data_5LLO
# 
_entry.id   5LLO 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.398 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   5LLO         pdb_00005llo 10.2210/pdb5llo/pdb 
WWPDB D_1200000961 ?            ?                   
# 
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 2017-08-16 
2 'Structure model' 1 1 2018-05-16 
3 'Structure model' 1 2 2024-01-10 
4 'Structure model' 1 3 2024-11-13 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Data collection'        
2 2 'Structure model' 'Database references'    
3 3 'Structure model' 'Data collection'        
4 3 'Structure model' 'Database references'    
5 3 'Structure model' 'Derived calculations'   
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' citation                      
2  2 'Structure model' citation_author               
3  3 'Structure model' chem_comp_atom                
4  3 'Structure model' chem_comp_bond                
5  3 'Structure model' database_2                    
6  3 'Structure model' diffrn_radiation_wavelength   
7  3 'Structure model' pdbx_initial_refinement_model 
8  3 'Structure model' struct_conn                   
9  4 'Structure model' pdbx_entry_details            
10 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' '_citation.country'                   
2  2 'Structure model' '_citation.journal_abbrev'            
3  2 'Structure model' '_citation.journal_id_CSD'            
4  2 'Structure model' '_citation.journal_id_ISSN'           
5  2 'Structure model' '_citation.journal_volume'            
6  2 'Structure model' '_citation.page_first'                
7  2 'Structure model' '_citation.page_last'                 
8  2 'Structure model' '_citation.pdbx_database_id_DOI'      
9  2 'Structure model' '_citation.pdbx_database_id_PubMed'   
10 2 'Structure model' '_citation.title'                     
11 2 'Structure model' '_citation.year'                      
12 2 'Structure model' '_citation_author.name'               
13 3 'Structure model' '_database_2.pdbx_DOI'                
14 3 'Structure model' '_database_2.pdbx_database_accession' 
15 3 'Structure model' '_struct_conn.pdbx_dist_value'        
16 3 'Structure model' '_struct_conn.ptnr1_auth_asym_id'     
17 3 'Structure model' '_struct_conn.ptnr1_auth_comp_id'     
18 3 'Structure model' '_struct_conn.ptnr1_auth_seq_id'      
19 3 'Structure model' '_struct_conn.ptnr1_label_asym_id'    
20 3 'Structure model' '_struct_conn.ptnr1_label_atom_id'    
21 3 'Structure model' '_struct_conn.ptnr1_label_comp_id'    
22 3 'Structure model' '_struct_conn.ptnr1_label_seq_id'     
23 3 'Structure model' '_struct_conn.ptnr2_auth_asym_id'     
24 3 'Structure model' '_struct_conn.ptnr2_auth_comp_id'     
25 3 'Structure model' '_struct_conn.ptnr2_auth_seq_id'      
26 3 'Structure model' '_struct_conn.ptnr2_label_asym_id'    
27 3 'Structure model' '_struct_conn.ptnr2_label_atom_id'    
28 3 '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                        5LLO 
_pdbx_database_status.recvd_initial_deposition_date   2016-07-28 
_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 
'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                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            PeerJ 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2167-8359 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            6 
_citation.language                  ? 
_citation.page_first                e4412 
_citation.page_last                 e4412 
_citation.title                     
'Crystal structure correlations with the intrinsic thermodynamics of human carbonic anhydrase inhibitor binding.' 
_citation.year                      2018 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.7717/peerj.4412 
_citation.pdbx_database_id_PubMed   29503769 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Smirnov, A.'  1 ? 
primary 'Zubriene, A.' 2 ? 
primary 'Manakova, E.' 3 ? 
primary 'Grazulis, S.' 4 ? 
primary 'Matulis, D.'  5 ? 
# 
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    ?       ? '3-[(1S)-2,3-Dihydro-1H-inden-1-ylamino]-2,5,6-trifluoro-4-[(2-hy-droxyethyl)sulfonyl]benzenesulfonamide' ? 
3 non-polymer syn 1,2-ETHANEDIOL                                                                                           62.068 
3    ?       ? Zn                                                                                                        ? 
4 non-polymer syn '3-[(1S)-2,3-dihydro-1H-inden-1-ylamino]-2,5,6-trifluoro-4-[(2-hydroxyethyl)sulfonyl]benzenesulfonamide' 450.452 
4    ?       ? EDO                                                                                                       ? 
5 water       nat water                                                                                                    18.015 
1053 ?       ? ?                                                                                                         ? 
# 
_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 '3-[(1S)-2,3-dihydro-1H-inden-1-ylamino]-2,5,6-trifluoro-4-[(2-hydroxyethyl)sulfonyl]benzenesulfonamide' 5EF 
5 water                                                                                                    HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   SER n 
1 3   LYS n 
1 4   TRP n 
1 5   THR n 
1 6   TYR n 
1 7   PHE n 
1 8   GLY n 
1 9   PRO n 
1 10  ASP n 
1 11  GLY n 
1 12  GLU n 
1 13  ASN n 
1 14  SER n 
1 15  TRP n 
1 16  SER n 
1 17  LYS n 
1 18  LYS n 
1 19  TYR n 
1 20  PRO n 
1 21  SER n 
1 22  CYS n 
1 23  GLY n 
1 24  GLY n 
1 25  LEU n 
1 26  LEU n 
1 27  GLN n 
1 28  SER n 
1 29  PRO n 
1 30  ILE n 
1 31  ASP n 
1 32  LEU n 
1 33  HIS n 
1 34  SER n 
1 35  ASP n 
1 36  ILE n 
1 37  LEU n 
1 38  GLN n 
1 39  TYR n 
1 40  ASP n 
1 41  ALA n 
1 42  SER n 
1 43  LEU n 
1 44  THR n 
1 45  PRO n 
1 46  LEU n 
1 47  GLU n 
1 48  PHE n 
1 49  GLN n 
1 50  GLY n 
1 51  TYR n 
1 52  ASN n 
1 53  LEU n 
1 54  SER n 
1 55  ALA n 
1 56  ASN n 
1 57  LYS n 
1 58  GLN n 
1 59  PHE n 
1 60  LEU n 
1 61  LEU n 
1 62  THR n 
1 63  ASN n 
1 64  ASN n 
1 65  GLY n 
1 66  HIS n 
1 67  SER n 
1 68  VAL n 
1 69  LYS n 
1 70  LEU n 
1 71  ASN n 
1 72  LEU n 
1 73  PRO n 
1 74  SER n 
1 75  ASP n 
1 76  MET n 
1 77  HIS n 
1 78  ILE n 
1 79  GLN n 
1 80  GLY n 
1 81  LEU n 
1 82  GLN n 
1 83  SER n 
1 84  ARG n 
1 85  TYR n 
1 86  SER n 
1 87  ALA n 
1 88  THR n 
1 89  GLN n 
1 90  LEU n 
1 91  HIS n 
1 92  LEU n 
1 93  HIS n 
1 94  TRP n 
1 95  GLY n 
1 96  ASN n 
1 97  PRO n 
1 98  ASN n 
1 99  ASP n 
1 100 PRO n 
1 101 HIS n 
1 102 GLY n 
1 103 SER n 
1 104 GLU n 
1 105 HIS n 
1 106 THR n 
1 107 VAL n 
1 108 SER n 
1 109 GLY n 
1 110 GLN n 
1 111 HIS n 
1 112 PHE n 
1 113 ALA n 
1 114 ALA n 
1 115 GLU n 
1 116 LEU n 
1 117 HIS n 
1 118 ILE n 
1 119 VAL n 
1 120 HIS n 
1 121 TYR n 
1 122 ASN n 
1 123 SER n 
1 124 ASP n 
1 125 LEU n 
1 126 TYR n 
1 127 PRO n 
1 128 ASP n 
1 129 ALA n 
1 130 SER n 
1 131 THR n 
1 132 ALA n 
1 133 SER n 
1 134 ASN n 
1 135 LYS n 
1 136 SER n 
1 137 GLU n 
1 138 GLY n 
1 139 LEU n 
1 140 ALA n 
1 141 VAL n 
1 142 LEU n 
1 143 ALA n 
1 144 VAL n 
1 145 LEU n 
1 146 ILE n 
1 147 GLU n 
1 148 MET n 
1 149 GLY n 
1 150 SER n 
1 151 PHE n 
1 152 ASN n 
1 153 PRO n 
1 154 SER n 
1 155 TYR n 
1 156 ASP n 
1 157 LYS n 
1 158 ILE n 
1 159 PHE n 
1 160 SER n 
1 161 HIS n 
1 162 LEU n 
1 163 GLN n 
1 164 HIS n 
1 165 VAL n 
1 166 LYS n 
1 167 TYR n 
1 168 LYS n 
1 169 GLY n 
1 170 GLN n 
1 171 GLU n 
1 172 ALA n 
1 173 PHE n 
1 174 VAL n 
1 175 PRO n 
1 176 GLY n 
1 177 PHE n 
1 178 ASN n 
1 179 ILE n 
1 180 GLU n 
1 181 GLU n 
1 182 LEU n 
1 183 LEU n 
1 184 PRO n 
1 185 GLU n 
1 186 ARG n 
1 187 THR n 
1 188 ALA n 
1 189 GLU n 
1 190 TYR n 
1 191 TYR n 
1 192 ARG n 
1 193 TYR n 
1 194 ARG n 
1 195 GLY n 
1 196 SER n 
1 197 LEU n 
1 198 THR n 
1 199 THR n 
1 200 PRO n 
1 201 PRO n 
1 202 CYS n 
1 203 ASN n 
1 204 PRO n 
1 205 THR n 
1 206 VAL n 
1 207 LEU n 
1 208 TRP n 
1 209 THR n 
1 210 VAL n 
1 211 PHE n 
1 212 ARG n 
1 213 ASN n 
1 214 PRO n 
1 215 VAL n 
1 216 GLN n 
1 217 ILE n 
1 218 SER n 
1 219 GLN n 
1 220 GLU n 
1 221 GLN n 
1 222 LEU n 
1 223 LEU n 
1 224 ALA n 
1 225 LEU n 
1 226 GLU n 
1 227 THR n 
1 228 ALA n 
1 229 LEU n 
1 230 TYR n 
1 231 CYS n 
1 232 THR n 
1 233 HIS n 
1 234 MET n 
1 235 ASP n 
1 236 ASP n 
1 237 PRO n 
1 238 SER n 
1 239 PRO n 
1 240 ARG n 
1 241 GLU n 
1 242 MET n 
1 243 ILE n 
1 244 ASN n 
1 245 ASN n 
1 246 PHE n 
1 247 ARG n 
1 248 GLN n 
1 249 VAL n 
1 250 GLN n 
1 251 LYS n 
1 252 PHE n 
1 253 ASP n 
1 254 GLU n 
1 255 ARG n 
1 256 LEU n 
1 257 VAL n 
1 258 TYR n 
1 259 THR n 
1 260 SER n 
1 261 PHE n 
1 262 SER n 
1 263 GLN n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   263 
_entity_src_gen.gene_src_common_name               Human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 CA12 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     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               'BL21(DE3)' 
_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 
5EF non-polymer         . '3-[(1S)-2,3-dihydro-1H-inden-1-ylamino]-2,5,6-trifluoro-4-[(2-hydroxyethyl)sulfonyl]benzenesulfonamide' 
?                 'C17 H17 F3 N2 O5 S2' 450.452 
ALA 'L-peptide linking' y ALANINE                                                                                                  
?                 'C3 H7 N O2'          89.093  
ARG 'L-peptide linking' y ARGININE                                                                                                 
?                 'C6 H15 N4 O2 1'      175.209 
ASN 'L-peptide linking' y ASPARAGINE                                                                                               
?                 'C4 H8 N2 O3'         132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                                                                                          
?                 'C4 H7 N O4'          133.103 
CYS 'L-peptide linking' y CYSTEINE                                                                                                 
?                 'C3 H7 N O2 S'        121.158 
EDO non-polymer         . 1,2-ETHANEDIOL                                                                                           
'ETHYLENE GLYCOL' 'C2 H6 O2'            62.068  
GLN 'L-peptide linking' y GLUTAMINE                                                                                                
?                 'C5 H10 N2 O3'        146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                                                                          
?                 'C5 H9 N O4'          147.129 
GLY 'peptide linking'   y GLYCINE                                                                                                  
?                 'C2 H5 N O2'          75.067  
HIS 'L-peptide linking' y HISTIDINE                                                                                                
?                 'C6 H10 N3 O2 1'      156.162 
HOH non-polymer         . WATER                                                                                                    
?                 'H2 O'                18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                                                                               
?                 'C6 H13 N O2'         131.173 
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 ?   ?   ?   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 4    ZN  ZN  A . 
F 3 EDO 1   302 1    EDO EDO A . 
G 4 5EF 1   303 4    5EF 5EF A . 
H 2 ZN  1   301 3    ZN  ZN  B . 
I 3 EDO 1   302 2    EDO EDO B . 
J 4 5EF 1   303 3    5EF 5EF B . 
K 2 ZN  1   301 1    ZN  ZN  C . 
L 4 5EF 1   302 1    5EF 5EF C . 
M 2 ZN  1   301 2    ZN  ZN  D . 
N 3 EDO 1   302 3    EDO EDO D . 
O 4 5EF 1   303 2    5EF 5EF D . 
P 5 HOH 1   401 524  HOH HOH A . 
P 5 HOH 2   402 450  HOH HOH A . 
P 5 HOH 3   403 600  HOH HOH A . 
P 5 HOH 4   404 399  HOH HOH A . 
P 5 HOH 5   405 606  HOH HOH A . 
P 5 HOH 6   406 1052 HOH HOH A . 
P 5 HOH 7   407 806  HOH HOH A . 
P 5 HOH 8   408 493  HOH HOH A . 
P 5 HOH 9   409 782  HOH HOH A . 
P 5 HOH 10  410 498  HOH HOH A . 
P 5 HOH 11  411 811  HOH HOH A . 
P 5 HOH 12  412 970  HOH HOH A . 
P 5 HOH 13  413 497  HOH HOH A . 
P 5 HOH 14  414 119  HOH HOH A . 
P 5 HOH 15  415 260  HOH HOH A . 
P 5 HOH 16  416 938  HOH HOH A . 
P 5 HOH 17  417 810  HOH HOH A . 
P 5 HOH 18  418 171  HOH HOH A . 
P 5 HOH 19  419 961  HOH HOH A . 
P 5 HOH 20  420 231  HOH HOH A . 
P 5 HOH 21  421 644  HOH HOH A . 
P 5 HOH 22  422 796  HOH HOH A . 
P 5 HOH 23  423 662  HOH HOH A . 
P 5 HOH 24  424 577  HOH HOH A . 
P 5 HOH 25  425 186  HOH HOH A . 
P 5 HOH 26  426 230  HOH HOH A . 
P 5 HOH 27  427 395  HOH HOH A . 
P 5 HOH 28  428 321  HOH HOH A . 
P 5 HOH 29  429 697  HOH HOH A . 
P 5 HOH 30  430 259  HOH HOH A . 
P 5 HOH 31  431 207  HOH HOH A . 
P 5 HOH 32  432 804  HOH HOH A . 
P 5 HOH 33  433 58   HOH HOH A . 
P 5 HOH 34  434 532  HOH HOH A . 
P 5 HOH 35  435 504  HOH HOH A . 
P 5 HOH 36  436 183  HOH HOH A . 
P 5 HOH 37  437 605  HOH HOH A . 
P 5 HOH 38  438 785  HOH HOH A . 
P 5 HOH 39  439 54   HOH HOH A . 
P 5 HOH 40  440 653  HOH HOH A . 
P 5 HOH 41  441 11   HOH HOH A . 
P 5 HOH 42  442 69   HOH HOH A . 
P 5 HOH 43  443 455  HOH HOH A . 
P 5 HOH 44  444 364  HOH HOH A . 
P 5 HOH 45  445 307  HOH HOH A . 
P 5 HOH 46  446 233  HOH HOH A . 
P 5 HOH 47  447 94   HOH HOH A . 
P 5 HOH 48  448 28   HOH HOH A . 
P 5 HOH 49  449 55   HOH HOH A . 
P 5 HOH 50  450 402  HOH HOH A . 
P 5 HOH 51  451 308  HOH HOH A . 
P 5 HOH 52  452 310  HOH HOH A . 
P 5 HOH 53  453 630  HOH HOH A . 
P 5 HOH 54  454 228  HOH HOH A . 
P 5 HOH 55  455 7    HOH HOH A . 
P 5 HOH 56  456 50   HOH HOH A . 
P 5 HOH 57  457 849  HOH HOH A . 
P 5 HOH 58  458 62   HOH HOH A . 
P 5 HOH 59  459 238  HOH HOH A . 
P 5 HOH 60  460 101  HOH HOH A . 
P 5 HOH 61  461 306  HOH HOH A . 
P 5 HOH 62  462 406  HOH HOH A . 
P 5 HOH 63  463 565  HOH HOH A . 
P 5 HOH 64  464 645  HOH HOH A . 
P 5 HOH 65  465 581  HOH HOH A . 
P 5 HOH 66  466 509  HOH HOH A . 
P 5 HOH 67  467 270  HOH HOH A . 
P 5 HOH 68  468 39   HOH HOH A . 
P 5 HOH 69  469 694  HOH HOH A . 
P 5 HOH 70  470 252  HOH HOH A . 
P 5 HOH 71  471 121  HOH HOH A . 
P 5 HOH 72  472 343  HOH HOH A . 
P 5 HOH 73  473 67   HOH HOH A . 
P 5 HOH 74  474 192  HOH HOH A . 
P 5 HOH 75  475 217  HOH HOH A . 
P 5 HOH 76  476 300  HOH HOH A . 
P 5 HOH 77  477 65   HOH HOH A . 
P 5 HOH 78  478 765  HOH HOH A . 
P 5 HOH 79  479 847  HOH HOH A . 
P 5 HOH 80  480 571  HOH HOH A . 
P 5 HOH 81  481 481  HOH HOH A . 
P 5 HOH 82  482 79   HOH HOH A . 
P 5 HOH 83  483 729  HOH HOH A . 
P 5 HOH 84  484 780  HOH HOH A . 
P 5 HOH 85  485 118  HOH HOH A . 
P 5 HOH 86  486 429  HOH HOH A . 
P 5 HOH 87  487 635  HOH HOH A . 
P 5 HOH 88  488 350  HOH HOH A . 
P 5 HOH 89  489 722  HOH HOH A . 
P 5 HOH 90  490 934  HOH HOH A . 
P 5 HOH 91  491 327  HOH HOH A . 
P 5 HOH 92  492 425  HOH HOH A . 
P 5 HOH 93  493 132  HOH HOH A . 
P 5 HOH 94  494 373  HOH HOH A . 
P 5 HOH 95  495 30   HOH HOH A . 
P 5 HOH 96  496 949  HOH HOH A . 
P 5 HOH 97  497 779  HOH HOH A . 
P 5 HOH 98  498 672  HOH HOH A . 
P 5 HOH 99  499 12   HOH HOH A . 
P 5 HOH 100 500 746  HOH HOH A . 
P 5 HOH 101 501 446  HOH HOH A . 
P 5 HOH 102 502 661  HOH HOH A . 
P 5 HOH 103 503 17   HOH HOH A . 
P 5 HOH 104 504 668  HOH HOH A . 
P 5 HOH 105 505 563  HOH HOH A . 
P 5 HOH 106 506 438  HOH HOH A . 
P 5 HOH 107 507 953  HOH HOH A . 
P 5 HOH 108 508 153  HOH HOH A . 
P 5 HOH 109 509 507  HOH HOH A . 
P 5 HOH 110 510 241  HOH HOH A . 
P 5 HOH 111 511 213  HOH HOH A . 
P 5 HOH 112 512 278  HOH HOH A . 
P 5 HOH 113 513 320  HOH HOH A . 
P 5 HOH 114 514 484  HOH HOH A . 
P 5 HOH 115 515 95   HOH HOH A . 
P 5 HOH 116 516 315  HOH HOH A . 
P 5 HOH 117 517 828  HOH HOH A . 
P 5 HOH 118 518 66   HOH HOH A . 
P 5 HOH 119 519 347  HOH HOH A . 
P 5 HOH 120 520 529  HOH HOH A . 
P 5 HOH 121 521 969  HOH HOH A . 
P 5 HOH 122 522 85   HOH HOH A . 
P 5 HOH 123 523 724  HOH HOH A . 
P 5 HOH 124 524 359  HOH HOH A . 
P 5 HOH 125 525 376  HOH HOH A . 
P 5 HOH 126 526 287  HOH HOH A . 
P 5 HOH 127 527 33   HOH HOH A . 
P 5 HOH 128 528 801  HOH HOH A . 
P 5 HOH 129 529 812  HOH HOH A . 
P 5 HOH 130 530 649  HOH HOH A . 
P 5 HOH 131 531 309  HOH HOH A . 
P 5 HOH 132 532 26   HOH HOH A . 
P 5 HOH 133 533 665  HOH HOH A . 
P 5 HOH 134 534 100  HOH HOH A . 
P 5 HOH 135 535 433  HOH HOH A . 
P 5 HOH 136 536 292  HOH HOH A . 
P 5 HOH 137 537 803  HOH HOH A . 
P 5 HOH 138 538 122  HOH HOH A . 
P 5 HOH 139 539 592  HOH HOH A . 
P 5 HOH 140 540 221  HOH HOH A . 
P 5 HOH 141 541 206  HOH HOH A . 
P 5 HOH 142 542 288  HOH HOH A . 
P 5 HOH 143 543 611  HOH HOH A . 
P 5 HOH 144 544 445  HOH HOH A . 
P 5 HOH 145 545 936  HOH HOH A . 
P 5 HOH 146 546 954  HOH HOH A . 
P 5 HOH 147 547 505  HOH HOH A . 
P 5 HOH 148 548 243  HOH HOH A . 
P 5 HOH 149 549 783  HOH HOH A . 
P 5 HOH 150 550 945  HOH HOH A . 
P 5 HOH 151 551 390  HOH HOH A . 
P 5 HOH 152 552 687  HOH HOH A . 
P 5 HOH 153 553 946  HOH HOH A . 
P 5 HOH 154 554 257  HOH HOH A . 
P 5 HOH 155 555 655  HOH HOH A . 
P 5 HOH 156 556 75   HOH HOH A . 
P 5 HOH 157 557 597  HOH HOH A . 
P 5 HOH 158 558 624  HOH HOH A . 
P 5 HOH 159 559 436  HOH HOH A . 
P 5 HOH 160 560 146  HOH HOH A . 
P 5 HOH 161 561 964  HOH HOH A . 
P 5 HOH 162 562 825  HOH HOH A . 
P 5 HOH 163 563 809  HOH HOH A . 
P 5 HOH 164 564 616  HOH HOH A . 
P 5 HOH 165 565 379  HOH HOH A . 
P 5 HOH 166 566 340  HOH HOH A . 
P 5 HOH 167 567 397  HOH HOH A . 
P 5 HOH 168 568 570  HOH HOH A . 
P 5 HOH 169 569 802  HOH HOH A . 
P 5 HOH 170 570 234  HOH HOH A . 
P 5 HOH 171 571 714  HOH HOH A . 
P 5 HOH 172 572 87   HOH HOH A . 
P 5 HOH 173 573 689  HOH HOH A . 
P 5 HOH 174 574 771  HOH HOH A . 
P 5 HOH 175 575 950  HOH HOH A . 
P 5 HOH 176 576 705  HOH HOH A . 
P 5 HOH 177 577 944  HOH HOH A . 
P 5 HOH 178 578 370  HOH HOH A . 
P 5 HOH 179 579 160  HOH HOH A . 
P 5 HOH 180 580 832  HOH HOH A . 
P 5 HOH 181 581 203  HOH HOH A . 
P 5 HOH 182 582 734  HOH HOH A . 
P 5 HOH 183 583 824  HOH HOH A . 
P 5 HOH 184 584 74   HOH HOH A . 
P 5 HOH 185 585 520  HOH HOH A . 
P 5 HOH 186 586 583  HOH HOH A . 
P 5 HOH 187 587 518  HOH HOH A . 
P 5 HOH 188 588 237  HOH HOH A . 
P 5 HOH 189 589 463  HOH HOH A . 
P 5 HOH 190 590 658  HOH HOH A . 
P 5 HOH 191 591 610  HOH HOH A . 
P 5 HOH 192 592 956  HOH HOH A . 
P 5 HOH 193 593 745  HOH HOH A . 
P 5 HOH 194 594 831  HOH HOH A . 
P 5 HOH 195 595 723  HOH HOH A . 
P 5 HOH 196 596 305  HOH HOH A . 
P 5 HOH 197 597 227  HOH HOH A . 
P 5 HOH 198 598 276  HOH HOH A . 
P 5 HOH 199 599 534  HOH HOH A . 
P 5 HOH 200 600 736  HOH HOH A . 
P 5 HOH 201 601 535  HOH HOH A . 
P 5 HOH 202 602 115  HOH HOH A . 
P 5 HOH 203 603 717  HOH HOH A . 
P 5 HOH 204 604 514  HOH HOH A . 
P 5 HOH 205 605 362  HOH HOH A . 
P 5 HOH 206 606 650  HOH HOH A . 
P 5 HOH 207 607 546  HOH HOH A . 
P 5 HOH 208 608 564  HOH HOH A . 
P 5 HOH 209 609 952  HOH HOH A . 
P 5 HOH 210 610 664  HOH HOH A . 
P 5 HOH 211 611 963  HOH HOH A . 
P 5 HOH 212 612 955  HOH HOH A . 
P 5 HOH 213 613 674  HOH HOH A . 
P 5 HOH 214 614 822  HOH HOH A . 
P 5 HOH 215 615 747  HOH HOH A . 
P 5 HOH 216 616 304  HOH HOH A . 
P 5 HOH 217 617 587  HOH HOH A . 
P 5 HOH 218 618 827  HOH HOH A . 
P 5 HOH 219 619 826  HOH HOH A . 
P 5 HOH 220 620 951  HOH HOH A . 
P 5 HOH 221 621 844  HOH HOH A . 
P 5 HOH 222 622 758  HOH HOH A . 
P 5 HOH 223 623 730  HOH HOH A . 
P 5 HOH 224 624 781  HOH HOH A . 
P 5 HOH 225 625 942  HOH HOH A . 
P 5 HOH 226 626 770  HOH HOH A . 
P 5 HOH 227 627 808  HOH HOH A . 
P 5 HOH 228 628 794  HOH HOH A . 
P 5 HOH 229 629 807  HOH HOH A . 
P 5 HOH 230 630 960  HOH HOH A . 
P 5 HOH 231 631 965  HOH HOH A . 
P 5 HOH 232 632 800  HOH HOH A . 
P 5 HOH 233 633 968  HOH HOH A . 
P 5 HOH 234 634 784  HOH HOH A . 
P 5 HOH 235 635 718  HOH HOH A . 
P 5 HOH 236 636 226  HOH HOH A . 
P 5 HOH 237 637 748  HOH HOH A . 
P 5 HOH 238 638 416  HOH HOH A . 
P 5 HOH 239 639 814  HOH HOH A . 
P 5 HOH 240 640 384  HOH HOH A . 
P 5 HOH 241 641 982  HOH HOH A . 
P 5 HOH 242 642 90   HOH HOH A . 
P 5 HOH 243 643 663  HOH HOH A . 
P 5 HOH 244 644 766  HOH HOH A . 
P 5 HOH 245 645 967  HOH HOH A . 
P 5 HOH 246 646 805  HOH HOH A . 
P 5 HOH 247 647 898  HOH HOH A . 
P 5 HOH 248 648 595  HOH HOH A . 
P 5 HOH 249 649 763  HOH HOH A . 
P 5 HOH 250 650 764  HOH HOH A . 
P 5 HOH 251 651 551  HOH HOH A . 
P 5 HOH 252 652 409  HOH HOH A . 
P 5 HOH 253 653 940  HOH HOH A . 
P 5 HOH 254 654 261  HOH HOH A . 
P 5 HOH 255 655 943  HOH HOH A . 
P 5 HOH 256 656 799  HOH HOH A . 
P 5 HOH 257 657 696  HOH HOH A . 
P 5 HOH 258 658 935  HOH HOH A . 
P 5 HOH 259 659 816  HOH HOH A . 
P 5 HOH 260 660 531  HOH HOH A . 
P 5 HOH 261 661 411  HOH HOH A . 
P 5 HOH 262 662 413  HOH HOH A . 
P 5 HOH 263 663 797  HOH HOH A . 
P 5 HOH 264 664 798  HOH HOH A . 
P 5 HOH 265 665 660  HOH HOH A . 
P 5 HOH 266 666 937  HOH HOH A . 
P 5 HOH 267 667 708  HOH HOH A . 
P 5 HOH 268 668 941  HOH HOH A . 
Q 5 HOH 1   401 861  HOH HOH B . 
Q 5 HOH 2   402 777  HOH HOH B . 
Q 5 HOH 3   403 620  HOH HOH B . 
Q 5 HOH 4   404 676  HOH HOH B . 
Q 5 HOH 5   405 453  HOH HOH B . 
Q 5 HOH 6   406 444  HOH HOH B . 
Q 5 HOH 7   407 63   HOH HOH B . 
Q 5 HOH 8   408 150  HOH HOH B . 
Q 5 HOH 9   409 792  HOH HOH B . 
Q 5 HOH 10  410 31   HOH HOH B . 
Q 5 HOH 11  411 258  HOH HOH B . 
Q 5 HOH 12  412 116  HOH HOH B . 
Q 5 HOH 13  413 51   HOH HOH B . 
Q 5 HOH 14  414 852  HOH HOH B . 
Q 5 HOH 15  415 976  HOH HOH B . 
Q 5 HOH 16  416 70   HOH HOH B . 
Q 5 HOH 17  417 732  HOH HOH B . 
Q 5 HOH 18  418 743  HOH HOH B . 
Q 5 HOH 19  419 251  HOH HOH B . 
Q 5 HOH 20  420 400  HOH HOH B . 
Q 5 HOH 21  421 521  HOH HOH B . 
Q 5 HOH 22  422 979  HOH HOH B . 
Q 5 HOH 23  423 656  HOH HOH B . 
Q 5 HOH 24  424 834  HOH HOH B . 
Q 5 HOH 25  425 477  HOH HOH B . 
Q 5 HOH 26  426 986  HOH HOH B . 
Q 5 HOH 27  427 778  HOH HOH B . 
Q 5 HOH 28  428 200  HOH HOH B . 
Q 5 HOH 29  429 208  HOH HOH B . 
Q 5 HOH 30  430 295  HOH HOH B . 
Q 5 HOH 31  431 64   HOH HOH B . 
Q 5 HOH 32  432 857  HOH HOH B . 
Q 5 HOH 33  433 725  HOH HOH B . 
Q 5 HOH 34  434 205  HOH HOH B . 
Q 5 HOH 35  435 846  HOH HOH B . 
Q 5 HOH 36  436 993  HOH HOH B . 
Q 5 HOH 37  437 870  HOH HOH B . 
Q 5 HOH 38  438 666  HOH HOH B . 
Q 5 HOH 39  439 603  HOH HOH B . 
Q 5 HOH 40  440 867  HOH HOH B . 
Q 5 HOH 41  441 494  HOH HOH B . 
Q 5 HOH 42  442 38   HOH HOH B . 
Q 5 HOH 43  443 353  HOH HOH B . 
Q 5 HOH 44  444 513  HOH HOH B . 
Q 5 HOH 45  445 197  HOH HOH B . 
Q 5 HOH 46  446 584  HOH HOH B . 
Q 5 HOH 47  447 47   HOH HOH B . 
Q 5 HOH 48  448 371  HOH HOH B . 
Q 5 HOH 49  449 749  HOH HOH B . 
Q 5 HOH 50  450 862  HOH HOH B . 
Q 5 HOH 51  451 267  HOH HOH B . 
Q 5 HOH 52  452 573  HOH HOH B . 
Q 5 HOH 53  453 680  HOH HOH B . 
Q 5 HOH 54  454 178  HOH HOH B . 
Q 5 HOH 55  455 223  HOH HOH B . 
Q 5 HOH 56  456 86   HOH HOH B . 
Q 5 HOH 57  457 835  HOH HOH B . 
Q 5 HOH 58  458 871  HOH HOH B . 
Q 5 HOH 59  459 108  HOH HOH B . 
Q 5 HOH 60  460 877  HOH HOH B . 
Q 5 HOH 61  461 737  HOH HOH B . 
Q 5 HOH 62  462 313  HOH HOH B . 
Q 5 HOH 63  463 317  HOH HOH B . 
Q 5 HOH 64  464 282  HOH HOH B . 
Q 5 HOH 65  465 843  HOH HOH B . 
Q 5 HOH 66  466 651  HOH HOH B . 
Q 5 HOH 67  467 978  HOH HOH B . 
Q 5 HOH 68  468 345  HOH HOH B . 
Q 5 HOH 69  469 246  HOH HOH B . 
Q 5 HOH 70  470 819  HOH HOH B . 
Q 5 HOH 71  471 973  HOH HOH B . 
Q 5 HOH 72  472 81   HOH HOH B . 
Q 5 HOH 73  473 848  HOH HOH B . 
Q 5 HOH 74  474 975  HOH HOH B . 
Q 5 HOH 75  475 29   HOH HOH B . 
Q 5 HOH 76  476 652  HOH HOH B . 
Q 5 HOH 77  477 557  HOH HOH B . 
Q 5 HOH 78  478 124  HOH HOH B . 
Q 5 HOH 79  479 607  HOH HOH B . 
Q 5 HOH 80  480 218  HOH HOH B . 
Q 5 HOH 81  481 229  HOH HOH B . 
Q 5 HOH 82  482 225  HOH HOH B . 
Q 5 HOH 83  483 112  HOH HOH B . 
Q 5 HOH 84  484 435  HOH HOH B . 
Q 5 HOH 85  485 341  HOH HOH B . 
Q 5 HOH 86  486 239  HOH HOH B . 
Q 5 HOH 87  487 104  HOH HOH B . 
Q 5 HOH 88  488 245  HOH HOH B . 
Q 5 HOH 89  489 447  HOH HOH B . 
Q 5 HOH 90  490 601  HOH HOH B . 
Q 5 HOH 91  491 84   HOH HOH B . 
Q 5 HOH 92  492 553  HOH HOH B . 
Q 5 HOH 93  493 823  HOH HOH B . 
Q 5 HOH 94  494 437  HOH HOH B . 
Q 5 HOH 95  495 159  HOH HOH B . 
Q 5 HOH 96  496 793  HOH HOH B . 
Q 5 HOH 97  497 136  HOH HOH B . 
Q 5 HOH 98  498 71   HOH HOH B . 
Q 5 HOH 99  499 474  HOH HOH B . 
Q 5 HOH 100 500 328  HOH HOH B . 
Q 5 HOH 101 501 91   HOH HOH B . 
Q 5 HOH 102 502 61   HOH HOH B . 
Q 5 HOH 103 503 224  HOH HOH B . 
Q 5 HOH 104 504 492  HOH HOH B . 
Q 5 HOH 105 505 856  HOH HOH B . 
Q 5 HOH 106 506 872  HOH HOH B . 
Q 5 HOH 107 507 44   HOH HOH B . 
Q 5 HOH 108 508 277  HOH HOH B . 
Q 5 HOH 109 509 710  HOH HOH B . 
Q 5 HOH 110 510 522  HOH HOH B . 
Q 5 HOH 111 511 356  HOH HOH B . 
Q 5 HOH 112 512 501  HOH HOH B . 
Q 5 HOH 113 513 604  HOH HOH B . 
Q 5 HOH 114 514 60   HOH HOH B . 
Q 5 HOH 115 515 667  HOH HOH B . 
Q 5 HOH 116 516 643  HOH HOH B . 
Q 5 HOH 117 517 424  HOH HOH B . 
Q 5 HOH 118 518 145  HOH HOH B . 
Q 5 HOH 119 519 188  HOH HOH B . 
Q 5 HOH 120 520 179  HOH HOH B . 
Q 5 HOH 121 521 14   HOH HOH B . 
Q 5 HOH 122 522 3    HOH HOH B . 
Q 5 HOH 123 523 599  HOH HOH B . 
Q 5 HOH 124 524 972  HOH HOH B . 
Q 5 HOH 125 525 841  HOH HOH B . 
Q 5 HOH 126 526 72   HOH HOH B . 
Q 5 HOH 127 527 980  HOH HOH B . 
Q 5 HOH 128 528 166  HOH HOH B . 
Q 5 HOH 129 529 149  HOH HOH B . 
Q 5 HOH 130 530 36   HOH HOH B . 
Q 5 HOH 131 531 15   HOH HOH B . 
Q 5 HOH 132 532 633  HOH HOH B . 
Q 5 HOH 133 533 284  HOH HOH B . 
Q 5 HOH 134 534 336  HOH HOH B . 
Q 5 HOH 135 535 700  HOH HOH B . 
Q 5 HOH 136 536 499  HOH HOH B . 
Q 5 HOH 137 537 974  HOH HOH B . 
Q 5 HOH 138 538 34   HOH HOH B . 
Q 5 HOH 139 539 460  HOH HOH B . 
Q 5 HOH 140 540 510  HOH HOH B . 
Q 5 HOH 141 541 140  HOH HOH B . 
Q 5 HOH 142 542 189  HOH HOH B . 
Q 5 HOH 143 543 641  HOH HOH B . 
Q 5 HOH 144 544 57   HOH HOH B . 
Q 5 HOH 145 545 382  HOH HOH B . 
Q 5 HOH 146 546 219  HOH HOH B . 
Q 5 HOH 147 547 52   HOH HOH B . 
Q 5 HOH 148 548 109  HOH HOH B . 
Q 5 HOH 149 549 165  HOH HOH B . 
Q 5 HOH 150 550 876  HOH HOH B . 
Q 5 HOH 151 551 275  HOH HOH B . 
Q 5 HOH 152 552 462  HOH HOH B . 
Q 5 HOH 153 553 175  HOH HOH B . 
Q 5 HOH 154 554 552  HOH HOH B . 
Q 5 HOH 155 555 527  HOH HOH B . 
Q 5 HOH 156 556 981  HOH HOH B . 
Q 5 HOH 157 557 247  HOH HOH B . 
Q 5 HOH 158 558 25   HOH HOH B . 
Q 5 HOH 159 559 35   HOH HOH B . 
Q 5 HOH 160 560 851  HOH HOH B . 
Q 5 HOH 161 561 299  HOH HOH B . 
Q 5 HOH 162 562 683  HOH HOH B . 
Q 5 HOH 163 563 619  HOH HOH B . 
Q 5 HOH 164 564 471  HOH HOH B . 
Q 5 HOH 165 565 508  HOH HOH B . 
Q 5 HOH 166 566 20   HOH HOH B . 
Q 5 HOH 167 567 640  HOH HOH B . 
Q 5 HOH 168 568 93   HOH HOH B . 
Q 5 HOH 169 569 211  HOH HOH B . 
Q 5 HOH 170 570 301  HOH HOH B . 
Q 5 HOH 171 571 271  HOH HOH B . 
Q 5 HOH 172 572 111  HOH HOH B . 
Q 5 HOH 173 573 222  HOH HOH B . 
Q 5 HOH 174 574 346  HOH HOH B . 
Q 5 HOH 175 575 318  HOH HOH B . 
Q 5 HOH 176 576 596  HOH HOH B . 
Q 5 HOH 177 577 269  HOH HOH B . 
Q 5 HOH 178 578 464  HOH HOH B . 
Q 5 HOH 179 579 840  HOH HOH B . 
Q 5 HOH 180 580 10   HOH HOH B . 
Q 5 HOH 181 581 612  HOH HOH B . 
Q 5 HOH 182 582 40   HOH HOH B . 
Q 5 HOH 183 583 850  HOH HOH B . 
Q 5 HOH 184 584 818  HOH HOH B . 
Q 5 HOH 185 585 984  HOH HOH B . 
Q 5 HOH 186 586 860  HOH HOH B . 
Q 5 HOH 187 587 172  HOH HOH B . 
Q 5 HOH 188 588 707  HOH HOH B . 
Q 5 HOH 189 589 264  HOH HOH B . 
Q 5 HOH 190 590 817  HOH HOH B . 
Q 5 HOH 191 591 580  HOH HOH B . 
Q 5 HOH 192 592 720  HOH HOH B . 
Q 5 HOH 193 593 815  HOH HOH B . 
Q 5 HOH 194 594 103  HOH HOH B . 
Q 5 HOH 195 595 279  HOH HOH B . 
Q 5 HOH 196 596 191  HOH HOH B . 
Q 5 HOH 197 597 235  HOH HOH B . 
Q 5 HOH 198 598 1051 HOH HOH B . 
Q 5 HOH 199 599 441  HOH HOH B . 
Q 5 HOH 200 600 594  HOH HOH B . 
Q 5 HOH 201 601 263  HOH HOH B . 
Q 5 HOH 202 602 548  HOH HOH B . 
Q 5 HOH 203 603 617  HOH HOH B . 
Q 5 HOH 204 604 190  HOH HOH B . 
Q 5 HOH 205 605 739  HOH HOH B . 
Q 5 HOH 206 606 939  HOH HOH B . 
Q 5 HOH 207 607 536  HOH HOH B . 
Q 5 HOH 208 608 232  HOH HOH B . 
Q 5 HOH 209 609 585  HOH HOH B . 
Q 5 HOH 210 610 985  HOH HOH B . 
Q 5 HOH 211 611 125  HOH HOH B . 
Q 5 HOH 212 612 682  HOH HOH B . 
Q 5 HOH 213 613 833  HOH HOH B . 
Q 5 HOH 214 614 88   HOH HOH B . 
Q 5 HOH 215 615 614  HOH HOH B . 
Q 5 HOH 216 616 615  HOH HOH B . 
Q 5 HOH 217 617 421  HOH HOH B . 
Q 5 HOH 218 618 636  HOH HOH B . 
Q 5 HOH 219 619 711  HOH HOH B . 
Q 5 HOH 220 620 854  HOH HOH B . 
Q 5 HOH 221 621 866  HOH HOH B . 
Q 5 HOH 222 622 991  HOH HOH B . 
Q 5 HOH 223 623 576  HOH HOH B . 
Q 5 HOH 224 624 786  HOH HOH B . 
Q 5 HOH 225 625 836  HOH HOH B . 
Q 5 HOH 226 626 983  HOH HOH B . 
Q 5 HOH 227 627 853  HOH HOH B . 
Q 5 HOH 228 628 873  HOH HOH B . 
Q 5 HOH 229 629 859  HOH HOH B . 
Q 5 HOH 230 630 752  HOH HOH B . 
Q 5 HOH 231 631 329  HOH HOH B . 
Q 5 HOH 232 632 579  HOH HOH B . 
Q 5 HOH 233 633 713  HOH HOH B . 
Q 5 HOH 234 634 839  HOH HOH B . 
Q 5 HOH 235 635 516  HOH HOH B . 
Q 5 HOH 236 636 863  HOH HOH B . 
Q 5 HOH 237 637 837  HOH HOH B . 
Q 5 HOH 238 638 977  HOH HOH B . 
Q 5 HOH 239 639 726  HOH HOH B . 
Q 5 HOH 240 640 1048 HOH HOH B . 
Q 5 HOH 241 641 789  HOH HOH B . 
Q 5 HOH 242 642 788  HOH HOH B . 
Q 5 HOH 243 643 868  HOH HOH B . 
Q 5 HOH 244 644 865  HOH HOH B . 
Q 5 HOH 245 645 550  HOH HOH B . 
Q 5 HOH 246 646 994  HOH HOH B . 
Q 5 HOH 247 647 989  HOH HOH B . 
Q 5 HOH 248 648 285  HOH HOH B . 
Q 5 HOH 249 649 365  HOH HOH B . 
Q 5 HOH 250 650 393  HOH HOH B . 
Q 5 HOH 251 651 869  HOH HOH B . 
Q 5 HOH 252 652 875  HOH HOH B . 
Q 5 HOH 253 653 198  HOH HOH B . 
Q 5 HOH 254 654 821  HOH HOH B . 
Q 5 HOH 255 655 410  HOH HOH B . 
Q 5 HOH 256 656 357  HOH HOH B . 
Q 5 HOH 257 657 858  HOH HOH B . 
Q 5 HOH 258 658 864  HOH HOH B . 
Q 5 HOH 259 659 767  HOH HOH B . 
Q 5 HOH 260 660 1015 HOH HOH B . 
Q 5 HOH 261 661 874  HOH HOH B . 
Q 5 HOH 262 662 338  HOH HOH B . 
Q 5 HOH 263 663 646  HOH HOH B . 
Q 5 HOH 264 664 566  HOH HOH B . 
Q 5 HOH 265 665 756  HOH HOH B . 
Q 5 HOH 266 666 855  HOH HOH B . 
Q 5 HOH 267 667 473  HOH HOH B . 
Q 5 HOH 268 668 757  HOH HOH B . 
Q 5 HOH 269 669 323  HOH HOH B . 
Q 5 HOH 270 670 845  HOH HOH B . 
Q 5 HOH 271 671 298  HOH HOH B . 
Q 5 HOH 272 672 820  HOH HOH B . 
Q 5 HOH 273 673 790  HOH HOH B . 
Q 5 HOH 274 674 971  HOH HOH B . 
Q 5 HOH 275 675 791  HOH HOH B . 
Q 5 HOH 276 676 634  HOH HOH B . 
Q 5 HOH 277 677 992  HOH HOH B . 
Q 5 HOH 278 678 414  HOH HOH B . 
Q 5 HOH 279 679 795  HOH HOH B . 
Q 5 HOH 280 680 787  HOH HOH B . 
Q 5 HOH 281 681 838  HOH HOH B . 
Q 5 HOH 282 682 751  HOH HOH B . 
Q 5 HOH 283 683 690  HOH HOH B . 
Q 5 HOH 284 684 1049 HOH HOH B . 
Q 5 HOH 285 685 418  HOH HOH B . 
Q 5 HOH 286 686 987  HOH HOH B . 
R 5 HOH 1   401 470  HOH HOH C . 
R 5 HOH 2   402 302  HOH HOH C . 
R 5 HOH 3   403 452  HOH HOH C . 
R 5 HOH 4   404 426  HOH HOH C . 
R 5 HOH 5   405 555  HOH HOH C . 
R 5 HOH 6   406 465  HOH HOH C . 
R 5 HOH 7   407 560  HOH HOH C . 
R 5 HOH 8   408 669  HOH HOH C . 
R 5 HOH 9   409 378  HOH HOH C . 
R 5 HOH 10  410 209  HOH HOH C . 
R 5 HOH 11  411 628  HOH HOH C . 
R 5 HOH 12  412 236  HOH HOH C . 
R 5 HOH 13  413 627  HOH HOH C . 
R 5 HOH 14  414 96   HOH HOH C . 
R 5 HOH 15  415 469  HOH HOH C . 
R 5 HOH 16  416 368  HOH HOH C . 
R 5 HOH 17  417 999  HOH HOH C . 
R 5 HOH 18  418 901  HOH HOH C . 
R 5 HOH 19  419 486  HOH HOH C . 
R 5 HOH 20  420 1007 HOH HOH C . 
R 5 HOH 21  421 142  HOH HOH C . 
R 5 HOH 22  422 461  HOH HOH C . 
R 5 HOH 23  423 631  HOH HOH C . 
R 5 HOH 24  424 475  HOH HOH C . 
R 5 HOH 25  425 77   HOH HOH C . 
R 5 HOH 26  426 372  HOH HOH C . 
R 5 HOH 27  427 107  HOH HOH C . 
R 5 HOH 28  428 215  HOH HOH C . 
R 5 HOH 29  429 169  HOH HOH C . 
R 5 HOH 30  430 727  HOH HOH C . 
R 5 HOH 31  431 1023 HOH HOH C . 
R 5 HOH 32  432 110  HOH HOH C . 
R 5 HOH 33  433 358  HOH HOH C . 
R 5 HOH 34  434 593  HOH HOH C . 
R 5 HOH 35  435 348  HOH HOH C . 
R 5 HOH 36  436 363  HOH HOH C . 
R 5 HOH 37  437 626  HOH HOH C . 
R 5 HOH 38  438 128  HOH HOH C . 
R 5 HOH 39  439 775  HOH HOH C . 
R 5 HOH 40  440 184  HOH HOH C . 
R 5 HOH 41  441 385  HOH HOH C . 
R 5 HOH 42  442 1005 HOH HOH C . 
R 5 HOH 43  443 642  HOH HOH C . 
R 5 HOH 44  444 427  HOH HOH C . 
R 5 HOH 45  445 294  HOH HOH C . 
R 5 HOH 46  446 18   HOH HOH C . 
R 5 HOH 47  447 98   HOH HOH C . 
R 5 HOH 48  448 366  HOH HOH C . 
R 5 HOH 49  449 709  HOH HOH C . 
R 5 HOH 50  450 549  HOH HOH C . 
R 5 HOH 51  451 272  HOH HOH C . 
R 5 HOH 52  452 106  HOH HOH C . 
R 5 HOH 53  453 903  HOH HOH C . 
R 5 HOH 54  454 998  HOH HOH C . 
R 5 HOH 55  455 22   HOH HOH C . 
R 5 HOH 56  456 556  HOH HOH C . 
R 5 HOH 57  457 45   HOH HOH C . 
R 5 HOH 58  458 135  HOH HOH C . 
R 5 HOH 59  459 896  HOH HOH C . 
R 5 HOH 60  460 495  HOH HOH C . 
R 5 HOH 61  461 248  HOH HOH C . 
R 5 HOH 62  462 537  HOH HOH C . 
R 5 HOH 63  463 374  HOH HOH C . 
R 5 HOH 64  464 468  HOH HOH C . 
R 5 HOH 65  465 735  HOH HOH C . 
R 5 HOH 66  466 589  HOH HOH C . 
R 5 HOH 67  467 480  HOH HOH C . 
R 5 HOH 68  468 176  HOH HOH C . 
R 5 HOH 69  469 181  HOH HOH C . 
R 5 HOH 70  470 332  HOH HOH C . 
R 5 HOH 71  471 623  HOH HOH C . 
R 5 HOH 72  472 1006 HOH HOH C . 
R 5 HOH 73  473 442  HOH HOH C . 
R 5 HOH 74  474 891  HOH HOH C . 
R 5 HOH 75  475 161  HOH HOH C . 
R 5 HOH 76  476 1    HOH HOH C . 
R 5 HOH 77  477 137  HOH HOH C . 
R 5 HOH 78  478 1009 HOH HOH C . 
R 5 HOH 79  479 525  HOH HOH C . 
R 5 HOH 80  480 894  HOH HOH C . 
R 5 HOH 81  481 830  HOH HOH C . 
R 5 HOH 82  482 500  HOH HOH C . 
R 5 HOH 83  483 544  HOH HOH C . 
R 5 HOH 84  484 126  HOH HOH C . 
R 5 HOH 85  485 380  HOH HOH C . 
R 5 HOH 86  486 16   HOH HOH C . 
R 5 HOH 87  487 995  HOH HOH C . 
R 5 HOH 88  488 622  HOH HOH C . 
R 5 HOH 89  489 701  HOH HOH C . 
R 5 HOH 90  490 541  HOH HOH C . 
R 5 HOH 91  491 918  HOH HOH C . 
R 5 HOH 92  492 545  HOH HOH C . 
R 5 HOH 93  493 42   HOH HOH C . 
R 5 HOH 94  494 432  HOH HOH C . 
R 5 HOH 95  495 578  HOH HOH C . 
R 5 HOH 96  496 392  HOH HOH C . 
R 5 HOH 97  497 542  HOH HOH C . 
R 5 HOH 98  498 1001 HOH HOH C . 
R 5 HOH 99  499 342  HOH HOH C . 
R 5 HOH 100 500 174  HOH HOH C . 
R 5 HOH 101 501 330  HOH HOH C . 
R 5 HOH 102 502 333  HOH HOH C . 
R 5 HOH 103 503 41   HOH HOH C . 
R 5 HOH 104 504 59   HOH HOH C . 
R 5 HOH 105 505 423  HOH HOH C . 
R 5 HOH 106 506 13   HOH HOH C . 
R 5 HOH 107 507 632  HOH HOH C . 
R 5 HOH 108 508 738  HOH HOH C . 
R 5 HOH 109 509 533  HOH HOH C . 
R 5 HOH 110 510 163  HOH HOH C . 
R 5 HOH 111 511 316  HOH HOH C . 
R 5 HOH 112 512 23   HOH HOH C . 
R 5 HOH 113 513 657  HOH HOH C . 
R 5 HOH 114 514 428  HOH HOH C . 
R 5 HOH 115 515 625  HOH HOH C . 
R 5 HOH 116 516 699  HOH HOH C . 
R 5 HOH 117 517 483  HOH HOH C . 
R 5 HOH 118 518 712  HOH HOH C . 
R 5 HOH 119 519 895  HOH HOH C . 
R 5 HOH 120 520 704  HOH HOH C . 
R 5 HOH 121 521 76   HOH HOH C . 
R 5 HOH 122 522 383  HOH HOH C . 
R 5 HOH 123 523 24   HOH HOH C . 
R 5 HOH 124 524 716  HOH HOH C . 
R 5 HOH 125 525 73   HOH HOH C . 
R 5 HOH 126 526 575  HOH HOH C . 
R 5 HOH 127 527 740  HOH HOH C . 
R 5 HOH 128 528 296  HOH HOH C . 
R 5 HOH 129 529 5    HOH HOH C . 
R 5 HOH 130 530 255  HOH HOH C . 
R 5 HOH 131 531 367  HOH HOH C . 
R 5 HOH 132 532 1000 HOH HOH C . 
R 5 HOH 133 533 733  HOH HOH C . 
R 5 HOH 134 534 434  HOH HOH C . 
R 5 HOH 135 535 78   HOH HOH C . 
R 5 HOH 136 536 568  HOH HOH C . 
R 5 HOH 137 537 303  HOH HOH C . 
R 5 HOH 138 538 519  HOH HOH C . 
R 5 HOH 139 539 220  HOH HOH C . 
R 5 HOH 140 540 439  HOH HOH C . 
R 5 HOH 141 541 448  HOH HOH C . 
R 5 HOH 142 542 502  HOH HOH C . 
R 5 HOH 143 543 523  HOH HOH C . 
R 5 HOH 144 544 547  HOH HOH C . 
R 5 HOH 145 545 997  HOH HOH C . 
R 5 HOH 146 546 613  HOH HOH C . 
R 5 HOH 147 547 478  HOH HOH C . 
R 5 HOH 148 548 905  HOH HOH C . 
R 5 HOH 149 549 671  HOH HOH C . 
R 5 HOH 150 550 311  HOH HOH C . 
R 5 HOH 151 551 196  HOH HOH C . 
R 5 HOH 152 552 772  HOH HOH C . 
R 5 HOH 153 553 899  HOH HOH C . 
R 5 HOH 154 554 466  HOH HOH C . 
R 5 HOH 155 555 401  HOH HOH C . 
R 5 HOH 156 556 506  HOH HOH C . 
R 5 HOH 157 557 742  HOH HOH C . 
R 5 HOH 158 558 449  HOH HOH C . 
R 5 HOH 159 559 262  HOH HOH C . 
R 5 HOH 160 560 131  HOH HOH C . 
R 5 HOH 161 561 574  HOH HOH C . 
R 5 HOH 162 562 377  HOH HOH C . 
R 5 HOH 163 563 688  HOH HOH C . 
R 5 HOH 164 564 440  HOH HOH C . 
R 5 HOH 165 565 355  HOH HOH C . 
R 5 HOH 166 566 559  HOH HOH C . 
R 5 HOH 167 567 515  HOH HOH C . 
R 5 HOH 168 568 1044 HOH HOH C . 
R 5 HOH 169 569 489  HOH HOH C . 
R 5 HOH 170 570 773  HOH HOH C . 
R 5 HOH 171 571 214  HOH HOH C . 
R 5 HOH 172 572 673  HOH HOH C . 
R 5 HOH 173 573 890  HOH HOH C . 
R 5 HOH 174 574 679  HOH HOH C . 
R 5 HOH 175 575 1003 HOH HOH C . 
R 5 HOH 176 576 404  HOH HOH C . 
R 5 HOH 177 577 887  HOH HOH C . 
R 5 HOH 178 578 629  HOH HOH C . 
R 5 HOH 179 579 1002 HOH HOH C . 
R 5 HOH 180 580 962  HOH HOH C . 
R 5 HOH 181 581 719  HOH HOH C . 
R 5 HOH 182 582 1010 HOH HOH C . 
R 5 HOH 183 583 776  HOH HOH C . 
R 5 HOH 184 584 268  HOH HOH C . 
R 5 HOH 185 585 813  HOH HOH C . 
R 5 HOH 186 586 755  HOH HOH C . 
R 5 HOH 187 587 702  HOH HOH C . 
R 5 HOH 188 588 695  HOH HOH C . 
R 5 HOH 189 589 885  HOH HOH C . 
R 5 HOH 190 590 759  HOH HOH C . 
R 5 HOH 191 591 1004 HOH HOH C . 
R 5 HOH 192 592 948  HOH HOH C . 
R 5 HOH 193 593 893  HOH HOH C . 
R 5 HOH 194 594 1012 HOH HOH C . 
R 5 HOH 195 595 774  HOH HOH C . 
R 5 HOH 196 596 900  HOH HOH C . 
R 5 HOH 197 597 988  HOH HOH C . 
R 5 HOH 198 598 761  HOH HOH C . 
R 5 HOH 199 599 904  HOH HOH C . 
R 5 HOH 200 600 907  HOH HOH C . 
R 5 HOH 201 601 1045 HOH HOH C . 
R 5 HOH 202 602 199  HOH HOH C . 
R 5 HOH 203 603 897  HOH HOH C . 
R 5 HOH 204 604 947  HOH HOH C . 
R 5 HOH 205 605 638  HOH HOH C . 
R 5 HOH 206 606 925  HOH HOH C . 
R 5 HOH 207 607 906  HOH HOH C . 
R 5 HOH 208 608 892  HOH HOH C . 
R 5 HOH 209 609 996  HOH HOH C . 
R 5 HOH 210 610 1053 HOH HOH C . 
R 5 HOH 211 611 902  HOH HOH C . 
R 5 HOH 212 612 684  HOH HOH C . 
R 5 HOH 213 613 113  HOH HOH C . 
R 5 HOH 214 614 289  HOH HOH C . 
R 5 HOH 215 615 1008 HOH HOH C . 
R 5 HOH 216 616 886  HOH HOH C . 
R 5 HOH 217 617 881  HOH HOH C . 
R 5 HOH 218 618 490  HOH HOH C . 
R 5 HOH 219 619 829  HOH HOH C . 
R 5 HOH 220 620 618  HOH HOH C . 
R 5 HOH 221 621 888  HOH HOH C . 
R 5 HOH 222 622 878  HOH HOH C . 
R 5 HOH 223 623 1011 HOH HOH C . 
S 5 HOH 1   401 164  HOH HOH D . 
S 5 HOH 2   402 929  HOH HOH D . 
S 5 HOH 3   403 459  HOH HOH D . 
S 5 HOH 4   404 457  HOH HOH D . 
S 5 HOH 5   405 129  HOH HOH D . 
S 5 HOH 6   406 1017 HOH HOH D . 
S 5 HOH 7   407 133  HOH HOH D . 
S 5 HOH 8   408 647  HOH HOH D . 
S 5 HOH 9   409 920  HOH HOH D . 
S 5 HOH 10  410 744  HOH HOH D . 
S 5 HOH 11  411 842  HOH HOH D . 
S 5 HOH 12  412 412  HOH HOH D . 
S 5 HOH 13  413 654  HOH HOH D . 
S 5 HOH 14  414 476  HOH HOH D . 
S 5 HOH 15  415 1039 HOH HOH D . 
S 5 HOH 16  416 141  HOH HOH D . 
S 5 HOH 17  417 933  HOH HOH D . 
S 5 HOH 18  418 496  HOH HOH D . 
S 5 HOH 19  419 83   HOH HOH D . 
S 5 HOH 20  420 1025 HOH HOH D . 
S 5 HOH 21  421 588  HOH HOH D . 
S 5 HOH 22  422 273  HOH HOH D . 
S 5 HOH 23  423 921  HOH HOH D . 
S 5 HOH 24  424 187  HOH HOH D . 
S 5 HOH 25  425 194  HOH HOH D . 
S 5 HOH 26  426 398  HOH HOH D . 
S 5 HOH 27  427 930  HOH HOH D . 
S 5 HOH 28  428 511  HOH HOH D . 
S 5 HOH 29  429 1020 HOH HOH D . 
S 5 HOH 30  430 253  HOH HOH D . 
S 5 HOH 31  431 114  HOH HOH D . 
S 5 HOH 32  432 675  HOH HOH D . 
S 5 HOH 33  433 291  HOH HOH D . 
S 5 HOH 34  434 154  HOH HOH D . 
S 5 HOH 35  435 915  HOH HOH D . 
S 5 HOH 36  436 4    HOH HOH D . 
S 5 HOH 37  437 127  HOH HOH D . 
S 5 HOH 38  438 678  HOH HOH D . 
S 5 HOH 39  439 1031 HOH HOH D . 
S 5 HOH 40  440 48   HOH HOH D . 
S 5 HOH 41  441 152  HOH HOH D . 
S 5 HOH 42  442 8    HOH HOH D . 
S 5 HOH 43  443 97   HOH HOH D . 
S 5 HOH 44  444 204  HOH HOH D . 
S 5 HOH 45  445 266  HOH HOH D . 
S 5 HOH 46  446 337  HOH HOH D . 
S 5 HOH 47  447 692  HOH HOH D . 
S 5 HOH 48  448 768  HOH HOH D . 
S 5 HOH 49  449 703  HOH HOH D . 
S 5 HOH 50  450 375  HOH HOH D . 
S 5 HOH 51  451 80   HOH HOH D . 
S 5 HOH 52  452 21   HOH HOH D . 
S 5 HOH 53  453 430  HOH HOH D . 
S 5 HOH 54  454 210  HOH HOH D . 
S 5 HOH 55  455 639  HOH HOH D . 
S 5 HOH 56  456 32   HOH HOH D . 
S 5 HOH 57  457 331  HOH HOH D . 
S 5 HOH 58  458 314  HOH HOH D . 
S 5 HOH 59  459 130  HOH HOH D . 
S 5 HOH 60  460 319  HOH HOH D . 
S 5 HOH 61  461 691  HOH HOH D . 
S 5 HOH 62  462 68   HOH HOH D . 
S 5 HOH 63  463 1034 HOH HOH D . 
S 5 HOH 64  464 360  HOH HOH D . 
S 5 HOH 65  465 120  HOH HOH D . 
S 5 HOH 66  466 677  HOH HOH D . 
S 5 HOH 67  467 19   HOH HOH D . 
S 5 HOH 68  468 922  HOH HOH D . 
S 5 HOH 69  469 82   HOH HOH D . 
S 5 HOH 70  470 37   HOH HOH D . 
S 5 HOH 71  471 177  HOH HOH D . 
S 5 HOH 72  472 562  HOH HOH D . 
S 5 HOH 73  473 443  HOH HOH D . 
S 5 HOH 74  474 389  HOH HOH D . 
S 5 HOH 75  475 297  HOH HOH D . 
S 5 HOH 76  476 454  HOH HOH D . 
S 5 HOH 77  477 185  HOH HOH D . 
S 5 HOH 78  478 334  HOH HOH D . 
S 5 HOH 79  479 530  HOH HOH D . 
S 5 HOH 80  480 49   HOH HOH D . 
S 5 HOH 81  481 9    HOH HOH D . 
S 5 HOH 82  482 381  HOH HOH D . 
S 5 HOH 83  483 46   HOH HOH D . 
S 5 HOH 84  484 156  HOH HOH D . 
S 5 HOH 85  485 659  HOH HOH D . 
S 5 HOH 86  486 162  HOH HOH D . 
S 5 HOH 87  487 526  HOH HOH D . 
S 5 HOH 88  488 670  HOH HOH D . 
S 5 HOH 89  489 27   HOH HOH D . 
S 5 HOH 90  490 485  HOH HOH D . 
S 5 HOH 91  491 591  HOH HOH D . 
S 5 HOH 92  492 608  HOH HOH D . 
S 5 HOH 93  493 598  HOH HOH D . 
S 5 HOH 94  494 1040 HOH HOH D . 
S 5 HOH 95  495 202  HOH HOH D . 
S 5 HOH 96  496 242  HOH HOH D . 
S 5 HOH 97  497 180  HOH HOH D . 
S 5 HOH 98  498 698  HOH HOH D . 
S 5 HOH 99  499 917  HOH HOH D . 
S 5 HOH 100 500 503  HOH HOH D . 
S 5 HOH 101 501 648  HOH HOH D . 
S 5 HOH 102 502 927  HOH HOH D . 
S 5 HOH 103 503 567  HOH HOH D . 
S 5 HOH 104 504 249  HOH HOH D . 
S 5 HOH 105 505 102  HOH HOH D . 
S 5 HOH 106 506 201  HOH HOH D . 
S 5 HOH 107 507 386  HOH HOH D . 
S 5 HOH 108 508 422  HOH HOH D . 
S 5 HOH 109 509 143  HOH HOH D . 
S 5 HOH 110 510 286  HOH HOH D . 
S 5 HOH 111 511 2    HOH HOH D . 
S 5 HOH 112 512 472  HOH HOH D . 
S 5 HOH 113 513 721  HOH HOH D . 
S 5 HOH 114 514 274  HOH HOH D . 
S 5 HOH 115 515 293  HOH HOH D . 
S 5 HOH 116 516 325  HOH HOH D . 
S 5 HOH 117 517 879  HOH HOH D . 
S 5 HOH 118 518 250  HOH HOH D . 
S 5 HOH 119 519 706  HOH HOH D . 
S 5 HOH 120 520 265  HOH HOH D . 
S 5 HOH 121 521 456  HOH HOH D . 
S 5 HOH 122 522 458  HOH HOH D . 
S 5 HOH 123 523 914  HOH HOH D . 
S 5 HOH 124 524 394  HOH HOH D . 
S 5 HOH 125 525 312  HOH HOH D . 
S 5 HOH 126 526 590  HOH HOH D . 
S 5 HOH 127 527 403  HOH HOH D . 
S 5 HOH 128 528 117  HOH HOH D . 
S 5 HOH 129 529 517  HOH HOH D . 
S 5 HOH 130 530 910  HOH HOH D . 
S 5 HOH 131 531 193  HOH HOH D . 
S 5 HOH 132 532 715  HOH HOH D . 
S 5 HOH 133 533 586  HOH HOH D . 
S 5 HOH 134 534 53   HOH HOH D . 
S 5 HOH 135 535 1041 HOH HOH D . 
S 5 HOH 136 536 361  HOH HOH D . 
S 5 HOH 137 537 396  HOH HOH D . 
S 5 HOH 138 538 354  HOH HOH D . 
S 5 HOH 139 539 148  HOH HOH D . 
S 5 HOH 140 540 170  HOH HOH D . 
S 5 HOH 141 541 167  HOH HOH D . 
S 5 HOH 142 542 482  HOH HOH D . 
S 5 HOH 143 543 388  HOH HOH D . 
S 5 HOH 144 544 147  HOH HOH D . 
S 5 HOH 145 545 741  HOH HOH D . 
S 5 HOH 146 546 405  HOH HOH D . 
S 5 HOH 147 547 139  HOH HOH D . 
S 5 HOH 148 548 182  HOH HOH D . 
S 5 HOH 149 549 89   HOH HOH D . 
S 5 HOH 150 550 144  HOH HOH D . 
S 5 HOH 151 551 417  HOH HOH D . 
S 5 HOH 152 552 157  HOH HOH D . 
S 5 HOH 153 553 56   HOH HOH D . 
S 5 HOH 154 554 609  HOH HOH D . 
S 5 HOH 155 555 431  HOH HOH D . 
S 5 HOH 156 556 173  HOH HOH D . 
S 5 HOH 157 557 1026 HOH HOH D . 
S 5 HOH 158 558 572  HOH HOH D . 
S 5 HOH 159 559 1013 HOH HOH D . 
S 5 HOH 160 560 99   HOH HOH D . 
S 5 HOH 161 561 326  HOH HOH D . 
S 5 HOH 162 562 512  HOH HOH D . 
S 5 HOH 163 563 43   HOH HOH D . 
S 5 HOH 164 564 195  HOH HOH D . 
S 5 HOH 165 565 244  HOH HOH D . 
S 5 HOH 166 566 134  HOH HOH D . 
S 5 HOH 167 567 6    HOH HOH D . 
S 5 HOH 168 568 212  HOH HOH D . 
S 5 HOH 169 569 569  HOH HOH D . 
S 5 HOH 170 570 1024 HOH HOH D . 
S 5 HOH 171 571 1021 HOH HOH D . 
S 5 HOH 172 572 123  HOH HOH D . 
S 5 HOH 173 573 467  HOH HOH D . 
S 5 HOH 174 574 1047 HOH HOH D . 
S 5 HOH 175 575 539  HOH HOH D . 
S 5 HOH 176 576 158  HOH HOH D . 
S 5 HOH 177 577 1029 HOH HOH D . 
S 5 HOH 178 578 488  HOH HOH D . 
S 5 HOH 179 579 602  HOH HOH D . 
S 5 HOH 180 580 254  HOH HOH D . 
S 5 HOH 181 581 924  HOH HOH D . 
S 5 HOH 182 582 1016 HOH HOH D . 
S 5 HOH 183 583 487  HOH HOH D . 
S 5 HOH 184 584 151  HOH HOH D . 
S 5 HOH 185 585 322  HOH HOH D . 
S 5 HOH 186 586 290  HOH HOH D . 
S 5 HOH 187 587 155  HOH HOH D . 
S 5 HOH 188 588 1030 HOH HOH D . 
S 5 HOH 189 589 240  HOH HOH D . 
S 5 HOH 190 590 92   HOH HOH D . 
S 5 HOH 191 591 919  HOH HOH D . 
S 5 HOH 192 592 344  HOH HOH D . 
S 5 HOH 193 593 931  HOH HOH D . 
S 5 HOH 194 594 105  HOH HOH D . 
S 5 HOH 195 595 349  HOH HOH D . 
S 5 HOH 196 596 1028 HOH HOH D . 
S 5 HOH 197 597 528  HOH HOH D . 
S 5 HOH 198 598 554  HOH HOH D . 
S 5 HOH 199 599 1014 HOH HOH D . 
S 5 HOH 200 600 387  HOH HOH D . 
S 5 HOH 201 601 256  HOH HOH D . 
S 5 HOH 202 602 369  HOH HOH D . 
S 5 HOH 203 603 558  HOH HOH D . 
S 5 HOH 204 604 281  HOH HOH D . 
S 5 HOH 205 605 451  HOH HOH D . 
S 5 HOH 206 606 911  HOH HOH D . 
S 5 HOH 207 607 889  HOH HOH D . 
S 5 HOH 208 608 932  HOH HOH D . 
S 5 HOH 209 609 543  HOH HOH D . 
S 5 HOH 210 610 1022 HOH HOH D . 
S 5 HOH 211 611 637  HOH HOH D . 
S 5 HOH 212 612 283  HOH HOH D . 
S 5 HOH 213 613 990  HOH HOH D . 
S 5 HOH 214 614 685  HOH HOH D . 
S 5 HOH 215 615 908  HOH HOH D . 
S 5 HOH 216 616 582  HOH HOH D . 
S 5 HOH 217 617 479  HOH HOH D . 
S 5 HOH 218 618 540  HOH HOH D . 
S 5 HOH 219 619 1038 HOH HOH D . 
S 5 HOH 220 620 561  HOH HOH D . 
S 5 HOH 221 621 538  HOH HOH D . 
S 5 HOH 222 622 913  HOH HOH D . 
S 5 HOH 223 623 491  HOH HOH D . 
S 5 HOH 224 624 731  HOH HOH D . 
S 5 HOH 225 625 335  HOH HOH D . 
S 5 HOH 226 626 923  HOH HOH D . 
S 5 HOH 227 627 1042 HOH HOH D . 
S 5 HOH 228 628 728  HOH HOH D . 
S 5 HOH 229 629 681  HOH HOH D . 
S 5 HOH 230 630 351  HOH HOH D . 
S 5 HOH 231 631 1027 HOH HOH D . 
S 5 HOH 232 632 1032 HOH HOH D . 
S 5 HOH 233 633 280  HOH HOH D . 
S 5 HOH 234 634 966  HOH HOH D . 
S 5 HOH 235 635 168  HOH HOH D . 
S 5 HOH 236 636 762  HOH HOH D . 
S 5 HOH 237 637 391  HOH HOH D . 
S 5 HOH 238 638 138  HOH HOH D . 
S 5 HOH 239 639 324  HOH HOH D . 
S 5 HOH 240 640 882  HOH HOH D . 
S 5 HOH 241 641 407  HOH HOH D . 
S 5 HOH 242 642 1035 HOH HOH D . 
S 5 HOH 243 643 754  HOH HOH D . 
S 5 HOH 244 644 753  HOH HOH D . 
S 5 HOH 245 645 415  HOH HOH D . 
S 5 HOH 246 646 339  HOH HOH D . 
S 5 HOH 247 647 916  HOH HOH D . 
S 5 HOH 248 648 760  HOH HOH D . 
S 5 HOH 249 649 686  HOH HOH D . 
S 5 HOH 250 650 1046 HOH HOH D . 
S 5 HOH 251 651 1036 HOH HOH D . 
S 5 HOH 252 652 420  HOH HOH D . 
S 5 HOH 253 653 912  HOH HOH D . 
S 5 HOH 254 654 352  HOH HOH D . 
S 5 HOH 255 655 1037 HOH HOH D . 
S 5 HOH 256 656 883  HOH HOH D . 
S 5 HOH 257 657 621  HOH HOH D . 
S 5 HOH 258 658 926  HOH HOH D . 
S 5 HOH 259 659 1033 HOH HOH D . 
S 5 HOH 260 660 959  HOH HOH D . 
S 5 HOH 261 661 1018 HOH HOH D . 
S 5 HOH 262 662 408  HOH HOH D . 
S 5 HOH 263 663 693  HOH HOH D . 
S 5 HOH 264 664 216  HOH HOH D . 
S 5 HOH 265 665 1043 HOH HOH D . 
S 5 HOH 266 666 884  HOH HOH D . 
S 5 HOH 267 667 1050 HOH HOH D . 
S 5 HOH 268 668 750  HOH HOH D . 
S 5 HOH 269 669 1019 HOH HOH D . 
S 5 HOH 270 670 880  HOH HOH D . 
S 5 HOH 271 671 909  HOH HOH D . 
S 5 HOH 272 672 419  HOH HOH D . 
S 5 HOH 273 673 957  HOH HOH D . 
S 5 HOH 274 674 958  HOH HOH D . 
S 5 HOH 275 675 769  HOH HOH D . 
S 5 HOH 276 676 928  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      ? ? ? 5.6.0117 1 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? SCALA       ? ? ? 3.3.20   2 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? 3.20     3 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? XDS         ? ? ? .        4 
? phasing           ? ? ? ? ? ? ? ? ? ? ? MOLREP      ? ? ? .        5 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   108.950 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     5LLO 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     77.291 
_cell.length_a_esd                 ? 
_cell.length_b                     74.111 
_cell.length_b_esd                 ? 
_cell.length_c                     91.585 
_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                         5LLO 
_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                   5LLO 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                      ? 
_exptl_crystal.density_diffrn              ? 
_exptl_crystal.density_Matthews            2.07 
_exptl_crystal.density_method              ? 
_exptl_crystal.density_percent_sol         40.1 
_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              7.0 
_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), 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_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M-F' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2012-11-30 
# 
_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   0.826606 
_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 P13 (MX1)' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.826606 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   'P13 (MX1)' 
_diffrn_source.pdbx_synchrotron_site       'PETRA III, EMBL c/o DESY' 
# 
_reflns.B_iso_Wilson_estimate            18.458 
_reflns.entry_id                         5LLO 
_reflns.data_reduction_details           ? 
_reflns.data_reduction_method            ? 
_reflns.d_resolution_high                1.600 
_reflns.d_resolution_low                 86.619 
_reflns.details                          ? 
_reflns.limit_h_max                      ? 
_reflns.limit_h_min                      ? 
_reflns.limit_k_max                      ? 
_reflns.limit_k_min                      ? 
_reflns.limit_l_max                      ? 
_reflns.limit_l_min                      ? 
_reflns.number_all                       ? 
_reflns.number_obs                       127546 
_reflns.observed_criterion               ? 
_reflns.observed_criterion_F_max         ? 
_reflns.observed_criterion_F_min         ? 
_reflns.observed_criterion_I_max         ? 
_reflns.observed_criterion_I_min         ? 
_reflns.observed_criterion_sigma_F       ? 
_reflns.observed_criterion_sigma_I       ? 
_reflns.percent_possible_obs             99.000 
_reflns.R_free_details                   ? 
_reflns.Rmerge_F_all                     ? 
_reflns.Rmerge_F_obs                     ? 
_reflns.Friedel_coverage                 ? 
_reflns.number_gt                        ? 
_reflns.threshold_expression             ? 
_reflns.pdbx_redundancy                  6.800 
_reflns.pdbx_Rmerge_I_obs                ? 
_reflns.pdbx_Rmerge_I_all                ? 
_reflns.pdbx_Rsym_value                  0.049 
_reflns.pdbx_netI_over_av_sigmaI         10.143 
_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                  ? 
_reflns.pdbx_Rpim_I_all                  ? 
_reflns.pdbx_d_opt                       ? 
_reflns.pdbx_number_measured_all         ? 
_reflns.pdbx_diffrn_id                   1 
_reflns.pdbx_ordinal                     1 
_reflns.pdbx_CC_half                     ? 
_reflns.pdbx_R_split                     ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_measured_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.number_unique_obs 
_reflns_shell.percent_possible_all 
_reflns_shell.percent_possible_obs 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_gt 
_reflns_shell.meanI_over_uI_all 
_reflns_shell.meanI_over_uI_gt 
_reflns_shell.number_measured_gt 
_reflns_shell.number_unique_gt 
_reflns_shell.percent_possible_gt 
_reflns_shell.Rmerge_F_gt 
_reflns_shell.Rmerge_I_gt 
_reflns_shell.pdbx_redundancy 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_netI_over_sigmaI_all 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_rejects 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_R_split 
1.600 1.690  ? 2.100  ? ? ? ? ? 99.100 ? ? ? ? 0.370 ? ? ? ? ? ? ? ? 6.900 ? ? ? ? ? ? ? 1  1 ? ? 
1.690 1.790  ? 3.000  ? ? ? ? ? 99.100 ? ? ? ? 0.251 ? ? ? ? ? ? ? ? 6.900 ? ? ? ? ? ? ? 2  1 ? ? 
1.790 1.910  ? 4.500  ? ? ? ? ? 98.900 ? ? ? ? 0.165 ? ? ? ? ? ? ? ? 6.600 ? ? ? ? ? ? ? 3  1 ? ? 
1.910 2.070  ? 7.100  ? ? ? ? ? 98.700 ? ? ? ? 0.104 ? ? ? ? ? ? ? ? 6.800 ? ? ? ? ? ? ? 4  1 ? ? 
2.070 2.260  ? 9.700  ? ? ? ? ? 99.100 ? ? ? ? 0.074 ? ? ? ? ? ? ? ? 7.000 ? ? ? ? ? ? ? 5  1 ? ? 
2.260 2.530  ? 12.300 ? ? ? ? ? 98.900 ? ? ? ? 0.057 ? ? ? ? ? ? ? ? 6.600 ? ? ? ? ? ? ? 6  1 ? ? 
2.530 2.920  ? 15.900 ? ? ? ? ? 99.500 ? ? ? ? 0.042 ? ? ? ? ? ? ? ? 7.200 ? ? ? ? ? ? ? 7  1 ? ? 
2.920 3.580  ? 18.400 ? ? ? ? ? 98.800 ? ? ? ? 0.033 ? ? ? ? ? ? ? ? 6.800 ? ? ? ? ? ? ? 8  1 ? ? 
3.580 5.060  ? 22.300 ? ? ? ? ? 99.100 ? ? ? ? 0.024 ? ? ? ? ? ? ? ? 6.900 ? ? ? ? ? ? ? 9  1 ? ? 
5.060 86.619 ? 13.000 ? ? ? ? ? 99.100 ? ? ? ? 0.026 ? ? ? ? ? ? ? ? 6.600 ? ? ? ? ? ? ? 10 1 ? ? 
# 
_refine.aniso_B[1][1]                            -0.1800 
_refine.aniso_B[1][2]                            0.0000 
_refine.aniso_B[1][3]                            0.4200 
_refine.aniso_B[2][2]                            0.5600 
_refine.aniso_B[2][3]                            0.0000 
_refine.aniso_B[3][3]                            -0.1100 
_refine.B_iso_max                                72.640 
_refine.B_iso_mean                               19.3130 
_refine.B_iso_min                                6.320 
_refine.correlation_coeff_Fo_to_Fc               0.9630 
_refine.correlation_coeff_Fo_to_Fc_free          0.9500 
_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                                 5LLO 
_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                            1.6000 
_refine.ls_d_res_low                             73.1000 
_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                     114891 
_refine.ls_number_reflns_R_free                  12532 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.8400 
_refine.ls_percent_reflns_R_free                 9.8000 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1893 
_refine.ls_R_factor_R_free                       0.2253 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1853 
_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                       0.1100 
_refine.pdbx_overall_ESU_R_Free                  0.1090 
_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             0.1105 
_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.cycle_id                         final 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.d_res_high                       1.6000 
_refine_hist.d_res_low                        73.1000 
_refine_hist.pdbx_number_atoms_ligand         132 
_refine_hist.number_atoms_solvent             1053 
_refine_hist.number_atoms_total               9566 
_refine_hist.pdbx_number_residues_total       1043 
_refine_hist.pdbx_B_iso_mean_ligand           23.52 
_refine_hist.pdbx_B_iso_mean_solvent          27.60 
_refine_hist.pdbx_number_atoms_protein        8381 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
# 
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' ? 0.022  0.020  8978  ? r_bond_refined_d       ? ? 
'X-RAY DIFFRACTION' ? 2.146  1.958  12275 ? r_angle_refined_deg    ? ? 
'X-RAY DIFFRACTION' ? 7.003  5.000  1085  ? r_dihedral_angle_1_deg ? ? 
'X-RAY DIFFRACTION' ? 37.353 24.610 449   ? r_dihedral_angle_2_deg ? ? 
'X-RAY DIFFRACTION' ? 14.291 15.000 1403  ? r_dihedral_angle_3_deg ? ? 
'X-RAY DIFFRACTION' ? 19.390 15.000 35    ? r_dihedral_angle_4_deg ? ? 
'X-RAY DIFFRACTION' ? 0.168  0.200  1276  ? r_chiral_restr         ? ? 
'X-RAY DIFFRACTION' ? 0.014  0.021  7103  ? r_gen_planes_refined   ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.6000 
_refine_ls_shell.d_res_low                        1.6420 
_refine_ls_shell.number_reflns_all                9433 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             927 
_refine_ls_shell.number_reflns_R_work             8506 
_refine_ls_shell.percent_reflns_obs               99.0300 
_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                  0.3440 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.2830 
_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                     5LLO 
_struct.title                        
;Crystal structure of human carbonic anhydrase isozyme XII with 3-[(1S)-2,3-Dihydro-1H-inden-1-ylamino]-2,5,6-trifluoro-4-[(2-hy-droxyethyl)sulfonyl]benzenesulfonamide
;
_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        5LLO 
_struct_keywords.text            
'drug design, carbonic anhydrase, benzenesulfonamide, metal-binding, lyase-lyase inhibitor comple, 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 4 ? 
H N N 2 ? 
I N N 3 ? 
J N N 4 ? 
K N N 2 ? 
L N N 4 ? 
M N N 2 ? 
N N N 3 ? 
O N N 4 ? 
P N N 5 ? 
Q N N 5 ? 
R N N 5 ? 
S N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    CAH12_HUMAN 
_struct_ref.pdbx_db_accession          O43570 
_struct_ref.pdbx_db_isoform            O43570-2 
_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 5LLO A 2 ? 263 ? O43570 30 ? 291 ? 2 263 
2 1 5LLO B 2 ? 263 ? O43570 30 ? 291 ? 2 263 
3 1 5LLO C 2 ? 263 ? O43570 30 ? 291 ? 2 263 
4 1 5LLO 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 5LLO MET A 1 ? UNP O43570 ? ? 'initiating methionine' 1 1 
2 5LLO MET B 1 ? UNP O43570 ? ? 'initiating methionine' 1 2 
3 5LLO MET C 1 ? UNP O43570 ? ? 'initiating methionine' 1 3 
4 5LLO 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,P,Q 
2 1 C,D,K,L,M,N,O,R,S   
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 GLY A 11  ? ASN A 13  ? GLY A 11  ASN A 13  5 ? 3  
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 SER B 14  ? LYS B 18  ? SER B 14  LYS B 18  5 ? 5  
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 ? ALA B 228 ? SER B 218 ALA B 228 1 ? 11 
HELX_P HELX_P18 AB9 GLY C 11  ? TRP C 15  ? GLY C 11  TRP C 15  5 ? 5  
HELX_P HELX_P19 AC1 TYR C 19  ? GLY C 24  ? TYR C 19  GLY C 24  5 ? 6  
HELX_P HELX_P20 AC2 HIS C 33  ? ASP C 35  ? HIS C 33  ASP C 35  5 ? 3  
HELX_P HELX_P21 AC3 ASP C 128 ? SER C 133 ? ASP C 128 SER C 133 1 ? 6  
HELX_P HELX_P22 AC4 ASN C 152 ? SER C 160 ? ASN C 152 SER C 160 1 ? 9  
HELX_P HELX_P23 AC5 HIS C 161 ? LYS C 166 ? HIS C 161 LYS C 166 5 ? 6  
HELX_P HELX_P24 AC6 ASN C 178 ? LEU C 183 ? ASN C 178 LEU C 183 5 ? 6  
HELX_P HELX_P25 AC7 SER C 218 ? LEU C 229 ? SER C 218 LEU C 229 1 ? 12 
HELX_P HELX_P26 AC8 GLY D 11  ? LYS D 18  ? GLY D 11  LYS D 18  5 ? 8  
HELX_P HELX_P27 AC9 TYR D 19  ? GLY D 24  ? TYR D 19  GLY D 24  5 ? 6  
HELX_P HELX_P28 AD1 HIS D 33  ? ASP D 35  ? HIS D 33  ASP D 35  5 ? 3  
HELX_P HELX_P29 AD2 ASP D 128 ? ASN D 134 ? ASP D 128 ASN D 134 1 ? 7  
HELX_P HELX_P30 AD3 TYR D 155 ? SER D 160 ? TYR D 155 SER D 160 1 ? 6  
HELX_P HELX_P31 AD4 HIS D 161 ? LYS D 166 ? HIS D 161 LYS D 166 5 ? 6  
HELX_P HELX_P32 AD5 ASN D 178 ? LEU D 183 ? ASN D 178 LEU D 183 5 ? 6  
HELX_P HELX_P33 AD6 GLN D 219 ? LEU D 229 ? GLN D 219 LEU D 229 1 ? 11 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1  disulf ? ? A CYS 22  SG  ? ? ? 1_555 A CYS 202 SG ? ? A CYS 22  A CYS 202 1_555 ? ? ? ? ? ? ? 2.036 ? ? 
disulf2  disulf ? ? B CYS 22  SG  ? ? ? 1_555 B CYS 202 SG ? ? B CYS 22  B CYS 202 1_555 ? ? ? ? ? ? ? 2.010 ? ? 
disulf3  disulf ? ? C CYS 22  SG  ? ? ? 1_555 C CYS 202 SG ? ? C CYS 22  C CYS 202 1_555 ? ? ? ? ? ? ? 2.004 ? ? 
disulf4  disulf ? ? D CYS 22  SG  ? ? ? 1_555 D CYS 202 SG ? ? D CYS 22  D CYS 202 1_555 ? ? ? ? ? ? ? 2.022 ? ? 
metalc1  metalc ? ? A HIS 91  NE2 ? ? ? 1_555 E ZN  .   ZN ? ? A HIS 91  A ZN  301 1_555 ? ? ? ? ? ? ? 2.079 ? ? 
metalc2  metalc ? ? A HIS 93  NE2 ? ? ? 1_555 E ZN  .   ZN ? ? A HIS 93  A ZN  301 1_555 ? ? ? ? ? ? ? 2.072 ? ? 
metalc3  metalc ? ? A HIS 117 ND1 ? ? ? 1_555 E ZN  .   ZN ? ? A HIS 117 A ZN  301 1_555 ? ? ? ? ? ? ? 1.986 ? ? 
metalc4  metalc ? ? E ZN  .   ZN  ? ? ? 1_555 G 5EF .   N4 ? ? A ZN  301 A 5EF 303 1_555 ? ? ? ? ? ? ? 2.006 ? ? 
metalc5  metalc ? ? B HIS 91  NE2 ? ? ? 1_555 H ZN  .   ZN ? ? B HIS 91  B ZN  301 1_555 ? ? ? ? ? ? ? 2.084 ? ? 
metalc6  metalc ? ? B HIS 93  NE2 ? ? ? 1_555 H ZN  .   ZN ? ? B HIS 93  B ZN  301 1_555 ? ? ? ? ? ? ? 2.043 ? ? 
metalc7  metalc ? ? B HIS 117 ND1 ? ? ? 1_555 H ZN  .   ZN ? ? B HIS 117 B ZN  301 1_555 ? ? ? ? ? ? ? 2.063 ? ? 
metalc8  metalc ? ? H ZN  .   ZN  ? ? ? 1_555 J 5EF .   N4 ? ? B ZN  301 B 5EF 303 1_555 ? ? ? ? ? ? ? 1.822 ? ? 
metalc9  metalc ? ? C HIS 91  NE2 ? ? ? 1_555 K ZN  .   ZN ? ? C HIS 91  C ZN  301 1_555 ? ? ? ? ? ? ? 2.103 ? ? 
metalc10 metalc ? ? C HIS 93  NE2 ? ? ? 1_555 K ZN  .   ZN ? ? C HIS 93  C ZN  301 1_555 ? ? ? ? ? ? ? 2.028 ? ? 
metalc11 metalc ? ? C HIS 117 ND1 ? ? ? 1_555 K ZN  .   ZN ? ? C HIS 117 C ZN  301 1_555 ? ? ? ? ? ? ? 1.981 ? ? 
metalc12 metalc ? ? K ZN  .   ZN  ? ? ? 1_555 L 5EF .   N4 ? ? C ZN  301 C 5EF 302 1_555 ? ? ? ? ? ? ? 1.884 ? ? 
metalc13 metalc ? ? D HIS 91  NE2 ? ? ? 1_555 M ZN  .   ZN ? ? D HIS 91  D ZN  301 1_555 ? ? ? ? ? ? ? 2.056 ? ? 
metalc14 metalc ? ? D HIS 93  NE2 ? ? ? 1_555 M ZN  .   ZN ? ? D HIS 93  D ZN  301 1_555 ? ? ? ? ? ? ? 2.022 ? ? 
metalc15 metalc ? ? D HIS 117 ND1 ? ? ? 1_555 M ZN  .   ZN ? ? D HIS 117 D ZN  301 1_555 ? ? ? ? ? ? ? 2.048 ? ? 
metalc16 metalc ? ? M ZN  .   ZN  ? ? ? 1_555 O 5EF .   N4 ? ? D ZN  301 D 5EF 303 1_555 ? ? ? ? ? ? ? 1.990 ? ? 
# 
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_555 105.7 ? 
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_555 108.9 ? 
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 99.7  ? 
4  NE2 ? A HIS 91  ? A HIS 91  ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 N4  ? G 5EF .   ? A 5EF 303 ? 1_555 118.9 ? 
5  NE2 ? A HIS 93  ? A HIS 93  ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 N4  ? G 5EF .   ? A 5EF 303 ? 1_555 113.3 ? 
6  ND1 ? A HIS 117 ? A HIS 117 ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 N4  ? G 5EF .   ? A 5EF 303 ? 1_555 108.6 ? 
7  NE2 ? B HIS 91  ? B HIS 91  ? 1_555 ZN ? H ZN . ? B ZN 301 ? 1_555 NE2 ? B HIS 93  ? B HIS 93  ? 1_555 107.2 ? 
8  NE2 ? B HIS 91  ? B HIS 91  ? 1_555 ZN ? H ZN . ? B ZN 301 ? 1_555 ND1 ? B HIS 117 ? B HIS 117 ? 1_555 112.8 ? 
9  NE2 ? B HIS 93  ? B HIS 93  ? 1_555 ZN ? H ZN . ? B ZN 301 ? 1_555 ND1 ? B HIS 117 ? B HIS 117 ? 1_555 100.0 ? 
10 NE2 ? B HIS 91  ? B HIS 91  ? 1_555 ZN ? H ZN . ? B ZN 301 ? 1_555 N4  ? J 5EF .   ? B 5EF 303 ? 1_555 114.9 ? 
11 NE2 ? B HIS 93  ? B HIS 93  ? 1_555 ZN ? H ZN . ? B ZN 301 ? 1_555 N4  ? J 5EF .   ? B 5EF 303 ? 1_555 113.7 ? 
12 ND1 ? B HIS 117 ? B HIS 117 ? 1_555 ZN ? H ZN . ? B ZN 301 ? 1_555 N4  ? J 5EF .   ? B 5EF 303 ? 1_555 107.2 ? 
13 NE2 ? C HIS 91  ? C HIS 91  ? 1_555 ZN ? K ZN . ? C ZN 301 ? 1_555 NE2 ? C HIS 93  ? C HIS 93  ? 1_555 104.3 ? 
14 NE2 ? C HIS 91  ? C HIS 91  ? 1_555 ZN ? K ZN . ? C ZN 301 ? 1_555 ND1 ? C HIS 117 ? C HIS 117 ? 1_555 111.6 ? 
15 NE2 ? C HIS 93  ? C HIS 93  ? 1_555 ZN ? K ZN . ? C ZN 301 ? 1_555 ND1 ? C HIS 117 ? C HIS 117 ? 1_555 98.7  ? 
16 NE2 ? C HIS 91  ? C HIS 91  ? 1_555 ZN ? K ZN . ? C ZN 301 ? 1_555 N4  ? L 5EF .   ? C 5EF 302 ? 1_555 116.0 ? 
17 NE2 ? C HIS 93  ? C HIS 93  ? 1_555 ZN ? K ZN . ? C ZN 301 ? 1_555 N4  ? L 5EF .   ? C 5EF 302 ? 1_555 116.7 ? 
18 ND1 ? C HIS 117 ? C HIS 117 ? 1_555 ZN ? K ZN . ? C ZN 301 ? 1_555 N4  ? L 5EF .   ? C 5EF 302 ? 1_555 108.2 ? 
19 NE2 ? D HIS 91  ? D HIS 91  ? 1_555 ZN ? M ZN . ? D ZN 301 ? 1_555 NE2 ? D HIS 93  ? D HIS 93  ? 1_555 102.8 ? 
20 NE2 ? D HIS 91  ? D HIS 91  ? 1_555 ZN ? M ZN . ? D ZN 301 ? 1_555 ND1 ? D HIS 117 ? D HIS 117 ? 1_555 109.7 ? 
21 NE2 ? D HIS 93  ? D HIS 93  ? 1_555 ZN ? M ZN . ? D ZN 301 ? 1_555 ND1 ? D HIS 117 ? D HIS 117 ? 1_555 97.7  ? 
22 NE2 ? D HIS 91  ? D HIS 91  ? 1_555 ZN ? M ZN . ? D ZN 301 ? 1_555 N4  ? O 5EF .   ? D 5EF 303 ? 1_555 120.8 ? 
23 NE2 ? D HIS 93  ? D HIS 93  ? 1_555 ZN ? M ZN . ? D ZN 301 ? 1_555 N4  ? O 5EF .   ? D 5EF 303 ? 1_555 117.0 ? 
24 ND1 ? D HIS 117 ? D HIS 117 ? 1_555 ZN ? M ZN . ? D ZN 301 ? 1_555 N4  ? O 5EF .   ? D 5EF 303 ? 1_555 106.4 ? 
# 
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 1.31  
2 PRO 200 A . ? PRO 200 A PRO 201 A ? PRO 201 A 1 10.46 
3 SER 28  B . ? SER 28  B PRO 29  B ? PRO 29  B 1 1.78  
4 PRO 200 B . ? PRO 200 B PRO 201 B ? PRO 201 B 1 9.52  
5 SER 28  C . ? SER 28  C PRO 29  C ? PRO 29  C 1 1.13  
6 PRO 200 C . ? PRO 200 C PRO 201 C ? PRO 201 C 1 9.89  
7 SER 28  D . ? SER 28  D PRO 29  D ? PRO 29  D 1 1.74  
8 PRO 200 D . ? PRO 200 D PRO 201 D ? PRO 201 D 1 2.40  
# 
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 ? GLY D 149 ? LEU D 139 GLY D 149 
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 ? GLY D 149 ? LEU D 139 GLY D 149 
AB3 6  VAL D 215 ? SER D 218 ? VAL D 215 SER D 218 
# 
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 VAL A 144 ? O VAL A 144 N LEU A 116 ? N LEU A 116 
AA2 6 7  O HIS A 117 ? O HIS A 117 N HIS A 91  ? N HIS A 91  
AA2 7 8  O LEU A 90  ? O LEU A 90  N LEU A 70  ? N LEU A 70  
AA2 8 9  O ASN A 71  ? O ASN A 71  N LEU A 60  ? N LEU A 60  
AA2 9 10 N LEU A 61  ? N LEU A 61  O ALA A 172 ? O ALA A 172 
AA3 1 2  N GLN A 49  ? N GLN A 49  O HIS A 77  ? O HIS A 77  
AA3 2 3  N ILE A 78  ? N ILE A 78  O TYR A 85  ? O TYR A 85  
AA3 3 4  N HIS A 91  ? N HIS A 91  O HIS A 117 ? O HIS A 117 
AA3 4 5  N LEU A 116 ? N LEU A 116 O VAL A 144 ? O VAL A 144 
AA3 5 6  N GLU A 147 ? N GLU A 147 O VAL A 215 ? O VAL A 215 
AA4 1 2  N LEU B 32  ? N LEU B 32  O THR B 106 ? O THR B 106 
AA5 1 2  N GLN B 38  ? N GLN B 38  O VAL B 257 ? O VAL B 257 
AA5 2 3  O TYR B 258 ? O TYR B 258 N ARG B 192 ? N ARG B 192 
AA5 3 4  N TYR B 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 VAL B 144 ? O VAL B 144 N LEU B 116 ? N LEU B 116 
AA5 6 7  O HIS B 117 ? O HIS B 117 N HIS B 91  ? N HIS B 91  
AA5 7 8  O LEU B 90  ? O LEU B 90  N LEU B 70  ? N LEU B 70  
AA5 8 9  O ASN B 71  ? O ASN B 71  N LEU B 60  ? N LEU B 60  
AA5 9 10 N LEU B 61  ? N LEU B 61  O ALA B 172 ? O ALA B 172 
AA6 1 2  N GLN B 49  ? N GLN B 49  O HIS B 77  ? O HIS B 77  
AA6 2 3  N ILE B 78  ? N ILE B 78  O TYR B 85  ? O TYR B 85  
AA6 3 4  N HIS B 91  ? N HIS B 91  O HIS B 117 ? O HIS B 117 
AA6 4 5  N LEU B 116 ? N LEU B 116 O VAL B 144 ? O VAL B 144 
AA6 5 6  N GLU B 147 ? N GLU B 147 O VAL B 215 ? O VAL B 215 
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 ILE C 146 ? O ILE C 146 N ALA C 114 ? N ALA C 114 
AA8 6 7  O TYR C 121 ? O TYR C 121 N SER C 86  ? N SER C 86  
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 SER C 86  ? N SER C 86  O TYR C 121 ? O TYR C 121 
AA9 4 5  N ALA C 114 ? N ALA C 114 O ILE C 146 ? O ILE C 146 
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 TYR D 191 ? N TYR D 191 O VAL D 210 ? O VAL D 210 
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 HIS D 117 ? O HIS D 117 N HIS D 91  ? N HIS D 91  
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 HIS D 91  ? N HIS D 91  O HIS D 117 ? O HIS D 117 
AB3 4 5  N ALA D 114 ? N ALA D 114 O ILE D 146 ? O ILE D 146 
AB3 5 6  N GLY D 149 ? N GLY D 149 O ILE D 217 ? O ILE D 217 
# 
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 ? 3  'binding site for residue EDO A 302' 
AC3 Software A 5EF 303 ? 14 'binding site for residue 5EF A 303' 
AC4 Software B ZN  301 ? 4  'binding site for residue ZN B 301'  
AC5 Software B EDO 302 ? 6  'binding site for residue EDO B 302' 
AC6 Software B 5EF 303 ? 14 'binding site for residue 5EF B 303' 
AC7 Software C ZN  301 ? 4  'binding site for residue ZN C 301'  
AC8 Software C 5EF 302 ? 16 'binding site for residue 5EF C 302' 
AC9 Software D ZN  301 ? 4  'binding site for residue ZN D 301'  
AD1 Software D EDO 302 ? 6  'binding site for residue EDO D 302' 
AD2 Software D 5EF 303 ? 13 'binding site for residue 5EF 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  5EF G .   ? 5EF A 303 . ? 1_555 ? 
5  AC2 3  ASP A 156 ? ASP A 156 . ? 1_555 ? 
6  AC2 3  SER A 160 ? SER A 160 . ? 1_555 ? 
7  AC2 3  HOH P .   ? HOH A 462 . ? 1_555 ? 
8  AC3 14 ASN A 64  ? ASN A 64  . ? 1_555 ? 
9  AC3 14 SER A 67  ? SER A 67  . ? 1_555 ? 
10 AC3 14 HIS A 91  ? HIS A 91  . ? 1_555 ? 
11 AC3 14 HIS A 93  ? HIS A 93  . ? 1_555 ? 
12 AC3 14 GLU A 104 ? GLU A 104 . ? 1_555 ? 
13 AC3 14 HIS A 117 ? HIS A 117 . ? 1_555 ? 
14 AC3 14 VAL A 119 ? VAL A 119 . ? 1_555 ? 
15 AC3 14 SER A 130 ? SER A 130 . ? 1_555 ? 
16 AC3 14 LEU A 197 ? LEU A 197 . ? 1_555 ? 
17 AC3 14 THR A 198 ? THR A 198 . ? 1_555 ? 
18 AC3 14 THR A 199 ? THR A 199 . ? 1_555 ? 
19 AC3 14 PRO A 200 ? PRO A 200 . ? 1_555 ? 
20 AC3 14 ZN  E .   ? ZN  A 301 . ? 1_555 ? 
21 AC3 14 HOH P .   ? HOH A 546 . ? 1_555 ? 
22 AC4 4  HIS B 91  ? HIS B 91  . ? 1_555 ? 
23 AC4 4  HIS B 93  ? HIS B 93  . ? 1_555 ? 
24 AC4 4  HIS B 117 ? HIS B 117 . ? 1_555 ? 
25 AC4 4  5EF J .   ? 5EF B 303 . ? 1_555 ? 
26 AC5 6  THR B 44  ? THR B 44  . ? 1_555 ? 
27 AC5 6  LEU B 46  ? LEU B 46  . ? 1_555 ? 
28 AC5 6  GLY B 80  ? GLY B 80  . ? 1_555 ? 
29 AC5 6  LEU B 81  ? LEU B 81  . ? 1_555 ? 
30 AC5 6  TYR B 190 ? TYR B 190 . ? 1_555 ? 
31 AC5 6  ARG B 192 ? ARG B 192 . ? 1_555 ? 
32 AC6 14 ASN B 64  ? ASN B 64  . ? 1_555 ? 
33 AC6 14 SER B 67  ? SER B 67  . ? 1_555 ? 
34 AC6 14 HIS B 91  ? HIS B 91  . ? 1_555 ? 
35 AC6 14 HIS B 93  ? HIS B 93  . ? 1_555 ? 
36 AC6 14 HIS B 117 ? HIS B 117 . ? 1_555 ? 
37 AC6 14 VAL B 119 ? VAL B 119 . ? 1_555 ? 
38 AC6 14 ALA B 129 ? ALA B 129 . ? 1_555 ? 
39 AC6 14 SER B 133 ? SER B 133 . ? 1_555 ? 
40 AC6 14 LEU B 197 ? LEU B 197 . ? 1_555 ? 
41 AC6 14 THR B 198 ? THR B 198 . ? 1_555 ? 
42 AC6 14 THR B 199 ? THR B 199 . ? 1_555 ? 
43 AC6 14 ZN  H .   ? ZN  B 301 . ? 1_555 ? 
44 AC6 14 HOH Q .   ? HOH B 402 . ? 1_555 ? 
45 AC6 14 HOH Q .   ? HOH B 598 . ? 1_555 ? 
46 AC7 4  HIS C 91  ? HIS C 91  . ? 1_555 ? 
47 AC7 4  HIS C 93  ? HIS C 93  . ? 1_555 ? 
48 AC7 4  HIS C 117 ? HIS C 117 . ? 1_555 ? 
49 AC7 4  5EF L .   ? 5EF C 302 . ? 1_555 ? 
50 AC8 16 ASN C 64  ? ASN C 64  . ? 1_555 ? 
51 AC8 16 GLN C 89  ? GLN C 89  . ? 1_555 ? 
52 AC8 16 HIS C 91  ? HIS C 91  . ? 1_555 ? 
53 AC8 16 HIS C 93  ? HIS C 93  . ? 1_555 ? 
54 AC8 16 GLU C 104 ? GLU C 104 . ? 1_555 ? 
55 AC8 16 HIS C 117 ? HIS C 117 . ? 1_555 ? 
56 AC8 16 VAL C 119 ? VAL C 119 . ? 1_555 ? 
57 AC8 16 ALA C 129 ? ALA C 129 . ? 1_555 ? 
58 AC8 16 SER C 130 ? SER C 130 . ? 1_555 ? 
59 AC8 16 LEU C 197 ? LEU C 197 . ? 1_555 ? 
60 AC8 16 THR C 198 ? THR C 198 . ? 1_555 ? 
61 AC8 16 THR C 199 ? THR C 199 . ? 1_555 ? 
62 AC8 16 PRO C 200 ? PRO C 200 . ? 1_555 ? 
63 AC8 16 ZN  K .   ? ZN  C 301 . ? 1_555 ? 
64 AC8 16 HOH R .   ? HOH C 518 . ? 1_555 ? 
65 AC8 16 HOH R .   ? HOH C 552 . ? 1_555 ? 
66 AC9 4  HIS D 91  ? HIS D 91  . ? 1_555 ? 
67 AC9 4  HIS D 93  ? HIS D 93  . ? 1_555 ? 
68 AC9 4  HIS D 117 ? HIS D 117 . ? 1_555 ? 
69 AC9 4  5EF O .   ? 5EF D 303 . ? 1_555 ? 
70 AD1 6  SER D 42  ? SER D 42  . ? 1_555 ? 
71 AD1 6  THR D 44  ? THR D 44  . ? 1_555 ? 
72 AD1 6  LEU D 46  ? LEU D 46  . ? 1_555 ? 
73 AD1 6  GLY D 80  ? GLY D 80  . ? 1_555 ? 
74 AD1 6  TYR D 190 ? TYR D 190 . ? 1_555 ? 
75 AD1 6  ARG D 192 ? ARG D 192 . ? 1_555 ? 
76 AD2 13 ASN D 64  ? ASN D 64  . ? 1_555 ? 
77 AD2 13 HIS D 91  ? HIS D 91  . ? 1_555 ? 
78 AD2 13 HIS D 93  ? HIS D 93  . ? 1_555 ? 
79 AD2 13 GLU D 104 ? GLU D 104 . ? 1_555 ? 
80 AD2 13 HIS D 117 ? HIS D 117 . ? 1_555 ? 
81 AD2 13 VAL D 119 ? VAL D 119 . ? 1_555 ? 
82 AD2 13 ALA D 129 ? ALA D 129 . ? 1_555 ? 
83 AD2 13 SER D 130 ? SER D 130 . ? 1_555 ? 
84 AD2 13 LEU D 197 ? LEU D 197 . ? 1_555 ? 
85 AD2 13 THR D 198 ? THR D 198 . ? 1_555 ? 
86 AD2 13 THR D 199 ? THR D 199 . ? 1_555 ? 
87 AD2 13 ZN  M .   ? ZN  D 301 . ? 1_555 ? 
88 AD2 13 HOH S .   ? HOH D 403 . ? 1_555 ? 
# 
_pdbx_entry_details.entry_id                   5LLO 
_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_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O   B HOH 418 ? ? O   B HOH 453 ? ? 1.80 
2 1 O   D HOH 447 ? ? O   D HOH 617 ? ? 1.98 
3 1 O   B HOH 582 ? ? O   B HOH 623 ? ? 2.10 
4 1 OE1 B GLN 49  ? B NE2 B HIS 77  ? ? 2.13 
# 
loop_
_pdbx_validate_rmsd_bond.id 
_pdbx_validate_rmsd_bond.PDB_model_num 
_pdbx_validate_rmsd_bond.auth_atom_id_1 
_pdbx_validate_rmsd_bond.auth_asym_id_1 
_pdbx_validate_rmsd_bond.auth_comp_id_1 
_pdbx_validate_rmsd_bond.auth_seq_id_1 
_pdbx_validate_rmsd_bond.PDB_ins_code_1 
_pdbx_validate_rmsd_bond.label_alt_id_1 
_pdbx_validate_rmsd_bond.auth_atom_id_2 
_pdbx_validate_rmsd_bond.auth_asym_id_2 
_pdbx_validate_rmsd_bond.auth_comp_id_2 
_pdbx_validate_rmsd_bond.auth_seq_id_2 
_pdbx_validate_rmsd_bond.PDB_ins_code_2 
_pdbx_validate_rmsd_bond.label_alt_id_2 
_pdbx_validate_rmsd_bond.bond_value 
_pdbx_validate_rmsd_bond.bond_target_value 
_pdbx_validate_rmsd_bond.bond_deviation 
_pdbx_validate_rmsd_bond.bond_standard_deviation 
_pdbx_validate_rmsd_bond.linker_flag 
1  1 CG A HIS 161 ? ? CD2 A HIS 161 ? ? 1.416 1.354 0.062 0.009 N 
2  1 CG B HIS 120 ? ? CD2 B HIS 120 ? ? 1.409 1.354 0.055 0.009 N 
3  1 CG B HIS 161 ? ? CD2 B HIS 161 ? ? 1.415 1.354 0.061 0.009 N 
4  1 CG B HIS 164 ? ? CD2 B HIS 164 ? ? 1.430 1.354 0.076 0.009 N 
5  1 CG C HIS 93  ? ? CD2 C HIS 93  ? ? 1.411 1.354 0.057 0.009 N 
6  1 CG C HIS 101 ? ? CD2 C HIS 101 ? ? 1.409 1.354 0.055 0.009 N 
7  1 CG C HIS 117 ? ? CD2 C HIS 117 ? ? 1.415 1.354 0.061 0.009 N 
8  1 CG D HIS 77  ? ? CD2 D HIS 77  ? ? 1.412 1.354 0.058 0.009 N 
9  1 CG D HIS 91  ? ? CD2 D HIS 91  ? ? 1.422 1.354 0.068 0.009 N 
10 1 CG D HIS 117 ? ? CD2 D HIS 117 ? ? 1.410 1.354 0.056 0.009 N 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             NE 
_pdbx_validate_rmsd_angle.auth_asym_id_1             C 
_pdbx_validate_rmsd_angle.auth_comp_id_1             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_1              84 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             B 
_pdbx_validate_rmsd_angle.auth_atom_id_2             CZ 
_pdbx_validate_rmsd_angle.auth_asym_id_2             C 
_pdbx_validate_rmsd_angle.auth_comp_id_2             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_2              84 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             B 
_pdbx_validate_rmsd_angle.auth_atom_id_3             NH1 
_pdbx_validate_rmsd_angle.auth_asym_id_3             C 
_pdbx_validate_rmsd_angle.auth_comp_id_3             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_3              84 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             B 
_pdbx_validate_rmsd_angle.angle_value                116.36 
_pdbx_validate_rmsd_angle.angle_target_value         120.30 
_pdbx_validate_rmsd_angle.angle_deviation            -3.94 
_pdbx_validate_rmsd_angle.angle_standard_deviation   0.50 
_pdbx_validate_rmsd_angle.linker_flag                N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ASP B 99  ? ? -152.69 78.06  
2  1 GLU B 137 ? ? 46.98   29.59  
3  1 ASP B 253 ? ? 32.67   51.28  
4  1 GLU B 254 ? ? 71.50   -3.90  
5  1 PHE C 7   ? ? -137.62 -77.12 
6  1 PRO C 9   ? ? -49.48  -8.59  
7  1 ASP C 99  ? ? -151.16 83.85  
8  1 PHE C 252 ? ? -152.74 89.52  
9  1 THR D 88  ? ? -130.08 -39.80 
10 1 ASP D 99  ? ? -156.46 80.14  
11 1 GLU D 254 ? ? 72.60   -2.39  
# 
_phasing.method   MR 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? C HOH 623 ? 6.18 . 
2 1 O ? D HOH 676 ? 6.05 . 
# 
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 A GLN 263 ? A GLN 263 
4 1 Y 1 B MET 1   ? B MET 1   
5 1 Y 1 B SER 2   ? B SER 2   
6 1 Y 1 C MET 1   ? C MET 1   
7 1 Y 1 C SER 2   ? C SER 2   
8 1 Y 1 D MET 1   ? D MET 1   
9 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 
5EF O19  O  N N 1   
5EF C17  C  N N 2   
5EF C6   C  Y N 3   
5EF F11  F  N N 4   
5EF C5   C  Y N 5   
5EF F12  F  N N 6   
5EF F13  F  N N 7   
5EF O16  O  N N 8   
5EF S14  S  N N 9   
5EF O15  O  N N 10  
5EF C18  C  N N 11  
5EF C8   C  Y N 12  
5EF C7   C  Y N 13  
5EF C9   C  Y N 14  
5EF C10  C  Y N 15  
5EF S1   S  N N 16  
5EF O3   O  N N 17  
5EF N4   N  N N 18  
5EF O2   O  N N 19  
5EF N20  N  N N 20  
5EF C21  C  N S 21  
5EF C25  C  N N 22  
5EF C24  C  N N 23  
5EF C23  C  Y N 24  
5EF C29  C  Y N 25  
5EF C28  C  Y N 26  
5EF C27  C  Y N 27  
5EF C26  C  Y N 28  
5EF C22  C  Y N 29  
5EF H1   H  N N 30  
5EF H2   H  N N 31  
5EF H3   H  N N 32  
5EF H4   H  N N 33  
5EF H5   H  N N 34  
5EF H6   H  N N 35  
5EF H7   H  N N 36  
5EF H8   H  N N 37  
5EF H9   H  N N 38  
5EF H10  H  N N 39  
5EF H11  H  N N 40  
5EF H12  H  N N 41  
5EF H13  H  N N 42  
5EF H14  H  N N 43  
5EF H15  H  N N 44  
5EF H16  H  N N 45  
5EF H17  H  N N 46  
ALA N    N  N N 47  
ALA CA   C  N S 48  
ALA C    C  N N 49  
ALA O    O  N N 50  
ALA CB   C  N N 51  
ALA OXT  O  N N 52  
ALA H    H  N N 53  
ALA H2   H  N N 54  
ALA HA   H  N N 55  
ALA HB1  H  N N 56  
ALA HB2  H  N N 57  
ALA HB3  H  N N 58  
ALA HXT  H  N N 59  
ARG N    N  N N 60  
ARG CA   C  N S 61  
ARG C    C  N N 62  
ARG O    O  N N 63  
ARG CB   C  N N 64  
ARG CG   C  N N 65  
ARG CD   C  N N 66  
ARG NE   N  N N 67  
ARG CZ   C  N N 68  
ARG NH1  N  N N 69  
ARG NH2  N  N N 70  
ARG OXT  O  N N 71  
ARG H    H  N N 72  
ARG H2   H  N N 73  
ARG HA   H  N N 74  
ARG HB2  H  N N 75  
ARG HB3  H  N N 76  
ARG HG2  H  N N 77  
ARG HG3  H  N N 78  
ARG HD2  H  N N 79  
ARG HD3  H  N N 80  
ARG HE   H  N N 81  
ARG HH11 H  N N 82  
ARG HH12 H  N N 83  
ARG HH21 H  N N 84  
ARG HH22 H  N N 85  
ARG HXT  H  N N 86  
ASN N    N  N N 87  
ASN CA   C  N S 88  
ASN C    C  N N 89  
ASN O    O  N N 90  
ASN CB   C  N N 91  
ASN CG   C  N N 92  
ASN OD1  O  N N 93  
ASN ND2  N  N N 94  
ASN OXT  O  N N 95  
ASN H    H  N N 96  
ASN H2   H  N N 97  
ASN HA   H  N N 98  
ASN HB2  H  N N 99  
ASN HB3  H  N N 100 
ASN HD21 H  N N 101 
ASN HD22 H  N N 102 
ASN HXT  H  N N 103 
ASP N    N  N N 104 
ASP CA   C  N S 105 
ASP C    C  N N 106 
ASP O    O  N N 107 
ASP CB   C  N N 108 
ASP CG   C  N N 109 
ASP OD1  O  N N 110 
ASP OD2  O  N N 111 
ASP OXT  O  N N 112 
ASP H    H  N N 113 
ASP H2   H  N N 114 
ASP HA   H  N N 115 
ASP HB2  H  N N 116 
ASP HB3  H  N N 117 
ASP HD2  H  N N 118 
ASP HXT  H  N N 119 
CYS N    N  N N 120 
CYS CA   C  N R 121 
CYS C    C  N N 122 
CYS O    O  N N 123 
CYS CB   C  N N 124 
CYS SG   S  N N 125 
CYS OXT  O  N N 126 
CYS H    H  N N 127 
CYS H2   H  N N 128 
CYS HA   H  N N 129 
CYS HB2  H  N N 130 
CYS HB3  H  N N 131 
CYS HG   H  N N 132 
CYS HXT  H  N N 133 
EDO C1   C  N N 134 
EDO O1   O  N N 135 
EDO C2   C  N N 136 
EDO O2   O  N N 137 
EDO H11  H  N N 138 
EDO H12  H  N N 139 
EDO HO1  H  N N 140 
EDO H21  H  N N 141 
EDO H22  H  N N 142 
EDO HO2  H  N N 143 
GLN N    N  N N 144 
GLN CA   C  N S 145 
GLN C    C  N N 146 
GLN O    O  N N 147 
GLN CB   C  N N 148 
GLN CG   C  N N 149 
GLN CD   C  N N 150 
GLN OE1  O  N N 151 
GLN NE2  N  N N 152 
GLN OXT  O  N N 153 
GLN H    H  N N 154 
GLN H2   H  N N 155 
GLN HA   H  N N 156 
GLN HB2  H  N N 157 
GLN HB3  H  N N 158 
GLN HG2  H  N N 159 
GLN HG3  H  N N 160 
GLN HE21 H  N N 161 
GLN HE22 H  N N 162 
GLN HXT  H  N N 163 
GLU N    N  N N 164 
GLU CA   C  N S 165 
GLU C    C  N N 166 
GLU O    O  N N 167 
GLU CB   C  N N 168 
GLU CG   C  N N 169 
GLU CD   C  N N 170 
GLU OE1  O  N N 171 
GLU OE2  O  N N 172 
GLU OXT  O  N N 173 
GLU H    H  N N 174 
GLU H2   H  N N 175 
GLU HA   H  N N 176 
GLU HB2  H  N N 177 
GLU HB3  H  N N 178 
GLU HG2  H  N N 179 
GLU HG3  H  N N 180 
GLU HE2  H  N N 181 
GLU HXT  H  N N 182 
GLY N    N  N N 183 
GLY CA   C  N N 184 
GLY C    C  N N 185 
GLY O    O  N N 186 
GLY OXT  O  N N 187 
GLY H    H  N N 188 
GLY H2   H  N N 189 
GLY HA2  H  N N 190 
GLY HA3  H  N N 191 
GLY HXT  H  N N 192 
HIS N    N  N N 193 
HIS CA   C  N S 194 
HIS C    C  N N 195 
HIS O    O  N N 196 
HIS CB   C  N N 197 
HIS CG   C  Y N 198 
HIS ND1  N  Y N 199 
HIS CD2  C  Y N 200 
HIS CE1  C  Y N 201 
HIS NE2  N  Y N 202 
HIS OXT  O  N N 203 
HIS H    H  N N 204 
HIS H2   H  N N 205 
HIS HA   H  N N 206 
HIS HB2  H  N N 207 
HIS HB3  H  N N 208 
HIS HD1  H  N N 209 
HIS HD2  H  N N 210 
HIS HE1  H  N N 211 
HIS HE2  H  N N 212 
HIS HXT  H  N N 213 
HOH O    O  N N 214 
HOH H1   H  N N 215 
HOH H2   H  N N 216 
ILE N    N  N N 217 
ILE CA   C  N S 218 
ILE C    C  N N 219 
ILE O    O  N N 220 
ILE CB   C  N S 221 
ILE CG1  C  N N 222 
ILE CG2  C  N N 223 
ILE CD1  C  N N 224 
ILE OXT  O  N N 225 
ILE H    H  N N 226 
ILE H2   H  N N 227 
ILE HA   H  N N 228 
ILE HB   H  N N 229 
ILE HG12 H  N N 230 
ILE HG13 H  N N 231 
ILE HG21 H  N N 232 
ILE HG22 H  N N 233 
ILE HG23 H  N N 234 
ILE HD11 H  N N 235 
ILE HD12 H  N N 236 
ILE HD13 H  N N 237 
ILE HXT  H  N N 238 
LEU N    N  N N 239 
LEU CA   C  N S 240 
LEU C    C  N N 241 
LEU O    O  N N 242 
LEU CB   C  N N 243 
LEU CG   C  N N 244 
LEU CD1  C  N N 245 
LEU CD2  C  N N 246 
LEU OXT  O  N N 247 
LEU H    H  N N 248 
LEU H2   H  N N 249 
LEU HA   H  N N 250 
LEU HB2  H  N N 251 
LEU HB3  H  N N 252 
LEU HG   H  N N 253 
LEU HD11 H  N N 254 
LEU HD12 H  N N 255 
LEU HD13 H  N N 256 
LEU HD21 H  N N 257 
LEU HD22 H  N N 258 
LEU HD23 H  N N 259 
LEU HXT  H  N N 260 
LYS N    N  N N 261 
LYS CA   C  N S 262 
LYS C    C  N N 263 
LYS O    O  N N 264 
LYS CB   C  N N 265 
LYS CG   C  N N 266 
LYS CD   C  N N 267 
LYS CE   C  N N 268 
LYS NZ   N  N N 269 
LYS OXT  O  N N 270 
LYS H    H  N N 271 
LYS H2   H  N N 272 
LYS HA   H  N N 273 
LYS HB2  H  N N 274 
LYS HB3  H  N N 275 
LYS HG2  H  N N 276 
LYS HG3  H  N N 277 
LYS HD2  H  N N 278 
LYS HD3  H  N N 279 
LYS HE2  H  N N 280 
LYS HE3  H  N N 281 
LYS HZ1  H  N N 282 
LYS HZ2  H  N N 283 
LYS HZ3  H  N N 284 
LYS HXT  H  N N 285 
MET N    N  N N 286 
MET CA   C  N S 287 
MET C    C  N N 288 
MET O    O  N N 289 
MET CB   C  N N 290 
MET CG   C  N N 291 
MET SD   S  N N 292 
MET CE   C  N N 293 
MET OXT  O  N N 294 
MET H    H  N N 295 
MET H2   H  N N 296 
MET HA   H  N N 297 
MET HB2  H  N N 298 
MET HB3  H  N N 299 
MET HG2  H  N N 300 
MET HG3  H  N N 301 
MET HE1  H  N N 302 
MET HE2  H  N N 303 
MET HE3  H  N N 304 
MET HXT  H  N N 305 
PHE N    N  N N 306 
PHE CA   C  N S 307 
PHE C    C  N N 308 
PHE O    O  N N 309 
PHE CB   C  N N 310 
PHE CG   C  Y N 311 
PHE CD1  C  Y N 312 
PHE CD2  C  Y N 313 
PHE CE1  C  Y N 314 
PHE CE2  C  Y N 315 
PHE CZ   C  Y N 316 
PHE OXT  O  N N 317 
PHE H    H  N N 318 
PHE H2   H  N N 319 
PHE HA   H  N N 320 
PHE HB2  H  N N 321 
PHE HB3  H  N N 322 
PHE HD1  H  N N 323 
PHE HD2  H  N N 324 
PHE HE1  H  N N 325 
PHE HE2  H  N N 326 
PHE HZ   H  N N 327 
PHE HXT  H  N N 328 
PRO N    N  N N 329 
PRO CA   C  N S 330 
PRO C    C  N N 331 
PRO O    O  N N 332 
PRO CB   C  N N 333 
PRO CG   C  N N 334 
PRO CD   C  N N 335 
PRO OXT  O  N N 336 
PRO H    H  N N 337 
PRO HA   H  N N 338 
PRO HB2  H  N N 339 
PRO HB3  H  N N 340 
PRO HG2  H  N N 341 
PRO HG3  H  N N 342 
PRO HD2  H  N N 343 
PRO HD3  H  N N 344 
PRO HXT  H  N N 345 
SER N    N  N N 346 
SER CA   C  N S 347 
SER C    C  N N 348 
SER O    O  N N 349 
SER CB   C  N N 350 
SER OG   O  N N 351 
SER OXT  O  N N 352 
SER H    H  N N 353 
SER H2   H  N N 354 
SER HA   H  N N 355 
SER HB2  H  N N 356 
SER HB3  H  N N 357 
SER HG   H  N N 358 
SER HXT  H  N N 359 
THR N    N  N N 360 
THR CA   C  N S 361 
THR C    C  N N 362 
THR O    O  N N 363 
THR CB   C  N R 364 
THR OG1  O  N N 365 
THR CG2  C  N N 366 
THR OXT  O  N N 367 
THR H    H  N N 368 
THR H2   H  N N 369 
THR HA   H  N N 370 
THR HB   H  N N 371 
THR HG1  H  N N 372 
THR HG21 H  N N 373 
THR HG22 H  N N 374 
THR HG23 H  N N 375 
THR HXT  H  N N 376 
TRP N    N  N N 377 
TRP CA   C  N S 378 
TRP C    C  N N 379 
TRP O    O  N N 380 
TRP CB   C  N N 381 
TRP CG   C  Y N 382 
TRP CD1  C  Y N 383 
TRP CD2  C  Y N 384 
TRP NE1  N  Y N 385 
TRP CE2  C  Y N 386 
TRP CE3  C  Y N 387 
TRP CZ2  C  Y N 388 
TRP CZ3  C  Y N 389 
TRP CH2  C  Y N 390 
TRP OXT  O  N N 391 
TRP H    H  N N 392 
TRP H2   H  N N 393 
TRP HA   H  N N 394 
TRP HB2  H  N N 395 
TRP HB3  H  N N 396 
TRP HD1  H  N N 397 
TRP HE1  H  N N 398 
TRP HE3  H  N N 399 
TRP HZ2  H  N N 400 
TRP HZ3  H  N N 401 
TRP HH2  H  N N 402 
TRP HXT  H  N N 403 
TYR N    N  N N 404 
TYR CA   C  N S 405 
TYR C    C  N N 406 
TYR O    O  N N 407 
TYR CB   C  N N 408 
TYR CG   C  Y N 409 
TYR CD1  C  Y N 410 
TYR CD2  C  Y N 411 
TYR CE1  C  Y N 412 
TYR CE2  C  Y N 413 
TYR CZ   C  Y N 414 
TYR OH   O  N N 415 
TYR OXT  O  N N 416 
TYR H    H  N N 417 
TYR H2   H  N N 418 
TYR HA   H  N N 419 
TYR HB2  H  N N 420 
TYR HB3  H  N N 421 
TYR HD1  H  N N 422 
TYR HD2  H  N N 423 
TYR HE1  H  N N 424 
TYR HE2  H  N N 425 
TYR HH   H  N N 426 
TYR HXT  H  N N 427 
VAL N    N  N N 428 
VAL CA   C  N S 429 
VAL C    C  N N 430 
VAL O    O  N N 431 
VAL CB   C  N N 432 
VAL CG1  C  N N 433 
VAL CG2  C  N N 434 
VAL OXT  O  N N 435 
VAL H    H  N N 436 
VAL H2   H  N N 437 
VAL HA   H  N N 438 
VAL HB   H  N N 439 
VAL HG11 H  N N 440 
VAL HG12 H  N N 441 
VAL HG13 H  N N 442 
VAL HG21 H  N N 443 
VAL HG22 H  N N 444 
VAL HG23 H  N N 445 
VAL HXT  H  N N 446 
ZN  ZN   ZN N N 447 
# 
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 
5EF C28 C29  doub Y N 1   
5EF C28 C27  sing Y N 2   
5EF C29 C23  sing Y N 3   
5EF C27 C26  doub Y N 4   
5EF C23 C24  sing N N 5   
5EF C23 C22  doub Y N 6   
5EF O19 C18  sing N N 7   
5EF C24 C25  sing N N 8   
5EF C26 C22  sing Y N 9   
5EF C18 C17  sing N N 10  
5EF C22 C21  sing N N 11  
5EF C25 C21  sing N N 12  
5EF C17 S14  sing N N 13  
5EF C21 N20  sing N N 14  
5EF O15 S14  doub N N 15  
5EF S14 C8   sing N N 16  
5EF S14 O16  doub N N 17  
5EF N20 C9   sing N N 18  
5EF C9  C8   doub Y N 19  
5EF C9  C10  sing Y N 20  
5EF C8  C7   sing Y N 21  
5EF C7  F12  sing N N 22  
5EF C7  C6   doub Y N 23  
5EF F13 C10  sing N N 24  
5EF C10 C5   doub Y N 25  
5EF C6  C5   sing Y N 26  
5EF C6  F11  sing N N 27  
5EF C5  S1   sing N N 28  
5EF N4  S1   sing N N 29  
5EF S1  O3   doub N N 30  
5EF S1  O2   doub N N 31  
5EF O19 H1   sing N N 32  
5EF C17 H2   sing N N 33  
5EF C17 H3   sing N N 34  
5EF C18 H4   sing N N 35  
5EF C18 H5   sing N N 36  
5EF N4  H6   sing N N 37  
5EF N4  H7   sing N N 38  
5EF N20 H8   sing N N 39  
5EF C21 H9   sing N N 40  
5EF C25 H10  sing N N 41  
5EF C25 H11  sing N N 42  
5EF C24 H12  sing N N 43  
5EF C24 H13  sing N N 44  
5EF C29 H14  sing N N 45  
5EF C28 H15  sing N N 46  
5EF C27 H16  sing N N 47  
5EF C26 H17  sing N N 48  
ALA N   CA   sing N N 49  
ALA N   H    sing N N 50  
ALA N   H2   sing N N 51  
ALA CA  C    sing N N 52  
ALA CA  CB   sing N N 53  
ALA CA  HA   sing N N 54  
ALA C   O    doub N N 55  
ALA C   OXT  sing N N 56  
ALA CB  HB1  sing N N 57  
ALA CB  HB2  sing N N 58  
ALA CB  HB3  sing N N 59  
ALA OXT HXT  sing N N 60  
ARG N   CA   sing N N 61  
ARG N   H    sing N N 62  
ARG N   H2   sing N N 63  
ARG CA  C    sing N N 64  
ARG CA  CB   sing N N 65  
ARG CA  HA   sing N N 66  
ARG C   O    doub N N 67  
ARG C   OXT  sing N N 68  
ARG CB  CG   sing N N 69  
ARG CB  HB2  sing N N 70  
ARG CB  HB3  sing N N 71  
ARG CG  CD   sing N N 72  
ARG CG  HG2  sing N N 73  
ARG CG  HG3  sing N N 74  
ARG CD  NE   sing N N 75  
ARG CD  HD2  sing N N 76  
ARG CD  HD3  sing N N 77  
ARG NE  CZ   sing N N 78  
ARG NE  HE   sing N N 79  
ARG CZ  NH1  sing N N 80  
ARG CZ  NH2  doub N N 81  
ARG NH1 HH11 sing N N 82  
ARG NH1 HH12 sing N N 83  
ARG NH2 HH21 sing N N 84  
ARG NH2 HH22 sing N N 85  
ARG OXT HXT  sing N N 86  
ASN N   CA   sing N N 87  
ASN N   H    sing N N 88  
ASN N   H2   sing N N 89  
ASN CA  C    sing N N 90  
ASN CA  CB   sing N N 91  
ASN CA  HA   sing N N 92  
ASN C   O    doub N N 93  
ASN C   OXT  sing N N 94  
ASN CB  CG   sing N N 95  
ASN CB  HB2  sing N N 96  
ASN CB  HB3  sing N N 97  
ASN CG  OD1  doub N N 98  
ASN CG  ND2  sing N N 99  
ASN ND2 HD21 sing N N 100 
ASN ND2 HD22 sing N N 101 
ASN OXT HXT  sing N N 102 
ASP N   CA   sing N N 103 
ASP N   H    sing N N 104 
ASP N   H2   sing N N 105 
ASP CA  C    sing N N 106 
ASP CA  CB   sing N N 107 
ASP CA  HA   sing N N 108 
ASP C   O    doub N N 109 
ASP C   OXT  sing N N 110 
ASP CB  CG   sing N N 111 
ASP CB  HB2  sing N N 112 
ASP CB  HB3  sing N N 113 
ASP CG  OD1  doub N N 114 
ASP CG  OD2  sing N N 115 
ASP OD2 HD2  sing N N 116 
ASP OXT HXT  sing N N 117 
CYS N   CA   sing N N 118 
CYS N   H    sing N N 119 
CYS N   H2   sing N N 120 
CYS CA  C    sing N N 121 
CYS CA  CB   sing N N 122 
CYS CA  HA   sing N N 123 
CYS C   O    doub N N 124 
CYS C   OXT  sing N N 125 
CYS CB  SG   sing N N 126 
CYS CB  HB2  sing N N 127 
CYS CB  HB3  sing N N 128 
CYS SG  HG   sing N N 129 
CYS OXT HXT  sing N N 130 
EDO C1  O1   sing N N 131 
EDO C1  C2   sing N N 132 
EDO C1  H11  sing N N 133 
EDO C1  H12  sing N N 134 
EDO O1  HO1  sing N N 135 
EDO C2  O2   sing N N 136 
EDO C2  H21  sing N N 137 
EDO C2  H22  sing N N 138 
EDO O2  HO2  sing N N 139 
GLN N   CA   sing N N 140 
GLN N   H    sing N N 141 
GLN N   H2   sing N N 142 
GLN CA  C    sing N N 143 
GLN CA  CB   sing N N 144 
GLN CA  HA   sing N N 145 
GLN C   O    doub N N 146 
GLN C   OXT  sing N N 147 
GLN CB  CG   sing N N 148 
GLN CB  HB2  sing N N 149 
GLN CB  HB3  sing N N 150 
GLN CG  CD   sing N N 151 
GLN CG  HG2  sing N N 152 
GLN CG  HG3  sing N N 153 
GLN CD  OE1  doub N N 154 
GLN CD  NE2  sing N N 155 
GLN NE2 HE21 sing N N 156 
GLN NE2 HE22 sing N N 157 
GLN OXT HXT  sing N N 158 
GLU N   CA   sing N N 159 
GLU N   H    sing N N 160 
GLU N   H2   sing N N 161 
GLU CA  C    sing N N 162 
GLU CA  CB   sing N N 163 
GLU CA  HA   sing N N 164 
GLU C   O    doub N N 165 
GLU C   OXT  sing N N 166 
GLU CB  CG   sing N N 167 
GLU CB  HB2  sing N N 168 
GLU CB  HB3  sing N N 169 
GLU CG  CD   sing N N 170 
GLU CG  HG2  sing N N 171 
GLU CG  HG3  sing N N 172 
GLU CD  OE1  doub N N 173 
GLU CD  OE2  sing N N 174 
GLU OE2 HE2  sing N N 175 
GLU OXT HXT  sing N N 176 
GLY N   CA   sing N N 177 
GLY N   H    sing N N 178 
GLY N   H2   sing N N 179 
GLY CA  C    sing N N 180 
GLY CA  HA2  sing N N 181 
GLY CA  HA3  sing N N 182 
GLY C   O    doub N N 183 
GLY C   OXT  sing N N 184 
GLY OXT HXT  sing N N 185 
HIS N   CA   sing N N 186 
HIS N   H    sing N N 187 
HIS N   H2   sing N N 188 
HIS CA  C    sing N N 189 
HIS CA  CB   sing N N 190 
HIS CA  HA   sing N N 191 
HIS C   O    doub N N 192 
HIS C   OXT  sing N N 193 
HIS CB  CG   sing N N 194 
HIS CB  HB2  sing N N 195 
HIS CB  HB3  sing N N 196 
HIS CG  ND1  sing Y N 197 
HIS CG  CD2  doub Y N 198 
HIS ND1 CE1  doub Y N 199 
HIS ND1 HD1  sing N N 200 
HIS CD2 NE2  sing Y N 201 
HIS CD2 HD2  sing N N 202 
HIS CE1 NE2  sing Y N 203 
HIS CE1 HE1  sing N N 204 
HIS NE2 HE2  sing N N 205 
HIS OXT HXT  sing N N 206 
HOH O   H1   sing N N 207 
HOH O   H2   sing N N 208 
ILE N   CA   sing N N 209 
ILE N   H    sing N N 210 
ILE N   H2   sing N N 211 
ILE CA  C    sing N N 212 
ILE CA  CB   sing N N 213 
ILE CA  HA   sing N N 214 
ILE C   O    doub N N 215 
ILE C   OXT  sing N N 216 
ILE CB  CG1  sing N N 217 
ILE CB  CG2  sing N N 218 
ILE CB  HB   sing N N 219 
ILE CG1 CD1  sing N N 220 
ILE CG1 HG12 sing N N 221 
ILE CG1 HG13 sing N N 222 
ILE CG2 HG21 sing N N 223 
ILE CG2 HG22 sing N N 224 
ILE CG2 HG23 sing N N 225 
ILE CD1 HD11 sing N N 226 
ILE CD1 HD12 sing N N 227 
ILE CD1 HD13 sing N N 228 
ILE OXT HXT  sing N N 229 
LEU N   CA   sing N N 230 
LEU N   H    sing N N 231 
LEU N   H2   sing N N 232 
LEU CA  C    sing N N 233 
LEU CA  CB   sing N N 234 
LEU CA  HA   sing N N 235 
LEU C   O    doub N N 236 
LEU C   OXT  sing N N 237 
LEU CB  CG   sing N N 238 
LEU CB  HB2  sing N N 239 
LEU CB  HB3  sing N N 240 
LEU CG  CD1  sing N N 241 
LEU CG  CD2  sing N N 242 
LEU CG  HG   sing N N 243 
LEU CD1 HD11 sing N N 244 
LEU CD1 HD12 sing N N 245 
LEU CD1 HD13 sing N N 246 
LEU CD2 HD21 sing N N 247 
LEU CD2 HD22 sing N N 248 
LEU CD2 HD23 sing N N 249 
LEU OXT HXT  sing N N 250 
LYS N   CA   sing N N 251 
LYS N   H    sing N N 252 
LYS N   H2   sing N N 253 
LYS CA  C    sing N N 254 
LYS CA  CB   sing N N 255 
LYS CA  HA   sing N N 256 
LYS C   O    doub N N 257 
LYS C   OXT  sing N N 258 
LYS CB  CG   sing N N 259 
LYS CB  HB2  sing N N 260 
LYS CB  HB3  sing N N 261 
LYS CG  CD   sing N N 262 
LYS CG  HG2  sing N N 263 
LYS CG  HG3  sing N N 264 
LYS CD  CE   sing N N 265 
LYS CD  HD2  sing N N 266 
LYS CD  HD3  sing N N 267 
LYS CE  NZ   sing N N 268 
LYS CE  HE2  sing N N 269 
LYS CE  HE3  sing N N 270 
LYS NZ  HZ1  sing N N 271 
LYS NZ  HZ2  sing N N 272 
LYS NZ  HZ3  sing N N 273 
LYS OXT HXT  sing N N 274 
MET N   CA   sing N N 275 
MET N   H    sing N N 276 
MET N   H2   sing N N 277 
MET CA  C    sing N N 278 
MET CA  CB   sing N N 279 
MET CA  HA   sing N N 280 
MET C   O    doub N N 281 
MET C   OXT  sing N N 282 
MET CB  CG   sing N N 283 
MET CB  HB2  sing N N 284 
MET CB  HB3  sing N N 285 
MET CG  SD   sing N N 286 
MET CG  HG2  sing N N 287 
MET CG  HG3  sing N N 288 
MET SD  CE   sing N N 289 
MET CE  HE1  sing N N 290 
MET CE  HE2  sing N N 291 
MET CE  HE3  sing N N 292 
MET OXT HXT  sing N N 293 
PHE N   CA   sing N N 294 
PHE N   H    sing N N 295 
PHE N   H2   sing N N 296 
PHE CA  C    sing N N 297 
PHE CA  CB   sing N N 298 
PHE CA  HA   sing N N 299 
PHE C   O    doub N N 300 
PHE C   OXT  sing N N 301 
PHE CB  CG   sing N N 302 
PHE CB  HB2  sing N N 303 
PHE CB  HB3  sing N N 304 
PHE CG  CD1  doub Y N 305 
PHE CG  CD2  sing Y N 306 
PHE CD1 CE1  sing Y N 307 
PHE CD1 HD1  sing N N 308 
PHE CD2 CE2  doub Y N 309 
PHE CD2 HD2  sing N N 310 
PHE CE1 CZ   doub Y N 311 
PHE CE1 HE1  sing N N 312 
PHE CE2 CZ   sing Y N 313 
PHE CE2 HE2  sing N N 314 
PHE CZ  HZ   sing N N 315 
PHE OXT HXT  sing N N 316 
PRO N   CA   sing N N 317 
PRO N   CD   sing N N 318 
PRO N   H    sing N N 319 
PRO CA  C    sing N N 320 
PRO CA  CB   sing N N 321 
PRO CA  HA   sing N N 322 
PRO C   O    doub N N 323 
PRO C   OXT  sing N N 324 
PRO CB  CG   sing N N 325 
PRO CB  HB2  sing N N 326 
PRO CB  HB3  sing N N 327 
PRO CG  CD   sing N N 328 
PRO CG  HG2  sing N N 329 
PRO CG  HG3  sing N N 330 
PRO CD  HD2  sing N N 331 
PRO CD  HD3  sing N N 332 
PRO OXT HXT  sing N N 333 
SER N   CA   sing N N 334 
SER N   H    sing N N 335 
SER N   H2   sing N N 336 
SER CA  C    sing N N 337 
SER CA  CB   sing N N 338 
SER CA  HA   sing N N 339 
SER C   O    doub N N 340 
SER C   OXT  sing N N 341 
SER CB  OG   sing N N 342 
SER CB  HB2  sing N N 343 
SER CB  HB3  sing N N 344 
SER OG  HG   sing N N 345 
SER OXT HXT  sing N N 346 
THR N   CA   sing N N 347 
THR N   H    sing N N 348 
THR N   H2   sing N N 349 
THR CA  C    sing N N 350 
THR CA  CB   sing N N 351 
THR CA  HA   sing N N 352 
THR C   O    doub N N 353 
THR C   OXT  sing N N 354 
THR CB  OG1  sing N N 355 
THR CB  CG2  sing N N 356 
THR CB  HB   sing N N 357 
THR OG1 HG1  sing N N 358 
THR CG2 HG21 sing N N 359 
THR CG2 HG22 sing N N 360 
THR CG2 HG23 sing N N 361 
THR OXT HXT  sing N N 362 
TRP N   CA   sing N N 363 
TRP N   H    sing N N 364 
TRP N   H2   sing N N 365 
TRP CA  C    sing N N 366 
TRP CA  CB   sing N N 367 
TRP CA  HA   sing N N 368 
TRP C   O    doub N N 369 
TRP C   OXT  sing N N 370 
TRP CB  CG   sing N N 371 
TRP CB  HB2  sing N N 372 
TRP CB  HB3  sing N N 373 
TRP CG  CD1  doub Y N 374 
TRP CG  CD2  sing Y N 375 
TRP CD1 NE1  sing Y N 376 
TRP CD1 HD1  sing N N 377 
TRP CD2 CE2  doub Y N 378 
TRP CD2 CE3  sing Y N 379 
TRP NE1 CE2  sing Y N 380 
TRP NE1 HE1  sing N N 381 
TRP CE2 CZ2  sing Y N 382 
TRP CE3 CZ3  doub Y N 383 
TRP CE3 HE3  sing N N 384 
TRP CZ2 CH2  doub Y N 385 
TRP CZ2 HZ2  sing N N 386 
TRP CZ3 CH2  sing Y N 387 
TRP CZ3 HZ3  sing N N 388 
TRP CH2 HH2  sing N N 389 
TRP OXT HXT  sing N N 390 
TYR N   CA   sing N N 391 
TYR N   H    sing N N 392 
TYR N   H2   sing N N 393 
TYR CA  C    sing N N 394 
TYR CA  CB   sing N N 395 
TYR CA  HA   sing N N 396 
TYR C   O    doub N N 397 
TYR C   OXT  sing N N 398 
TYR CB  CG   sing N N 399 
TYR CB  HB2  sing N N 400 
TYR CB  HB3  sing N N 401 
TYR CG  CD1  doub Y N 402 
TYR CG  CD2  sing Y N 403 
TYR CD1 CE1  sing Y N 404 
TYR CD1 HD1  sing N N 405 
TYR CD2 CE2  doub Y N 406 
TYR CD2 HD2  sing N N 407 
TYR CE1 CZ   doub Y N 408 
TYR CE1 HE1  sing N N 409 
TYR CE2 CZ   sing Y N 410 
TYR CE2 HE2  sing N N 411 
TYR CZ  OH   sing N N 412 
TYR OH  HH   sing N N 413 
TYR OXT HXT  sing N N 414 
VAL N   CA   sing N N 415 
VAL N   H    sing N N 416 
VAL N   H2   sing N N 417 
VAL CA  C    sing N N 418 
VAL CA  CB   sing N N 419 
VAL CA  HA   sing N N 420 
VAL C   O    doub N N 421 
VAL C   OXT  sing N N 422 
VAL CB  CG1  sing N N 423 
VAL CB  CG2  sing N N 424 
VAL CB  HB   sing N N 425 
VAL CG1 HG11 sing N N 426 
VAL CG1 HG12 sing N N 427 
VAL CG1 HG13 sing N N 428 
VAL CG2 HG21 sing N N 429 
VAL CG2 HG22 sing N N 430 
VAL CG2 HG23 sing N N 431 
VAL OXT HXT  sing N N 432 
# 
_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                    5LLO 
_atom_sites.fract_transf_matrix[1][1]   0.012938 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.004443 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.013493 
_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]   0.011545 
_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  
F  
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . LYS A 1 3   ? 15.886  17.380  18.601  1.00 36.20 ? 3   LYS A N   1 
ATOM   2    C  CA  . LYS A 1 3   ? 16.956  16.387  18.286  1.00 37.25 ? 3   LYS A CA  1 
ATOM   3    C  C   . LYS A 1 3   ? 16.315  14.996  18.204  1.00 33.55 ? 3   LYS A C   1 
ATOM   4    O  O   . LYS A 1 3   ? 15.477  14.604  19.034  1.00 34.65 ? 3   LYS A O   1 
ATOM   5    C  CB  . LYS A 1 3   ? 18.061  16.395  19.345  1.00 43.00 ? 3   LYS A CB  1 
ATOM   6    C  CG  . LYS A 1 3   ? 19.296  15.583  18.953  1.00 44.16 ? 3   LYS A CG  1 
ATOM   7    C  CD  . LYS A 1 3   ? 20.312  15.498  20.084  1.00 46.66 ? 3   LYS A CD  1 
ATOM   8    C  CE  . LYS A 1 3   ? 21.735  15.630  19.520  1.00 48.69 ? 3   LYS A CE  1 
ATOM   9    N  NZ  . LYS A 1 3   ? 22.720  14.665  20.119  1.00 47.33 ? 3   LYS A NZ  1 
ATOM   10   N  N   . TRP A 1 4   ? 16.783  14.226  17.247  1.00 24.79 ? 4   TRP A N   1 
ATOM   11   C  CA  . TRP A 1 4   ? 16.019  13.102  16.813  1.00 19.99 ? 4   TRP A CA  1 
ATOM   12   C  C   . TRP A 1 4   ? 16.038  11.944  17.809  1.00 19.34 ? 4   TRP A C   1 
ATOM   13   O  O   . TRP A 1 4   ? 16.982  11.778  18.600  1.00 18.69 ? 4   TRP A O   1 
ATOM   14   C  CB  . TRP A 1 4   ? 16.497  12.724  15.410  1.00 16.47 ? 4   TRP A CB  1 
ATOM   15   C  CG  . TRP A 1 4   ? 17.854  12.137  15.356  1.00 14.98 ? 4   TRP A CG  1 
ATOM   16   C  CD1 . TRP A 1 4   ? 19.043  12.802  15.164  1.00 15.62 ? 4   TRP A CD1 1 
ATOM   17   C  CD2 . TRP A 1 4   ? 18.219  10.697  15.483  1.00 13.57 ? 4   TRP A CD2 1 
ATOM   18   N  NE1 . TRP A 1 4   ? 20.099  11.908  15.113  1.00 16.12 ? 4   TRP A NE1 1 
ATOM   19   C  CE2 . TRP A 1 4   ? 19.645  10.617  15.313  1.00 15.31 ? 4   TRP A CE2 1 
ATOM   20   C  CE3 . TRP A 1 4   ? 17.490  9.480   15.658  1.00 13.28 ? 4   TRP A CE3 1 
ATOM   21   C  CZ2 . TRP A 1 4   ? 20.312  9.406   15.335  1.00 15.11 ? 4   TRP A CZ2 1 
ATOM   22   C  CZ3 . TRP A 1 4   ? 18.180  8.272   15.678  1.00 13.00 ? 4   TRP A CZ3 1 
ATOM   23   C  CH2 . TRP A 1 4   ? 19.573  8.249   15.528  1.00 14.24 ? 4   TRP A CH2 1 
ATOM   24   N  N   . THR A 1 5   ? 14.942  11.204  17.788  1.00 18.22 ? 5   THR A N   1 
ATOM   25   C  CA  . THR A 1 5   ? 14.745  10.062  18.655  1.00 18.13 ? 5   THR A CA  1 
ATOM   26   C  C   . THR A 1 5   ? 14.013  9.018   17.840  1.00 14.92 ? 5   THR A C   1 
ATOM   27   O  O   . THR A 1 5   ? 13.787  9.190   16.631  1.00 14.03 ? 5   THR A O   1 
ATOM   28   C  CB  . THR A 1 5   ? 13.820  10.407  19.820  1.00 19.71 ? 5   THR A CB  1 
ATOM   29   O  OG1 . THR A 1 5   ? 12.543  10.672  19.225  1.00 19.72 ? 5   THR A OG1 1 
ATOM   30   C  CG2 . THR A 1 5   ? 14.324  11.682  20.570  1.00 18.79 ? 5   THR A CG2 1 
ATOM   31   N  N   . TYR A 1 6   ? 13.678  7.890   18.525  1.00 17.65 ? 6   TYR A N   1 
ATOM   32   C  CA  . TYR A 1 6   ? 12.916  6.772   17.983  1.00 17.98 ? 6   TYR A CA  1 
ATOM   33   C  C   . TYR A 1 6   ? 11.449  6.719   18.511  1.00 18.98 ? 6   TYR A C   1 
ATOM   34   O  O   . TYR A 1 6   ? 10.725  5.763   18.253  1.00 19.55 ? 6   TYR A O   1 
ATOM   35   C  CB  . TYR A 1 6   ? 13.591  5.394   18.228  1.00 17.56 ? 6   TYR A CB  1 
ATOM   36   C  CG  . TYR A 1 6   ? 14.851  5.105   17.426  1.00 15.62 ? 6   TYR A CG  1 
ATOM   37   C  CD1 . TYR A 1 6   ? 16.104  5.370   17.955  1.00 16.02 ? 6   TYR A CD1 1 
ATOM   38   C  CD2 . TYR A 1 6   ? 14.782  4.529   16.163  1.00 12.94 ? 6   TYR A CD2 1 
ATOM   39   C  CE1 . TYR A 1 6   ? 17.259  5.096   17.243  1.00 15.20 ? 6   TYR A CE1 1 
ATOM   40   C  CE2 . TYR A 1 6   ? 15.936  4.251   15.444  1.00 12.99 ? 6   TYR A CE2 1 
ATOM   41   C  CZ  . TYR A 1 6   ? 17.172  4.539   15.992  1.00 14.52 ? 6   TYR A CZ  1 
ATOM   42   O  OH  . TYR A 1 6   ? 18.330  4.272   15.297  1.00 15.23 ? 6   TYR A OH  1 
ATOM   43   N  N   . PHE A 1 7   ? 11.011  7.703   19.311  1.00 24.89 ? 7   PHE A N   1 
ATOM   44   C  CA  . PHE A 1 7   ? 9.714   7.616   20.017  1.00 32.31 ? 7   PHE A CA  1 
ATOM   45   C  C   . PHE A 1 7   ? 9.225   9.032   20.246  1.00 35.00 ? 7   PHE A C   1 
ATOM   46   O  O   . PHE A 1 7   ? 9.961   9.807   20.839  1.00 37.67 ? 7   PHE A O   1 
ATOM   47   C  CB  . PHE A 1 7   ? 9.925   6.923   21.392  1.00 36.21 ? 7   PHE A CB  1 
ATOM   48   C  CG  . PHE A 1 7   ? 8.651   6.802   22.264  1.00 44.76 ? 7   PHE A CG  1 
ATOM   49   C  CD1 . PHE A 1 7   ? 7.755   5.720   22.099  1.00 46.33 ? 7   PHE A CD1 1 
ATOM   50   C  CD2 . PHE A 1 7   ? 8.363   7.740   23.275  1.00 48.84 ? 7   PHE A CD2 1 
ATOM   51   C  CE1 . PHE A 1 7   ? 6.606   5.598   22.902  1.00 43.14 ? 7   PHE A CE1 1 
ATOM   52   C  CE2 . PHE A 1 7   ? 7.208   7.618   24.067  1.00 47.28 ? 7   PHE A CE2 1 
ATOM   53   C  CZ  . PHE A 1 7   ? 6.335   6.543   23.881  1.00 49.24 ? 7   PHE A CZ  1 
ATOM   54   N  N   . GLY A 1 8   ? 8.009   9.382   19.813  1.00 31.67 ? 8   GLY A N   1 
ATOM   55   C  CA  . GLY A 1 8   ? 7.380   10.636  20.309  1.00 29.50 ? 8   GLY A CA  1 
ATOM   56   C  C   . GLY A 1 8   ? 7.434   11.547  19.108  1.00 33.56 ? 8   GLY A C   1 
ATOM   57   O  O   . GLY A 1 8   ? 7.561   11.063  17.974  1.00 36.57 ? 8   GLY A O   1 
ATOM   58   N  N   . PRO A 1 9   ? 7.405   12.862  19.332  1.00 27.37 ? 9   PRO A N   1 
ATOM   59   C  CA  . PRO A 1 9   ? 7.261   13.834  18.237  1.00 27.14 ? 9   PRO A CA  1 
ATOM   60   C  C   . PRO A 1 9   ? 8.543   14.018  17.471  1.00 22.31 ? 9   PRO A C   1 
ATOM   61   O  O   . PRO A 1 9   ? 8.551   14.599  16.411  1.00 22.57 ? 9   PRO A O   1 
ATOM   62   C  CB  . PRO A 1 9   ? 6.934   15.159  18.973  1.00 28.46 ? 9   PRO A CB  1 
ATOM   63   C  CG  . PRO A 1 9   ? 7.376   14.979  20.381  1.00 25.76 ? 9   PRO A CG  1 
ATOM   64   C  CD  . PRO A 1 9   ? 7.649   13.506  20.644  1.00 30.10 ? 9   PRO A CD  1 
ATOM   65   N  N   . ASP A 1 10  ? 9.645   13.471  17.997  1.00 22.42 ? 10  ASP A N   1 
ATOM   66   C  CA  . ASP A 1 10  ? 10.890  13.609  17.343  1.00 20.53 ? 10  ASP A CA  1 
ATOM   67   C  C   . ASP A 1 10  ? 11.345  12.323  16.636  1.00 17.95 ? 10  ASP A C   1 
ATOM   68   O  O   . ASP A 1 10  ? 12.567  12.243  16.157  1.00 19.65 ? 10  ASP A O   1 
ATOM   69   C  CB  . ASP A 1 10  ? 11.975  14.078  18.348  1.00 22.16 ? 10  ASP A CB  1 
ATOM   70   C  CG  . ASP A 1 10  ? 11.785  15.557  18.785  1.00 29.88 ? 10  ASP A CG  1 
ATOM   71   O  OD1 . ASP A 1 10  ? 11.320  16.426  17.969  1.00 31.78 ? 10  ASP A OD1 1 
ATOM   72   O  OD2 . ASP A 1 10  ? 12.087  15.839  19.976  1.00 32.03 ? 10  ASP A OD2 1 
ATOM   73   N  N   . GLY A 1 11  ? 10.373  11.389  16.507  1.00 17.43 ? 11  GLY A N   1 
ATOM   74   C  CA  . GLY A 1 11  ? 10.665  9.987   16.000  1.00 11.81 ? 11  GLY A CA  1 
ATOM   75   C  C   . GLY A 1 11  ? 10.742  9.961   14.489  1.00 12.02 ? 11  GLY A C   1 
ATOM   76   O  O   . GLY A 1 11  ? 10.805  11.018  13.831  1.00 13.47 ? 11  GLY A O   1 
ATOM   77   N  N   . GLU A 1 12  ? 10.833  8.729   13.965  1.00 11.82 ? 12  GLU A N   1 
ATOM   78   C  CA  . GLU A 1 12  ? 11.212  8.522   12.593  1.00 10.66 ? 12  GLU A CA  1 
ATOM   79   C  C   . GLU A 1 12  ? 10.401  9.262   11.529  1.00 9.81  ? 12  GLU A C   1 
ATOM   80   O  O   . GLU A 1 12  ? 10.917  9.621   10.450  1.00 9.45  ? 12  GLU A O   1 
ATOM   81   C  CB  . GLU A 1 12  ? 11.477  7.023   12.320  1.00 10.25 ? 12  GLU A CB  1 
ATOM   82   C  CG  . GLU A 1 12  ? 10.177  6.282   12.260  1.00 9.30  ? 12  GLU A CG  1 
ATOM   83   C  CD  . GLU A 1 12  ? 10.452  4.825   12.421  1.00 8.73  ? 12  GLU A CD  1 
ATOM   84   O  OE1 . GLU A 1 12  ? 10.693  4.176   11.379  1.00 10.01 ? 12  GLU A OE1 1 
ATOM   85   O  OE2 . GLU A 1 12  ? 10.485  4.369   13.592  1.00 10.85 ? 12  GLU A OE2 1 
ATOM   86   N  N   . ASN A 1 13  ? 9.088   9.456   11.776  1.00 10.68 ? 13  ASN A N   1 
ATOM   87   C  CA  . ASN A 1 13  ? 8.330   10.061  10.739  1.00 11.17 ? 13  ASN A CA  1 
ATOM   88   C  C   . ASN A 1 13  ? 8.622   11.568  10.628  1.00 10.33 ? 13  ASN A C   1 
ATOM   89   O  O   . ASN A 1 13  ? 8.245   12.147  9.600   1.00 11.80 ? 13  ASN A O   1 
ATOM   90   C  CB  . ASN A 1 13  ? 6.844   9.996   10.996  1.00 10.77 ? 13  ASN A CB  1 
ATOM   91   C  CG  . ASN A 1 13  ? 6.304   8.562   10.910  1.00 11.71 ? 13  ASN A CG  1 
ATOM   92   O  OD1 . ASN A 1 13  ? 6.967   7.707   10.390  1.00 12.48 ? 13  ASN A OD1 1 
ATOM   93   N  ND2 . ASN A 1 13  ? 5.038   8.366   11.345  1.00 11.54 ? 13  ASN A ND2 1 
ATOM   94   N  N   A SER A 1 14  ? 9.316   12.141  11.610  0.50 10.69 ? 14  SER A N   1 
ATOM   95   N  N   B SER A 1 14  ? 9.284   12.140  11.653  0.50 11.37 ? 14  SER A N   1 
ATOM   96   C  CA  A SER A 1 14  ? 9.675   13.554  11.537  0.50 10.79 ? 14  SER A CA  1 
ATOM   97   C  CA  B SER A 1 14  ? 9.705   13.560  11.670  0.50 12.09 ? 14  SER A CA  1 
ATOM   98   C  C   A SER A 1 14  ? 11.146  13.796  11.238  0.50 11.13 ? 14  SER A C   1 
ATOM   99   C  C   B SER A 1 14  ? 11.111  13.788  11.077  0.50 11.75 ? 14  SER A C   1 
ATOM   100  O  O   A SER A 1 14  ? 11.598  14.944  11.271  0.50 10.06 ? 14  SER A O   1 
ATOM   101  O  O   B SER A 1 14  ? 11.507  14.914  10.770  0.50 10.49 ? 14  SER A O   1 
ATOM   102  C  CB  A SER A 1 14  ? 9.381   14.236  12.872  0.50 11.36 ? 14  SER A CB  1 
ATOM   103  C  CB  B SER A 1 14  ? 9.729   14.128  13.120  0.50 13.28 ? 14  SER A CB  1 
ATOM   104  O  OG  A SER A 1 14  ? 8.015   14.093  13.145  0.50 9.70  ? 14  SER A OG  1 
ATOM   105  O  OG  B SER A 1 14  ? 10.818  13.609  13.856  0.50 15.89 ? 14  SER A OG  1 
ATOM   106  N  N   . TRP A 1 15  ? 11.901  12.732  10.968  1.00 10.75 ? 15  TRP A N   1 
ATOM   107  C  CA  . TRP A 1 15  ? 13.338  12.915  10.597  1.00 10.47 ? 15  TRP A CA  1 
ATOM   108  C  C   . TRP A 1 15  ? 13.545  13.756  9.360   1.00 13.27 ? 15  TRP A C   1 
ATOM   109  O  O   . TRP A 1 15  ? 14.545  14.491  9.296   1.00 12.66 ? 15  TRP A O   1 
ATOM   110  C  CB  . TRP A 1 15  ? 14.082  11.578  10.418  1.00 10.53 ? 15  TRP A CB  1 
ATOM   111  C  CG  . TRP A 1 15  ? 14.196  10.792  11.691  1.00 9.37  ? 15  TRP A CG  1 
ATOM   112  C  CD1 . TRP A 1 15  ? 13.943  11.112  13.017  1.00 10.68 ? 15  TRP A CD1 1 
ATOM   113  C  CD2 . TRP A 1 15  ? 14.684  9.404   11.711  1.00 9.43  ? 15  TRP A CD2 1 
ATOM   114  N  NE1 . TRP A 1 15  ? 14.224  9.991   13.836  1.00 11.38 ? 15  TRP A NE1 1 
ATOM   115  C  CE2 . TRP A 1 15  ? 14.686  8.990   13.114  1.00 9.71  ? 15  TRP A CE2 1 
ATOM   116  C  CE3 . TRP A 1 15  ? 15.139  8.556   10.750  1.00 9.78  ? 15  TRP A CE3 1 
ATOM   117  C  CZ2 . TRP A 1 15  ? 15.097  7.682   13.502  1.00 10.16 ? 15  TRP A CZ2 1 
ATOM   118  C  CZ3 . TRP A 1 15  ? 15.568  7.226   11.121  1.00 9.41  ? 15  TRP A CZ3 1 
ATOM   119  C  CH2 . TRP A 1 15  ? 15.536  6.848   12.482  1.00 9.33  ? 15  TRP A CH2 1 
ATOM   120  N  N   . SER A 1 16  ? 12.642  13.686  8.408   1.00 11.90 ? 16  SER A N   1 
ATOM   121  C  CA  . SER A 1 16  ? 12.844  14.299  7.131   1.00 11.96 ? 16  SER A CA  1 
ATOM   122  C  C   . SER A 1 16  ? 12.735  15.820  7.244   1.00 12.31 ? 16  SER A C   1 
ATOM   123  O  O   . SER A 1 16  ? 13.141  16.452  6.274   1.00 12.00 ? 16  SER A O   1 
ATOM   124  C  CB  . SER A 1 16  ? 11.812  13.809  6.136   1.00 11.85 ? 16  SER A CB  1 
ATOM   125  O  OG  . SER A 1 16  ? 10.513  14.101  6.629   1.00 12.79 ? 16  SER A OG  1 
ATOM   126  N  N   . LYS A 1 17  ? 12.213  16.298  8.359   1.00 11.92 ? 17  LYS A N   1 
ATOM   127  C  CA  . LYS A 1 17  ? 12.149  17.815  8.492   1.00 12.31 ? 17  LYS A CA  1 
ATOM   128  C  C   . LYS A 1 17  ? 13.542  18.331  8.506   1.00 14.02 ? 17  LYS A C   1 
ATOM   129  O  O   . LYS A 1 17  ? 13.893  19.299  7.737   1.00 14.16 ? 17  LYS A O   1 
ATOM   130  C  CB  . LYS A 1 17  ? 11.412  18.309  9.711   1.00 14.17 ? 17  LYS A CB  1 
ATOM   131  C  CG  . LYS A 1 17  ? 9.928   17.949  9.673   1.00 19.82 ? 17  LYS A CG  1 
ATOM   132  C  CD  . LYS A 1 17  ? 9.380   18.081  11.089  1.00 23.75 ? 17  LYS A CD  1 
ATOM   133  C  CE  . LYS A 1 17  ? 8.103   17.243  11.293  1.00 26.86 ? 17  LYS A CE  1 
ATOM   134  N  NZ  . LYS A 1 17  ? 7.539   17.531  12.670  1.00 30.63 ? 17  LYS A NZ  1 
ATOM   135  N  N   . LYS A 1 18  ? 14.376  17.769  9.386   1.00 11.78 ? 18  LYS A N   1 
ATOM   136  C  CA  . LYS A 1 18  ? 15.763  18.295  9.529   1.00 12.35 ? 18  LYS A CA  1 
ATOM   137  C  C   . LYS A 1 18  ? 16.727  17.638  8.570   1.00 12.71 ? 18  LYS A C   1 
ATOM   138  O  O   . LYS A 1 18  ? 17.771  18.211  8.225   1.00 15.19 ? 18  LYS A O   1 
ATOM   139  C  CB  . LYS A 1 18  ? 16.234  18.212  11.002  1.00 12.56 ? 18  LYS A CB  1 
ATOM   140  C  CG  . LYS A 1 18  ? 17.689  18.639  11.307  1.00 19.51 ? 18  LYS A CG  1 
ATOM   141  C  CD  . LYS A 1 18  ? 17.903  18.669  12.841  1.00 23.22 ? 18  LYS A CD  1 
ATOM   142  C  CE  . LYS A 1 18  ? 19.284  19.145  13.299  1.00 35.36 ? 18  LYS A CE  1 
ATOM   143  N  NZ  . LYS A 1 18  ? 20.360  18.591  12.441  1.00 37.77 ? 18  LYS A NZ  1 
ATOM   144  N  N   . TYR A 1 19  ? 16.412  16.389  8.170   1.00 11.95 ? 19  TYR A N   1 
ATOM   145  C  CA  . TYR A 1 19  ? 17.306  15.589  7.422   1.00 12.09 ? 19  TYR A CA  1 
ATOM   146  C  C   . TYR A 1 19  ? 16.564  15.128  6.168   1.00 12.59 ? 19  TYR A C   1 
ATOM   147  O  O   . TYR A 1 19  ? 15.927  14.035  6.125   1.00 11.83 ? 19  TYR A O   1 
ATOM   148  C  CB  . TYR A 1 19  ? 17.673  14.399  8.307   1.00 11.17 ? 19  TYR A CB  1 
ATOM   149  C  CG  . TYR A 1 19  ? 18.325  14.747  9.630   1.00 10.59 ? 19  TYR A CG  1 
ATOM   150  C  CD1 . TYR A 1 19  ? 19.740  15.050  9.673   1.00 12.25 ? 19  TYR A CD1 1 
ATOM   151  C  CD2 . TYR A 1 19  ? 17.606  14.755  10.799  1.00 12.15 ? 19  TYR A CD2 1 
ATOM   152  C  CE1 . TYR A 1 19  ? 20.338  15.357  10.880  1.00 12.98 ? 19  TYR A CE1 1 
ATOM   153  C  CE2 . TYR A 1 19  ? 18.204  15.029  12.011  1.00 11.41 ? 19  TYR A CE2 1 
ATOM   154  C  CZ  . TYR A 1 19  ? 19.578  15.308  12.040  1.00 14.50 ? 19  TYR A CZ  1 
ATOM   155  O  OH  . TYR A 1 19  ? 20.145  15.611  13.279  1.00 17.83 ? 19  TYR A OH  1 
ATOM   156  N  N   . PRO A 1 20  ? 16.628  15.883  5.092   1.00 12.01 ? 20  PRO A N   1 
ATOM   157  C  CA  . PRO A 1 20  ? 15.782  15.644  3.948   1.00 12.43 ? 20  PRO A CA  1 
ATOM   158  C  C   . PRO A 1 20  ? 15.998  14.296  3.274   1.00 11.75 ? 20  PRO A C   1 
ATOM   159  O  O   . PRO A 1 20  ? 15.029  13.753  2.649   1.00 13.15 ? 20  PRO A O   1 
ATOM   160  C  CB  . PRO A 1 20  ? 16.117  16.763  2.968   1.00 13.49 ? 20  PRO A CB  1 
ATOM   161  C  CG  . PRO A 1 20  ? 16.717  17.804  3.838   1.00 14.05 ? 20  PRO A CG  1 
ATOM   162  C  CD  . PRO A 1 20  ? 17.399  17.117  5.001   1.00 14.44 ? 20  PRO A CD  1 
ATOM   163  N  N   . SER A 1 21  ? 17.219  13.693  3.344   1.00 10.67 ? 21  SER A N   1 
ATOM   164  C  CA  . SER A 1 21  ? 17.378  12.413  2.717   1.00 10.54 ? 21  SER A CA  1 
ATOM   165  C  C   . SER A 1 21  ? 16.532  11.363  3.356   1.00 10.89 ? 21  SER A C   1 
ATOM   166  O  O   . SER A 1 21  ? 16.323  10.297  2.715   1.00 9.88  ? 21  SER A O   1 
ATOM   167  C  CB  . SER A 1 21  ? 18.867  11.993  2.781   1.00 11.01 ? 21  SER A CB  1 
ATOM   168  O  OG  . SER A 1 21  ? 19.602  12.916  1.924   1.00 13.25 ? 21  SER A OG  1 
ATOM   169  N  N   . CYS A 1 22  ? 16.092  11.581  4.609   1.00 9.32  ? 22  CYS A N   1 
ATOM   170  C  CA  . CYS A 1 22  ? 15.202  10.508  5.252   1.00 9.92  ? 22  CYS A CA  1 
ATOM   171  C  C   . CYS A 1 22  ? 13.858  10.341  4.552   1.00 10.81 ? 22  CYS A C   1 
ATOM   172  O  O   . CYS A 1 22  ? 13.191  9.310   4.742   1.00 11.49 ? 22  CYS A O   1 
ATOM   173  C  CB  . CYS A 1 22  ? 14.986  10.801  6.763   1.00 9.06  ? 22  CYS A CB  1 
ATOM   174  S  SG  . CYS A 1 22  ? 16.591  10.905  7.629   1.00 12.15 ? 22  CYS A SG  1 
ATOM   175  N  N   . GLY A 1 23  ? 13.456  11.385  3.812   1.00 11.16 ? 23  GLY A N   1 
ATOM   176  C  CA  . GLY A 1 23  ? 12.313  11.312  2.856   1.00 11.48 ? 23  GLY A CA  1 
ATOM   177  C  C   . GLY A 1 23  ? 12.633  11.108  1.408   1.00 10.17 ? 23  GLY A C   1 
ATOM   178  O  O   . GLY A 1 23  ? 11.751  11.155  0.549   1.00 11.48 ? 23  GLY A O   1 
ATOM   179  N  N   . GLY A 1 24  ? 13.901  10.872  1.069   1.00 10.88 ? 24  GLY A N   1 
ATOM   180  C  CA  . GLY A 1 24  ? 14.230  10.641  -0.350  1.00 12.88 ? 24  GLY A CA  1 
ATOM   181  C  C   . GLY A 1 24  ? 14.393  9.201   -0.748  1.00 13.57 ? 24  GLY A C   1 
ATOM   182  O  O   . GLY A 1 24  ? 13.681  8.327   -0.174  1.00 14.89 ? 24  GLY A O   1 
ATOM   183  N  N   . LEU A 1 25  ? 15.221  8.945   -1.777  1.00 13.40 ? 25  LEU A N   1 
ATOM   184  C  CA  . LEU A 1 25  ? 15.307  7.636   -2.409  1.00 15.60 ? 25  LEU A CA  1 
ATOM   185  C  C   . LEU A 1 25  ? 16.213  6.691   -1.648  1.00 13.30 ? 25  LEU A C   1 
ATOM   186  O  O   . LEU A 1 25  ? 16.958  7.095   -0.795  1.00 14.17 ? 25  LEU A O   1 
ATOM   187  C  CB  . LEU A 1 25  ? 15.803  7.813   -3.837  1.00 19.42 ? 25  LEU A CB  1 
ATOM   188  C  CG  . LEU A 1 25  ? 14.899  8.687   -4.698  1.00 21.87 ? 25  LEU A CG  1 
ATOM   189  C  CD1 . LEU A 1 25  ? 15.533  8.687   -6.055  1.00 24.55 ? 25  LEU A CD1 1 
ATOM   190  C  CD2 . LEU A 1 25  ? 13.438  8.214   -4.745  1.00 22.59 ? 25  LEU A CD2 1 
ATOM   191  N  N   . LEU A 1 26  ? 16.034  5.394   -1.956  1.00 14.25 ? 26  LEU A N   1 
ATOM   192  C  CA  . LEU A 1 26  ? 16.977  4.303   -1.594  1.00 13.17 ? 26  LEU A CA  1 
ATOM   193  C  C   . LEU A 1 26  ? 17.054  4.140   -0.070  1.00 13.67 ? 26  LEU A C   1 
ATOM   194  O  O   . LEU A 1 26  ? 18.044  3.749   0.481   1.00 14.81 ? 26  LEU A O   1 
ATOM   195  C  CB  . LEU A 1 26  ? 18.408  4.500   -2.187  1.00 14.98 ? 26  LEU A CB  1 
ATOM   196  C  CG  . LEU A 1 26  ? 18.599  4.548   -3.713  1.00 18.43 ? 26  LEU A CG  1 
ATOM   197  C  CD1 . LEU A 1 26  ? 20.092  4.921   -3.988  1.00 20.46 ? 26  LEU A CD1 1 
ATOM   198  C  CD2 . LEU A 1 26  ? 18.216  3.179   -4.262  1.00 20.40 ? 26  LEU A CD2 1 
ATOM   199  N  N   . GLN A 1 27  ? 15.958  4.418   0.603   1.00 11.69 ? 27  GLN A N   1 
ATOM   200  C  CA  . GLN A 1 27  ? 15.914  4.275   2.062   1.00 10.03 ? 27  GLN A CA  1 
ATOM   201  C  C   . GLN A 1 27  ? 15.936  2.806   2.556   1.00 9.36  ? 27  GLN A C   1 
ATOM   202  O  O   . GLN A 1 27  ? 15.319  1.825   1.999   1.00 11.87 ? 27  GLN A O   1 
ATOM   203  C  CB  . GLN A 1 27  ? 14.701  4.977   2.618   1.00 9.17  ? 27  GLN A CB  1 
ATOM   204  C  CG  . GLN A 1 27  ? 14.843  6.495   2.400   1.00 9.73  ? 27  GLN A CG  1 
ATOM   205  C  CD  . GLN A 1 27  ? 16.051  7.019   3.122   1.00 8.33  ? 27  GLN A CD  1 
ATOM   206  O  OE1 . GLN A 1 27  ? 16.082  7.182   4.336   1.00 8.88  ? 27  GLN A OE1 1 
ATOM   207  N  NE2 . GLN A 1 27  ? 17.048  7.349   2.340   1.00 10.30 ? 27  GLN A NE2 1 
ATOM   208  N  N   . SER A 1 28  ? 16.626  2.663   3.696   1.00 10.25 ? 28  SER A N   1 
ATOM   209  C  CA  . SER A 1 28  ? 16.805  1.350   4.404   1.00 8.34  ? 28  SER A CA  1 
ATOM   210  C  C   . SER A 1 28  ? 16.231  1.534   5.820   1.00 8.72  ? 28  SER A C   1 
ATOM   211  O  O   . SER A 1 28  ? 16.141  2.634   6.336   1.00 9.69  ? 28  SER A O   1 
ATOM   212  C  CB  . SER A 1 28  ? 18.307  1.093   4.567   1.00 8.82  ? 28  SER A CB  1 
ATOM   213  O  OG  . SER A 1 28  ? 18.865  0.757   3.296   1.00 9.65  ? 28  SER A OG  1 
ATOM   214  N  N   . PRO A 1 29  ? 15.895  0.442   6.529   1.00 8.28  ? 29  PRO A N   1 
ATOM   215  C  CA  . PRO A 1 29  ? 16.018  -0.985  6.156   1.00 8.91  ? 29  PRO A CA  1 
ATOM   216  C  C   . PRO A 1 29  ? 14.805  -1.475  5.328   1.00 8.79  ? 29  PRO A C   1 
ATOM   217  O  O   . PRO A 1 29  ? 13.909  -0.669  5.105   1.00 10.80 ? 29  PRO A O   1 
ATOM   218  C  CB  . PRO A 1 29  ? 16.055  -1.645  7.549   1.00 9.23  ? 29  PRO A CB  1 
ATOM   219  C  CG  . PRO A 1 29  ? 14.954  -0.892  8.305   1.00 8.14  ? 29  PRO A CG  1 
ATOM   220  C  CD  . PRO A 1 29  ? 15.369  0.577   7.935   1.00 7.70  ? 29  PRO A CD  1 
ATOM   221  N  N   . ILE A 1 30  ? 14.770  -2.721  4.893   1.00 10.23 ? 30  ILE A N   1 
ATOM   222  C  CA  . ILE A 1 30  ? 13.720  -3.223  4.055   1.00 9.35  ? 30  ILE A CA  1 
ATOM   223  C  C   . ILE A 1 30  ? 13.503  -4.699  4.474   1.00 10.10 ? 30  ILE A C   1 
ATOM   224  O  O   . ILE A 1 30  ? 14.294  -5.249  5.249   1.00 10.03 ? 30  ILE A O   1 
ATOM   225  C  CB  . ILE A 1 30  ? 14.128  -3.214  2.550   1.00 9.76  ? 30  ILE A CB  1 
ATOM   226  C  CG1 . ILE A 1 30  ? 15.373  -4.058  2.344   1.00 10.10 ? 30  ILE A CG1 1 
ATOM   227  C  CG2 . ILE A 1 30  ? 14.410  -1.771  2.112   1.00 12.22 ? 30  ILE A CG2 1 
ATOM   228  C  CD1 . ILE A 1 30  ? 15.744  -4.268  0.887   1.00 12.06 ? 30  ILE A CD1 1 
ATOM   229  N  N   . ASP A 1 31  ? 12.310  -5.178  4.101   1.00 10.28 ? 31  ASP A N   1 
ATOM   230  C  CA  . ASP A 1 31  ? 12.026  -6.580  4.274   1.00 11.57 ? 31  ASP A CA  1 
ATOM   231  C  C   . ASP A 1 31  ? 12.636  -7.340  3.139   1.00 12.71 ? 31  ASP A C   1 
ATOM   232  O  O   . ASP A 1 31  ? 12.445  -7.020  1.947   1.00 12.83 ? 31  ASP A O   1 
ATOM   233  C  CB  . ASP A 1 31  ? 10.492  -6.751  4.228   1.00 12.42 ? 31  ASP A CB  1 
ATOM   234  C  CG  . ASP A 1 31  ? 10.052  -8.177  4.439   1.00 14.67 ? 31  ASP A CG  1 
ATOM   235  O  OD1 . ASP A 1 31  ? 10.559  -8.837  5.352   1.00 13.51 ? 31  ASP A OD1 1 
ATOM   236  O  OD2 . ASP A 1 31  ? 9.079   -8.595  3.771   1.00 19.12 ? 31  ASP A OD2 1 
ATOM   237  N  N   . LEU A 1 32  ? 13.374  -8.427  3.489   1.00 11.42 ? 32  LEU A N   1 
ATOM   238  C  CA  . LEU A 1 32  ? 14.022  -9.282  2.554   1.00 14.27 ? 32  LEU A CA  1 
ATOM   239  C  C   . LEU A 1 32  ? 13.072  -10.487 2.358   1.00 16.49 ? 32  LEU A C   1 
ATOM   240  O  O   . LEU A 1 32  ? 12.920  -11.391 3.199   1.00 17.60 ? 32  LEU A O   1 
ATOM   241  C  CB  . LEU A 1 32  ? 15.399  -9.767  3.112   1.00 13.83 ? 32  LEU A CB  1 
ATOM   242  C  CG  . LEU A 1 32  ? 16.275  -8.584  3.589   1.00 13.02 ? 32  LEU A CG  1 
ATOM   243  C  CD1 . LEU A 1 32  ? 17.487  -9.046  4.383   1.00 14.32 ? 32  LEU A CD1 1 
ATOM   244  C  CD2 . LEU A 1 32  ? 16.807  -7.786  2.353   1.00 16.92 ? 32  LEU A CD2 1 
ATOM   245  N  N   . HIS A 1 33  ? 12.368  -10.506 1.249   1.00 19.14 ? 33  HIS A N   1 
ATOM   246  C  CA  . HIS A 1 33  ? 11.456  -11.625 1.084   1.00 22.15 ? 33  HIS A CA  1 
