 96  ASN B CG  1 
ATOM   2959 O  OD1 . ASN B 1 96  ? 3.154   -3.956  -8.503  1.00 18.89 ? 96  ASN B OD1 1 
ATOM   2960 N  ND2 . ASN B 1 96  ? 3.350   -2.986  -6.520  1.00 15.70 ? 96  ASN B ND2 1 
ATOM   2961 N  N   . PRO B 1 97  ? 0.041   -4.448  -9.817  1.00 12.22 ? 97  PRO B N   1 
ATOM   2962 C  CA  . PRO B 1 97  ? -0.149  -5.671  -10.565 1.00 14.06 ? 97  PRO B CA  1 
ATOM   2963 C  C   . PRO B 1 97  ? 0.946   -6.707  -10.418 1.00 12.82 ? 97  PRO B C   1 
ATOM   2964 O  O   . PRO B 1 97  ? 0.670   -7.918  -10.469 1.00 15.73 ? 97  PRO B O   1 
ATOM   2965 C  CB  . PRO B 1 97  ? -0.267  -5.175  -12.017 1.00 15.48 ? 97  PRO B CB  1 
ATOM   2966 C  CG  . PRO B 1 97  ? -0.888  -3.822  -11.842 1.00 16.21 ? 97  PRO B CG  1 
ATOM   2967 C  CD  . PRO B 1 97  ? -0.130  -3.258  -10.666 1.00 14.94 ? 97  PRO B CD  1 
ATOM   2968 N  N   . ASN B 1 98  ? 2.170   -6.230  -10.232 1.00 11.47 ? 98  ASN B N   1 
ATOM   2969 C  CA  . ASN B 1 98  ? 3.294   -7.150  -10.165 1.00 14.96 ? 98  ASN B CA  1 
ATOM   2970 C  C   . ASN B 1 98  ? 3.538   -7.544  -8.718  1.00 18.31 ? 98  ASN B C   1 
ATOM   2971 O  O   . ASN B 1 98  ? 4.391   -8.401  -8.457  1.00 23.30 ? 98  ASN B O   1 
ATOM   2972 C  CB  . ASN B 1 98  ? 4.517   -6.458  -10.785 1.00 14.10 ? 98  ASN B CB  1 
ATOM   2973 C  CG  . ASN B 1 98  ? 4.308   -6.211  -12.267 1.00 14.39 ? 98  ASN B CG  1 
ATOM   2974 O  OD1 . ASN B 1 98  ? 4.086   -7.150  -13.015 1.00 14.38 ? 98  ASN B OD1 1 
ATOM   2975 N  ND2 . ASN B 1 98  ? 4.165   -4.962  -12.641 1.00 16.03 ? 98  ASN B ND2 1 
ATOM   2976 N  N   . ASP B 1 99  ? 2.859   -6.885  -7.765  1.00 15.80 ? 99  ASP B N   1 
ATOM   2977 C  CA  . ASP B 1 99  ? 3.065   -7.264  -6.365  1.00 15.99 ? 99  ASP B CA  1 
ATOM   2978 C  C   . ASP B 1 99  ? 1.789   -6.944  -5.592  1.00 12.88 ? 99  ASP B C   1 
ATOM   2979 O  O   . ASP B 1 99  ? 1.614   -5.851  -5.063  1.00 11.85 ? 99  ASP B O   1 
ATOM   2980 C  CB  . ASP B 1 99  ? 4.263   -6.529  -5.750  1.00 21.73 ? 99  ASP B CB  1 
ATOM   2981 C  CG  . ASP B 1 99  ? 4.557   -6.896  -4.298  1.00 29.32 ? 99  ASP B CG  1 
ATOM   2982 O  OD1 . ASP B 1 99  ? 4.041   -7.940  -3.836  1.00 31.83 ? 99  ASP B OD1 1 
ATOM   2983 O  OD2 . ASP B 1 99  ? 5.303   -6.137  -3.668  1.00 33.71 ? 99  ASP B OD2 1 
ATOM   2984 N  N   . PRO B 1 100 ? 0.822   -7.866  -5.591  1.00 12.27 ? 100 PRO B N   1 
ATOM   2985 C  CA  . PRO B 1 100 ? -0.485  -7.611  -4.969  1.00 12.60 ? 100 PRO B CA  1 
ATOM   2986 C  C   . PRO B 1 100 ? -0.445  -7.857  -3.463  1.00 11.82 ? 100 PRO B C   1 
ATOM   2987 O  O   . PRO B 1 100 ? -1.035  -8.801  -2.966  1.00 13.03 ? 100 PRO B O   1 
ATOM   2988 C  CB  . PRO B 1 100 ? -1.401  -8.534  -5.795  1.00 13.91 ? 100 PRO B CB  1 
ATOM   2989 C  CG  . PRO B 1 100 ? -0.486  -9.713  -6.163  1.00 16.21 ? 100 PRO B CG  1 
ATOM   2990 C  CD  . PRO B 1 100 ? 0.901   -9.150  -6.317  1.00 15.39 ? 100 PRO B CD  1 
ATOM   2991 N  N   . HIS B 1 101 ? 0.260   -6.992  -2.741  1.00 11.06 ? 101 HIS B N   1 
ATOM   2992 C  CA  . HIS B 1 101 ? 0.461   -7.134  -1.299  1.00 12.36 ? 101 HIS B CA  1 
ATOM   2993 C  C   . HIS B 1 101 ? 0.344   -5.780  -0.606  1.00 12.84 ? 101 HIS B C   1 
ATOM   2994 O  O   . HIS B 1 101 ? 1.274   -5.395  0.137   1.00 18.54 ? 101 HIS B O   1 
ATOM   2995 C  CB  . HIS B 1 101 ? 1.797   -7.797  -0.933  1.00 15.77 ? 101 HIS B CB  1 
ATOM   2996 C  CG  . HIS B 1 101 ? 1.824   -9.193  -1.430  1.00 21.36 ? 101 HIS B CG  1 
ATOM   2997 N  ND1 . HIS B 1 101 ? 1.179   -10.238 -0.785  1.00 26.24 ? 101 HIS B ND1 1 
ATOM   2998 C  CD2 . HIS B 1 101 ? 2.338   -9.683  -2.569  1.00 19.35 ? 101 HIS B CD2 1 
ATOM   2999 C  CE1 . HIS B 1 101 ? 1.316   -11.338 -1.508  1.00 26.48 ? 101 HIS B CE1 1 
ATOM   3000 N  NE2 . HIS B 1 101 ? 1.993   -11.022 -2.614  1.00 24.14 ? 101 HIS B NE2 1 
ATOM   3001 N  N   . GLY B 1 102 ? -0.834  -5.170  -0.673  1.00 9.76  ? 102 GLY B N   1 
ATOM   3002 C  CA  . GLY B 1 102 ? -1.014  -3.765  -0.321  1.00 9.25  ? 102 GLY B CA  1 
ATOM   3003 C  C   . GLY B 1 102 ? -1.946  -3.535  0.876   1.00 8.12  ? 102 GLY B C   1 
ATOM   3004 O  O   . GLY B 1 102 ? -2.459  -2.436  1.026   1.00 8.77  ? 102 GLY B O   1 
ATOM   3005 N  N   . SER B 1 103 ? -2.153  -4.500  1.786   1.00 8.10  ? 103 SER B N   1 
ATOM   3006 C  CA  . SER B 1 103 ? -2.887  -4.168  2.982   1.00 7.86  ? 103 SER B CA  1 
ATOM   3007 C  C   . SER B 1 103 ? -2.104  -3.167  3.822   1.00 7.83  ? 103 SER B C   1 
ATOM   3008 O  O   . SER B 1 103 ? -0.885  -3.051  3.684   1.00 8.76  ? 103 SER B O   1 
ATOM   3009 C  CB  . SER B 1 103 ? -3.239  -5.430  3.807   1.00 7.72  ? 103 SER B CB  1 
ATOM   3010 O  OG  . SER B 1 103 ? -2.041  -5.960  4.407   1.00 8.02  ? 103 SER B OG  1 
ATOM   3011 N  N   . GLU B 1 104 ? -2.781  -2.471  4.727   1.00 6.98  ? 104 GLU B N   1 
ATOM   3012 C  CA  . GLU B 1 104 ? -2.140  -1.550  5.653   1.00 7.00  ? 104 GLU B CA  1 
ATOM   3013 C  C   . GLU B 1 104 ? -1.727  -2.255  6.934   1.00 7.01  ? 104 GLU B C   1 
ATOM   3014 O  O   . GLU B 1 104 ? -0.554  -2.289  7.263   1.00 7.60  ? 104 GLU B O   1 
ATOM   3015 C  CB  . GLU B 1 104 ? -3.050  -0.359  5.955   1.00 7.72  ? 104 GLU B CB  1 
ATOM   3016 C  CG  . GLU B 1 104 ? -3.486  0.382   4.661   1.00 7.79  ? 104 GLU B CG  1 
ATOM   3017 C  CD  . GLU B 1 104 ? -3.577  1.846   4.958   1.00 7.56  ? 104 GLU B CD  1 
ATOM   3018 O  OE1 . GLU B 1 104 ? -4.583  2.265   5.563   1.00 8.30  ? 104 GLU B OE1 1 
ATOM   3019 O  OE2 . GLU B 1 104 ? -2.636  2.572   4.629   1.00 8.29  ? 104 GLU B OE2 1 
ATOM   3020 N  N   . HIS B 1 105 ? -2.671  -2.876  7.629   1.00 7.64  ? 105 HIS B N   1 
ATOM   3021 C  CA  . HIS B 1 105 ? -2.285  -3.742  8.743   1.00 7.81  ? 105 HIS B CA  1 
ATOM   3022 C  C   . HIS B 1 105 ? -1.635  -5.002  8.197   1.00 8.06  ? 105 HIS B C   1 
ATOM   3023 O  O   . HIS B 1 105 ? -1.958  -5.473  7.114   1.00 8.88  ? 105 HIS B O   1 
ATOM   3024 C  CB  . HIS B 1 105 ? -3.507  -4.099  9.586   1.00 8.30  ? 105 HIS B CB  1 
ATOM   3025 C  CG  . HIS B 1 105 ? -4.055  -2.911  10.279  1.00 7.82  ? 105 HIS B CG  1 
ATOM   3026 N  ND1 . HIS B 1 105 ? -4.994  -2.084  9.687   1.00 8.59  ? 105 HIS B ND1 1 
ATOM   3027 C  CD2 . HIS B 1 105 ? -3.753  -2.363  11.474  1.00 7.71  ? 105 HIS B CD2 1 
ATOM   3028 C  CE1 . HIS B 1 105 ? -5.233  -1.080  10.531  1.00 8.48  ? 105 HIS B CE1 1 
ATOM   3029 N  NE2 . HIS B 1 105 ? -4.483  -1.239  11.658  1.00 8.80  ? 105 HIS B NE2 1 
ATOM   3030 N  N   . THR B 1 106 ? -0.687  -5.510  9.000   1.00 8.55  ? 106 THR B N   1 
ATOM   3031 C  CA  . THR B 1 106 ? -0.055  -6.793  8.715   1.00 8.71  ? 106 THR B CA  1 
ATOM   3032 C  C   . THR B 1 106 ? -0.322  -7.712  9.893   1.00 8.69  ? 106 THR B C   1 
ATOM   3033 O  O   . THR B 1 106 ? -0.685  -7.260  10.960  1.00 9.43  ? 106 THR B O   1 
ATOM   3034 C  CB  . THR B 1 106 ? 1.427   -6.606  8.408   1.00 9.52  ? 106 THR B CB  1 
ATOM   3035 O  OG1 . THR B 1 106 ? 2.087   -6.043  9.543   1.00 10.09 ? 106 THR B OG1 1 
ATOM   3036 C  CG2 . THR B 1 106 ? 1.631   -5.720  7.195   1.00 11.58 ? 106 THR B CG2 1 
ATOM   3037 N  N   . VAL B 1 107 ? -0.221  -9.018  9.610   1.00 9.91  ? 107 VAL B N   1 
ATOM   3038 C  CA  . VAL B 1 107 ? -0.450  -9.983  10.682  1.00 12.50 ? 107 VAL B CA  1 
ATOM   3039 C  C   . VAL B 1 107 ? 0.767   -10.899 10.732  1.00 11.26 ? 107 VAL B C   1 
ATOM   3040 O  O   . VAL B 1 107 ? 1.140   -11.478 9.714   1.00 13.23 ? 107 VAL B O   1 
ATOM   3041 C  CB  . VAL B 1 107 ? -1.737  -10.816 10.475  1.00 11.80 ? 107 VAL B CB  1 
ATOM   3042 C  CG1 . VAL B 1 107 ? -1.871  -11.842 11.629  1.00 14.28 ? 107 VAL B CG1 1 
ATOM   3043 C  CG2 . VAL B 1 107 ? -3.019  -9.948  10.463  1.00 13.37 ? 107 VAL B CG2 1 
ATOM   3044 N  N   . SER B 1 108 ? 1.409   -10.809 11.912  1.00 12.58 ? 108 SER B N   1 
ATOM   3045 C  CA  . SER B 1 108 ? 2.673   -11.544 12.117  1.00 13.76 ? 108 SER B CA  1 
ATOM   3046 C  C   . SER B 1 108 ? 3.643   -11.285 10.958  1.00 13.38 ? 108 SER B C   1 
ATOM   3047 O  O   . SER B 1 108 ? 4.235   -12.187 10.342  1.00 14.68 ? 108 SER B O   1 
ATOM   3048 C  CB  . SER B 1 108 ? 2.413   -13.044 12.333  1.00 15.50 ? 108 SER B CB  1 
ATOM   3049 O  OG  . SER B 1 108 ? 1.597   -13.249 13.467  1.00 17.90 ? 108 SER B OG  1 
ATOM   3050 N  N   . GLY B 1 109 ? 3.742   -10.024 10.557  1.00 14.16 ? 109 GLY B N   1 
ATOM   3051 C  CA  . GLY B 1 109 ? 4.684   -9.576  9.553   1.00 14.71 ? 109 GLY B CA  1 
ATOM   3052 C  C   . GLY B 1 109 ? 4.226   -9.709  8.092   1.00 15.99 ? 109 GLY B C   1 
ATOM   3053 O  O   . GLY B 1 109 ? 4.986   -9.240  7.215   1.00 19.81 ? 109 GLY B O   1 
ATOM   3054 N  N   . GLN B 1 110 ? 3.045   -10.264 7.857   1.00 15.07 ? 110 GLN B N   1 
ATOM   3055 C  CA  . GLN B 1 110 ? 2.665   -10.540 6.474   1.00 16.95 ? 110 GLN B CA  1 
ATOM   3056 C  C   . GLN B 1 110 ? 1.589   -9.545  6.021   1.00 12.13 ? 110 GLN B C   1 
ATOM   3057 O  O   . GLN B 1 110 ? 0.606   -9.326  6.729   1.00 11.43 ? 110 GLN B O   1 
ATOM   3058 C  CB  . GLN B 1 110 ? 2.120   -11.961 6.355   1.00 20.38 ? 110 GLN B CB  1 
ATOM   3059 C  CG  . GLN B 1 110 ? 2.984   -13.010 7.085   1.00 21.14 ? 110 GLN B CG  1 
ATOM   3060 C  CD  . GLN B 1 110 ? 4.406   -13.026 6.584   1.00 28.26 ? 110 GLN B CD  1 
ATOM   3061 O  OE1 . GLN B 1 110 ? 4.655   -13.235 5.395   1.00 30.64 ? 110 GLN B OE1 1 
ATOM   3062 N  NE2 . GLN B 1 110 ? 5.345   -12.837 7.515   1.00 29.51 ? 110 GLN B NE2 1 
ATOM   3063 N  N   . HIS B 1 111 ? 1.805   -9.010  4.815   1.00 12.12 ? 111 HIS B N   1 
ATOM   3064 C  CA  . HIS B 1 111 ? 0.758   -8.245  4.151   1.00 11.12 ? 111 HIS B CA  1 
ATOM   3065 C  C   . HIS B 1 111 ? -0.246  -9.140  3.481   1.00 11.60 ? 111 HIS B C   1 
ATOM   3066 O  O   . HIS B 1 111 ? 0.086   -10.172 2.859   1.00 15.60 ? 111 HIS B O   1 
ATOM   3067 C  CB  . HIS B 1 111 ? 1.278   -7.406  2.960   1.00 13.15 ? 111 HIS B CB  1 
ATOM   3068 C  CG  . HIS B 1 111 ? 1.951   -6.148  3.383   1.00 12.79 ? 111 HIS B CG  1 
ATOM   3069 N  ND1 . HIS B 1 111 ? 1.306   -4.913  3.561   1.00 14.53 ? 111 HIS B ND1 1 
ATOM   3070 C  CD2 . HIS B 1 111 ? 3.234   -5.976  3.798   1.00 13.56 ? 111 HIS B CD2 1 
ATOM   3071 C  CE1 . HIS B 1 111 ? 2.227   -4.043  4.016   1.00 13.39 ? 111 HIS B CE1 1 
ATOM   3072 N  NE2 . HIS B 1 111 ? 3.408   -4.656  4.192   1.00 17.58 ? 111 HIS B NE2 1 
ATOM   3073 N  N   . PHE B 1 112 ? -1.496  -8.703  3.561   1.00 9.32  ? 112 PHE B N   1 
ATOM   3074 C  CA  . PHE B 1 112 ? -2.569  -9.212  2.737   1.00 9.39  ? 112 PHE B CA  1 
ATOM   3075 C  C   . PHE B 1 112 ? -2.583  -8.463  1.393   1.00 7.82  ? 112 PHE B C   1 
ATOM   3076 O  O   . PHE B 1 112 ? -1.835  -7.493  1.227   1.00 8.95  ? 112 PHE B O   1 
ATOM   3077 C  CB  . PHE B 1 112 ? -3.895  -9.136  3.503   1.00 11.40 ? 112 PHE B CB  1 
ATOM   3078 C  CG  . PHE B 1 112 ? -4.071  -10.190 4.567   1.00 12.66 ? 112 PHE B CG  1 
ATOM   3079 C  CD1 . PHE B 1 112 ? -3.531  -10.020 5.832   1.00 15.54 ? 112 PHE B CD1 1 
ATOM   3080 C  CD2 . PHE B 1 112 ? -4.775  -11.354 4.304   1.00 14.97 ? 112 PHE B CD2 1 
ATOM   3081 C  CE1 . PHE B 1 112 ? -3.693  -10.990 6.809   1.00 17.25 ? 112 PHE B CE1 1 
ATOM   3082 C  CE2 . PHE B 1 112 ? -4.936  -12.323 5.282   1.00 21.26 ? 112 PHE B CE2 1 
ATOM   3083 C  CZ  . PHE B 1 112 ? -4.395  -12.139 6.533   1.00 17.55 ? 112 PHE B CZ  1 
ATOM   3084 N  N   . ALA B 1 113 ? -3.394  -8.938  0.459   1.00 7.45  ? 113 ALA B N   1 
ATOM   3085 C  CA  . ALA B 1 113 ? -3.448  -8.361  -0.878  1.00 7.74  ? 113 ALA B CA  1 
ATOM   3086 C  C   . ALA B 1 113 ? -3.961  -6.929  -0.815  1.00 7.42  ? 113 ALA B C   1 
ATOM   3087 O  O   . ALA B 1 113 ? -3.472  -6.067  -1.553  1.00 8.22  ? 113 ALA B O   1 
ATOM   3088 C  CB  . ALA B 1 113 ? -4.300  -9.178  -1.818  1.00 9.21  ? 113 ALA B CB  1 
ATOM   3089 N  N   . ALA B 1 114 ? -4.955  -6.665  0.047   1.00 7.18  ? 114 ALA B N   1 
ATOM   3090 C  CA  . ALA B 1 114 ? -5.606  -5.350  0.054   1.00 6.03  ? 114 ALA B CA  1 
ATOM   3091 C  C   . ALA B 1 114 ? -6.358  -5.245  1.364   1.00 6.52  ? 114 ALA B C   1 
ATOM   3092 O  O   . ALA B 1 114 ? -6.327  -6.164  2.186   1.00 6.86  ? 114 ALA B O   1 
ATOM   3093 C  CB  . ALA B 1 114 ? -6.554  -5.213  -1.127  1.00 6.73  ? 114 ALA B CB  1 
ATOM   3094 N  N   . GLU B 1 115 ? -6.965  -4.067  1.584   1.00 6.37  ? 115 GLU B N   1 
ATOM   3095 C  CA  . GLU B 1 115 ? -7.692  -3.848  2.837   1.00 6.27  ? 115 GLU B CA  1 
ATOM   3096 C  C   . GLU B 1 115 ? -8.844  -2.887  2.588   1.00 7.00  ? 115 GLU B C   1 
ATOM   3097 O  O   . GLU B 1 115 ? -8.686  -1.874  1.851   1.00 7.32  ? 115 GLU B O   1 
ATOM   3098 C  CB  . GLU B 1 115 ? -6.741  -3.262  3.874   1.00 6.83  ? 115 GLU B CB  1 
ATOM   3099 C  CG  . GLU B 1 115 ? -7.272  -3.200  5.308   1.00 7.54  ? 115 GLU B CG  1 
ATOM   3100 C  CD  . GLU B 1 115 ? -6.201  -2.918  6.371   1.00 8.51  ? 115 GLU B CD  1 
ATOM   3101 O  OE1 . GLU B 1 115 ? -5.032  -3.386  6.162   1.00 8.25  ? 115 GLU B OE1 1 
ATOM   3102 O  OE2 . GLU B 1 115 ? -6.483  -2.292  7.421   1.00 8.20  ? 115 GLU B OE2 1 
ATOM   3103 N  N   . LEU B 1 116 ? -9.986  -3.213  3.185   1.00 6.19  ? 116 LEU B N   1 
ATOM   3104 C  CA  . LEU B 1 116 ? -11.179 -2.367  3.095   1.00 5.94  ? 116 LEU B CA  1 
ATOM   3105 C  C   . LEU B 1 116 ? -11.319 -1.655  4.428   1.00 5.89  ? 116 LEU B C   1 
ATOM   3106 O  O   . LEU B 1 116 ? -11.224 -2.314  5.506   1.00 6.05  ? 116 LEU B O   1 
ATOM   3107 C  CB  . LEU B 1 116 ? -12.435 -3.238  2.894   1.00 7.35  ? 116 LEU B CB  1 
ATOM   3108 C  CG  . LEU B 1 116 ? -13.769 -2.488  3.068   1.00 8.00  ? 116 LEU B CG  1 
ATOM   3109 C  CD1 . LEU B 1 116 ? -14.061 -1.623  1.830   1.00 9.00  ? 116 LEU B CD1 1 
ATOM   3110 C  CD2 . LEU B 1 116 ? -14.883 -3.491  3.259   1.00 9.20  ? 116 LEU B CD2 1 
ATOM   3111 N  N   . HIS B 1 117 ? -11.611 -0.342  4.407   1.00 5.58  ? 117 HIS B N   1 
ATOM   3112 C  CA  . HIS B 1 117 ? -11.934 0.401   5.628   1.00 5.83  ? 117 HIS B CA  1 
ATOM   3113 C  C   . HIS B 1 117 ? -13.330 0.963   5.512   1.00 5.95  ? 117 HIS B C   1 
ATOM   3114 O  O   . HIS B 1 117 ? -13.632 1.691   4.560   1.00 6.27  ? 117 HIS B O   1 
ATOM   3115 C  CB  . HIS B 1 117 ? -10.950 1.582   5.757   1.00 5.95  ? 117 HIS B CB  1 
ATOM   3116 C  CG  . HIS B 1 117 ? -9.583  1.095   6.090   1.00 6.02  ? 117 HIS B CG  1 
ATOM   3117 N  ND1 . HIS B 1 117 ? -8.403  1.848   5.825   1.00 6.14  ? 117 HIS B ND1 1 
ATOM   3118 C  CD2 . HIS B 1 117 ? -9.201  -0.082  6.673   1.00 6.65  ? 117 HIS B CD2 1 
ATOM   3119 C  CE1 . HIS B 1 117 ? -7.383  1.112   6.252   1.00 6.77  ? 117 HIS B CE1 1 
ATOM   3120 N  NE2 . HIS B 1 117 ? -7.824  -0.068  6.771   1.00 6.81  ? 117 HIS B NE2 1 
ATOM   3121 N  N   . ILE B 1 118 ? -14.125 0.716   6.560   1.00 6.00  ? 118 ILE B N   1 
ATOM   3122 C  CA  . ILE B 1 118 ? -15.461 1.338   6.611   1.00 6.77  ? 118 ILE B CA  1 
ATOM   3123 C  C   . ILE B 1 118 ? -15.438 2.339   7.745   1.00 6.99  ? 118 ILE B C   1 
ATOM   3124 O  O   . ILE B 1 118 ? -15.286 1.967   8.943   1.00 6.79  ? 118 ILE B O   1 
ATOM   3125 C  CB  . ILE B 1 118 ? -16.566 0.281   6.814   1.00 7.24  ? 118 ILE B CB  1 
ATOM   3126 C  CG1 . ILE B 1 118 ? -16.459 -0.892  5.838   1.00 7.32  ? 118 ILE B CG1 1 
ATOM   3127 C  CG2 . ILE B 1 118 ? -17.936 0.996   6.694   1.00 7.68  ? 118 ILE B CG2 1 
ATOM   3128 C  CD1 . ILE B 1 118 ? -17.555 -1.983  6.077   1.00 8.59  ? 118 ILE B CD1 1 
ATOM   3129 N  N   . VAL B 1 119 ? -15.432 3.631   7.380   1.00 7.03  ? 119 VAL B N   1 
ATOM   3130 C  CA  . VAL B 1 119 ? -15.258 4.722   8.340   1.00 7.18  ? 119 VAL B CA  1 
ATOM   3131 C  C   . VAL B 1 119 ? -16.606 5.156   8.922   1.00 7.10  ? 119 VAL B C   1 
ATOM   3132 O  O   . VAL B 1 119 ? -17.539 5.407   8.155   1.00 8.23  ? 119 VAL B O   1 
ATOM   3133 C  CB  . VAL B 1 119 ? -14.595 5.918   7.620   1.00 7.87  ? 119 VAL B CB  1 
ATOM   3134 C  CG1 . VAL B 1 119 ? -14.263 7.045   8.594   1.00 9.52  ? 119 VAL B CG1 1 
ATOM   3135 C  CG2 . VAL B 1 119 ? -13.313 5.480   6.872   1.00 8.35  ? 119 VAL B CG2 1 
ATOM   3136 N  N   . HIS B 1 120 ? -16.639 5.252   10.242  1.00 7.65  ? 120 HIS B N   1 
ATOM   3137 C  CA  . HIS B 1 120 ? -17.814 5.702   10.985  1.00 8.36  ? 120 HIS B CA  1 
ATOM   3138 C  C   . HIS B 1 120 ? -17.368 6.823   11.917  1.00 8.71  ? 120 HIS B C   1 
ATOM   3139 O  O   . HIS B 1 120 ? -16.205 6.986   12.279  1.00 9.54  ? 120 HIS B O   1 
ATOM   3140 C  CB  . HIS B 1 120 ? -18.371 4.556   11.836  1.00 8.24  ? 120 HIS B CB  1 
ATOM   3141 C  CG  . HIS B 1 120 ? -18.793 3.328   11.141  1.00 7.99  ? 120 HIS B CG  1 
ATOM   3142 N  ND1 . HIS B 1 120 ? -17.839 2.456   10.571  1.00 8.90  ? 120 HIS B ND1 1 
ATOM   3143 C  CD2 . HIS B 1 120 ? -20.000 2.752   10.919  1.00 9.18  ? 120 HIS B CD2 1 
ATOM   3144 C  CE1 . HIS B 1 120 ? -18.476 1.430   10.034  1.00 9.65  ? 120 HIS B CE1 1 
ATOM   3145 N  NE2 . HIS B 1 120 ? -19.817 1.571   10.246  1.00 9.60  ? 120 HIS B NE2 1 
ATOM   3146 N  N   . TYR B 1 121 ? -18.355 7.650   12.321  1.00 10.00 ? 121 TYR B N   1 
ATOM   3147 C  CA  . TYR B 1 121 ? -18.103 8.740   13.245  1.00 11.12 ? 121 TYR B CA  1 
ATOM   3148 C  C   . TYR B 1 121 ? -19.130 8.717   14.385  1.00 11.76 ? 121 TYR B C   1 
ATOM   3149 O  O   . TYR B 1 121 ? -20.188 8.167   14.263  1.00 11.28 ? 121 TYR B O   1 
ATOM   3150 C  CB  . TYR B 1 121 ? -18.132 10.108  12.541  1.00 11.87 ? 121 TYR B CB  1 
ATOM   3151 C  CG  . TYR B 1 121 ? -19.491 10.559  12.056  1.00 13.06 ? 121 TYR B CG  1 
ATOM   3152 C  CD1 . TYR B 1 121 ? -20.034 10.026  10.908  1.00 15.53 ? 121 TYR B CD1 1 
ATOM   3153 C  CD2 . TYR B 1 121 ? -20.249 11.443  12.815  1.00 15.37 ? 121 TYR B CD2 1 
ATOM   3154 C  CE1 . TYR B 1 121 ? -21.278 10.417  10.449  1.00 16.56 ? 121 TYR B CE1 1 
ATOM   3155 C  CE2 . TYR B 1 121 ? -21.516 11.830  12.373  1.00 16.40 ? 121 TYR B CE2 1 
ATOM   3156 C  CZ  . TYR B 1 121 ? -22.011 11.296  11.206  1.00 19.66 ? 121 TYR B CZ  1 
ATOM   3157 O  OH  . TYR B 1 121 ? -23.264 11.642  10.783  1.00 22.23 ? 121 TYR B OH  1 
ATOM   3158 N  N   . ASN B 1 122 ? -18.735 9.277   15.529  1.00 11.99 ? 122 ASN B N   1 
ATOM   3159 C  CA  . ASN B 1 122 ? -19.616 9.329   16.697  1.00 13.13 ? 122 ASN B CA  1 
ATOM   3160 C  C   . ASN B 1 122 ? -20.758 10.348  16.457  1.00 13.13 ? 122 ASN B C   1 
ATOM   3161 O  O   . ASN B 1 122 ? -20.560 11.560  16.651  1.00 15.26 ? 122 ASN B O   1 
ATOM   3162 C  CB  . ASN B 1 122 ? -18.785 9.615   17.945  1.00 14.25 ? 122 ASN B CB  1 
ATOM   3163 C  CG  . ASN B 1 122 ? -19.634 9.555   19.198  1.00 18.86 ? 122 ASN B CG  1 
ATOM   3164 O  OD1 . ASN B 1 122 ? -20.845 9.660   19.134  1.00 18.19 ? 122 ASN B OD1 1 
ATOM   3165 N  ND2 . ASN B 1 122 ? -18.977 9.323   20.321  1.00 21.35 ? 122 ASN B ND2 1 
ATOM   3166 N  N   . SER B 1 123 ? -21.914 9.846   16.028  1.00 16.48 ? 123 SER B N   1 
ATOM   3167 C  CA  . SER B 1 123 ? -23.046 10.683  15.640  1.00 18.26 ? 123 SER B CA  1 
ATOM   3168 C  C   . SER B 1 123 ? -23.884 11.085  16.858  1.00 22.67 ? 123 SER B C   1 
ATOM   3169 O  O   . SER B 1 123 ? -24.748 11.977  16.748  1.00 19.80 ? 123 SER B O   1 
ATOM   3170 C  CB  . SER B 1 123 ? -23.884 10.026  14.557  1.00 16.99 ? 123 SER B CB  1 
ATOM   3171 O  OG  . SER B 1 123 ? -24.191 8.694   14.872  1.00 17.12 ? 123 SER B OG  1 
ATOM   3172 N  N   . ASP B 1 124 ? -23.610 10.435  17.986  1.00 20.49 ? 124 ASP B N   1 
ATOM   3173 C  CA  . ASP B 1 124 ? -24.229 10.821  19.254  1.00 21.05 ? 124 ASP B CA  1 
ATOM   3174 C  C   . ASP B 1 124 ? -23.686 12.193  19.672  1.00 23.03 ? 124 ASP B C   1 
ATOM   3175 O  O   . ASP B 1 124 ? -24.449 13.051  20.127  1.00 21.51 ? 124 ASP B O   1 
ATOM   3176 C  CB  . ASP B 1 124 ? -24.068 9.717   20.315  1.00 19.80 ? 124 ASP B CB  1 
ATOM   3177 C  CG  . ASP B 1 124 ? -24.946 8.474   20.185  1.00 20.42 ? 124 ASP B CG  1 
ATOM   3178 O  OD1 . ASP B 1 124 ? -25.922 8.491   19.398  1.00 25.67 ? 124 ASP B OD1 1 
ATOM   3179 O  OD2 . ASP B 1 124 ? -24.665 7.488   20.908  1.00 24.81 ? 124 ASP B OD2 1 
ATOM   3180 N  N   . LEU B 1 125 ? -22.384 12.430  19.458  1.00 20.79 ? 125 LEU B N   1 
ATOM   3181 C  CA  . LEU B 1 125 ? -21.648 13.610  19.892  1.00 19.60 ? 125 LEU B CA  1 
ATOM   3182 C  C   . LEU B 1 125 ? -21.480 14.647  18.783  1.00 23.58 ? 125 LEU B C   1 
ATOM   3183 O  O   . LEU B 1 125 ? -21.439 15.845  19.061  1.00 23.12 ? 125 LEU B O   1 
ATOM   3184 C  CB  . LEU B 1 125 ? -20.296 13.245  20.509  1.00 20.98 ? 125 LEU B CB  1 
ATOM   3185 C  CG  . LEU B 1 125 ? -20.336 12.353  21.747  1.00 21.51 ? 125 LEU B CG  1 
ATOM   3186 C  CD1 . LEU B 1 125 ? -18.931 12.161  22.289  1.00 20.99 ? 125 LEU B CD1 1 
ATOM   3187 C  CD2 . LEU B 1 125 ? -21.187 13.000  22.848  1.00 23.41 ? 125 LEU B CD2 1 
ATOM   3188 N  N   . TYR B 1 126 ? -21.339 14.215  17.530  1.00 19.49 ? 126 TYR B N   1 
ATOM   3189 C  CA  . TYR B 1 126 ? -20.891 15.135  16.490  1.00 19.63 ? 126 TYR B CA  1 
ATOM   3190 C  C   . TYR B 1 126 ? -21.867 15.162  15.325  1.00 21.13 ? 126 TYR B C   1 
ATOM   3191 O  O   . TYR B 1 126 ? -22.514 14.165  15.024  1.00 20.50 ? 126 TYR B O   1 
ATOM   3192 C  CB  . TYR B 1 126 ? -19.433 14.836  16.073  1.00 18.90 ? 126 TYR B CB  1 
ATOM   3193 C  CG  . TYR B 1 126 ? -18.524 14.709  17.259  1.00 19.57 ? 126 TYR B CG  1 
ATOM   3194 C  CD1 . TYR B 1 126 ? -18.254 15.825  18.043  1.00 24.95 ? 126 TYR B CD1 1 
ATOM   3195 C  CD2 . TYR B 1 126 ? -17.975 13.486  17.628  1.00 18.62 ? 126 TYR B CD2 1 
ATOM   3196 C  CE1 . TYR B 1 126 ? -17.454 15.724  19.166  1.00 22.68 ? 126 TYR B CE1 1 
ATOM   3197 C  CE2 . TYR B 1 126 ? -17.178 13.371  18.753  1.00 20.86 ? 126 TYR B CE2 1 
ATOM   3198 C  CZ  . TYR B 1 126 ? -16.911 14.501  19.512  1.00 24.85 ? 126 TYR B CZ  1 
ATOM   3199 O  OH  . TYR B 1 126 ? -16.107 14.405  20.609  1.00 25.76 ? 126 TYR B OH  1 
ATOM   3200 N  N   . PRO B 1 127 ? -21.995 16.318  14.635  1.00 25.19 ? 127 PRO B N   1 
ATOM   3201 C  CA  . PRO B 1 127 ? -22.965 16.438  13.550  1.00 24.84 ? 127 PRO B CA  1 
ATOM   3202 C  C   . PRO B 1 127 ? -22.491 15.931  12.190  1.00 24.57 ? 127 PRO B C   1 
ATOM   3203 O  O   . PRO B 1 127 ? -23.306 15.802  11.269  1.00 31.81 ? 127 PRO B O   1 
ATOM   3204 C  CB  . PRO B 1 127 ? -23.198 17.960  13.479  1.00 28.67 ? 127 PRO B CB  1 
ATOM   3205 C  CG  . PRO B 1 127 ? -21.900 18.574  13.943  1.00 29.40 ? 127 PRO B CG  1 
ATOM   3206 C  CD  . PRO B 1 127 ? -21.296 17.587  14.928  1.00 26.20 ? 127 PRO B CD  1 
ATOM   3207 N  N   . ASP B 1 128 ? -21.198 15.574  12.101  1.00 21.54 ? 128 ASP B N   1 
ATOM   3208 C  CA  . ASP B 1 128 ? -20.624 15.087  10.857  1.00 19.69 ? 128 ASP B CA  1 
ATOM   3209 C  C   . ASP B 1 128 ? -19.231 14.542  11.135  1.00 20.57 ? 128 ASP B C   1 
ATOM   3210 O  O   . ASP B 1 128 ? -18.661 14.758  12.188  1.00 18.90 ? 128 ASP B O   1 
ATOM   3211 C  CB  . ASP B 1 128 ? -20.513 16.258  9.869   1.00 21.99 ? 128 ASP B CB  1 
ATOM   3212 C  CG  . ASP B 1 128 ? -19.611 17.317  10.435  1.00 26.01 ? 128 ASP B CG  1 
ATOM   3213 O  OD1 . ASP B 1 128 ? -20.061 18.033  11.385  1.00 30.38 ? 128 ASP B OD1 1 
ATOM   3214 O  OD2 . ASP B 1 128 ? -18.477 17.409  9.951   1.00 30.12 ? 128 ASP B OD2 1 
ATOM   3215 N  N   . ALA B 1 129 ? -18.709 13.768  10.186  1.00 19.95 ? 129 ALA B N   1 
ATOM   3216 C  CA  . ALA B 1 129 ? -17.485 13.029  10.364  1.00 18.96 ? 129 ALA B CA  1 
ATOM   3217 C  C   . ALA B 1 129 ? -16.293 13.984  10.434  1.00 18.58 ? 129 ALA B C   1 
ATOM   3218 O  O   . ALA B 1 129 ? -15.340 13.753  11.145  1.00 18.75 ? 129 ALA B O   1 
ATOM   3219 C  CB  . ALA B 1 129 ? -17.390 12.052  9.192   1.00 20.36 ? 129 ALA B CB  1 
ATOM   3220 N  N   . SER B 1 130 ? -16.328 15.095  9.681   1.00 19.84 ? 130 SER B N   1 
ATOM   3221 C  CA  . SER B 1 130 ? -15.191 16.017  9.691   1.00 21.11 ? 130 SER B CA  1 
ATOM   3222 C  C   . SER B 1 130 ? -14.996 16.596  11.106  1.00 21.37 ? 130 SER B C   1 
ATOM   3223 O  O   . SER B 1 130 ? -13.887 16.636  11.649  1.00 20.63 ? 130 SER B O   1 
ATOM   3224 C  CB  . SER B 1 130 ? -15.363 17.083  8.611   1.00 23.06 ? 130 SER B CB  1 
ATOM   3225 O  OG  . SER B 1 130 ? -14.231 17.937  8.556   1.00 28.87 ? 130 SER B OG  1 
ATOM   3226 N  N   . THR B 1 131 ? -16.087 17.049  11.735  1.00 21.36 ? 131 THR B N   1 
ATOM   3227 C  CA  . THR B 1 131 ? -16.023 17.523  13.111  1.00 23.12 ? 131 THR B CA  1 
ATOM   3228 C  C   . THR B 1 131 ? -15.497 16.459  14.068  1.00 24.06 ? 131 THR B C   1 
ATOM   3229 O  O   . THR B 1 131 ? -14.655 16.762  14.917  1.00 24.55 ? 131 THR B O   1 
ATOM   3230 C  CB  . THR B 1 131 ? -17.422 17.909  13.602  1.00 25.01 ? 131 THR B CB  1 
ATOM   3231 O  OG1 . THR B 1 131 ? -17.848 18.973  12.750  1.00 25.29 ? 131 THR B OG1 1 
ATOM   3232 C  CG2 . THR B 1 131 ? -17.439 18.304  15.070  1.00 24.15 ? 131 THR B CG2 1 
ATOM   3233 N  N   . ALA B 1 132 ? -16.031 15.221  13.958  1.00 18.85 ? 132 ALA B N   1 
ATOM   3234 C  CA  . ALA B 1 132 ? -15.617 14.100  14.792  1.00 17.42 ? 132 ALA B CA  1 
ATOM   3235 C  C   . ALA B 1 132 ? -14.127 13.790  14.606  1.00 17.13 ? 132 ALA B C   1 
ATOM   3236 O  O   . ALA B 1 132 ? -13.551 13.288  15.551  1.00 15.62 ? 132 ALA B O   1 
ATOM   3237 C  CB  . ALA B 1 132 ? -16.444 12.858  14.531  1.00 16.00 ? 132 ALA B CB  1 
ATOM   3238 N  N   . SER B 1 133 ? -13.542 14.098  13.434  1.00 17.34 ? 133 SER B N   1 
ATOM   3239 C  CA  . SER B 1 133 ? -12.245 13.540  13.051  1.00 17.94 ? 133 SER B CA  1 
ATOM   3240 C  C   . SER B 1 133 ? -11.121 14.140  13.869  1.00 20.08 ? 133 SER B C   1 
ATOM   3241 O  O   . SER B 1 133 ? -10.004 13.618  13.899  1.00 18.99 ? 133 SER B O   1 
ATOM   3242 C  CB  . SER B 1 133 ? -11.991 13.704  11.585  1.00 19.79 ? 133 SER B CB  1 
ATOM   3243 O  OG  . SER B 1 133 ? -11.672 15.063  11.264  1.00 21.02 ? 133 SER B OG  1 
ATOM   3244 N  N   . ASN B 1 134 ? -11.451 15.225  14.564  1.00 21.08 ? 134 ASN B N   1 
ATOM   3245 C  CA  . ASN B 1 134 ? -10.512 15.984  15.374  1.00 23.84 ? 134 ASN B CA  1 
ATOM   3246 C  C   . ASN B 1 134 ? -10.676 15.677  16.854  1.00 23.57 ? 134 ASN B C   1 
ATOM   3247 O  O   . ASN B 1 134 ? -10.002 16.312  17.665  1.00 29.11 ? 134 ASN B O   1 
ATOM   3248 C  CB  . ASN B 1 134 ? -10.809 17.492  15.277  1.00 29.68 ? 134 ASN B CB  1 
ATOM   3249 C  CG  . ASN B 1 134 ? -10.457 18.020  13.910  1.00 33.93 ? 134 ASN B CG  1 
ATOM   3250 O  OD1 . ASN B 1 134 ? -9.351  17.775  13.435  1.00 38.57 ? 134 ASN B OD1 1 
ATOM   3251 N  ND2 . ASN B 1 134 ? -11.400 18.681  13.261  1.00 42.11 ? 134 ASN B ND2 1 
ATOM   3252 N  N   . LYS B 1 135 ? -11.584 14.771  17.234  1.00 21.84 ? 135 LYS B N   1 
ATOM   3253 C  CA  . LYS B 1 135 ? -11.924 14.567  18.650  1.00 23.84 ? 135 LYS B CA  1 
ATOM   3254 C  C   . LYS B 1 135 ? -11.584 13.151  19.090  1.00 25.35 ? 135 LYS B C   1 
ATOM   3255 O  O   . LYS B 1 135 ? -11.721 12.239  18.307  1.00 23.17 ? 135 LYS B O   1 
ATOM   3256 C  CB  . LYS B 1 135 ? -13.435 14.658  18.864  1.00 29.33 ? 135 LYS B CB  1 
ATOM   3257 C  CG  . LYS B 1 135 ? -14.115 15.858  18.217  1.00 31.07 ? 135 LYS B CG  1 
ATOM   3258 C  CD  . LYS B 1 135 ? -14.008 17.131  19.031  1.00 37.23 ? 135 LYS B CD  1 
ATOM   3259 C  CE  . LYS B 1 135 ? -14.806 18.264  18.420  1.00 37.72 ? 135 LYS B CE  1 
ATOM   3260 N  NZ  . LYS B 1 135 ? -14.155 18.813  17.205  1.00 43.11 ? 135 LYS B NZ  1 
ATOM   3261 N  N   . SER B 1 136 ? -11.199 12.928  20.361  1.00 28.71 ? 136 SER B N   1 
ATOM   3262 C  CA  . SER B 1 136 ? -10.699 11.616  20.763  1.00 31.54 ? 136 SER B CA  1 
ATOM   3263 C  C   . SER B 1 136 ? -11.819 10.578  20.596  1.00 24.70 ? 136 SER B C   1 
ATOM   3264 O  O   . SER B 1 136 ? -12.958 10.861  20.901  1.00 21.64 ? 136 SER B O   1 
ATOM   3265 C  CB  . SER B 1 136 ? -10.184 11.657  22.198  1.00 39.40 ? 136 SER B CB  1 
ATOM   3266 O  OG  . SER B 1 136 ? -11.273 11.569  23.119  1.00 43.58 ? 136 SER B OG  1 
ATOM   3267 N  N   . GLU B 1 137 ? -11.481 9.391   20.073  1.00 24.57 ? 137 GLU B N   1 
ATOM   3268 C  CA  . GLU B 1 137 ? -12.444 8.372   19.650  1.00 26.62 ? 137 GLU B CA  1 
ATOM   3269 C  C   . GLU B 1 137 ? -13.652 8.916   18.865  1.00 20.47 ? 137 GLU B C   1 
ATOM   3270 O  O   . GLU B 1 137 ? -14.748 8.319   18.908  1.00 21.47 ? 137 GLU B O   1 
ATOM   3271 C  CB  . GLU B 1 137 ? -12.862 7.476   20.829  1.00 33.49 ? 137 GLU B CB  1 
ATOM   3272 C  CG  . GLU B 1 137 ? -13.563 8.199   21.979  1.00 47.71 ? 137 GLU B CG  1 
ATOM   3273 C  CD  . GLU B 1 137 ? -13.179 7.722   23.379  1.00 56.74 ? 137 GLU B CD  1 
ATOM   3274 O  OE1 . GLU B 1 137 ? -13.072 6.486   23.590  1.00 57.55 ? 137 GLU B OE1 1 
ATOM   3275 O  OE2 . GLU B 1 137 ? -12.974 8.589   24.264  1.00 56.78 ? 137 GLU B OE2 1 
ATOM   3276 N  N   . GLY B 1 138 ? -13.475 10.033  18.131  1.00 15.39 ? 138 GLY B N   1 
ATOM   3277 C  CA  . GLY B 1 138 ? -14.468 10.584  17.230  1.00 13.55 ? 138 GLY B CA  1 
ATOM   3278 C  C   . GLY B 1 138 ? -14.798 9.619   16.093  1.00 11.10 ? 138 GLY B C   1 
ATOM   3279 O  O   . GLY B 1 138 ? -15.878 9.689   15.526  1.00 12.24 ? 138 GLY B O   1 
ATOM   3280 N  N   . LEU B 1 139 ? -13.814 8.809   15.658  1.00 10.32 ? 139 LEU B N   1 
ATOM   3281 C  CA  . LEU B 1 139 ? -14.052 7.910   14.521  1.00 9.80  ? 139 LEU B CA  1 
ATOM   3282 C  C   . LEU B 1 139 ? -13.916 6.465   14.959  1.00 9.22  ? 139 LEU B C   1 
ATOM   3283 O  O   . LEU B 1 139 ? -13.126 6.162   15.876  1.00 9.60  ? 139 LEU B O   1 
ATOM   3284 C  CB  . LEU B 1 139 ? -13.032 8.179   13.415  1.00 10.40 ? 139 LEU B CB  1 
ATOM   3285 C  CG  . LEU B 1 139 ? -13.037 9.620   12.889  1.00 9.37  ? 139 LEU B CG  1 
ATOM   3286 C  CD1 . LEU B 1 139 ? -11.850 9.821   11.926  1.00 11.34 ? 139 LEU B CD1 1 
ATOM   3287 C  CD2 . LEU B 1 139 ? -14.370 9.989   12.226  1.00 11.68 ? 139 LEU B CD2 1 
ATOM   3288 N  N   . ALA B 1 140 ? -14.595 5.565   14.235  1.00 9.10  ? 140 ALA B N   1 
ATOM   3289 C  CA  . ALA B 1 140 ? -14.392 4.138   14.428  1.00 8.86  ? 140 ALA B CA  1 
ATOM   3290 C  C   . ALA B 1 140 ? -14.290 3.561   13.030  1.00 8.68  ? 140 ALA B C   1 
ATOM   3291 O  O   . ALA B 1 140 ? -15.176 3.806   12.175  1.00 9.58  ? 140 ALA B O   1 
ATOM   3292 C  CB  . ALA B 1 140 ? -15.527 3.496   15.195  1.00 9.75  ? 140 ALA B CB  1 
ATOM   3293 N  N   . VAL B 1 141 ? -13.243 2.767   12.785  1.00 7.89  ? 141 VAL B N   1 
ATOM   3294 C  CA  . VAL B 1 141 ? -13.106 2.193   11.469  1.00 7.25  ? 141 VAL B CA  1 
ATOM   3295 C  C   . VAL B 1 141 ? -13.183 0.681   11.592  1.00 7.68  ? 141 VAL B C   1 
ATOM   3296 O  O   . VAL B 1 141 ? -12.548 0.115   12.475  1.00 8.63  ? 141 VAL B O   1 
ATOM   3297 C  CB  . VAL B 1 141 ? -11.765 2.600   10.818  1.00 8.24  ? 141 VAL B CB  1 
ATOM   3298 C  CG1 . VAL B 1 141 ? -11.600 1.900   9.443   1.00 9.49  ? 141 VAL B CG1 1 
ATOM   3299 C  CG2 . VAL B 1 141 ? -11.747 4.098   10.627  1.00 9.68  ? 141 VAL B CG2 1 
ATOM   3300 N  N   . LEU B 1 142 ? -13.883 0.026   10.692  1.00 6.39  ? 142 LEU B N   1 
ATOM   3301 C  CA  . LEU B 1 142 ? -13.831 -1.420  10.546  1.00 7.24  ? 142 LEU B CA  1 
ATOM   3302 C  C   . LEU B 1 142 ? -12.883 -1.740  9.411   1.00 7.11  ? 142 LEU B C   1 
ATOM   3303 O  O   . LEU B 1 142 ? -13.029 -1.199  8.303   1.00 8.20  ? 142 LEU B O   1 
ATOM   3304 C  CB  . LEU B 1 142 ? -15.198 -1.986  10.202  1.00 8.21  ? 142 LEU B CB  1 
ATOM   3305 C  CG  . LEU B 1 142 ? -16.365 -1.659  11.121  1.00 8.81  ? 142 LEU B CG  1 
ATOM   3306 C  CD1 . LEU B 1 142 ? -17.644 -2.330  10.614  1.00 11.91 ? 142 LEU B CD1 1 
ATOM   3307 C  CD2 . LEU B 1 142 ? -16.068 -2.064  12.571  1.00 10.57 ? 142 LEU B CD2 1 
ATOM   3308 N  N   . ALA B 1 143 ? -11.935 -2.620  9.663   1.00 7.00  ? 143 ALA B N   1 
ATOM   3309 C  CA  . ALA B 1 143 ? -10.968 -3.000  8.664   1.00 6.78  ? 143 ALA B CA  1 
ATOM   3310 C  C   . ALA B 1 143 ? -11.104 -4.469  8.313   1.00 6.36  ? 143 ALA B C   1 
ATOM   3311 O  O   . ALA B 1 143 ? -11.196 -5.332  9.215   1.00 6.72  ? 143 ALA B O   1 
ATOM   3312 C  CB  . ALA B 1 143 ? -9.560  -2.735  9.160   1.00 7.48  ? 143 ALA B CB  1 
ATOM   3313 N  N   . VAL B 1 144 ? -11.205 -4.751  7.008   1.00 6.21  ? 144 VAL B N   1 
ATOM   3314 C  CA  . VAL B 1 144 ? -11.304 -6.120  6.529   1.00 6.48  ? 144 VAL B CA  1 
ATOM   3315 C  C   . VAL B 1 144 ? -10.055 -6.364  5.703   1.00 6.70  ? 144 VAL B C   1 
ATOM   3316 O  O   . VAL B 1 144 ? -9.776  -5.640  4.715   1.00 6.61  ? 144 VAL B O   1 
ATOM   3317 C  CB  . VAL B 1 144 ? -12.546 -6.308  5.629   1.00 6.74  ? 144 VAL B CB  1 
ATOM   3318 C  CG1 . VAL B 1 144 ? -12.625 -7.753  5.156   1.00 7.92  ? 144 VAL B CG1 1 
ATOM   3319 C  CG2 . VAL B 1 144 ? -13.825 -5.942  6.373   1.00 7.95  ? 144 VAL B CG2 1 
ATOM   3320 N  N   . LEU B 1 145 ? -9.318  -7.399  6.072   1.00 6.74  ? 145 LEU B N   1 
ATOM   3321 C  CA  . LEU B 1 145 ? -8.152  -7.848  5.334   1.00 6.93  ? 145 LEU B CA  1 
ATOM   3322 C  C   . LEU B 1 145 ? -8.603  -8.642  4.129   1.00 7.00  ? 145 LEU B C   1 
ATOM   3323 O  O   . LEU B 1 145 ? -9.533  -9.459  4.234   1.00 7.87  ? 145 LEU B O   1 
ATOM   3324 C  CB  . LEU B 1 145 ? -7.283  -8.697  6.260   1.00 8.58  ? 145 LEU B CB  1 
ATOM   3325 C  CG  . LEU B 1 145 ? -6.768  -7.976  7.497   1.00 10.26 ? 145 LEU B CG  1 
ATOM   3326 C  CD1 . LEU B 1 145 ? -6.180  -8.966  8.510   1.00 11.55 ? 145 LEU B CD1 1 
ATOM   3327 C  CD2 . LEU B 1 145 ? -5.714  -6.972  7.116   1.00 13.27 ? 145 LEU B CD2 1 
ATOM   3328 N  N   . ILE B 1 146 ? -7.997  -8.420  2.964   1.00 7.59  ? 146 ILE B N   1 
ATOM   3329 C  CA  . ILE B 1 146 ? -8.445  -9.049  1.730   1.00 7.92  ? 146 ILE B CA  1 
ATOM   3330 C  C   . ILE B 1 146 ? -7.287  -9.891  1.186   1.00 7.35  ? 146 ILE B C   1 
ATOM   3331 O  O   . ILE B 1 146 ? -6.161  -9.383  0.991   1.00 8.02  ? 146 ILE B O   1 
ATOM   3332 C  CB  . ILE B 1 146 ? -8.821  -7.993  0.690   1.00 7.84  ? 146 ILE B CB  1 
ATOM   3333 C  CG1 . ILE B 1 146 ? -9.978  -7.170  1.235   1.00 8.19  ? 146 ILE B CG1 1 
ATOM   3334 C  CG2 . ILE B 1 146 ? -9.161  -8.660  -0.646  1.00 8.24  ? 146 ILE B CG2 1 
ATOM   3335 C  CD1 . ILE B 1 146 ? -10.259 -5.897  0.432   1.00 9.57  ? 146 ILE B CD1 1 
ATOM   3336 N  N   A GLU B 1 147 ? -7.611  -11.145 0.863   0.50 7.87  ? 147 GLU B N   1 
ATOM   3337 N  N   B GLU B 1 147 ? -7.529  -11.166 0.918   0.50 8.48  ? 147 GLU B N   1 
ATOM   3338 C  CA  A GLU B 1 147 ? -6.656  -12.135 0.355   0.50 8.99  ? 147 GLU B CA  1 
ATOM   3339 C  CA  B GLU B 1 147 ? -6.467  -11.931 0.266   0.50 9.96  ? 147 GLU B CA  1 
ATOM   3340 C  C   A GLU B 1 147 ? -6.998  -12.474 -1.097  0.50 8.01  ? 147 GLU B C   1 
ATOM   3341 C  C   B GLU B 1 147 ? -6.946  -12.366 -1.106  0.50 8.54  ? 147 GLU B C   1 
ATOM   3342 O  O   A GLU B 1 147 ? -8.184  -12.485 -1.479  0.50 8.07  ? 147 GLU B O   1 
ATOM   3343 O  O   B GLU B 1 147 ? -8.146  -12.352 -1.410  0.50 8.95  ? 147 GLU B O   1 
ATOM   3344 C  CB  A GLU B 1 147 ? -6.584  -13.338 1.312   0.50 11.60 ? 147 GLU B CB  1 
ATOM   3345 C  CB  B GLU B 1 147 ? -6.051  -13.174 1.061   0.50 14.62 ? 147 GLU B CB  1 
ATOM   3346 C  CG  A GLU B 1 147 ? -7.592  -14.412 1.142   0.50 14.98 ? 147 GLU B CG  1 
ATOM   3347 C  CG  B GLU B 1 147 ? -4.695  -13.729 0.612   0.50 17.91 ? 147 GLU B CG  1 
ATOM   3348 C  CD  A GLU B 1 147 ? -7.312  -15.456 2.229   0.50 16.20 ? 147 GLU B CD  1 
ATOM   3349 C  CD  B GLU B 1 147 ? -3.606  -12.728 0.238   0.50 17.21 ? 147 GLU B CD  1 
ATOM   3350 O  OE1 A GLU B 1 147 ? -6.233  -15.331 2.904   0.50 15.21 ? 147 GLU B OE1 1 
ATOM   3351 O  OE1 B GLU B 1 147 ? -3.223  -12.655 -0.993  0.50 12.83 ? 147 GLU B OE1 1 
ATOM   3352 O  OE2 A GLU B 1 147 ? -8.184  -16.333 2.454   0.50 20.69 ? 147 GLU B OE2 1 
ATOM   3353 O  OE2 B GLU B 1 147 ? -3.114  -12.064 1.206   0.50 14.67 ? 147 GLU B OE2 1 
ATOM   3354 N  N   . MET B 1 148 ? -5.992  -12.779 -1.917  1.00 8.69  ? 148 MET B N   1 
ATOM   3355 C  CA  . MET B 1 148 ? -6.256  -13.290 -3.247  1.00 9.18  ? 148 MET B CA  1 
ATOM   3356 C  C   . MET B 1 148 ? -6.833  -14.701 -3.155  1.00 9.63  ? 148 MET B C   1 
ATOM   3357 O  O   . MET B 1 148 ? -6.265  -15.573 -2.505  1.00 10.50 ? 148 MET B O   1 
ATOM   3358 C  CB  . MET B 1 148 ? -4.948  -13.337 -4.036  1.00 10.11 ? 148 MET B CB  1 
ATOM   3359 C  CG  . MET B 1 148 ? -5.162  -13.715 -5.501  1.00 10.69 ? 148 MET B CG  1 
ATOM   3360 S  SD  . MET B 1 148 ? -3.673  -13.824 -6.466  1.00 13.42 ? 148 MET B SD  1 
ATOM   3361 C  CE  . MET B 1 148 ? -3.198  -12.103 -6.480  1.00 13.16 ? 148 MET B CE  1 
ATOM   3362 N  N   . GLY B 1 149 ? -8.016  -14.848 -3.749  1.00 8.55  ? 149 GLY B N   1 
ATOM   3363 C  CA  . GLY B 1 149 ? -8.723  -16.131 -3.641  1.00 9.38  ? 149 GLY B CA  1 
ATOM   3364 C  C   . GLY B 1 149 ? -9.822  -16.226 -4.690  1.00 7.98  ? 149 GLY B C   1 
ATOM   3365 O  O   . GLY B 1 149 ? -9.644  -15.895 -5.866  1.00 9.09  ? 149 GLY B O   1 
ATOM   3366 N  N   . SER B 1 150 ? -11.000 -16.646 -4.220  1.00 8.28  ? 150 SER B N   1 
ATOM   3367 C  CA  . SER B 1 150 ? -12.163 -16.729 -5.085  1.00 9.24  ? 150 SER B CA  1 
ATOM   3368 C  C   . SER B 1 150 ? -12.684 -15.348 -5.501  1.00 9.03  ? 150 SER B C   1 
ATOM   3369 O  O   . SER B 1 150 ? -12.634 -14.385 -4.714  1.00 9.38  ? 150 SER B O   1 
ATOM   3370 C  CB  . SER B 1 150 ? -13.301 -17.469 -4.404  1.00 8.06  ? 150 SER B CB  1 
ATOM   3371 O  OG  . SER B 1 150 ? -12.919 -18.846 -4.216  1.00 10.04 ? 150 SER B OG  1 
ATOM   3372 N  N   . PHE B 1 151 ? -13.315 -15.318 -6.690  1.00 8.65  ? 151 PHE B N   1 
ATOM   3373 C  CA  . PHE B 1 151 ? -14.112 -14.168 -7.124  1.00 8.70  ? 151 PHE B CA  1 
ATOM   3374 C  C   . PHE B 1 151 ? -15.146 -13.870 -6.065  1.00 8.89  ? 151 PHE B C   1 
ATOM   3375 O  O   . PHE B 1 151 ? -15.778 -14.764 -5.511  1.00 10.77 ? 151 PHE B O   1 
ATOM   3376 C  CB  . PHE B 1 151 ? -14.794 -14.512 -8.444  1.00 9.31  ? 151 PHE B CB  1 
ATOM   3377 C  CG  . PHE B 1 151 ? -15.621 -13.363 -8.976  1.00 9.47  ? 151 PHE B CG  1 
ATOM   3378 C  CD1 . PHE B 1 151 ? -15.012 -12.275 -9.622  1.00 10.46 ? 151 PHE B CD1 1 
ATOM   3379 C  CD2 . PHE B 1 151 ? -16.998 -13.387 -8.842  1.00 9.89  ? 151 PHE B CD2 1 
ATOM   3380 C  CE1 . PHE B 1 151 ? -15.796 -11.219 -10.089 1.00 10.54 ? 151 PHE B CE1 1 
ATOM   3381 C  CE2 . PHE B 1 151 ? -17.775 -12.316 -9.302  1.00 10.56 ? 151 PHE B CE2 1 
ATOM   3382 C  CZ  . PHE B 1 151 ? -17.161 -11.243 -9.917  1.00 10.74 ? 151 PHE B CZ  1 
ATOM   3383 N  N   . ASN B 1 152 ? -15.350 -12.568 -5.807  1.00 8.23  ? 152 ASN B N   1 
ATOM   3384 C  CA  . ASN B 1 152 ? -16.262 -12.118 -4.772  1.00 8.20  ? 152 ASN B CA  1 
ATOM   3385 C  C   . ASN B 1 152 ? -17.327 -11.222 -5.395  1.00 8.41  ? 152 ASN B C   1 
ATOM   3386 O  O   . ASN B 1 152 ? -17.055 -10.068 -5.742  1.00 8.40  ? 152 ASN B O   1 
ATOM   3387 C  CB  . ASN B 1 152 ? -15.451 -11.377 -3.686  1.00 7.96  ? 152 ASN B CB  1 
ATOM   3388 C  CG  . ASN B 1 152 ? -16.270 -11.101 -2.462  1.00 8.73  ? 152 ASN B CG  1 
ATOM   3389 O  OD1 . ASN B 1 152 ? -17.405 -10.599 -2.576  1.00 9.61  ? 152 ASN B OD1 1 
ATOM   3390 N  ND2 . ASN B 1 152 ? -15.695 -11.402 -1.293  1.00 8.94  ? 152 ASN B ND2 1 
ATOM   3391 N  N   A PRO B 1 153 ? -18.521 -11.749 -5.711  0.50 8.20  ? 153 PRO B N   1 
ATOM   3392 N  N   B PRO B 1 153 ? -18.582 -11.697 -5.533  0.50 8.89  ? 153 PRO B N   1 
ATOM   3393 C  CA  A PRO B 1 153 ? -19.624 -10.945 -6.279  0.50 8.54  ? 153 PRO B CA  1 
ATOM   3394 C  CA  B PRO B 1 153 ? -19.543 -10.917 -6.317  0.50 9.35  ? 153 PRO B CA  1 
ATOM   3395 C  C   A PRO B 1 153 ? -20.019 -9.689  -5.500  0.50 9.63  ? 153 PRO B C   1 
ATOM   3396 C  C   B PRO B 1 153 ? -19.877 -9.653  -5.529  0.50 9.97  ? 153 PRO B C   1 
ATOM   3397 O  O   A PRO B 1 153 ? -20.564 -8.726  -6.057  0.50 9.81  ? 153 PRO B O   1 
ATOM   3398 O  O   B PRO B 1 153 ? -20.087 -8.610  -6.148  0.50 9.88  ? 153 PRO B O   1 
ATOM   3399 C  CB  A PRO B 1 153 ? -20.793 -11.951 -6.172  0.50 8.54  ? 153 PRO B CB  1 
ATOM   3400 C  CB  B PRO B 1 153 ? -20.660 -11.934 -6.618  0.50 9.94  ? 153 PRO B CB  1 
ATOM   3401 C  CG  A PRO B 1 153 ? -20.135 -13.301 -6.417  0.50 7.80  ? 153 PRO B CG  1 
ATOM   3402 C  CG  B PRO B 1 153 ? -20.575 -12.914 -5.455  0.50 11.08 ? 153 PRO B CG  1 
ATOM   3403 C  CD  A PRO B 1 153 ? -18.836 -13.196 -5.634  0.50 7.53  ? 153 PRO B CD  1 
ATOM   3404 C  CD  B PRO B 1 153 ? -19.102 -13.012 -5.084  0.50 9.28  ? 153 PRO B CD  1 
ATOM   3405 N  N   . SER B 1 154 ? -19.829 -9.706  -4.187  1.00 9.25  ? 154 SER B N   1 
ATOM   3406 C  CA  . SER B 1 154 ? -20.182 -8.544  -3.373  1.00 9.29  ? 154 SER B CA  1 
ATOM   3407 C  C   . SER B 1 154 ? -19.190 -7.391  -3.599  1.00 9.68  ? 154 SER B C   1 
ATOM   3408 O  O   . SER B 1 154 ? -19.596 -6.245  -3.840  1.00 9.68  ? 154 SER B O   1 
ATOM   3409 C  CB  . SER B 1 154 ? -20.330 -8.862  -1.904  1.00 12.37 ? 154 SER B CB  1 
ATOM   3410 O  OG  . SER B 1 154 ? -21.279 -9.916  -1.761  1.00 16.02 ? 154 SER B OG  1 
ATOM   3411 N  N   . TYR B 1 155 ? -17.872 -7.693  -3.523  1.00 8.52  ? 155 TYR B N   1 
ATOM   3412 C  CA  . TYR B 1 155 ? -16.877 -6.682  -3.843  1.00 8.31  ? 155 TYR B CA  1 
ATOM   3413 C  C   . TYR B 1 155 ? -17.070 -6.181  -5.269  1.00 8.13  ? 155 TYR B C   1 
ATOM   3414 O  O   . TYR B 1 155 ? -16.716 -5.029  -5.592  1.00 7.89  ? 155 TYR B O   1 
ATOM   3415 C  CB  . TYR B 1 155 ? -15.445 -7.127  -3.536  1.00 7.62  ? 155 TYR B CB  1 
ATOM   3416 C  CG  . TYR B 1 155 ? -15.106 -7.009  -2.064  1.00 7.78  ? 155 TYR B CG  1 
ATOM   3417 C  CD1 . TYR B 1 155 ? -15.524 -7.937  -1.119  1.00 7.62  ? 155 TYR B CD1 1 
ATOM   3418 C  CD2 . TYR B 1 155 ? -14.331 -5.935  -1.604  1.00 8.01  ? 155 TYR B CD2 1 
ATOM   3419 C  CE1 . TYR B 1 155 ? -15.252 -7.793  0.222   1.00 8.53  ? 155 TYR B CE1 1 
ATOM   3420 C  CE2 . TYR B 1 155 ? -14.029 -5.800  -0.253  1.00 8.38  ? 155 TYR B CE2 1 
ATOM   3421 C  CZ  . TYR B 1 155 ? -14.524 -6.708  0.658   1.00 8.51  ? 155 TYR B CZ  1 
ATOM   3422 O  OH  . TYR B 1 155 ? -14.214 -6.592  1.986   1.00 8.58  ? 155 TYR B OH  1 
ATOM   3423 N  N   . ASP B 1 156 ? -17.454 -7.067  -6.173  1.00 8.39  ? 156 ASP B N   1 
ATOM   3424 C  CA  . ASP B 1 156 ? -17.605 -6.656  -7.555  1.00 8.79  ? 156 ASP B CA  1 
ATOM   3425 C  C   . ASP B 1 156 ? -18.723 -5.627  -7.717  1.00 8.85  ? 156 ASP B C   1 
ATOM   3426 O  O   . ASP B 1 156 ? -18.701 -4.917  -8.748  1.00 9.71  ? 156 ASP B O   1 
ATOM   3427 C  CB  . ASP B 1 156 ? -17.777 -7.848  -8.549  1.00 9.73  ? 156 ASP B CB  1 
ATOM   3428 C  CG  . ASP B 1 156 ? -16.778 -7.646  -9.710  1.00 10.55 ? 156 ASP B CG  1 
ATOM   3429 O  OD1 . ASP B 1 156 ? -15.582 -7.405  -9.524  1.00 10.88 ? 156 ASP B OD1 1 
ATOM   3430 O  OD2 . ASP B 1 156 ? -17.289 -7.748  -10.884 1.00 16.36 ? 156 ASP B OD2 1 
ATOM   3431 N  N   . LYS B 1 157 ? -19.636 -5.482  -6.765  1.00 9.16  ? 157 LYS B N   1 
ATOM   3432 C  CA  . LYS B 1 157 ? -20.645 -4.421  -6.864  1.00 11.10 ? 157 LYS B CA  1 
ATOM   3433 C  C   . LYS B 1 157 ? -19.939 -3.066  -6.826  1.00 11.50 ? 157 LYS B C   1 
ATOM   3434 O  O   . LYS B 1 157 ? -20.485 -2.116  -7.430  1.00 12.08 ? 157 LYS B O   1 
ATOM   3435 C  CB  . LYS B 1 157 ? -21.720 -4.574  -5.799  1.00 11.87 ? 157 LYS B CB  1 
ATOM   3436 C  CG  . LYS B 1 157 ? -22.522 -5.855  -5.967  1.00 15.32 ? 157 LYS B CG  1 
ATOM   3437 C  CD  . LYS B 1 157 ? -23.513 -6.224  -4.871  1.00 19.84 ? 157 LYS B CD  1 
ATOM   3438 C  CE  . LYS B 1 157 ? -24.256 -7.499  -5.245  1.00 25.01 ? 157 LYS B CE  1 
ATOM   3439 N  NZ  . LYS B 1 157 ? -24.927 -8.090  -4.055  1.00 27.06 ? 157 LYS B NZ  1 
ATOM   3440 N  N   . ILE B 1 158 ? -18.723 -2.976  -6.242  1.00 9.86  ? 158 ILE B N   1 
ATOM   3441 C  CA  . ILE B 1 158 ? -17.935 -1.753  -6.277  1.00 9.94  ? 158 ILE B CA  1 
ATOM   3442 C  C   . ILE B 1 158 ? -17.019 -1.809  -7.474  1.00 10.95 ? 158 ILE B C   1 
ATOM   3443 O  O   . ILE B 1 158 ? -16.974 -0.866  -8.278  1.00 10.65 ? 158 ILE B O   1 
ATOM   3444 C  CB  . ILE B 1 158 ? -17.122 -1.598  -4.985  1.00 10.79 ? 158 ILE B CB  1 
ATOM   3445 C  CG1 . ILE B 1 158 ? -18.099 -1.452  -3.820  1.00 12.79 ? 158 ILE B CG1 1 
ATOM   3446 C  CG2 . ILE B 1 158 ? -16.117 -0.431  -5.074  1.00 11.35 ? 158 ILE B CG2 1 
ATOM   3447 C  CD1 . ILE B 1 158 ? -17.452 -1.612  -2.465  1.00 15.68 ? 158 ILE B CD1 1 
ATOM   3448 N  N   . PHE B 1 159 ? -16.288 -2.912  -7.665  1.00 9.15  ? 159 PHE B N   1 
ATOM   3449 C  CA  . PHE B 1 159 ? -15.225 -2.917  -8.656  1.00 10.18 ? 159 PHE B CA  1 
ATOM   3450 C  C   . PHE B 1 159 ? -15.723 -2.776  -10.093 1.00 10.92 ? 159 PHE B C   1 
ATOM   3451 O  O   . PHE B 1 159 ? -14.963 -2.361  -10.973 1.00 12.98 ? 159 PHE B O   1 
ATOM   3452 C  CB  . PHE B 1 159 ? -14.364 -4.168  -8.555  1.00 10.18 ? 159 PHE B CB  1 
ATOM   3453 C  CG  . PHE B 1 159 ? -13.665 -4.378  -7.244  1.00 10.24 ? 159 PHE B CG  1 
ATOM   3454 C  CD1 . PHE B 1 159 ? -13.295 -3.331  -6.399  1.00 11.78 ? 159 PHE B CD1 1 
ATOM   3455 C  CD2 . PHE B 1 159 ? -13.362 -5.669  -6.845  1.00 11.63 ? 159 PHE B CD2 1 
ATOM   3456 C  CE1 . PHE B 1 159 ? -12.662 -3.599  -5.186  1.00 11.61 ? 159 PHE B CE1 1 
ATOM   3457 C  CE2 . PHE B 1 159 ? -12.719 -5.917  -5.650  1.00 11.25 ? 159 PHE B CE2 1 
ATOM   3458 C  CZ  . PHE B 1 159 ? -12.322 -4.897  -4.836  1.00 11.62 ? 159 PHE B CZ  1 
ATOM   3459 N  N   . SER B 1 160 ? -16.952 -3.211  -10.331 1.00 11.15 ? 160 SER B N   1 
ATOM   3460 C  CA  . SER B 1 160 ? -17.530 -3.130  -11.682 1.00 10.91 ? 160 SER B CA  1 
ATOM   3461 C  C   . SER B 1 160 ? -17.702 -1.690  -12.141 1.00 12.35 ? 160 SER B C   1 
ATOM   3462 O  O   . SER B 1 160 ? -17.884 -1.461  -13.329 1.00 15.21 ? 160 SER B O   1 
ATOM   3463 C  CB  . SER B 1 160 ? -18.817 -3.948  -11.777 1.00 13.72 ? 160 SER B CB  1 
ATOM   3464 O  OG  . SER B 1 160 ? -19.810 -3.398  -10.961 1.00 14.09 ? 160 SER B OG  1 
ATOM   3465 N  N   . HIS B 1 161 ? -17.570 -0.700  -11.240 1.00 11.94 ? 161 HIS B N   1 
ATOM   3466 C  CA  . HIS B 1 161 ? -17.662 0.716   -11.603 1.00 13.02 ? 161 HIS B CA  1 
ATOM   3467 C  C   . HIS B 1 161 ? -16.304 1.403   -11.746 1.00 15.02 ? 161 HIS B C   1 
ATOM   3468 O  O   . HIS B 1 161 ? -16.302 2.603   -12.059 1.00 15.48 ? 161 HIS B O   1 
ATOM   3469 C  CB  . HIS B 1 161 ? -18.535 1.456   -10.596 1.00 12.41 ? 161 HIS B CB  1 
ATOM   3470 C  CG  . HIS B 1 161 ? -19.923 0.929   -10.539 1.00 13.78 ? 161 HIS B CG  1 
ATOM   3471 N  ND1 . HIS B 1 161 ? -20.905 1.479   -11.347 1.00 15.30 ? 161 HIS B ND1 1 
ATOM   3472 C  CD2 . HIS B 1 161 ? -20.515 -0.066  -9.871  1.00 13.73 ? 161 HIS B CD2 1 
ATOM   3473 C  CE1 . HIS B 1 161 ? -22.052 0.840   -11.168 1.00 14.78 ? 161 HIS B CE1 1 
ATOM   3474 N  NE2 . HIS B 1 161 ? -21.839 -0.113  -10.238 1.00 15.48 ? 161 HIS B NE2 1 
ATOM   3475 N  N   . LEU B 1 162 ? -15.172 0.677   -11.629 1.00 15.02 ? 162 LEU B N   1 
ATOM   3476 C  CA  . LEU B 1 162 ? -13.889 1.372   -11.510 1.00 15.67 ? 162 LEU B CA  1 
ATOM   3477 C  C   . LEU B 1 162 ? -13.510 2.126   -12.776 1.00 15.53 ? 162 LEU B C   1 
ATOM   3478 O  O   . LEU B 1 162 ? -12.918 3.220   -12.676 1.00 16.52 ? 162 LEU B O   1 
ATOM   3479 C  CB  . LEU B 1 162 ? -12.764 0.406   -11.169 1.00 18.15 ? 162 LEU B CB  1 
ATOM   3480 C  CG  . LEU B 1 162 ? -12.857 -0.257  -9.790  1.00 18.58 ? 162 LEU B CG  1 
ATOM   3481 C  CD1 . LEU B 1 162 ? -11.870 -1.399  -9.755  1.00 17.98 ? 162 LEU B CD1 1 
ATOM   3482 C  CD2 . LEU B 1 162 ? -12.655 0.733   -8.655  1.00 22.69 ? 162 LEU B CD2 1 
ATOM   3483 N  N   . GLN B 1 163 ? -13.932 1.655   -13.944 1.00 16.11 ? 163 GLN B N   1 
ATOM   3484 C  CA  . GLN B 1 163 ? -13.571 2.321   -15.176 1.00 16.00 ? 163 GLN B CA  1 
ATOM   3485 C  C   . GLN B 1 163 ? -14.327 3.619   -15.362 1.00 16.11 ? 163 GLN B C   1 
ATOM   3486 O  O   . GLN B 1 163 ? -14.095 4.340   -16.353 1.00 18.43 ? 163 GLN B O   1 
ATOM   3487 C  CB  . GLN B 1 163 ? -13.814 1.436   -16.408 1.00 19.69 ? 163 GLN B CB  1 
ATOM   3488 C  CG  . GLN B 1 163 ? -12.865 0.230   -16.505 1.00 22.81 ? 163 GLN B CG  1 
ATOM   3489 C  CD  . GLN B 1 163 ? -11.365 0.472   -16.411 1.00 26.78 ? 163 GLN B CD  1 
ATOM   3490 O  OE1 . GLN B 1 163 ? -10.833 1.472   -16.862 1.00 27.48 ? 163 GLN B OE1 1 
ATOM   3491 N  NE2 . GLN B 1 163 ? -10.653 -0.467  -15.803 1.00 29.21 ? 163 GLN B NE2 1 
ATOM   3492 N  N   . HIS B 1 164 ? -15.178 3.957   -14.412 1.00 14.73 ? 164 HIS B N   1 
ATOM   3493 C  CA  . HIS B 1 164 ? -15.982 5.162   -14.460 1.00 13.01 ? 164 HIS B CA  1 
ATOM   3494 C  C   . HIS B 1 164 ? -15.548 6.242   -13.460 1.00 13.36 ? 164 HIS B C   1 
ATOM   3495 O  O   . HIS B 1 164 ? -16.136 7.320   -13.351 1.00 14.22 ? 164 HIS B O   1 
ATOM   3496 C  CB  . HIS B 1 164 ? -17.470 4.817   -14.446 1.00 16.43 ? 164 HIS B CB  1 
ATOM   3497 C  CG  . HIS B 1 164 ? -17.739 3.717   -15.408 1.00 17.81 ? 164 HIS B CG  1 
ATOM   3498 N  ND1 . HIS B 1 164 ? -17.367 3.833   -16.748 1.00 20.80 ? 164 HIS B ND1 1 
ATOM   3499 C  CD2 . HIS B 1 164 ? -18.244 2.477   -15.238 1.00 20.93 ? 164 HIS B CD2 1 
ATOM   3500 C  CE1 . HIS B 1 164 ? -17.612 2.689   -17.353 1.00 19.92 ? 164 HIS B CE1 1 
ATOM   3501 N  NE2 . HIS B 1 164 ? -18.203 1.870   -16.472 1.00 20.87 ? 164 HIS B NE2 1 
ATOM   3502 N  N   . VAL B 1 165 ? -14.557 5.911   -12.637 1.00 12.15 ? 165 VAL B N   1 
ATOM   3503 C  CA  . VAL B 1 165 ? -13.996 6.858   -11.676 1.00 11.48 ? 165 VAL B CA  1 
ATOM   3504 C  C   . VAL B 1 165 ? -12.477 6.801   -11.804 1.00 10.04 ? 165 VAL B C   1 
ATOM   3505 O  O   . VAL B 1 165 ? -11.706 6.843   -10.843 1.00 10.96 ? 165 VAL B O   1 
ATOM   3506 C  CB  . VAL B 1 165 ? -14.446 6.584   -10.222 1.00 12.84 ? 165 VAL B CB  1 
ATOM   3507 C  CG1 . VAL B 1 165 ? -15.912 6.943   -10.013 1.00 14.31 ? 165 VAL B CG1 1 
ATOM   3508 C  CG2 . VAL B 1 165 ? -14.217 5.153   -9.789  1.00 12.99 ? 165 VAL B CG2 1 
ATOM   3509 N  N   . LYS B 1 166 ? -12.020 6.676   -13.057 1.00 10.32 ? 166 LYS B N   1 
ATOM   3510 C  CA  . LYS B 1 166 ? -10.614 6.423   -13.289 1.00 11.02 ? 166 LYS B CA  1 
ATOM   3511 C  C   . LYS B 1 166 ? -9.745  7.588   -12.809 1.00 9.87  ? 166 LYS B C   1 
ATOM   3512 O  O   . LYS B 1 166 ? -8.619  7.379   -12.361 1.00 10.60 ? 166 LYS B O   1 
ATOM   3513 C  CB  . LYS B 1 166 ? -10.304 6.254   -14.783 1.00 13.19 ? 166 LYS B CB  1 
ATOM   3514 C  CG  . LYS B 1 166 ? -10.885 4.970   -15.337 1.00 14.72 ? 166 LYS B CG  1 
ATOM   3515 C  CD  . LYS B 1 166 ? -10.444 4.746   -16.790 1.00 17.14 ? 166 LYS B CD  1 
ATOM   3516 C  CE  . LYS B 1 166 ? -8.958  4.531   -16.940 1.00 18.46 ? 166 LYS B CE  1 
ATOM   3517 N  NZ  . LYS B 1 166 ? -8.617  3.210   -16.364 1.00 17.98 ? 166 LYS B NZ  1 
ATOM   3518 N  N   . TYR B 1 167 ? -10.280 8.843   -12.833 1.00 9.94  ? 167 TYR B N   1 
ATOM   3519 C  CA  . TYR B 1 167 ? -9.452  10.011  -12.570 1.00 10.10 ? 167 TYR B CA  1 
ATOM   3520 C  C   . TYR B 1 167 ? -9.928  10.783  -11.331 1.00 9.46  ? 167 TYR B C   1 
ATOM   3521 O  O   . TYR B 1 167 ? -11.119 10.720  -10.967 1.00 9.71  ? 167 TYR B O   1 
ATOM   3522 C  CB  . TYR B 1 167 ? -9.442  10.946  -13.812 1.00 11.70 ? 167 TYR B CB  1 
ATOM   3523 C  CG  . TYR B 1 167 ? -9.073  10.229  -15.104 1.00 12.20 ? 167 TYR B CG  1 
ATOM   3524 C  CD1 . TYR B 1 167 ? -7.790  9.796   -15.291 1.00 13.93 ? 167 TYR B CD1 1 
ATOM   3525 C  CD2 . TYR B 1 167 ? -10.034 9.905   -16.060 1.00 13.50 ? 167 TYR B CD2 1 
ATOM   3526 C  CE1 . TYR B 1 167 ? -7.431  9.104   -16.442 1.00 14.30 ? 167 TYR B CE1 1 
ATOM   3527 C  CE2 . TYR B 1 167 ? -9.735  9.170   -17.203 1.00 15.99 ? 167 TYR B CE2 1 
ATOM   3528 C  CZ  . TYR B 1 167 ? -8.412  8.792   -17.359 1.00 15.24 ? 167 TYR B CZ  1 
ATOM   3529 O  OH  . TYR B 1 167 ? -8.124  8.077   -18.502 1.00 19.64 ? 167 TYR B OH  1 
ATOM   3530 N  N   . LYS B 1 168 ? -8.996  11.516  -10.709 1.00 9.86  ? 168 LYS B N   1 
ATOM   3531 C  CA  . LYS B 1 168 ? -9.279  12.305  -9.523  1.00 11.52 ? 168 LYS B CA  1 
ATOM   3532 C  C   . LYS B 1 168 ? -10.474 13.205  -9.770  1.00 12.12 ? 168 LYS B C   1 
ATOM   3533 O  O   . LYS B 1 168 ? -10.571 13.888  -10.809 1.00 12.34 ? 168 LYS B O   1 
ATOM   3534 C  CB  . LYS B 1 168 ? -8.089  13.213  -9.200  1.00 13.28 ? 168 LYS B CB  1 
ATOM   3535 C  CG  . LYS B 1 168 ? -8.299  13.905  -7.861  1.00 14.66 ? 168 LYS B CG  1 
ATOM   3536 C  CD  . LYS B 1 168 ? -7.010  14.537  -7.377  1.00 17.25 ? 168 LYS B CD  1 
ATOM   3537 C  CE  . LYS B 1 168 ? -7.171  15.304  -6.073  1.00 20.57 ? 168 LYS B CE  1 
ATOM   3538 N  NZ  . LYS B 1 168 ? -5.863  15.643  -5.417  1.00 25.61 ? 168 LYS B NZ  1 
ATOM   3539 N  N   . GLY B 1 169 ? -11.413 13.180  -8.816  1.00 11.44 ? 169 GLY B N   1 
ATOM   3540 C  CA  . GLY B 1 169 ? -12.560 14.056  -8.847  1.00 13.29 ? 169 GLY B CA  1 
ATOM   3541 C  C   . GLY B 1 169 ? -13.765 13.434  -9.549  1.00 13.90 ? 169 GLY B C   1 
ATOM   3542 O  O   . GLY B 1 169 ? -14.887 13.933  -9.456  1.00 16.94 ? 169 GLY B O   1 
ATOM   3543 N  N   . GLN B 1 170 ? -13.572 12.339  -10.271 1.00 12.09 ? 170 GLN B N   1 
ATOM   3544 C  CA  . GLN B 1 170 ? -14.679 11.695  -10.972 1.00 12.39 ? 170 GLN B CA  1 
ATOM   3545 C  C   . GLN B 1 170 ? -15.591 10.963  -9.978  1.00 12.46 ? 170 GLN B C   1 
ATOM   3546 O  O   . GLN B 1 170 ? -15.130 10.406  -8.977  1.00 12.27 ? 170 GLN B O   1 
ATOM   3547 C  CB  . GLN B 1 170 ? -14.179 10.767  -12.066 1.00 11.61 ? 170 GLN B CB  1 
ATOM   3548 C  CG  . GLN B 1 170 ? -13.511 11.604  -13.182 1.00 13.55 ? 170 GLN B CG  1 
ATOM   3549 C  CD  . GLN B 1 170 ? -13.148 10.756  -14.372 1.00 16.26 ? 170 GLN B CD  1 
ATOM   3550 O  OE1 . GLN B 1 170 ? -12.774 9.579   -14.291 1.00 15.13 ? 170 GLN B OE1 1 
ATOM   3551 N  NE2 . GLN B 1 170 ? -13.225 11.407  -15.533 1.00 21.60 ? 170 GLN B NE2 1 
ATOM   3552 N  N   . GLU B 1 171 ? -16.881 10.930  -10.299 1.00 13.13 ? 171 GLU B N   1 
ATOM   3553 C  CA  . GLU B 1 171 ? -17.947 10.361  -9.460  1.00 13.21 ? 171 GLU B CA  1 
ATOM   3554 C  C   . GLU B 1 171 ? -18.833 9.449   -10.304 1.00 15.24 ? 171 GLU B C   1 
ATOM   3555 O  O   . GLU B 1 171 ? -19.035 9.665   -11.508 1.00 16.46 ? 171 GLU B O   1 
ATOM   3556 C  CB  . GLU B 1 171 ? -18.829 11.486  -8.915  1.00 16.95 ? 171 GLU B CB  1 
ATOM   3557 C  CG  . GLU B 1 171 ? -18.071 12.440  -8.008  1.00 21.78 ? 171 GLU B CG  1 
ATOM   3558 C  CD  . GLU B 1 171 ? -18.898 13.584  -7.439  1.00 26.42 ? 171 GLU B CD  1 
ATOM   3559 O  OE1 . GLU B 1 171 ? -19.966 13.889  -8.013  1.00 31.92 ? 171 GLU B OE1 1 
ATOM   3560 O  OE2 . GLU B 1 171 ? -18.462 14.134  -6.403  1.00 32.86 ? 171 GLU B OE2 1 
ATOM   3561 N  N   . ALA B 1 172 ? -19.361 8.390   -9.686  1.00 12.69 ? 172 ALA B N   1 
ATOM   3562 C  CA  . ALA B 1 172 ? -20.287 7.480   -10.332 1.00 12.93 ? 172 ALA B CA  1 
ATOM   3563 C  C   . ALA B 1 172 ? -21.279 7.048   -9.266  1.00 13.08 ? 172 ALA B C   1 
ATOM   3564 O  O   . ALA B 1 172 ? -21.000 7.207   -8.068  1.00 15.21 ? 172 ALA B O   1 
ATOM   3565 C  CB  . ALA B 1 172 ? -19.573 6.271   -10.893 1.00 13.30 ? 172 ALA B CB  1 
ATOM   3566 N  N   . PHE B 1 173 ? -22.397 6.489   -9.666  1.00 12.66 ? 173 PHE B N   1 
ATOM   3567 C  CA  . PHE B 1 173 ? -23.379 5.974   -8.728  1.00 11.78 ? 173 PHE B CA  1 
ATOM   3568 C  C   . PHE B 1 173 ? -23.363 4.462   -8.749  1.00 12.52 ? 173 PHE B C   1 
ATOM   3569 O  O   . PHE B 1 173 ? -23.239 3.810   -9.784  1.00 16.13 ? 173 PHE B O   1 
ATOM   3570 C  CB  . PHE B 1 173 ? -24.778 6.472   -9.095  1.00 13.80 ? 173 PHE B CB  1 
ATOM   3571 C  CG  . PHE B 1 173 ? -25.069 7.840   -8.538  1.00 15.99 ? 173 PHE B CG  1 
ATOM   3572 C  CD1 . PHE B 1 173 ? -25.131 8.015   -7.166  1.00 18.33 ? 173 PHE B CD1 1 
ATOM   3573 C  CD2 . PHE B 1 173 ? -25.376 8.925   -9.358  1.00 20.50 ? 173 PHE B CD2 1 
ATOM   3574 C  CE1 . PHE B 1 173 ? -25.427 9.238   -6.584  1.00 19.91 ? 173 PHE B CE1 1 
ATOM   3575 C  CE2 . PHE B 1 173 ? -25.651 10.167  -8.791  1.00 21.41 ? 173 PHE B CE2 1 
ATOM   3576 C  CZ  . PHE B 1 173 ? -25.688 10.325  -7.410  1.00 23.29 ? 173 PHE B CZ  1 
ATOM   3577 N  N   . VAL B 1 174 ? -23.463 3.907   -7.547  1.00 11.63 ? 174 VAL B N   1 
ATOM   3578 C  CA  . VAL B 1 174 ? -23.456 2.462   -7.334  1.00 11.55 ? 174 VAL B CA  1 
ATOM   3579 C  C   . VAL B 1 174 ? -24.783 2.100   -6.697  1.00 10.46 ? 174 VAL B C   1 
ATOM   3580 O  O   . VAL B 1 174 ? -25.125 2.643   -5.650  1.00 11.34 ? 174 VAL B O   1 
ATOM   3581 C  CB  . VAL B 1 174 ? -22.317 2.041   -6.370  1.00 9.94  ? 174 VAL B CB  1 
ATOM   3582 C  CG1 . VAL B 1 174 ? -22.345 0.555   -6.006  1.00 13.32 ? 174 VAL B CG1 1 
ATOM   3583 C  CG2 . VAL B 1 174 ? -20.936 2.362   -6.959  1.00 13.10 ? 174 VAL B CG2 1 
ATOM   3584 N  N   . PRO B 1 175 ? -25.572 1.171   -7.284  1.00 9.94  ? 175 PRO B N   1 
ATOM   3585 C  CA  . PRO B 1 175 ? -26.803 0.776   -6.617  1.00 10.08 ? 175 PRO B CA  1 
ATOM   3586 C  C   . PRO B 1 175 ? -26.498 0.219   -5.226  1.00 10.35 ? 175 PRO B C   1 
ATOM   3587 O  O   . PRO B 1 175 ? -25.507 -0.485  -5.008  1.00 10.59 ? 175 PRO B O   1 
ATOM   3588 C  CB  . PRO B 1 175 ? -27.384 -0.293  -7.534  1.00 11.28 ? 175 PRO B CB  1 
ATOM   3589 C  CG  . PRO B 1 175 ? -26.793 0.053   -8.902  1.00 11.84 ? 175 PRO B CG  1 
ATOM   3590 C  CD  . PRO B 1 175 ? -25.373 0.552   -8.603  1.00 10.36 ? 175 PRO B CD  1 
ATOM   3591 N  N   . GLY B 1 176 ? -27.436 0.398   -4.310  1.00 10.54 ? 176 GLY B N   1 
ATOM   3592 C  CA  . GLY B 1 176 ? -27.241 -0.142  -2.977  1.00 10.35 ? 176 GLY B CA  1 
ATOM   3593 C  C   . GLY B 1 176 ? -27.165 -1.665  -2.976  1.00 11.19 ? 176 GLY B C   1 
ATOM   3594 O  O   . GLY B 1 176 ? -27.708 -2.359  -3.826  1.00 11.35 ? 176 GLY B O   1 
ATOM   3595 N  N   . PHE B 1 177 ? -26.360 -2.151  -2.038  1.00 10.02 ? 177 PHE B N   1 
ATOM   3596 C  CA  . PHE B 1 177 ? -26.275 -3.579  -1.788  1.00 10.25 ? 177 PHE B CA  1 
ATOM   3597 C  C   . PHE B 1 177 ? -25.989 -3.719  -0.294  1.00 10.03 ? 177 PHE B C   1 
ATOM   3598 O  O   . PHE B 1 177 ? -25.827 -2.758  0.449   1.00 10.03 ? 177 PHE B O   1 
ATOM   3599 C  CB  . PHE B 1 177 ? -25.205 -4.267  -2.649  1.00 11.74 ? 177 PHE B CB  1 
ATOM   3600 C  CG  . PHE B 1 177 ? -23.801 -3.801  -2.380  1.00 11.55 ? 177 PHE B CG  1 
ATOM   3601 C  CD1 . PHE B 1 177 ? -23.316 -2.623  -2.915  1.00 11.86 ? 177 PHE B CD1 1 
ATOM   3602 C  CD2 . PHE B 1 177 ? -22.956 -4.592  -1.595  1.00 13.53 ? 177 PHE B CD2 1 
ATOM   3603 C  CE1 . PHE B 1 177 ? -22.000 -2.212  -2.703  1.00 12.37 ? 177 PHE B CE1 1 
ATOM   3604 C  CE2 . PHE B 1 177 ? -21.663 -4.163  -1.373  1.00 12.73 ? 177 PHE B CE2 1 
ATOM   3605 C  CZ  . PHE B 1 177 ? -21.185 -3.011  -1.932  1.00 12.97 ? 177 PHE B CZ  1 
ATOM   3606 N  N   . ASN B 1 178 ? -25.981 -4.980  0.135   1.00 10.61 ? 178 ASN B N   1 
ATOM   3607 C  CA  . ASN B 1 178 ? -25.779 -5.259  1.535   1.00 10.28 ? 178 ASN B CA  1 
ATOM   3608 C  C   . ASN B 1 178 ? -24.278 -5.193  1.860   1.00 9.73  ? 178 ASN B C   1 
ATOM   3609 O  O   . ASN B 1 178 ? -23.514 -6.085  1.534   1.00 10.96 ? 178 ASN B O   1 
ATOM   3610 C  CB  . ASN B 1 178 ? -26.383 -6.618  1.908   1.00 12.41 ? 178 ASN B CB  1 
ATOM   3611 C  CG  . ASN B 1 178 ? -26.265 -6.893  3.370   1.00 11.64 ? 178 ASN B CG  1 
ATOM   3612 O  OD1 . ASN B 1 178 ? -25.853 -6.072  4.191   1.00 11.68 ? 178 ASN B OD1 1 
ATOM   3613 N  ND2 . ASN B 1 178 ? -26.609 -8.147  3.703   1.00 15.47 ? 178 ASN B ND2 1 
ATOM   3614 N  N   . ILE B 1 179 ? -23.925 -4.104  2.521   1.00 9.50  ? 179 ILE B N   1 
ATOM   3615 C  CA  . ILE B 1 179 ? -22.520 -3.870  2.882   1.00 9.43  ? 179 ILE B CA  1 
ATOM   3616 C  C   . ILE B 1 179 ? -21.989 -4.947  3.821   1.00 9.40  ? 179 ILE B C   1 
ATOM   3617 O  O   . ILE B 1 179 ? -20.768 -5.155  3.892   1.00 9.77  ? 179 ILE B O   1 
ATOM   3618 C  CB  . ILE B 1 179 ? -22.371 -2.477  3.471   1.00 8.94  ? 179 ILE B CB  1 
ATOM   3619 C  CG1 . ILE B 1 179 ? -22.890 -1.392  2.510   1.00 10.63 ? 179 ILE B CG1 1 
ATOM   3620 C  CG2 . ILE B 1 179 ? -20.926 -2.191  3.875   1.00 10.03 ? 179 ILE B CG2 1 
ATOM   3621 C  CD1 . ILE B 1 179 ? -22.232 -1.373  1.114   1.00 10.78 ? 179 ILE B CD1 1 
ATOM   3622 N  N   . GLU B 1 180 ? -22.873 -5.615  4.595   1.00 9.96  ? 180 GLU B N   1 
ATOM   3623 C  CA  . GLU B 1 180 ? -22.394 -6.687  5.442   1.00 11.59 ? 180 GLU B CA  1 
ATOM   3624 C  C   . GLU B 1 180 ? -21.794 -7.812  4.615   1.00 11.38 ? 180 GLU B C   1 
ATOM   3625 O  O   . GLU B 1 180 ? -20.965 -8.587  5.172   1.00 11.71 ? 180 GLU B O   1 
ATOM   3626 C  CB  . GLU B 1 180 ? -23.530 -7.206  6.299   1.00 14.34 ? 180 GLU B CB  1 
ATOM   3627 C  CG  . GLU B 1 180 ? -23.046 -7.972  7.522   1.00 20.42 ? 180 GLU B CG  1 
ATOM   3628 C  CD  . GLU B 1 180 ? -24.072 -8.162  8.632   1.00 22.83 ? 180 GLU B CD  1 
ATOM   3629 O  OE1 . GLU B 1 180 ? -25.227 -7.686  8.476   1.00 23.83 ? 180 GLU B OE1 1 
ATOM   3630 O  OE2 . GLU B 1 180 ? -23.706 -8.785  9.656   1.00 27.64 ? 180 GLU B OE2 1 
ATOM   3631 N  N   . GLU B 1 181 ? -22.147 -7.910  3.321   1.00 10.45 ? 181 GLU B N   1 
ATOM   3632 C  CA  . GLU B 1 181 ? -21.544 -8.943  2.487   1.00 10.98 ? 181 GLU B CA  1 
ATOM   3633 C  C   . GLU B 1 181 ? -20.054 -8.680  2.242   1.00 11.49 ? 181 GLU B C   1 
ATOM   3634 O  O   . GLU B 1 181 ? -19.352 -9.600  1.783   1.00 12.89 ? 181 GLU B O   1 
ATOM   3635 C  CB  . GLU B 1 181 ? -22.221 -9.011  1.117   1.00 12.95 ? 181 GLU B CB  1 
ATOM   3636 C  CG  . GLU B 1 181 ? -23.666 -9.436  1.121   1.00 17.27 ? 181 GLU B CG  1 
ATOM   3637 C  CD  . GLU B 1 181 ? -24.357 -9.194  -0.216  1.00 21.73 ? 181 GLU B CD  1 
ATOM   3638 O  OE1 . GLU B 1 181 ? -23.684 -8.847  -1.243  1.00 21.88 ? 181 GLU B OE1 1 
ATOM   3639 O  OE2 . GLU B 1 181 ? -25.620 -9.327  -0.270  1.00 21.25 ? 181 GLU B OE2 1 
ATOM   3640 N  N   . LEU B 1 182 ? -19.540 -7.477  2.591   1.00 9.13  ? 182 LEU B N   1 
ATOM   3641 C  CA  . LEU B 1 182 ? -18.096 -7.206  2.426   1.00 9.13  ? 182 LEU B CA  1 
ATOM   3642 C  C   . LEU B 1 182 ? -17.331 -7.717  3.634   1.00 9.34  ? 182 LEU B C   1 
ATOM   3643 O  O   . LEU B 1 182 ? -16.092 -7.692  3.624   1.00 8.79  ? 182 LEU B O   1 
ATOM   3644 C  CB  . LEU B 1 182 ? -17.897 -5.689  2.239   1.00 8.95  ? 182 LEU B CB  1 
ATOM   3645 C  CG  . LEU B 1 182 ? -18.603 -5.071  1.028   1.00 7.52  ? 182 LEU B CG  1 
ATOM   3646 C  CD1 . LEU B 1 182 ? -18.307 -3.563  0.982   1.00 8.91  ? 182 LEU B CD1 1 
ATOM   3647 C  CD2 . LEU B 1 182 ? -18.193 -5.730  -0.278  1.00 9.21  ? 182 LEU B CD2 1 
ATOM   3648 N  N   . LEU B 1 183 ? -17.995 -7.993  4.758   1.00 9.42  ? 183 LEU B N   1 
ATOM   3649 C  CA  . LEU B 1 183 ? -17.345 -8.407  6.012   1.00 9.47  ? 183 LEU B CA  1 
ATOM   3650 C  C   . LEU B 1 183 ? -17.057 -9.904  5.974   1.00 9.57  ? 183 LEU B C   1 
ATOM   3651 O  O   . LEU B 1 183 ? -17.768 -10.674 5.315   1.00 11.29 ? 183 LEU B O   1 
ATOM   3652 C  CB  . LEU B 1 183 ? -18.257 -8.111  7.208   1.00 10.74 ? 183 LEU B CB  1 
ATOM   3653 C  CG  . LEU B 1 183 ? -18.700 -6.654  7.309   1.00 12.17 ? 183 LEU B CG  1 
ATOM   3654 C  CD1 . LEU B 1 183 ? -19.560 -6.394  8.553   1.00 14.87 ? 183 LEU B CD1 1 
ATOM   3655 C  CD2 . LEU B 1 183 ? -17.531 -5.712  7.253   1.00 13.03 ? 183 LEU B CD2 1 
ATOM   3656 N  N   . PRO B 1 184 ? -16.030 -10.370 6.712   1.00 9.98  ? 184 PRO B N   1 
ATOM   3657 C  CA  . PRO B 1 184 ? -15.674 -11.785 6.726   1.00 10.50 ? 184 PRO B CA  1 
ATOM   3658 C  C   . PRO B 1 184 ? -16.544 -12.573 7.676   1.00 12.94 ? 184 PRO B C   1 
ATOM   3659 O  O   . PRO B 1 184 ? -17.467 -12.062 8.302   1.00 14.51 ? 184 PRO B O   1 
ATOM   3660 C  CB  . PRO B 1 184 ? -14.247 -11.717 7.331   1.00 11.67 ? 184 PRO B CB  1 
ATOM   3661 C  CG  . PRO B 1 184 ? -14.297 -10.514 8.290   1.00 11.02 ? 184 PRO B CG  1 
ATOM   3662 C  CD  . PRO B 1 184 ? -15.168 -9.545  7.557   1.00 9.36  ? 184 PRO B CD  1 
ATOM   3663 N  N   . GLU B 1 185 ? -16.116 -13.843 7.756   1.00 14.04 ? 185 GLU B N   1 
ATOM   3664 C  CA  . GLU B 1 185 ? -16.776 -14.783 8.651   1.00 15.34 ? 185 GLU B CA  1 
ATOM   3665 C  C   . GLU B 1 185 ? -16.363 -14.444 10.076  1.00 15.45 ? 185 GLU B C   1 
ATOM   3666 O  O   . GLU B 1 185 ? -15.264 -13.927 10.346  1.00 14.85 ? 185 GLU B O   1 
ATOM   3667 C  CB  . GLU B 1 185 ? -16.301 -16.194 8.296   1.00 19.62 ? 185 GLU B CB  1 
ATOM   3668 C  CG  . GLU B 1 185 ? -16.866 -16.686 6.963   1.00 26.71 ? 185 GLU B CG  1 
ATOM   3669 C  CD  . GLU B 1 185 ? -18.368 -16.961 6.948   1.00 39.51 ? 185 GLU B CD  1 
ATOM   3670 O  OE1 . GLU B 1 185 ? -18.754 -18.163 6.874   1.00 49.71 ? 185 GLU B OE1 1 
ATOM   3671 O  OE2 . GLU B 1 185 ? -19.165 -15.980 7.016   1.00 46.82 ? 185 GLU B OE2 1 
ATOM   3672 N  N   . ARG B 1 186 ? -17.285 -14.686 11.006  1.00 14.27 ? 186 ARG B N   1 
ATOM   3673 C  CA  . ARG B 1 186 ? -17.013 -14.654 12.431  1.00 15.52 ? 186 ARG B CA  1 
ATOM   3674 C  C   . ARG B 1 186 ? -16.589 -13.236 12.815  1.00 12.99 ? 186 ARG B C   1 
ATOM   3675 O  O   . ARG B 1 186 ? -15.521 -12.981 13.388  1.00 13.18 ? 186 ARG B O   1 
ATOM   3676 C  CB  . ARG B 1 186 ? -16.011 -15.735 12.837  1.00 18.30 ? 186 ARG B CB  1 
ATOM   3677 C  CG  . ARG B 1 186 ? -16.551 -17.158 12.678  1.00 21.74 ? 186 ARG B CG  1 
ATOM   3678 C  CD  . ARG B 1 186 ? -15.620 -18.217 13.265  1.00 26.25 ? 186 ARG B CD  1 
ATOM   3679 N  NE  . ARG B 1 186 ? -14.405 -18.375 12.486  1.00 28.64 ? 186 ARG B NE  1 
ATOM   3680 C  CZ  . ARG B 1 186 ? -14.346 -18.866 11.245  1.00 35.84 ? 186 ARG B CZ  1 
ATOM   3681 N  NH1 . ARG B 1 186 ? -15.447 -19.278 10.632  1.00 36.77 ? 186 ARG B NH1 1 
ATOM   3682 N  NH2 . ARG B 1 186 ? -13.180 -18.954 10.625  1.00 39.77 ? 186 ARG B NH2 1 
ATOM   3683 N  N   . THR B 1 187 ? -17.446 -12.287 12.460  1.00 11.29 ? 187 THR B N   1 
ATOM   3684 C  CA  . THR B 1 187 ? -17.124 -10.931 12.831  1.00 10.69 ? 187 THR B CA  1 
ATOM   3685 C  C   . THR B 1 187 ? -16.973 -10.723 14.326  1.00 11.38 ? 187 THR B C   1 
ATOM   3686 O  O   . THR B 1 187 ? -16.470 -9.701  14.742  1.00 11.29 ? 187 THR B O   1 
ATOM   3687 C  CB  . THR B 1 187 ? -18.095 -9.918  12.234  1.00 10.90 ? 187 THR B CB  1 
ATOM   3688 O  OG1 . THR B 1 187 ? -19.427 -10.332 12.579  1.00 14.08 ? 187 THR B OG1 1 
ATOM   3689 C  CG2 . THR B 1 187 ? -17.929 -9.848  10.729  1.00 12.75 ? 187 THR B CG2 1 
ATOM   3690 N  N   . ALA B 1 188 ? -17.451 -11.673 15.154  1.00 11.66 ? 188 ALA B N   1 
ATOM   3691 C  CA  . ALA B 1 188 ? -17.250 -11.538 16.587  1.00 10.89 ? 188 ALA B CA  1 
ATOM   3692 C  C   . ALA B 1 188 ? -15.770 -11.600 16.980  1.00 9.69  ? 188 ALA B C   1 
ATOM   3693 O  O   . ALA B 1 188 ? -15.440 -11.182 18.075  1.00 11.02 ? 188 ALA B O   1 
ATOM   3694 C  CB  . ALA B 1 188 ? -18.057 -12.598 17.335  1.00 13.78 ? 188 ALA B CB  1 
ATOM   3695 N  N   . GLU B 1 189 ? -14.918 -12.101 16.095  1.00 10.53 ? 189 GLU B N   1 
ATOM   3696 C  CA  . GLU B 1 189 ? -13.476 -12.239 16.326  1.00 9.78  ? 189 GLU B CA  1 
ATOM   3697 C  C   . GLU B 1 189 ? -12.739 -11.067 15.670  1.00 8.95  ? 189 GLU B C   1 
ATOM   3698 O  O   . GLU B 1 189 ? -12.728 -10.974 14.419  1.00 9.56  ? 189 GLU B O   1 
ATOM   3699 C  CB  . GLU B 1 189 ? -12.995 -13.565 15.773  1.00 11.96 ? 189 GLU B CB  1 
ATOM   3700 C  CG  . GLU B 1 189 ? -13.716 -14.740 16.432  1.00 14.42 ? 189 GLU B CG  1 
ATOM   3701 C  CD  . GLU B 1 189 ? -13.250 -16.128 16.069  1.00 21.91 ? 189 GLU B CD  1 
ATOM   3702 O  OE1 . GLU B 1 189 ? -12.045 -16.337 15.799  1.00 22.60 ? 189 GLU B OE1 1 
ATOM   3703 O  OE2 . GLU B 1 189 ? -14.123 -17.037 16.118  1.00 25.77 ? 189 GLU B OE2 1 
ATOM   3704 N  N   . TYR B 1 190 ? -12.180 -10.202 16.506  1.00 7.87  ? 190 TYR B N   1 
ATOM   3705 C  CA  . TYR B 1 190 ? -11.549 -8.983  15.982  1.00 7.38  ? 190 TYR B CA  1 
ATOM   3706 C  C   . TYR B 1 190 ? -10.431 -8.582  16.910  1.00 8.21  ? 190 TYR B C   1 
ATOM   3707 O  O   . TYR B 1 190 ? -10.378 -8.927  18.103  1.00 9.33  ? 190 TYR B O   1 
ATOM   3708 C  CB  . TYR B 1 190 ? -12.576 -7.852  15.756  1.00 7.61  ? 190 TYR B CB  1 
ATOM   3709 C  CG  . TYR B 1 190 ? -13.375 -7.473  16.992  1.00 7.32  ? 190 TYR B CG  1 
ATOM   3710 C  CD1 . TYR B 1 190 ? -12.907 -6.541  17.910  1.00 7.77  ? 190 TYR B CD1 1 
ATOM   3711 C  CD2 . TYR B 1 190 ? -14.649 -8.007  17.170  1.00 8.24  ? 190 TYR B CD2 1 
ATOM   3712 C  CE1 . TYR B 1 190 ? -13.677 -6.173  19.008  1.00 8.57  ? 190 TYR B CE1 1 
ATOM   3713 C  CE2 . TYR B 1 190 ? -15.416 -7.650  18.278  1.00 8.66  ? 190 TYR B CE2 1 
ATOM   3714 C  CZ  . TYR B 1 190 ? -14.934 -6.739  19.177  1.00 9.23  ? 190 TYR B CZ  1 
ATOM   3715 O  OH  . TYR B 1 190 ? -15.631 -6.292  20.295  1.00 10.38 ? 190 TYR B OH  1 
ATOM   3716 N  N   . TYR B 1 191 ? -9.586  -7.690  16.373  1.00 8.57  ? 191 TYR B N   1 
ATOM   3717 C  CA  . TYR B 1 191 ? -8.558  -6.960  17.071  1.00 7.97  ? 191 TYR B CA  1 
ATOM   3718 C  C   . TYR B 1 191 ? -9.075  -5.542  17.278  1.00 8.22  ? 191 TYR B C   1 
ATOM   3719 O  O   . TYR B 1 191 ? -9.718  -4.946  16.388  1.00 9.36  ? 191 TYR B O   1 
ATOM   3720 C  CB  . TYR B 1 191 ? -7.263  -6.848  16.233  1.00 8.09  ? 191 TYR B CB  1 
ATOM   3721 C  CG  . TYR B 1 191 ? -6.681  -8.127  15.688  1.00 8.20  ? 191 TYR B CG  1 
ATOM   3722 C  CD1 . TYR B 1 191 ? -7.026  -8.623  14.450  1.00 8.46  ? 191 TYR B CD1 1 
ATOM   3723 C  CD2 . TYR B 1 191 ? -5.685  -8.770  16.391  1.00 9.07  ? 191 TYR B CD2 1 
ATOM   3724 C  CE1 . TYR B 1 191 ? -6.439  -9.747  13.893  1.00 9.92  ? 191 TYR B CE1 1 
ATOM   3725 C  CE2 . TYR B 1 191 ? -5.117  -9.930  15.900  1.00 9.90  ? 191 TYR B CE2 1 
ATOM   3726 C  CZ  . TYR B 1 191 ? -5.474  -10.393 14.651  1.00 9.47  ? 191 TYR B CZ  1 
ATOM   3727 O  OH  . TYR B 1 191 ? -4.878  -11.510 14.101  1.00 13.46 ? 191 TYR B OH  1 
ATOM   3728 N  N   . ARG B 1 192 ? -8.784  -4.955  18.426  1.00 8.24  ? 192 ARG B N   1 
ATOM   3729 C  CA  . ARG B 1 192 ? -9.238  -3.622  18.772  1.00 8.32  ? 192 ARG B CA  1 
ATOM   3730 C  C   . ARG B 1 192 ? -8.087  -2.813  19.316  1.00 9.49  ? 192 ARG B C   1 
ATOM   3731 O  O   . ARG B 1 192 ? -7.392  -3.263  20.231  1.00 9.12  ? 192 ARG B O   1 
ATOM   3732 C  CB  . ARG B 1 192 ? -10.315 -3.714  19.875  1.00 8.84  ? 192 ARG B CB  1 
ATOM   3733 C  CG  . ARG B 1 192 ? -10.668 -2.408  20.577  1.00 11.32 ? 192 ARG B CG  1 
ATOM   3734 C  CD  . ARG B 1 192 ? -11.366 -1.379  19.686  1.00 11.47 ? 192 ARG B CD  1 
ATOM   3735 N  NE  . ARG B 1 192 ? -12.467 -1.920  18.908  1.00 12.35 ? 192 ARG B NE  1 
ATOM   3736 C  CZ  . ARG B 1 192 ? -13.664 -2.240  19.398  1.00 12.21 ? 192 ARG B CZ  1 
ATOM   3737 N  NH1 . ARG B 1 192 ? -13.918 -2.064  20.711  1.00 14.32 ? 192 ARG B NH1 1 
ATOM   3738 N  NH2 . ARG B 1 192 ? -14.597 -2.740  18.623  1.00 12.31 ? 192 ARG B NH2 1 
ATOM   3739 N  N   . TYR B 1 193 ? -7.881  -1.602  18.828  1.00 8.57  ? 193 TYR B N   1 
ATOM   3740 C  CA  . TYR B 1 193 ? -6.840  -0.725  19.351  1.00 9.67  ? 193 TYR B CA  1 
ATOM   3741 C  C   . TYR B 1 193 ? -7.122  0.724   19.051  1.00 9.46  ? 193 TYR B C   1 
ATOM   3742 O  O   . TYR B 1 193 ? -7.906  1.013   18.147  1.00 9.53  ? 193 TYR B O   1 
ATOM   3743 C  CB  . TYR B 1 193 ? -5.423  -1.153  18.928  1.00 8.78  ? 193 TYR B CB  1 
ATOM   3744 C  CG  . TYR B 1 193 ? -5.036  -0.769  17.507  1.00 8.18  ? 193 TYR B CG  1 
ATOM   3745 C  CD1 . TYR B 1 193 ? -5.459  -1.489  16.405  1.00 8.51  ? 193 TYR B CD1 1 
ATOM   3746 C  CD2 . TYR B 1 193 ? -4.289  0.381   17.267  1.00 8.99  ? 193 TYR B CD2 1 
ATOM   3747 C  CE1 . TYR B 1 193 ? -5.146  -1.112  15.092  1.00 7.64  ? 193 TYR B CE1 1 
ATOM   3748 C  CE2 . TYR B 1 193 ? -3.962  0.792   15.996  1.00 8.22  ? 193 TYR B CE2 1 
ATOM   3749 C  CZ  . TYR B 1 193 ? -4.409  0.060   14.918  1.00 7.70  ? 193 TYR B CZ  1 
ATOM   3750 O  OH  . TYR B 1 193 ? -4.060  0.454   13.643  1.00 8.41  ? 193 TYR B OH  1 
ATOM   3751 N  N   . ARG B 1 194 ? -6.424  1.582   19.784  1.00 10.95 ? 194 ARG B N   1 
ATOM   3752 C  CA  . ARG B 1 194 ? -6.547  3.008   19.591  1.00 11.56 ? 194 ARG B CA  1 
ATOM   3753 C  C   . ARG B 1 194 ? -5.445  3.441   18.656  1.00 9.77  ? 194 ARG B C   1 
ATOM   3754 O  O   . ARG B 1 194 ? -4.263  3.209   18.840  1.00 11.93 ? 194 ARG B O   1 
ATOM   3755 C  CB  . ARG B 1 194 ? -6.242  3.744   20.906  1.00 16.20 ? 194 ARG B CB  1 
ATOM   3756 C  CG  . ARG B 1 194 ? -7.196  3.348   22.021  1.00 23.84 ? 194 ARG B CG  1 
ATOM   3757 C  CD  . ARG B 1 194 ? -8.376  4.278   22.214  1.00 35.52 ? 194 ARG B CD  1 
ATOM   3758 N  NE  . ARG B 1 194 ? -9.192  3.869   23.360  1.00 46.01 ? 194 ARG B NE  1 
ATOM   3759 C  CZ  . ARG B 1 194 ? -10.373 4.398   23.660  1.00 51.15 ? 194 ARG B CZ  1 
ATOM   3760 N  NH1 . ARG B 1 194 ? -10.869 5.375   22.915  1.00 56.99 ? 194 ARG B NH1 1 
ATOM   3761 N  NH2 . ARG B 1 194 ? -11.054 3.952   24.701  1.00 54.56 ? 194 ARG B NH2 1 
ATOM   3762 N  N   . GLY B 1 195 ? -5.863  4.149   17.588  1.00 9.10  ? 195 GLY B N   1 
ATOM   3763 C  CA  . GLY B 1 195 ? -4.920  4.594   16.591  1.00 9.92  ? 195 GLY B CA  1 
ATOM   3764 C  C   . GLY B 1 195 ? -5.375  5.856   15.876  1.00 8.74  ? 195 GLY B C   1 
ATOM   3765 O  O   . GLY B 1 195 ? -6.024  6.736   16.451  1.00 9.83  ? 195 GLY B O   1 
ATOM   3766 N  N   . SER B 1 196 ? -4.991  5.912   14.609  1.00 8.43  ? 196 SER B N   1 
ATOM   3767 C  CA  . SER B 1 196 ? -5.094  7.162   13.873  1.00 8.36  ? 196 SER B CA  1 
ATOM   3768 C  C   . SER B 1 196 ? -5.666  6.910   12.485  1.00 8.36  ? 196 SER B C   1 
ATOM   3769 O  O   . SER B 1 196 ? -5.764  5.789   11.978  1.00 7.88  ? 196 SER B O   1 
ATOM   3770 C  CB  . SER B 1 196 ? -3.719  7.815   13.704  1.00 9.01  ? 196 SER B CB  1 
ATOM   3771 O  OG  . SER B 1 196 ? -2.906  7.126   12.732  1.00 8.21  ? 196 SER B OG  1 
ATOM   3772 N  N   . LEU B 1 197 ? -6.000  8.005   11.797  1.00 7.58  ? 197 LEU B N   1 
ATOM   3773 C  CA  . LEU B 1 197 ? -6.112  7.952   10.325  1.00 7.95  ? 197 LEU B CA  1 
ATOM   3774 C  C   . LEU B 1 197 ? -4.780  7.423   9.776   1.00 7.83  ? 197 LEU B C   1 
ATOM   3775 O  O   . LEU B 1 197 ? -3.687  7.818   10.228  1.00 8.03  ? 197 LEU B O   1 
ATOM   3776 C  CB  . LEU B 1 197 ? -6.336  9.352   9.699   1.00 9.00  ? 197 LEU B CB  1 
ATOM   3777 C  CG  . LEU B 1 197 ? -7.774  9.831   9.577   1.00 10.41 ? 197 LEU B CG  1 
ATOM   3778 C  CD1 . LEU B 1 197 ? -8.335  10.101  10.931  1.00 13.96 ? 197 LEU B CD1 1 
ATOM   3779 C  CD2 . LEU B 1 197 ? -7.772  11.169  8.800   1.00 11.77 ? 197 LEU B CD2 1 
ATOM   3780 N  N   . THR B 1 198 ? -4.846  6.583   8.729   1.00 7.17  ? 198 THR B N   1 
ATOM   3781 C  CA  . THR B 1 198 ? -3.617  6.131   8.093   1.00 7.38  ? 198 THR B CA  1 
ATOM   3782 C  C   . THR B 1 198 ? -3.163  7.013   6.947   1.00 7.68  ? 198 THR B C   1 
ATOM   3783 O  O   . THR B 1 198 ? -2.176  6.716   6.274   1.00 8.49  ? 198 THR B O   1 
ATOM   3784 C  CB  . THR B 1 198 ? -3.757  4.700   7.596   1.00 6.62  ? 198 THR B CB  1 
ATOM   3785 O  OG1 . THR B 1 198 ? -4.677  4.698   6.515   1.00 6.36  ? 198 THR B OG1 1 
ATOM   3786 C  CG2 . THR B 1 198 ? -4.143  3.691   8.652   1.00 7.75  ? 198 THR B CG2 1 
ATOM   3787 N  N   . THR B 1 199 ? -3.948  8.083   6.677   1.00 8.38  ? 199 THR B N   1 
ATOM   3788 C  CA  . THR B 1 199 ? -3.628  9.069   5.653   1.00 8.14  ? 199 THR B CA  1 
ATOM   3789 C  C   . THR B 1 199 ? -3.516  10.384  6.396   1.00 8.13  ? 199 THR B C   1 
ATOM   3790 O  O   . THR B 1 199 ? -4.160  10.587  7.410   1.00 9.07  ? 199 THR B O   1 
ATOM   3791 C  CB  . THR B 1 199 ? -4.752  9.181   4.613   1.00 8.53  ? 199 THR B CB  1 
ATOM   3792 O  OG1 . THR B 1 199 ? -5.949  9.597   5.239   1.00 10.20 ? 199 THR B OG1 1 
ATOM   3793 C  CG2 . THR B 1 199 ? -5.030  7.835   3.972   1.00 9.45  ? 199 THR B CG2 1 
ATOM   3794 N  N   . PRO B 1 200 ? -2.838  11.395  5.775   1.00 7.97  ? 200 PRO B N   1 
ATOM   3795 C  CA  . PRO B 1 200 ? -2.927  12.776  6.287   1.00 9.26  ? 200 PRO B CA  1 
ATOM   3796 C  C   . PRO B 1 200 ? -4.394  13.135  6.445   1.00 9.97  ? 200 PRO B C   1 
ATOM   3797 O  O   . PRO B 1 200 ? -5.220  12.756  5.596   1.00 11.09 ? 200 PRO B O   1 
ATOM   3798 C  CB  . PRO B 1 200 ? -2.204  13.526  5.177   1.00 9.38  ? 200 PRO B CB  1 
ATOM   3799 C  CG  . PRO B 1 200 ? -1.129  12.603  4.682   1.00 8.68  ? 200 PRO B CG  1 
ATOM   3800 C  CD  . PRO B 1 200 ? -1.922  11.288  4.645   1.00 8.17  ? 200 PRO B CD  1 
ATOM   3801 N  N   A PRO B 1 201 ? -4.772  13.857  7.512   0.50 9.60  ? 201 PRO B N   1 
ATOM   3802 N  N   B PRO B 1 201 ? -4.782  13.939  7.447   0.50 10.23 ? 201 PRO B N   1 
ATOM   3803 C  CA  A PRO B 1 201 ? -3.835  14.478  8.462   0.50 9.12  ? 201 PRO B CA  1 
ATOM   3804 C  CA  B PRO B 1 201 ? -3.891  14.513  8.468   0.50 9.70  ? 201 PRO B CA  1 
ATOM   3805 C  C   A PRO B 1 201 ? -3.411  13.622  9.663   0.50 9.48  ? 201 PRO B C   1 
ATOM   3806 C  C   B PRO B 1 201 ? -3.374  13.622  9.601   0.50 9.84  ? 201 PRO B C   1 
ATOM   3807 O  O   A PRO B 1 201 ? -2.874  14.101  10.668  0.50 8.75  ? 201 PRO B O   1 
ATOM   3808 O  O   B PRO B 1 201 ? -2.732  14.120  10.519  0.50 9.63  ? 201 PRO B O   1 
ATOM   3809 C  CB  A PRO B 1 201 ? -4.645  15.729  8.874   0.50 9.80  ? 201 PRO B CB  1 
ATOM   3810 C  CB  B PRO B 1 201 ? -4.735  15.671  9.083   0.50 10.58 ? 201 PRO B CB  1 
ATOM   3811 C  CG  A PRO B 1 201 ? -6.090  15.272  8.827   0.50 9.26  ? 201 PRO B CG  1 
ATOM   3812 C  CG  B PRO B 1 201 ? -5.818  15.918  8.050   0.50 10.92 ? 201 PRO B CG  1 
ATOM   3813 C  CD  A PRO B 1 201 ? -6.167  14.240  7.737   0.50 9.67  ? 201 PRO B CD  1 
ATOM   3814 C  CD  B PRO B 1 201 ? -6.111  14.553  7.444   0.50 10.17 ? 201 PRO B CD  1 
ATOM   3815 N  N   . CYS B 1 202 ? -3.722  12.320  9.593   1.00 8.84  ? 202 CYS B N   1 
ATOM   3816 C  CA  . CYS B 1 202 ? -3.205  11.314  10.549  1.00 9.54  ? 202 CYS B CA  1 
ATOM   3817 C  C   . CYS B 1 202 ? -3.692  11.552  11.980  1.00 10.08 ? 202 CYS B C   1 
ATOM   3818 O  O   . CYS B 1 202 ? -3.019  11.204  12.937  1.00 9.80  ? 202 CYS B O   1 
ATOM   3819 C  CB  . CYS B 1 202 ? -1.673  11.265  10.588  1.00 9.77  ? 202 CYS B CB  1 
ATOM   3820 S  SG  . CYS B 1 202 ? -0.885  10.917  9.002   1.00 9.08  ? 202 CYS B SG  1 
ATOM   3821 N  N   A ASN B 1 203 ? -4.903  12.096  12.116  0.50 11.06 ? 203 ASN B N   1 
ATOM   3822 N  N   B ASN B 1 203 ? -4.889  12.123  12.115  0.50 11.53 ? 203 ASN B N   1 
ATOM   3823 C  CA  A ASN B 1 203 ? -5.398  12.456  13.438  0.50 11.45 ? 203 ASN B CA  1 
ATOM   3824 C  CA  B ASN B 1 203 ? -5.382  12.464  13.441  0.50 12.16 ? 203 ASN B CA  1 
ATOM   3825 C  C   A ASN B 1 203 ? -5.507  11.215  14.309  0.50 11.05 ? 203 ASN B C   1 
ATOM   3826 C  C   B ASN B 1 203 ? -5.468  11.211  14.299  0.50 11.44 ? 203 ASN B C   1 