ATOM   247  C  C   . HIS A 1 33  ? 11.574  -12.173 -0.293  1.00 23.04 ? 33  HIS A C   1 
ATOM   248  O  O   . HIS A 1 33  ? 12.107  -11.498 -1.172  1.00 24.18 ? 33  HIS A O   1 
ATOM   249  C  CB  . HIS A 1 33  ? 10.070  -11.131 1.390   1.00 23.99 ? 33  HIS A CB  1 
ATOM   250  C  CG  . HIS A 1 33  ? 9.598   -10.044 0.456   1.00 26.25 ? 33  HIS A CG  1 
ATOM   251  N  ND1 . HIS A 1 33  ? 9.872   -8.754  0.657   1.00 27.11 ? 33  HIS A ND1 1 
ATOM   252  C  CD2 . HIS A 1 33  ? 8.881   -10.108 -0.751  1.00 30.01 ? 33  HIS A CD2 1 
ATOM   253  C  CE1 . HIS A 1 33  ? 9.315   -8.002  -0.348  1.00 30.27 ? 33  HIS A CE1 1 
ATOM   254  N  NE2 . HIS A 1 33  ? 8.728   -8.832  -1.203  1.00 31.50 ? 33  HIS A NE2 1 
ATOM   255  N  N   . SER A 1 34  ? 11.024  -13.371 -0.526  1.00 26.94 ? 34  SER A N   1 
ATOM   256  C  CA  . SER A 1 34  ? 11.443  -14.169 -1.645  1.00 28.92 ? 34  SER A CA  1 
ATOM   257  C  C   . SER A 1 34  ? 11.106  -13.522 -2.955  1.00 29.91 ? 34  SER A C   1 
ATOM   258  O  O   . SER A 1 34  ? 11.841  -13.725 -3.894  1.00 31.96 ? 34  SER A O   1 
ATOM   259  C  CB  . SER A 1 34  ? 10.877  -15.588 -1.620  1.00 33.95 ? 34  SER A CB  1 
ATOM   260  O  OG  . SER A 1 34  ? 10.366  -15.877 -0.354  1.00 43.85 ? 34  SER A OG  1 
ATOM   261  N  N   . ASP A 1 35  ? 10.006  -12.758 -3.011  1.00 30.69 ? 35  ASP A N   1 
ATOM   262  C  CA  . ASP A 1 35  ? 9.542   -12.211 -4.274  1.00 35.67 ? 35  ASP A CA  1 
ATOM   263  C  C   . ASP A 1 35  ? 10.569  -11.285 -4.872  1.00 33.83 ? 35  ASP A C   1 
ATOM   264  O  O   . ASP A 1 35  ? 10.598  -11.129 -6.102  1.00 31.65 ? 35  ASP A O   1 
ATOM   265  C  CB  . ASP A 1 35  ? 8.204   -11.457 -4.115  1.00 38.59 ? 35  ASP A CB  1 
ATOM   266  C  CG  . ASP A 1 35  ? 7.012   -12.405 -3.962  1.00 46.46 ? 35  ASP A CG  1 
ATOM   267  O  OD1 . ASP A 1 35  ? 7.209   -13.650 -4.054  1.00 48.67 ? 35  ASP A OD1 1 
ATOM   268  O  OD2 . ASP A 1 35  ? 5.882   -11.901 -3.756  1.00 45.05 ? 35  ASP A OD2 1 
ATOM   269  N  N   . ILE A 1 36  ? 11.400  -10.659 -4.017  1.00 27.08 ? 36  ILE A N   1 
ATOM   270  C  CA  . ILE A 1 36  ? 12.338  -9.614  -4.487  1.00 25.66 ? 36  ILE A CA  1 
ATOM   271  C  C   . ILE A 1 36  ? 13.786  -10.085 -4.508  1.00 24.30 ? 36  ILE A C   1 
ATOM   272  O  O   . ILE A 1 36  ? 14.703  -9.291  -4.730  1.00 24.70 ? 36  ILE A O   1 
ATOM   273  C  CB  . ILE A 1 36  ? 12.217  -8.248  -3.729  1.00 27.25 ? 36  ILE A CB  1 
ATOM   274  C  CG1 . ILE A 1 36  ? 12.492  -8.430  -2.218  1.00 26.26 ? 36  ILE A CG1 1 
ATOM   275  C  CG2 . ILE A 1 36  ? 10.861  -7.597  -3.977  1.00 27.60 ? 36  ILE A CG2 1 
ATOM   276  C  CD1 . ILE A 1 36  ? 12.810  -7.166  -1.480  1.00 29.26 ? 36  ILE A CD1 1 
ATOM   277  N  N   . LEU A 1 37  ? 13.980  -11.359 -4.216  1.00 22.67 ? 37  LEU A N   1 
ATOM   278  C  CA  . LEU A 1 37  ? 15.341  -11.933 -4.163  1.00 23.17 ? 37  LEU A CA  1 
ATOM   279  C  C   . LEU A 1 37  ? 15.822  -12.451 -5.517  1.00 24.11 ? 37  LEU A C   1 
ATOM   280  O  O   . LEU A 1 37  ? 15.090  -13.129 -6.241  1.00 26.61 ? 37  LEU A O   1 
ATOM   281  C  CB  . LEU A 1 37  ? 15.387  -13.027 -3.120  1.00 20.98 ? 37  LEU A CB  1 
ATOM   282  C  CG  . LEU A 1 37  ? 15.107  -12.686 -1.673  1.00 20.06 ? 37  LEU A CG  1 
ATOM   283  C  CD1 . LEU A 1 37  ? 15.465  -13.983 -0.951  1.00 24.06 ? 37  LEU A CD1 1 
ATOM   284  C  CD2 . LEU A 1 37  ? 15.949  -11.514 -1.159  1.00 17.64 ? 37  LEU A CD2 1 
ATOM   285  N  N   . GLN A 1 38  ? 17.064  -12.139 -5.882  1.00 21.65 ? 38  GLN A N   1 
ATOM   286  C  CA  . GLN A 1 38  ? 17.587  -12.711 -7.141  1.00 24.53 ? 38  GLN A CA  1 
ATOM   287  C  C   . GLN A 1 38  ? 19.018  -13.173 -6.984  1.00 23.14 ? 38  GLN A C   1 
ATOM   288  O  O   . GLN A 1 38  ? 19.878  -12.384 -6.567  1.00 17.32 ? 38  GLN A O   1 
ATOM   289  C  CB  . GLN A 1 38  ? 17.515  -11.693 -8.291  1.00 26.23 ? 38  GLN A CB  1 
ATOM   290  C  CG  . GLN A 1 38  ? 18.008  -12.247 -9.611  1.00 31.65 ? 38  GLN A CG  1 
ATOM   291  C  CD  . GLN A 1 38  ? 17.749  -11.316 -10.767 1.00 36.71 ? 38  GLN A CD  1 
ATOM   292  O  OE1 . GLN A 1 38  ? 16.631  -11.277 -11.290 1.00 38.48 ? 38  GLN A OE1 1 
ATOM   293  N  NE2 . GLN A 1 38  ? 18.786  -10.582 -11.197 1.00 35.48 ? 38  GLN A NE2 1 
ATOM   294  N  N   . TYR A 1 39  ? 19.284  -14.440 -7.312  1.00 20.69 ? 39  TYR A N   1 
ATOM   295  C  CA  . TYR A 1 39  ? 20.643  -14.953 -7.229  1.00 21.88 ? 39  TYR A CA  1 
ATOM   296  C  C   . TYR A 1 39  ? 21.565  -14.173 -8.181  1.00 22.26 ? 39  TYR A C   1 
ATOM   297  O  O   . TYR A 1 39  ? 21.181  -13.925 -9.312  1.00 21.13 ? 39  TYR A O   1 
ATOM   298  C  CB  . TYR A 1 39  ? 20.682  -16.459 -7.583  1.00 23.47 ? 39  TYR A CB  1 
ATOM   299  C  CG  . TYR A 1 39  ? 22.049  -17.028 -7.671  1.00 23.70 ? 39  TYR A CG  1 
ATOM   300  C  CD1 . TYR A 1 39  ? 22.871  -17.126 -6.528  1.00 21.74 ? 39  TYR A CD1 1 
ATOM   301  C  CD2 . TYR A 1 39  ? 22.557  -17.476 -8.904  1.00 22.17 ? 39  TYR A CD2 1 
ATOM   302  C  CE1 . TYR A 1 39  ? 24.134  -17.660 -6.612  1.00 23.72 ? 39  TYR A CE1 1 
ATOM   303  C  CE2 . TYR A 1 39  ? 23.825  -18.008 -8.995  1.00 26.50 ? 39  TYR A CE2 1 
ATOM   304  C  CZ  . TYR A 1 39  ? 24.612  -18.098 -7.864  1.00 25.25 ? 39  TYR A CZ  1 
ATOM   305  O  OH  . TYR A 1 39  ? 25.894  -18.636 -7.975  1.00 33.27 ? 39  TYR A OH  1 
ATOM   306  N  N   . ASP A 1 40  ? 22.779  -13.858 -7.749  1.00 22.22 ? 40  ASP A N   1 
ATOM   307  C  CA  . ASP A 1 40  ? 23.726  -13.145 -8.581  1.00 23.77 ? 40  ASP A CA  1 
ATOM   308  C  C   . ASP A 1 40  ? 25.038  -13.883 -8.356  1.00 24.32 ? 40  ASP A C   1 
ATOM   309  O  O   . ASP A 1 40  ? 25.622  -13.826 -7.281  1.00 21.25 ? 40  ASP A O   1 
ATOM   310  C  CB  . ASP A 1 40  ? 23.728  -11.641 -8.248  1.00 26.78 ? 40  ASP A CB  1 
ATOM   311  C  CG  . ASP A 1 40  ? 24.655  -10.815 -9.169  1.00 31.16 ? 40  ASP A CG  1 
ATOM   312  O  OD1 . ASP A 1 40  ? 25.582  -11.390 -9.739  1.00 29.26 ? 40  ASP A OD1 1 
ATOM   313  O  OD2 . ASP A 1 40  ? 24.459  -9.571  -9.320  1.00 33.26 ? 40  ASP A OD2 1 
ATOM   314  N  N   . ALA A 1 41  ? 25.477  -14.667 -9.365  1.00 23.89 ? 41  ALA A N   1 
ATOM   315  C  CA  . ALA A 1 41  ? 26.760  -15.380 -9.260  1.00 28.54 ? 41  ALA A CA  1 
ATOM   316  C  C   . ALA A 1 41  ? 27.947  -14.426 -9.102  1.00 24.20 ? 41  ALA A C   1 
ATOM   317  O  O   . ALA A 1 41  ? 29.039  -14.862 -8.749  1.00 28.70 ? 41  ALA A O   1 
ATOM   318  C  CB  . ALA A 1 41  ? 26.976  -16.287 -10.479 1.00 29.79 ? 41  ALA A CB  1 
ATOM   319  N  N   . SER A 1 42  ? 27.761  -13.141 -9.345  1.00 25.59 ? 42  SER A N   1 
ATOM   320  C  CA  . SER A 1 42  ? 28.883  -12.201 -9.220  1.00 24.32 ? 42  SER A CA  1 
ATOM   321  C  C   . SER A 1 42  ? 29.268  -11.925 -7.777  1.00 28.74 ? 42  SER A C   1 
ATOM   322  O  O   . SER A 1 42  ? 30.371  -11.514 -7.497  1.00 29.42 ? 42  SER A O   1 
ATOM   323  C  CB  . SER A 1 42  ? 28.571  -10.916 -9.982  1.00 28.88 ? 42  SER A CB  1 
ATOM   324  O  OG  . SER A 1 42  ? 27.892  -9.981  -9.193  1.00 30.21 ? 42  SER A OG  1 
ATOM   325  N  N   . LEU A 1 43  ? 28.378  -12.259 -6.849  1.00 19.88 ? 43  LEU A N   1 
ATOM   326  C  CA  . LEU A 1 43  ? 28.571  -11.945 -5.428  1.00 21.97 ? 43  LEU A CA  1 
ATOM   327  C  C   . LEU A 1 43  ? 29.463  -12.992 -4.734  1.00 21.21 ? 43  LEU A C   1 
ATOM   328  O  O   . LEU A 1 43  ? 28.948  -13.953 -4.133  1.00 27.21 ? 43  LEU A O   1 
ATOM   329  C  CB  . LEU A 1 43  ? 27.186  -11.938 -4.739  1.00 18.58 ? 43  LEU A CB  1 
ATOM   330  C  CG  . LEU A 1 43  ? 26.307  -10.801 -5.269  1.00 18.37 ? 43  LEU A CG  1 
ATOM   331  C  CD1 . LEU A 1 43  ? 24.918  -10.783 -4.560  1.00 15.68 ? 43  LEU A CD1 1 
ATOM   332  C  CD2 . LEU A 1 43  ? 26.992  -9.445  -5.082  1.00 17.27 ? 43  LEU A CD2 1 
ATOM   333  N  N   . THR A 1 44  ? 30.787  -12.808 -4.790  1.00 21.71 ? 44  THR A N   1 
ATOM   334  C  CA  . THR A 1 44  ? 31.720  -13.739 -4.233  1.00 21.59 ? 44  THR A CA  1 
ATOM   335  C  C   . THR A 1 44  ? 32.023  -13.384 -2.755  1.00 23.13 ? 44  THR A C   1 
ATOM   336  O  O   . THR A 1 44  ? 31.561  -12.331 -2.279  1.00 18.47 ? 44  THR A O   1 
ATOM   337  C  CB  . THR A 1 44  ? 33.044  -13.630 -5.009  1.00 25.27 ? 44  THR A CB  1 
ATOM   338  O  OG1 . THR A 1 44  ? 33.351  -12.234 -5.130  1.00 26.79 ? 44  THR A OG1 1 
ATOM   339  C  CG2 . THR A 1 44  ? 32.883  -14.200 -6.362  1.00 31.34 ? 44  THR A CG2 1 
ATOM   340  N  N   . PRO A 1 45  ? 32.717  -14.275 -2.013  1.00 23.19 ? 45  PRO A N   1 
ATOM   341  C  CA  . PRO A 1 45  ? 32.962  -13.995 -0.595  1.00 19.82 ? 45  PRO A CA  1 
ATOM   342  C  C   . PRO A 1 45  ? 33.820  -12.791 -0.284  1.00 19.98 ? 45  PRO A C   1 
ATOM   343  O  O   . PRO A 1 45  ? 34.864  -12.612 -0.902  1.00 22.30 ? 45  PRO A O   1 
ATOM   344  C  CB  . PRO A 1 45  ? 33.707  -15.266 -0.122  1.00 22.30 ? 45  PRO A CB  1 
ATOM   345  C  CG  . PRO A 1 45  ? 33.201  -16.338 -1.048  1.00 23.64 ? 45  PRO A CG  1 
ATOM   346  C  CD  . PRO A 1 45  ? 33.196  -15.644 -2.374  1.00 22.88 ? 45  PRO A CD  1 
ATOM   347  N  N   . LEU A 1 46  ? 33.434  -12.018 0.728   1.00 17.28 ? 46  LEU A N   1 
ATOM   348  C  CA  . LEU A 1 46  ? 34.224  -10.878 1.222   1.00 17.42 ? 46  LEU A CA  1 
ATOM   349  C  C   . LEU A 1 46  ? 35.341  -11.468 2.053   1.00 19.98 ? 46  LEU A C   1 
ATOM   350  O  O   . LEU A 1 46  ? 35.191  -12.576 2.568   1.00 19.88 ? 46  LEU A O   1 
ATOM   351  C  CB  . LEU A 1 46  ? 33.370  -9.981  2.100   1.00 16.65 ? 46  LEU A CB  1 
ATOM   352  C  CG  . LEU A 1 46  ? 32.209  -9.382  1.319   1.00 17.79 ? 46  LEU A CG  1 
ATOM   353  C  CD1 . LEU A 1 46  ? 31.430  -8.609  2.360   1.00 19.76 ? 46  LEU A CD1 1 
ATOM   354  C  CD2 . LEU A 1 46  ? 32.751  -8.383  0.255   1.00 21.91 ? 46  LEU A CD2 1 
ATOM   355  N  N   . GLU A 1 47  ? 36.450  -10.748 2.120   1.00 17.27 ? 47  GLU A N   1 
ATOM   356  C  CA  . GLU A 1 47  ? 37.534  -11.079 2.978   1.00 18.48 ? 47  GLU A CA  1 
ATOM   357  C  C   . GLU A 1 47  ? 37.631  -10.032 4.027   1.00 15.02 ? 47  GLU A C   1 
ATOM   358  O  O   . GLU A 1 47  ? 37.600  -8.808  3.733   1.00 17.66 ? 47  GLU A O   1 
ATOM   359  C  CB  . GLU A 1 47  ? 38.846  -11.251 2.206   1.00 24.41 ? 47  GLU A CB  1 
ATOM   360  C  CG  . GLU A 1 47  ? 38.623  -12.310 1.107   1.00 32.98 ? 47  GLU A CG  1 
ATOM   361  C  CD  . GLU A 1 47  ? 39.801  -12.576 0.182   1.00 43.18 ? 47  GLU A CD  1 
ATOM   362  O  OE1 . GLU A 1 47  ? 39.543  -13.038 -0.968  1.00 45.45 ? 47  GLU A OE1 1 
ATOM   363  O  OE2 . GLU A 1 47  ? 40.963  -12.350 0.596   1.00 47.08 ? 47  GLU A OE2 1 
ATOM   364  N  N   . PHE A 1 48  ? 37.713  -10.459 5.284   1.00 15.97 ? 48  PHE A N   1 
ATOM   365  C  CA  . PHE A 1 48  ? 37.798  -9.533  6.415   1.00 16.47 ? 48  PHE A CA  1 
ATOM   366  C  C   . PHE A 1 48  ? 39.241  -9.439  6.890   1.00 18.66 ? 48  PHE A C   1 
ATOM   367  O  O   . PHE A 1 48  ? 39.790  -10.400 7.425   1.00 19.86 ? 48  PHE A O   1 
ATOM   368  C  CB  . PHE A 1 48  ? 36.835  -10.009 7.515   1.00 17.61 ? 48  PHE A CB  1 
ATOM   369  C  CG  . PHE A 1 48  ? 35.486  -10.401 6.949   1.00 15.55 ? 48  PHE A CG  1 
ATOM   370  C  CD1 . PHE A 1 48  ? 34.574  -9.444  6.514   1.00 16.10 ? 48  PHE A CD1 1 
ATOM   371  C  CD2 . PHE A 1 48  ? 35.142  -11.797 6.792   1.00 17.24 ? 48  PHE A CD2 1 
ATOM   372  C  CE1 . PHE A 1 48  ? 33.363  -9.829  5.959   1.00 16.74 ? 48  PHE A CE1 1 
ATOM   373  C  CE2 . PHE A 1 48  ? 33.958  -12.160 6.173   1.00 16.41 ? 48  PHE A CE2 1 
ATOM   374  C  CZ  . PHE A 1 48  ? 33.034  -11.167 5.790   1.00 16.41 ? 48  PHE A CZ  1 
ATOM   375  N  N   . GLN A 1 49  ? 39.834  -8.289  6.648   1.00 17.47 ? 49  GLN A N   1 
ATOM   376  C  CA  . GLN A 1 49  ? 41.277  -8.066  6.840   1.00 16.76 ? 49  GLN A CA  1 
ATOM   377  C  C   . GLN A 1 49  ? 41.463  -7.110  7.983   1.00 15.26 ? 49  GLN A C   1 
ATOM   378  O  O   . GLN A 1 49  ? 40.772  -6.080  8.111   1.00 14.41 ? 49  GLN A O   1 
ATOM   379  C  CB  . GLN A 1 49  ? 41.882  -7.413  5.586   1.00 17.85 ? 49  GLN A CB  1 
ATOM   380  C  CG  . GLN A 1 49  ? 41.617  -8.242  4.352   1.00 22.84 ? 49  GLN A CG  1 
ATOM   381  C  CD  . GLN A 1 49  ? 42.692  -8.174  3.305   1.00 31.78 ? 49  GLN A CD  1 
ATOM   382  O  OE1 . GLN A 1 49  ? 43.176  -7.078  2.948   1.00 37.71 ? 49  GLN A OE1 1 
ATOM   383  N  NE2 . GLN A 1 49  ? 43.079  -9.356  2.782   1.00 31.35 ? 49  GLN A NE2 1 
ATOM   384  N  N   . GLY A 1 50  ? 42.424  -7.400  8.873   1.00 16.27 ? 50  GLY A N   1 
ATOM   385  C  CA  . GLY A 1 50  ? 42.630  -6.536  9.989   1.00 15.44 ? 50  GLY A CA  1 
ATOM   386  C  C   . GLY A 1 50  ? 41.523  -6.560  11.092  1.00 14.97 ? 50  GLY A C   1 
ATOM   387  O  O   . GLY A 1 50  ? 41.486  -5.716  11.916  1.00 16.60 ? 50  GLY A O   1 
ATOM   388  N  N   . TYR A 1 51  ? 40.659  -7.565  11.027  1.00 16.51 ? 51  TYR A N   1 
ATOM   389  C  CA  . TYR A 1 51  ? 39.567  -7.779  12.014  1.00 15.25 ? 51  TYR A CA  1 
ATOM   390  C  C   . TYR A 1 51  ? 40.055  -8.312  13.360  1.00 15.03 ? 51  TYR A C   1 
ATOM   391  O  O   . TYR A 1 51  ? 39.419  -8.146  14.422  1.00 15.10 ? 51  TYR A O   1 
ATOM   392  C  CB  . TYR A 1 51  ? 38.465  -8.684  11.401  1.00 14.82 ? 51  TYR A CB  1 
ATOM   393  C  CG  . TYR A 1 51  ? 37.446  -7.971  10.606  1.00 14.64 ? 51  TYR A CG  1 
ATOM   394  C  CD1 . TYR A 1 51  ? 36.083  -8.243  10.830  1.00 13.72 ? 51  TYR A CD1 1 
ATOM   395  C  CD2 . TYR A 1 51  ? 37.773  -7.143  9.562   1.00 13.96 ? 51  TYR A CD2 1 
ATOM   396  C  CE1 . TYR A 1 51  ? 35.092  -7.577  10.105  1.00 13.59 ? 51  TYR A CE1 1 
ATOM   397  C  CE2 . TYR A 1 51  ? 36.788  -6.460  8.807   1.00 15.69 ? 51  TYR A CE2 1 
ATOM   398  C  CZ  . TYR A 1 51  ? 35.433  -6.712  9.089   1.00 14.18 ? 51  TYR A CZ  1 
ATOM   399  O  OH  . TYR A 1 51  ? 34.426  -6.058  8.389   1.00 15.56 ? 51  TYR A OH  1 
ATOM   400  N  N   . ASN A 1 52  ? 41.244  -8.951  13.331  1.00 16.81 ? 52  ASN A N   1 
ATOM   401  C  CA  . ASN A 1 52  ? 41.811  -9.469  14.579  1.00 20.08 ? 52  ASN A CA  1 
ATOM   402  C  C   . ASN A 1 52  ? 42.563  -8.375  15.327  1.00 21.29 ? 52  ASN A C   1 
ATOM   403  O  O   . ASN A 1 52  ? 43.776  -8.200  15.200  1.00 23.09 ? 52  ASN A O   1 
ATOM   404  C  CB  . ASN A 1 52  ? 42.663  -10.717 14.296  1.00 20.91 ? 52  ASN A CB  1 
ATOM   405  C  CG  . ASN A 1 52  ? 42.909  -11.572 15.523  1.00 21.26 ? 52  ASN A CG  1 
ATOM   406  O  OD1 . ASN A 1 52  ? 42.475  -11.294 16.612  1.00 21.01 ? 52  ASN A OD1 1 
ATOM   407  N  ND2 . ASN A 1 52  ? 43.638  -12.684 15.310  1.00 29.00 ? 52  ASN A ND2 1 
ATOM   408  N  N   . LEU A 1 53  ? 41.837  -7.570  16.071  1.00 17.24 ? 53  LEU A N   1 
ATOM   409  C  CA  . LEU A 1 53  ? 42.384  -6.346  16.684  1.00 17.87 ? 53  LEU A CA  1 
ATOM   410  C  C   . LEU A 1 53  ? 43.357  -6.695  17.776  1.00 20.76 ? 53  LEU A C   1 
ATOM   411  O  O   . LEU A 1 53  ? 43.088  -7.543  18.649  1.00 21.17 ? 53  LEU A O   1 
ATOM   412  C  CB  . LEU A 1 53  ? 41.280  -5.452  17.253  1.00 17.11 ? 53  LEU A CB  1 
ATOM   413  C  CG  . LEU A 1 53  ? 40.209  -5.121  16.208  1.00 16.05 ? 53  LEU A CG  1 
ATOM   414  C  CD1 . LEU A 1 53  ? 39.132  -4.336  16.930  1.00 15.19 ? 53  LEU A CD1 1 
ATOM   415  C  CD2 . LEU A 1 53  ? 40.791  -4.291  15.077  1.00 17.09 ? 53  LEU A CD2 1 
ATOM   416  N  N   . SER A 1 54  ? 44.488  -6.007  17.711  1.00 22.60 ? 54  SER A N   1 
ATOM   417  C  CA  . SER A 1 54  ? 45.505  -6.136  18.742  1.00 25.10 ? 54  SER A CA  1 
ATOM   418  C  C   . SER A 1 54  ? 44.894  -6.161  20.148  1.00 24.92 ? 54  SER A C   1 
ATOM   419  O  O   . SER A 1 54  ? 44.279  -5.154  20.574  1.00 23.14 ? 54  SER A O   1 
ATOM   420  C  CB  . SER A 1 54  ? 46.481  -4.955  18.626  1.00 24.29 ? 54  SER A CB  1 
ATOM   421  O  OG  . SER A 1 54  ? 47.550  -5.106  19.550  1.00 26.15 ? 54  SER A OG  1 
ATOM   422  N  N   . ALA A 1 55  ? 45.095  -7.255  20.892  1.00 22.93 ? 55  ALA A N   1 
ATOM   423  C  CA  . ALA A 1 55  ? 44.705  -7.227  22.302  1.00 22.24 ? 55  ALA A CA  1 
ATOM   424  C  C   . ALA A 1 55  ? 45.546  -6.258  23.154  1.00 22.86 ? 55  ALA A C   1 
ATOM   425  O  O   . ALA A 1 55  ? 45.214  -5.953  24.307  1.00 25.57 ? 55  ALA A O   1 
ATOM   426  C  CB  . ALA A 1 55  ? 44.685  -8.628  22.931  1.00 26.99 ? 55  ALA A CB  1 
ATOM   427  N  N   . ASN A 1 56  ? 46.609  -5.708  22.561  1.00 24.82 ? 56  ASN A N   1 
ATOM   428  C  CA  . ASN A 1 56  ? 47.366  -4.611  23.241  1.00 25.02 ? 56  ASN A CA  1 
ATOM   429  C  C   . ASN A 1 56  ? 46.915  -3.172  22.890  1.00 25.35 ? 56  ASN A C   1 
ATOM   430  O  O   . ASN A 1 56  ? 47.490  -2.192  23.344  1.00 26.72 ? 56  ASN A O   1 
ATOM   431  C  CB  . ASN A 1 56  ? 48.848  -4.766  22.913  1.00 27.07 ? 56  ASN A CB  1 
ATOM   432  C  CG  . ASN A 1 56  ? 49.381  -6.148  23.261  1.00 30.76 ? 56  ASN A CG  1 
ATOM   433  O  OD1 . ASN A 1 56  ? 49.163  -6.667  24.386  1.00 33.14 ? 56  ASN A OD1 1 
ATOM   434  N  ND2 . ASN A 1 56  ? 50.053  -6.776  22.289  1.00 29.62 ? 56  ASN A ND2 1 
ATOM   435  N  N   . LYS A 1 57  ? 45.837  -3.047  22.104  1.00 24.76 ? 57  LYS A N   1 
ATOM   436  C  CA  . LYS A 1 57  ? 45.252  -1.763  21.784  1.00 20.17 ? 57  LYS A CA  1 
ATOM   437  C  C   . LYS A 1 57  ? 43.894  -1.657  22.455  1.00 20.30 ? 57  LYS A C   1 
ATOM   438  O  O   . LYS A 1 57  ? 43.253  -2.706  22.662  1.00 21.68 ? 57  LYS A O   1 
ATOM   439  C  CB  . LYS A 1 57  ? 45.059  -1.674  20.260  1.00 22.58 ? 57  LYS A CB  1 
ATOM   440  C  CG  . LYS A 1 57  ? 45.323  -0.281  19.733  1.00 27.76 ? 57  LYS A CG  1 
ATOM   441  C  CD  . LYS A 1 57  ? 45.517  -0.304  18.200  1.00 28.26 ? 57  LYS A CD  1 
ATOM   442  C  CE  . LYS A 1 57  ? 44.794  0.841   17.475  1.00 31.32 ? 57  LYS A CE  1 
ATOM   443  N  NZ  . LYS A 1 57  ? 45.358  1.091   16.090  1.00 33.85 ? 57  LYS A NZ  1 
ATOM   444  N  N   . GLN A 1 58  ? 43.447  -0.430  22.761  1.00 20.23 ? 58  GLN A N   1 
ATOM   445  C  CA  . GLN A 1 58  ? 42.083  -0.221  23.292  1.00 20.80 ? 58  GLN A CA  1 
ATOM   446  C  C   . GLN A 1 58  ? 41.212  0.558   22.337  1.00 20.50 ? 58  GLN A C   1 
ATOM   447  O  O   . GLN A 1 58  ? 41.692  1.388   21.600  1.00 22.15 ? 58  GLN A O   1 
ATOM   448  C  CB  . GLN A 1 58  ? 42.119  0.454   24.638  1.00 21.00 ? 58  GLN A CB  1 
ATOM   449  C  CG  . GLN A 1 58  ? 42.689  -0.543  25.586  1.00 21.79 ? 58  GLN A CG  1 
ATOM   450  C  CD  . GLN A 1 58  ? 43.017  0.032   26.934  1.00 24.55 ? 58  GLN A CD  1 
ATOM   451  O  OE1 . GLN A 1 58  ? 43.508  -0.692  27.770  1.00 29.72 ? 58  GLN A OE1 1 
ATOM   452  N  NE2 . GLN A 1 58  ? 42.813  1.332   27.131  1.00 26.79 ? 58  GLN A NE2 1 
ATOM   453  N  N   . PHE A 1 59  ? 39.899  0.199   22.272  1.00 21.45 ? 59  PHE A N   1 
ATOM   454  C  CA  . PHE A 1 59  ? 38.993  0.859   21.336  1.00 19.71 ? 59  PHE A CA  1 
ATOM   455  C  C   . PHE A 1 59  ? 37.856  1.479   22.102  1.00 17.51 ? 59  PHE A C   1 
ATOM   456  O  O   . PHE A 1 59  ? 37.319  0.857   23.005  1.00 18.81 ? 59  PHE A O   1 
ATOM   457  C  CB  . PHE A 1 59  ? 38.508  -0.187  20.326  1.00 18.68 ? 59  PHE A CB  1 
ATOM   458  C  CG  . PHE A 1 59  ? 39.667  -0.816  19.559  1.00 19.09 ? 59  PHE A CG  1 
ATOM   459  C  CD1 . PHE A 1 59  ? 40.107  -0.236  18.368  1.00 20.47 ? 59  PHE A CD1 1 
ATOM   460  C  CD2 . PHE A 1 59  ? 40.391  -1.914  20.086  1.00 19.11 ? 59  PHE A CD2 1 
ATOM   461  C  CE1 . PHE A 1 59  ? 41.214  -0.746  17.700  1.00 19.40 ? 59  PHE A CE1 1 
ATOM   462  C  CE2 . PHE A 1 59  ? 41.533  -2.419  19.420  1.00 17.69 ? 59  PHE A CE2 1 
ATOM   463  C  CZ  . PHE A 1 59  ? 41.913  -1.836  18.208  1.00 18.72 ? 59  PHE A CZ  1 
ATOM   464  N  N   . LEU A 1 60  ? 37.542  2.730   21.775  1.00 18.42 ? 60  LEU A N   1 
ATOM   465  C  CA  . LEU A 1 60  ? 36.570  3.526   22.506  1.00 17.62 ? 60  LEU A CA  1 
ATOM   466  C  C   . LEU A 1 60  ? 35.108  3.084   22.285  1.00 19.22 ? 60  LEU A C   1 
ATOM   467  O  O   . LEU A 1 60  ? 34.648  3.049   21.153  1.00 17.84 ? 60  LEU A O   1 
ATOM   468  C  CB  . LEU A 1 60  ? 36.721  4.981   22.091  1.00 20.46 ? 60  LEU A CB  1 
ATOM   469  C  CG  . LEU A 1 60  ? 36.004  5.975   22.952  1.00 22.27 ? 60  LEU A CG  1 
ATOM   470  C  CD1 . LEU A 1 60  ? 36.472  5.946   24.424  1.00 24.29 ? 60  LEU A CD1 1 
ATOM   471  C  CD2 . LEU A 1 60  ? 36.021  7.366   22.323  1.00 23.74 ? 60  LEU A CD2 1 
ATOM   472  N  N   . LEU A 1 61  ? 34.406  2.789   23.356  1.00 16.14 ? 61  LEU A N   1 
ATOM   473  C  CA  . LEU A 1 61  ? 32.986  2.456   23.319  1.00 17.20 ? 61  LEU A CA  1 
ATOM   474  C  C   . LEU A 1 61  ? 32.282  3.718   23.834  1.00 17.40 ? 61  LEU A C   1 
ATOM   475  O  O   . LEU A 1 61  ? 32.656  4.208   24.867  1.00 17.05 ? 61  LEU A O   1 
ATOM   476  C  CB  . LEU A 1 61  ? 32.683  1.280   24.257  1.00 16.79 ? 61  LEU A CB  1 
ATOM   477  C  CG  . LEU A 1 61  ? 31.250  0.723   24.289  1.00 17.21 ? 61  LEU A CG  1 
ATOM   478  C  CD1 . LEU A 1 61  ? 31.060  -0.019  22.966  1.00 18.78 ? 61  LEU A CD1 1 
ATOM   479  C  CD2 . LEU A 1 61  ? 31.056  -0.245  25.437  1.00 18.88 ? 61  LEU A CD2 1 
ATOM   480  N  N   . THR A 1 62  ? 31.291  4.240   23.105  1.00 15.74 ? 62  THR A N   1 
ATOM   481  C  CA  . THR A 1 62  ? 30.549  5.412   23.565  1.00 19.01 ? 62  THR A CA  1 
ATOM   482  C  C   . THR A 1 62  ? 29.035  5.198   23.473  1.00 21.14 ? 62  THR A C   1 
ATOM   483  O  O   . THR A 1 62  ? 28.526  4.504   22.555  1.00 22.24 ? 62  THR A O   1 
ATOM   484  C  CB  . THR A 1 62  ? 30.933  6.711   22.825  1.00 21.62 ? 62  THR A CB  1 
ATOM   485  O  OG1 . THR A 1 62  ? 30.489  6.656   21.453  1.00 27.09 ? 62  THR A OG1 1 
ATOM   486  C  CG2 . THR A 1 62  ? 32.361  6.910   22.763  1.00 21.83 ? 62  THR A CG2 1 
ATOM   487  N  N   . ASN A 1 63  ? 28.312  5.814   24.403  1.00 20.29 ? 63  ASN A N   1 
ATOM   488  C  CA  . ASN A 1 63  ? 26.860  5.952   24.288  1.00 18.48 ? 63  ASN A CA  1 
ATOM   489  C  C   . ASN A 1 63  ? 26.570  7.369   23.791  1.00 19.33 ? 63  ASN A C   1 
ATOM   490  O  O   . ASN A 1 63  ? 26.873  8.363   24.429  1.00 23.60 ? 63  ASN A O   1 
ATOM   491  C  CB  . ASN A 1 63  ? 26.284  5.775   25.640  1.00 17.82 ? 63  ASN A CB  1 
ATOM   492  C  CG  . ASN A 1 63  ? 24.778  5.959   25.688  1.00 17.92 ? 63  ASN A CG  1 
ATOM   493  O  OD1 . ASN A 1 63  ? 24.174  6.721   24.863  1.00 18.05 ? 63  ASN A OD1 1 
ATOM   494  N  ND2 . ASN A 1 63  ? 24.156  5.318   26.719  1.00 17.87 ? 63  ASN A ND2 1 
ATOM   495  N  N   . ASN A 1 64  ? 26.008  7.488   22.567  1.00 23.65 ? 64  ASN A N   1 
ATOM   496  C  CA  . ASN A 1 64  ? 25.817  8.809   21.992  1.00 25.71 ? 64  ASN A CA  1 
ATOM   497  C  C   . ASN A 1 64  ? 24.392  9.359   22.130  1.00 23.59 ? 64  ASN A C   1 
ATOM   498  O  O   . ASN A 1 64  ? 24.079  10.432  21.619  1.00 28.37 ? 64  ASN A O   1 
ATOM   499  C  CB  . ASN A 1 64  ? 26.238  8.834   20.505  1.00 27.59 ? 64  ASN A CB  1 
ATOM   500  C  CG  . ASN A 1 64  ? 25.497  7.800   19.657  1.00 28.62 ? 64  ASN A CG  1 
ATOM   501  O  OD1 . ASN A 1 64  ? 24.434  7.265   20.020  1.00 25.24 ? 64  ASN A OD1 1 
ATOM   502  N  ND2 . ASN A 1 64  ? 26.095  7.488   18.484  1.00 27.03 ? 64  ASN A ND2 1 
ATOM   503  N  N   . GLY A 1 65  ? 23.591  8.666   22.931  1.00 22.49 ? 65  GLY A N   1 
ATOM   504  C  CA  . GLY A 1 65  ? 22.184  8.945   23.076  1.00 23.52 ? 65  GLY A CA  1 
ATOM   505  C  C   . GLY A 1 65  ? 21.248  8.249   22.105  1.00 24.04 ? 65  GLY A C   1 
ATOM   506  O  O   . GLY A 1 65  ? 20.038  8.334   22.290  1.00 21.19 ? 65  GLY A O   1 
ATOM   507  N  N   . HIS A 1 66  ? 21.798  7.574   21.072  1.00 23.45 ? 66  HIS A N   1 
ATOM   508  C  CA  . HIS A 1 66  ? 21.054  6.831   20.022  1.00 20.29 ? 66  HIS A CA  1 
ATOM   509  C  C   . HIS A 1 66  ? 21.346  5.335   19.919  1.00 20.51 ? 66  HIS A C   1 
ATOM   510  O  O   . HIS A 1 66  ? 20.434  4.503   19.681  1.00 22.27 ? 66  HIS A O   1 
ATOM   511  C  CB  . HIS A 1 66  ? 21.204  7.516   18.643  1.00 23.08 ? 66  HIS A CB  1 
ATOM   512  C  CG  . HIS A 1 66  ? 20.947  9.017   18.638  1.00 22.06 ? 66  HIS A CG  1 
ATOM   513  N  ND1 . HIS A 1 66  ? 19.696  9.570   18.725  1.00 21.96 ? 66  HIS A ND1 1 
ATOM   514  C  CD2 . HIS A 1 66  ? 21.808  10.067  18.515  1.00 24.44 ? 66  HIS A CD2 1 
ATOM   515  C  CE1 . HIS A 1 66  ? 19.800  10.892  18.691  1.00 23.81 ? 66  HIS A CE1 1 
ATOM   516  N  NE2 . HIS A 1 66  ? 21.100  11.199  18.589  1.00 24.57 ? 66  HIS A NE2 1 
ATOM   517  N  N   A SER A 1 67  ? 22.621  4.983   20.100  0.50 22.07 ? 67  SER A N   1 
ATOM   518  N  N   B SER A 1 67  ? 22.608  4.931   20.105  0.50 21.44 ? 67  SER A N   1 
ATOM   519  C  CA  A SER A 1 67  ? 23.047  3.592   20.138  0.50 21.06 ? 67  SER A CA  1 
ATOM   520  C  CA  B SER A 1 67  ? 22.967  3.506   20.237  0.50 20.41 ? 67  SER A CA  1 
ATOM   521  C  C   A SER A 1 67  ? 24.372  3.564   20.887  0.50 21.18 ? 67  SER A C   1 
ATOM   522  C  C   B SER A 1 67  ? 24.243  3.489   21.073  0.50 20.04 ? 67  SER A C   1 
ATOM   523  O  O   A SER A 1 67  ? 24.857  4.617   21.285  0.50 22.45 ? 67  SER A O   1 
ATOM   524  O  O   B SER A 1 67  ? 24.573  4.449   21.707  0.50 18.17 ? 67  SER A O   1 
ATOM   525  C  CB  A SER A 1 67  ? 23.166  2.946   18.736  0.50 22.02 ? 67  SER A CB  1 
ATOM   526  C  CB  B SER A 1 67  ? 23.149  2.750   18.879  0.50 21.56 ? 67  SER A CB  1 
ATOM   527  O  OG  A SER A 1 67  ? 24.380  3.264   18.065  0.50 19.36 ? 67  SER A OG  1 
ATOM   528  O  OG  B SER A 1 67  ? 23.518  1.349   19.014  0.50 19.90 ? 67  SER A OG  1 
ATOM   529  N  N   . VAL A 1 68  ? 24.900  2.359   21.087  1.00 20.09 ? 68  VAL A N   1 
ATOM   530  C  CA  . VAL A 1 68  ? 26.210  2.222   21.747  1.00 18.33 ? 68  VAL A CA  1 
ATOM   531  C  C   . VAL A 1 68  ? 27.130  1.880   20.554  1.00 16.92 ? 68  VAL A C   1 
ATOM   532  O  O   . VAL A 1 68  ? 26.805  1.002   19.776  1.00 19.08 ? 68  VAL A O   1 
ATOM   533  C  CB  . VAL A 1 68  ? 26.184  1.146   22.860  1.00 22.10 ? 68  VAL A CB  1 
ATOM   534  C  CG1 . VAL A 1 68  ? 25.778  -0.244  22.320  1.00 23.41 ? 68  VAL A CG1 1 
ATOM   535  C  CG2 . VAL A 1 68  ? 27.560  1.057   23.481  1.00 20.35 ? 68  VAL A CG2 1 
ATOM   536  N  N   . LYS A 1 69  ? 28.238  2.598   20.436  1.00 18.23 ? 69  LYS A N   1 
ATOM   537  C  CA  . LYS A 1 69  ? 29.124  2.362   19.306  1.00 16.46 ? 69  LYS A CA  1 
ATOM   538  C  C   . LYS A 1 69  ? 30.531  2.087   19.797  1.00 14.08 ? 69  LYS A C   1 
ATOM   539  O  O   . LYS A 1 69  ? 30.968  2.682   20.784  1.00 15.45 ? 69  LYS A O   1 
ATOM   540  C  CB  . LYS A 1 69  ? 29.104  3.489   18.300  1.00 19.85 ? 69  LYS A CB  1 
ATOM   541  C  CG  . LYS A 1 69  ? 29.632  4.810   18.760  1.00 21.72 ? 69  LYS A CG  1 
ATOM   542  C  CD  . LYS A 1 69  ? 29.860  5.675   17.539  1.00 25.51 ? 69  LYS A CD  1 
ATOM   543  C  CE  . LYS A 1 69  ? 30.298  7.081   17.957  1.00 32.73 ? 69  LYS A CE  1 
ATOM   544  N  NZ  . LYS A 1 69  ? 30.257  7.967   16.738  1.00 31.06 ? 69  LYS A NZ  1 
ATOM   545  N  N   . LEU A 1 70  ? 31.193  1.184   19.094  1.00 13.08 ? 70  LEU A N   1 
ATOM   546  C  CA  . LEU A 1 70  ? 32.632  0.933   19.334  1.00 13.30 ? 70  LEU A CA  1 
ATOM   547  C  C   . LEU A 1 70  ? 33.412  1.456   18.149  1.00 13.64 ? 70  LEU A C   1 
ATOM   548  O  O   . LEU A 1 70  ? 33.143  1.083   17.023  1.00 12.73 ? 70  LEU A O   1 
ATOM   549  C  CB  . LEU A 1 70  ? 32.776  -0.594  19.391  1.00 12.44 ? 70  LEU A CB  1 
ATOM   550  C  CG  . LEU A 1 70  ? 34.290  -1.019  19.586  1.00 14.42 ? 70  LEU A CG  1 
ATOM   551  C  CD1 . LEU A 1 70  ? 34.733  -0.605  20.932  1.00 13.48 ? 70  LEU A CD1 1 
ATOM   552  C  CD2 . LEU A 1 70  ? 34.374  -2.511  19.515  1.00 14.37 ? 70  LEU A CD2 1 
ATOM   553  N  N   A ASN A 1 71  ? 34.424  2.298   18.421  0.50 13.17 ? 71  ASN A N   1 
ATOM   554  N  N   B ASN A 1 71  ? 34.403  2.349   18.383  0.50 14.48 ? 71  ASN A N   1 
ATOM   555  C  CA  A ASN A 1 71  ? 35.283  2.785   17.352  0.50 13.28 ? 71  ASN A CA  1 
ATOM   556  C  CA  B ASN A 1 71  ? 35.216  2.861   17.257  0.50 15.33 ? 71  ASN A CA  1 
ATOM   557  C  C   A ASN A 1 71  ? 36.187  1.682   16.829  0.50 13.80 ? 71  ASN A C   1 
ATOM   558  C  C   B ASN A 1 71  ? 36.188  1.785   16.832  0.50 15.20 ? 71  ASN A C   1 
ATOM   559  O  O   A ASN A 1 71  ? 36.595  0.795   17.582  0.50 14.85 ? 71  ASN A O   1 
ATOM   560  O  O   B ASN A 1 71  ? 36.661  1.039   17.679  0.50 16.81 ? 71  ASN A O   1 
ATOM   561  C  CB  A ASN A 1 71  ? 36.116  3.945   17.860  0.50 12.98 ? 71  ASN A CB  1 
ATOM   562  C  CB  B ASN A 1 71  ? 35.998  4.110   17.640  0.50 17.25 ? 71  ASN A CB  1 
ATOM   563  C  CG  A ASN A 1 71  ? 35.329  5.220   17.937  0.50 13.49 ? 71  ASN A CG  1 
ATOM   564  C  CG  B ASN A 1 71  ? 36.113  5.120   16.492  0.50 20.55 ? 71  ASN A CG  1 
ATOM   565  O  OD1 A ASN A 1 71  ? 34.168  5.242   17.585  0.50 14.03 ? 71  ASN A OD1 1 
ATOM   566  O  OD1 B ASN A 1 71  ? 36.631  4.841   15.389  0.50 20.84 ? 71  ASN A OD1 1 
ATOM   567  N  ND2 A ASN A 1 71  ? 35.943  6.281   18.429  0.50 15.45 ? 71  ASN A ND2 1 
ATOM   568  N  ND2 B ASN A 1 71  ? 35.613  6.335   16.767  0.50 24.33 ? 71  ASN A ND2 1 
ATOM   569  N  N   . LEU A 1 72  ? 36.438  1.694   15.517  1.00 13.35 ? 72  LEU A N   1 
ATOM   570  C  CA  . LEU A 1 72  ? 37.254  0.629   14.926  1.00 13.60 ? 72  LEU A CA  1 
ATOM   571  C  C   . LEU A 1 72  ? 38.378  1.331   14.165  1.00 15.55 ? 72  LEU A C   1 
ATOM   572  O  O   . LEU A 1 72  ? 38.184  2.454   13.651  1.00 14.30 ? 72  LEU A O   1 
ATOM   573  C  CB  . LEU A 1 72  ? 36.380  -0.249  13.962  1.00 14.37 ? 72  LEU A CB  1 
ATOM   574  C  CG  . LEU A 1 72  ? 35.284  -1.051  14.673  1.00 13.24 ? 72  LEU A CG  1 
ATOM   575  C  CD1 . LEU A 1 72  ? 34.392  -1.617  13.551  1.00 11.82 ? 72  LEU A CD1 1 
ATOM   576  C  CD2 . LEU A 1 72  ? 35.882  -2.145  15.607  1.00 13.16 ? 72  LEU A CD2 1 
ATOM   577  N  N   . PRO A 1 73  ? 39.512  0.640   13.989  1.00 14.80 ? 73  PRO A N   1 
ATOM   578  C  CA  . PRO A 1 73  ? 40.623  1.298   13.277  1.00 18.13 ? 73  PRO A CA  1 
ATOM   579  C  C   . PRO A 1 73  ? 40.587  1.217   11.757  1.00 18.00 ? 73  PRO A C   1 
ATOM   580  O  O   . PRO A 1 73  ? 40.059  0.265   11.205  1.00 19.96 ? 73  PRO A O   1 
ATOM   581  C  CB  . PRO A 1 73  ? 41.843  0.583   13.833  1.00 17.49 ? 73  PRO A CB  1 
ATOM   582  C  CG  . PRO A 1 73  ? 41.369  -0.810  14.089  1.00 14.53 ? 73  PRO A CG  1 
ATOM   583  C  CD  . PRO A 1 73  ? 39.852  -0.740  14.396  1.00 16.09 ? 73  PRO A CD  1 
ATOM   584  N  N   . SER A 1 74  ? 41.191  2.227   11.112  1.00 22.23 ? 74  SER A N   1 
ATOM   585  C  CA  . SER A 1 74  ? 41.140  2.319   9.648   1.00 22.83 ? 74  SER A CA  1 
ATOM   586  C  C   . SER A 1 74  ? 41.981  1.229   8.961   1.00 20.02 ? 74  SER A C   1 
ATOM   587  O  O   . SER A 1 74  ? 41.830  1.049   7.772   1.00 22.61 ? 74  SER A O   1 
ATOM   588  C  CB  . SER A 1 74  ? 41.573  3.700   9.179   1.00 26.97 ? 74  SER A CB  1 
ATOM   589  O  OG  . SER A 1 74  ? 42.863  3.922   9.690   1.00 29.84 ? 74  SER A OG  1 
ATOM   590  N  N   . ASP A 1 75  ? 42.893  0.529   9.664   1.00 18.82 ? 75  ASP A N   1 
ATOM   591  C  CA  . ASP A 1 75  ? 43.485  -0.670  9.004   1.00 18.67 ? 75  ASP A CA  1 
ATOM   592  C  C   . ASP A 1 75  ? 42.630  -1.882  8.899   1.00 16.59 ? 75  ASP A C   1 
ATOM   593  O  O   . ASP A 1 75  ? 43.017  -2.847  8.216   1.00 17.14 ? 75  ASP A O   1 
ATOM   594  C  CB  . ASP A 1 75  ? 44.796  -1.118  9.662   1.00 20.97 ? 75  ASP A CB  1 
ATOM   595  C  CG  . ASP A 1 75  ? 44.588  -1.540  11.097  1.00 23.11 ? 75  ASP A CG  1 
ATOM   596  O  OD1 . ASP A 1 75  ? 44.273  -0.691  11.934  1.00 26.35 ? 75  ASP A OD1 1 
ATOM   597  O  OD2 . ASP A 1 75  ? 44.766  -2.736  11.377  1.00 27.44 ? 75  ASP A OD2 1 
ATOM   598  N  N   . MET A 1 76  ? 41.480  -1.877  9.610   1.00 14.95 ? 76  MET A N   1 
ATOM   599  C  CA  . MET A 1 76  ? 40.483  -2.973  9.490   1.00 14.75 ? 76  MET A CA  1 
ATOM   600  C  C   . MET A 1 76  ? 39.699  -2.737  8.231   1.00 13.49 ? 76  MET A C   1 
ATOM   601  O  O   . MET A 1 76  ? 39.274  -1.612  8.019   1.00 14.05 ? 76  MET A O   1 
ATOM   602  C  CB  . MET A 1 76  ? 39.576  -2.927  10.723  1.00 13.89 ? 76  MET A CB  1 
ATOM   603  C  CG  . MET A 1 76  ? 38.381  -3.849  10.669  1.00 14.24 ? 76  MET A CG  1 
ATOM   604  S  SD  . MET A 1 76  ? 37.714  -3.823  12.337  1.00 15.82 ? 76  MET A SD  1 
ATOM   605  C  CE  . MET A 1 76  ? 36.110  -4.538  11.924  1.00 14.41 ? 76  MET A CE  1 
ATOM   606  N  N   . HIS A 1 77  ? 39.578  -3.719  7.358   1.00 13.89 ? 77  HIS A N   1 
ATOM   607  C  CA  . HIS A 1 77  ? 38.870  -3.463  6.068   1.00 15.01 ? 77  HIS A CA  1 
ATOM   608  C  C   . HIS A 1 77  ? 38.267  -4.628  5.401   1.00 15.31 ? 77  HIS A C   1 
ATOM   609  O  O   . HIS A 1 77  ? 38.564  -5.801  5.712   1.00 17.23 ? 77  HIS A O   1 
ATOM   610  C  CB  . HIS A 1 77  ? 39.728  -2.649  5.088   1.00 17.09 ? 77  HIS A CB  1 
ATOM   611  C  CG  . HIS A 1 77  ? 40.958  -3.384  4.627   1.00 18.85 ? 77  HIS A CG  1 
ATOM   612  N  ND1 . HIS A 1 77  ? 42.146  -3.260  5.248   1.00 20.40 ? 77  HIS A ND1 1 
ATOM   613  C  CD2 . HIS A 1 77  ? 41.129  -4.318  3.642   1.00 21.32 ? 77  HIS A CD2 1 
ATOM   614  C  CE1 . HIS A 1 77  ? 43.052  -4.075  4.647   1.00 19.47 ? 77  HIS A CE1 1 
ATOM   615  N  NE2 . HIS A 1 77  ? 42.454  -4.693  3.659   1.00 20.79 ? 77  HIS A NE2 1 
ATOM   616  N  N   A ILE A 1 78  ? 37.344  -4.360  4.485   0.50 15.81 ? 78  ILE A N   1 
ATOM   617  N  N   B ILE A 1 78  ? 37.385  -4.335  4.442   0.50 16.25 ? 78  ILE A N   1 
ATOM   618  C  CA  A ILE A 1 78  ? 36.762  -5.399  3.701   0.50 15.74 ? 78  ILE A CA  1 
ATOM   619  C  CA  B ILE A 1 78  ? 36.746  -5.330  3.619   0.50 16.54 ? 78  ILE A CA  1 
ATOM   620  C  C   A ILE A 1 78  ? 37.514  -5.423  2.384   0.50 16.55 ? 78  ILE A C   1 
ATOM   621  C  C   B ILE A 1 78  ? 37.443  -5.418  2.281   0.50 16.99 ? 78  ILE A C   1 
ATOM   622  O  O   A ILE A 1 78  ? 37.771  -4.369  1.812   0.50 15.63 ? 78  ILE A O   1 
ATOM   623  O  O   B ILE A 1 78  ? 37.575  -4.420  1.572   0.50 15.91 ? 78  ILE A O   1 
ATOM   624  C  CB  A ILE A 1 78  ? 35.285  -5.071  3.357   0.50 15.89 ? 78  ILE A CB  1 
ATOM   625  C  CB  B ILE A 1 78  ? 35.270  -4.935  3.330   0.50 17.04 ? 78  ILE A CB  1 
ATOM   626  C  CG1 A ILE A 1 78  ? 34.532  -4.457  4.544   0.50 17.13 ? 78  ILE A CG1 1 
ATOM   627  C  CG1 B ILE A 1 78  ? 34.437  -5.308  4.539   0.50 18.16 ? 78  ILE A CG1 1 
ATOM   628  C  CG2 A ILE A 1 78  ? 34.618  -6.311  2.777   0.50 17.47 ? 78  ILE A CG2 1 
ATOM   629  C  CG2 B ILE A 1 78  ? 34.742  -5.645  2.077   0.50 17.71 ? 78  ILE A CG2 1 
ATOM   630  C  CD1 A ILE A 1 78  ? 33.089  -4.168  4.173   0.50 12.67 ? 78  ILE A CD1 1 
ATOM   631  C  CD1 B ILE A 1 78  ? 34.827  -6.587  5.178   0.50 19.17 ? 78  ILE A CD1 1 
ATOM   632  N  N   . GLN A 1 79  ? 37.877  -6.606  1.904   1.00 17.12 ? 79  GLN A N   1 
ATOM   633  C  CA  . GLN A 1 79  ? 38.324  -6.693  0.521   1.00 21.33 ? 79  GLN A CA  1 
ATOM   634  C  C   . GLN A 1 79  ? 37.364  -7.615  -0.227  1.00 20.90 ? 79  GLN A C   1 
ATOM   635  O  O   . GLN A 1 79  ? 36.747  -8.536  0.368   1.00 22.30 ? 79  GLN A O   1 
ATOM   636  C  CB  . GLN A 1 79  ? 39.769  -7.092  0.471   1.00 30.92 ? 79  GLN A CB  1 
ATOM   637  C  CG  . GLN A 1 79  ? 40.004  -8.436  1.072   1.00 35.43 ? 79  GLN A CG  1 
ATOM   638  C  CD  . GLN A 1 79  ? 40.861  -9.257  0.128   1.00 50.33 ? 79  GLN A CD  1 
ATOM   639  O  OE1 . GLN A 1 79  ? 42.091  -9.334  0.289   1.00 55.44 ? 79  GLN A OE1 1 
ATOM   640  N  NE2 . GLN A 1 79  ? 40.220  -9.836  -0.906  1.00 53.98 ? 79  GLN A NE2 1 
ATOM   641  N  N   . GLY A 1 80  ? 37.146  -7.319  -1.504  1.00 23.26 ? 80  GLY A N   1 
ATOM   642  C  CA  . GLY A 1 80  ? 36.159  -8.052  -2.302  1.00 22.14 ? 80  GLY A CA  1 
ATOM   643  C  C   . GLY A 1 80  ? 35.251  -7.054  -3.047  1.00 20.90 ? 80  GLY A C   1 
ATOM   644  O  O   . GLY A 1 80  ? 34.661  -7.403  -4.086  1.00 24.43 ? 80  GLY A O   1 
ATOM   645  N  N   . LEU A 1 81  ? 35.163  -5.821  -2.558  1.00 21.56 ? 81  LEU A N   1 
ATOM   646  C  CA  . LEU A 1 81  ? 34.324  -4.815  -3.203  1.00 23.02 ? 81  LEU A CA  1 
ATOM   647  C  C   . LEU A 1 81  ? 35.173  -4.081  -4.250  1.00 24.17 ? 81  LEU A C   1 
ATOM   648  O  O   . LEU A 1 81  ? 36.368  -4.400  -4.358  1.00 23.55 ? 81  LEU A O   1 
ATOM   649  C  CB  . LEU A 1 81  ? 33.583  -3.869  -2.201  1.00 21.46 ? 81  LEU A CB  1 
ATOM   650  C  CG  . LEU A 1 81  ? 32.662  -4.557  -1.146  1.00 22.45 ? 81  LEU A CG  1 
ATOM   651  C  CD1 . LEU A 1 81  ? 32.113  -3.598  -0.096  1.00 19.88 ? 81  LEU A CD1 1 
ATOM   652  C  CD2 . LEU A 1 81  ? 31.476  -5.227  -1.854  1.00 21.36 ? 81  LEU A CD2 1 
ATOM   653  N  N   . GLN A 1 82  ? 34.554  -3.207  -5.058  1.00 29.45 ? 82  GLN A N   1 
ATOM   654  C  CA  . GLN A 1 82  ? 35.325  -2.596  -6.168  1.00 30.13 ? 82  GLN A CA  1 
ATOM   655  C  C   . GLN A 1 82  ? 36.423  -1.723  -5.543  1.00 28.61 ? 82  GLN A C   1 
ATOM   656  O  O   . GLN A 1 82  ? 37.605  -1.699  -6.026  1.00 31.70 ? 82  GLN A O   1 
ATOM   657  C  CB  . GLN A 1 82  ? 34.423  -1.855  -7.163  1.00 39.73 ? 82  GLN A CB  1 
ATOM   658  C  CG  . GLN A 1 82  ? 34.900  -1.991  -8.624  1.00 45.64 ? 82  GLN A CG  1 
ATOM   659  C  CD  . GLN A 1 82  ? 34.521  -3.307  -9.307  1.00 51.05 ? 82  GLN A CD  1 
ATOM   660  O  OE1 . GLN A 1 82  ? 35.400  -4.059  -9.776  1.00 50.97 ? 82  GLN A OE1 1 
ATOM   661  N  NE2 . GLN A 1 82  ? 33.210  -3.589  -9.388  1.00 51.97 ? 82  GLN A NE2 1 
ATOM   662  N  N   . SER A 1 83  ? 36.088  -1.099  -4.413  1.00 21.68 ? 83  SER A N   1 
ATOM   663  C  CA  . SER A 1 83  ? 37.083  -0.276  -3.720  1.00 16.89 ? 83  SER A CA  1 
ATOM   664  C  C   . SER A 1 83  ? 37.351  -0.908  -2.373  1.00 17.88 ? 83  SER A C   1 
ATOM   665  O  O   . SER A 1 83  ? 36.518  -1.677  -1.922  1.00 14.95 ? 83  SER A O   1 
ATOM   666  C  CB  . SER A 1 83  ? 36.557  1.131   -3.445  1.00 17.14 ? 83  SER A CB  1 
ATOM   667  O  OG  . SER A 1 83  ? 36.364  1.773   -4.697  1.00 20.77 ? 83  SER A OG  1 
ATOM   668  N  N   . ARG A 1 84  ? 38.476  -0.590  -1.733  1.00 14.83 ? 84  ARG A N   1 
ATOM   669  C  CA  . ARG A 1 84  ? 38.622  -0.959  -0.322  1.00 14.36 ? 84  ARG A CA  1 
ATOM   670  C  C   . ARG A 1 84  ? 37.707  -0.178  0.541   1.00 12.87 ? 84  ARG A C   1 
ATOM   671  O  O   . ARG A 1 84  ? 37.638  1.072   0.483   1.00 13.21 ? 84  ARG A O   1 
ATOM   672  C  CB  . ARG A 1 84  ? 40.099  -0.820  0.147   1.00 14.47 ? 84  ARG A CB  1 
ATOM   673  C  CG  . ARG A 1 84  ? 40.223  -1.074  1.663   1.00 15.55 ? 84  ARG A CG  1 
ATOM   674  C  CD  . ARG A 1 84  ? 41.700  -0.883  2.114   1.00 16.69 ? 84  ARG A CD  1 
ATOM   675  N  NE  . ARG A 1 84  ? 42.520  -1.938  1.574   1.00 18.75 ? 84  ARG A NE  1 
ATOM   676  C  CZ  . ARG A 1 84  ? 43.836  -2.054  1.875   1.00 17.68 ? 84  ARG A CZ  1 
ATOM   677  N  NH1 . ARG A 1 84  ? 44.340  -1.288  2.813   1.00 17.90 ? 84  ARG A NH1 1 
ATOM   678  N  NH2 . ARG A 1 84  ? 44.541  -3.085  1.396   1.00 18.66 ? 84  ARG A NH2 1 
ATOM   679  N  N   . TYR A 1 85  ? 36.965  -0.884  1.435   1.00 13.43 ? 85  TYR A N   1 
ATOM   680  C  CA  . TYR A 1 85  ? 36.197  -0.206  2.467   1.00 12.04 ? 85  TYR A CA  1 
ATOM   681  C  C   . TYR A 1 85  ? 36.713  -0.461  3.891   1.00 12.60 ? 85  TYR A C   1 
ATOM   682  O  O   . TYR A 1 85  ? 36.816  -1.667  4.318   1.00 14.27 ? 85  TYR A O   1 
ATOM   683  C  CB  . TYR A 1 85  ? 34.683  -0.616  2.427   1.00 12.80 ? 85  TYR A CB  1 
ATOM   684  C  CG  . TYR A 1 85  ? 33.953  -0.036  1.227   1.00 11.44 ? 85  TYR A CG  1 
ATOM   685  C  CD1 . TYR A 1 85  ? 33.117  1.031   1.380   1.00 14.63 ? 85  TYR A CD1 1 
ATOM   686  C  CD2 . TYR A 1 85  ? 34.102  -0.595  -0.027  1.00 14.11 ? 85  TYR A CD2 1 
ATOM   687  C  CE1 . TYR A 1 85  ? 32.433  1.609   0.261   1.00 13.22 ? 85  TYR A CE1 1 
ATOM   688  C  CE2 . TYR A 1 85  ? 33.442  -0.075  -1.125  1.00 14.03 ? 85  TYR A CE2 1 
ATOM   689  C  CZ  . TYR A 1 85  ? 32.621  1.090   -0.953  1.00 14.42 ? 85  TYR A CZ  1 
ATOM   690  O  OH  . TYR A 1 85  ? 31.907  1.598   -2.043  1.00 20.54 ? 85  TYR A OH  1 
ATOM   691  N  N   . SER A 1 86  ? 37.119  0.647   4.528   1.00 11.24 ? 86  SER A N   1 
ATOM   692  C  CA  . SER A 1 86  ? 37.784  0.567   5.850   1.00 11.66 ? 86  SER A CA  1 
ATOM   693  C  C   . SER A 1 86  ? 36.793  0.766   6.990   1.00 13.22 ? 86  SER A C   1 
ATOM   694  O  O   . SER A 1 86  ? 35.852  1.592   6.872   1.00 12.83 ? 86  SER A O   1 
ATOM   695  C  CB  . SER A 1 86  ? 38.882  1.668   5.960   1.00 14.26 ? 86  SER A CB  1 
ATOM   696  O  OG  . SER A 1 86  ? 39.864  1.398   4.957   1.00 17.26 ? 86  SER A OG  1 
ATOM   697  N  N   . ALA A 1 87  ? 36.972  0.008   8.067   1.00 13.77 ? 87  ALA A N   1 
ATOM   698  C  CA  . ALA A 1 87  ? 36.058  0.093   9.191   1.00 14.40 ? 87  ALA A CA  1 
ATOM   699  C  C   . ALA A 1 87  ? 36.125  1.469   9.871   1.00 13.42 ? 87  ALA A C   1 
ATOM   700  O  O   . ALA A 1 87  ? 37.195  2.113   9.951   1.00 14.33 ? 87  ALA A O   1 
ATOM   701  C  CB  . ALA A 1 87  ? 36.335  -0.984  10.233  1.00 14.94 ? 87  ALA A CB  1 
ATOM   702  N  N   . THR A 1 88  ? 34.995  1.927   10.373  1.00 12.33 ? 88  THR A N   1 
ATOM   703  C  CA  . THR A 1 88  ? 34.940  3.117   11.226  1.00 12.66 ? 88  THR A CA  1 
ATOM   704  C  C   . THR A 1 88  ? 34.312  2.859   12.591  1.00 11.79 ? 88  THR A C   1 
ATOM   705  O  O   . THR A 1 88  ? 34.740  3.378   13.574  1.00 12.84 ? 88  THR A O   1 
ATOM   706  C  CB  . THR A 1 88  ? 34.295  4.367   10.508  1.00 14.23 ? 88  THR A CB  1 
ATOM   707  O  OG1 . THR A 1 88  ? 34.356  5.552   11.314  1.00 16.91 ? 88  THR A OG1 1 
ATOM   708  C  CG2 . THR A 1 88  ? 32.818  4.094   10.123  1.00 13.41 ? 88  THR A CG2 1 
ATOM   709  N  N   . GLN A 1 89  ? 33.231  2.060   12.651  1.00 11.98 ? 89  GLN A N   1 
ATOM   710  C  CA  . GLN A 1 89  ? 32.614  1.786   13.985  1.00 11.34 ? 89  GLN A CA  1 
ATOM   711  C  C   . GLN A 1 89  ? 31.646  0.618   13.780  1.00 10.21 ? 89  GLN A C   1 
ATOM   712  O  O   . GLN A 1 89  ? 31.304  0.289   12.648  1.00 11.40 ? 89  GLN A O   1 
ATOM   713  C  CB  . GLN A 1 89  ? 31.812  2.996   14.560  1.00 11.53 ? 89  GLN A CB  1 
ATOM   714  C  CG  . GLN A 1 89  ? 30.822  3.594   13.605  1.00 13.12 ? 89  GLN A CG  1 
ATOM   715  C  CD  . GLN A 1 89  ? 29.408  3.319   14.047  1.00 13.87 ? 89  GLN A CD  1 
ATOM   716  O  OE1 . GLN A 1 89  ? 29.062  2.200   14.220  1.00 15.23 ? 89  GLN A OE1 1 
ATOM   717  N  NE2 . GLN A 1 89  ? 28.677  4.319   14.301  1.00 19.39 ? 89  GLN A NE2 1 
ATOM   718  N  N   . LEU A 1 90  ? 31.231  0.025   14.909  1.00 10.75 ? 90  LEU A N   1 
ATOM   719  C  CA  . LEU A 1 90  ? 30.109  -0.910  14.912  1.00 10.86 ? 90  LEU A CA  1 
ATOM   720  C  C   . LEU A 1 90  ? 29.124  -0.482  16.005  1.00 10.33 ? 90  LEU A C   1 
ATOM   721  O  O   . LEU A 1 90  ? 29.471  0.214   16.966  1.00 9.96  ? 90  LEU A O   1 
ATOM   722  C  CB  . LEU A 1 90  ? 30.605  -2.370  15.021  1.00 11.53 ? 90  LEU A CB  1 
ATOM   723  C  CG  . LEU A 1 90  ? 31.361  -2.842  16.278  1.00 10.81 ? 90  LEU A CG  1 
ATOM   724  C  CD1 . LEU A 1 90  ? 30.493  -2.988  17.530  1.00 12.82 ? 90  LEU A CD1 1 
ATOM   725  C  CD2 . LEU A 1 90  ? 32.012  -4.183  15.962  1.00 11.40 ? 90  LEU A CD2 1 
ATOM   726  N  N   . HIS A 1 91  ? 27.882  -0.987  15.878  1.00 10.40 ? 91  HIS A N   1 
ATOM   727  C  CA  . HIS A 1 91  ? 26.806  -0.674  16.838  1.00 9.03  ? 91  HIS A CA  1 
ATOM   728  C  C   . HIS A 1 91  ? 25.716  -1.687  16.626  1.00 10.01 ? 91  HIS A C   1 
ATOM   729  O  O   . HIS A 1 91  ? 25.774  -2.517  15.697  1.00 10.04 ? 91  HIS A O   1 
ATOM   730  C  CB  . HIS A 1 91  ? 26.240  0.777   16.652  1.00 9.65  ? 91  HIS A CB  1 
ATOM   731  C  CG  . HIS A 1 91  ? 25.692  0.974   15.282  1.00 9.82  ? 91  HIS A CG  1 
ATOM   732  N  ND1 . HIS A 1 91  ? 26.454  1.306   14.282  1.00 9.68  ? 91  HIS A ND1 1 
ATOM   733  C  CD2 . HIS A 1 91  ? 24.442  0.672   14.732  1.00 9.08  ? 91  HIS A CD2 1 
ATOM   734  C  CE1 . HIS A 1 91  ? 25.833  1.323   13.131  1.00 8.73  ? 91  HIS A CE1 1 
ATOM   735  N  NE2 . HIS A 1 91  ? 24.544  0.871   13.379  1.00 9.18  ? 91  HIS A NE2 1 
ATOM   736  N  N   . LEU A 1 92  ? 24.702  -1.602  17.504  1.00 11.15 ? 92  LEU A N   1 
ATOM   737  C  CA  . LEU A 1 92  ? 23.595  -2.545  17.500  1.00 10.13 ? 92  LEU A CA  1 
ATOM   738  C  C   . LEU A 1 92  ? 22.257  -1.832  17.556  1.00 8.89  ? 92  LEU A C   1 
ATOM   739  O  O   . LEU A 1 92  ? 22.152  -0.619  17.881  1.00 9.78  ? 92  LEU A O   1 
ATOM   740  C  CB  . LEU A 1 92  ? 23.662  -3.491  18.736  1.00 12.30 ? 92  LEU A CB  1 
ATOM   741  C  CG  . LEU A 1 92  ? 24.891  -4.376  18.689  1.00 13.35 ? 92  LEU A CG  1 
ATOM   742  C  CD1 . LEU A 1 92  ? 25.920  -3.797  19.631  1.00 15.50 ? 92  LEU A CD1 1 
ATOM   743  C  CD2 . LEU A 1 92  ? 24.484  -5.803  19.008  1.00 13.54 ? 92  LEU A CD2 1 
ATOM   744  N  N   . HIS A 1 93  ? 21.218  -2.591  17.211  1.00 8.87  ? 93  HIS A N   1 
ATOM   745  C  CA  . HIS A 1 93  ? 19.794  -2.100  17.292  1.00 8.97  ? 93  HIS A CA  1 
ATOM   746  C  C   . HIS A 1 93  ? 19.031  -3.145  17.918  1.00 10.23 ? 93  HIS A C   1 
ATOM   747  O  O   . HIS A 1 93  ? 19.326  -4.319  17.725  1.00 9.77  ? 93  HIS A O   1 
ATOM   748  C  CB  . HIS A 1 93  ? 19.228  -1.939  15.870  1.00 9.76  ? 93  HIS A CB  1 
ATOM   749  C  CG  . HIS A 1 93  ? 19.962  -0.905  15.060  1.00 8.86  ? 93  HIS A CG  1 
ATOM   750  N  ND1 . HIS A 1 93  ? 19.620  0.446   15.030  1.00 9.64  ? 93  HIS A ND1 1 
ATOM   751  C  CD2 . HIS A 1 93  ? 21.065  -1.048  14.203  1.00 9.53  ? 93  HIS A CD2 1 
ATOM   752  C  CE1 . HIS A 1 93  ? 20.479  1.078   14.204  1.00 9.67  ? 93  HIS A CE1 1 
ATOM   753  N  NE2 . HIS A 1 93  ? 21.328  0.163   13.699  1.00 10.34 ? 93  HIS A NE2 1 
ATOM   754  N  N   . TRP A 1 94  ? 18.012  -2.787  18.705  1.00 10.68 ? 94  TRP A N   1 
ATOM   755  C  CA  . TRP A 1 94  ? 17.286  -3.876  19.472  1.00 9.87  ? 94  TRP A CA  1 
ATOM   756  C  C   . TRP A 1 94  ? 15.904  -3.381  19.832  1.00 11.11 ? 94  TRP A C   1 
ATOM   757  O  O   . TRP A 1 94  ? 15.586  -2.189  19.634  1.00 10.51 ? 94  TRP A O   1 
ATOM   758  C  CB  . TRP A 1 94  ? 17.973  -4.304  20.766  1.00 9.98  ? 94  TRP A CB  1 
ATOM   759  C  CG  . TRP A 1 94  ? 18.305  -3.155  21.680  1.00 10.48 ? 94  TRP A CG  1 
ATOM   760  C  CD1 . TRP A 1 94  ? 17.493  -2.635  22.699  1.00 11.01 ? 94  TRP A CD1 1 
ATOM   761  C  CD2 . TRP A 1 94  ? 19.507  -2.331  21.660  1.00 11.12 ? 94  TRP A CD2 1 
ATOM   762  N  NE1 . TRP A 1 94  ? 18.150  -1.551  23.332  1.00 12.09 ? 94  TRP A NE1 1 
ATOM   763  C  CE2 . TRP A 1 94  ? 19.382  -1.365  22.756  1.00 11.79 ? 94  TRP A CE2 1 
ATOM   764  C  CE3 . TRP A 1 94  ? 20.690  -2.332  20.886  1.00 11.53 ? 94  TRP A CE3 1 
ATOM   765  C  CZ2 . TRP A 1 94  ? 20.368  -0.418  23.018  1.00 10.56 ? 94  TRP A CZ2 1 
ATOM   766  C  CZ3 . TRP A 1 94  ? 21.634  -1.323  21.105  1.00 10.32 ? 94  TRP A CZ3 1 
ATOM   767  C  CH2 . TRP A 1 94  ? 21.530  -0.454  22.227  1.00 11.52 ? 94  TRP A CH2 1 
ATOM   768  N  N   . GLY A 1 95  ? 15.108  -4.267  20.452  1.00 10.22 ? 95  GLY A N   1 
ATOM   769  C  CA  . GLY A 1 95  ? 13.727  -3.817  20.803  1.00 11.23 ? 95  GLY A CA  1 
ATOM   770  C  C   . GLY A 1 95  ? 13.636  -3.572  22.283  1.00 10.18 ? 95  GLY A C   1 
ATOM   771  O  O   . GLY A 1 95  ? 14.248  -2.681  22.842  1.00 11.67 ? 95  GLY A O   1 
ATOM   772  N  N   . ASN A 1 96  ? 12.780  -4.364  22.946  1.00 11.58 ? 96  ASN A N   1 
ATOM   773  C  CA  . ASN A 1 96  ? 12.544  -4.155  24.431  1.00 12.67 ? 96  ASN A CA  1 
ATOM   774  C  C   . ASN A 1 96  ? 12.036  -5.449  25.049  1.00 14.23 ? 96  ASN A C   1 
ATOM   775  O  O   . ASN A 1 96  ? 11.579  -6.304  24.319  1.00 11.61 ? 96  ASN A O   1 
ATOM   776  C  CB  . ASN A 1 96  ? 11.595  -2.977  24.637  1.00 13.51 ? 96  ASN A CB  1 
ATOM   777  C  CG  . ASN A 1 96  ? 10.128  -3.321  24.380  1.00 17.25 ? 96  ASN A CG  1 
ATOM   778  O  OD1 . ASN A 1 96  ? 9.471   -3.862  25.283  1.00 21.19 ? 96  ASN A OD1 1 
ATOM   779  N  ND2 . ASN A 1 96  ? 9.599   -3.005  23.173  1.00 17.26 ? 96  ASN A ND2 1 
ATOM   780  N  N   . PRO A 1 97  ? 12.142  -5.606  26.385  1.00 14.15 ? 97  PRO A N   1 
ATOM   781  C  CA  . PRO A 1 97  ? 11.874  -6.978  26.866  1.00 13.85 ? 97  PRO A CA  1 
ATOM   782  C  C   . PRO A 1 97  ? 10.392  -7.398  26.672  1.00 14.09 ? 97  PRO A C   1 
ATOM   783  O  O   . PRO A 1 97  ? 10.138  -8.568  26.680  1.00 15.62 ? 97  PRO A O   1 
ATOM   784  C  CB  . PRO A 1 97  ? 12.161  -6.849  28.355  1.00 14.32 ? 97  PRO A CB  1 
ATOM   785  C  CG  . PRO A 1 97  ? 13.226  -5.733  28.453  1.00 14.39 ? 97  PRO A CG  1 
ATOM   786  C  CD  . PRO A 1 97  ? 12.774  -4.768  27.403  1.00 14.35 ? 97  PRO A CD  1 
ATOM   787  N  N   . ASN A 1 98  ? 9.454   -6.482  26.532  1.00 13.28 ? 98  ASN A N   1 
ATOM   788  C  CA  . ASN A 1 98  ? 8.060   -6.863  26.246  1.00 15.91 ? 98  ASN A CA  1 
ATOM   789  C  C   . ASN A 1 98  ? 7.836   -7.177  24.770  1.00 15.17 ? 98  ASN A C   1 
ATOM   790  O  O   . ASN A 1 98  ? 6.793   -7.762  24.396  1.00 19.02 ? 98  ASN A O   1 
ATOM   791  C  CB  . ASN A 1 98  ? 7.162   -5.636  26.549  1.00 16.30 ? 98  ASN A CB  1 
ATOM   792  C  CG  . ASN A 1 98  ? 6.913   -5.467  28.005  1.00 23.02 ? 98  ASN A CG  1 
ATOM   793  O  OD1 . ASN A 1 98  ? 6.958   -6.425  28.760  1.00 27.12 ? 98  ASN A OD1 1 
ATOM   794  N  ND2 . ASN A 1 98  ? 6.571   -4.259  28.407  1.00 26.38 ? 98  ASN A ND2 1 
ATOM   795  N  N   . ASP A 1 99  ? 8.739   -6.726  23.874  1.00 13.36 ? 99  ASP A N   1 
ATOM   796  C  CA  . ASP A 1 99  ? 8.603   -7.107  22.463  1.00 14.41 ? 99  ASP A CA  1 
ATOM   797  C  C   . ASP A 1 99  ? 10.021  -7.212  21.889  1.00 13.81 ? 99  ASP A C   1 
ATOM   798  O  O   . ASP A 1 99  ? 10.504  -6.314  21.300  1.00 13.47 ? 99  ASP A O   1 
ATOM   799  C  CB  . ASP A 1 99  ? 7.749   -6.037  21.722  1.00 16.24 ? 99  ASP A CB  1 
ATOM   800  C  CG  . ASP A 1 99  ? 7.289   -6.474  20.365  1.00 18.37 ? 99  ASP A CG  1 
ATOM   801  O  OD1 . ASP A 1 99  ? 7.648   -7.539  19.871  1.00 19.78 ? 99  ASP A OD1 1 
ATOM   802  O  OD2 . ASP A 1 99  ? 6.506   -5.757  19.748  1.00 21.42 ? 99  ASP A OD2 1 
ATOM   803  N  N   . PRO A 1 100 ? 10.670  -8.346  22.123  1.00 13.26 ? 100 PRO A N   1 
ATOM   804  C  CA  . PRO A 1 100 ? 12.150  -8.407  21.984  1.00 13.35 ? 100 PRO A CA  1 
ATOM   805  C  C   . PRO A 1 100 ? 12.533  -8.747  20.556  1.00 12.75 ? 100 PRO A C   1 
ATOM   806  O  O   . PRO A 1 100 ? 13.115  -9.808  20.263  1.00 13.57 ? 100 PRO A O   1 
ATOM   807  C  CB  . PRO A 1 100 ? 12.541  -9.521  22.977  1.00 13.88 ? 100 PRO A CB  1 
ATOM   808  C  CG  . PRO A 1 100 ? 11.359  -10.455 22.943  1.00 16.57 ? 100 PRO A CG  1 
ATOM   809  C  CD  . PRO A 1 100 ? 10.186  -9.514  22.888  1.00 13.68 ? 100 PRO A CD  1 
ATOM   810  N  N   . HIS A 1 101 ? 12.156  -7.874  19.641  1.00 12.46 ? 101 HIS A N   1 
ATOM   811  C  CA  . HIS A 1 101 ? 12.285  -8.213  18.184  1.00 13.70 ? 101 HIS A CA  1 
ATOM   812  C  C   . HIS A 1 101 ? 12.600  -6.971  17.475  1.00 14.99 ? 101 HIS A C   1 
ATOM   813  O  O   . HIS A 1 101 ? 11.708  -6.391  16.792  1.00 20.09 ? 101 HIS A O   1 
ATOM   814  C  CB  . HIS A 1 101 ? 10.930  -8.684  17.640  1.00 14.93 ? 101 HIS A CB  1 
ATOM   815  C  CG  . HIS A 1 101 ? 10.391  -9.841  18.389  1.00 17.04 ? 101 HIS A CG  1 
ATOM   816  N  ND1 . HIS A 1 101 ? 10.914  -11.100 18.278  1.00 18.05 ? 101 HIS A ND1 1 
ATOM   817  C  CD2 . HIS A 1 101 ? 9.391   -9.906  19.362  1.00 17.54 ? 101 HIS A CD2 1 
ATOM   818  C  CE1 . HIS A 1 101 ? 10.259  -11.937 19.110  1.00 21.03 ? 101 HIS A CE1 1 
ATOM   819  N  NE2 . HIS A 1 101 ? 9.352   -11.217 19.806  1.00 19.80 ? 101 HIS A NE2 1 
ATOM   820  N  N   . GLY A 1 102 ? 13.852  -6.518  17.604  1.00 11.55 ? 102 GLY A N   1 
ATOM   821  C  CA  . GLY A 1 102 ? 14.187  -5.137  17.248  1.00 10.83 ? 102 GLY A CA  1 
ATOM   822  C  C   . GLY A 1 102 ? 15.295  -5.112  16.170  1.00 10.90 ? 102 GLY A C   1 
ATOM   823  O  O   . GLY A 1 102 ? 16.018  -4.144  16.086  1.00 9.85  ? 102 GLY A O   1 
ATOM   824  N  N   . SER A 1 103 ? 15.417  -6.146  15.343  1.00 10.42 ? 103 SER A N   1 
ATOM   825  C  CA  . SER A 1 103 ? 16.294  -5.984  14.137  1.00 9.54  ? 103 SER A CA  1 
ATOM   826  C  C   . SER A 1 103 ? 15.714  -4.877  13.248  1.00 12.32 ? 103 SER A C   1 
ATOM   827  O  O   . SER A 1 103 ? 14.514  -4.594  13.328  1.00 12.86 ? 103 SER A O   1 
ATOM   828  C  CB  . SER A 1 103 ? 16.415  -7.348  13.401  1.00 9.68  ? 103 SER A CB  1 
ATOM   829  O  OG  . SER A 1 103 ? 15.212  -7.761  12.711  1.00 10.02 ? 103 SER A OG  1 
ATOM   830  N  N   . GLU A 1 104 ? 16.555  -4.334  12.362  1.00 10.32 ? 104 GLU A N   1 
ATOM   831  C  CA  . GLU A 1 104 ? 16.128  -3.352  11.361  1.00 10.36 ? 104 GLU A CA  1 
ATOM   832  C  C   . GLU A 1 104 ? 15.606  -4.056  10.117  1.00 10.95 ? 104 GLU A C   1 
ATOM   833  O  O   . GLU A 1 104 ? 14.453  -3.888  9.707   1.00 12.23 ? 104 GLU A O   1 
ATOM   834  C  CB  . GLU A 1 104 ? 17.281  -2.403  11.006  1.00 10.50 ? 104 GLU A CB  1 
ATOM   835  C  CG  . GLU A 1 104 ? 17.804  -1.736  12.265  1.00 9.94  ? 104 GLU A CG  1 
ATOM   836  C  CD  . GLU A 1 104 ? 18.177  -0.297  11.957  1.00 11.04 ? 104 GLU A CD  1 
ATOM   837  O  OE1 . GLU A 1 104 ? 19.190  -0.111  11.251  1.00 10.47 ? 104 GLU A OE1 1 
ATOM   838  O  OE2 . GLU A 1 104 ? 17.392  0.626   12.232  1.00 11.39 ? 104 GLU A OE2 1 
ATOM   839  N  N   . HIS A 1 105 ? 16.454  -4.842  9.495   1.00 9.49  ? 105 HIS A N   1 
ATOM   840  C  CA  . HIS A 1 105 ? 15.962  -5.766  8.425   1.00 9.01  ? 105 HIS A CA  1 
ATOM   841  C  C   . HIS A 1 105 ? 15.089  -6.882  8.951   1.00 9.80  ? 105 HIS A C   1 
ATOM   842  O  O   . HIS A 1 105 ? 15.322  -7.410  10.032  1.00 10.53 ? 105 HIS A O   1 
ATOM   843  C  CB  . HIS A 1 105 ? 17.113  -6.334  7.593   1.00 8.77  ? 105 HIS A CB  1 
ATOM   844  C  CG  . HIS A 1 105 ? 17.922  -5.251  6.903   1.00 8.55  ? 105 HIS A CG  1 
ATOM   845  N  ND1 . HIS A 1 105 ? 18.951  -4.568  7.487   1.00 11.02 ? 105 HIS A ND1 1 
ATOM   846  C  CD2 . HIS A 1 105 ? 17.824  -4.761  5.603   1.00 8.39  ? 105 HIS A CD2 1 
ATOM   847  C  CE1 . HIS A 1 105 ? 19.426  -3.636  6.633   1.00 10.07 ? 105 HIS A CE1 1 
ATOM   848  N  NE2 . HIS A 1 105 ? 18.785  -3.768  5.469   1.00 9.11  ? 105 HIS A NE2 1 
ATOM   849  N  N   . THR A 1 106 ? 14.121  -7.206  8.155   1.00 9.53  ? 106 THR A N   1 
ATOM   850  C  CA  . THR A 1 106 ? 13.302  -8.398  8.389   1.00 9.94  ? 106 THR A CA  1 
ATOM   851  C  C   . THR A 1 106 ? 13.451  -9.333  7.264   1.00 10.21 ? 106 THR A C   1 
ATOM   852  O  O   . THR A 1 106 ? 13.879  -9.032  6.172   1.00 10.36 ? 106 THR A O   1 
ATOM   853  C  CB  . THR A 1 106 ? 11.800  -7.915  8.547   1.00 9.95  ? 106 THR A CB  1 
ATOM   854  O  OG1 . THR A 1 106 ? 11.360  -7.338  7.315   1.00 11.22 ? 106 THR A OG1 1 
ATOM   855  C  CG2 . THR A 1 106 ? 11.614  -7.022  9.769   1.00 9.62  ? 106 THR A CG2 1 
ATOM   856  N  N   . VAL A 1 107 ? 13.083  -10.606 7.540   1.00 10.66 ? 107 VAL A N   1 
ATOM   857  C  CA  . VAL A 1 107 ? 13.222  -11.745 6.566   1.00 12.50 ? 107 VAL A CA  1 
ATOM   858  C  C   . VAL A 1 107 ? 11.818  -12.383 6.472   1.00 12.71 ? 107 VAL A C   1 
ATOM   859  O  O   . VAL A 1 107 ? 11.278  -12.782 7.489   1.00 14.08 ? 107 VAL A O   1 
ATOM   860  C  CB  . VAL A 1 107 ? 14.278  -12.741 6.975   1.00 12.22 ? 107 VAL A CB  1 
ATOM   861  C  CG1 . VAL A 1 107 ? 14.306  -13.970 6.025   1.00 14.59 ? 107 VAL A CG1 1 
ATOM   862  C  CG2 . VAL A 1 107 ? 15.662  -12.083 7.073   1.00 13.32 ? 107 VAL A CG2 1 
ATOM   863  N  N   . SER A 1 108 ? 11.238  -12.297 5.275   1.00 12.46 ? 108 SER A N   1 
ATOM   864  C  CA  . SER A 1 108 ? 9.850   -12.720 5.049   1.00 15.19 ? 108 SER A CA  1 
ATOM   865  C  C   . SER A 1 108 ? 8.913   -12.143 6.118   1.00 14.99 ? 108 SER A C   1 
ATOM   866  O  O   . SER A 1 108 ? 8.041   -12.844 6.693   1.00 14.77 ? 108 SER A O   1 
ATOM   867  C  CB  . SER A 1 108 ? 9.810   -14.265 5.010   1.00 16.82 ? 108 SER A CB  1 
ATOM   868  O  OG  . SER A 1 108 ? 10.682  -14.718 3.957   1.00 22.77 ? 108 SER A OG  1 
ATOM   869  N  N   . GLY A 1 109 ? 9.133   -10.857 6.432   1.00 13.26 ? 109 GLY A N   1 
ATOM   870  C  CA  . GLY A 1 109 ? 8.299   -10.043 7.313   1.00 15.10 ? 109 GLY A CA  1 
ATOM   871  C  C   . GLY A 1 109 ? 8.611   -10.210 8.793   1.00 16.02 ? 109 GLY A C   1 
ATOM   872  O  O   . GLY A 1 109 ? 8.035   -9.493  9.612   1.00 23.15 ? 109 GLY A O   1 
ATOM   873  N  N   . GLN A 1 110 ? 9.557   -11.096 9.137   1.00 14.45 ? 110 GLN A N   1 
ATOM   874  C  CA  . GLN A 1 110 ? 9.900   -11.389 10.516  1.00 15.38 ? 110 GLN A CA  1 
ATOM   875  C  C   . GLN A 1 110 ? 11.136  -10.666 11.017  1.00 14.26 ? 110 GLN A C   1 
ATOM   876  O  O   . GLN A 1 110 ? 12.133  -10.640 10.336  1.00 12.13 ? 110 GLN A O   1 
ATOM   877  C  CB  . GLN A 1 110 ? 10.143  -12.889 10.650  1.00 16.11 ? 110 GLN A CB  1 
ATOM   878  C  CG  . GLN A 1 110 ? 9.013   -13.759 10.114  1.00 20.15 ? 110 GLN A CG  1 
ATOM   879  C  CD  . GLN A 1 110 ? 7.619   -13.359 10.631  1.00 19.62 ? 110 GLN A CD  1 
ATOM   880  O  OE1 . GLN A 1 110 ? 7.358   -13.241 11.837  1.00 24.25 ? 110 GLN A OE1 1 
ATOM   881  N  NE2 . GLN A 1 110 ? 6.687   -13.187 9.689   1.00 22.84 ? 110 GLN A NE2 1 
ATOM   882  N  N   . HIS A 1 111 ? 10.994  -10.025 12.179  1.00 15.20 ? 111 HIS A N   1 
ATOM   883  C  CA  . HIS A 1 111 ? 12.095  -9.401  12.898  1.00 13.64 ? 111 HIS A CA  1 
ATOM   884  C  C   . HIS A 1 111 ? 12.883  -10.426 13.607  1.00 15.17 ? 111 HIS A C   1 
ATOM   885  O  O   . HIS A 1 111 ? 12.346  -11.381 14.146  1.00 17.68 ? 111 HIS A O   1 
ATOM   886  C  CB  . HIS A 1 111 ? 11.626  -8.450  13.959  1.00 17.57 ? 111 HIS A CB  1 
ATOM   887  C  CG  . HIS A 1 111 ? 11.328  -7.074  13.451  1.00 15.38 ? 111 HIS A CG  1 
ATOM   888  N  ND1 . HIS A 1 111 ? 10.088  -6.716  13.001  1.00 20.30 ? 111 HIS A ND1 1 
ATOM   889  C  CD2 . HIS A 1 111 ? 12.141  -5.956  13.305  1.00 14.98 ? 111 HIS A CD2 1 
ATOM   890  C  CE1 . HIS A 1 111 ? 10.108  -5.406  12.599  1.00 15.41 ? 111 HIS A CE1 1 
ATOM   891  N  NE2 . HIS A 1 111 ? 11.372  -4.938  12.808  1.00 20.60 ? 111 HIS A NE2 1 
ATOM   892  N  N   . PHE A 1 112 ? 14.189  -10.217 13.597  1.00 12.19 ? 112 PHE A N   1 
ATOM   893  C  CA  . PHE A 1 112 ? 15.120  -10.876 14.530  1.00 12.47 ? 112 PHE A CA  1 
ATOM   894  C  C   . PHE A 1 112 ? 15.149  -10.125 15.867  1.00 11.39 ? 112 PHE A C   1 
ATOM   895  O  O   . PHE A 1 112 ? 14.681  -8.944  15.951  1.00 11.60 ? 112 PHE A O   1 
ATOM   896  C  CB  . PHE A 1 112 ? 16.498  -11.067 13.860  1.00 12.03 ? 112 PHE A CB  1 
ATOM   897  C  CG  . PHE A 1 112 ? 16.464  -12.185 12.846  1.00 14.71 ? 112 PHE A CG  1 
ATOM   898  C  CD1 . PHE A 1 112 ? 16.890  -13.447 13.262  1.00 15.82 ? 112 PHE A CD1 1 
ATOM   899  C  CD2 . PHE A 1 112 ? 15.900  -12.042 11.564  1.00 16.97 ? 112 PHE A CD2 1 
ATOM   900  C  CE1 . PHE A 1 112 ? 16.837  -14.570 12.425  1.00 18.04 ? 112 PHE A CE1 1 
ATOM   901  C  CE2 . PHE A 1 112 ? 15.837  -13.182 10.718  1.00 17.77 ? 112 PHE A CE2 1 
ATOM   902  C  CZ  . PHE A 1 112 ? 16.338  -14.415 11.161  1.00 19.90 ? 112 PHE A CZ  1 
ATOM   903  N  N   . ALA A 1 113 ? 15.773  -10.713 16.870  1.00 10.95 ? 113 ALA A N   1 
ATOM   904  C  CA  . ALA A 1 113 ? 15.876  -10.095 18.194  1.00 10.26 ? 113 ALA A CA  1 
ATOM   905  C  C   . ALA A 1 113 ? 16.602  -8.802  18.129  1.00 10.55 ? 113 ALA A C   1 
ATOM   906  O  O   . ALA A 1 113 ? 16.220  -7.829  18.781  1.00 11.01 ? 113 ALA A O   1 
ATOM   907  C  CB  . ALA A 1 113 ? 16.566  -11.025 19.243  1.00 10.83 ? 113 ALA A CB  1 
ATOM   908  N  N   . ALA A 1 114 ? 17.713  -8.790  17.362  1.00 10.20 ? 114 ALA A N   1 
ATOM   909  C  CA  . ALA A 1 114 ? 18.565  -7.570  17.332  1.00 9.48  ? 114 ALA A CA  1 
ATOM   910  C  C   . ALA A 1 114 ? 19.412  -7.645  16.077  1.00 9.75  ? 114 ALA A C   1 
ATOM   911  O  O   . ALA A 1 114 ? 19.304  -8.588  15.260  1.00 10.14 ? 114 ALA A O   1 
ATOM   912  C  CB  . ALA A 1 114 ? 19.506  -7.526  18.542  1.00 10.76 ? 114 ALA A CB  1 
ATOM   913  N  N   . GLU A 1 115 ? 20.225  -6.603  15.862  1.00 9.16  ? 115 GLU A N   1 
ATOM   914  C  CA  . GLU A 1 115 ? 21.018  -6.552  14.613  1.00 9.64  ? 115 GLU A CA  1 
ATOM   915  C  C   . GLU A 1 115 ? 22.269  -5.742  14.900  1.00 10.18 ? 115 GLU A C   1 
ATOM   916  O  O   . GLU A 1 115 ? 22.233  -4.675  15.544  1.00 10.39 ? 115 GLU A O   1 
ATOM   917  C  CB  . GLU A 1 115 ? 20.169  -5.919  13.492  1.00 8.94  ? 115 GLU A CB  1 
ATOM   918  C  CG  . GLU A 1 115 ? 20.813  -5.947  12.104  1.00 8.81  ? 115 GLU A CG  1 
ATOM   919  C  CD  . GLU A 1 115 ? 19.871  -5.581  10.965  1.00 9.81  ? 115 GLU A CD  1 
ATOM   920  O  OE1 . GLU A 1 115 ? 18.665  -5.867  11.086  1.00 10.40 ? 115 GLU A OE1 1 
ATOM   921  O  OE2 . GLU A 1 115 ? 20.354  -5.165  9.890   1.00 9.52  ? 115 GLU A OE2 1 
ATOM   922  N  N   A LEU A 1 116 ? 23.412  -6.320  14.432  0.50 9.28  ? 116 LEU A N   1 
ATOM   923  N  N   B LEU A 1 116 ? 23.426  -6.295  14.513  0.50 9.76  ? 116 LEU A N   1 
ATOM   924  C  CA  A LEU A 1 116 ? 24.791  -5.747  14.514  0.50 8.45  ? 116 LEU A CA  1 
ATOM   925  C  CA  B LEU A 1 116 ? 24.672  -5.563  14.679  0.50 9.00  ? 116 LEU A CA  1 
ATOM   926  C  C   A LEU A 1 116 ? 25.161  -5.162  13.179  0.50 8.36  ? 116 LEU A C   1 
ATOM   927  C  C   B LEU A 1 116 ? 25.150  -5.152  13.299  0.50 8.71  ? 116 LEU A C   1 
ATOM   928  O  O   A LEU A 1 116 ? 25.001  -5.783  12.113  0.50 8.03  ? 116 LEU A O   1 
ATOM   929  O  O   B LEU A 1 116 ? 24.984  -5.847  12.320  0.50 8.50  ? 116 LEU A O   1 
ATOM   930  C  CB  A LEU A 1 116 ? 25.833  -6.840  14.908  0.50 8.37  ? 116 LEU A CB  1 
ATOM   931  C  CB  B LEU A 1 116 ? 25.693  -6.395  15.434  0.50 9.46  ? 116 LEU A CB  1 
ATOM   932  C  CG  A LEU A 1 116 ? 27.305  -6.287  14.816  0.50 8.37  ? 116 LEU A CG  1 
ATOM   933  C  CG  B LEU A 1 116 ? 27.132  -5.898  15.363  0.50 9.90  ? 116 LEU A CG  1 
ATOM   934  C  CD1 A LEU A 1 116 ? 27.667  -5.145  15.824  0.50 9.13  ? 116 LEU A CD1 1 
ATOM   935  C  CD1 B LEU A 1 116 ? 27.800  -6.304  16.665  0.50 9.79  ? 116 LEU A CD1 1 
ATOM   936  C  CD2 A LEU A 1 116 ? 28.266  -7.481  14.841  0.50 8.55  ? 116 LEU A CD2 1 
ATOM   937  C  CD2 B LEU A 1 116 ? 27.760  -6.406  14.084  0.50 9.85  ? 116 LEU A CD2 1 
ATOM   938  N  N   . HIS A 1 117 ? 25.650  -3.901  13.226  1.00 8.12  ? 117 HIS A N   1 
ATOM   939  C  CA  . HIS A 1 117 ? 26.140  -3.237  11.959  1.00 8.45  ? 117 HIS A CA  1 
ATOM   940  C  C   . HIS A 1 117 ? 27.560  -2.808  12.138  1.00 8.83  ? 117 HIS A C   1 
ATOM   941  O  O   . HIS A 1 117 ? 27.920  -2.287  13.169  1.00 9.95  ? 117 HIS A O   1 
ATOM   942  C  CB  . HIS A 1 117 ? 25.355  -1.960  11.735  1.00 8.46  ? 117 HIS A CB  1 
ATOM   943  C  CG  . HIS A 1 117 ? 23.947  -2.228  11.357  1.00 9.41  ? 117 HIS A CG  1 
ATOM   944  N  ND1 . HIS A 1 117 ? 22.930  -1.308  11.486  1.00 9.08  ? 117 HIS A ND1 1 
ATOM   945  C  CD2 . HIS A 1 117 ? 23.402  -3.336  10.782  1.00 9.44  ? 117 HIS A CD2 1 
ATOM   946  C  CE1 . HIS A 1 117 ? 21.830  -1.838  10.925  1.00 8.49  ? 117 HIS A CE1 1 
ATOM   947  N  NE2 . HIS A 1 117 ? 22.070  -3.085  10.607  1.00 9.50  ? 117 HIS A NE2 1 
ATOM   948  N  N   . ILE A 1 118 ? 28.379  -3.147  11.143  1.00 9.50  ? 118 ILE A N   1 
ATOM   949  C  CA  . ILE A 1 118 ? 29.828  -2.790  11.161  1.00 9.88  ? 118 ILE A CA  1 
ATOM   950  C  C   . ILE A 1 118 ? 29.922  -1.813  10.003  1.00 10.04 ? 118 ILE A C   1 
ATOM   951  O  O   . ILE A 1 118 ? 29.766  -2.182  8.815   1.00 8.92  ? 118 ILE A O   1 
ATOM   952  C  CB  . ILE A 1 118 ? 30.764  -4.020  10.928  1.00 10.74 ? 118 ILE A CB  1 
ATOM   953  C  CG1 . ILE A 1 118 ? 30.471  -5.130  11.924  1.00 11.75 ? 118 ILE A CG1 1 
ATOM   954  C  CG2 . ILE A 1 118 ? 32.226  -3.520  11.185  1.00 12.00 ? 118 ILE A CG2 1 
ATOM   955  C  CD1 . ILE A 1 118 ? 31.238  -6.468  11.794  1.00 13.92 ? 118 ILE A CD1 1 
ATOM   956  N  N   . VAL A 1 119 ? 30.113  -0.535  10.314  1.00 10.10 ? 119 VAL A N   1 
ATOM   957  C  CA  . VAL A 1 119 ? 30.121  0.449   9.220   1.00 10.27 ? 119 VAL A CA  1 
ATOM   958  C  C   . VAL A 1 119 ? 31.517  0.607   8.700   1.00 10.18 ? 119 VAL A C   1 
ATOM   959  O  O   . VAL A 1 119 ? 32.440  0.747   9.496   1.00 11.00 ? 119 VAL A O   1 
ATOM   960  C  CB  . VAL A 1 119 ? 29.678  1.768   9.867   1.00 10.84 ? 119 VAL A CB  1 
ATOM   961  C  CG1 . VAL A 1 119 ? 29.552  2.970   8.906   1.00 12.75 ? 119 VAL A CG1 1 
ATOM   962  C  CG2 . VAL A 1 119 ? 28.248  1.553   10.468  1.00 9.63  ? 119 VAL A CG2 1 
ATOM   963  N  N   . HIS A 1 120 ? 31.620  0.699   7.376   1.00 9.34  ? 120 HIS A N   1 
ATOM   964  C  CA  . HIS A 1 120 ? 32.935  0.918   6.587   1.00 11.32 ? 120 HIS A CA  1 
ATOM   965  C  C   . HIS A 1 120 ? 32.757  2.075   5.655   1.00 12.82 ? 120 HIS A C   1 
ATOM   966  O  O   . HIS A 1 120 ? 31.619  2.453   5.230   1.00 11.36 ? 120 HIS A O   1 
ATOM   967  C  CB  . HIS A 1 120 ? 33.342  -0.317  5.767   1.00 12.45 ? 120 HIS A CB  1 
ATOM   968  C  CG  . HIS A 1 120 ? 33.511  -1.565  6.600   1.00 12.15 ? 120 HIS A CG  1 
ATOM   969  N  ND1 . HIS A 1 120 ? 32.443  -2.211  7.243   1.00 12.85 ? 120 HIS A ND1 1 
ATOM   970  C  CD2 . HIS A 1 120 ? 34.642  -2.326  6.866   1.00 11.94 ? 120 HIS A CD2 1 
ATOM   971  C  CE1 . HIS A 1 120 ? 32.903  -3.285  7.898   1.00 12.53 ? 120 HIS A CE1 1 
ATOM   972  N  NE2 . HIS A 1 120 ? 34.237  -3.417  7.598   1.00 12.81 ? 120 HIS A NE2 1 
ATOM   973  N  N   . TYR A 1 121 ? 33.885  2.678   5.267   1.00 12.35 ? 121 TYR A N   1 
ATOM   974  C  CA  . TYR A 1 121 ? 33.835  3.773   4.294   1.00 13.51 ? 121 TYR A CA  1 
ATOM   975  C  C   . TYR A 1 121 ? 34.832  3.572   3.200   1.00 14.98 ? 121 TYR A C   1 
ATOM   976  O  O   . TYR A 1 121 ? 35.814  2.839   3.374   1.00 14.69 ? 121 TYR A O   1 
ATOM   977  C  CB  . TYR A 1 121 ? 34.048  5.149   4.957   1.00 13.61 ? 121 TYR A CB  1 
ATOM   978  C  CG  . TYR A 1 121 ? 35.454  5.367   5.468   1.00 14.53 ? 121 TYR A CG  1 
ATOM   979  C  CD1 . TYR A 1 121 ? 36.346  6.078   4.677   1.00 17.04 ? 121 TYR A CD1 1 
ATOM   980  C  CD2 . TYR A 1 121 ? 35.856  4.854   6.729   1.00 15.33 ? 121 TYR A CD2 1 
ATOM   981  C  CE1 . TYR A 1 121 ? 37.704  6.227   5.124   1.00 16.81 ? 121 TYR A CE1 1 
ATOM   982  C  CE2 . TYR A 1 121 ? 37.164  5.014   7.201   1.00 18.17 ? 121 TYR A CE2 1 
ATOM   983  C  CZ  . TYR A 1 121 ? 38.070  5.739   6.401   1.00 20.02 ? 121 TYR A CZ  1 
ATOM   984  O  OH  . TYR A 1 121 ? 39.406  5.918   6.812   1.00 21.34 ? 121 TYR A OH  1 
ATOM   985  N  N   . ASN A 1 122 ? 34.561  4.209   2.050   1.00 15.43 ? 122 ASN A N   1 
ATOM   986  C  CA  . ASN A 1 122 ? 35.429  4.022   0.868   1.00 14.65 ? 122 ASN A CA  1 
ATOM   987  C  C   . ASN A 1 122 ? 36.702  4.826   1.103   1.00 14.50 ? 122 ASN A C   1 
ATOM   988  O  O   . ASN A 1 122 ? 36.755  5.999   0.834   1.00 16.26 ? 122 ASN A O   1 
ATOM   989  C  CB  . ASN A 1 122 ? 34.753  4.447   -0.450  1.00 14.78 ? 122 ASN A CB  1 
ATOM   990  C  CG  . ASN A 1 122 ? 35.498  4.012   -1.691  1.00 17.40 ? 122 ASN A CG  1 
ATOM   991  O  OD1 . ASN A 1 122 ? 36.738  3.879   -1.703  1.00 16.61 ? 122 ASN A OD1 1 
ATOM   992  N  ND2 . ASN A 1 122 ? 34.759  3.737   -2.754  1.00 18.47 ? 122 ASN A ND2 1 
ATOM   993  N  N   . SER A 1 123 ? 37.771  4.127   1.498   1.00 14.75 ? 123 SER A N   1 
ATOM   994  C  CA  . SER A 1 123 ? 38.977  4.814   1.892   1.00 15.74 ? 123 SER A CA  1 
ATOM   995  C  C   . SER A 1 123 ? 39.882  4.998   0.647   1.00 18.50 ? 123 SER A C   1 
ATOM   996  O  O   . SER A 1 123 ? 40.881  5.726   0.746   1.00 18.91 ? 123 SER A O   1 
ATOM   997  C  CB  . SER A 1 123 ? 39.708  3.968   2.974   1.00 13.75 ? 123 SER A CB  1 
ATOM   998  O  OG  . SER A 1 123 ? 39.857  2.636   2.609   1.00 13.95 ? 123 SER A OG  1 
ATOM   999  N  N   . ASP A 1 124 ? 39.577  4.283   -0.437  1.00 15.88 ? 124 ASP A N   1 
ATOM   1000 C  CA  . ASP A 1 124 ? 40.303  4.496   -1.750  1.00 18.22 ? 124 ASP A CA  1 
ATOM   1001 C  C   . ASP A 1 124 ? 39.964  5.861   -2.289  1.00 21.22 ? 124 ASP A C   1 
ATOM   1002 O  O   . ASP A 1 124 ? 40.816  6.560   -2.851  1.00 24.73 ? 124 ASP A O   1 
ATOM   1003 C  CB  . ASP A 1 124 ? 39.979  3.441   -2.778  1.00 17.63 ? 124 ASP A CB  1 
ATOM   1004 C  CG  . ASP A 1 124 ? 40.567  2.143   -2.485  1.00 15.67 ? 124 ASP A CG  1 
ATOM   1005 O  OD1 . ASP A 1 124 ? 41.595  2.055   -1.750  1.00 16.77 ? 124 ASP A OD1 1 
ATOM   1006 O  OD2 . ASP A 1 124 ? 40.075  1.148   -3.056  1.00 17.74 ? 124 ASP A OD2 1 
ATOM   1007 N  N   . LEU A 1 125 ? 38.713  6.268   -2.109  1.00 20.16 ? 125 LEU A N   1 
ATOM   1008 C  CA  . LEU A 1 125 ? 38.200  7.560   -2.648  1.00 22.29 ? 125 LEU A CA  1 
ATOM   1009 C  C   . LEU A 1 125 ? 38.124  8.740   -1.708  1.00 19.98 ? 125 LEU A C   1 
ATOM   1010 O  O   . LEU A 1 125 ? 38.216  9.892   -2.178  1.00 24.56 ? 125 LEU A O   1 
ATOM   1011 C  CB  . LEU A 1 125 ? 36.824  7.284   -3.275  1.00 22.33 ? 125 LEU A CB  1 
ATOM   1012 C  CG  . LEU A 1 125 ? 36.705  6.747   -4.718  1.00 26.61 ? 125 LEU A CG  1 
ATOM   1013 C  CD1 . LEU A 1 125 ? 37.962  6.142   -5.333  1.00 27.24 ? 125 LEU A CD1 1 
ATOM   1014 C  CD2 . LEU A 1 125 ? 35.482  5.868   -4.938  1.00 24.40 ? 125 LEU A CD2 1 
ATOM   1015 N  N   . TYR A 1 126 ? 37.906  8.497   -0.382  1.00 19.07 ? 126 TYR A N   1 
ATOM   1016 C  CA  . TYR A 1 126 ? 37.713  9.535   0.671   1.00 18.27 ? 126 TYR A CA  1 
ATOM   1017 C  C   . TYR A 1 126 ? 38.588  9.416   1.963   1.00 20.05 ? 126 TYR A C   1 
ATOM   1018 O  O   . TYR A 1 126 ? 38.989  8.325   2.354   1.00 21.67 ? 126 TYR A O   1 
ATOM   1019 C  CB  . TYR A 1 126 ? 36.223  9.608   1.139   1.00 19.85 ? 126 TYR A CB  1 
ATOM   1020 C  CG  . TYR A 1 126 ? 35.292  9.559   -0.051  1.00 22.18 ? 126 TYR A CG  1 
ATOM   1021 C  CD1 . TYR A 1 126 ? 35.213  10.621  -0.935  1.00 26.46 ? 126 TYR A CD1 1 
ATOM   1022 C  CD2 . TYR A 1 126 ? 34.526  8.396   -0.331  1.00 22.87 ? 126 TYR A CD2 1 
ATOM   1023 C  CE1 . TYR A 1 126 ? 34.404  10.532  -2.063  1.00 25.99 ? 126 TYR A CE1 1 
ATOM   1024 C  CE2 . TYR A 1 126 ? 33.722  8.289   -1.467  1.00 28.35 ? 126 TYR A CE2 1 
ATOM   1025 C  CZ  . TYR A 1 126 ? 33.644  9.360   -2.330  1.00 28.28 ? 126 TYR A CZ  1 
ATOM   1026 O  OH  . TYR A 1 126 ? 32.802  9.245   -3.437  1.00 34.72 ? 126 TYR A OH  1 
ATOM   1027 N  N   . PRO A 1 127 ? 38.906  10.549  2.618   1.00 21.95 ? 127 PRO A N   1 
ATOM   1028 C  CA  . PRO A 1 127 ? 39.874  10.481  3.701   1.00 23.71 ? 127 PRO A CA  1 
ATOM   1029 C  C   . PRO A 1 127 ? 39.339  9.954   5.008   1.00 24.09 ? 127 PRO A C   1 
ATOM   1030 O  O   . PRO A 1 127 ? 40.115  9.565   5.871   1.00 26.06 ? 127 PRO A O   1 
ATOM   1031 C  CB  . PRO A 1 127 ? 40.322  11.939  3.865   1.00 24.70 ? 127 PRO A CB  1 
ATOM   1032 C  CG  . PRO A 1 127 ? 39.100  12.708  3.504   1.00 20.20 ? 127 PRO A CG  1 
ATOM   1033 C  CD  . PRO A 1 127 ? 38.529  11.962  2.346   1.00 19.52 ? 127 PRO A CD  1 
ATOM   1034 N  N   . ASP A 1 128 ? 38.007  9.918   5.177   1.00 21.78 ? 128 ASP A N   1 
ATOM   1035 C  CA  . ASP A 1 128 ? 37.416  9.535   6.472   1.00 21.58 ? 128 ASP A CA  1 
ATOM   1036 C  C   . ASP A 1 128 ? 35.928  9.297   6.224   1.00 20.06 ? 128 ASP A C   1 
ATOM   1037 O  O   . ASP A 1 128 ? 35.433  9.697   5.154   1.00 19.99 ? 128 ASP A O   1 
ATOM   1038 C  CB  . ASP A 1 128 ? 37.620  10.598  7.551   1.00 25.16 ? 128 ASP A CB  1 
ATOM   1039 C  CG  . ASP A 1 128 ? 37.186  11.967  7.098   1.00 28.45 ? 128 ASP A CG  1 
ATOM   1040 O  OD1 . ASP A 1 128 ? 38.012  12.874  7.194   1.00 34.45 ? 128 ASP A OD1 1 
ATOM   1041 O  OD2 . ASP A 1 128 ? 36.047  12.172  6.679   1.00 27.01 ? 128 ASP A OD2 1 
ATOM   1042 N  N   . ALA A 1 129 ? 35.278  8.579   7.145   1.00 19.62 ? 129 ALA A N   1 
ATOM   1043 C  CA  . ALA A 1 129 ? 33.909  8.159   6.904   1.00 19.30 ? 129 ALA A CA  1 
ATOM   1044 C  C   . ALA A 1 129 ? 32.969  9.351   6.863   1.00 19.36 ? 129 ALA A C   1 
ATOM   1045 O  O   . ALA A 1 129 ? 32.017  9.327   6.081   1.00 19.01 ? 129 ALA A O   1 
ATOM   1046 C  CB  . ALA A 1 129 ? 33.465  7.196   7.994   1.00 19.10 ? 129 ALA A CB  1 
ATOM   1047 N  N   . SER A 1 130 ? 33.239  10.372  7.669   1.00 19.76 ? 130 SER A N   1 
ATOM   1048 C  CA  . SER A 1 130 ? 32.392  11.600  7.677   1.00 20.86 ? 130 SER A CA  1 
ATOM   1049 C  C   . SER A 1 130 ? 32.300  12.187  6.255   1.00 21.48 ? 130 SER A C   1 
ATOM   1050 O  O   . SER A 1 130 ? 31.213  12.410  5.690   1.00 20.35 ? 130 SER A O   1 
ATOM   1051 C  CB  . SER A 1 130 ? 32.932  12.534  8.788   1.00 23.62 ? 130 SER A CB  1 
ATOM   1052 O  OG  . SER A 1 130 ? 32.401  13.837  8.728   1.00 29.52 ? 130 SER A OG  1 
ATOM   1053 N  N   . THR A 1 131 ? 33.446  12.429  5.623   1.00 20.32 ? 131 THR A N   1 
ATOM   1054 C  CA  . THR A 1 131 ? 33.485  12.937  4.274   1.00 18.74 ? 131 THR A CA  1 
ATOM   1055 C  C   . THR A 1 131 ? 32.851  11.929  3.293   1.00 19.85 ? 131 THR A C   1 
ATOM   1056 O  O   . THR A 1 131 ? 32.205  12.292  2.327   1.00 19.55 ? 131 THR A O   1 
ATOM   1057 C  CB  . THR A 1 131 ? 34.961  13.271  3.902   1.00 20.24 ? 131 THR A CB  1 
ATOM   1058 O  OG1 . THR A 1 131 ? 35.512  14.090  4.931   1.00 22.88 ? 131 THR A OG1 1 
ATOM   1059 C  CG2 . THR A 1 131 ? 35.122  13.943  2.539   1.00 22.03 ? 131 THR A CG2 1 
ATOM   1060 N  N   . ALA A 1 132 ? 33.055  10.631  3.481   1.00 18.95 ? 132 ALA A N   1 
ATOM   1061 C  CA  . ALA A 1 132 ? 32.473  9.716   2.495   1.00 15.61 ? 132 ALA A CA  1 
ATOM   1062 C  C   . ALA A 1 132 ? 30.926  9.632   2.527   1.00 16.17 ? 132 ALA A C   1 
ATOM   1063 O  O   . ALA A 1 132 ? 30.332  9.242   1.565   1.00 18.82 ? 132 ALA A O   1 
ATOM   1064 C  CB  . ALA A 1 132 ? 32.955  8.285   2.772   1.00 17.39 ? 132 ALA A CB  1 
ATOM   1065 N  N   . SER A 1 133 ? 30.404  9.882   3.685   1.00 18.38 ? 133 SER A N   1 
ATOM   1066 C  CA  . SER A 1 133 ? 29.016  9.461   4.035   1.00 18.53 ? 133 SER A CA  1 
ATOM   1067 C  C   . SER A 1 133 ? 27.948  10.091  3.133   1.00 20.93 ? 133 SER A C   1 
ATOM   1068 O  O   . SER A 1 133 ? 26.824  9.522   2.978   1.00 18.70 ? 133 SER A O   1 
ATOM   1069 C  CB  . SER A 1 133 ? 28.725  9.819   5.496   1.00 17.32 ? 133 SER A CB  1 
ATOM   1070 O  OG  . SER A 1 133 ? 28.629  11.257  5.726   1.00 19.93 ? 133 SER A OG  1 
ATOM   1071 N  N   . ASN A 1 134 ? 28.254  11.247  2.553   1.00 23.27 ? 134 ASN A N   1 
ATOM   1072 C  CA  . ASN A 1 134 ? 27.327  11.867  1.600   1.00 23.97 ? 134 ASN A CA  1 
ATOM   1073 C  C   . ASN A 1 134 ? 27.776  11.816  0.141   1.00 23.12 ? 134 ASN A C   1 
ATOM   1074 O  O   . ASN A 1 134 ? 27.305  12.587  -0.712  1.00 26.46 ? 134 ASN A O   1 
ATOM   1075 C  CB  . ASN A 1 134 ? 26.930  13.277  2.047   1.00 26.91 ? 134 ASN A CB  1 
ATOM   1076 C  CG  . ASN A 1 134 ? 28.065  14.247  1.895   1.00 31.08 ? 134 ASN A CG  1 
ATOM   1077 O  OD1 . ASN A 1 134 ? 29.214  13.828  1.850   1.00 29.06 ? 134 ASN A OD1 1 
ATOM   1078 N  ND2 . ASN A 1 134 ? 27.751  15.569  1.782   1.00 30.04 ? 134 ASN A ND2 1 
ATOM   1079 N  N   . LYS A 1 135 ? 28.678  10.890  -0.165  1.00 19.16 ? 135 LYS A N   1 
ATOM   1080 C  CA  . LYS A 1 135 ? 29.179  10.724  -1.467  1.00 19.53 ? 135 LYS A CA  1 
ATOM   1081 C  C   . LYS A 1 135 ? 28.876  9.454   -2.107  1.00 20.96 ? 135 LYS A C   1 
ATOM   1082 O  O   . LYS A 1 135 ? 28.554  8.428   -1.482  1.00 19.47 ? 135 LYS A O   1 
ATOM   1083 C  CB  . LYS A 1 135 ? 30.708  10.934  -1.466  1.00 22.72 ? 135 LYS A CB  1 
ATOM   1084 C  CG  . LYS A 1 135 ? 31.017  12.213  -0.713  1.00 25.93 ? 135 LYS A CG  1 
ATOM   1085 C  CD  . LYS A 1 135 ? 31.957  13.128  -1.456  1.00 29.33 ? 135 LYS A CD  1 
ATOM   1086 C  CE  . LYS A 1 135 ? 32.184  14.457  -0.744  1.00 29.44 ? 135 LYS A CE  1 
ATOM   1087 N  NZ  . LYS A 1 135 ? 31.811  14.602  0.694   1.00 27.25 ? 135 LYS A NZ  1 
ATOM   1088 N  N   . SER A 1 136 ? 28.952  9.514   -3.426  1.00 23.54 ? 136 SER A N   1 
ATOM   1089 C  CA  . SER A 1 136 ? 28.714  8.366   -4.237  1.00 24.16 ? 136 SER A CA  1 
ATOM   1090 C  C   . SER A 1 136 ? 29.623  7.194   -3.824  1.00 25.12 ? 136 SER A C   1 
ATOM   1091 O  O   . SER A 1 136 ? 30.838  7.358   -3.682  1.00 27.96 ? 136 SER A O   1 
ATOM   1092 C  CB  . SER A 1 136 ? 28.986  8.744   -5.687  1.00 28.26 ? 136 SER A CB  1 
ATOM   1093 O  OG  . SER A 1 136 ? 28.452  7.756   -6.538  1.00 34.32 ? 136 SER A OG  1 
ATOM   1094 N  N   . GLU A 1 137 ? 29.023  6.023   -3.651  1.00 27.14 ? 137 GLU A N   1 
ATOM   1095 C  CA  . GLU A 1 137 ? 29.799  4.836   -3.233  1.00 25.41 ? 137 GLU A CA  1 
ATOM   1096 C  C   . GLU A 1 137 ? 30.486  4.992   -1.875  1.00 22.84 ? 137 GLU A C   1 
ATOM   1097 O  O   . GLU A 1 137 ? 31.499  4.266   -1.617  1.00 21.89 ? 137 GLU A O   1 
ATOM   1098 C  CB  . GLU A 1 137 ? 30.866  4.463   -4.289  1.00 32.51 ? 137 GLU A CB  1 
ATOM   1099 C  CG  . GLU A 1 137 ? 30.365  4.415   -5.729  1.00 44.74 ? 137 GLU A CG  1 
ATOM   1100 C  CD  . GLU A 1 137 ? 29.749  3.086   -6.124  1.00 53.06 ? 137 GLU A CD  1 
ATOM   1101 O  OE1 . GLU A 1 137 ? 30.510  2.140   -6.456  1.00 62.09 ? 137 GLU A OE1 1 
ATOM   1102 O  OE2 . GLU A 1 137 ? 28.502  2.999   -6.132  1.00 62.26 ? 137 GLU A OE2 1 
ATOM   1103 N  N   . GLY A 1 138 ? 29.998  5.875   -0.977  1.00 17.54 ? 138 GLY A N   1 
ATOM   1104 C  CA  . GLY A 1 138 ? 30.799  6.292   0.150   1.00 17.02 ? 138 GLY A CA  1 
ATOM   1105 C  C   . GLY A 1 138 ? 30.920  5.232   1.252   1.00 15.94 ? 138 GLY A C   1 
ATOM   1106 O  O   . GLY A 1 138 ? 31.976  5.148   1.922   1.00 14.59 ? 138 GLY A O   1 
ATOM   1107 N  N   . LEU A 1 139 ? 29.819  4.473   1.492   1.00 13.53 ? 139 LEU A N   1 
ATOM   1108 C  CA  . LEU A 1 139 ? 29.795  3.582   2.666   1.00 12.22 ? 139 LEU A CA  1 
ATOM   1109 C  C   . LEU A 1 139 ? 29.389  2.141   2.332   1.00 11.39 ? 139 LEU A C   1 
ATOM   1110 O  O   . LEU A 1 139 ? 28.758  1.843   1.329   1.00 11.76 ? 139 LEU A O   1 
ATOM   1111 C  CB  . LEU A 1 139 ? 28.751  4.085   3.666   1.00 11.58 ? 139 LEU A CB  1 
ATOM   1112 C  CG  . LEU A 1 139 ? 29.010  5.564   4.182   1.00 13.65 ? 139 LEU A CG  1 
ATOM   1113 C  CD1 . LEU A 1 139 ? 27.783  6.007   4.993   1.00 14.64 ? 139 LEU A CD1 1 
ATOM   1114 C  CD2 . LEU A 1 139 ? 30.349  5.639   4.958   1.00 14.20 ? 139 LEU A CD2 1 
ATOM   1115 N  N   . ALA A 1 140 ? 29.833  1.276   3.212   1.00 10.93 ? 140 ALA A N   1 
ATOM   1116 C  CA  . ALA A 1 140 ? 29.413  -0.106  3.120   1.00 10.16 ? 140 ALA A CA  1 
ATOM   1117 C  C   . ALA A 1 140 ? 29.134  -0.588  4.507   1.00 10.83 ? 140 ALA A C   1 
ATOM   1118 O  O   . ALA A 1 140 ? 29.954  -0.403  5.380   1.00 10.63 ? 140 ALA A O   1 
ATOM   1119 C  CB  . ALA A 1 140 ? 30.479  -0.996  2.457   1.00 12.69 ? 140 ALA A CB  1 
ATOM   1120 N  N   . VAL A 1 141 ? 27.974  -1.229  4.771   1.00 9.91  ? 141 VAL A N   1 
ATOM   1121 C  CA  . VAL A 1 141 ? 27.755  -1.685  6.125   1.00 10.17 ? 141 VAL A CA  1 
ATOM   1122 C  C   . VAL A 1 141 ? 27.500  -3.202  6.114   1.00 10.14 ? 141 VAL A C   1 
ATOM   1123 O  O   . VAL A 1 141 ? 26.830  -3.681  5.198   1.00 12.53 ? 141 VAL A O   1 
ATOM   1124 C  CB  . VAL A 1 141 ? 26.472  -1.000  6.735   1.00 9.17  ? 141 VAL A CB  1 
ATOM   1125 C  CG1 . VAL A 1 141 ? 26.229  -1.501  8.179   1.00 9.46  ? 141 VAL A CG1 1 
ATOM   1126 C  CG2 . VAL A 1 141 ? 26.647  0.535   6.794   1.00 9.92  ? 141 VAL A CG2 1 
ATOM   1127 N  N   . LEU A 1 142 ? 28.115  -3.931  7.044   1.00 10.19 ? 142 LEU A N   1 
ATOM   1128 C  CA  . LEU A 1 142 ? 27.816  -5.316  7.174   1.00 9.30  ? 142 LEU A CA  1 
ATOM   1129 C  C   . LEU A 1 142 ? 26.750  -5.413  8.262   1.00 8.45  ? 142 LEU A C   1 
ATOM   1130 O  O   . LEU A 1 142 ? 26.964  -4.871  9.328   1.00 9.89  ? 142 LEU A O   1 
ATOM   1131 C  CB  . LEU A 1 142 ? 29.056  -6.088  7.686   1.00 10.88 ? 142 LEU A CB  1 
ATOM   1132 C  CG  . LEU A 1 142 ? 30.243  -6.040  6.713   1.00 11.40 ? 142 LEU A CG  1 
ATOM   1133 C  CD1 . LEU A 1 142 ? 31.364  -6.912  7.259   1.00 12.48 ? 142 LEU A CD1 1 
ATOM   1134 C  CD2 . LEU A 1 142 ? 29.878  -6.537  5.346   1.00 11.21 ? 142 LEU A CD2 1 
ATOM   1135 N  N   . ALA A 1 143 ? 25.749  -6.289  8.033   1.00 9.11  ? 143 ALA A N   1 
ATOM   1136 C  CA  . ALA A 1 143 ? 24.703  -6.475  9.069   1.00 9.29  ? 143 ALA A CA  1 
ATOM   1137 C  C   . ALA A 1 143 ? 24.599  -7.961  9.414   1.00 8.86  ? 143 ALA A C   1 
ATOM   1138 O  O   . ALA A 1 143 ? 24.541  -8.923  8.573   1.00 9.91  ? 143 ALA A O   1 
ATOM   1139 C  CB  . ALA A 1 143 ? 23.369  -5.960  8.536   1.00 11.34 ? 143 ALA A CB  1 
ATOM   1140 N  N   . VAL A 1 144 ? 24.583  -8.146  10.758  1.00 8.79  ? 144 VAL A N   1 
ATOM   1141 C  CA  . VAL A 1 144 ? 24.475  -9.508  11.314  1.00 10.05 ? 144 VAL A CA  1 
ATOM   1142 C  C   . VAL A 1 144 ? 23.133  -9.555  12.088  1.00 10.88 ? 144 VAL A C   1 
ATOM   1143 O  O   . VAL A 1 144 ? 22.883  -8.730  13.024  1.00 10.58 ? 144 VAL A O   1 
ATOM   1144 C  CB  . VAL A 1 144 ? 25.621  -9.861  12.287  1.00 9.97  ? 144 VAL A CB  1 
ATOM   1145 C  CG1 . VAL A 1 144 ? 25.433  -11.281 12.893  1.00 11.49 ? 144 VAL A CG1 1 
ATOM   1146 C  CG2 . VAL A 1 144 ? 26.943  -9.862  11.502  1.00 10.49 ? 144 VAL A CG2 1 
ATOM   1147 N  N   . LEU A 1 145 ? 22.276  -10.512 11.681  1.00 10.40 ? 145 LEU A N   1 
ATOM   1148 C  CA  . LEU A 1 145 ? 20.994  -10.752 12.428  1.00 10.91 ? 145 LEU A CA  1 
ATOM   1149 C  C   . LEU A 1 145 ? 21.258  -11.530 13.700  1.00 11.03 ? 145 LEU A C   1 
ATOM   1150 O  O   . LEU A 1 145 ? 22.062  -12.445 13.667  1.00 11.25 ? 145 LEU A O   1 
ATOM   1151 C  CB  . LEU A 1 145 ? 19.959  -11.410 11.492  1.00 11.06 ? 145 LEU A CB  1 
ATOM   1152 C  CG  . LEU A 1 145 ? 19.690  -10.689 10.129  1.00 12.25 ? 145 LEU A CG  1 
ATOM   1153 C  CD1 . LEU A 1 145 ? 19.003  -11.606 9.122   1.00 13.09 ? 145 LEU A CD1 1 
ATOM   1154 C  CD2 . LEU A 1 145 ? 18.749  -9.483  10.492  1.00 12.50 ? 145 LEU A CD2 1 
ATOM   1155 N  N   . ILE A 1 146 ? 20.558  -11.217 14.791  1.00 9.88  ? 146 ILE A N   1 
ATOM   1156 C  CA  . ILE A 1 146 ? 20.830  -11.795 16.112  1.00 10.92 ? 146 ILE A CA  1 
ATOM   1157 C  C   . ILE A 1 146 ? 19.536  -12.412 16.622  1.00 11.46 ? 146 ILE A C   1 
ATOM   1158 O  O   . ILE A 1 146 ? 18.532  -11.712 16.647  1.00 12.56 ? 146 ILE A O   1 
ATOM   1159 C  CB  . ILE A 1 146 ? 21.321  -10.742 17.125  1.00 10.26 ? 146 ILE A CB  1 
ATOM   1160 C  CG1 . ILE A 1 146 ? 22.711  -10.180 16.661  1.00 11.77 ? 146 ILE A CG1 1 
ATOM   1161 C  CG2 . ILE A 1 146 ? 21.572  -11.425 18.545  1.00 11.68 ? 146 ILE A CG2 1 
ATOM   1162 C  CD1 . ILE A 1 146 ? 23.109  -8.906  17.414  1.00 10.96 ? 146 ILE A CD1 1 
ATOM   1163 N  N   . GLU A 1 147 ? 19.592  -13.681 17.003  1.00 11.82 ? 147 GLU A N   1 
ATOM   1164 C  CA  . GLU A 1 147 ? 18.438  -14.398 17.628  1.00 13.21 ? 147 GLU A CA  1 
ATOM   1165 C  C   . GLU A 1 147 ? 18.825  -14.890 19.009  1.00 13.45 ? 147 GLU A C   1 
ATOM   1166 O  O   . GLU A 1 147 ? 20.003  -15.044 19.286  1.00 12.66 ? 147 GLU A O   1 
ATOM   1167 C  CB  . GLU A 1 147 ? 17.902  -15.543 16.766  1.00 15.51 ? 147 GLU A CB  1 
ATOM   1168 C  CG  . GLU A 1 147 ? 18.828  -16.751 16.583  1.00 16.19 ? 147 GLU A CG  1 
ATOM   1169 C  CD  . GLU A 1 147 ? 18.421  -17.723 15.494  1.00 19.56 ? 147 GLU A CD  1 
ATOM   1170 O  OE1 . GLU A 1 147 ? 17.410  -17.532 14.768  1.00 20.70 ? 147 GLU A OE1 1 
ATOM   1171 O  OE2 . GLU A 1 147 ? 19.136  -18.738 15.371  1.00 20.29 ? 147 GLU A OE2 1 
ATOM   1172 N  N   . MET A 1 148 ? 17.847  -15.095 19.877  1.00 15.12 ? 148 MET A N   1 
ATOM   1173 C  CA  . MET A 1 148 ? 18.109  -15.713 21.142  1.00 18.31 ? 148 MET A CA  1 
ATOM   1174 C  C   . MET A 1 148 ? 18.458  -17.273 21.028  1.00 17.27 ? 148 MET A C   1 
ATOM   1175 O  O   . MET A 1 148 ? 17.862  -18.091 20.272  1.00 18.84 ? 148 MET A O   1 
ATOM   1176 C  CB  . MET A 1 148 ? 16.893  -15.413 22.039  1.00 19.68 ? 148 MET A CB  1 
ATOM   1177 C  CG  . MET A 1 148 ? 17.294  -15.619 23.486  1.00 23.29 ? 148 MET A CG  1 
ATOM   1178 S  SD  . MET A 1 148 ? 17.020  -17.312 24.047  1.00 28.85 ? 148 MET A SD  1 
ATOM   1179 C  CE  . MET A 1 148 ? 15.203  -17.361 24.079  1.00 25.35 ? 148 MET A CE  1 
ATOM   1180 N  N   . GLY A 1 149 ? 19.528  -17.690 21.689  1.00 16.57 ? 149 GLY A N   1 
ATOM   1181 C  CA  . GLY A 1 149 ? 19.918  -19.105 21.718  1.00 18.72 ? 149 GLY A CA  1 
ATOM   1182 C  C   . GLY A 1 149 ? 20.976  -19.288 22.794  1.00 15.46 ? 149 GLY A C   1 
ATOM   1183 O  O   . GLY A 1 149 ? 20.822  -18.842 23.921  1.00 16.32 ? 149 GLY A O   1 
ATOM   1184 N  N   A SER A 1 150 ? 22.101  -19.888 22.393  0.50 17.35 ? 150 SER A N   1 
ATOM   1185 N  N   B SER A 1 150 ? 22.079  -19.943 22.432  0.50 16.78 ? 150 SER A N   1 
ATOM   1186 C  CA  A SER A 1 150 ? 23.229  -20.094 23.278  0.50 17.05 ? 150 SER A CA  1 
ATOM   1187 C  CA  B SER A 1 150 ? 23.140  -20.187 23.380  0.50 16.26 ? 150 SER A CA  1 
ATOM   1188 C  C   A SER A 1 150 ? 23.982  -18.841 23.647  0.50 16.26 ? 150 SER A C   1 
ATOM   1189 C  C   B SER A 1 150 ? 23.973  -18.935 23.640  0.50 15.79 ? 150 SER A C   1 
ATOM   1190 O  O   A SER A 1 150 ? 24.102  -17.892 22.866  0.50 15.70 ? 150 SER A O   1 
ATOM   1191 O  O   B SER A 1 150 ? 24.101  -18.064 22.765  0.50 15.61 ? 150 SER A O   1 
ATOM   1192 C  CB  A SER A 1 150 ? 24.234  -21.075 22.658  0.50 19.73 ? 150 SER A CB  1 
ATOM   1193 C  CB  B SER A 1 150 ? 24.058  -21.306 22.874  0.50 18.01 ? 150 SER A CB  1 
ATOM   1194 O  OG  A SER A 1 150 ? 23.513  -22.178 22.172  0.50 20.34 ? 150 SER A OG  1 
ATOM   1195 O  OG  B SER A 1 150 ? 24.572  -20.950 21.598  0.50 16.51 ? 150 SER A OG  1 
ATOM   1196 N  N   . PHE A 1 151 ? 24.499  -18.852 24.863  1.00 15.05 ? 151 PHE A N   1 
ATOM   1197 C  CA  . PHE A 1 151 ? 25.427  -17.782 25.307  1.00 15.46 ? 151 PHE A CA  1 
ATOM   1198 C  C   . PHE A 1 151 ? 26.570  -17.573 24.283  1.00 16.60 ? 151 PHE A C   1 
ATOM   1199 O  O   . PHE A 1 151 ? 27.208  -18.535 23.782  1.00 16.41 ? 151 PHE A O   1 
ATOM   1200 C  CB  . PHE A 1 151 ? 25.970  -18.091 26.732  1.00 16.70 ? 151 PHE A CB  1 
ATOM   1201 C  CG  . PHE A 1 151 ? 26.950  -17.123 27.213  1.00 16.91 ? 151 PHE A CG  1 
ATOM   1202 C  CD1 . PHE A 1 151 ? 26.544  -15.857 27.713  1.00 15.52 ? 151 PHE A CD1 1 
ATOM   1203 C  CD2 . PHE A 1 151 ? 28.321  -17.392 27.123  1.00 17.18 ? 151 PHE A CD2 1 
ATOM   1204 C  CE1 . PHE A 1 151 ? 27.508  -14.916 28.127  1.00 15.25 ? 151 PHE A CE1 1 
ATOM   1205 C  CE2 . PHE A 1 151 ? 29.247  -16.439 27.535  1.00 17.35 ? 151 PHE A CE2 1 
ATOM   1206 C  CZ  . PHE A 1 151 ? 28.879  -15.188 28.015  1.00 15.56 ? 151 PHE A CZ  1 
ATOM   1207 N  N   . ASN A 1 152 ? 26.820  -16.323 23.968  1.00 14.60 ? 152 ASN A N   1 
ATOM   1208 C  CA  . ASN A 1 152 ? 27.890  -15.978 23.045  1.00 15.69 ? 152 ASN A CA  1 
ATOM   1209 C  C   . ASN A 1 152 ? 29.065  -15.241 23.702  1.00 13.98 ? 152 ASN A C   1 
ATOM   1210 O  O   . ASN A 1 152 ? 29.047  -14.022 23.954  1.00 14.67 ? 152 ASN A O   1 
ATOM   1211 C  CB  . ASN A 1 152 ? 27.286  -15.125 21.875  1.00 14.00 ? 152 ASN A CB  1 
ATOM   1212 C  CG  . ASN A 1 152 ? 28.201  -15.075 20.646  1.00 13.01 ? 152 ASN A CG  1 
ATOM   1213 O  OD1 . ASN A 1 152 ? 29.373  -14.786 20.726  1.00 13.66 ? 152 ASN A OD1 1 
ATOM   1214 N  ND2 . ASN A 1 152 ? 27.628  -15.276 19.523  1.00 13.13 ? 152 ASN A ND2 1 
ATOM   1215 N  N   . PRO A 1 153 ? 30.183  -15.990 23.968  1.00 16.31 ? 153 PRO A N   1 
ATOM   1216 C  CA  . PRO A 1 153 ? 31.410  -15.412 24.508  1.00 16.94 ? 153 PRO A CA  1 
ATOM   1217 C  C   . PRO A 1 153 ? 31.894  -14.191 23.735  1.00 16.04 ? 153 PRO A C   1 
ATOM   1218 O  O   . PRO A 1 153 ? 32.402  -13.223 24.310  1.00 16.20 ? 153 PRO A O   1 
ATOM   1219 C  CB  . PRO A 1 153 ? 32.424  -16.572 24.324  1.00 19.48 ? 153 PRO A CB  1 
ATOM   1220 C  CG  . PRO A 1 153 ? 31.538  -17.780 24.502  1.00 21.77 ? 153 PRO A CG  1 
ATOM   1221 C  CD  . PRO A 1 153 ? 30.309  -17.440 23.699  1.00 17.07 ? 153 PRO A CD  1 
ATOM   1222 N  N   . SER A 1 154 ? 31.768  -14.249 22.419  1.00 14.69 ? 154 SER A N   1 
ATOM   1223 C  CA  . SER A 1 154 ? 32.402  -13.145 21.685  1.00 15.74 ? 154 SER A CA  1 
ATOM   1224 C  C   . SER A 1 154 ? 31.589  -11.883 21.842  1.00 13.83 ? 154 SER A C   1 
ATOM   1225 O  O   . SER A 1 154 ? 32.148  -10.792 21.974  1.00 14.92 ? 154 SER A O   1 
ATOM   1226 C  CB  . SER A 1 154 ? 32.527  -13.482 20.242  1.00 16.16 ? 154 SER A CB  1 
ATOM   1227 O  OG  . SER A 1 154 ? 33.404  -14.631 20.093  1.00 18.62 ? 154 SER A OG  1 
ATOM   1228 N  N   . TYR A 1 155 ? 30.261  -12.013 21.717  1.00 13.98 ? 155 TYR A N   1 
ATOM   1229 C  CA  . TYR A 1 155 ? 29.448  -10.787 21.953  1.00 12.03 ? 155 TYR A CA  1 
ATOM   1230 C  C   . TYR A 1 155 ? 29.622  -10.256 23.347  1.00 14.27 ? 155 TYR A C   1 
ATOM   1231 O  O   . TYR A 1 155 ? 29.536  -9.032  23.631  1.00 13.22 ? 155 TYR A O   1 
ATOM   1232 C  CB  . TYR A 1 155 ? 27.957  -11.073 21.606  1.00 12.58 ? 155 TYR A CB  1 
ATOM   1233 C  CG  . TYR A 1 155 ? 27.702  -10.882 20.100  1.00 12.65 ? 155 TYR A CG  1 
ATOM   1234 C  CD1 . TYR A 1 155 ? 27.119  -9.697  19.624  1.00 12.96 ? 155 TYR A CD1 1 
ATOM   1235 C  CD2 . TYR A 1 155 ? 28.046  -11.821 19.171  1.00 12.88 ? 155 TYR A CD2 1 
ATOM   1236 C  CE1 . TYR A 1 155 ? 26.890  -9.505  18.261  1.00 12.34 ? 155 TYR A CE1 1 
ATOM   1237 C  CE2 . TYR A 1 155 ? 27.799  -11.625 17.787  1.00 10.70 ? 155 TYR A CE2 1 
ATOM   1238 C  CZ  . TYR A 1 155 ? 27.245  -10.427 17.348  1.00 12.62 ? 155 TYR A CZ  1 
ATOM   1239 O  OH  . TYR A 1 155 ? 26.999  -10.223 15.993  1.00 12.08 ? 155 TYR A OH  1 
ATOM   1240 N  N   . ASP A 1 156 ? 29.939  -11.146 24.266  1.00 13.99 ? 156 ASP A N   1 
ATOM   1241 C  CA  . ASP A 1 156 ? 30.154  -10.684 25.638  1.00 14.91 ? 156 ASP A CA  1 
ATOM   1242 C  C   . ASP A 1 156 ? 31.397  -9.820  25.837  1.00 15.90 ? 156 ASP A C   1 
ATOM   1243 O  O   . ASP A 1 156 ? 31.457  -9.026  26.817  1.00 18.72 ? 156 ASP A O   1 
ATOM   1244 C  CB  . ASP A 1 156 ? 30.035  -11.837 26.608  1.00 18.07 ? 156 ASP A CB  1 
ATOM   1245 C  CG  . ASP A 1 156 ? 29.016  -11.470 27.762  1.00 19.90 ? 156 ASP A CG  1 
ATOM   1246 O  OD1 . ASP A 1 156 ? 27.841  -10.979 27.483  1.00 17.07 ? 156 ASP A OD1 1 
ATOM   1247 O  OD2 . ASP A 1 156 ? 29.422  -11.517 28.941  1.00 24.62 ? 156 ASP A OD2 1 
ATOM   1248 N  N   . LYS A 1 157 ? 32.286  -9.853  24.845  1.00 14.15 ? 157 LYS A N   1 
ATOM   1249 C  CA  . LYS A 1 157 ? 33.442  -8.972  24.849  1.00 15.80 ? 157 LYS A CA  1 
ATOM   1250 C  C   . LYS A 1 157 ? 33.016  -7.525  24.758  1.00 16.92 ? 157 LYS A C   1 
ATOM   1251 O  O   . LYS A 1 157 ? 33.745  -6.624  25.189  1.00 20.37 ? 157 LYS A O   1 
ATOM   1252 C  CB  . LYS A 1 157 ? 34.516  -9.336  23.810  1.00 14.70 ? 157 LYS A CB  1 
ATOM   1253 C  CG  . LYS A 1 157 ? 35.057  -10.752 24.097  1.00 17.11 ? 157 LYS A CG  1 
ATOM   1254 C  CD  . LYS A 1 157 ? 35.912  -11.346 23.009  1.00 18.88 ? 157 LYS A CD  1 
ATOM   1255 C  CE  . LYS A 1 157 ? 36.368  -12.782 23.314  1.00 22.53 ? 157 LYS A CE  1 
ATOM   1256 N  NZ  . LYS A 1 157 ? 37.265  -13.287 22.228  1.00 23.43 ? 157 LYS A NZ  1 
ATOM   1257 N  N   . ILE A 1 158 ? 31.855  -7.294  24.144  1.00 15.47 ? 158 ILE A N   1 
ATOM   1258 C  CA  . ILE A 1 158 ? 31.302  -5.911  24.116  1.00 15.78 ? 158 ILE A CA  1 
ATOM   1259 C  C   . ILE A 1 158 ? 30.365  -5.713  25.270  1.00 15.74 ? 158 ILE A C   1 
ATOM   1260 O  O   . ILE A 1 158 ? 30.481  -4.755  26.007  1.00 17.27 ? 158 ILE A O   1 
ATOM   1261 C  CB  . ILE A 1 158 ? 30.563  -5.596  22.791  1.00 16.77 ? 158 ILE A CB  1 
ATOM   1262 C  CG1 . ILE A 1 158 ? 31.461  -5.814  21.555  1.00 17.43 ? 158 ILE A CG1 1 
ATOM   1263 C  CG2 . ILE A 1 158 ? 29.996  -4.138  22.810  1.00 17.77 ? 158 ILE A CG2 1 
ATOM   1264 C  CD1 . ILE A 1 158 ? 30.768  -5.755  20.204  1.00 16.68 ? 158 ILE A CD1 1 
ATOM   1265 N  N   . PHE A 1 159 ? 29.427  -6.644  25.406  1.00 14.47 ? 159 PHE A N   1 
ATOM   1266 C  CA  . PHE A 1 159 ? 28.344  -6.475  26.355  1.00 15.31 ? 159 PHE A CA  1 
ATOM   1267 C  C   . PHE A 1 159 ? 28.826  -6.362  27.776  1.00 15.92 ? 159 PHE A C   1 
ATOM   1268 O  O   . PHE A 1 159 ? 28.189  -5.647  28.531  1.00 16.52 ? 159 PHE A O   1 
ATOM   1269 C  CB  . PHE A 1 159 ? 27.353  -7.619  26.303  1.00 15.45 ? 159 PHE A CB  1 
ATOM   1270 C  CG  . PHE A 1 159 ? 26.610  -7.755  24.977  1.00 17.10 ? 159 PHE A CG  1 
ATOM   1271 C  CD1 . PHE A 1 159 ? 26.526  -6.729  24.027  1.00 16.90 ? 159 PHE A CD1 1 
ATOM   1272 C  CD2 . PHE A 1 159 ? 25.886  -8.964  24.740  1.00 17.22 ? 159 PHE A CD2 1 
ATOM   1273 C  CE1 . PHE A 1 159 ? 25.804  -6.963  22.821  1.00 15.54 ? 159 PHE A CE1 1 
ATOM   1274 C  CE2 . PHE A 1 159 ? 25.170  -9.160  23.590  1.00 16.58 ? 159 PHE A CE2 1 
ATOM   1275 C  CZ  . PHE A 1 159 ? 25.126  -8.185  22.629  1.00 15.32 ? 159 PHE A CZ  1 
ATOM   1276 N  N   . SER A 1 160 ? 29.955  -7.009  28.104  1.00 15.48 ? 160 SER A N   1 
ATOM   1277 C  CA  . SER A 1 160 ? 30.476  -6.854  29.505  1.00 17.09 ? 160 SER A CA  1 
ATOM   1278 C  C   . SER A 1 160 ? 30.876  -5.399  29.888  1.00 18.81 ? 160 SER A C   1 
ATOM   1279 O  O   . SER A 1 160 ? 31.098  -5.089  31.067  1.00 22.19 ? 160 SER A O   1 
ATOM   1280 C  CB  . SER A 1 160 ? 31.629  -7.842  29.729  1.00 16.12 ? 160 SER A CB  1 
ATOM   1281 O  OG  . SER A 1 160 ? 32.793  -7.391  29.088  1.00 18.73 ? 160 SER A OG  1 
ATOM   1282 N  N   . HIS A 1 161 ? 31.002  -4.522  28.891  1.00 17.88 ? 161 HIS A N   1 
ATOM   1283 C  CA  . HIS A 1 161 ? 31.288  -3.110  29.153  1.00 19.66 ? 161 HIS A CA  1 
ATOM   1284 C  C   . HIS A 1 161 ? 30.133  -2.200  29.174  1.00 20.12 ? 161 HIS A C   1 
ATOM   1285 O  O   . HIS A 1 161 ? 30.314  -1.007  29.452  1.00 18.98 ? 161 HIS A O   1 
ATOM   1286 C  CB  . HIS A 1 161 ? 32.277  -2.613  28.125  1.00 18.85 ? 161 HIS A CB  1 
ATOM   1287 C  CG  . HIS A 1 161 ? 33.589  -3.327  28.173  1.00 20.08 ? 161 HIS A CG  1 
ATOM   1288 N  ND1 . HIS A 1 161 ? 34.682  -2.818  28.818  1.00 21.31 ? 161 HIS A ND1 1 
ATOM   1289 C  CD2 . HIS A 1 161 ? 34.001  -4.555  27.601  1.00 21.17 ? 161 HIS A CD2 1 
ATOM   1290 C  CE1 . HIS A 1 161 ? 35.731  -3.698  28.726  1.00 22.17 ? 161 HIS A CE1 1 
ATOM   1291 N  NE2 . HIS A 1 161 ? 35.315  -4.768  27.995  1.00 21.99 ? 161 HIS A NE2 1 
ATOM   1292 N  N   . LEU A 1 162 ? 28.938  -2.713  28.850  1.00 18.70 ? 162 LEU A N   1 
ATOM   1293 C  CA  . LEU A 1 162 ? 27.783  -1.866  28.769  1.00 19.17 ? 162 LEU A CA  1 
ATOM   1294 C  C   . LEU A 1 162 ? 27.469  -1.078  30.060  1.00 20.73 ? 162 LEU A C   1 
ATOM   1295 O  O   . LEU A 1 162 ? 27.000  0.049   29.966  1.00 20.90 ? 162 LEU A O   1 
ATOM   1296 C  CB  . LEU A 1 162 ? 26.516  -2.643  28.368  1.00 20.41 ? 162 LEU A CB  1 
ATOM   1297 C  CG  . LEU A 1 162 ? 26.522  -3.149  26.926  1.00 20.62 ? 162 LEU A CG  1 
ATOM   1298 C  CD1 . LEU A 1 162 ? 25.308  -4.057  26.675  1.00 21.64 ? 162 LEU A CD1 1 
ATOM   1299 C  CD2 . LEU A 1 162 ? 26.705  -2.035  25.893  1.00 22.28 ? 162 LEU A CD2 1 
ATOM   1300 N  N   . GLN A 1 163 ? 27.710  -1.664  31.231  1.00 24.50 ? 163 GLN A N   1 
ATOM   1301 C  CA  . GLN A 1 163 ? 27.311  -0.900  32.418  1.00 26.77 ? 163 GLN A CA  1 
ATOM   1302 C  C   . GLN A 1 163 ? 28.141  0.378   32.619  1.00 27.31 ? 163 GLN A C   1 
ATOM   1303 O  O   . GLN A 1 163 ? 27.643  1.298   33.251  1.00 28.70 ? 163 GLN A O   1 
ATOM   1304 C  CB  . GLN A 1 163 ? 27.213  -1.740  33.682  1.00 29.92 ? 163 GLN A CB  1 
ATOM   1305 C  CG  . GLN A 1 163 ? 28.562  -1.995  34.316  1.00 34.81 ? 163 GLN A CG  1 
ATOM   1306 C  CD  . GLN A 1 163 ? 29.401  -2.920  33.472  1.00 42.18 ? 163 GLN A CD  1 
ATOM   1307 O  OE1 . GLN A 1 163 ? 28.950  -4.016  33.101  1.00 52.55 ? 163 GLN A OE1 1 
ATOM   1308 N  NE2 . GLN A 1 163 ? 30.631  -2.512  33.180  1.00 35.64 ? 163 GLN A NE2 1 
ATOM   1309 N  N   . HIS A 1 164 ? 29.323  0.465   32.000  1.00 20.49 ? 164 HIS A N   1 
ATOM   1310 C  CA  . HIS A 1 164 ? 30.150  1.680   32.008  1.00 21.17 ? 164 HIS A CA  1 
ATOM   1311 C  C   . HIS A 1 164 ? 29.753  2.751   31.029  1.00 19.47 ? 164 HIS A C   1 
ATOM   1312 O  O   . HIS A 1 164 ? 30.342  3.843   31.060  1.00 19.36 ? 164 HIS A O   1 
ATOM   1313 C  CB  . HIS A 1 164 ? 31.626  1.323   31.758  1.00 20.95 ? 164 HIS A CB  1 
ATOM   1314 C  CG  . HIS A 1 164 ? 32.265  0.452   32.834  1.00 22.59 ? 164 HIS A CG  1 
ATOM   1315 N  ND1 . HIS A 1 164 ? 31.932  0.542   34.120  1.00 22.31 ? 164 HIS A ND1 1 
ATOM   1316 C  CD2 . HIS A 1 164 ? 33.278  -0.481  32.763  1.00 25.42 ? 164 HIS A CD2 1 
ATOM   1317 C  CE1 . HIS A 1 164 ? 32.645  -0.346  34.850  1.00 23.31 ? 164 HIS A CE1 1 
ATOM   1318 N  NE2 . HIS A 1 164 ? 33.476  -0.961  34.037  1.00 28.34 ? 164 HIS A NE2 1 
ATOM   1319 N  N   . VAL A 1 165 ? 28.834  2.439   30.088  1.00 17.41 ? 165 VAL A N   1 
ATOM   1320 C  CA  . VAL A 1 165 ? 28.358  3.426   29.116  1.00 17.13 ? 165 VAL A CA  1 
ATOM   1321 C  C   . VAL A 1 165 ? 26.845  3.553   29.215  1.00 17.46 ? 165 VAL A C   1 
ATOM   1322 O  O   . VAL A 1 165 ? 26.184  3.835   28.226  1.00 18.03 ? 165 VAL A O   1 
ATOM   1323 C  CB  . VAL A 1 165 ? 28.812  3.118   27.646  1.00 16.46 ? 165 VAL A CB  1 
ATOM   1324 C  CG1 . VAL A 1 165 ? 30.334  3.362   27.540  1.00 17.05 ? 165 VAL A CG1 1 
ATOM   1325 C  CG2 . VAL A 1 165 ? 28.438  1.668   27.163  1.00 16.04 ? 165 VAL A CG2 1 
ATOM   1326 N  N   . LYS A 1 166 ? 26.314  3.380   30.435  1.00 18.95 ? 166 LYS A N   1 
ATOM   1327 C  CA  . LYS A 1 166 ? 24.862  3.487   30.701  1.00 18.59 ? 166 LYS A CA  1 
ATOM   1328 C  C   . LYS A 1 166 ? 24.225  4.778   30.197  1.00 19.21 ? 166 LYS A C   1 
ATOM   1329 O  O   . LYS A 1 166 ? 23.137  4.743   29.693  1.00 18.75 ? 166 LYS A O   1 
ATOM   1330 C  CB  . LYS A 1 166 ? 24.626  3.335   32.208  1.00 20.54 ? 166 LYS A CB  1 
ATOM   1331 C  CG  . LYS A 1 166 ? 23.206  3.277   32.747  1.00 20.57 ? 166 LYS A CG  1 
ATOM   1332 C  CD  . LYS A 1 166 ? 23.193  2.893   34.258  1.00 25.95 ? 166 LYS A CD  1 
ATOM   1333 C  CE  . LYS A 1 166 ? 23.377  1.372   34.434  1.00 28.56 ? 166 LYS A CE  1 
ATOM   1334 N  NZ  . LYS A 1 166 ? 24.810  0.905   34.417  1.00 32.81 ? 166 LYS A NZ  1 
ATOM   1335 N  N   . TYR A 1 167 ? 24.889  5.942   30.372  1.00 17.95 ? 167 TYR A N   1 
ATOM   1336 C  CA  . TYR A 1 167 ? 24.215  7.215   30.025  1.00 17.59 ? 167 TYR A CA  1 
ATOM   1337 C  C   . TYR A 1 167 ? 24.874  7.912   28.865  1.00 17.90 ? 167 TYR A C   1 
ATOM   1338 O  O   . TYR A 1 167 ? 26.062  7.672   28.568  1.00 19.06 ? 167 TYR A O   1 
ATOM   1339 C  CB  . TYR A 1 167 ? 24.288  8.169   31.217  1.00 18.49 ? 167 TYR A CB  1 
ATOM   1340 C  CG  . TYR A 1 167 ? 23.558  7.596   32.413  1.00 17.62 ? 167 TYR A CG  1 
ATOM   1341 C  CD1 . TYR A 1 167 ? 22.161  7.606   32.470  1.00 17.47 ? 167 TYR A CD1 1 
ATOM   1342 C  CD2 . TYR A 1 167 ? 24.252  7.001   33.437  1.00 17.87 ? 167 TYR A CD2 1 
ATOM   1343 C  CE1 . TYR A 1 167 ? 21.468  7.079   33.568  1.00 22.13 ? 167 TYR A CE1 1 
ATOM   1344 C  CE2 . TYR A 1 167 ? 23.600  6.459   34.545  1.00 22.98 ? 167 TYR A CE2 1 
ATOM   1345 C  CZ  . TYR A 1 167 ? 22.204  6.491   34.593  1.00 22.07 ? 167 TYR A CZ  1 
ATOM   1346 O  OH  . TYR A 1 167 ? 21.557  5.958   35.677  1.00 23.68 ? 167 TYR A OH  1 
ATOM   1347 N  N   . LYS A 1 168 ? 24.125  8.813   28.227  1.00 19.15 ? 168 LYS A N   1 
ATOM   1348 C  CA  . LYS A 1 168 ? 24.616  9.621   27.147  1.00 20.18 ? 168 LYS A CA  1 
ATOM   1349 C  C   . LYS A 1 168 ? 25.920  10.372  27.524  1.00 23.26 ? 168 LYS A C   1 
ATOM   1350 O  O   . LYS A 1 168 ? 26.034  10.986  28.609  1.00 21.66 ? 168 LYS A O   1 
ATOM   1351 C  CB  . LYS A 1 168 ? 23.515  10.596  26.669  1.00 21.77 ? 168 LYS A CB  1 
ATOM   1352 C  CG  . LYS A 1 168 ? 24.003  11.497  25.528  1.00 26.88 ? 168 LYS A CG  1 
ATOM   1353 C  CD  . LYS A 1 168 ? 22.935  12.458  24.995  1.00 28.96 ? 168 LYS A CD  1 
ATOM   1354 C  CE  . LYS A 1 168 ? 23.399  12.945  23.629  1.00 33.39 ? 168 LYS A CE  1 
ATOM   1355 N  NZ  . LYS A 1 168 ? 23.098  14.377  23.347  1.00 35.35 ? 168 LYS A NZ  1 
ATOM   1356 N  N   . GLY A 1 169 ? 26.911  10.298  26.638  1.00 24.11 ? 169 GLY A N   1 
ATOM   1357 C  CA  . GLY A 1 169 ? 28.182  10.917  26.881  1.00 22.79 ? 169 GLY A CA  1 
ATOM   1358 C  C   . GLY A 1 169 ? 29.193  10.066  27.622  1.00 23.02 ? 169 GLY A C   1 
ATOM   1359 O  O   . GLY A 1 169 ? 30.350  10.417  27.688  1.00 27.78 ? 169 GLY A O   1 
ATOM   1360 N  N   . GLN A 1 170 ? 28.773  8.939   28.170  1.00 20.48 ? 170 GLN A N   1 
ATOM   1361 C  CA  . GLN A 1 170 ? 29.751  8.064   28.795  1.00 19.49 ? 170 GLN A CA  1 
ATOM   1362 C  C   . GLN A 1 170 ? 30.533  7.243   27.814  1.00 18.82 ? 170 GLN A C   1 
ATOM   1363 O  O   . GLN A 1 170 ? 30.065  6.979   26.675  1.00 17.13 ? 170 GLN A O   1 
ATOM   1364 C  CB  . GLN A 1 170 ? 29.049  7.200   29.802  1.00 18.25 ? 170 GLN A CB  1 
ATOM   1365 C  CG  . GLN A 1 170 ? 28.514  8.056   30.959  1.00 18.83 ? 170 GLN A CG  1 
ATOM   1366 C  CD  . GLN A 1 170 ? 27.937  7.236   32.079  1.00 20.25 ? 170 GLN A CD  1 
ATOM   1367 O  OE1 . GLN A 1 170 ? 27.426  6.136   31.849  1.00 20.09 ? 170 GLN A OE1 1 
ATOM   1368 N  NE2 . GLN A 1 170 ? 28.052  7.737   33.318  1.00 21.16 ? 170 GLN A NE2 1 
ATOM   1369 N  N   A GLU A 1 171 ? 31.757  6.867   28.196  0.50 19.76 ? 171 GLU A N   1 
ATOM   1370 N  N   B GLU A 1 171 ? 31.738  6.870   28.240  0.50 18.83 ? 171 GLU A N   1 
ATOM   1371 C  CA  A GLU A 1 171 ? 32.698  6.172   27.322  0.50 19.82 ? 171 GLU A CA  1 
ATOM   1372 C  CA  B GLU A 1 171 ? 32.660  6.094   27.452  0.50 17.94 ? 171 GLU A CA  1 
ATOM   1373 C  C   A GLU A 1 171 ? 33.533  5.198   28.123  0.50 20.44 ? 171 GLU A C   1 
ATOM   1374 C  C   B GLU A 1 171 ? 33.341  5.006   28.246  0.50 19.13 ? 171 GLU A C   1 
ATOM   1375 O  O   A GLU A 1 171 ? 33.847  5.462   29.288  0.50 23.42 ? 171 GLU A O   1 
ATOM   1376 O  O   B GLU A 1 171 ? 33.345  4.956   29.500  0.50 19.37 ? 171 GLU A O   1 
ATOM   1377 C  CB  A GLU A 1 171 ? 33.622  7.188   26.609  0.50 21.83 ? 171 GLU A CB  1 
ATOM   1378 C  CB  B GLU A 1 171 ? 33.715  7.004   26.786  0.50 19.10 ? 171 GLU A CB  1 
ATOM   1379 C  CG  A GLU A 1 171 ? 32.949  8.514   26.269  0.50 22.06 ? 171 GLU A CG  1 
ATOM   1380 C  CG  B GLU A 1 171 ? 34.619  7.753   27.753  0.50 18.70 ? 171 GLU A CG  1 
ATOM   1381 C  CD  A GLU A 1 171 ? 33.762  9.413   25.339  0.50 23.47 ? 171 GLU A CD  1 
ATOM   1382 C  CD  B GLU A 1 171 ? 35.737  8.532   27.038  0.50 19.12 ? 171 GLU A CD  1 
ATOM   1383 O  OE1 A GLU A 1 171 ? 35.027  9.356   25.310  0.50 26.03 ? 171 GLU A OE1 1 
ATOM   1384 O  OE1 B GLU A 1 171 ? 35.529  9.005   25.895  0.50 20.81 ? 171 GLU A OE1 1 
ATOM   1385 O  OE2 A GLU A 1 171 ? 33.101  10.155  24.607  0.50 21.97 ? 171 GLU A OE2 1 
ATOM   1386 O  OE2 B GLU A 1 171 ? 36.855  8.655   27.608  0.50 17.08 ? 171 GLU A OE2 1 
ATOM   1387 N  N   . ALA A 1 172 ? 33.892  4.083   27.505  1.00 19.13 ? 172 ALA A N   1 
ATOM   1388 C  CA  . ALA A 1 172 ? 34.701  3.044   28.110  1.00 20.53 ? 172 ALA A CA  1 
ATOM   1389 C  C   . ALA A 1 172 ? 35.726  2.585   27.074  1.00 20.07 ? 172 ALA A C   1 
ATOM   1390 O  O   . ALA A 1 172 ? 35.592  2.872   25.840  1.00 20.57 ? 172 ALA A O   1 
ATOM   1391 C  CB  . ALA A 1 172 ? 33.813  1.898   28.538  1.00 20.63 ? 172 ALA A CB  1 
ATOM   1392 N  N   . PHE A 1 173 ? 36.715  1.830   27.531  1.00 21.65 ? 173 PHE A N   1 
ATOM   1393 C  CA  . PHE A 1 173 ? 37.675  1.199   26.636  1.00 23.18 ? 173 PHE A CA  1 
ATOM   1394 C  C   . PHE A 1 173 ? 37.551  -0.316  26.567  1.00 23.71 ? 173 PHE A C   1 
ATOM   1395 O  O   . PHE A 1 173 ? 37.526  -1.030  27.577  1.00 24.69 ? 173 PHE A O   1 
ATOM   1396 C  CB  . PHE A 1 173 ? 39.105  1.632   26.985  1.00 24.12 ? 173 PHE A CB  1 
ATOM   1397 C  CG  . PHE A 1 173 ? 39.392  3.072   26.674  1.00 28.81 ? 173 PHE A CG  1 
ATOM   1398 C  CD1 . PHE A 1 173 ? 39.759  3.467   25.386  1.00 30.04 ? 173 PHE A CD1 1 
ATOM   1399 C  CD2 . PHE A 1 173 ? 39.300  4.038   27.684  1.00 33.20 ? 173 PHE A CD2 1 
ATOM   1400 C  CE1 . PHE A 1 173 ? 40.043  4.801   25.105  1.00 32.05 ? 173 PHE A CE1 1 
ATOM   1401 C  CE2 . PHE A 1 173 ? 39.580  5.372   27.410  1.00 32.77 ? 173 PHE A CE2 1 
ATOM   1402 C  CZ  . PHE A 1 173 ? 39.941  5.749   26.113  1.00 33.32 ? 173 PHE A CZ  1 
ATOM   1403 N  N   . VAL A 1 174 ? 37.513  -0.816  25.335  1.00 18.85 ? 174 VAL A N   1 
ATOM   1404 C  CA  . VAL A 1 174 ? 37.462  -2.227  25.033  1.00 18.19 ? 174 VAL A CA  1 
ATOM   1405 C  C   . VAL A 1 174 ? 38.776  -2.709  24.390  1.00 19.97 ? 174 VAL A C   1 
ATOM   1406 O  O   . VAL A 1 174 ? 39.165  -2.240  23.334  1.00 20.35 ? 174 VAL A O   1 
ATOM   1407 C  CB  . VAL A 1 174 ? 36.263  -2.535  24.077  1.00 17.50 ? 174 VAL A CB  1 
ATOM   1408 C  CG1 . VAL A 1 174 ? 36.089  -4.052  23.939  1.00 16.37 ? 174 VAL A CG1 1 
ATOM   1409 C  CG2 . VAL A 1 174 ? 34.968  -2.008  24.688  1.00 18.84 ? 174 VAL A CG2 1 
ATOM   1410 N  N   . PRO A 1 175 ? 39.436  -3.700  25.000  1.00 21.16 ? 175 PRO A N   1 
ATOM   1411 C  CA  . PRO A 1 175 ? 40.683  -4.257  24.462  1.00 21.44 ? 175 PRO A CA  1 
ATOM   1412 C  C   . PRO A 1 175 ? 40.399  -4.970  23.169  1.00 20.55 ? 175 PRO A C   1 
ATOM   1413 O  O   . PRO A 1 175 ? 39.334  -5.569  23.040  1.00 19.00 ? 175 PRO A O   1 
ATOM   1414 C  CB  . PRO A 1 175 ? 41.105  -5.264  25.549  1.00 23.43 ? 175 PRO A CB  1 
ATOM   1415 C  CG  . PRO A 1 175 ? 40.428  -4.781  26.776  1.00 25.25 ? 175 PRO A CG  1 
ATOM   1416 C  CD  . PRO A 1 175 ? 39.112  -4.224  26.331  1.00 22.71 ? 175 PRO A CD  1 
ATOM   1417 N  N   . GLY A 1 176 ? 41.294  -4.864  22.201  1.00 18.34 ? 176 GLY A N   1 
ATOM   1418 C  CA  . GLY A 1 176 ? 41.092  -5.471  20.929  1.00 18.01 ? 176 GLY A CA  1 
ATOM   1419 C  C   . GLY A 1 176 ? 40.741  -6.944  21.070  1.00 18.54 ? 176 GLY A C   1 
ATOM   1420 O  O   . GLY A 1 176 ? 41.375  -7.705  21.832  1.00 21.08 ? 176 GLY A O   1 
ATOM   1421 N  N   . PHE A 1 177 ? 39.775  -7.369  20.249  1.00 18.41 ? 177 PHE A N   1 
ATOM   1422 C  CA  . PHE A 1 177 ? 39.523  -8.768  20.026  1.00 17.55 ? 177 PHE A CA  1 
ATOM   1423 C  C   . PHE A 1 177 ? 39.201  -9.027  18.569  1.00 16.63 ? 177 PHE A C   1 
ATOM   1424 O  O   . PHE A 1 177 ? 39.191  -8.123  17.784  1.00 17.32 ? 177 PHE A O   1 
ATOM   1425 C  CB  . PHE A 1 177 ? 38.422  -9.307  20.923  1.00 17.48 ? 177 PHE A CB  1 
ATOM   1426 C  CG  . PHE A 1 177 ? 37.048  -8.772  20.599  1.00 18.80 ? 177 PHE A CG  1 
ATOM   1427 C  CD1 . PHE A 1 177 ? 36.138  -9.547  19.901  1.00 19.58 ? 177 PHE A CD1 1 
ATOM   1428 C  CD2 . PHE A 1 177 ? 36.666  -7.488  21.052  1.00 18.02 ? 177 PHE A CD2 1 
ATOM   1429 C  CE1 . PHE A 1 177 ? 34.853  -9.044  19.619  1.00 19.97 ? 177 PHE A CE1 1 
ATOM   1430 C  CE2 . PHE A 1 177 ? 35.389  -6.985  20.767  1.00 21.06 ? 177 PHE A CE2 1 
ATOM   1431 C  CZ  . PHE A 1 177 ? 34.505  -7.777  20.047  1.00 19.59 ? 177 PHE A CZ  1 
ATOM   1432 N  N   . ASN A 1 178 ? 39.014  -10.283 18.203  1.00 16.49 ? 178 ASN A N   1 
ATOM   1433 C  CA  . ASN A 1 178 ? 38.787  -10.593 16.793  1.00 15.84 ? 178 ASN A CA  1 
ATOM   1434 C  C   . ASN A 1 178 ? 37.311  -10.352 16.417  1.00 15.64 ? 178 ASN A C   1 
ATOM   1435 O  O   . ASN A 1 178 ? 36.393  -11.171 16.707  1.00 15.83 ? 178 ASN A O   1 
ATOM   1436 C  CB  . ASN A 1 178 ? 39.161  -12.052 16.515  1.00 17.20 ? 178 ASN A CB  1 
ATOM   1437 C  CG  . ASN A 1 178 ? 39.056  -12.399 15.041  1.00 19.34 ? 178 ASN A CG  1 
ATOM   1438 O  OD1 . ASN A 1 178 ? 38.770  -11.577 14.160  1.00 19.75 ? 178 ASN A OD1 1 
ATOM   1439 N  ND2 . ASN A 1 178 ? 39.216  -13.626 14.763  1.00 20.82 ? 178 ASN A ND2 1 
ATOM   1440 N  N   . ILE A 1 179 ? 37.082  -9.184  15.840  1.00 14.89 ? 179 ILE A N   1 
ATOM   1441 C  CA  . ILE A 1 179 ? 35.698  -8.836  15.414  1.00 14.25 ? 179 ILE A CA  1 
ATOM   1442 C  C   . ILE A 1 179 ? 35.046  -9.909  14.463  1.00 14.23 ? 179 ILE A C   1 
ATOM   1443 O  O   . ILE A 1 179 ? 33.800  -9.963  14.336  1.00 14.07 ? 179 ILE A O   1 
ATOM   1444 C  CB  . ILE A 1 179 ? 35.721  -7.508  14.653  1.00 14.68 ? 179 ILE A CB  1 
ATOM   1445 C  CG1 . ILE A 1 179 ? 36.383  -6.375  15.492  1.00 12.60 ? 179 ILE A CG1 1 
ATOM   1446 C  CG2 . ILE A 1 179 ? 34.337  -7.100  14.142  1.00 14.93 ? 179 ILE A CG2 1 
ATOM   1447 C  CD1 . ILE A 1 179 ? 35.833  -6.155  16.911  1.00 15.28 ? 179 ILE A CD1 1 
ATOM   1448 N  N   . GLU A 1 180 ? 35.825  -10.705 13.725  1.00 13.67 ? 180 GLU A N   1 
ATOM   1449 C  CA  . GLU A 1 180 ? 35.233  -11.718 12.881  1.00 15.73 ? 180 GLU A CA  1 
ATOM   1450 C  C   . GLU A 1 180 ? 34.410  -12.764 13.746  1.00 14.21 ? 180 GLU A C   1 
ATOM   1451 O  O   . GLU A 1 180 ? 33.547  -13.462 13.207  1.00 15.25 ? 180 GLU A O   1 
ATOM   1452 C  CB  . GLU A 1 180 ? 36.310  -12.348 11.960  1.00 19.23 ? 180 GLU A CB  1 
ATOM   1453 C  CG  . GLU A 1 180 ? 35.758  -13.256 10.861  1.00 23.77 ? 180 GLU A CG  1 
ATOM   1454 C  CD  . GLU A 1 180 ? 36.814  -13.672 9.825   1.00 23.18 ? 180 GLU A CD  1 
ATOM   1455 O  OE1 . GLU A 1 180 ? 37.976  -13.236 9.903   1.00 24.34 ? 180 GLU A OE1 1 
ATOM   1456 O  OE2 . GLU A 1 180 ? 36.436  -14.480 8.985   1.00 27.03 ? 180 GLU A OE2 1 
ATOM   1457 N  N   . GLU A 1 181 ? 34.707  -12.847 15.051  1.00 14.01 ? 181 GLU A N   1 
ATOM   1458 C  CA  . GLU A 1 181 ? 33.997  -13.718 15.969  1.00 13.77 ? 181 GLU A CA  1 
ATOM   1459 C  C   . GLU A 1 181 ? 32.512  -13.260 16.092  1.00 13.92 ? 181 GLU A C   1 
ATOM   1460 O  O   . GLU A 1 181 ? 31.682  -14.108 16.401  1.00 16.05 ? 181 GLU A O   1 
ATOM   1461 C  CB  . GLU A 1 181 ? 34.608  -13.723 17.362  1.00 15.25 ? 181 GLU A CB  1 
ATOM   1462 C  CG  . GLU A 1 181 ? 36.018  -14.353 17.497  1.00 16.91 ? 181 GLU A CG  1 
ATOM   1463 C  CD  . GLU A 1 181 ? 36.667  -14.086 18.879  1.00 20.26 ? 181 GLU A CD  1 
ATOM   1464 O  OE1 . GLU A 1 181 ? 36.010  -13.568 19.858  1.00 22.46 ? 181 GLU A OE1 1 
ATOM   1465 O  OE2 . GLU A 1 181 ? 37.926  -14.321 19.019  1.00 19.86 ? 181 GLU A OE2 1 
ATOM   1466 N  N   . LEU A 1 182 ? 32.219  -11.967 15.833  1.00 13.45 ? 182 LEU A N   1 
ATOM   1467 C  CA  . LEU A 1 182 ? 30.824  -11.528 15.808  1.00 11.58 ? 182 LEU A CA  1 
ATOM   1468 C  C   . LEU A 1 182 ? 30.045  -11.890 14.519  1.00 13.62 ? 182 LEU A C   1 
ATOM   1469 O  O   . LEU A 1 182 ? 28.806  -11.609 14.467  1.00 13.55 ? 182 LEU A O   1 
ATOM   1470 C  CB  . LEU A 1 182 ? 30.862  -9.976  15.918  1.00 11.20 ? 182 LEU A CB  1 
ATOM   1471 C  CG  . LEU A 1 182 ? 31.649  -9.468  17.110  1.00 12.82 ? 182 LEU A CG  1 
ATOM   1472 C  CD1 . LEU A 1 182 ? 31.561  -7.956  17.054  1.00 13.28 ? 182 LEU A CD1 1 
ATOM   1473 C  CD2 . LEU A 1 182 ? 31.120  -9.983  18.479  1.00 11.95 ? 182 LEU A CD2 1 
ATOM   1474 N  N   . LEU A 1 183 ? 30.659  -12.457 13.459  1.00 11.79 ? 183 LEU A N   1 
ATOM   1475 C  CA  . LEU A 1 183 ? 30.001  -12.728 12.224  1.00 12.15 ? 183 LEU A CA  1 
ATOM   1476 C  C   . LEU A 1 183 ? 29.490  -14.191 12.317  1.00 13.04 ? 183 LEU A C   1 
ATOM   1477 O  O   . LEU A 1 183 ? 30.035  -15.009 13.084  1.00 13.35 ? 183 LEU A O   1 
ATOM   1478 C  CB  . LEU A 1 183 ? 30.993  -12.628 11.030  1.00 13.06 ? 183 LEU A CB  1 
ATOM   1479 C  CG  . LEU A 1 183 ? 31.740  -11.315 10.905  1.00 14.94 ? 183 LEU A CG  1 
ATOM   1480 C  CD1 . LEU A 1 183 ? 32.615  -11.262 9.651   1.00 15.46 ? 183 LEU A CD1 1 
ATOM   1481 C  CD2 . LEU A 1 183 ? 30.721  -10.155 10.869  1.00 15.32 ? 183 LEU A CD2 1 
ATOM   1482 N  N   . PRO A 1 184 ? 28.478  -14.498 11.543  1.00 13.21 ? 184 PRO A N   1 
ATOM   1483 C  CA  . PRO A 1 184 ? 27.803  -15.763 11.596  1.00 14.54 ? 184 PRO A CA  1 
ATOM   1484 C  C   . PRO A 1 184 ? 28.522  -16.850 10.779  1.00 16.40 ? 184 PRO A C   1 
ATOM   1485 O  O   . PRO A 1 184 ? 29.534  -16.612 10.160  1.00 16.00 ? 184 PRO A O   1 
ATOM   1486 C  CB  . PRO A 1 184 ? 26.428  -15.413 10.998  1.00 15.55 ? 184 PRO A CB  1 
ATOM   1487 C  CG  . PRO A 1 184 ? 26.792  -14.392 9.883   1.00 14.21 ? 184 PRO A CG  1 
ATOM   1488 C  CD  . PRO A 1 184 ? 27.760  -13.523 10.663  1.00 14.49 ? 184 PRO A CD  1 
ATOM   1489 N  N   . GLU A 1 185 ? 27.952  -18.055 10.787  1.00 18.09 ? 185 GLU A N   1 
ATOM   1490 C  CA  . GLU A 1 185 ? 28.434  -19.122 9.910   1.00 21.27 ? 185 GLU A CA  1 
ATOM   1491 C  C   . GLU A 1 185 ? 28.235  -18.778 8.443   1.00 21.59 ? 185 GLU A C   1 
ATOM   1492 O  O   . GLU A 1 185 ? 27.267  -18.012 8.096   1.00 20.64 ? 185 GLU A O   1 
ATOM   1493 C  CB  . GLU A 1 185 ? 27.637  -20.395 10.249  1.00 26.67 ? 185 GLU A CB  1 
ATOM   1494 C  CG  . GLU A 1 185 ? 28.017  -20.969 11.627  1.00 31.66 ? 185 GLU A CG  1 
ATOM   1495 C  CD  . GLU A 1 185 ? 29.528  -21.134 11.833  1.00 37.06 ? 185 GLU A CD  1 
ATOM   1496 O  OE1 . GLU A 1 185 ? 30.211  -21.733 10.966  1.00 36.41 ? 185 GLU A OE1 1 
ATOM   1497 O  OE2 . GLU A 1 185 ? 30.040  -20.658 12.868  1.00 40.73 ? 185 GLU A OE2 1 
ATOM   1498 N  N   . ARG A 1 186 ? 29.102  -19.325 7.591   1.00 15.97 ? 186 ARG A N   1 
ATOM   1499 C  CA  . ARG A 1 186 ? 28.883  -19.248 6.169   1.00 19.34 ? 186 ARG A CA  1 
ATOM   1500 C  C   . ARG A 1 186 ? 28.624  -17.752 5.756   1.00 16.95 ? 186 ARG A C   1 
ATOM   1501 O  O   . ARG A 1 186 ? 27.654  -17.421 5.003   1.00 18.33 ? 186 ARG A O   1 
ATOM   1502 C  CB  . ARG A 1 186 ? 27.780  -20.200 5.717   1.00 23.19 ? 186 ARG A CB  1 
ATOM   1503 C  CG  . ARG A 1 186 ? 28.106  -21.634 6.142   1.00 29.29 ? 186 ARG A CG  1 
ATOM   1504 C  CD  . ARG A 1 186 ? 27.228  -22.756 5.575   1.00 28.64 ? 186 ARG A CD  1 
ATOM   1505 N  NE  . ARG A 1 186 ? 25.784  -22.486 5.586   1.00 30.25 ? 186 ARG A NE  1 
ATOM   1506 C  CZ  . ARG A 1 186 ? 24.993  -22.549 6.649   1.00 33.84 ? 186 ARG A CZ  1 
ATOM   1507 N  NH1 . ARG A 1 186 ? 25.501  -22.844 7.831   1.00 32.47 ? 186 ARG A NH1 1 
ATOM   1508 N  NH2 . ARG A 1 186 ? 23.691  -22.263 6.522   1.00 37.79 ? 186 ARG A NH2 1 
ATOM   1509 N  N   . THR A 1 187 ? 29.595  -16.921 6.095   1.00 15.89 ? 187 THR A N   1 
ATOM   1510 C  CA  . THR A 1 187 ? 29.543  -15.551 5.621   1.00 13.96 ? 187 THR A CA  1 
ATOM   1511 C  C   . THR A 1 187 ? 29.566  -15.433 4.093   1.00 15.37 ? 187 THR A C   1 
ATOM   1512 O  O   . THR A 1 187 ? 29.207  -14.349 3.612   1.00 15.33 ? 187 THR A O   1 
ATOM   1513 C  CB  . THR A 1 187 ? 30.659  -14.653 6.174   1.00 14.73 ? 187 THR A CB  1 
ATOM   1514 O  OG1 . THR A 1 187 ? 31.937  -15.313 5.941   1.00 16.37 ? 187 THR A OG1 1 
ATOM   1515 C  CG2 . THR A 1 187 ? 30.526  -14.477 7.713   1.00 14.21 ? 187 THR A CG2 1 
ATOM   1516 N  N   . ALA A 1 188 ? 29.953  -16.459 3.332   1.00 14.83 ? 188 ALA A N   1 
ATOM   1517 C  CA  . ALA A 1 188 ? 29.727  -16.358 1.835   1.00 13.88 ? 188 ALA A CA  1 
ATOM   1518 C  C   . ALA A 1 188 ? 28.250  -16.183 1.438   1.00 14.29 ? 188 ALA A C   1 
ATOM   1519 O  O   . ALA A 1 188 ? 27.987  -15.793 0.302   1.00 14.31 ? 188 ALA A O   1 
ATOM   1520 C  CB  . ALA A 1 188 ? 30.326  -17.615 1.132   1.00 19.02 ? 188 ALA A CB  1 
ATOM   1521 N  N   . GLU A 1 189 ? 27.314  -16.549 2.341   1.00 15.00 ? 189 GLU A N   1 
ATOM   1522 C  CA  . GLU A 1 189 ? 25.884  -16.489 2.076   1.00 15.55 ? 189 GLU A CA  1 
ATOM   1523 C  C   . GLU A 1 189 ? 25.380  -15.142 2.562   1.00 14.35 ? 189 GLU A C   1 
ATOM   1524 O  O   . GLU A 1 189 ? 25.371  -14.899 3.763   1.00 13.70 ? 189 GLU A O   1 
ATOM   1525 C  CB  . GLU A 1 189 ? 25.129  -17.657 2.767   1.00 16.90 ? 189 GLU A CB  1 
ATOM   1526 C  CG  . GLU A 1 189 ? 25.558  -19.027 2.204   1.00 22.31 ? 189 GLU A CG  1 
ATOM   1527 C  CD  . GLU A 1 189 ? 25.102  -20.211 3.049   1.00 26.39 ? 189 GLU A CD  1 
ATOM   1528 O  OE1 . GLU A 1 189 ? 24.352  -20.029 4.019   1.00 25.28 ? 189 GLU A OE1 1 
ATOM   1529 O  OE2 . GLU A 1 189 ? 25.572  -21.364 2.789   1.00 31.83 ? 189 GLU A OE2 1 
ATOM   1530 N  N   . TYR A 1 190 ? 24.896  -14.290 1.664   1.00 14.18 ? 190 TYR A N   1 
ATOM   1531 C  CA  . TYR A 1 190 ? 24.425  -12.935 2.049   1.00 12.66 ? 190 TYR A CA  1 
ATOM   1532 C  C   . TYR A 1 190 ? 23.470  -12.321 1.051   1.00 11.09 ? 190 TYR A C   1 
ATOM   1533 O  O   . TYR A 1 190 ? 23.399  -12.706 -0.138  1.00 11.23 ? 190 TYR A O   1 
ATOM   1534 C  CB  . TYR A 1 190 ? 25.608  -11.947 2.255   1.00 12.00 ? 190 TYR A CB  1 
ATOM   1535 C  CG  . TYR A 1 190 ? 26.531  -11.765 1.052   1.00 11.28 ? 190 TYR A CG  1 
ATOM   1536 C  CD1 . TYR A 1 190 ? 26.212  -10.888 0.027   1.00 12.43 ? 190 TYR A CD1 1 
ATOM   1537 C  CD2 . TYR A 1 190 ? 27.766  -12.452 1.035   1.00 11.74 ? 190 TYR A CD2 1 
ATOM   1538 C  CE1 . TYR A 1 190 ? 27.098  -10.662 -1.045  1.00 13.85 ? 190 TYR A CE1 1 
ATOM   1539 C  CE2 . TYR A 1 190 ? 28.632  -12.221 -0.029  1.00 12.11 ? 190 TYR A CE2 1 
ATOM   1540 C  CZ  . TYR A 1 190 ? 28.255  -11.418 -1.039  1.00 12.45 ? 190 TYR A CZ  1 
ATOM   1541 O  OH  . TYR A 1 190 ? 29.224  -11.249 -2.069  1.00 17.63 ? 190 TYR A OH  1 
ATOM   1542 N  N   . TYR A 1 191 ? 22.687  -11.350 1.533   1.00 11.42 ? 191 TYR A N   1 
ATOM   1543 C  CA  . TYR A 1 191 ? 21.864  -10.439 0.727   1.00 11.02 ? 191 TYR A CA  1 
ATOM   1544 C  C   . TYR A 1 191 ? 22.649  -9.167  0.446   1.00 11.68 ? 191 TYR A C   1 
ATOM   1545 O  O   . TYR A 1 191 ? 23.367  -8.688  1.321   1.00 12.18 ? 191 TYR A O   1 
ATOM   1546 C  CB  . TYR A 1 191 ? 20.615  -10.052 1.524   1.00 11.09 ? 191 TYR A CB  1 
ATOM   1547 C  CG  . TYR A 1 191 ? 19.782  -11.209 2.098   1.00 12.42 ? 191 TYR A CG  1 
ATOM   1548 C  CD1 . TYR A 1 191 ? 18.735  -11.702 1.373   1.00 13.16 ? 191 TYR A CD1 1 
ATOM   1549 C  CD2 . TYR A 1 191 ? 20.038  -11.681 3.400   1.00 13.47 ? 191 TYR A CD2 1 
ATOM   1550 C  CE1 . TYR A 1 191 ? 17.950  -12.706 1.904   1.00 13.88 ? 191 TYR A CE1 1 
ATOM   1551 C  CE2 . TYR A 1 191 ? 19.235  -12.658 3.984   1.00 14.83 ? 191 TYR A CE2 1 
ATOM   1552 C  CZ  . TYR A 1 191 ? 18.219  -13.193 3.208   1.00 15.67 ? 191 TYR A CZ  1 
ATOM   1553 O  OH  . TYR A 1 191 ? 17.427  -14.215 3.748   1.00 16.08 ? 191 TYR A OH  1 
ATOM   1554 N  N   . ARG A 1 192 ? 22.502  -8.621  -0.761  1.00 11.27 ? 192 ARG A N   1 
ATOM   1555 C  CA  . ARG A 1 192 ? 23.229  -7.324  -1.023  1.00 12.40 ? 192 ARG A CA  1 
ATOM   1556 C  C   . ARG A 1 192 ? 22.261  -6.377  -1.687  1.00 11.48 ? 192 ARG A C   1 
ATOM   1557 O  O   . ARG A 1 192 ? 21.546  -6.768  -2.671  1.00 10.76 ? 192 ARG A O   1 
ATOM   1558 C  CB  . ARG A 1 192 ? 24.317  -7.708  -2.092  1.00 14.80 ? 192 ARG A CB  1 
ATOM   1559 C  CG  . ARG A 1 192 ? 25.014  -6.535  -2.803  1.00 15.80 ? 192 ARG A CG  1 
ATOM   1560 C  CD  . ARG A 1 192 ? 25.889  -5.618  -1.956  1.00 14.87 ? 192 ARG A CD  1 
ATOM   1561 N  NE  . ARG A 1 192 ? 26.891  -6.311  -1.161  1.00 16.76 ? 192 ARG A NE  1 
ATOM   1562 C  CZ  . ARG A 1 192 ? 27.979  -6.928  -1.596  1.00 15.47 ? 192 ARG A CZ  1 
ATOM   1563 N  NH1 . ARG A 1 192 ? 28.311  -6.883  -2.911  1.00 17.66 ? 192 ARG A NH1 1 
ATOM   1564 N  NH2 . ARG A 1 192 ? 28.808  -7.520  -0.744  1.00 15.41 ? 192 ARG A NH2 1 
ATOM   1565 N  N   . TYR A 1 193 ? 22.283  -5.100  -1.317  1.00 11.20 ? 193 TYR A N   1 
ATOM   1566 C  CA  . TYR A 1 193 ? 21.402  -4.178  -2.030  1.00 9.44  ? 193 TYR A CA  1 
ATOM   1567 C  C   . TYR A 1 193 ? 21.958  -2.773  -1.794  1.00 9.86  ? 193 TYR A C   1 
ATOM   1568 O  O   . TYR A 1 193 ? 22.695  -2.557  -0.823  1.00 10.52 ? 193 TYR A O   1 
ATOM   1569 C  CB  . TYR A 1 193 ? 19.857  -4.216  -1.676  1.00 10.94 ? 193 TYR A CB  1 
ATOM   1570 C  CG  . TYR A 1 193 ? 19.521  -3.714  -0.317  1.00 9.54  ? 193 TYR A CG  1 
ATOM   1571 C  CD1 . TYR A 1 193 ? 18.986  -2.418  -0.172  1.00 8.48  ? 193 TYR A CD1 1 
ATOM   1572 C  CD2 . TYR A 1 193 ? 19.744  -4.458  0.848   1.00 9.31  ? 193 TYR A CD2 1 
ATOM   1573 C  CE1 . TYR A 1 193 ? 18.698  -1.875  1.067   1.00 9.41  ? 193 TYR A CE1 1 
ATOM   1574 C  CE2 . TYR A 1 193 ? 19.414  -3.931  2.096   1.00 9.22  ? 193 TYR A CE2 1 
ATOM   1575 C  CZ  . TYR A 1 193 ? 18.907  -2.613  2.182   1.00 8.65  ? 193 TYR A CZ  1 
ATOM   1576 O  OH  . TYR A 1 193 ? 18.629  -2.096  3.396   1.00 8.84  ? 193 TYR A OH  1 
ATOM   1577 N  N   . ARG A 1 194 ? 21.541  -1.822  -2.640  1.00 13.05 ? 194 ARG A N   1 
ATOM   1578 C  CA  . ARG A 1 194 ? 21.975  -0.447  -2.419  1.00 11.06 ? 194 ARG A CA  1 
ATOM   1579 C  C   . ARG A 1 194 ? 20.907  0.316   -1.597  1.00 12.97 ? 194 ARG A C   1 
ATOM   1580 O  O   . ARG A 1 194 ? 19.720  0.309   -1.945  1.00 12.40 ? 194 ARG A O   1 
ATOM   1581 C  CB  . ARG A 1 194 ? 22.096  0.267   -3.815  1.00 17.05 ? 194 ARG A CB  1 
ATOM   1582 C  CG  . ARG A 1 194 ? 23.432  -0.134  -4.453  1.00 20.00 ? 194 ARG A CG  1 
ATOM   1583 C  CD  . ARG A 1 194 ? 23.886  0.810   -5.604  1.00 32.04 ? 194 ARG A CD  1 
ATOM   1584 N  NE  . ARG A 1 194 ? 25.205  0.337   -6.092  1.00 39.00 ? 194 ARG A NE  1 
ATOM   1585 C  CZ  . ARG A 1 194 ? 26.364  0.419   -5.421  1.00 45.79 ? 194 ARG A CZ  1 
ATOM   1586 N  NH1 . ARG A 1 194 ? 26.435  1.017   -4.241  1.00 46.32 ? 194 ARG A NH1 1 
ATOM   1587 N  NH2 . ARG A 1 194 ? 27.478  -0.102  -5.933  1.00 48.65 ? 194 ARG A NH2 1 
ATOM   1588 N  N   . GLY A 1 195 ? 21.306  0.921   -0.469  1.00 11.25 ? 195 GLY A N   1 
ATOM   1589 C  CA  . GLY A 1 195 ? 20.327  1.585   0.372   1.00 11.58 ? 195 GLY A CA  1 
ATOM   1590 C  C   . GLY A 1 195 ? 20.972  2.810   1.033   1.00 10.72 ? 195 GLY A C   1 
ATOM   1591 O  O   . GLY A 1 195 ? 21.818  3.509   0.444   1.00 13.43 ? 195 GLY A O   1 
ATOM   1592 N  N   . SER A 1 196 ? 20.602  3.024   2.277   1.00 9.26  ? 196 SER A N   1 
ATOM   1593 C  CA  . SER A 1 196 ? 20.901  4.275   2.961   1.00 9.81  ? 196 SER A CA  1 
ATOM   1594 C  C   . SER A 1 196 ? 21.287  3.932   4.443   1.00 10.70 ? 196 SER A C   1 
ATOM   1595 O  O   . SER A 1 196 ? 21.128  2.781   4.934   1.00 9.59  ? 196 SER A O   1 
ATOM   1596 C  CB  . SER A 1 196 ? 19.604  5.079   2.988   1.00 10.47 ? 196 SER A CB  1 
ATOM   1597 O  OG  . SER A 1 196 ? 18.738  4.683   4.078   1.00 9.92  ? 196 SER A OG  1 
ATOM   1598 N  N   . LEU A 1 197 ? 21.805  4.945   5.105   1.00 9.86  ? 197 LEU A N   1 
ATOM   1599 C  CA  . LEU A 1 197 ? 21.921  4.950   6.584   1.00 10.36 ? 197 LEU A CA  1 
ATOM   1600 C  C   . LEU A 1 197 ? 20.526  4.790   7.112   1.00 9.90  ? 197 LEU A C   1 
ATOM   1601 O  O   . LEU A 1 197 ? 19.575  5.379   6.548   1.00 10.25 ? 197 LEU A O   1 
ATOM   1602 C  CB  . LEU A 1 197 ? 22.510  6.301   7.041   1.00 10.92 ? 197 LEU A CB  1 
ATOM   1603 C  CG  . LEU A 1 197 ? 23.957  6.516   6.637   1.00 11.65 ? 197 LEU A CG  1 
ATOM   1604 C  CD1 . LEU A 1 197 ? 24.374  7.904   7.100   1.00 11.20 ? 197 LEU A CD1 1 
ATOM   1605 C  CD2 . LEU A 1 197 ? 24.883  5.509   7.235   1.00 12.13 ? 197 LEU A CD2 1 
ATOM   1606 N  N   . THR A 1 198 ? 20.379  4.134   8.261   1.00 10.64 ? 198 THR A N   1 
ATOM   1607 C  CA  . THR A 1 198 ? 19.071  3.956   8.851   1.00 10.58 ? 198 THR A CA  1 
ATOM   1608 C  C   . THR A 1 198 ? 18.779  4.960   9.973   1.00 11.03 ? 198 THR A C   1 
ATOM   1609 O  O   . THR A 1 198 ? 17.714  4.920   10.645  1.00 10.26 ? 198 THR A O   1 
ATOM   1610 C  CB  . THR A 1 198 ? 18.873  2.493   9.339   1.00 11.99 ? 198 THR A CB  1 
ATOM   1611 O  OG1 . THR A 1 198 ? 19.686  2.276   10.485  1.00 13.06 ? 198 THR A OG1 1 
ATOM   1612 C  CG2 . THR A 1 198 ? 19.075  1.440   8.277   1.00 11.31 ? 198 THR A CG2 1 
ATOM   1613 N  N   . THR A 1 199 ? 19.687  5.944   10.164  1.00 10.77 ? 199 THR A N   1 
ATOM   1614 C  CA  . THR A 1 199 ? 19.540  6.977   11.078  1.00 11.38 ? 199 THR A CA  1 
ATOM   1615 C  C   . THR A 1 199 ? 19.876  8.260   10.318  1.00 9.59  ? 199 THR A C   1 
ATOM   1616 O  O   . THR A 1 199 ? 20.537  8.158   9.212   1.00 11.45 ? 199 THR A O   1 
ATOM   1617 C  CB  . THR A 1 199 ? 20.520  6.924   12.234  1.00 11.96 ? 199 THR A CB  1 
ATOM   1618 O  OG1 . THR A 1 199 ? 21.864  6.983   11.698  1.00 13.11 ? 199 THR A OG1 1 
ATOM   1619 C  CG2 . THR A 1 199 ? 20.296  5.601   13.115  1.00 12.47 ? 199 THR A CG2 1 
ATOM   1620 N  N   . PRO A 1 200 ? 19.353  9.397   10.832  1.00 11.84 ? 200 PRO A N   1 
ATOM   1621 C  CA  . PRO A 1 200 ? 19.798  10.672  10.272  1.00 10.91 ? 200 PRO A CA  1 
ATOM   1622 C  C   . PRO A 1 200 ? 21.330  10.691  10.120  1.00 11.72 ? 200 PRO A C   1 
ATOM   1623 O  O   . PRO A 1 200 ? 22.032  10.223  11.046  1.00 10.90 ? 200 PRO A O   1 
ATOM   1624 C  CB  . PRO A 1 200 ? 19.314  11.662  11.323  1.00 9.61  ? 200 PRO A CB  1 
ATOM   1625 C  CG  . PRO A 1 200 ? 17.994  11.028  11.764  1.00 9.38  ? 200 PRO A CG  1 
ATOM   1626 C  CD  . PRO A 1 200 ? 18.408  9.586   11.955  1.00 9.95  ? 200 PRO A CD  1 
ATOM   1627 N  N   . PRO A 1 201 ? 21.793  11.207  8.990   1.00 11.41 ? 201 PRO A N   1 
ATOM   1628 C  CA  . PRO A 1 201 ? 21.021  11.951  7.970   1.00 12.87 ? 201 PRO A CA  1 
ATOM   1629 C  C   . PRO A 1 201 ? 20.390  11.106  6.854   1.00 10.93 ? 201 PRO A C   1 
ATOM   1630 O  O   . PRO A 1 201 ? 19.936  11.645  5.889   1.00 12.37 ? 201 PRO A O   1 
ATOM   1631 C  CB  . PRO A 1 201 ? 22.089  12.900  7.328   1.00 12.69 ? 201 PRO A CB  1 
ATOM   1632 C  CG  . PRO A 1 201 ? 23.256  12.791  8.194   1.00 14.13 ? 201 PRO A CG  1 
ATOM   1633 C  CD  . PRO A 1 201 ? 23.235  11.334  8.725   1.00 12.93 ? 201 PRO A CD  1 
ATOM   1634 N  N   . CYS A 1 202 ? 20.406  9.756   6.956   1.00 10.96 ? 202 CYS A N   1 
ATOM   1635 C  CA  . CYS A 1 202 ? 19.757  8.774   6.027   1.00 9.74  ? 202 CYS A CA  1 
ATOM   1636 C  C   . CYS A 1 202 ? 20.330  8.904   4.629   1.00 9.65  ? 202 CYS A C   1 
ATOM   1637 O  O   . CYS A 1 202 ? 19.662  8.635   3.641   1.00 10.13 ? 202 CYS A O   1 
ATOM   1638 C  CB  . CYS A 1 202 ? 18.156  8.939   5.978   1.00 10.84 ? 202 CYS A CB  1 
ATOM   1639 S  SG  . CYS A 1 202 ? 17.344  9.014   7.571   1.00 11.16 ? 202 CYS A SG  1 
ATOM   1640 N  N   . ASN A 1 203 ? 21.642  9.254   4.514   1.00 9.23  ? 203 ASN A N   1 
ATOM   1641 C  CA  . ASN A 1 203 ? 22.164  9.402   3.152   1.00 9.81  ? 203 ASN A CA  1 
ATOM   1642 C  C   . ASN A 1 203 ? 22.070  8.088   2.387   1.00 9.90  ? 203 ASN A C   1 
ATOM   1643 O  O   . ASN A 1 203 ? 22.370  6.990   2.936   1.00 10.18 ? 203 ASN A O   1 
ATOM   1644 C  CB  . ASN A 1 203 ? 23.653  9.722   3.298   1.00 11.66 ? 203 ASN A CB  1 
ATOM   1645 C  CG  . ASN A 1 203 ? 23.869  10.979  4.097   1.00 14.83 ? 203 ASN A CG  1 
ATOM   1646 O  OD1 . ASN A 1 203 ? 23.900  10.939  5.335   1.00 16.61 ? 203 ASN A OD1 1 
ATOM   1647 N  ND2 . ASN A 1 203 ? 23.864  12.111  3.426   1.00 21.00 ? 203 ASN A ND2 1 
ATOM   1648 N  N   . PRO A 1 204 ? 21.733  8.137   1.091   1.00 10.17 ? 204 PRO A N   1 
ATOM   1649 C  CA  . PRO A 1 204 ? 21.514  6.922   0.258   1.00 12.04 ? 204 PRO A CA  1 
ATOM   1650 C  C   . PRO A 1 204 ? 22.809  6.464   -0.341  1.00 12.14 ? 204 PRO A C   1 
ATOM   1651 O  O   . PRO A 1 204 ? 22.956  6.375   -1.607  1.00 14.07 ? 204 PRO A O   1 
ATOM   1652 C  CB  . PRO A 1 204 ? 20.514  7.382   -0.837  1.00 11.19 ? 204 PRO A CB  1 
ATOM   1653 C  CG  . PRO A 1 204 ? 20.812  8.933   -0.946  1.00 12.25 ? 204 PRO A CG  1 
ATOM   1654 C  CD  . PRO A 1 204 ? 21.188  9.382   0.468   1.00 11.28 ? 204 PRO A CD  1 
ATOM   1655 N  N   . THR A 1 205 ? 23.743  6.232   0.557   1.00 11.67 ? 205 THR A N   1 
ATOM   1656 C  CA  . THR A 1 205 ? 25.130  6.043   0.103   1.00 11.71 ? 205 THR A CA  1 
ATOM   1657 C  C   . THR A 1 205 ? 25.711  4.731   0.578   1.00 11.68 ? 205 THR A C   1 
ATOM   1658 O  O   . THR A 1 205 ? 26.920  4.550   0.491   1.00 11.59 ? 205 THR A O   1 
ATOM   1659 C  CB  . THR A 1 205 ? 26.009  7.191   0.627   1.00 10.95 ? 205 THR A CB  1 
ATOM   1660 O  OG1 . THR A 1 205 ? 25.897  7.234   2.040   1.00 11.52 ? 205 THR A OG1 1 
ATOM   1661 C  CG2 . THR A 1 205 ? 25.493  8.619   0.071   1.00 14.26 ? 205 THR A CG2 1 
ATOM   1662 N  N   . VAL A 1 206 ? 24.859  3.790   0.998   1.00 10.87 ? 206 VAL A N   1 
ATOM   1663 C  CA  . VAL A 1 206 ? 25.316  2.550   1.622   1.00 11.76 ? 206 VAL A CA  1 
ATOM   1664 C  C   . VAL A 1 206 ? 25.103  1.361   0.749   1.00 11.60 ? 206 VAL A C   1 
ATOM   1665 O  O   . VAL A 1 206 ? 23.988  1.048   0.328   1.00 13.87 ? 206 VAL A O   1 
ATOM   1666 C  CB  . VAL A 1 206 ? 24.598  2.338   3.004   1.00 10.41 ? 206 VAL A CB  1 
ATOM   1667 C  CG1 . VAL A 1 206 ? 24.986  0.957   3.554   1.00 11.34 ? 206 VAL A CG1 1 
ATOM   1668 C  CG2 . VAL A 1 206 ? 24.863  3.474   3.995   1.00 10.34 ? 206 VAL A CG2 1 
ATOM   1669 N  N   . LEU A 1 207 ? 26.172  0.594   0.535   1.00 11.27 ? 207 LEU A N   1 
ATOM   1670 C  CA  . LEU A 1 207 ? 26.091  -0.749  -0.038  1.00 11.89 ? 207 LEU A CA  1 
ATOM   1671 C  C   . LEU A 1 207 ? 25.889  -1.695  1.177   1.00 11.47 ? 207 LEU A C   1 
ATOM   1672 O  O   . LEU A 1 207 ? 26.710  -1.816  2.029   1.00 12.16 ? 207 LEU A O   1 
ATOM   1673 C  CB  . LEU A 1 207 ? 27.360  -1.056  -0.848  1.00 13.10 ? 207 LEU A CB  1 
ATOM   1674 C  CG  . LEU A 1 207 ? 27.226  -2.425  -1.529  1.00 16.59 ? 207 LEU A CG  1 
ATOM   1675 C  CD1 . LEU A 1 207 ? 26.279  -2.302  -2.733  1.00 17.37 ? 207 LEU A CD1 1 
ATOM   1676 C  CD2 . LEU A 1 207 ? 28.616  -2.788  -2.023  1.00 19.28 ? 207 LEU A CD2 1 
ATOM   1677 N  N   . TRP A 1 208 ? 24.716  -2.333  1.239   1.00 10.69 ? 208 TRP A N   1 
ATOM   1678 C  CA  . TRP A 1 208 ? 24.354  -3.212  2.361   1.00 10.04 ? 208 TRP A CA  1 
ATOM   1679 C  C   . TRP A 1 208 ? 24.713  -4.605  2.056   1.00 10.14 ? 208 TRP A C   1 
ATOM   1680 O  O   . TRP A 1 208 ? 24.444  -5.125  0.961   1.00 10.52 ? 208 TRP A O   1 
ATOM   1681 C  CB  . TRP A 1 208 ? 22.819  -3.159  2.588   1.00 10.26 ? 208 TRP A CB  1 
ATOM   1682 C  CG  . TRP A 1 208 ? 22.470  -1.951  3.425   1.00 10.26 ? 208 TRP A CG  1 
ATOM   1683 C  CD1 . TRP A 1 208 ? 22.005  -0.715  2.986   1.00 10.85 ? 208 TRP A CD1 1 
ATOM   1684 C  CD2 . TRP A 1 208 ? 22.609  -1.806  4.883   1.00 9.81  ? 208 TRP A CD2 1 
ATOM   1685 N  NE1 . TRP A 1 208 ? 21.828  0.145   4.039   1.00 11.32 ? 208 TRP A NE1 1 
ATOM   1686 C  CE2 . TRP A 1 208 ? 22.172  -0.445  5.203   1.00 10.20 ? 208 TRP A CE2 1 
ATOM   1687 C  CE3 . TRP A 1 208 ? 23.023  -2.638  5.913   1.00 9.64  ? 208 TRP A CE3 1 
ATOM   1688 C  CZ2 . TRP A 1 208 ? 22.158  0.035   6.500   1.00 10.28 ? 208 TRP A CZ2 1 
ATOM   1689 C  CZ3 . TRP A 1 208 ? 23.002  -2.142  7.218   1.00 9.49  ? 208 TRP A CZ3 1 
ATOM   1690 C  CH2 . TRP A 1 208 ? 22.580  -0.838  7.502   1.00 10.33 ? 208 TRP A CH2 1 
ATOM   1691 N  N   . THR A 1 209 ? 25.327  -5.256  3.038   1.00 8.22  ? 209 THR A N   1 
ATOM   1692 C  CA  . THR A 1 209 ? 25.531  -6.725  2.975   1.00 8.82  ? 209 THR A CA  1 
ATOM   1693 C  C   . THR A 1 209 ? 24.895  -7.259  4.250   1.00 8.18  ? 209 THR A C   1 
ATOM   1694 O  O   . THR A 1 209 ? 25.379  -6.967  5.354   1.00 9.48  ? 209 THR A O   1 
ATOM   1695 C  CB  . THR A 1 209 ? 27.047  -7.064  2.961   1.00 9.56  ? 209 THR A CB  1 
ATOM   1696 O  OG1 . THR A 1 209 ? 27.593  -6.548  1.728   1.00 10.69 ? 209 THR A OG1 1 
ATOM   1697 C  CG2 . THR A 1 209 ? 27.234  -8.569  2.988   1.00 10.95 ? 209 THR A CG2 1 
ATOM   1698 N  N   . VAL A 1 210 ? 23.802  -8.105  4.112   1.00 8.85  ? 210 VAL A N   1 
ATOM   1699 C  CA  . VAL A 1 210 ? 23.174  -8.678  5.319   1.00 9.14  ? 210 VAL A CA  1 
ATOM   1700 C  C   . VAL A 1 210 ? 23.419  -10.206 5.256   1.00 9.86  ? 210 VAL A C   1 
ATOM   1701 O  O   . VAL A 1 210 ? 23.094  -10.792 4.236   1.00 11.52 ? 210 VAL A O   1 
ATOM   1702 C  CB  . VAL A 1 210 ? 21.615  -8.430  5.264   1.00 10.65 ? 210 VAL A CB  1 
ATOM   1703 C  CG1 . VAL A 1 210 ? 20.934  -8.982  6.554   1.00 11.02 ? 210 VAL A CG1 1 
ATOM   1704 C  CG2 . VAL A 1 210 ? 21.305  -6.932  5.103   1.00 9.88  ? 210 VAL A CG2 1 
ATOM   1705 N  N   . PHE A 1 211 ? 24.126  -10.744 6.235   1.00 9.81  ? 211 PHE A N   1 
ATOM   1706 C  CA  . PHE A 1 211 ? 24.465  -12.186 6.174   1.00 10.06 ? 211 PHE A CA  1 
ATOM   1707 C  C   . PHE A 1 211 ? 23.185  -12.954 6.295   1.00 11.23 ? 211 PHE A C   1 
ATOM   1708 O  O   . PHE A 1 211 ? 22.269  -12.611 7.053   1.00 11.97 ? 211 PHE A O   1 
ATOM   1709 C  CB  . PHE A 1 211 ? 25.525  -12.529 7.225   1.00 10.35 ? 211 PHE A CB  1 
ATOM   1710 C  CG  . PHE A 1 211 ? 26.852  -11.857 6.979   1.00 10.52 ? 211 PHE A CG  1 
ATOM   1711 C  CD1 . PHE A 1 211 ? 27.595  -12.220 5.858   1.00 11.14 ? 211 PHE A CD1 1 
ATOM   1712 C  CD2 . PHE A 1 211 ? 27.297  -10.758 7.767   1.00 10.82 ? 211 PHE A CD2 1 
ATOM   1713 C  CE1 . PHE A 1 211 ? 28.777  -11.555 5.536   1.00 14.06 ? 211 PHE A CE1 1 
ATOM   1714 C  CE2 . PHE A 1 211 ? 28.513  -10.108 7.428   1.00 11.94 ? 211 PHE A CE2 1 
ATOM   1715 C  CZ  . PHE A 1 211 ? 29.233  -10.483 6.311   1.00 12.18 ? 211 PHE A CZ  1 
ATOM   1716 N  N   . ARG A 1 212 ? 23.136  -14.044 5.505   1.00 10.57 ? 212 ARG A N   1 
ATOM   1717 C  CA  . ARG A 1 212 ? 21.929  -14.927 5.494   1.00 11.35 ? 212 ARG A CA  1 
ATOM   1718 C  C   . ARG A 1 212 ? 21.687  -15.536 6.884   1.00 11.78 ? 212 ARG A C   1 
ATOM   1719 O  O   . ARG A 1 212 ? 20.518  -15.580 7.326   1.00 13.61 ? 212 ARG A O   1 
ATOM   1720 C  CB  . ARG A 1 212 ? 22.072  -16.004 4.426   1.00 13.75 ? 212 ARG A CB  1 
ATOM   1721 C  CG  . ARG A 1 212 ? 20.843  -16.924 4.301   1.00 16.33 ? 212 ARG A CG  1 
ATOM   1722 C  CD  . ARG A 1 212 ? 21.304  -18.235 3.675   1.00 19.22 ? 212 ARG A CD  1 
ATOM   1723 N  NE  . ARG A 1 212 ? 20.125  -19.059 3.473   1.00 27.19 ? 212 ARG A NE  1 
ATOM   1724 C  CZ  . ARG A 1 212 ? 19.799  -20.096 4.259   1.00 32.95 ? 212 ARG A CZ  1 
ATOM   1725 N  NH1 . ARG A 1 212 ? 20.571  -20.474 5.302   1.00 36.76 ? 212 ARG A NH1 1 
ATOM   1726 N  NH2 . ARG A 1 212 ? 18.681  -20.766 4.007   1.00 35.35 ? 212 ARG A NH2 1 
ATOM   1727 N  N   . ASN A 1 213 ? 22.747  -16.010 7.546   1.00 10.67 ? 213 ASN A N   1 
ATOM   1728 C  CA  . ASN A 1 213 ? 22.567  -16.681 8.847   1.00 12.64 ? 213 ASN A CA  1 
ATOM   1729 C  C   . ASN A 1 213 ? 22.708  -15.810 10.047  1.00 11.79 ? 213 ASN A C   1 
ATOM   1730 O  O   . ASN A 1 213 ? 23.625  -14.996 10.106  1.00 14.06 ? 213 ASN A O   1 
ATOM   1731 C  CB  . ASN A 1 213 ? 23.605  -17.792 8.856   1.00 13.14 ? 213 ASN A CB  1 
ATOM   1732 C  CG  . ASN A 1 213 ? 23.466  -18.688 7.585   1.00 15.17 ? 213 ASN A CG  1 
ATOM   1733 O  OD1 . ASN A 1 213 ? 22.371  -19.110 7.214   1.00 19.94 ? 213 ASN A OD1 1 
ATOM   1734 N  ND2 . ASN A 1 213 ? 24.570  -18.904 6.892   1.00 16.02 ? 213 ASN A ND2 1 
ATOM   1735 N  N   . PRO A 1 214 ? 21.808  -15.955 11.032  1.00 12.04 ? 214 PRO A N   1 
ATOM   1736 C  CA  . PRO A 1 214 ? 21.950  -15.201 12.233  1.00 12.91 ? 214 PRO A CA  1 
ATOM   1737 C  C   . PRO A 1 214 ? 22.975  -15.840 13.181  1.00 12.30 ? 214 PRO A C   1 
ATOM   1738 O  O   . PRO A 1 214 ? 23.413  -17.068 13.030  1.00 13.53 ? 214 PRO A O   1 
ATOM   1739 C  CB  . PRO A 1 214 ? 20.545  -15.279 12.851  1.00 14.13 ? 214 PRO A CB  1 
ATOM   1740 C  CG  . PRO A 1 214 ? 20.172  -16.692 12.492  1.00 13.35 ? 214 PRO A CG  1 
ATOM   1741 C  CD  . PRO A 1 214 ? 20.610  -16.841 11.058  1.00 14.39 ? 214 PRO A CD  1 
ATOM   1742 N  N   . VAL A 1 215 ? 23.347  -15.020 14.146  1.00 12.44 ? 215 VAL A N   1 
ATOM   1743 C  CA  . VAL A 1 215 ? 24.099  -15.529 15.280  1.00 12.00 ? 215 VAL A CA  1 
ATOM   1744 C  C   . VAL A 1 215 ? 23.147  -15.678 16.482  1.00 12.45 ? 215 VAL A C   1 
ATOM   1745 O  O   . VAL A 1 215 ? 21.997  -15.205 16.398  1.00 12.01 ? 215 VAL A O   1 
ATOM   1746 C  CB  . VAL A 1 215 ? 25.226  -14.602 15.677  1.00 11.48 ? 215 VAL A CB  1 
ATOM   1747 C  CG1 . VAL A 1 215 ? 26.274  -14.469 14.560  1.00 12.49 ? 215 VAL A CG1 1 
ATOM   1748 C  CG2 . VAL A 1 215 ? 24.751  -13.226 16.161  1.00 12.29 ? 215 VAL A CG2 1 
ATOM   1749 N  N   A GLN A 1 216 ? 23.639  -16.320 17.547  0.50 12.92 ? 216 GLN A N   1 
ATOM   1750 N  N   B GLN A 1 216 ? 23.570  -16.381 17.530  0.50 12.97 ? 216 GLN A N   1 
ATOM   1751 C  CA  A GLN A 1 216 ? 22.895  -16.423 18.818  0.50 12.95 ? 216 GLN A CA  1 
ATOM   1752 C  CA  B GLN A 1 216 ? 22.727  -16.546 18.735  0.50 13.24 ? 216 GLN A CA  1 
ATOM   1753 C  C   A GLN A 1 216 ? 23.534  -15.720 19.929  0.50 13.34 ? 216 GLN A C   1 
ATOM   1754 C  C   B GLN A 1 216 ? 23.423  -15.920 19.912  0.50 13.48 ? 216 GLN A C   1 
ATOM   1755 O  O   A GLN A 1 216 ? 24.746  -15.691 20.082  0.50 13.15 ? 216 GLN A O   1 
ATOM   1756 O  O   B GLN A 1 216 ? 24.636  -16.103 20.042  0.50 13.58 ? 216 GLN A O   1 
ATOM   1757 C  CB  A GLN A 1 216 ? 22.628  -17.885 19.227  0.50 12.46 ? 216 GLN A CB  1 
ATOM   1758 C  CB  B GLN A 1 216 ? 22.404  -18.048 18.966  0.50 12.11 ? 216 GLN A CB  1 
ATOM   1759 C  CG  A GLN A 1 216 ? 21.803  -18.607 18.195  0.50 12.85 ? 216 GLN A CG  1 
ATOM   1760 C  CG  B GLN A 1 216 ? 21.712  -18.742 17.777  0.50 12.77 ? 216 GLN A CG  1 
ATOM   1761 C  CD  A GLN A 1 216 ? 21.358  -19.987 18.605  0.50 14.23 ? 216 GLN A CD  1 
ATOM   1762 C  CD  B GLN A 1 216 ? 22.606  -18.999 16.538  0.50 13.43 ? 216 GLN A CD  1 
ATOM   1763 O  OE1 A GLN A 1 216 ? 21.866  -20.560 19.592  0.50 14.11 ? 216 GLN A OE1 1 
ATOM   1764 O  OE1 B GLN A 1 216 ? 23.738  -19.397 16.669  0.50 15.10 ? 216 GLN A OE1 1 
ATOM   1765 N  NE2 A GLN A 1 216 ? 20.363  -20.496 17.891  0.50 15.38 ? 216 GLN A NE2 1 
ATOM   1766 N  NE2 B GLN A 1 216 ? 22.043  -18.864 15.328  0.50 13.60 ? 216 GLN A NE2 1 
ATOM   1767 N  N   . ILE A 1 217 ? 22.675  -15.170 20.760  1.00 12.32 ? 217 ILE A N   1 
ATOM   1768 C  CA  . ILE A 1 217 ? 23.107  -14.703 22.097  1.00 13.13 ? 217 ILE A CA  1 
ATOM   1769 C  C   . ILE A 1 217 ? 22.099  -15.221 23.141  1.00 12.10 ? 217 ILE A C   1 
ATOM   1770 O  O   . ILE A 1 217 ? 20.948  -15.594 22.769  1.00 12.28 ? 217 ILE A O   1 
ATOM   1771 C  CB  . ILE A 1 217 ? 23.249  -13.156 22.145  1.00 12.12 ? 217 ILE A CB  1 
ATOM   1772 C  CG1 . ILE A 1 217 ? 21.895  -12.410 22.066  1.00 13.71 ? 217 ILE A CG1 1 
ATOM   1773 C  CG2 . ILE A 1 217 ? 24.329  -12.656 21.162  1.00 14.13 ? 217 ILE A CG2 1 
ATOM   1774 C  CD1 . ILE A 1 217 ? 22.092  -10.922 22.211  1.00 13.98 ? 217 ILE A CD1 1 
ATOM   1775 N  N   . SER A 1 218 ? 22.516  -15.271 24.414  1.00 12.42 ? 218 SER A N   1 
ATOM   1776 C  CA  . SER A 1 218 ? 21.578  -15.870 25.383  1.00 15.55 ? 218 SER A CA  1 
ATOM   1777 C  C   . SER A 1 218 ? 20.452  -14.939 25.770  1.00 15.96 ? 218 SER A C   1 
ATOM   1778 O  O   . SER A 1 218 ? 20.495  -13.726 25.511  1.00 13.37 ? 218 SER A O   1 
ATOM   1779 C  CB  . SER A 1 218 ? 22.252  -16.189 26.698  1.00 14.54 ? 218 SER A CB  1 
ATOM   1780 O  OG  . SER A 1 218 ? 22.823  -15.080 27.389  1.00 14.92 ? 218 SER A OG  1 
ATOM   1781 N  N   . GLN A 1 219 ? 19.418  -15.509 26.370  1.00 16.07 ? 219 GLN A N   1 
ATOM   1782 C  CA  . GLN A 1 219 ? 18.348  -14.647 26.859  1.00 17.56 ? 219 GLN A CA  1 
ATOM   1783 C  C   . GLN A 1 219 ? 18.858  -13.616 27.860  1.00 18.08 ? 219 GLN A C   1 
ATOM   1784 O  O   . GLN A 1 219 ? 18.403  -12.463 27.803  1.00 15.05 ? 219 GLN A O   1 
ATOM   1785 C  CB  . GLN A 1 219 ? 17.181  -15.497 27.366  1.00 23.63 ? 219 GLN A CB  1 
ATOM   1786 C  CG  . GLN A 1 219 ? 17.386  -16.205 28.682  1.00 31.98 ? 219 GLN A CG  1 
ATOM   1787 C  CD  . GLN A 1 219 ? 16.094  -16.913 29.104  1.00 36.97 ? 219 GLN A CD  1 
ATOM   1788 O  OE1 . GLN A 1 219 ? 15.599  -17.811 28.397  1.00 37.18 ? 219 GLN A OE1 1 
ATOM   1789 N  NE2 . GLN A 1 219 ? 15.513  -16.472 30.229  1.00 42.13 ? 219 GLN A NE2 1 
ATOM   1790 N  N   . GLU A 1 220 ? 19.874  -13.959 28.679  1.00 17.56 ? 220 GLU A N   1 
ATOM   1791 C  CA  . GLU A 1 220 ? 20.382  -13.018 29.645  1.00 16.98 ? 220 GLU A CA  1 
ATOM   1792 C  C   . GLU A 1 220 ? 21.154  -11.909 28.906  1.00 15.42 ? 220 GLU A C   1 
ATOM   1793 O  O   . GLU A 1 220 ? 21.090  -10.721 29.288  1.00 15.01 ? 220 GLU A O   1 
ATOM   1794 C  CB  . GLU A 1 220 ? 21.245  -13.690 30.735  1.00 18.81 ? 220 GLU A CB  1 
ATOM   1795 C  CG  . GLU A 1 220 ? 20.484  -14.744 31.592  1.00 22.09 ? 220 GLU A CG  1 
ATOM   1796 C  CD  . GLU A 1 220 ? 20.204  -16.114 30.913  1.00 27.75 ? 220 GLU A CD  1 
ATOM   1797 O  OE1 . GLU A 1 220 ? 20.751  -16.522 29.840  1.00 25.29 ? 220 GLU A OE1 1 
ATOM   1798 O  OE2 . GLU A 1 220 ? 19.338  -16.858 31.459  1.00 29.25 ? 220 GLU A OE2 1 
ATOM   1799 N  N   . GLN A 1 221 ? 21.850  -12.300 27.803  1.00 13.83 ? 221 GLN A N   1 
ATOM   1800 C  CA  . GLN A 1 221 ? 22.637  -11.279 27.093  1.00 12.36 ? 221 GLN A CA  1 
ATOM   1801 C  C   . GLN A 1 221 ? 21.683  -10.268 26.370  1.00 13.40 ? 221 GLN A C   1 
ATOM   1802 O  O   . GLN A 1 221 ? 21.928  -9.040  26.406  1.00 12.87 ? 221 GLN A O   1 
ATOM   1803 C  CB  . GLN A 1 221 ? 23.542  -11.869 26.021  1.00 14.31 ? 221 GLN A CB  1 
ATOM   1804 C  CG  . GLN A 1 221 ? 24.793  -12.524 26.604  1.00 15.36 ? 221 GLN A CG  1 
ATOM   1805 C  CD  . GLN A 1 221 ? 25.619  -13.224 25.540  1.00 13.42 ? 221 GLN A CD  1 
ATOM   1806 O  OE1 . GLN A 1 221 ? 25.189  -14.143 24.872  1.00 13.04 ? 221 GLN A OE1 1 
ATOM   1807 N  NE2 . GLN A 1 221 ? 26.860  -12.818 25.437  1.00 14.80 ? 221 GLN A NE2 1 
ATOM   1808 N  N   . LEU A 1 222 ? 20.640  -10.806 25.781  1.00 13.27 ? 222 LEU A N   1 
ATOM   1809 C  CA  . LEU A 1 222 ? 19.663  -9.953  25.068  1.00 12.12 ? 222 LEU A CA  1 
ATOM   1810 C  C   . LEU A 1 222 ? 18.975  -9.049  26.074  1.00 12.82 ? 222 LEU A C   1 
ATOM   1811 O  O   . LEU A 1 222 ? 18.780  -7.888  25.809  1.00 12.47 ? 222 LEU A O   1 
ATOM   1812 C  CB  . LEU A 1 222 ? 18.650  -10.810 24.268  1.00 12.19 ? 222 LEU A CB  1 
ATOM   1813 C  CG  . LEU A 1 222 ? 17.454  -10.045 23.683  1.00 13.60 ? 222 LEU A CG  1 
ATOM   1814 C  CD1 . LEU A 1 222 ? 18.009  -9.071  22.588  1.00 13.25 ? 222 LEU A CD1 1 
ATOM   1815 C  CD2 . LEU A 1 222 ? 16.475  -11.112 23.108  1.00 14.22 ? 222 LEU A CD2 1 
ATOM   1816 N  N   . LEU A 1 223 ? 18.595  -9.586  27.257  1.00 11.88 ? 223 LEU A N   1 
ATOM   1817 C  CA  . LEU A 1 223 ? 17.944  -8.749  28.252  1.00 12.96 ? 223 LEU A CA  1 
ATOM   1818 C  C   . LEU A 1 223 ? 18.933  -7.656  28.732  1.00 11.95 ? 223 LEU A C   1 
ATOM   1819 O  O   . LEU A 1 223 ? 18.466  -6.553  28.967  1.00 14.55 ? 223 LEU A O   1 
ATOM   1820 C  CB  . LEU A 1 223 ? 17.459  -9.555  29.452  1.00 13.38 ? 223 LEU A CB  1 
ATOM   1821 C  CG  . LEU A 1 223 ? 16.755  -8.882  30.635  1.00 14.84 ? 223 LEU A CG  1 
ATOM   1822 C  CD1 . LEU A 1 223 ? 15.446  -8.246  30.189  1.00 16.85 ? 223 LEU A CD1 1 
ATOM   1823 C  CD2 . LEU A 1 223 ? 16.496  -9.921  31.718  1.00 16.31 ? 223 LEU A CD2 1 
ATOM   1824 N  N   . ALA A 1 224 ? 20.247  -7.971  28.860  1.00 12.19 ? 224 ALA A N   1 
ATOM   1825 C  CA  . ALA A 1 224 ? 21.211  -6.978  29.236  1.00 14.22 ? 224 ALA A CA  1 
ATOM   1826 C  C   . ALA A 1 224 ? 21.287  -5.853  28.235  1.00 14.84 ? 224 ALA A C   1 
ATOM   1827 O  O   . ALA A 1 224 ? 21.310  -4.639  28.600  1.00 15.62 ? 224 ALA A O   1 
ATOM   1828 C  CB  . ALA A 1 224 ? 22.586  -7.644  29.421  1.00 14.76 ? 224 ALA A CB  1 
ATOM   1829 N  N   . LEU A 1 225 ? 21.386  -6.242  26.973  1.00 13.57 ? 225 LEU A N   1 
ATOM   1830 C  CA  . LEU A 1 225 ? 21.435  -5.209  25.936  1.00 13.97 ? 225 LEU A CA  1 
ATOM   1831 C  C   . LEU A 1 225 ? 20.216  -4.306  25.994  1.00 15.74 ? 225 LEU A C   1 
ATOM   1832 O  O   . LEU A 1 225 ? 20.323  -3.091  25.887  1.00 16.94 ? 225 LEU A O   1 
ATOM   1833 C  CB  . LEU A 1 225 ? 21.540  -5.858  24.583  1.00 13.33 ? 225 LEU A CB  1 
ATOM   1834 C  CG  . LEU A 1 225 ? 21.699  -4.998  23.375  1.00 14.24 ? 225 LEU A CG  1 
ATOM   1835 C  CD1 . LEU A 1 225 ? 23.007  -4.192  23.418  1.00 14.90 ? 225 LEU A CD1 1 
ATOM   1836 C  CD2 . LEU A 1 225 ? 21.624  -5.848  22.118  1.00 12.15 ? 225 LEU A CD2 1 
ATOM   1837 N  N   . GLU A 1 226 ? 19.059  -4.919  26.233  1.00 12.38 ? 226 GLU A N   1 
ATOM   1838 C  CA  . GLU A 1 226 ? 17.808  -4.144  26.215  1.00 12.50 ? 226 GLU A CA  1 
ATOM   1839 C  C   . GLU A 1 226 ? 17.619  -3.211  27.422  1.00 13.99 ? 226 GLU A C   1 
ATOM   1840 O  O   . GLU A 1 226 ? 16.750  -2.305  27.370  1.00 15.77 ? 226 GLU A O   1 
ATOM   1841 C  CB  . GLU A 1 226 ? 16.633  -5.107  26.179  1.00 12.35 ? 226 GLU A CB  1 
ATOM   1842 C  CG  . GLU A 1 226 ? 16.438  -5.790  24.810  1.00 13.25 ? 226 GLU A CG  1 
ATOM   1843 C  CD  . GLU A 1 226 ? 15.557  -7.036  24.899  1.00 13.38 ? 226 GLU A CD  1 
ATOM   1844 O  OE1 . GLU A 1 226 ? 15.276  -7.560  26.037  1.00 13.60 ? 226 GLU A OE1 1 
ATOM   1845 O  OE2 . GLU A 1 226 ? 15.144  -7.489  23.856  1.00 12.92 ? 226 GLU A OE2 1 
ATOM   1846 N  N   . THR A 1 227 ? 18.309  -3.467  28.523  1.00 14.06 ? 227 THR A N   1 
ATOM   1847 C  CA  . THR A 1 227 ? 18.048  -2.816  29.815  1.00 15.18 ? 227 THR A CA  1 
ATOM   1848 C  C   . THR A 1 227 ? 19.258  -2.025  30.340  1.00 17.84 ? 227 THR A C   1 
ATOM   1849 O  O   . THR A 1 227 ? 19.092  -1.301  31.355  1.00 19.94 ? 227 THR A O   1 
ATOM   1850 C  CB  . THR A 1 227 ? 17.630  -3.817  30.945  1.00 14.54 ? 227 THR A CB  1 
ATOM   1851 O  OG1 . THR A 1 227 ? 18.616  -4.825  31.110  1.00 15.58 ? 227 THR A OG1 1 
ATOM   1852 C  CG2 . THR A 1 227 ? 16.359  -4.538  30.566  1.00 15.52 ? 227 THR A CG2 1 
ATOM   1853 N  N   . ALA A 1 228 ? 20.439  -2.209  29.725  1.00 17.80 ? 228 ALA A N   1 
ATOM   1854 C  CA  . ALA A 1 228 ? 21.658  -1.595  30.212  1.00 17.24 ? 228 ALA A CA  1 
ATOM   1855 C  C   . ALA A 1 228 ? 21.740  -0.084  29.932  1.00 17.89 ? 228 ALA A C   1 
ATOM   1856 O  O   . ALA A 1 228 ? 22.407  0.604   30.707  1.00 21.05 ? 228 ALA A O   1 
ATOM   1857 C  CB  . ALA A 1 228 ? 22.914  -2.359  29.729  1.00 18.63 ? 228 ALA A CB  1 
ATOM   1858 N  N   . LEU A 1 229 ? 21.060  0.433   28.872  1.00 14.65 ? 229 LEU A N   1 
ATOM   1859 C  CA  . LEU A 1 229 ? 21.419  1.822   28.451  1.00 14.88 ? 229 LEU A CA  1 
ATOM   1860 C  C   . LEU A 1 229 ? 20.298  2.698   28.465  1.00 14.73 ? 229 LEU A C   1 
ATOM   1861 O  O   . LEU A 1 229 ? 19.184  2.293   28.266  1.00 15.68 ? 229 LEU A O   1 
ATOM   1862 C  CB  . LEU A 1 229 ? 21.972  1.822   27.022  1.00 14.05 ? 229 LEU A CB  1 
ATOM   1863 C  CG  . LEU A 1 229 ? 23.018  0.688   26.787  1.00 16.49 ? 229 LEU A CG  1 
ATOM   1864 C  CD1 . LEU A 1 229 ? 23.274  0.571   25.263  1.00 19.99 ? 229 LEU A CD1 1 
ATOM   1865 C  CD2 . LEU A 1 229 ? 24.309  0.938   27.590  1.00 18.82 ? 229 LEU A CD2 1 
ATOM   1866 N  N   . TYR A 1 230 ? 20.653  3.971   28.622  1.00 15.27 ? 230 TYR A N   1 
ATOM   1867 C  CA  . TYR A 1 230 ? 19.724  5.116   28.506  1.00 17.03 ? 230 TYR A CA  1 
ATOM   1868 C  C   . TYR A 1 230 ? 20.159  6.024   27.362  1.00 17.61 ? 230 TYR A C   1 
ATOM   1869 O  O   . TYR A 1 230 ? 21.366  6.131   27.069  1.00 17.34 ? 230 TYR A O   1 
ATOM   1870 C  CB  . TYR A 1 230 ? 19.706  5.927   29.852  1.00 22.38 ? 230 TYR A CB  1 
ATOM   1871 C  CG  . TYR A 1 230 ? 18.986  5.280   30.994  1.00 27.47 ? 230 TYR A CG  1 
ATOM   1872 C  CD1 . TYR A 1 230 ? 17.830  5.840   31.514  1.00 34.31 ? 230 TYR A CD1 1 
ATOM   1873 C  CD2 . TYR A 1 230 ? 19.452  4.081   31.557  1.00 32.51 ? 230 TYR A CD2 1 
ATOM   1874 C  CE1 . TYR A 1 230 ? 17.140  5.221   32.550  1.00 36.08 ? 230 TYR A CE1 1 
ATOM   1875 C  CE2 . TYR A 1 230 ? 18.776  3.454   32.582  1.00 39.34 ? 230 TYR A CE2 1 
ATOM   1876 C  CZ  . TYR A 1 230 ? 17.614  4.032   33.072  1.00 40.17 ? 230 TYR A CZ  1 
ATOM   1877 O  OH  . TYR A 1 230 ? 16.950  3.411   34.107  1.00 42.73 ? 230 TYR A OH  1 
ATOM   1878 N  N   . CYS A 1 231 ? 19.212  6.808   26.819  1.00 18.91 ? 231 CYS A N   1 
ATOM   1879 C  CA  . CYS A 1 231 ? 19.424  7.843   25.804  1.00 20.41 ? 231 CYS A CA  1 
ATOM   1880 C  C   . CYS A 1 231 ? 19.840  9.148   26.387  1.00 18.94 ? 231 CYS A C   1 
ATOM   1881 O  O   . CYS A 1 231 ? 20.378  10.030  25.695  1.00 21.69 ? 231 CYS A O   1 
ATOM   1882 C  CB  . CYS A 1 231 ? 18.133  8.166   25.096  1.00 19.12 ? 231 CYS A CB  1 
ATOM   1883 S  SG  . CYS A 1 231 ? 17.529  6.761   24.167  1.00 21.93 ? 231 CYS A SG  1 
ATOM   1884 N  N   . THR A 1 232 ? 19.543  9.280   27.676  1.00 18.95 ? 232 THR A N   1 
ATOM   1885 C  CA  . THR A 1 232 ? 19.717  10.597  28.357  1.00 18.52 ? 232 THR A CA  1 
ATOM   1886 C  C   . THR A 1 232 ? 20.992  10.689  29.161  1.00 17.56 ? 232 THR A C   1 
ATOM   1887 O  O   . THR A 1 232 ? 21.589  9.652   29.510  1.00 16.68 ? 232 THR A O   1 
ATOM   1888 C  CB  . THR A 1 232 ? 18.505  10.851  29.254  1.00 19.42 ? 232 THR A CB  1 
ATOM   1889 O  OG1 . THR A 1 232 ? 18.157  9.607   29.883  1.00 19.48 ? 232 THR A OG1 1 
ATOM   1890 C  CG2 . THR A 1 232 ? 17.289  11.345  28.442  1.00 22.61 ? 232 THR A CG2 1 
ATOM   1891 N  N   . HIS A 1 233 ? 21.424  11.945  29.491  1.00 18.16 ? 233 HIS A N   1 
ATOM   1892 C  CA  . HIS A 1 233 ? 22.532  12.179  30.427  1.00 22.16 ? 233 HIS A CA  1 
ATOM   1893 C  C   . HIS A 1 233 ? 22.179  11.707  31.810  1.00 20.46 ? 233 HIS A C   1 
ATOM   1894 O  O   . HIS A 1 233 ? 20.974  11.659  32.176  1.00 20.61 ? 233 HIS A O   1 
ATOM   1895 C  CB  . HIS A 1 233 ? 22.896  13.686  30.489  1.00 21.55 ? 233 HIS A CB  1 
ATOM   1896 C  CG  . HIS A 1 233 ? 23.545  14.194  29.223  1.00 25.45 ? 233 HIS A CG  1 
ATOM   1897 N  ND1 . HIS A 1 233 ? 22.877  14.975  28.314  1.00 34.06 ? 233 HIS A ND1 1 
ATOM   1898 C  CD2 . HIS A 1 233 ? 24.830  14.012  28.720  1.00 29.96 ? 233 HIS A CD2 1 
ATOM   1899 C  CE1 . HIS A 1 233 ? 23.707  15.275  27.294  1.00 31.63 ? 233 HIS A CE1 1 
ATOM   1900 N  NE2 . HIS A 1 233 ? 24.902  14.680  27.536  1.00 28.61 ? 233 HIS A NE2 1 
ATOM   1901 N  N   . MET A 1 234 ? 23.223  11.332  32.548  1.00 21.44 ? 234 MET A N   1 
ATOM   1902 C  CA  . MET A 1 234 ? 23.078  10.886  33.929  1.00 23.63 ? 234 MET A CA  1 
ATOM   1903 C  C   . MET A 1 234 ? 22.249  11.817  34.823  1.00 24.33 ? 234 MET A C   1 
ATOM   1904 O  O   . MET A 1 234 ? 21.438  11.352  35.604  1.00 23.47 ? 234 MET A O   1 
ATOM   1905 C  CB  . MET A 1 234 ? 24.416  10.609  34.562  1.00 24.05 ? 234 MET A CB  1 
ATOM   1906 C  CG  . MET A 1 234 ? 24.293  9.757   35.821  1.00 28.81 ? 234 MET A CG  1 
ATOM   1907 S  SD  . MET A 1 234 ? 25.903  9.606   36.580  1.00 32.79 ? 234 MET A SD  1 
ATOM   1908 C  CE  . MET A 1 234 ? 26.464  11.305  36.460  1.00 37.13 ? 234 MET A CE  1 
ATOM   1909 N  N   . ASP A 1 235 ? 22.416  13.131  34.668  1.00 25.86 ? 235 ASP A N   1 
ATOM   1910 C  CA  . ASP A 1 235 ? 21.652  14.073  35.494  1.00 30.87 ? 235 ASP A CA  1 
ATOM   1911 C  C   . ASP A 1 235 ? 20.312  14.579  34.933  1.00 30.69 ? 235 ASP A C   1 
ATOM   1912 O  O   . ASP A 1 235 ? 19.713  15.516  35.492  1.00 29.72 ? 235 ASP A O   1 
ATOM   1913 C  CB  . ASP A 1 235 ? 22.545  15.250  35.898  1.00 37.07 ? 235 ASP A CB  1 
ATOM   1914 C  CG  . ASP A 1 235 ? 22.660  16.301  34.795  1.00 45.01 ? 235 ASP A CG  1 
ATOM   1915 O  OD1 . ASP A 1 235 ? 22.496  15.979  33.579  1.00 46.80 ? 235 ASP A OD1 1 
ATOM   1916 O  OD2 . ASP A 1 235 ? 22.898  17.470  35.161  1.00 52.66 ? 235 ASP A OD2 1 
ATOM   1917 N  N   . ASP A 1 236 ? 19.823  13.976  33.845  1.00 27.43 ? 236 ASP A N   1 
ATOM   1918 C  CA  . ASP A 1 236 ? 18.526  14.300  33.285  1.00 28.67 ? 236 ASP A CA  1 
ATOM   1919 C  C   . ASP A 1 236 ? 17.395  13.917  34.237  1.00 29.46 ? 236 ASP A C   1 
ATOM   1920 O  O   . ASP A 1 236 ? 17.236  12.742  34.602  1.00 26.86 ? 236 ASP A O   1 
ATOM   1921 C  CB  . ASP A 1 236 ? 18.343  13.614  31.913  1.00 26.74 ? 236 ASP A CB  1 
ATOM   1922 C  CG  . ASP A 1 236 ? 17.284  14.303  31.036  1.00 30.01 ? 236 ASP A CG  1 
ATOM   1923 O  OD1 . ASP A 1 236 ? 16.204  14.690  31.524  1.00 33.55 ? 236 ASP A OD1 1 
ATOM   1924 O  OD2 . ASP A 1 236 ? 17.506  14.469  29.820  1.00 26.50 ? 236 ASP A OD2 1 
ATOM   1925 N  N   . PRO A 1 237 ? 16.578  14.901  34.649  1.00 31.13 ? 237 PRO A N   1 
ATOM   1926 C  CA  . PRO A 1 237 ? 15.413  14.612  35.491  1.00 33.62 ? 237 PRO A CA  1 
ATOM   1927 C  C   . PRO A 1 237 ? 14.331  13.736  34.819  1.00 31.69 ? 237 PRO A C   1 
ATOM   1928 O  O   . PRO A 1 237 ? 13.432  13.210  35.491  1.00 32.14 ? 237 PRO A O   1 
ATOM   1929 C  CB  . PRO A 1 237 ? 14.835  16.025  35.772  1.00 32.36 ? 237 PRO A CB  1 
ATOM   1930 C  CG  . PRO A 1 237 ? 15.217  16.787  34.550  1.00 35.97 ? 237 PRO A CG  1 
ATOM   1931 C  CD  . PRO A 1 237 ? 16.642  16.341  34.323  1.00 29.80 ? 237 PRO A CD  1 
ATOM   1932 N  N   . SER A 1 238 ? 14.420  13.576  33.502  1.00 31.21 ? 238 SER A N   1 
ATOM   1933 C  CA  . SER A 1 238 ? 13.431  12.806  32.772  1.00 31.31 ? 238 SER A CA  1 
ATOM   1934 C  C   . SER A 1 238 ? 14.142  11.738  31.963  1.00 28.75 ? 238 SER A C   1 
ATOM   1935 O  O   . SER A 1 238 ? 14.246  11.835  30.733  1.00 27.86 ? 238 SER A O   1 
ATOM   1936 C  CB  . SER A 1 238 ? 12.663  13.719  31.847  1.00 33.35 ? 238 SER A CB  1 
ATOM   1937 O  OG  . SER A 1 238 ? 11.858  14.589  32.615  1.00 38.12 ? 238 SER A OG  1 
ATOM   1938 N  N   . PRO A 1 239 ? 14.597  10.688  32.650  1.00 25.40 ? 239 PRO A N   1 
ATOM   1939 C  CA  . PRO A 1 239 ? 15.425  9.770   31.884  1.00 25.38 ? 239 PRO A CA  1 
ATOM   1940 C  C   . PRO A 1 239 ? 14.632  8.983   30.844  1.00 26.21 ? 239 PRO A C   1 
ATOM   1941 O  O   . PRO A 1 239 ? 13.404  8.862   30.941  1.00 25.39 ? 239 PRO A O   1 
ATOM   1942 C  CB  . PRO A 1 239 ? 15.988  8.862   32.955  1.00 23.47 ? 239 PRO A CB  1 
ATOM   1943 C  CG  . PRO A 1 239 ? 15.085  9.035   34.142  1.00 29.79 ? 239 PRO A CG  1 
ATOM   1944 C  CD  . PRO A 1 239 ? 14.773  10.484  34.091  1.00 23.58 ? 239 PRO A CD  1 
ATOM   1945 N  N   . ARG A 1 240 ? 15.342  8.482   29.840  1.00 25.30 ? 240 ARG A N   1 
ATOM   1946 C  CA  . ARG A 1 240 ? 14.741  7.725   28.772  1.00 23.15 ? 240 ARG A CA  1 
ATOM   1947 C  C   . ARG A 1 240 ? 15.538  6.448   28.527  1.00 20.63 ? 240 ARG A C   1 
ATOM   1948 O  O   . ARG A 1 240 ? 16.675  6.542   28.201  1.00 19.78 ? 240 ARG A O   1 
ATOM   1949 C  CB  . ARG A 1 240 ? 14.674  8.566   27.473  1.00 25.39 ? 240 ARG A CB  1 
ATOM   1950 C  CG  . ARG A 1 240 ? 13.692  9.755   27.484  1.00 31.30 ? 240 ARG A CG  1 
ATOM   1951 C  CD  . ARG A 1 240 ? 13.669  10.563  26.173  1.00 27.14 ? 240 ARG A CD  1 
ATOM   1952 N  NE  . ARG A 1 240 ? 14.805  11.490  25.949  1.00 29.97 ? 240 ARG A NE  1 
ATOM   1953 C  CZ  . ARG A 1 240 ? 15.680  11.391  24.922  1.00 28.74 ? 240 ARG A CZ  1 
ATOM   1954 N  NH1 . ARG A 1 240 ? 15.623  10.367  24.088  1.00 26.15 ? 240 ARG A NH1 1 
ATOM   1955 N  NH2 . ARG A 1 240 ? 16.667  12.272  24.763  1.00 31.66 ? 240 ARG A NH2 1 
ATOM   1956 N  N   . GLU A 1 241 ? 14.913  5.288   28.657  1.00 20.61 ? 241 GLU A N   1 
ATOM   1957 C  CA  . GLU A 1 241 ? 15.616  4.034   28.291  1.00 19.51 ? 241 GLU A CA  1 
ATOM   1958 C  C   . GLU A 1 241 ? 15.979  3.967   26.811  1.00 17.12 ? 241 GLU A C   1 
ATOM   1959 O  O   . GLU A 1 241 ? 15.213  4.415   25.939  1.00 18.35 ? 241 GLU A O   1 
ATOM   1960 C  CB  . GLU A 1 241 ? 14.790  2.815   28.645  1.00 20.76 ? 241 GLU A CB  1 
ATOM   1961 C  CG  . GLU A 1 241 ? 14.469  2.618   30.115  1.00 27.12 ? 241 GLU A CG  1 
ATOM   1962 C  CD  . GLU A 1 241 ? 13.363  1.575   30.349  1.00 29.05 ? 241 GLU A CD  1 
ATOM   1963 O  OE1 . GLU A 1 241 ? 12.555  1.291   29.431  1.00 37.95 ? 241 GLU A OE1 1 
ATOM   1964 O  OE2 . GLU A 1 241 ? 13.275  1.028   31.471  1.00 36.75 ? 241 GLU A OE2 1 
ATOM   1965 N  N   . MET A 1 242 ? 17.148  3.424   26.503  1.00 15.21 ? 242 MET A N   1 
ATOM   1966 C  CA  . MET A 1 242 ? 17.484  3.204   25.103  1.00 11.06 ? 242 MET A CA  1 
ATOM   1967 C  C   . MET A 1 242 ? 16.919  1.823   24.761  1.00 13.10 ? 242 MET A C   1 
ATOM   1968 O  O   . MET A 1 242 ? 17.591  0.741   24.955  1.00 13.43 ? 242 MET A O   1 
ATOM   1969 C  CB  . MET A 1 242 ? 19.022  3.186   24.919  1.00 13.93 ? 242 MET A CB  1 
ATOM   1970 C  CG  . MET A 1 242 ? 19.419  3.086   23.414  1.00 15.22 ? 242 MET A CG  1 
ATOM   1971 S  SD  . MET A 1 242 ? 21.200  3.182   23.181  1.00 15.65 ? 242 MET A SD  1 
ATOM   1972 C  CE  . MET A 1 242 ? 21.460  4.954   23.517  1.00 15.54 ? 242 MET A CE  1 
ATOM   1973 N  N   . ILE A 1 243 ? 15.727  1.867   24.137  1.00 12.55 ? 243 ILE A N   1 
ATOM   1974 C  CA  . ILE A 1 243 ? 15.032  0.682   23.637  1.00 12.26 ? 243 ILE A CA  1 
ATOM   1975 C  C   . ILE A 1 243 ? 14.407  0.995   22.259  1.00 12.42 ? 243 ILE A C   1 
ATOM   1976 O  O   . ILE A 1 243 ? 14.166  2.178   21.912  1.00 12.27 ? 243 ILE A O   1 
ATOM   1977 C  CB  . ILE A 1 243 ? 13.907  0.235   24.606  1.00 12.94 ? 243 ILE A CB  1 
ATOM   1978 C  CG1 . ILE A 1 243 ? 12.994  1.428   24.949  1.00 15.80 ? 243 ILE A CG1 1 
ATOM   1979 C  CG2 . ILE A 1 243 ? 14.499  -0.460  25.876  1.00 15.43 ? 243 ILE A CG2 1 
ATOM   1980 C  CD1 . ILE A 1 243 ? 11.788  1.027   25.819  1.00 15.57 ? 243 ILE A CD1 1 
ATOM   1981 N  N   . ASN A 1 244 ? 14.066  -0.048  21.504  1.00 9.87  ? 244 ASN A N   1 
ATOM   1982 C  CA  . ASN A 1 244 ? 13.364  0.080   20.247  1.00 11.95 ? 244 ASN A CA  1 
ATOM   1983 C  C   . ASN A 1 244 ? 14.092  1.095   19.313  1.00 11.50 ? 244 ASN A C   1 
ATOM   1984 O  O   . ASN A 1 244 ? 13.451  1.939   18.647  1.00 12.20 ? 244 ASN A O   1 
ATOM   1985 C  CB  . ASN A 1 244 ? 11.900  0.536   20.499  1.00 13.44 ? 244 ASN A CB  1 
ATOM   1986 C  CG  . ASN A 1 244 ? 11.178  -0.346  21.447  1.00 15.88 ? 244 ASN A CG  1 
ATOM   1987 O  OD1 . ASN A 1 244 ? 11.313  -1.593  21.383  1.00 14.28 ? 244 ASN A OD1 1 
ATOM   1988 N  ND2 . ASN A 1 244 ? 10.441  0.291   22.395  1.00 15.61 ? 244 ASN A ND2 1 
ATOM   1989 N  N   . ASN A 1 245 ? 15.448  1.010   19.330  1.00 9.98  ? 245 ASN A N   1 
ATOM   1990 C  CA  . ASN A 1 245 ? 16.275  1.875   18.475  1.00 11.03 ? 245 ASN A CA  1 
ATOM   1991 C  C   . ASN A 1 245 ? 16.484  1.264   17.086  1.00 10.38 ? 245 ASN A C   1 
ATOM   1992 O  O   . ASN A 1 245 ? 17.585  1.007   16.658  1.00 11.83 ? 245 ASN A O   1 
ATOM   1993 C  CB  . ASN A 1 245 ? 17.579  2.203   19.183  1.00 10.92 ? 245 ASN A CB  1 
ATOM   1994 C  CG  . ASN A 1 245 ? 18.420  0.960   19.543  1.00 11.69 ? 245 ASN A CG  1 
ATOM   1995 O  OD1 . ASN A 1 245 ? 17.935  -0.170  19.627  1.00 12.53 ? 245 ASN A OD1 1 
ATOM   1996 N  ND2 . ASN A 1 245 ? 19.738  1.185   19.718  1.00 13.64 ? 245 ASN A ND2 1 
ATOM   1997 N  N   . PHE A 1 246 ? 15.420  0.970   16.393  1.00 8.86  ? 246 PHE A N   1 
ATOM   1998 C  CA  . PHE A 1 246 ? 15.455  0.477   15.054  1.00 9.53  ? 246 PHE A CA  1 
ATOM   1999 C  C   . PHE A 1 246 ? 14.439  1.264   14.230  1.00 10.06 ? 246 PHE A C   1 
ATOM   2000 O  O   . PHE A 1 246 ? 13.410  1.784   14.766  1.00 10.70 ? 246 PHE A O   1 
ATOM   2001 C  CB  . PHE A 1 246 ? 15.109  -1.086  14.999  1.00 9.71  ? 246 PHE A CB  1 
ATOM   2002 C  CG  . PHE A 1 246 ? 13.709  -1.436  15.493  1.00 8.66  ? 246 PHE A CG  1 
ATOM   2003 C  CD1 . PHE A 1 246 ? 12.635  -1.585  14.583  1.00 10.37 ? 246 PHE A CD1 1 
ATOM   2004 C  CD2 . PHE A 1 246 ? 13.501  -1.679  16.881  1.00 9.98  ? 246 PHE A CD2 1 
ATOM   2005 C  CE1 . PHE A 1 246 ? 11.324  -1.857  15.050  1.00 9.33  ? 246 PHE A CE1 1 
ATOM   2006 C  CE2 . PHE A 1 246 ? 12.185  -1.932  17.335  1.00 10.91 ? 246 PHE A CE2 1 
ATOM   2007 C  CZ  . PHE A 1 246 ? 11.125  -2.016  16.422  1.00 10.57 ? 246 PHE A CZ  1 
ATOM   2008 N  N   . ARG A 1 247 ? 14.753  1.387   12.932  1.00 9.46  ? 247 ARG A N   1 
ATOM   2009 C  CA  . ARG A 1 247 ? 13.797  2.113   12.021  1.00 9.29  ? 247 ARG A CA  1 
ATOM   2010 C  C   . ARG A 1 247 ? 12.839  1.122   11.407  1.00 8.66  ? 247 ARG A C   1 
ATOM   2011 O  O   . ARG A 1 247 ? 13.213  -0.019  11.186  1.00 8.91  ? 247 ARG A O   1 
ATOM   2012 C  CB  . ARG A 1 247 ? 14.615  2.786   10.888  1.00 9.72  ? 247 ARG A CB  1 
ATOM   2013 C  CG  . ARG A 1 247 ? 13.859  3.900   10.148  1.00 9.51  ? 247 ARG A CG  1 
ATOM   2014 C  CD  . ARG A 1 247 ? 14.638  4.321   8.906   1.00 8.61  ? 247 ARG A CD  1 
ATOM   2015 N  NE  . ARG A 1 247 ? 14.051  5.514   8.282   1.00 8.58  ? 247 ARG A NE  1 
ATOM   2016 C  CZ  . ARG A 1 247 ? 14.565  6.065   7.144   1.00 8.61  ? 247 ARG A CZ  1 
ATOM   2017 N  NH1 . ARG A 1 247 ? 15.574  5.443   6.479   1.00 9.68  ? 247 ARG A NH1 1 
ATOM   2018 N  NH2 . ARG A 1 247 ? 13.998  7.170   6.635   1.00 9.31  ? 247 ARG A NH2 1 
ATOM   2019 N  N   . GLN A 1 248 ? 11.569  1.484   11.251  1.00 8.76  ? 248 GLN A N   1 
ATOM   2020 C  CA  . GLN A 1 248 ? 10.611  0.660   10.509  1.00 8.81  ? 248 GLN A CA  1 
ATOM   2021 C  C   . GLN A 1 248 ? 11.056  0.402   9.075   1.00 9.43  ? 248 GLN A C   1 
ATOM   2022 O  O   . GLN A 1 248 ? 11.817  1.232   8.476   1.00 10.79 ? 248 GLN A O   1 
ATOM   2023 C  CB  . GLN A 1 248 ? 9.221   1.335   10.434  1.00 9.41  ? 248 GLN A CB  1 
ATOM   2024 C  CG  . GLN A 1 248 ? 8.613   1.635   11.811  1.00 9.05  ? 248 GLN A CG  1 
ATOM   2025 C  CD  . GLN A 1 248 ? 8.231   0.381   12.544  1.00 10.14 ? 248 GLN A CD  1 
ATOM   2026 O  OE1 . GLN A 1 248 ? 8.965   -0.097  13.439  1.00 11.30 ? 248 GLN A OE1 1 
ATOM   2027 N  NE2 . GLN A 1 248 ? 7.049   -0.126  12.204  1.00 10.15 ? 248 GLN A NE2 1 
ATOM   2028 N  N   . VAL A 1 249 ? 10.715  -0.768  8.572   1.00 9.50  ? 249 VAL A N   1 
ATOM   2029 C  CA  . VAL A 1 249 ? 11.063  -1.058  7.192   1.00 10.08 ? 249 VAL A CA  1 
ATOM   2030 C  C   . VAL A 1 249 ? 10.468  -0.062  6.179   1.00 11.49 ? 249 VAL A C   1 
ATOM   2031 O  O   . VAL A 1 249 ? 9.308   0.515   6.366   1.00 11.47 ? 249 VAL A O   1 
ATOM   2032 C  CB  . VAL A 1 249 ? 10.672  -2.503  6.772   1.00 10.08 ? 249 VAL A CB  1 
ATOM   2033 C  CG1 . VAL A 1 249 ? 11.585  -3.573  7.443   1.00 10.44 ? 249 VAL A CG1 1 
ATOM   2034 C  CG2 . VAL A 1 249 ? 9.169   -2.718  6.974   1.00 12.22 ? 249 VAL A CG2 1 
ATOM   2035 N  N   . GLN A 1 250 ? 11.224  0.157   5.091   1.00 10.77 ? 250 GLN A N   1 
ATOM   2036 C  CA  . GLN A 1 250 ? 10.828  1.155   4.060   1.00 11.22 ? 250 GLN A CA  1 
ATOM   2037 C  C   . GLN A 1 250 ? 10.170  0.463   2.828   1.00 11.35 ? 250 GLN A C   1 
ATOM   2038 O  O   . GLN A 1 250 ? 10.423  -0.678  2.565   1.00 12.02 ? 250 GLN A O   1 
ATOM   2039 C  CB  . GLN A 1 250 ? 12.081  1.882   3.579   1.00 9.30  ? 250 GLN A CB  1 
ATOM   2040 C  CG  . GLN A 1 250 ? 12.852  2.503   4.734   1.00 10.59 ? 250 GLN A CG  1 
ATOM   2041 C  CD  . GLN A 1 250 ? 12.104  3.632   5.402   1.00 8.99  ? 250 GLN A CD  1 
ATOM   2042 O  OE1 . GLN A 1 250 ? 11.869  4.692   4.813   1.00 12.86 ? 250 GLN A OE1 1 
ATOM   2043 N  NE2 . GLN A 1 250 ? 11.824  3.467   6.727   1.00 7.89  ? 250 GLN A NE2 1 
ATOM   2044 N  N   . LYS A 1 251 ? 9.302   1.155   2.074   1.00 11.52 ? 251 LYS A N   1 
ATOM   2045 C  CA  . LYS A 1 251 ? 8.864   0.672   0.761   1.00 12.86 ? 251 LYS A CA  1 
ATOM   2046 C  C   . LYS A 1 251 ? 10.073  0.429   -0.117  1.00 15.15 ? 251 LYS A C   1 
ATOM   2047 O  O   . LYS A 1 251 ? 11.059  1.188   -0.018  1.00 13.78 ? 251 LYS A O   1 
ATOM   2048 C  CB  . LYS A 1 251 ? 7.906   1.689   0.162   1.00 12.80 ? 251 LYS A CB  1 
ATOM   2049 C  CG  . LYS A 1 251 ? 6.579   1.797   0.966   1.00 14.65 ? 251 LYS A CG  1 
ATOM   2050 C  CD  . LYS A 1 251 ? 5.538   2.425   0.168   1.00 15.19 ? 251 LYS A CD  1 
ATOM   2051 C  CE  . LYS A 1 251 ? 4.081   2.136   0.662   1.00 12.11 ? 251 LYS A CE  1 
ATOM   2052 N  NZ  . LYS A 1 251 ? 3.958   2.179   2.151   1.00 10.78 ? 251 LYS A NZ  1 
ATOM   2053 N  N   . PHE A 1 252 ? 10.023  -0.692  -0.868  1.00 15.57 ? 252 PHE A N   1 
ATOM   2054 C  CA  . PHE A 1 252 ? 11.118  -1.070  -1.767  1.00 17.85 ? 252 PHE A CA  1 
ATOM   2055 C  C   . PHE A 1 252 ? 10.446  -1.638  -3.020  1.00 23.51 ? 252 PHE A C   1 
ATOM   2056 O  O   . PHE A 1 252 ? 10.104  -2.865  -3.033  1.00 27.39 ? 252 PHE A O   1 
ATOM   2057 C  CB  . PHE A 1 252 ? 11.817  -2.252  -1.120  1.00 19.10 ? 252 PHE A CB  1 
ATOM   2058 C  CG  . PHE A 1 252 ? 13.140  -2.613  -1.750  1.00 16.86 ? 252 PHE A CG  1 
ATOM   2059 C  CD1 . PHE A 1 252 ? 14.244  -1.741  -1.666  1.00 17.86 ? 252 PHE A CD1 1 
ATOM   2060 C  CD2 . PHE A 1 252 ? 13.296  -3.856  -2.401  1.00 22.12 ? 252 PHE A CD2 1 
ATOM   2061 C  CE1 . PHE A 1 252 ? 15.470  -2.132  -2.204  1.00 21.67 ? 252 PHE A CE1 1 
ATOM   2062 C  CE2 . PHE A 1 252 ? 14.532  -4.208  -2.951  1.00 20.59 ? 252 PHE A CE2 1 
ATOM   2063 C  CZ  . PHE A 1 252 ? 15.616  -3.355  -2.825  1.00 18.98 ? 252 PHE A CZ  1 
ATOM   2064 N  N   . ASP A 1 253 ? 10.222  -0.832  -4.028  1.00 31.47 ? 253 ASP A N   1 
ATOM   2065 C  CA  . ASP A 1 253 ? 9.335   -1.300  -5.154  1.00 29.97 ? 253 ASP A CA  1 
ATOM   2066 C  C   . ASP A 1 253 ? 10.062  -1.198  -6.458  1.00 30.90 ? 253 ASP A C   1 
ATOM   2067 O  O   . ASP A 1 253 ? 10.826  -0.263  -6.676  1.00 27.88 ? 253 ASP A O   1 
ATOM   2068 C  CB  . ASP A 1 253 ? 8.014   -0.492  -5.238  1.00 35.54 ? 253 ASP A CB  1 
ATOM   2069 C  CG  . ASP A 1 253 ? 6.925   -1.184  -6.134  1.00 41.46 ? 253 ASP A CG  1 
ATOM   2070 O  OD1 . ASP A 1 253 ? 6.696   -2.425  -6.038  1.00 42.45 ? 253 ASP A OD1 1 
ATOM   2071 O  OD2 . ASP A 1 253 ? 6.279   -0.476  -6.937  1.00 41.51 ? 253 ASP A OD2 1 
ATOM   2072 N  N   . GLU A 1 254 ? 9.800   -2.182  -7.317  1.00 30.65 ? 254 GLU A N   1 
ATOM   2073 C  CA  . GLU A 1 254 ? 10.480  -2.315  -8.596  1.00 35.21 ? 254 GLU A CA  1 
ATOM   2074 C  C   . GLU A 1 254 ? 12.006  -2.448  -8.428  1.00 33.70 ? 254 GLU A C   1 
ATOM   2075 O  O   . GLU A 1 254 ? 12.779  -1.989  -9.250  1.00 32.52 ? 254 GLU A O   1 
ATOM   2076 C  CB  . GLU A 1 254 ? 10.013  -1.191  -9.536  1.00 35.99 ? 254 GLU A CB  1 
ATOM   2077 C  CG  . GLU A 1 254 ? 8.514   -1.372  -9.757  1.00 42.26 ? 254 GLU A CG  1 
ATOM   2078 C  CD  . GLU A 1 254 ? 7.912   -0.445  -10.800 1.00 54.68 ? 254 GLU A CD  1 
ATOM   2079 O  OE1 . GLU A 1 254 ? 8.340   0.737   -10.887 1.00 51.98 ? 254 GLU A OE1 1 
ATOM   2080 O  OE2 . GLU A 1 254 ? 6.989   -0.907  -11.518 1.00 53.37 ? 254 GLU A OE2 1 
ATOM   2081 N  N   . ARG A 1 255 ? 12.394  -3.129  -7.345  1.00 31.26 ? 255 ARG A N   1 
ATOM   2082 C  CA  . ARG A 1 255 ? 13.786  -3.364  -7.006  1.00 30.18 ? 255 ARG A CA  1 
ATOM   2083 C  C   . ARG A 1 255 ? 14.018  -4.802  -6.566  1.00 28.46 ? 255 ARG A C   1 
ATOM   2084 O  O   . ARG A 1 255 ? 13.098  -5.518  -6.115  1.00 28.01 ? 255 ARG A O   1 
ATOM   2085 C  CB  . ARG A 1 255 ? 14.226  -2.344  -5.933  1.00 25.11 ? 255 ARG A CB  1 
ATOM   2086 C  CG  . ARG A 1 255 ? 14.140  -0.891  -6.401  1.00 28.05 ? 255 ARG A CG  1 
ATOM   2087 C  CD  . ARG A 1 255 ? 14.717  0.093   -5.377  1.00 24.13 ? 255 ARG A CD  1 
ATOM   2088 N  NE  . ARG A 1 255 ? 16.126  -0.235  -5.162  1.00 25.18 ? 255 ARG A NE  1 
ATOM   2089 C  CZ  . ARG A 1 255 ? 16.810  0.010   -4.050  1.00 23.59 ? 255 ARG A CZ  1 
ATOM   2090 N  NH1 . ARG A 1 255 ? 16.230  0.608   -3.018  1.00 24.52 ? 255 ARG A NH1 1 
ATOM   2091 N  NH2 . ARG A 1 255 ? 18.086  -0.342  -3.975  1.00 19.53 ? 255 ARG A NH2 1 
ATOM   2092 N  N   . LEU A 1 256 ? 15.270  -5.212  -6.737  1.00 26.33 ? 256 LEU A N   1 
ATOM   2093 C  CA  . LEU A 1 256 ? 15.746  -6.504  -6.335  1.00 25.64 ? 256 LEU A CA  1 
ATOM   2094 C  C   . LEU A 1 256 ? 16.754  -6.359  -5.181  1.00 22.19 ? 256 LEU A C   1 
ATOM   2095 O  O   . LEU A 1 256 ? 17.496  -5.357  -5.069  1.00 22.99 ? 256 LEU A O   1 
ATOM   2096 C  CB  . LEU A 1 256 ? 16.398  -7.237  -7.506  1.00 27.44 ? 256 LEU A CB  1 
ATOM   2097 C  CG  . LEU A 1 256 ? 15.381  -7.688  -8.583  1.00 28.74 ? 256 LEU A CG  1 
ATOM   2098 C  CD1 . LEU A 1 256 ? 16.145  -8.062  -9.834  1.00 29.81 ? 256 LEU A CD1 1 
ATOM   2099 C  CD2 . LEU A 1 256 ? 14.447  -8.849  -8.160  1.00 30.12 ? 256 LEU A CD2 1 
ATOM   2100 N  N   . VAL A 1 257 ? 16.765  -7.405  -4.382  1.00 22.16 ? 257 VAL A N   1 
ATOM   2101 C  CA  . VAL A 1 257 ? 17.886  -7.672  -3.506  1.00 19.73 ? 257 VAL A CA  1 
ATOM   2102 C  C   . VAL A 1 257 ? 18.625  -8.888  -4.091  1.00 17.33 ? 257 VAL A C   1 
ATOM   2103 O  O   . VAL A 1 257 ? 18.029  -10.022 -4.283  1.00 18.02 ? 257 VAL A O   1 
ATOM   2104 C  CB  . VAL A 1 257 ? 17.399  -8.000  -2.068  1.00 19.30 ? 257 VAL A CB  1 
ATOM   2105 C  CG1 . VAL A 1 257 ? 18.505  -8.518  -1.140  1.00 19.27 ? 257 VAL A CG1 1 
ATOM   2106 C  CG2 . VAL A 1 257 ? 16.656  -6.852  -1.439  1.00 20.53 ? 257 VAL A CG2 1 
ATOM   2107 N  N   . TYR A 1 258 ? 19.932  -8.750  -4.281  1.00 14.63 ? 258 TYR A N   1 
ATOM   2108 C  CA  . TYR A 1 258 ? 20.729  -9.821  -4.850  1.00 17.15 ? 258 TYR A CA  1 
ATOM   2109 C  C   . TYR A 1 258 ? 21.198  -10.728 -3.766  1.00 15.40 ? 258 TYR A C   1 
ATOM   2110 O  O   . TYR A 1 258 ? 21.412  -10.301 -2.623  1.00 15.08 ? 258 TYR A O   1 
ATOM   2111 C  CB  . TYR A 1 258 ? 21.877  -9.186  -5.628  1.00 16.53 ? 258 TYR A CB  1 
ATOM   2112 C  CG  . TYR A 1 258 ? 21.274  -8.268  -6.664  1.00 20.41 ? 258 TYR A CG  1 
ATOM   2113 C  CD1 . TYR A 1 258 ? 20.717  -8.790  -7.842  1.00 19.74 ? 258 TYR A CD1 1 
ATOM   2114 C  CD2 . TYR A 1 258 ? 21.172  -6.897  -6.432  1.00 21.76 ? 258 TYR A CD2 1 
ATOM   2115 C  CE1 . TYR A 1 258 ? 20.119  -7.943  -8.798  1.00 28.26 ? 258 TYR A CE1 1 
ATOM   2116 C  CE2 . TYR A 1 258 ? 20.561  -6.080  -7.343  1.00 25.61 ? 258 TYR A CE2 1 
ATOM   2117 C  CZ  . TYR A 1 258 ? 20.063  -6.589  -8.527  1.00 24.80 ? 258 TYR A CZ  1 
ATOM   2118 O  OH  . TYR A 1 258 ? 19.474  -5.647  -9.352  1.00 28.39 ? 258 TYR A OH  1 
ATOM   2119 N  N   . THR A 1 259 ? 21.254  -12.036 -4.055  1.00 13.67 ? 259 THR A N   1 
ATOM   2120 C  CA  . THR A 1 259 ? 21.705  -12.983 -3.069  1.00 15.32 ? 259 THR A CA  1 
ATOM   2121 C  C   . THR A 1 259 ? 22.900  -13.757 -3.614  1.00 15.70 ? 259 THR A C   1 
ATOM   2122 O  O   . THR A 1 259 ? 23.019  -14.002 -4.840  1.00 15.90 ? 259 THR A O   1 
ATOM   2123 C  CB  . THR A 1 259 ? 20.613  -13.973 -2.609  1.00 16.11 ? 259 THR A CB  1 
ATOM   2124 O  OG1 . THR A 1 259 ? 20.164  -14.686 -3.750  1.00 19.45 ? 259 THR A OG1 1 
ATOM   2125 C  CG2 . THR A 1 259 ? 19.445  -13.148 -1.977  1.00 14.51 ? 259 THR A CG2 1 
ATOM   2126 N  N   . SER A 1 260 ? 23.820  -14.071 -2.734  1.00 13.32 ? 260 SER A N   1 
ATOM   2127 C  CA  . SER A 1 260 ? 25.013  -14.848 -3.145  1.00 16.75 ? 260 SER A CA  1 
ATOM   2128 C  C   . SER A 1 260 ? 24.700  -16.320 -3.118  1.00 18.79 ? 260 SER A C   1 
ATOM   2129 O  O   . SER A 1 260 ? 25.580  -17.166 -3.438  1.00 21.18 ? 260 SER A O   1 
ATOM   2130 C  CB  . SER A 1 260 ? 26.180  -14.530 -2.226  1.00 16.40 ? 260 SER A CB  1 
ATOM   2131 O  OG  . SER A 1 260 ? 25.907  -15.025 -0.911  1.00 16.58 ? 260 SER A OG  1 
ATOM   2132 N  N   . PHE A 1 261 ? 23.500  -16.662 -2.695  1.00 19.37 ? 261 PHE A N   1 
ATOM   2133 C  CA  . PHE A 1 261 ? 23.088  -18.088 -2.656  1.00 20.91 ? 261 PHE A CA  1 
ATOM   2134 C  C   . PHE A 1 261 ? 21.801  -18.218 -3.482  1.00 24.04 ? 261 PHE A C   1 
ATOM   2135 O  O   . PHE A 1 261 ? 20.996  -17.253 -3.651  1.00 25.46 ? 261 PHE A O   1 
ATOM   2136 C  CB  . PHE A 1 261 ? 22.816  -18.492 -1.208  1.00 17.99 ? 261 PHE A CB  1 
ATOM   2137 C  CG  . PHE A 1 261 ? 21.883  -17.545 -0.499  1.00 16.41 ? 261 PHE A CG  1 
ATOM   2138 C  CD1 . PHE A 1 261 ? 20.528  -17.790 -0.448  1.00 18.32 ? 261 PHE A CD1 1 
ATOM   2139 C  CD2 . PHE A 1 261 ? 22.362  -16.367 0.043   1.00 16.98 ? 261 PHE A CD2 1 
ATOM   2140 C  CE1 . PHE A 1 261 ? 19.646  -16.942 0.187   1.00 19.17 ? 261 PHE A CE1 1 
ATOM   2141 C  CE2 . PHE A 1 261 ? 21.481  -15.489 0.672   1.00 17.64 ? 261 PHE A CE2 1 
ATOM   2142 C  CZ  . PHE A 1 261 ? 20.124  -15.765 0.749   1.00 18.62 ? 261 PHE A CZ  1 
ATOM   2143 N  N   . SER A 1 262 ? 21.575  -19.420 -3.976  1.00 30.19 ? 262 SER A N   1 
ATOM   2144 C  CA  . SER A 1 262 ? 20.249  -19.796 -4.427  1.00 31.53 ? 262 SER A CA  1 
ATOM   2145 C  C   . SER A 1 262 ? 19.845  -20.893 -3.448  1.00 38.58 ? 262 SER A C   1 
ATOM   2146 O  O   . SER A 1 262 ? 20.570  -21.889 -3.274  1.00 38.26 ? 262 SER A O   1 
ATOM   2147 C  CB  . SER A 1 262 ? 20.272  -20.295 -5.876  1.00 37.38 ? 262 SER A CB  1 
ATOM   2148 O  OG  . SER A 1 262 ? 21.539  -20.801 -6.203  1.00 38.24 ? 262 SER A OG  1 
ATOM   2149 N  N   . LYS B 1 3   ? -0.366  18.113  -1.710  1.00 37.95 ? 3   LYS B N   1 
ATOM   2150 C  CA  . LYS B 1 3   ? -0.147  17.143  -2.814  1.00 32.90 ? 3   LYS B CA  1 
ATOM   2151 C  C   . LYS B 1 3   ? 0.665   15.989  -2.253  1.00 30.52 ? 3   LYS B C   1 
ATOM   2152 O  O   . LYS B 1 3   ? 1.598   15.483  -2.939  1.00 29.50 ? 3   LYS B O   1 
ATOM   2153 C  CB  . LYS B 1 3   ? 0.686   17.746  -3.903  1.00 36.72 ? 3   LYS B CB  1 
ATOM   2154 C  CG  . LYS B 1 3   ? 1.851   18.485  -3.295  1.00 38.01 ? 3   LYS B CG  1 
ATOM   2155 C  CD  . LYS B 1 3   ? 1.793   19.976  -3.615  1.00 42.26 ? 3   LYS B CD  1 
ATOM   2156 C  CE  . LYS B 1 3   ? 3.147   20.347  -4.182  1.00 42.07 ? 3   LYS B CE  1 
ATOM   2157 N  NZ  . LYS B 1 3   ? 4.102   19.180  -4.073  1.00 43.79 ? 3   LYS B NZ  1 
ATOM   2158 N  N   . TRP B 1 4   ? 0.367   15.601  -1.011  1.00 17.33 ? 4   TRP B N   1 
ATOM   2159 C  CA  . TRP B 1 4   ? 0.984   14.358  -0.470  1.00 15.19 ? 4   TRP B CA  1 
ATOM   2160 C  C   . TRP B 1 4   ? 0.698   13.173  -1.329  1.00 13.29 ? 4   TRP B C   1 
ATOM   2161 O  O   . TRP B 1 4   ? -0.281  13.146  -2.049  1.00 15.00 ? 4   TRP B O   1 
ATOM   2162 C  CB  . TRP B 1 4   ? 0.536   14.141  0.953   1.00 13.48 ? 4   TRP B CB  1 
ATOM   2163 C  CG  . TRP B 1 4   ? -0.989  13.849  1.128   1.00 12.72 ? 4   TRP B CG  1 
ATOM   2164 C  CD1 . TRP B 1 4   ? -2.017  14.751  1.359   1.00 13.97 ? 4   TRP B CD1 1 
ATOM   2165 C  CD2 . TRP B 1 4   ? -1.652  12.560  1.100   1.00 12.51 ? 4   TRP B CD2 1 
ATOM   2166 N  NE1 . TRP B 1 4   ? -3.240  14.113  1.452   1.00 13.48 ? 4   TRP B NE1 1 
ATOM   2167 C  CE2 . TRP B 1 4   ? -3.082  12.792  1.337   1.00 11.42 ? 4   TRP B CE2 1 
ATOM   2168 C  CE3 . TRP B 1 4   ? -1.211  11.255  0.963   1.00 13.93 ? 4   TRP B CE3 1 
ATOM   2169 C  CZ2 . TRP B 1 4   ? -4.014  11.711  1.437   1.00 11.74 ? 4   TRP B CZ2 1 
ATOM   2170 C  CZ3 . TRP B 1 4   ? -2.175  10.199  0.960   1.00 13.73 ? 4   TRP B CZ3 1 
ATOM   2171 C  CH2 . TRP B 1 4   ? -3.518  10.435  1.254   1.00 13.20 ? 4   TRP B CH2 1 
ATOM   2172 N  N   . THR B 1 5   ? 1.609   12.194  -1.298  1.00 11.89 ? 5   THR B N   1 
ATOM   2173 C  CA  . THR B 1 5   ? 1.481   10.975  -2.116  1.00 10.87 ? 5   THR B CA  1 
ATOM   2174 C  C   . THR B 1 5   ? 1.973   9.770   -1.302  1.00 10.77 ? 5   THR B C   1 
ATOM   2175 O  O   . THR B 1 5   ? 2.300   9.844   -0.058  1.00 10.95 ? 5   THR B O   1 
ATOM   2176 C  CB  . THR B 1 5   ? 2.390   11.031  -3.348  1.00 12.43 ? 5   THR B CB  1 
ATOM   2177 O  OG1 . THR B 1 5   ? 3.746   10.975  -2.873  1.00 13.05 ? 5   THR B OG1 1 
ATOM   2178 C  CG2 . THR B 1 5   ? 2.007   12.317  -4.195  1.00 12.80 ? 5   THR B CG2 1 
ATOM   2179 N  N   . TYR B 1 6   ? 1.900   8.620   -1.929  1.00 12.02 ? 6   TYR B N   1 
ATOM   2180 C  CA  . TYR B 1 6   ? 2.577   7.455   -1.363  1.00 11.72 ? 6   TYR B CA  1 
ATOM   2181 C  C   . TYR B 1 6   ? 3.911   7.093   -1.943  1.00 13.91 ? 6   TYR B C   1 
ATOM   2182 O  O   . TYR B 1 6   ? 4.441   6.023   -1.601  1.00 12.59 ? 6   TYR B O   1 
ATOM   2183 C  CB  . TYR B 1 6   ? 1.668   6.220   -1.510  1.00 12.75 ? 6   TYR B CB  1 
ATOM   2184 C  CG  . TYR B 1 6   ? 0.381   6.295   -0.708  1.00 12.08 ? 6   TYR B CG  1 
ATOM   2185 C  CD1 . TYR B 1 6   ? 0.332   5.699   0.577   1.00 12.09 ? 6   TYR B CD1 1 
ATOM   2186 C  CD2 . TYR B 1 6   ? -0.787  6.931   -1.195  1.00 11.78 ? 6   TYR B CD2 1 
ATOM   2187 C  CE1 . TYR B 1 6   ? -0.861  5.710   1.355   1.00 11.64 ? 6   TYR B CE1 1 
ATOM   2188 C  CE2 . TYR B 1 6   ? -1.966  6.896   -0.455  1.00 12.17 ? 6   TYR B CE2 1 
ATOM   2189 C  CZ  . TYR B 1 6   ? -1.984  6.330   0.840   1.00 13.06 ? 6   TYR B CZ  1 
ATOM   2190 O  OH  . TYR B 1 6   ? -3.178  6.298   1.509   1.00 11.27 ? 6   TYR B OH  1 
ATOM   2191 N  N   . PHE B 1 7   ? 4.461   7.908   -2.812  1.00 14.48 ? 7   PHE B N   1 
ATOM   2192 C  CA  . PHE B 1 7   ? 5.704   7.573   -3.494  1.00 16.22 ? 7   PHE B CA  1 
ATOM   2193 C  C   . PHE B 1 7   ? 6.460   8.841   -3.832  1.00 16.71 ? 7   PHE B C   1 
ATOM   2194 O  O   . PHE B 1 7   ? 5.890   9.748   -4.421  1.00 17.46 ? 7   PHE B O   1 
ATOM   2195 C  CB  . PHE B 1 7   ? 5.415   6.851   -4.839  1.00 21.47 ? 7   PHE B CB  1 
ATOM   2196 C  CG  . PHE B 1 7   ? 6.663   6.508   -5.606  1.00 26.70 ? 7   PHE B CG  1 
ATOM   2197 C  CD1 . PHE B 1 7   ? 7.470   5.413   -5.215  1.00 28.54 ? 7   PHE B CD1 1 
ATOM   2198 C  CD2 . PHE B 1 7   ? 7.063   7.274   -6.697  1.00 32.60 ? 7   PHE B CD2 1 
ATOM   2199 C  CE1 . PHE B 1 7   ? 8.629   5.086   -5.911  1.00 35.61 ? 7   PHE B CE1 1 
ATOM   2200 C  CE2 . PHE B 1 7   ? 8.233   6.953   -7.405  1.00 37.49 ? 7   PHE B CE2 1 
ATOM   2201 C  CZ  . PHE B 1 7   ? 9.008   5.866   -7.014  1.00 39.59 ? 7   PHE B CZ  1 
ATOM   2202 N  N   . GLY B 1 8   ? 7.766   8.838   -3.534  1.00 16.72 ? 8   GLY B N   1 
ATOM   2203 C  CA  . GLY B 1 8   ? 8.671   9.934   -3.921  1.00 19.66 ? 8   GLY B CA  1 
ATOM   2204 C  C   . GLY B 1 8   ? 8.746   11.055  -2.894  1.00 18.69 ? 8   GLY B C   1 
ATOM   2205 O  O   . GLY B 1 8   ? 8.447   10.877  -1.709  1.00 20.12 ? 8   GLY B O   1 
ATOM   2206 N  N   . PRO B 1 9   ? 9.114   12.265  -3.331  1.00 21.29 ? 9   PRO B N   1 
ATOM   2207 C  CA  . PRO B 1 9   ? 9.417   13.313  -2.380  1.00 21.89 ? 9   PRO B CA  1 
ATOM   2208 C  C   . PRO B 1 9   ? 8.351   13.690  -1.452  1.00 20.65 ? 9   PRO B C   1 
ATOM   2209 O  O   . PRO B 1 9   ? 8.680   14.156  -0.377  1.00 20.49 ? 9   PRO B O   1 
ATOM   2210 C  CB  . PRO B 1 9   ? 9.758   14.541  -3.243  1.00 23.37 ? 9   PRO B CB  1 
ATOM   2211 C  CG  . PRO B 1 9   ? 9.447   14.166  -4.625  1.00 23.91 ? 9   PRO B CG  1 
ATOM   2212 C  CD  . PRO B 1 9   ? 9.416   12.663  -4.713  1.00 24.10 ? 9   PRO B CD  1 
ATOM   2213 N  N   . ASP B 1 10  ? 7.087   13.520  -1.866  1.00 16.24 ? 10  ASP B N   1 
ATOM   2214 C  CA  . ASP B 1 10  ? 5.960   13.816  -1.057  1.00 16.46 ? 10  ASP B CA  1 
ATOM   2215 C  C   . ASP B 1 10  ? 5.281   12.606  -0.386  1.00 12.88 ? 10  ASP B C   1 
ATOM   2216 O  O   . ASP B 1 10  ? 4.146   12.740  0.120   1.00 13.33 ? 10  ASP B O   1 
ATOM   2217 C  CB  . ASP B 1 10  ? 4.899   14.546  -1.901  1.00 18.76 ? 10  ASP B CB  1 
ATOM   2218 C  CG  . ASP B 1 10  ? 5.435   15.867  -2.449  1.00 24.59 ? 10  ASP B CG  1 
ATOM   2219 O  OD1 . ASP B 1 10  ? 6.062   16.560  -1.638  1.00 24.14 ? 10  ASP B OD1 1 
ATOM   2220 O  OD2 . ASP B 1 10  ? 5.353   16.103  -3.655  1.00 27.14 ? 10  ASP B OD2 1 
ATOM   2221 N  N   . GLY B 1 11  ? 6.024   11.517  -0.297  1.00 11.60 ? 11  GLY B N   1 
ATOM   2222 C  CA  . GLY B 1 11  ? 5.500   10.265  0.287   1.00 11.01 ? 11  GLY B CA  1 
ATOM   2223 C  C   . GLY B 1 11  ? 5.593   10.274  1.817   1.00 10.34 ? 11  GLY B C   1 
ATOM   2224 O  O   . GLY B 1 11  ? 5.774   11.360  2.466   1.00 10.41 ? 11  GLY B O   1 
ATOM   2225 N  N   . GLU B 1 12  ? 5.321   9.086   2.390   1.00 10.38 ? 12  GLU B N   1 
ATOM   2226 C  CA  . GLU B 1 12  ? 4.925   9.032   3.745   1.00 9.58  ? 12  GLU B CA  1 
ATOM   2227 C  C   . GLU B 1 12  ? 5.914   9.597   4.758   1.00 9.04  ? 12  GLU B C   1 
ATOM   2228 O  O   . GLU B 1 12  ? 5.563   10.000  5.844   1.00 9.49  ? 12  GLU B O   1 
ATOM   2229 C  CB  . GLU B 1 12  ? 4.351   7.665   4.144   1.00 9.77  ? 12  GLU B CB  1 
ATOM   2230 C  CG  . GLU B 1 12  ? 5.437   6.611   4.224   1.00 8.75  ? 12  GLU B CG  1 
ATOM   2231 C  CD  . GLU B 1 12  ? 4.878   5.223   4.165   1.00 8.79  ? 12  GLU B CD  1 
ATOM   2232 O  OE1 . GLU B 1 12  ? 4.496   4.716   5.236   1.00 9.42  ? 12  GLU B OE1 1 
ATOM   2233 O  OE2 . GLU B 1 12  ? 4.829   4.651   3.061   1.00 9.52  ? 12  GLU B OE2 1 
ATOM   2234 N  N   . ASN B 1 13  ? 7.240   9.431   4.462   1.00 10.79 ? 13  ASN B N   1 
ATOM   2235 C  CA  . ASN B 1 13  ? 8.214   9.937   5.427   1.00 10.92 ? 13  ASN B CA  1 
ATOM   2236 C  C   . ASN B 1 13  ? 8.280   11.478  5.478   1.00 10.74 ? 13  ASN B C   1 
ATOM   2237 O  O   . ASN B 1 13  ? 8.815   12.029  6.453   1.00 10.41 ? 13  ASN B O   1 
ATOM   2238 C  CB  . ASN B 1 13  ? 9.631   9.436   5.111   1.00 11.10 ? 13  ASN B CB  1 
ATOM   2239 C  CG  . ASN B 1 13  ? 9.777   7.940   5.323   1.00 11.44 ? 13  ASN B CG  1 
ATOM   2240 O  OD1 . ASN B 1 13  ? 8.847   7.263   5.794   1.00 10.76 ? 13  ASN B OD1 1 
ATOM   2241 N  ND2 . ASN B 1 13  ? 10.941  7.390   4.906   1.00 12.09 ? 13  ASN B ND2 1 
ATOM   2242 N  N   . SER B 1 14  ? 7.562   12.073  4.522   1.00 9.98  ? 14  SER B N   1 
ATOM   2243 C  CA  . SER B 1 14  ? 7.463   13.557  4.433   1.00 10.08 ? 14  SER B CA  1 
ATOM   2244 C  C   . SER B 1 14  ? 6.143   14.100  4.870   1.00 10.67 ? 14  SER B C   1 
ATOM   2245 O  O   . SER B 1 14  ? 5.990   15.334  5.034   1.00 10.21 ? 14  SER B O   1 
ATOM   2246 C  CB  . SER B 1 14  ? 7.729   13.999  3.019   1.00 9.38  ? 14  SER B CB  1 
ATOM   2247 O  OG  . SER B 1 14  ? 9.086   13.817  2.749   1.00 12.21 ? 14  SER B OG  1 
ATOM   2248 N  N   . TRP B 1 15  ? 5.158   13.263  5.148   1.00 8.67  ? 15  TRP B N   1 
ATOM   2249 C  CA  . TRP B 1 15  ? 3.822   13.823  5.558   1.00 10.60 ? 15  TRP B CA  1 
ATOM   2250 C  C   . TRP B 1 15  ? 3.863   14.757  6.717   1.00 10.05 ? 15  TRP B C   1 
ATOM   2251 O  O   . TRP B 1 15  ? 3.154   15.760  6.762   1.00 11.95 ? 15  TRP B O   1 
ATOM   2252 C  CB  . TRP B 1 15  ? 2.822   12.739  5.865   1.00 10.29 ? 15  TRP B CB  1 
ATOM   2253 C  CG  . TRP B 1 15  ? 2.431   11.825  4.703   1.00 8.64  ? 15  TRP B CG  1 
ATOM   2254 C  CD1 . TRP B 1 15  ? 2.732   11.974  3.348   1.00 8.53  ? 15  TRP B CD1 1 
ATOM   2255 C  CD2 . TRP B 1 15  ? 1.650   10.573  4.777   1.00 8.61  ? 15  TRP B CD2 1 
ATOM   2256 N  NE1 . TRP B 1 15  ? 2.200   10.939  2.611   1.00 10.25 ? 15  TRP B NE1 1 
ATOM   2257 C  CE2 . TRP B 1 15  ? 1.540   10.071  3.405   1.00 8.86  ? 15  TRP B CE2 1 
ATOM   2258 C  CE3 . TRP B 1 15  ? 1.045   9.858   5.802   1.00 9.56  ? 15  TRP B CE3 1 
ATOM   2259 C  CZ2 . TRP B 1 15  ? 0.857   8.899   3.103   1.00 9.19  ? 15  TRP B CZ2 1 
ATOM   2260 C  CZ3 . TRP B 1 15  ? 0.368   8.681   5.485   1.00 10.07 ? 15  TRP B CZ3 1 
ATOM   2261 C  CH2 . TRP B 1 15  ? 0.278   8.214   4.170   1.00 9.10  ? 15  TRP B CH2 1 
ATOM   2262 N  N   . SER B 1 16  ? 4.685   14.448  7.722   1.00 11.86 ? 16  SER B N   1 
ATOM   2263 C  CA  . SER B 1 16  ? 4.719   15.149  9.012   1.00 10.96 ? 16  SER B CA  1 
ATOM   2264 C  C   . SER B 1 16  ? 5.257   16.577  8.814   1.00 10.98 ? 16  SER B C   1 
ATOM   2265 O  O   . SER B 1 16  ? 5.016   17.398  9.679   1.00 13.38 ? 16  SER B O   1 
ATOM   2266 C  CB  . SER B 1 16  ? 5.651   14.452  10.001  1.00 12.79 ? 16  SER B CB  1 
ATOM   2267 O  OG  . SER B 1 16  ? 6.974   14.625  9.483   1.00 15.91 ? 16  SER B OG  1 
ATOM   2268 N  N   . LYS B 1 17  ? 5.879   16.820  7.664   1.00 12.90 ? 17  LYS B N   1 
ATOM   2269 C  CA  . LYS B 1 17  ? 6.312   18.244  7.346   1.00 11.08 ? 17  LYS B CA  1 
ATOM   2270 C  C   . LYS B 1 17  ? 5.136   19.124  7.238   1.00 14.39 ? 17  LYS B C   1 
ATOM   2271 O  O   . LYS B 1 17  ? 5.323   20.342  7.549   1.00 14.68 ? 17  LYS B O   1 
ATOM   2272 C  CB  . LYS B 1 17  ? 7.082   18.328  6.025   1.00 11.28 ? 17  LYS B CB  1 
ATOM   2273 C  CG  . LYS B 1 17  ? 8.412   17.519  6.049   1.00 10.48 ? 17  LYS B CG  1 
ATOM   2274 C  CD  . LYS B 1 17  ? 9.079   17.475  4.664   1.00 10.09 ? 17  LYS B CD  1 
ATOM   2275 C  CE  . LYS B 1 17  ? 10.287  16.497  4.416   1.00 11.56 ? 17  LYS B CE  1 
ATOM   2276 N  NZ  . LYS B 1 17  ? 10.832  16.605  3.040   1.00 11.48 ? 17  LYS B NZ  1 
ATOM   2277 N  N   . LYS B 1 18  ? 3.996   18.649  6.735   1.00 12.28 ? 18  LYS B N   1 
ATOM   2278 C  CA  . LYS B 1 18  ? 2.830   19.571  6.536   1.00 12.49 ? 18  LYS B CA  1 
ATOM   2279 C  C   . LYS B 1 18  ? 1.674   19.200  7.485   1.00 13.57 ? 18  LYS B C   1 
ATOM   2280 O  O   . LYS B 1 18  ? 0.771   20.035  7.735   1.00 15.77 ? 18  LYS B O   1 
ATOM   2281 C  CB  . LYS B 1 18  ? 2.326   19.498  5.104   1.00 15.57 ? 18  LYS B CB  1 
ATOM   2282 C  CG  . LYS B 1 18  ? 3.352   19.933  4.024   1.00 20.81 ? 18  LYS B CG  1 
ATOM   2283 C  CD  . LYS B 1 18  ? 2.695   19.961  2.638   1.00 26.08 ? 18  LYS B CD  1 
ATOM   2284 C  CE  . LYS B 1 18  ? 3.404   20.897  1.645   1.00 27.75 ? 18  LYS B CE  1 
ATOM   2285 N  NZ  . LYS B 1 18  ? 2.621   20.978  0.381   1.00 35.12 ? 18  LYS B NZ  1 
ATOM   2286 N  N   . TYR B 1 19  ? 1.715   17.978  8.062   1.00 11.17 ? 19  TYR B N   1 
ATOM   2287 C  CA  . TYR B 1 19  ? 0.604   17.463  8.825   1.00 12.63 ? 19  TYR B CA  1 
ATOM   2288 C  C   . TYR B 1 19  ? 1.255   16.911  10.124  1.00 12.54 ? 19  TYR B C   1 
ATOM   2289 O  O   . TYR B 1 19  ? 1.755   15.710  10.175  1.00 11.52 ? 19  TYR B O   1 
ATOM   2290 C  CB  . TYR B 1 19  ? -0.085  16.294  8.054   1.00 12.50 ? 19  TYR B CB  1 
ATOM   2291 C  CG  . TYR B 1 19  ? -0.643  16.734  6.730   1.00 11.07 ? 19  TYR B CG  1 
ATOM   2292 C  CD1 . TYR B 1 19  ? -1.884  17.325  6.663   1.00 12.92 ? 19  TYR B CD1 1 
ATOM   2293 C  CD2 . TYR B 1 19  ? 0.048   16.514  5.529   1.00 11.73 ? 19  TYR B CD2 1 
ATOM   2294 C  CE1 . TYR B 1 19  ? -2.360  17.717  5.419   1.00 15.43 ? 19  TYR B CE1 1 
ATOM   2295 C  CE2 . TYR B 1 19  ? -0.446  16.934  4.315   1.00 12.38 ? 19  TYR B CE2 1 
ATOM   2296 C  CZ  . TYR B 1 19  ? -1.684  17.517  4.289   1.00 15.10 ? 19  TYR B CZ  1 
ATOM   2297 O  OH  . TYR B 1 19  ? -2.224  17.938  3.041   1.00 19.69 ? 19  TYR B OH  1 
ATOM   2298 N  N   . PRO B 1 20  ? 1.345   17.699  11.183  1.00 12.23 ? 20  PRO B N   1 
ATOM   2299 C  CA  . PRO B 1 20  ? 2.144   17.353  12.336  1.00 13.14 ? 20  PRO B CA  1 
ATOM   2300 C  C   . PRO B 1 20  ? 1.682   16.077  13.050  1.00 11.62 ? 20  PRO B C   1 
ATOM   2301 O  O   . PRO B 1 20  ? 2.501   15.401  13.631  1.00 14.27 ? 20  PRO B O   1 
ATOM   2302 C  CB  . PRO B 1 20  ? 2.093   18.591  13.249  1.00 15.65 ? 20  PRO B CB  1 
ATOM   2303 C  CG  . PRO B 1 20  ? 1.490   19.668  12.398  1.00 15.69 ? 20  PRO B CG  1 
ATOM   2304 C  CD  . PRO B 1 20  ? 0.948   19.142  11.108  1.00 14.40 ? 20  PRO B CD  1 
ATOM   2305 N  N   . SER B 1 21  ? 0.409   15.781  12.990  1.00 12.00 ? 21  SER B N   1 
ATOM   2306 C  CA  . SER B 1 21  ? -0.057  14.584  13.666  1.00 12.77 ? 21  SER B CA  1 
ATOM   2307 C  C   . SER B 1 21  ? 0.504   13.326  13.052  1.00 13.18 ? 21  SER B C   1 
ATOM   2308 O  O   . SER B 1 21  ? 0.488   12.298  13.721  1.00 11.34 ? 21  SER B O   1 
ATOM   2309 C  CB  . SER B 1 21  ? -1.571  14.544  13.656  1.00 13.65 ? 21  SER B CB  1 
ATOM   2310 O  OG  . SER B 1 21  ? -2.128  15.545  14.502  1.00 17.37 ? 21  SER B OG  1 
ATOM   2311 N  N   . CYS B 1 22  ? 0.953   13.402  11.797  1.00 10.74 ? 22  CYS B N   1 
ATOM   2312 C  CA  . CYS B 1 22  ? 1.533   12.200  11.155  1.00 10.37 ? 22  CYS B CA  1 
ATOM   2313 C  C   . CYS B 1 22  ? 2.831   11.806  11.782  1.00 11.60 ? 22  CYS B C   1 
ATOM   2314 O  O   . CYS B 1 22  ? 3.269   10.663  11.585  1.00 13.00 ? 22  CYS B O   1 
ATOM   2315 C  CB  . CYS B 1 22  ? 1.720   12.354  9.634   1.00 9.45  ? 22  CYS B CB  1 
ATOM   2316 S  SG  . CYS B 1 22  ? 0.147   12.703  8.757   1.00 11.01 ? 22  CYS B SG  1 
ATOM   2317 N  N   . GLY B 1 23  ? 3.519   12.753  12.481  1.00 13.03 ? 23  GLY B N   1 
ATOM   2318 C  CA  . GLY B 1 23  ? 4.730   12.418  13.286  1.00 14.68 ? 23  GLY B CA  1 
ATOM   2319 C  C   . GLY B 1 23  ? 4.409   12.322  14.766  1.00 14.76 ? 23  GLY B C   1 
ATOM   2320 O  O   . GLY B 1 23  ? 5.319   12.294  15.614  1.00 17.57 ? 23  GLY B O   1 
ATOM   2321 N  N   . GLY B 1 24  ? 3.111   12.276  15.162  1.00 14.67 ? 24  GLY B N   1 
ATOM   2322 C  CA  . GLY B 1 24  ? 2.772   12.252  16.593  1.00 16.51 ? 24  GLY B CA  1 
ATOM   2323 C  C   . GLY B 1 24  ? 2.483   10.868  17.095  1.00 18.35 ? 24  GLY B C   1 
ATOM   2324 O  O   . GLY B 1 24  ? 2.948   9.906   16.540  1.00 17.34 ? 24  GLY B O   1 
ATOM   2325 N  N   . LEU B 1 25  ? 1.760   10.778  18.184  1.00 20.00 ? 25  LEU B N   1 
ATOM   2326 C  CA  . LEU B 1 25  ? 1.581   9.413   18.748  1.00 22.86 ? 25  LEU B CA  1 
ATOM   2327 C  C   . LEU B 1 25  ? 0.326   8.751   18.223  1.00 18.40 ? 25  LEU B C   1 
ATOM   2328 O  O   . LEU B 1 25  ? -0.431  9.338   17.427  1.00 18.92 ? 25  LEU B O   1 
ATOM   2329 C  CB  . LEU B 1 25  ? 1.636   9.434   20.271  1.00 26.44 ? 25  LEU B CB  1 
ATOM   2330 C  CG  . LEU B 1 25  ? 3.038   9.735   20.883  1.00 25.36 ? 25  LEU B CG  1 
ATOM   2331 C  CD1 . LEU B 1 25  ? 2.905   10.120  22.344  1.00 30.90 ? 25  LEU B CD1 1 
ATOM   2332 C  CD2 . LEU B 1 25  ? 4.136   8.670   20.663  1.00 30.66 ? 25  LEU B CD2 1 
ATOM   2333 N  N   . LEU B 1 26  ? 0.165   7.481   18.629  1.00 20.05 ? 26  LEU B N   1 
ATOM   2334 C  CA  . LEU B 1 26  ? -1.029  6.685   18.350  1.00 18.43 ? 26  LEU B CA  1 
ATOM   2335 C  C   . LEU B 1 26  ? -1.255  6.442   16.835  1.00 14.19 ? 26  LEU B C   1 
ATOM   2336 O  O   . LEU B 1 26  ? -2.419  6.372   16.367  1.00 13.77 ? 26  LEU B O   1 
ATOM   2337 C  CB  . LEU B 1 26  ? -2.276  7.347   18.958  1.00 21.49 ? 26  LEU B CB  1 
ATOM   2338 C  CG  . LEU B 1 26  ? -2.285  7.498   20.510  1.00 26.07 ? 26  LEU B CG  1 
ATOM   2339 C  CD1 . LEU B 1 26  ? -3.538  8.241   20.982  1.00 29.55 ? 26  LEU B CD1 1 
ATOM   2340 C  CD2 . LEU B 1 26  ? -2.156  6.146   21.210  1.00 26.14 ? 26  LEU B CD2 1 
ATOM   2341 N  N   . GLN B 1 27  ? -0.191  6.328   16.077  1.00 13.56 ? 27  GLN B N   1 
ATOM   2342 C  CA  . GLN B 1 27  ? -0.355  6.240   14.587  1.00 11.05 ? 27  GLN B CA  1 
ATOM   2343 C  C   . GLN B 1 27  ? -0.718  4.802   14.153  1.00 10.88 ? 27  GLN B C   1 
ATOM   2344 O  O   . GLN B 1 27  ? -0.236  3.797   14.730  1.00 11.76 ? 27  GLN B O   1 
ATOM   2345 C  CB  . GLN B 1 27  ? 0.948   6.719   13.897  1.00 12.23 ? 27  GLN B CB  1 
ATOM   2346 C  CG  . GLN B 1 27  ? 1.122   8.212   14.108  1.00 11.60 ? 27  GLN B CG  1 
ATOM   2347 C  CD  . GLN B 1 27  ? 0.047   9.011   13.430  1.00 9.04  ? 27  GLN B CD  1 
ATOM   2348 O  OE1 . GLN B 1 27  ? 0.047   9.161   12.183  1.00 9.92  ? 27  GLN B OE1 1 
ATOM   2349 N  NE2 . GLN B 1 27  ? -0.865  9.530   14.220  1.00 10.22 ? 27  GLN B NE2 1 
ATOM   2350 N  N   . SER B 1 28  ? -1.487  4.721   13.059  1.00 10.38 ? 28  SER B N   1 
ATOM   2351 C  CA  . SER B 1 28  ? -1.856  3.450   12.410  1.00 9.56  ? 28  SER B CA  1 
ATOM   2352 C  C   . SER B 1 28  ? -1.294  3.500   10.960  1.00 10.16 ? 28  SER B C   1 
ATOM   2353 O  O   . SER B 1 28  ? -1.054  4.585   10.432  1.00 10.22 ? 28  SER B O   1 
ATOM   2354 C  CB  . SER B 1 28  ? -3.387  3.436   12.345  1.00 9.25  ? 28  SER B CB  1 
ATOM   2355 O  OG  . SER B 1 28  ? -3.904  3.378   13.653  1.00 9.59  ? 28  SER B OG  1 
ATOM   2356 N  N   . PRO B 1 29  ? -1.168  2.370   10.294  1.00 8.92  ? 29  PRO B N   1 
ATOM   2357 C  CA  . PRO B 1 29  ? -1.535  1.003   10.740  1.00 9.28  ? 29  PRO B CA  1 
ATOM   2358 C  C   . PRO B 1 29  ? -0.398  0.404   11.577  1.00 9.24  ? 29  PRO B C   1 
ATOM   2359 O  O   . PRO B 1 29  ? 0.648   1.034   11.822  1.00 10.22 ? 29  PRO B O   1 
ATOM   2360 C  CB  . PRO B 1 29  ? -1.721  0.216   9.422   1.00 9.51  ? 29  PRO B CB  1 
ATOM   2361 C  CG  . PRO B 1 29  ? -0.622  0.828   8.552   1.00 8.98  ? 29  PRO B CG  1 
ATOM   2362 C  CD  . PRO B 1 29  ? -0.686  2.323   8.883   1.00 8.66  ? 29  PRO B CD  1 
ATOM   2363 N  N   . ILE B 1 30  ? -0.685  -0.815  12.042  1.00 9.65  ? 30  ILE B N   1 
ATOM   2364 C  CA  . ILE B 1 30  ? 0.323   -1.570  12.795  1.00 9.03  ? 30  ILE B CA  1 
ATOM   2365 C  C   . ILE B 1 30  ? 0.349   -3.047  12.404  1.00 9.10  ? 30  ILE B C   1 
ATOM   2366 O  O   . ILE B 1 30  ? -0.543  -3.539  11.694  1.00 10.14 ? 30  ILE B O   1 
ATOM   2367 C  CB  . ILE B 1 30  ? -0.035  -1.524  14.307  1.00 9.47  ? 30  ILE B CB  1 
ATOM   2368 C  CG1 . ILE B 1 30  ? -1.489  -2.028  14.560  1.00 10.23 ? 30  ILE B CG1 1 
ATOM   2369 C  CG2 . ILE B 1 30  ? 0.153   -0.051  14.833  1.00 10.27 ? 30  ILE B CG2 1 
ATOM   2370 C  CD1 . ILE B 1 30  ? -1.785  -2.197  16.061  1.00 12.60 ? 30  ILE B CD1 1 
ATOM   2371 N  N   . ASP B 1 31  ? 1.436   -3.726  12.849  1.00 9.81  ? 31  ASP B N   1 
ATOM   2372 C  CA  . ASP B 1 31  ? 1.567   -5.162  12.663  1.00 10.55 ? 31  ASP B CA  1 
ATOM   2373 C  C   . ASP B 1 31  ? 0.974   -5.852  13.835  1.00 11.02 ? 31  ASP B C   1 
ATOM   2374 O  O   . ASP B 1 31  ? 1.344   -5.558  14.965  1.00 13.80 ? 31  ASP B O   1 
ATOM   2375 C  CB  . ASP B 1 31  ? 3.057   -5.531  12.615  1.00 10.51 ? 31  ASP B CB  1 
ATOM   2376 C  CG  . ASP B 1 31  ? 3.238   -7.030  12.449  1.00 13.29 ? 31  ASP B CG  1 
ATOM   2377 O  OD1 . ASP B 1 31  ? 2.764   -7.562  11.451  1.00 15.08 ? 31  ASP B OD1 1 
ATOM   2378 O  OD2 . ASP B 1 31  ? 3.885   -7.604  13.334  1.00 16.18 ? 31  ASP B OD2 1 
ATOM   2379 N  N   . LEU B 1 32  ? 0.080   -6.792  13.573  1.00 12.19 ? 32  LEU B N   1 
ATOM   2380 C  CA  . LEU B 1 32  ? -0.639  -7.452  14.655  1.00 13.14 ? 32  LEU B CA  1 
ATOM   2381 C  C   . LEU B 1 32  ? 0.148   -8.729  14.909  1.00 14.50 ? 32  LEU B C   1 
ATOM   2382 O  O   . LEU B 1 32  ? 0.198   -9.577  14.046  1.00 17.75 ? 32  LEU B O   1 
ATOM   2383 C  CB  . LEU B 1 32  ? -2.068  -7.769  14.167  1.00 14.37 ? 32  LEU B CB  1 
ATOM   2384 C  CG  . LEU B 1 32  ? -2.885  -6.493  13.816  1.00 15.61 ? 32  LEU B CG  1 
ATOM   2385 C  CD1 . LEU B 1 32  ? -4.190  -6.860  13.072  1.00 16.40 ? 32  LEU B CD1 1 
ATOM   2386 C  CD2 . LEU B 1 32  ? -3.204  -5.574  15.006  1.00 18.98 ? 32  LEU B CD2 1 
ATOM   2387 N  N   . HIS B 1 33  ? 0.845   -8.791  16.054  1.00 13.84 ? 33  HIS B N   1 
ATOM   2388 C  CA  . HIS B 1 33  ? 1.709   -9.937  16.364  1.00 13.67 ? 33  HIS B CA  1 
ATOM   2389 C  C   . HIS B 1 33  ? 1.546   -10.281 17.849  1.00 11.85 ? 33  HIS B C   1 
ATOM   2390 O  O   . HIS B 1 33  ? 1.226   -9.457  18.686  1.00 13.40 ? 33  HIS B O   1 
ATOM   2391 C  CB  . HIS B 1 33  ? 3.182   -9.714  15.930  1.00 13.83 ? 33  HIS B CB  1 
ATOM   2392 C  CG  . HIS B 1 33  ? 3.855   -8.557  16.638  1.00 15.39 ? 33  HIS B CG  1 
ATOM   2393 N  ND1 . HIS B 1 33  ? 3.594   -7.276  16.303  1.00 16.67 ? 33  HIS B ND1 1 
ATOM   2394 C  CD2 . HIS B 1 33  ? 4.802   -8.513  17.654  1.00 15.12 ? 33  HIS B CD2 1 
ATOM   2395 C  CE1 . HIS B 1 33  ? 4.316   -6.451  17.114  1.00 19.04 ? 33  HIS B CE1 1 
ATOM   2396 N  NE2 . HIS B 1 33  ? 5.046   -7.213  17.920  1.00 17.44 ? 33  HIS B NE2 1 
ATOM   2397 N  N   . SER B 1 34  ? 1.882   -11.514 18.183  1.00 14.00 ? 34  SER B N   1 
ATOM   2398 C  CA  . SER B 1 34  ? 1.534   -12.004 19.516  1.00 14.45 ? 34  SER B CA  1 
ATOM   2399 C  C   . SER B 1 34  ? 2.033   -11.226 20.689  1.00 13.89 ? 34  SER B C   1 
ATOM   2400 O  O   . SER B 1 34  ? 1.314   -11.149 21.679  1.00 14.86 ? 34  SER B O   1 
ATOM   2401 C  CB  . SER B 1 34  ? 1.965   -13.478 19.649  1.00 18.05 ? 34  SER B CB  1 
ATOM   2402 O  OG  . SER B 1 34  ? 3.370   -13.539 19.591  1.00 21.62 ? 34  SER B OG  1 
ATOM   2403 N  N   . ASP B 1 35  ? 3.254   -10.650 20.655  1.00 13.81 ? 35  ASP B N   1 
ATOM   2404 C  CA  . ASP B 1 35  ? 3.762   -9.931  21.829  1.00 15.22 ? 35  ASP B CA  1 
ATOM   2405 C  C   . ASP B 1 35  ? 2.930   -8.732  22.272  1.00 16.60 ? 35  ASP B C   1 
ATOM   2406 O  O   . ASP B 1 35  ? 3.030   -8.258  23.444  1.00 21.63 ? 35  ASP B O   1 
ATOM   2407 C  CB  . ASP B 1 35  ? 5.198   -9.416  21.558  1.00 17.88 ? 35  ASP B CB  1 
ATOM   2408 C  CG  . ASP B 1 35  ? 6.077   -10.482 20.962  1.00 18.86 ? 35  ASP B CG  1 
ATOM   2409 O  OD1 . ASP B 1 35  ? 5.841   -10.868 19.789  1.00 19.04 ? 35  ASP B OD1 1 
ATOM   2410 O  OD2 . ASP B 1 35  ? 7.052   -10.832 21.673  1.00 19.81 ? 35  ASP B OD2 1 
ATOM   2411 N  N   . ILE B 1 36  ? 2.073   -8.243  21.393  1.00 16.42 ? 36  ILE B N   1 
ATOM   2412 C  CA  . ILE B 1 36  ? 1.326   -7.051  21.748  1.00 16.02 ? 36  ILE B CA  1 
ATOM   2413 C  C   . ILE B 1 36  ? -0.170  -7.306  21.811  1.00 14.26 ? 36  ILE B C   1 
ATOM   2414 O  O   . ILE B 1 36  ? -0.942  -6.368  22.005  1.00 14.88 ? 36  ILE B O   1 
ATOM   2415 C  CB  . ILE B 1 36  ? 1.711   -5.819  20.872  1.00 16.39 ? 36  ILE B CB  1 
ATOM   2416 C  CG1 . ILE B 1 36  ? 1.601   -6.168  19.400  1.00 19.16 ? 36  ILE B CG1 1 
ATOM   2417 C  CG2 . ILE B 1 36  ? 3.174   -5.449  21.191  1.00 19.80 ? 36  ILE B CG2 1 
ATOM   2418 C  CD1 . ILE B 1 36  ? 0.236   -6.152  18.831  1.00 17.97 ? 36  ILE B CD1 1 
ATOM   2419 N  N   . LEU B 1 37  ? -0.546  -8.563  21.698  1.00 14.08 ? 37  LEU B N   1 
ATOM   2420 C  CA  . LEU B 1 37  ? -2.005  -8.947  21.707  1.00 15.11 ? 37  LEU B CA  1 
ATOM   2421 C  C   . LEU B 1 37  ? -2.422  -9.310  23.126  1.00 15.97 ? 37  LEU B C   1 
ATOM   2422 O  O   . LEU B 1 37  ? -1.676  -10.012 23.798  1.00 19.59 ? 37  LEU B O   1 
ATOM   2423 C  CB  . LEU B 1 37  ? -2.310  -10.128 20.792  1.00 15.15 ? 37  LEU B CB  1 
ATOM   2424 C  CG  . LEU B 1 37  ? -2.020  -9.997  19.278  1.00 16.48 ? 37  LEU B CG  1 
ATOM   2425 C  CD1 . LEU B 1 37  ? -2.265  -11.245 18.487  1.00 18.86 ? 37  LEU B CD1 1 
ATOM   2426 C  CD2 . LEU B 1 37  ? -2.724  -8.816  18.652  1.00 14.99 ? 37  LEU B CD2 1 
ATOM   2427 N  N   . GLN B 1 38  ? -3.630  -8.909  23.538  1.00 15.06 ? 38  GLN B N   1 
ATOM   2428 C  CA  . GLN B 1 38  ? -4.134  -9.306  24.891  1.00 14.66 ? 38  GLN B CA  1 
ATOM   2429 C  C   . GLN B 1 38  ? -5.628  -9.558  24.795  1.00 14.62 ? 38  GLN B C   1 
ATOM   2430 O  O   . GLN B 1 38  ? -6.393  -8.667  24.418  1.00 16.58 ? 38  GLN B O   1 
ATOM   2431 C  CB  . GLN B 1 38  ? -3.841  -8.308  25.983  1.00 17.98 ? 38  GLN B CB  1 
ATOM   2432 C  CG  . GLN B 1 38  ? -4.266  -8.758  27.399  1.00 19.25 ? 38  GLN B CG  1 
ATOM   2433 C  CD  . GLN B 1 38  ? -3.904  -7.670  28.363  1.00 25.36 ? 38  GLN B CD  1 
ATOM   2434 O  OE1 . GLN B 1 38  ? -2.721  -7.377  28.557  1.00 33.62 ? 38  GLN B OE1 1 
ATOM   2435 N  NE2 . GLN B 1 38  ? -4.876  -7.012  28.903  1.00 26.92 ? 38  GLN B NE2 1 
ATOM   2436 N  N   . TYR B 1 39  ? -6.021  -10.758 25.214  1.00 14.28 ? 39  TYR B N   1 
ATOM   2437 C  CA  . TYR B 1 39  ? -7.437  -11.110 25.177  1.00 14.66 ? 39  TYR B CA  1 
ATOM   2438 C  C   . TYR B 1 39  ? -8.240  -10.193 26.086  1.00 13.61 ? 39  TYR B C   1 
ATOM   2439 O  O   . TYR B 1 39  ? -7.858  -9.977  27.252  1.00 14.24 ? 39  TYR B O   1 
ATOM   2440 C  CB  . TYR B 1 39  ? -7.674  -12.600 25.580  1.00 16.16 ? 39  TYR B CB  1 
ATOM   2441 C  CG  . TYR B 1 39  ? -9.148  -12.963 25.748  1.00 14.59 ? 39  TYR B CG  1 
ATOM   2442 C  CD1 . TYR B 1 39  ? -10.027 -12.920 24.676  1.00 15.63 ? 39  TYR B CD1 1 
ATOM   2443 C  CD2 . TYR B 1 39  ? -9.662  -13.295 27.029  1.00 15.73 ? 39  TYR B CD2 1 
ATOM   2444 C  CE1 . TYR B 1 39  ? -11.367 -13.220 24.827  1.00 17.15 ? 39  TYR B CE1 1 
ATOM   2445 C  CE2 . TYR B 1 39  ? -11.006 -13.602 27.168  1.00 16.92 ? 39  TYR B CE2 1 
ATOM   2446 C  CZ  . TYR B 1 39  ? -11.833 -13.612 26.068  1.00 18.01 ? 39  TYR B CZ  1 
ATOM   2447 O  OH  . TYR B 1 39  ? -13.196 -13.929 26.131  1.00 20.20 ? 39  TYR B OH  1 
ATOM   2448 N  N   . ASP B 1 40  ? -9.403  -9.758  25.605  1.00 15.21 ? 40  ASP B N   1 
ATOM   2449 C  CA  . ASP B 1 40  ? -10.281 -8.856  26.416  1.00 15.01 ? 40  ASP B CA  1 
ATOM   2450 C  C   . ASP B 1 40  ? -11.718 -9.370  26.302  1.00 16.73 ? 40  ASP B C   1 
ATOM   2451 O  O   . ASP B 1 40  ? -12.379 -9.143  25.294  1.00 15.02 ? 40  ASP B O   1 
ATOM   2452 C  CB  . ASP B 1 40  ? -10.096 -7.386  26.028  1.00 17.71 ? 40  ASP B CB  1 
ATOM   2453 C  CG  . ASP B 1 40  ? -10.982 -6.441  26.816  1.00 19.21 ? 40  ASP B CG  1 
ATOM   2454 O  OD1 . ASP B 1 40  ? -11.803 -6.871  27.633  1.00 19.33 ? 40  ASP B OD1 1 
ATOM   2455 O  OD2 . ASP B 1 40  ? -10.824 -5.208  26.644  1.00 21.60 ? 40  ASP B OD2 1 
ATOM   2456 N  N   . ALA B 1 41  ? -12.228 -10.030 27.341  1.00 14.72 ? 41  ALA B N   1 
ATOM   2457 C  CA  . ALA B 1 41  ? -13.563 -10.627 27.292  1.00 16.28 ? 41  ALA B CA  1 
ATOM   2458 C  C   . ALA B 1 41  ? -14.695 -9.557  27.220  1.00 15.21 ? 41  ALA B C   1 
ATOM   2459 O  O   . ALA B 1 41  ? -15.835 -9.890  26.873  1.00 17.89 ? 41  ALA B O   1 
ATOM   2460 C  CB  . ALA B 1 41  ? -13.728 -11.474 28.547  1.00 15.93 ? 41  ALA B CB  1 
ATOM   2461 N  N   . SER B 1 42  ? -14.385 -8.311  27.492  1.00 17.57 ? 42  SER B N   1 
ATOM   2462 C  CA  . SER B 1 42  ? -15.408 -7.272  27.362  1.00 16.38 ? 42  SER B CA  1 
ATOM   2463 C  C   . SER B 1 42  ? -15.672 -6.789  25.877  1.00 15.76 ? 42  SER B C   1 
ATOM   2464 O  O   . SER B 1 42  ? -16.552 -5.914  25.581  1.00 16.52 ? 42  SER B O   1 
ATOM   2465 C  CB  . SER B 1 42  ? -15.028 -6.092  28.231  1.00 21.61 ? 42  SER B CB  1 
ATOM   2466 O  OG  . SER B 1 42  ? -14.092 -5.253  27.618  1.00 25.44 ? 42  SER B OG  1 
ATOM   2467 N  N   . LEU B 1 43  ? -14.874 -7.321  24.956  1.00 13.13 ? 43  LEU B N   1 
ATOM   2468 C  CA  . LEU B 1 43  ? -15.093 -7.063  23.512  1.00 12.56 ? 43  LEU B CA  1 
ATOM   2469 C  C   . LEU B 1 43  ? -16.189 -7.950  22.923  1.00 13.43 ? 43  LEU B C   1 
ATOM   2470 O  O   . LEU B 1 43  ? -15.915 -8.998  22.296  1.00 13.78 ? 43  LEU B O   1 
ATOM   2471 C  CB  . LEU B 1 43  ? -13.753 -7.165  22.725  1.00 13.75 ? 43  LEU B CB  1 
ATOM   2472 C  CG  . LEU B 1 43  ? -12.649 -6.190  23.183  1.00 13.88 ? 43  LEU B CG  1 
ATOM   2473 C  CD1 . LEU B 1 43  ? -11.337 -6.512  22.423  1.00 13.95 ? 43  LEU B CD1 1 
ATOM   2474 C  CD2 . LEU B 1 43  ? -13.056 -4.751  22.981  1.00 13.75 ? 43  LEU B CD2 1 
ATOM   2475 N  N   . THR B 1 44  ? -17.420 -7.534  23.181  1.00 15.05 ? 44  THR B N   1 
ATOM   2476 C  CA  . THR B 1 44  ? -18.618 -8.232  22.745  1.00 14.91 ? 44  THR B CA  1 
ATOM   2477 C  C   . THR B 1 44  ? -18.909 -7.951  21.263  1.00 14.40 ? 44  THR B C   1 
ATOM   2478 O  O   . THR B 1 44  ? -18.267 -7.030  20.644  1.00 12.90 ? 44  THR B O   1 
ATOM   2479 C  CB  . THR B 1 44  ? -19.768 -7.786  23.650  1.00 15.81 ? 44  THR B CB  1 
ATOM   2480 O  OG1 . THR B 1 44  ? -19.730 -6.363  23.770  1.00 20.15 ? 44  THR B OG1 1 
ATOM   2481 C  CG2 . THR B 1 44  ? -19.518 -8.275  25.104  1.00 16.71 ? 44  THR B CG2 1 
ATOM   2482 N  N   . PRO B 1 45  ? -19.846 -8.705  20.654  1.00 14.18 ? 45  PRO B N   1 
ATOM   2483 C  CA  . PRO B 1 45  ? -20.061 -8.599  19.207  1.00 13.99 ? 45  PRO B CA  1 
ATOM   2484 C  C   . PRO B 1 45  ? -20.620 -7.226  18.803  1.00 16.60 ? 45  PRO B C   1 
ATOM   2485 O  O   . PRO B 1 45  ? -21.510 -6.710  19.491  1.00 18.10 ? 45  PRO B O   1 
ATOM   2486 C  CB  . PRO B 1 45  ? -21.039 -9.740  18.896  1.00 17.15 ? 45  PRO B CB  1 
ATOM   2487 C  CG  . PRO B 1 45  ? -20.628 -10.757 19.876  1.00 17.36 ? 45  PRO B CG  1 
ATOM   2488 C  CD  . PRO B 1 45  ? -20.477 -9.971  21.121  1.00 15.35 ? 45  PRO B CD  1 
ATOM   2489 N  N   . LEU B 1 46  ? -20.087 -6.649  17.709  1.00 15.15 ? 46  LEU B N   1 
ATOM   2490 C  CA  . LEU B 1 46  ? -20.756 -5.432  17.147  1.00 15.59 ? 46  LEU B CA  1 
ATOM   2491 C  C   . LEU B 1 46  ? -22.042 -5.887  16.436  1.00 14.79 ? 46  LEU B C   1 
ATOM   2492 O  O   . LEU B 1 46  ? -22.115 -7.000  15.914  1.00 15.82 ? 46  LEU B O   1 
ATOM   2493 C  CB  . LEU B 1 46  ? -19.852 -4.748  16.120  1.00 16.27 ? 46  LEU B CB  1 
ATOM   2494 C  CG  . LEU B 1 46  ? -18.578 -4.134  16.698  1.00 19.56 ? 46  LEU B CG  1 
ATOM   2495 C  CD1 . LEU B 1 46  ? -17.764 -3.579  15.547  1.00 18.93 ? 46  LEU B CD1 1 
ATOM   2496 C  CD2 . LEU B 1 46  ? -18.837 -3.001  17.670  1.00 21.93 ? 46  LEU B CD2 1 
ATOM   2497 N  N   . GLU B 1 47  ? -23.033 -4.987  16.349  1.00 16.16 ? 47  GLU B N   1 
ATOM   2498 C  CA  . GLU B 1 47  ? -24.167 -5.245  15.481  1.00 18.45 ? 47  GLU B CA  1 
ATOM   2499 C  C   . GLU B 1 47  ? -24.146 -4.160  14.396  1.00 16.65 ? 47  GLU B C   1 
ATOM   2500 O  O   . GLU B 1 47  ? -23.826 -2.970  14.660  1.00 17.41 ? 47  GLU B O   1 
ATOM   2501 C  CB  . GLU B 1 47  ? -25.505 -5.218  16.260  1.00 23.48 ? 47  GLU B CB  1 
ATOM   2502 C  CG  . GLU B 1 47  ? -25.617 -6.289  17.363  1.00 26.27 ? 47  GLU B CG  1 
ATOM   2503 C  CD  . GLU B 1 47  ? -26.904 -6.151  18.171  1.00 31.23 ? 47  GLU B CD  1 
ATOM   2504 O  OE1 . GLU B 1 47  ? -27.063 -5.188  18.971  1.00 40.35 ? 47  GLU B OE1 1 
ATOM   2505 O  OE2 . GLU B 1 47  ? -27.781 -7.001  18.021  1.00 38.97 ? 47  GLU B OE2 1 
ATOM   2506 N  N   . PHE B 1 48  ? -24.451 -4.620  13.207  1.00 18.63 ? 48  PHE B N   1 
ATOM   2507 C  CA  . PHE B 1 48  ? -24.360 -3.762  11.981  1.00 16.89 ? 48  PHE B CA  1 
ATOM   2508 C  C   . PHE B 1 48  ? -25.758 -3.414  11.552  1.00 17.66 ? 48  PHE B C   1 
ATOM   2509 O  O   . PHE B 1 48  ? -26.495 -4.303  11.103  1.00 20.32 ? 48  PHE B O   1 
ATOM   2510 C  CB  . PHE B 1 48  ? -23.571 -4.487  10.904  1.00 16.63 ? 48  PHE B CB  1 
ATOM   2511 C  CG  . PHE B 1 48  ? -22.253 -5.029  11.411  1.00 17.24 ? 48  PHE B CG  1 
ATOM   2512 C  CD1 . PHE B 1 48  ? -21.165 -4.229  11.623  1.00 15.33 ? 48  PHE B CD1 1 
ATOM   2513 C  CD2 . PHE B 1 48  ? -22.132 -6.385  11.725  1.00 17.81 ? 48  PHE B CD2 1 
ATOM   2514 C  CE1 . PHE B 1 48  ? -19.955 -4.771  12.162  1.00 15.13 ? 48  PHE B CE1 1 
ATOM   2515 C  CE2 . PHE B 1 48  ? -20.947 -6.944  12.217  1.00 19.01 ? 48  PHE B CE2 1 
ATOM   2516 C  CZ  . PHE B 1 48  ? -19.855 -6.134  12.435  1.00 19.05 ? 48  PHE B CZ  1 
ATOM   2517 N  N   A GLN B 1 49  ? -26.144 -2.139  11.694  0.50 16.25 ? 49  GLN B N   1 
ATOM   2518 N  N   B GLN B 1 49  ? -26.152 -2.150  11.717  0.50 16.30 ? 49  GLN B N   1 
ATOM   2519 C  CA  A GLN B 1 49  ? -27.552 -1.770  11.524  0.50 16.50 ? 49  GLN B CA  1 
ATOM   2520 C  CA  B GLN B 1 49  ? -27.543 -1.816  11.465  0.50 16.49 ? 49  GLN B CA  1 
ATOM   2521 C  C   A GLN B 1 49  ? -27.720 -0.845  10.310  0.50 15.03 ? 49  GLN B C   1 
ATOM   2522 C  C   B GLN B 1 49  ? -27.621 -0.971  10.206  0.50 14.77 ? 49  GLN B C   1 
ATOM   2523 O  O   A GLN B 1 49  ? -27.012 0.161   10.183  0.50 15.78 ? 49  GLN B O   1 
ATOM   2524 O  O   B GLN B 1 49  ? -26.759 -0.177  9.928   0.50 14.73 ? 49  GLN B O   1 
ATOM   2525 C  CB  A GLN B 1 49  ? -28.088 -1.133  12.795  0.50 16.86 ? 49  GLN B CB  1 
ATOM   2526 C  CB  B GLN B 1 49  ? -28.155 -1.096  12.642  0.50 16.75 ? 49  GLN B CB  1 
ATOM   2527 C  CG  A GLN B 1 49  ? -27.872 -2.035  14.006  0.50 18.77 ? 49  GLN B CG  1 
ATOM   2528 C  CG  B GLN B 1 49  ? -28.353 -2.009  13.830  0.50 19.42 ? 49  GLN B CG  1 
ATOM   2529 C  CD  A GLN B 1 49  ? -28.759 -3.269  13.970  0.50 20.44 ? 49  GLN B CD  1 
ATOM   2530 C  CD  B GLN B 1 49  ? -28.369 -1.222  15.103  0.50 21.51 ? 49  GLN B CD  1 
ATOM   2531 O  OE1 A GLN B 1 49  ? -28.325 -4.393  14.277  0.50 21.35 ? 49  GLN B OE1 1 
ATOM   2532 O  OE1 B GLN B 1 49  ? -27.792 -0.158  15.160  0.50 22.65 ? 49  GLN B OE1 1 
ATOM   2533 N  NE2 A GLN B 1 49  ? -30.027 -3.067  13.581  0.50 18.12 ? 49  GLN B NE2 1 
ATOM   2534 N  NE2 B GLN B 1 49  ? -29.041 -1.731  16.129  0.50 21.55 ? 49  GLN B NE2 1 
ATOM   2535 N  N   . GLY B 1 50  ? -28.658 -1.206  9.430   1.00 16.14 ? 50  GLY B N   1 
ATOM   2536 C  CA  . GLY B 1 50  ? -28.915 -0.472  8.200   1.00 15.05 ? 50  GLY B CA  1 
ATOM   2537 C  C   . GLY B 1 50  ? -27.768 -0.575  7.233   1.00 12.80 ? 50  GLY B C   1 
ATOM   2538 O  O   . GLY B 1 50  ? -27.614 0.343   6.376   1.00 13.32 ? 50  GLY B O   1 
ATOM   2539 N  N   . TYR B 1 51  ? -27.036 -1.693  7.333   1.00 13.20 ? 51  TYR B N   1 
ATOM   2540 C  CA  . TYR B 1 51  ? -26.000 -1.993  6.328   1.00 11.50 ? 51  TYR B CA  1 
ATOM   2541 C  C   . TYR B 1 51  ? -26.629 -2.441  5.002   1.00 11.25 ? 51  TYR B C   1 
ATOM   2542 O  O   . TYR B 1 51  ? -26.032 -2.400  3.944   1.00 10.85 ? 51  TYR B O   1 
ATOM   2543 C  CB  . TYR B 1 51  ? -25.055 -3.120  6.776   1.00 11.47 ? 51  TYR B CB  1 
ATOM   2544 C  CG  . TYR B 1 51  ? -23.854 -2.562  7.526   1.00 11.12 ? 51  TYR B CG  1 
ATOM   2545 C  CD1 . TYR B 1 51  ? -22.573 -3.003  7.243   1.00 11.57 ? 51  TYR B CD1 1 
ATOM   2546 C  CD2 . TYR B 1 51  ? -24.000 -1.570  8.495   1.00 10.88 ? 51  TYR B CD2 1 
ATOM   2547 C  CE1 . TYR B 1 51  ? -21.474 -2.496  7.910   1.00 11.30 ? 51  TYR B CE1 1 
ATOM   2548 C  CE2 . TYR B 1 51  ? -22.900 -1.057  9.168   1.00 11.33 ? 51  TYR B CE2 1 
ATOM   2549 C  CZ  . TYR B 1 51  ? -21.638 -1.528  8.867   1.00 11.99 ? 51  TYR B CZ  1 
ATOM   2550 O  OH  . TYR B 1 51  ? -20.523 -1.045  9.512   1.00 13.74 ? 51  TYR B OH  1 
ATOM   2551 N  N   . ASN B 1 52  ? -27.892 -2.952  5.070   1.00 12.51 ? 52  ASN B N   1 
ATOM   2552 C  CA  . ASN B 1 52  ? -28.511 -3.428  3.836   1.00 13.47 ? 52  ASN B CA  1 
ATOM   2553 C  C   . ASN B 1 52  ? -29.115 -2.322  3.010   1.00 14.17 ? 52  ASN B C   1 
ATOM   2554 O  O   . ASN B 1 52  ? -30.271 -1.974  3.166   1.00 15.32 ? 52  ASN B O   1 
ATOM   2555 C  CB  . ASN B 1 52  ? -29.557 -4.508  4.175   1.00 16.02 ? 52  ASN B CB  1 
ATOM   2556 C  CG  . ASN B 1 52  ? -30.157 -5.132  2.987   1.00 19.89 ? 52  ASN B CG  1 
ATOM   2557 O  OD1 . ASN B 1 52  ? -29.774 -4.906  1.839   1.00 23.43 ? 52  ASN B OD1 1 
ATOM   2558 N  ND2 . ASN B 1 52  ? -31.183 -5.969  3.259   1.00 21.43 ? 52  ASN B ND2 1 
ATOM   2559 N  N   . LEU B 1 53  ? -28.269 -1.655  2.260   1.00 11.95 ? 53  LEU B N   1 
ATOM   2560 C  CA  . LEU B 1 53  ? -28.729 -0.413  1.550   1.00 13.60 ? 53  LEU B CA  1 
ATOM   2561 C  C   . LEU B 1 53  ? -29.712 -0.864  0.371   1.00 12.80 ? 53  LEU B C   1 
ATOM   2562 O  O   . LEU B 1 53  ? -29.490 -1.833  -0.349  1.00 12.46 ? 53  LEU B O   1 
ATOM   2563 C  CB  . LEU B 1 53  ? -27.544 0.242   0.896   1.00 13.95 ? 53  LEU B CB  1 
ATOM   2564 C  CG  . LEU B 1 53  ? -26.440 0.564   1.882   1.00 15.03 ? 53  LEU B CG  1 
ATOM   2565 C  CD1 . LEU B 1 53  ? -25.335 1.231   1.038   1.00 15.52 ? 53  LEU B CD1 1 
ATOM   2566 C  CD2 . LEU B 1 53  ? -26.875 1.461   3.038   1.00 16.65 ? 53  LEU B CD2 1 
ATOM   2567 N  N   . SER B 1 54  ? -30.763 -0.093  0.160   1.00 12.40 ? 54  SER B N   1 
ATOM   2568 C  CA  . SER B 1 54  ? -31.710 -0.457  -0.848  1.00 14.26 ? 54  SER B CA  1 
ATOM   2569 C  C   . SER B 1 54  ? -31.133 -0.376  -2.252  1.00 15.67 ? 54  SER B C   1 
ATOM   2570 O  O   . SER B 1 54  ? -30.518 0.597   -2.586  1.00 14.62 ? 54  SER B O   1 
ATOM   2571 C  CB  . SER B 1 54  ? -32.858 0.521   -0.798  1.00 15.18 ? 54  SER B CB  1 
ATOM   2572 O  OG  . SER B 1 54  ? -33.669 0.176   -1.880  1.00 15.82 ? 54  SER B OG  1 
ATOM   2573 N  N   . ALA B 1 55  ? -31.336 -1.449  -3.010  1.00 13.72 ? 55  ALA B N   1 
ATOM   2574 C  CA  . ALA B 1 55  ? -30.942 -1.558  -4.438  1.00 15.31 ? 55  ALA B CA  1 
ATOM   2575 C  C   . ALA B 1 55  ? -31.592 -0.541  -5.330  1.00 15.89 ? 55  ALA B C   1 
ATOM   2576 O  O   . ALA B 1 55  ? -31.119 -0.296  -6.478  1.00 17.19 ? 55  ALA B O   1 
ATOM   2577 C  CB  . ALA B 1 55  ? -31.113 -3.009  -4.970  1.00 18.99 ? 55  ALA B CB  1 
ATOM   2578 N  N   . ASN B 1 56  ? -32.654 0.077   -4.845  1.00 16.78 ? 56  ASN B N   1 
ATOM   2579 C  CA  . ASN B 1 56  ? -33.323 1.076   -5.671  1.00 17.35 ? 56  ASN B CA  1 
ATOM   2580 C  C   . ASN B 1 56  ? -32.799 2.465   -5.393  1.00 16.06 ? 56  ASN B C   1 
ATOM   2581 O  O   . ASN B 1 56  ? -33.168 3.438   -6.074  1.00 19.05 ? 56  ASN B O   1 
ATOM   2582 C  CB  . ASN B 1 56  ? -34.842 1.032   -5.479  1.00 18.12 ? 56  ASN B CB  1 
ATOM   2583 C  CG  . ASN B 1 56  ? -35.427 -0.329  -5.869  1.00 19.98 ? 56  ASN B CG  1 
ATOM   2584 O  OD1 . ASN B 1 56  ? -34.882 -1.105  -6.684  1.00 19.67 ? 56  ASN B OD1 1 
ATOM   2585 N  ND2 . ASN B 1 56  ? -36.612 -0.591  -5.328  1.00 23.99 ? 56  ASN B ND2 1 
ATOM   2586 N  N   . LYS B 1 57  ? -31.936 2.550   -4.396  1.00 16.22 ? 57  LYS B N   1 
ATOM   2587 C  CA  . LYS B 1 57  ? -31.256 3.833   -4.054  1.00 11.63 ? 57  LYS B CA  1 
ATOM   2588 C  C   . LYS B 1 57  ? -29.857 3.801   -4.652  1.00 12.32 ? 57  LYS B C   1 
ATOM   2589 O  O   . LYS B 1 57  ? -29.374 2.697   -5.046  1.00 13.83 ? 57  LYS B O   1 
ATOM   2590 C  CB  . LYS B 1 57  ? -31.165 3.989   -2.526  1.00 14.23 ? 57  LYS B CB  1 
ATOM   2591 C  CG  . LYS B 1 57  ? -32.457 4.577   -1.959  1.00 20.48 ? 57  LYS B CG  1 
ATOM   2592 C  CD  . LYS B 1 57  ? -32.400 4.570   -0.445  1.00 21.99 ? 57  LYS B CD  1 
ATOM   2593 C  CE  . LYS B 1 57  ? -32.861 5.891   0.146   1.00 29.27 ? 57  LYS B CE  1 
ATOM   2594 N  NZ  . LYS B 1 57  ? -33.337 5.540   1.522   1.00 27.96 ? 57  LYS B NZ  1 
ATOM   2595 N  N   . GLN B 1 58  ? -29.230 4.966   -4.783  1.00 13.33 ? 58  GLN B N   1 
ATOM   2596 C  CA  . GLN B 1 58  ? -27.801 4.879   -5.253  1.00 14.77 ? 58  GLN B CA  1 
ATOM   2597 C  C   . GLN B 1 58  ? -26.902 5.775   -4.459  1.00 14.57 ? 58  GLN B C   1 
ATOM   2598 O  O   . GLN B 1 58  ? -27.327 6.761   -3.811  1.00 15.26 ? 58  GLN B O   1 
ATOM   2599 C  CB  . GLN B 1 58  ? -27.652 5.137   -6.738  1.00 20.01 ? 58  GLN B CB  1 
ATOM   2600 C  CG  . GLN B 1 58  ? -28.246 6.471   -7.140  1.00 19.28 ? 58  GLN B CG  1 
ATOM   2601 C  CD  . GLN B 1 58  ? -28.523 6.611   -8.661  1.00 26.41 ? 58  GLN B CD  1 
ATOM   2602 O  OE1 . GLN B 1 58  ? -28.392 5.659   -9.498  1.00 23.12 ? 58  GLN B OE1 1 
ATOM   2603 N  NE2 . GLN B 1 58  ? -28.885 7.860   -9.032  1.00 28.57 ? 58  GLN B NE2 1 
ATOM   2604 N  N   . PHE B 1 59  ? -25.618 5.376   -4.435  1.00 12.28 ? 59  PHE B N   1 
ATOM   2605 C  CA  . PHE B 1 59  ? -24.623 6.021   -3.507  1.00 12.49 ? 59  PHE B CA  1 
ATOM   2606 C  C   . PHE B 1 59  ? -23.410 6.500   -4.257  1.00 11.13 ? 59  PHE B C   1 
ATOM   2607 O  O   . PHE B 1 59  ? -23.021 5.893   -5.245  1.00 12.83 ? 59  PHE B O   1 
ATOM   2608 C  CB  . PHE B 1 59  ? -24.239 4.954   -2.409  1.00 11.96 ? 59  PHE B CB  1 
ATOM   2609 C  CG  . PHE B 1 59  ? -25.511 4.539   -1.639  1.00 12.17 ? 59  PHE B CG  1 
ATOM   2610 C  CD1 . PHE B 1 59  ? -26.365 3.535   -2.149  1.00 12.21 ? 59  PHE B CD1 1 
ATOM   2611 C  CD2 . PHE B 1 59  ? -25.839 5.211   -0.476  1.00 12.58 ? 59  PHE B CD2 1 
ATOM   2612 C  CE1 . PHE B 1 59  ? -27.598 3.283   -1.446  1.00 11.08 ? 59  PHE B CE1 1 
ATOM   2613 C  CE2 . PHE B 1 59  ? -27.082 4.980   0.222   1.00 12.46 ? 59  PHE B CE2 1 
ATOM   2614 C  CZ  . PHE B 1 59  ? -27.910 3.976   -0.276  1.00 14.10 ? 59  PHE B CZ  1 
ATOM   2615 N  N   . LEU B 1 60  ? -22.955 7.681   -3.873  1.00 12.19 ? 60  LEU B N   1 
ATOM   2616 C  CA  . LEU B 1 60  ? -21.890 8.333   -4.619  1.00 12.88 ? 60  LEU B CA  1 
ATOM   2617 C  C   . LEU B 1 60  ? -20.512 7.748   -4.409  1.00 11.95 ? 60  LEU B C   1 
ATOM   2618 O  O   . LEU B 1 60  ? -20.048 7.664   -3.306  1.00 11.75 ? 60  LEU B O   1 
ATOM   2619 C  CB  . LEU B 1 60  ? -21.859 9.825   -4.253  1.00 15.27 ? 60  LEU B CB  1 
ATOM   2620 C  CG  . LEU B 1 60  ? -21.092 10.848  -5.135  1.00 18.23 ? 60  LEU B CG  1 
ATOM   2621 C  CD1 . LEU B 1 60  ? -21.756 10.999  -6.514  1.00 17.54 ? 60  LEU B CD1 1 
ATOM   2622 C  CD2 . LEU B 1 60  ? -20.885 12.165  -4.356  1.00 21.39 ? 60  LEU B CD2 1 
ATOM   2623 N  N   . LEU B 1 61  ? -19.884 7.418   -5.531  1.00 11.64 ? 61  LEU B N   1 
ATOM   2624 C  CA  . LEU B 1 61  ? -18.509 6.843   -5.583  1.00 12.11 ? 61  LEU B CA  1 
ATOM   2625 C  C   . LEU B 1 61  ? -17.655 8.033   -6.104  1.00 13.08 ? 61  LEU B C   1 
ATOM   2626 O  O   . LEU B 1 61  ? -18.000 8.638   -7.121  1.00 14.50 ? 61  LEU B O   1 
ATOM   2627 C  CB  . LEU B 1 61  ? -18.464 5.620   -6.492  1.00 12.51 ? 61  LEU B CB  1 
ATOM   2628 C  CG  . LEU B 1 61  ? -17.158 4.829   -6.498  1.00 13.22 ? 61  LEU B CG  1 
ATOM   2629 C  CD1 . LEU B 1 61  ? -16.894 4.072   -5.171  1.00 14.08 ? 61  LEU B CD1 1 
ATOM   2630 C  CD2 . LEU B 1 61  ? -17.175 3.806   -7.655  1.00 13.96 ? 61  LEU B CD2 1 
ATOM   2631 N  N   . THR B 1 62  ? -16.535 8.356   -5.429  1.00 12.54 ? 62  THR B N   1 
ATOM   2632 C  CA  . THR B 1 62  ? -15.705 9.508   -5.843  1.00 14.37 ? 62  THR B CA  1 
ATOM   2633 C  C   . THR B 1 62  ? -14.225 9.121   -5.810  1.00 13.42 ? 62  THR B C   1 
ATOM   2634 O  O   . THR B 1 62  ? -13.741 8.610   -4.831  1.00 13.28 ? 62  THR B O   1 
ATOM   2635 C  CB  . THR B 1 62  ? -15.825 10.691  -4.889  1.00 19.17 ? 62  THR B CB  1 
ATOM   2636 O  OG1 . THR B 1 62  ? -17.174 11.079  -4.702  1.00 20.75 ? 62  THR B OG1 1 
ATOM   2637 C  CG2 . THR B 1 62  ? -15.049 11.965  -5.425  1.00 20.40 ? 62  THR B CG2 1 
ATOM   2638 N  N   . ASN B 1 63  ? -13.485 9.544   -6.828  1.00 13.15 ? 63  ASN B N   1 
ATOM   2639 C  CA  . ASN B 1 63  ? -12.018 9.538   -6.820  1.00 11.90 ? 63  ASN B CA  1 
ATOM   2640 C  C   . ASN B 1 63  ? -11.571 10.935  -6.395  1.00 13.45 ? 63  ASN B C   1 
ATOM   2641 O  O   . ASN B 1 63  ? -11.813 11.905  -7.075  1.00 13.74 ? 63  ASN B O   1 
ATOM   2642 C  CB  . ASN B 1 63  ? -11.550 9.209   -8.238  1.00 13.22 ? 63  ASN B CB  1 
ATOM   2643 C  CG  . ASN B 1 63  ? -10.057 9.136   -8.343  1.00 12.46 ? 63  ASN B CG  1 
ATOM   2644 O  OD1 . ASN B 1 63  ? -9.367  9.766   -7.546  1.00 12.79 ? 63  ASN B OD1 1 
ATOM   2645 N  ND2 . ASN B 1 63  ? -9.560  8.470   -9.367  1.00 11.72 ? 63  ASN B ND2 1 
ATOM   2646 N  N   . ASN B 1 64  ? -10.893 11.023  -5.231  1.00 14.63 ? 64  ASN B N   1 
ATOM   2647 C  CA  . ASN B 1 64  ? -10.438 12.356  -4.798  1.00 15.65 ? 64  ASN B CA  1 
ATOM   2648 C  C   . ASN B 1 64  ? -8.958  12.567  -5.063  1.00 15.90 ? 64  ASN B C   1 
ATOM   2649 O  O   . ASN B 1 64  ? -8.391  13.517  -4.529  1.00 16.82 ? 64  ASN B O   1 
ATOM   2650 C  CB  . ASN B 1 64  ? -10.719 12.653  -3.298  1.00 18.33 ? 64  ASN B CB  1 
ATOM   2651 C  CG  . ASN B 1 64  ? -10.011 11.682  -2.357  1.00 18.76 ? 64  ASN B CG  1 
ATOM   2652 O  OD1 . ASN B 1 64  ? -8.976  11.065  -2.672  1.00 17.00 ? 64  ASN B OD1 1 
ATOM   2653 N  ND2 . ASN B 1 64  ? -10.556 11.574  -1.108  1.00 23.69 ? 64  ASN B ND2 1 
ATOM   2654 N  N   . GLY B 1 65  ? -8.356  11.627  -5.812  1.00 13.19 ? 65  GLY B N   1 
ATOM   2655 C  CA  . GLY B 1 65  ? -6.907  11.764  -6.097  1.00 14.42 ? 65  GLY B CA  1 
ATOM   2656 C  C   . GLY B 1 65  ? -6.049  10.963  -5.171  1.00 17.08 ? 65  GLY B C   1 
ATOM   2657 O  O   . GLY B 1 65  ? -4.880  10.668  -5.506  1.00 15.10 ? 65  GLY B O   1 
ATOM   2658 N  N   . HIS B 1 66  ? -6.554  10.606  -3.989  1.00 15.95 ? 66  HIS B N   1 
ATOM   2659 C  CA  . HIS B 1 66  ? -5.731  9.892   -2.996  1.00 16.32 ? 66  HIS B CA  1 
ATOM   2660 C  C   . HIS B 1 66  ? -6.356  8.546   -2.713  1.00 15.86 ? 66  HIS B C   1 
ATOM   2661 O  O   . HIS B 1 66  ? -5.689  7.569   -2.356  1.00 18.56 ? 66  HIS B O   1 
ATOM   2662 C  CB  . HIS B 1 66  ? -5.636  10.680  -1.652  1.00 13.45 ? 66  HIS B CB  1 
ATOM   2663 C  CG  . HIS B 1 66  ? -4.909  12.027  -1.739  1.00 14.82 ? 66  HIS B CG  1 
ATOM   2664 N  ND1 . HIS B 1 66  ? -3.555  12.089  -1.895  1.00 14.73 ? 66  HIS B ND1 1 
ATOM   2665 C  CD2 . HIS B 1 66  ? -5.340  13.339  -1.649  1.00 14.50 ? 66  HIS B CD2 1 
ATOM   2666 C  CE1 . HIS B 1 66  ? -3.179  13.399  -1.911  1.00 14.70 ? 66  HIS B CE1 1 
ATOM   2667 N  NE2 . HIS B 1 66  ? -4.264  14.140  -1.811  1.00 17.57 ? 66  HIS B NE2 1 
ATOM   2668 N  N   . SER B 1 67  ? -7.692  8.512   -2.918  1.00 16.19 ? 67  SER B N   1 
ATOM   2669 C  CA  . SER B 1 67  ? -8.490  7.352   -2.629  1.00 17.46 ? 67  SER B CA  1 
ATOM   2670 C  C   . SER B 1 67  ? -9.712  7.301   -3.577  1.00 17.05 ? 67  SER B C   1 
ATOM   2671 O  O   . SER B 1 67  ? -10.060 8.329   -4.164  1.00 19.06 ? 67  SER B O   1 
ATOM   2672 C  CB  . SER B 1 67  ? -8.991  7.522   -1.198  1.00 16.86 ? 67  SER B CB  1 
ATOM   2673 O  OG  . SER B 1 67  ? -9.549  6.306   -0.654  1.00 18.28 ? 67  SER B OG  1 
ATOM   2674 N  N   . VAL B 1 68  ? -10.352 6.125   -3.657  1.00 16.59 ? 68  VAL B N   1 
ATOM   2675 C  CA  . VAL B 1 68  ? -11.750 6.018   -4.199  1.00 14.88 ? 68  VAL B CA  1 
ATOM   2676 C  C   . VAL B 1 68  ? -12.682 5.695   -3.020  1.00 12.70 ? 68  VAL B C   1 
ATOM   2677 O  O   . VAL B 1 68  ? -12.460 4.742   -2.355  1.00 13.39 ? 68  VAL B O   1 
ATOM   2678 C  CB  . VAL B 1 68  ? -11.897 5.004   -5.311  1.00 15.40 ? 68  VAL B CB  1 
ATOM   2679 C  CG1 . VAL B 1 68  ? -11.579 3.535   -4.938  1.00 19.82 ? 68  VAL B CG1 1 
ATOM   2680 C  CG2 . VAL B 1 68  ? -13.314 5.048   -5.900  1.00 16.28 ? 68  VAL B CG2 1 
ATOM   2681 N  N   . LYS B 1 69  ? -13.680 6.530   -2.781  1.00 12.85 ? 69  LYS B N   1 
ATOM   2682 C  CA  . LYS B 1 69  ? -14.553 6.290   -1.572  1.00 11.11 ? 69  LYS B CA  1 
ATOM   2683 C  C   . LYS B 1 69  ? -16.001 6.175   -2.060  1.00 11.37 ? 69  LYS B C   1 
ATOM   2684 O  O   . LYS B 1 69  ? -16.421 6.763   -3.101  1.00 11.29 ? 69  LYS B O   1 
ATOM   2685 C  CB  . LYS B 1 69  ? -14.325 7.370   -0.535  1.00 16.21 ? 69  LYS B CB  1 
ATOM   2686 C  CG  . LYS B 1 69  ? -14.839 8.746   -1.003  1.00 16.99 ? 69  LYS B CG  1 
ATOM   2687 C  CD  . LYS B 1 69  ? -14.716 9.754   0.118   1.00 20.86 ? 69  LYS B CD  1 
ATOM   2688 C  CE  . LYS B 1 69  ? -14.701 11.128  -0.542  1.00 23.59 ? 69  LYS B CE  1 
ATOM   2689 N  NZ  . LYS B 1 69  ? -15.083 12.205  0.451   1.00 30.61 ? 69  LYS B NZ  1 
ATOM   2690 N  N   . LEU B 1 70  ? -16.739 5.312   -1.362  1.00 8.69  ? 70  LEU B N   1 
ATOM   2691 C  CA  . LEU B 1 70  ? -18.216 5.234   -1.555  1.00 8.52  ? 70  LEU B CA  1 
ATOM   2692 C  C   . LEU B 1 70  ? -18.843 5.896   -0.369  1.00 8.58  ? 70  LEU B C   1 
ATOM   2693 O  O   . LEU B 1 70  ? -18.589 5.527   0.799   1.00 8.83  ? 70  LEU B O   1 
ATOM   2694 C  CB  . LEU B 1 70  ? -18.565 3.725   -1.630  1.00 9.34  ? 70  LEU B CB  1 
ATOM   2695 C  CG  . LEU B 1 70  ? -20.092 3.604   -1.811  1.00 9.04  ? 70  LEU B CG  1 
ATOM   2696 C  CD1 . LEU B 1 70  ? -20.573 4.028   -3.217  1.00 11.37 ? 70  LEU B CD1 1 
ATOM   2697 C  CD2 . LEU B 1 70  ? -20.405 2.128   -1.687  1.00 10.57 ? 70  LEU B CD2 1 
ATOM   2698 N  N   . ASN B 1 71  ? -19.728 6.934   -0.623  1.00 9.78  ? 71  ASN B N   1 
ATOM   2699 C  CA  . ASN B 1 71  ? -20.431 7.616   0.518   1.00 11.68 ? 71  ASN B CA  1 
ATOM   2700 C  C   . ASN B 1 71  ? -21.523 6.674   1.085   1.00 11.43 ? 71  ASN B C   1 
ATOM   2701 O  O   . ASN B 1 71  ? -22.136 5.949   0.303   1.00 12.06 ? 71  ASN B O   1 
ATOM   2702 C  CB  . ASN B 1 71  ? -21.061 8.901   -0.040  1.00 15.49 ? 71  ASN B CB  1 
ATOM   2703 C  CG  . ASN B 1 71  ? -20.053 10.059  -0.211  1.00 20.23 ? 71  ASN B CG  1 
ATOM   2704 O  OD1 . ASN B 1 71  ? -18.860 9.942   0.059   1.00 22.06 ? 71  ASN B OD1 1 
ATOM   2705 N  ND2 . ASN B 1 71  ? -20.590 11.239  -0.646  1.00 24.79 ? 71  ASN B ND2 1 
ATOM   2706 N  N   . LEU B 1 72  ? -21.695 6.723   2.411   1.00 11.36 ? 72  LEU B N   1 
ATOM   2707 C  CA  . LEU B 1 72  ? -22.675 5.864   3.022   1.00 11.71 ? 72  LEU B CA  1 
ATOM   2708 C  C   . LEU B 1 72  ? -23.602 6.758   3.820   1.00 12.61 ? 72  LEU B C   1 
ATOM   2709 O  O   . LEU B 1 72  ? -23.207 7.862   4.268   1.00 12.61 ? 72  LEU B O   1 
ATOM   2710 C  CB  . LEU B 1 72  ? -21.912 4.874   3.936   1.00 11.59 ? 72  LEU B CB  1 
ATOM   2711 C  CG  . LEU B 1 72  ? -20.949 3.910   3.248   1.00 11.84 ? 72  LEU B CG  1 
ATOM   2712 C  CD1 . LEU B 1 72  ? -20.124 3.192   4.301   1.00 11.40 ? 72  LEU B CD1 1 
ATOM   2713 C  CD2 . LEU B 1 72  ? -21.725 2.910   2.408   1.00 11.17 ? 72  LEU B CD2 1 
ATOM   2714 N  N   . PRO B 1 73  ? -24.866 6.292   3.982   1.00 12.40 ? 73  PRO B N   1 
ATOM   2715 C  CA  . PRO B 1 73  ? -25.883 7.102   4.652   1.00 14.00 ? 73  PRO B CA  1 
ATOM   2716 C  C   . PRO B 1 73  ? -25.777 7.028   6.190   1.00 15.21 ? 73  PRO B C   1 
ATOM   2717 O  O   . PRO B 1 73  ? -25.318 6.015   6.729   1.00 16.88 ? 73  PRO B O   1 
ATOM   2718 C  CB  . PRO B 1 73  ? -27.140 6.446   4.194   1.00 14.27 ? 73  PRO B CB  1 
ATOM   2719 C  CG  . PRO B 1 73  ? -26.776 5.001   4.127   1.00 13.85 ? 73  PRO B CG  1 
ATOM   2720 C  CD  . PRO B 1 73  ? -25.418 5.026   3.474   1.00 13.40 ? 73  PRO B CD  1 
ATOM   2721 N  N   . SER B 1 74  ? -26.147 8.100   6.853   1.00 18.98 ? 74  SER B N   1 
ATOM   2722 C  CA  . SER B 1 74  ? -25.996 8.169   8.308   1.00 18.34 ? 74  SER B CA  1 
ATOM   2723 C  C   . SER B 1 74  ? -26.978 7.282   9.064   1.00 18.68 ? 74  SER B C   1 
ATOM   2724 O  O   . SER B 1 74  ? -26.777 7.061   10.266  1.00 21.55 ? 74  SER B O   1 
ATOM   2725 C  CB  . SER B 1 74  ? -26.101 9.606   8.782   1.00 19.18 ? 74  SER B CB  1 
ATOM   2726 O  OG  . SER B 1 74  ? -27.391 10.096  8.481   1.00 21.32 ? 74  SER B OG  1 
ATOM   2727 N  N   . ASP B 1 75  ? -27.969 6.720   8.399   1.00 17.96 ? 75  ASP B N   1 
ATOM   2728 C  CA  . ASP B 1 75  ? -28.853 5.733   9.043   1.00 20.08 ? 75  ASP B CA  1 
ATOM   2729 C  C   . ASP B 1 75  ? -28.185 4.324   9.128   1.00 17.81 ? 75  ASP B C   1 
ATOM   2730 O  O   . ASP B 1 75  ? -28.734 3.401   9.753   1.00 22.79 ? 75  ASP B O   1 
ATOM   2731 C  CB  . ASP B 1 75  ? -30.285 5.610   8.485   1.00 23.62 ? 75  ASP B CB  1 
ATOM   2732 C  CG  . ASP B 1 75  ? -30.391 5.474   6.962   1.00 28.84 ? 75  ASP B CG  1 
ATOM   2733 O  OD1 . ASP B 1 75  ? -29.420 5.124   6.264   1.00 26.57 ? 75  ASP B OD1 1 
ATOM   2734 O  OD2 . ASP B 1 75  ? -31.523 5.699   6.467   1.00 39.33 ? 75  ASP B OD2 1 
ATOM   2735 N  N   . MET B 1 76  ? -26.997 4.207   8.534   1.00 15.50 ? 76  MET B N   1 
ATOM   2736 C  CA  . MET B 1 76  ? -26.217 3.003   8.619   1.00 13.82 ? 76  MET B CA  1 
ATOM   2737 C  C   . MET B 1 76  ? -25.329 3.166   9.853   1.00 13.85 ? 76  MET B C   1 
ATOM   2738 O  O   . MET B 1 76  ? -24.590 4.166   10.008  1.00 13.76 ? 76  MET B O   1 
ATOM   2739 C  CB  . MET B 1 76  ? -25.408 2.906   7.321   1.00 13.09 ? 76  MET B CB  1 
ATOM   2740 C  CG  . MET B 1 76  ? -24.451 1.739   7.365   1.00 14.70 ? 76  MET B CG  1 
ATOM   2741 S  SD  . MET B 1 76  ? -23.702 1.561   5.686   1.00 15.12 ? 76  MET B SD  1 
ATOM   2742 C  CE  . MET B 1 76  ? -22.253 0.581   6.095   1.00 13.66 ? 76  MET B CE  1 
ATOM   2743 N  N   . HIS B 1 77  ? -25.365 2.181   10.767  1.00 14.67 ? 77  HIS B N   1 
ATOM   2744 C  CA  . HIS B 1 77  ? -24.578 2.303   11.981  1.00 15.39 ? 77  HIS B CA  1 
ATOM   2745 C  C   . HIS B 1 77  ? -24.075 1.056   12.579  1.00 13.87 ? 77  HIS B C   1 
ATOM   2746 O  O   . HIS B 1 77  ? -24.504 -0.058  12.241  1.00 15.92 ? 77  HIS B O   1 
ATOM   2747 C  CB  . HIS B 1 77  ? -25.217 3.192   13.058  1.00 20.34 ? 77  HIS B CB  1 
ATOM   2748 C  CG  . HIS B 1 77  ? -26.519 2.720   13.512  1.00 24.81 ? 77  HIS B CG  1 
ATOM   2749 N  ND1 . HIS B 1 77  ? -27.668 2.981   12.820  1.00 27.14 ? 77  HIS B ND1 1 
ATOM   2750 C  CD2 . HIS B 1 77  ? -26.898 2.025   14.665  1.00 31.72 ? 77  HIS B CD2 1 
ATOM   2751 C  CE1 . HIS B 1 77  ? -28.706 2.403   13.463  1.00 28.87 ? 77  HIS B CE1 1 
ATOM   2752 N  NE2 . HIS B 1 77  ? -28.244 1.847   14.597  1.00 28.55 ? 77  HIS B NE2 1 
ATOM   2753 N  N   . ILE B 1 78  ? -23.137 1.256   13.491  1.00 15.06 ? 78  ILE B N   1 
ATOM   2754 C  CA  . ILE B 1 78  ? -22.705 0.128   14.351  1.00 17.04 ? 78  ILE B CA  1 
ATOM   2755 C  C   . ILE B 1 78  ? -23.170 0.324   15.787  1.00 17.95 ? 78  ILE B C   1 
ATOM   2756 O  O   . ILE B 1 78  ? -23.057 1.431   16.348  1.00 19.78 ? 78  ILE B O   1 
ATOM   2757 C  CB  . ILE B 1 78  ? -21.173 -0.201  14.243  1.00 18.10 ? 78  ILE B CB  1 
ATOM   2758 C  CG1 . ILE B 1 78  ? -20.299 1.018   14.273  1.00 20.35 ? 78  ILE B CG1 1 
ATOM   2759 C  CG2 . ILE B 1 78  ? -20.844 -0.859  12.927  1.00 19.51 ? 78  ILE B CG2 1 
ATOM   2760 C  CD1 . ILE B 1 78  ? -18.797 0.655   14.193  1.00 19.67 ? 78  ILE B CD1 1 
ATOM   2761 N  N   . GLN B 1 79  ? -23.795 -0.733  16.305  1.00 20.39 ? 79  GLN B N   1 
ATOM   2762 C  CA  . GLN B 1 79  ? -24.258 -0.761  17.711  1.00 24.72 ? 79  GLN B CA  1 
ATOM   2763 C  C   . GLN B 1 79  ? -23.297 -1.706  18.448  1.00 24.75 ? 79  GLN B C   1 
ATOM   2764 O  O   . GLN B 1 79  ? -22.943 -2.767  17.905  1.00 23.87 ? 79  GLN B O   1 
ATOM   2765 C  CB  . GLN B 1 79  ? -25.669 -1.333  17.759  1.00 28.90 ? 79  GLN B CB  1 
ATOM   2766 C  CG  . GLN B 1 79  ? -26.323 -1.064  19.129  1.00 39.07 ? 79  GLN B CG  1 
ATOM   2767 C  CD  . GLN B 1 79  ? -27.666 -1.719  19.273  1.00 42.13 ? 79  GLN B CD  1 
ATOM   2768 O  OE1 . GLN B 1 79  ? -28.678 -1.190  18.818  1.00 48.17 ? 79  GLN B OE1 1 
ATOM   2769 N  NE2 . GLN B 1 79  ? -27.695 -2.863  19.944  1.00 46.13 ? 79  GLN B NE2 1 
ATOM   2770 N  N   . GLY B 1 80  ? -22.915 -1.342  19.659  1.00 25.09 ? 80  GLY B N   1 
ATOM   2771 C  CA  . GLY B 1 80  ? -22.063 -2.243  20.481  1.00 26.37 ? 80  GLY B CA  1 
ATOM   2772 C  C   . GLY B 1 80  ? -21.006 -1.435  21.154  1.00 25.20 ? 80  GLY B C   1 
ATOM   2773 O  O   . GLY B 1 80  ? -20.589 -1.756  22.299  1.00 23.34 ? 80  GLY B O   1 
ATOM   2774 N  N   . LEU B 1 81  ? -20.648 -0.321  20.495  1.00 24.53 ? 81  LEU B N   1 
ATOM   2775 C  CA  . LEU B 1 81  ? -19.702 0.649   21.063  1.00 25.26 ? 81  LEU B CA  1 
ATOM   2776 C  C   . LEU B 1 81  ? -20.392 1.484   22.139  1.00 26.39 ? 81  LEU B C   1 
ATOM   2777 O  O   . LEU B 1 81  ? -21.597 1.294   22.422  1.00 26.48 ? 81  LEU B O   1 
ATOM   2778 C  CB  . LEU B 1 81  ? -18.923 1.484   20.013  1.00 23.23 ? 81  LEU B CB  1 
ATOM   2779 C  CG  . LEU B 1 81  ? -18.177 0.662   18.975  1.00 25.34 ? 81  LEU B CG  1 
ATOM   2780 C  CD1 . LEU B 1 81  ? -17.752 1.479   17.758  1.00 23.38 ? 81  LEU B CD1 1 
ATOM   2781 C  CD2 . LEU B 1 81  ? -16.969 0.164   19.738  1.00 21.08 ? 81  LEU B CD2 1 
ATOM   2782 N  N   . GLN B 1 82  ? -19.634 2.370   22.774  1.00 29.03 ? 82  GLN B N   1 
ATOM   2783 C  CA  . GLN B 1 82  ? -20.190 3.066   23.929  1.00 30.99 ? 82  GLN B CA  1 
ATOM   2784 C  C   . GLN B 1 82  ? -21.023 4.285   23.504  1.00 31.97 ? 82  GLN B C   1 
ATOM   2785 O  O   . GLN B 1 82  ? -21.718 4.909   24.327  1.00 32.13 ? 82  GLN B O   1 
ATOM   2786 C  CB  . GLN B 1 82  ? -19.082 3.392   24.915  1.00 35.05 ? 82  GLN B CB  1 
ATOM   2787 C  CG  . GLN B 1 82  ? -18.678 2.223   25.812  1.00 32.95 ? 82  GLN B CG  1 
ATOM   2788 C  CD  . GLN B 1 82  ? -17.557 2.676   26.723  1.00 40.02 ? 82  GLN B CD  1 
ATOM   2789 O  OE1 . GLN B 1 82  ? -17.667 2.668   27.965  1.00 41.45 ? 82  GLN B OE1 1 
ATOM   2790 N  NE2 . GLN B 1 82  ? -16.487 3.166   26.103  1.00 35.77 ? 82  GLN B NE2 1 
ATOM   2791 N  N   . SER B 1 83  ? -20.930 4.633   22.220  1.00 25.46 ? 83  SER B N   1 
ATOM   2792 C  CA  . SER B 1 83  ? -21.935 5.482   21.547  1.00 23.70 ? 83  SER B CA  1 
ATOM   2793 C  C   . SER B 1 83  ? -22.298 4.821   20.234  1.00 21.46 ? 83  SER B C   1 
ATOM   2794 O  O   . SER B 1 83  ? -21.587 3.936   19.799  1.00 21.28 ? 83  SER B O   1 
ATOM   2795 C  CB  . SER B 1 83  ? -21.366 6.887   21.285  1.00 25.14 ? 83  SER B CB  1 
ATOM   2796 O  OG  . SER B 1 83  ? -21.007 7.476   22.529  1.00 24.13 ? 83  SER B OG  1 
ATOM   2797 N  N   A ARG B 1 84  ? -23.401 5.249   19.632  0.50 20.85 ? 84  ARG B N   1 
ATOM   2798 N  N   B ARG B 1 84  ? -23.398 5.248   19.611  0.50 20.21 ? 84  ARG B N   1 
ATOM   2799 C  CA  A ARG B 1 84  ? -23.691 4.860   18.267  0.50 20.06 ? 84  ARG B CA  1 
ATOM   2800 C  CA  B ARG B 1 84  ? -23.745 4.791   18.258  0.50 18.90 ? 84  ARG B CA  1 
ATOM   2801 C  C   A ARG B 1 84  ? -22.628 5.523   17.375  0.50 19.76 ? 84  ARG B C   1 
ATOM   2802 C  C   B ARG B 1 84  ? -22.828 5.522   17.250  0.50 18.21 ? 84  ARG B C   1 
ATOM   2803 O  O   A ARG B 1 84  ? -22.203 6.689   17.603  0.50 18.10 ? 84  ARG B O   1 
ATOM   2804 O  O   B ARG B 1 84  ? -22.656 6.747   17.303  0.50 15.35 ? 84  ARG B O   1 
ATOM   2805 C  CB  A ARG B 1 84  ? -25.088 5.325   17.855  0.50 20.46 ? 84  ARG B CB  1 
ATOM   2806 C  CB  B ARG B 1 84  ? -25.222 5.072   17.954  0.50 19.36 ? 84  ARG B CB  1 
ATOM   2807 C  CG  A ARG B 1 84  ? -25.265 5.386   16.347  0.50 22.34 ? 84  ARG B CG  1 
ATOM   2808 C  CG  B ARG B 1 84  ? -25.644 4.698   16.539  0.50 21.31 ? 84  ARG B CG  1 
ATOM   2809 C  CD  A ARG B 1 84  ? -26.590 6.013   15.990  0.50 23.57 ? 84  ARG B CD  1 
ATOM   2810 C  CD  B ARG B 1 84  ? -27.016 5.258   16.174  0.50 21.43 ? 84  ARG B CD  1 
ATOM   2811 N  NE  A ARG B 1 84  ? -27.648 5.122   16.390  0.50 22.69 ? 84  ARG B NE  1 
ATOM   2812 N  NE  B ARG B 1 84  ? -26.993 5.674   14.763  0.50 21.34 ? 84  ARG B NE  1 
ATOM   2813 C  CZ  A ARG B 1 84  ? -28.928 5.350   16.120  0.50 22.10 ? 84  ARG B CZ  1 
ATOM   2814 C  CZ  B ARG B 1 84  ? -28.055 5.772   13.985  0.50 22.53 ? 84  ARG B CZ  1 
ATOM   2815 N  NH1 A ARG B 1 84  ? -29.287 6.462   15.487  0.50 25.38 ? 84  ARG B NH1 1 
ATOM   2816 N  NH1 B ARG B 1 84  ? -29.251 5.491   14.482  0.50 23.76 ? 84  ARG B NH1 1 
ATOM   2817 N  NH2 A ARG B 1 84  ? -29.832 4.482   16.515  0.50 21.69 ? 84  ARG B NH2 1 
ATOM   2818 N  NH2 B ARG B 1 84  ? -27.912 6.124   12.716  0.50 22.28 ? 84  ARG B NH2 1 
ATOM   2819 N  N   . TYR B 1 85  ? -22.163 4.764   16.391  1.00 16.26 ? 85  TYR B N   1 
ATOM   2820 C  CA  . TYR B 1 85  ? -21.314 5.361   15.367  1.00 15.23 ? 85  TYR B CA  1 
ATOM   2821 C  C   . TYR B 1 85  ? -21.990 5.158   14.062  1.00 13.82 ? 85  TYR B C   1 
ATOM   2822 O  O   . TYR B 1 85  ? -22.401 4.047   13.736  1.00 15.42 ? 85  TYR B O   1 
ATOM   2823 C  CB  . TYR B 1 85  ? -19.938 4.695   15.317  1.00 13.35 ? 85  TYR B CB  1 
ATOM   2824 C  CG  . TYR B 1 85  ? -19.080 5.133   16.435  1.00 13.75 ? 85  TYR B CG  1 
ATOM   2825 C  CD1 . TYR B 1 85  ? -18.064 6.033   16.203  1.00 13.07 ? 85  TYR B CD1 1 
ATOM   2826 C  CD2 . TYR B 1 85  ? -19.310 4.694   17.760  1.00 15.14 ? 85  TYR B CD2 1 
ATOM   2827 C  CE1 . TYR B 1 85  ? -17.201 6.397   17.209  1.00 14.93 ? 85  TYR B CE1 1 
ATOM   2828 C  CE2 . TYR B 1 85  ? -18.451 5.071   18.786  1.00 16.95 ? 85  TYR B CE2 1 
ATOM   2829 C  CZ  . TYR B 1 85  ? -17.439 5.968   18.507  1.00 16.46 ? 85  TYR B CZ  1 
ATOM   2830 O  OH  . TYR B 1 85  ? -16.586 6.348   19.504  1.00 19.89 ? 85  TYR B OH  1 
ATOM   2831 N  N   . SER B 1 86  ? -22.170 6.248   13.310  1.00 15.20 ? 86  SER B N   1 
ATOM   2832 C  CA  . SER B 1 86  ? -22.819 6.172   11.998  1.00 14.34 ? 86  SER B CA  1 
ATOM   2833 C  C   . SER B 1 86  ? -21.772 6.170   10.869  1.00 11.13 ? 86  SER B C   1 
ATOM   2834 O  O   . SER B 1 86  ? -20.710 6.859   10.931  1.00 12.12 ? 86  SER B O   1 
ATOM   2835 C  CB  . SER B 1 86  ? -23.734 7.382   11.746  1.00 19.06 ? 86  SER B CB  1 
ATOM   2836 O  OG  . SER B 1 86  ? -24.843 7.279   12.643  1.00 25.10 ? 86  SER B OG  1 
ATOM   2837 N  N   . ALA B 1 87  ? -22.126 5.461   9.810   1.00 11.90 ? 87  ALA B N   1 
ATOM   2838 C  CA  . ALA B 1 87  ? -21.212 5.274   8.636   1.00 12.21 ? 87  ALA B CA  1 
ATOM   2839 C  C   . ALA B 1 87  ? -21.107 6.607   7.953   1.00 11.69 ? 87  ALA B C   1 
ATOM   2840 O  O   . ALA B 1 87  ? -22.081 7.431   7.927   1.00 13.63 ? 87  ALA B O   1 
ATOM   2841 C  CB  . ALA B 1 87  ? -21.671 4.078   7.734   1.00 12.81 ? 87  ALA B CB  1 
ATOM   2842 N  N   . THR B 1 88  ? -19.958 6.860   7.332   1.00 11.65 ? 88  THR B N   1 
ATOM   2843 C  CA  . THR B 1 88  ? -19.825 8.042   6.485   1.00 11.61 ? 88  THR B CA  1 
ATOM   2844 C  C   . THR B 1 88  ? -19.247 7.688   5.112   1.00 10.64 ? 88  THR B C   1 
ATOM   2845 O  O   . THR B 1 88  ? -19.687 8.196   4.085   1.00 13.33 ? 88  THR B O   1 
ATOM   2846 C  CB  . THR B 1 88  ? -19.025 9.160   7.157   1.00 13.24 ? 88  THR B CB  1 
ATOM   2847 O  OG1 . THR B 1 88  ? -19.019 10.224  6.197   1.00 17.28 ? 88  THR B OG1 1 
ATOM   2848 C  CG2 . THR B 1 88  ? -17.534 8.711   7.485   1.00 13.27 ? 88  THR B CG2 1 
ATOM   2849 N  N   . GLN B 1 89  ? -18.325 6.690   5.082   1.00 9.97  ? 89  GLN B N   1 
ATOM   2850 C  CA  . GLN B 1 89  ? -17.811 6.282   3.731   1.00 8.90  ? 89  GLN B CA  1 
ATOM   2851 C  C   . GLN B 1 89  ? -17.011 4.976   3.862   1.00 7.96  ? 89  GLN B C   1 
ATOM   2852 O  O   . GLN B 1 89  ? -16.693 4.661   4.974   1.00 7.46  ? 89  GLN B O   1 
ATOM   2853 C  CB  . GLN B 1 89  ? -16.875 7.404   3.113   1.00 9.93  ? 89  GLN B CB  1 
ATOM   2854 C  CG  . GLN B 1 89  ? -15.686 7.746   4.025   1.00 11.62 ? 89  GLN B CG  1 
ATOM   2855 C  CD  . GLN B 1 89  ? -14.355 7.182   3.501   1.00 11.80 ? 89  GLN B CD  1 
ATOM   2856 O  OE1 . GLN B 1 89  ? -14.287 6.002   3.258   1.00 14.05 ? 89  GLN B OE1 1 
ATOM   2857 N  NE2 . GLN B 1 89  ? -13.428 8.014   3.146   1.00 12.97 ? 89  GLN B NE2 1 
ATOM   2858 N  N   . LEU B 1 90  ? -16.805 4.271   2.758   1.00 7.33  ? 90  LEU B N   1 
ATOM   2859 C  CA  . LEU B 1 90  ? -15.811 3.140   2.757   1.00 7.37  ? 90  LEU B CA  1 
ATOM   2860 C  C   . LEU B 1 90  ? -14.809 3.348   1.599   1.00 8.71  ? 90  LEU B C   1 
ATOM   2861 O  O   . LEU B 1 90  ? -15.093 4.041   0.657   1.00 8.96  ? 90  LEU B O   1 
ATOM   2862 C  CB  . LEU B 1 90  ? -16.484 1.703   2.757   1.00 7.91  ? 90  LEU B CB  1 
ATOM   2863 C  CG  . LEU B 1 90  ? -17.394 1.446   1.608   1.00 8.38  ? 90  LEU B CG  1 
ATOM   2864 C  CD1 . LEU B 1 90  ? -16.631 1.219   0.303   1.00 8.95  ? 90  LEU B CD1 1 
ATOM   2865 C  CD2 . LEU B 1 90  ? -18.316 0.258   1.934   1.00 10.21 ? 90  LEU B CD2 1 
ATOM   2866 N  N   . HIS B 1 91  ? -13.608 2.750   1.722   1.00 7.52  ? 91  HIS B N   1 
ATOM   2867 C  CA  . HIS B 1 91  ? -12.622 2.877   0.630   1.00 7.88  ? 91  HIS B CA  1 
ATOM   2868 C  C   . HIS B 1 91  ? -11.704 1.670   0.812   1.00 7.96  ? 91  HIS B C   1 
ATOM   2869 O  O   . HIS B 1 91  ? -11.821 0.971   1.827   1.00 8.25  ? 91  HIS B O   1 
ATOM   2870 C  CB  . HIS B 1 91  ? -11.887 4.264   0.814   1.00 8.11  ? 91  HIS B CB  1 
ATOM   2871 C  CG  . HIS B 1 91  ? -11.255 4.390   2.156   1.00 6.96  ? 91  HIS B CG  1 
ATOM   2872 N  ND1 . HIS B 1 91  ? -11.846 4.848   3.251   1.00 8.16  ? 91  HIS B ND1 1 
ATOM   2873 C  CD2 . HIS B 1 91  ? -9.968  4.035   2.566   1.00 7.39  ? 91  HIS B CD2 1 
ATOM   2874 C  CE1 . HIS B 1 91  ? -11.075 4.849   4.281   1.00 7.70  ? 91  HIS B CE1 1 
ATOM   2875 N  NE2 . HIS B 1 91  ? -9.915  4.234   3.929   1.00 8.54  ? 91  HIS B NE2 1 
ATOM   2876 N  N   . LEU B 1 92  ? -10.750 1.570   -0.117  1.00 8.86  ? 92  LEU B N   1 
ATOM   2877 C  CA  . LEU B 1 92  ? -9.764  0.446   -0.062  1.00 8.36  ? 92  LEU B CA  1 
ATOM   2878 C  C   . LEU B 1 92  ? -8.337  0.961   -0.139  1.00 8.31  ? 92  LEU B C   1 
ATOM   2879 O  O   . LEU B 1 92  ? -8.057  2.133   -0.472  1.00 9.25  ? 92  LEU B O   1 
ATOM   2880 C  CB  . LEU B 1 92  ? -10.045 -0.616  -1.144  1.00 10.55 ? 92  LEU B CB  1 
ATOM   2881 C  CG  . LEU B 1 92  ? -11.435 -1.224  -1.017  1.00 12.11 ? 92  LEU B CG  1 
ATOM   2882 C  CD1 . LEU B 1 92  ? -12.401 -0.515  -1.942  1.00 12.79 ? 92  LEU B CD1 1 
ATOM   2883 C  CD2 . LEU B 1 92  ? -11.321 -2.665  -1.421  1.00 13.27 ? 92  LEU B CD2 1 
ATOM   2884 N  N   . HIS B 1 93  ? -7.461  0.002   0.129   1.00 7.28  ? 93  HIS B N   1 
ATOM   2885 C  CA  . HIS B 1 93  ? -5.990  0.233   -0.057  1.00 7.65  ? 93  HIS B CA  1 
ATOM   2886 C  C   . HIS B 1 93  ? -5.419  -0.973  -0.695  1.00 8.47  ? 93  HIS B C   1 
ATOM   2887 O  O   . HIS B 1 93  ? -5.919  -2.094  -0.425  1.00 9.76  ? 93  HIS B O   1 
ATOM   2888 C  CB  . HIS B 1 93  ? -5.295  0.390   1.289   1.00 8.24  ? 93  HIS B CB  1 
ATOM   2889 C  CG  . HIS B 1 93  ? -5.801  1.531   2.110   1.00 7.19  ? 93  HIS B CG  1 
ATOM   2890 N  ND1 . HIS B 1 93  ? -5.160  2.787   2.148   1.00 7.19  ? 93  HIS B ND1 1 
ATOM   2891 C  CD2 . HIS B 1 93  ? -6.850  1.605   3.032   1.00 6.32  ? 93  HIS B CD2 1 
ATOM   2892 C  CE1 . HIS B 1 93  ? -5.906  3.613   2.966   1.00 8.52  ? 93  HIS B CE1 1 
ATOM   2893 N  NE2 . HIS B 1 93  ? -6.895  2.921   3.483   1.00 7.18  ? 93  HIS B NE2 1 
ATOM   2894 N  N   . TRP B 1 94  ? -4.431  -0.807  -1.596  1.00 8.73  ? 94  TRP B N   1 
ATOM   2895 C  CA  . TRP B 1 94  ? -3.932  -1.975  -2.393  1.00 8.74  ? 94  TRP B CA  1 
ATOM   2896 C  C   . TRP B 1 94  ? -2.556  -1.711  -2.903  1.00 9.66  ? 94  TRP B C   1 
ATOM   2897 O  O   . TRP B 1 94  ? -1.995  -0.624  -2.661  1.00 9.02  ? 94  TRP B O   1 
ATOM   2898 C  CB  . TRP B 1 94  ? -4.834  -2.200  -3.606  1.00 9.85  ? 94  TRP B CB  1 
ATOM   2899 C  CG  . TRP B 1 94  ? -5.001  -1.003  -4.514  1.00 9.83  ? 94  TRP B CG  1 
ATOM   2900 C  CD1 . TRP B 1 94  ? -4.222  -0.637  -5.612  1.00 11.07 ? 94  TRP B CD1 1 
ATOM   2901 C  CD2 . TRP B 1 94  ? -6.049  0.021   -4.432  1.00 9.95  ? 94  TRP B CD2 1 
ATOM   2902 N  NE1 . TRP B 1 94  ? -4.704  0.513   -6.191  1.00 10.11 ? 94  TRP B NE1 1 
ATOM   2903 C  CE2 . TRP B 1 94  ? -5.798  0.960   -5.526  1.00 10.31 ? 94  TRP B CE2 1 
ATOM   2904 C  CE3 . TRP B 1 94  ? -7.124  0.245   -3.586  1.00 8.98  ? 94  TRP B CE3 1 
ATOM   2905 C  CZ2 . TRP B 1 94  ? -6.608  2.064   -5.742  1.00 10.26 ? 94  TRP B CZ2 1 
ATOM   2906 C  CZ3 . TRP B 1 94  ? -7.934  1.358   -3.816  1.00 10.23 ? 94  TRP B CZ3 1 
ATOM   2907 C  CH2 . TRP B 1 94  ? -7.680  2.246   -4.866  1.00 8.86  ? 94  TRP B CH2 1 
ATOM   2908 N  N   . GLY B 1 95  ? -2.002  -2.756  -3.554  1.00 8.82  ? 95  GLY B N   1 
ATOM   2909 C  CA  . GLY B 1 95  ? -0.557  -2.704  -4.013  1.00 8.81  ? 95  GLY B CA  1 
ATOM   2910 C  C   . GLY B 1 95  ? -0.519  -2.344  -5.505  1.00 9.70  ? 95  GLY B C   1 
ATOM   2911 O  O   . GLY B 1 95  ? -1.001  -1.286  -5.946  1.00 9.39  ? 95  GLY B O   1 
ATOM   2912 N  N   . ASN B 1 96  ? 0.035   -3.222  -6.325  1.00 10.21 ? 96  ASN B N   1 
ATOM   2913 C  CA  . ASN B 1 96  ? 0.167   -2.957  -7.760  1.00 11.98 ? 96  ASN B CA  1 
ATOM   2914 C  C   . ASN B 1 96  ? 0.161   -4.264  -8.489  1.00 12.37 ? 96  ASN B C   1 
ATOM   2915 O  O   . ASN B 1 96  ? 0.254   -5.278  -7.850  1.00 11.19 ? 96  ASN B O   1 
ATOM   2916 C  CB  . ASN B 1 96  ? 1.408   -2.110  -8.031  1.00 12.51 ? 96  ASN B CB  1 
ATOM   2917 C  CG  . ASN B 1 96  ? 2.719   -2.876  -7.795  1.00 17.75 ? 96  ASN B CG  1 
ATOM   2918 O  OD1 . ASN B 1 96  ? 3.112   -3.656  -8.676  1.00 20.34 ? 96  ASN B OD1 1 
ATOM   2919 N  ND2 . ASN B 1 96  ? 3.370   -2.678  -6.664  1.00 15.24 ? 96  ASN B ND2 1 
ATOM   2920 N  N   . PRO B 1 97  ? 0.087   -4.256  -9.846  1.00 12.21 ? 97  PRO B N   1 