ATOM   3827 O  O   A ASN B 1 203 ? -6.042  10.194  13.872  0.50 9.53  ? 203 ASN B O   1 
ATOM   3828 O  O   B ASN B 1 203 ? -5.930  10.168  13.843  0.50 9.90  ? 203 ASN B O   1 
ATOM   3829 C  CB  A ASN B 1 203 ? -6.802  13.027  13.380  0.50 13.09 ? 203 ASN B CB  1 
ATOM   3830 C  CB  B ASN B 1 203 ? -6.786  13.038  13.389  0.50 14.64 ? 203 ASN B CB  1 
ATOM   3831 C  CG  A ASN B 1 203 ? -6.898  14.183  12.409  0.50 14.19 ? 203 ASN B CG  1 
ATOM   3832 C  CG  B ASN B 1 203 ? -6.855  14.323  12.591  0.50 17.53 ? 203 ASN B CG  1 
ATOM   3833 O  OD1 A ASN B 1 203 ? -6.918  13.962  11.218  0.50 14.41 ? 203 ASN B OD1 1 
ATOM   3834 O  OD1 B ASN B 1 203 ? -5.832  14.879  12.221  0.50 19.29 ? 203 ASN B OD1 1 
ATOM   3835 N  ND2 A ASN B 1 203 ? -6.936  15.410  12.925  0.50 16.73 ? 203 ASN B ND2 1 
ATOM   3836 N  ND2 B ASN B 1 203 ? -8.056  14.825  12.364  0.50 16.18 ? 203 ASN B ND2 1 
ATOM   3837 N  N   . PRO B 1 204 ? -5.014  11.252  15.575  1.00 10.93 ? 204 PRO B N   1 
ATOM   3838 C  CA  . PRO B 1 204 ? -5.025  10.073  16.448  1.00 12.43 ? 204 PRO B CA  1 
ATOM   3839 C  C   . PRO B 1 204 ? -6.373  9.841   17.129  1.00 12.09 ? 204 PRO B C   1 
ATOM   3840 O  O   . PRO B 1 204 ? -6.473  9.837   18.360  1.00 14.43 ? 204 PRO B O   1 
ATOM   3841 C  CB  . PRO B 1 204 ? -3.881  10.379  17.441  1.00 12.66 ? 204 PRO B CB  1 
ATOM   3842 C  CG  . PRO B 1 204 ? -3.912  11.903  17.579  1.00 14.04 ? 204 PRO B CG  1 
ATOM   3843 C  CD  . PRO B 1 204 ? -4.357  12.421  16.204  1.00 12.53 ? 204 PRO B CD  1 
ATOM   3844 N  N   . THR B 1 205 ? -7.423  9.703   16.332  1.00 10.72 ? 205 THR B N   1 
ATOM   3845 C  CA  . THR B 1 205 ? -8.787  9.803   16.828  1.00 11.45 ? 205 THR B CA  1 
ATOM   3846 C  C   . THR B 1 205 ? -9.649  8.619   16.420  1.00 10.87 ? 205 THR B C   1 
ATOM   3847 O  O   . THR B 1 205 ? -10.878 8.700   16.428  1.00 11.71 ? 205 THR B O   1 
ATOM   3848 C  CB  . THR B 1 205 ? -9.400  11.095  16.287  1.00 13.27 ? 205 THR B CB  1 
ATOM   3849 O  OG1 . THR B 1 205 ? -9.283  11.045  14.863  1.00 12.19 ? 205 THR B OG1 1 
ATOM   3850 C  CG2 . THR B 1 205 ? -8.739  12.341  16.857  1.00 14.33 ? 205 THR B CG2 1 
ATOM   3851 N  N   . VAL B 1 206 ? -8.964  7.524   16.062  1.00 9.40  ? 206 VAL B N   1 
ATOM   3852 C  CA  . VAL B 1 206 ? -9.671  6.341   15.548  1.00 9.48  ? 206 VAL B CA  1 
ATOM   3853 C  C   . VAL B 1 206 ? -9.662  5.157   16.519  1.00 9.01  ? 206 VAL B C   1 
ATOM   3854 O  O   . VAL B 1 206 ? -8.605  4.722   16.958  1.00 10.23 ? 206 VAL B O   1 
ATOM   3855 C  CB  . VAL B 1 206 ? -9.074  5.890   14.189  1.00 8.27  ? 206 VAL B CB  1 
ATOM   3856 C  CG1 . VAL B 1 206 ? -9.778  4.630   13.685  1.00 9.97  ? 206 VAL B CG1 1 
ATOM   3857 C  CG2 . VAL B 1 206 ? -9.123  6.999   13.163  1.00 9.59  ? 206 VAL B CG2 1 
ATOM   3858 N  N   . LEU B 1 207 ? -10.831 4.632   16.786  1.00 8.75  ? 207 LEU B N   1 
ATOM   3859 C  CA  . LEU B 1 207 ? -10.969 3.332   17.400  1.00 8.94  ? 207 LEU B CA  1 
ATOM   3860 C  C   . LEU B 1 207 ? -10.990 2.298   16.276  1.00 7.91  ? 207 LEU B C   1 
ATOM   3861 O  O   . LEU B 1 207 ? -11.921 2.207   15.472  1.00 8.43  ? 207 LEU B O   1 
ATOM   3862 C  CB  . LEU B 1 207 ? -12.290 3.249   18.182  1.00 12.28 ? 207 LEU B CB  1 
ATOM   3863 C  CG  . LEU B 1 207 ? -12.365 2.088   19.168  1.00 18.65 ? 207 LEU B CG  1 
ATOM   3864 C  CD1 . LEU B 1 207 ? -11.332 2.229   20.284  1.00 22.36 ? 207 LEU B CD1 1 
ATOM   3865 C  CD2 . LEU B 1 207 ? -13.754 2.026   19.765  1.00 23.29 ? 207 LEU B CD2 1 
ATOM   3866 N  N   . TRP B 1 208 ? -9.937  1.495   16.197  1.00 7.49  ? 208 TRP B N   1 
ATOM   3867 C  CA  . TRP B 1 208 ? -9.790  0.503   15.133  1.00 7.54  ? 208 TRP B CA  1 
ATOM   3868 C  C   . TRP B 1 208 ? -10.394 -0.843  15.526  1.00 7.85  ? 208 TRP B C   1 
ATOM   3869 O  O   . TRP B 1 208 ? -10.119 -1.317  16.675  1.00 8.81  ? 208 TRP B O   1 
ATOM   3870 C  CB  . TRP B 1 208 ? -8.308  0.278   14.791  1.00 8.22  ? 208 TRP B CB  1 
ATOM   3871 C  CG  . TRP B 1 208 ? -7.782  1.365   13.902  1.00 7.48  ? 208 TRP B CG  1 
ATOM   3872 C  CD1 . TRP B 1 208 ? -7.120  2.512   14.258  1.00 8.04  ? 208 TRP B CD1 1 
ATOM   3873 C  CD2 . TRP B 1 208 ? -7.915  1.420   12.462  1.00 7.61  ? 208 TRP B CD2 1 
ATOM   3874 N  NE1 . TRP B 1 208 ? -6.865  3.297   13.152  1.00 7.99  ? 208 TRP B NE1 1 
ATOM   3875 C  CE2 . TRP B 1 208 ? -7.362  2.664   12.031  1.00 7.00  ? 208 TRP B CE2 1 
ATOM   3876 C  CE3 . TRP B 1 208 ? -8.494  0.585   11.508  1.00 7.72  ? 208 TRP B CE3 1 
ATOM   3877 C  CZ2 . TRP B 1 208 ? -7.364  3.037   10.687  1.00 6.88  ? 208 TRP B CZ2 1 
ATOM   3878 C  CZ3 . TRP B 1 208 ? -8.485  0.944   10.184  1.00 7.43  ? 208 TRP B CZ3 1 
ATOM   3879 C  CH2 . TRP B 1 208 ? -7.889  2.144   9.779   1.00 7.49  ? 208 TRP B CH2 1 
ATOM   3880 N  N   . THR B 1 209 ? -11.102 -1.488  14.600  1.00 7.74  ? 209 THR B N   1 
ATOM   3881 C  CA  . THR B 1 209 ? -11.555 -2.858  14.732  1.00 7.21  ? 209 THR B CA  1 
ATOM   3882 C  C   . THR B 1 209 ? -11.044 -3.529  13.469  1.00 7.31  ? 209 THR B C   1 
ATOM   3883 O  O   . THR B 1 209 ? -11.522 -3.207  12.369  1.00 8.24  ? 209 THR B O   1 
ATOM   3884 C  CB  . THR B 1 209 ? -13.081 -2.937  14.860  1.00 7.34  ? 209 THR B CB  1 
ATOM   3885 O  OG1 . THR B 1 209 ? -13.490 -2.211  16.031  1.00 8.77  ? 209 THR B OG1 1 
ATOM   3886 C  CG2 . THR B 1 209 ? -13.573 -4.377  14.973  1.00 8.64  ? 209 THR B CG2 1 
ATOM   3887 N  N   . VAL B 1 210 ? -10.130 -4.495  13.603  1.00 7.70  ? 210 VAL B N   1 
ATOM   3888 C  CA  . VAL B 1 210 ? -9.661  -5.237  12.443  1.00 7.23  ? 210 VAL B CA  1 
ATOM   3889 C  C   . VAL B 1 210 ? -10.191 -6.651  12.581  1.00 7.21  ? 210 VAL B C   1 
ATOM   3890 O  O   . VAL B 1 210 ? -9.917  -7.321  13.609  1.00 7.91  ? 210 VAL B O   1 
ATOM   3891 C  CB  . VAL B 1 210 ? -8.118  -5.243  12.362  1.00 7.51  ? 210 VAL B CB  1 
ATOM   3892 C  CG1 . VAL B 1 210 ? -7.661  -6.022  11.157  1.00 8.29  ? 210 VAL B CG1 1 
ATOM   3893 C  CG2 . VAL B 1 210 ? -7.525  -3.847  12.392  1.00 8.87  ? 210 VAL B CG2 1 
ATOM   3894 N  N   . PHE B 1 211 ? -10.999 -7.102  11.660  1.00 6.96  ? 211 PHE B N   1 
ATOM   3895 C  CA  . PHE B 1 211 ? -11.524 -8.464  11.805  1.00 7.49  ? 211 PHE B CA  1 
ATOM   3896 C  C   . PHE B 1 211 ? -10.428 -9.510  11.695  1.00 7.82  ? 211 PHE B C   1 
ATOM   3897 O  O   . PHE B 1 211 ? -9.461  -9.358  10.934  1.00 8.40  ? 211 PHE B O   1 
ATOM   3898 C  CB  . PHE B 1 211 ? -12.636 -8.708  10.774  1.00 8.37  ? 211 PHE B CB  1 
ATOM   3899 C  CG  . PHE B 1 211 ? -13.838 -7.846  11.097  1.00 8.01  ? 211 PHE B CG  1 
ATOM   3900 C  CD1 . PHE B 1 211 ? -14.616 -8.060  12.241  1.00 8.98  ? 211 PHE B CD1 1 
ATOM   3901 C  CD2 . PHE B 1 211 ? -14.170 -6.791  10.239  1.00 9.02  ? 211 PHE B CD2 1 
ATOM   3902 C  CE1 . PHE B 1 211 ? -15.695 -7.236  12.531  1.00 9.29  ? 211 PHE B CE1 1 
ATOM   3903 C  CE2 . PHE B 1 211 ? -15.253 -5.964  10.513  1.00 10.26 ? 211 PHE B CE2 1 
ATOM   3904 C  CZ  . PHE B 1 211 ? -16.032 -6.188  11.655  1.00 10.93 ? 211 PHE B CZ  1 
ATOM   3905 N  N   . ARG B 1 212 ? -10.571 -10.588 12.488  1.00 8.13  ? 212 ARG B N   1 
ATOM   3906 C  CA  . ARG B 1 212 ? -9.539  -11.624 12.493  1.00 9.39  ? 212 ARG B CA  1 
ATOM   3907 C  C   . ARG B 1 212 ? -9.453  -12.317 11.147  1.00 9.74  ? 212 ARG B C   1 
ATOM   3908 O  O   . ARG B 1 212 ? -8.347  -12.624 10.728  1.00 10.51 ? 212 ARG B O   1 
ATOM   3909 C  CB  . ARG B 1 212 ? -9.853  -12.667 13.569  1.00 10.51 ? 212 ARG B CB  1 
ATOM   3910 C  CG  . ARG B 1 212 ? -8.742  -13.708 13.759  1.00 10.97 ? 212 ARG B CG  1 
ATOM   3911 C  CD  . ARG B 1 212 ? -9.326  -14.848 14.649  1.00 12.77 ? 212 ARG B CD  1 
ATOM   3912 N  NE  . ARG B 1 212 ? -8.179  -15.710 14.948  1.00 14.73 ? 212 ARG B NE  1 
ATOM   3913 C  CZ  . ARG B 1 212 ? -8.166  -16.619 15.916  1.00 17.68 ? 212 ARG B CZ  1 
ATOM   3914 N  NH1 . ARG B 1 212 ? -9.296  -16.911 16.529  1.00 16.23 ? 212 ARG B NH1 1 
ATOM   3915 N  NH2 . ARG B 1 212 ? -7.023  -17.256 16.188  1.00 18.23 ? 212 ARG B NH2 1 
ATOM   3916 N  N   . ASN B 1 213 ? -10.590 -12.585 10.523  1.00 8.80  ? 213 ASN B N   1 
ATOM   3917 C  CA  . ASN B 1 213 ? -10.598 -13.402 9.327   1.00 10.06 ? 213 ASN B CA  1 
ATOM   3918 C  C   . ASN B 1 213 ? -10.633 -12.526 8.078   1.00 10.19 ? 213 ASN B C   1 
ATOM   3919 O  O   . ASN B 1 213 ? -11.368 -11.536 8.029   1.00 9.96  ? 213 ASN B O   1 
ATOM   3920 C  CB  . ASN B 1 213 ? -11.818 -14.335 9.327   1.00 12.82 ? 213 ASN B CB  1 
ATOM   3921 C  CG  . ASN B 1 213 ? -11.748 -15.298 10.511  1.00 14.17 ? 213 ASN B CG  1 
ATOM   3922 O  OD1 . ASN B 1 213 ? -10.715 -15.913 10.710  1.00 20.77 ? 213 ASN B OD1 1 
ATOM   3923 N  ND2 . ASN B 1 213 ? -12.741 -15.283 11.347  1.00 17.62 ? 213 ASN B ND2 1 
ATOM   3924 N  N   . PRO B 1 214 ? -9.847  -12.870 7.053   1.00 9.50  ? 214 PRO B N   1 
ATOM   3925 C  CA  . PRO B 1 214 ? -9.892  -12.128 5.792   1.00 9.94  ? 214 PRO B CA  1 
ATOM   3926 C  C   . PRO B 1 214 ? -11.070 -12.563 4.923   1.00 9.19  ? 214 PRO B C   1 
ATOM   3927 O  O   . PRO B 1 214 ? -11.680 -13.636 5.131   1.00 10.76 ? 214 PRO B O   1 
ATOM   3928 C  CB  . PRO B 1 214 ? -8.542  -12.512 5.132   1.00 11.01 ? 214 PRO B CB  1 
ATOM   3929 C  CG  . PRO B 1 214 ? -8.399  -13.957 5.597   1.00 13.00 ? 214 PRO B CG  1 
ATOM   3930 C  CD  . PRO B 1 214 ? -8.811  -13.934 7.072   1.00 12.16 ? 214 PRO B CD  1 
ATOM   3931 N  N   . VAL B 1 215 ? -11.353 -11.751 3.913   1.00 8.74  ? 215 VAL B N   1 
ATOM   3932 C  CA  . VAL B 1 215 ? -12.200 -12.132 2.793   1.00 8.26  ? 215 VAL B CA  1 
ATOM   3933 C  C   . VAL B 1 215 ? -11.312 -12.424 1.606   1.00 7.77  ? 215 VAL B C   1 
ATOM   3934 O  O   . VAL B 1 215 ? -10.117 -12.089 1.616   1.00 8.91  ? 215 VAL B O   1 
ATOM   3935 C  CB  . VAL B 1 215 ? -13.234 -11.054 2.458   1.00 7.87  ? 215 VAL B CB  1 
ATOM   3936 C  CG1 . VAL B 1 215 ? -14.137 -10.811 3.657   1.00 9.57  ? 215 VAL B CG1 1 
ATOM   3937 C  CG2 . VAL B 1 215 ? -12.606 -9.747  1.940   1.00 9.18  ? 215 VAL B CG2 1 
ATOM   3938 N  N   . GLN B 1 216 ? -11.854 -13.028 0.564   1.00 7.84  ? 216 GLN B N   1 
ATOM   3939 C  CA  . GLN B 1 216 ? -11.144 -13.299 -0.679  1.00 8.06  ? 216 GLN B CA  1 
ATOM   3940 C  C   . GLN B 1 216 ? -11.757 -12.496 -1.817  1.00 7.10  ? 216 GLN B C   1 
ATOM   3941 O  O   . GLN B 1 216 ? -12.999 -12.363 -1.919  1.00 8.77  ? 216 GLN B O   1 
ATOM   3942 C  CB  . GLN B 1 216 ? -11.225 -14.758 -1.128  1.00 9.27  ? 216 GLN B CB  1 
ATOM   3943 C  CG  . GLN B 1 216 ? -10.530 -15.675 -0.131  1.00 11.47 ? 216 GLN B CG  1 
ATOM   3944 C  CD  . GLN B 1 216 ? -10.573 -17.136 -0.519  1.00 14.10 ? 216 GLN B CD  1 
ATOM   3945 O  OE1 . GLN B 1 216 ? -11.048 -17.595 -1.571  1.00 11.97 ? 216 GLN B OE1 1 
ATOM   3946 N  NE2 . GLN B 1 216 ? -10.053 -17.939 0.390   1.00 20.07 ? 216 GLN B NE2 1 
ATOM   3947 N  N   . ILE B 1 217 ? -10.908 -11.969 -2.698  1.00 6.67  ? 217 ILE B N   1 
ATOM   3948 C  CA  . ILE B 1 217 ? -11.302 -11.501 -4.025  1.00 6.71  ? 217 ILE B CA  1 
ATOM   3949 C  C   . ILE B 1 217 ? -10.335 -12.158 -5.022  1.00 6.60  ? 217 ILE B C   1 
ATOM   3950 O  O   . ILE B 1 217 ? -9.234  -12.551 -4.632  1.00 7.82  ? 217 ILE B O   1 
ATOM   3951 C  CB  . ILE B 1 217 ? -11.315 -9.947  -4.114  1.00 7.13  ? 217 ILE B CB  1 
ATOM   3952 C  CG1 . ILE B 1 217 ? -9.917  -9.356  -4.125  1.00 7.37  ? 217 ILE B CG1 1 
ATOM   3953 C  CG2 . ILE B 1 217 ? -12.252 -9.342  -3.068  1.00 7.68  ? 217 ILE B CG2 1 
ATOM   3954 C  CD1 . ILE B 1 217 ? -9.874  -7.834  -4.269  1.00 10.00 ? 217 ILE B CD1 1 
ATOM   3955 N  N   . SER B 1 218 ? -10.690 -12.192 -6.292  1.00 6.61  ? 218 SER B N   1 
ATOM   3956 C  CA  . SER B 1 218 ? -9.843  -12.930 -7.219  1.00 7.81  ? 218 SER B CA  1 
ATOM   3957 C  C   . SER B 1 218 ? -8.685  -12.122 -7.716  1.00 8.67  ? 218 SER B C   1 
ATOM   3958 O  O   . SER B 1 218 ? -8.644  -10.885 -7.630  1.00 8.61  ? 218 SER B O   1 
ATOM   3959 C  CB  . SER B 1 218 ? -10.646 -13.411 -8.420  1.00 8.30  ? 218 SER B CB  1 
ATOM   3960 O  OG  . SER B 1 218 ? -11.072 -12.280 -9.219  1.00 9.67  ? 218 SER B OG  1 
ATOM   3961 N  N   . GLN B 1 219 ? -7.734  -12.803 -8.350  1.00 9.24  ? 219 GLN B N   1 
ATOM   3962 C  CA  . GLN B 1 219 ? -6.621  -12.136 -9.032  1.00 10.47 ? 219 GLN B CA  1 
ATOM   3963 C  C   . GLN B 1 219 ? -7.138  -11.131 -10.059 1.00 10.24 ? 219 GLN B C   1 
ATOM   3964 O  O   . GLN B 1 219 ? -6.553  -10.027 -10.192 1.00 10.46 ? 219 GLN B O   1 
ATOM   3965 C  CB  . GLN B 1 219 ? -5.771  -13.175 -9.788  1.00 13.78 ? 219 GLN B CB  1 
ATOM   3966 C  CG  . GLN B 1 219 ? -4.436  -12.572 -10.252 1.00 19.46 ? 219 GLN B CG  1 
ATOM   3967 C  CD  . GLN B 1 219 ? -4.442  -11.916 -11.615 1.00 24.80 ? 219 GLN B CD  1 
ATOM   3968 O  OE1 . GLN B 1 219 ? -3.589  -11.080 -11.929 1.00 27.54 ? 219 GLN B OE1 1 
ATOM   3969 N  NE2 . GLN B 1 219 ? -5.383  -12.316 -12.456 1.00 25.32 ? 219 GLN B NE2 1 
ATOM   3970 N  N   . GLU B 1 220 ? -8.184  -11.476 -10.798 1.00 10.02 ? 220 GLU B N   1 
ATOM   3971 C  CA  . GLU B 1 220 ? -8.689  -10.561 -11.821 1.00 10.95 ? 220 GLU B CA  1 
ATOM   3972 C  C   . GLU B 1 220 ? -9.316  -9.319  -11.178 1.00 9.69  ? 220 GLU B C   1 
ATOM   3973 O  O   . GLU B 1 220 ? -9.178  -8.208  -11.699 1.00 10.73 ? 220 GLU B O   1 
ATOM   3974 C  CB  . GLU B 1 220 ? -9.689  -11.293 -12.711 1.00 11.68 ? 220 GLU B CB  1 
ATOM   3975 C  CG  . GLU B 1 220 ? -9.016  -12.431 -13.543 1.00 14.21 ? 220 GLU B CG  1 
ATOM   3976 C  CD  . GLU B 1 220 ? -8.781  -13.775 -12.854 1.00 16.92 ? 220 GLU B CD  1 
ATOM   3977 O  OE1 . GLU B 1 220 ? -9.201  -13.997 -11.692 1.00 15.27 ? 220 GLU B OE1 1 
ATOM   3978 O  OE2 . GLU B 1 220 ? -8.097  -14.609 -13.463 1.00 22.89 ? 220 GLU B OE2 1 
ATOM   3979 N  N   . GLN B 1 221 ? -9.977  -9.477  -10.024 1.00 8.59  ? 221 GLN B N   1 
ATOM   3980 C  CA  . GLN B 1 221 ? -10.535 -8.312  -9.343  1.00 8.30  ? 221 GLN B CA  1 
ATOM   3981 C  C   . GLN B 1 221 ? -9.426  -7.435  -8.787  1.00 8.61  ? 221 GLN B C   1 
ATOM   3982 O  O   . GLN B 1 221 ? -9.499  -6.211  -8.961  1.00 8.90  ? 221 GLN B O   1 
ATOM   3983 C  CB  . GLN B 1 221 ? -11.422 -8.763  -8.187  1.00 8.50  ? 221 GLN B CB  1 
ATOM   3984 C  CG  . GLN B 1 221 ? -12.718 -9.376  -8.677  1.00 8.46  ? 221 GLN B CG  1 
ATOM   3985 C  CD  . GLN B 1 221 ? -13.605 -9.850  -7.548  1.00 7.61  ? 221 GLN B CD  1 
ATOM   3986 O  OE1 . GLN B 1 221 ? -13.280 -10.807 -6.796  1.00 8.51  ? 221 GLN B OE1 1 
ATOM   3987 N  NE2 . GLN B 1 221 ? -14.768 -9.211  -7.386  1.00 8.37  ? 221 GLN B NE2 1 
ATOM   3988 N  N   . LEU B 1 222 ? -8.371  -8.023  -8.228  1.00 8.45  ? 222 LEU B N   1 
ATOM   3989 C  CA  . LEU B 1 222 ? -7.245  -7.245  -7.773  1.00 9.06  ? 222 LEU B CA  1 
ATOM   3990 C  C   . LEU B 1 222 ? -6.618  -6.519  -8.958  1.00 9.41  ? 222 LEU B C   1 
ATOM   3991 O  O   . LEU B 1 222 ? -6.244  -5.352  -8.818  1.00 9.46  ? 222 LEU B O   1 
ATOM   3992 C  CB  . LEU B 1 222 ? -6.236  -8.178  -7.093  1.00 9.82  ? 222 LEU B CB  1 
ATOM   3993 C  CG  . LEU B 1 222 ? -6.577  -8.541  -5.676  1.00 9.11  ? 222 LEU B CG  1 
ATOM   3994 C  CD1 . LEU B 1 222 ? -5.899  -9.839  -5.175  1.00 10.72 ? 222 LEU B CD1 1 
ATOM   3995 C  CD2 . LEU B 1 222 ? -6.200  -7.397  -4.722  1.00 10.96 ? 222 LEU B CD2 1 
ATOM   3996 N  N   . LEU B 1 223 ? -6.435  -7.199  -10.085 1.00 9.33  ? 223 LEU B N   1 
ATOM   3997 C  CA  . LEU B 1 223 ? -5.772  -6.561  -11.224 1.00 10.47 ? 223 LEU B CA  1 
ATOM   3998 C  C   . LEU B 1 223 ? -6.616  -5.392  -11.715 1.00 11.14 ? 223 LEU B C   1 
ATOM   3999 O  O   . LEU B 1 223 ? -6.026  -4.358  -12.035 1.00 10.84 ? 223 LEU B O   1 
ATOM   4000 C  CB  . LEU B 1 223 ? -5.621  -7.588  -12.359 1.00 12.70 ? 223 LEU B CB  1 
ATOM   4001 C  CG  . LEU B 1 223 ? -4.864  -7.046  -13.574 1.00 14.21 ? 223 LEU B CG  1 
ATOM   4002 C  CD1 . LEU B 1 223 ? -3.468  -6.644  -13.192 1.00 16.27 ? 223 LEU B CD1 1 
ATOM   4003 C  CD2 . LEU B 1 223 ? -4.862  -8.081  -14.696 1.00 16.19 ? 223 LEU B CD2 1 
ATOM   4004 N  N   . ALA B 1 224 ? -7.935  -5.524  -11.764 1.00 10.86 ? 224 ALA B N   1 
ATOM   4005 C  CA  . ALA B 1 224 ? -8.779  -4.384  -12.123 1.00 11.40 ? 224 ALA B CA  1 
ATOM   4006 C  C   . ALA B 1 224 ? -8.592  -3.240  -11.148 1.00 12.09 ? 224 ALA B C   1 
ATOM   4007 O  O   . ALA B 1 224 ? -8.365  -2.082  -11.570 1.00 12.87 ? 224 ALA B O   1 
ATOM   4008 C  CB  . ALA B 1 224 ? -10.209 -4.812  -12.163 1.00 12.84 ? 224 ALA B CB  1 
ATOM   4009 N  N   . LEU B 1 225 ? -8.649  -3.512  -9.838  1.00 10.62 ? 225 LEU B N   1 
ATOM   4010 C  CA  . LEU B 1 225 ? -8.442  -2.467  -8.842  1.00 10.01 ? 225 LEU B CA  1 
ATOM   4011 C  C   . LEU B 1 225 ? -7.093  -1.784  -8.999  1.00 10.40 ? 225 LEU B C   1 
ATOM   4012 O  O   . LEU B 1 225 ? -7.017  -0.546  -8.862  1.00 12.16 ? 225 LEU B O   1 
ATOM   4013 C  CB  . LEU B 1 225 ? -8.640  -3.102  -7.462  1.00 10.07 ? 225 LEU B CB  1 
ATOM   4014 C  CG  . LEU B 1 225 ? -8.425  -2.162  -6.272  1.00 10.49 ? 225 LEU B CG  1 
ATOM   4015 C  CD1 . LEU B 1 225 ? -9.481  -1.052  -6.293  1.00 10.73 ? 225 LEU B CD1 1 
ATOM   4016 C  CD2 . LEU B 1 225 ? -8.496  -2.966  -4.975  1.00 10.81 ? 225 LEU B CD2 1 
ATOM   4017 N  N   . GLU B 1 226 ? -6.034  -2.533  -9.331  1.00 10.58 ? 226 GLU B N   1 
ATOM   4018 C  CA  . GLU B 1 226 ? -4.669  -2.041  -9.391  1.00 10.94 ? 226 GLU B CA  1 
ATOM   4019 C  C   . GLU B 1 226 ? -4.379  -1.334  -10.728 1.00 10.82 ? 226 GLU B C   1 
ATOM   4020 O  O   . GLU B 1 226 ? -3.293  -0.764  -10.819 1.00 13.82 ? 226 GLU B O   1 
ATOM   4021 C  CB  . GLU B 1 226 ? -3.677  -3.215  -9.195  1.00 11.15 ? 226 GLU B CB  1 
ATOM   4022 C  CG  . GLU B 1 226 ? -3.750  -3.891  -7.812  1.00 10.63 ? 226 GLU B CG  1 
ATOM   4023 C  CD  . GLU B 1 226 ? -3.382  -5.351  -7.832  1.00 12.62 ? 226 GLU B CD  1 
ATOM   4024 O  OE1 . GLU B 1 226 ? -3.108  -5.884  -8.933  1.00 11.81 ? 226 GLU B OE1 1 
ATOM   4025 O  OE2 . GLU B 1 226 ? -3.435  -5.982  -6.781  1.00 12.81 ? 226 GLU B OE2 1 
ATOM   4026 N  N   . THR B 1 227 ? -5.236  -1.476  -11.726 1.00 10.98 ? 227 THR B N   1 
ATOM   4027 C  CA  . THR B 1 227 ? -4.915  -0.888  -13.030 1.00 12.05 ? 227 THR B CA  1 
ATOM   4028 C  C   . THR B 1 227 ? -5.927  0.163   -13.439 1.00 14.58 ? 227 THR B C   1 
ATOM   4029 O  O   . THR B 1 227 ? -5.648  0.844   -14.434 1.00 15.41 ? 227 THR B O   1 
ATOM   4030 C  CB  . THR B 1 227 ? -4.849  -1.948  -14.146 1.00 12.02 ? 227 THR B CB  1 
ATOM   4031 O  OG1 . THR B 1 227 ? -6.097  -2.640  -14.221 1.00 12.49 ? 227 THR B OG1 1 
ATOM   4032 C  CG2 . THR B 1 227 ? -3.714  -2.947  -13.944 1.00 12.17 ? 227 THR B CG2 1 
ATOM   4033 N  N   . ALA B 1 228 ? -7.045  0.286   -12.748 1.00 11.23 ? 228 ALA B N   1 
ATOM   4034 C  CA  . ALA B 1 228 ? -8.064  1.164   -13.293 1.00 12.16 ? 228 ALA B CA  1 
ATOM   4035 C  C   . ALA B 1 228 ? -7.822  2.632   -12.931 1.00 11.65 ? 228 ALA B C   1 
ATOM   4036 O  O   . ALA B 1 228 ? -8.333  3.487   -13.681 1.00 13.92 ? 228 ALA B O   1 
ATOM   4037 C  CB  . ALA B 1 228 ? -9.398  0.782   -12.763 1.00 14.56 ? 228 ALA B CB  1 
ATOM   4038 N  N   . LEU B 1 229 ? -7.161  2.961   -11.828 1.00 10.92 ? 229 LEU B N   1 
ATOM   4039 C  CA  . LEU B 1 229 ? -7.334  4.295   -11.256 1.00 10.15 ? 229 LEU B CA  1 
ATOM   4040 C  C   . LEU B 1 229 ? -6.033  5.063   -11.281 1.00 10.24 ? 229 LEU B C   1 
ATOM   4041 O  O   . LEU B 1 229 ? -4.947  4.512   -11.252 1.00 10.07 ? 229 LEU B O   1 
ATOM   4042 C  CB  . LEU B 1 229 ? -7.847  4.211   -9.805  1.00 11.62 ? 229 LEU B CB  1 
ATOM   4043 C  CG  . LEU B 1 229 ? -9.061  3.306   -9.620  1.00 12.75 ? 229 LEU B CG  1 
ATOM   4044 C  CD1 . LEU B 1 229 ? -9.350  3.188   -8.107  1.00 14.22 ? 229 LEU B CD1 1 
ATOM   4045 C  CD2 . LEU B 1 229 ? -10.257 3.810   -10.391 1.00 14.82 ? 229 LEU B CD2 1 
ATOM   4046 N  N   . TYR B 1 230 ? -6.202  6.387   -11.258 1.00 10.19 ? 230 TYR B N   1 
ATOM   4047 C  CA  . TYR B 1 230 ? -5.143  7.394   -11.306 1.00 11.10 ? 230 TYR B CA  1 
ATOM   4048 C  C   . TYR B 1 230 ? -5.321  8.357   -10.145 1.00 10.48 ? 230 TYR B C   1 
ATOM   4049 O  O   . TYR B 1 230 ? -6.456  8.743   -9.851  1.00 10.79 ? 230 TYR B O   1 
ATOM   4050 C  CB  . TYR B 1 230 ? -5.135  8.128   -12.667 1.00 11.48 ? 230 TYR B CB  1 
ATOM   4051 C  CG  . TYR B 1 230 ? -4.706  7.202   -13.774 1.00 10.56 ? 230 TYR B CG  1 
ATOM   4052 C  CD1 . TYR B 1 230 ? -5.638  6.343   -14.325 1.00 12.89 ? 230 TYR B CD1 1 
ATOM   4053 C  CD2 . TYR B 1 230 ? -3.370  7.076   -14.147 1.00 12.97 ? 230 TYR B CD2 1 
ATOM   4054 C  CE1 . TYR B 1 230 ? -5.241  5.359   -15.211 1.00 13.60 ? 230 TYR B CE1 1 
ATOM   4055 C  CE2 . TYR B 1 230 ? -2.967  6.103   -15.066 1.00 13.56 ? 230 TYR B CE2 1 
ATOM   4056 C  CZ  . TYR B 1 230 ? -3.925  5.266   -15.600 1.00 13.63 ? 230 TYR B CZ  1 
ATOM   4057 O  OH  . TYR B 1 230 ? -3.552  4.254   -16.458 1.00 19.15 ? 230 TYR B OH  1 
ATOM   4058 N  N   . CYS B 1 231 ? -4.226  8.809   -9.559  1.00 11.47 ? 231 CYS B N   1 
ATOM   4059 C  CA  . CYS B 1 231 ? -4.313  9.842   -8.534  1.00 12.50 ? 231 CYS B CA  1 
ATOM   4060 C  C   . CYS B 1 231 ? -4.577  11.224  -9.114  1.00 12.35 ? 231 CYS B C   1 
ATOM   4061 O  O   . CYS B 1 231 ? -4.891  12.170  -8.409  1.00 13.85 ? 231 CYS B O   1 
ATOM   4062 C  CB  . CYS B 1 231 ? -3.015  10.016  -7.743  1.00 15.15 ? 231 CYS B CB  1 
ATOM   4063 S  SG  . CYS B 1 231 ? -2.326  8.486   -7.039  1.00 21.92 ? 231 CYS B SG  1 
ATOM   4064 N  N   . THR B 1 232 ? -4.408  11.341  -10.439 1.00 11.24 ? 232 THR B N   1 
ATOM   4065 C  CA  . THR B 1 232 ? -4.391  12.626  -11.141 1.00 10.66 ? 232 THR B CA  1 
ATOM   4066 C  C   . THR B 1 232 ? -5.704  12.849  -11.874 1.00 11.27 ? 232 THR B C   1 
ATOM   4067 O  O   . THR B 1 232 ? -6.445  11.928  -12.191 1.00 11.47 ? 232 THR B O   1 
ATOM   4068 C  CB  . THR B 1 232 ? -3.182  12.626  -12.095 1.00 10.00 ? 232 THR B CB  1 
ATOM   4069 O  OG1 . THR B 1 232 ? -3.021  11.331  -12.722 1.00 10.94 ? 232 THR B OG1 1 
ATOM   4070 C  CG2 . THR B 1 232 ? -1.898  12.915  -11.350 1.00 12.42 ? 232 THR B CG2 1 
ATOM   4071 N  N   . HIS B 1 233 ? -5.956  14.117  -12.204 1.00 11.19 ? 233 HIS B N   1 
ATOM   4072 C  CA  . HIS B 1 233 ? -7.095  14.460  -13.019 1.00 12.01 ? 233 HIS B CA  1 
ATOM   4073 C  C   . HIS B 1 233 ? -6.970  13.970  -14.456 1.00 12.00 ? 233 HIS B C   1 
ATOM   4074 O  O   . HIS B 1 233 ? -5.867  13.726  -14.942 1.00 12.66 ? 233 HIS B O   1 
ATOM   4075 C  CB  . HIS B 1 233 ? -7.243  15.997  -13.046 1.00 15.18 ? 233 HIS B CB  1 
ATOM   4076 C  CG  . HIS B 1 233 ? -7.683  16.517  -11.728 1.00 17.97 ? 233 HIS B CG  1 
ATOM   4077 N  ND1 . HIS B 1 233 ? -6.820  16.990  -10.751 1.00 24.51 ? 233 HIS B ND1 1 
ATOM   4078 C  CD2 . HIS B 1 233 ? -8.901  16.528  -11.165 1.00 21.56 ? 233 HIS B CD2 1 
ATOM   4079 C  CE1 . HIS B 1 233 ? -7.502  17.354  -9.672  1.00 24.58 ? 233 HIS B CE1 1 
ATOM   4080 N  NE2 . HIS B 1 233 ? -8.783  17.120  -9.927  1.00 22.60 ? 233 HIS B NE2 1 
ATOM   4081 N  N   A MET B 1 234 ? -8.116  13.873  -15.134 0.50 12.83 ? 234 MET B N   1 
ATOM   4082 N  N   B MET B 1 234 ? -8.117  13.845  -15.130 0.50 13.27 ? 234 MET B N   1 
ATOM   4083 C  CA  A MET B 1 234 ? -8.224  13.341  -16.490 0.50 13.09 ? 234 MET B CA  1 
ATOM   4084 C  CA  B MET B 1 234 ? -8.194  13.324  -16.492 0.50 13.82 ? 234 MET B CA  1 
ATOM   4085 C  C   A MET B 1 234 ? -7.379  14.141  -17.485 0.50 13.19 ? 234 MET B C   1 
ATOM   4086 C  C   B MET B 1 234 ? -7.248  14.103  -17.413 0.50 13.88 ? 234 MET B C   1 
ATOM   4087 O  O   A MET B 1 234 ? -6.939  13.593  -18.502 0.50 13.19 ? 234 MET B O   1 
ATOM   4088 O  O   B MET B 1 234 ? -6.584  13.507  -18.273 0.50 13.24 ? 234 MET B O   1 
ATOM   4089 C  CB  A MET B 1 234 ? -9.678  13.396  -16.959 0.50 13.02 ? 234 MET B CB  1 
ATOM   4090 C  CB  B MET B 1 234 ? -9.632  13.417  -17.018 0.50 14.56 ? 234 MET B CB  1 
ATOM   4091 C  CG  A MET B 1 234 ? -9.869  12.828  -18.362 0.50 14.84 ? 234 MET B CG  1 
ATOM   4092 C  CG  B MET B 1 234 ? -9.903  12.559  -18.272 0.50 17.19 ? 234 MET B CG  1 
ATOM   4093 S  SD  A MET B 1 234 ? -11.598 12.832  -18.797 0.50 17.23 ? 234 MET B SD  1 
ATOM   4094 S  SD  B MET B 1 234 ? -11.673 12.216  -18.510 0.50 20.53 ? 234 MET B SD  1 
ATOM   4095 C  CE  A MET B 1 234 ? -11.565 11.809  -20.273 0.50 14.46 ? 234 MET B CE  1 
ATOM   4096 C  CE  B MET B 1 234 ? -12.288 13.901  -18.410 0.50 20.56 ? 234 MET B CE  1 
ATOM   4097 N  N   . ASP B 1 235 ? -7.129  15.414  -17.168 1.00 13.50 ? 235 ASP B N   1 
ATOM   4098 C  CA  . ASP B 1 235 ? -6.354  16.242  -18.105 1.00 15.26 ? 235 ASP B CA  1 
ATOM   4099 C  C   . ASP B 1 235 ? -4.915  16.473  -17.659 1.00 15.82 ? 235 ASP B C   1 
ATOM   4100 O  O   . ASP B 1 235 ? -4.180  17.256  -18.268 1.00 16.71 ? 235 ASP B O   1 
ATOM   4101 C  CB  . ASP B 1 235 ? -7.040  17.592  -18.338 1.00 19.74 ? 235 ASP B CB  1 
ATOM   4102 C  CG  . ASP B 1 235 ? -7.027  18.475  -17.101 1.00 24.37 ? 235 ASP B CG  1 
ATOM   4103 O  OD1 . ASP B 1 235 ? -6.595  18.015  -16.010 1.00 24.78 ? 235 ASP B OD1 1 
ATOM   4104 O  OD2 . ASP B 1 235 ? -7.437  19.652  -17.222 1.00 29.55 ? 235 ASP B OD2 1 
ATOM   4105 N  N   . ASP B 1 236 ? -4.385  15.746  -16.673 1.00 13.09 ? 236 ASP B N   1 
ATOM   4106 C  CA  . ASP B 1 236 ? -3.087  16.055  -16.132 1.00 12.68 ? 236 ASP B CA  1 
ATOM   4107 C  C   . ASP B 1 236 ? -2.041  15.569  -17.113 1.00 13.90 ? 236 ASP B C   1 
ATOM   4108 O  O   . ASP B 1 236 ? -2.059  14.409  -17.513 1.00 14.40 ? 236 ASP B O   1 
ATOM   4109 C  CB  . ASP B 1 236 ? -2.908  15.315  -14.785 1.00 14.34 ? 236 ASP B CB  1 
ATOM   4110 C  CG  . ASP B 1 236 ? -1.741  15.878  -13.987 1.00 15.58 ? 236 ASP B CG  1 
ATOM   4111 O  OD1 . ASP B 1 236 ? -0.673  16.087  -14.574 1.00 15.47 ? 236 ASP B OD1 1 
ATOM   4112 O  OD2 . ASP B 1 236 ? -1.900  16.104  -12.770 1.00 17.34 ? 236 ASP B OD2 1 
ATOM   4113 N  N   . PRO B 1 237 ? -1.087  16.409  -17.580 1.00 13.67 ? 237 PRO B N   1 
ATOM   4114 C  CA  . PRO B 1 237 ? -0.010  15.919  -18.455 1.00 14.62 ? 237 PRO B CA  1 
ATOM   4115 C  C   . PRO B 1 237 ? 1.066   15.040  -17.795 1.00 14.32 ? 237 PRO B C   1 
ATOM   4116 O  O   . PRO B 1 237 ? 1.932   14.509  -18.487 1.00 15.79 ? 237 PRO B O   1 
ATOM   4117 C  CB  . PRO B 1 237 ? 0.570   17.254  -18.975 1.00 14.47 ? 237 PRO B CB  1 
ATOM   4118 C  CG  . PRO B 1 237 ? 0.373   18.183  -17.778 1.00 15.58 ? 237 PRO B CG  1 
ATOM   4119 C  CD  . PRO B 1 237 ? -1.033  17.866  -17.314 1.00 13.85 ? 237 PRO B CD  1 
ATOM   4120 N  N   A SER B 1 238 ? 0.961   14.788  -16.475 0.50 13.70 ? 238 SER B N   1 
ATOM   4121 N  N   B SER B 1 238 ? 1.011   14.863  -16.457 0.50 13.33 ? 238 SER B N   1 
ATOM   4122 C  CA  A SER B 1 238 ? 1.909   13.946  -15.752 0.50 14.93 ? 238 SER B CA  1 
ATOM   4123 C  CA  B SER B 1 238 ? 1.878   13.937  -15.737 0.50 14.07 ? 238 SER B CA  1 
ATOM   4124 C  C   A SER B 1 238 ? 1.147   12.898  -14.949 0.50 13.56 ? 238 SER B C   1 
ATOM   4125 C  C   B SER B 1 238 ? 0.984   13.002  -14.930 0.50 12.77 ? 238 SER B C   1 
ATOM   4126 O  O   A SER B 1 238 ? 1.250   12.874  -13.729 0.50 14.76 ? 238 SER B O   1 
ATOM   4127 O  O   B SER B 1 238 ? 0.764   13.180  -13.717 0.50 12.43 ? 238 SER B O   1 
ATOM   4128 C  CB  A SER B 1 238 ? 2.725   14.770  -14.787 0.50 16.85 ? 238 SER B CB  1 
ATOM   4129 C  CB  B SER B 1 238 ? 2.856   14.647  -14.826 0.50 15.27 ? 238 SER B CB  1 
ATOM   4130 O  OG  A SER B 1 238 ? 3.801   14.008  -14.272 0.50 20.62 ? 238 SER B OG  1 
ATOM   4131 O  OG  B SER B 1 238 ? 3.529   15.697  -15.522 0.50 17.90 ? 238 SER B OG  1 
ATOM   4132 N  N   . PRO B 1 239 ? 0.392   11.995  -15.598 1.00 12.35 ? 239 PRO B N   1 
ATOM   4133 C  CA  . PRO B 1 239 ? -0.496  11.068  -14.873 1.00 12.53 ? 239 PRO B CA  1 
ATOM   4134 C  C   . PRO B 1 239 ? 0.286   10.181  -13.923 1.00 13.91 ? 239 PRO B C   1 
ATOM   4135 O  O   . PRO B 1 239 ? 1.458   9.842   -14.136 1.00 14.99 ? 239 PRO B O   1 
ATOM   4136 C  CB  . PRO B 1 239 ? -1.117  10.215  -15.960 1.00 15.02 ? 239 PRO B CB  1 
ATOM   4137 C  CG  . PRO B 1 239 ? -0.380  10.505  -17.231 1.00 16.89 ? 239 PRO B CG  1 
ATOM   4138 C  CD  . PRO B 1 239 ? 0.451   11.742  -17.043 1.00 13.38 ? 239 PRO B CD  1 
ATOM   4139 N  N   . ARG B 1 240 ? -0.405  9.839   -12.827 1.00 12.58 ? 240 ARG B N   1 
ATOM   4140 C  CA  . ARG B 1 240 ? 0.190   8.935   -11.838 1.00 13.49 ? 240 ARG B CA  1 
ATOM   4141 C  C   . ARG B 1 240 ? -0.829  7.824   -11.540 1.00 11.90 ? 240 ARG B C   1 
ATOM   4142 O  O   . ARG B 1 240 ? -1.984  8.087   -11.232 1.00 12.23 ? 240 ARG B O   1 
ATOM   4143 C  CB  . ARG B 1 240 ? 0.524   9.695   -10.555 1.00 14.21 ? 240 ARG B CB  1 
ATOM   4144 C  CG  . ARG B 1 240 ? 1.700   10.648  -10.755 1.00 18.22 ? 240 ARG B CG  1 
ATOM   4145 C  CD  . ARG B 1 240 ? 2.033   11.423  -9.477  1.00 23.86 ? 240 ARG B CD  1 
ATOM   4146 N  NE  . ARG B 1 240 ? 1.039   12.381  -8.985  1.00 27.51 ? 240 ARG B NE  1 
ATOM   4147 C  CZ  . ARG B 1 240 ? 0.249   12.145  -7.930  1.00 29.58 ? 240 ARG B CZ  1 
ATOM   4148 N  NH1 . ARG B 1 240 ? 0.342   10.999  -7.274  1.00 30.96 ? 240 ARG B NH1 1 
ATOM   4149 N  NH2 . ARG B 1 240 ? -0.618  13.054  -7.525  1.00 30.09 ? 240 ARG B NH2 1 
ATOM   4150 N  N   . GLU B 1 241 ? -0.420  6.575   -11.683 1.00 13.44 ? 241 GLU B N   1 
ATOM   4151 C  CA  . GLU B 1 241 ? -1.250  5.413   -11.371 1.00 13.57 ? 241 GLU B CA  1 
ATOM   4152 C  C   . GLU B 1 241 ? -1.463  5.335   -9.861  1.00 11.76 ? 241 GLU B C   1 
ATOM   4153 O  O   . GLU B 1 241 ? -0.543  5.438   -9.075  1.00 13.17 ? 241 GLU B O   1 
ATOM   4154 C  CB  . GLU B 1 241 ? -0.490  4.171   -11.795 1.00 16.83 ? 241 GLU B CB  1 
ATOM   4155 C  CG  . GLU B 1 241 ? -0.401  4.108   -13.311 1.00 18.49 ? 241 GLU B CG  1 
ATOM   4156 C  CD  . GLU B 1 241 ? 0.409   2.919   -13.789 1.00 25.89 ? 241 GLU B CD  1 
ATOM   4157 O  OE1 . GLU B 1 241 ? 1.381   2.559   -13.109 1.00 35.38 ? 241 GLU B OE1 1 
ATOM   4158 O  OE2 . GLU B 1 241 ? 0.044   2.340   -14.820 1.00 29.64 ? 241 GLU B OE2 1 
ATOM   4159 N  N   . MET B 1 242 ? -2.711  5.059   -9.499  1.00 10.24 ? 242 MET B N   1 
ATOM   4160 C  CA  . MET B 1 242 ? -3.066  4.837   -8.089  1.00 10.01 ? 242 MET B CA  1 
ATOM   4161 C  C   . MET B 1 242 ? -2.810  3.369   -7.693  1.00 9.01  ? 242 MET B C   1 
ATOM   4162 O  O   . MET B 1 242 ? -3.635  2.481   -7.929  1.00 9.95  ? 242 MET B O   1 
ATOM   4163 C  CB  . MET B 1 242 ? -4.534  5.193   -7.900  1.00 10.94 ? 242 MET B CB  1 
ATOM   4164 C  CG  . MET B 1 242 ? -4.913  5.150   -6.391  1.00 11.11 ? 242 MET B CG  1 
ATOM   4165 S  SD  . MET B 1 242 ? -6.603  5.504   -6.085  1.00 10.99 ? 242 MET B SD  1 
ATOM   4166 C  CE  . MET B 1 242 ? -6.729  7.197   -6.672  1.00 11.09 ? 242 MET B CE  1 
ATOM   4167 N  N   . ILE B 1 243 ? -1.592  3.170   -7.185  1.00 8.76  ? 243 ILE B N   1 
ATOM   4168 C  CA  . ILE B 1 243 ? -1.073  1.869   -6.787  1.00 9.37  ? 243 ILE B CA  1 
ATOM   4169 C  C   . ILE B 1 243 ? -0.305  2.087   -5.496  1.00 8.77  ? 243 ILE B C   1 
ATOM   4170 O  O   . ILE B 1 243 ? 0.142   3.188   -5.138  1.00 9.24  ? 243 ILE B O   1 
ATOM   4171 C  CB  . ILE B 1 243 ? -0.140  1.270   -7.874  1.00 9.36  ? 243 ILE B CB  1 
ATOM   4172 C  CG1 . ILE B 1 243 ? 1.035   2.211   -8.194  1.00 12.19 ? 243 ILE B CG1 1 
ATOM   4173 C  CG2 . ILE B 1 243 ? -0.910  0.780   -9.073  1.00 12.20 ? 243 ILE B CG2 1 
ATOM   4174 C  CD1 . ILE B 1 243 ? 2.061   1.654   -9.179  1.00 14.92 ? 243 ILE B CD1 1 
ATOM   4175 N  N   . ASN B 1 244 ? -0.173  0.997   -4.748  1.00 8.00  ? 244 ASN B N   1 
ATOM   4176 C  CA  . ASN B 1 244 ? 0.666   1.023   -3.555  1.00 8.06  ? 244 ASN B CA  1 
ATOM   4177 C  C   . ASN B 1 244 ? 0.226   2.110   -2.602  1.00 8.07  ? 244 ASN B C   1 
ATOM   4178 O  O   . ASN B 1 244 ? 1.032   2.747   -1.963  1.00 8.13  ? 244 ASN B O   1 
ATOM   4179 C  CB  . ASN B 1 244 ? 2.168   1.106   -3.831  1.00 9.85  ? 244 ASN B CB  1 
ATOM   4180 C  CG  . ASN B 1 244 ? 2.579   0.045   -4.803  1.00 11.49 ? 244 ASN B CG  1 
ATOM   4181 O  OD1 . ASN B 1 244 ? 2.209   -1.126  -4.745  1.00 12.88 ? 244 ASN B OD1 1 
ATOM   4182 N  ND2 . ASN B 1 244 ? 3.461   0.437   -5.714  1.00 14.60 ? 244 ASN B ND2 1 
ATOM   4183 N  N   . ASN B 1 245 ? -1.104  2.243   -2.412  1.00 7.41  ? 245 ASN B N   1 
ATOM   4184 C  CA  . ASN B 1 245 ? -1.653  3.326   -1.617  1.00 7.22  ? 245 ASN B CA  1 
ATOM   4185 C  C   . ASN B 1 245 ? -1.889  2.836   -0.194  1.00 7.69  ? 245 ASN B C   1 
ATOM   4186 O  O   . ASN B 1 245 ? -2.999  2.940   0.334   1.00 8.39  ? 245 ASN B O   1 
ATOM   4187 C  CB  . ASN B 1 245 ? -2.902  3.947   -2.261  1.00 7.60  ? 245 ASN B CB  1 
ATOM   4188 C  CG  . ASN B 1 245 ? -4.032  2.957   -2.422  1.00 7.36  ? 245 ASN B CG  1 
ATOM   4189 O  OD1 . ASN B 1 245 ? -3.832  1.747   -2.418  1.00 8.30  ? 245 ASN B OD1 1 
ATOM   4190 N  ND2 . ASN B 1 245 ? -5.247  3.436   -2.625  1.00 8.58  ? 245 ASN B ND2 1 
ATOM   4191 N  N   . PHE B 1 246 ? -0.840  2.339   0.418   1.00 7.32  ? 246 PHE B N   1 
ATOM   4192 C  CA  . PHE B 1 246 ? -0.883  1.908   1.819   1.00 7.43  ? 246 PHE B CA  1 
ATOM   4193 C  C   . PHE B 1 246 ? 0.299   2.499   2.556   1.00 7.31  ? 246 PHE B C   1 
ATOM   4194 O  O   . PHE B 1 246 ? 1.371   2.690   1.976   1.00 6.81  ? 246 PHE B O   1 
ATOM   4195 C  CB  . PHE B 1 246 ? -0.847  0.364   1.892   1.00 8.26  ? 246 PHE B CB  1 
ATOM   4196 C  CG  . PHE B 1 246 ? 0.411   -0.282  1.311   1.00 7.77  ? 246 PHE B CG  1 
ATOM   4197 C  CD1 . PHE B 1 246 ? 0.513   -0.546  -0.052  1.00 7.89  ? 246 PHE B CD1 1 
ATOM   4198 C  CD2 . PHE B 1 246 ? 1.500   -0.625  2.129   1.00 8.65  ? 246 PHE B CD2 1 
ATOM   4199 C  CE1 . PHE B 1 246 ? 1.664   -1.100  -0.615  1.00 8.00  ? 246 PHE B CE1 1 
ATOM   4200 C  CE2 . PHE B 1 246 ? 2.635   -1.202  1.583   1.00 9.05  ? 246 PHE B CE2 1 
ATOM   4201 C  CZ  . PHE B 1 246 ? 2.736   -1.403  0.218   1.00 8.86  ? 246 PHE B CZ  1 
ATOM   4202 N  N   . ARG B 1 247 ? 0.113   2.767   3.816   1.00 6.73  ? 247 ARG B N   1 
ATOM   4203 C  CA  . ARG B 1 247 ? 1.179   3.288   4.684   1.00 7.29  ? 247 ARG B CA  1 
ATOM   4204 C  C   . ARG B 1 247 ? 1.925   2.116   5.300   1.00 7.53  ? 247 ARG B C   1 
ATOM   4205 O  O   . ARG B 1 247 ? 1.308   1.117   5.640   1.00 7.53  ? 247 ARG B O   1 
ATOM   4206 C  CB  . ARG B 1 247 ? 0.575   4.114   5.832   1.00 7.36  ? 247 ARG B CB  1 
ATOM   4207 C  CG  . ARG B 1 247 ? 1.551   5.038   6.557   1.00 6.33  ? 247 ARG B CG  1 
ATOM   4208 C  CD  . ARG B 1 247 ? 0.855   5.692   7.714   1.00 7.63  ? 247 ARG B CD  1 
ATOM   4209 N  NE  . ARG B 1 247 ? 1.708   6.776   8.297   1.00 6.80  ? 247 ARG B NE  1 
ATOM   4210 C  CZ  . ARG B 1 247 ? 1.369   7.472   9.368   1.00 7.08  ? 247 ARG B CZ  1 
ATOM   4211 N  NH1 . ARG B 1 247 ? 0.262   7.190   10.054  1.00 7.82  ? 247 ARG B NH1 1 
ATOM   4212 N  NH2 . ARG B 1 247 ? 2.117   8.503   9.751   1.00 7.94  ? 247 ARG B NH2 1 
ATOM   4213 N  N   . GLN B 1 248 ? 3.245   2.251   5.508   1.00 6.88  ? 248 GLN B N   1 
ATOM   4214 C  CA  . GLN B 1 248 ? 3.975   1.264   6.284   1.00 7.40  ? 248 GLN B CA  1 
ATOM   4215 C  C   . GLN B 1 248 ? 3.476   1.181   7.715   1.00 6.98  ? 248 GLN B C   1 
ATOM   4216 O  O   . GLN B 1 248 ? 2.953   2.151   8.279   1.00 7.35  ? 248 GLN B O   1 
ATOM   4217 C  CB  . GLN B 1 248 ? 5.471   1.633   6.336   1.00 7.20  ? 248 GLN B CB  1 
ATOM   4218 C  CG  . GLN B 1 248 ? 6.173   1.613   4.977   1.00 7.89  ? 248 GLN B CG  1 
ATOM   4219 C  CD  . GLN B 1 248 ? 6.174   0.280   4.294   1.00 8.11  ? 248 GLN B CD  1 
ATOM   4220 O  OE1 . GLN B 1 248 ? 5.304   -0.059  3.500   1.00 9.25  ? 248 GLN B OE1 1 
ATOM   4221 N  NE2 . GLN B 1 248 ? 7.177   -0.521  4.627   1.00 9.46  ? 248 GLN B NE2 1 
ATOM   4222 N  N   . VAL B 1 249 ? 3.697   0.034   8.374   1.00 6.89  ? 249 VAL B N   1 
ATOM   4223 C  CA  . VAL B 1 249 ? 3.277   -0.085  9.774   1.00 7.59  ? 249 VAL B CA  1 
ATOM   4224 C  C   . VAL B 1 249 ? 4.132   0.813   10.679  1.00 7.14  ? 249 VAL B C   1 
ATOM   4225 O  O   . VAL B 1 249 ? 5.279   1.143   10.316  1.00 7.54  ? 249 VAL B O   1 
ATOM   4226 C  CB  . VAL B 1 249 ? 3.343   -1.533  10.270  1.00 7.79  ? 249 VAL B CB  1 
ATOM   4227 C  CG1 . VAL B 1 249 ? 2.299   -2.392  9.540   1.00 8.58  ? 249 VAL B CG1 1 
ATOM   4228 C  CG2 . VAL B 1 249 ? 4.713   -2.150  10.112  1.00 10.18 ? 249 VAL B CG2 1 
ATOM   4229 N  N   . GLN B 1 250 ? 3.550   1.188   11.790  1.00 7.52  ? 250 GLN B N   1 
ATOM   4230 C  CA  . GLN B 1 250 ? 4.082   2.187   12.704  1.00 7.94  ? 250 GLN B CA  1 
ATOM   4231 C  C   . GLN B 1 250 ? 4.565   1.561   13.995  1.00 8.92  ? 250 GLN B C   1 
ATOM   4232 O  O   . GLN B 1 250 ? 4.118   0.475   14.390  1.00 10.01 ? 250 GLN B O   1 
ATOM   4233 C  CB  . GLN B 1 250 ? 2.974   3.201   13.014  1.00 8.03  ? 250 GLN B CB  1 
ATOM   4234 C  CG  . GLN B 1 250 ? 2.308   3.812   11.790  1.00 7.82  ? 250 GLN B CG  1 
ATOM   4235 C  CD  . GLN B 1 250 ? 3.242   4.749   11.059  1.00 8.10  ? 250 GLN B CD  1 
ATOM   4236 O  OE1 . GLN B 1 250 ? 3.686   5.761   11.642  1.00 9.34  ? 250 GLN B OE1 1 
ATOM   4237 N  NE2 . GLN B 1 250 ? 3.553   4.442   9.818   1.00 8.51  ? 250 GLN B NE2 1 
ATOM   4238 N  N   . LYS B 1 251 ? 5.493   2.250   14.660  1.00 8.66  ? 251 LYS B N   1 
ATOM   4239 C  CA  . LYS B 1 251 ? 5.910   1.789   15.973  1.00 10.52 ? 251 LYS B CA  1 
ATOM   4240 C  C   . LYS B 1 251 ? 4.689   1.731   16.903  1.00 10.85 ? 251 LYS B C   1 
ATOM   4241 O  O   . LYS B 1 251 ? 3.762   2.531   16.822  1.00 10.80 ? 251 LYS B O   1 
ATOM   4242 C  CB  . LYS B 1 251 ? 6.901   2.791   16.564  1.00 11.17 ? 251 LYS B CB  1 
ATOM   4243 C  CG  . LYS B 1 251 ? 8.275   2.898   15.899  1.00 13.57 ? 251 LYS B CG  1 
ATOM   4244 C  CD  . LYS B 1 251 ? 9.169   1.819   16.453  1.00 14.22 ? 251 LYS B CD  1 
ATOM   4245 C  CE  . LYS B 1 251 ? 10.639  1.948   16.063  1.00 12.78 ? 251 LYS B CE  1 
ATOM   4246 N  NZ  . LYS B 1 251 ? 10.790  1.822   14.577  1.00 10.98 ? 251 LYS B NZ  1 
ATOM   4247 N  N   . PHE B 1 252 ? 4.702   0.790   17.857  1.00 12.40 ? 252 PHE B N   1 
ATOM   4248 C  CA  . PHE B 1 252 ? 3.608   0.655   18.815  1.00 13.90 ? 252 PHE B CA  1 
ATOM   4249 C  C   . PHE B 1 252 ? 3.463   1.786   19.831  1.00 20.99 ? 252 PHE B C   1 
ATOM   4250 O  O   . PHE B 1 252 ? 2.348   2.031   20.294  1.00 21.99 ? 252 PHE B O   1 
ATOM   4251 C  CB  . PHE B 1 252 ? 3.787   -0.659  19.569  1.00 19.11 ? 252 PHE B CB  1 
ATOM   4252 C  CG  . PHE B 1 252 ? 3.104   -1.701  18.717  1.00 21.46 ? 252 PHE B CG  1 
ATOM   4253 C  CD1 . PHE B 1 252 ? 3.783   -2.326  17.670  1.00 26.54 ? 252 PHE B CD1 1 
ATOM   4254 C  CD2 . PHE B 1 252 ? 1.748   -1.976  18.890  1.00 26.94 ? 252 PHE B CD2 1 
ATOM   4255 C  CE1 . PHE B 1 252 ? 3.152   -3.250  16.830  1.00 26.04 ? 252 PHE B CE1 1 
ATOM   4256 C  CE2 . PHE B 1 252 ? 1.133   -2.905  18.062  1.00 27.37 ? 252 PHE B CE2 1 
ATOM   4257 C  CZ  . PHE B 1 252 ? 1.821   -3.513  17.031  1.00 25.03 ? 252 PHE B CZ  1 
ATOM   4258 N  N   . ASP B 1 253 ? 4.569   2.428   20.255  1.00 20.26 ? 253 ASP B N   1 
ATOM   4259 C  CA  . ASP B 1 253 ? 4.482   3.478   21.278  1.00 24.42 ? 253 ASP B CA  1 
ATOM   4260 C  C   . ASP B 1 253 ? 3.811   2.933   22.557  1.00 27.97 ? 253 ASP B C   1 
ATOM   4261 O  O   . ASP B 1 253 ? 3.017   3.666   23.156  1.00 27.50 ? 253 ASP B O   1 
ATOM   4262 C  CB  . ASP B 1 253 ? 3.710   4.724   20.793  1.00 28.34 ? 253 ASP B CB  1 
ATOM   4263 C  CG  . ASP B 1 253 ? 4.255   5.452   19.560  1.00 34.37 ? 253 ASP B CG  1 
ATOM   4264 O  OD1 . ASP B 1 253 ? 5.475   5.356   19.317  1.00 28.83 ? 253 ASP B OD1 1 
ATOM   4265 O  OD2 . ASP B 1 253 ? 3.432   6.125   18.837  1.00 32.50 ? 253 ASP B OD2 1 
ATOM   4266 N  N   . GLU B 1 254 ? 4.117   1.676   22.968  1.00 23.57 ? 254 GLU B N   1 
ATOM   4267 C  CA  . GLU B 1 254 ? 3.685   1.049   24.216  1.00 27.46 ? 254 GLU B CA  1 
ATOM   4268 C  C   . GLU B 1 254 ? 2.227   0.553   24.193  1.00 24.28 ? 254 GLU B C   1 
ATOM   4269 O  O   . GLU B 1 254 ? 1.743   -0.014  25.183  1.00 24.98 ? 254 GLU B O   1 
ATOM   4270 C  CB  . GLU B 1 254 ? 3.998   1.936   25.431  1.00 33.55 ? 254 GLU B CB  1 
ATOM   4271 C  CG  . GLU B 1 254 ? 5.490   2.054   25.701  1.00 43.04 ? 254 GLU B CG  1 
ATOM   4272 C  CD  . GLU B 1 254 ? 5.973   3.472   25.977  1.00 53.17 ? 254 GLU B CD  1 
ATOM   4273 O  OE1 . GLU B 1 254 ? 6.630   4.074   25.081  1.00 52.93 ? 254 GLU B OE1 1 
ATOM   4274 O  OE2 . GLU B 1 254 ? 5.694   3.976   27.090  1.00 57.72 ? 254 GLU B OE2 1 
ATOM   4275 N  N   . ARG B 1 255 ? 1.537   0.703   23.058  1.00 21.96 ? 255 ARG B N   1 
ATOM   4276 C  CA  . ARG B 1 255 ? 0.173   0.211   22.922  1.00 19.27 ? 255 ARG B CA  1 
ATOM   4277 C  C   . ARG B 1 255 ? 0.152   -1.333  22.948  1.00 21.25 ? 255 ARG B C   1 
ATOM   4278 O  O   . ARG B 1 255 ? 1.062   -2.003  22.448  1.00 23.42 ? 255 ARG B O   1 
ATOM   4279 C  CB  . ARG B 1 255 ? -0.409  0.726   21.577  1.00 18.45 ? 255 ARG B CB  1 
ATOM   4280 C  CG  . ARG B 1 255 ? -0.782  2.208   21.551  1.00 21.71 ? 255 ARG B CG  1 
ATOM   4281 C  CD  . ARG B 1 255 ? -1.240  2.711   20.168  1.00 17.09 ? 255 ARG B CD  1 
ATOM   4282 N  NE  . ARG B 1 255 ? -0.143  2.785   19.214  1.00 19.93 ? 255 ARG B NE  1 
ATOM   4283 C  CZ  . ARG B 1 255 ? -0.290  3.010   17.913  1.00 17.95 ? 255 ARG B CZ  1 
ATOM   4284 N  NH1 . ARG B 1 255 ? -1.498  3.185   17.404  1.00 14.03 ? 255 ARG B NH1 1 
ATOM   4285 N  NH2 . ARG B 1 255 ? 0.769   3.059   17.126  1.00 15.88 ? 255 ARG B NH2 1 
ATOM   4286 N  N   . LEU B 1 256 ? -0.929  -1.916  23.505  1.00 19.01 ? 256 LEU B N   1 
ATOM   4287 C  CA  . LEU B 1 256 ? -1.338  -3.266  23.165  1.00 18.37 ? 256 LEU B CA  1 
ATOM   4288 C  C   . LEU B 1 256 ? -2.552  -3.235  22.235  1.00 17.04 ? 256 LEU B C   1 
ATOM   4289 O  O   . LEU B 1 256 ? -3.268  -2.223  22.088  1.00 17.74 ? 256 LEU B O   1 
ATOM   4290 C  CB  . LEU B 1 256 ? -1.731  -4.006  24.437  1.00 20.39 ? 256 LEU B CB  1 
ATOM   4291 C  CG  . LEU B 1 256 ? -0.658  -4.057  25.513  1.00 22.96 ? 256 LEU B CG  1 
ATOM   4292 C  CD1 . LEU B 1 256 ? -1.184  -4.890  26.675  1.00 26.26 ? 256 LEU B CD1 1 
ATOM   4293 C  CD2 . LEU B 1 256 ? 0.645   -4.606  24.948  1.00 24.19 ? 256 LEU B CD2 1 
ATOM   4294 N  N   . VAL B 1 257 ? -2.754  -4.376  21.615  1.00 14.63 ? 257 VAL B N   1 
ATOM   4295 C  CA  . VAL B 1 257 ? -3.938  -4.606  20.801  1.00 12.25 ? 257 VAL B CA  1 
ATOM   4296 C  C   . VAL B 1 257 ? -4.752  -5.642  21.548  1.00 12.55 ? 257 VAL B C   1 
ATOM   4297 O  O   . VAL B 1 257 ? -4.237  -6.725  21.902  1.00 14.14 ? 257 VAL B O   1 
ATOM   4298 C  CB  . VAL B 1 257 ? -3.518  -5.125  19.424  1.00 13.04 ? 257 VAL B CB  1 
ATOM   4299 C  CG1 . VAL B 1 257 ? -4.718  -5.522  18.610  1.00 12.33 ? 257 VAL B CG1 1 
ATOM   4300 C  CG2 . VAL B 1 257 ? -2.696  -4.096  18.654  1.00 12.65 ? 257 VAL B CG2 1 
ATOM   4301 N  N   . TYR B 1 258 ? -6.030  -5.359  21.754  1.00 11.16 ? 258 TYR B N   1 
ATOM   4302 C  CA  . TYR B 1 258 ? -6.911  -6.239  22.490  1.00 11.77 ? 258 TYR B CA  1 
ATOM   4303 C  C   . TYR B 1 258 ? -7.669  -7.125  21.535  1.00 12.09 ? 258 TYR B C   1 
ATOM   4304 O  O   . TYR B 1 258 ? -8.095  -6.688  20.463  1.00 12.42 ? 258 TYR B O   1 
ATOM   4305 C  CB  . TYR B 1 258 ? -7.825  -5.385  23.350  1.00 14.14 ? 258 TYR B CB  1 
ATOM   4306 C  CG  . TYR B 1 258 ? -7.008  -4.488  24.242  1.00 16.30 ? 258 TYR B CG  1 
ATOM   4307 C  CD1 . TYR B 1 258 ? -6.436  -5.029  25.403  1.00 19.15 ? 258 TYR B CD1 1 
ATOM   4308 C  CD2 . TYR B 1 258 ? -6.668  -3.192  23.865  1.00 17.26 ? 258 TYR B CD2 1 
ATOM   4309 C  CE1 . TYR B 1 258 ? -5.608  -4.258  26.206  1.00 21.42 ? 258 TYR B CE1 1 
ATOM   4310 C  CE2 . TYR B 1 258 ? -5.855  -2.411  24.686  1.00 21.99 ? 258 TYR B CE2 1 
ATOM   4311 C  CZ  . TYR B 1 258 ? -5.320  -2.949  25.846  1.00 22.70 ? 258 TYR B CZ  1 
ATOM   4312 O  OH  . TYR B 1 258 ? -4.503  -2.158  26.618  1.00 24.97 ? 258 TYR B OH  1 
ATOM   4313 N  N   . THR B 1 259 ? -7.831  -8.401  21.848  1.00 10.69 ? 259 THR B N   1 
ATOM   4314 C  CA  . THR B 1 259 ? -8.496  -9.327  20.965  1.00 10.47 ? 259 THR B CA  1 
ATOM   4315 C  C   . THR B 1 259 ? -9.772  -9.855  21.602  1.00 10.00 ? 259 THR B C   1 
ATOM   4316 O  O   . THR B 1 259 ? -9.821  -10.101 22.829  1.00 11.27 ? 259 THR B O   1 
ATOM   4317 C  CB  . THR B 1 259 ? -7.617  -10.512 20.559  1.00 10.18 ? 259 THR B CB  1 
ATOM   4318 O  OG1 . THR B 1 259 ? -7.193  -11.257 21.720  1.00 12.54 ? 259 THR B OG1 1 
ATOM   4319 C  CG2 . THR B 1 259 ? -6.343  -10.073 19.844  1.00 11.45 ? 259 THR B CG2 1 
ATOM   4320 N  N   . SER B 1 260 ? -10.812 -10.065 20.801  1.00 9.44  ? 260 SER B N   1 
ATOM   4321 C  CA  . SER B 1 260 ? -12.071 -10.612 21.313  1.00 9.74  ? 260 SER B CA  1 
ATOM   4322 C  C   . SER B 1 260 ? -12.004 -12.138 21.317  1.00 11.37 ? 260 SER B C   1 
ATOM   4323 O  O   . SER B 1 260 ? -12.989 -12.788 21.725  1.00 14.00 ? 260 SER B O   1 
ATOM   4324 C  CB  . SER B 1 260 ? -13.230 -10.150 20.420  1.00 10.55 ? 260 SER B CB  1 
ATOM   4325 O  OG  . SER B 1 260 ? -13.092 -10.732 19.144  1.00 10.31 ? 260 SER B OG  1 
ATOM   4326 N  N   . PHE B 1 261 ? -10.896 -12.738 20.871  1.00 10.87 ? 261 PHE B N   1 
ATOM   4327 C  CA  . PHE B 1 261 ? -10.710 -14.178 20.789  1.00 11.53 ? 261 PHE B CA  1 
ATOM   4328 C  C   . PHE B 1 261 ? -9.456  -14.469 21.610  1.00 12.81 ? 261 PHE B C   1 
ATOM   4329 O  O   . PHE B 1 261 ? -8.522  -13.680 21.694  1.00 12.25 ? 261 PHE B O   1 
ATOM   4330 C  CB  . PHE B 1 261 ? -10.533 -14.631 19.337  1.00 12.88 ? 261 PHE B CB  1 
ATOM   4331 C  CG  . PHE B 1 261 ? -9.478  -13.863 18.577  1.00 11.91 ? 261 PHE B CG  1 
ATOM   4332 C  CD1 . PHE B 1 261 ? -9.797  -12.644 17.973  1.00 11.03 ? 261 PHE B CD1 1 
ATOM   4333 C  CD2 . PHE B 1 261 ? -8.190  -14.360 18.439  1.00 13.37 ? 261 PHE B CD2 1 
ATOM   4334 C  CE1 . PHE B 1 261 ? -8.820  -11.963 17.261  1.00 12.07 ? 261 PHE B CE1 1 
ATOM   4335 C  CE2 . PHE B 1 261 ? -7.214  -13.638 17.757  1.00 14.08 ? 261 PHE B CE2 1 
ATOM   4336 C  CZ  . PHE B 1 261 ? -7.541  -12.450 17.149  1.00 12.89 ? 261 PHE B CZ  1 
ATOM   4337 N  N   . SER B 1 262 ? -9.456  -15.664 22.230  1.00 16.94 ? 262 SER B N   1 
ATOM   4338 C  CA  . SER B 1 262 ? -8.373  -15.906 23.166  1.00 21.91 ? 262 SER B CA  1 
ATOM   4339 C  C   . SER B 1 262 ? -7.347  -16.800 22.511  1.00 24.95 ? 262 SER B C   1 
ATOM   4340 O  O   . SER B 1 262 ? -6.201  -16.821 22.963  1.00 30.99 ? 262 SER B O   1 
ATOM   4341 C  CB  . SER B 1 262 ? -8.827  -16.456 24.509  1.00 23.52 ? 262 SER B CB  1 
ATOM   4342 O  OG  . SER B 1 262 ? -9.484  -17.698 24.344  1.00 26.63 ? 262 SER B OG  1 
ATOM   4343 N  N   . GLN B 1 263 ? -7.794  -17.572 21.517  1.00 28.33 ? 263 GLN B N   1 
ATOM   4344 C  CA  . GLN B 1 263 ? -6.944  -18.457 20.743  1.00 31.25 ? 263 GLN B CA  1 
ATOM   4345 C  C   . GLN B 1 263 ? -7.575  -18.614 19.357  1.00 29.30 ? 263 GLN B C   1 
ATOM   4346 O  O   . GLN B 1 263 ? -6.938  -19.184 18.429  1.00 30.44 ? 263 GLN B O   1 
ATOM   4347 C  CB  . GLN B 1 263 ? -6.745  -19.813 21.440  1.00 31.35 ? 263 GLN B CB  1 
ATOM   4348 C  CG  . GLN B 1 263 ? -8.040  -20.552 21.769  1.00 35.02 ? 263 GLN B CG  1 
ATOM   4349 C  CD  . GLN B 1 263 ? -7.776  -21.926 22.344  1.00 40.79 ? 263 GLN B CD  1 
ATOM   4350 O  OE1 . GLN B 1 263 ? -7.502  -22.882 21.615  1.00 46.75 ? 263 GLN B OE1 1 
ATOM   4351 N  NE2 . GLN B 1 263 ? -7.889  -22.051 23.657  1.00 34.10 ? 263 GLN B NE2 1 
ATOM   4352 O  OXT . GLN B 1 263 ? -8.735  -18.149 19.226  1.00 25.06 ? 263 GLN B OXT 1 
ATOM   4353 N  N   . LYS C 1 3   ? 32.741  19.551  -26.516 1.00 35.63 ? 3   LYS C N   1 
ATOM   4354 C  CA  . LYS C 1 3   ? 32.860  18.102  -26.223 1.00 36.38 ? 3   LYS C CA  1 
ATOM   4355 C  C   . LYS C 1 3   ? 31.639  17.338  -26.744 1.00 30.83 ? 3   LYS C C   1 
ATOM   4356 O  O   . LYS C 1 3   ? 30.792  17.848  -27.486 1.00 32.93 ? 3   LYS C O   1 
ATOM   4357 C  CB  . LYS C 1 3   ? 33.090  17.822  -24.731 1.00 38.61 ? 3   LYS C CB  1 
ATOM   4358 C  CG  . LYS C 1 3   ? 32.278  18.651  -23.742 1.00 41.53 ? 3   LYS C CG  1 
ATOM   4359 C  CD  . LYS C 1 3   ? 30.779  18.442  -23.780 1.00 41.86 ? 3   LYS C CD  1 
ATOM   4360 C  CE  . LYS C 1 3   ? 30.053  19.240  -24.848 1.00 49.45 ? 3   LYS C CE  1 
ATOM   4361 N  NZ  . LYS C 1 3   ? 30.463  20.665  -24.906 1.00 60.87 ? 3   LYS C NZ  1 
ATOM   4362 N  N   . TRP C 1 4   ? 31.560  16.093  -26.277 1.00 23.39 ? 4   TRP C N   1 
ATOM   4363 C  CA  . TRP C 1 4   ? 30.698  15.082  -26.856 1.00 16.95 ? 4   TRP C CA  1 
ATOM   4364 C  C   . TRP C 1 4   ? 30.626  13.912  -25.889 1.00 15.90 ? 4   TRP C C   1 
ATOM   4365 O  O   . TRP C 1 4   ? 31.571  13.610  -25.138 1.00 16.49 ? 4   TRP C O   1 
ATOM   4366 C  CB  . TRP C 1 4   ? 31.229  14.648  -28.239 1.00 14.67 ? 4   TRP C CB  1 
ATOM   4367 C  CG  . TRP C 1 4   ? 32.581  14.004  -28.258 1.00 12.71 ? 4   TRP C CG  1 
ATOM   4368 C  CD1 . TRP C 1 4   ? 33.802  14.593  -28.442 1.00 13.89 ? 4   TRP C CD1 1 
ATOM   4369 C  CD2 . TRP C 1 4   ? 32.863  12.597  -28.129 1.00 12.17 ? 4   TRP C CD2 1 
ATOM   4370 N  NE1 . TRP C 1 4   ? 34.795  13.667  -28.417 1.00 15.35 ? 4   TRP C NE1 1 
ATOM   4371 C  CE2 . TRP C 1 4   ? 34.255  12.413  -28.229 1.00 13.40 ? 4   TRP C CE2 1 
ATOM   4372 C  CE3 . TRP C 1 4   ? 32.054  11.448  -27.998 1.00 12.46 ? 4   TRP C CE3 1 
ATOM   4373 C  CZ2 . TRP C 1 4   ? 34.863  11.157  -28.148 1.00 13.51 ? 4   TRP C CZ2 1 
ATOM   4374 C  CZ3 . TRP C 1 4   ? 32.662  10.201  -27.910 1.00 11.59 ? 4   TRP C CZ3 1 
ATOM   4375 C  CH2 . TRP C 1 4   ? 34.051  10.044  -27.985 1.00 12.35 ? 4   TRP C CH2 1 
ATOM   4376 N  N   . THR C 1 5   ? 29.503  13.203  -25.942 1.00 14.80 ? 5   THR C N   1 
ATOM   4377 C  CA  . THR C 1 5   ? 29.286  12.058  -25.082 1.00 14.57 ? 5   THR C CA  1 
ATOM   4378 C  C   . THR C 1 5   ? 28.598  10.947  -25.875 1.00 14.12 ? 5   THR C C   1 
ATOM   4379 O  O   . THR C 1 5   ? 28.367  11.049  -27.099 1.00 13.65 ? 5   THR C O   1 
ATOM   4380 C  CB  . THR C 1 5   ? 28.308  12.450  -23.968 1.00 17.64 ? 5   THR C CB  1 
ATOM   4381 O  OG1 . THR C 1 5   ? 27.055  12.733  -24.614 1.00 18.19 ? 5   THR C OG1 1 
ATOM   4382 C  CG2 . THR C 1 5   ? 28.785  13.656  -23.165 1.00 19.12 ? 5   THR C CG2 1 
ATOM   4383 N  N   . TYR C 1 6   ? 28.175  9.894   -25.142 1.00 14.22 ? 6   TYR C N   1 
ATOM   4384 C  CA  . TYR C 1 6   ? 27.283  8.876   -25.697 1.00 14.94 ? 6   TYR C CA  1 
ATOM   4385 C  C   . TYR C 1 6   ? 25.857  8.928   -25.164 1.00 16.37 ? 6   TYR C C   1 
ATOM   4386 O  O   . TYR C 1 6   ? 25.157  7.907   -25.143 1.00 17.89 ? 6   TYR C O   1 
ATOM   4387 C  CB  . TYR C 1 6   ? 27.871  7.472   -25.524 1.00 13.71 ? 6   TYR C CB  1 
ATOM   4388 C  CG  . TYR C 1 6   ? 29.168  7.222   -26.246 1.00 12.93 ? 6   TYR C CG  1 
ATOM   4389 C  CD1 . TYR C 1 6   ? 30.410  7.452   -25.664 1.00 12.63 ? 6   TYR C CD1 1 
ATOM   4390 C  CD2 . TYR C 1 6   ? 29.158  6.669   -27.516 1.00 11.85 ? 6   TYR C CD2 1 
ATOM   4391 C  CE1 . TYR C 1 6   ? 31.603  7.183   -26.327 1.00 12.77 ? 6   TYR C CE1 1 
ATOM   4392 C  CE2 . TYR C 1 6   ? 30.322  6.412   -28.190 1.00 10.27 ? 6   TYR C CE2 1 
ATOM   4393 C  CZ  . TYR C 1 6   ? 31.556  6.671   -27.626 1.00 10.64 ? 6   TYR C CZ  1 
ATOM   4394 O  OH  . TYR C 1 6   ? 32.710  6.361   -28.262 1.00 13.43 ? 6   TYR C OH  1 
ATOM   4395 N  N   . PHE C 1 7   ? 25.390  10.094  -24.738 1.00 20.51 ? 7   PHE C N   1 
ATOM   4396 C  CA  . PHE C 1 7   ? 23.954  10.205  -24.352 1.00 23.27 ? 7   PHE C CA  1 
ATOM   4397 C  C   . PHE C 1 7   ? 23.478  11.601  -24.733 1.00 23.91 ? 7   PHE C C   1 
ATOM   4398 O  O   . PHE C 1 7   ? 24.250  12.496  -24.688 1.00 23.49 ? 7   PHE C O   1 
ATOM   4399 C  CB  . PHE C 1 7   ? 23.707  9.894   -22.879 1.00 25.67 ? 7   PHE C CB  1 
ATOM   4400 C  CG  . PHE C 1 7   ? 24.400  10.853  -21.954 1.00 29.54 ? 7   PHE C CG  1 
ATOM   4401 C  CD1 . PHE C 1 7   ? 23.711  11.885  -21.361 1.00 29.37 ? 7   PHE C CD1 1 
ATOM   4402 C  CD2 . PHE C 1 7   ? 25.739  10.713  -21.689 1.00 30.39 ? 7   PHE C CD2 1 
ATOM   4403 C  CE1 . PHE C 1 7   ? 24.353  12.763  -20.506 1.00 30.62 ? 7   PHE C CE1 1 
ATOM   4404 C  CE2 . PHE C 1 7   ? 26.390  11.598  -20.846 1.00 30.76 ? 7   PHE C CE2 1 
ATOM   4405 C  CZ  . PHE C 1 7   ? 25.696  12.630  -20.278 1.00 31.08 ? 7   PHE C CZ  1 
ATOM   4406 N  N   . GLY C 1 8   ? 22.208  11.798  -25.066 1.00 20.92 ? 8   GLY C N   1 
ATOM   4407 C  CA  . GLY C 1 8   ? 21.808  13.165  -25.452 1.00 25.15 ? 8   GLY C CA  1 
ATOM   4408 C  C   . GLY C 1 8   ? 21.893  14.099  -24.264 1.00 29.12 ? 8   GLY C C   1 
ATOM   4409 O  O   . GLY C 1 8   ? 21.657  13.636  -23.152 1.00 34.43 ? 8   GLY C O   1 
ATOM   4410 N  N   . PRO C 1 9   ? 22.074  15.414  -24.446 1.00 18.91 ? 9   PRO C N   1 
ATOM   4411 C  CA  . PRO C 1 9   ? 22.048  16.057  -25.761 1.00 19.13 ? 9   PRO C CA  1 
ATOM   4412 C  C   . PRO C 1 9   ? 23.364  16.213  -26.537 1.00 17.82 ? 9   PRO C C   1 
ATOM   4413 O  O   . PRO C 1 9   ? 23.366  16.768  -27.567 1.00 19.07 ? 9   PRO C O   1 
ATOM   4414 C  CB  . PRO C 1 9   ? 21.623  17.498  -25.395 1.00 20.66 ? 9   PRO C CB  1 
ATOM   4415 C  CG  . PRO C 1 9   ? 22.194  17.713  -24.013 1.00 19.73 ? 9   PRO C CG  1 
ATOM   4416 C  CD  . PRO C 1 9   ? 22.102  16.377  -23.331 1.00 19.05 ? 9   PRO C CD  1 
ATOM   4417 N  N   . ASP C 1 10  ? 24.456  15.754  -25.955 1.00 18.67 ? 10  ASP C N   1 
ATOM   4418 C  CA  . ASP C 1 10  ? 25.755  15.843  -26.608 1.00 18.94 ? 10  ASP C CA  1 
ATOM   4419 C  C   . ASP C 1 10  ? 26.191  14.486  -27.154 1.00 16.05 ? 10  ASP C C   1 
ATOM   4420 O  O   . ASP C 1 10  ? 27.347  14.325  -27.536 1.00 14.41 ? 10  ASP C O   1 
ATOM   4421 C  CB  . ASP C 1 10  ? 26.846  16.413  -25.693 1.00 20.27 ? 10  ASP C CB  1 
ATOM   4422 C  CG  . ASP C 1 10  ? 26.556  17.861  -25.311 1.00 25.70 ? 10  ASP C CG  1 
ATOM   4423 O  OD1 . ASP C 1 10  ? 26.116  18.624  -26.186 1.00 28.84 ? 10  ASP C OD1 1 
ATOM   4424 O  OD2 . ASP C 1 10  ? 26.724  18.192  -24.128 1.00 32.58 ? 10  ASP C OD2 1 
ATOM   4425 N  N   . GLY C 1 11  ? 25.211  13.590  -27.292 1.00 16.51 ? 11  GLY C N   1 
ATOM   4426 C  CA  . GLY C 1 11  ? 25.498  12.223  -27.732 1.00 14.53 ? 11  GLY C CA  1 
ATOM   4427 C  C   . GLY C 1 11  ? 25.508  12.099  -29.256 1.00 12.74 ? 11  GLY C C   1 
ATOM   4428 O  O   . GLY C 1 11  ? 25.549  13.083  -30.009 1.00 12.39 ? 11  GLY C O   1 
ATOM   4429 N  N   . GLU C 1 12  ? 25.487  10.833  -29.715 1.00 10.68 ? 12  GLU C N   1 
ATOM   4430 C  CA  . GLU C 1 12  ? 25.971  10.573  -31.067 1.00 9.22  ? 12  GLU C CA  1 
ATOM   4431 C  C   . GLU C 1 12  ? 25.101  11.219  -32.151 1.00 9.03  ? 12  GLU C C   1 
ATOM   4432 O  O   . GLU C 1 12  ? 25.647  11.534  -33.205 1.00 9.22  ? 12  GLU C O   1 
ATOM   4433 C  CB  . GLU C 1 12  ? 26.155  9.066   -31.277 1.00 9.09  ? 12  GLU C CB  1 
ATOM   4434 C  CG  . GLU C 1 12  ? 24.846  8.293   -31.407 1.00 9.71  ? 12  GLU C CG  1 
ATOM   4435 C  CD  . GLU C 1 12  ? 25.113  6.807   -31.212 1.00 9.19  ? 12  GLU C CD  1 
ATOM   4436 O  OE1 . GLU C 1 12  ? 25.382  6.081   -32.163 1.00 9.72  ? 12  GLU C OE1 1 
ATOM   4437 O  OE2 . GLU C 1 12  ? 25.093  6.393   -29.990 1.00 11.47 ? 12  GLU C OE2 1 
ATOM   4438 N  N   . ASN C 1 13  ? 23.797  11.372  -31.931 1.00 8.94  ? 13  ASN C N   1 
ATOM   4439 C  CA  . ASN C 1 13  ? 23.003  12.034  -32.982 1.00 9.34  ? 13  ASN C CA  1 
ATOM   4440 C  C   . ASN C 1 13  ? 23.340  13.514  -33.166 1.00 9.43  ? 13  ASN C C   1 
ATOM   4441 O  O   . ASN C 1 13  ? 22.979  14.061  -34.199 1.00 10.13 ? 13  ASN C O   1 
ATOM   4442 C  CB  . ASN C 1 13  ? 21.512  11.858  -32.717 1.00 9.21  ? 13  ASN C CB  1 
ATOM   4443 C  CG  . ASN C 1 13  ? 21.060  10.411  -32.797 1.00 9.17  ? 13  ASN C CG  1 
ATOM   4444 O  OD1 . ASN C 1 13  ? 21.746  9.521   -33.331 1.00 10.41 ? 13  ASN C OD1 1 
ATOM   4445 N  ND2 . ASN C 1 13  ? 19.874  10.216  -32.298 1.00 8.90  ? 13  ASN C ND2 1 
ATOM   4446 N  N   . SER C 1 14  ? 23.990  14.101  -32.136 1.00 9.47  ? 14  SER C N   1 
ATOM   4447 C  CA  . SER C 1 14  ? 24.388  15.520  -32.175 1.00 9.88  ? 14  SER C CA  1 
ATOM   4448 C  C   . SER C 1 14  ? 25.841  15.720  -32.542 1.00 9.71  ? 14  SER C C   1 
ATOM   4449 O  O   . SER C 1 14  ? 26.222  16.879  -32.784 1.00 10.48 ? 14  SER C O   1 
ATOM   4450 C  CB  . SER C 1 14  ? 24.149  16.166  -30.825 1.00 12.88 ? 14  SER C CB  1 
ATOM   4451 O  OG  . SER C 1 14  ? 22.764  16.175  -30.551 1.00 16.94 ? 14  SER C OG  1 
ATOM   4452 N  N   . TRP C 1 15  ? 26.628  14.658  -32.704 1.00 9.37  ? 15  TRP C N   1 
ATOM   4453 C  CA  . TRP C 1 15  ? 28.045  14.866  -33.003 1.00 9.68  ? 15  TRP C CA  1 
ATOM   4454 C  C   . TRP C 1 15  ? 28.249  15.711  -34.264 1.00 9.84  ? 15  TRP C C   1 
ATOM   4455 O  O   . TRP C 1 15  ? 29.194  16.500  -34.378 1.00 10.25 ? 15  TRP C O   1 
ATOM   4456 C  CB  . TRP C 1 15  ? 28.742  13.542  -33.221 1.00 8.88  ? 15  TRP C CB  1 
ATOM   4457 C  CG  . TRP C 1 15  ? 28.899  12.712  -31.979 1.00 8.53  ? 15  TRP C CG  1 
ATOM   4458 C  CD1 . TRP C 1 15  ? 28.588  13.044  -30.680 1.00 9.21  ? 15  TRP C CD1 1 
ATOM   4459 C  CD2 . TRP C 1 15  ? 29.352  11.349  -31.948 1.00 9.35  ? 15  TRP C CD2 1 
ATOM   4460 N  NE1 . TRP C 1 15  ? 28.919  11.990  -29.835 1.00 9.63  ? 15  TRP C NE1 1 
ATOM   4461 C  CE2 . TRP C 1 15  ? 29.359  10.925  -30.598 1.00 8.96  ? 15  TRP C CE2 1 
ATOM   4462 C  CE3 . TRP C 1 15  ? 29.770  10.450  -32.951 1.00 8.87  ? 15  TRP C CE3 1 
ATOM   4463 C  CZ2 . TRP C 1 15  ? 29.753  9.639   -30.231 1.00 9.43  ? 15  TRP C CZ2 1 
ATOM   4464 C  CZ3 . TRP C 1 15  ? 30.180  9.182   -32.571 1.00 8.20  ? 15  TRP C CZ3 1 
ATOM   4465 C  CH2 . TRP C 1 15  ? 30.149  8.783   -31.230 1.00 9.35  ? 15  TRP C CH2 1 
ATOM   4466 N  N   . SER C 1 16  ? 27.374  15.544  -35.252 1.00 9.64  ? 16  SER C N   1 
ATOM   4467 C  CA  . SER C 1 16  ? 27.546  16.171  -36.565 1.00 9.23  ? 16  SER C CA  1 
ATOM   4468 C  C   . SER C 1 16  ? 27.463  17.697  -36.485 1.00 10.69 ? 16  SER C C   1 
ATOM   4469 O  O   . SER C 1 16  ? 27.927  18.333  -37.421 1.00 10.97 ? 16  SER C O   1 
ATOM   4470 C  CB  . SER C 1 16  ? 26.541  15.680  -37.579 1.00 10.18 ? 16  SER C CB  1 
ATOM   4471 O  OG  . SER C 1 16  ? 25.232  16.046  -37.164 1.00 10.90 ? 16  SER C OG  1 
ATOM   4472 N  N   A LYS C 1 17  ? 26.901  18.254  -35.418 0.50 10.66 ? 17  LYS C N   1 
ATOM   4473 N  N   B LYS C 1 17  ? 26.946  18.219  -35.374 0.50 10.97 ? 17  LYS C N   1 
ATOM   4474 C  CA  A LYS C 1 17  ? 26.898  19.713  -35.319 0.50 10.99 ? 17  LYS C CA  1 
ATOM   4475 C  CA  B LYS C 1 17  ? 26.818  19.666  -35.284 0.50 11.66 ? 17  LYS C CA  1 
ATOM   4476 C  C   A LYS C 1 17  ? 28.339  20.225  -35.331 0.50 10.52 ? 17  LYS C C   1 
ATOM   4477 C  C   B LYS C 1 17  ? 28.179  20.327  -35.123 0.50 11.54 ? 17  LYS C C   1 
ATOM   4478 O  O   A LYS C 1 17  ? 28.763  21.078  -36.133 0.50 9.61  ? 17  LYS C O   1 
ATOM   4479 O  O   B LYS C 1 17  ? 28.333  21.437  -35.576 0.50 11.88 ? 17  LYS C O   1 
ATOM   4480 C  CB  A LYS C 1 17  ? 26.196  20.102  -34.014 0.50 11.19 ? 17  LYS C CB  1 
ATOM   4481 C  CB  B LYS C 1 17  ? 25.896  20.079  -34.141 0.50 11.88 ? 17  LYS C CB  1 
ATOM   4482 C  CG  A LYS C 1 17  ? 24.763  19.593  -33.870 0.50 14.47 ? 17  LYS C CG  1 
ATOM   4483 C  CG  B LYS C 1 17  ? 24.412  19.828  -34.384 0.50 14.09 ? 17  LYS C CG  1 
ATOM   4484 C  CD  A LYS C 1 17  ? 24.114  19.929  -32.543 0.50 13.70 ? 17  LYS C CD  1 
ATOM   4485 C  CD  B LYS C 1 17  ? 23.591  20.133  -33.159 0.50 14.63 ? 17  LYS C CD  1 
ATOM   4486 C  CE  A LYS C 1 17  ? 22.819  19.177  -32.333 0.50 12.79 ? 17  LYS C CE  1 
ATOM   4487 C  CE  B LYS C 1 17  ? 23.608  21.615  -32.840 0.50 16.61 ? 17  LYS C CE  1 
ATOM   4488 N  NZ  A LYS C 1 17  ? 22.218  19.473  -31.010 0.50 13.78 ? 17  LYS C NZ  1 
ATOM   4489 N  NZ  B LYS C 1 17  ? 22.768  21.911  -31.660 0.50 18.85 ? 17  LYS C NZ  1 
ATOM   4490 N  N   . LYS C 1 18  ? 29.108  19.731  -34.361 1.00 10.65 ? 18  LYS C N   1 
ATOM   4491 C  CA  . LYS C 1 18  ? 30.472  20.229  -34.197 1.00 12.91 ? 18  LYS C CA  1 
ATOM   4492 C  C   . LYS C 1 18  ? 31.460  19.499  -35.095 1.00 14.51 ? 18  LYS C C   1 
ATOM   4493 O  O   . LYS C 1 18  ? 32.562  19.984  -35.348 1.00 15.68 ? 18  LYS C O   1 
ATOM   4494 C  CB  . LYS C 1 18  ? 30.916  20.171  -32.729 1.00 15.49 ? 18  LYS C CB  1 
ATOM   4495 C  CG  . LYS C 1 18  ? 30.326  21.183  -31.737 1.00 24.42 ? 18  LYS C CG  1 
ATOM   4496 C  CD  . LYS C 1 18  ? 30.304  22.671  -32.139 1.00 30.36 ? 18  LYS C CD  1 
ATOM   4497 C  CE  . LYS C 1 18  ? 31.613  23.435  -32.054 1.00 36.07 ? 18  LYS C CE  1 
ATOM   4498 N  NZ  . LYS C 1 18  ? 31.569  24.571  -31.094 1.00 38.98 ? 18  LYS C NZ  1 
ATOM   4499 N  N   . TYR C 1 19  ? 31.143  18.257  -35.515 1.00 11.62 ? 19  TYR C N   1 
ATOM   4500 C  CA  . TYR C 1 19  ? 32.061  17.389  -36.227 1.00 10.75 ? 19  TYR C CA  1 
ATOM   4501 C  C   . TYR C 1 19  ? 31.387  16.931  -37.508 1.00 10.77 ? 19  TYR C C   1 
ATOM   4502 O  O   . TYR C 1 19  ? 30.703  15.873  -37.525 1.00 10.81 ? 19  TYR C O   1 
ATOM   4503 C  CB  . TYR C 1 19  ? 32.407  16.158  -35.378 1.00 11.61 ? 19  TYR C CB  1 
ATOM   4504 C  CG  . TYR C 1 19  ? 33.012  16.547  -34.045 1.00 11.67 ? 19  TYR C CG  1 
ATOM   4505 C  CD1 . TYR C 1 19  ? 34.355  16.902  -33.973 1.00 12.68 ? 19  TYR C CD1 1 
ATOM   4506 C  CD2 . TYR C 1 19  ? 32.273  16.561  -32.875 1.00 12.41 ? 19  TYR C CD2 1 
ATOM   4507 C  CE1 . TYR C 1 19  ? 34.954  17.244  -32.768 1.00 13.47 ? 19  TYR C CE1 1 
ATOM   4508 C  CE2 . TYR C 1 19  ? 32.870  16.907  -31.667 1.00 13.63 ? 19  TYR C CE2 1 
ATOM   4509 C  CZ  . TYR C 1 19  ? 34.198  17.234  -31.612 1.00 13.31 ? 19  TYR C CZ  1 
ATOM   4510 O  OH  . TYR C 1 19  ? 34.772  17.526  -30.375 1.00 18.32 ? 19  TYR C OH  1 
ATOM   4511 N  N   . PRO C 1 20  ? 31.455  17.718  -38.589 1.00 9.99  ? 20  PRO C N   1 
ATOM   4512 C  CA  . PRO C 1 20  ? 30.600  17.481  -39.730 1.00 10.81 ? 20  PRO C CA  1 
ATOM   4513 C  C   . PRO C 1 20  ? 30.784  16.106  -40.381 1.00 10.94 ? 20  PRO C C   1 
ATOM   4514 O  O   . PRO C 1 20  ? 29.845  15.574  -40.958 1.00 10.64 ? 20  PRO C O   1 
ATOM   4515 C  CB  . PRO C 1 20  ? 30.884  18.605  -40.750 1.00 12.42 ? 20  PRO C CB  1 
ATOM   4516 C  CG  . PRO C 1 20  ? 31.662  19.648  -39.919 1.00 16.00 ? 20  PRO C CG  1 
ATOM   4517 C  CD  . PRO C 1 20  ? 32.204  18.992  -38.664 1.00 12.01 ? 20  PRO C CD  1 
ATOM   4518 N  N   . SER C 1 21  ? 31.971  15.540  -40.255 1.00 10.18 ? 21  SER C N   1 
ATOM   4519 C  CA  . SER C 1 21  ? 32.167  14.219  -40.848 1.00 10.17 ? 21  SER C CA  1 
ATOM   4520 C  C   . SER C 1 21  ? 31.293  13.151  -40.205 1.00 9.92  ? 21  SER C C   1 
ATOM   4521 O  O   . SER C 1 21  ? 31.076  12.139  -40.850 1.00 9.53  ? 21  SER C O   1 
ATOM   4522 C  CB  . SER C 1 21  ? 33.627  13.794  -40.760 1.00 10.59 ? 21  SER C CB  1 
ATOM   4523 O  OG  . SER C 1 21  ? 34.383  14.625  -41.656 1.00 13.18 ? 21  SER C OG  1 
ATOM   4524 N  N   . CYS C 1 22  ? 30.785  13.387  -39.001 1.00 9.52  ? 22  CYS C N   1 
ATOM   4525 C  CA  . CYS C 1 22  ? 29.929  12.367  -38.387 1.00 10.04 ? 22  CYS C CA  1 
ATOM   4526 C  C   . CYS C 1 22  ? 28.599  12.210  -39.101 1.00 10.97 ? 22  CYS C C   1 
ATOM   4527 O  O   . CYS C 1 22  ? 27.918  11.201  -38.884 1.00 10.37 ? 22  CYS C O   1 
ATOM   4528 C  CB  . CYS C 1 22  ? 29.724  12.682  -36.914 1.00 10.08 ? 22  CYS C CB  1 
ATOM   4529 S  SG  . CYS C 1 22  ? 31.235  12.784  -35.915 1.00 11.31 ? 22  CYS C SG  1 
ATOM   4530 N  N   . GLY C 1 23  ? 28.247  13.148  -39.967 1.00 10.72 ? 23  GLY C N   1 
ATOM   4531 C  CA  . GLY C 1 23  ? 27.066  13.022  -40.829 1.00 10.21 ? 23  GLY C CA  1 
ATOM   4532 C  C   . GLY C 1 23  ? 27.426  12.821  -42.295 1.00 9.93  ? 23  GLY C C   1 
ATOM   4533 O  O   . GLY C 1 23  ? 26.525  12.874  -43.136 1.00 10.15 ? 23  GLY C O   1 
ATOM   4534 N  N   . GLY C 1 24  ? 28.686  12.516  -42.583 1.00 9.66  ? 24  GLY C N   1 
ATOM   4535 C  CA  . GLY C 1 24  ? 29.162  12.328  -43.946 1.00 10.97 ? 24  GLY C CA  1 
ATOM   4536 C  C   . GLY C 1 24  ? 29.231  10.856  -44.352 1.00 11.64 ? 24  GLY C C   1 
ATOM   4537 O  O   . GLY C 1 24  ? 28.533  10.003  -43.787 1.00 12.57 ? 24  GLY C O   1 
ATOM   4538 N  N   . LEU C 1 25  ? 30.028  10.603  -45.370 1.00 12.61 ? 25  LEU C N   1 
ATOM   4539 C  CA  . LEU C 1 25  ? 30.161  9.267   -45.973 1.00 13.36 ? 25  LEU C CA  1 
ATOM   4540 C  C   . LEU C 1 25  ? 31.046  8.359   -45.105 1.00 12.44 ? 25  LEU C C   1 
ATOM   4541 O  O   . LEU C 1 25  ? 31.842  8.783   -44.262 1.00 11.40 ? 25  LEU C O   1 
ATOM   4542 C  CB  . LEU C 1 25  ? 30.783  9.404   -47.371 1.00 16.70 ? 25  LEU C CB  1 
ATOM   4543 C  CG  . LEU C 1 25  ? 29.991  10.358  -48.275 1.00 20.16 ? 25  LEU C CG  1 
ATOM   4544 C  CD1 . LEU C 1 25  ? 30.603  10.437  -49.671 1.00 24.38 ? 25  LEU C CD1 1 
ATOM   4545 C  CD2 . LEU C 1 25  ? 28.553  9.889   -48.368 1.00 24.56 ? 25  LEU C CD2 1 
ATOM   4546 N  N   . LEU C 1 26  ? 30.984  7.070   -45.465 1.00 12.34 ? 26  LEU C N   1 
ATOM   4547 C  CA  . LEU C 1 26  ? 31.860  5.990   -45.031 1.00 12.19 ? 26  LEU C CA  1 
ATOM   4548 C  C   . LEU C 1 26  ? 31.854  5.847   -43.501 1.00 11.30 ? 26  LEU C C   1 
ATOM   4549 O  O   . LEU C 1 26  ? 32.872  5.501   -42.934 1.00 12.60 ? 26  LEU C O   1 
ATOM   4550 C  CB  . LEU C 1 26  ? 33.298  6.267   -45.510 1.00 14.77 ? 26  LEU C CB  1 
ATOM   4551 C  CG  . LEU C 1 26  ? 33.631  6.273   -47.016 1.00 18.85 ? 26  LEU C CG  1 
ATOM   4552 C  CD1 . LEU C 1 26  ? 35.161  6.181   -47.223 1.00 21.27 ? 26  LEU C CD1 1 
ATOM   4553 C  CD2 . LEU C 1 26  ? 32.912  5.195   -47.825 1.00 19.41 ? 26  LEU C CD2 1 
ATOM   4554 N  N   . GLN C 1 27  ? 30.739  6.040   -42.822 1.00 9.02  ? 27  GLN C N   1 
ATOM   4555 C  CA  . GLN C 1 27  ? 30.702  5.971   -41.368 1.00 8.76  ? 27  GLN C CA  1 
ATOM   4556 C  C   . GLN C 1 27  ? 30.764  4.533   -40.880 1.00 9.63  ? 27  GLN C C   1 
ATOM   4557 O  O   . GLN C 1 27  ? 30.120  3.615   -41.378 1.00 11.13 ? 27  GLN C O   1 
ATOM   4558 C  CB  . GLN C 1 27  ? 29.534  6.737   -40.798 1.00 8.40  ? 27  GLN C CB  1 
ATOM   4559 C  CG  . GLN C 1 27  ? 29.623  8.235   -41.133 1.00 7.96  ? 27  GLN C CG  1 
ATOM   4560 C  CD  . GLN C 1 27  ? 30.779  8.863   -40.407 1.00 8.00  ? 27  GLN C CD  1 
ATOM   4561 O  OE1 . GLN C 1 27  ? 30.737  9.075   -39.193 1.00 8.12  ? 27  GLN C OE1 1 
ATOM   4562 N  NE2 . GLN C 1 27  ? 31.832  9.164   -41.158 1.00 8.50  ? 27  GLN C NE2 1 
ATOM   4563 N  N   . SER C 1 28  ? 31.488  4.381   -39.767 1.00 8.45  ? 28  SER C N   1 
ATOM   4564 C  CA  . SER C 1 28  ? 31.607  3.149   -38.988 1.00 7.65  ? 28  SER C CA  1 
ATOM   4565 C  C   . SER C 1 28  ? 30.984  3.347   -37.619 1.00 7.77  ? 28  SER C C   1 
ATOM   4566 O  O   . SER C 1 28  ? 30.889  4.491   -37.148 1.00 8.70  ? 28  SER C O   1 
ATOM   4567 C  CB  . SER C 1 28  ? 33.084  2.814   -38.826 1.00 7.96  ? 28  SER C CB  1 
ATOM   4568 O  OG  . SER C 1 28  ? 33.653  2.563   -40.115 1.00 8.67  ? 28  SER C OG  1 
ATOM   4569 N  N   . PRO C 1 29  ? 30.594  2.289   -36.894 1.00 7.58  ? 29  PRO C N   1 
ATOM   4570 C  CA  . PRO C 1 29  ? 30.728  0.881   -37.265 1.00 7.11  ? 29  PRO C CA  1 
ATOM   4571 C  C   . PRO C 1 29  ? 29.510  0.426   -38.077 1.00 7.18  ? 29  PRO C C   1 
ATOM   4572 O  O   . PRO C 1 29  ? 28.592  1.172   -38.358 1.00 7.63  ? 29  PRO C O   1 
ATOM   4573 C  CB  . PRO C 1 29  ? 30.724  0.186   -35.878 1.00 7.56  ? 29  PRO C CB  1 
ATOM   4574 C  CG  . PRO C 1 29  ? 29.740  1.025   -35.086 1.00 7.94  ? 29  PRO C CG  1 
ATOM   4575 C  CD  . PRO C 1 29  ? 30.015  2.449   -35.559 1.00 7.45  ? 29  PRO C CD  1 
ATOM   4576 N  N   . ILE C 1 30  ? 29.548  -0.829  -38.492 1.00 7.77  ? 30  ILE C N   1 
ATOM   4577 C  CA  . ILE C 1 30  ? 28.530  -1.411  -39.363 1.00 7.43  ? 30  ILE C CA  1 
ATOM   4578 C  C   . ILE C 1 30  ? 28.256  -2.830  -38.859 1.00 8.62  ? 30  ILE C C   1 
ATOM   4579 O  O   . ILE C 1 30  ? 29.029  -3.449  -38.078 1.00 8.59  ? 30  ILE C O   1 
ATOM   4580 C  CB  . ILE C 1 30  ? 29.026  -1.453  -40.829 1.00 8.38  ? 30  ILE C CB  1 
ATOM   4581 C  CG1 . ILE C 1 30  ? 30.281  -2.335  -40.988 1.00 8.65  ? 30  ILE C CG1 1 
ATOM   4582 C  CG2 . ILE C 1 30  ? 29.235  -0.014  -41.341 1.00 10.01 ? 30  ILE C CG2 1 
ATOM   4583 C  CD1 . ILE C 1 30  ? 30.647  -2.609  -42.447 1.00 10.19 ? 30  ILE C CD1 1 
ATOM   4584 N  N   . ASP C 1 31  ? 27.134  -3.342  -39.359 1.00 9.22  ? 31  ASP C N   1 
ATOM   4585 C  CA  . ASP C 1 31  ? 26.771  -4.737  -39.150 1.00 10.34 ? 31  ASP C CA  1 
ATOM   4586 C  C   . ASP C 1 31  ? 27.373  -5.594  -40.244 1.00 10.84 ? 31  ASP C C   1 
ATOM   4587 O  O   . ASP C 1 31  ? 27.252  -5.281  -41.443 1.00 12.81 ? 31  ASP C O   1 
ATOM   4588 C  CB  . ASP C 1 31  ? 25.259  -4.912  -39.279 1.00 11.01 ? 31  ASP C CB  1 
ATOM   4589 C  CG  . ASP C 1 31  ? 24.839  -6.353  -38.996 1.00 12.31 ? 31  ASP C CG  1 
ATOM   4590 O  OD1 . ASP C 1 31  ? 25.336  -7.007  -38.026 1.00 12.53 ? 31  ASP C OD1 1 
ATOM   4591 O  OD2 . ASP C 1 31  ? 23.989  -6.860  -39.780 1.00 16.76 ? 31  ASP C OD2 1 
ATOM   4592 N  N   . LEU C 1 32  ? 28.085  -6.643  -39.847 1.00 10.61 ? 32  LEU C N   1 
ATOM   4593 C  CA  . LEU C 1 32  ? 28.758  -7.571  -40.746 1.00 12.07 ? 32  LEU C CA  1 
ATOM   4594 C  C   . LEU C 1 32  ? 27.884  -8.800  -40.915 1.00 12.61 ? 32  LEU C C   1 
ATOM   4595 O  O   . LEU C 1 32  ? 27.663  -9.567  -39.975 1.00 13.21 ? 32  LEU C O   1 
ATOM   4596 C  CB  . LEU C 1 32  ? 30.099  -7.983  -40.111 1.00 12.06 ? 32  LEU C CB  1 
ATOM   4597 C  CG  . LEU C 1 32  ? 31.011  -6.820  -39.699 1.00 12.69 ? 32  LEU C CG  1 
ATOM   4598 C  CD1 . LEU C 1 32  ? 32.234  -7.294  -38.931 1.00 13.68 ? 32  LEU C CD1 1 
ATOM   4599 C  CD2 . LEU C 1 32  ? 31.421  -6.075  -40.969 1.00 14.64 ? 32  LEU C CD2 1 
ATOM   4600 N  N   . HIS C 1 33  ? 27.307  -8.965  -42.108 1.00 15.50 ? 33  HIS C N   1 
ATOM   4601 C  CA  . HIS C 1 33  ? 26.319  -10.026 -42.291 1.00 17.71 ? 33  HIS C CA  1 
ATOM   4602 C  C   . HIS C 1 33  ? 26.505  -10.633 -43.677 1.00 18.45 ? 33  HIS C C   1 
ATOM   4603 O  O   . HIS C 1 33  ? 26.978  -9.949  -44.568 1.00 16.69 ? 33  HIS C O   1 
ATOM   4604 C  CB  . HIS C 1 33  ? 24.888  -9.517  -42.064 1.00 18.85 ? 33  HIS C CB  1 
ATOM   4605 C  CG  . HIS C 1 33  ? 24.459  -8.426  -42.976 1.00 19.03 ? 33  HIS C CG  1 
ATOM   4606 N  ND1 . HIS C 1 33  ? 23.764  -8.691  -44.151 1.00 24.31 ? 33  HIS C ND1 1 
ATOM   4607 C  CD2 . HIS C 1 33  ? 24.591  -7.085  -42.886 1.00 19.46 ? 33  HIS C CD2 1 
ATOM   4608 C  CE1 . HIS C 1 33  ? 23.509  -7.544  -44.735 1.00 23.60 ? 33  HIS C CE1 1 
ATOM   4609 N  NE2 . HIS C 1 33  ? 24.012  -6.556  -44.012 1.00 23.25 ? 33  HIS C NE2 1 
ATOM   4610 N  N   . SER C 1 34  ? 26.044  -11.883 -43.877 1.00 18.96 ? 34  SER C N   1 
ATOM   4611 C  CA  . SER C 1 34  ? 26.435  -12.720 -45.007 1.00 21.66 ? 34  SER C CA  1 
ATOM   4612 C  C   . SER C 1 34  ? 26.210  -12.057 -46.349 1.00 20.47 ? 34  SER C C   1 
ATOM   4613 O  O   . SER C 1 34  ? 27.045  -12.238 -47.244 1.00 19.41 ? 34  SER C O   1 
ATOM   4614 C  CB  . SER C 1 34  ? 25.684  -14.032 -44.994 1.00 23.27 ? 34  SER C CB  1 
ATOM   4615 O  OG  . SER C 1 34  ? 25.879  -14.668 -43.753 1.00 33.20 ? 34  SER C OG  1 
ATOM   4616 N  N   . ASP C 1 35  ? 25.102  -11.318 -46.482 1.00 21.71 ? 35  ASP C N   1 
ATOM   4617 C  CA  . ASP C 1 35  ? 24.649  -10.864 -47.794 1.00 25.25 ? 35  ASP C CA  1 
ATOM   4618 C  C   . ASP C 1 35  ? 25.552  -9.778  -48.361 1.00 20.32 ? 35  ASP C C   1 
ATOM   4619 O  O   . ASP C 1 35  ? 25.485  -9.428  -49.542 1.00 22.96 ? 35  ASP C O   1 
ATOM   4620 C  CB  . ASP C 1 35  ? 23.172  -10.445 -47.783 1.00 31.02 ? 35  ASP C CB  1 
ATOM   4621 C  CG  . ASP C 1 35  ? 22.220  -11.624 -47.591 1.00 45.16 ? 35  ASP C CG  1 
ATOM   4622 O  OD1 . ASP C 1 35  ? 22.596  -12.759 -47.975 1.00 46.79 ? 35  ASP C OD1 1 
ATOM   4623 O  OD2 . ASP C 1 35  ? 21.111  -11.409 -47.033 1.00 54.80 ? 35  ASP C OD2 1 
ATOM   4624 N  N   . ILE C 1 36  ? 26.428  -9.219  -47.517 1.00 17.09 ? 36  ILE C N   1 
ATOM   4625 C  CA  . ILE C 1 36  ? 27.282  -8.136  -47.991 1.00 16.05 ? 36  ILE C CA  1 
ATOM   4626 C  C   . ILE C 1 36  ? 28.746  -8.556  -47.948 1.00 15.64 ? 36  ILE C C   1 
ATOM   4627 O  O   . ILE C 1 36  ? 29.609  -7.739  -48.231 1.00 16.18 ? 36  ILE C O   1 
ATOM   4628 C  CB  . ILE C 1 36  ? 27.085  -6.800  -47.237 1.00 14.93 ? 36  ILE C CB  1 
ATOM   4629 C  CG1 . ILE C 1 36  ? 27.340  -6.998  -45.737 1.00 16.89 ? 36  ILE C CG1 1 
ATOM   4630 C  CG2 . ILE C 1 36  ? 25.697  -6.212  -47.526 1.00 18.15 ? 36  ILE C CG2 1 
ATOM   4631 C  CD1 . ILE C 1 36  ? 27.520  -5.711  -44.936 1.00 17.70 ? 36  ILE C CD1 1 
ATOM   4632 N  N   . LEU C 1 37  ? 29.025  -9.803  -47.624 1.00 15.62 ? 37  LEU C N   1 
ATOM   4633 C  CA  . LEU C 1 37  ? 30.406  -10.285 -47.617 1.00 15.00 ? 37  LEU C CA  1 
ATOM   4634 C  C   . LEU C 1 37  ? 30.881  -10.775 -48.977 1.00 16.65 ? 37  LEU C C   1 
ATOM   4635 O  O   . LEU C 1 37  ? 30.118  -11.428 -49.731 1.00 20.00 ? 37  LEU C O   1 
ATOM   4636 C  CB  . LEU C 1 37  ? 30.521  -11.454 -46.644 1.00 17.21 ? 37  LEU C CB  1 
ATOM   4637 C  CG  . LEU C 1 37  ? 30.092  -11.202 -45.212 1.00 15.70 ? 37  LEU C CG  1 
ATOM   4638 C  CD1 . LEU C 1 37  ? 30.442  -12.435 -44.390 1.00 18.58 ? 37  LEU C CD1 1 
ATOM   4639 C  CD2 . LEU C 1 37  ? 30.781  -9.951  -44.657 1.00 18.12 ? 37  LEU C CD2 1 
ATOM   4640 N  N   . GLN C 1 38  ? 32.139  -10.515 -49.319 1.00 14.72 ? 38  GLN C N   1 
ATOM   4641 C  CA  . GLN C 1 38  ? 32.718  -11.083 -50.543 1.00 16.01 ? 38  GLN C CA  1 
ATOM   4642 C  C   . GLN C 1 38  ? 34.161  -11.500 -50.279 1.00 15.28 ? 38  GLN C C   1 
ATOM   4643 O  O   . GLN C 1 38  ? 34.950  -10.670 -49.833 1.00 13.80 ? 38  GLN C O   1 
ATOM   4644 C  CB  . GLN C 1 38  ? 32.622  -10.064 -51.695 1.00 16.47 ? 38  GLN C CB  1 
ATOM   4645 C  CG  . GLN C 1 38  ? 33.033  -10.628 -53.072 1.00 19.74 ? 38  GLN C CG  1 
ATOM   4646 C  CD  . GLN C 1 38  ? 32.763  -9.650  -54.192 1.00 22.98 ? 38  GLN C CD  1 
ATOM   4647 O  OE1 . GLN C 1 38  ? 31.626  -9.525  -54.663 1.00 32.84 ? 38  GLN C OE1 1 
ATOM   4648 N  NE2 . GLN C 1 38  ? 33.783  -8.927  -54.577 1.00 24.68 ? 38  GLN C NE2 1 
ATOM   4649 N  N   . TYR C 1 39  ? 34.514  -12.756 -50.596 1.00 15.25 ? 39  TYR C N   1 
ATOM   4650 C  CA  . TYR C 1 39  ? 35.898  -13.170 -50.498 1.00 14.00 ? 39  TYR C CA  1 
ATOM   4651 C  C   . TYR C 1 39  ? 36.755  -12.365 -51.454 1.00 15.00 ? 39  TYR C C   1 
ATOM   4652 O  O   . TYR C 1 39  ? 36.363  -12.104 -52.607 1.00 16.91 ? 39  TYR C O   1 
ATOM   4653 C  CB  . TYR C 1 39  ? 35.956  -14.670 -50.856 1.00 16.50 ? 39  TYR C CB  1 
ATOM   4654 C  CG  . TYR C 1 39  ? 37.381  -15.129 -51.011 1.00 18.99 ? 39  TYR C CG  1 
ATOM   4655 C  CD1 . TYR C 1 39  ? 38.199  -15.262 -49.898 1.00 21.69 ? 39  TYR C CD1 1 
ATOM   4656 C  CD2 . TYR C 1 39  ? 37.898  -15.458 -52.258 1.00 18.93 ? 39  TYR C CD2 1 
ATOM   4657 C  CE1 . TYR C 1 39  ? 39.527  -15.658 -50.034 1.00 22.80 ? 39  TYR C CE1 1 
ATOM   4658 C  CE2 . TYR C 1 39  ? 39.219  -15.861 -52.406 1.00 24.28 ? 39  TYR C CE2 1 
ATOM   4659 C  CZ  . TYR C 1 39  ? 40.027  -15.988 -51.289 1.00 24.01 ? 39  TYR C CZ  1 
ATOM   4660 O  OH  . TYR C 1 39  ? 41.341  -16.362 -51.513 1.00 24.57 ? 39  TYR C OH  1 
ATOM   4661 N  N   . ASP C 1 40  ? 37.956  -11.977 -50.986 1.00 14.75 ? 40  ASP C N   1 
ATOM   4662 C  CA  . ASP C 1 40  ? 38.887  -11.185 -51.770 1.00 15.94 ? 40  ASP C CA  1 
ATOM   4663 C  C   . ASP C 1 40  ? 40.286  -11.778 -51.562 1.00 16.05 ? 40  ASP C C   1 
ATOM   4664 O  O   . ASP C 1 40  ? 40.853  -11.715 -50.465 1.00 16.61 ? 40  ASP C O   1 
ATOM   4665 C  CB  . ASP C 1 40  ? 38.776  -9.729  -51.317 1.00 16.49 ? 40  ASP C CB  1 
ATOM   4666 C  CG  . ASP C 1 40  ? 39.745  -8.751  -51.937 1.00 21.28 ? 40  ASP C CG  1 
ATOM   4667 O  OD1 . ASP C 1 40  ? 40.630  -9.180  -52.653 1.00 19.34 ? 40  ASP C OD1 1 
ATOM   4668 O  OD2 . ASP C 1 40  ? 39.629  -7.542  -51.617 1.00 24.75 ? 40  ASP C OD2 1 
ATOM   4669 N  N   . ALA C 1 41  ? 40.876  -12.296 -52.662 1.00 17.11 ? 41  ALA C N   1 
ATOM   4670 C  CA  . ALA C 1 41  ? 42.147  -13.031 -52.612 1.00 17.37 ? 41  ALA C CA  1 
ATOM   4671 C  C   . ALA C 1 41  ? 43.298  -12.114 -52.230 1.00 16.94 ? 41  ALA C C   1 
ATOM   4672 O  O   . ALA C 1 41  ? 44.405  -12.549 -51.873 1.00 18.06 ? 41  ALA C O   1 
ATOM   4673 C  CB  . ALA C 1 41  ? 42.399  -13.569 -54.015 1.00 19.39 ? 41  ALA C CB  1 
ATOM   4674 N  N   . SER C 1 42  ? 43.101  -10.799 -52.370 1.00 17.40 ? 42  SER C N   1 
ATOM   4675 C  CA  . SER C 1 42  ? 44.124  -9.832  -52.028 1.00 16.28 ? 42  SER C CA  1 
ATOM   4676 C  C   . SER C 1 42  ? 44.415  -9.767  -50.521 1.00 16.73 ? 42  SER C C   1 
ATOM   4677 O  O   . SER C 1 42  ? 45.433  -9.183  -50.129 1.00 17.65 ? 42  SER C O   1 
ATOM   4678 C  CB  . SER C 1 42  ? 43.822  -8.443  -52.554 1.00 19.34 ? 42  SER C CB  1 
ATOM   4679 O  OG  . SER C 1 42  ? 42.913  -7.743  -51.698 1.00 18.90 ? 42  SER C OG  1 
ATOM   4680 N  N   . LEU C 1 43  ? 43.476  -10.305 -49.716 1.00 15.03 ? 43  LEU C N   1 
ATOM   4681 C  CA  . LEU C 1 43  ? 43.518  -10.123 -48.259 1.00 15.28 ? 43  LEU C CA  1 
ATOM   4682 C  C   . LEU C 1 43  ? 44.381  -11.195 -47.605 1.00 15.58 ? 43  LEU C C   1 
ATOM   4683 O  O   . LEU C 1 43  ? 43.904  -12.131 -46.945 1.00 15.75 ? 43  LEU C O   1 
ATOM   4684 C  CB  . LEU C 1 43  ? 42.090  -10.123 -47.705 1.00 14.54 ? 43  LEU C CB  1 
ATOM   4685 C  CG  . LEU C 1 43  ? 41.244  -8.967  -48.197 1.00 13.05 ? 43  LEU C CG  1 
ATOM   4686 C  CD1 . LEU C 1 43  ? 39.872  -9.002  -47.516 1.00 14.06 ? 43  LEU C CD1 1 
ATOM   4687 C  CD2 . LEU C 1 43  ? 41.897  -7.625  -48.028 1.00 14.20 ? 43  LEU C CD2 1 
ATOM   4688 N  N   . THR C 1 44  ? 45.680  -10.973 -47.765 1.00 17.11 ? 44  THR C N   1 
ATOM   4689 C  CA  . THR C 1 44  ? 46.719  -11.846 -47.245 1.00 18.19 ? 44  THR C CA  1 
ATOM   4690 C  C   . THR C 1 44  ? 46.921  -11.594 -45.750 1.00 19.59 ? 44  THR C C   1 
ATOM   4691 O  O   . THR C 1 44  ? 46.482  -10.580 -45.212 1.00 16.94 ? 44  THR C O   1 
ATOM   4692 C  CB  . THR C 1 44  ? 47.991  -11.662 -48.086 1.00 18.32 ? 44  THR C CB  1 
ATOM   4693 O  OG1 . THR C 1 44  ? 48.306  -10.271 -48.140 1.00 20.54 ? 44  THR C OG1 1 
ATOM   4694 C  CG2 . THR C 1 44  ? 47.837  -12.231 -49.482 1.00 22.09 ? 44  THR C CG2 1 
ATOM   4695 N  N   . PRO C 1 45  ? 47.621  -12.477 -44.999 1.00 18.51 ? 45  PRO C N   1 