ATOM   2921 C  CA  . PRO B 1 97  ? -0.151  -5.492  -10.563 1.00 14.47 ? 97  PRO B CA  1 
ATOM   2922 C  C   . PRO B 1 97  ? 0.959   -6.502  -10.349 1.00 13.40 ? 97  PRO B C   1 
ATOM   2923 O  O   . PRO B 1 97  ? 0.728   -7.741  -10.415 1.00 15.95 ? 97  PRO B O   1 
ATOM   2924 C  CB  . PRO B 1 97  ? -0.147  -5.019  -12.006 1.00 14.23 ? 97  PRO B CB  1 
ATOM   2925 C  CG  . PRO B 1 97  ? -0.778  -3.647  -11.951 1.00 15.17 ? 97  PRO B CG  1 
ATOM   2926 C  CD  . PRO B 1 97  ? -0.215  -3.087  -10.663 1.00 13.71 ? 97  PRO B CD  1 
ATOM   2927 N  N   . ASN B 1 98  ? 2.168   -6.001  -10.133 1.00 12.53 ? 98  ASN B N   1 
ATOM   2928 C  CA  . ASN B 1 98  ? 3.314   -6.901  -10.008 1.00 14.78 ? 98  ASN B CA  1 
ATOM   2929 C  C   . ASN B 1 98  ? 3.666   -7.250  -8.581  1.00 16.02 ? 98  ASN B C   1 
ATOM   2930 O  O   . ASN B 1 98  ? 4.604   -8.066  -8.311  1.00 18.50 ? 98  ASN B O   1 
ATOM   2931 C  CB  . ASN B 1 98  ? 4.533   -6.246  -10.691 1.00 13.86 ? 98  ASN B CB  1 
ATOM   2932 C  CG  . ASN B 1 98  ? 4.321   -6.023  -12.161 1.00 14.54 ? 98  ASN B CG  1 
ATOM   2933 O  OD1 . ASN B 1 98  ? 4.128   -6.999  -12.933 1.00 15.70 ? 98  ASN B OD1 1 
ATOM   2934 N  ND2 . ASN B 1 98  ? 4.200   -4.730  -12.557 1.00 18.98 ? 98  ASN B ND2 1 
ATOM   2935 N  N   . ASP B 1 99  ? 2.927   -6.683  -7.651  1.00 12.17 ? 99  ASP B N   1 
ATOM   2936 C  CA  . ASP B 1 99  ? 3.110   -6.929  -6.205  1.00 13.95 ? 99  ASP B CA  1 
ATOM   2937 C  C   . ASP B 1 99  ? 1.775   -6.716  -5.477  1.00 12.03 ? 99  ASP B C   1 
ATOM   2938 O  O   . ASP B 1 99  ? 1.507   -5.610  -4.939  1.00 12.17 ? 99  ASP B O   1 
ATOM   2939 C  CB  . ASP B 1 99  ? 4.161   -6.014  -5.595  1.00 17.07 ? 99  ASP B CB  1 
ATOM   2940 C  CG  . ASP B 1 99  ? 4.437   -6.369  -4.069  1.00 21.35 ? 99  ASP B CG  1 
ATOM   2941 O  OD1 . ASP B 1 99  ? 4.159   -7.531  -3.695  1.00 27.26 ? 99  ASP B OD1 1 
ATOM   2942 O  OD2 . ASP B 1 99  ? 4.822   -5.455  -3.310  1.00 28.44 ? 99  ASP B OD2 1 
ATOM   2943 N  N   . PRO B 1 100 ? 0.888   -7.718  -5.577  1.00 12.46 ? 100 PRO B N   1 
ATOM   2944 C  CA  . PRO B 1 100 ? -0.462  -7.527  -5.041  1.00 12.80 ? 100 PRO B CA  1 
ATOM   2945 C  C   . PRO B 1 100 ? -0.474  -7.802  -3.526  1.00 12.37 ? 100 PRO B C   1 
ATOM   2946 O  O   . PRO B 1 100 ? -1.028  -8.812  -3.015  1.00 14.00 ? 100 PRO B O   1 
ATOM   2947 C  CB  . PRO B 1 100 ? -1.274  -8.479  -5.881  1.00 13.47 ? 100 PRO B CB  1 
ATOM   2948 C  CG  . PRO B 1 100 ? -0.297  -9.619  -6.115  1.00 16.71 ? 100 PRO B CG  1 
ATOM   2949 C  CD  . PRO B 1 100 ? 1.017   -8.986  -6.329  1.00 15.24 ? 100 PRO B CD  1 
ATOM   2950 N  N   . HIS B 1 101 ? 0.190   -6.899  -2.797  1.00 11.82 ? 101 HIS B N   1 
ATOM   2951 C  CA  . HIS B 1 101 ? 0.354   -6.992  -1.289  1.00 12.70 ? 101 HIS B CA  1 
ATOM   2952 C  C   . HIS B 1 101 ? 0.286   -5.660  -0.635  1.00 15.89 ? 101 HIS B C   1 
ATOM   2953 O  O   . HIS B 1 101 ? 1.228   -5.205  0.013   1.00 20.82 ? 101 HIS B O   1 
ATOM   2954 C  CB  . HIS B 1 101 ? 1.666   -7.681  -0.887  1.00 14.33 ? 101 HIS B CB  1 
ATOM   2955 C  CG  . HIS B 1 101 ? 1.775   -9.019  -1.463  1.00 17.34 ? 101 HIS B CG  1 
ATOM   2956 N  ND1 . HIS B 1 101 ? 1.208   -10.111 -0.883  1.00 23.34 ? 101 HIS B ND1 1 
ATOM   2957 C  CD2 . HIS B 1 101 ? 2.295   -9.433  -2.677  1.00 17.31 ? 101 HIS B CD2 1 
ATOM   2958 C  CE1 . HIS B 1 101 ? 1.388   -11.182 -1.702  1.00 22.45 ? 101 HIS B CE1 1 
ATOM   2959 N  NE2 . HIS B 1 101 ? 2.036   -10.775 -2.790  1.00 22.93 ? 101 HIS B NE2 1 
ATOM   2960 N  N   . GLY B 1 102 ? -0.908  -5.090  -0.670  1.00 11.91 ? 102 GLY B N   1 
ATOM   2961 C  CA  . GLY B 1 102 ? -1.053  -3.668  -0.245  1.00 10.35 ? 102 GLY B CA  1 
ATOM   2962 C  C   . GLY B 1 102 ? -2.047  -3.457  0.920   1.00 10.02 ? 102 GLY B C   1 
ATOM   2963 O  O   . GLY B 1 102 ? -2.537  -2.331  1.069   1.00 9.66  ? 102 GLY B O   1 
ATOM   2964 N  N   . SER B 1 103 ? -2.273  -4.421  1.777   1.00 10.32 ? 103 SER B N   1 
ATOM   2965 C  CA  . SER B 1 103 ? -2.975  -4.112  3.012   1.00 9.79  ? 103 SER B CA  1 
ATOM   2966 C  C   . SER B 1 103 ? -2.176  -3.145  3.861   1.00 12.37 ? 103 SER B C   1 
ATOM   2967 O  O   . SER B 1 103 ? -0.932  -3.064  3.729   1.00 10.53 ? 103 SER B O   1 
ATOM   2968 C  CB  . SER B 1 103 ? -3.317  -5.393  3.810   1.00 10.57 ? 103 SER B CB  1 
ATOM   2969 O  OG  . SER B 1 103 ? -2.084  -5.918  4.380   1.00 10.26 ? 103 SER B OG  1 
ATOM   2970 N  N   . GLU B 1 104 ? -2.881  -2.404  4.711   1.00 9.53  ? 104 GLU B N   1 
ATOM   2971 C  CA  . GLU B 1 104 ? -2.277  -1.499  5.657   1.00 9.83  ? 104 GLU B CA  1 
ATOM   2972 C  C   . GLU B 1 104 ? -1.841  -2.189  6.910   1.00 9.26  ? 104 GLU B C   1 
ATOM   2973 O  O   . GLU B 1 104 ? -0.694  -2.198  7.175   1.00 9.18  ? 104 GLU B O   1 
ATOM   2974 C  CB  . GLU B 1 104 ? -3.183  -0.279  5.992   1.00 9.99  ? 104 GLU B CB  1 
ATOM   2975 C  CG  . GLU B 1 104 ? -3.524  0.447   4.719   1.00 10.01 ? 104 GLU B CG  1 
ATOM   2976 C  CD  . GLU B 1 104 ? -3.650  1.906   5.013   1.00 10.89 ? 104 GLU B CD  1 
ATOM   2977 O  OE1 . GLU B 1 104 ? -4.651  2.314   5.650   1.00 10.56 ? 104 GLU B OE1 1 
ATOM   2978 O  OE2 . GLU B 1 104 ? -2.767  2.693   4.640   1.00 11.27 ? 104 GLU B OE2 1 
ATOM   2979 N  N   . HIS B 1 105 ? -2.732  -2.812  7.657   1.00 9.99  ? 105 HIS B N   1 
ATOM   2980 C  CA  . HIS B 1 105 ? -2.282  -3.689  8.723   1.00 9.56  ? 105 HIS B CA  1 
ATOM   2981 C  C   . HIS B 1 105 ? -1.687  -4.989  8.204   1.00 10.24 ? 105 HIS B C   1 
ATOM   2982 O  O   . HIS B 1 105 ? -2.043  -5.470  7.093   1.00 9.98  ? 105 HIS B O   1 
ATOM   2983 C  CB  . HIS B 1 105 ? -3.540  -4.067  9.576   1.00 10.17 ? 105 HIS B CB  1 
ATOM   2984 C  CG  . HIS B 1 105 ? -4.151  -2.886  10.249  1.00 9.56  ? 105 HIS B CG  1 
ATOM   2985 N  ND1 . HIS B 1 105 ? -5.062  -2.064  9.655   1.00 9.97  ? 105 HIS B ND1 1 
ATOM   2986 C  CD2 . HIS B 1 105 ? -3.862  -2.333  11.462  1.00 9.49  ? 105 HIS B CD2 1 
ATOM   2987 C  CE1 . HIS B 1 105 ? -5.364  -1.090  10.482  1.00 9.84  ? 105 HIS B CE1 1 
ATOM   2988 N  NE2 . HIS B 1 105 ? -4.667  -1.262  11.608  1.00 10.59 ? 105 HIS B NE2 1 
ATOM   2989 N  N   . THR B 1 106 ? -0.680  -5.448  8.975   1.00 10.25 ? 106 THR B N   1 
ATOM   2990 C  CA  . THR B 1 106 ? -0.110  -6.763  8.643   1.00 10.31 ? 106 THR B CA  1 
ATOM   2991 C  C   . THR B 1 106 ? -0.349  -7.632  9.845   1.00 10.24 ? 106 THR B C   1 
ATOM   2992 O  O   . THR B 1 106 ? -0.694  -7.192  10.925  1.00 9.20  ? 106 THR B O   1 
ATOM   2993 C  CB  . THR B 1 106 ? 1.427   -6.605  8.366   1.00 11.77 ? 106 THR B CB  1 
ATOM   2994 O  OG1 . THR B 1 106 ? 2.036   -5.932  9.487   1.00 11.94 ? 106 THR B OG1 1 
ATOM   2995 C  CG2 . THR B 1 106 ? 1.633   -5.715  7.177   1.00 13.33 ? 106 THR B CG2 1 
ATOM   2996 N  N   . VAL B 1 107 ? -0.131  -8.949  9.628   1.00 12.58 ? 107 VAL B N   1 
ATOM   2997 C  CA  . VAL B 1 107 ? -0.434  -9.954  10.668  1.00 16.10 ? 107 VAL B CA  1 
ATOM   2998 C  C   . VAL B 1 107 ? 0.792   -10.820 10.676  1.00 14.99 ? 107 VAL B C   1 
ATOM   2999 O  O   . VAL B 1 107 ? 1.185   -11.367 9.637   1.00 18.37 ? 107 VAL B O   1 
ATOM   3000 C  CB  . VAL B 1 107 ? -1.723  -10.807 10.425  1.00 15.57 ? 107 VAL B CB  1 
ATOM   3001 C  CG1 . VAL B 1 107 ? -1.881  -11.874 11.504  1.00 17.00 ? 107 VAL B CG1 1 
ATOM   3002 C  CG2 . VAL B 1 107 ? -2.977  -9.948  10.388  1.00 15.06 ? 107 VAL B CG2 1 
ATOM   3003 N  N   . SER B 1 108 ? 1.418   -10.851 11.852  1.00 17.31 ? 108 SER B N   1 
ATOM   3004 C  CA  . SER B 1 108 ? 2.710   -11.534 12.085  1.00 19.19 ? 108 SER B CA  1 
ATOM   3005 C  C   . SER B 1 108 ? 3.640   -11.222 10.903  1.00 19.72 ? 108 SER B C   1 
ATOM   3006 O  O   . SER B 1 108 ? 4.212   -12.128 10.271  1.00 20.74 ? 108 SER B O   1 
ATOM   3007 C  CB  . SER B 1 108 ? 2.470   -13.045 12.324  1.00 20.22 ? 108 SER B CB  1 
ATOM   3008 O  OG  . SER B 1 108 ? 1.585   -13.188 13.437  1.00 21.00 ? 108 SER B OG  1 
ATOM   3009 N  N   . GLY B 1 109 ? 3.760   -9.933  10.582  1.00 18.46 ? 109 GLY B N   1 
ATOM   3010 C  CA  . GLY B 1 109 ? 4.638   -9.410  9.602   1.00 18.64 ? 109 GLY B CA  1 
ATOM   3011 C  C   . GLY B 1 109 ? 4.330   -9.524  8.086   1.00 20.37 ? 109 GLY B C   1 
ATOM   3012 O  O   . GLY B 1 109 ? 5.097   -8.956  7.253   1.00 25.61 ? 109 GLY B O   1 
ATOM   3013 N  N   . GLN B 1 110 ? 3.201   -10.153 7.769   1.00 19.78 ? 110 GLN B N   1 
ATOM   3014 C  CA  . GLN B 1 110 ? 2.770   -10.377 6.383   1.00 19.85 ? 110 GLN B CA  1 
ATOM   3015 C  C   . GLN B 1 110 ? 1.630   -9.427  5.964   1.00 15.07 ? 110 GLN B C   1 
ATOM   3016 O  O   . GLN B 1 110 ? 0.617   -9.200  6.744   1.00 13.66 ? 110 GLN B O   1 
ATOM   3017 C  CB  . GLN B 1 110 ? 2.249   -11.811 6.242   1.00 22.61 ? 110 GLN B CB  1 
ATOM   3018 C  CG  . GLN B 1 110 ? 2.958   -12.908 7.062   1.00 31.15 ? 110 GLN B CG  1 
ATOM   3019 C  CD  . GLN B 1 110 ? 3.744   -13.851 6.198   1.00 37.17 ? 110 GLN B CD  1 
ATOM   3020 O  OE1 . GLN B 1 110 ? 4.652   -13.449 5.424   1.00 38.88 ? 110 GLN B OE1 1 
ATOM   3021 N  NE2 . GLN B 1 110 ? 3.368   -15.126 6.272   1.00 40.93 ? 110 GLN B NE2 1 
ATOM   3022 N  N   . HIS B 1 111 ? 1.774   -8.899  4.740   1.00 13.90 ? 111 HIS B N   1 
ATOM   3023 C  CA  . HIS B 1 111 ? 0.742   -8.125  4.094   1.00 14.45 ? 111 HIS B CA  1 
ATOM   3024 C  C   . HIS B 1 111 ? -0.282  -9.014  3.424   1.00 12.29 ? 111 HIS B C   1 
ATOM   3025 O  O   . HIS B 1 111 ? 0.077   -10.010 2.772   1.00 17.30 ? 111 HIS B O   1 
ATOM   3026 C  CB  . HIS B 1 111 ? 1.261   -7.246  2.938   1.00 17.26 ? 111 HIS B CB  1 
ATOM   3027 C  CG  . HIS B 1 111 ? 1.924   -6.007  3.382   1.00 17.66 ? 111 HIS B CG  1 
ATOM   3028 N  ND1 . HIS B 1 111 ? 1.248   -4.829  3.545   1.00 17.21 ? 111 HIS B ND1 1 
ATOM   3029 C  CD2 . HIS B 1 111 ? 3.265   -5.772  3.689   1.00 17.90 ? 111 HIS B CD2 1 
ATOM   3030 C  CE1 . HIS B 1 111 ? 2.146   -3.868  3.947   1.00 17.53 ? 111 HIS B CE1 1 
ATOM   3031 N  NE2 . HIS B 1 111 ? 3.380   -4.471  4.068   1.00 20.44 ? 111 HIS B NE2 1 
ATOM   3032 N  N   . PHE B 1 112 ? -1.556  -8.708  3.549   1.00 10.82 ? 112 PHE B N   1 
ATOM   3033 C  CA  . PHE B 1 112 ? -2.586  -9.152  2.707   1.00 10.85 ? 112 PHE B CA  1 
ATOM   3034 C  C   . PHE B 1 112 ? -2.668  -8.376  1.391   1.00 10.72 ? 112 PHE B C   1 
ATOM   3035 O  O   . PHE B 1 112 ? -1.929  -7.404  1.198   1.00 10.82 ? 112 PHE B O   1 
ATOM   3036 C  CB  . PHE B 1 112 ? -3.892  -9.057  3.514   1.00 13.67 ? 112 PHE B CB  1 
ATOM   3037 C  CG  . PHE B 1 112 ? -4.015  -10.148 4.555   1.00 14.10 ? 112 PHE B CG  1 
ATOM   3038 C  CD1 . PHE B 1 112 ? -4.713  -11.308 4.259   1.00 17.13 ? 112 PHE B CD1 1 
ATOM   3039 C  CD2 . PHE B 1 112 ? -3.367  -10.015 5.799   1.00 17.93 ? 112 PHE B CD2 1 
ATOM   3040 C  CE1 . PHE B 1 112 ? -4.802  -12.343 5.178   1.00 22.12 ? 112 PHE B CE1 1 
ATOM   3041 C  CE2 . PHE B 1 112 ? -3.448  -11.038 6.732   1.00 19.30 ? 112 PHE B CE2 1 
ATOM   3042 C  CZ  . PHE B 1 112 ? -4.175  -12.190 6.389   1.00 18.50 ? 112 PHE B CZ  1 
ATOM   3043 N  N   . ALA B 1 113 ? -3.493  -8.848  0.459   1.00 10.48 ? 113 ALA B N   1 
ATOM   3044 C  CA  . ALA B 1 113 ? -3.457  -8.314  -0.900  1.00 9.86  ? 113 ALA B CA  1 
ATOM   3045 C  C   . ALA B 1 113 ? -3.963  -6.867  -0.855  1.00 9.57  ? 113 ALA B C   1 
ATOM   3046 O  O   . ALA B 1 113 ? -3.489  -5.984  -1.579  1.00 9.82  ? 113 ALA B O   1 
ATOM   3047 C  CB  . ALA B 1 113 ? -4.369  -9.095  -1.829  1.00 10.82 ? 113 ALA B CB  1 
ATOM   3048 N  N   . ALA B 1 114 ? -4.996  -6.660  -0.027  1.00 8.88  ? 114 ALA B N   1 
ATOM   3049 C  CA  . ALA B 1 114 ? -5.687  -5.313  -0.002  1.00 7.90  ? 114 ALA B CA  1 
ATOM   3050 C  C   . ALA B 1 114 ? -6.455  -5.229  1.335   1.00 8.74  ? 114 ALA B C   1 
ATOM   3051 O  O   . ALA B 1 114 ? -6.362  -6.142  2.169   1.00 9.75  ? 114 ALA B O   1 
ATOM   3052 C  CB  . ALA B 1 114 ? -6.634  -5.190  -1.187  1.00 8.54  ? 114 ALA B CB  1 
ATOM   3053 N  N   . GLU B 1 115 ? -7.040  -4.015  1.550   1.00 7.71  ? 115 GLU B N   1 
ATOM   3054 C  CA  . GLU B 1 115 ? -7.747  -3.800  2.786   1.00 7.60  ? 115 GLU B CA  1 
ATOM   3055 C  C   . GLU B 1 115 ? -8.890  -2.883  2.572   1.00 8.33  ? 115 GLU B C   1 
ATOM   3056 O  O   . GLU B 1 115 ? -8.800  -1.901  1.866   1.00 9.23  ? 115 GLU B O   1 
ATOM   3057 C  CB  . GLU B 1 115 ? -6.753  -3.306  3.850   1.00 7.59  ? 115 GLU B CB  1 
ATOM   3058 C  CG  . GLU B 1 115 ? -7.322  -3.274  5.287   1.00 8.59  ? 115 GLU B CG  1 
ATOM   3059 C  CD  . GLU B 1 115 ? -6.275  -2.979  6.315   1.00 9.64  ? 115 GLU B CD  1 
ATOM   3060 O  OE1 . GLU B 1 115 ? -6.560  -2.331  7.342   1.00 10.68 ? 115 GLU B OE1 1 
ATOM   3061 O  OE2 . GLU B 1 115 ? -5.104  -3.363  6.123   1.00 10.56 ? 115 GLU B OE2 1 
ATOM   3062 N  N   . LEU B 1 116 ? -10.053 -3.295  3.090   1.00 7.51  ? 116 LEU B N   1 
ATOM   3063 C  CA  . LEU B 1 116 ? -11.282 -2.407  3.032   1.00 7.21  ? 116 LEU B CA  1 
ATOM   3064 C  C   . LEU B 1 116 ? -11.483 -1.750  4.413   1.00 7.98  ? 116 LEU B C   1 
ATOM   3065 O  O   . LEU B 1 116 ? -11.346 -2.353  5.492   1.00 7.73  ? 116 LEU B O   1 
ATOM   3066 C  CB  . LEU B 1 116 ? -12.579 -3.257  2.713   1.00 8.34  ? 116 LEU B CB  1 
ATOM   3067 C  CG  . LEU B 1 116 ? -13.903 -2.480  3.030   1.00 9.84  ? 116 LEU B CG  1 
ATOM   3068 C  CD1 . LEU B 1 116 ? -14.181 -1.634  1.828   1.00 12.22 ? 116 LEU B CD1 1 
ATOM   3069 C  CD2 . LEU B 1 116 ? -14.996 -3.532  3.158   1.00 10.04 ? 116 LEU B CD2 1 
ATOM   3070 N  N   . HIS B 1 117 ? -11.688 -0.392  4.361   1.00 7.56  ? 117 HIS B N   1 
ATOM   3071 C  CA  . HIS B 1 117 ? -12.028 0.419   5.565   1.00 7.68  ? 117 HIS B CA  1 
ATOM   3072 C  C   . HIS B 1 117 ? -13.415 0.966   5.451   1.00 7.44  ? 117 HIS B C   1 
ATOM   3073 O  O   . HIS B 1 117 ? -13.778 1.569   4.462   1.00 7.60  ? 117 HIS B O   1 
ATOM   3074 C  CB  . HIS B 1 117 ? -11.047 1.575   5.751   1.00 7.40  ? 117 HIS B CB  1 
ATOM   3075 C  CG  . HIS B 1 117 ? -9.678  1.083   6.148   1.00 7.51  ? 117 HIS B CG  1 
ATOM   3076 N  ND1 . HIS B 1 117 ? -8.520  1.784   5.926   1.00 8.44  ? 117 HIS B ND1 1 
ATOM   3077 C  CD2 . HIS B 1 117 ? -9.283  -0.144  6.606   1.00 7.09  ? 117 HIS B CD2 1 
ATOM   3078 C  CE1 . HIS B 1 117 ? -7.506  1.140   6.412   1.00 7.36  ? 117 HIS B CE1 1 
ATOM   3079 N  NE2 . HIS B 1 117 ? -7.912  -0.112  6.721   1.00 7.29  ? 117 HIS B NE2 1 
ATOM   3080 N  N   . ILE B 1 118 ? -14.227 0.757   6.510   1.00 9.07  ? 118 ILE B N   1 
ATOM   3081 C  CA  . ILE B 1 118 ? -15.567 1.378   6.584   1.00 8.56  ? 118 ILE B CA  1 
ATOM   3082 C  C   . ILE B 1 118 ? -15.486 2.360   7.742   1.00 7.99  ? 118 ILE B C   1 
ATOM   3083 O  O   . ILE B 1 118 ? -15.326 2.030   8.919   1.00 7.73  ? 118 ILE B O   1 
ATOM   3084 C  CB  . ILE B 1 118 ? -16.684 0.360   6.828   1.00 8.53  ? 118 ILE B CB  1 
ATOM   3085 C  CG1 . ILE B 1 118 ? -16.620 -0.801  5.844   1.00 9.66  ? 118 ILE B CG1 1 
ATOM   3086 C  CG2 . ILE B 1 118 ? -18.016 1.142   6.739   1.00 9.30  ? 118 ILE B CG2 1 
ATOM   3087 C  CD1 . ILE B 1 118 ? -17.663 -1.932  6.054   1.00 12.25 ? 118 ILE B CD1 1 
ATOM   3088 N  N   . VAL B 1 119 ? -15.546 3.698   7.412   1.00 8.87  ? 119 VAL B N   1 
ATOM   3089 C  CA  . VAL B 1 119 ? -15.303 4.818   8.336   1.00 9.79  ? 119 VAL B CA  1 
ATOM   3090 C  C   . VAL B 1 119 ? -16.640 5.223   8.955   1.00 9.10  ? 119 VAL B C   1 
ATOM   3091 O  O   . VAL B 1 119 ? -17.553 5.406   8.226   1.00 10.27 ? 119 VAL B O   1 
ATOM   3092 C  CB  . VAL B 1 119 ? -14.710 6.009   7.555   1.00 10.06 ? 119 VAL B CB  1 
ATOM   3093 C  CG1 . VAL B 1 119 ? -14.389 7.138   8.577   1.00 11.32 ? 119 VAL B CG1 1 
ATOM   3094 C  CG2 . VAL B 1 119 ? -13.379 5.529   6.881   1.00 8.90  ? 119 VAL B CG2 1 
ATOM   3095 N  N   . HIS B 1 120 ? -16.674 5.285   10.273  1.00 10.30 ? 120 HIS B N   1 
ATOM   3096 C  CA  . HIS B 1 120 ? -17.866 5.754   10.995  1.00 12.67 ? 120 HIS B CA  1 
ATOM   3097 C  C   . HIS B 1 120 ? -17.437 6.864   11.944  1.00 11.66 ? 120 HIS B C   1 
ATOM   3098 O  O   . HIS B 1 120 ? -16.254 7.038   12.333  1.00 10.81 ? 120 HIS B O   1 
ATOM   3099 C  CB  . HIS B 1 120 ? -18.459 4.631   11.878  1.00 12.26 ? 120 HIS B CB  1 
ATOM   3100 C  CG  . HIS B 1 120 ? -18.792 3.341   11.163  1.00 11.77 ? 120 HIS B CG  1 
ATOM   3101 N  ND1 . HIS B 1 120 ? -17.844 2.500   10.585  1.00 12.00 ? 120 HIS B ND1 1 
ATOM   3102 C  CD2 . HIS B 1 120 ? -20.048 2.750   10.924  1.00 11.84 ? 120 HIS B CD2 1 
ATOM   3103 C  CE1 . HIS B 1 120 ? -18.498 1.431   10.024  1.00 11.65 ? 120 HIS B CE1 1 
ATOM   3104 N  NE2 . HIS B 1 120 ? -19.851 1.548   10.268  1.00 12.96 ? 120 HIS B NE2 1 
ATOM   3105 N  N   . TYR B 1 121 ? -18.421 7.677   12.358  1.00 13.08 ? 121 TYR B N   1 
ATOM   3106 C  CA  . TYR B 1 121 ? -18.182 8.753   13.319  1.00 14.49 ? 121 TYR B CA  1 
ATOM   3107 C  C   . TYR B 1 121 ? -19.237 8.718   14.433  1.00 14.61 ? 121 TYR B C   1 
ATOM   3108 O  O   . TYR B 1 121 ? -20.351 8.258   14.189  1.00 14.71 ? 121 TYR B O   1 
ATOM   3109 C  CB  . TYR B 1 121 ? -18.237 10.117  12.570  1.00 13.28 ? 121 TYR B CB  1 
ATOM   3110 C  CG  . TYR B 1 121 ? -19.640 10.512  12.091  1.00 14.88 ? 121 TYR B CG  1 
ATOM   3111 C  CD1 . TYR B 1 121 ? -20.439 11.444  12.829  1.00 17.90 ? 121 TYR B CD1 1 
ATOM   3112 C  CD2 . TYR B 1 121 ? -20.123 10.029  10.893  1.00 15.10 ? 121 TYR B CD2 1 
ATOM   3113 C  CE1 . TYR B 1 121 ? -21.700 11.786  12.363  1.00 15.84 ? 121 TYR B CE1 1 
ATOM   3114 C  CE2 . TYR B 1 121 ? -21.410 10.330  10.469  1.00 15.65 ? 121 TYR B CE2 1 
ATOM   3115 C  CZ  . TYR B 1 121 ? -22.145 11.270  11.195  1.00 18.31 ? 121 TYR B CZ  1 
ATOM   3116 O  OH  . TYR B 1 121 ? -23.402 11.634  10.749  1.00 23.14 ? 121 TYR B OH  1 
ATOM   3117 N  N   . ASN B 1 122 ? -18.882 9.211   15.617  1.00 14.53 ? 122 ASN B N   1 
ATOM   3118 C  CA  . ASN B 1 122 ? -19.832 9.210   16.729  1.00 15.60 ? 122 ASN B CA  1 
ATOM   3119 C  C   . ASN B 1 122 ? -20.982 10.249  16.518  1.00 17.21 ? 122 ASN B C   1 
ATOM   3120 O  O   . ASN B 1 122 ? -20.746 11.464  16.706  1.00 17.64 ? 122 ASN B O   1 
ATOM   3121 C  CB  . ASN B 1 122 ? -19.139 9.559   18.018  1.00 18.31 ? 122 ASN B CB  1 
ATOM   3122 C  CG  . ASN B 1 122 ? -20.111 9.532   19.207  1.00 17.21 ? 122 ASN B CG  1 
ATOM   3123 O  OD1 . ASN B 1 122 ? -21.343 9.679   19.071  1.00 20.59 ? 122 ASN B OD1 1 
ATOM   3124 N  ND2 . ASN B 1 122 ? -19.567 9.321   20.360  1.00 20.49 ? 122 ASN B ND2 1 
ATOM   3125 N  N   . SER B 1 123 ? -22.093 9.771   15.984  1.00 20.66 ? 123 SER B N   1 
ATOM   3126 C  CA  . SER B 1 123 ? -23.237 10.633  15.607  1.00 19.11 ? 123 SER B CA  1 
ATOM   3127 C  C   . SER B 1 123 ? -24.156 10.926  16.803  1.00 23.68 ? 123 SER B C   1 
ATOM   3128 O  O   . SER B 1 123 ? -25.104 11.735  16.680  1.00 22.11 ? 123 SER B O   1 
ATOM   3129 C  CB  . SER B 1 123 ? -24.037 9.961   14.500  1.00 22.22 ? 123 SER B CB  1 
ATOM   3130 O  OG  . SER B 1 123 ? -24.423 8.659   14.921  1.00 22.20 ? 123 SER B OG  1 
ATOM   3131 N  N   . ASP B 1 124 ? -23.921 10.266  17.919  1.00 22.53 ? 124 ASP B N   1 
ATOM   3132 C  CA  . ASP B 1 124 ? -24.534 10.673  19.205  1.00 25.35 ? 124 ASP B CA  1 
ATOM   3133 C  C   . ASP B 1 124 ? -24.063 12.061  19.638  1.00 28.19 ? 124 ASP B C   1 
ATOM   3134 O  O   . ASP B 1 124 ? -24.850 12.859  20.181  1.00 26.06 ? 124 ASP B O   1 
ATOM   3135 C  CB  . ASP B 1 124 ? -24.226 9.653   20.315  1.00 25.24 ? 124 ASP B CB  1 
ATOM   3136 C  CG  . ASP B 1 124 ? -25.059 8.388   20.206  1.00 26.75 ? 124 ASP B CG  1 
ATOM   3137 O  OD1 . ASP B 1 124 ? -26.081 8.417   19.455  1.00 31.09 ? 124 ASP B OD1 1 
ATOM   3138 O  OD2 . ASP B 1 124 ? -24.721 7.358   20.872  1.00 26.83 ? 124 ASP B OD2 1 
ATOM   3139 N  N   . LEU B 1 125 ? -22.802 12.360  19.338  1.00 22.82 ? 125 LEU B N   1 
ATOM   3140 C  CA  . LEU B 1 125 ? -22.063 13.537  19.862  1.00 23.54 ? 125 LEU B CA  1 
ATOM   3141 C  C   . LEU B 1 125 ? -21.800 14.589  18.801  1.00 27.70 ? 125 LEU B C   1 
ATOM   3142 O  O   . LEU B 1 125 ? -21.793 15.805  19.126  1.00 25.84 ? 125 LEU B O   1 
ATOM   3143 C  CB  . LEU B 1 125 ? -20.762 13.042  20.458  1.00 24.29 ? 125 LEU B CB  1 
ATOM   3144 C  CG  . LEU B 1 125 ? -20.480 12.994  21.952  1.00 29.60 ? 125 LEU B CG  1 
ATOM   3145 C  CD1 . LEU B 1 125 ? -21.729 12.764  22.817  1.00 26.00 ? 125 LEU B CD1 1 
ATOM   3146 C  CD2 . LEU B 1 125 ? -19.277 12.131  22.350  1.00 25.25 ? 125 LEU B CD2 1 
ATOM   3147 N  N   . TYR B 1 126 ? -21.624 14.170  17.528  1.00 23.31 ? 126 TYR B N   1 
ATOM   3148 C  CA  . TYR B 1 126 ? -21.202 15.093  16.454  1.00 23.29 ? 126 TYR B CA  1 
ATOM   3149 C  C   . TYR B 1 126 ? -22.128 15.043  15.269  1.00 24.32 ? 126 TYR B C   1 
ATOM   3150 O  O   . TYR B 1 126 ? -22.740 13.998  14.993  1.00 23.93 ? 126 TYR B O   1 
ATOM   3151 C  CB  . TYR B 1 126 ? -19.693 14.881  16.058  1.00 23.62 ? 126 TYR B CB  1 
ATOM   3152 C  CG  . TYR B 1 126 ? -18.819 14.776  17.260  1.00 23.84 ? 126 TYR B CG  1 
ATOM   3153 C  CD1 . TYR B 1 126 ? -18.633 15.885  18.092  1.00 26.18 ? 126 TYR B CD1 1 
ATOM   3154 C  CD2 . TYR B 1 126 ? -18.222 13.547  17.630  1.00 24.31 ? 126 TYR B CD2 1 
ATOM   3155 C  CE1 . TYR B 1 126 ? -17.877 15.799  19.229  1.00 26.20 ? 126 TYR B CE1 1 
ATOM   3156 C  CE2 . TYR B 1 126 ? -17.478 13.435  18.781  1.00 25.81 ? 126 TYR B CE2 1 
ATOM   3157 C  CZ  . TYR B 1 126 ? -17.310 14.572  19.580  1.00 27.78 ? 126 TYR B CZ  1 
ATOM   3158 O  OH  . TYR B 1 126 ? -16.554 14.490  20.731  1.00 32.57 ? 126 TYR B OH  1 
ATOM   3159 N  N   . PRO B 1 127 ? -22.298 16.188  14.583  1.00 23.85 ? 127 PRO B N   1 
ATOM   3160 C  CA  . PRO B 1 127 ? -23.245 16.222  13.515  1.00 25.44 ? 127 PRO B CA  1 
ATOM   3161 C  C   . PRO B 1 127 ? -22.673 15.766  12.148  1.00 25.26 ? 127 PRO B C   1 
ATOM   3162 O  O   . PRO B 1 127 ? -23.431 15.656  11.176  1.00 29.44 ? 127 PRO B O   1 
ATOM   3163 C  CB  . PRO B 1 127 ? -23.659 17.716  13.511  1.00 27.37 ? 127 PRO B CB  1 
ATOM   3164 C  CG  . PRO B 1 127 ? -22.382 18.425  13.866  1.00 30.55 ? 127 PRO B CG  1 
ATOM   3165 C  CD  . PRO B 1 127 ? -21.692 17.509  14.849  1.00 25.78 ? 127 PRO B CD  1 
ATOM   3166 N  N   . ASP B 1 128 ? -21.384 15.432  12.080  1.00 25.51 ? 128 ASP B N   1 
ATOM   3167 C  CA  . ASP B 1 128 ? -20.776 15.010  10.820  1.00 22.38 ? 128 ASP B CA  1 
ATOM   3168 C  C   . ASP B 1 128 ? -19.403 14.523  11.178  1.00 22.51 ? 128 ASP B C   1 
ATOM   3169 O  O   . ASP B 1 128 ? -18.864 14.869  12.232  1.00 20.56 ? 128 ASP B O   1 
ATOM   3170 C  CB  . ASP B 1 128 ? -20.652 16.215  9.880   1.00 26.05 ? 128 ASP B CB  1 
ATOM   3171 C  CG  . ASP B 1 128 ? -19.798 17.272  10.453  1.00 27.47 ? 128 ASP B CG  1 
ATOM   3172 O  OD1 . ASP B 1 128 ? -20.281 18.030  11.342  1.00 32.35 ? 128 ASP B OD1 1 
ATOM   3173 O  OD2 . ASP B 1 128 ? -18.657 17.385  10.006  1.00 28.37 ? 128 ASP B OD2 1 
ATOM   3174 N  N   . ALA B 1 129 ? -18.858 13.669  10.299  1.00 20.95 ? 129 ALA B N   1 
ATOM   3175 C  CA  . ALA B 1 129 ? -17.564 13.046  10.463  1.00 21.38 ? 129 ALA B CA  1 
ATOM   3176 C  C   . ALA B 1 129 ? -16.386 14.001  10.554  1.00 19.41 ? 129 ALA B C   1 
ATOM   3177 O  O   . ALA B 1 129 ? -15.445 13.752  11.339  1.00 20.25 ? 129 ALA B O   1 
ATOM   3178 C  CB  . ALA B 1 129 ? -17.322 12.009  9.334   1.00 22.24 ? 129 ALA B CB  1 
ATOM   3179 N  N   . SER B 1 130 ? -16.444 15.126  9.821   1.00 19.46 ? 130 SER B N   1 
ATOM   3180 C  CA  . SER B 1 130 ? -15.305 16.081  9.897   1.00 22.95 ? 130 SER B CA  1 
ATOM   3181 C  C   . SER B 1 130 ? -15.154 16.663  11.287  1.00 20.50 ? 130 SER B C   1 
ATOM   3182 O  O   . SER B 1 130 ? -14.064 16.754  11.811  1.00 20.34 ? 130 SER B O   1 
ATOM   3183 C  CB  . SER B 1 130 ? -15.425 17.230  8.923   1.00 26.41 ? 130 SER B CB  1 
ATOM   3184 O  OG  . SER B 1 130 ? -15.630 16.814  7.609   1.00 29.68 ? 130 SER B OG  1 
ATOM   3185 N  N   . THR B 1 131 ? -16.272 17.044  11.878  1.00 20.85 ? 131 THR B N   1 
ATOM   3186 C  CA  . THR B 1 131 ? -16.252 17.495  13.260  1.00 21.91 ? 131 THR B CA  1 
ATOM   3187 C  C   . THR B 1 131 ? -15.714 16.445  14.235  1.00 23.43 ? 131 THR B C   1 
ATOM   3188 O  O   . THR B 1 131 ? -14.915 16.774  15.070  1.00 23.79 ? 131 THR B O   1 
ATOM   3189 C  CB  . THR B 1 131 ? -17.685 17.880  13.709  1.00 25.95 ? 131 THR B CB  1 
ATOM   3190 O  OG1 . THR B 1 131 ? -18.178 18.924  12.841  1.00 27.78 ? 131 THR B OG1 1 
ATOM   3191 C  CG2 . THR B 1 131 ? -17.731 18.273  15.230  1.00 26.01 ? 131 THR B CG2 1 
ATOM   3192 N  N   . ALA B 1 132 ? -16.218 15.179  14.132  1.00 20.28 ? 132 ALA B N   1 
ATOM   3193 C  CA  . ALA B 1 132 ? -15.800 14.050  14.957  1.00 19.72 ? 132 ALA B CA  1 
ATOM   3194 C  C   . ALA B 1 132 ? -14.302 13.749  14.861  1.00 20.67 ? 132 ALA B C   1 
ATOM   3195 O  O   . ALA B 1 132 ? -13.704 13.273  15.811  1.00 18.54 ? 132 ALA B O   1 
ATOM   3196 C  CB  . ALA B 1 132 ? -16.598 12.769  14.616  1.00 20.91 ? 132 ALA B CB  1 
ATOM   3197 N  N   . SER B 1 133 ? -13.755 13.995  13.676  1.00 21.70 ? 133 SER B N   1 
ATOM   3198 C  CA  . SER B 1 133 ? -12.386 13.569  13.361  1.00 20.50 ? 133 SER B CA  1 
ATOM   3199 C  C   . SER B 1 133 ? -11.294 14.249  14.238  1.00 22.64 ? 133 SER B C   1 
ATOM   3200 O  O   . SER B 1 133 ? -10.199 13.669  14.391  1.00 21.63 ? 133 SER B O   1 
ATOM   3201 C  CB  . SER B 1 133 ? -12.115 13.747  11.873  1.00 19.49 ? 133 SER B CB  1 
ATOM   3202 O  OG  . SER B 1 133 ? -11.875 15.164  11.565  1.00 22.88 ? 133 SER B OG  1 
ATOM   3203 N  N   . ASN B 1 134 ? -11.600 15.418  14.849  1.00 26.13 ? 134 ASN B N   1 
ATOM   3204 C  CA  . ASN B 1 134 ? -10.696 16.121  15.788  1.00 26.87 ? 134 ASN B CA  1 
ATOM   3205 C  C   . ASN B 1 134 ? -10.997 15.786  17.239  1.00 29.55 ? 134 ASN B C   1 
ATOM   3206 O  O   . ASN B 1 134 ? -10.449 16.404  18.150  1.00 33.76 ? 134 ASN B O   1 
ATOM   3207 C  CB  . ASN B 1 134 ? -10.812 17.662  15.693  1.00 30.81 ? 134 ASN B CB  1 
ATOM   3208 C  CG  . ASN B 1 134 ? -10.850 18.160  14.290  1.00 34.48 ? 134 ASN B CG  1 
ATOM   3209 O  OD1 . ASN B 1 134 ? -11.868 18.693  13.835  1.00 42.15 ? 134 ASN B OD1 1 
ATOM   3210 N  ND2 . ASN B 1 134 ? -9.767  17.953  13.572  1.00 32.13 ? 134 ASN B ND2 1 
ATOM   3211 N  N   . LYS B 1 135 ? -11.926 14.886  17.493  1.00 29.96 ? 135 LYS B N   1 
ATOM   3212 C  CA  . LYS B 1 135 ? -12.347 14.679  18.893  1.00 30.14 ? 135 LYS B CA  1 
ATOM   3213 C  C   . LYS B 1 135 ? -11.987 13.314  19.382  1.00 29.98 ? 135 LYS B C   1 
ATOM   3214 O  O   . LYS B 1 135 ? -11.875 12.382  18.568  1.00 22.94 ? 135 LYS B O   1 
ATOM   3215 C  CB  . LYS B 1 135 ? -13.819 15.030  19.112  1.00 34.87 ? 135 LYS B CB  1 
ATOM   3216 C  CG  . LYS B 1 135 ? -13.923 16.372  19.859  1.00 39.50 ? 135 LYS B CG  1 
ATOM   3217 C  CD  . LYS B 1 135 ? -15.113 17.211  19.443  1.00 42.54 ? 135 LYS B CD  1 
ATOM   3218 C  CE  . LYS B 1 135 ? -14.735 18.656  19.177  1.00 43.23 ? 135 LYS B CE  1 
ATOM   3219 N  NZ  . LYS B 1 135 ? -14.147 18.684  17.800  1.00 46.31 ? 135 LYS B NZ  1 
ATOM   3220 N  N   . SER B 1 136 ? -11.813 13.204  20.708  1.00 30.06 ? 136 SER B N   1 
ATOM   3221 C  CA  . SER B 1 136 ? -11.378 11.979  21.346  1.00 33.17 ? 136 SER B CA  1 
ATOM   3222 C  C   . SER B 1 136 ? -12.385 10.871  20.967  1.00 29.91 ? 136 SER B C   1 
ATOM   3223 O  O   . SER B 1 136 ? -13.583 11.084  21.069  1.00 31.99 ? 136 SER B O   1 
ATOM   3224 C  CB  . SER B 1 136 ? -11.289 12.191  22.882  1.00 38.02 ? 136 SER B CB  1 
ATOM   3225 O  OG  . SER B 1 136 ? -11.846 11.096  23.609  1.00 37.07 ? 136 SER B OG  1 
ATOM   3226 N  N   . GLU B 1 137 ? -11.882 9.734   20.487  1.00 27.55 ? 137 GLU B N   1 
ATOM   3227 C  CA  . GLU B 1 137 ? -12.710 8.609   20.009  1.00 28.45 ? 137 GLU B CA  1 
ATOM   3228 C  C   . GLU B 1 137 ? -13.859 9.009   19.066  1.00 25.43 ? 137 GLU B C   1 
ATOM   3229 O  O   . GLU B 1 137 ? -14.915 8.333   19.032  1.00 23.82 ? 137 GLU B O   1 
ATOM   3230 C  CB  . GLU B 1 137 ? -13.293 7.784   21.154  1.00 29.10 ? 137 GLU B CB  1 
ATOM   3231 C  CG  . GLU B 1 137 ? -12.266 7.088   22.038  1.00 36.13 ? 137 GLU B CG  1 
ATOM   3232 C  CD  . GLU B 1 137 ? -12.822 6.644   23.402  1.00 43.13 ? 137 GLU B CD  1 
ATOM   3233 O  OE1 . GLU B 1 137 ? -14.056 6.479   23.568  1.00 36.88 ? 137 GLU B OE1 1 
ATOM   3234 O  OE2 . GLU B 1 137 ? -12.007 6.449   24.336  1.00 43.03 ? 137 GLU B OE2 1 
ATOM   3235 N  N   . GLY B 1 138 ? -13.653 10.092  18.320  1.00 20.28 ? 138 GLY B N   1 
ATOM   3236 C  CA  . GLY B 1 138 ? -14.630 10.582  17.399  1.00 19.23 ? 138 GLY B CA  1 
ATOM   3237 C  C   . GLY B 1 138 ? -14.921 9.669   16.202  1.00 14.62 ? 138 GLY B C   1 
ATOM   3238 O  O   . GLY B 1 138 ? -16.020 9.703   15.644  1.00 15.37 ? 138 GLY B O   1 
ATOM   3239 N  N   . LEU B 1 139 ? -13.926 8.892   15.762  1.00 13.65 ? 139 LEU B N   1 
ATOM   3240 C  CA  . LEU B 1 139 ? -14.108 8.010   14.559  1.00 12.33 ? 139 LEU B CA  1 
ATOM   3241 C  C   . LEU B 1 139 ? -13.990 6.510   14.958  1.00 10.41 ? 139 LEU B C   1 
ATOM   3242 O  O   . LEU B 1 139 ? -13.293 6.168   15.903  1.00 11.32 ? 139 LEU B O   1 
ATOM   3243 C  CB  . LEU B 1 139 ? -13.043 8.302   13.473  1.00 13.41 ? 139 LEU B CB  1 
ATOM   3244 C  CG  . LEU B 1 139 ? -13.084 9.779   12.975  1.00 13.85 ? 139 LEU B CG  1 
ATOM   3245 C  CD1 . LEU B 1 139 ? -12.002 9.961   11.948  1.00 13.86 ? 139 LEU B CD1 1 
ATOM   3246 C  CD2 . LEU B 1 139 ? -14.425 10.082  12.326  1.00 14.96 ? 139 LEU B CD2 1 
ATOM   3247 N  N   . ALA B 1 140 ? -14.688 5.626   14.286  1.00 10.77 ? 140 ALA B N   1 
ATOM   3248 C  CA  . ALA B 1 140 ? -14.449 4.164   14.472  1.00 9.25  ? 140 ALA B CA  1 
ATOM   3249 C  C   . ALA B 1 140 ? -14.347 3.661   13.042  1.00 9.53  ? 140 ALA B C   1 
ATOM   3250 O  O   . ALA B 1 140 ? -15.245 3.795   12.191  1.00 9.69  ? 140 ALA B O   1 
ATOM   3251 C  CB  . ALA B 1 140 ? -15.643 3.534   15.190  1.00 9.50  ? 140 ALA B CB  1 
ATOM   3252 N  N   . VAL B 1 141 ? -13.257 2.928   12.766  1.00 9.76  ? 141 VAL B N   1 
ATOM   3253 C  CA  . VAL B 1 141 ? -13.107 2.396   11.396  1.00 8.05  ? 141 VAL B CA  1 
ATOM   3254 C  C   . VAL B 1 141 ? -13.092 0.858   11.494  1.00 8.92  ? 141 VAL B C   1 
ATOM   3255 O  O   . VAL B 1 141 ? -12.391 0.365   12.431  1.00 9.24  ? 141 VAL B O   1 
ATOM   3256 C  CB  . VAL B 1 141 ? -11.743 2.864   10.772  1.00 7.76  ? 141 VAL B CB  1 
ATOM   3257 C  CG1 . VAL B 1 141 ? -11.593 2.336   9.347   1.00 8.73  ? 141 VAL B CG1 1 
ATOM   3258 C  CG2 . VAL B 1 141 ? -11.728 4.395   10.680  1.00 9.45  ? 141 VAL B CG2 1 
ATOM   3259 N  N   . LEU B 1 142 ? -13.873 0.194   10.659  1.00 8.23  ? 142 LEU B N   1 
ATOM   3260 C  CA  . LEU B 1 142 ? -13.810 -1.297  10.588  1.00 8.61  ? 142 LEU B CA  1 
ATOM   3261 C  C   . LEU B 1 142 ? -12.859 -1.619  9.463   1.00 9.11  ? 142 LEU B C   1 
ATOM   3262 O  O   . LEU B 1 142 ? -12.981 -1.128  8.375   1.00 9.89  ? 142 LEU B O   1 
ATOM   3263 C  CB  . LEU B 1 142 ? -15.205 -1.805  10.252  1.00 9.79  ? 142 LEU B CB  1 
ATOM   3264 C  CG  . LEU B 1 142 ? -16.337 -1.451  11.211  1.00 10.95 ? 142 LEU B CG  1 
ATOM   3265 C  CD1 . LEU B 1 142 ? -17.585 -2.207  10.670  1.00 13.84 ? 142 LEU B CD1 1 
ATOM   3266 C  CD2 . LEU B 1 142 ? -16.042 -1.837  12.628  1.00 11.38 ? 142 LEU B CD2 1 
ATOM   3267 N  N   . ALA B 1 143 ? -11.950 -2.597  9.690   1.00 9.02  ? 143 ALA B N   1 
ATOM   3268 C  CA  . ALA B 1 143 ? -11.044 -2.977  8.650   1.00 8.35  ? 143 ALA B CA  1 
ATOM   3269 C  C   . ALA B 1 143 ? -11.229 -4.467  8.322   1.00 8.44  ? 143 ALA B C   1 
ATOM   3270 O  O   . ALA B 1 143 ? -11.311 -5.305  9.227   1.00 10.54 ? 143 ALA B O   1 
ATOM   3271 C  CB  . ALA B 1 143 ? -9.614  -2.719  9.135   1.00 10.16 ? 143 ALA B CB  1 
ATOM   3272 N  N   . VAL B 1 144 ? -11.327 -4.684  6.993   1.00 7.78  ? 144 VAL B N   1 
ATOM   3273 C  CA  . VAL B 1 144 ? -11.390 -6.080  6.481   1.00 8.86  ? 144 VAL B CA  1 
ATOM   3274 C  C   . VAL B 1 144 ? -10.125 -6.369  5.647   1.00 8.10  ? 144 VAL B C   1 
ATOM   3275 O  O   . VAL B 1 144 ? -9.829  -5.649  4.689   1.00 8.09  ? 144 VAL B O   1 
ATOM   3276 C  CB  . VAL B 1 144 ? -12.636 -6.308  5.596   1.00 8.84  ? 144 VAL B CB  1 
ATOM   3277 C  CG1 . VAL B 1 144 ? -12.709 -7.759  5.115   1.00 9.35  ? 144 VAL B CG1 1 
ATOM   3278 C  CG2 . VAL B 1 144 ? -13.957 -6.076  6.354   1.00 10.17 ? 144 VAL B CG2 1 
ATOM   3279 N  N   . LEU B 1 145 ? -9.375  -7.414  6.030   1.00 8.21  ? 145 LEU B N   1 
ATOM   3280 C  CA  . LEU B 1 145 ? -8.212  -7.880  5.308   1.00 8.72  ? 145 LEU B CA  1 
ATOM   3281 C  C   . LEU B 1 145 ? -8.724  -8.648  4.106   1.00 8.20  ? 145 LEU B C   1 
ATOM   3282 O  O   . LEU B 1 145 ? -9.678  -9.468  4.203   1.00 8.70  ? 145 LEU B O   1 
ATOM   3283 C  CB  . LEU B 1 145 ? -7.296  -8.743  6.239   1.00 8.99  ? 145 LEU B CB  1 
ATOM   3284 C  CG  . LEU B 1 145 ? -6.802  -7.960  7.458   1.00 10.90 ? 145 LEU B CG  1 
ATOM   3285 C  CD1 . LEU B 1 145 ? -6.218  -8.910  8.501   1.00 13.17 ? 145 LEU B CD1 1 
ATOM   3286 C  CD2 . LEU B 1 145 ? -5.726  -6.858  7.116   1.00 11.76 ? 145 LEU B CD2 1 
ATOM   3287 N  N   . ILE B 1 146 ? -8.053  -8.422  2.972   1.00 8.70  ? 146 ILE B N   1 
ATOM   3288 C  CA  . ILE B 1 146 ? -8.433  -8.989  1.712   1.00 9.98  ? 146 ILE B CA  1 
ATOM   3289 C  C   . ILE B 1 146 ? -7.306  -9.828  1.130   1.00 10.74 ? 146 ILE B C   1 
ATOM   3290 O  O   . ILE B 1 146 ? -6.204  -9.349  0.984   1.00 10.93 ? 146 ILE B O   1 
ATOM   3291 C  CB  . ILE B 1 146 ? -8.872  -7.925  0.701   1.00 9.06  ? 146 ILE B CB  1 
ATOM   3292 C  CG1 . ILE B 1 146 ? -10.110 -7.148  1.197   1.00 10.63 ? 146 ILE B CG1 1 
ATOM   3293 C  CG2 . ILE B 1 146 ? -9.112  -8.635  -0.672  1.00 9.67  ? 146 ILE B CG2 1 
ATOM   3294 C  CD1 . ILE B 1 146 ? -10.327 -5.862  0.375   1.00 11.13 ? 146 ILE B CD1 1 
ATOM   3295 N  N   . GLU B 1 147 ? -7.570  -11.088 0.882   1.00 11.30 ? 147 GLU B N   1 
ATOM   3296 C  CA  . GLU B 1 147 ? -6.528  -11.982 0.309   1.00 12.47 ? 147 GLU B CA  1 
ATOM   3297 C  C   . GLU B 1 147 ? -6.969  -12.369 -1.100  1.00 10.56 ? 147 GLU B C   1 
ATOM   3298 O  O   . GLU B 1 147 ? -8.193  -12.431 -1.451  1.00 9.02  ? 147 GLU B O   1 
ATOM   3299 C  CB  . GLU B 1 147 ? -6.386  -13.227 1.211   1.00 16.00 ? 147 GLU B CB  1 
ATOM   3300 C  CG  . GLU B 1 147 ? -7.532  -14.179 1.303   1.00 23.44 ? 147 GLU B CG  1 
ATOM   3301 C  CD  . GLU B 1 147 ? -7.167  -15.404 2.186   1.00 28.48 ? 147 GLU B CD  1 
ATOM   3302 O  OE1 . GLU B 1 147 ? -6.043  -15.383 2.750   1.00 29.10 ? 147 GLU B OE1 1 
ATOM   3303 O  OE2 . GLU B 1 147 ? -8.032  -16.329 2.330   1.00 31.17 ? 147 GLU B OE2 1 
ATOM   3304 N  N   . MET B 1 148 ? -5.991  -12.689 -1.962  1.00 9.48  ? 148 MET B N   1 
ATOM   3305 C  CA  . MET B 1 148 ? -6.232  -13.215 -3.300  1.00 10.24 ? 148 MET B CA  1 
ATOM   3306 C  C   . MET B 1 148 ? -6.820  -14.611 -3.183  1.00 10.34 ? 148 MET B C   1 
ATOM   3307 O  O   . MET B 1 148 ? -6.245  -15.521 -2.531  1.00 12.52 ? 148 MET B O   1 
ATOM   3308 C  CB  . MET B 1 148 ? -4.906  -13.401 -4.093  1.00 10.19 ? 148 MET B CB  1 
ATOM   3309 C  CG  . MET B 1 148 ? -5.191  -13.498 -5.593  1.00 11.08 ? 148 MET B CG  1 
ATOM   3310 S  SD  . MET B 1 148 ? -3.654  -13.687 -6.517  1.00 14.03 ? 148 MET B SD  1 
ATOM   3311 C  CE  . MET B 1 148 ? -3.142  -11.962 -6.463  1.00 10.57 ? 148 MET B CE  1 
ATOM   3312 N  N   . GLY B 1 149 ? -8.011  -14.732 -3.792  1.00 9.85  ? 149 GLY B N   1 
ATOM   3313 C  CA  . GLY B 1 149 ? -8.739  -16.025 -3.732  1.00 9.55  ? 149 GLY B CA  1 
ATOM   3314 C  C   . GLY B 1 149 ? -9.819  -16.109 -4.769  1.00 8.83  ? 149 GLY B C   1 
ATOM   3315 O  O   . GLY B 1 149 ? -9.640  -15.810 -5.974  1.00 10.28 ? 149 GLY B O   1 
ATOM   3316 N  N   . SER B 1 150 ? -10.996 -16.567 -4.308  1.00 10.48 ? 150 SER B N   1 
ATOM   3317 C  CA  . SER B 1 150 ? -12.165 -16.613 -5.186  1.00 11.96 ? 150 SER B CA  1 
ATOM   3318 C  C   . SER B 1 150 ? -12.733 -15.242 -5.551  1.00 11.30 ? 150 SER B C   1 
ATOM   3319 O  O   . SER B 1 150 ? -12.685 -14.306 -4.731  1.00 13.21 ? 150 SER B O   1 
ATOM   3320 C  CB  . SER B 1 150 ? -13.273 -17.335 -4.486  1.00 10.78 ? 150 SER B CB  1 
ATOM   3321 O  OG  . SER B 1 150 ? -12.907 -18.729 -4.396  1.00 12.73 ? 150 SER B OG  1 
ATOM   3322 N  N   . PHE B 1 151 ? -13.284 -15.250 -6.776  1.00 11.67 ? 151 PHE B N   1 
ATOM   3323 C  CA  . PHE B 1 151 ? -14.079 -14.083 -7.237  1.00 11.36 ? 151 PHE B CA  1 
ATOM   3324 C  C   . PHE B 1 151 ? -15.164 -13.790 -6.178  1.00 12.31 ? 151 PHE B C   1 
ATOM   3325 O  O   . PHE B 1 151 ? -15.907 -14.667 -5.679  1.00 12.60 ? 151 PHE B O   1 
ATOM   3326 C  CB  . PHE B 1 151 ? -14.770 -14.359 -8.605  1.00 11.32 ? 151 PHE B CB  1 
ATOM   3327 C  CG  . PHE B 1 151 ? -15.612 -13.223 -9.084  1.00 10.79 ? 151 PHE B CG  1 
ATOM   3328 C  CD1 . PHE B 1 151 ? -15.010 -12.133 -9.672  1.00 12.99 ? 151 PHE B CD1 1 
ATOM   3329 C  CD2 . PHE B 1 151 ? -16.992 -13.231 -8.926  1.00 11.82 ? 151 PHE B CD2 1 
ATOM   3330 C  CE1 . PHE B 1 151 ? -15.759 -11.065 -10.107 1.00 11.51 ? 151 PHE B CE1 1 
ATOM   3331 C  CE2 . PHE B 1 151 ? -17.754 -12.165 -9.357  1.00 12.90 ? 151 PHE B CE2 1 
ATOM   3332 C  CZ  . PHE B 1 151 ? -17.134 -11.078 -9.951  1.00 12.95 ? 151 PHE B CZ  1 
ATOM   3333 N  N   . ASN B 1 152 ? -15.311 -12.490 -5.875  1.00 10.16 ? 152 ASN B N   1 
ATOM   3334 C  CA  . ASN B 1 152 ? -16.267 -12.050 -4.889  1.00 10.11 ? 152 ASN B CA  1 
ATOM   3335 C  C   . ASN B 1 152 ? -17.328 -11.153 -5.541  1.00 10.02 ? 152 ASN B C   1 
ATOM   3336 O  O   . ASN B 1 152 ? -17.082 -9.964  -5.828  1.00 10.11 ? 152 ASN B O   1 
ATOM   3337 C  CB  . ASN B 1 152 ? -15.488 -11.272 -3.735  1.00 10.54 ? 152 ASN B CB  1 
ATOM   3338 C  CG  . ASN B 1 152 ? -16.329 -11.074 -2.539  1.00 11.28 ? 152 ASN B CG  1 
ATOM   3339 O  OD1 . ASN B 1 152 ? -17.476 -10.644 -2.663  1.00 10.57 ? 152 ASN B OD1 1 
ATOM   3340 N  ND2 . ASN B 1 152 ? -15.777 -11.339 -1.335  1.00 10.12 ? 152 ASN B ND2 1 
ATOM   3341 N  N   . PRO B 1 153 ? -18.534 -11.649 -5.719  1.00 10.21 ? 153 PRO B N   1 
ATOM   3342 C  CA  . PRO B 1 153 ? -19.597 -10.865 -6.375  1.00 12.21 ? 153 PRO B CA  1 
ATOM   3343 C  C   . PRO B 1 153 ? -19.956 -9.612  -5.589  1.00 11.92 ? 153 PRO B C   1 
ATOM   3344 O  O   . PRO B 1 153 ? -20.322 -8.583  -6.210  1.00 11.71 ? 153 PRO B O   1 
ATOM   3345 C  CB  . PRO B 1 153 ? -20.739 -11.846 -6.454  1.00 13.55 ? 153 PRO B CB  1 
ATOM   3346 C  CG  . PRO B 1 153 ? -20.155 -13.225 -6.285  1.00 17.17 ? 153 PRO B CG  1 
ATOM   3347 C  CD  . PRO B 1 153 ? -18.933 -13.054 -5.426  1.00 13.10 ? 153 PRO B CD  1 
ATOM   3348 N  N   . SER B 1 154 ? -19.876 -9.676  -4.259  1.00 11.95 ? 154 SER B N   1 
ATOM   3349 C  CA  . SER B 1 154 ? -20.248 -8.456  -3.489  1.00 11.18 ? 154 SER B CA  1 
ATOM   3350 C  C   . SER B 1 154 ? -19.259 -7.341  -3.664  1.00 11.22 ? 154 SER B C   1 
ATOM   3351 O  O   . SER B 1 154 ? -19.655 -6.197  -3.861  1.00 10.30 ? 154 SER B O   1 
ATOM   3352 C  CB  . SER B 1 154 ? -20.398 -8.754  -1.979  1.00 13.33 ? 154 SER B CB  1 
ATOM   3353 O  OG  . SER B 1 154 ? -21.336 -9.853  -1.853  1.00 17.78 ? 154 SER B OG  1 
ATOM   3354 N  N   . TYR B 1 155 ? -17.955 -7.639  -3.604  1.00 9.29  ? 155 TYR B N   1 
ATOM   3355 C  CA  . TYR B 1 155 ? -16.969 -6.576  -3.847  1.00 8.66  ? 155 TYR B CA  1 
ATOM   3356 C  C   . TYR B 1 155 ? -17.107 -6.087  -5.288  1.00 8.83  ? 155 TYR B C   1 
ATOM   3357 O  O   . TYR B 1 155 ? -16.784 -4.899  -5.589  1.00 9.45  ? 155 TYR B O   1 
ATOM   3358 C  CB  . TYR B 1 155 ? -15.514 -7.034  -3.578  1.00 8.88  ? 155 TYR B CB  1 
ATOM   3359 C  CG  . TYR B 1 155 ? -15.177 -6.955  -2.068  1.00 9.19  ? 155 TYR B CG  1 
ATOM   3360 C  CD1 . TYR B 1 155 ? -14.358 -5.885  -1.572  1.00 9.17  ? 155 TYR B CD1 1 
ATOM   3361 C  CD2 . TYR B 1 155 ? -15.576 -7.898  -1.152  1.00 9.65  ? 155 TYR B CD2 1 
ATOM   3362 C  CE1 . TYR B 1 155 ? -14.090 -5.745  -0.216  1.00 10.22 ? 155 TYR B CE1 1 
ATOM   3363 C  CE2 . TYR B 1 155 ? -15.327 -7.762  0.202   1.00 9.83  ? 155 TYR B CE2 1 
ATOM   3364 C  CZ  . TYR B 1 155 ? -14.575 -6.663  0.674   1.00 10.74 ? 155 TYR B CZ  1 
ATOM   3365 O  OH  . TYR B 1 155 ? -14.246 -6.555  2.001   1.00 10.61 ? 155 TYR B OH  1 
ATOM   3366 N  N   . ASP B 1 156 ? -17.480 -6.938  -6.200  1.00 9.26  ? 156 ASP B N   1 
ATOM   3367 C  CA  . ASP B 1 156 ? -17.556 -6.535  -7.555  1.00 9.33  ? 156 ASP B CA  1 
ATOM   3368 C  C   . ASP B 1 156 ? -18.698 -5.454  -7.767  1.00 10.25 ? 156 ASP B C   1 
ATOM   3369 O  O   . ASP B 1 156 ? -18.688 -4.767  -8.803  1.00 11.55 ? 156 ASP B O   1 
ATOM   3370 C  CB  . ASP B 1 156 ? -17.750 -7.704  -8.542  1.00 12.69 ? 156 ASP B CB  1 
ATOM   3371 C  CG  . ASP B 1 156 ? -16.868 -7.513  -9.723  1.00 12.34 ? 156 ASP B CG  1 
ATOM   3372 O  OD1 . ASP B 1 156 ? -15.646 -7.295  -9.516  1.00 12.28 ? 156 ASP B OD1 1 
ATOM   3373 O  OD2 . ASP B 1 156 ? -17.370 -7.483  -10.886 1.00 18.76 ? 156 ASP B OD2 1 
ATOM   3374 N  N   . LYS B 1 157 ? -19.632 -5.355  -6.825  1.00 11.64 ? 157 LYS B N   1 
ATOM   3375 C  CA  . LYS B 1 157 ? -20.690 -4.324  -6.906  1.00 11.67 ? 157 LYS B CA  1 
ATOM   3376 C  C   . LYS B 1 157 ? -19.997 -2.979  -6.834  1.00 13.36 ? 157 LYS B C   1 
ATOM   3377 O  O   . LYS B 1 157 ? -20.530 -2.007  -7.388  1.00 14.72 ? 157 LYS B O   1 
ATOM   3378 C  CB  . LYS B 1 157 ? -21.757 -4.441  -5.841  1.00 11.95 ? 157 LYS B CB  1 
ATOM   3379 C  CG  . LYS B 1 157 ? -22.614 -5.715  -6.092  1.00 13.64 ? 157 LYS B CG  1 
ATOM   3380 C  CD  . LYS B 1 157 ? -23.519 -6.021  -4.889  1.00 17.86 ? 157 LYS B CD  1 
ATOM   3381 C  CE  . LYS B 1 157 ? -24.205 -7.396  -5.098  1.00 21.11 ? 157 LYS B CE  1 
ATOM   3382 N  NZ  . LYS B 1 157 ? -25.028 -7.844  -3.930  1.00 24.75 ? 157 LYS B NZ  1 
ATOM   3383 N  N   . ILE B 1 158 ? -18.832 -2.934  -6.215  1.00 11.52 ? 158 ILE B N   1 
ATOM   3384 C  CA  . ILE B 1 158 ? -18.056 -1.643  -6.227  1.00 12.45 ? 158 ILE B CA  1 
ATOM   3385 C  C   . ILE B 1 158 ? -17.118 -1.645  -7.404  1.00 13.27 ? 158 ILE B C   1 
ATOM   3386 O  O   . ILE B 1 158 ? -17.034 -0.680  -8.104  1.00 13.21 ? 158 ILE B O   1 
ATOM   3387 C  CB  . ILE B 1 158 ? -17.267 -1.459  -4.935  1.00 12.53 ? 158 ILE B CB  1 
ATOM   3388 C  CG1 . ILE B 1 158 ? -18.212 -1.280  -3.738  1.00 14.27 ? 158 ILE B CG1 1 
ATOM   3389 C  CG2 . ILE B 1 158 ? -16.303 -0.249  -4.992  1.00 13.61 ? 158 ILE B CG2 1 
ATOM   3390 C  CD1 . ILE B 1 158 ? -17.551 -1.679  -2.432  1.00 16.18 ? 158 ILE B CD1 1 
ATOM   3391 N  N   . PHE B 1 159 ? -16.387 -2.751  -7.630  1.00 11.44 ? 159 PHE B N   1 
ATOM   3392 C  CA  . PHE B 1 159 ? -15.305 -2.726  -8.615  1.00 11.62 ? 159 PHE B CA  1 
ATOM   3393 C  C   . PHE B 1 159 ? -15.769 -2.574  -10.025 1.00 12.89 ? 159 PHE B C   1 
ATOM   3394 O  O   . PHE B 1 159 ? -15.000 -2.068  -10.905 1.00 16.17 ? 159 PHE B O   1 
ATOM   3395 C  CB  . PHE B 1 159 ? -14.527 -4.045  -8.555  1.00 11.18 ? 159 PHE B CB  1 
ATOM   3396 C  CG  . PHE B 1 159 ? -13.844 -4.266  -7.211  1.00 12.12 ? 159 PHE B CG  1 
ATOM   3397 C  CD1 . PHE B 1 159 ? -13.424 -3.225  -6.388  1.00 13.64 ? 159 PHE B CD1 1 
ATOM   3398 C  CD2 . PHE B 1 159 ? -13.430 -5.577  -6.859  1.00 13.42 ? 159 PHE B CD2 1 
ATOM   3399 C  CE1 . PHE B 1 159 ? -12.771 -3.446  -5.165  1.00 13.50 ? 159 PHE B CE1 1 
ATOM   3400 C  CE2 . PHE B 1 159 ? -12.729 -5.798  -5.674  1.00 14.18 ? 159 PHE B CE2 1 
ATOM   3401 C  CZ  . PHE B 1 159 ? -12.367 -4.731  -4.821  1.00 15.02 ? 159 PHE B CZ  1 
ATOM   3402 N  N   . SER B 1 160 ? -17.004 -2.986  -10.272 1.00 14.41 ? 160 SER B N   1 
ATOM   3403 C  CA  . SER B 1 160 ? -17.577 -2.831  -11.621 1.00 15.97 ? 160 SER B CA  1 
ATOM   3404 C  C   . SER B 1 160 ? -17.761 -1.374  -12.012 1.00 17.70 ? 160 SER B C   1 
ATOM   3405 O  O   . SER B 1 160 ? -17.905 -1.144  -13.163 1.00 19.04 ? 160 SER B O   1 
ATOM   3406 C  CB  . SER B 1 160 ? -18.912 -3.620  -11.745 1.00 17.88 ? 160 SER B CB  1 
ATOM   3407 O  OG  . SER B 1 160 ? -19.879 -3.072  -10.912 1.00 20.61 ? 160 SER B OG  1 
ATOM   3408 N  N   . HIS B 1 161 ? -17.601 -0.419  -11.076 1.00 13.41 ? 161 HIS B N   1 
ATOM   3409 C  CA  . HIS B 1 161 ? -17.805 1.050   -11.349 1.00 15.26 ? 161 HIS B CA  1 
ATOM   3410 C  C   . HIS B 1 161 ? -16.527 1.829   -11.421 1.00 16.33 ? 161 HIS B C   1 
ATOM   3411 O  O   . HIS B 1 161 ? -16.562 3.068   -11.670 1.00 18.96 ? 161 HIS B O   1 
ATOM   3412 C  CB  . HIS B 1 161 ? -18.729 1.722   -10.340 1.00 14.97 ? 161 HIS B CB  1 
ATOM   3413 C  CG  . HIS B 1 161 ? -20.134 1.176   -10.367 1.00 16.04 ? 161 HIS B CG  1 
ATOM   3414 N  ND1 . HIS B 1 161 ? -21.093 1.685   -11.189 1.00 16.99 ? 161 HIS B ND1 1 
ATOM   3415 C  CD2 . HIS B 1 161 ? -20.709 0.053   -9.727  1.00 16.46 ? 161 HIS B CD2 1 
ATOM   3416 C  CE1 . HIS B 1 161 ? -22.260 0.983   -11.017 1.00 17.50 ? 161 HIS B CE1 1 
ATOM   3417 N  NE2 . HIS B 1 161 ? -22.010 -0.035  -10.150 1.00 15.77 ? 161 HIS B NE2 1 
ATOM   3418 N  N   . LEU B 1 162 ? -15.402 1.158   -11.179 1.00 19.08 ? 162 LEU B N   1 
ATOM   3419 C  CA  . LEU B 1 162 ? -14.130 1.917   -11.172 1.00 22.67 ? 162 LEU B CA  1 
ATOM   3420 C  C   . LEU B 1 162 ? -13.696 2.553   -12.454 1.00 24.57 ? 162 LEU B C   1 
ATOM   3421 O  O   . LEU B 1 162 ? -13.073 3.609   -12.416 1.00 25.07 ? 162 LEU B O   1 
ATOM   3422 C  CB  . LEU B 1 162 ? -12.991 1.108   -10.584 1.00 27.10 ? 162 LEU B CB  1 
ATOM   3423 C  CG  . LEU B 1 162 ? -13.155 0.536   -9.167  1.00 24.30 ? 162 LEU B CG  1 
ATOM   3424 C  CD1 . LEU B 1 162 ? -11.909 -0.242  -8.793  1.00 27.11 ? 162 LEU B CD1 1 
ATOM   3425 C  CD2 . LEU B 1 162 ? -13.469 1.580   -8.100  1.00 25.93 ? 162 LEU B CD2 1 
ATOM   3426 N  N   A GLN B 1 163 ? -14.022 1.944   -13.601 0.50 25.37 ? 163 GLN B N   1 
ATOM   3427 N  N   B GLN B 1 163 ? -14.024 1.904   -13.571 0.50 25.69 ? 163 GLN B N   1 
ATOM   3428 C  CA  A GLN B 1 163 ? -13.650 2.507   -14.921 0.50 23.85 ? 163 GLN B CA  1 
ATOM   3429 C  CA  B GLN B 1 163 ? -13.753 2.414   -14.911 0.50 24.68 ? 163 GLN B CA  1 
ATOM   3430 C  C   A GLN B 1 163 ? -14.458 3.776   -15.217 0.50 24.57 ? 163 GLN B C   1 
ATOM   3431 C  C   B GLN B 1 163 ? -14.281 3.846   -15.054 0.50 25.14 ? 163 GLN B C   1 
ATOM   3432 O  O   A GLN B 1 163 ? -14.352 4.403   -16.309 0.50 24.45 ? 163 GLN B O   1 
ATOM   3433 O  O   B GLN B 1 163 ? -13.792 4.659   -15.862 0.50 29.83 ? 163 GLN B O   1 
ATOM   3434 C  CB  A GLN B 1 163 ? -13.797 1.455   -16.046 0.50 24.33 ? 163 GLN B CB  1 
ATOM   3435 C  CB  B GLN B 1 163 ? -14.371 1.458   -15.957 0.50 24.21 ? 163 GLN B CB  1 
ATOM   3436 C  CG  A GLN B 1 163 ? -12.915 0.202   -15.876 0.50 23.42 ? 163 GLN B CG  1 
ATOM   3437 C  CG  B GLN B 1 163 ? -15.620 0.688   -15.489 0.50 25.80 ? 163 GLN B CG  1 
ATOM   3438 C  CD  A GLN B 1 163 ? -11.440 0.439   -16.176 0.50 23.10 ? 163 GLN B CD  1 
ATOM   3439 C  CD  B GLN B 1 163 ? -15.342 -0.611  -14.727 0.50 21.10 ? 163 GLN B CD  1 
ATOM   3440 O  OE1 A GLN B 1 163 ? -11.068 1.485   -16.669 0.50 19.20 ? 163 GLN B OE1 1 
ATOM   3441 O  OE1 B GLN B 1 163 ? -14.750 -0.623  -13.632 0.50 19.03 ? 163 GLN B OE1 1 
ATOM   3442 N  NE2 A GLN B 1 163 ? -10.594 -0.557  -15.898 0.50 20.73 ? 163 GLN B NE2 1 
ATOM   3443 N  NE2 B GLN B 1 163 ? -15.778 -1.729  -15.308 0.50 25.11 ? 163 GLN B NE2 1 
ATOM   3444 N  N   . HIS B 1 164 ? -15.285 4.145   -14.245 1.00 22.47 ? 164 HIS B N   1 
ATOM   3445 C  CA  . HIS B 1 164 ? -16.063 5.341   -14.344 1.00 19.36 ? 164 HIS B CA  1 
ATOM   3446 C  C   . HIS B 1 164 ? -15.671 6.430   -13.371 1.00 17.21 ? 164 HIS B C   1 
ATOM   3447 O  O   . HIS B 1 164 ? -16.209 7.563   -13.385 1.00 16.65 ? 164 HIS B O   1 
ATOM   3448 C  CB  . HIS B 1 164 ? -17.508 4.873   -14.412 1.00 27.95 ? 164 HIS B CB  1 
ATOM   3449 C  CG  . HIS B 1 164 ? -17.659 3.654   -15.335 1.00 28.62 ? 164 HIS B CG  1 
ATOM   3450 N  ND1 . HIS B 1 164 ? -17.289 3.679   -16.657 1.00 33.85 ? 164 HIS B ND1 1 
ATOM   3451 C  CD2 . HIS B 1 164 ? -18.131 2.328   -15.085 1.00 35.83 ? 164 HIS B CD2 1 
ATOM   3452 C  CE1 . HIS B 1 164 ? -17.510 2.450   -17.222 1.00 34.14 ? 164 HIS B CE1 1 
ATOM   3453 N  NE2 . HIS B 1 164 ? -18.023 1.625   -16.261 1.00 33.25 ? 164 HIS B NE2 1 
ATOM   3454 N  N   . VAL B 1 165 ? -14.675 6.156   -12.525 1.00 14.29 ? 165 VAL B N   1 
ATOM   3455 C  CA  . VAL B 1 165 ? -14.134 7.182   -11.632 1.00 13.65 ? 165 VAL B CA  1 
ATOM   3456 C  C   . VAL B 1 165 ? -12.586 7.092   -11.751 1.00 12.84 ? 165 VAL B C   1 
ATOM   3457 O  O   . VAL B 1 165 ? -11.861 7.216   -10.793 1.00 14.00 ? 165 VAL B O   1 
ATOM   3458 C  CB  . VAL B 1 165 ? -14.611 7.067   -10.175 1.00 14.58 ? 165 VAL B CB  1 
ATOM   3459 C  CG1 . VAL B 1 165 ? -16.080 7.514   -10.094 1.00 15.36 ? 165 VAL B CG1 1 
ATOM   3460 C  CG2 . VAL B 1 165 ? -14.359 5.682   -9.612  1.00 15.37 ? 165 VAL B CG2 1 
ATOM   3461 N  N   A LYS B 1 166 ? -12.164 6.923   -12.988 0.50 12.37 ? 166 LYS B N   1 
ATOM   3462 N  N   B LYS B 1 166 ? -12.097 6.838   -12.958 0.50 12.77 ? 166 LYS B N   1 
ATOM   3463 C  CA  A LYS B 1 166 ? -10.761 6.646   -13.304 0.50 11.11 ? 166 LYS B CA  1 
ATOM   3464 C  CA  B LYS B 1 166 ? -10.628 6.611   -13.151 0.50 11.32 ? 166 LYS B CA  1 
ATOM   3465 C  C   A LYS B 1 166 ? -9.827  7.778   -12.975 0.50 10.92 ? 166 LYS B C   1 
ATOM   3466 C  C   B LYS B 1 166 ? -9.808  7.792   -12.652 0.50 11.24 ? 166 LYS B C   1 
ATOM   3467 O  O   A LYS B 1 166 ? -8.663  7.537   -12.814 0.50 9.47  ? 166 LYS B O   1 
ATOM   3468 O  O   B LYS B 1 166 ? -8.711  7.617   -12.071 0.50 9.38  ? 166 LYS B O   1 
ATOM   3469 C  CB  A LYS B 1 166 ? -10.612 6.321   -14.788 0.50 12.00 ? 166 LYS B CB  1 
ATOM   3470 C  CB  B LYS B 1 166 ? -10.246 6.388   -14.629 0.50 12.79 ? 166 LYS B CB  1 
ATOM   3471 C  CG  A LYS B 1 166 ? -11.204 4.975   -15.170 0.50 13.32 ? 166 LYS B CG  1 
ATOM   3472 C  CG  B LYS B 1 166 ? -10.706 5.110   -15.276 0.50 14.31 ? 166 LYS B CG  1 
ATOM   3473 C  CD  A LYS B 1 166 ? -10.791 4.474   -16.550 0.50 14.29 ? 166 LYS B CD  1 
ATOM   3474 C  CD  B LYS B 1 166 ? -10.601 5.282   -16.781 0.50 16.68 ? 166 LYS B CD  1 
ATOM   3475 C  CE  A LYS B 1 166 ? -9.312  4.645   -16.807 0.50 15.40 ? 166 LYS B CE  1 
ATOM   3476 C  CE  B LYS B 1 166 ? -9.315  4.713   -17.396 0.50 17.34 ? 166 LYS B CE  1 
ATOM   3477 N  NZ  A LYS B 1 166 ? -8.504  3.514   -16.297 0.50 15.31 ? 166 LYS B NZ  1 
ATOM   3478 N  NZ  B LYS B 1 166 ? -8.045  5.353   -16.898 0.50 17.36 ? 166 LYS B NZ  1 
ATOM   3479 N  N   . TYR B 1 167 ? -10.336 9.009   -12.848 1.00 10.65 ? 167 TYR B N   1 
ATOM   3480 C  CA  . TYR B 1 167 ? -9.492  10.149  -12.602 1.00 11.96 ? 167 TYR B CA  1 
ATOM   3481 C  C   . TYR B 1 167 ? -9.949  11.003  -11.427 1.00 10.93 ? 167 TYR B C   1 
ATOM   3482 O  O   . TYR B 1 167 ? -11.161 11.004  -11.078 1.00 11.14 ? 167 TYR B O   1 
ATOM   3483 C  CB  . TYR B 1 167 ? -9.461  11.087  -13.851 1.00 12.41 ? 167 TYR B CB  1 
ATOM   3484 C  CG  . TYR B 1 167 ? -9.046  10.327  -15.110 1.00 13.66 ? 167 TYR B CG  1 
ATOM   3485 C  CD1 . TYR B 1 167 ? -7.694  9.955   -15.309 1.00 13.99 ? 167 TYR B CD1 1 
ATOM   3486 C  CD2 . TYR B 1 167 ? -10.005 9.924   -16.067 1.00 15.29 ? 167 TYR B CD2 1 
ATOM   3487 C  CE1 . TYR B 1 167 ? -7.328  9.187   -16.424 1.00 15.49 ? 167 TYR B CE1 1 
ATOM   3488 C  CE2 . TYR B 1 167 ? -9.618  9.234   -17.221 1.00 15.83 ? 167 TYR B CE2 1 
ATOM   3489 C  CZ  . TYR B 1 167 ? -8.290  8.849   -17.376 1.00 18.03 ? 167 TYR B CZ  1 
ATOM   3490 O  OH  . TYR B 1 167 ? -7.946  8.120   -18.525 1.00 18.36 ? 167 TYR B OH  1 
ATOM   3491 N  N   . LYS B 1 168 ? -9.008  11.785  -10.871 1.00 11.13 ? 168 LYS B N   1 
ATOM   3492 C  CA  . LYS B 1 168 ? -9.328  12.634  -9.771  1.00 11.84 ? 168 LYS B CA  1 
ATOM   3493 C  C   . LYS B 1 168 ? -10.502 13.556  -10.100 1.00 12.53 ? 168 LYS B C   1 
ATOM   3494 O  O   . LYS B 1 168 ? -10.572 14.178  -11.174 1.00 15.05 ? 168 LYS B O   1 
ATOM   3495 C  CB  . LYS B 1 168 ? -8.130  13.568  -9.505  1.00 11.34 ? 168 LYS B CB  1 
ATOM   3496 C  CG  . LYS B 1 168 ? -8.379  14.428  -8.290  1.00 13.69 ? 168 LYS B CG  1 
ATOM   3497 C  CD  . LYS B 1 168 ? -7.141  15.262  -8.005  1.00 15.86 ? 168 LYS B CD  1 
ATOM   3498 C  CE  . LYS B 1 168 ? -7.408  16.286  -6.873  1.00 22.35 ? 168 LYS B CE  1 
ATOM   3499 N  NZ  . LYS B 1 168 ? -6.195  17.162  -6.762  1.00 23.31 ? 168 LYS B NZ  1 
ATOM   3500 N  N   . GLY B 1 169 ? -11.420 13.643  -9.123  1.00 13.51 ? 169 GLY B N   1 
ATOM   3501 C  CA  . GLY B 1 169 ? -12.635 14.537  -9.209  1.00 14.31 ? 169 GLY B CA  1 
ATOM   3502 C  C   . GLY B 1 169 ? -13.825 13.896  -9.850  1.00 16.88 ? 169 GLY B C   1 
ATOM   3503 O  O   . GLY B 1 169 ? -14.940 14.474  -9.853  1.00 16.81 ? 169 GLY B O   1 
ATOM   3504 N  N   . GLN B 1 170 ? -13.662 12.720  -10.443 1.00 13.41 ? 170 GLN B N   1 
ATOM   3505 C  CA  . GLN B 1 170 ? -14.794 12.023  -11.108 1.00 16.60 ? 170 GLN B CA  1 
ATOM   3506 C  C   . GLN B 1 170 ? -15.657 11.337  -10.031 1.00 16.01 ? 170 GLN B C   1 
ATOM   3507 O  O   . GLN B 1 170 ? -15.159 10.903  -8.975  1.00 14.91 ? 170 GLN B O   1 
ATOM   3508 C  CB  . GLN B 1 170 ? -14.283 11.041  -12.145 1.00 15.22 ? 170 GLN B CB  1 
ATOM   3509 C  CG  . GLN B 1 170 ? -13.512 11.741  -13.299 1.00 15.14 ? 170 GLN B CG  1 
ATOM   3510 C  CD  . GLN B 1 170 ? -13.226 10.834  -14.479 1.00 16.39 ? 170 GLN B CD  1 
ATOM   3511 O  OE1 . GLN B 1 170 ? -12.866 9.635   -14.345 1.00 16.08 ? 170 GLN B OE1 1 
ATOM   3512 N  NE2 . GLN B 1 170 ? -13.403 11.389  -15.692 1.00 18.43 ? 170 GLN B NE2 1 
ATOM   3513 N  N   . GLU B 1 171 ? -16.942 11.238  -10.355 1.00 16.07 ? 171 GLU B N   1 
ATOM   3514 C  CA  . GLU B 1 171 ? -18.005 10.712  -9.464  1.00 15.91 ? 171 GLU B CA  1 
ATOM   3515 C  C   . GLU B 1 171 ? -18.925 9.847   -10.306 1.00 15.23 ? 171 GLU B C   1 
ATOM   3516 O  O   . GLU B 1 171 ? -19.080 10.055  -11.537 1.00 16.69 ? 171 GLU B O   1 
ATOM   3517 C  CB  . GLU B 1 171 ? -18.771 11.903  -8.816  1.00 18.04 ? 171 GLU B CB  1 
ATOM   3518 C  CG  . GLU B 1 171 ? -17.947 12.665  -7.771  1.00 22.92 ? 171 GLU B CG  1 
ATOM   3519 C  CD  . GLU B 1 171 ? -18.602 13.949  -7.222  1.00 30.13 ? 171 GLU B CD  1 
ATOM   3520 O  OE1 . GLU B 1 171 ? -19.702 14.327  -7.679  1.00 29.92 ? 171 GLU B OE1 1 
ATOM   3521 O  OE2 . GLU B 1 171 ? -17.979 14.583  -6.334  1.00 37.46 ? 171 GLU B OE2 1 
ATOM   3522 N  N   . ALA B 1 172 ? -19.360 8.724   -9.695  1.00 14.58 ? 172 ALA B N   1 
ATOM   3523 C  CA  . ALA B 1 172 ? -20.269 7.767   -10.273 1.00 15.23 ? 172 ALA B CA  1 
ATOM   3524 C  C   . ALA B 1 172 ? -21.258 7.388   -9.159  1.00 14.99 ? 172 ALA B C   1 
ATOM   3525 O  O   . ALA B 1 172 ? -21.019 7.675   -7.966  1.00 17.05 ? 172 ALA B O   1 
ATOM   3526 C  CB  . ALA B 1 172 ? -19.526 6.540   -10.815 1.00 15.70 ? 172 ALA B CB  1 
ATOM   3527 N  N   . PHE B 1 173 ? -22.355 6.784   -9.553  1.00 16.42 ? 173 PHE B N   1 
ATOM   3528 C  CA  . PHE B 1 173 ? -23.341 6.246   -8.624  1.00 13.03 ? 173 PHE B CA  1 
ATOM   3529 C  C   . PHE B 1 173 ? -23.383 4.690   -8.626  1.00 13.99 ? 173 PHE B C   1 
ATOM   3530 O  O   . PHE B 1 173 ? -23.255 4.037   -9.659  1.00 17.04 ? 173 PHE B O   1 
ATOM   3531 C  CB  . PHE B 1 173 ? -24.764 6.792   -8.968  1.00 15.36 ? 173 PHE B CB  1 
ATOM   3532 C  CG  . PHE B 1 173 ? -25.064 8.148   -8.390  1.00 18.70 ? 173 PHE B CG  1 
ATOM   3533 C  CD1 . PHE B 1 173 ? -25.132 8.324   -6.993  1.00 19.60 ? 173 PHE B CD1 1 
ATOM   3534 C  CD2 . PHE B 1 173 ? -25.275 9.240   -9.199  1.00 23.42 ? 173 PHE B CD2 1 
ATOM   3535 C  CE1 . PHE B 1 173 ? -25.381 9.550   -6.403  1.00 24.79 ? 173 PHE B CE1 1 
ATOM   3536 C  CE2 . PHE B 1 173 ? -25.510 10.503  -8.608  1.00 20.77 ? 173 PHE B CE2 1 
ATOM   3537 C  CZ  . PHE B 1 173 ? -25.565 10.668  -7.217  1.00 24.78 ? 173 PHE B CZ  1 
ATOM   3538 N  N   . VAL B 1 174 ? -23.438 4.162   -7.402  1.00 11.81 ? 174 VAL B N   1 
ATOM   3539 C  CA  . VAL B 1 174 ? -23.419 2.724   -7.177  1.00 12.40 ? 174 VAL B CA  1 
ATOM   3540 C  C   . VAL B 1 174 ? -24.802 2.366   -6.562  1.00 11.80 ? 174 VAL B C   1 
ATOM   3541 O  O   . VAL B 1 174 ? -25.156 2.906   -5.532  1.00 13.26 ? 174 VAL B O   1 
ATOM   3542 C  CB  . VAL B 1 174 ? -22.264 2.291   -6.272  1.00 13.16 ? 174 VAL B CB  1 
ATOM   3543 C  CG1 . VAL B 1 174 ? -22.343 0.789   -6.052  1.00 13.38 ? 174 VAL B CG1 1 
ATOM   3544 C  CG2 . VAL B 1 174 ? -20.928 2.564   -6.941  1.00 13.60 ? 174 VAL B CG2 1 
ATOM   3545 N  N   . PRO B 1 175 ? -25.517 1.371   -7.185  1.00 11.89 ? 175 PRO B N   1 
ATOM   3546 C  CA  . PRO B 1 175 ? -26.802 1.002   -6.558  1.00 11.87 ? 175 PRO B CA  1 
ATOM   3547 C  C   . PRO B 1 175 ? -26.532 0.440   -5.141  1.00 11.62 ? 175 PRO B C   1 
ATOM   3548 O  O   . PRO B 1 175 ? -25.525 -0.277  -4.909  1.00 11.88 ? 175 PRO B O   1 
ATOM   3549 C  CB  . PRO B 1 175 ? -27.356 -0.072  -7.504  1.00 10.53 ? 175 PRO B CB  1 
ATOM   3550 C  CG  . PRO B 1 175 ? -26.789 0.247   -8.883  1.00 12.00 ? 175 PRO B CG  1 
ATOM   3551 C  CD  . PRO B 1 175 ? -25.372 0.843   -8.565  1.00 11.56 ? 175 PRO B CD  1 
ATOM   3552 N  N   . GLY B 1 176 ? -27.464 0.634   -4.192  1.00 12.78 ? 176 GLY B N   1 
ATOM   3553 C  CA  . GLY B 1 176 ? -27.274 0.003   -2.897  1.00 11.69 ? 176 GLY B CA  1 
ATOM   3554 C  C   . GLY B 1 176 ? -27.237 -1.532  -2.951  1.00 11.59 ? 176 GLY B C   1 
ATOM   3555 O  O   . GLY B 1 176 ? -27.824 -2.182  -3.845  1.00 13.91 ? 176 GLY B O   1 
ATOM   3556 N  N   . PHE B 1 177 ? -26.487 -2.021  -1.972  1.00 11.81 ? 177 PHE B N   1 
ATOM   3557 C  CA  . PHE B 1 177 ? -26.376 -3.480  -1.719  1.00 10.95 ? 177 PHE B CA  1 
ATOM   3558 C  C   . PHE B 1 177 ? -26.100 -3.638  -0.232  1.00 11.54 ? 177 PHE B C   1 
ATOM   3559 O  O   . PHE B 1 177 ? -25.924 -2.665  0.490   1.00 12.13 ? 177 PHE B O   1 
ATOM   3560 C  CB  . PHE B 1 177 ? -25.322 -4.141  -2.626  1.00 12.28 ? 177 PHE B CB  1 
ATOM   3561 C  CG  . PHE B 1 177 ? -23.895 -3.723  -2.358  1.00 12.01 ? 177 PHE B CG  1 
ATOM   3562 C  CD1 . PHE B 1 177 ? -23.041 -4.599  -1.632  1.00 13.34 ? 177 PHE B CD1 1 
ATOM   3563 C  CD2 . PHE B 1 177 ? -23.395 -2.497  -2.878  1.00 12.16 ? 177 PHE B CD2 1 
ATOM   3564 C  CE1 . PHE B 1 177 ? -21.717 -4.246  -1.386  1.00 12.69 ? 177 PHE B CE1 1 
ATOM   3565 C  CE2 . PHE B 1 177 ? -22.039 -2.128  -2.592  1.00 13.40 ? 177 PHE B CE2 1 
ATOM   3566 C  CZ  . PHE B 1 177 ? -21.242 -3.041  -1.876  1.00 13.45 ? 177 PHE B CZ  1 
ATOM   3567 N  N   . ASN B 1 178 ? -26.035 -4.915  0.182   1.00 12.10 ? 178 ASN B N   1 
ATOM   3568 C  CA  . ASN B 1 178 ? -25.892 -5.145  1.577   1.00 10.75 ? 178 ASN B CA  1 
ATOM   3569 C  C   . ASN B 1 178 ? -24.410 -5.101  1.885   1.00 11.48 ? 178 ASN B C   1 
ATOM   3570 O  O   . ASN B 1 178 ? -23.620 -5.999  1.557   1.00 11.82 ? 178 ASN B O   1 
ATOM   3571 C  CB  . ASN B 1 178 ? -26.503 -6.519  1.923   1.00 12.45 ? 178 ASN B CB  1 
ATOM   3572 C  CG  . ASN B 1 178 ? -26.347 -6.816  3.367   1.00 12.45 ? 178 ASN B CG  1 
ATOM   3573 O  OD1 . ASN B 1 178 ? -25.968 -5.965  4.257   1.00 12.09 ? 178 ASN B OD1 1 
ATOM   3574 N  ND2 . ASN B 1 178 ? -26.668 -8.133  3.676   1.00 16.85 ? 178 ASN B ND2 1 
ATOM   3575 N  N   . ILE B 1 179 ? -24.048 -3.988  2.502   1.00 10.16 ? 179 ILE B N   1 
ATOM   3576 C  CA  . ILE B 1 179 ? -22.588 -3.832  2.881   1.00 11.44 ? 179 ILE B CA  1 
ATOM   3577 C  C   . ILE B 1 179 ? -22.060 -4.960  3.820   1.00 12.42 ? 179 ILE B C   1 
ATOM   3578 O  O   . ILE B 1 179 ? -20.828 -5.249  3.857   1.00 13.07 ? 179 ILE B O   1 
ATOM   3579 C  CB  . ILE B 1 179 ? -22.355 -2.424  3.521   1.00 11.38 ? 179 ILE B CB  1 
ATOM   3580 C  CG1 . ILE B 1 179 ? -22.819 -1.264  2.591   1.00 12.51 ? 179 ILE B CG1 1 
ATOM   3581 C  CG2 . ILE B 1 179 ? -20.887 -2.161  3.943   1.00 11.62 ? 179 ILE B CG2 1 
ATOM   3582 C  CD1 . ILE B 1 179 ? -22.295 -1.283  1.130   1.00 11.93 ? 179 ILE B CD1 1 
ATOM   3583 N  N   . GLU B 1 180 ? -22.921 -5.574  4.639   1.00 12.72 ? 180 GLU B N   1 
ATOM   3584 C  CA  . GLU B 1 180 ? -22.503 -6.711  5.444   1.00 15.23 ? 180 GLU B CA  1 
ATOM   3585 C  C   . GLU B 1 180 ? -21.912 -7.819  4.605   1.00 13.10 ? 180 GLU B C   1 
ATOM   3586 O  O   . GLU B 1 180 ? -21.122 -8.611  5.117   1.00 13.85 ? 180 GLU B O   1 
ATOM   3587 C  CB  . GLU B 1 180 ? -23.684 -7.283  6.276   1.00 15.87 ? 180 GLU B CB  1 
ATOM   3588 C  CG  . GLU B 1 180 ? -23.210 -8.173  7.407   1.00 21.46 ? 180 GLU B CG  1 
ATOM   3589 C  CD  . GLU B 1 180 ? -24.204 -8.239  8.567   1.00 22.54 ? 180 GLU B CD  1 
ATOM   3590 O  OE1 . GLU B 1 180 ? -25.309 -7.670  8.429   1.00 24.28 ? 180 GLU B OE1 1 
ATOM   3591 O  OE2 . GLU B 1 180 ? -23.828 -8.793  9.607   1.00 29.05 ? 180 GLU B OE2 1 
ATOM   3592 N  N   . GLU B 1 181 ? -22.272 -7.915  3.321   1.00 13.00 ? 181 GLU B N   1 
ATOM   3593 C  CA  . GLU B 1 181 ? -21.654 -8.882  2.430   1.00 14.56 ? 181 GLU B CA  1 
ATOM   3594 C  C   . GLU B 1 181 ? -20.152 -8.693  2.251   1.00 12.88 ? 181 GLU B C   1 
ATOM   3595 O  O   . GLU B 1 181 ? -19.495 -9.606  1.691   1.00 15.08 ? 181 GLU B O   1 
ATOM   3596 C  CB  . GLU B 1 181 ? -22.313 -8.864  1.050   1.00 14.42 ? 181 GLU B CB  1 
ATOM   3597 C  CG  . GLU B 1 181 ? -23.779 -9.294  1.072   1.00 17.91 ? 181 GLU B CG  1 
ATOM   3598 C  CD  . GLU B 1 181 ? -24.466 -9.080  -0.282  1.00 20.48 ? 181 GLU B CD  1 
ATOM   3599 O  OE1 . GLU B 1 181 ? -23.832 -8.633  -1.321  1.00 22.72 ? 181 GLU B OE1 1 
ATOM   3600 O  OE2 . GLU B 1 181 ? -25.745 -9.248  -0.345  1.00 23.24 ? 181 GLU B OE2 1 
ATOM   3601 N  N   . LEU B 1 182 ? -19.658 -7.479  2.549   1.00 10.35 ? 182 LEU B N   1 
ATOM   3602 C  CA  . LEU B 1 182 ? -18.212 -7.255  2.406   1.00 9.31  ? 182 LEU B CA  1 
ATOM   3603 C  C   . LEU B 1 182 ? -17.443 -7.695  3.650   1.00 9.23  ? 182 LEU B C   1 
ATOM   3604 O  O   . LEU B 1 182 ? -16.140 -7.632  3.646   1.00 9.60  ? 182 LEU B O   1 
ATOM   3605 C  CB  . LEU B 1 182 ? -18.006 -5.724  2.270   1.00 9.29  ? 182 LEU B CB  1 
ATOM   3606 C  CG  . LEU B 1 182 ? -18.668 -5.145  0.989   1.00 8.14  ? 182 LEU B CG  1 
ATOM   3607 C  CD1 . LEU B 1 182 ? -18.357 -3.598  0.991   1.00 9.44  ? 182 LEU B CD1 1 
ATOM   3608 C  CD2 . LEU B 1 182 ? -18.266 -5.741  -0.319  1.00 9.93  ? 182 LEU B CD2 1 
ATOM   3609 N  N   . LEU B 1 183 ? -18.136 -7.939  4.767   1.00 10.06 ? 183 LEU B N   1 
ATOM   3610 C  CA  . LEU B 1 183 ? -17.490 -8.394  5.994   1.00 11.07 ? 183 LEU B CA  1 
ATOM   3611 C  C   . LEU B 1 183 ? -17.199 -9.916  5.955   1.00 11.32 ? 183 LEU B C   1 
ATOM   3612 O  O   . LEU B 1 183 ? -17.868 -10.726 5.259   1.00 12.56 ? 183 LEU B O   1 
ATOM   3613 C  CB  . LEU B 1 183 ? -18.350 -8.095  7.188   1.00 13.30 ? 183 LEU B CB  1 
ATOM   3614 C  CG  . LEU B 1 183 ? -18.733 -6.652  7.405   1.00 13.78 ? 183 LEU B CG  1 
ATOM   3615 C  CD1 . LEU B 1 183 ? -19.222 -6.581  8.887   1.00 17.51 ? 183 LEU B CD1 1 
ATOM   3616 C  CD2 . LEU B 1 183 ? -17.683 -5.619  7.125   1.00 15.19 ? 183 LEU B CD2 1 
ATOM   3617 N  N   . PRO B 1 184 ? -16.182 -10.334 6.710   1.00 12.25 ? 184 PRO B N   1 
ATOM   3618 C  CA  . PRO B 1 184 ? -15.831 -11.754 6.683   1.00 12.61 ? 184 PRO B CA  1 
ATOM   3619 C  C   . PRO B 1 184 ? -16.694 -12.578 7.573   1.00 15.36 ? 184 PRO B C   1 
ATOM   3620 O  O   . PRO B 1 184 ? -17.674 -12.100 8.145   1.00 15.54 ? 184 PRO B O   1 
ATOM   3621 C  CB  . PRO B 1 184 ? -14.463 -11.743 7.322   1.00 13.43 ? 184 PRO B CB  1 
ATOM   3622 C  CG  . PRO B 1 184 ? -14.547 -10.620 8.336   1.00 15.65 ? 184 PRO B CG  1 
ATOM   3623 C  CD  . PRO B 1 184 ? -15.260 -9.586  7.528   1.00 12.03 ? 184 PRO B CD  1 
ATOM   3624 N  N   . GLU B 1 185 ? -16.292 -13.857 7.657   1.00 16.61 ? 185 GLU B N   1 
ATOM   3625 C  CA  . GLU B 1 185 ? -16.876 -14.804 8.609   1.00 19.56 ? 185 GLU B CA  1 
ATOM   3626 C  C   . GLU B 1 185 ? -16.503 -14.481 10.021  1.00 18.53 ? 185 GLU B C   1 
ATOM   3627 O  O   . GLU B 1 185 ? -15.400 -13.908 10.288  1.00 18.35 ? 185 GLU B O   1 
ATOM   3628 C  CB  . GLU B 1 185 ? -16.360 -16.204 8.291   1.00 21.60 ? 185 GLU B CB  1 
ATOM   3629 C  CG  . GLU B 1 185 ? -16.825 -16.713 6.965   1.00 26.39 ? 185 GLU B CG  1 
ATOM   3630 C  CD  . GLU B 1 185 ? -16.703 -18.239 6.911   1.00 32.82 ? 185 GLU B CD  1 
ATOM   3631 O  OE1 . GLU B 1 185 ? -17.752 -18.925 6.806   1.00 42.95 ? 185 GLU B OE1 1 
ATOM   3632 O  OE2 . GLU B 1 185 ? -15.567 -18.760 7.035   1.00 38.35 ? 185 GLU B OE2 1 
ATOM   3633 N  N   A ARG B 1 186 ? -17.379 -14.860 10.945  0.50 18.65 ? 186 ARG B N   1 
ATOM   3634 N  N   B ARG B 1 186 ? -17.439 -14.802 10.906  0.50 18.90 ? 186 ARG B N   1 
ATOM   3635 C  CA  A ARG B 1 186 ? -17.136 -14.706 12.385  0.50 16.79 ? 186 ARG B CA  1 
ATOM   3636 C  CA  B ARG B 1 186 ? -17.285 -14.670 12.351  0.50 17.44 ? 186 ARG B CA  1 
ATOM   3637 C  C   A ARG B 1 186 ? -16.757 -13.254 12.718  0.50 14.82 ? 186 ARG B C   1 
ATOM   3638 C  C   B ARG B 1 186 ? -16.791 -13.268 12.701  0.50 15.30 ? 186 ARG B C   1 
ATOM   3639 O  O   A ARG B 1 186 ? -15.707 -12.994 13.318  0.50 15.34 ? 186 ARG B O   1 
ATOM   3640 O  O   B ARG B 1 186 ? -15.716 -13.076 13.279  0.50 16.10 ? 186 ARG B O   1 
ATOM   3641 C  CB  A ARG B 1 186 ? -16.012 -15.706 12.845  0.50 19.54 ? 186 ARG B CB  1 
ATOM   3642 C  CB  B ARG B 1 186 ? -16.350 -15.775 12.875  0.50 20.62 ? 186 ARG B CB  1 
ATOM   3643 C  CG  A ARG B 1 186 ? -16.389 -17.206 12.778  0.50 21.06 ? 186 ARG B CG  1 
ATOM   3644 C  CG  B ARG B 1 186 ? -17.006 -17.164 12.878  0.50 21.57 ? 186 ARG B CG  1 
ATOM   3645 C  CD  A ARG B 1 186 ? -15.282 -18.123 13.293  0.50 21.12 ? 186 ARG B CD  1 
ATOM   3646 C  CD  B ARG B 1 186 ? -16.043 -18.293 13.216  0.50 23.28 ? 186 ARG B CD  1 
ATOM   3647 N  NE  A ARG B 1 186 ? -14.433 -18.641 12.218  0.50 21.86 ? 186 ARG B NE  1 
ATOM   3648 N  NE  B ARG B 1 186 ? -15.017 -18.517 12.204  0.50 25.58 ? 186 ARG B NE  1 
ATOM   3649 C  CZ  A ARG B 1 186 ? -13.118 -18.441 12.129  0.50 21.29 ? 186 ARG B CZ  1 
ATOM   3650 C  CZ  B ARG B 1 186 ? -15.254 -18.970 10.976  0.50 23.21 ? 186 ARG B CZ  1 
ATOM   3651 N  NH1 A ARG B 1 186 ? -12.479 -17.734 13.050  0.50 17.30 ? 186 ARG B NH1 1 
ATOM   3652 N  NH1 B ARG B 1 186 ? -16.490 -19.249 10.596  0.50 22.63 ? 186 ARG B NH1 1 
ATOM   3653 N  NH2 A ARG B 1 186 ? -12.436 -18.949 11.112  0.50 21.92 ? 186 ARG B NH2 1 
ATOM   3654 N  NH2 B ARG B 1 186 ? -14.247 -19.138 10.125  0.50 22.12 ? 186 ARG B NH2 1 
ATOM   3655 N  N   . THR B 1 187 ? -17.593 -12.287 12.337  1.00 14.16 ? 187 THR B N   1 
ATOM   3656 C  CA  . THR B 1 187 ? -17.258 -10.947 12.738  1.00 12.78 ? 187 THR B CA  1 
ATOM   3657 C  C   . THR B 1 187 ? -17.095 -10.754 14.269  1.00 12.76 ? 187 THR B C   1 
ATOM   3658 O  O   . THR B 1 187 ? -16.507 -9.718  14.752  1.00 12.12 ? 187 THR B O   1 
ATOM   3659 C  CB  . THR B 1 187 ? -18.211 -9.910  12.216  1.00 12.02 ? 187 THR B CB  1 
ATOM   3660 O  OG1 . THR B 1 187 ? -19.591 -10.351 12.517  1.00 14.42 ? 187 THR B OG1 1 
ATOM   3661 C  CG2 . THR B 1 187 ? -18.024 -9.764  10.674  1.00 12.51 ? 187 THR B CG2 1 
ATOM   3662 N  N   . ALA B 1 188 ? -17.613 -11.672 15.111  1.00 11.46 ? 188 ALA B N   1 
ATOM   3663 C  CA  . ALA B 1 188 ? -17.368 -11.460 16.514  1.00 10.35 ? 188 ALA B CA  1 
ATOM   3664 C  C   . ALA B 1 188 ? -15.863 -11.540 16.923  1.00 10.56 ? 188 ALA B C   1 
ATOM   3665 O  O   . ALA B 1 188 ? -15.547 -11.206 18.025  1.00 12.57 ? 188 ALA B O   1 
ATOM   3666 C  CB  . ALA B 1 188 ? -18.237 -12.375 17.406  1.00 13.72 ? 188 ALA B CB  1 
ATOM   3667 N  N   . GLU B 1 189 ? -15.035 -12.096 16.040  1.00 12.46 ? 189 GLU B N   1 
ATOM   3668 C  CA  . GLU B 1 189 ? -13.603 -12.227 16.336  1.00 11.97 ? 189 GLU B CA  1 
ATOM   3669 C  C   . GLU B 1 189 ? -12.860 -11.056 15.665  1.00 11.46 ? 189 GLU B C   1 
ATOM   3670 O  O   . GLU B 1 189 ? -12.823 -10.982 14.393  1.00 10.24 ? 189 GLU B O   1 
ATOM   3671 C  CB  . GLU B 1 189 ? -13.071 -13.527 15.763  1.00 14.84 ? 189 GLU B CB  1 
ATOM   3672 C  CG  . GLU B 1 189 ? -13.876 -14.676 16.385  1.00 17.44 ? 189 GLU B CG  1 
ATOM   3673 C  CD  . GLU B 1 189 ? -13.460 -16.010 15.917  1.00 21.33 ? 189 GLU B CD  1 
ATOM   3674 O  OE1 . GLU B 1 189 ? -12.263 -16.275 15.727  1.00 22.34 ? 189 GLU B OE1 1 
ATOM   3675 O  OE2 . GLU B 1 189 ? -14.344 -16.931 15.846  1.00 27.94 ? 189 GLU B OE2 1 
ATOM   3676 N  N   . TYR B 1 190 ? -12.301 -10.188 16.470  1.00 10.77 ? 190 TYR B N   1 
ATOM   3677 C  CA  . TYR B 1 190 ? -11.634 -8.983  15.967  1.00 10.82 ? 190 TYR B CA  1 
ATOM   3678 C  C   . TYR B 1 190 ? -10.543 -8.545  16.901  1.00 11.23 ? 190 TYR B C   1 
ATOM   3679 O  O   . TYR B 1 190 ? -10.503 -8.888  18.075  1.00 10.93 ? 190 TYR B O   1 
ATOM   3680 C  CB  . TYR B 1 190 ? -12.636 -7.814  15.662  1.00 9.58  ? 190 TYR B CB  1 
ATOM   3681 C  CG  . TYR B 1 190 ? -13.456 -7.444  16.908  1.00 9.01  ? 190 TYR B CG  1 
ATOM   3682 C  CD1 . TYR B 1 190 ? -12.996 -6.512  17.837  1.00 9.50  ? 190 TYR B CD1 1 
ATOM   3683 C  CD2 . TYR B 1 190 ? -14.775 -7.980  17.074  1.00 9.76  ? 190 TYR B CD2 1 
ATOM   3684 C  CE1 . TYR B 1 190 ? -13.773 -6.149  18.969  1.00 9.32  ? 190 TYR B CE1 1 
ATOM   3685 C  CE2 . TYR B 1 190 ? -15.540 -7.627  18.204  1.00 10.93 ? 190 TYR B CE2 1 
ATOM   3686 C  CZ  . TYR B 1 190 ? -15.039 -6.678  19.096  1.00 10.87 ? 190 TYR B CZ  1 
ATOM   3687 O  OH  . TYR B 1 190 ? -15.728 -6.290  20.241  1.00 12.75 ? 190 TYR B OH  1 
ATOM   3688 N  N   . TYR B 1 191 ? -9.680  -7.656  16.364  1.00 10.82 ? 191 TYR B N   1 
ATOM   3689 C  CA  . TYR B 1 191 ? -8.670  -6.927  17.097  1.00 8.97  ? 191 TYR B CA  1 
ATOM   3690 C  C   . TYR B 1 191 ? -9.163  -5.485  17.234  1.00 9.42  ? 191 TYR B C   1 
ATOM   3691 O  O   . TYR B 1 191 ? -9.783  -4.940  16.349  1.00 10.40 ? 191 TYR B O   1 
ATOM   3692 C  CB  . TYR B 1 191 ? -7.382  -6.819  16.232  1.00 9.14  ? 191 TYR B CB  1 
ATOM   3693 C  CG  . TYR B 1 191 ? -6.782  -8.083  15.707  1.00 10.50 ? 191 TYR B CG  1 
ATOM   3694 C  CD1 . TYR B 1 191 ? -5.785  -8.690  16.445  1.00 12.13 ? 191 TYR B CD1 1 
ATOM   3695 C  CD2 . TYR B 1 191 ? -7.119  -8.562  14.446  1.00 10.60 ? 191 TYR B CD2 1 
ATOM   3696 C  CE1 . TYR B 1 191 ? -5.200  -9.862  15.981  1.00 12.78 ? 191 TYR B CE1 1 
ATOM   3697 C  CE2 . TYR B 1 191 ? -6.507  -9.738  13.900  1.00 12.63 ? 191 TYR B CE2 1 
ATOM   3698 C  CZ  . TYR B 1 191 ? -5.530  -10.327 14.660  1.00 12.55 ? 191 TYR B CZ  1 
ATOM   3699 O  OH  . TYR B 1 191 ? -4.969  -11.527 14.132  1.00 16.52 ? 191 TYR B OH  1 
ATOM   3700 N  N   . ARG B 1 192 ? -8.859  -4.928  18.397  1.00 9.10  ? 192 ARG B N   1 
ATOM   3701 C  CA  . ARG B 1 192 ? -9.287  -3.591  18.729  1.00 9.26  ? 192 ARG B CA  1 
ATOM   3702 C  C   . ARG B 1 192 ? -8.145  -2.807  19.274  1.00 10.17 ? 192 ARG B C   1 
ATOM   3703 O  O   . ARG B 1 192 ? -7.474  -3.214  20.214  1.00 10.32 ? 192 ARG B O   1 
ATOM   3704 C  CB  . ARG B 1 192 ? -10.432 -3.727  19.822  1.00 10.54 ? 192 ARG B CB  1 
ATOM   3705 C  CG  . ARG B 1 192 ? -10.801 -2.373  20.521  1.00 11.94 ? 192 ARG B CG  1 
ATOM   3706 C  CD  . ARG B 1 192 ? -11.463 -1.288  19.697  1.00 13.38 ? 192 ARG B CD  1 
ATOM   3707 N  NE  . ARG B 1 192 ? -12.591 -1.795  18.903  1.00 13.67 ? 192 ARG B NE  1 
ATOM   3708 C  CZ  . ARG B 1 192 ? -13.803 -2.183  19.376  1.00 12.08 ? 192 ARG B CZ  1 
ATOM   3709 N  NH1 . ARG B 1 192 ? -14.088 -2.103  20.676  1.00 16.54 ? 192 ARG B NH1 1 
ATOM   3710 N  NH2 . ARG B 1 192 ? -14.718 -2.650  18.591  1.00 11.72 ? 192 ARG B NH2 1 
ATOM   3711 N  N   . TYR B 1 193 ? -8.037  -1.574  18.813  1.00 8.71  ? 193 TYR B N   1 
ATOM   3712 C  CA  . TYR B 1 193 ? -6.973  -0.682  19.365  1.00 10.16 ? 193 TYR B CA  1 
ATOM   3713 C  C   . TYR B 1 193 ? -7.206  0.782   19.095  1.00 10.69 ? 193 TYR B C   1 
ATOM   3714 O  O   . TYR B 1 193 ? -7.980  1.123   18.163  1.00 11.50 ? 193 TYR B O   1 
ATOM   3715 C  CB  . TYR B 1 193 ? -5.529  -1.153  18.952  1.00 11.15 ? 193 TYR B CB  1 
ATOM   3716 C  CG  . TYR B 1 193 ? -5.108  -0.743  17.529  1.00 9.78  ? 193 TYR B CG  1 
ATOM   3717 C  CD1 . TYR B 1 193 ? -4.404  0.443   17.311  1.00 9.10  ? 193 TYR B CD1 1 
ATOM   3718 C  CD2 . TYR B 1 193 ? -5.526  -1.470  16.414  1.00 8.28  ? 193 TYR B CD2 1 
ATOM   3719 C  CE1 . TYR B 1 193 ? -4.039  0.826   16.030  1.00 9.29  ? 193 TYR B CE1 1 
ATOM   3720 C  CE2 . TYR B 1 193 ? -5.215  -1.088  15.103  1.00 8.60  ? 193 TYR B CE2 1 
ATOM   3721 C  CZ  . TYR B 1 193 ? -4.485  0.125   14.938  1.00 7.96  ? 193 TYR B CZ  1 
ATOM   3722 O  OH  . TYR B 1 193 ? -4.160  0.447   13.622  1.00 9.12  ? 193 TYR B OH  1 
ATOM   3723 N  N   . ARG B 1 194 ? -6.498  1.655   19.863  1.00 12.53 ? 194 ARG B N   1 
ATOM   3724 C  CA  . ARG B 1 194 ? -6.614  3.128   19.671  1.00 11.80 ? 194 ARG B CA  1 
ATOM   3725 C  C   . ARG B 1 194 ? -5.554  3.464   18.687  1.00 12.54 ? 194 ARG B C   1 
ATOM   3726 O  O   . ARG B 1 194 ? -4.386  3.171   18.883  1.00 13.10 ? 194 ARG B O   1 
ATOM   3727 C  CB  . ARG B 1 194 ? -6.305  3.892   20.972  1.00 17.40 ? 194 ARG B CB  1 
ATOM   3728 C  CG  . ARG B 1 194 ? -7.008  3.330   22.182  1.00 24.48 ? 194 ARG B CG  1 
ATOM   3729 C  CD  . ARG B 1 194 ? -8.442  3.708   22.040  1.00 30.25 ? 194 ARG B CD  1 
ATOM   3730 N  NE  . ARG B 1 194 ? -9.221  3.606   23.269  1.00 47.04 ? 194 ARG B NE  1 
ATOM   3731 C  CZ  . ARG B 1 194 ? -9.803  4.650   23.846  1.00 52.65 ? 194 ARG B CZ  1 
ATOM   3732 N  NH1 . ARG B 1 194 ? -9.649  5.862   23.314  1.00 52.71 ? 194 ARG B NH1 1 
ATOM   3733 N  NH2 . ARG B 1 194 ? -10.535 4.482   24.948  1.00 61.44 ? 194 ARG B NH2 1 
ATOM   3734 N  N   . GLY B 1 195 ? -5.940  4.120   17.583  1.00 11.70 ? 195 GLY B N   1 
ATOM   3735 C  CA  . GLY B 1 195 ? -4.913  4.646   16.629  1.00 12.93 ? 195 GLY B CA  1 
ATOM   3736 C  C   . GLY B 1 195 ? -5.367  5.884   15.900  1.00 12.25 ? 195 GLY B C   1 
ATOM   3737 O  O   . GLY B 1 195 ? -5.980  6.756   16.489  1.00 12.53 ? 195 GLY B O   1 
ATOM   3738 N  N   . SER B 1 196 ? -5.038  5.942   14.616  1.00 12.51 ? 196 SER B N   1 
ATOM   3739 C  CA  . SER B 1 196 ? -5.210  7.160   13.888  1.00 10.74 ? 196 SER B CA  1 
ATOM   3740 C  C   . SER B 1 196 ? -5.729  6.924   12.479  1.00 10.45 ? 196 SER B C   1 
ATOM   3741 O  O   . SER B 1 196 ? -5.790  5.809   11.994  1.00 10.08 ? 196 SER B O   1 
ATOM   3742 C  CB  . SER B 1 196 ? -3.817  7.818   13.802  1.00 11.23 ? 196 SER B CB  1 
ATOM   3743 O  OG  . SER B 1 196 ? -3.019  7.233   12.770  1.00 10.41 ? 196 SER B OG  1 
ATOM   3744 N  N   . LEU B 1 197 ? -6.060  8.017   11.815  1.00 9.80  ? 197 LEU B N   1 
ATOM   3745 C  CA  . LEU B 1 197 ? -6.203  8.011   10.347  1.00 8.91  ? 197 LEU B CA  1 
ATOM   3746 C  C   . LEU B 1 197 ? -4.872  7.544   9.758   1.00 9.04  ? 197 LEU B C   1 
ATOM   3747 O  O   . LEU B 1 197 ? -3.761  7.952   10.285  1.00 10.01 ? 197 LEU B O   1 
ATOM   3748 C  CB  . LEU B 1 197 ? -6.487  9.451   9.780   1.00 9.56  ? 197 LEU B CB  1 
ATOM   3749 C  CG  . LEU B 1 197 ? -7.828  9.947   10.321  1.00 12.39 ? 197 LEU B CG  1 
ATOM   3750 C  CD1 . LEU B 1 197 ? -7.901  11.386  9.864   1.00 14.31 ? 197 LEU B CD1 1 
ATOM   3751 C  CD2 . LEU B 1 197 ? -9.065  9.225   9.892   1.00 14.38 ? 197 LEU B CD2 1 
ATOM   3752 N  N   . THR B 1 198 ? -4.937  6.759   8.646   1.00 9.16  ? 198 THR B N   1 
ATOM   3753 C  CA  . THR B 1 198 ? -3.680  6.314   8.038   1.00 9.37  ? 198 THR B CA  1 
ATOM   3754 C  C   . THR B 1 198 ? -3.265  7.191   6.864   1.00 10.49 ? 198 THR B C   1 
ATOM   3755 O  O   . THR B 1 198 ? -2.304  6.898   6.156   1.00 10.45 ? 198 THR B O   1 
ATOM   3756 C  CB  . THR B 1 198 ? -3.799  4.835   7.549   1.00 9.16  ? 198 THR B CB  1 
ATOM   3757 O  OG1 . THR B 1 198 ? -4.707  4.801   6.425   1.00 9.35  ? 198 THR B OG1 1 
ATOM   3758 C  CG2 . THR B 1 198 ? -4.231  3.863   8.685   1.00 10.71 ? 198 THR B CG2 1 
ATOM   3759 N  N   . THR B 1 199 ? -3.984  8.346   6.694   1.00 10.66 ? 199 THR B N   1 
ATOM   3760 C  CA  . THR B 1 199 ? -3.597  9.342   5.680   1.00 10.40 ? 199 THR B CA  1 
ATOM   3761 C  C   . THR B 1 199 ? -3.562  10.665  6.437   1.00 11.11 ? 199 THR B C   1 
ATOM   3762 O  O   . THR B 1 199 ? -4.192  10.778  7.502   1.00 11.07 ? 199 THR B O   1 
ATOM   3763 C  CB  . THR B 1 199 ? -4.657  9.419   4.549   1.00 11.79 ? 199 THR B CB  1 
ATOM   3764 O  OG1 . THR B 1 199 ? -5.930  9.791   5.116   1.00 13.05 ? 199 THR B OG1 1 
ATOM   3765 C  CG2 . THR B 1 199 ? -4.753  8.069   3.869   1.00 11.51 ? 199 THR B CG2 1 
ATOM   3766 N  N   . PRO B 1 200 ? -2.828  11.644  5.883   1.00 11.25 ? 200 PRO B N   1 
ATOM   3767 C  CA  . PRO B 1 200 ? -3.002  13.049  6.308   1.00 11.15 ? 200 PRO B CA  1 
ATOM   3768 C  C   . PRO B 1 200 ? -4.504  13.353  6.501   1.00 10.50 ? 200 PRO B C   1 
ATOM   3769 O  O   . PRO B 1 200 ? -5.278  13.059  5.613   1.00 12.30 ? 200 PRO B O   1 
ATOM   3770 C  CB  . PRO B 1 200 ? -2.366  13.814  5.151   1.00 10.60 ? 200 PRO B CB  1 
ATOM   3771 C  CG  . PRO B 1 200 ? -1.215  12.909  4.773   1.00 10.83 ? 200 PRO B CG  1 
ATOM   3772 C  CD  . PRO B 1 200 ? -1.949  11.543  4.718   1.00 11.20 ? 200 PRO B CD  1 
ATOM   3773 N  N   . PRO B 1 201 ? -4.854  14.026  7.619   1.00 11.58 ? 201 PRO B N   1 
ATOM   3774 C  CA  . PRO B 1 201 ? -3.964  14.666  8.572   1.00 11.82 ? 201 PRO B CA  1 
ATOM   3775 C  C   . PRO B 1 201 ? -3.503  13.720  9.742   1.00 12.38 ? 201 PRO B C   1 
ATOM   3776 O  O   . PRO B 1 201 ? -2.917  14.202  10.697  1.00 12.13 ? 201 PRO B O   1 
ATOM   3777 C  CB  . PRO B 1 201 ? -4.818  15.861  9.108   1.00 13.25 ? 201 PRO B CB  1 
ATOM   3778 C  CG  . PRO B 1 201 ? -6.250  15.369  9.025   1.00 15.25 ? 201 PRO B CG  1 
ATOM   3779 C  CD  . PRO B 1 201 ? -6.249  14.534  7.737   1.00 12.45 ? 201 PRO B CD  1 
ATOM   3780 N  N   . CYS B 1 202 ? -3.785  12.414  9.654   1.00 11.16 ? 202 CYS B N   1 
ATOM   3781 C  CA  . CYS B 1 202 ? -3.273  11.392  10.628  1.00 10.16 ? 202 CYS B CA  1 
ATOM   3782 C  C   . CYS B 1 202 ? -3.804  11.647  12.053  1.00 9.61  ? 202 CYS B C   1 
ATOM   3783 O  O   . CYS B 1 202 ? -3.148  11.257  13.012  1.00 9.77  ? 202 CYS B O   1 
ATOM   3784 C  CB  . CYS B 1 202 ? -1.704  11.303  10.668  1.00 10.83 ? 202 CYS B CB  1 
ATOM   3785 S  SG  . CYS B 1 202 ? -0.943  11.039  9.048   1.00 11.24 ? 202 CYS B SG  1 
ATOM   3786 N  N   . ASN B 1 203 ? -5.022  12.187  12.138  1.00 12.11 ? 203 ASN B N   1 
ATOM   3787 C  CA  . ASN B 1 203 ? -5.583  12.525  13.466  1.00 12.83 ? 203 ASN B CA  1 
ATOM   3788 C  C   . ASN B 1 203 ? -5.594  11.298  14.329  1.00 13.08 ? 203 ASN B C   1 
ATOM   3789 O  O   . ASN B 1 203 ? -6.090  10.218  13.916  1.00 10.99 ? 203 ASN B O   1 
ATOM   3790 C  CB  . ASN B 1 203 ? -7.036  13.025  13.338  1.00 15.16 ? 203 ASN B CB  1 
ATOM   3791 C  CG  . ASN B 1 203 ? -7.186  14.429  12.704  1.00 21.38 ? 203 ASN B CG  1 
ATOM   3792 O  OD1 . ASN B 1 203 ? -8.328  14.850  12.401  1.00 25.86 ? 203 ASN B OD1 1 
ATOM   3793 N  ND2 . ASN B 1 203 ? -6.079  15.156  12.529  1.00 22.77 ? 203 ASN B ND2 1 
ATOM   3794 N  N   . PRO B 1 204 ? -5.176  11.411  15.582  1.00 12.50 ? 204 PRO B N   1 
ATOM   3795 C  CA  . PRO B 1 204 ? -5.121  10.151  16.460  1.00 13.14 ? 204 PRO B CA  1 
ATOM   3796 C  C   . PRO B 1 204 ? -6.463  9.841   17.183  1.00 12.55 ? 204 PRO B C   1 
ATOM   3797 O  O   . PRO B 1 204 ? -6.549  9.806   18.474  1.00 13.86 ? 204 PRO B O   1 
ATOM   3798 C  CB  . PRO B 1 204 ? -3.971  10.429  17.414  1.00 12.90 ? 204 PRO B CB  1 
ATOM   3799 C  CG  . PRO B 1 204 ? -4.026  11.948  17.553  1.00 13.59 ? 204 PRO B CG  1 
ATOM   3800 C  CD  . PRO B 1 204 ? -4.341  12.480  16.149  1.00 14.98 ? 204 PRO B CD  1 
ATOM   3801 N  N   . THR B 1 205 ? -7.519  9.766   16.391  1.00 12.93 ? 205 THR B N   1 
ATOM   3802 C  CA  . THR B 1 205 ? -8.846  9.867   16.902  1.00 13.79 ? 205 THR B CA  1 
ATOM   3803 C  C   . THR B 1 205 ? -9.689  8.669   16.540  1.00 13.84 ? 205 THR B C   1 
ATOM   3804 O  O   . THR B 1 205 ? -10.892 8.723   16.613  1.00 15.81 ? 205 THR B O   1 
ATOM   3805 C  CB  . THR B 1 205 ? -9.565  11.145  16.382  1.00 13.97 ? 205 THR B CB  1 
ATOM   3806 O  OG1 . THR B 1 205 ? -9.421  11.209  14.950  1.00 13.57 ? 205 THR B OG1 1 
ATOM   3807 C  CG2 . THR B 1 205 ? -8.850  12.386  17.022  1.00 16.58 ? 205 THR B CG2 1 
ATOM   3808 N  N   . VAL B 1 206 ? -9.043  7.584   16.161  1.00 12.63 ? 206 VAL B N   1 
ATOM   3809 C  CA  . VAL B 1 206 ? -9.752  6.422   15.608  1.00 13.09 ? 206 VAL B CA  1 
ATOM   3810 C  C   . VAL B 1 206 ? -9.733  5.209   16.533  1.00 11.69 ? 206 VAL B C   1 
ATOM   3811 O  O   . VAL B 1 206 ? -8.722  4.828   17.016  1.00 12.01 ? 206 VAL B O   1 
ATOM   3812 C  CB  . VAL B 1 206 ? -9.139  5.975   14.213  1.00 12.67 ? 206 VAL B CB  1 
ATOM   3813 C  CG1 . VAL B 1 206 ? -9.848  4.714   13.705  1.00 13.26 ? 206 VAL B CG1 1 
ATOM   3814 C  CG2 . VAL B 1 206 ? -9.270  7.111   13.221  1.00 12.55 ? 206 VAL B CG2 1 
ATOM   3815 N  N   . LEU B 1 207 ? -10.887 4.652   16.805  1.00 10.57 ? 207 LEU B N   1 
ATOM   3816 C  CA  . LEU B 1 207 ? -11.000 3.349   17.438  1.00 12.64 ? 207 LEU B CA  1 
ATOM   3817 C  C   . LEU B 1 207 ? -11.033 2.315   16.284  1.00 10.33 ? 207 LEU B C   1 
ATOM   3818 O  O   . LEU B 1 207 ? -11.943 2.295   15.523  1.00 11.01 ? 207 LEU B O   1 
ATOM   3819 C  CB  . LEU B 1 207 ? -12.318 3.355   18.214  1.00 15.05 ? 207 LEU B CB  1 
ATOM   3820 C  CG  . LEU B 1 207 ? -12.460 2.165   19.141  1.00 20.04 ? 207 LEU B CG  1 
ATOM   3821 C  CD1 . LEU B 1 207 ? -11.413 2.194   20.270  1.00 22.57 ? 207 LEU B CD1 1 
ATOM   3822 C  CD2 . LEU B 1 207 ? -13.841 2.241   19.726  1.00 23.11 ? 207 LEU B CD2 1 
ATOM   3823 N  N   . TRP B 1 208 ? -9.948  1.537   16.148  1.00 9.86  ? 208 TRP B N   1 
ATOM   3824 C  CA  . TRP B 1 208 ? -9.859  0.497   15.078  1.00 9.67  ? 208 TRP B CA  1 
ATOM   3825 C  C   . TRP B 1 208 ? -10.429 -0.806  15.526  1.00 10.84 ? 208 TRP B C   1 
ATOM   3826 O  O   . TRP B 1 208 ? -10.228 -1.277  16.674  1.00 10.71 ? 208 TRP B O   1 
ATOM   3827 C  CB  . TRP B 1 208 ? -8.382  0.289   14.707  1.00 9.87  ? 208 TRP B CB  1 
ATOM   3828 C  CG  . TRP B 1 208 ? -7.866  1.404   13.822  1.00 8.87  ? 208 TRP B CG  1 
ATOM   3829 C  CD1 . TRP B 1 208 ? -7.218  2.572   14.188  1.00 10.24 ? 208 TRP B CD1 1 
ATOM   3830 C  CD2 . TRP B 1 208 ? -8.040  1.466   12.372  1.00 9.20  ? 208 TRP B CD2 1 
ATOM   3831 N  NE1 . TRP B 1 208 ? -6.965  3.329   13.096  1.00 10.32 ? 208 TRP B NE1 1 
ATOM   3832 C  CE2 . TRP B 1 208 ? -7.454  2.741   11.958  1.00 9.02  ? 208 TRP B CE2 1 
ATOM   3833 C  CE3 . TRP B 1 208 ? -8.607  0.656   11.446  1.00 9.19  ? 208 TRP B CE3 1 
ATOM   3834 C  CZ2 . TRP B 1 208 ? -7.415  3.115   10.611  1.00 9.03  ? 208 TRP B CZ2 1 
ATOM   3835 C  CZ3 . TRP B 1 208 ? -8.581  1.003   10.106  1.00 9.41  ? 208 TRP B CZ3 1 
ATOM   3836 C  CH2 . TRP B 1 208 ? -7.971  2.223   9.691   1.00 9.42  ? 208 TRP B CH2 1 
ATOM   3837 N  N   . THR B 1 209 ? -11.154 -1.400  14.614  1.00 8.88  ? 209 THR B N   1 
ATOM   3838 C  CA  . THR B 1 209 ? -11.611 -2.846  14.723  1.00 8.61  ? 209 THR B CA  1 
ATOM   3839 C  C   . THR B 1 209 ? -11.113 -3.501  13.458  1.00 8.95  ? 209 THR B C   1 
ATOM   3840 O  O   . THR B 1 209 ? -11.631 -3.184  12.403  1.00 10.06 ? 209 THR B O   1 
ATOM   3841 C  CB  . THR B 1 209 ? -13.173 -2.855  14.797  1.00 8.87  ? 209 THR B CB  1 
ATOM   3842 O  OG1 . THR B 1 209 ? -13.497 -2.219  16.020  1.00 10.66 ? 209 THR B OG1 1 
ATOM   3843 C  CG2 . THR B 1 209 ? -13.613 -4.378  14.896  1.00 10.27 ? 209 THR B CG2 1 
ATOM   3844 N  N   . VAL B 1 210 ? -10.211 -4.503  13.594  1.00 8.87  ? 210 VAL B N   1 
ATOM   3845 C  CA  . VAL B 1 210 ? -9.728  -5.244  12.427  1.00 9.31  ? 210 VAL B CA  1 
ATOM   3846 C  C   . VAL B 1 210 ? -10.285 -6.688  12.572  1.00 9.08  ? 210 VAL B C   1 
ATOM   3847 O  O   . VAL B 1 210 ? -10.051 -7.269  13.628  1.00 9.75  ? 210 VAL B O   1 
ATOM   3848 C  CB  . VAL B 1 210 ? -8.181  -5.273  12.407  1.00 8.97  ? 210 VAL B CB  1 
ATOM   3849 C  CG1 . VAL B 1 210 ? -7.775  -6.023  11.146  1.00 9.53  ? 210 VAL B CG1 1 
ATOM   3850 C  CG2 . VAL B 1 210 ? -7.657  -3.836  12.375  1.00 10.11 ? 210 VAL B CG2 1 
ATOM   3851 N  N   . PHE B 1 211 ? -11.148 -7.091  11.642  1.00 9.46  ? 211 PHE B N   1 
ATOM   3852 C  CA  . PHE B 1 211 ? -11.667 -8.473  11.804  1.00 9.49  ? 211 PHE B CA  1 
ATOM   3853 C  C   . PHE B 1 211 ? -10.571 -9.462  11.686  1.00 9.75  ? 211 PHE B C   1 
ATOM   3854 O  O   . PHE B 1 211 ? -9.556  -9.221  10.944  1.00 10.22 ? 211 PHE B O   1 
ATOM   3855 C  CB  . PHE B 1 211 ? -12.803 -8.689  10.797  1.00 9.71  ? 211 PHE B CB  1 
ATOM   3856 C  CG  . PHE B 1 211 ? -14.002 -7.816  11.086  1.00 10.17 ? 211 PHE B CG  1 
ATOM   3857 C  CD1 . PHE B 1 211 ? -14.296 -6.689  10.259  1.00 11.46 ? 211 PHE B CD1 1 
ATOM   3858 C  CD2 . PHE B 1 211 ? -14.742 -7.991  12.287  1.00 10.09 ? 211 PHE B CD2 1 
ATOM   3859 C  CE1 . PHE B 1 211 ? -15.365 -5.800  10.601  1.00 11.70 ? 211 PHE B CE1 1 
ATOM   3860 C  CE2 . PHE B 1 211 ? -15.826 -7.145  12.604  1.00 10.91 ? 211 PHE B CE2 1 
ATOM   3861 C  CZ  . PHE B 1 211 ? -16.166 -6.079  11.717  1.00 12.14 ? 211 PHE B CZ  1 
ATOM   3862 N  N   . ARG B 1 212 ? -10.733 -10.576 12.436  1.00 8.97  ? 212 ARG B N   1 
ATOM   3863 C  CA  . ARG B 1 212 ? -9.663  -11.574 12.487  1.00 10.12 ? 212 ARG B CA  1 
ATOM   3864 C  C   . ARG B 1 212 ? -9.577  -12.283 11.150  1.00 10.55 ? 212 ARG B C   1 
ATOM   3865 O  O   . ARG B 1 212 ? -8.439  -12.537 10.728  1.00 13.95 ? 212 ARG B O   1 
ATOM   3866 C  CB  . ARG B 1 212 ? -9.926  -12.582 13.630  1.00 10.49 ? 212 ARG B CB  1 
ATOM   3867 C  CG  . ARG B 1 212 ? -8.876  -13.722 13.628  1.00 11.21 ? 212 ARG B CG  1 
ATOM   3868 C  CD  . ARG B 1 212 ? -9.427  -14.745 14.648  1.00 13.76 ? 212 ARG B CD  1 
ATOM   3869 N  NE  . ARG B 1 212 ? -8.297  -15.661 14.950  1.00 15.09 ? 212 ARG B NE  1 
ATOM   3870 C  CZ  . ARG B 1 212 ? -8.309  -16.565 15.913  1.00 17.36 ? 212 ARG B CZ  1 
ATOM   3871 N  NH1 . ARG B 1 212 ? -9.425  -16.863 16.560  1.00 17.28 ? 212 ARG B NH1 1 
ATOM   3872 N  NH2 . ARG B 1 212 ? -7.179  -17.265 16.144  1.00 18.88 ? 212 ARG B NH2 1 
ATOM   3873 N  N   . ASN B 1 213 ? -10.712 -12.578 10.480  1.00 10.27 ? 213 ASN B N   1 
ATOM   3874 C  CA  . ASN B 1 213 ? -10.684 -13.385 9.287   1.00 11.84 ? 213 ASN B CA  1 
ATOM   3875 C  C   . ASN B 1 213 ? -10.714 -12.523 8.050   1.00 11.07 ? 213 ASN B C   1 
ATOM   3876 O  O   . ASN B 1 213 ? -11.517 -11.559 7.952   1.00 11.55 ? 213 ASN B O   1 
ATOM   3877 C  CB  . ASN B 1 213 ? -11.896 -14.355 9.286   1.00 13.76 ? 213 ASN B CB  1 
ATOM   3878 C  CG  . ASN B 1 213 ? -11.916 -15.271 10.530  1.00 17.37 ? 213 ASN B CG  1 
ATOM   3879 O  OD1 . ASN B 1 213 ? -12.951 -15.403 11.262  1.00 22.71 ? 213 ASN B OD1 1 
ATOM   3880 N  ND2 . ASN B 1 213 ? -10.779 -15.953 10.767  1.00 18.60 ? 213 ASN B ND2 1 
ATOM   3881 N  N   . PRO B 1 214 ? -9.882  -12.823 7.052   1.00 10.58 ? 214 PRO B N   1 
ATOM   3882 C  CA  . PRO B 1 214 ? -9.906  -12.122 5.748   1.00 11.30 ? 214 PRO B CA  1 
ATOM   3883 C  C   . PRO B 1 214 ? -11.067 -12.531 4.860   1.00 11.05 ? 214 PRO B C   1 
ATOM   3884 O  O   . PRO B 1 214 ? -11.710 -13.618 5.064   1.00 12.87 ? 214 PRO B O   1 
ATOM   3885 C  CB  . PRO B 1 214 ? -8.552  -12.485 5.162   1.00 10.89 ? 214 PRO B CB  1 
ATOM   3886 C  CG  . PRO B 1 214 ? -8.436  -13.996 5.561   1.00 12.03 ? 214 PRO B CG  1 
ATOM   3887 C  CD  . PRO B 1 214 ? -8.982  -14.028 7.032   1.00 11.96 ? 214 PRO B CD  1 
ATOM   3888 N  N   . VAL B 1 215 ? -11.384 -11.685 3.889   1.00 9.81  ? 215 VAL B N   1 
ATOM   3889 C  CA  . VAL B 1 215 ? -12.232 -12.104 2.777   1.00 9.94  ? 215 VAL B CA  1 
ATOM   3890 C  C   . VAL B 1 215 ? -11.349 -12.343 1.528   1.00 10.19 ? 215 VAL B C   1 
ATOM   3891 O  O   . VAL B 1 215 ? -10.131 -12.036 1.604   1.00 10.71 ? 215 VAL B O   1 
ATOM   3892 C  CB  . VAL B 1 215 ? -13.338 -11.071 2.489   1.00 10.43 ? 215 VAL B CB  1 
ATOM   3893 C  CG1 . VAL B 1 215 ? -14.194 -10.847 3.747   1.00 11.98 ? 215 VAL B CG1 1 
ATOM   3894 C  CG2 . VAL B 1 215 ? -12.692 -9.754  1.967   1.00 10.43 ? 215 VAL B CG2 1 
ATOM   3895 N  N   . GLN B 1 216 ? -11.907 -12.966 0.501   1.00 10.33 ? 216 GLN B N   1 
ATOM   3896 C  CA  . GLN B 1 216 ? -11.191 -13.223 -0.766  1.00 10.57 ? 216 GLN B CA  1 
ATOM   3897 C  C   . GLN B 1 216 ? -11.794 -12.361 -1.864  1.00 9.81  ? 216 GLN B C   1 
ATOM   3898 O  O   . GLN B 1 216 ? -13.052 -12.266 -1.952  1.00 12.11 ? 216 GLN B O   1 
ATOM   3899 C  CB  . GLN B 1 216 ? -11.216 -14.704 -1.207  1.00 12.30 ? 216 GLN B CB  1 
ATOM   3900 C  CG  . GLN B 1 216 ? -10.539 -15.632 -0.182  1.00 11.56 ? 216 GLN B CG  1 
ATOM   3901 C  CD  . GLN B 1 216 ? -10.411 -17.068 -0.656  1.00 14.57 ? 216 GLN B CD  1 
ATOM   3902 O  OE1 . GLN B 1 216 ? -11.002 -17.493 -1.659  1.00 13.07 ? 216 GLN B OE1 1 
ATOM   3903 N  NE2 . GLN B 1 216 ? -9.455  -17.759 -0.029  1.00 20.38 ? 216 GLN B NE2 1 
ATOM   3904 N  N   . ILE B 1 217 ? -10.918 -11.889 -2.757  1.00 9.16  ? 217 ILE B N   1 
ATOM   3905 C  CA  . ILE B 1 217 ? -11.333 -11.443 -4.090  1.00 8.68  ? 217 ILE B CA  1 
ATOM   3906 C  C   . ILE B 1 217 ? -10.357 -12.051 -5.085  1.00 8.92  ? 217 ILE B C   1 
ATOM   3907 O  O   . ILE B 1 217 ? -9.232  -12.468 -4.714  1.00 10.15 ? 217 ILE B O   1 
ATOM   3908 C  CB  . ILE B 1 217 ? -11.366 -9.860  -4.217  1.00 9.18  ? 217 ILE B CB  1 
ATOM   3909 C  CG1 . ILE B 1 217 ? -9.947  -9.265  -4.166  1.00 8.24  ? 217 ILE B CG1 1 
ATOM   3910 C  CG2 . ILE B 1 217 ? -12.288 -9.224  -3.119  1.00 10.63 ? 217 ILE B CG2 1 
ATOM   3911 C  CD1 . ILE B 1 217 ? -9.913  -7.724  -4.232  1.00 10.94 ? 217 ILE B CD1 1 
ATOM   3912 N  N   . SER B 1 218 ? -10.735 -12.066 -6.339  1.00 9.04  ? 218 SER B N   1 
ATOM   3913 C  CA  . SER B 1 218 ? -9.848  -12.809 -7.296  1.00 9.97  ? 218 SER B CA  1 
ATOM   3914 C  C   . SER B 1 218 ? -8.663  -12.033 -7.796  1.00 11.32 ? 218 SER B C   1 
ATOM   3915 O  O   . SER B 1 218 ? -8.633  -10.804 -7.700  1.00 10.32 ? 218 SER B O   1 
ATOM   3916 C  CB  . SER B 1 218 ? -10.686 -13.292 -8.495  1.00 10.92 ? 218 SER B CB  1 
ATOM   3917 O  OG  . SER B 1 218 ? -11.112 -12.187 -9.321  1.00 11.75 ? 218 SER B OG  1 
ATOM   3918 N  N   . GLN B 1 219 ? -7.698  -12.739 -8.368  1.00 11.75 ? 219 GLN B N   1 
ATOM   3919 C  CA  . GLN B 1 219 ? -6.608  -12.101 -9.085  1.00 12.96 ? 219 GLN B CA  1 
ATOM   3920 C  C   . GLN B 1 219 ? -7.085  -11.018 -10.130 1.00 13.12 ? 219 GLN B C   1 
ATOM   3921 O  O   . GLN B 1 219 ? -6.519  -9.908  -10.202 1.00 14.32 ? 219 GLN B O   1 
ATOM   3922 C  CB  . GLN B 1 219 ? -5.751  -13.174 -9.768  1.00 16.31 ? 219 GLN B CB  1 
ATOM   3923 C  CG  . GLN B 1 219 ? -4.441  -12.497 -10.259 1.00 25.50 ? 219 GLN B CG  1 
ATOM   3924 C  CD  . GLN B 1 219 ? -4.489  -11.809 -11.627 1.00 29.14 ? 219 GLN B CD  1 
ATOM   3925 O  OE1 . GLN B 1 219 ? -3.647  -10.916 -11.921 1.00 31.90 ? 219 GLN B OE1 1 
ATOM   3926 N  NE2 . GLN B 1 219 ? -5.419  -12.223 -12.482 1.00 28.58 ? 219 GLN B NE2 1 
ATOM   3927 N  N   . GLU B 1 220 ? -8.138  -11.352 -10.886 1.00 14.46 ? 220 GLU B N   1 
ATOM   3928 C  CA  . GLU B 1 220 ? -8.630  -10.438 -11.895 1.00 14.43 ? 220 GLU B CA  1 
ATOM   3929 C  C   . GLU B 1 220 ? -9.239  -9.204  -11.243 1.00 15.21 ? 220 GLU B C   1 
ATOM   3930 O  O   . GLU B 1 220 ? -9.078  -8.068  -11.761 1.00 13.92 ? 220 GLU B O   1 
ATOM   3931 C  CB  . GLU B 1 220 ? -9.620  -11.156 -12.816 1.00 17.02 ? 220 GLU B CB  1 
ATOM   3932 C  CG  . GLU B 1 220 ? -8.930  -12.255 -13.620 1.00 16.67 ? 220 GLU B CG  1 
ATOM   3933 C  CD  . GLU B 1 220 ? -8.805  -13.625 -12.963 1.00 18.99 ? 220 GLU B CD  1 
ATOM   3934 O  OE1 . GLU B 1 220 ? -9.215  -13.801 -11.792 1.00 19.69 ? 220 GLU B OE1 1 
ATOM   3935 O  OE2 . GLU B 1 220 ? -8.249  -14.523 -13.644 1.00 21.73 ? 220 GLU B OE2 1 
ATOM   3936 N  N   . GLN B 1 221 ? -9.920  -9.393  -10.093 1.00 11.99 ? 221 GLN B N   1 
ATOM   3937 C  CA  . GLN B 1 221 ? -10.506 -8.194  -9.388  1.00 10.28 ? 221 GLN B CA  1 
ATOM   3938 C  C   . GLN B 1 221 ? -9.402  -7.344  -8.827  1.00 10.13 ? 221 GLN B C   1 
ATOM   3939 O  O   . GLN B 1 221 ? -9.461  -6.086  -8.934  1.00 9.33  ? 221 GLN B O   1 
ATOM   3940 C  CB  . GLN B 1 221 ? -11.443 -8.598  -8.263  1.00 10.49 ? 221 GLN B CB  1 
ATOM   3941 C  CG  . GLN B 1 221 ? -12.735 -9.223  -8.775  1.00 10.71 ? 221 GLN B CG  1 
ATOM   3942 C  CD  . GLN B 1 221 ? -13.610 -9.699  -7.640  1.00 10.25 ? 221 GLN B CD  1 
ATOM   3943 O  OE1 . GLN B 1 221 ? -13.278 -10.641 -6.901  1.00 10.67 ? 221 GLN B OE1 1 
ATOM   3944 N  NE2 . GLN B 1 221 ? -14.800 -9.044  -7.479  1.00 10.05 ? 221 GLN B NE2 1 
ATOM   3945 N  N   . LEU B 1 222 ? -8.361  -7.978  -8.259  1.00 10.33 ? 222 LEU B N   1 
ATOM   3946 C  CA  . LEU B 1 222 ? -7.221  -7.161  -7.807  1.00 10.76 ? 222 LEU B CA  1 
ATOM   3947 C  C   . LEU B 1 222 ? -6.558  -6.453  -8.998  1.00 11.30 ? 222 LEU B C   1 
ATOM   3948 O  O   . LEU B 1 222 ? -6.164  -5.293  -8.864  1.00 10.07 ? 222 LEU B O   1 
ATOM   3949 C  CB  . LEU B 1 222 ? -6.182  -8.048  -7.075  1.00 12.08 ? 222 LEU B CB  1 
ATOM   3950 C  CG  . LEU B 1 222 ? -6.660  -8.455  -5.689  1.00 12.58 ? 222 LEU B CG  1 
ATOM   3951 C  CD1 . LEU B 1 222 ? -5.923  -9.738  -5.252  1.00 12.81 ? 222 LEU B CD1 1 
ATOM   3952 C  CD2 . LEU B 1 222 ? -6.243  -7.336  -4.746  1.00 12.51 ? 222 LEU B CD2 1 
ATOM   3953 N  N   . LEU B 1 223 ? -6.379  -7.139  -10.133 1.00 11.56 ? 223 LEU B N   1 
ATOM   3954 C  CA  . LEU B 1 223 ? -5.712  -6.518  -11.304 1.00 12.18 ? 223 LEU B CA  1 
ATOM   3955 C  C   . LEU B 1 223 ? -6.543  -5.328  -11.785 1.00 12.05 ? 223 LEU B C   1 
ATOM   3956 O  O   . LEU B 1 223 ? -5.969  -4.241  -12.026 1.00 10.89 ? 223 LEU B O   1 
ATOM   3957 C  CB  . LEU B 1 223 ? -5.589  -7.537  -12.463 1.00 13.43 ? 223 LEU B CB  1 
ATOM   3958 C  CG  . LEU B 1 223 ? -4.743  -6.932  -13.609 1.00 13.83 ? 223 LEU B CG  1 
ATOM   3959 C  CD1 . LEU B 1 223 ? -3.366  -6.523  -13.121 1.00 16.42 ? 223 LEU B CD1 1 
ATOM   3960 C  CD2 . LEU B 1 223 ? -4.683  -7.842  -14.804 1.00 16.31 ? 223 LEU B CD2 1 
ATOM   3961 N  N   . ALA B 1 224 ? -7.879  -5.464  -11.833 1.00 12.76 ? 224 ALA B N   1 
ATOM   3962 C  CA  . ALA B 1 224 ? -8.753  -4.319  -12.178 1.00 13.66 ? 224 ALA B CA  1 
ATOM   3963 C  C   . ALA B 1 224 ? -8.532  -3.194  -11.248 1.00 13.64 ? 224 ALA B C   1 
ATOM   3964 O  O   . ALA B 1 224 ? -8.356  -2.047  -11.667 1.00 14.68 ? 224 ALA B O   1 
ATOM   3965 C  CB  . ALA B 1 224 ? -10.202 -4.722  -12.188 1.00 17.15 ? 224 ALA B CB  1 
ATOM   3966 N  N   . LEU B 1 225 ? -8.625  -3.453  -9.940  1.00 11.53 ? 225 LEU B N   1 
ATOM   3967 C  CA  . LEU B 1 225 ? -8.488  -2.415  -8.933  1.00 11.84 ? 225 LEU B CA  1 
ATOM   3968 C  C   . LEU B 1 225 ? -7.149  -1.697  -9.063  1.00 11.02 ? 225 LEU B C   1 
ATOM   3969 O  O   . LEU B 1 225 ? -7.026  -0.471  -8.889  1.00 13.51 ? 225 LEU B O   1 
ATOM   3970 C  CB  . LEU B 1 225 ? -8.655  -3.093  -7.533  1.00 13.19 ? 225 LEU B CB  1 
ATOM   3971 C  CG  . LEU B 1 225 ? -8.441  -2.243  -6.347  1.00 13.77 ? 225 LEU B CG  1 
ATOM   3972 C  CD1 . LEU B 1 225 ? -9.438  -1.078  -6.242  1.00 13.62 ? 225 LEU B CD1 1 
ATOM   3973 C  CD2 . LEU B 1 225 ? -8.556  -3.040  -5.038  1.00 14.29 ? 225 LEU B CD2 1 
ATOM   3974 N  N   . GLU B 1 226 ? -6.112  -2.471  -9.318  1.00 9.82  ? 226 GLU B N   1 
ATOM   3975 C  CA  . GLU B 1 226 ? -4.750  -1.932  -9.428  1.00 9.83  ? 226 GLU B CA  1 
ATOM   3976 C  C   . GLU B 1 226 ? -4.414  -1.218  -10.755 1.00 10.91 ? 226 GLU B C   1 
ATOM   3977 O  O   . GLU B 1 226 ? -3.330  -0.634  -10.828 1.00 13.50 ? 226 GLU B O   1 
ATOM   3978 C  CB  . GLU B 1 226 ? -3.717  -3.098  -9.243  1.00 9.72  ? 226 GLU B CB  1 
ATOM   3979 C  CG  . GLU B 1 226 ? -3.787  -3.729  -7.878  1.00 10.47 ? 226 GLU B CG  1 
ATOM   3980 C  CD  . GLU B 1 226 ? -3.371  -5.219  -7.889  1.00 11.67 ? 226 GLU B CD  1 
ATOM   3981 O  OE1 . GLU B 1 226 ? -3.050  -5.798  -8.965  1.00 12.73 ? 226 GLU B OE1 1 
ATOM   3982 O  OE2 . GLU B 1 226 ? -3.411  -5.827  -6.801  1.00 12.53 ? 226 GLU B OE2 1 
ATOM   3983 N  N   . THR B 1 227 ? -5.223  -1.434  -11.774 1.00 11.27 ? 227 THR B N   1 
ATOM   3984 C  CA  . THR B 1 227 ? -4.983  -0.789  -13.071 1.00 12.48 ? 227 THR B CA  1 
ATOM   3985 C  C   . THR B 1 227 ? -6.026  0.243   -13.422 1.00 14.35 ? 227 THR B C   1 
ATOM   3986 O  O   . THR B 1 227 ? -5.781  1.078   -14.329 1.00 16.66 ? 227 THR B O   1 
ATOM   3987 C  CB  . THR B 1 227 ? -4.889  -1.801  -14.212 1.00 13.35 ? 227 THR B CB  1 
ATOM   3988 O  OG1 . THR B 1 227 ? -6.108  -2.522  -14.260 1.00 12.64 ? 227 THR B OG1 1 
ATOM   3989 C  CG2 . THR B 1 227 ? -3.672  -2.793  -13.947 1.00 12.69 ? 227 THR B CG2 1 
ATOM   3990 N  N   . ALA B 1 228 ? -7.140  0.303   -12.709 1.00 12.72 ? 228 ALA B N   1 
ATOM   3991 C  CA  . ALA B 1 228 ? -8.199  1.173   -13.176 1.00 13.67 ? 228 ALA B CA  1 
ATOM   3992 C  C   . ALA B 1 228 ? -7.978  2.736   -12.913 1.00 14.04 ? 228 ALA B C   1 
ATOM   3993 O  O   . ALA B 1 228 ? -8.652  3.560   -13.538 1.00 17.22 ? 228 ALA B O   1 
ATOM   3994 C  CB  . ALA B 1 228 ? -9.499  0.738   -12.531 1.00 15.70 ? 228 ALA B CB  1 
ATOM   3995 N  N   . LEU B 1 229 ? -7.252  3.063   -11.861 1.00 11.71 ? 229 LEU B N   1 
ATOM   3996 C  CA  . LEU B 1 229 ? -7.437  4.415   -11.249 1.00 10.18 ? 229 LEU B CA  1 
ATOM   3997 C  C   . LEU B 1 229 ? -6.156  5.200   -11.243 1.00 9.47  ? 229 LEU B C   1 
ATOM   3998 O  O   . LEU B 1 229 ? -5.056  4.653   -11.151 1.00 10.09 ? 229 LEU B O   1 
ATOM   3999 C  CB  . LEU B 1 229 ? -7.913  4.323   -9.753  1.00 11.00 ? 229 LEU B CB  1 
ATOM   4000 C  CG  . LEU B 1 229 ? -9.128  3.384   -9.558  1.00 13.87 ? 229 LEU B CG  1 
ATOM   4001 C  CD1 . LEU B 1 229 ? -9.361  3.007   -8.099  1.00 14.15 ? 229 LEU B CD1 1 
ATOM   4002 C  CD2 . LEU B 1 229 ? -10.381 4.041   -10.100 1.00 16.54 ? 229 LEU B CD2 1 
ATOM   4003 N  N   . TYR B 1 230 ? -6.347  6.497   -11.329 1.00 9.44  ? 230 TYR B N   1 
ATOM   4004 C  CA  . TYR B 1 230 ? -5.268  7.525   -11.363 1.00 10.21 ? 230 TYR B CA  1 
ATOM   4005 C  C   . TYR B 1 230 ? -5.475  8.500   -10.206 1.00 10.89 ? 230 TYR B C   1 
ATOM   4006 O  O   . TYR B 1 230 ? -6.612  8.845   -9.846  1.00 10.96 ? 230 TYR B O   1 
ATOM   4007 C  CB  . TYR B 1 230 ? -5.252  8.266   -12.760 1.00 10.94 ? 230 TYR B CB  1 
ATOM   4008 C  CG  . TYR B 1 230 ? -4.719  7.329   -13.780 1.00 10.80 ? 230 TYR B CG  1 
ATOM   4009 C  CD1 . TYR B 1 230 ? -3.365  7.358   -14.087 1.00 12.73 ? 230 TYR B CD1 1 
ATOM   4010 C  CD2 . TYR B 1 230 ? -5.552  6.402   -14.381 1.00 13.13 ? 230 TYR B CD2 1 
ATOM   4011 C  CE1 . TYR B 1 230 ? -2.824  6.353   -14.925 1.00 14.47 ? 230 TYR B CE1 1 
ATOM   4012 C  CE2 . TYR B 1 230 ? -5.041  5.425   -15.244 1.00 15.19 ? 230 TYR B CE2 1 
ATOM   4013 C  CZ  . TYR B 1 230 ? -3.684  5.391   -15.447 1.00 14.29 ? 230 TYR B CZ  1 
ATOM   4014 O  OH  . TYR B 1 230 ? -3.109  4.466   -16.342 1.00 19.36 ? 230 TYR B OH  1 
ATOM   4015 N  N   . CYS B 1 231 ? -4.374  8.989   -9.653  1.00 11.83 ? 231 CYS B N   1 
ATOM   4016 C  CA  . CYS B 1 231 ? -4.382  10.095  -8.638  1.00 11.97 ? 231 CYS B CA  1 
ATOM   4017 C  C   . CYS B 1 231 ? -4.666  11.450  -9.264  1.00 11.79 ? 231 CYS B C   1 
ATOM   4018 O  O   . CYS B 1 231 ? -4.918  12.388  -8.539  1.00 14.23 ? 231 CYS B O   1 
ATOM   4019 C  CB  . CYS B 1 231 ? -3.021  10.181  -7.953  1.00 11.84 ? 231 CYS B CB  1 
ATOM   4020 S  SG  . CYS B 1 231 ? -2.545  8.638   -7.067  1.00 13.93 ? 231 CYS B SG  1 
ATOM   4021 N  N   . THR B 1 232 ? -4.536  11.521  -10.590 1.00 11.22 ? 232 THR B N   1 
ATOM   4022 C  CA  . THR B 1 232 ? -4.428  12.845  -11.248 1.00 11.69 ? 232 THR B CA  1 
ATOM   4023 C  C   . THR B 1 232 ? -5.723  13.088  -12.054 1.00 12.67 ? 232 THR B C   1 
ATOM   4024 O  O   . THR B 1 232 ? -6.489  12.134  -12.410 1.00 11.80 ? 232 THR B O   1 
ATOM   4025 C  CB  . THR B 1 232 ? -3.124  12.825  -12.166 1.00 11.92 ? 232 THR B CB  1 
ATOM   4026 O  OG1 . THR B 1 232 ? -2.976  11.477  -12.721 1.00 10.58 ? 232 THR B OG1 1 
ATOM   4027 C  CG2 . THR B 1 232 ? -1.919  13.181  -11.292 1.00 13.59 ? 232 THR B CG2 1 
ATOM   4028 N  N   . HIS B 1 233 ? -5.990  14.369  -12.393 1.00 12.27 ? 233 HIS B N   1 
ATOM   4029 C  CA  . HIS B 1 233 ? -7.111  14.655  -13.275 1.00 13.94 ? 233 HIS B CA  1 
ATOM   4030 C  C   . HIS B 1 233 ? -6.945  14.083  -14.683 1.00 13.08 ? 233 HIS B C   1 
ATOM   4031 O  O   . HIS B 1 233 ? -5.835  13.797  -15.134 1.00 12.46 ? 233 HIS B O   1 
ATOM   4032 C  CB  . HIS B 1 233 ? -7.215  16.180  -13.444 1.00 15.76 ? 233 HIS B CB  1 
ATOM   4033 C  CG  . HIS B 1 233 ? -7.619  16.910  -12.176 1.00 18.53 ? 233 HIS B CG  1 
ATOM   4034 N  ND1 . HIS B 1 233 ? -6.868  17.928  -11.649 1.00 24.51 ? 233 HIS B ND1 1 
ATOM   4035 C  CD2 . HIS B 1 233 ? -8.749  16.817  -11.394 1.00 20.34 ? 233 HIS B CD2 1 
ATOM   4036 C  CE1 . HIS B 1 233 ? -7.477  18.427  -10.539 1.00 21.40 ? 233 HIS B CE1 1 
ATOM   4037 N  NE2 . HIS B 1 233 ? -8.621  17.759  -10.374 1.00 20.16 ? 233 HIS B NE2 1 
ATOM   4038 N  N   . MET B 1 234 ? -8.082  13.907  -15.352 1.00 13.93 ? 234 MET B N   1 
ATOM   4039 C  CA  . MET B 1 234 ? -8.176  13.352  -16.728 1.00 15.48 ? 234 MET B CA  1 
ATOM   4040 C  C   . MET B 1 234 ? -7.232  14.095  -17.671 1.00 16.01 ? 234 MET B C   1 
ATOM   4041 O  O   . MET B 1 234 ? -6.622  13.488  -18.540 1.00 15.99 ? 234 MET B O   1 
ATOM   4042 C  CB  . MET B 1 234 ? -9.620  13.434  -17.252 1.00 16.88 ? 234 MET B CB  1 
ATOM   4043 C  CG  . MET B 1 234 ? -9.805  12.636  -18.553 1.00 19.50 ? 234 MET B CG  1 
ATOM   4044 S  SD  . MET B 1 234 ? -11.592 12.445  -18.857 1.00 26.17 ? 234 MET B SD  1 
ATOM   4045 C  CE  . MET B 1 234 ? -11.625 11.419  -20.330 1.00 25.81 ? 234 MET B CE  1 
ATOM   4046 N  N   . ASP B 1 235 ? -7.066  15.391  -17.441 1.00 15.52 ? 235 ASP B N   1 
ATOM   4047 C  CA  . ASP B 1 235 ? -6.258  16.196  -18.389 1.00 17.16 ? 235 ASP B CA  1 
ATOM   4048 C  C   . ASP B 1 235 ? -4.848  16.495  -17.876 1.00 17.05 ? 235 ASP B C   1 
ATOM   4049 O  O   . ASP B 1 235 ? -4.170  17.435  -18.388 1.00 20.76 ? 235 ASP B O   1 
ATOM   4050 C  CB  . ASP B 1 235 ? -6.966  17.548  -18.679 1.00 21.14 ? 235 ASP B CB  1 
ATOM   4051 C  CG  . ASP B 1 235 ? -6.952  18.505  -17.483 1.00 26.10 ? 235 ASP B CG  1 
ATOM   4052 O  OD1 . ASP B 1 235 ? -6.584  18.140  -16.363 1.00 31.66 ? 235 ASP B OD1 1 
ATOM   4053 O  OD2 . ASP B 1 235 ? -7.362  19.679  -17.677 1.00 31.72 ? 235 ASP B OD2 1 
ATOM   4054 N  N   . ASP B 1 236 ? -4.354  15.728  -16.880 1.00 14.90 ? 236 ASP B N   1 
ATOM   4055 C  CA  . ASP B 1 236 ? -3.065  16.072  -16.304 1.00 13.84 ? 236 ASP B CA  1 
ATOM   4056 C  C   . ASP B 1 236 ? -1.980  15.585  -17.231 1.00 14.11 ? 236 ASP B C   1 
ATOM   4057 O  O   . ASP B 1 236 ? -1.950  14.394  -17.585 1.00 14.38 ? 236 ASP B O   1 
ATOM   4058 C  CB  . ASP B 1 236 ? -2.868  15.440  -14.889 1.00 14.99 ? 236 ASP B CB  1 
ATOM   4059 C  CG  . ASP B 1 236 ? -1.762  16.161  -14.061 1.00 15.78 ? 236 ASP B CG  1 
ATOM   4060 O  OD1 . ASP B 1 236 ? -0.625  16.301  -14.531 1.00 18.19 ? 236 ASP B OD1 1 
ATOM   4061 O  OD2 . ASP B 1 236 ? -1.943  16.454  -12.869 1.00 17.86 ? 236 ASP B OD2 1 
ATOM   4062 N  N   . PRO B 1 237 ? -1.015  16.446  -17.573 1.00 13.97 ? 237 PRO B N   1 
ATOM   4063 C  CA  . PRO B 1 237 ? 0.045   15.972  -18.444 1.00 15.07 ? 237 PRO B CA  1 
ATOM   4064 C  C   . PRO B 1 237 ? 1.150   15.129  -17.731 1.00 14.08 ? 237 PRO B C   1 
ATOM   4065 O  O   . PRO B 1 237 ? 2.100   14.664  -18.387 1.00 14.88 ? 237 PRO B O   1 
ATOM   4066 C  CB  . PRO B 1 237 ? 0.660   17.302  -18.961 1.00 15.77 ? 237 PRO B CB  1 
ATOM   4067 C  CG  . PRO B 1 237 ? 0.348   18.279  -17.827 1.00 16.10 ? 237 PRO B CG  1 
ATOM   4068 C  CD  . PRO B 1 237 ? -1.087  17.925  -17.497 1.00 14.72 ? 237 PRO B CD  1 
ATOM   4069 N  N   A SER B 1 238 ? 1.056   14.955  -16.410 0.50 13.38 ? 238 SER B N   1 
ATOM   4070 N  N   B SER B 1 238 ? 1.049   14.982  -16.404 0.50 13.18 ? 238 SER B N   1 
ATOM   4071 C  CA  A SER B 1 238 ? 1.992   14.081  -15.668 0.50 13.60 ? 238 SER B CA  1 
ATOM   4072 C  CA  B SER B 1 238 ? 1.952   14.133  -15.589 0.50 13.36 ? 238 SER B CA  1 
ATOM   4073 C  C   A SER B 1 238 ? 1.204   13.073  -14.853 0.50 12.66 ? 238 SER B C   1 
ATOM   4074 C  C   B SER B 1 238 ? 1.061   13.153  -14.825 0.50 12.49 ? 238 SER B C   1 
ATOM   4075 O  O   A SER B 1 238 ? 1.232   13.100  -13.612 0.50 13.64 ? 238 SER B O   1 
ATOM   4076 O  O   B SER B 1 238 ? 0.840   13.295  -13.610 0.50 12.99 ? 238 SER B O   1 
ATOM   4077 C  CB  A SER B 1 238 ? 2.847   14.914  -14.725 0.50 14.82 ? 238 SER B CB  1 
ATOM   4078 C  CB  B SER B 1 238 ? 2.753   15.023  -14.624 0.50 14.01 ? 238 SER B CB  1 
ATOM   4079 O  OG  A SER B 1 238 ? 3.964   14.147  -14.359 0.50 16.35 ? 238 SER B OG  1 
ATOM   4080 O  OG  B SER B 1 238 ? 3.654   15.833  -15.354 0.50 15.15 ? 238 SER B OG  1 
ATOM   4081 N  N   . PRO B 1 239 ? 0.483   12.188  -15.545 1.00 12.96 ? 239 PRO B N   1 
ATOM   4082 C  CA  . PRO B 1 239 ? -0.400  11.209  -14.842 1.00 13.15 ? 239 PRO B CA  1 
ATOM   4083 C  C   . PRO B 1 239 ? 0.361   10.367  -13.800 1.00 14.12 ? 239 PRO B C   1 
ATOM   4084 O  O   . PRO B 1 239 ? 1.543   10.071  -13.965 1.00 13.20 ? 239 PRO B O   1 
ATOM   4085 C  CB  . PRO B 1 239 ? -0.890  10.286  -15.958 1.00 16.39 ? 239 PRO B CB  1 
ATOM   4086 C  CG  . PRO B 1 239 ? -0.343  10.747  -17.229 1.00 16.68 ? 239 PRO B CG  1 
ATOM   4087 C  CD  . PRO B 1 239 ? 0.563   11.939  -17.015 1.00 13.19 ? 239 PRO B CD  1 
ATOM   4088 N  N   . ARG B 1 240 ? -0.329  10.055  -12.688 1.00 12.48 ? 240 ARG B N   1 
ATOM   4089 C  CA  . ARG B 1 240 ? 0.201   9.118   -11.710 1.00 12.38 ? 240 ARG B CA  1 
ATOM   4090 C  C   . ARG B 1 240 ? -0.837  8.021   -11.451 1.00 11.52 ? 240 ARG B C   1 
ATOM   4091 O  O   . ARG B 1 240 ? -1.996  8.355   -11.162 1.00 12.91 ? 240 ARG B O   1 
ATOM   4092 C  CB  . ARG B 1 240 ? 0.514   9.863   -10.425 1.00 12.09 ? 240 ARG B CB  1 
ATOM   4093 C  CG  . ARG B 1 240 ? 1.642   10.914  -10.635 1.00 12.32 ? 240 ARG B CG  1 
ATOM   4094 C  CD  . ARG B 1 240 ? 1.949   11.662  -9.342  1.00 12.48 ? 240 ARG B CD  1 
ATOM   4095 N  NE  . ARG B 1 240 ? 0.877   12.659  -9.079  1.00 14.47 ? 240 ARG B NE  1 
ATOM   4096 C  CZ  . ARG B 1 240 ? 0.014   12.528  -8.047  1.00 12.29 ? 240 ARG B CZ  1 
ATOM   4097 N  NH1 . ARG B 1 240 ? 0.028   11.420  -7.261  1.00 13.53 ? 240 ARG B NH1 1 
ATOM   4098 N  NH2 . ARG B 1 240 ? -0.934  13.448  -7.872  1.00 16.59 ? 240 ARG B NH2 1 
ATOM   4099 N  N   . GLU B 1 241 ? -0.480  6.761   -11.590 1.00 11.78 ? 241 GLU B N   1 
ATOM   4100 C  CA  . GLU B 1 241 ? -1.408  5.698   -11.261 1.00 11.81 ? 241 GLU B CA  1 
ATOM   4101 C  C   . GLU B 1 241 ? -1.703  5.682   -9.735  1.00 11.02 ? 241 GLU B C   1 
ATOM   4102 O  O   . GLU B 1 241 ? -0.814  5.938   -8.899  1.00 12.44 ? 241 GLU B O   1 
ATOM   4103 C  CB  . GLU B 1 241 ? -0.686  4.432   -11.584 1.00 13.58 ? 241 GLU B CB  1 
ATOM   4104 C  CG  . GLU B 1 241 ? -0.616  4.243   -13.095 1.00 14.68 ? 241 GLU B CG  1 
ATOM   4105 C  CD  . GLU B 1 241 ? 0.405   3.188   -13.446 1.00 20.18 ? 241 GLU B CD  1 
ATOM   4106 O  OE1 . GLU B 1 241 ? 1.526   3.186   -12.883 1.00 25.47 ? 241 GLU B OE1 1 
ATOM   4107 O  OE2 . GLU B 1 241 ? 0.074   2.407   -14.325 1.00 26.34 ? 241 GLU B OE2 1 
ATOM   4108 N  N   . MET B 1 242 ? -2.932  5.271   -9.374  1.00 9.68  ? 242 MET B N   1 
ATOM   4109 C  CA  . MET B 1 242 ? -3.259  5.157   -7.904  1.00 8.64  ? 242 MET B CA  1 
ATOM   4110 C  C   . MET B 1 242 ? -2.981  3.681   -7.585  1.00 9.83  ? 242 MET B C   1 
ATOM   4111 O  O   . MET B 1 242 ? -3.799  2.755   -7.860  1.00 10.13 ? 242 MET B O   1 
ATOM   4112 C  CB  . MET B 1 242 ? -4.749  5.519   -7.700  1.00 9.49  ? 242 MET B CB  1 
ATOM   4113 C  CG  . MET B 1 242 ? -5.075  5.547   -6.210  1.00 9.34  ? 242 MET B CG  1 
ATOM   4114 S  SD  . MET B 1 242 ? -6.818  5.825   -5.920  1.00 11.02 ? 242 MET B SD  1 
ATOM   4115 C  CE  . MET B 1 242 ? -6.963  7.552   -6.460  1.00 11.18 ? 242 MET B CE  1 
ATOM   4116 N  N   . ILE B 1 243 ? -1.735  3.527   -7.105  1.00 10.23 ? 243 ILE B N   1 
ATOM   4117 C  CA  . ILE B 1 243 ? -1.187  2.182   -6.761  1.00 9.73  ? 243 ILE B CA  1 
ATOM   4118 C  C   . ILE B 1 243 ? -0.460  2.318   -5.441  1.00 9.83  ? 243 ILE B C   1 
ATOM   4119 O  O   . ILE B 1 243 ? 0.028   3.431   -5.063  1.00 10.00 ? 243 ILE B O   1 
ATOM   4120 C  CB  . ILE B 1 243 ? -0.262  1.562   -7.833  1.00 11.34 ? 243 ILE B CB  1 
ATOM   4121 C  CG1 . ILE B 1 243 ? 0.833   2.604   -8.233  1.00 12.63 ? 243 ILE B CG1 1 
ATOM   4122 C  CG2 . ILE B 1 243 ? -0.967  0.998   -9.003  1.00 11.80 ? 243 ILE B CG2 1 
ATOM   4123 C  CD1 . ILE B 1 243 ? 1.896   1.947   -9.157  1.00 15.41 ? 243 ILE B CD1 1 
ATOM   4124 N  N   . ASN B 1 244 ? -0.267  1.141   -4.779  1.00 9.06  ? 244 ASN B N   1 
ATOM   4125 C  CA  . ASN B 1 244 ? 0.534   1.142   -3.525  1.00 9.44  ? 244 ASN B CA  1 
ATOM   4126 C  C   . ASN B 1 244 ? 0.137   2.242   -2.543  1.00 9.33  ? 244 ASN B C   1 
ATOM   4127 O  O   . ASN B 1 244 ? 0.978   2.885   -1.874  1.00 9.40  ? 244 ASN B O   1 
ATOM   4128 C  CB  . ASN B 1 244 ? 2.096   1.241   -3.851  1.00 10.88 ? 244 ASN B CB  1 
ATOM   4129 C  CG  . ASN B 1 244 ? 2.498   0.247   -4.898  1.00 14.64 ? 244 ASN B CG  1 
ATOM   4130 O  OD1 . ASN B 1 244 ? 2.104   -0.930  -4.860  1.00 14.22 ? 244 ASN B OD1 1 
ATOM   4131 N  ND2 . ASN B 1 244 ? 3.254   0.722   -5.896  1.00 16.88 ? 244 ASN B ND2 1 
ATOM   4132 N  N   . ASN B 1 245 ? -1.221  2.413   -2.447  1.00 7.96  ? 245 ASN B N   1 
ATOM   4133 C  CA  . ASN B 1 245 ? -1.768  3.401   -1.577  1.00 8.90  ? 245 ASN B CA  1 
ATOM   4134 C  C   . ASN B 1 245 ? -2.002  2.876   -0.149  1.00 8.86  ? 245 ASN B C   1 
ATOM   4135 O  O   . ASN B 1 245 ? -3.115  2.889   0.411   1.00 10.41 ? 245 ASN B O   1 
ATOM   4136 C  CB  . ASN B 1 245 ? -3.082  4.015   -2.158  1.00 9.01  ? 245 ASN B CB  1 
ATOM   4137 C  CG  . ASN B 1 245 ? -4.167  2.994   -2.362  1.00 9.75  ? 245 ASN B CG  1 
ATOM   4138 O  OD1 . ASN B 1 245 ? -3.967  1.790   -2.519  1.00 11.54 ? 245 ASN B OD1 1 
ATOM   4139 N  ND2 . ASN B 1 245 ? -5.416  3.518   -2.388  1.00 9.98  ? 245 ASN B ND2 1 
ATOM   4140 N  N   . PHE B 1 246 ? -0.953  2.419   0.470   1.00 8.19  ? 246 PHE B N   1 
ATOM   4141 C  CA  . PHE B 1 246 ? -1.013  2.028   1.851   1.00 7.55  ? 246 PHE B CA  1 
ATOM   4142 C  C   . PHE B 1 246 ? 0.166   2.630   2.581   1.00 8.84  ? 246 PHE B C   1 
ATOM   4143 O  O   . PHE B 1 246 ? 1.254   2.885   1.985   1.00 8.77  ? 246 PHE B O   1 
ATOM   4144 C  CB  . PHE B 1 246 ? -0.919  0.431   1.937   1.00 8.46  ? 246 PHE B CB  1 
ATOM   4145 C  CG  . PHE B 1 246 ? 0.376   -0.177  1.332   1.00 8.07  ? 246 PHE B CG  1 
ATOM   4146 C  CD1 . PHE B 1 246 ? 1.432   -0.518  2.126   1.00 9.33  ? 246 PHE B CD1 1 
ATOM   4147 C  CD2 . PHE B 1 246 ? 0.452   -0.403  -0.061  1.00 8.71  ? 246 PHE B CD2 1 
ATOM   4148 C  CE1 . PHE B 1 246 ? 2.558   -1.107  1.593   1.00 9.35  ? 246 PHE B CE1 1 
ATOM   4149 C  CE2 . PHE B 1 246 ? 1.625   -0.943  -0.642  1.00 8.99  ? 246 PHE B CE2 1 
ATOM   4150 C  CZ  . PHE B 1 246 ? 2.675   -1.271  0.225   1.00 9.31  ? 246 PHE B CZ  1 
ATOM   4151 N  N   . ARG B 1 247 ? -0.024  2.806   3.879   1.00 9.23  ? 247 ARG B N   1 
ATOM   4152 C  CA  . ARG B 1 247 ? 1.079   3.369   4.720   1.00 9.66  ? 247 ARG B CA  1 
ATOM   4153 C  C   . ARG B 1 247 ? 1.850   2.250   5.366   1.00 9.76  ? 247 ARG B C   1 
ATOM   4154 O  O   . ARG B 1 247 ? 1.277   1.177   5.671   1.00 9.72  ? 247 ARG B O   1 
ATOM   4155 C  CB  . ARG B 1 247 ? 0.501   4.196   5.838   1.00 10.91 ? 247 ARG B CB  1 
ATOM   4156 C  CG  . ARG B 1 247 ? 1.428   5.164   6.545   1.00 9.30  ? 247 ARG B CG  1 
ATOM   4157 C  CD  . ARG B 1 247 ? 0.749   5.775   7.748   1.00 9.19  ? 247 ARG B CD  1 
ATOM   4158 N  NE  . ARG B 1 247 ? 1.552   6.921   8.311   1.00 9.75  ? 247 ARG B NE  1 
ATOM   4159 C  CZ  . ARG B 1 247 ? 1.261   7.582   9.440   1.00 8.83  ? 247 ARG B CZ  1 
ATOM   4160 N  NH1 . ARG B 1 247 ? 0.156   7.295   10.109  1.00 8.58  ? 247 ARG B NH1 1 
ATOM   4161 N  NH2 . ARG B 1 247 ? 1.978   8.706   9.752   1.00 8.91  ? 247 ARG B NH2 1 
ATOM   4162 N  N   . GLN B 1 248 ? 3.179   2.410   5.526   1.00 10.00 ? 248 GLN B N   1 
ATOM   4163 C  CA  . GLN B 1 248 ? 3.903   1.432   6.318   1.00 8.43  ? 248 GLN B CA  1 
ATOM   4164 C  C   . GLN B 1 248 ? 3.434   1.316   7.747   1.00 8.37  ? 248 GLN B C   1 
ATOM   4165 O  O   . GLN B 1 248 ? 2.829   2.240   8.279   1.00 9.34  ? 248 GLN B O   1 
ATOM   4166 C  CB  . GLN B 1 248 ? 5.408   1.797   6.372   1.00 8.20  ? 248 GLN B CB  1 
ATOM   4167 C  CG  . GLN B 1 248 ? 6.053   1.778   4.970   1.00 8.80  ? 248 GLN B CG  1 
ATOM   4168 C  CD  . GLN B 1 248 ? 6.092   0.371   4.325   1.00 9.76  ? 248 GLN B CD  1 
ATOM   4169 O  OE1 . GLN B 1 248 ? 5.218   0.016   3.528   1.00 10.74 ? 248 GLN B OE1 1 
ATOM   4170 N  NE2 . GLN B 1 248 ? 7.110   -0.431  4.676   1.00 11.87 ? 248 GLN B NE2 1 
ATOM   4171 N  N   . VAL B 1 249 ? 3.628   0.145   8.351   1.00 8.51  ? 249 VAL B N   1 
ATOM   4172 C  CA  . VAL B 1 249 ? 3.219   0.024   9.774   1.00 8.78  ? 249 VAL B CA  1 
ATOM   4173 C  C   . VAL B 1 249 ? 4.061   0.903   10.679  1.00 9.49  ? 249 VAL B C   1 
ATOM   4174 O  O   . VAL B 1 249 ? 5.219   1.293   10.335  1.00 10.41 ? 249 VAL B O   1 
ATOM   4175 C  CB  . VAL B 1 249 ? 3.218   -1.432  10.277  1.00 9.00  ? 249 VAL B CB  1 
ATOM   4176 C  CG1 . VAL B 1 249 ? 2.121   -2.280  9.518   1.00 10.15 ? 249 VAL B CG1 1 
ATOM   4177 C  CG2 . VAL B 1 249 ? 4.630   -1.990  10.163  1.00 10.07 ? 249 VAL B CG2 1 
ATOM   4178 N  N   . GLN B 1 250 ? 3.476   1.253   11.814  1.00 11.64 ? 250 GLN B N   1 
ATOM   4179 C  CA  . GLN B 1 250 ? 4.027   2.237   12.747  1.00 10.91 ? 250 GLN B CA  1 
ATOM   4180 C  C   . GLN B 1 250 ? 4.543   1.625   14.038  1.00 11.83 ? 250 GLN B C   1 
ATOM   4181 O  O   . GLN B 1 250 ? 4.085   0.573   14.428  1.00 11.01 ? 250 GLN B O   1 
ATOM   4182 C  CB  . GLN B 1 250 ? 2.922   3.262   13.121  1.00 12.32 ? 250 GLN B CB  1 
ATOM   4183 C  CG  . GLN B 1 250 ? 2.267   3.850   11.888  1.00 10.59 ? 250 GLN B CG  1 
ATOM   4184 C  CD  . GLN B 1 250 ? 3.182   4.816   11.155  1.00 9.85  ? 250 GLN B CD  1 
ATOM   4185 O  OE1 . GLN B 1 250 ? 3.546   5.853   11.724  1.00 12.00 ? 250 GLN B OE1 1 
ATOM   4186 N  NE2 . GLN B 1 250 ? 3.398   4.582   9.834   1.00 9.73  ? 250 GLN B NE2 1 
ATOM   4187 N  N   . LYS B 1 251 ? 5.474   2.328   14.724  1.00 10.82 ? 251 LYS B N   1 
ATOM   4188 C  CA  . LYS B 1 251 ? 5.909   1.904   16.063  1.00 11.54 ? 251 LYS B CA  1 
ATOM   4189 C  C   . LYS B 1 251 ? 4.664   1.777   16.974  1.00 12.16 ? 251 LYS B C   1 
ATOM   4190 O  O   . LYS B 1 251 ? 3.708   2.596   16.858  1.00 10.39 ? 251 LYS B O   1 
ATOM   4191 C  CB  . LYS B 1 251 ? 6.898   2.948   16.632  1.00 11.31 ? 251 LYS B CB  1 
ATOM   4192 C  CG  . LYS B 1 251 ? 8.303   2.988   16.036  1.00 11.95 ? 251 LYS B CG  1 
ATOM   4193 C  CD  . LYS B 1 251 ? 9.045   1.734   16.463  1.00 12.32 ? 251 LYS B CD  1 
ATOM   4194 C  CE  . LYS B 1 251 ? 10.570  1.667   16.150  1.00 10.46 ? 251 LYS B CE  1 
ATOM   4195 N  NZ  . LYS B 1 251 ? 10.805  1.784   14.647  1.00 10.51 ? 251 LYS B NZ  1 
ATOM   4196 N  N   . PHE B 1 252 ? 4.715   0.813   17.922  1.00 14.88 ? 252 PHE B N   1 
ATOM   4197 C  CA  . PHE B 1 252 ? 3.633   0.666   18.816  1.00 18.03 ? 252 PHE B CA  1 
ATOM   4198 C  C   . PHE B 1 252 ? 3.466   1.732   19.876  1.00 27.80 ? 252 PHE B C   1 
ATOM   4199 O  O   . PHE B 1 252 ? 2.362   1.747   20.407  1.00 30.40 ? 252 PHE B O   1 
ATOM   4200 C  CB  . PHE B 1 252 ? 3.667   -0.719  19.437  1.00 20.95 ? 252 PHE B CB  1 
ATOM   4201 C  CG  . PHE B 1 252 ? 3.082   -1.762  18.550  1.00 27.25 ? 252 PHE B CG  1 
ATOM   4202 C  CD1 . PHE B 1 252 ? 1.730   -2.043  18.608  1.00 29.05 ? 252 PHE B CD1 1 
ATOM   4203 C  CD2 . PHE B 1 252 ? 3.865   -2.425  17.624  1.00 33.38 ? 252 PHE B CD2 1 
ATOM   4204 C  CE1 . PHE B 1 252 ? 1.175   -2.995  17.780  1.00 28.27 ? 252 PHE B CE1 1 
ATOM   4205 C  CE2 . PHE B 1 252 ? 3.318   -3.380  16.792  1.00 29.91 ? 252 PHE B CE2 1 
ATOM   4206 C  CZ  . PHE B 1 252 ? 1.969   -3.665  16.873  1.00 31.86 ? 252 PHE B CZ  1 
ATOM   4207 N  N   . ASP B 1 253 ? 4.446   2.566   20.183  1.00 27.36 ? 253 ASP B N   1 
ATOM   4208 C  CA  . ASP B 1 253 ? 4.491   3.394   21.406  1.00 30.48 ? 253 ASP B CA  1 
ATOM   4209 C  C   . ASP B 1 253 ? 3.855   2.845   22.727  1.00 30.27 ? 253 ASP B C   1 
ATOM   4210 O  O   . ASP B 1 253 ? 3.086   3.568   23.370  1.00 35.15 ? 253 ASP B O   1 
ATOM   4211 C  CB  . ASP B 1 253 ? 3.824   4.704   21.032  1.00 35.72 ? 253 ASP B CB  1 
ATOM   4212 C  CG  . ASP B 1 253 ? 4.349   5.260   19.712  1.00 44.55 ? 253 ASP B CG  1 
ATOM   4213 O  OD1 . ASP B 1 253 ? 5.561   4.969   19.412  1.00 40.72 ? 253 ASP B OD1 1 
ATOM   4214 O  OD2 . ASP B 1 253 ? 3.549   5.962   18.991  1.00 38.41 ? 253 ASP B OD2 1 
ATOM   4215 N  N   . GLU B 1 254 ? 4.210   1.614   23.144  1.00 28.96 ? 254 GLU B N   1 
ATOM   4216 C  CA  . GLU B 1 254 ? 3.672   0.958   24.384  1.00 30.71 ? 254 GLU B CA  1 
ATOM   4217 C  C   . GLU B 1 254 ? 2.181   0.498   24.302  1.00 27.70 ? 254 GLU B C   1 
ATOM   4218 O  O   . GLU B 1 254 ? 1.702   -0.125  25.250  1.00 27.84 ? 254 GLU B O   1 
ATOM   4219 C  CB  . GLU B 1 254 ? 3.883   1.846   25.635  1.00 34.41 ? 254 GLU B CB  1 
ATOM   4220 C  CG  . GLU B 1 254 ? 5.273   2.488   25.727  1.00 41.10 ? 254 GLU B CG  1 
ATOM   4221 C  CD  . GLU B 1 254 ? 6.115   1.948   26.870  1.00 50.83 ? 254 GLU B CD  1 
ATOM   4222 O  OE1 . GLU B 1 254 ? 5.542   1.760   27.970  1.00 47.92 ? 254 GLU B OE1 1 
ATOM   4223 O  OE2 . GLU B 1 254 ? 7.359   1.738   26.678  1.00 56.49 ? 254 GLU B OE2 1 
ATOM   4224 N  N   . ARG B 1 255 ? 1.478   0.771   23.221  1.00 23.72 ? 255 ARG B N   1 
ATOM   4225 C  CA  . ARG B 1 255 ? 0.135   0.288   23.070  1.00 20.24 ? 255 ARG B CA  1 
ATOM   4226 C  C   . ARG B 1 255 ? 0.015   -1.282  23.133  1.00 21.82 ? 255 ARG B C   1 
ATOM   4227 O  O   . ARG B 1 255 ? 0.914   -1.994  22.748  1.00 22.75 ? 255 ARG B O   1 
ATOM   4228 C  CB  . ARG B 1 255 ? -0.411  0.738   21.720  1.00 21.94 ? 255 ARG B CB  1 
ATOM   4229 C  CG  . ARG B 1 255 ? -0.535  2.237   21.587  1.00 25.74 ? 255 ARG B CG  1 
ATOM   4230 C  CD  . ARG B 1 255 ? -1.216  2.589   20.286  1.00 31.78 ? 255 ARG B CD  1 
ATOM   4231 N  NE  . ARG B 1 255 ? -0.184  2.775   19.291  1.00 25.93 ? 255 ARG B NE  1 
ATOM   4232 C  CZ  . ARG B 1 255 ? -0.393  3.034   17.996  1.00 22.39 ? 255 ARG B CZ  1 
ATOM   4233 N  NH1 . ARG B 1 255 ? -1.616  3.160   17.493  1.00 21.13 ? 255 ARG B NH1 1 
ATOM   4234 N  NH2 . ARG B 1 255 ? 0.645   3.177   17.187  1.00 18.28 ? 255 ARG B NH2 1 
ATOM   4235 N  N   . LEU B 1 256 ? -1.134  -1.789  23.591  1.00 18.21 ? 256 LEU B N   1 
ATOM   4236 C  CA  . LEU B 1 256 ? -1.471  -3.169  23.251  1.00 19.24 ? 256 LEU B CA  1 
ATOM   4237 C  C   . LEU B 1 256 ? -2.656  -3.133  22.253  1.00 16.64 ? 256 LEU B C   1 
ATOM   4238 O  O   . LEU B 1 256 ? -3.407  -2.139  22.146  1.00 19.65 ? 256 LEU B O   1 
ATOM   4239 C  CB  . LEU B 1 256 ? -1.849  -3.962  24.495  1.00 23.50 ? 256 LEU B CB  1 
ATOM   4240 C  CG  . LEU B 1 256 ? -0.805  -4.185  25.573  1.00 24.88 ? 256 LEU B CG  1 
ATOM   4241 C  CD1 . LEU B 1 256 ? -1.577  -4.852  26.689  1.00 25.37 ? 256 LEU B CD1 1 
ATOM   4242 C  CD2 . LEU B 1 256 ? 0.338   -5.048  25.030  1.00 26.43 ? 256 LEU B CD2 1 
ATOM   4243 N  N   . VAL B 1 257 ? -2.850  -4.263  21.616  1.00 15.02 ? 257 VAL B N   1 
ATOM   4244 C  CA  . VAL B 1 257 ? -4.024  -4.552  20.773  1.00 13.73 ? 257 VAL B CA  1 
ATOM   4245 C  C   . VAL B 1 257 ? -4.851  -5.600  21.512  1.00 12.81 ? 257 VAL B C   1 
ATOM   4246 O  O   . VAL B 1 257 ? -4.306  -6.655  21.947  1.00 14.95 ? 257 VAL B O   1 
ATOM   4247 C  CB  . VAL B 1 257 ? -3.558  -5.089  19.400  1.00 14.43 ? 257 VAL B CB  1 
ATOM   4248 C  CG1 . VAL B 1 257 ? -4.747  -5.426  18.574  1.00 13.96 ? 257 VAL B CG1 1 
ATOM   4249 C  CG2 . VAL B 1 257 ? -2.727  -4.044  18.647  1.00 14.92 ? 257 VAL B CG2 1 
ATOM   4250 N  N   . TYR B 1 258 ? -6.126  -5.276  21.779  1.00 12.43 ? 258 TYR B N   1 
ATOM   4251 C  CA  . TYR B 1 258 ? -7.024  -6.154  22.494  1.00 13.69 ? 258 TYR B CA  1 
ATOM   4252 C  C   . TYR B 1 258 ? -7.753  -7.075  21.567  1.00 12.73 ? 258 TYR B C   1 
ATOM   4253 O  O   . TYR B 1 258 ? -8.162  -6.720  20.476  1.00 12.88 ? 258 TYR B O   1 
ATOM   4254 C  CB  . TYR B 1 258 ? -7.995  -5.277  23.285  1.00 13.36 ? 258 TYR B CB  1 
ATOM   4255 C  CG  . TYR B 1 258 ? -7.170  -4.430  24.218  1.00 16.84 ? 258 TYR B CG  1 
ATOM   4256 C  CD1 . TYR B 1 258 ? -6.628  -4.979  25.418  1.00 19.69 ? 258 TYR B CD1 1 
ATOM   4257 C  CD2 . TYR B 1 258 ? -6.811  -3.136  23.861  1.00 16.58 ? 258 TYR B CD2 1 
ATOM   4258 C  CE1 . TYR B 1 258 ? -5.817  -4.203  26.237  1.00 21.04 ? 258 TYR B CE1 1 
ATOM   4259 C  CE2 . TYR B 1 258 ? -5.969  -2.375  24.650  1.00 20.52 ? 258 TYR B CE2 1 
ATOM   4260 C  CZ  . TYR B 1 258 ? -5.500  -2.898  25.861  1.00 19.71 ? 258 TYR B CZ  1 
ATOM   4261 O  OH  . TYR B 1 258 ? -4.634  -2.117  26.630  1.00 22.12 ? 258 TYR B OH  1 
ATOM   4262 N  N   . THR B 1 259 ? -7.924  -8.324  21.933  1.00 11.17 ? 259 THR B N   1 
ATOM   4263 C  CA  . THR B 1 259 ? -8.581  -9.267  20.993  1.00 11.98 ? 259 THR B CA  1 
ATOM   4264 C  C   . THR B 1 259 ? -9.894  -9.785  21.614  1.00 12.62 ? 259 THR B C   1 
ATOM   4265 O  O   . THR B 1 259 ? -9.921  -9.985  22.839  1.00 12.38 ? 259 THR B O   1 
ATOM   4266 C  CB  . THR B 1 259 ? -7.723  -10.501 20.622  1.00 12.26 ? 259 THR B CB  1 
ATOM   4267 O  OG1 . THR B 1 259 ? -7.302  -11.199 21.810  1.00 14.62 ? 259 THR B OG1 1 
ATOM   4268 C  CG2 . THR B 1 259 ? -6.452  -10.045 19.816  1.00 12.53 ? 259 THR B CG2 1 
ATOM   4269 N  N   . SER B 1 260 ? -10.936 -10.038 20.818  1.00 11.51 ? 260 SER B N   1 
ATOM   4270 C  CA  . SER B 1 260 ? -12.231 -10.639 21.293  1.00 11.09 ? 260 SER B CA  1 
ATOM   4271 C  C   . SER B 1 260 ? -12.159 -12.153 21.306  1.00 13.30 ? 260 SER B C   1 
ATOM   4272 O  O   . SER B 1 260 ? -13.160 -12.836 21.663  1.00 14.72 ? 260 SER B O   1 
ATOM   4273 C  CB  . SER B 1 260 ? -13.389 -10.184 20.420  1.00 12.31 ? 260 SER B CB  1 
ATOM   4274 O  OG  . SER B 1 260 ? -13.197 -10.722 19.137  1.00 11.35 ? 260 SER B OG  1 
ATOM   4275 N  N   . PHE B 1 261 ? -11.042 -12.687 20.852  1.00 14.23 ? 261 PHE B N   1 
ATOM   4276 C  CA  . PHE B 1 261 ? -10.845 -14.132 20.733  1.00 14.50 ? 261 PHE B CA  1 
ATOM   4277 C  C   . PHE B 1 261 ? -9.634  -14.458 21.616  1.00 17.88 ? 261 PHE B C   1 
ATOM   4278 O  O   . PHE B 1 261 ? -8.645  -13.751 21.658  1.00 14.77 ? 261 PHE B O   1 
ATOM   4279 C  CB  . PHE B 1 261 ? -10.664 -14.627 19.291  1.00 13.15 ? 261 PHE B CB  1 
ATOM   4280 C  CG  . PHE B 1 261 ? -9.633  -13.867 18.522  1.00 14.74 ? 261 PHE B CG  1 
ATOM   4281 C  CD1 . PHE B 1 261 ? -8.363  -14.355 18.418  1.00 17.03 ? 261 PHE B CD1 1 
ATOM   4282 C  CD2 . PHE B 1 261 ? -9.930  -12.610 17.982  1.00 16.28 ? 261 PHE B CD2 1 
ATOM   4283 C  CE1 . PHE B 1 261 ? -7.380  -13.664 17.709  1.00 18.21 ? 261 PHE B CE1 1 
ATOM   4284 C  CE2 . PHE B 1 261 ? -8.973  -11.927 17.247  1.00 16.37 ? 261 PHE B CE2 1 
ATOM   4285 C  CZ  . PHE B 1 261 ? -7.692  -12.412 17.131  1.00 17.48 ? 261 PHE B CZ  1 
ATOM   4286 N  N   . SER B 1 262 ? -9.749  -15.542 22.373  1.00 19.94 ? 262 SER B N   1 
ATOM   4287 C  CA  . SER B 1 262 ? -8.654  -15.904 23.239  1.00 28.41 ? 262 SER B CA  1 
ATOM   4288 C  C   . SER B 1 262 ? -7.628  -16.781 22.559  1.00 27.46 ? 262 SER B C   1 
ATOM   4289 O  O   . SER B 1 262 ? -6.458  -16.731 22.937  1.00 29.73 ? 262 SER B O   1 
ATOM   4290 C  CB  . SER B 1 262 ? -9.178  -16.545 24.517  1.00 28.94 ? 262 SER B CB  1 
ATOM   4291 O  OG  . SER B 1 262 ? -9.765  -17.784 24.157  1.00 29.86 ? 262 SER B OG  1 
ATOM   4292 N  N   . GLN B 1 263 ? -8.052  -17.628 21.614  1.00 29.38 ? 263 GLN B N   1 
ATOM   4293 C  CA  . GLN B 1 263 ? -7.129  -18.492 20.841  1.00 26.63 ? 263 GLN B CA  1 
ATOM   4294 C  C   . GLN B 1 263 ? -7.677  -18.647 19.425  1.00 25.94 ? 263 GLN B C   1 
ATOM   4295 O  O   . GLN B 1 263 ? -6.944  -19.122 18.504  1.00 28.92 ? 263 GLN B O   1 
ATOM   4296 C  CB  . GLN B 1 263 ? -6.909  -19.875 21.501  1.00 28.89 ? 263 GLN B CB  1 
ATOM   4297 C  CG  . GLN B 1 263 ? -8.149  -20.362 22.201  1.00 33.53 ? 263 GLN B CG  1 
ATOM   4298 C  CD  . GLN B 1 263 ? -8.019  -21.786 22.703  1.00 36.83 ? 263 GLN B CD  1 
ATOM   4299 O  OE1 . GLN B 1 263 ? -7.342  -22.614 22.091  1.00 38.75 ? 263 GLN B OE1 1 
ATOM   4300 N  NE2 . GLN B 1 263 ? -8.695  -22.085 23.799  1.00 35.12 ? 263 GLN B NE2 1 
ATOM   4301 O  OXT . GLN B 1 263 ? -8.822  -18.211 19.207  1.00 21.99 ? 263 GLN B OXT 1 
ATOM   4302 N  N   . LYS C 1 3   ? 33.384  17.458  -23.947 1.00 46.06 ? 3   LYS C N   1 
ATOM   4303 C  CA  . LYS C 1 3   ? 32.638  18.071  -25.079 1.00 50.11 ? 3   LYS C CA  1 
ATOM   4304 C  C   . LYS C 1 3   ? 31.512  17.108  -25.464 1.00 48.10 ? 3   LYS C C   1 
ATOM   4305 O  O   . LYS C 1 3   ? 30.355  17.294  -25.071 1.00 51.37 ? 3   LYS C O   1 
ATOM   4306 C  CB  . LYS C 1 3   ? 33.584  18.299  -26.276 1.00 58.99 ? 3   LYS C CB  1 
ATOM   4307 C  CG  . LYS C 1 3   ? 33.115  19.369  -27.255 1.00 66.19 ? 3   LYS C CG  1 
ATOM   4308 C  CD  . LYS C 1 3   ? 33.322  20.775  -26.685 1.00 67.77 ? 3   LYS C CD  1 
ATOM   4309 C  CE  . LYS C 1 3   ? 32.505  21.836  -27.421 1.00 68.33 ? 3   LYS C CE  1 
ATOM   4310 N  NZ  . LYS C 1 3   ? 32.925  23.225  -27.055 1.00 62.24 ? 3   LYS C NZ  1 
ATOM   4311 N  N   . TRP C 1 4   ? 31.897  16.070  -26.208 1.00 35.85 ? 4   TRP C N   1 
ATOM   4312 C  CA  . TRP C 1 4   ? 31.014  14.991  -26.655 1.00 25.39 ? 4   TRP C CA  1 
ATOM   4313 C  C   . TRP C 1 4   ? 30.940  13.845  -25.663 1.00 24.57 ? 4   TRP C C   1 
ATOM   4314 O  O   . TRP C 1 4   ? 31.883  13.582  -24.913 1.00 24.89 ? 4   TRP C O   1 
ATOM   4315 C  CB  . TRP C 1 4   ? 31.460  14.489  -28.068 1.00 20.48 ? 4   TRP C CB  1 
ATOM   4316 C  CG  . TRP C 1 4   ? 32.797  13.861  -28.116 1.00 18.31 ? 4   TRP C CG  1 
ATOM   4317 C  CD1 . TRP C 1 4   ? 34.040  14.482  -28.226 1.00 18.11 ? 4   TRP C CD1 1 
ATOM   4318 C  CD2 . TRP C 1 4   ? 33.106  12.430  -27.984 1.00 15.06 ? 4   TRP C CD2 1 
ATOM   4319 N  NE1 . TRP C 1 4   ? 35.045  13.568  -28.238 1.00 18.56 ? 4   TRP C NE1 1 
ATOM   4320 C  CE2 . TRP C 1 4   ? 34.538  12.295  -28.106 1.00 17.66 ? 4   TRP C CE2 1 
ATOM   4321 C  CE3 . TRP C 1 4   ? 32.325  11.251  -27.837 1.00 16.34 ? 4   TRP C CE3 1 
ATOM   4322 C  CZ2 . TRP C 1 4   ? 35.174  11.043  -28.035 1.00 16.19 ? 4   TRP C CZ2 1 
ATOM   4323 C  CZ3 . TRP C 1 4   ? 32.967  9.988   -27.784 1.00 14.86 ? 4   TRP C CZ3 1 
ATOM   4324 C  CH2 . TRP C 1 4   ? 34.365  9.874   -27.882 1.00 16.58 ? 4   TRP C CH2 1 
ATOM   4325 N  N   . THR C 1 5   ? 29.828  13.113  -25.721 1.00 24.23 ? 5   THR C N   1 
ATOM   4326 C  CA  . THR C 1 5   ? 29.584  11.937  -24.864 1.00 24.13 ? 5   THR C CA  1 
ATOM   4327 C  C   . THR C 1 5   ? 28.918  10.820  -25.656 1.00 24.78 ? 5   THR C C   1 
ATOM   4328 O  O   . THR C 1 5   ? 28.590  10.968  -26.860 1.00 24.83 ? 5   THR C O   1 
ATOM   4329 C  CB  . THR C 1 5   ? 28.582  12.291  -23.726 1.00 23.10 ? 5   THR C CB  1 
ATOM   4330 O  OG1 . THR C 1 5   ? 27.286  12.582  -24.289 1.00 23.02 ? 5   THR C OG1 1 
ATOM   4331 C  CG2 . THR C 1 5   ? 29.076  13.572  -23.035 1.00 27.36 ? 5   THR C CG2 1 
ATOM   4332 N  N   . TYR C 1 6   ? 28.684  9.704   -24.968 1.00 26.78 ? 6   TYR C N   1 
ATOM   4333 C  CA  . TYR C 1 6   ? 27.749  8.663   -25.454 1.00 27.37 ? 6   TYR C CA  1 
ATOM   4334 C  C   . TYR C 1 6   ? 26.302  8.669   -24.899 1.00 31.12 ? 6   TYR C C   1 
ATOM   4335 O  O   . TYR C 1 6   ? 25.633  7.669   -25.048 1.00 33.22 ? 6   TYR C O   1 
ATOM   4336 C  CB  . TYR C 1 6   ? 28.369  7.256   -25.311 1.00 22.71 ? 6   TYR C CB  1 
ATOM   4337 C  CG  . TYR C 1 6   ? 29.653  6.972   -26.053 1.00 23.13 ? 6   TYR C CG  1 
ATOM   4338 C  CD1 . TYR C 1 6   ? 30.888  7.141   -25.438 1.00 21.26 ? 6   TYR C CD1 1 
ATOM   4339 C  CD2 . TYR C 1 6   ? 29.634  6.455   -27.371 1.00 19.61 ? 6   TYR C CD2 1 
ATOM   4340 C  CE1 . TYR C 1 6   ? 32.062  6.813   -26.046 1.00 20.27 ? 6   TYR C CE1 1 
ATOM   4341 C  CE2 . TYR C 1 6   ? 30.802  6.105   -28.005 1.00 19.91 ? 6   TYR C CE2 1 
ATOM   4342 C  CZ  . TYR C 1 6   ? 32.003  6.331   -27.390 1.00 19.83 ? 6   TYR C CZ  1 
ATOM   4343 O  OH  . TYR C 1 6   ? 33.109  5.980   -28.026 1.00 21.14 ? 6   TYR C OH  1 
ATOM   4344 N  N   . PHE C 1 7   ? 25.835  9.754   -24.288 1.00 36.85 ? 7   PHE C N   1 
ATOM   4345 C  CA  . PHE C 1 7   ? 24.498  9.731   -23.669 1.00 44.30 ? 7   PHE C CA  1 
ATOM   4346 C  C   . PHE C 1 7   ? 23.500  10.897  -23.793 1.00 47.20 ? 7   PHE C C   1 
ATOM   4347 O  O   . PHE C 1 7   ? 22.536  10.791  -24.548 1.00 51.92 ? 7   PHE C O   1 
ATOM   4348 C  CB  . PHE C 1 7   ? 24.605  9.375   -22.182 1.00 51.03 ? 7   PHE C CB  1 
ATOM   4349 C  CG  . PHE C 1 7   ? 25.177  10.474  -21.338 1.00 55.41 ? 7   PHE C CG  1 
ATOM   4350 C  CD1 . PHE C 1 7   ? 24.359  11.470  -20.829 1.00 57.06 ? 7   PHE C CD1 1 
ATOM   4351 C  CD2 . PHE C 1 7   ? 26.527  10.510  -21.052 1.00 55.42 ? 7   PHE C CD2 1 
ATOM   4352 C  CE1 . PHE C 1 7   ? 24.885  12.487  -20.052 1.00 54.67 ? 7   PHE C CE1 1 
ATOM   4353 C  CE2 . PHE C 1 7   ? 27.059  11.516  -20.274 1.00 54.68 ? 7   PHE C CE2 1 
ATOM   4354 C  CZ  . PHE C 1 7   ? 26.238  12.509  -19.771 1.00 54.76 ? 7   PHE C CZ  1 
ATOM   4355 N  N   . GLY C 1 8   ? 23.720  11.967  -23.026 1.00 44.16 ? 8   GLY C N   1 
ATOM   4356 C  CA  . GLY C 1 8   ? 22.797  13.102  -22.946 1.00 35.40 ? 8   GLY C CA  1 
ATOM   4357 C  C   . GLY C 1 8   ? 22.913  13.876  -24.246 1.00 39.83 ? 8   GLY C C   1 
ATOM   4358 O  O   . GLY C 1 8   ? 23.537  13.354  -25.241 1.00 40.45 ? 8   GLY C O   1 
ATOM   4359 N  N   . PRO C 1 9   ? 22.379  15.097  -24.320 1.00 37.92 ? 9   PRO C N   1 
ATOM   4360 C  CA  . PRO C 1 9   ? 22.317  15.925  -25.545 1.00 37.37 ? 9   PRO C CA  1 
ATOM   4361 C  C   . PRO C 1 9   ? 23.633  16.057  -26.301 1.00 33.78 ? 9   PRO C C   1 
ATOM   4362 O  O   . PRO C 1 9   ? 23.666  16.655  -27.390 1.00 33.61 ? 9   PRO C O   1 
ATOM   4363 C  CB  . PRO C 1 9   ? 21.910  17.318  -25.009 1.00 41.27 ? 9   PRO C CB  1 
ATOM   4364 C  CG  . PRO C 1 9   ? 22.414  17.346  -23.581 1.00 39.81 ? 9   PRO C CG  1 
ATOM   4365 C  CD  . PRO C 1 9   ? 22.367  15.915  -23.077 1.00 40.25 ? 9   PRO C CD  1 
ATOM   4366 N  N   . ASP C 1 10  ? 24.714  15.576  -25.702 1.00 30.77 ? 10  ASP C N   1 
ATOM   4367 C  CA  . ASP C 1 10  ? 26.010  15.618  -26.364 1.00 31.49 ? 10  ASP C CA  1 
ATOM   4368 C  C   . ASP C 1 10  ? 26.411  14.290  -26.995 1.00 24.92 ? 10  ASP C C   1 
ATOM   4369 O  O   . ASP C 1 10  ? 27.618  14.157  -27.419 1.00 24.97 ? 10  ASP C O   1 
ATOM   4370 C  CB  . ASP C 1 10  ? 27.092  16.128  -25.398 1.00 32.27 ? 10  ASP C CB  1 
ATOM   4371 C  CG  . ASP C 1 10  ? 26.858  17.599  -25.027 1.00 42.75 ? 10  ASP C CG  1 
ATOM   4372 O  OD1 . ASP C 1 10  ? 26.709  18.456  -25.959 1.00 36.30 ? 10  ASP C OD1 1 
ATOM   4373 O  OD2 . ASP C 1 10  ? 26.768  17.873  -23.807 1.00 41.48 ? 10  ASP C OD2 1 
ATOM   4374 N  N   . GLY C 1 11  ? 25.412  13.361  -27.041 1.00 26.39 ? 11  GLY C N   1 
ATOM   4375 C  CA  . GLY C 1 11  ? 25.514  11.941  -27.497 1.00 18.41 ? 11  GLY C CA  1 
ATOM   4376 C  C   . GLY C 1 11  ? 25.689  11.831  -29.024 1.00 15.63 ? 11  GLY C C   1 
ATOM   4377 O  O   . GLY C 1 11  ? 25.701  12.846  -29.745 1.00 16.12 ? 11  GLY C O   1 
ATOM   4378 N  N   . GLU C 1 12  ? 25.801  10.596  -29.501 1.00 12.87 ? 12  GLU C N   1 
ATOM   4379 C  CA  . GLU C 1 12  ? 26.210  10.363  -30.886 1.00 12.34 ? 12  GLU C CA  1 
ATOM   4380 C  C   . GLU C 1 12  ? 25.370  11.053  -31.956 1.00 12.12 ? 12  GLU C C   1 
ATOM   4381 O  O   . GLU C 1 12  ? 25.929  11.381  -33.000 1.00 11.10 ? 12  GLU C O   1 
ATOM   4382 C  CB  . GLU C 1 12  ? 26.420  8.846   -31.094 1.00 12.82 ? 12  GLU C CB  1 
ATOM   4383 C  CG  . GLU C 1 12  ? 25.118  8.093   -31.276 1.00 12.13 ? 12  GLU C CG  1 
ATOM   4384 C  CD  . GLU C 1 12  ? 25.393  6.604   -31.049 1.00 13.70 ? 12  GLU C CD  1 
ATOM   4385 O  OE1 . GLU C 1 12  ? 25.612  5.895   -32.039 1.00 12.92 ? 12  GLU C OE1 1 
ATOM   4386 O  OE2 . GLU C 1 12  ? 25.411  6.154   -29.860 1.00 15.44 ? 12  GLU C OE2 1 
ATOM   4387 N  N   . ASN C 1 13  ? 24.048  11.221  -31.805 1.00 11.30 ? 13  ASN C N   1 
ATOM   4388 C  CA  . ASN C 1 13  ? 23.301  11.815  -32.908 1.00 11.32 ? 13  ASN C CA  1 
ATOM   4389 C  C   . ASN C 1 13  ? 23.623  13.301  -33.047 1.00 11.07 ? 13  ASN C C   1 
ATOM   4390 O  O   . ASN C 1 13  ? 23.293  13.870  -34.096 1.00 13.15 ? 13  ASN C O   1 
ATOM   4391 C  CB  . ASN C 1 13  ? 21.850  11.698  -32.550 1.00 11.57 ? 13  ASN C CB  1 
ATOM   4392 C  CG  . ASN C 1 13  ? 21.365  10.268  -32.650 1.00 12.95 ? 13  ASN C CG  1 
ATOM   4393 O  OD1 . ASN C 1 13  ? 22.056  9.365   -33.145 1.00 14.94 ? 13  ASN C OD1 1 
ATOM   4394 N  ND2 . ASN C 1 13  ? 20.135  10.055  -32.207 1.00 11.11 ? 13  ASN C ND2 1 
ATOM   4395 N  N   A SER C 1 14  ? 24.238  13.861  -31.999 0.50 12.46 ? 14  SER C N   1 
ATOM   4396 N  N   B SER C 1 14  ? 24.241  13.903  -32.019 0.50 12.96 ? 14  SER C N   1 
ATOM   4397 C  CA  A SER C 1 14  ? 24.611  15.266  -31.998 0.50 12.32 ? 14  SER C CA  1 
ATOM   4398 C  CA  B SER C 1 14  ? 24.624  15.327  -32.098 0.50 12.94 ? 14  SER C CA  1 
ATOM   4399 C  C   A SER C 1 14  ? 26.032  15.528  -32.475 0.50 11.85 ? 14  SER C C   1 
ATOM   4400 C  C   B SER C 1 14  ? 26.111  15.547  -32.321 0.50 12.56 ? 14  SER C C   1 
ATOM   4401 O  O   A SER C 1 14  ? 26.362  16.699  -32.810 0.50 11.12 ? 14  SER C O   1 
ATOM   4402 O  O   B SER C 1 14  ? 26.589  16.696  -32.283 0.50 12.17 ? 14  SER C O   1 
ATOM   4403 C  CB  A SER C 1 14  ? 24.346  15.862  -30.602 0.50 13.47 ? 14  SER C CB  1 
ATOM   4404 C  CB  B SER C 1 14  ? 24.229  16.044  -30.804 0.50 14.52 ? 14  SER C CB  1 
ATOM   4405 O  OG  A SER C 1 14  ? 22.944  16.058  -30.426 0.50 13.41 ? 14  SER C OG  1 
ATOM   4406 O  OG  B SER C 1 14  ? 25.116  15.633  -29.791 0.50 15.61 ? 14  SER C OG  1 
ATOM   4407 N  N   . TRP C 1 15  ? 26.868  14.496  -32.504 1.00 12.41 ? 15  TRP C N   1 
ATOM   4408 C  CA  . TRP C 1 15  ? 28.290  14.674  -32.905 1.00 12.76 ? 15  TRP C CA  1 
ATOM   4409 C  C   . TRP C 1 15  ? 28.515  15.546  -34.118 1.00 12.74 ? 15  TRP C C   1 
ATOM   4410 O  O   . TRP C 1 15  ? 29.498  16.340  -34.162 1.00 13.78 ? 15  TRP C O   1 
ATOM   4411 C  CB  . TRP C 1 15  ? 29.009  13.355  -33.078 1.00 11.65 ? 15  TRP C CB  1 
ATOM   4412 C  CG  . TRP C 1 15  ? 29.177  12.531  -31.844 1.00 11.49 ? 15  TRP C CG  1 
ATOM   4413 C  CD1 . TRP C 1 15  ? 28.935  12.885  -30.520 1.00 11.75 ? 15  TRP C CD1 1 
ATOM   4414 C  CD2 . TRP C 1 15  ? 29.648  11.158  -31.798 1.00 11.99 ? 15  TRP C CD2 1 
ATOM   4415 N  NE1 . TRP C 1 15  ? 29.219  11.836  -29.682 1.00 12.23 ? 15  TRP C NE1 1 
ATOM   4416 C  CE2 . TRP C 1 15  ? 29.653  10.768  -30.390 1.00 12.24 ? 15  TRP C CE2 1 
ATOM   4417 C  CE3 . TRP C 1 15  ? 30.051  10.244  -32.752 1.00 11.27 ? 15  TRP C CE3 1 
ATOM   4418 C  CZ2 . TRP C 1 15  ? 30.049  9.510   -29.984 1.00 13.05 ? 15  TRP C CZ2 1 
ATOM   4419 C  CZ3 . TRP C 1 15  ? 30.449  8.980   -32.334 1.00 10.73 ? 15  TRP C CZ3 1 
ATOM   4420 C  CH2 . TRP C 1 15  ? 30.447  8.622   -30.983 1.00 12.03 ? 15  TRP C CH2 1 
ATOM   4421 N  N   . SER C 1 16  ? 27.640  15.415  -35.111 1.00 11.89 ? 16  SER C N   1 
ATOM   4422 C  CA  . SER C 1 16  ? 27.867  15.991  -36.438 1.00 12.10 ? 16  SER C CA  1 
ATOM   4423 C  C   . SER C 1 16  ? 27.775  17.528  -36.356 1.00 13.98 ? 16  SER C C   1 
ATOM   4424 O  O   . SER C 1 16  ? 28.174  18.198  -37.285 1.00 15.28 ? 16  SER C O   1 
ATOM   4425 C  CB  . SER C 1 16  ? 26.846  15.450  -37.413 1.00 12.90 ? 16  SER C CB  1 
ATOM   4426 O  OG  . SER C 1 16  ? 25.519  15.820  -37.001 1.00 13.81 ? 16  SER C OG  1 
ATOM   4427 N  N   A LYS C 1 17  ? 27.232  18.067  -35.269 0.50 14.19 ? 17  LYS C N   1 
ATOM   4428 N  N   B LYS C 1 17  ? 27.291  18.054  -35.226 0.50 14.68 ? 17  LYS C N   1 
ATOM   4429 C  CA  A LYS C 1 17  ? 27.199  19.554  -35.146 0.50 12.98 ? 17  LYS C CA  1 
ATOM   4430 C  CA  B LYS C 1 17  ? 27.160  19.539  -35.106 0.50 13.86 ? 17  LYS C CA  1 
ATOM   4431 C  C   A LYS C 1 17  ? 28.657  20.071  -35.179 0.50 12.84 ? 17  LYS C C   1 
ATOM   4432 C  C   B LYS C 1 17  ? 28.528  20.210  -35.015 0.50 14.02 ? 17  LYS C C   1 
ATOM   4433 O  O   A LYS C 1 17  ? 29.085  20.856  -36.067 0.50 12.21 ? 17  LYS C O   1 
ATOM   4434 O  O   B LYS C 1 17  ? 28.722  21.283  -35.632 0.50 14.68 ? 17  LYS C O   1 
ATOM   4435 C  CB  A LYS C 1 17  ? 26.477  19.963  -33.860 0.50 12.56 ? 17  LYS C CB  1 
ATOM   4436 C  CB  B LYS C 1 17  ? 26.258  19.953  -33.943 0.50 13.69 ? 17  LYS C CB  1 
ATOM   4437 C  CG  A LYS C 1 17  ? 24.985  19.575  -33.763 0.50 14.58 ? 17  LYS C CG  1 
ATOM   4438 C  CG  B LYS C 1 17  ? 24.740  19.874  -34.222 0.50 15.33 ? 17  LYS C CG  1 
ATOM   4439 C  CD  A LYS C 1 17  ? 24.469  19.632  -32.314 0.50 14.13 ? 17  LYS C CD  1 
ATOM   4440 C  CD  B LYS C 1 17  ? 23.924  19.967  -32.943 0.50 16.74 ? 17  LYS C CD  1 
ATOM   4441 C  CE  A LYS C 1 17  ? 23.040  19.098  -32.117 0.50 15.69 ? 17  LYS C CE  1 
ATOM   4442 C  CE  B LYS C 1 17  ? 24.236  21.263  -32.218 0.50 17.20 ? 17  LYS C CE  1 
ATOM   4443 N  NZ  A LYS C 1 17  ? 22.647  19.367  -30.684 0.50 16.10 ? 17  LYS C NZ  1 
ATOM   4444 N  NZ  B LYS C 1 17  ? 23.042  21.903  -31.607 0.50 17.15 ? 17  LYS C NZ  1 
ATOM   4445 N  N   . LYS C 1 18  ? 29.431  19.626  -34.219 1.00 13.42 ? 18  LYS C N   1 
ATOM   4446 C  CA  . LYS C 1 18  ? 30.820  20.118  -34.096 1.00 16.57 ? 18  LYS C CA  1 
ATOM   4447 C  C   . LYS C 1 18  ? 31.772  19.318  -34.946 1.00 15.92 ? 18  LYS C C   1 
ATOM   4448 O  O   . LYS C 1 18  ? 32.847  19.792  -35.244 1.00 18.02 ? 18  LYS C O   1 
ATOM   4449 C  CB  . LYS C 1 18  ? 31.285  20.212  -32.639 1.00 19.74 ? 18  LYS C CB  1 
ATOM   4450 C  CG  . LYS C 1 18  ? 30.531  21.199  -31.718 1.00 28.86 ? 18  LYS C CG  1 
ATOM   4451 C  CD  . LYS C 1 18  ? 30.936  22.657  -31.977 1.00 31.76 ? 18  LYS C CD  1 
ATOM   4452 C  CE  . LYS C 1 18  ? 30.864  23.524  -30.736 1.00 36.97 ? 18  LYS C CE  1 
ATOM   4453 N  NZ  . LYS C 1 18  ? 31.902  24.590  -30.844 1.00 43.22 ? 18  LYS C NZ  1 
ATOM   4454 N  N   . TYR C 1 19  ? 31.411  18.069  -35.329 1.00 15.96 ? 19  TYR C N   1 
ATOM   4455 C  CA  . TYR C 1 19  ? 32.319  17.254  -36.074 1.00 13.68 ? 19  TYR C CA  1 
ATOM   4456 C  C   . TYR C 1 19  ? 31.617  16.819  -37.355 1.00 13.26 ? 19  TYR C C   1 
ATOM   4457 O  O   . TYR C 1 19  ? 31.018  15.720  -37.377 1.00 13.98 ? 19  TYR C O   1 
ATOM   4458 C  CB  . TYR C 1 19  ? 32.684  16.021  -35.202 1.00 13.39 ? 19  TYR C CB  1 
ATOM   4459 C  CG  . TYR C 1 19  ? 33.323  16.406  -33.868 1.00 15.74 ? 19  TYR C CG  1 
ATOM   4460 C  CD1 . TYR C 1 19  ? 34.691  16.716  -33.792 1.00 15.98 ? 19  TYR C CD1 1 
ATOM   4461 C  CD2 . TYR C 1 19  ? 32.550  16.514  -32.703 1.00 16.67 ? 19  TYR C CD2 1 
ATOM   4462 C  CE1 . TYR C 1 19  ? 35.267  17.069  -32.584 1.00 18.20 ? 19  TYR C CE1 1 
ATOM   4463 C  CE2 . TYR C 1 19  ? 33.128  16.869  -31.498 1.00 17.31 ? 19  TYR C CE2 1 
ATOM   4464 C  CZ  . TYR C 1 19  ? 34.482  17.136  -31.435 1.00 18.80 ? 19  TYR C CZ  1 
ATOM   4465 O  OH  . TYR C 1 19  ? 35.119  17.489  -30.217 1.00 21.66 ? 19  TYR C OH  1 
ATOM   4466 N  N   . PRO C 1 20  ? 31.694  17.591  -38.428 1.00 13.59 ? 20  PRO C N   1 
ATOM   4467 C  CA  . PRO C 1 20  ? 30.843  17.399  -39.584 1.00 13.49 ? 20  PRO C CA  1 
ATOM   4468 C  C   . PRO C 1 20  ? 31.059  16.008  -40.191 1.00 11.35 ? 20  PRO C C   1 
ATOM   4469 O  O   . PRO C 1 20  ? 30.112  15.554  -40.817 1.00 12.90 ? 20  PRO C O   1 
ATOM   4470 C  CB  . PRO C 1 20  ? 31.280  18.475  -40.591 1.00 14.45 ? 20  PRO C CB  1 
ATOM   4471 C  CG  . PRO C 1 20  ? 31.978  19.467  -39.743 1.00 16.60 ? 20  PRO C CG  1 
ATOM   4472 C  CD  . PRO C 1 20  ? 32.480  18.835  -38.501 1.00 13.61 ? 20  PRO C CD  1 
ATOM   4473 N  N   . SER C 1 21  ? 32.241  15.414  -40.142 1.00 12.09 ? 21  SER C N   1 
ATOM   4474 C  CA  . SER C 1 21  ? 32.459  14.075  -40.692 1.00 11.13 ? 21  SER C CA  1 
ATOM   4475 C  C   . SER C 1 21  ? 31.601  12.982  -40.090 1.00 11.69 ? 21  SER C C   1 
ATOM   4476 O  O   . SER C 1 21  ? 31.300  12.048  -40.738 1.00 13.92 ? 21  SER C O   1 
ATOM   4477 C  CB  . SER C 1 21  ? 33.951  13.657  -40.618 1.00 10.94 ? 21  SER C CB  1 
ATOM   4478 O  OG  . SER C 1 21  ? 34.609  14.482  -41.544 1.00 14.33 ? 21  SER C OG  1 
ATOM   4479 N  N   . CYS C 1 22  ? 31.088  13.216  -38.884 1.00 11.95 ? 22  CYS C N   1 
ATOM   4480 C  CA  . CYS C 1 22  ? 30.160  12.247  -38.217 1.00 12.30 ? 22  CYS C CA  1 
ATOM   4481 C  C   . CYS C 1 22  ? 28.842  12.086  -38.964 1.00 12.76 ? 22  CYS C C   1 
ATOM   4482 O  O   . CYS C 1 22  ? 28.222  10.993  -38.805 1.00 12.79 ? 22  CYS C O   1 
ATOM   4483 C  CB  . CYS C 1 22  ? 29.979  12.599  -36.714 1.00 11.75 ? 22  CYS C CB  1 
ATOM   4484 S  SG  . CYS C 1 22  ? 31.531  12.616  -35.768 1.00 13.79 ? 22  CYS C SG  1 
ATOM   4485 N  N   . GLY C 1 23  ? 28.458  12.980  -39.855 1.00 12.33 ? 23  GLY C N   1 
ATOM   4486 C  CA  . GLY C 1 23  ? 27.228  12.858  -40.676 1.00 12.04 ? 23  GLY C CA  1 
ATOM   4487 C  C   . GLY C 1 23  ? 27.630  12.621  -42.113 1.00 12.10 ? 23  GLY C C   1 
ATOM   4488 O  O   . GLY C 1 23  ? 26.795  12.715  -43.000 1.00 13.68 ? 23  GLY C O   1 
ATOM   4489 N  N   . GLY C 1 24  ? 28.916  12.329  -42.390 1.00 12.90 ? 24  GLY C N   1 
ATOM   4490 C  CA  . GLY C 1 24  ? 29.339  12.206  -43.799 1.00 12.90 ? 24  GLY C CA  1 
ATOM   4491 C  C   . GLY C 1 24  ? 29.458  10.772  -44.265 1.00 14.12 ? 24  GLY C C   1 
ATOM   4492 O  O   . GLY C 1 24  ? 28.770  9.888   -43.713 1.00 13.93 ? 24  GLY C O   1 
ATOM   4493 N  N   . LEU C 1 25  ? 30.269  10.514  -45.284 1.00 13.14 ? 25  LEU C N   1 
ATOM   4494 C  CA  . LEU C 1 25  ? 30.313  9.161   -45.859 1.00 15.08 ? 25  LEU C CA  1 
ATOM   4495 C  C   . LEU C 1 25  ? 31.214  8.228   -45.027 1.00 14.08 ? 25  LEU C C   1 
ATOM   4496 O  O   . LEU C 1 25  ? 32.066  8.681   -44.210 1.00 14.04 ? 25  LEU C O   1 
ATOM   4497 C  CB  . LEU C 1 25  ? 30.890  9.242   -47.300 1.00 19.04 ? 25  LEU C CB  1 
ATOM   4498 C  CG  . LEU C 1 25  ? 30.095  10.186  -48.209 1.00 21.78 ? 25  LEU C CG  1 
ATOM   4499 C  CD1 . LEU C 1 25  ? 30.773  10.322  -49.565 1.00 26.52 ? 25  LEU C CD1 1 
ATOM   4500 C  CD2 . LEU C 1 25  ? 28.692  9.603   -48.349 1.00 27.13 ? 25  LEU C CD2 1 
ATOM   4501 N  N   . LEU C 1 26  ? 31.116  6.937   -45.392 1.00 14.90 ? 26  LEU C N   1 
ATOM   4502 C  CA  . LEU C 1 26  ? 32.040  5.863   -44.954 1.00 14.01 ? 26  LEU C CA  1 
ATOM   4503 C  C   . LEU C 1 26  ? 32.068  5.714   -43.437 1.00 11.99 ? 26  LEU C C   1 
ATOM   4504 O  O   . LEU C 1 26  ? 33.088  5.312   -42.875 1.00 13.68 ? 26  LEU C O   1 
ATOM   4505 C  CB  . LEU C 1 26  ? 33.512  5.988   -45.450 1.00 14.75 ? 26  LEU C CB  1 
ATOM   4506 C  CG  . LEU C 1 26  ? 33.923  5.944   -46.923 1.00 20.25 ? 26  LEU C CG  1 
ATOM   4507 C  CD1 . LEU C 1 26  ? 35.453  5.855   -47.044 1.00 18.10 ? 26  LEU C CD1 1 
ATOM   4508 C  CD2 . LEU C 1 26  ? 33.210  4.877   -47.683 1.00 20.01 ? 26  LEU C CD2 1 
ATOM   4509 N  N   . GLN C 1 27  ? 30.941  5.978   -42.771 1.00 10.40 ? 27  GLN C N   1 
ATOM   4510 C  CA  . GLN C 1 27  ? 30.945  5.828   -41.296 1.00 9.74  ? 27  GLN C CA  1 
ATOM   4511 C  C   . GLN C 1 27  ? 30.913  4.338   -40.768 1.00 9.25  ? 27  GLN C C   1 
ATOM   4512 O  O   . GLN C 1 27  ? 30.280  3.471   -41.349 1.00 12.04 ? 27  GLN C O   1 
ATOM   4513 C  CB  . GLN C 1 27  ? 29.764  6.588   -40.687 1.00 10.40 ? 27  GLN C CB  1 
ATOM   4514 C  CG  . GLN C 1 27  ? 29.813  8.106   -40.970 1.00 10.11 ? 27  GLN C CG  1 
ATOM   4515 C  CD  . GLN C 1 27  ? 31.019  8.780   -40.296 1.00 9.89  ? 27  GLN C CD  1 
ATOM   4516 O  OE1 . GLN C 1 27  ? 31.031  8.980   -39.058 1.00 10.68 ? 27  GLN C OE1 1 
ATOM   4517 N  NE2 . GLN C 1 27  ? 32.048  9.044   -41.072 1.00 9.97  ? 27  GLN C NE2 1 
ATOM   4518 N  N   . SER C 1 28  ? 31.646  4.120   -39.659 1.00 9.03  ? 28  SER C N   1 
ATOM   4519 C  CA  . SER C 1 28  ? 31.737  2.806   -38.954 1.00 8.98  ? 28  SER C CA  1 
ATOM   4520 C  C   . SER C 1 28  ? 31.163  3.073   -37.552 1.00 10.40 ? 28  SER C C   1 
ATOM   4521 O  O   . SER C 1 28  ? 31.042  4.213   -37.093 1.00 9.88  ? 28  SER C O   1 
ATOM   4522 C  CB  . SER C 1 28  ? 33.251  2.529   -38.747 1.00 8.83  ? 28  SER C CB  1 
ATOM   4523 O  OG  . SER C 1 28  ? 33.832  2.373   -40.044 1.00 9.54  ? 28  SER C OG  1 
ATOM   4524 N  N   . PRO C 1 29  ? 30.855  2.069   -36.834 1.00 9.56  ? 29  PRO C N   1 
ATOM   4525 C  CA  . PRO C 1 29  ? 31.011  0.657   -37.194 1.00 8.88  ? 29  PRO C CA  1 
ATOM   4526 C  C   . PRO C 1 29  ? 29.749  0.211   -37.980 1.00 10.46 ? 29  PRO C C   1 
ATOM   4527 O  O   . PRO C 1 29  ? 28.822  0.973   -38.252 1.00 11.58 ? 29  PRO C O   1 
ATOM   4528 C  CB  . PRO C 1 29  ? 30.967  -0.018  -35.822 1.00 10.49 ? 29  PRO C CB  1 
ATOM   4529 C  CG  . PRO C 1 29  ? 29.880  0.737   -35.126 1.00 11.26 ? 29  PRO C CG  1 
ATOM   4530 C  CD  . PRO C 1 29  ? 30.268  2.199   -35.483 1.00 10.97 ? 29  PRO C CD  1 
ATOM   4531 N  N   . ILE C 1 30  ? 29.769  -1.041  -38.400 1.00 9.99  ? 30  ILE C N   1 
ATOM   4532 C  CA  . ILE C 1 30  ? 28.715  -1.665  -39.233 1.00 9.52  ? 30  ILE C CA  1 
ATOM   4533 C  C   . ILE C 1 30  ? 28.450  -3.111  -38.777 1.00 10.26 ? 30  ILE C C   1 
ATOM   4534 O  O   . ILE C 1 30  ? 29.228  -3.721  -38.014 1.00 10.29 ? 30  ILE C O   1 
ATOM   4535 C  CB  . ILE C 1 30  ? 29.188  -1.774  -40.738 1.00 9.60  ? 30  ILE C CB  1 
ATOM   4536 C  CG1 . ILE C 1 30  ? 30.449  -2.574  -40.874 1.00 8.19  ? 30  ILE C CG1 1 
ATOM   4537 C  CG2 . ILE C 1 30  ? 29.458  -0.337  -41.178 1.00 10.78 ? 30  ILE C CG2 1 
ATOM   4538 C  CD1 . ILE C 1 30  ? 30.836  -2.752  -42.321 1.00 10.46 ? 30  ILE C CD1 1 
ATOM   4539 N  N   . ASP C 1 31  ? 27.285  -3.604  -39.252 1.00 11.11 ? 31  ASP C N   1 
ATOM   4540 C  CA  . ASP C 1 31  ? 26.955  -5.070  -39.150 1.00 11.45 ? 31  ASP C CA  1 
ATOM   4541 C  C   . ASP C 1 31  ? 27.612  -5.837  -40.192 1.00 12.00 ? 31  ASP C C   1 
ATOM   4542 O  O   . ASP C 1 31  ? 27.488  -5.547  -41.396 1.00 12.86 ? 31  ASP C O   1 
ATOM   4543 C  CB  . ASP C 1 31  ? 25.454  -5.266  -39.260 1.00 12.27 ? 31  ASP C CB  1 
ATOM   4544 C  CG  . ASP C 1 31  ? 25.033  -6.724  -39.030 1.00 12.70 ? 31  ASP C CG  1 
ATOM   4545 O  OD1 . ASP C 1 31  ? 25.506  -7.284  -38.009 1.00 13.48 ? 31  ASP C OD1 1 
ATOM   4546 O  OD2 . ASP C 1 31  ? 24.125  -7.161  -39.772 1.00 17.15 ? 31  ASP C OD2 1 
ATOM   4547 N  N   . LEU C 1 32  ? 28.284  -6.929  -39.745 1.00 12.35 ? 32  LEU C N   1 
ATOM   4548 C  CA  . LEU C 1 32  ? 28.916  -7.786  -40.656 1.00 13.14 ? 32  LEU C CA  1 
ATOM   4549 C  C   . LEU C 1 32  ? 28.039  -9.009  -40.864 1.00 15.21 ? 32  LEU C C   1 
ATOM   4550 O  O   . LEU C 1 32  ? 27.794  -9.744  -39.950 1.00 17.41 ? 32  LEU C O   1 
ATOM   4551 C  CB  . LEU C 1 32  ? 30.288  -8.163  -40.072 1.00 13.18 ? 32  LEU C CB  1 
ATOM   4552 C  CG  . LEU C 1 32  ? 31.235  -7.036  -39.567 1.00 12.11 ? 32  LEU C CG  1 
ATOM   4553 C  CD1 . LEU C 1 32  ? 32.484  -7.611  -38.843 1.00 12.56 ? 32  LEU C CD1 1 
ATOM   4554 C  CD2 . LEU C 1 32  ? 31.688  -6.211  -40.787 1.00 13.53 ? 32  LEU C CD2 1 
ATOM   4555 N  N   . HIS C 1 33  ? 27.518  -9.157  -42.045 1.00 17.89 ? 33  HIS C N   1 
ATOM   4556 C  CA  . HIS C 1 33  ? 26.574  -10.235 -42.307 1.00 20.09 ? 33  HIS C CA  1 
ATOM   4557 C  C   . HIS C 1 33  ? 26.756  -10.836 -43.668 1.00 20.01 ? 33  HIS C C   1 
ATOM   4558 O  O   . HIS C 1 33  ? 27.218  -10.190 -44.553 1.00 19.77 ? 33  HIS C O   1 
ATOM   4559 C  CB  . HIS C 1 33  ? 25.126  -9.778  -42.057 1.00 20.25 ? 33  HIS C CB  1 
ATOM   4560 C  CG  . HIS C 1 33  ? 24.627  -8.762  -43.012 1.00 22.34 ? 33  HIS C CG  1 
ATOM   4561 N  ND1 . HIS C 1 33  ? 23.928  -9.102  -44.102 1.00 25.66 ? 33  HIS C ND1 1 
ATOM   4562 C  CD2 . HIS C 1 33  ? 24.761  -7.373  -43.043 1.00 23.62 ? 33  HIS C CD2 1 
ATOM   4563 C  CE1 . HIS C 1 33  ? 23.623  -7.999  -44.806 1.00 27.07 ? 33  HIS C CE1 1 
ATOM   4564 N  NE2 . HIS C 1 33  ? 24.134  -6.935  -44.169 1.00 26.02 ? 33  HIS C NE2 1 
ATOM   4565 N  N   . SER C 1 34  ? 26.250  -12.068 -43.857 1.00 21.53 ? 34  SER C N   1 
ATOM   4566 C  CA  . SER C 1 34  ? 26.555  -12.930 -44.977 1.00 23.94 ? 34  SER C CA  1 
ATOM   4567 C  C   . SER C 1 34  ? 26.390  -12.311 -46.317 1.00 21.20 ? 34  SER C C   1 
ATOM   4568 O  O   . SER C 1 34  ? 27.211  -12.489 -47.188 1.00 23.16 ? 34  SER C O   1 
ATOM   4569 C  CB  . SER C 1 34  ? 25.623  -14.133 -44.933 1.00 27.59 ? 34  SER C CB  1 
ATOM   4570 O  OG  . SER C 1 34  ? 26.292  -15.269 -44.461 1.00 31.86 ? 34  SER C OG  1 
ATOM   4571 N  N   . ASP C 1 35  ? 25.307  -11.565 -46.494 1.00 21.37 ? 35  ASP C N   1 
ATOM   4572 C  CA  . ASP C 1 35  ? 24.928  -11.174 -47.829 1.00 25.31 ? 35  ASP C CA  1 
ATOM   4573 C  C   . ASP C 1 35  ? 25.795  -10.045 -48.371 1.00 21.25 ? 35  ASP C C   1 
ATOM   4574 O  O   . ASP C 1 35  ? 25.712  -9.699  -49.571 1.00 23.85 ? 35  ASP C O   1 
ATOM   4575 C  CB  . ASP C 1 35  ? 23.424  -10.826 -47.866 1.00 33.64 ? 35  ASP C CB  1 
ATOM   4576 C  CG  . ASP C 1 35  ? 22.548  -12.013 -47.482 1.00 43.66 ? 35  ASP C CG  1 
ATOM   4577 O  OD1 . ASP C 1 35  ? 23.080  -13.149 -47.428 1.00 53.10 ? 35  ASP C OD1 1 
ATOM   4578 O  OD2 . ASP C 1 35  ? 21.335  -11.825 -47.224 1.00 48.75 ? 35  ASP C OD2 1 
ATOM   4579 N  N   . ILE C 1 36  ? 26.613  -9.428  -47.511 1.00 17.73 ? 36  ILE C N   1 
ATOM   4580 C  CA  . ILE C 1 36  ? 27.515  -8.393  -47.998 1.00 17.75 ? 36  ILE C CA  1 
ATOM   4581 C  C   . ILE C 1 36  ? 28.992  -8.792  -47.973 1.00 15.38 ? 36  ILE C C   1 
ATOM   4582 O  O   . ILE C 1 36  ? 29.827  -7.941  -48.207 1.00 17.13 ? 36  ILE C O   1 
ATOM   4583 C  CB  . ILE C 1 36  ? 27.336  -7.057  -47.247 1.00 15.52 ? 36  ILE C CB  1 
ATOM   4584 C  CG1 . ILE C 1 36  ? 27.561  -7.166  -45.710 1.00 16.23 ? 36  ILE C CG1 1 
ATOM   4585 C  CG2 . ILE C 1 36  ? 25.934  -6.528  -47.557 1.00 19.98 ? 36  ILE C CG2 1 
ATOM   4586 C  CD1 . ILE C 1 36  ? 27.725  -5.807  -44.982 1.00 16.19 ? 36  ILE C CD1 1 
ATOM   4587 N  N   . LEU C 1 37  ? 29.267  -10.060 -47.722 1.00 17.40 ? 37  LEU C N   1 
ATOM   4588 C  CA  . LEU C 1 37  ? 30.635  -10.555 -47.644 1.00 16.84 ? 37  LEU C CA  1 
ATOM   4589 C  C   . LEU C 1 37  ? 31.124  -11.085 -48.973 1.00 18.20 ? 37  LEU C C   1 
ATOM   4590 O  O   . LEU C 1 37  ? 30.365  -11.657 -49.787 1.00 19.82 ? 37  LEU C O   1 
ATOM   4591 C  CB  . LEU C 1 37  ? 30.751  -11.693 -46.641 1.00 16.11 ? 37  LEU C CB  1 
ATOM   4592 C  CG  . LEU C 1 37  ? 30.321  -11.482 -45.187 1.00 16.95 ? 37  LEU C CG  1 
ATOM   4593 C  CD1 . LEU C 1 37  ? 30.638  -12.684 -44.305 1.00 18.55 ? 37  LEU C CD1 1 
ATOM   4594 C  CD2 . LEU C 1 37  ? 31.015  -10.243 -44.598 1.00 16.18 ? 37  LEU C CD2 1 
ATOM   4595 N  N   . GLN C 1 38  ? 32.378  -10.740 -49.290 1.00 15.43 ? 38  GLN C N   1 
ATOM   4596 C  CA  . GLN C 1 38  ? 32.956  -11.262 -50.514 1.00 17.09 ? 38  GLN C CA  1 
ATOM   4597 C  C   . GLN C 1 38  ? 34.382  -11.667 -50.267 1.00 17.47 ? 38  GLN C C   1 
ATOM   4598 O  O   . GLN C 1 38  ? 35.182  -10.824 -49.836 1.00 14.93 ? 38  GLN C O   1 
ATOM   4599 C  CB  . GLN C 1 38  ? 32.837  -10.228 -51.618 1.00 18.84 ? 38  GLN C CB  1 
ATOM   4600 C  CG  . GLN C 1 38  ? 33.189  -10.796 -52.985 1.00 22.37 ? 38  GLN C CG  1 
ATOM   4601 C  CD  . GLN C 1 38  ? 32.943  -9.772  -54.087 1.00 25.30 ? 38  GLN C CD  1 
ATOM   4602 O  OE1 . GLN C 1 38  ? 31.789  -9.531  -54.533 1.00 30.90 ? 38  GLN C OE1 1 
ATOM   4603 N  NE2 . GLN C 1 38  ? 33.988  -9.117  -54.459 1.00 22.38 ? 38  GLN C NE2 1 
ATOM   4604 N  N   . TYR C 1 39  ? 34.718  -12.956 -50.515 1.00 16.05 ? 39  TYR C N   1 
ATOM   4605 C  CA  . TYR C 1 39  ? 36.146  -13.328 -50.482 1.00 15.05 ? 39  TYR C CA  1 
ATOM   4606 C  C   . TYR C 1 39  ? 37.044  -12.487 -51.389 1.00 14.77 ? 39  TYR C C   1 
ATOM   4607 O  O   . TYR C 1 39  ? 36.661  -12.216 -52.564 1.00 15.41 ? 39  TYR C O   1 
ATOM   4608 C  CB  . TYR C 1 39  ? 36.253  -14.825 -50.921 1.00 15.87 ? 39  TYR C CB  1 
ATOM   4609 C  CG  . TYR C 1 39  ? 37.674  -15.259 -51.032 1.00 16.98 ? 39  TYR C CG  1 
ATOM   4610 C  CD1 . TYR C 1 39  ? 38.496  -15.341 -49.910 1.00 19.43 ? 39  TYR C CD1 1 
ATOM   4611 C  CD2 . TYR C 1 39  ? 38.186  -15.549 -52.287 1.00 19.36 ? 39  TYR C CD2 1 
ATOM   4612 C  CE1 . TYR C 1 39  ? 39.818  -15.737 -50.050 1.00 22.23 ? 39  TYR C CE1 1 
ATOM   4613 C  CE2 . TYR C 1 39  ? 39.509  -15.982 -52.449 1.00 21.80 ? 39  TYR C CE2 1 
ATOM   4614 C  CZ  . TYR C 1 39  ? 40.312  -16.087 -51.322 1.00 23.46 ? 39  TYR C CZ  1 
ATOM   4615 O  OH  . TYR C 1 39  ? 41.642  -16.473 -51.473 1.00 24.43 ? 39  TYR C OH  1 
ATOM   4616 N  N   . ASP C 1 40  ? 38.227  -12.134 -50.898 1.00 14.71 ? 40  ASP C N   1 
ATOM   4617 C  CA  . ASP C 1 40  ? 39.167  -11.254 -51.658 1.00 16.39 ? 40  ASP C CA  1 
ATOM   4618 C  C   . ASP C 1 40  ? 40.552  -11.887 -51.489 1.00 15.59 ? 40  ASP C C   1 
ATOM   4619 O  O   . ASP C 1 40  ? 41.115  -11.871 -50.380 1.00 16.67 ? 40  ASP C O   1 
ATOM   4620 C  CB  . ASP C 1 40  ? 39.121  -9.838  -51.075 1.00 18.58 ? 40  ASP C CB  1 
ATOM   4621 C  CG  . ASP C 1 40  ? 40.076  -8.857  -51.726 1.00 23.00 ? 40  ASP C CG  1 
ATOM   4622 O  OD1 . ASP C 1 40  ? 40.935  -9.227  -52.544 1.00 18.19 ? 40  ASP C OD1 1 
ATOM   4623 O  OD2 . ASP C 1 40  ? 39.957  -7.652  -51.336 1.00 22.91 ? 40  ASP C OD2 1 
ATOM   4624 N  N   . ALA C 1 41  ? 41.116  -12.407 -52.589 1.00 15.02 ? 41  ALA C N   1 
ATOM   4625 C  CA  . ALA C 1 41  ? 42.459  -13.025 -52.546 1.00 15.66 ? 41  ALA C CA  1 
ATOM   4626 C  C   . ALA C 1 41  ? 43.619  -12.107 -52.155 1.00 17.23 ? 41  ALA C C   1 
ATOM   4627 O  O   . ALA C 1 41  ? 44.714  -12.540 -51.737 1.00 17.30 ? 41  ALA C O   1 
ATOM   4628 C  CB  . ALA C 1 41  ? 42.725  -13.583 -53.928 1.00 15.87 ? 41  ALA C CB  1 
ATOM   4629 N  N   . SER C 1 42  ? 43.434  -10.813 -52.191 1.00 17.66 ? 42  SER C N   1 
ATOM   4630 C  CA  . SER C 1 42  ? 44.525  -9.938  -51.821 1.00 18.14 ? 42  SER C CA  1 
ATOM   4631 C  C   . SER C 1 42  ? 44.702  -9.850  -50.292 1.00 17.34 ? 42  SER C C   1 
ATOM   4632 O  O   . SER C 1 42  ? 45.673  -9.216  -49.808 1.00 18.93 ? 42  SER C O   1 
ATOM   4633 C  CB  . SER C 1 42  ? 44.272  -8.538  -52.322 1.00 17.01 ? 42  SER C CB  1 
ATOM   4634 O  OG  . SER C 1 42  ? 43.213  -7.960  -51.582 1.00 18.56 ? 42  SER C OG  1 
ATOM   4635 N  N   . LEU C 1 43  ? 43.748  -10.476 -49.552 1.00 16.63 ? 43  LEU C N   1 
ATOM   4636 C  CA  . LEU C 1 43  ? 43.748  -10.287 -48.099 1.00 16.16 ? 43  LEU C CA  1 
ATOM   4637 C  C   . LEU C 1 43  ? 44.658  -11.325 -47.425 1.00 15.78 ? 43  LEU C C   1 
ATOM   4638 O  O   . LEU C 1 43  ? 44.167  -12.291 -46.797 1.00 17.32 ? 43  LEU C O   1 
ATOM   4639 C  CB  . LEU C 1 43  ? 42.333  -10.261 -47.526 1.00 14.45 ? 43  LEU C CB  1 
ATOM   4640 C  CG  . LEU C 1 43  ? 41.486  -9.141  -48.095 1.00 14.08 ? 43  LEU C CG  1 
ATOM   4641 C  CD1 . LEU C 1 43  ? 40.020  -9.198  -47.476 1.00 12.91 ? 43  LEU C CD1 1 
ATOM   4642 C  CD2 . LEU C 1 43  ? 42.083  -7.733  -47.924 1.00 13.49 ? 43  LEU C CD2 1 
ATOM   4643 N  N   . THR C 1 44  ? 45.967  -11.130 -47.602 1.00 17.36 ? 44  THR C N   1 
ATOM   4644 C  CA  . THR C 1 44  ? 46.962  -12.069 -47.088 1.00 20.84 ? 44  THR C CA  1 
ATOM   4645 C  C   . THR C 1 44  ? 47.167  -11.846 -45.568 1.00 24.78 ? 44  THR C C   1 
ATOM   4646 O  O   . THR C 1 44  ? 46.684  -10.816 -45.019 1.00 21.43 ? 44  THR C O   1 
ATOM   4647 C  CB  . THR C 1 44  ? 48.276  -11.890 -47.856 1.00 21.24 ? 44  THR C CB  1 
ATOM   4648 O  OG1 . THR C 1 44  ? 48.606  -10.496 -47.974 1.00 23.60 ? 44  THR C OG1 1 
ATOM   4649 C  CG2 . THR C 1 44  ? 48.126  -12.493 -49.227 1.00 20.70 ? 44  THR C CG2 1 
ATOM   4650 N  N   . PRO C 1 45  ? 47.878  -12.758 -44.887 1.00 24.96 ? 45  PRO C N   1 
ATOM   4651 C  CA  . PRO C 1 45  ? 48.163  -12.538 -43.435 1.00 24.91 ? 45  PRO C CA  1 
ATOM   4652 C  C   . PRO C 1 45  ? 48.965  -11.299 -43.121 1.00 24.91 ? 45  PRO C C   1 
ATOM   4653 O  O   . PRO C 1 45  ? 49.981  -10.999 -43.753 1.00 25.72 ? 45  PRO C O   1 
ATOM   4654 C  CB  . PRO C 1 45  ? 48.924  -13.815 -43.047 1.00 26.64 ? 45  PRO C CB  1 
ATOM   4655 C  CG  . PRO C 1 45  ? 48.317  -14.854 -43.952 1.00 24.30 ? 45  PRO C CG  1 
ATOM   4656 C  CD  . PRO C 1 45  ? 48.153  -14.171 -45.275 1.00 25.05 ? 45  PRO C CD  1 
ATOM   4657 N  N   . LEU C 1 46  ? 48.508  -10.563 -42.132 1.00 22.62 ? 46  LEU C N   1 
ATOM   4658 C  CA  . LEU C 1 46  ? 49.247  -9.418  -41.647 1.00 24.14 ? 46  LEU C CA  1 
ATOM   4659 C  C   . LEU C 1 46  ? 50.363  -9.892  -40.719 1.00 22.62 ? 46  LEU C C   1 
ATOM   4660 O  O   . LEU C 1 46  ? 50.210  -10.903 -40.021 1.00 25.11 ? 46  LEU C O   1 
ATOM   4661 C  CB  . LEU C 1 46  ? 48.339  -8.485  -40.891 1.00 22.35 ? 46  LEU C CB  1 
ATOM   4662 C  CG  . LEU C 1 46  ? 47.267  -7.782  -41.744 1.00 22.22 ? 46  LEU C CG  1 
ATOM   4663 C  CD1 . LEU C 1 46  ? 46.429  -6.952  -40.783 1.00 21.63 ? 46  LEU C CD1 1 
ATOM   4664 C  CD2 . LEU C 1 46  ? 47.854  -6.964  -42.894 1.00 21.53 ? 46  LEU C CD2 1 
ATOM   4665 N  N   . GLU C 1 47  ? 51.456  -9.144  -40.721 1.00 22.89 ? 47  GLU C N   1 
ATOM   4666 C  CA  . GLU C 1 47  ? 52.496  -9.375  -39.759 1.00 24.54 ? 47  GLU C CA  1 
ATOM   4667 C  C   . GLU C 1 47  ? 52.529  -8.260  -38.770 1.00 22.07 ? 47  GLU C C   1 
ATOM   4668 O  O   . GLU C 1 47  ? 52.494  -7.043  -39.118 1.00 21.66 ? 47  GLU C O   1 
ATOM   4669 C  CB  . GLU C 1 47  ? 53.835  -9.441  -40.509 1.00 30.72 ? 47  GLU C CB  1 
ATOM   4670 C  CG  . GLU C 1 47  ? 53.944  -10.525 -41.585 1.00 39.94 ? 47  GLU C CG  1 
ATOM   4671 C  CD  . GLU C 1 47  ? 55.357  -10.586 -42.206 1.00 49.39 ? 47  GLU C CD  1 
ATOM   4672 O  OE1 . GLU C 1 47  ? 56.351  -10.604 -41.421 1.00 50.00 ? 47  GLU C OE1 1 
ATOM   4673 O  OE2 . GLU C 1 47  ? 55.479  -10.611 -43.470 1.00 51.51 ? 47  GLU C OE2 1 
ATOM   4674 N  N   . PHE C 1 48  ? 52.667  -8.633  -37.493 1.00 22.45 ? 48  PHE C N   1 
ATOM   4675 C  CA  . PHE C 1 48  ? 52.695  -7.659  -36.393 1.00 25.28 ? 48  PHE C CA  1 
ATOM   4676 C  C   . PHE C 1 48  ? 54.116  -7.462  -35.882 1.00 26.01 ? 48  PHE C C   1 
ATOM   4677 O  O   . PHE C 1 48  ? 54.737  -8.417  -35.417 1.00 30.03 ? 48  PHE C O   1 
ATOM   4678 C  CB  . PHE C 1 48  ? 51.704  -8.105  -35.304 1.00 26.49 ? 48  PHE C CB  1 
ATOM   4679 C  CG  . PHE C 1 48  ? 50.354  -8.450  -35.883 1.00 25.27 ? 48  PHE C CG  1 
ATOM   4680 C  CD1 . PHE C 1 48  ? 49.495  -7.437  -36.337 1.00 23.50 ? 48  PHE C CD1 1 
ATOM   4681 C  CD2 . PHE C 1 48  ? 50.001  -9.762  -36.093 1.00 23.09 ? 48  PHE C CD2 1 
ATOM   4682 C  CE1 . PHE C 1 48  ? 48.314  -7.775  -36.962 1.00 22.05 ? 48  PHE C CE1 1 
ATOM   4683 C  CE2 . PHE C 1 48  ? 48.798  -10.099 -36.676 1.00 24.75 ? 48  PHE C CE2 1 
ATOM   4684 C  CZ  . PHE C 1 48  ? 47.944  -9.103  -37.063 1.00 20.63 ? 48  PHE C CZ  1 
ATOM   4685 N  N   . GLN C 1 49  ? 54.637  -6.254  -36.016 1.00 22.95 ? 49  GLN C N   1 
ATOM   4686 C  CA  . GLN C 1 49  ? 56.077  -6.039  -35.746 1.00 24.93 ? 49  GLN C CA  1 
ATOM   4687 C  C   . GLN C 1 49  ? 56.316  -5.095  -34.631 1.00 24.54 ? 49  GLN C C   1 
ATOM   4688 O  O   . GLN C 1 49  ? 55.650  -4.038  -34.511 1.00 20.22 ? 49  GLN C O   1 
ATOM   4689 C  CB  . GLN C 1 49  ? 56.745  -5.587  -37.043 1.00 25.45 ? 49  GLN C CB  1 
ATOM   4690 C  CG  . GLN C 1 49  ? 56.615  -6.710  -38.036 1.00 29.26 ? 49  GLN C CG  1 
ATOM   4691 C  CD  . GLN C 1 49  ? 57.462  -6.565  -39.276 1.00 42.48 ? 49  GLN C CD  1 
ATOM   4692 O  OE1 . GLN C 1 49  ? 57.847  -5.439  -39.682 1.00 46.43 ? 49  GLN C OE1 1 
ATOM   4693 N  NE2 . GLN C 1 49  ? 57.778  -7.729  -39.904 1.00 41.66 ? 49  GLN C NE2 1 
ATOM   4694 N  N   . GLY C 1 50  ? 57.270  -5.458  -33.762 1.00 21.42 ? 50  GLY C N   1 
ATOM   4695 C  CA  . GLY C 1 50  ? 57.520  -4.647  -32.595 1.00 25.72 ? 50  GLY C CA  1 
ATOM   4696 C  C   . GLY C 1 50  ? 56.383  -4.599  -31.584 1.00 21.92 ? 50  GLY C C   1 
ATOM   4697 O  O   . GLY C 1 50  ? 56.306  -3.650  -30.797 1.00 24.16 ? 50  GLY C O   1 
ATOM   4698 N  N   . TYR C 1 51  ? 55.551  -5.631  -31.549 1.00 22.05 ? 51  TYR C N   1 
ATOM   4699 C  CA  . TYR C 1 51  ? 54.408  -5.635  -30.602 1.00 21.06 ? 51  TYR C CA  1 
ATOM   4700 C  C   . TYR C 1 51  ? 54.868  -6.134  -29.271 1.00 21.87 ? 51  TYR C C   1 
ATOM   4701 O  O   . TYR C 1 51  ? 54.197  -5.956  -28.266 1.00 19.35 ? 51  TYR C O   1 
ATOM   4702 C  CB  . TYR C 1 51  ? 53.240  -6.546  -31.096 1.00 21.38 ? 51  TYR C CB  1 
ATOM   4703 C  CG  . TYR C 1 51  ? 52.245  -5.875  -32.041 1.00 20.59 ? 51  TYR C CG  1 
ATOM   4704 C  CD1 . TYR C 1 51  ? 50.894  -6.131  -31.882 1.00 18.78 ? 51  TYR C CD1 1 
ATOM   4705 C  CD2 . TYR C 1 51  ? 52.650  -4.978  -33.029 1.00 18.45 ? 51  TYR C CD2 1 
ATOM   4706 C  CE1 . TYR C 1 51  ? 49.933  -5.534  -32.720 1.00 19.69 ? 51  TYR C CE1 1 
ATOM   4707 C  CE2 . TYR C 1 51  ? 51.712  -4.348  -33.875 1.00 17.80 ? 51  TYR C CE2 1 
ATOM   4708 C  CZ  . TYR C 1 51  ? 50.330  -4.648  -33.711 1.00 21.47 ? 51  TYR C CZ  1 
ATOM   4709 O  OH  . TYR C 1 51  ? 49.377  -4.016  -34.578 1.00 20.13 ? 51  TYR C OH  1 
ATOM   4710 N  N   . ASN C 1 52  ? 56.019  -6.821  -29.262 1.00 23.77 ? 52  ASN C N   1 
ATOM   4711 C  CA  . ASN C 1 52  ? 56.453  -7.400  -27.996 1.00 28.99 ? 52  ASN C CA  1 
ATOM   4712 C  C   . ASN C 1 52  ? 57.193  -6.341  -27.148 1.00 30.64 ? 52  ASN C C   1 
ATOM   4713 O  O   . ASN C 1 52  ? 58.409  -6.194  -27.298 1.00 33.29 ? 52  ASN C O   1 
ATOM   4714 C  CB  . ASN C 1 52  ? 57.330  -8.642  -28.279 1.00 27.05 ? 52  ASN C CB  1 
ATOM   4715 C  CG  . ASN C 1 52  ? 57.686  -9.362  -27.039 1.00 32.00 ? 52  ASN C CG  1 
ATOM   4716 O  OD1 . ASN C 1 52  ? 57.160  -9.055  -25.972 1.00 29.92 ? 52  ASN C OD1 1 
ATOM   4717 N  ND2 . ASN C 1 52  ? 58.566  -10.370 -27.158 1.00 37.96 ? 52  ASN C ND2 1 
ATOM   4718 N  N   . LEU C 1 53  ? 56.459  -5.634  -26.285 1.00 27.52 ? 53  LEU C N   1 
ATOM   4719 C  CA  . LEU C 1 53  ? 57.035  -4.456  -25.597 1.00 31.58 ? 53  LEU C CA  1 
ATOM   4720 C  C   . LEU C 1 53  ? 57.633  -4.925  -24.267 1.00 33.36 ? 53  LEU C C   1 
ATOM   4721 O  O   . LEU C 1 53  ? 56.990  -5.662  -23.500 1.00 30.11 ? 53  LEU C O   1 
ATOM   4722 C  CB  . LEU C 1 53  ? 56.013  -3.336  -25.372 1.00 26.94 ? 53  LEU C CB  1 
ATOM   4723 C  CG  . LEU C 1 53  ? 54.955  -2.926  -26.426 1.00 26.56 ? 53  LEU C CG  1 
ATOM   4724 C  CD1 . LEU C 1 53  ? 53.934  -1.994  -25.760 1.00 23.27 ? 53  LEU C CD1 1 
ATOM   4725 C  CD2 . LEU C 1 53  ? 55.567  -2.165  -27.599 1.00 25.96 ? 53  LEU C CD2 1 
ATOM   4726 N  N   . SER C 1 54  ? 58.850  -4.459  -23.993 1.00 39.98 ? 54  SER C N   1 
ATOM   4727 C  CA  . SER C 1 54  ? 59.605  -4.887  -22.817 1.00 41.85 ? 54  SER C CA  1 
ATOM   4728 C  C   . SER C 1 54  ? 58.885  -4.644  -21.468 1.00 41.21 ? 54  SER C C   1 
ATOM   4729 O  O   . SER C 1 54  ? 58.311  -3.556  -21.221 1.00 37.22 ? 54  SER C O   1 
ATOM   4730 C  CB  . SER C 1 54  ? 60.979  -4.226  -22.822 1.00 42.28 ? 54  SER C CB  1 
ATOM   4731 O  OG  . SER C 1 54  ? 61.814  -4.833  -21.855 1.00 54.51 ? 54  SER C OG  1 
ATOM   4732 N  N   . ALA C 1 55  ? 58.938  -5.672  -20.612 1.00 43.31 ? 55  ALA C N   1 
ATOM   4733 C  CA  . ALA C 1 55  ? 58.451  -5.600  -19.219 1.00 42.51 ? 55  ALA C CA  1 
ATOM   4734 C  C   . ALA C 1 55  ? 59.027  -4.395  -18.436 1.00 42.22 ? 55  ALA C C   1 
ATOM   4735 O  O   . ALA C 1 55  ? 58.370  -3.846  -17.515 1.00 41.82 ? 55  ALA C O   1 
ATOM   4736 C  CB  . ALA C 1 55  ? 58.747  -6.899  -18.503 1.00 39.18 ? 55  ALA C CB  1 
ATOM   4737 N  N   . ASN C 1 56  ? 60.231  -3.960  -18.801 1.00 39.18 ? 56  ASN C N   1 
ATOM   4738 C  CA  . ASN C 1 56  ? 60.815  -2.832  -18.071 1.00 45.42 ? 56  ASN C CA  1 
ATOM   4739 C  C   . ASN C 1 56  ? 60.509  -1.436  -18.683 1.00 48.39 ? 56  ASN C C   1 
ATOM   4740 O  O   . ASN C 1 56  ? 60.820  -0.394  -18.051 1.00 41.77 ? 56  ASN C O   1 
ATOM   4741 C  CB  . ASN C 1 56  ? 62.310  -3.065  -17.716 1.00 48.40 ? 56  ASN C CB  1 
ATOM   4742 C  CG  . ASN C 1 56  ? 63.227  -2.947  -18.908 1.00 54.76 ? 56  ASN C CG  1 
ATOM   4743 O  OD1 . ASN C 1 56  ? 62.767  -2.781  -20.044 1.00 56.34 ? 56  ASN C OD1 1 
ATOM   4744 N  ND2 . ASN C 1 56  ? 64.532  -3.020  -18.660 1.00 50.78 ? 56  ASN C ND2 1 
ATOM   4745 N  N   . LYS C 1 57  ? 59.873  -1.438  -19.876 1.00 43.68 ? 57  LYS C N   1 
ATOM   4746 C  CA  . LYS C 1 57  ? 59.342  -0.222  -20.523 1.00 43.24 ? 57  LYS C CA  1 
ATOM   4747 C  C   . LYS C 1 57  ? 57.974  0.070   -19.903 1.00 35.10 ? 57  LYS C C   1 
ATOM   4748 O  O   . LYS C 1 57  ? 57.357  -0.813  -19.296 1.00 30.67 ? 57  LYS C O   1 
ATOM   4749 C  CB  . LYS C 1 57  ? 59.199  -0.402  -22.042 1.00 50.68 ? 57  LYS C CB  1 
ATOM   4750 C  CG  . LYS C 1 57  ? 60.478  -0.624  -22.843 1.00 55.52 ? 57  LYS C CG  1 
ATOM   4751 C  CD  . LYS C 1 57  ? 61.063  0.641   -23.451 1.00 58.84 ? 57  LYS C CD  1 
ATOM   4752 C  CE  . LYS C 1 57  ? 62.156  0.258   -24.449 1.00 64.12 ? 57  LYS C CE  1 
ATOM   4753 N  NZ  . LYS C 1 57  ? 63.185  1.307   -24.733 1.00 62.39 ? 57  LYS C NZ  1 
ATOM   4754 N  N   . GLN C 1 58  ? 57.533  1.331   -19.934 1.00 32.50 ? 58  GLN C N   1 
ATOM   4755 C  CA  . GLN C 1 58  ? 56.183  1.611   -19.487 1.00 29.49 ? 58  GLN C CA  1 
ATOM   4756 C  C   . GLN C 1 58  ? 55.449  2.527   -20.477 1.00 27.07 ? 58  GLN C C   1 
ATOM   4757 O  O   . GLN C 1 58  ? 56.078  3.359   -21.156 1.00 25.38 ? 58  GLN C O   1 
ATOM   4758 C  CB  . GLN C 1 58  ? 56.159  2.209   -18.046 1.00 30.07 ? 58  GLN C CB  1 
ATOM   4759 C  CG  . GLN C 1 58  ? 56.631  3.667   -17.935 1.00 28.00 ? 58  GLN C CG  1 
ATOM   4760 C  CD  . GLN C 1 58  ? 56.580  4.266   -16.499 1.00 30.66 ? 58  GLN C CD  1 
ATOM   4761 O  OE1 . GLN C 1 58  ? 56.195  3.571   -15.534 1.00 29.26 ? 58  GLN C OE1 1 
ATOM   4762 N  NE2 . GLN C 1 58  ? 56.888  5.574   -16.368 1.00 29.92 ? 58  GLN C NE2 1 
ATOM   4763 N  N   . PHE C 1 59  ? 54.112  2.353   -20.504 1.00 27.00 ? 59  PHE C N   1 
ATOM   4764 C  CA  . PHE C 1 59  ? 53.175  3.013   -21.432 1.00 27.81 ? 59  PHE C CA  1 
ATOM   4765 C  C   . PHE C 1 59  ? 52.043  3.742   -20.743 1.00 23.97 ? 59  PHE C C   1 
ATOM   4766 O  O   . PHE C 1 59  ? 51.479  3.240   -19.798 1.00 26.94 ? 59  PHE C O   1 
ATOM   4767 C  CB  . PHE C 1 59  ? 52.759  1.941   -22.425 1.00 25.09 ? 59  PHE C CB  1 
ATOM   4768 C  CG  . PHE C 1 59  ? 53.958  1.299   -23.052 1.00 27.62 ? 59  PHE C CG  1 
ATOM   4769 C  CD1 . PHE C 1 59  ? 54.600  1.924   -24.113 1.00 26.26 ? 59  PHE C CD1 1 
ATOM   4770 C  CD2 . PHE C 1 59  ? 54.532  0.140   -22.490 1.00 28.00 ? 59  PHE C CD2 1 
ATOM   4771 C  CE1 . PHE C 1 59  ? 55.756  1.365   -24.667 1.00 29.62 ? 59  PHE C CE1 1 
ATOM   4772 C  CE2 . PHE C 1 59  ? 55.679  -0.437  -23.048 1.00 26.53 ? 59  PHE C CE2 1 
ATOM   4773 C  CZ  . PHE C 1 59  ? 56.301  0.179   -24.122 1.00 26.35 ? 59  PHE C CZ  1 
ATOM   4774 N  N   . LEU C 1 60  ? 51.763  4.996   -21.140 1.00 21.84 ? 60  LEU C N   1 
ATOM   4775 C  CA  . LEU C 1 60  ? 50.775  5.806   -20.452 1.00 21.79 ? 60  LEU C CA  1 
ATOM   4776 C  C   . LEU C 1 60  ? 49.306  5.323   -20.692 1.00 24.56 ? 60  LEU C C   1 
ATOM   4777 O  O   . LEU C 1 60  ? 48.869  5.163   -21.846 1.00 23.43 ? 60  LEU C O   1 
ATOM   4778 C  CB  . LEU C 1 60  ? 50.927  7.273   -20.889 1.00 23.17 ? 60  LEU C CB  1 
ATOM   4779 C  CG  . LEU C 1 60  ? 50.140  8.405   -20.178 1.00 26.13 ? 60  LEU C CG  1 
ATOM   4780 C  CD1 . LEU C 1 60  ? 50.520  8.552   -18.691 1.00 27.36 ? 60  LEU C CD1 1 
ATOM   4781 C  CD2 . LEU C 1 60  ? 50.301  9.749   -20.896 1.00 28.66 ? 60  LEU C CD2 1 
ATOM   4782 N  N   . LEU C 1 61  ? 48.570  5.132   -19.610 1.00 20.66 ? 61  LEU C N   1 
ATOM   4783 C  CA  . LEU C 1 61  ? 47.165  4.747   -19.632 1.00 22.95 ? 61  LEU C CA  1 
ATOM   4784 C  C   . LEU C 1 61  ? 46.401  5.992   -19.247 1.00 25.26 ? 61  LEU C C   1 
ATOM   4785 O  O   . LEU C 1 61  ? 46.796  6.635   -18.246 1.00 24.79 ? 61  LEU C O   1 
ATOM   4786 C  CB  . LEU C 1 61  ? 46.922  3.695   -18.553 1.00 26.59 ? 61  LEU C CB  1 
ATOM   4787 C  CG  . LEU C 1 61  ? 46.644  2.251   -18.953 1.00 30.84 ? 61  LEU C CG  1 
ATOM   4788 C  CD1 . LEU C 1 61  ? 46.069  1.497   -17.761 1.00 29.17 ? 61  LEU C CD1 1 
ATOM   4789 C  CD2 . LEU C 1 61  ? 45.682  2.218   -20.129 1.00 30.09 ? 61  LEU C CD2 1 
ATOM   4790 N  N   . THR C 1 62  ? 45.373  6.362   -19.988 1.00 22.52 ? 62  THR C N   1 
ATOM   4791 C  CA  . THR C 1 62  ? 44.713  7.665   -19.762 1.00 23.78 ? 62  THR C CA  1 
ATOM   4792 C  C   . THR C 1 62  ? 43.236  7.414   -19.797 1.00 27.01 ? 62  THR C C   1 
ATOM   4793 O  O   . THR C 1 62  ? 42.728  6.800   -20.731 1.00 24.27 ? 62  THR C O   1 
ATOM   4794 C  CB  . THR C 1 62  ? 45.042  8.710   -20.859 1.00 24.37 ? 62  THR C CB  1 
ATOM   4795 O  OG1 . THR C 1 62  ? 46.403  9.115   -20.720 1.00 23.87 ? 62  THR C OG1 1 
ATOM   4796 C  CG2 . THR C 1 62  ? 44.111  9.964   -20.743 1.00 29.05 ? 62  THR C CG2 1 
ATOM   4797 N  N   . ASN C 1 63  ? 42.521  7.867   -18.772 1.00 27.14 ? 63  ASN C N   1 
ATOM   4798 C  CA  . ASN C 1 63  ? 41.105  7.973   -18.897 1.00 24.16 ? 63  ASN C CA  1 
ATOM   4799 C  C   . ASN C 1 63  ? 40.841  9.330   -19.513 1.00 28.08 ? 63  ASN C C   1 
ATOM   4800 O  O   . ASN C 1 63  ? 41.030  10.372  -18.864 1.00 25.84 ? 63  ASN C O   1 
ATOM   4801 C  CB  . ASN C 1 63  ? 40.481  7.786   -17.504 1.00 27.50 ? 63  ASN C CB  1 
ATOM   4802 C  CG  . ASN C 1 63  ? 38.956  8.008   -17.446 1.00 27.54 ? 63  ASN C CG  1 
ATOM   4803 O  OD1 . ASN C 1 63  ? 38.351  8.685   -18.265 1.00 26.86 ? 63  ASN C OD1 1 
ATOM   4804 N  ND2 . ASN C 1 63  ? 38.366  7.559   -16.351 1.00 22.80 ? 63  ASN C ND2 1 
ATOM   4805 N  N   . ASN C 1 64  ? 40.405  9.348   -20.777 1.00 27.09 ? 64  ASN C N   1 
ATOM   4806 C  CA  . ASN C 1 64  ? 40.141  10.628  -21.399 1.00 26.77 ? 64  ASN C CA  1 
ATOM   4807 C  C   . ASN C 1 64  ? 38.715  11.046  -21.188 1.00 27.71 ? 64  ASN C C   1 
ATOM   4808 O  O   . ASN C 1 64  ? 38.239  12.000  -21.784 1.00 29.01 ? 64  ASN C O   1 
ATOM   4809 C  CB  . ASN C 1 64  ? 40.550  10.633  -22.900 1.00 26.70 ? 64  ASN C CB  1 
ATOM   4810 C  CG  . ASN C 1 64  ? 39.919  9.514   -23.648 1.00 26.78 ? 64  ASN C CG  1 
ATOM   4811 O  OD1 . ASN C 1 64  ? 38.796  9.113   -23.320 1.00 26.03 ? 64  ASN C OD1 1 
ATOM   4812 N  ND2 . ASN C 1 64  ? 40.637  8.957   -24.643 1.00 24.26 ? 64  ASN C ND2 1 
ATOM   4813 N  N   . GLY C 1 65  ? 37.988  10.260  -20.387 1.00 29.48 ? 65  GLY C N   1 
ATOM   4814 C  CA  . GLY C 1 65  ? 36.595  10.556  -20.135 1.00 27.19 ? 65  GLY C CA  1 
ATOM   4815 C  C   . GLY C 1 65  ? 35.671  9.961   -21.171 1.00 28.85 ? 65  GLY C C   1 
ATOM   4816 O  O   . GLY C 1 65  ? 34.451  10.150  -21.065 1.00 27.89 ? 65  GLY C O   1 
ATOM   4817 N  N   . HIS C 1 66  ? 36.245  9.283   -22.193 1.00 24.51 ? 66  HIS C N   1 
ATOM   4818 C  CA  . HIS C 1 66  ? 35.490  8.596   -23.233 1.00 26.31 ? 66  HIS C CA  1 
ATOM   4819 C  C   . HIS C 1 66  ? 35.735  7.115   -23.266 1.00 21.85 ? 66  HIS C C   1 
ATOM   4820 O  O   . HIS C 1 66  ? 34.796  6.331   -23.486 1.00 25.65 ? 66  HIS C O   1 
ATOM   4821 C  CB  . HIS C 1 66  ? 35.786  9.202   -24.607 1.00 22.34 ? 66  HIS C CB  1 
ATOM   4822 C  CG  . HIS C 1 66  ? 35.529  10.653  -24.666 1.00 22.32 ? 66  HIS C CG  1 
ATOM   4823 N  ND1 . HIS C 1 66  ? 36.518  11.555  -24.754 1.00 25.77 ? 66  HIS C ND1 1 
ATOM   4824 C  CD2 . HIS C 1 66  ? 34.352  11.365  -24.653 1.00 20.26 ? 66  HIS C CD2 1 
ATOM   4825 C  CE1 . HIS C 1 66  ? 35.982  12.778  -24.793 1.00 21.54 ? 66  HIS C CE1 1 
ATOM   4826 N  NE2 . HIS C 1 66  ? 34.660  12.652  -24.707 1.00 26.14 ? 66  HIS C NE2 1 
ATOM   4827 N  N   . SER C 1 67  ? 36.985  6.725   -23.080 1.00 22.07 ? 67  SER C N   1 
ATOM   4828 C  CA  . SER C 1 67  ? 37.404  5.340   -23.034 1.00 22.85 ? 67  SER C CA  1 
ATOM   4829 C  C   . SER C 1 67  ? 38.674  5.392   -22.190 1.00 26.56 ? 67  SER C C   1 
ATOM   4830 O  O   . SER C 1 67  ? 39.017  6.465   -21.630 1.00 26.68 ? 67  SER C O   1 
ATOM   4831 C  CB  . SER C 1 67  ? 37.676  4.796   -24.468 1.00 25.60 ? 67  SER C CB  1 
ATOM   4832 O  OG  . SER C 1 67  ? 38.051  3.438   -24.428 1.00 28.98 ? 67  SER C OG  1 
ATOM   4833 N  N   . VAL C 1 68  ? 39.317  4.252   -22.063 1.00 22.64 ? 68  VAL C N   1 
ATOM   4834 C  CA  . VAL C 1 68  ? 40.624  4.176   -21.434 1.00 25.11 ? 68  VAL C CA  1 
ATOM   4835 C  C   . VAL C 1 68  ? 41.546  3.835   -22.578 1.00 23.12 ? 68  VAL C C   1 
ATOM   4836 O  O   . VAL C 1 68  ? 41.224  2.948   -23.351 1.00 20.96 ? 68  VAL C O   1 
ATOM   4837 C  CB  . VAL C 1 68  ? 40.715  3.090   -20.304 1.00 24.56 ? 68  VAL C CB  1 
ATOM   4838 C  CG1 . VAL C 1 68  ? 40.474  1.698   -20.836 1.00 20.66 ? 68  VAL C CG1 1 
ATOM   4839 C  CG2 . VAL C 1 68  ? 42.086  3.112   -19.617 1.00 22.64 ? 68  VAL C CG2 1 
ATOM   4840 N  N   . LYS C 1 69  ? 42.661  4.567   -22.712 1.00 20.92 ? 69  LYS C N   1 
ATOM   4841 C  CA  . LYS C 1 69  ? 43.564  4.325   -23.851 1.00 21.16 ? 69  LYS C CA  1 
ATOM   4842 C  C   . LYS C 1 69  ? 44.945  4.070   -23.306 1.00 23.68 ? 69  LYS C C   1 
ATOM   4843 O  O   . LYS C 1 69  ? 45.312  4.630   -22.253 1.00 24.42 ? 69  LYS C O   1 
ATOM   4844 C  CB  . LYS C 1 69  ? 43.510  5.504   -24.845 1.00 24.41 ? 69  LYS C CB  1 
ATOM   4845 C  CG  . LYS C 1 69  ? 44.552  6.602   -24.667 1.00 26.80 ? 69  LYS C CG  1 
ATOM   4846 C  CD  . LYS C 1 69  ? 44.231  7.816   -25.534 1.00 29.76 ? 69  LYS C CD  1 
ATOM   4847 C  CE  . LYS C 1 69  ? 44.861  9.065   -24.905 1.00 28.14 ? 69  LYS C CE  1 
ATOM   4848 N  NZ  . LYS C 1 69  ? 44.746  10.227  -25.840 1.00 29.30 ? 69  LYS C NZ  1 
ATOM   4849 N  N   . LEU C 1 70  ? 45.645  3.159   -23.947 1.00 18.96 ? 70  LEU C N   1 
ATOM   4850 C  CA  . LEU C 1 70  ? 47.074  2.931   -23.734 1.00 20.85 ? 70  LEU C CA  1 
ATOM   4851 C  C   . LEU C 1 70  ? 47.889  3.527   -24.881 1.00 21.43 ? 70  LEU C C   1 
ATOM   4852 O  O   . LEU C 1 70  ? 47.695  3.122   -26.045 1.00 20.13 ? 70  LEU C O   1 
ATOM   4853 C  CB  . LEU C 1 70  ? 47.304  1.430   -23.600 1.00 16.22 ? 70  LEU C CB  1 
ATOM   4854 C  CG  . LEU C 1 70  ? 48.692  0.961   -23.252 1.00 20.11 ? 70  LEU C CG  1 
ATOM   4855 C  CD1 . LEU C 1 70  ? 48.973  1.517   -21.821 1.00 19.70 ? 70  LEU C CD1 1 
ATOM   4856 C  CD2 . LEU C 1 70  ? 48.843  -0.578  -23.329 1.00 18.88 ? 70  LEU C CD2 1 
ATOM   4857 N  N   . ASN C 1 71  ? 48.834  4.444   -24.587 1.00 20.27 ? 71  ASN C N   1 
ATOM   4858 C  CA  . ASN C 1 71  ? 49.756  4.900   -25.623 1.00 23.03 ? 71  ASN C CA  1 
ATOM   4859 C  C   . ASN C 1 71  ? 50.691  3.769   -26.100 1.00 20.64 ? 71  ASN C C   1 
ATOM   4860 O  O   . ASN C 1 71  ? 51.086  2.927   -25.311 1.00 20.58 ? 71  ASN C O   1 
ATOM   4861 C  CB  . ASN C 1 71  ? 50.553  6.142   -25.187 1.00 21.17 ? 71  ASN C CB  1 
ATOM   4862 C  CG  . ASN C 1 71  ? 49.671  7.352   -25.033 1.00 26.45 ? 71  ASN C CG  1 
ATOM   4863 O  OD1 . ASN C 1 71  ? 48.488  7.322   -25.418 1.00 23.50 ? 71  ASN C OD1 1 
ATOM   4864 N  ND2 . ASN C 1 71  ? 50.241  8.461   -24.523 1.00 25.26 ? 71  ASN C ND2 1 
ATOM   4865 N  N   . LEU C 1 72  ? 50.956  3.681   -27.414 1.00 18.44 ? 72  LEU C N   1 
ATOM   4866 C  CA  . LEU C 1 72  ? 51.786  2.602   -27.964 1.00 20.22 ? 72  LEU C CA  1 
ATOM   4867 C  C   . LEU C 1 72  ? 52.917  3.268   -28.780 1.00 19.30 ? 72  LEU C C   1 
ATOM   4868 O  O   . LEU C 1 72  ? 52.739  4.424   -29.263 1.00 19.61 ? 72  LEU C O   1 
ATOM   4869 C  CB  . LEU C 1 72  ? 50.958  1.766   -28.934 1.00 17.92 ? 72  LEU C CB  1 
ATOM   4870 C  CG  . LEU C 1 72  ? 49.852  0.993   -28.245 1.00 20.42 ? 72  LEU C CG  1 
ATOM   4871 C  CD1 . LEU C 1 72  ? 48.984  0.415   -29.347 1.00 19.74 ? 72  LEU C CD1 1 
ATOM   4872 C  CD2 . LEU C 1 72  ? 50.372  -0.127  -27.358 1.00 18.81 ? 72  LEU C CD2 1 
ATOM   4873 N  N   . PRO C 1 73  ? 54.107  2.631   -28.849 1.00 23.81 ? 73  PRO C N   1 
ATOM   4874 C  CA  . PRO C 1 73  ? 55.254  3.369   -29.431 1.00 26.02 ? 73  PRO C CA  1 
ATOM   4875 C  C   . PRO C 1 73  ? 55.280  3.275   -30.968 1.00 26.45 ? 73  PRO C C   1 
ATOM   4876 O  O   . PRO C 1 73  ? 54.838  2.298   -31.495 1.00 26.19 ? 73  PRO C O   1 
ATOM   4877 C  CB  . PRO C 1 73  ? 56.471  2.615   -28.860 1.00 27.10 ? 73  PRO C CB  1 
ATOM   4878 C  CG  . PRO C 1 73  ? 55.989  1.209   -28.707 1.00 24.72 ? 73  PRO C CG  1 
ATOM   4879 C  CD  . PRO C 1 73  ? 54.489  1.238   -28.458 1.00 23.92 ? 73  PRO C CD  1 
ATOM   4880 N  N   . SER C 1 74  ? 55.826  4.276   -31.649 1.00 28.68 ? 74  SER C N   1 
ATOM   4881 C  CA  . SER C 1 74  ? 55.728  4.338   -33.100 1.00 29.74 ? 74  SER C CA  1 
ATOM   4882 C  C   . SER C 1 74  ? 56.597  3.324   -33.867 1.00 30.05 ? 74  SER C C   1 
ATOM   4883 O  O   . SER C 1 74  ? 56.372  3.094   -35.056 1.00 30.28 ? 74  SER C O   1 
ATOM   4884 C  CB  . SER C 1 74  ? 55.932  5.785   -33.600 1.00 33.13 ? 74  SER C CB  1 
ATOM   4885 O  OG  . SER C 1 74  ? 57.219  6.266   -33.238 1.00 33.36 ? 74  SER C OG  1 
ATOM   4886 N  N   . ASP C 1 75  ? 57.590  2.705   -33.229 1.00 27.37 ? 75  ASP C N   1 
ATOM   4887 C  CA  . ASP C 1 75  ? 58.328  1.631   -33.921 1.00 27.29 ? 75  ASP C CA  1 
ATOM   4888 C  C   . ASP C 1 75  ? 57.493  0.328   -33.921 1.00 23.85 ? 75  ASP C C   1 
ATOM   4889 O  O   . ASP C 1 75  ? 57.838  -0.668  -34.568 1.00 25.72 ? 75  ASP C O   1 
ATOM   4890 C  CB  . ASP C 1 75  ? 59.688  1.380   -33.254 1.00 31.84 ? 75  ASP C CB  1 
ATOM   4891 C  CG  . ASP C 1 75  ? 59.510  0.854   -31.875 1.00 35.35 ? 75  ASP C CG  1 
ATOM   4892 O  OD1 . ASP C 1 75  ? 59.253  1.684   -30.973 1.00 34.45 ? 75  ASP C OD1 1 
ATOM   4893 O  OD2 . ASP C 1 75  ? 59.555  -0.398  -31.725 1.00 41.82 ? 75  ASP C OD2 1 
ATOM   4894 N  N   . MET C 1 76  ? 56.358  0.341   -33.245 1.00 22.21 ? 76  MET C N   1 
ATOM   4895 C  CA  . MET C 1 76  ? 55.413  -0.791  -33.372 1.00 20.92 ? 76  MET C CA  1 
ATOM   4896 C  C   . MET C 1 76  ? 54.541  -0.611  -34.648 1.00 18.93 ? 76  MET C C   1 
ATOM   4897 O  O   . MET C 1 76  ? 54.048  0.496   -34.869 1.00 20.49 ? 76  MET C O   1 
ATOM   4898 C  CB  . MET C 1 76  ? 54.539  -0.810  -32.134 1.00 23.51 ? 76  MET C CB  1 
ATOM   4899 C  CG  . MET C 1 76  ? 53.412  -1.807  -32.111 1.00 21.93 ? 76  MET C CG  1 
ATOM   4900 S  SD  . MET C 1 76  ? 52.706  -1.706  -30.437 1.00 24.91 ? 76  MET C SD  1 
ATOM   4901 C  CE  . MET C 1 76  ? 51.124  -2.494  -30.831 1.00 24.21 ? 76  MET C CE  1 
ATOM   4902 N  N   . HIS C 1 77  ? 54.367  -1.651  -35.447 1.00 17.68 ? 77  HIS C N   1 
ATOM   4903 C  CA  . HIS C 1 77  ? 53.781  -1.469  -36.810 1.00 23.08 ? 77  HIS C CA  1 
ATOM   4904 C  C   . HIS C 1 77  ? 53.178  -2.704  -37.481 1.00 21.61 ? 77  HIS C C   1 
ATOM   4905 O  O   . HIS C 1 77  ? 53.518  -3.854  -37.203 1.00 19.65 ? 77  HIS C O   1 
ATOM   4906 C  CB  . HIS C 1 77  ? 54.733  -0.653  -37.732 1.00 24.58 ? 77  HIS C CB  1 
ATOM   4907 C  CG  . HIS C 1 77  ? 55.957  -1.416  -38.161 1.00 26.25 ? 77  HIS C CG  1 
ATOM   4908 N  ND1 . HIS C 1 77  ? 57.171  -1.161  -37.662 1.00 30.08 ? 77  HIS C ND1 1 
ATOM   4909 C  CD2 . HIS C 1 77  ? 56.120  -2.425  -39.116 1.00 30.14 ? 77  HIS C CD2 1 
ATOM   4910 C  CE1 . HIS C 1 77  ? 58.066  -1.983  -38.233 1.00 29.20 ? 77  HIS C CE1 1 
ATOM   4911 N  NE2 . HIS C 1 77  ? 57.424  -2.759  -39.124 1.00 32.63 ? 77  HIS C NE2 1 
ATOM   4912 N  N   . ILE C 1 78  ? 52.204  -2.443  -38.368 1.00 20.66 ? 78  ILE C N   1 
ATOM   4913 C  CA  . ILE C 1 78  ? 51.730  -3.502  -39.235 1.00 19.64 ? 78  ILE C CA  1 
ATOM   4914 C  C   . ILE C 1 78  ? 52.467  -3.569  -40.581 1.00 21.08 ? 78  ILE C C   1 
ATOM   4915 O  O   . ILE C 1 78  ? 52.663  -2.557  -41.239 1.00 25.52 ? 78  ILE C O   1 
ATOM   4916 C  CB  . ILE C 1 78  ? 50.213  -3.324  -39.565 1.00 20.58 ? 78  ILE C CB  1 
ATOM   4917 C  CG1 . ILE C 1 78  ? 49.373  -3.224  -38.328 1.00 21.19 ? 78  ILE C CG1 1 
ATOM   4918 C  CG2 . ILE C 1 78  ? 49.705  -4.477  -40.410 1.00 23.92 ? 78  ILE C CG2 1 
ATOM   4919 C  CD1 . ILE C 1 78  ? 48.011  -2.599  -38.648 1.00 21.44 ? 78  ILE C CD1 1 
ATOM   4920 N  N   . GLN C 1 79  ? 52.853  -4.786  -40.932 1.00 24.18 ? 79  GLN C N   1 
ATOM   4921 C  CA  . GLN C 1 79  ? 53.497  -5.141  -42.165 1.00 27.78 ? 79  GLN C CA  1 
ATOM   4922 C  C   . GLN C 1 79  ? 52.483  -5.940  -42.972 1.00 28.16 ? 79  GLN C C   1 
ATOM   4923 O  O   . GLN C 1 79  ? 51.869  -6.846  -42.426 1.00 25.55 ? 79  GLN C O   1 
ATOM   4924 C  CB  . GLN C 1 79  ? 54.635  -6.106  -41.747 1.00 31.36 ? 79  GLN C CB  1 
ATOM   4925 C  CG  . GLN C 1 79  ? 55.451  -6.755  -42.852 1.00 42.01 ? 79  GLN C CG  1 
ATOM   4926 C  CD  . GLN C 1 79  ? 56.614  -5.864  -43.214 1.00 48.42 ? 79  GLN C CD  1 
ATOM   4927 O  OE1 . GLN C 1 79  ? 56.404  -4.707  -43.606 1.00 51.40 ? 79  GLN C OE1 1 
ATOM   4928 N  NE2 . GLN C 1 79  ? 57.848  -6.367  -43.035 1.00 47.41 ? 79  GLN C NE2 1 
ATOM   4929 N  N   . GLY C 1 80  ? 52.308  -5.631  -44.262 1.00 24.11 ? 80  GLY C N   1 
ATOM   4930 C  CA  . GLY C 1 80  ? 51.400  -6.403  -45.121 1.00 27.00 ? 80  GLY C CA  1 
ATOM   4931 C  C   . GLY C 1 80  ? 50.366  -5.566  -45.830 1.00 26.07 ? 80  GLY C C   1 
ATOM   4932 O  O   . GLY C 1 80  ? 49.658  -6.037  -46.744 1.00 27.73 ? 80  GLY C O   1 
ATOM   4933 N  N   . LEU C 1 81  ? 50.279  -4.290  -45.460 1.00 26.67 ? 81  LEU C N   1 
ATOM   4934 C  CA  . LEU C 1 81  ? 49.340  -3.386  -46.111 1.00 27.14 ? 81  LEU C CA  1 
ATOM   4935 C  C   . LEU C 1 81  ? 50.101  -2.535  -47.157 1.00 29.05 ? 81  LEU C C   1 
ATOM   4936 O  O   . LEU C 1 81  ? 51.330  -2.695  -47.304 1.00 30.28 ? 81  LEU C O   1 
ATOM   4937 C  CB  . LEU C 1 81  ? 48.637  -2.493  -45.073 1.00 26.11 ? 81  LEU C CB  1 
ATOM   4938 C  CG  . LEU C 1 81  ? 47.731  -3.275  -44.139 1.00 25.63 ? 81  LEU C CG  1 
ATOM   4939 C  CD1 . LEU C 1 81  ? 47.265  -2.483  -42.928 1.00 23.11 ? 81  LEU C CD1 1 
ATOM   4940 C  CD2 . LEU C 1 81  ? 46.483  -3.803  -44.860 1.00 25.91 ? 81  LEU C CD2 1 
ATOM   4941 N  N   . GLN C 1 82  ? 49.412  -1.651  -47.868 1.00 30.47 ? 82  GLN C N   1 
ATOM   4942 C  CA  . GLN C 1 82  ? 50.045  -0.900  -48.982 1.00 30.58 ? 82  GLN C CA  1 
ATOM   4943 C  C   . GLN C 1 82  ? 51.074  0.091   -48.508 1.00 29.14 ? 82  GLN C C   1 
ATOM   4944 O  O   . GLN C 1 82  ? 51.938  0.484   -49.294 1.00 30.04 ? 82  GLN C O   1 
ATOM   4945 C  CB  . GLN C 1 82  ? 49.014  -0.185  -49.897 1.00 38.01 ? 82  GLN C CB  1 
ATOM   4946 C  CG  . GLN C 1 82  ? 48.360  -1.079  -50.966 1.00 45.90 ? 82  GLN C CG  1 
ATOM   4947 C  CD  . GLN C 1 82  ? 49.350  -1.820  -51.879 1.00 48.81 ? 82  GLN C CD  1 
ATOM   4948 O  OE1 . GLN C 1 82  ? 49.198  -3.022  -52.092 1.00 46.50 ? 82  GLN C OE1 1 
ATOM   4949 N  NE2 . GLN C 1 82  ? 50.355  -1.099  -52.439 1.00 46.78 ? 82  GLN C NE2 1 
ATOM   4950 N  N   . SER C 1 83  ? 51.002  0.483   -47.236 1.00 21.83 ? 83  SER C N   1 
ATOM   4951 C  CA  . SER C 1 83  ? 51.931  1.397   -46.627 1.00 21.23 ? 83  SER C CA  1 
ATOM   4952 C  C   . SER C 1 83  ? 52.180  0.796   -45.259 1.00 20.21 ? 83  SER C C   1 
ATOM   4953 O  O   . SER C 1 83  ? 51.354  0.046   -44.778 1.00 18.30 ? 83  SER C O   1 
ATOM   4954 C  CB  . SER C 1 83  ? 51.336  2.810   -46.428 1.00 21.94 ? 83  SER C CB  1 
ATOM   4955 O  OG  . SER C 1 83  ? 50.963  3.421   -47.683 1.00 24.25 ? 83  SER C OG  1 
ATOM   4956 N  N   A ARG C 1 84  ? 53.326  1.039   -44.628 0.50 19.15 ? 84  ARG C N   1 
ATOM   4957 N  N   B ARG C 1 84  ? 53.263  1.265   -44.608 0.50 17.28 ? 84  ARG C N   1 
ATOM   4958 C  CA  A ARG C 1 84  ? 53.417  0.603   -43.220 0.50 18.20 ? 84  ARG C CA  1 
ATOM   4959 C  CA  B ARG C 1 84  ? 53.474  1.032   -43.168 0.50 15.13 ? 84  ARG C CA  1 
ATOM   4960 C  C   A ARG C 1 84  ? 52.507  1.536   -42.406 0.50 17.08 ? 84  ARG C C   1 
ATOM   4961 C  C   B ARG C 1 84  ? 52.509  1.740   -42.239 0.50 15.96 ? 84  ARG C C   1 
ATOM   4962 O  O   A ARG C 1 84  ? 52.371  2.708   -42.761 0.50 15.14 ? 84  ARG C O   1 
ATOM   4963 O  O   B ARG C 1 84  ? 52.465  2.983   -42.199 0.50 16.50 ? 84  ARG C O   1 
ATOM   4964 C  CB  A ARG C 1 84  ? 54.900  0.546   -42.789 0.50 19.09 ? 84  ARG C CB  1 
ATOM   4965 C  CB  B ARG C 1 84  ? 54.900  1.439   -42.740 0.50 13.25 ? 84  ARG C CB  1 
ATOM   4966 C  CG  A ARG C 1 84  ? 55.204  0.519   -41.300 0.50 18.79 ? 84  ARG C CG  1 
ATOM   4967 C  CG  B ARG C 1 84  ? 55.090  1.359   -41.223 0.50 12.63 ? 84  ARG C CG  1 
ATOM   4968 C  CD  A ARG C 1 84  ? 56.449  1.416   -41.069 0.50 20.38 ? 84  ARG C CD  1 
ATOM   4969 C  CD  B ARG C 1 84  ? 56.539  1.177   -40.761 0.50 12.44 ? 84  ARG C CD  1 
ATOM   4970 N  NE  A ARG C 1 84  ? 56.342  2.694   -41.796 0.50 20.57 ? 84  ARG C NE  1 
ATOM   4971 N  NE  B ARG C 1 84  ? 57.251  0.068   -41.435 0.50 10.19 ? 84  ARG C NE  1 
ATOM   4972 C  CZ  A ARG C 1 84  ? 57.054  3.778   -41.489 0.50 21.01 ? 84  ARG C CZ  1 
ATOM   4973 C  CZ  B ARG C 1 84  ? 58.553  -0.104  -41.205 0.50 13.18 ? 84  ARG C CZ  1 
ATOM   4974 N  NH1 A ARG C 1 84  ? 57.972  3.727   -40.495 0.50 23.69 ? 84  ARG C NH1 1 
ATOM   4975 N  NH1 B ARG C 1 84  ? 59.124  0.762   -40.382 0.50 11.91 ? 84  ARG C NH1 1 
ATOM   4976 N  NH2 A ARG C 1 84  ? 56.861  4.898   -42.129 0.50 17.90 ? 84  ARG C NH2 1 
ATOM   4977 N  NH2 B ARG C 1 84  ? 59.254  -1.085  -41.798 0.50 12.28 ? 84  ARG C NH2 1 
ATOM   4978 N  N   . TYR C 1 85  ? 51.815  0.977   -41.395 1.00 17.56 ? 85  TYR C N   1 
ATOM   4979 C  CA  . TYR C 1 85  ? 51.015  1.689   -40.409 1.00 16.80 ? 85  TYR C CA  1 
ATOM   4980 C  C   . TYR C 1 85  ? 51.653  1.448   -39.038 1.00 17.87 ? 85  TYR C C   1 
ATOM   4981 O  O   . TYR C 1 85  ? 51.857  0.299   -38.654 1.00 16.54 ? 85  TYR C O   1 
ATOM   4982 C  CB  . TYR C 1 85  ? 49.555  1.144   -40.449 1.00 15.80 ? 85  TYR C CB  1 
ATOM   4983 C  CG  . TYR C 1 85  ? 48.777  1.657   -41.658 1.00 16.12 ? 85  TYR C CG  1 
ATOM   4984 C  CD1 . TYR C 1 85  ? 47.973  2.798   -41.537 1.00 16.89 ? 85  TYR C CD1 1 
ATOM   4985 C  CD2 . TYR C 1 85  ? 48.930  1.089   -42.916 1.00 16.22 ? 85  TYR C CD2 1 
ATOM   4986 C  CE1 . TYR C 1 85  ? 47.239  3.275   -42.631 1.00 15.82 ? 85  TYR C CE1 1 
ATOM   4987 C  CE2 . TYR C 1 85  ? 48.195  1.544   -44.000 1.00 15.21 ? 85  TYR C CE2 1 
ATOM   4988 C  CZ  . TYR C 1 85  ? 47.367  2.659   -43.856 1.00 17.91 ? 85  TYR C CZ  1 
ATOM   4989 O  OH  . TYR C 1 85  ? 46.659  3.151   -44.941 1.00 18.50 ? 85  TYR C OH  1 
ATOM   4990 N  N   . SER C 1 86  ? 52.028  2.538   -38.368 1.00 18.66 ? 86  SER C N   1 
ATOM   4991 C  CA  . SER C 1 86  ? 52.626  2.524   -37.059 1.00 19.30 ? 86  SER C CA  1 
ATOM   4992 C  C   . SER C 1 86  ? 51.608  2.751   -35.940 1.00 18.50 ? 86  SER C C   1 
ATOM   4993 O  O   . SER C 1 86  ? 50.692  3.621   -36.050 1.00 18.83 ? 86  SER C O   1 
ATOM   4994 C  CB  . SER C 1 86  ? 53.770  3.519   -36.985 1.00 21.14 ? 86  SER C CB  1 
ATOM   4995 O  OG  . SER C 1 86  ? 54.720  3.176   -37.988 1.00 21.31 ? 86  SER C OG  1 
ATOM   4996 N  N   . ALA C 1 87  ? 51.804  2.013   -34.861 1.00 19.18 ? 87  ALA C N   1 
ATOM   4997 C  CA  . ALA C 1 87  ? 50.917  2.164   -33.637 1.00 16.92 ? 87  ALA C CA  1 
ATOM   4998 C  C   . ALA C 1 87  ? 50.916  3.541   -33.012 1.00 18.16 ? 87  ALA C C   1 
ATOM   4999 O  O   . ALA C 1 87  ? 51.942  4.297   -33.047 1.00 15.79 ? 87  ALA C O   1 
ATOM   5000 C  CB  . ALA C 1 87  ? 51.154  1.063   -32.649 1.00 16.24 ? 87  ALA C CB  1 
ATOM   5001 N  N   . THR C 1 88  ? 49.730  3.926   -32.519 1.00 16.08 ? 88  THR C N   1 
ATOM   5002 C  CA  . THR C 1 88  ? 49.593  5.105   -31.689 1.00 16.90 ? 88  THR C CA  1 
ATOM   5003 C  C   . THR C 1 88  ? 48.950  4.840   -30.326 1.00 18.11 ? 88  THR C C   1 
ATOM   5004 O  O   . THR C 1 88  ? 49.430  5.378   -29.315 1.00 16.38 ? 88  THR C O   1 
ATOM   5005 C  CB  . THR C 1 88  ? 48.965  6.243   -32.454 1.00 17.99 ? 88  THR C CB  1 
ATOM   5006 O  OG1 . THR C 1 88  ? 48.942  7.389   -31.651 1.00 16.57 ? 88  THR C OG1 1 
ATOM   5007 C  CG2 . THR C 1 88  ? 47.554  5.911   -32.966 1.00 15.70 ? 88  THR C CG2 1 
ATOM   5008 N  N   . GLN C 1 89  ? 47.898  3.991   -30.265 1.00 16.52 ? 89  GLN C N   1 
ATOM   5009 C  CA  . GLN C 1 89  ? 47.239  3.774   -28.941 1.00 15.88 ? 89  GLN C CA  1 
ATOM   5010 C  C   . GLN C 1 89  ? 46.296  2.616   -29.159 1.00 17.37 ? 89  GLN C C   1 
ATOM   5011 O  O   . GLN C 1 89  ? 45.945  2.285   -30.336 1.00 15.93 ? 89  GLN C O   1 
ATOM   5012 C  CB  . GLN C 1 89  ? 46.521  5.022   -28.440 1.00 17.07 ? 89  GLN C CB  1 
ATOM   5013 C  CG  . GLN C 1 89  ? 45.471  5.621   -29.372 1.00 17.94 ? 89  GLN C CG  1 
ATOM   5014 C  CD  . GLN C 1 89  ? 44.048  5.278   -28.930 1.00 17.70 ? 89  GLN C CD  1 
ATOM   5015 O  OE1 . GLN C 1 89  ? 43.743  4.119   -28.808 1.00 18.99 ? 89  GLN C OE1 1 
ATOM   5016 N  NE2 . GLN C 1 89  ? 43.228  6.264   -28.674 1.00 20.68 ? 89  GLN C NE2 1 
ATOM   5017 N  N   . LEU C 1 90  ? 45.890  1.998   -28.061 1.00 16.32 ? 90  LEU C N   1 
ATOM   5018 C  CA  . LEU C 1 90  ? 44.810  0.993   -28.132 1.00 15.57 ? 90  LEU C CA  1 
ATOM   5019 C  C   . LEU C 1 90  ? 43.777  1.418   -27.067 1.00 16.75 ? 90  LEU C C   1 
ATOM   5020 O  O   . LEU C 1 90  ? 44.080  2.159   -26.130 1.00 18.32 ? 90  LEU C O   1 
ATOM   5021 C  CB  . LEU C 1 90  ? 45.272  -0.432  -27.944 1.00 13.66 ? 90  LEU C CB  1 
ATOM   5022 C  CG  . LEU C 1 90  ? 45.964  -0.799  -26.643 1.00 15.76 ? 90  LEU C CG  1 
ATOM   5023 C  CD1 . LEU C 1 90  ? 44.980  -0.902  -25.487 1.00 19.82 ? 90  LEU C CD1 1 
ATOM   5024 C  CD2 . LEU C 1 90  ? 46.563  -2.162  -26.910 1.00 15.18 ? 90  LEU C CD2 1 
ATOM   5025 N  N   . HIS C 1 91  ? 42.517  1.021   -27.279 1.00 17.05 ? 91  HIS C N   1 
ATOM   5026 C  CA  . HIS C 1 91  ? 41.427  1.307   -26.302 1.00 14.99 ? 91  HIS C CA  1 
ATOM   5027 C  C   . HIS C 1 91  ? 40.335  0.228   -26.476 1.00 16.19 ? 91  HIS C C   1 
ATOM   5028 O  O   . HIS C 1 91  ? 40.441  -0.595  -27.343 1.00 15.99 ? 91  HIS C O   1 
ATOM   5029 C  CB  . HIS C 1 91  ? 40.863  2.694   -26.522 1.00 17.20 ? 91  HIS C CB  1 
ATOM   5030 C  CG  . HIS C 1 91  ? 40.333  2.874   -27.921 1.00 16.13 ? 91  HIS C CG  1 
ATOM   5031 N  ND1 . HIS C 1 91  ? 41.107  3.342   -28.926 1.00 15.39 ? 91  HIS C ND1 1 
ATOM   5032 C  CD2 . HIS C 1 91  ? 39.104  2.548   -28.486 1.00 14.29 ? 91  HIS C CD2 1 
ATOM   5033 C  CE1 . HIS C 1 91  ? 40.456  3.297   -30.068 1.00 13.70 ? 91  HIS C CE1 1 
ATOM   5034 N  NE2 . HIS C 1 91  ? 39.215  2.820   -29.823 1.00 11.88 ? 91  HIS C NE2 1 
ATOM   5035 N  N   . LEU C 1 92  ? 39.263  0.321   -25.657 1.00 16.99 ? 92  LEU C N   1 
ATOM   5036 C  CA  . LEU C 1 92  ? 38.163  -0.650  -25.631 1.00 16.13 ? 92  LEU C CA  1 
ATOM   5037 C  C   . LEU C 1 92  ? 36.866  0.048   -25.620 1.00 12.75 ? 92  LEU C C   1 
ATOM   5038 O  O   . LEU C 1 92  ? 36.735  1.256   -25.377 1.00 14.81 ? 92  LEU C O   1 
ATOM   5039 C  CB  . LEU C 1 92  ? 38.216  -1.597  -24.388 1.00 18.61 ? 92  LEU C CB  1 
ATOM   5040 C  CG  . LEU C 1 92  ? 39.417  -2.523  -24.526 1.00 20.07 ? 92  LEU C CG  1 
ATOM   5041 C  CD1 . LEU C 1 92  ? 40.464  -1.939  -23.594 1.00 21.97 ? 92  LEU C CD1 1 
ATOM   5042 C  CD2 . LEU C 1 92  ? 39.142  -3.954  -24.152 1.00 22.70 ? 92  LEU C CD2 1 
ATOM   5043 N  N   . HIS C 1 93  ? 35.856  -0.751  -25.986 1.00 13.40 ? 93  HIS C N   1 
ATOM   5044 C  CA  . HIS C 1 93  ? 34.423  -0.347  -25.982 1.00 12.64 ? 93  HIS C CA  1 
ATOM   5045 C  C   . HIS C 1 93  ? 33.688  -1.504  -25.316 1.00 12.24 ? 93  HIS C C   1 
ATOM   5046 O  O   . HIS C 1 93  ? 33.976  -2.699  -25.563 1.00 12.77 ? 93  HIS C O   1 
ATOM   5047 C  CB  . HIS C 1 93  ? 33.913  -0.185  -27.443 1.00 12.76 ? 93  HIS C CB  1 
ATOM   5048 C  CG  . HIS C 1 93  ? 34.687  0.834   -28.245 1.00 10.51 ? 93  HIS C CG  1 
ATOM   5049 N  ND1 . HIS C 1 93  ? 34.388  2.115   -28.221 1.00 12.54 ? 93  HIS C ND1 1 
ATOM   5050 C  CD2 . HIS C 1 93  ? 35.812  0.708   -29.087 1.00 11.73 ? 93  HIS C CD2 1 
ATOM   5051 C  CE1 . HIS C 1 93  ? 35.249  2.808   -29.023 1.00 10.96 ? 93  HIS C CE1 1 
ATOM   5052 N  NE2 . HIS C 1 93  ? 36.083  1.949   -29.556 1.00 11.32 ? 93  HIS C NE2 1 
ATOM   5053 N  N   . TRP C 1 94  ? 32.733  -1.097  -24.456 1.00 13.89 ? 94  TRP C N   1 
ATOM   5054 C  CA  . TRP C 1 94  ? 31.907  -2.040  -23.697 1.00 15.88 ? 94  TRP C CA  1 
ATOM   5055 C  C   . TRP C 1 94  ? 30.534  -1.533  -23.444 1.00 14.57 ? 94  TRP C C   1 
ATOM   5056 O  O   . TRP C 1 94  ? 30.217  -0.367  -23.742 1.00 14.31 ? 94  TRP C O   1 
ATOM   5057 C  CB  . TRP C 1 94  ? 32.630  -2.465  -22.363 1.00 16.98 ? 94  TRP C CB  1 
ATOM   5058 C  CG  . TRP C 1 94  ? 32.933  -1.287  -21.461 1.00 17.70 ? 94  TRP C CG  1 
ATOM   5059 C  CD1 . TRP C 1 94  ? 32.127  -0.760  -20.455 1.00 17.44 ? 94  TRP C CD1 1 
ATOM   5060 C  CD2 . TRP C 1 94  ? 34.137  -0.436  -21.465 1.00 15.39 ? 94  TRP C CD2 1 
ATOM   5061 N  NE1 . TRP C 1 94  ? 32.732  0.314   -19.855 1.00 18.19 ? 94  TRP C NE1 1 
ATOM   5062 C  CE2 . TRP C 1 94  ? 33.936  0.562   -20.412 1.00 16.82 ? 94  TRP C CE2 1 
ATOM   5063 C  CE3 . TRP C 1 94  ? 35.311  -0.406  -22.203 1.00 17.76 ? 94  TRP C CE3 1 
ATOM   5064 C  CZ2 . TRP C 1 94  ? 34.881  1.532   -20.130 1.00 16.14 ? 94  TRP C CZ2 1 
ATOM   5065 C  CZ3 . TRP C 1 94  ? 36.257  0.579   -21.908 1.00 16.04 ? 94  TRP C CZ3 1 
ATOM   5066 C  CH2 . TRP C 1 94  ? 36.044  1.523   -20.896 1.00 17.56 ? 94  TRP C CH2 1 
ATOM   5067 N  N   . GLY C 1 95  ? 29.729  -2.444  -22.854 1.00 16.97 ? 95  GLY C N   1 
ATOM   5068 C  CA  . GLY C 1 95  ? 28.357  -2.141  -22.488 1.00 16.54 ? 95  GLY C CA  1 
ATOM   5069 C  C   . GLY C 1 95  ? 28.194  -1.811  -21.011 1.00 17.82 ? 95  GLY C C   1 
ATOM   5070 O  O   . GLY C 1 95  ? 28.740  -0.837  -20.493 1.00 16.90 ? 95  GLY C O   1 
ATOM   5071 N  N   . ASN C 1 96  ? 27.290  -2.547  -20.366 1.00 17.77 ? 96  ASN C N   1 
ATOM   5072 C  CA  . ASN C 1 96  ? 26.964  -2.255  -18.908 1.00 17.68 ? 96  ASN C CA  1 
ATOM   5073 C  C   . ASN C 1 96  ? 26.534  -3.576  -18.299 1.00 17.22 ? 96  ASN C C   1 
ATOM   5074 O  O   . ASN C 1 96  ? 26.215  -4.501  -19.022 1.00 18.58 ? 96  ASN C O   1 
ATOM   5075 C  CB  . ASN C 1 96  ? 25.945  -1.089  -18.779 1.00 20.38 ? 96  ASN C CB  1 
ATOM   5076 C  CG  . ASN C 1 96  ? 24.525  -1.490  -19.108 1.00 26.61 ? 96  ASN C CG  1 
ATOM   5077 O  OD1 . ASN C 1 96  ? 23.773  -1.908  -18.222 1.00 27.55 ? 96  ASN C OD1 1 
ATOM   5078 N  ND2 . ASN C 1 96  ? 24.128  -1.305  -20.367 1.00 25.84 ? 96  ASN C ND2 1 
ATOM   5079 N  N   . PRO C 1 97  ? 26.590  -3.735  -16.951 1.00 19.98 ? 97  PRO C N   1 
ATOM   5080 C  CA  . PRO C 1 97  ? 26.227  -5.011  -16.363 1.00 20.72 ? 97  PRO C CA  1 
ATOM   5081 C  C   . PRO C 1 97  ? 24.817  -5.496  -16.687 1.00 20.11 ? 97  PRO C C   1 
ATOM   5082 O  O   . PRO C 1 97  ? 24.557  -6.729  -16.672 1.00 22.67 ? 97  PRO C O   1 
ATOM   5083 C  CB  . PRO C 1 97  ? 26.282  -4.690  -14.850 1.00 20.26 ? 97  PRO C CB  1 
ATOM   5084 C  CG  . PRO C 1 97  ? 27.464  -3.813  -14.778 1.00 20.48 ? 97  PRO C CG  1 
ATOM   5085 C  CD  . PRO C 1 97  ? 27.298  -2.885  -15.959 1.00 21.80 ? 97  PRO C CD  1 
ATOM   5086 N  N   . ASN C 1 98  ? 23.912  -4.545  -16.923 1.00 20.86 ? 98  ASN C N   1 
ATOM   5087 C  CA  . ASN C 1 98  ? 22.516  -4.940  -17.229 1.00 22.87 ? 98  ASN C CA  1 
ATOM   5088 C  C   . ASN C 1 98  ? 22.339  -5.386  -18.674 1.00 23.48 ? 98  ASN C C   1 
ATOM   5089 O  O   . ASN C 1 98  ? 21.361  -6.063  -18.990 1.00 22.83 ? 98  ASN C O   1 
ATOM   5090 C  CB  . ASN C 1 98  ? 21.551  -3.806  -16.924 1.00 25.28 ? 98  ASN C CB  1 
ATOM   5091 C  CG  . ASN C 1 98  ? 21.421  -3.569  -15.453 1.00 29.70 ? 98  ASN C CG  1 
ATOM   5092 O  OD1 . ASN C 1 98  ? 21.372  -4.525  -14.664 1.00 31.90 ? 98  ASN C OD1 1 
ATOM   5093 N  ND2 . ASN C 1 98  ? 21.381  -2.305  -15.067 1.00 33.82 ? 98  ASN C ND2 1 
ATOM   5094 N  N   . ASP C 1 99  ? 23.268  -5.007  -19.546 1.00 21.65 ? 99  ASP C N   1 
ATOM   5095 C  CA  . ASP C 1 99  ? 23.185  -5.388  -20.979 1.00 19.02 ? 99  ASP C CA  1 
ATOM   5096 C  C   . ASP C 1 99  ? 24.655  -5.451  -21.471 1.00 18.73 ? 99  ASP C C   1 
ATOM   5097 O  O   . ASP C 1 99  ? 25.171  -4.420  -22.009 1.00 19.15 ? 99  ASP C O   1 
ATOM   5098 C  CB  . ASP C 1 99  ? 22.417  -4.280  -21.714 1.00 19.42 ? 99  ASP C CB  1 
ATOM   5099 C  CG  . ASP C 1 99  ? 21.954  -4.677  -23.092 1.00 20.67 ? 99  ASP C CG  1 
ATOM   5100 O  OD1 . ASP C 1 99  ? 22.077  -5.834  -23.436 1.00 23.15 ? 99  ASP C OD1 1 
ATOM   5101 O  OD2 . ASP C 1 99  ? 21.442  -3.795  -23.831 1.00 22.66 ? 99  ASP C OD2 1 
ATOM   5102 N  N   . PRO C 1 100 ? 25.314  -6.587  -21.243 1.00 18.16 ? 100 PRO C N   1 
ATOM   5103 C  CA  . PRO C 1 100 ? 26.768  -6.673  -21.358 1.00 17.82 ? 100 PRO C CA  1 
ATOM   5104 C  C   . PRO C 1 100 ? 27.143  -7.035  -22.779 1.00 17.17 ? 100 PRO C C   1 
ATOM   5105 O  O   . PRO C 1 100 ? 27.702  -8.094  -23.058 1.00 16.94 ? 100 PRO C O   1 
ATOM   5106 C  CB  . PRO C 1 100 ? 27.122  -7.784  -20.379 1.00 19.96 ? 100 PRO C CB  1 
ATOM   5107 C  CG  . PRO C 1 100 ? 25.888  -8.654  -20.289 1.00 23.15 ? 100 PRO C CG  1 
ATOM   5108 C  CD  . PRO C 1 100 ? 24.778  -7.664  -20.373 1.00 20.65 ? 100 PRO C CD  1 
ATOM   5109 N  N   . HIS C 1 101 ? 26.736  -6.155  -23.695 1.00 15.38 ? 101 HIS C N   1 
ATOM   5110 C  CA  . HIS C 1 101 ? 26.894  -6.419  -25.173 1.00 16.16 ? 101 HIS C CA  1 
ATOM   5111 C  C   . HIS C 1 101 ? 27.267  -5.140  -25.842 1.00 17.09 ? 101 HIS C C   1 
ATOM   5112 O  O   . HIS C 1 101 ? 26.442  -4.576  -26.557 1.00 19.75 ? 101 HIS C O   1 
ATOM   5113 C  CB  . HIS C 1 101 ? 25.581  -6.935  -25.760 1.00 19.00 ? 101 HIS C CB  1 
ATOM   5114 C  CG  . HIS C 1 101 ? 25.012  -8.137  -25.008 1.00 19.69 ? 101 HIS C CG  1 
ATOM   5115 N  ND1 . HIS C 1 101 ? 25.535  -9.406  -25.089 1.00 19.29 ? 101 HIS C ND1 1 
ATOM   5116 C  CD2 . HIS C 1 101 ? 24.001  -8.178  -24.027 1.00 20.37 ? 101 HIS C CD2 1 
ATOM   5117 C  CE1 . HIS C 1 101 ? 24.852  -10.196 -24.237 1.00 22.99 ? 101 HIS C CE1 1 
ATOM   5118 N  NE2 . HIS C 1 101 ? 23.928  -9.430  -23.581 1.00 21.33 ? 101 HIS C NE2 1 
ATOM   5119 N  N   . GLY C 1 102 ? 28.538  -4.744  -25.723 1.00 13.79 ? 102 GLY C N   1 
ATOM   5120 C  CA  . GLY C 1 102 ? 28.926  -3.388  -26.113 1.00 14.50 ? 102 GLY C CA  1 
ATOM   5121 C  C   . GLY C 1 102 ? 30.040  -3.323  -27.145 1.00 14.83 ? 102 GLY C C   1 
ATOM   5122 O  O   . GLY C 1 102 ? 30.702  -2.251  -27.258 1.00 15.75 ? 102 GLY C O   1 
ATOM   5123 N  N   . SER C 1 103 ? 30.172  -4.376  -27.946 1.00 14.59 ? 103 SER C N   1 
ATOM   5124 C  CA  . SER C 1 103 ? 31.009  -4.251  -29.176 1.00 13.88 ? 103 SER C CA  1 
ATOM   5125 C  C   . SER C 1 103 ? 30.484  -3.161  -30.103 1.00 16.67 ? 103 SER C C   1 
ATOM   5126 O  O   . SER C 1 103 ? 29.298  -2.784  -30.023 1.00 15.21 ? 103 SER C O   1 
ATOM   5127 C  CB  . SER C 1 103 ? 31.209  -5.556  -29.921 1.00 13.94 ? 103 SER C CB  1 
ATOM   5128 O  OG  . SER C 1 103 ? 29.969  -5.968  -30.514 1.00 12.51 ? 103 SER C OG  1 
ATOM   5129 N  N   . GLU C 1 104 ? 31.363  -2.630  -30.961 1.00 13.39 ? 104 GLU C N   1 
ATOM   5130 C  CA  . GLU C 1 104 ? 30.944  -1.642  -31.919 1.00 12.53 ? 104 GLU C CA  1 
ATOM   5131 C  C   . GLU C 1 104 ? 30.496  -2.335  -33.208 1.00 11.45 ? 104 GLU C C   1 
ATOM   5132 O  O   . GLU C 1 104 ? 29.354  -2.170  -33.654 1.00 10.15 ? 104 GLU C O   1 
ATOM   5133 C  CB  . GLU C 1 104 ? 32.086  -0.633  -32.229 1.00 13.02 ? 104 GLU C CB  1 
ATOM   5134 C  CG  . GLU C 1 104 ? 32.613  0.043   -30.983 1.00 12.52 ? 104 GLU C CG  1 
ATOM   5135 C  CD  . GLU C 1 104 ? 32.952  1.463   -31.315 1.00 14.21 ? 104 GLU C CD  1 
ATOM   5136 O  OE1 . GLU C 1 104 ? 33.979  1.605   -32.054 1.00 12.77 ? 104 GLU C OE1 1 
ATOM   5137 O  OE2 . GLU C 1 104 ? 32.165  2.397   -31.039 1.00 13.96 ? 104 GLU C OE2 1 
ATOM   5138 N  N   . HIS C 1 105 ? 31.326  -3.179  -33.826 1.00 12.34 ? 105 HIS C N   1 
ATOM   5139 C  CA  . HIS C 1 105 ? 30.811  -4.047  -34.915 1.00 11.48 ? 105 HIS C CA  1 
ATOM   5140 C  C   . HIS C 1 105 ? 29.932  -5.187  -34.398 1.00 13.25 ? 105 HIS C C   1 
ATOM   5141 O  O   . HIS C 1 105 ? 30.123  -5.703  -33.277 1.00 13.59 ? 105 HIS C O   1 
ATOM   5142 C  CB  . HIS C 1 105 ? 32.006  -4.597  -35.664 1.00 12.11 ? 105 HIS C CB  1 
ATOM   5143 C  CG  . HIS C 1 105 ? 32.819  -3.532  -36.344 1.00 11.64 ? 105 HIS C CG  1 
ATOM   5144 N  ND1 . HIS C 1 105 ? 33.854  -2.866  -35.734 1.00 11.82 ? 105 HIS C ND1 1 
ATOM   5145 C  CD2 . HIS C 1 105 ? 32.716  -2.992  -37.617 1.00 11.57 ? 105 HIS C CD2 1 
ATOM   5146 C  CE1 . HIS C 1 105 ? 34.391  -2.020  -36.620 1.00 12.06 ? 105 HIS C CE1 1 
ATOM   5147 N  NE2 . HIS C 1 105 ? 33.710  -2.110  -37.756 1.00 11.99 ? 105 HIS C NE2 1 
ATOM   5148 N  N   . THR C 1 106 ? 28.949  -5.514  -35.198 1.00 11.26 ? 106 THR C N   1 
ATOM   5149 C  CA  . THR C 1 106 ? 28.118  -6.655  -34.877 1.00 11.17 ? 106 THR C CA  1 
ATOM   5150 C  C   . THR C 1 106 ? 28.338  -7.720  -35.973 1.00 11.75 ? 106 THR C C   1 
ATOM   5151 O  O   . THR C 1 106 ? 28.783  -7.407  -37.104 1.00 11.53 ? 106 THR C O   1 
ATOM   5152 C  CB  . THR C 1 106 ? 26.629  -6.245  -34.801 1.00 11.44 ? 106 THR C CB  1 
ATOM   5153 O  OG1 . THR C 1 106 ? 26.154  -5.609  -36.012 1.00 13.23 ? 106 THR C OG1 1 
ATOM   5154 C  CG2 . THR C 1 106 ? 26.381  -5.185  -33.669 1.00 13.14 ? 106 THR C CG2 1 
ATOM   5155 N  N   . VAL C 1 107 ? 27.963  -8.997  -35.665 1.00 12.74 ? 107 VAL C N   1 
ATOM   5156 C  CA  . VAL C 1 107 ? 28.054  -10.057 -36.603 1.00 13.90 ? 107 VAL C CA  1 
ATOM   5157 C  C   . VAL C 1 107 ? 26.651  -10.705 -36.719 1.00 13.80 ? 107 VAL C C   1 
ATOM   5158 O  O   . VAL C 1 107 ? 26.126  -11.173 -35.707 1.00 15.25 ? 107 VAL C O   1 
ATOM   5159 C  CB  . VAL C 1 107 ? 29.058  -11.140 -36.246 1.00 14.63 ? 107 VAL C CB  1 
ATOM   5160 C  CG1 . VAL C 1 107 ? 29.032  -12.213 -37.332 1.00 16.56 ? 107 VAL C CG1 1 
ATOM   5161 C  CG2 . VAL C 1 107 ? 30.449  -10.487 -36.121 1.00 15.37 ? 107 VAL C CG2 1 
ATOM   5162 N  N   . SER C 1 108 ? 26.080  -10.618 -37.919 1.00 14.80 ? 108 SER C N   1 
ATOM   5163 C  CA  . SER C 1 108 ? 24.722  -11.142 -38.170 1.00 14.74 ? 108 SER C CA  1 
ATOM   5164 C  C   . SER C 1 108 ? 23.756  -10.526 -37.111 1.00 14.78 ? 108 SER C C   1 
ATOM   5165 O  O   . SER C 1 108 ? 22.871  -11.221 -36.536 1.00 15.72 ? 108 SER C O   1 
ATOM   5166 C  CB  . SER C 1 108 ? 24.711  -12.679 -38.074 1.00 16.96 ? 108 SER C CB  1 
ATOM   5167 O  OG  . SER C 1 108 ? 25.570  -13.227 -39.015 1.00 21.72 ? 108 SER C OG  1 
ATOM   5168 N  N   . GLY C 1 109 ? 23.904  -9.209  -36.897 1.00 13.71 ? 109 GLY C N   1 
ATOM   5169 C  CA  . GLY C 1 109 ? 23.033  -8.455  -36.025 1.00 14.89 ? 109 GLY C CA  1 
ATOM   5170 C  C   . GLY C 1 109 ? 23.363  -8.533  -34.565 1.00 15.13 ? 109 GLY C C   1 
ATOM   5171 O  O   . GLY C 1 109 ? 22.841  -7.784  -33.779 1.00 17.94 ? 109 GLY C O   1 
ATOM   5172 N  N   . GLN C 1 110 ? 24.312  -9.371  -34.181 1.00 13.53 ? 110 GLN C N   1 
ATOM   5173 C  CA  . GLN C 1 110 ? 24.615  -9.554  -32.765 1.00 15.06 ? 110 GLN C CA  1 
ATOM   5174 C  C   . GLN C 1 110 ? 25.868  -8.813  -32.247 1.00 15.50 ? 110 GLN C C   1 
ATOM   5175 O  O   . GLN C 1 110 ? 26.947  -8.867  -32.891 1.00 14.81 ? 110 GLN C O   1 
ATOM   5176 C  CB  . GLN C 1 110 ? 24.868  -11.059 -32.513 1.00 16.35 ? 110 GLN C CB  1 
ATOM   5177 C  CG  . GLN C 1 110 ? 23.823  -11.999 -33.052 1.00 21.44 ? 110 GLN C CG  1 
ATOM   5178 C  CD  . GLN C 1 110 ? 22.425  -11.615 -32.601 1.00 22.45 ? 110 GLN C CD  1 
ATOM   5179 O  OE1 . GLN C 1 110 ? 21.571  -11.363 -33.477 1.00 33.84 ? 110 GLN C OE1 1 
ATOM   5180 N  NE2 . GLN C 1 110 ? 22.200  -11.454 -31.295 1.00 23.39 ? 110 GLN C NE2 1 
ATOM   5181 N  N   . HIS C 1 111 ? 25.728  -8.173  -31.097 1.00 17.76 ? 111 HIS C N   1 
ATOM   5182 C  CA  . HIS C 1 111 ? 26.892  -7.591  -30.425 1.00 14.72 ? 111 HIS C CA  1 
ATOM   5183 C  C   . HIS C 1 111 ? 27.633  -8.609  -29.715 1.00 17.13 ? 111 HIS C C   1 
ATOM   5184 O  O   . HIS C 1 111 ? 27.068  -9.611  -29.227 1.00 18.07 ? 111 HIS C O   1 
ATOM   5185 C  CB  . HIS C 1 111 ? 26.495  -6.562  -29.373 1.00 15.29 ? 111 HIS C CB  1 
ATOM   5186 C  CG  . HIS C 1 111 ? 26.047  -5.251  -29.940 1.00 15.29 ? 111 HIS C CG  1 
ATOM   5187 N  ND1 . HIS C 1 111 ? 26.860  -4.194  -30.034 1.00 16.00 ? 111 HIS C ND1 1 
ATOM   5188 C  CD2 . HIS C 1 111 ? 24.804  -4.846  -30.440 1.00 16.38 ? 111 HIS C CD2 1 
ATOM   5189 C  CE1 . HIS C 1 111 ? 26.176  -3.141  -30.532 1.00 15.40 ? 111 HIS C CE1 1 
ATOM   5190 N  NE2 . HIS C 1 111 ? 24.919  -3.547  -30.792 1.00 16.97 ? 111 HIS C NE2 1 
ATOM   5191 N  N   . PHE C 1 112 ? 28.940  -8.386  -29.646 1.00 16.33 ? 112 PHE C N   1 
ATOM   5192 C  CA  . PHE C 1 112 ? 29.786  -9.150  -28.745 1.00 16.41 ? 112 PHE C CA  1 
ATOM   5193 C  C   . PHE C 1 112 ? 29.850  -8.434  -27.416 1.00 17.16 ? 112 PHE C C   1 
ATOM   5194 O  O   . PHE C 1 112 ? 29.430  -7.285  -27.332 1.00 15.52 ? 112 PHE C O   1 
ATOM   5195 C  CB  . PHE C 1 112 ? 31.196  -9.339  -29.380 1.00 17.20 ? 112 PHE C CB  1 
ATOM   5196 C  CG  . PHE C 1 112 ? 31.231  -10.482 -30.311 1.00 20.48 ? 112 PHE C CG  1 
ATOM   5197 C  CD1 . PHE C 1 112 ? 31.680  -11.756 -29.884 1.00 21.83 ? 112 PHE C CD1 1 
ATOM   5198 C  CD2 . PHE C 1 112 ? 30.746  -10.329 -31.613 1.00 21.25 ? 112 PHE C CD2 1 
ATOM   5199 C  CE1 . PHE C 1 112 ? 31.676  -12.824 -30.766 1.00 23.84 ? 112 PHE C CE1 1 
ATOM   5200 C  CE2 . PHE C 1 112 ? 30.750  -11.413 -32.507 1.00 24.25 ? 112 PHE C CE2 1 
ATOM   5201 C  CZ  . PHE C 1 112 ? 31.222  -12.651 -32.074 1.00 24.59 ? 112 PHE C CZ  1 
ATOM   5202 N  N   . ALA C 1 113 ? 30.438  -9.028  -26.360 1.00 16.14 ? 113 ALA C N   1 
ATOM   5203 C  CA  . ALA C 1 113 ? 30.589  -8.287  -25.100 1.00 15.80 ? 113 ALA C CA  1 
ATOM   5204 C  C   . ALA C 1 113 ? 31.272  -6.942  -25.107 1.00 14.47 ? 113 ALA C C   1 
ATOM   5205 O  O   . ALA C 1 113 ? 30.887  -6.042  -24.398 1.00 16.92 ? 113 ALA C O   1 
ATOM   5206 C  CB  . ALA C 1 113 ? 31.195  -9.169  -23.998 1.00 16.05 ? 113 ALA C CB  1 
ATOM   5207 N  N   . ALA C 1 114 ? 32.371  -6.857  -25.891 1.00 14.28 ? 114 ALA C N   1 
ATOM   5208 C  CA  . ALA C 1 114 ? 33.256  -5.709  -25.837 1.00 13.43 ? 114 ALA C CA  1 
ATOM   5209 C  C   . ALA C 1 114 ? 34.092  -5.825  -27.130 1.00 12.80 ? 114 ALA C C   1 
ATOM   5210 O  O   . ALA C 1 114 ? 33.951  -6.830  -27.866 1.00 17.22 ? 114 ALA C O   1 
ATOM   5211 C  CB  . ALA C 1 114 ? 34.146  -5.863  -24.617 1.00 13.65 ? 114 ALA C CB  1 
ATOM   5212 N  N   . GLU C 1 115 ? 34.908  -4.791  -27.400 1.00 11.67 ? 115 GLU C N   1 
ATOM   5213 C  CA  . GLU C 1 115 ? 35.715  -4.770  -28.600 1.00 12.84 ? 115 GLU C CA  1 
ATOM   5214 C  C   . GLU C 1 115 ? 36.959  -4.003  -28.204 1.00 13.20 ? 115 GLU C C   1 
ATOM   5215 O  O   . GLU C 1 115 ? 36.869  -2.948  -27.606 1.00 14.76 ? 115 GLU C O   1 
ATOM   5216 C  CB  . GLU C 1 115 ? 34.955  -4.083  -29.701 1.00 11.45 ? 115 GLU C CB  1 
ATOM   5217 C  CG  . GLU C 1 115 ? 35.643  -4.229  -31.039 1.00 12.17 ? 115 GLU C CG  1 
ATOM   5218 C  CD  . GLU C 1 115 ? 34.694  -3.885  -32.207 1.00 13.58 ? 115 GLU C CD  1 
ATOM   5219 O  OE1 . GLU C 1 115 ? 35.162  -3.394  -33.246 1.00 13.24 ? 115 GLU C OE1 1 
ATOM   5220 O  OE2 . GLU C 1 115 ? 33.463  -4.198  -32.173 1.00 13.36 ? 115 GLU C OE2 1 
ATOM   5221 N  N   . LEU C 1 116 ? 38.121  -4.507  -28.624 1.00 13.87 ? 116 LEU C N   1 
ATOM   5222 C  CA  . LEU C 1 116 ? 39.362  -3.791  -28.414 1.00 13.97 ? 116 LEU C CA  1 
ATOM   5223 C  C   . LEU C 1 116 ? 39.892  -3.289  -29.801 1.00 13.18 ? 116 LEU C C   1 
ATOM   5224 O  O   . LEU C 1 116 ? 39.774  -4.021  -30.784 1.00 16.32 ? 116 LEU C O   1 
ATOM   5225 C  CB  . LEU C 1 116 ? 40.424  -4.799  -27.930 1.00 14.62 ? 116 LEU C CB  1 
ATOM   5226 C  CG  . LEU C 1 116 ? 41.871  -4.269  -28.023 1.00 16.79 ? 116 LEU C CG  1 
ATOM   5227 C  CD1 . LEU C 1 116 ? 42.286  -3.769  -26.677 1.00 19.95 ? 116 LEU C CD1 1 
ATOM   5228 C  CD2 . LEU C 1 116 ? 42.740  -5.460  -28.454 1.00 18.10 ? 116 LEU C CD2 1 
ATOM   5229 N  N   . HIS C 1 117 ? 40.344  -2.017  -29.864 1.00 13.58 ? 117 HIS C N   1 
ATOM   5230 C  CA  . HIS C 1 117 ? 40.885  -1.484  -31.101 1.00 12.00 ? 117 HIS C CA  1 
ATOM   5231 C  C   . HIS C 1 117 ? 42.342  -1.116  -30.864 1.00 14.02 ? 117 HIS C C   1 
ATOM   5232 O  O   . HIS C 1 117 ? 42.686  -0.473  -29.871 1.00 15.00 ? 117 HIS C O   1 
ATOM   5233 C  CB  . HIS C 1 117 ? 40.127  -0.256  -31.424 1.00 12.92 ? 117 HIS C CB  1 
ATOM   5234 C  CG  . HIS C 1 117 ? 38.747  -0.560  -31.843 1.00 12.61 ? 117 HIS C CG  1 
ATOM   5235 N  ND1 . HIS C 1 117 ? 37.707  0.357   -31.577 1.00 13.06 ? 117 HIS C ND1 1 
ATOM   5236 C  CD2 . HIS C 1 117 ? 38.190  -1.711  -32.450 1.00 13.46 ? 117 HIS C CD2 1 
ATOM   5237 C  CE1 . HIS C 1 117 ? 36.591  -0.163  -32.189 1.00 13.23 ? 117 HIS C CE1 1 
ATOM   5238 N  NE2 . HIS C 1 117 ? 36.868  -1.433  -32.685 1.00 11.55 ? 117 HIS C NE2 1 
ATOM   5239 N  N   . ILE C 1 118 ? 43.135  -1.512  -31.839 1.00 13.75 ? 118 ILE C N   1 
ATOM   5240 C  CA  . ILE C 1 118 ? 44.588  -1.064  -31.951 1.00 14.58 ? 118 ILE C CA  1 
ATOM   5241 C  C   . ILE C 1 118 ? 44.779  -0.099  -33.098 1.00 13.93 ? 118 ILE C C   1 
ATOM   5242 O  O   . ILE C 1 118 ? 44.669  -0.550  -34.252 1.00 14.24 ? 118 ILE C O   1 
ATOM   5243 C  CB  . ILE C 1 118 ? 45.504  -2.241  -32.092 1.00 15.58 ? 118 ILE C CB  1 
ATOM   5244 C  CG1 . ILE C 1 118 ? 45.166  -3.192  -30.968 1.00 16.11 ? 118 ILE C CG1 1 
ATOM   5245 C  CG2 . ILE C 1 118 ? 46.974  -1.747  -31.828 1.00 16.35 ? 118 ILE C CG2 1 
ATOM   5246 C  CD1 . ILE C 1 118 ? 45.898  -4.537  -30.980 1.00 17.21 ? 118 ILE C CD1 1 
ATOM   5247 N  N   . VAL C 1 119 ? 44.980  1.192   -32.781 1.00 13.38 ? 119 VAL C N   1 
ATOM   5248 C  CA  . VAL C 1 119 ? 44.912  2.356   -33.732 1.00 13.97 ? 119 VAL C CA  1 
ATOM   5249 C  C   . VAL C 1 119 ? 46.298  2.614   -34.284 1.00 14.86 ? 119 VAL C C   1 
ATOM   5250 O  O   . VAL C 1 119 ? 47.254  2.783   -33.488 1.00 16.04 ? 119 VAL C O   1 
ATOM   5251 C  CB  . VAL C 1 119 ? 44.394  3.664   -33.094 1.00 14.37 ? 119 VAL C CB  1 
ATOM   5252 C  CG1 . VAL C 1 119 ? 44.275  4.743   -34.160 1.00 15.63 ? 119 VAL C CG1 1 
ATOM   5253 C  CG2 . VAL C 1 119 ? 43.034  3.397   -32.411 1.00 14.94 ? 119 VAL C CG2 1 
ATOM   5254 N  N   . HIS C 1 120 ? 46.450  2.576   -35.631 1.00 15.07 ? 120 HIS C N   1 
ATOM   5255 C  CA  . HIS C 1 120 ? 47.770  2.855   -36.278 1.00 15.79 ? 120 HIS C CA  1 
ATOM   5256 C  C   . HIS C 1 120 ? 47.605  3.975   -37.253 1.00 16.76 ? 120 HIS C C   1 
ATOM   5257 O  O   . HIS C 1 120 ? 46.489  4.284   -37.703 1.00 14.59 ? 120 HIS C O   1 
ATOM   5258 C  CB  . HIS C 1 120 ? 48.196  1.635   -37.069 1.00 16.81 ? 120 HIS C CB  1 
ATOM   5259 C  CG  . HIS C 1 120 ? 48.339  0.378   -36.290 1.00 17.70 ? 120 HIS C CG  1 
ATOM   5260 N  ND1 . HIS C 1 120 ? 47.273  -0.359  -35.758 1.00 16.48 ? 120 HIS C ND1 1 
ATOM   5261 C  CD2 . HIS C 1 120 ? 49.486  -0.361  -36.020 1.00 20.34 ? 120 HIS C CD2 1 
ATOM   5262 C  CE1 . HIS C 1 120 ? 47.776  -1.514  -35.193 1.00 17.24 ? 120 HIS C CE1 1 
ATOM   5263 N  NE2 . HIS C 1 120 ? 49.105  -1.512  -35.360 1.00 19.63 ? 120 HIS C NE2 1 
ATOM   5264 N  N   . TYR C 1 121 ? 48.730  4.637   -37.606 1.00 15.86 ? 121 TYR C N   1 
ATOM   5265 C  CA  . TYR C 1 121 ? 48.710  5.749   -38.540 1.00 17.29 ? 121 TYR C CA  1 
ATOM   5266 C  C   . TYR C 1 121 ? 49.678  5.473   -39.696 1.00 16.36 ? 121 TYR C C   1 
ATOM   5267 O  O   . TYR C 1 121 ? 50.617  4.653   -39.558 1.00 14.37 ? 121 TYR C O   1 
ATOM   5268 C  CB  . TYR C 1 121 ? 48.973  7.093   -37.825 1.00 17.77 ? 121 TYR C CB  1 
ATOM   5269 C  CG  . TYR C 1 121 ? 50.392  7.326   -37.410 1.00 17.75 ? 121 TYR C CG  1 
ATOM   5270 C  CD1 . TYR C 1 121 ? 51.214  8.062   -38.211 1.00 18.40 ? 121 TYR C CD1 1 
ATOM   5271 C  CD2 . TYR C 1 121 ? 50.867  6.801   -36.229 1.00 17.72 ? 121 TYR C CD2 1 
ATOM   5272 C  CE1 . TYR C 1 121 ? 52.557  8.295   -37.835 1.00 18.61 ? 121 TYR C CE1 1 
ATOM   5273 C  CE2 . TYR C 1 121 ? 52.184  6.966   -35.841 1.00 20.63 ? 121 TYR C CE2 1 
ATOM   5274 C  CZ  . TYR C 1 121 ? 53.018  7.749   -36.654 1.00 22.12 ? 121 TYR C CZ  1 
ATOM   5275 O  OH  . TYR C 1 121 ? 54.334  7.963   -36.287 1.00 22.87 ? 121 TYR C OH  1 
ATOM   5276 N  N   . ASN C 1 122 ? 49.448  6.112   -40.834 1.00 16.02 ? 122 ASN C N   1 
ATOM   5277 C  CA  . ASN C 1 122 ? 50.259  5.716   -42.025 1.00 15.53 ? 122 ASN C CA  1 
ATOM   5278 C  C   . ASN C 1 122 ? 51.515  6.554   -41.923 1.00 15.42 ? 122 ASN C C   1 
ATOM   5279 O  O   . ASN C 1 122 ? 51.472  7.712   -42.206 1.00 17.17 ? 122 ASN C O   1 
ATOM   5280 C  CB  . ASN C 1 122 ? 49.503  6.143   -43.276 1.00 18.06 ? 122 ASN C CB  1 
ATOM   5281 C  CG  . ASN C 1 122 ? 50.206  5.851   -44.554 1.00 20.66 ? 122 ASN C CG  1 
ATOM   5282 O  OD1 . ASN C 1 122 ? 51.440  5.863   -44.630 1.00 19.67 ? 122 ASN C OD1 1 
ATOM   5283 N  ND2 . ASN C 1 122 ? 49.419  5.583   -45.593 1.00 19.10 ? 122 ASN C ND2 1 
ATOM   5284 N  N   . SER C 1 123 ? 52.591  5.939   -41.501 1.00 16.59 ? 123 SER C N   1 
ATOM   5285 C  CA  . SER C 1 123 ? 53.803  6.727   -41.153 1.00 16.73 ? 123 SER C CA  1 
ATOM   5286 C  C   . SER C 1 123 ? 54.656  6.925   -42.414 1.00 18.09 ? 123 SER C C   1 
ATOM   5287 O  O   . SER C 1 123 ? 55.592  7.753   -42.374 1.00 18.93 ? 123 SER C O   1 
ATOM   5288 C  CB  . SER C 1 123 ? 54.552  6.035   -40.028 1.00 17.60 ? 123 SER C CB  1 
ATOM   5289 O  OG  . SER C 1 123 ? 54.710  4.665   -40.274 1.00 14.76 ? 123 SER C OG  1 
ATOM   5290 N  N   . ASP C 1 124 ? 54.301  6.260   -43.506 1.00 19.42 ? 124 ASP C N   1 
ATOM   5291 C  CA  . ASP C 1 124 ? 55.006  6.453   -44.825 1.00 18.57 ? 124 ASP C CA  1 
ATOM   5292 C  C   . ASP C 1 124 ? 54.591  7.807   -45.393 1.00 24.28 ? 124 ASP C C   1 
ATOM   5293 O  O   . ASP C 1 124 ? 55.398  8.536   -45.983 1.00 25.16 ? 124 ASP C O   1 
ATOM   5294 C  CB  . ASP C 1 124 ? 54.716  5.311   -45.793 1.00 18.32 ? 124 ASP C CB  1 
ATOM   5295 C  CG  . ASP C 1 124 ? 55.372  3.998   -45.403 1.00 18.17 ? 124 ASP C CG  1 
ATOM   5296 O  OD1 . ASP C 1 124 ? 56.385  3.991   -44.640 1.00 19.26 ? 124 ASP C OD1 1 
ATOM   5297 O  OD2 . ASP C 1 124 ? 54.971  2.931   -45.892 1.00 17.74 ? 124 ASP C OD2 1 
ATOM   5298 N  N   . LEU C 1 125 ? 53.338  8.180   -45.161 1.00 19.55 ? 125 LEU C N   1 
ATOM   5299 C  CA  . LEU C 1 125 ? 52.809  9.445   -45.645 1.00 21.08 ? 125 LEU C CA  1 
ATOM   5300 C  C   . LEU C 1 125 ? 52.871  10.613  -44.615 1.00 21.42 ? 125 LEU C C   1 
ATOM   5301 O  O   . LEU C 1 125 ? 52.938  11.803  -45.005 1.00 23.97 ? 125 LEU C O   1 
ATOM   5302 C  CB  . LEU C 1 125 ? 51.348  9.281   -46.123 1.00 20.67 ? 125 LEU C CB  1 
ATOM   5303 C  CG  . LEU C 1 125 ? 51.093  8.339   -47.325 1.00 23.01 ? 125 LEU C CG  1 
ATOM   5304 C  CD1 . LEU C 1 125 ? 49.592  8.270   -47.644 1.00 22.02 ? 125 LEU C CD1 1 
ATOM   5305 C  CD2 . LEU C 1 125 ? 51.869  8.839   -48.546 1.00 22.99 ? 125 LEU C CD2 1 
ATOM   5306 N  N   . TYR C 1 126 ? 52.750  10.305  -43.319 1.00 20.73 ? 126 TYR C N   1 
ATOM   5307 C  CA  . TYR C 1 126 ? 52.498  11.348  -42.325 1.00 17.60 ? 126 TYR C CA  1 
ATOM   5308 C  C   . TYR C 1 126 ? 53.386  11.203  -41.106 1.00 18.63 ? 126 TYR C C   1 
ATOM   5309 O  O   . TYR C 1 126 ? 53.745  10.065  -40.713 1.00 17.41 ? 126 TYR C O   1 
ATOM   5310 C  CB  . TYR C 1 126 ? 51.017  11.233  -41.856 1.00 18.44 ? 126 TYR C CB  1 
ATOM   5311 C  CG  . TYR C 1 126 ? 50.071  11.269  -43.025 1.00 19.10 ? 126 TYR C CG  1 
ATOM   5312 C  CD1 . TYR C 1 126 ? 50.098  12.341  -43.915 1.00 20.75 ? 126 TYR C CD1 1 
ATOM   5313 C  CD2 . TYR C 1 126 ? 49.190  10.202  -43.274 1.00 19.49 ? 126 TYR C CD2 1 
ATOM   5314 C  CE1 . TYR C 1 126 ? 49.273  12.374  -45.003 1.00 20.94 ? 126 TYR C CE1 1 
ATOM   5315 C  CE2 . TYR C 1 126 ? 48.376  10.216  -44.365 1.00 22.44 ? 126 TYR C CE2 1 
ATOM   5316 C  CZ  . TYR C 1 126 ? 48.402  11.311  -45.222 1.00 22.98 ? 126 TYR C CZ  1 
ATOM   5317 O  OH  . TYR C 1 126 ? 47.592  11.373  -46.339 1.00 23.56 ? 126 TYR C OH  1 
ATOM   5318 N  N   . PRO C 1 127 ? 53.708  12.357  -40.456 1.00 19.33 ? 127 PRO C N   1 
ATOM   5319 C  CA  . PRO C 1 127 ? 54.691  12.333  -39.402 1.00 22.58 ? 127 PRO C CA  1 
ATOM   5320 C  C   . PRO C 1 127 ? 54.163  11.829  -38.068 1.00 23.75 ? 127 PRO C C   1 
ATOM   5321 O  O   . PRO C 1 127 ? 54.947  11.391  -37.231 1.00 26.72 ? 127 PRO C O   1 
ATOM   5322 C  CB  . PRO C 1 127 ? 55.059  13.817  -39.248 1.00 22.34 ? 127 PRO C CB  1 
ATOM   5323 C  CG  . PRO C 1 127 ? 53.896  14.579  -39.736 1.00 22.18 ? 127 PRO C CG  1 
ATOM   5324 C  CD  . PRO C 1 127 ? 53.371  13.742  -40.858 1.00 21.51 ? 127 PRO C CD  1 
ATOM   5325 N  N   . ASP C 1 128 ? 52.844  11.896  -37.861 1.00 21.13 ? 128 ASP C N   1 
ATOM   5326 C  CA  . ASP C 1 128 ? 52.319  11.372  -36.610 1.00 24.04 ? 128 ASP C CA  1 
ATOM   5327 C  C   . ASP C 1 128 ? 50.844  11.041  -36.798 1.00 20.47 ? 128 ASP C C   1 
ATOM   5328 O  O   . ASP C 1 128 ? 50.262  11.394  -37.836 1.00 19.01 ? 128 ASP C O   1 
ATOM   5329 C  CB  . ASP C 1 128 ? 52.510  12.403  -35.495 1.00 23.43 ? 128 ASP C CB  1 
ATOM   5330 C  CG  . ASP C 1 128 ? 52.099  13.793  -35.919 1.00 29.03 ? 128 ASP C CG  1 
ATOM   5331 O  OD1 . ASP C 1 128 ? 52.956  14.706  -35.993 1.00 32.34 ? 128 ASP C OD1 1 
ATOM   5332 O  OD2 . ASP C 1 128 ? 50.926  13.993  -36.188 1.00 25.77 ? 128 ASP C OD2 1 
ATOM   5333 N  N   . ALA C 1 129 ? 50.228  10.493  -35.756 1.00 19.13 ? 129 ALA C N   1 
ATOM   5334 C  CA  . ALA C 1 129 ? 48.812  10.100  -35.838 1.00 19.67 ? 129 ALA C CA  1 
ATOM   5335 C  C   . ALA C 1 129 ? 47.812  11.251  -35.984 1.00 22.07 ? 129 ALA C C   1 
ATOM   5336 O  O   . ALA C 1 129 ? 46.856  11.153  -36.765 1.00 20.65 ? 129 ALA C O   1 
ATOM   5337 C  CB  . ALA C 1 129 ? 48.479  9.216   -34.671 1.00 21.62 ? 129 ALA C CB  1 
ATOM   5338 N  N   A SER C 1 130 ? 48.035  12.325  -35.258 0.50 21.64 ? 130 SER C N   1 
ATOM   5339 N  N   B SER C 1 130 ? 48.040  12.316  -35.227 0.50 21.75 ? 130 SER C N   1 
ATOM   5340 C  CA  A SER C 1 130 ? 47.194  13.507  -35.367 0.50 22.97 ? 130 SER C CA  1 
ATOM   5341 C  CA  B SER C 1 130 ? 47.246  13.543  -35.305 0.50 23.13 ? 130 SER C CA  1 
ATOM   5342 C  C   A SER C 1 130 ? 47.128  14.108  -36.764 0.50 21.92 ? 130 SER C C   1 
ATOM   5343 C  C   B SER C 1 130 ? 47.142  14.103  -36.728 0.50 21.97 ? 130 SER C C   1 
ATOM   5344 O  O   A SER C 1 130 ? 46.030  14.368  -37.303 0.50 23.50 ? 130 SER C O   1 
ATOM   5345 O  O   B SER C 1 130 ? 46.031  14.330  -37.247 0.50 23.89 ? 130 SER C O   1 
ATOM   5346 C  CB  A SER C 1 130 ? 47.641  14.526  -34.337 0.50 22.85 ? 130 SER C CB  1 
ATOM   5347 C  CB  B SER C 1 130 ? 47.787  14.605  -34.335 0.50 23.06 ? 130 SER C CB  1 
ATOM   5348 O  OG  A SER C 1 130 ? 47.183  14.078  -33.096 0.50 24.74 ? 130 SER C OG  1 
ATOM   5349 O  OG  B SER C 1 130 ? 46.935  15.745  -34.340 0.50 25.00 ? 130 SER C OG  1 
ATOM   5350 N  N   . THR C 1 131 ? 48.310  14.316  -37.363 1.00 21.15 ? 131 THR C N   1 
ATOM   5351 C  CA  . THR C 1 131 ? 48.399  14.815  -38.719 1.00 21.30 ? 131 THR C CA  1 
ATOM   5352 C  C   . THR C 1 131 ? 47.732  13.819  -39.667 1.00 21.34 ? 131 THR C C   1 
ATOM   5353 O  O   . THR C 1 131 ? 46.996  14.210  -40.579 1.00 20.82 ? 131 THR C O   1 
ATOM   5354 C  CB  . THR C 1 131 ? 49.884  14.986  -39.120 1.00 21.59 ? 131 THR C CB  1 
ATOM   5355 O  OG1 . THR C 1 131 ? 50.500  15.862  -38.161 1.00 24.33 ? 131 THR C OG1 1 
ATOM   5356 C  CG2 . THR C 1 131 ? 50.010  15.569  -40.529 1.00 19.93 ? 131 THR C CG2 1 
ATOM   5357 N  N   . ALA C 1 132 ? 47.979  12.529  -39.460 1.00 16.64 ? 132 ALA C N   1 
ATOM   5358 C  CA  . ALA C 1 132 ? 47.383  11.509  -40.386 1.00 16.99 ? 132 ALA C CA  1 
ATOM   5359 C  C   . ALA C 1 132 ? 45.853  11.458  -40.286 1.00 16.88 ? 132 ALA C C   1 
ATOM   5360 O  O   . ALA C 1 132 ? 45.200  11.027  -41.240 1.00 16.31 ? 132 ALA C O   1 
ATOM   5361 C  CB  . ALA C 1 132 ? 47.912  10.173  -39.973 1.00 15.55 ? 132 ALA C CB  1 
ATOM   5362 N  N   . SER C 1 133 ? 45.330  11.766  -39.107 1.00 17.66 ? 133 SER C N   1 
ATOM   5363 C  CA  . SER C 1 133 ? 43.942  11.311  -38.821 1.00 18.22 ? 133 SER C CA  1 
ATOM   5364 C  C   . SER C 1 133 ? 42.852  11.895  -39.728 1.00 20.29 ? 133 SER C C   1 
ATOM   5365 O  O   . SER C 1 133 ? 41.785  11.263  -39.889 1.00 19.56 ? 133 SER C O   1 
ATOM   5366 C  CB  . SER C 1 133 ? 43.637  11.510  -37.329 1.00 17.46 ? 133 SER C CB  1 
ATOM   5367 O  OG  . SER C 1 133 ? 43.569  12.927  -37.061 1.00 17.42 ? 133 SER C OG  1 
ATOM   5368 N  N   . ASN C 1 134 ? 43.083  13.048  -40.346 1.00 18.71 ? 134 ASN C N   1 
ATOM   5369 C  CA  . ASN C 1 134 ? 42.079  13.624  -41.224 1.00 20.42 ? 134 ASN C CA  1 
ATOM   5370 C  C   . ASN C 1 134 ? 42.515  13.596  -42.687 1.00 18.92 ? 134 ASN C C   1 
ATOM   5371 O  O   . ASN C 1 134 ? 41.991  14.331  -43.536 1.00 20.64 ? 134 ASN C O   1 
ATOM   5372 C  CB  . ASN C 1 134 ? 41.710  15.049  -40.780 1.00 21.97 ? 134 ASN C CB  1 
ATOM   5373 C  CG  . ASN C 1 134 ? 42.900  16.028  -40.895 1.00 23.59 ? 134 ASN C CG  1 
ATOM   5374 O  OD1 . ASN C 1 134 ? 44.030  15.611  -40.932 1.00 24.70 ? 134 ASN C OD1 1 
ATOM   5375 N  ND2 . ASN C 1 134 ? 42.605  17.325  -41.029 1.00 28.13 ? 134 ASN C ND2 1 
ATOM   5376 N  N   . LYS C 1 135 ? 43.482  12.771  -42.982 1.00 19.43 ? 135 LYS C N   1 
ATOM   5377 C  CA  . LYS C 1 135 ? 44.053  12.700  -44.317 1.00 17.52 ? 135 LYS C CA  1 
ATOM   5378 C  C   . LYS C 1 135 ? 43.892  11.341  -44.975 1.00 17.27 ? 135 LYS C C   1 
ATOM   5379 O  O   . LYS C 1 135 ? 43.708  10.296  -44.327 1.00 20.32 ? 135 LYS C O   1 
ATOM   5380 C  CB  . LYS C 1 135 ? 45.557  13.068  -44.234 1.00 20.25 ? 135 LYS C CB  1 
ATOM   5381 C  CG  . LYS C 1 135 ? 45.698  14.485  -43.673 1.00 20.40 ? 135 LYS C CG  1 
ATOM   5382 C  CD  . LYS C 1 135 ? 47.110  15.061  -43.672 1.00 22.36 ? 135 LYS C CD  1 
ATOM   5383 C  CE  . LYS C 1 135 ? 47.065  16.534  -43.270 1.00 23.18 ? 135 LYS C CE  1 
ATOM   5384 N  NZ  . LYS C 1 135 ? 46.738  16.730  -41.800 1.00 25.52 ? 135 LYS C NZ  1 
ATOM   5385 N  N   . SER C 1 136 ? 43.961  11.390  -46.303 1.00 19.52 ? 136 SER C N   1 
ATOM   5386 C  CA  . SER C 1 136 ? 43.765  10.255  -47.128 1.00 20.17 ? 136 SER C CA  1 
ATOM   5387 C  C   . SER C 1 136 ? 44.637  9.086   -46.674 1.00 18.56 ? 136 SER C C   1 
ATOM   5388 O  O   . SER C 1 136 ? 45.877  9.249   -46.418 1.00 20.44 ? 136 SER C O   1 
ATOM   5389 C  CB  . SER C 1 136 ? 44.169  10.691  -48.533 1.00 21.12 ? 136 SER C CB  1 
ATOM   5390 O  OG  . SER C 1 136 ? 44.116  9.552   -49.341 1.00 21.99 ? 136 SER C OG  1 
ATOM   5391 N  N   . GLU C 1 137 ? 44.021  7.903   -46.534 1.00 18.74 ? 137 GLU C N   1 
ATOM   5392 C  CA  . GLU C 1 137 ? 44.780  6.683   -46.155 1.00 18.78 ? 137 GLU C CA  1 
ATOM   5393 C  C   . GLU C 1 137 ? 45.532  6.821   -44.837 1.00 18.49 ? 137 GLU C C   1 
ATOM   5394 O  O   . GLU C 1 137 ? 46.556  6.129   -44.590 1.00 17.29 ? 137 GLU C O   1 
ATOM   5395 C  CB  . GLU C 1 137 ? 45.722  6.240   -47.277 1.00 21.19 ? 137 GLU C CB  1 
ATOM   5396 C  CG  . GLU C 1 137 ? 45.006  5.850   -48.568 1.00 24.33 ? 137 GLU C CG  1 
ATOM   5397 C  CD  . GLU C 1 137 ? 45.972  5.594   -49.754 1.00 30.68 ? 137 GLU C CD  1 
ATOM   5398 O  OE1 . GLU C 1 137 ? 45.486  5.388   -50.886 1.00 35.13 ? 137 GLU C OE1 1 
ATOM   5399 O  OE2 . GLU C 1 137 ? 47.218  5.642   -49.577 1.00 39.05 ? 137 GLU C OE2 1 
ATOM   5400 N  N   . GLY C 1 138 ? 44.990  7.662   -43.961 1.00 15.77 ? 138 GLY C N   1 
ATOM   5401 C  CA  . GLY C 1 138 ? 45.714  8.097   -42.789 1.00 16.20 ? 138 GLY C CA  1 
ATOM   5402 C  C   . GLY C 1 138 ? 45.809  7.061   -41.685 1.00 15.30 ? 138 GLY C C   1 
ATOM   5403 O  O   . GLY C 1 138 ? 46.811  7.015   -40.960 1.00 15.84 ? 138 GLY C O   1 
ATOM   5404 N  N   . LEU C 1 139 ? 44.772  6.198   -41.502 1.00 14.77 ? 139 LEU C N   1 
ATOM   5405 C  CA  . LEU C 1 139 ? 44.729  5.325   -40.314 1.00 13.35 ? 139 LEU C CA  1 
ATOM   5406 C  C   . LEU C 1 139 ? 44.392  3.873   -40.658 1.00 13.34 ? 139 LEU C C   1 
ATOM   5407 O  O   . LEU C 1 139 ? 43.796  3.609   -41.719 1.00 13.61 ? 139 LEU C O   1 
ATOM   5408 C  CB  . LEU C 1 139 ? 43.697  5.855   -39.311 1.00 13.96 ? 139 LEU C CB  1 
ATOM   5409 C  CG  . LEU C 1 139 ? 43.880  7.314   -38.770 1.00 15.69 ? 139 LEU C CG  1 
ATOM   5410 C  CD1 . LEU C 1 139 ? 42.659  7.704   -37.963 1.00 18.70 ? 139 LEU C CD1 1 
ATOM   5411 C  CD2 . LEU C 1 139 ? 45.156  7.444   -37.941 1.00 16.86 ? 139 LEU C CD2 1 
ATOM   5412 N  N   . ALA C 1 140 ? 44.757  2.920   -39.800 1.00 11.77 ? 140 ALA C N   1 
ATOM   5413 C  CA  . ALA C 1 140 ? 44.329  1.510   -39.956 1.00 12.70 ? 140 ALA C CA  1 
ATOM   5414 C  C   . ALA C 1 140 ? 44.033  1.055   -38.552 1.00 14.49 ? 140 ALA C C   1 
ATOM   5415 O  O   . ALA C 1 140 ? 44.848  1.246   -37.690 1.00 13.52 ? 140 ALA C O   1 
ATOM   5416 C  CB  . ALA C 1 140 ? 45.422  0.691   -40.556 1.00 13.51 ? 140 ALA C CB  1 
ATOM   5417 N  N   . VAL C 1 141 ? 42.860  0.436   -38.275 1.00 11.99 ? 141 VAL C N   1 
ATOM   5418 C  CA  . VAL C 1 141 ? 42.622  0.022   -36.886 1.00 12.88 ? 141 VAL C CA  1 
ATOM   5419 C  C   . VAL C 1 141 ? 42.412  -1.495  -36.973 1.00 12.33 ? 141 VAL C C   1 
ATOM   5420 O  O   . VAL C 1 141 ? 41.779  -2.001  -37.955 1.00 13.91 ? 141 VAL C O   1 
ATOM   5421 C  CB  . VAL C 1 141 ? 41.366  0.716   -36.343 1.00 11.65 ? 141 VAL C CB  1 
ATOM   5422 C  CG1 . VAL C 1 141 ? 41.071  0.217   -34.900 1.00 13.79 ? 141 VAL C CG1 1 
ATOM   5423 C  CG2 . VAL C 1 141 ? 41.547  2.211   -36.309 1.00 13.05 ? 141 VAL C CG2 1 
ATOM   5424 N  N   . LEU C 1 142 ? 42.912  -2.224  -35.954 1.00 11.67 ? 142 LEU C N   1 
ATOM   5425 C  CA  . LEU C 1 142 ? 42.679  -3.688  -35.849 1.00 13.44 ? 142 LEU C CA  1 
ATOM   5426 C  C   . LEU C 1 142 ? 41.648  -3.848  -34.772 1.00 12.34 ? 142 LEU C C   1 
ATOM   5427 O  O   . LEU C 1 142 ? 41.824  -3.260  -33.676 1.00 16.68 ? 142 LEU C O   1 
ATOM   5428 C  CB  . LEU C 1 142 ? 43.913  -4.487  -35.349 1.00 14.65 ? 142 LEU C CB  1 
ATOM   5429 C  CG  . LEU C 1 142 ? 45.181  -4.237  -36.180 1.00 15.21 ? 142 LEU C CG  1 
ATOM   5430 C  CD1 . LEU C 1 142 ? 46.311  -5.056  -35.567 1.00 18.01 ? 142 LEU C CD1 1 
ATOM   5431 C  CD2 . LEU C 1 142 ? 44.874  -4.720  -37.582 1.00 13.41 ? 142 LEU C CD2 1 
ATOM   5432 N  N   . ALA C 1 143 ? 40.607  -4.611  -35.043 1.00 12.19 ? 143 ALA C N   1 
ATOM   5433 C  CA  . ALA C 1 143 ? 39.483  -4.824  -34.067 1.00 12.29 ? 143 ALA C CA  1 
ATOM   5434 C  C   . ALA C 1 143 ? 39.400  -6.240  -33.676 1.00 11.23 ? 143 ALA C C   1 
ATOM   5435 O  O   . ALA C 1 143 ? 39.397  -7.075  -34.477 1.00 13.51 ? 143 ALA C O   1 
ATOM   5436 C  CB  . ALA C 1 143 ? 38.134  -4.382  -34.683 1.00 13.27 ? 143 ALA C CB  1 
ATOM   5437 N  N   . VAL C 1 144 ? 39.354  -6.465  -32.354 1.00 12.00 ? 144 VAL C N   1 
ATOM   5438 C  CA  . VAL C 1 144 ? 39.185  -7.830  -31.785 1.00 14.24 ? 144 VAL C CA  1 
ATOM   5439 C  C   . VAL C 1 144 ? 37.824  -7.824  -31.025 1.00 12.11 ? 144 VAL C C   1 
ATOM   5440 O  O   . VAL C 1 144 ? 37.564  -6.962  -30.127 1.00 14.64 ? 144 VAL C O   1 
ATOM   5441 C  CB  . VAL C 1 144 ? 40.328  -8.148  -30.770 1.00 15.29 ? 144 VAL C CB  1 
ATOM   5442 C  CG1 . VAL C 1 144 ? 40.131  -9.541  -30.216 1.00 15.82 ? 144 VAL C CG1 1 
ATOM   5443 C  CG2 . VAL C 1 144 ? 41.716  -8.103  -31.465 1.00 15.09 ? 144 VAL C CG2 1 
ATOM   5444 N  N   . LEU C 1 145 ? 37.015  -8.836  -31.343 1.00 14.95 ? 145 LEU C N   1 
ATOM   5445 C  CA  . LEU C 1 145 ? 35.705  -9.006  -30.714 1.00 14.45 ? 145 LEU C CA  1 
ATOM   5446 C  C   . LEU C 1 145 ? 35.983  -9.785  -29.449 1.00 16.91 ? 145 LEU C C   1 
ATOM   5447 O  O   . LEU C 1 145 ? 36.704  -10.822 -29.498 1.00 15.44 ? 145 LEU C O   1 
ATOM   5448 C  CB  . LEU C 1 145 ? 34.767  -9.754  -31.665 1.00 15.21 ? 145 LEU C CB  1 
ATOM   5449 C  CG  . LEU C 1 145 ? 34.465  -9.041  -33.015 1.00 16.22 ? 145 LEU C CG  1 
ATOM   5450 C  CD1 . LEU C 1 145 ? 33.822  -9.933  -34.068 1.00 16.07 ? 145 LEU C CD1 1 
ATOM   5451 C  CD2 . LEU C 1 145 ? 33.619  -7.806  -32.711 1.00 16.45 ? 145 LEU C CD2 1 
ATOM   5452 N  N   . ILE C 1 146 ? 35.333  -9.349  -28.380 1.00 14.26 ? 146 ILE C N   1 
ATOM   5453 C  CA  . ILE C 1 146 ? 35.498  -9.970  -27.028 1.00 16.61 ? 146 ILE C CA  1 
ATOM   5454 C  C   . ILE C 1 146 ? 34.171  -10.619 -26.592 1.00 15.98 ? 146 ILE C C   1 
ATOM   5455 O  O   . ILE C 1 146 ? 33.092  -9.969  -26.557 1.00 17.36 ? 146 ILE C O   1 
ATOM   5456 C  CB  . ILE C 1 146 ? 35.946  -8.957  -26.022 1.00 16.56 ? 146 ILE C CB  1 
ATOM   5457 C  CG1 . ILE C 1 146 ? 37.361  -8.403  -26.357 1.00 17.32 ? 146 ILE C CG1 1 
ATOM   5458 C  CG2 . ILE C 1 146 ? 36.109  -9.618  -24.629 1.00 17.00 ? 146 ILE C CG2 1 
ATOM   5459 C  CD1 . ILE C 1 146 ? 37.674  -7.072  -25.728 1.00 17.41 ? 146 ILE C CD1 1 
ATOM   5460 N  N   . GLU C 1 147 ? 34.260  -11.890 -26.229 1.00 18.72 ? 147 GLU C N   1 
ATOM   5461 C  CA  . GLU C 1 147 ? 33.115  -12.545 -25.576 1.00 21.52 ? 147 GLU C CA  1 
ATOM   5462 C  C   . GLU C 1 147 ? 33.478  -13.126 -24.214 1.00 23.24 ? 147 GLU C C   1 
ATOM   5463 O  O   . GLU C 1 147 ? 34.632  -13.209 -23.896 1.00 23.26 ? 147 GLU C O   1 
ATOM   5464 C  CB  . GLU C 1 147 ? 32.647  -13.678 -26.443 1.00 20.71 ? 147 GLU C CB  1 
ATOM   5465 C  CG  . GLU C 1 147 ? 33.611  -14.846 -26.581 1.00 22.44 ? 147 GLU C CG  1 
ATOM   5466 C  CD  . GLU C 1 147 ? 33.162  -15.846 -27.652 1.00 26.44 ? 147 GLU C CD  1 
ATOM   5467 O  OE1 . GLU C 1 147 ? 32.120  -15.607 -28.363 1.00 25.35 ? 147 GLU C OE1 1 
ATOM   5468 O  OE2 . GLU C 1 147 ? 33.841  -16.881 -27.792 1.00 28.96 ? 147 GLU C OE2 1 
ATOM   5469 N  N   . MET C 1 148 ? 32.469  -13.476 -23.414 1.00 23.58 ? 148 MET C N   1 
ATOM   5470 C  CA  . MET C 1 148 ? 32.692  -14.087 -22.108 1.00 29.39 ? 148 MET C CA  1 
ATOM   5471 C  C   . MET C 1 148 ? 33.104  -15.569 -22.242 1.00 27.63 ? 148 MET C C   1 
ATOM   5472 O  O   . MET C 1 148 ? 32.588  -16.309 -23.057 1.00 27.13 ? 148 MET C O   1 
ATOM   5473 C  CB  . MET C 1 148 ? 31.449  -13.929 -21.217 1.00 35.33 ? 148 MET C CB  1 
ATOM   5474 C  CG  . MET C 1 148 ? 31.307  -12.579 -20.517 1.00 40.61 ? 148 MET C CG  1 
ATOM   5475 S  SD  . MET C 1 148 ? 30.007  -12.627 -19.222 1.00 72.64 ? 148 MET C SD  1 
ATOM   5476 C  CE  . MET C 1 148 ? 28.498  -12.099 -20.064 1.00 49.89 ? 148 MET C CE  1 
ATOM   5477 N  N   . GLY C 1 149 ? 34.115  -15.966 -21.465 1.00 30.19 ? 149 GLY C N   1 
ATOM   5478 C  CA  . GLY C 1 149 ? 34.611  -17.343 -21.401 1.00 29.22 ? 149 GLY C CA  1 
ATOM   5479 C  C   . GLY C 1 149 ? 35.667  -17.425 -20.298 1.00 28.58 ? 149 GLY C C   1 
ATOM   5480 O  O   . GLY C 1 149 ? 35.462  -16.894 -19.187 1.00 25.32 ? 149 GLY C O   1 
ATOM   5481 N  N   . SER C 1 150 ? 36.817  -18.036 -20.620 1.00 34.72 ? 150 SER C N   1 
ATOM   5482 C  CA  . SER C 1 150 ? 37.926  -18.224 -19.674 1.00 30.83 ? 150 SER C CA  1 
ATOM   5483 C  C   . SER C 1 150 ? 38.656  -16.954 -19.336 1.00 32.34 ? 150 SER C C   1 
ATOM   5484 O  O   . SER C 1 150 ? 38.746  -16.075 -20.185 1.00 26.06 ? 150 SER C O   1 
ATOM   5485 C  CB  . SER C 1 150 ? 38.944  -19.210 -20.238 1.00 35.69 ? 150 SER C CB  1 
ATOM   5486 O  OG  . SER C 1 150 ? 38.390  -20.507 -20.281 1.00 43.47 ? 150 SER C OG  1 
ATOM   5487 N  N   . PHE C 1 151 ? 39.160  -16.869 -18.096 1.00 27.10 ? 151 PHE C N   1 
ATOM   5488 C  CA  . PHE C 1 151 ? 40.055  -15.774 -17.630 1.00 28.35 ? 151 PHE C CA  1 
ATOM   5489 C  C   . PHE C 1 151 ? 41.172  -15.542 -18.641 1.00 25.89 ? 151 PHE C C   1 
ATOM   5490 O  O   . PHE C 1 151 ? 41.690  -16.468 -19.209 1.00 27.37 ? 151 PHE C O   1 
ATOM   5491 C  CB  . PHE C 1 151 ? 40.670  -16.074 -16.198 1.00 26.91 ? 151 PHE C CB  1 
ATOM   5492 C  CG  . PHE C 1 151 ? 41.616  -15.008 -15.720 1.00 24.50 ? 151 PHE C CG  1 
ATOM   5493 C  CD1 . PHE C 1 151 ? 41.145  -13.749 -15.327 1.00 24.68 ? 151 PHE C CD1 1 
ATOM   5494 C  CD2 . PHE C 1 151 ? 42.985  -15.227 -15.692 1.00 25.70 ? 151 PHE C CD2 1 
ATOM   5495 C  CE1 . PHE C 1 151 ? 42.015  -12.723 -14.924 1.00 27.93 ? 151 PHE C CE1 1 
ATOM   5496 C  CE2 . PHE C 1 151 ? 43.848  -14.229 -15.311 1.00 25.62 ? 151 PHE C CE2 1 
ATOM   5497 C  CZ  . PHE C 1 151 ? 43.379  -12.954 -14.917 1.00 26.38 ? 151 PHE C CZ  1 
ATOM   5498 N  N   . ASN C 1 152 ? 41.551  -14.285 -18.845 1.00 29.38 ? 152 ASN C N   1 
ATOM   5499 C  CA  . ASN C 1 152 ? 42.567  -13.953 -19.838 1.00 26.02 ? 152 ASN C CA  1 
ATOM   5500 C  C   . ASN C 1 152 ? 43.682  -13.128 -19.209 1.00 24.21 ? 152 ASN C C   1 
ATOM   5501 O  O   . ASN C 1 152 ? 43.508  -11.963 -18.877 1.00 28.10 ? 152 ASN C O   1 
ATOM   5502 C  CB  . ASN C 1 152 ? 41.891  -13.157 -21.018 1.00 26.46 ? 152 ASN C CB  1 
ATOM   5503 C  CG  . ASN C 1 152 ? 42.838  -12.925 -22.175 1.00 28.48 ? 152 ASN C CG  1 
ATOM   5504 O  OD1 . ASN C 1 152 ? 43.951  -12.442 -21.962 1.00 26.60 ? 152 ASN C OD1 1 
ATOM   5505 N  ND2 . ASN C 1 152 ? 42.388  -13.214 -23.424 1.00 28.71 ? 152 ASN C ND2 1 
ATOM   5506 N  N   . PRO C 1 153 ? 44.851  -13.757 -18.967 1.00 29.34 ? 153 PRO C N   1 
ATOM   5507 C  CA  . PRO C 1 153 ? 46.049  -13.132 -18.357 1.00 29.20 ? 153 PRO C CA  1 
ATOM   5508 C  C   . PRO C 1 153 ? 46.499  -11.866 -19.073 1.00 25.13 ? 153 PRO C C   1 
ATOM   5509 O  O   . PRO C 1 153 ? 46.897  -10.850 -18.444 1.00 26.95 ? 153 PRO C O   1 
ATOM   5510 C  CB  . PRO C 1 153 ? 47.115  -14.209 -18.565 1.00 29.12 ? 153 PRO C CB  1 
ATOM   5511 C  CG  . PRO C 1 153 ? 46.338  -15.493 -18.555 1.00 27.82 ? 153 PRO C CG  1 
ATOM   5512 C  CD  . PRO C 1 153 ? 44.967  -15.214 -19.129 1.00 24.91 ? 153 PRO C CD  1 
ATOM   5513 N  N   . SER C 1 154 ? 46.455  -11.934 -20.406 1.00 28.52 ? 154 SER C N   1 
ATOM   5514 C  CA  . SER C 1 154 ? 46.984  -10.853 -21.210 1.00 24.21 ? 154 SER C CA  1 
ATOM   5515 C  C   . SER C 1 154 ? 46.066  -9.656  -21.079 1.00 20.97 ? 154 SER C C   1 
ATOM   5516 O  O   . SER C 1 154 ? 46.541  -8.540  -20.826 1.00 23.35 ? 154 SER C O   1 
ATOM   5517 C  CB  . SER C 1 154 ? 47.170  -11.350 -22.631 1.00 26.22 ? 154 SER C CB  1 
ATOM   5518 O  OG  . SER C 1 154 ? 47.932  -12.571 -22.621 1.00 30.80 ? 154 SER C OG  1 
ATOM   5519 N  N   . TYR C 1 155 ? 44.732  -9.844  -21.182 1.00 22.89 ? 155 TYR C N   1 
ATOM   5520 C  CA  . TYR C 1 155 ? 43.871  -8.703  -20.955 1.00 24.09 ? 155 TYR C CA  1 
ATOM   5521 C  C   . TYR C 1 155 ? 44.034  -8.129  -19.553 1.00 22.47 ? 155 TYR C C   1 
ATOM   5522 O  O   . TYR C 1 155 ? 43.856  -6.883  -19.309 1.00 23.76 ? 155 TYR C O   1 
ATOM   5523 C  CB  . TYR C 1 155 ? 42.388  -8.962  -21.309 1.00 19.72 ? 155 TYR C CB  1 
ATOM   5524 C  CG  . TYR C 1 155 ? 42.166  -8.869  -22.825 1.00 21.11 ? 155 TYR C CG  1 
ATOM   5525 C  CD1 . TYR C 1 155 ? 41.617  -7.695  -23.376 1.00 21.99 ? 155 TYR C CD1 1 
ATOM   5526 C  CD2 . TYR C 1 155 ? 42.566  -9.911  -23.701 1.00 23.85 ? 155 TYR C CD2 1 
ATOM   5527 C  CE1 . TYR C 1 155 ? 41.433  -7.587  -24.780 1.00 23.47 ? 155 TYR C CE1 1 
ATOM   5528 C  CE2 . TYR C 1 155 ? 42.418  -9.804  -25.133 1.00 21.89 ? 155 TYR C CE2 1 
ATOM   5529 C  CZ  . TYR C 1 155 ? 41.826  -8.628  -25.644 1.00 21.27 ? 155 TYR C CZ  1 
ATOM   5530 O  OH  . TYR C 1 155 ? 41.658  -8.390  -27.044 1.00 20.83 ? 155 TYR C OH  1 
ATOM   5531 N  N   . ASP C 1 156 ? 44.342  -9.026  -18.628 1.00 27.65 ? 156 ASP C N   1 
ATOM   5532 C  CA  . ASP C 1 156 ? 44.586  -8.581  -17.259 1.00 32.88 ? 156 ASP C CA  1 
ATOM   5533 C  C   . ASP C 1 156 ? 45.761  -7.636  -17.044 1.00 29.29 ? 156 ASP C C   1 
ATOM   5534 O  O   . ASP C 1 156 ? 45.778  -6.873  -16.028 1.00 29.30 ? 156 ASP C O   1 
ATOM   5535 C  CB  . ASP C 1 156 ? 44.547  -9.719  -16.244 1.00 32.95 ? 156 ASP C CB  1 
ATOM   5536 C  CG  . ASP C 1 156 ? 43.521  -9.442  -15.149 1.00 38.92 ? 156 ASP C CG  1 
ATOM   5537 O  OD1 . ASP C 1 156 ? 42.362  -9.024  -15.492 1.00 33.41 ? 156 ASP C OD1 1 
ATOM   5538 O  OD2 . ASP C 1 156 ? 43.878  -9.604  -13.954 1.00 40.36 ? 156 ASP C OD2 1 
ATOM   5539 N  N   . LYS C 1 157 ? 46.645  -7.578  -18.053 1.00 27.97 ? 157 LYS C N   1 
ATOM   5540 C  CA  . LYS C 1 157 ? 47.808  -6.694  -17.996 1.00 26.77 ? 157 LYS C CA  1 
ATOM   5541 C  C   . LYS C 1 157 ? 47.329  -5.249  -18.106 1.00 28.36 ? 157 LYS C C   1 
ATOM   5542 O  O   . LYS C 1 157 ? 47.992  -4.300  -17.582 1.00 29.59 ? 157 LYS C O   1 
ATOM   5543 C  CB  . LYS C 1 157 ? 48.790  -7.096  -19.062 1.00 27.44 ? 157 LYS C CB  1 
ATOM   5544 C  CG  . LYS C 1 157 ? 49.340  -8.503  -18.721 1.00 27.04 ? 157 LYS C CG  1 
ATOM   5545 C  CD  . LYS C 1 157 ? 50.366  -8.959  -19.693 1.00 26.81 ? 157 LYS C CD  1 
ATOM   5546 C  CE  . LYS C 1 157 ? 51.101  -10.149 -19.123 1.00 28.63 ? 157 LYS C CE  1 
ATOM   5547 N  NZ  . LYS C 1 157 ? 51.453  -11.096 -20.206 1.00 28.66 ? 157 LYS C NZ  1 
ATOM   5548 N  N   . ILE C 1 158 ? 46.154  -5.068  -18.735 1.00 23.38 ? 158 ILE C N   1 
ATOM   5549 C  CA  . ILE C 1 158 ? 45.568  -3.732  -18.792 1.00 25.23 ? 158 ILE C CA  1 
ATOM   5550 C  C   . ILE C 1 158 ? 44.641  -3.590  -17.600 1.00 24.73 ? 158 ILE C C   1 
ATOM   5551 O  O   . ILE C 1 158 ? 44.686  -2.528  -16.896 1.00 24.73 ? 158 ILE C O   1 
ATOM   5552 C  CB  . ILE C 1 158 ? 44.849  -3.438  -20.155 1.00 20.98 ? 158 ILE C CB  1 
ATOM   5553 C  CG1 . ILE C 1 158 ? 45.913  -3.310  -21.234 1.00 26.49 ? 158 ILE C CG1 1 
ATOM   5554 C  CG2 . ILE C 1 158 ? 44.095  -2.091  -20.070 1.00 24.30 ? 158 ILE C CG2 1 
ATOM   5555 C  CD1 . ILE C 1 158 ? 45.471  -3.494  -22.679 1.00 25.52 ? 158 ILE C CD1 1 
ATOM   5556 N  N   . PHE C 1 159 ? 43.804  -4.621  -17.392 1.00 25.90 ? 159 PHE C N   1 
ATOM   5557 C  CA  . PHE C 1 159 ? 42.607  -4.511  -16.526 1.00 24.47 ? 159 PHE C CA  1 
ATOM   5558 C  C   . PHE C 1 159 ? 42.979  -4.192  -15.047 1.00 25.83 ? 159 PHE C C   1 
ATOM   5559 O  O   . PHE C 1 159 ? 42.236  -3.497  -14.328 1.00 25.19 ? 159 PHE C O   1 
ATOM   5560 C  CB  . PHE C 1 159 ? 41.674  -5.745  -16.616 1.00 28.83 ? 159 PHE C CB  1 
ATOM   5561 C  CG  . PHE C 1 159 ? 40.933  -5.894  -17.962 1.00 29.36 ? 159 PHE C CG  1 
ATOM   5562 C  CD1 . PHE C 1 159 ? 40.813  -4.803  -18.870 1.00 28.32 ? 159 PHE C CD1 1 
ATOM   5563 C  CD2 . PHE C 1 159 ? 40.354  -7.124  -18.310 1.00 27.16 ? 159 PHE C CD2 1 
ATOM   5564 C  CE1 . PHE C 1 159 ? 40.130  -4.978  -20.096 1.00 26.71 ? 159 PHE C CE1 1 
ATOM   5565 C  CE2 . PHE C 1 159 ? 39.686  -7.292  -19.530 1.00 29.79 ? 159 PHE C CE2 1 
ATOM   5566 C  CZ  . PHE C 1 159 ? 39.602  -6.229  -20.416 1.00 24.54 ? 159 PHE C CZ  1 
ATOM   5567 N  N   . SER C 1 160 ? 44.172  -4.618  -14.670 1.00 27.64 ? 160 SER C N   1 
ATOM   5568 C  CA  . SER C 1 160 ? 44.641  -4.543  -13.307 1.00 26.98 ? 160 SER C CA  1 
ATOM   5569 C  C   . SER C 1 160 ? 45.188  -3.161  -12.990 1.00 30.59 ? 160 SER C C   1 
ATOM   5570 O  O   . SER C 1 160 ? 45.589  -2.880  -11.848 1.00 29.02 ? 160 SER C O   1 
ATOM   5571 C  CB  . SER C 1 160 ? 45.662  -5.649  -13.052 1.00 28.04 ? 160 SER C CB  1 
ATOM   5572 O  OG  . SER C 1 160 ? 46.813  -5.442  -13.841 1.00 30.65 ? 160 SER C OG  1 
ATOM   5573 N  N   . HIS C 1 161 ? 45.156  -2.264  -13.961 1.00 27.33 ? 161 HIS C N   1 
ATOM   5574 C  CA  . HIS C 1 161 ? 45.477  -0.899  -13.709 1.00 29.25 ? 161 HIS C CA  1 
ATOM   5575 C  C   . HIS C 1 161 ? 44.351  0.052   -13.725 1.00 25.17 ? 161 HIS C C   1 
ATOM   5576 O  O   . HIS C 1 161 ? 44.573  1.268   -13.490 1.00 26.56 ? 161 HIS C O   1 
ATOM   5577 C  CB  . HIS C 1 161 ? 46.576  -0.462  -14.681 1.00 32.01 ? 161 HIS C CB  1 
ATOM   5578 C  CG  . HIS C 1 161 ? 47.906  -1.097  -14.358 1.00 37.62 ? 161 HIS C CG  1 
ATOM   5579 N  ND1 . HIS C 1 161 ? 48.221  -2.367  -14.743 1.00 37.66 ? 161 HIS C ND1 1 
ATOM   5580 C  CD2 . HIS C 1 161 ? 48.976  -0.638  -13.567 1.00 36.20 ? 161 HIS C CD2 1 
ATOM   5581 C  CE1 . HIS C 1 161 ? 49.448  -2.681  -14.264 1.00 39.24 ? 161 HIS C CE1 1 
ATOM   5582 N  NE2 . HIS C 1 161 ? 49.905  -1.617  -13.548 1.00 41.21 ? 161 HIS C NE2 1 
ATOM   5583 N  N   . LEU C 1 162 ? 43.129  -0.431  -14.020 1.00 25.99 ? 162 LEU C N   1 
ATOM   5584 C  CA  . LEU C 1 162 ? 41.975  0.456   -14.163 1.00 24.51 ? 162 LEU C CA  1 
ATOM   5585 C  C   . LEU C 1 162 ? 41.608  1.349   -12.952 1.00 23.87 ? 162 LEU C C   1 
ATOM   5586 O  O   . LEU C 1 162 ? 41.146  2.552   -13.143 1.00 21.25 ? 162 LEU C O   1 
ATOM   5587 C  CB  . LEU C 1 162 ? 40.746  -0.329  -14.676 1.00 27.76 ? 162 LEU C CB  1 
ATOM   5588 C  CG  . LEU C 1 162 ? 40.967  -1.000  -16.046 1.00 28.69 ? 162 LEU C CG  1 
ATOM   5589 C  CD1 . LEU C 1 162 ? 39.809  -1.925  -16.374 1.00 29.61 ? 162 LEU C CD1 1 
ATOM   5590 C  CD2 . LEU C 1 162 ? 41.239  -0.034  -17.218 1.00 31.02 ? 162 LEU C CD2 1 
ATOM   5591 N  N   . GLN C 1 163 ? 41.836  0.855   -11.729 1.00 23.04 ? 163 GLN C N   1 
ATOM   5592 C  CA  . GLN C 1 163 ? 41.495  1.646   -10.542 1.00 25.30 ? 163 GLN C CA  1 
ATOM   5593 C  C   . GLN C 1 163 ? 42.382  2.894   -10.348 1.00 22.75 ? 163 GLN C C   1 
ATOM   5594 O  O   . GLN C 1 163 ? 42.048  3.755   -9.500  1.00 25.34 ? 163 GLN C O   1 
ATOM   5595 C  CB  . GLN C 1 163 ? 41.503  0.793   -9.266  1.00 29.40 ? 163 GLN C CB  1 