ATOM   4696 C  CA  . PRO C 1 45  ? 47.827  -12.235 -43.565 1.00 18.67 ? 45  PRO C CA  1 
ATOM   4697 C  C   . PRO C 1 45  ? 48.650  -10.986 -43.269 1.00 20.18 ? 45  PRO C C   1 
ATOM   4698 O  O   . PRO C 1 45  ? 49.647  -10.685 -43.929 1.00 23.28 ? 45  PRO C O   1 
ATOM   4699 C  CB  . PRO C 1 45  ? 48.559  -13.513 -43.118 1.00 20.20 ? 45  PRO C CB  1 
ATOM   4700 C  CG  . PRO C 1 45  ? 48.196  -14.558 -44.168 1.00 20.52 ? 45  PRO C CG  1 
ATOM   4701 C  CD  . PRO C 1 45  ? 48.159  -13.773 -45.461 1.00 20.32 ? 45  PRO C CD  1 
ATOM   4702 N  N   . LEU C 1 46  ? 48.229  -10.210 -42.268 1.00 16.74 ? 46  LEU C N   1 
ATOM   4703 C  CA  . LEU C 1 46  ? 49.020  -9.082  -41.810 1.00 17.67 ? 46  LEU C CA  1 
ATOM   4704 C  C   . LEU C 1 46  ? 50.137  -9.621  -40.915 1.00 16.91 ? 46  LEU C C   1 
ATOM   4705 O  O   . LEU C 1 46  ? 49.955  -10.668 -40.305 1.00 19.69 ? 46  LEU C O   1 
ATOM   4706 C  CB  . LEU C 1 46  ? 48.110  -8.156  -41.002 1.00 17.59 ? 46  LEU C CB  1 
ATOM   4707 C  CG  . LEU C 1 46  ? 46.984  -7.484  -41.782 1.00 17.38 ? 46  LEU C CG  1 
ATOM   4708 C  CD1 . LEU C 1 46  ? 46.165  -6.581  -40.876 1.00 20.82 ? 46  LEU C CD1 1 
ATOM   4709 C  CD2 . LEU C 1 46  ? 47.525  -6.700  -42.972 1.00 21.54 ? 46  LEU C CD2 1 
ATOM   4710 N  N   . GLU C 1 47  ? 51.214  -8.849  -40.810 1.00 17.60 ? 47  GLU C N   1 
ATOM   4711 C  CA  . GLU C 1 47  ? 52.238  -9.153  -39.816 1.00 18.48 ? 47  GLU C CA  1 
ATOM   4712 C  C   . GLU C 1 47  ? 52.279  -8.040  -38.779 1.00 17.79 ? 47  GLU C C   1 
ATOM   4713 O  O   . GLU C 1 47  ? 52.249  -6.862  -39.136 1.00 19.70 ? 47  GLU C O   1 
ATOM   4714 C  CB  . GLU C 1 47  ? 53.594  -9.265  -40.516 1.00 23.61 ? 47  GLU C CB  1 
ATOM   4715 C  CG  . GLU C 1 47  ? 53.594  -10.323 -41.609 1.00 31.41 ? 47  GLU C CG  1 
ATOM   4716 C  CD  . GLU C 1 47  ? 53.521  -11.760 -41.102 1.00 40.92 ? 47  GLU C CD  1 
ATOM   4717 O  OE1 . GLU C 1 47  ? 54.180  -12.062 -40.061 1.00 52.70 ? 47  GLU C OE1 1 
ATOM   4718 O  OE2 . GLU C 1 47  ? 52.796  -12.584 -41.727 1.00 47.64 ? 47  GLU C OE2 1 
ATOM   4719 N  N   . PHE C 1 48  ? 52.444  -8.401  -37.504 1.00 15.38 ? 48  PHE C N   1 
ATOM   4720 C  CA  . PHE C 1 48  ? 52.449  -7.456  -36.402 1.00 17.65 ? 48  PHE C CA  1 
ATOM   4721 C  C   . PHE C 1 48  ? 53.876  -7.338  -35.902 1.00 17.13 ? 48  PHE C C   1 
ATOM   4722 O  O   . PHE C 1 48  ? 54.358  -8.281  -35.273 1.00 22.03 ? 48  PHE C O   1 
ATOM   4723 C  CB  . PHE C 1 48  ? 51.442  -7.882  -35.319 1.00 17.84 ? 48  PHE C CB  1 
ATOM   4724 C  CG  . PHE C 1 48  ? 50.112  -8.287  -35.932 1.00 17.89 ? 48  PHE C CG  1 
ATOM   4725 C  CD1 . PHE C 1 48  ? 49.296  -7.332  -36.526 1.00 19.48 ? 48  PHE C CD1 1 
ATOM   4726 C  CD2 . PHE C 1 48  ? 49.742  -9.619  -36.011 1.00 18.40 ? 48  PHE C CD2 1 
ATOM   4727 C  CE1 . PHE C 1 48  ? 48.103  -7.695  -37.141 1.00 18.78 ? 48  PHE C CE1 1 
ATOM   4728 C  CE2 . PHE C 1 48  ? 48.553  -9.979  -36.624 1.00 19.24 ? 48  PHE C CE2 1 
ATOM   4729 C  CZ  . PHE C 1 48  ? 47.752  -9.018  -37.198 1.00 17.65 ? 48  PHE C CZ  1 
ATOM   4730 N  N   . GLN C 1 49  ? 54.458  -6.172  -36.126 1.00 16.19 ? 49  GLN C N   1 
ATOM   4731 C  CA  . GLN C 1 49  ? 55.891  -5.990  -35.878 1.00 19.07 ? 49  GLN C CA  1 
ATOM   4732 C  C   . GLN C 1 49  ? 56.083  -5.062  -34.702 1.00 19.15 ? 49  GLN C C   1 
ATOM   4733 O  O   . GLN C 1 49  ? 55.476  -4.004  -34.615 1.00 17.96 ? 49  GLN C O   1 
ATOM   4734 C  CB  . GLN C 1 49  ? 56.553  -5.451  -37.148 1.00 22.29 ? 49  GLN C CB  1 
ATOM   4735 C  CG  . GLN C 1 49  ? 56.567  -6.504  -38.241 1.00 27.00 ? 49  GLN C CG  1 
ATOM   4736 C  CD  . GLN C 1 49  ? 57.470  -6.209  -39.419 1.00 37.60 ? 49  GLN C CD  1 
ATOM   4737 O  OE1 . GLN C 1 49  ? 57.786  -5.056  -39.724 1.00 43.78 ? 49  GLN C OE1 1 
ATOM   4738 N  NE2 . GLN C 1 49  ? 57.896  -7.264  -40.101 1.00 38.22 ? 49  GLN C NE2 1 
ATOM   4739 N  N   . GLY C 1 50  ? 57.029  -5.441  -33.815 1.00 17.61 ? 50  GLY C N   1 
ATOM   4740 C  CA  . GLY C 1 50  ? 57.343  -4.563  -32.713 1.00 20.54 ? 50  GLY C CA  1 
ATOM   4741 C  C   . GLY C 1 50  ? 56.273  -4.580  -31.631 1.00 17.00 ? 50  GLY C C   1 
ATOM   4742 O  O   . GLY C 1 50  ? 56.281  -3.696  -30.790 1.00 18.86 ? 50  GLY C O   1 
ATOM   4743 N  N   . TYR C 1 51  ? 55.367  -5.560  -31.657 1.00 18.18 ? 51  TYR C N   1 
ATOM   4744 C  CA  . TYR C 1 51  ? 54.270  -5.593  -30.695 1.00 18.00 ? 51  TYR C CA  1 
ATOM   4745 C  C   . TYR C 1 51  ? 54.699  -6.098  -29.319 1.00 17.21 ? 51  TYR C C   1 
ATOM   4746 O  O   . TYR C 1 51  ? 53.991  -5.929  -28.353 1.00 16.88 ? 51  TYR C O   1 
ATOM   4747 C  CB  . TYR C 1 51  ? 53.099  -6.466  -31.164 1.00 15.68 ? 51  TYR C CB  1 
ATOM   4748 C  CG  . TYR C 1 51  ? 52.113  -5.797  -32.098 1.00 15.26 ? 51  TYR C CG  1 
ATOM   4749 C  CD1 . TYR C 1 51  ? 52.493  -4.956  -33.142 1.00 15.01 ? 51  TYR C CD1 1 
ATOM   4750 C  CD2 . TYR C 1 51  ? 50.760  -6.047  -31.908 1.00 13.62 ? 51  TYR C CD2 1 
ATOM   4751 C  CE1 . TYR C 1 51  ? 51.558  -4.332  -33.974 1.00 15.84 ? 51  TYR C CE1 1 
ATOM   4752 C  CE2 . TYR C 1 51  ? 49.815  -5.433  -32.735 1.00 16.34 ? 51  TYR C CE2 1 
ATOM   4753 C  CZ  . TYR C 1 51  ? 50.216  -4.598  -33.763 1.00 16.03 ? 51  TYR C CZ  1 
ATOM   4754 O  OH  . TYR C 1 51  ? 49.241  -3.984  -34.526 1.00 17.01 ? 51  TYR C OH  1 
ATOM   4755 N  N   . ASN C 1 52  ? 55.880  -6.739  -29.235 1.00 18.85 ? 52  ASN C N   1 
ATOM   4756 C  CA  . ASN C 1 52  ? 56.339  -7.311  -27.974 1.00 21.17 ? 52  ASN C CA  1 
ATOM   4757 C  C   . ASN C 1 52  ? 57.054  -6.227  -27.170 1.00 22.79 ? 52  ASN C C   1 
ATOM   4758 O  O   . ASN C 1 52  ? 58.273  -6.080  -27.295 1.00 26.75 ? 52  ASN C O   1 
ATOM   4759 C  CB  . ASN C 1 52  ? 57.261  -8.491  -28.288 1.00 22.32 ? 52  ASN C CB  1 
ATOM   4760 C  CG  . ASN C 1 52  ? 57.593  -9.262  -27.032 1.00 25.62 ? 52  ASN C CG  1 
ATOM   4761 O  OD1 . ASN C 1 52  ? 56.841  -9.244  -26.054 1.00 25.48 ? 52  ASN C OD1 1 
ATOM   4762 N  ND2 . ASN C 1 52  ? 58.773  -9.872  -27.028 1.00 31.15 ? 52  ASN C ND2 1 
ATOM   4763 N  N   . LEU C 1 53  ? 56.291  -5.474  -26.368 1.00 20.63 ? 53  LEU C N   1 
ATOM   4764 C  CA  . LEU C 1 53  ? 56.863  -4.353  -25.618 1.00 22.62 ? 53  LEU C CA  1 
ATOM   4765 C  C   . LEU C 1 53  ? 57.508  -4.878  -24.319 1.00 22.91 ? 53  LEU C C   1 
ATOM   4766 O  O   . LEU C 1 53  ? 56.950  -5.738  -23.634 1.00 23.83 ? 53  LEU C O   1 
ATOM   4767 C  CB  . LEU C 1 53  ? 55.804  -3.266  -25.367 1.00 21.08 ? 53  LEU C CB  1 
ATOM   4768 C  CG  . LEU C 1 53  ? 54.879  -2.872  -26.529 1.00 19.31 ? 53  LEU C CG  1 
ATOM   4769 C  CD1 . LEU C 1 53  ? 53.805  -1.919  -26.029 1.00 18.43 ? 53  LEU C CD1 1 
ATOM   4770 C  CD2 . LEU C 1 53  ? 55.662  -2.252  -27.674 1.00 22.74 ? 53  LEU C CD2 1 
ATOM   4771 N  N   A SER C 1 54  ? 58.702  -4.370  -23.987 0.50 26.15 ? 54  SER C N   1 
ATOM   4772 N  N   B SER C 1 54  ? 58.666  -4.304  -23.976 0.50 23.97 ? 54  SER C N   1 
ATOM   4773 C  CA  A SER C 1 54  ? 59.426  -4.887  -22.831 0.50 27.12 ? 54  SER C CA  1 
ATOM   4774 C  CA  B SER C 1 54  ? 59.413  -4.696  -22.792 0.50 23.89 ? 54  SER C CA  1 
ATOM   4775 C  C   A SER C 1 54  ? 58.775  -4.442  -21.524 0.50 28.06 ? 54  SER C C   1 
ATOM   4776 C  C   B SER C 1 54  ? 58.619  -4.445  -21.509 0.50 24.64 ? 54  SER C C   1 
ATOM   4777 O  O   A SER C 1 54  ? 58.415  -3.273  -21.379 0.50 28.26 ? 54  SER C O   1 
ATOM   4778 O  O   B SER C 1 54  ? 57.973  -3.416  -21.340 0.50 21.22 ? 54  SER C O   1 
ATOM   4779 C  CB  A SER C 1 54  ? 60.863  -4.474  -22.866 0.50 29.06 ? 54  SER C CB  1 
ATOM   4780 C  CB  B SER C 1 54  ? 60.728  -3.980  -22.778 0.50 23.59 ? 54  SER C CB  1 
ATOM   4781 O  OG  A SER C 1 54  ? 61.503  -4.850  -21.657 0.50 30.24 ? 54  SER C OG  1 
ATOM   4782 O  OG  B SER C 1 54  ? 61.549  -4.430  -23.855 0.50 24.74 ? 54  SER C OG  1 
ATOM   4783 N  N   . ALA C 1 55  ? 58.720  -5.379  -20.558 1.00 27.43 ? 55  ALA C N   1 
ATOM   4784 C  CA  . ALA C 1 55  ? 58.038  -5.242  -19.267 1.00 27.82 ? 55  ALA C CA  1 
ATOM   4785 C  C   . ALA C 1 55  ? 58.665  -4.126  -18.438 1.00 30.64 ? 55  ALA C C   1 
ATOM   4786 O  O   . ALA C 1 55  ? 57.998  -3.544  -17.564 1.00 29.28 ? 55  ALA C O   1 
ATOM   4787 C  CB  . ALA C 1 55  ? 58.076  -6.548  -18.504 1.00 28.66 ? 55  ALA C CB  1 
ATOM   4788 N  N   . ASN C 1 56  ? 59.918  -3.787  -18.766 1.00 27.66 ? 56  ASN C N   1 
ATOM   4789 C  CA  . ASN C 1 56  ? 60.586  -2.783  -17.952 1.00 29.94 ? 56  ASN C CA  1 
ATOM   4790 C  C   . ASN C 1 56  ? 60.393  -1.412  -18.605 1.00 28.88 ? 56  ASN C C   1 
ATOM   4791 O  O   . ASN C 1 56  ? 60.844  -0.390  -18.075 1.00 28.45 ? 56  ASN C O   1 
ATOM   4792 C  CB  . ASN C 1 56  ? 61.991  -3.245  -17.553 1.00 33.34 ? 56  ASN C CB  1 
ATOM   4793 C  CG  . ASN C 1 56  ? 62.980  -3.074  -18.684 1.00 36.60 ? 56  ASN C CG  1 
ATOM   4794 O  OD1 . ASN C 1 56  ? 62.590  -2.765  -19.809 1.00 34.58 ? 56  ASN C OD1 1 
ATOM   4795 N  ND2 . ASN C 1 56  ? 64.254  -3.230  -18.386 1.00 33.56 ? 56  ASN C ND2 1 
ATOM   4796 N  N   . LYS C 1 57  ? 59.648  -1.381  -19.732 1.00 25.06 ? 57  LYS C N   1 
ATOM   4797 C  CA  . LYS C 1 57  ? 59.220  -0.117  -20.317 1.00 26.58 ? 57  LYS C CA  1 
ATOM   4798 C  C   . LYS C 1 57  ? 57.794  0.156   -19.861 1.00 19.84 ? 57  LYS C C   1 
ATOM   4799 O  O   . LYS C 1 57  ? 57.153  -0.706  -19.249 1.00 22.88 ? 57  LYS C O   1 
ATOM   4800 C  CB  . LYS C 1 57  ? 59.192  -0.167  -21.844 1.00 27.31 ? 57  LYS C CB  1 
ATOM   4801 C  CG  . LYS C 1 57  ? 60.562  -0.244  -22.496 1.00 29.40 ? 57  LYS C CG  1 
ATOM   4802 C  CD  . LYS C 1 57  ? 60.460  0.121   -23.963 1.00 31.91 ? 57  LYS C CD  1 
ATOM   4803 C  CE  . LYS C 1 57  ? 60.421  1.618   -24.197 0.01 30.88 ? 57  LYS C CE  1 
ATOM   4804 N  NZ  . LYS C 1 57  ? 60.189  1.947   -25.623 0.01 30.98 ? 57  LYS C NZ  1 
ATOM   4805 N  N   . GLN C 1 58  ? 57.357  1.420   -20.011 1.00 22.03 ? 58  GLN C N   1 
ATOM   4806 C  CA  . GLN C 1 58  ? 56.012  1.751   -19.572 1.00 22.14 ? 58  GLN C CA  1 
ATOM   4807 C  C   . GLN C 1 58  ? 55.306  2.652   -20.588 1.00 17.59 ? 58  GLN C C   1 
ATOM   4808 O  O   . GLN C 1 58  ? 55.911  3.434   -21.330 1.00 19.11 ? 58  GLN C O   1 
ATOM   4809 C  CB  . GLN C 1 58  ? 56.014  2.290   -18.125 1.00 20.01 ? 58  GLN C CB  1 
ATOM   4810 C  CG  . GLN C 1 58  ? 56.472  3.738   -18.018 1.00 20.92 ? 58  GLN C CG  1 
ATOM   4811 C  CD  . GLN C 1 58  ? 56.425  4.238   -16.584 1.00 21.16 ? 58  GLN C CD  1 
ATOM   4812 O  OE1 . GLN C 1 58  ? 56.024  3.524   -15.651 1.00 24.42 ? 58  GLN C OE1 1 
ATOM   4813 N  NE2 . GLN C 1 58  ? 56.743  5.503   -16.409 1.00 20.05 ? 58  GLN C NE2 1 
ATOM   4814 N  N   . PHE C 1 59  ? 53.967  2.543   -20.536 1.00 18.16 ? 59  PHE C N   1 
ATOM   4815 C  CA  . PHE C 1 59  ? 53.055  3.120   -21.529 1.00 16.75 ? 59  PHE C CA  1 
ATOM   4816 C  C   . PHE C 1 59  ? 51.912  3.812   -20.798 1.00 15.25 ? 59  PHE C C   1 
ATOM   4817 O  O   . PHE C 1 59  ? 51.345  3.261   -19.833 1.00 16.34 ? 59  PHE C O   1 
ATOM   4818 C  CB  . PHE C 1 59  ? 52.632  1.964   -22.453 1.00 16.58 ? 59  PHE C CB  1 
ATOM   4819 C  CG  . PHE C 1 59  ? 53.841  1.378   -23.117 1.00 16.54 ? 59  PHE C CG  1 
ATOM   4820 C  CD1 . PHE C 1 59  ? 54.394  2.035   -24.204 1.00 16.22 ? 59  PHE C CD1 1 
ATOM   4821 C  CD2 . PHE C 1 59  ? 54.519  0.283   -22.577 1.00 16.83 ? 59  PHE C CD2 1 
ATOM   4822 C  CE1 . PHE C 1 59  ? 55.587  1.586   -24.769 1.00 19.76 ? 59  PHE C CE1 1 
ATOM   4823 C  CE2 . PHE C 1 59  ? 55.727  -0.149  -23.115 1.00 17.99 ? 59  PHE C CE2 1 
ATOM   4824 C  CZ  . PHE C 1 59  ? 56.241  0.490   -24.221 1.00 16.19 ? 59  PHE C CZ  1 
ATOM   4825 N  N   . LEU C 1 60  ? 51.585  5.047   -21.216 1.00 16.73 ? 60  LEU C N   1 
ATOM   4826 C  CA  . LEU C 1 60  ? 50.615  5.863   -20.508 1.00 16.87 ? 60  LEU C CA  1 
ATOM   4827 C  C   . LEU C 1 60  ? 49.189  5.361   -20.765 1.00 15.98 ? 60  LEU C C   1 
ATOM   4828 O  O   . LEU C 1 60  ? 48.726  5.285   -21.927 1.00 16.36 ? 60  LEU C O   1 
ATOM   4829 C  CB  . LEU C 1 60  ? 50.766  7.296   -20.992 1.00 16.82 ? 60  LEU C CB  1 
ATOM   4830 C  CG  . LEU C 1 60  ? 49.915  8.344   -20.286 1.00 18.64 ? 60  LEU C CG  1 
ATOM   4831 C  CD1 . LEU C 1 60  ? 50.411  8.501   -18.841 1.00 19.12 ? 60  LEU C CD1 1 
ATOM   4832 C  CD2 . LEU C 1 60  ? 50.063  9.653   -21.035 1.00 20.55 ? 60  LEU C CD2 1 
ATOM   4833 N  N   . LEU C 1 61  ? 48.460  5.079   -19.701 1.00 15.85 ? 61  LEU C N   1 
ATOM   4834 C  CA  . LEU C 1 61  ? 47.046  4.773   -19.685 1.00 14.88 ? 61  LEU C CA  1 
ATOM   4835 C  C   . LEU C 1 61  ? 46.285  6.016   -19.244 1.00 16.23 ? 61  LEU C C   1 
ATOM   4836 O  O   . LEU C 1 61  ? 46.600  6.589   -18.198 1.00 17.13 ? 61  LEU C O   1 
ATOM   4837 C  CB  . LEU C 1 61  ? 46.879  3.590   -18.731 1.00 16.76 ? 61  LEU C CB  1 
ATOM   4838 C  CG  . LEU C 1 61  ? 45.501  2.954   -18.689 1.00 18.23 ? 61  LEU C CG  1 
ATOM   4839 C  CD1 . LEU C 1 61  ? 45.336  2.058   -19.920 1.00 19.70 ? 61  LEU C CD1 1 
ATOM   4840 C  CD2 . LEU C 1 61  ? 45.337  2.117   -17.393 1.00 20.23 ? 61  LEU C CD2 1 
ATOM   4841 N  N   . THR C 1 62  ? 45.257  6.417   -19.977 1.00 14.87 ? 62  THR C N   1 
ATOM   4842 C  CA  . THR C 1 62  ? 44.526  7.638   -19.743 1.00 14.82 ? 62  THR C CA  1 
ATOM   4843 C  C   . THR C 1 62  ? 43.041  7.305   -19.775 1.00 16.20 ? 62  THR C C   1 
ATOM   4844 O  O   . THR C 1 62  ? 42.535  6.695   -20.726 1.00 15.93 ? 62  THR C O   1 
ATOM   4845 C  CB  . THR C 1 62  ? 44.738  8.707   -20.820 1.00 17.39 ? 62  THR C CB  1 
ATOM   4846 O  OG1 . THR C 1 62  ? 46.122  9.045   -20.899 1.00 17.95 ? 62  THR C OG1 1 
ATOM   4847 C  CG2 . THR C 1 62  ? 44.000  9.998   -20.544 1.00 18.06 ? 62  THR C CG2 1 
ATOM   4848 N  N   . ASN C 1 63  ? 42.321  7.751   -18.753 1.00 15.68 ? 63  ASN C N   1 
ATOM   4849 C  CA  . ASN C 1 63  ? 40.897  7.962   -18.881 1.00 14.71 ? 63  ASN C CA  1 
ATOM   4850 C  C   . ASN C 1 63  ? 40.636  9.325   -19.477 1.00 16.17 ? 63  ASN C C   1 
ATOM   4851 O  O   . ASN C 1 63  ? 40.852  10.350  -18.840 1.00 17.30 ? 63  ASN C O   1 
ATOM   4852 C  CB  . ASN C 1 63  ? 40.303  7.881   -17.480 1.00 13.93 ? 63  ASN C CB  1 
ATOM   4853 C  CG  . ASN C 1 63  ? 38.801  8.081   -17.419 1.00 15.06 ? 63  ASN C CG  1 
ATOM   4854 O  OD1 . ASN C 1 63  ? 38.210  8.726   -18.278 1.00 14.78 ? 63  ASN C OD1 1 
ATOM   4855 N  ND2 . ASN C 1 63  ? 38.174  7.672   -16.322 1.00 14.02 ? 63  ASN C ND2 1 
ATOM   4856 N  N   . ASN C 1 64  ? 40.169  9.322   -20.742 1.00 16.44 ? 64  ASN C N   1 
ATOM   4857 C  CA  . ASN C 1 64  ? 39.923  10.552  -21.475 1.00 16.35 ? 64  ASN C CA  1 
ATOM   4858 C  C   . ASN C 1 64  ? 38.473  10.983  -21.416 1.00 15.83 ? 64  ASN C C   1 
ATOM   4859 O  O   . ASN C 1 64  ? 38.060  11.898  -22.141 1.00 17.46 ? 64  ASN C O   1 
ATOM   4860 C  CB  . ASN C 1 64  ? 40.447  10.440  -22.901 1.00 15.96 ? 64  ASN C CB  1 
ATOM   4861 C  CG  . ASN C 1 64  ? 39.688  9.449   -23.755 1.00 14.66 ? 64  ASN C CG  1 
ATOM   4862 O  OD1 . ASN C 1 64  ? 38.652  8.900   -23.334 1.00 16.94 ? 64  ASN C OD1 1 
ATOM   4863 N  ND2 . ASN C 1 64  ? 40.297  9.091   -24.873 1.00 19.39 ? 64  ASN C ND2 1 
ATOM   4864 N  N   . GLY C 1 65  ? 37.685  10.360  -20.526 1.00 14.20 ? 65  GLY C N   1 
ATOM   4865 C  CA  . GLY C 1 65  ? 36.275  10.676  -20.438 1.00 16.87 ? 65  GLY C CA  1 
ATOM   4866 C  C   . GLY C 1 65  ? 35.407  9.966   -21.484 1.00 16.97 ? 65  GLY C C   1 
ATOM   4867 O  O   . GLY C 1 65  ? 34.191  10.046  -21.369 1.00 19.72 ? 65  GLY C O   1 
ATOM   4868 N  N   . HIS C 1 66  ? 36.030  9.237   -22.418 1.00 15.35 ? 66  HIS C N   1 
ATOM   4869 C  CA  . HIS C 1 66  ? 35.256  8.575   -23.473 1.00 15.59 ? 66  HIS C CA  1 
ATOM   4870 C  C   . HIS C 1 66  ? 35.559  7.091   -23.454 1.00 15.36 ? 66  HIS C C   1 
ATOM   4871 O  O   . HIS C 1 66  ? 34.723  6.275   -23.858 1.00 18.46 ? 66  HIS C O   1 
ATOM   4872 C  CB  . HIS C 1 66  ? 35.651  9.116   -24.838 1.00 14.66 ? 66  HIS C CB  1 
ATOM   4873 C  CG  . HIS C 1 66  ? 35.325  10.570  -24.919 1.00 16.26 ? 66  HIS C CG  1 
ATOM   4874 N  ND1 . HIS C 1 66  ? 36.321  11.523  -25.118 1.00 19.02 ? 66  HIS C ND1 1 
ATOM   4875 C  CD2 . HIS C 1 66  ? 34.164  11.228  -24.822 1.00 15.25 ? 66  HIS C CD2 1 
ATOM   4876 C  CE1 . HIS C 1 66  ? 35.753  12.727  -25.155 1.00 15.26 ? 66  HIS C CE1 1 
ATOM   4877 N  NE2 . HIS C 1 66  ? 34.420  12.569  -24.984 1.00 19.17 ? 66  HIS C NE2 1 
ATOM   4878 N  N   . SER C 1 67  ? 36.752  6.720   -23.004 1.00 14.68 ? 67  SER C N   1 
ATOM   4879 C  CA  . SER C 1 67  ? 37.242  5.364   -22.964 1.00 13.21 ? 67  SER C CA  1 
ATOM   4880 C  C   . SER C 1 67  ? 38.452  5.355   -22.034 1.00 14.85 ? 67  SER C C   1 
ATOM   4881 O  O   . SER C 1 67  ? 38.766  6.399   -21.449 1.00 15.52 ? 67  SER C O   1 
ATOM   4882 C  CB  . SER C 1 67  ? 37.604  4.868   -24.392 1.00 14.89 ? 67  SER C CB  1 
ATOM   4883 O  OG  . SER C 1 67  ? 38.059  3.532   -24.406 1.00 16.31 ? 67  SER C OG  1 
ATOM   4884 N  N   . VAL C 1 68  ? 39.090  4.198   -21.988 1.00 13.75 ? 68  VAL C N   1 
ATOM   4885 C  CA  . VAL C 1 68  ? 40.435  4.105   -21.456 1.00 13.86 ? 68  VAL C CA  1 
ATOM   4886 C  C   . VAL C 1 68  ? 41.345  3.779   -22.618 1.00 16.19 ? 68  VAL C C   1 
ATOM   4887 O  O   . VAL C 1 68  ? 41.076  2.842   -23.380 1.00 14.14 ? 68  VAL C O   1 
ATOM   4888 C  CB  . VAL C 1 68  ? 40.477  3.126   -20.273 1.00 15.51 ? 68  VAL C CB  1 
ATOM   4889 C  CG1 . VAL C 1 68  ? 40.247  1.691   -20.677 1.00 16.38 ? 68  VAL C CG1 1 
ATOM   4890 C  CG2 . VAL C 1 68  ? 41.826  3.264   -19.585 1.00 16.66 ? 68  VAL C CG2 1 
ATOM   4891 N  N   . LYS C 1 69  ? 42.440  4.531   -22.711 1.00 15.34 ? 69  LYS C N   1 
ATOM   4892 C  CA  . LYS C 1 69  ? 43.351  4.482   -23.855 1.00 15.19 ? 69  LYS C CA  1 
ATOM   4893 C  C   . LYS C 1 69  ? 44.752  4.215   -23.322 1.00 16.85 ? 69  LYS C C   1 
ATOM   4894 O  O   . LYS C 1 69  ? 45.142  4.714   -22.255 1.00 17.37 ? 69  LYS C O   1 
ATOM   4895 C  CB  . LYS C 1 69  ? 43.279  5.855   -24.523 1.00 19.79 ? 69  LYS C CB  1 
ATOM   4896 C  CG  . LYS C 1 69  ? 44.251  6.155   -25.644 1.00 23.89 ? 69  LYS C CG  1 
ATOM   4897 C  CD  . LYS C 1 69  ? 44.128  7.607   -26.096 1.00 27.40 ? 69  LYS C CD  1 
ATOM   4898 C  CE  . LYS C 1 69  ? 44.489  8.710   -25.119 1.00 27.45 ? 69  LYS C CE  1 
ATOM   4899 N  NZ  . LYS C 1 69  ? 44.773  9.998   -25.824 1.00 27.32 ? 69  LYS C NZ  1 
ATOM   4900 N  N   . LEU C 1 70  ? 45.470  3.349   -24.011 1.00 13.80 ? 70  LEU C N   1 
ATOM   4901 C  CA  . LEU C 1 70  ? 46.883  3.104   -23.763 1.00 13.36 ? 70  LEU C CA  1 
ATOM   4902 C  C   . LEU C 1 70  ? 47.657  3.642   -24.940 1.00 12.94 ? 70  LEU C C   1 
ATOM   4903 O  O   . LEU C 1 70  ? 47.490  3.198   -26.086 1.00 14.26 ? 70  LEU C O   1 
ATOM   4904 C  CB  . LEU C 1 70  ? 47.073  1.602   -23.574 1.00 13.33 ? 70  LEU C CB  1 
ATOM   4905 C  CG  . LEU C 1 70  ? 48.509  1.167   -23.293 1.00 15.22 ? 70  LEU C CG  1 
ATOM   4906 C  CD1 . LEU C 1 70  ? 48.927  1.548   -21.870 1.00 16.59 ? 70  LEU C CD1 1 
ATOM   4907 C  CD2 . LEU C 1 70  ? 48.612  -0.338  -23.480 1.00 16.39 ? 70  LEU C CD2 1 
ATOM   4908 N  N   . ASN C 1 71  ? 48.598  4.580   -24.705 1.00 12.87 ? 71  ASN C N   1 
ATOM   4909 C  CA  . ASN C 1 71  ? 49.472  5.019   -25.784 1.00 13.53 ? 71  ASN C CA  1 
ATOM   4910 C  C   . ASN C 1 71  ? 50.444  3.913   -26.181 1.00 14.39 ? 71  ASN C C   1 
ATOM   4911 O  O   . ASN C 1 71  ? 50.904  3.115   -25.347 1.00 16.56 ? 71  ASN C O   1 
ATOM   4912 C  CB  . ASN C 1 71  ? 50.252  6.277   -25.376 1.00 14.75 ? 71  ASN C CB  1 
ATOM   4913 C  CG  . ASN C 1 71  ? 49.351  7.479   -25.218 1.00 18.61 ? 71  ASN C CG  1 
ATOM   4914 O  OD1 . ASN C 1 71  ? 48.144  7.440   -25.481 1.00 19.32 ? 71  ASN C OD1 1 
ATOM   4915 N  ND2 . ASN C 1 71  ? 49.920  8.597   -24.790 1.00 21.29 ? 71  ASN C ND2 1 
ATOM   4916 N  N   . LEU C 1 72  ? 50.748  3.824   -27.487 1.00 12.88 ? 72  LEU C N   1 
ATOM   4917 C  CA  . LEU C 1 72  ? 51.610  2.788   -28.014 1.00 13.59 ? 72  LEU C CA  1 
ATOM   4918 C  C   . LEU C 1 72  ? 52.716  3.425   -28.844 1.00 13.55 ? 72  LEU C C   1 
ATOM   4919 O  O   . LEU C 1 72  ? 52.537  4.533   -29.343 1.00 14.42 ? 72  LEU C O   1 
ATOM   4920 C  CB  . LEU C 1 72  ? 50.806  1.851   -28.934 1.00 13.74 ? 72  LEU C CB  1 
ATOM   4921 C  CG  . LEU C 1 72  ? 49.710  1.057   -28.233 1.00 13.94 ? 72  LEU C CG  1 
ATOM   4922 C  CD1 . LEU C 1 72  ? 48.835  0.398   -29.296 1.00 15.02 ? 72  LEU C CD1 1 
ATOM   4923 C  CD2 . LEU C 1 72  ? 50.284  -0.001  -27.285 1.00 16.41 ? 72  LEU C CD2 1 
ATOM   4924 N  N   . PRO C 1 73  ? 53.924  2.836   -28.898 1.00 16.25 ? 73  PRO C N   1 
ATOM   4925 C  CA  . PRO C 1 73  ? 55.048  3.473   -29.552 1.00 15.14 ? 73  PRO C CA  1 
ATOM   4926 C  C   . PRO C 1 73  ? 55.012  3.259   -31.067 1.00 17.30 ? 73  PRO C C   1 
ATOM   4927 O  O   . PRO C 1 73  ? 54.531  2.220   -31.537 1.00 18.09 ? 73  PRO C O   1 
ATOM   4928 C  CB  . PRO C 1 73  ? 56.236  2.750   -28.855 1.00 16.88 ? 73  PRO C CB  1 
ATOM   4929 C  CG  . PRO C 1 73  ? 55.773  1.298   -28.722 1.00 15.69 ? 73  PRO C CG  1 
ATOM   4930 C  CD  . PRO C 1 73  ? 54.270  1.464   -28.477 1.00 15.86 ? 73  PRO C CD  1 
ATOM   4931 N  N   . SER C 1 74  ? 55.500  4.261   -31.793 1.00 18.86 ? 74  SER C N   1 
ATOM   4932 C  CA  . SER C 1 74  ? 55.436  4.281   -33.244 1.00 19.86 ? 74  SER C CA  1 
ATOM   4933 C  C   . SER C 1 74  ? 56.339  3.239   -33.894 1.00 21.79 ? 74  SER C C   1 
ATOM   4934 O  O   . SER C 1 74  ? 56.269  3.017   -35.104 1.00 22.63 ? 74  SER C O   1 
ATOM   4935 C  CB  . SER C 1 74  ? 55.681  5.662   -33.783 1.00 25.54 ? 74  SER C CB  1 
ATOM   4936 O  OG  . SER C 1 74  ? 56.991  6.097   -33.455 1.00 27.37 ? 74  SER C OG  1 
ATOM   4937 N  N   . ASP C 1 75  ? 57.197  2.563   -33.117 1.00 21.98 ? 75  ASP C N   1 
ATOM   4938 C  CA  . ASP C 1 75  ? 57.982  1.542   -33.786 1.00 22.60 ? 75  ASP C CA  1 
ATOM   4939 C  C   . ASP C 1 75  ? 57.175  0.244   -33.915 1.00 21.41 ? 75  ASP C C   1 
ATOM   4940 O  O   . ASP C 1 75  ? 57.576  -0.701  -34.581 1.00 23.41 ? 75  ASP C O   1 
ATOM   4941 C  CB  . ASP C 1 75  ? 59.383  1.443   -33.179 1.00 29.19 ? 75  ASP C CB  1 
ATOM   4942 C  CG  . ASP C 1 75  ? 59.265  0.965   -31.763 1.00 32.83 ? 75  ASP C CG  1 
ATOM   4943 O  OD1 . ASP C 1 75  ? 59.021  1.822   -30.893 1.00 36.09 ? 75  ASP C OD1 1 
ATOM   4944 O  OD2 . ASP C 1 75  ? 59.356  -0.254  -31.568 1.00 40.50 ? 75  ASP C OD2 1 
ATOM   4945 N  N   . MET C 1 76  ? 55.983  0.179   -33.309 1.00 18.35 ? 76  MET C N   1 
ATOM   4946 C  CA  . MET C 1 76  ? 55.079  -0.934  -33.492 1.00 17.25 ? 76  MET C CA  1 
ATOM   4947 C  C   . MET C 1 76  ? 54.300  -0.706  -34.797 1.00 15.86 ? 76  MET C C   1 
ATOM   4948 O  O   . MET C 1 76  ? 53.861  0.409   -35.041 1.00 17.74 ? 76  MET C O   1 
ATOM   4949 C  CB  . MET C 1 76  ? 54.153  -0.797  -32.288 1.00 20.81 ? 76  MET C CB  1 
ATOM   4950 C  CG  . MET C 1 76  ? 53.212  -1.852  -32.058 1.00 22.69 ? 76  MET C CG  1 
ATOM   4951 S  SD  . MET C 1 76  ? 52.472  -1.633  -30.395 1.00 20.91 ? 76  MET C SD  1 
ATOM   4952 C  CE  . MET C 1 76  ? 50.903  -2.383  -30.832 1.00 17.76 ? 76  MET C CE  1 
ATOM   4953 N  N   . HIS C 1 77  ? 54.250  -1.706  -35.671 1.00 15.63 ? 77  HIS C N   1 
ATOM   4954 C  CA  . HIS C 1 77  ? 53.563  -1.416  -36.943 1.00 16.43 ? 77  HIS C CA  1 
ATOM   4955 C  C   . HIS C 1 77  ? 52.993  -2.676  -37.559 1.00 16.28 ? 77  HIS C C   1 
ATOM   4956 O  O   . HIS C 1 77  ? 53.320  -3.802  -37.199 1.00 16.00 ? 77  HIS C O   1 
ATOM   4957 C  CB  . HIS C 1 77  ? 54.400  -0.588  -37.935 1.00 20.19 ? 77  HIS C CB  1 
ATOM   4958 C  CG  . HIS C 1 77  ? 55.642  -1.303  -38.321 1.00 23.25 ? 77  HIS C CG  1 
ATOM   4959 N  ND1 . HIS C 1 77  ? 56.844  -1.048  -37.711 1.00 25.58 ? 77  HIS C ND1 1 
ATOM   4960 C  CD2 . HIS C 1 77  ? 55.844  -2.278  -39.229 1.00 26.43 ? 77  HIS C CD2 1 
ATOM   4961 C  CE1 . HIS C 1 77  ? 57.759  -1.837  -38.224 1.00 23.43 ? 77  HIS C CE1 1 
ATOM   4962 N  NE2 . HIS C 1 77  ? 57.180  -2.607  -39.178 1.00 27.70 ? 77  HIS C NE2 1 
ATOM   4963 N  N   . ILE C 1 78  ? 52.017  -2.458  -38.462 1.00 16.56 ? 78  ILE C N   1 
ATOM   4964 C  CA  . ILE C 1 78  ? 51.460  -3.512  -39.286 1.00 16.92 ? 78  ILE C CA  1 
ATOM   4965 C  C   . ILE C 1 78  ? 52.266  -3.526  -40.579 1.00 16.70 ? 78  ILE C C   1 
ATOM   4966 O  O   . ILE C 1 78  ? 52.488  -2.472  -41.173 1.00 19.11 ? 78  ILE C O   1 
ATOM   4967 C  CB  . ILE C 1 78  ? 49.973  -3.153  -39.610 1.00 16.00 ? 78  ILE C CB  1 
ATOM   4968 C  CG1 . ILE C 1 78  ? 49.071  -3.065  -38.381 1.00 16.88 ? 78  ILE C CG1 1 
ATOM   4969 C  CG2 . ILE C 1 78  ? 49.403  -4.094  -40.663 1.00 17.51 ? 78  ILE C CG2 1 
ATOM   4970 C  CD1 . ILE C 1 78  ? 47.704  -2.411  -38.695 1.00 15.55 ? 78  ILE C CD1 1 
ATOM   4971 N  N   . GLN C 1 79  ? 52.619  -4.738  -41.017 1.00 18.71 ? 79  GLN C N   1 
ATOM   4972 C  CA  . GLN C 1 79  ? 53.192  -4.975  -42.322 1.00 21.85 ? 79  GLN C CA  1 
ATOM   4973 C  C   . GLN C 1 79  ? 52.166  -5.796  -43.098 1.00 21.33 ? 79  GLN C C   1 
ATOM   4974 O  O   . GLN C 1 79  ? 51.514  -6.692  -42.544 1.00 20.48 ? 79  GLN C O   1 
ATOM   4975 C  CB  . GLN C 1 79  ? 54.506  -5.740  -42.084 1.00 26.74 ? 79  GLN C CB  1 
ATOM   4976 C  CG  . GLN C 1 79  ? 55.045  -6.455  -43.319 1.00 35.83 ? 79  GLN C CG  1 
ATOM   4977 C  CD  . GLN C 1 79  ? 55.763  -5.491  -44.235 1.00 47.53 ? 79  GLN C CD  1 
ATOM   4978 O  OE1 . GLN C 1 79  ? 55.958  -5.755  -45.422 1.00 60.17 ? 79  GLN C OE1 1 
ATOM   4979 N  NE2 . GLN C 1 79  ? 56.167  -4.354  -43.692 1.00 48.47 ? 79  GLN C NE2 1 
ATOM   4980 N  N   . GLY C 1 80  ? 52.037  -5.485  -44.386 1.00 20.76 ? 80  GLY C N   1 
ATOM   4981 C  CA  . GLY C 1 80  ? 51.128  -6.214  -45.258 1.00 21.97 ? 80  GLY C CA  1 
ATOM   4982 C  C   . GLY C 1 80  ? 50.142  -5.320  -46.002 1.00 23.56 ? 80  GLY C C   1 
ATOM   4983 O  O   . GLY C 1 80  ? 49.519  -5.759  -46.967 1.00 26.39 ? 80  GLY C O   1 
ATOM   4984 N  N   . LEU C 1 81  ? 49.957  -4.077  -45.547 1.00 21.56 ? 81  LEU C N   1 
ATOM   4985 C  CA  . LEU C 1 81  ? 49.109  -3.114  -46.246 1.00 22.01 ? 81  LEU C CA  1 
ATOM   4986 C  C   . LEU C 1 81  ? 49.929  -2.357  -47.306 1.00 24.08 ? 81  LEU C C   1 
ATOM   4987 O  O   . LEU C 1 81  ? 51.123  -2.625  -47.444 1.00 30.35 ? 81  LEU C O   1 
ATOM   4988 C  CB  . LEU C 1 81  ? 48.412  -2.195  -45.230 1.00 19.16 ? 81  LEU C CB  1 
ATOM   4989 C  CG  . LEU C 1 81  ? 47.545  -2.930  -44.206 1.00 16.14 ? 81  LEU C CG  1 
ATOM   4990 C  CD1 . LEU C 1 81  ? 47.146  -2.015  -43.039 1.00 18.36 ? 81  LEU C CD1 1 
ATOM   4991 C  CD2 . LEU C 1 81  ? 46.276  -3.475  -44.883 1.00 17.75 ? 81  LEU C CD2 1 
ATOM   4992 N  N   . GLN C 1 82  ? 49.294  -1.405  -48.020 1.00 27.48 ? 82  GLN C N   1 
ATOM   4993 C  CA  . GLN C 1 82  ? 49.924  -0.662  -49.105 1.00 28.75 ? 82  GLN C CA  1 
ATOM   4994 C  C   . GLN C 1 82  ? 50.982  0.307   -48.578 1.00 28.08 ? 82  GLN C C   1 
ATOM   4995 O  O   . GLN C 1 82  ? 51.884  0.652   -49.330 1.00 30.38 ? 82  GLN C O   1 
ATOM   4996 C  CB  . GLN C 1 82  ? 48.883  0.124   -49.918 1.00 30.71 ? 82  GLN C CB  1 
ATOM   4997 C  CG  . GLN C 1 82  ? 48.215  -0.688  -51.031 1.00 39.89 ? 82  GLN C CG  1 
ATOM   4998 C  CD  . GLN C 1 82  ? 49.089  -0.906  -52.245 1.00 45.24 ? 82  GLN C CD  1 
ATOM   4999 O  OE1 . GLN C 1 82  ? 49.575  0.040   -52.874 1.00 47.05 ? 82  GLN C OE1 1 
ATOM   5000 N  NE2 . GLN C 1 82  ? 49.322  -2.171  -52.576 1.00 46.28 ? 82  GLN C NE2 1 
ATOM   5001 N  N   . SER C 1 83  ? 50.809  0.815   -47.340 1.00 20.70 ? 83  SER C N   1 
ATOM   5002 C  CA  . SER C 1 83  ? 51.713  1.706   -46.612 1.00 17.54 ? 83  SER C CA  1 
ATOM   5003 C  C   . SER C 1 83  ? 51.977  1.034   -45.274 1.00 17.12 ? 83  SER C C   1 
ATOM   5004 O  O   . SER C 1 83  ? 51.213  0.174   -44.839 1.00 15.08 ? 83  SER C O   1 
ATOM   5005 C  CB  . SER C 1 83  ? 51.093  3.041   -46.323 1.00 20.95 ? 83  SER C CB  1 
ATOM   5006 O  OG  . SER C 1 83  ? 50.829  3.781   -47.511 1.00 22.16 ? 83  SER C OG  1 
ATOM   5007 N  N   . ARG C 1 84  ? 53.093  1.391   -44.638 1.00 15.18 ? 84  ARG C N   1 
ATOM   5008 C  CA  . ARG C 1 84  ? 53.288  1.048   -43.243 1.00 14.02 ? 84  ARG C CA  1 
ATOM   5009 C  C   . ARG C 1 84  ? 52.312  1.870   -42.406 1.00 13.27 ? 84  ARG C C   1 
ATOM   5010 O  O   . ARG C 1 84  ? 52.201  3.077   -42.547 1.00 15.17 ? 84  ARG C O   1 
ATOM   5011 C  CB  . ARG C 1 84  ? 54.732  1.381   -42.819 1.00 14.35 ? 84  ARG C CB  1 
ATOM   5012 C  CG  . ARG C 1 84  ? 54.930  1.127   -41.330 1.00 16.40 ? 84  ARG C CG  1 
ATOM   5013 C  CD  . ARG C 1 84  ? 56.371  1.280   -40.872 1.00 16.53 ? 84  ARG C CD  1 
ATOM   5014 N  NE  . ARG C 1 84  ? 57.179  0.201   -41.360 1.00 16.29 ? 84  ARG C NE  1 
ATOM   5015 C  CZ  . ARG C 1 84  ? 58.501  0.178   -41.108 1.00 17.82 ? 84  ARG C CZ  1 
ATOM   5016 N  NH1 . ARG C 1 84  ? 59.021  1.148   -40.381 1.00 18.39 ? 84  ARG C NH1 1 
ATOM   5017 N  NH2 . ARG C 1 84  ? 59.233  -0.824  -41.529 1.00 18.48 ? 84  ARG C NH2 1 
ATOM   5018 N  N   . TYR C 1 85  ? 51.669  1.150   -41.464 1.00 13.02 ? 85  TYR C N   1 
ATOM   5019 C  CA  . TYR C 1 85  ? 50.844  1.804   -40.456 1.00 13.08 ? 85  TYR C CA  1 
ATOM   5020 C  C   . TYR C 1 85  ? 51.468  1.586   -39.083 1.00 12.75 ? 85  TYR C C   1 
ATOM   5021 O  O   . TYR C 1 85  ? 51.625  0.421   -38.715 1.00 14.01 ? 85  TYR C O   1 
ATOM   5022 C  CB  . TYR C 1 85  ? 49.398  1.255   -40.547 1.00 13.40 ? 85  TYR C CB  1 
ATOM   5023 C  CG  . TYR C 1 85  ? 48.628  1.816   -41.712 1.00 12.22 ? 85  TYR C CG  1 
ATOM   5024 C  CD1 . TYR C 1 85  ? 48.727  1.209   -42.951 1.00 12.49 ? 85  TYR C CD1 1 
ATOM   5025 C  CD2 . TYR C 1 85  ? 47.854  2.964   -41.579 1.00 11.89 ? 85  TYR C CD2 1 
ATOM   5026 C  CE1 . TYR C 1 85  ? 48.031  1.719   -44.053 1.00 12.81 ? 85  TYR C CE1 1 
ATOM   5027 C  CE2 . TYR C 1 85  ? 47.125  3.460   -42.653 1.00 12.25 ? 85  TYR C CE2 1 
ATOM   5028 C  CZ  . TYR C 1 85  ? 47.251  2.849   -43.893 1.00 13.18 ? 85  TYR C CZ  1 
ATOM   5029 O  OH  . TYR C 1 85  ? 46.529  3.363   -44.960 1.00 16.24 ? 85  TYR C OH  1 
ATOM   5030 N  N   . SER C 1 86  ? 51.807  2.684   -38.418 1.00 12.70 ? 86  SER C N   1 
ATOM   5031 C  CA  . SER C 1 86  ? 52.447  2.648   -37.121 1.00 12.37 ? 86  SER C CA  1 
ATOM   5032 C  C   . SER C 1 86  ? 51.452  2.855   -35.985 1.00 12.85 ? 86  SER C C   1 
ATOM   5033 O  O   . SER C 1 86  ? 50.539  3.674   -36.075 1.00 13.42 ? 86  SER C O   1 
ATOM   5034 C  CB  . SER C 1 86  ? 53.584  3.662   -37.077 1.00 14.94 ? 86  SER C CB  1 
ATOM   5035 O  OG  . SER C 1 86  ? 54.563  3.375   -38.074 1.00 15.89 ? 86  SER C OG  1 
ATOM   5036 N  N   . ALA C 1 87  ? 51.664  2.153   -34.873 1.00 12.93 ? 87  ALA C N   1 
ATOM   5037 C  CA  . ALA C 1 87  ? 50.730  2.243   -33.750 1.00 12.40 ? 87  ALA C CA  1 
ATOM   5038 C  C   . ALA C 1 87  ? 50.733  3.631   -33.135 1.00 13.17 ? 87  ALA C C   1 
ATOM   5039 O  O   . ALA C 1 87  ? 51.791  4.287   -33.071 1.00 13.16 ? 87  ALA C O   1 
ATOM   5040 C  CB  . ALA C 1 87  ? 51.026  1.167   -32.746 1.00 13.87 ? 87  ALA C CB  1 
ATOM   5041 N  N   . THR C 1 88  ? 49.576  4.012   -32.589 1.00 11.81 ? 88  THR C N   1 
ATOM   5042 C  CA  . THR C 1 88  ? 49.458  5.226   -31.793 1.00 11.36 ? 88  THR C CA  1 
ATOM   5043 C  C   . THR C 1 88  ? 48.822  4.953   -30.429 1.00 12.58 ? 88  THR C C   1 
ATOM   5044 O  O   . THR C 1 88  ? 49.252  5.507   -29.420 1.00 12.57 ? 88  THR C O   1 
ATOM   5045 C  CB  . THR C 1 88  ? 48.818  6.389   -32.543 1.00 11.45 ? 88  THR C CB  1 
ATOM   5046 O  OG1 . THR C 1 88  ? 48.721  7.522   -31.688 1.00 13.70 ? 88  THR C OG1 1 
ATOM   5047 C  CG2 . THR C 1 88  ? 47.432  6.119   -33.081 1.00 13.06 ? 88  THR C CG2 1 
ATOM   5048 N  N   . GLN C 1 89  ? 47.763  4.133   -30.342 1.00 11.68 ? 89  GLN C N   1 
ATOM   5049 C  CA  . GLN C 1 89  ? 47.074  3.898   -29.075 1.00 11.71 ? 89  GLN C CA  1 
ATOM   5050 C  C   . GLN C 1 89  ? 46.097  2.747   -29.280 1.00 12.38 ? 89  GLN C C   1 
ATOM   5051 O  O   . GLN C 1 89  ? 45.761  2.418   -30.431 1.00 11.41 ? 89  GLN C O   1 
ATOM   5052 C  CB  . GLN C 1 89  ? 46.358  5.156   -28.575 1.00 12.02 ? 89  GLN C CB  1 
ATOM   5053 C  CG  . GLN C 1 89  ? 45.420  5.787   -29.607 1.00 13.31 ? 89  GLN C CG  1 
ATOM   5054 C  CD  . GLN C 1 89  ? 43.964  5.545   -29.289 1.00 11.49 ? 89  GLN C CD  1 
ATOM   5055 O  OE1 . GLN C 1 89  ? 43.551  4.442   -28.989 1.00 12.93 ? 89  GLN C OE1 1 
ATOM   5056 N  NE2 . GLN C 1 89  ? 43.177  6.579   -29.396 1.00 16.06 ? 89  GLN C NE2 1 
ATOM   5057 N  N   . LEU C 1 90  ? 45.709  2.119   -28.195 1.00 11.48 ? 90  LEU C N   1 
ATOM   5058 C  CA  . LEU C 1 90  ? 44.568  1.236   -28.214 1.00 10.59 ? 90  LEU C CA  1 
ATOM   5059 C  C   . LEU C 1 90  ? 43.586  1.692   -27.180 1.00 11.01 ? 90  LEU C C   1 
ATOM   5060 O  O   . LEU C 1 90  ? 43.896  2.447   -26.256 1.00 11.36 ? 90  LEU C O   1 
ATOM   5061 C  CB  . LEU C 1 90  ? 45.024  -0.223  -28.073 1.00 10.93 ? 90  LEU C CB  1 
ATOM   5062 C  CG  . LEU C 1 90  ? 45.698  -0.628  -26.741 1.00 12.02 ? 90  LEU C CG  1 
ATOM   5063 C  CD1 . LEU C 1 90  ? 44.770  -0.704  -25.528 1.00 13.00 ? 90  LEU C CD1 1 
ATOM   5064 C  CD2 . LEU C 1 90  ? 46.338  -1.966  -26.956 1.00 12.37 ? 90  LEU C CD2 1 
ATOM   5065 N  N   . HIS C 1 91  ? 42.339  1.268   -27.352 1.00 10.20 ? 91  HIS C N   1 
ATOM   5066 C  CA  . HIS C 1 91  ? 41.291  1.584   -26.409 1.00 10.05 ? 91  HIS C CA  1 
ATOM   5067 C  C   . HIS C 1 91  ? 40.141  0.583   -26.567 1.00 9.21  ? 91  HIS C C   1 
ATOM   5068 O  O   . HIS C 1 91  ? 40.186  -0.264  -27.453 1.00 10.90 ? 91  HIS C O   1 
ATOM   5069 C  CB  . HIS C 1 91  ? 40.826  3.029   -26.606 1.00 10.84 ? 91  HIS C CB  1 
ATOM   5070 C  CG  . HIS C 1 91  ? 40.229  3.182   -27.979 1.00 10.35 ? 91  HIS C CG  1 
ATOM   5071 N  ND1 . HIS C 1 91  ? 40.938  3.578   -29.101 1.00 10.20 ? 91  HIS C ND1 1 
ATOM   5072 C  CD2 . HIS C 1 91  ? 38.973  2.882   -28.383 1.00 9.84  ? 91  HIS C CD2 1 
ATOM   5073 C  CE1 . HIS C 1 91  ? 40.119  3.552   -30.168 1.00 10.09 ? 91  HIS C CE1 1 
ATOM   5074 N  NE2 . HIS C 1 91  ? 38.914  3.054   -29.795 1.00 8.56  ? 91  HIS C NE2 1 
ATOM   5075 N  N   . LEU C 1 92  ? 39.121  0.702   -25.697 1.00 10.57 ? 92  LEU C N   1 
ATOM   5076 C  CA  . LEU C 1 92  ? 38.036  -0.275  -25.701 1.00 11.40 ? 92  LEU C CA  1 
ATOM   5077 C  C   . LEU C 1 92  ? 36.678  0.414   -25.717 1.00 8.99  ? 92  LEU C C   1 
ATOM   5078 O  O   . LEU C 1 92  ? 36.514  1.591   -25.410 1.00 11.49 ? 92  LEU C O   1 
ATOM   5079 C  CB  . LEU C 1 92  ? 38.153  -1.188  -24.460 1.00 13.08 ? 92  LEU C CB  1 
ATOM   5080 C  CG  . LEU C 1 92  ? 39.376  -2.110  -24.469 1.00 13.55 ? 92  LEU C CG  1 
ATOM   5081 C  CD1 . LEU C 1 92  ? 40.350  -1.728  -23.396 1.00 20.97 ? 92  LEU C CD1 1 
ATOM   5082 C  CD2 . LEU C 1 92  ? 38.993  -3.545  -24.315 1.00 17.31 ? 92  LEU C CD2 1 
ATOM   5083 N  N   . HIS C 1 93  ? 35.673  -0.387  -26.122 1.00 10.21 ? 93  HIS C N   1 
ATOM   5084 C  CA  . HIS C 1 93  ? 34.281  0.010   -26.056 1.00 9.39  ? 93  HIS C CA  1 
ATOM   5085 C  C   . HIS C 1 93  ? 33.491  -1.112  -25.372 1.00 9.53  ? 93  HIS C C   1 
ATOM   5086 O  O   . HIS C 1 93  ? 33.763  -2.271  -25.630 1.00 10.33 ? 93  HIS C O   1 
ATOM   5087 C  CB  . HIS C 1 93  ? 33.732  0.190   -27.498 1.00 9.75  ? 93  HIS C CB  1 
ATOM   5088 C  CG  . HIS C 1 93  ? 34.494  1.204   -28.290 1.00 8.80  ? 93  HIS C CG  1 
ATOM   5089 N  ND1 . HIS C 1 93  ? 34.154  2.572   -28.323 1.00 9.16  ? 93  HIS C ND1 1 
ATOM   5090 C  CD2 . HIS C 1 93  ? 35.577  1.066   -29.102 1.00 9.59  ? 93  HIS C CD2 1 
ATOM   5091 C  CE1 . HIS C 1 93  ? 35.035  3.195   -29.121 1.00 8.89  ? 93  HIS C CE1 1 
ATOM   5092 N  NE2 . HIS C 1 93  ? 35.888  2.331   -29.579 1.00 9.96  ? 93  HIS C NE2 1 
ATOM   5093 N  N   . TRP C 1 94  ? 32.499  -0.739  -24.553 1.00 9.85  ? 94  TRP C N   1 
ATOM   5094 C  CA  . TRP C 1 94  ? 31.743  -1.734  -23.811 1.00 10.39 ? 94  TRP C CA  1 
ATOM   5095 C  C   . TRP C 1 94  ? 30.327  -1.231  -23.542 1.00 9.92  ? 94  TRP C C   1 
ATOM   5096 O  O   . TRP C 1 94  ? 29.989  -0.067  -23.761 1.00 10.74 ? 94  TRP C O   1 
ATOM   5097 C  CB  . TRP C 1 94  ? 32.501  -2.114  -22.509 1.00 11.33 ? 94  TRP C CB  1 
ATOM   5098 C  CG  . TRP C 1 94  ? 32.761  -0.953  -21.571 1.00 11.17 ? 94  TRP C CG  1 
ATOM   5099 C  CD1 . TRP C 1 94  ? 31.935  -0.454  -20.612 1.00 12.60 ? 94  TRP C CD1 1 
ATOM   5100 C  CD2 . TRP C 1 94  ? 33.946  -0.116  -21.515 1.00 11.03 ? 94  TRP C CD2 1 
ATOM   5101 N  NE1 . TRP C 1 94  ? 32.514  0.640   -19.976 1.00 12.37 ? 94  TRP C NE1 1 
ATOM   5102 C  CE2 . TRP C 1 94  ? 33.765  0.870   -20.498 1.00 12.11 ? 94  TRP C CE2 1 
ATOM   5103 C  CE3 . TRP C 1 94  ? 35.093  -0.020  -22.317 1.00 11.14 ? 94  TRP C CE3 1 
ATOM   5104 C  CZ2 . TRP C 1 94  ? 34.714  1.855   -20.209 1.00 12.05 ? 94  TRP C CZ2 1 
ATOM   5105 C  CZ3 . TRP C 1 94  ? 36.045  0.934   -21.999 1.00 12.09 ? 94  TRP C CZ3 1 
ATOM   5106 C  CH2 . TRP C 1 94  ? 35.854  1.863   -20.973 1.00 12.94 ? 94  TRP C CH2 1 
ATOM   5107 N  N   . GLY C 1 95  ? 29.554  -2.132  -22.911 1.00 11.51 ? 95  GLY C N   1 
ATOM   5108 C  CA  . GLY C 1 95  ? 28.158  -1.873  -22.599 1.00 12.94 ? 95  GLY C CA  1 
ATOM   5109 C  C   . GLY C 1 95  ? 27.982  -1.523  -21.118 1.00 12.15 ? 95  GLY C C   1 
ATOM   5110 O  O   . GLY C 1 95  ? 28.638  -0.624  -20.579 1.00 12.82 ? 95  GLY C O   1 
ATOM   5111 N  N   . ASN C 1 96  ? 27.088  -2.286  -20.465 1.00 14.27 ? 96  ASN C N   1 
ATOM   5112 C  CA  . ASN C 1 96  ? 26.905  -2.039  -19.040 1.00 15.18 ? 96  ASN C CA  1 
ATOM   5113 C  C   . ASN C 1 96  ? 26.445  -3.339  -18.408 1.00 15.74 ? 96  ASN C C   1 
ATOM   5114 O  O   . ASN C 1 96  ? 26.058  -4.272  -19.093 1.00 15.94 ? 96  ASN C O   1 
ATOM   5115 C  CB  . ASN C 1 96  ? 25.918  -0.904  -18.811 1.00 16.56 ? 96  ASN C CB  1 
ATOM   5116 C  CG  . ASN C 1 96  ? 24.487  -1.267  -19.133 1.00 22.02 ? 96  ASN C CG  1 
ATOM   5117 O  OD1 . ASN C 1 96  ? 23.778  -1.812  -18.276 1.00 25.92 ? 96  ASN C OD1 1 
ATOM   5118 N  ND2 . ASN C 1 96  ? 24.018  -0.928  -20.314 1.00 23.64 ? 96  ASN C ND2 1 
ATOM   5119 N  N   . PRO C 1 97  ? 26.470  -3.477  -17.059 1.00 17.30 ? 97  PRO C N   1 
ATOM   5120 C  CA  . PRO C 1 97  ? 26.133  -4.776  -16.467 1.00 16.52 ? 97  PRO C CA  1 
ATOM   5121 C  C   . PRO C 1 97  ? 24.709  -5.288  -16.695 1.00 16.52 ? 97  PRO C C   1 
ATOM   5122 O  O   . PRO C 1 97  ? 24.524  -6.503  -16.756 1.00 18.46 ? 97  PRO C O   1 
ATOM   5123 C  CB  . PRO C 1 97  ? 26.423  -4.557  -14.966 1.00 16.87 ? 97  PRO C CB  1 
ATOM   5124 C  CG  . PRO C 1 97  ? 27.390  -3.403  -14.959 1.00 17.63 ? 97  PRO C CG  1 
ATOM   5125 C  CD  . PRO C 1 97  ? 26.954  -2.479  -16.081 1.00 17.64 ? 97  PRO C CD  1 
ATOM   5126 N  N   . ASN C 1 98  ? 23.791  -4.376  -16.977 1.00 18.62 ? 98  ASN C N   1 
ATOM   5127 C  CA  . ASN C 1 98  ? 22.403  -4.761  -17.247 1.00 20.02 ? 98  ASN C CA  1 
ATOM   5128 C  C   . ASN C 1 98  ? 22.196  -5.164  -18.720 1.00 20.38 ? 98  ASN C C   1 
ATOM   5129 O  O   . ASN C 1 98  ? 21.214  -5.846  -19.041 1.00 22.17 ? 98  ASN C O   1 
ATOM   5130 C  CB  . ASN C 1 98  ? 21.413  -3.683  -16.817 1.00 21.38 ? 98  ASN C CB  1 
ATOM   5131 C  CG  . ASN C 1 98  ? 21.273  -3.609  -15.305 1.00 28.35 ? 98  ASN C CG  1 
ATOM   5132 O  OD1 . ASN C 1 98  ? 21.440  -4.622  -14.627 1.00 33.13 ? 98  ASN C OD1 1 
ATOM   5133 N  ND2 . ASN C 1 98  ? 20.968  -2.436  -14.783 1.00 34.39 ? 98  ASN C ND2 1 
ATOM   5134 N  N   . ASP C 1 99  ? 23.123  -4.776  -19.611 1.00 18.07 ? 99  ASP C N   1 
ATOM   5135 C  CA  . ASP C 1 99  ? 23.073  -5.069  -21.045 1.00 16.57 ? 99  ASP C CA  1 
ATOM   5136 C  C   . ASP C 1 99  ? 24.510  -5.167  -21.558 1.00 14.93 ? 99  ASP C C   1 
ATOM   5137 O  O   . ASP C 1 99  ? 25.032  -4.215  -22.156 1.00 15.24 ? 99  ASP C O   1 
ATOM   5138 C  CB  . ASP C 1 99  ? 22.263  -3.970  -21.749 1.00 16.29 ? 99  ASP C CB  1 
ATOM   5139 C  CG  . ASP C 1 99  ? 21.765  -4.358  -23.134 1.00 20.17 ? 99  ASP C CG  1 
ATOM   5140 O  OD1 . ASP C 1 99  ? 21.982  -5.496  -23.499 1.00 21.61 ? 99  ASP C OD1 1 
ATOM   5141 O  OD2 . ASP C 1 99  ? 21.253  -3.466  -23.842 1.00 22.76 ? 99  ASP C OD2 1 
ATOM   5142 N  N   . PRO C 1 100 ? 25.185  -6.282  -21.265 1.00 14.30 ? 100 PRO C N   1 
ATOM   5143 C  CA  . PRO C 1 100 ? 26.634  -6.382  -21.456 1.00 14.64 ? 100 PRO C CA  1 
ATOM   5144 C  C   . PRO C 1 100 ? 26.981  -6.742  -22.892 1.00 14.85 ? 100 PRO C C   1 
ATOM   5145 O  O   . PRO C 1 100 ? 27.602  -7.735  -23.165 1.00 14.28 ? 100 PRO C O   1 
ATOM   5146 C  CB  . PRO C 1 100 ? 27.053  -7.444  -20.422 1.00 16.09 ? 100 PRO C CB  1 
ATOM   5147 C  CG  . PRO C 1 100 ? 25.836  -8.359  -20.335 1.00 17.69 ? 100 PRO C CG  1 
ATOM   5148 C  CD  . PRO C 1 100 ? 24.661  -7.434  -20.484 1.00 15.43 ? 100 PRO C CD  1 
ATOM   5149 N  N   . HIS C 1 101 ? 26.599  -5.844  -23.804 1.00 13.63 ? 101 HIS C N   1 
ATOM   5150 C  CA  . HIS C 1 101 ? 26.713  -6.148  -25.229 1.00 14.70 ? 101 HIS C CA  1 
ATOM   5151 C  C   . HIS C 1 101 ? 27.090  -4.851  -25.924 1.00 16.16 ? 101 HIS C C   1 
ATOM   5152 O  O   . HIS C 1 101 ? 26.307  -4.324  -26.713 1.00 17.93 ? 101 HIS C O   1 
ATOM   5153 C  CB  . HIS C 1 101 ? 25.364  -6.650  -25.777 1.00 16.92 ? 101 HIS C CB  1 
ATOM   5154 C  CG  . HIS C 1 101 ? 24.826  -7.812  -25.019 1.00 17.41 ? 101 HIS C CG  1 
ATOM   5155 N  ND1 . HIS C 1 101 ? 25.384  -9.090  -25.064 1.00 18.80 ? 101 HIS C ND1 1 
ATOM   5156 C  CD2 . HIS C 1 101 ? 23.814  -7.853  -24.120 1.00 18.91 ? 101 HIS C CD2 1 
ATOM   5157 C  CE1 . HIS C 1 101 ? 24.681  -9.884  -24.256 1.00 20.69 ? 101 HIS C CE1 1 
ATOM   5158 N  NE2 . HIS C 1 101 ? 23.737  -9.149  -23.676 1.00 19.60 ? 101 HIS C NE2 1 
ATOM   5159 N  N   . GLY C 1 102 ? 28.326  -4.392  -25.728 1.00 12.33 ? 102 GLY C N   1 
ATOM   5160 C  CA  . GLY C 1 102 ? 28.727  -3.074  -26.174 1.00 12.05 ? 102 GLY C CA  1 
ATOM   5161 C  C   . GLY C 1 102 ? 29.882  -3.072  -27.173 1.00 10.48 ? 102 GLY C C   1 
ATOM   5162 O  O   . GLY C 1 102 ? 30.529  -2.026  -27.242 1.00 11.39 ? 102 GLY C O   1 
ATOM   5163 N  N   . SER C 1 103 ? 30.049  -4.119  -27.998 1.00 10.91 ? 103 SER C N   1 
ATOM   5164 C  CA  . SER C 1 103 ? 30.881  -3.958  -29.188 1.00 10.05 ? 103 SER C CA  1 
ATOM   5165 C  C   . SER C 1 103 ? 30.324  -2.878  -30.123 1.00 10.17 ? 103 SER C C   1 
ATOM   5166 O  O   . SER C 1 103 ? 29.123  -2.543  -30.064 1.00 10.18 ? 103 SER C O   1 
ATOM   5167 C  CB  . SER C 1 103 ? 31.043  -5.259  -29.930 1.00 9.81  ? 103 SER C CB  1 
ATOM   5168 O  OG  . SER C 1 103 ? 29.807  -5.687  -30.542 1.00 10.48 ? 103 SER C OG  1 
ATOM   5169 N  N   . GLU C 1 104 ? 31.192  -2.386  -31.011 1.00 9.11  ? 104 GLU C N   1 
ATOM   5170 C  CA  . GLU C 1 104 ? 30.775  -1.407  -32.006 1.00 8.62  ? 104 GLU C CA  1 
ATOM   5171 C  C   . GLU C 1 104 ? 30.274  -2.128  -33.254 1.00 8.72  ? 104 GLU C C   1 
ATOM   5172 O  O   . GLU C 1 104 ? 29.114  -1.934  -33.684 1.00 8.58  ? 104 GLU C O   1 
ATOM   5173 C  CB  . GLU C 1 104 ? 31.898  -0.394  -32.278 1.00 8.66  ? 104 GLU C CB  1 
ATOM   5174 C  CG  . GLU C 1 104 ? 32.386  0.318   -31.009 1.00 10.53 ? 104 GLU C CG  1 
ATOM   5175 C  CD  . GLU C 1 104 ? 32.747  1.738   -31.348 1.00 9.68  ? 104 GLU C CD  1 
ATOM   5176 O  OE1 . GLU C 1 104 ? 33.794  1.876   -31.964 1.00 9.91  ? 104 GLU C OE1 1 
ATOM   5177 O  OE2 . GLU C 1 104 ? 31.942  2.634   -31.101 1.00 10.44 ? 104 GLU C OE2 1 
ATOM   5178 N  N   . HIS C 1 105 ? 31.137  -2.941  -33.872 1.00 7.96  ? 105 HIS C N   1 
ATOM   5179 C  CA  . HIS C 1 105 ? 30.680  -3.792  -34.962 1.00 8.21  ? 105 HIS C CA  1 
ATOM   5180 C  C   . HIS C 1 105 ? 29.747  -4.871  -34.415 1.00 8.50  ? 105 HIS C C   1 
ATOM   5181 O  O   . HIS C 1 105 ? 29.900  -5.340  -33.264 1.00 9.89  ? 105 HIS C O   1 
ATOM   5182 C  CB  . HIS C 1 105 ? 31.892  -4.396  -35.660 1.00 8.46  ? 105 HIS C CB  1 
ATOM   5183 C  CG  . HIS C 1 105 ? 32.657  -3.357  -36.412 1.00 8.69  ? 105 HIS C CG  1 
ATOM   5184 N  ND1 . HIS C 1 105 ? 33.688  -2.664  -35.858 1.00 8.66  ? 105 HIS C ND1 1 
ATOM   5185 C  CD2 . HIS C 1 105 ? 32.450  -2.826  -37.646 1.00 8.79  ? 105 HIS C CD2 1 
ATOM   5186 C  CE1 . HIS C 1 105 ? 34.147  -1.765  -36.710 1.00 8.43  ? 105 HIS C CE1 1 
ATOM   5187 N  NE2 . HIS C 1 105 ? 33.406  -1.868  -37.859 1.00 9.87  ? 105 HIS C NE2 1 
ATOM   5188 N  N   . THR C 1 106 ? 28.814  -5.275  -35.250 1.00 8.90  ? 106 THR C N   1 
ATOM   5189 C  CA  . THR C 1 106 ? 27.935  -6.399  -34.963 1.00 9.73  ? 106 THR C CA  1 
ATOM   5190 C  C   . THR C 1 106 ? 28.140  -7.428  -36.048 1.00 9.54  ? 106 THR C C   1 
ATOM   5191 O  O   . THR C 1 106 ? 28.622  -7.136  -37.128 1.00 9.66  ? 106 THR C O   1 
ATOM   5192 C  CB  . THR C 1 106 ? 26.465  -5.988  -34.797 1.00 10.39 ? 106 THR C CB  1 
ATOM   5193 O  OG1 . THR C 1 106 ? 26.046  -5.393  -36.036 1.00 11.23 ? 106 THR C OG1 1 
ATOM   5194 C  CG2 . THR C 1 106 ? 26.274  -4.954  -33.712 1.00 11.29 ? 106 THR C CG2 1 
ATOM   5195 N  N   . VAL C 1 107 ? 27.796  -8.685  -35.723 1.00 10.40 ? 107 VAL C N   1 
ATOM   5196 C  CA  . VAL C 1 107 ? 27.857  -9.764  -36.679 1.00 10.84 ? 107 VAL C CA  1 
ATOM   5197 C  C   . VAL C 1 107 ? 26.470  -10.388 -36.747 1.00 11.11 ? 107 VAL C C   1 
ATOM   5198 O  O   . VAL C 1 107 ? 25.948  -10.842 -35.732 1.00 11.61 ? 107 VAL C O   1 
ATOM   5199 C  CB  . VAL C 1 107 ? 28.931  -10.796 -36.297 1.00 12.62 ? 107 VAL C CB  1 
ATOM   5200 C  CG1 . VAL C 1 107 ? 28.935  -11.964 -37.268 1.00 13.75 ? 107 VAL C CG1 1 
ATOM   5201 C  CG2 . VAL C 1 107 ? 30.337  -10.180 -36.134 1.00 13.41 ? 107 VAL C CG2 1 
ATOM   5202 N  N   . SER C 1 108 ? 25.863  -10.340 -37.936 1.00 10.94 ? 108 SER C N   1 
ATOM   5203 C  CA  . SER C 1 108 ? 24.536  -10.904 -38.134 1.00 12.49 ? 108 SER C CA  1 
ATOM   5204 C  C   . SER C 1 108 ? 23.553  -10.291 -37.145 1.00 12.74 ? 108 SER C C   1 
ATOM   5205 O  O   . SER C 1 108 ? 22.687  -10.969 -36.550 1.00 12.90 ? 108 SER C O   1 
ATOM   5206 C  CB  . SER C 1 108 ? 24.526  -12.419 -38.004 1.00 14.00 ? 108 SER C CB  1 
ATOM   5207 O  OG  . SER C 1 108 ? 25.345  -12.946 -39.032 1.00 17.74 ? 108 SER C OG  1 
ATOM   5208 N  N   . GLY C 1 109 ? 23.751  -8.990  -36.920 1.00 11.54 ? 109 GLY C N   1 
ATOM   5209 C  CA  . GLY C 1 109 ? 22.888  -8.224  -36.060 1.00 11.10 ? 109 GLY C CA  1 
ATOM   5210 C  C   . GLY C 1 109 ? 23.269  -8.254  -34.573 1.00 12.06 ? 109 GLY C C   1 
ATOM   5211 O  O   . GLY C 1 109 ? 22.632  -7.556  -33.787 1.00 15.29 ? 109 GLY C O   1 
ATOM   5212 N  N   . GLN C 1 110 ? 24.227  -9.104  -34.172 1.00 11.13 ? 110 GLN C N   1 
ATOM   5213 C  CA  . GLN C 1 110 ? 24.485  -9.311  -32.754 1.00 12.57 ? 110 GLN C CA  1 
ATOM   5214 C  C   . GLN C 1 110 ? 25.736  -8.538  -32.287 1.00 10.67 ? 110 GLN C C   1 
ATOM   5215 O  O   . GLN C 1 110 ? 26.796  -8.593  -32.922 1.00 10.80 ? 110 GLN C O   1 
ATOM   5216 C  CB  . GLN C 1 110 ? 24.722  -10.810 -32.478 1.00 13.13 ? 110 GLN C CB  1 
ATOM   5217 C  CG  . GLN C 1 110 ? 23.700  -11.751 -33.121 1.00 14.23 ? 110 GLN C CG  1 
ATOM   5218 C  CD  . GLN C 1 110 ? 22.292  -11.355 -32.757 1.00 15.39 ? 110 GLN C CD  1 
ATOM   5219 O  OE1 . GLN C 1 110 ? 21.495  -11.032 -33.668 1.00 19.51 ? 110 GLN C OE1 1 
ATOM   5220 N  NE2 . GLN C 1 110 ? 21.994  -11.332 -31.477 1.00 15.34 ? 110 GLN C NE2 1 
ATOM   5221 N  N   . HIS C 1 111 ? 25.594  -7.849  -31.159 1.00 11.43 ? 111 HIS C N   1 
ATOM   5222 C  CA  . HIS C 1 111 ? 26.750  -7.291  -30.487 1.00 12.23 ? 111 HIS C CA  1 
ATOM   5223 C  C   . HIS C 1 111 ? 27.545  -8.383  -29.789 1.00 12.94 ? 111 HIS C C   1 
ATOM   5224 O  O   . HIS C 1 111 ? 26.993  -9.385  -29.327 1.00 16.12 ? 111 HIS C O   1 
ATOM   5225 C  CB  . HIS C 1 111 ? 26.349  -6.296  -29.391 1.00 13.24 ? 111 HIS C CB  1 
ATOM   5226 C  CG  . HIS C 1 111 ? 25.845  -5.016  -29.943 1.00 12.28 ? 111 HIS C CG  1 
ATOM   5227 N  ND1 . HIS C 1 111 ? 26.647  -3.909  -30.143 1.00 12.28 ? 111 HIS C ND1 1 
ATOM   5228 C  CD2 . HIS C 1 111 ? 24.613  -4.682  -30.441 1.00 13.54 ? 111 HIS C CD2 1 
ATOM   5229 C  CE1 . HIS C 1 111 ? 25.929  -2.935  -30.663 1.00 12.74 ? 111 HIS C CE1 1 
ATOM   5230 N  NE2 . HIS C 1 111 ? 24.672  -3.367  -30.792 1.00 15.88 ? 111 HIS C NE2 1 
ATOM   5231 N  N   . PHE C 1 112 ? 28.829  -8.177  -29.672 1.00 11.64 ? 112 PHE C N   1 
ATOM   5232 C  CA  . PHE C 1 112 ? 29.677  -8.871  -28.701 1.00 11.12 ? 112 PHE C CA  1 
ATOM   5233 C  C   . PHE C 1 112 ? 29.731  -8.045  -27.425 1.00 11.52 ? 112 PHE C C   1 
ATOM   5234 O  O   . PHE C 1 112 ? 29.221  -6.939  -27.376 1.00 12.14 ? 112 PHE C O   1 
ATOM   5235 C  CB  . PHE C 1 112 ? 31.057  -9.114  -29.312 1.00 13.26 ? 112 PHE C CB  1 
ATOM   5236 C  CG  . PHE C 1 112 ? 31.031  -10.218 -30.322 1.00 14.74 ? 112 PHE C CG  1 
ATOM   5237 C  CD1 . PHE C 1 112 ? 30.467  -10.064 -31.600 1.00 16.37 ? 112 PHE C CD1 1 
ATOM   5238 C  CD2 . PHE C 1 112 ? 31.544  -11.452 -29.959 1.00 17.51 ? 112 PHE C CD2 1 
ATOM   5239 C  CE1 . PHE C 1 112 ? 30.399  -11.166 -32.456 1.00 20.03 ? 112 PHE C CE1 1 
ATOM   5240 C  CE2 . PHE C 1 112 ? 31.512  -12.524 -30.839 1.00 17.99 ? 112 PHE C CE2 1 
ATOM   5241 C  CZ  . PHE C 1 112 ? 30.978  -12.369 -32.088 1.00 20.04 ? 112 PHE C CZ  1 
ATOM   5242 N  N   . ALA C 1 113 ? 30.336  -8.597  -26.343 1.00 12.43 ? 113 ALA C N   1 
ATOM   5243 C  CA  . ALA C 1 113 ? 30.386  -7.915  -25.079 1.00 12.14 ? 113 ALA C CA  1 
ATOM   5244 C  C   . ALA C 1 113 ? 31.117  -6.593  -25.145 1.00 9.79  ? 113 ALA C C   1 
ATOM   5245 O  O   . ALA C 1 113 ? 30.718  -5.628  -24.507 1.00 11.48 ? 113 ALA C O   1 
ATOM   5246 C  CB  . ALA C 1 113 ? 31.011  -8.819  -24.026 1.00 13.59 ? 113 ALA C CB  1 
ATOM   5247 N  N   . ALA C 1 114 ? 32.221  -6.577  -25.916 1.00 10.86 ? 114 ALA C N   1 
ATOM   5248 C  CA  . ALA C 1 114 ? 33.073  -5.399  -25.929 1.00 10.72 ? 114 ALA C CA  1 
ATOM   5249 C  C   . ALA C 1 114 ? 33.946  -5.480  -27.174 1.00 10.66 ? 114 ALA C C   1 
ATOM   5250 O  O   . ALA C 1 114 ? 33.865  -6.450  -27.904 1.00 10.24 ? 114 ALA C O   1 
ATOM   5251 C  CB  . ALA C 1 114 ? 33.900  -5.365  -24.629 1.00 12.42 ? 114 ALA C CB  1 
ATOM   5252 N  N   . GLU C 1 115 ? 34.721  -4.423  -27.448 1.00 10.39 ? 115 GLU C N   1 
ATOM   5253 C  CA  . GLU C 1 115 ? 35.555  -4.422  -28.629 1.00 10.81 ? 115 GLU C CA  1 
ATOM   5254 C  C   . GLU C 1 115 ? 36.835  -3.652  -28.298 1.00 9.83  ? 115 GLU C C   1 
ATOM   5255 O  O   . GLU C 1 115 ? 36.767  -2.547  -27.719 1.00 10.74 ? 115 GLU C O   1 
ATOM   5256 C  CB  . GLU C 1 115 ? 34.754  -3.788  -29.780 1.00 10.65 ? 115 GLU C CB  1 
ATOM   5257 C  CG  . GLU C 1 115 ? 35.438  -3.891  -31.150 1.00 9.62  ? 115 GLU C CG  1 
ATOM   5258 C  CD  . GLU C 1 115 ? 34.484  -3.517  -32.288 1.00 9.96  ? 115 GLU C CD  1 
ATOM   5259 O  OE1 . GLU C 1 115 ? 34.978  -3.043  -33.320 1.00 10.97 ? 115 GLU C OE1 1 
ATOM   5260 O  OE2 . GLU C 1 115 ? 33.297  -3.811  -32.183 1.00 11.79 ? 115 GLU C OE2 1 
ATOM   5261 N  N   . LEU C 1 116 ? 37.973  -4.209  -28.756 1.00 10.10 ? 116 LEU C N   1 
ATOM   5262 C  CA  . LEU C 1 116 ? 39.245  -3.495  -28.624 1.00 10.68 ? 116 LEU C CA  1 
ATOM   5263 C  C   . LEU C 1 116 ? 39.676  -2.955  -29.986 1.00 9.36  ? 116 LEU C C   1 
ATOM   5264 O  O   . LEU C 1 116 ? 39.531  -3.668  -30.998 1.00 10.47 ? 116 LEU C O   1 
ATOM   5265 C  CB  . LEU C 1 116 ? 40.295  -4.520  -28.150 1.00 11.56 ? 116 LEU C CB  1 
ATOM   5266 C  CG  . LEU C 1 116 ? 41.754  -4.057  -28.280 1.00 12.05 ? 116 LEU C CG  1 
ATOM   5267 C  CD1 . LEU C 1 116 ? 42.142  -3.107  -27.166 1.00 14.01 ? 116 LEU C CD1 1 
ATOM   5268 C  CD2 . LEU C 1 116 ? 42.706  -5.251  -28.391 1.00 14.56 ? 116 LEU C CD2 1 
ATOM   5269 N  N   . HIS C 1 117 ? 40.145  -1.698  -29.974 1.00 9.82  ? 117 HIS C N   1 
ATOM   5270 C  CA  . HIS C 1 117 ? 40.642  -1.086  -31.203 1.00 9.33  ? 117 HIS C CA  1 
ATOM   5271 C  C   . HIS C 1 117 ? 42.114  -0.751  -31.013 1.00 9.10  ? 117 HIS C C   1 
ATOM   5272 O  O   . HIS C 1 117 ? 42.427  -0.031  -30.054 1.00 9.93  ? 117 HIS C O   1 
ATOM   5273 C  CB  . HIS C 1 117 ? 39.880  0.186   -31.510 1.00 9.63  ? 117 HIS C CB  1 
ATOM   5274 C  CG  . HIS C 1 117 ? 38.474  -0.101  -31.894 1.00 7.99  ? 117 HIS C CG  1 
ATOM   5275 N  ND1 . HIS C 1 117 ? 37.462  0.813   -31.791 1.00 9.53  ? 117 HIS C ND1 1 
ATOM   5276 C  CD2 . HIS C 1 117 ? 38.000  -1.203  -32.520 1.00 8.72  ? 117 HIS C CD2 1 
ATOM   5277 C  CE1 . HIS C 1 117 ? 36.372  0.242   -32.283 1.00 8.68  ? 117 HIS C CE1 1 
ATOM   5278 N  NE2 . HIS C 1 117 ? 36.647  -0.994  -32.713 1.00 8.40  ? 117 HIS C NE2 1 
ATOM   5279 N  N   . ILE C 1 118 ? 42.937  -1.248  -31.917 1.00 9.79  ? 118 ILE C N   1 
ATOM   5280 C  CA  . ILE C 1 118 ? 44.356  -0.867  -31.933 1.00 10.56 ? 118 ILE C CA  1 
ATOM   5281 C  C   . ILE C 1 118 ? 44.569  0.064   -33.121 1.00 8.34  ? 118 ILE C C   1 
ATOM   5282 O  O   . ILE C 1 118 ? 44.436  -0.386  -34.279 1.00 9.74  ? 118 ILE C O   1 
ATOM   5283 C  CB  . ILE C 1 118 ? 45.287  -2.087  -31.994 1.00 11.38 ? 118 ILE C CB  1 
ATOM   5284 C  CG1 . ILE C 1 118 ? 44.906  -3.144  -30.965 1.00 13.07 ? 118 ILE C CG1 1 
ATOM   5285 C  CG2 . ILE C 1 118 ? 46.743  -1.595  -31.835 1.00 12.54 ? 118 ILE C CG2 1 
ATOM   5286 C  CD1 . ILE C 1 118 ? 45.789  -4.401  -31.062 1.00 15.02 ? 118 ILE C CD1 1 
ATOM   5287 N  N   . VAL C 1 119 ? 44.758  1.357   -32.858 1.00 9.49  ? 119 VAL C N   1 
ATOM   5288 C  CA  . VAL C 1 119 ? 44.772  2.450   -33.814 1.00 10.02 ? 119 VAL C CA  1 
ATOM   5289 C  C   . VAL C 1 119 ? 46.178  2.649   -34.319 1.00 10.96 ? 119 VAL C C   1 
ATOM   5290 O  O   . VAL C 1 119 ? 47.127  2.792   -33.516 1.00 11.59 ? 119 VAL C O   1 
ATOM   5291 C  CB  . VAL C 1 119 ? 44.237  3.761   -33.225 1.00 10.04 ? 119 VAL C CB  1 
ATOM   5292 C  CG1 . VAL C 1 119 ? 44.169  4.878   -34.257 1.00 11.59 ? 119 VAL C CG1 1 
ATOM   5293 C  CG2 . VAL C 1 119 ? 42.890  3.596   -32.530 1.00 11.87 ? 119 VAL C CG2 1 
ATOM   5294 N  N   . HIS C 1 120 ? 46.321  2.656   -35.653 1.00 10.31 ? 120 HIS C N   1 
ATOM   5295 C  CA  . HIS C 1 120 ? 47.587  2.918   -36.336 1.00 11.26 ? 120 HIS C CA  1 
ATOM   5296 C  C   . HIS C 1 120 ? 47.428  4.063   -37.319 1.00 12.39 ? 120 HIS C C   1 
ATOM   5297 O  O   . HIS C 1 120 ? 46.327  4.329   -37.803 1.00 11.07 ? 120 HIS C O   1 
ATOM   5298 C  CB  . HIS C 1 120 ? 48.066  1.695   -37.096 1.00 10.61 ? 120 HIS C CB  1 
ATOM   5299 C  CG  . HIS C 1 120 ? 48.213  0.447   -36.321 1.00 12.38 ? 120 HIS C CG  1 
ATOM   5300 N  ND1 . HIS C 1 120 ? 47.152  -0.237  -35.745 1.00 11.48 ? 120 HIS C ND1 1 
ATOM   5301 C  CD2 . HIS C 1 120 ? 49.329  -0.245  -36.007 1.00 12.54 ? 120 HIS C CD2 1 
ATOM   5302 C  CE1 . HIS C 1 120 ? 47.616  -1.356  -35.178 1.00 11.71 ? 120 HIS C CE1 1 
ATOM   5303 N  NE2 . HIS C 1 120 ? 48.966  -1.368  -35.298 1.00 13.19 ? 120 HIS C NE2 1 
ATOM   5304 N  N   . TYR C 1 121 ? 48.528  4.732   -37.658 1.00 12.10 ? 121 TYR C N   1 
ATOM   5305 C  CA  . TYR C 1 121 ? 48.498  5.834   -38.610 1.00 12.52 ? 121 TYR C CA  1 
ATOM   5306 C  C   . TYR C 1 121 ? 49.476  5.521   -39.732 1.00 12.98 ? 121 TYR C C   1 
ATOM   5307 O  O   . TYR C 1 121 ? 50.477  4.800   -39.554 1.00 13.04 ? 121 TYR C O   1 
ATOM   5308 C  CB  . TYR C 1 121 ? 48.772  7.187   -37.956 1.00 13.76 ? 121 TYR C CB  1 
ATOM   5309 C  CG  . TYR C 1 121 ? 50.192  7.442   -37.511 1.00 13.80 ? 121 TYR C CG  1 
ATOM   5310 C  CD1 . TYR C 1 121 ? 50.670  6.854   -36.337 1.00 14.35 ? 121 TYR C CD1 1 
ATOM   5311 C  CD2 . TYR C 1 121 ? 51.078  8.164   -38.296 1.00 14.15 ? 121 TYR C CD2 1 
ATOM   5312 C  CE1 . TYR C 1 121 ? 51.981  7.055   -35.898 1.00 16.70 ? 121 TYR C CE1 1 
ATOM   5313 C  CE2 . TYR C 1 121 ? 52.405  8.343   -37.885 1.00 16.63 ? 121 TYR C CE2 1 
ATOM   5314 C  CZ  . TYR C 1 121 ? 52.836  7.798   -36.688 1.00 17.50 ? 121 TYR C CZ  1 
ATOM   5315 O  OH  . TYR C 1 121 ? 54.148  7.939   -36.259 1.00 20.89 ? 121 TYR C OH  1 
ATOM   5316 N  N   . ASN C 1 122 ? 49.215  6.139   -40.884 1.00 13.39 ? 122 ASN C N   1 
ATOM   5317 C  CA  . ASN C 1 122 ? 50.072  5.925   -42.032 1.00 13.51 ? 122 ASN C CA  1 
ATOM   5318 C  C   . ASN C 1 122 ? 51.332  6.788   -41.929 1.00 13.56 ? 122 ASN C C   1 
ATOM   5319 O  O   . ASN C 1 122 ? 51.313  7.993   -42.195 1.00 14.28 ? 122 ASN C O   1 
ATOM   5320 C  CB  . ASN C 1 122 ? 49.296  6.375   -43.259 1.00 13.94 ? 122 ASN C CB  1 
ATOM   5321 C  CG  . ASN C 1 122 ? 49.974  5.944   -44.530 1.00 15.73 ? 122 ASN C CG  1 
ATOM   5322 O  OD1 . ASN C 1 122 ? 51.215  5.915   -44.597 1.00 15.74 ? 122 ASN C OD1 1 
ATOM   5323 N  ND2 . ASN C 1 122 ? 49.185  5.664   -45.563 1.00 16.26 ? 122 ASN C ND2 1 
ATOM   5324 N  N   . SER C 1 123 ? 52.402  6.096   -41.498 1.00 13.58 ? 123 SER C N   1 
ATOM   5325 C  CA  . SER C 1 123 ? 53.646  6.781   -41.168 1.00 14.84 ? 123 SER C CA  1 
ATOM   5326 C  C   . SER C 1 123 ? 54.492  7.002   -42.413 1.00 15.86 ? 123 SER C C   1 
ATOM   5327 O  O   . SER C 1 123 ? 55.414  7.804   -42.363 1.00 16.30 ? 123 SER C O   1 
ATOM   5328 C  CB  . SER C 1 123 ? 54.384  6.035   -40.075 1.00 14.81 ? 123 SER C CB  1 
ATOM   5329 O  OG  . SER C 1 123 ? 54.531  4.672   -40.365 1.00 15.63 ? 123 SER C OG  1 
ATOM   5330 N  N   . ASP C 1 124 ? 54.126  6.399   -43.523 1.00 14.58 ? 124 ASP C N   1 
ATOM   5331 C  CA  . ASP C 1 124 ? 54.798  6.649   -44.790 1.00 15.12 ? 124 ASP C CA  1 
ATOM   5332 C  C   . ASP C 1 124 ? 54.335  7.998   -45.349 1.00 16.99 ? 124 ASP C C   1 
ATOM   5333 O  O   . ASP C 1 124 ? 55.140  8.733   -45.932 1.00 19.67 ? 124 ASP C O   1 
ATOM   5334 C  CB  . ASP C 1 124 ? 54.524  5.528   -45.800 1.00 14.30 ? 124 ASP C CB  1 
ATOM   5335 C  CG  . ASP C 1 124 ? 55.207  4.201   -45.499 1.00 16.70 ? 124 ASP C CG  1 
ATOM   5336 O  OD1 . ASP C 1 124 ? 56.232  4.237   -44.736 1.00 17.49 ? 124 ASP C OD1 1 
ATOM   5337 O  OD2 . ASP C 1 124 ? 54.792  3.183   -46.025 1.00 16.69 ? 124 ASP C OD2 1 
ATOM   5338 N  N   . LEU C 1 125 ? 53.050  8.341   -45.183 1.00 15.16 ? 125 LEU C N   1 
ATOM   5339 C  CA  . LEU C 1 125 ? 52.525  9.607   -45.687 1.00 17.55 ? 125 LEU C CA  1 
ATOM   5340 C  C   . LEU C 1 125 ? 52.581  10.734  -44.667 1.00 18.26 ? 125 LEU C C   1 
ATOM   5341 O  O   . LEU C 1 125 ? 52.651  11.901  -45.058 1.00 18.93 ? 125 LEU C O   1 
ATOM   5342 C  CB  . LEU C 1 125 ? 51.073  9.409   -46.158 1.00 16.18 ? 125 LEU C CB  1 
ATOM   5343 C  CG  . LEU C 1 125 ? 50.908  8.430   -47.316 1.00 16.92 ? 125 LEU C CG  1 
ATOM   5344 C  CD1 . LEU C 1 125 ? 49.439  8.280   -47.719 1.00 18.34 ? 125 LEU C CD1 1 
ATOM   5345 C  CD2 . LEU C 1 125 ? 51.718  8.854   -48.536 1.00 19.90 ? 125 LEU C CD2 1 
ATOM   5346 N  N   . TYR C 1 126 ? 52.472  10.406  -43.374 1.00 15.81 ? 126 TYR C N   1 
ATOM   5347 C  CA  . TYR C 1 126 ? 52.209  11.458  -42.407 1.00 16.07 ? 126 TYR C CA  1 
ATOM   5348 C  C   . TYR C 1 126 ? 53.127  11.348  -41.200 1.00 17.31 ? 126 TYR C C   1 
ATOM   5349 O  O   . TYR C 1 126 ? 53.523  10.240  -40.842 1.00 17.14 ? 126 TYR C O   1 
ATOM   5350 C  CB  . TYR C 1 126 ? 50.745  11.425  -41.933 1.00 16.81 ? 126 TYR C CB  1 
ATOM   5351 C  CG  . TYR C 1 126 ? 49.773  11.447  -43.077 1.00 16.81 ? 126 TYR C CG  1 
ATOM   5352 C  CD1 . TYR C 1 126 ? 49.707  12.533  -43.946 1.00 18.19 ? 126 TYR C CD1 1 
ATOM   5353 C  CD2 . TYR C 1 126 ? 48.961  10.342  -43.335 1.00 16.03 ? 126 TYR C CD2 1 
ATOM   5354 C  CE1 . TYR C 1 126 ? 48.871  12.518  -45.043 1.00 17.33 ? 126 TYR C CE1 1 
ATOM   5355 C  CE2 . TYR C 1 126 ? 48.115  10.325  -44.425 1.00 16.08 ? 126 TYR C CE2 1 
ATOM   5356 C  CZ  . TYR C 1 126 ? 48.074  11.415  -45.277 1.00 16.66 ? 126 TYR C CZ  1 
ATOM   5357 O  OH  . TYR C 1 126 ? 47.238  11.389  -46.362 1.00 16.97 ? 126 TYR C OH  1 
ATOM   5358 N  N   . PRO C 1 127 ? 53.465  12.484  -40.554 1.00 19.30 ? 127 PRO C N   1 
ATOM   5359 C  CA  . PRO C 1 127 ? 54.484  12.472  -39.505 1.00 19.36 ? 127 PRO C CA  1 
ATOM   5360 C  C   . PRO C 1 127 ? 53.999  11.994  -38.142 1.00 21.25 ? 127 PRO C C   1 
ATOM   5361 O  O   . PRO C 1 127 ? 54.811  11.561  -37.320 1.00 23.34 ? 127 PRO C O   1 
ATOM   5362 C  CB  . PRO C 1 127 ? 54.900  13.946  -39.399 1.00 21.25 ? 127 PRO C CB  1 
ATOM   5363 C  CG  . PRO C 1 127 ? 53.691  14.729  -39.875 1.00 20.28 ? 127 PRO C CG  1 
ATOM   5364 C  CD  . PRO C 1 127 ? 53.081  13.851  -40.951 1.00 18.94 ? 127 PRO C CD  1 
ATOM   5365 N  N   . ASP C 1 128 ? 52.676  12.013  -37.926 1.00 18.87 ? 128 ASP C N   1 
ATOM   5366 C  CA  . ASP C 1 128 ? 52.117  11.606  -36.647 1.00 18.35 ? 128 ASP C CA  1 
ATOM   5367 C  C   . ASP C 1 128 ? 50.638  11.287  -36.851 1.00 18.32 ? 128 ASP C C   1 
ATOM   5368 O  O   . ASP C 1 128 ? 50.021  11.686  -37.836 1.00 17.17 ? 128 ASP C O   1 
ATOM   5369 C  CB  . ASP C 1 128 ? 52.343  12.681  -35.566 1.00 21.07 ? 128 ASP C CB  1 
ATOM   5370 C  CG  . ASP C 1 128 ? 51.935  14.077  -36.001 1.00 26.56 ? 128 ASP C CG  1 
ATOM   5371 O  OD1 . ASP C 1 128 ? 50.771  14.274  -36.322 1.00 28.41 ? 128 ASP C OD1 1 
ATOM   5372 O  OD2 . ASP C 1 128 ? 52.807  14.967  -35.974 1.00 34.59 ? 128 ASP C OD2 1 
ATOM   5373 N  N   . ALA C 1 129 ? 50.034  10.707  -35.813 1.00 16.87 ? 129 ALA C N   1 
ATOM   5374 C  CA  . ALA C 1 129 ? 48.663  10.254  -35.952 1.00 16.99 ? 129 ALA C CA  1 
ATOM   5375 C  C   . ALA C 1 129 ? 47.662  11.419  -36.061 1.00 19.95 ? 129 ALA C C   1 
ATOM   5376 O  O   . ALA C 1 129 ? 46.668  11.333  -36.783 1.00 18.30 ? 129 ALA C O   1 
ATOM   5377 C  CB  . ALA C 1 129 ? 48.374  9.374   -34.763 1.00 18.54 ? 129 ALA C CB  1 
ATOM   5378 N  N   . SER C 1 130 ? 47.864  12.492  -35.302 1.00 20.26 ? 130 SER C N   1 
ATOM   5379 C  CA  . SER C 1 130 ? 46.899  13.582  -35.381 1.00 23.07 ? 130 SER C CA  1 
ATOM   5380 C  C   . SER C 1 130 ? 46.892  14.218  -36.767 1.00 20.82 ? 130 SER C C   1 
ATOM   5381 O  O   . SER C 1 130 ? 45.816  14.451  -37.312 1.00 22.16 ? 130 SER C O   1 
ATOM   5382 C  CB  . SER C 1 130 ? 47.063  14.585  -34.281 1.00 27.60 ? 130 SER C CB  1 
ATOM   5383 O  OG  . SER C 1 130 ? 48.422  14.941  -34.128 1.00 35.36 ? 130 SER C OG  1 
ATOM   5384 N  N   . THR C 1 131 ? 48.083  14.420  -37.362 1.00 19.30 ? 131 THR C N   1 
ATOM   5385 C  CA  . THR C 1 131 ? 48.168  14.926  -38.735 1.00 18.95 ? 131 THR C CA  1 
ATOM   5386 C  C   . THR C 1 131 ? 47.465  13.946  -39.686 1.00 17.30 ? 131 THR C C   1 
ATOM   5387 O  O   . THR C 1 131 ? 46.740  14.348  -40.607 1.00 17.79 ? 131 THR C O   1 
ATOM   5388 C  CB  . THR C 1 131 ? 49.623  15.130  -39.198 1.00 19.64 ? 131 THR C CB  1 
ATOM   5389 O  OG1 . THR C 1 131 ? 50.269  16.039  -38.307 1.00 23.41 ? 131 THR C OG1 1 
ATOM   5390 C  CG2 . THR C 1 131 ? 49.688  15.669  -40.617 1.00 20.36 ? 131 THR C CG2 1 
ATOM   5391 N  N   . ALA C 1 132 ? 47.666  12.639  -39.462 1.00 16.38 ? 132 ALA C N   1 
ATOM   5392 C  CA  . ALA C 1 132 ? 47.111  11.630  -40.359 1.00 15.94 ? 132 ALA C CA  1 
ATOM   5393 C  C   . ALA C 1 132 ? 45.580  11.547  -40.299 1.00 13.78 ? 132 ALA C C   1 
ATOM   5394 O  O   . ALA C 1 132 ? 44.981  11.189  -41.293 1.00 14.35 ? 132 ALA C O   1 
ATOM   5395 C  CB  . ALA C 1 132 ? 47.694  10.288  -40.040 1.00 15.13 ? 132 ALA C CB  1 
ATOM   5396 N  N   . SER C 1 133 ? 44.984  11.872  -39.153 1.00 14.23 ? 133 SER C N   1 
ATOM   5397 C  CA  . SER C 1 133 ? 43.652  11.385  -38.820 1.00 14.60 ? 133 SER C CA  1 
ATOM   5398 C  C   . SER C 1 133 ? 42.603  11.963  -39.754 1.00 15.14 ? 133 SER C C   1 
ATOM   5399 O  O   . SER C 1 133 ? 41.556  11.355  -39.961 1.00 15.09 ? 133 SER C O   1 
ATOM   5400 C  CB  . SER C 1 133 ? 43.345  11.676  -37.370 1.00 17.38 ? 133 SER C CB  1 
ATOM   5401 O  OG  . SER C 1 133 ? 43.313  13.104  -37.178 1.00 17.01 ? 133 SER C OG  1 
ATOM   5402 N  N   . ASN C 1 134 ? 42.835  13.118  -40.362 1.00 14.33 ? 134 ASN C N   1 
ATOM   5403 C  CA  . ASN C 1 134 ? 41.820  13.721  -41.221 1.00 16.33 ? 134 ASN C CA  1 
ATOM   5404 C  C   . ASN C 1 134 ? 42.256  13.678  -42.685 1.00 16.65 ? 134 ASN C C   1 
ATOM   5405 O  O   . ASN C 1 134 ? 41.691  14.387  -43.495 1.00 19.78 ? 134 ASN C O   1 
ATOM   5406 C  CB  . ASN C 1 134 ? 41.423  15.142  -40.790 1.00 18.93 ? 134 ASN C CB  1 
ATOM   5407 C  CG  . ASN C 1 134 ? 42.569  16.133  -40.891 1.00 23.22 ? 134 ASN C CG  1 
ATOM   5408 O  OD1 . ASN C 1 134 ? 43.717  15.736  -41.092 1.00 22.58 ? 134 ASN C OD1 1 
ATOM   5409 N  ND2 . ASN C 1 134 ? 42.256  17.413  -40.787 1.00 25.32 ? 134 ASN C ND2 1 
ATOM   5410 N  N   . LYS C 1 135 ? 43.207  12.810  -43.043 1.00 17.80 ? 135 LYS C N   1 
ATOM   5411 C  CA  . LYS C 1 135 ? 43.775  12.817  -44.371 1.00 17.78 ? 135 LYS C CA  1 
ATOM   5412 C  C   . LYS C 1 135 ? 43.642  11.455  -45.025 1.00 17.29 ? 135 LYS C C   1 
ATOM   5413 O  O   . LYS C 1 135 ? 43.431  10.438  -44.351 1.00 15.11 ? 135 LYS C O   1 
ATOM   5414 C  CB  . LYS C 1 135 ? 45.256  13.207  -44.251 1.00 18.91 ? 135 LYS C CB  1 
ATOM   5415 C  CG  . LYS C 1 135 ? 45.450  14.694  -43.965 1.00 21.70 ? 135 LYS C CG  1 
ATOM   5416 C  CD  . LYS C 1 135 ? 46.862  15.179  -43.891 1.00 23.60 ? 135 LYS C CD  1 
ATOM   5417 C  CE  . LYS C 1 135 ? 46.937  16.602  -43.387 1.00 23.56 ? 135 LYS C CE  1 
ATOM   5418 N  NZ  . LYS C 1 135 ? 46.385  16.766  -42.018 1.00 24.78 ? 135 LYS C NZ  1 
ATOM   5419 N  N   . SER C 1 136 ? 43.743  11.434  -46.362 1.00 16.38 ? 136 SER C N   1 
ATOM   5420 C  CA  . SER C 1 136 ? 43.535  10.256  -47.168 1.00 16.18 ? 136 SER C CA  1 
ATOM   5421 C  C   . SER C 1 136 ? 44.458  9.144   -46.696 1.00 15.44 ? 136 SER C C   1 
ATOM   5422 O  O   . SER C 1 136 ? 45.670  9.360   -46.491 1.00 15.46 ? 136 SER C O   1 
ATOM   5423 C  CB  . SER C 1 136 ? 43.799  10.612  -48.606 1.00 19.63 ? 136 SER C CB  1 
ATOM   5424 O  OG  . SER C 1 136 ? 43.859  9.469   -49.403 1.00 26.61 ? 136 SER C OG  1 
ATOM   5425 N  N   . GLU C 1 137 ? 43.864  7.969   -46.519 1.00 16.16 ? 137 GLU C N   1 
ATOM   5426 C  CA  . GLU C 1 137 ? 44.577  6.760   -46.137 1.00 14.91 ? 137 GLU C CA  1 
ATOM   5427 C  C   . GLU C 1 137 ? 45.309  6.955   -44.809 1.00 15.22 ? 137 GLU C C   1 
ATOM   5428 O  O   . GLU C 1 137 ? 46.329  6.302   -44.542 1.00 14.72 ? 137 GLU C O   1 
ATOM   5429 C  CB  . GLU C 1 137 ? 45.566  6.337   -47.233 1.00 16.54 ? 137 GLU C CB  1 
ATOM   5430 C  CG  . GLU C 1 137 ? 44.900  5.898   -48.548 1.00 19.72 ? 137 GLU C CG  1 
ATOM   5431 C  CD  . GLU C 1 137 ? 45.841  5.529   -49.693 1.00 28.17 ? 137 GLU C CD  1 
ATOM   5432 O  OE1 . GLU C 1 137 ? 47.042  5.870   -49.633 1.00 32.75 ? 137 GLU C OE1 1 
ATOM   5433 O  OE2 . GLU C 1 137 ? 45.377  4.909   -50.653 1.00 31.22 ? 137 GLU C OE2 1 
ATOM   5434 N  N   . GLY C 1 138 ? 44.724  7.759   -43.925 1.00 13.20 ? 138 GLY C N   1 
ATOM   5435 C  CA  . GLY C 1 138 ? 45.428  8.206   -42.730 1.00 14.20 ? 138 GLY C CA  1 
ATOM   5436 C  C   . GLY C 1 138 ? 45.565  7.145   -41.635 1.00 13.13 ? 138 GLY C C   1 
ATOM   5437 O  O   . GLY C 1 138 ? 46.594  7.122   -40.952 1.00 12.86 ? 138 GLY C O   1 
ATOM   5438 N  N   . LEU C 1 139 ? 44.556  6.271   -41.454 1.00 11.13 ? 139 LEU C N   1 
ATOM   5439 C  CA  . LEU C 1 139 ? 44.470  5.417   -40.278 1.00 9.99  ? 139 LEU C CA  1 
ATOM   5440 C  C   . LEU C 1 139 ? 44.149  3.999   -40.683 1.00 9.98  ? 139 LEU C C   1 
ATOM   5441 O  O   . LEU C 1 139 ? 43.493  3.765   -41.699 1.00 10.92 ? 139 LEU C O   1 
ATOM   5442 C  CB  . LEU C 1 139 ? 43.420  5.950   -39.307 1.00 10.86 ? 139 LEU C CB  1 
ATOM   5443 C  CG  . LEU C 1 139 ? 43.673  7.332   -38.747 1.00 10.46 ? 139 LEU C CG  1 
ATOM   5444 C  CD1 . LEU C 1 139 ? 42.463  7.821   -37.957 1.00 13.20 ? 139 LEU C CD1 1 
ATOM   5445 C  CD2 . LEU C 1 139 ? 44.954  7.363   -37.894 1.00 12.76 ? 139 LEU C CD2 1 
ATOM   5446 N  N   . ALA C 1 140 ? 44.539  3.049   -39.862 1.00 10.20 ? 140 ALA C N   1 
ATOM   5447 C  CA  . ALA C 1 140 ? 44.152  1.667   -39.960 1.00 9.88  ? 140 ALA C CA  1 
ATOM   5448 C  C   . ALA C 1 140 ? 43.891  1.179   -38.548 1.00 9.89  ? 140 ALA C C   1 
ATOM   5449 O  O   . ALA C 1 140 ? 44.698  1.406   -37.637 1.00 11.53 ? 140 ALA C O   1 
ATOM   5450 C  CB  . ALA C 1 140 ? 45.213  0.819   -40.625 1.00 11.37 ? 140 ALA C CB  1 
ATOM   5451 N  N   . VAL C 1 141 ? 42.778  0.494   -38.324 1.00 9.43  ? 141 VAL C N   1 
ATOM   5452 C  CA  . VAL C 1 141 ? 42.461  -0.005  -36.991 1.00 9.32  ? 141 VAL C CA  1 
ATOM   5453 C  C   . VAL C 1 141 ? 42.317  -1.508  -37.062 1.00 9.50  ? 141 VAL C C   1 
ATOM   5454 O  O   . VAL C 1 141 ? 41.726  -2.077  -38.004 1.00 10.31 ? 141 VAL C O   1 
ATOM   5455 C  CB  . VAL C 1 141 ? 41.176  0.655   -36.454 1.00 9.81  ? 141 VAL C CB  1 
ATOM   5456 C  CG1 . VAL C 1 141 ? 40.785  0.104   -35.086 1.00 11.55 ? 141 VAL C CG1 1 
ATOM   5457 C  CG2 . VAL C 1 141 ? 41.314  2.164   -36.374 1.00 12.02 ? 141 VAL C CG2 1 
ATOM   5458 N  N   . LEU C 1 142 ? 42.879  -2.177  -36.056 1.00 9.73  ? 142 LEU C N   1 
ATOM   5459 C  CA  . LEU C 1 142 ? 42.601  -3.579  -35.842 1.00 9.81  ? 142 LEU C CA  1 
ATOM   5460 C  C   . LEU C 1 142 ? 41.528  -3.667  -34.768 1.00 10.35 ? 142 LEU C C   1 
ATOM   5461 O  O   . LEU C 1 142 ? 41.710  -3.109  -33.674 1.00 11.00 ? 142 LEU C O   1 
ATOM   5462 C  CB  . LEU C 1 142 ? 43.876  -4.300  -35.363 1.00 11.61 ? 142 LEU C CB  1 
ATOM   5463 C  CG  . LEU C 1 142 ? 45.097  -4.137  -36.255 1.00 10.68 ? 142 LEU C CG  1 
ATOM   5464 C  CD1 . LEU C 1 142 ? 46.225  -4.939  -35.574 1.00 13.37 ? 142 LEU C CD1 1 
ATOM   5465 C  CD2 . LEU C 1 142 ? 44.878  -4.695  -37.646 1.00 11.65 ? 142 LEU C CD2 1 
ATOM   5466 N  N   . ALA C 1 143 ? 40.445  -4.389  -35.069 1.00 10.14 ? 143 ALA C N   1 
ATOM   5467 C  CA  . ALA C 1 143 ? 39.341  -4.558  -34.144 1.00 10.31 ? 143 ALA C CA  1 
ATOM   5468 C  C   . ALA C 1 143 ? 39.235  -6.007  -33.701 1.00 10.00 ? 143 ALA C C   1 
ATOM   5469 O  O   . ALA C 1 143 ? 39.213  -6.926  -34.514 1.00 10.65 ? 143 ALA C O   1 
ATOM   5470 C  CB  . ALA C 1 143 ? 38.062  -4.090  -34.797 1.00 10.07 ? 143 ALA C CB  1 
ATOM   5471 N  N   . VAL C 1 144 ? 39.199  -6.154  -32.365 1.00 9.73  ? 144 VAL C N   1 
ATOM   5472 C  CA  . VAL C 1 144 ? 39.013  -7.481  -31.787 1.00 11.27 ? 144 VAL C CA  1 
ATOM   5473 C  C   . VAL C 1 144 ? 37.697  -7.507  -31.018 1.00 10.73 ? 144 VAL C C   1 
ATOM   5474 O  O   . VAL C 1 144 ? 37.451  -6.681  -30.133 1.00 11.00 ? 144 VAL C O   1 
ATOM   5475 C  CB  . VAL C 1 144 ? 40.153  -7.769  -30.796 1.00 11.46 ? 144 VAL C CB  1 
ATOM   5476 C  CG1 . VAL C 1 144 ? 39.993  -9.169  -30.227 1.00 13.41 ? 144 VAL C CG1 1 
ATOM   5477 C  CG2 . VAL C 1 144 ? 41.484  -7.717  -31.522 1.00 12.09 ? 144 VAL C CG2 1 
ATOM   5478 N  N   . LEU C 1 145 ? 36.832  -8.450  -31.408 1.00 11.96 ? 145 LEU C N   1 
ATOM   5479 C  CA  . LEU C 1 145 ? 35.573  -8.649  -30.706 1.00 12.12 ? 145 LEU C CA  1 
ATOM   5480 C  C   . LEU C 1 145 ? 35.811  -9.457  -29.418 1.00 12.53 ? 145 LEU C C   1 
ATOM   5481 O  O   . LEU C 1 145 ? 36.620  -10.392 -29.469 1.00 13.44 ? 145 LEU C O   1 
ATOM   5482 C  CB  . LEU C 1 145 ? 34.591  -9.362  -31.631 1.00 12.71 ? 145 LEU C CB  1 
ATOM   5483 C  CG  . LEU C 1 145 ? 34.285  -8.631  -32.945 1.00 13.02 ? 145 LEU C CG  1 
ATOM   5484 C  CD1 . LEU C 1 145 ? 33.603  -9.573  -33.939 1.00 15.34 ? 145 LEU C CD1 1 
ATOM   5485 C  CD2 . LEU C 1 145 ? 33.423  -7.419  -32.652 1.00 15.95 ? 145 LEU C CD2 1 
ATOM   5486 N  N   . ILE C 1 146 ? 35.108  -9.080  -28.356 1.00 11.28 ? 146 ILE C N   1 
ATOM   5487 C  CA  . ILE C 1 146 ? 35.384  -9.663  -27.019 1.00 11.97 ? 146 ILE C CA  1 
ATOM   5488 C  C   . ILE C 1 146 ? 34.075  -10.269 -26.534 1.00 13.69 ? 146 ILE C C   1 
ATOM   5489 O  O   . ILE C 1 146 ? 33.046  -9.593  -26.549 1.00 13.25 ? 146 ILE C O   1 
ATOM   5490 C  CB  . ILE C 1 146 ? 35.904  -8.589  -26.052 1.00 12.51 ? 146 ILE C CB  1 
ATOM   5491 C  CG1 . ILE C 1 146 ? 37.235  -7.975  -26.509 1.00 12.09 ? 146 ILE C CG1 1 
ATOM   5492 C  CG2 . ILE C 1 146 ? 36.016  -9.219  -24.642 1.00 13.44 ? 146 ILE C CG2 1 
ATOM   5493 C  CD1 . ILE C 1 146 ? 37.599  -6.678  -25.835 1.00 14.14 ? 146 ILE C CD1 1 
ATOM   5494 N  N   . GLU C 1 147 ? 34.141  -11.527 -26.044 1.00 14.93 ? 147 GLU C N   1 
ATOM   5495 C  CA  . GLU C 1 147 ? 32.994  -12.171 -25.421 1.00 16.43 ? 147 GLU C CA  1 
ATOM   5496 C  C   . GLU C 1 147 ? 33.399  -12.768 -24.072 1.00 16.76 ? 147 GLU C C   1 
ATOM   5497 O  O   . GLU C 1 147 ? 34.586  -12.886 -23.746 1.00 17.10 ? 147 GLU C O   1 
ATOM   5498 C  CB  . GLU C 1 147 ? 32.474  -13.292 -26.316 1.00 17.09 ? 147 GLU C CB  1 
ATOM   5499 C  CG  . GLU C 1 147 ? 33.461  -14.412 -26.546 1.00 17.05 ? 147 GLU C CG  1 
ATOM   5500 C  CD  . GLU C 1 147 ? 33.036  -15.453 -27.593 1.00 21.30 ? 147 GLU C CD  1 
ATOM   5501 O  OE1 . GLU C 1 147 ? 31.992  -15.259 -28.254 1.00 23.94 ? 147 GLU C OE1 1 
ATOM   5502 O  OE2 . GLU C 1 147 ? 33.764  -16.482 -27.767 1.00 27.55 ? 147 GLU C OE2 1 
ATOM   5503 N  N   . MET C 1 148 ? 32.352  -13.005 -23.268 1.00 18.78 ? 148 MET C N   1 
ATOM   5504 C  CA  . MET C 1 148 ? 32.576  -13.676 -21.998 1.00 21.72 ? 148 MET C CA  1 
ATOM   5505 C  C   . MET C 1 148 ? 33.047  -15.112 -22.220 1.00 21.83 ? 148 MET C C   1 
ATOM   5506 O  O   . MET C 1 148 ? 32.568  -15.840 -23.095 1.00 21.82 ? 148 MET C O   1 
ATOM   5507 C  CB  . MET C 1 148 ? 31.287  -13.723 -21.182 1.00 24.98 ? 148 MET C CB  1 
ATOM   5508 C  CG  . MET C 1 148 ? 31.377  -12.936 -19.897 1.00 36.70 ? 148 MET C CG  1 
ATOM   5509 S  SD  . MET C 1 148 ? 29.896  -13.135 -18.859 1.00 53.87 ? 148 MET C SD  1 
ATOM   5510 C  CE  . MET C 1 148 ? 28.664  -13.107 -20.162 1.00 31.45 ? 148 MET C CE  1 
ATOM   5511 N  N   . GLY C 1 149 ? 34.024  -15.514 -21.390 1.00 21.32 ? 149 GLY C N   1 
ATOM   5512 C  CA  . GLY C 1 149 ? 34.487  -16.899 -21.366 1.00 23.46 ? 149 GLY C CA  1 
ATOM   5513 C  C   . GLY C 1 149 ? 35.547  -17.068 -20.275 1.00 22.44 ? 149 GLY C C   1 
ATOM   5514 O  O   . GLY C 1 149 ? 35.381  -16.574 -19.156 1.00 20.59 ? 149 GLY C O   1 
ATOM   5515 N  N   . SER C 1 150 ? 36.650  -17.728 -20.653 1.00 24.24 ? 150 SER C N   1 
ATOM   5516 C  CA  . SER C 1 150 ? 37.821  -17.922 -19.808 1.00 22.73 ? 150 SER C CA  1 
ATOM   5517 C  C   . SER C 1 150 ? 38.480  -16.598 -19.431 1.00 26.02 ? 150 SER C C   1 
ATOM   5518 O  O   . SER C 1 150 ? 38.514  -15.657 -20.240 1.00 21.54 ? 150 SER C O   1 
ATOM   5519 C  CB  . SER C 1 150 ? 38.856  -18.766 -20.523 1.00 26.34 ? 150 SER C CB  1 
ATOM   5520 O  OG  . SER C 1 150 ? 38.300  -19.995 -20.957 1.00 35.68 ? 150 SER C OG  1 
ATOM   5521 N  N   . PHE C 1 151 ? 39.116  -16.592 -18.249 1.00 21.35 ? 151 PHE C N   1 
ATOM   5522 C  CA  . PHE C 1 151 ? 39.955  -15.509 -17.764 1.00 21.45 ? 151 PHE C CA  1 
ATOM   5523 C  C   . PHE C 1 151 ? 41.106  -15.279 -18.744 1.00 22.03 ? 151 PHE C C   1 
ATOM   5524 O  O   . PHE C 1 151 ? 41.754  -16.223 -19.210 1.00 24.72 ? 151 PHE C O   1 
ATOM   5525 C  CB  . PHE C 1 151 ? 40.494  -15.827 -16.355 1.00 21.29 ? 151 PHE C CB  1 
ATOM   5526 C  CG  . PHE C 1 151 ? 41.484  -14.809 -15.852 1.00 20.13 ? 151 PHE C CG  1 
ATOM   5527 C  CD1 . PHE C 1 151 ? 41.063  -13.578 -15.362 1.00 20.60 ? 151 PHE C CD1 1 
ATOM   5528 C  CD2 . PHE C 1 151 ? 42.846  -15.077 -15.879 1.00 20.73 ? 151 PHE C CD2 1 
ATOM   5529 C  CE1 . PHE C 1 151 ? 41.985  -12.619 -14.968 1.00 19.87 ? 151 PHE C CE1 1 
ATOM   5530 C  CE2 . PHE C 1 151 ? 43.771  -14.123 -15.498 1.00 21.47 ? 151 PHE C CE2 1 
ATOM   5531 C  CZ  . PHE C 1 151 ? 43.332  -12.903 -15.013 1.00 21.58 ? 151 PHE C CZ  1 
ATOM   5532 N  N   . ASN C 1 152 ? 41.389  -14.001 -19.027 1.00 19.35 ? 152 ASN C N   1 
ATOM   5533 C  CA  . ASN C 1 152 ? 42.416  -13.708 -20.008 1.00 17.54 ? 152 ASN C CA  1 
ATOM   5534 C  C   . ASN C 1 152 ? 43.560  -12.932 -19.374 1.00 19.64 ? 152 ASN C C   1 
ATOM   5535 O  O   . ASN C 1 152 ? 43.435  -11.743 -19.056 1.00 19.68 ? 152 ASN C O   1 
ATOM   5536 C  CB  . ASN C 1 152 ? 41.799  -12.887 -21.153 1.00 17.91 ? 152 ASN C CB  1 
ATOM   5537 C  CG  . ASN C 1 152 ? 42.706  -12.782 -22.345 1.00 18.05 ? 152 ASN C CG  1 
ATOM   5538 O  OD1 . ASN C 1 152 ? 43.873  -12.410 -22.211 1.00 19.14 ? 152 ASN C OD1 1 
ATOM   5539 N  ND2 . ASN C 1 152 ? 42.160  -12.976 -23.545 1.00 18.06 ? 152 ASN C ND2 1 
ATOM   5540 N  N   . PRO C 1 153 ? 44.713  -13.583 -19.085 1.00 21.22 ? 153 PRO C N   1 
ATOM   5541 C  CA  . PRO C 1 153 ? 45.822  -12.897 -18.436 1.00 22.87 ? 153 PRO C CA  1 
ATOM   5542 C  C   . PRO C 1 153 ? 46.376  -11.690 -19.178 1.00 21.34 ? 153 PRO C C   1 
ATOM   5543 O  O   . PRO C 1 153 ? 46.830  -10.732 -18.560 1.00 23.33 ? 153 PRO C O   1 
ATOM   5544 C  CB  . PRO C 1 153 ? 46.895  -13.991 -18.219 1.00 23.93 ? 153 PRO C CB  1 
ATOM   5545 C  CG  . PRO C 1 153 ? 46.425  -15.203 -18.974 1.00 27.16 ? 153 PRO C CG  1 
ATOM   5546 C  CD  . PRO C 1 153 ? 44.959  -15.020 -19.337 1.00 21.87 ? 153 PRO C CD  1 
ATOM   5547 N  N   . SER C 1 154 ? 46.247  -11.685 -20.509 1.00 21.13 ? 154 SER C N   1 
ATOM   5548 C  CA  . SER C 1 154 ? 46.813  -10.625 -21.320 1.00 19.66 ? 154 SER C CA  1 
ATOM   5549 C  C   . SER C 1 154 ? 45.963  -9.366  -21.179 1.00 15.11 ? 154 SER C C   1 
ATOM   5550 O  O   . SER C 1 154 ? 46.480  -8.265  -20.961 1.00 18.18 ? 154 SER C O   1 
ATOM   5551 C  CB  . SER C 1 154 ? 46.973  -11.099 -22.729 1.00 20.64 ? 154 SER C CB  1 
ATOM   5552 O  OG  . SER C 1 154 ? 47.715  -12.315 -22.736 1.00 25.85 ? 154 SER C OG  1 
ATOM   5553 N  N   . TYR C 1 155 ? 44.631  -9.553  -21.241 1.00 16.37 ? 155 TYR C N   1 
ATOM   5554 C  CA  . TYR C 1 155 ? 43.740  -8.423  -21.021 1.00 18.04 ? 155 TYR C CA  1 
ATOM   5555 C  C   . TYR C 1 155 ? 43.889  -7.867  -19.611 1.00 18.97 ? 155 TYR C C   1 
ATOM   5556 O  O   . TYR C 1 155 ? 43.749  -6.658  -19.384 1.00 18.42 ? 155 TYR C O   1 
ATOM   5557 C  CB  . TYR C 1 155 ? 42.302  -8.734  -21.451 1.00 16.74 ? 155 TYR C CB  1 
ATOM   5558 C  CG  . TYR C 1 155 ? 42.113  -8.582  -22.953 1.00 15.49 ? 155 TYR C CG  1 
ATOM   5559 C  CD1 . TYR C 1 155 ? 42.474  -9.597  -23.825 1.00 16.95 ? 155 TYR C CD1 1 
ATOM   5560 C  CD2 . TYR C 1 155 ? 41.554  -7.416  -23.482 1.00 15.20 ? 155 TYR C CD2 1 
ATOM   5561 C  CE1 . TYR C 1 155 ? 42.313  -9.460  -25.208 1.00 16.74 ? 155 TYR C CE1 1 
ATOM   5562 C  CE2 . TYR C 1 155 ? 41.357  -7.278  -24.860 1.00 15.38 ? 155 TYR C CE2 1 
ATOM   5563 C  CZ  . TYR C 1 155 ? 41.746  -8.291  -25.710 1.00 15.57 ? 155 TYR C CZ  1 
ATOM   5564 O  OH  . TYR C 1 155 ? 41.577  -8.087  -27.061 1.00 14.77 ? 155 TYR C OH  1 
ATOM   5565 N  N   . ASP C 1 156 ? 44.236  -8.731  -18.643 1.00 18.84 ? 156 ASP C N   1 
ATOM   5566 C  CA  . ASP C 1 156 ? 44.355  -8.251  -17.275 1.00 20.91 ? 156 ASP C CA  1 
ATOM   5567 C  C   . ASP C 1 156 ? 45.582  -7.354  -17.086 1.00 19.24 ? 156 ASP C C   1 
ATOM   5568 O  O   . ASP C 1 156 ? 45.618  -6.571  -16.140 1.00 20.05 ? 156 ASP C O   1 
ATOM   5569 C  CB  . ASP C 1 156 ? 44.293  -9.409  -16.269 1.00 23.26 ? 156 ASP C CB  1 
ATOM   5570 C  CG  . ASP C 1 156 ? 43.255  -9.150  -15.188 1.00 27.36 ? 156 ASP C CG  1 
ATOM   5571 O  OD1 . ASP C 1 156 ? 42.084  -8.765  -15.518 1.00 23.93 ? 156 ASP C OD1 1 
ATOM   5572 O  OD2 . ASP C 1 156 ? 43.629  -9.297  -14.013 1.00 32.19 ? 156 ASP C OD2 1 
ATOM   5573 N  N   . LYS C 1 157 ? 46.490  -7.359  -18.063 1.00 18.90 ? 157 LYS C N   1 
ATOM   5574 C  CA  . LYS C 1 157 ? 47.675  -6.515  -18.056 1.00 21.37 ? 157 LYS C CA  1 
ATOM   5575 C  C   . LYS C 1 157 ? 47.226  -5.067  -18.176 1.00 21.94 ? 157 LYS C C   1 
ATOM   5576 O  O   . LYS C 1 157 ? 47.879  -4.186  -17.606 1.00 26.02 ? 157 LYS C O   1 
ATOM   5577 C  CB  . LYS C 1 157 ? 48.701  -6.971  -19.093 1.00 23.81 ? 157 LYS C CB  1 
ATOM   5578 C  CG  . LYS C 1 157 ? 49.283  -8.353  -18.801 1.00 25.20 ? 157 LYS C CG  1 
ATOM   5579 C  CD  . LYS C 1 157 ? 50.413  -8.826  -19.694 1.00 27.76 ? 157 LYS C CD  1 
ATOM   5580 C  CE  . LYS C 1 157 ? 50.848  -10.241 -19.348 1.00 30.92 ? 157 LYS C CE  1 
ATOM   5581 N  NZ  . LYS C 1 157 ? 51.312  -11.011 -20.531 1.00 30.73 ? 157 LYS C NZ  1 
ATOM   5582 N  N   . ILE C 1 158 ? 46.033  -4.852  -18.774 1.00 19.62 ? 158 ILE C N   1 
ATOM   5583 C  CA  . ILE C 1 158 ? 45.438  -3.523  -18.777 1.00 19.99 ? 158 ILE C CA  1 
ATOM   5584 C  C   . ILE C 1 158 ? 44.480  -3.392  -17.588 1.00 18.91 ? 158 ILE C C   1 
ATOM   5585 O  O   . ILE C 1 158 ? 44.453  -2.356  -16.883 1.00 19.40 ? 158 ILE C O   1 
ATOM   5586 C  CB  . ILE C 1 158 ? 44.729  -3.299  -20.134 1.00 20.26 ? 158 ILE C CB  1 
ATOM   5587 C  CG1 . ILE C 1 158 ? 45.735  -3.318  -21.292 1.00 23.06 ? 158 ILE C CG1 1 
ATOM   5588 C  CG2 . ILE C 1 158 ? 43.886  -2.024  -20.148 1.00 18.61 ? 158 ILE C CG2 1 
ATOM   5589 C  CD1 . ILE C 1 158 ? 45.078  -3.423  -22.677 1.00 23.52 ? 158 ILE C CD1 1 
ATOM   5590 N  N   . PHE C 1 159 ? 43.567  -4.361  -17.468 1.00 16.63 ? 159 PHE C N   1 
ATOM   5591 C  CA  . PHE C 1 159 ? 42.427  -4.207  -16.580 1.00 17.29 ? 159 PHE C CA  1 
ATOM   5592 C  C   . PHE C 1 159 ? 42.861  -4.031  -15.111 1.00 17.44 ? 159 PHE C C   1 
ATOM   5593 O  O   . PHE C 1 159 ? 42.112  -3.434  -14.331 1.00 18.08 ? 159 PHE C O   1 
ATOM   5594 C  CB  . PHE C 1 159 ? 41.460  -5.389  -16.697 1.00 16.61 ? 159 PHE C CB  1 
ATOM   5595 C  CG  . PHE C 1 159 ? 40.750  -5.567  -18.027 1.00 17.73 ? 159 PHE C CG  1 
ATOM   5596 C  CD1 . PHE C 1 159 ? 40.621  -4.529  -18.961 1.00 19.88 ? 159 PHE C CD1 1 
ATOM   5597 C  CD2 . PHE C 1 159 ? 40.197  -6.806  -18.319 1.00 17.25 ? 159 PHE C CD2 1 
ATOM   5598 C  CE1 . PHE C 1 159 ? 39.954  -4.767  -20.166 1.00 17.74 ? 159 PHE C CE1 1 
ATOM   5599 C  CE2 . PHE C 1 159 ? 39.515  -7.029  -19.509 1.00 20.28 ? 159 PHE C CE2 1 
ATOM   5600 C  CZ  . PHE C 1 159 ? 39.419  -6.010  -20.421 1.00 18.90 ? 159 PHE C CZ  1 
ATOM   5601 N  N   . SER C 1 160 ? 44.089  -4.488  -14.803 1.00 18.47 ? 160 SER C N   1 
ATOM   5602 C  CA  . SER C 1 160 ? 44.595  -4.485  -13.442 1.00 20.14 ? 160 SER C CA  1 
ATOM   5603 C  C   . SER C 1 160 ? 45.026  -3.094  -13.021 1.00 23.82 ? 160 SER C C   1 
ATOM   5604 O  O   . SER C 1 160 ? 45.383  -2.905  -11.860 1.00 23.38 ? 160 SER C O   1 
ATOM   5605 C  CB  . SER C 1 160 ? 45.697  -5.495  -13.286 1.00 22.38 ? 160 SER C CB  1 
ATOM   5606 O  OG  . SER C 1 160 ? 46.852  -5.152  -14.044 1.00 23.70 ? 160 SER C OG  1 
ATOM   5607 N  N   . HIS C 1 161 ? 44.959  -2.121  -13.935 1.00 18.09 ? 161 HIS C N   1 
ATOM   5608 C  CA  . HIS C 1 161 ? 45.324  -0.733  -13.683 1.00 18.58 ? 161 HIS C CA  1 
ATOM   5609 C  C   . HIS C 1 161 ? 44.134  0.216   -13.643 1.00 14.86 ? 161 HIS C C   1 
ATOM   5610 O  O   . HIS C 1 161 ? 44.303  1.431   -13.449 1.00 16.87 ? 161 HIS C O   1 
ATOM   5611 C  CB  . HIS C 1 161 ? 46.431  -0.255  -14.654 1.00 19.26 ? 161 HIS C CB  1 
ATOM   5612 C  CG  . HIS C 1 161 ? 47.701  -1.032  -14.481 1.00 24.67 ? 161 HIS C CG  1 
ATOM   5613 N  ND1 . HIS C 1 161 ? 48.770  -0.565  -13.707 1.00 29.92 ? 161 HIS C ND1 1 
ATOM   5614 C  CD2 . HIS C 1 161 ? 48.023  -2.287  -14.871 1.00 26.11 ? 161 HIS C CD2 1 
ATOM   5615 C  CE1 . HIS C 1 161 ? 49.709  -1.493  -13.670 1.00 31.27 ? 161 HIS C CE1 1 
ATOM   5616 N  NE2 . HIS C 1 161 ? 49.270  -2.566  -14.365 1.00 28.92 ? 161 HIS C NE2 1 
ATOM   5617 N  N   . LEU C 1 162 ? 42.912  -0.313  -13.893 1.00 15.72 ? 162 LEU C N   1 
ATOM   5618 C  CA  . LEU C 1 162 ? 41.811  0.600   -14.128 1.00 16.07 ? 162 LEU C CA  1 
ATOM   5619 C  C   . LEU C 1 162 ? 41.458  1.454   -12.912 1.00 13.93 ? 162 LEU C C   1 
ATOM   5620 O  O   . LEU C 1 162 ? 40.979  2.575   -13.073 1.00 13.94 ? 162 LEU C O   1 
ATOM   5621 C  CB  . LEU C 1 162 ? 40.587  -0.192  -14.616 1.00 17.35 ? 162 LEU C CB  1 
ATOM   5622 C  CG  . LEU C 1 162 ? 40.737  -0.864  -15.977 1.00 19.83 ? 162 LEU C CG  1 
ATOM   5623 C  CD1 . LEU C 1 162 ? 39.482  -1.692  -16.263 1.00 22.94 ? 162 LEU C CD1 1 
ATOM   5624 C  CD2 . LEU C 1 162 ? 40.998  0.198   -17.049 1.00 21.73 ? 162 LEU C CD2 1 
ATOM   5625 N  N   . GLN C 1 163 ? 41.706  0.906   -11.675 1.00 14.83 ? 163 GLN C N   1 
ATOM   5626 C  CA  . GLN C 1 163 ? 41.335  1.658   -10.479 1.00 17.49 ? 163 GLN C CA  1 
ATOM   5627 C  C   . GLN C 1 163 ? 42.278  2.850   -10.268 1.00 15.81 ? 163 GLN C C   1 
ATOM   5628 O  O   . GLN C 1 163 ? 42.012  3.658   -9.388  1.00 18.94 ? 163 GLN C O   1 
ATOM   5629 C  CB  . GLN C 1 163 ? 41.313  0.733   -9.249  1.00 18.19 ? 163 GLN C CB  1 
ATOM   5630 C  CG  . GLN C 1 163 ? 40.300  -0.414  -9.309  1.00 20.01 ? 163 GLN C CG  1 
ATOM   5631 C  CD  . GLN C 1 163 ? 38.865  0.050   -9.366  1.00 22.92 ? 163 GLN C CD  1 
ATOM   5632 O  OE1 . GLN C 1 163 ? 38.454  1.055   -8.783  1.00 22.47 ? 163 GLN C OE1 1 
ATOM   5633 N  NE2 . GLN C 1 163 ? 38.063  -0.669  -10.140 1.00 23.84 ? 163 GLN C NE2 1 
ATOM   5634 N  N   . HIS C 1 164 ? 43.336  3.007   -11.077 1.00 15.19 ? 164 HIS C N   1 
ATOM   5635 C  CA  . HIS C 1 164 ? 44.235  4.152   -10.985 1.00 15.71 ? 164 HIS C CA  1 
ATOM   5636 C  C   . HIS C 1 164 ? 43.827  5.300   -11.906 1.00 16.55 ? 164 HIS C C   1 
ATOM   5637 O  O   . HIS C 1 164 ? 44.429  6.378   -11.907 1.00 18.16 ? 164 HIS C O   1 
ATOM   5638 C  CB  . HIS C 1 164 ? 45.692  3.745   -11.289 1.00 17.90 ? 164 HIS C CB  1 
ATOM   5639 C  CG  . HIS C 1 164 ? 46.204  2.709   -10.349 1.00 16.00 ? 164 HIS C CG  1 
ATOM   5640 N  ND1 . HIS C 1 164 ? 46.271  2.927   -8.975  1.00 19.11 ? 164 HIS C ND1 1 
ATOM   5641 C  CD2 . HIS C 1 164 ? 46.658  1.453   -10.576 1.00 16.91 ? 164 HIS C CD2 1 
ATOM   5642 C  CE1 . HIS C 1 164 ? 46.704  1.818   -8.395  1.00 17.25 ? 164 HIS C CE1 1 
ATOM   5643 N  NE2 . HIS C 1 164 ? 46.933  0.895   -9.336  1.00 18.57 ? 164 HIS C NE2 1 
ATOM   5644 N  N   . VAL C 1 165 ? 42.850  5.022   -12.772 1.00 17.94 ? 165 VAL C N   1 
ATOM   5645 C  CA  . VAL C 1 165 ? 42.384  6.029   -13.715 1.00 16.87 ? 165 VAL C CA  1 
ATOM   5646 C  C   . VAL C 1 165 ? 40.862  6.146   -13.672 1.00 17.93 ? 165 VAL C C   1 
ATOM   5647 O  O   . VAL C 1 165 ? 40.196  6.350   -14.701 1.00 16.61 ? 165 VAL C O   1 
ATOM   5648 C  CB  . VAL C 1 165 ? 42.949  5.803   -15.129 1.00 15.77 ? 165 VAL C CB  1 
ATOM   5649 C  CG1 . VAL C 1 165 ? 44.460  5.996   -15.152 1.00 16.40 ? 165 VAL C CG1 1 
ATOM   5650 C  CG2 . VAL C 1 165 ? 42.557  4.438   -15.665 1.00 16.31 ? 165 VAL C CG2 1 
ATOM   5651 N  N   . LYS C 1 166 ? 40.284  6.078   -12.471 1.00 16.84 ? 166 LYS C N   1 
ATOM   5652 C  CA  . LYS C 1 166 ? 38.838  6.045   -12.397 1.00 17.00 ? 166 LYS C CA  1 
ATOM   5653 C  C   . LYS C 1 166 ? 38.166  7.300   -12.922 1.00 18.68 ? 166 LYS C C   1 
ATOM   5654 O  O   . LYS C 1 166 ? 36.988  7.233   -13.308 1.00 17.28 ? 166 LYS C O   1 
ATOM   5655 C  CB  . LYS C 1 166 ? 38.396  5.799   -10.946 1.00 19.71 ? 166 LYS C CB  1 
ATOM   5656 C  CG  . LYS C 1 166 ? 38.747  4.423   -10.403 1.00 21.13 ? 166 LYS C CG  1 
ATOM   5657 C  CD  . LYS C 1 166 ? 38.207  4.132   -9.018  1.00 21.49 ? 166 LYS C CD  1 
ATOM   5658 C  CE  . LYS C 1 166 ? 36.699  3.989   -8.999  1.00 23.81 ? 166 LYS C CE  1 
ATOM   5659 N  NZ  . LYS C 1 166 ? 36.278  2.685   -9.569  1.00 21.29 ? 166 LYS C NZ  1 
ATOM   5660 N  N   . TYR C 1 167 ? 38.847  8.443   -12.899 1.00 16.36 ? 167 TYR C N   1 
ATOM   5661 C  CA  . TYR C 1 167 ? 38.179  9.690   -13.234 1.00 15.70 ? 167 TYR C CA  1 
ATOM   5662 C  C   . TYR C 1 167 ? 38.770  10.295  -14.498 1.00 14.67 ? 167 TYR C C   1 
ATOM   5663 O  O   . TYR C 1 167 ? 39.952  10.098  -14.788 1.00 15.66 ? 167 TYR C O   1 
ATOM   5664 C  CB  . TYR C 1 167 ? 38.241  10.722  -12.108 1.00 17.32 ? 167 TYR C CB  1 
ATOM   5665 C  CG  . TYR C 1 167 ? 37.648  10.278  -10.796 1.00 19.95 ? 167 TYR C CG  1 
ATOM   5666 C  CD1 . TYR C 1 167 ? 36.283  10.361  -10.561 1.00 21.12 ? 167 TYR C CD1 1 
ATOM   5667 C  CD2 . TYR C 1 167 ? 38.468  9.787   -9.778  1.00 18.87 ? 167 TYR C CD2 1 
ATOM   5668 C  CE1 . TYR C 1 167 ? 35.735  9.952   -9.346  1.00 21.73 ? 167 TYR C CE1 1 
ATOM   5669 C  CE2 . TYR C 1 167 ? 37.925  9.372   -8.567  1.00 21.50 ? 167 TYR C CE2 1 
ATOM   5670 C  CZ  . TYR C 1 167 ? 36.563  9.446   -8.355  1.00 20.75 ? 167 TYR C CZ  1 
ATOM   5671 O  OH  . TYR C 1 167 ? 36.050  9.017   -7.152  1.00 23.72 ? 167 TYR C OH  1 
ATOM   5672 N  N   . LYS C 1 168 ? 37.929  11.096  -15.166 1.00 15.54 ? 168 LYS C N   1 
ATOM   5673 C  CA  . LYS C 1 168 ? 38.305  11.763  -16.390 1.00 15.62 ? 168 LYS C CA  1 
ATOM   5674 C  C   . LYS C 1 168 ? 39.600  12.536  -16.177 1.00 17.34 ? 168 LYS C C   1 
ATOM   5675 O  O   . LYS C 1 168 ? 39.736  13.361  -15.235 1.00 19.10 ? 168 LYS C O   1 
ATOM   5676 C  CB  . LYS C 1 168 ? 37.174  12.695  -16.840 1.00 16.96 ? 168 LYS C CB  1 
ATOM   5677 C  CG  . LYS C 1 168 ? 37.481  13.382  -18.163 1.00 18.93 ? 168 LYS C CG  1 
ATOM   5678 C  CD  . LYS C 1 168 ? 36.343  14.202  -18.710 1.00 20.36 ? 168 LYS C CD  1 
ATOM   5679 C  CE  . LYS C 1 168 ? 36.775  14.852  -20.005 1.00 23.43 ? 168 LYS C CE  1 
ATOM   5680 N  NZ  . LYS C 1 168 ? 35.708  15.725  -20.562 1.00 31.16 ? 168 LYS C NZ  1 
ATOM   5681 N  N   . GLY C 1 169 ? 40.527  12.365  -17.124 1.00 17.07 ? 169 GLY C N   1 
ATOM   5682 C  CA  . GLY C 1 169 ? 41.774  13.098  -17.116 1.00 19.56 ? 169 GLY C CA  1 
ATOM   5683 C  C   . GLY C 1 169 ? 42.878  12.390  -16.351 1.00 17.86 ? 169 GLY C C   1 
ATOM   5684 O  O   . GLY C 1 169 ? 44.046  12.788  -16.460 1.00 20.96 ? 169 GLY C O   1 
ATOM   5685 N  N   . GLN C 1 170 ? 42.533  11.354  -15.570 1.00 16.54 ? 170 GLN C N   1 
ATOM   5686 C  CA  . GLN C 1 170 ? 43.567  10.694  -14.802 1.00 17.19 ? 170 GLN C CA  1 
ATOM   5687 C  C   . GLN C 1 170 ? 44.429  9.805   -15.685 1.00 18.33 ? 170 GLN C C   1 
ATOM   5688 O  O   . GLN C 1 170 ? 43.949  9.199   -16.677 1.00 16.66 ? 170 GLN C O   1 
ATOM   5689 C  CB  . GLN C 1 170 ? 43.016  9.887   -13.617 1.00 16.77 ? 170 GLN C CB  1 
ATOM   5690 C  CG  . GLN C 1 170 ? 42.437  10.796  -12.542 1.00 17.85 ? 170 GLN C CG  1 
ATOM   5691 C  CD  . GLN C 1 170 ? 41.962  10.000  -11.353 1.00 18.67 ? 170 GLN C CD  1 
ATOM   5692 O  OE1 . GLN C 1 170 ? 41.376  8.918   -11.459 1.00 16.84 ? 170 GLN C OE1 1 
ATOM   5693 N  NE2 . GLN C 1 170 ? 42.197  10.551  -10.167 1.00 23.15 ? 170 GLN C NE2 1 
ATOM   5694 N  N   . GLU C 1 171 ? 45.681  9.652   -15.275 1.00 19.64 ? 171 GLU C N   1 
ATOM   5695 C  CA  . GLU C 1 171 ? 46.624  8.883   -16.064 1.00 18.94 ? 171 GLU C CA  1 
ATOM   5696 C  C   . GLU C 1 171 ? 47.425  8.012   -15.121 1.00 18.20 ? 171 GLU C C   1 
ATOM   5697 O  O   . GLU C 1 171 ? 47.643  8.377   -13.947 1.00 18.77 ? 171 GLU C O   1 
ATOM   5698 C  CB  . GLU C 1 171 ? 47.623  9.842   -16.710 1.00 20.07 ? 171 GLU C CB  1 
ATOM   5699 C  CG  . GLU C 1 171 ? 47.054  10.721  -17.822 1.00 25.58 ? 171 GLU C CG  1 
ATOM   5700 C  CD  . GLU C 1 171 ? 47.961  11.837  -18.334 1.00 28.74 ? 171 GLU C CD  1 
ATOM   5701 O  OE1 . GLU C 1 171 ? 49.103  11.959  -17.836 1.00 27.83 ? 171 GLU C OE1 1 
ATOM   5702 O  OE2 . GLU C 1 171 ? 47.515  12.572  -19.257 1.00 34.81 ? 171 GLU C OE2 1 
ATOM   5703 N  N   . ALA C 1 172 ? 47.931  6.922   -15.677 1.00 16.44 ? 172 ALA C N   1 
ATOM   5704 C  CA  . ALA C 1 172 ? 48.781  5.969   -14.988 1.00 17.98 ? 172 ALA C CA  1 
ATOM   5705 C  C   . ALA C 1 172 ? 49.647  5.261   -16.006 1.00 22.19 ? 172 ALA C C   1 
ATOM   5706 O  O   . ALA C 1 172 ? 49.468  5.405   -17.201 1.00 24.09 ? 172 ALA C O   1 
ATOM   5707 C  CB  . ALA C 1 172 ? 47.966  4.996   -14.144 1.00 22.06 ? 172 ALA C CB  1 
ATOM   5708 N  N   . PHE C 1 173 ? 50.672  4.575   -15.552 1.00 21.57 ? 173 PHE C N   1 
ATOM   5709 C  CA  . PHE C 1 173 ? 51.536  3.854   -16.466 1.00 21.54 ? 173 PHE C CA  1 
ATOM   5710 C  C   . PHE C 1 173 ? 51.282  2.358   -16.301 1.00 22.18 ? 173 PHE C C   1 
ATOM   5711 O  O   . PHE C 1 173 ? 50.933  1.896   -15.206 1.00 24.36 ? 173 PHE C O   1 
ATOM   5712 C  CB  . PHE C 1 173 ? 53.010  4.228   -16.281 1.00 21.30 ? 173 PHE C CB  1 
ATOM   5713 C  CG  . PHE C 1 173 ? 53.442  5.559   -16.851 1.00 20.93 ? 173 PHE C CG  1 
ATOM   5714 C  CD1 . PHE C 1 173 ? 53.706  5.701   -18.213 1.00 20.19 ? 173 PHE C CD1 1 
ATOM   5715 C  CD2 . PHE C 1 173 ? 53.575  6.683   -16.034 1.00 22.33 ? 173 PHE C CD2 1 
ATOM   5716 C  CE1 . PHE C 1 173 ? 54.126  6.923   -18.728 1.00 22.09 ? 173 PHE C CE1 1 
ATOM   5717 C  CE2 . PHE C 1 173 ? 53.966  7.903   -16.564 1.00 23.10 ? 173 PHE C CE2 1 
ATOM   5718 C  CZ  . PHE C 1 173 ? 54.210  8.037   -17.914 1.00 23.00 ? 173 PHE C CZ  1 
ATOM   5719 N  N   . VAL C 1 174 ? 51.332  1.666   -17.438 1.00 22.11 ? 174 VAL C N   1 
ATOM   5720 C  CA  . VAL C 1 174 ? 51.175  0.222   -17.495 1.00 24.60 ? 174 VAL C CA  1 
ATOM   5721 C  C   . VAL C 1 174 ? 52.523  -0.306  -17.972 1.00 24.16 ? 174 VAL C C   1 
ATOM   5722 O  O   . VAL C 1 174 ? 53.060  0.203   -18.944 1.00 23.23 ? 174 VAL C O   1 
ATOM   5723 C  CB  . VAL C 1 174 ? 50.077  -0.174  -18.515 1.00 23.21 ? 174 VAL C CB  1 
ATOM   5724 C  CG1 . VAL C 1 174 ? 50.155  -1.647  -18.917 1.00 26.15 ? 174 VAL C CG1 1 
ATOM   5725 C  CG2 . VAL C 1 174 ? 48.692  0.188   -18.015 1.00 29.81 ? 174 VAL C CG2 1 
ATOM   5726 N  N   . PRO C 1 175 ? 53.129  -1.335  -17.323 1.00 20.97 ? 175 PRO C N   1 
ATOM   5727 C  CA  . PRO C 1 175 ? 54.353  -1.912  -17.852 1.00 21.32 ? 175 PRO C CA  1 
ATOM   5728 C  C   . PRO C 1 175 ? 54.074  -2.542  -19.207 1.00 23.67 ? 175 PRO C C   1 
ATOM   5729 O  O   . PRO C 1 175 ? 52.964  -3.002  -19.448 1.00 22.23 ? 175 PRO C O   1 
ATOM   5730 C  CB  . PRO C 1 175 ? 54.704  -3.053  -16.861 1.00 21.12 ? 175 PRO C CB  1 
ATOM   5731 C  CG  . PRO C 1 175 ? 53.864  -2.778  -15.640 1.00 23.24 ? 175 PRO C CG  1 
ATOM   5732 C  CD  . PRO C 1 175 ? 52.666  -1.958  -16.076 1.00 21.66 ? 175 PRO C CD  1 
ATOM   5733 N  N   . GLY C 1 176 ? 55.099  -2.570  -20.044 1.00 20.55 ? 176 GLY C N   1 
ATOM   5734 C  CA  . GLY C 1 176 ? 55.065  -3.184  -21.360 1.00 23.24 ? 176 GLY C CA  1 
ATOM   5735 C  C   . GLY C 1 176 ? 54.666  -4.648  -21.285 1.00 23.45 ? 176 GLY C C   1 
ATOM   5736 O  O   . GLY C 1 176 ? 54.923  -5.329  -20.278 1.00 23.77 ? 176 GLY C O   1 
ATOM   5737 N  N   . PHE C 1 177 ? 54.074  -5.126  -22.394 1.00 22.39 ? 177 PHE C N   1 
ATOM   5738 C  CA  . PHE C 1 177 ? 53.770  -6.540  -22.577 1.00 19.63 ? 177 PHE C CA  1 
ATOM   5739 C  C   . PHE C 1 177 ? 53.579  -6.752  -24.080 1.00 19.74 ? 177 PHE C C   1 
ATOM   5740 O  O   . PHE C 1 177 ? 53.655  -5.794  -24.862 1.00 20.95 ? 177 PHE C O   1 
ATOM   5741 C  CB  . PHE C 1 177 ? 52.562  -6.947  -21.728 1.00 20.56 ? 177 PHE C CB  1 
ATOM   5742 C  CG  . PHE C 1 177 ? 51.218  -6.414  -22.188 1.00 21.30 ? 177 PHE C CG  1 
ATOM   5743 C  CD1 . PHE C 1 177 ? 50.813  -5.144  -21.787 1.00 21.06 ? 177 PHE C CD1 1 
ATOM   5744 C  CD2 . PHE C 1 177 ? 50.335  -7.184  -22.937 1.00 23.25 ? 177 PHE C CD2 1 
ATOM   5745 C  CE1 . PHE C 1 177 ? 49.578  -4.629  -22.163 1.00 25.51 ? 177 PHE C CE1 1 
ATOM   5746 C  CE2 . PHE C 1 177 ? 49.100  -6.658  -23.322 1.00 23.26 ? 177 PHE C CE2 1 
ATOM   5747 C  CZ  . PHE C 1 177 ? 48.732  -5.393  -22.935 1.00 24.16 ? 177 PHE C CZ  1 
ATOM   5748 N  N   . ASN C 1 178 ? 53.391  -8.009  -24.480 1.00 18.66 ? 178 ASN C N   1 
ATOM   5749 C  CA  . ASN C 1 178 ? 53.232  -8.329  -25.890 1.00 18.65 ? 178 ASN C CA  1 
ATOM   5750 C  C   . ASN C 1 178 ? 51.777  -8.071  -26.331 1.00 16.92 ? 178 ASN C C   1 
ATOM   5751 O  O   . ASN C 1 178 ? 50.862  -8.792  -25.989 1.00 17.66 ? 178 ASN C O   1 
ATOM   5752 C  CB  . ASN C 1 178 ? 53.707  -9.757  -26.136 1.00 18.86 ? 178 ASN C CB  1 
ATOM   5753 C  CG  . ASN C 1 178 ? 53.577  -10.173 -27.579 1.00 21.60 ? 178 ASN C CG  1 
ATOM   5754 O  OD1 . ASN C 1 178 ? 53.375  -9.334  -28.451 1.00 21.53 ? 178 ASN C OD1 1 
ATOM   5755 N  ND2 . ASN C 1 178 ? 53.757  -11.450 -27.850 1.00 23.55 ? 178 ASN C ND2 1 
ATOM   5756 N  N   . ILE C 1 179 ? 51.608  -6.992  -27.115 1.00 17.12 ? 179 ILE C N   1 
ATOM   5757 C  CA  . ILE C 1 179 ? 50.271  -6.550  -27.520 1.00 16.27 ? 179 ILE C CA  1 
ATOM   5758 C  C   . ILE C 1 179 ? 49.618  -7.614  -28.401 1.00 17.76 ? 179 ILE C C   1 
ATOM   5759 O  O   . ILE C 1 179 ? 48.389  -7.707  -28.474 1.00 16.44 ? 179 ILE C O   1 
ATOM   5760 C  CB  . ILE C 1 179 ? 50.386  -5.180  -28.188 1.00 16.81 ? 179 ILE C CB  1 
ATOM   5761 C  CG1 . ILE C 1 179 ? 51.057  -4.161  -27.267 1.00 17.61 ? 179 ILE C CG1 1 
ATOM   5762 C  CG2 . ILE C 1 179 ? 49.017  -4.703  -28.644 1.00 16.73 ? 179 ILE C CG2 1 
ATOM   5763 C  CD1 . ILE C 1 179 ? 50.321  -3.943  -25.953 1.00 19.39 ? 179 ILE C CD1 1 
ATOM   5764 N  N   . GLU C 1 180 ? 50.434  -8.425  -29.058 1.00 16.50 ? 180 GLU C N   1 
ATOM   5765 C  CA  . GLU C 1 180 ? 49.906  -9.457  -29.936 1.00 18.36 ? 180 GLU C CA  1 
ATOM   5766 C  C   . GLU C 1 180 ? 49.100  -10.482 -29.138 1.00 19.38 ? 180 GLU C C   1 
ATOM   5767 O  O   . GLU C 1 180 ? 48.283  -11.181 -29.714 1.00 19.11 ? 180 GLU C O   1 
ATOM   5768 C  CB  . GLU C 1 180 ? 51.015  -10.066 -30.785 1.00 19.94 ? 180 GLU C CB  1 
ATOM   5769 C  CG  . GLU C 1 180 ? 50.483  -10.783 -32.001 1.00 22.15 ? 180 GLU C CG  1 
ATOM   5770 C  CD  . GLU C 1 180 ? 51.535  -11.358 -32.924 1.00 25.56 ? 180 GLU C CD  1 
ATOM   5771 O  OE1 . GLU C 1 180 ? 52.732  -11.084 -32.706 1.00 25.88 ? 180 GLU C OE1 1 
ATOM   5772 O  OE2 . GLU C 1 180 ? 51.132  -12.081 -33.837 1.00 27.39 ? 180 GLU C OE2 1 
ATOM   5773 N  N   . GLU C 1 181 ? 49.289  -10.536 -27.812 1.00 16.87 ? 181 GLU C N   1 
ATOM   5774 C  CA  . GLU C 1 181 ? 48.535  -11.438 -26.954 1.00 19.47 ? 181 GLU C CA  1 
ATOM   5775 C  C   . GLU C 1 181 ? 47.059  -11.026 -26.863 1.00 17.23 ? 181 GLU C C   1 
ATOM   5776 O  O   . GLU C 1 181 ? 46.255  -11.808 -26.387 1.00 17.85 ? 181 GLU C O   1 
ATOM   5777 C  CB  . GLU C 1 181 ? 49.127  -11.437 -25.543 1.00 21.95 ? 181 GLU C CB  1 
ATOM   5778 C  CG  . GLU C 1 181 ? 50.425  -12.228 -25.393 1.00 24.19 ? 181 GLU C CG  1 
ATOM   5779 C  CD  . GLU C 1 181 ? 51.050  -12.020 -24.009 1.00 26.74 ? 181 GLU C CD  1 
ATOM   5780 O  OE1 . GLU C 1 181 ? 50.317  -11.685 -23.041 1.00 26.66 ? 181 GLU C OE1 1 
ATOM   5781 O  OE2 . GLU C 1 181 ? 52.300  -12.168 -23.879 1.00 30.39 ? 181 GLU C OE2 1 
ATOM   5782 N  N   . LEU C 1 182 ? 46.739  -9.778  -27.262 1.00 15.54 ? 182 LEU C N   1 
ATOM   5783 C  CA  . LEU C 1 182 ? 45.358  -9.286  -27.251 1.00 15.11 ? 182 LEU C CA  1 
ATOM   5784 C  C   . LEU C 1 182 ? 44.577  -9.736  -28.484 1.00 15.30 ? 182 LEU C C   1 
ATOM   5785 O  O   . LEU C 1 182 ? 43.352  -9.614  -28.513 1.00 15.40 ? 182 LEU C O   1 
ATOM   5786 C  CB  . LEU C 1 182 ? 45.386  -7.757  -27.126 1.00 15.79 ? 182 LEU C CB  1 
ATOM   5787 C  CG  . LEU C 1 182 ? 46.121  -7.178  -25.918 1.00 14.78 ? 182 LEU C CG  1 
ATOM   5788 C  CD1 . LEU C 1 182 ? 46.041  -5.658  -25.939 1.00 15.86 ? 182 LEU C CD1 1 
ATOM   5789 C  CD2 . LEU C 1 182 ? 45.606  -7.699  -24.565 1.00 14.62 ? 182 LEU C CD2 1 
ATOM   5790 N  N   . LEU C 1 183 ? 45.285  -10.222 -29.499 1.00 15.23 ? 183 LEU C N   1 
ATOM   5791 C  CA  . LEU C 1 183 ? 44.669  -10.607 -30.752 1.00 15.25 ? 183 LEU C CA  1 
ATOM   5792 C  C   . LEU C 1 183 ? 44.117  -12.021 -30.621 1.00 18.38 ? 183 LEU C C   1 
ATOM   5793 O  O   . LEU C 1 183 ? 44.599  -12.845 -29.810 1.00 18.29 ? 183 LEU C O   1 
ATOM   5794 C  CB  . LEU C 1 183 ? 45.664  -10.514 -31.913 1.00 16.74 ? 183 LEU C CB  1 
ATOM   5795 C  CG  . LEU C 1 183 ? 46.295  -9.143  -32.087 1.00 16.65 ? 183 LEU C CG  1 
ATOM   5796 C  CD1 . LEU C 1 183 ? 47.133  -9.141  -33.348 1.00 19.94 ? 183 LEU C CD1 1 
ATOM   5797 C  CD2 . LEU C 1 183 ? 45.281  -8.028  -32.158 1.00 19.90 ? 183 LEU C CD2 1 
ATOM   5798 N  N   . PRO C 1 184 ? 43.083  -12.359 -31.412 1.00 15.52 ? 184 PRO C N   1 
ATOM   5799 C  CA  . PRO C 1 184 ? 42.466  -13.672 -31.346 1.00 18.22 ? 184 PRO C CA  1 
ATOM   5800 C  C   . PRO C 1 184 ? 43.243  -14.724 -32.124 1.00 18.72 ? 184 PRO C C   1 
ATOM   5801 O  O   . PRO C 1 184 ? 44.280  -14.464 -32.722 1.00 19.23 ? 184 PRO C O   1 
ATOM   5802 C  CB  . PRO C 1 184 ? 41.107  -13.448 -32.033 1.00 18.82 ? 184 PRO C CB  1 
ATOM   5803 C  CG  . PRO C 1 184 ? 41.352  -12.324 -33.021 1.00 17.62 ? 184 PRO C CG  1 
ATOM   5804 C  CD  . PRO C 1 184 ? 42.420  -11.470 -32.387 1.00 14.61 ? 184 PRO C CD  1 
ATOM   5805 N  N   . GLU C 1 185 ? 42.721  -15.954 -32.062 1.00 22.19 ? 185 GLU C N   1 
ATOM   5806 C  CA  . GLU C 1 185 ? 43.175  -17.033 -32.912 1.00 22.25 ? 185 GLU C CA  1 
ATOM   5807 C  C   . GLU C 1 185 ? 42.892  -16.736 -34.386 1.00 21.66 ? 185 GLU C C   1 
ATOM   5808 O  O   . GLU C 1 185 ? 41.882  -16.094 -34.773 1.00 20.04 ? 185 GLU C O   1 
ATOM   5809 C  CB  . GLU C 1 185 ? 42.409  -18.320 -32.586 1.00 27.51 ? 185 GLU C CB  1 
ATOM   5810 C  CG  . GLU C 1 185 ? 42.606  -18.795 -31.161 1.00 32.20 ? 185 GLU C CG  1 
ATOM   5811 C  CD  . GLU C 1 185 ? 44.052  -19.107 -30.851 1.00 42.01 ? 185 GLU C CD  1 
ATOM   5812 O  OE1 . GLU C 1 185 ? 44.682  -19.872 -31.623 1.00 42.83 ? 185 GLU C OE1 1 
ATOM   5813 O  OE2 . GLU C 1 185 ? 44.551  -18.567 -29.855 1.00 48.88 ? 185 GLU C OE2 1 
ATOM   5814 N  N   A ARG C 1 186 ? 43.766  -17.279 -35.237 0.50 20.63 ? 186 ARG C N   1 
ATOM   5815 N  N   B ARG C 1 186 ? 43.856  -17.154 -35.211 0.50 19.77 ? 186 ARG C N   1 
ATOM   5816 C  CA  A ARG C 1 186 ? 43.638  -17.213 -36.683 0.50 20.42 ? 186 ARG C CA  1 
ATOM   5817 C  CA  B ARG C 1 186 ? 43.699  -17.220 -36.654 0.50 19.63 ? 186 ARG C CA  1 
ATOM   5818 C  C   A ARG C 1 186 ? 43.410  -15.774 -37.143 0.50 17.75 ? 186 ARG C C   1 
ATOM   5819 C  C   B ARG C 1 186 ? 43.483  -15.822 -37.231 0.50 16.96 ? 186 ARG C C   1 
ATOM   5820 O  O   A ARG C 1 186 ? 42.392  -15.444 -37.792 0.50 19.33 ? 186 ARG C O   1 
ATOM   5821 O  O   B ARG C 1 186 ? 42.552  -15.566 -38.029 0.50 17.21 ? 186 ARG C O   1 
ATOM   5822 C  CB  A ARG C 1 186 ? 42.568  -18.171 -37.200 0.50 21.35 ? 186 ARG C CB  1 
ATOM   5823 C  CB  B ARG C 1 186 ? 42.605  -18.221 -37.009 0.50 20.31 ? 186 ARG C CB  1 
ATOM   5824 C  CG  A ARG C 1 186 ? 42.995  -19.631 -37.125 0.50 23.48 ? 186 ARG C CG  1 
ATOM   5825 C  CG  B ARG C 1 186 ? 42.880  -19.611 -36.446 0.50 22.17 ? 186 ARG C CG  1 
ATOM   5826 C  CD  A ARG C 1 186 ? 41.860  -20.596 -37.415 0.50 24.10 ? 186 ARG C CD  1 
ATOM   5827 C  CD  B ARG C 1 186 ? 41.748  -20.590 -36.703 0.50 23.28 ? 186 ARG C CD  1 
ATOM   5828 N  NE  A ARG C 1 186 ? 40.636  -20.270 -36.680 0.50 26.38 ? 186 ARG C NE  1 
ATOM   5829 N  NE  B ARG C 1 186 ? 40.757  -20.623 -35.635 0.50 24.33 ? 186 ARG C NE  1 
ATOM   5830 C  CZ  A ARG C 1 186 ? 39.434  -20.790 -36.925 0.50 28.27 ? 186 ARG C CZ  1 
ATOM   5831 C  CZ  B ARG C 1 186 ? 41.005  -21.081 -34.414 0.50 24.09 ? 186 ARG C CZ  1 
ATOM   5832 N  NH1 A ARG C 1 186 ? 39.275  -21.684 -37.888 0.50 28.02 ? 186 ARG C NH1 1 
ATOM   5833 N  NH1 B ARG C 1 186 ? 42.210  -21.540 -34.127 0.50 24.94 ? 186 ARG C NH1 1 
ATOM   5834 N  NH2 A ARG C 1 186 ? 38.398  -20.430 -36.190 0.50 30.64 ? 186 ARG C NH2 1 
ATOM   5835 N  NH2 B ARG C 1 186 ? 40.060  -21.074 -33.489 0.50 28.07 ? 186 ARG C NH2 1 
ATOM   5836 N  N   . THR C 1 187 ? 44.406  -14.940 -36.858 1.00 17.17 ? 187 THR C N   1 
ATOM   5837 C  CA  . THR C 1 187 ? 44.394  -13.573 -37.362 1.00 17.28 ? 187 THR C CA  1 
ATOM   5838 C  C   . THR C 1 187 ? 44.320  -13.495 -38.885 1.00 17.54 ? 187 THR C C   1 
ATOM   5839 O  O   . THR C 1 187 ? 43.943  -12.443 -39.368 1.00 16.54 ? 187 THR C O   1 
ATOM   5840 C  CB  . THR C 1 187 ? 45.463  -12.672 -36.748 1.00 17.87 ? 187 THR C CB  1 
ATOM   5841 O  OG1 . THR C 1 187 ? 46.730  -13.290 -36.939 1.00 21.89 ? 187 THR C OG1 1 
ATOM   5842 C  CG2 . THR C 1 187 ? 45.205  -12.430 -35.272 1.00 18.92 ? 187 THR C CG2 1 
ATOM   5843 N  N   . ALA C 1 188 ? 44.711  -14.545 -39.624 1.00 16.82 ? 188 ALA C N   1 
ATOM   5844 C  CA  . ALA C 1 188 ? 44.571  -14.508 -41.073 1.00 16.72 ? 188 ALA C CA  1 
ATOM   5845 C  C   . ALA C 1 188 ? 43.111  -14.372 -41.530 1.00 15.88 ? 188 ALA C C   1 
ATOM   5846 O  O   . ALA C 1 188 ? 42.876  -14.015 -42.685 1.00 16.11 ? 188 ALA C O   1 
ATOM   5847 C  CB  . ALA C 1 188 ? 45.213  -15.760 -41.656 1.00 18.92 ? 188 ALA C CB  1 
ATOM   5848 N  N   . GLU C 1 189 ? 42.140  -14.677 -40.652 1.00 16.35 ? 189 GLU C N   1 
ATOM   5849 C  CA  . GLU C 1 189 ? 40.716  -14.581 -40.955 1.00 15.63 ? 189 GLU C CA  1 
ATOM   5850 C  C   . GLU C 1 189 ? 40.138  -13.243 -40.474 1.00 13.32 ? 189 GLU C C   1 
ATOM   5851 O  O   . GLU C 1 189 ? 40.084  -12.996 -39.270 1.00 13.88 ? 189 GLU C O   1 
ATOM   5852 C  CB  . GLU C 1 189 ? 39.927  -15.691 -40.265 1.00 18.94 ? 189 GLU C CB  1 
ATOM   5853 C  CG  . GLU C 1 189 ? 40.297  -17.069 -40.820 1.00 22.14 ? 189 GLU C CG  1 
ATOM   5854 C  CD  . GLU C 1 189 ? 39.860  -18.238 -39.942 1.00 28.40 ? 189 GLU C CD  1 
ATOM   5855 O  OE1 . GLU C 1 189 ? 38.879  -18.099 -39.159 1.00 29.58 ? 189 GLU C OE1 1 
ATOM   5856 O  OE2 . GLU C 1 189 ? 40.508  -19.303 -40.021 1.00 31.38 ? 189 GLU C OE2 1 
ATOM   5857 N  N   . TYR C 1 190 ? 39.792  -12.375 -41.427 1.00 12.00 ? 190 TYR C N   1 
ATOM   5858 C  CA  . TYR C 1 190 ? 39.295  -11.068 -41.028 1.00 12.30 ? 190 TYR C CA  1 
ATOM   5859 C  C   . TYR C 1 190 ? 38.351  -10.503 -42.087 1.00 12.00 ? 190 TYR C C   1 
ATOM   5860 O  O   . TYR C 1 190 ? 38.331  -10.908 -43.241 1.00 12.32 ? 190 TYR C O   1 
ATOM   5861 C  CB  . TYR C 1 190 ? 40.467  -10.102 -40.792 1.00 12.25 ? 190 TYR C CB  1 
ATOM   5862 C  CG  . TYR C 1 190 ? 41.429  -9.934  -41.951 1.00 12.20 ? 190 TYR C CG  1 
ATOM   5863 C  CD1 . TYR C 1 190 ? 41.195  -9.006  -42.970 1.00 12.04 ? 190 TYR C CD1 1 
ATOM   5864 C  CD2 . TYR C 1 190 ? 42.607  -10.683 -42.021 1.00 13.87 ? 190 TYR C CD2 1 
ATOM   5865 C  CE1 . TYR C 1 190 ? 42.088  -8.827  -44.027 1.00 13.43 ? 190 TYR C CE1 1 
ATOM   5866 C  CE2 . TYR C 1 190 ? 43.513  -10.502 -43.062 1.00 13.03 ? 190 TYR C CE2 1 
ATOM   5867 C  CZ  . TYR C 1 190 ? 43.223  -9.613  -44.092 1.00 14.05 ? 190 TYR C CZ  1 
ATOM   5868 O  OH  . TYR C 1 190 ? 44.113  -9.355  -45.099 1.00 13.74 ? 190 TYR C OH  1 
ATOM   5869 N  N   . TYR C 1 191 ? 37.564  -9.511  -41.646 1.00 11.00 ? 191 TYR C N   1 
ATOM   5870 C  CA  . TYR C 1 191 ? 36.771  -8.647  -42.484 1.00 10.77 ? 191 TYR C CA  1 
ATOM   5871 C  C   . TYR C 1 191 ? 37.522  -7.352  -42.733 1.00 10.22 ? 191 TYR C C   1 
ATOM   5872 O  O   . TYR C 1 191 ? 38.247  -6.880  -41.832 1.00 11.08 ? 191 TYR C O   1 
ATOM   5873 C  CB  . TYR C 1 191 ? 35.531  -8.241  -41.708 1.00 10.79 ? 191 TYR C CB  1 
ATOM   5874 C  CG  . TYR C 1 191 ? 34.666  -9.364  -41.181 1.00 10.29 ? 191 TYR C CG  1 
ATOM   5875 C  CD1 . TYR C 1 191 ? 33.638  -9.949  -41.934 1.00 11.07 ? 191 TYR C CD1 1 
ATOM   5876 C  CD2 . TYR C 1 191 ? 34.818  -9.795  -39.859 1.00 11.36 ? 191 TYR C CD2 1 
ATOM   5877 C  CE1 . TYR C 1 191 ? 32.838  -10.950 -41.388 1.00 12.89 ? 191 TYR C CE1 1 
ATOM   5878 C  CE2 . TYR C 1 191 ? 34.020  -10.768 -39.291 1.00 11.65 ? 191 TYR C CE2 1 
ATOM   5879 C  CZ  . TYR C 1 191 ? 33.021  -11.339 -40.064 1.00 13.06 ? 191 TYR C CZ  1 
ATOM   5880 O  OH  . TYR C 1 191 ? 32.182  -12.313 -39.552 1.00 16.55 ? 191 TYR C OH  1 
ATOM   5881 N  N   . ARG C 1 192 ? 37.353  -6.799  -43.934 1.00 10.99 ? 192 ARG C N   1 
ATOM   5882 C  CA  . ARG C 1 192 ? 38.042  -5.565  -44.332 1.00 10.52 ? 192 ARG C CA  1 
ATOM   5883 C  C   . ARG C 1 192 ? 37.072  -4.624  -45.022 1.00 10.07 ? 192 ARG C C   1 
ATOM   5884 O  O   . ARG C 1 192 ? 36.338  -5.028  -45.948 1.00 9.86  ? 192 ARG C O   1 
ATOM   5885 C  CB  . ARG C 1 192 ? 39.110  -5.939  -45.345 1.00 10.97 ? 192 ARG C CB  1 
ATOM   5886 C  CG  . ARG C 1 192 ? 39.773  -4.780  -46.077 1.00 10.79 ? 192 ARG C CG  1 
ATOM   5887 C  CD  . ARG C 1 192 ? 40.558  -3.802  -45.220 1.00 11.41 ? 192 ARG C CD  1 
ATOM   5888 N  NE  . ARG C 1 192 ? 41.534  -4.408  -44.337 1.00 12.65 ? 192 ARG C NE  1 
ATOM   5889 C  CZ  . ARG C 1 192 ? 42.692  -4.975  -44.707 1.00 13.55 ? 192 ARG C CZ  1 
ATOM   5890 N  NH1 . ARG C 1 192 ? 43.062  -4.909  -45.987 1.00 14.26 ? 192 ARG C NH1 1 
ATOM   5891 N  NH2 . ARG C 1 192 ? 43.461  -5.554  -43.791 1.00 13.67 ? 192 ARG C NH2 1 
ATOM   5892 N  N   . TYR C 1 193 ? 37.055  -3.364  -44.602 1.00 8.82  ? 193 TYR C N   1 
ATOM   5893 C  CA  . TYR C 1 193 ? 36.300  -2.355  -45.367 1.00 9.25  ? 193 TYR C CA  1 
ATOM   5894 C  C   . TYR C 1 193 ? 36.897  -0.991  -45.085 1.00 8.92  ? 193 TYR C C   1 
ATOM   5895 O  O   . TYR C 1 193 ? 37.563  -0.776  -44.039 1.00 9.03  ? 193 TYR C O   1 
ATOM   5896 C  CB  . TYR C 1 193 ? 34.784  -2.382  -45.058 1.00 9.02  ? 193 TYR C CB  1 
ATOM   5897 C  CG  . TYR C 1 193 ? 34.384  -1.872  -43.694 1.00 8.03  ? 193 TYR C CG  1 
ATOM   5898 C  CD1 . TYR C 1 193 ? 34.572  -2.618  -42.546 1.00 8.02  ? 193 TYR C CD1 1 
ATOM   5899 C  CD2 . TYR C 1 193 ? 33.877  -0.600  -43.577 1.00 8.65  ? 193 TYR C CD2 1 
ATOM   5900 C  CE1 . TYR C 1 193 ? 34.242  -2.091  -41.298 1.00 8.15  ? 193 TYR C CE1 1 
ATOM   5901 C  CE2 . TYR C 1 193 ? 33.509  -0.057  -42.340 1.00 8.45  ? 193 TYR C CE2 1 
ATOM   5902 C  CZ  . TYR C 1 193 ? 33.690  -0.828  -41.199 1.00 8.48  ? 193 TYR C CZ  1 
ATOM   5903 O  OH  . TYR C 1 193 ? 33.356  -0.274  -39.991 1.00 8.69  ? 193 TYR C OH  1 
ATOM   5904 N  N   . ARG C 1 194 ? 36.548  -0.016  -45.942 1.00 10.10 ? 194 ARG C N   1 
ATOM   5905 C  CA  . ARG C 1 194 ? 36.939  1.370   -45.707 1.00 10.35 ? 194 ARG C CA  1 
ATOM   5906 C  C   . ARG C 1 194 ? 35.852  2.103   -44.950 1.00 10.75 ? 194 ARG C C   1 
ATOM   5907 O  O   . ARG C 1 194 ? 34.674  2.087   -45.333 1.00 11.14 ? 194 ARG C O   1 
ATOM   5908 C  CB  . ARG C 1 194 ? 37.123  2.124   -47.042 1.00 13.01 ? 194 ARG C CB  1 
ATOM   5909 C  CG  . ARG C 1 194 ? 38.280  1.544   -47.845 1.00 17.30 ? 194 ARG C CG  1 
ATOM   5910 C  CD  . ARG C 1 194 ? 38.745  2.230   -49.142 1.00 31.01 ? 194 ARG C CD  1 
ATOM   5911 N  NE  . ARG C 1 194 ? 40.062  1.611   -49.444 1.00 37.92 ? 194 ARG C NE  1 
ATOM   5912 C  CZ  . ARG C 1 194 ? 41.280  1.990   -48.996 1.00 43.24 ? 194 ARG C CZ  1 
ATOM   5913 N  NH1 . ARG C 1 194 ? 41.447  3.064   -48.231 1.00 41.49 ? 194 ARG C NH1 1 
ATOM   5914 N  NH2 . ARG C 1 194 ? 42.348  1.284   -49.336 1.00 44.87 ? 194 ARG C NH2 1 
ATOM   5915 N  N   . GLY C 1 195 ? 36.224  2.698   -43.817 1.00 8.86  ? 195 GLY C N   1 
ATOM   5916 C  CA  . GLY C 1 195 ? 35.274  3.396   -42.965 1.00 9.37  ? 195 GLY C CA  1 
ATOM   5917 C  C   . GLY C 1 195 ? 35.827  4.633   -42.304 1.00 8.85  ? 195 GLY C C   1 
ATOM   5918 O  O   . GLY C 1 195 ? 36.686  5.348   -42.860 1.00 9.06  ? 195 GLY C O   1 
ATOM   5919 N  N   . SER C 1 196 ? 35.377  4.827   -41.052 1.00 8.41  ? 196 SER C N   1 
ATOM   5920 C  CA  . SER C 1 196 ? 35.620  6.093   -40.369 1.00 8.46  ? 196 SER C CA  1 
ATOM   5921 C  C   . SER C 1 196 ? 36.076  5.849   -38.937 1.00 8.92  ? 196 SER C C   1 
ATOM   5922 O  O   . SER C 1 196 ? 35.950  4.734   -38.423 1.00 8.86  ? 196 SER C O   1 
ATOM   5923 C  CB  . SER C 1 196 ? 34.404  6.971   -40.405 1.00 8.93  ? 196 SER C CB  1 
ATOM   5924 O  OG  . SER C 1 196 ? 33.441  6.533   -39.454 1.00 8.51  ? 196 SER C OG  1 
ATOM   5925 N  N   . LEU C 1 197 ? 36.556  6.906   -38.291 1.00 8.75  ? 197 LEU C N   1 
ATOM   5926 C  CA  . LEU C 1 197 ? 36.569  6.861   -36.826 1.00 9.10  ? 197 LEU C CA  1 
ATOM   5927 C  C   . LEU C 1 197 ? 35.138  6.621   -36.358 1.00 8.40  ? 197 LEU C C   1 
ATOM   5928 O  O   . LEU C 1 197 ? 34.201  7.229   -36.910 1.00 8.77  ? 197 LEU C O   1 
ATOM   5929 C  CB  . LEU C 1 197 ? 37.114  8.154   -36.194 1.00 10.82 ? 197 LEU C CB  1 
ATOM   5930 C  CG  . LEU C 1 197 ? 38.615  8.444   -36.293 1.00 11.91 ? 197 LEU C CG  1 
ATOM   5931 C  CD1 . LEU C 1 197 ? 39.009  8.961   -37.657 1.00 13.45 ? 197 LEU C CD1 1 
ATOM   5932 C  CD2 . LEU C 1 197 ? 38.932  9.496   -35.259 1.00 14.66 ? 197 LEU C CD2 1 
ATOM   5933 N  N   . THR C 1 198 ? 34.994  5.887   -35.256 1.00 9.08  ? 198 THR C N   1 
ATOM   5934 C  CA  . THR C 1 198 ? 33.684  5.704   -34.667 1.00 8.81  ? 198 THR C CA  1 
ATOM   5935 C  C   . THR C 1 198 ? 33.385  6.710   -33.565 1.00 9.59  ? 198 THR C C   1 
ATOM   5936 O  O   . THR C 1 198 ? 32.316  6.695   -32.961 1.00 9.31  ? 198 THR C O   1 
ATOM   5937 C  CB  . THR C 1 198 ? 33.460  4.311   -34.082 1.00 8.51  ? 198 THR C CB  1 
ATOM   5938 O  OG1 . THR C 1 198 ? 34.367  4.219   -32.966 1.00 9.26  ? 198 THR C OG1 1 
ATOM   5939 C  CG2 . THR C 1 198 ? 33.805  3.197   -35.048 1.00 8.99  ? 198 THR C CG2 1 
ATOM   5940 N  N   . THR C 1 199 ? 34.356  7.593   -33.320 1.00 9.94  ? 199 THR C N   1 
ATOM   5941 C  CA  . THR C 1 199 ? 34.161  8.715   -32.427 1.00 9.30  ? 199 THR C CA  1 
ATOM   5942 C  C   . THR C 1 199 ? 34.367  10.012  -33.204 1.00 10.17 ? 199 THR C C   1 
ATOM   5943 O  O   . THR C 1 199 ? 35.047  9.991   -34.226 1.00 10.27 ? 199 THR C O   1 
ATOM   5944 C  CB  . THR C 1 199 ? 35.182  8.737   -31.278 1.00 10.25 ? 199 THR C CB  1 
ATOM   5945 O  OG1 . THR C 1 199 ? 36.488  8.907   -31.831 1.00 11.82 ? 199 THR C OG1 1 
ATOM   5946 C  CG2 . THR C 1 199 ? 35.182  7.417   -30.530 1.00 11.15 ? 199 THR C CG2 1 
ATOM   5947 N  N   . PRO C 1 200 ? 33.914  11.170  -32.678 1.00 9.81  ? 200 PRO C N   1 
ATOM   5948 C  CA  . PRO C 1 200 ? 34.335  12.441  -33.300 1.00 10.25 ? 200 PRO C CA  1 
ATOM   5949 C  C   . PRO C 1 200 ? 35.854  12.441  -33.433 1.00 11.38 ? 200 PRO C C   1 
ATOM   5950 O  O   . PRO C 1 200 ? 36.564  11.883  -32.558 1.00 12.06 ? 200 PRO C O   1 
ATOM   5951 C  CB  . PRO C 1 200 ? 33.861  13.491  -32.281 1.00 10.56 ? 200 PRO C CB  1 
ATOM   5952 C  CG  . PRO C 1 200 ? 32.614  12.840  -31.695 1.00 10.45 ? 200 PRO C CG  1 
ATOM   5953 C  CD  . PRO C 1 200 ? 32.976  11.378  -31.554 1.00 10.10 ? 200 PRO C CD  1 
ATOM   5954 N  N   . PRO C 1 201 ? 36.409  13.055  -34.493 1.00 10.57 ? 201 PRO C N   1 
ATOM   5955 C  CA  . PRO C 1 201 ? 35.629  13.762  -35.538 1.00 11.01 ? 201 PRO C CA  1 
ATOM   5956 C  C   . PRO C 1 201 ? 35.070  12.933  -36.701 1.00 9.18  ? 201 PRO C C   1 
ATOM   5957 O  O   . PRO C 1 201 ? 34.574  13.464  -37.687 1.00 10.70 ? 201 PRO C O   1 
ATOM   5958 C  CB  . PRO C 1 201 ? 36.628  14.785  -36.127 1.00 11.27 ? 201 PRO C CB  1 
ATOM   5959 C  CG  . PRO C 1 201 ? 37.795  14.748  -35.146 1.00 12.95 ? 201 PRO C CG  1 
ATOM   5960 C  CD  . PRO C 1 201 ? 37.857  13.332  -34.577 1.00 12.15 ? 201 PRO C CD  1 
ATOM   5961 N  N   . CYS C 1 202 ? 35.089  11.601  -36.566 1.00 8.86  ? 202 CYS C N   1 
ATOM   5962 C  CA  . CYS C 1 202 ? 34.390  10.681  -37.478 1.00 9.49  ? 202 CYS C CA  1 
ATOM   5963 C  C   . CYS C 1 202 ? 34.975  10.732  -38.885 1.00 9.50  ? 202 CYS C C   1 
ATOM   5964 O  O   . CYS C 1 202 ? 34.281  10.433  -39.844 1.00 9.81  ? 202 CYS C O   1 
ATOM   5965 C  CB  . CYS C 1 202 ? 32.871  10.931  -37.595 1.00 10.23 ? 202 CYS C CB  1 
ATOM   5966 S  SG  . CYS C 1 202 ? 31.997  10.869  -36.013 1.00 10.03 ? 202 CYS C SG  1 
ATOM   5967 N  N   . ASN C 1 203 ? 36.256  11.105  -39.035 1.00 10.29 ? 203 ASN C N   1 
ATOM   5968 C  CA  . ASN C 1 203 ? 36.800  11.256  -40.375 1.00 10.43 ? 203 ASN C CA  1 
ATOM   5969 C  C   . ASN C 1 203 ? 36.753  9.927   -41.135 1.00 10.71 ? 203 ASN C C   1 
ATOM   5970 O  O   . ASN C 1 203 ? 37.026  8.863   -40.524 1.00 10.17 ? 203 ASN C O   1 
ATOM   5971 C  CB  . ASN C 1 203 ? 38.263  11.726  -40.303 1.00 12.07 ? 203 ASN C CB  1 
ATOM   5972 C  CG  . ASN C 1 203 ? 38.412  12.913  -39.381 1.00 13.28 ? 203 ASN C CG  1 
ATOM   5973 O  OD1 . ASN C 1 203 ? 38.503  12.762  -38.175 1.00 15.16 ? 203 ASN C OD1 1 
ATOM   5974 N  ND2 . ASN C 1 203 ? 38.309  14.100  -39.946 1.00 15.73 ? 203 ASN C ND2 1 
ATOM   5975 N  N   . PRO C 1 204 ? 36.440  9.958   -42.455 1.00 10.25 ? 204 PRO C N   1 
ATOM   5976 C  CA  . PRO C 1 204 ? 36.293  8.733   -43.258 1.00 11.16 ? 204 PRO C CA  1 
ATOM   5977 C  C   . PRO C 1 204 ? 37.649  8.256   -43.766 1.00 10.60 ? 204 PRO C C   1 
ATOM   5978 O  O   . PRO C 1 204 ? 37.854  8.080   -44.972 1.00 12.89 ? 204 PRO C O   1 
ATOM   5979 C  CB  . PRO C 1 204 ? 35.368  9.220   -44.394 1.00 11.67 ? 204 PRO C CB  1 
ATOM   5980 C  CG  . PRO C 1 204 ? 35.754  10.691  -44.594 1.00 10.89 ? 204 PRO C CG  1 
ATOM   5981 C  CD  . PRO C 1 204 ? 35.986  11.192  -43.172 1.00 11.84 ? 204 PRO C CD  1 
ATOM   5982 N  N   . THR C 1 205 ? 38.554  8.010   -42.808 1.00 9.69  ? 205 THR C N   1 
ATOM   5983 C  CA  . THR C 1 205 ? 39.947  7.846   -43.160 1.00 11.54 ? 205 THR C CA  1 
ATOM   5984 C  C   . THR C 1 205 ? 40.529  6.560   -42.583 1.00 11.32 ? 205 THR C C   1 
ATOM   5985 O  O   . THR C 1 205 ? 41.760  6.382   -42.513 1.00 12.05 ? 205 THR C O   1 
ATOM   5986 C  CB  . THR C 1 205 ? 40.754  9.014   -42.593 1.00 10.82 ? 205 THR C CB  1 
ATOM   5987 O  OG1 . THR C 1 205 ? 40.499  9.042   -41.189 1.00 12.27 ? 205 THR C OG1 1 
ATOM   5988 C  CG2 . THR C 1 205 ? 40.435  10.381  -43.195 1.00 13.70 ? 205 THR C CG2 1 
ATOM   5989 N  N   . VAL C 1 206 ? 39.660  5.625   -42.166 1.00 10.30 ? 206 VAL C N   1 
ATOM   5990 C  CA  . VAL C 1 206 ? 40.118  4.405   -41.498 1.00 9.21  ? 206 VAL C CA  1 
ATOM   5991 C  C   . VAL C 1 206 ? 39.981  3.155   -42.357 1.00 9.35  ? 206 VAL C C   1 
ATOM   5992 O  O   . VAL C 1 206 ? 38.862  2.867   -42.818 1.00 11.18 ? 206 VAL C O   1 
ATOM   5993 C  CB  . VAL C 1 206 ? 39.309  4.187   -40.194 1.00 9.22  ? 206 VAL C CB  1 
ATOM   5994 C  CG1 . VAL C 1 206 ? 39.734  2.847   -39.560 1.00 9.72  ? 206 VAL C CG1 1 
ATOM   5995 C  CG2 . VAL C 1 206 ? 39.453  5.331   -39.192 1.00 10.98 ? 206 VAL C CG2 1 
ATOM   5996 N  N   . LEU C 1 207 ? 41.051  2.391   -42.551 1.00 9.89  ? 207 LEU C N   1 
ATOM   5997 C  CA  . LEU C 1 207 ? 40.992  1.062   -43.122 1.00 10.49 ? 207 LEU C CA  1 
ATOM   5998 C  C   . LEU C 1 207 ? 40.712  0.087   -41.994 1.00 9.95  ? 207 LEU C C   1 
ATOM   5999 O  O   . LEU C 1 207 ? 41.573  -0.054  -41.113 1.00 10.15 ? 207 LEU C O   1 
ATOM   6000 C  CB  . LEU C 1 207 ? 42.326  0.771   -43.843 1.00 12.17 ? 207 LEU C CB  1 
ATOM   6001 C  CG  . LEU C 1 207 ? 42.244  -0.516  -44.670 1.00 14.87 ? 207 LEU C CG  1 
ATOM   6002 C  CD1 . LEU C 1 207 ? 41.418  -0.289  -45.951 1.00 19.93 ? 207 LEU C CD1 1 
ATOM   6003 C  CD2 . LEU C 1 207 ? 43.628  -1.053  -45.014 1.00 22.44 ? 207 LEU C CD2 1 
ATOM   6004 N  N   . TRP C 1 208 ? 39.519  -0.496  -41.963 1.00 9.16  ? 208 TRP C N   1 
ATOM   6005 C  CA  . TRP C 1 208 ? 39.143  -1.385  -40.869 1.00 9.26  ? 208 TRP C CA  1 
ATOM   6006 C  C   . TRP C 1 208 ? 39.528  -2.820  -41.161 1.00 9.19  ? 208 TRP C C   1 
ATOM   6007 O  O   . TRP C 1 208 ? 39.315  -3.335  -42.274 1.00 9.66  ? 208 TRP C O   1 
ATOM   6008 C  CB  . TRP C 1 208 ? 37.622  -1.351  -40.659 1.00 8.22  ? 208 TRP C CB  1 
ATOM   6009 C  CG  . TRP C 1 208 ? 37.226  -0.136  -39.882 1.00 7.93  ? 208 TRP C CG  1 
ATOM   6010 C  CD1 . TRP C 1 208 ? 36.803  1.079   -40.348 1.00 8.18  ? 208 TRP C CD1 1 
ATOM   6011 C  CD2 . TRP C 1 208 ? 37.310  0.014   -38.437 1.00 7.29  ? 208 TRP C CD2 1 
ATOM   6012 N  NE1 . TRP C 1 208 ? 36.575  1.939   -39.324 1.00 9.45  ? 208 TRP C NE1 1 
ATOM   6013 C  CE2 . TRP C 1 208 ? 36.910  1.324   -38.147 1.00 8.39  ? 208 TRP C CE2 1 
ATOM   6014 C  CE3 . TRP C 1 208 ? 37.669  -0.831  -37.382 1.00 9.11  ? 208 TRP C CE3 1 
ATOM   6015 C  CZ2 . TRP C 1 208 ? 36.867  1.824   -36.840 1.00 9.39  ? 208 TRP C CZ2 1 
ATOM   6016 C  CZ3 . TRP C 1 208 ? 37.597  -0.367  -36.078 1.00 9.48  ? 208 TRP C CZ3 1 
ATOM   6017 C  CH2 . TRP C 1 208 ? 37.239  0.957   -35.825 1.00 9.30  ? 208 TRP C CH2 1 
ATOM   6018 N  N   . THR C 1 209 ? 40.065  -3.480  -40.142 1.00 9.55  ? 209 THR C N   1 
ATOM   6019 C  CA  . THR C 1 209 ? 40.308  -4.905  -40.119 1.00 9.75  ? 209 THR C CA  1 
ATOM   6020 C  C   . THR C 1 209 ? 39.637  -5.444  -38.867 1.00 9.87  ? 209 THR C C   1 
ATOM   6021 O  O   . THR C 1 209 ? 40.090  -5.094  -37.777 1.00 10.85 ? 209 THR C O   1 
ATOM   6022 C  CB  . THR C 1 209 ? 41.810  -5.227  -40.117 1.00 10.23 ? 209 THR C CB  1 
ATOM   6023 O  OG1 . THR C 1 209 ? 42.384  -4.693  -41.323 1.00 10.57 ? 209 THR C OG1 1 
ATOM   6024 C  CG2 . THR C 1 209 ? 42.055  -6.729  -40.089 1.00 10.99 ? 209 THR C CG2 1 
ATOM   6025 N  N   . VAL C 1 210 ? 38.592  -6.230  -39.045 1.00 9.75  ? 210 VAL C N   1 
ATOM   6026 C  CA  . VAL C 1 210 ? 37.921  -6.778  -37.885 1.00 9.67  ? 210 VAL C CA  1 
ATOM   6027 C  C   . VAL C 1 210 ? 38.163  -8.273  -37.902 1.00 9.61  ? 210 VAL C C   1 
ATOM   6028 O  O   . VAL C 1 210 ? 37.840  -8.949  -38.882 1.00 10.52 ? 210 VAL C O   1 
ATOM   6029 C  CB  . VAL C 1 210 ? 36.402  -6.534  -37.912 1.00 8.55  ? 210 VAL C CB  1 
ATOM   6030 C  CG1 . VAL C 1 210 ? 35.698  -7.089  -36.667 1.00 10.36 ? 210 VAL C CG1 1 
ATOM   6031 C  CG2 . VAL C 1 210 ? 36.106  -5.041  -38.130 1.00 9.89  ? 210 VAL C CG2 1 
ATOM   6032 N  N   . PHE C 1 211 ? 38.821  -8.778  -36.852 1.00 10.10 ? 211 PHE C N   1 
ATOM   6033 C  CA  . PHE C 1 211 ? 39.110  -10.197 -36.962 1.00 10.87 ? 211 PHE C CA  1 
ATOM   6034 C  C   . PHE C 1 211 ? 37.836  -11.025 -36.847 1.00 11.05 ? 211 PHE C C   1 
ATOM   6035 O  O   . PHE C 1 211 ? 36.906  -10.679 -36.126 1.00 12.11 ? 211 PHE C O   1 
ATOM   6036 C  CB  . PHE C 1 211 ? 40.147  -10.622 -35.907 1.00 11.97 ? 211 PHE C CB  1 
ATOM   6037 C  CG  . PHE C 1 211 ? 41.484  -9.950  -36.107 1.00 11.09 ? 211 PHE C CG  1 
ATOM   6038 C  CD1 . PHE C 1 211 ? 42.299  -10.336 -37.155 1.00 12.04 ? 211 PHE C CD1 1 
ATOM   6039 C  CD2 . PHE C 1 211 ? 41.896  -8.884  -35.304 1.00 13.49 ? 211 PHE C CD2 1 
ATOM   6040 C  CE1 . PHE C 1 211 ? 43.525  -9.702  -37.373 1.00 13.70 ? 211 PHE C CE1 1 
ATOM   6041 C  CE2 . PHE C 1 211 ? 43.120  -8.277  -35.515 1.00 13.00 ? 211 PHE C CE2 1 
ATOM   6042 C  CZ  . PHE C 1 211 ? 43.907  -8.668  -36.550 1.00 13.08 ? 211 PHE C CZ  1 
ATOM   6043 N  N   A ARG C 1 212 ? 37.818  -12.158 -37.555 0.50 11.55 ? 212 ARG C N   1 
ATOM   6044 N  N   B ARG C 1 212 ? 37.814  -12.165 -37.549 0.50 11.68 ? 212 ARG C N   1 
ATOM   6045 C  CA  A ARG C 1 212 ? 36.637  -13.001 -37.581 0.50 13.05 ? 212 ARG C CA  1 
ATOM   6046 C  CA  B ARG C 1 212 ? 36.614  -12.986 -37.591 0.50 13.25 ? 212 ARG C CA  1 
ATOM   6047 C  C   A ARG C 1 212 ? 36.348  -13.582 -36.194 0.50 12.94 ? 212 ARG C C   1 
ATOM   6048 C  C   B ARG C 1 212 ? 36.346  -13.638 -36.228 0.50 13.17 ? 212 ARG C C   1 
ATOM   6049 O  O   A ARG C 1 212 ? 35.197  -13.673 -35.782 0.50 14.20 ? 212 ARG C O   1 
ATOM   6050 O  O   B ARG C 1 212 ? 35.188  -13.822 -35.866 0.50 14.49 ? 212 ARG C O   1 
ATOM   6051 C  CB  A ARG C 1 212 ? 36.890  -14.164 -38.538 0.50 13.83 ? 212 ARG C CB  1 
ATOM   6052 C  CB  B ARG C 1 212 ? 36.742  -14.036 -38.699 0.50 14.37 ? 212 ARG C CB  1 
ATOM   6053 C  CG  A ARG C 1 212 ? 35.775  -15.198 -38.544 0.50 15.57 ? 212 ARG C CG  1 
ATOM   6054 C  CG  B ARG C 1 212 ? 35.515  -14.919 -38.889 0.50 16.05 ? 212 ARG C CG  1 
ATOM   6055 C  CD  A ARG C 1 212 ? 36.192  -16.429 -39.337 0.50 18.03 ? 212 ARG C CD  1 
ATOM   6056 C  CD  B ARG C 1 212 ? 35.885  -16.101 -39.763 0.50 18.36 ? 212 ARG C CD  1 
ATOM   6057 N  NE  A ARG C 1 212 ? 35.057  -17.326 -39.542 0.50 17.30 ? 212 ARG C NE  1 
ATOM   6058 N  NE  B ARG C 1 212 ? 34.732  -16.702 -40.404 0.50 20.67 ? 212 ARG C NE  1 
ATOM   6059 C  CZ  A ARG C 1 212 ? 34.694  -18.329 -38.741 0.50 20.66 ? 212 ARG C CZ  1 
ATOM   6060 C  CZ  B ARG C 1 212 ? 34.762  -17.809 -41.142 0.50 21.06 ? 212 ARG C CZ  1 
ATOM   6061 N  NH1 A ARG C 1 212 ? 35.386  -18.620 -37.656 0.50 20.48 ? 212 ARG C NH1 1 
ATOM   6062 N  NH1 B ARG C 1 212 ? 35.893  -18.471 -41.323 0.50 22.99 ? 212 ARG C NH1 1 
ATOM   6063 N  NH2 A ARG C 1 212 ? 33.632  -19.056 -39.037 0.50 22.12 ? 212 ARG C NH2 1 
ATOM   6064 N  NH2 B ARG C 1 212 ? 33.650  -18.232 -41.703 0.50 19.72 ? 212 ARG C NH2 1 
ATOM   6065 N  N   . ASN C 1 213 ? 37.417  -13.989 -35.489 1.00 13.77 ? 213 ASN C N   1 
ATOM   6066 C  CA  . ASN C 1 213 ? 37.234  -14.760 -34.256 1.00 14.72 ? 213 ASN C CA  1 
ATOM   6067 C  C   . ASN C 1 213 ? 37.375  -13.832 -33.056 1.00 13.65 ? 213 ASN C C   1 
ATOM   6068 O  O   . ASN C 1 213 ? 38.265  -13.003 -33.019 1.00 15.47 ? 213 ASN C O   1 
ATOM   6069 C  CB  . ASN C 1 213 ? 38.289  -15.871 -34.146 1.00 17.95 ? 213 ASN C CB  1 
ATOM   6070 C  CG  . ASN C 1 213 ? 38.270  -16.793 -35.349 1.00 19.24 ? 213 ASN C CG  1 
ATOM   6071 O  OD1 . ASN C 1 213 ? 39.284  -16.994 -36.033 1.00 21.77 ? 213 ASN C OD1 1 
ATOM   6072 N  ND2 . ASN C 1 213 ? 37.100  -17.315 -35.670 1.00 21.39 ? 213 ASN C ND2 1 
ATOM   6073 N  N   . PRO C 1 214 ? 36.481  -13.971 -32.051 1.00 13.78 ? 214 PRO C N   1 
ATOM   6074 C  CA  . PRO C 1 214 ? 36.559  -13.172 -30.841 1.00 14.85 ? 214 PRO C CA  1 
ATOM   6075 C  C   . PRO C 1 214 ? 37.562  -13.744 -29.850 1.00 15.62 ? 214 PRO C C   1 
ATOM   6076 O  O   . PRO C 1 214 ? 38.037  -14.873 -30.005 1.00 18.77 ? 214 PRO C O   1 
ATOM   6077 C  CB  . PRO C 1 214 ? 35.170  -13.316 -30.216 1.00 16.62 ? 214 PRO C CB  1 
ATOM   6078 C  CG  . PRO C 1 214 ? 34.758  -14.718 -30.669 1.00 18.39 ? 214 PRO C CG  1 
ATOM   6079 C  CD  . PRO C 1 214 ? 35.317  -14.886 -32.074 1.00 17.87 ? 214 PRO C CD  1 
ATOM   6080 N  N   . VAL C 1 215 ? 37.999  -12.880 -28.946 1.00 13.66 ? 215 VAL C N   1 
ATOM   6081 C  CA  . VAL C 1 215 ? 38.694  -13.317 -27.729 1.00 14.97 ? 215 VAL C CA  1 
ATOM   6082 C  C   . VAL C 1 215 ? 37.691  -13.416 -26.592 1.00 16.65 ? 215 VAL C C   1 
ATOM   6083 O  O   . VAL C 1 215 ? 36.566  -12.895 -26.672 1.00 15.83 ? 215 VAL C O   1 
ATOM   6084 C  CB  . VAL C 1 215 ? 39.816  -12.349 -27.347 1.00 18.14 ? 215 VAL C CB  1 
ATOM   6085 C  CG1 . VAL C 1 215 ? 40.911  -12.269 -28.388 1.00 18.24 ? 215 VAL C CG1 1 
ATOM   6086 C  CG2 . VAL C 1 215 ? 39.350  -10.979 -26.866 1.00 16.67 ? 215 VAL C CG2 1 
ATOM   6087 N  N   . GLN C 1 216 ? 38.107  -14.118 -25.518 1.00 17.64 ? 216 GLN C N   1 
ATOM   6088 C  CA  . GLN C 1 216 ? 37.337  -14.296 -24.299 1.00 17.57 ? 216 GLN C CA  1 
ATOM   6089 C  C   . GLN C 1 216 ? 38.022  -13.611 -23.125 1.00 17.90 ? 216 GLN C C   1 
ATOM   6090 O  O   . GLN C 1 216 ? 39.246  -13.597 -23.011 1.00 19.08 ? 216 GLN C O   1 
ATOM   6091 C  CB  . GLN C 1 216 ? 37.209  -15.801 -24.020 1.00 18.77 ? 216 GLN C CB  1 
ATOM   6092 C  CG  . GLN C 1 216 ? 36.361  -16.501 -25.061 1.00 23.02 ? 216 GLN C CG  1 
ATOM   6093 C  CD  . GLN C 1 216 ? 35.910  -17.856 -24.584 1.00 30.74 ? 216 GLN C CD  1 
ATOM   6094 O  OE1 . GLN C 1 216 ? 36.361  -18.367 -23.540 1.00 33.41 ? 216 GLN C OE1 1 
ATOM   6095 N  NE2 . GLN C 1 216 ? 34.953  -18.396 -25.323 1.00 36.99 ? 216 GLN C NE2 1 
ATOM   6096 N  N   . ILE C 1 217 ? 37.182  -13.003 -22.287 1.00 17.01 ? 217 ILE C N   1 
ATOM   6097 C  CA  . ILE C 1 217 ? 37.548  -12.495 -20.977 1.00 16.99 ? 217 ILE C CA  1 
ATOM   6098 C  C   . ILE C 1 217 ? 36.535  -13.037 -19.977 1.00 16.93 ? 217 ILE C C   1 
ATOM   6099 O  O   . ILE C 1 217 ? 35.412  -13.406 -20.325 1.00 18.45 ? 217 ILE C O   1 
ATOM   6100 C  CB  . ILE C 1 217 ? 37.680  -10.958 -20.930 1.00 17.02 ? 217 ILE C CB  1 
ATOM   6101 C  CG1 . ILE C 1 217 ? 36.338  -10.226 -21.108 1.00 15.93 ? 217 ILE C CG1 1 
ATOM   6102 C  CG2 . ILE C 1 217 ? 38.770  -10.498 -21.911 1.00 18.60 ? 217 ILE C CG2 1 
ATOM   6103 C  CD1 . ILE C 1 217 ? 36.416  -8.709  -20.866 1.00 16.57 ? 217 ILE C CD1 1 
ATOM   6104 N  N   . SER C 1 218 ? 36.991  -13.184 -18.724 1.00 18.23 ? 218 SER C N   1 
ATOM   6105 C  CA  . SER C 1 218 ? 36.060  -13.735 -17.756 1.00 19.30 ? 218 SER C CA  1 
ATOM   6106 C  C   . SER C 1 218 ? 34.900  -12.778 -17.513 1.00 21.21 ? 218 SER C C   1 
ATOM   6107 O  O   . SER C 1 218 ? 34.990  -11.547 -17.687 1.00 20.64 ? 218 SER C O   1 
ATOM   6108 C  CB  . SER C 1 218 ? 36.741  -14.086 -16.439 1.00 19.03 ? 218 SER C CB  1 
ATOM   6109 O  OG  . SER C 1 218 ? 37.226  -12.923 -15.792 1.00 21.98 ? 218 SER C OG  1 
ATOM   6110 N  N   . GLN C 1 219 ? 33.806  -13.356 -17.006 1.00 23.17 ? 219 GLN C N   1 
ATOM   6111 C  CA  . GLN C 1 219 ? 32.715  -12.579 -16.464 1.00 24.65 ? 219 GLN C CA  1 
ATOM   6112 C  C   . GLN C 1 219 ? 33.213  -11.512 -15.488 1.00 22.61 ? 219 GLN C C   1 
ATOM   6113 O  O   . GLN C 1 219 ? 32.752  -10.374 -15.501 1.00 20.47 ? 219 GLN C O   1 
ATOM   6114 C  CB  . GLN C 1 219 ? 31.784  -13.546 -15.727 1.00 29.16 ? 219 GLN C CB  1 
ATOM   6115 C  CG  . GLN C 1 219 ? 30.378  -13.036 -15.497 1.00 41.33 ? 219 GLN C CG  1 
ATOM   6116 C  CD  . GLN C 1 219 ? 29.613  -14.108 -14.753 1.00 51.43 ? 219 GLN C CD  1 
ATOM   6117 O  OE1 . GLN C 1 219 ? 29.889  -14.395 -13.583 1.00 58.61 ? 219 GLN C OE1 1 
ATOM   6118 N  NE2 . GLN C 1 219 ? 28.675  -14.741 -15.447 1.00 49.42 ? 219 GLN C NE2 1 
ATOM   6119 N  N   . GLU C 1 220 ? 34.144  -11.884 -14.597 1.00 21.74 ? 220 GLU C N   1 
ATOM   6120 C  CA  . GLU C 1 220 ? 34.705  -10.948 -13.636 1.00 22.35 ? 220 GLU C CA  1 
ATOM   6121 C  C   . GLU C 1 220 ? 35.472  -9.804  -14.315 1.00 16.51 ? 220 GLU C C   1 
ATOM   6122 O  O   . GLU C 1 220 ? 35.339  -8.684  -13.882 1.00 19.98 ? 220 GLU C O   1 
ATOM   6123 C  CB  . GLU C 1 220 ? 35.565  -11.631 -12.559 1.00 26.05 ? 220 GLU C CB  1 
ATOM   6124 C  CG  . GLU C 1 220 ? 34.909  -12.900 -11.992 1.00 33.05 ? 220 GLU C CG  1 
ATOM   6125 C  CD  . GLU C 1 220 ? 35.152  -14.283 -12.621 1.00 41.03 ? 220 GLU C CD  1 
ATOM   6126 O  OE1 . GLU C 1 220 ? 34.679  -14.542 -13.760 1.00 36.11 ? 220 GLU C OE1 1 
ATOM   6127 O  OE2 . GLU C 1 220 ? 35.796  -15.141 -11.939 1.00 43.28 ? 220 GLU C OE2 1 
ATOM   6128 N  N   . GLN C 1 221 ? 36.249  -10.093 -15.368 1.00 20.20 ? 221 GLN C N   1 
ATOM   6129 C  CA  . GLN C 1 221 ? 37.016  -9.067  -16.064 1.00 17.38 ? 221 GLN C CA  1 
ATOM   6130 C  C   . GLN C 1 221 ? 36.092  -8.101  -16.808 1.00 14.50 ? 221 GLN C C   1 
ATOM   6131 O  O   . GLN C 1 221 ? 36.260  -6.880  -16.715 1.00 16.68 ? 221 GLN C O   1 
ATOM   6132 C  CB  . GLN C 1 221 ? 37.971  -9.738  -17.035 1.00 18.67 ? 221 GLN C CB  1 
ATOM   6133 C  CG  . GLN C 1 221 ? 39.124  -10.466 -16.344 1.00 16.48 ? 221 GLN C CG  1 
ATOM   6134 C  CD  . GLN C 1 221 ? 40.004  -11.046 -17.422 1.00 16.60 ? 221 GLN C CD  1 
ATOM   6135 O  OE1 . GLN C 1 221 ? 39.592  -11.936 -18.147 1.00 16.98 ? 221 GLN C OE1 1 
ATOM   6136 N  NE2 . GLN C 1 221 ? 41.196  -10.508 -17.559 1.00 19.41 ? 221 GLN C NE2 1 
ATOM   6137 N  N   . LEU C 1 222 ? 35.033  -8.672  -17.396 1.00 16.12 ? 222 LEU C N   1 
ATOM   6138 C  CA  . LEU C 1 222 ? 34.051  -7.837  -18.091 1.00 16.29 ? 222 LEU C CA  1 
ATOM   6139 C  C   . LEU C 1 222 ? 33.315  -6.890  -17.145 1.00 15.81 ? 222 LEU C C   1 
ATOM   6140 O  O   . LEU C 1 222 ? 33.189  -5.712  -17.451 1.00 15.81 ? 222 LEU C O   1 
ATOM   6141 C  CB  . LEU C 1 222 ? 33.054  -8.714  -18.842 1.00 17.09 ? 222 LEU C CB  1 
ATOM   6142 C  CG  . LEU C 1 222 ? 31.989  -7.967  -19.635 1.00 16.98 ? 222 LEU C CG  1 
ATOM   6143 C  CD1 . LEU C 1 222 ? 32.593  -7.036  -20.672 1.00 16.97 ? 222 LEU C CD1 1 
ATOM   6144 C  CD2 . LEU C 1 222 ? 31.047  -8.971  -20.297 1.00 17.39 ? 222 LEU C CD2 1 
ATOM   6145 N  N   . LEU C 1 223 ? 32.825  -7.385  -15.960 1.00 17.04 ? 223 LEU C N   1 
ATOM   6146 C  CA  . LEU C 1 223 ? 32.177  -6.537  -14.963 1.00 18.06 ? 223 LEU C CA  1 
ATOM   6147 C  C   . LEU C 1 223 ? 33.130  -5.451  -14.462 1.00 15.49 ? 223 LEU C C   1 
ATOM   6148 O  O   . LEU C 1 223 ? 32.739  -4.296  -14.245 1.00 16.37 ? 223 LEU C O   1 
ATOM   6149 C  CB  . LEU C 1 223 ? 31.703  -7.435  -13.812 1.00 21.99 ? 223 LEU C CB  1 
ATOM   6150 C  CG  . LEU C 1 223 ? 30.744  -6.783  -12.822 1.00 28.33 ? 223 LEU C CG  1 
ATOM   6151 C  CD1 . LEU C 1 223 ? 29.509  -6.218  -13.502 1.00 26.73 ? 223 LEU C CD1 1 
ATOM   6152 C  CD2 . LEU C 1 223 ? 30.318  -7.808  -11.781 1.00 28.41 ? 223 LEU C CD2 1 
ATOM   6153 N  N   . ALA C 1 224 ? 34.385  -5.842  -14.270 1.00 16.78 ? 224 ALA C N   1 
ATOM   6154 C  CA  . ALA C 1 224 ? 35.405  -4.899  -13.828 1.00 19.23 ? 224 ALA C CA  1 
ATOM   6155 C  C   . ALA C 1 224 ? 35.523  -3.748  -14.826 1.00 17.24 ? 224 ALA C C   1 
ATOM   6156 O  O   . ALA C 1 224 ? 35.416  -2.584  -14.459 1.00 19.49 ? 224 ALA C O   1 
ATOM   6157 C  CB  . ALA C 1 224 ? 36.732  -5.629  -13.581 1.00 20.20 ? 224 ALA C CB  1 
ATOM   6158 N  N   . LEU C 1 225 ? 35.637  -4.062  -16.136 1.00 17.94 ? 225 LEU C N   1 
ATOM   6159 C  CA  . LEU C 1 225 ? 35.761  -3.022  -17.148 1.00 17.97 ? 225 LEU C CA  1 
ATOM   6160 C  C   . LEU C 1 225 ? 34.509  -2.143  -17.159 1.00 14.78 ? 225 LEU C C   1 
ATOM   6161 O  O   . LEU C 1 225 ? 34.620  -0.925  -17.246 1.00 17.94 ? 225 LEU C O   1 
ATOM   6162 C  CB  . LEU C 1 225 ? 35.970  -3.709  -18.507 1.00 15.98 ? 225 LEU C CB  1 
ATOM   6163 C  CG  . LEU C 1 225 ? 35.959  -2.770  -19.718 1.00 15.66 ? 225 LEU C CG  1 
ATOM   6164 C  CD1 . LEU C 1 225 ? 37.138  -1.814  -19.619 1.00 16.46 ? 225 LEU C CD1 1 
ATOM   6165 C  CD2 . LEU C 1 225 ? 35.982  -3.555  -21.026 1.00 14.88 ? 225 LEU C CD2 1 
ATOM   6166 N  N   . GLU C 1 226 ? 33.327  -2.766  -17.049 1.00 16.03 ? 226 GLU C N   1 
ATOM   6167 C  CA  . GLU C 1 226 ? 32.080  -2.017  -17.115 1.00 15.77 ? 226 GLU C CA  1 
ATOM   6168 C  C   . GLU C 1 226 ? 31.821  -1.132  -15.893 1.00 16.05 ? 226 GLU C C   1 
ATOM   6169 O  O   . GLU C 1 226 ? 31.070  -0.166  -15.968 1.00 17.84 ? 226 GLU C O   1 
ATOM   6170 C  CB  . GLU C 1 226 ? 30.906  -2.980  -17.227 1.00 16.61 ? 226 GLU C CB  1 
ATOM   6171 C  CG  . GLU C 1 226 ? 30.899  -3.778  -18.536 1.00 15.27 ? 226 GLU C CG  1 
ATOM   6172 C  CD  . GLU C 1 226 ? 29.965  -4.972  -18.502 1.00 16.08 ? 226 GLU C CD  1 
ATOM   6173 O  OE1 . GLU C 1 226 ? 29.597  -5.444  -17.349 1.00 17.38 ? 226 GLU C OE1 1 
ATOM   6174 O  OE2 . GLU C 1 226 ? 29.591  -5.480  -19.542 1.00 18.50 ? 226 GLU C OE2 1 
ATOM   6175 N  N   . THR C 1 227 ? 32.481  -1.432  -14.765 1.00 17.26 ? 227 THR C N   1 
ATOM   6176 C  CA  . THR C 1 227 ? 32.157  -0.748  -13.514 1.00 17.00 ? 227 THR C CA  1 
ATOM   6177 C  C   . THR C 1 227 ? 33.336  0.027   -12.933 1.00 17.40 ? 227 THR C C   1 
ATOM   6178 O  O   . THR C 1 227 ? 33.168  0.603   -11.861 1.00 19.86 ? 227 THR C O   1 
ATOM   6179 C  CB  . THR C 1 227 ? 31.572  -1.716  -12.466 1.00 18.10 ? 227 THR C CB  1 
ATOM   6180 O  OG1 . THR C 1 227 ? 32.561  -2.712  -12.222 1.00 20.05 ? 227 THR C OG1 1 
ATOM   6181 C  CG2 . THR C 1 227 ? 30.267  -2.328  -12.945 1.00 21.11 ? 227 THR C CG2 1 
ATOM   6182 N  N   . ALA C 1 228 ? 34.460  0.103   -13.638 1.00 15.81 ? 228 ALA C N   1 
ATOM   6183 C  CA  . ALA C 1 228 ? 35.655  0.657   -13.012 1.00 17.12 ? 228 ALA C CA  1 
ATOM   6184 C  C   . ALA C 1 228 ? 35.742  2.178   -13.160 1.00 18.81 ? 228 ALA C C   1 
ATOM   6185 O  O   . ALA C 1 228 ? 36.397  2.838   -12.359 1.00 19.16 ? 228 ALA C O   1 
ATOM   6186 C  CB  . ALA C 1 228 ? 36.907  -0.042  -13.505 1.00 19.51 ? 228 ALA C CB  1 
ATOM   6187 N  N   . LEU C 1 229 ? 35.164  2.774   -14.228 1.00 16.04 ? 229 LEU C N   1 
ATOM   6188 C  CA  . LEU C 1 229 ? 35.478  4.145   -14.611 1.00 15.75 ? 229 LEU C CA  1 
ATOM   6189 C  C   . LEU C 1 229 ? 34.266  5.048   -14.554 1.00 16.71 ? 229 LEU C C   1 
ATOM   6190 O  O   . LEU C 1 229 ? 33.132  4.666   -14.831 1.00 15.30 ? 229 LEU C O   1 
ATOM   6191 C  CB  . LEU C 1 229 ? 36.073  4.199   -16.018 1.00 15.46 ? 229 LEU C CB  1 
ATOM   6192 C  CG  . LEU C 1 229 ? 37.193  3.199   -16.297 1.00 14.99 ? 229 LEU C CG  1 
ATOM   6193 C  CD1 . LEU C 1 229 ? 37.669  3.423   -17.741 1.00 18.17 ? 229 LEU C CD1 1 
ATOM   6194 C  CD2 . LEU C 1 229 ? 38.368  3.376   -15.338 1.00 16.16 ? 229 LEU C CD2 1 
ATOM   6195 N  N   . TYR C 1 230 ? 34.536  6.282   -14.134 1.00 17.37 ? 230 TYR C N   1 
ATOM   6196 C  CA  . TYR C 1 230 ? 33.624  7.377   -14.388 1.00 16.61 ? 230 TYR C CA  1 
ATOM   6197 C  C   . TYR C 1 230 ? 34.072  8.130   -15.633 1.00 18.47 ? 230 TYR C C   1 
ATOM   6198 O  O   . TYR C 1 230 ? 35.241  8.124   -15.994 1.00 19.63 ? 230 TYR C O   1 
ATOM   6199 C  CB  . TYR C 1 230 ? 33.653  8.325   -13.189 1.00 18.99 ? 230 TYR C CB  1 
ATOM   6200 C  CG  . TYR C 1 230 ? 33.275  7.733   -11.847 1.00 24.12 ? 230 TYR C CG  1 
ATOM   6201 C  CD1 . TYR C 1 230 ? 31.948  7.528   -11.480 1.00 25.10 ? 230 TYR C CD1 1 
ATOM   6202 C  CD2 . TYR C 1 230 ? 34.264  7.469   -10.909 1.00 27.04 ? 230 TYR C CD2 1 
ATOM   6203 C  CE1 . TYR C 1 230 ? 31.620  7.068   -10.209 1.00 25.57 ? 230 TYR C CE1 1 
ATOM   6204 C  CE2 . TYR C 1 230 ? 33.955  6.998   -9.640  1.00 27.40 ? 230 TYR C CE2 1 
ATOM   6205 C  CZ  . TYR C 1 230 ? 32.629  6.797   -9.294  1.00 27.11 ? 230 TYR C CZ  1 
ATOM   6206 O  OH  . TYR C 1 230 ? 32.352  6.329   -8.034  1.00 30.41 ? 230 TYR C OH  1 
ATOM   6207 N  N   . CYS C 1 231 ? 33.130  8.820   -16.284 1.00 17.71 ? 231 CYS C N   1 
ATOM   6208 C  CA  . CYS C 1 231 ? 33.492  9.710   -17.362 1.00 21.37 ? 231 CYS C CA  1 
ATOM   6209 C  C   . CYS C 1 231 ? 33.582  11.176  -16.909 1.00 21.35 ? 231 CYS C C   1 
ATOM   6210 O  O   . CYS C 1 231 ? 33.903  12.066  -17.698 1.00 21.10 ? 231 CYS C O   1 
ATOM   6211 C  CB  . CYS C 1 231 ? 32.547  9.517   -18.548 1.00 21.98 ? 231 CYS C CB  1 
ATOM   6212 S  SG  . CYS C 1 231 ? 30.814  9.850   -18.186 1.00 28.33 ? 231 CYS C SG  1 
ATOM   6213 N  N   . THR C 1 232 ? 33.376  11.413  -15.609 1.00 19.40 ? 232 THR C N   1 
ATOM   6214 C  CA  . THR C 1 232 ? 33.431  12.733  -14.988 1.00 18.70 ? 232 THR C CA  1 
ATOM   6215 C  C   . THR C 1 232 ? 34.754  12.925  -14.246 1.00 20.21 ? 232 THR C C   1 
ATOM   6216 O  O   . THR C 1 232 ? 35.438  11.965  -13.911 1.00 17.29 ? 232 THR C O   1 
ATOM   6217 C  CB  . THR C 1 232 ? 32.219  12.872  -14.043 1.00 19.77 ? 232 THR C CB  1 
ATOM   6218 O  OG1 . THR C 1 232 ? 31.997  11.670  -13.269 1.00 19.61 ? 232 THR C OG1 1 
ATOM   6219 C  CG2 . THR C 1 232 ? 30.970  13.298  -14.798 1.00 21.48 ? 232 THR C CG2 1 
ATOM   6220 N  N   . HIS C 1 233 ? 35.072  14.201  -13.957 1.00 21.69 ? 233 HIS C N   1 
ATOM   6221 C  CA  . HIS C 1 233 ? 36.283  14.556  -13.213 1.00 23.67 ? 233 HIS C CA  1 
ATOM   6222 C  C   . HIS C 1 233 ? 36.104  14.193  -11.747 1.00 20.93 ? 233 HIS C C   1 
ATOM   6223 O  O   . HIS C 1 233 ? 34.983  14.076  -11.247 1.00 23.64 ? 233 HIS C O   1 
ATOM   6224 C  CB  . HIS C 1 233 ? 36.609  16.053  -13.356 1.00 24.57 ? 233 HIS C CB  1 
ATOM   6225 C  CG  . HIS C 1 233 ? 37.133  16.409  -14.703 1.00 27.14 ? 233 HIS C CG  1 
ATOM   6226 N  ND1 . HIS C 1 233 ? 36.389  17.147  -15.604 1.00 31.49 ? 233 HIS C ND1 1 
ATOM   6227 C  CD2 . HIS C 1 233 ? 38.312  16.150  -15.307 1.00 27.97 ? 233 HIS C CD2 1 
ATOM   6228 C  CE1 . HIS C 1 233 ? 37.079  17.313  -16.715 1.00 31.26 ? 233 HIS C CE1 1 
ATOM   6229 N  NE2 . HIS C 1 233 ? 38.254  16.713  -16.562 1.00 28.93 ? 233 HIS C NE2 1 
ATOM   6230 N  N   . MET C 1 234 ? 37.232  14.009  -11.057 1.00 24.24 ? 234 MET C N   1 
ATOM   6231 C  CA  . MET C 1 234 ? 37.238  13.633  -9.653  1.00 29.29 ? 234 MET C CA  1 
ATOM   6232 C  C   . MET C 1 234 ? 36.413  14.602  -8.804  1.00 31.91 ? 234 MET C C   1 
ATOM   6233 O  O   . MET C 1 234 ? 35.674  14.174  -7.923  1.00 37.50 ? 234 MET C O   1 
ATOM   6234 C  CB  . MET C 1 234 ? 38.683  13.560  -9.157  1.00 29.80 ? 234 MET C CB  1 
ATOM   6235 C  CG  . MET C 1 234 ? 38.819  12.935  -7.772  1.00 34.49 ? 234 MET C CG  1 
ATOM   6236 S  SD  . MET C 1 234 ? 40.556  12.829  -7.274  1.00 39.70 ? 234 MET C SD  1 
ATOM   6237 C  CE  . MET C 1 234 ? 40.831  11.060  -7.260  1.00 34.21 ? 234 MET C CE  1 
ATOM   6238 N  N   . ASP C 1 235 ? 36.468  15.902  -9.112  1.00 33.18 ? 235 ASP C N   1 
ATOM   6239 C  CA  . ASP C 1 235 ? 35.823  16.886  -8.252  1.00 40.53 ? 235 ASP C CA  1 
ATOM   6240 C  C   . ASP C 1 235 ? 34.322  17.022  -8.543  1.00 39.64 ? 235 ASP C C   1 
ATOM   6241 O  O   . ASP C 1 235 ? 33.634  17.770  -7.853  1.00 43.42 ? 235 ASP C O   1 
ATOM   6242 C  CB  . ASP C 1 235 ? 36.573  18.222  -8.265  0.01 38.50 ? 235 ASP C CB  1 
ATOM   6243 C  CG  . ASP C 1 235 ? 36.536  18.948  -9.600  0.01 38.59 ? 235 ASP C CG  1 
ATOM   6244 O  OD1 . ASP C 1 235 ? 36.523  18.265  -10.644 0.01 38.61 ? 235 ASP C OD1 1 
ATOM   6245 O  OD2 . ASP C 1 235 ? 36.520  20.195  -9.585  0.01 38.52 ? 235 ASP C OD2 1 
ATOM   6246 N  N   . ASP C 1 236 ? 33.795  16.287  -9.532  1.00 32.60 ? 236 ASP C N   1 
ATOM   6247 C  CA  . ASP C 1 236 ? 32.409  16.459  -9.953  1.00 33.56 ? 236 ASP C CA  1 
ATOM   6248 C  C   . ASP C 1 236 ? 31.451  15.942  -8.874  1.00 33.83 ? 236 ASP C C   1 
ATOM   6249 O  O   . ASP C 1 236 ? 31.496  14.763  -8.504  1.00 31.73 ? 236 ASP C O   1 
ATOM   6250 C  CB  . ASP C 1 236 ? 32.149  15.835  -11.336 1.00 30.29 ? 236 ASP C CB  1 
ATOM   6251 C  CG  . ASP C 1 236 ? 30.836  16.278  -11.966 1.00 31.48 ? 236 ASP C CG  1 
ATOM   6252 O  OD1 . ASP C 1 236 ? 29.900  16.593  -11.198 1.00 34.26 ? 236 ASP C OD1 1 
ATOM   6253 O  OD2 . ASP C 1 236 ? 30.743  16.325  -13.239 1.00 30.54 ? 236 ASP C OD2 1 
ATOM   6254 N  N   . PRO C 1 237 ? 30.548  16.804  -8.338  1.00 34.12 ? 237 PRO C N   1 
ATOM   6255 C  CA  . PRO C 1 237 ? 29.600  16.375  -7.306  1.00 32.91 ? 237 PRO C CA  1 
ATOM   6256 C  C   . PRO C 1 237 ? 28.486  15.491  -7.874  1.00 32.17 ? 237 PRO C C   1 
ATOM   6257 O  O   . PRO C 1 237 ? 27.722  14.915  -7.106  1.00 31.07 ? 237 PRO C O   1 
ATOM   6258 C  CB  . PRO C 1 237 ? 29.063  17.699  -6.743  1.00 34.12 ? 237 PRO C CB  1 
ATOM   6259 C  CG  . PRO C 1 237 ? 29.170  18.670  -7.897  1.00 35.33 ? 237 PRO C CG  1 
ATOM   6260 C  CD  . PRO C 1 237 ? 30.384  18.227  -8.696  1.00 35.74 ? 237 PRO C CD  1 
ATOM   6261 N  N   . SER C 1 238 ? 28.439  15.367  -9.211  1.00 32.02 ? 238 SER C N   1 
ATOM   6262 C  CA  . SER C 1 238 ? 27.488  14.517  -9.918  1.00 32.16 ? 238 SER C CA  1 
ATOM   6263 C  C   . SER C 1 238 ? 28.201  13.496  -10.811 1.00 26.95 ? 238 SER C C   1 
ATOM   6264 O  O   . SER C 1 238 ? 28.170  13.578  -12.047 1.00 27.70 ? 238 SER C O   1 
ATOM   6265 C  CB  . SER C 1 238 ? 26.513  15.348  -10.705 1.00 34.05 ? 238 SER C CB  1 
ATOM   6266 O  OG  . SER C 1 238 ? 25.367  15.629  -9.913  1.00 40.68 ? 238 SER C OG  1 
ATOM   6267 N  N   . PRO C 1 239 ? 28.869  12.475  -10.234 1.00 28.41 ? 239 PRO C N   1 
ATOM   6268 C  CA  . PRO C 1 239 ? 29.590  11.481  -11.030 1.00 25.69 ? 239 PRO C CA  1 
ATOM   6269 C  C   . PRO C 1 239 ? 28.709  10.650  -11.961 1.00 25.95 ? 239 PRO C C   1 
ATOM   6270 O  O   . PRO C 1 239 ? 27.526  10.404  -11.701 1.00 26.24 ? 239 PRO C O   1 
ATOM   6271 C  CB  . PRO C 1 239 ? 30.223  10.557  -9.982  1.00 26.31 ? 239 PRO C CB  1 
ATOM   6272 C  CG  . PRO C 1 239 ? 29.350  10.757  -8.759  1.00 28.25 ? 239 PRO C CG  1 
ATOM   6273 C  CD  . PRO C 1 239 ? 29.043  12.232  -8.789  1.00 27.77 ? 239 PRO C CD  1 
ATOM   6274 N  N   . ARG C 1 240 ? 29.303  10.290  -13.095 1.00 22.67 ? 240 ARG C N   1 
ATOM   6275 C  CA  . ARG C 1 240 ? 28.603  9.443   -14.058 1.00 20.79 ? 240 ARG C CA  1 
ATOM   6276 C  C   . ARG C 1 240 ? 29.513  8.269   -14.371 1.00 20.11 ? 240 ARG C C   1 
ATOM   6277 O  O   . ARG C 1 240 ? 30.703  8.483   -14.611 1.00 22.12 ? 240 ARG C O   1 
ATOM   6278 C  CB  . ARG C 1 240 ? 28.309  10.205  -15.350 1.00 23.90 ? 240 ARG C CB  1 
ATOM   6279 C  CG  . ARG C 1 240 ? 27.430  9.445   -16.342 1.00 24.52 ? 240 ARG C CG  1 
ATOM   6280 C  CD  . ARG C 1 240 ? 27.103  10.327  -17.546 1.00 30.92 ? 240 ARG C CD  1 
ATOM   6281 N  NE  . ARG C 1 240 ? 26.873  11.714  -17.113 1.00 37.78 ? 240 ARG C NE  1 
ATOM   6282 C  CZ  . ARG C 1 240 ? 27.738  12.743  -17.263 1.00 40.87 ? 240 ARG C CZ  1 
ATOM   6283 N  NH1 . ARG C 1 240 ? 28.911  12.573  -17.859 1.00 44.82 ? 240 ARG C NH1 1 
ATOM   6284 N  NH2 . ARG C 1 240 ? 27.418  13.948  -16.823 1.00 37.76 ? 240 ARG C NH2 1 
ATOM   6285 N  N   . GLU C 1 241 ? 28.953  7.050   -14.421 1.00 19.04 ? 241 GLU C N   1 
ATOM   6286 C  CA  . GLU C 1 241 ? 29.724  5.867   -14.784 1.00 20.35 ? 241 GLU C CA  1 
ATOM   6287 C  C   . GLU C 1 241 ? 29.998  5.818   -16.289 1.00 18.79 ? 241 GLU C C   1 
ATOM   6288 O  O   . GLU C 1 241 ? 29.158  6.203   -17.098 1.00 20.36 ? 241 GLU C O   1 
ATOM   6289 C  CB  . GLU C 1 241 ? 28.997  4.565   -14.456 1.00 25.36 ? 241 GLU C CB  1 
ATOM   6290 C  CG  . GLU C 1 241 ? 28.494  4.487   -13.029 1.00 32.37 ? 241 GLU C CG  1 
ATOM   6291 C  CD  . GLU C 1 241 ? 27.464  3.403   -12.732 1.00 41.92 ? 241 GLU C CD  1 
ATOM   6292 O  OE1 . GLU C 1 241 ? 26.869  2.826   -13.694 1.00 42.34 ? 241 GLU C OE1 1 
ATOM   6293 O  OE2 . GLU C 1 241 ? 27.249  3.133   -11.527 1.00 50.59 ? 241 GLU C OE2 1 
ATOM   6294 N  N   . MET C 1 242 ? 31.214  5.404   -16.649 1.00 16.44 ? 242 MET C N   1 
ATOM   6295 C  CA  . MET C 1 242 ? 31.607  5.255   -18.053 1.00 15.19 ? 242 MET C CA  1 
ATOM   6296 C  C   . MET C 1 242 ? 31.122  3.888   -18.543 1.00 13.59 ? 242 MET C C   1 
ATOM   6297 O  O   . MET C 1 242 ? 31.709  2.845   -18.288 1.00 13.92 ? 242 MET C O   1 
ATOM   6298 C  CB  . MET C 1 242 ? 33.130  5.368   -18.261 1.00 15.27 ? 242 MET C CB  1 
ATOM   6299 C  CG  . MET C 1 242 ? 33.501  5.378   -19.770 1.00 15.88 ? 242 MET C CG  1 
ATOM   6300 S  SD  . MET C 1 242 ? 35.257  5.341   -20.011 1.00 16.44 ? 242 MET C SD  1 
ATOM   6301 C  CE  . MET C 1 242 ? 35.727  6.963   -19.362 1.00 15.00 ? 242 MET C CE  1 
ATOM   6302 N  N   . ILE C 1 243 ? 29.973  3.903   -19.239 1.00 13.03 ? 243 ILE C N   1 
ATOM   6303 C  CA  . ILE C 1 243 ? 29.313  2.725   -19.747 1.00 13.71 ? 243 ILE C CA  1 
ATOM   6304 C  C   . ILE C 1 243 ? 28.769  3.065   -21.156 1.00 12.27 ? 243 ILE C C   1 
ATOM   6305 O  O   . ILE C 1 243 ? 28.536  4.228   -21.482 1.00 13.06 ? 243 ILE C O   1 
ATOM   6306 C  CB  . ILE C 1 243 ? 28.170  2.257   -18.812 1.00 14.19 ? 243 ILE C CB  1 
ATOM   6307 C  CG1 . ILE C 1 243 ? 27.168  3.377   -18.526 1.00 15.55 ? 243 ILE C CG1 1 
ATOM   6308 C  CG2 . ILE C 1 243 ? 28.728  1.632   -17.539 1.00 16.41 ? 243 ILE C CG2 1 
ATOM   6309 C  CD1 . ILE C 1 243 ? 26.013  2.895   -17.619 1.00 18.49 ? 243 ILE C CD1 1 
ATOM   6310 N  N   . ASN C 1 244 ? 28.467  2.003   -21.941 1.00 11.31 ? 244 ASN C N   1 
ATOM   6311 C  CA  . ASN C 1 244 ? 27.765  2.136   -23.230 1.00 12.41 ? 244 ASN C CA  1 
ATOM   6312 C  C   . ASN C 1 244 ? 28.492  3.128   -24.134 1.00 12.39 ? 244 ASN C C   1 
ATOM   6313 O  O   . ASN C 1 244 ? 27.884  3.984   -24.777 1.00 12.81 ? 244 ASN C O   1 
ATOM   6314 C  CB  . ASN C 1 244 ? 26.310  2.564   -23.040 1.00 13.69 ? 244 ASN C CB  1 
ATOM   6315 C  CG  . ASN C 1 244 ? 25.573  1.693   -22.058 1.00 15.49 ? 244 ASN C CG  1 
ATOM   6316 O  OD1 . ASN C 1 244 ? 25.734  0.484   -22.113 1.00 16.20 ? 244 ASN C OD1 1 
ATOM   6317 N  ND2 . ASN C 1 244 ? 24.811  2.347   -21.182 1.00 18.16 ? 244 ASN C ND2 1 
ATOM   6318 N  N   . ASN C 1 245 ? 29.819  2.994   -24.174 1.00 11.44 ? 245 ASN C N   1 
ATOM   6319 C  CA  . ASN C 1 245 ? 30.647  3.951   -24.907 1.00 10.86 ? 245 ASN C CA  1 
ATOM   6320 C  C   . ASN C 1 245 ? 30.990  3.454   -26.312 1.00 10.44 ? 245 ASN C C   1 
ATOM   6321 O  O   . ASN C 1 245 ? 32.125  3.363   -26.719 1.00 11.51 ? 245 ASN C O   1 
ATOM   6322 C  CB  . ASN C 1 245 ? 31.904  4.315   -24.122 1.00 11.38 ? 245 ASN C CB  1 
ATOM   6323 C  CG  . ASN C 1 245 ? 32.789  3.131   -23.850 1.00 12.83 ? 245 ASN C CG  1 
ATOM   6324 O  OD1 . ASN C 1 245 ? 32.365  1.979   -23.881 1.00 13.51 ? 245 ASN C OD1 1 
ATOM   6325 N  ND2 . ASN C 1 245 ? 34.054  3.398   -23.543 1.00 14.45 ? 245 ASN C ND2 1 
ATOM   6326 N  N   . PHE C 1 246 ? 29.930  3.051   -27.023 1.00 9.81  ? 246 PHE C N   1 
ATOM   6327 C  CA  . PHE C 1 246 ? 29.996  2.525   -28.391 1.00 9.84  ? 246 PHE C CA  1 
ATOM   6328 C  C   . PHE C 1 246 ? 29.009  3.346   -29.219 1.00 9.08  ? 246 PHE C C   1 
ATOM   6329 O  O   . PHE C 1 246 ? 27.988  3.813   -28.717 1.00 9.46  ? 246 PHE C O   1 
ATOM   6330 C  CB  . PHE C 1 246 ? 29.654  1.021   -28.419 1.00 10.69 ? 246 PHE C CB  1 
ATOM   6331 C  CG  . PHE C 1 246 ? 28.247  0.713   -27.955 1.00 9.34  ? 246 PHE C CG  1 
ATOM   6332 C  CD1 . PHE C 1 246 ? 27.967  0.495   -26.606 1.00 10.40 ? 246 PHE C CD1 1 
ATOM   6333 C  CD2 . PHE C 1 246 ? 27.198  0.590   -28.875 1.00 11.62 ? 246 PHE C CD2 1 
ATOM   6334 C  CE1 . PHE C 1 246 ? 26.700  0.180   -26.168 1.00 11.10 ? 246 PHE C CE1 1 
ATOM   6335 C  CE2 . PHE C 1 246 ? 25.910  0.298   -28.422 1.00 12.14 ? 246 PHE C CE2 1 
ATOM   6336 C  CZ  . PHE C 1 246 ? 25.652  0.106   -27.080 1.00 12.21 ? 246 PHE C CZ  1 
ATOM   6337 N  N   . ARG C 1 247 ? 29.344  3.472   -30.493 1.00 8.63  ? 247 ARG C N   1 
ATOM   6338 C  CA  . ARG C 1 247 ? 28.436  4.130   -31.453 1.00 8.98  ? 247 ARG C CA  1 
ATOM   6339 C  C   . ARG C 1 247 ? 27.476  3.079   -31.996 1.00 7.57  ? 247 ARG C C   1 
ATOM   6340 O  O   . ARG C 1 247 ? 27.886  1.943   -32.224 1.00 8.58  ? 247 ARG C O   1 
ATOM   6341 C  CB  . ARG C 1 247 ? 29.244  4.745   -32.602 1.00 8.68  ? 247 ARG C CB  1 
ATOM   6342 C  CG  . ARG C 1 247 ? 28.495  5.787   -33.433 1.00 8.29  ? 247 ARG C CG  1 
ATOM   6343 C  CD  . ARG C 1 247 ? 29.302  6.175   -34.667 1.00 7.61  ? 247 ARG C CD  1 
ATOM   6344 N  NE  . ARG C 1 247 ? 28.705  7.329   -35.309 1.00 7.88  ? 247 ARG C NE  1 
ATOM   6345 C  CZ  . ARG C 1 247 ? 29.244  7.900   -36.371 1.00 8.52  ? 247 ARG C CZ  1 
ATOM   6346 N  NH1 . ARG C 1 247 ? 30.241  7.312   -37.008 1.00 10.10 ? 247 ARG C NH1 1 
ATOM   6347 N  NH2 . ARG C 1 247 ? 28.692  9.006   -36.845 1.00 9.77  ? 247 ARG C NH2 1 
ATOM   6348 N  N   . GLN C 1 248 ? 26.228  3.475   -32.238 1.00 8.00  ? 248 GLN C N   1 
ATOM   6349 C  CA  . GLN C 1 248 ? 25.269  2.612   -32.939 1.00 7.79  ? 248 GLN C CA  1 
ATOM   6350 C  C   . GLN C 1 248 ? 25.775  2.307   -34.365 1.00 8.15  ? 248 GLN C C   1 
ATOM   6351 O  O   . GLN C 1 248 ? 26.502  3.095   -34.986 1.00 8.30  ? 248 GLN C O   1 
ATOM   6352 C  CB  . GLN C 1 248 ? 23.908  3.306   -33.084 1.00 8.52  ? 248 GLN C CB  1 
ATOM   6353 C  CG  . GLN C 1 248 ? 23.227  3.608   -31.741 1.00 8.61  ? 248 GLN C CG  1 
ATOM   6354 C  CD  . GLN C 1 248 ? 22.859  2.389   -30.914 1.00 9.70  ? 248 GLN C CD  1 
ATOM   6355 O  OE1 . GLN C 1 248 ? 23.575  1.992   -29.983 1.00 11.90 ? 248 GLN C OE1 1 
ATOM   6356 N  NE2 . GLN C 1 248 ? 21.750  1.745   -31.251 1.00 11.77 ? 248 GLN C NE2 1 
ATOM   6357 N  N   . VAL C 1 249 ? 25.381  1.149   -34.929 1.00 8.23  ? 249 VAL C N   1 
ATOM   6358 C  CA  . VAL C 1 249 ? 25.753  0.845   -36.299 1.00 8.93  ? 249 VAL C CA  1 
ATOM   6359 C  C   . VAL C 1 249 ? 25.144  1.844   -37.302 1.00 8.76  ? 249 VAL C C   1 
ATOM   6360 O  O   . VAL C 1 249 ? 24.023  2.329   -37.125 1.00 8.72  ? 249 VAL C O   1 
ATOM   6361 C  CB  . VAL C 1 249 ? 25.446  -0.609  -36.703 1.00 10.14 ? 249 VAL C CB  1 
ATOM   6362 C  CG1 . VAL C 1 249 ? 26.282  -1.634  -35.911 1.00 10.49 ? 249 VAL C CG1 1 
ATOM   6363 C  CG2 . VAL C 1 249 ? 23.978  -0.896  -36.632 1.00 12.38 ? 249 VAL C CG2 1 
ATOM   6364 N  N   . GLN C 1 250 ? 25.894  2.039   -38.376 1.00 8.51  ? 250 GLN C N   1 
ATOM   6365 C  CA  . GLN C 1 250 ? 25.537  2.999   -39.404 1.00 8.66  ? 250 GLN C CA  1 
ATOM   6366 C  C   . GLN C 1 250 ? 24.981  2.260   -40.612 1.00 9.80  ? 250 GLN C C   1 
ATOM   6367 O  O   . GLN C 1 250 ? 25.308  1.107   -40.885 1.00 10.92 ? 250 GLN C O   1 
ATOM   6368 C  CB  . GLN C 1 250 ? 26.832  3.674   -39.862 1.00 8.53  ? 250 GLN C CB  1 
ATOM   6369 C  CG  . GLN C 1 250 ? 27.620  4.319   -38.678 1.00 8.56  ? 250 GLN C CG  1 
ATOM   6370 C  CD  . GLN C 1 250 ? 26.883  5.462   -38.025 1.00 8.67  ? 250 GLN C CD  1 
ATOM   6371 O  OE1 . GLN C 1 250 ? 26.619  6.466   -38.717 1.00 9.51  ? 250 GLN C OE1 1 
ATOM   6372 N  NE2 . GLN C 1 250 ? 26.506  5.352   -36.761 1.00 10.09 ? 250 GLN C NE2 1 
ATOM   6373 N  N   . LYS C 1 251 ? 24.131  2.973   -41.360 1.00 9.97  ? 251 LYS C N   1 
ATOM   6374 C  CA  . LYS C 1 251 ? 23.700  2.402   -42.640 1.00 10.91 ? 251 LYS C CA  1 
ATOM   6375 C  C   . LYS C 1 251 ? 24.910  2.135   -43.518 1.00 11.18 ? 251 LYS C C   1 
ATOM   6376 O  O   . LYS C 1 251 ? 25.852  2.931   -43.563 1.00 10.75 ? 251 LYS C O   1 
ATOM   6377 C  CB  . LYS C 1 251 ? 22.690  3.325   -43.319 1.00 10.55 ? 251 LYS C CB  1 
ATOM   6378 C  CG  . LYS C 1 251 ? 21.323  3.246   -42.646 1.00 11.50 ? 251 LYS C CG  1 
ATOM   6379 C  CD  . LYS C 1 251 ? 20.377  4.244   -43.207 1.00 11.21 ? 251 LYS C CD  1 
ATOM   6380 C  CE  . LYS C 1 251 ? 18.917  3.971   -42.851 1.00 10.30 ? 251 LYS C CE  1 
ATOM   6381 N  NZ  . LYS C 1 251 ? 18.674  3.969   -41.384 1.00 9.20  ? 251 LYS C NZ  1 
ATOM   6382 N  N   . PHE C 1 252 ? 24.816  1.072   -44.299 1.00 11.24 ? 252 PHE C N   1 
ATOM   6383 C  CA  . PHE C 1 252 ? 25.882  0.646   -45.200 1.00 12.38 ? 252 PHE C CA  1 
ATOM   6384 C  C   . PHE C 1 252 ? 25.221  0.051   -46.437 1.00 15.87 ? 252 PHE C C   1 
ATOM   6385 O  O   . PHE C 1 252 ? 24.841  -1.110  -46.397 1.00 17.73 ? 252 PHE C O   1 
ATOM   6386 C  CB  . PHE C 1 252 ? 26.697  -0.436  -44.486 1.00 12.59 ? 252 PHE C CB  1 
ATOM   6387 C  CG  . PHE C 1 252 ? 27.982  -0.882  -45.140 1.00 12.19 ? 252 PHE C CG  1 
ATOM   6388 C  CD1 . PHE C 1 252 ? 29.129  -0.107  -45.084 1.00 11.05 ? 252 PHE C CD1 1 
ATOM   6389 C  CD2 . PHE C 1 252 ? 28.040  -2.145  -45.692 1.00 13.58 ? 252 PHE C CD2 1 
ATOM   6390 C  CE1 . PHE C 1 252 ? 30.309  -0.578  -45.640 1.00 11.41 ? 252 PHE C CE1 1 
ATOM   6391 C  CE2 . PHE C 1 252 ? 29.228  -2.601  -46.256 1.00 13.57 ? 252 PHE C CE2 1 
ATOM   6392 C  CZ  . PHE C 1 252 ? 30.367  -1.829  -46.171 1.00 12.36 ? 252 PHE C CZ  1 
ATOM   6393 N  N   . ASP C 1 253 ? 24.940  0.917   -47.402 1.00 20.05 ? 253 ASP C N   1 
ATOM   6394 C  CA  . ASP C 1 253 ? 24.084  0.606   -48.547 1.00 20.69 ? 253 ASP C CA  1 
ATOM   6395 C  C   . ASP C 1 253 ? 24.918  0.490   -49.819 1.00 18.09 ? 253 ASP C C   1 
ATOM   6396 O  O   . ASP C 1 253 ? 25.784  1.316   -50.083 1.00 18.78 ? 253 ASP C O   1 
ATOM   6397 C  CB  . ASP C 1 253 ? 23.098  1.758   -48.725 1.00 30.00 ? 253 ASP C CB  1 
ATOM   6398 C  CG  . ASP C 1 253 ? 21.988  1.505   -49.730 1.00 36.99 ? 253 ASP C CG  1 
ATOM   6399 O  OD1 . ASP C 1 253 ? 21.309  0.453   -49.613 1.00 47.80 ? 253 ASP C OD1 1 
ATOM   6400 O  OD2 . ASP C 1 253 ? 21.801  2.365   -50.620 1.00 49.89 ? 253 ASP C OD2 1 
ATOM   6401 N  N   . GLU C 1 254 ? 24.625  -0.561  -50.595 1.00 18.62 ? 254 GLU C N   1 
ATOM   6402 C  CA  . GLU C 1 254 ? 25.261  -0.803  -51.879 1.00 20.78 ? 254 GLU C CA  1 
ATOM   6403 C  C   . GLU C 1 254 ? 26.767  -0.891  -51.722 1.00 20.00 ? 254 GLU C C   1 
ATOM   6404 O  O   . GLU C 1 254 ? 27.490  -0.417  -52.605 1.00 21.61 ? 254 GLU C O   1 
ATOM   6405 C  CB  . GLU C 1 254 ? 24.837  0.255   -52.903 1.00 23.82 ? 254 GLU C CB  1 
ATOM   6406 C  CG  . GLU C 1 254 ? 23.340  0.206   -53.239 1.00 30.69 ? 254 GLU C CG  1 
ATOM   6407 C  CD  . GLU C 1 254 ? 22.867  -1.085  -53.898 1.00 43.39 ? 254 GLU C CD  1 
ATOM   6408 O  OE1 . GLU C 1 254 ? 23.616  -1.649  -54.746 1.00 48.64 ? 254 GLU C OE1 1 
ATOM   6409 O  OE2 . GLU C 1 254 ? 21.756  -1.542  -53.562 1.00 48.38 ? 254 GLU C OE2 1 
ATOM   6410 N  N   . ARG C 1 255 ? 27.206  -1.491  -50.610 1.00 16.49 ? 255 ARG C N   1 
ATOM   6411 C  CA  . ARG C 1 255 ? 28.638  -1.681  -50.393 1.00 14.53 ? 255 ARG C CA  1 
ATOM   6412 C  C   . ARG C 1 255 ? 28.893  -3.099  -49.893 1.00 13.34 ? 255 ARG C C   1 
ATOM   6413 O  O   . ARG C 1 255 ? 28.022  -3.746  -49.315 1.00 15.32 ? 255 ARG C O   1 
ATOM   6414 C  CB  . ARG C 1 255 ? 29.171  -0.679  -49.364 1.00 13.75 ? 255 ARG C CB  1 
ATOM   6415 C  CG  . ARG C 1 255 ? 29.097  0.778   -49.806 1.00 15.04 ? 255 ARG C CG  1 
ATOM   6416 C  CD  . ARG C 1 255 ? 29.733  1.782   -48.850 1.00 14.93 ? 255 ARG C CD  1 
ATOM   6417 N  NE  . ARG C 1 255 ? 31.111  1.391   -48.601 1.00 16.68 ? 255 ARG C NE  1 
ATOM   6418 C  CZ  . ARG C 1 255 ? 31.822  1.673   -47.491 1.00 16.01 ? 255 ARG C CZ  1 
ATOM   6419 N  NH1 . ARG C 1 255 ? 31.254  2.402   -46.535 1.00 17.03 ? 255 ARG C NH1 1 
ATOM   6420 N  NH2 . ARG C 1 255 ? 33.068  1.216   -47.416 1.00 13.16 ? 255 ARG C NH2 1 
ATOM   6421 N  N   . LEU C 1 256 ? 30.140  -3.561  -50.096 1.00 14.95 ? 256 LEU C N   1 
ATOM   6422 C  CA  . LEU C 1 256 ? 30.558  -4.866  -49.621 1.00 14.23 ? 256 LEU C CA  1 
ATOM   6423 C  C   . LEU C 1 256 ? 31.594  -4.747  -48.497 1.00 13.34 ? 256 LEU C C   1 
ATOM   6424 O  O   . LEU C 1 256 ? 32.264  -3.756  -48.343 1.00 13.46 ? 256 LEU C O   1 
ATOM   6425 C  CB  . LEU C 1 256 ? 31.186  -5.644  -50.787 1.00 17.95 ? 256 LEU C CB  1 
ATOM   6426 C  CG  . LEU C 1 256 ? 30.268  -5.934  -51.970 1.00 19.66 ? 256 LEU C CG  1 
ATOM   6427 C  CD1 . LEU C 1 256 ? 31.086  -6.380  -53.179 1.00 22.41 ? 256 LEU C CD1 1 
ATOM   6428 C  CD2 . LEU C 1 256 ? 29.286  -7.024  -51.585 1.00 21.68 ? 256 LEU C CD2 1 
ATOM   6429 N  N   . VAL C 1 257 ? 31.638  -5.791  -47.688 1.00 13.07 ? 257 VAL C N   1 
ATOM   6430 C  CA  . VAL C 1 257 ? 32.726  -6.032  -46.761 1.00 12.57 ? 257 VAL C CA  1 
ATOM   6431 C  C   . VAL C 1 257 ? 33.497  -7.216  -47.324 1.00 12.89 ? 257 VAL C C   1 