ATOM   5596 C  CG  . GLN C 1 163 ? 40.486  -0.367  -9.258  1.00 33.50 ? 163 GLN C CG  1 
ATOM   5597 C  CD  . GLN C 1 163 ? 39.005  0.023   -9.267  1.00 36.90 ? 163 GLN C CD  1 
ATOM   5598 O  OE1 . GLN C 1 163 ? 38.592  1.110   -8.803  1.00 35.17 ? 163 GLN C OE1 1 
ATOM   5599 N  NE2 . GLN C 1 163 ? 38.178  -0.899  -9.787  1.00 39.82 ? 163 GLN C NE2 1 
ATOM   5600 N  N   . HIS C 1 164 ? 43.515  2.947   -11.081 1.00 24.70 ? 164 HIS C N   1 
ATOM   5601 C  CA  . HIS C 1 164 ? 44.413  4.115   -11.110 1.00 24.37 ? 164 HIS C CA  1 
ATOM   5602 C  C   . HIS C 1 164 ? 43.963  5.291   -11.962 1.00 27.91 ? 164 HIS C C   1 
ATOM   5603 O  O   . HIS C 1 164 ? 44.418  6.442   -11.777 1.00 26.63 ? 164 HIS C O   1 
ATOM   5604 C  CB  . HIS C 1 164 ? 45.848  3.668   -11.378 1.00 23.06 ? 164 HIS C CB  1 
ATOM   5605 C  CG  . HIS C 1 164 ? 46.326  2.684   -10.341 1.00 22.30 ? 164 HIS C CG  1 
ATOM   5606 N  ND1 . HIS C 1 164 ? 46.340  2.987   -8.999  1.00 24.89 ? 164 HIS C ND1 1 
ATOM   5607 C  CD2 . HIS C 1 164 ? 46.713  1.360   -10.462 1.00 21.39 ? 164 HIS C CD2 1 
ATOM   5608 C  CE1 . HIS C 1 164 ? 46.724  1.898   -8.309  1.00 24.52 ? 164 HIS C CE1 1 
ATOM   5609 N  NE2 . HIS C 1 164 ? 46.913  0.886   -9.187  1.00 23.14 ? 164 HIS C NE2 1 
ATOM   5610 N  N   . VAL C 1 165 ? 43.008  5.020   -12.864 1.00 25.67 ? 165 VAL C N   1 
ATOM   5611 C  CA  . VAL C 1 165 ? 42.503  6.048   -13.763 1.00 23.50 ? 165 VAL C CA  1 
ATOM   5612 C  C   . VAL C 1 165 ? 40.976  6.142   -13.751 1.00 23.85 ? 165 VAL C C   1 
ATOM   5613 O  O   . VAL C 1 165 ? 40.316  6.324   -14.793 1.00 22.05 ? 165 VAL C O   1 
ATOM   5614 C  CB  . VAL C 1 165 ? 43.100  5.823   -15.191 1.00 22.54 ? 165 VAL C CB  1 
ATOM   5615 C  CG1 . VAL C 1 165 ? 44.588  6.212   -15.188 1.00 22.42 ? 165 VAL C CG1 1 
ATOM   5616 C  CG2 . VAL C 1 165 ? 42.923  4.368   -15.623 1.00 23.25 ? 165 VAL C CG2 1 
ATOM   5617 N  N   A LYS C 1 166 ? 40.392  6.045   -12.562 0.50 22.39 ? 166 LYS C N   1 
ATOM   5618 N  N   B LYS C 1 166 ? 40.398  6.052   -12.561 0.50 23.60 ? 166 LYS C N   1 
ATOM   5619 C  CA  A LYS C 1 166 ? 38.938  6.025   -12.449 0.50 24.02 ? 166 LYS C CA  1 
ATOM   5620 C  CA  B LYS C 1 166 ? 38.950  6.017   -12.439 0.50 26.06 ? 166 LYS C CA  1 
ATOM   5621 C  C   A LYS C 1 166 ? 38.224  7.285   -12.908 0.50 25.92 ? 166 LYS C C   1 
ATOM   5622 C  C   B LYS C 1 166 ? 38.228  7.279   -12.896 0.50 27.24 ? 166 LYS C C   1 
ATOM   5623 O  O   A LYS C 1 166 ? 37.040  7.226   -13.275 0.50 28.36 ? 166 LYS C O   1 
ATOM   5624 O  O   B LYS C 1 166 ? 37.041  7.214   -13.250 0.50 29.68 ? 166 LYS C O   1 
ATOM   5625 C  CB  A LYS C 1 166 ? 38.503  5.711   -11.003 0.50 23.66 ? 166 LYS C CB  1 
ATOM   5626 C  CB  B LYS C 1 166 ? 38.555  5.727   -10.984 0.50 27.54 ? 166 LYS C CB  1 
ATOM   5627 C  CG  A LYS C 1 166 ? 38.754  4.279   -10.568 0.50 21.66 ? 166 LYS C CG  1 
ATOM   5628 C  CG  B LYS C 1 166 ? 38.853  6.893   -10.066 0.50 27.37 ? 166 LYS C CG  1 
ATOM   5629 C  CD  A LYS C 1 166 ? 38.239  4.074   -9.148  0.50 22.27 ? 166 LYS C CD  1 
ATOM   5630 C  CD  B LYS C 1 166 ? 38.208  6.707   -8.718  0.50 27.87 ? 166 LYS C CD  1 
ATOM   5631 C  CE  A LYS C 1 166 ? 36.717  4.061   -9.111  0.50 21.93 ? 166 LYS C CE  1 
ATOM   5632 C  CE  B LYS C 1 166 ? 36.863  6.055   -8.882  0.50 27.42 ? 166 LYS C CE  1 
ATOM   5633 N  NZ  A LYS C 1 166 ? 36.184  2.692   -9.349  0.50 20.15 ? 166 LYS C NZ  1 
ATOM   5634 N  NZ  B LYS C 1 166 ? 35.870  6.612   -7.941  0.50 26.67 ? 166 LYS C NZ  1 
ATOM   5635 N  N   . TYR C 1 167 ? 38.911  8.420   -12.887 1.00 25.04 ? 167 TYR C N   1 
ATOM   5636 C  CA  . TYR C 1 167 ? 38.263  9.673   -13.254 1.00 27.51 ? 167 TYR C CA  1 
ATOM   5637 C  C   . TYR C 1 167 ? 38.819  10.242  -14.540 1.00 26.05 ? 167 TYR C C   1 
ATOM   5638 O  O   . TYR C 1 167 ? 39.999  10.050  -14.838 1.00 28.71 ? 167 TYR C O   1 
ATOM   5639 C  CB  . TYR C 1 167 ? 38.421  10.736  -12.161 1.00 28.17 ? 167 TYR C CB  1 
ATOM   5640 C  CG  . TYR C 1 167 ? 37.773  10.376  -10.858 1.00 31.16 ? 167 TYR C CG  1 
ATOM   5641 C  CD1 . TYR C 1 167 ? 36.378  10.470  -10.691 1.00 32.46 ? 167 TYR C CD1 1 
ATOM   5642 C  CD2 . TYR C 1 167 ? 38.547  9.949   -9.784  1.00 32.41 ? 167 TYR C CD2 1 
ATOM   5643 C  CE1 . TYR C 1 167 ? 35.775  10.126  -9.463  1.00 37.25 ? 167 TYR C CE1 1 
ATOM   5644 C  CE2 . TYR C 1 167 ? 37.962  9.618   -8.558  1.00 34.18 ? 167 TYR C CE2 1 
ATOM   5645 C  CZ  . TYR C 1 167 ? 36.579  9.695   -8.398  1.00 36.22 ? 167 TYR C CZ  1 
ATOM   5646 O  OH  . TYR C 1 167 ? 36.018  9.359   -7.181  1.00 39.92 ? 167 TYR C OH  1 
ATOM   5647 N  N   . LYS C 1 168 ? 37.990  11.043  -15.226 1.00 27.82 ? 168 LYS C N   1 
ATOM   5648 C  CA  . LYS C 1 168 ? 38.414  11.750  -16.424 1.00 26.65 ? 168 LYS C CA  1 
ATOM   5649 C  C   . LYS C 1 168 ? 39.630  12.610  -16.152 1.00 31.64 ? 168 LYS C C   1 
ATOM   5650 O  O   . LYS C 1 168 ? 39.678  13.357  -15.139 1.00 36.75 ? 168 LYS C O   1 
ATOM   5651 C  CB  . LYS C 1 168 ? 37.310  12.691  -16.941 1.00 33.07 ? 168 LYS C CB  1 
ATOM   5652 C  CG  . LYS C 1 168 ? 37.799  13.427  -18.194 1.00 33.18 ? 168 LYS C CG  1 
ATOM   5653 C  CD  . LYS C 1 168 ? 36.764  14.273  -18.914 1.00 40.30 ? 168 LYS C CD  1 
ATOM   5654 C  CE  . LYS C 1 168 ? 37.474  15.066  -20.009 1.00 43.02 ? 168 LYS C CE  1 
ATOM   5655 N  NZ  . LYS C 1 168 ? 36.830  14.928  -21.345 1.00 53.82 ? 168 LYS C NZ  1 
ATOM   5656 N  N   . GLY C 1 169 ? 40.600  12.523  -17.072 1.00 29.81 ? 169 GLY C N   1 
ATOM   5657 C  CA  . GLY C 1 169 ? 41.870  13.228  -16.951 1.00 31.20 ? 169 GLY C CA  1 
ATOM   5658 C  C   . GLY C 1 169 ? 42.978  12.446  -16.273 1.00 28.10 ? 169 GLY C C   1 
ATOM   5659 O  O   . GLY C 1 169 ? 44.173  12.796  -16.392 1.00 30.59 ? 169 GLY C O   1 
ATOM   5660 N  N   . GLN C 1 170 ? 42.631  11.397  -15.535 1.00 26.10 ? 170 GLN C N   1 
ATOM   5661 C  CA  . GLN C 1 170 ? 43.689  10.704  -14.796 1.00 25.03 ? 170 GLN C CA  1 
ATOM   5662 C  C   . GLN C 1 170 ? 44.543  9.838   -15.674 1.00 24.29 ? 170 GLN C C   1 
ATOM   5663 O  O   . GLN C 1 170 ? 44.068  9.347   -16.708 1.00 23.54 ? 170 GLN C O   1 
ATOM   5664 C  CB  . GLN C 1 170 ? 43.100  9.861   -13.676 1.00 24.92 ? 170 GLN C CB  1 
ATOM   5665 C  CG  . GLN C 1 170 ? 42.471  10.718  -12.566 1.00 27.51 ? 170 GLN C CG  1 
ATOM   5666 C  CD  . GLN C 1 170 ? 42.087  9.863   -11.366 1.00 29.27 ? 170 GLN C CD  1 
ATOM   5667 O  OE1 . GLN C 1 170 ? 41.538  8.782   -11.545 1.00 28.10 ? 170 GLN C OE1 1 
ATOM   5668 N  NE2 . GLN C 1 170 ? 42.438  10.318  -10.121 1.00 31.44 ? 170 GLN C NE2 1 
ATOM   5669 N  N   . GLU C 1 171 ? 45.795  9.659   -15.274 1.00 23.66 ? 171 GLU C N   1 
ATOM   5670 C  CA  . GLU C 1 171 ? 46.802  8.887   -16.041 1.00 26.90 ? 171 GLU C CA  1 
ATOM   5671 C  C   . GLU C 1 171 ? 47.575  7.983   -15.094 1.00 26.00 ? 171 GLU C C   1 
ATOM   5672 O  O   . GLU C 1 171 ? 47.722  8.344   -13.904 1.00 27.52 ? 171 GLU C O   1 
ATOM   5673 C  CB  . GLU C 1 171 ? 47.801  9.823   -16.734 1.00 27.88 ? 171 GLU C CB  1 
ATOM   5674 C  CG  . GLU C 1 171 ? 47.154  10.954  -17.500 1.00 30.96 ? 171 GLU C CG  1 
ATOM   5675 C  CD  . GLU C 1 171 ? 48.172  11.845  -18.201 1.00 35.68 ? 171 GLU C CD  1 
ATOM   5676 O  OE1 . GLU C 1 171 ? 49.372  11.806  -17.814 1.00 36.75 ? 171 GLU C OE1 1 
ATOM   5677 O  OE2 . GLU C 1 171 ? 47.742  12.562  -19.151 1.00 35.54 ? 171 GLU C OE2 1 
ATOM   5678 N  N   . ALA C 1 172 ? 48.067  6.875   -15.597 1.00 22.06 ? 172 ALA C N   1 
ATOM   5679 C  CA  . ALA C 1 172 ? 48.927  5.974   -14.870 1.00 21.53 ? 172 ALA C CA  1 
ATOM   5680 C  C   . ALA C 1 172 ? 49.853  5.323   -15.865 1.00 22.28 ? 172 ALA C C   1 
ATOM   5681 O  O   . ALA C 1 172 ? 49.779  5.576   -17.042 1.00 20.74 ? 172 ALA C O   1 
ATOM   5682 C  CB  . ALA C 1 172 ? 48.146  4.938   -14.102 1.00 19.28 ? 172 ALA C CB  1 
ATOM   5683 N  N   . PHE C 1 173 ? 50.767  4.527   -15.387 1.00 30.05 ? 173 PHE C N   1 
ATOM   5684 C  CA  . PHE C 1 173 ? 51.620  3.769   -16.269 1.00 31.15 ? 173 PHE C CA  1 
ATOM   5685 C  C   . PHE C 1 173 ? 51.278  2.294   -16.086 1.00 27.99 ? 173 PHE C C   1 
ATOM   5686 O  O   . PHE C 1 173 ? 50.995  1.886   -15.017 1.00 23.08 ? 173 PHE C O   1 
ATOM   5687 C  CB  . PHE C 1 173 ? 53.116  4.083   -16.035 1.00 34.48 ? 173 PHE C CB  1 
ATOM   5688 C  CG  . PHE C 1 173 ? 53.576  5.403   -16.607 1.00 36.72 ? 173 PHE C CG  1 
ATOM   5689 C  CD1 . PHE C 1 173 ? 53.850  5.527   -17.944 1.00 39.19 ? 173 PHE C CD1 1 
ATOM   5690 C  CD2 . PHE C 1 173 ? 53.724  6.513   -15.828 1.00 39.64 ? 173 PHE C CD2 1 
ATOM   5691 C  CE1 . PHE C 1 173 ? 54.271  6.727   -18.490 1.00 42.02 ? 173 PHE C CE1 1 
ATOM   5692 C  CE2 . PHE C 1 173 ? 54.120  7.722   -16.363 1.00 42.04 ? 173 PHE C CE2 1 
ATOM   5693 C  CZ  . PHE C 1 173 ? 54.397  7.834   -17.694 1.00 41.17 ? 173 PHE C CZ  1 
ATOM   5694 N  N   . VAL C 1 174 ? 51.383  1.548   -17.154 1.00 29.44 ? 174 VAL C N   1 
ATOM   5695 C  CA  . VAL C 1 174 ? 51.205  0.118   -17.148 1.00 30.07 ? 174 VAL C CA  1 
ATOM   5696 C  C   . VAL C 1 174 ? 52.494  -0.417  -17.735 1.00 29.31 ? 174 VAL C C   1 
ATOM   5697 O  O   . VAL C 1 174 ? 52.961  0.075   -18.759 1.00 29.73 ? 174 VAL C O   1 
ATOM   5698 C  CB  . VAL C 1 174 ? 50.040  -0.289  -18.063 1.00 32.60 ? 174 VAL C CB  1 
ATOM   5699 C  CG1 . VAL C 1 174 ? 50.232  -1.702  -18.586 1.00 30.43 ? 174 VAL C CG1 1 
ATOM   5700 C  CG2 . VAL C 1 174 ? 48.713  -0.145  -17.335 1.00 35.66 ? 174 VAL C CG2 1 
ATOM   5701 N  N   . PRO C 1 175 ? 53.105  -1.449  -17.096 1.00 31.86 ? 175 PRO C N   1 
ATOM   5702 C  CA  . PRO C 1 175 ? 54.370  -1.957  -17.684 1.00 28.53 ? 175 PRO C CA  1 
ATOM   5703 C  C   . PRO C 1 175 ? 54.125  -2.511  -19.086 1.00 31.13 ? 175 PRO C C   1 
ATOM   5704 O  O   . PRO C 1 175 ? 52.991  -2.834  -19.408 1.00 27.97 ? 175 PRO C O   1 
ATOM   5705 C  CB  . PRO C 1 175 ? 54.816  -3.090  -16.728 1.00 29.05 ? 175 PRO C CB  1 
ATOM   5706 C  CG  . PRO C 1 175 ? 53.864  -3.072  -15.571 1.00 31.08 ? 175 PRO C CG  1 
ATOM   5707 C  CD  . PRO C 1 175 ? 52.782  -2.044  -15.775 1.00 27.51 ? 175 PRO C CD  1 
ATOM   5708 N  N   . GLY C 1 176 ? 55.169  -2.641  -19.894 1.00 28.43 ? 176 GLY C N   1 
ATOM   5709 C  CA  . GLY C 1 176 ? 55.017  -3.215  -21.222 1.00 30.31 ? 176 GLY C CA  1 
ATOM   5710 C  C   . GLY C 1 176 ? 54.773  -4.715  -21.177 1.00 32.97 ? 176 GLY C C   1 
ATOM   5711 O  O   . GLY C 1 176 ? 55.032  -5.365  -20.168 1.00 28.91 ? 176 GLY C O   1 
ATOM   5712 N  N   . PHE C 1 177 ? 54.211  -5.228  -22.274 1.00 29.69 ? 177 PHE C N   1 
ATOM   5713 C  CA  . PHE C 1 177 ? 53.977  -6.660  -22.486 1.00 26.46 ? 177 PHE C CA  1 
ATOM   5714 C  C   . PHE C 1 177 ? 53.809  -6.892  -24.013 1.00 28.23 ? 177 PHE C C   1 
ATOM   5715 O  O   . PHE C 1 177 ? 53.670  -5.921  -24.787 1.00 22.17 ? 177 PHE C O   1 
ATOM   5716 C  CB  . PHE C 1 177 ? 52.766  -7.129  -21.642 1.00 28.34 ? 177 PHE C CB  1 
ATOM   5717 C  CG  . PHE C 1 177 ? 51.416  -6.612  -22.114 1.00 30.27 ? 177 PHE C CG  1 
ATOM   5718 C  CD1 . PHE C 1 177 ? 50.546  -7.452  -22.800 1.00 26.31 ? 177 PHE C CD1 1 
ATOM   5719 C  CD2 . PHE C 1 177 ? 50.996  -5.302  -21.824 1.00 26.89 ? 177 PHE C CD2 1 
ATOM   5720 C  CE1 . PHE C 1 177 ? 49.318  -7.010  -23.225 1.00 25.44 ? 177 PHE C CE1 1 
ATOM   5721 C  CE2 . PHE C 1 177 ? 49.750  -4.845  -22.241 1.00 30.67 ? 177 PHE C CE2 1 
ATOM   5722 C  CZ  . PHE C 1 177 ? 48.916  -5.710  -22.952 1.00 26.46 ? 177 PHE C CZ  1 
ATOM   5723 N  N   . ASN C 1 178 ? 53.781  -8.150  -24.446 1.00 25.11 ? 178 ASN C N   1 
ATOM   5724 C  CA  . ASN C 1 178 ? 53.500  -8.461  -25.818 1.00 24.58 ? 178 ASN C CA  1 
ATOM   5725 C  C   . ASN C 1 178 ? 52.015  -8.180  -26.229 1.00 23.51 ? 178 ASN C C   1 
ATOM   5726 O  O   . ASN C 1 178 ? 51.063  -8.837  -25.800 1.00 22.30 ? 178 ASN C O   1 
ATOM   5727 C  CB  . ASN C 1 178 ? 53.856  -9.934  -26.051 1.00 25.20 ? 178 ASN C CB  1 
ATOM   5728 C  CG  . ASN C 1 178 ? 53.796  -10.311 -27.505 1.00 28.89 ? 178 ASN C CG  1 
ATOM   5729 O  OD1 . ASN C 1 178 ? 53.647  -9.429  -28.375 1.00 23.69 ? 178 ASN C OD1 1 
ATOM   5730 N  ND2 . ASN C 1 178 ? 53.865  -11.622 -27.792 1.00 27.23 ? 178 ASN C ND2 1 
ATOM   5731 N  N   . ILE C 1 179 ? 51.839  -7.144  -27.043 1.00 23.44 ? 179 ILE C N   1 
ATOM   5732 C  CA  . ILE C 1 179 ? 50.507  -6.730  -27.463 1.00 22.52 ? 179 ILE C CA  1 
ATOM   5733 C  C   . ILE C 1 179 ? 49.823  -7.745  -28.368 1.00 22.83 ? 179 ILE C C   1 
ATOM   5734 O  O   . ILE C 1 179 ? 48.567  -7.823  -28.440 1.00 22.04 ? 179 ILE C O   1 
ATOM   5735 C  CB  . ILE C 1 179 ? 50.618  -5.370  -28.121 1.00 23.48 ? 179 ILE C CB  1 
ATOM   5736 C  CG1 . ILE C 1 179 ? 51.338  -4.466  -27.154 1.00 25.38 ? 179 ILE C CG1 1 
ATOM   5737 C  CG2 . ILE C 1 179 ? 49.266  -4.882  -28.643 1.00 21.70 ? 179 ILE C CG2 1 
ATOM   5738 C  CD1 . ILE C 1 179 ? 51.055  -2.987  -27.254 1.00 32.95 ? 179 ILE C CD1 1 
ATOM   5739 N  N   . GLU C 1 180 ? 50.629  -8.517  -29.063 1.00 24.14 ? 180 GLU C N   1 
ATOM   5740 C  CA  . GLU C 1 180 ? 50.135  -9.668  -29.846 1.00 24.20 ? 180 GLU C CA  1 
ATOM   5741 C  C   . GLU C 1 180 ? 49.306  -10.647 -29.023 1.00 23.74 ? 180 GLU C C   1 
ATOM   5742 O  O   . GLU C 1 180 ? 48.473  -11.338 -29.571 1.00 21.84 ? 180 GLU C O   1 
ATOM   5743 C  CB  . GLU C 1 180 ? 51.220  -10.346 -30.673 1.00 26.46 ? 180 GLU C CB  1 
ATOM   5744 C  CG  . GLU C 1 180 ? 50.651  -11.179 -31.801 1.00 29.02 ? 180 GLU C CG  1 
ATOM   5745 C  CD  . GLU C 1 180 ? 51.715  -11.609 -32.798 1.00 30.98 ? 180 GLU C CD  1 
ATOM   5746 O  OE1 . GLU C 1 180 ? 52.897  -11.223 -32.631 1.00 32.04 ? 180 GLU C OE1 1 
ATOM   5747 O  OE2 . GLU C 1 180 ? 51.372  -12.398 -33.699 1.00 32.79 ? 180 GLU C OE2 1 
ATOM   5748 N  N   . GLU C 1 181 ? 49.527  -10.688 -27.700 1.00 21.87 ? 181 GLU C N   1 
ATOM   5749 C  CA  . GLU C 1 181 ? 48.745  -11.582 -26.870 1.00 21.31 ? 181 GLU C CA  1 
ATOM   5750 C  C   . GLU C 1 181 ? 47.237  -11.209 -26.874 1.00 20.95 ? 181 GLU C C   1 
ATOM   5751 O  O   . GLU C 1 181 ? 46.435  -12.089 -26.645 1.00 23.58 ? 181 GLU C O   1 
ATOM   5752 C  CB  . GLU C 1 181 ? 49.333  -11.695 -25.449 1.00 23.57 ? 181 GLU C CB  1 
ATOM   5753 C  CG  . GLU C 1 181 ? 50.839  -12.041 -25.370 1.00 26.62 ? 181 GLU C CG  1 
ATOM   5754 C  CD  . GLU C 1 181 ? 51.393  -12.017 -23.916 1.00 30.47 ? 181 GLU C CD  1 
ATOM   5755 O  OE1 . GLU C 1 181 ? 50.648  -11.670 -22.952 1.00 32.13 ? 181 GLU C OE1 1 
ATOM   5756 O  OE2 . GLU C 1 181 ? 52.614  -12.329 -23.696 1.00 31.59 ? 181 GLU C OE2 1 
ATOM   5757 N  N   . LEU C 1 182 ? 46.918  -9.927  -27.144 1.00 19.81 ? 182 LEU C N   1 
ATOM   5758 C  CA  . LEU C 1 182 ? 45.550  -9.422  -27.162 1.00 17.36 ? 182 LEU C CA  1 
ATOM   5759 C  C   . LEU C 1 182 ? 44.765  -9.962  -28.411 1.00 20.60 ? 182 LEU C C   1 
ATOM   5760 O  O   . LEU C 1 182 ? 43.506  -9.918  -28.471 1.00 20.16 ? 182 LEU C O   1 
ATOM   5761 C  CB  . LEU C 1 182 ? 45.596  -7.854  -27.058 1.00 18.48 ? 182 LEU C CB  1 
ATOM   5762 C  CG  . LEU C 1 182 ? 46.230  -7.283  -25.778 1.00 16.54 ? 182 LEU C CG  1 
ATOM   5763 C  CD1 . LEU C 1 182 ? 46.335  -5.775  -25.725 1.00 17.60 ? 182 LEU C CD1 1 
ATOM   5764 C  CD2 . LEU C 1 182 ? 45.657  -7.770  -24.427 1.00 19.07 ? 182 LEU C CD2 1 
ATOM   5765 N  N   . LEU C 1 183 ? 45.474  -10.429 -29.433 1.00 19.66 ? 183 LEU C N   1 
ATOM   5766 C  CA  . LEU C 1 183 ? 44.871  -10.799 -30.695 1.00 21.91 ? 183 LEU C CA  1 
ATOM   5767 C  C   . LEU C 1 183 ? 44.342  -12.249 -30.625 1.00 21.28 ? 183 LEU C C   1 
ATOM   5768 O  O   . LEU C 1 183 ? 44.869  -13.047 -29.837 1.00 23.11 ? 183 LEU C O   1 
ATOM   5769 C  CB  . LEU C 1 183 ? 45.847  -10.648 -31.881 1.00 21.61 ? 183 LEU C CB  1 
ATOM   5770 C  CG  . LEU C 1 183 ? 46.392  -9.241  -31.995 1.00 20.89 ? 183 LEU C CG  1 
ATOM   5771 C  CD1 . LEU C 1 183 ? 47.346  -9.272  -33.166 1.00 25.35 ? 183 LEU C CD1 1 
ATOM   5772 C  CD2 . LEU C 1 183 ? 45.397  -8.106  -32.174 1.00 25.15 ? 183 LEU C CD2 1 
ATOM   5773 N  N   . PRO C 1 184 ? 43.304  -12.584 -31.422 1.00 22.66 ? 184 PRO C N   1 
ATOM   5774 C  CA  . PRO C 1 184 ? 42.667  -13.894 -31.321 1.00 25.67 ? 184 PRO C CA  1 
ATOM   5775 C  C   . PRO C 1 184 ? 43.442  -14.984 -32.038 1.00 26.11 ? 184 PRO C C   1 
ATOM   5776 O  O   . PRO C 1 184 ? 44.453  -14.694 -32.692 1.00 24.26 ? 184 PRO C O   1 
ATOM   5777 C  CB  . PRO C 1 184 ? 41.316  -13.670 -32.001 1.00 26.37 ? 184 PRO C CB  1 
ATOM   5778 C  CG  . PRO C 1 184 ? 41.636  -12.656 -33.055 1.00 22.14 ? 184 PRO C CG  1 
ATOM   5779 C  CD  . PRO C 1 184 ? 42.564  -11.695 -32.361 1.00 21.88 ? 184 PRO C CD  1 
ATOM   5780 N  N   . GLU C 1 185 ? 42.955  -16.223 -31.942 1.00 28.44 ? 185 GLU C N   1 
ATOM   5781 C  CA  . GLU C 1 185 ? 43.453  -17.306 -32.777 1.00 32.73 ? 185 GLU C CA  1 
ATOM   5782 C  C   . GLU C 1 185 ? 43.202  -16.986 -34.257 1.00 30.91 ? 185 GLU C C   1 
ATOM   5783 O  O   . GLU C 1 185 ? 42.175  -16.324 -34.646 1.00 27.18 ? 185 GLU C O   1 
ATOM   5784 C  CB  . GLU C 1 185 ? 42.713  -18.622 -32.505 1.00 38.01 ? 185 GLU C CB  1 
ATOM   5785 C  CG  . GLU C 1 185 ? 42.961  -19.269 -31.149 1.00 46.38 ? 185 GLU C CG  1 
ATOM   5786 C  CD  . GLU C 1 185 ? 44.389  -19.727 -30.968 1.00 52.54 ? 185 GLU C CD  1 
ATOM   5787 O  OE1 . GLU C 1 185 ? 45.127  -19.043 -30.232 1.00 53.62 ? 185 GLU C OE1 1 
ATOM   5788 O  OE2 . GLU C 1 185 ? 44.784  -20.751 -31.571 1.00 54.08 ? 185 GLU C OE2 1 
ATOM   5789 N  N   . ARG C 1 186 ? 44.108  -17.508 -35.078 1.00 28.60 ? 186 ARG C N   1 
ATOM   5790 C  CA  . ARG C 1 186 ? 44.027  -17.421 -36.532 1.00 28.37 ? 186 ARG C CA  1 
ATOM   5791 C  C   . ARG C 1 186 ? 43.821  -15.983 -37.087 1.00 24.39 ? 186 ARG C C   1 
ATOM   5792 O  O   . ARG C 1 186 ? 42.839  -15.691 -37.808 1.00 27.39 ? 186 ARG C O   1 
ATOM   5793 C  CB  . ARG C 1 186 ? 43.031  -18.463 -37.021 1.00 29.26 ? 186 ARG C CB  1 
ATOM   5794 C  CG  . ARG C 1 186 ? 43.334  -19.845 -36.441 1.00 35.10 ? 186 ARG C CG  1 
ATOM   5795 C  CD  . ARG C 1 186 ? 42.314  -20.908 -36.870 1.00 44.83 ? 186 ARG C CD  1 
ATOM   5796 N  NE  . ARG C 1 186 ? 41.071  -20.856 -36.073 1.00 53.27 ? 186 ARG C NE  1 
ATOM   5797 C  CZ  . ARG C 1 186 ? 39.836  -20.978 -36.577 1.00 57.81 ? 186 ARG C CZ  1 
ATOM   5798 N  NH1 . ARG C 1 186 ? 39.651  -21.149 -37.882 1.00 58.93 ? 186 ARG C NH1 1 
ATOM   5799 N  NH2 . ARG C 1 186 ? 38.775  -20.922 -35.779 1.00 56.79 ? 186 ARG C NH2 1 
ATOM   5800 N  N   . THR C 1 187 ? 44.775  -15.093 -36.771 1.00 21.51 ? 187 THR C N   1 
ATOM   5801 C  CA  . THR C 1 187 ? 44.620  -13.717 -37.177 1.00 20.22 ? 187 THR C CA  1 
ATOM   5802 C  C   . THR C 1 187 ? 44.558  -13.645 -38.746 1.00 19.93 ? 187 THR C C   1 
ATOM   5803 O  O   . THR C 1 187 ? 44.202  -12.593 -39.266 1.00 17.87 ? 187 THR C O   1 
ATOM   5804 C  CB  . THR C 1 187 ? 45.743  -12.814 -36.651 1.00 20.94 ? 187 THR C CB  1 
ATOM   5805 O  OG1 . THR C 1 187 ? 46.991  -13.437 -36.951 1.00 25.67 ? 187 THR C OG1 1 
ATOM   5806 C  CG2 . THR C 1 187 ? 45.635  -12.607 -35.144 1.00 23.09 ? 187 THR C CG2 1 
ATOM   5807 N  N   . ALA C 1 188 ? 44.836  -14.748 -39.459 1.00 18.84 ? 188 ALA C N   1 
ATOM   5808 C  CA  . ALA C 1 188 ? 44.750  -14.741 -40.972 1.00 19.94 ? 188 ALA C CA  1 
ATOM   5809 C  C   . ALA C 1 188 ? 43.270  -14.595 -41.500 1.00 18.79 ? 188 ALA C C   1 
ATOM   5810 O  O   . ALA C 1 188 ? 43.045  -14.300 -42.694 1.00 17.81 ? 188 ALA C O   1 
ATOM   5811 C  CB  . ALA C 1 188 ? 45.409  -15.985 -41.566 1.00 21.81 ? 188 ALA C CB  1 
ATOM   5812 N  N   . GLU C 1 189 ? 42.288  -14.872 -40.623 1.00 19.49 ? 189 GLU C N   1 
ATOM   5813 C  CA  . GLU C 1 189 ? 40.883  -14.793 -40.985 1.00 20.67 ? 189 GLU C CA  1 
ATOM   5814 C  C   . GLU C 1 189 ? 40.370  -13.470 -40.460 1.00 17.34 ? 189 GLU C C   1 
ATOM   5815 O  O   . GLU C 1 189 ? 40.384  -13.239 -39.201 1.00 16.40 ? 189 GLU C O   1 
ATOM   5816 C  CB  . GLU C 1 189 ? 40.119  -15.895 -40.277 1.00 22.41 ? 189 GLU C CB  1 
ATOM   5817 C  CG  . GLU C 1 189 ? 40.701  -17.253 -40.662 1.00 25.49 ? 189 GLU C CG  1 
ATOM   5818 C  CD  . GLU C 1 189 ? 40.143  -18.408 -39.863 1.00 29.63 ? 189 GLU C CD  1 
ATOM   5819 O  OE1 . GLU C 1 189 ? 39.151  -18.244 -39.137 1.00 31.06 ? 189 GLU C OE1 1 
ATOM   5820 O  OE2 . GLU C 1 189 ? 40.730  -19.521 -39.964 1.00 30.28 ? 189 GLU C OE2 1 
ATOM   5821 N  N   . TYR C 1 190 ? 39.968  -12.614 -41.409 1.00 15.22 ? 190 TYR C N   1 
ATOM   5822 C  CA  . TYR C 1 190 ? 39.466  -11.297 -41.005 1.00 14.46 ? 190 TYR C CA  1 
ATOM   5823 C  C   . TYR C 1 190 ? 38.547  -10.715 -42.055 1.00 12.88 ? 190 TYR C C   1 
ATOM   5824 O  O   . TYR C 1 190 ? 38.593  -11.077 -43.220 1.00 13.62 ? 190 TYR C O   1 
ATOM   5825 C  CB  . TYR C 1 190 ? 40.646  -10.358 -40.718 1.00 15.07 ? 190 TYR C CB  1 
ATOM   5826 C  CG  . TYR C 1 190 ? 41.644  -10.200 -41.856 1.00 16.27 ? 190 TYR C CG  1 
ATOM   5827 C  CD1 . TYR C 1 190 ? 41.411  -9.215  -42.840 1.00 14.30 ? 190 TYR C CD1 1 
ATOM   5828 C  CD2 . TYR C 1 190 ? 42.819  -10.964 -41.928 1.00 15.98 ? 190 TYR C CD2 1 
ATOM   5829 C  CE1 . TYR C 1 190 ? 42.298  -8.997  -43.903 1.00 16.34 ? 190 TYR C CE1 1 
ATOM   5830 C  CE2 . TYR C 1 190 ? 43.721  -10.768 -42.970 1.00 18.56 ? 190 TYR C CE2 1 
ATOM   5831 C  CZ  . TYR C 1 190 ? 43.469  -9.789  -43.964 1.00 18.76 ? 190 TYR C CZ  1 
ATOM   5832 O  OH  . TYR C 1 190 ? 44.438  -9.517  -44.998 1.00 16.72 ? 190 TYR C OH  1 
ATOM   5833 N  N   . TYR C 1 191 ? 37.776  -9.685  -41.626 1.00 12.56 ? 191 TYR C N   1 
ATOM   5834 C  CA  . TYR C 1 191 ? 36.959  -8.892  -42.440 1.00 12.09 ? 191 TYR C CA  1 
ATOM   5835 C  C   . TYR C 1 191 ? 37.722  -7.624  -42.702 1.00 12.28 ? 191 TYR C C   1 
ATOM   5836 O  O   . TYR C 1 191 ? 38.384  -7.135  -41.793 1.00 12.77 ? 191 TYR C O   1 
ATOM   5837 C  CB  . TYR C 1 191 ? 35.712  -8.502  -41.652 1.00 11.17 ? 191 TYR C CB  1 
ATOM   5838 C  CG  . TYR C 1 191 ? 34.837  -9.626  -41.122 1.00 12.76 ? 191 TYR C CG  1 
ATOM   5839 C  CD1 . TYR C 1 191 ? 33.799  -10.147 -41.896 1.00 12.76 ? 191 TYR C CD1 1 
ATOM   5840 C  CD2 . TYR C 1 191 ? 34.990  -10.078 -39.765 1.00 12.16 ? 191 TYR C CD2 1 
ATOM   5841 C  CE1 . TYR C 1 191 ? 33.003  -11.187 -41.395 1.00 13.31 ? 191 TYR C CE1 1 
ATOM   5842 C  CE2 . TYR C 1 191 ? 34.170  -11.082 -39.237 1.00 13.35 ? 191 TYR C CE2 1 
ATOM   5843 C  CZ  . TYR C 1 191 ? 33.167  -11.594 -40.027 1.00 14.53 ? 191 TYR C CZ  1 
ATOM   5844 O  OH  . TYR C 1 191 ? 32.376  -12.586 -39.538 1.00 15.92 ? 191 TYR C OH  1 
ATOM   5845 N  N   . ARG C 1 192 ? 37.543  -7.079  -43.915 1.00 11.57 ? 192 ARG C N   1 
ATOM   5846 C  CA  . ARG C 1 192 ? 38.200  -5.782  -44.265 1.00 11.30 ? 192 ARG C CA  1 
ATOM   5847 C  C   . ARG C 1 192 ? 37.203  -4.867  -44.921 1.00 12.73 ? 192 ARG C C   1 
ATOM   5848 O  O   . ARG C 1 192 ? 36.509  -5.232  -45.880 1.00 11.10 ? 192 ARG C O   1 
ATOM   5849 C  CB  . ARG C 1 192 ? 39.342  -6.092  -45.277 1.00 13.07 ? 192 ARG C CB  1 
ATOM   5850 C  CG  . ARG C 1 192 ? 39.949  -4.912  -46.029 1.00 13.61 ? 192 ARG C CG  1 
ATOM   5851 C  CD  . ARG C 1 192 ? 40.722  -3.932  -45.140 1.00 15.69 ? 192 ARG C CD  1 
ATOM   5852 N  NE  . ARG C 1 192 ? 41.724  -4.553  -44.267 1.00 14.41 ? 192 ARG C NE  1 
ATOM   5853 C  CZ  . ARG C 1 192 ? 42.913  -5.075  -44.620 1.00 14.78 ? 192 ARG C CZ  1 
ATOM   5854 N  NH1 . ARG C 1 192 ? 43.275  -5.049  -45.907 1.00 16.44 ? 192 ARG C NH1 1 
ATOM   5855 N  NH2 . ARG C 1 192 ? 43.698  -5.672  -43.710 1.00 16.34 ? 192 ARG C NH2 1 
ATOM   5856 N  N   . TYR C 1 193 ? 37.235  -3.592  -44.516 1.00 10.05 ? 193 TYR C N   1 
ATOM   5857 C  CA  . TYR C 1 193 ? 36.442  -2.556  -45.272 1.00 10.25 ? 193 TYR C CA  1 
ATOM   5858 C  C   . TYR C 1 193 ? 37.052  -1.194  -45.041 1.00 10.78 ? 193 TYR C C   1 
ATOM   5859 O  O   . TYR C 1 193 ? 37.742  -1.013  -44.031 1.00 12.33 ? 193 TYR C O   1 
ATOM   5860 C  CB  . TYR C 1 193 ? 34.936  -2.574  -44.975 1.00 10.17 ? 193 TYR C CB  1 
ATOM   5861 C  CG  . TYR C 1 193 ? 34.574  -2.046  -43.607 1.00 9.06  ? 193 TYR C CG  1 
ATOM   5862 C  CD1 . TYR C 1 193 ? 34.017  -0.788  -43.465 1.00 8.10  ? 193 TYR C CD1 1 
ATOM   5863 C  CD2 . TYR C 1 193 ? 34.784  -2.802  -42.459 1.00 8.99  ? 193 TYR C CD2 1 
ATOM   5864 C  CE1 . TYR C 1 193 ? 33.680  -0.288  -42.224 1.00 10.01 ? 193 TYR C CE1 1 
ATOM   5865 C  CE2 . TYR C 1 193 ? 34.450  -2.309  -41.208 1.00 9.03  ? 193 TYR C CE2 1 
ATOM   5866 C  CZ  . TYR C 1 193 ? 33.894  -1.050  -41.101 1.00 8.72  ? 193 TYR C CZ  1 
ATOM   5867 O  OH  . TYR C 1 193 ? 33.547  -0.527  -39.877 1.00 9.55  ? 193 TYR C OH  1 
ATOM   5868 N  N   . ARG C 1 194 ? 36.728  -0.192  -45.890 1.00 12.54 ? 194 ARG C N   1 
ATOM   5869 C  CA  . ARG C 1 194 ? 37.129  1.241   -45.703 1.00 11.79 ? 194 ARG C CA  1 
ATOM   5870 C  C   . ARG C 1 194 ? 36.034  1.949   -44.890 1.00 13.06 ? 194 ARG C C   1 
ATOM   5871 O  O   . ARG C 1 194 ? 34.856  1.864   -45.209 1.00 12.81 ? 194 ARG C O   1 
ATOM   5872 C  CB  . ARG C 1 194 ? 37.226  1.871   -47.089 1.00 15.09 ? 194 ARG C CB  1 
ATOM   5873 C  CG  . ARG C 1 194 ? 38.463  1.297   -47.792 1.00 20.92 ? 194 ARG C CG  1 
ATOM   5874 C  CD  . ARG C 1 194 ? 38.953  2.006   -49.055 1.00 32.51 ? 194 ARG C CD  1 
ATOM   5875 N  NE  . ARG C 1 194 ? 40.274  1.394   -49.385 1.00 41.73 ? 194 ARG C NE  1 
ATOM   5876 C  CZ  . ARG C 1 194 ? 41.485  1.800   -48.934 1.00 50.97 ? 194 ARG C CZ  1 
ATOM   5877 N  NH1 . ARG C 1 194 ? 41.634  2.874   -48.144 1.00 45.87 ? 194 ARG C NH1 1 
ATOM   5878 N  NH2 . ARG C 1 194 ? 42.583  1.123   -49.295 1.00 46.81 ? 194 ARG C NH2 1 
ATOM   5879 N  N   . GLY C 1 195 ? 36.417  2.526   -43.764 1.00 11.64 ? 195 GLY C N   1 
ATOM   5880 C  CA  . GLY C 1 195 ? 35.468  3.186   -42.857 1.00 12.26 ? 195 GLY C CA  1 
ATOM   5881 C  C   . GLY C 1 195 ? 35.972  4.422   -42.207 1.00 12.00 ? 195 GLY C C   1 
ATOM   5882 O  O   . GLY C 1 195 ? 36.791  5.222   -42.816 1.00 12.56 ? 195 GLY C O   1 
ATOM   5883 N  N   . SER C 1 196 ? 35.555  4.583   -40.938 1.00 11.55 ? 196 SER C N   1 
ATOM   5884 C  CA  . SER C 1 196 ? 35.813  5.891   -40.326 1.00 11.42 ? 196 SER C CA  1 
ATOM   5885 C  C   . SER C 1 196 ? 36.200  5.635   -38.856 1.00 10.75 ? 196 SER C C   1 
ATOM   5886 O  O   . SER C 1 196 ? 36.121  4.526   -38.344 1.00 10.05 ? 196 SER C O   1 
ATOM   5887 C  CB  . SER C 1 196 ? 34.531  6.719   -40.366 1.00 12.19 ? 196 SER C CB  1 
ATOM   5888 O  OG  . SER C 1 196 ? 33.669  6.341   -39.292 1.00 13.37 ? 196 SER C OG  1 
ATOM   5889 N  N   . LEU C 1 197 ? 36.738  6.685   -38.228 1.00 10.10 ? 197 LEU C N   1 
ATOM   5890 C  CA  . LEU C 1 197 ? 36.834  6.753   -36.759 1.00 10.52 ? 197 LEU C CA  1 
ATOM   5891 C  C   . LEU C 1 197 ? 35.403  6.503   -36.244 1.00 10.98 ? 197 LEU C C   1 
ATOM   5892 O  O   . LEU C 1 197 ? 34.464  7.052   -36.829 1.00 12.78 ? 197 LEU C O   1 
ATOM   5893 C  CB  . LEU C 1 197 ? 37.391  8.149   -36.376 1.00 11.69 ? 197 LEU C CB  1 
ATOM   5894 C  CG  . LEU C 1 197 ? 38.910  8.221   -36.593 1.00 12.96 ? 197 LEU C CG  1 
ATOM   5895 C  CD1 . LEU C 1 197 ? 39.297  9.619   -36.208 1.00 13.17 ? 197 LEU C CD1 1 
ATOM   5896 C  CD2 . LEU C 1 197 ? 39.651  7.214   -35.797 1.00 13.99 ? 197 LEU C CD2 1 
ATOM   5897 N  N   . THR C 1 198 ? 35.260  5.750   -35.123 1.00 11.15 ? 198 THR C N   1 
ATOM   5898 C  CA  . THR C 1 198 ? 33.941  5.622   -34.529 1.00 11.72 ? 198 THR C CA  1 
ATOM   5899 C  C   . THR C 1 198 ? 33.614  6.650   -33.410 1.00 13.62 ? 198 THR C C   1 
ATOM   5900 O  O   . THR C 1 198 ? 32.544  6.637   -32.802 1.00 13.72 ? 198 THR C O   1 
ATOM   5901 C  CB  . THR C 1 198 ? 33.676  4.201   -34.033 1.00 12.29 ? 198 THR C CB  1 
ATOM   5902 O  OG1 . THR C 1 198 ? 34.487  3.974   -32.921 1.00 11.80 ? 198 THR C OG1 1 
ATOM   5903 C  CG2 . THR C 1 198 ? 33.997  3.130   -34.994 1.00 13.97 ? 198 THR C CG2 1 
ATOM   5904 N  N   . THR C 1 199 ? 34.576  7.507   -33.104 1.00 12.20 ? 199 THR C N   1 
ATOM   5905 C  CA  . THR C 1 199 ? 34.367  8.685   -32.300 1.00 13.89 ? 199 THR C CA  1 
ATOM   5906 C  C   . THR C 1 199 ? 34.720  9.898   -33.090 1.00 14.05 ? 199 THR C C   1 
ATOM   5907 O  O   . THR C 1 199 ? 35.389  9.808   -34.150 1.00 14.37 ? 199 THR C O   1 
ATOM   5908 C  CB  . THR C 1 199 ? 35.406  8.632   -31.143 1.00 16.06 ? 199 THR C CB  1 
ATOM   5909 O  OG1 . THR C 1 199 ? 36.724  8.437   -31.706 1.00 14.43 ? 199 THR C OG1 1 
ATOM   5910 C  CG2 . THR C 1 199 ? 35.087  7.443   -30.113 1.00 15.79 ? 199 THR C CG2 1 
ATOM   5911 N  N   . PRO C 1 200 ? 34.295  11.066  -32.585 1.00 13.05 ? 200 PRO C N   1 
ATOM   5912 C  CA  . PRO C 1 200 ? 34.664  12.366  -33.199 1.00 13.61 ? 200 PRO C CA  1 
ATOM   5913 C  C   . PRO C 1 200 ? 36.179  12.396  -33.344 1.00 13.96 ? 200 PRO C C   1 
ATOM   5914 O  O   . PRO C 1 200 ? 36.859  11.922  -32.442 1.00 13.32 ? 200 PRO C O   1 
ATOM   5915 C  CB  . PRO C 1 200 ? 34.171  13.368  -32.134 1.00 14.33 ? 200 PRO C CB  1 
ATOM   5916 C  CG  . PRO C 1 200 ? 32.939  12.689  -31.602 1.00 12.54 ? 200 PRO C CG  1 
ATOM   5917 C  CD  . PRO C 1 200 ? 33.350  11.242  -31.447 1.00 11.56 ? 200 PRO C CD  1 
ATOM   5918 N  N   . PRO C 1 201 ? 36.684  12.927  -34.469 1.00 13.15 ? 201 PRO C N   1 
ATOM   5919 C  CA  . PRO C 1 201 ? 35.947  13.662  -35.486 1.00 14.75 ? 201 PRO C CA  1 
ATOM   5920 C  C   . PRO C 1 201 ? 35.345  12.826  -36.599 1.00 11.92 ? 201 PRO C C   1 
ATOM   5921 O  O   . PRO C 1 201 ? 34.881  13.364  -37.551 1.00 15.00 ? 201 PRO C O   1 
ATOM   5922 C  CB  . PRO C 1 201 ? 37.023  14.678  -36.016 1.00 13.42 ? 201 PRO C CB  1 
ATOM   5923 C  CG  . PRO C 1 201 ? 38.064  14.694  -34.958 1.00 16.00 ? 201 PRO C CG  1 
ATOM   5924 C  CD  . PRO C 1 201 ? 38.133  13.238  -34.549 1.00 14.73 ? 201 PRO C CD  1 
ATOM   5925 N  N   . CYS C 1 202 ? 35.331  11.490  -36.404 1.00 13.19 ? 202 CYS C N   1 
ATOM   5926 C  CA  . CYS C 1 202 ? 34.670  10.555  -37.325 1.00 11.11 ? 202 CYS C CA  1 
ATOM   5927 C  C   . CYS C 1 202 ? 35.286  10.569  -38.712 1.00 12.23 ? 202 CYS C C   1 
ATOM   5928 O  O   . CYS C 1 202 ? 34.577  10.269  -39.685 1.00 12.57 ? 202 CYS C O   1 
ATOM   5929 C  CB  . CYS C 1 202 ? 33.091  10.787  -37.450 1.00 12.74 ? 202 CYS C CB  1 
ATOM   5930 S  SG  . CYS C 1 202 ? 32.242  10.744  -35.844 1.00 12.62 ? 202 CYS C SG  1 
ATOM   5931 N  N   . ASN C 1 203 ? 36.595  10.870  -38.829 1.00 12.01 ? 203 ASN C N   1 
ATOM   5932 C  CA  . ASN C 1 203 ? 37.127  11.003  -40.156 1.00 13.51 ? 203 ASN C CA  1 
ATOM   5933 C  C   . ASN C 1 203 ? 37.029  9.709   -40.956 1.00 13.20 ? 203 ASN C C   1 
ATOM   5934 O  O   . ASN C 1 203 ? 37.276  8.628   -40.406 1.00 11.68 ? 203 ASN C O   1 
ATOM   5935 C  CB  . ASN C 1 203 ? 38.598  11.474  -40.122 1.00 14.60 ? 203 ASN C CB  1 
ATOM   5936 C  CG  . ASN C 1 203 ? 38.767  12.716  -39.273 1.00 15.59 ? 203 ASN C CG  1 
ATOM   5937 O  OD1 . ASN C 1 203 ? 38.873  12.620  -38.041 1.00 16.07 ? 203 ASN C OD1 1 
ATOM   5938 N  ND2 . ASN C 1 203 ? 38.696  13.850  -39.889 1.00 18.42 ? 203 ASN C ND2 1 
ATOM   5939 N  N   . PRO C 1 204 ? 36.686  9.821   -42.241 1.00 13.16 ? 204 PRO C N   1 
ATOM   5940 C  CA  . PRO C 1 204 ? 36.489  8.592   -43.095 1.00 13.92 ? 204 PRO C CA  1 
ATOM   5941 C  C   . PRO C 1 204 ? 37.834  8.129   -43.681 1.00 13.89 ? 204 PRO C C   1 
ATOM   5942 O  O   . PRO C 1 204 ? 37.943  7.901   -44.904 1.00 13.73 ? 204 PRO C O   1 
ATOM   5943 C  CB  . PRO C 1 204 ? 35.585  9.065   -44.204 1.00 13.81 ? 204 PRO C CB  1 
ATOM   5944 C  CG  . PRO C 1 204 ? 35.975  10.570  -44.333 1.00 14.19 ? 204 PRO C CG  1 
ATOM   5945 C  CD  . PRO C 1 204 ? 36.243  11.060  -42.920 1.00 13.48 ? 204 PRO C CD  1 
ATOM   5946 N  N   . THR C 1 205 ? 38.778  7.891   -42.783 1.00 13.60 ? 205 THR C N   1 
ATOM   5947 C  CA  . THR C 1 205 ? 40.168  7.676   -43.147 1.00 13.38 ? 205 THR C CA  1 
ATOM   5948 C  C   . THR C 1 205 ? 40.762  6.374   -42.611 1.00 13.61 ? 205 THR C C   1 
ATOM   5949 O  O   . THR C 1 205 ? 42.003  6.138   -42.615 1.00 15.30 ? 205 THR C O   1 
ATOM   5950 C  CB  . THR C 1 205 ? 41.015  8.837   -42.590 1.00 12.29 ? 205 THR C CB  1 
ATOM   5951 O  OG1 . THR C 1 205 ? 40.784  8.881   -41.167 1.00 12.95 ? 205 THR C OG1 1 
ATOM   5952 C  CG2 . THR C 1 205 ? 40.573  10.121  -43.233 1.00 15.23 ? 205 THR C CG2 1 
ATOM   5953 N  N   . VAL C 1 206 ? 39.871  5.481   -42.161 1.00 13.90 ? 206 VAL C N   1 
ATOM   5954 C  CA  . VAL C 1 206 ? 40.274  4.266   -41.511 1.00 11.94 ? 206 VAL C CA  1 
ATOM   5955 C  C   . VAL C 1 206 ? 40.124  2.997   -42.373 1.00 13.20 ? 206 VAL C C   1 
ATOM   5956 O  O   . VAL C 1 206 ? 39.033  2.667   -42.829 1.00 15.14 ? 206 VAL C O   1 
ATOM   5957 C  CB  . VAL C 1 206 ? 39.484  4.016   -40.195 1.00 10.35 ? 206 VAL C CB  1 
ATOM   5958 C  CG1 . VAL C 1 206 ? 39.954  2.632   -39.648 1.00 10.90 ? 206 VAL C CG1 1 
ATOM   5959 C  CG2 . VAL C 1 206 ? 39.776  5.167   -39.198 1.00 10.94 ? 206 VAL C CG2 1 
ATOM   5960 N  N   . LEU C 1 207 ? 41.246  2.259   -42.571 1.00 11.94 ? 207 LEU C N   1 
ATOM   5961 C  CA  . LEU C 1 207 ? 41.170  0.888   -43.118 1.00 12.89 ? 207 LEU C CA  1 
ATOM   5962 C  C   . LEU C 1 207 ? 40.938  -0.074  -41.966 1.00 12.85 ? 207 LEU C C   1 
ATOM   5963 O  O   . LEU C 1 207 ? 41.781  -0.221  -41.059 1.00 13.35 ? 207 LEU C O   1 
ATOM   5964 C  CB  . LEU C 1 207 ? 42.507  0.580   -43.879 1.00 15.41 ? 207 LEU C CB  1 
ATOM   5965 C  CG  . LEU C 1 207 ? 42.476  -0.777  -44.589 1.00 19.62 ? 207 LEU C CG  1 
ATOM   5966 C  CD1 . LEU C 1 207 ? 41.671  -0.635  -45.871 1.00 20.67 ? 207 LEU C CD1 1 
ATOM   5967 C  CD2 . LEU C 1 207 ? 43.860  -1.329  -44.957 1.00 25.95 ? 207 LEU C CD2 1 
ATOM   5968 N  N   . TRP C 1 208 ? 39.730  -0.686  -41.939 1.00 10.66 ? 208 TRP C N   1 
ATOM   5969 C  CA  . TRP C 1 208 ? 39.359  -1.589  -40.833 1.00 11.49 ? 208 TRP C CA  1 
ATOM   5970 C  C   . TRP C 1 208 ? 39.693  -3.028  -41.072 1.00 12.21 ? 208 TRP C C   1 
ATOM   5971 O  O   . TRP C 1 208 ? 39.477  -3.518  -42.168 1.00 10.99 ? 208 TRP C O   1 
ATOM   5972 C  CB  . TRP C 1 208 ? 37.835  -1.499  -40.596 1.00 11.01 ? 208 TRP C CB  1 
ATOM   5973 C  CG  . TRP C 1 208 ? 37.457  -0.289  -39.778 1.00 10.95 ? 208 TRP C CG  1 
ATOM   5974 C  CD1 . TRP C 1 208 ? 36.963  0.945   -40.197 1.00 11.27 ? 208 TRP C CD1 1 
ATOM   5975 C  CD2 . TRP C 1 208 ? 37.562  -0.158  -38.327 1.00 11.30 ? 208 TRP C CD2 1 
ATOM   5976 N  NE1 . TRP C 1 208 ? 36.772  1.770   -39.173 1.00 12.40 ? 208 TRP C NE1 1 
ATOM   5977 C  CE2 . TRP C 1 208 ? 37.140  1.210   -38.005 1.00 11.07 ? 208 TRP C CE2 1 
ATOM   5978 C  CE3 . TRP C 1 208 ? 37.946  -1.003  -37.327 1.00 11.85 ? 208 TRP C CE3 1 
ATOM   5979 C  CZ2 . TRP C 1 208 ? 37.066  1.689   -36.662 1.00 10.49 ? 208 TRP C CZ2 1 
ATOM   5980 C  CZ3 . TRP C 1 208 ? 37.892  -0.531  -36.010 1.00 10.80 ? 208 TRP C CZ3 1 
ATOM   5981 C  CH2 . TRP C 1 208 ? 37.438  0.757   -35.685 1.00 13.24 ? 208 TRP C CH2 1 
ATOM   5982 N  N   . THR C 1 209 ? 40.280  -3.668  -40.081 1.00 11.93 ? 209 THR C N   1 
ATOM   5983 C  CA  . THR C 1 209 ? 40.467  -5.127  -40.079 1.00 12.18 ? 209 THR C CA  1 
ATOM   5984 C  C   . THR C 1 209 ? 39.820  -5.640  -38.835 1.00 13.17 ? 209 THR C C   1 
ATOM   5985 O  O   . THR C 1 209 ? 40.287  -5.290  -37.749 1.00 15.07 ? 209 THR C O   1 
ATOM   5986 C  CB  . THR C 1 209 ? 41.979  -5.423  -40.031 1.00 13.51 ? 209 THR C CB  1 
ATOM   5987 O  OG1 . THR C 1 209 ? 42.541  -4.856  -41.228 1.00 12.64 ? 209 THR C OG1 1 
ATOM   5988 C  CG2 . THR C 1 209 ? 42.196  -6.953  -39.995 1.00 12.58 ? 209 THR C CG2 1 
ATOM   5989 N  N   . VAL C 1 210 ? 38.707  -6.389  -38.979 1.00 12.25 ? 210 VAL C N   1 
ATOM   5990 C  CA  . VAL C 1 210 ? 38.037  -6.979  -37.810 1.00 12.04 ? 210 VAL C CA  1 
ATOM   5991 C  C   . VAL C 1 210 ? 38.344  -8.473  -37.871 1.00 12.15 ? 210 VAL C C   1 
ATOM   5992 O  O   . VAL C 1 210 ? 38.058  -9.140  -38.838 1.00 12.51 ? 210 VAL C O   1 
ATOM   5993 C  CB  . VAL C 1 210 ? 36.534  -6.779  -37.892 1.00 11.31 ? 210 VAL C CB  1 
ATOM   5994 C  CG1 . VAL C 1 210 ? 35.844  -7.384  -36.666 1.00 12.60 ? 210 VAL C CG1 1 
ATOM   5995 C  CG2 . VAL C 1 210 ? 36.306  -5.257  -38.080 1.00 12.41 ? 210 VAL C CG2 1 
ATOM   5996 N  N   . PHE C 1 211 ? 38.969  -8.971  -36.838 1.00 13.54 ? 211 PHE C N   1 
ATOM   5997 C  CA  . PHE C 1 211 ? 39.328  -10.379 -36.914 1.00 13.06 ? 211 PHE C CA  1 
ATOM   5998 C  C   . PHE C 1 211 ? 38.077  -11.283 -36.834 1.00 15.04 ? 211 PHE C C   1 
ATOM   5999 O  O   . PHE C 1 211 ? 37.118  -10.962 -36.097 1.00 17.10 ? 211 PHE C O   1 
ATOM   6000 C  CB  . PHE C 1 211 ? 40.341  -10.655 -35.801 1.00 14.11 ? 211 PHE C CB  1 
ATOM   6001 C  CG  . PHE C 1 211 ? 41.717  -10.025 -36.042 1.00 14.28 ? 211 PHE C CG  1 
ATOM   6002 C  CD1 . PHE C 1 211 ? 42.525  -10.453 -37.074 1.00 18.67 ? 211 PHE C CD1 1 
ATOM   6003 C  CD2 . PHE C 1 211 ? 42.137  -8.996  -35.268 1.00 16.35 ? 211 PHE C CD2 1 
ATOM   6004 C  CE1 . PHE C 1 211 ? 43.769  -9.864  -37.324 1.00 15.43 ? 211 PHE C CE1 1 
ATOM   6005 C  CE2 . PHE C 1 211 ? 43.393  -8.367  -35.501 1.00 17.20 ? 211 PHE C CE2 1 
ATOM   6006 C  CZ  . PHE C 1 211 ? 44.180  -8.812  -36.544 1.00 16.51 ? 211 PHE C CZ  1 
ATOM   6007 N  N   . ARG C 1 212 ? 38.059  -12.369 -37.593 1.00 14.77 ? 212 ARG C N   1 
ATOM   6008 C  CA  . ARG C 1 212 ? 36.869  -13.253 -37.614 1.00 17.63 ? 212 ARG C CA  1 
ATOM   6009 C  C   . ARG C 1 212 ? 36.549  -13.877 -36.235 1.00 17.63 ? 212 ARG C C   1 
ATOM   6010 O  O   . ARG C 1 212 ? 35.379  -14.054 -35.874 1.00 17.47 ? 212 ARG C O   1 
ATOM   6011 C  CB  . ARG C 1 212 ? 37.077  -14.454 -38.509 1.00 19.44 ? 212 ARG C CB  1 
ATOM   6012 C  CG  . ARG C 1 212 ? 35.770  -15.185 -38.874 1.00 21.88 ? 212 ARG C CG  1 
ATOM   6013 C  CD  . ARG C 1 212 ? 36.173  -16.361 -39.724 1.00 25.23 ? 212 ARG C CD  1 
ATOM   6014 N  NE  . ARG C 1 212 ? 35.092  -17.309 -39.862 1.00 30.20 ? 212 ARG C NE  1 
ATOM   6015 C  CZ  . ARG C 1 212 ? 34.943  -18.364 -39.050 1.00 40.03 ? 212 ARG C CZ  1 
ATOM   6016 N  NH1 . ARG C 1 212 ? 35.805  -18.608 -38.055 1.00 42.25 ? 212 ARG C NH1 1 
ATOM   6017 N  NH2 . ARG C 1 212 ? 33.925  -19.194 -39.224 1.00 50.97 ? 212 ARG C NH2 1 
ATOM   6018 N  N   . ASN C 1 213 ? 37.597  -14.322 -35.546 1.00 18.92 ? 213 ASN C N   1 
ATOM   6019 C  CA  . ASN C 1 213 ? 37.445  -15.053 -34.250 1.00 18.41 ? 213 ASN C CA  1 
ATOM   6020 C  C   . ASN C 1 213 ? 37.586  -14.149 -33.068 1.00 18.30 ? 213 ASN C C   1 
ATOM   6021 O  O   . ASN C 1 213 ? 38.465  -13.284 -33.035 1.00 17.55 ? 213 ASN C O   1 
ATOM   6022 C  CB  . ASN C 1 213 ? 38.461  -16.235 -34.187 1.00 22.39 ? 213 ASN C CB  1 
ATOM   6023 C  CG  . ASN C 1 213 ? 38.445  -17.014 -35.460 1.00 22.20 ? 213 ASN C CG  1 
ATOM   6024 O  OD1 . ASN C 1 213 ? 39.487  -17.153 -36.150 1.00 26.14 ? 213 ASN C OD1 1 
ATOM   6025 N  ND2 . ASN C 1 213 ? 37.260  -17.439 -35.858 1.00 26.34 ? 213 ASN C ND2 1 
ATOM   6026 N  N   . PRO C 1 214 ? 36.656  -14.290 -32.119 1.00 19.13 ? 214 PRO C N   1 
ATOM   6027 C  CA  . PRO C 1 214 ? 36.682  -13.526 -30.906 1.00 19.42 ? 214 PRO C CA  1 
ATOM   6028 C  C   . PRO C 1 214 ? 37.746  -14.011 -29.906 1.00 20.83 ? 214 PRO C C   1 
ATOM   6029 O  O   . PRO C 1 214 ? 38.199  -15.198 -30.001 1.00 22.03 ? 214 PRO C O   1 
ATOM   6030 C  CB  . PRO C 1 214 ? 35.302  -13.813 -30.288 1.00 18.80 ? 214 PRO C CB  1 
ATOM   6031 C  CG  . PRO C 1 214 ? 34.934  -15.184 -30.815 1.00 21.09 ? 214 PRO C CG  1 
ATOM   6032 C  CD  . PRO C 1 214 ? 35.449  -15.134 -32.249 1.00 20.57 ? 214 PRO C CD  1 
ATOM   6033 N  N   . VAL C 1 215 ? 38.150  -13.114 -29.005 1.00 18.46 ? 215 VAL C N   1 
ATOM   6034 C  CA  . VAL C 1 215 ? 38.814  -13.610 -27.755 1.00 20.05 ? 215 VAL C CA  1 
ATOM   6035 C  C   . VAL C 1 215 ? 37.810  -13.775 -26.618 1.00 23.50 ? 215 VAL C C   1 
ATOM   6036 O  O   . VAL C 1 215 ? 36.691  -13.255 -26.667 1.00 19.17 ? 215 VAL C O   1 
ATOM   6037 C  CB  . VAL C 1 215 ? 39.953  -12.725 -27.265 1.00 20.18 ? 215 VAL C CB  1 
ATOM   6038 C  CG1 . VAL C 1 215 ? 40.994  -12.614 -28.382 1.00 20.26 ? 215 VAL C CG1 1 
ATOM   6039 C  CG2 . VAL C 1 215 ? 39.434  -11.358 -26.762 1.00 21.17 ? 215 VAL C CG2 1 
ATOM   6040 N  N   . GLN C 1 216 ? 38.249  -14.495 -25.581 1.00 22.08 ? 216 GLN C N   1 
ATOM   6041 C  CA  . GLN C 1 216 ? 37.507  -14.602 -24.314 1.00 24.76 ? 216 GLN C CA  1 
ATOM   6042 C  C   . GLN C 1 216 ? 38.147  -13.902 -23.129 1.00 25.94 ? 216 GLN C C   1 
ATOM   6043 O  O   . GLN C 1 216 ? 39.385  -13.876 -22.956 1.00 28.12 ? 216 GLN C O   1 
ATOM   6044 C  CB  . GLN C 1 216 ? 37.351  -16.043 -23.969 1.00 27.50 ? 216 GLN C CB  1 
ATOM   6045 C  CG  . GLN C 1 216 ? 36.442  -16.755 -24.917 1.00 32.83 ? 216 GLN C CG  1 
ATOM   6046 C  CD  . GLN C 1 216 ? 36.117  -18.145 -24.456 1.00 41.46 ? 216 GLN C CD  1 
ATOM   6047 O  OE1 . GLN C 1 216 ? 36.679  -18.646 -23.457 1.00 43.34 ? 216 GLN C OE1 1 
ATOM   6048 N  NE2 . GLN C 1 216 ? 35.172  -18.784 -25.152 1.00 44.24 ? 216 GLN C NE2 1 
ATOM   6049 N  N   . ILE C 1 217 ? 37.281  -13.284 -22.343 1.00 23.41 ? 217 ILE C N   1 
ATOM   6050 C  CA  . ILE C 1 217 ? 37.598  -12.752 -21.033 1.00 22.23 ? 217 ILE C CA  1 
ATOM   6051 C  C   . ILE C 1 217 ? 36.552  -13.315 -20.006 1.00 25.80 ? 217 ILE C C   1 
ATOM   6052 O  O   . ILE C 1 217 ? 35.492  -13.778 -20.406 1.00 23.43 ? 217 ILE C O   1 
ATOM   6053 C  CB  . ILE C 1 217 ? 37.773  -11.215 -20.976 1.00 24.15 ? 217 ILE C CB  1 
ATOM   6054 C  CG1 . ILE C 1 217 ? 36.423  -10.453 -21.074 1.00 21.29 ? 217 ILE C CG1 1 
ATOM   6055 C  CG2 . ILE C 1 217 ? 38.873  -10.766 -21.977 1.00 23.55 ? 217 ILE C CG2 1 
ATOM   6056 C  CD1 . ILE C 1 217 ? 36.497  -8.931  -20.946 1.00 21.75 ? 217 ILE C CD1 1 
ATOM   6057 N  N   . SER C 1 218 ? 36.896  -13.395 -18.712 1.00 28.40 ? 218 SER C N   1 
ATOM   6058 C  CA  . SER C 1 218 ? 35.975  -14.113 -17.799 1.00 26.04 ? 218 SER C CA  1 
ATOM   6059 C  C   . SER C 1 218 ? 34.853  -13.144 -17.475 1.00 27.23 ? 218 SER C C   1 
ATOM   6060 O  O   . SER C 1 218 ? 35.008  -11.931 -17.671 1.00 26.34 ? 218 SER C O   1 
ATOM   6061 C  CB  . SER C 1 218 ? 36.719  -14.517 -16.497 1.00 27.30 ? 218 SER C CB  1 
ATOM   6062 O  OG  . SER C 1 218 ? 37.053  -13.357 -15.720 1.00 25.84 ? 218 SER C OG  1 
ATOM   6063 N  N   . GLN C 1 219 ? 33.742  -13.653 -16.926 1.00 27.20 ? 219 GLN C N   1 
ATOM   6064 C  CA  . GLN C 1 219 ? 32.713  -12.763 -16.333 1.00 29.76 ? 219 GLN C CA  1 
ATOM   6065 C  C   . GLN C 1 219 ? 33.289  -11.703 -15.382 1.00 26.10 ? 219 GLN C C   1 
ATOM   6066 O  O   . GLN C 1 219 ? 32.930  -10.496 -15.411 1.00 24.72 ? 219 GLN C O   1 
ATOM   6067 C  CB  . GLN C 1 219 ? 31.566  -13.585 -15.650 1.00 33.32 ? 219 GLN C CB  1 
ATOM   6068 C  CG  . GLN C 1 219 ? 30.929  -14.610 -16.580 1.00 38.49 ? 219 GLN C CG  1 
ATOM   6069 C  CD  . GLN C 1 219 ? 29.431  -14.933 -16.344 1.00 46.83 ? 219 GLN C CD  1 
ATOM   6070 O  OE1 . GLN C 1 219 ? 28.588  -14.045 -16.113 1.00 45.45 ? 219 GLN C OE1 1 
ATOM   6071 N  NE2 . GLN C 1 219 ? 29.093  -16.217 -16.463 1.00 44.41 ? 219 GLN C NE2 1 
ATOM   6072 N  N   . GLU C 1 220 ? 34.204  -12.139 -14.517 1.00 30.23 ? 220 GLU C N   1 
ATOM   6073 C  CA  . GLU C 1 220 ? 34.801  -11.204 -13.584 1.00 30.25 ? 220 GLU C CA  1 
ATOM   6074 C  C   . GLU C 1 220 ? 35.574  -10.151 -14.335 1.00 26.08 ? 220 GLU C C   1 
ATOM   6075 O  O   . GLU C 1 220 ? 35.446  -8.981  -13.984 1.00 25.05 ? 220 GLU C O   1 
ATOM   6076 C  CB  . GLU C 1 220 ? 35.669  -11.889 -12.504 1.00 39.43 ? 220 GLU C CB  1 
ATOM   6077 C  CG  . GLU C 1 220 ? 35.047  -13.139 -11.872 1.00 42.70 ? 220 GLU C CG  1 
ATOM   6078 C  CD  . GLU C 1 220 ? 35.222  -14.414 -12.693 1.00 45.33 ? 220 GLU C CD  1 
ATOM   6079 O  OE1 . GLU C 1 220 ? 34.636  -14.540 -13.790 1.00 43.49 ? 220 GLU C OE1 1 
ATOM   6080 O  OE2 . GLU C 1 220 ? 35.937  -15.323 -12.220 1.00 54.44 ? 220 GLU C OE2 1 
ATOM   6081 N  N   . GLN C 1 221 ? 36.342  -10.539 -15.369 1.00 27.31 ? 221 GLN C N   1 
ATOM   6082 C  CA  . GLN C 1 221 ? 37.083  -9.501  -16.135 1.00 22.20 ? 221 GLN C CA  1 
ATOM   6083 C  C   . GLN C 1 221 ? 36.132  -8.516  -16.782 1.00 20.05 ? 221 GLN C C   1 
ATOM   6084 O  O   . GLN C 1 221 ? 36.308  -7.291  -16.632 1.00 20.79 ? 221 GLN C O   1 
ATOM   6085 C  CB  . GLN C 1 221 ? 38.024  -10.105 -17.134 1.00 23.31 ? 221 GLN C CB  1 
ATOM   6086 C  CG  . GLN C 1 221 ? 39.183  -10.847 -16.473 1.00 24.95 ? 221 GLN C CG  1 
ATOM   6087 C  CD  . GLN C 1 221 ? 40.072  -11.407 -17.523 1.00 23.75 ? 221 GLN C CD  1 
ATOM   6088 O  OE1 . GLN C 1 221 ? 39.764  -12.425 -18.158 1.00 25.53 ? 221 GLN C OE1 1 
ATOM   6089 N  NE2 . GLN C 1 221 ? 41.247  -10.787 -17.666 1.00 25.06 ? 221 GLN C NE2 1 
ATOM   6090 N  N   . LEU C 1 222 ? 35.046  -9.031  -17.376 1.00 22.79 ? 222 LEU C N   1 
ATOM   6091 C  CA  . LEU C 1 222 ? 34.083  -8.108  -18.029 1.00 23.67 ? 222 LEU C CA  1 
ATOM   6092 C  C   . LEU C 1 222 ? 33.425  -7.161  -17.062 1.00 23.69 ? 222 LEU C C   1 
ATOM   6093 O  O   . LEU C 1 222 ? 33.310  -5.978  -17.297 1.00 21.81 ? 222 LEU C O   1 
ATOM   6094 C  CB  . LEU C 1 222 ? 33.034  -8.890  -18.792 1.00 23.69 ? 222 LEU C CB  1 
ATOM   6095 C  CG  . LEU C 1 222 ? 31.989  -8.090  -19.561 1.00 23.52 ? 222 LEU C CG  1 
ATOM   6096 C  CD1 . LEU C 1 222 ? 32.574  -7.167  -20.624 1.00 20.89 ? 222 LEU C CD1 1 
ATOM   6097 C  CD2 . LEU C 1 222 ? 31.150  -9.154  -20.226 1.00 21.23 ? 222 LEU C CD2 1 
ATOM   6098 N  N   . LEU C 1 223 ? 32.953  -7.714  -15.926 1.00 24.08 ? 223 LEU C N   1 
ATOM   6099 C  CA  . LEU C 1 223 ? 32.356  -6.877  -14.879 1.00 24.73 ? 223 LEU C CA  1 
ATOM   6100 C  C   . LEU C 1 223 ? 33.262  -5.773  -14.377 1.00 20.33 ? 223 LEU C C   1 
ATOM   6101 O  O   . LEU C 1 223 ? 32.836  -4.614  -14.193 1.00 19.05 ? 223 LEU C O   1 
ATOM   6102 C  CB  . LEU C 1 223 ? 31.918  -7.802  -13.745 1.00 26.57 ? 223 LEU C CB  1 
ATOM   6103 C  CG  . LEU C 1 223 ? 31.144  -7.161  -12.616 1.00 33.11 ? 223 LEU C CG  1 
ATOM   6104 C  CD1 . LEU C 1 223 ? 29.779  -6.726  -13.120 1.00 32.09 ? 223 LEU C CD1 1 
ATOM   6105 C  CD2 . LEU C 1 223 ? 31.094  -8.242  -11.534 1.00 29.35 ? 223 LEU C CD2 1 
ATOM   6106 N  N   . ALA C 1 224 ? 34.511  -6.139  -14.165 1.00 23.38 ? 224 ALA C N   1 
ATOM   6107 C  CA  . ALA C 1 224 ? 35.556  -5.248  -13.679 1.00 23.46 ? 224 ALA C CA  1 
ATOM   6108 C  C   . ALA C 1 224 ? 35.669  -4.066  -14.637 1.00 22.69 ? 224 ALA C C   1 
ATOM   6109 O  O   . ALA C 1 224 ? 35.600  -2.900  -14.213 1.00 27.03 ? 224 ALA C O   1 
ATOM   6110 C  CB  . ALA C 1 224 ? 36.891  -6.020  -13.547 1.00 23.42 ? 224 ALA C CB  1 
ATOM   6111 N  N   . LEU C 1 225 ? 35.743  -4.407  -15.923 1.00 23.61 ? 225 LEU C N   1 
ATOM   6112 C  CA  . LEU C 1 225 ? 35.916  -3.415  -17.008 1.00 22.17 ? 225 LEU C CA  1 
ATOM   6113 C  C   . LEU C 1 225 ? 34.691  -2.509  -17.060 1.00 20.93 ? 225 LEU C C   1 
ATOM   6114 O  O   . LEU C 1 225 ? 34.778  -1.268  -17.089 1.00 22.61 ? 225 LEU C O   1 
ATOM   6115 C  CB  . LEU C 1 225 ? 36.100  -4.149  -18.362 1.00 21.02 ? 225 LEU C CB  1 
ATOM   6116 C  CG  . LEU C 1 225 ? 36.104  -3.228  -19.587 1.00 19.37 ? 225 LEU C CG  1 
ATOM   6117 C  CD1 . LEU C 1 225 ? 37.248  -2.215  -19.475 1.00 21.26 ? 225 LEU C CD1 1 
ATOM   6118 C  CD2 . LEU C 1 225 ? 36.155  -4.016  -20.886 1.00 23.38 ? 225 LEU C CD2 1 
ATOM   6119 N  N   . GLU C 1 226 ? 33.512  -3.113  -17.045 1.00 19.55 ? 226 GLU C N   1 
ATOM   6120 C  CA  . GLU C 1 226 ? 32.260  -2.290  -17.006 1.00 21.58 ? 226 GLU C CA  1 
ATOM   6121 C  C   . GLU C 1 226 ? 32.035  -1.375  -15.786 1.00 22.07 ? 226 GLU C C   1 
ATOM   6122 O  O   . GLU C 1 226 ? 31.287  -0.421  -15.869 1.00 22.06 ? 226 GLU C O   1 
ATOM   6123 C  CB  . GLU C 1 226 ? 31.037  -3.160  -17.142 1.00 21.22 ? 226 GLU C CB  1 
ATOM   6124 C  CG  . GLU C 1 226 ? 31.085  -4.110  -18.363 1.00 23.35 ? 226 GLU C CG  1 
ATOM   6125 C  CD  . GLU C 1 226 ? 30.075  -5.224  -18.318 1.00 26.07 ? 226 GLU C CD  1 
ATOM   6126 O  OE1 . GLU C 1 226 ? 29.752  -5.727  -17.194 1.00 24.14 ? 226 GLU C OE1 1 
ATOM   6127 O  OE2 . GLU C 1 226 ? 29.636  -5.655  -19.399 1.00 22.70 ? 226 GLU C OE2 1 
ATOM   6128 N  N   . THR C 1 227 ? 32.675  -1.712  -14.665 1.00 24.14 ? 227 THR C N   1 
ATOM   6129 C  CA  . THR C 1 227 ? 32.430  -1.013  -13.398 1.00 26.38 ? 227 THR C CA  1 
ATOM   6130 C  C   . THR C 1 227 ? 33.573  -0.121  -12.844 1.00 27.58 ? 227 THR C C   1 
ATOM   6131 O  O   . THR C 1 227 ? 33.352  0.614   -11.875 1.00 28.43 ? 227 THR C O   1 
ATOM   6132 C  CB  . THR C 1 227 ? 31.913  -2.006  -12.301 1.00 22.83 ? 227 THR C CB  1 
ATOM   6133 O  OG1 . THR C 1 227 ? 32.877  -3.032  -12.087 1.00 24.78 ? 227 THR C OG1 1 
ATOM   6134 C  CG2 . THR C 1 227 ? 30.586  -2.622  -12.751 1.00 25.47 ? 227 THR C CG2 1 
ATOM   6135 N  N   . ALA C 1 228 ? 34.759  -0.162  -13.461 1.00 25.89 ? 228 ALA C N   1 
ATOM   6136 C  CA  . ALA C 1 228 ? 35.930  0.504   -12.931 1.00 25.32 ? 228 ALA C CA  1 
ATOM   6137 C  C   . ALA C 1 228 ? 35.935  1.990   -13.166 1.00 28.71 ? 228 ALA C C   1 
ATOM   6138 O  O   . ALA C 1 228 ? 36.527  2.712   -12.346 1.00 28.68 ? 228 ALA C O   1 
ATOM   6139 C  CB  . ALA C 1 228 ? 37.197  -0.108  -13.515 1.00 32.11 ? 228 ALA C CB  1 
ATOM   6140 N  N   . LEU C 1 229 ? 35.310  2.492   -14.241 1.00 24.74 ? 229 LEU C N   1 
ATOM   6141 C  CA  . LEU C 1 229 ? 35.611  3.880   -14.637 1.00 22.93 ? 229 LEU C CA  1 
ATOM   6142 C  C   . LEU C 1 229 ? 34.500  4.836   -14.639 1.00 25.18 ? 229 LEU C C   1 
ATOM   6143 O  O   . LEU C 1 229 ? 33.336  4.457   -14.866 1.00 24.63 ? 229 LEU C O   1 
ATOM   6144 C  CB  . LEU C 1 229 ? 36.282  3.864   -16.026 1.00 23.94 ? 229 LEU C CB  1 
ATOM   6145 C  CG  . LEU C 1 229 ? 37.499  2.948   -16.185 1.00 23.17 ? 229 LEU C CG  1 
ATOM   6146 C  CD1 . LEU C 1 229 ? 37.886  2.782   -17.676 1.00 26.07 ? 229 LEU C CD1 1 
ATOM   6147 C  CD2 . LEU C 1 229 ? 38.707  3.458   -15.392 1.00 21.70 ? 229 LEU C CD2 1 
ATOM   6148 N  N   . TYR C 1 230 ? 34.826  6.076   -14.340 1.00 26.18 ? 230 TYR C N   1 
ATOM   6149 C  CA  . TYR C 1 230 ? 33.924  7.172   -14.509 1.00 30.05 ? 230 TYR C CA  1 
ATOM   6150 C  C   . TYR C 1 230 ? 34.374  8.002   -15.704 1.00 27.53 ? 230 TYR C C   1 
ATOM   6151 O  O   . TYR C 1 230 ? 35.550  7.992   -16.106 1.00 30.61 ? 230 TYR C O   1 
ATOM   6152 C  CB  . TYR C 1 230 ? 33.935  8.075   -13.264 1.00 33.21 ? 230 TYR C CB  1 
ATOM   6153 C  CG  . TYR C 1 230 ? 33.342  7.552   -11.941 1.00 40.13 ? 230 TYR C CG  1 
ATOM   6154 C  CD1 . TYR C 1 230 ? 31.960  7.280   -11.796 1.00 42.46 ? 230 TYR C CD1 1 
ATOM   6155 C  CD2 . TYR C 1 230 ? 34.139  7.479   -10.793 1.00 44.19 ? 230 TYR C CD2 1 
ATOM   6156 C  CE1 . TYR C 1 230 ? 31.422  6.882   -10.566 1.00 42.66 ? 230 TYR C CE1 1 
ATOM   6157 C  CE2 . TYR C 1 230 ? 33.607  7.098   -9.552  1.00 43.50 ? 230 TYR C CE2 1 
ATOM   6158 C  CZ  . TYR C 1 230 ? 32.260  6.801   -9.432  1.00 46.67 ? 230 TYR C CZ  1 
ATOM   6159 O  OH  . TYR C 1 230 ? 31.786  6.409   -8.182  1.00 50.29 ? 230 TYR C OH  1 
ATOM   6160 N  N   . CYS C 1 231 ? 33.421  8.708   -16.284 1.00 28.82 ? 231 CYS C N   1 
ATOM   6161 C  CA  . CYS C 1 231 ? 33.678  9.537   -17.419 1.00 33.22 ? 231 CYS C CA  1 
ATOM   6162 C  C   . CYS C 1 231 ? 34.116  10.895  -16.960 1.00 36.79 ? 231 CYS C C   1 
ATOM   6163 O  O   . CYS C 1 231 ? 34.732  11.634  -17.720 1.00 36.69 ? 231 CYS C O   1 
ATOM   6164 C  CB  . CYS C 1 231 ? 32.404  9.776   -18.147 1.00 32.17 ? 231 CYS C CB  1 
ATOM   6165 S  SG  . CYS C 1 231 ? 32.037  8.451   -19.258 1.00 41.55 ? 231 CYS C SG  1 
ATOM   6166 N  N   . THR C 1 232 ? 33.713  11.218  -15.728 1.00 33.95 ? 232 THR C N   1 
ATOM   6167 C  CA  . THR C 1 232 ? 33.759  12.567  -15.165 1.00 32.33 ? 232 THR C CA  1 
ATOM   6168 C  C   . THR C 1 232 ? 34.963  12.751  -14.259 1.00 32.39 ? 232 THR C C   1 
ATOM   6169 O  O   . THR C 1 232 ? 35.596  11.769  -13.843 1.00 24.66 ? 232 THR C O   1 
ATOM   6170 C  CB  . THR C 1 232 ? 32.531  12.849  -14.290 1.00 31.64 ? 232 THR C CB  1 
ATOM   6171 O  OG1 . THR C 1 232 ? 32.279  11.706  -13.445 1.00 32.65 ? 232 THR C OG1 1 
ATOM   6172 C  CG2 . THR C 1 232 ? 31.337  13.157  -15.152 1.00 33.20 ? 232 THR C CG2 1 
ATOM   6173 N  N   . HIS C 1 233 ? 35.240  14.029  -13.942 1.00 36.39 ? 233 HIS C N   1 
ATOM   6174 C  CA  . HIS C 1 233 ? 36.443  14.441  -13.180 1.00 36.39 ? 233 HIS C CA  1 
ATOM   6175 C  C   . HIS C 1 233 ? 36.326  14.144  -11.729 1.00 37.08 ? 233 HIS C C   1 
ATOM   6176 O  O   . HIS C 1 233 ? 35.214  14.032  -11.221 1.00 32.57 ? 233 HIS C O   1 
ATOM   6177 C  CB  . HIS C 1 233 ? 36.742  15.916  -13.378 1.00 39.99 ? 233 HIS C CB  1 
ATOM   6178 C  CG  . HIS C 1 233 ? 37.591  16.194  -14.600 1.00 45.97 ? 233 HIS C CG  1 
ATOM   6179 N  ND1 . HIS C 1 233 ? 37.072  16.678  -15.758 1.00 49.21 ? 233 HIS C ND1 1 
ATOM   6180 C  CD2 . HIS C 1 233 ? 38.954  16.023  -14.815 1.00 43.19 ? 233 HIS C CD2 1 
ATOM   6181 C  CE1 . HIS C 1 233 ? 38.065  16.815  -16.659 1.00 45.77 ? 233 HIS C CE1 1 
ATOM   6182 N  NE2 . HIS C 1 233 ? 39.215  16.404  -16.079 1.00 47.59 ? 233 HIS C NE2 1 
ATOM   6183 N  N   . MET C 1 234 ? 37.499  14.054  -11.089 1.00 41.34 ? 234 MET C N   1 
ATOM   6184 C  CA  . MET C 1 234 ? 37.758  13.498  -9.721  1.00 49.36 ? 234 MET C CA  1 
ATOM   6185 C  C   . MET C 1 234 ? 36.763  13.703  -8.577  1.00 51.49 ? 234 MET C C   1 
ATOM   6186 O  O   . MET C 1 234 ? 36.452  12.768  -7.811  1.00 50.10 ? 234 MET C O   1 
ATOM   6187 C  CB  . MET C 1 234 ? 39.161  13.884  -9.210  1.00 51.03 ? 234 MET C CB  1 
ATOM   6188 C  CG  . MET C 1 234 ? 39.937  12.655  -8.740  1.00 51.67 ? 234 MET C CG  1 
ATOM   6189 S  SD  . MET C 1 234 ? 40.626  12.590  -7.062  1.00 56.63 ? 234 MET C SD  1 
ATOM   6190 C  CE  . MET C 1 234 ? 41.028  10.834  -6.953  1.00 43.61 ? 234 MET C CE  1 
ATOM   6191 N  N   . ASP C 1 235 ? 36.284  14.927  -8.460  1.00 54.97 ? 235 ASP C N   1 
ATOM   6192 C  CA  . ASP C 1 235 ? 35.394  15.285  -7.381  1.00 54.59 ? 235 ASP C CA  1 
ATOM   6193 C  C   . ASP C 1 235 ? 34.228  16.102  -7.953  1.00 53.64 ? 235 ASP C C   1 
ATOM   6194 O  O   . ASP C 1 235 ? 33.605  16.892  -7.241  1.00 48.33 ? 235 ASP C O   1 
ATOM   6195 C  CB  . ASP C 1 235 ? 36.182  16.036  -6.281  1.00 57.70 ? 235 ASP C CB  1 
ATOM   6196 C  CG  . ASP C 1 235 ? 37.330  16.874  -6.858  1.00 58.93 ? 235 ASP C CG  1 
ATOM   6197 O  OD1 . ASP C 1 235 ? 38.515  16.586  -6.570  1.00 57.73 ? 235 ASP C OD1 1 
ATOM   6198 O  OD2 . ASP C 1 235 ? 37.044  17.805  -7.634  1.00 62.26 ? 235 ASP C OD2 1 
ATOM   6199 N  N   . ASP C 1 236 ? 33.956  15.900  -9.250  1.00 49.84 ? 236 ASP C N   1 
ATOM   6200 C  CA  . ASP C 1 236 ? 32.660  16.237  -9.843  1.00 49.29 ? 236 ASP C CA  1 
ATOM   6201 C  C   . ASP C 1 236 ? 31.586  15.620  -8.938  1.00 49.85 ? 236 ASP C C   1 
ATOM   6202 O  O   . ASP C 1 236 ? 31.577  14.382  -8.714  1.00 44.69 ? 236 ASP C O   1 
ATOM   6203 C  CB  . ASP C 1 236 ? 32.538  15.700  -11.295 1.00 49.64 ? 236 ASP C CB  1 
ATOM   6204 C  CG  . ASP C 1 236 ? 31.187  16.030  -11.956 1.00 47.45 ? 236 ASP C CG  1 
ATOM   6205 O  OD1 . ASP C 1 236 ? 30.160  16.104  -11.244 1.00 51.77 ? 236 ASP C OD1 1 
ATOM   6206 O  OD2 . ASP C 1 236 ? 31.136  16.217  -13.202 1.00 45.60 ? 236 ASP C OD2 1 
ATOM   6207 N  N   . PRO C 1 237 ? 30.684  16.482  -8.409  1.00 55.46 ? 237 PRO C N   1 
ATOM   6208 C  CA  . PRO C 1 237 ? 29.630  16.011  -7.498  1.00 55.03 ? 237 PRO C CA  1 
ATOM   6209 C  C   . PRO C 1 237 ? 28.545  15.141  -8.191  1.00 52.70 ? 237 PRO C C   1 
ATOM   6210 O  O   . PRO C 1 237 ? 27.649  14.625  -7.511  1.00 47.16 ? 237 PRO C O   1 
ATOM   6211 C  CB  . PRO C 1 237 ? 29.048  17.322  -6.916  1.00 54.96 ? 237 PRO C CB  1 
ATOM   6212 C  CG  . PRO C 1 237 ? 29.341  18.369  -7.941  1.00 54.06 ? 237 PRO C CG  1 
ATOM   6213 C  CD  . PRO C 1 237 ? 30.623  17.948  -8.621  1.00 54.92 ? 237 PRO C CD  1 
ATOM   6214 N  N   . SER C 1 238 ? 28.638  14.971  -9.514  1.00 47.95 ? 238 SER C N   1 
ATOM   6215 C  CA  . SER C 1 238 ? 27.672  14.152  -10.264 1.00 44.99 ? 238 SER C CA  1 
ATOM   6216 C  C   . SER C 1 238 ? 28.420  13.130  -11.090 1.00 41.13 ? 238 SER C C   1 
ATOM   6217 O  O   . SER C 1 238 ? 28.530  13.284  -12.308 1.00 41.93 ? 238 SER C O   1 
ATOM   6218 C  CB  . SER C 1 238 ? 26.807  15.018  -11.184 1.00 46.79 ? 238 SER C CB  1 
ATOM   6219 O  OG  . SER C 1 238 ? 26.044  15.935  -10.436 1.00 54.73 ? 238 SER C OG  1 
ATOM   6220 N  N   . PRO C 1 239 ? 28.971  12.098  -10.428 1.00 37.13 ? 239 PRO C N   1 
ATOM   6221 C  CA  . PRO C 1 239 ? 29.832  11.159  -11.157 1.00 35.17 ? 239 PRO C CA  1 
ATOM   6222 C  C   . PRO C 1 239 ? 29.007  10.304  -12.091 1.00 36.19 ? 239 PRO C C   1 
ATOM   6223 O  O   . PRO C 1 239 ? 27.933  9.819   -11.716 1.00 35.18 ? 239 PRO C O   1 
ATOM   6224 C  CB  . PRO C 1 239 ? 30.430  10.275  -10.077 1.00 33.26 ? 239 PRO C CB  1 
ATOM   6225 C  CG  . PRO C 1 239 ? 29.673  10.564  -8.832  1.00 35.42 ? 239 PRO C CG  1 
ATOM   6226 C  CD  . PRO C 1 239 ? 28.978  11.868  -8.972  1.00 37.08 ? 239 PRO C CD  1 
ATOM   6227 N  N   . ARG C 1 240 ? 29.498  10.123  -13.294 1.00 32.69 ? 240 ARG C N   1 
ATOM   6228 C  CA  . ARG C 1 240 ? 28.817  9.210   -14.180 1.00 35.79 ? 240 ARG C CA  1 
ATOM   6229 C  C   . ARG C 1 240 ? 29.771  8.105   -14.581 1.00 30.58 ? 240 ARG C C   1 
ATOM   6230 O  O   . ARG C 1 240 ? 30.939  8.353   -14.889 1.00 28.56 ? 240 ARG C O   1 
ATOM   6231 C  CB  . ARG C 1 240 ? 28.153  9.930   -15.377 1.00 37.32 ? 240 ARG C CB  1 
ATOM   6232 C  CG  . ARG C 1 240 ? 29.007  10.944  -16.119 1.00 45.71 ? 240 ARG C CG  1 
ATOM   6233 C  CD  . ARG C 1 240 ? 28.175  11.859  -17.027 1.00 52.00 ? 240 ARG C CD  1 
ATOM   6234 N  NE  . ARG C 1 240 ? 28.930  13.043  -17.481 1.00 54.61 ? 240 ARG C NE  1 
ATOM   6235 C  CZ  . ARG C 1 240 ? 29.775  13.079  -18.523 1.00 56.08 ? 240 ARG C CZ  1 
ATOM   6236 N  NH1 . ARG C 1 240 ? 30.003  11.990  -19.264 1.00 51.70 ? 240 ARG C NH1 1 
ATOM   6237 N  NH2 . ARG C 1 240 ? 30.413  14.219  -18.813 1.00 51.81 ? 240 ARG C NH2 1 
ATOM   6238 N  N   . GLU C 1 241 ? 29.274  6.879   -14.514 1.00 28.65 ? 241 GLU C N   1 
ATOM   6239 C  CA  . GLU C 1 241 ? 30.028  5.718   -14.923 1.00 27.86 ? 241 GLU C CA  1 
ATOM   6240 C  C   . GLU C 1 241 ? 30.337  5.751   -16.432 1.00 24.44 ? 241 GLU C C   1 
ATOM   6241 O  O   . GLU C 1 241 ? 29.534  6.226   -17.262 1.00 27.85 ? 241 GLU C O   1 
ATOM   6242 C  CB  . GLU C 1 241 ? 29.289  4.414   -14.588 1.00 31.39 ? 241 GLU C CB  1 
ATOM   6243 C  CG  . GLU C 1 241 ? 28.281  4.553   -13.470 1.00 37.80 ? 241 GLU C CG  1 
ATOM   6244 C  CD  . GLU C 1 241 ? 27.615  3.249   -13.063 1.00 42.17 ? 241 GLU C CD  1 
ATOM   6245 O  OE1 . GLU C 1 241 ? 26.897  2.604   -13.870 1.00 44.58 ? 241 GLU C OE1 1 
ATOM   6246 O  OE2 . GLU C 1 241 ? 27.777  2.877   -11.881 1.00 53.83 ? 241 GLU C OE2 1 
ATOM   6247 N  N   . MET C 1 242 ? 31.495  5.204   -16.748 1.00 22.78 ? 242 MET C N   1 
ATOM   6248 C  CA  . MET C 1 242 ? 31.925  5.035   -18.124 1.00 20.45 ? 242 MET C CA  1 
ATOM   6249 C  C   . MET C 1 242 ? 31.409  3.646   -18.559 1.00 17.95 ? 242 MET C C   1 
ATOM   6250 O  O   . MET C 1 242 ? 32.002  2.535   -18.307 1.00 17.56 ? 242 MET C O   1 
ATOM   6251 C  CB  . MET C 1 242 ? 33.435  5.227   -18.279 1.00 20.97 ? 242 MET C CB  1 
ATOM   6252 C  CG  . MET C 1 242 ? 33.828  5.104   -19.748 1.00 20.57 ? 242 MET C CG  1 
ATOM   6253 S  SD  . MET C 1 242 ? 35.607  5.134   -19.984 1.00 22.71 ? 242 MET C SD  1 
ATOM   6254 C  CE  . MET C 1 242 ? 35.985  6.849   -19.600 1.00 19.97 ? 242 MET C CE  1 
ATOM   6255 N  N   . ILE C 1 243 ? 30.216  3.737   -19.163 1.00 17.56 ? 243 ILE C N   1 
ATOM   6256 C  CA  . ILE C 1 243 ? 29.515  2.575   -19.674 1.00 16.49 ? 243 ILE C CA  1 
ATOM   6257 C  C   . ILE C 1 243 ? 28.983  2.804   -21.087 1.00 14.35 ? 243 ILE C C   1 
ATOM   6258 O  O   . ILE C 1 243 ? 28.771  3.949   -21.469 1.00 16.18 ? 243 ILE C O   1 
ATOM   6259 C  CB  . ILE C 1 243 ? 28.383  2.048   -18.714 1.00 14.90 ? 243 ILE C CB  1 
ATOM   6260 C  CG1 . ILE C 1 243 ? 27.428  3.187   -18.319 1.00 17.18 ? 243 ILE C CG1 1 
ATOM   6261 C  CG2 . ILE C 1 243 ? 29.027  1.173   -17.548 1.00 18.32 ? 243 ILE C CG2 1 
ATOM   6262 C  CD1 . ILE C 1 243 ? 26.316  2.694   -17.382 1.00 18.11 ? 243 ILE C CD1 1 
ATOM   6263 N  N   . ASN C 1 244 ? 28.710  1.709   -21.798 1.00 14.95 ? 244 ASN C N   1 
ATOM   6264 C  CA  . ASN C 1 244 ? 28.008  1.823   -23.125 1.00 17.01 ? 244 ASN C CA  1 
ATOM   6265 C  C   . ASN C 1 244 ? 28.751  2.757   -24.069 1.00 17.46 ? 244 ASN C C   1 
ATOM   6266 O  O   . ASN C 1 244 ? 28.145  3.604   -24.745 1.00 15.98 ? 244 ASN C O   1 
ATOM   6267 C  CB  . ASN C 1 244 ? 26.561  2.361   -22.936 1.00 17.27 ? 244 ASN C CB  1 
ATOM   6268 C  CG  . ASN C 1 244 ? 25.746  1.500   -22.013 1.00 18.04 ? 244 ASN C CG  1 
ATOM   6269 O  OD1 . ASN C 1 244 ? 25.878  0.249   -22.025 1.00 20.84 ? 244 ASN C OD1 1 
ATOM   6270 N  ND2 . ASN C 1 244 ? 24.995  2.186   -21.094 1.00 18.88 ? 244 ASN C ND2 1 
ATOM   6271 N  N   . ASN C 1 245 ? 30.077  2.691   -24.023 1.00 17.00 ? 245 ASN C N   1 
ATOM   6272 C  CA  . ASN C 1 245 ? 30.840  3.646   -24.846 1.00 15.50 ? 245 ASN C CA  1 
ATOM   6273 C  C   . ASN C 1 245 ? 31.151  3.149   -26.242 1.00 15.54 ? 245 ASN C C   1 
ATOM   6274 O  O   . ASN C 1 245 ? 32.336  3.015   -26.656 1.00 15.29 ? 245 ASN C O   1 
ATOM   6275 C  CB  . ASN C 1 245 ? 32.106  4.092   -24.103 1.00 16.23 ? 245 ASN C CB  1 
ATOM   6276 C  CG  . ASN C 1 245 ? 32.980  2.955   -23.670 1.00 14.49 ? 245 ASN C CG  1 
ATOM   6277 O  OD1 . ASN C 1 245 ? 32.644  1.754   -23.711 1.00 15.67 ? 245 ASN C OD1 1 
ATOM   6278 N  ND2 . ASN C 1 245 ? 34.189  3.324   -23.306 1.00 15.41 ? 245 ASN C ND2 1 
ATOM   6279 N  N   . PHE C 1 246 ? 30.090  2.841   -26.953 1.00 14.69 ? 246 PHE C N   1 
ATOM   6280 C  CA  . PHE C 1 246 ? 30.230  2.244   -28.288 1.00 13.87 ? 246 PHE C CA  1 
ATOM   6281 C  C   . PHE C 1 246 ? 29.278  3.049   -29.108 1.00 12.67 ? 246 PHE C C   1 
ATOM   6282 O  O   . PHE C 1 246 ? 28.208  3.485   -28.625 1.00 13.82 ? 246 PHE C O   1 
ATOM   6283 C  CB  . PHE C 1 246 ? 29.923  0.685   -28.323 1.00 13.11 ? 246 PHE C CB  1 
ATOM   6284 C  CG  . PHE C 1 246 ? 28.529  0.358   -27.907 1.00 14.34 ? 246 PHE C CG  1 
ATOM   6285 C  CD1 . PHE C 1 246 ? 27.470  0.338   -28.830 1.00 14.52 ? 246 PHE C CD1 1 
ATOM   6286 C  CD2 . PHE C 1 246 ? 28.262  0.201   -26.549 1.00 15.27 ? 246 PHE C CD2 1 
ATOM   6287 C  CE1 . PHE C 1 246 ? 26.134  0.158   -28.431 1.00 14.76 ? 246 PHE C CE1 1 
ATOM   6288 C  CE2 . PHE C 1 246 ? 26.929  -0.020  -26.119 1.00 14.93 ? 246 PHE C CE2 1 
ATOM   6289 C  CZ  . PHE C 1 246 ? 25.875  -0.027  -27.046 1.00 14.73 ? 246 PHE C CZ  1 
ATOM   6290 N  N   . ARG C 1 247 ? 29.606  3.211   -30.405 1.00 10.79 ? 247 ARG C N   1 
ATOM   6291 C  CA  . ARG C 1 247 ? 28.658  3.841   -31.374 1.00 11.69 ? 247 ARG C CA  1 
ATOM   6292 C  C   . ARG C 1 247 ? 27.685  2.815   -31.958 1.00 10.59 ? 247 ARG C C   1 
ATOM   6293 O  O   . ARG C 1 247 ? 28.077  1.651   -32.160 1.00 10.80 ? 247 ARG C O   1 
ATOM   6294 C  CB  . ARG C 1 247 ? 29.495  4.496   -32.493 1.00 11.13 ? 247 ARG C CB  1 
ATOM   6295 C  CG  . ARG C 1 247 ? 28.767  5.557   -33.265 1.00 11.38 ? 247 ARG C CG  1 
ATOM   6296 C  CD  . ARG C 1 247 ? 29.574  5.926   -34.529 1.00 9.99  ? 247 ARG C CD  1 
ATOM   6297 N  NE  . ARG C 1 247 ? 29.005  7.122   -35.118 1.00 10.96 ? 247 ARG C NE  1 
ATOM   6298 C  CZ  . ARG C 1 247 ? 29.465  7.676   -36.263 1.00 9.08  ? 247 ARG C CZ  1 
ATOM   6299 N  NH1 . ARG C 1 247 ? 30.466  7.104   -36.932 1.00 10.31 ? 247 ARG C NH1 1 
ATOM   6300 N  NH2 . ARG C 1 247 ? 28.929  8.839   -36.713 1.00 9.41  ? 247 ARG C NH2 1 
ATOM   6301 N  N   . GLN C 1 248 ? 26.432  3.232   -32.216 1.00 11.89 ? 248 GLN C N   1 
ATOM   6302 C  CA  . GLN C 1 248 ? 25.464  2.319   -32.841 1.00 11.53 ? 248 GLN C CA  1 
ATOM   6303 C  C   . GLN C 1 248 ? 25.932  2.033   -34.275 1.00 12.14 ? 248 GLN C C   1 
ATOM   6304 O  O   . GLN C 1 248 ? 26.663  2.877   -34.864 1.00 12.28 ? 248 GLN C O   1 
ATOM   6305 C  CB  . GLN C 1 248 ? 24.131  3.072   -32.995 1.00 11.21 ? 248 GLN C CB  1 
ATOM   6306 C  CG  . GLN C 1 248 ? 23.434  3.430   -31.674 1.00 11.29 ? 248 GLN C CG  1 
ATOM   6307 C  CD  . GLN C 1 248 ? 23.094  2.204   -30.853 1.00 12.61 ? 248 GLN C CD  1 
ATOM   6308 O  OE1 . GLN C 1 248 ? 23.810  1.851   -29.878 1.00 15.24 ? 248 GLN C OE1 1 
ATOM   6309 N  NE2 . GLN C 1 248 ? 21.962  1.536   -31.219 1.00 15.58 ? 248 GLN C NE2 1 
ATOM   6310 N  N   . VAL C 1 249 ? 25.632  0.849   -34.805 1.00 11.68 ? 249 VAL C N   1 
ATOM   6311 C  CA  . VAL C 1 249 ? 25.958  0.570   -36.230 1.00 11.77 ? 249 VAL C CA  1 
ATOM   6312 C  C   . VAL C 1 249 ? 25.347  1.592   -37.214 1.00 12.33 ? 249 VAL C C   1 
ATOM   6313 O  O   . VAL C 1 249 ? 24.228  2.125   -36.985 1.00 12.05 ? 249 VAL C O   1 
ATOM   6314 C  CB  . VAL C 1 249 ? 25.641  -0.896  -36.692 1.00 12.85 ? 249 VAL C CB  1 
ATOM   6315 C  CG1 . VAL C 1 249 ? 26.393  -1.878  -35.857 1.00 13.45 ? 249 VAL C CG1 1 
ATOM   6316 C  CG2 . VAL C 1 249 ? 24.180  -1.281  -36.589 1.00 16.02 ? 249 VAL C CG2 1 
ATOM   6317 N  N   . GLN C 1 250 ? 26.067  1.778   -38.310 1.00 11.17 ? 250 GLN C N   1 
ATOM   6318 C  CA  . GLN C 1 250 ? 25.743  2.791   -39.365 1.00 10.74 ? 250 GLN C CA  1 
ATOM   6319 C  C   . GLN C 1 250 ? 25.120  2.079   -40.533 1.00 12.31 ? 250 GLN C C   1 
ATOM   6320 O  O   . GLN C 1 250 ? 25.502  0.954   -40.822 1.00 13.74 ? 250 GLN C O   1 
ATOM   6321 C  CB  . GLN C 1 250 ? 27.044  3.526   -39.827 1.00 11.28 ? 250 GLN C CB  1 
ATOM   6322 C  CG  . GLN C 1 250 ? 27.840  4.080   -38.612 1.00 11.21 ? 250 GLN C CG  1 
ATOM   6323 C  CD  . GLN C 1 250 ? 27.133  5.223   -37.955 1.00 10.86 ? 250 GLN C CD  1 
ATOM   6324 O  OE1 . GLN C 1 250 ? 26.920  6.267   -38.611 1.00 11.72 ? 250 GLN C OE1 1 
ATOM   6325 N  NE2 . GLN C 1 250 ? 26.802  5.071   -36.634 1.00 12.07 ? 250 GLN C NE2 1 
ATOM   6326 N  N   . LYS C 1 251 ? 24.250  2.757   -41.268 1.00 13.32 ? 251 LYS C N   1 
ATOM   6327 C  CA  . LYS C 1 251 ? 23.882  2.181   -42.596 1.00 11.78 ? 251 LYS C CA  1 
ATOM   6328 C  C   . LYS C 1 251 ? 25.115  2.017   -43.492 1.00 12.66 ? 251 LYS C C   1 
ATOM   6329 O  O   . LYS C 1 251 ? 26.077  2.832   -43.426 1.00 14.17 ? 251 LYS C O   1 
ATOM   6330 C  CB  . LYS C 1 251 ? 22.881  3.131   -43.203 1.00 12.99 ? 251 LYS C CB  1 
ATOM   6331 C  CG  . LYS C 1 251 ? 21.518  3.029   -42.518 1.00 15.30 ? 251 LYS C CG  1 
ATOM   6332 C  CD  . LYS C 1 251 ? 20.594  4.016   -43.154 1.00 12.45 ? 251 LYS C CD  1 
ATOM   6333 C  CE  . LYS C 1 251 ? 19.085  3.861   -42.758 1.00 10.50 ? 251 LYS C CE  1 
ATOM   6334 N  NZ  . LYS C 1 251 ? 18.894  3.842   -41.254 1.00 11.72 ? 251 LYS C NZ  1 
ATOM   6335 N  N   . PHE C 1 252 ? 25.044  0.968   -44.333 1.00 15.65 ? 252 PHE C N   1 
ATOM   6336 C  CA  . PHE C 1 252 ? 26.141  0.534   -45.172 1.00 15.53 ? 252 PHE C CA  1 
ATOM   6337 C  C   . PHE C 1 252 ? 25.460  -0.124  -46.339 1.00 21.00 ? 252 PHE C C   1 
ATOM   6338 O  O   . PHE C 1 252 ? 25.118  -1.318  -46.289 1.00 23.90 ? 252 PHE C O   1 
ATOM   6339 C  CB  . PHE C 1 252 ? 26.868  -0.532  -44.422 1.00 16.54 ? 252 PHE C CB  1 
ATOM   6340 C  CG  . PHE C 1 252 ? 28.108  -1.050  -45.080 1.00 14.78 ? 252 PHE C CG  1 
ATOM   6341 C  CD1 . PHE C 1 252 ? 29.271  -0.391  -44.958 1.00 13.41 ? 252 PHE C CD1 1 
ATOM   6342 C  CD2 . PHE C 1 252 ? 28.124  -2.310  -45.654 1.00 16.43 ? 252 PHE C CD2 1 
ATOM   6343 C  CE1 . PHE C 1 252 ? 30.476  -0.854  -45.523 1.00 14.17 ? 252 PHE C CE1 1 
ATOM   6344 C  CE2 . PHE C 1 252 ? 29.334  -2.811  -46.230 1.00 16.06 ? 252 PHE C CE2 1 
ATOM   6345 C  CZ  . PHE C 1 252 ? 30.505  -2.105  -46.119 1.00 14.72 ? 252 PHE C CZ  1 
ATOM   6346 N  N   . ASP C 1 253 ? 25.195  0.701   -47.304 1.00 22.87 ? 253 ASP C N   1 
ATOM   6347 C  CA  . ASP C 1 253 ? 24.338  0.328   -48.420 1.00 25.93 ? 253 ASP C CA  1 
ATOM   6348 C  C   . ASP C 1 253 ? 25.075  0.202   -49.754 1.00 22.81 ? 253 ASP C C   1 
ATOM   6349 O  O   . ASP C 1 253 ? 25.873  1.069   -50.141 1.00 24.03 ? 253 ASP C O   1 
ATOM   6350 C  CB  . ASP C 1 253 ? 23.181  1.326   -48.523 1.00 29.30 ? 253 ASP C CB  1 
ATOM   6351 C  CG  . ASP C 1 253 ? 22.086  0.825   -49.455 1.00 37.78 ? 253 ASP C CG  1 
ATOM   6352 O  OD1 . ASP C 1 253 ? 21.541  -0.317  -49.240 1.00 40.27 ? 253 ASP C OD1 1 
ATOM   6353 O  OD2 . ASP C 1 253 ? 21.816  1.572   -50.408 1.00 40.83 ? 253 ASP C OD2 1 
ATOM   6354 N  N   . GLU C 1 254 ? 24.769  -0.870  -50.483 1.00 24.67 ? 254 GLU C N   1 
ATOM   6355 C  CA  . GLU C 1 254 ? 25.387  -1.110  -51.766 1.00 25.12 ? 254 GLU C CA  1 
ATOM   6356 C  C   . GLU C 1 254 ? 26.906  -1.124  -51.627 1.00 21.72 ? 254 GLU C C   1 
ATOM   6357 O  O   . GLU C 1 254 ? 27.630  -0.654  -52.491 1.00 22.58 ? 254 GLU C O   1 
ATOM   6358 C  CB  . GLU C 1 254 ? 24.912  -0.076  -52.802 1.00 26.00 ? 254 GLU C CB  1 
ATOM   6359 C  CG  . GLU C 1 254 ? 23.400  -0.151  -52.999 1.00 29.17 ? 254 GLU C CG  1 
ATOM   6360 C  CD  . GLU C 1 254 ? 22.897  0.600   -54.216 1.00 41.12 ? 254 GLU C CD  1 
ATOM   6361 O  OE1 . GLU C 1 254 ? 23.720  0.915   -55.114 1.00 44.44 ? 254 GLU C OE1 1 
ATOM   6362 O  OE2 . GLU C 1 254 ? 21.666  0.864   -54.281 1.00 46.38 ? 254 GLU C OE2 1 
ATOM   6363 N  N   . ARG C 1 255 ? 27.364  -1.616  -50.493 1.00 18.18 ? 255 ARG C N   1 
ATOM   6364 C  CA  . ARG C 1 255 ? 28.800  -1.865  -50.307 1.00 19.50 ? 255 ARG C CA  1 
ATOM   6365 C  C   . ARG C 1 255 ? 29.093  -3.272  -49.866 1.00 18.41 ? 255 ARG C C   1 
ATOM   6366 O  O   . ARG C 1 255 ? 28.193  -4.006  -49.364 1.00 20.85 ? 255 ARG C O   1 
ATOM   6367 C  CB  . ARG C 1 255 ? 29.408  -0.892  -49.294 1.00 19.09 ? 255 ARG C CB  1 
ATOM   6368 C  CG  . ARG C 1 255 ? 29.235  0.535   -49.743 1.00 17.89 ? 255 ARG C CG  1 
ATOM   6369 C  CD  . ARG C 1 255 ? 29.768  1.513   -48.703 1.00 20.63 ? 255 ARG C CD  1 
ATOM   6370 N  NE  . ARG C 1 255 ? 31.161  1.171   -48.535 1.00 19.05 ? 255 ARG C NE  1 
ATOM   6371 C  CZ  . ARG C 1 255 ? 31.895  1.480   -47.464 1.00 20.16 ? 255 ARG C CZ  1 
ATOM   6372 N  NH1 . ARG C 1 255 ? 31.341  2.215   -46.509 1.00 18.66 ? 255 ARG C NH1 1 
ATOM   6373 N  NH2 . ARG C 1 255 ? 33.174  1.038   -47.424 1.00 14.75 ? 255 ARG C NH2 1 
ATOM   6374 N  N   . LEU C 1 256 ? 30.372  -3.684  -50.053 1.00 17.97 ? 256 LEU C N   1 
ATOM   6375 C  CA  . LEU C 1 256 ? 30.810  -5.005  -49.580 1.00 18.52 ? 256 LEU C CA  1 
ATOM   6376 C  C   . LEU C 1 256 ? 31.797  -4.924  -48.365 1.00 16.97 ? 256 LEU C C   1 
ATOM   6377 O  O   . LEU C 1 256 ? 32.510  -3.922  -48.152 1.00 17.38 ? 256 LEU C O   1 
ATOM   6378 C  CB  . LEU C 1 256 ? 31.464  -5.850  -50.698 1.00 20.47 ? 256 LEU C CB  1 
ATOM   6379 C  CG  . LEU C 1 256 ? 30.584  -6.168  -51.924 1.00 24.68 ? 256 LEU C CG  1 
ATOM   6380 C  CD1 . LEU C 1 256 ? 31.445  -6.224  -53.158 1.00 23.96 ? 256 LEU C CD1 1 
ATOM   6381 C  CD2 . LEU C 1 256 ? 29.755  -7.442  -51.748 1.00 25.33 ? 256 LEU C CD2 1 
ATOM   6382 N  N   . VAL C 1 257 ? 31.858  -6.032  -47.630 1.00 16.34 ? 257 VAL C N   1 
ATOM   6383 C  CA  . VAL C 1 257 ? 32.934  -6.242  -46.668 1.00 15.15 ? 257 VAL C CA  1 
ATOM   6384 C  C   . VAL C 1 257 ? 33.721  -7.412  -47.245 1.00 14.46 ? 257 VAL C C   1 
ATOM   6385 O  O   . VAL C 1 257 ? 33.157  -8.448  -47.591 1.00 17.61 ? 257 VAL C O   1 
ATOM   6386 C  CB  . VAL C 1 257 ? 32.413  -6.625  -45.281 1.00 16.20 ? 257 VAL C CB  1 
ATOM   6387 C  CG1 . VAL C 1 257 ? 33.552  -7.061  -44.381 1.00 15.88 ? 257 VAL C CG1 1 
ATOM   6388 C  CG2 . VAL C 1 257 ? 31.661  -5.464  -44.661 1.00 19.66 ? 257 VAL C CG2 1 
ATOM   6389 N  N   . TYR C 1 258 ? 35.013  -7.215  -47.410 1.00 13.48 ? 258 TYR C N   1 
ATOM   6390 C  CA  . TYR C 1 258 ? 35.828  -8.246  -48.051 1.00 14.40 ? 258 TYR C CA  1 
ATOM   6391 C  C   . TYR C 1 258 ? 36.365  -9.203  -46.998 1.00 12.64 ? 258 TYR C C   1 
ATOM   6392 O  O   . TYR C 1 258 ? 36.629  -8.812  -45.853 1.00 14.49 ? 258 TYR C O   1 
ATOM   6393 C  CB  . TYR C 1 258 ? 36.941  -7.560  -48.845 1.00 14.02 ? 258 TYR C CB  1 
ATOM   6394 C  CG  . TYR C 1 258 ? 36.336  -6.704  -49.882 1.00 16.52 ? 258 TYR C CG  1 
ATOM   6395 C  CD1 . TYR C 1 258 ? 35.817  -7.265  -51.065 1.00 16.07 ? 258 TYR C CD1 1 
ATOM   6396 C  CD2 . TYR C 1 258 ? 36.215  -5.327  -49.658 1.00 17.66 ? 258 TYR C CD2 1 
ATOM   6397 C  CE1 . TYR C 1 258 ? 35.173  -6.471  -52.011 1.00 20.46 ? 258 TYR C CE1 1 
ATOM   6398 C  CE2 . TYR C 1 258 ? 35.594  -4.504  -50.609 1.00 21.02 ? 258 TYR C CE2 1 
ATOM   6399 C  CZ  . TYR C 1 258 ? 35.096  -5.066  -51.788 1.00 20.77 ? 258 TYR C CZ  1 
ATOM   6400 O  OH  . TYR C 1 258 ? 34.455  -4.265  -52.741 1.00 23.78 ? 258 TYR C OH  1 
ATOM   6401 N  N   . THR C 1 259 ? 36.435  -10.493 -47.302 1.00 13.44 ? 259 THR C N   1 
ATOM   6402 C  CA  . THR C 1 259 ? 36.894  -11.404 -46.309 1.00 13.79 ? 259 THR C CA  1 
ATOM   6403 C  C   . THR C 1 259 ? 38.151  -12.200 -46.782 1.00 15.19 ? 259 THR C C   1 
ATOM   6404 O  O   . THR C 1 259 ? 38.330  -12.487 -47.970 1.00 14.82 ? 259 THR C O   1 
ATOM   6405 C  CB  . THR C 1 259 ? 35.831  -12.459 -45.940 1.00 13.80 ? 259 THR C CB  1 
ATOM   6406 O  OG1 . THR C 1 259 ? 35.511  -13.176 -47.155 1.00 16.37 ? 259 THR C OG1 1 
ATOM   6407 C  CG2 . THR C 1 259 ? 34.505  -11.725 -45.420 1.00 15.77 ? 259 THR C CG2 1 
ATOM   6408 N  N   . SER C 1 260 ? 38.998  -12.548 -45.828 1.00 16.22 ? 260 SER C N   1 
ATOM   6409 C  CA  . SER C 1 260 ? 40.252  -13.229 -46.205 1.00 17.06 ? 260 SER C CA  1 
ATOM   6410 C  C   . SER C 1 260 ? 39.975  -14.688 -46.203 1.00 18.74 ? 260 SER C C   1 
ATOM   6411 O  O   . SER C 1 260 ? 40.875  -15.490 -46.524 1.00 23.22 ? 260 SER C O   1 
ATOM   6412 C  CB  . SER C 1 260 ? 41.368  -12.932 -45.221 1.00 16.84 ? 260 SER C CB  1 
ATOM   6413 O  OG  . SER C 1 260 ? 40.985  -13.410 -43.944 1.00 16.01 ? 260 SER C OG  1 
ATOM   6414 N  N   . PHE C 1 261 ? 38.762  -15.031 -45.863 1.00 17.17 ? 261 PHE C N   1 
ATOM   6415 C  CA  . PHE C 1 261 ? 38.361  -16.412 -45.730 1.00 20.58 ? 261 PHE C CA  1 
ATOM   6416 C  C   . PHE C 1 261 ? 37.257  -16.672 -46.680 1.00 25.66 ? 261 PHE C C   1 
ATOM   6417 O  O   . PHE C 1 261 ? 36.476  -15.784 -47.004 1.00 24.73 ? 261 PHE C O   1 
ATOM   6418 C  CB  . PHE C 1 261 ? 37.977  -16.758 -44.275 1.00 19.60 ? 261 PHE C CB  1 
ATOM   6419 C  CG  . PHE C 1 261 ? 36.948  -15.852 -43.679 1.00 18.77 ? 261 PHE C CG  1 
ATOM   6420 C  CD1 . PHE C 1 261 ? 35.607  -16.208 -43.688 1.00 21.13 ? 261 PHE C CD1 1 
ATOM   6421 C  CD2 . PHE C 1 261 ? 37.320  -14.654 -43.114 1.00 18.95 ? 261 PHE C CD2 1 
ATOM   6422 C  CE1 . PHE C 1 261 ? 34.654  -15.385 -43.105 1.00 23.00 ? 261 PHE C CE1 1 
ATOM   6423 C  CE2 . PHE C 1 261 ? 36.371  -13.827 -42.523 1.00 17.37 ? 261 PHE C CE2 1 
ATOM   6424 C  CZ  . PHE C 1 261 ? 35.032  -14.172 -42.545 1.00 19.92 ? 261 PHE C CZ  1 
ATOM   6425 N  N   . SER C 1 262 ? 37.228  -17.884 -47.213 1.00 29.48 ? 262 SER C N   1 
ATOM   6426 C  CA  . SER C 1 262 ? 36.062  -18.256 -47.975 1.00 39.13 ? 262 SER C CA  1 
ATOM   6427 C  C   . SER C 1 262 ? 35.072  -18.941 -47.079 1.00 45.11 ? 262 SER C C   1 
ATOM   6428 O  O   . SER C 1 262 ? 33.880  -18.591 -46.999 1.00 51.32 ? 262 SER C O   1 
ATOM   6429 C  CB  . SER C 1 262 ? 36.406  -19.227 -49.071 1.00 42.84 ? 262 SER C CB  1 
ATOM   6430 O  OG  . SER C 1 262 ? 35.183  -19.858 -49.420 1.00 41.66 ? 262 SER C OG  1 
ATOM   6431 N  N   . GLN C 1 263 ? 35.584  -19.964 -46.433 1.00 43.35 ? 263 GLN C N   1 
ATOM   6432 C  CA  . GLN C 1 263 ? 34.771  -20.823 -45.616 1.00 45.41 ? 263 GLN C CA  1 
ATOM   6433 C  C   . GLN C 1 263 ? 34.855  -20.376 -44.154 1.00 44.83 ? 263 GLN C C   1 
ATOM   6434 O  O   . GLN C 1 263 ? 34.178  -20.943 -43.291 1.00 54.21 ? 263 GLN C O   1 
ATOM   6435 C  CB  . GLN C 1 263 ? 35.222  -22.279 -45.823 1.00 40.96 ? 263 GLN C CB  1 
ATOM   6436 C  CG  . GLN C 1 263 ? 36.668  -22.550 -45.445 1.00 41.49 ? 263 GLN C CG  1 
ATOM   6437 C  CD  . GLN C 1 263 ? 37.172  -23.915 -45.878 1.00 35.93 ? 263 GLN C CD  1 
ATOM   6438 O  OE1 . GLN C 1 263 ? 38.347  -24.235 -45.671 1.00 37.56 ? 263 GLN C OE1 1 
ATOM   6439 N  NE2 . GLN C 1 263 ? 36.303  -24.719 -46.497 1.00 27.70 ? 263 GLN C NE2 1 
ATOM   6440 N  N   . LYS D 1 3   ? 14.092  19.447  -45.535 1.00 37.99 ? 3   LYS D N   1 
ATOM   6441 C  CA  . LYS D 1 3   ? 14.971  18.809  -46.555 1.00 31.25 ? 3   LYS D CA  1 
ATOM   6442 C  C   . LYS D 1 3   ? 15.688  17.619  -45.920 1.00 27.53 ? 3   LYS D C   1 
ATOM   6443 O  O   . LYS D 1 3   ? 16.565  17.048  -46.569 1.00 23.61 ? 3   LYS D O   1 
ATOM   6444 C  CB  . LYS D 1 3   ? 16.025  19.793  -47.029 1.00 34.52 ? 3   LYS D CB  1 
ATOM   6445 C  CG  . LYS D 1 3   ? 16.873  20.278  -45.906 1.00 36.68 ? 3   LYS D CG  1 
ATOM   6446 C  CD  . LYS D 1 3   ? 18.313  20.019  -46.229 1.00 39.36 ? 3   LYS D CD  1 
ATOM   6447 C  CE  . LYS D 1 3   ? 18.706  20.519  -47.627 1.00 39.56 ? 3   LYS D CE  1 
ATOM   6448 N  NZ  . LYS D 1 3   ? 20.181  20.418  -47.727 1.00 40.95 ? 3   LYS D NZ  1 
ATOM   6449 N  N   . TRP D 1 4   ? 15.332  17.252  -44.662 1.00 19.46 ? 4   TRP D N   1 
ATOM   6450 C  CA  . TRP D 1 4   ? 15.997  16.078  -44.041 1.00 16.04 ? 4   TRP D CA  1 
ATOM   6451 C  C   . TRP D 1 4   ? 15.725  14.851  -44.884 1.00 14.71 ? 4   TRP D C   1 
ATOM   6452 O  O   . TRP D 1 4   ? 14.739  14.841  -45.626 1.00 15.35 ? 4   TRP D O   1 
ATOM   6453 C  CB  . TRP D 1 4   ? 15.524  15.891  -42.581 1.00 15.45 ? 4   TRP D CB  1 
ATOM   6454 C  CG  . TRP D 1 4   ? 14.031  15.581  -42.416 1.00 12.85 ? 4   TRP D CG  1 
ATOM   6455 C  CD1 . TRP D 1 4   ? 12.987  16.444  -42.147 1.00 12.98 ? 4   TRP D CD1 1 
ATOM   6456 C  CD2 . TRP D 1 4   ? 13.404  14.227  -42.384 1.00 12.83 ? 4   TRP D CD2 1 
ATOM   6457 N  NE1 . TRP D 1 4   ? 11.802  15.761  -42.045 1.00 13.13 ? 4   TRP D NE1 1 
ATOM   6458 C  CE2 . TRP D 1 4   ? 11.981  14.436  -42.178 1.00 13.09 ? 4   TRP D CE2 1 
ATOM   6459 C  CE3 . TRP D 1 4   ? 13.882  12.910  -42.569 1.00 14.22 ? 4   TRP D CE3 1 
ATOM   6460 C  CZ2 . TRP D 1 4   ? 11.088  13.382  -42.077 1.00 12.24 ? 4   TRP D CZ2 1 
ATOM   6461 C  CZ3 . TRP D 1 4   ? 12.949  11.820  -42.489 1.00 13.02 ? 4   TRP D CZ3 1 
ATOM   6462 C  CH2 . TRP D 1 4   ? 11.604  12.044  -42.233 1.00 12.69 ? 4   TRP D CH2 1 
ATOM   6463 N  N   . THR D 1 5   ? 16.614  13.846  -44.827 1.00 13.96 ? 5   THR D N   1 
ATOM   6464 C  CA  . THR D 1 5   ? 16.478  12.618  -45.649 1.00 13.67 ? 5   THR D CA  1 
ATOM   6465 C  C   . THR D 1 5   ? 16.958  11.440  -44.815 1.00 11.90 ? 5   THR D C   1 
ATOM   6466 O  O   . THR D 1 5   ? 17.303  11.585  -43.606 1.00 11.95 ? 5   THR D O   1 
ATOM   6467 C  CB  . THR D 1 5   ? 17.429  12.606  -46.898 1.00 13.95 ? 5   THR D CB  1 
ATOM   6468 O  OG1 . THR D 1 5   ? 18.765  12.617  -46.398 1.00 15.93 ? 5   THR D OG1 1 
ATOM   6469 C  CG2 . THR D 1 5   ? 17.127  13.872  -47.762 1.00 13.50 ? 5   THR D CG2 1 
ATOM   6470 N  N   . TYR D 1 6   ? 16.949  10.233  -45.427 1.00 12.90 ? 6   TYR D N   1 
ATOM   6471 C  CA  . TYR D 1 6   ? 17.593  9.027   -44.844 1.00 12.32 ? 6   TYR D CA  1 
ATOM   6472 C  C   . TYR D 1 6   ? 18.948  8.661   -45.424 1.00 13.86 ? 6   TYR D C   1 
ATOM   6473 O  O   . TYR D 1 6   ? 19.494  7.602   -45.149 1.00 14.70 ? 6   TYR D O   1 
ATOM   6474 C  CB  . TYR D 1 6   ? 16.661  7.824   -45.050 1.00 12.53 ? 6   TYR D CB  1 
ATOM   6475 C  CG  . TYR D 1 6   ? 15.392  7.899   -44.176 1.00 11.22 ? 6   TYR D CG  1 
ATOM   6476 C  CD1 . TYR D 1 6   ? 15.407  7.381   -42.869 1.00 11.48 ? 6   TYR D CD1 1 
ATOM   6477 C  CD2 . TYR D 1 6   ? 14.217  8.490   -44.658 1.00 11.89 ? 6   TYR D CD2 1 
ATOM   6478 C  CE1 . TYR D 1 6   ? 14.251  7.374   -42.075 1.00 11.33 ? 6   TYR D CE1 1 
ATOM   6479 C  CE2 . TYR D 1 6   ? 13.052  8.550   -43.892 1.00 12.20 ? 6   TYR D CE2 1 
ATOM   6480 C  CZ  . TYR D 1 6   ? 13.073  8.011   -42.618 1.00 10.70 ? 6   TYR D CZ  1 
ATOM   6481 O  OH  . TYR D 1 6   ? 11.900  8.058   -41.892 1.00 12.18 ? 6   TYR D OH  1 
ATOM   6482 N  N   . PHE D 1 7   ? 19.517  9.518   -46.283 1.00 15.25 ? 7   PHE D N   1 
ATOM   6483 C  CA  . PHE D 1 7   ? 20.717  9.148   -47.070 1.00 19.39 ? 7   PHE D CA  1 
ATOM   6484 C  C   . PHE D 1 7   ? 21.455  10.399  -47.459 1.00 16.77 ? 7   PHE D C   1 
ATOM   6485 O  O   . PHE D 1 7   ? 20.874  11.341  -48.068 1.00 17.22 ? 7   PHE D O   1 
ATOM   6486 C  CB  . PHE D 1 7   ? 20.324  8.355   -48.338 1.00 20.41 ? 7   PHE D CB  1 
ATOM   6487 C  CG  . PHE D 1 7   ? 21.485  7.917   -49.189 1.00 25.55 ? 7   PHE D CG  1 
ATOM   6488 C  CD1 . PHE D 1 7   ? 22.276  6.847   -48.800 1.00 26.40 ? 7   PHE D CD1 1 
ATOM   6489 C  CD2 . PHE D 1 7   ? 21.743  8.554   -50.407 1.00 29.08 ? 7   PHE D CD2 1 
ATOM   6490 C  CE1 . PHE D 1 7   ? 23.360  6.427   -49.572 1.00 28.30 ? 7   PHE D CE1 1 
ATOM   6491 C  CE2 . PHE D 1 7   ? 22.806  8.135   -51.207 1.00 32.56 ? 7   PHE D CE2 1 
ATOM   6492 C  CZ  . PHE D 1 7   ? 23.612  7.066   -50.786 1.00 30.70 ? 7   PHE D CZ  1 
ATOM   6493 N  N   . GLY D 1 8   ? 22.737  10.404  -47.095 1.00 16.57 ? 8   GLY D N   1 
ATOM   6494 C  CA  . GLY D 1 8   ? 23.649  11.465  -47.548 1.00 18.87 ? 8   GLY D CA  1 
ATOM   6495 C  C   . GLY D 1 8   ? 23.802  12.495  -46.487 1.00 19.34 ? 8   GLY D C   1 
ATOM   6496 O  O   . GLY D 1 8   ? 23.501  12.257  -45.305 1.00 17.00 ? 8   GLY D O   1 
ATOM   6497 N  N   . PRO D 1 9   ? 24.207  13.707  -46.907 1.00 18.52 ? 9   PRO D N   1 
ATOM   6498 C  CA  . PRO D 1 9   ? 24.571  14.777  -45.985 1.00 20.48 ? 9   PRO D CA  1 
ATOM   6499 C  C   . PRO D 1 9   ? 23.466  15.243  -45.084 1.00 18.45 ? 9   PRO D C   1 
ATOM   6500 O  O   . PRO D 1 9   ? 23.778  15.743  -44.006 1.00 18.39 ? 9   PRO D O   1 
ATOM   6501 C  CB  . PRO D 1 9   ? 25.123  15.886  -46.904 1.00 22.47 ? 9   PRO D CB  1 
ATOM   6502 C  CG  . PRO D 1 9   ? 24.629  15.553  -48.278 1.00 24.05 ? 9   PRO D CG  1 
ATOM   6503 C  CD  . PRO D 1 9   ? 24.464  14.043  -48.325 1.00 20.40 ? 9   PRO D CD  1 
ATOM   6504 N  N   . ASP D 1 10  ? 22.181  15.039  -45.443 1.00 18.42 ? 10  ASP D N   1 
ATOM   6505 C  CA  . ASP D 1 10  ? 21.027  15.450  -44.646 1.00 16.90 ? 10  ASP D CA  1 
ATOM   6506 C  C   . ASP D 1 10  ? 20.338  14.237  -44.002 1.00 13.24 ? 10  ASP D C   1 
ATOM   6507 O  O   . ASP D 1 10  ? 19.249  14.380  -43.483 1.00 14.38 ? 10  ASP D O   1 
ATOM   6508 C  CB  . ASP D 1 10  ? 20.019  16.211  -45.475 1.00 18.04 ? 10  ASP D CB  1 
ATOM   6509 C  CG  . ASP D 1 10  ? 20.597  17.529  -46.023 1.00 22.54 ? 10  ASP D CG  1 
ATOM   6510 O  OD1 . ASP D 1 10  ? 21.252  18.244  -45.224 1.00 24.68 ? 10  ASP D OD1 1 
ATOM   6511 O  OD2 . ASP D 1 10  ? 20.390  17.765  -47.226 1.00 27.60 ? 10  ASP D OD2 1 
ATOM   6512 N  N   . GLY D 1 11  ? 21.052  13.113  -43.929 1.00 11.76 ? 11  GLY D N   1 
ATOM   6513 C  CA  . GLY D 1 11  ? 20.533  11.867  -43.347 1.00 10.78 ? 11  GLY D CA  1 
ATOM   6514 C  C   . GLY D 1 11  ? 20.619  11.907  -41.814 1.00 12.13 ? 11  GLY D C   1 
ATOM   6515 O  O   . GLY D 1 11  ? 20.814  12.966  -41.165 1.00 10.87 ? 11  GLY D O   1 
ATOM   6516 N  N   . GLU D 1 12  ? 20.409  10.770  -41.212 1.00 9.58  ? 12  GLU D N   1 
ATOM   6517 C  CA  . GLU D 1 12  ? 19.954  10.739  -39.825 1.00 9.05  ? 12  GLU D CA  1 
ATOM   6518 C  C   . GLU D 1 12  ? 20.964  11.237  -38.796 1.00 9.85  ? 12  GLU D C   1 
ATOM   6519 O  O   . GLU D 1 12  ? 20.556  11.703  -37.741 1.00 10.86 ? 12  GLU D O   1 
ATOM   6520 C  CB  . GLU D 1 12  ? 19.385  9.323   -39.420 1.00 9.24  ? 12  GLU D CB  1 
ATOM   6521 C  CG  . GLU D 1 12  ? 20.480  8.288   -39.288 1.00 9.60  ? 12  GLU D CG  1 
ATOM   6522 C  CD  . GLU D 1 12  ? 19.862  6.859   -39.347 1.00 10.23 ? 12  GLU D CD  1 
ATOM   6523 O  OE1 . GLU D 1 12  ? 19.567  6.384   -38.219 1.00 10.77 ? 12  GLU D OE1 1 
ATOM   6524 O  OE2 . GLU D 1 12  ? 19.811  6.234   -40.445 1.00 12.19 ? 12  GLU D OE2 1 
ATOM   6525 N  N   . ASN D 1 13  ? 22.266  11.097  -39.081 1.00 10.25 ? 13  ASN D N   1 
ATOM   6526 C  CA  . ASN D 1 13  ? 23.253  11.564  -38.168 1.00 10.43 ? 13  ASN D CA  1 
ATOM   6527 C  C   . ASN D 1 13  ? 23.328  13.084  -38.156 1.00 11.38 ? 13  ASN D C   1 
ATOM   6528 O  O   . ASN D 1 13  ? 23.897  13.615  -37.207 1.00 12.20 ? 13  ASN D O   1 
ATOM   6529 C  CB  . ASN D 1 13  ? 24.643  11.038  -38.519 1.00 11.05 ? 13  ASN D CB  1 
ATOM   6530 C  CG  . ASN D 1 13  ? 24.785  9.549   -38.272 1.00 12.89 ? 13  ASN D CG  1 
ATOM   6531 O  OD1 . ASN D 1 13  ? 23.854  8.899   -37.778 1.00 13.03 ? 13  ASN D OD1 1 
ATOM   6532 N  ND2 . ASN D 1 13  ? 25.976  9.001   -38.593 1.00 13.07 ? 13  ASN D ND2 1 
ATOM   6533 N  N   . SER D 1 14  ? 22.639  13.699  -39.085 1.00 12.06 ? 14  SER D N   1 
ATOM   6534 C  CA  . SER D 1 14  ? 22.569  15.211  -39.165 1.00 10.54 ? 14  SER D CA  1 
ATOM   6535 C  C   . SER D 1 14  ? 21.254  15.803  -38.748 1.00 12.33 ? 14  SER D C   1 
ATOM   6536 O  O   . SER D 1 14  ? 21.131  17.033  -38.665 1.00 11.34 ? 14  SER D O   1 
ATOM   6537 C  CB  . SER D 1 14  ? 22.867  15.658  -40.615 1.00 11.13 ? 14  SER D CB  1 
ATOM   6538 O  OG  . SER D 1 14  ? 24.206  15.298  -40.886 1.00 13.33 ? 14  SER D OG  1 
ATOM   6539 N  N   . TRP D 1 15  ? 20.253  14.998  -38.445 1.00 10.01 ? 15  TRP D N   1 
ATOM   6540 C  CA  . TRP D 1 15  ? 18.943  15.567  -38.090 1.00 10.51 ? 15  TRP D CA  1 
ATOM   6541 C  C   . TRP D 1 15  ? 18.978  16.466  -36.869 1.00 10.78 ? 15  TRP D C   1 
ATOM   6542 O  O   . TRP D 1 15  ? 18.243  17.487  -36.833 1.00 11.74 ? 15  TRP D O   1 
ATOM   6543 C  CB  . TRP D 1 15  ? 17.925  14.455  -37.724 1.00 10.98 ? 15  TRP D CB  1 
ATOM   6544 C  CG  . TRP D 1 15  ? 17.545  13.600  -38.882 1.00 10.38 ? 15  TRP D CG  1 
ATOM   6545 C  CD1 . TRP D 1 15  ? 17.816  13.749  -40.245 1.00 9.65  ? 15  TRP D CD1 1 
ATOM   6546 C  CD2 . TRP D 1 15  ? 16.767  12.312  -38.782 1.00 9.07  ? 15  TRP D CD2 1 
ATOM   6547 N  NE1 . TRP D 1 15  ? 17.263  12.644  -40.979 1.00 10.69 ? 15  TRP D NE1 1 
ATOM   6548 C  CE2 . TRP D 1 15  ? 16.590  11.818  -40.135 1.00 9.70  ? 15  TRP D CE2 1 
ATOM   6549 C  CE3 . TRP D 1 15  ? 16.108  11.668  -37.746 1.00 9.71  ? 15  TRP D CE3 1 
ATOM   6550 C  CZ2 . TRP D 1 15  ? 15.908  10.593  -40.415 1.00 11.10 ? 15  TRP D CZ2 1 
ATOM   6551 C  CZ3 . TRP D 1 15  ? 15.459  10.443  -38.039 1.00 11.27 ? 15  TRP D CZ3 1 
ATOM   6552 C  CH2 . TRP D 1 15  ? 15.292  9.987   -39.347 1.00 10.30 ? 15  TRP D CH2 1 
ATOM   6553 N  N   . SER D 1 16  ? 19.861  16.186  -35.934 1.00 12.34 ? 16  SER D N   1 
ATOM   6554 C  CA  . SER D 1 16  ? 19.924  16.976  -34.660 1.00 12.38 ? 16  SER D CA  1 
ATOM   6555 C  C   . SER D 1 16  ? 20.427  18.419  -34.928 1.00 13.15 ? 16  SER D C   1 
ATOM   6556 O  O   . SER D 1 16  ? 20.238  19.262  -34.073 1.00 13.09 ? 16  SER D O   1 
ATOM   6557 C  CB  . SER D 1 16  ? 20.809  16.286  -33.677 1.00 14.75 ? 16  SER D CB  1 
ATOM   6558 O  OG  . SER D 1 16  ? 22.153  16.334  -34.203 1.00 20.06 ? 16  SER D OG  1 
ATOM   6559 N  N   . LYS D 1 17  ? 21.024  18.660  -36.098 1.00 13.56 ? 17  LYS D N   1 
ATOM   6560 C  CA  . LYS D 1 17  ? 21.523  20.058  -36.413 1.00 13.34 ? 17  LYS D CA  1 
ATOM   6561 C  C   . LYS D 1 17  ? 20.355  21.010  -36.500 1.00 14.02 ? 17  LYS D C   1 
ATOM   6562 O  O   . LYS D 1 17  ? 20.485  22.183  -36.117 1.00 13.41 ? 17  LYS D O   1 
ATOM   6563 C  CB  . LYS D 1 17  ? 22.257  20.087  -37.717 1.00 12.04 ? 17  LYS D CB  1 
ATOM   6564 C  CG  . LYS D 1 17  ? 23.518  19.199  -37.718 1.00 11.52 ? 17  LYS D CG  1 
ATOM   6565 C  CD  . LYS D 1 17  ? 24.071  19.136  -39.174 1.00 11.45 ? 17  LYS D CD  1 
ATOM   6566 C  CE  . LYS D 1 17  ? 25.345  18.304  -39.302 1.00 13.65 ? 17  LYS D CE  1 
ATOM   6567 N  NZ  . LYS D 1 17  ? 25.916  18.438  -40.722 1.00 12.73 ? 17  LYS D NZ  1 
ATOM   6568 N  N   . LYS D 1 18  ? 19.220  20.543  -36.994 1.00 11.94 ? 18  LYS D N   1 
ATOM   6569 C  CA  . LYS D 1 18  ? 18.011  21.296  -37.118 1.00 12.37 ? 18  LYS D CA  1 
ATOM   6570 C  C   . LYS D 1 18  ? 16.896  20.919  -36.114 1.00 12.98 ? 18  LYS D C   1 
ATOM   6571 O  O   . LYS D 1 18  ? 15.962  21.685  -35.942 1.00 15.64 ? 18  LYS D O   1 
ATOM   6572 C  CB  . LYS D 1 18  ? 17.464  21.147  -38.522 1.00 15.30 ? 18  LYS D CB  1 
ATOM   6573 C  CG  . LYS D 1 18  ? 18.304  21.829  -39.623 1.00 21.42 ? 18  LYS D CG  1 
ATOM   6574 C  CD  . LYS D 1 18  ? 17.698  21.576  -41.016 1.00 25.03 ? 18  LYS D CD  1 
ATOM   6575 C  CE  . LYS D 1 18  ? 18.305  22.524  -42.064 1.00 28.14 ? 18  LYS D CE  1 
ATOM   6576 N  NZ  . LYS D 1 18  ? 17.955  22.024  -43.425 1.00 35.68 ? 18  LYS D NZ  1 
ATOM   6577 N  N   . TYR D 1 19  ? 16.932  19.693  -35.597 1.00 12.51 ? 19  TYR D N   1 
ATOM   6578 C  CA  . TYR D 1 19  ? 15.828  19.229  -34.809 1.00 12.65 ? 19  TYR D CA  1 
ATOM   6579 C  C   . TYR D 1 19  ? 16.457  18.713  -33.535 1.00 13.24 ? 19  TYR D C   1 
ATOM   6580 O  O   . TYR D 1 19  ? 16.850  17.560  -33.453 1.00 12.21 ? 19  TYR D O   1 
ATOM   6581 C  CB  . TYR D 1 19  ? 15.093  18.066  -35.565 1.00 10.88 ? 19  TYR D CB  1 
ATOM   6582 C  CG  . TYR D 1 19  ? 14.511  18.469  -36.827 1.00 10.62 ? 19  TYR D CG  1 
ATOM   6583 C  CD1 . TYR D 1 19  ? 13.333  19.242  -36.885 1.00 12.58 ? 19  TYR D CD1 1 
ATOM   6584 C  CD2 . TYR D 1 19  ? 15.194  18.220  -38.000 1.00 11.22 ? 19  TYR D CD2 1 
ATOM   6585 C  CE1 . TYR D 1 19  ? 12.816  19.603  -38.090 1.00 13.38 ? 19  TYR D CE1 1 
ATOM   6586 C  CE2 . TYR D 1 19  ? 14.680  18.615  -39.226 1.00 11.88 ? 19  TYR D CE2 1 
ATOM   6587 C  CZ  . TYR D 1 19  ? 13.519  19.343  -39.239 1.00 13.65 ? 19  TYR D CZ  1 
ATOM   6588 O  OH  . TYR D 1 19  ? 13.070  19.704  -40.524 1.00 18.16 ? 19  TYR D OH  1 
ATOM   6589 N  N   . PRO D 1 20  ? 16.593  19.515  -32.489 1.00 13.70 ? 20  PRO D N   1 
ATOM   6590 C  CA  . PRO D 1 20  ? 17.371  19.162  -31.296 1.00 13.67 ? 20  PRO D CA  1 
ATOM   6591 C  C   . PRO D 1 20  ? 16.927  17.835  -30.587 1.00 12.39 ? 20  PRO D C   1 
ATOM   6592 O  O   . PRO D 1 20  ? 17.767  17.183  -30.009 1.00 13.61 ? 20  PRO D O   1 
ATOM   6593 C  CB  . PRO D 1 20  ? 17.292  20.447  -30.359 1.00 15.23 ? 20  PRO D CB  1 
ATOM   6594 C  CG  . PRO D 1 20  ? 16.448  21.320  -31.093 1.00 15.85 ? 20  PRO D CG  1 
ATOM   6595 C  CD  . PRO D 1 20  ? 16.184  20.942  -32.491 1.00 13.78 ? 20  PRO D CD  1 
ATOM   6596 N  N   . SER D 1 21  ? 15.631  17.553  -30.586 1.00 12.76 ? 21  SER D N   1 
ATOM   6597 C  CA  . SER D 1 21  ? 15.166  16.326  -29.916 1.00 13.19 ? 21  SER D CA  1 
ATOM   6598 C  C   . SER D 1 21  ? 15.716  15.115  -30.578 1.00 12.50 ? 21  SER D C   1 
ATOM   6599 O  O   . SER D 1 21  ? 15.809  14.143  -29.890 1.00 13.66 ? 21  SER D O   1 
ATOM   6600 C  CB  . SER D 1 21  ? 13.654  16.195  -29.829 1.00 13.53 ? 21  SER D CB  1 
ATOM   6601 O  OG  . SER D 1 21  ? 13.157  17.308  -29.065 1.00 16.60 ? 21  SER D OG  1 
ATOM   6602 N  N   . CYS D 1 22  ? 16.175  15.205  -31.839 1.00 11.18 ? 22  CYS D N   1 
ATOM   6603 C  CA  . CYS D 1 22  ? 16.766  14.040  -32.461 1.00 11.30 ? 22  CYS D CA  1 
ATOM   6604 C  C   . CYS D 1 22  ? 18.102  13.709  -31.836 1.00 13.50 ? 22  CYS D C   1 
ATOM   6605 O  O   . CYS D 1 22  ? 18.578  12.609  -32.019 1.00 12.96 ? 22  CYS D O   1 
ATOM   6606 C  CB  . CYS D 1 22  ? 16.912  14.263  -33.967 1.00 12.06 ? 22  CYS D CB  1 
ATOM   6607 S  SG  . CYS D 1 22  ? 15.356  14.531  -34.843 1.00 11.50 ? 22  CYS D SG  1 
ATOM   6608 N  N   . GLY D 1 23  ? 18.729  14.640  -31.113 1.00 14.60 ? 23  GLY D N   1 
ATOM   6609 C  CA  . GLY D 1 23  ? 19.967  14.303  -30.367 1.00 15.59 ? 23  GLY D CA  1 
ATOM   6610 C  C   . GLY D 1 23  ? 19.667  14.282  -28.862 1.00 16.95 ? 23  GLY D C   1 
ATOM   6611 O  O   . GLY D 1 23  ? 20.594  14.323  -28.006 1.00 18.12 ? 23  GLY D O   1 
ATOM   6612 N  N   . GLY D 1 24  ? 18.384  14.246  -28.481 1.00 17.28 ? 24  GLY D N   1 
ATOM   6613 C  CA  . GLY D 1 24  ? 18.022  14.115  -27.056 1.00 19.24 ? 24  GLY D CA  1 
ATOM   6614 C  C   . GLY D 1 24  ? 17.766  12.712  -26.553 1.00 18.74 ? 24  GLY D C   1 
ATOM   6615 O  O   . GLY D 1 24  ? 18.238  11.716  -27.107 1.00 22.29 ? 24  GLY D O   1 
ATOM   6616 N  N   . LEU D 1 25  ? 17.127  12.650  -25.397 1.00 18.00 ? 25  LEU D N   1 
ATOM   6617 C  CA  . LEU D 1 25  ? 16.936  11.380  -24.770 1.00 19.31 ? 25  LEU D CA  1 
ATOM   6618 C  C   . LEU D 1 25  ? 15.708  10.683  -25.356 1.00 16.05 ? 25  LEU D C   1 
ATOM   6619 O  O   . LEU D 1 25  ? 14.855  11.301  -26.074 1.00 15.11 ? 25  LEU D O   1 
ATOM   6620 C  CB  . LEU D 1 25  ? 16.822  11.581  -23.239 1.00 22.68 ? 25  LEU D CB  1 
ATOM   6621 C  CG  . LEU D 1 25  ? 18.137  12.012  -22.553 1.00 23.09 ? 25  LEU D CG  1 
ATOM   6622 C  CD1 . LEU D 1 25  ? 17.948  12.323  -21.069 1.00 22.97 ? 25  LEU D CD1 1 
ATOM   6623 C  CD2 . LEU D 1 25  ? 19.135  10.855  -22.677 1.00 27.63 ? 25  LEU D CD2 1 
ATOM   6624 N  N   . LEU D 1 26  ? 15.636  9.386   -24.984 1.00 14.53 ? 26  LEU D N   1 
ATOM   6625 C  CA  . LEU D 1 26  ? 14.469  8.488   -25.188 1.00 15.24 ? 26  LEU D CA  1 
ATOM   6626 C  C   . LEU D 1 26  ? 14.056  8.363   -26.592 1.00 12.42 ? 26  LEU D C   1 
ATOM   6627 O  O   . LEU D 1 26  ? 12.850  8.461   -26.991 1.00 13.66 ? 26  LEU D O   1 
ATOM   6628 C  CB  . LEU D 1 26  ? 13.327  9.052   -24.367 1.00 20.19 ? 26  LEU D CB  1 
ATOM   6629 C  CG  . LEU D 1 26  ? 13.774  9.299   -22.935 1.00 23.73 ? 26  LEU D CG  1 
ATOM   6630 C  CD1 . LEU D 1 26  ? 12.512  9.629   -22.173 1.00 27.50 ? 26  LEU D CD1 1 
ATOM   6631 C  CD2 . LEU D 1 26  ? 14.490  8.087   -22.346 1.00 22.37 ? 26  LEU D CD2 1 
ATOM   6632 N  N   . GLN D 1 27  ? 15.047  8.174   -27.425 1.00 12.92 ? 27  GLN D N   1 
ATOM   6633 C  CA  . GLN D 1 27  ? 14.732  8.114   -28.891 1.00 10.42 ? 27  GLN D CA  1 
ATOM   6634 C  C   . GLN D 1 27  ? 14.354  6.692   -29.311 1.00 10.62 ? 27  GLN D C   1 
ATOM   6635 O  O   . GLN D 1 27  ? 14.776  5.677   -28.690 1.00 12.54 ? 27  GLN D O   1 
ATOM   6636 C  CB  . GLN D 1 27  ? 15.970  8.510   -29.689 1.00 11.47 ? 27  GLN D CB  1 
ATOM   6637 C  CG  . GLN D 1 27  ? 16.360  9.963   -29.464 1.00 12.32 ? 27  GLN D CG  1 
ATOM   6638 C  CD  . GLN D 1 27  ? 15.344  10.884  -30.081 1.00 10.04 ? 27  GLN D CD  1 
ATOM   6639 O  OE1 . GLN D 1 27  ? 15.325  11.048  -31.340 1.00 10.38 ? 27  GLN D OE1 1 
ATOM   6640 N  NE2 . GLN D 1 27  ? 14.443  11.446  -29.271 1.00 12.31 ? 27  GLN D NE2 1 
ATOM   6641 N  N   . SER D 1 28  ? 13.637  6.628   -30.443 1.00 10.41 ? 28  SER D N   1 
ATOM   6642 C  CA  . SER D 1 28  ? 13.192  5.372   -31.045 1.00 9.97  ? 28  SER D CA  1 
ATOM   6643 C  C   . SER D 1 28  ? 13.739  5.329   -32.499 1.00 10.85 ? 28  SER D C   1 
ATOM   6644 O  O   . SER D 1 28  ? 14.063  6.358   -33.075 1.00 10.31 ? 28  SER D O   1 
ATOM   6645 C  CB  . SER D 1 28  ? 11.664  5.359   -31.106 1.00 9.63  ? 28  SER D CB  1 
ATOM   6646 O  OG  . SER D 1 28  ? 11.134  5.233   -29.804 1.00 11.42 ? 28  SER D OG  1 
ATOM   6647 N  N   . PRO D 1 29  ? 13.843  4.170   -33.106 1.00 9.60  ? 29  PRO D N   1 
ATOM   6648 C  CA  . PRO D 1 29  ? 13.465  2.803   -32.603 1.00 10.04 ? 29  PRO D CA  1 
ATOM   6649 C  C   . PRO D 1 29  ? 14.572  2.202   -31.775 1.00 11.74 ? 29  PRO D C   1 
ATOM   6650 O  O   . PRO D 1 29  ? 15.612  2.829   -31.604 1.00 10.43 ? 29  PRO D O   1 
ATOM   6651 C  CB  . PRO D 1 29  ? 13.221  2.004   -33.916 1.00 10.17 ? 29  PRO D CB  1 
ATOM   6652 C  CG  . PRO D 1 29  ? 14.294  2.590   -34.807 1.00 10.03 ? 29  PRO D CG  1 
ATOM   6653 C  CD  . PRO D 1 29  ? 14.343  4.104   -34.514 1.00 11.14 ? 29  PRO D CD  1 
ATOM   6654 N  N   . ILE D 1 30  ? 14.346  0.985   -31.266 1.00 10.29 ? 30  ILE D N   1 
ATOM   6655 C  CA  . ILE D 1 30  ? 15.320  0.269   -30.476 1.00 11.20 ? 30  ILE D CA  1 
ATOM   6656 C  C   . ILE D 1 30  ? 15.301  -1.199  -30.842 1.00 10.14 ? 30  ILE D C   1 
ATOM   6657 O  O   . ILE D 1 30  ? 14.412  -1.671  -31.534 1.00 11.50 ? 30  ILE D O   1 
ATOM   6658 C  CB  . ILE D 1 30  ? 14.968  0.424   -28.961 1.00 12.24 ? 30  ILE D CB  1 
ATOM   6659 C  CG1 . ILE D 1 30  ? 13.501  0.013   -28.715 1.00 12.58 ? 30  ILE D CG1 1 
ATOM   6660 C  CG2 . ILE D 1 30  ? 15.255  1.893   -28.504 1.00 11.60 ? 30  ILE D CG2 1 
ATOM   6661 C  CD1 . ILE D 1 30  ? 13.222  -0.055  -27.217 1.00 13.81 ? 30  ILE D CD1 1 
ATOM   6662 N  N   . ASP D 1 31  ? 16.358  -1.916  -30.445 1.00 10.98 ? 31  ASP D N   1 
ATOM   6663 C  CA  . ASP D 1 31  ? 16.398  -3.375  -30.626 1.00 12.23 ? 31  ASP D CA  1 
ATOM   6664 C  C   . ASP D 1 31  ? 15.820  -4.025  -29.436 1.00 14.65 ? 31  ASP D C   1 
ATOM   6665 O  O   . ASP D 1 31  ? 16.245  -3.800  -28.285 1.00 13.94 ? 31  ASP D O   1 
ATOM   6666 C  CB  . ASP D 1 31  ? 17.853  -3.806  -30.762 1.00 12.95 ? 31  ASP D CB  1 
ATOM   6667 C  CG  . ASP D 1 31  ? 17.983  -5.304  -30.898 1.00 14.88 ? 31  ASP D CG  1 
ATOM   6668 O  OD1 . ASP D 1 31  ? 17.501  -5.839  -31.866 1.00 13.91 ? 31  ASP D OD1 1 
ATOM   6669 O  OD2 . ASP D 1 31  ? 18.563  -5.920  -30.002 1.00 17.80 ? 31  ASP D OD2 1 
ATOM   6670 N  N   . LEU D 1 32  ? 14.907  -4.929  -29.716 1.00 13.61 ? 32  LEU D N   1 
ATOM   6671 C  CA  . LEU D 1 32  ? 14.177  -5.685  -28.664 1.00 14.81 ? 32  LEU D CA  1 
ATOM   6672 C  C   . LEU D 1 32  ? 14.926  -7.010  -28.418 1.00 15.56 ? 32  LEU D C   1 
ATOM   6673 O  O   . LEU D 1 32  ? 14.880  -7.913  -29.278 1.00 16.26 ? 32  LEU D O   1 
ATOM   6674 C  CB  . LEU D 1 32  ? 12.748  -5.968  -29.163 1.00 14.99 ? 32  LEU D CB  1 
ATOM   6675 C  CG  . LEU D 1 32  ? 11.988  -4.668  -29.554 1.00 15.82 ? 32  LEU D CG  1 
ATOM   6676 C  CD1 . LEU D 1 32  ? 10.716  -5.070  -30.281 1.00 18.01 ? 32  LEU D CD1 1 
ATOM   6677 C  CD2 . LEU D 1 32  ? 11.648  -3.855  -28.297 1.00 19.12 ? 32  LEU D CD2 1 
ATOM   6678 N  N   . HIS D 1 33  ? 15.669  -7.070  -27.282 1.00 14.97 ? 33  HIS D N   1 
ATOM   6679 C  CA  . HIS D 1 33  ? 16.444  -8.252  -26.943 1.00 14.92 ? 33  HIS D CA  1 
ATOM   6680 C  C   . HIS D 1 33  ? 16.363  -8.556  -25.451 1.00 13.90 ? 33  HIS D C   1 
ATOM   6681 O  O   . HIS D 1 33  ? 15.996  -7.700  -24.629 1.00 15.32 ? 33  HIS D O   1 
ATOM   6682 C  CB  . HIS D 1 33  ? 17.909  -8.126  -27.445 1.00 15.25 ? 33  HIS D CB  1 
ATOM   6683 C  CG  . HIS D 1 33  ? 18.674  -7.075  -26.752 1.00 16.44 ? 33  HIS D CG  1 
ATOM   6684 N  ND1 . HIS D 1 33  ? 18.524  -5.738  -27.044 1.00 17.88 ? 33  HIS D ND1 1 
ATOM   6685 C  CD2 . HIS D 1 33  ? 19.566  -7.137  -25.674 1.00 17.08 ? 33  HIS D CD2 1 
ATOM   6686 C  CE1 . HIS D 1 33  ? 19.301  -5.015  -26.222 1.00 22.87 ? 33  HIS D CE1 1 
ATOM   6687 N  NE2 . HIS D 1 33  ? 19.916  -5.853  -25.376 1.00 18.75 ? 33  HIS D NE2 1 
ATOM   6688 N  N   . SER D 1 34  ? 16.615  -9.837  -25.133 1.00 14.96 ? 34  SER D N   1 
ATOM   6689 C  CA  . SER D 1 34  ? 16.221  -10.351 -23.825 1.00 15.67 ? 34  SER D CA  1 
ATOM   6690 C  C   . SER D 1 34  ? 16.713  -9.561  -22.649 1.00 16.16 ? 34  SER D C   1 
ATOM   6691 O  O   . SER D 1 34  ? 15.974  -9.422  -21.664 1.00 17.01 ? 34  SER D O   1 
ATOM   6692 C  CB  . SER D 1 34  ? 16.650  -11.810 -23.711 1.00 19.79 ? 34  SER D CB  1 
ATOM   6693 O  OG  . SER D 1 34  ? 18.036  -11.827 -23.689 1.00 24.63 ? 34  SER D OG  1 
ATOM   6694 N  N   . ASP D 1 35  ? 17.965  -9.071  -22.677 1.00 15.62 ? 35  ASP D N   1 
ATOM   6695 C  CA  . ASP D 1 35  ? 18.521  -8.401  -21.499 1.00 17.11 ? 35  ASP D CA  1 
ATOM   6696 C  C   . ASP D 1 35  ? 17.747  -7.181  -21.039 1.00 17.27 ? 35  ASP D C   1 
ATOM   6697 O  O   . ASP D 1 35  ? 17.773  -6.871  -19.848 1.00 16.89 ? 35  ASP D O   1 
ATOM   6698 C  CB  . ASP D 1 35  ? 19.974  -7.940  -21.770 1.00 19.22 ? 35  ASP D CB  1 
ATOM   6699 C  CG  . ASP D 1 35  ? 20.819  -9.019  -22.395 1.00 22.37 ? 35  ASP D CG  1 
ATOM   6700 O  OD1 . ASP D 1 35  ? 21.751  -9.450  -21.664 1.00 22.08 ? 35  ASP D OD1 1 
ATOM   6701 O  OD2 . ASP D 1 35  ? 20.568  -9.474  -23.579 1.00 22.17 ? 35  ASP D OD2 1 
ATOM   6702 N  N   . ILE D 1 36  ? 16.986  -6.572  -21.953 1.00 16.03 ? 36  ILE D N   1 
ATOM   6703 C  CA  . ILE D 1 36  ? 16.259  -5.354  -21.591 1.00 15.23 ? 36  ILE D CA  1 
ATOM   6704 C  C   . ILE D 1 36  ? 14.787  -5.560  -21.514 1.00 14.90 ? 36  ILE D C   1 
ATOM   6705 O  O   . ILE D 1 36  ? 14.040  -4.529  -21.385 1.00 17.25 ? 36  ILE D O   1 
ATOM   6706 C  CB  . ILE D 1 36  ? 16.671  -4.127  -22.468 1.00 20.24 ? 36  ILE D CB  1 
ATOM   6707 C  CG1 . ILE D 1 36  ? 16.577  -4.446  -23.989 1.00 18.67 ? 36  ILE D CG1 1 
ATOM   6708 C  CG2 . ILE D 1 36  ? 18.086  -3.653  -22.064 1.00 19.89 ? 36  ILE D CG2 1 
ATOM   6709 C  CD1 . ILE D 1 36  ? 15.175  -4.602  -24.526 1.00 19.75 ? 36  ILE D CD1 1 
ATOM   6710 N  N   . LEU D 1 37  ? 14.347  -6.840  -21.580 1.00 14.67 ? 37  LEU D N   1 
ATOM   6711 C  CA  . LEU D 1 37  ? 12.901  -7.118  -21.501 1.00 15.47 ? 37  LEU D CA  1 
ATOM   6712 C  C   . LEU D 1 37  ? 12.459  -7.343  -20.081 1.00 16.04 ? 37  LEU D C   1 
ATOM   6713 O  O   . LEU D 1 37  ? 13.174  -7.968  -19.322 1.00 18.85 ? 37  LEU D O   1 
ATOM   6714 C  CB  . LEU D 1 37  ? 12.471  -8.288  -22.386 1.00 15.03 ? 37  LEU D CB  1 
ATOM   6715 C  CG  . LEU D 1 37  ? 12.753  -8.155  -23.905 1.00 15.46 ? 37  LEU D CG  1 
ATOM   6716 C  CD1 . LEU D 1 37  ? 12.325  -9.371  -24.700 1.00 17.96 ? 37  LEU D CD1 1 
ATOM   6717 C  CD2 . LEU D 1 37  ? 12.129  -6.896  -24.542 1.00 15.60 ? 37  LEU D CD2 1 
ATOM   6718 N  N   . GLN D 1 38  ? 11.299  -6.824  -19.698 1.00 14.29 ? 38  GLN D N   1 
ATOM   6719 C  CA  . GLN D 1 38  ? 10.777  -7.224  -18.375 1.00 15.49 ? 38  GLN D CA  1 
ATOM   6720 C  C   . GLN D 1 38  ? 9.249   -7.379  -18.407 1.00 15.29 ? 38  GLN D C   1 
ATOM   6721 O  O   . GLN D 1 38  ? 8.533   -6.448  -18.803 1.00 15.81 ? 38  GLN D O   1 
ATOM   6722 C  CB  . GLN D 1 38  ? 11.170  -6.227  -17.354 1.00 17.42 ? 38  GLN D CB  1 
ATOM   6723 C  CG  . GLN D 1 38  ? 10.702  -6.580  -15.956 1.00 20.29 ? 38  GLN D CG  1 
ATOM   6724 C  CD  . GLN D 1 38  ? 11.322  -5.636  -14.958 1.00 22.19 ? 38  GLN D CD  1 
ATOM   6725 O  OE1 . GLN D 1 38  ? 12.498  -5.765  -14.644 1.00 28.00 ? 38  GLN D OE1 1 
ATOM   6726 N  NE2 . GLN D 1 38  ? 10.548  -4.649  -14.481 1.00 25.48 ? 38  GLN D NE2 1 
ATOM   6727 N  N   . TYR D 1 39  ? 8.764   -8.527  -17.939 1.00 13.84 ? 39  TYR D N   1 
ATOM   6728 C  CA  . TYR D 1 39  ? 7.336   -8.756  -17.859 1.00 13.27 ? 39  TYR D CA  1 
ATOM   6729 C  C   . TYR D 1 39  ? 6.642   -7.734  -16.906 1.00 12.81 ? 39  TYR D C   1 
ATOM   6730 O  O   . TYR D 1 39  ? 7.170   -7.486  -15.787 1.00 14.97 ? 39  TYR D O   1 
ATOM   6731 C  CB  . TYR D 1 39  ? 7.090   -10.225 -17.401 1.00 12.46 ? 39  TYR D CB  1 
ATOM   6732 C  CG  . TYR D 1 39  ? 5.613   -10.505 -17.151 1.00 13.30 ? 39  TYR D CG  1 
ATOM   6733 C  CD1 . TYR D 1 39  ? 4.712   -10.463 -18.171 1.00 14.38 ? 39  TYR D CD1 1 
ATOM   6734 C  CD2 . TYR D 1 39  ? 5.129   -10.617 -15.833 1.00 13.64 ? 39  TYR D CD2 1 
ATOM   6735 C  CE1 . TYR D 1 39  ? 3.356   -10.665 -17.949 1.00 14.83 ? 39  TYR D CE1 1 
ATOM   6736 C  CE2 . TYR D 1 39  ? 3.774   -10.766 -15.594 1.00 15.05 ? 39  TYR D CE2 1 
ATOM   6737 C  CZ  . TYR D 1 39  ? 2.899   -10.773 -16.608 1.00 15.14 ? 39  TYR D CZ  1 
ATOM   6738 O  OH  . TYR D 1 39  ? 1.533   -10.967 -16.375 1.00 18.20 ? 39  TYR D OH  1 
ATOM   6739 N  N   . ASP D 1 40  ? 5.475   -7.233  -17.342 1.00 13.03 ? 40  ASP D N   1 
ATOM   6740 C  CA  . ASP D 1 40  ? 4.709   -6.285  -16.531 1.00 13.53 ? 40  ASP D CA  1 
ATOM   6741 C  C   . ASP D 1 40  ? 3.254   -6.721  -16.597 1.00 14.95 ? 40  ASP D C   1 
ATOM   6742 O  O   . ASP D 1 40  ? 2.617   -6.660  -17.649 1.00 14.30 ? 40  ASP D O   1 
ATOM   6743 C  CB  . ASP D 1 40  ? 4.922   -4.879  -17.093 1.00 15.40 ? 40  ASP D CB  1 
ATOM   6744 C  CG  . ASP D 1 40  ? 4.191   -3.777  -16.302 1.00 20.36 ? 40  ASP D CG  1 
ATOM   6745 O  OD1 . ASP D 1 40  ? 3.394   -4.037  -15.380 1.00 16.51 ? 40  ASP D OD1 1 
ATOM   6746 O  OD2 . ASP D 1 40  ? 4.492   -2.592  -16.614 1.00 20.04 ? 40  ASP D OD2 1 
ATOM   6747 N  N   . ALA D 1 41  ? 2.752   -7.158  -15.425 1.00 13.86 ? 41  ALA D N   1 
ATOM   6748 C  CA  . ALA D 1 41  ? 1.369   -7.609  -15.380 1.00 13.90 ? 41  ALA D CA  1 
ATOM   6749 C  C   . ALA D 1 41  ? 0.364   -6.433  -15.548 1.00 13.84 ? 41  ALA D C   1 
ATOM   6750 O  O   . ALA D 1 41  ? -0.811  -6.666  -15.773 1.00 14.89 ? 41  ALA D O   1 
ATOM   6751 C  CB  . ALA D 1 41  ? 1.169   -8.294  -14.023 1.00 13.49 ? 41  ALA D CB  1 
ATOM   6752 N  N   . SER D 1 42  ? 0.844   -5.173  -15.529 1.00 13.89 ? 42  SER D N   1 
ATOM   6753 C  CA  . SER D 1 42  ? 0.038   -3.910  -15.754 1.00 16.00 ? 42  SER D CA  1 
ATOM   6754 C  C   . SER D 1 42  ? -0.417  -3.835  -17.193 1.00 16.32 ? 42  SER D C   1 
ATOM   6755 O  O   . SER D 1 42  ? -1.343  -3.055  -17.489 1.00 18.38 ? 42  SER D O   1 
ATOM   6756 C  CB  . SER D 1 42  ? 0.974   -2.663  -15.644 1.00 20.40 ? 42  SER D CB  1 
ATOM   6757 O  OG  . SER D 1 42  ? 1.265   -2.429  -14.279 1.00 27.78 ? 42  SER D OG  1 
ATOM   6758 N  N   . LEU D 1 43  ? 0.286   -4.560  -18.095 1.00 13.85 ? 43  LEU D N   1 
ATOM   6759 C  CA  . LEU D 1 43  ? 0.046   -4.486  -19.532 1.00 15.85 ? 43  LEU D CA  1 
ATOM   6760 C  C   . LEU D 1 43  ? -1.101  -5.386  -20.000 1.00 16.36 ? 43  LEU D C   1 
ATOM   6761 O  O   . LEU D 1 43  ? -0.910  -6.484  -20.506 1.00 16.12 ? 43  LEU D O   1 
ATOM   6762 C  CB  . LEU D 1 43  ? 1.391   -4.745  -20.277 1.00 15.82 ? 43  LEU D CB  1 
ATOM   6763 C  CG  . LEU D 1 43  ? 2.529   -3.817  -19.945 1.00 17.46 ? 43  LEU D CG  1 
ATOM   6764 C  CD1 . LEU D 1 43  ? 3.736   -4.245  -20.780 1.00 18.67 ? 43  LEU D CD1 1 
ATOM   6765 C  CD2 . LEU D 1 43  ? 2.232   -2.328  -20.130 1.00 20.14 ? 43  LEU D CD2 1 
ATOM   6766 N  N   . THR D 1 44  ? -2.326  -4.842  -19.881 1.00 16.94 ? 44  THR D N   1 
ATOM   6767 C  CA  . THR D 1 44  ? -3.538  -5.568  -20.190 1.00 17.65 ? 44  THR D CA  1 
ATOM   6768 C  C   . THR D 1 44  ? -3.873  -5.351  -21.683 1.00 18.25 ? 44  THR D C   1 
ATOM   6769 O  O   . THR D 1 44  ? -3.288  -4.488  -22.313 1.00 18.18 ? 44  THR D O   1 
ATOM   6770 C  CB  . THR D 1 44  ? -4.630  -5.028  -19.215 1.00 19.08 ? 44  THR D CB  1 
ATOM   6771 O  OG1 . THR D 1 44  ? -4.662  -3.615  -19.277 1.00 24.58 ? 44  THR D OG1 1 
ATOM   6772 C  CG2 . THR D 1 44  ? -4.242  -5.343  -17.736 1.00 21.94 ? 44  THR D CG2 1 
ATOM   6773 N  N   . PRO D 1 45  ? -4.852  -6.091  -22.243 1.00 18.18 ? 45  PRO D N   1 
ATOM   6774 C  CA  . PRO D 1 45  ? -5.065  -6.052  -23.690 1.00 18.06 ? 45  PRO D CA  1 
ATOM   6775 C  C   . PRO D 1 45  ? -5.627  -4.704  -24.154 1.00 17.69 ? 45  PRO D C   1 
ATOM   6776 O  O   . PRO D 1 45  ? -6.501  -4.151  -23.492 1.00 18.68 ? 45  PRO D O   1 
ATOM   6777 C  CB  . PRO D 1 45  ? -6.050  -7.217  -23.918 1.00 19.63 ? 45  PRO D CB  1 
ATOM   6778 C  CG  . PRO D 1 45  ? -5.716  -8.133  -22.779 1.00 20.68 ? 45  PRO D CG  1 
ATOM   6779 C  CD  . PRO D 1 45  ? -5.570  -7.227  -21.644 1.00 20.68 ? 45  PRO D CD  1 
ATOM   6780 N  N   . LEU D 1 46  ? -5.128  -4.191  -25.267 1.00 15.87 ? 46  LEU D N   1 
ATOM   6781 C  CA  . LEU D 1 46  ? -5.703  -2.970  -25.819 1.00 16.96 ? 46  LEU D CA  1 
ATOM   6782 C  C   . LEU D 1 46  ? -6.999  -3.354  -26.538 1.00 18.37 ? 46  LEU D C   1 
ATOM   6783 O  O   . LEU D 1 46  ? -7.162  -4.468  -27.065 1.00 18.20 ? 46  LEU D O   1 
ATOM   6784 C  CB  . LEU D 1 46  ? -4.773  -2.358  -26.880 1.00 17.55 ? 46  LEU D CB  1 
ATOM   6785 C  CG  . LEU D 1 46  ? -3.416  -1.802  -26.404 1.00 20.32 ? 46  LEU D CG  1 
ATOM   6786 C  CD1 . LEU D 1 46  ? -2.514  -1.420  -27.605 1.00 21.62 ? 46  LEU D CD1 1 
ATOM   6787 C  CD2 . LEU D 1 46  ? -3.638  -0.577  -25.548 1.00 24.30 ? 46  LEU D CD2 1 
ATOM   6788 N  N   . GLU D 1 47  ? -7.916  -2.374  -26.567 1.00 18.96 ? 47  GLU D N   1 
ATOM   6789 C  CA  . GLU D 1 47  ? -9.106  -2.526  -27.352 1.00 20.99 ? 47  GLU D CA  1 
ATOM   6790 C  C   . GLU D 1 47  ? -9.077  -1.554  -28.549 1.00 17.90 ? 47  GLU D C   1 
ATOM   6791 O  O   . GLU D 1 47  ? -8.758  -0.348  -28.423 1.00 19.27 ? 47  GLU D O   1 
ATOM   6792 C  CB  . GLU D 1 47  ? -10.362 -2.311  -26.515 1.00 28.39 ? 47  GLU D CB  1 
ATOM   6793 C  CG  . GLU D 1 47  ? -10.835 -3.575  -25.806 1.00 35.67 ? 47  GLU D CG  1 
ATOM   6794 C  CD  . GLU D 1 47  ? -11.900 -3.280  -24.750 1.00 45.21 ? 47  GLU D CD  1 
ATOM   6795 O  OE1 . GLU D 1 47  ? -12.073 -2.080  -24.348 1.00 53.22 ? 47  GLU D OE1 1 
ATOM   6796 O  OE2 . GLU D 1 47  ? -12.559 -4.249  -24.337 1.00 45.19 ? 47  GLU D OE2 1 
ATOM   6797 N  N   . PHE D 1 48  ? -9.398  -2.099  -29.683 1.00 16.57 ? 48  PHE D N   1 
ATOM   6798 C  CA  . PHE D 1 48  ? -9.370  -1.304  -30.953 1.00 18.32 ? 48  PHE D CA  1 
ATOM   6799 C  C   . PHE D 1 48  ? -10.768 -0.874  -31.335 1.00 19.82 ? 48  PHE D C   1 
ATOM   6800 O  O   . PHE D 1 48  ? -11.566 -1.730  -31.671 1.00 23.20 ? 48  PHE D O   1 
ATOM   6801 C  CB  . PHE D 1 48  ? -8.652  -2.111  -32.049 1.00 17.90 ? 48  PHE D CB  1 
ATOM   6802 C  CG  . PHE D 1 48  ? -7.351  -2.695  -31.581 1.00 17.85 ? 48  PHE D CG  1 
ATOM   6803 C  CD1 . PHE D 1 48  ? -6.253  -1.886  -31.353 1.00 18.48 ? 48  PHE D CD1 1 
ATOM   6804 C  CD2 . PHE D 1 48  ? -7.232  -4.077  -31.312 1.00 19.40 ? 48  PHE D CD2 1 
ATOM   6805 C  CE1 . PHE D 1 48  ? -5.032  -2.422  -30.860 1.00 17.65 ? 48  PHE D CE1 1 
ATOM   6806 C  CE2 . PHE D 1 48  ? -6.018  -4.613  -30.845 1.00 16.79 ? 48  PHE D CE2 1 
ATOM   6807 C  CZ  . PHE D 1 48  ? -4.913  -3.786  -30.626 1.00 19.18 ? 48  PHE D CZ  1 
ATOM   6808 N  N   . GLN D 1 49  ? -11.098 0.418   -31.182 1.00 15.96 ? 49  GLN D N   1 
ATOM   6809 C  CA  . GLN D 1 49  ? -12.513 0.884   -31.388 1.00 19.68 ? 49  GLN D CA  1 
ATOM   6810 C  C   . GLN D 1 49  ? -12.606 1.685   -32.695 1.00 17.59 ? 49  GLN D C   1 
ATOM   6811 O  O   . GLN D 1 49  ? -11.766 2.556   -32.936 1.00 16.88 ? 49  GLN D O   1 
ATOM   6812 C  CB  . GLN D 1 49  ? -12.993 1.706   -30.195 1.00 22.78 ? 49  GLN D CB  1 
ATOM   6813 C  CG  . GLN D 1 49  ? -12.684 1.120   -28.790 1.00 31.03 ? 49  GLN D CG  1 
ATOM   6814 C  CD  . GLN D 1 49  ? -13.303 -0.271  -28.425 1.00 37.84 ? 49  GLN D CD  1 
ATOM   6815 O  OE1 . GLN D 1 49  ? -13.540 -0.569  -27.225 1.00 44.18 ? 49  GLN D OE1 1 
ATOM   6816 N  NE2 . GLN D 1 49  ? -13.540 -1.120  -29.415 1.00 37.24 ? 49  GLN D NE2 1 
ATOM   6817 N  N   . GLY D 1 50  ? -13.628 1.386   -33.504 1.00 16.72 ? 50  GLY D N   1 
ATOM   6818 C  CA  . GLY D 1 50  ? -13.898 2.063   -34.739 1.00 18.22 ? 50  GLY D CA  1 
ATOM   6819 C  C   . GLY D 1 50  ? -12.821 1.873   -35.793 1.00 15.54 ? 50  GLY D C   1 
ATOM   6820 O  O   . GLY D 1 50  ? -12.641 2.811   -36.642 1.00 14.00 ? 50  GLY D O   1 
ATOM   6821 N  N   . TYR D 1 51  ? -12.085 0.735   -35.668 1.00 16.22 ? 51  TYR D N   1 
ATOM   6822 C  CA  . TYR D 1 51  ? -11.093 0.346   -36.713 1.00 14.27 ? 51  TYR D CA  1 
ATOM   6823 C  C   . TYR D 1 51  ? -11.752 -0.115  -37.946 1.00 13.51 ? 51  TYR D C   1 
ATOM   6824 O  O   . TYR D 1 51  ? -11.171 -0.130  -39.033 1.00 12.65 ? 51  TYR D O   1 
ATOM   6825 C  CB  . TYR D 1 51  ? -10.140 -0.726  -36.148 1.00 13.95 ? 51  TYR D CB  1 
ATOM   6826 C  CG  . TYR D 1 51  ? -8.936  -0.126  -35.429 1.00 13.54 ? 51  TYR D CG  1 
ATOM   6827 C  CD1 . TYR D 1 51  ? -7.669  -0.627  -35.730 1.00 12.74 ? 51  TYR D CD1 1 
ATOM   6828 C  CD2 . TYR D 1 51  ? -9.044  0.909   -34.468 1.00 13.08 ? 51  TYR D CD2 1 
ATOM   6829 C  CE1 . TYR D 1 51  ? -6.554  -0.136  -35.117 1.00 14.03 ? 51  TYR D CE1 1 
ATOM   6830 C  CE2 . TYR D 1 51  ? -7.919  1.415   -33.849 1.00 13.62 ? 51  TYR D CE2 1 
ATOM   6831 C  CZ  . TYR D 1 51  ? -6.667  0.900   -34.195 1.00 12.80 ? 51  TYR D CZ  1 
ATOM   6832 O  OH  . TYR D 1 51  ? -5.546  1.429   -33.613 1.00 14.14 ? 51  TYR D OH  1 
ATOM   6833 N  N   . ASN D 1 52  ? -13.061 -0.470  -37.835 1.00 15.97 ? 52  ASN D N   1 
ATOM   6834 C  CA  . ASN D 1 52  ? -13.710 -0.992  -39.007 1.00 16.70 ? 52  ASN D CA  1 
ATOM   6835 C  C   . ASN D 1 52  ? -14.269 0.130   -39.864 1.00 17.71 ? 52  ASN D C   1 
ATOM   6836 O  O   . ASN D 1 52  ? -15.449 0.564   -39.729 1.00 18.59 ? 52  ASN D O   1 
ATOM   6837 C  CB  . ASN D 1 52  ? -14.782 -2.023  -38.603 1.00 19.47 ? 52  ASN D CB  1 
ATOM   6838 C  CG  . ASN D 1 52  ? -15.312 -2.787  -39.771 1.00 20.56 ? 52  ASN D CG  1 
ATOM   6839 O  OD1 . ASN D 1 52  ? -15.166 -2.365  -40.903 1.00 23.07 ? 52  ASN D OD1 1 
ATOM   6840 N  ND2 . ASN D 1 52  ? -16.031 -3.893  -39.487 1.00 25.06 ? 52  ASN D ND2 1 
ATOM   6841 N  N   . LEU D 1 53  ? -13.470 0.593   -40.808 1.00 15.19 ? 53  LEU D N   1 
ATOM   6842 C  CA  . LEU D 1 53  ? -13.906 1.740   -41.584 1.00 15.60 ? 53  LEU D CA  1 
ATOM   6843 C  C   . LEU D 1 53  ? -14.860 1.336   -42.740 1.00 17.49 ? 53  LEU D C   1 
ATOM   6844 O  O   . LEU D 1 53  ? -14.682 0.337   -43.384 1.00 17.18 ? 53  LEU D O   1 
ATOM   6845 C  CB  . LEU D 1 53  ? -12.696 2.458   -42.167 1.00 16.35 ? 53  LEU D CB  1 
ATOM   6846 C  CG  . LEU D 1 53  ? -11.611 2.795   -41.122 1.00 17.16 ? 53  LEU D CG  1 
ATOM   6847 C  CD1 . LEU D 1 53  ? -10.479 3.511   -41.881 1.00 18.12 ? 53  LEU D CD1 1 
ATOM   6848 C  CD2 . LEU D 1 53  ? -12.114 3.839   -40.138 1.00 19.74 ? 53  LEU D CD2 1 
ATOM   6849 N  N   . SER D 1 54  ? -15.838 2.170   -42.999 1.00 15.44 ? 54  SER D N   1 
ATOM   6850 C  CA  . SER D 1 54  ? -16.836 1.772   -43.994 1.00 18.27 ? 54  SER D CA  1 
ATOM   6851 C  C   . SER D 1 54  ? -16.295 1.824   -45.420 1.00 18.89 ? 54  SER D C   1 
ATOM   6852 O  O   . SER D 1 54  ? -15.688 2.835   -45.813 1.00 16.87 ? 54  SER D O   1 
ATOM   6853 C  CB  . SER D 1 54  ? -18.015 2.748   -43.980 1.00 19.10 ? 54  SER D CB  1 
ATOM   6854 O  OG  . SER D 1 54  ? -18.964 2.395   -45.020 1.00 20.01 ? 54  SER D OG  1 
ATOM   6855 N  N   . ALA D 1 55  ? -16.599 0.777   -46.163 1.00 18.90 ? 55  ALA D N   1 
ATOM   6856 C  CA  . ALA D 1 55  ? -16.329 0.705   -47.638 1.00 19.26 ? 55  ALA D CA  1 
ATOM   6857 C  C   . ALA D 1 55  ? -16.900 1.829   -48.496 1.00 20.75 ? 55  ALA D C   1 
ATOM   6858 O  O   . ALA D 1 55  ? -16.461 2.073   -49.643 1.00 21.17 ? 55  ALA D O   1 
ATOM   6859 C  CB  . ALA D 1 55  ? -16.862 -0.637  -48.183 1.00 22.27 ? 55  ALA D CB  1 
ATOM   6860 N  N   . ASN D 1 56  ? -17.924 2.495   -48.012 1.00 20.33 ? 56  ASN D N   1 
ATOM   6861 C  CA  . ASN D 1 56  ? -18.557 3.570   -48.717 1.00 22.06 ? 56  ASN D CA  1 
ATOM   6862 C  C   . ASN D 1 56  ? -17.967 4.916   -48.342 1.00 20.43 ? 56  ASN D C   1 
ATOM   6863 O  O   . ASN D 1 56  ? -18.331 5.960   -48.914 1.00 21.79 ? 56  ASN D O   1 
ATOM   6864 C  CB  . ASN D 1 56  ? -20.086 3.636   -48.393 1.00 23.19 ? 56  ASN D CB  1 
ATOM   6865 C  CG  . ASN D 1 56  ? -20.905 2.565   -49.091 1.00 31.07 ? 56  ASN D CG  1 
ATOM   6866 O  OD1 . ASN D 1 56  ? -20.370 1.652   -49.771 1.00 31.46 ? 56  ASN D OD1 1 
ATOM   6867 N  ND2 . ASN D 1 56  ? -22.244 2.644   -48.889 1.00 32.18 ? 56  ASN D ND2 1 
ATOM   6868 N  N   . LYS D 1 57  ? -17.021 4.906   -47.398 1.00 16.59 ? 57  LYS D N   1 
ATOM   6869 C  CA  . LYS D 1 57  ? -16.297 6.122   -47.138 1.00 15.45 ? 57  LYS D CA  1 
ATOM   6870 C  C   . LYS D 1 57  ? -14.921 5.975   -47.742 1.00 16.58 ? 57  LYS D C   1 
ATOM   6871 O  O   . LYS D 1 57  ? -14.517 4.850   -48.154 1.00 16.17 ? 57  LYS D O   1 
ATOM   6872 C  CB  . LYS D 1 57  ? -16.153 6.283   -45.621 1.00 17.12 ? 57  LYS D CB  1 
ATOM   6873 C  CG  . LYS D 1 57  ? -17.482 6.686   -44.978 1.00 21.14 ? 57  LYS D CG  1 
ATOM   6874 C  CD  . LYS D 1 57  ? -17.342 6.965   -43.483 1.00 26.01 ? 57  LYS D CD  1 
ATOM   6875 C  CE  . LYS D 1 57  ? -18.421 7.946   -43.002 1.00 28.84 ? 57  LYS D CE  1 
ATOM   6876 N  NZ  . LYS D 1 57  ? -18.391 8.067   -41.509 1.00 34.01 ? 57  LYS D NZ  1 
ATOM   6877 N  N   . GLN D 1 58  ? -14.211 7.080   -47.805 1.00 16.96 ? 58  GLN D N   1 
ATOM   6878 C  CA  . GLN D 1 58  ? -12.860 6.988   -48.386 1.00 18.59 ? 58  GLN D CA  1 
ATOM   6879 C  C   . GLN D 1 58  ? -11.868 7.867   -47.573 1.00 16.35 ? 58  GLN D C   1 
ATOM   6880 O  O   . GLN D 1 58  ? -12.259 8.787   -46.846 1.00 17.07 ? 58  GLN D O   1 
ATOM   6881 C  CB  . GLN D 1 58  ? -12.906 7.300   -49.892 1.00 21.76 ? 58  GLN D CB  1 
ATOM   6882 C  CG  . GLN D 1 58  ? -13.277 8.744   -50.171 1.00 25.41 ? 58  GLN D CG  1 
ATOM   6883 C  CD  . GLN D 1 58  ? -13.408 9.074   -51.669 1.00 28.69 ? 58  GLN D CD  1 
ATOM   6884 O  OE1 . GLN D 1 58  ? -13.226 8.214   -52.564 1.00 27.45 ? 58  GLN D OE1 1 
ATOM   6885 N  NE2 . GLN D 1 58  ? -13.661 10.359  -51.939 1.00 28.81 ? 58  GLN D NE2 1 
ATOM   6886 N  N   . PHE D 1 59  ? -10.576 7.541   -47.658 1.00 14.61 ? 59  PHE D N   1 
ATOM   6887 C  CA  . PHE D 1 59  ? -9.563  8.093   -46.748 1.00 14.91 ? 59  PHE D CA  1 
ATOM   6888 C  C   . PHE D 1 59  ? -8.383  8.473   -47.574 1.00 14.23 ? 59  PHE D C   1 
ATOM   6889 O  O   . PHE D 1 59  ? -8.043  7.770   -48.477 1.00 15.22 ? 59  PHE D O   1 
ATOM   6890 C  CB  . PHE D 1 59  ? -9.223  7.096   -45.605 1.00 16.15 ? 59  PHE D CB  1 
ATOM   6891 C  CG  . PHE D 1 59  ? -10.466 6.718   -44.811 1.00 14.80 ? 59  PHE D CG  1 
ATOM   6892 C  CD1 . PHE D 1 59  ? -11.352 5.720   -45.279 1.00 14.34 ? 59  PHE D CD1 1 
ATOM   6893 C  CD2 . PHE D 1 59  ? -10.804 7.436   -43.688 1.00 13.75 ? 59  PHE D CD2 1 
ATOM   6894 C  CE1 . PHE D 1 59  ? -12.558 5.460   -44.589 1.00 15.01 ? 59  PHE D CE1 1 
ATOM   6895 C  CE2 . PHE D 1 59  ? -11.967 7.191   -42.990 1.00 13.82 ? 59  PHE D CE2 1 
ATOM   6896 C  CZ  . PHE D 1 59  ? -12.861 6.205   -43.441 1.00 15.40 ? 59  PHE D CZ  1 
ATOM   6897 N  N   . LEU D 1 60  ? -7.831  9.646   -47.256 1.00 14.35 ? 60  LEU D N   1 
ATOM   6898 C  CA  . LEU D 1 60  ? -6.768  10.221  -48.022 1.00 15.74 ? 60  LEU D CA  1 
ATOM   6899 C  C   . LEU D 1 60  ? -5.412  9.544   -47.820 1.00 15.67 ? 60  LEU D C   1 
ATOM   6900 O  O   . LEU D 1 60  ? -4.878  9.545   -46.710 1.00 16.41 ? 60  LEU D O   1 
ATOM   6901 C  CB  . LEU D 1 60  ? -6.704  11.712  -47.656 1.00 17.27 ? 60  LEU D CB  1 
ATOM   6902 C  CG  . LEU D 1 60  ? -5.980  12.517  -48.722 1.00 21.01 ? 60  LEU D CG  1 
ATOM   6903 C  CD1 . LEU D 1 60  ? -6.639  12.447  -50.111 1.00 22.93 ? 60  LEU D CD1 1 
ATOM   6904 C  CD2 . LEU D 1 60  ? -5.850  13.926  -48.107 1.00 21.86 ? 60  LEU D CD2 1 
ATOM   6905 N  N   . LEU D 1 61  ? -4.842  9.079   -48.942 1.00 14.00 ? 61  LEU D N   1 
ATOM   6906 C  CA  . LEU D 1 61  ? -3.431  8.615   -49.023 1.00 14.60 ? 61  LEU D CA  1 
ATOM   6907 C  C   . LEU D 1 61  ? -2.581  9.760   -49.629 1.00 17.68 ? 61  LEU D C   1 
ATOM   6908 O  O   . LEU D 1 61  ? -2.904  10.299  -50.715 1.00 16.69 ? 61  LEU D O   1 
ATOM   6909 C  CB  . LEU D 1 61  ? -3.367  7.342   -49.845 1.00 15.76 ? 61  LEU D CB  1 
ATOM   6910 C  CG  . LEU D 1 61  ? -2.114  6.464   -49.797 1.00 15.15 ? 61  LEU D CG  1 
ATOM   6911 C  CD1 . LEU D 1 61  ? -1.954  5.694   -48.470 1.00 14.06 ? 61  LEU D CD1 1 
ATOM   6912 C  CD2 . LEU D 1 61  ? -2.112  5.496   -51.010 1.00 17.53 ? 61  LEU D CD2 1 
ATOM   6913 N  N   . THR D 1 62  ? -1.442  10.068  -48.975 1.00 18.60 ? 62  THR D N   1 
ATOM   6914 C  CA  . THR D 1 62  ? -0.626  11.217  -49.339 1.00 17.57 ? 62  THR D CA  1 
ATOM   6915 C  C   . THR D 1 62  ? 0.848   10.749  -49.340 1.00 16.07 ? 62  THR D C   1 
ATOM   6916 O  O   . THR D 1 62  ? 1.285   10.087  -48.421 1.00 16.40 ? 62  THR D O   1 
ATOM   6917 C  CB  . THR D 1 62  ? -0.760  12.357  -48.356 1.00 20.02 ? 62  THR D CB  1 
ATOM   6918 O  OG1 . THR D 1 62  ? -2.119  12.841  -48.309 1.00 25.37 ? 62  THR D OG1 1 
ATOM   6919 C  CG2 . THR D 1 62  ? 0.112   13.563  -48.718 1.00 21.74 ? 62  THR D CG2 1 
ATOM   6920 N  N   . ASN D 1 63  ? 1.594   11.140  -50.371 1.00 16.31 ? 63  ASN D N   1 
ATOM   6921 C  CA  . ASN D 1 63  ? 3.063   11.028  -50.333 1.00 16.71 ? 63  ASN D CA  1 
ATOM   6922 C  C   . ASN D 1 63  ? 3.540   12.408  -49.877 1.00 16.82 ? 63  ASN D C   1 
ATOM   6923 O  O   . ASN D 1 63  ? 3.375   13.424  -50.571 1.00 17.41 ? 63  ASN D O   1 
ATOM   6924 C  CB  . ASN D 1 63  ? 3.532   10.707  -51.768 1.00 18.09 ? 63  ASN D CB  1 
ATOM   6925 C  CG  . ASN D 1 63  ? 5.044   10.735  -51.886 1.00 18.57 ? 63  ASN D CG  1 
ATOM   6926 O  OD1 . ASN D 1 63  ? 5.696   11.378  -51.060 1.00 16.07 ? 63  ASN D OD1 1 
ATOM   6927 N  ND2 . ASN D 1 63  ? 5.601   10.010  -52.845 1.00 16.72 ? 63  ASN D ND2 1 
ATOM   6928 N  N   . ASN D 1 64  ? 4.183   12.457  -48.704 1.00 16.82 ? 64  ASN D N   1 
ATOM   6929 C  CA  . ASN D 1 64  ? 4.637   13.741  -48.160 1.00 18.57 ? 64  ASN D CA  1 
ATOM   6930 C  C   . ASN D 1 64  ? 6.106   13.991  -48.361 1.00 16.92 ? 64  ASN D C   1 
ATOM   6931 O  O   . ASN D 1 64  ? 6.701   14.990  -47.815 1.00 21.43 ? 64  ASN D O   1 
ATOM   6932 C  CB  . ASN D 1 64  ? 4.297   13.918  -46.697 1.00 20.93 ? 64  ASN D CB  1 