ATOM   6432 O  O   . VAL C 1 257 ? 32.906  -8.238  -47.679 1.00 13.69 ? 257 VAL C O   1 
ATOM   6433 C  CB  . VAL C 1 257 ? 32.211  -6.363  -45.362 1.00 12.90 ? 257 VAL C CB  1 
ATOM   6434 C  CG1 . VAL C 1 257 ? 33.357  -6.781  -44.436 1.00 13.34 ? 257 VAL C CG1 1 
ATOM   6435 C  CG2 . VAL C 1 257 ? 31.523  -5.178  -44.724 1.00 14.41 ? 257 VAL C CG2 1 
ATOM   6436 N  N   . TYR C 1 258 ? 34.808  -7.071  -47.434 1.00 11.64 ? 258 TYR C N   1 
ATOM   6437 C  CA  . TYR C 1 258 ? 35.635  -8.066  -48.076 1.00 12.79 ? 258 TYR C CA  1 
ATOM   6438 C  C   . TYR C 1 258 ? 36.176  -8.995  -47.008 1.00 13.84 ? 258 TYR C C   1 
ATOM   6439 O  O   . TYR C 1 258 ? 36.487  -8.564  -45.890 1.00 14.30 ? 258 TYR C O   1 
ATOM   6440 C  CB  . TYR C 1 258 ? 36.733  -7.395  -48.900 1.00 13.09 ? 258 TYR C CB  1 
ATOM   6441 C  CG  . TYR C 1 258 ? 36.146  -6.498  -49.938 1.00 15.71 ? 258 TYR C CG  1 
ATOM   6442 C  CD1 . TYR C 1 258 ? 35.649  -7.031  -51.126 1.00 17.77 ? 258 TYR C CD1 1 
ATOM   6443 C  CD2 . TYR C 1 258 ? 35.969  -5.149  -49.694 1.00 16.36 ? 258 TYR C CD2 1 
ATOM   6444 C  CE1 . TYR C 1 258 ? 35.066  -6.220  -52.088 1.00 20.06 ? 258 TYR C CE1 1 
ATOM   6445 C  CE2 . TYR C 1 258 ? 35.333  -4.336  -50.618 1.00 19.30 ? 258 TYR C CE2 1 
ATOM   6446 C  CZ  . TYR C 1 258 ? 34.928  -4.862  -51.836 1.00 19.39 ? 258 TYR C CZ  1 
ATOM   6447 O  OH  . TYR C 1 258 ? 34.291  -4.019  -52.730 1.00 23.26 ? 258 TYR C OH  1 
ATOM   6448 N  N   . THR C 1 259 ? 36.252  -10.296 -47.302 1.00 13.74 ? 259 THR C N   1 
ATOM   6449 C  CA  . THR C 1 259 ? 36.708  -11.203 -46.278 1.00 13.20 ? 259 THR C CA  1 
ATOM   6450 C  C   . THR C 1 259 ? 37.916  -11.970 -46.786 1.00 13.68 ? 259 THR C C   1 
ATOM   6451 O  O   . THR C 1 259 ? 38.044  -12.258 -47.994 1.00 14.60 ? 259 THR C O   1 
ATOM   6452 C  CB  . THR C 1 259 ? 35.595  -12.174 -45.904 1.00 12.47 ? 259 THR C CB  1 
ATOM   6453 O  OG1 . THR C 1 259 ? 35.230  -12.938 -47.072 1.00 15.53 ? 259 THR C OG1 1 
ATOM   6454 C  CG2 . THR C 1 259 ? 34.367  -11.499 -45.337 1.00 14.37 ? 259 THR C CG2 1 
ATOM   6455 N  N   . SER C 1 260 ? 38.788  -12.338 -45.845 1.00 13.71 ? 260 SER C N   1 
ATOM   6456 C  CA  . SER C 1 260 ? 40.003  -13.044 -46.239 1.00 14.45 ? 260 SER C CA  1 
ATOM   6457 C  C   . SER C 1 260 ? 39.733  -14.545 -46.243 1.00 16.63 ? 260 SER C C   1 
ATOM   6458 O  O   . SER C 1 260 ? 40.613  -15.335 -46.623 1.00 21.27 ? 260 SER C O   1 
ATOM   6459 C  CB  . SER C 1 260 ? 41.124  -12.730 -45.313 1.00 13.81 ? 260 SER C CB  1 
ATOM   6460 O  OG  . SER C 1 260 ? 40.756  -13.243 -44.048 1.00 14.64 ? 260 SER C OG  1 
ATOM   6461 N  N   . PHE C 1 261 ? 38.530  -14.911 -45.831 1.00 16.38 ? 261 PHE C N   1 
ATOM   6462 C  CA  . PHE C 1 261 ? 38.117  -16.299 -45.726 1.00 18.54 ? 261 PHE C CA  1 
ATOM   6463 C  C   . PHE C 1 261 ? 36.904  -16.507 -46.609 1.00 21.84 ? 261 PHE C C   1 
ATOM   6464 O  O   . PHE C 1 261 ? 36.192  -15.574 -46.965 1.00 23.13 ? 261 PHE C O   1 
ATOM   6465 C  CB  . PHE C 1 261 ? 37.726  -16.593 -44.275 1.00 19.00 ? 261 PHE C CB  1 
ATOM   6466 C  CG  . PHE C 1 261 ? 36.688  -15.659 -43.702 1.00 19.09 ? 261 PHE C CG  1 
ATOM   6467 C  CD1 . PHE C 1 261 ? 37.079  -14.500 -43.045 1.00 16.73 ? 261 PHE C CD1 1 
ATOM   6468 C  CD2 . PHE C 1 261 ? 35.330  -15.945 -43.770 1.00 17.91 ? 261 PHE C CD2 1 
ATOM   6469 C  CE1 . PHE C 1 261 ? 36.114  -13.673 -42.481 1.00 17.83 ? 261 PHE C CE1 1 
ATOM   6470 C  CE2 . PHE C 1 261 ? 34.360  -15.110 -43.229 1.00 21.50 ? 261 PHE C CE2 1 
ATOM   6471 C  CZ  . PHE C 1 261 ? 34.766  -13.963 -42.572 1.00 18.75 ? 261 PHE C CZ  1 
ATOM   6472 N  N   . SER C 1 262 ? 36.661  -17.774 -46.970 1.00 28.62 ? 262 SER C N   1 
ATOM   6473 C  CA  . SER C 1 262 ? 35.456  -18.053 -47.728 1.00 34.53 ? 262 SER C CA  1 
ATOM   6474 C  C   . SER C 1 262 ? 34.503  -18.939 -46.925 1.00 43.83 ? 262 SER C C   1 
ATOM   6475 O  O   . SER C 1 262 ? 33.312  -18.635 -46.780 1.00 43.21 ? 262 SER C O   1 
ATOM   6476 C  CB  . SER C 1 262 ? 35.811  -18.699 -49.028 1.00 39.97 ? 262 SER C CB  1 
ATOM   6477 O  OG  . SER C 1 262 ? 34.673  -19.367 -49.543 1.00 45.36 ? 262 SER C OG  1 
ATOM   6478 N  N   . GLN C 1 263 ? 35.043  -20.057 -46.431 1.00 41.63 ? 263 GLN C N   1 
ATOM   6479 C  CA  . GLN C 1 263 ? 34.209  -21.071 -45.798 1.00 47.63 ? 263 GLN C CA  1 
ATOM   6480 C  C   . GLN C 1 263 ? 33.850  -20.663 -44.358 1.00 49.62 ? 263 GLN C C   1 
ATOM   6481 O  O   . GLN C 1 263 ? 34.513  -19.738 -43.842 1.00 50.76 ? 263 GLN C O   1 
ATOM   6482 C  CB  . GLN C 1 263 ? 34.811  -22.476 -45.930 1.00 38.91 ? 263 GLN C CB  1 
ATOM   6483 C  CG  . GLN C 1 263 ? 36.269  -22.616 -45.499 1.00 36.06 ? 263 GLN C CG  1 
ATOM   6484 C  CD  . GLN C 1 263 ? 36.811  -23.974 -45.887 1.00 33.59 ? 263 GLN C CD  1 
ATOM   6485 O  OE1 . GLN C 1 263 ? 37.924  -24.353 -45.523 1.00 33.41 ? 263 GLN C OE1 1 
ATOM   6486 N  NE2 . GLN C 1 263 ? 36.018  -24.730 -46.641 1.00 22.40 ? 263 GLN C NE2 1 
ATOM   6487 N  N   . LYS D 1 3   ? 14.048  19.632  -45.461 1.00 33.42 ? 3   LYS D N   1 
ATOM   6488 C  CA  . LYS D 1 3   ? 14.475  18.715  -46.556 1.00 29.11 ? 3   LYS D CA  1 
ATOM   6489 C  C   . LYS D 1 3   ? 15.264  17.537  -45.964 1.00 24.44 ? 3   LYS D C   1 
ATOM   6490 O  O   . LYS D 1 3   ? 16.168  16.983  -46.600 1.00 23.85 ? 3   LYS D O   1 
ATOM   6491 C  CB  . LYS D 1 3   ? 15.352  19.505  -47.522 1.00 31.22 ? 3   LYS D CB  1 
ATOM   6492 C  CG  . LYS D 1 3   ? 16.500  20.221  -46.828 1.00 36.00 ? 3   LYS D CG  1 
ATOM   6493 C  CD  . LYS D 1 3   ? 17.121  21.291  -47.703 1.00 42.07 ? 3   LYS D CD  1 
ATOM   6494 C  CE  . LYS D 1 3   ? 18.250  20.730  -48.532 1.00 40.77 ? 3   LYS D CE  1 
ATOM   6495 N  NZ  . LYS D 1 3   ? 19.446  20.463  -47.689 1.00 35.47 ? 3   LYS D NZ  1 
ATOM   6496 N  N   . TRP D 1 4   ? 14.902  17.143  -44.724 1.00 14.93 ? 4   TRP D N   1 
ATOM   6497 C  CA  . TRP D 1 4   ? 15.561  15.993  -44.110 1.00 13.74 ? 4   TRP D CA  1 
ATOM   6498 C  C   . TRP D 1 4   ? 15.301  14.767  -44.988 1.00 12.88 ? 4   TRP D C   1 
ATOM   6499 O  O   . TRP D 1 4   ? 14.274  14.669  -45.670 1.00 14.14 ? 4   TRP D O   1 
ATOM   6500 C  CB  . TRP D 1 4   ? 15.040  15.815  -42.680 1.00 11.45 ? 4   TRP D CB  1 
ATOM   6501 C  CG  . TRP D 1 4   ? 13.580  15.522  -42.543 1.00 10.30 ? 4   TRP D CG  1 
ATOM   6502 C  CD1 . TRP D 1 4   ? 12.560  16.395  -42.317 1.00 11.57 ? 4   TRP D CD1 1 
ATOM   6503 C  CD2 . TRP D 1 4   ? 12.988  14.198  -42.481 1.00 10.78 ? 4   TRP D CD2 1 
ATOM   6504 N  NE1 . TRP D 1 4   ? 11.373  15.710  -42.192 1.00 12.56 ? 4   TRP D NE1 1 
ATOM   6505 C  CE2 . TRP D 1 4   ? 11.610  14.356  -42.275 1.00 10.52 ? 4   TRP D CE2 1 
ATOM   6506 C  CE3 . TRP D 1 4   ? 13.506  12.892  -42.613 1.00 10.31 ? 4   TRP D CE3 1 
ATOM   6507 C  CZ2 . TRP D 1 4   ? 10.716  13.282  -42.180 1.00 10.71 ? 4   TRP D CZ2 1 
ATOM   6508 C  CZ3 . TRP D 1 4   ? 12.619  11.819  -42.486 1.00 10.44 ? 4   TRP D CZ3 1 
ATOM   6509 C  CH2 . TRP D 1 4   ? 11.262  12.032  -42.286 1.00 11.26 ? 4   TRP D CH2 1 
ATOM   6510 N  N   . THR D 1 5   ? 16.252  13.853  -44.930 1.00 11.98 ? 5   THR D N   1 
ATOM   6511 C  CA  . THR D 1 5   ? 16.159  12.631  -45.714 1.00 11.62 ? 5   THR D CA  1 
ATOM   6512 C  C   . THR D 1 5   ? 16.648  11.440  -44.891 1.00 12.58 ? 5   THR D C   1 
ATOM   6513 O  O   . THR D 1 5   ? 17.016  11.609  -43.713 1.00 10.66 ? 5   THR D O   1 
ATOM   6514 C  CB  . THR D 1 5   ? 17.095  12.724  -46.943 1.00 13.77 ? 5   THR D CB  1 
ATOM   6515 O  OG1 . THR D 1 5   ? 18.433  12.699  -46.449 1.00 14.71 ? 5   THR D OG1 1 
ATOM   6516 C  CG2 . THR D 1 5   ? 16.930  13.953  -47.822 1.00 14.41 ? 5   THR D CG2 1 
ATOM   6517 N  N   . TYR D 1 6   ? 16.764  10.268  -45.522 1.00 10.92 ? 6   TYR D N   1 
ATOM   6518 C  CA  . TYR D 1 6   ? 17.354  9.102   -44.883 1.00 11.03 ? 6   TYR D CA  1 
ATOM   6519 C  C   . TYR D 1 6   ? 18.703  8.706   -45.460 1.00 12.12 ? 6   TYR D C   1 
ATOM   6520 O  O   . TYR D 1 6   ? 19.260  7.674   -45.140 1.00 12.04 ? 6   TYR D O   1 
ATOM   6521 C  CB  . TYR D 1 6   ? 16.405  7.907   -45.029 1.00 10.29 ? 6   TYR D CB  1 
ATOM   6522 C  CG  . TYR D 1 6   ? 15.170  8.010   -44.169 1.00 9.37  ? 6   TYR D CG  1 
ATOM   6523 C  CD1 . TYR D 1 6   ? 15.160  7.545   -42.852 1.00 9.15  ? 6   TYR D CD1 1 
ATOM   6524 C  CD2 . TYR D 1 6   ? 14.003  8.551   -44.669 1.00 9.09  ? 6   TYR D CD2 1 
ATOM   6525 C  CE1 . TYR D 1 6   ? 14.022  7.560   -42.061 1.00 8.77  ? 6   TYR D CE1 1 
ATOM   6526 C  CE2 . TYR D 1 6   ? 12.852  8.597   -43.881 1.00 9.50  ? 6   TYR D CE2 1 
ATOM   6527 C  CZ  . TYR D 1 6   ? 12.849  8.089   -42.576 1.00 8.29  ? 6   TYR D CZ  1 
ATOM   6528 O  OH  . TYR D 1 6   ? 11.689  8.144   -41.856 1.00 9.30  ? 6   TYR D OH  1 
ATOM   6529 N  N   . PHE D 1 7   ? 19.244  9.541   -46.337 1.00 13.98 ? 7   PHE D N   1 
ATOM   6530 C  CA  . PHE D 1 7   ? 20.519  9.201   -46.941 1.00 17.86 ? 7   PHE D CA  1 
ATOM   6531 C  C   . PHE D 1 7   ? 21.251  10.489  -47.300 1.00 17.87 ? 7   PHE D C   1 
ATOM   6532 O  O   . PHE D 1 7   ? 20.609  11.411  -47.822 1.00 21.49 ? 7   PHE D O   1 
ATOM   6533 C  CB  . PHE D 1 7   ? 20.302  8.353   -48.207 1.00 24.08 ? 7   PHE D CB  1 
ATOM   6534 C  CG  . PHE D 1 7   ? 21.579  8.060   -48.951 1.00 30.26 ? 7   PHE D CG  1 
ATOM   6535 C  CD1 . PHE D 1 7   ? 22.447  7.069   -48.497 1.00 33.22 ? 7   PHE D CD1 1 
ATOM   6536 C  CD2 . PHE D 1 7   ? 21.944  8.808   -50.070 1.00 34.33 ? 7   PHE D CD2 1 
ATOM   6537 C  CE1 . PHE D 1 7   ? 23.635  6.797   -49.163 1.00 35.16 ? 7   PHE D CE1 1 
ATOM   6538 C  CE2 . PHE D 1 7   ? 23.139  8.543   -50.727 1.00 35.35 ? 7   PHE D CE2 1 
ATOM   6539 C  CZ  . PHE D 1 7   ? 23.978  7.541   -50.275 1.00 37.49 ? 7   PHE D CZ  1 
ATOM   6540 N  N   . GLY D 1 8   ? 22.585  10.483  -47.110 1.00 17.55 ? 8   GLY D N   1 
ATOM   6541 C  CA  . GLY D 1 8   ? 23.380  11.606  -47.585 1.00 18.79 ? 8   GLY D CA  1 
ATOM   6542 C  C   . GLY D 1 8   ? 23.427  12.727  -46.556 1.00 20.16 ? 8   GLY D C   1 
ATOM   6543 O  O   . GLY D 1 8   ? 23.164  12.520  -45.367 1.00 19.53 ? 8   GLY D O   1 
ATOM   6544 N  N   . PRO D 1 9   ? 23.813  13.941  -46.976 1.00 19.66 ? 9   PRO D N   1 
ATOM   6545 C  CA  . PRO D 1 9   ? 24.161  15.003  -46.047 1.00 20.16 ? 9   PRO D CA  1 
ATOM   6546 C  C   . PRO D 1 9   ? 23.057  15.404  -45.083 1.00 17.26 ? 9   PRO D C   1 
ATOM   6547 O  O   . PRO D 1 9   ? 23.365  15.942  -44.020 1.00 19.47 ? 9   PRO D O   1 
ATOM   6548 C  CB  . PRO D 1 9   ? 24.483  16.192  -46.985 1.00 20.99 ? 9   PRO D CB  1 
ATOM   6549 C  CG  . PRO D 1 9   ? 24.913  15.547  -48.254 1.00 23.54 ? 9   PRO D CG  1 
ATOM   6550 C  CD  . PRO D 1 9   ? 24.078  14.289  -48.393 1.00 20.46 ? 9   PRO D CD  1 
ATOM   6551 N  N   . ASP D 1 10  ? 21.780  15.226  -45.483 1.00 15.66 ? 10  ASP D N   1 
ATOM   6552 C  CA  . ASP D 1 10  ? 20.645  15.604  -44.664 1.00 14.69 ? 10  ASP D CA  1 
ATOM   6553 C  C   . ASP D 1 10  ? 19.995  14.367  -44.018 1.00 12.24 ? 10  ASP D C   1 
ATOM   6554 O  O   . ASP D 1 10  ? 18.867  14.482  -43.589 1.00 12.18 ? 10  ASP D O   1 
ATOM   6555 C  CB  . ASP D 1 10  ? 19.615  16.400  -45.468 1.00 16.25 ? 10  ASP D CB  1 
ATOM   6556 C  CG  . ASP D 1 10  ? 20.209  17.668  -46.071 1.00 22.37 ? 10  ASP D CG  1 
ATOM   6557 O  OD1 . ASP D 1 10  ? 20.794  18.434  -45.303 1.00 25.76 ? 10  ASP D OD1 1 
ATOM   6558 O  OD2 . ASP D 1 10  ? 20.121  17.820  -47.300 1.00 25.54 ? 10  ASP D OD2 1 
ATOM   6559 N  N   . GLY D 1 11  ? 20.744  13.269  -43.972 1.00 12.09 ? 11  GLY D N   1 
ATOM   6560 C  CA  . GLY D 1 11  ? 20.262  12.020  -43.376 1.00 9.28  ? 11  GLY D CA  1 
ATOM   6561 C  C   . GLY D 1 11  ? 20.329  12.072  -41.850 1.00 9.23  ? 11  GLY D C   1 
ATOM   6562 O  O   . GLY D 1 11  ? 20.496  13.121  -41.220 1.00 9.53  ? 11  GLY D O   1 
ATOM   6563 N  N   . GLU D 1 12  ? 20.059  10.905  -41.258 1.00 8.29  ? 12  GLU D N   1 
ATOM   6564 C  CA  . GLU D 1 12  ? 19.637  10.845  -39.878 1.00 7.40  ? 12  GLU D CA  1 
ATOM   6565 C  C   . GLU D 1 12  ? 20.687  11.327  -38.868 1.00 7.66  ? 12  GLU D C   1 
ATOM   6566 O  O   . GLU D 1 12  ? 20.293  11.791  -37.819 1.00 8.39  ? 12  GLU D O   1 
ATOM   6567 C  CB  . GLU D 1 12  ? 19.168  9.441   -39.502 1.00 7.79  ? 12  GLU D CB  1 
ATOM   6568 C  CG  . GLU D 1 12  ? 20.238  8.404   -39.350 1.00 8.20  ? 12  GLU D CG  1 
ATOM   6569 C  CD  . GLU D 1 12  ? 19.658  7.000   -39.365 1.00 8.52  ? 12  GLU D CD  1 
ATOM   6570 O  OE1 . GLU D 1 12  ? 19.280  6.507   -38.307 1.00 9.33  ? 12  GLU D OE1 1 
ATOM   6571 O  OE2 . GLU D 1 12  ? 19.558  6.465   -40.488 1.00 10.30 ? 12  GLU D OE2 1 
ATOM   6572 N  N   . ASN D 1 13  ? 21.977  11.240  -39.194 1.00 7.72  ? 13  ASN D N   1 
ATOM   6573 C  CA  . ASN D 1 13  ? 22.974  11.755  -38.272 1.00 8.26  ? 13  ASN D CA  1 
ATOM   6574 C  C   . ASN D 1 13  ? 22.980  13.272  -38.284 1.00 9.56  ? 13  ASN D C   1 
ATOM   6575 O  O   . ASN D 1 13  ? 23.604  13.817  -37.373 1.00 9.94  ? 13  ASN D O   1 
ATOM   6576 C  CB  . ASN D 1 13  ? 24.354  11.202  -38.592 1.00 9.30  ? 13  ASN D CB  1 
ATOM   6577 C  CG  . ASN D 1 13  ? 24.511  9.724   -38.323 1.00 8.69  ? 13  ASN D CG  1 
ATOM   6578 O  OD1 . ASN D 1 13  ? 23.598  9.076   -37.814 1.00 9.26  ? 13  ASN D OD1 1 
ATOM   6579 N  ND2 . ASN D 1 13  ? 25.690  9.237   -38.619 1.00 9.04  ? 13  ASN D ND2 1 
ATOM   6580 N  N   . SER D 1 14  ? 22.305  13.928  -39.230 1.00 9.00  ? 14  SER D N   1 
ATOM   6581 C  CA  . SER D 1 14  ? 22.286  15.386  -39.311 1.00 8.70  ? 14  SER D CA  1 
ATOM   6582 C  C   . SER D 1 14  ? 20.944  15.929  -38.863 1.00 9.34  ? 14  SER D C   1 
ATOM   6583 O  O   . SER D 1 14  ? 20.812  17.136  -38.765 1.00 10.26 ? 14  SER D O   1 
ATOM   6584 C  CB  . SER D 1 14  ? 22.572  15.790  -40.726 1.00 9.51  ? 14  SER D CB  1 
ATOM   6585 O  OG  . SER D 1 14  ? 23.936  15.494  -41.010 1.00 11.64 ? 14  SER D OG  1 
ATOM   6586 N  N   . TRP D 1 15  ? 19.919  15.119  -38.573 1.00 8.20  ? 15  TRP D N   1 
ATOM   6587 C  CA  . TRP D 1 15  ? 18.611  15.672  -38.231 1.00 8.21  ? 15  TRP D CA  1 
ATOM   6588 C  C   . TRP D 1 15  ? 18.676  16.615  -37.042 1.00 8.34  ? 15  TRP D C   1 
ATOM   6589 O  O   . TRP D 1 15  ? 17.964  17.631  -37.051 1.00 8.85  ? 15  TRP D O   1 
ATOM   6590 C  CB  . TRP D 1 15  ? 17.607  14.551  -37.881 1.00 8.27  ? 15  TRP D CB  1 
ATOM   6591 C  CG  . TRP D 1 15  ? 17.237  13.654  -39.014 1.00 8.10  ? 15  TRP D CG  1 
ATOM   6592 C  CD1 . TRP D 1 15  ? 17.517  13.798  -40.331 1.00 8.24  ? 15  TRP D CD1 1 
ATOM   6593 C  CD2 . TRP D 1 15  ? 16.479  12.433  -38.877 1.00 7.57  ? 15  TRP D CD2 1 
ATOM   6594 N  NE1 . TRP D 1 15  ? 16.939  12.775  -41.046 1.00 8.84  ? 15  TRP D NE1 1 
ATOM   6595 C  CE2 . TRP D 1 15  ? 16.298  11.937  -40.176 1.00 7.49  ? 15  TRP D CE2 1 
ATOM   6596 C  CE3 . TRP D 1 15  ? 15.877  11.763  -37.787 1.00 7.73  ? 15  TRP D CE3 1 
ATOM   6597 C  CZ2 . TRP D 1 15  ? 15.602  10.742  -40.440 1.00 7.88  ? 15  TRP D CZ2 1 
ATOM   6598 C  CZ3 . TRP D 1 15  ? 15.183  10.588  -38.045 1.00 8.57  ? 15  TRP D CZ3 1 
ATOM   6599 C  CH2 . TRP D 1 15  ? 15.060  10.091  -39.355 1.00 7.81  ? 15  TRP D CH2 1 
ATOM   6600 N  N   . SER D 1 16  ? 19.544  16.317  -36.073 1.00 8.29  ? 16  SER D N   1 
ATOM   6601 C  CA  . SER D 1 16  ? 19.625  17.109  -34.848 1.00 9.55  ? 16  SER D CA  1 
ATOM   6602 C  C   . SER D 1 16  ? 20.102  18.527  -35.130 1.00 10.41 ? 16  SER D C   1 
ATOM   6603 O  O   . SER D 1 16  ? 19.915  19.362  -34.261 1.00 11.48 ? 16  SER D O   1 
ATOM   6604 C  CB  . SER D 1 16  ? 20.568  16.478  -33.867 1.00 10.98 ? 16  SER D CB  1 
ATOM   6605 O  OG  . SER D 1 16  ? 21.868  16.490  -34.383 1.00 14.99 ? 16  SER D OG  1 
ATOM   6606 N  N   . LYS D 1 17  ? 20.705  18.781  -36.288 1.00 9.15  ? 17  LYS D N   1 
ATOM   6607 C  CA  . LYS D 1 17  ? 21.163  20.141  -36.585 1.00 9.93  ? 17  LYS D CA  1 
ATOM   6608 C  C   . LYS D 1 17  ? 19.973  21.073  -36.708 1.00 11.32 ? 17  LYS D C   1 
ATOM   6609 O  O   . LYS D 1 17  ? 20.106  22.290  -36.447 1.00 11.74 ? 17  LYS D O   1 
ATOM   6610 C  CB  . LYS D 1 17  ? 21.942  20.174  -37.892 1.00 9.78  ? 17  LYS D CB  1 
ATOM   6611 C  CG  . LYS D 1 17  ? 23.198  19.325  -37.905 1.00 10.83 ? 17  LYS D CG  1 
ATOM   6612 C  CD  . LYS D 1 17  ? 23.809  19.338  -39.281 1.00 11.18 ? 17  LYS D CD  1 
ATOM   6613 C  CE  . LYS D 1 17  ? 24.934  18.350  -39.491 1.00 11.13 ? 17  LYS D CE  1 
ATOM   6614 N  NZ  . LYS D 1 17  ? 25.592  18.580  -40.801 1.00 13.09 ? 17  LYS D NZ  1 
ATOM   6615 N  N   . LYS D 1 18  ? 18.823  20.583  -37.159 1.00 10.75 ? 18  LYS D N   1 
ATOM   6616 C  CA  . LYS D 1 18  ? 17.591  21.363  -37.345 1.00 11.07 ? 18  LYS D CA  1 
ATOM   6617 C  C   . LYS D 1 18  ? 16.513  21.023  -36.314 1.00 11.78 ? 18  LYS D C   1 
ATOM   6618 O  O   . LYS D 1 18  ? 15.579  21.785  -36.141 1.00 13.49 ? 18  LYS D O   1 
ATOM   6619 C  CB  . LYS D 1 18  ? 17.031  21.224  -38.767 1.00 12.88 ? 18  LYS D CB  1 
ATOM   6620 C  CG  . LYS D 1 18  ? 17.893  21.897  -39.866 1.00 16.23 ? 18  LYS D CG  1 
ATOM   6621 C  CD  . LYS D 1 18  ? 17.364  21.640  -41.276 1.00 19.50 ? 18  LYS D CD  1 
ATOM   6622 C  CE  . LYS D 1 18  ? 18.161  22.424  -42.305 1.00 24.18 ? 18  LYS D CE  1 
ATOM   6623 N  NZ  . LYS D 1 18  ? 17.674  22.130  -43.682 1.00 28.72 ? 18  LYS D NZ  1 
ATOM   6624 N  N   . TYR D 1 19  ? 16.551  19.814  -35.767 1.00 9.70  ? 19  TYR D N   1 
ATOM   6625 C  CA  . TYR D 1 19  ? 15.453  19.283  -34.975 1.00 10.29 ? 19  TYR D CA  1 
ATOM   6626 C  C   . TYR D 1 19  ? 16.074  18.805  -33.689 1.00 10.99 ? 19  TYR D C   1 
ATOM   6627 O  O   . TYR D 1 19  ? 16.551  17.645  -33.609 1.00 9.80  ? 19  TYR D O   1 
ATOM   6628 C  CB  . TYR D 1 19  ? 14.773  18.123  -35.742 1.00 10.13 ? 19  TYR D CB  1 
ATOM   6629 C  CG  . TYR D 1 19  ? 14.157  18.507  -37.051 1.00 10.02 ? 19  TYR D CG  1 
ATOM   6630 C  CD1 . TYR D 1 19  ? 12.953  19.183  -37.112 1.00 11.51 ? 19  TYR D CD1 1 
ATOM   6631 C  CD2 . TYR D 1 19  ? 14.823  18.282  -38.251 1.00 11.00 ? 19  TYR D CD2 1 
ATOM   6632 C  CE1 . TYR D 1 19  ? 12.425  19.569  -38.323 1.00 12.80 ? 19  TYR D CE1 1 
ATOM   6633 C  CE2 . TYR D 1 19  ? 14.300  18.640  -39.471 1.00 12.31 ? 19  TYR D CE2 1 
ATOM   6634 C  CZ  . TYR D 1 19  ? 13.076  19.267  -39.489 1.00 13.57 ? 19  TYR D CZ  1 
ATOM   6635 O  OH  . TYR D 1 19  ? 12.517  19.648  -40.691 1.00 17.22 ? 19  TYR D OH  1 
ATOM   6636 N  N   . PRO D 1 20  ? 16.218  19.666  -32.667 1.00 10.70 ? 20  PRO D N   1 
ATOM   6637 C  CA  . PRO D 1 20  ? 17.002  19.308  -31.502 1.00 11.40 ? 20  PRO D CA  1 
ATOM   6638 C  C   . PRO D 1 20  ? 16.539  18.039  -30.770 1.00 10.38 ? 20  PRO D C   1 
ATOM   6639 O  O   . PRO D 1 20  ? 17.412  17.380  -30.196 1.00 11.63 ? 20  PRO D O   1 
ATOM   6640 C  CB  . PRO D 1 20  ? 16.891  20.547  -30.554 1.00 12.01 ? 20  PRO D CB  1 
ATOM   6641 C  CG  . PRO D 1 20  ? 16.246  21.576  -31.350 1.00 15.76 ? 20  PRO D CG  1 
ATOM   6642 C  CD  . PRO D 1 20  ? 15.727  21.067  -32.661 1.00 10.68 ? 20  PRO D CD  1 
ATOM   6643 N  N   . SER D 1 21  ? 15.229  17.715  -30.806 1.00 10.66 ? 21  SER D N   1 
ATOM   6644 C  CA  . SER D 1 21  ? 14.815  16.506  -30.091 1.00 10.38 ? 21  SER D CA  1 
ATOM   6645 C  C   . SER D 1 21  ? 15.390  15.234  -30.723 1.00 10.03 ? 21  SER D C   1 
ATOM   6646 O  O   . SER D 1 21  ? 15.472  14.232  -30.026 1.00 10.05 ? 21  SER D O   1 
ATOM   6647 C  CB  . SER D 1 21  ? 13.327  16.398  -30.017 1.00 11.07 ? 21  SER D CB  1 
ATOM   6648 O  OG  . SER D 1 21  ? 12.788  17.454  -29.211 1.00 13.78 ? 21  SER D OG  1 
ATOM   6649 N  N   . CYS D 1 22  ? 15.828  15.268  -31.975 1.00 10.28 ? 22  CYS D N   1 
ATOM   6650 C  CA  . CYS D 1 22  ? 16.399  14.090  -32.608 1.00 9.71  ? 22  CYS D CA  1 
ATOM   6651 C  C   . CYS D 1 22  ? 17.740  13.785  -31.947 1.00 11.71 ? 22  CYS D C   1 
ATOM   6652 O  O   . CYS D 1 22  ? 18.235  12.692  -32.143 1.00 11.80 ? 22  CYS D O   1 
ATOM   6653 C  CB  . CYS D 1 22  ? 16.554  14.322  -34.112 1.00 10.34 ? 22  CYS D CB  1 
ATOM   6654 S  SG  . CYS D 1 22  ? 15.023  14.589  -35.014 1.00 10.21 ? 22  CYS D SG  1 
ATOM   6655 N  N   . GLY D 1 23  ? 18.382  14.729  -31.203 1.00 11.16 ? 23  GLY D N   1 
ATOM   6656 C  CA  . GLY D 1 23  ? 19.595  14.512  -30.420 1.00 11.77 ? 23  GLY D CA  1 
ATOM   6657 C  C   . GLY D 1 23  ? 19.313  14.431  -28.918 1.00 13.65 ? 23  GLY D C   1 
ATOM   6658 O  O   . GLY D 1 23  ? 20.263  14.450  -28.090 1.00 15.95 ? 23  GLY D O   1 
ATOM   6659 N  N   . GLY D 1 24  ? 18.038  14.369  -28.555 1.00 12.10 ? 24  GLY D N   1 
ATOM   6660 C  CA  . GLY D 1 24  ? 17.604  14.319  -27.158 1.00 15.59 ? 24  GLY D CA  1 
ATOM   6661 C  C   . GLY D 1 24  ? 17.495  12.897  -26.616 1.00 16.80 ? 24  GLY D C   1 
ATOM   6662 O  O   . GLY D 1 24  ? 18.003  11.937  -27.186 1.00 17.37 ? 24  GLY D O   1 
ATOM   6663 N  N   . LEU D 1 25  ? 16.836  12.772  -25.473 1.00 18.21 ? 25  LEU D N   1 
ATOM   6664 C  CA  . LEU D 1 25  ? 16.738  11.453  -24.861 1.00 17.46 ? 25  LEU D CA  1 
ATOM   6665 C  C   . LEU D 1 25  ? 15.496  10.747  -25.426 1.00 15.21 ? 25  LEU D C   1 
ATOM   6666 O  O   . LEU D 1 25  ? 14.633  11.354  -26.089 1.00 15.55 ? 25  LEU D O   1 
ATOM   6667 C  CB  . LEU D 1 25  ? 16.653  11.563  -23.322 1.00 21.08 ? 25  LEU D CB  1 
ATOM   6668 C  CG  . LEU D 1 25  ? 17.884  12.158  -22.608 1.00 20.90 ? 25  LEU D CG  1 
ATOM   6669 C  CD1 . LEU D 1 25  ? 17.552  12.486  -21.147 1.00 24.80 ? 25  LEU D CD1 1 
ATOM   6670 C  CD2 . LEU D 1 25  ? 19.074  11.209  -22.676 1.00 22.90 ? 25  LEU D CD2 1 
ATOM   6671 N  N   . LEU D 1 26  ? 15.391  9.443   -25.093 1.00 14.94 ? 26  LEU D N   1 
ATOM   6672 C  CA  . LEU D 1 26  ? 14.191  8.628   -25.287 1.00 14.73 ? 26  LEU D CA  1 
ATOM   6673 C  C   . LEU D 1 26  ? 13.764  8.495   -26.749 1.00 11.63 ? 26  LEU D C   1 
ATOM   6674 O  O   . LEU D 1 26  ? 12.577  8.571   -27.110 1.00 11.94 ? 26  LEU D O   1 
ATOM   6675 C  CB  . LEU D 1 26  ? 13.012  9.182   -24.493 1.00 17.51 ? 26  LEU D CB  1 
ATOM   6676 C  CG  . LEU D 1 26  ? 13.273  9.317   -22.983 1.00 23.49 ? 26  LEU D CG  1 
ATOM   6677 C  CD1 . LEU D 1 26  ? 11.950  9.493   -22.278 1.00 24.27 ? 26  LEU D CD1 1 
ATOM   6678 C  CD2 . LEU D 1 26  ? 14.039  8.121   -22.380 1.00 25.60 ? 26  LEU D CD2 1 
ATOM   6679 N  N   . GLN D 1 27  ? 14.775  8.290   -27.578 1.00 11.47 ? 27  GLN D N   1 
ATOM   6680 C  CA  . GLN D 1 27  ? 14.537  8.191   -29.025 1.00 9.47  ? 27  GLN D CA  1 
ATOM   6681 C  C   . GLN D 1 27  ? 14.089  6.791   -29.420 1.00 8.75  ? 27  GLN D C   1 
ATOM   6682 O  O   . GLN D 1 27  ? 14.483  5.781   -28.824 1.00 10.18 ? 27  GLN D O   1 
ATOM   6683 C  CB  . GLN D 1 27  ? 15.742  8.662   -29.829 1.00 9.85  ? 27  GLN D CB  1 
ATOM   6684 C  CG  . GLN D 1 27  ? 16.057  10.134  -29.550 1.00 10.24 ? 27  GLN D CG  1 
ATOM   6685 C  CD  . GLN D 1 27  ? 14.983  10.971  -30.191 1.00 10.27 ? 27  GLN D CD  1 
ATOM   6686 O  OE1 . GLN D 1 27  ? 15.011  11.119  -31.428 1.00 10.16 ? 27  GLN D OE1 1 
ATOM   6687 N  NE2 . GLN D 1 27  ? 14.079  11.544  -29.421 1.00 10.12 ? 27  GLN D NE2 1 
ATOM   6688 N  N   . SER D 1 28  ? 13.326  6.752   -30.506 1.00 8.45  ? 28  SER D N   1 
ATOM   6689 C  CA  . SER D 1 28  ? 12.878  5.525   -31.155 1.00 7.98  ? 28  SER D CA  1 
ATOM   6690 C  C   . SER D 1 28  ? 13.449  5.457   -32.560 1.00 8.54  ? 28  SER D C   1 
ATOM   6691 O  O   . SER D 1 28  ? 13.738  6.507   -33.166 1.00 8.94  ? 28  SER D O   1 
ATOM   6692 C  CB  . SER D 1 28  ? 11.405  5.504   -31.211 1.00 7.37  ? 28  SER D CB  1 
ATOM   6693 O  OG  . SER D 1 28  ? 10.867  5.429   -29.882 1.00 7.99  ? 28  SER D OG  1 
ATOM   6694 N  N   . PRO D 1 29  ? 13.554  4.298   -33.218 1.00 6.96  ? 29  PRO D N   1 
ATOM   6695 C  CA  . PRO D 1 29  ? 13.184  2.980   -32.671 1.00 8.17  ? 29  PRO D CA  1 
ATOM   6696 C  C   . PRO D 1 29  ? 14.330  2.383   -31.875 1.00 8.03  ? 29  PRO D C   1 
ATOM   6697 O  O   . PRO D 1 29  ? 15.369  2.983   -31.716 1.00 8.40  ? 29  PRO D O   1 
ATOM   6698 C  CB  . PRO D 1 29  ? 12.972  2.230   -34.023 1.00 8.52  ? 29  PRO D CB  1 
ATOM   6699 C  CG  . PRO D 1 29  ? 14.099  2.758   -34.898 1.00 8.00  ? 29  PRO D CG  1 
ATOM   6700 C  CD  . PRO D 1 29  ? 14.074  4.228   -34.602 1.00 8.42  ? 29  PRO D CD  1 
ATOM   6701 N  N   . ILE D 1 30  ? 14.092  1.163   -31.370 1.00 7.64  ? 30  ILE D N   1 
ATOM   6702 C  CA  . ILE D 1 30  ? 15.071  0.452   -30.554 1.00 8.60  ? 30  ILE D CA  1 
ATOM   6703 C  C   . ILE D 1 30  ? 15.055  -1.012  -30.948 1.00 8.06  ? 30  ILE D C   1 
ATOM   6704 O  O   . ILE D 1 30  ? 14.159  -1.497  -31.648 1.00 8.53  ? 30  ILE D O   1 
ATOM   6705 C  CB  . ILE D 1 30  ? 14.736  0.591   -29.062 1.00 9.27  ? 30  ILE D CB  1 
ATOM   6706 C  CG1 . ILE D 1 30  ? 13.300  0.120   -28.744 1.00 10.61 ? 30  ILE D CG1 1 
ATOM   6707 C  CG2 . ILE D 1 30  ? 15.002  2.011   -28.537 1.00 10.98 ? 30  ILE D CG2 1 
ATOM   6708 C  CD1 . ILE D 1 30  ? 13.036  -0.077  -27.265 1.00 13.29 ? 30  ILE D CD1 1 
ATOM   6709 N  N   . ASP D 1 31  ? 16.127  -1.682  -30.506 1.00 9.03  ? 31  ASP D N   1 
ATOM   6710 C  CA  . ASP D 1 31  ? 16.215  -3.134  -30.664 1.00 9.79  ? 31  ASP D CA  1 
ATOM   6711 C  C   . ASP D 1 31  ? 15.579  -3.825  -29.467 1.00 11.54 ? 31  ASP D C   1 
ATOM   6712 O  O   . ASP D 1 31  ? 15.975  -3.601  -28.321 1.00 13.09 ? 31  ASP D O   1 
ATOM   6713 C  CB  . ASP D 1 31  ? 17.677  -3.545  -30.762 1.00 11.26 ? 31  ASP D CB  1 
ATOM   6714 C  CG  . ASP D 1 31  ? 17.824  -5.060  -30.885 1.00 12.03 ? 31  ASP D CG  1 
ATOM   6715 O  OD1 . ASP D 1 31  ? 17.265  -5.660  -31.791 1.00 11.81 ? 31  ASP D OD1 1 
ATOM   6716 O  OD2 . ASP D 1 31  ? 18.458  -5.671  -30.002 1.00 15.32 ? 31  ASP D OD2 1 
ATOM   6717 N  N   . LEU D 1 32  ? 14.724  -4.776  -29.720 1.00 10.69 ? 32  LEU D N   1 
ATOM   6718 C  CA  . LEU D 1 32  ? 13.967  -5.471  -28.675 1.00 11.33 ? 32  LEU D CA  1 
ATOM   6719 C  C   . LEU D 1 32  ? 14.708  -6.763  -28.391 1.00 12.04 ? 32  LEU D C   1 
ATOM   6720 O  O   . LEU D 1 32  ? 14.750  -7.636  -29.248 1.00 13.21 ? 32  LEU D O   1 
ATOM   6721 C  CB  . LEU D 1 32  ? 12.558  -5.743  -29.210 1.00 12.35 ? 32  LEU D CB  1 
ATOM   6722 C  CG  . LEU D 1 32  ? 11.775  -4.490  -29.554 1.00 13.06 ? 32  LEU D CG  1 
ATOM   6723 C  CD1 . LEU D 1 32  ? 10.502  -4.849  -30.285 1.00 12.82 ? 32  LEU D CD1 1 
ATOM   6724 C  CD2 . LEU D 1 32  ? 11.486  -3.640  -28.309 1.00 15.76 ? 32  LEU D CD2 1 
ATOM   6725 N  N   . HIS D 1 33  ? 15.459  -6.822  -27.279 1.00 12.13 ? 33  HIS D N   1 
ATOM   6726 C  CA  . HIS D 1 33  ? 16.263  -8.019  -27.019 1.00 11.88 ? 33  HIS D CA  1 
ATOM   6727 C  C   . HIS D 1 33  ? 16.125  -8.331  -25.535 1.00 12.65 ? 33  HIS D C   1 
ATOM   6728 O  O   . HIS D 1 33  ? 15.833  -7.467  -24.714 1.00 12.21 ? 33  HIS D O   1 
ATOM   6729 C  CB  . HIS D 1 33  ? 17.743  -7.853  -27.471 1.00 13.48 ? 33  HIS D CB  1 
ATOM   6730 C  CG  . HIS D 1 33  ? 18.495  -6.790  -26.748 1.00 13.96 ? 33  HIS D CG  1 
ATOM   6731 N  ND1 . HIS D 1 33  ? 18.386  -5.465  -27.055 1.00 16.09 ? 33  HIS D ND1 1 
ATOM   6732 C  CD2 . HIS D 1 33  ? 19.364  -6.844  -25.701 1.00 16.27 ? 33  HIS D CD2 1 
ATOM   6733 C  CE1 . HIS D 1 33  ? 19.124  -4.734  -26.235 1.00 20.26 ? 33  HIS D CE1 1 
ATOM   6734 N  NE2 . HIS D 1 33  ? 19.763  -5.593  -25.427 1.00 17.16 ? 33  HIS D NE2 1 
ATOM   6735 N  N   . SER D 1 34  ? 16.495  -9.586  -25.215 1.00 12.95 ? 34  SER D N   1 
ATOM   6736 C  CA  . SER D 1 34  ? 16.124  -10.134 -23.907 1.00 14.09 ? 34  SER D CA  1 
ATOM   6737 C  C   . SER D 1 34  ? 16.619  -9.322  -22.714 1.00 14.03 ? 34  SER D C   1 
ATOM   6738 O  O   . SER D 1 34  ? 15.888  -9.182  -21.731 1.00 13.95 ? 34  SER D O   1 
ATOM   6739 C  CB  . SER D 1 34  ? 16.555  -11.551 -23.823 1.00 17.53 ? 34  SER D CB  1 
ATOM   6740 O  OG  . SER D 1 34  ? 17.945  -11.610 -23.799 1.00 22.04 ? 34  SER D OG  1 
ATOM   6741 N  N   . ASP D 1 35  ? 17.846  -8.797  -22.734 1.00 12.76 ? 35  ASP D N   1 
ATOM   6742 C  CA  . ASP D 1 35  ? 18.394  -8.237  -21.515 1.00 14.14 ? 35  ASP D CA  1 
ATOM   6743 C  C   . ASP D 1 35  ? 17.584  -7.024  -21.057 1.00 13.49 ? 35  ASP D C   1 
ATOM   6744 O  O   . ASP D 1 35  ? 17.690  -6.608  -19.911 1.00 16.01 ? 35  ASP D O   1 
ATOM   6745 C  CB  . ASP D 1 35  ? 19.817  -7.722  -21.769 1.00 17.60 ? 35  ASP D CB  1 
ATOM   6746 C  CG  . ASP D 1 35  ? 20.747  -8.712  -22.441 1.00 21.70 ? 35  ASP D CG  1 
ATOM   6747 O  OD1 . ASP D 1 35  ? 20.483  -9.087  -23.645 1.00 23.45 ? 35  ASP D OD1 1 
ATOM   6748 O  OD2 . ASP D 1 35  ? 21.734  -9.121  -21.757 1.00 18.96 ? 35  ASP D OD2 1 
ATOM   6749 N  N   . ILE D 1 36  ? 16.832  -6.373  -21.980 1.00 12.75 ? 36  ILE D N   1 
ATOM   6750 C  CA  . ILE D 1 36  ? 16.127  -5.158  -21.610 1.00 13.26 ? 36  ILE D CA  1 
ATOM   6751 C  C   . ILE D 1 36  ? 14.618  -5.365  -21.584 1.00 12.99 ? 36  ILE D C   1 
ATOM   6752 O  O   . ILE D 1 36  ? 13.885  -4.380  -21.409 1.00 14.81 ? 36  ILE D O   1 
ATOM   6753 C  CB  . ILE D 1 36  ? 16.541  -3.909  -22.439 1.00 14.95 ? 36  ILE D CB  1 
ATOM   6754 C  CG1 . ILE D 1 36  ? 16.464  -4.134  -23.948 1.00 16.65 ? 36  ILE D CG1 1 
ATOM   6755 C  CG2 . ILE D 1 36  ? 17.973  -3.513  -22.079 1.00 18.77 ? 36  ILE D CG2 1 
ATOM   6756 C  CD1 . ILE D 1 36  ? 15.069  -4.340  -24.487 1.00 16.68 ? 36  ILE D CD1 1 
ATOM   6757 N  N   . LEU D 1 37  ? 14.148  -6.631  -21.673 1.00 12.34 ? 37  LEU D N   1 
ATOM   6758 C  CA  . LEU D 1 37  ? 12.712  -6.909  -21.571 1.00 12.82 ? 37  LEU D CA  1 
ATOM   6759 C  C   . LEU D 1 37  ? 12.305  -7.266  -20.148 1.00 14.57 ? 37  LEU D C   1 
ATOM   6760 O  O   . LEU D 1 37  ? 13.044  -7.966  -19.444 1.00 16.00 ? 37  LEU D O   1 
ATOM   6761 C  CB  . LEU D 1 37  ? 12.351  -8.094  -22.460 1.00 12.67 ? 37  LEU D CB  1 
ATOM   6762 C  CG  . LEU D 1 37  ? 12.620  -7.887  -23.958 1.00 14.06 ? 37  LEU D CG  1 
ATOM   6763 C  CD1 . LEU D 1 37  ? 12.208  -9.127  -24.741 1.00 17.05 ? 37  LEU D CD1 1 
ATOM   6764 C  CD2 . LEU D 1 37  ? 11.889  -6.649  -24.475 1.00 14.24 ? 37  LEU D CD2 1 
ATOM   6765 N  N   . GLN D 1 38  ? 11.135  -6.811  -19.741 1.00 12.42 ? 38  GLN D N   1 
ATOM   6766 C  CA  . GLN D 1 38  ? 10.628  -7.205  -18.432 1.00 14.73 ? 38  GLN D CA  1 
ATOM   6767 C  C   . GLN D 1 38  ? 9.117   -7.329  -18.491 1.00 12.72 ? 38  GLN D C   1 
ATOM   6768 O  O   . GLN D 1 38  ? 8.411   -6.414  -18.915 1.00 11.91 ? 38  GLN D O   1 
ATOM   6769 C  CB  . GLN D 1 38  ? 10.990  -6.104  -17.461 1.00 16.63 ? 38  GLN D CB  1 
ATOM   6770 C  CG  . GLN D 1 38  ? 10.559  -6.476  -16.044 1.00 20.00 ? 38  GLN D CG  1 
ATOM   6771 C  CD  . GLN D 1 38  ? 11.121  -5.511  -15.037 1.00 23.37 ? 38  GLN D CD  1 
ATOM   6772 O  OE1 . GLN D 1 38  ? 12.313  -5.563  -14.740 1.00 30.09 ? 38  GLN D OE1 1 
ATOM   6773 N  NE2 . GLN D 1 38  ? 10.288  -4.590  -14.562 1.00 25.71 ? 38  GLN D NE2 1 
ATOM   6774 N  N   . TYR D 1 39  ? 8.597   -8.465  -18.032 1.00 12.45 ? 39  TYR D N   1 
ATOM   6775 C  CA  . TYR D 1 39  ? 7.174   -8.742  -17.998 1.00 11.62 ? 39  TYR D CA  1 
ATOM   6776 C  C   . TYR D 1 39  ? 6.516   -7.772  -17.014 1.00 11.65 ? 39  TYR D C   1 
ATOM   6777 O  O   . TYR D 1 39  ? 7.089   -7.472  -15.955 1.00 12.79 ? 39  TYR D O   1 
ATOM   6778 C  CB  . TYR D 1 39  ? 6.992   -10.195 -17.536 1.00 11.87 ? 39  TYR D CB  1 
ATOM   6779 C  CG  . TYR D 1 39  ? 5.535   -10.479 -17.270 1.00 12.41 ? 39  TYR D CG  1 
ATOM   6780 C  CD1 . TYR D 1 39  ? 4.590   -10.467 -18.282 1.00 12.76 ? 39  TYR D CD1 1 
ATOM   6781 C  CD2 . TYR D 1 39  ? 5.069   -10.679 -15.968 1.00 13.07 ? 39  TYR D CD2 1 
ATOM   6782 C  CE1 . TYR D 1 39  ? 3.229   -10.681 -18.094 1.00 14.02 ? 39  TYR D CE1 1 
ATOM   6783 C  CE2 . TYR D 1 39  ? 3.709   -10.878 -15.772 1.00 13.12 ? 39  TYR D CE2 1 
ATOM   6784 C  CZ  . TYR D 1 39  ? 2.798   -10.907 -16.792 1.00 15.37 ? 39  TYR D CZ  1 
ATOM   6785 O  OH  . TYR D 1 39  ? 1.463   -11.083 -16.523 1.00 17.55 ? 39  TYR D OH  1 
ATOM   6786 N  N   . ASP D 1 40  ? 5.378   -7.209  -17.435 1.00 11.00 ? 40  ASP D N   1 
ATOM   6787 C  CA  . ASP D 1 40  ? 4.623   -6.287  -16.583 1.00 12.24 ? 40  ASP D CA  1 
ATOM   6788 C  C   . ASP D 1 40  ? 3.171   -6.709  -16.664 1.00 12.69 ? 40  ASP D C   1 
ATOM   6789 O  O   . ASP D 1 40  ? 2.480   -6.612  -17.704 1.00 11.93 ? 40  ASP D O   1 
ATOM   6790 C  CB  . ASP D 1 40  ? 4.889   -4.859  -17.071 1.00 13.75 ? 40  ASP D CB  1 
ATOM   6791 C  CG  . ASP D 1 40  ? 4.120   -3.786  -16.342 1.00 17.51 ? 40  ASP D CG  1 
ATOM   6792 O  OD1 . ASP D 1 40  ? 3.382   -4.118  -15.415 1.00 15.93 ? 40  ASP D OD1 1 
ATOM   6793 O  OD2 . ASP D 1 40  ? 4.255   -2.607  -16.746 1.00 21.27 ? 40  ASP D OD2 1 
ATOM   6794 N  N   . ALA D 1 41  ? 2.666   -7.180  -15.484 1.00 11.43 ? 41  ALA D N   1 
ATOM   6795 C  CA  . ALA D 1 41  ? 1.269   -7.615  -15.447 1.00 13.31 ? 41  ALA D CA  1 
ATOM   6796 C  C   . ALA D 1 41  ? 0.240   -6.483  -15.596 1.00 13.32 ? 41  ALA D C   1 
ATOM   6797 O  O   . ALA D 1 41  ? -0.930  -6.767  -15.866 1.00 14.52 ? 41  ALA D O   1 
ATOM   6798 C  CB  . ALA D 1 41  ? 1.052   -8.387  -14.146 1.00 15.64 ? 41  ALA D CB  1 
ATOM   6799 N  N   . SER D 1 42  ? 0.696   -5.228  -15.526 1.00 13.29 ? 42  SER D N   1 
ATOM   6800 C  CA  . SER D 1 42  ? -0.213  -4.115  -15.759 1.00 14.55 ? 42  SER D CA  1 
ATOM   6801 C  C   . SER D 1 42  ? -0.577  -3.970  -17.236 1.00 15.48 ? 42  SER D C   1 
ATOM   6802 O  O   . SER D 1 42  ? -1.433  -3.110  -17.539 1.00 17.77 ? 42  SER D O   1 
ATOM   6803 C  CB  . SER D 1 42  ? 0.269   -2.815  -15.191 1.00 16.90 ? 42  SER D CB  1 
ATOM   6804 O  OG  . SER D 1 42  ? 1.331   -2.322  -15.971 1.00 21.57 ? 42  SER D OG  1 
ATOM   6805 N  N   . LEU D 1 43  ? 0.121   -4.694  -18.140 1.00 14.24 ? 43  LEU D N   1 
ATOM   6806 C  CA  . LEU D 1 43  ? -0.094  -4.459  -19.563 1.00 14.95 ? 43  LEU D CA  1 
ATOM   6807 C  C   . LEU D 1 43  ? -1.233  -5.335  -20.020 1.00 14.84 ? 43  LEU D C   1 
ATOM   6808 O  O   . LEU D 1 43  ? -1.097  -6.420  -20.557 1.00 15.10 ? 43  LEU D O   1 
ATOM   6809 C  CB  . LEU D 1 43  ? 1.195   -4.753  -20.336 1.00 13.78 ? 43  LEU D CB  1 
ATOM   6810 C  CG  . LEU D 1 43  ? 2.316   -3.798  -20.034 1.00 14.46 ? 43  LEU D CG  1 
ATOM   6811 C  CD1 . LEU D 1 43  ? 3.502   -4.219  -20.865 1.00 12.30 ? 43  LEU D CD1 1 
ATOM   6812 C  CD2 . LEU D 1 43  ? 1.977   -2.337  -20.369 1.00 15.03 ? 43  LEU D CD2 1 
ATOM   6813 N  N   . THR D 1 44  ? -2.441  -4.765  -19.899 1.00 15.68 ? 44  THR D N   1 
ATOM   6814 C  CA  . THR D 1 44  ? -3.644  -5.492  -20.204 1.00 15.56 ? 44  THR D CA  1 
ATOM   6815 C  C   . THR D 1 44  ? -3.992  -5.293  -21.675 1.00 15.32 ? 44  THR D C   1 
ATOM   6816 O  O   . THR D 1 44  ? -3.393  -4.457  -22.357 1.00 14.68 ? 44  THR D O   1 
ATOM   6817 C  CB  . THR D 1 44  ? -4.774  -4.975  -19.281 1.00 17.03 ? 44  THR D CB  1 
ATOM   6818 O  OG1 . THR D 1 44  ? -4.850  -3.563  -19.426 1.00 21.06 ? 44  THR D OG1 1 
ATOM   6819 C  CG2 . THR D 1 44  ? -4.510  -5.294  -17.822 1.00 21.60 ? 44  THR D CG2 1 
ATOM   6820 N  N   . PRO D 1 45  ? -4.923  -6.075  -22.236 1.00 15.89 ? 45  PRO D N   1 
ATOM   6821 C  CA  . PRO D 1 45  ? -5.176  -6.015  -23.687 1.00 17.44 ? 45  PRO D CA  1 
ATOM   6822 C  C   . PRO D 1 45  ? -5.782  -4.691  -24.141 1.00 18.43 ? 45  PRO D C   1 
ATOM   6823 O  O   . PRO D 1 45  ? -6.590  -4.096  -23.439 1.00 20.58 ? 45  PRO D O   1 
ATOM   6824 C  CB  . PRO D 1 45  ? -6.213  -7.113  -23.900 1.00 19.92 ? 45  PRO D CB  1 
ATOM   6825 C  CG  . PRO D 1 45  ? -5.973  -8.040  -22.716 1.00 17.79 ? 45  PRO D CG  1 
ATOM   6826 C  CD  . PRO D 1 45  ? -5.682  -7.127  -21.551 1.00 16.64 ? 45  PRO D CD  1 
ATOM   6827 N  N   . LEU D 1 46  ? -5.306  -4.189  -25.289 1.00 16.64 ? 46  LEU D N   1 
ATOM   6828 C  CA  . LEU D 1 46  ? -5.908  -3.023  -25.901 1.00 15.78 ? 46  LEU D CA  1 
ATOM   6829 C  C   . LEU D 1 46  ? -7.155  -3.426  -26.656 1.00 14.86 ? 46  LEU D C   1 
ATOM   6830 O  O   . LEU D 1 46  ? -7.326  -4.527  -27.156 1.00 16.17 ? 46  LEU D O   1 
ATOM   6831 C  CB  . LEU D 1 46  ? -4.906  -2.421  -26.881 1.00 16.62 ? 46  LEU D CB  1 
ATOM   6832 C  CG  . LEU D 1 46  ? -3.646  -1.874  -26.225 1.00 18.05 ? 46  LEU D CG  1 
ATOM   6833 C  CD1 . LEU D 1 46  ? -2.691  -1.363  -27.307 1.00 21.90 ? 46  LEU D CD1 1 
ATOM   6834 C  CD2 . LEU D 1 46  ? -4.004  -0.735  -25.265 1.00 20.59 ? 46  LEU D CD2 1 
ATOM   6835 N  N   . GLU D 1 47  ? -8.050  -2.429  -26.718 1.00 16.57 ? 47  GLU D N   1 
ATOM   6836 C  CA  . GLU D 1 47  ? -9.223  -2.545  -27.552 1.00 18.22 ? 47  GLU D CA  1 
ATOM   6837 C  C   . GLU D 1 47  ? -9.171  -1.522  -28.694 1.00 15.73 ? 47  GLU D C   1 
ATOM   6838 O  O   . GLU D 1 47  ? -8.748  -0.369  -28.481 1.00 16.68 ? 47  GLU D O   1 
ATOM   6839 C  CB  . GLU D 1 47  ? -10.508 -2.490  -26.717 1.00 23.27 ? 47  GLU D CB  1 
ATOM   6840 C  CG  . GLU D 1 47  ? -10.891 -3.876  -26.173 1.00 31.28 ? 47  GLU D CG  1 
ATOM   6841 C  CD  . GLU D 1 47  ? -12.113 -3.997  -25.264 1.00 42.22 ? 47  GLU D CD  1 
ATOM   6842 O  OE1 . GLU D 1 47  ? -12.528 -2.977  -24.668 1.00 48.77 ? 47  GLU D OE1 1 
ATOM   6843 O  OE2 . GLU D 1 47  ? -12.650 -5.129  -25.141 1.00 51.34 ? 47  GLU D OE2 1 
ATOM   6844 N  N   . PHE D 1 48  ? -9.507  -2.029  -29.875 1.00 16.85 ? 48  PHE D N   1 
ATOM   6845 C  CA  . PHE D 1 48  ? -9.412  -1.270  -31.122 1.00 15.69 ? 48  PHE D CA  1 
ATOM   6846 C  C   . PHE D 1 48  ? -10.837 -0.943  -31.530 1.00 20.89 ? 48  PHE D C   1 
ATOM   6847 O  O   . PHE D 1 48  ? -11.516 -1.818  -32.054 1.00 21.88 ? 48  PHE D O   1 
ATOM   6848 C  CB  . PHE D 1 48  ? -8.692  -2.073  -32.224 1.00 17.19 ? 48  PHE D CB  1 
ATOM   6849 C  CG  . PHE D 1 48  ? -7.376  -2.611  -31.728 1.00 15.73 ? 48  PHE D CG  1 
ATOM   6850 C  CD1 . PHE D 1 48  ? -6.330  -1.775  -31.399 1.00 13.47 ? 48  PHE D CD1 1 
ATOM   6851 C  CD2 . PHE D 1 48  ? -7.251  -3.979  -31.450 1.00 17.48 ? 48  PHE D CD2 1 
ATOM   6852 C  CE1 . PHE D 1 48  ? -5.174  -2.289  -30.836 1.00 16.26 ? 48  PHE D CE1 1 
ATOM   6853 C  CE2 . PHE D 1 48  ? -6.091  -4.491  -30.891 1.00 17.67 ? 48  PHE D CE2 1 
ATOM   6854 C  CZ  . PHE D 1 48  ? -5.069  -3.641  -30.601 1.00 15.32 ? 48  PHE D CZ  1 
ATOM   6855 N  N   . GLN D 1 49  ? -11.210 0.321   -31.322 1.00 15.70 ? 49  GLN D N   1 
ATOM   6856 C  CA  . GLN D 1 49  ? -12.583 0.778   -31.504 1.00 19.08 ? 49  GLN D CA  1 
ATOM   6857 C  C   . GLN D 1 49  ? -12.708 1.646   -32.751 1.00 16.07 ? 49  GLN D C   1 
ATOM   6858 O  O   . GLN D 1 49  ? -11.927 2.545   -32.993 1.00 15.00 ? 49  GLN D O   1 
ATOM   6859 C  CB  . GLN D 1 49  ? -13.026 1.609   -30.303 1.00 22.00 ? 49  GLN D CB  1 
ATOM   6860 C  CG  . GLN D 1 49  ? -12.967 0.905   -28.959 1.00 30.98 ? 49  GLN D CG  1 
ATOM   6861 C  CD  . GLN D 1 49  ? -13.876 -0.293  -28.776 1.00 40.71 ? 49  GLN D CD  1 
ATOM   6862 O  OE1 . GLN D 1 49  ? -14.837 -0.525  -29.521 1.00 43.94 ? 49  GLN D OE1 1 
ATOM   6863 N  NE2 . GLN D 1 49  ? -13.607 -1.043  -27.716 1.00 42.40 ? 49  GLN D NE2 1 
ATOM   6864 N  N   . GLY D 1 50  ? -13.762 1.410   -33.516 1.00 15.18 ? 50  GLY D N   1 
ATOM   6865 C  CA  . GLY D 1 50  ? -14.026 2.139   -34.746 1.00 15.37 ? 50  GLY D CA  1 
ATOM   6866 C  C   . GLY D 1 50  ? -12.956 1.921   -35.822 1.00 13.66 ? 50  GLY D C   1 
ATOM   6867 O  O   . GLY D 1 50  ? -12.885 2.730   -36.746 1.00 14.72 ? 50  GLY D O   1 
ATOM   6868 N  N   . TYR D 1 51  ? -12.278 0.759   -35.759 1.00 12.62 ? 51  TYR D N   1 
ATOM   6869 C  CA  . TYR D 1 51  ? -11.289 0.410   -36.798 1.00 12.47 ? 51  TYR D CA  1 
ATOM   6870 C  C   . TYR D 1 51  ? -11.928 -0.116  -38.066 1.00 12.32 ? 51  TYR D C   1 
ATOM   6871 O  O   . TYR D 1 51  ? -11.346 -0.182  -39.129 1.00 12.20 ? 51  TYR D O   1 
ATOM   6872 C  CB  . TYR D 1 51  ? -10.317 -0.643  -36.246 1.00 12.61 ? 51  TYR D CB  1 
ATOM   6873 C  CG  . TYR D 1 51  ? -9.122  -0.070  -35.534 1.00 10.43 ? 51  TYR D CG  1 
ATOM   6874 C  CD1 . TYR D 1 51  ? -9.212  0.926   -34.594 1.00 11.96 ? 51  TYR D CD1 1 
ATOM   6875 C  CD2 . TYR D 1 51  ? -7.856  -0.575  -35.808 1.00 10.79 ? 51  TYR D CD2 1 
ATOM   6876 C  CE1 . TYR D 1 51  ? -8.136  1.433   -33.912 1.00 11.94 ? 51  TYR D CE1 1 
ATOM   6877 C  CE2 . TYR D 1 51  ? -6.748  -0.018  -35.170 1.00 11.33 ? 51  TYR D CE2 1 
ATOM   6878 C  CZ  . TYR D 1 51  ? -6.877  0.959   -34.210 1.00 11.54 ? 51  TYR D CZ  1 
ATOM   6879 O  OH  . TYR D 1 51  ? -5.730  1.437   -33.680 1.00 12.58 ? 51  TYR D OH  1 
ATOM   6880 N  N   . ASN D 1 52  ? -13.237 -0.481  -37.977 1.00 13.26 ? 52  ASN D N   1 
ATOM   6881 C  CA  . ASN D 1 52  ? -13.854 -1.053  -39.140 1.00 14.12 ? 52  ASN D CA  1 
ATOM   6882 C  C   . ASN D 1 52  ? -14.461 0.071   -39.975 1.00 16.08 ? 52  ASN D C   1 
ATOM   6883 O  O   . ASN D 1 52  ? -15.640 0.403   -39.809 1.00 17.33 ? 52  ASN D O   1 
ATOM   6884 C  CB  . ASN D 1 52  ? -14.889 -2.091  -38.691 1.00 15.76 ? 52  ASN D CB  1 
ATOM   6885 C  CG  . ASN D 1 52  ? -15.490 -2.879  -39.832 1.00 19.86 ? 52  ASN D CG  1 
ATOM   6886 O  OD1 . ASN D 1 52  ? -15.106 -2.787  -40.976 1.00 21.46 ? 52  ASN D OD1 1 
ATOM   6887 N  ND2 . ASN D 1 52  ? -16.506 -3.668  -39.518 1.00 24.35 ? 52  ASN D ND2 1 
ATOM   6888 N  N   . LEU D 1 53  ? -13.708 0.593   -40.937 1.00 14.49 ? 53  LEU D N   1 
ATOM   6889 C  CA  . LEU D 1 53  ? -14.121 1.757   -41.715 1.00 14.42 ? 53  LEU D CA  1 
ATOM   6890 C  C   . LEU D 1 53  ? -15.071 1.337   -42.837 1.00 15.19 ? 53  LEU D C   1 
ATOM   6891 O  O   . LEU D 1 53  ? -14.875 0.312   -43.482 1.00 15.70 ? 53  LEU D O   1 
ATOM   6892 C  CB  . LEU D 1 53  ? -12.864 2.441   -42.266 1.00 14.21 ? 53  LEU D CB  1 
ATOM   6893 C  CG  . LEU D 1 53  ? -11.829 2.863   -41.219 1.00 15.74 ? 53  LEU D CG  1 
ATOM   6894 C  CD1 . LEU D 1 53  ? -10.679 3.577   -41.928 1.00 18.09 ? 53  LEU D CD1 1 
ATOM   6895 C  CD2 . LEU D 1 53  ? -12.391 3.746   -40.148 1.00 16.94 ? 53  LEU D CD2 1 
ATOM   6896 N  N   . SER D 1 54  ? -16.116 2.142   -43.087 1.00 12.98 ? 54  SER D N   1 
ATOM   6897 C  CA  . SER D 1 54  ? -17.108 1.786   -44.082 1.00 13.66 ? 54  SER D CA  1 
ATOM   6898 C  C   . SER D 1 54  ? -16.487 1.769   -45.486 1.00 13.88 ? 54  SER D C   1 
ATOM   6899 O  O   . SER D 1 54  ? -15.843 2.737   -45.895 1.00 14.38 ? 54  SER D O   1 
ATOM   6900 C  CB  . SER D 1 54  ? -18.236 2.785   -44.022 1.00 15.32 ? 54  SER D CB  1 
ATOM   6901 O  OG  . SER D 1 54  ? -19.162 2.477   -45.043 1.00 17.31 ? 54  SER D OG  1 
ATOM   6902 N  N   . ALA D 1 55  ? -16.865 0.755   -46.256 1.00 15.98 ? 55  ALA D N   1 
ATOM   6903 C  CA  . ALA D 1 55  ? -16.435 0.655   -47.650 1.00 17.37 ? 55  ALA D CA  1 
ATOM   6904 C  C   . ALA D 1 55  ? -17.078 1.724   -48.522 1.00 17.57 ? 55  ALA D C   1 
ATOM   6905 O  O   . ALA D 1 55  ? -16.636 1.945   -49.652 1.00 19.57 ? 55  ALA D O   1 
ATOM   6906 C  CB  . ALA D 1 55  ? -16.742 -0.732  -48.184 1.00 21.26 ? 55  ALA D CB  1 
ATOM   6907 N  N   . ASN D 1 56  ? -18.108 2.412   -48.015 1.00 16.31 ? 56  ASN D N   1 
ATOM   6908 C  CA  . ASN D 1 56  ? -18.769 3.494   -48.733 1.00 17.61 ? 56  ASN D CA  1 
ATOM   6909 C  C   . ASN D 1 56  ? -18.195 4.865   -48.431 1.00 17.50 ? 56  ASN D C   1 
ATOM   6910 O  O   . ASN D 1 56  ? -18.621 5.835   -49.071 1.00 20.50 ? 56  ASN D O   1 
ATOM   6911 C  CB  . ASN D 1 56  ? -20.282 3.573   -48.460 1.00 19.61 ? 56  ASN D CB  1 
ATOM   6912 C  CG  . ASN D 1 56  ? -20.950 2.338   -49.007 1.00 28.06 ? 56  ASN D CG  1 
ATOM   6913 O  OD1 . ASN D 1 56  ? -20.660 1.934   -50.130 1.00 30.41 ? 56  ASN D OD1 1 
ATOM   6914 N  ND2 . ASN D 1 56  ? -21.788 1.709   -48.205 1.00 29.95 ? 56  ASN D ND2 1 
ATOM   6915 N  N   . LYS D 1 57  ? -17.208 4.908   -47.534 1.00 15.30 ? 57  LYS D N   1 
ATOM   6916 C  CA  . LYS D 1 57  ? -16.485 6.123   -47.218 1.00 14.55 ? 57  LYS D CA  1 
ATOM   6917 C  C   . LYS D 1 57  ? -15.087 5.982   -47.806 1.00 15.19 ? 57  LYS D C   1 
ATOM   6918 O  O   . LYS D 1 57  ? -14.701 4.872   -48.244 1.00 15.94 ? 57  LYS D O   1 
ATOM   6919 C  CB  . LYS D 1 57  ? -16.436 6.358   -45.716 1.00 15.26 ? 57  LYS D CB  1 
ATOM   6920 C  CG  . LYS D 1 57  ? -17.797 6.665   -45.082 1.00 19.56 ? 57  LYS D CG  1 
ATOM   6921 C  CD  . LYS D 1 57  ? -17.569 7.226   -43.716 1.00 21.28 ? 57  LYS D CD  1 
ATOM   6922 C  CE  . LYS D 1 57  ? -18.817 7.753   -43.040 1.00 26.35 ? 57  LYS D CE  1 
ATOM   6923 N  NZ  . LYS D 1 57  ? -18.590 7.828   -41.571 1.00 31.01 ? 57  LYS D NZ  1 
ATOM   6924 N  N   . GLN D 1 58  ? -14.440 7.133   -47.972 1.00 14.15 ? 58  GLN D N   1 
ATOM   6925 C  CA  . GLN D 1 58  ? -13.124 7.136   -48.596 1.00 13.74 ? 58  GLN D CA  1 
ATOM   6926 C  C   . GLN D 1 58  ? -12.190 7.960   -47.723 1.00 12.66 ? 58  GLN D C   1 
ATOM   6927 O  O   . GLN D 1 58  ? -12.543 8.862   -46.995 1.00 13.38 ? 58  GLN D O   1 
ATOM   6928 C  CB  . GLN D 1 58  ? -13.187 7.442   -50.092 1.00 19.62 ? 58  GLN D CB  1 
ATOM   6929 C  CG  . GLN D 1 58  ? -13.667 8.825   -50.398 1.00 22.95 ? 58  GLN D CG  1 
ATOM   6930 C  CD  . GLN D 1 58  ? -13.730 9.086   -51.892 1.00 23.10 ? 58  GLN D CD  1 
ATOM   6931 O  OE1 . GLN D 1 58  ? -13.503 8.208   -52.741 1.00 22.95 ? 58  GLN D OE1 1 
ATOM   6932 N  NE2 . GLN D 1 58  ? -14.012 10.342  -52.217 1.00 28.10 ? 58  GLN D NE2 1 
ATOM   6933 N  N   . PHE D 1 59  ? -10.921 7.544   -47.737 1.00 11.33 ? 59  PHE D N   1 
ATOM   6934 C  CA  . PHE D 1 59  ? -9.866  8.037   -46.853 1.00 10.30 ? 59  PHE D CA  1 
ATOM   6935 C  C   . PHE D 1 59  ? -8.682  8.429   -47.720 1.00 10.06 ? 59  PHE D C   1 
ATOM   6936 O  O   . PHE D 1 59  ? -8.355  7.763   -48.683 1.00 11.31 ? 59  PHE D O   1 
ATOM   6937 C  CB  . PHE D 1 59  ? -9.499  6.952   -45.836 1.00 11.18 ? 59  PHE D CB  1 
ATOM   6938 C  CG  . PHE D 1 59  ? -10.723 6.631   -45.014 1.00 11.21 ? 59  PHE D CG  1 
ATOM   6939 C  CD1 . PHE D 1 59  ? -11.638 5.688   -45.480 1.00 12.01 ? 59  PHE D CD1 1 
ATOM   6940 C  CD2 . PHE D 1 59  ? -11.030 7.400   -43.894 1.00 11.81 ? 59  PHE D CD2 1 
ATOM   6941 C  CE1 . PHE D 1 59  ? -12.842 5.497   -44.778 1.00 12.03 ? 59  PHE D CE1 1 
ATOM   6942 C  CE2 . PHE D 1 59  ? -12.214 7.169   -43.174 1.00 11.98 ? 59  PHE D CE2 1 
ATOM   6943 C  CZ  . PHE D 1 59  ? -13.110 6.237   -43.641 1.00 12.05 ? 59  PHE D CZ  1 
ATOM   6944 N  N   . LEU D 1 60  ? -8.069  9.558   -47.350 1.00 10.50 ? 60  LEU D N   1 
ATOM   6945 C  CA  . LEU D 1 60  ? -7.038  10.139  -48.206 1.00 12.39 ? 60  LEU D CA  1 
ATOM   6946 C  C   . LEU D 1 60  ? -5.665  9.503   -48.002 1.00 11.07 ? 60  LEU D C   1 
ATOM   6947 O  O   . LEU D 1 60  ? -5.154  9.472   -46.883 1.00 11.62 ? 60  LEU D O   1 
ATOM   6948 C  CB  . LEU D 1 60  ? -6.948  11.604  -47.794 1.00 14.63 ? 60  LEU D CB  1 
ATOM   6949 C  CG  . LEU D 1 60  ? -6.196  12.459  -48.806 1.00 17.04 ? 60  LEU D CG  1 
ATOM   6950 C  CD1 . LEU D 1 60  ? -6.895  12.499  -50.152 1.00 18.37 ? 60  LEU D CD1 1 
ATOM   6951 C  CD2 . LEU D 1 60  ? -6.011  13.861  -48.246 1.00 21.27 ? 60  LEU D CD2 1 
ATOM   6952 N  N   . LEU D 1 61  ? -5.086  9.009   -49.082 1.00 10.92 ? 61  LEU D N   1 
ATOM   6953 C  CA  . LEU D 1 61  ? -3.711  8.495   -49.144 1.00 10.80 ? 61  LEU D CA  1 
ATOM   6954 C  C   . LEU D 1 61  ? -2.837  9.577   -49.759 1.00 12.21 ? 61  LEU D C   1 
ATOM   6955 O  O   . LEU D 1 61  ? -3.206  10.164  -50.784 1.00 13.72 ? 61  LEU D O   1 
ATOM   6956 C  CB  . LEU D 1 61  ? -3.731  7.231   -49.998 1.00 12.63 ? 61  LEU D CB  1 
ATOM   6957 C  CG  . LEU D 1 61  ? -2.439  6.413   -50.016 1.00 11.43 ? 61  LEU D CG  1 
ATOM   6958 C  CD1 . LEU D 1 61  ? -2.285  5.607   -48.740 1.00 12.73 ? 61  LEU D CD1 1 
ATOM   6959 C  CD2 . LEU D 1 61  ? -2.494  5.450   -51.200 1.00 14.22 ? 61  LEU D CD2 1 
ATOM   6960 N  N   . THR D 1 62  ? -1.672  9.839   -49.153 1.00 11.72 ? 62  THR D N   1 
ATOM   6961 C  CA  . THR D 1 62  ? -0.823  10.938  -49.605 1.00 12.88 ? 62  THR D CA  1 
ATOM   6962 C  C   . THR D 1 62  ? 0.630   10.479  -49.562 1.00 11.72 ? 62  THR D C   1 
ATOM   6963 O  O   . THR D 1 62  ? 1.054   9.759   -48.643 1.00 13.31 ? 62  THR D O   1 
ATOM   6964 C  CB  . THR D 1 62  ? -0.824  12.064  -48.566 1.00 15.57 ? 62  THR D CB  1 
ATOM   6965 O  OG1 . THR D 1 62  ? -2.147  12.601  -48.423 1.00 20.81 ? 62  THR D OG1 1 
ATOM   6966 C  CG2 . THR D 1 62  ? 0.123   13.201  -48.909 1.00 19.41 ? 62  THR D CG2 1 
ATOM   6967 N  N   . ASN D 1 63  ? 1.396   10.853  -50.575 1.00 11.69 ? 63  ASN D N   1 
ATOM   6968 C  CA  . ASN D 1 63  ? 2.847   10.747  -50.527 1.00 11.51 ? 63  ASN D CA  1 
ATOM   6969 C  C   . ASN D 1 63  ? 3.375   12.039  -49.908 1.00 11.76 ? 63  ASN D C   1 
ATOM   6970 O  O   . ASN D 1 63  ? 3.182   13.150  -50.466 1.00 12.02 ? 63  ASN D O   1 
ATOM   6971 C  CB  . ASN D 1 63  ? 3.366   10.514  -51.951 1.00 13.94 ? 63  ASN D CB  1 
ATOM   6972 C  CG  . ASN D 1 63  ? 4.882   10.566  -52.069 1.00 11.29 ? 63  ASN D CG  1 
ATOM   6973 O  OD1 . ASN D 1 63  ? 5.564   11.121  -51.196 1.00 11.86 ? 63  ASN D OD1 1 
ATOM   6974 N  ND2 . ASN D 1 63  ? 5.394   9.948   -53.109 1.00 11.80 ? 63  ASN D ND2 1 
ATOM   6975 N  N   . ASN D 1 64  ? 3.938   11.955  -48.697 1.00 11.54 ? 64  ASN D N   1 
ATOM   6976 C  CA  . ASN D 1 64  ? 4.321   13.185  -48.004 1.00 13.56 ? 64  ASN D CA  1 
ATOM   6977 C  C   . ASN D 1 64  ? 5.806   13.510  -48.201 1.00 14.67 ? 64  ASN D C   1 
ATOM   6978 O  O   . ASN D 1 64  ? 6.368   14.379  -47.513 1.00 15.69 ? 64  ASN D O   1 
ATOM   6979 C  CB  . ASN D 1 64  ? 3.940   13.154  -46.529 1.00 13.35 ? 64  ASN D CB  1 
ATOM   6980 C  CG  . ASN D 1 64  ? 4.607   12.033  -45.776 1.00 15.10 ? 64  ASN D CG  1 
ATOM   6981 O  OD1 . ASN D 1 64  ? 5.565   11.402  -46.237 1.00 14.01 ? 64  ASN D OD1 1 
ATOM   6982 N  ND2 . ASN D 1 64  ? 4.128   11.808  -44.567 1.00 16.24 ? 64  ASN D ND2 1 
ATOM   6983 N  N   . GLY D 1 65  ? 6.440   12.776  -49.103 1.00 13.37 ? 65  GLY D N   1 
ATOM   6984 C  CA  . GLY D 1 65  ? 7.855   12.963  -49.337 1.00 13.34 ? 65  GLY D CA  1 
ATOM   6985 C  C   . GLY D 1 65  ? 8.726   12.110  -48.411 1.00 14.79 ? 65  GLY D C   1 
ATOM   6986 O  O   . GLY D 1 65  ? 9.937   12.099  -48.591 1.00 15.53 ? 65  GLY D O   1 
ATOM   6987 N  N   . HIS D 1 66  ? 8.131   11.344  -47.482 1.00 12.93 ? 66  HIS D N   1 
ATOM   6988 C  CA  . HIS D 1 66  ? 8.929   10.575  -46.516 1.00 12.67 ? 66  HIS D CA  1 
ATOM   6989 C  C   . HIS D 1 66  ? 8.379   9.168   -46.360 1.00 11.99 ? 66  HIS D C   1 
ATOM   6990 O  O   . HIS D 1 66  ? 9.115   8.271   -45.919 1.00 11.56 ? 66  HIS D O   1 
ATOM   6991 C  CB  . HIS D 1 66  ? 8.942   11.290  -45.145 1.00 12.84 ? 66  HIS D CB  1 
ATOM   6992 C  CG  . HIS D 1 66  ? 9.528   12.672  -45.246 1.00 13.96 ? 66  HIS D CG  1 
ATOM   6993 N  ND1 . HIS D 1 66  ? 10.888  12.919  -45.492 1.00 16.46 ? 66  HIS D ND1 1 
ATOM   6994 C  CD2 . HIS D 1 66  ? 8.926   13.854  -45.064 1.00 16.78 ? 66  HIS D CD2 1 
ATOM   6995 C  CE1 . HIS D 1 66  ? 11.055  14.251  -45.491 1.00 15.89 ? 66  HIS D CE1 1 
ATOM   6996 N  NE2 . HIS D 1 66  ? 9.859   14.822  -45.232 1.00 17.20 ? 66  HIS D NE2 1 
ATOM   6997 N  N   . SER D 1 67  ? 7.090   9.000   -46.637 1.00 10.85 ? 67  SER D N   1 
ATOM   6998 C  CA  . SER D 1 67  ? 6.422   7.693   -46.616 1.00 10.81 ? 67  SER D CA  1 
ATOM   6999 C  C   . SER D 1 67  ? 5.142   7.829   -47.429 1.00 11.55 ? 67  SER D C   1 
ATOM   7000 O  O   . SER D 1 67  ? 4.905   8.886   -48.028 1.00 12.17 ? 67  SER D O   1 
ATOM   7001 C  CB  . SER D 1 67  ? 6.043   7.393   -45.161 1.00 11.49 ? 67  SER D CB  1 
ATOM   7002 O  OG  . SER D 1 67  ? 5.511   6.075   -44.995 1.00 11.18 ? 67  SER D OG  1 
ATOM   7003 N  N   . VAL D 1 68  ? 4.329   6.779   -47.370 1.00 11.03 ? 68  VAL D N   1 
ATOM   7004 C  CA  . VAL D 1 68  ? 2.971   6.893   -47.846 1.00 11.70 ? 68  VAL D CA  1 
ATOM   7005 C  C   . VAL D 1 68  ? 2.105   6.856   -46.593 1.00 10.83 ? 68  VAL D C   1 
ATOM   7006 O  O   . VAL D 1 68  ? 2.253   5.963   -45.777 1.00 10.91 ? 68  VAL D O   1 
ATOM   7007 C  CB  . VAL D 1 68  ? 2.669   5.801   -48.881 1.00 12.55 ? 68  VAL D CB  1 
ATOM   7008 C  CG1 . VAL D 1 68  ? 2.892   4.383   -48.417 1.00 13.53 ? 68  VAL D CG1 1 
ATOM   7009 C  CG2 . VAL D 1 68  ? 1.236   5.945   -49.415 1.00 15.36 ? 68  VAL D CG2 1 
ATOM   7010 N  N   . LYS D 1 69  ? 1.118   7.762   -46.528 1.00 10.62 ? 69  LYS D N   1 
ATOM   7011 C  CA  . LYS D 1 69  ? 0.292   7.856   -45.344 1.00 10.63 ? 69  LYS D CA  1 
ATOM   7012 C  C   . LYS D 1 69  ? -1.170  7.826   -45.740 1.00 9.05  ? 69  LYS D C   1 
ATOM   7013 O  O   . LYS D 1 69  ? -1.574  8.380   -46.746 1.00 10.80 ? 69  LYS D O   1 
ATOM   7014 C  CB  . LYS D 1 69  ? 0.725   9.120   -44.609 1.00 14.50 ? 69  LYS D CB  1 
ATOM   7015 C  CG  . LYS D 1 69  ? -0.050  10.386  -44.797 1.00 21.23 ? 69  LYS D CG  1 
ATOM   7016 C  CD  . LYS D 1 69  ? 0.082   11.348  -43.594 1.00 18.66 ? 69  LYS D CD  1 
ATOM   7017 C  CE  . LYS D 1 69  ? -0.451  12.609  -44.208 1.00 22.88 ? 69  LYS D CE  1 
ATOM   7018 N  NZ  . LYS D 1 69  ? -0.071  13.769  -43.392 1.00 22.05 ? 69  LYS D NZ  1 
ATOM   7019 N  N   . LEU D 1 70  ? -1.959  7.164   -44.905 1.00 8.44  ? 70  LEU D N   1 
ATOM   7020 C  CA  . LEU D 1 70  ? -3.414  7.118   -45.025 1.00 8.13  ? 70  LEU D CA  1 
ATOM   7021 C  C   . LEU D 1 70  ? -3.986  7.850   -43.826 1.00 8.31  ? 70  LEU D C   1 
ATOM   7022 O  O   . LEU D 1 70  ? -3.713  7.537   -42.683 1.00 8.81  ? 70  LEU D O   1 
ATOM   7023 C  CB  . LEU D 1 70  ? -3.857  5.663   -45.002 1.00 8.91  ? 70  LEU D CB  1 
ATOM   7024 C  CG  . LEU D 1 70  ? -5.364  5.482   -45.142 1.00 9.03  ? 70  LEU D CG  1 
ATOM   7025 C  CD1 . LEU D 1 70  ? -5.812  5.906   -46.539 1.00 11.28 ? 70  LEU D CD1 1 
ATOM   7026 C  CD2 . LEU D 1 70  ? -5.742  4.014   -44.856 1.00 11.85 ? 70  LEU D CD2 1 
ATOM   7027 N  N   . ASN D 1 71  ? -4.820  8.839   -44.124 1.00 9.79  ? 71  ASN D N   1 
ATOM   7028 C  CA  . ASN D 1 71  ? -5.529  9.584   -43.080 1.00 10.38 ? 71  ASN D CA  1 
ATOM   7029 C  C   . ASN D 1 71  ? -6.635  8.742   -42.473 1.00 10.14 ? 71  ASN D C   1 
ATOM   7030 O  O   . ASN D 1 71  ? -7.305  7.988   -43.206 1.00 12.76 ? 71  ASN D O   1 
ATOM   7031 C  CB  . ASN D 1 71  ? -6.097  10.905  -43.630 1.00 12.67 ? 71  ASN D CB  1 
ATOM   7032 C  CG  . ASN D 1 71  ? -5.079  11.981  -43.836 1.00 15.53 ? 71  ASN D CG  1 
ATOM   7033 O  OD1 . ASN D 1 71  ? -3.904  11.822  -43.532 1.00 20.27 ? 71  ASN D OD1 1 
ATOM   7034 N  ND2 . ASN D 1 71  ? -5.581  13.115  -44.317 1.00 19.57 ? 71  ASN D ND2 1 
ATOM   7035 N  N   . LEU D 1 72  ? -6.760  8.863   -41.166 1.00 9.72  ? 72  LEU D N   1 
ATOM   7036 C  CA  . LEU D 1 72  ? -7.733  8.053   -40.440 1.00 10.64 ? 72  LEU D CA  1 
ATOM   7037 C  C   . LEU D 1 72  ? -8.660  8.992   -39.667 1.00 12.00 ? 72  LEU D C   1 
ATOM   7038 O  O   . LEU D 1 72  ? -8.263  10.094  -39.275 1.00 13.24 ? 72  LEU D O   1 
ATOM   7039 C  CB  . LEU D 1 72  ? -6.983  7.160   -39.441 1.00 10.41 ? 72  LEU D CB  1 
ATOM   7040 C  CG  . LEU D 1 72  ? -6.075  6.106   -40.110 1.00 10.78 ? 72  LEU D CG  1 
ATOM   7041 C  CD1 . LEU D 1 72  ? -5.248  5.401   -39.045 1.00 10.84 ? 72  LEU D CD1 1 
ATOM   7042 C  CD2 . LEU D 1 72  ? -6.883  5.112   -40.919 1.00 11.18 ? 72  LEU D CD2 1 
ATOM   7043 N  N   . PRO D 1 73  ? -9.899  8.558   -39.383 1.00 11.59 ? 73  PRO D N   1 
ATOM   7044 C  CA  . PRO D 1 73  ? -10.885 9.418   -38.697 1.00 13.16 ? 73  PRO D CA  1 
ATOM   7045 C  C   . PRO D 1 73  ? -10.742 9.348   -37.182 1.00 14.40 ? 73  PRO D C   1 
ATOM   7046 O  O   . PRO D 1 73  ? -10.297 8.339   -36.619 1.00 13.91 ? 73  PRO D O   1 
ATOM   7047 C  CB  . PRO D 1 73  ? -12.170 8.753   -39.181 1.00 12.78 ? 73  PRO D CB  1 
ATOM   7048 C  CG  . PRO D 1 73  ? -11.852 7.262   -39.232 1.00 13.18 ? 73  PRO D CG  1 
ATOM   7049 C  CD  . PRO D 1 73  ? -10.459 7.275   -39.841 1.00 12.33 ? 73  PRO D CD  1 
ATOM   7050 N  N   . SER D 1 74  ? -11.027 10.446  -36.474 1.00 17.55 ? 74  SER D N   1 
ATOM   7051 C  CA  . SER D 1 74  ? -10.751 10.479  -35.048 1.00 17.49 ? 74  SER D CA  1 
ATOM   7052 C  C   . SER D 1 74  ? -11.770 9.664   -34.235 1.00 16.93 ? 74  SER D C   1 
ATOM   7053 O  O   . SER D 1 74  ? -11.525 9.448   -33.033 1.00 19.42 ? 74  SER D O   1 
ATOM   7054 C  CB  . SER D 1 74  ? -10.653 11.908  -34.582 1.00 21.92 ? 74  SER D CB  1 
ATOM   7055 O  OG  . SER D 1 74  ? -11.879 12.576  -34.894 1.00 24.93 ? 74  SER D OG  1 
ATOM   7056 N  N   . ASP D 1 75  ? -12.813 9.157   -34.912 1.00 18.53 ? 75  ASP D N   1 
ATOM   7057 C  CA  . ASP D 1 75  ? -13.723 8.235   -34.239 1.00 22.61 ? 75  ASP D CA  1 
ATOM   7058 C  C   . ASP D 1 75  ? -13.061 6.886   -33.976 1.00 20.76 ? 75  ASP D C   1 
ATOM   7059 O  O   . ASP D 1 75  ? -13.505 6.141   -33.117 1.00 21.60 ? 75  ASP D O   1 
ATOM   7060 C  CB  . ASP D 1 75  ? -15.109 8.064   -34.876 1.00 25.59 ? 75  ASP D CB  1 
ATOM   7061 C  CG  . ASP D 1 75  ? -15.255 7.802   -36.368 1.00 39.36 ? 75  ASP D CG  1 
ATOM   7062 O  OD1 . ASP D 1 75  ? -14.302 7.314   -37.008 1.00 45.82 ? 75  ASP D OD1 1 
ATOM   7063 O  OD2 . ASP D 1 75  ? -16.363 8.080   -36.894 1.00 51.30 ? 75  ASP D OD2 1 
ATOM   7064 N  N   . MET D 1 76  ? -12.007 6.577   -34.732 1.00 15.77 ? 76  MET D N   1 
ATOM   7065 C  CA  . MET D 1 76  ? -11.207 5.372   -34.502 1.00 15.50 ? 76  MET D CA  1 
ATOM   7066 C  C   . MET D 1 76  ? -10.289 5.609   -33.290 1.00 13.34 ? 76  MET D C   1 
ATOM   7067 O  O   . MET D 1 76  ? -9.640  6.655   -33.192 1.00 14.08 ? 76  MET D O   1 
ATOM   7068 C  CB  . MET D 1 76  ? -10.442 5.186   -35.818 1.00 18.84 ? 76  MET D CB  1 
ATOM   7069 C  CG  . MET D 1 76  ? -9.626  3.968   -35.871 1.00 17.60 ? 76  MET D CG  1 
ATOM   7070 S  SD  . MET D 1 76  ? -8.930  3.901   -37.588 1.00 15.91 ? 76  MET D SD  1 
ATOM   7071 C  CE  . MET D 1 76  ? -7.508  2.897   -37.177 1.00 14.72 ? 76  MET D CE  1 
ATOM   7072 N  N   . HIS D 1 77  ? -10.268 4.684   -32.269 1.00 12.31 ? 77  HIS D N   1 
ATOM   7073 C  CA  . HIS D 1 77  ? -9.482  4.959   -31.090 1.00 14.01 ? 77  HIS D CA  1 
ATOM   7074 C  C   . HIS D 1 77  ? -9.026  3.694   -30.417 1.00 12.36 ? 77  HIS D C   1 
ATOM   7075 O  O   . HIS D 1 77  ? -9.601  2.648   -30.716 1.00 14.76 ? 77  HIS D O   1 
ATOM   7076 C  CB  . HIS D 1 77  ? -10.284 5.878   -30.148 1.00 16.99 ? 77  HIS D CB  1 
ATOM   7077 C  CG  . HIS D 1 77  ? -11.546 5.313   -29.584 1.00 22.24 ? 77  HIS D CG  1 
ATOM   7078 N  ND1 . HIS D 1 77  ? -12.740 5.219   -30.295 1.00 25.74 ? 77  HIS D ND1 1 
ATOM   7079 C  CD2 . HIS D 1 77  ? -11.822 4.857   -28.342 1.00 24.61 ? 77  HIS D CD2 1 
ATOM   7080 C  CE1 . HIS D 1 77  ? -13.685 4.673   -29.522 1.00 24.08 ? 77  HIS D CE1 1 
ATOM   7081 N  NE2 . HIS D 1 77  ? -13.142 4.465   -28.323 1.00 27.83 ? 77  HIS D NE2 1 
ATOM   7082 N  N   . ILE D 1 78  ? -8.051  3.892   -29.550 1.00 13.59 ? 78  ILE D N   1 
ATOM   7083 C  CA  . ILE D 1 78  ? -7.543  2.832   -28.697 1.00 15.78 ? 78  ILE D CA  1 
ATOM   7084 C  C   . ILE D 1 78  ? -8.122  3.071   -27.308 1.00 18.31 ? 78  ILE D C   1 
ATOM   7085 O  O   . ILE D 1 78  ? -8.038  4.201   -26.786 1.00 18.42 ? 78  ILE D O   1 
ATOM   7086 C  CB  . ILE D 1 78  ? -6.015  2.810   -28.600 1.00 16.37 ? 78  ILE D CB  1 
ATOM   7087 C  CG1 . ILE D 1 78  ? -5.237  2.560   -29.893 1.00 19.29 ? 78  ILE D CG1 1 
ATOM   7088 C  CG2 . ILE D 1 78  ? -5.581  1.779   -27.559 1.00 19.67 ? 78  ILE D CG2 1 
ATOM   7089 C  CD1 . ILE D 1 78  ? -3.807  3.097   -29.759 1.00 20.40 ? 78  ILE D CD1 1 
ATOM   7090 N  N   . GLN D 1 79  ? -8.517  1.963   -26.681 1.00 20.79 ? 79  GLN D N   1 
ATOM   7091 C  CA  . GLN D 1 79  ? -8.896  1.961   -25.276 1.00 25.17 ? 79  GLN D CA  1 
ATOM   7092 C  C   . GLN D 1 79  ? -7.964  1.042   -24.492 1.00 22.74 ? 79  GLN D C   1 
ATOM   7093 O  O   . GLN D 1 79  ? -7.480  0.010   -24.993 1.00 21.48 ? 79  GLN D O   1 
ATOM   7094 C  CB  . GLN D 1 79  ? -10.377 1.594   -25.114 1.00 30.61 ? 79  GLN D CB  1 
ATOM   7095 C  CG  . GLN D 1 79  ? -11.308 2.799   -25.246 1.00 40.41 ? 79  GLN D CG  1 
ATOM   7096 C  CD  . GLN D 1 79  ? -11.100 3.896   -24.223 1.00 46.49 ? 79  GLN D CD  1 
ATOM   7097 O  OE1 . GLN D 1 79  ? -10.492 3.704   -23.168 1.00 54.69 ? 79  GLN D OE1 1 
ATOM   7098 N  NE2 . GLN D 1 79  ? -11.605 5.078   -24.530 1.00 45.57 ? 79  GLN D NE2 1 
ATOM   7099 N  N   . GLY D 1 80  ? -7.587  1.468   -23.282 1.00 22.93 ? 80  GLY D N   1 
ATOM   7100 C  CA  . GLY D 1 80  ? -6.762  0.582   -22.485 1.00 20.11 ? 80  GLY D CA  1 
ATOM   7101 C  C   . GLY D 1 80  ? -5.585  1.325   -21.888 1.00 22.30 ? 80  GLY D C   1 
ATOM   7102 O  O   . GLY D 1 80  ? -4.971  0.813   -20.969 1.00 23.37 ? 80  GLY D O   1 
ATOM   7103 N  N   . LEU D 1 81  ? -5.221  2.495   -22.463 1.00 18.26 ? 81  LEU D N   1 
ATOM   7104 C  CA  . LEU D 1 81  ? -4.062  3.249   -22.014 1.00 19.14 ? 81  LEU D CA  1 
ATOM   7105 C  C   . LEU D 1 81  ? -4.471  4.252   -20.927 1.00 18.49 ? 81  LEU D C   1 
ATOM   7106 O  O   . LEU D 1 81  ? -5.599  4.216   -20.484 1.00 21.08 ? 81  LEU D O   1 
ATOM   7107 C  CB  . LEU D 1 81  ? -3.491  3.952   -23.253 1.00 20.26 ? 81  LEU D CB  1 
ATOM   7108 C  CG  . LEU D 1 81  ? -2.967  3.019   -24.366 1.00 18.50 ? 81  LEU D CG  1 
ATOM   7109 C  CD1 . LEU D 1 81  ? -2.671  3.831   -25.632 1.00 20.03 ? 81  LEU D CD1 1 
ATOM   7110 C  CD2 . LEU D 1 81  ? -1.730  2.282   -23.863 1.00 18.52 ? 81  LEU D CD2 1 
ATOM   7111 N  N   . GLN D 1 82  ? -3.589  5.176   -20.516 1.00 17.71 ? 82  GLN D N   1 
ATOM   7112 C  CA  . GLN D 1 82  ? -3.931  6.056   -19.379 1.00 17.12 ? 82  GLN D CA  1 
ATOM   7113 C  C   . GLN D 1 82  ? -4.914  7.148   -19.811 1.00 17.95 ? 82  GLN D C   1 
ATOM   7114 O  O   . GLN D 1 82  ? -5.555  7.757   -18.965 1.00 18.05 ? 82  GLN D O   1 
ATOM   7115 C  CB  . GLN D 1 82  ? -2.668  6.652   -18.734 1.00 18.64 ? 82  GLN D CB  1 
ATOM   7116 C  CG  . GLN D 1 82  ? -2.200  7.978   -19.351 1.00 21.69 ? 82  GLN D CG  1 
ATOM   7117 C  CD  . GLN D 1 82  ? -1.658  7.821   -20.759 1.00 23.71 ? 82  GLN D CD  1 
ATOM   7118 O  OE1 . GLN D 1 82  ? -1.406  6.710   -21.250 1.00 23.06 ? 82  GLN D OE1 1 
ATOM   7119 N  NE2 . GLN D 1 82  ? -1.488  8.945   -21.438 1.00 24.17 ? 82  GLN D NE2 1 
ATOM   7120 N  N   . SER D 1 83  ? -5.140  7.316   -21.125 1.00 16.67 ? 83  SER D N   1 
ATOM   7121 C  CA  . SER D 1 83  ? -6.038  8.304   -21.739 1.00 17.44 ? 83  SER D CA  1 
ATOM   7122 C  C   . SER D 1 83  ? -6.620  7.674   -23.010 1.00 17.66 ? 83  SER D C   1 
ATOM   7123 O  O   . SER D 1 83  ? -6.002  6.709   -23.524 1.00 16.41 ? 83  SER D O   1 
ATOM   7124 C  CB  . SER D 1 83  ? -5.267  9.567   -22.103 1.00 16.59 ? 83  SER D CB  1 
ATOM   7125 O  OG  . SER D 1 83  ? -4.688  10.186  -20.923 1.00 17.49 ? 83  SER D OG  1 
ATOM   7126 N  N   . ARG D 1 84  ? -7.714  8.212   -23.581 1.00 16.61 ? 84  ARG D N   1 
ATOM   7127 C  CA  . ARG D 1 84  ? -8.219  7.866   -24.907 1.00 16.89 ? 84  ARG D CA  1 
ATOM   7128 C  C   . ARG D 1 84  ? -7.234  8.443   -25.935 1.00 15.45 ? 84  ARG D C   1 
ATOM   7129 O  O   . ARG D 1 84  ? -6.846  9.621   -25.893 1.00 15.80 ? 84  ARG D O   1 
ATOM   7130 C  CB  . ARG D 1 84  ? -9.587  8.482   -25.262 1.00 18.78 ? 84  ARG D CB  1 
ATOM   7131 C  CG  . ARG D 1 84  ? -10.091 8.173   -26.665 1.00 22.70 ? 84  ARG D CG  1 
ATOM   7132 C  CD  . ARG D 1 84  ? -11.545 8.479   -26.993 1.00 25.82 ? 84  ARG D CD  1 
ATOM   7133 N  NE  . ARG D 1 84  ? -11.651 8.553   -28.449 1.00 28.54 ? 84  ARG D NE  1 
ATOM   7134 C  CZ  . ARG D 1 84  ? -12.789 8.418   -29.144 1.00 30.56 ? 84  ARG D CZ  1 
ATOM   7135 N  NH1 . ARG D 1 84  ? -13.940 8.283   -28.486 1.00 31.56 ? 84  ARG D NH1 1 
ATOM   7136 N  NH2 . ARG D 1 84  ? -12.784 8.465   -30.474 1.00 30.43 ? 84  ARG D NH2 1 
ATOM   7137 N  N   . TYR D 1 85  ? -6.772  7.581   -26.849 1.00 13.56 ? 85  TYR D N   1 
ATOM   7138 C  CA  . TYR D 1 85  ? -5.989  8.006   -27.998 1.00 13.31 ? 85  TYR D CA  1 
ATOM   7139 C  C   . TYR D 1 85  ? -6.795  7.751   -29.254 1.00 13.63 ? 85  TYR D C   1 
ATOM   7140 O  O   . TYR D 1 85  ? -7.231  6.657   -29.536 1.00 15.25 ? 85  TYR D O   1 
ATOM   7141 C  CB  . TYR D 1 85  ? -4.697  7.206   -27.970 1.00 12.34 ? 85  TYR D CB  1 
ATOM   7142 C  CG  . TYR D 1 85  ? -3.685  7.713   -27.003 1.00 11.74 ? 85  TYR D CG  1 
ATOM   7143 C  CD1 . TYR D 1 85  ? -3.691  7.288   -25.660 1.00 12.42 ? 85  TYR D CD1 1 
ATOM   7144 C  CD2 . TYR D 1 85  ? -2.715  8.632   -27.377 1.00 11.04 ? 85  TYR D CD2 1 
ATOM   7145 C  CE1 . TYR D 1 85  ? -2.752  7.767   -24.754 1.00 13.48 ? 85  TYR D CE1 1 
ATOM   7146 C  CE2 . TYR D 1 85  ? -1.792  9.100   -26.470 1.00 11.65 ? 85  TYR D CE2 1 
ATOM   7147 C  CZ  . TYR D 1 85  ? -1.798  8.705   -25.141 1.00 13.42 ? 85  TYR D CZ  1 
ATOM   7148 O  OH  . TYR D 1 85  ? -0.822  9.119   -24.268 1.00 14.84 ? 85  TYR D OH  1 
ATOM   7149 N  N   . SER D 1 86  ? -6.926  8.801   -30.075 1.00 11.50 ? 86  SER D N   1 
ATOM   7150 C  CA  . SER D 1 86  ? -7.693  8.774   -31.305 1.00 12.35 ? 86  SER D CA  1 
ATOM   7151 C  C   . SER D 1 86  ? -6.774  8.702   -32.546 1.00 9.94  ? 86  SER D C   1 
ATOM   7152 O  O   . SER D 1 86  ? -5.716  9.319   -32.554 1.00 10.76 ? 86  SER D O   1 
ATOM   7153 C  CB  . SER D 1 86  ? -8.578  9.987   -31.433 1.00 12.54 ? 86  SER D CB  1 
ATOM   7154 O  OG  . SER D 1 86  ? -9.492  10.029  -30.307 1.00 15.41 ? 86  SER D OG  1 
ATOM   7155 N  N   . ALA D 1 87  ? -7.192  7.873   -33.512 1.00 10.63 ? 87  ALA D N   1 
ATOM   7156 C  CA  . ALA D 1 87  ? -6.338  7.727   -34.713 1.00 10.31 ? 87  ALA D CA  1 
ATOM   7157 C  C   . ALA D 1 87  ? -6.210  9.041   -35.471 1.00 11.37 ? 87  ALA D C   1 
ATOM   7158 O  O   . ALA D 1 87  ? -7.143  9.866   -35.534 1.00 12.20 ? 87  ALA D O   1 
ATOM   7159 C  CB  . ALA D 1 87  ? -6.898  6.672   -35.619 1.00 11.86 ? 87  ALA D CB  1 
ATOM   7160 N  N   . THR D 1 88  ? -5.056  9.194   -36.135 1.00 10.02 ? 88  THR D N   1 
ATOM   7161 C  CA  . THR D 1 88  ? -4.827  10.309  -37.060 1.00 10.75 ? 88  THR D CA  1 
ATOM   7162 C  C   . THR D 1 88  ? -4.348  9.835   -38.440 1.00 9.27  ? 88  THR D C   1 
ATOM   7163 O  O   . THR D 1 88  ? -4.789  10.322  -39.474 1.00 10.18 ? 88  THR D O   1 
ATOM   7164 C  CB  . THR D 1 88  ? -3.985  11.430  -36.444 1.00 13.58 ? 88  THR D CB  1 
ATOM   7165 O  OG1 . THR D 1 88  ? -3.828  12.507  -37.392 1.00 15.96 ? 88  THR D OG1 1 
ATOM   7166 C  CG2 . THR D 1 88  ? -2.622  10.957  -36.013 1.00 13.68 ? 88  THR D CG2 1 
ATOM   7167 N  N   . GLN D 1 89  ? -3.427  8.844   -38.477 1.00 8.84  ? 89  GLN D N   1 
ATOM   7168 C  CA  . GLN D 1 89  ? -2.936  8.379   -39.777 1.00 8.41  ? 89  GLN D CA  1 
ATOM   7169 C  C   . GLN D 1 89  ? -2.176  7.081   -39.541 1.00 7.48  ? 89  GLN D C   1 
ATOM   7170 O  O   . GLN D 1 89  ? -1.753  6.789   -38.429 1.00 8.20  ? 89  GLN D O   1 
ATOM   7171 C  CB  . GLN D 1 89  ? -2.002  9.442   -40.435 1.00 8.65  ? 89  GLN D CB  1 
ATOM   7172 C  CG  . GLN D 1 89  ? -0.870  9.911   -39.535 1.00 10.84 ? 89  GLN D CG  1 
ATOM   7173 C  CD  . GLN D 1 89  ? 0.491   9.521   -40.015 1.00 11.08 ? 89  GLN D CD  1 
ATOM   7174 O  OE1 . GLN D 1 89  ? 0.707   8.356   -40.262 1.00 11.78 ? 89  GLN D OE1 1 
ATOM   7175 N  NE2 . GLN D 1 89  ? 1.418   10.443  -39.948 1.00 13.88 ? 89  GLN D NE2 1 
ATOM   7176 N  N   . LEU D 1 90  ? -1.987  6.363   -40.637 1.00 7.14  ? 90  LEU D N   1 
ATOM   7177 C  CA  . LEU D 1 90  ? -1.022  5.262   -40.631 1.00 7.25  ? 90  LEU D CA  1 
ATOM   7178 C  C   . LEU D 1 90  ? -0.044  5.434   -41.791 1.00 6.62  ? 90  LEU D C   1 
ATOM   7179 O  O   . LEU D 1 90  ? -0.362  6.107   -42.769 1.00 8.18  ? 90  LEU D O   1 
ATOM   7180 C  CB  . LEU D 1 90  ? -1.685  3.868   -40.652 1.00 7.73  ? 90  LEU D CB  1 
ATOM   7181 C  CG  . LEU D 1 90  ? -2.651  3.505   -41.762 1.00 7.19  ? 90  LEU D CG  1 
ATOM   7182 C  CD1 . LEU D 1 90  ? -1.921  3.172   -43.081 1.00 8.52  ? 90  LEU D CD1 1 
ATOM   7183 C  CD2 . LEU D 1 90  ? -3.500  2.324   -41.364 1.00 8.90  ? 90  LEU D CD2 1 
ATOM   7184 N  N   . HIS D 1 91  ? 1.126   4.796   -41.669 1.00 6.91  ? 91  HIS D N   1 
ATOM   7185 C  CA  . HIS D 1 91  ? 2.133   4.910   -42.711 1.00 6.72  ? 91  HIS D CA  1 
ATOM   7186 C  C   . HIS D 1 91  ? 3.071   3.726   -42.535 1.00 7.00  ? 91  HIS D C   1 
ATOM   7187 O  O   . HIS D 1 91  ? 2.976   2.948   -41.566 1.00 7.17  ? 91  HIS D O   1 
ATOM   7188 C  CB  . HIS D 1 91  ? 2.869   6.273   -42.658 1.00 6.90  ? 91  HIS D CB  1 
ATOM   7189 C  CG  . HIS D 1 91  ? 3.602   6.433   -41.377 1.00 6.31  ? 91  HIS D CG  1 
ATOM   7190 N  ND1 . HIS D 1 91  ? 3.084   7.056   -40.248 1.00 7.18  ? 91  HIS D ND1 1 
ATOM   7191 C  CD2 . HIS D 1 91  ? 4.797   5.929   -40.988 1.00 7.08  ? 91  HIS D CD2 1 
ATOM   7192 C  CE1 . HIS D 1 91  ? 3.944   6.932   -39.239 1.00 6.92  ? 91  HIS D CE1 1 
ATOM   7193 N  NE2 . HIS D 1 91  ? 4.999   6.232   -39.668 1.00 7.18  ? 91  HIS D NE2 1 
ATOM   7194 N  N   . LEU D 1 92  ? 4.033   3.603   -43.494 1.00 7.20  ? 92  LEU D N   1 
ATOM   7195 C  CA  . LEU D 1 92  ? 4.955   2.472   -43.456 1.00 7.80  ? 92  LEU D CA  1 
ATOM   7196 C  C   . LEU D 1 92  ? 6.418   2.908   -43.599 1.00 7.39  ? 92  LEU D C   1 
ATOM   7197 O  O   . LEU D 1 92  ? 6.748   4.016   -43.966 1.00 8.04  ? 92  LEU D O   1 
ATOM   7198 C  CB  . LEU D 1 92  ? 4.615   1.516   -44.600 1.00 9.94  ? 92  LEU D CB  1 
ATOM   7199 C  CG  . LEU D 1 92  ? 3.230   0.873   -44.484 1.00 10.00 ? 92  LEU D CG  1 
ATOM   7200 C  CD1 . LEU D 1 92  ? 2.226   1.532   -45.368 1.00 15.56 ? 92  LEU D CD1 1 
ATOM   7201 C  CD2 . LEU D 1 92  ? 3.293   -0.610  -44.626 1.00 12.56 ? 92  LEU D CD2 1 
ATOM   7202 N  N   . HIS D 1 93  ? 7.263   1.972   -43.255 1.00 6.92  ? 93  HIS D N   1 
ATOM   7203 C  CA  . HIS D 1 93  ? 8.713   2.127   -43.439 1.00 6.81  ? 93  HIS D CA  1 
ATOM   7204 C  C   . HIS D 1 93  ? 9.218   0.860   -44.089 1.00 6.98  ? 93  HIS D C   1 
ATOM   7205 O  O   . HIS D 1 93  ? 8.734   -0.241  -43.764 1.00 7.61  ? 93  HIS D O   1 
ATOM   7206 C  CB  . HIS D 1 93  ? 9.433   2.274   -42.084 1.00 7.09  ? 93  HIS D CB  1 
ATOM   7207 C  CG  . HIS D 1 93  ? 8.967   3.445   -41.297 1.00 7.35  ? 93  HIS D CG  1 
ATOM   7208 N  ND1 . HIS D 1 93  ? 9.560   4.689   -41.388 1.00 7.46  ? 93  HIS D ND1 1 
ATOM   7209 C  CD2 . HIS D 1 93  ? 7.902   3.610   -40.463 1.00 6.44  ? 93  HIS D CD2 1 
ATOM   7210 C  CE1 . HIS D 1 93  ? 8.900   5.565   -40.616 1.00 6.88  ? 93  HIS D CE1 1 
ATOM   7211 N  NE2 . HIS D 1 93  ? 7.898   4.931   -40.007 1.00 6.03  ? 93  HIS D NE2 1 
ATOM   7212 N  N   . TRP D 1 94  ? 10.201  0.985   -45.013 1.00 6.61  ? 94  TRP D N   1 
ATOM   7213 C  CA  . TRP D 1 94  ? 10.671  -0.175  -45.790 1.00 6.75  ? 94  TRP D CA  1 
ATOM   7214 C  C   . TRP D 1 94  ? 12.125  0.065   -46.220 1.00 6.92  ? 94  TRP D C   1 
ATOM   7215 O  O   . TRP D 1 94  ? 12.724  1.125   -46.041 1.00 7.71  ? 94  TRP D O   1 
ATOM   7216 C  CB  . TRP D 1 94  ? 9.737   -0.443  -46.979 1.00 8.08  ? 94  TRP D CB  1 
ATOM   7217 C  CG  . TRP D 1 94  ? 9.622   0.738   -47.906 1.00 7.94  ? 94  TRP D CG  1 
ATOM   7218 C  CD1 . TRP D 1 94  ? 10.438  1.034   -48.971 1.00 8.38  ? 94  TRP D CD1 1 
ATOM   7219 C  CD2 . TRP D 1 94  ? 8.622   1.795   -47.901 1.00 7.57  ? 94  TRP D CD2 1 
ATOM   7220 N  NE1 . TRP D 1 94  ? 10.029  2.187   -49.629 1.00 8.73  ? 94  TRP D NE1 1 
ATOM   7221 C  CE2 . TRP D 1 94  ? 8.899   2.667   -48.974 1.00 7.89  ? 94  TRP D CE2 1 
ATOM   7222 C  CE3 . TRP D 1 94  ? 7.536   2.095   -47.037 1.00 8.21  ? 94  TRP D CE3 1 
ATOM   7223 C  CZ2 . TRP D 1 94  ? 8.105   3.779   -49.272 1.00 7.88  ? 94  TRP D CZ2 1 
ATOM   7224 C  CZ3 . TRP D 1 94  ? 6.780   3.230   -47.314 1.00 8.32  ? 94  TRP D CZ3 1 
ATOM   7225 C  CH2 . TRP D 1 94  ? 7.054   4.044   -48.409 1.00 8.74  ? 94  TRP D CH2 1 
ATOM   7226 N  N   . GLY D 1 95  ? 12.633  -0.978  -46.869 1.00 7.39  ? 95  GLY D N   1 
ATOM   7227 C  CA  . GLY D 1 95  ? 14.017  -1.055  -47.338 1.00 8.19  ? 95  GLY D CA  1 
ATOM   7228 C  C   . GLY D 1 95  ? 14.082  -0.780  -48.842 1.00 8.71  ? 95  GLY D C   1 
ATOM   7229 O  O   . GLY D 1 95  ? 13.631  0.234   -49.356 1.00 8.25  ? 95  GLY D O   1 
ATOM   7230 N  N   . ASN D 1 96  ? 14.694  -1.732  -49.583 1.00 10.21 ? 96  ASN D N   1 
ATOM   7231 C  CA  . ASN D 1 96  ? 14.798  -1.522  -51.017 1.00 11.86 ? 96  ASN D CA  1 
ATOM   7232 C  C   . ASN D 1 96  ? 14.936  -2.909  -51.627 1.00 11.68 ? 96  ASN D C   1 
ATOM   7233 O  O   . ASN D 1 96  ? 15.117  -3.884  -50.912 1.00 11.88 ? 96  ASN D O   1 
ATOM   7234 C  CB  . ASN D 1 96  ? 16.015  -0.630  -51.334 1.00 13.27 ? 96  ASN D CB  1 
ATOM   7235 C  CG  . ASN D 1 96  ? 17.346  -1.306  -51.093 1.00 15.36 ? 96  ASN D CG  1 
ATOM   7236 O  OD1 . ASN D 1 96  ? 17.819  -2.043  -51.971 1.00 21.37 ? 96  ASN D OD1 1 
ATOM   7237 N  ND2 . ASN D 1 96  ? 17.969  -1.114  -49.956 1.00 15.28 ? 96  ASN D ND2 1 
ATOM   7238 N  N   . PRO D 1 97  ? 14.837  -3.025  -52.979 1.00 13.95 ? 97  PRO D N   1 
ATOM   7239 C  CA  . PRO D 1 97  ? 14.806  -4.356  -53.578 1.00 16.36 ? 97  PRO D CA  1 
ATOM   7240 C  C   . PRO D 1 97  ? 16.044  -5.205  -53.310 1.00 16.73 ? 97  PRO D C   1 
ATOM   7241 O  O   . PRO D 1 97  ? 15.919  -6.420  -53.132 1.00 23.74 ? 97  PRO D O   1 
ATOM   7242 C  CB  . PRO D 1 97  ? 14.565  -4.011  -55.041 1.00 17.85 ? 97  PRO D CB  1 
ATOM   7243 C  CG  . PRO D 1 97  ? 13.915  -2.646  -55.069 1.00 18.69 ? 97  PRO D CG  1 
ATOM   7244 C  CD  . PRO D 1 97  ? 14.576  -1.938  -53.920 1.00 14.73 ? 97  PRO D CD  1 
ATOM   7245 N  N   . ASN D 1 98  ? 17.200  -4.556  -53.136 1.00 16.23 ? 98  ASN D N   1 
ATOM   7246 C  CA  . ASN D 1 98  ? 18.434  -5.277  -52.864 1.00 21.22 ? 98  ASN D CA  1 
ATOM   7247 C  C   . ASN D 1 98  ? 18.629  -5.521  -51.368 1.00 24.02 ? 98  ASN D C   1 
ATOM   7248 O  O   . ASN D 1 98  ? 19.601  -6.175  -50.994 1.00 23.75 ? 98  ASN D O   1 
ATOM   7249 C  CB  . ASN D 1 98  ? 19.666  -4.490  -53.323 1.00 21.80 ? 98  ASN D CB  1 
ATOM   7250 C  CG  . ASN D 1 98  ? 19.693  -4.276  -54.824 1.00 30.17 ? 98  ASN D CG  1 
ATOM   7251 O  OD1 . ASN D 1 98  ? 19.079  -5.036  -55.585 1.00 36.48 ? 98  ASN D OD1 1 
ATOM   7252 N  ND2 . ASN D 1 98  ? 20.377  -3.225  -55.250 1.00 31.93 ? 98  ASN D ND2 1 
ATOM   7253 N  N   . ASP D 1 99  ? 17.803  -4.914  -50.498 1.00 18.05 ? 99  ASP D N   1 
ATOM   7254 C  CA  . ASP D 1 99  ? 17.929  -5.185  -49.071 1.00 18.44 ? 99  ASP D CA  1 
ATOM   7255 C  C   . ASP D 1 99  ? 16.538  -4.990  -48.461 1.00 14.86 ? 99  ASP D C   1 
ATOM   7256 O  O   . ASP D 1 99  ? 16.222  -3.905  -47.952 1.00 13.49 ? 99  ASP D O   1 
ATOM   7257 C  CB  . ASP D 1 99  ? 18.991  -4.303  -48.401 1.00 18.56 ? 99  ASP D CB  1 
ATOM   7258 C  CG  . ASP D 1 99  ? 19.115  -4.464  -46.889 1.00 23.39 ? 99  ASP D CG  1 
ATOM   7259 O  OD1 . ASP D 1 99  ? 18.744  -5.541  -46.380 1.00 24.43 ? 99  ASP D OD1 1 
ATOM   7260 O  OD2 . ASP D 1 99  ? 19.563  -3.498  -46.223 1.00 31.77 ? 99  ASP D OD2 1 
ATOM   7261 N  N   . PRO D 1 100 ? 15.656  -5.981  -48.563 1.00 13.92 ? 100 PRO D N   1 
ATOM   7262 C  CA  . PRO D 1 100 ? 14.257  -5.833  -48.132 1.00 12.55 ? 100 PRO D CA  1 
ATOM   7263 C  C   . PRO D 1 100 ? 14.130  -6.045  -46.625 1.00 11.88 ? 100 PRO D C   1 
ATOM   7264 O  O   . PRO D 1 100 ? 13.514  -6.977  -46.151 1.00 13.26 ? 100 PRO D O   1 
ATOM   7265 C  CB  . PRO D 1 100 ? 13.480  -6.884  -48.954 1.00 15.38 ? 100 PRO D CB  1 
ATOM   7266 C  CG  . PRO D 1 100 ? 14.542  -7.960  -49.178 1.00 15.91 ? 100 PRO D CG  1 
ATOM   7267 C  CD  . PRO D 1 100 ? 15.897  -7.281  -49.238 1.00 15.93 ? 100 PRO D CD  1 
ATOM   7268 N  N   . HIS D 1 101 ? 14.832  -5.197  -45.859 1.00 11.62 ? 101 HIS D N   1 
ATOM   7269 C  CA  . HIS D 1 101 ? 14.973  -5.352  -44.409 1.00 12.71 ? 101 HIS D CA  1 
ATOM   7270 C  C   . HIS D 1 101 ? 14.902  -3.980  -43.752 1.00 12.20 ? 101 HIS D C   1 
ATOM   7271 O  O   . HIS D 1 101 ? 15.852  -3.552  -43.071 1.00 15.05 ? 101 HIS D O   1 
ATOM   7272 C  CB  . HIS D 1 101 ? 16.321  -6.042  -44.070 1.00 15.65 ? 101 HIS D CB  1 
ATOM   7273 C  CG  . HIS D 1 101 ? 16.398  -7.412  -44.662 1.00 18.49 ? 101 HIS D CG  1 
ATOM   7274 N  ND1 . HIS D 1 101 ? 15.706  -8.501  -44.167 1.00 22.61 ? 101 HIS D ND1 1 
ATOM   7275 C  CD2 . HIS D 1 101 ? 17.075  -7.861  -45.734 1.00 18.79 ? 101 HIS D CD2 1 
ATOM   7276 C  CE1 . HIS D 1 101 ? 15.926  -9.564  -44.931 1.00 22.23 ? 101 HIS D CE1 1 
ATOM   7277 N  NE2 . HIS D 1 101 ? 16.748  -9.181  -45.923 1.00 22.13 ? 101 HIS D NE2 1 
ATOM   7278 N  N   . GLY D 1 102 ? 13.759  -3.339  -43.896 1.00 9.46  ? 102 GLY D N   1 
ATOM   7279 C  CA  . GLY D 1 102 ? 13.588  -1.941  -43.553 1.00 9.12  ? 102 GLY D CA  1 
ATOM   7280 C  C   . GLY D 1 102 ? 12.605  -1.657  -42.419 1.00 8.78  ? 102 GLY D C   1 
ATOM   7281 O  O   . GLY D 1 102 ? 12.123  -0.536  -42.318 1.00 9.97  ? 102 GLY D O   1 
ATOM   7282 N  N   . SER D 1 103 ? 12.359  -2.633  -41.530 1.00 8.39  ? 103 SER D N   1 
ATOM   7283 C  CA  . SER D 1 103 ? 11.628  -2.262  -40.316 1.00 7.72  ? 103 SER D CA  1 
ATOM   7284 C  C   . SER D 1 103 ? 12.452  -1.262  -39.510 1.00 8.04  ? 103 SER D C   1 
ATOM   7285 O  O   . SER D 1 103 ? 13.686  -1.217  -39.624 1.00 8.56  ? 103 SER D O   1 
ATOM   7286 C  CB  . SER D 1 103 ? 11.289  -3.453  -39.424 1.00 8.21  ? 103 SER D CB  1 
ATOM   7287 O  OG  . SER D 1 103 ? 12.479  -4.063  -38.882 1.00 7.99  ? 103 SER D OG  1 
ATOM   7288 N  N   . GLU D 1 104 ? 11.777  -0.498  -38.657 1.00 7.38  ? 104 GLU D N   1 
ATOM   7289 C  CA  . GLU D 1 104 ? 12.484  0.405   -37.747 1.00 7.40  ? 104 GLU D CA  1 
ATOM   7290 C  C   . GLU D 1 104 ? 12.895  -0.327  -36.476 1.00 6.71  ? 104 GLU D C   1 
ATOM   7291 O  O   . GLU D 1 104 ? 14.049  -0.335  -36.113 1.00 7.22  ? 104 GLU D O   1 
ATOM   7292 C  CB  . GLU D 1 104 ? 11.599  1.612   -37.458 1.00 8.36  ? 104 GLU D CB  1 
ATOM   7293 C  CG  . GLU D 1 104 ? 11.174  2.323   -38.725 1.00 8.74  ? 104 GLU D CG  1 
ATOM   7294 C  CD  . GLU D 1 104 ? 11.089  3.823   -38.496 1.00 8.51  ? 104 GLU D CD  1 
ATOM   7295 O  OE1 . GLU D 1 104 ? 10.120  4.233   -37.884 1.00 8.61  ? 104 GLU D OE1 1 
ATOM   7296 O  OE2 . GLU D 1 104 ? 12.049  4.530   -38.852 1.00 9.07  ? 104 GLU D OE2 1 
ATOM   7297 N  N   . HIS D 1 105 ? 11.941  -0.905  -35.755 1.00 7.17  ? 105 HIS D N   1 
ATOM   7298 C  CA  . HIS D 1 105 ? 12.281  -1.761  -34.623 1.00 7.84  ? 105 HIS D CA  1 
ATOM   7299 C  C   . HIS D 1 105 ? 12.933  -3.023  -35.162 1.00 7.77  ? 105 HIS D C   1 
ATOM   7300 O  O   . HIS D 1 105 ? 12.577  -3.540  -36.233 1.00 8.43  ? 105 HIS D O   1 
ATOM   7301 C  CB  . HIS D 1 105 ? 11.027  -2.055  -33.785 1.00 7.96  ? 105 HIS D CB  1 
ATOM   7302 C  CG  . HIS D 1 105 ? 10.532  -0.835  -33.093 1.00 7.72  ? 105 HIS D CG  1 
ATOM   7303 N  ND1 . HIS D 1 105 ? 9.600   -0.000  -33.680 1.00 8.82  ? 105 HIS D ND1 1 
ATOM   7304 C  CD2 . HIS D 1 105 ? 10.858  -0.251  -31.902 1.00 8.00  ? 105 HIS D CD2 1 
ATOM   7305 C  CE1 . HIS D 1 105 ? 9.359   1.035   -32.870 1.00 8.88  ? 105 HIS D CE1 1 
ATOM   7306 N  NE2 . HIS D 1 105 ? 10.112  0.894   -31.783 1.00 8.56  ? 105 HIS D NE2 1 
ATOM   7307 N  N   . THR D 1 106 ? 13.838  -3.546  -34.359 1.00 8.11  ? 106 THR D N   1 
ATOM   7308 C  CA  . THR D 1 106 ? 14.464  -4.830  -34.633 1.00 8.67  ? 106 THR D CA  1 
ATOM   7309 C  C   . THR D 1 106 ? 14.191  -5.750  -33.454 1.00 9.46  ? 106 THR D C   1 
ATOM   7310 O  O   . THR D 1 106 ? 13.890  -5.278  -32.382 1.00 9.43  ? 106 THR D O   1 
ATOM   7311 C  CB  . THR D 1 106 ? 15.952  -4.677  -34.929 1.00 9.05  ? 106 THR D CB  1 
ATOM   7312 O  OG1 . THR D 1 106 ? 16.608  -4.056  -33.809 1.00 9.50  ? 106 THR D OG1 1 
ATOM   7313 C  CG2 . THR D 1 106 ? 16.189  -3.826  -36.152 1.00 11.25 ? 106 THR D CG2 1 
ATOM   7314 N  N   . VAL D 1 107 ? 14.252  -7.057  -33.688 1.00 10.35 ? 107 VAL D N   1 
ATOM   7315 C  CA  . VAL D 1 107 ? 14.055  -8.048  -32.638 1.00 12.39 ? 107 VAL D CA  1 
ATOM   7316 C  C   . VAL D 1 107 ? 15.302  -8.906  -32.603 1.00 12.40 ? 107 VAL D C   1 
ATOM   7317 O  O   . VAL D 1 107 ? 15.697  -9.491  -33.602 1.00 12.99 ? 107 VAL D O   1 
ATOM   7318 C  CB  . VAL D 1 107 ? 12.769  -8.882  -32.843 1.00 11.69 ? 107 VAL D CB  1 
ATOM   7319 C  CG1 . VAL D 1 107 ? 12.681  -9.931  -31.749 1.00 15.87 ? 107 VAL D CG1 1 
ATOM   7320 C  CG2 . VAL D 1 107 ? 11.520  -7.996  -32.789 1.00 13.26 ? 107 VAL D CG2 1 
ATOM   7321 N  N   . SER D 1 108 ? 15.943  -8.906  -31.432 1.00 12.65 ? 108 SER D N   1 
ATOM   7322 C  CA  . SER D 1 108 ? 17.199  -9.671  -31.247 1.00 13.53 ? 108 SER D CA  1 
ATOM   7323 C  C   . SER D 1 108 ? 18.195  -9.366  -32.370 1.00 13.73 ? 108 SER D C   1 
ATOM   7324 O  O   . SER D 1 108 ? 18.820  -10.257 -32.967 1.00 14.18 ? 108 SER D O   1 
ATOM   7325 C  CB  . SER D 1 108 ? 16.934  -11.161 -31.114 1.00 15.43 ? 108 SER D CB  1 
ATOM   7326 O  OG  . SER D 1 108 ? 16.115  -11.385 -30.002 1.00 17.84 ? 108 SER D OG  1 
ATOM   7327 N  N   . GLY D 1 109 ? 18.277  -8.088  -32.694 1.00 11.78 ? 109 GLY D N   1 
ATOM   7328 C  CA  . GLY D 1 109 ? 19.179  -7.548  -33.711 1.00 13.20 ? 109 GLY D CA  1 
ATOM   7329 C  C   . GLY D 1 109 ? 18.761  -7.736  -35.183 1.00 14.23 ? 109 GLY D C   1 
ATOM   7330 O  O   . GLY D 1 109 ? 19.553  -7.390  -36.064 1.00 18.04 ? 109 GLY D O   1 
ATOM   7331 N  N   A GLN D 1 110 ? 17.558  -8.246  -35.438 0.50 12.65 ? 110 GLN D N   1 
ATOM   7332 N  N   B GLN D 1 110 ? 17.586  -8.289  -35.462 0.50 13.37 ? 110 GLN D N   1 
ATOM   7333 C  CA  A GLN D 1 110 ? 17.107  -8.599  -36.780 0.50 12.28 ? 110 GLN D CA  1 
ATOM   7334 C  CA  B GLN D 1 110 ? 17.228  -8.531  -36.853 0.50 13.37 ? 110 GLN D CA  1 
ATOM   7335 C  C   A GLN D 1 110 ? 16.032  -7.612  -37.248 0.50 10.47 ? 110 GLN D C   1 
ATOM   7336 C  C   B GLN D 1 110 ? 16.085  -7.597  -37.247 0.50 11.18 ? 110 GLN D C   1 
ATOM   7337 O  O   A GLN D 1 110 ? 15.040  -7.414  -36.538 0.50 10.23 ? 110 GLN D O   1 
ATOM   7338 O  O   B GLN D 1 110 ? 15.117  -7.424  -36.502 0.50 11.13 ? 110 GLN D O   1 
ATOM   7339 C  CB  A GLN D 1 110 ? 16.530  -10.021 -36.777 0.50 14.15 ? 110 GLN D CB  1 
ATOM   7340 C  CB  B GLN D 1 110 ? 16.792  -9.979  -37.101 0.50 16.56 ? 110 GLN D CB  1 
ATOM   7341 C  CG  A GLN D 1 110 ? 17.500  -11.060 -36.202 0.50 16.32 ? 110 GLN D CG  1 
ATOM   7342 C  CG  B GLN D 1 110 ? 17.549  -11.029 -36.290 0.50 21.20 ? 110 GLN D CG  1 
ATOM   7343 C  CD  A GLN D 1 110 ? 18.911  -10.799 -36.672 0.50 16.46 ? 110 GLN D CD  1 
ATOM   7344 C  CD  B GLN D 1 110 ? 18.338  -11.975 -37.160 0.50 23.29 ? 110 GLN D CD  1 
ATOM   7345 O  OE1 A GLN D 1 110 ? 19.177  -10.736 -37.869 0.50 20.91 ? 110 GLN D OE1 1 
ATOM   7346 O  OE1 B GLN D 1 110 ? 19.193  -11.569 -37.939 0.50 26.66 ? 110 GLN D OE1 1 
ATOM   7347 N  NE2 A GLN D 1 110 ? 19.842  -10.679 -35.730 0.50 16.48 ? 110 GLN D NE2 1 
ATOM   7348 N  NE2 B GLN D 1 110 ? 18.080  -13.260 -37.002 0.50 24.72 ? 110 GLN D NE2 1 
ATOM   7349 N  N   . HIS D 1 111 ? 16.243  -7.041  -38.440 1.00 11.18 ? 111 HIS D N   1 
ATOM   7350 C  CA  . HIS D 1 111 ? 15.180  -6.300  -39.104 1.00 9.28  ? 111 HIS D CA  1 
ATOM   7351 C  C   . HIS D 1 111 ? 14.173  -7.234  -39.726 1.00 12.01 ? 111 HIS D C   1 
ATOM   7352 O  O   . HIS D 1 111 ? 14.489  -8.351  -40.197 1.00 13.98 ? 111 HIS D O   1 
ATOM   7353 C  CB  . HIS D 1 111 ? 15.691  -5.501  -40.293 1.00 11.41 ? 111 HIS D CB  1 
ATOM   7354 C  CG  . HIS D 1 111 ? 16.408  -4.281  -39.884 1.00 10.32 ? 111 HIS D CG  1 
ATOM   7355 N  ND1 . HIS D 1 111 ? 15.798  -3.057  -39.698 1.00 11.34 ? 111 HIS D ND1 1 
ATOM   7356 C  CD2 . HIS D 1 111 ? 17.718  -4.102  -39.645 1.00 11.82 ? 111 HIS D CD2 1 
ATOM   7357 C  CE1 . HIS D 1 111 ? 16.735  -2.173  -39.331 1.00 12.37 ? 111 HIS D CE1 1 
ATOM   7358 N  NE2 . HIS D 1 111 ? 17.903  -2.783  -39.312 1.00 15.06 ? 111 HIS D NE2 1 
ATOM   7359 N  N   . PHE D 1 112 ? 12.934  -6.794  -39.678 1.00 9.03  ? 112 PHE D N   1 
ATOM   7360 C  CA  . PHE D 1 112 ? 11.887  -7.349  -40.516 1.00 8.80  ? 112 PHE D CA  1 
ATOM   7361 C  C   . PHE D 1 112 ? 11.901  -6.605  -41.854 1.00 8.19  ? 112 PHE D C   1 
ATOM   7362 O  O   . PHE D 1 112 ? 12.610  -5.621  -42.010 1.00 8.45  ? 112 PHE D O   1 
ATOM   7363 C  CB  . PHE D 1 112 ? 10.548  -7.249  -39.766 1.00 10.66 ? 112 PHE D CB  1 
ATOM   7364 C  CG  . PHE D 1 112 ? 10.331  -8.309  -38.715 1.00 12.20 ? 112 PHE D CG  1 
ATOM   7365 C  CD1 . PHE D 1 112 ? 10.888  -8.181  -37.453 1.00 15.34 ? 112 PHE D CD1 1 
ATOM   7366 C  CD2 . PHE D 1 112 ? 9.569   -9.434  -38.987 1.00 16.83 ? 112 PHE D CD2 1 
ATOM   7367 C  CE1 . PHE D 1 112 ? 10.688  -9.155  -36.487 1.00 17.99 ? 112 PHE D CE1 1 
ATOM   7368 C  CE2 . PHE D 1 112 ? 9.370   -10.407 -38.021 1.00 21.72 ? 112 PHE D CE2 1 
ATOM   7369 C  CZ  . PHE D 1 112 ? 9.930   -10.266 -36.772 1.00 18.31 ? 112 PHE D CZ  1 
ATOM   7370 N  N   . ALA D 1 113 ? 11.093  -7.070  -42.802 1.00 7.59  ? 113 ALA D N   1 
ATOM   7371 C  CA  . ALA D 1 113 ? 11.054  -6.483  -44.134 1.00 8.40  ? 113 ALA D CA  1 
ATOM   7372 C  C   . ALA D 1 113 ? 10.581  -5.025  -44.097 1.00 7.67  ? 113 ALA D C   1 
ATOM   7373 O  O   . ALA D 1 113 ? 11.058  -4.190  -44.853 1.00 8.96  ? 113 ALA D O   1 
ATOM   7374 C  CB  . ALA D 1 113 ? 10.201  -7.299  -45.102 1.00 9.20  ? 113 ALA D CB  1 
ATOM   7375 N  N   . ALA D 1 114 ? 9.542   -4.762  -43.314 1.00 7.25  ? 114 ALA D N   1 
ATOM   7376 C  CA  . ALA D 1 114 ? 8.932   -3.433  -43.302 1.00 6.59  ? 114 ALA D CA  1 
ATOM   7377 C  C   . ALA D 1 114 ? 8.172   -3.301  -41.967 1.00 6.66  ? 114 ALA D C   1 
ATOM   7378 O  O   . ALA D 1 114 ? 8.172   -4.214  -41.112 1.00 7.49  ? 114 ALA D O   1 
ATOM   7379 C  CB  . ALA D 1 114 ? 7.975   -3.278  -44.488 1.00 7.53  ? 114 ALA D CB  1 
ATOM   7380 N  N   . GLU D 1 115 ? 7.572   -2.097  -41.757 1.00 7.14  ? 115 GLU D N   1 
ATOM   7381 C  CA  . GLU D 1 115 ? 6.852   -1.875  -40.502 1.00 6.80  ? 115 GLU D CA  1 
ATOM   7382 C  C   . GLU D 1 115 ? 5.700   -0.907  -40.789 1.00 7.17  ? 115 GLU D C   1 
ATOM   7383 O  O   . GLU D 1 115 ? 5.887   0.104   -41.490 1.00 7.80  ? 115 GLU D O   1 
ATOM   7384 C  CB  . GLU D 1 115 ? 7.818   -1.277  -39.474 1.00 7.32  ? 115 GLU D CB  1 
ATOM   7385 C  CG  . GLU D 1 115 ? 7.289   -1.173  -38.042 1.00 7.69  ? 115 GLU D CG  1 
ATOM   7386 C  CD  . GLU D 1 115 ? 8.374   -0.905  -37.014 1.00 8.06  ? 115 GLU D CD  1 
ATOM   7387 O  OE1 . GLU D 1 115 ? 9.542   -1.340  -37.234 1.00 8.28  ? 115 GLU D OE1 1 
ATOM   7388 O  OE2 . GLU D 1 115 ? 8.082   -0.270  -35.968 1.00 8.30  ? 115 GLU D OE2 1 
ATOM   7389 N  N   . LEU D 1 116 ? 4.549   -1.175  -40.168 1.00 6.69  ? 116 LEU D N   1 
ATOM   7390 C  CA  . LEU D 1 116 ? 3.379   -0.280  -40.231 1.00 6.58  ? 116 LEU D CA  1 
ATOM   7391 C  C   . LEU D 1 116 ? 3.250   0.401   -38.895 1.00 6.96  ? 116 LEU D C   1 
ATOM   7392 O  O   . LEU D 1 116 ? 3.384   -0.218  -37.830 1.00 7.07  ? 116 LEU D O   1 
ATOM   7393 C  CB  . LEU D 1 116 ? 2.123   -1.156  -40.420 1.00 7.28  ? 116 LEU D CB  1 
ATOM   7394 C  CG  . LEU D 1 116 ? 0.791   -0.382  -40.278 1.00 7.93  ? 116 LEU D CG  1 
ATOM   7395 C  CD1 . LEU D 1 116 ? 0.539   0.448   -41.491 1.00 8.68  ? 116 LEU D CD1 1 
ATOM   7396 C  CD2 . LEU D 1 116 ? -0.364  -1.362  -40.086 1.00 8.94  ? 116 LEU D CD2 1 
ATOM   7397 N  N   . HIS D 1 117 ? 3.016   1.727   -38.957 1.00 6.68  ? 117 HIS D N   1 
ATOM   7398 C  CA  . HIS D 1 117 ? 2.723   2.523   -37.759 1.00 6.55  ? 117 HIS D CA  1 
ATOM   7399 C  C   . HIS D 1 117 ? 1.344   3.142   -37.881 1.00 6.70  ? 117 HIS D C   1 
ATOM   7400 O  O   . HIS D 1 117 ? 1.026   3.800   -38.872 1.00 7.55  ? 117 HIS D O   1 
ATOM   7401 C  CB  . HIS D 1 117 ? 3.720   3.675   -37.668 1.00 6.72  ? 117 HIS D CB  1 
ATOM   7402 C  CG  . HIS D 1 117 ? 5.080   3.160   -37.347 1.00 6.22  ? 117 HIS D CG  1 
ATOM   7403 N  ND1 . HIS D 1 117 ? 6.285   3.874   -37.637 1.00 6.09  ? 117 HIS D ND1 1 
ATOM   7404 C  CD2 . HIS D 1 117 ? 5.463   1.985   -36.724 1.00 7.43  ? 117 HIS D CD2 1 
ATOM   7405 C  CE1 . HIS D 1 117 ? 7.278   3.126   -37.197 1.00 7.62  ? 117 HIS D CE1 1 
ATOM   7406 N  NE2 . HIS D 1 117 ? 6.837   1.986   -36.649 1.00 7.20  ? 117 HIS D NE2 1 
ATOM   7407 N  N   . ILE D 1 118 ? 0.518   2.853   -36.877 1.00 6.92  ? 118 ILE D N   1 
ATOM   7408 C  CA  . ILE D 1 118 ? -0.795  3.517   -36.787 1.00 7.76  ? 118 ILE D CA  1 
ATOM   7409 C  C   . ILE D 1 118 ? -0.720  4.540   -35.672 1.00 7.86  ? 118 ILE D C   1 
ATOM   7410 O  O   . ILE D 1 118 ? -0.573  4.209   -34.475 1.00 7.95  ? 118 ILE D O   1 
ATOM   7411 C  CB  . ILE D 1 118 ? -1.919  2.489   -36.562 1.00 7.94  ? 118 ILE D CB  1 
ATOM   7412 C  CG1 . ILE D 1 118 ? -1.831  1.293   -37.509 1.00 8.10  ? 118 ILE D CG1 1 
ATOM   7413 C  CG2 . ILE D 1 118 ? -3.238  3.224   -36.669 1.00 7.89  ? 118 ILE D CG2 1 
ATOM   7414 C  CD1 . ILE D 1 118 ? -2.910  0.211   -37.226 1.00 10.00 ? 118 ILE D CD1 1 
ATOM   7415 N  N   . VAL D 1 119 ? -0.715  5.820   -36.074 1.00 7.91  ? 119 VAL D N   1 
ATOM   7416 C  CA  . VAL D 1 119 ? -0.499  6.948   -35.173 1.00 8.07  ? 119 VAL D CA  1 
ATOM   7417 C  C   . VAL D 1 119 ? -1.825  7.451   -34.584 1.00 7.42  ? 119 VAL D C   1 
ATOM   7418 O  O   . VAL D 1 119 ? -2.768  7.671   -35.328 1.00 8.88  ? 119 VAL D O   1 
ATOM   7419 C  CB  . VAL D 1 119 ? 0.240   8.065   -35.920 1.00 7.96  ? 119 VAL D CB  1 
ATOM   7420 C  CG1 . VAL D 1 119 ? 0.600   9.203   -34.965 1.00 8.82  ? 119 VAL D CG1 1 
ATOM   7421 C  CG2 . VAL D 1 119 ? 1.494   7.520   -36.642 1.00 8.10  ? 119 VAL D CG2 1 
ATOM   7422 N  N   . HIS D 1 120 ? -1.803  7.559   -33.241 1.00 8.37  ? 120 HIS D N   1 
ATOM   7423 C  CA  . HIS D 1 120 ? -2.937  8.117   -32.488 1.00 8.80  ? 120 HIS D CA  1 
ATOM   7424 C  C   . HIS D 1 120 ? -2.418  9.253   -31.621 1.00 9.18  ? 120 HIS D C   1 
ATOM   7425 O  O   . HIS D 1 120 ? -1.268  9.328   -31.254 1.00 10.24 ? 120 HIS D O   1 
ATOM   7426 C  CB  . HIS D 1 120 ? -3.504  7.009   -31.593 1.00 9.25  ? 120 HIS D CB  1 
ATOM   7427 C  CG  . HIS D 1 120 ? -3.962  5.778   -32.285 1.00 9.47  ? 120 HIS D CG  1 
ATOM   7428 N  ND1 . HIS D 1 120 ? -3.041  4.837   -32.827 1.00 9.75  ? 120 HIS D ND1 1 
ATOM   7429 C  CD2 . HIS D 1 120 ? -5.182  5.244   -32.416 1.00 10.00 ? 120 HIS D CD2 1 
ATOM   7430 C  CE1 . HIS D 1 120 ? -3.755  3.825   -33.301 1.00 10.49 ? 120 HIS D CE1 1 
ATOM   7431 N  NE2 . HIS D 1 120 ? -5.095  4.021   -33.078 1.00 11.76 ? 120 HIS D NE2 1 
ATOM   7432 N  N   . TYR D 1 121 ? -3.362  10.152  -31.220 1.00 10.32 ? 121 TYR D N   1 
ATOM   7433 C  CA  . TYR D 1 121 ? -3.047  11.306  -30.368 1.00 10.81 ? 121 TYR D CA  1 
ATOM   7434 C  C   . TYR D 1 121 ? -3.991  11.297  -29.169 1.00 10.60 ? 121 TYR D C   1 
ATOM   7435 O  O   . TYR D 1 121 ? -5.081  10.748  -29.247 1.00 10.29 ? 121 TYR D O   1 
ATOM   7436 C  CB  . TYR D 1 121 ? -3.130  12.616  -31.162 1.00 11.27 ? 121 TYR D CB  1 
ATOM   7437 C  CG  . TYR D 1 121 ? -4.514  13.076  -31.480 1.00 11.27 ? 121 TYR D CG  1 
ATOM   7438 C  CD1 . TYR D 1 121 ? -5.223  12.584  -32.551 1.00 12.73 ? 121 TYR D CD1 1 
ATOM   7439 C  CD2 . TYR D 1 121 ? -5.135  14.066  -30.711 1.00 12.99 ? 121 TYR D CD2 1 
ATOM   7440 C  CE1 . TYR D 1 121 ? -6.511  12.958  -32.869 1.00 14.38 ? 121 TYR D CE1 1 
ATOM   7441 C  CE2 . TYR D 1 121 ? -6.441  14.442  -31.013 1.00 14.53 ? 121 TYR D CE2 1 
ATOM   7442 C  CZ  . TYR D 1 121 ? -7.114  13.909  -32.086 1.00 16.80 ? 121 TYR D CZ  1 
ATOM   7443 O  OH  . TYR D 1 121 ? -8.390  14.266  -32.423 1.00 20.92 ? 121 TYR D OH  1 
ATOM   7444 N  N   . ASN D 1 122 ? -3.501  11.935  -28.127 1.00 11.49 ? 122 ASN D N   1 
ATOM   7445 C  CA  . ASN D 1 122 ? -4.199  12.039  -26.833 1.00 13.39 ? 122 ASN D CA  1 
ATOM   7446 C  C   . ASN D 1 122 ? -5.324  13.077  -26.952 1.00 13.77 ? 122 ASN D C   1 
ATOM   7447 O  O   . ASN D 1 122 ? -5.057  14.273  -26.765 1.00 13.94 ? 122 ASN D O   1 
ATOM   7448 C  CB  . ASN D 1 122 ? -3.196  12.327  -25.727 1.00 13.46 ? 122 ASN D CB  1 
ATOM   7449 C  CG  . ASN D 1 122 ? -3.798  12.192  -24.340 1.00 13.02 ? 122 ASN D CG  1 
ATOM   7450 O  OD1 . ASN D 1 122 ? -5.025  12.312  -24.197 1.00 14.30 ? 122 ASN D OD1 1 
ATOM   7451 N  ND2 . ASN D 1 122 ? -2.946  11.905  -23.374 1.00 15.11 ? 122 ASN D ND2 1 
ATOM   7452 N  N   . SER D 1 123 ? -6.510  12.584  -27.287 1.00 11.21 ? 123 SER D N   1 
ATOM   7453 C  CA  . SER D 1 123 ? -7.666  13.459  -27.519 1.00 14.02 ? 123 SER D CA  1 
ATOM   7454 C  C   . SER D 1 123 ? -8.316  13.858  -26.197 1.00 15.67 ? 123 SER D C   1 
ATOM   7455 O  O   . SER D 1 123 ? -9.183  14.737  -26.195 1.00 19.51 ? 123 SER D O   1 
ATOM   7456 C  CB  . SER D 1 123 ? -8.644  12.902  -28.509 1.00 12.91 ? 123 SER D CB  1 
ATOM   7457 O  OG  . SER D 1 123 ? -8.934  11.544  -28.169 1.00 16.20 ? 123 SER D OG  1 
ATOM   7458 N  N   . ASP D 1 124 ? -7.883  13.259  -25.082 1.00 14.20 ? 124 ASP D N   1 
ATOM   7459 C  CA  . ASP D 1 124 ? -8.379  13.761  -23.791 1.00 15.29 ? 124 ASP D CA  1 
ATOM   7460 C  C   . ASP D 1 124 ? -7.691  15.069  -23.446 1.00 17.44 ? 124 ASP D C   1 
ATOM   7461 O  O   . ASP D 1 124 ? -8.237  15.849  -22.659 1.00 20.93 ? 124 ASP D O   1 
ATOM   7462 C  CB  . ASP D 1 124 ? -8.069  12.770  -22.670 1.00 17.16 ? 124 ASP D CB  1 
ATOM   7463 C  CG  . ASP D 1 124 ? -8.926  11.518  -22.714 1.00 16.44 ? 124 ASP D CG  1 
ATOM   7464 O  OD1 . ASP D 1 124 ? -9.902  11.467  -23.416 1.00 16.38 ? 124 ASP D OD1 1 
ATOM   7465 O  OD2 . ASP D 1 124 ? -8.623  10.592  -21.975 1.00 18.61 ? 124 ASP D OD2 1 
ATOM   7466 N  N   . LEU D 1 125 ? -6.469  15.266  -23.878 1.00 14.48 ? 125 LEU D N   1 
ATOM   7467 C  CA  . LEU D 1 125 ? -5.674  16.404  -23.476 1.00 16.01 ? 125 LEU D CA  1 
ATOM   7468 C  C   . LEU D 1 125 ? -5.600  17.426  -24.599 1.00 17.12 ? 125 LEU D C   1 
ATOM   7469 O  O   . LEU D 1 125 ? -5.416  18.601  -24.282 1.00 16.11 ? 125 LEU D O   1 
ATOM   7470 C  CB  . LEU D 1 125 ? -4.261  15.942  -23.135 1.00 16.66 ? 125 LEU D CB  1 
ATOM   7471 C  CG  . LEU D 1 125 ? -3.976  15.561  -21.676 1.00 18.07 ? 125 LEU D CG  1 
ATOM   7472 C  CD1 . LEU D 1 125 ? -4.811  14.361  -21.274 1.00 21.48 ? 125 LEU D CD1 1 
ATOM   7473 C  CD2 . LEU D 1 125 ? -2.505  15.246  -21.496 1.00 18.37 ? 125 LEU D CD2 1 
ATOM   7474 N  N   . TYR D 1 126 ? -5.669  16.994  -25.879 1.00 14.46 ? 126 TYR D N   1 
ATOM   7475 C  CA  . TYR D 1 126 ? -5.275  17.861  -26.978 1.00 14.49 ? 126 TYR D CA  1 
ATOM   7476 C  C   . TYR D 1 126 ? -6.342  17.881  -28.067 1.00 15.08 ? 126 TYR D C   1 
ATOM   7477 O  O   . TYR D 1 126 ? -7.030  16.897  -28.322 1.00 16.18 ? 126 TYR D O   1 
ATOM   7478 C  CB  . TYR D 1 126 ? -3.910  17.424  -27.536 1.00 13.85 ? 126 TYR D CB  1 
ATOM   7479 C  CG  . TYR D 1 126 ? -2.844  17.390  -26.481 1.00 12.83 ? 126 TYR D CG  1 
ATOM   7480 C  CD1 . TYR D 1 126 ? -2.455  18.542  -25.788 1.00 13.13 ? 126 TYR D CD1 1 
ATOM   7481 C  CD2 . TYR D 1 126 ? -2.255  16.181  -26.075 1.00 12.82 ? 126 TYR D CD2 1 
ATOM   7482 C  CE1 . TYR D 1 126 ? -1.567  18.485  -24.725 1.00 13.19 ? 126 TYR D CE1 1 
ATOM   7483 C  CE2 . TYR D 1 126 ? -1.269  16.131  -25.097 1.00 12.51 ? 126 TYR D CE2 1 
ATOM   7484 C  CZ  . TYR D 1 126 ? -0.953  17.281  -24.379 1.00 13.10 ? 126 TYR D CZ  1 
ATOM   7485 O  OH  . TYR D 1 126 ? -0.039  17.218  -23.354 1.00 13.61 ? 126 TYR D OH  1 
ATOM   7486 N  N   . PRO D 1 127 ? -6.482  19.024  -28.779 1.00 16.28 ? 127 PRO D N   1 
ATOM   7487 C  CA  . PRO D 1 127 ? -7.575  19.138  -29.745 1.00 15.91 ? 127 PRO D CA  1 
ATOM   7488 C  C   . PRO D 1 127 ? -7.329  18.517  -31.107 1.00 16.92 ? 127 PRO D C   1 
ATOM   7489 O  O   . PRO D 1 127 ? -8.242  18.360  -31.907 1.00 19.65 ? 127 PRO D O   1 
ATOM   7490 C  CB  . PRO D 1 127 ? -7.675  20.665  -29.936 1.00 17.59 ? 127 PRO D CB  1 
ATOM   7491 C  CG  . PRO D 1 127 ? -6.281  21.142  -29.630 1.00 16.46 ? 127 PRO D CG  1 
ATOM   7492 C  CD  . PRO D 1 127 ? -5.791  20.282  -28.472 1.00 17.01 ? 127 PRO D CD  1 
ATOM   7493 N  N   . ASP D 1 128 ? -6.070  18.190  -31.377 1.00 15.22 ? 128 ASP D N   1 
ATOM   7494 C  CA  . ASP D 1 128 ? -5.672  17.614  -32.641 1.00 15.33 ? 128 ASP D CA  1 
ATOM   7495 C  C   . ASP D 1 128 ? -4.269  17.052  -32.537 1.00 15.90 ? 128 ASP D C   1 
ATOM   7496 O  O   . ASP D 1 128 ? -3.543  17.338  -31.596 1.00 14.60 ? 128 ASP D O   1 
ATOM   7497 C  CB  . ASP D 1 128 ? -5.745  18.685  -33.743 1.00 17.24 ? 128 ASP D CB  1 
ATOM   7498 C  CG  . ASP D 1 128 ? -4.771  19.814  -33.471 1.00 19.37 ? 128 ASP D CG  1 
ATOM   7499 O  OD1 . ASP D 1 128 ? -5.167  20.846  -32.807 1.00 21.73 ? 128 ASP D OD1 1 
ATOM   7500 O  OD2 . ASP D 1 128 ? -3.633  19.677  -33.881 1.00 21.63 ? 128 ASP D OD2 1 
ATOM   7501 N  N   . ALA D 1 129 ? -3.847  16.258  -33.537 1.00 14.76 ? 129 ALA D N   1 
ATOM   7502 C  CA  . ALA D 1 129 ? -2.624  15.512  -33.434 1.00 14.14 ? 129 ALA D CA  1 
ATOM   7503 C  C   . ALA D 1 129 ? -1.382  16.409  -33.489 1.00 14.54 ? 129 ALA D C   1 
ATOM   7504 O  O   . ALA D 1 129 ? -0.383  16.141  -32.834 1.00 14.80 ? 129 ALA D O   1 
ATOM   7505 C  CB  . ALA D 1 129 ? -2.587  14.470  -34.550 1.00 16.23 ? 129 ALA D CB  1 
ATOM   7506 N  N   A SER D 1 130 ? -1.436  17.459  -34.337 0.50 15.12 ? 130 SER D N   1 
ATOM   7507 N  N   B SER D 1 130 ? -1.427  17.457  -34.344 0.50 16.01 ? 130 SER D N   1 
ATOM   7508 C  CA  A SER D 1 130 ? -0.304  18.364  -34.458 0.50 14.31 ? 130 SER D CA  1 
ATOM   7509 C  CA  B SER D 1 130 ? -0.309  18.383  -34.469 0.50 15.71 ? 130 SER D CA  1 
ATOM   7510 C  C   A SER D 1 130 ? -0.009  19.029  -33.112 0.50 13.50 ? 130 SER D C   1 
ATOM   7511 C  C   B SER D 1 130 ? -0.008  19.033  -33.115 0.50 14.22 ? 130 SER D C   1 
ATOM   7512 O  O   A SER D 1 130 ? 1.130   19.041  -32.659 0.50 13.98 ? 130 SER D O   1 
ATOM   7513 O  O   B SER D 1 130 ? 1.134   19.054  -32.666 0.50 14.49 ? 130 SER D O   1 
ATOM   7514 C  CB  A SER D 1 130 ? -0.534  19.372  -35.560 0.50 14.69 ? 130 SER D CB  1 
ATOM   7515 C  CB  B SER D 1 130 ? -0.586  19.422  -35.542 0.50 17.58 ? 130 SER D CB  1 
ATOM   7516 O  OG  A SER D 1 130 ? 0.623   20.174  -35.750 0.50 14.19 ? 130 SER D OG  1 
ATOM   7517 O  OG  B SER D 1 130 ? -0.712  18.834  -36.832 0.50 20.56 ? 130 SER D OG  1 
ATOM   7518 N  N   . THR D 1 131 ? -1.065  19.552  -32.476 1.00 14.49 ? 131 THR D N   1 
ATOM   7519 C  CA  . THR D 1 131 ? -0.923  20.147  -31.158 1.00 14.29 ? 131 THR D CA  1 
ATOM   7520 C  C   . THR D 1 131 ? -0.363  19.153  -30.142 1.00 15.01 ? 131 THR D C   1 
ATOM   7521 O  O   . THR D 1 131 ? 0.519   19.489  -29.368 1.00 15.33 ? 131 THR D O   1 
ATOM   7522 C  CB  . THR D 1 131 ? -2.262  20.711  -30.690 1.00 15.48 ? 131 THR D CB  1 
ATOM   7523 O  OG1 . THR D 1 131 ? -2.680  21.721  -31.615 1.00 17.93 ? 131 THR D OG1 1 
ATOM   7524 C  CG2 . THR D 1 131 ? -2.181  21.381  -29.329 1.00 17.03 ? 131 THR D CG2 1 
ATOM   7525 N  N   . ALA D 1 132 ? -0.832  17.915  -30.214 1.00 13.15 ? 132 ALA D N   1 
ATOM   7526 C  CA  . ALA D 1 132 ? -0.411  16.873  -29.284 1.00 12.87 ? 132 ALA D CA  1 
ATOM   7527 C  C   . ALA D 1 132 ? 1.047   16.469  -29.440 1.00 13.10 ? 132 ALA D C   1 
ATOM   7528 O  O   . ALA D 1 132 ? 1.712   16.029  -28.493 1.00 12.78 ? 132 ALA D O   1 
ATOM   7529 C  CB  . ALA D 1 132 ? -1.270  15.636  -29.487 1.00 13.24 ? 132 ALA D CB  1 
ATOM   7530 N  N   . SER D 1 133 ? 1.534   16.564  -30.687 1.00 12.60 ? 133 SER D N   1 
ATOM   7531 C  CA  . SER D 1 133 ? 2.753   15.881  -31.060 1.00 13.03 ? 133 SER D CA  1 
ATOM   7532 C  C   . SER D 1 133 ? 4.010   16.328  -30.299 1.00 13.49 ? 133 SER D C   1 
ATOM   7533 O  O   . SER D 1 133 ? 4.975   15.604  -30.168 1.00 13.73 ? 133 SER D O   1 
ATOM   7534 C  CB  . SER D 1 133 ? 2.936   15.989  -32.568 1.00 14.55 ? 133 SER D CB  1 
ATOM   7535 O  OG  . SER D 1 133 ? 3.357   17.311  -32.927 1.00 15.39 ? 133 SER D OG  1 
ATOM   7536 N  N   . ASN D 1 134 ? 4.047   17.579  -29.801 1.00 13.37 ? 134 ASN D N   1 
ATOM   7537 C  CA  . ASN D 1 134 ? 5.207   18.054  -29.063 1.00 14.50 ? 134 ASN D CA  1 
ATOM   7538 C  C   . ASN D 1 134 ? 4.928   18.206  -27.572 1.00 16.43 ? 134 ASN D C   1 
ATOM   7539 O  O   . ASN D 1 134 ? 5.704   18.844  -26.855 1.00 17.21 ? 134 ASN D O   1 
ATOM   7540 C  CB  . ASN D 1 134 ? 5.823   19.332  -29.669 1.00 15.95 ? 134 ASN D CB  1 
ATOM   7541 C  CG  . ASN D 1 134 ? 4.952   20.543  -29.453 1.00 19.43 ? 134 ASN D CG  1 
ATOM   7542 O  OD1 . ASN D 1 134 ? 3.735   20.428  -29.316 1.00 18.62 ? 134 ASN D OD1 1 
ATOM   7543 N  ND2 . ASN D 1 134 ? 5.593   21.711  -29.413 1.00 20.29 ? 134 ASN D ND2 1 
ATOM   7544 N  N   . LYS D 1 135 ? 3.852   17.567  -27.118 1.00 13.18 ? 135 LYS D N   1 
ATOM   7545 C  CA  . LYS D 1 135 ? 3.427   17.768  -25.739 1.00 14.59 ? 135 LYS D CA  1 
ATOM   7546 C  C   . LYS D 1 135 ? 3.369   16.450  -24.974 1.00 14.71 ? 135 LYS D C   1 
ATOM   7547 O  O   . LYS D 1 135 ? 3.324   15.362  -25.549 1.00 14.18 ? 135 LYS D O   1 
ATOM   7548 C  CB  . LYS D 1 135 ? 2.084   18.513  -25.725 1.00 14.76 ? 135 LYS D CB  1 
ATOM   7549 C  CG  . LYS D 1 135 ? 2.249   19.970  -26.190 1.00 15.40 ? 135 LYS D CG  1 
ATOM   7550 C  CD  . LYS D 1 135 ? 0.975   20.803  -26.199 1.00 17.50 ? 135 LYS D CD  1 
ATOM   7551 C  CE  . LYS D 1 135 ? 1.138   22.107  -26.981 1.00 17.91 ? 135 LYS D CE  1 
ATOM   7552 N  NZ  . LYS D 1 135 ? 1.527   21.901  -28.413 1.00 17.87 ? 135 LYS D NZ  1 
ATOM   7553 N  N   . SER D 1 136 ? 3.380   16.568  -23.633 1.00 14.96 ? 136 SER D N   1 
ATOM   7554 C  CA  . SER D 1 136 ? 3.460   15.417  -22.755 1.00 15.50 ? 136 SER D CA  1 
ATOM   7555 C  C   . SER D 1 136 ? 2.322   14.451  -23.047 1.00 14.03 ? 136 SER D C   1 
ATOM   7556 O  O   . SER D 1 136 ? 1.167   14.848  -23.187 1.00 12.97 ? 136 SER D O   1 
ATOM   7557 C  CB  . SER D 1 136 ? 3.293   15.968  -21.360 1.00 18.53 ? 136 SER D CB  1 
ATOM   7558 O  OG  . SER D 1 136 ? 3.468   14.895  -20.423 1.00 22.42 ? 136 SER D OG  1 
ATOM   7559 N  N   . GLU D 1 137 ? 2.656   13.137  -23.118 1.00 13.56 ? 137 GLU D N   1 
ATOM   7560 C  CA  . GLU D 1 137 ? 1.660   12.106  -23.335 1.00 14.02 ? 137 GLU D CA  1 
ATOM   7561 C  C   . GLU D 1 137 ? 0.903   12.270  -24.663 1.00 13.24 ? 137 GLU D C   1 
ATOM   7562 O  O   . GLU D 1 137 ? -0.222  11.848  -24.804 1.00 14.01 ? 137 GLU D O   1 
ATOM   7563 C  CB  . GLU D 1 137 ? 0.693   11.975  -22.137 1.00 16.14 ? 137 GLU D CB  1 
ATOM   7564 C  CG  . GLU D 1 137 ? 1.390   11.878  -20.781 1.00 19.78 ? 137 GLU D CG  1 
ATOM   7565 C  CD  . GLU D 1 137 ? 2.068   10.553  -20.447 1.00 25.60 ? 137 GLU D CD  1 
ATOM   7566 O  OE1 . GLU D 1 137 ? 2.002   9.608   -21.265 1.00 29.56 ? 137 GLU D OE1 1 
ATOM   7567 O  OE2 . GLU D 1 137 ? 2.631   10.446  -19.345 1.00 36.20 ? 137 GLU D OE2 1 
ATOM   7568 N  N   . GLY D 1 138 ? 1.510   12.968  -25.631 1.00 13.24 ? 138 GLY D N   1 
ATOM   7569 C  CA  . GLY D 1 138 ? 0.702   13.395  -26.754 1.00 12.33 ? 138 GLY D CA  1 
ATOM   7570 C  C   . GLY D 1 138 ? 0.303   12.289  -27.742 1.00 11.17 ? 138 GLY D C   1 
ATOM   7571 O  O   . GLY D 1 138 ? -0.748  12.358  -28.339 1.00 10.93 ? 138 GLY D O   1 
ATOM   7572 N  N   . LEU D 1 139 ? 1.153   11.246  -27.925 1.00 10.64 ? 139 LEU D N   1 
ATOM   7573 C  CA  . LEU D 1 139 ? 0.915   10.302  -29.050 1.00 9.84  ? 139 LEU D CA  1 
ATOM   7574 C  C   . LEU D 1 139 ? 1.052   8.860   -28.566 1.00 10.38 ? 139 LEU D C   1 
ATOM   7575 O  O   . LEU D 1 139 ? 1.789   8.575   -27.604 1.00 10.38 ? 139 LEU D O   1 
ATOM   7576 C  CB  . LEU D 1 139 ? 1.942   10.526  -30.186 1.00 10.53 ? 139 LEU D CB  1 
ATOM   7577 C  CG  . LEU D 1 139 ? 1.949   11.913  -30.827 1.00 9.80  ? 139 LEU D CG  1 
ATOM   7578 C  CD1 . LEU D 1 139 ? 3.121   12.093  -31.776 1.00 12.45 ? 139 LEU D CD1 1 
ATOM   7579 C  CD2 . LEU D 1 139 ? 0.622   12.183  -31.546 1.00 12.46 ? 139 LEU D CD2 1 
ATOM   7580 N  N   . ALA D 1 140 ? 0.373   7.968   -29.298 1.00 9.87  ? 140 ALA D N   1 
ATOM   7581 C  CA  . ALA D 1 140 ? 0.556   6.546   -29.054 1.00 8.96  ? 140 ALA D CA  1 
ATOM   7582 C  C   . ALA D 1 140 ? 0.569   5.924   -30.445 1.00 9.41  ? 140 ALA D C   1 
ATOM   7583 O  O   . ALA D 1 140 ? -0.294  6.210   -31.283 1.00 10.59 ? 140 ALA D O   1 
ATOM   7584 C  CB  . ALA D 1 140 ? -0.554  5.966   -28.212 1.00 11.10 ? 140 ALA D CB  1 
ATOM   7585 N  N   . VAL D 1 141 ? 1.555   5.070   -30.680 1.00 8.97  ? 141 VAL D N   1 
ATOM   7586 C  CA  . VAL D 1 141 ? 1.662   4.396   -31.974 1.00 9.18  ? 141 VAL D CA  1 
ATOM   7587 C  C   . VAL D 1 141 ? 1.529   2.883   -31.803 1.00 8.46  ? 141 VAL D C   1 
ATOM   7588 O  O   . VAL D 1 141 ? 2.090   2.325   -30.868 1.00 9.37  ? 141 VAL D O   1 
ATOM   7589 C  CB  . VAL D 1 141 ? 2.984   4.772   -32.649 1.00 8.32  ? 141 VAL D CB  1 
ATOM   7590 C  CG1 . VAL D 1 141 ? 3.087   4.056   -34.027 1.00 8.95  ? 141 VAL D CG1 1 
ATOM   7591 C  CG2 . VAL D 1 141 ? 3.054   6.284   -32.885 1.00 9.45  ? 141 VAL D CG2 1 
ATOM   7592 N  N   . LEU D 1 142 ? 0.807   2.252   -32.703 1.00 7.76  ? 142 LEU D N   1 
ATOM   7593 C  CA  . LEU D 1 142 ? 0.797   0.802   -32.794 1.00 8.38  ? 142 LEU D CA  1 
ATOM   7594 C  C   . LEU D 1 142 ? 1.741   0.437   -33.925 1.00 8.01  ? 142 LEU D C   1 
ATOM   7595 O  O   . LEU D 1 142 ? 1.590   0.953   -35.049 1.00 9.13  ? 142 LEU D O   1 
ATOM   7596 C  CB  . LEU D 1 142 ? -0.608  0.313   -33.127 1.00 9.12  ? 142 LEU D CB  1 
ATOM   7597 C  CG  . LEU D 1 142 ? -1.737  0.664   -32.152 1.00 9.86  ? 142 LEU D CG  1 
ATOM   7598 C  CD1 . LEU D 1 142 ? -3.024  0.018   -32.595 1.00 11.85 ? 142 LEU D CD1 1 
ATOM   7599 C  CD2 . LEU D 1 142 ? -1.410  0.275   -30.701 1.00 10.69 ? 142 LEU D CD2 1 
ATOM   7600 N  N   . ALA D 1 143 ? 2.700   -0.438  -33.635 1.00 8.30  ? 143 ALA D N   1 
ATOM   7601 C  CA  . ALA D 1 143 ? 3.667   -0.867  -34.661 1.00 7.66  ? 143 ALA D CA  1 
ATOM   7602 C  C   . ALA D 1 143 ? 3.473   -2.340  -34.987 1.00 7.77  ? 143 ALA D C   1 
ATOM   7603 O  O   . ALA D 1 143 ? 3.418   -3.193  -34.068 1.00 8.44  ? 143 ALA D O   1 
ATOM   7604 C  CB  . ALA D 1 143 ? 5.064   -0.625  -34.118 1.00 8.99  ? 143 ALA D CB  1 
ATOM   7605 N  N   . VAL D 1 144 ? 3.342   -2.628  -36.283 1.00 7.21  ? 144 VAL D N   1 
ATOM   7606 C  CA  . VAL D 1 144 ? 3.219   -4.017  -36.744 1.00 7.55  ? 144 VAL D CA  1 
ATOM   7607 C  C   . VAL D 1 144 ? 4.455   -4.309  -37.585 1.00 7.72  ? 144 VAL D C   1 
ATOM   7608 O  O   . VAL D 1 144 ? 4.729   -3.635  -38.589 1.00 7.87  ? 144 VAL D O   1 
ATOM   7609 C  CB  . VAL D 1 144 ? 1.981   -4.182  -37.616 1.00 7.73  ? 144 VAL D CB  1 
ATOM   7610 C  CG1 . VAL D 1 144 ? 1.829   -5.632  -38.052 1.00 9.23  ? 144 VAL D CG1 1 
ATOM   7611 C  CG2 . VAL D 1 144 ? 0.738   -3.731  -36.849 1.00 8.98  ? 144 VAL D CG2 1 
ATOM   7612 N  N   . LEU D 1 145 ? 5.218   -5.328  -37.170 1.00 7.47  ? 145 LEU D N   1 
ATOM   7613 C  CA  . LEU D 1 145 ? 6.364   -5.813  -37.930 1.00 7.72  ? 145 LEU D CA  1 
ATOM   7614 C  C   . LEU D 1 145 ? 5.879   -6.626  -39.113 1.00 7.37  ? 145 LEU D C   1 
ATOM   7615 O  O   . LEU D 1 145 ? 4.931   -7.396  -38.966 1.00 8.15  ? 145 LEU D O   1 
ATOM   7616 C  CB  . LEU D 1 145 ? 7.226   -6.677  -37.025 1.00 9.01  ? 145 LEU D CB  1 
ATOM   7617 C  CG  . LEU D 1 145 ? 7.758   -5.913  -35.806 1.00 10.88 ? 145 LEU D CG  1 
ATOM   7618 C  CD1 . LEU D 1 145 ? 8.243   -6.869  -34.720 1.00 13.02 ? 145 LEU D CD1 1 
ATOM   7619 C  CD2 . LEU D 1 145 ? 8.877   -4.953  -36.216 1.00 14.60 ? 145 LEU D CD2 1 
ATOM   7620 N  N   . ILE D 1 146 ? 6.482   -6.414  -40.277 1.00 7.47  ? 146 ILE D N   1 
ATOM   7621 C  CA  . ILE D 1 146 ? 6.034   -7.048  -41.509 1.00 8.14  ? 146 ILE D CA  1 
ATOM   7622 C  C   . ILE D 1 146 ? 7.158   -7.910  -42.059 1.00 8.07  ? 146 ILE D C   1 
ATOM   7623 O  O   . ILE D 1 146 ? 8.264   -7.441  -42.286 1.00 8.50  ? 146 ILE D O   1 
ATOM   7624 C  CB  . ILE D 1 146 ? 5.628   -5.992  -42.551 1.00 7.92  ? 146 ILE D CB  1 
ATOM   7625 C  CG1 . ILE D 1 146 ? 4.500   -5.094  -42.018 1.00 9.06  ? 146 ILE D CG1 1 
ATOM   7626 C  CG2 . ILE D 1 146 ? 5.239   -6.675  -43.875 1.00 8.73  ? 146 ILE D CG2 1 
ATOM   7627 C  CD1 . ILE D 1 146 ? 4.165   -3.894  -42.933 1.00 8.74  ? 146 ILE D CD1 1 
ATOM   7628 N  N   A GLU D 1 147 ? 6.913   -9.227  -42.185 0.50 9.08  ? 147 GLU D N   1 
ATOM   7629 N  N   B GLU D 1 147 ? 6.813   -9.175  -42.329 0.50 8.90  ? 147 GLU D N   1 
ATOM   7630 C  CA  A GLU D 1 147 ? 7.892   -10.153 -42.748 0.50 10.32 ? 147 GLU D CA  1 
ATOM   7631 C  CA  B GLU D 1 147 ? 7.733   -10.194 -42.809 0.50 9.96  ? 147 GLU D CA  1 
ATOM   7632 C  C   A GLU D 1 147 ? 7.453   -10.542 -44.163 0.50 9.15  ? 147 GLU D C   1 
ATOM   7633 C  C   B GLU D 1 147 ? 7.411   -10.462 -44.276 0.50 8.84  ? 147 GLU D C   1 
ATOM   7634 O  O   A GLU D 1 147 ? 6.252   -10.620 -44.445 0.50 9.28  ? 147 GLU D O   1 
ATOM   7635 O  O   B GLU D 1 147 ? 6.267   -10.398 -44.726 0.50 8.64  ? 147 GLU D O   1 
ATOM   7636 C  CB  A GLU D 1 147 ? 8.040   -11.384 -41.831 0.50 12.03 ? 147 GLU D CB  1 
ATOM   7637 C  CB  B GLU D 1 147 ? 7.526   -11.500 -42.019 0.50 10.54 ? 147 GLU D CB  1 
ATOM   7638 C  CG  A GLU D 1 147 ? 6.991   -12.482 -42.006 0.50 15.49 ? 147 GLU D CG  1 
ATOM   7639 C  CG  B GLU D 1 147 ? 8.579   -12.570 -42.297 0.50 13.57 ? 147 GLU D CG  1 
ATOM   7640 C  CD  A GLU D 1 147 ? 6.980   -13.575 -40.910 0.50 16.15 ? 147 GLU D CD  1 
ATOM   7641 C  CD  B GLU D 1 147 ? 8.811   -13.567 -41.155 0.50 16.58 ? 147 GLU D CD  1 
ATOM   7642 O  OE1 A GLU D 1 147 ? 7.896   -13.585 -40.087 0.50 16.75 ? 147 GLU D OE1 1 
ATOM   7643 O  OE1 B GLU D 1 147 ? 8.592   -13.208 -39.974 0.50 19.08 ? 147 GLU D OE1 1 
ATOM   7644 O  OE2 A GLU D 1 147 ? 5.991   -14.385 -40.810 0.50 19.44 ? 147 GLU D OE2 1 
ATOM   7645 O  OE2 B GLU D 1 147 ? 9.222   -14.712 -41.446 0.50 20.11 ? 147 GLU D OE2 1 
ATOM   7646 N  N   . MET D 1 148 ? 8.438   -10.803 -45.051 1.00 9.42  ? 148 MET D N   1 
ATOM   7647 C  CA  . MET D 1 148 ? 8.175   -11.335 -46.383 1.00 10.06 ? 148 MET D CA  1 
ATOM   7648 C  C   . MET D 1 148 ? 7.593   -12.731 -46.279 1.00 9.49  ? 148 MET D C   1 
ATOM   7649 O  O   . MET D 1 148 ? 8.174   -13.615 -45.666 1.00 10.23 ? 148 MET D O   1 
ATOM   7650 C  CB  . MET D 1 148 ? 9.496   -11.405 -47.152 1.00 11.25 ? 148 MET D CB  1 
ATOM   7651 C  CG  . MET D 1 148 ? 9.308   -11.780 -48.573 1.00 12.71 ? 148 MET D CG  1 
ATOM   7652 S  SD  . MET D 1 148 ? 10.862  -11.848 -49.531 1.00 14.32 ? 148 MET D SD  1 
ATOM   7653 C  CE  . MET D 1 148 ? 11.375  -10.136 -49.550 1.00 16.13 ? 148 MET D CE  1 
ATOM   7654 N  N   . GLY D 1 149 ? 6.399   -12.901 -46.826 1.00 9.57  ? 149 GLY D N   1 
ATOM   7655 C  CA  . GLY D 1 149 ? 5.715   -14.196 -46.768 1.00 8.74  ? 149 GLY D CA  1 
ATOM   7656 C  C   . GLY D 1 149 ? 4.604   -14.268 -47.819 1.00 8.60  ? 149 GLY D C   1 
ATOM   7657 O  O   . GLY D 1 149 ? 4.828   -14.029 -49.002 1.00 9.62  ? 149 GLY D O   1 
ATOM   7658 N  N   . SER D 1 150 ? 3.410   -14.646 -47.371 1.00 8.87  ? 150 SER D N   1 
ATOM   7659 C  CA  . SER D 1 150 ? 2.241   -14.755 -48.246 1.00 9.49  ? 150 SER D CA  1 
ATOM   7660 C  C   . SER D 1 150 ? 1.642   -13.397 -48.603 1.00 9.32  ? 150 SER D C   1 
ATOM   7661 O  O   . SER D 1 150 ? 1.730   -12.454 -47.833 1.00 10.96 ? 150 SER D O   1 
ATOM   7662 C  CB  . SER D 1 150 ? 1.158   -15.565 -47.533 1.00 9.86  ? 150 SER D CB  1 
ATOM   7663 O  OG  . SER D 1 150 ? 1.602   -16.927 -47.394 1.00 10.28 ? 150 SER D OG  1 
ATOM   7664 N  N   . PHE D 1 151 ? 1.054   -13.347 -49.785 1.00 9.88  ? 151 PHE D N   1 
ATOM   7665 C  CA  . PHE D 1 151 ? 0.279   -12.202 -50.228 1.00 9.84  ? 151 PHE D CA  1 
ATOM   7666 C  C   . PHE D 1 151 ? -0.773  -11.881 -49.186 1.00 10.93 ? 151 PHE D C   1 
ATOM   7667 O  O   . PHE D 1 151 ? -1.442  -12.749 -48.637 1.00 12.80 ? 151 PHE D O   1 
ATOM   7668 C  CB  . PHE D 1 151 ? -0.389  -12.566 -51.549 1.00 10.39 ? 151 PHE D CB  1 
ATOM   7669 C  CG  . PHE D 1 151 ? -1.235  -11.426 -52.098 1.00 10.20 ? 151 PHE D CG  1 
ATOM   7670 C  CD1 . PHE D 1 151 ? -0.640  -10.346 -52.743 1.00 12.13 ? 151 PHE D CD1 1 
ATOM   7671 C  CD2 . PHE D 1 151 ? -2.598  -11.461 -51.922 1.00 11.82 ? 151 PHE D CD2 1 
ATOM   7672 C  CE1 . PHE D 1 151 ? -1.432  -9.283  -53.194 1.00 11.35 ? 151 PHE D CE1 1 
ATOM   7673 C  CE2 . PHE D 1 151 ? -3.382  -10.409 -52.354 1.00 11.74 ? 151 PHE D CE2 1 
ATOM   7674 C  CZ  . PHE D 1 151 ? -2.787  -9.352  -53.001 1.00 11.72 ? 151 PHE D CZ  1 
ATOM   7675 N  N   . ASN D 1 152 ? -0.910  -10.566 -48.928 1.00 9.74  ? 152 ASN D N   1 
ATOM   7676 C  CA  . ASN D 1 152 ? -1.805  -10.113 -47.893 1.00 10.09 ? 152 ASN D CA  1 
ATOM   7677 C  C   . ASN D 1 152 ? -2.866  -9.229  -48.544 1.00 11.13 ? 152 ASN D C   1 
ATOM   7678 O  O   . ASN D 1 152 ? -2.600  -8.094  -48.932 1.00 10.00 ? 152 ASN D O   1 
ATOM   7679 C  CB  . ASN D 1 152 ? -1.016  -9.312  -46.861 1.00 9.15  ? 152 ASN D CB  1 
ATOM   7680 C  CG  . ASN D 1 152 ? -1.816  -9.080  -45.604 1.00 8.98  ? 152 ASN D CG  1 
ATOM   7681 O  OD1 . ASN D 1 152 ? -2.963  -8.555  -45.730 1.00 10.49 ? 152 ASN D OD1 1 
ATOM   7682 N  ND2 . ASN D 1 152 ? -1.281  -9.374  -44.429 1.00 9.32  ? 152 ASN D ND2 1 
ATOM   7683 N  N   A PRO D 1 153 ? -4.087  -9.753  -48.799 0.50 10.77 ? 153 PRO D N   1 
ATOM   7684 N  N   B PRO D 1 153 ? -4.132  -9.696  -48.647 0.50 11.44 ? 153 PRO D N   1 
ATOM   7685 C  CA  A PRO D 1 153 ? -5.166  -8.960  -49.402 0.50 11.25 ? 153 PRO D CA  1 
ATOM   7686 C  CA  B PRO D 1 153 ? -5.110  -8.927  -49.418 0.50 11.91 ? 153 PRO D CA  1 
ATOM   7687 C  C   A PRO D 1 153 ? -5.586  -7.704  -48.639 0.50 11.64 ? 153 PRO D C   1 
ATOM   7688 C  C   B PRO D 1 153 ? -5.470  -7.646  -48.662 0.50 11.87 ? 153 PRO D C   1 
ATOM   7689 O  O   A PRO D 1 153 ? -6.139  -6.780  -49.235 0.50 13.37 ? 153 PRO D O   1 
ATOM   7690 O  O   B PRO D 1 153 ? -5.758  -6.620  -49.296 0.50 12.63 ? 153 PRO D O   1 
ATOM   7691 C  CB  A PRO D 1 153 ? -6.344  -9.948  -49.304 0.50 11.51 ? 153 PRO D CB  1 
ATOM   7692 C  CB  B PRO D 1 153 ? -6.254  -9.939  -49.627 0.50 13.15 ? 153 PRO D CB  1 
ATOM   7693 C  CG  A PRO D 1 153 ? -5.703  -11.309 -49.456 0.50 10.54 ? 153 PRO D CG  1 
ATOM   7694 C  CG  B PRO D 1 153 ? -6.140  -10.929 -48.462 0.50 13.42 ? 153 PRO D CG  1 
ATOM   7695 C  CD  A PRO D 1 153 ? -4.455  -11.169 -48.601 0.50 10.36 ? 153 PRO D CD  1 
ATOM   7696 C  CD  B PRO D 1 153 ? -4.672  -10.946 -48.067 0.50 11.66 ? 153 PRO D CD  1 
ATOM   7697 N  N   . SER D 1 154 ? -5.380  -7.672  -47.331 1.00 10.85 ? 154 SER D N   1 
ATOM   7698 C  CA  . SER D 1 154 ? -5.757  -6.492  -46.559 1.00 11.46 ? 154 SER D CA  1 
ATOM   7699 C  C   . SER D 1 154 ? -4.726  -5.374  -46.804 1.00 12.30 ? 154 SER D C   1 
ATOM   7700 O  O   . SER D 1 154 ? -5.094  -4.214  -47.032 1.00 12.23 ? 154 SER D O   1 
ATOM   7701 C  CB  . SER D 1 154 ? -5.870  -6.821  -45.095 1.00 13.26 ? 154 SER D CB  1 
ATOM   7702 O  OG  . SER D 1 154 ? -6.891  -7.792  -44.849 1.00 16.88 ? 154 SER D OG  1 
ATOM   7703 N  N   . TYR D 1 155 ? -3.406  -5.640  -46.693 1.00 10.50 ? 155 TYR D N   1 
ATOM   7704 C  CA  . TYR D 1 155 ? -2.402  -4.640  -47.055 1.00 10.94 ? 155 TYR D CA  1 
ATOM   7705 C  C   . TYR D 1 155 ? -2.552  -4.177  -48.493 1.00 10.78 ? 155 TYR D C   1 
ATOM   7706 O  O   . TYR D 1 155 ? -2.233  -3.038  -48.838 1.00 10.14 ? 155 TYR D O   1 
ATOM   7707 C  CB  . TYR D 1 155 ? -0.973  -5.084  -46.716 1.00 9.93  ? 155 TYR D CB  1 
ATOM   7708 C  CG  . TYR D 1 155 ? -0.646  -4.953  -45.259 1.00 8.90  ? 155 TYR D CG  1 
ATOM   7709 C  CD1 . TYR D 1 155 ? -1.081  -5.871  -44.310 1.00 8.65  ? 155 TYR D CD1 1 
ATOM   7710 C  CD2 . TYR D 1 155 ? 0.107   -3.853  -44.834 1.00 9.00  ? 155 TYR D CD2 1 
ATOM   7711 C  CE1 . TYR D 1 155 ? -0.800  -5.739  -42.960 1.00 9.16  ? 155 TYR D CE1 1 
ATOM   7712 C  CE2 . TYR D 1 155 ? 0.443   -3.744  -43.502 1.00 9.88  ? 155 TYR D CE2 1 
ATOM   7713 C  CZ  . TYR D 1 155 ? -0.016  -4.659  -42.553 1.00 8.85  ? 155 TYR D CZ  1 
ATOM   7714 O  OH  . TYR D 1 155 ? 0.246   -4.520  -41.228 1.00 10.32 ? 155 TYR D OH  1 
ATOM   7715 N  N   . ASP D 1 156 ? -3.031  -5.073  -49.377 1.00 9.86  ? 156 ASP D N   1 
ATOM   7716 C  CA  . ASP D 1 156 ? -3.140  -4.684  -50.768 1.00 10.52 ? 156 ASP D CA  1 
ATOM   7717 C  C   . ASP D 1 156 ? -4.265  -3.638  -50.978 1.00 9.77  ? 156 ASP D C   1 
ATOM   7718 O  O   . ASP D 1 156 ? -4.227  -2.985  -52.004 1.00 11.59 ? 156 ASP D O   1 
ATOM   7719 C  CB  . ASP D 1 156 ? -3.390  -5.910  -51.701 1.00 11.88 ? 156 ASP D CB  1 
ATOM   7720 C  CG  . ASP D 1 156 ? -2.491  -5.782  -52.926 1.00 14.88 ? 156 ASP D CG  1 
ATOM   7721 O  OD1 . ASP D 1 156 ? -1.204  -5.568  -52.840 1.00 12.80 ? 156 ASP D OD1 1 
ATOM   7722 O  OD2 . ASP D 1 156 ? -3.127  -5.796  -54.045 1.00 16.94 ? 156 ASP D OD2 1 
ATOM   7723 N  N   . LYS D 1 157 ? -5.173  -3.469  -50.008 1.00 11.14 ? 157 LYS D N   1 
ATOM   7724 C  CA  . LYS D 1 157 ? -6.194  -2.409  -50.103 1.00 13.14 ? 157 LYS D CA  1 
ATOM   7725 C  C   . LYS D 1 157 ? -5.486  -1.050  -50.044 1.00 13.55 ? 157 LYS D C   1 
ATOM   7726 O  O   . LYS D 1 157 ? -5.960  -0.120  -50.702 1.00 15.73 ? 157 LYS D O   1 
ATOM   7727 C  CB  . LYS D 1 157 ? -7.228  -2.572  -48.994 1.00 14.25 ? 157 LYS D CB  1 
ATOM   7728 C  CG  . LYS D 1 157 ? -8.068  -3.827  -49.157 1.00 16.21 ? 157 LYS D CG  1 
ATOM   7729 C  CD  . LYS D 1 157 ? -8.987  -4.206  -47.972 1.00 20.03 ? 157 LYS D CD  1 
ATOM   7730 C  CE  . LYS D 1 157 ? -9.758  -5.510  -48.207 1.00 21.87 ? 157 LYS D CE  1 
ATOM   7731 N  NZ  . LYS D 1 157 ? -10.356 -6.091  -46.963 1.00 25.79 ? 157 LYS D NZ  1 
ATOM   7732 N  N   . ILE D 1 158 ? -4.239  -0.971  -49.522 1.00 12.12 ? 158 ILE D N   1 
ATOM   7733 C  CA  . ILE D 1 158 ? -3.428  0.233   -49.551 1.00 12.39 ? 158 ILE D CA  1 
ATOM   7734 C  C   . ILE D 1 158 ? -2.563  0.184   -50.801 1.00 11.00 ? 158 ILE D C   1 
ATOM   7735 O  O   . ILE D 1 158 ? -2.493  1.123   -51.605 1.00 10.74 ? 158 ILE D O   1 
ATOM   7736 C  CB  . ILE D 1 158 ? -2.596  0.370   -48.274 1.00 12.31 ? 158 ILE D CB  1 
ATOM   7737 C  CG1 . ILE D 1 158 ? -3.513  0.574   -47.065 1.00 15.04 ? 158 ILE D CG1 1 
ATOM   7738 C  CG2 . ILE D 1 158 ? -1.596  1.515   -48.442 1.00 13.05 ? 158 ILE D CG2 1 
ATOM   7739 C  CD1 . ILE D 1 158 ? -2.786  0.394   -45.751 1.00 18.72 ? 158 ILE D CD1 1 
ATOM   7740 N  N   . PHE D 1 159 ? -1.850  -0.947  -50.975 1.00 10.90 ? 159 PHE D N   1 
ATOM   7741 C  CA  . PHE D 1 159 ? -0.817  -0.973  -51.977 1.00 11.05 ? 159 PHE D CA  1 
ATOM   7742 C  C   . PHE D 1 159 ? -1.323  -0.831  -53.409 1.00 11.73 ? 159 PHE D C   1 
ATOM   7743 O  O   . PHE D 1 159 ? -0.586  -0.362  -54.262 1.00 12.72 ? 159 PHE D O   1 
ATOM   7744 C  CB  . PHE D 1 159 ? 0.040   -2.244  -51.879 1.00 10.89 ? 159 PHE D CB  1 
ATOM   7745 C  CG  . PHE D 1 159 ? 0.764   -2.488  -50.576 1.00 10.96 ? 159 PHE D CG  1 
ATOM   7746 C  CD1 . PHE D 1 159 ? 1.172   -1.456  -49.745 1.00 13.97 ? 159 PHE D CD1 1 
ATOM   7747 C  CD2 . PHE D 1 159 ? 1.030   -3.803  -50.204 1.00 12.50 ? 159 PHE D CD2 1 
ATOM   7748 C  CE1 . PHE D 1 159 ? 1.826   -1.730  -48.544 1.00 12.84 ? 159 PHE D CE1 1 
ATOM   7749 C  CE2 . PHE D 1 159 ? 1.699   -4.055  -49.006 1.00 12.57 ? 159 PHE D CE2 1 
ATOM   7750 C  CZ  . PHE D 1 159 ? 2.121   -3.029  -48.174 1.00 12.36 ? 159 PHE D CZ  1 
ATOM   7751 N  N   . SER D 1 160 ? -2.578  -1.224  -53.656 1.00 12.05 ? 160 SER D N   1 
ATOM   7752 C  CA  . SER D 1 160 ? -3.103  -1.116  -55.016 1.00 12.86 ? 160 SER D CA  1 
ATOM   7753 C  C   . SER D 1 160 ? -3.237  0.330   -55.477 1.00 12.96 ? 160 SER D C   1 
ATOM   7754 O  O   . SER D 1 160 ? -3.321  0.577   -56.680 1.00 14.89 ? 160 SER D O   1 
ATOM   7755 C  CB  . SER D 1 160 ? -4.437  -1.840  -55.152 1.00 14.22 ? 160 SER D CB  1 
ATOM   7756 O  OG  . SER D 1 160 ? -5.410  -1.212  -54.359 1.00 16.77 ? 160 SER D OG  1 
ATOM   7757 N  N   . HIS D 1 161 ? -3.122  1.288   -54.542 1.00 12.01 ? 161 HIS D N   1 
ATOM   7758 C  CA  . HIS D 1 161 ? -3.233  2.696   -54.872 1.00 13.13 ? 161 HIS D CA  1 
ATOM   7759 C  C   . HIS D 1 161 ? -1.895  3.398   -55.038 1.00 12.68 ? 161 HIS D C   1 
ATOM   7760 O  O   . HIS D 1 161 ? -1.878  4.586   -55.385 1.00 14.07 ? 161 HIS D O   1 
ATOM   7761 C  CB  . HIS D 1 161 ? -4.056  3.440   -53.806 1.00 13.20 ? 161 HIS D CB  1 
ATOM   7762 C  CG  . HIS D 1 161 ? -5.450  2.963   -53.726 1.00 14.43 ? 161 HIS D CG  1 
ATOM   7763 N  ND1 . HIS D 1 161 ? -6.467  3.599   -54.441 1.00 17.38 ? 161 HIS D ND1 1 
ATOM   7764 C  CD2 . HIS D 1 161 ? -6.019  1.980   -53.017 1.00 14.11 ? 161 HIS D CD2 1 
ATOM   7765 C  CE1 . HIS D 1 161 ? -7.598  2.947   -54.227 1.00 16.00 ? 161 HIS D CE1 1 
ATOM   7766 N  NE2 . HIS D 1 161 ? -7.370  1.959   -53.328 1.00 16.32 ? 161 HIS D NE2 1 
ATOM   7767 N  N   . LEU D 1 162 ? -0.765  2.683   -54.875 1.00 13.60 ? 162 LEU D N   1 
ATOM   7768 C  CA  . LEU D 1 162 ? 0.529   3.373   -54.844 1.00 15.29 ? 162 LEU D CA  1 
ATOM   7769 C  C   . LEU D 1 162 ? 0.862   4.088   -56.150 1.00 15.82 ? 162 LEU D C   1 
ATOM   7770 O  O   . LEU D 1 162 ? 1.534   5.139   -56.147 1.00 17.22 ? 162 LEU D O   1 
ATOM   7771 C  CB  . LEU D 1 162 ? 1.666   2.388   -54.535 1.00 16.38 ? 162 LEU D CB  1 
ATOM   7772 C  CG  . LEU D 1 162 ? 1.613   1.674   -53.175 1.00 16.73 ? 162 LEU D CG  1 
ATOM   7773 C  CD1 . LEU D 1 162 ? 2.674   0.566   -53.114 1.00 19.85 ? 162 LEU D CD1 1 
ATOM   7774 C  CD2 . LEU D 1 162 ? 1.846   2.682   -52.056 1.00 21.28 ? 162 LEU D CD2 1 
ATOM   7775 N  N   . GLN D 1 163 ? 0.410   3.548   -57.285 1.00 19.67 ? 163 GLN D N   1 
ATOM   7776 C  CA  . GLN D 1 163 ? 0.761   4.191   -58.539 1.00 19.67 ? 163 GLN D CA  1 
ATOM   7777 C  C   . GLN D 1 163 ? 0.040   5.530   -58.738 1.00 20.33 ? 163 GLN D C   1 
ATOM   7778 O  O   . GLN D 1 163 ? 0.374   6.233   -59.680 1.00 24.69 ? 163 GLN D O   1 
ATOM   7779 C  CB  . GLN D 1 163 ? 0.561   3.298   -59.765 1.00 24.66 ? 163 GLN D CB  1 
ATOM   7780 C  CG  . GLN D 1 163 ? 1.528   2.108   -59.888 1.00 31.53 ? 163 GLN D CG  1 
ATOM   7781 C  CD  . GLN D 1 163 ? 3.015   2.303   -59.639 1.00 32.73 ? 163 GLN D CD  1 
ATOM   7782 O  OE1 . GLN D 1 163 ? 3.654   3.225   -60.155 1.00 37.53 ? 163 GLN D OE1 1 
ATOM   7783 N  NE2 . GLN D 1 163 ? 3.593   1.388   -58.873 1.00 33.26 ? 163 GLN D NE2 1 
ATOM   7784 N  N   . HIS D 1 164 ? -0.858  5.934   -57.847 1.00 17.09 ? 164 HIS D N   1 
ATOM   7785 C  CA  . HIS D 1 164 ? -1.544  7.211   -57.920 1.00 17.38 ? 164 HIS D CA  1 
ATOM   7786 C  C   . HIS D 1 164 ? -0.964  8.253   -56.967 1.00 18.32 ? 164 HIS D C   1 
ATOM   7787 O  O   . HIS D 1 164 ? -1.456  9.377   -56.896 1.00 19.53 ? 164 HIS D O   1 
ATOM   7788 C  CB  . HIS D 1 164 ? -3.041  6.977   -57.689 1.00 20.15 ? 164 HIS D CB  1 
ATOM   7789 C  CG  . HIS D 1 164 ? -3.645  6.074   -58.722 1.00 25.21 ? 164 HIS D CG  1 
ATOM   7790 N  ND1 . HIS D 1 164 ? -3.997  6.521   -59.988 1.00 31.22 ? 164 HIS D ND1 1 
ATOM   7791 C  CD2 . HIS D 1 164 ? -3.959  4.760   -58.695 1.00 31.72 ? 164 HIS D CD2 1 
ATOM   7792 C  CE1 . HIS D 1 164 ? -4.508  5.521   -60.684 1.00 35.23 ? 164 HIS D CE1 1 
ATOM   7793 N  NE2 . HIS D 1 164 ? -4.486  4.426   -59.921 1.00 38.72 ? 164 HIS D NE2 1 
ATOM   7794 N  N   . VAL D 1 165 ? 0.044   7.863   -56.158 1.00 14.90 ? 165 VAL D N   1 
ATOM   7795 C  CA  . VAL D 1 165 ? 0.679   8.775   -55.236 1.00 14.65 ? 165 VAL D CA  1 
ATOM   7796 C  C   . VAL D 1 165 ? 2.203   8.639   -55.406 1.00 13.56 ? 165 VAL D C   1 
ATOM   7797 O  O   . VAL D 1 165 ? 2.963   8.770   -54.442 1.00 13.21 ? 165 VAL D O   1 
ATOM   7798 C  CB  . VAL D 1 165 ? 0.215   8.498   -53.795 1.00 15.39 ? 165 VAL D CB  1 
ATOM   7799 C  CG1 . VAL D 1 165 ? -1.250  8.885   -53.570 1.00 17.02 ? 165 VAL D CG1 1 
ATOM   7800 C  CG2 . VAL D 1 165 ? 0.451   7.036   -53.380 1.00 16.15 ? 165 VAL D CG2 1 
ATOM   7801 N  N   . LYS D 1 166 ? 2.645   8.519   -56.659 1.00 14.57 ? 166 LYS D N   1 
ATOM   7802 C  CA  . LYS D 1 166 ? 4.046   8.271   -56.916 1.00 14.22 ? 166 LYS D CA  1 
ATOM   7803 C  C   . LYS D 1 166 ? 4.936   9.425   -56.426 1.00 13.38 ? 166 LYS D C   1 
ATOM   7804 O  O   . LYS D 1 166 ? 6.054   9.163   -55.991 1.00 13.97 ? 166 LYS D O   1 
ATOM   7805 C  CB  . LYS D 1 166 ? 4.219   8.091   -58.427 1.00 16.50 ? 166 LYS D CB  1 
ATOM   7806 C  CG  . LYS D 1 166 ? 5.626   7.862   -58.922 1.00 22.26 ? 166 LYS D CG  1 
ATOM   7807 C  CD  . LYS D 1 166 ? 5.611   7.502   -60.407 1.00 27.86 ? 166 LYS D CD  1 
ATOM   7808 C  CE  . LYS D 1 166 ? 5.040   6.121   -60.665 1.00 29.30 ? 166 LYS D CE  1 
ATOM   7809 N  NZ  . LYS D 1 166 ? 5.807   5.037   -59.997 1.00 35.27 ? 166 LYS D NZ  1 
ATOM   7810 N  N   . TYR D 1 167 ? 4.495   10.688  -56.518 1.00 14.35 ? 167 TYR D N   1 
ATOM   7811 C  CA  . TYR D 1 167 ? 5.355   11.824  -56.209 1.00 13.42 ? 167 TYR D CA  1 
ATOM   7812 C  C   . TYR D 1 167 ? 4.890   12.614  -55.012 1.00 11.75 ? 167 TYR D C   1 
ATOM   7813 O  O   . TYR D 1 167 ? 3.714   12.588  -54.647 1.00 11.77 ? 167 TYR D O   1 
ATOM   7814 C  CB  . TYR D 1 167 ? 5.459   12.764  -57.413 1.00 15.83 ? 167 TYR D CB  1 
ATOM   7815 C  CG  . TYR D 1 167 ? 6.153   12.082  -58.553 1.00 17.84 ? 167 TYR D CG  1 
ATOM   7816 C  CD1 . TYR D 1 167 ? 7.537   11.937  -58.545 1.00 19.69 ? 167 TYR D CD1 1 
ATOM   7817 C  CD2 . TYR D 1 167 ? 5.405   11.581  -59.588 1.00 18.85 ? 167 TYR D CD2 1 
ATOM   7818 C  CE1 . TYR D 1 167 ? 8.167   11.277  -59.588 1.00 21.43 ? 167 TYR D CE1 1 
ATOM   7819 C  CE2 . TYR D 1 167 ? 6.025   10.933  -60.654 1.00 22.79 ? 167 TYR D CE2 1 
ATOM   7820 C  CZ  . TYR D 1 167 ? 7.403   10.782  -60.632 1.00 22.21 ? 167 TYR D CZ  1 
ATOM   7821 O  OH  . TYR D 1 167 ? 8.041   10.149  -61.672 1.00 29.29 ? 167 TYR D OH  1 
ATOM   7822 N  N   . LYS D 1 168 ? 5.866   13.309  -54.410 1.00 12.80 ? 168 LYS D N   1 
ATOM   7823 C  CA  . LYS D 1 168 ? 5.578   14.063  -53.209 1.00 14.68 ? 168 LYS D CA  1 
ATOM   7824 C  C   . LYS D 1 168 ? 4.411   15.004  -53.463 1.00 13.97 ? 168 LYS D C   1 
ATOM   7825 O  O   . LYS D 1 168 ? 4.378   15.718  -54.470 1.00 15.04 ? 168 LYS D O   1 
ATOM   7826 C  CB  . LYS D 1 168 ? 6.763   14.952  -52.835 1.00 14.86 ? 168 LYS D CB  1 
ATOM   7827 C  CG  . LYS D 1 168 ? 6.577   15.690  -51.522 1.00 17.41 ? 168 LYS D CG  1 
ATOM   7828 C  CD  . LYS D 1 168 ? 7.871   16.284  -51.059 1.00 18.63 ? 168 LYS D CD  1 
ATOM   7829 C  CE  . LYS D 1 168 ? 7.692   17.112  -49.805 1.00 22.12 ? 168 LYS D CE  1 
ATOM   7830 N  NZ  . LYS D 1 168 ? 8.988   17.385  -49.138 1.00 27.46 ? 168 LYS D NZ  1 
ATOM   7831 N  N   . GLY D 1 169 ? 3.440   15.000  -52.549 1.00 14.88 ? 169 GLY D N   1 
ATOM   7832 C  CA  . GLY D 1 169 ? 2.290   15.889  -52.595 1.00 16.65 ? 169 GLY D CA  1 
ATOM   7833 C  C   . GLY D 1 169 ? 1.064   15.273  -53.270 1.00 17.70 ? 169 GLY D C   1 
ATOM   7834 O  O   . GLY D 1 169 ? -0.046  15.791  -53.149 1.00 20.38 ? 169 GLY D O   1 
ATOM   7835 N  N   . GLN D 1 170 ? 1.218   14.167  -53.988 1.00 14.73 ? 170 GLN D N   1 
ATOM   7836 C  CA  . GLN D 1 170 ? 0.118   13.508  -54.671 1.00 15.01 ? 170 GLN D CA  1 
ATOM   7837 C  C   . GLN D 1 170 ? -0.776  12.750  -53.688 1.00 16.64 ? 170 GLN D C   1 
ATOM   7838 O  O   . GLN D 1 170 ? -0.315  12.268  -52.637 1.00 14.59 ? 170 GLN D O   1 
ATOM   7839 C  CB  . GLN D 1 170 ? 0.669   12.598  -55.751 1.00 14.60 ? 170 GLN D CB  1 
ATOM   7840 C  CG  . GLN D 1 170 ? 1.303   13.446  -56.864 1.00 15.52 ? 170 GLN D CG  1 
ATOM   7841 C  CD  . GLN D 1 170 ? 1.681   12.597  -58.042 1.00 17.82 ? 170 GLN D CD  1 
ATOM   7842 O  OE1 . GLN D 1 170 ? 1.976   11.417  -57.942 1.00 18.24 ? 170 GLN D OE1 1 
ATOM   7843 N  NE2 . GLN D 1 170 ? 1.677   13.207  -59.231 1.00 20.00 ? 170 GLN D NE2 1 
ATOM   7844 N  N   . GLU D 1 171 ? -2.074  12.722  -54.033 1.00 17.71 ? 171 GLU D N   1 
ATOM   7845 C  CA  . GLU D 1 171 ? -3.101  12.152  -53.174 1.00 17.75 ? 171 GLU D CA  1 
ATOM   7846 C  C   . GLU D 1 171 ? -4.050  11.277  -53.980 1.00 18.87 ? 171 GLU D C   1 
ATOM   7847 O  O   . GLU D 1 171 ? -4.202  11.409  -55.208 1.00 20.06 ? 171 GLU D O   1 
ATOM   7848 C  CB  . GLU D 1 171 ? -3.930  13.262  -52.547 1.00 21.53 ? 171 GLU D CB  1 
ATOM   7849 C  CG  . GLU D 1 171 ? -3.199  14.233  -51.644 1.00 24.89 ? 171 GLU D CG  1 
ATOM   7850 C  CD  . GLU D 1 171 ? -4.116  15.405  -51.333 1.00 31.28 ? 171 GLU D CD  1 
ATOM   7851 O  OE1 . GLU D 1 171 ? -5.125  15.548  -52.059 1.00 36.75 ? 171 GLU D OE1 1 
ATOM   7852 O  OE2 . GLU D 1 171 ? -3.830  16.155  -50.376 1.00 35.70 ? 171 GLU D OE2 1 
ATOM   7853 N  N   . ALA D 1 172 ? -4.693  10.355  -53.269 1.00 17.05 ? 172 ALA D N   1 
ATOM   7854 C  CA  . ALA D 1 172 ? -5.616  9.409   -53.878 1.00 16.29 ? 172 ALA D CA  1 
ATOM   7855 C  C   . ALA D 1 172 ? -6.589  8.997   -52.783 1.00 16.07 ? 172 ALA D C   1 
ATOM   7856 O  O   . ALA D 1 172 ? -6.227  9.002   -51.624 1.00 17.32 ? 172 ALA D O   1 
ATOM   7857 C  CB  . ALA D 1 172 ? -4.886  8.229   -54.434 1.00 18.35 ? 172 ALA D CB  1 
ATOM   7858 N  N   . PHE D 1 173 ? -7.794  8.568   -53.148 1.00 16.54 ? 173 PHE D N   1 
ATOM   7859 C  CA  . PHE D 1 173 ? -8.760  8.117   -52.142 1.00 14.55 ? 173 PHE D CA  1 
ATOM   7860 C  C   . PHE D 1 173 ? -8.773  6.593   -52.101 1.00 14.07 ? 173 PHE D C   1 
ATOM   7861 O  O   . PHE D 1 173 ? -8.721  5.935   -53.157 1.00 17.95 ? 173 PHE D O   1 
ATOM   7862 C  CB  . PHE D 1 173 ? -10.163 8.647   -52.464 1.00 16.93 ? 173 PHE D CB  1 
ATOM   7863 C  CG  . PHE D 1 173 ? -10.376 10.042  -51.937 1.00 17.90 ? 173 PHE D CG  1 
ATOM   7864 C  CD1 . PHE D 1 173 ? -10.349 10.309  -50.571 1.00 21.60 ? 173 PHE D CD1 1 
ATOM   7865 C  CD2 . PHE D 1 173 ? -10.637 11.090  -52.807 1.00 25.85 ? 173 PHE D CD2 1 
ATOM   7866 C  CE1 . PHE D 1 173 ? -10.555 11.591  -50.071 1.00 25.58 ? 173 PHE D CE1 1 
ATOM   7867 C  CE2 . PHE D 1 173 ? -10.844 12.370  -52.310 1.00 26.69 ? 173 PHE D CE2 1 
ATOM   7868 C  CZ  . PHE D 1 173 ? -10.796 12.626  -50.952 1.00 28.36 ? 173 PHE D CZ  1 
ATOM   7869 N  N   . VAL D 1 174 ? -8.819  6.065   -50.877 1.00 12.75 ? 174 VAL D N   1 
ATOM   7870 C  CA  . VAL D 1 174 ? -8.878  4.642   -50.596 1.00 12.47 ? 174 VAL D CA  1 
ATOM   7871 C  C   . VAL D 1 174 ? -10.246 4.390   -49.970 1.00 13.05 ? 174 VAL D C   1 
ATOM   7872 O  O   . VAL D 1 174 ? -10.577 4.965   -48.924 1.00 13.72 ? 174 VAL D O   1 
ATOM   7873 C  CB  . VAL D 1 174 ? -7.751  4.221   -49.627 1.00 11.83 ? 174 VAL D CB  1 
ATOM   7874 C  CG1 . VAL D 1 174 ? -7.782  2.724   -49.332 1.00 15.62 ? 174 VAL D CG1 1 
ATOM   7875 C  CG2 . VAL D 1 174 ? -6.384  4.598   -50.250 1.00 14.44 ? 174 VAL D CG2 1 
ATOM   7876 N  N   . PRO D 1 175 ? -11.059 3.453   -50.509 1.00 12.89 ? 175 PRO D N   1 
ATOM   7877 C  CA  . PRO D 1 175 ? -12.300 3.067   -49.828 1.00 12.33 ? 175 PRO D CA  1 
ATOM   7878 C  C   . PRO D 1 175 ? -12.000 2.487   -48.454 1.00 13.17 ? 175 PRO D C   1 
ATOM   7879 O  O   . PRO D 1 175 ? -10.985 1.833   -48.218 1.00 13.05 ? 175 PRO D O   1 
ATOM   7880 C  CB  . PRO D 1 175 ? -12.894 1.990   -50.765 1.00 14.20 ? 175 PRO D CB  1 
ATOM   7881 C  CG  . PRO D 1 175 ? -12.232 2.223   -52.107 1.00 16.47 ? 175 PRO D CG  1 
ATOM   7882 C  CD  . PRO D 1 175 ? -10.829 2.695   -51.747 1.00 13.89 ? 175 PRO D CD  1 
ATOM   7883 N  N   . GLY D 1 176 ? -12.872 2.725   -47.474 1.00 13.19 ? 176 GLY D N   1 
ATOM   7884 C  CA  . GLY D 1 176 ? -12.662 2.189   -46.147 1.00 11.83 ? 176 GLY D CA  1 
ATOM   7885 C  C   . GLY D 1 176 ? -12.607 0.656   -46.164 1.00 12.13 ? 176 GLY D C   1 
ATOM   7886 O  O   . GLY D 1 176 ? -13.222 0.006   -47.008 1.00 14.76 ? 176 GLY D O   1 
ATOM   7887 N  N   . PHE D 1 177 ? -11.863 0.160   -45.181 1.00 12.79 ? 177 PHE D N   1 
ATOM   7888 C  CA  . PHE D 1 177 ? -11.792 -1.273  -44.895 1.00 13.11 ? 177 PHE D CA  1 
ATOM   7889 C  C   . PHE D 1 177 ? -11.483 -1.389  -43.418 1.00 13.62 ? 177 PHE D C   1 
ATOM   7890 O  O   . PHE D 1 177 ? -11.270 -0.428  -42.704 1.00 13.07 ? 177 PHE D O   1 
ATOM   7891 C  CB  . PHE D 1 177 ? -10.760 -1.986  -45.773 1.00 13.25 ? 177 PHE D CB  1 
ATOM   7892 C  CG  . PHE D 1 177 ? -9.307  -1.589  -45.566 1.00 13.57 ? 177 PHE D CG  1 
ATOM   7893 C  CD1 . PHE D 1 177 ? -8.789  -0.424  -46.124 1.00 14.47 ? 177 PHE D CD1 1 
ATOM   7894 C  CD2 . PHE D 1 177 ? -8.494  -2.365  -44.736 1.00 15.35 ? 177 PHE D CD2 1 
ATOM   7895 C  CE1 . PHE D 1 177 ? -7.450  -0.098  -45.917 1.00 14.39 ? 177 PHE D CE1 1 
ATOM   7896 C  CE2 . PHE D 1 177 ? -7.154  -2.048  -44.527 1.00 15.35 ? 177 PHE D CE2 1 
ATOM   7897 C  CZ  . PHE D 1 177 ? -6.653  -0.910  -45.109 1.00 15.24 ? 177 PHE D CZ  1 
ATOM   7898 N  N   . ASN D 1 178 ? -11.539 -2.630  -42.915 1.00 14.19 ? 178 ASN D N   1 
ATOM   7899 C  CA  . ASN D 1 178 ? -11.315 -2.884  -41.513 1.00 14.07 ? 178 ASN D CA  1 
ATOM   7900 C  C   . ASN D 1 178 ? -9.805  -2.847  -41.261 1.00 13.45 ? 178 ASN D C   1 
ATOM   7901 O  O   . ASN D 1 178 ? -9.081  -3.789  -41.589 1.00 14.06 ? 178 ASN D O   1 
ATOM   7902 C  CB  . ASN D 1 178 ? -11.898 -4.257  -41.112 1.00 15.21 ? 178 ASN D CB  1 
ATOM   7903 C  CG  . ASN D 1 178 ? -11.735 -4.504  -39.648 1.00 15.24 ? 178 ASN D CG  1 
ATOM   7904 O  OD1 . ASN D 1 178 ? -11.353 -3.644  -38.859 1.00 15.02 ? 178 ASN D OD1 1 
ATOM   7905 N  ND2 . ASN D 1 178 ? -12.086 -5.725  -39.220 1.00 19.98 ? 178 ASN D ND2 1 
ATOM   7906 N  N   . ILE D 1 179 ? -9.369  -1.796  -40.598 1.00 13.05 ? 179 ILE D N   1 
ATOM   7907 C  CA  . ILE D 1 179 ? -7.960  -1.587  -40.284 1.00 12.04 ? 179 ILE D CA  1 
ATOM   7908 C  C   . ILE D 1 179 ? -7.453  -2.639  -39.301 1.00 12.40 ? 179 ILE D C   1 
ATOM   7909 O  O   . ILE D 1 179 ? -6.250  -2.906  -39.261 1.00 11.77 ? 179 ILE D O   1 
ATOM   7910 C  CB  . ILE D 1 179 ? -7.755  -0.153  -39.754 1.00 11.78 ? 179 ILE D CB  1 
ATOM   7911 C  CG1 . ILE D 1 179 ? -8.237  0.917   -40.741 1.00 13.02 ? 179 ILE D CG1 1 
ATOM   7912 C  CG2 . ILE D 1 179 ? -6.293  0.093   -39.364 1.00 11.17 ? 179 ILE D CG2 1 
ATOM   7913 C  CD1 . ILE D 1 179 ? -7.583  0.868   -42.110 1.00 14.21 ? 179 ILE D CD1 1 
ATOM   7914 N  N   . GLU D 1 180 ? -8.329  -3.265  -38.507 1.00 11.72 ? 180 GLU D N   1 
ATOM   7915 C  CA  . GLU D 1 180 ? -7.887  -4.359  -37.664 1.00 13.04 ? 180 GLU D CA  1 
ATOM   7916 C  C   . GLU D 1 180 ? -7.319  -5.513  -38.496 1.00 11.87 ? 180 GLU D C   1 
ATOM   7917 O  O   . GLU D 1 180 ? -6.517  -6.286  -37.942 1.00 13.52 ? 180 GLU D O   1 
ATOM   7918 C  CB  . GLU D 1 180 ? -9.017  -4.860  -36.736 1.00 16.59 ? 180 GLU D CB  1 
ATOM   7919 C  CG  . GLU D 1 180 ? -8.486  -5.560  -35.492 1.00 21.85 ? 180 GLU D CG  1 
ATOM   7920 C  CD  . GLU D 1 180 ? -9.513  -5.718  -34.374 1.00 24.34 ? 180 GLU D CD  1 
ATOM   7921 O  OE1 . GLU D 1 180 ? -10.625 -5.164  -34.483 1.00 26.17 ? 180 GLU D OE1 1 
ATOM   7922 O  OE2 . GLU D 1 180 ? -9.182  -6.388  -33.406 1.00 27.55 ? 180 GLU D OE2 1 
ATOM   7923 N  N   . GLU D 1 181 ? -7.671  -5.619  -39.770 1.00 11.79 ? 181 GLU D N   1 
ATOM   7924 C  CA  . GLU D 1 181 ? -7.106  -6.656  -40.644 1.00 12.50 ? 181 GLU D CA  1 
ATOM   7925 C  C   . GLU D 1 181 ? -5.611  -6.470  -40.875 1.00 12.65 ? 181 GLU D C   1 
ATOM   7926 O  O   . GLU D 1 181 ? -4.971  -7.406  -41.356 1.00 13.36 ? 181 GLU D O   1 
ATOM   7927 C  CB  . GLU D 1 181 ? -7.766  -6.727  -42.014 1.00 14.37 ? 181 GLU D CB  1 
ATOM   7928 C  CG  . GLU D 1 181 ? -9.209  -7.195  -41.980 1.00 17.28 ? 181 GLU D CG  1 
ATOM   7929 C  CD  . GLU D 1 181 ? -9.898  -6.924  -43.318 1.00 21.39 ? 181 GLU D CD  1 
ATOM   7930 O  OE1 . GLU D 1 181 ? -9.238  -6.620  -44.375 1.00 23.43 ? 181 GLU D OE1 1 
ATOM   7931 O  OE2 . GLU D 1 181 ? -11.143 -7.010  -43.353 1.00 22.50 ? 181 GLU D OE2 1 
ATOM   7932 N  N   . LEU D 1 182 ? -5.084  -5.277  -40.581 1.00 11.29 ? 182 LEU D N   1 
ATOM   7933 C  CA  . LEU D 1 182 ? -3.639  -5.060  -40.725 1.00 10.60 ? 182 LEU D CA  1 
ATOM   7934 C  C   . LEU D 1 182 ? -2.870  -5.536  -39.508 1.00 11.54 ? 182 LEU D C   1 
ATOM   7935 O  O   . LEU D 1 182 ? -1.636  -5.532  -39.535 1.00 10.64 ? 182 LEU D O   1 
ATOM   7936 C  CB  . LEU D 1 182 ? -3.403  -3.558  -40.935 1.00 9.98  ? 182 LEU D CB  1 
ATOM   7937 C  CG  . LEU D 1 182 ? -4.114  -2.918  -42.133 1.00 9.69  ? 182 LEU D CG  1 
ATOM   7938 C  CD1 . LEU D 1 182 ? -3.757  -1.435  -42.215 1.00 11.03 ? 182 LEU D CD1 1 
ATOM   7939 C  CD2 . LEU D 1 182 ? -3.799  -3.606  -43.461 1.00 10.62 ? 182 LEU D CD2 1 
ATOM   7940 N  N   . LEU D 1 183 ? -3.528  -5.829  -38.390 1.00 11.27 ? 183 LEU D N   1 
ATOM   7941 C  CA  . LEU D 1 183 ? -2.890  -6.221  -37.161 1.00 11.41 ? 183 LEU D CA  1 
ATOM   7942 C  C   . LEU D 1 183 ? -2.631  -7.720  -37.143 1.00 10.66 ? 183 LEU D C   1 
ATOM   7943 O  O   . LEU D 1 183 ? -3.316  -8.479  -37.830 1.00 12.57 ? 183 LEU D O   1 
ATOM   7944 C  CB  . LEU D 1 183 ? -3.818  -5.847  -35.989 1.00 12.42 ? 183 LEU D CB  1 
ATOM   7945 C  CG  . LEU D 1 183 ? -4.197  -4.365  -35.822 1.00 13.94 ? 183 LEU D CG  1 
ATOM   7946 C  CD1 . LEU D 1 183 ? -4.921  -4.124  -34.491 1.00 15.80 ? 183 LEU D CD1 1 
ATOM   7947 C  CD2 . LEU D 1 183 ? -2.956  -3.504  -35.815 1.00 16.20 ? 183 LEU D CD2 1 
ATOM   7948 N  N   . PRO D 1 184 ? -1.601  -8.145  -36.385 1.00 10.30 ? 184 PRO D N   1 
ATOM   7949 C  CA  . PRO D 1 184 ? -1.244  -9.561  -36.308 1.00 12.24 ? 184 PRO D CA  1 
ATOM   7950 C  C   . PRO D 1 184 ? -2.123  -10.342 -35.353 1.00 14.47 ? 184 PRO D C   1 
ATOM   7951 O  O   . PRO D 1 184 ? -3.049  -9.835  -34.717 1.00 16.18 ? 184 PRO D O   1 
ATOM   7952 C  CB  . PRO D 1 184 ? 0.192   -9.500  -35.760 1.00 12.53 ? 184 PRO D CB  1 
ATOM   7953 C  CG  . PRO D 1 184 ? 0.175   -8.255  -34.857 1.00 10.95 ? 184 PRO D CG  1 
ATOM   7954 C  CD  . PRO D 1 184 ? -0.719  -7.287  -35.588 1.00 10.55 ? 184 PRO D CD  1 
ATOM   7955 N  N   . GLU D 1 185 ? -1.760  -11.630 -35.308 1.00 14.89 ? 185 GLU D N   1 
ATOM   7956 C  CA  . GLU D 1 185 ? -2.407  -12.521 -34.381 1.00 16.50 ? 185 GLU D CA  1 
ATOM   7957 C  C   . GLU D 1 185 ? -1.990  -12.147 -32.961 1.00 15.30 ? 185 GLU D C   1 
ATOM   7958 O  O   . GLU D 1 185 ? -0.869  -11.642 -32.696 1.00 14.47 ? 185 GLU D O   1 
ATOM   7959 C  CB  . GLU D 1 185 ? -1.934  -13.947 -34.655 1.00 21.10 ? 185 GLU D CB  1 
ATOM   7960 C  CG  . GLU D 1 185 ? -2.301  -14.422 -36.041 1.00 25.42 ? 185 GLU D CG  1 
ATOM   7961 C  CD  . GLU D 1 185 ? -3.724  -14.900 -36.254 1.00 38.15 ? 185 GLU D CD  1 
ATOM   7962 O  OE1 . GLU D 1 185 ? -3.887  -16.037 -36.776 1.00 46.46 ? 185 GLU D OE1 1 
ATOM   7963 O  OE2 . GLU D 1 185 ? -4.664  -14.140 -35.930 1.00 44.99 ? 185 GLU D OE2 1 
ATOM   7964 N  N   . ARG D 1 186 ? -2.917  -12.399 -32.032 1.00 14.73 ? 186 ARG D N   1 
ATOM   7965 C  CA  . ARG D 1 186 ? -2.605  -12.312 -30.604 1.00 16.60 ? 186 ARG D CA  1 
ATOM   7966 C  C   . ARG D 1 186 ? -2.112  -10.912 -30.226 1.00 14.76 ? 186 ARG D C   1 
ATOM   7967 O  O   . ARG D 1 186 ? -1.053  -10.729 -29.635 1.00 13.73 ? 186 ARG D O   1 
ATOM   7968 C  CB  . ARG D 1 186 ? -1.683  -13.420 -30.090 1.00 18.57 ? 186 ARG D CB  1 
ATOM   7969 C  CG  . ARG D 1 186 ? -2.299  -14.806 -30.210 1.00 23.61 ? 186 ARG D CG  1 
ATOM   7970 C  CD  . ARG D 1 186 ? -1.414  -15.951 -29.740 1.00 27.32 ? 186 ARG D CD  1 
ATOM   7971 N  NE  . ARG D 1 186 ? -0.344  -16.174 -30.702 1.00 29.13 ? 186 ARG D NE  1 
ATOM   7972 C  CZ  . ARG D 1 186 ? -0.491  -16.755 -31.899 1.00 33.37 ? 186 ARG D CZ  1 
ATOM   7973 N  NH1 . ARG D 1 186 ? -1.670  -17.219 -32.287 1.00 33.94 ? 186 ARG D NH1 1 
ATOM   7974 N  NH2 . ARG D 1 186 ? 0.554   -16.875 -32.705 1.00 35.85 ? 186 ARG D NH2 1 
ATOM   7975 N  N   . THR D 1 187 ? -2.954  -9.933  -30.552 1.00 13.67 ? 187 THR D N   1 
ATOM   7976 C  CA  . THR D 1 187 ? -2.620  -8.569  -30.210 1.00 14.73 ? 187 THR D CA  1 
ATOM   7977 C  C   . THR D 1 187 ? -2.440  -8.312  -28.723 1.00 13.79 ? 187 THR D C   1 
ATOM   7978 O  O   . THR D 1 187 ? -1.839  -7.304  -28.356 1.00 14.02 ? 187 THR D O   1 
ATOM   7979 C  CB  . THR D 1 187 ? -3.619  -7.578  -30.817 1.00 12.76 ? 187 THR D CB  1 
ATOM   7980 O  OG1 . THR D 1 187 ? -4.939  -7.941  -30.400 1.00 16.34 ? 187 THR D OG1 1 
ATOM   7981 C  CG2 . THR D 1 187 ? -3.554  -7.608  -32.330 1.00 14.40 ? 187 THR D CG2 1 
ATOM   7982 N  N   . ALA D 1 188 ? -2.930  -9.211  -27.840 1.00 13.14 ? 188 ALA D N   1 
ATOM   7983 C  CA  . ALA D 1 188 ? -2.695  -9.047  -26.406 1.00 12.37 ? 188 ALA D CA  1 
ATOM   7984 C  C   . ALA D 1 188 ? -1.213  -9.194  -26.037 1.00 12.15 ? 188 ALA D C   1 
ATOM   7985 O  O   . ALA D 1 188 ? -0.831  -8.789  -24.956 1.00 13.26 ? 188 ALA D O   1 
ATOM   7986 C  CB  . ALA D 1 188 ? -3.518  -10.099 -25.650 1.00 14.37 ? 188 ALA D CB  1 
ATOM   7987 N  N   . GLU D 1 189 ? -0.406  -9.784  -26.927 1.00 12.07 ? 189 GLU D N   1 
ATOM   7988 C  CA  . GLU D 1 189 ? 1.029   -9.922  -26.699 1.00 10.84 ? 189 GLU D CA  1 
ATOM   7989 C  C   . GLU D 1 189 ? 1.798   -8.816  -27.463 1.00 9.01  ? 189 GLU D C   1 
ATOM   7990 O  O   . GLU D 1 189 ? 1.777   -8.742  -28.705 1.00 10.65 ? 189 GLU D O   1 
ATOM   7991 C  CB  . GLU D 1 189 ? 1.461   -11.284 -27.256 1.00 13.16 ? 189 GLU D CB  1 
ATOM   7992 C  CG  . GLU D 1 189 ? 0.719   -12.431 -26.495 1.00 14.80 ? 189 GLU D CG  1 
ATOM   7993 C  CD  . GLU D 1 189 ? 1.080   -13.814 -27.007 1.00 21.44 ? 189 GLU D CD  1 
ATOM   7994 O  OE1 . GLU D 1 189 ? 2.220   -14.019 -27.391 1.00 21.68 ? 189 GLU D OE1 1 
ATOM   7995 O  OE2 . GLU D 1 189 ? 0.200   -14.717 -26.947 1.00 28.17 ? 189 GLU D OE2 1 
ATOM   7996 N  N   . TYR D 1 190 ? 2.389   -7.973  -26.638 1.00 9.13  ? 190 TYR D N   1 
ATOM   7997 C  CA  . TYR D 1 190 ? 3.043   -6.782  -27.168 1.00 8.99  ? 190 TYR D CA  1 
ATOM   7998 C  C   . TYR D 1 190 ? 4.181   -6.361  -26.280 1.00 9.83  ? 190 TYR D C   1 
ATOM   7999 O  O   . TYR D 1 190 ? 4.263   -6.728  -25.082 1.00 10.46 ? 190 TYR D O   1 
ATOM   8000 C  CB  . TYR D 1 190 ? 2.049   -5.646  -27.426 1.00 10.23 ? 190 TYR D CB  1 
ATOM   8001 C  CG  . TYR D 1 190 ? 1.286   -5.189  -26.189 1.00 9.56  ? 190 TYR D CG  1 
ATOM   8002 C  CD1 . TYR D 1 190 ? 1.851   -4.313  -25.299 1.00 9.82  ? 190 TYR D CD1 1 
ATOM   8003 C  CD2 . TYR D 1 190 ? 0.007   -5.687  -25.955 1.00 10.75 ? 190 TYR D CD2 1 
ATOM   8004 C  CE1 . TYR D 1 190 ? 1.121   -3.872  -24.184 1.00 10.88 ? 190 TYR D CE1 1 
ATOM   8005 C  CE2 . TYR D 1 190 ? -0.709  -5.266  -24.834 1.00 10.25 ? 190 TYR D CE2 1 
ATOM   8006 C  CZ  . TYR D 1 190 ? -0.135  -4.378  -23.950 1.00 11.32 ? 190 TYR D CZ  1 
ATOM   8007 O  OH  . TYR D 1 190 ? -0.836  -3.921  -22.821 1.00 12.15 ? 190 TYR D OH  1 
ATOM   8008 N  N   . TYR D 1 191 ? 5.063   -5.524  -26.862 1.00 9.04  ? 191 TYR D N   1 
ATOM   8009 C  CA  . TYR D 1 191 ? 6.122   -4.772  -26.208 1.00 8.78  ? 191 TYR D CA  1 
ATOM   8010 C  C   . TYR D 1 191 ? 5.620   -3.336  -26.044 1.00 9.22  ? 191 TYR D C   1 
ATOM   8011 O  O   . TYR D 1 191 ? 4.935   -2.798  -26.937 1.00 9.76  ? 191 TYR D O   1 
ATOM   8012 C  CB  . TYR D 1 191 ? 7.353   -4.716  -27.129 1.00 8.88  ? 191 TYR D CB  1 
ATOM   8013 C  CG  . TYR D 1 191 ? 7.920   -6.029  -27.608 1.00 9.64  ? 191 TYR D CG  1 
ATOM   8014 C  CD1 . TYR D 1 191 ? 8.905   -6.705  -26.901 1.00 9.85  ? 191 TYR D CD1 1 
ATOM   8015 C  CD2 . TYR D 1 191 ? 7.508   -6.556  -28.819 1.00 9.62  ? 191 TYR D CD2 1 
ATOM   8016 C  CE1 . TYR D 1 191 ? 9.448   -7.899  -27.363 1.00 9.96  ? 191 TYR D CE1 1 
ATOM   8017 C  CE2 . TYR D 1 191 ? 8.083   -7.704  -29.344 1.00 10.13 ? 191 TYR D CE2 1 
ATOM   8018 C  CZ  . TYR D 1 191 ? 9.044   -8.359  -28.600 1.00 10.45 ? 191 TYR D CZ  1 
ATOM   8019 O  OH  . TYR D 1 191 ? 9.608   -9.504  -29.131 1.00 13.18 ? 191 TYR D OH  1 
ATOM   8020 N  N   . ARG D 1 192 ? 5.949   -2.724  -24.906 1.00 9.62  ? 192 ARG D N   1 
ATOM   8021 C  CA  . ARG D 1 192 ? 5.538   -1.370  -24.599 1.00 9.61  ? 192 ARG D CA  1 
ATOM   8022 C  C   . ARG D 1 192 ? 6.720   -0.595  -24.061 1.00 9.39  ? 192 ARG D C   1 
ATOM   8023 O  O   . ARG D 1 192 ? 7.397   -1.030  -23.146 1.00 10.89 ? 192 ARG D O   1 
ATOM   8024 C  CB  . ARG D 1 192 ? 4.438   -1.434  -23.545 1.00 10.87 ? 192 ARG D CB  1 
ATOM   8025 C  CG  . ARG D 1 192 ? 4.157   -0.133  -22.798 1.00 15.04 ? 192 ARG D CG  1 
ATOM   8026 C  CD  . ARG D 1 192 ? 3.449   0.861   -23.673 1.00 14.04 ? 192 ARG D CD  1 
ATOM   8027 N  NE  . ARG D 1 192 ? 2.299   0.348   -24.392 1.00 14.50 ? 192 ARG D NE  1 
ATOM   8028 C  CZ  . ARG D 1 192 ? 1.113   0.005   -23.896 1.00 14.33 ? 192 ARG D CZ  1 
ATOM   8029 N  NH1 . ARG D 1 192 ? 0.867   0.217   -22.583 1.00 17.30 ? 192 ARG D NH1 1 
ATOM   8030 N  NH2 . ARG D 1 192 ? 0.164   -0.520  -24.658 1.00 15.14 ? 192 ARG D NH2 1 
ATOM   8031 N  N   . TYR D 1 193 ? 6.916   0.636   -24.582 1.00 8.95  ? 193 TYR D N   1 
ATOM   8032 C  CA  . TYR D 1 193 ? 7.966   1.479   -24.038 1.00 9.98  ? 193 TYR D CA  1 
ATOM   8033 C  C   . TYR D 1 193 ? 7.694   2.943   -24.357 1.00 9.21  ? 193 TYR D C   1 
ATOM   8034 O  O   . TYR D 1 193 ? 6.890   3.241   -25.224 1.00 10.22 ? 193 TYR D O   1 
ATOM   8035 C  CB  . TYR D 1 193 ? 9.363   1.039   -24.504 1.00 9.82  ? 193 TYR D CB  1 
ATOM   8036 C  CG  . TYR D 1 193 ? 9.687   1.402   -25.948 1.00 9.07  ? 193 TYR D CG  1 
ATOM   8037 C  CD1 . TYR D 1 193 ? 9.280   0.642   -27.042 1.00 9.38  ? 193 TYR D CD1 1 
ATOM   8038 C  CD2 . TYR D 1 193 ? 10.442  2.538   -26.200 1.00 9.63  ? 193 TYR D CD2 1 
ATOM   8039 C  CE1 . TYR D 1 193 ? 9.564   1.026   -28.346 1.00 9.23  ? 193 TYR D CE1 1 
ATOM   8040 C  CE2 . TYR D 1 193 ? 10.735  2.970   -27.493 1.00 9.43  ? 193 TYR D CE2 1 
ATOM   8041 C  CZ  . TYR D 1 193 ? 10.286  2.195   -28.541 1.00 8.57  ? 193 TYR D CZ  1 
ATOM   8042 O  OH  . TYR D 1 193 ? 10.599  2.612   -29.817 1.00 9.12  ? 193 TYR D OH  1 
ATOM   8043 N  N   . ARG D 1 194 ? 8.451   3.785   -23.661 1.00 10.61 ? 194 ARG D N   1 
ATOM   8044 C  CA  . ARG D 1 194 ? 8.352   5.226   -23.901 1.00 11.62 ? 194 ARG D CA  1 
ATOM   8045 C  C   . ARG D 1 194 ? 9.420   5.662   -24.879 1.00 10.16 ? 194 ARG D C   1 
ATOM   8046 O  O   . ARG D 1 194 ? 10.600  5.434   -24.680 1.00 11.52 ? 194 ARG D O   1 
ATOM   8047 C  CB  . ARG D 1 194 ? 8.625   5.973   -22.595 1.00 14.67 ? 194 ARG D CB  1 
ATOM   8048 C  CG  . ARG D 1 194 ? 7.607   5.662   -21.511 1.00 19.84 ? 194 ARG D CG  1 
ATOM   8049 C  CD  . ARG D 1 194 ? 6.423   6.568   -21.722 1.00 26.12 ? 194 ARG D CD  1 
ATOM   8050 N  NE  . ARG D 1 194 ? 5.493   6.263   -20.651 1.00 36.22 ? 194 ARG D NE  1 
ATOM   8051 C  CZ  . ARG D 1 194 ? 4.336   6.877   -20.474 1.00 39.29 ? 194 ARG D CZ  1 
ATOM   8052 N  NH1 . ARG D 1 194 ? 3.987   7.872   -21.281 1.00 37.09 ? 194 ARG D NH1 1 
ATOM   8053 N  NH2 . ARG D 1 194 ? 3.549   6.493   -19.482 1.00 39.77 ? 194 ARG D NH2 1 
ATOM   8054 N  N   . GLY D 1 195 ? 8.976   6.358   -25.940 1.00 9.75  ? 195 GLY D N   1 
ATOM   8055 C  CA  . GLY D 1 195 ? 9.963   6.835   -26.893 1.00 9.96  ? 195 GLY D CA  1 
ATOM   8056 C  C   . GLY D 1 195 ? 9.489   8.069   -27.644 1.00 10.18 ? 195 GLY D C   1 
ATOM   8057 O  O   . GLY D 1 195 ? 8.834   8.945   -27.107 1.00 10.69 ? 195 GLY D O   1 
ATOM   8058 N  N   . SER D 1 196 ? 9.809   8.077   -28.930 1.00 8.52  ? 196 SER D N   1 
ATOM   8059 C  CA  . SER D 1 196 ? 9.709   9.306   -29.716 1.00 8.69  ? 196 SER D CA  1 
ATOM   8060 C  C   . SER D 1 196 ? 9.118   9.062   -31.091 1.00 8.89  ? 196 SER D C   1 
ATOM   8061 O  O   . SER D 1 196 ? 9.011   7.918   -31.545 1.00 8.70  ? 196 SER D O   1 
ATOM   8062 C  CB  . SER D 1 196 ? 11.074  9.922   -29.875 1.00 9.58  ? 196 SER D CB  1 
ATOM   8063 O  OG  . SER D 1 196 ? 11.900  9.230   -30.860 1.00 9.09  ? 196 SER D OG  1 
ATOM   8064 N  N   . LEU D 1 197 ? 8.836   10.131  -31.818 1.00 9.07  ? 197 LEU D N   1 
ATOM   8065 C  CA  . LEU D 1 197 ? 8.689   10.029  -33.265 1.00 8.71  ? 197 LEU D CA  1 
ATOM   8066 C  C   . LEU D 1 197 ? 10.019  9.525   -33.814 1.00 7.56  ? 197 LEU D C   1 
ATOM   8067 O  O   . LEU D 1 197 ? 11.113  9.912   -33.384 1.00 8.62  ? 197 LEU D O   1 
ATOM   8068 C  CB  . LEU D 1 197 ? 8.445   11.411  -33.908 1.00 8.78  ? 197 LEU D CB  1 
ATOM   8069 C  CG  . LEU D 1 197 ? 7.038   11.968  -33.894 1.00 9.66  ? 197 LEU D CG  1 
ATOM   8070 C  CD1 . LEU D 1 197 ? 6.637   12.460  -32.498 1.00 11.97 ? 197 LEU D CD1 1 
ATOM   8071 C  CD2 . LEU D 1 197 ? 6.926   13.139  -34.926 1.00 10.81 ? 197 LEU D CD2 1 
ATOM   8072 N  N   . THR D 1 198 ? 9.925   8.606   -34.790 1.00 7.70  ? 198 THR D N   1 
ATOM   8073 C  CA  . THR D 1 198 ? 11.132  8.129   -35.474 1.00 7.69  ? 198 THR D CA  1 
ATOM   8074 C  C   . THR D 1 198 ? 11.571  9.009   -36.617 1.00 8.21  ? 198 THR D C   1 
ATOM   8075 O  O   . THR D 1 198 ? 12.556  8.707   -37.284 1.00 8.32  ? 198 THR D O   1 
ATOM   8076 C  CB  . THR D 1 198 ? 10.994  6.685   -35.963 1.00 7.31  ? 198 THR D CB  1 
ATOM   8077 O  OG1 . THR D 1 198 ? 10.055  6.709   -37.013 1.00 7.04  ? 198 THR D OG1 1 
ATOM   8078 C  CG2 . THR D 1 198 ? 10.578  5.687   -34.896 1.00 8.27  ? 198 THR D CG2 1 
ATOM   8079 N  N   . THR D 1 199 ? 10.812  10.072  -36.879 1.00 8.12  ? 199 THR D N   1 
ATOM   8080 C  CA  . THR D 1 199 ? 11.169  11.044  -37.922 1.00 7.38  ? 199 THR D CA  1 
ATOM   8081 C  C   . THR D 1 199 ? 11.242  12.398  -37.230 1.00 8.17  ? 199 THR D C   1 
ATOM   8082 O  O   . THR D 1 199 ? 10.619  12.580  -36.200 1.00 9.31  ? 199 THR D O   1 
ATOM   8083 C  CB  . THR D 1 199 ? 10.045  11.176  -38.977 1.00 7.68  ? 199 THR D CB  1 
ATOM   8084 O  OG1 . THR D 1 199 ? 8.833   11.609  -38.367 1.00 9.90  ? 199 THR D OG1 1 
ATOM   8085 C  CG2 . THR D 1 199 ? 9.721   9.829   -39.598 1.00 8.99  ? 199 THR D CG2 1 
ATOM   8086 N  N   . PRO D 1 200 ? 11.941  13.387  -37.842 1.00 7.46  ? 200 PRO D N   1 
ATOM   8087 C  CA  . PRO D 1 200 ? 11.829  14.764  -37.357 1.00 8.90  ? 200 PRO D CA  1 
ATOM   8088 C  C   . PRO D 1 200 ? 10.375  15.140  -37.164 1.00 10.65 ? 200 PRO D C   1 
ATOM   8089 O  O   . PRO D 1 200 ? 9.551   14.745  -37.983 1.00 11.60 ? 200 PRO D O   1 
ATOM   8090 C  CB  . PRO D 1 200 ? 12.498  15.536  -38.512 1.00 9.22  ? 200 PRO D CB  1 
ATOM   8091 C  CG  . PRO D 1 200 ? 13.594  14.598  -38.986 1.00 8.86  ? 200 PRO D CG  1 
ATOM   8092 C  CD  . PRO D 1 200 ? 12.855  13.251  -38.982 1.00 8.76  ? 200 PRO D CD  1 
ATOM   8093 N  N   . PRO D 1 201 ? 10.046  15.931  -36.124 1.00 10.30 ? 201 PRO D N   1 
ATOM   8094 C  CA  . PRO D 1 201 ? 11.012  16.500  -35.172 1.00 9.99  ? 201 PRO D CA  1 
ATOM   8095 C  C   . PRO D 1 201 ? 11.480  15.636  -34.012 1.00 10.17 ? 201 PRO D C   1 
ATOM   8096 O  O   . PRO D 1 201 ? 12.104  16.116  -33.063 1.00 10.56 ? 201 PRO D O   1 
ATOM   8097 C  CB  . PRO D 1 201 ? 10.274  17.717  -34.563 1.00 11.18 ? 201 PRO D CB  1 
ATOM   8098 C  CG  . PRO D 1 201 ? 9.051   17.882  -35.415 1.00 14.01 ? 201 PRO D CG  1 
ATOM   8099 C  CD  . PRO D 1 201 ? 8.715   16.498  -35.940 1.00 11.71 ? 201 PRO D CD  1 
ATOM   8100 N  N   . CYS D 1 202 ? 11.136  14.339  -34.032 1.00 9.19  ? 202 CYS D N   1 
ATOM   8101 C  CA  . CYS D 1 202 ? 11.677  13.347  -33.078 1.00 9.91  ? 202 CYS D CA  1 
ATOM   8102 C  C   . CYS D 1 202 ? 11.189  13.636  -31.638 1.00 9.78  ? 202 CYS D C   1 
ATOM   8103 O  O   . CYS D 1 202 ? 11.858  13.243  -30.674 1.00 9.58  ? 202 CYS D O   1 
ATOM   8104 C  CB  . CYS D 1 202 ? 13.200  13.258  -33.055 1.00 9.65  ? 202 CYS D CB  1 
ATOM   8105 S  SG  . CYS D 1 202 ? 13.950  12.900  -34.657 1.00 9.85  ? 202 CYS D SG  1 
ATOM   8106 N  N   . ASN D 1 203 ? 10.014  14.218  -31.481 1.00 10.47 ? 203 ASN D N   1 
ATOM   8107 C  CA  . ASN D 1 203 ? 9.583   14.600  -30.125 1.00 11.37 ? 203 ASN D CA  1 
ATOM   8108 C  C   . ASN D 1 203 ? 9.476   13.360  -29.265 1.00 12.01 ? 203 ASN D C   1 
ATOM   8109 O  O   . ASN D 1 203 ? 8.952   12.354  -29.721 1.00 10.22 ? 203 ASN D O   1 
ATOM   8110 C  CB  . ASN D 1 203 ? 8.246   15.301  -30.163 1.00 12.18 ? 203 ASN D CB  1 
ATOM   8111 C  CG  . ASN D 1 203 ? 8.303   16.453  -31.133 1.00 14.96 ? 203 ASN D CG  1 
ATOM   8112 O  OD1 . ASN D 1 203 ? 8.182   16.271  -32.333 1.00 17.49 ? 203 ASN D OD1 1 
ATOM   8113 N  ND2 . ASN D 1 203 ? 8.614   17.618  -30.616 1.00 16.98 ? 203 ASN D ND2 1 
ATOM   8114 N  N   . PRO D 1 204 ? 9.937   13.396  -28.000 1.00 10.67 ? 204 PRO D N   1 
ATOM   8115 C  CA  . PRO D 1 204 ? 9.868   12.211  -27.129 1.00 11.88 ? 204 PRO D CA  1 
ATOM   8116 C  C   . PRO D 1 204 ? 8.505   12.111  -26.439 1.00 11.95 ? 204 PRO D C   1 
ATOM   8117 O  O   . PRO D 1 204 ? 8.385   12.173  -25.189 1.00 13.40 ? 204 PRO D O   1 
ATOM   8118 C  CB  . PRO D 1 204 ? 11.011  12.422  -26.103 1.00 13.02 ? 204 PRO D CB  1 
ATOM   8119 C  CG  . PRO D 1 204 ? 11.085  13.933  -26.034 1.00 13.28 ? 204 PRO D CG  1 
ATOM   8120 C  CD  . PRO D 1 204 ? 10.824  14.443  -27.452 1.00 12.03 ? 204 PRO D CD  1 
ATOM   8121 N  N   . THR D 1 205 ? 7.463   11.933  -27.226 1.00 9.61  ? 205 THR D N   1 
ATOM   8122 C  CA  . THR D 1 205 ? 6.083   12.068  -26.792 1.00 10.37 ? 205 THR D CA  1 
ATOM   8123 C  C   . THR D 1 205 ? 5.226   10.858  -27.168 1.00 9.80  ? 205 THR D C   1 
ATOM   8124 O  O   . THR D 1 205 ? 4.005   10.949  -27.181 1.00 10.18 ? 205 THR D O   1 
ATOM   8125 C  CB  . THR D 1 205 ? 5.515   13.348  -27.412 1.00 11.05 ? 205 THR D CB  1 
ATOM   8126 O  OG1 . THR D 1 205 ? 5.642   13.202  -28.847 1.00 11.68 ? 205 THR D OG1 1 
ATOM   8127 C  CG2 . THR D 1 205 ? 6.191   14.629  -26.934 1.00 11.69 ? 205 THR D CG2 1 
ATOM   8128 N  N   . VAL D 1 206 ? 5.907   9.737   -27.524 1.00 10.57 ? 206 VAL D N   1 
ATOM   8129 C  CA  . VAL D 1 206 ? 5.190   8.562   -28.035 1.00 9.89  ? 206 VAL D CA  1 
ATOM   8130 C  C   . VAL D 1 206 ? 5.240   7.386   -27.062 1.00 9.32  ? 206 VAL D C   1 
ATOM   8131 O  O   . VAL D 1 206 ? 6.294   6.985   -26.639 1.00 10.45 ? 206 VAL D O   1 
ATOM   8132 C  CB  . VAL D 1 206 ? 5.753   8.107   -29.405 1.00 9.08  ? 206 VAL D CB  1 
ATOM   8133 C  CG1 . VAL D 1 206 ? 4.998   6.884   -29.907 1.00 11.11 ? 206 VAL D CG1 1 
ATOM   8134 C  CG2 . VAL D 1 206 ? 5.752   9.242   -30.418 1.00 10.62 ? 206 VAL D CG2 1 
ATOM   8135 N  N   . LEU D 1 207 ? 4.031   6.917   -26.761 1.00 9.23  ? 207 LEU D N   1 
ATOM   8136 C  CA  . LEU D 1 207 ? 3.910   5.622   -26.108 1.00 10.25 ? 207 LEU D CA  1 
ATOM   8137 C  C   . LEU D 1 207 ? 3.822   4.561   -27.203 1.00 8.39  ? 207 LEU D C   1 
ATOM   8138 O  O   . LEU D 1 207 ? 2.872   4.526   -27.962 1.00 9.70  ? 207 LEU D O   1 
ATOM   8139 C  CB  . LEU D 1 207 ? 2.646   5.613   -25.253 1.00 14.31 ? 207 LEU D CB  1 
ATOM   8140 C  CG  . LEU D 1 207 ? 2.563   4.393   -24.319 1.00 17.08 ? 207 LEU D CG  1 
ATOM   8141 C  CD1 . LEU D 1 207 ? 3.746   4.371   -23.351 1.00 19.10 ? 207 LEU D CD1 1 
ATOM   8142 C  CD2 . LEU D 1 207 ? 1.275   4.466   -23.531 1.00 23.75 ? 207 LEU D CD2 1 
ATOM   8143 N  N   . TRP D 1 208 ? 4.861   3.731   -27.231 1.00 8.53  ? 208 TRP D N   1 
ATOM   8144 C  CA  . TRP D 1 208 ? 4.986   2.713   -28.275 1.00 8.74  ? 208 TRP D CA  1 
ATOM   8145 C  C   . TRP D 1 208 ? 4.377   1.384   -27.834 1.00 8.67  ? 208 TRP D C   1 
ATOM   8146 O  O   . TRP D 1 208 ? 4.703   0.929   -26.714 1.00 10.55 ? 208 TRP D O   1 
ATOM   8147 C  CB  . TRP D 1 208 ? 6.453   2.483   -28.658 1.00 8.87  ? 208 TRP D CB  1 
ATOM   8148 C  CG  . TRP D 1 208 ? 6.970   3.545   -29.566 1.00 8.16  ? 208 TRP D CG  1 
ATOM   8149 C  CD1 . TRP D 1 208 ? 7.653   4.678   -29.221 1.00 9.46  ? 208 TRP D CD1 1 
ATOM   8150 C  CD2 . TRP D 1 208 ? 6.828   3.559   -30.999 1.00 8.77  ? 208 TRP D CD2 1 
ATOM   8151 N  NE1 . TRP D 1 208 ? 7.893   5.418   -30.345 1.00 9.07  ? 208 TRP D NE1 1 
ATOM   8152 C  CE2 . TRP D 1 208 ? 7.372   4.782   -31.448 1.00 8.69  ? 208 TRP D CE2 1 
ATOM   8153 C  CE3 . TRP D 1 208 ? 6.190   2.730   -31.942 1.00 8.82  ? 208 TRP D CE3 1 
ATOM   8154 C  CZ2 . TRP D 1 208 ? 7.369   5.139   -32.802 1.00 8.84  ? 208 TRP D CZ2 1 
ATOM   8155 C  CZ3 . TRP D 1 208 ? 6.220   3.078   -33.272 1.00 8.75  ? 208 TRP D CZ3 1 
ATOM   8156 C  CH2 . TRP D 1 208 ? 6.778   4.276   -33.698 1.00 9.11  ? 208 TRP D CH2 1 
ATOM   8157 N  N   . THR D 1 209 ? 3.641   0.761   -28.734 1.00 8.76  ? 209 THR D N   1 
ATOM   8158 C  CA  . THR D 1 209 ? 3.148   -0.607  -28.582 1.00 8.44  ? 209 THR D CA  1 
ATOM   8159 C  C   . THR D 1 209 ? 3.585   -1.336  -29.847 1.00 8.52  ? 209 THR D C   1 
ATOM   8160 O  O   . THR D 1 209 ? 3.148   -0.990  -30.939 1.00 9.87  ? 209 THR D O   1 
ATOM   8161 C  CB  . THR D 1 209 ? 1.623   -0.665  -28.465 1.00 8.86  ? 209 THR D CB  1 
ATOM   8162 O  OG1 . THR D 1 209 ? 1.282   0.075   -27.271 1.00 10.01 ? 209 THR D OG1 1 
ATOM   8163 C  CG2 . THR D 1 209 ? 1.147   -2.111  -28.314 1.00 10.27 ? 209 THR D CG2 1 
ATOM   8164 N  N   . VAL D 1 210 ? 4.494   -2.292  -29.712 1.00 8.19  ? 210 VAL D N   1 
ATOM   8165 C  CA  . VAL D 1 210 ? 4.949   -3.094  -30.861 1.00 7.98  ? 210 VAL D CA  1 
ATOM   8166 C  C   . VAL D 1 210 ? 4.391   -4.511  -30.668 1.00 8.01  ? 210 VAL D C   1 
ATOM   8167 O  O   . VAL D 1 210 ? 4.676   -5.130  -29.639 1.00 8.62  ? 210 VAL D O   1 
ATOM   8168 C  CB  . VAL D 1 210 ? 6.491   -3.141  -30.923 1.00 7.79  ? 210 VAL D CB  1 