ATOM   6933 C  CG  . ASN D 1 64  ? 5.059   12.998  -45.767 1.00 23.27 ? 64  ASN D CG  1 
ATOM   6934 O  OD1 . ASN D 1 64  ? 5.947   12.222  -46.155 1.00 23.59 ? 64  ASN D OD1 1 
ATOM   6935 N  ND2 . ASN D 1 64  ? 4.590   12.977  -44.496 1.00 27.45 ? 64  ASN D ND2 1 
ATOM   6936 N  N   . GLY D 1 65  ? 6.659   13.166  -49.231 1.00 16.60 ? 65  GLY D N   1 
ATOM   6937 C  CA  . GLY D 1 65  ? 8.053   13.250  -49.598 1.00 17.47 ? 65  GLY D CA  1 
ATOM   6938 C  C   . GLY D 1 65  ? 8.991   12.597  -48.608 1.00 16.99 ? 65  GLY D C   1 
ATOM   6939 O  O   . GLY D 1 65  ? 10.194  12.538  -48.854 1.00 17.80 ? 65  GLY D O   1 
ATOM   6940 N  N   . HIS D 1 66  ? 8.492   12.168  -47.442 1.00 20.24 ? 66  HIS D N   1 
ATOM   6941 C  CA  . HIS D 1 66  ? 9.264   11.331  -46.499 1.00 18.81 ? 66  HIS D CA  1 
ATOM   6942 C  C   . HIS D 1 66  ? 8.662   9.990   -46.287 1.00 21.14 ? 66  HIS D C   1 
ATOM   6943 O  O   . HIS D 1 66  ? 9.324   9.048   -45.909 1.00 20.66 ? 66  HIS D O   1 
ATOM   6944 C  CB  . HIS D 1 66  ? 9.364   12.073  -45.163 1.00 17.47 ? 66  HIS D CB  1 
ATOM   6945 C  CG  . HIS D 1 66  ? 10.094  13.377  -45.242 1.00 16.01 ? 66  HIS D CG  1 
ATOM   6946 N  ND1 . HIS D 1 66  ? 11.434  13.447  -45.430 1.00 15.27 ? 66  HIS D ND1 1 
ATOM   6947 C  CD2 . HIS D 1 66  ? 9.649   14.653  -45.110 1.00 16.62 ? 66  HIS D CD2 1 
ATOM   6948 C  CE1 . HIS D 1 66  ? 11.801  14.748  -45.423 1.00 17.04 ? 66  HIS D CE1 1 
ATOM   6949 N  NE2 . HIS D 1 66  ? 10.677  15.476  -45.251 1.00 19.59 ? 66  HIS D NE2 1 
ATOM   6950 N  N   . SER D 1 67  ? 7.335   9.893   -46.491 1.00 21.91 ? 67  SER D N   1 
ATOM   6951 C  CA  . SER D 1 67  ? 6.575   8.704   -46.180 1.00 22.74 ? 67  SER D CA  1 
ATOM   6952 C  C   . SER D 1 67  ? 5.339   8.601   -47.102 1.00 21.26 ? 67  SER D C   1 
ATOM   6953 O  O   . SER D 1 67  ? 4.977   9.618   -47.697 1.00 25.13 ? 67  SER D O   1 
ATOM   6954 C  CB  . SER D 1 67  ? 6.007   8.918   -44.760 1.00 26.12 ? 67  SER D CB  1 
ATOM   6955 O  OG  . SER D 1 67  ? 5.556   7.680   -44.236 1.00 26.20 ? 67  SER D OG  1 
ATOM   6956 N  N   . VAL D 1 68  ? 4.664   7.433   -47.111 1.00 18.47 ? 68  VAL D N   1 
ATOM   6957 C  CA  . VAL D 1 68  ? 3.249   7.392   -47.655 1.00 17.41 ? 68  VAL D CA  1 
ATOM   6958 C  C   . VAL D 1 68  ? 2.309   7.229   -46.435 1.00 14.09 ? 68  VAL D C   1 
ATOM   6959 O  O   . VAL D 1 68  ? 2.492   6.334   -45.655 1.00 15.42 ? 68  VAL D O   1 
ATOM   6960 C  CB  . VAL D 1 68  ? 3.045   6.311   -48.764 1.00 18.59 ? 68  VAL D CB  1 
ATOM   6961 C  CG1 . VAL D 1 68  ? 3.217   4.832   -48.257 1.00 19.19 ? 68  VAL D CG1 1 
ATOM   6962 C  CG2 . VAL D 1 68  ? 1.675   6.471   -49.336 1.00 20.49 ? 68  VAL D CG2 1 
ATOM   6963 N  N   . LYS D 1 69  ? 1.343   8.120   -46.270 1.00 14.01 ? 69  LYS D N   1 
ATOM   6964 C  CA  . LYS D 1 69  ? 0.468   8.083   -45.087 1.00 13.83 ? 69  LYS D CA  1 
ATOM   6965 C  C   . LYS D 1 69  ? -1.001  7.996   -45.489 1.00 13.03 ? 69  LYS D C   1 
ATOM   6966 O  O   . LYS D 1 69  ? -1.367  8.504   -46.519 1.00 15.06 ? 69  LYS D O   1 
ATOM   6967 C  CB  . LYS D 1 69  ? 0.714   9.223   -44.105 1.00 15.33 ? 69  LYS D CB  1 
ATOM   6968 C  CG  . LYS D 1 69  ? 0.118   10.527  -44.542 1.00 18.99 ? 69  LYS D CG  1 
ATOM   6969 C  CD  . LYS D 1 69  ? 0.428   11.660  -43.611 1.00 24.22 ? 69  LYS D CD  1 
ATOM   6970 C  CE  . LYS D 1 69  ? -0.252  12.865  -44.215 1.00 25.10 ? 69  LYS D CE  1 
ATOM   6971 N  NZ  . LYS D 1 69  ? 0.154   14.081  -43.433 1.00 31.06 ? 69  LYS D NZ  1 
ATOM   6972 N  N   . LEU D 1 70  ? -1.764  7.256   -44.716 1.00 10.78 ? 70  LEU D N   1 
ATOM   6973 C  CA  . LEU D 1 70  ? -3.196  7.188   -44.904 1.00 10.39 ? 70  LEU D CA  1 
ATOM   6974 C  C   . LEU D 1 70  ? -3.849  7.910   -43.722 1.00 10.31 ? 70  LEU D C   1 
ATOM   6975 O  O   . LEU D 1 70  ? -3.584  7.543   -42.573 1.00 10.60 ? 70  LEU D O   1 
ATOM   6976 C  CB  . LEU D 1 70  ? -3.631  5.658   -44.904 1.00 11.14 ? 70  LEU D CB  1 
ATOM   6977 C  CG  . LEU D 1 70  ? -5.149  5.499   -45.080 1.00 11.83 ? 70  LEU D CG  1 
ATOM   6978 C  CD1 . LEU D 1 70  ? -5.579  6.007   -46.509 1.00 14.72 ? 70  LEU D CD1 1 
ATOM   6979 C  CD2 . LEU D 1 70  ? -5.499  4.004   -45.002 1.00 14.60 ? 70  LEU D CD2 1 
ATOM   6980 N  N   . ASN D 1 71  ? -4.643  8.970   -44.007 1.00 12.50 ? 71  ASN D N   1 
ATOM   6981 C  CA  . ASN D 1 71  ? -5.362  9.627   -42.927 1.00 13.87 ? 71  ASN D CA  1 
ATOM   6982 C  C   . ASN D 1 71  ? -6.401  8.762   -42.303 1.00 13.15 ? 71  ASN D C   1 
ATOM   6983 O  O   . ASN D 1 71  ? -7.063  7.975   -43.035 1.00 14.02 ? 71  ASN D O   1 
ATOM   6984 C  CB  . ASN D 1 71  ? -6.019  10.897  -43.419 1.00 18.32 ? 71  ASN D CB  1 
ATOM   6985 C  CG  . ASN D 1 71  ? -5.013  11.974  -43.701 1.00 21.36 ? 71  ASN D CG  1 
ATOM   6986 O  OD1 . ASN D 1 71  ? -3.816  11.782  -43.513 1.00 25.08 ? 71  ASN D OD1 1 
ATOM   6987 N  ND2 . ASN D 1 71  ? -5.506  13.158  -44.122 1.00 25.52 ? 71  ASN D ND2 1 
ATOM   6988 N  N   . LEU D 1 72  ? -6.565  8.849   -40.976 1.00 12.00 ? 72  LEU D N   1 
ATOM   6989 C  CA  . LEU D 1 72  ? -7.545  8.002   -40.265 1.00 12.95 ? 72  LEU D CA  1 
ATOM   6990 C  C   . LEU D 1 72  ? -8.469  8.941   -39.476 1.00 14.33 ? 72  LEU D C   1 
ATOM   6991 O  O   . LEU D 1 72  ? -8.068  10.115  -39.131 1.00 13.99 ? 72  LEU D O   1 
ATOM   6992 C  CB  . LEU D 1 72  ? -6.874  7.076   -39.255 1.00 13.81 ? 72  LEU D CB  1 
ATOM   6993 C  CG  . LEU D 1 72  ? -5.935  6.108   -39.967 1.00 14.67 ? 72  LEU D CG  1 
ATOM   6994 C  CD1 . LEU D 1 72  ? -5.083  5.364   -38.942 1.00 12.60 ? 72  LEU D CD1 1 
ATOM   6995 C  CD2 . LEU D 1 72  ? -6.784  5.184   -40.797 1.00 13.23 ? 72  LEU D CD2 1 
ATOM   6996 N  N   . PRO D 1 73  ? -9.710  8.472   -39.280 1.00 13.10 ? 73  PRO D N   1 
ATOM   6997 C  CA  . PRO D 1 73  ? -10.742 9.311   -38.587 1.00 15.57 ? 73  PRO D CA  1 
ATOM   6998 C  C   . PRO D 1 73  ? -10.555 9.375   -37.077 1.00 15.79 ? 73  PRO D C   1 
ATOM   6999 O  O   . PRO D 1 73  ? -10.138 8.405   -36.441 1.00 15.97 ? 73  PRO D O   1 
ATOM   7000 C  CB  . PRO D 1 73  ? -12.018 8.688   -39.043 1.00 14.77 ? 73  PRO D CB  1 
ATOM   7001 C  CG  . PRO D 1 73  ? -11.701 7.199   -39.085 1.00 14.81 ? 73  PRO D CG  1 
ATOM   7002 C  CD  . PRO D 1 73  ? -10.273 7.149   -39.620 1.00 13.74 ? 73  PRO D CD  1 
ATOM   7003 N  N   . SER D 1 74  ? -10.882 10.498  -36.472 1.00 18.76 ? 74  SER D N   1 
ATOM   7004 C  CA  . SER D 1 74  ? -10.677 10.612  -35.030 1.00 19.01 ? 74  SER D CA  1 
ATOM   7005 C  C   . SER D 1 74  ? -11.635 9.741   -34.206 1.00 17.95 ? 74  SER D C   1 
ATOM   7006 O  O   . SER D 1 74  ? -11.399 9.523   -32.998 1.00 22.14 ? 74  SER D O   1 
ATOM   7007 C  CB  . SER D 1 74  ? -10.688 12.092  -34.573 1.00 21.50 ? 74  SER D CB  1 
ATOM   7008 O  OG  . SER D 1 74  ? -11.910 12.692  -34.965 1.00 23.60 ? 74  SER D OG  1 
ATOM   7009 N  N   . ASP D 1 75  ? -12.674 9.217   -34.828 1.00 18.99 ? 75  ASP D N   1 
ATOM   7010 C  CA  . ASP D 1 75  ? -13.574 8.350   -34.087 1.00 22.22 ? 75  ASP D CA  1 
ATOM   7011 C  C   . ASP D 1 75  ? -12.900 6.934   -33.890 1.00 20.99 ? 75  ASP D C   1 
ATOM   7012 O  O   . ASP D 1 75  ? -13.411 6.086   -33.105 1.00 24.35 ? 75  ASP D O   1 
ATOM   7013 C  CB  . ASP D 1 75  ? -15.008 8.267   -34.609 1.00 27.46 ? 75  ASP D CB  1 
ATOM   7014 C  CG  . ASP D 1 75  ? -15.123 7.735   -36.023 1.00 34.94 ? 75  ASP D CG  1 
ATOM   7015 O  OD1 . ASP D 1 75  ? -14.123 7.703   -36.768 1.00 40.76 ? 75  ASP D OD1 1 
ATOM   7016 O  OD2 . ASP D 1 75  ? -16.259 7.359   -36.391 1.00 45.23 ? 75  ASP D OD2 1 
ATOM   7017 N  N   . MET D 1 76  ? -11.781 6.723   -34.591 1.00 16.77 ? 76  MET D N   1 
ATOM   7018 C  CA  . MET D 1 76  ? -11.039 5.474   -34.429 1.00 18.59 ? 76  MET D CA  1 
ATOM   7019 C  C   . MET D 1 76  ? -10.101 5.688   -33.237 1.00 14.62 ? 76  MET D C   1 
ATOM   7020 O  O   . MET D 1 76  ? -9.392  6.685   -33.152 1.00 14.38 ? 76  MET D O   1 
ATOM   7021 C  CB  . MET D 1 76  ? -10.302 5.166   -35.766 1.00 18.69 ? 76  MET D CB  1 
ATOM   7022 C  CG  . MET D 1 76  ? -9.364  4.000   -35.709 1.00 18.20 ? 76  MET D CG  1 
ATOM   7023 S  SD  . MET D 1 76  ? -8.714  3.837   -37.414 1.00 17.57 ? 76  MET D SD  1 
ATOM   7024 C  CE  . MET D 1 76  ? -7.369  2.710   -37.098 1.00 14.62 ? 76  MET D CE  1 
ATOM   7025 N  N   . HIS D 1 77  ? -10.153 4.806   -32.252 1.00 15.76 ? 77  HIS D N   1 
ATOM   7026 C  CA  . HIS D 1 77  ? -9.378  4.983   -31.062 1.00 16.11 ? 77  HIS D CA  1 
ATOM   7027 C  C   . HIS D 1 77  ? -8.905  3.729   -30.407 1.00 15.30 ? 77  HIS D C   1 
ATOM   7028 O  O   . HIS D 1 77  ? -9.429  2.662   -30.716 1.00 15.98 ? 77  HIS D O   1 
ATOM   7029 C  CB  . HIS D 1 77  ? -10.102 5.990   -30.101 1.00 19.74 ? 77  HIS D CB  1 
ATOM   7030 C  CG  . HIS D 1 77  ? -11.357 5.486   -29.473 1.00 25.92 ? 77  HIS D CG  1 
ATOM   7031 N  ND1 . HIS D 1 77  ? -12.555 5.505   -30.107 1.00 27.69 ? 77  HIS D ND1 1 
ATOM   7032 C  CD2 . HIS D 1 77  ? -11.609 5.004   -28.170 1.00 28.60 ? 77  HIS D CD2 1 
ATOM   7033 C  CE1 . HIS D 1 77  ? -13.509 4.990   -29.297 1.00 28.08 ? 77  HIS D CE1 1 
ATOM   7034 N  NE2 . HIS D 1 77  ? -12.933 4.697   -28.108 1.00 27.22 ? 77  HIS D NE2 1 
ATOM   7035 N  N   . ILE D 1 78  ? -8.013  3.915   -29.457 1.00 15.10 ? 78  ILE D N   1 
ATOM   7036 C  CA  . ILE D 1 78  ? -7.622  2.812   -28.618 1.00 16.56 ? 78  ILE D CA  1 
ATOM   7037 C  C   . ILE D 1 78  ? -7.979  3.093   -27.170 1.00 16.84 ? 78  ILE D C   1 
ATOM   7038 O  O   . ILE D 1 78  ? -7.868  4.247   -26.673 1.00 16.13 ? 78  ILE D O   1 
ATOM   7039 C  CB  . ILE D 1 78  ? -6.131  2.439   -28.763 1.00 17.14 ? 78  ILE D CB  1 
ATOM   7040 C  CG1 . ILE D 1 78  ? -5.233  3.660   -28.571 1.00 17.48 ? 78  ILE D CG1 1 
ATOM   7041 C  CG2 . ILE D 1 78  ? -5.876  1.793   -30.116 1.00 15.77 ? 78  ILE D CG2 1 
ATOM   7042 C  CD1 . ILE D 1 78  ? -3.794  3.409   -28.967 1.00 18.54 ? 78  ILE D CD1 1 
ATOM   7043 N  N   . GLN D 1 79  ? -8.389  2.009   -26.530 1.00 19.98 ? 79  GLN D N   1 
ATOM   7044 C  CA  . GLN D 1 79  ? -8.643  2.050   -25.083 1.00 21.63 ? 79  GLN D CA  1 
ATOM   7045 C  C   . GLN D 1 79  ? -7.730  1.115   -24.376 1.00 20.91 ? 79  GLN D C   1 
ATOM   7046 O  O   . GLN D 1 79  ? -7.420  0.051   -24.919 1.00 24.51 ? 79  GLN D O   1 
ATOM   7047 C  CB  . GLN D 1 79  ? -10.102 1.707   -24.732 1.00 24.85 ? 79  GLN D CB  1 
ATOM   7048 C  CG  . GLN D 1 79  ? -11.173 2.740   -25.168 1.00 32.62 ? 79  GLN D CG  1 
ATOM   7049 C  CD  . GLN D 1 79  ? -11.043 4.201   -24.635 1.00 41.50 ? 79  GLN D CD  1 
ATOM   7050 O  OE1 . GLN D 1 79  ? -10.025 4.631   -24.069 1.00 43.98 ? 79  GLN D OE1 1 
ATOM   7051 N  NE2 . GLN D 1 79  ? -12.103 4.977   -24.855 1.00 44.66 ? 79  GLN D NE2 1 
ATOM   7052 N  N   . GLY D 1 80  ? -7.303  1.470   -23.161 1.00 20.06 ? 80  GLY D N   1 
ATOM   7053 C  CA  . GLY D 1 80  ? -6.464  0.551   -22.403 1.00 21.42 ? 80  GLY D CA  1 
ATOM   7054 C  C   . GLY D 1 80  ? -5.285  1.245   -21.834 1.00 25.83 ? 80  GLY D C   1 
ATOM   7055 O  O   . GLY D 1 80  ? -4.666  0.753   -20.909 1.00 30.61 ? 80  GLY D O   1 
ATOM   7056 N  N   . LEU D 1 81  ? -4.938  2.391   -22.411 1.00 18.53 ? 81  LEU D N   1 
ATOM   7057 C  CA  . LEU D 1 81  ? -3.836  3.188   -21.912 1.00 19.14 ? 81  LEU D CA  1 
ATOM   7058 C  C   . LEU D 1 81  ? -4.294  4.151   -20.788 1.00 17.12 ? 81  LEU D C   1 
ATOM   7059 O  O   . LEU D 1 81  ? -5.454  4.104   -20.346 1.00 18.77 ? 81  LEU D O   1 
ATOM   7060 C  CB  . LEU D 1 81  ? -3.262  3.986   -23.069 1.00 17.26 ? 81  LEU D CB  1 
ATOM   7061 C  CG  . LEU D 1 81  ? -2.642  3.104   -24.168 1.00 19.09 ? 81  LEU D CG  1 
ATOM   7062 C  CD1 . LEU D 1 81  ? -2.313  3.904   -25.428 1.00 20.01 ? 81  LEU D CD1 1 
ATOM   7063 C  CD2 . LEU D 1 81  ? -1.445  2.290   -23.656 1.00 19.52 ? 81  LEU D CD2 1 
ATOM   7064 N  N   . GLN D 1 82  ? -3.393  5.051   -20.359 1.00 19.47 ? 82  GLN D N   1 
ATOM   7065 C  CA  . GLN D 1 82  ? -3.744  5.997   -19.265 1.00 17.24 ? 82  GLN D CA  1 
ATOM   7066 C  C   . GLN D 1 82  ? -4.739  7.098   -19.699 1.00 18.04 ? 82  GLN D C   1 
ATOM   7067 O  O   . GLN D 1 82  ? -5.370  7.741   -18.865 1.00 18.90 ? 82  GLN D O   1 
ATOM   7068 C  CB  . GLN D 1 82  ? -2.494  6.647   -18.659 1.00 19.34 ? 82  GLN D CB  1 
ATOM   7069 C  CG  . GLN D 1 82  ? -2.021  7.961   -19.295 1.00 21.08 ? 82  GLN D CG  1 
ATOM   7070 C  CD  . GLN D 1 82  ? -1.504  7.849   -20.750 1.00 23.53 ? 82  GLN D CD  1 
ATOM   7071 O  OE1 . GLN D 1 82  ? -1.143  6.770   -21.252 1.00 24.25 ? 82  GLN D OE1 1 
ATOM   7072 N  NE2 . GLN D 1 82  ? -1.459  8.998   -21.427 1.00 23.43 ? 82  GLN D NE2 1 
ATOM   7073 N  N   . SER D 1 83  ? -4.894  7.279   -21.003 1.00 17.68 ? 83  SER D N   1 
ATOM   7074 C  CA  . SER D 1 83  ? -5.885  8.215   -21.603 1.00 18.08 ? 83  SER D CA  1 
ATOM   7075 C  C   . SER D 1 83  ? -6.426  7.596   -22.886 1.00 17.55 ? 83  SER D C   1 
ATOM   7076 O  O   . SER D 1 83  ? -5.764  6.732   -23.407 1.00 15.82 ? 83  SER D O   1 
ATOM   7077 C  CB  . SER D 1 83  ? -5.196  9.502   -22.053 1.00 17.19 ? 83  SER D CB  1 
ATOM   7078 O  OG  . SER D 1 83  ? -4.532  10.177  -20.962 1.00 17.29 ? 83  SER D OG  1 
ATOM   7079 N  N   . ARG D 1 84  ? -7.533  8.068   -23.466 1.00 16.03 ? 84  ARG D N   1 
ATOM   7080 C  CA  . ARG D 1 84  ? -8.004  7.719   -24.782 1.00 16.62 ? 84  ARG D CA  1 
ATOM   7081 C  C   . ARG D 1 84  ? -7.090  8.378   -25.842 1.00 15.61 ? 84  ARG D C   1 
ATOM   7082 O  O   . ARG D 1 84  ? -6.809  9.617   -25.787 1.00 15.33 ? 84  ARG D O   1 
ATOM   7083 C  CB  . ARG D 1 84  ? -9.411  8.216   -25.076 1.00 20.07 ? 84  ARG D CB  1 
ATOM   7084 C  CG  . ARG D 1 84  ? -9.852  7.748   -26.484 1.00 24.88 ? 84  ARG D CG  1 
ATOM   7085 C  CD  . ARG D 1 84  ? -10.671 8.729   -27.339 1.00 31.54 ? 84  ARG D CD  1 
ATOM   7086 N  NE  . ARG D 1 84  ? -12.103 8.396   -27.358 1.00 40.07 ? 84  ARG D NE  1 
ATOM   7087 C  CZ  . ARG D 1 84  ? -12.906 8.390   -28.428 1.00 37.04 ? 84  ARG D CZ  1 
ATOM   7088 N  NH1 . ARG D 1 84  ? -12.454 8.695   -29.640 1.00 35.78 ? 84  ARG D NH1 1 
ATOM   7089 N  NH2 . ARG D 1 84  ? -14.188 8.073   -28.275 1.00 36.79 ? 84  ARG D NH2 1 
ATOM   7090 N  N   . TYR D 1 85  ? -6.593  7.557   -26.748 1.00 15.80 ? 85  TYR D N   1 
ATOM   7091 C  CA  . TYR D 1 85  ? -5.800  7.983   -27.878 1.00 12.74 ? 85  TYR D CA  1 
ATOM   7092 C  C   . TYR D 1 85  ? -6.584  7.740   -29.146 1.00 13.18 ? 85  TYR D C   1 
ATOM   7093 O  O   . TYR D 1 85  ? -7.134  6.644   -29.375 1.00 14.57 ? 85  TYR D O   1 
ATOM   7094 C  CB  . TYR D 1 85  ? -4.499  7.175   -27.910 1.00 11.98 ? 85  TYR D CB  1 
ATOM   7095 C  CG  . TYR D 1 85  ? -3.486  7.716   -26.915 1.00 12.20 ? 85  TYR D CG  1 
ATOM   7096 C  CD1 . TYR D 1 85  ? -2.460  8.626   -27.297 1.00 11.92 ? 85  TYR D CD1 1 
ATOM   7097 C  CD2 . TYR D 1 85  ? -3.500  7.293   -25.528 1.00 12.77 ? 85  TYR D CD2 1 
ATOM   7098 C  CE1 . TYR D 1 85  ? -1.490  9.041   -26.357 1.00 12.13 ? 85  TYR D CE1 1 
ATOM   7099 C  CE2 . TYR D 1 85  ? -2.521  7.684   -24.638 1.00 14.29 ? 85  TYR D CE2 1 
ATOM   7100 C  CZ  . TYR D 1 85  ? -1.556  8.633   -25.024 1.00 14.53 ? 85  TYR D CZ  1 
ATOM   7101 O  OH  . TYR D 1 85  ? -0.618  9.016   -24.084 1.00 15.26 ? 85  TYR D OH  1 
ATOM   7102 N  N   . SER D 1 86  ? -6.662  8.791   -29.958 1.00 13.20 ? 86  SER D N   1 
ATOM   7103 C  CA  . SER D 1 86  ? -7.458  8.720   -31.188 1.00 12.91 ? 86  SER D CA  1 
ATOM   7104 C  C   . SER D 1 86  ? -6.553  8.664   -32.410 1.00 11.77 ? 86  SER D C   1 
ATOM   7105 O  O   . SER D 1 86  ? -5.497  9.301   -32.442 1.00 11.60 ? 86  SER D O   1 
ATOM   7106 C  CB  . SER D 1 86  ? -8.279  9.992   -31.327 1.00 13.59 ? 86  SER D CB  1 
ATOM   7107 O  OG  . SER D 1 86  ? -9.297  10.005  -30.309 1.00 15.85 ? 86  SER D OG  1 
ATOM   7108 N  N   . ALA D 1 87  ? -6.985  7.862   -33.378 1.00 13.02 ? 87  ALA D N   1 
ATOM   7109 C  CA  . ALA D 1 87  ? -6.154  7.683   -34.599 1.00 13.26 ? 87  ALA D CA  1 
ATOM   7110 C  C   . ALA D 1 87  ? -5.991  8.985   -35.364 1.00 12.31 ? 87  ALA D C   1 
ATOM   7111 O  O   . ALA D 1 87  ? -6.947  9.839   -35.386 1.00 13.08 ? 87  ALA D O   1 
ATOM   7112 C  CB  . ALA D 1 87  ? -6.732  6.605   -35.461 1.00 11.09 ? 87  ALA D CB  1 
ATOM   7113 N  N   . THR D 1 88  ? -4.863  9.132   -36.050 1.00 12.22 ? 88  THR D N   1 
ATOM   7114 C  CA  . THR D 1 88  ? -4.610  10.263  -36.952 1.00 11.96 ? 88  THR D CA  1 
ATOM   7115 C  C   . THR D 1 88  ? -4.115  9.808   -38.325 1.00 12.08 ? 88  THR D C   1 
ATOM   7116 O  O   . THR D 1 88  ? -4.531  10.324  -39.345 1.00 12.39 ? 88  THR D O   1 
ATOM   7117 C  CB  . THR D 1 88  ? -3.724  11.345  -36.305 1.00 15.02 ? 88  THR D CB  1 
ATOM   7118 O  OG1 . THR D 1 88  ? -3.595  12.435  -37.209 1.00 16.72 ? 88  THR D OG1 1 
ATOM   7119 C  CG2 . THR D 1 88  ? -2.318  10.825  -35.926 1.00 14.45 ? 88  THR D CG2 1 
ATOM   7120 N  N   . GLN D 1 89  ? -3.244  8.787   -38.351 1.00 11.63 ? 89  GLN D N   1 
ATOM   7121 C  CA  . GLN D 1 89  ? -2.734  8.349   -39.679 1.00 10.73 ? 89  GLN D CA  1 
ATOM   7122 C  C   . GLN D 1 89  ? -1.957  7.050   -39.471 1.00 9.10  ? 89  GLN D C   1 
ATOM   7123 O  O   . GLN D 1 89  ? -1.629  6.703   -38.351 1.00 10.64 ? 89  GLN D O   1 
ATOM   7124 C  CB  . GLN D 1 89  ? -1.841  9.441   -40.396 1.00 11.64 ? 89  GLN D CB  1 
ATOM   7125 C  CG  . GLN D 1 89  ? -0.615  9.753   -39.518 1.00 11.81 ? 89  GLN D CG  1 
ATOM   7126 C  CD  . GLN D 1 89  ? 0.682   9.150   -40.037 1.00 13.39 ? 89  GLN D CD  1 
ATOM   7127 O  OE1 . GLN D 1 89  ? 0.773   7.913   -40.150 1.00 14.35 ? 89  GLN D OE1 1 
ATOM   7128 N  NE2 . GLN D 1 89  ? 1.637   9.992   -40.402 1.00 15.41 ? 89  GLN D NE2 1 
ATOM   7129 N  N   . LEU D 1 90  ? -1.836  6.305   -40.550 1.00 10.43 ? 90  LEU D N   1 
ATOM   7130 C  CA  . LEU D 1 90  ? -0.863  5.182   -40.552 1.00 9.82  ? 90  LEU D CA  1 
ATOM   7131 C  C   . LEU D 1 90  ? 0.124   5.376   -41.723 1.00 9.81  ? 90  LEU D C   1 
ATOM   7132 O  O   . LEU D 1 90  ? -0.113  6.076   -42.684 1.00 9.27  ? 90  LEU D O   1 
ATOM   7133 C  CB  . LEU D 1 90  ? -1.528  3.796   -40.587 1.00 10.37 ? 90  LEU D CB  1 
ATOM   7134 C  CG  . LEU D 1 90  ? -2.458  3.431   -41.674 1.00 9.67  ? 90  LEU D CG  1 
ATOM   7135 C  CD1 . LEU D 1 90  ? -1.758  3.058   -42.972 1.00 10.16 ? 90  LEU D CD1 1 
ATOM   7136 C  CD2 . LEU D 1 90  ? -3.376  2.257   -41.223 1.00 10.71 ? 90  LEU D CD2 1 
ATOM   7137 N  N   . HIS D 1 91  ? 1.258   4.648   -41.644 1.00 9.10  ? 91  HIS D N   1 
ATOM   7138 C  CA  . HIS D 1 91  ? 2.295   4.744   -42.682 1.00 10.02 ? 91  HIS D CA  1 
ATOM   7139 C  C   . HIS D 1 91  ? 3.203   3.570   -42.452 1.00 9.32  ? 91  HIS D C   1 
ATOM   7140 O  O   . HIS D 1 91  ? 3.120   2.904   -41.419 1.00 8.40  ? 91  HIS D O   1 
ATOM   7141 C  CB  . HIS D 1 91  ? 3.100   6.074   -42.577 1.00 10.45 ? 91  HIS D CB  1 
ATOM   7142 C  CG  . HIS D 1 91  ? 3.793   6.233   -41.260 1.00 9.68  ? 91  HIS D CG  1 
ATOM   7143 N  ND1 . HIS D 1 91  ? 3.244   6.834   -40.184 1.00 10.03 ? 91  HIS D ND1 1 
ATOM   7144 C  CD2 . HIS D 1 91  ? 5.041   5.707   -40.828 1.00 8.21  ? 91  HIS D CD2 1 
ATOM   7145 C  CE1 . HIS D 1 91  ? 4.028   6.764   -39.139 1.00 10.15 ? 91  HIS D CE1 1 
ATOM   7146 N  NE2 . HIS D 1 91  ? 5.153   6.014   -39.477 1.00 10.52 ? 91  HIS D NE2 1 
ATOM   7147 N  N   . LEU D 1 92  ? 4.210   3.437   -43.371 1.00 9.92  ? 92  LEU D N   1 
ATOM   7148 C  CA  . LEU D 1 92  ? 5.100   2.223   -43.356 1.00 10.18 ? 92  LEU D CA  1 
ATOM   7149 C  C   . LEU D 1 92  ? 6.561   2.708   -43.500 1.00 9.85  ? 92  LEU D C   1 
ATOM   7150 O  O   . LEU D 1 92  ? 6.826   3.871   -43.829 1.00 9.63  ? 92  LEU D O   1 
ATOM   7151 C  CB  . LEU D 1 92  ? 4.817   1.307   -44.516 1.00 11.01 ? 92  LEU D CB  1 
ATOM   7152 C  CG  . LEU D 1 92  ? 3.402   0.673   -44.361 1.00 13.23 ? 92  LEU D CG  1 
ATOM   7153 C  CD1 . LEU D 1 92  ? 2.477   1.253   -45.376 1.00 14.78 ? 92  LEU D CD1 1 
ATOM   7154 C  CD2 . LEU D 1 92  ? 3.544   -0.827  -44.638 1.00 14.71 ? 92  LEU D CD2 1 
ATOM   7155 N  N   . HIS D 1 93  ? 7.450   1.795   -43.206 1.00 9.43  ? 93  HIS D N   1 
ATOM   7156 C  CA  . HIS D 1 93  ? 8.937   1.996   -43.365 1.00 10.06 ? 93  HIS D CA  1 
ATOM   7157 C  C   . HIS D 1 93  ? 9.430   0.777   -44.023 1.00 10.07 ? 93  HIS D C   1 
ATOM   7158 O  O   . HIS D 1 93  ? 8.957   -0.319  -43.720 1.00 10.10 ? 93  HIS D O   1 
ATOM   7159 C  CB  . HIS D 1 93  ? 9.609   2.111   -41.980 1.00 10.01 ? 93  HIS D CB  1 
ATOM   7160 C  CG  . HIS D 1 93  ? 9.153   3.287   -41.201 1.00 10.78 ? 93  HIS D CG  1 
ATOM   7161 N  ND1 . HIS D 1 93  ? 9.763   4.532   -41.246 1.00 10.89 ? 93  HIS D ND1 1 
ATOM   7162 C  CD2 . HIS D 1 93  ? 8.061   3.398   -40.355 1.00 10.01 ? 93  HIS D CD2 1 
ATOM   7163 C  CE1 . HIS D 1 93  ? 9.077   5.374   -40.424 1.00 9.87  ? 93  HIS D CE1 1 
ATOM   7164 N  NE2 . HIS D 1 93  ? 8.023   4.692   -39.890 1.00 9.24  ? 93  HIS D NE2 1 
ATOM   7165 N  N   . TRP D 1 94  ? 10.390  0.930   -44.947 1.00 9.35  ? 94  TRP D N   1 
ATOM   7166 C  CA  . TRP D 1 94  ? 10.915  -0.295  -45.706 1.00 8.68  ? 94  TRP D CA  1 
ATOM   7167 C  C   . TRP D 1 94  ? 12.321  -0.043  -46.181 1.00 9.33  ? 94  TRP D C   1 
ATOM   7168 O  O   . TRP D 1 94  ? 12.930  1.053   -45.975 1.00 10.50 ? 94  TRP D O   1 
ATOM   7169 C  CB  . TRP D 1 94  ? 10.015  -0.604  -46.893 1.00 11.31 ? 94  TRP D CB  1 
ATOM   7170 C  CG  . TRP D 1 94  ? 9.843   0.653   -47.796 1.00 9.22  ? 94  TRP D CG  1 
ATOM   7171 C  CD1 . TRP D 1 94  ? 10.632  0.976   -48.931 1.00 9.89  ? 94  TRP D CD1 1 
ATOM   7172 C  CD2 . TRP D 1 94  ? 8.812   1.720   -47.746 1.00 10.48 ? 94  TRP D CD2 1 
ATOM   7173 N  NE1 . TRP D 1 94  ? 10.195  2.114   -49.536 1.00 10.66 ? 94  TRP D NE1 1 
ATOM   7174 C  CE2 . TRP D 1 94  ? 9.080   2.606   -48.876 1.00 11.02 ? 94  TRP D CE2 1 
ATOM   7175 C  CE3 . TRP D 1 94  ? 7.717   2.010   -46.918 1.00 11.15 ? 94  TRP D CE3 1 
ATOM   7176 C  CZ2 . TRP D 1 94  ? 8.314   3.792   -49.107 1.00 10.87 ? 94  TRP D CZ2 1 
ATOM   7177 C  CZ3 . TRP D 1 94  ? 6.977   3.189   -47.140 1.00 10.52 ? 94  TRP D CZ3 1 
ATOM   7178 C  CH2 . TRP D 1 94  ? 7.229   4.028   -48.246 1.00 10.80 ? 94  TRP D CH2 1 
ATOM   7179 N  N   . GLY D 1 95  ? 12.867  -1.096  -46.804 1.00 10.03 ? 95  GLY D N   1 
ATOM   7180 C  CA  . GLY D 1 95  ? 14.275  -1.074  -47.267 1.00 10.90 ? 95  GLY D CA  1 
ATOM   7181 C  C   . GLY D 1 95  ? 14.312  -0.781  -48.790 1.00 10.78 ? 95  GLY D C   1 
ATOM   7182 O  O   . GLY D 1 95  ? 13.860  0.230   -49.300 1.00 12.09 ? 95  GLY D O   1 
ATOM   7183 N  N   . ASN D 1 96  ? 14.858  -1.724  -49.522 1.00 11.42 ? 96  ASN D N   1 
ATOM   7184 C  CA  . ASN D 1 96  ? 14.997  -1.541  -50.964 1.00 12.39 ? 96  ASN D CA  1 
ATOM   7185 C  C   . ASN D 1 96  ? 15.126  -2.934  -51.619 1.00 13.34 ? 96  ASN D C   1 
ATOM   7186 O  O   . ASN D 1 96  ? 15.237  -3.920  -50.931 1.00 14.38 ? 96  ASN D O   1 
ATOM   7187 C  CB  . ASN D 1 96  ? 16.161  -0.601  -51.256 1.00 15.23 ? 96  ASN D CB  1 
ATOM   7188 C  CG  . ASN D 1 96  ? 17.493  -1.280  -51.177 1.00 17.17 ? 96  ASN D CG  1 
ATOM   7189 O  OD1 . ASN D 1 96  ? 17.959  -1.802  -52.219 1.00 22.85 ? 96  ASN D OD1 1 
ATOM   7190 N  ND2 . ASN D 1 96  ? 18.146  -1.236  -49.984 1.00 15.60 ? 96  ASN D ND2 1 
ATOM   7191 N  N   . PRO D 1 97  ? 14.965  -2.998  -52.965 1.00 16.15 ? 97  PRO D N   1 
ATOM   7192 C  CA  . PRO D 1 97  ? 14.923  -4.299  -53.589 1.00 16.06 ? 97  PRO D CA  1 
ATOM   7193 C  C   . PRO D 1 97  ? 16.174  -5.119  -53.339 1.00 16.88 ? 97  PRO D C   1 
ATOM   7194 O  O   . PRO D 1 97  ? 16.035  -6.313  -53.190 1.00 22.28 ? 97  PRO D O   1 
ATOM   7195 C  CB  . PRO D 1 97  ? 14.708  -3.987  -55.065 1.00 16.10 ? 97  PRO D CB  1 
ATOM   7196 C  CG  . PRO D 1 97  ? 14.362  -2.515  -55.178 1.00 18.14 ? 97  PRO D CG  1 
ATOM   7197 C  CD  . PRO D 1 97  ? 14.771  -1.876  -53.882 1.00 14.96 ? 97  PRO D CD  1 
ATOM   7198 N  N   . ASN D 1 98  ? 17.343  -4.516  -53.148 1.00 17.44 ? 98  ASN D N   1 
ATOM   7199 C  CA  . ASN D 1 98  ? 18.565  -5.262  -52.840 1.00 20.78 ? 98  ASN D CA  1 
ATOM   7200 C  C   . ASN D 1 98  ? 18.778  -5.572  -51.339 1.00 21.91 ? 98  ASN D C   1 
ATOM   7201 O  O   . ASN D 1 98  ? 19.799  -6.181  -50.940 1.00 22.67 ? 98  ASN D O   1 
ATOM   7202 C  CB  . ASN D 1 98  ? 19.784  -4.456  -53.326 1.00 26.34 ? 98  ASN D CB  1 
ATOM   7203 C  CG  . ASN D 1 98  ? 19.759  -4.201  -54.844 1.00 32.85 ? 98  ASN D CG  1 
ATOM   7204 O  OD1 . ASN D 1 98  ? 19.439  -5.103  -55.639 1.00 38.60 ? 98  ASN D OD1 1 
ATOM   7205 N  ND2 . ASN D 1 98  ? 20.084  -2.950  -55.256 1.00 37.99 ? 98  ASN D ND2 1 
ATOM   7206 N  N   . ASP D 1 99  ? 17.917  -5.028  -50.470 1.00 17.37 ? 99  ASP D N   1 
ATOM   7207 C  CA  . ASP D 1 99  ? 18.069  -5.249  -49.039 1.00 17.46 ? 99  ASP D CA  1 
ATOM   7208 C  C   . ASP D 1 99  ? 16.661  -5.029  -48.425 1.00 14.67 ? 99  ASP D C   1 
ATOM   7209 O  O   . ASP D 1 99  ? 16.343  -3.958  -47.908 1.00 14.48 ? 99  ASP D O   1 
ATOM   7210 C  CB  . ASP D 1 99  ? 19.103  -4.282  -48.403 1.00 18.83 ? 99  ASP D CB  1 
ATOM   7211 C  CG  . ASP D 1 99  ? 19.264  -4.492  -46.888 1.00 21.25 ? 99  ASP D CG  1 
ATOM   7212 O  OD1 . ASP D 1 99  ? 18.987  -5.632  -46.453 1.00 22.92 ? 99  ASP D OD1 1 
ATOM   7213 O  OD2 . ASP D 1 99  ? 19.562  -3.506  -46.141 1.00 23.99 ? 99  ASP D OD2 1 
ATOM   7214 N  N   . PRO D 1 100 ? 15.802  -6.024  -48.517 1.00 14.76 ? 100 PRO D N   1 
ATOM   7215 C  CA  . PRO D 1 100 ? 14.397  -5.882  -48.092 1.00 13.23 ? 100 PRO D CA  1 
ATOM   7216 C  C   . PRO D 1 100 ? 14.329  -6.163  -46.608 1.00 12.62 ? 100 PRO D C   1 
ATOM   7217 O  O   . PRO D 1 100 ? 13.697  -7.111  -46.138 1.00 13.59 ? 100 PRO D O   1 
ATOM   7218 C  CB  . PRO D 1 100 ? 13.703  -6.912  -48.946 1.00 14.67 ? 100 PRO D CB  1 
ATOM   7219 C  CG  . PRO D 1 100 ? 14.692  -7.998  -48.944 1.00 14.59 ? 100 PRO D CG  1 
ATOM   7220 C  CD  . PRO D 1 100 ? 16.028  -7.343  -49.158 1.00 16.98 ? 100 PRO D CD  1 
ATOM   7221 N  N   . HIS D 1 101 ? 15.018  -5.333  -45.847 1.00 11.32 ? 101 HIS D N   1 
ATOM   7222 C  CA  . HIS D 1 101 ? 15.181  -5.507  -44.343 1.00 11.05 ? 101 HIS D CA  1 
ATOM   7223 C  C   . HIS D 1 101 ? 15.118  -4.128  -43.713 1.00 11.76 ? 101 HIS D C   1 
ATOM   7224 O  O   . HIS D 1 101 ? 16.083  -3.621  -43.053 1.00 14.94 ? 101 HIS D O   1 
ATOM   7225 C  CB  . HIS D 1 101 ? 16.500  -6.188  -44.029 1.00 13.56 ? 101 HIS D CB  1 
ATOM   7226 C  CG  . HIS D 1 101 ? 16.573  -7.591  -44.645 1.00 17.79 ? 101 HIS D CG  1 
ATOM   7227 N  ND1 . HIS D 1 101 ? 15.913  -8.659  -44.138 1.00 19.31 ? 101 HIS D ND1 1 
ATOM   7228 C  CD2 . HIS D 1 101 ? 17.120  -8.018  -45.850 1.00 17.42 ? 101 HIS D CD2 1 
ATOM   7229 C  CE1 . HIS D 1 101 ? 16.123  -9.750  -44.912 1.00 22.09 ? 101 HIS D CE1 1 
ATOM   7230 N  NE2 . HIS D 1 101 ? 16.854  -9.364  -45.961 1.00 21.88 ? 101 HIS D NE2 1 
ATOM   7231 N  N   . GLY D 1 102 ? 13.951  -3.556  -43.844 1.00 9.87  ? 102 GLY D N   1 
ATOM   7232 C  CA  . GLY D 1 102 ? 13.806  -2.114  -43.515 1.00 9.56  ? 102 GLY D CA  1 
ATOM   7233 C  C   . GLY D 1 102 ? 12.881  -1.825  -42.320 1.00 9.64  ? 102 GLY D C   1 
ATOM   7234 O  O   . GLY D 1 102 ? 12.329  -0.714  -42.251 1.00 11.08 ? 102 GLY D O   1 
ATOM   7235 N  N   . SER D 1 103 ? 12.599  -2.809  -41.483 1.00 10.09 ? 103 SER D N   1 
ATOM   7236 C  CA  . SER D 1 103 ? 11.850  -2.425  -40.285 1.00 10.49 ? 103 SER D CA  1 
ATOM   7237 C  C   . SER D 1 103 ? 12.647  -1.388  -39.449 1.00 10.16 ? 103 SER D C   1 
ATOM   7238 O  O   . SER D 1 103 ? 13.912  -1.300  -39.518 1.00 10.84 ? 103 SER D O   1 
ATOM   7239 C  CB  . SER D 1 103 ? 11.471  -3.606  -39.386 1.00 11.60 ? 103 SER D CB  1 
ATOM   7240 O  OG  . SER D 1 103 ? 12.672  -4.224  -38.830 1.00 12.65 ? 103 SER D OG  1 
ATOM   7241 N  N   . GLU D 1 104 ? 11.960  -0.649  -38.597 1.00 9.78  ? 104 GLU D N   1 
ATOM   7242 C  CA  . GLU D 1 104 ? 12.634  0.264   -37.648 1.00 10.49 ? 104 GLU D CA  1 
ATOM   7243 C  C   . GLU D 1 104 ? 13.058  -0.461  -36.396 1.00 9.64  ? 104 GLU D C   1 
ATOM   7244 O  O   . GLU D 1 104 ? 14.246  -0.490  -36.016 1.00 9.55  ? 104 GLU D O   1 
ATOM   7245 C  CB  . GLU D 1 104 ? 11.772  1.485   -37.339 1.00 10.98 ? 104 GLU D CB  1 
ATOM   7246 C  CG  . GLU D 1 104 ? 11.365  2.193   -38.628 1.00 10.67 ? 104 GLU D CG  1 
ATOM   7247 C  CD  . GLU D 1 104 ? 11.277  3.706   -38.351 1.00 11.39 ? 104 GLU D CD  1 
ATOM   7248 O  OE1 . GLU D 1 104 ? 10.284  4.152   -37.702 1.00 10.50 ? 104 GLU D OE1 1 
ATOM   7249 O  OE2 . GLU D 1 104 ? 12.261  4.435   -38.748 1.00 11.76 ? 104 GLU D OE2 1 
ATOM   7250 N  N   . HIS D 1 105 ? 12.098  -1.083  -35.718 1.00 10.38 ? 105 HIS D N   1 
ATOM   7251 C  CA  . HIS D 1 105 ? 12.433  -1.908  -34.590 1.00 10.11 ? 105 HIS D CA  1 
ATOM   7252 C  C   . HIS D 1 105 ? 13.067  -3.188  -35.077 1.00 10.33 ? 105 HIS D C   1 
ATOM   7253 O  O   . HIS D 1 105 ? 12.724  -3.723  -36.130 1.00 11.46 ? 105 HIS D O   1 
ATOM   7254 C  CB  . HIS D 1 105 ? 11.167  -2.212  -33.735 1.00 10.41 ? 105 HIS D CB  1 
ATOM   7255 C  CG  . HIS D 1 105 ? 10.688  -1.005  -33.029 1.00 10.18 ? 105 HIS D CG  1 
ATOM   7256 N  ND1 . HIS D 1 105 ? 9.795   -0.184  -33.592 1.00 10.85 ? 105 HIS D ND1 1 
ATOM   7257 C  CD2 . HIS D 1 105 ? 11.062  -0.436  -31.830 1.00 10.81 ? 105 HIS D CD2 1 
ATOM   7258 C  CE1 . HIS D 1 105 ? 9.617   0.920   -32.765 1.00 9.99  ? 105 HIS D CE1 1 
ATOM   7259 N  NE2 . HIS D 1 105 ? 10.359  0.743   -31.705 1.00 9.80  ? 105 HIS D NE2 1 
ATOM   7260 N  N   . THR D 1 106 ? 14.037  -3.685  -34.305 1.00 11.96 ? 106 THR D N   1 
ATOM   7261 C  CA  . THR D 1 106 ? 14.645  -4.985  -34.607 1.00 12.32 ? 106 THR D CA  1 
ATOM   7262 C  C   . THR D 1 106 ? 14.409  -5.964  -33.464 1.00 12.26 ? 106 THR D C   1 
ATOM   7263 O  O   . THR D 1 106 ? 14.115  -5.527  -32.361 1.00 11.02 ? 106 THR D O   1 
ATOM   7264 C  CB  . THR D 1 106 ? 16.154  -4.836  -34.888 1.00 12.16 ? 106 THR D CB  1 
ATOM   7265 O  OG1 . THR D 1 106 ? 16.850  -4.197  -33.794 1.00 13.67 ? 106 THR D OG1 1 
ATOM   7266 C  CG2 . THR D 1 106 ? 16.425  -3.982  -36.149 1.00 13.08 ? 106 THR D CG2 1 
ATOM   7267 N  N   . VAL D 1 107 ? 14.519  -7.284  -33.743 1.00 13.52 ? 107 VAL D N   1 
ATOM   7268 C  CA  . VAL D 1 107 ? 14.260  -8.246  -32.662 1.00 14.96 ? 107 VAL D CA  1 
ATOM   7269 C  C   . VAL D 1 107 ? 15.492  -9.134  -32.630 1.00 15.21 ? 107 VAL D C   1 
ATOM   7270 O  O   . VAL D 1 107 ? 15.851  -9.748  -33.652 1.00 17.93 ? 107 VAL D O   1 
ATOM   7271 C  CB  . VAL D 1 107 ? 12.941  -9.048  -32.806 1.00 15.54 ? 107 VAL D CB  1 
ATOM   7272 C  CG1 . VAL D 1 107 ? 12.864  -10.078 -31.670 1.00 16.91 ? 107 VAL D CG1 1 
ATOM   7273 C  CG2 . VAL D 1 107 ? 11.745  -8.078  -32.809 1.00 16.03 ? 107 VAL D CG2 1 
ATOM   7274 N  N   . SER D 1 108 ? 16.137  -9.097  -31.457 1.00 17.21 ? 108 SER D N   1 
ATOM   7275 C  CA  . SER D 1 108 ? 17.417  -9.824  -31.187 1.00 16.89 ? 108 SER D CA  1 
ATOM   7276 C  C   . SER D 1 108 ? 18.378  -9.509  -32.309 1.00 16.53 ? 108 SER D C   1 
ATOM   7277 O  O   . SER D 1 108 ? 18.958  -10.422 -32.938 1.00 16.76 ? 108 SER D O   1 
ATOM   7278 C  CB  . SER D 1 108 ? 17.116  -11.351 -31.107 1.00 17.91 ? 108 SER D CB  1 
ATOM   7279 O  OG  . SER D 1 108 ? 16.358  -11.582 -29.960 1.00 20.15 ? 108 SER D OG  1 
ATOM   7280 N  N   . GLY D 1 109 ? 18.489  -8.219  -32.627 1.00 14.24 ? 109 GLY D N   1 
ATOM   7281 C  CA  . GLY D 1 109 ? 19.396  -7.766  -33.694 1.00 14.41 ? 109 GLY D CA  1 
ATOM   7282 C  C   . GLY D 1 109 ? 18.980  -7.936  -35.185 1.00 15.11 ? 109 GLY D C   1 
ATOM   7283 O  O   . GLY D 1 109 ? 19.751  -7.561  -36.048 1.00 19.65 ? 109 GLY D O   1 
ATOM   7284 N  N   . GLN D 1 110 ? 17.794  -8.465  -35.471 1.00 17.02 ? 110 GLN D N   1 
ATOM   7285 C  CA  . GLN D 1 110 ? 17.405  -8.806  -36.846 1.00 17.25 ? 110 GLN D CA  1 
ATOM   7286 C  C   . GLN D 1 110 ? 16.314  -7.817  -37.259 1.00 13.92 ? 110 GLN D C   1 
ATOM   7287 O  O   . GLN D 1 110 ? 15.313  -7.631  -36.489 1.00 14.01 ? 110 GLN D O   1 
ATOM   7288 C  CB  . GLN D 1 110 ? 16.813  -10.232 -36.931 1.00 21.00 ? 110 GLN D CB  1 
ATOM   7289 C  CG  . GLN D 1 110 ? 17.636  -11.374 -36.325 1.00 24.52 ? 110 GLN D CG  1 
ATOM   7290 C  CD  . GLN D 1 110 ? 19.041  -11.406 -36.872 1.00 28.38 ? 110 GLN D CD  1 
ATOM   7291 O  OE1 . GLN D 1 110 ? 19.258  -11.544 -38.083 1.00 33.99 ? 110 GLN D OE1 1 
ATOM   7292 N  NE2 . GLN D 1 110 ? 20.023  -11.247 -35.971 1.00 31.40 ? 110 GLN D NE2 1 
ATOM   7293 N  N   . HIS D 1 111 ? 16.437  -7.275  -38.486 1.00 13.41 ? 111 HIS D N   1 
ATOM   7294 C  CA  . HIS D 1 111 ? 15.364  -6.412  -39.055 1.00 12.69 ? 111 HIS D CA  1 
ATOM   7295 C  C   . HIS D 1 111 ? 14.330  -7.325  -39.634 1.00 13.27 ? 111 HIS D C   1 
ATOM   7296 O  O   . HIS D 1 111 ? 14.655  -8.434  -40.131 1.00 15.90 ? 111 HIS D O   1 
ATOM   7297 C  CB  . HIS D 1 111 ? 15.834  -5.596  -40.246 1.00 14.02 ? 111 HIS D CB  1 
ATOM   7298 C  CG  . HIS D 1 111 ? 16.603  -4.387  -39.853 1.00 12.61 ? 111 HIS D CG  1 
ATOM   7299 N  ND1 . HIS D 1 111 ? 16.002  -3.144  -39.689 1.00 14.39 ? 111 HIS D ND1 1 
ATOM   7300 C  CD2 . HIS D 1 111 ? 17.929  -4.230  -39.593 1.00 14.44 ? 111 HIS D CD2 1 
ATOM   7301 C  CE1 . HIS D 1 111 ? 16.953  -2.272  -39.328 1.00 15.23 ? 111 HIS D CE1 1 
ATOM   7302 N  NE2 . HIS D 1 111 ? 18.132  -2.923  -39.295 1.00 15.84 ? 111 HIS D NE2 1 
ATOM   7303 N  N   . PHE D 1 112 ? 13.089  -6.899  -39.608 1.00 11.20 ? 112 PHE D N   1 
ATOM   7304 C  CA  . PHE D 1 112 ? 12.080  -7.520  -40.435 1.00 12.65 ? 112 PHE D CA  1 
ATOM   7305 C  C   . PHE D 1 112 ? 12.047  -6.769  -41.783 1.00 11.36 ? 112 PHE D C   1 
ATOM   7306 O  O   . PHE D 1 112 ? 12.783  -5.766  -41.963 1.00 11.00 ? 112 PHE D O   1 
ATOM   7307 C  CB  . PHE D 1 112 ? 10.722  -7.454  -39.713 1.00 13.56 ? 112 PHE D CB  1 
ATOM   7308 C  CG  . PHE D 1 112 ? 10.590  -8.529  -38.625 1.00 15.05 ? 112 PHE D CG  1 
ATOM   7309 C  CD1 . PHE D 1 112 ? 9.859   -9.688  -38.927 1.00 17.13 ? 112 PHE D CD1 1 
ATOM   7310 C  CD2 . PHE D 1 112 ? 11.201  -8.396  -37.365 1.00 16.79 ? 112 PHE D CD2 1 
ATOM   7311 C  CE1 . PHE D 1 112 ? 9.744   -10.717 -38.018 1.00 19.02 ? 112 PHE D CE1 1 
ATOM   7312 C  CE2 . PHE D 1 112 ? 11.069  -9.423  -36.442 1.00 17.67 ? 112 PHE D CE2 1 
ATOM   7313 C  CZ  . PHE D 1 112 ? 10.335  -10.558 -36.779 1.00 17.76 ? 112 PHE D CZ  1 
ATOM   7314 N  N   . ALA D 1 113 ? 11.211  -7.200  -42.713 1.00 10.54 ? 113 ALA D N   1 
ATOM   7315 C  CA  . ALA D 1 113 ? 11.289  -6.633  -44.054 1.00 9.49  ? 113 ALA D CA  1 
ATOM   7316 C  C   . ALA D 1 113 ? 10.794  -5.149  -44.056 1.00 9.86  ? 113 ALA D C   1 
ATOM   7317 O  O   . ALA D 1 113 ? 11.280  -4.321  -44.817 1.00 10.53 ? 113 ALA D O   1 
ATOM   7318 C  CB  . ALA D 1 113 ? 10.418  -7.364  -45.022 1.00 9.34  ? 113 ALA D CB  1 
ATOM   7319 N  N   . ALA D 1 114 ? 9.724   -4.963  -43.292 1.00 9.80  ? 114 ALA D N   1 
ATOM   7320 C  CA  . ALA D 1 114 ? 9.127   -3.576  -43.245 1.00 9.00  ? 114 ALA D CA  1 
ATOM   7321 C  C   . ALA D 1 114 ? 8.364   -3.476  -41.900 1.00 9.62  ? 114 ALA D C   1 
ATOM   7322 O  O   . ALA D 1 114 ? 8.376   -4.357  -41.031 1.00 9.99  ? 114 ALA D O   1 
ATOM   7323 C  CB  . ALA D 1 114 ? 8.158   -3.389  -44.389 1.00 9.17  ? 114 ALA D CB  1 
ATOM   7324 N  N   . GLU D 1 115 ? 7.760   -2.291  -41.693 1.00 9.34  ? 115 GLU D N   1 
ATOM   7325 C  CA  . GLU D 1 115 ? 7.075   -2.012  -40.435 1.00 10.47 ? 115 GLU D CA  1 
ATOM   7326 C  C   . GLU D 1 115 ? 5.900   -1.045  -40.663 1.00 10.55 ? 115 GLU D C   1 
ATOM   7327 O  O   . GLU D 1 115 ? 5.999   -0.079  -41.414 1.00 11.01 ? 115 GLU D O   1 
ATOM   7328 C  CB  . GLU D 1 115 ? 8.057   -1.385  -39.447 1.00 10.74 ? 115 GLU D CB  1 
ATOM   7329 C  CG  . GLU D 1 115 ? 7.516   -1.301  -38.010 1.00 11.17 ? 115 GLU D CG  1 
ATOM   7330 C  CD  . GLU D 1 115 ? 8.555   -1.083  -36.935 1.00 10.79 ? 115 GLU D CD  1 
ATOM   7331 O  OE1 . GLU D 1 115 ? 9.694   -1.576  -37.144 1.00 10.92 ? 115 GLU D OE1 1 
ATOM   7332 O  OE2 . GLU D 1 115 ? 8.263   -0.457  -35.854 1.00 11.14 ? 115 GLU D OE2 1 
ATOM   7333 N  N   . LEU D 1 116 ? 4.720   -1.406  -40.103 1.00 9.30  ? 116 LEU D N   1 
ATOM   7334 C  CA  . LEU D 1 116 ? 3.532   -0.488  -40.154 1.00 10.18 ? 116 LEU D CA  1 
ATOM   7335 C  C   . LEU D 1 116 ? 3.372   0.189   -38.857 1.00 8.82  ? 116 LEU D C   1 
ATOM   7336 O  O   . LEU D 1 116 ? 3.428   -0.409  -37.788 1.00 8.17  ? 116 LEU D O   1 
ATOM   7337 C  CB  . LEU D 1 116 ? 2.231   -1.300  -40.414 1.00 10.58 ? 116 LEU D CB  1 
ATOM   7338 C  CG  . LEU D 1 116 ? 0.921   -0.503  -40.211 1.00 10.91 ? 116 LEU D CG  1 
ATOM   7339 C  CD1 . LEU D 1 116 ? 0.702   0.424   -41.410 1.00 11.92 ? 116 LEU D CD1 1 
ATOM   7340 C  CD2 . LEU D 1 116 ? -0.182  -1.557  -40.094 1.00 12.65 ? 116 LEU D CD2 1 
ATOM   7341 N  N   . HIS D 1 117 ? 3.175   1.545   -38.951 1.00 9.30  ? 117 HIS D N   1 
ATOM   7342 C  CA  . HIS D 1 117 ? 2.858   2.305   -37.733 1.00 8.77  ? 117 HIS D CA  1 
ATOM   7343 C  C   . HIS D 1 117 ? 1.528   2.954   -37.811 1.00 9.13  ? 117 HIS D C   1 
ATOM   7344 O  O   . HIS D 1 117 ? 1.227   3.626   -38.778 1.00 10.10 ? 117 HIS D O   1 
ATOM   7345 C  CB  . HIS D 1 117 ? 3.863   3.434   -37.597 1.00 9.32  ? 117 HIS D CB  1 
ATOM   7346 C  CG  . HIS D 1 117 ? 5.218   2.935   -37.188 1.00 9.68  ? 117 HIS D CG  1 
ATOM   7347 N  ND1 . HIS D 1 117 ? 6.415   3.597   -37.522 1.00 10.10 ? 117 HIS D ND1 1 
ATOM   7348 C  CD2 . HIS D 1 117 ? 5.614   1.700   -36.634 1.00 9.26  ? 117 HIS D CD2 1 
ATOM   7349 C  CE1 . HIS D 1 117 ? 7.438   2.900   -37.011 1.00 9.51  ? 117 HIS D CE1 1 
ATOM   7350 N  NE2 . HIS D 1 117 ? 6.986   1.728   -36.521 1.00 8.94  ? 117 HIS D NE2 1 
ATOM   7351 N  N   . ILE D 1 118 ? 0.702   2.737   -36.794 1.00 8.94  ? 118 ILE D N   1 
ATOM   7352 C  CA  . ILE D 1 118 ? -0.612  3.427   -36.710 1.00 9.08  ? 118 ILE D CA  1 
ATOM   7353 C  C   . ILE D 1 118 ? -0.483  4.488   -35.637 1.00 8.36  ? 118 ILE D C   1 
ATOM   7354 O  O   . ILE D 1 118 ? -0.369  4.179   -34.436 1.00 8.90  ? 118 ILE D O   1 
ATOM   7355 C  CB  . ILE D 1 118 ? -1.754  2.446   -36.432 1.00 9.71  ? 118 ILE D CB  1 
ATOM   7356 C  CG1 . ILE D 1 118 ? -1.679  1.273   -37.375 1.00 10.53 ? 118 ILE D CG1 1 
ATOM   7357 C  CG2 . ILE D 1 118 ? -3.080  3.168   -36.543 1.00 10.49 ? 118 ILE D CG2 1 
ATOM   7358 C  CD1 . ILE D 1 118 ? -2.770  0.248   -37.030 1.00 9.71  ? 118 ILE D CD1 1 
ATOM   7359 N  N   . VAL D 1 119 ? -0.485  5.802   -36.021 1.00 9.94  ? 119 VAL D N   1 
ATOM   7360 C  CA  . VAL D 1 119 ? -0.224  6.924   -35.082 1.00 10.58 ? 119 VAL D CA  1 
ATOM   7361 C  C   . VAL D 1 119 ? -1.530  7.455   -34.475 1.00 10.50 ? 119 VAL D C   1 
ATOM   7362 O  O   . VAL D 1 119 ? -2.513  7.621   -35.193 1.00 10.70 ? 119 VAL D O   1 
ATOM   7363 C  CB  . VAL D 1 119 ? 0.456   8.073   -35.873 1.00 10.25 ? 119 VAL D CB  1 
ATOM   7364 C  CG1 . VAL D 1 119 ? 0.840   9.209   -34.928 1.00 9.51  ? 119 VAL D CG1 1 
ATOM   7365 C  CG2 . VAL D 1 119 ? 1.744   7.527   -36.569 1.00 9.54  ? 119 VAL D CG2 1 
ATOM   7366 N  N   . HIS D 1 120 ? -1.506  7.574   -33.142 1.00 10.68 ? 120 HIS D N   1 
ATOM   7367 C  CA  . HIS D 1 120 ? -2.654  8.097   -32.364 1.00 11.71 ? 120 HIS D CA  1 
ATOM   7368 C  C   . HIS D 1 120 ? -2.205  9.268   -31.530 1.00 11.98 ? 120 HIS D C   1 
ATOM   7369 O  O   . HIS D 1 120 ? -1.004  9.390   -31.168 1.00 12.54 ? 120 HIS D O   1 
ATOM   7370 C  CB  . HIS D 1 120 ? -3.244  6.999   -31.433 1.00 12.16 ? 120 HIS D CB  1 
ATOM   7371 C  CG  . HIS D 1 120 ? -3.675  5.746   -32.136 1.00 11.90 ? 120 HIS D CG  1 
ATOM   7372 N  ND1 . HIS D 1 120 ? -2.779  4.781   -32.601 1.00 11.70 ? 120 HIS D ND1 1 
ATOM   7373 C  CD2 . HIS D 1 120 ? -4.953  5.218   -32.295 1.00 12.21 ? 120 HIS D CD2 1 
ATOM   7374 C  CE1 . HIS D 1 120 ? -3.504  3.704   -33.089 1.00 11.73 ? 120 HIS D CE1 1 
ATOM   7375 N  NE2 . HIS D 1 120 ? -4.838  3.972   -32.913 1.00 11.68 ? 120 HIS D NE2 1 
ATOM   7376 N  N   . TYR D 1 121 ? -3.147  10.148  -31.161 1.00 12.60 ? 121 TYR D N   1 
ATOM   7377 C  CA  . TYR D 1 121 ? -2.789  11.246  -30.305 1.00 12.14 ? 121 TYR D CA  1 
ATOM   7378 C  C   . TYR D 1 121 ? -3.734  11.258  -29.077 1.00 12.42 ? 121 TYR D C   1 
ATOM   7379 O  O   . TYR D 1 121 ? -4.868  10.725  -29.124 1.00 12.85 ? 121 TYR D O   1 
ATOM   7380 C  CB  . TYR D 1 121 ? -2.873  12.601  -31.069 1.00 11.73 ? 121 TYR D CB  1 
ATOM   7381 C  CG  . TYR D 1 121 ? -4.267  13.060  -31.400 1.00 13.22 ? 121 TYR D CG  1 
ATOM   7382 C  CD1 . TYR D 1 121 ? -4.866  14.038  -30.592 1.00 14.28 ? 121 TYR D CD1 1 
ATOM   7383 C  CD2 . TYR D 1 121 ? -4.990  12.532  -32.497 1.00 13.58 ? 121 TYR D CD2 1 
ATOM   7384 C  CE1 . TYR D 1 121 ? -6.167  14.445  -30.853 1.00 14.48 ? 121 TYR D CE1 1 
ATOM   7385 C  CE2 . TYR D 1 121 ? -6.295  12.933  -32.760 1.00 13.79 ? 121 TYR D CE2 1 
ATOM   7386 C  CZ  . TYR D 1 121 ? -6.848  13.884  -31.898 1.00 14.71 ? 121 TYR D CZ  1 
ATOM   7387 O  OH  . TYR D 1 121 ? -8.131  14.373  -32.150 1.00 19.39 ? 121 TYR D OH  1 
ATOM   7388 N  N   . ASN D 1 122 ? -3.247  11.925  -28.047 1.00 12.73 ? 122 ASN D N   1 
ATOM   7389 C  CA  . ASN D 1 122 ? -3.954  12.012  -26.765 1.00 13.40 ? 122 ASN D CA  1 
ATOM   7390 C  C   . ASN D 1 122 ? -5.060  13.044  -26.850 1.00 13.37 ? 122 ASN D C   1 
ATOM   7391 O  O   . ASN D 1 122 ? -4.817  14.265  -26.636 1.00 14.65 ? 122 ASN D O   1 
ATOM   7392 C  CB  . ASN D 1 122 ? -2.981  12.327  -25.663 1.00 13.04 ? 122 ASN D CB  1 
ATOM   7393 C  CG  . ASN D 1 122 ? -3.601  12.148  -24.267 1.00 14.13 ? 122 ASN D CG  1 
ATOM   7394 O  OD1 . ASN D 1 122 ? -4.805  12.324  -24.100 1.00 13.61 ? 122 ASN D OD1 1 
ATOM   7395 N  ND2 . ASN D 1 122 ? -2.759  11.857  -23.263 1.00 12.80 ? 122 ASN D ND2 1 
ATOM   7396 N  N   . SER D 1 123 ? -6.238  12.521  -27.111 1.00 13.21 ? 123 SER D N   1 
ATOM   7397 C  CA  . SER D 1 123 ? -7.415  13.407  -27.350 1.00 13.94 ? 123 SER D CA  1 
ATOM   7398 C  C   . SER D 1 123 ? -8.085  13.792  -26.064 1.00 13.24 ? 123 SER D C   1 
ATOM   7399 O  O   . SER D 1 123 ? -8.939  14.691  -26.057 1.00 15.49 ? 123 SER D O   1 
ATOM   7400 C  CB  . SER D 1 123 ? -8.388  12.814  -28.358 1.00 15.42 ? 123 SER D CB  1 
ATOM   7401 O  OG  . SER D 1 123 ? -8.763  11.437  -28.020 1.00 16.90 ? 123 SER D OG  1 
ATOM   7402 N  N   . ASP D 1 124 ? -7.682  13.196  -24.957 1.00 13.68 ? 124 ASP D N   1 
ATOM   7403 C  CA  . ASP D 1 124 ? -8.114  13.683  -23.654 1.00 14.94 ? 124 ASP D CA  1 
ATOM   7404 C  C   . ASP D 1 124 ? -7.443  15.027  -23.289 1.00 17.68 ? 124 ASP D C   1 
ATOM   7405 O  O   . ASP D 1 124 ? -8.012  15.875  -22.547 1.00 21.06 ? 124 ASP D O   1 
ATOM   7406 C  CB  . ASP D 1 124 ? -7.805  12.682  -22.564 1.00 15.30 ? 124 ASP D CB  1 
ATOM   7407 C  CG  . ASP D 1 124 ? -8.742  11.454  -22.595 1.00 14.07 ? 124 ASP D CG  1 
ATOM   7408 O  OD1 . ASP D 1 124 ? -9.790  11.482  -23.288 1.00 15.67 ? 124 ASP D OD1 1 
ATOM   7409 O  OD2 . ASP D 1 124 ? -8.402  10.422  -21.914 1.00 16.25 ? 124 ASP D OD2 1 
ATOM   7410 N  N   . LEU D 1 125 ? -6.248  15.224  -23.790 1.00 15.89 ? 125 LEU D N   1 
ATOM   7411 C  CA  . LEU D 1 125 ? -5.419  16.348  -23.392 1.00 16.34 ? 125 LEU D CA  1 
ATOM   7412 C  C   . LEU D 1 125 ? -5.325  17.391  -24.483 1.00 17.52 ? 125 LEU D C   1 
ATOM   7413 O  O   . LEU D 1 125 ? -5.174  18.586  -24.157 1.00 17.35 ? 125 LEU D O   1 
ATOM   7414 C  CB  . LEU D 1 125 ? -4.008  15.866  -22.987 1.00 15.30 ? 125 LEU D CB  1 
ATOM   7415 C  CG  . LEU D 1 125 ? -3.734  15.465  -21.537 1.00 15.30 ? 125 LEU D CG  1 
ATOM   7416 C  CD1 . LEU D 1 125 ? -4.555  14.212  -21.203 1.00 18.11 ? 125 LEU D CD1 1 
ATOM   7417 C  CD2 . LEU D 1 125 ? -2.265  15.156  -21.480 1.00 16.68 ? 125 LEU D CD2 1 
ATOM   7418 N  N   . TYR D 1 126 ? -5.328  16.945  -25.740 1.00 15.10 ? 126 TYR D N   1 
ATOM   7419 C  CA  . TYR D 1 126 ? -5.060  17.786  -26.881 1.00 15.22 ? 126 TYR D CA  1 
ATOM   7420 C  C   . TYR D 1 126 ? -6.137  17.810  -27.926 1.00 16.06 ? 126 TYR D C   1 
ATOM   7421 O  O   . TYR D 1 126 ? -6.840  16.819  -28.165 1.00 15.47 ? 126 TYR D O   1 
ATOM   7422 C  CB  . TYR D 1 126 ? -3.668  17.437  -27.513 1.00 15.49 ? 126 TYR D CB  1 
ATOM   7423 C  CG  . TYR D 1 126 ? -2.599  17.392  -26.428 1.00 14.80 ? 126 TYR D CG  1 
ATOM   7424 C  CD1 . TYR D 1 126 ? -2.216  18.545  -25.749 1.00 15.71 ? 126 TYR D CD1 1 
ATOM   7425 C  CD2 . TYR D 1 126 ? -2.025  16.188  -26.040 1.00 13.93 ? 126 TYR D CD2 1 
ATOM   7426 C  CE1 . TYR D 1 126 ? -1.268  18.500  -24.741 1.00 14.09 ? 126 TYR D CE1 1 
ATOM   7427 C  CE2 . TYR D 1 126 ? -1.080  16.136  -25.028 1.00 15.01 ? 126 TYR D CE2 1 
ATOM   7428 C  CZ  . TYR D 1 126 ? -0.701  17.294  -24.378 1.00 13.84 ? 126 TYR D CZ  1 
ATOM   7429 O  OH  . TYR D 1 126 ? 0.242   17.257  -23.363 1.00 15.11 ? 126 TYR D OH  1 
ATOM   7430 N  N   . PRO D 1 127 ? -6.283  18.980  -28.612 1.00 17.58 ? 127 PRO D N   1 
ATOM   7431 C  CA  . PRO D 1 127 ? -7.350  19.155  -29.607 1.00 17.66 ? 127 PRO D CA  1 
ATOM   7432 C  C   . PRO D 1 127 ? -7.118  18.545  -30.979 1.00 17.13 ? 127 PRO D C   1 
ATOM   7433 O  O   . PRO D 1 127 ? -8.067  18.372  -31.763 1.00 20.43 ? 127 PRO D O   1 
ATOM   7434 C  CB  . PRO D 1 127 ? -7.414  20.695  -29.726 1.00 18.01 ? 127 PRO D CB  1 
ATOM   7435 C  CG  . PRO D 1 127 ? -6.018  21.151  -29.461 1.00 16.91 ? 127 PRO D CG  1 
ATOM   7436 C  CD  . PRO D 1 127 ? -5.592  20.256  -28.294 1.00 19.26 ? 127 PRO D CD  1 
ATOM   7437 N  N   . ASP D 1 128 ? -5.858  18.182  -31.262 1.00 15.77 ? 128 ASP D N   1 
ATOM   7438 C  CA  . ASP D 1 128 ? -5.501  17.654  -32.515 1.00 15.54 ? 128 ASP D CA  1 
ATOM   7439 C  C   . ASP D 1 128 ? -4.077  17.105  -32.406 1.00 15.95 ? 128 ASP D C   1 
ATOM   7440 O  O   . ASP D 1 128 ? -3.325  17.363  -31.460 1.00 16.86 ? 128 ASP D O   1 
ATOM   7441 C  CB  . ASP D 1 128 ? -5.549  18.739  -33.594 1.00 18.25 ? 128 ASP D CB  1 
ATOM   7442 C  CG  . ASP D 1 128 ? -4.591  19.868  -33.296 1.00 20.74 ? 128 ASP D CG  1 
ATOM   7443 O  OD1 . ASP D 1 128 ? -4.980  20.898  -32.594 1.00 21.58 ? 128 ASP D OD1 1 
ATOM   7444 O  OD2 . ASP D 1 128 ? -3.454  19.784  -33.772 1.00 20.09 ? 128 ASP D OD2 1 
ATOM   7445 N  N   . ALA D 1 129 ? -3.732  16.297  -33.396 1.00 15.05 ? 129 ALA D N   1 
ATOM   7446 C  CA  . ALA D 1 129 ? -2.475  15.551  -33.395 1.00 13.84 ? 129 ALA D CA  1 
ATOM   7447 C  C   . ALA D 1 129 ? -1.206  16.396  -33.462 1.00 14.10 ? 129 ALA D C   1 
ATOM   7448 O  O   . ALA D 1 129 ? -0.186  16.113  -32.783 1.00 14.07 ? 129 ALA D O   1 
ATOM   7449 C  CB  . ALA D 1 129 ? -2.499  14.564  -34.544 1.00 17.41 ? 129 ALA D CB  1 
ATOM   7450 N  N   A SER D 1 130 ? -1.240  17.400  -34.341 0.50 14.38 ? 130 SER D N   1 
ATOM   7451 N  N   B SER D 1 130 ? -1.238  17.421  -34.315 0.50 14.15 ? 130 SER D N   1 
ATOM   7452 C  CA  A SER D 1 130 ? -0.137  18.363  -34.417 0.50 13.59 ? 130 SER D CA  1 
ATOM   7453 C  CA  B SER D 1 130 ? -0.084  18.328  -34.392 0.50 13.10 ? 130 SER D CA  1 
ATOM   7454 C  C   A SER D 1 130 ? 0.140   18.981  -33.033 0.50 13.28 ? 130 SER D C   1 
ATOM   7455 C  C   B SER D 1 130 ? 0.178   19.075  -33.062 0.50 12.96 ? 130 SER D C   1 
ATOM   7456 O  O   A SER D 1 130 ? 1.247   18.904  -32.509 0.50 14.41 ? 130 SER D O   1 
ATOM   7457 O  O   B SER D 1 130 ? 1.332   19.237  -32.631 0.50 13.73 ? 130 SER D O   1 
ATOM   7458 C  CB  A SER D 1 130 ? -0.510  19.431  -35.445 0.50 14.62 ? 130 SER D CB  1 
ATOM   7459 C  CB  B SER D 1 130 ? -0.290  19.330  -35.519 0.50 14.03 ? 130 SER D CB  1 
ATOM   7460 O  OG  A SER D 1 130 ? -0.543  18.849  -36.734 0.50 16.38 ? 130 SER D OG  1 
ATOM   7461 O  OG  B SER D 1 130 ? 0.854   20.130  -35.568 0.50 14.97 ? 130 SER D OG  1 
ATOM   7462 N  N   . THR D 1 131 ? -0.883  19.560  -32.431 1.00 13.27 ? 131 THR D N   1 
ATOM   7463 C  CA  . THR D 1 131 ? -0.746  20.127  -31.072 1.00 13.13 ? 131 THR D CA  1 
ATOM   7464 C  C   . THR D 1 131 ? -0.147  19.145  -30.059 1.00 14.62 ? 131 THR D C   1 
ATOM   7465 O  O   . THR D 1 131 ? 0.758   19.471  -29.245 1.00 14.16 ? 131 THR D O   1 
ATOM   7466 C  CB  . THR D 1 131 ? -2.096  20.734  -30.613 1.00 15.85 ? 131 THR D CB  1 
ATOM   7467 O  OG1 . THR D 1 131 ? -2.510  21.723  -31.566 1.00 16.43 ? 131 THR D OG1 1 
ATOM   7468 C  CG2 . THR D 1 131 ? -2.066  21.326  -29.140 1.00 15.54 ? 131 THR D CG2 1 
ATOM   7469 N  N   . ALA D 1 132 ? -0.593  17.884  -30.156 1.00 13.19 ? 132 ALA D N   1 
ATOM   7470 C  CA  . ALA D 1 132 ? -0.209  16.811  -29.244 1.00 14.99 ? 132 ALA D CA  1 
ATOM   7471 C  C   . ALA D 1 132 ? 1.218   16.374  -29.436 1.00 14.79 ? 132 ALA D C   1 
ATOM   7472 O  O   . ALA D 1 132 ? 1.870   16.013  -28.489 1.00 13.29 ? 132 ALA D O   1 
ATOM   7473 C  CB  . ALA D 1 132 ? -1.099  15.608  -29.457 1.00 15.45 ? 132 ALA D CB  1 
ATOM   7474 N  N   . SER D 1 133 ? 1.724   16.515  -30.663 1.00 14.91 ? 133 SER D N   1 
ATOM   7475 C  CA  . SER D 1 133 ? 2.953   15.820  -31.050 1.00 13.00 ? 133 SER D CA  1 
ATOM   7476 C  C   . SER D 1 133 ? 4.210   16.233  -30.297 1.00 15.53 ? 133 SER D C   1 
ATOM   7477 O  O   . SER D 1 133 ? 5.191   15.463  -30.223 1.00 14.83 ? 133 SER D O   1 
ATOM   7478 C  CB  . SER D 1 133 ? 3.151   15.926  -32.565 1.00 16.25 ? 133 SER D CB  1 
ATOM   7479 O  OG  . SER D 1 133 ? 3.499   17.284  -32.933 1.00 15.99 ? 133 SER D OG  1 
ATOM   7480 N  N   . ASN D 1 134 ? 4.261   17.488  -29.816 1.00 15.29 ? 134 ASN D N   1 
ATOM   7481 C  CA  . ASN D 1 134 ? 5.433   17.953  -29.053 1.00 16.66 ? 134 ASN D CA  1 
ATOM   7482 C  C   . ASN D 1 134 ? 5.206   18.133  -27.542 1.00 16.74 ? 134 ASN D C   1 
ATOM   7483 O  O   . ASN D 1 134 ? 5.990   18.753  -26.805 1.00 17.01 ? 134 ASN D O   1 
ATOM   7484 C  CB  . ASN D 1 134 ? 6.075   19.219  -29.647 1.00 19.19 ? 134 ASN D CB  1 
ATOM   7485 C  CG  . ASN D 1 134 ? 5.182   20.440  -29.511 1.00 20.33 ? 134 ASN D CG  1 
ATOM   7486 O  OD1 . ASN D 1 134 ? 3.961   20.331  -29.459 1.00 21.26 ? 134 ASN D OD1 1 
ATOM   7487 N  ND2 . ASN D 1 134 ? 5.803   21.651  -29.468 1.00 22.40 ? 134 ASN D ND2 1 
ATOM   7488 N  N   . LYS D 1 135 ? 4.141   17.508  -27.086 1.00 15.53 ? 135 LYS D N   1 
ATOM   7489 C  CA  . LYS D 1 135 ? 3.667   17.731  -25.711 1.00 13.87 ? 135 LYS D CA  1 
ATOM   7490 C  C   . LYS D 1 135 ? 3.631   16.435  -24.945 1.00 14.24 ? 135 LYS D C   1 
ATOM   7491 O  O   . LYS D 1 135 ? 3.587   15.326  -25.503 1.00 14.41 ? 135 LYS D O   1 
ATOM   7492 C  CB  . LYS D 1 135 ? 2.295   18.435  -25.748 1.00 13.90 ? 135 LYS D CB  1 
ATOM   7493 C  CG  . LYS D 1 135 ? 2.532   19.874  -26.235 1.00 15.09 ? 135 LYS D CG  1 
ATOM   7494 C  CD  . LYS D 1 135 ? 1.283   20.734  -26.217 1.00 18.63 ? 135 LYS D CD  1 
ATOM   7495 C  CE  . LYS D 1 135 ? 1.527   22.025  -27.023 1.00 16.76 ? 135 LYS D CE  1 
ATOM   7496 N  NZ  . LYS D 1 135 ? 1.634   21.963  -28.547 1.00 18.12 ? 135 LYS D NZ  1 
ATOM   7497 N  N   . SER D 1 136 ? 3.647   16.620  -23.623 1.00 15.27 ? 136 SER D N   1 
ATOM   7498 C  CA  . SER D 1 136 ? 3.704   15.477  -22.683 1.00 14.82 ? 136 SER D CA  1 
ATOM   7499 C  C   . SER D 1 136 ? 2.585   14.481  -22.945 1.00 13.57 ? 136 SER D C   1 
ATOM   7500 O  O   . SER D 1 136 ? 1.404   14.852  -23.070 1.00 14.62 ? 136 SER D O   1 
ATOM   7501 C  CB  . SER D 1 136 ? 3.522   16.057  -21.271 1.00 17.37 ? 136 SER D CB  1 
ATOM   7502 O  OG  . SER D 1 136 ? 3.785   15.025  -20.350 1.00 19.30 ? 136 SER D OG  1 
ATOM   7503 N  N   . GLU D 1 137 ? 2.975   13.191  -22.996 1.00 13.10 ? 137 GLU D N   1 
ATOM   7504 C  CA  . GLU D 1 137 ? 2.000   12.138  -23.229 1.00 14.51 ? 137 GLU D CA  1 
ATOM   7505 C  C   . GLU D 1 137 ? 1.221   12.294  -24.547 1.00 13.61 ? 137 GLU D C   1 
ATOM   7506 O  O   . GLU D 1 137 ? 0.096   11.837  -24.653 1.00 14.00 ? 137 GLU D O   1 
ATOM   7507 C  CB  . GLU D 1 137 ? 1.032   11.924  -22.039 1.00 14.99 ? 137 GLU D CB  1 
ATOM   7508 C  CG  . GLU D 1 137 ? 1.644   11.924  -20.636 1.00 19.05 ? 137 GLU D CG  1 
ATOM   7509 C  CD  . GLU D 1 137 ? 2.555   10.738  -20.362 1.00 25.29 ? 137 GLU D CD  1 
ATOM   7510 O  OE1 . GLU D 1 137 ? 2.263   9.636   -20.886 1.00 27.28 ? 137 GLU D OE1 1 
ATOM   7511 O  OE2 . GLU D 1 137 ? 3.572   10.909  -19.628 1.00 32.27 ? 137 GLU D OE2 1 
ATOM   7512 N  N   . GLY D 1 138 ? 1.768   12.963  -25.544 1.00 12.73 ? 138 GLY D N   1 
ATOM   7513 C  CA  . GLY D 1 138 ? 0.976   13.359  -26.669 1.00 13.33 ? 138 GLY D CA  1 
ATOM   7514 C  C   . GLY D 1 138 ? 0.560   12.220  -27.616 1.00 11.96 ? 138 GLY D C   1 
ATOM   7515 O  O   . GLY D 1 138 ? -0.489  12.311  -28.254 1.00 13.30 ? 138 GLY D O   1 
ATOM   7516 N  N   . LEU D 1 139 ? 1.417   11.212  -27.774 1.00 10.92 ? 139 LEU D N   1 
ATOM   7517 C  CA  . LEU D 1 139 ? 1.188   10.292  -28.929 1.00 11.35 ? 139 LEU D CA  1 
ATOM   7518 C  C   . LEU D 1 139 ? 1.323   8.816   -28.459 1.00 11.48 ? 139 LEU D C   1 
ATOM   7519 O  O   . LEU D 1 139 ? 2.046   8.522   -27.510 1.00 10.54 ? 139 LEU D O   1 
ATOM   7520 C  CB  . LEU D 1 139 ? 2.234   10.533  -30.082 1.00 11.48 ? 139 LEU D CB  1 
ATOM   7521 C  CG  . LEU D 1 139 ? 2.226   11.954  -30.708 1.00 11.95 ? 139 LEU D CG  1 
ATOM   7522 C  CD1 . LEU D 1 139 ? 3.403   12.070  -31.649 1.00 13.48 ? 139 LEU D CD1 1 
ATOM   7523 C  CD2 . LEU D 1 139 ? 0.909   12.273  -31.524 1.00 13.07 ? 139 LEU D CD2 1 
ATOM   7524 N  N   . ALA D 1 140 ? 0.592   7.934   -29.119 1.00 11.42 ? 140 ALA D N   1 
ATOM   7525 C  CA  . ALA D 1 140 ? 0.807   6.458   -28.930 1.00 10.22 ? 140 ALA D CA  1 
ATOM   7526 C  C   . ALA D 1 140 ? 0.838   5.898   -30.343 1.00 10.23 ? 140 ALA D C   1 
ATOM   7527 O  O   . ALA D 1 140 ? -0.081  6.140   -31.129 1.00 10.89 ? 140 ALA D O   1 
ATOM   7528 C  CB  . ALA D 1 140 ? -0.285  5.866   -28.119 1.00 10.99 ? 140 ALA D CB  1 
ATOM   7529 N  N   . VAL D 1 141 ? 1.876   5.064   -30.640 1.00 9.12  ? 141 VAL D N   1 
ATOM   7530 C  CA  . VAL D 1 141 ? 1.971   4.443   -31.981 1.00 9.48  ? 141 VAL D CA  1 
ATOM   7531 C  C   . VAL D 1 141 ? 1.894   2.936   -31.786 1.00 10.95 ? 141 VAL D C   1 
ATOM   7532 O  O   . VAL D 1 141 ? 2.509   2.415   -30.853 1.00 11.57 ? 141 VAL D O   1 
ATOM   7533 C  CB  . VAL D 1 141 ? 3.297   4.842   -32.654 1.00 8.59  ? 141 VAL D CB  1 
ATOM   7534 C  CG1 . VAL D 1 141 ? 3.320   4.303   -34.113 1.00 9.77  ? 141 VAL D CG1 1 
ATOM   7535 C  CG2 . VAL D 1 141 ? 3.317   6.372   -32.801 1.00 9.16  ? 141 VAL D CG2 1 
ATOM   7536 N  N   . LEU D 1 142 ? 1.133   2.307   -32.637 1.00 9.59  ? 142 LEU D N   1 
ATOM   7537 C  CA  . LEU D 1 142 ? 1.127   0.854   -32.697 1.00 9.38  ? 142 LEU D CA  1 
ATOM   7538 C  C   . LEU D 1 142 ? 2.013   0.445   -33.837 1.00 10.41 ? 142 LEU D C   1 
ATOM   7539 O  O   . LEU D 1 142 ? 1.857   0.965   -34.944 1.00 11.79 ? 142 LEU D O   1 
ATOM   7540 C  CB  . LEU D 1 142 ? -0.296  0.379   -33.008 1.00 11.31 ? 142 LEU D CB  1 
ATOM   7541 C  CG  . LEU D 1 142 ? -1.403  0.716   -32.025 1.00 10.81 ? 142 LEU D CG  1 
ATOM   7542 C  CD1 . LEU D 1 142 ? -2.689  -0.076  -32.469 1.00 11.65 ? 142 LEU D CD1 1 
ATOM   7543 C  CD2 . LEU D 1 142 ? -1.014  0.542   -30.516 1.00 12.66 ? 142 LEU D CD2 1 
ATOM   7544 N  N   . ALA D 1 143 ? 2.915   -0.523  -33.568 1.00 10.59 ? 143 ALA D N   1 
ATOM   7545 C  CA  . ALA D 1 143 ? 3.897   -1.011  -34.581 1.00 10.34 ? 143 ALA D CA  1 
ATOM   7546 C  C   . ALA D 1 143 ? 3.653   -2.491  -34.884 1.00 10.05 ? 143 ALA D C   1 
ATOM   7547 O  O   . ALA D 1 143 ? 3.564   -3.353  -34.005 1.00 9.81  ? 143 ALA D O   1 
ATOM   7548 C  CB  . ALA D 1 143 ? 5.317   -0.806  -34.123 1.00 10.44 ? 143 ALA D CB  1 
ATOM   7549 N  N   . VAL D 1 144 ? 3.515   -2.729  -36.170 1.00 9.75  ? 144 VAL D N   1 
ATOM   7550 C  CA  . VAL D 1 144 ? 3.383   -4.128  -36.655 1.00 9.78  ? 144 VAL D CA  1 
ATOM   7551 C  C   . VAL D 1 144 ? 4.653   -4.462  -37.451 1.00 10.13 ? 144 VAL D C   1 
ATOM   7552 O  O   . VAL D 1 144 ? 4.927   -3.839  -38.461 1.00 11.25 ? 144 VAL D O   1 
ATOM   7553 C  CB  . VAL D 1 144 ? 2.138   -4.312  -37.515 1.00 9.30  ? 144 VAL D CB  1 
ATOM   7554 C  CG1 . VAL D 1 144 ? 1.987   -5.788  -37.968 1.00 10.64 ? 144 VAL D CG1 1 
ATOM   7555 C  CG2 . VAL D 1 144 ? 0.939   -3.844  -36.689 1.00 11.42 ? 144 VAL D CG2 1 
ATOM   7556 N  N   . LEU D 1 145 ? 5.379   -5.518  -37.053 1.00 10.52 ? 145 LEU D N   1 
ATOM   7557 C  CA  . LEU D 1 145 ? 6.529   -5.902  -37.827 1.00 10.80 ? 145 LEU D CA  1 
ATOM   7558 C  C   . LEU D 1 145 ? 6.058   -6.713  -39.018 1.00 11.22 ? 145 LEU D C   1 
ATOM   7559 O  O   . LEU D 1 145 ? 5.105   -7.527  -38.895 1.00 10.09 ? 145 LEU D O   1 
ATOM   7560 C  CB  . LEU D 1 145 ? 7.418   -6.764  -36.963 1.00 12.53 ? 145 LEU D CB  1 
ATOM   7561 C  CG  . LEU D 1 145 ? 7.986   -6.115  -35.736 1.00 13.24 ? 145 LEU D CG  1 
ATOM   7562 C  CD1 . LEU D 1 145 ? 8.474   -7.143  -34.680 1.00 13.98 ? 145 LEU D CD1 1 
ATOM   7563 C  CD2 . LEU D 1 145 ? 9.133   -5.198  -36.228 1.00 16.25 ? 145 LEU D CD2 1 
ATOM   7564 N  N   . ILE D 1 146 ? 6.690   -6.485  -40.166 1.00 10.00 ? 146 ILE D N   1 
ATOM   7565 C  CA  . ILE D 1 146 ? 6.269   -7.107  -41.469 1.00 10.70 ? 146 ILE D CA  1 
ATOM   7566 C  C   . ILE D 1 146 ? 7.358   -8.020  -42.017 1.00 10.53 ? 146 ILE D C   1 
ATOM   7567 O  O   . ILE D 1 146 ? 8.442   -7.558  -42.231 1.00 10.77 ? 146 ILE D O   1 
ATOM   7568 C  CB  . ILE D 1 146 ? 5.846   -6.092  -42.543 1.00 11.18 ? 146 ILE D CB  1 
ATOM   7569 C  CG1 . ILE D 1 146 ? 4.614   -5.279  -42.084 1.00 12.74 ? 146 ILE D CG1 1 
ATOM   7570 C  CG2 . ILE D 1 146 ? 5.483   -6.751  -43.865 1.00 11.46 ? 146 ILE D CG2 1 
ATOM   7571 C  CD1 . ILE D 1 146 ? 4.409   -4.012  -42.903 1.00 10.93 ? 146 ILE D CD1 1 
ATOM   7572 N  N   A GLU D 1 147 ? 7.087   -9.328  -42.129 0.50 10.78 ? 147 GLU D N   1 
ATOM   7573 N  N   B GLU D 1 147 ? 7.012   -9.312  -42.176 0.50 10.09 ? 147 GLU D N   1 
ATOM   7574 C  CA  A GLU D 1 147 ? 8.090   -10.266 -42.647 0.50 12.40 ? 147 GLU D CA  1 
ATOM   7575 C  CA  B GLU D 1 147 ? 7.916   -10.340 -42.686 0.50 11.37 ? 147 GLU D CA  1 
ATOM   7576 C  C   A GLU D 1 147 ? 7.653   -10.692 -44.060 0.50 11.79 ? 147 GLU D C   1 
ATOM   7577 C  C   B GLU D 1 147 ? 7.591   -10.614 -44.163 0.50 11.05 ? 147 GLU D C   1 
ATOM   7578 O  O   A GLU D 1 147 ? 6.469   -10.817 -44.331 0.50 11.37 ? 147 GLU D O   1 
ATOM   7579 O  O   B GLU D 1 147 ? 6.423   -10.567 -44.588 0.50 10.86 ? 147 GLU D O   1 
ATOM   7580 C  CB  A GLU D 1 147 ? 8.191   -11.488 -41.735 0.50 13.84 ? 147 GLU D CB  1 
ATOM   7581 C  CB  B GLU D 1 147 ? 7.716   -11.642 -41.895 0.50 10.81 ? 147 GLU D CB  1 
ATOM   7582 C  CG  A GLU D 1 147 ? 7.533   -12.774 -42.210 0.50 16.88 ? 147 GLU D CG  1 
ATOM   7583 C  CG  B GLU D 1 147 ? 8.699   -12.770 -42.287 0.50 12.06 ? 147 GLU D CG  1 
ATOM   7584 C  CD  A GLU D 1 147 ? 7.420   -13.801 -41.073 0.50 16.34 ? 147 GLU D CD  1 
ATOM   7585 C  CD  B GLU D 1 147 ? 8.993   -13.771 -41.150 0.50 14.84 ? 147 GLU D CD  1 
ATOM   7586 O  OE1 A GLU D 1 147 ? 7.983   -13.571 -40.007 0.50 16.59 ? 147 GLU D OE1 1 
ATOM   7587 O  OE1 B GLU D 1 147 ? 8.778   -13.429 -39.957 0.50 17.39 ? 147 GLU D OE1 1 
ATOM   7588 O  OE2 A GLU D 1 147 ? 6.712   -14.800 -41.223 0.50 21.42 ? 147 GLU D OE2 1 
ATOM   7589 O  OE2 B GLU D 1 147 ? 9.478   -14.908 -41.421 0.50 17.42 ? 147 GLU D OE2 1 
ATOM   7590 N  N   . MET D 1 148 ? 8.625   -10.927 -44.952 1.00 11.92 ? 148 MET D N   1 
ATOM   7591 C  CA  . MET D 1 148 ? 8.391   -11.424 -46.302 1.00 11.50 ? 148 MET D CA  1 
ATOM   7592 C  C   . MET D 1 148 ? 7.827   -12.833 -46.240 1.00 11.17 ? 148 MET D C   1 
ATOM   7593 O  O   . MET D 1 148 ? 8.374   -13.734 -45.540 1.00 12.73 ? 148 MET D O   1 
ATOM   7594 C  CB  . MET D 1 148 ? 9.686   -11.499 -47.128 1.00 12.04 ? 148 MET D CB  1 
ATOM   7595 C  CG  . MET D 1 148 ? 9.443   -11.943 -48.562 1.00 14.39 ? 148 MET D CG  1 
ATOM   7596 S  SD  . MET D 1 148 ? 11.040  -11.967 -49.511 1.00 16.06 ? 148 MET D SD  1 
ATOM   7597 C  CE  . MET D 1 148 ? 11.514  -10.190 -49.515 1.00 14.13 ? 148 MET D CE  1 
ATOM   7598 N  N   . GLY D 1 149 ? 6.631   -12.958 -46.793 1.00 10.14 ? 149 GLY D N   1 
ATOM   7599 C  CA  . GLY D 1 149 ? 5.914   -14.294 -46.779 1.00 11.72 ? 149 GLY D CA  1 
ATOM   7600 C  C   . GLY D 1 149 ? 4.799   -14.388 -47.787 1.00 9.51  ? 149 GLY D C   1 
ATOM   7601 O  O   . GLY D 1 149 ? 4.954   -14.164 -48.987 1.00 11.77 ? 149 GLY D O   1 
ATOM   7602 N  N   . SER D 1 150 ? 3.590   -14.694 -47.283 1.00 11.82 ? 150 SER D N   1 
ATOM   7603 C  CA  . SER D 1 150 ? 2.414   -14.859 -48.159 1.00 11.64 ? 150 SER D CA  1 
ATOM   7604 C  C   . SER D 1 150 ? 1.826   -13.510 -48.546 1.00 11.94 ? 150 SER D C   1 
ATOM   7605 O  O   . SER D 1 150 ? 1.908   -12.585 -47.758 1.00 13.57 ? 150 SER D O   1 
ATOM   7606 C  CB  . SER D 1 150 ? 1.318   -15.653 -47.482 1.00 13.27 ? 150 SER D CB  1 
ATOM   7607 O  OG  . SER D 1 150 ? 1.734   -17.030 -47.408 1.00 13.39 ? 150 SER D OG  1 
ATOM   7608 N  N   . PHE D 1 151 ? 1.277   -13.463 -49.759 1.00 11.95 ? 151 PHE D N   1 
ATOM   7609 C  CA  . PHE D 1 151 ? 0.435   -12.339 -50.185 1.00 12.23 ? 151 PHE D CA  1 
ATOM   7610 C  C   . PHE D 1 151 ? -0.590  -11.973 -49.145 1.00 13.03 ? 151 PHE D C   1 
ATOM   7611 O  O   . PHE D 1 151 ? -1.298  -12.876 -48.589 1.00 13.49 ? 151 PHE D O   1 
ATOM   7612 C  CB  . PHE D 1 151 ? -0.219  -12.636 -51.517 1.00 12.58 ? 151 PHE D CB  1 
ATOM   7613 C  CG  . PHE D 1 151 ? -1.036  -11.504 -52.048 1.00 13.11 ? 151 PHE D CG  1 
ATOM   7614 C  CD1 . PHE D 1 151 ? -0.420  -10.409 -52.603 1.00 14.00 ? 151 PHE D CD1 1 
ATOM   7615 C  CD2 . PHE D 1 151 ? -2.424  -11.569 -51.950 1.00 15.64 ? 151 PHE D CD2 1 
ATOM   7616 C  CE1 . PHE D 1 151 ? -1.218  -9.363  -53.060 1.00 11.90 ? 151 PHE D CE1 1 
ATOM   7617 C  CE2 . PHE D 1 151 ? -3.204  -10.520 -52.377 1.00 15.56 ? 151 PHE D CE2 1 
ATOM   7618 C  CZ  . PHE D 1 151 ? -2.606  -9.425  -52.939 1.00 13.93 ? 151 PHE D CZ  1 
ATOM   7619 N  N   . ASN D 1 152 ? -0.755  -10.644 -48.916 1.00 11.64 ? 152 ASN D N   1 
ATOM   7620 C  CA  . ASN D 1 152 ? -1.670  -10.176 -47.856 1.00 11.42 ? 152 ASN D CA  1 
ATOM   7621 C  C   . ASN D 1 152 ? -2.716  -9.290  -48.521 1.00 12.14 ? 152 ASN D C   1 
ATOM   7622 O  O   . ASN D 1 152 ? -2.449  -8.123  -48.906 1.00 11.44 ? 152 ASN D O   1 
ATOM   7623 C  CB  . ASN D 1 152 ? -0.865  -9.396  -46.807 1.00 10.42 ? 152 ASN D CB  1 
ATOM   7624 C  CG  . ASN D 1 152 ? -1.677  -9.091  -45.569 1.00 10.79 ? 152 ASN D CG  1 
ATOM   7625 O  OD1 . ASN D 1 152 ? -2.849  -8.516  -45.669 1.00 11.13 ? 152 ASN D OD1 1 
ATOM   7626 N  ND2 . ASN D 1 152 ? -1.128  -9.411  -44.414 1.00 12.03 ? 152 ASN D ND2 1 
ATOM   7627 N  N   . PRO D 1 153 ? -3.965  -9.800  -48.656 1.00 13.03 ? 153 PRO D N   1 
ATOM   7628 C  CA  . PRO D 1 153 ? -4.949  -9.053  -49.391 1.00 13.14 ? 153 PRO D CA  1 
ATOM   7629 C  C   . PRO D 1 153 ? -5.320  -7.715  -48.675 1.00 11.25 ? 153 PRO D C   1 
ATOM   7630 O  O   . PRO D 1 153 ? -5.667  -6.770  -49.312 1.00 15.23 ? 153 PRO D O   1 
ATOM   7631 C  CB  . PRO D 1 153 ? -6.148  -10.011 -49.453 1.00 14.60 ? 153 PRO D CB  1 
ATOM   7632 C  CG  . PRO D 1 153 ? -5.520  -11.365 -49.434 1.00 16.10 ? 153 PRO D CG  1 
ATOM   7633 C  CD  . PRO D 1 153 ? -4.443  -11.173 -48.370 1.00 16.10 ? 153 PRO D CD  1 
ATOM   7634 N  N   . SER D 1 154 ? -5.226  -7.697  -47.347 1.00 11.10 ? 154 SER D N   1 
ATOM   7635 C  CA  . SER D 1 154 ? -5.664  -6.554  -46.562 1.00 13.36 ? 154 SER D CA  1 
ATOM   7636 C  C   . SER D 1 154 ? -4.610  -5.466  -46.762 1.00 12.76 ? 154 SER D C   1 
ATOM   7637 O  O   . SER D 1 154 ? -4.952  -4.273  -46.969 1.00 12.87 ? 154 SER D O   1 
ATOM   7638 C  CB  . SER D 1 154 ? -5.758  -6.936  -45.090 1.00 13.64 ? 154 SER D CB  1 
ATOM   7639 O  OG  . SER D 1 154 ? -6.865  -7.847  -44.933 1.00 17.61 ? 154 SER D OG  1 
ATOM   7640 N  N   . TYR D 1 155 ? -3.294  -5.819  -46.720 1.00 12.32 ? 155 TYR D N   1 
ATOM   7641 C  CA  . TYR D 1 155 ? -2.284  -4.732  -46.944 1.00 10.82 ? 155 TYR D CA  1 
ATOM   7642 C  C   . TYR D 1 155 ? -2.343  -4.256  -48.395 1.00 11.95 ? 155 TYR D C   1 
ATOM   7643 O  O   . TYR D 1 155 ? -2.042  -3.072  -48.722 1.00 13.21 ? 155 TYR D O   1 
ATOM   7644 C  CB  . TYR D 1 155 ? -0.823  -5.209  -46.666 1.00 10.48 ? 155 TYR D CB  1 
ATOM   7645 C  CG  . TYR D 1 155 ? -0.487  -5.081  -45.194 1.00 10.36 ? 155 TYR D CG  1 
ATOM   7646 C  CD1 . TYR D 1 155 ? 0.274   -4.020  -44.721 1.00 11.26 ? 155 TYR D CD1 1 
ATOM   7647 C  CD2 . TYR D 1 155 ? -0.975  -5.998  -44.271 1.00 11.04 ? 155 TYR D CD2 1 
ATOM   7648 C  CE1 . TYR D 1 155 ? 0.564   -3.892  -43.375 1.00 12.17 ? 155 TYR D CE1 1 
ATOM   7649 C  CE2 . TYR D 1 155 ? -0.691  -5.879  -42.924 1.00 10.84 ? 155 TYR D CE2 1 
ATOM   7650 C  CZ  . TYR D 1 155 ? 0.079   -4.825  -42.481 1.00 11.25 ? 155 TYR D CZ  1 
ATOM   7651 O  OH  . TYR D 1 155 ? 0.363   -4.704  -41.139 1.00 11.82 ? 155 TYR D OH  1 
ATOM   7652 N  N   . ASP D 1 156 ? -2.774  -5.127  -49.281 1.00 12.56 ? 156 ASP D N   1 
ATOM   7653 C  CA  . ASP D 1 156 ? -2.908  -4.717  -50.655 1.00 12.80 ? 156 ASP D CA  1 
ATOM   7654 C  C   . ASP D 1 156 ? -4.027  -3.671  -50.892 1.00 13.86 ? 156 ASP D C   1 
ATOM   7655 O  O   . ASP D 1 156 ? -4.011  -2.998  -51.923 1.00 13.31 ? 156 ASP D O   1 
ATOM   7656 C  CB  . ASP D 1 156 ? -3.143  -5.941  -51.601 1.00 14.21 ? 156 ASP D CB  1 
ATOM   7657 C  CG  . ASP D 1 156 ? -2.286  -5.845  -52.852 1.00 15.22 ? 156 ASP D CG  1 
ATOM   7658 O  OD1 . ASP D 1 156 ? -1.015  -5.626  -52.741 1.00 13.83 ? 156 ASP D OD1 1 
ATOM   7659 O  OD2 . ASP D 1 156 ? -2.947  -5.905  -53.947 1.00 18.11 ? 156 ASP D OD2 1 
ATOM   7660 N  N   . LYS D 1 157 ? -4.929  -3.543  -49.918 1.00 14.28 ? 157 LYS D N   1 
ATOM   7661 C  CA  . LYS D 1 157 ? -5.960  -2.480  -50.062 1.00 13.71 ? 157 LYS D CA  1 
ATOM   7662 C  C   . LYS D 1 157 ? -5.279  -1.090  -49.978 1.00 14.26 ? 157 LYS D C   1 
ATOM   7663 O  O   . LYS D 1 157 ? -5.762  -0.130  -50.559 1.00 18.62 ? 157 LYS D O   1 
ATOM   7664 C  CB  . LYS D 1 157 ? -7.098  -2.624  -49.036 1.00 14.59 ? 157 LYS D CB  1 
ATOM   7665 C  CG  . LYS D 1 157 ? -7.898  -3.923  -49.224 1.00 14.94 ? 157 LYS D CG  1 
ATOM   7666 C  CD  . LYS D 1 157 ? -8.640  -4.233  -47.892 1.00 17.22 ? 157 LYS D CD  1 
ATOM   7667 C  CE  . LYS D 1 157 ? -9.467  -5.520  -48.081 1.00 23.21 ? 157 LYS D CE  1 
ATOM   7668 N  NZ  . LYS D 1 157 ? -10.256 -6.063  -46.918 1.00 25.14 ? 157 LYS D NZ  1 
ATOM   7669 N  N   . ILE D 1 158 ? -4.090  -1.040  -49.401 1.00 13.19 ? 158 ILE D N   1 
ATOM   7670 C  CA  . ILE D 1 158 ? -3.307  0.221   -49.423 1.00 13.66 ? 158 ILE D CA  1 
ATOM   7671 C  C   . ILE D 1 158 ? -2.400  0.160   -50.625 1.00 13.31 ? 158 ILE D C   1 
ATOM   7672 O  O   . ILE D 1 158 ? -2.345  1.082   -51.410 1.00 15.23 ? 158 ILE D O   1 
ATOM   7673 C  CB  . ILE D 1 158 ? -2.445  0.338   -48.158 1.00 14.36 ? 158 ILE D CB  1 
ATOM   7674 C  CG1 . ILE D 1 158 ? -3.345  0.504   -46.926 1.00 13.70 ? 158 ILE D CG1 1 
ATOM   7675 C  CG2 . ILE D 1 158 ? -1.368  1.433   -48.302 1.00 15.09 ? 158 ILE D CG2 1 
ATOM   7676 C  CD1 . ILE D 1 158 ? -2.640  0.387   -45.598 1.00 15.53 ? 158 ILE D CD1 1 
ATOM   7677 N  N   . PHE D 1 159 ? -1.675  -0.973  -50.791 1.00 12.02 ? 159 PHE D N   1 
ATOM   7678 C  CA  . PHE D 1 159 ? -0.599  -0.965  -51.765 1.00 12.26 ? 159 PHE D CA  1 
ATOM   7679 C  C   . PHE D 1 159 ? -1.092  -0.824  -53.190 1.00 11.82 ? 159 PHE D C   1 
ATOM   7680 O  O   . PHE D 1 159 ? -0.355  -0.406  -54.071 1.00 14.05 ? 159 PHE D O   1 
ATOM   7681 C  CB  . PHE D 1 159 ? 0.182   -2.302  -51.723 1.00 12.35 ? 159 PHE D CB  1 
ATOM   7682 C  CG  . PHE D 1 159 ? 0.927   -2.543  -50.412 1.00 14.08 ? 159 PHE D CG  1 
ATOM   7683 C  CD1 . PHE D 1 159 ? 1.279   -1.512  -49.554 1.00 15.27 ? 159 PHE D CD1 1 
ATOM   7684 C  CD2 . PHE D 1 159 ? 1.254   -3.902  -50.033 1.00 14.44 ? 159 PHE D CD2 1 
ATOM   7685 C  CE1 . PHE D 1 159 ? 1.994   -1.788  -48.339 1.00 15.48 ? 159 PHE D CE1 1 
ATOM   7686 C  CE2 . PHE D 1 159 ? 1.928   -4.153  -48.829 1.00 13.63 ? 159 PHE D CE2 1 
ATOM   7687 C  CZ  . PHE D 1 159 ? 2.306   -3.103  -47.994 1.00 14.64 ? 159 PHE D CZ  1 
ATOM   7688 N  N   . SER D 1 160 ? -2.358  -1.142  -53.494 1.00 12.71 ? 160 SER D N   1 
ATOM   7689 C  CA  . SER D 1 160 ? -2.853  -1.012  -54.872 1.00 14.11 ? 160 SER D CA  1 
ATOM   7690 C  C   . SER D 1 160 ? -2.990  0.398   -55.325 1.00 14.01 ? 160 SER D C   1 
ATOM   7691 O  O   . SER D 1 160 ? -3.048  0.632   -56.513 1.00 16.04 ? 160 SER D O   1 
ATOM   7692 C  CB  . SER D 1 160 ? -4.214  -1.685  -55.023 1.00 16.56 ? 160 SER D CB  1 
ATOM   7693 O  OG  . SER D 1 160 ? -5.165  -1.057  -54.250 1.00 16.95 ? 160 SER D OG  1 
ATOM   7694 N  N   . HIS D 1 161 ? -2.864  1.326   -54.404 1.00 14.15 ? 161 HIS D N   1 
ATOM   7695 C  CA  . HIS D 1 161 ? -2.964  2.761   -54.687 1.00 14.72 ? 161 HIS D CA  1 
ATOM   7696 C  C   . HIS D 1 161 ? -1.632  3.435   -54.796 1.00 16.22 ? 161 HIS D C   1 
ATOM   7697 O  O   . HIS D 1 161 ? -1.597  4.616   -55.099 1.00 15.34 ? 161 HIS D O   1 
ATOM   7698 C  CB  . HIS D 1 161 ? -3.832  3.489   -53.565 1.00 15.30 ? 161 HIS D CB  1 
ATOM   7699 C  CG  . HIS D 1 161 ? -5.257  3.025   -53.548 1.00 17.39 ? 161 HIS D CG  1 
ATOM   7700 N  ND1 . HIS D 1 161 ? -6.191  3.635   -54.300 1.00 18.64 ? 161 HIS D ND1 1 
ATOM   7701 C  CD2 . HIS D 1 161 ? -5.909  2.000   -52.839 1.00 17.50 ? 161 HIS D CD2 1 
ATOM   7702 C  CE1 . HIS D 1 161 ? -7.399  3.011   -54.148 1.00 18.20 ? 161 HIS D CE1 1 
ATOM   7703 N  NE2 . HIS D 1 161 ? -7.236  2.014   -53.251 1.00 17.82 ? 161 HIS D NE2 1 
ATOM   7704 N  N   . LEU D 1 162 ? -0.540  2.695   -54.605 1.00 17.93 ? 162 LEU D N   1 
ATOM   7705 C  CA  . LEU D 1 162 ? 0.804   3.331   -54.550 1.00 18.62 ? 162 LEU D CA  1 
ATOM   7706 C  C   . LEU D 1 162 ? 1.140   4.079   -55.839 1.00 20.05 ? 162 LEU D C   1 
ATOM   7707 O  O   . LEU D 1 162 ? 1.727   5.217   -55.792 1.00 23.25 ? 162 LEU D O   1 
ATOM   7708 C  CB  . LEU D 1 162 ? 1.857   2.234   -54.252 1.00 21.43 ? 162 LEU D CB  1 
ATOM   7709 C  CG  . LEU D 1 162 ? 1.797   1.874   -52.767 1.00 23.53 ? 162 LEU D CG  1 
ATOM   7710 C  CD1 . LEU D 1 162 ? 2.666   0.682   -52.462 1.00 25.54 ? 162 LEU D CD1 1 
ATOM   7711 C  CD2 . LEU D 1 162 ? 2.228   3.020   -51.881 1.00 26.97 ? 162 LEU D CD2 1 
ATOM   7712 N  N   A GLN D 1 163 ? 0.786   3.530   -56.991 0.50 21.14 ? 163 GLN D N   1 
ATOM   7713 N  N   B GLN D 1 163 ? 0.685   3.474   -56.930 0.50 20.19 ? 163 GLN D N   1 
ATOM   7714 C  CA  A GLN D 1 163 ? 1.168   4.204   -58.237 0.50 20.78 ? 163 GLN D CA  1 
ATOM   7715 C  CA  B GLN D 1 163 ? 0.924   3.922   -58.283 0.50 19.08 ? 163 GLN D CA  1 
ATOM   7716 C  C   A GLN D 1 163 ? 0.534   5.586   -58.336 0.50 20.46 ? 163 GLN D C   1 
ATOM   7717 C  C   B GLN D 1 163 ? 0.206   5.222   -58.622 0.50 19.01 ? 163 GLN D C   1 
ATOM   7718 O  O   A GLN D 1 163 ? 1.074   6.511   -58.959 0.50 19.78 ? 163 GLN D O   1 
ATOM   7719 O  O   B GLN D 1 163 ? 0.400   5.704   -59.758 0.50 17.22 ? 163 GLN D O   1 
ATOM   7720 C  CB  A GLN D 1 163 ? 0.896   3.329   -59.445 0.50 23.19 ? 163 GLN D CB  1 
ATOM   7721 C  CB  B GLN D 1 163 ? 0.525   2.820   -59.259 0.50 21.14 ? 163 GLN D CB  1 
ATOM   7722 C  CG  A GLN D 1 163 ? 1.804   2.096   -59.458 0.50 24.75 ? 163 GLN D CG  1 
ATOM   7723 C  CG  B GLN D 1 163 ? -0.976  2.659   -59.409 0.50 21.82 ? 163 GLN D CG  1 
ATOM   7724 C  CD  A GLN D 1 163 ? 3.272   2.391   -59.112 0.50 25.18 ? 163 GLN D CD  1 
ATOM   7725 C  CD  B GLN D 1 163 ? -1.300  1.760   -60.585 0.50 22.74 ? 163 GLN D CD  1 
ATOM   7726 O  OE1 A GLN D 1 163 ? 3.654   3.532   -58.776 0.50 30.11 ? 163 GLN D OE1 1 
ATOM   7727 O  OE1 B GLN D 1 163 ? -1.188  0.550   -60.477 0.50 24.83 ? 163 GLN D OE1 1 
ATOM   7728 N  NE2 A GLN D 1 163 ? 4.099   1.363   -59.170 0.50 22.88 ? 163 GLN D NE2 1 
ATOM   7729 N  NE2 B GLN D 1 163 ? -1.667  2.350   -61.721 0.50 22.21 ? 163 GLN D NE2 1 
ATOM   7730 N  N   . HIS D 1 164 ? -0.583  5.754   -57.656 1.00 18.75 ? 164 HIS D N   1 
ATOM   7731 C  CA  . HIS D 1 164 ? -1.250  7.070   -57.685 1.00 18.11 ? 164 HIS D CA  1 
ATOM   7732 C  C   . HIS D 1 164 ? -0.717  8.173   -56.787 1.00 19.25 ? 164 HIS D C   1 
ATOM   7733 O  O   . HIS D 1 164 ? -1.165  9.313   -56.832 1.00 18.19 ? 164 HIS D O   1 
ATOM   7734 C  CB  . HIS D 1 164 ? -2.761  6.904   -57.513 1.00 22.28 ? 164 HIS D CB  1 
ATOM   7735 C  CG  . HIS D 1 164 ? -3.372  5.962   -58.509 1.00 23.87 ? 164 HIS D CG  1 
ATOM   7736 N  ND1 . HIS D 1 164 ? -3.576  6.303   -59.798 1.00 26.21 ? 164 HIS D ND1 1 
ATOM   7737 C  CD2 . HIS D 1 164 ? -3.814  4.640   -58.375 1.00 29.39 ? 164 HIS D CD2 1 
ATOM   7738 C  CE1 . HIS D 1 164 ? -4.148  5.269   -60.456 1.00 31.69 ? 164 HIS D CE1 1 
ATOM   7739 N  NE2 . HIS D 1 164 ? -4.275  4.246   -59.590 1.00 33.19 ? 164 HIS D NE2 1 
ATOM   7740 N  N   . VAL D 1 165 ? 0.269   7.839   -55.942 1.00 17.76 ? 165 VAL D N   1 
ATOM   7741 C  CA  . VAL D 1 165 ? 0.887   8.795   -55.100 1.00 16.51 ? 165 VAL D CA  1 
ATOM   7742 C  C   . VAL D 1 165 ? 2.410   8.680   -55.248 1.00 16.51 ? 165 VAL D C   1 
ATOM   7743 O  O   . VAL D 1 165 ? 3.153   8.803   -54.243 1.00 15.15 ? 165 VAL D O   1 
ATOM   7744 C  CB  . VAL D 1 165 ? 0.442   8.591   -53.623 1.00 18.78 ? 165 VAL D CB  1 
ATOM   7745 C  CG1 . VAL D 1 165 ? -1.063  8.765   -53.508 1.00 19.11 ? 165 VAL D CG1 1 
ATOM   7746 C  CG2 . VAL D 1 165 ? 0.709   7.159   -53.180 1.00 17.02 ? 165 VAL D CG2 1 
ATOM   7747 N  N   A LYS D 1 166 ? 2.867   8.488   -56.482 0.50 15.53 ? 166 LYS D N   1 
ATOM   7748 N  N   B LYS D 1 166 ? 2.867   8.480   -56.481 0.50 15.42 ? 166 LYS D N   1 
ATOM   7749 C  CA  A LYS D 1 166 ? 4.289   8.210   -56.745 0.50 15.59 ? 166 LYS D CA  1 
ATOM   7750 C  CA  B LYS D 1 166 ? 4.291   8.216   -56.742 0.50 15.39 ? 166 LYS D CA  1 
ATOM   7751 C  C   A LYS D 1 166 ? 5.228   9.361   -56.376 0.50 15.23 ? 166 LYS D C   1 
ATOM   7752 C  C   B LYS D 1 166 ? 5.186   9.356   -56.245 0.50 14.99 ? 166 LYS D C   1 
ATOM   7753 O  O   A LYS D 1 166 ? 6.392   9.107   -56.086 0.50 16.70 ? 166 LYS D O   1 
ATOM   7754 O  O   B LYS D 1 166 ? 6.255   9.097   -55.715 0.50 16.34 ? 166 LYS D O   1 
ATOM   7755 C  CB  A LYS D 1 166 ? 4.509   7.790   -58.220 0.50 16.66 ? 166 LYS D CB  1 
ATOM   7756 C  CB  B LYS D 1 166 ? 4.543   7.959   -58.250 0.50 16.20 ? 166 LYS D CB  1 
ATOM   7757 C  CG  A LYS D 1 166 ? 4.217   6.310   -58.443 0.50 16.64 ? 166 LYS D CG  1 
ATOM   7758 C  CG  B LYS D 1 166 ? 5.918   7.380   -58.541 0.50 16.83 ? 166 LYS D CG  1 
ATOM   7759 C  CD  A LYS D 1 166 ? 4.393   5.814   -59.878 0.50 19.02 ? 166 LYS D CD  1 
ATOM   7760 C  CD  B LYS D 1 166 ? 6.080   6.780   -59.945 0.50 17.32 ? 166 LYS D CD  1 
ATOM   7761 C  CE  A LYS D 1 166 ? 4.650   4.299   -59.819 0.50 20.75 ? 166 LYS D CE  1 
ATOM   7762 C  CE  B LYS D 1 166 ? 5.905   5.237   -59.995 0.50 15.93 ? 166 LYS D CE  1 
ATOM   7763 N  NZ  A LYS D 1 166 ? 6.012   3.977   -60.325 0.50 20.86 ? 166 LYS D NZ  1 
ATOM   7764 N  NZ  B LYS D 1 166 ? 7.092   4.304   -59.871 0.50 19.10 ? 166 LYS D NZ  1 
ATOM   7765 N  N   . TYR D 1 167 ? 4.730   10.599  -56.385 1.00 16.35 ? 167 TYR D N   1 
ATOM   7766 C  CA  . TYR D 1 167 ? 5.564   11.777  -56.121 1.00 14.53 ? 167 TYR D CA  1 
ATOM   7767 C  C   . TYR D 1 167 ? 5.131   12.630  -54.963 1.00 16.44 ? 167 TYR D C   1 
ATOM   7768 O  O   . TYR D 1 167 ? 3.928   12.676  -54.591 1.00 17.02 ? 167 TYR D O   1 
ATOM   7769 C  CB  . TYR D 1 167 ? 5.611   12.649  -57.398 1.00 16.36 ? 167 TYR D CB  1 
ATOM   7770 C  CG  . TYR D 1 167 ? 6.284   11.950  -58.570 1.00 16.90 ? 167 TYR D CG  1 
ATOM   7771 C  CD1 . TYR D 1 167 ? 7.676   11.758  -58.556 1.00 18.58 ? 167 TYR D CD1 1 
ATOM   7772 C  CD2 . TYR D 1 167 ? 5.545   11.434  -59.630 1.00 23.67 ? 167 TYR D CD2 1 
ATOM   7773 C  CE1 . TYR D 1 167 ? 8.317   11.160  -59.606 1.00 19.74 ? 167 TYR D CE1 1 
ATOM   7774 C  CE2 . TYR D 1 167 ? 6.179   10.795  -60.699 1.00 22.90 ? 167 TYR D CE2 1 
ATOM   7775 C  CZ  . TYR D 1 167 ? 7.572   10.662  -60.665 1.00 23.95 ? 167 TYR D CZ  1 
ATOM   7776 O  OH  . TYR D 1 167 ? 8.270   10.083  -61.707 1.00 28.78 ? 167 TYR D OH  1 
ATOM   7777 N  N   . LYS D 1 168 ? 6.100   13.384  -54.429 1.00 14.25 ? 168 LYS D N   1 
ATOM   7778 C  CA  . LYS D 1 168 ? 5.793   14.198  -53.266 1.00 15.84 ? 168 LYS D CA  1 
ATOM   7779 C  C   . LYS D 1 168 ? 4.638   15.118  -53.630 1.00 18.27 ? 168 LYS D C   1 
ATOM   7780 O  O   . LYS D 1 168 ? 4.601   15.664  -54.752 1.00 21.19 ? 168 LYS D O   1 
ATOM   7781 C  CB  . LYS D 1 168 ? 7.033   15.016  -52.931 1.00 16.51 ? 168 LYS D CB  1 
ATOM   7782 C  CG  . LYS D 1 168 ? 6.793   15.960  -51.803 1.00 20.77 ? 168 LYS D CG  1 
ATOM   7783 C  CD  . LYS D 1 168 ? 8.087   16.564  -51.291 1.00 22.62 ? 168 LYS D CD  1 
ATOM   7784 C  CE  . LYS D 1 168 ? 7.737   17.483  -50.128 1.00 28.66 ? 168 LYS D CE  1 
ATOM   7785 N  NZ  . LYS D 1 168 ? 8.764   18.551  -49.858 1.00 30.46 ? 168 LYS D NZ  1 
ATOM   7786 N  N   . GLY D 1 169 ? 3.661   15.200  -52.723 1.00 17.27 ? 169 GLY D N   1 
ATOM   7787 C  CA  . GLY D 1 169 ? 2.439   15.965  -52.847 1.00 22.09 ? 169 GLY D CA  1 
ATOM   7788 C  C   . GLY D 1 169 ? 1.243   15.286  -53.513 1.00 21.02 ? 169 GLY D C   1 
ATOM   7789 O  O   . GLY D 1 169 ? 0.108   15.834  -53.489 1.00 22.58 ? 169 GLY D O   1 
ATOM   7790 N  N   . GLN D 1 170 ? 1.453   14.141  -54.148 1.00 18.91 ? 170 GLN D N   1 
ATOM   7791 C  CA  . GLN D 1 170 ? 0.334   13.475  -54.777 1.00 20.32 ? 170 GLN D CA  1 
ATOM   7792 C  C   . GLN D 1 170 ? -0.556  12.779  -53.712 1.00 22.72 ? 170 GLN D C   1 
ATOM   7793 O  O   . GLN D 1 170 ? -0.062  12.324  -52.643 1.00 18.79 ? 170 GLN D O   1 
ATOM   7794 C  CB  . GLN D 1 170 ? 0.823   12.540  -55.862 1.00 18.71 ? 170 GLN D CB  1 
ATOM   7795 C  CG  . GLN D 1 170 ? 1.605   13.273  -56.975 1.00 18.94 ? 170 GLN D CG  1 
ATOM   7796 C  CD  . GLN D 1 170 ? 1.932   12.370  -58.141 1.00 20.65 ? 170 GLN D CD  1 
ATOM   7797 O  OE1 . GLN D 1 170 ? 2.301   11.224  -57.962 1.00 20.97 ? 170 GLN D OE1 1 
ATOM   7798 N  NE2 . GLN D 1 170 ? 1.777   12.878  -59.357 1.00 20.71 ? 170 GLN D NE2 1 
ATOM   7799 N  N   . GLU D 1 171 ? -1.876  12.734  -53.995 1.00 20.60 ? 171 GLU D N   1 
ATOM   7800 C  CA  . GLU D 1 171 ? -2.906  12.250  -53.023 1.00 20.31 ? 171 GLU D CA  1 
ATOM   7801 C  C   . GLU D 1 171 ? -3.849  11.302  -53.790 1.00 18.07 ? 171 GLU D C   1 
ATOM   7802 O  O   . GLU D 1 171 ? -3.999  11.423  -55.035 1.00 21.49 ? 171 GLU D O   1 
ATOM   7803 C  CB  . GLU D 1 171 ? -3.705  13.419  -52.442 1.00 23.20 ? 171 GLU D CB  1 
ATOM   7804 C  CG  . GLU D 1 171 ? -2.896  14.370  -51.549 1.00 28.02 ? 171 GLU D CG  1 
ATOM   7805 C  CD  . GLU D 1 171 ? -3.698  15.569  -51.062 1.00 35.03 ? 171 GLU D CD  1 
ATOM   7806 O  OE1 . GLU D 1 171 ? -4.778  15.819  -51.627 1.00 38.92 ? 171 GLU D OE1 1 
ATOM   7807 O  OE2 . GLU D 1 171 ? -3.232  16.263  -50.122 1.00 37.25 ? 171 GLU D OE2 1 
ATOM   7808 N  N   . ALA D 1 172 ? -4.352  10.287  -53.124 1.00 19.62 ? 172 ALA D N   1 
ATOM   7809 C  CA  . ALA D 1 172 ? -5.231  9.285   -53.728 1.00 17.07 ? 172 ALA D CA  1 
ATOM   7810 C  C   . ALA D 1 172 ? -6.214  8.897   -52.635 1.00 16.98 ? 172 ALA D C   1 
ATOM   7811 O  O   . ALA D 1 172 ? -5.938  8.985   -51.461 1.00 19.10 ? 172 ALA D O   1 
ATOM   7812 C  CB  . ALA D 1 172 ? -4.492  8.006   -54.203 1.00 18.65 ? 172 ALA D CB  1 
ATOM   7813 N  N   . PHE D 1 173 ? -7.403  8.494   -53.012 1.00 17.84 ? 173 PHE D N   1 
ATOM   7814 C  CA  . PHE D 1 173 ? -8.388  8.140   -51.954 1.00 16.85 ? 173 PHE D CA  1 
ATOM   7815 C  C   . PHE D 1 173 ? -8.463  6.634   -51.914 1.00 17.11 ? 173 PHE D C   1 
ATOM   7816 O  O   . PHE D 1 173 ? -8.489  5.983   -52.960 1.00 20.49 ? 173 PHE D O   1 
ATOM   7817 C  CB  . PHE D 1 173 ? -9.794  8.666   -52.271 1.00 18.03 ? 173 PHE D CB  1 
ATOM   7818 C  CG  . PHE D 1 173 ? -10.091 10.031  -51.682 1.00 20.89 ? 173 PHE D CG  1 
ATOM   7819 C  CD1 . PHE D 1 173 ? -10.156 10.240  -50.276 1.00 21.07 ? 173 PHE D CD1 1 
ATOM   7820 C  CD2 . PHE D 1 173 ? -10.347 11.095  -52.509 1.00 26.36 ? 173 PHE D CD2 1 
ATOM   7821 C  CE1 . PHE D 1 173 ? -10.412 11.492  -49.740 1.00 28.17 ? 173 PHE D CE1 1 
ATOM   7822 C  CE2 . PHE D 1 173 ? -10.613 12.352  -51.982 1.00 27.52 ? 173 PHE D CE2 1 
ATOM   7823 C  CZ  . PHE D 1 173 ? -10.648 12.559  -50.602 1.00 29.07 ? 173 PHE D CZ  1 
ATOM   7824 N  N   . VAL D 1 174 ? -8.529  6.109   -50.704 1.00 14.57 ? 174 VAL D N   1 
ATOM   7825 C  CA  . VAL D 1 174 ? -8.599  4.657   -50.471 1.00 15.89 ? 174 VAL D CA  1 
ATOM   7826 C  C   . VAL D 1 174 ? -9.961  4.418   -49.809 1.00 15.69 ? 174 VAL D C   1 
ATOM   7827 O  O   . VAL D 1 174 ? -10.250 5.034   -48.734 1.00 14.59 ? 174 VAL D O   1 
ATOM   7828 C  CB  . VAL D 1 174 ? -7.508  4.179   -49.485 1.00 14.42 ? 174 VAL D CB  1 
ATOM   7829 C  CG1 . VAL D 1 174 ? -7.583  2.686   -49.154 1.00 15.39 ? 174 VAL D CG1 1 
ATOM   7830 C  CG2 . VAL D 1 174 ? -6.105  4.538   -50.035 1.00 16.73 ? 174 VAL D CG2 1 
ATOM   7831 N  N   . PRO D 1 175 ? -10.732 3.446   -50.356 1.00 16.68 ? 175 PRO D N   1 
ATOM   7832 C  CA  . PRO D 1 175 ? -12.005 3.156   -49.713 1.00 16.54 ? 175 PRO D CA  1 
ATOM   7833 C  C   . PRO D 1 175 ? -11.758 2.574   -48.330 1.00 15.17 ? 175 PRO D C   1 
ATOM   7834 O  O   . PRO D 1 175 ? -10.730 1.939   -48.081 1.00 13.80 ? 175 PRO D O   1 
ATOM   7835 C  CB  . PRO D 1 175 ? -12.590 2.064   -50.596 1.00 16.03 ? 175 PRO D CB  1 
ATOM   7836 C  CG  . PRO D 1 175 ? -12.018 2.266   -51.975 1.00 18.21 ? 175 PRO D CG  1 
ATOM   7837 C  CD  . PRO D 1 175 ? -10.583 2.726   -51.653 1.00 17.00 ? 175 PRO D CD  1 
ATOM   7838 N  N   . GLY D 1 176 ? -12.640 2.847   -47.362 1.00 15.08 ? 176 GLY D N   1 
ATOM   7839 C  CA  . GLY D 1 176 ? -12.454 2.198   -46.096 1.00 12.45 ? 176 GLY D CA  1 
ATOM   7840 C  C   . GLY D 1 176 ? -12.456 0.660   -46.059 1.00 13.04 ? 176 GLY D C   1 
ATOM   7841 O  O   . GLY D 1 176 ? -13.041 -0.014  -46.895 1.00 16.04 ? 176 GLY D O   1 
ATOM   7842 N  N   . PHE D 1 177 ? -11.763 0.174   -45.061 1.00 14.08 ? 177 PHE D N   1 
ATOM   7843 C  CA  . PHE D 1 177 ? -11.632 -1.241  -44.756 1.00 12.78 ? 177 PHE D CA  1 
ATOM   7844 C  C   . PHE D 1 177 ? -11.351 -1.452  -43.271 1.00 14.22 ? 177 PHE D C   1 
ATOM   7845 O  O   . PHE D 1 177 ? -11.152 -0.520  -42.523 1.00 15.44 ? 177 PHE D O   1 
ATOM   7846 C  CB  . PHE D 1 177 ? -10.647 -1.958  -45.696 1.00 14.33 ? 177 PHE D CB  1 
ATOM   7847 C  CG  . PHE D 1 177 ? -9.182  -1.644  -45.453 1.00 15.19 ? 177 PHE D CG  1 
ATOM   7848 C  CD1 . PHE D 1 177 ? -8.366  -2.503  -44.648 1.00 14.93 ? 177 PHE D CD1 1 
ATOM   7849 C  CD2 . PHE D 1 177 ? -8.637  -0.516  -46.063 1.00 16.27 ? 177 PHE D CD2 1 
ATOM   7850 C  CE1 . PHE D 1 177 ? -7.004  -2.201  -44.483 1.00 14.73 ? 177 PHE D CE1 1 
ATOM   7851 C  CE2 . PHE D 1 177 ? -7.298  -0.208  -45.884 1.00 15.82 ? 177 PHE D CE2 1 
ATOM   7852 C  CZ  . PHE D 1 177 ? -6.531  -1.026  -45.082 1.00 15.30 ? 177 PHE D CZ  1 
ATOM   7853 N  N   . ASN D 1 178 ? -11.351 -2.704  -42.830 1.00 14.55 ? 178 ASN D N   1 
ATOM   7854 C  CA  . ASN D 1 178 ? -11.196 -2.862  -41.423 1.00 13.19 ? 178 ASN D CA  1 
ATOM   7855 C  C   . ASN D 1 178 ? -9.718  -2.835  -41.164 1.00 13.90 ? 178 ASN D C   1 
ATOM   7856 O  O   . ASN D 1 178 ? -9.032  -3.806  -41.514 1.00 16.20 ? 178 ASN D O   1 
ATOM   7857 C  CB  . ASN D 1 178 ? -11.798 -4.228  -40.993 1.00 14.78 ? 178 ASN D CB  1 
ATOM   7858 C  CG  . ASN D 1 178 ? -11.599 -4.481  -39.515 1.00 17.06 ? 178 ASN D CG  1 
ATOM   7859 O  OD1 . ASN D 1 178 ? -11.252 -3.594  -38.727 1.00 17.42 ? 178 ASN D OD1 1 
ATOM   7860 N  ND2 . ASN D 1 178 ? -11.844 -5.718  -39.114 1.00 22.42 ? 178 ASN D ND2 1 
ATOM   7861 N  N   . ILE D 1 179 ? -9.277  -1.766  -40.508 1.00 13.10 ? 179 ILE D N   1 
ATOM   7862 C  CA  . ILE D 1 179 ? -7.817  -1.610  -40.135 1.00 12.33 ? 179 ILE D CA  1 
ATOM   7863 C  C   . ILE D 1 179 ? -7.263  -2.663  -39.190 1.00 14.09 ? 179 ILE D C   1 
ATOM   7864 O  O   . ILE D 1 179 ? -6.043  -2.894  -39.141 1.00 14.36 ? 179 ILE D O   1 
ATOM   7865 C  CB  . ILE D 1 179 ? -7.564  -0.149  -39.612 1.00 13.03 ? 179 ILE D CB  1 
ATOM   7866 C  CG1 . ILE D 1 179 ? -8.109  0.771   -40.655 1.00 14.04 ? 179 ILE D CG1 1 
ATOM   7867 C  CG2 . ILE D 1 179 ? -6.080  0.227   -39.276 1.00 12.78 ? 179 ILE D CG2 1 
ATOM   7868 C  CD1 . ILE D 1 179 ? -7.398  0.669   -42.034 1.00 15.77 ? 179 ILE D CD1 1 
ATOM   7869 N  N   . GLU D 1 180 ? -8.163  -3.396  -38.507 1.00 15.52 ? 180 GLU D N   1 
ATOM   7870 C  CA  . GLU D 1 180 ? -7.743  -4.467  -37.649 1.00 16.46 ? 180 GLU D CA  1 
ATOM   7871 C  C   . GLU D 1 180 ? -7.202  -5.616  -38.477 1.00 12.71 ? 180 GLU D C   1 
ATOM   7872 O  O   . GLU D 1 180 ? -6.396  -6.364  -37.944 1.00 14.40 ? 180 GLU D O   1 
ATOM   7873 C  CB  . GLU D 1 180 ? -8.897  -4.991  -36.728 1.00 21.83 ? 180 GLU D CB  1 
ATOM   7874 C  CG  . GLU D 1 180 ? -8.306  -5.552  -35.435 1.00 24.63 ? 180 GLU D CG  1 
ATOM   7875 C  CD  . GLU D 1 180 ? -9.361  -5.774  -34.354 1.00 28.66 ? 180 GLU D CD  1 
ATOM   7876 O  OE1 . GLU D 1 180 ? -10.465 -5.160  -34.431 1.00 27.95 ? 180 GLU D OE1 1 
ATOM   7877 O  OE2 . GLU D 1 180 ? -9.049  -6.602  -33.461 1.00 34.10 ? 180 GLU D OE2 1 
ATOM   7878 N  N   . GLU D 1 181 ? -7.538  -5.678  -39.745 1.00 14.11 ? 181 GLU D N   1 
ATOM   7879 C  CA  . GLU D 1 181 ? -6.988  -6.753  -40.603 1.00 14.28 ? 181 GLU D CA  1 
ATOM   7880 C  C   . GLU D 1 181 ? -5.511  -6.578  -40.843 1.00 13.98 ? 181 GLU D C   1 
ATOM   7881 O  O   . GLU D 1 181 ? -4.792  -7.594  -41.210 1.00 14.26 ? 181 GLU D O   1 
ATOM   7882 C  CB  . GLU D 1 181 ? -7.662  -6.796  -41.949 1.00 15.68 ? 181 GLU D CB  1 
ATOM   7883 C  CG  . GLU D 1 181 ? -9.135  -7.162  -41.916 1.00 17.37 ? 181 GLU D CG  1 
ATOM   7884 C  CD  . GLU D 1 181 ? -9.806  -7.028  -43.294 1.00 21.17 ? 181 GLU D CD  1 
ATOM   7885 O  OE1 . GLU D 1 181 ? -9.153  -6.704  -44.357 1.00 23.86 ? 181 GLU D OE1 1 
ATOM   7886 O  OE2 . GLU D 1 181 ? -11.083 -7.241  -43.355 1.00 21.19 ? 181 GLU D OE2 1 
ATOM   7887 N  N   . LEU D 1 182 ? -5.028  -5.352  -40.574 1.00 13.78 ? 182 LEU D N   1 
ATOM   7888 C  CA  . LEU D 1 182 ? -3.547  -5.136  -40.621 1.00 12.82 ? 182 LEU D CA  1 
ATOM   7889 C  C   . LEU D 1 182 ? -2.739  -5.670  -39.417 1.00 13.49 ? 182 LEU D C   1 
ATOM   7890 O  O   . LEU D 1 182 ? -1.483  -5.677  -39.418 1.00 12.52 ? 182 LEU D O   1 
ATOM   7891 C  CB  . LEU D 1 182 ? -3.241  -3.594  -40.835 1.00 12.16 ? 182 LEU D CB  1 
ATOM   7892 C  CG  . LEU D 1 182 ? -3.895  -3.006  -42.124 1.00 11.05 ? 182 LEU D CG  1 
ATOM   7893 C  CD1 . LEU D 1 182 ? -3.603  -1.482  -42.215 1.00 13.46 ? 182 LEU D CD1 1 
ATOM   7894 C  CD2 . LEU D 1 182 ? -3.637  -3.747  -43.435 1.00 12.66 ? 182 LEU D CD2 1 
ATOM   7895 N  N   . LEU D 1 183 ? -3.442  -5.923  -38.326 1.00 13.11 ? 183 LEU D N   1 
ATOM   7896 C  CA  . LEU D 1 183 ? -2.835  -6.338  -37.094 1.00 13.05 ? 183 LEU D CA  1 
ATOM   7897 C  C   . LEU D 1 183 ? -2.521  -7.829  -37.070 1.00 12.93 ? 183 LEU D C   1 
ATOM   7898 O  O   . LEU D 1 183 ? -3.207  -8.603  -37.732 1.00 14.21 ? 183 LEU D O   1 
ATOM   7899 C  CB  . LEU D 1 183 ? -3.713  -6.006  -35.876 1.00 14.68 ? 183 LEU D CB  1 
ATOM   7900 C  CG  . LEU D 1 183 ? -3.999  -4.490  -35.767 1.00 14.16 ? 183 LEU D CG  1 
ATOM   7901 C  CD1 . LEU D 1 183 ? -4.928  -4.239  -34.565 1.00 16.77 ? 183 LEU D CD1 1 
ATOM   7902 C  CD2 . LEU D 1 183 ? -2.739  -3.643  -35.601 1.00 18.06 ? 183 LEU D CD2 1 
ATOM   7903 N  N   . PRO D 1 184 ? -1.489  -8.216  -36.317 1.00 14.52 ? 184 PRO D N   1 
ATOM   7904 C  CA  . PRO D 1 184 ? -1.115  -9.640  -36.195 1.00 15.81 ? 184 PRO D CA  1 
ATOM   7905 C  C   . PRO D 1 184 ? -1.996  -10.485 -35.261 1.00 17.87 ? 184 PRO D C   1 
ATOM   7906 O  O   . PRO D 1 184 ? -2.992  -9.991  -34.657 1.00 17.65 ? 184 PRO D O   1 
ATOM   7907 C  CB  . PRO D 1 184 ? 0.291   -9.558  -35.639 1.00 15.36 ? 184 PRO D CB  1 
ATOM   7908 C  CG  . PRO D 1 184 ? 0.271   -8.299  -34.749 1.00 17.05 ? 184 PRO D CG  1 
ATOM   7909 C  CD  . PRO D 1 184 ? -0.558  -7.363  -35.560 1.00 14.74 ? 184 PRO D CD  1 
ATOM   7910 N  N   . GLU D 1 185 ? -1.632  -11.779 -35.239 1.00 18.60 ? 185 GLU D N   1 
ATOM   7911 C  CA  . GLU D 1 185 ? -2.236  -12.721 -34.325 1.00 18.95 ? 185 GLU D CA  1 
ATOM   7912 C  C   . GLU D 1 185 ? -1.923  -12.290 -32.906 1.00 17.93 ? 185 GLU D C   1 
ATOM   7913 O  O   . GLU D 1 185 ? -0.859  -11.701 -32.636 1.00 20.13 ? 185 GLU D O   1 
ATOM   7914 C  CB  . GLU D 1 185 ? -1.666  -14.096 -34.587 1.00 21.92 ? 185 GLU D CB  1 
ATOM   7915 C  CG  . GLU D 1 185 ? -2.164  -14.594 -35.922 1.00 27.30 ? 185 GLU D CG  1 
ATOM   7916 C  CD  . GLU D 1 185 ? -2.208  -16.104 -35.958 1.00 38.94 ? 185 GLU D CD  1 
ATOM   7917 O  OE1 . GLU D 1 185 ? -3.295  -16.614 -36.311 1.00 49.28 ? 185 GLU D OE1 1 
ATOM   7918 O  OE2 . GLU D 1 185 ? -1.206  -16.779 -35.598 1.00 42.79 ? 185 GLU D OE2 1 
ATOM   7919 N  N   . ARG D 1 186 ? -2.823  -12.620 -31.988 1.00 17.64 ? 186 ARG D N   1 
ATOM   7920 C  CA  . ARG D 1 186 ? -2.536  -12.462 -30.552 1.00 16.15 ? 186 ARG D CA  1 
ATOM   7921 C  C   . ARG D 1 186 ? -2.051  -11.026 -30.156 1.00 16.45 ? 186 ARG D C   1 
ATOM   7922 O  O   . ARG D 1 186 ? -0.984  -10.866 -29.529 1.00 16.43 ? 186 ARG D O   1 
ATOM   7923 C  CB  . ARG D 1 186 ? -1.569  -13.576 -30.055 1.00 21.27 ? 186 ARG D CB  1 
ATOM   7924 C  CG  . ARG D 1 186 ? -2.258  -14.953 -30.149 1.00 23.98 ? 186 ARG D CG  1 
ATOM   7925 C  CD  . ARG D 1 186 ? -1.382  -16.102 -29.670 1.00 27.62 ? 186 ARG D CD  1 
ATOM   7926 N  NE  . ARG D 1 186 ? -0.278  -16.231 -30.614 1.00 28.52 ? 186 ARG D NE  1 
ATOM   7927 C  CZ  . ARG D 1 186 ? -0.398  -16.708 -31.866 1.00 30.83 ? 186 ARG D CZ  1 
ATOM   7928 N  NH1 . ARG D 1 186 ? -1.566  -17.180 -32.333 1.00 30.13 ? 186 ARG D NH1 1 
ATOM   7929 N  NH2 . ARG D 1 186 ? 0.673   -16.699 -32.653 1.00 32.24 ? 186 ARG D NH2 1 
ATOM   7930 N  N   . THR D 1 187 ? -2.836  -10.030 -30.530 1.00 16.30 ? 187 THR D N   1 
ATOM   7931 C  CA  . THR D 1 187 ? -2.488  -8.647  -30.143 1.00 15.77 ? 187 THR D CA  1 
ATOM   7932 C  C   . THR D 1 187 ? -2.346  -8.396  -28.641 1.00 15.14 ? 187 THR D C   1 
ATOM   7933 O  O   . THR D 1 187 ? -1.702  -7.410  -28.256 1.00 14.41 ? 187 THR D O   1 
ATOM   7934 C  CB  . THR D 1 187 ? -3.480  -7.551  -30.689 1.00 13.83 ? 187 THR D CB  1 
ATOM   7935 O  OG1 . THR D 1 187 ? -4.819  -7.957  -30.348 1.00 16.14 ? 187 THR D OG1 1 
ATOM   7936 C  CG2 . THR D 1 187 ? -3.408  -7.473  -32.240 1.00 15.71 ? 187 THR D CG2 1 
ATOM   7937 N  N   . ALA D 1 188 ? -2.881  -9.242  -27.764 1.00 14.90 ? 188 ALA D N   1 
ATOM   7938 C  CA  . ALA D 1 188 ? -2.628  -9.061  -26.334 1.00 14.51 ? 188 ALA D CA  1 
ATOM   7939 C  C   . ALA D 1 188 ? -1.111  -9.224  -25.943 1.00 14.60 ? 188 ALA D C   1 
ATOM   7940 O  O   . ALA D 1 188 ? -0.723  -8.821  -24.862 1.00 14.12 ? 188 ALA D O   1 
ATOM   7941 C  CB  . ALA D 1 188 ? -3.444  -10.091 -25.523 1.00 17.31 ? 188 ALA D CB  1 
ATOM   7942 N  N   . GLU D 1 189 ? -0.335  -9.881  -26.829 1.00 15.73 ? 189 GLU D N   1 
ATOM   7943 C  CA  . GLU D 1 189 ? 1.116   -10.045 -26.591 1.00 14.00 ? 189 GLU D CA  1 
ATOM   7944 C  C   . GLU D 1 189 ? 1.896   -8.906  -27.282 1.00 12.86 ? 189 GLU D C   1 
ATOM   7945 O  O   . GLU D 1 189 ? 1.929   -8.818  -28.515 1.00 12.82 ? 189 GLU D O   1 
ATOM   7946 C  CB  . GLU D 1 189 ? 1.488   -11.370 -27.207 1.00 16.98 ? 189 GLU D CB  1 
ATOM   7947 C  CG  . GLU D 1 189 ? 0.705   -12.475 -26.532 1.00 21.07 ? 189 GLU D CG  1 
ATOM   7948 C  CD  . GLU D 1 189 ? 1.107   -13.826 -27.051 1.00 23.89 ? 189 GLU D CD  1 
ATOM   7949 O  OE1 . GLU D 1 189 ? 2.239   -14.007 -27.477 1.00 23.13 ? 189 GLU D OE1 1 
ATOM   7950 O  OE2 . GLU D 1 189 ? 0.261   -14.741 -27.016 1.00 28.45 ? 189 GLU D OE2 1 
ATOM   7951 N  N   . TYR D 1 190 ? 2.582   -8.130  -26.475 1.00 13.18 ? 190 TYR D N   1 
ATOM   7952 C  CA  . TYR D 1 190 ? 3.247   -6.913  -27.036 1.00 11.65 ? 190 TYR D CA  1 
ATOM   7953 C  C   . TYR D 1 190 ? 4.378   -6.509  -26.205 1.00 11.31 ? 190 TYR D C   1 
ATOM   7954 O  O   . TYR D 1 190 ? 4.451   -6.817  -24.966 1.00 12.20 ? 190 TYR D O   1 
ATOM   7955 C  CB  . TYR D 1 190 ? 2.240   -5.722  -27.302 1.00 13.35 ? 190 TYR D CB  1 
ATOM   7956 C  CG  . TYR D 1 190 ? 1.484   -5.309  -26.117 1.00 12.41 ? 190 TYR D CG  1 
ATOM   7957 C  CD1 . TYR D 1 190 ? 2.048   -4.403  -25.220 1.00 11.70 ? 190 TYR D CD1 1 
ATOM   7958 C  CD2 . TYR D 1 190 ? 0.168   -5.728  -25.964 1.00 12.14 ? 190 TYR D CD2 1 
ATOM   7959 C  CE1 . TYR D 1 190 ? 1.324   -3.953  -24.106 1.00 12.14 ? 190 TYR D CE1 1 
ATOM   7960 C  CE2 . TYR D 1 190 ? -0.566  -5.316  -24.837 1.00 11.84 ? 190 TYR D CE2 1 
ATOM   7961 C  CZ  . TYR D 1 190 ? 0.037   -4.404  -23.950 1.00 12.44 ? 190 TYR D CZ  1 
ATOM   7962 O  OH  . TYR D 1 190 ? -0.668  -3.936  -22.831 1.00 13.40 ? 190 TYR D OH  1 
ATOM   7963 N  N   . TYR D 1 191 ? 5.239   -5.644  -26.817 1.00 10.56 ? 191 TYR D N   1 
ATOM   7964 C  CA  . TYR D 1 191 ? 6.256   -4.882  -26.104 1.00 11.33 ? 191 TYR D CA  1 
ATOM   7965 C  C   . TYR D 1 191 ? 5.784   -3.412  -25.935 1.00 11.65 ? 191 TYR D C   1 
ATOM   7966 O  O   . TYR D 1 191 ? 5.137   -2.918  -26.816 1.00 10.91 ? 191 TYR D O   1 
ATOM   7967 C  CB  . TYR D 1 191 ? 7.544   -4.840  -26.988 1.00 11.24 ? 191 TYR D CB  1 
ATOM   7968 C  CG  . TYR D 1 191 ? 8.104   -6.172  -27.495 1.00 11.72 ? 191 TYR D CG  1 
ATOM   7969 C  CD1 . TYR D 1 191 ? 9.073   -6.888  -26.733 1.00 11.83 ? 191 TYR D CD1 1 
ATOM   7970 C  CD2 . TYR D 1 191 ? 7.686   -6.684  -28.755 1.00 12.49 ? 191 TYR D CD2 1 
ATOM   7971 C  CE1 . TYR D 1 191 ? 9.600   -8.070  -27.180 1.00 12.51 ? 191 TYR D CE1 1 
ATOM   7972 C  CE2 . TYR D 1 191 ? 8.250   -7.873  -29.235 1.00 14.95 ? 191 TYR D CE2 1 
ATOM   7973 C  CZ  . TYR D 1 191 ? 9.197   -8.550  -28.452 1.00 14.68 ? 191 TYR D CZ  1 
ATOM   7974 O  OH  . TYR D 1 191 ? 9.699   -9.740  -29.016 1.00 17.34 ? 191 TYR D OH  1 
ATOM   7975 N  N   . ARG D 1 192 ? 6.149   -2.764  -24.797 1.00 10.75 ? 192 ARG D N   1 
ATOM   7976 C  CA  . ARG D 1 192 ? 5.678   -1.371  -24.545 1.00 11.07 ? 192 ARG D CA  1 
ATOM   7977 C  C   . ARG D 1 192 ? 6.912   -0.637  -24.046 1.00 10.62 ? 192 ARG D C   1 
ATOM   7978 O  O   . ARG D 1 192 ? 7.541   -1.059  -23.123 1.00 11.94 ? 192 ARG D O   1 
ATOM   7979 C  CB  . ARG D 1 192 ? 4.582   -1.470  -23.513 1.00 12.74 ? 192 ARG D CB  1 
ATOM   7980 C  CG  . ARG D 1 192 ? 4.284   -0.213  -22.771 1.00 18.09 ? 192 ARG D CG  1 
ATOM   7981 C  CD  . ARG D 1 192 ? 3.540   0.698   -23.672 1.00 17.23 ? 192 ARG D CD  1 
ATOM   7982 N  NE  . ARG D 1 192 ? 2.365   0.185   -24.356 1.00 20.95 ? 192 ARG D NE  1 
ATOM   7983 C  CZ  . ARG D 1 192 ? 1.228   -0.208  -23.837 1.00 15.95 ? 192 ARG D CZ  1 
ATOM   7984 N  NH1 . ARG D 1 192 ? 1.015   -0.129  -22.495 1.00 22.52 ? 192 ARG D NH1 1 
ATOM   7985 N  NH2 . ARG D 1 192 ? 0.276   -0.624  -24.633 1.00 16.60 ? 192 ARG D NH2 1 
ATOM   7986 N  N   . TYR D 1 193 ? 7.183   0.567   -24.571 1.00 11.09 ? 193 TYR D N   1 
ATOM   7987 C  CA  . TYR D 1 193 ? 8.273   1.317   -23.921 1.00 10.14 ? 193 TYR D CA  1 
ATOM   7988 C  C   . TYR D 1 193 ? 8.031   2.823   -24.220 1.00 10.91 ? 193 TYR D C   1 
ATOM   7989 O  O   . TYR D 1 193 ? 7.218   3.165   -25.104 1.00 13.55 ? 193 TYR D O   1 
ATOM   7990 C  CB  . TYR D 1 193 ? 9.638   0.827   -24.427 1.00 10.84 ? 193 TYR D CB  1 
ATOM   7991 C  CG  . TYR D 1 193 ? 9.947   1.261   -25.876 1.00 8.85  ? 193 TYR D CG  1 
ATOM   7992 C  CD1 . TYR D 1 193 ? 10.695  2.385   -26.125 1.00 9.34  ? 193 TYR D CD1 1 
ATOM   7993 C  CD2 . TYR D 1 193 ? 9.479   0.531   -26.979 1.00 10.14 ? 193 TYR D CD2 1 
ATOM   7994 C  CE1 . TYR D 1 193 ? 10.974  2.794   -27.418 1.00 8.96  ? 193 TYR D CE1 1 
ATOM   7995 C  CE2 . TYR D 1 193 ? 9.769   0.934   -28.287 1.00 8.85  ? 193 TYR D CE2 1 
ATOM   7996 C  CZ  . TYR D 1 193 ? 10.529  2.072   -28.494 1.00 8.92  ? 193 TYR D CZ  1 
ATOM   7997 O  OH  . TYR D 1 193 ? 10.841  2.534   -29.761 1.00 10.73 ? 193 TYR D OH  1 
ATOM   7998 N  N   . ARG D 1 194 ? 8.760   3.707   -23.518 1.00 12.37 ? 194 ARG D N   1 
ATOM   7999 C  CA  . ARG D 1 194 ? 8.581   5.183   -23.761 1.00 12.93 ? 194 ARG D CA  1 
ATOM   8000 C  C   . ARG D 1 194 ? 9.628   5.645   -24.732 1.00 12.42 ? 194 ARG D C   1 
ATOM   8001 O  O   . ARG D 1 194 ? 10.859  5.389   -24.515 1.00 13.64 ? 194 ARG D O   1 
ATOM   8002 C  CB  . ARG D 1 194 ? 8.923   5.760   -22.438 1.00 15.76 ? 194 ARG D CB  1 
ATOM   8003 C  CG  . ARG D 1 194 ? 7.825   5.438   -21.457 1.00 20.67 ? 194 ARG D CG  1 
ATOM   8004 C  CD  . ARG D 1 194 ? 6.799   6.532   -21.420 1.00 28.73 ? 194 ARG D CD  1 
ATOM   8005 N  NE  . ARG D 1 194 ? 5.810   6.213   -20.401 1.00 39.63 ? 194 ARG D NE  1 
ATOM   8006 C  CZ  . ARG D 1 194 ? 4.588   6.739   -20.370 1.00 43.62 ? 194 ARG D CZ  1 
ATOM   8007 N  NH1 . ARG D 1 194 ? 4.234   7.630   -21.299 1.00 38.65 ? 194 ARG D NH1 1 
ATOM   8008 N  NH2 . ARG D 1 194 ? 3.720   6.360   -19.424 1.00 38.52 ? 194 ARG D NH2 1 
ATOM   8009 N  N   . GLY D 1 195 ? 9.189   6.194   -25.845 1.00 11.16 ? 195 GLY D N   1 
ATOM   8010 C  CA  . GLY D 1 195 ? 10.127  6.589   -26.852 1.00 11.33 ? 195 GLY D CA  1 
ATOM   8011 C  C   . GLY D 1 195 ? 9.803   7.908   -27.525 1.00 12.12 ? 195 GLY D C   1 
ATOM   8012 O  O   . GLY D 1 195 ? 9.193   8.800   -26.946 1.00 11.92 ? 195 GLY D O   1 
ATOM   8013 N  N   . SER D 1 196 ? 10.123  7.930   -28.804 1.00 10.36 ? 196 SER D N   1 
ATOM   8014 C  CA  . SER D 1 196 ? 9.995   9.183   -29.556 1.00 9.94  ? 196 SER D CA  1 
ATOM   8015 C  C   . SER D 1 196 ? 9.431   8.920   -30.943 1.00 10.45 ? 196 SER D C   1 
ATOM   8016 O  O   . SER D 1 196 ? 9.307   7.762   -31.429 1.00 10.69 ? 196 SER D O   1 
ATOM   8017 C  CB  . SER D 1 196 ? 11.408  9.793   -29.712 1.00 11.64 ? 196 SER D CB  1 
ATOM   8018 O  OG  . SER D 1 196 ? 12.212  9.100   -30.710 1.00 9.97  ? 196 SER D OG  1 
ATOM   8019 N  N   . LEU D 1 197 ? 9.175   10.007  -31.614 1.00 10.46 ? 197 LEU D N   1 
ATOM   8020 C  CA  . LEU D 1 197 ? 9.027   9.920   -33.083 1.00 10.58 ? 197 LEU D CA  1 
ATOM   8021 C  C   . LEU D 1 197 ? 10.314  9.437   -33.679 1.00 10.92 ? 197 LEU D C   1 
ATOM   8022 O  O   . LEU D 1 197 ? 11.404  9.861   -33.232 1.00 11.88 ? 197 LEU D O   1 
ATOM   8023 C  CB  . LEU D 1 197 ? 8.719   11.333  -33.626 1.00 11.30 ? 197 LEU D CB  1 
ATOM   8024 C  CG  . LEU D 1 197 ? 7.348   11.928  -33.309 1.00 12.35 ? 197 LEU D CG  1 
ATOM   8025 C  CD1 . LEU D 1 197 ? 7.409   13.347  -33.849 1.00 12.18 ? 197 LEU D CD1 1 
ATOM   8026 C  CD2 . LEU D 1 197 ? 6.174   11.205  -33.891 1.00 13.32 ? 197 LEU D CD2 1 
ATOM   8027 N  N   . THR D 1 198 ? 10.209  8.640   -34.764 1.00 9.75  ? 198 THR D N   1 
ATOM   8028 C  CA  . THR D 1 198 ? 11.423  8.100   -35.388 1.00 10.08 ? 198 THR D CA  1 
ATOM   8029 C  C   . THR D 1 198 ? 11.828  8.990   -36.600 1.00 10.54 ? 198 THR D C   1 
ATOM   8030 O  O   . THR D 1 198 ? 12.768  8.661   -37.315 1.00 9.91  ? 198 THR D O   1 
ATOM   8031 C  CB  . THR D 1 198 ? 11.311  6.661   -35.869 1.00 10.51 ? 198 THR D CB  1 
ATOM   8032 O  OG1 . THR D 1 198 ? 10.364  6.584   -36.927 1.00 9.84  ? 198 THR D OG1 1 
ATOM   8033 C  CG2 . THR D 1 198 ? 10.808  5.787   -34.789 1.00 10.99 ? 198 THR D CG2 1 
ATOM   8034 N  N   . THR D 1 199 ? 11.106  10.078  -36.783 1.00 9.52  ? 199 THR D N   1 
ATOM   8035 C  CA  . THR D 1 199 ? 11.515  11.113  -37.771 1.00 11.08 ? 199 THR D CA  1 
ATOM   8036 C  C   . THR D 1 199 ? 11.543  12.455  -37.107 1.00 11.54 ? 199 THR D C   1 
ATOM   8037 O  O   . THR D 1 199 ? 10.911  12.614  -36.042 1.00 13.30 ? 199 THR D O   1 
ATOM   8038 C  CB  . THR D 1 199 ? 10.478  11.255  -38.915 1.00 11.93 ? 199 THR D CB  1 
ATOM   8039 O  OG1 . THR D 1 199 ? 9.184   11.549  -38.358 1.00 12.02 ? 199 THR D OG1 1 
ATOM   8040 C  CG2 . THR D 1 199 ? 10.441  9.983   -39.718 1.00 11.40 ? 199 THR D CG2 1 
ATOM   8041 N  N   . PRO D 1 200 ? 12.251  13.423  -37.742 1.00 11.39 ? 200 PRO D N   1 
ATOM   8042 C  CA  . PRO D 1 200 ? 12.181  14.771  -37.263 1.00 11.47 ? 200 PRO D CA  1 
ATOM   8043 C  C   . PRO D 1 200 ? 10.727  15.162  -37.035 1.00 11.63 ? 200 PRO D C   1 
ATOM   8044 O  O   . PRO D 1 200 ? 9.883   14.867  -37.873 1.00 12.47 ? 200 PRO D O   1 
ATOM   8045 C  CB  . PRO D 1 200 ? 12.793  15.560  -38.420 1.00 10.39 ? 200 PRO D CB  1 
ATOM   8046 C  CG  . PRO D 1 200 ? 13.935  14.652  -38.779 1.00 11.10 ? 200 PRO D CG  1 
ATOM   8047 C  CD  . PRO D 1 200 ? 13.205  13.294  -38.848 1.00 10.59 ? 200 PRO D CD  1 
ATOM   8048 N  N   . PRO D 1 201 ? 10.457  15.911  -35.944 1.00 10.84 ? 201 PRO D N   1 
ATOM   8049 C  CA  . PRO D 1 201 ? 11.363  16.448  -34.963 1.00 12.22 ? 201 PRO D CA  1 
ATOM   8050 C  C   . PRO D 1 201 ? 11.789  15.558  -33.835 1.00 12.89 ? 201 PRO D C   1 
ATOM   8051 O  O   . PRO D 1 201 ? 12.431  16.029  -32.882 1.00 12.84 ? 201 PRO D O   1 
ATOM   8052 C  CB  . PRO D 1 201 ? 10.586  17.675  -34.397 1.00 12.45 ? 201 PRO D CB  1 
ATOM   8053 C  CG  . PRO D 1 201 ? 9.356   17.774  -35.222 1.00 15.45 ? 201 PRO D CG  1 
ATOM   8054 C  CD  . PRO D 1 201 ? 9.081   16.401  -35.736 1.00 13.31 ? 201 PRO D CD  1 
ATOM   8055 N  N   . CYS D 1 202 ? 11.427  14.253  -33.905 1.00 10.70 ? 202 CYS D N   1 
ATOM   8056 C  CA  . CYS D 1 202 ? 12.003  13.261  -32.923 1.00 11.21 ? 202 CYS D CA  1 
ATOM   8057 C  C   . CYS D 1 202 ? 11.538  13.534  -31.485 1.00 12.29 ? 202 CYS D C   1 
ATOM   8058 O  O   . CYS D 1 202 ? 12.176  13.098  -30.536 1.00 13.56 ? 202 CYS D O   1 
ATOM   8059 C  CB  . CYS D 1 202 ? 13.556  13.164  -32.910 1.00 11.53 ? 202 CYS D CB  1 
ATOM   8060 S  SG  . CYS D 1 202 ? 14.287  12.841  -34.543 1.00 11.78 ? 202 CYS D SG  1 
ATOM   8061 N  N   . ASN D 1 203 ? 10.391  14.197  -31.371 1.00 11.43 ? 203 ASN D N   1 
ATOM   8062 C  CA  . ASN D 1 203 ? 9.874   14.473  -30.013 1.00 11.95 ? 203 ASN D CA  1 
ATOM   8063 C  C   . ASN D 1 203 ? 9.727   13.211  -29.169 1.00 12.46 ? 203 ASN D C   1 
ATOM   8064 O  O   . ASN D 1 203 ? 9.193   12.196  -29.670 1.00 11.47 ? 203 ASN D O   1 
ATOM   8065 C  CB  . ASN D 1 203 ? 8.563   15.228  -30.072 1.00 12.42 ? 203 ASN D CB  1 
ATOM   8066 C  CG  . ASN D 1 203 ? 8.678   16.449  -30.969 1.00 14.76 ? 203 ASN D CG  1 
ATOM   8067 O  OD1 . ASN D 1 203 ? 8.546   16.326  -32.133 1.00 17.80 ? 203 ASN D OD1 1 
ATOM   8068 N  ND2 . ASN D 1 203 ? 9.001   17.569  -30.439 1.00 18.33 ? 203 ASN D ND2 1 
ATOM   8069 N  N   . PRO D 1 204 ? 10.165  13.269  -27.910 1.00 12.97 ? 204 PRO D N   1 
ATOM   8070 C  CA  . PRO D 1 204 ? 10.170  12.076  -26.994 1.00 12.29 ? 204 PRO D CA  1 
ATOM   8071 C  C   . PRO D 1 204 ? 8.792   12.008  -26.280 1.00 11.20 ? 204 PRO D C   1 
ATOM   8072 O  O   . PRO D 1 204 ? 8.703   12.092  -25.041 1.00 13.34 ? 204 PRO D O   1 
ATOM   8073 C  CB  . PRO D 1 204 ? 11.310  12.389  -26.019 1.00 13.18 ? 204 PRO D CB  1 
ATOM   8074 C  CG  . PRO D 1 204 ? 11.274  13.962  -25.934 1.00 11.82 ? 204 PRO D CG  1 
ATOM   8075 C  CD  . PRO D 1 204 ? 11.022  14.371  -27.378 1.00 12.69 ? 204 PRO D CD  1 
ATOM   8076 N  N   . THR D 1 205 ? 7.762   11.973  -27.097 1.00 11.01 ? 205 THR D N   1 
ATOM   8077 C  CA  . THR D 1 205 ? 6.370   12.040  -26.664 1.00 11.51 ? 205 THR D CA  1 
ATOM   8078 C  C   . THR D 1 205 ? 5.530   10.798  -27.077 1.00 10.54 ? 205 THR D C   1 
ATOM   8079 O  O   . THR D 1 205 ? 4.306   10.824  -26.986 1.00 12.07 ? 205 THR D O   1 
ATOM   8080 C  CB  . THR D 1 205 ? 5.731   13.276  -27.304 1.00 12.07 ? 205 THR D CB  1 
ATOM   8081 O  OG1 . THR D 1 205 ? 5.847   13.149  -28.733 1.00 13.27 ? 205 THR D OG1 1 
ATOM   8082 C  CG2 . THR D 1 205 ? 6.422   14.667  -26.838 1.00 15.12 ? 205 THR D CG2 1 
ATOM   8083 N  N   . VAL D 1 206 ? 6.168   9.700   -27.459 1.00 12.48 ? 206 VAL D N   1 
ATOM   8084 C  CA  . VAL D 1 206 ? 5.452   8.579   -28.001 1.00 11.52 ? 206 VAL D CA  1 
ATOM   8085 C  C   . VAL D 1 206 ? 5.514   7.382   -27.036 1.00 10.81 ? 206 VAL D C   1 
ATOM   8086 O  O   . VAL D 1 206 ? 6.572   6.944   -26.612 1.00 11.52 ? 206 VAL D O   1 
ATOM   8087 C  CB  . VAL D 1 206 ? 6.070   8.105   -29.363 1.00 11.23 ? 206 VAL D CB  1 
ATOM   8088 C  CG1 . VAL D 1 206 ? 5.340   6.840   -29.844 1.00 11.82 ? 206 VAL D CG1 1 
ATOM   8089 C  CG2 . VAL D 1 206 ? 6.000   9.232   -30.373 1.00 11.37 ? 206 VAL D CG2 1 
ATOM   8090 N  N   . LEU D 1 207 ? 4.355   6.843   -26.721 1.00 12.15 ? 207 LEU D N   1 
ATOM   8091 C  CA  . LEU D 1 207 ? 4.212   5.628   -25.950 1.00 13.22 ? 207 LEU D CA  1 
ATOM   8092 C  C   . LEU D 1 207 ? 4.123   4.517   -27.017 1.00 10.61 ? 207 LEU D C   1 
ATOM   8093 O  O   . LEU D 1 207 ? 3.200   4.463   -27.802 1.00 12.14 ? 207 LEU D O   1 
ATOM   8094 C  CB  . LEU D 1 207 ? 2.968   5.597   -25.111 1.00 15.67 ? 207 LEU D CB  1 
ATOM   8095 C  CG  . LEU D 1 207 ? 2.941   4.281   -24.343 1.00 17.57 ? 207 LEU D CG  1 
ATOM   8096 C  CD1 . LEU D 1 207 ? 4.034   4.237   -23.282 1.00 17.85 ? 207 LEU D CD1 1 
ATOM   8097 C  CD2 . LEU D 1 207 ? 1.567   4.205   -23.714 1.00 21.17 ? 207 LEU D CD2 1 
ATOM   8098 N  N   . TRP D 1 208 ? 5.133   3.677   -27.077 1.00 9.04  ? 208 TRP D N   1 
ATOM   8099 C  CA  . TRP D 1 208 ? 5.187   2.604   -28.203 1.00 10.01 ? 208 TRP D CA  1 
ATOM   8100 C  C   . TRP D 1 208 ? 4.651   1.291   -27.776 1.00 9.96  ? 208 TRP D C   1 
ATOM   8101 O  O   . TRP D 1 208 ? 4.942   0.851   -26.639 1.00 11.13 ? 208 TRP D O   1 
ATOM   8102 C  CB  . TRP D 1 208 ? 6.646   2.376   -28.673 1.00 10.29 ? 208 TRP D CB  1 
ATOM   8103 C  CG  . TRP D 1 208 ? 7.154   3.447   -29.591 1.00 9.83  ? 208 TRP D CG  1 
ATOM   8104 C  CD1 . TRP D 1 208 ? 7.894   4.580   -29.265 1.00 9.69  ? 208 TRP D CD1 1 
ATOM   8105 C  CD2 . TRP D 1 208 ? 6.969   3.508   -31.033 1.00 9.72  ? 208 TRP D CD2 1 
ATOM   8106 N  NE1 . TRP D 1 208 ? 8.172   5.316   -30.388 1.00 10.94 ? 208 TRP D NE1 1 
ATOM   8107 C  CE2 . TRP D 1 208 ? 7.644   4.726   -31.484 1.00 9.74  ? 208 TRP D CE2 1 
ATOM   8108 C  CE3 . TRP D 1 208 ? 6.338   2.705   -31.965 1.00 11.40 ? 208 TRP D CE3 1 
ATOM   8109 C  CZ2 . TRP D 1 208 ? 7.668   5.097   -32.813 1.00 9.41  ? 208 TRP D CZ2 1 
ATOM   8110 C  CZ3 . TRP D 1 208 ? 6.368   3.090   -33.300 1.00 9.89  ? 208 TRP D CZ3 1 
ATOM   8111 C  CH2 . TRP D 1 208 ? 7.018   4.257   -33.713 1.00 12.18 ? 208 TRP D CH2 1 
ATOM   8112 N  N   . THR D 1 209 ? 3.918   0.668   -28.725 1.00 9.43  ? 209 THR D N   1 
ATOM   8113 C  CA  . THR D 1 209 ? 3.410   -0.702  -28.519 1.00 8.64  ? 209 THR D CA  1 
ATOM   8114 C  C   . THR D 1 209 ? 3.874   -1.395  -29.796 1.00 9.14  ? 209 THR D C   1 
ATOM   8115 O  O   . THR D 1 209 ? 3.375   -1.024  -30.845 1.00 10.18 ? 209 THR D O   1 
ATOM   8116 C  CB  . THR D 1 209 ? 1.877   -0.684  -28.405 1.00 10.52 ? 209 THR D CB  1 
ATOM   8117 O  OG1 . THR D 1 209 ? 1.548   0.036   -27.196 1.00 11.57 ? 209 THR D OG1 1 
ATOM   8118 C  CG2 . THR D 1 209 ? 1.371   -2.126  -28.177 1.00 11.80 ? 209 THR D CG2 1 
ATOM   8119 N  N   . VAL D 1 210 ? 4.730   -2.419  -29.649 1.00 9.60  ? 210 VAL D N   1 
ATOM   8120 C  CA  . VAL D 1 210 ? 5.184   -3.202  -30.794 1.00 8.77  ? 210 VAL D CA  1 
ATOM   8121 C  C   . VAL D 1 210 ? 4.578   -4.624  -30.549 1.00 8.58  ? 210 VAL D C   1 
ATOM   8122 O  O   . VAL D 1 210 ? 4.874   -5.201  -29.527 1.00 11.00 ? 210 VAL D O   1 
ATOM   8123 C  CB  . VAL D 1 210 ? 6.710   -3.220  -30.837 1.00 8.80  ? 210 VAL D CB  1 
ATOM   8124 C  CG1 . VAL D 1 210 ? 7.172   -4.092  -32.016 1.00 10.68 ? 210 VAL D CG1 1 
ATOM   8125 C  CG2 . VAL D 1 210 ? 7.268   -1.788  -30.939 1.00 9.67  ? 210 VAL D CG2 1 
ATOM   8126 N  N   . PHE D 1 211 ? 3.723   -5.068  -31.473 1.00 9.92  ? 211 PHE D N   1 
ATOM   8127 C  CA  . PHE D 1 211 ? 3.133   -6.410  -31.296 1.00 10.11 ? 211 PHE D CA  1 
ATOM   8128 C  C   . PHE D 1 211 ? 4.227   -7.439  -31.387 1.00 12.26 ? 211 PHE D C   1 
ATOM   8129 O  O   . PHE D 1 211 ? 5.109   -7.386  -32.236 1.00 14.33 ? 211 PHE D O   1 
ATOM   8130 C  CB  . PHE D 1 211 ? 2.021   -6.612  -32.288 1.00 11.19 ? 211 PHE D CB  1 
ATOM   8131 C  CG  . PHE D 1 211 ? 0.856   -5.696  -32.027 1.00 10.81 ? 211 PHE D CG  1 
ATOM   8132 C  CD1 . PHE D 1 211 ? 0.077   -5.874  -30.841 1.00 11.60 ? 211 PHE D CD1 1 
ATOM   8133 C  CD2 . PHE D 1 211 ? 0.614   -4.554  -32.860 1.00 12.10 ? 211 PHE D CD2 1 
ATOM   8134 C  CE1 . PHE D 1 211 ? -0.957  -4.967  -30.529 1.00 11.96 ? 211 PHE D CE1 1 
ATOM   8135 C  CE2 . PHE D 1 211 ? -0.458  -3.707  -32.578 1.00 12.17 ? 211 PHE D CE2 1 
ATOM   8136 C  CZ  . PHE D 1 211 ? -1.253  -3.915  -31.430 1.00 10.56 ? 211 PHE D CZ  1 
ATOM   8137 N  N   . ARG D 1 212 ? 4.073   -8.442  -30.558 1.00 11.64 ? 212 ARG D N   1 
ATOM   8138 C  CA  . ARG D 1 212 ? 5.045   -9.599  -30.553 1.00 12.19 ? 212 ARG D CA  1 
ATOM   8139 C  C   . ARG D 1 212 ? 5.105   -10.333 -31.876 1.00 12.52 ? 212 ARG D C   1 
ATOM   8140 O  O   . ARG D 1 212 ? 6.175   -10.852 -32.271 1.00 15.95 ? 212 ARG D O   1 
ATOM   8141 C  CB  . ARG D 1 212 ? 4.759   -10.549 -29.377 1.00 12.83 ? 212 ARG D CB  1 
ATOM   8142 C  CG  . ARG D 1 212 ? 5.780   -11.664 -29.265 1.00 12.56 ? 212 ARG D CG  1 
ATOM   8143 C  CD  . ARG D 1 212 ? 5.262   -12.739 -28.302 1.00 15.13 ? 212 ARG D CD  1 
ATOM   8144 N  NE  . ARG D 1 212 ? 6.356   -13.680 -27.963 1.00 17.19 ? 212 ARG D NE  1 
ATOM   8145 C  CZ  . ARG D 1 212 ? 6.186   -14.681 -27.106 1.00 22.34 ? 212 ARG D CZ  1 
ATOM   8146 N  NH1 . ARG D 1 212 ? 4.997   -14.911 -26.550 1.00 27.20 ? 212 ARG D NH1 1 
ATOM   8147 N  NH2 . ARG D 1 212 ? 7.211   -15.470 -26.826 1.00 25.43 ? 212 ARG D NH2 1 
ATOM   8148 N  N   . ASN D 1 213 ? 3.972   -10.558 -32.518 1.00 11.87 ? 213 ASN D N   1 
ATOM   8149 C  CA  . ASN D 1 213 ? 3.938   -11.375 -33.706 1.00 14.63 ? 213 ASN D CA  1 
ATOM   8150 C  C   . ASN D 1 213 ? 3.940   -10.510 -34.975 1.00 13.49 ? 213 ASN D C   1 
ATOM   8151 O  O   . ASN D 1 213 ? 3.221   -9.500  -35.032 1.00 13.10 ? 213 ASN D O   1 
ATOM   8152 C  CB  . ASN D 1 213 ? 2.652   -12.176 -33.686 1.00 15.30 ? 213 ASN D CB  1 
ATOM   8153 C  CG  . ASN D 1 213 ? 2.665   -13.177 -32.602 1.00 18.14 ? 213 ASN D CG  1 
ATOM   8154 O  OD1 . ASN D 1 213 ? 1.712   -13.258 -31.815 1.00 22.10 ? 213 ASN D OD1 1 
ATOM   8155 N  ND2 . ASN D 1 213 ? 3.793   -13.855 -32.478 1.00 16.80 ? 213 ASN D ND2 1 
ATOM   8156 N  N   . PRO D 1 214 ? 4.734   -10.874 -35.999 1.00 12.86 ? 214 PRO D N   1 
ATOM   8157 C  CA  . PRO D 1 214 ? 4.665   -10.193 -37.309 1.00 13.59 ? 214 PRO D CA  1 
ATOM   8158 C  C   . PRO D 1 214 ? 3.487   -10.609 -38.135 1.00 13.18 ? 214 PRO D C   1 
ATOM   8159 O  O   . PRO D 1 214 ? 2.834   -11.638 -37.849 1.00 14.44 ? 214 PRO D O   1 
ATOM   8160 C  CB  . PRO D 1 214 ? 5.968   -10.619 -38.003 1.00 14.20 ? 214 PRO D CB  1 
ATOM   8161 C  CG  . PRO D 1 214 ? 6.096   -12.052 -37.522 1.00 14.22 ? 214 PRO D CG  1 
ATOM   8162 C  CD  . PRO D 1 214 ? 5.741   -11.985 -36.010 1.00 12.95 ? 214 PRO D CD  1 
ATOM   8163 N  N   . VAL D 1 215 ? 3.207   -9.786  -39.160 1.00 12.39 ? 215 VAL D N   1 
ATOM   8164 C  CA  . VAL D 1 215 ? 2.388   -10.200 -40.296 1.00 11.89 ? 215 VAL D CA  1 
ATOM   8165 C  C   . VAL D 1 215 ? 3.297   -10.522 -41.442 1.00 12.02 ? 215 VAL D C   1 
ATOM   8166 O  O   . VAL D 1 215 ? 4.529   -10.261 -41.356 1.00 11.91 ? 215 VAL D O   1 
ATOM   8167 C  CB  . VAL D 1 215 ? 1.295   -9.141  -40.691 1.00 10.77 ? 215 VAL D CB  1 
ATOM   8168 C  CG1 . VAL D 1 215 ? 0.355   -8.900  -39.496 1.00 12.10 ? 215 VAL D CG1 1 
ATOM   8169 C  CG2 . VAL D 1 215 ? 1.976   -7.843  -41.193 1.00 10.68 ? 215 VAL D CG2 1 
ATOM   8170 N  N   . GLN D 1 216 ? 2.715   -11.060 -42.496 1.00 12.01 ? 216 GLN D N   1 
ATOM   8171 C  CA  . GLN D 1 216 ? 3.386   -11.344 -43.770 1.00 11.78 ? 216 GLN D CA  1 
ATOM   8172 C  C   . GLN D 1 216 ? 2.783   -10.563 -44.896 1.00 12.76 ? 216 GLN D C   1 
ATOM   8173 O  O   . GLN D 1 216 ? 1.552   -10.462 -45.006 1.00 13.28 ? 216 GLN D O   1 
ATOM   8174 C  CB  . GLN D 1 216 ? 3.361   -12.865 -44.132 1.00 12.82 ? 216 GLN D CB  1 
ATOM   8175 C  CG  . GLN D 1 216 ? 4.109   -13.661 -43.152 1.00 15.14 ? 216 GLN D CG  1 
ATOM   8176 C  CD  . GLN D 1 216 ? 4.106   -15.131 -43.537 1.00 15.69 ? 216 GLN D CD  1 
ATOM   8177 O  OE1 . GLN D 1 216 ? 3.574   -15.524 -44.560 1.00 15.55 ? 216 GLN D OE1 1 
ATOM   8178 N  NE2 . GLN D 1 216 ? 4.747   -15.984 -42.639 1.00 23.58 ? 216 GLN D NE2 1 
ATOM   8179 N  N   . ILE D 1 217 ? 3.641   -10.109 -45.806 1.00 11.38 ? 217 ILE D N   1 
ATOM   8180 C  CA  . ILE D 1 217 ? 3.233   -9.633  -47.134 1.00 11.21 ? 217 ILE D CA  1 
ATOM   8181 C  C   . ILE D 1 217 ? 4.183   -10.351 -48.097 1.00 11.01 ? 217 ILE D C   1 
ATOM   8182 O  O   . ILE D 1 217 ? 5.308   -10.759 -47.700 1.00 9.99  ? 217 ILE D O   1 
ATOM   8183 C  CB  . ILE D 1 217 ? 3.230   -8.062  -47.311 1.00 10.15 ? 217 ILE D CB  1 
ATOM   8184 C  CG1 . ILE D 1 217 ? 4.694   -7.522  -47.316 1.00 10.37 ? 217 ILE D CG1 1 
ATOM   8185 C  CG2 . ILE D 1 217 ? 2.347   -7.360  -46.230 1.00 11.34 ? 217 ILE D CG2 1 
ATOM   8186 C  CD1 . ILE D 1 217 ? 4.736   -5.967  -47.429 1.00 10.63 ? 217 ILE D CD1 1 
ATOM   8187 N  N   . SER D 1 218 ? 3.805   -10.408 -49.360 1.00 10.25 ? 218 SER D N   1 
ATOM   8188 C  CA  . SER D 1 218 ? 4.664   -11.143 -50.298 1.00 11.77 ? 218 SER D CA  1 
ATOM   8189 C  C   . SER D 1 218 ? 5.869   -10.378 -50.814 1.00 10.78 ? 218 SER D C   1 
ATOM   8190 O  O   . SER D 1 218 ? 5.953   -9.156  -50.732 1.00 11.88 ? 218 SER D O   1 
ATOM   8191 C  CB  . SER D 1 218 ? 3.854   -11.645 -51.476 1.00 12.06 ? 218 SER D CB  1 
ATOM   8192 O  OG  . SER D 1 218 ? 3.515   -10.558 -52.325 1.00 10.57 ? 218 SER D OG  1 
ATOM   8193 N  N   . GLN D 1 219 ? 6.837   -11.126 -51.332 1.00 11.55 ? 219 GLN D N   1 
ATOM   8194 C  CA  . GLN D 1 219 ? 7.950   -10.499 -52.103 1.00 13.24 ? 219 GLN D CA  1 
ATOM   8195 C  C   . GLN D 1 219 ? 7.511   -9.474  -53.180 1.00 13.68 ? 219 GLN D C   1 
ATOM   8196 O  O   . GLN D 1 219 ? 8.097   -8.362  -53.257 1.00 12.57 ? 219 GLN D O   1 
ATOM   8197 C  CB  . GLN D 1 219 ? 8.736   -11.609 -52.818 1.00 14.84 ? 219 GLN D CB  1 
ATOM   8198 C  CG  . GLN D 1 219 ? 10.123  -11.177 -53.321 1.00 18.45 ? 219 GLN D CG  1 
ATOM   8199 C  CD  . GLN D 1 219 ? 10.067  -10.270 -54.554 1.00 22.27 ? 219 GLN D CD  1 
ATOM   8200 O  OE1 . GLN D 1 219 ? 9.270   -10.520 -55.443 1.00 27.34 ? 219 GLN D OE1 1 
ATOM   8201 N  NE2 . GLN D 1 219 ? 10.927  -9.184  -54.591 1.00 23.13 ? 219 GLN D NE2 1 
ATOM   8202 N  N   . GLU D 1 220 ? 6.443   -9.776  -53.901 1.00 12.97 ? 220 GLU D N   1 
ATOM   8203 C  CA  . GLU D 1 220 ? 5.992   -8.943  -54.970 1.00 13.79 ? 220 GLU D CA  1 
ATOM   8204 C  C   . GLU D 1 220 ? 5.402   -7.680  -54.342 1.00 13.35 ? 220 GLU D C   1 
ATOM   8205 O  O   . GLU D 1 220 ? 5.608   -6.584  -54.843 1.00 13.36 ? 220 GLU D O   1 
ATOM   8206 C  CB  . GLU D 1 220 ? 4.952   -9.671  -55.817 1.00 16.66 ? 220 GLU D CB  1 
ATOM   8207 C  CG  . GLU D 1 220 ? 5.609   -10.754 -56.687 1.00 16.75 ? 220 GLU D CG  1 
ATOM   8208 C  CD  . GLU D 1 220 ? 5.845   -12.074 -55.959 1.00 21.70 ? 220 GLU D CD  1 
ATOM   8209 O  OE1 . GLU D 1 220 ? 5.465   -12.249 -54.766 1.00 19.78 ? 220 GLU D OE1 1 
ATOM   8210 O  OE2 . GLU D 1 220 ? 6.418   -12.965 -56.630 1.00 26.01 ? 220 GLU D OE2 1 
ATOM   8211 N  N   . GLN D 1 221 ? 4.732   -7.833  -53.169 1.00 13.39 ? 221 GLN D N   1 
ATOM   8212 C  CA  . GLN D 1 221 ? 4.203   -6.663  -52.465 1.00 13.77 ? 221 GLN D CA  1 
ATOM   8213 C  C   . GLN D 1 221 ? 5.285   -5.779  -51.988 1.00 12.86 ? 221 GLN D C   1 
ATOM   8214 O  O   . GLN D 1 221 ? 5.231   -4.535  -52.147 1.00 12.77 ? 221 GLN D O   1 
ATOM   8215 C  CB  . GLN D 1 221 ? 3.300   -7.071  -51.315 1.00 12.50 ? 221 GLN D CB  1 
ATOM   8216 C  CG  . GLN D 1 221 ? 1.969   -7.599  -51.862 1.00 12.61 ? 221 GLN D CG  1 
ATOM   8217 C  CD  . GLN D 1 221 ? 1.038   -7.995  -50.727 1.00 12.32 ? 221 GLN D CD  1 
ATOM   8218 O  OE1 . GLN D 1 221 ? 1.338   -8.920  -49.924 1.00 13.66 ? 221 GLN D OE1 1 
ATOM   8219 N  NE2 . GLN D 1 221 ? -0.092  -7.257  -50.588 1.00 10.66 ? 221 GLN D NE2 1 
ATOM   8220 N  N   . LEU D 1 222 ? 6.330   -6.398  -51.425 1.00 12.02 ? 222 LEU D N   1 
ATOM   8221 C  CA  . LEU D 1 222 ? 7.445   -5.604  -50.909 1.00 12.45 ? 222 LEU D CA  1 
ATOM   8222 C  C   . LEU D 1 222 ? 8.221   -4.910  -52.095 1.00 12.32 ? 222 LEU D C   1 
ATOM   8223 O  O   . LEU D 1 222 ? 8.596   -3.713  -51.997 1.00 13.18 ? 222 LEU D O   1 
ATOM   8224 C  CB  . LEU D 1 222 ? 8.401   -6.529  -50.157 1.00 12.58 ? 222 LEU D CB  1 
ATOM   8225 C  CG  . LEU D 1 222 ? 7.980   -6.832  -48.740 1.00 15.36 ? 222 LEU D CG  1 
ATOM   8226 C  CD1 . LEU D 1 222 ? 8.700   -8.081  -48.215 1.00 16.32 ? 222 LEU D CD1 1 
ATOM   8227 C  CD2 . LEU D 1 222 ? 8.429   -5.687  -47.869 1.00 15.19 ? 222 LEU D CD2 1 
ATOM   8228 N  N   . LEU D 1 223 ? 8.336   -5.576  -53.238 1.00 12.58 ? 223 LEU D N   1 
ATOM   8229 C  CA  . LEU D 1 223 ? 9.081   -5.009  -54.333 1.00 11.91 ? 223 LEU D CA  1 
ATOM   8230 C  C   . LEU D 1 223 ? 8.261   -3.857  -54.878 1.00 13.65 ? 223 LEU D C   1 
ATOM   8231 O  O   . LEU D 1 223 ? 8.849   -2.812  -55.233 1.00 12.66 ? 223 LEU D O   1 
ATOM   8232 C  CB  . LEU D 1 223 ? 9.304   -6.114  -55.435 1.00 12.02 ? 223 LEU D CB  1 
ATOM   8233 C  CG  . LEU D 1 223 ? 10.053  -5.469  -56.660 1.00 14.81 ? 223 LEU D CG  1 
ATOM   8234 C  CD1 . LEU D 1 223 ? 11.468  -5.036  -56.263 1.00 17.45 ? 223 LEU D CD1 1 
ATOM   8235 C  CD2 . LEU D 1 223 ? 10.121  -6.582  -57.710 1.00 16.51 ? 223 LEU D CD2 1 
ATOM   8236 N  N   . ALA D 1 224 ? 6.927   -4.003  -54.892 1.00 12.98 ? 224 ALA D N   1 
ATOM   8237 C  CA  . ALA D 1 224 ? 6.134   -2.810  -55.335 1.00 14.04 ? 224 ALA D CA  1 
ATOM   8238 C  C   . ALA D 1 224 ? 6.267   -1.619  -54.420 1.00 16.28 ? 224 ALA D C   1 
ATOM   8239 O  O   . ALA D 1 224 ? 6.452   -0.521  -54.869 1.00 16.60 ? 224 ALA D O   1 
ATOM   8240 C  CB  . ALA D 1 224 ? 4.704   -3.195  -55.585 1.00 13.67 ? 224 ALA D CB  1 
ATOM   8241 N  N   . LEU D 1 225 ? 6.259   -1.876  -53.124 1.00 14.16 ? 225 LEU D N   1 
ATOM   8242 C  CA  . LEU D 1 225 ? 6.436   -0.843  -52.109 1.00 13.59 ? 225 LEU D CA  1 
ATOM   8243 C  C   . LEU D 1 225 ? 7.774   -0.138  -52.273 1.00 13.33 ? 225 LEU D C   1 
ATOM   8244 O  O   . LEU D 1 225 ? 7.872   1.068   -52.210 1.00 15.19 ? 225 LEU D O   1 
ATOM   8245 C  CB  . LEU D 1 225 ? 6.202   -1.471  -50.737 1.00 12.87 ? 225 LEU D CB  1 
ATOM   8246 C  CG  . LEU D 1 225 ? 6.266   -0.488  -49.556 1.00 13.74 ? 225 LEU D CG  1 
ATOM   8247 C  CD1 . LEU D 1 225 ? 5.200   0.667   -49.642 1.00 13.80 ? 225 LEU D CD1 1 
ATOM   8248 C  CD2 . LEU D 1 225 ? 6.170   -1.182  -48.213 1.00 12.88 ? 225 LEU D CD2 1 
ATOM   8249 N  N   . GLU D 1 226 ? 8.792   -0.959  -52.495 1.00 13.21 ? 226 GLU D N   1 
ATOM   8250 C  CA  . GLU D 1 226 ? 10.155  -0.438  -52.593 1.00 12.17 ? 226 GLU D CA  1 
ATOM   8251 C  C   . GLU D 1 226 ? 10.503  0.241   -53.880 1.00 14.71 ? 226 GLU D C   1 
ATOM   8252 O  O   . GLU D 1 226 ? 11.615  0.777   -53.978 1.00 17.68 ? 226 GLU D O   1 
ATOM   8253 C  CB  . GLU D 1 226 ? 11.142  -1.628  -52.445 1.00 12.41 ? 226 GLU D CB  1 
ATOM   8254 C  CG  . GLU D 1 226 ? 11.138  -2.273  -51.068 1.00 11.93 ? 226 GLU D CG  1 
ATOM   8255 C  CD  . GLU D 1 226 ? 11.522  -3.775  -51.096 1.00 12.60 ? 226 GLU D CD  1 
ATOM   8256 O  OE1 . GLU D 1 226 ? 11.743  -4.334  -52.210 1.00 12.05 ? 226 GLU D OE1 1 
ATOM   8257 O  OE2 . GLU D 1 226 ? 11.575  -4.345  -50.013 1.00 14.09 ? 226 GLU D OE2 1 
ATOM   8258 N  N   . THR D 1 227 ? 9.638   0.162   -54.891 1.00 13.84 ? 227 THR D N   1 
ATOM   8259 C  CA  . THR D 1 227 ? 9.926   0.716   -56.230 1.00 12.75 ? 227 THR D CA  1 
ATOM   8260 C  C   . THR D 1 227 ? 8.902   1.753   -56.652 1.00 15.05 ? 227 THR D C   1 
ATOM   8261 O  O   . THR D 1 227 ? 9.144   2.406   -57.642 1.00 15.35 ? 227 THR D O   1 
ATOM   8262 C  CB  . THR D 1 227 ? 10.134  -0.350  -57.321 1.00 15.15 ? 227 THR D CB  1 
ATOM   8263 O  OG1 . THR D 1 227 ? 8.926   -1.088  -57.507 1.00 13.81 ? 227 THR D OG1 1 
ATOM   8264 C  CG2 . THR D 1 227 ? 11.385  -1.300  -56.995 1.00 15.95 ? 227 THR D CG2 1 
ATOM   8265 N  N   . ALA D 1 228 ? 7.806   1.916   -55.909 1.00 14.98 ? 228 ALA D N   1 
ATOM   8266 C  CA  . ALA D 1 228 ? 6.716   2.741   -56.385 1.00 16.07 ? 228 ALA D CA  1 
ATOM   8267 C  C   . ALA D 1 228 ? 6.987   4.228   -56.169 1.00 17.48 ? 228 ALA D C   1 
ATOM   8268 O  O   . ALA D 1 228 ? 6.406   5.041   -56.906 1.00 18.74 ? 228 ALA D O   1 
ATOM   8269 C  CB  . ALA D 1 228 ? 5.422   2.352   -55.667 1.00 15.90 ? 228 ALA D CB  1 