ATOM   8169 C  CG1 . VAL D 1 210 ? 6.937   -3.934  -32.149 1.00 9.21  ? 210 VAL D CG1 1 
ATOM   8170 C  CG2 . VAL D 1 210 ? 7.160   -1.760  -30.911 1.00 8.47  ? 210 VAL D CG2 1 
ATOM   8171 N  N   . PHE D 1 211 ? 3.559   -4.982  -31.577 1.00 7.80  ? 211 PHE D N   1 
ATOM   8172 C  CA  . PHE D 1 211 ? 2.995   -6.313  -31.387 1.00 8.34  ? 211 PHE D CA  1 
ATOM   8173 C  C   . PHE D 1 211 ? 4.089   -7.373  -31.495 1.00 9.18  ? 211 PHE D C   1 
ATOM   8174 O  O   . PHE D 1 211 ? 5.048   -7.274  -32.273 1.00 9.72  ? 211 PHE D O   1 
ATOM   8175 C  CB  . PHE D 1 211 ? 1.873   -6.559  -32.389 1.00 9.63  ? 211 PHE D CB  1 
ATOM   8176 C  CG  . PHE D 1 211 ? 0.714   -5.638  -32.110 1.00 9.92  ? 211 PHE D CG  1 
ATOM   8177 C  CD1 . PHE D 1 211 ? -0.056  -5.798  -30.950 1.00 11.03 ? 211 PHE D CD1 1 
ATOM   8178 C  CD2 . PHE D 1 211 ? 0.382   -4.593  -32.993 1.00 11.17 ? 211 PHE D CD2 1 
ATOM   8179 C  CE1 . PHE D 1 211 ? -1.085  -4.908  -30.671 1.00 12.21 ? 211 PHE D CE1 1 
ATOM   8180 C  CE2 . PHE D 1 211 ? -0.670  -3.738  -32.725 1.00 11.92 ? 211 PHE D CE2 1 
ATOM   8181 C  CZ  . PHE D 1 211 ? -1.416  -3.902  -31.567 1.00 12.16 ? 211 PHE D CZ  1 
ATOM   8182 N  N   . ARG D 1 212 ? 3.940   -8.440  -30.669 1.00 9.19  ? 212 ARG D N   1 
ATOM   8183 C  CA  . ARG D 1 212 ? 4.929   -9.510  -30.617 1.00 10.57 ? 212 ARG D CA  1 
ATOM   8184 C  C   . ARG D 1 212 ? 5.005   -10.244 -31.955 1.00 10.31 ? 212 ARG D C   1 
ATOM   8185 O  O   . ARG D 1 212 ? 6.110   -10.603 -32.396 1.00 11.17 ? 212 ARG D O   1 
ATOM   8186 C  CB  . ARG D 1 212 ? 4.547   -10.471 -29.489 1.00 11.05 ? 212 ARG D CB  1 
ATOM   8187 C  CG  . ARG D 1 212 ? 5.633   -11.544 -29.335 1.00 11.59 ? 212 ARG D CG  1 
ATOM   8188 C  CD  . ARG D 1 212 ? 5.137   -12.664 -28.463 1.00 14.84 ? 212 ARG D CD  1 
ATOM   8189 N  NE  . ARG D 1 212 ? 6.216   -13.589 -28.147 1.00 15.53 ? 212 ARG D NE  1 
ATOM   8190 C  CZ  . ARG D 1 212 ? 6.098   -14.542 -27.238 1.00 19.42 ? 212 ARG D CZ  1 
ATOM   8191 N  NH1 . ARG D 1 212 ? 4.913   -14.776 -26.719 1.00 19.43 ? 212 ARG D NH1 1 
ATOM   8192 N  NH2 . ARG D 1 212 ? 7.167   -15.251 -26.900 1.00 21.48 ? 212 ARG D NH2 1 
ATOM   8193 N  N   . ASN D 1 213 ? 3.880   -10.462 -32.598 1.00 9.83  ? 213 ASN D N   1 
ATOM   8194 C  CA  . ASN D 1 213 ? 3.814   -11.254 -33.800 1.00 10.74 ? 213 ASN D CA  1 
ATOM   8195 C  C   . ASN D 1 213 ? 3.807   -10.380 -35.051 1.00 11.72 ? 213 ASN D C   1 
ATOM   8196 O  O   . ASN D 1 213 ? 3.069   -9.380  -35.136 1.00 10.77 ? 213 ASN D O   1 
ATOM   8197 C  CB  . ASN D 1 213 ? 2.609   -12.194 -33.772 1.00 12.86 ? 213 ASN D CB  1 
ATOM   8198 C  CG  . ASN D 1 213 ? 2.696   -13.155 -32.604 1.00 16.03 ? 213 ASN D CG  1 
ATOM   8199 O  OD1 . ASN D 1 213 ? 3.728   -13.781 -32.398 1.00 20.38 ? 213 ASN D OD1 1 
ATOM   8200 N  ND2 . ASN D 1 213 ? 1.685   -13.121 -31.768 1.00 18.13 ? 213 ASN D ND2 1 
ATOM   8201 N  N   . PRO D 1 214 ? 4.545   -10.769 -36.095 1.00 9.70  ? 214 PRO D N   1 
ATOM   8202 C  CA  . PRO D 1 214 ? 4.526   -10.051 -37.357 1.00 10.04 ? 214 PRO D CA  1 
ATOM   8203 C  C   . PRO D 1 214 ? 3.336   -10.482 -38.189 1.00 10.34 ? 214 PRO D C   1 
ATOM   8204 O  O   . PRO D 1 214 ? 2.708   -11.508 -37.959 1.00 11.33 ? 214 PRO D O   1 
ATOM   8205 C  CB  . PRO D 1 214 ? 5.834   -10.457 -38.021 1.00 9.89  ? 214 PRO D CB  1 
ATOM   8206 C  CG  . PRO D 1 214 ? 5.982   -11.916 -37.577 1.00 11.52 ? 214 PRO D CG  1 
ATOM   8207 C  CD  . PRO D 1 214 ? 5.547   -11.890 -36.097 1.00 10.27 ? 214 PRO D CD  1 
ATOM   8208 N  N   . VAL D 1 215 ? 3.080   -9.699  -39.223 1.00 9.93  ? 215 VAL D N   1 
ATOM   8209 C  CA  . VAL D 1 215 ? 2.212   -10.096 -40.330 1.00 8.91  ? 215 VAL D CA  1 
ATOM   8210 C  C   . VAL D 1 215 ? 3.096   -10.372 -41.516 1.00 8.27  ? 215 VAL D C   1 
ATOM   8211 O  O   . VAL D 1 215 ? 4.304   -10.134 -41.472 1.00 9.49  ? 215 VAL D O   1 
ATOM   8212 C  CB  . VAL D 1 215 ? 1.182   -9.004  -40.699 1.00 8.50  ? 215 VAL D CB  1 
ATOM   8213 C  CG1 . VAL D 1 215 ? 0.252   -8.708  -39.532 1.00 10.51 ? 215 VAL D CG1 1 
ATOM   8214 C  CG2 . VAL D 1 215 ? 1.878   -7.722  -41.215 1.00 9.55  ? 215 VAL D CG2 1 
ATOM   8215 N  N   . GLN D 1 216 ? 2.521   -10.935 -42.574 1.00 8.37  ? 216 GLN D N   1 
ATOM   8216 C  CA  . GLN D 1 216 ? 3.240   -11.251 -43.794 1.00 8.83  ? 216 GLN D CA  1 
ATOM   8217 C  C   . GLN D 1 216 ? 2.643   -10.476 -44.953 1.00 8.28  ? 216 GLN D C   1 
ATOM   8218 O  O   . GLN D 1 216 ? 1.426   -10.319 -45.035 1.00 9.78  ? 216 GLN D O   1 
ATOM   8219 C  CB  . GLN D 1 216 ? 3.124   -12.731 -44.188 1.00 10.34 ? 216 GLN D CB  1 
ATOM   8220 C  CG  . GLN D 1 216 ? 3.920   -13.617 -43.255 1.00 12.36 ? 216 GLN D CG  1 
ATOM   8221 C  CD  . GLN D 1 216 ? 3.851   -15.080 -43.642 1.00 14.35 ? 216 GLN D CD  1 
ATOM   8222 O  OE1 . GLN D 1 216 ? 3.361   -15.512 -44.686 1.00 13.07 ? 216 GLN D OE1 1 
ATOM   8223 N  NE2 . GLN D 1 216 ? 4.401   -15.875 -42.737 1.00 20.12 ? 216 GLN D NE2 1 
ATOM   8224 N  N   . ILE D 1 217 ? 3.482   -9.969  -45.860 1.00 7.98  ? 217 ILE D N   1 
ATOM   8225 C  CA  . ILE D 1 217 ? 3.094   -9.546  -47.208 1.00 8.33  ? 217 ILE D CA  1 
ATOM   8226 C  C   . ILE D 1 217 ? 4.060   -10.215 -48.200 1.00 8.28  ? 217 ILE D C   1 
ATOM   8227 O  O   . ILE D 1 217 ? 5.160   -10.668 -47.815 1.00 8.87  ? 217 ILE D O   1 
ATOM   8228 C  CB  . ILE D 1 217 ? 3.116   -7.997  -47.377 1.00 8.57  ? 217 ILE D CB  1 
ATOM   8229 C  CG1 . ILE D 1 217 ? 4.548   -7.451  -47.362 1.00 9.12  ? 217 ILE D CG1 1 
ATOM   8230 C  CG2 . ILE D 1 217 ? 2.199   -7.312  -46.368 1.00 9.62  ? 217 ILE D CG2 1 
ATOM   8231 C  CD1 . ILE D 1 217 ? 4.530   -5.926  -47.581 1.00 11.66 ? 217 ILE D CD1 1 
ATOM   8232 N  N   . SER D 1 218 ? 3.657   -10.311 -49.467 1.00 8.13  ? 218 SER D N   1 
ATOM   8233 C  CA  . SER D 1 218 ? 4.519   -11.065 -50.379 1.00 8.54  ? 218 SER D CA  1 
ATOM   8234 C  C   . SER D 1 218 ? 5.713   -10.296 -50.876 1.00 9.48  ? 218 SER D C   1 
ATOM   8235 O  O   . SER D 1 218 ? 5.782   -9.067  -50.774 1.00 9.86  ? 218 SER D O   1 
ATOM   8236 C  CB  . SER D 1 218 ? 3.712   -11.577 -51.539 1.00 9.36  ? 218 SER D CB  1 
ATOM   8237 O  OG  . SER D 1 218 ? 3.318   -10.488 -52.368 1.00 9.97  ? 218 SER D OG  1 
ATOM   8238 N  N   . GLN D 1 219 ? 6.673   -11.007 -51.453 1.00 9.74  ? 219 GLN D N   1 
ATOM   8239 C  CA  . GLN D 1 219 ? 7.751   -10.402 -52.177 1.00 11.38 ? 219 GLN D CA  1 
ATOM   8240 C  C   . GLN D 1 219 ? 7.249   -9.404  -53.220 1.00 10.37 ? 219 GLN D C   1 
ATOM   8241 O  O   . GLN D 1 219 ? 7.862   -8.343  -53.363 1.00 11.41 ? 219 GLN D O   1 
ATOM   8242 C  CB  . GLN D 1 219 ? 8.630   -11.498 -52.781 1.00 14.40 ? 219 GLN D CB  1 
ATOM   8243 C  CG  . GLN D 1 219 ? 9.970   -10.954 -53.278 1.00 19.88 ? 219 GLN D CG  1 
ATOM   8244 C  CD  . GLN D 1 219 ? 9.913   -10.269 -54.612 1.00 22.16 ? 219 GLN D CD  1 
ATOM   8245 O  OE1 . GLN D 1 219 ? 9.053   -10.580 -55.440 1.00 29.03 ? 219 GLN D OE1 1 
ATOM   8246 N  NE2 . GLN D 1 219 ? 10.784  -9.280  -54.773 1.00 26.15 ? 219 GLN D NE2 1 
ATOM   8247 N  N   . GLU D 1 220 ? 6.210   -9.754  -53.954 1.00 10.69 ? 220 GLU D N   1 
ATOM   8248 C  CA  . GLU D 1 220 ? 5.757   -8.880  -55.006 1.00 11.71 ? 220 GLU D CA  1 
ATOM   8249 C  C   . GLU D 1 220 ? 5.137   -7.620  -54.387 1.00 10.00 ? 220 GLU D C   1 
ATOM   8250 O  O   . GLU D 1 220 ? 5.358   -6.530  -54.934 1.00 11.37 ? 220 GLU D O   1 
ATOM   8251 C  CB  . GLU D 1 220 ? 4.732   -9.621  -55.877 1.00 12.89 ? 220 GLU D CB  1 
ATOM   8252 C  CG  . GLU D 1 220 ? 5.384   -10.734 -56.706 1.00 15.48 ? 220 GLU D CG  1 
ATOM   8253 C  CD  . GLU D 1 220 ? 5.645   -12.050 -56.004 1.00 21.57 ? 220 GLU D CD  1 
ATOM   8254 O  OE1 . GLU D 1 220 ? 5.188   -12.241 -54.865 1.00 21.17 ? 220 GLU D OE1 1 
ATOM   8255 O  OE2 . GLU D 1 220 ? 6.247   -12.944 -56.662 1.00 27.95 ? 220 GLU D OE2 1 
ATOM   8256 N  N   . GLN D 1 221 ? 4.439   -7.742  -53.236 1.00 9.36  ? 221 GLN D N   1 
ATOM   8257 C  CA  . GLN D 1 221 ? 3.920   -6.526  -52.607 1.00 9.40  ? 221 GLN D CA  1 
ATOM   8258 C  C   . GLN D 1 221 ? 5.055   -5.657  -52.082 1.00 9.93  ? 221 GLN D C   1 
ATOM   8259 O  O   . GLN D 1 221 ? 5.019   -4.432  -52.219 1.00 10.34 ? 221 GLN D O   1 
ATOM   8260 C  CB  . GLN D 1 221 ? 3.033   -6.936  -51.456 1.00 9.69  ? 221 GLN D CB  1 
ATOM   8261 C  CG  . GLN D 1 221 ? 1.727   -7.548  -51.948 1.00 8.68  ? 221 GLN D CG  1 
ATOM   8262 C  CD  . GLN D 1 221 ? 0.838   -7.947  -50.807 1.00 9.36  ? 221 GLN D CD  1 
ATOM   8263 O  OE1 . GLN D 1 221 ? 1.141   -8.872  -50.006 1.00 8.87  ? 221 GLN D OE1 1 
ATOM   8264 N  NE2 . GLN D 1 221 ? -0.322  -7.303  -50.654 1.00 9.34  ? 221 GLN D NE2 1 
ATOM   8265 N  N   . LEU D 1 222 ? 6.092   -6.270  -51.492 1.00 9.43  ? 222 LEU D N   1 
ATOM   8266 C  CA  . LEU D 1 222 ? 7.224   -5.507  -50.995 1.00 10.16 ? 222 LEU D CA  1 
ATOM   8267 C  C   . LEU D 1 222 ? 7.932   -4.815  -52.152 1.00 9.44  ? 222 LEU D C   1 
ATOM   8268 O  O   . LEU D 1 222 ? 8.301   -3.633  -52.035 1.00 9.74  ? 222 LEU D O   1 
ATOM   8269 C  CB  . LEU D 1 222 ? 8.193   -6.432  -50.267 1.00 11.13 ? 222 LEU D CB  1 
ATOM   8270 C  CG  . LEU D 1 222 ? 7.878   -6.670  -48.818 1.00 11.79 ? 222 LEU D CG  1 
ATOM   8271 C  CD1 . LEU D 1 222 ? 8.580   -7.946  -48.339 1.00 13.37 ? 222 LEU D CD1 1 
ATOM   8272 C  CD2 . LEU D 1 222 ? 8.330   -5.450  -47.948 1.00 13.18 ? 222 LEU D CD2 1 
ATOM   8273 N  N   . LEU D 1 223 ? 8.140   -5.506  -53.275 1.00 9.73  ? 223 LEU D N   1 
ATOM   8274 C  CA  . LEU D 1 223 ? 8.847   -4.917  -54.400 1.00 11.25 ? 223 LEU D CA  1 
ATOM   8275 C  C   . LEU D 1 223 ? 8.031   -3.737  -54.910 1.00 11.76 ? 223 LEU D C   1 
ATOM   8276 O  O   . LEU D 1 223 ? 8.615   -2.713  -55.295 1.00 11.79 ? 223 LEU D O   1 
ATOM   8277 C  CB  . LEU D 1 223 ? 9.091   -5.994  -55.485 1.00 10.98 ? 223 LEU D CB  1 
ATOM   8278 C  CG  . LEU D 1 223 ? 9.762   -5.421  -56.731 1.00 13.53 ? 223 LEU D CG  1 
ATOM   8279 C  CD1 . LEU D 1 223 ? 11.175  -4.991  -56.381 1.00 14.56 ? 223 LEU D CD1 1 
ATOM   8280 C  CD2 . LEU D 1 223 ? 9.847   -6.458  -57.829 1.00 14.43 ? 223 LEU D CD2 1 
ATOM   8281 N  N   . ALA D 1 224 ? 6.711   -3.903  -54.964 1.00 11.43 ? 224 ALA D N   1 
ATOM   8282 C  CA  . ALA D 1 224 ? 5.882   -2.795  -55.420 1.00 12.24 ? 224 ALA D CA  1 
ATOM   8283 C  C   . ALA D 1 224 ? 6.036   -1.601  -54.498 1.00 11.57 ? 224 ALA D C   1 
ATOM   8284 O  O   . ALA D 1 224 ? 6.216   -0.467  -54.941 1.00 13.60 ? 224 ALA D O   1 
ATOM   8285 C  CB  . ALA D 1 224 ? 4.424   -3.203  -55.541 1.00 14.47 ? 224 ALA D CB  1 
ATOM   8286 N  N   . LEU D 1 225 ? 5.967   -1.832  -53.191 1.00 11.35 ? 225 LEU D N   1 
ATOM   8287 C  CA  . LEU D 1 225 ? 6.126   -0.761  -52.230 1.00 11.75 ? 225 LEU D CA  1 
ATOM   8288 C  C   . LEU D 1 225 ? 7.471   -0.073  -52.379 1.00 11.55 ? 225 LEU D C   1 
ATOM   8289 O  O   . LEU D 1 225 ? 7.562   1.151   -52.343 1.00 13.35 ? 225 LEU D O   1 
ATOM   8290 C  CB  . LEU D 1 225 ? 5.908   -1.313  -50.835 1.00 11.49 ? 225 LEU D CB  1 
ATOM   8291 C  CG  . LEU D 1 225 ? 6.100   -0.343  -49.671 1.00 11.45 ? 225 LEU D CG  1 
ATOM   8292 C  CD1 . LEU D 1 225 ? 5.096   0.833   -49.743 1.00 12.60 ? 225 LEU D CD1 1 
ATOM   8293 C  CD2 . LEU D 1 225 ? 5.992   -1.098  -48.350 1.00 11.19 ? 225 LEU D CD2 1 
ATOM   8294 N  N   . GLU D 1 226 ? 8.527   -0.845  -52.581 1.00 10.85 ? 226 GLU D N   1 
ATOM   8295 C  CA  . GLU D 1 226 ? 9.909   -0.388  -52.640 1.00 11.02 ? 226 GLU D CA  1 
ATOM   8296 C  C   . GLU D 1 226 ? 10.232  0.350   -53.936 1.00 12.75 ? 226 GLU D C   1 
ATOM   8297 O  O   . GLU D 1 226 ? 11.258  1.021   -53.980 1.00 15.98 ? 226 GLU D O   1 
ATOM   8298 C  CB  . GLU D 1 226 ? 10.842  -1.614  -52.505 1.00 11.04 ? 226 GLU D CB  1 
ATOM   8299 C  CG  . GLU D 1 226 ? 10.881  -2.213  -51.107 1.00 10.75 ? 226 GLU D CG  1 
ATOM   8300 C  CD  . GLU D 1 226 ? 11.282  -3.670  -51.125 1.00 13.60 ? 226 GLU D CD  1 
ATOM   8301 O  OE1 . GLU D 1 226 ? 11.578  -4.239  -52.216 1.00 12.43 ? 226 GLU D OE1 1 
ATOM   8302 O  OE2 . GLU D 1 226 ? 11.273  -4.255  -50.080 1.00 14.60 ? 226 GLU D OE2 1 
ATOM   8303 N  N   . THR D 1 227 ? 9.409   0.232   -54.969 1.00 11.34 ? 227 THR D N   1 
ATOM   8304 C  CA  . THR D 1 227 ? 9.722   0.800   -56.278 1.00 12.73 ? 227 THR D CA  1 
ATOM   8305 C  C   . THR D 1 227 ? 8.648   1.774   -56.744 1.00 13.91 ? 227 THR D C   1 
ATOM   8306 O  O   . THR D 1 227 ? 8.835   2.355   -57.809 1.00 17.64 ? 227 THR D O   1 
ATOM   8307 C  CB  . THR D 1 227 ? 9.908   -0.290  -57.350 1.00 14.27 ? 227 THR D CB  1 
ATOM   8308 O  OG1 . THR D 1 227 ? 8.712   -1.054  -57.483 1.00 14.70 ? 227 THR D OG1 1 
ATOM   8309 C  CG2 . THR D 1 227 ? 11.119  -1.148  -57.047 1.00 14.48 ? 227 THR D CG2 1 
ATOM   8310 N  N   . ALA D 1 228 ? 7.580   1.956   -55.999 1.00 12.66 ? 228 ALA D N   1 
ATOM   8311 C  CA  . ALA D 1 228 ? 6.485   2.771   -56.505 1.00 15.17 ? 228 ALA D CA  1 
ATOM   8312 C  C   . ALA D 1 228 ? 6.761   4.259   -56.318 1.00 15.66 ? 228 ALA D C   1 
ATOM   8313 O  O   . ALA D 1 228 ? 6.188   5.035   -57.101 1.00 19.20 ? 228 ALA D O   1 
ATOM   8314 C  CB  . ALA D 1 228 ? 5.207   2.402   -55.822 1.00 17.04 ? 228 ALA D CB  1 
ATOM   8315 N  N   . LEU D 1 229 ? 7.462   4.677   -55.276 1.00 13.96 ? 229 LEU D N   1 
ATOM   8316 C  CA  . LEU D 1 229 ? 7.308   6.056   -54.830 1.00 13.55 ? 229 LEU D CA  1 
ATOM   8317 C  C   . LEU D 1 229 ? 8.628   6.812   -54.929 1.00 14.55 ? 229 LEU D C   1 
ATOM   8318 O  O   . LEU D 1 229 ? 9.712   6.257   -54.827 1.00 12.74 ? 229 LEU D O   1 
ATOM   8319 C  CB  . LEU D 1 229 ? 6.820   6.082   -53.382 1.00 15.24 ? 229 LEU D CB  1 
ATOM   8320 C  CG  . LEU D 1 229 ? 5.536   5.285   -53.075 1.00 16.06 ? 229 LEU D CG  1 
ATOM   8321 C  CD1 . LEU D 1 229 ? 5.255   5.318   -51.588 1.00 18.76 ? 229 LEU D CD1 1 
ATOM   8322 C  CD2 . LEU D 1 229 ? 4.335   5.754   -53.897 1.00 17.46 ? 229 LEU D CD2 1 
ATOM   8323 N  N   . TYR D 1 230 ? 8.490   8.149   -55.002 1.00 15.46 ? 230 TYR D N   1 
ATOM   8324 C  CA  . TYR D 1 230 ? 9.608   9.101   -54.963 1.00 16.04 ? 230 TYR D CA  1 
ATOM   8325 C  C   . TYR D 1 230 ? 9.440   10.063  -53.803 1.00 15.22 ? 230 TYR D C   1 
ATOM   8326 O  O   . TYR D 1 230 ? 8.316   10.480  -53.477 1.00 14.96 ? 230 TYR D O   1 
ATOM   8327 C  CB  . TYR D 1 230 ? 9.697   9.899   -56.265 1.00 16.40 ? 230 TYR D CB  1 
ATOM   8328 C  CG  . TYR D 1 230 ? 10.112  9.034   -57.408 1.00 18.48 ? 230 TYR D CG  1 
ATOM   8329 C  CD1 . TYR D 1 230 ? 9.206   8.194   -58.038 1.00 23.53 ? 230 TYR D CD1 1 
ATOM   8330 C  CD2 . TYR D 1 230 ? 11.442  8.978   -57.773 1.00 20.80 ? 230 TYR D CD2 1 
ATOM   8331 C  CE1 . TYR D 1 230 ? 9.602   7.339   -59.051 1.00 27.94 ? 230 TYR D CE1 1 
ATOM   8332 C  CE2 . TYR D 1 230 ? 11.852  8.124   -58.784 1.00 24.75 ? 230 TYR D CE2 1 
ATOM   8333 C  CZ  . TYR D 1 230 ? 10.931  7.322   -59.436 1.00 27.73 ? 230 TYR D CZ  1 
ATOM   8334 O  OH  . TYR D 1 230 ? 11.323  6.460   -60.425 1.00 32.22 ? 230 TYR D OH  1 
ATOM   8335 N  N   . CYS D 1 231 ? 10.537  10.508  -53.190 1.00 16.00 ? 231 CYS D N   1 
ATOM   8336 C  CA  . CYS D 1 231 ? 10.407  11.503  -52.101 1.00 17.01 ? 231 CYS D CA  1 
ATOM   8337 C  C   . CYS D 1 231 ? 10.325  12.903  -52.721 1.00 15.14 ? 231 CYS D C   1 
ATOM   8338 O  O   . CYS D 1 231 ? 10.011  13.800  -51.979 1.00 18.46 ? 231 CYS D O   1 
ATOM   8339 C  CB  . CYS D 1 231 ? 11.599  11.430  -51.155 1.00 19.54 ? 231 CYS D CB  1 
ATOM   8340 S  SG  . CYS D 1 231 ? 12.047  9.738   -50.686 1.00 26.71 ? 231 CYS D SG  1 
ATOM   8341 N  N   . THR D 1 232 ? 10.524  13.025  -54.037 1.00 14.49 ? 232 THR D N   1 
ATOM   8342 C  CA  . THR D 1 232 ? 10.562  14.345  -54.673 1.00 14.93 ? 232 THR D CA  1 
ATOM   8343 C  C   . THR D 1 232 ? 9.255   14.638  -55.402 1.00 15.02 ? 232 THR D C   1 
ATOM   8344 O  O   . THR D 1 232 ? 8.427   13.792  -55.768 1.00 14.11 ? 232 THR D O   1 
ATOM   8345 C  CB  . THR D 1 232 ? 11.752  14.360  -55.647 1.00 16.77 ? 232 THR D CB  1 
ATOM   8346 O  OG1 . THR D 1 232 ? 11.815  13.107  -56.344 1.00 16.42 ? 232 THR D OG1 1 
ATOM   8347 C  CG2 . THR D 1 232 ? 13.056  14.644  -54.935 1.00 19.01 ? 232 THR D CG2 1 
ATOM   8348 N  N   . HIS D 1 233 ? 9.043   15.935  -55.619 1.00 14.11 ? 233 HIS D N   1 
ATOM   8349 C  CA  . HIS D 1 233 ? 7.939   16.373  -56.439 1.00 14.40 ? 233 HIS D CA  1 
ATOM   8350 C  C   . HIS D 1 233 ? 8.126   15.917  -57.878 1.00 14.67 ? 233 HIS D C   1 
ATOM   8351 O  O   . HIS D 1 233 ? 9.241   15.703  -58.360 1.00 15.68 ? 233 HIS D O   1 
ATOM   8352 C  CB  . HIS D 1 233 ? 7.873   17.911  -56.402 1.00 16.97 ? 233 HIS D CB  1 
ATOM   8353 C  CG  . HIS D 1 233 ? 7.383   18.424  -55.100 1.00 19.54 ? 233 HIS D CG  1 
ATOM   8354 N  ND1 . HIS D 1 233 ? 8.213   19.109  -54.229 1.00 27.38 ? 233 HIS D ND1 1 
ATOM   8355 C  CD2 . HIS D 1 233 ? 6.197   18.291  -54.477 1.00 22.68 ? 233 HIS D CD2 1 
ATOM   8356 C  CE1 . HIS D 1 233 ? 7.534   19.417  -53.138 1.00 27.43 ? 233 HIS D CE1 1 
ATOM   8357 N  NE2 . HIS D 1 233 ? 6.301   18.950  -53.281 1.00 24.75 ? 233 HIS D NE2 1 
ATOM   8358 N  N   . MET D 1 234 ? 7.017   15.761  -58.574 1.00 15.21 ? 234 MET D N   1 
ATOM   8359 C  CA  . MET D 1 234 ? 7.033   15.259  -59.948 1.00 16.64 ? 234 MET D CA  1 
ATOM   8360 C  C   . MET D 1 234 ? 7.934   16.101  -60.870 1.00 20.03 ? 234 MET D C   1 
ATOM   8361 O  O   . MET D 1 234 ? 8.616   15.524  -61.738 1.00 20.23 ? 234 MET D O   1 
ATOM   8362 C  CB  . MET D 1 234 ? 5.606   15.243  -60.477 1.00 18.60 ? 234 MET D CB  1 
ATOM   8363 C  CG  . MET D 1 234 ? 5.519   14.618  -61.849 1.00 22.67 ? 234 MET D CG  1 
ATOM   8364 S  SD  . MET D 1 234 ? 3.785   14.548  -62.359 1.00 30.32 ? 234 MET D SD  1 
ATOM   8365 C  CE  . MET D 1 234 ? 3.948   13.410  -63.736 1.00 32.47 ? 234 MET D CE  1 
ATOM   8366 N  N   . ASP D 1 235 ? 8.016   17.422  -60.605 1.00 19.49 ? 235 ASP D N   1 
ATOM   8367 C  CA  . ASP D 1 235 ? 8.785   18.300  -61.487 1.00 21.88 ? 235 ASP D CA  1 
ATOM   8368 C  C   . ASP D 1 235 ? 10.248  18.462  -61.075 1.00 22.59 ? 235 ASP D C   1 
ATOM   8369 O  O   . ASP D 1 235 ? 10.988  19.181  -61.741 1.00 25.26 ? 235 ASP D O   1 
ATOM   8370 C  CB  . ASP D 1 235 ? 8.089   19.659  -61.658 1.00 26.30 ? 235 ASP D CB  1 
ATOM   8371 C  CG  . ASP D 1 235 ? 7.964   20.502  -60.403 1.00 31.02 ? 235 ASP D CG  1 
ATOM   8372 O  OD1 . ASP D 1 235 ? 8.358   20.032  -59.309 1.00 29.72 ? 235 ASP D OD1 1 
ATOM   8373 O  OD2 . ASP D 1 235 ? 7.455   21.635  -60.522 1.00 33.07 ? 235 ASP D OD2 1 
ATOM   8374 N  N   . ASP D 1 236 ? 10.726  17.719  -60.071 1.00 21.63 ? 236 ASP D N   1 
ATOM   8375 C  CA  . ASP D 1 236 ? 12.058  17.908  -59.535 1.00 20.24 ? 236 ASP D CA  1 
ATOM   8376 C  C   . ASP D 1 236 ? 13.092  17.402  -60.537 1.00 22.37 ? 236 ASP D C   1 
ATOM   8377 O  O   . ASP D 1 236 ? 13.022  16.254  -60.966 1.00 25.10 ? 236 ASP D O   1 
ATOM   8378 C  CB  . ASP D 1 236 ? 12.233  17.145  -58.207 1.00 20.26 ? 236 ASP D CB  1 
ATOM   8379 C  CG  . ASP D 1 236 ? 13.462  17.583  -57.428 1.00 22.15 ? 236 ASP D CG  1 
ATOM   8380 O  OD1 . ASP D 1 236 ? 14.533  17.695  -58.045 1.00 24.98 ? 236 ASP D OD1 1 
ATOM   8381 O  OD2 . ASP D 1 236 ? 13.348  17.799  -56.216 1.00 26.20 ? 236 ASP D OD2 1 
ATOM   8382 N  N   . PRO D 1 237 ? 14.078  18.230  -60.969 1.00 24.55 ? 237 PRO D N   1 
ATOM   8383 C  CA  . PRO D 1 237 ? 15.107  17.751  -61.899 1.00 25.45 ? 237 PRO D CA  1 
ATOM   8384 C  C   . PRO D 1 237 ? 16.069  16.721  -61.313 1.00 28.63 ? 237 PRO D C   1 
ATOM   8385 O  O   . PRO D 1 237 ? 16.815  16.081  -62.070 1.00 28.04 ? 237 PRO D O   1 
ATOM   8386 C  CB  . PRO D 1 237 ? 15.862  19.044  -62.278 1.00 26.15 ? 237 PRO D CB  1 
ATOM   8387 C  CG  . PRO D 1 237 ? 15.649  19.962  -61.092 1.00 26.45 ? 237 PRO D CG  1 
ATOM   8388 C  CD  . PRO D 1 237 ? 14.251  19.645  -60.572 1.00 25.30 ? 237 PRO D CD  1 
ATOM   8389 N  N   . SER D 1 238 ? 15.999  16.524  -59.981 1.00 27.13 ? 238 SER D N   1 
ATOM   8390 C  CA  . SER D 1 238 ? 16.870  15.582  -59.294 1.00 28.02 ? 238 SER D CA  1 
ATOM   8391 C  C   . SER D 1 238 ? 16.019  14.604  -58.475 1.00 23.54 ? 238 SER D C   1 
ATOM   8392 O  O   . SER D 1 238 ? 15.938  14.716  -57.266 1.00 24.43 ? 238 SER D O   1 
ATOM   8393 C  CB  . SER D 1 238 ? 17.864  16.313  -58.427 1.00 34.32 ? 238 SER D CB  1 
ATOM   8394 O  OG  . SER D 1 238 ? 18.872  15.420  -57.975 1.00 41.36 ? 238 SER D OG  1 
ATOM   8395 N  N   . PRO D 1 239 ? 15.347  13.645  -59.128 1.00 22.16 ? 239 PRO D N   1 
ATOM   8396 C  CA  . PRO D 1 239 ? 14.444  12.725  -58.425 1.00 23.50 ? 239 PRO D CA  1 
ATOM   8397 C  C   . PRO D 1 239 ? 15.163  11.801  -57.454 1.00 26.22 ? 239 PRO D C   1 
ATOM   8398 O  O   . PRO D 1 239 ? 16.306  11.414  -57.660 1.00 25.79 ? 239 PRO D O   1 
ATOM   8399 C  CB  . PRO D 1 239 ? 13.740  11.899  -59.507 1.00 22.97 ? 239 PRO D CB  1 
ATOM   8400 C  CG  . PRO D 1 239 ? 14.348  12.309  -60.847 1.00 28.51 ? 239 PRO D CG  1 
ATOM   8401 C  CD  . PRO D 1 239 ? 15.350  13.408  -60.570 1.00 23.75 ? 239 PRO D CD  1 
ATOM   8402 N  N   . ARG D 1 240 ? 14.485  11.488  -56.350 1.00 25.37 ? 240 ARG D N   1 
ATOM   8403 C  CA  . ARG D 1 240 ? 15.035  10.515  -55.422 1.00 21.70 ? 240 ARG D CA  1 
ATOM   8404 C  C   . ARG D 1 240 ? 13.962  9.459   -55.125 1.00 21.62 ? 240 ARG D C   1 
ATOM   8405 O  O   . ARG D 1 240 ? 12.833  9.824   -54.772 1.00 19.06 ? 240 ARG D O   1 
ATOM   8406 C  CB  . ARG D 1 240 ? 15.499  11.152  -54.108 1.00 27.76 ? 240 ARG D CB  1 
ATOM   8407 C  CG  . ARG D 1 240 ? 16.577  12.218  -54.267 1.00 37.05 ? 240 ARG D CG  1 
ATOM   8408 C  CD  . ARG D 1 240 ? 16.951  12.856  -52.936 1.00 43.97 ? 240 ARG D CD  1 
ATOM   8409 N  NE  . ARG D 1 240 ? 16.003  13.816  -52.368 1.00 44.09 ? 240 ARG D NE  1 
ATOM   8410 C  CZ  . ARG D 1 240 ? 15.238  13.568  -51.304 1.00 49.35 ? 240 ARG D CZ  1 
ATOM   8411 N  NH1 . ARG D 1 240 ? 15.290  12.385  -50.709 1.00 50.16 ? 240 ARG D NH1 1 
ATOM   8412 N  NH2 . ARG D 1 240 ? 14.410  14.497  -50.850 1.00 49.29 ? 240 ARG D NH2 1 
ATOM   8413 N  N   . GLU D 1 241 ? 14.295  8.176   -55.335 1.00 18.21 ? 241 GLU D N   1 
ATOM   8414 C  CA  . GLU D 1 241 ? 13.397  7.074   -54.989 1.00 18.17 ? 241 GLU D CA  1 
ATOM   8415 C  C   . GLU D 1 241 ? 13.241  6.952   -53.480 1.00 15.49 ? 241 GLU D C   1 
ATOM   8416 O  O   . GLU D 1 241 ? 14.153  7.154   -52.674 1.00 18.15 ? 241 GLU D O   1 
ATOM   8417 C  CB  . GLU D 1 241 ? 13.960  5.754   -55.515 1.00 21.83 ? 241 GLU D CB  1 
ATOM   8418 C  CG  . GLU D 1 241 ? 13.983  5.691   -57.038 1.00 24.21 ? 241 GLU D CG  1 
ATOM   8419 C  CD  . GLU D 1 241 ? 14.904  4.604   -57.549 1.00 27.13 ? 241 GLU D CD  1 
ATOM   8420 O  OE1 . GLU D 1 241 ? 16.139  4.827   -57.512 1.00 36.50 ? 241 GLU D OE1 1 
ATOM   8421 O  OE2 . GLU D 1 241 ? 14.409  3.518   -57.933 1.00 34.58 ? 241 GLU D OE2 1 
ATOM   8422 N  N   . MET D 1 242 ? 11.984  6.705   -53.092 1.00 13.00 ? 242 MET D N   1 
ATOM   8423 C  CA  . MET D 1 242 ? 11.654  6.589   -51.687 1.00 11.83 ? 242 MET D CA  1 
ATOM   8424 C  C   . MET D 1 242 ? 11.912  5.144   -51.213 1.00 10.73 ? 242 MET D C   1 
ATOM   8425 O  O   . MET D 1 242 ? 11.100  4.218   -51.392 1.00 12.18 ? 242 MET D O   1 
ATOM   8426 C  CB  . MET D 1 242 ? 10.190  6.952   -51.452 1.00 12.56 ? 242 MET D CB  1 
ATOM   8427 C  CG  . MET D 1 242 ? 9.883   6.979   -49.956 1.00 12.40 ? 242 MET D CG  1 
ATOM   8428 S  SD  . MET D 1 242 ? 8.137   7.313   -49.601 1.00 12.29 ? 242 MET D SD  1 
ATOM   8429 C  CE  . MET D 1 242 ? 7.987   8.966   -50.284 1.00 13.19 ? 242 MET D CE  1 
ATOM   8430 N  N   . ILE D 1 243 ? 13.128  4.936   -50.700 1.00 10.35 ? 243 ILE D N   1 
ATOM   8431 C  CA  . ILE D 1 243 ? 13.624  3.633   -50.275 1.00 10.10 ? 243 ILE D CA  1 
ATOM   8432 C  C   . ILE D 1 243 ? 14.338  3.855   -48.946 1.00 9.02  ? 243 ILE D C   1 
ATOM   8433 O  O   . ILE D 1 243 ? 14.799  4.952   -48.659 1.00 9.32  ? 243 ILE D O   1 
ATOM   8434 C  CB  . ILE D 1 243 ? 14.593  3.044   -51.310 1.00 11.38 ? 243 ILE D CB  1 
ATOM   8435 C  CG1 . ILE D 1 243 ? 15.695  4.038   -51.713 1.00 13.38 ? 243 ILE D CG1 1 
ATOM   8436 C  CG2 . ILE D 1 243 ? 13.810  2.508   -52.501 1.00 13.99 ? 243 ILE D CG2 1 
ATOM   8437 C  CD1 . ILE D 1 243 ? 16.823  3.381   -52.520 1.00 18.87 ? 243 ILE D CD1 1 
ATOM   8438 N  N   . ASN D 1 244 ? 14.467  2.778   -48.171 1.00 8.76  ? 244 ASN D N   1 
ATOM   8439 C  CA  . ASN D 1 244 ? 15.275  2.753   -46.957 1.00 8.50  ? 244 ASN D CA  1 
ATOM   8440 C  C   . ASN D 1 244 ? 14.871  3.911   -46.038 1.00 8.83  ? 244 ASN D C   1 
ATOM   8441 O  O   . ASN D 1 244 ? 15.703  4.593   -45.435 1.00 8.91  ? 244 ASN D O   1 
ATOM   8442 C  CB  . ASN D 1 244 ? 16.774  2.916   -47.255 1.00 10.04 ? 244 ASN D CB  1 
ATOM   8443 C  CG  . ASN D 1 244 ? 17.215  1.851   -48.208 1.00 12.75 ? 244 ASN D CG  1 
ATOM   8444 O  OD1 . ASN D 1 244 ? 16.803  0.688   -48.127 1.00 11.88 ? 244 ASN D OD1 1 
ATOM   8445 N  ND2 . ASN D 1 244 ? 18.069  2.281   -49.133 1.00 16.66 ? 244 ASN D ND2 1 
ATOM   8446 N  N   . ASN D 1 245 ? 13.552  4.079   -45.838 1.00 7.35  ? 245 ASN D N   1 
ATOM   8447 C  CA  . ASN D 1 245 ? 13.034  5.200   -45.087 1.00 7.31  ? 245 ASN D CA  1 
ATOM   8448 C  C   . ASN D 1 245 ? 12.763  4.755   -43.653 1.00 7.87  ? 245 ASN D C   1 
ATOM   8449 O  O   . ASN D 1 245 ? 11.663  4.872   -43.139 1.00 8.67  ? 245 ASN D O   1 
ATOM   8450 C  CB  . ASN D 1 245 ? 11.775  5.774   -45.737 1.00 7.76  ? 245 ASN D CB  1 
ATOM   8451 C  CG  . ASN D 1 245 ? 10.624  4.804   -45.874 1.00 8.24  ? 245 ASN D CG  1 
ATOM   8452 O  OD1 . ASN D 1 245 ? 10.783  3.596   -45.821 1.00 9.21  ? 245 ASN D OD1 1 
ATOM   8453 N  ND2 . ASN D 1 245 ? 9.380   5.291   -46.059 1.00 9.10  ? 245 ASN D ND2 1 
ATOM   8454 N  N   . PHE D 1 246 ? 13.792  4.207   -43.031 1.00 6.95  ? 246 PHE D N   1 
ATOM   8455 C  CA  . PHE D 1 246 ? 13.757  3.797   -41.631 1.00 7.04  ? 246 PHE D CA  1 
ATOM   8456 C  C   . PHE D 1 246 ? 14.954  4.422   -40.920 1.00 7.76  ? 246 PHE D C   1 
ATOM   8457 O  O   . PHE D 1 246 ? 16.032  4.563   -41.521 1.00 7.97  ? 246 PHE D O   1 
ATOM   8458 C  CB  . PHE D 1 246 ? 13.806  2.250   -41.526 1.00 8.10  ? 246 PHE D CB  1 
ATOM   8459 C  CG  . PHE D 1 246 ? 15.037  1.594   -42.136 1.00 7.74  ? 246 PHE D CG  1 
ATOM   8460 C  CD1 . PHE D 1 246 ? 15.119  1.280   -43.502 1.00 8.54  ? 246 PHE D CD1 1 
ATOM   8461 C  CD2 . PHE D 1 246 ? 16.126  1.256   -41.304 1.00 8.70  ? 246 PHE D CD2 1 
ATOM   8462 C  CE1 . PHE D 1 246 ? 16.264  0.672   -44.017 1.00 9.04  ? 246 PHE D CE1 1 
ATOM   8463 C  CE2 . PHE D 1 246 ? 17.270  0.682   -41.835 1.00 9.84  ? 246 PHE D CE2 1 
ATOM   8464 C  CZ  . PHE D 1 246 ? 17.345  0.393   -43.186 1.00 10.15 ? 246 PHE D CZ  1 
ATOM   8465 N  N   . ARG D 1 247 ? 14.770  4.719   -39.637 1.00 7.07  ? 247 ARG D N   1 
ATOM   8466 C  CA  . ARG D 1 247 ? 15.855  5.197   -38.788 1.00 6.81  ? 247 ARG D CA  1 
ATOM   8467 C  C   . ARG D 1 247 ? 16.591  4.034   -38.146 1.00 7.37  ? 247 ARG D C   1 
ATOM   8468 O  O   . ARG D 1 247 ? 15.937  3.058   -37.816 1.00 7.49  ? 247 ARG D O   1 
ATOM   8469 C  CB  . ARG D 1 247 ? 15.242  6.076   -37.691 1.00 6.94  ? 247 ARG D CB  1 
ATOM   8470 C  CG  . ARG D 1 247 ? 16.241  6.977   -36.991 1.00 7.26  ? 247 ARG D CG  1 
ATOM   8471 C  CD  . ARG D 1 247 ? 15.544  7.640   -35.825 1.00 7.64  ? 247 ARG D CD  1 
ATOM   8472 N  NE  . ARG D 1 247 ? 16.396  8.747   -35.273 1.00 7.00  ? 247 ARG D NE  1 
ATOM   8473 C  CZ  . ARG D 1 247 ? 16.063  9.467   -34.205 1.00 7.49  ? 247 ARG D CZ  1 
ATOM   8474 N  NH1 . ARG D 1 247 ? 14.978  9.193   -33.493 1.00 8.27  ? 247 ARG D NH1 1 
ATOM   8475 N  NH2 . ARG D 1 247 ? 16.849  10.484  -33.837 1.00 7.85  ? 247 ARG D NH2 1 
ATOM   8476 N  N   . GLN D 1 248 ? 17.917  4.164   -37.973 1.00 7.01  ? 248 GLN D N   1 
ATOM   8477 C  CA  . GLN D 1 248 ? 18.641  3.194   -37.149 1.00 7.10  ? 248 GLN D CA  1 
ATOM   8478 C  C   . GLN D 1 248 ? 18.114  3.141   -35.732 1.00 7.07  ? 248 GLN D C   1 
ATOM   8479 O  O   . GLN D 1 248 ? 17.578  4.109   -35.209 1.00 7.30  ? 248 GLN D O   1 
ATOM   8480 C  CB  . GLN D 1 248 ? 20.124  3.571   -37.121 1.00 7.50  ? 248 GLN D CB  1 
ATOM   8481 C  CG  . GLN D 1 248 ? 20.830  3.527   -38.489 1.00 7.82  ? 248 GLN D CG  1 
ATOM   8482 C  CD  . GLN D 1 248 ? 20.818  2.165   -39.149 1.00 9.08  ? 248 GLN D CD  1 
ATOM   8483 O  OE1 . GLN D 1 248 ? 19.901  1.827   -39.917 1.00 9.79  ? 248 GLN D OE1 1 
ATOM   8484 N  NE2 . GLN D 1 248 ? 21.831  1.388   -38.820 1.00 9.69  ? 248 GLN D NE2 1 
ATOM   8485 N  N   . VAL D 1 249 ? 18.347  1.981   -35.108 1.00 7.55  ? 249 VAL D N   1 
ATOM   8486 C  CA  . VAL D 1 249 ? 17.935  1.897   -33.706 1.00 8.67  ? 249 VAL D CA  1 
ATOM   8487 C  C   . VAL D 1 249 ? 18.816  2.830   -32.833 1.00 8.12  ? 249 VAL D C   1 
ATOM   8488 O  O   . VAL D 1 249 ? 19.978  3.137   -33.141 1.00 8.39  ? 249 VAL D O   1 
ATOM   8489 C  CB  . VAL D 1 249 ? 17.973  0.457   -33.159 1.00 8.70  ? 249 VAL D CB  1 
ATOM   8490 C  CG1 . VAL D 1 249 ? 16.941  -0.439  -33.819 1.00 10.36 ? 249 VAL D CG1 1 
ATOM   8491 C  CG2 . VAL D 1 249 ? 19.350  -0.196  -33.241 1.00 10.59 ? 249 VAL D CG2 1 
ATOM   8492 N  N   . GLN D 1 250 ? 18.230  3.192   -31.694 1.00 7.87  ? 250 GLN D N   1 
ATOM   8493 C  CA  . GLN D 1 250 ? 18.755  4.205   -30.774 1.00 8.48  ? 250 GLN D CA  1 
ATOM   8494 C  C   . GLN D 1 250 ? 19.240  3.599   -29.461 1.00 9.34  ? 250 GLN D C   1 
ATOM   8495 O  O   . GLN D 1 250 ? 18.807  2.523   -29.028 1.00 10.51 ? 250 GLN D O   1 
ATOM   8496 C  CB  . GLN D 1 250 ? 17.620  5.183   -30.462 1.00 8.56  ? 250 GLN D CB  1 
ATOM   8497 C  CG  . GLN D 1 250 ? 16.991  5.813   -31.722 1.00 8.41  ? 250 GLN D CG  1 
ATOM   8498 C  CD  . GLN D 1 250 ? 17.942  6.735   -32.445 1.00 8.69  ? 250 GLN D CD  1 
ATOM   8499 O  OE1 . GLN D 1 250 ? 18.360  7.776   -31.863 1.00 9.63  ? 250 GLN D OE1 1 
ATOM   8500 N  NE2 . GLN D 1 250 ? 18.255  6.439   -33.692 1.00 8.66  ? 250 GLN D NE2 1 
ATOM   8501 N  N   . LYS D 1 251 ? 20.107  4.339   -28.793 1.00 9.29  ? 251 LYS D N   1 
ATOM   8502 C  CA  . LYS D 1 251 ? 20.534  3.953   -27.437 1.00 10.31 ? 251 LYS D CA  1 
ATOM   8503 C  C   . LYS D 1 251 ? 19.329  3.921   -26.498 1.00 10.27 ? 251 LYS D C   1 
ATOM   8504 O  O   . LYS D 1 251 ? 18.353  4.643   -26.604 1.00 10.19 ? 251 LYS D O   1 
ATOM   8505 C  CB  . LYS D 1 251 ? 21.438  5.057   -26.888 1.00 11.12 ? 251 LYS D CB  1 
ATOM   8506 C  CG  . LYS D 1 251 ? 22.842  5.120   -27.516 1.00 12.12 ? 251 LYS D CG  1 
ATOM   8507 C  CD  . LYS D 1 251 ? 23.748  4.026   -26.891 1.00 12.68 ? 251 LYS D CD  1 
ATOM   8508 C  CE  . LYS D 1 251 ? 25.213  4.105   -27.317 1.00 11.32 ? 251 LYS D CE  1 
ATOM   8509 N  NZ  . LYS D 1 251 ? 25.326  3.955   -28.806 1.00 11.37 ? 251 LYS D NZ  1 
ATOM   8510 N  N   . PHE D 1 252 ? 19.343  2.941   -25.577 1.00 12.13 ? 252 PHE D N   1 
ATOM   8511 C  CA  . PHE D 1 252 ? 18.264  2.774   -24.610 1.00 13.51 ? 252 PHE D CA  1 
ATOM   8512 C  C   . PHE D 1 252 ? 18.108  3.924   -23.593 1.00 14.98 ? 252 PHE D C   1 
ATOM   8513 O  O   . PHE D 1 252 ? 17.012  4.171   -23.089 1.00 15.80 ? 252 PHE D O   1 
ATOM   8514 C  CB  . PHE D 1 252 ? 18.485  1.441   -23.878 1.00 15.35 ? 252 PHE D CB  1 
ATOM   8515 C  CG  . PHE D 1 252 ? 17.851  0.368   -24.722 1.00 16.76 ? 252 PHE D CG  1 
ATOM   8516 C  CD1 . PHE D 1 252 ? 16.511  0.070   -24.510 1.00 20.55 ? 252 PHE D CD1 1 
ATOM   8517 C  CD2 . PHE D 1 252 ? 18.554  -0.284  -25.728 1.00 23.54 ? 252 PHE D CD2 1 
ATOM   8518 C  CE1 . PHE D 1 252 ? 15.869  -0.863  -25.306 1.00 22.44 ? 252 PHE D CE1 1 
ATOM   8519 C  CE2 . PHE D 1 252 ? 17.892  -1.211  -26.539 1.00 20.78 ? 252 PHE D CE2 1 
ATOM   8520 C  CZ  . PHE D 1 252 ? 16.560  -1.460  -26.332 1.00 19.89 ? 252 PHE D CZ  1 
ATOM   8521 N  N   . ASP D 1 253 ? 19.190  4.619   -23.182 1.00 15.05 ? 253 ASP D N   1 
ATOM   8522 C  CA  . ASP D 1 253 ? 19.023  5.716   -22.215 1.00 19.42 ? 253 ASP D CA  1 
ATOM   8523 C  C   . ASP D 1 253 ? 18.358  5.205   -20.921 1.00 19.53 ? 253 ASP D C   1 
ATOM   8524 O  O   . ASP D 1 253 ? 17.494  5.900   -20.379 1.00 21.38 ? 253 ASP D O   1 
ATOM   8525 C  CB  . ASP D 1 253 ? 18.247  6.928   -22.761 1.00 20.65 ? 253 ASP D CB  1 
ATOM   8526 C  CG  . ASP D 1 253 ? 18.916  7.630   -23.952 1.00 23.21 ? 253 ASP D CG  1 
ATOM   8527 O  OD1 . ASP D 1 253 ? 20.153  7.551   -24.068 1.00 24.44 ? 253 ASP D OD1 1 
ATOM   8528 O  OD2 . ASP D 1 253 ? 18.183  8.274   -24.741 1.00 21.68 ? 253 ASP D OD2 1 
ATOM   8529 N  N   . GLU D 1 254 ? 18.725  3.980   -20.488 1.00 20.12 ? 254 GLU D N   1 
ATOM   8530 C  CA  . GLU D 1 254 ? 18.312  3.368   -19.216 1.00 20.99 ? 254 GLU D CA  1 
ATOM   8531 C  C   . GLU D 1 254 ? 16.877  2.815   -19.245 1.00 20.59 ? 254 GLU D C   1 
ATOM   8532 O  O   . GLU D 1 254 ? 16.365  2.278   -18.246 1.00 20.97 ? 254 GLU D O   1 
ATOM   8533 C  CB  . GLU D 1 254 ? 18.489  4.328   -18.027 1.00 24.97 ? 254 GLU D CB  1 
ATOM   8534 C  CG  . GLU D 1 254 ? 19.939  4.625   -17.696 1.00 34.78 ? 254 GLU D CG  1 
ATOM   8535 C  CD  . GLU D 1 254 ? 20.103  5.729   -16.659 1.00 46.25 ? 254 GLU D CD  1 
ATOM   8536 O  OE1 . GLU D 1 254 ? 20.909  5.532   -15.733 1.00 58.17 ? 254 GLU D OE1 1 
ATOM   8537 O  OE2 . GLU D 1 254 ? 19.418  6.776   -16.762 1.00 52.38 ? 254 GLU D OE2 1 
ATOM   8538 N  N   . ARG D 1 255 ? 16.175  2.957   -20.370 1.00 16.71 ? 255 ARG D N   1 
ATOM   8539 C  CA  . ARG D 1 255 ? 14.829  2.419   -20.483 1.00 16.73 ? 255 ARG D CA  1 
ATOM   8540 C  C   . ARG D 1 255 ? 14.845  0.892   -20.471 1.00 18.23 ? 255 ARG D C   1 
ATOM   8541 O  O   . ARG D 1 255 ? 15.786  0.260   -20.977 1.00 20.21 ? 255 ARG D O   1 
ATOM   8542 C  CB  . ARG D 1 255 ? 14.172  2.869   -21.810 1.00 15.92 ? 255 ARG D CB  1 
ATOM   8543 C  CG  . ARG D 1 255 ? 13.847  4.349   -21.845 1.00 15.50 ? 255 ARG D CG  1 
ATOM   8544 C  CD  . ARG D 1 255 ? 13.400  4.677   -23.292 1.00 15.11 ? 255 ARG D CD  1 
ATOM   8545 N  NE  . ARG D 1 255 ? 14.485  4.678   -24.271 1.00 14.53 ? 255 ARG D NE  1 
ATOM   8546 C  CZ  . ARG D 1 255 ? 14.342  5.000   -25.551 1.00 14.01 ? 255 ARG D CZ  1 
ATOM   8547 N  NH1 . ARG D 1 255 ? 13.156  5.350   -26.018 1.00 11.89 ? 255 ARG D NH1 1 
ATOM   8548 N  NH2 . ARG D 1 255 ? 15.386  4.971   -26.361 1.00 12.60 ? 255 ARG D NH2 1 
ATOM   8549 N  N   . LEU D 1 256 ? 13.743  0.313   -19.965 1.00 16.73 ? 256 LEU D N   1 
ATOM   8550 C  CA  . LEU D 1 256 ? 13.367  -1.076  -20.224 1.00 14.88 ? 256 LEU D CA  1 
ATOM   8551 C  C   . LEU D 1 256 ? 12.200  -1.059  -21.197 1.00 15.59 ? 256 LEU D C   1 
ATOM   8552 O  O   . LEU D 1 256 ? 11.514  -0.038  -21.409 1.00 16.47 ? 256 LEU D O   1 
ATOM   8553 C  CB  . LEU D 1 256 ? 12.949  -1.777  -18.928 1.00 16.13 ? 256 LEU D CB  1 
ATOM   8554 C  CG  . LEU D 1 256 ? 14.047  -1.876  -17.881 1.00 16.35 ? 256 LEU D CG  1 
ATOM   8555 C  CD1 . LEU D 1 256 ? 13.441  -2.470  -16.602 1.00 21.55 ? 256 LEU D CD1 1 
ATOM   8556 C  CD2 . LEU D 1 256 ? 15.276  -2.646  -18.389 1.00 20.43 ? 256 LEU D CD2 1 
ATOM   8557 N  N   . VAL D 1 257 ? 12.001  -2.217  -21.801 1.00 13.57 ? 257 VAL D N   1 
ATOM   8558 C  CA  . VAL D 1 257 ? 10.822  -2.461  -22.609 1.00 12.60 ? 257 VAL D CA  1 
ATOM   8559 C  C   . VAL D 1 257 ? 9.996   -3.485  -21.867 1.00 13.19 ? 257 VAL D C   1 
ATOM   8560 O  O   . VAL D 1 257 ? 10.502  -4.547  -21.473 1.00 13.51 ? 257 VAL D O   1 
ATOM   8561 C  CB  . VAL D 1 257 ? 11.191  -3.017  -23.997 1.00 13.24 ? 257 VAL D CB  1 
ATOM   8562 C  CG1 . VAL D 1 257 ? 9.951   -3.431  -24.748 1.00 12.93 ? 257 VAL D CG1 1 
ATOM   8563 C  CG2 . VAL D 1 257 ? 11.983  -1.987  -24.791 1.00 13.92 ? 257 VAL D CG2 1 
ATOM   8564 N  N   . TYR D 1 258 ? 8.747   -3.132  -21.632 1.00 11.17 ? 258 TYR D N   1 
ATOM   8565 C  CA  . TYR D 1 258 ? 7.852   -3.968  -20.843 1.00 11.85 ? 258 TYR D CA  1 
ATOM   8566 C  C   . TYR D 1 258 ? 7.046   -4.864  -21.759 1.00 12.08 ? 258 TYR D C   1 
ATOM   8567 O  O   . TYR D 1 258 ? 6.670   -4.470  -22.869 1.00 12.76 ? 258 TYR D O   1 
ATOM   8568 C  CB  . TYR D 1 258 ? 6.999   -3.093  -19.906 1.00 14.03 ? 258 TYR D CB  1 
ATOM   8569 C  CG  . TYR D 1 258 ? 7.856   -2.235  -19.009 1.00 14.44 ? 258 TYR D CG  1 
ATOM   8570 C  CD1 . TYR D 1 258 ? 8.366   -2.725  -17.818 1.00 15.69 ? 258 TYR D CD1 1 
ATOM   8571 C  CD2 . TYR D 1 258 ? 8.269   -0.962  -19.410 1.00 16.08 ? 258 TYR D CD2 1 
ATOM   8572 C  CE1 . TYR D 1 258 ? 9.251   -1.970  -17.047 1.00 19.03 ? 258 TYR D CE1 1 
ATOM   8573 C  CE2 . TYR D 1 258 ? 9.110   -0.189  -18.625 1.00 20.04 ? 258 TYR D CE2 1 
ATOM   8574 C  CZ  . TYR D 1 258 ? 9.585   -0.684  -17.425 1.00 19.53 ? 258 TYR D CZ  1 
ATOM   8575 O  OH  . TYR D 1 258 ? 10.431  0.098   -16.688 1.00 20.84 ? 258 TYR D OH  1 
ATOM   8576 N  N   . THR D 1 259 ? 6.822   -6.121  -21.344 1.00 11.33 ? 259 THR D N   1 
ATOM   8577 C  CA  . THR D 1 259 ? 6.120   -7.033  -22.210 1.00 10.66 ? 259 THR D CA  1 
ATOM   8578 C  C   . THR D 1 259 ? 4.862   -7.534  -21.513 1.00 10.84 ? 259 THR D C   1 
ATOM   8579 O  O   . THR D 1 259 ? 4.814   -7.678  -20.267 1.00 11.62 ? 259 THR D O   1 
ATOM   8580 C  CB  . THR D 1 259 ? 6.947   -8.254  -22.617 1.00 10.77 ? 259 THR D CB  1 
ATOM   8581 O  OG1 . THR D 1 259 ? 7.393   -8.941  -21.443 1.00 12.74 ? 259 THR D OG1 1 
ATOM   8582 C  CG2 . THR D 1 259 ? 8.216   -7.842  -23.341 1.00 11.97 ? 259 THR D CG2 1 
ATOM   8583 N  N   . SER D 1 260 ? 3.841   -7.807  -22.310 1.00 10.90 ? 260 SER D N   1 
ATOM   8584 C  CA  . SER D 1 260 ? 2.584   -8.353  -21.770 1.00 12.05 ? 260 SER D CA  1 
ATOM   8585 C  C   . SER D 1 260 ? 2.618   -9.880  -21.748 1.00 14.73 ? 260 SER D C   1 
ATOM   8586 O  O   . SER D 1 260 ? 1.636   -10.568 -21.380 1.00 17.78 ? 260 SER D O   1 
ATOM   8587 C  CB  . SER D 1 260 ? 1.416   -7.851  -22.585 1.00 14.08 ? 260 SER D CB  1 
ATOM   8588 O  OG  . SER D 1 260 ? 1.525   -8.375  -23.919 1.00 13.02 ? 260 SER D OG  1 
ATOM   8589 N  N   . PHE D 1 261 ? 3.771   -10.451 -22.088 1.00 14.07 ? 261 PHE D N   1 
ATOM   8590 C  CA  . PHE D 1 261 ? 3.955   -11.902 -22.194 1.00 15.66 ? 261 PHE D CA  1 
ATOM   8591 C  C   . PHE D 1 261 ? 5.247   -12.230 -21.473 1.00 18.76 ? 261 PHE D C   1 
ATOM   8592 O  O   . PHE D 1 261 ? 6.133   -11.418 -21.320 1.00 16.54 ? 261 PHE D O   1 
ATOM   8593 C  CB  . PHE D 1 261 ? 3.951   -12.365 -23.661 1.00 15.91 ? 261 PHE D CB  1 
ATOM   8594 C  CG  . PHE D 1 261 ? 5.005   -11.669 -24.503 1.00 15.16 ? 261 PHE D CG  1 
ATOM   8595 C  CD1 . PHE D 1 261 ? 6.290   -12.192 -24.640 1.00 16.19 ? 261 PHE D CD1 1 
ATOM   8596 C  CD2 . PHE D 1 261 ? 4.752   -10.436 -25.123 1.00 14.21 ? 261 PHE D CD2 1 
ATOM   8597 C  CE1 . PHE D 1 261 ? 7.279   -11.546 -25.382 1.00 16.08 ? 261 PHE D CE1 1 
ATOM   8598 C  CE2 . PHE D 1 261 ? 5.751   -9.786  -25.866 1.00 14.56 ? 261 PHE D CE2 1 
ATOM   8599 C  CZ  . PHE D 1 261 ? 7.012   -10.323 -25.989 1.00 13.90 ? 261 PHE D CZ  1 
ATOM   8600 N  N   . SER D 1 262 ? 5.367   -13.442 -20.938 1.00 26.92 ? 262 SER D N   1 
ATOM   8601 C  CA  . SER D 1 262 ? 6.690   -13.907 -20.433 1.00 32.80 ? 262 SER D CA  1 
ATOM   8602 C  C   . SER D 1 262 ? 7.155   -14.979 -21.424 1.00 35.57 ? 262 SER D C   1 
ATOM   8603 O  O   . SER D 1 262 ? 8.317   -15.022 -21.849 1.00 38.77 ? 262 SER D O   1 
ATOM   8604 C  CB  . SER D 1 262 ? 6.655   -14.353 -19.022 1.00 39.41 ? 262 SER D CB  1 
ATOM   8605 O  OG  . SER D 1 262 ? 5.409   -14.917 -18.687 1.00 43.75 ? 262 SER D OG  1 
ATOM   8606 N  N   . GLN D 1 263 ? 6.168   -15.763 -21.781 1.00 44.17 ? 263 GLN D N   1 
ATOM   8607 C  CA  . GLN D 1 263 ? 6.060   -16.767 -22.843 1.00 54.09 ? 263 GLN D CA  1 
ATOM   8608 C  C   . GLN D 1 263 ? 7.392   -17.213 -23.402 1.00 59.38 ? 263 GLN D C   1 
ATOM   8609 O  O   . GLN D 1 263 ? 8.127   -17.926 -22.708 1.00 64.89 ? 263 GLN D O   1 
ATOM   8610 C  CB  . GLN D 1 263 ? 5.353   -16.051 -23.984 1.00 47.08 ? 263 GLN D CB  1 
ATOM   8611 C  CG  . GLN D 1 263 ? 3.930   -16.538 -24.171 1.00 51.51 ? 263 GLN D CG  1 
ATOM   8612 C  CD  . GLN D 1 263 ? 2.946   -15.835 -23.272 1.00 54.04 ? 263 GLN D CD  1 
ATOM   8613 O  OE1 . GLN D 1 263 ? 3.199   -15.557 -22.102 1.00 44.38 ? 263 GLN D OE1 1 
ATOM   8614 N  NE2 . GLN D 1 263 ? 1.795   -15.510 -23.839 1.00 55.02 ? 263 GLN D NE2 1 
ATOM   8615 O  OXT . GLN D 1 263 ? 7.596   -16.887 -24.567 1.00 57.74 ? 263 GLN D OXT 1 
HETATM 8616 ZN ZN  . ZN  E 2 .   ? 22.897  0.564   12.266  1.00 7.37  ? 301 ZN  A ZN  1 
HETATM 8617 C  C1  . EDO F 3 .   ? 27.269  -9.106  31.087  1.00 31.22 ? 302 EDO A C1  1 
HETATM 8618 O  O1  . EDO F 3 .   ? 28.592  -9.427  30.654  1.00 33.19 ? 302 EDO A O1  1 
HETATM 8619 C  C2  . EDO F 3 .   ? 26.379  -8.820  29.923  1.00 27.80 ? 302 EDO A C2  1 
HETATM 8620 O  O2  . EDO F 3 .   ? 26.131  -9.926  29.032  1.00 25.59 ? 302 EDO A O2  1 
HETATM 8621 C  C1  . EDO G 3 .   ? 36.418  6.196   14.054  1.00 26.58 ? 303 EDO A C1  1 
HETATM 8622 O  O1  . EDO G 3 .   ? 36.900  4.919   14.402  1.00 25.63 ? 303 EDO A O1  1 
HETATM 8623 C  C2  . EDO G 3 .   ? 37.069  6.804   12.846  1.00 25.38 ? 303 EDO A C2  1 
HETATM 8624 O  O2  . EDO G 3 .   ? 36.876  6.144   11.575  1.00 20.98 ? 303 EDO A O2  1 
HETATM 8625 S  S   . DMS H 4 .   ? 12.849  -14.884 12.864  1.00 48.95 ? 304 DMS A S   1 
HETATM 8626 O  O   . DMS H 4 .   ? 13.812  -15.871 13.497  1.00 43.45 ? 304 DMS A O   1 
HETATM 8627 C  C1  . DMS H 4 .   ? 11.273  -15.202 13.642  1.00 38.66 ? 304 DMS A C1  1 
HETATM 8628 C  C2  . DMS H 4 .   ? 12.458  -15.635 11.301  1.00 33.98 ? 304 DMS A C2  1 
HETATM 8629 O  O13 . EA3 I 5 .   ? 26.202  5.667   13.985  1.00 14.86 ? 305 EA3 A O13 1 
HETATM 8630 C  C12 . EA3 I 5 .   ? 25.265  5.884   13.152  1.00 13.06 ? 305 EA3 A C12 1 
HETATM 8631 N  N14 . EA3 I 5 .   ? 24.124  6.481   13.466  1.00 13.76 ? 305 EA3 A N14 1 
HETATM 8632 C  C15 . EA3 I 5 .   ? 23.889  7.048   14.816  1.00 17.88 ? 305 EA3 A C15 1 
HETATM 8633 C  C16 . EA3 I 5 .   ? 24.244  8.502   15.164  1.00 29.04 ? 305 EA3 A C16 1 
HETATM 8634 O  O17 . EA3 I 5 .   ? 24.180  9.356   14.090  1.00 30.21 ? 305 EA3 A O17 1 
HETATM 8635 C  C9  . EA3 I 5 .   ? 25.396  5.291   11.825  1.00 11.09 ? 305 EA3 A C9  1 
HETATM 8636 C  C10 . EA3 I 5 .   ? 24.544  4.248   11.421  1.00 8.89  ? 305 EA3 A C10 1 
HETATM 8637 C  C3  . EA3 I 5 .   ? 24.631  3.586   10.202  1.00 7.73  ? 305 EA3 A C3  1 
HETATM 8638 S  S2  . EA3 I 5 .   ? 23.636  2.197   9.831   1.00 8.14  ? 305 EA3 A S2  1 
HETATM 8639 O  O4  . EA3 I 5 .   ? 24.567  1.058   9.821   1.00 8.07  ? 305 EA3 A O4  1 
HETATM 8640 O  O5  . EA3 I 5 .   ? 22.927  2.485   8.581   1.00 7.33  ? 305 EA3 A O5  1 
HETATM 8641 N  N1  . EA3 I 5 .   ? 22.616  2.029   11.028  1.00 7.54  ? 305 EA3 A N1  1 
HETATM 8642 C  C8  . EA3 I 5 .   ? 26.390  5.648   10.936  1.00 10.09 ? 305 EA3 A C8  1 
HETATM 8643 C  C7  . EA3 I 5 .   ? 26.494  5.051   9.699   1.00 11.10 ? 305 EA3 A C7  1 
HETATM 8644 C  C6  . EA3 I 5 .   ? 25.652  4.010   9.331   1.00 9.72  ? 305 EA3 A C6  1 
HETATM 8645 CL CL1 . EA3 I 5 .   ? 25.932  3.309   7.808   1.00 10.07 ? 305 EA3 A CL1 1 
HETATM 8646 S  S18 . EA3 I 5 .   ? 27.388  7.035   11.462  1.00 15.99 ? 305 EA3 A S18 1 
HETATM 8647 C  C19 . EA3 I 5 .   ? 28.191  7.600   9.954   1.00 18.45 ? 305 EA3 A C19 1 
HETATM 8648 C  C24 . EA3 I 5 .   ? 29.485  6.838   9.654   1.00 23.27 ? 305 EA3 A C24 1 
HETATM 8649 C  C23 . EA3 I 5 .   ? 30.617  7.690   10.199  1.00 32.65 ? 305 EA3 A C23 1 
HETATM 8650 C  C22 . EA3 I 5 .   ? 30.734  8.803   9.155   1.00 26.91 ? 305 EA3 A C22 1 
HETATM 8651 C  C21 . EA3 I 5 .   ? 29.447  9.609   9.107   1.00 25.07 ? 305 EA3 A C21 1 
HETATM 8652 C  C20 . EA3 I 5 .   ? 28.509  9.077   10.185  1.00 25.25 ? 305 EA3 A C20 1 
HETATM 8653 ZN ZN  . ZN  J 2 .   ? -8.094  3.577   4.879   1.00 6.33  ? 301 ZN  B ZN  1 
HETATM 8654 C  C1  . EDO K 3 .   ? -13.661 -5.966  -12.233 1.00 22.87 ? 302 EDO B C1  1 
HETATM 8655 O  O1  . EDO K 3 .   ? -13.535 -6.977  -11.240 1.00 19.42 ? 302 EDO B O1  1 
HETATM 8656 C  C2  . EDO K 3 .   ? -14.753 -6.084  -13.258 1.00 24.62 ? 302 EDO B C2  1 
HETATM 8657 O  O2  . EDO K 3 .   ? -16.087 -5.973  -12.724 1.00 22.68 ? 302 EDO B O2  1 
HETATM 8658 C  C1  . EDO L 3 .   ? -17.027 -3.467  23.016  1.00 28.97 ? 303 EDO B C1  1 
HETATM 8659 O  O1  . EDO L 3 .   ? -16.027 -2.464  23.180  1.00 31.06 ? 303 EDO B O1  1 
HETATM 8660 C  C2  . EDO L 3 .   ? -17.454 -3.698  21.608  1.00 24.43 ? 303 EDO B C2  1 
HETATM 8661 O  O2  . EDO L 3 .   ? -16.430 -3.717  20.556  1.00 19.75 ? 303 EDO B O2  1 
HETATM 8662 C  C1  . EDO M 3 .   ? -27.852 -4.856  -6.028  1.00 46.33 ? 304 EDO B C1  1 
HETATM 8663 O  O1  . EDO M 3 .   ? -27.046 -3.712  -5.990  1.00 37.72 ? 304 EDO B O1  1 
HETATM 8664 C  C2  . EDO M 3 .   ? -27.989 -5.390  -4.664  1.00 41.58 ? 304 EDO B C2  1 
HETATM 8665 O  O2  . EDO M 3 .   ? -27.229 -6.563  -4.472  1.00 38.54 ? 304 EDO B O2  1 
HETATM 8666 O  O13 . EA3 N 5 .   ? -10.492 9.180   3.136   1.00 13.55 ? 305 EA3 B O13 1 
HETATM 8667 C  C12 . EA3 N 5 .   ? -9.510  9.168   3.871   1.00 13.00 ? 305 EA3 B C12 1 
HETATM 8668 N  N14 . EA3 N 5 .   ? -8.325  9.529   3.452   1.00 12.21 ? 305 EA3 B N14 1 
HETATM 8669 C  C15 . EA3 N 5 .   ? -8.002  10.064  2.103   1.00 17.17 ? 305 EA3 B C15 1 
HETATM 8670 C  C16 . EA3 N 5 .   ? -7.612  11.513  2.385   1.00 23.56 ? 305 EA3 B C16 1 
HETATM 8671 O  O17 . EA3 N 5 .   ? -8.144  12.246  1.356   1.00 40.06 ? 305 EA3 B O17 1 
HETATM 8672 C  C9  . EA3 N 5 .   ? -9.702  8.714   5.230   1.00 10.66 ? 305 EA3 B C9  1 
HETATM 8673 C  C10 . EA3 N 5 .   ? -9.041  7.528   5.594   1.00 9.29  ? 305 EA3 B C10 1 
HETATM 8674 C  C3  . EA3 N 5 .   ? -9.148  6.952   6.849   1.00 7.65  ? 305 EA3 B C3  1 
HETATM 8675 S  S2  . EA3 N 5 .   ? -8.369  5.407   7.250   1.00 7.08  ? 305 EA3 B S2  1 
HETATM 8676 O  O4  . EA3 N 5 .   ? -9.458  4.466   7.364   1.00 7.71  ? 305 EA3 B O4  1 
HETATM 8677 O  O5  . EA3 N 5 .   ? -7.602  5.631   8.444   1.00 6.76  ? 305 EA3 B O5  1 
HETATM 8678 N  N1  . EA3 N 5 .   ? -7.489  4.982   5.996   1.00 7.61  ? 305 EA3 B N1  1 
HETATM 8679 C  C8  . EA3 N 5 .   ? -10.540 9.279   6.191   1.00 9.03  ? 305 EA3 B C8  1 
HETATM 8680 C  C7  . EA3 N 5 .   ? -10.679 8.744   7.464   1.00 9.80  ? 305 EA3 B C7  1 
HETATM 8681 C  C6  . EA3 N 5 .   ? -10.009 7.571   7.749   1.00 8.80  ? 305 EA3 B C6  1 
HETATM 8682 CL CL1 . EA3 N 5 .   ? -10.313 6.985   9.336   1.00 9.71  ? 305 EA3 B CL1 1 
HETATM 8683 S  S18 . EA3 N 5 .   ? -11.360 10.776  5.614   1.00 14.76 ? 305 EA3 B S18 1 
HETATM 8684 C  C19 . EA3 N 5 .   ? -11.995 11.509  7.115   1.00 17.55 ? 305 EA3 B C19 1 
HETATM 8685 C  C24 . EA3 N 5 .   ? -13.295 10.711  7.309   1.00 22.02 ? 305 EA3 B C24 1 
HETATM 8686 C  C23 . EA3 N 5 .   ? -13.963 11.387  8.484   1.00 21.79 ? 305 EA3 B C23 1 
HETATM 8687 C  C22 . EA3 N 5 .   ? -14.224 12.871  8.076   1.00 22.34 ? 305 EA3 B C22 1 
HETATM 8688 C  C21 . EA3 N 5 .   ? -12.900 13.616  7.935   1.00 22.05 ? 305 EA3 B C21 1 
HETATM 8689 C  C20 . EA3 N 5 .   ? -12.292 12.972  6.714   1.00 20.25 ? 305 EA3 B C20 1 
HETATM 8690 ZN ZN  . ZN  O 2 .   ? 37.359  2.629   -30.969 1.00 9.34  ? 301 ZN  C ZN  1 
HETATM 8691 C  C1  . EDO P 3 .   ? 50.627  8.595   -28.782 1.00 19.12 ? 302 EDO C C1  1 
HETATM 8692 O  O1  . EDO P 3 .   ? 51.174  7.311   -28.502 1.00 18.29 ? 302 EDO C O1  1 
HETATM 8693 C  C2  . EDO P 3 .   ? 51.474  9.145   -29.903 1.00 18.42 ? 302 EDO C C2  1 
HETATM 8694 O  O2  . EDO P 3 .   ? 51.270  8.453   -31.169 1.00 18.24 ? 302 EDO C O2  1 
HETATM 8695 C  C1  . EDO Q 3 .   ? 46.412  -7.135  -46.377 1.00 24.36 ? 303 EDO C C1  1 
HETATM 8696 O  O1  . EDO Q 3 .   ? 45.227  -6.892  -45.593 1.00 18.14 ? 303 EDO C O1  1 
HETATM 8697 C  C2  . EDO Q 3 .   ? 46.226  -6.789  -47.832 1.00 25.26 ? 303 EDO C C2  1 
HETATM 8698 O  O2  . EDO Q 3 .   ? 45.329  -5.716  -48.153 1.00 26.32 ? 303 EDO C O2  1 
HETATM 8699 S  S   . DMS R 4 .   ? 27.387  -12.834 -30.429 1.00 53.21 ? 304 DMS C S   1 
HETATM 8700 O  O   . DMS R 4 .   ? 28.266  -13.900 -29.806 1.00 50.26 ? 304 DMS C O   1 
HETATM 8701 C  C1  . DMS R 4 .   ? 25.727  -13.164 -29.856 1.00 43.40 ? 304 DMS C C1  1 
HETATM 8702 C  C2  . DMS R 4 .   ? 27.152  -13.462 -32.072 1.00 39.21 ? 304 DMS C C2  1 
HETATM 8703 O  O13 . EA3 S 5 .   ? 40.578  7.758   -29.203 1.00 17.40 ? 305 EA3 C O13 1 
HETATM 8704 C  C12 . EA3 S 5 .   ? 39.687  7.961   -30.078 1.00 16.46 ? 305 EA3 C C12 1 
HETATM 8705 N  N14 . EA3 S 5 .   ? 38.640  8.655   -29.842 1.00 16.29 ? 305 EA3 C N14 1 
HETATM 8706 C  C15 . EA3 S 5 .   ? 38.411  9.387   -28.595 1.00 22.10 ? 305 EA3 C C15 1 
HETATM 8707 C  C16 . EA3 S 5 .   ? 38.278  10.818  -29.105 1.00 28.50 ? 305 EA3 C C16 1 
HETATM 8708 O  O17 . EA3 S 5 .   ? 39.426  11.573  -28.938 1.00 37.91 ? 305 EA3 C O17 1 
HETATM 8709 C  C9  . EA3 S 5 .   ? 39.830  7.353   -31.411 1.00 13.76 ? 305 EA3 C C9  1 
HETATM 8710 C  C10 . EA3 S 5 .   ? 39.007  6.263   -31.777 1.00 11.35 ? 305 EA3 C C10 1 
HETATM 8711 C  C3  . EA3 S 5 .   ? 39.151  5.617   -33.002 1.00 9.63  ? 305 EA3 C C3  1 
HETATM 8712 S  S2  . EA3 S 5 .   ? 38.155  4.230   -33.406 1.00 9.68  ? 305 EA3 C S2  1 
HETATM 8713 O  O4  . EA3 S 5 .   ? 39.060  3.137   -33.410 1.00 8.82  ? 305 EA3 C O4  1 
HETATM 8714 O  O5  . EA3 S 5 .   ? 37.477  4.546   -34.685 1.00 9.33  ? 305 EA3 C O5  1 
HETATM 8715 N  N1  . EA3 S 5 .   ? 37.052  4.043   -32.256 1.00 8.49  ? 305 EA3 C N1  1 
HETATM 8716 C  C8  . EA3 S 5 .   ? 40.824  7.744   -32.283 1.00 12.33 ? 305 EA3 C C8  1 
HETATM 8717 C  C7  . EA3 S 5 .   ? 41.025  7.091   -33.477 1.00 13.04 ? 305 EA3 C C7  1 
HETATM 8718 C  C6  . EA3 S 5 .   ? 40.201  6.041   -33.843 1.00 11.21 ? 305 EA3 C C6  1 
HETATM 8719 CL CL1 . EA3 S 5 .   ? 40.478  5.338   -35.386 1.00 11.49 ? 305 EA3 C CL1 1 
HETATM 8720 S  S18 . EA3 S 5 .   ? 41.877  9.112   -31.714 1.00 18.89 ? 305 EA3 C S18 1 
HETATM 8721 C  C19 . EA3 S 5 .   ? 42.509  9.728   -33.267 1.00 21.99 ? 305 EA3 C C19 1 
HETATM 8722 C  C24 . EA3 S 5 .   ? 43.756  8.965   -33.781 1.00 30.06 ? 305 EA3 C C24 1 
HETATM 8723 C  C23 . EA3 S 5 .   ? 45.037  9.580   -33.242 1.00 34.45 ? 305 EA3 C C23 1 
HETATM 8724 C  C22 . EA3 S 5 .   ? 45.100  11.095  -33.444 1.00 33.04 ? 305 EA3 C C22 1 
HETATM 8725 C  C21 . EA3 S 5 .   ? 43.796  11.815  -33.780 1.00 30.80 ? 305 EA3 C C21 1 
HETATM 8726 C  C20 . EA3 S 5 .   ? 42.669  11.224  -32.967 1.00 31.24 ? 305 EA3 C C20 1 
HETATM 8727 ZN ZN  . ZN  T 2 .   ? 6.605   5.592   -38.596 1.00 6.81  ? 301 ZN  D ZN  1 
HETATM 8728 C  C1  . EDO U 3 .   ? -2.101  -1.069  -20.432 1.00 23.25 ? 302 EDO D C1  1 
HETATM 8729 O  O1  . EDO U 3 .   ? -1.274  0.093   -20.327 1.00 28.93 ? 302 EDO D O1  1 
HETATM 8730 C  C2  . EDO U 3 .   ? -2.746  -1.300  -21.766 1.00 21.87 ? 302 EDO D C2  1 
HETATM 8731 O  O2  . EDO U 3 .   ? -1.744  -1.387  -22.803 1.00 20.55 ? 302 EDO D O2  1 
HETATM 8732 O  O13 . EA3 V 5 .   ? 4.282   11.255  -40.398 1.00 14.07 ? 303 EA3 D O13 1 
HETATM 8733 C  C12 . EA3 V 5 .   ? 5.284   11.231  -39.669 1.00 11.10 ? 303 EA3 D C12 1 
HETATM 8734 N  N14 . EA3 V 5 .   ? 6.464   11.600  -40.066 1.00 12.58 ? 303 EA3 D N14 1 
HETATM 8735 C  C15 . EA3 V 5 .   ? 6.786   12.136  -41.441 1.00 15.68 ? 303 EA3 D C15 1 
HETATM 8736 C  C16 . EA3 V 5 .   ? 7.291   13.600  -41.340 1.00 20.40 ? 303 EA3 D C16 1 
HETATM 8737 O  O17 . EA3 V 5 .   ? 6.312   14.441  -40.877 1.00 33.55 ? 303 EA3 D O17 1 
HETATM 8738 C  C9  . EA3 V 5 .   ? 5.106   10.745  -38.318 1.00 10.22 ? 303 EA3 D C9  1 
HETATM 8739 C  C10 . EA3 V 5 .   ? 5.739   9.570   -37.970 1.00 9.42  ? 303 EA3 D C10 1 
HETATM 8740 C  C3  . EA3 V 5 .   ? 5.624   9.062   -36.692 1.00 8.50  ? 303 EA3 D C3  1 
HETATM 8741 S  S2  . EA3 V 5 .   ? 6.355   7.486   -36.260 1.00 7.72  ? 303 EA3 D S2  1 
HETATM 8742 O  O4  . EA3 V 5 .   ? 5.200   6.589   -36.132 1.00 7.61  ? 303 EA3 D O4  1 
HETATM 8743 O  O5  . EA3 V 5 .   ? 7.149   7.703   -35.089 1.00 8.01  ? 303 EA3 D O5  1 
HETATM 8744 N  N1  . EA3 V 5 .   ? 7.268   7.059   -37.499 1.00 7.42  ? 303 EA3 D N1  1 
HETATM 8745 C  C8  . EA3 V 5 .   ? 4.278   11.361  -37.367 1.00 9.86  ? 303 EA3 D C8  1 
HETATM 8746 C  C7  . EA3 V 5 .   ? 4.103   10.827  -36.096 1.00 10.77 ? 303 EA3 D C7  1 
HETATM 8747 C  C6  . EA3 V 5 .   ? 4.754   9.672   -35.772 1.00 9.34  ? 303 EA3 D C6  1 
HETATM 8748 CL CL1 . EA3 V 5 .   ? 4.480   9.138   -34.166 1.00 10.00 ? 303 EA3 D CL1 1 
HETATM 8749 S  S18 . EA3 V 5 .   ? 3.466   12.876  -37.921 1.00 15.48 ? 303 EA3 D S18 1 
HETATM 8750 C  C19 . EA3 V 5 .   ? 2.948   13.631  -36.305 1.00 18.15 ? 303 EA3 D C19 1 
HETATM 8751 C  C24 . EA3 V 5 .   ? 1.597   13.049  -35.814 1.00 22.77 ? 303 EA3 D C24 1 
HETATM 8752 C  C23 . EA3 V 5 .   ? 0.497   13.579  -36.698 1.00 24.87 ? 303 EA3 D C23 1 
HETATM 8753 C  C22 . EA3 V 5 .   ? 0.495   15.090  -36.432 1.00 23.17 ? 303 EA3 D C22 1 
HETATM 8754 C  C21 . EA3 V 5 .   ? 1.751   15.638  -37.111 1.00 24.48 ? 303 EA3 D C21 1 
HETATM 8755 C  C20 . EA3 V 5 .   ? 2.921   15.208  -36.240 1.00 25.56 ? 303 EA3 D C20 1 
HETATM 8756 O  O   . HOH W 6 .   ? 15.107  -15.958 15.284  1.00 23.82 ? 401 HOH A O   1 
HETATM 8757 O  O   . HOH W 6 .   ? 5.734   -11.048 -2.042  1.00 39.85 ? 402 HOH A O   1 
HETATM 8758 O  O   . HOH W 6 .   ? 28.394  8.515   17.367  1.00 26.52 ? 403 HOH A O   1 
HETATM 8759 O  O   . HOH W 6 .   ? 33.793  3.710   -7.882  1.00 30.52 ? 404 HOH A O   1 
HETATM 8760 O  O   . HOH W 6 .   ? 32.915  6.887   15.646  1.00 25.15 ? 405 HOH A O   1 
HETATM 8761 O  O   . HOH W 6 .   ? 16.922  -13.643 30.952  1.00 24.08 ? 406 HOH A O   1 
HETATM 8762 O  O   . HOH W 6 .   ? 41.156  -4.448  0.401   1.00 29.07 ? 407 HOH A O   1 
HETATM 8763 O  O   . HOH W 6 .   ? 19.364  -26.211 -3.018  1.00 35.37 ? 408 HOH A O   1 
HETATM 8764 O  O   . HOH W 6 .   ? 34.063  1.323   -5.949  1.00 28.91 ? 409 HOH A O   1 
HETATM 8765 O  O   . HOH W 6 .   ? 8.707   -14.281 13.597  1.00 38.26 ? 410 HOH A O   1 
HETATM 8766 O  O   . HOH W 6 .   ? 41.614  5.817   5.288   1.00 25.38 ? 411 HOH A O   1 
HETATM 8767 O  O   . HOH W 6 .   ? 34.818  -11.242 -3.321  1.00 32.47 ? 412 HOH A O   1 
HETATM 8768 O  O   . HOH W 6 .   ? 6.159   -4.017  -8.087  1.00 42.48 ? 413 HOH A O   1 
HETATM 8769 O  O   . HOH W 6 .   ? 42.383  -0.491  5.637   1.00 29.53 ? 414 HOH A O   1 
HETATM 8770 O  O   . HOH W 6 .   ? 43.778  -4.603  12.858  1.00 23.00 ? 415 HOH A O   1 
HETATM 8771 O  O   . HOH W 6 .   ? 14.487  4.872   24.008  1.00 28.11 ? 416 HOH A O   1 
HETATM 8772 O  O   . HOH W 6 .   ? 37.442  15.635  3.946   1.00 37.88 ? 417 HOH A O   1 
HETATM 8773 O  O   . HOH W 6 .   ? 18.183  -3.194  -5.690  1.00 30.76 ? 418 HOH A O   1 
HETATM 8774 O  O   . HOH W 6 .   ? 19.649  13.864  28.545  1.00 22.97 ? 419 HOH A O   1 
HETATM 8775 O  O   . HOH W 6 .   ? 17.824  7.894   19.508  1.00 30.31 ? 420 HOH A O   1 
HETATM 8776 O  O   . HOH W 6 .   ? 10.873  12.515  20.490  1.00 25.02 ? 421 HOH A O   1 
HETATM 8777 O  O   . HOH W 6 .   ? 17.873  3.163   12.799  1.00 10.12 ? 422 HOH A O   1 
HETATM 8778 O  O   . HOH W 6 .   ? 6.028   -3.433  20.983  1.00 28.64 ? 423 HOH A O   1 
HETATM 8779 O  O   . HOH W 6 .   ? 19.053  -6.522  -11.922 1.00 36.07 ? 424 HOH A O   1 
HETATM 8780 O  O   . HOH W 6 .   ? 45.156  -4.586  7.737   1.00 30.17 ? 425 HOH A O   1 
HETATM 8781 O  O   . HOH W 6 .   ? 19.515  13.416  19.436  1.00 37.70 ? 426 HOH A O   1 
HETATM 8782 O  O   . HOH W 6 .   ? 14.467  -10.065 26.025  1.00 16.38 ? 427 HOH A O   1 
HETATM 8783 O  O   . HOH W 6 .   ? 30.422  13.248  10.126  1.00 37.44 ? 428 HOH A O   1 
HETATM 8784 O  O   . HOH W 6 .   ? 16.805  -18.519 12.717  1.00 35.47 ? 429 HOH A O   1 
HETATM 8785 O  O   . HOH W 6 .   ? 7.736   -8.301  11.883  1.00 24.71 ? 430 HOH A O   1 
HETATM 8786 O  O   . HOH W 6 .   ? 27.847  -21.753 1.942   1.00 28.99 ? 431 HOH A O   1 
HETATM 8787 O  O   . HOH W 6 .   ? 12.054  -17.028 4.889   1.00 34.31 ? 432 HOH A O   1 
HETATM 8788 O  O   . HOH W 6 .   ? 37.322  7.314   29.919  1.00 33.15 ? 433 HOH A O   1 
HETATM 8789 O  O   . HOH W 6 .   ? 42.053  2.453   29.318  1.00 26.82 ? 434 HOH A O   1 
HETATM 8790 O  O   . HOH W 6 .   ? 39.360  -15.845 17.064  1.00 29.28 ? 435 HOH A O   1 
HETATM 8791 O  O   . HOH W 6 .   ? 47.199  -3.646  10.271  1.00 24.66 ? 436 HOH A O   1 
HETATM 8792 O  O   . HOH W 6 .   ? 39.473  4.790   15.003  1.00 31.88 ? 437 HOH A O   1 
HETATM 8793 O  O   . HOH W 6 .   ? 29.603  0.627   -2.880  1.00 28.92 ? 438 HOH A O   1 
HETATM 8794 O  O   . HOH W 6 .   ? 19.475  9.676   32.478  1.00 22.76 ? 439 HOH A O   1 
HETATM 8795 O  O   . HOH W 6 .   ? 17.990  -15.206 6.229   1.00 17.29 ? 440 HOH A O   1 
HETATM 8796 O  O   . HOH W 6 .   ? 42.774  -10.386 19.074  1.00 26.01 ? 441 HOH A O   1 
HETATM 8797 O  O   . HOH W 6 .   ? 30.414  14.331  4.220   1.00 34.57 ? 442 HOH A O   1 
HETATM 8798 O  O   . HOH W 6 .   ? 11.248  3.351   19.297  1.00 19.04 ? 443 HOH A O   1 
HETATM 8799 O  O   . HOH W 6 .   ? 28.012  3.871   33.497  1.00 24.22 ? 444 HOH A O   1 
HETATM 8800 O  O   . HOH W 6 .   ? 26.000  11.063  30.943  1.00 20.62 ? 445 HOH A O   1 
HETATM 8801 O  O   . HOH W 6 .   ? 31.489  5.576   32.492  1.00 28.07 ? 446 HOH A O   1 
HETATM 8802 O  O   . HOH W 6 .   ? 38.718  -5.829  -3.065  1.00 25.45 ? 447 HOH A O   1 
HETATM 8803 O  O   . HOH W 6 .   ? 14.077  1.826   -3.017  1.00 24.49 ? 448 HOH A O   1 
HETATM 8804 O  O   . HOH W 6 .   ? 10.240  4.772   8.749   1.00 10.91 ? 449 HOH A O   1 
HETATM 8805 O  O   . HOH W 6 .   ? 41.055  -10.617 9.806   1.00 17.44 ? 450 HOH A O   1 
HETATM 8806 O  O   . HOH W 6 .   ? 10.564  6.249   15.330  1.00 13.21 ? 451 HOH A O   1 
HETATM 8807 O  O   . HOH W 6 .   ? 13.655  16.392  11.783  1.00 15.14 ? 452 HOH A O   1 
HETATM 8808 O  O   . HOH W 6 .   ? 10.476  -3.391  2.817   1.00 13.38 ? 453 HOH A O   1 
HETATM 8809 O  O   . HOH W 6 .   ? 39.937  -12.239 11.789  1.00 20.26 ? 454 HOH A O   1 
HETATM 8810 O  O   . HOH W 6 .   ? 5.612   -12.076 13.342  1.00 18.28 ? 455 HOH A O   1 
HETATM 8811 O  O   . HOH W 6 .   ? 12.725  -12.374 16.547  1.00 17.69 ? 456 HOH A O   1 
HETATM 8812 O  O   . HOH W 6 .   ? 9.454   -5.161  16.692  1.00 28.06 ? 457 HOH A O   1 
HETATM 8813 O  O   . HOH W 6 .   ? 9.216   11.404  1.080   1.00 15.63 ? 458 HOH A O   1 
HETATM 8814 O  O   . HOH W 6 .   ? 19.321  -18.419 26.123  1.00 25.95 ? 459 HOH A O   1 
HETATM 8815 O  O   . HOH W 6 .   ? 16.019  -12.141 26.879  1.00 18.71 ? 460 HOH A O   1 
HETATM 8816 O  O   . HOH W 6 .   ? 13.912  1.594   -0.239  1.00 17.99 ? 461 HOH A O   1 
HETATM 8817 O  O   . HOH W 6 .   ? 12.582  14.558  2.289   1.00 13.57 ? 462 HOH A O   1 
HETATM 8818 O  O   . HOH W 6 .   ? 39.516  -12.704 20.014  1.00 23.16 ? 463 HOH A O   1 
HETATM 8819 O  O   . HOH W 6 .   ? 15.245  -6.866  21.156  1.00 11.01 ? 464 HOH A O   1 
HETATM 8820 O  O   . HOH W 6 .   ? 36.169  -7.079  26.432  1.00 20.01 ? 465 HOH A O   1 
HETATM 8821 O  O   . HOH W 6 .   ? 4.974   -9.277  25.704  1.00 30.72 ? 466 HOH A O   1 
HETATM 8822 O  O   . HOH W 6 .   ? 28.414  -4.267  2.544   1.00 9.71  ? 467 HOH A O   1 
HETATM 8823 O  O   . HOH W 6 .   ? 32.974  6.763   12.985  1.00 25.64 ? 468 HOH A O   1 
HETATM 8824 O  O   . HOH W 6 .   ? 23.887  -16.034 29.769  1.00 22.95 ? 469 HOH A O   1 
HETATM 8825 O  O   . HOH W 6 .   ? 11.360  5.240   2.194   1.00 10.23 ? 470 HOH A O   1 
HETATM 8826 O  O   . HOH W 6 .   ? 35.970  -14.965 4.175   1.00 30.89 ? 471 HOH A O   1 
HETATM 8827 O  O   . HOH W 6 .   ? 32.866  4.916   20.188  1.00 21.62 ? 472 HOH A O   1 
HETATM 8828 O  O   . HOH W 6 .   ? 11.284  3.819   -0.110  1.00 26.21 ? 473 HOH A O   1 
HETATM 8829 O  O   . HOH W 6 .   ? 34.682  3.575   31.537  1.00 32.70 ? 474 HOH A O   1 
HETATM 8830 O  O   . HOH W 6 .   ? 25.672  -18.496 12.758  1.00 23.26 ? 475 HOH A O   1 
HETATM 8831 O  O   . HOH W 6 .   ? 33.915  -13.427 26.665  1.00 27.40 ? 476 HOH A O   1 
HETATM 8832 O  O   . HOH W 6 .   ? 30.314  -8.932  -2.664  1.00 17.31 ? 477 HOH A O   1 
HETATM 8833 O  O   . HOH W 6 .   ? 29.180  -16.926 14.925  1.00 23.98 ? 478 HOH A O   1 
HETATM 8834 O  O   . HOH W 6 .   ? 12.108  -10.539 27.361  1.00 16.63 ? 479 HOH A O   1 
HETATM 8835 O  O   . HOH W 6 .   ? 12.446  -2.668  11.036  1.00 9.26  ? 480 HOH A O   1 
HETATM 8836 O  O   . HOH W 6 .   ? 38.461  6.287   18.946  1.00 31.08 ? 481 HOH A O   1 
HETATM 8837 O  O   . HOH W 6 .   ? 42.101  2.178   0.890   1.00 14.66 ? 482 HOH A O   1 
HETATM 8838 O  O   . HOH W 6 .   ? 31.326  -13.299 2.424   1.00 22.23 ? 483 HOH A O   1 
HETATM 8839 O  O   . HOH W 6 .   ? 29.713  -15.850 -1.740  1.00 20.65 ? 484 HOH A O   1 
HETATM 8840 O  O   . HOH W 6 .   ? 38.023  -7.625  24.558  1.00 22.36 ? 485 HOH A O   1 
HETATM 8841 O  O   . HOH W 6 .   ? 17.357  0.221   28.582  1.00 18.42 ? 486 HOH A O   1 
HETATM 8842 O  O   . HOH W 6 .   ? 6.342   15.869  15.668  1.00 34.04 ? 487 HOH A O   1 
HETATM 8843 O  O   . HOH W 6 .   ? 37.244  7.812   9.409   1.00 25.33 ? 488 HOH A O   1 
HETATM 8844 O  O   . HOH W 6 .   ? 38.555  3.960   11.362  1.00 18.09 ? 489 HOH A O   1 
HETATM 8845 O  O   . HOH W 6 .   ? 6.765   0.398   -14.058 1.00 38.57 ? 490 HOH A O   1 
HETATM 8846 O  O   . HOH W 6 .   ? 6.797   -9.952  4.325   1.00 27.30 ? 491 HOH A O   1 
HETATM 8847 O  O   . HOH W 6 .   ? 22.525  7.113   -4.214  1.00 31.22 ? 492 HOH A O   1 
HETATM 8848 O  O   . HOH W 6 .   ? 26.085  -18.539 20.598  1.00 17.55 ? 493 HOH A O   1 
HETATM 8849 O  O   . HOH W 6 .   ? 20.891  -4.562  32.662  1.00 32.60 ? 494 HOH A O   1 
HETATM 8850 O  O   . HOH W 6 .   ? 8.659   2.901   7.341   1.00 8.06  ? 495 HOH A O   1 
HETATM 8851 O  O   . HOH W 6 .   ? 33.008  -15.016 3.551   1.00 21.46 ? 496 HOH A O   1 
HETATM 8852 O  O   . HOH W 6 .   ? 45.319  1.453   22.422  1.00 31.58 ? 497 HOH A O   1 
HETATM 8853 O  O   . HOH W 6 .   ? 13.104  14.079  13.951  1.00 20.47 ? 498 HOH A O   1 
HETATM 8854 O  O   . HOH W 6 .   ? 22.538  -19.540 12.339  1.00 31.77 ? 499 HOH A O   1 
HETATM 8855 O  O   . HOH W 6 .   ? 42.142  4.103   12.557  1.00 36.40 ? 500 HOH A O   1 
HETATM 8856 O  O   . HOH W 6 .   ? 17.617  -18.178 4.872   1.00 41.48 ? 501 HOH A O   1 
HETATM 8857 O  O   . HOH W 6 .   ? 10.759  -4.558  -5.459  1.00 36.49 ? 502 HOH A O   1 
HETATM 8858 O  O   . HOH W 6 .   ? 36.680  -4.591  -0.810  1.00 16.27 ? 503 HOH A O   1 
HETATM 8859 O  O   . HOH W 6 .   ? 16.640  10.802  -3.110  1.00 26.89 ? 504 HOH A O   1 
HETATM 8860 O  O   . HOH W 6 .   ? 23.000  -12.398 9.802   1.00 10.66 ? 505 HOH A O   1 
HETATM 8861 O  O   . HOH W 6 .   ? 42.443  5.257   -5.096  1.00 25.45 ? 506 HOH A O   1 
HETATM 8862 O  O   . HOH W 6 .   ? 26.109  -17.930 17.498  1.00 20.22 ? 507 HOH A O   1 
HETATM 8863 O  O   . HOH W 6 .   ? 32.145  -3.233  -5.378  1.00 32.31 ? 508 HOH A O   1 
HETATM 8864 O  O   . HOH W 6 .   ? 26.550  5.208   -3.772  1.00 27.45 ? 509 HOH A O   1 
HETATM 8865 O  O   . HOH W 6 .   ? 7.851   -1.728  15.236  1.00 26.57 ? 510 HOH A O   1 
HETATM 8866 O  O   . HOH W 6 .   ? 37.238  10.344  24.036  1.00 39.79 ? 511 HOH A O   1 
HETATM 8867 O  O   . HOH W 6 .   ? 9.376   -14.385 1.816   1.00 26.78 ? 512 HOH A O   1 
HETATM 8868 O  O   . HOH W 6 .   ? 7.379   -6.691  2.635   1.00 23.27 ? 513 HOH A O   1 
HETATM 8869 O  O   . HOH W 6 .   ? 32.584  -15.958 12.259  1.00 38.86 ? 514 HOH A O   1 
HETATM 8870 O  O   . HOH W 6 .   ? 37.807  10.088  -5.109  1.00 26.16 ? 515 HOH A O   1 
HETATM 8871 O  O   . HOH W 6 .   ? 19.598  -0.621  26.676  1.00 15.99 ? 516 HOH A O   1 
HETATM 8872 O  O   . HOH W 6 .   ? 12.009  2.151   -6.768  1.00 34.32 ? 517 HOH A O   1 
HETATM 8873 O  O   . HOH W 6 .   ? 7.345   4.945   11.217  1.00 10.25 ? 518 HOH A O   1 
HETATM 8874 O  O   . HOH W 6 .   ? 20.758  4.038   16.433  1.00 15.15 ? 519 HOH A O   1 
HETATM 8875 O  O   . HOH W 6 .   ? 24.404  -11.713 30.313  1.00 26.56 ? 520 HOH A O   1 
HETATM 8876 O  O   . HOH W 6 .   ? 20.651  17.779  7.481   1.00 30.83 ? 521 HOH A O   1 
HETATM 8877 O  O   . HOH W 6 .   ? 19.394  14.133  5.080   1.00 11.98 ? 522 HOH A O   1 
HETATM 8878 O  O   . HOH W 6 .   ? 29.089  -15.001 16.991  1.00 18.54 ? 523 HOH A O   1 
HETATM 8879 O  O   . HOH W 6 .   ? 32.356  -16.916 10.207  1.00 30.17 ? 524 HOH A O   1 
HETATM 8880 O  O   . HOH W 6 .   ? 28.404  2.272   -1.349  1.00 23.12 ? 525 HOH A O   1 
HETATM 8881 O  O   . HOH W 6 .   ? 44.763  -1.707  14.646  1.00 30.44 ? 526 HOH A O   1 
HETATM 8882 O  O   . HOH W 6 .   ? 17.283  -3.880  -8.320  1.00 29.88 ? 527 HOH A O   1 
HETATM 8883 O  O   . HOH W 6 .   ? 35.232  -0.951  30.702  1.00 25.45 ? 528 HOH A O   1 
HETATM 8884 O  O   . HOH W 6 .   ? 20.739  -9.841  31.888  1.00 19.34 ? 529 HOH A O   1 
HETATM 8885 O  O   . HOH W 6 .   ? 13.666  -12.538 20.888  1.00 17.49 ? 530 HOH A O   1 
HETATM 8886 O  O   . HOH W 6 .   ? 15.315  -15.712 2.678   1.00 29.64 ? 531 HOH A O   1 
HETATM 8887 O  O   . HOH W 6 .   ? 32.075  -16.919 17.068  1.00 34.76 ? 532 HOH A O   1 
HETATM 8888 O  O   . HOH W 6 .   ? 25.621  4.527   16.502  1.00 20.40 ? 533 HOH A O   1 
HETATM 8889 O  O   . HOH W 6 .   ? 11.960  7.461   8.650   1.00 10.73 ? 534 HOH A O   1 
HETATM 8890 O  O   . HOH W 6 .   ? 11.039  11.170  8.048   1.00 9.70  ? 535 HOH A O   1 
HETATM 8891 O  O   . HOH W 6 .   ? 27.661  -21.304 24.680  1.00 28.08 ? 536 HOH A O   1 
HETATM 8892 O  O   . HOH W 6 .   ? 15.333  -17.367 19.704  1.00 43.12 ? 537 HOH A O   1 
HETATM 8893 O  O   . HOH W 6 .   ? 8.759   -6.476  7.417   1.00 19.19 ? 538 HOH A O   1 
HETATM 8894 O  O   . HOH W 6 .   ? 10.969  -5.143  0.763   1.00 22.56 ? 539 HOH A O   1 
HETATM 8895 O  O   . HOH W 6 .   ? 38.658  12.269  -1.996  1.00 34.60 ? 540 HOH A O   1 
HETATM 8896 O  O   . HOH W 6 .   ? 44.083  -9.927  8.171   1.00 27.24 ? 541 HOH A O   1 
HETATM 8897 O  O   . HOH W 6 .   ? 25.127  13.990  33.218  1.00 34.93 ? 542 HOH A O   1 
HETATM 8898 O  O   . HOH W 6 .   ? 26.280  11.797  6.566   1.00 28.29 ? 543 HOH A O   1 
HETATM 8899 O  O   . HOH W 6 .   ? 23.300  3.182   -2.055  1.00 15.81 ? 544 HOH A O   1 
HETATM 8900 O  O   . HOH W 6 .   ? 28.012  -4.927  31.304  1.00 26.01 ? 545 HOH A O   1 
HETATM 8901 O  O   . HOH W 6 .   ? 17.728  9.543   0.132   1.00 11.07 ? 546 HOH A O   1 
HETATM 8902 O  O   . HOH W 6 .   ? 11.896  -15.418 8.483   1.00 22.30 ? 547 HOH A O   1 
HETATM 8903 O  O   . HOH W 6 .   ? 8.940   3.887   2.708   1.00 13.58 ? 548 HOH A O   1 
HETATM 8904 O  O   . HOH W 6 .   ? 15.606  4.581   21.360  1.00 25.95 ? 549 HOH A O   1 
HETATM 8905 O  O   . HOH W 6 .   ? 20.824  -2.800  -5.230  1.00 21.98 ? 550 HOH A O   1 
HETATM 8906 O  O   . HOH W 6 .   ? 10.206  -4.074  19.552  1.00 21.99 ? 551 HOH A O   1 
HETATM 8907 O  O   . HOH W 6 .   ? 41.993  6.927   2.686   1.00 24.57 ? 552 HOH A O   1 
HETATM 8908 O  O   . HOH W 6 .   ? 8.158   -10.524 26.388  1.00 27.52 ? 553 HOH A O   1 
HETATM 8909 O  O   . HOH W 6 .   ? 17.116  0.647   -0.527  1.00 14.74 ? 554 HOH A O   1 
HETATM 8910 O  O   . HOH W 6 .   ? 31.866  -17.025 20.720  1.00 37.04 ? 555 HOH A O   1 
HETATM 8911 O  O   . HOH W 6 .   ? 9.443   17.023  14.617  1.00 31.06 ? 556 HOH A O   1 
HETATM 8912 O  O   . HOH W 6 .   ? 23.705  -21.547 -3.406  1.00 34.69 ? 557 HOH A O   1 
HETATM 8913 O  O   . HOH W 6 .   ? 8.426   -0.038  24.287  1.00 28.07 ? 558 HOH A O   1 
HETATM 8914 O  O   . HOH W 6 .   ? 18.984  11.795  -0.847  1.00 20.04 ? 559 HOH A O   1 
HETATM 8915 O  O   . HOH W 6 .   ? 18.380  -15.653 34.130  1.00 28.55 ? 560 HOH A O   1 
HETATM 8916 O  O   . HOH W 6 .   ? 17.317  -16.526 -7.953  1.00 31.30 ? 561 HOH A O   1 
HETATM 8917 O  O   . HOH W 6 .   ? 43.381  -9.754  11.455  1.00 24.57 ? 562 HOH A O   1 
HETATM 8918 O  O   . HOH W 6 .   ? 14.238  4.355   -3.997  1.00 20.72 ? 563 HOH A O   1 
HETATM 8919 O  O   . HOH W 6 .   ? 27.263  -5.597  -5.212  1.00 19.46 ? 564 HOH A O   1 
HETATM 8920 O  O   . HOH W 6 .   ? 7.692   9.089   14.125  1.00 14.83 ? 565 HOH A O   1 
HETATM 8921 O  O   . HOH W 6 .   ? 15.178  -14.447 19.373  1.00 15.22 ? 566 HOH A O   1 
HETATM 8922 O  O   . HOH W 6 .   ? 9.656   -2.638  10.412  1.00 20.80 ? 567 HOH A O   1 
HETATM 8923 O  O   . HOH W 6 .   ? 11.449  9.783   -2.131  1.00 24.60 ? 568 HOH A O   1 
HETATM 8924 O  O   . HOH W 6 .   ? 24.140  -21.041 26.771  1.00 30.66 ? 569 HOH A O   1 
HETATM 8925 O  O   . HOH W 6 .   ? 32.877  -0.234  -4.413  1.00 43.46 ? 570 HOH A O   1 
HETATM 8926 O  O   . HOH W 6 .   ? 10.207  3.056   22.292  1.00 30.58 ? 571 HOH A O   1 
HETATM 8927 O  O   . HOH W 6 .   ? 46.110  -9.237  16.854  1.00 35.44 ? 572 HOH A O   1 
HETATM 8928 O  O   . HOH W 6 .   ? 14.587  7.084   21.064  1.00 28.48 ? 573 HOH A O   1 
HETATM 8929 O  O   . HOH W 6 .   ? 32.477  7.567   30.800  1.00 21.62 ? 574 HOH A O   1 
HETATM 8930 O  O   . HOH W 6 .   ? 13.385  5.005   -0.400  1.00 19.46 ? 575 HOH A O   1 
HETATM 8931 O  O   . HOH W 6 .   ? 23.172  12.181  14.642  1.00 26.86 ? 576 HOH A O   1 
HETATM 8932 O  O   . HOH W 6 .   ? 31.222  -20.951 8.699   1.00 28.85 ? 577 HOH A O   1 
HETATM 8933 O  O   . HOH W 6 .   ? 39.796  -11.915 23.131  1.00 37.95 ? 578 HOH A O   1 
HETATM 8934 O  O   . HOH W 6 .   ? 39.185  3.679   19.550  1.00 22.81 ? 579 HOH A O   1 
HETATM 8935 O  O   . HOH W 6 .   ? 11.598  7.975   1.691   1.00 12.23 ? 580 HOH A O   1 
HETATM 8936 O  O   . HOH W 6 .   ? 7.769   -12.795 -1.193  1.00 29.33 ? 581 HOH A O   1 
HETATM 8937 O  O   . HOH W 6 .   ? 36.652  -14.848 -1.741  1.00 38.05 ? 582 HOH A O   1 
HETATM 8938 O  O   . HOH W 6 .   ? 7.909   -7.127  16.942  1.00 23.85 ? 583 HOH A O   1 
HETATM 8939 O  O   . HOH W 6 .   ? 25.591  -16.038 6.634   1.00 12.28 ? 584 HOH A O   1 
HETATM 8940 O  O   . HOH W 6 .   ? 11.529  1.662   -4.140  1.00 31.29 ? 585 HOH A O   1 
HETATM 8941 O  O   . HOH W 6 .   ? 32.160  -18.228 7.146   1.00 30.40 ? 586 HOH A O   1 
HETATM 8942 O  O   . HOH W 6 .   ? 7.419   -2.015  -0.805  1.00 23.47 ? 587 HOH A O   1 
HETATM 8943 O  O   . HOH W 6 .   ? 31.364  -19.074 4.262   1.00 21.68 ? 588 HOH A O   1 
HETATM 8944 O  O   . HOH W 6 .   ? 27.165  -15.945 -5.685  1.00 29.79 ? 589 HOH A O   1 
HETATM 8945 O  O   . HOH W 6 .   ? 12.134  4.859   29.552  1.00 34.62 ? 590 HOH A O   1 
HETATM 8946 O  O   . HOH W 6 .   ? 29.771  10.113  33.744  1.00 27.68 ? 591 HOH A O   1 
HETATM 8947 O  O   . HOH W 6 .   ? 25.243  11.200  -2.652  1.00 37.50 ? 592 HOH A O   1 
HETATM 8948 O  O   . HOH W 6 .   ? 27.434  5.814   35.441  1.00 21.86 ? 593 HOH A O   1 
HETATM 8949 O  O   . HOH W 6 .   ? 24.663  -28.937 -0.907  1.00 27.33 ? 594 HOH A O   1 
HETATM 8950 O  O   . HOH W 6 .   ? 14.601  -17.912 11.448  1.00 39.38 ? 595 HOH A O   1 
HETATM 8951 O  O   . HOH W 6 .   ? 44.914  -4.248  15.528  1.00 29.43 ? 596 HOH A O   1 
HETATM 8952 O  O   . HOH W 6 .   ? 16.185  -0.581  31.192  1.00 37.05 ? 597 HOH A O   1 
HETATM 8953 O  O   . HOH W 6 .   ? 38.049  -13.620 5.831   1.00 25.93 ? 598 HOH A O   1 
HETATM 8954 O  O   . HOH W 6 .   ? 23.986  14.773  4.700   1.00 26.61 ? 599 HOH A O   1 
HETATM 8955 O  O   . HOH W 6 .   ? 7.338   -0.828  8.173   1.00 30.12 ? 600 HOH A O   1 
HETATM 8956 O  O   . HOH W 6 .   ? 29.713  11.755  -4.965  1.00 24.41 ? 601 HOH A O   1 
HETATM 8957 O  O   . HOH W 6 .   ? 9.124   -11.020 14.180  1.00 28.85 ? 602 HOH A O   1 
HETATM 8958 O  O   . HOH W 6 .   ? 36.623  1.399   30.460  1.00 28.66 ? 603 HOH A O   1 
HETATM 8959 O  O   . HOH W 6 .   ? 33.882  16.712  0.585   1.00 44.92 ? 604 HOH A O   1 
HETATM 8960 O  O   . HOH W 6 .   ? 12.434  4.473   22.098  1.00 28.61 ? 605 HOH A O   1 
HETATM 8961 O  O   . HOH W 6 .   ? 19.701  10.885  22.307  1.00 31.82 ? 606 HOH A O   1 
HETATM 8962 O  O   . HOH W 6 .   ? 38.406  -15.540 12.280  1.00 25.94 ? 607 HOH A O   1 
HETATM 8963 O  O   . HOH W 6 .   ? 9.554   -5.401  -1.314  1.00 35.54 ? 608 HOH A O   1 
HETATM 8964 O  O   . HOH W 6 .   ? 28.290  -24.113 8.343   1.00 37.19 ? 609 HOH A O   1 
HETATM 8965 O  O   . HOH W 6 .   ? 24.159  11.887  0.429   1.00 29.65 ? 610 HOH A O   1 
HETATM 8966 O  O   . HOH W 6 .   ? 27.704  7.992   15.260  1.00 31.51 ? 611 HOH A O   1 
HETATM 8967 O  O   . HOH W 6 .   ? 34.014  8.523   19.098  1.00 50.45 ? 612 HOH A O   1 
HETATM 8968 O  O   . HOH W 6 .   ? 26.769  -19.272 -1.265  1.00 34.67 ? 613 HOH A O   1 
HETATM 8969 O  O   . HOH W 6 .   ? 15.124  -13.623 16.787  1.00 13.99 ? 614 HOH A O   1 
HETATM 8970 O  O   . HOH W 6 .   ? 6.221   -2.904  13.310  1.00 19.43 ? 615 HOH A O   1 
HETATM 8971 O  O   . HOH W 6 .   ? 24.429  -7.071  -8.154  1.00 49.35 ? 616 HOH A O   1 
HETATM 8972 O  O   . HOH W 6 .   ? 45.415  -7.127  12.992  1.00 42.00 ? 617 HOH A O   1 
HETATM 8973 O  O   . HOH W 6 .   ? 14.301  -1.974  29.010  1.00 22.82 ? 618 HOH A O   1 
HETATM 8974 O  O   . HOH W 6 .   ? 23.788  -15.319 -11.779 1.00 30.48 ? 619 HOH A O   1 
HETATM 8975 O  O   . HOH W 6 .   ? 7.593   -15.754 7.708   1.00 41.85 ? 620 HOH A O   1 
HETATM 8976 O  O   . HOH W 6 .   ? 35.421  10.206  9.940   1.00 25.78 ? 621 HOH A O   1 
HETATM 8977 O  O   . HOH W 6 .   ? 26.744  13.338  24.625  1.00 33.42 ? 622 HOH A O   1 
HETATM 8978 O  O   . HOH W 6 .   ? 30.570  7.023   13.616  1.00 18.26 ? 623 HOH A O   1 
HETATM 8979 O  O   . HOH W 6 .   ? 15.840  13.908  -0.503  1.00 32.12 ? 624 HOH A O   1 
HETATM 8980 O  O   . HOH W 6 .   ? 17.785  -6.589  33.571  1.00 31.33 ? 625 HOH A O   1 
HETATM 8981 O  O   . HOH W 6 .   ? 20.124  -7.431  32.283  1.00 27.72 ? 626 HOH A O   1 
HETATM 8982 O  O   . HOH W 6 .   ? 41.509  10.360  0.157   1.00 34.53 ? 627 HOH A O   1 
HETATM 8983 O  O   . HOH W 6 .   ? 17.751  -17.002 -3.265  1.00 35.84 ? 628 HOH A O   1 
HETATM 8984 O  O   . HOH W 6 .   ? 11.103  8.608   29.454  1.00 39.76 ? 629 HOH A O   1 
HETATM 8985 O  O   . HOH W 6 .   ? 24.622  -2.914  33.255  1.00 32.06 ? 630 HOH A O   1 
HETATM 8986 O  O   . HOH W 6 .   ? 17.934  5.658   20.779  1.00 24.59 ? 631 HOH A O   1 
HETATM 8987 O  O   . HOH W 6 .   ? 28.803  -18.716 20.667  1.00 21.94 ? 632 HOH A O   1 
HETATM 8988 O  O   . HOH W 6 .   ? 23.122  3.668   15.260  1.00 19.09 ? 633 HOH A O   1 
HETATM 8989 O  O   . HOH W 6 .   ? 9.955   2.743   -7.556  1.00 44.58 ? 634 HOH A O   1 
HETATM 8990 O  O   . HOH W 6 .   ? 40.272  -4.008  -2.043  1.00 26.93 ? 635 HOH A O   1 
HETATM 8991 O  O   . HOH W 6 .   ? 29.513  9.532   14.201  1.00 35.67 ? 636 HOH A O   1 
HETATM 8992 O  O   . HOH W 6 .   ? 39.496  2.899   16.896  1.00 32.40 ? 637 HOH A O   1 
HETATM 8993 O  O   . HOH W 6 .   ? 31.393  -4.295  38.274  1.00 43.40 ? 638 HOH A O   1 
HETATM 8994 O  O   . HOH W 6 .   ? 30.276  -17.663 18.618  1.00 34.65 ? 639 HOH A O   1 
HETATM 8995 O  O   . HOH W 6 .   ? 45.672  1.699   7.933   1.00 33.28 ? 640 HOH A O   1 
HETATM 8996 O  O   . HOH W 6 .   ? 7.189   -5.918  5.314   1.00 32.55 ? 641 HOH A O   1 
HETATM 8997 O  O   . HOH W 6 .   ? 7.940   -3.967  11.944  1.00 32.07 ? 642 HOH A O   1 
HETATM 8998 O  O   . HOH W 6 .   ? 45.430  0.035   5.990   1.00 29.35 ? 643 HOH A O   1 
HETATM 8999 O  O   . HOH W 6 .   ? 16.633  2.203   -7.826  1.00 31.72 ? 644 HOH A O   1 
HETATM 9000 O  O   . HOH W 6 .   ? 9.535   2.899   -2.886  1.00 47.76 ? 645 HOH A O   1 
HETATM 9001 O  O   . HOH W 6 .   ? 36.087  -16.250 13.401  1.00 39.62 ? 646 HOH A O   1 
HETATM 9002 O  O   . HOH W 6 .   ? 27.074  11.351  22.809  1.00 37.34 ? 647 HOH A O   1 
HETATM 9003 O  O   . HOH W 6 .   ? 40.315  8.982   -5.597  1.00 32.59 ? 648 HOH A O   1 
HETATM 9004 O  O   . HOH W 6 .   ? 13.271  13.595  -1.874  1.00 30.98 ? 649 HOH A O   1 
HETATM 9005 O  O   . HOH W 6 .   ? 3.924   13.810  19.592  1.00 31.08 ? 650 HOH A O   1 
HETATM 9006 O  O   . HOH W 6 .   ? 33.538  -17.557 2.978   1.00 29.34 ? 651 HOH A O   1 
HETATM 9007 O  O   . HOH W 6 .   ? 27.067  -18.565 14.824  1.00 41.10 ? 652 HOH A O   1 
HETATM 9008 O  O   . HOH W 6 .   ? 14.693  -12.392 29.487  1.00 20.00 ? 653 HOH A O   1 
HETATM 9009 O  O   . HOH W 6 .   ? 13.790  21.152  11.494  1.00 33.49 ? 654 HOH A O   1 
HETATM 9010 O  O   . HOH W 6 .   ? 29.732  -4.293  -5.246  1.00 47.77 ? 655 HOH A O   1 
HETATM 9011 O  O   . HOH W 6 .   ? 44.240  7.262   -4.488  1.00 36.56 ? 656 HOH A O   1 
HETATM 9012 O  O   . HOH W 6 .   ? 39.526  -9.667  25.031  1.00 41.45 ? 657 HOH A O   1 
HETATM 9013 O  O   . HOH W 6 .   ? 42.365  -13.891 12.104  1.00 39.19 ? 658 HOH A O   1 
HETATM 9014 O  O   . HOH W 6 .   ? 23.550  -10.106 32.495  1.00 26.24 ? 659 HOH A O   1 
HETATM 9015 O  O   . HOH W 6 .   ? 7.840   6.621   15.520  1.00 15.69 ? 660 HOH A O   1 
HETATM 9016 O  O   . HOH W 6 .   ? 23.534  -4.284  -5.522  1.00 37.27 ? 661 HOH A O   1 
HETATM 9017 O  O   . HOH W 6 .   ? 27.037  12.414  9.080   1.00 32.17 ? 662 HOH A O   1 
HETATM 9018 O  O   . HOH W 6 .   ? 51.079  -9.289  27.085  1.00 38.64 ? 663 HOH A O   1 
HETATM 9019 O  O   . HOH W 6 .   ? 6.453   11.866  23.168  1.00 32.63 ? 664 HOH A O   1 
HETATM 9020 O  O   . HOH W 6 .   ? 8.195   -4.974  9.583   1.00 30.13 ? 665 HOH A O   1 
HETATM 9021 O  O   . HOH W 6 .   ? 38.966  -4.517  30.222  1.00 34.22 ? 666 HOH A O   1 
HETATM 9022 O  O   . HOH W 6 .   ? 27.281  -28.266 -1.295  1.00 35.66 ? 667 HOH A O   1 
HETATM 9023 O  O   . HOH W 6 .   ? 33.712  9.461   11.869  1.00 35.58 ? 668 HOH A O   1 
HETATM 9024 O  O   . HOH W 6 .   ? 30.085  -18.263 -2.688  1.00 30.28 ? 669 HOH A O   1 
HETATM 9025 O  O   . HOH W 6 .   ? 16.225  -16.330 8.128   1.00 32.26 ? 670 HOH A O   1 
HETATM 9026 O  O   . HOH W 6 .   ? 32.573  -15.030 28.323  1.00 33.66 ? 671 HOH A O   1 
HETATM 9027 O  O   . HOH W 6 .   ? 25.209  -13.983 30.993  1.00 36.99 ? 672 HOH A O   1 
HETATM 9028 O  O   . HOH W 6 .   ? 24.901  -5.323  31.780  1.00 32.96 ? 673 HOH A O   1 
HETATM 9029 O  O   . HOH W 6 .   ? 38.208  15.274  0.775   1.00 39.72 ? 674 HOH A O   1 
HETATM 9030 O  O   . HOH W 6 .   ? 21.368  16.057  5.288   1.00 24.20 ? 675 HOH A O   1 
HETATM 9031 O  O   . HOH W 6 .   ? 11.568  -13.060 25.852  1.00 25.58 ? 676 HOH A O   1 
HETATM 9032 O  O   . HOH W 6 .   ? 36.674  13.721  -1.056  1.00 31.24 ? 677 HOH A O   1 
HETATM 9033 O  O   . HOH W 6 .   ? 4.294   13.675  22.406  1.00 31.98 ? 678 HOH A O   1 
HETATM 9034 O  O   . HOH W 6 .   ? 14.389  -14.873 23.114  1.00 31.16 ? 679 HOH A O   1 
HETATM 9035 O  O   . HOH W 6 .   ? 16.001  4.608   -6.722  1.00 31.04 ? 680 HOH A O   1 
HETATM 9036 O  O   . HOH W 6 .   ? 13.848  -12.794 23.839  1.00 28.93 ? 681 HOH A O   1 
HETATM 9037 O  O   . HOH W 6 .   ? 21.081  11.801  -2.722  1.00 32.70 ? 682 HOH A O   1 
HETATM 9038 O  O   . HOH W 6 .   ? 25.185  -18.332 30.263  1.00 45.99 ? 683 HOH A O   1 
HETATM 9039 O  O   . HOH W 6 .   ? 13.607  -17.120 7.667   1.00 31.53 ? 684 HOH A O   1 
HETATM 9040 O  O   . HOH W 6 .   ? 39.288  -8.126  27.701  1.00 44.81 ? 685 HOH A O   1 
HETATM 9041 O  O   . HOH W 6 .   ? 22.669  16.312  8.238   1.00 42.50 ? 686 HOH A O   1 
HETATM 9042 O  O   . HOH W 6 .   ? 19.303  10.308  -4.374  1.00 27.09 ? 687 HOH A O   1 
HETATM 9043 O  O   . HOH W 6 .   ? 24.208  16.062  6.646   1.00 39.57 ? 688 HOH A O   1 
HETATM 9044 O  O   . HOH W 6 .   ? 31.426  -20.239 -1.416  1.00 37.58 ? 689 HOH A O   1 
HETATM 9045 O  O   . HOH X 6 .   ? -0.844  17.976  0.482   1.00 36.55 ? 401 HOH B O   1 
HETATM 9046 O  O   . HOH X 6 .   ? 1.828   6.539   20.639  1.00 31.58 ? 402 HOH B O   1 
HETATM 9047 O  O   . HOH X 6 .   ? -0.081  16.468  -11.167 1.00 31.60 ? 403 HOH B O   1 
HETATM 9048 O  O   . HOH X 6 .   ? -17.265 11.118  4.418   1.00 32.54 ? 404 HOH B O   1 
HETATM 9049 O  O   . HOH X 6 .   ? -27.906 7.027   19.688  1.00 47.16 ? 405 HOH B O   1 
HETATM 9050 O  O   . HOH X 6 .   ? -27.446 3.544   -10.407 1.00 39.56 ? 406 HOH B O   1 
HETATM 9051 O  O   . HOH X 6 .   ? -19.686 -7.752  -11.665 1.00 33.48 ? 407 HOH B O   1 
HETATM 9052 O  O   . HOH X 6 .   ? 3.538   18.218  -15.702 1.00 40.24 ? 408 HOH B O   1 
HETATM 9053 O  O   . HOH X 6 .   ? -17.184 11.225  1.695   1.00 33.40 ? 409 HOH B O   1 
HETATM 9054 O  O   . HOH X 6 .   ? -18.464 8.261   -13.766 1.00 30.23 ? 410 HOH B O   1 
HETATM 9055 O  O   . HOH X 6 .   ? 8.976   16.570  0.846   1.00 18.04 ? 411 HOH B O   1 
HETATM 9056 O  O   . HOH X 6 .   ? -17.535 19.780  10.185  1.00 48.65 ? 412 HOH B O   1 
HETATM 9057 O  O   . HOH X 6 .   ? -3.908  -17.855 22.473  1.00 20.72 ? 413 HOH B O   1 
HETATM 9058 O  O   . HOH X 6 .   ? -16.940 -0.106  23.599  1.00 37.42 ? 414 HOH B O   1 
HETATM 9059 O  O   . HOH X 6 .   ? -27.084 -10.055 1.718   1.00 24.05 ? 415 HOH B O   1 
HETATM 9060 O  O   . HOH X 6 .   ? -12.110 -17.515 13.278  1.00 29.55 ? 416 HOH B O   1 
HETATM 9061 O  O   . HOH X 6 .   ? -29.324 2.416   5.899   1.00 19.84 ? 417 HOH B O   1 
HETATM 9062 O  O   . HOH X 6 .   ? -4.008  16.039  -11.277 1.00 18.11 ? 418 HOH B O   1 
HETATM 9063 O  O   . HOH X 6 .   ? -32.952 -1.679  -8.440  1.00 25.29 ? 419 HOH B O   1 
HETATM 9064 O  O   . HOH X 6 .   ? -30.570 1.958   10.506  1.00 31.07 ? 420 HOH B O   1 
HETATM 9065 O  O   . HOH X 6 .   ? -13.840 -15.094 28.486  1.00 23.84 ? 421 HOH B O   1 
HETATM 9066 O  O   . HOH X 6 .   ? 7.180   -11.472 24.148  1.00 27.74 ? 422 HOH B O   1 
HETATM 9067 O  O   . HOH X 6 .   ? -16.694 -16.899 16.573  1.00 32.75 ? 423 HOH B O   1 
HETATM 9068 O  O   . HOH X 6 .   ? -5.727  -11.596 -14.946 1.00 28.67 ? 424 HOH B O   1 
HETATM 9069 O  O   . HOH X 6 .   ? 1.983   6.066   -8.789  1.00 34.65 ? 425 HOH B O   1 
HETATM 9070 O  O   . HOH X 6 .   ? -3.260  2.615   21.187  1.00 25.51 ? 426 HOH B O   1 
HETATM 9071 O  O   . HOH X 6 .   ? -2.646  5.129   4.050   1.00 9.39  ? 427 HOH B O   1 
HETATM 9072 O  O   . HOH X 6 .   ? -29.887 -4.673  -0.642  1.00 19.25 ? 428 HOH B O   1 
HETATM 9073 O  O   . HOH X 6 .   ? -27.552 -4.287  8.707   1.00 17.33 ? 429 HOH B O   1 
HETATM 9074 O  O   . HOH X 6 .   ? -15.484 16.217  -8.304  1.00 27.84 ? 430 HOH B O   1 
HETATM 9075 O  O   . HOH X 6 .   ? -3.671  19.012  -20.155 1.00 27.34 ? 431 HOH B O   1 
HETATM 9076 O  O   . HOH X 6 .   ? -21.349 -9.950  9.721   1.00 42.25 ? 432 HOH B O   1 
HETATM 9077 O  O   . HOH X 6 .   ? 5.854   -9.449  13.553  1.00 16.52 ? 433 HOH B O   1 
HETATM 9078 O  O   . HOH X 6 .   ? 1.541   14.271  -11.437 1.00 27.28 ? 434 HOH B O   1 
HETATM 9079 O  O   . HOH X 6 .   ? -12.709 17.394  6.458   1.00 40.45 ? 435 HOH B O   1 
HETATM 9080 O  O   . HOH X 6 .   ? 5.223   6.329   1.030   1.00 11.60 ? 436 HOH B O   1 
HETATM 9081 O  O   . HOH X 6 .   ? -3.141  -13.024 15.412  1.00 27.88 ? 437 HOH B O   1 
HETATM 9082 O  O   . HOH X 6 .   ? 5.848   12.257  -4.322  1.00 18.23 ? 438 HOH B O   1 
HETATM 9083 O  O   . HOH X 6 .   ? -20.177 -11.935 0.807   1.00 33.11 ? 439 HOH B O   1 
HETATM 9084 O  O   . HOH X 6 .   ? -7.387  -7.596  28.462  1.00 35.99 ? 440 HOH B O   1 
HETATM 9085 O  O   . HOH X 6 .   ? -13.884 0.275   15.157  1.00 10.66 ? 441 HOH B O   1 
HETATM 9086 O  O   . HOH X 6 .   ? -13.471 7.396   -15.651 1.00 19.44 ? 442 HOH B O   1 
HETATM 9087 O  O   . HOH X 6 .   ? -17.547 13.142  -4.105  1.00 28.51 ? 443 HOH B O   1 
HETATM 9088 O  O   . HOH X 6 .   ? -4.295  -19.499 18.289  1.00 36.98 ? 444 HOH B O   1 
HETATM 9089 O  O   . HOH X 6 .   ? -21.169 11.464  6.222   1.00 24.30 ? 445 HOH B O   1 
HETATM 9090 O  O   . HOH X 6 .   ? -5.786  -12.646 11.864  1.00 16.57 ? 446 HOH B O   1 
HETATM 9091 O  O   . HOH X 6 .   ? 4.685   -5.926  8.928   1.00 23.14 ? 447 HOH B O   1 
HETATM 9092 O  O   . HOH X 6 .   ? -21.818 1.499   18.723  1.00 22.97 ? 448 HOH B O   1 
HETATM 9093 O  O   . HOH X 6 .   ? -17.788 9.107   -2.695  1.00 18.88 ? 449 HOH B O   1 
HETATM 9094 O  O   . HOH X 6 .   ? -21.602 -2.455  -12.715 1.00 28.13 ? 450 HOH B O   1 
HETATM 9095 O  O   . HOH X 6 .   ? -25.238 3.104   -11.429 1.00 28.98 ? 451 HOH B O   1 
HETATM 9096 O  O   . HOH X 6 .   ? 2.735   -13.355 15.897  1.00 19.61 ? 452 HOH B O   1 
HETATM 9097 O  O   . HOH X 6 .   ? 3.735   -2.117  22.686  1.00 22.93 ? 453 HOH B O   1 
HETATM 9098 O  O   . HOH X 6 .   ? -20.150 -11.977 8.197   1.00 28.89 ? 454 HOH B O   1 
HETATM 9099 O  O   . HOH X 6 .   ? -21.706 -8.822  -8.487  1.00 17.16 ? 455 HOH B O   1 
HETATM 9100 O  O   . HOH X 6 .   ? 4.127   12.959  -18.476 1.00 38.32 ? 456 HOH B O   1 
HETATM 9101 O  O   . HOH X 6 .   ? -20.104 -12.281 -2.263  1.00 28.05 ? 457 HOH B O   1 
HETATM 9102 O  O   . HOH X 6 .   ? -13.967 -14.786 5.969   1.00 17.70 ? 458 HOH B O   1 
HETATM 9103 O  O   . HOH X 6 .   ? -12.712 -9.198  -12.526 1.00 27.13 ? 459 HOH B O   1 
HETATM 9104 O  O   . HOH X 6 .   ? -0.470  -0.096  26.725  1.00 35.69 ? 460 HOH B O   1 
HETATM 9105 O  O   . HOH X 6 .   ? 4.437   6.425   14.150  1.00 11.71 ? 461 HOH B O   1 
HETATM 9106 O  O   . HOH X 6 .   ? 3.748   3.431   -2.478  1.00 16.35 ? 462 HOH B O   1 
HETATM 9107 O  O   . HOH X 6 .   ? 9.136   7.118   8.430   1.00 15.21 ? 463 HOH B O   1 
HETATM 9108 O  O   . HOH X 6 .   ? 1.795   17.017  0.146   1.00 36.93 ? 464 HOH B O   1 
HETATM 9109 O  O   . HOH X 6 .   ? 3.723   -2.154  13.889  1.00 13.96 ? 465 HOH B O   1 
HETATM 9110 O  O   . HOH X 6 .   ? -26.596 -7.188  -1.610  1.00 19.93 ? 466 HOH B O   1 
HETATM 9111 O  O   . HOH X 6 .   ? 5.355   5.455   7.688   1.00 11.51 ? 467 HOH B O   1 
HETATM 9112 O  O   . HOH X 6 .   ? 3.022   15.320  -5.118  1.00 35.68 ? 468 HOH B O   1 
HETATM 9113 O  O   . HOH X 6 .   ? 9.186   6.952   -2.116  1.00 35.41 ? 469 HOH B O   1 
HETATM 9114 O  O   . HOH X 6 .   ? -24.606 -2.534  -6.542  1.00 16.34 ? 470 HOH B O   1 
HETATM 9115 O  O   . HOH X 6 .   ? 7.901   11.773  14.739  1.00 18.79 ? 471 HOH B O   1 
HETATM 9116 O  O   . HOH X 6 .   ? 3.161   5.331   16.256  1.00 19.77 ? 472 HOH B O   1 
HETATM 9117 O  O   . HOH X 6 .   ? -2.877  -5.421  -4.184  1.00 11.25 ? 473 HOH B O   1 
HETATM 9118 O  O   . HOH X 6 .   ? 4.734   16.942  3.302   1.00 27.63 ? 474 HOH B O   1 
HETATM 9119 O  O   . HOH X 6 .   ? -17.439 -12.610 3.434   1.00 22.74 ? 475 HOH B O   1 
HETATM 9120 O  O   . HOH X 6 .   ? -26.282 8.921   16.602  1.00 32.82 ? 476 HOH B O   1 
HETATM 9121 O  O   . HOH X 6 .   ? -26.587 9.024   -2.914  1.00 28.86 ? 477 HOH B O   1 
HETATM 9122 O  O   . HOH X 6 .   ? -7.898  17.744  11.127  1.00 33.12 ? 478 HOH B O   1 
HETATM 9123 O  O   . HOH X 6 .   ? -5.548  1.544   -9.827  1.00 12.02 ? 479 HOH B O   1 
HETATM 9124 O  O   . HOH X 6 .   ? -12.229 -13.656 -11.277 1.00 16.56 ? 480 HOH B O   1 
HETATM 9125 O  O   . HOH X 6 .   ? 1.176   12.977  19.439  1.00 31.33 ? 481 HOH B O   1 
HETATM 9126 O  O   . HOH X 6 .   ? -20.988 -4.992  21.994  1.00 24.24 ? 482 HOH B O   1 
HETATM 9127 O  O   . HOH X 6 .   ? -14.588 -13.501 24.069  1.00 25.93 ? 483 HOH B O   1 
HETATM 9128 O  O   . HOH X 6 .   ? -20.767 -11.288 5.556   1.00 32.84 ? 484 HOH B O   1 
HETATM 9129 O  O   . HOH X 6 .   ? 1.175   18.007  -13.954 1.00 33.31 ? 485 HOH B O   1 
HETATM 9130 O  O   . HOH X 6 .   ? -15.949 -0.464  -14.988 1.00 20.66 ? 486 HOH B O   1 
HETATM 9131 O  O   . HOH X 6 .   ? -7.765  -15.624 -7.840  1.00 10.90 ? 487 HOH B O   1 
HETATM 9132 O  O   . HOH X 6 .   ? 6.978   -11.549 17.349  1.00 25.74 ? 488 HOH B O   1 
HETATM 9133 O  O   . HOH X 6 .   ? -1.602  16.562  11.041  1.00 12.34 ? 489 HOH B O   1 
HETATM 9134 O  O   . HOH X 6 .   ? -16.445 -12.300 25.799  1.00 24.31 ? 490 HOH B O   1 
HETATM 9135 O  O   . HOH X 6 .   ? -3.937  12.542  -18.243 1.00 20.92 ? 491 HOH B O   1 
HETATM 9136 O  O   . HOH X 6 .   ? -4.536  11.258  -15.016 1.00 18.43 ? 492 HOH B O   1 
HETATM 9137 O  O   . HOH X 6 .   ? 5.011   -9.683  -12.475 1.00 29.48 ? 493 HOH B O   1 
HETATM 9138 O  O   . HOH X 6 .   ? -20.377 -9.512  15.027  1.00 18.82 ? 494 HOH B O   1 
HETATM 9139 O  O   . HOH X 6 .   ? -11.080 15.172  21.949  1.00 37.54 ? 495 HOH B O   1 
HETATM 9140 O  O   . HOH X 6 .   ? -18.426 -8.185  16.088  1.00 17.25 ? 496 HOH B O   1 
HETATM 9141 O  O   . HOH X 6 .   ? -16.379 5.114   21.980  1.00 37.03 ? 497 HOH B O   1 
HETATM 9142 O  O   . HOH X 6 .   ? -22.909 -2.276  -8.728  1.00 15.10 ? 498 HOH B O   1 
HETATM 9143 O  O   . HOH X 6 .   ? -26.976 -6.292  6.700   1.00 16.34 ? 499 HOH B O   1 
HETATM 9144 O  O   . HOH X 6 .   ? 4.221   -14.935 10.093  1.00 35.72 ? 500 HOH B O   1 
HETATM 9145 O  O   . HOH X 6 .   ? -23.095 9.484   6.429   1.00 17.68 ? 501 HOH B O   1 
HETATM 9146 O  O   . HOH X 6 .   ? -23.974 0.839   20.977  1.00 27.87 ? 502 HOH B O   1 
HETATM 9147 O  O   . HOH X 6 .   ? 5.391   19.855  10.764  1.00 20.34 ? 503 HOH B O   1 
HETATM 9148 O  O   . HOH X 6 .   ? 6.624   3.264   9.161   1.00 8.11  ? 504 HOH B O   1 
HETATM 9149 O  O   . HOH X 6 .   ? -17.628 -16.631 -6.370  1.00 25.66 ? 505 HOH B O   1 
HETATM 9150 O  O   . HOH X 6 .   ? -5.723  11.113  20.696  1.00 31.71 ? 506 HOH B O   1 
HETATM 9151 O  O   . HOH X 6 .   ? 4.125   -6.290  24.888  1.00 31.48 ? 507 HOH B O   1 
HETATM 9152 O  O   . HOH X 6 .   ? 5.265   15.984  13.499  1.00 25.46 ? 508 HOH B O   1 
HETATM 9153 O  O   . HOH X 6 .   ? -5.496  6.459   0.458   1.00 13.12 ? 509 HOH B O   1 
HETATM 9154 O  O   . HOH X 6 .   ? -29.050 -6.650  -2.389  1.00 38.51 ? 510 HOH B O   1 
HETATM 9155 O  O   . HOH X 6 .   ? 1.716   -1.628  5.819   1.00 9.44  ? 511 HOH B O   1 
HETATM 9156 O  O   . HOH X 6 .   ? -16.927 -10.843 1.277   1.00 14.03 ? 512 HOH B O   1 
HETATM 9157 O  O   . HOH X 6 .   ? -31.861 5.246   -7.564  1.00 18.82 ? 513 HOH B O   1 
HETATM 9158 O  O   . HOH X 6 .   ? -1.769  20.548  8.282   1.00 29.24 ? 514 HOH B O   1 
HETATM 9159 O  O   . HOH X 6 .   ? 8.124   4.582   5.157   1.00 10.03 ? 515 HOH B O   1 
HETATM 9160 O  O   . HOH X 6 .   ? -10.239 -9.002  8.233   1.00 8.74  ? 516 HOH B O   1 
HETATM 9161 O  O   . HOH X 6 .   ? -8.956  -7.960  -14.461 1.00 16.09 ? 517 HOH B O   1 
HETATM 9162 O  O   . HOH X 6 .   ? 6.009   11.669  7.885   1.00 10.30 ? 518 HOH B O   1 
HETATM 9163 O  O   . HOH X 6 .   ? -1.939  9.446   -3.017  1.00 24.83 ? 519 HOH B O   1 
HETATM 9164 O  O   . HOH X 6 .   ? 2.226   4.984   -5.592  1.00 27.02 ? 520 HOH B O   1 
HETATM 9165 O  O   . HOH X 6 .   ? -16.957 -10.441 20.295  1.00 14.79 ? 521 HOH B O   1 
HETATM 9166 O  O   . HOH X 6 .   ? -3.428  -8.642  -9.209  1.00 27.30 ? 522 HOH B O   1 
HETATM 9167 O  O   . HOH X 6 .   ? -1.876  -11.489 -3.144  1.00 17.64 ? 523 HOH B O   1 
HETATM 9168 O  O   . HOH X 6 .   ? -6.248  -18.336 -2.093  1.00 29.63 ? 524 HOH B O   1 
HETATM 9169 O  O   . HOH X 6 .   ? 6.138   7.260   17.381  1.00 34.21 ? 525 HOH B O   1 
HETATM 9170 O  O   . HOH X 6 .   ? -2.061  -12.708 24.584  1.00 32.01 ? 526 HOH B O   1 
HETATM 9171 O  O   . HOH X 6 .   ? -27.409 6.760   -11.801 1.00 22.39 ? 527 HOH B O   1 
HETATM 9172 O  O   . HOH X 6 .   ? -12.452 12.350  -0.151  1.00 24.57 ? 528 HOH B O   1 
HETATM 9173 O  O   . HOH X 6 .   ? -17.771 -10.127 28.817  1.00 27.12 ? 529 HOH B O   1 
HETATM 9174 O  O   . HOH X 6 .   ? 6.548   0.539   22.160  1.00 29.84 ? 530 HOH B O   1 
HETATM 9175 O  O   . HOH X 6 .   ? -3.580  2.173   -11.996 1.00 16.61 ? 531 HOH B O   1 
HETATM 9176 O  O   . HOH X 6 .   ? -1.369  14.537  17.005  1.00 20.66 ? 532 HOH B O   1 
HETATM 9177 O  O   . HOH X 6 .   ? 1.361   -0.190  -12.493 1.00 32.46 ? 533 HOH B O   1 
HETATM 9178 O  O   . HOH X 6 .   ? -0.947  5.761   -4.774  1.00 21.69 ? 534 HOH B O   1 
HETATM 9179 O  O   . HOH X 6 .   ? -10.479 14.274  -13.599 1.00 17.31 ? 535 HOH B O   1 
HETATM 9180 O  O   . HOH X 6 .   ? -8.001  12.493  5.198   1.00 35.29 ? 536 HOH B O   1 
HETATM 9181 O  O   . HOH X 6 .   ? -14.332 -2.284  -13.725 1.00 27.11 ? 537 HOH B O   1 
HETATM 9182 O  O   . HOH X 6 .   ? -1.233  -0.604  -12.749 1.00 19.83 ? 538 HOH B O   1 
HETATM 9183 O  O   . HOH X 6 .   ? 5.569   -8.228  -1.473  1.00 30.91 ? 539 HOH B O   1 
HETATM 9184 O  O   . HOH X 6 .   ? -10.285 7.564   0.822   1.00 18.71 ? 540 HOH B O   1 
HETATM 9185 O  O   . HOH X 6 .   ? -16.811 6.250   -18.125 1.00 33.19 ? 541 HOH B O   1 
HETATM 9186 O  O   . HOH X 6 .   ? -0.713  4.011   -16.994 1.00 27.34 ? 542 HOH B O   1 
HETATM 9187 O  O   . HOH X 6 .   ? -19.292 -0.753  -16.305 1.00 25.71 ? 543 HOH B O   1 
HETATM 9188 O  O   . HOH X 6 .   ? 4.928   9.168   14.388  1.00 13.68 ? 544 HOH B O   1 
HETATM 9189 O  O   . HOH X 6 .   ? -19.703 -16.002 10.278  1.00 27.93 ? 545 HOH B O   1 
HETATM 9190 O  O   . HOH X 6 .   ? -4.587  0.286   21.810  1.00 19.26 ? 546 HOH B O   1 
HETATM 9191 O  O   . HOH X 6 .   ? -10.430 -10.499 29.736  1.00 22.62 ? 547 HOH B O   1 
HETATM 9192 O  O   . HOH X 6 .   ? -6.419  -11.551 29.164  1.00 29.87 ? 548 HOH B O   1 
HETATM 9193 O  O   . HOH X 6 .   ? -11.028 -17.740 21.053  1.00 40.50 ? 549 HOH B O   1 
HETATM 9194 O  O   . HOH X 6 .   ? -14.501 -14.414 19.920  1.00 33.21 ? 550 HOH B O   1 
HETATM 9195 O  O   . HOH X 6 .   ? -1.383  -6.814  30.967  1.00 37.77 ? 551 HOH B O   1 
HETATM 9196 O  O   . HOH X 6 .   ? -0.288  -13.282 22.513  1.00 30.68 ? 552 HOH B O   1 
HETATM 9197 O  O   . HOH X 6 .   ? -5.920  2.440   -16.950 1.00 27.16 ? 553 HOH B O   1 
HETATM 9198 O  O   . HOH X 6 .   ? 0.134   -13.973 8.723   1.00 38.50 ? 554 HOH B O   1 
HETATM 9199 O  O   . HOH X 6 .   ? -25.417 -7.351  13.034  1.00 29.98 ? 555 HOH B O   1 
HETATM 9200 O  O   . HOH X 6 .   ? -20.589 13.495  8.036   1.00 26.86 ? 556 HOH B O   1 
HETATM 9201 O  O   . HOH X 6 .   ? -31.976 -6.627  6.011   1.00 24.35 ? 557 HOH B O   1 
HETATM 9202 O  O   . HOH X 6 .   ? -29.241 7.134   -1.817  1.00 28.01 ? 558 HOH B O   1 
HETATM 9203 O  O   . HOH X 6 .   ? -6.076  -16.669 5.444   1.00 27.05 ? 559 HOH B O   1 
HETATM 9204 O  O   . HOH X 6 .   ? -0.660  11.934  16.191  1.00 13.79 ? 560 HOH B O   1 
HETATM 9205 O  O   . HOH X 6 .   ? -8.731  8.548   20.024  1.00 41.68 ? 561 HOH B O   1 
HETATM 9206 O  O   . HOH X 6 .   ? 6.061   -6.118  14.640  1.00 27.62 ? 562 HOH B O   1 
HETATM 9207 O  O   . HOH X 6 .   ? -31.039 1.953   1.872   1.00 23.37 ? 563 HOH B O   1 
HETATM 9208 O  O   . HOH X 6 .   ? -7.233  6.920   19.057  1.00 25.61 ? 564 HOH B O   1 
HETATM 9209 O  O   . HOH X 6 .   ? 2.296   6.122   -12.525 1.00 30.76 ? 565 HOH B O   1 
HETATM 9210 O  O   . HOH X 6 .   ? -5.823  -15.268 13.350  1.00 27.39 ? 566 HOH B O   1 
HETATM 9211 O  O   . HOH X 6 .   ? 4.187   8.185   7.688   1.00 9.66  ? 567 HOH B O   1 
HETATM 9212 O  O   . HOH X 6 .   ? 3.591   -11.418 3.410   1.00 36.77 ? 568 HOH B O   1 
HETATM 9213 O  O   . HOH X 6 .   ? -29.853 -3.163  7.100   1.00 21.58 ? 569 HOH B O   1 
HETATM 9214 O  O   . HOH X 6 .   ? 6.543   4.792   13.752  1.00 11.39 ? 570 HOH B O   1 
HETATM 9215 O  O   . HOH X 6 .   ? -11.861 11.358  1.805   1.00 34.00 ? 571 HOH B O   1 
HETATM 9216 O  O   . HOH X 6 .   ? -13.333 -12.075 11.719  1.00 10.34 ? 572 HOH B O   1 
HETATM 9217 O  O   . HOH X 6 .   ? 3.931   -16.031 18.245  1.00 38.46 ? 573 HOH B O   1 
HETATM 9218 O  O   . HOH X 6 .   ? 4.355   -2.096  6.522   1.00 14.26 ? 574 HOH B O   1 
HETATM 9219 O  O   . HOH X 6 .   ? 8.706   8.769   1.932   1.00 17.56 ? 575 HOH B O   1 
HETATM 9220 O  O   . HOH X 6 .   ? -6.203  14.542  1.674   1.00 37.74 ? 576 HOH B O   1 
HETATM 9221 O  O   . HOH X 6 .   ? -26.099 -9.715  6.097   1.00 25.88 ? 577 HOH B O   1 
HETATM 9222 O  O   . HOH X 6 .   ? -26.520 10.273  5.122   1.00 29.58 ? 578 HOH B O   1 
HETATM 9223 O  O   . HOH X 6 .   ? 6.982   -1.021  17.787  1.00 23.78 ? 579 HOH B O   1 
HETATM 9224 O  O   . HOH X 6 .   ? 4.367   3.206   -5.867  1.00 24.22 ? 580 HOH B O   1 
HETATM 9225 O  O   . HOH X 6 .   ? -14.556 -14.119 0.727   1.00 16.37 ? 581 HOH B O   1 
HETATM 9226 O  O   . HOH X 6 .   ? -30.742 7.082   -4.355  1.00 23.67 ? 582 HOH B O   1 
HETATM 9227 O  O   . HOH X 6 .   ? -16.631 2.455   22.443  1.00 41.19 ? 583 HOH B O   1 
HETATM 9228 O  O   . HOH X 6 .   ? -12.475 -0.547  22.751  1.00 19.32 ? 584 HOH B O   1 
HETATM 9229 O  O   . HOH X 6 .   ? -24.110 8.862   -1.759  1.00 18.45 ? 585 HOH B O   1 
HETATM 9230 O  O   . HOH X 6 .   ? -32.401 -4.151  -2.008  1.00 24.82 ? 586 HOH B O   1 
HETATM 9231 O  O   . HOH X 6 .   ? -17.636 -3.722  26.938  1.00 31.26 ? 587 HOH B O   1 
HETATM 9232 O  O   . HOH X 6 .   ? -17.548 12.629  -12.605 1.00 27.67 ? 588 HOH B O   1 
HETATM 9233 O  O   . HOH X 6 .   ? -2.702  -0.238  25.147  1.00 22.24 ? 589 HOH B O   1 
HETATM 9234 O  O   . HOH X 6 .   ? 4.113   -9.299  3.012   1.00 20.95 ? 590 HOH B O   1 
HETATM 9235 O  O   . HOH X 6 .   ? -23.297 -9.068  14.135  1.00 35.26 ? 591 HOH B O   1 
HETATM 9236 O  O   . HOH X 6 .   ? -2.766  1.481   -14.573 1.00 27.51 ? 592 HOH B O   1 
HETATM 9237 O  O   . HOH X 6 .   ? 11.461  14.495  -0.054  1.00 33.19 ? 593 HOH B O   1 
HETATM 9238 O  O   . HOH X 6 .   ? -4.808  -12.941 22.165  1.00 31.08 ? 594 HOH B O   1 
HETATM 9239 O  O   . HOH X 6 .   ? -3.971  13.215  -5.362  1.00 25.61 ? 595 HOH B O   1 
HETATM 9240 O  O   . HOH X 6 .   ? 0.700   7.946   -4.571  1.00 20.39 ? 596 HOH B O   1 
HETATM 9241 O  O   . HOH X 6 .   ? -14.210 -10.944 23.952  1.00 22.35 ? 597 HOH B O   1 
HETATM 9242 O  O   . HOH X 6 .   ? -10.014 12.779  25.518  1.00 38.87 ? 598 HOH B O   1 
HETATM 9243 O  O   . HOH X 6 .   ? 5.935   -2.397  1.761   1.00 24.61 ? 599 HOH B O   1 
HETATM 9244 O  O   . HOH X 6 .   ? 3.590   15.145  1.641   1.00 30.20 ? 600 HOH B O   1 
HETATM 9245 O  O   . HOH X 6 .   ? -29.515 8.199   6.198   1.00 35.41 ? 601 HOH B O   1 
HETATM 9246 O  O   . HOH X 6 .   ? -23.043 7.153   -12.514 1.00 24.36 ? 602 HOH B O   1 
HETATM 9247 O  O   . HOH X 6 .   ? -24.553 -10.847 -5.190  1.00 47.33 ? 603 HOH B O   1 
HETATM 9248 O  O   . HOH X 6 .   ? -23.278 11.313  -1.198  1.00 20.92 ? 604 HOH B O   1 
HETATM 9249 O  O   . HOH X 6 .   ? -19.471 -13.799 14.478  1.00 23.45 ? 605 HOH B O   1 
HETATM 9250 O  O   . HOH X 6 .   ? -14.760 -14.734 -2.511  1.00 16.11 ? 606 HOH B O   1 
HETATM 9251 O  O   . HOH X 6 .   ? -4.186  -13.073 25.880  1.00 25.70 ? 607 HOH B O   1 
HETATM 9252 O  O   . HOH X 6 .   ? -3.002  7.160   -3.770  1.00 18.36 ? 608 HOH B O   1 
HETATM 9253 O  O   . HOH X 6 .   ? -9.402  16.915  -15.803 1.00 24.29 ? 609 HOH B O   1 
HETATM 9254 O  O   . HOH X 6 .   ? -11.104 -15.867 3.174   1.00 27.09 ? 610 HOH B O   1 
HETATM 9255 O  O   . HOH X 6 .   ? 4.188   10.043  -6.890  1.00 32.64 ? 611 HOH B O   1 
HETATM 9256 O  O   . HOH X 6 .   ? -20.319 11.975  -13.008 1.00 39.58 ? 612 HOH B O   1 
HETATM 9257 O  O   . HOH X 6 .   ? -34.756 -2.868  -2.011  1.00 29.50 ? 613 HOH B O   1 
HETATM 9258 O  O   . HOH X 6 .   ? 4.157   -4.774  0.887   1.00 25.72 ? 614 HOH B O   1 
HETATM 9259 O  O   . HOH X 6 .   ? 7.431   1.482   19.770  1.00 28.11 ? 615 HOH B O   1 
HETATM 9260 O  O   . HOH X 6 .   ? -20.622 -0.346  -14.127 1.00 31.29 ? 616 HOH B O   1 
HETATM 9261 O  O   . HOH X 6 .   ? -28.880 -5.659  12.231  1.00 38.42 ? 617 HOH B O   1 
HETATM 9262 O  O   . HOH X 6 .   ? -6.413  15.534  15.950  1.00 28.70 ? 618 HOH B O   1 
HETATM 9263 O  O   . HOH X 6 .   ? -14.684 11.155  3.615   1.00 20.49 ? 619 HOH B O   1 
HETATM 9264 O  O   . HOH X 6 .   ? 3.404   21.360  9.566   1.00 24.55 ? 620 HOH B O   1 
HETATM 9265 O  O   . HOH X 6 .   ? -20.158 -13.622 11.778  1.00 35.08 ? 621 HOH B O   1 
HETATM 9266 O  O   . HOH X 6 .   ? -1.747  11.871  -4.693  1.00 28.28 ? 622 HOH B O   1 
HETATM 9267 O  O   . HOH X 6 .   ? 4.427   -13.199 22.534  1.00 37.78 ? 623 HOH B O   1 
HETATM 9268 O  O   . HOH X 6 .   ? 3.232   13.691  -7.187  1.00 40.92 ? 624 HOH B O   1 
HETATM 9269 O  O   . HOH X 6 .   ? -33.589 2.934   2.498   1.00 26.57 ? 625 HOH B O   1 
HETATM 9270 O  O   . HOH X 6 .   ? -8.349  -16.930 8.921   1.00 36.31 ? 626 HOH B O   1 
HETATM 9271 O  O   . HOH X 6 .   ? -0.825  -12.781 15.405  1.00 35.58 ? 627 HOH B O   1 
HETATM 9272 O  O   . HOH X 6 .   ? 7.765   -3.398  3.481   1.00 18.53 ? 628 HOH B O   1 
HETATM 9273 O  O   . HOH X 6 .   ? 1.281   22.412  9.407   1.00 33.71 ? 629 HOH B O   1 
HETATM 9274 O  O   . HOH X 6 .   ? -29.346 9.405   -6.200  1.00 43.46 ? 630 HOH B O   1 
HETATM 9275 O  O   . HOH X 6 .   ? -10.972 16.766  -7.589  1.00 36.57 ? 631 HOH B O   1 
HETATM 9276 O  O   . HOH X 6 .   ? -24.458 -1.193  -11.775 1.00 26.58 ? 632 HOH B O   1 
HETATM 9277 O  O   . HOH X 6 .   ? -2.718  -10.829 -15.053 1.00 33.78 ? 633 HOH B O   1 
HETATM 9278 O  O   . HOH X 6 .   ? -30.163 4.658   2.483   1.00 33.53 ? 634 HOH B O   1 
HETATM 9279 O  O   . HOH X 6 .   ? -9.611  -18.231 12.785  1.00 43.14 ? 635 HOH B O   1 
HETATM 9280 O  O   . HOH X 6 .   ? -0.899  -12.990 4.348   1.00 37.32 ? 636 HOH B O   1 
HETATM 9281 O  O   . HOH X 6 .   ? -20.164 -4.034  26.181  1.00 33.54 ? 637 HOH B O   1 
HETATM 9282 O  O   . HOH X 6 .   ? -21.456 -6.525  -9.849  1.00 26.32 ? 638 HOH B O   1 
HETATM 9283 O  O   . HOH X 6 .   ? -9.950  20.211  -9.022  1.00 33.02 ? 639 HOH B O   1 
HETATM 9284 O  O   . HOH X 6 .   ? -12.368 -20.538 0.295   1.00 45.37 ? 640 HOH B O   1 
HETATM 9285 O  O   . HOH X 6 .   ? -7.877  6.445   1.869   1.00 16.64 ? 641 HOH B O   1 
HETATM 9286 O  O   . HOH X 6 .   ? -13.590 13.506  -2.284  1.00 40.99 ? 642 HOH B O   1 
HETATM 9287 O  O   . HOH X 6 .   ? -17.913 -13.857 0.055   1.00 37.98 ? 643 HOH B O   1 
HETATM 9288 O  O   . HOH X 6 .   ? -17.468 -14.466 -2.377  1.00 24.52 ? 644 HOH B O   1 
HETATM 9289 O  O   . HOH X 6 .   ? -29.590 6.968   1.100   1.00 29.39 ? 645 HOH B O   1 
HETATM 9290 O  O   . HOH X 6 .   ? -0.240  -13.331 -4.358  1.00 32.47 ? 646 HOH B O   1 
HETATM 9291 O  O   . HOH X 6 .   ? 12.641  11.358  -3.718  1.00 34.20 ? 647 HOH B O   1 
HETATM 9292 O  O   . HOH X 6 .   ? -23.242 -4.564  -10.091 1.00 30.89 ? 648 HOH B O   1 
HETATM 9293 O  O   . HOH X 6 .   ? 6.401   -5.864  11.125  1.00 31.03 ? 649 HOH B O   1 
HETATM 9294 O  O   . HOH X 6 .   ? -10.940 14.793  -5.445  1.00 39.08 ? 650 HOH B O   1 
HETATM 9295 O  O   . HOH X 6 .   ? 5.966   2.253   -3.566  1.00 29.50 ? 651 HOH B O   1 
HETATM 9296 O  O   . HOH X 6 .   ? -13.005 -17.418 7.187   1.00 36.65 ? 652 HOH B O   1 
HETATM 9297 O  O   . HOH X 6 .   ? -8.180  -5.751  -15.548 1.00 25.23 ? 653 HOH B O   1 
HETATM 9298 O  O   . HOH X 6 .   ? -17.206 -16.821 3.637   1.00 44.30 ? 654 HOH B O   1 
HETATM 9299 O  O   . HOH X 6 .   ? -29.118 -7.607  6.562   1.00 28.03 ? 655 HOH B O   1 
HETATM 9300 O  O   . HOH X 6 .   ? -23.878 -11.050 5.682   1.00 46.44 ? 656 HOH B O   1 
HETATM 9301 O  O   . HOH X 6 .   ? -14.695 1.230   23.249  1.00 34.74 ? 657 HOH B O   1 
HETATM 9302 O  O   . HOH X 6 .   ? 7.836   5.965   0.803   1.00 22.05 ? 658 HOH B O   1 
HETATM 9303 O  O   . HOH X 6 .   ? -21.321 -12.070 15.923  1.00 27.80 ? 659 HOH B O   1 
HETATM 9304 O  O   . HOH X 6 .   ? 4.693   -11.823 24.763  1.00 41.86 ? 660 HOH B O   1 
HETATM 9305 O  O   . HOH X 6 .   ? -11.472 -8.389  -14.963 1.00 26.61 ? 661 HOH B O   1 
HETATM 9306 O  O   . HOH X 6 .   ? 5.822   -0.479  -2.576  1.00 28.54 ? 662 HOH B O   1 
HETATM 9307 O  O   . HOH X 6 .   ? -16.692 -14.169 27.923  1.00 22.92 ? 663 HOH B O   1 
HETATM 9308 O  O   . HOH X 6 .   ? 1.799   -15.789 16.608  1.00 27.82 ? 664 HOH B O   1 
HETATM 9309 O  O   . HOH X 6 .   ? 7.676   -9.382  15.726  1.00 21.06 ? 665 HOH B O   1 
HETATM 9310 O  O   . HOH X 6 .   ? -16.877 19.222  5.768   1.00 38.23 ? 666 HOH B O   1 
HETATM 9311 O  O   . HOH X 6 .   ? -21.398 10.016  -14.856 1.00 44.03 ? 667 HOH B O   1 
HETATM 9312 O  O   . HOH X 6 .   ? -19.186 -16.461 -3.908  1.00 34.66 ? 668 HOH B O   1 
HETATM 9313 O  O   . HOH X 6 .   ? -1.291  21.906  10.468  1.00 43.92 ? 669 HOH B O   1 
HETATM 9314 O  O   . HOH X 6 .   ? 5.356   -13.181 15.798  1.00 23.51 ? 670 HOH B O   1 
HETATM 9315 O  O   . HOH X 6 .   ? -15.673 -14.559 3.662   1.00 31.55 ? 671 HOH B O   1 
HETATM 9316 O  O   . HOH X 6 .   ? -18.468 -11.806 23.906  1.00 30.62 ? 672 HOH B O   1 
HETATM 9317 O  O   . HOH X 6 .   ? -4.366  -13.779 9.885   1.00 32.35 ? 673 HOH B O   1 
HETATM 9318 O  O   . HOH X 6 .   ? -17.664 -12.845 21.285  1.00 25.84 ? 674 HOH B O   1 
HETATM 9319 O  O   . HOH X 6 .   ? 5.027   -7.354  1.153   1.00 22.40 ? 675 HOH B O   1 
HETATM 9320 O  O   . HOH X 6 .   ? -20.927 -10.799 -9.928  1.00 24.47 ? 676 HOH B O   1 
HETATM 9321 O  O   . HOH X 6 .   ? -8.941  15.235  5.371   1.00 37.39 ? 677 HOH B O   1 
HETATM 9322 O  O   . HOH X 6 .   ? -3.447  15.151  18.681  1.00 28.70 ? 678 HOH B O   1 
HETATM 9323 O  O   . HOH X 6 .   ? -13.523 -11.924 -13.004 1.00 24.02 ? 679 HOH B O   1 
HETATM 9324 O  O   . HOH X 6 .   ? -4.120  1.882   24.045  1.00 31.23 ? 680 HOH B O   1 
HETATM 9325 O  O   . HOH X 6 .   ? -3.136  18.787  10.507  1.00 33.54 ? 681 HOH B O   1 
HETATM 9326 O  O   . HOH X 6 .   ? -0.276  -12.235 -8.822  1.00 28.40 ? 682 HOH B O   1 
HETATM 9327 O  O   . HOH X 6 .   ? -18.972 -16.102 15.557  1.00 34.28 ? 683 HOH B O   1 
HETATM 9328 O  O   . HOH X 6 .   ? -5.703  18.982  9.884   1.00 37.56 ? 684 HOH B O   1 
HETATM 9329 O  O   . HOH X 6 .   ? -12.702 -14.220 30.964  1.00 22.73 ? 685 HOH B O   1 
HETATM 9330 O  O   . HOH X 6 .   ? -7.690  -9.993  -15.975 1.00 20.08 ? 686 HOH B O   1 
HETATM 9331 O  O   . HOH X 6 .   ? -10.289 -13.166 30.632  1.00 23.84 ? 687 HOH B O   1 
HETATM 9332 O  O   . HOH X 6 .   ? -2.024  -15.388 11.058  1.00 33.50 ? 688 HOH B O   1 
HETATM 9333 O  O   . HOH X 6 .   ? -1.897  20.418  13.183  1.00 41.69 ? 689 HOH B O   1 
HETATM 9334 O  O   . HOH X 6 .   ? 13.014  11.470  -6.344  1.00 34.57 ? 690 HOH B O   1 
HETATM 9335 O  O   . HOH X 6 .   ? -3.210  4.028   23.845  1.00 44.74 ? 691 HOH B O   1 
HETATM 9336 O  O   . HOH X 6 .   ? -21.795 -13.416 -9.506  1.00 29.83 ? 692 HOH B O   1 
HETATM 9337 O  O   . HOH X 6 .   ? -21.841 -13.506 18.428  1.00 34.88 ? 693 HOH B O   1 
HETATM 9338 O  O   . HOH Y 6 .   ? 29.672  -13.877 -28.050 1.00 28.80 ? 401 HOH C O   1 
HETATM 9339 O  O   . HOH Y 6 .   ? 48.654  6.846   -50.980 1.00 34.74 ? 402 HOH C O   1 
HETATM 9340 O  O   . HOH Y 6 .   ? 33.002  12.935  -8.454  1.00 33.67 ? 403 HOH C O   1 
HETATM 9341 O  O   . HOH Y 6 .   ? 55.589  5.597   -22.391 1.00 34.05 ? 404 HOH C O   1 
HETATM 9342 O  O   . HOH Y 6 .   ? 56.114  8.316   -37.652 1.00 27.99 ? 405 HOH C O   1 
HETATM 9343 O  O   . HOH Y 6 .   ? 56.886  -8.193  -23.454 1.00 35.90 ? 406 HOH C O   1 
HETATM 9344 O  O   . HOH Y 6 .   ? 42.894  -19.584 -40.585 1.00 40.55 ? 407 HOH C O   1 
HETATM 9345 O  O   . HOH Y 6 .   ? 28.574  7.023   -19.415 1.00 29.29 ? 408 HOH C O   1 
HETATM 9346 O  O   . HOH Y 6 .   ? 49.710  -5.495  -49.484 1.00 42.48 ? 409 HOH C O   1 
HETATM 9347 O  O   . HOH Y 6 .   ? 36.122  -9.585  -53.809 1.00 34.55 ? 410 HOH C O   1 
HETATM 9348 O  O   . HOH Y 6 .   ? 19.714  1.207   -51.606 1.00 32.69 ? 411 HOH C O   1 
HETATM 9349 O  O   . HOH Y 6 .   ? 22.084  -8.612  -39.903 1.00 27.93 ? 412 HOH C O   1 
HETATM 9350 O  O   . HOH Y 6 .   ? 46.381  8.036   -11.505 1.00 23.31 ? 413 HOH C O   1 
HETATM 9351 O  O   . HOH Y 6 .   ? 58.449  -2.217  -30.137 1.00 28.73 ? 414 HOH C O   1 
HETATM 9352 O  O   . HOH Y 6 .   ? 28.317  -14.430 -47.821 1.00 41.27 ? 415 HOH C O   1 
HETATM 9353 O  O   . HOH Y 6 .   ? 35.735  -13.665 -54.599 1.00 21.11 ? 416 HOH C O   1 
HETATM 9354 O  O   . HOH Y 6 .   ? 42.352  10.963  -25.973 1.00 31.36 ? 417 HOH C O   1 
HETATM 9355 O  O   . HOH Y 6 .   ? 40.120  -8.007  -13.968 1.00 35.80 ? 418 HOH C O   1 
HETATM 9356 O  O   . HOH Y 6 .   ? 22.264  -6.289  -31.529 1.00 23.05 ? 419 HOH C O   1 
HETATM 9357 O  O   . HOH Y 6 .   ? 32.399  5.164   -30.567 1.00 12.22 ? 420 HOH C O   1 
HETATM 9358 O  O   . HOH Y 6 .   ? 22.524  -1.953  -31.273 1.00 32.34 ? 421 HOH C O   1 
HETATM 9359 O  O   . HOH Y 6 .   ? 41.642  6.849   -9.871  1.00 26.30 ? 422 HOH C O   1 
HETATM 9360 O  O   . HOH Y 6 .   ? 49.744  -9.114  -46.274 1.00 27.43 ? 423 HOH C O   1 
HETATM 9361 O  O   . HOH Y 6 .   ? 33.130  -1.379  -49.046 1.00 21.09 ? 424 HOH C O   1 
HETATM 9362 O  O   . HOH Y 6 .   ? 43.945  -14.643 -28.008 1.00 31.68 ? 425 HOH C O   1 
HETATM 9363 O  O   . HOH Y 6 .   ? 33.257  -16.405 -17.606 1.00 34.14 ? 426 HOH C O   1 
HETATM 9364 O  O   . HOH Y 6 .   ? 53.933  -13.246 -25.652 1.00 28.90 ? 427 HOH C O   1 
HETATM 9365 O  O   . HOH Y 6 .   ? 33.249  12.114  -10.893 1.00 24.19 ? 428 HOH C O   1 
HETATM 9366 O  O   . HOH Y 6 .   ? 52.881  6.374   -31.423 1.00 17.86 ? 429 HOH C O   1 
HETATM 9367 O  O   . HOH Y 6 .   ? 59.892  -1.813  -35.228 1.00 30.91 ? 430 HOH C O   1 
HETATM 9368 O  O   . HOH Y 6 .   ? 46.885  -14.595 -32.257 1.00 35.65 ? 431 HOH C O   1 
HETATM 9369 O  O   . HOH Y 6 .   ? 57.872  -3.480  -41.857 1.00 51.00 ? 432 HOH C O   1 
HETATM 9370 O  O   . HOH Y 6 .   ? 47.384  -1.667  -9.869  1.00 34.04 ? 433 HOH C O   1 
HETATM 9371 O  O   . HOH Y 6 .   ? 56.323  3.708   -13.017 1.00 20.79 ? 434 HOH C O   1 
HETATM 9372 O  O   . HOH Y 6 .   ? 24.650  -12.953 -41.601 1.00 24.91 ? 435 HOH C O   1 
HETATM 9373 O  O   . HOH Y 6 .   ? 28.616  -7.920  -17.254 1.00 22.32 ? 436 HOH C O   1 
HETATM 9374 O  O   . HOH Y 6 .   ? 35.217  17.153  -41.470 1.00 31.13 ? 437 HOH C O   1 
HETATM 9375 O  O   . HOH Y 6 .   ? 46.897  2.322   -47.395 1.00 34.47 ? 438 HOH C O   1 
HETATM 9376 O  O   . HOH Y 6 .   ? 46.956  11.436  -21.763 1.00 33.73 ? 439 HOH C O   1 
HETATM 9377 O  O   . HOH Y 6 .   ? 52.555  1.071   -13.242 1.00 27.00 ? 440 HOH C O   1 
HETATM 9378 O  O   . HOH Y 6 .   ? 47.109  -13.724 -29.495 1.00 38.53 ? 441 HOH C O   1 
HETATM 9379 O  O   . HOH Y 6 .   ? 47.086  9.224   -27.178 1.00 20.70 ? 442 HOH C O   1 
HETATM 9380 O  O   . HOH Y 6 .   ? 43.876  -5.592  -50.407 1.00 24.38 ? 443 HOH C O   1 
HETATM 9381 O  O   . HOH Y 6 .   ? 50.084  -4.647  -16.144 1.00 27.34 ? 444 HOH C O   1 
HETATM 9382 O  O   . HOH Y 6 .   ? 44.473  -14.914 -50.599 1.00 31.07 ? 445 HOH C O   1 
HETATM 9383 O  O   . HOH Y 6 .   ? 35.400  -21.311 -51.250 1.00 22.66 ? 446 HOH C O   1 
HETATM 9384 O  O   . HOH Y 6 .   ? 26.031  5.612   -43.495 1.00 19.59 ? 447 HOH C O   1 
HETATM 9385 O  O   . HOH Y 6 .   ? 45.875  -18.697 -34.330 1.00 40.21 ? 448 HOH C O   1 
HETATM 9386 O  O   . HOH Y 6 .   ? 29.758  6.533   -22.137 1.00 28.80 ? 449 HOH C O   1 
HETATM 9387 O  O   . HOH Y 6 .   ? 47.249  9.117   -30.098 1.00 28.87 ? 450 HOH C O   1 
HETATM 9388 O  O   . HOH Y 6 .   ? 52.725  4.940   -49.032 1.00 27.51 ? 451 HOH C O   1 
HETATM 9389 O  O   . HOH Y 6 .   ? 25.209  -1.580  -40.725 1.00 11.32 ? 452 HOH C O   1 
HETATM 9390 O  O   . HOH Y 6 .   ? 38.325  -13.912 -13.540 1.00 30.55 ? 453 HOH C O   1 
HETATM 9391 O  O   . HOH Y 6 .   ? 56.636  4.590   -42.046 1.00 20.21 ? 454 HOH C O   1 
HETATM 9392 O  O   . HOH Y 6 .   ? 26.007  7.118   -41.262 1.00 11.02 ? 455 HOH C O   1 
HETATM 9393 O  O   . HOH Y 6 .   ? 23.921  13.100  -42.468 1.00 16.32 ? 456 HOH C O   1 
HETATM 9394 O  O   . HOH Y 6 .   ? 48.050  -10.964 -16.165 1.00 26.43 ? 457 HOH C O   1 
HETATM 9395 O  O   . HOH Y 6 .   ? 53.358  -3.395  -46.141 1.00 33.20 ? 458 HOH C O   1 
HETATM 9396 O  O   . HOH Y 6 .   ? 25.093  8.380   -28.162 1.00 14.64 ? 459 HOH C O   1 
HETATM 9397 O  O   . HOH Y 6 .   ? 53.100  14.557  -44.873 1.00 33.98 ? 460 HOH C O   1 
HETATM 9398 O  O   . HOH Y 6 .   ? 33.413  9.367   -6.688  1.00 30.00 ? 461 HOH C O   1 
HETATM 9399 O  O   . HOH Y 6 .   ? 48.634  3.421   -49.046 1.00 38.61 ? 462 HOH C O   1 
HETATM 9400 O  O   . HOH Y 6 .   ? 29.562  -4.806  -22.160 1.00 14.55 ? 463 HOH C O   1 
HETATM 9401 O  O   . HOH Y 6 .   ? 32.740  -13.357 -37.118 1.00 22.06 ? 464 HOH C O   1 
HETATM 9402 O  O   . HOH Y 6 .   ? 41.440  -8.392  -55.113 1.00 25.87 ? 465 HOH C O   1 
HETATM 9403 O  O   . HOH Y 6 .   ? 27.312  16.415  -41.428 1.00 14.01 ? 466 HOH C O   1 
HETATM 9404 O  O   . HOH Y 6 .   ? 43.146  -2.221  -40.507 1.00 11.74 ? 467 HOH C O   1 
HETATM 9405 O  O   . HOH Y 6 .   ? 27.207  -10.244 -26.759 1.00 22.84 ? 468 HOH C O   1 
HETATM 9406 O  O   . HOH Y 6 .   ? 55.596  -8.216  -32.856 1.00 23.03 ? 469 HOH C O   1 
HETATM 9407 O  O   . HOH Y 6 .   ? 25.790  -3.336  -42.651 1.00 18.33 ? 470 HOH C O   1 
HETATM 9408 O  O   . HOH Y 6 .   ? 46.684  -3.462  -48.834 1.00 41.10 ? 471 HOH C O   1 
HETATM 9409 O  O   . HOH Y 6 .   ? 23.472  -4.511  -35.976 1.00 18.98 ? 472 HOH C O   1 
HETATM 9410 O  O   . HOH Y 6 .   ? 34.809  -7.908  -11.327 1.00 29.44 ? 473 HOH C O   1 
HETATM 9411 O  O   . HOH Y 6 .   ? 23.854  -3.149  -26.594 1.00 34.93 ? 474 HOH C O   1 
HETATM 9412 O  O   . HOH Y 6 .   ? 51.910  -5.169  -18.180 1.00 31.13 ? 475 HOH C O   1 
HETATM 9413 O  O   . HOH Y 6 .   ? 24.914  6.702   -34.775 1.00 10.87 ? 476 HOH C O   1 
HETATM 9414 O  O   . HOH Y 6 .   ? 46.173  -11.113 -40.722 1.00 23.83 ? 477 HOH C O   1 
HETATM 9415 O  O   . HOH Y 6 .   ? 20.799  -1.878  -50.934 1.00 35.31 ? 478 HOH C O   1 
HETATM 9416 O  O   . HOH Y 6 .   ? 41.913  -17.799 -53.760 1.00 34.67 ? 479 HOH C O   1 
HETATM 9417 O  O   . HOH Y 6 .   ? 51.500  -2.303  -43.724 1.00 22.09 ? 480 HOH C O   1 
HETATM 9418 O  O   . HOH Y 6 .   ? 28.580  3.426   -43.627 1.00 14.06 ? 481 HOH C O   1 
HETATM 9419 O  O   . HOH Y 6 .   ? 47.597  -9.152  -51.804 1.00 31.19 ? 482 HOH C O   1 
HETATM 9420 O  O   . HOH Y 6 .   ? 20.158  -10.052 -29.902 1.00 20.80 ? 483 HOH C O   1 
HETATM 9421 O  O   . HOH Y 6 .   ? 28.172  18.447  -31.667 1.00 16.93 ? 484 HOH C O   1 
HETATM 9422 O  O   . HOH Y 6 .   ? 54.031  -6.819  -18.158 1.00 34.53 ? 485 HOH C O   1 
HETATM 9423 O  O   . HOH Y 6 .   ? 54.532  -9.969  -30.966 1.00 23.33 ? 486 HOH C O   1 
HETATM 9424 O  O   . HOH Y 6 .   ? 25.705  5.488   -23.965 1.00 22.46 ? 487 HOH C O   1 
HETATM 9425 O  O   . HOH Y 6 .   ? 53.851  7.009   -27.963 1.00 22.17 ? 488 HOH C O   1 
HETATM 9426 O  O   . HOH Y 6 .   ? 26.357  -8.442  -16.099 1.00 26.92 ? 489 HOH C O   1 
HETATM 9427 O  O   . HOH Y 6 .   ? 20.109  18.051  -29.963 1.00 28.19 ? 490 HOH C O   1 
HETATM 9428 O  O   . HOH Y 6 .   ? 43.650  4.231   -44.407 1.00 19.66 ? 491 HOH C O   1 
HETATM 9429 O  O   . HOH Y 6 .   ? 34.024  16.059  -38.426 1.00 12.82 ? 492 HOH C O   1 
HETATM 9430 O  O   . HOH Y 6 .   ? 22.095  -0.843  -23.897 1.00 26.84 ? 493 HOH C O   1 
HETATM 9431 O  O   . HOH Y 6 .   ? 51.993  17.914  -39.358 1.00 36.95 ? 494 HOH C O   1 
HETATM 9432 O  O   . HOH Y 6 .   ? 42.228  16.790  -44.732 1.00 28.98 ? 495 HOH C O   1 
HETATM 9433 O  O   . HOH Y 6 .   ? 39.042  -26.597 -44.368 1.00 25.42 ? 496 HOH C O   1 
HETATM 9434 O  O   . HOH Y 6 .   ? 38.837  -2.877  -11.606 1.00 30.27 ? 497 HOH C O   1 
HETATM 9435 O  O   . HOH Y 6 .   ? 28.844  9.203   -22.552 1.00 27.00 ? 498 HOH C O   1 
HETATM 9436 O  O   . HOH Y 6 .   ? 56.233  9.205   -40.126 1.00 31.60 ? 499 HOH C O   1 
HETATM 9437 O  O   . HOH Y 6 .   ? 47.949  -12.755 -39.361 1.00 23.60 ? 500 HOH C O   1 
HETATM 9438 O  O   . HOH Y 6 .   ? 25.516  -2.983  -48.426 1.00 22.57 ? 501 HOH C O   1 
HETATM 9439 O  O   . HOH Y 6 .   ? 46.957  7.326   -22.903 1.00 18.78 ? 502 HOH C O   1 
HETATM 9440 O  O   . HOH Y 6 .   ? 40.329  -16.373 -30.421 1.00 24.44 ? 503 HOH C O   1 
HETATM 9441 O  O   . HOH Y 6 .   ? 40.699  14.006  -36.993 1.00 24.24 ? 504 HOH C O   1 
HETATM 9442 O  O   . HOH Y 6 .   ? 43.213  -1.553  -10.789 1.00 32.48 ? 505 HOH C O   1 
HETATM 9443 O  O   . HOH Y 6 .   ? 44.707  -13.821 -44.760 1.00 20.60 ? 506 HOH C O   1 
HETATM 9444 O  O   . HOH Y 6 .   ? 33.759  1.638   -16.623 1.00 15.38 ? 507 HOH C O   1 
HETATM 9445 O  O   . HOH Y 6 .   ? 43.677  -12.753 -25.981 1.00 22.27 ? 508 HOH C O   1 
HETATM 9446 O  O   . HOH Y 6 .   ? 21.144  14.335  -20.514 1.00 29.05 ? 509 HOH C O   1 
HETATM 9447 O  O   . HOH Y 6 .   ? 27.004  -0.690  -32.363 1.00 10.29 ? 510 HOH C O   1 
HETATM 9448 O  O   . HOH Y 6 .   ? 38.852  1.961   -6.182  1.00 16.58 ? 511 HOH C O   1 
HETATM 9449 O  O   . HOH Y 6 .   ? 39.676  13.808  -12.486 1.00 26.71 ? 512 HOH C O   1 
HETATM 9450 O  O   . HOH Y 6 .   ? 37.618  -10.275 -33.363 1.00 13.00 ? 513 HOH C O   1 
HETATM 9451 O  O   . HOH Y 6 .   ? 26.180  6.873   -14.188 1.00 30.66 ? 514 HOH C O   1 
HETATM 9452 O  O   . HOH Y 6 .   ? 25.272  14.726  -23.360 1.00 25.37 ? 515 HOH C O   1 
HETATM 9453 O  O   . HOH Y 6 .   ? 31.875  2.636   -43.822 1.00 14.33 ? 516 HOH C O   1 
HETATM 9454 O  O   . HOH Y 6 .   ? 35.128  6.156   -26.879 1.00 17.54 ? 517 HOH C O   1 
HETATM 9455 O  O   . HOH Y 6 .   ? 30.266  -10.092 -16.744 1.00 28.48 ? 518 HOH C O   1 
HETATM 9456 O  O   . HOH Y 6 .   ? 24.730  -1.913  -23.715 1.00 25.03 ? 519 HOH C O   1 
HETATM 9457 O  O   . HOH Y 6 .   ? 46.546  -0.932  -47.789 1.00 33.32 ? 520 HOH C O   1 
HETATM 9458 O  O   . HOH Y 6 .   ? 41.161  7.384   -46.944 1.00 25.41 ? 521 HOH C O   1 
HETATM 9459 O  O   . HOH Y 6 .   ? 57.630  7.066   -18.558 1.00 36.71 ? 522 HOH C O   1 
HETATM 9460 O  O   . HOH Y 6 .   ? 22.340  0.438   -28.005 1.00 23.74 ? 523 HOH C O   1 
HETATM 9461 O  O   . HOH Y 6 .   ? 24.274  19.074  -28.875 1.00 31.43 ? 524 HOH C O   1 
HETATM 9462 O  O   . HOH Y 6 .   ? 49.062  2.030   -12.679 1.00 29.04 ? 525 HOH C O   1 
HETATM 9463 O  O   . HOH Y 6 .   ? 23.303  4.852   -36.126 1.00 7.75  ? 526 HOH C O   1 
HETATM 9464 O  O   . HOH Y 6 .   ? 54.835  1.072   -14.972 1.00 27.07 ? 527 HOH C O   1 
HETATM 9465 O  O   . HOH Y 6 .   ? 26.569  9.457   -34.856 1.00 10.53 ? 528 HOH C O   1 
HETATM 9466 O  O   . HOH Y 6 .   ? 54.354  9.650   -34.039 1.00 31.87 ? 529 HOH C O   1 
HETATM 9467 O  O   . HOH Y 6 .   ? 46.813  -13.040 -53.249 1.00 19.40 ? 530 HOH C O   1 
HETATM 9468 O  O   . HOH Y 6 .   ? 59.777  -2.576  -25.906 1.00 27.34 ? 531 HOH C O   1 
HETATM 9469 O  O   . HOH Y 6 .   ? 35.709  -0.935  -48.473 1.00 20.06 ? 532 HOH C O   1 
HETATM 9470 O  O   . HOH Y 6 .   ? 25.733  13.119  -35.537 1.00 10.14 ? 533 HOH C O   1 
HETATM 9471 O  O   . HOH Y 6 .   ? 42.067  -3.910  -48.435 1.00 23.95 ? 534 HOH C O   1 
HETATM 9472 O  O   . HOH Y 6 .   ? 50.990  11.106  -15.914 1.00 35.09 ? 535 HOH C O   1 
HETATM 9473 O  O   . HOH Y 6 .   ? 51.647  10.087  -33.443 1.00 22.17 ? 536 HOH C O   1 
HETATM 9474 O  O   . HOH Y 6 .   ? 35.285  19.624  -36.023 1.00 33.50 ? 537 HOH C O   1 
HETATM 9475 O  O   . HOH Y 6 .   ? 37.528  14.348  -28.687 1.00 31.84 ? 538 HOH C O   1 
HETATM 9476 O  O   . HOH Y 6 .   ? 22.020  6.905   -32.288 1.00 11.23 ? 539 HOH C O   1 
HETATM 9477 O  O   . HOH Y 6 .   ? 38.582  -19.729 -46.262 1.00 34.64 ? 540 HOH C O   1 
HETATM 9478 O  O   . HOH Y 6 .   ? 53.839  -10.083 -22.605 1.00 30.12 ? 541 HOH C O   1 
HETATM 9479 O  O   . HOH Y 6 .   ? 26.462  -13.402 -34.636 1.00 22.44 ? 542 HOH C O   1 
HETATM 9480 O  O   . HOH Y 6 .   ? 31.434  2.411   -14.551 1.00 20.51 ? 543 HOH C O   1 
HETATM 9481 O  O   . HOH Y 6 .   ? 31.393  12.779  -46.577 1.00 25.03 ? 544 HOH C O   1 
HETATM 9482 O  O   . HOH Y 6 .   ? 27.833  2.401   -52.524 1.00 38.62 ? 545 HOH C O   1 
HETATM 9483 O  O   . HOH Y 6 .   ? 52.659  8.655   -24.038 1.00 24.39 ? 546 HOH C O   1 
HETATM 9484 O  O   . HOH Y 6 .   ? 48.475  -12.989 -34.274 1.00 34.34 ? 547 HOH C O   1 
HETATM 9485 O  O   . HOH Y 6 .   ? 27.605  16.112  -29.736 1.00 23.53 ? 548 HOH C O   1 
HETATM 9486 O  O   . HOH Y 6 .   ? 39.802  6.818   -26.631 1.00 22.74 ? 549 HOH C O   1 
HETATM 9487 O  O   . HOH Y 6 .   ? 24.322  -3.516  -44.964 1.00 25.53 ? 550 HOH C O   1 
HETATM 9488 O  O   . HOH Y 6 .   ? 28.729  3.700   -46.298 1.00 18.00 ? 551 HOH C O   1 
HETATM 9489 O  O   . HOH Y 6 .   ? 22.825  -11.388 -44.752 1.00 30.72 ? 552 HOH C O   1 
HETATM 9490 O  O   . HOH Y 6 .   ? 22.324  11.100  -29.497 1.00 16.70 ? 553 HOH C O   1 
HETATM 9491 O  O   . HOH Y 6 .   ? 31.205  -16.375 -30.767 1.00 35.19 ? 554 HOH C O   1 
HETATM 9492 O  O   . HOH Y 6 .   ? 32.432  11.417  -43.312 1.00 11.20 ? 555 HOH C O   1 
HETATM 9493 O  O   . HOH Y 6 .   ? 37.329  9.132   -47.582 1.00 29.75 ? 556 HOH C O   1 
HETATM 9494 O  O   . HOH Y 6 .   ? 44.344  18.148  -43.475 1.00 43.10 ? 557 HOH C O   1 
HETATM 9495 O  O   . HOH Y 6 .   ? 37.356  -17.562 -30.726 1.00 38.77 ? 558 HOH C O   1 
HETATM 9496 O  O   . HOH Y 6 .   ? 38.212  5.127   -45.278 1.00 16.89 ? 559 HOH C O   1 
HETATM 9497 O  O   . HOH Y 6 .   ? 40.938  3.806   -6.733  1.00 21.27 ? 560 HOH C O   1 
HETATM 9498 O  O   . HOH Y 6 .   ? 58.009  -7.258  -31.085 1.00 24.63 ? 561 HOH C O   1 
HETATM 9499 O  O   . HOH Y 6 .   ? 29.109  6.157   -47.434 1.00 17.75 ? 562 HOH C O   1 
HETATM 9500 O  O   . HOH Y 6 .   ? 32.519  0.707   -51.015 1.00 41.63 ? 563 HOH C O   1 
HETATM 9501 O  O   . HOH Y 6 .   ? 33.642  13.647  -44.265 1.00 19.12 ? 564 HOH C O   1 
HETATM 9502 O  O   . HOH Y 6 .   ? 39.731  -11.827 -55.267 1.00 24.76 ? 565 HOH C O   1 
HETATM 9503 O  O   . HOH Y 6 .   ? 26.334  3.444   -47.497 1.00 27.84 ? 566 HOH C O   1 
HETATM 9504 O  O   . HOH Y 6 .   ? 60.567  -6.817  -25.697 1.00 44.65 ? 567 HOH C O   1 
HETATM 9505 O  O   . HOH Y 6 .   ? 61.867  -0.907  -32.845 1.00 28.20 ? 568 HOH C O   1 
HETATM 9506 O  O   . HOH Y 6 .   ? 40.348  -13.949 -36.394 1.00 16.08 ? 569 HOH C O   1 
HETATM 9507 O  O   . HOH Y 6 .   ? 43.974  13.935  -47.803 1.00 27.80 ? 570 HOH C O   1 
HETATM 9508 O  O   . HOH Y 6 .   ? 33.178  16.308  -14.819 1.00 31.19 ? 571 HOH C O   1 
HETATM 9509 O  O   . HOH Y 6 .   ? 58.709  -7.608  -34.774 1.00 31.53 ? 572 HOH C O   1 
HETATM 9510 O  O   . HOH Y 6 .   ? 24.212  -0.609  -32.933 1.00 17.52 ? 573 HOH C O   1 
HETATM 9511 O  O   . HOH Y 6 .   ? 59.993  -7.956  -20.988 1.00 34.81 ? 574 HOH C O   1 
HETATM 9512 O  O   . HOH Y 6 .   ? 22.153  -4.951  -40.986 1.00 26.58 ? 575 HOH C O   1 
HETATM 9513 O  O   . HOH Y 6 .   ? 32.490  -14.596 -51.597 1.00 22.00 ? 576 HOH C O   1 
HETATM 9514 O  O   . HOH Y 6 .   ? 23.615  5.788   -40.795 1.00 11.94 ? 577 HOH C O   1 
HETATM 9515 O  O   . HOH Y 6 .   ? 26.324  9.787   -41.894 1.00 12.23 ? 578 HOH C O   1 
HETATM 9516 O  O   . HOH Y 6 .   ? 32.030  -2.013  -51.697 1.00 29.23 ? 579 HOH C O   1 
HETATM 9517 O  O   . HOH Y 6 .   ? 29.587  -12.318 -23.912 1.00 20.49 ? 580 HOH C O   1 
HETATM 9518 O  O   . HOH Y 6 .   ? 40.620  -15.606 -25.437 1.00 24.74 ? 581 HOH C O   1 
HETATM 9519 O  O   . HOH Y 6 .   ? 48.104  19.005  -41.239 1.00 36.50 ? 582 HOH C O   1 
HETATM 9520 O  O   . HOH Y 6 .   ? 46.499  11.567  -13.216 1.00 33.84 ? 583 HOH C O   1 
HETATM 9521 O  O   . HOH Y 6 .   ? 59.305  3.476   -20.761 1.00 30.41 ? 584 HOH C O   1 
HETATM 9522 O  O   . HOH Y 6 .   ? 22.256  -0.365  -44.283 1.00 21.45 ? 585 HOH C O   1 
HETATM 9523 O  O   . HOH Y 6 .   ? 41.012  4.554   -45.739 1.00 29.91 ? 586 HOH C O   1 
HETATM 9524 O  O   . HOH Y 6 .   ? 41.638  9.041   -7.710  1.00 34.64 ? 587 HOH C O   1 
HETATM 9525 O  O   . HOH Y 6 .   ? 26.306  11.637  -45.793 1.00 28.81 ? 588 HOH C O   1 
HETATM 9526 O  O   . HOH Y 6 .   ? 38.606  -18.860 -16.437 1.00 33.64 ? 589 HOH C O   1 
HETATM 9527 O  O   . HOH Y 6 .   ? 26.701  6.521   -21.217 1.00 30.89 ? 590 HOH C O   1 
HETATM 9528 O  O   . HOH Y 6 .   ? 28.213  6.915   -44.082 1.00 17.41 ? 591 HOH C O   1 
HETATM 9529 O  O   . HOH Y 6 .   ? 28.038  -10.593 -22.528 1.00 22.19 ? 592 HOH C O   1 
HETATM 9530 O  O   . HOH Y 6 .   ? 46.875  -16.223 -35.806 1.00 29.66 ? 593 HOH C O   1 
HETATM 9531 O  O   . HOH Y 6 .   ? 51.582  13.090  -47.568 1.00 32.05 ? 594 HOH C O   1 
HETATM 9532 O  O   . HOH Y 6 .   ? 39.364  18.081  -41.039 1.00 31.02 ? 595 HOH C O   1 
HETATM 9533 O  O   . HOH Y 6 .   ? 36.659  -17.022 -28.216 1.00 41.73 ? 596 HOH C O   1 
HETATM 9534 O  O   . HOH Y 6 .   ? 53.369  5.920   -23.438 1.00 22.79 ? 597 HOH C O   1 
HETATM 9535 O  O   . HOH Y 6 .   ? 38.501  16.771  -38.633 1.00 20.65 ? 598 HOH C O   1 
HETATM 9536 O  O   . HOH Y 6 .   ? 24.443  5.308   -21.241 1.00 31.41 ? 599 HOH C O   1 
HETATM 9537 O  O   . HOH Y 6 .   ? 23.680  -8.985  -29.150 1.00 28.77 ? 600 HOH C O   1 
HETATM 9538 O  O   . HOH Y 6 .   ? 46.656  13.862  -47.965 1.00 31.79 ? 601 HOH C O   1 
HETATM 9539 O  O   . HOH Y 6 .   ? 51.850  5.395   -12.906 1.00 24.10 ? 602 HOH C O   1 
HETATM 9540 O  O   . HOH Y 6 .   ? 40.715  -16.175 -22.499 1.00 29.58 ? 603 HOH C O   1 
HETATM 9541 O  O   . HOH Y 6 .   ? 48.618  11.244  -24.180 1.00 27.23 ? 604 HOH C O   1 
HETATM 9542 O  O   . HOH Y 6 .   ? 46.293  -16.946 -38.707 1.00 29.17 ? 605 HOH C O   1 
HETATM 9543 O  O   . HOH Y 6 .   ? 22.470  -8.652  -17.303 1.00 39.92 ? 606 HOH C O   1 
HETATM 9544 O  O   . HOH Y 6 .   ? 22.667  2.128   -19.056 1.00 28.62 ? 607 HOH C O   1 
HETATM 9545 O  O   . HOH Y 6 .   ? 27.039  4.071   -50.226 1.00 31.16 ? 608 HOH C O   1 
HETATM 9546 O  O   . HOH Y 6 .   ? 53.064  -13.237 -30.203 1.00 33.73 ? 609 HOH C O   1 
HETATM 9547 O  O   . HOH Y 6 .   ? 56.441  7.431   -14.082 1.00 32.29 ? 610 HOH C O   1 
HETATM 9548 O  O   . HOH Y 6 .   ? 41.345  -19.119 -18.384 1.00 45.08 ? 611 HOH C O   1 
HETATM 9549 O  O   . HOH Y 6 .   ? 55.741  6.775   -30.087 1.00 26.56 ? 612 HOH C O   1 
HETATM 9550 O  O   . HOH Y 6 .   ? 49.765  12.366  -32.920 1.00 26.48 ? 613 HOH C O   1 
HETATM 9551 O  O   . HOH Y 6 .   ? 60.063  -11.756 -24.982 1.00 43.15 ? 614 HOH C O   1 
HETATM 9552 O  O   . HOH Y 6 .   ? 29.619  -11.585 -26.540 1.00 17.95 ? 615 HOH C O   1 
HETATM 9553 O  O   . HOH Y 6 .   ? 64.818  -3.634  -15.382 1.00 32.26 ? 616 HOH C O   1 
HETATM 9554 O  O   . HOH Y 6 .   ? 29.385  -12.070 -40.830 1.00 34.00 ? 617 HOH C O   1 
HETATM 9555 O  O   . HOH Y 6 .   ? 52.560  -11.433 -36.890 1.00 32.82 ? 618 HOH C O   1 
HETATM 9556 O  O   . HOH Y 6 .   ? 38.615  13.966  -43.028 1.00 22.97 ? 619 HOH C O   1 
HETATM 9557 O  O   . HOH Y 6 .   ? 54.851  -1.832  -45.011 1.00 34.98 ? 620 HOH C O   1 
HETATM 9558 O  O   . HOH Y 6 .   ? 42.305  10.438  -28.342 1.00 41.20 ? 621 HOH C O   1 
HETATM 9559 O  O   . HOH Y 6 .   ? 27.932  -10.188 -51.640 1.00 43.33 ? 622 HOH C O   1 
HETATM 9560 O  O   . HOH Y 6 .   ? 44.446  7.186   -8.854  1.00 27.94 ? 623 HOH C O   1 
HETATM 9561 O  O   . HOH Y 6 .   ? 20.868  -1.010  -29.983 1.00 21.57 ? 624 HOH C O   1 
HETATM 9562 O  O   . HOH Y 6 .   ? 22.184  -13.940 -35.603 1.00 36.86 ? 625 HOH C O   1 
HETATM 9563 O  O   . HOH Y 6 .   ? 32.128  7.711   -22.528 1.00 27.98 ? 626 HOH C O   1 
HETATM 9564 O  O   . HOH Y 6 .   ? 44.837  9.379   -29.347 1.00 20.42 ? 627 HOH C O   1 
HETATM 9565 O  O   . HOH Y 6 .   ? 21.055  -0.020  -21.398 1.00 30.95 ? 628 HOH C O   1 
HETATM 9566 O  O   . HOH Y 6 .   ? 39.484  -4.978  -49.563 1.00 28.61 ? 629 HOH C O   1 
HETATM 9567 O  O   . HOH Y 6 .   ? 53.982  -9.423  -19.372 1.00 38.56 ? 630 HOH C O   1 
HETATM 9568 O  O   . HOH Y 6 .   ? 43.441  -16.518 -22.266 1.00 37.46 ? 631 HOH C O   1 
HETATM 9569 O  O   . HOH Y 6 .   ? 37.518  5.852   -28.037 1.00 22.44 ? 632 HOH C O   1 
HETATM 9570 O  O   . HOH Y 6 .   ? 56.024  12.065  -42.996 1.00 39.30 ? 633 HOH C O   1 
HETATM 9571 O  O   . HOH Y 6 .   ? 53.984  5.001   -26.051 1.00 24.68 ? 634 HOH C O   1 
HETATM 9572 O  O   . HOH Y 6 .   ? 25.366  -12.537 -26.186 1.00 33.22 ? 635 HOH C O   1 
HETATM 9573 O  O   . HOH Y 6 .   ? 31.443  -11.206 -12.209 1.00 30.59 ? 636 HOH C O   1 
HETATM 9574 O  O   . HOH Y 6 .   ? 40.095  12.749  -46.369 1.00 38.40 ? 637 HOH C O   1 
HETATM 9575 O  O   . HOH Y 6 .   ? 45.201  15.284  -32.348 1.00 45.91 ? 638 HOH C O   1 
HETATM 9576 O  O   . HOH Y 6 .   ? 56.416  -11.614 -30.428 1.00 37.35 ? 639 HOH C O   1 
HETATM 9577 O  O   . HOH Y 6 .   ? 24.652  5.315   -46.142 1.00 41.15 ? 640 HOH C O   1 
HETATM 9578 O  O   . HOH Y 6 .   ? 48.042  11.619  -26.773 1.00 35.93 ? 641 HOH C O   1 
HETATM 9579 O  O   . HOH Y 6 .   ? 48.376  -15.444 -40.084 1.00 40.95 ? 642 HOH C O   1 
HETATM 9580 O  O   . HOH Y 6 .   ? 31.110  15.469  -44.567 1.00 37.68 ? 643 HOH C O   1 
HETATM 9581 O  O   . HOH Y 6 .   ? 36.583  15.782  -25.710 1.00 35.54 ? 644 HOH C O   1 
HETATM 9582 O  O   . HOH Y 6 .   ? 33.736  21.241  -29.927 1.00 44.96 ? 645 HOH C O   1 
HETATM 9583 O  O   . HOH Y 6 .   ? 35.466  1.208   -50.475 1.00 39.03 ? 646 HOH C O   1 
HETATM 9584 O  O   . HOH Y 6 .   ? 28.227  15.479  -45.521 1.00 36.68 ? 647 HOH C O   1 
HETATM 9585 O  O   . HOH Y 6 .   ? 40.414  6.716   -7.496  1.00 39.20 ? 648 HOH C O   1 
HETATM 9586 O  O   . HOH Y 6 .   ? 22.533  -2.738  -34.038 1.00 30.31 ? 649 HOH C O   1 
HETATM 9587 O  O   . HOH Y 6 .   ? 22.409  8.712   -27.896 1.00 16.95 ? 650 HOH C O   1 
HETATM 9588 O  O   . HOH Y 6 .   ? 44.561  9.409   -7.148  1.00 39.93 ? 651 HOH C O   1 
HETATM 9589 O  O   . HOH Y 6 .   ? 21.820  -3.930  -38.099 1.00 25.64 ? 652 HOH C O   1 
HETATM 9590 O  O   . HOH Y 6 .   ? 41.261  14.130  -33.830 1.00 36.49 ? 653 HOH C O   1 
HETATM 9591 O  O   . HOH Y 6 .   ? 18.844  15.858  -21.127 1.00 31.54 ? 654 HOH C O   1 
HETATM 9592 O  O   . HOH Y 6 .   ? 28.301  27.127  -30.717 1.00 25.96 ? 655 HOH C O   1 
HETATM 9593 O  O   . HOH Y 6 .   ? 38.407  -2.376  -48.867 1.00 34.94 ? 656 HOH C O   1 
HETATM 9594 O  O   . HOH Y 6 .   ? 45.258  -16.009 -45.814 1.00 30.67 ? 657 HOH C O   1 
HETATM 9595 O  O   . HOH Y 6 .   ? 31.015  -14.441 -35.232 1.00 36.20 ? 658 HOH C O   1 
HETATM 9596 O  O   . HOH Y 6 .   ? 40.252  16.876  -37.041 1.00 33.71 ? 659 HOH C O   1 
HETATM 9597 O  O   . HOH Y 6 .   ? 41.833  -25.977 -44.843 1.00 36.22 ? 660 HOH C O   1 
HETATM 9598 O  O   . HOH Y 6 .   ? 46.854  -13.194 -15.001 1.00 35.49 ? 661 HOH C O   1 
HETATM 9599 O  O   . HOH Y 6 .   ? 48.231  11.719  -30.618 1.00 33.76 ? 662 HOH C O   1 
HETATM 9600 O  O   . HOH Y 6 .   ? 27.046  20.839  -30.621 1.00 32.03 ? 663 HOH C O   1 
HETATM 9601 O  O   . HOH Y 6 .   ? 41.849  -10.597 -56.702 1.00 20.85 ? 664 HOH C O   1 
HETATM 9602 O  O   . HOH Y 6 .   ? 35.935  18.075  -38.289 1.00 22.96 ? 665 HOH C O   1 
HETATM 9603 O  O   . HOH Y 6 .   ? 51.147  16.018  -43.999 1.00 36.53 ? 666 HOH C O   1 
HETATM 9604 O  O   . HOH Y 6 .   ? 34.479  9.776   -47.938 1.00 36.10 ? 667 HOH C O   1 
HETATM 9605 O  O   . HOH Y 6 .   ? 48.755  -11.270 -53.033 1.00 23.02 ? 668 HOH C O   1 
HETATM 9606 O  O   . HOH Y 6 .   ? 30.276  6.355   -50.065 1.00 35.39 ? 669 HOH C O   1 
HETATM 9607 O  O   . HOH Y 6 .   ? 25.742  -11.092 -17.231 1.00 36.03 ? 670 HOH C O   1 
HETATM 9608 O  O   . HOH Y 6 .   ? 40.271  -14.983 -56.563 1.00 28.78 ? 671 HOH C O   1 
HETATM 9609 O  O   . HOH Y 6 .   ? 35.914  13.818  -46.119 1.00 34.59 ? 672 HOH C O   1 
HETATM 9610 O  O   . HOH Y 6 .   ? 28.138  -15.140 -35.621 1.00 32.92 ? 673 HOH C O   1 
HETATM 9611 O  O   . HOH Y 6 .   ? 33.996  12.053  -47.851 1.00 27.39 ? 674 HOH C O   1 
HETATM 9612 O  O   . HOH Y 6 .   ? 29.634  12.742  -52.206 1.00 42.45 ? 675 HOH C O   1 
HETATM 9613 O  O   . HOH Z 6 .   ? -7.574  3.510   -21.240 1.00 31.33 ? 401 HOH D O   1 
HETATM 9614 O  O   . HOH Z 6 .   ? 14.185  19.754  -43.118 1.00 32.11 ? 402 HOH D O   1 
HETATM 9615 O  O   . HOH Z 6 .   ? 17.419  -6.601  -56.334 1.00 29.48 ? 403 HOH D O   1 
HETATM 9616 O  O   . HOH Z 6 .   ? 1.433   7.817   -22.833 1.00 37.47 ? 404 HOH D O   1 
HETATM 9617 O  O   . HOH Z 6 .   ? 8.451   -14.500 -37.831 1.00 32.10 ? 405 HOH D O   1 
HETATM 9618 O  O   . HOH Z 6 .   ? -0.255  -10.465 -18.267 1.00 29.90 ? 406 HOH D O   1 
HETATM 9619 O  O   . HOH Z 6 .   ? 23.777  8.933   -45.507 1.00 40.04 ? 407 HOH D O   1 
HETATM 9620 O  O   . HOH Z 6 .   ? -2.270  13.387  -39.211 1.00 27.58 ? 408 HOH D O   1 
HETATM 9621 O  O   . HOH Z 6 .   ? 14.263  -8.334  -52.773 1.00 29.49 ? 409 HOH D O   1 
HETATM 9622 O  O   . HOH Z 6 .   ? 12.429  19.975  -29.553 1.00 27.61 ? 410 HOH D O   1 
HETATM 9623 O  O   . HOH Z 6 .   ? 2.473   14.096  -43.568 1.00 23.77 ? 411 HOH D O   1 
HETATM 9624 O  O   . HOH Z 6 .   ? -12.576 -7.752  -41.349 1.00 25.35 ? 412 HOH D O   1 
HETATM 9625 O  O   . HOH Z 6 .   ? -5.607  -9.531  -34.715 1.00 27.01 ? 413 HOH D O   1 
HETATM 9626 O  O   . HOH Z 6 .   ? -7.182  -2.929  -53.604 1.00 31.06 ? 414 HOH D O   1 
HETATM 9627 O  O   . HOH Z 6 .   ? -6.351  4.328   -24.497 1.00 24.79 ? 415 HOH D O   1 
HETATM 9628 O  O   . HOH Z 6 .   ? 12.711  11.268  -46.327 1.00 26.37 ? 416 HOH D O   1 
HETATM 9629 O  O   . HOH Z 6 .   ? 22.679  13.809  -28.806 1.00 22.11 ? 417 HOH D O   1 
HETATM 9630 O  O   . HOH Z 6 .   ? -6.138  13.703  -37.453 1.00 22.05 ? 418 HOH D O   1 
HETATM 9631 O  O   . HOH Z 6 .   ? -2.158  11.292  -58.514 1.00 37.45 ? 419 HOH D O   1 
HETATM 9632 O  O   . HOH Z 6 .   ? 4.214   -0.905  -14.773 1.00 36.39 ? 420 HOH D O   1 
HETATM 9633 O  O   . HOH Z 6 .   ? 12.065  7.070   -39.511 1.00 9.19  ? 421 HOH D O   1 
HETATM 9634 O  O   . HOH Z 6 .   ? -9.974  15.130  -20.853 1.00 28.38 ? 422 HOH D O   1 
HETATM 9635 O  O   . HOH Z 6 .   ? -14.644 4.752   -37.353 1.00 23.20 ? 423 HOH D O   1 
HETATM 9636 O  O   . HOH Z 6 .   ? -5.737  -5.622  -54.003 1.00 26.52 ? 424 HOH D O   1 
HETATM 9637 O  O   . HOH Z 6 .   ? -12.083 -8.964  -44.819 1.00 39.88 ? 425 HOH D O   1 
HETATM 9638 O  O   . HOH Z 6 .   ? -2.489  13.345  -41.941 1.00 26.16 ? 426 HOH D O   1 
HETATM 9639 O  O   . HOH Z 6 .   ? 11.154  17.840  -54.780 1.00 25.91 ? 427 HOH D O   1 
HETATM 9640 O  O   . HOH Z 6 .   ? -10.645 11.808  -26.196 1.00 20.44 ? 428 HOH D O   1 
HETATM 9641 O  O   . HOH Z 6 .   ? 20.579  14.035  -47.978 1.00 20.76 ? 429 HOH D O   1 
HETATM 9642 O  O   . HOH Z 6 .   ? -1.929  -9.003  -16.830 1.00 23.03 ? 430 HOH D O   1 
HETATM 9643 O  O   . HOH Z 6 .   ? 20.423  -7.420  -29.915 1.00 19.29 ? 431 HOH D O   1 
HETATM 9644 O  O   . HOH Z 6 .   ? -15.453 -2.251  -43.709 1.00 23.01 ? 432 HOH D O   1 
HETATM 9645 O  O   . HOH Z 6 .   ? 14.192  2.533   -16.773 1.00 32.63 ? 433 HOH D O   1 
HETATM 9646 O  O   . HOH Z 6 .   ? 16.504  18.941  -43.635 1.00 36.47 ? 434 HOH D O   1 
HETATM 9647 O  O   . HOH Z 6 .   ? -5.668  19.523  -21.812 1.00 28.23 ? 435 HOH D O   1 
HETATM 9648 O  O   . HOH Z 6 .   ? -1.614  1.808   -58.296 1.00 48.65 ? 436 HOH D O   1 
HETATM 9649 O  O   . HOH Z 6 .   ? 10.703  13.490  -58.724 1.00 22.36 ? 437 HOH D O   1 
HETATM 9650 O  O   . HOH Z 6 .   ? -3.016  -10.442 -39.603 1.00 23.50 ? 438 HOH D O   1 
HETATM 9651 O  O   . HOH Z 6 .   ? 19.889  8.187   -42.492 1.00 11.90 ? 439 HOH D O   1 
HETATM 9652 O  O   . HOH Z 6 .   ? 8.647   -10.613 -31.356 1.00 17.39 ? 440 HOH D O   1 
HETATM 9653 O  O   . HOH Z 6 .   ? 18.414  -0.040  -20.621 1.00 24.43 ? 441 HOH D O   1 
HETATM 9654 O  O   . HOH Z 6 .   ? 18.400  5.286   -45.980 1.00 17.48 ? 442 HOH D O   1 
HETATM 9655 O  O   . HOH Z 6 .   ? -9.869  8.564   -20.756 1.00 29.00 ? 443 HOH D O   1 
HETATM 9656 O  O   . HOH Z 6 .   ? -18.869 5.367   -40.556 1.00 30.82 ? 444 HOH D O   1 
HETATM 9657 O  O   . HOH Z 6 .   ? 7.535   17.482  -25.456 1.00 31.91 ? 445 HOH D O   1 
HETATM 9658 O  O   . HOH Z 6 .   ? -12.200 10.095  -23.341 1.00 26.58 ? 446 HOH D O   1 
HETATM 9659 O  O   . HOH Z 6 .   ? 6.582   14.952  -38.261 1.00 31.23 ? 447 HOH D O   1 
HETATM 9660 O  O   . HOH Z 6 .   ? 11.966  -6.894  -52.181 1.00 21.94 ? 448 HOH D O   1 
HETATM 9661 O  O   . HOH Z 6 .   ? 23.770  9.095   -35.134 1.00 12.49 ? 449 HOH D O   1 
HETATM 9662 O  O   . HOH Z 6 .   ? 19.237  -3.843  -34.317 1.00 22.64 ? 450 HOH D O   1 
HETATM 9663 O  O   . HOH Z 6 .   ? -5.669  -10.153 -45.244 1.00 31.64 ? 451 HOH D O   1 
HETATM 9664 O  O   . HOH Z 6 .   ? -11.755 11.264  -46.073 1.00 32.38 ? 452 HOH D O   1 
HETATM 9665 O  O   . HOH Z 6 .   ? -2.366  -14.183 -26.320 1.00 43.95 ? 453 HOH D O   1 
HETATM 9666 O  O   . HOH Z 6 .   ? 20.156  -6.826  -44.477 1.00 33.79 ? 454 HOH D O   1 
HETATM 9667 O  O   . HOH Z 6 .   ? -7.261  -6.924  -51.682 1.00 22.02 ? 455 HOH D O   1 
HETATM 9668 O  O   . HOH Z 6 .   ? 19.109  8.506   -29.374 1.00 12.54 ? 456 HOH D O   1 
HETATM 9669 O  O   . HOH Z 6 .   ? 16.563  -10.032 -40.616 1.00 46.62 ? 457 HOH D O   1 
HETATM 9670 O  O   . HOH Z 6 .   ? 19.968  21.783  -33.061 1.00 26.85 ? 458 HOH D O   1 
HETATM 9671 O  O   . HOH Z 6 .   ? -12.930 -1.791  -34.360 1.00 18.85 ? 459 HOH D O   1 
HETATM 9672 O  O   . HOH Z 6 .   ? -10.114 -0.329  -49.594 1.00 17.17 ? 460 HOH D O   1 
HETATM 9673 O  O   . HOH Z 6 .   ? 0.913   2.569   -28.256 1.00 10.63 ? 461 HOH D O   1 
HETATM 9674 O  O   . HOH Z 6 .   ? -6.267  5.240   -56.587 1.00 24.62 ? 462 HOH D O   1 
HETATM 9675 O  O   . HOH Z 6 .   ? 23.770  18.552  -42.806 1.00 18.88 ? 463 HOH D O   1 
HETATM 9676 O  O   . HOH Z 6 .   ? -6.536  -2.461  -21.244 1.00 26.42 ? 464 HOH D O   1 
HETATM 9677 O  O   . HOH Z 6 .   ? 17.867  7.367   -27.279 1.00 15.95 ? 465 HOH D O   1 
HETATM 9678 O  O   . HOH Z 6 .   ? 1.017   9.248   -59.276 1.00 23.44 ? 466 HOH D O   1 
HETATM 9679 O  O   . HOH Z 6 .   ? 18.337  -0.112  -29.539 1.00 13.80 ? 467 HOH D O   1 
HETATM 9680 O  O   . HOH Z 6 .   ? -5.908  -9.855  -42.106 1.00 31.64 ? 468 HOH D O   1 
HETATM 9681 O  O   . HOH Z 6 .   ? 2.044   -11.810 -54.385 1.00 16.93 ? 469 HOH D O   1 
HETATM 9682 O  O   . HOH Z 6 .   ? -8.098  11.915  -37.061 1.00 18.28 ? 470 HOH D O   1 
HETATM 9683 O  O   . HOH Z 6 .   ? 8.909   3.384   -53.145 1.00 13.21 ? 471 HOH D O   1 
HETATM 9684 O  O   . HOH Z 6 .   ? -3.617  -5.621  -26.884 1.00 18.25 ? 472 HOH D O   1 
HETATM 9685 O  O   . HOH Z 6 .   ? 21.228  5.246   -34.341 1.00 9.05  ? 473 HOH D O   1 
HETATM 9686 O  O   . HOH Z 6 .   ? 19.605  11.228  -29.285 1.00 15.29 ? 474 HOH D O   1 
HETATM 9687 O  O   . HOH Z 6 .   ? 9.226   8.336   -43.028 1.00 12.78 ? 475 HOH D O   1 
HETATM 9688 O  O   . HOH Z 6 .   ? 13.136  22.666  -35.284 1.00 31.39 ? 476 HOH D O   1 
HETATM 9689 O  O   . HOH Z 6 .   ? -2.326  11.438  -20.342 1.00 24.36 ? 477 HOH D O   1 
HETATM 9690 O  O   . HOH Z 6 .   ? 2.127   -15.213 -29.851 1.00 25.88 ? 478 HOH D O   1 
HETATM 9691 O  O   . HOH Z 6 .   ? -6.964  11.083  -19.690 1.00 16.01 ? 479 HOH D O   1 
HETATM 9692 O  O   . HOH Z 6 .   ? 20.055  7.475   -35.860 1.00 11.79 ? 480 HOH D O   1 
HETATM 9693 O  O   . HOH Z 6 .   ? 15.963  15.004  -24.137 1.00 30.58 ? 481 HOH D O   1 
HETATM 9694 O  O   . HOH Z 6 .   ? 8.351   -9.009  -14.061 1.00 29.05 ? 482 HOH D O   1 
HETATM 9695 O  O   . HOH Z 6 .   ? -3.009  11.169  -46.240 1.00 18.06 ? 483 HOH D O   1 
HETATM 9696 O  O   . HOH Z 6 .   ? 6.655   -13.847 -51.053 1.00 11.65 ? 484 HOH D O   1 
HETATM 9697 O  O   . HOH Z 6 .   ? -12.091 -4.510  -31.951 1.00 35.05 ? 485 HOH D O   1 
HETATM 9698 O  O   . HOH Z 6 .   ? -3.214  -14.669 -49.512 1.00 26.91 ? 486 HOH D O   1 
HETATM 9699 O  O   . HOH Z 6 .   ? -14.459 9.523   -45.127 1.00 27.58 ? 487 HOH D O   1 
HETATM 9700 O  O   . HOH Z 6 .   ? 11.563  -10.835 -27.713 1.00 34.58 ? 488 HOH D O   1 
HETATM 9701 O  O   . HOH Z 6 .   ? 16.314  0.338   -37.552 1.00 8.99  ? 489 HOH D O   1 
HETATM 9702 O  O   . HOH Z 6 .   ? 13.230  18.598  -32.630 1.00 13.48 ? 490 HOH D O   1 
HETATM 9703 O  O   . HOH Z 6 .   ? 4.242   -6.886  -34.981 1.00 9.13  ? 491 HOH D O   1 
HETATM 9704 O  O   . HOH Z 6 .   ? 14.076  -10.942 -20.614 1.00 32.59 ? 492 HOH D O   1 
HETATM 9705 O  O   . HOH Z 6 .   ? 16.340  19.637  -57.274 1.00 35.89 ? 493 HOH D O   1 
HETATM 9706 O  O   . HOH Z 6 .   ? 5.835   -6.330  -57.648 1.00 15.67 ? 494 HOH D O   1 
HETATM 9707 O  O   . HOH Z 6 .   ? 5.682   -0.191  -57.988 1.00 28.49 ? 495 HOH D O   1 
HETATM 9708 O  O   . HOH Z 6 .   ? 4.534   16.023  -57.213 1.00 17.53 ? 496 HOH D O   1 
HETATM 9709 O  O   . HOH Z 6 .   ? 6.001   17.700  -33.643 1.00 26.31 ? 497 HOH D O   1 
HETATM 9710 O  O   . HOH Z 6 .   ? 19.488  18.904  -40.434 1.00 23.78 ? 498 HOH D O   1 
HETATM 9711 O  O   . HOH Z 6 .   ? 11.824  -3.562  -47.453 1.00 11.84 ? 499 HOH D O   1 
HETATM 9712 O  O   . HOH Z 6 .   ? -8.489  -0.131  -51.895 1.00 16.19 ? 500 HOH D O   1 
HETATM 9713 O  O   . HOH Z 6 .   ? -2.568  -8.691  -41.860 1.00 14.96 ? 501 HOH D O   1 
HETATM 9714 O  O   . HOH Z 6 .   ? 22.789  6.476   -38.330 1.00 10.12 ? 502 HOH D O   1 
HETATM 9715 O  O   . HOH Z 6 .   ? 22.789  6.698   -23.942 1.00 26.14 ? 503 HOH D O   1 
HETATM 9716 O  O   . HOH Z 6 .   ? -5.741  -7.004  -27.911 1.00 21.09 ? 504 HOH D O   1 
HETATM 9717 O  O   . HOH Z 6 .   ? 7.519   -4.808  -14.612 1.00 28.31 ? 505 HOH D O   1 
HETATM 9718 O  O   . HOH Z 6 .   ? -2.887  15.248  -47.923 1.00 41.10 ? 506 HOH D O   1 
HETATM 9719 O  O   . HOH Z 6 .   ? 0.302   -12.616 -37.111 1.00 16.47 ? 507 HOH D O   1 
HETATM 9720 O  O   . HOH Z 6 .   ? 9.672   -13.276 -55.733 1.00 42.66 ? 508 HOH D O   1 
HETATM 9721 O  O   . HOH Z 6 .   ? -0.001  0.071   -56.948 1.00 29.50 ? 509 HOH D O   1 
HETATM 9722 O  O   . HOH Z 6 .   ? -12.268 -4.824  -44.666 1.00 24.23 ? 510 HOH D O   1 
HETATM 9723 O  O   . HOH Z 6 .   ? 18.623  -3.248  -43.190 1.00 25.10 ? 511 HOH D O   1 
HETATM 9724 O  O   . HOH Z 6 .   ? 20.701  13.643  -35.766 1.00 9.51  ? 512 HOH D O   1 
HETATM 9725 O  O   . HOH Z 6 .   ? -6.885  0.210   -56.260 1.00 26.32 ? 513 HOH D O   1 
HETATM 9726 O  O   . HOH Z 6 .   ? 21.043  2.598   -21.217 1.00 29.03 ? 514 HOH D O   1 
HETATM 9727 O  O   . HOH Z 6 .   ? 21.681  -9.488  -26.150 1.00 31.98 ? 515 HOH D O   1 
HETATM 9728 O  O   . HOH Z 6 .   ? 18.022  17.068  -49.003 1.00 36.37 ? 516 HOH D O   1 
HETATM 9729 O  O   . HOH Z 6 .   ? -10.686 19.534  -31.167 1.00 29.54 ? 517 HOH D O   1 
HETATM 9730 O  O   . HOH Z 6 .   ? 8.723   16.648  -42.030 1.00 35.34 ? 518 HOH D O   1 
HETATM 9731 O  O   . HOH Z 6 .   ? -12.361 -3.716  -36.230 1.00 22.26 ? 519 HOH D O   1 
HETATM 9732 O  O   . HOH Z 6 .   ? 11.022  3.822   -55.372 1.00 17.79 ? 520 HOH D O   1 
HETATM 9733 O  O   . HOH Z 6 .   ? 6.010   -14.732 -33.754 1.00 40.01 ? 521 HOH D O   1 
HETATM 9734 O  O   . HOH Z 6 .   ? -4.885  10.036  -57.575 1.00 37.75 ? 522 HOH D O   1 
HETATM 9735 O  O   . HOH Z 6 .   ? 0.960   -4.948  -54.545 1.00 25.74 ? 523 HOH D O   1 
HETATM 9736 O  O   . HOH Z 6 .   ? 16.936  6.763   -49.030 1.00 29.17 ? 524 HOH D O   1 
HETATM 9737 O  O   . HOH Z 6 .   ? 10.211  2.466   -21.602 1.00 17.26 ? 525 HOH D O   1 
HETATM 9738 O  O   . HOH Z 6 .   ? 0.703   19.553  -21.936 1.00 35.17 ? 526 HOH D O   1 
HETATM 9739 O  O   . HOH Z 6 .   ? -9.856  16.028  -28.626 1.00 39.33 ? 527 HOH D O   1 
HETATM 9740 O  O   . HOH Z 6 .   ? 17.316  -11.406 -27.433 1.00 22.20 ? 528 HOH D O   1 
HETATM 9741 O  O   . HOH Z 6 .   ? 0.606   -8.267  -19.043 1.00 19.86 ? 529 HOH D O   1 
HETATM 9742 O  O   . HOH Z 6 .   ? 20.633  9.544   -26.034 1.00 27.30 ? 530 HOH D O   1 
HETATM 9743 O  O   . HOH Z 6 .   ? 10.862  13.814  -61.422 1.00 33.22 ? 531 HOH D O   1 
HETATM 9744 O  O   . HOH Z 6 .   ? 18.959  4.979   -49.207 1.00 26.71 ? 532 HOH D O   1 
HETATM 9745 O  O   . HOH Z 6 .   ? 5.346   12.205  -23.032 1.00 24.66 ? 533 HOH D O   1 
HETATM 9746 O  O   . HOH Z 6 .   ? -2.329  -7.868  -22.678 1.00 18.17 ? 534 HOH D O   1 
HETATM 9747 O  O   . HOH Z 6 .   ? 4.418   9.618   -42.768 1.00 19.70 ? 535 HOH D O   1 
HETATM 9748 O  O   . HOH Z 6 .   ? 2.445   9.409   -24.959 1.00 17.63 ? 536 HOH D O   1 
HETATM 9749 O  O   . HOH Z 6 .   ? 14.539  -12.001 -34.314 1.00 32.32 ? 537 HOH D O   1 
HETATM 9750 O  O   . HOH Z 6 .   ? 12.595  -9.682  -46.207 1.00 18.47 ? 538 HOH D O   1 
HETATM 9751 O  O   . HOH Z 6 .   ? 8.546   -13.573 -29.803 1.00 39.22 ? 539 HOH D O   1 
HETATM 9752 O  O   . HOH Z 6 .   ? 13.666  7.545   -48.248 1.00 20.42 ? 540 HOH D O   1 
HETATM 9753 O  O   . HOH Z 6 .   ? 18.939  -0.201  -36.863 1.00 13.40 ? 541 HOH D O   1 
HETATM 9754 O  O   . HOH Z 6 .   ? 8.159   -16.433 -45.163 1.00 26.65 ? 542 HOH D O   1 
HETATM 9755 O  O   . HOH Z 6 .   ? 14.130  5.919   -60.638 1.00 35.92 ? 543 HOH D O   1 
HETATM 9756 O  O   . HOH Z 6 .   ? 15.535  9.798   -48.072 1.00 20.92 ? 544 HOH D O   1 
HETATM 9757 O  O   . HOH Z 6 .   ? 12.058  1.948   -18.165 1.00 20.45 ? 545 HOH D O   1 
HETATM 9758 O  O   . HOH Z 6 .   ? 3.209   -13.701 -39.749 1.00 32.28 ? 546 HOH D O   1 
HETATM 9759 O  O   . HOH Z 6 .   ? -10.406 -4.751  -30.120 1.00 29.90 ? 547 HOH D O   1 
HETATM 9760 O  O   . HOH Z 6 .   ? 5.724   21.431  -25.588 1.00 20.71 ? 548 HOH D O   1 
HETATM 9761 O  O   . HOH Z 6 .   ? 26.211  16.207  -43.651 1.00 27.96 ? 549 HOH D O   1 
HETATM 9762 O  O   . HOH Z 6 .   ? -8.581  9.017   -55.885 1.00 24.22 ? 550 HOH D O   1 
HETATM 9763 O  O   . HOH Z 6 .   ? -2.747  -0.634  -16.859 1.00 26.11 ? 551 HOH D O   1 
HETATM 9764 O  O   . HOH Z 6 .   ? -13.004 8.629   -55.554 1.00 27.03 ? 552 HOH D O   1 
HETATM 9765 O  O   . HOH Z 6 .   ? 14.282  13.959  -27.408 1.00 14.96 ? 553 HOH D O   1 
HETATM 9766 O  O   . HOH Z 6 .   ? 8.802   -10.084 -58.276 1.00 24.28 ? 554 HOH D O   1 
HETATM 9767 O  O   . HOH Z 6 .   ? -11.502 -7.398  -36.934 1.00 32.43 ? 555 HOH D O   1 
HETATM 9768 O  O   . HOH Z 6 .   ? 0.688   -11.997 -13.889 1.00 31.06 ? 556 HOH D O   1 
HETATM 9769 O  O   . HOH Z 6 .   ? -16.287 4.436   -41.330 1.00 19.54 ? 557 HOH D O   1 
HETATM 9770 O  O   . HOH Z 6 .   ? -0.126  -12.090 -42.375 1.00 16.09 ? 558 HOH D O   1 
HETATM 9771 O  O   . HOH Z 6 .   ? 18.664  -4.430  -18.270 1.00 31.02 ? 559 HOH D O   1 
HETATM 9772 O  O   . HOH Z 6 .   ? 18.906  10.164  -35.851 1.00 9.86  ? 560 HOH D O   1 
HETATM 9773 O  O   . HOH Z 6 .   ? 18.697  -0.742  -46.461 1.00 27.63 ? 561 HOH D O   1 
HETATM 9774 O  O   . HOH Z 6 .   ? -9.301  11.115  -45.236 1.00 17.89 ? 562 HOH D O   1 
HETATM 9775 O  O   . HOH Z 6 .   ? -13.900 -1.321  -49.497 1.00 24.58 ? 563 HOH D O   1 
HETATM 9776 O  O   . HOH Z 6 .   ? 7.721   9.165   -24.437 1.00 20.40 ? 564 HOH D O   1 
HETATM 9777 O  O   . HOH Z 6 .   ? -18.009 -1.694  -45.189 1.00 35.38 ? 565 HOH D O   1 
HETATM 9778 O  O   . HOH Z 6 .   ? -17.011 3.566   -52.035 1.00 32.57 ? 566 HOH D O   1 
HETATM 9779 O  O   . HOH Z 6 .   ? -8.424  13.545  -44.759 1.00 27.31 ? 567 HOH D O   1 
HETATM 9780 O  O   . HOH Z 6 .   ? 21.206  6.852   -29.770 1.00 12.04 ? 568 HOH D O   1 
HETATM 9781 O  O   . HOH Z 6 .   ? 1.431   -17.368 -26.973 1.00 49.86 ? 569 HOH D O   1 
HETATM 9782 O  O   . HOH Z 6 .   ? 8.557   17.694  -27.690 1.00 21.34 ? 570 HOH D O   1 
HETATM 9783 O  O   . HOH Z 6 .   ? 17.110  7.693   -55.990 1.00 29.86 ? 571 HOH D O   1 
HETATM 9784 O  O   . HOH Z 6 .   ? -4.122  15.512  -45.162 1.00 38.32 ? 572 HOH D O   1 
HETATM 9785 O  O   . HOH Z 6 .   ? 18.657  -13.168 -33.310 1.00 30.52 ? 573 HOH D O   1 
HETATM 9786 O  O   . HOH Z 6 .   ? -12.383 5.598   -53.488 1.00 32.40 ? 574 HOH D O   1 
HETATM 9787 O  O   . HOH Z 6 .   ? -5.482  -13.658 -32.719 1.00 27.12 ? 575 HOH D O   1 
HETATM 9788 O  O   . HOH Z 6 .   ? 13.393  1.346   -55.974 1.00 22.75 ? 576 HOH D O   1 
HETATM 9789 O  O   . HOH Z 6 .   ? 11.154  -10.523 -43.962 1.00 22.40 ? 577 HOH D O   1 
HETATM 9790 O  O   . HOH Z 6 .   ? 23.422  10.546  -41.663 1.00 17.34 ? 578 HOH D O   1 
HETATM 9791 O  O   . HOH Z 6 .   ? 19.319  -7.677  -17.703 1.00 35.67 ? 579 HOH D O   1 
HETATM 9792 O  O   . HOH Z 6 .   ? -16.007 9.586   -47.495 1.00 23.29 ? 580 HOH D O   1 
HETATM 9793 O  O   . HOH Z 6 .   ? -14.521 11.995  -49.824 1.00 44.54 ? 581 HOH D O   1 
HETATM 9794 O  O   . HOH Z 6 .   ? 11.003  14.820  -49.015 1.00 27.45 ? 582 HOH D O   1 
HETATM 9795 O  O   . HOH Z 6 .   ? 1.146   -9.851  -31.403 1.00 11.56 ? 583 HOH D O   1 
HETATM 9796 O  O   . HOH Z 6 .   ? 0.823   24.107  -30.258 1.00 33.78 ? 584 HOH D O   1 
HETATM 9797 O  O   . HOH Z 6 .   ? 8.980   20.178  -32.058 1.00 22.57 ? 585 HOH D O   1 
HETATM 9798 O  O   . HOH Z 6 .   ? -11.843 12.653  -38.275 1.00 29.82 ? 586 HOH D O   1 
HETATM 9799 O  O   . HOH Z 6 .   ? -12.659 -4.349  -47.666 1.00 30.42 ? 587 HOH D O   1 
HETATM 9800 O  O   . HOH Z 6 .   ? -17.875 8.436   -50.303 1.00 38.81 ? 588 HOH D O   1 
HETATM 9801 O  O   . HOH Z 6 .   ? -4.055  9.893   -17.537 1.00 22.20 ? 589 HOH D O   1 
HETATM 9802 O  O   . HOH Z 6 .   ? 21.881  1.426   -25.233 1.00 26.70 ? 590 HOH D O   1 
HETATM 9803 O  O   . HOH Z 6 .   ? 22.037  3.817   -23.511 1.00 23.05 ? 591 HOH D O   1 
HETATM 9804 O  O   . HOH Z 6 .   ? 18.260  23.213  -34.301 1.00 21.69 ? 592 HOH D O   1 
HETATM 9805 O  O   . HOH Z 6 .   ? 8.549   21.747  -29.775 1.00 20.73 ? 593 HOH D O   1 
HETATM 9806 O  O   . HOH Z 6 .   ? -15.253 -0.566  -35.782 1.00 23.72 ? 594 HOH D O   1 
HETATM 9807 O  O   . HOH Z 6 .   ? -9.508  0.574   -54.883 1.00 27.05 ? 595 HOH D O   1 
HETATM 9808 O  O   . HOH Z 6 .   ? 13.770  16.434  -26.578 1.00 21.27 ? 596 HOH D O   1 
HETATM 9809 O  O   . HOH Z 6 .   ? 11.691  8.980   -47.264 1.00 22.29 ? 597 HOH D O   1 
HETATM 9810 O  O   . HOH Z 6 .   ? -5.101  -11.204 -28.361 1.00 22.79 ? 598 HOH D O   1 
HETATM 9811 O  O   . HOH Z 6 .   ? -15.412 4.166   -31.920 1.00 28.89 ? 599 HOH D O   1 
HETATM 9812 O  O   . HOH Z 6 .   ? 18.502  -7.639  -40.314 1.00 20.78 ? 600 HOH D O   1 
HETATM 9813 O  O   . HOH Z 6 .   ? -1.949  -4.090  -56.212 1.00 39.58 ? 601 HOH D O   1 
HETATM 9814 O  O   . HOH Z 6 .   ? 10.497  -10.528 -16.942 1.00 26.32 ? 602 HOH D O   1 
HETATM 9815 O  O   . HOH Z 6 .   ? -5.744  -10.868 -31.210 1.00 28.12 ? 603 HOH D O   1 
HETATM 9816 O  O   . HOH Z 6 .   ? 2.290   1.752   -20.400 1.00 30.01 ? 604 HOH D O   1 
HETATM 9817 O  O   . HOH Z 6 .   ? 21.362  -11.965 -23.321 1.00 35.71 ? 605 HOH D O   1 
HETATM 9818 O  O   . HOH Z 6 .   ? 20.623  -4.002  -28.695 1.00 29.16 ? 606 HOH D O   1 
HETATM 9819 O  O   . HOH Z 6 .   ? -0.334  -12.738 -45.551 1.00 16.90 ? 607 HOH D O   1 
HETATM 9820 O  O   . HOH Z 6 .   ? 0.254   13.244  -40.176 1.00 19.46 ? 608 HOH D O   1 
HETATM 9821 O  O   . HOH Z 6 .   ? 1.465   4.382   -20.209 1.00 43.51 ? 609 HOH D O   1 
HETATM 9822 O  O   . HOH Z 6 .   ? -14.655 10.588  -37.248 1.00 37.96 ? 610 HOH D O   1 
HETATM 9823 O  O   . HOH Z 6 .   ? -17.234 -4.090  -36.572 1.00 32.09 ? 611 HOH D O   1 
HETATM 9824 O  O   . HOH Z 6 .   ? -14.341 12.846  -53.969 1.00 47.54 ? 612 HOH D O   1 
HETATM 9825 O  O   . HOH Z 6 .   ? 4.008   24.129  -28.369 1.00 30.71 ? 613 HOH D O   1 
HETATM 9826 O  O   . HOH Z 6 .   ? -2.686  13.867  -56.822 1.00 25.57 ? 614 HOH D O   1 
HETATM 9827 O  O   . HOH Z 6 .   ? -8.767  16.523  -34.488 1.00 39.89 ? 615 HOH D O   1 
HETATM 9828 O  O   . HOH Z 6 .   ? 5.550   18.755  -59.317 1.00 27.54 ? 616 HOH D O   1 
HETATM 9829 O  O   . HOH Z 6 .   ? 13.497  -11.098 -39.186 1.00 34.58 ? 617 HOH D O   1 
HETATM 9830 O  O   . HOH Z 6 .   ? 16.097  24.346  -34.458 1.00 24.96 ? 618 HOH D O   1 
HETATM 9831 O  O   . HOH Z 6 .   ? 9.891   -10.742 -20.938 1.00 36.64 ? 619 HOH D O   1 
HETATM 9832 O  O   . HOH Z 6 .   ? 18.377  17.119  -41.988 1.00 31.46 ? 620 HOH D O   1 
HETATM 9833 O  O   . HOH Z 6 .   ? 18.803  11.658  -50.383 1.00 34.25 ? 621 HOH D O   1 
HETATM 9834 O  O   . HOH Z 6 .   ? 15.949  1.863   -55.745 1.00 37.98 ? 622 HOH D O   1 
HETATM 9835 O  O   . HOH Z 6 .   ? -16.273 3.353   -38.858 1.00 34.90 ? 623 HOH D O   1 
HETATM 9836 O  O   . HOH Z 6 .   ? 3.886   18.708  -51.204 1.00 39.23 ? 624 HOH D O   1 
HETATM 9837 O  O   . HOH Z 6 .   ? 22.450  -1.533  -40.005 1.00 20.49 ? 625 HOH D O   1 
HETATM 9838 O  O   . HOH Z 6 .   ? 16.118  16.315  -54.478 1.00 50.33 ? 626 HOH D O   1 
HETATM 9839 O  O   . HOH Z 6 .   ? 12.601  -2.916  -12.884 1.00 46.13 ? 627 HOH D O   1 
HETATM 9840 O  O   . HOH Z 6 .   ? 5.070   9.516   -23.872 1.00 27.20 ? 628 HOH D O   1 
HETATM 9841 O  O   . HOH Z 6 .   ? -11.986 12.126  -30.694 1.00 38.01 ? 629 HOH D O   1 
HETATM 9842 O  O   . HOH Z 6 .   ? -8.933  -6.654  -29.071 1.00 34.88 ? 630 HOH D O   1 
HETATM 9843 O  O   . HOH Z 6 .   ? -2.794  -14.610 -39.573 1.00 30.47 ? 631 HOH D O   1 
HETATM 9844 O  O   . HOH Z 6 .   ? 6.901   -15.333 -30.907 1.00 46.56 ? 632 HOH D O   1 
HETATM 9845 O  O   . HOH Z 6 .   ? -8.665  19.361  -26.230 1.00 37.45 ? 633 HOH D O   1 
HETATM 9846 O  O   . HOH Z 6 .   ? -15.353 7.056   -40.990 1.00 25.95 ? 634 HOH D O   1 
HETATM 9847 O  O   . HOH Z 6 .   ? 20.592  -0.858  -41.910 1.00 28.68 ? 635 HOH D O   1 
HETATM 9848 O  O   . HOH Z 6 .   ? -3.017  -12.442 -45.554 1.00 28.30 ? 636 HOH D O   1 
HETATM 9849 O  O   . HOH Z 6 .   ? 6.833   8.428   -41.654 1.00 15.83 ? 637 HOH D O   1 
HETATM 9850 O  O   . HOH Z 6 .   ? 22.126  -6.187  -47.039 1.00 33.38 ? 638 HOH D O   1 
HETATM 9851 O  O   . HOH Z 6 .   ? -16.314 9.965   -54.968 1.00 26.29 ? 639 HOH D O   1 
HETATM 9852 O  O   . HOH Z 6 .   ? 18.309  15.699  -23.965 1.00 35.94 ? 640 HOH D O   1 
HETATM 9853 O  O   . HOH Z 6 .   ? -0.717  23.306  -34.195 1.00 38.28 ? 641 HOH D O   1 
HETATM 9854 O  O   . HOH Z 6 .   ? -17.228 2.167   -37.073 1.00 34.88 ? 642 HOH D O   1 
HETATM 9855 O  O   . HOH Z 6 .   ? 9.868   19.967  -28.117 1.00 29.81 ? 643 HOH D O   1 
HETATM 9856 O  O   . HOH Z 6 .   ? 6.910   -4.085  -58.623 1.00 26.68 ? 644 HOH D O   1 
HETATM 9857 O  O   . HOH Z 6 .   ? 1.800   -7.436  -55.787 1.00 30.25 ? 645 HOH D O   1 
HETATM 9858 O  O   . HOH Z 6 .   ? 20.475  4.046   -46.972 1.00 28.53 ? 646 HOH D O   1 
HETATM 9859 O  O   . HOH Z 6 .   ? 1.796   15.680  -45.945 1.00 41.24 ? 647 HOH D O   1 
HETATM 9860 O  O   . HOH Z 6 .   ? -22.271 6.388   -49.311 1.00 26.76 ? 648 HOH D O   1 
HETATM 9861 O  O   . HOH Z 6 .   ? 22.130  -7.374  -27.679 1.00 24.90 ? 649 HOH D O   1 
HETATM 9862 O  O   . HOH Z 6 .   ? 14.315  -11.442 -47.659 1.00 30.07 ? 650 HOH D O   1 
HETATM 9863 O  O   . HOH Z 6 .   ? 4.751   -16.566 -30.107 1.00 42.19 ? 651 HOH D O   1 
HETATM 9864 O  O   . HOH Z 6 .   ? 4.869   22.253  -52.200 1.00 37.59 ? 652 HOH D O   1 
HETATM 9865 O  O   . HOH Z 6 .   ? -3.692  -11.856 -42.891 1.00 39.23 ? 653 HOH D O   1 
HETATM 9866 O  O   . HOH Z 6 .   ? 12.077  -12.411 -56.798 1.00 30.93 ? 654 HOH D O   1 
HETATM 9867 O  O   . HOH Z 6 .   ? 0.860   -14.640 -41.952 1.00 31.27 ? 655 HOH D O   1 
HETATM 9868 O  O   . HOH Z 6 .   ? -6.658  7.861   -57.616 1.00 29.22 ? 656 HOH D O   1 
HETATM 9869 O  O   . HOH Z 6 .   ? -2.060  -11.484 -41.345 1.00 29.39 ? 657 HOH D O   1 
HETATM 9870 O  O   . HOH Z 6 .   ? 22.487  7.767   -42.582 1.00 21.90 ? 658 HOH D O   1 
HETATM 9871 O  O   . HOH Z 6 .   ? 21.029  -3.865  -32.212 1.00 27.63 ? 659 HOH D O   1 
HETATM 9872 O  O   . HOH Z 6 .   ? 27.580  13.182  -47.315 1.00 30.26 ? 660 HOH D O   1 
HETATM 9873 O  O   . HOH Z 6 .   ? 3.868   17.092  -48.924 1.00 42.43 ? 661 HOH D O   1 
HETATM 9874 O  O   . HOH Z 6 .   ? 3.209   -6.652  -58.246 1.00 23.99 ? 662 HOH D O   1 
HETATM 9875 O  O   . HOH Z 6 .   ? -14.914 9.333   -42.246 1.00 28.19 ? 663 HOH D O   1 
HETATM 9876 O  O   . HOH Z 6 .   ? -1.362  -12.381 -39.248 1.00 28.78 ? 664 HOH D O   1 
HETATM 9877 O  O   . HOH Z 6 .   ? 4.937   -2.406  -59.124 1.00 27.55 ? 665 HOH D O   1 
HETATM 9878 O  O   . HOH Z 6 .   ? 7.049   20.136  -33.357 1.00 43.54 ? 666 HOH D O   1 
HETATM 9879 O  O   . HOH Z 6 .   ? 16.173  -13.832 -26.766 1.00 37.04 ? 667 HOH D O   1 
HETATM 9880 O  O   . HOH Z 6 .   ? 1.448   -15.507 -39.960 1.00 36.53 ? 668 HOH D O   1 
HETATM 9881 O  O   . HOH Z 6 .   ? -6.942  -9.248  -26.990 1.00 29.29 ? 669 HOH D O   1 
HETATM 9882 O  O   . HOH Z 6 .   ? -11.693 -2.385  -50.006 1.00 26.76 ? 670 HOH D O   1 
HETATM 9883 O  O   . HOH Z 6 .   ? 5.450   18.429  -36.331 1.00 34.00 ? 671 HOH D O   1 
HETATM 9884 O  O   . HOH Z 6 .   ? -4.017  -8.709  -18.675 1.00 22.55 ? 672 HOH D O   1 
HETATM 9885 O  O   . HOH Z 6 .   ? 19.876  -11.098 -27.453 1.00 27.74 ? 673 HOH D O   1 
HETATM 9886 O  O   . HOH Z 6 .   ? -3.311  -9.894  -21.241 1.00 24.65 ? 674 HOH D O   1 
HETATM 9887 O  O   . HOH Z 6 .   ? -1.112  -15.307 -44.629 1.00 31.65 ? 675 HOH D O   1 
HETATM 9888 O  O   . HOH Z 6 .   ? -4.682  -14.452 -46.565 1.00 37.32 ? 676 HOH D O   1 
HETATM 9889 O  O   . HOH Z 6 .   ? 9.978   -11.875 -33.504 1.00 29.24 ? 677 HOH D O   1 
HETATM 9890 O  O   . HOH Z 6 .   ? 8.953   -13.188 -17.169 1.00 42.39 ? 678 HOH D O   1 
HETATM 9891 O  O   . HOH Z 6 .   ? 19.626  -5.612  -42.002 1.00 24.53 ? 679 HOH D O   1 
HETATM 9892 O  O   . HOH Z 6 .   ? 20.191  1.258   -45.525 1.00 30.02 ? 680 HOH D O   1 
HETATM 9893 O  O   . HOH Z 6 .   ? -6.602  -8.984  -53.127 1.00 25.46 ? 681 HOH D O   1 
HETATM 9894 O  O   . HOH Z 6 .   ? 5.188   -15.481 -36.520 1.00 38.79 ? 682 HOH D O   1 
HETATM 9895 O  O   . HOH Z 6 .   ? 10.462  3.906   -19.336 1.00 22.63 ? 683 HOH D O   1 
HETATM 9896 O  O   . HOH Z 6 .   ? 11.712  20.833  -32.837 1.00 26.53 ? 684 HOH D O   1 
HETATM 9897 O  O   . HOH Z 6 .   ? 27.464  13.247  -49.895 1.00 32.19 ? 685 HOH D O   1 
HETATM 9898 O  O   . HOH Z 6 .   ? 14.774  26.393  -35.409 1.00 28.77 ? 686 HOH D O   1 
HETATM 9899 O  O   . HOH Z 6 .   ? 6.942   -8.389  -59.189 1.00 24.82 ? 687 HOH D O   1 
HETATM 9900 O  O   . HOH Z 6 .   ? -7.241  -12.555 -46.196 1.00 47.48 ? 688 HOH D O   1 
HETATM 9901 O  O   . HOH Z 6 .   ? 14.529  -12.417 -54.861 1.00 27.07 ? 689 HOH D O   1 
HETATM 9902 O  O   . HOH Z 6 .   ? -6.726  -8.650  -18.314 1.00 23.58 ? 690 HOH D O   1 
HETATM 9903 O  O   . HOH Z 6 .   ? 11.480  6.303   -19.755 1.00 32.20 ? 691 HOH D O   1 
HETATM 9904 O  O   . HOH Z 6 .   ? -8.104  -10.058 -20.589 1.00 36.80 ? 692 HOH D O   1 
HETATM 9905 O  O   . HOH Z 6 .   ? -7.519  -10.857 -24.881 1.00 38.03 ? 693 HOH D O   1 
# 