ATOM   8270 N  N   . LEU D 1 229 ? 7.716   4.590   -55.115 1.00 14.27 ? 229 LEU D N   1 
ATOM   8271 C  CA  . LEU D 1 229 ? 7.566   5.946   -54.619 1.00 12.80 ? 229 LEU D CA  1 
ATOM   8272 C  C   . LEU D 1 229 ? 8.823   6.725   -54.715 1.00 12.97 ? 229 LEU D C   1 
ATOM   8273 O  O   . LEU D 1 229 ? 9.898   6.201   -54.594 1.00 13.23 ? 229 LEU D O   1 
ATOM   8274 C  CB  . LEU D 1 229 ? 7.121   5.943   -53.119 1.00 13.33 ? 229 LEU D CB  1 
ATOM   8275 C  CG  . LEU D 1 229 ? 5.805   5.116   -52.956 1.00 14.70 ? 229 LEU D CG  1 
ATOM   8276 C  CD1 . LEU D 1 229 ? 5.510   5.027   -51.463 1.00 14.78 ? 229 LEU D CD1 1 
ATOM   8277 C  CD2 . LEU D 1 229 ? 4.618   5.751   -53.729 1.00 18.69 ? 229 LEU D CD2 1 
ATOM   8278 N  N   . TYR D 1 230 ? 8.636   8.027   -54.926 1.00 11.75 ? 230 TYR D N   1 
ATOM   8279 C  CA  . TYR D 1 230 ? 9.775   8.988   -54.886 1.00 14.47 ? 230 TYR D CA  1 
ATOM   8280 C  C   . TYR D 1 230 ? 9.587   9.977   -53.763 1.00 13.89 ? 230 TYR D C   1 
ATOM   8281 O  O   . TYR D 1 230 ? 8.447   10.351  -53.368 1.00 15.64 ? 230 TYR D O   1 
ATOM   8282 C  CB  . TYR D 1 230 ? 9.812   9.796   -56.189 1.00 12.99 ? 230 TYR D CB  1 
ATOM   8283 C  CG  . TYR D 1 230 ? 10.364  8.951   -57.282 1.00 18.12 ? 230 TYR D CG  1 
ATOM   8284 C  CD1 . TYR D 1 230 ? 11.728  8.976   -57.563 1.00 18.65 ? 230 TYR D CD1 1 
ATOM   8285 C  CD2 . TYR D 1 230 ? 9.544   8.042   -57.992 1.00 20.31 ? 230 TYR D CD2 1 
ATOM   8286 C  CE1 . TYR D 1 230 ? 12.273  8.132   -58.521 1.00 23.61 ? 230 TYR D CE1 1 
ATOM   8287 C  CE2 . TYR D 1 230 ? 10.083  7.233   -58.987 1.00 24.17 ? 230 TYR D CE2 1 
ATOM   8288 C  CZ  . TYR D 1 230 ? 11.440  7.251   -59.221 1.00 24.15 ? 230 TYR D CZ  1 
ATOM   8289 O  OH  . TYR D 1 230 ? 11.962  6.416   -60.203 1.00 29.65 ? 230 TYR D OH  1 
ATOM   8290 N  N   . CYS D 1 231 ? 10.721  10.484  -53.228 1.00 15.11 ? 231 CYS D N   1 
ATOM   8291 C  CA  . CYS D 1 231 ? 10.677  11.466  -52.159 1.00 14.70 ? 231 CYS D CA  1 
ATOM   8292 C  C   . CYS D 1 231 ? 10.473  12.910  -52.726 1.00 13.87 ? 231 CYS D C   1 
ATOM   8293 O  O   . CYS D 1 231 ? 10.219  13.869  -51.985 1.00 17.02 ? 231 CYS D O   1 
ATOM   8294 C  CB  . CYS D 1 231 ? 12.013  11.568  -51.487 1.00 16.03 ? 231 CYS D CB  1 
ATOM   8295 S  SG  . CYS D 1 231 ? 12.509  10.127  -50.555 1.00 16.46 ? 231 CYS D SG  1 
ATOM   8296 N  N   . THR D 1 232 ? 10.704  13.003  -54.027 1.00 13.15 ? 232 THR D N   1 
ATOM   8297 C  CA  . THR D 1 232 ? 10.731  14.320  -54.752 1.00 14.32 ? 232 THR D CA  1 
ATOM   8298 C  C   . THR D 1 232 ? 9.469   14.627  -55.591 1.00 16.46 ? 232 THR D C   1 
ATOM   8299 O  O   . THR D 1 232 ? 8.686   13.735  -55.950 1.00 16.96 ? 232 THR D O   1 
ATOM   8300 C  CB  . THR D 1 232 ? 11.977  14.287  -55.685 1.00 15.35 ? 232 THR D CB  1 
ATOM   8301 O  OG1 . THR D 1 232 ? 12.083  12.996  -56.306 1.00 16.27 ? 232 THR D OG1 1 
ATOM   8302 C  CG2 . THR D 1 232 ? 13.213  14.559  -54.870 1.00 17.89 ? 232 THR D CG2 1 
ATOM   8303 N  N   . HIS D 1 233 ? 9.277   15.920  -55.905 1.00 17.60 ? 233 HIS D N   1 
ATOM   8304 C  CA  . HIS D 1 233 ? 8.156   16.374  -56.690 1.00 18.36 ? 233 HIS D CA  1 
ATOM   8305 C  C   . HIS D 1 233 ? 8.435   15.923  -58.064 1.00 19.44 ? 233 HIS D C   1 
ATOM   8306 O  O   . HIS D 1 233 ? 9.585   15.703  -58.436 1.00 19.23 ? 233 HIS D O   1 
ATOM   8307 C  CB  . HIS D 1 233 ? 8.106   17.899  -56.734 1.00 21.69 ? 233 HIS D CB  1 
ATOM   8308 C  CG  . HIS D 1 233 ? 7.644   18.533  -55.462 1.00 24.73 ? 233 HIS D CG  1 
ATOM   8309 N  ND1 . HIS D 1 233 ? 8.486   19.255  -54.667 1.00 27.90 ? 233 HIS D ND1 1 
ATOM   8310 C  CD2 . HIS D 1 233 ? 6.401   18.588  -54.865 1.00 27.09 ? 233 HIS D CD2 1 
ATOM   8311 C  CE1 . HIS D 1 233 ? 7.797   19.732  -53.607 1.00 30.35 ? 233 HIS D CE1 1 
ATOM   8312 N  NE2 . HIS D 1 233 ? 6.524   19.346  -53.736 1.00 28.17 ? 233 HIS D NE2 1 
ATOM   8313 N  N   . MET D 1 234 ? 7.354   15.697  -58.788 1.00 22.58 ? 234 MET D N   1 
ATOM   8314 C  CA  . MET D 1 234 ? 7.386   15.168  -60.151 1.00 23.92 ? 234 MET D CA  1 
ATOM   8315 C  C   . MET D 1 234 ? 8.353   15.979  -61.042 1.00 27.47 ? 234 MET D C   1 
ATOM   8316 O  O   . MET D 1 234 ? 9.080   15.404  -61.868 1.00 27.13 ? 234 MET D O   1 
ATOM   8317 C  CB  . MET D 1 234 ? 5.955   15.263  -60.659 1.00 28.57 ? 234 MET D CB  1 
ATOM   8318 C  CG  . MET D 1 234 ? 5.661   14.571  -61.946 1.00 33.75 ? 234 MET D CG  1 
ATOM   8319 S  SD  . MET D 1 234 ? 3.852   14.597  -62.172 1.00 38.87 ? 234 MET D SD  1 
ATOM   8320 C  CE  . MET D 1 234 ? 3.716   13.241  -63.338 1.00 41.55 ? 234 MET D CE  1 
ATOM   8321 N  N   . ASP D 1 235 ? 8.454   17.297  -60.800 1.00 24.32 ? 235 ASP D N   1 
ATOM   8322 C  CA  . ASP D 1 235 ? 9.320   18.108  -61.639 1.00 28.96 ? 235 ASP D CA  1 
ATOM   8323 C  C   . ASP D 1 235 ? 10.756  18.322  -61.169 1.00 25.27 ? 235 ASP D C   1 
ATOM   8324 O  O   . ASP D 1 235 ? 11.500  19.113  -61.758 1.00 27.46 ? 235 ASP D O   1 
ATOM   8325 C  CB  . ASP D 1 235 ? 8.638   19.464  -61.896 1.00 30.58 ? 235 ASP D CB  1 
ATOM   8326 C  CG  . ASP D 1 235 ? 8.433   20.267  -60.615 1.00 34.59 ? 235 ASP D CG  1 
ATOM   8327 O  OD1 . ASP D 1 235 ? 8.868   19.809  -59.521 1.00 37.24 ? 235 ASP D OD1 1 
ATOM   8328 O  OD2 . ASP D 1 235 ? 7.828   21.347  -60.706 1.00 32.74 ? 235 ASP D OD2 1 
ATOM   8329 N  N   . ASP D 1 236 ? 11.185  17.621  -60.124 1.00 24.50 ? 236 ASP D N   1 
ATOM   8330 C  CA  . ASP D 1 236 ? 12.524  17.787  -59.594 1.00 24.20 ? 236 ASP D CA  1 
ATOM   8331 C  C   . ASP D 1 236 ? 13.578  17.229  -60.571 1.00 22.94 ? 236 ASP D C   1 
ATOM   8332 O  O   . ASP D 1 236 ? 13.538  16.050  -60.970 1.00 24.12 ? 236 ASP D O   1 
ATOM   8333 C  CB  . ASP D 1 236 ? 12.654  17.079  -58.204 1.00 22.56 ? 236 ASP D CB  1 
ATOM   8334 C  CG  . ASP D 1 236 ? 13.825  17.583  -57.390 1.00 23.65 ? 236 ASP D CG  1 
ATOM   8335 O  OD1 . ASP D 1 236 ? 14.932  17.787  -57.928 1.00 23.90 ? 236 ASP D OD1 1 
ATOM   8336 O  OD2 . ASP D 1 236 ? 13.670  17.747  -56.158 1.00 26.64 ? 236 ASP D OD2 1 
ATOM   8337 N  N   . PRO D 1 237 ? 14.570  18.044  -60.925 1.00 24.72 ? 237 PRO D N   1 
ATOM   8338 C  CA  . PRO D 1 237 ? 15.683  17.592  -61.763 1.00 25.48 ? 237 PRO D CA  1 
ATOM   8339 C  C   . PRO D 1 237 ? 16.622  16.564  -61.079 1.00 24.10 ? 237 PRO D C   1 
ATOM   8340 O  O   . PRO D 1 237 ? 17.437  15.919  -61.762 1.00 25.91 ? 237 PRO D O   1 
ATOM   8341 C  CB  . PRO D 1 237 ? 16.423  18.927  -62.079 1.00 26.30 ? 237 PRO D CB  1 
ATOM   8342 C  CG  . PRO D 1 237 ? 16.173  19.765  -60.869 1.00 26.03 ? 237 PRO D CG  1 
ATOM   8343 C  CD  . PRO D 1 237 ? 14.719  19.461  -60.539 1.00 25.67 ? 237 PRO D CD  1 
ATOM   8344 N  N   . SER D 1 238 ? 16.451  16.373  -59.747 1.00 21.58 ? 238 SER D N   1 
ATOM   8345 C  CA  . SER D 1 238 ? 17.263  15.477  -58.963 1.00 22.26 ? 238 SER D CA  1 
ATOM   8346 C  C   . SER D 1 238 ? 16.359  14.497  -58.215 1.00 18.34 ? 238 SER D C   1 
ATOM   8347 O  O   . SER D 1 238 ? 16.290  14.553  -56.995 1.00 18.80 ? 238 SER D O   1 
ATOM   8348 C  CB  . SER D 1 238 ? 18.110  16.206  -57.931 1.00 26.57 ? 238 SER D CB  1 
ATOM   8349 O  OG  . SER D 1 238 ? 19.452  16.149  -58.338 1.00 35.88 ? 238 SER D OG  1 
ATOM   8350 N  N   . PRO D 1 239 ? 15.736  13.586  -58.962 1.00 20.12 ? 239 PRO D N   1 
ATOM   8351 C  CA  . PRO D 1 239 ? 14.807  12.662  -58.291 1.00 18.41 ? 239 PRO D CA  1 
ATOM   8352 C  C   . PRO D 1 239 ? 15.491  11.748  -57.323 1.00 19.03 ? 239 PRO D C   1 
ATOM   8353 O  O   . PRO D 1 239 ? 16.631  11.271  -57.581 1.00 19.96 ? 239 PRO D O   1 
ATOM   8354 C  CB  . PRO D 1 239 ? 14.170  11.838  -59.429 1.00 20.46 ? 239 PRO D CB  1 
ATOM   8355 C  CG  . PRO D 1 239 ? 14.889  12.205  -60.662 1.00 19.99 ? 239 PRO D CG  1 
ATOM   8356 C  CD  . PRO D 1 239 ? 15.857  13.331  -60.404 1.00 19.78 ? 239 PRO D CD  1 
ATOM   8357 N  N   . ARG D 1 240 ? 14.774  11.431  -56.222 1.00 17.94 ? 240 ARG D N   1 
ATOM   8358 C  CA  . ARG D 1 240 ? 15.287  10.555  -55.156 1.00 16.41 ? 240 ARG D CA  1 
ATOM   8359 C  C   . ARG D 1 240 ? 14.193  9.489   -54.835 1.00 15.45 ? 240 ARG D C   1 
ATOM   8360 O  O   . ARG D 1 240 ? 13.032  9.903   -54.491 1.00 16.64 ? 240 ARG D O   1 
ATOM   8361 C  CB  . ARG D 1 240 ? 15.567  11.329  -53.898 1.00 16.51 ? 240 ARG D CB  1 
ATOM   8362 C  CG  . ARG D 1 240 ? 16.832  12.232  -54.028 1.00 18.84 ? 240 ARG D CG  1 
ATOM   8363 C  CD  . ARG D 1 240 ? 17.115  12.973  -52.719 1.00 18.64 ? 240 ARG D CD  1 
ATOM   8364 N  NE  . ARG D 1 240 ? 16.143  14.066  -52.504 1.00 18.05 ? 240 ARG D NE  1 
ATOM   8365 C  CZ  . ARG D 1 240 ? 15.177  14.031  -51.561 1.00 18.74 ? 240 ARG D CZ  1 
ATOM   8366 N  NH1 . ARG D 1 240 ? 15.031  12.967  -50.727 1.00 17.34 ? 240 ARG D NH1 1 
ATOM   8367 N  NH2 . ARG D 1 240 ? 14.324  15.050  -51.460 1.00 19.72 ? 240 ARG D NH2 1 
ATOM   8368 N  N   . GLU D 1 241 ? 14.535  8.211   -55.013 1.00 14.60 ? 241 GLU D N   1 
ATOM   8369 C  CA  . GLU D 1 241 ? 13.616  7.153   -54.590 1.00 13.79 ? 241 GLU D CA  1 
ATOM   8370 C  C   . GLU D 1 241 ? 13.326  7.127   -53.110 1.00 13.90 ? 241 GLU D C   1 
ATOM   8371 O  O   . GLU D 1 241 ? 14.206  7.321   -52.268 1.00 14.24 ? 241 GLU D O   1 
ATOM   8372 C  CB  . GLU D 1 241 ? 14.212  5.844   -55.008 1.00 15.15 ? 241 GLU D CB  1 
ATOM   8373 C  CG  . GLU D 1 241 ? 14.377  5.794   -56.525 1.00 19.66 ? 241 GLU D CG  1 
ATOM   8374 C  CD  . GLU D 1 241 ? 15.313  4.703   -56.938 1.00 26.33 ? 241 GLU D CD  1 
ATOM   8375 O  OE1 . GLU D 1 241 ? 16.534  4.809   -56.691 1.00 28.93 ? 241 GLU D OE1 1 
ATOM   8376 O  OE2 . GLU D 1 241 ? 14.822  3.755   -57.560 1.00 31.11 ? 241 GLU D OE2 1 
ATOM   8377 N  N   . MET D 1 242 ? 12.043  6.863   -52.787 1.00 11.13 ? 242 MET D N   1 
ATOM   8378 C  CA  . MET D 1 242 ? 11.698  6.663   -51.375 1.00 10.43 ? 242 MET D CA  1 
ATOM   8379 C  C   . MET D 1 242 ? 12.024  5.211   -50.960 1.00 11.02 ? 242 MET D C   1 
ATOM   8380 O  O   . MET D 1 242 ? 11.210  4.300   -51.158 1.00 11.60 ? 242 MET D O   1 
ATOM   8381 C  CB  . MET D 1 242 ? 10.223  7.066   -51.143 1.00 10.52 ? 242 MET D CB  1 
ATOM   8382 C  CG  . MET D 1 242 ? 9.923   7.161   -49.643 1.00 10.59 ? 242 MET D CG  1 
ATOM   8383 S  SD  . MET D 1 242 ? 8.184   7.438   -49.361 1.00 12.63 ? 242 MET D SD  1 
ATOM   8384 C  CE  . MET D 1 242 ? 8.137   9.183   -49.862 1.00 12.56 ? 242 MET D CE  1 
ATOM   8385 N  N   . ILE D 1 243 ? 13.242  5.013   -50.464 1.00 11.78 ? 243 ILE D N   1 
ATOM   8386 C  CA  . ILE D 1 243 ? 13.767  3.685   -50.104 1.00 11.28 ? 243 ILE D CA  1 
ATOM   8387 C  C   . ILE D 1 243 ? 14.548  3.847   -48.784 1.00 10.69 ? 243 ILE D C   1 
ATOM   8388 O  O   . ILE D 1 243 ? 14.999  5.004   -48.441 1.00 11.46 ? 243 ILE D O   1 
ATOM   8389 C  CB  . ILE D 1 243 ? 14.680  3.133   -51.174 1.00 13.02 ? 243 ILE D CB  1 
ATOM   8390 C  CG1 . ILE D 1 243 ? 15.873  4.109   -51.452 1.00 12.56 ? 243 ILE D CG1 1 
ATOM   8391 C  CG2 . ILE D 1 243 ? 13.885  2.658   -52.365 1.00 15.25 ? 243 ILE D CG2 1 
ATOM   8392 C  CD1 . ILE D 1 243 ? 16.731  3.663   -52.596 1.00 14.48 ? 243 ILE D CD1 1 
ATOM   8393 N  N   . ASN D 1 244 ? 14.725  2.714   -48.098 1.00 9.91  ? 244 ASN D N   1 
ATOM   8394 C  CA  . ASN D 1 244 ? 15.478  2.705   -46.833 1.00 10.23 ? 244 ASN D CA  1 
ATOM   8395 C  C   . ASN D 1 244 ? 15.089  3.859   -45.896 1.00 9.99  ? 244 ASN D C   1 
ATOM   8396 O  O   . ASN D 1 244 ? 15.937  4.511   -45.238 1.00 11.47 ? 244 ASN D O   1 
ATOM   8397 C  CB  . ASN D 1 244 ? 16.972  2.850   -47.188 1.00 12.16 ? 244 ASN D CB  1 
ATOM   8398 C  CG  . ASN D 1 244 ? 17.409  1.835   -48.187 1.00 14.39 ? 244 ASN D CG  1 
ATOM   8399 O  OD1 . ASN D 1 244 ? 16.974  0.658   -48.140 1.00 13.42 ? 244 ASN D OD1 1 
ATOM   8400 N  ND2 . ASN D 1 244 ? 18.293  2.275   -49.141 1.00 15.78 ? 244 ASN D ND2 1 
ATOM   8401 N  N   . ASN D 1 245 ? 13.765  4.067   -45.822 1.00 10.27 ? 245 ASN D N   1 
ATOM   8402 C  CA  . ASN D 1 245 ? 13.178  5.078   -44.961 1.00 10.02 ? 245 ASN D CA  1 
ATOM   8403 C  C   . ASN D 1 245 ? 12.933  4.611   -43.516 1.00 10.50 ? 245 ASN D C   1 
ATOM   8404 O  O   . ASN D 1 245 ? 11.808  4.703   -42.999 1.00 12.16 ? 245 ASN D O   1 
ATOM   8405 C  CB  . ASN D 1 245 ? 11.879  5.690   -45.579 1.00 9.71  ? 245 ASN D CB  1 
ATOM   8406 C  CG  . ASN D 1 245 ? 10.788  4.690   -45.770 1.00 10.15 ? 245 ASN D CG  1 
ATOM   8407 O  OD1 . ASN D 1 245 ? 10.976  3.480   -45.792 1.00 9.95  ? 245 ASN D OD1 1 
ATOM   8408 N  ND2 . ASN D 1 245 ? 9.572   5.214   -45.820 1.00 11.87 ? 245 ASN D ND2 1 
ATOM   8409 N  N   . PHE D 1 246 ? 13.966  4.073   -42.895 1.00 10.07 ? 246 PHE D N   1 
ATOM   8410 C  CA  . PHE D 1 246 ? 13.938  3.655   -41.498 1.00 8.93  ? 246 PHE D CA  1 
ATOM   8411 C  C   . PHE D 1 246 ? 15.156  4.264   -40.811 1.00 9.76  ? 246 PHE D C   1 
ATOM   8412 O  O   . PHE D 1 246 ? 16.237  4.444   -41.426 1.00 9.80  ? 246 PHE D O   1 
ATOM   8413 C  CB  . PHE D 1 246 ? 13.967  2.053   -41.444 1.00 9.90  ? 246 PHE D CB  1 
ATOM   8414 C  CG  . PHE D 1 246 ? 15.240  1.404   -42.021 1.00 10.60 ? 246 PHE D CG  1 
ATOM   8415 C  CD1 . PHE D 1 246 ? 16.319  0.977   -41.187 1.00 11.27 ? 246 PHE D CD1 1 
ATOM   8416 C  CD2 . PHE D 1 246 ? 15.323  1.135   -43.407 1.00 10.40 ? 246 PHE D CD2 1 
ATOM   8417 C  CE1 . PHE D 1 246 ? 17.463  0.439   -41.741 1.00 12.82 ? 246 PHE D CE1 1 
ATOM   8418 C  CE2 . PHE D 1 246 ? 16.460  0.504   -43.957 1.00 10.48 ? 246 PHE D CE2 1 
ATOM   8419 C  CZ  . PHE D 1 246 ? 17.525  0.178   -43.129 1.00 12.30 ? 246 PHE D CZ  1 
ATOM   8420 N  N   . ARG D 1 247 ? 14.926  4.593   -39.551 1.00 9.52  ? 247 ARG D N   1 
ATOM   8421 C  CA  . ARG D 1 247 ? 16.020  5.048   -38.693 1.00 11.01 ? 247 ARG D CA  1 
ATOM   8422 C  C   . ARG D 1 247 ? 16.772  3.902   -38.017 1.00 9.83  ? 247 ARG D C   1 
ATOM   8423 O  O   . ARG D 1 247 ? 16.158  2.887   -37.663 1.00 9.65  ? 247 ARG D O   1 
ATOM   8424 C  CB  . ARG D 1 247 ? 15.430  6.042   -37.647 1.00 10.73 ? 247 ARG D CB  1 
ATOM   8425 C  CG  . ARG D 1 247 ? 16.433  6.855   -36.870 1.00 11.09 ? 247 ARG D CG  1 
ATOM   8426 C  CD  . ARG D 1 247 ? 15.777  7.584   -35.691 1.00 9.78  ? 247 ARG D CD  1 
ATOM   8427 N  NE  . ARG D 1 247 ? 16.632  8.649   -35.146 1.00 9.91  ? 247 ARG D NE  1 
ATOM   8428 C  CZ  . ARG D 1 247 ? 16.375  9.349   -34.030 1.00 10.96 ? 247 ARG D CZ  1 
ATOM   8429 N  NH1 . ARG D 1 247 ? 15.251  9.117   -33.295 1.00 11.92 ? 247 ARG D NH1 1 
ATOM   8430 N  NH2 . ARG D 1 247 ? 17.176  10.379  -33.691 1.00 10.97 ? 247 ARG D NH2 1 
ATOM   8431 N  N   . GLN D 1 248 ? 18.117  4.014   -37.869 1.00 9.22  ? 248 GLN D N   1 
ATOM   8432 C  CA  . GLN D 1 248 ? 18.872  3.037   -37.099 1.00 10.38 ? 248 GLN D CA  1 
ATOM   8433 C  C   . GLN D 1 248 ? 18.366  2.995   -35.653 1.00 9.52  ? 248 GLN D C   1 
ATOM   8434 O  O   . GLN D 1 248 ? 17.834  3.981   -35.114 1.00 9.96  ? 248 GLN D O   1 
ATOM   8435 C  CB  . GLN D 1 248 ? 20.364  3.411   -37.042 1.00 9.27  ? 248 GLN D CB  1 
ATOM   8436 C  CG  . GLN D 1 248 ? 20.994  3.421   -38.434 1.00 11.37 ? 248 GLN D CG  1 
ATOM   8437 C  CD  . GLN D 1 248 ? 20.993  2.023   -39.055 1.00 11.33 ? 248 GLN D CD  1 
ATOM   8438 O  OE1 . GLN D 1 248 ? 20.105  1.656   -39.860 1.00 12.83 ? 248 GLN D OE1 1 
ATOM   8439 N  NE2 . GLN D 1 248 ? 22.043  1.259   -38.739 1.00 11.54 ? 248 GLN D NE2 1 
ATOM   8440 N  N   . VAL D 1 249 ? 18.481  1.814   -35.065 1.00 9.86  ? 249 VAL D N   1 
ATOM   8441 C  CA  . VAL D 1 249 ? 18.157  1.712   -33.624 1.00 9.94  ? 249 VAL D CA  1 
ATOM   8442 C  C   . VAL D 1 249 ? 19.035  2.647   -32.761 1.00 11.13 ? 249 VAL D C   1 
ATOM   8443 O  O   . VAL D 1 249 ? 20.213  2.952   -33.094 1.00 11.24 ? 249 VAL D O   1 
ATOM   8444 C  CB  . VAL D 1 249 ? 18.173  0.284   -33.052 1.00 10.54 ? 249 VAL D CB  1 
ATOM   8445 C  CG1 . VAL D 1 249 ? 17.064  -0.575  -33.738 1.00 11.77 ? 249 VAL D CG1 1 
ATOM   8446 C  CG2 . VAL D 1 249 ? 19.533  -0.389  -33.153 1.00 11.71 ? 249 VAL D CG2 1 
ATOM   8447 N  N   . GLN D 1 250 ? 18.475  2.977   -31.599 1.00 10.05 ? 250 GLN D N   1 
ATOM   8448 C  CA  . GLN D 1 250 ? 19.033  3.995   -30.657 1.00 11.25 ? 250 GLN D CA  1 
ATOM   8449 C  C   . GLN D 1 250 ? 19.533  3.423   -29.318 1.00 11.90 ? 250 GLN D C   1 
ATOM   8450 O  O   . GLN D 1 250 ? 19.141  2.363   -28.866 1.00 12.50 ? 250 GLN D O   1 
ATOM   8451 C  CB  . GLN D 1 250 ? 17.890  5.007   -30.330 1.00 10.47 ? 250 GLN D CB  1 
ATOM   8452 C  CG  . GLN D 1 250 ? 17.250  5.650   -31.580 1.00 9.50  ? 250 GLN D CG  1 
ATOM   8453 C  CD  . GLN D 1 250 ? 18.228  6.520   -32.290 1.00 10.73 ? 250 GLN D CD  1 
ATOM   8454 O  OE1 . GLN D 1 250 ? 18.572  7.544   -31.753 1.00 11.14 ? 250 GLN D OE1 1 
ATOM   8455 N  NE2 . GLN D 1 250 ? 18.500  6.246   -33.577 1.00 9.18  ? 250 GLN D NE2 1 
ATOM   8456 N  N   . LYS D 1 251 ? 20.420  4.159   -28.661 1.00 12.06 ? 251 LYS D N   1 
ATOM   8457 C  CA  . LYS D 1 251 ? 20.782  3.779   -27.303 1.00 12.50 ? 251 LYS D CA  1 
ATOM   8458 C  C   . LYS D 1 251 ? 19.554  3.690   -26.422 1.00 13.70 ? 251 LYS D C   1 
ATOM   8459 O  O   . LYS D 1 251 ? 18.629  4.491   -26.513 1.00 13.02 ? 251 LYS D O   1 
ATOM   8460 C  CB  . LYS D 1 251 ? 21.694  4.842   -26.777 1.00 12.95 ? 251 LYS D CB  1 
ATOM   8461 C  CG  . LYS D 1 251 ? 23.096  4.881   -27.413 1.00 11.60 ? 251 LYS D CG  1 
ATOM   8462 C  CD  . LYS D 1 251 ? 23.907  3.745   -26.897 1.00 13.85 ? 251 LYS D CD  1 
ATOM   8463 C  CE  . LYS D 1 251 ? 25.398  3.852   -27.217 1.00 11.91 ? 251 LYS D CE  1 
ATOM   8464 N  NZ  . LYS D 1 251 ? 25.587  3.761   -28.755 1.00 9.34  ? 251 LYS D NZ  1 
ATOM   8465 N  N   . PHE D 1 252 ? 19.601  2.718   -25.509 1.00 14.93 ? 252 PHE D N   1 
ATOM   8466 C  CA  . PHE D 1 252 ? 18.539  2.591   -24.507 1.00 16.17 ? 252 PHE D CA  1 
ATOM   8467 C  C   . PHE D 1 252 ? 18.417  3.701   -23.464 1.00 20.71 ? 252 PHE D C   1 
ATOM   8468 O  O   . PHE D 1 252 ? 17.349  3.896   -22.931 1.00 20.44 ? 252 PHE D O   1 
ATOM   8469 C  CB  . PHE D 1 252 ? 18.686  1.220   -23.830 1.00 17.68 ? 252 PHE D CB  1 
ATOM   8470 C  CG  . PHE D 1 252 ? 18.123  0.133   -24.678 1.00 20.85 ? 252 PHE D CG  1 
ATOM   8471 C  CD1 . PHE D 1 252 ? 16.767  -0.196  -24.563 1.00 24.96 ? 252 PHE D CD1 1 
ATOM   8472 C  CD2 . PHE D 1 252 ? 18.903  -0.472  -25.685 1.00 23.77 ? 252 PHE D CD2 1 
ATOM   8473 C  CE1 . PHE D 1 252 ? 16.194  -1.167  -25.391 1.00 26.06 ? 252 PHE D CE1 1 
ATOM   8474 C  CE2 . PHE D 1 252 ? 18.321  -1.438  -26.533 1.00 27.08 ? 252 PHE D CE2 1 
ATOM   8475 C  CZ  . PHE D 1 252 ? 16.974  -1.745  -26.393 1.00 25.96 ? 252 PHE D CZ  1 
ATOM   8476 N  N   . ASP D 1 253 ? 19.476  4.434   -23.137 1.00 19.81 ? 253 ASP D N   1 
ATOM   8477 C  CA  . ASP D 1 253 ? 19.313  5.494   -22.124 1.00 20.96 ? 253 ASP D CA  1 
ATOM   8478 C  C   . ASP D 1 253 ? 18.676  4.937   -20.829 1.00 22.61 ? 253 ASP D C   1 
ATOM   8479 O  O   . ASP D 1 253 ? 17.817  5.602   -20.241 1.00 23.85 ? 253 ASP D O   1 
ATOM   8480 C  CB  . ASP D 1 253 ? 18.517  6.705   -22.660 1.00 24.89 ? 253 ASP D CB  1 
ATOM   8481 C  CG  . ASP D 1 253 ? 19.209  7.390   -23.849 1.00 26.45 ? 253 ASP D CG  1 
ATOM   8482 O  OD1 . ASP D 1 253 ? 20.440  7.294   -23.961 1.00 25.40 ? 253 ASP D OD1 1 
ATOM   8483 O  OD2 . ASP D 1 253 ? 18.526  8.036   -24.659 1.00 25.60 ? 253 ASP D OD2 1 
ATOM   8484 N  N   . GLU D 1 254 ? 19.099  3.730   -20.408 1.00 20.99 ? 254 GLU D N   1 
ATOM   8485 C  CA  . GLU D 1 254 ? 18.636  3.139   -19.126 1.00 23.54 ? 254 GLU D CA  1 
ATOM   8486 C  C   . GLU D 1 254 ? 17.142  2.629   -19.136 1.00 24.58 ? 254 GLU D C   1 
ATOM   8487 O  O   . GLU D 1 254 ? 16.636  2.106   -18.110 1.00 22.11 ? 254 GLU D O   1 
ATOM   8488 C  CB  . GLU D 1 254 ? 18.865  4.101   -17.945 1.00 29.19 ? 254 GLU D CB  1 
ATOM   8489 C  CG  . GLU D 1 254 ? 20.325  4.280   -17.477 1.00 37.11 ? 254 GLU D CG  1 
ATOM   8490 C  CD  . GLU D 1 254 ? 20.416  5.125   -16.193 1.00 48.98 ? 254 GLU D CD  1 
ATOM   8491 O  OE1 . GLU D 1 254 ? 20.325  4.557   -15.067 1.00 54.31 ? 254 GLU D OE1 1 
ATOM   8492 O  OE2 . GLU D 1 254 ? 20.558  6.371   -16.303 1.00 56.94 ? 254 GLU D OE2 1 
ATOM   8493 N  N   . ARG D 1 255 ? 16.431  2.815   -20.251 1.00 19.09 ? 255 ARG D N   1 
ATOM   8494 C  CA  . ARG D 1 255 ? 15.110  2.248   -20.412 1.00 18.97 ? 255 ARG D CA  1 
ATOM   8495 C  C   . ARG D 1 255 ? 15.083  0.703   -20.372 1.00 19.57 ? 255 ARG D C   1 
ATOM   8496 O  O   . ARG D 1 255 ? 16.007  0.002   -20.831 1.00 22.44 ? 255 ARG D O   1 
ATOM   8497 C  CB  . ARG D 1 255 ? 14.479  2.699   -21.758 1.00 16.85 ? 255 ARG D CB  1 
ATOM   8498 C  CG  . ARG D 1 255 ? 14.162  4.189   -21.782 1.00 19.59 ? 255 ARG D CG  1 
ATOM   8499 C  CD  . ARG D 1 255 ? 13.664  4.543   -23.199 1.00 18.74 ? 255 ARG D CD  1 
ATOM   8500 N  NE  . ARG D 1 255 ? 14.738  4.558   -24.207 1.00 18.01 ? 255 ARG D NE  1 
ATOM   8501 C  CZ  . ARG D 1 255 ? 14.580  4.855   -25.522 1.00 18.40 ? 255 ARG D CZ  1 
ATOM   8502 N  NH1 . ARG D 1 255 ? 13.368  5.142   -26.045 1.00 13.63 ? 255 ARG D NH1 1 
ATOM   8503 N  NH2 . ARG D 1 255 ? 15.664  4.875   -26.347 1.00 16.88 ? 255 ARG D NH2 1 
ATOM   8504 N  N   . LEU D 1 256 ? 14.001  0.152   -19.796 1.00 16.72 ? 256 LEU D N   1 
ATOM   8505 C  CA  . LEU D 1 256 ? 13.615  -1.217  -20.098 1.00 15.99 ? 256 LEU D CA  1 
ATOM   8506 C  C   . LEU D 1 256 ? 12.426  -1.234  -21.084 1.00 15.28 ? 256 LEU D C   1 
ATOM   8507 O  O   . LEU D 1 256 ? 11.756  -0.193  -21.339 1.00 18.54 ? 256 LEU D O   1 
ATOM   8508 C  CB  . LEU D 1 256 ? 13.185  -1.898  -18.813 1.00 18.24 ? 256 LEU D CB  1 
ATOM   8509 C  CG  . LEU D 1 256 ? 14.242  -1.965  -17.758 1.00 19.27 ? 256 LEU D CG  1 
ATOM   8510 C  CD1 . LEU D 1 256 ? 13.616  -2.644  -16.531 1.00 20.73 ? 256 LEU D CD1 1 
ATOM   8511 C  CD2 . LEU D 1 256 ? 15.556  -2.638  -18.226 1.00 19.94 ? 256 LEU D CD2 1 
ATOM   8512 N  N   . VAL D 1 257 ? 12.203  -2.403  -21.694 1.00 15.09 ? 257 VAL D N   1 
ATOM   8513 C  CA  . VAL D 1 257 ? 11.021  -2.589  -22.562 1.00 14.54 ? 257 VAL D CA  1 
ATOM   8514 C  C   . VAL D 1 257 ? 10.172  -3.561  -21.789 1.00 14.35 ? 257 VAL D C   1 
ATOM   8515 O  O   . VAL D 1 257 ? 10.594  -4.698  -21.472 1.00 14.68 ? 257 VAL D O   1 
ATOM   8516 C  CB  . VAL D 1 257 ? 11.362  -3.128  -24.001 1.00 13.02 ? 257 VAL D CB  1 
ATOM   8517 C  CG1 . VAL D 1 257 ? 10.104  -3.602  -24.708 1.00 12.91 ? 257 VAL D CG1 1 
ATOM   8518 C  CG2 . VAL D 1 257 ? 12.098  -2.064  -24.826 1.00 14.94 ? 257 VAL D CG2 1 
ATOM   8519 N  N   . TYR D 1 258 ? 8.956   -3.172  -21.486 1.00 12.91 ? 258 TYR D N   1 
ATOM   8520 C  CA  . TYR D 1 258 ? 8.015   -4.033  -20.706 1.00 15.00 ? 258 TYR D CA  1 
ATOM   8521 C  C   . TYR D 1 258 ? 7.222   -4.910  -21.622 1.00 14.35 ? 258 TYR D C   1 
ATOM   8522 O  O   . TYR D 1 258 ? 6.871   -4.528  -22.764 1.00 13.31 ? 258 TYR D O   1 
ATOM   8523 C  CB  . TYR D 1 258 ? 7.093   -3.150  -19.869 1.00 15.45 ? 258 TYR D CB  1 
ATOM   8524 C  CG  . TYR D 1 258 ? 7.973   -2.302  -18.961 1.00 15.32 ? 258 TYR D CG  1 
ATOM   8525 C  CD1 . TYR D 1 258 ? 8.490   -2.838  -17.759 1.00 15.97 ? 258 TYR D CD1 1 
ATOM   8526 C  CD2 . TYR D 1 258 ? 8.409   -1.029  -19.399 1.00 16.96 ? 258 TYR D CD2 1 
ATOM   8527 C  CE1 . TYR D 1 258 ? 9.357   -2.110  -16.978 1.00 18.36 ? 258 TYR D CE1 1 
ATOM   8528 C  CE2 . TYR D 1 258 ? 9.273   -0.289  -18.609 1.00 17.94 ? 258 TYR D CE2 1 
ATOM   8529 C  CZ  . TYR D 1 258 ? 9.731   -0.809  -17.402 1.00 19.24 ? 258 TYR D CZ  1 
ATOM   8530 O  OH  . TYR D 1 258 ? 10.591  -0.055  -16.628 1.00 21.54 ? 258 TYR D OH  1 
ATOM   8531 N  N   . THR D 1 259 ? 6.979   -6.150  -21.234 1.00 12.66 ? 259 THR D N   1 
ATOM   8532 C  CA  . THR D 1 259 ? 6.239   -7.034  -22.116 1.00 12.71 ? 259 THR D CA  1 
ATOM   8533 C  C   . THR D 1 259 ? 4.960   -7.550  -21.430 1.00 13.54 ? 259 THR D C   1 
ATOM   8534 O  O   . THR D 1 259 ? 4.928   -7.607  -20.190 1.00 14.56 ? 259 THR D O   1 
ATOM   8535 C  CB  . THR D 1 259 ? 7.105   -8.208  -22.518 1.00 11.75 ? 259 THR D CB  1 
ATOM   8536 O  OG1 . THR D 1 259 ? 7.529   -8.930  -21.327 1.00 15.06 ? 259 THR D OG1 1 
ATOM   8537 C  CG2 . THR D 1 259 ? 8.394   -7.717  -23.247 1.00 11.80 ? 259 THR D CG2 1 
ATOM   8538 N  N   . SER D 1 260 ? 3.972   -7.913  -22.234 1.00 13.28 ? 260 SER D N   1 
ATOM   8539 C  CA  . SER D 1 260 ? 2.712   -8.498  -21.683 1.00 13.13 ? 260 SER D CA  1 
ATOM   8540 C  C   . SER D 1 260 ? 2.777   -10.033 -21.672 1.00 16.50 ? 260 SER D C   1 
ATOM   8541 O  O   . SER D 1 260 ? 1.733   -10.715 -21.417 1.00 18.94 ? 260 SER D O   1 
ATOM   8542 C  CB  . SER D 1 260 ? 1.492   -7.997  -22.467 1.00 13.29 ? 260 SER D CB  1 
ATOM   8543 O  OG  . SER D 1 260 ? 1.591   -8.524  -23.819 1.00 14.90 ? 260 SER D OG  1 
ATOM   8544 N  N   . PHE D 1 261 ? 3.965   -10.571 -21.934 1.00 16.27 ? 261 PHE D N   1 
ATOM   8545 C  CA  . PHE D 1 261 ? 4.096   -12.045 -22.077 1.00 17.16 ? 261 PHE D CA  1 
ATOM   8546 C  C   . PHE D 1 261 ? 5.404   -12.409 -21.380 1.00 19.48 ? 261 PHE D C   1 
ATOM   8547 O  O   . PHE D 1 261 ? 6.315   -11.583 -21.243 1.00 18.49 ? 261 PHE D O   1 
ATOM   8548 C  CB  . PHE D 1 261 ? 4.101   -12.509 -23.539 1.00 17.35 ? 261 PHE D CB  1 
ATOM   8549 C  CG  . PHE D 1 261 ? 5.151   -11.840 -24.374 1.00 17.59 ? 261 PHE D CG  1 
ATOM   8550 C  CD1 . PHE D 1 261 ? 6.391   -12.432 -24.552 1.00 17.98 ? 261 PHE D CD1 1 
ATOM   8551 C  CD2 . PHE D 1 261 ? 4.904   -10.596 -25.007 1.00 17.22 ? 261 PHE D CD2 1 
ATOM   8552 C  CE1 . PHE D 1 261 ? 7.373   -11.821 -25.344 1.00 19.84 ? 261 PHE D CE1 1 
ATOM   8553 C  CE2 . PHE D 1 261 ? 5.912   -9.989  -25.828 1.00 17.51 ? 261 PHE D CE2 1 
ATOM   8554 C  CZ  . PHE D 1 261 ? 7.133   -10.577 -25.935 1.00 19.91 ? 261 PHE D CZ  1 
ATOM   8555 N  N   . SER D 1 262 ? 5.529   -13.655 -20.937 1.00 27.71 ? 262 SER D N   1 
ATOM   8556 C  CA  . SER D 1 262 ? 6.829   -14.146 -20.496 1.00 31.31 ? 262 SER D CA  1 
ATOM   8557 C  C   . SER D 1 262 ? 7.551   -15.008 -21.534 1.00 37.77 ? 262 SER D C   1 
ATOM   8558 O  O   . SER D 1 262 ? 8.793   -14.964 -21.637 1.00 40.90 ? 262 SER D O   1 
ATOM   8559 C  CB  . SER D 1 262 ? 6.690   -14.888 -19.176 1.00 38.60 ? 262 SER D CB  1 
ATOM   8560 O  OG  . SER D 1 262 ? 6.284   -13.973 -18.184 1.00 39.22 ? 262 SER D OG  1 
ATOM   8561 N  N   . GLN D 1 263 ? 6.789   -15.797 -22.289 1.00 41.17 ? 263 GLN D N   1 
ATOM   8562 C  CA  . GLN D 1 263 ? 7.344   -16.613 -23.390 1.00 47.96 ? 263 GLN D CA  1 
ATOM   8563 C  C   . GLN D 1 263 ? 6.246   -17.202 -24.302 1.00 51.58 ? 263 GLN D C   1 
ATOM   8564 O  O   . GLN D 1 263 ? 6.510   -18.051 -25.180 1.00 47.44 ? 263 GLN D O   1 
ATOM   8565 C  CB  . GLN D 1 263 ? 8.305   -17.714 -22.870 1.00 52.50 ? 263 GLN D CB  1 
ATOM   8566 C  CG  . GLN D 1 263 ? 8.223   -18.059 -21.380 1.00 54.41 ? 263 GLN D CG  1 
ATOM   8567 C  CD  . GLN D 1 263 ? 7.168   -19.096 -21.014 1.00 57.94 ? 263 GLN D CD  1 
ATOM   8568 O  OE1 . GLN D 1 263 ? 6.274   -18.825 -20.212 1.00 60.01 ? 263 GLN D OE1 1 
ATOM   8569 N  NE2 . GLN D 1 263 ? 7.293   -20.303 -21.570 1.00 61.42 ? 263 GLN D NE2 1 
HETATM 8570 ZN ZN  . ZN  E 2 .   ? 22.811  0.503   12.292  1.00 10.09 ? 301 ZN  A ZN  1 
HETATM 8571 C  C1  . EDO F 3 .   ? 26.098  -8.725  29.872  1.00 24.68 ? 302 EDO A C1  1 
HETATM 8572 O  O1  . EDO F 3 .   ? 25.951  -9.889  29.029  1.00 24.08 ? 302 EDO A O1  1 
HETATM 8573 C  C2  . EDO F 3 .   ? 27.043  -8.986  31.035  1.00 28.81 ? 302 EDO A C2  1 
HETATM 8574 O  O2  . EDO F 3 .   ? 28.382  -9.312  30.565  1.00 27.31 ? 302 EDO A O2  1 
HETATM 8575 O  O19 . 5EF G 4 .   ? 23.693  8.764   13.028  1.00 40.40 ? 303 5EF A O19 1 
HETATM 8576 C  C17 . 5EF G 4 .   ? 24.265  8.217   15.219  1.00 34.82 ? 303 5EF A C17 1 
HETATM 8577 C  C6  . 5EF G 4 .   ? 23.472  4.011   12.799  1.00 15.94 ? 303 5EF A C6  1 
HETATM 8578 F  F11 . 5EF G 4 .   ? 22.434  3.210   13.195  1.00 16.67 ? 303 5EF A F11 1 
HETATM 8579 C  C5  . 5EF G 4 .   ? 24.051  3.910   11.535  1.00 15.28 ? 303 5EF A C5  1 
HETATM 8580 F  F12 . 5EF G 4 .   ? 23.333  4.951   14.990  1.00 18.81 ? 303 5EF A F12 1 
HETATM 8581 F  F13 . 5EF G 4 .   ? 25.730  4.653   10.145  1.00 18.92 ? 303 5EF A F13 1 
HETATM 8582 O  O16 . 5EF G 4 .   ? 26.804  7.640   14.412  1.00 26.92 ? 303 5EF A O16 1 
HETATM 8583 S  S14 . 5EF G 4 .   ? 25.440  6.942   14.733  1.00 28.92 ? 303 5EF A S14 1 
HETATM 8584 O  O15 . 5EF G 4 .   ? 25.798  6.122   15.970  1.00 30.53 ? 303 5EF A O15 1 
HETATM 8585 C  C18 . 5EF G 4 .   ? 24.274  9.306   14.178  1.00 38.80 ? 303 5EF A C18 1 
HETATM 8586 C  C8  . 5EF G 4 .   ? 24.960  5.752   13.472  1.00 22.16 ? 303 5EF A C8  1 
HETATM 8587 C  C7  . 5EF G 4 .   ? 23.884  4.904   13.768  1.00 17.24 ? 303 5EF A C7  1 
HETATM 8588 C  C9  . 5EF G 4 .   ? 25.584  5.687   12.227  1.00 20.88 ? 303 5EF A C9  1 
HETATM 8589 C  C10 . 5EF G 4 .   ? 25.127  4.783   11.296  1.00 17.81 ? 303 5EF A C10 1 
HETATM 8590 S  S1  . 5EF G 4 .   ? 23.541  2.703   10.328  1.00 13.87 ? 303 5EF A S1  1 
HETATM 8591 O  O3  . 5EF G 4 .   ? 24.672  1.782   9.991   1.00 12.53 ? 303 5EF A O3  1 
HETATM 8592 N  N4  . 5EF G 4 .   ? 22.267  1.803   10.865  1.00 13.69 ? 303 5EF A N4  1 
HETATM 8593 O  O2  . 5EF G 4 .   ? 23.113  3.427   9.057   1.00 16.38 ? 303 5EF A O2  1 
HETATM 8594 N  N20 . 5EF G 4 .   ? 26.651  6.575   11.828  1.00 24.26 ? 303 5EF A N20 1 
HETATM 8595 C  C21 . 5EF G 4 .   ? 26.646  7.239   10.498  1.00 25.87 ? 303 5EF A C21 1 
HETATM 8596 C  C25 . 5EF G 4 .   ? 25.958  8.622   10.574  1.00 26.97 ? 303 5EF A C25 1 
HETATM 8597 C  C24 . 5EF G 4 .   ? 26.708  9.520   9.546   1.00 26.45 ? 303 5EF A C24 1 
HETATM 8598 C  C23 . 5EF G 4 .   ? 28.059  8.955   9.733   1.00 26.60 ? 303 5EF A C23 1 
HETATM 8599 C  C29 . 5EF G 4 .   ? 29.297  9.584   9.443   1.00 31.36 ? 303 5EF A C29 1 
HETATM 8600 C  C28 . 5EF G 4 .   ? 30.527  8.928   9.714   1.00 30.93 ? 303 5EF A C28 1 
HETATM 8601 C  C27 . 5EF G 4 .   ? 30.505  7.611   10.276  1.00 30.69 ? 303 5EF A C27 1 
HETATM 8602 C  C26 . 5EF G 4 .   ? 29.241  7.020   10.535  1.00 27.09 ? 303 5EF A C26 1 
HETATM 8603 C  C22 . 5EF G 4 .   ? 28.044  7.683   10.241  1.00 28.06 ? 303 5EF A C22 1 
HETATM 8604 ZN ZN  . ZN  H 2 .   ? -8.208  3.555   4.914   1.00 9.43  ? 301 ZN  B ZN  1 
HETATM 8605 C  C1  . EDO I 3 .   ? -17.464 -3.323  22.845  1.00 31.62 ? 302 EDO B C1  1 
HETATM 8606 O  O1  . EDO I 3 .   ? -16.256 -2.513  22.946  1.00 32.92 ? 302 EDO B O1  1 
HETATM 8607 C  C2  . EDO I 3 .   ? -17.754 -3.740  21.409  1.00 30.93 ? 302 EDO B C2  1 
HETATM 8608 O  O2  . EDO I 3 .   ? -16.659 -3.411  20.497  1.00 29.64 ? 302 EDO B O2  1 
HETATM 8609 O  O19 . 5EF J 4 .   ? -8.116  13.411  1.528   1.00 43.03 ? 303 5EF B O19 1 
HETATM 8610 C  C17 . 5EF J 4 .   ? -7.985  11.184  1.883   1.00 30.52 ? 303 5EF B C17 1 
HETATM 8611 C  C6  . 5EF J 4 .   ? -8.150  7.182   4.319   1.00 14.47 ? 303 5EF B C6  1 
HETATM 8612 F  F11 . 5EF J 4 .   ? -7.359  6.180   3.795   1.00 17.94 ? 303 5EF B F11 1 
HETATM 8613 C  C5  . 5EF J 4 .   ? -8.729  7.159   5.532   1.00 15.35 ? 303 5EF B C5  1 
HETATM 8614 F  F12 . 5EF J 4 .   ? -7.902  8.020   2.121   1.00 18.25 ? 303 5EF B F12 1 
HETATM 8615 F  F13 . 5EF J 4 .   ? -10.159 8.246   7.056   1.00 19.44 ? 303 5EF B F13 1 
HETATM 8616 O  O16 . 5EF J 4 .   ? -10.547 11.557  2.872   1.00 34.61 ? 303 5EF B O16 1 
HETATM 8617 S  S14 . 5EF J 4 .   ? -9.563  10.460  2.392   1.00 28.65 ? 303 5EF B S14 1 
HETATM 8618 O  O15 . 5EF J 4 .   ? -10.307 9.766   1.246   1.00 35.36 ? 303 5EF B O15 1 
HETATM 8619 C  C18 . 5EF J 4 .   ? -7.737  12.504  2.535   1.00 37.61 ? 303 5EF B C18 1 
HETATM 8620 C  C8  . 5EF J 4 .   ? -9.338  9.157   3.654   1.00 20.26 ? 303 5EF B C8  1 
HETATM 8621 C  C7  . 5EF J 4 .   ? -8.458  8.119   3.348   1.00 16.16 ? 303 5EF B C7  1 
HETATM 8622 C  C9  . 5EF J 4 .   ? -9.894  9.206   4.910   1.00 19.57 ? 303 5EF B C9  1 
HETATM 8623 C  C10 . 5EF J 4 .   ? -9.621  8.219   5.844   1.00 17.34 ? 303 5EF B C10 1 
HETATM 8624 S  S1  . 5EF J 4 .   ? -8.428  5.957   6.814   1.00 13.26 ? 303 5EF B S1  1 
HETATM 8625 O  O3  . 5EF J 4 .   ? -9.708  5.291   7.202   1.00 12.24 ? 303 5EF B O3  1 
HETATM 8626 N  N4  . 5EF J 4 .   ? -7.486  4.734   6.101   1.00 12.74 ? 303 5EF B N4  1 
HETATM 8627 O  O2  . 5EF J 4 .   ? -7.743  6.658   7.941   1.00 14.66 ? 303 5EF B O2  1 
HETATM 8628 N  N20 . 5EF J 4 .   ? -10.753 10.318  5.269   1.00 23.04 ? 303 5EF B N20 1 
HETATM 8629 C  C21 . 5EF J 4 .   ? -10.334 11.102  6.463   1.00 24.18 ? 303 5EF B C21 1 
HETATM 8630 C  C25 . 5EF J 4 .   ? -9.774  12.504  6.108   1.00 25.39 ? 303 5EF B C25 1 
HETATM 8631 C  C24 . 5EF J 4 .   ? -10.190 13.387  7.304   1.00 24.17 ? 303 5EF B C24 1 
HETATM 8632 C  C23 . 5EF J 4 .   ? -11.523 12.762  7.623   1.00 25.17 ? 303 5EF B C23 1 
HETATM 8633 C  C29 . 5EF J 4 .   ? -12.585 13.371  8.321   1.00 30.75 ? 303 5EF B C29 1 
HETATM 8634 C  C28 . 5EF J 4 .   ? -13.767 12.655  8.517   1.00 35.37 ? 303 5EF B C28 1 
HETATM 8635 C  C27 . 5EF J 4 .   ? -13.862 11.308  8.028   1.00 34.71 ? 303 5EF B C27 1 
HETATM 8636 C  C26 . 5EF J 4 .   ? -12.769 10.731  7.332   1.00 28.82 ? 303 5EF B C26 1 
HETATM 8637 C  C22 . 5EF J 4 .   ? -11.600 11.467  7.157   1.00 27.67 ? 303 5EF B C22 1 
HETATM 8638 ZN ZN  . ZN  K 2 .   ? 37.537  2.226   -30.942 1.00 14.04 ? 301 ZN  C ZN  1 
HETATM 8639 O  O19 . 5EF L 4 .   ? 39.132  11.816  -29.979 1.00 39.28 ? 302 5EF C O19 1 
HETATM 8640 C  C17 . 5EF L 4 .   ? 38.959  9.923   -28.444 1.00 27.21 ? 302 5EF C C17 1 
HETATM 8641 C  C6  . 5EF L 4 .   ? 38.249  5.725   -30.566 1.00 18.25 ? 302 5EF C C6  1 
HETATM 8642 F  F11 . 5EF L 4 .   ? 37.112  5.036   -30.211 1.00 17.14 ? 302 5EF C F11 1 
HETATM 8643 C  C5  . 5EF L 4 .   ? 38.895  5.538   -31.795 1.00 18.24 ? 302 5EF C C5  1 
HETATM 8644 F  F12 . 5EF L 4 .   ? 38.072  6.815   -28.465 1.00 21.97 ? 302 5EF C F12 1 
HETATM 8645 F  F13 . 5EF L 4 .   ? 40.683  6.083   -33.186 1.00 19.48 ? 302 5EF C F13 1 
HETATM 8646 O  O16 . 5EF L 4 .   ? 41.469  9.391   -28.985 1.00 24.12 ? 302 5EF C O16 1 
HETATM 8647 S  S14 . 5EF L 4 .   ? 40.177  8.570   -28.611 1.00 25.20 ? 302 5EF C S14 1 
HETATM 8648 O  O15 . 5EF L 4 .   ? 40.526  7.603   -27.434 1.00 28.02 ? 302 5EF C O15 1 
HETATM 8649 C  C18 . 5EF L 4 .   ? 38.655  10.485  -29.847 1.00 29.07 ? 302 5EF C C18 1 
HETATM 8650 C  C8  . 5EF L 4 .   ? 39.846  7.386   -29.929 1.00 22.34 ? 302 5EF C C8  1 
HETATM 8651 C  C7  . 5EF L 4 .   ? 38.698  6.652   -29.672 1.00 18.28 ? 302 5EF C C7  1 
HETATM 8652 C  C9  . 5EF L 4 .   ? 40.559  7.208   -31.135 1.00 21.89 ? 302 5EF C C9  1 
HETATM 8653 C  C10 . 5EF L 4 .   ? 40.030  6.304   -32.064 1.00 18.86 ? 302 5EF C C10 1 
HETATM 8654 S  S1  . 5EF L 4 .   ? 38.373  4.313   -33.025 1.00 17.17 ? 302 5EF C S1  1 
HETATM 8655 O  O3  . 5EF L 4 .   ? 39.491  3.354   -33.246 1.00 16.17 ? 302 5EF C O3  1 
HETATM 8656 N  N4  . 5EF L 4 .   ? 37.102  3.313   -32.418 1.00 17.75 ? 302 5EF C N4  1 
HETATM 8657 O  O2  . 5EF L 4 .   ? 37.818  4.973   -34.259 1.00 18.85 ? 302 5EF C O2  1 
HETATM 8658 N  N20 . 5EF L 4 .   ? 41.710  7.983   -31.515 1.00 22.18 ? 302 5EF C N20 1 
HETATM 8659 C  C21 . 5EF L 4 .   ? 41.719  8.718   -32.806 1.00 22.08 ? 302 5EF C C21 1 
HETATM 8660 C  C25 . 5EF L 4 .   ? 40.903  10.005  -32.764 1.00 25.65 ? 302 5EF C C25 1 
HETATM 8661 C  C24 . 5EF L 4 .   ? 41.642  11.013  -33.685 1.00 22.61 ? 302 5EF C C24 1 
HETATM 8662 C  C23 . 5EF L 4 .   ? 43.019  10.557  -33.391 1.00 23.17 ? 302 5EF C C23 1 
HETATM 8663 C  C29 . 5EF L 4 .   ? 44.199  11.291  -33.567 1.00 21.26 ? 302 5EF C C29 1 
HETATM 8664 C  C28 . 5EF L 4 .   ? 45.429  10.686  -33.215 1.00 22.45 ? 302 5EF C C28 1 
HETATM 8665 C  C27 . 5EF L 4 .   ? 45.513  9.370   -32.673 1.00 27.67 ? 302 5EF C C27 1 
HETATM 8666 C  C26 . 5EF L 4 .   ? 44.290  8.637   -32.506 1.00 25.14 ? 302 5EF C C26 1 
HETATM 8667 C  C22 . 5EF L 4 .   ? 43.091  9.263   -32.903 1.00 22.66 ? 302 5EF C C22 1 
HETATM 8668 ZN ZN  . ZN  M 2 .   ? 6.809   5.389   -38.431 1.00 10.36 ? 301 ZN  D ZN  1 
HETATM 8669 C  C1  . EDO N 3 .   ? -2.497  -1.596  -20.635 1.00 27.71 ? 302 EDO D C1  1 
HETATM 8670 O  O1  . EDO N 3 .   ? -1.438  -0.712  -20.270 1.00 35.64 ? 302 EDO D O1  1 
HETATM 8671 C  C2  . EDO N 3 .   ? -2.819  -1.413  -22.109 1.00 29.86 ? 302 EDO D C2  1 
HETATM 8672 O  O2  . EDO N 3 .   ? -1.523  -1.493  -22.700 1.00 30.44 ? 302 EDO D O2  1 
HETATM 8673 O  O19 . 5EF O 4 .   ? 6.620   15.153  -42.271 1.00 45.98 ? 303 5EF D O19 1 
HETATM 8674 C  C17 . 5EF O 4 .   ? 6.876   13.176  -40.909 1.00 27.18 ? 303 5EF D C17 1 
HETATM 8675 C  C6  . 5EF O 4 .   ? 6.817   8.967   -38.986 1.00 15.00 ? 303 5EF D C6  1 
HETATM 8676 F  F11 . 5EF O 4 .   ? 7.756   8.065   -39.423 1.00 16.35 ? 303 5EF D F11 1 
HETATM 8677 C  C5  . 5EF O 4 .   ? 6.249   8.932   -37.716 1.00 14.45 ? 303 5EF D C5  1 
HETATM 8678 F  F12 . 5EF O 4 .   ? 7.098   9.992   -41.104 1.00 20.75 ? 303 5EF D F12 1 
HETATM 8679 F  F13 . 5EF O 4 .   ? 4.651   9.779   -36.216 1.00 17.13 ? 303 5EF D F13 1 
HETATM 8680 O  O16 . 5EF O 4 .   ? 4.150   13.035  -40.502 1.00 33.15 ? 303 5EF D O16 1 
HETATM 8681 S  S14 . 5EF O 4 .   ? 5.378   12.112  -40.897 1.00 29.18 ? 303 5EF D S14 1 
HETATM 8682 O  O15 . 5EF O 4 .   ? 5.035   11.537  -42.246 1.00 33.29 ? 303 5EF D O15 1 
HETATM 8683 C  C18 . 5EF O 4 .   ? 7.183   13.842  -42.242 1.00 33.49 ? 303 5EF D C18 1 
HETATM 8684 C  C8  . 5EF O 4 .   ? 5.526   10.881  -39.595 1.00 21.88 ? 303 5EF D C8  1 
HETATM 8685 C  C7  . 5EF O 4 .   ? 6.495   9.933   -39.901 1.00 20.31 ? 303 5EF D C7  1 
HETATM 8686 C  C9  . 5EF O 4 .   ? 4.898   10.860  -38.342 1.00 20.52 ? 303 5EF D C9  1 
HETATM 8687 C  C10 . 5EF O 4 .   ? 5.251   9.908   -37.416 1.00 17.73 ? 303 5EF D C10 1 
HETATM 8688 S  S1  . 5EF O 4 .   ? 6.600   7.683   -36.450 1.00 13.90 ? 303 5EF D S1  1 
HETATM 8689 O  O3  . 5EF O 4 .   ? 5.300   7.089   -36.042 1.00 14.29 ? 303 5EF D O3  1 
HETATM 8690 N  N4  . 5EF O 4 .   ? 7.637   6.552   -37.045 1.00 13.15 ? 303 5EF D N4  1 
HETATM 8691 O  O2  . 5EF O 4 .   ? 7.344   8.423   -35.362 1.00 14.55 ? 303 5EF D O2  1 
HETATM 8692 N  N20 . 5EF O 4 .   ? 3.890   11.819  -37.976 1.00 22.96 ? 303 5EF D N20 1 
HETATM 8693 C  C21 . 5EF O 4 .   ? 3.812   12.369  -36.630 1.00 24.18 ? 303 5EF D C21 1 
HETATM 8694 C  C25 . 5EF O 4 .   ? 4.947   13.411  -36.627 1.00 24.17 ? 303 5EF D C25 1 
HETATM 8695 C  C24 . 5EF O 4 .   ? 4.437   14.800  -36.134 1.00 23.75 ? 303 5EF D C24 1 
HETATM 8696 C  C23 . 5EF O 4 .   ? 2.991   14.595  -36.326 1.00 22.67 ? 303 5EF D C23 1 
HETATM 8697 C  C29 . 5EF O 4 .   ? 2.012   15.599  -36.293 1.00 22.26 ? 303 5EF D C29 1 
HETATM 8698 C  C28 . 5EF O 4 .   ? 0.673   15.265  -36.531 1.00 21.80 ? 303 5EF D C28 1 
HETATM 8699 C  C27 . 5EF O 4 .   ? 0.316   13.924  -36.791 1.00 26.12 ? 303 5EF D C27 1 
HETATM 8700 C  C26 . 5EF O 4 .   ? 1.312   12.955  -36.842 1.00 22.07 ? 303 5EF D C26 1 
HETATM 8701 C  C22 . 5EF O 4 .   ? 2.640   13.287  -36.596 1.00 21.61 ? 303 5EF D C22 1 
HETATM 8702 O  O   . HOH P 5 .   ? 4.667   -0.135  -8.390  1.00 26.42 ? 401 HOH A O   1 
HETATM 8703 O  O   . HOH P 5 .   ? 27.770  -4.818  31.275  1.00 29.30 ? 402 HOH A O   1 
HETATM 8704 O  O   . HOH P 5 .   ? 18.275  10.617  34.841  1.00 34.60 ? 403 HOH A O   1 
HETATM 8705 O  O   . HOH P 5 .   ? 13.088  14.303  14.259  1.00 23.86 ? 404 HOH A O   1 
HETATM 8706 O  O   . HOH P 5 .   ? 42.152  -0.324  5.782   1.00 32.98 ? 405 HOH A O   1 
HETATM 8707 O  O   . HOH P 5 .   ? 28.415  9.202   17.791  1.00 39.26 ? 406 HOH A O   1 
HETATM 8708 O  O   . HOH P 5 .   ? 42.132  -12.000 2.728   1.00 35.01 ? 407 HOH A O   1 
HETATM 8709 O  O   . HOH P 5 .   ? 39.445  -12.579 19.915  1.00 26.60 ? 408 HOH A O   1 
HETATM 8710 O  O   . HOH P 5 .   ? 13.975  12.989  28.503  1.00 34.70 ? 409 HOH A O   1 
HETATM 8711 O  O   . HOH P 5 .   ? 9.425   -14.648 1.652   1.00 34.46 ? 410 HOH A O   1 
HETATM 8712 O  O   . HOH P 5 .   ? 36.699  6.298   11.956  1.00 30.42 ? 411 HOH A O   1 
HETATM 8713 O  O   . HOH P 5 .   ? 18.090  -16.067 -4.296  1.00 37.33 ? 412 HOH A O   1 
HETATM 8714 O  O   . HOH P 5 .   ? 36.538  -4.212  -0.754  1.00 23.34 ? 413 HOH A O   1 
HETATM 8715 O  O   . HOH P 5 .   ? 14.300  -9.932  26.082  1.00 13.69 ? 414 HOH A O   1 
HETATM 8716 O  O   . HOH P 5 .   ? 43.703  -4.344  13.075  1.00 24.96 ? 415 HOH A O   1 
HETATM 8717 O  O   . HOH P 5 .   ? 13.305  5.454   24.539  1.00 35.37 ? 416 HOH A O   1 
HETATM 8718 O  O   . HOH P 5 .   ? 41.306  -9.221  23.929  1.00 41.58 ? 417 HOH A O   1 
HETATM 8719 O  O   . HOH P 5 .   ? 7.718   -8.200  11.836  1.00 28.79 ? 418 HOH A O   1 
HETATM 8720 O  O   . HOH P 5 .   ? 5.770   -3.519  20.833  1.00 30.25 ? 419 HOH A O   1 
HETATM 8721 O  O   . HOH P 5 .   ? 13.579  16.501  11.917  1.00 15.85 ? 420 HOH A O   1 
HETATM 8722 O  O   . HOH P 5 .   ? 42.719  -10.106 18.991  1.00 30.63 ? 421 HOH A O   1 
HETATM 8723 O  O   . HOH P 5 .   ? 26.456  5.513   -3.682  1.00 32.89 ? 422 HOH A O   1 
HETATM 8724 O  O   . HOH P 5 .   ? 45.008  -4.444  7.632   1.00 26.31 ? 423 HOH A O   1 
HETATM 8725 O  O   . HOH P 5 .   ? 11.033  3.287   19.074  1.00 24.38 ? 424 HOH A O   1 
HETATM 8726 O  O   . HOH P 5 .   ? 10.170  4.762   8.870   1.00 12.35 ? 425 HOH A O   1 
HETATM 8727 O  O   . HOH P 5 .   ? 12.678  -12.474 16.515  1.00 21.34 ? 426 HOH A O   1 
HETATM 8728 O  O   . HOH P 5 .   ? 27.716  3.902   33.625  1.00 23.74 ? 427 HOH A O   1 
HETATM 8729 O  O   . HOH P 5 .   ? 31.421  5.706   32.575  1.00 25.51 ? 428 HOH A O   1 
HETATM 8730 O  O   . HOH P 5 .   ? 10.955  -5.178  0.799   1.00 29.20 ? 429 HOH A O   1 
HETATM 8731 O  O   . HOH P 5 .   ? 23.718  -16.281 29.563  1.00 24.24 ? 430 HOH A O   1 
HETATM 8732 O  O   . HOH P 5 .   ? 30.376  -8.602  -2.577  1.00 20.72 ? 431 HOH A O   1 
HETATM 8733 O  O   . HOH P 5 .   ? 18.993  -6.557  -11.788 1.00 33.62 ? 432 HOH A O   1 
HETATM 8734 O  O   . HOH P 5 .   ? 23.048  -12.437 9.769   1.00 11.98 ? 433 HOH A O   1 
HETATM 8735 O  O   . HOH P 5 .   ? 19.578  12.137  24.307  1.00 28.66 ? 434 HOH A O   1 
HETATM 8736 O  O   . HOH P 5 .   ? 5.515   -12.123 13.374  1.00 21.84 ? 435 HOH A O   1 
HETATM 8737 O  O   . HOH P 5 .   ? 19.250  9.660   32.441  1.00 21.22 ? 436 HOH A O   1 
HETATM 8738 O  O   . HOH P 5 .   ? 19.810  14.005  28.580  1.00 24.25 ? 437 HOH A O   1 
HETATM 8739 O  O   . HOH P 5 .   ? 6.259   15.756  15.707  1.00 33.46 ? 438 HOH A O   1 
HETATM 8740 O  O   . HOH P 5 .   ? 17.854  3.164   12.891  1.00 13.77 ? 439 HOH A O   1 
HETATM 8741 O  O   . HOH P 5 .   ? 43.495  -5.639  0.730   1.00 38.08 ? 440 HOH A O   1 
HETATM 8742 O  O   . HOH P 5 .   ? 41.946  2.428   0.963   1.00 18.05 ? 441 HOH A O   1 
HETATM 8743 O  O   . HOH P 5 .   ? 41.050  -10.245 9.780   1.00 20.71 ? 442 HOH A O   1 
HETATM 8744 O  O   . HOH P 5 .   ? 33.752  -13.467 26.607  1.00 27.24 ? 443 HOH A O   1 
HETATM 8745 O  O   . HOH P 5 .   ? 7.743   -1.594  15.293  1.00 24.54 ? 444 HOH A O   1 
HETATM 8746 O  O   . HOH P 5 .   ? 9.137   11.449  1.101   1.00 18.35 ? 445 HOH A O   1 
HETATM 8747 O  O   . HOH P 5 .   ? 13.868  1.886   -2.899  1.00 23.70 ? 446 HOH A O   1 
HETATM 8748 O  O   . HOH P 5 .   ? 17.071  0.777   -0.464  1.00 18.07 ? 447 HOH A O   1 
HETATM 8749 O  O   . HOH P 5 .   ? 10.481  6.303   15.474  1.00 12.43 ? 448 HOH A O   1 
HETATM 8750 O  O   . HOH P 5 .   ? 12.428  -2.600  11.106  1.00 11.60 ? 449 HOH A O   1 
HETATM 8751 O  O   . HOH P 5 .   ? 10.644  12.420  20.788  1.00 27.48 ? 450 HOH A O   1 
HETATM 8752 O  O   . HOH P 5 .   ? 10.703  -4.505  -5.381  1.00 40.18 ? 451 HOH A O   1 
HETATM 8753 O  O   . HOH P 5 .   ? 27.634  -21.068 24.623  1.00 30.63 ? 452 HOH A O   1 
HETATM 8754 O  O   . HOH P 5 .   ? 45.437  1.621   12.716  1.00 40.18 ? 453 HOH A O   1 
HETATM 8755 O  O   . HOH P 5 .   ? 31.331  -13.144 2.447   1.00 22.45 ? 454 HOH A O   1 
HETATM 8756 O  O   . HOH P 5 .   ? 15.139  -6.888  21.140  1.00 12.45 ? 455 HOH A O   1 
HETATM 8757 O  O   . HOH P 5 .   ? 19.559  -0.622  26.705  1.00 13.98 ? 456 HOH A O   1 
HETATM 8758 O  O   . HOH P 5 .   ? 47.038  -3.735  10.284  1.00 28.01 ? 457 HOH A O   1 
HETATM 8759 O  O   . HOH P 5 .   ? 36.196  -7.048  26.272  1.00 21.58 ? 458 HOH A O   1 
HETATM 8760 O  O   . HOH P 5 .   ? 28.396  2.452   -1.291  1.00 25.50 ? 459 HOH A O   1 
HETATM 8761 O  O   . HOH P 5 .   ? 18.077  -15.088 6.243   1.00 19.64 ? 460 HOH A O   1 
HETATM 8762 O  O   . HOH P 5 .   ? 5.888   -4.003  -8.097  1.00 37.06 ? 461 HOH A O   1 
HETATM 8763 O  O   . HOH P 5 .   ? 24.381  -11.720 30.286  1.00 25.80 ? 462 HOH A O   1 
HETATM 8764 O  O   . HOH P 5 .   ? 31.947  -16.868 20.621  1.00 34.35 ? 463 HOH A O   1 
HETATM 8765 O  O   . HOH P 5 .   ? 6.776   -9.954  4.278   1.00 27.58 ? 464 HOH A O   1 
HETATM 8766 O  O   . HOH P 5 .   ? 25.974  11.142  31.326  1.00 26.88 ? 465 HOH A O   1 
HETATM 8767 O  O   . HOH P 5 .   ? 11.234  1.696   -4.061  1.00 36.03 ? 466 HOH A O   1 
HETATM 8768 O  O   . HOH P 5 .   ? 10.285  -3.392  2.777   1.00 15.12 ? 467 HOH A O   1 
HETATM 8769 O  O   . HOH P 5 .   ? 8.586   2.953   7.367   1.00 8.77  ? 468 HOH A O   1 
HETATM 8770 O  O   . HOH P 5 .   ? 6.844   0.180   -14.024 1.00 44.61 ? 469 HOH A O   1 
HETATM 8771 O  O   . HOH P 5 .   ? 39.934  -12.013 11.715  1.00 22.84 ? 470 HOH A O   1 
HETATM 8772 O  O   . HOH P 5 .   ? 29.759  -15.528 -1.777  1.00 22.78 ? 471 HOH A O   1 
HETATM 8773 O  O   . HOH P 5 .   ? 38.723  2.163   -6.050  1.00 23.67 ? 472 HOH A O   1 
HETATM 8774 O  O   . HOH P 5 .   ? 17.299  0.320   28.598  1.00 14.59 ? 473 HOH A O   1 
HETATM 8775 O  O   . HOH P 5 .   ? 15.804  -11.990 27.036  1.00 20.19 ? 474 HOH A O   1 
HETATM 8776 O  O   . HOH P 5 .   ? 25.684  -18.524 12.473  1.00 21.43 ? 475 HOH A O   1 
HETATM 8777 O  O   . HOH P 5 .   ? 15.054  -16.115 14.941  1.00 22.78 ? 476 HOH A O   1 
HETATM 8778 O  O   . HOH P 5 .   ? 10.989  11.189  8.181   1.00 13.89 ? 477 HOH A O   1 
HETATM 8779 O  O   . HOH P 5 .   ? 37.140  7.589   30.139  1.00 26.55 ? 478 HOH A O   1 
HETATM 8780 O  O   . HOH P 5 .   ? 5.256   16.235  13.529  1.00 39.34 ? 479 HOH A O   1 
HETATM 8781 O  O   . HOH P 5 .   ? 13.787  1.833   -0.305  1.00 22.07 ? 480 HOH A O   1 
HETATM 8782 O  O   . HOH P 5 .   ? 35.117  -0.775  30.635  1.00 25.70 ? 481 HOH A O   1 
HETATM 8783 O  O   . HOH P 5 .   ? 28.378  -4.062  2.660   1.00 12.54 ? 482 HOH A O   1 
HETATM 8784 O  O   . HOH P 5 .   ? 10.694  2.482   -7.035  1.00 42.41 ? 483 HOH A O   1 
HETATM 8785 O  O   . HOH P 5 .   ? 13.812  8.326   23.598  1.00 28.34 ? 484 HOH A O   1 
HETATM 8786 O  O   . HOH P 5 .   ? 7.252   5.072   11.218  1.00 10.71 ? 485 HOH A O   1 
HETATM 8787 O  O   . HOH P 5 .   ? 33.169  -14.780 3.503   1.00 26.17 ? 486 HOH A O   1 
HETATM 8788 O  O   . HOH P 5 .   ? 8.085   -10.439 26.503  1.00 26.01 ? 487 HOH A O   1 
HETATM 8789 O  O   . HOH P 5 .   ? 32.309  -16.825 10.109  1.00 30.99 ? 488 HOH A O   1 
HETATM 8790 O  O   . HOH P 5 .   ? 34.254  -6.267  31.174  1.00 38.84 ? 489 HOH A O   1 
HETATM 8791 O  O   . HOH P 5 .   ? 9.486   18.521  18.080  1.00 40.59 ? 490 HOH A O   1 
HETATM 8792 O  O   . HOH P 5 .   ? 39.262  -15.790 17.063  1.00 22.26 ? 491 HOH A O   1 
HETATM 8793 O  O   . HOH P 5 .   ? 18.161  5.691   20.773  1.00 19.14 ? 492 HOH A O   1 
HETATM 8794 O  O   . HOH P 5 .   ? 11.969  -10.536 27.423  1.00 14.34 ? 493 HOH A O   1 
HETATM 8795 O  O   . HOH P 5 .   ? 19.591  -18.542 26.408  1.00 18.93 ? 494 HOH A O   1 
HETATM 8796 O  O   . HOH P 5 .   ? 11.331  5.406   2.166   1.00 12.42 ? 495 HOH A O   1 
HETATM 8797 O  O   . HOH P 5 .   ? 34.969  -10.986 -3.172  1.00 29.90 ? 496 HOH A O   1 
HETATM 8798 O  O   . HOH P 5 .   ? 11.483  9.971   23.184  1.00 28.58 ? 497 HOH A O   1 
HETATM 8799 O  O   . HOH P 5 .   ? 22.823  12.560  15.029  1.00 33.41 ? 498 HOH A O   1 
HETATM 8800 O  O   . HOH P 5 .   ? 19.332  14.274  5.121   1.00 14.19 ? 499 HOH A O   1 
HETATM 8801 O  O   . HOH P 5 .   ? 30.385  14.745  4.373   1.00 31.73 ? 500 HOH A O   1 
HETATM 8802 O  O   . HOH P 5 .   ? 20.588  -10.010 31.960  1.00 22.70 ? 501 HOH A O   1 
HETATM 8803 O  O   . HOH P 5 .   ? 36.380  -15.378 6.320   1.00 29.27 ? 502 HOH A O   1 
HETATM 8804 O  O   . HOH P 5 .   ? 5.940   11.731  8.042   1.00 11.55 ? 503 HOH A O   1 
HETATM 8805 O  O   . HOH P 5 .   ? 32.734  6.669   13.327  1.00 24.57 ? 504 HOH A O   1 
HETATM 8806 O  O   . HOH P 5 .   ? 31.243  -20.954 8.431   1.00 29.02 ? 505 HOH A O   1 
HETATM 8807 O  O   . HOH P 5 .   ? 7.373   -6.739  2.506   1.00 24.40 ? 506 HOH A O   1 
HETATM 8808 O  O   . HOH P 5 .   ? 23.685  11.932  12.565  1.00 38.39 ? 507 HOH A O   1 
HETATM 8809 O  O   . HOH P 5 .   ? 26.138  12.318  6.523   1.00 23.83 ? 508 HOH A O   1 
HETATM 8810 O  O   . HOH P 5 .   ? 11.676  -15.427 8.393   1.00 27.34 ? 509 HOH A O   1 
HETATM 8811 O  O   . HOH P 5 .   ? 29.053  -14.979 16.955  1.00 18.44 ? 510 HOH A O   1 
HETATM 8812 O  O   . HOH P 5 .   ? 4.858   -9.360  25.693  1.00 24.90 ? 511 HOH A O   1 
HETATM 8813 O  O   . HOH P 5 .   ? 13.978  -16.051 26.894  1.00 25.77 ? 512 HOH A O   1 
HETATM 8814 O  O   . HOH P 5 .   ? 38.497  4.229   11.305  1.00 21.23 ? 513 HOH A O   1 
HETATM 8815 O  O   . HOH P 5 .   ? 17.714  10.146  22.192  1.00 22.46 ? 514 HOH A O   1 
HETATM 8816 O  O   . HOH P 5 .   ? 23.306  3.450   -1.964  1.00 18.68 ? 515 HOH A O   1 
HETATM 8817 O  O   . HOH P 5 .   ? 38.065  -7.589  24.570  1.00 24.22 ? 516 HOH A O   1 
HETATM 8818 O  O   . HOH P 5 .   ? 13.376  -14.818 29.325  1.00 29.91 ? 517 HOH A O   1 
HETATM 8819 O  O   . HOH P 5 .   ? 8.712   -6.324  7.635   1.00 19.87 ? 518 HOH A O   1 
HETATM 8820 O  O   . HOH P 5 .   ? 9.632   -2.631  10.450  1.00 21.46 ? 519 HOH A O   1 
HETATM 8821 O  O   . HOH P 5 .   ? 20.616  18.000  8.004   1.00 29.49 ? 520 HOH A O   1 
HETATM 8822 O  O   . HOH P 5 .   ? 12.108  4.891   29.092  1.00 35.52 ? 521 HOH A O   1 
HETATM 8823 O  O   . HOH P 5 .   ? 18.792  12.021  -0.677  1.00 19.16 ? 522 HOH A O   1 
HETATM 8824 O  O   . HOH P 5 .   ? 9.006   -11.016 14.003  1.00 32.75 ? 523 HOH A O   1 
HETATM 8825 O  O   . HOH P 5 .   ? 23.810  -21.061 26.577  1.00 25.42 ? 524 HOH A O   1 
HETATM 8826 O  O   . HOH P 5 .   ? 26.093  -17.827 17.442  1.00 19.90 ? 525 HOH A O   1 
HETATM 8827 O  O   . HOH P 5 .   ? 32.335  7.745   30.921  1.00 21.66 ? 526 HOH A O   1 
HETATM 8828 O  O   . HOH P 5 .   ? 17.652  9.704   0.218   1.00 15.06 ? 527 HOH A O   1 
HETATM 8829 O  O   . HOH P 5 .   ? 9.307   -5.034  -1.301  1.00 41.53 ? 528 HOH A O   1 
HETATM 8830 O  O   . HOH P 5 .   ? 10.121  -3.982  19.631  1.00 29.68 ? 529 HOH A O   1 
HETATM 8831 O  O   . HOH P 5 .   ? 44.096  -9.633  8.105   1.00 26.95 ? 530 HOH A O   1 
HETATM 8832 O  O   . HOH P 5 .   ? 15.794  4.570   21.769  1.00 18.54 ? 531 HOH A O   1 
HETATM 8833 O  O   . HOH P 5 .   ? 11.929  7.535   8.712   1.00 8.58  ? 532 HOH A O   1 
HETATM 8834 O  O   . HOH P 5 .   ? 29.874  9.851   34.098  1.00 35.94 ? 533 HOH A O   1 
HETATM 8835 O  O   . HOH P 5 .   ? 20.727  -2.717  -5.276  1.00 25.06 ? 534 HOH A O   1 
HETATM 8836 O  O   . HOH P 5 .   ? 26.063  -18.580 20.538  1.00 20.69 ? 535 HOH A O   1 
HETATM 8837 O  O   . HOH P 5 .   ? 14.118  4.491   -3.952  1.00 22.66 ? 536 HOH A O   1 
HETATM 8838 O  O   . HOH P 5 .   ? 19.261  -15.276 -11.034 1.00 36.40 ? 537 HOH A O   1 
HETATM 8839 O  O   . HOH P 5 .   ? 11.496  8.058   1.732   1.00 16.23 ? 538 HOH A O   1 
HETATM 8840 O  O   . HOH P 5 .   ? 17.111  -3.535  -8.248  1.00 30.52 ? 539 HOH A O   1 
HETATM 8841 O  O   . HOH P 5 .   ? 31.503  -18.778 4.177   1.00 24.22 ? 540 HOH A O   1 
HETATM 8842 O  O   . HOH P 5 .   ? 39.180  3.904   19.661  1.00 26.60 ? 541 HOH A O   1 
HETATM 8843 O  O   . HOH P 5 .   ? 16.572  11.202  -3.047  1.00 23.09 ? 542 HOH A O   1 
HETATM 8844 O  O   . HOH P 5 .   ? 27.363  -15.994 -5.497  1.00 26.94 ? 543 HOH A O   1 
HETATM 8845 O  O   . HOH P 5 .   ? 32.887  5.212   20.217  1.00 24.68 ? 544 HOH A O   1 
HETATM 8846 O  O   . HOH P 5 .   ? 16.973  20.076  18.242  1.00 45.77 ? 545 HOH A O   1 
HETATM 8847 O  O   . HOH P 5 .   ? 28.666  9.502   13.128  1.00 33.20 ? 546 HOH A O   1 
HETATM 8848 O  O   . HOH P 5 .   ? 29.540  11.940  -4.968  1.00 30.03 ? 547 HOH A O   1 
HETATM 8849 O  O   . HOH P 5 .   ? 15.063  -14.506 19.130  1.00 22.40 ? 548 HOH A O   1 
HETATM 8850 O  O   . HOH P 5 .   ? 24.821  14.117  33.288  1.00 31.71 ? 549 HOH A O   1 
HETATM 8851 O  O   . HOH P 5 .   ? 24.083  -15.218 -11.912 1.00 38.45 ? 550 HOH A O   1 
HETATM 8852 O  O   . HOH P 5 .   ? 7.354   -1.961  -0.851  1.00 24.16 ? 551 HOH A O   1 
HETATM 8853 O  O   . HOH P 5 .   ? 44.582  -1.456  14.799  1.00 29.68 ? 552 HOH A O   1 
HETATM 8854 O  O   . HOH P 5 .   ? 25.639  -11.749 -12.688 1.00 33.17 ? 553 HOH A O   1 
HETATM 8855 O  O   . HOH P 5 .   ? 10.031  3.234   22.462  1.00 27.93 ? 554 HOH A O   1 
HETATM 8856 O  O   . HOH P 5 .   ? 7.158   -2.070  25.812  1.00 29.05 ? 555 HOH A O   1 
HETATM 8857 O  O   . HOH P 5 .   ? 25.654  -15.856 6.564   1.00 14.14 ? 556 HOH A O   1 
HETATM 8858 O  O   . HOH P 5 .   ? 44.871  -3.923  15.624  1.00 29.95 ? 557 HOH A O   1 
HETATM 8859 O  O   . HOH P 5 .   ? 41.109  -4.302  0.444   1.00 36.44 ? 558 HOH A O   1 
HETATM 8860 O  O   . HOH P 5 .   ? 11.290  9.476   -1.868  1.00 28.46 ? 559 HOH A O   1 
HETATM 8861 O  O   . HOH P 5 .   ? 13.619  -12.659 20.970  1.00 19.58 ? 560 HOH A O   1 
HETATM 8862 O  O   . HOH P 5 .   ? 24.160  -22.071 18.426  1.00 34.41 ? 561 HOH A O   1 
HETATM 8863 O  O   . HOH P 5 .   ? 16.834  -20.595 21.534  1.00 37.01 ? 562 HOH A O   1 
HETATM 8864 O  O   . HOH P 5 .   ? 46.023  -9.285  16.843  1.00 37.08 ? 563 HOH A O   1 
HETATM 8865 O  O   . HOH P 5 .   ? 8.408   -0.190  24.531  1.00 27.80 ? 564 HOH A O   1 
HETATM 8866 O  O   . HOH P 5 .   ? 43.462  -9.506  11.403  1.00 24.42 ? 565 HOH A O   1 
HETATM 8867 O  O   . HOH P 5 .   ? 23.839  12.133  0.427   1.00 22.34 ? 566 HOH A O   1 
HETATM 8868 O  O   . HOH P 5 .   ? 14.703  7.158   21.253  1.00 22.92 ? 567 HOH A O   1 
HETATM 8869 O  O   . HOH P 5 .   ? 27.184  -5.401  -5.277  1.00 24.86 ? 568 HOH A O   1 
HETATM 8870 O  O   . HOH P 5 .   ? 7.772   -12.894 -0.997  1.00 40.01 ? 569 HOH A O   1 
HETATM 8871 O  O   . HOH P 5 .   ? 13.233  5.270   -0.353  1.00 20.86 ? 570 HOH A O   1 
HETATM 8872 O  O   . HOH P 5 .   ? 24.084  14.868  4.616   1.00 29.68 ? 571 HOH A O   1 
HETATM 8873 O  O   . HOH P 5 .   ? 16.654  -13.751 30.831  1.00 19.22 ? 572 HOH A O   1 
HETATM 8874 O  O   . HOH P 5 .   ? 40.720  8.668   8.684   1.00 36.45 ? 573 HOH A O   1 
HETATM 8875 O  O   . HOH P 5 .   ? 30.012  7.075   13.863  1.00 26.73 ? 574 HOH A O   1 
HETATM 8876 O  O   . HOH P 5 .   ? 45.013  -7.618  12.501  1.00 33.99 ? 575 HOH A O   1 
HETATM 8877 O  O   . HOH P 5 .   ? 42.872  3.664   23.233  1.00 44.85 ? 576 HOH A O   1 
HETATM 8878 O  O   . HOH P 5 .   ? 31.686  -2.290  -4.620  1.00 43.09 ? 577 HOH A O   1 
HETATM 8879 O  O   . HOH P 5 .   ? 38.202  -13.452 5.543   1.00 27.15 ? 578 HOH A O   1 
HETATM 8880 O  O   . HOH P 5 .   ? 14.150  -1.975  28.921  1.00 21.75 ? 579 HOH A O   1 
HETATM 8881 O  O   . HOH P 5 .   ? 23.892  -21.338 -3.497  1.00 35.41 ? 580 HOH A O   1 
HETATM 8882 O  O   . HOH P 5 .   ? 7.502   9.097   14.352  1.00 18.30 ? 581 HOH A O   1 
HETATM 8883 O  O   . HOH P 5 .   ? 12.360  4.604   22.278  1.00 27.46 ? 582 HOH A O   1 
HETATM 8884 O  O   . HOH P 5 .   ? 30.290  17.250  1.655   1.00 33.82 ? 583 HOH A O   1 
HETATM 8885 O  O   . HOH P 5 .   ? 8.810   4.100   2.706   1.00 16.35 ? 584 HOH A O   1 
HETATM 8886 O  O   . HOH P 5 .   ? 18.059  -15.815 34.031  1.00 24.10 ? 585 HOH A O   1 
HETATM 8887 O  O   . HOH P 5 .   ? 14.977  -17.394 19.529  1.00 25.93 ? 586 HOH A O   1 
HETATM 8888 O  O   . HOH P 5 .   ? 32.203  -18.381 6.892   1.00 28.92 ? 587 HOH A O   1 
HETATM 8889 O  O   . HOH P 5 .   ? 38.482  -15.401 12.334  1.00 29.71 ? 588 HOH A O   1 
HETATM 8890 O  O   . HOH P 5 .   ? 36.907  7.941   9.703   1.00 28.99 ? 589 HOH A O   1 
HETATM 8891 O  O   . HOH P 5 .   ? 18.706  15.364  38.420  1.00 38.57 ? 590 HOH A O   1 
HETATM 8892 O  O   . HOH P 5 .   ? 4.376   13.433  19.667  1.00 31.80 ? 591 HOH A O   1 
HETATM 8893 O  O   . HOH P 5 .   ? 34.168  16.630  0.465   1.00 44.14 ? 592 HOH A O   1 
HETATM 8894 O  O   . HOH P 5 .   ? 24.548  -7.100  -7.413  1.00 38.23 ? 593 HOH A O   1 
HETATM 8895 O  O   . HOH P 5 .   ? 16.161  -0.243  31.065  1.00 34.60 ? 594 HOH A O   1 
HETATM 8896 O  O   . HOH P 5 .   ? 41.367  10.422  0.676   1.00 36.56 ? 595 HOH A O   1 
HETATM 8897 O  O   . HOH P 5 .   ? 24.808  16.580  2.277   1.00 32.63 ? 596 HOH A O   1 
HETATM 8898 O  O   . HOH P 5 .   ? 15.006  -13.762 16.604  1.00 16.54 ? 597 HOH A O   1 
HETATM 8899 O  O   . HOH P 5 .   ? 17.268  8.159   20.174  1.00 20.45 ? 598 HOH A O   1 
HETATM 8900 O  O   . HOH P 5 .   ? 34.984  10.153  10.316  1.00 27.30 ? 599 HOH A O   1 
HETATM 8901 O  O   . HOH P 5 .   ? 28.040  -13.293 31.189  1.00 33.51 ? 600 HOH A O   1 
HETATM 8902 O  O   . HOH P 5 .   ? 39.846  -11.669 23.196  1.00 33.60 ? 601 HOH A O   1 
HETATM 8903 O  O   . HOH P 5 .   ? 17.638  -6.429  33.716  1.00 26.95 ? 602 HOH A O   1 
HETATM 8904 O  O   . HOH P 5 .   ? 45.391  -13.610 17.874  1.00 30.39 ? 603 HOH A O   1 
HETATM 8905 O  O   . HOH P 5 .   ? 28.516  -24.091 8.041   1.00 35.30 ? 604 HOH A O   1 
HETATM 8906 O  O   . HOH P 5 .   ? 6.116   -3.034  13.399  1.00 21.60 ? 605 HOH A O   1 
HETATM 8907 O  O   . HOH P 5 .   ? 15.794  14.005  -0.546  1.00 31.96 ? 606 HOH A O   1 
HETATM 8908 O  O   . HOH P 5 .   ? 20.052  -7.505  32.453  1.00 27.44 ? 607 HOH A O   1 
HETATM 8909 O  O   . HOH P 5 .   ? 39.957  -3.565  -1.813  1.00 35.66 ? 608 HOH A O   1 
HETATM 8910 O  O   . HOH P 5 .   ? 45.581  2.070   8.387   1.00 39.65 ? 609 HOH A O   1 
HETATM 8911 O  O   . HOH P 5 .   ? 26.891  -19.348 -1.233  1.00 40.90 ? 610 HOH A O   1 
HETATM 8912 O  O   . HOH P 5 .   ? 25.264  11.187  -2.997  1.00 36.42 ? 611 HOH A O   1 
HETATM 8913 O  O   . HOH P 5 .   ? 36.023  15.219  8.581   1.00 44.00 ? 612 HOH A O   1 
HETATM 8914 O  O   . HOH P 5 .   ? 34.146  -3.833  32.379  1.00 32.90 ? 613 HOH A O   1 
HETATM 8915 O  O   . HOH P 5 .   ? 43.859  2.147   2.799   1.00 29.57 ? 614 HOH A O   1 
HETATM 8916 O  O   . HOH P 5 .   ? 28.769  -18.452 20.579  1.00 21.55 ? 615 HOH A O   1 
HETATM 8917 O  O   . HOH P 5 .   ? 13.053  -14.586 12.784  1.00 34.93 ? 616 HOH A O   1 
HETATM 8918 O  O   . HOH P 5 .   ? 31.320  -8.498  -4.708  1.00 32.47 ? 617 HOH A O   1 
HETATM 8919 O  O   . HOH P 5 .   ? 34.097  -10.869 28.367  1.00 38.01 ? 618 HOH A O   1 
HETATM 8920 O  O   . HOH P 5 .   ? 30.031  -17.741 18.456  1.00 30.44 ? 619 HOH A O   1 
HETATM 8921 O  O   . HOH P 5 .   ? 39.788  2.897   16.856  1.00 32.36 ? 620 HOH A O   1 
HETATM 8922 O  O   . HOH P 5 .   ? 13.054  13.511  -1.953  1.00 35.32 ? 621 HOH A O   1 
HETATM 8923 O  O   . HOH P 5 .   ? 45.592  0.214   5.936   1.00 29.22 ? 622 HOH A O   1 
HETATM 8924 O  O   . HOH P 5 .   ? 9.989   3.487   -2.700  1.00 36.55 ? 623 HOH A O   1 
HETATM 8925 O  O   . HOH P 5 .   ? 19.951  14.542  26.072  1.00 38.48 ? 624 HOH A O   1 
HETATM 8926 O  O   . HOH P 5 .   ? 16.623  2.284   -7.883  1.00 36.29 ? 625 HOH A O   1 
HETATM 8927 O  O   . HOH P 5 .   ? 32.718  -14.947 -9.426  1.00 35.18 ? 626 HOH A O   1 
HETATM 8928 O  O   . HOH P 5 .   ? 36.047  -16.296 13.408  1.00 34.72 ? 627 HOH A O   1 
HETATM 8929 O  O   . HOH P 5 .   ? 11.598  5.864   -2.180  1.00 32.49 ? 628 HOH A O   1 
HETATM 8930 O  O   . HOH P 5 .   ? 42.042  -14.079 12.136  1.00 31.64 ? 629 HOH A O   1 
HETATM 8931 O  O   . HOH P 5 .   ? 11.094  -14.851 17.430  1.00 33.02 ? 630 HOH A O   1 
HETATM 8932 O  O   . HOH P 5 .   ? 24.221  -2.707  33.135  1.00 33.59 ? 631 HOH A O   1 
HETATM 8933 O  O   . HOH P 5 .   ? 7.140   -5.587  5.351   1.00 29.94 ? 632 HOH A O   1 
HETATM 8934 O  O   . HOH P 5 .   ? 24.576  13.073  37.945  1.00 42.95 ? 633 HOH A O   1 
HETATM 8935 O  O   . HOH P 5 .   ? 12.601  13.580  23.442  1.00 44.59 ? 634 HOH A O   1 
HETATM 8936 O  O   . HOH P 5 .   ? 33.711  -17.553 2.803   1.00 32.00 ? 635 HOH A O   1 
HETATM 8937 O  O   . HOH P 5 .   ? 7.827   6.675   15.658  1.00 15.52 ? 636 HOH A O   1 
HETATM 8938 O  O   . HOH P 5 .   ? 5.959   -0.428  -2.630  1.00 25.86 ? 637 HOH A O   1 
HETATM 8939 O  O   . HOH P 5 .   ? 23.370  -10.211 32.619  1.00 24.93 ? 638 HOH A O   1 
HETATM 8940 O  O   . HOH P 5 .   ? 10.317  -4.120  30.095  1.00 33.38 ? 639 HOH A O   1 
HETATM 8941 O  O   . HOH P 5 .   ? 40.754  -14.269 24.223  1.00 37.62 ? 640 HOH A O   1 
HETATM 8942 O  O   . HOH P 5 .   ? 13.803  21.279  11.685  1.00 33.42 ? 641 HOH A O   1 
HETATM 8943 O  O   . HOH P 5 .   ? 14.494  -12.368 29.558  1.00 18.31 ? 642 HOH A O   1 
HETATM 8944 O  O   . HOH P 5 .   ? 29.635  -3.860  -5.677  1.00 38.66 ? 643 HOH A O   1 
HETATM 8945 O  O   . HOH P 5 .   ? 38.886  -4.093  30.317  1.00 36.80 ? 644 HOH A O   1 
HETATM 8946 O  O   . HOH P 5 .   ? 26.455  13.974  35.961  1.00 34.33 ? 645 HOH A O   1 
HETATM 8947 O  O   . HOH P 5 .   ? 29.949  -18.097 -2.790  1.00 31.48 ? 646 HOH A O   1 
HETATM 8948 O  O   . HOH P 5 .   ? 26.905  -8.913  -13.268 1.00 31.63 ? 647 HOH A O   1 
HETATM 8949 O  O   . HOH P 5 .   ? 32.491  -15.003 28.336  1.00 32.43 ? 648 HOH A O   1 
HETATM 8950 O  O   . HOH P 5 .   ? 25.052  -14.193 31.081  1.00 35.96 ? 649 HOH A O   1 
HETATM 8951 O  O   . HOH P 5 .   ? 37.121  -6.643  31.557  1.00 34.11 ? 650 HOH A O   1 
HETATM 8952 O  O   . HOH P 5 .   ? 24.838  -5.240  31.431  1.00 27.15 ? 651 HOH A O   1 
HETATM 8953 O  O   . HOH P 5 .   ? 14.815  -14.056 25.627  1.00 26.27 ? 652 HOH A O   1 
HETATM 8954 O  O   . HOH P 5 .   ? 19.715  8.075   -4.292  1.00 40.33 ? 653 HOH A O   1 
HETATM 8955 O  O   . HOH P 5 .   ? 21.170  16.211  5.169   1.00 22.30 ? 654 HOH A O   1 
HETATM 8956 O  O   . HOH P 5 .   ? 21.242  2.425   -6.943  1.00 32.27 ? 655 HOH A O   1 
HETATM 8957 O  O   . HOH P 5 .   ? 15.622  4.862   -6.477  1.00 33.30 ? 656 HOH A O   1 
HETATM 8958 O  O   . HOH P 5 .   ? 17.052  15.880  -0.860  1.00 35.17 ? 657 HOH A O   1 
HETATM 8959 O  O   . HOH P 5 .   ? 4.184   13.595  22.529  1.00 32.46 ? 658 HOH A O   1 
HETATM 8960 O  O   . HOH P 5 .   ? 11.497  -12.929 26.035  1.00 25.12 ? 659 HOH A O   1 
HETATM 8961 O  O   . HOH P 5 .   ? 12.382  -15.846 10.766  1.00 29.46 ? 660 HOH A O   1 
HETATM 8962 O  O   . HOH P 5 .   ? 24.960  -18.528 30.289  1.00 35.46 ? 661 HOH A O   1 
HETATM 8963 O  O   . HOH P 5 .   ? 11.871  5.344   -4.384  1.00 33.09 ? 662 HOH A O   1 
HETATM 8964 O  O   . HOH P 5 .   ? 19.030  10.644  -4.216  1.00 29.26 ? 663 HOH A O   1 
HETATM 8965 O  O   . HOH P 5 .   ? 21.093  12.000  -2.771  1.00 30.14 ? 664 HOH A O   1 
HETATM 8966 O  O   . HOH P 5 .   ? 13.828  -17.163 7.517   1.00 27.40 ? 665 HOH A O   1 
HETATM 8967 O  O   . HOH P 5 .   ? 22.642  16.470  8.442   1.00 33.06 ? 666 HOH A O   1 
HETATM 8968 O  O   . HOH P 5 .   ? 33.543  -17.881 27.960  1.00 36.83 ? 667 HOH A O   1 
HETATM 8969 O  O   . HOH P 5 .   ? 18.643  6.792   -6.812  1.00 34.78 ? 668 HOH A O   1 
HETATM 8970 O  O   . HOH Q 5 .   ? -14.353 19.591  15.733  1.00 41.96 ? 401 HOH B O   1 
HETATM 8971 O  O   . HOH Q 5 .   ? -11.171 7.584   1.234   1.00 22.47 ? 402 HOH B O   1 
HETATM 8972 O  O   . HOH Q 5 .   ? 6.489   6.867   18.212  1.00 25.56 ? 403 HOH B O   1 
HETATM 8973 O  O   . HOH Q 5 .   ? -23.597 -8.762  15.068  1.00 35.15 ? 404 HOH B O   1 
HETATM 8974 O  O   . HOH Q 5 .   ? 6.397   0.922   22.222  1.00 28.64 ? 405 HOH B O   1 
HETATM 8975 O  O   . HOH Q 5 .   ? -10.726 2.959   -2.459  1.00 27.60 ? 406 HOH B O   1 
HETATM 8976 O  O   . HOH Q 5 .   ? -7.777  4.631   -0.126  1.00 20.17 ? 407 HOH B O   1 
HETATM 8977 O  O   . HOH Q 5 .   ? 7.706   11.863  14.968  1.00 23.61 ? 408 HOH B O   1 
HETATM 8978 O  O   . HOH Q 5 .   ? 3.213   1.298   -12.770 1.00 34.91 ? 409 HOH B O   1 
HETATM 8979 O  O   . HOH Q 5 .   ? -2.817  5.127   3.913   1.00 11.21 ? 410 HOH B O   1 
HETATM 8980 O  O   . HOH Q 5 .   ? 6.726   -11.501 17.490  1.00 27.47 ? 411 HOH B O   1 
HETATM 8981 O  O   . HOH Q 5 .   ? -0.019  16.858  -11.242 1.00 23.79 ? 412 HOH B O   1 
HETATM 8982 O  O   . HOH Q 5 .   ? 5.852   12.301  -4.283  1.00 17.81 ? 413 HOH B O   1 
HETATM 8983 O  O   . HOH Q 5 .   ? -26.866 9.114   -2.922  1.00 33.00 ? 414 HOH B O   1 
HETATM 8984 O  O   . HOH Q 5 .   ? -21.545 -9.896  9.963   1.00 34.04 ? 415 HOH B O   1 
HETATM 8985 O  O   . HOH Q 5 .   ? -21.849 1.411   18.616  1.00 26.09 ? 416 HOH B O   1 
HETATM 8986 O  O   . HOH Q 5 .   ? -21.289 11.428  6.285   1.00 31.24 ? 417 HOH B O   1 
HETATM 8987 O  O   . HOH Q 5 .   ? 2.626   6.788   16.736  1.00 24.41 ? 418 HOH B O   1 
HETATM 8988 O  O   . HOH Q 5 .   ? -20.352 -12.160 -2.431  1.00 27.24 ? 419 HOH B O   1 
HETATM 8989 O  O   . HOH Q 5 .   ? -20.241 -11.926 8.219   1.00 27.36 ? 420 HOH B O   1 
HETATM 8990 O  O   . HOH Q 5 .   ? 0.947   18.328  -14.227 1.00 26.38 ? 421 HOH B O   1 
HETATM 8991 O  O   . HOH Q 5 .   ? -23.976 7.991   23.268  1.00 36.38 ? 422 HOH B O   1 
HETATM 8992 O  O   . HOH Q 5 .   ? 7.322   -11.346 24.197  1.00 30.38 ? 423 HOH B O   1 
HETATM 8993 O  O   . HOH Q 5 .   ? -0.028  17.802  0.841   1.00 42.71 ? 424 HOH B O   1 
HETATM 8994 O  O   . HOH Q 5 .   ? -27.237 -10.095 1.601   1.00 21.18 ? 425 HOH B O   1 
HETATM 8995 O  O   . HOH Q 5 .   ? -16.846 -17.145 16.511  1.00 39.43 ? 426 HOH B O   1 
HETATM 8996 O  O   . HOH Q 5 .   ? -17.415 11.343  1.705   1.00 35.20 ? 427 HOH B O   1 
HETATM 8997 O  O   . HOH Q 5 .   ? -4.104  -17.794 22.619  1.00 23.48 ? 428 HOH B O   1 
HETATM 8998 O  O   . HOH Q 5 .   ? -13.647 7.580   -15.750 1.00 24.25 ? 429 HOH B O   1 
HETATM 8999 O  O   . HOH Q 5 .   ? -3.646  12.484  -18.125 1.00 24.16 ? 430 HOH B O   1 
HETATM 9000 O  O   . HOH Q 5 .   ? -5.861  -12.507 11.880  1.00 21.36 ? 431 HOH B O   1 
HETATM 9001 O  O   . HOH Q 5 .   ? -30.596 1.912   10.827  1.00 35.59 ? 432 HOH B O   1 
HETATM 9002 O  O   . HOH Q 5 .   ? -17.954 19.896  9.758   1.00 35.78 ? 433 HOH B O   1 
HETATM 9003 O  O   . HOH Q 5 .   ? -3.733  14.058  -6.888  1.00 23.19 ? 434 HOH B O   1 
HETATM 9004 O  O   . HOH Q 5 .   ? 6.304   16.719  0.980   1.00 29.40 ? 435 HOH B O   1 
HETATM 9005 O  O   . HOH Q 5 .   ? -4.340  -19.430 18.226  1.00 33.98 ? 436 HOH B O   1 
HETATM 9006 O  O   . HOH Q 5 .   ? -5.488  -11.477 -15.011 1.00 31.08 ? 437 HOH B O   1 
HETATM 9007 O  O   . HOH Q 5 .   ? -6.160  2.543   -17.019 1.00 37.15 ? 438 HOH B O   1 
HETATM 9008 O  O   . HOH Q 5 .   ? -7.498  -7.253  28.676  1.00 29.86 ? 439 HOH B O   1 
HETATM 9009 O  O   . HOH Q 5 .   ? -21.924 -2.444  -12.465 1.00 32.66 ? 440 HOH B O   1 
HETATM 9010 O  O   . HOH Q 5 .   ? -26.399 8.351   16.653  1.00 26.93 ? 441 HOH B O   1 
HETATM 9011 O  O   . HOH Q 5 .   ? 1.637   6.600   -8.147  1.00 15.32 ? 442 HOH B O   1 
HETATM 9012 O  O   . HOH Q 5 .   ? 12.530  14.686  2.368   1.00 15.03 ? 443 HOH B O   1 
HETATM 9013 O  O   . HOH Q 5 .   ? -27.171 -6.304  6.597   1.00 20.33 ? 444 HOH B O   1 
HETATM 9014 O  O   . HOH Q 5 .   ? -5.426  6.030   -0.206  1.00 18.24 ? 445 HOH B O   1 
HETATM 9015 O  O   . HOH Q 5 .   ? -3.252  2.615   21.223  1.00 28.43 ? 446 HOH B O   1 
HETATM 9016 O  O   . HOH Q 5 .   ? 7.715   21.466  7.918   1.00 13.14 ? 447 HOH B O   1 
HETATM 9017 O  O   . HOH Q 5 .   ? -17.902 -10.160 28.542  1.00 25.14 ? 448 HOH B O   1 
HETATM 9018 O  O   . HOH Q 5 .   ? -29.349 1.440   16.995  1.00 29.84 ? 449 HOH B O   1 
HETATM 9019 O  O   . HOH Q 5 .   ? 5.934   20.583  -5.422  1.00 27.93 ? 450 HOH B O   1 
HETATM 9020 O  O   . HOH Q 5 .   ? -3.070  -12.966 15.343  1.00 27.72 ? 451 HOH B O   1 
HETATM 9021 O  O   . HOH Q 5 .   ? -14.160 -14.928 28.424  1.00 27.82 ? 452 HOH B O   1 
HETATM 9022 O  O   . HOH Q 5 .   ? 3.304   5.183   16.284  1.00 26.57 ? 453 HOH B O   1 
HETATM 9023 O  O   . HOH Q 5 .   ? -4.634  0.245   21.979  1.00 22.65 ? 454 HOH B O   1 
HETATM 9024 O  O   . HOH Q 5 .   ? -17.613 -16.555 -6.543  1.00 26.60 ? 455 HOH B O   1 
HETATM 9025 O  O   . HOH Q 5 .   ? -4.120  16.241  -11.307 1.00 16.28 ? 456 HOH B O   1 
HETATM 9026 O  O   . HOH Q 5 .   ? -1.749  20.642  8.447   1.00 32.37 ? 457 HOH B O   1 
HETATM 9027 O  O   . HOH Q 5 .   ? -17.232 9.875   -14.300 1.00 33.41 ? 458 HOH B O   1 
HETATM 9028 O  O   . HOH Q 5 .   ? 6.512   3.353   9.187   1.00 9.07  ? 459 HOH B O   1 
HETATM 9029 O  O   . HOH Q 5 .   ? -8.218  -20.831 16.859  1.00 38.01 ? 460 HOH B O   1 
HETATM 9030 O  O   . HOH Q 5 .   ? 3.389   18.478  -15.788 1.00 38.58 ? 461 HOH B O   1 
HETATM 9031 O  O   . HOH Q 5 .   ? 4.305   6.485   14.230  1.00 12.64 ? 462 HOH B O   1 
HETATM 9032 O  O   . HOH Q 5 .   ? -1.860  -11.373 -3.133  1.00 19.37 ? 463 HOH B O   1 
HETATM 9033 O  O   . HOH Q 5 .   ? -5.537  1.592   -9.784  1.00 13.15 ? 464 HOH B O   1 
HETATM 9034 O  O   . HOH Q 5 .   ? -18.724 6.645   23.710  1.00 41.00 ? 465 HOH B O   1 
HETATM 9035 O  O   . HOH Q 5 .   ? -5.981  -18.205 -2.379  1.00 29.71 ? 466 HOH B O   1 
HETATM 9036 O  O   . HOH Q 5 .   ? -30.073 -4.498  -0.815  1.00 24.67 ? 467 HOH B O   1 
HETATM 9037 O  O   . HOH Q 5 .   ? -21.131 3.855   -12.811 1.00 20.11 ? 468 HOH B O   1 
HETATM 9038 O  O   . HOH Q 5 .   ? -18.071 9.592   -2.622  1.00 20.27 ? 469 HOH B O   1 
HETATM 9039 O  O   . HOH Q 5 .   ? -6.537  -11.314 29.207  1.00 26.61 ? 470 HOH B O   1 
HETATM 9040 O  O   . HOH Q 5 .   ? -9.696  16.124  10.261  1.00 33.61 ? 471 HOH B O   1 
HETATM 9041 O  O   . HOH Q 5 .   ? 4.008   11.785  -13.021 1.00 39.36 ? 472 HOH B O   1 
HETATM 9042 O  O   . HOH Q 5 .   ? -18.153 -3.958  26.582  1.00 27.95 ? 473 HOH B O   1 
HETATM 9043 O  O   . HOH Q 5 .   ? -24.091 -9.210  12.282  1.00 41.40 ? 474 HOH B O   1 
HETATM 9044 O  O   . HOH Q 5 .   ? 1.664   -1.512  5.850   1.00 9.29  ? 475 HOH B O   1 
HETATM 9045 O  O   . HOH Q 5 .   ? 11.340  14.619  -0.003  1.00 26.79 ? 476 HOH B O   1 
HETATM 9046 O  O   . HOH Q 5 .   ? -14.724 -13.350 23.947  1.00 25.35 ? 477 HOH B O   1 
HETATM 9047 O  O   . HOH Q 5 .   ? -2.886  -5.356  -4.164  1.00 9.09  ? 478 HOH B O   1 
HETATM 9048 O  O   . HOH Q 5 .   ? -1.282  14.142  -4.383  1.00 26.98 ? 479 HOH B O   1 
HETATM 9049 O  O   . HOH Q 5 .   ? -13.868 0.400   15.142  1.00 13.70 ? 480 HOH B O   1 
HETATM 9050 O  O   . HOH Q 5 .   ? 9.054   7.304   8.518   1.00 18.07 ? 481 HOH B O   1 
HETATM 9051 O  O   . HOH Q 5 .   ? -27.715 -4.289  8.658   1.00 18.11 ? 482 HOH B O   1 
HETATM 9052 O  O   . HOH Q 5 .   ? 5.184   6.472   1.050   1.00 10.99 ? 483 HOH B O   1 
HETATM 9053 O  O   . HOH Q 5 .   ? 3.672   3.504   -2.345  1.00 21.99 ? 484 HOH B O   1 
HETATM 9054 O  O   . HOH Q 5 .   ? 5.873   -9.486  13.444  1.00 18.70 ? 485 HOH B O   1 
HETATM 9055 O  O   . HOH Q 5 .   ? -23.166 9.538   6.435   1.00 18.45 ? 486 HOH B O   1 
HETATM 9056 O  O   . HOH Q 5 .   ? -30.735 7.223   -4.374  1.00 20.76 ? 487 HOH B O   1 
HETATM 9057 O  O   . HOH Q 5 .   ? -21.187 -4.986  21.896  1.00 19.58 ? 488 HOH B O   1 
HETATM 9058 O  O   . HOH Q 5 .   ? 4.422   17.201  3.770   1.00 24.85 ? 489 HOH B O   1 
HETATM 9059 O  O   . HOH Q 5 .   ? 1.233   0.627   -16.068 1.00 31.34 ? 490 HOH B O   1 
HETATM 9060 O  O   . HOH Q 5 .   ? -21.768 -8.674  -8.547  1.00 16.61 ? 491 HOH B O   1 
HETATM 9061 O  O   . HOH Q 5 .   ? -17.107 10.974  4.367   1.00 21.80 ? 492 HOH B O   1 
HETATM 9062 O  O   . HOH Q 5 .   ? -29.440 2.255   5.615   1.00 24.22 ? 493 HOH B O   1 
HETATM 9063 O  O   . HOH Q 5 .   ? -29.752 -3.259  7.078   1.00 25.29 ? 494 HOH B O   1 
HETATM 9064 O  O   . HOH Q 5 .   ? -22.988 -2.144  -8.670  1.00 14.77 ? 495 HOH B O   1 
HETATM 9065 O  O   . HOH Q 5 .   ? -8.412  -19.036 2.685   1.00 33.70 ? 496 HOH B O   1 
HETATM 9066 O  O   . HOH Q 5 .   ? -12.315 -13.480 -11.438 1.00 17.33 ? 497 HOH B O   1 
HETATM 9067 O  O   . HOH Q 5 .   ? -4.384  11.451  -15.186 1.00 17.38 ? 498 HOH B O   1 
HETATM 9068 O  O   . HOH Q 5 .   ? -17.546 -12.705 3.359   1.00 20.09 ? 499 HOH B O   1 
HETATM 9069 O  O   . HOH Q 5 .   ? -27.141 -3.671  -6.070  1.00 28.91 ? 500 HOH B O   1 
HETATM 9070 O  O   . HOH Q 5 .   ? 5.310   5.572   7.738   1.00 13.27 ? 501 HOH B O   1 
HETATM 9071 O  O   . HOH Q 5 .   ? -18.461 -8.162  16.059  1.00 16.98 ? 502 HOH B O   1 
HETATM 9072 O  O   . HOH Q 5 .   ? -24.647 -2.434  -6.411  1.00 16.94 ? 503 HOH B O   1 
HETATM 9073 O  O   . HOH Q 5 .   ? -31.797 5.287   -7.619  1.00 26.13 ? 504 HOH B O   1 
HETATM 9074 O  O   . HOH Q 5 .   ? -35.008 5.310   -5.182  1.00 31.73 ? 505 HOH B O   1 
HETATM 9075 O  O   . HOH Q 5 .   ? -6.058  -15.466 13.324  1.00 27.06 ? 506 HOH B O   1 
HETATM 9076 O  O   . HOH Q 5 .   ? -17.054 -10.840 1.228   1.00 15.62 ? 507 HOH B O   1 
HETATM 9077 O  O   . HOH Q 5 .   ? -20.546 -9.468  14.968  1.00 21.43 ? 508 HOH B O   1 
HETATM 9078 O  O   . HOH Q 5 .   ? -23.863 -7.804  20.474  1.00 30.67 ? 509 HOH B O   1 
HETATM 9079 O  O   . HOH Q 5 .   ? -13.628 13.304  22.812  1.00 34.17 ? 510 HOH B O   1 
HETATM 9080 O  O   . HOH Q 5 .   ? -8.894  -7.827  -14.525 1.00 18.21 ? 511 HOH B O   1 
HETATM 9081 O  O   . HOH Q 5 .   ? 2.727   -13.237 15.972  1.00 25.45 ? 512 HOH B O   1 
HETATM 9082 O  O   . HOH Q 5 .   ? -25.357 -4.247  20.956  1.00 43.68 ? 513 HOH B O   1 
HETATM 9083 O  O   . HOH Q 5 .   ? 3.658   -2.142  13.994  1.00 15.80 ? 514 HOH B O   1 
HETATM 9084 O  O   . HOH Q 5 .   ? -16.510 -12.329 25.713  1.00 26.42 ? 515 HOH B O   1 
HETATM 9085 O  O   . HOH Q 5 .   ? -19.839 -16.107 10.354  1.00 27.73 ? 516 HOH B O   1 
HETATM 9086 O  O   . HOH Q 5 .   ? -10.507 14.553  -13.938 1.00 16.57 ? 517 HOH B O   1 
HETATM 9087 O  O   . HOH Q 5 .   ? -3.281  7.552   -3.767  1.00 15.68 ? 518 HOH B O   1 
HETATM 9088 O  O   . HOH Q 5 .   ? -26.621 10.287  5.184   1.00 31.59 ? 519 HOH B O   1 
HETATM 9089 O  O   . HOH Q 5 .   ? 8.047   4.661   5.152   1.00 11.05 ? 520 HOH B O   1 
HETATM 9090 O  O   . HOH Q 5 .   ? -17.124 -10.463 20.243  1.00 15.61 ? 521 HOH B O   1 
HETATM 9091 O  O   . HOH Q 5 .   ? -10.341 -9.030  8.219   1.00 10.54 ? 522 HOH B O   1 
HETATM 9092 O  O   . HOH Q 5 .   ? 4.829   -9.647  -12.334 1.00 23.19 ? 523 HOH B O   1 
HETATM 9093 O  O   . HOH Q 5 .   ? -5.603  17.919  12.340  1.00 38.31 ? 524 HOH B O   1 
HETATM 9094 O  O   . HOH Q 5 .   ? -9.250  8.760   20.314  1.00 33.96 ? 525 HOH B O   1 
HETATM 9095 O  O   . HOH Q 5 .   ? 1.470   14.529  -11.163 1.00 15.97 ? 526 HOH B O   1 
HETATM 9096 O  O   . HOH Q 5 .   ? 5.965   -6.162  14.567  1.00 24.87 ? 527 HOH B O   1 
HETATM 9097 O  O   . HOH Q 5 .   ? 5.346   19.923  10.880  1.00 19.09 ? 528 HOH B O   1 
HETATM 9098 O  O   . HOH Q 5 .   ? -1.265  5.927   -4.885  1.00 13.61 ? 529 HOH B O   1 
HETATM 9099 O  O   . HOH Q 5 .   ? -1.722  16.713  11.148  1.00 13.71 ? 530 HOH B O   1 
HETATM 9100 O  O   . HOH Q 5 .   ? 2.172   6.196   -12.364 1.00 19.71 ? 531 HOH B O   1 
HETATM 9101 O  O   . HOH Q 5 .   ? -3.540  -3.058  29.055  1.00 34.40 ? 532 HOH B O   1 
HETATM 9102 O  O   . HOH Q 5 .   ? -1.182  -0.426  -12.649 1.00 21.48 ? 533 HOH B O   1 
HETATM 9103 O  O   . HOH Q 5 .   ? -14.571 -10.959 23.822  1.00 26.96 ? 534 HOH B O   1 
HETATM 9104 O  O   . HOH Q 5 .   ? 4.044   14.968  1.856   1.00 26.45 ? 535 HOH B O   1 
HETATM 9105 O  O   . HOH Q 5 .   ? -19.320 -0.889  -16.238 1.00 24.89 ? 536 HOH B O   1 
HETATM 9106 O  O   . HOH Q 5 .   ? -4.959  -12.773 22.024  1.00 32.93 ? 537 HOH B O   1 
HETATM 9107 O  O   . HOH Q 5 .   ? -0.704  11.992  16.274  1.00 18.12 ? 538 HOH B O   1 
HETATM 9108 O  O   . HOH Q 5 .   ? -26.874 -6.969  -1.596  1.00 22.99 ? 539 HOH B O   1 
HETATM 9109 O  O   . HOH Q 5 .   ? 2.092   5.254   -5.737  1.00 17.66 ? 540 HOH B O   1 
HETATM 9110 O  O   . HOH Q 5 .   ? 8.765   16.662  0.949   1.00 20.15 ? 541 HOH B O   1 
HETATM 9111 O  O   . HOH Q 5 .   ? -0.635  16.152  -8.682  1.00 22.27 ? 542 HOH B O   1 
HETATM 9112 O  O   . HOH Q 5 .   ? -27.369 7.088   -11.728 1.00 23.57 ? 543 HOH B O   1 
HETATM 9113 O  O   . HOH Q 5 .   ? -14.100 -14.888 5.933   1.00 19.61 ? 544 HOH B O   1 
HETATM 9114 O  O   . HOH Q 5 .   ? 1.063   13.189  19.519  1.00 31.25 ? 545 HOH B O   1 
HETATM 9115 O  O   . HOH Q 5 .   ? -6.024  -15.730 25.565  1.00 26.81 ? 546 HOH B O   1 
HETATM 9116 O  O   . HOH Q 5 .   ? -3.638  2.328   -11.997 1.00 16.42 ? 547 HOH B O   1 
HETATM 9117 O  O   . HOH Q 5 .   ? 4.766   9.198   14.456  1.00 12.97 ? 548 HOH B O   1 
HETATM 9118 O  O   . HOH Q 5 .   ? -12.683 -0.719  22.747  1.00 25.02 ? 549 HOH B O   1 
HETATM 9119 O  O   . HOH Q 5 .   ? 3.240   -2.084  26.659  1.00 35.17 ? 550 HOH B O   1 
HETATM 9120 O  O   . HOH Q 5 .   ? 4.188   10.165  -6.686  1.00 19.22 ? 551 HOH B O   1 
HETATM 9121 O  O   . HOH Q 5 .   ? -7.015  6.867   19.158  1.00 26.78 ? 552 HOH B O   1 
HETATM 9122 O  O   . HOH Q 5 .   ? -1.368  14.551  17.080  1.00 20.06 ? 553 HOH B O   1 
HETATM 9123 O  O   . HOH Q 5 .   ? -10.681 17.664  -8.379  1.00 24.68 ? 554 HOH B O   1 
HETATM 9124 O  O   . HOH Q 5 .   ? -32.587 -3.803  -1.941  1.00 28.86 ? 555 HOH B O   1 
HETATM 9125 O  O   . HOH Q 5 .   ? -27.586 11.978  20.312  1.00 37.57 ? 556 HOH B O   1 
HETATM 9126 O  O   . HOH Q 5 .   ? 1.654   9.095   -6.775  1.00 15.18 ? 557 HOH B O   1 
HETATM 9127 O  O   . HOH Q 5 .   ? 6.492   4.875   13.833  1.00 12.92 ? 558 HOH B O   1 
HETATM 9128 O  O   . HOH Q 5 .   ? 4.187   3.456   -5.950  1.00 19.47 ? 559 HOH B O   1 
HETATM 9129 O  O   . HOH Q 5 .   ? -29.108 7.369   -1.618  1.00 29.48 ? 560 HOH B O   1 
HETATM 9130 O  O   . HOH Q 5 .   ? 0.523   8.279   -4.448  1.00 20.03 ? 561 HOH B O   1 
HETATM 9131 O  O   . HOH Q 5 .   ? -16.424 4.981   22.050  1.00 32.97 ? 562 HOH B O   1 
HETATM 9132 O  O   . HOH Q 5 .   ? -13.369 -19.656 15.899  1.00 36.57 ? 563 HOH B O   1 
HETATM 9133 O  O   . HOH Q 5 .   ? -19.595 -13.702 14.522  1.00 24.64 ? 564 HOH B O   1 
HETATM 9134 O  O   . HOH Q 5 .   ? -4.174  -12.883 25.901  1.00 27.62 ? 565 HOH B O   1 
HETATM 9135 O  O   . HOH Q 5 .   ? -25.500 -7.321  13.018  1.00 24.97 ? 566 HOH B O   1 
HETATM 9136 O  O   . HOH Q 5 .   ? -23.429 11.688  -1.096  1.00 24.93 ? 567 HOH B O   1 
HETATM 9137 O  O   . HOH Q 5 .   ? 7.061   -0.913  17.945  1.00 19.30 ? 568 HOH B O   1 
HETATM 9138 O  O   . HOH Q 5 .   ? -24.131 1.112   20.997  1.00 33.24 ? 569 HOH B O   1 
HETATM 9139 O  O   . HOH Q 5 .   ? -24.317 8.989   -1.655  1.00 19.19 ? 570 HOH B O   1 
HETATM 9140 O  O   . HOH Q 5 .   ? -13.402 -6.676  -11.276 1.00 21.81 ? 571 HOH B O   1 
HETATM 9141 O  O   . HOH Q 5 .   ? 4.784   -5.451  8.630   1.00 28.43 ? 572 HOH B O   1 
HETATM 9142 O  O   . HOH Q 5 .   ? -26.189 -9.763  6.057   1.00 21.88 ? 573 HOH B O   1 
HETATM 9143 O  O   . HOH Q 5 .   ? -3.458  -8.678  -9.288  1.00 27.64 ? 574 HOH B O   1 
HETATM 9144 O  O   . HOH Q 5 .   ? 4.150   -9.147  3.045   1.00 26.15 ? 575 HOH B O   1 
HETATM 9145 O  O   . HOH Q 5 .   ? -22.735 6.186   -12.398 1.00 27.99 ? 576 HOH B O   1 
HETATM 9146 O  O   . HOH Q 5 .   ? 4.009   -2.470  -3.242  1.00 28.52 ? 577 HOH B O   1 
HETATM 9147 O  O   . HOH Q 5 .   ? -14.584 -14.152 0.730   1.00 17.66 ? 578 HOH B O   1 
HETATM 9148 O  O   . HOH Q 5 .   ? -5.917  11.593  20.718  1.00 24.23 ? 579 HOH B O   1 
HETATM 9149 O  O   . HOH Q 5 .   ? 4.128   8.276   7.748   1.00 10.27 ? 580 HOH B O   1 
HETATM 9150 O  O   . HOH Q 5 .   ? -30.902 2.090   2.133   1.00 30.58 ? 581 HOH B O   1 
HETATM 9151 O  O   . HOH Q 5 .   ? -3.237  -12.667 -0.909  1.00 20.74 ? 582 HOH B O   1 
HETATM 9152 O  O   . HOH Q 5 .   ? -27.166 -7.396  10.710  1.00 34.21 ? 583 HOH B O   1 
HETATM 9153 O  O   . HOH Q 5 .   ? -0.641  -9.219  27.553  1.00 36.89 ? 584 HOH B O   1 
HETATM 9154 O  O   . HOH Q 5 .   ? -13.028 -17.275 7.322   1.00 39.61 ? 585 HOH B O   1 
HETATM 9155 O  O   . HOH Q 5 .   ? -15.412 19.870  11.781  1.00 36.24 ? 586 HOH B O   1 
HETATM 9156 O  O   . HOH Q 5 .   ? 4.352   -2.016  6.467   1.00 18.22 ? 587 HOH B O   1 
HETATM 9157 O  O   . HOH Q 5 .   ? -10.567 -10.395 29.763  1.00 25.18 ? 588 HOH B O   1 
HETATM 9158 O  O   . HOH Q 5 .   ? -2.914  -0.115  25.268  1.00 21.83 ? 589 HOH B O   1 
HETATM 9159 O  O   . HOH Q 5 .   ? 1.020   -8.991  25.495  1.00 28.54 ? 590 HOH B O   1 
HETATM 9160 O  O   . HOH Q 5 .   ? -5.745  15.616  1.958   1.00 25.03 ? 591 HOH B O   1 
HETATM 9161 O  O   . HOH Q 5 .   ? -31.888 -6.487  6.094   1.00 30.72 ? 592 HOH B O   1 
HETATM 9162 O  O   . HOH Q 5 .   ? 4.469   -13.331 22.349  1.00 33.07 ? 593 HOH B O   1 
HETATM 9163 O  O   . HOH Q 5 .   ? -17.781 12.914  -12.691 1.00 32.02 ? 594 HOH B O   1 
HETATM 9164 O  O   . HOH Q 5 .   ? -1.994  11.875  -5.093  1.00 17.15 ? 595 HOH B O   1 
HETATM 9165 O  O   . HOH Q 5 .   ? -13.454 -11.976 11.613  1.00 13.55 ? 596 HOH B O   1 
HETATM 9166 O  O   . HOH Q 5 .   ? 8.691   8.805   1.908   1.00 22.41 ? 597 HOH B O   1 
HETATM 9167 O  O   . HOH Q 5 .   ? -12.774 13.308  3.892   1.00 35.91 ? 598 HOH B O   1 
HETATM 9168 O  O   . HOH Q 5 .   ? -16.112 -5.579  -12.852 1.00 25.97 ? 599 HOH B O   1 
HETATM 9169 O  O   . HOH Q 5 .   ? -2.858  1.808   -14.698 1.00 28.52 ? 600 HOH B O   1 
HETATM 9170 O  O   . HOH Q 5 .   ? -21.667 10.338  3.306   1.00 28.55 ? 601 HOH B O   1 
HETATM 9171 O  O   . HOH Q 5 .   ? -20.472 13.443  7.757   1.00 27.23 ? 602 HOH B O   1 
HETATM 9172 O  O   . HOH Q 5 .   ? -27.326 -6.044  -4.739  1.00 31.26 ? 603 HOH B O   1 
HETATM 9173 O  O   . HOH Q 5 .   ? -14.157 10.955  3.310   1.00 27.77 ? 604 HOH B O   1 
HETATM 9174 O  O   . HOH Q 5 .   ? -11.091 -15.839 3.091   1.00 27.87 ? 605 HOH B O   1 
HETATM 9175 O  O   . HOH Q 5 .   ? -8.076  -16.593 -11.407 1.00 32.02 ? 606 HOH B O   1 
HETATM 9176 O  O   . HOH Q 5 .   ? 3.254   21.490  9.464   1.00 24.29 ? 607 HOH B O   1 
HETATM 9177 O  O   . HOH Q 5 .   ? -14.836 -14.739 -2.614  1.00 16.16 ? 608 HOH B O   1 
HETATM 9178 O  O   . HOH Q 5 .   ? -20.396 -13.430 11.786  1.00 27.30 ? 609 HOH B O   1 
HETATM 9179 O  O   . HOH Q 5 .   ? -20.855 -18.915 6.803   1.00 36.08 ? 610 HOH B O   1 
HETATM 9180 O  O   . HOH Q 5 .   ? 5.907   -2.378  1.636   1.00 30.70 ? 611 HOH B O   1 
HETATM 9181 O  O   . HOH Q 5 .   ? -34.893 -2.694  -2.189  1.00 33.63 ? 612 HOH B O   1 
HETATM 9182 O  O   . HOH Q 5 .   ? -5.364  14.550  -4.729  1.00 29.40 ? 613 HOH B O   1 
HETATM 9183 O  O   . HOH Q 5 .   ? 7.566   -3.320  3.516   1.00 22.37 ? 614 HOH B O   1 
HETATM 9184 O  O   . HOH Q 5 .   ? -26.892 9.654   12.374  1.00 36.40 ? 615 HOH B O   1 
HETATM 9185 O  O   . HOH Q 5 .   ? 8.823   6.351   -1.870  1.00 22.83 ? 616 HOH B O   1 
HETATM 9186 O  O   . HOH Q 5 .   ? -1.832  9.806   -3.271  1.00 21.19 ? 617 HOH B O   1 
HETATM 9187 O  O   . HOH Q 5 .   ? -9.552  16.899  -16.133 1.00 22.84 ? 618 HOH B O   1 
HETATM 9188 O  O   . HOH Q 5 .   ? -2.586  -10.631 -14.916 1.00 31.62 ? 619 HOH B O   1 
HETATM 9189 O  O   . HOH Q 5 .   ? -29.681 8.450   6.321   1.00 30.60 ? 620 HOH B O   1 
HETATM 9190 O  O   . HOH Q 5 .   ? -24.723 -1.086  -11.490 1.00 24.27 ? 621 HOH B O   1 
HETATM 9191 O  O   . HOH Q 5 .   ? -13.010 14.697  -15.480 1.00 33.78 ? 622 HOH B O   1 
HETATM 9192 O  O   . HOH Q 5 .   ? -3.057  -12.113 1.104   1.00 26.65 ? 623 HOH B O   1 
HETATM 9193 O  O   . HOH Q 5 .   ? 12.375  11.480  -3.743  1.00 29.00 ? 624 HOH B O   1 
HETATM 9194 O  O   . HOH Q 5 .   ? 1.112   22.680  9.833   1.00 30.60 ? 625 HOH B O   1 
HETATM 9195 O  O   . HOH Q 5 .   ? -27.658 -10.027 -4.101  1.00 44.48 ? 626 HOH B O   1 
HETATM 9196 O  O   . HOH Q 5 .   ? -24.883 8.407   1.283   1.00 25.02 ? 627 HOH B O   1 
HETATM 9197 O  O   . HOH Q 5 .   ? -3.543  16.254  -8.745  1.00 30.63 ? 628 HOH B O   1 
HETATM 9198 O  O   . HOH Q 5 .   ? -25.446 15.120  17.304  1.00 37.44 ? 629 HOH B O   1 
HETATM 9199 O  O   . HOH Q 5 .   ? -10.743 15.771  -5.731  1.00 39.70 ? 630 HOH B O   1 
HETATM 9200 O  O   . HOH Q 5 .   ? -21.631 -6.337  -9.789  1.00 28.23 ? 631 HOH B O   1 
HETATM 9201 O  O   . HOH Q 5 .   ? 7.717   1.345   19.741  1.00 27.48 ? 632 HOH B O   1 
HETATM 9202 O  O   . HOH Q 5 .   ? -0.817  -13.014 4.434   1.00 43.71 ? 633 HOH B O   1 
HETATM 9203 O  O   . HOH Q 5 .   ? -6.692  15.376  16.023  1.00 29.72 ? 634 HOH B O   1 
HETATM 9204 O  O   . HOH Q 5 .   ? -30.233 4.340   2.874   1.00 33.05 ? 635 HOH B O   1 
HETATM 9205 O  O   . HOH Q 5 .   ? -17.638 -14.257 -2.390  1.00 29.20 ? 636 HOH B O   1 
HETATM 9206 O  O   . HOH Q 5 .   ? -0.111  -13.144 -4.532  1.00 28.89 ? 637 HOH B O   1 
HETATM 9207 O  O   . HOH Q 5 .   ? -23.980 -10.980 4.960   1.00 35.48 ? 638 HOH B O   1 
HETATM 9208 O  O   . HOH Q 5 .   ? 2.214   -15.786 16.844  1.00 31.34 ? 639 HOH B O   1 
HETATM 9209 O  O   . HOH Q 5 .   ? -8.306  18.459  -3.886  1.00 36.63 ? 640 HOH B O   1 
HETATM 9210 O  O   . HOH Q 5 .   ? 5.867   13.708  -6.555  1.00 39.90 ? 641 HOH B O   1 
HETATM 9211 O  O   . HOH Q 5 .   ? 8.084   10.603  -7.404  1.00 35.85 ? 642 HOH B O   1 
HETATM 9212 O  O   . HOH Q 5 .   ? -20.124 -9.766  -12.215 1.00 38.50 ? 643 HOH B O   1 
HETATM 9213 O  O   . HOH Q 5 .   ? -23.328 -4.513  -10.111 1.00 30.48 ? 644 HOH B O   1 
HETATM 9214 O  O   . HOH Q 5 .   ? 5.895   2.314   -3.615  1.00 25.70 ? 645 HOH B O   1 
HETATM 9215 O  O   . HOH Q 5 .   ? 4.075   15.008  -10.598 1.00 31.29 ? 646 HOH B O   1 
HETATM 9216 O  O   . HOH Q 5 .   ? -13.860 -5.114  -13.064 1.00 37.06 ? 647 HOH B O   1 
HETATM 9217 O  O   . HOH Q 5 .   ? -12.896 -9.011  -12.638 1.00 27.96 ? 648 HOH B O   1 
HETATM 9218 O  O   . HOH Q 5 .   ? -3.829  15.354  18.051  1.00 31.59 ? 649 HOH B O   1 
HETATM 9219 O  O   . HOH Q 5 .   ? -8.017  -5.720  -15.766 1.00 27.27 ? 650 HOH B O   1 
HETATM 9220 O  O   . HOH Q 5 .   ? -11.394 -8.214  -15.030 1.00 29.18 ? 651 HOH B O   1 
HETATM 9221 O  O   . HOH Q 5 .   ? -3.543  -17.653 20.054  1.00 28.54 ? 652 HOH B O   1 
HETATM 9222 O  O   . HOH Q 5 .   ? 7.832   6.088   0.794   1.00 21.10 ? 653 HOH B O   1 
HETATM 9223 O  O   . HOH Q 5 .   ? -16.926 -14.092 27.651  1.00 23.97 ? 654 HOH B O   1 
HETATM 9224 O  O   . HOH Q 5 .   ? -21.540 -12.183 15.886  1.00 22.95 ? 655 HOH B O   1 
HETATM 9225 O  O   . HOH Q 5 .   ? 7.585   -9.523  15.797  1.00 25.30 ? 656 HOH B O   1 
HETATM 9226 O  O   . HOH Q 5 .   ? -4.680  -13.790 9.755   1.00 30.03 ? 657 HOH B O   1 
HETATM 9227 O  O   . HOH Q 5 .   ? -19.273 -16.392 -4.109  1.00 29.34 ? 658 HOH B O   1 
HETATM 9228 O  O   . HOH Q 5 .   ? -17.620 -12.778 21.226  1.00 27.62 ? 659 HOH B O   1 
HETATM 9229 O  O   . HOH Q 5 .   ? 2.556   -11.237 -11.738 1.00 38.08 ? 660 HOH B O   1 
HETATM 9230 O  O   . HOH Q 5 .   ? 1.878   18.496  -11.993 1.00 33.64 ? 661 HOH B O   1 
HETATM 9231 O  O   . HOH Q 5 .   ? -4.147  1.471   24.167  1.00 33.72 ? 662 HOH B O   1 
HETATM 9232 O  O   . HOH Q 5 .   ? -15.589 -14.728 3.591   1.00 31.94 ? 663 HOH B O   1 
HETATM 9233 O  O   . HOH Q 5 .   ? 5.371   -13.202 15.829  1.00 23.10 ? 664 HOH B O   1 
HETATM 9234 O  O   . HOH Q 5 .   ? 4.430   -12.053 24.853  1.00 28.90 ? 665 HOH B O   1 
HETATM 9235 O  O   . HOH Q 5 .   ? -29.394 7.198   1.293   1.00 35.34 ? 666 HOH B O   1 
HETATM 9236 O  O   . HOH Q 5 .   ? 4.977   -7.112  1.063   1.00 22.04 ? 667 HOH B O   1 
HETATM 9237 O  O   . HOH Q 5 .   ? -18.907 -11.778 23.790  1.00 29.65 ? 668 HOH B O   1 
HETATM 9238 O  O   . HOH Q 5 .   ? -13.414 -11.556 -13.074 1.00 21.99 ? 669 HOH B O   1 
HETATM 9239 O  O   . HOH Q 5 .   ? -13.398 -21.110 3.920   1.00 31.23 ? 670 HOH B O   1 
HETATM 9240 O  O   . HOH Q 5 .   ? -21.012 -10.853 -10.035 1.00 24.35 ? 671 HOH B O   1 
HETATM 9241 O  O   . HOH Q 5 .   ? -13.062 -14.307 30.691  1.00 24.38 ? 672 HOH B O   1 
HETATM 9242 O  O   . HOH Q 5 .   ? 5.594   9.654   -9.032  1.00 33.24 ? 673 HOH B O   1 
HETATM 9243 O  O   . HOH Q 5 .   ? -3.099  18.919  10.750  1.00 35.98 ? 674 HOH B O   1 
HETATM 9244 O  O   . HOH Q 5 .   ? 3.779   6.421   -9.757  1.00 28.33 ? 675 HOH B O   1 
HETATM 9245 O  O   . HOH Q 5 .   ? -19.260 -16.047 15.806  1.00 31.63 ? 676 HOH B O   1 
HETATM 9246 O  O   . HOH Q 5 .   ? -13.337 15.567  -17.902 1.00 31.54 ? 677 HOH B O   1 
HETATM 9247 O  O   . HOH Q 5 .   ? -7.647  -9.846  -15.942 1.00 19.86 ? 678 HOH B O   1 
HETATM 9248 O  O   . HOH Q 5 .   ? 10.688  9.417   -7.273  1.00 42.62 ? 679 HOH B O   1 
HETATM 9249 O  O   . HOH Q 5 .   ? 12.809  11.618  -6.330  1.00 29.84 ? 680 HOH B O   1 
HETATM 9250 O  O   . HOH Q 5 .   ? -2.104  20.410  13.176  1.00 33.21 ? 681 HOH B O   1 
HETATM 9251 O  O   . HOH Q 5 .   ? -10.301 -13.236 30.610  1.00 24.75 ? 682 HOH B O   1 
HETATM 9252 O  O   . HOH Q 5 .   ? -3.471  4.158   23.853  1.00 34.65 ? 683 HOH B O   1 
HETATM 9253 O  O   . HOH Q 5 .   ? -4.534  19.462  8.702   1.00 37.82 ? 684 HOH B O   1 
HETATM 9254 O  O   . HOH Q 5 .   ? -21.951 -13.388 18.137  1.00 39.17 ? 685 HOH B O   1 
HETATM 9255 O  O   . HOH Q 5 .   ? -19.853 -14.317 20.274  1.00 30.70 ? 686 HOH B O   1 
HETATM 9256 O  O   . HOH R 5 .   ? 19.876  1.305   -51.638 1.00 27.28 ? 401 HOH C O   1 
HETATM 9257 O  O   . HOH R 5 .   ? 47.456  -1.350  -9.523  1.00 31.37 ? 402 HOH C O   1 
HETATM 9258 O  O   . HOH R 5 .   ? 35.594  -21.437 -51.133 1.00 23.25 ? 403 HOH C O   1 
HETATM 9259 O  O   . HOH R 5 .   ? 21.126  9.307   -25.846 1.00 26.96 ? 404 HOH C O   1 
HETATM 9260 O  O   . HOH R 5 .   ? 28.753  -7.948  -17.065 1.00 26.97 ? 405 HOH C O   1 
HETATM 9261 O  O   . HOH R 5 .   ? 57.209  -8.124  -23.554 1.00 36.35 ? 406 HOH C O   1 
HETATM 9262 O  O   . HOH R 5 .   ? 41.959  6.800   -10.087 1.00 36.89 ? 407 HOH C O   1 
HETATM 9263 O  O   . HOH R 5 .   ? 20.395  -10.370 -29.886 1.00 21.84 ? 408 HOH C O   1 
HETATM 9264 O  O   . HOH R 5 .   ? 22.474  -9.094  -39.870 1.00 28.30 ? 409 HOH C O   1 
HETATM 9265 O  O   . HOH R 5 .   ? 28.527  18.219  -31.648 1.00 18.66 ? 410 HOH C O   1 
HETATM 9266 O  O   . HOH R 5 .   ? 32.989  -18.600 -49.903 1.00 33.65 ? 411 HOH C O   1 
HETATM 9267 O  O   . HOH R 5 .   ? 27.642  16.236  -41.124 1.00 15.56 ? 412 HOH C O   1 
HETATM 9268 O  O   . HOH R 5 .   ? 50.118  -9.539  -46.114 1.00 32.18 ? 413 HOH C O   1 
HETATM 9269 O  O   . HOH R 5 .   ? 32.591  4.881   -30.473 1.00 18.40 ? 414 HOH C O   1 
HETATM 9270 O  O   . HOH R 5 .   ? 61.965  -0.968  -32.467 1.00 29.24 ? 415 HOH C O   1 
HETATM 9271 O  O   . HOH R 5 .   ? 33.264  11.886  -11.061 1.00 27.14 ? 416 HOH C O   1 
HETATM 9272 O  O   . HOH R 5 .   ? 60.000  -2.758  -25.566 1.00 37.51 ? 417 HOH C O   1 
HETATM 9273 O  O   . HOH R 5 .   ? 46.847  -14.879 -22.175 1.00 44.32 ? 418 HOH C O   1 
HETATM 9274 O  O   . HOH R 5 .   ? 25.957  5.216   -24.271 1.00 32.46 ? 419 HOH C O   1 
HETATM 9275 O  O   . HOH R 5 .   ? 46.368  8.120   -11.445 1.00 31.63 ? 420 HOH C O   1 
HETATM 9276 O  O   . HOH R 5 .   ? 28.611  3.426   -43.527 1.00 17.38 ? 421 HOH C O   1 
HETATM 9277 O  O   . HOH R 5 .   ? 28.079  15.892  -29.315 1.00 25.80 ? 422 HOH C O   1 
HETATM 9278 O  O   . HOH R 5 .   ? 52.771  4.844   -48.920 1.00 29.70 ? 423 HOH C O   1 
HETATM 9279 O  O   . HOH R 5 .   ? 22.417  -6.412  -31.595 1.00 23.11 ? 424 HOH C O   1 
HETATM 9280 O  O   . HOH R 5 .   ? 35.777  -13.641 -54.576 1.00 19.82 ? 425 HOH C O   1 
HETATM 9281 O  O   . HOH R 5 .   ? 40.619  -5.629  -52.864 1.00 32.85 ? 426 HOH C O   1 
HETATM 9282 O  O   . HOH R 5 .   ? 20.826  -2.243  -50.881 1.00 29.88 ? 427 HOH C O   1 
HETATM 9283 O  O   . HOH R 5 .   ? 45.419  -7.126  -45.515 1.00 17.72 ? 428 HOH C O   1 
HETATM 9284 O  O   . HOH R 5 .   ? 25.429  8.016   -27.991 1.00 22.55 ? 429 HOH C O   1 
HETATM 9285 O  O   . HOH R 5 .   ? 33.331  -1.603  -49.112 1.00 22.62 ? 430 HOH C O   1 
HETATM 9286 O  O   . HOH R 5 .   ? 62.922  3.499   -26.187 1.00 34.48 ? 431 HOH C O   1 
HETATM 9287 O  O   . HOH R 5 .   ? 25.894  -3.201  -48.331 1.00 25.81 ? 432 HOH C O   1 
HETATM 9288 O  O   . HOH R 5 .   ? 41.724  -8.363  -54.922 1.00 22.95 ? 433 HOH C O   1 
HETATM 9289 O  O   . HOH R 5 .   ? 24.994  -13.194 -41.603 1.00 30.51 ? 434 HOH C O   1 
HETATM 9290 O  O   . HOH R 5 .   ? 40.315  -16.705 -30.543 1.00 26.81 ? 435 HOH C O   1 
HETATM 9291 O  O   . HOH R 5 .   ? 43.850  4.050   -44.340 1.00 21.50 ? 436 HOH C O   1 
HETATM 9292 O  O   . HOH R 5 .   ? 33.390  22.331  -34.636 1.00 33.91 ? 437 HOH C O   1 
HETATM 9293 O  O   . HOH R 5 .   ? 25.183  6.446   -34.615 1.00 13.65 ? 438 HOH C O   1 
HETATM 9294 O  O   . HOH R 5 .   ? 51.411  8.305   -31.202 1.00 28.98 ? 439 HOH C O   1 
HETATM 9295 O  O   . HOH R 5 .   ? 27.246  -0.886  -32.272 1.00 11.68 ? 440 HOH C O   1 
HETATM 9296 O  O   . HOH R 5 .   ? 58.506  -1.971  -29.833 1.00 30.49 ? 441 HOH C O   1 
HETATM 9297 O  O   . HOH R 5 .   ? 41.739  -19.112 -18.789 1.00 47.22 ? 442 HOH C O   1 
HETATM 9298 O  O   . HOH R 5 .   ? 46.971  11.286  -22.186 1.00 31.36 ? 443 HOH C O   1 
HETATM 9299 O  O   . HOH R 5 .   ? 51.674  -2.499  -43.730 1.00 27.33 ? 444 HOH C O   1 
HETATM 9300 O  O   . HOH R 5 .   ? 24.195  13.101  -42.444 1.00 18.56 ? 445 HOH C O   1 
HETATM 9301 O  O   . HOH R 5 .   ? 25.375  -1.738  -40.667 1.00 12.23 ? 446 HOH C O   1 
HETATM 9302 O  O   . HOH R 5 .   ? 41.424  7.214   -46.842 1.00 25.48 ? 447 HOH C O   1 
HETATM 9303 O  O   . HOH R 5 .   ? 33.925  1.596   -16.643 1.00 22.06 ? 448 HOH C O   1 
HETATM 9304 O  O   . HOH R 5 .   ? 50.694  -4.328  -53.942 1.00 35.47 ? 449 HOH C O   1 
HETATM 9305 O  O   . HOH R 5 .   ? 38.408  -14.701 -13.784 1.00 35.12 ? 450 HOH C O   1 
HETATM 9306 O  O   . HOH R 5 .   ? 23.595  -4.689  -35.993 1.00 23.13 ? 451 HOH C O   1 
HETATM 9307 O  O   . HOH R 5 .   ? 29.733  -5.204  -22.082 1.00 17.36 ? 452 HOH C O   1 
HETATM 9308 O  O   . HOH R 5 .   ? 53.747  -10.024 -22.470 1.00 31.08 ? 453 HOH C O   1 
HETATM 9309 O  O   . HOH R 5 .   ? 42.451  -17.565 -53.837 1.00 33.62 ? 454 HOH C O   1 
HETATM 9310 O  O   . HOH R 5 .   ? 34.311  15.931  -38.288 1.00 12.97 ? 455 HOH C O   1 
HETATM 9311 O  O   . HOH R 5 .   ? 22.168  -1.161  -23.870 1.00 29.88 ? 456 HOH C O   1 
HETATM 9312 O  O   . HOH R 5 .   ? 43.347  -2.343  -40.340 1.00 15.00 ? 457 HOH C O   1 
HETATM 9313 O  O   . HOH R 5 .   ? 32.939  -13.618 -37.070 1.00 21.43 ? 458 HOH C O   1 
HETATM 9314 O  O   . HOH R 5 .   ? 22.561  -8.487  -17.306 1.00 36.05 ? 459 HOH C O   1 
HETATM 9315 O  O   . HOH R 5 .   ? 47.199  9.126   -27.028 1.00 24.85 ? 460 HOH C O   1 
HETATM 9316 O  O   . HOH R 5 .   ? 47.043  -13.130 -53.063 1.00 19.19 ? 461 HOH C O   1 
HETATM 9317 O  O   . HOH R 5 .   ? 41.005  13.879  -36.819 1.00 25.50 ? 462 HOH C O   1 
HETATM 9318 O  O   . HOH R 5 .   ? 23.081  -11.672 -44.568 1.00 27.27 ? 463 HOH C O   1 
HETATM 9319 O  O   . HOH R 5 .   ? 26.104  -3.546  -42.673 1.00 19.94 ? 464 HOH C O   1 
HETATM 9320 O  O   . HOH R 5 .   ? 40.253  -22.222 -21.352 1.00 45.98 ? 465 HOH C O   1 
HETATM 9321 O  O   . HOH R 5 .   ? 40.455  -8.030  -13.774 1.00 40.32 ? 466 HOH C O   1 
HETATM 9322 O  O   . HOH R 5 .   ? 56.963  1.693   -37.395 1.00 34.40 ? 467 HOH C O   1 
HETATM 9323 O  O   . HOH R 5 .   ? 24.025  8.886   -35.010 1.00 15.99 ? 468 HOH C O   1 
HETATM 9324 O  O   . HOH R 5 .   ? 55.883  -8.161  -32.595 1.00 25.11 ? 469 HOH C O   1 
HETATM 9325 O  O   . HOH R 5 .   ? 27.435  -10.634 -26.689 1.00 23.29 ? 470 HOH C O   1 
HETATM 9326 O  O   . HOH R 5 .   ? 54.700  -9.900  -31.010 1.00 34.39 ? 471 HOH C O   1 
HETATM 9327 O  O   . HOH R 5 .   ? 43.018  -1.395  -10.645 1.00 41.33 ? 472 HOH C O   1 
HETATM 9328 O  O   . HOH R 5 .   ? 28.029  -10.750 -22.365 1.00 25.07 ? 473 HOH C O   1 
HETATM 9329 O  O   . HOH R 5 .   ? 28.323  -10.571 -51.303 1.00 38.54 ? 474 HOH C O   1 
HETATM 9330 O  O   . HOH R 5 .   ? 22.261  6.771   -32.207 1.00 11.92 ? 475 HOH C O   1 
HETATM 9331 O  O   . HOH R 5 .   ? 21.018  13.517  -35.633 1.00 11.83 ? 476 HOH C O   1 
HETATM 9332 O  O   . HOH R 5 .   ? 44.997  -13.831 -44.600 1.00 20.98 ? 477 HOH C O   1 
HETATM 9333 O  O   . HOH R 5 .   ? 33.268  16.231  -14.968 1.00 37.33 ? 478 HOH C O   1 
HETATM 9334 O  O   . HOH R 5 .   ? 26.349  3.218   -47.376 1.00 29.82 ? 479 HOH C O   1 
HETATM 9335 O  O   . HOH R 5 .   ? 26.475  -8.584  -15.927 1.00 29.45 ? 480 HOH C O   1 
HETATM 9336 O  O   . HOH R 5 .   ? 48.075  -8.964  -51.166 1.00 33.86 ? 481 HOH C O   1 
HETATM 9337 O  O   . HOH R 5 .   ? 22.416  -5.349  -40.990 1.00 28.19 ? 482 HOH C O   1 
HETATM 9338 O  O   . HOH R 5 .   ? 19.663  -7.666  -17.480 1.00 30.51 ? 483 HOH C O   1 
HETATM 9339 O  O   . HOH R 5 .   ? 37.757  -10.566 -33.394 1.00 18.16 ? 484 HOH C O   1 
HETATM 9340 O  O   . HOH R 5 .   ? 46.410  -11.267 -40.442 1.00 25.77 ? 485 HOH C O   1 
HETATM 9341 O  O   . HOH R 5 .   ? 32.680  11.220  -43.234 1.00 13.96 ? 486 HOH C O   1 
HETATM 9342 O  O   . HOH R 5 .   ? 20.574  17.735  -29.769 1.00 32.67 ? 487 HOH C O   1 
HETATM 9343 O  O   . HOH R 5 .   ? 29.673  -14.254 -28.209 1.00 28.76 ? 488 HOH C O   1 
HETATM 9344 O  O   . HOH R 5 .   ? 24.679  4.951   -20.759 1.00 32.64 ? 489 HOH C O   1 
HETATM 9345 O  O   . HOH R 5 .   ? 48.045  -12.836 -39.480 1.00 26.72 ? 490 HOH C O   1 
HETATM 9346 O  O   . HOH R 5 .   ? 39.397  -26.544 -44.465 1.00 28.96 ? 491 HOH C O   1 
HETATM 9347 O  O   . HOH R 5 .   ? 32.457  7.460   -22.415 1.00 32.48 ? 492 HOH C O   1 
HETATM 9348 O  O   . HOH R 5 .   ? 23.538  4.689   -36.062 1.00 11.21 ? 493 HOH C O   1 
HETATM 9349 O  O   . HOH R 5 .   ? 33.901  13.493  -44.080 1.00 19.34 ? 494 HOH C O   1 
HETATM 9350 O  O   . HOH R 5 .   ? 22.636  0.184   -27.937 1.00 23.96 ? 495 HOH C O   1 
HETATM 9351 O  O   . HOH R 5 .   ? 48.059  18.905  -40.585 1.00 35.70 ? 496 HOH C O   1 
HETATM 9352 O  O   . HOH R 5 .   ? 44.017  -5.621  -50.223 1.00 22.60 ? 497 HOH C O   1 
HETATM 9353 O  O   . HOH R 5 .   ? 52.308  12.790  -47.580 1.00 39.10 ? 498 HOH C O   1 
HETATM 9354 O  O   . HOH R 5 .   ? 53.138  -11.359 -36.870 1.00 32.90 ? 499 HOH C O   1 
HETATM 9355 O  O   . HOH R 5 .   ? 22.697  10.903  -29.329 1.00 20.12 ? 500 HOH C O   1 
HETATM 9356 O  O   . HOH R 5 .   ? 26.547  -13.799 -34.712 1.00 23.50 ? 501 HOH C O   1 
HETATM 9357 O  O   . HOH R 5 .   ? 31.711  12.651  -46.490 1.00 23.70 ? 502 HOH C O   1 
HETATM 9358 O  O   . HOH R 5 .   ? 38.396  4.927   -45.148 1.00 18.30 ? 503 HOH C O   1 
HETATM 9359 O  O   . HOH R 5 .   ? 24.355  -0.916  -32.971 1.00 22.39 ? 504 HOH C O   1 
HETATM 9360 O  O   . HOH R 5 .   ? 47.175  7.233   -22.841 1.00 23.00 ? 505 HOH C O   1 
HETATM 9361 O  O   . HOH R 5 .   ? 26.060  12.923  -35.398 1.00 12.17 ? 506 HOH C O   1 
HETATM 9362 O  O   . HOH R 5 .   ? 47.867  -14.115 -29.848 1.00 37.53 ? 507 HOH C O   1 
HETATM 9363 O  O   . HOH R 5 .   ? 34.097  -16.477 -16.688 1.00 42.69 ? 508 HOH C O   1 
HETATM 9364 O  O   . HOH R 5 .   ? 53.076  6.324   -31.369 1.00 20.21 ? 509 HOH C O   1 
HETATM 9365 O  O   . HOH R 5 .   ? 29.315  5.976   -47.396 1.00 18.95 ? 510 HOH C O   1 
HETATM 9366 O  O   . HOH R 5 .   ? 40.039  -12.129 -55.226 1.00 23.19 ? 511 HOH C O   1 
HETATM 9367 O  O   . HOH R 5 .   ? 26.830  9.318   -34.771 1.00 12.25 ? 512 HOH C O   1 
HETATM 9368 O  O   . HOH R 5 .   ? 29.272  9.075   -22.236 1.00 33.34 ? 513 HOH C O   1 
HETATM 9369 O  O   . HOH R 5 .   ? 31.634  2.183   -14.467 1.00 23.42 ? 514 HOH C O   1 
HETATM 9370 O  O   . HOH R 5 .   ? 35.606  -17.159 -14.449 1.00 44.05 ? 515 HOH C O   1 
HETATM 9371 O  O   . HOH R 5 .   ? 30.121  6.486   -21.591 1.00 28.21 ? 516 HOH C O   1 
HETATM 9372 O  O   . HOH R 5 .   ? 34.722  0.216   -9.241  1.00 43.09 ? 517 HOH C O   1 
HETATM 9373 O  O   . HOH R 5 .   ? 37.804  14.249  -28.722 1.00 35.90 ? 518 HOH C O   1 
HETATM 9374 O  O   . HOH R 5 .   ? 30.209  -10.398 -16.377 1.00 31.66 ? 519 HOH C O   1 
HETATM 9375 O  O   . HOH R 5 .   ? 56.446  9.125   -39.977 1.00 30.25 ? 520 HOH C O   1 
HETATM 9376 O  O   . HOH R 5 .   ? 35.884  -1.145  -48.488 1.00 18.49 ? 521 HOH C O   1 
HETATM 9377 O  O   . HOH R 5 .   ? 58.415  -7.207  -30.840 1.00 29.14 ? 522 HOH C O   1 
HETATM 9378 O  O   . HOH R 5 .   ? 26.272  6.889   -41.363 1.00 11.25 ? 523 HOH C O   1 
HETATM 9379 O  O   . HOH R 5 .   ? 46.794  -0.564  -47.262 1.00 34.41 ? 524 HOH C O   1 
HETATM 9380 O  O   . HOH R 5 .   ? 23.909  5.580   -40.690 1.00 14.77 ? 525 HOH C O   1 
HETATM 9381 O  O   . HOH R 5 .   ? 42.337  -4.032  -48.459 1.00 23.27 ? 526 HOH C O   1 
HETATM 9382 O  O   . HOH R 5 .   ? 53.063  8.545   -23.832 1.00 28.26 ? 527 HOH C O   1 
HETATM 9383 O  O   . HOH R 5 .   ? 51.460  7.319   -28.543 1.00 22.24 ? 528 HOH C O   1 
HETATM 9384 O  O   . HOH R 5 .   ? 32.117  2.339   -43.704 1.00 17.66 ? 529 HOH C O   1 
HETATM 9385 O  O   . HOH R 5 .   ? 28.807  3.642   -46.299 1.00 21.66 ? 530 HOH C O   1 
HETATM 9386 O  O   . HOH R 5 .   ? 47.213  8.859   -29.819 1.00 23.09 ? 531 HOH C O   1 
HETATM 9387 O  O   . HOH R 5 .   ? 24.833  -1.960  -23.621 1.00 29.95 ? 532 HOH C O   1 
HETATM 9388 O  O   . HOH R 5 .   ? 43.770  -13.229 -25.996 1.00 27.67 ? 533 HOH C O   1 
HETATM 9389 O  O   . HOH R 5 .   ? 51.771  9.991   -33.316 1.00 23.17 ? 534 HOH C O   1 
HETATM 9390 O  O   . HOH R 5 .   ? 26.581  9.649   -41.779 1.00 16.96 ? 535 HOH C O   1 
HETATM 9391 O  O   . HOH R 5 .   ? 28.717  -0.368  -14.452 1.00 26.48 ? 536 HOH C O   1 
HETATM 9392 O  O   . HOH R 5 .   ? 24.423  -3.754  -44.794 1.00 27.08 ? 537 HOH C O   1 
HETATM 9393 O  O   . HOH R 5 .   ? 49.796  12.176  -32.871 1.00 24.81 ? 538 HOH C O   1 
HETATM 9394 O  O   . HOH R 5 .   ? 39.711  17.913  -40.960 1.00 26.05 ? 539 HOH C O   1 
HETATM 9395 O  O   . HOH R 5 .   ? 38.920  13.748  -42.836 1.00 23.61 ? 540 HOH C O   1 
HETATM 9396 O  O   . HOH R 5 .   ? 29.673  -12.797 -24.134 1.00 25.17 ? 541 HOH C O   1 
HETATM 9397 O  O   . HOH R 5 .   ? 26.639  11.307  -45.612 1.00 28.43 ? 542 HOH C O   1 
HETATM 9398 O  O   . HOH R 5 .   ? 32.131  -2.024  -51.782 1.00 32.34 ? 543 HOH C O   1 
HETATM 9399 O  O   . HOH R 5 .   ? 44.405  14.069  -47.535 1.00 34.55 ? 544 HOH C O   1 
HETATM 9400 O  O   . HOH R 5 .   ? 42.942  -14.327 -48.625 1.00 36.02 ? 545 HOH C O   1 
HETATM 9401 O  O   . HOH R 5 .   ? 23.895  -9.324  -29.020 1.00 29.57 ? 546 HOH C O   1 
HETATM 9402 O  O   . HOH R 5 .   ? 53.671  5.835   -23.299 1.00 23.08 ? 547 HOH C O   1 
HETATM 9403 O  O   . HOH R 5 .   ? 40.394  -1.510  -48.615 1.00 31.06 ? 548 HOH C O   1 
HETATM 9404 O  O   . HOH R 5 .   ? 32.808  0.603   -50.987 1.00 34.66 ? 549 HOH C O   1 
HETATM 9405 O  O   . HOH R 5 .   ? 28.215  6.691   -43.831 1.00 17.40 ? 550 HOH C O   1 
HETATM 9406 O  O   . HOH R 5 .   ? 22.317  -14.099 -35.845 1.00 41.55 ? 551 HOH C O   1 
HETATM 9407 O  O   . HOH R 5 .   ? 44.482  9.225   -29.005 1.00 31.56 ? 552 HOH C O   1 
HETATM 9408 O  O   . HOH R 5 .   ? 40.740  -16.599 -22.399 1.00 30.54 ? 553 HOH C O   1 
HETATM 9409 O  O   . HOH R 5 .   ? 46.571  -17.023 -38.463 1.00 30.25 ? 554 HOH C O   1 
HETATM 9410 O  O   . HOH R 5 .   ? 38.707  16.692  -38.828 1.00 22.16 ? 555 HOH C O   1 
HETATM 9411 O  O   . HOH R 5 .   ? 22.346  -0.445  -44.273 1.00 24.19 ? 556 HOH C O   1 
HETATM 9412 O  O   . HOH R 5 .   ? 44.491  -15.199 -50.263 1.00 33.91 ? 557 HOH C O   1 
HETATM 9413 O  O   . HOH R 5 .   ? 49.645  12.080  -48.481 1.00 29.55 ? 558 HOH C O   1 
HETATM 9414 O  O   . HOH R 5 .   ? 42.880  16.977  -44.768 1.00 32.05 ? 559 HOH C O   1 
HETATM 9415 O  O   . HOH R 5 .   ? 40.600  -14.064 -36.267 1.00 23.05 ? 560 HOH C O   1 
HETATM 9416 O  O   . HOH R 5 .   ? 53.839  6.866   -27.771 1.00 25.50 ? 561 HOH C O   1 
HETATM 9417 O  O   . HOH R 5 .   ? 22.906  1.718   -18.893 1.00 27.80 ? 562 HOH C O   1 
HETATM 9418 O  O   . HOH R 5 .   ? 40.821  4.002   -6.683  1.00 26.09 ? 563 HOH C O   1 
HETATM 9419 O  O   . HOH R 5 .   ? 29.593  -11.974 -26.705 1.00 20.02 ? 564 HOH C O   1 
HETATM 9420 O  O   . HOH R 5 .   ? 21.067  -1.165  -30.014 1.00 23.04 ? 565 HOH C O   1 
HETATM 9421 O  O   . HOH R 5 .   ? 21.320  -0.692  -21.540 1.00 29.88 ? 566 HOH C O   1 
HETATM 9422 O  O   . HOH R 5 .   ? 34.818  20.524  -30.880 1.00 38.80 ? 567 HOH C O   1 
HETATM 9423 O  O   . HOH R 5 .   ? 48.826  11.202  -23.999 1.00 33.34 ? 568 HOH C O   1 
HETATM 9424 O  O   . HOH R 5 .   ? 34.759  -8.129  -11.051 1.00 27.30 ? 569 HOH C O   1 
HETATM 9425 O  O   . HOH R 5 .   ? 43.365  11.748  -29.876 1.00 31.51 ? 570 HOH C O   1 
HETATM 9426 O  O   . HOH R 5 .   ? 31.644  -15.805 -19.491 1.00 36.51 ? 571 HOH C O   1 
HETATM 9427 O  O   . HOH R 5 .   ? 30.527  15.419  -43.973 1.00 30.38 ? 572 HOH C O   1 
HETATM 9428 O  O   . HOH R 5 .   ? 26.570  8.337   -45.421 1.00 32.12 ? 573 HOH C O   1 
HETATM 9429 O  O   . HOH R 5 .   ? 39.521  -5.060  -49.516 1.00 31.25 ? 574 HOH C O   1 
HETATM 9430 O  O   . HOH R 5 .   ? 43.992  14.582  -33.859 1.00 41.06 ? 575 HOH C O   1 
HETATM 9431 O  O   . HOH R 5 .   ? 29.467  -12.586 -40.898 1.00 37.11 ? 576 HOH C O   1 
HETATM 9432 O  O   . HOH R 5 .   ? 27.952  2.549   -52.189 1.00 30.63 ? 577 HOH C O   1 
HETATM 9433 O  O   . HOH R 5 .   ? 31.790  9.763   -23.021 1.00 32.14 ? 578 HOH C O   1 
HETATM 9434 O  O   . HOH R 5 .   ? 56.143  11.779  -42.676 1.00 37.98 ? 579 HOH C O   1 
HETATM 9435 O  O   . HOH R 5 .   ? 26.957  11.801  -5.810  1.00 37.28 ? 580 HOH C O   1 
HETATM 9436 O  O   . HOH R 5 .   ? 54.733  -2.035  -44.854 1.00 32.67 ? 581 HOH C O   1 
HETATM 9437 O  O   . HOH R 5 .   ? 24.856  4.885   -45.858 1.00 38.51 ? 582 HOH C O   1 
HETATM 9438 O  O   . HOH R 5 .   ? 32.017  -21.249 -48.174 1.00 33.79 ? 583 HOH C O   1 
HETATM 9439 O  O   . HOH R 5 .   ? 32.634  4.331   -10.817 1.00 41.54 ? 584 HOH C O   1 
HETATM 9440 O  O   . HOH R 5 .   ? 42.844  -5.786  -54.360 1.00 23.42 ? 585 HOH C O   1 
HETATM 9441 O  O   . HOH R 5 .   ? 27.818  -13.009 -29.961 1.00 33.53 ? 586 HOH C O   1 
HETATM 9442 O  O   . HOH R 5 .   ? 20.654  1.213   -46.135 1.00 32.51 ? 587 HOH C O   1 
HETATM 9443 O  O   . HOH R 5 .   ? 54.230  5.072   -26.079 1.00 29.11 ? 588 HOH C O   1 
HETATM 9444 O  O   . HOH R 5 .   ? 20.491  4.527   -51.937 1.00 39.18 ? 589 HOH C O   1 
HETATM 9445 O  O   . HOH R 5 .   ? 39.579  12.684  -26.347 1.00 37.20 ? 590 HOH C O   1 
HETATM 9446 O  O   . HOH R 5 .   ? 41.627  14.303  -34.231 1.00 38.80 ? 591 HOH C O   1 
HETATM 9447 O  O   . HOH R 5 .   ? 31.026  -12.503 -12.500 1.00 40.97 ? 592 HOH C O   1 
HETATM 9448 O  O   . HOH R 5 .   ? 48.796  -15.275 -39.746 1.00 35.30 ? 593 HOH C O   1 
HETATM 9449 O  O   . HOH R 5 .   ? 23.187  -4.201  -47.896 1.00 35.11 ? 594 HOH C O   1 
HETATM 9450 O  O   . HOH R 5 .   ? 48.140  11.533  -30.406 1.00 29.18 ? 595 HOH C O   1 
HETATM 9451 O  O   . HOH R 5 .   ? 43.344  -17.182 -22.628 1.00 40.05 ? 596 HOH C O   1 
HETATM 9452 O  O   . HOH R 5 .   ? 65.143  -5.297  -15.570 1.00 33.67 ? 597 HOH C O   1 
HETATM 9453 O  O   . HOH R 5 .   ? 28.407  15.241  -45.525 1.00 28.59 ? 598 HOH C O   1 
HETATM 9454 O  O   . HOH R 5 .   ? 51.010  -14.327 -29.436 1.00 41.96 ? 599 HOH C O   1 
HETATM 9455 O  O   . HOH R 5 .   ? 39.161  -11.349 -12.736 1.00 42.45 ? 600 HOH C O   1 
HETATM 9456 O  O   . HOH R 5 .   ? 48.345  11.591  -26.909 1.00 37.00 ? 601 HOH C O   1 
HETATM 9457 O  O   . HOH R 5 .   ? 22.737  8.445   -27.816 1.00 18.13 ? 602 HOH C O   1 
HETATM 9458 O  O   . HOH R 5 .   ? 25.892  -11.082 -16.996 1.00 40.08 ? 603 HOH C O   1 
HETATM 9459 O  O   . HOH R 5 .   ? 29.271  -10.776 -13.544 1.00 35.87 ? 604 HOH C O   1 
HETATM 9460 O  O   . HOH R 5 .   ? 21.961  -4.080  -38.091 1.00 22.45 ? 605 HOH C O   1 
HETATM 9461 O  O   . HOH R 5 .   ? 28.514  26.998  -30.548 1.00 25.26 ? 606 HOH C O   1 
HETATM 9462 O  O   . HOH R 5 .   ? 37.233  -8.525  -10.237 1.00 36.69 ? 607 HOH C O   1 
HETATM 9463 O  O   . HOH R 5 .   ? 45.396  -16.140 -45.697 1.00 27.57 ? 608 HOH C O   1 
HETATM 9464 O  O   . HOH R 5 .   ? 32.320  17.169  -44.027 1.00 36.03 ? 609 HOH C O   1 
HETATM 9465 O  O   . HOH R 5 .   ? 21.595  -15.804 -50.366 1.00 36.75 ? 610 HOH C O   1 
HETATM 9466 O  O   . HOH R 5 .   ? 47.127  -12.971 -14.670 1.00 34.00 ? 611 HOH C O   1 
HETATM 9467 O  O   . HOH R 5 .   ? 40.831  16.665  -37.126 1.00 28.86 ? 612 HOH C O   1 
HETATM 9468 O  O   . HOH R 5 .   ? 42.082  -10.774 -56.500 1.00 18.66 ? 613 HOH C O   1 
HETATM 9469 O  O   . HOH R 5 .   ? 36.139  17.909  -38.375 1.00 24.24 ? 614 HOH C O   1 
HETATM 9470 O  O   . HOH R 5 .   ? 45.836  -19.253 -39.502 1.00 40.90 ? 615 HOH C O   1 
HETATM 9471 O  O   . HOH R 5 .   ? 30.348  5.964   -49.841 1.00 30.62 ? 616 HOH C O   1 
HETATM 9472 O  O   . HOH R 5 .   ? 34.158  11.728  -47.574 1.00 27.51 ? 617 HOH C O   1 
HETATM 9473 O  O   . HOH R 5 .   ? 49.292  -11.411 -52.591 1.00 25.20 ? 618 HOH C O   1 
HETATM 9474 O  O   . HOH R 5 .   ? 40.481  -14.956 -56.560 1.00 27.49 ? 619 HOH C O   1 
HETATM 9475 O  O   . HOH R 5 .   ? 36.109  13.582  -45.985 1.00 32.97 ? 620 HOH C O   1 
HETATM 9476 O  O   . HOH R 5 .   ? 26.949  6.992   -47.902 1.00 36.27 ? 621 HOH C O   1 
HETATM 9477 O  O   . HOH R 5 .   ? 37.597  18.553  -34.403 1.00 37.42 ? 622 HOH C O   1 
HETATM 9478 O  O   . HOH R 5 .   ? 27.347  7.046   -50.704 1.00 45.60 ? 623 HOH C O   1 
HETATM 9479 O  O   . HOH S 5 .   ? 7.237   6.311   -43.309 1.00 23.16 ? 401 HOH D O   1 
HETATM 9480 O  O   . HOH S 5 .   ? -5.366  -9.966  -34.590 1.00 27.10 ? 402 HOH D O   1 
HETATM 9481 O  O   . HOH S 5 .   ? 3.843   9.474   -42.221 1.00 27.99 ? 403 HOH D O   1 
HETATM 9482 O  O   . HOH S 5 .   ? 4.306   4.666   -45.869 1.00 28.45 ? 404 HOH D O   1 
HETATM 9483 O  O   . HOH S 5 .   ? -10.373 11.618  -26.093 1.00 21.57 ? 405 HOH D O   1 
HETATM 9484 O  O   . HOH S 5 .   ? 0.442   -12.355 -22.842 1.00 35.61 ? 406 HOH D O   1 
HETATM 9485 O  O   . HOH S 5 .   ? 1.476   8.980   -59.378 1.00 28.60 ? 407 HOH D O   1 
HETATM 9486 O  O   . HOH S 5 .   ? 2.414   15.155  -43.853 1.00 34.96 ? 408 HOH D O   1 
HETATM 9487 O  O   . HOH S 5 .   ? 1.525   8.118   -22.787 1.00 31.25 ? 409 HOH D O   1 
HETATM 9488 O  O   . HOH S 5 .   ? -9.570  5.438   -21.695 1.00 36.22 ? 410 HOH D O   1 
HETATM 9489 O  O   . HOH S 5 .   ? 14.462  5.896   -60.290 1.00 30.23 ? 411 HOH D O   1 
HETATM 9490 O  O   . HOH S 5 .   ? 11.677  14.336  -61.364 1.00 29.60 ? 412 HOH D O   1 
HETATM 9491 O  O   . HOH S 5 .   ? 15.521  18.188  -54.444 1.00 33.73 ? 413 HOH D O   1 
HETATM 9492 O  O   . HOH S 5 .   ? 4.135   -0.781  -14.835 1.00 27.75 ? 414 HOH D O   1 
HETATM 9493 O  O   . HOH S 5 .   ? 0.764   -15.398 -36.511 1.00 33.62 ? 415 HOH D O   1 
HETATM 9494 O  O   . HOH S 5 .   ? 17.574  -6.767  -56.258 1.00 30.99 ? 416 HOH D O   1 
HETATM 9495 O  O   . HOH S 5 .   ? 12.737  19.831  -29.441 1.00 29.19 ? 417 HOH D O   1 
HETATM 9496 O  O   . HOH S 5 .   ? -6.042  5.192   -56.361 1.00 25.99 ? 418 HOH D O   1 
HETATM 9497 O  O   . HOH S 5 .   ? -2.798  -10.541 -39.402 1.00 25.54 ? 419 HOH D O   1 
HETATM 9498 O  O   . HOH S 5 .   ? -14.071 7.712   -25.710 1.00 39.83 ? 420 HOH D O   1 
HETATM 9499 O  O   . HOH S 5 .   ? -9.136  16.061  -29.105 1.00 31.88 ? 421 HOH D O   1 
HETATM 9500 O  O   . HOH S 5 .   ? 19.849  11.186  -29.072 1.00 19.47 ? 422 HOH D O   1 
HETATM 9501 O  O   . HOH S 5 .   ? -12.002 10.119  -23.335 1.00 28.29 ? 423 HOH D O   1 
HETATM 9502 O  O   . HOH S 5 .   ? 12.264  6.943   -39.566 1.00 11.81 ? 424 HOH D O   1 
HETATM 9503 O  O   . HOH S 5 .   ? 12.099  -6.915  -52.223 1.00 26.18 ? 425 HOH D O   1 
HETATM 9504 O  O   . HOH S 5 .   ? -1.828  -19.248 -36.161 1.00 37.24 ? 426 HOH D O   1 
HETATM 9505 O  O   . HOH S 5 .   ? -2.075  11.266  -58.306 1.00 33.93 ? 427 HOH D O   1 
HETATM 9506 O  O   . HOH S 5 .   ? 17.365  15.839  -64.371 1.00 33.27 ? 428 HOH D O   1 
HETATM 9507 O  O   . HOH S 5 .   ? -6.537  -2.685  -21.329 1.00 31.14 ? 429 HOH D O   1 
HETATM 9508 O  O   . HOH S 5 .   ? -12.413 -7.707  -41.142 1.00 26.91 ? 430 HOH D O   1 
HETATM 9509 O  O   . HOH S 5 .   ? -5.904  -9.934  -41.725 1.00 33.23 ? 431 HOH D O   1 
HETATM 9510 O  O   . HOH S 5 .   ? 18.593  -0.194  -20.326 1.00 28.29 ? 432 HOH D O   1 
HETATM 9511 O  O   . HOH S 5 .   ? 2.130   -15.328 -29.765 1.00 23.57 ? 433 HOH D O   1 
HETATM 9512 O  O   . HOH S 5 .   ? 19.457  -4.173  -34.237 1.00 23.04 ? 434 HOH D O   1 
HETATM 9513 O  O   . HOH S 5 .   ? 18.683  -13.036 -33.241 1.00 35.40 ? 435 HOH D O   1 
HETATM 9514 O  O   . HOH S 5 .   ? 0.507   -12.634 -37.078 1.00 16.93 ? 436 HOH D O   1 
HETATM 9515 O  O   . HOH S 5 .   ? -14.373 4.771   -37.043 1.00 23.96 ? 437 HOH D O   1 
HETATM 9516 O  O   . HOH S 5 .   ? 18.181  2.851   -56.013 1.00 35.99 ? 438 HOH D O   1 
HETATM 9517 O  O   . HOH S 5 .   ? -4.042  9.970   -57.249 1.00 37.26 ? 439 HOH D O   1 
HETATM 9518 O  O   . HOH S 5 .   ? -7.044  -6.963  -51.572 1.00 21.54 ? 440 HOH D O   1 
HETATM 9519 O  O   . HOH S 5 .   ? 18.113  7.304   -27.179 1.00 18.94 ? 441 HOH D O   1 
HETATM 9520 O  O   . HOH S 5 .   ? 16.477  0.250   -37.527 1.00 11.02 ? 442 HOH D O   1 
HETATM 9521 O  O   . HOH S 5 .   ? 8.740   -10.998 -31.155 1.00 19.37 ? 443 HOH D O   1 
HETATM 9522 O  O   . HOH S 5 .   ? -6.747  11.019  -19.751 1.00 16.81 ? 444 HOH D O   1 
HETATM 9523 O  O   . HOH S 5 .   ? -10.060 15.192  -20.984 1.00 25.79 ? 445 HOH D O   1 
HETATM 9524 O  O   . HOH S 5 .   ? 20.298  21.474  -32.586 1.00 25.55 ? 446 HOH D O   1 
HETATM 9525 O  O   . HOH S 5 .   ? -3.687  -1.770  -17.348 1.00 31.42 ? 447 HOH D O   1 
HETATM 9526 O  O   . HOH S 5 .   ? -12.625 8.749   -55.117 1.00 27.78 ? 448 HOH D O   1 
HETATM 9527 O  O   . HOH S 5 .   ? -1.859  -8.911  -16.811 1.00 23.84 ? 449 HOH D O   1 
HETATM 9528 O  O   . HOH S 5 .   ? -15.257 -2.255  -43.796 1.00 25.04 ? 450 HOH D O   1 
HETATM 9529 O  O   . HOH S 5 .   ? 23.029  6.385   -38.247 1.00 10.60 ? 451 HOH D O   1 
HETATM 9530 O  O   . HOH S 5 .   ? 20.161  8.021   -42.426 1.00 12.25 ? 452 HOH D O   1 
HETATM 9531 O  O   . HOH S 5 .   ? -3.005  11.412  -46.203 1.00 24.85 ? 453 HOH D O   1 
HETATM 9532 O  O   . HOH S 5 .   ? 11.065  13.254  -58.788 1.00 19.28 ? 454 HOH D O   1 
HETATM 9533 O  O   . HOH S 5 .   ? 21.566  -9.960  -26.036 1.00 33.14 ? 455 HOH D O   1 
HETATM 9534 O  O   . HOH S 5 .   ? 20.844  14.024  -47.799 1.00 19.93 ? 456 HOH D O   1 
HETATM 9535 O  O   . HOH S 5 .   ? 2.273   -11.830 -54.353 1.00 17.24 ? 457 HOH D O   1 
HETATM 9536 O  O   . HOH S 5 .   ? 20.617  -7.661  -29.817 1.00 19.57 ? 458 HOH D O   1 
HETATM 9537 O  O   . HOH S 5 .   ? -3.006  -14.774 -49.465 1.00 31.15 ? 459 HOH D O   1 
HETATM 9538 O  O   . HOH S 5 .   ? 8.629   -16.419 -45.315 1.00 24.70 ? 460 HOH D O   1 
HETATM 9539 O  O   . HOH S 5 .   ? -2.484  13.466  -41.861 1.00 33.76 ? 461 HOH D O   1 
HETATM 9540 O  O   . HOH S 5 .   ? 9.561   7.692   -43.574 1.00 17.91 ? 462 HOH D O   1 
HETATM 9541 O  O   . HOH S 5 .   ? -5.645  -5.844  -53.672 1.00 31.98 ? 463 HOH D O   1 
HETATM 9542 O  O   . HOH S 5 .   ? 21.497  5.072   -34.197 1.00 10.68 ? 464 HOH D O   1 
HETATM 9543 O  O   . HOH S 5 .   ? 0.537   -8.153  -18.926 1.00 21.18 ? 465 HOH D O   1 
HETATM 9544 O  O   . HOH S 5 .   ? 11.567  -11.160 -27.644 1.00 34.49 ? 466 HOH D O   1 
HETATM 9545 O  O   . HOH S 5 .   ? 22.968  23.169  -35.601 1.00 15.70 ? 467 HOH D O   1 
HETATM 9546 O  O   . HOH S 5 .   ? 14.213  -8.266  -52.653 1.00 30.87 ? 468 HOH D O   1 
HETATM 9547 O  O   . HOH S 5 .   ? -2.432  -8.810  -41.824 1.00 18.00 ? 469 HOH D O   1 
HETATM 9548 O  O   . HOH S 5 .   ? 20.302  7.357   -35.780 1.00 14.08 ? 470 HOH D O   1 
HETATM 9549 O  O   . HOH S 5 .   ? -12.750 -1.792  -34.127 1.00 18.61 ? 471 HOH D O   1 
HETATM 9550 O  O   . HOH S 5 .   ? 0.761   -11.800 -13.895 1.00 28.85 ? 472 HOH D O   1 
HETATM 9551 O  O   . HOH S 5 .   ? 11.336  17.833  -54.742 1.00 20.43 ? 473 HOH D O   1 
HETATM 9552 O  O   . HOH S 5 .   ? -6.376  -9.092  -37.810 1.00 29.06 ? 474 HOH D O   1 
HETATM 9553 O  O   . HOH S 5 .   ? 4.877   16.176  -57.421 1.00 21.79 ? 475 HOH D O   1 
HETATM 9554 O  O   . HOH S 5 .   ? -12.065 -4.662  -44.597 1.00 23.84 ? 476 HOH D O   1 
HETATM 9555 O  O   . HOH S 5 .   ? -6.092  4.214   -24.416 1.00 19.72 ? 477 HOH D O   1 
HETATM 9556 O  O   . HOH S 5 .   ? 16.653  15.988  -54.694 1.00 23.72 ? 478 HOH D O   1 
HETATM 9557 O  O   . HOH S 5 .   ? -10.553 19.229  -30.997 1.00 24.68 ? 479 HOH D O   1 
HETATM 9558 O  O   . HOH S 5 .   ? 4.417   -7.040  -34.872 1.00 11.75 ? 480 HOH D O   1 
HETATM 9559 O  O   . HOH S 5 .   ? 13.576  18.488  -32.493 1.00 15.82 ? 481 HOH D O   1 
HETATM 9560 O  O   . HOH S 5 .   ? 18.704  5.028   -45.667 1.00 21.97 ? 482 HOH D O   1 
HETATM 9561 O  O   . HOH S 5 .   ? 19.142  4.864   -49.456 1.00 20.83 ? 483 HOH D O   1 
HETATM 9562 O  O   . HOH S 5 .   ? 11.991  -3.637  -47.378 1.00 14.04 ? 484 HOH D O   1 
HETATM 9563 O  O   . HOH S 5 .   ? 16.547  15.014  -24.129 1.00 29.77 ? 485 HOH D O   1 
HETATM 9564 O  O   . HOH S 5 .   ? 19.214  11.574  -50.243 1.00 18.25 ? 486 HOH D O   1 
HETATM 9565 O  O   . HOH S 5 .   ? -12.397 -4.479  -47.589 1.00 27.38 ? 487 HOH D O   1 
HETATM 9566 O  O   . HOH S 5 .   ? 6.164   17.719  -33.476 1.00 28.88 ? 488 HOH D O   1 
HETATM 9567 O  O   . HOH S 5 .   ? 1.227   2.590   -28.254 1.00 12.11 ? 489 HOH D O   1 
HETATM 9568 O  O   . HOH S 5 .   ? 9.083   -10.167 -58.179 1.00 22.35 ? 490 HOH D O   1 
HETATM 9569 O  O   . HOH S 5 .   ? 2.329   -1.004  -54.391 1.00 33.65 ? 491 HOH D O   1 
HETATM 9570 O  O   . HOH S 5 .   ? 18.834  -3.368  -43.283 1.00 25.47 ? 492 HOH D O   1 
HETATM 9571 O  O   . HOH S 5 .   ? -13.708 -1.329  -49.243 1.00 27.33 ? 493 HOH D O   1 
HETATM 9572 O  O   . HOH S 5 .   ? 16.854  19.630  -57.154 1.00 35.96 ? 494 HOH D O   1 
HETATM 9573 O  O   . HOH S 5 .   ? 9.322   3.277   -53.065 1.00 14.21 ? 495 HOH D O   1 
HETATM 9574 O  O   . HOH S 5 .   ? 19.411  8.401   -29.247 1.00 13.22 ? 496 HOH D O   1 
HETATM 9575 O  O   . HOH S 5 .   ? -12.241 -3.877  -36.140 1.00 26.95 ? 497 HOH D O   1 
HETATM 9576 O  O   . HOH S 5 .   ? 13.512  22.557  -34.958 1.00 29.28 ? 498 HOH D O   1 
HETATM 9577 O  O   . HOH S 5 .   ? -2.309  -14.366 -26.020 1.00 30.05 ? 499 HOH D O   1 
HETATM 9578 O  O   . HOH S 5 .   ? -5.789  -10.363 -45.436 1.00 29.45 ? 500 HOH D O   1 
HETATM 9579 O  O   . HOH S 5 .   ? -6.095  13.639  -36.994 1.00 26.88 ? 501 HOH D O   1 
HETATM 9580 O  O   . HOH S 5 .   ? -6.796  -3.213  -53.587 1.00 28.12 ? 502 HOH D O   1 
HETATM 9581 O  O   . HOH S 5 .   ? 23.783  8.463   -45.396 1.00 28.14 ? 503 HOH D O   1 
HETATM 9582 O  O   . HOH S 5 .   ? 21.182  2.098   -21.274 1.00 26.79 ? 504 HOH D O   1 
HETATM 9583 O  O   . HOH S 5 .   ? -5.624  -7.013  -27.854 1.00 21.01 ? 505 HOH D O   1 
HETATM 9584 O  O   . HOH S 5 .   ? -3.408  -5.694  -26.870 1.00 19.74 ? 506 HOH D O   1 
HETATM 9585 O  O   . HOH S 5 .   ? 19.607  18.914  -40.053 1.00 27.24 ? 507 HOH D O   1 
HETATM 9586 O  O   . HOH S 5 .   ? -2.209  11.500  -20.157 1.00 26.15 ? 508 HOH D O   1 
HETATM 9587 O  O   . HOH S 5 .   ? 8.099   9.076   -24.392 1.00 19.26 ? 509 HOH D O   1 
HETATM 9588 O  O   . HOH S 5 .   ? 16.745  8.261   -51.585 1.00 21.18 ? 510 HOH D O   1 
HETATM 9589 O  O   . HOH S 5 .   ? 18.589  -0.333  -29.387 1.00 15.93 ? 511 HOH D O   1 
HETATM 9590 O  O   . HOH S 5 .   ? -5.347  -13.699 -32.549 1.00 24.55 ? 512 HOH D O   1 
HETATM 9591 O  O   . HOH S 5 .   ? 9.722   -13.268 -55.760 1.00 33.77 ? 513 HOH D O   1 
HETATM 9592 O  O   . HOH S 5 .   ? 17.099  6.733   -49.117 1.00 20.06 ? 514 HOH D O   1 
HETATM 9593 O  O   . HOH S 5 .   ? 23.994  18.438  -42.763 1.00 21.55 ? 515 HOH D O   1 
HETATM 9594 O  O   . HOH S 5 .   ? 8.558   -9.155  -14.012 1.00 26.91 ? 516 HOH D O   1 
HETATM 9595 O  O   . HOH S 5 .   ? 26.534  16.091  -43.616 1.00 26.59 ? 517 HOH D O   1 
HETATM 9596 O  O   . HOH S 5 .   ? -9.824  8.331   -20.698 1.00 23.81 ? 518 HOH D O   1 
HETATM 9597 O  O   . HOH S 5 .   ? -8.018  3.595   -21.374 1.00 30.92 ? 519 HOH D O   1 
HETATM 9598 O  O   . HOH S 5 .   ? 9.359   19.984  -31.829 1.00 21.95 ? 520 HOH D O   1 
HETATM 9599 O  O   . HOH S 5 .   ? 18.568  22.929  -34.203 1.00 21.45 ? 521 HOH D O   1 
HETATM 9600 O  O   . HOH S 5 .   ? 5.595   12.175  -23.044 1.00 20.15 ? 522 HOH D O   1 
HETATM 9601 O  O   . HOH S 5 .   ? 14.489  -12.052 -34.516 1.00 34.46 ? 523 HOH D O   1 
HETATM 9602 O  O   . HOH S 5 .   ? -7.876  12.017  -36.909 1.00 20.71 ? 524 HOH D O   1 
HETATM 9603 O  O   . HOH S 5 .   ? 14.589  13.784  -27.376 1.00 16.40 ? 525 HOH D O   1 
HETATM 9604 O  O   . HOH S 5 .   ? -0.072  -10.581 -18.659 1.00 34.65 ? 526 HOH D O   1 
HETATM 9605 O  O   . HOH S 5 .   ? 19.219  16.594  -41.739 1.00 25.73 ? 527 HOH D O   1 
HETATM 9606 O  O   . HOH S 5 .   ? 17.196  7.523   -55.649 1.00 21.37 ? 528 HOH D O   1 
HETATM 9607 O  O   . HOH S 5 .   ? 17.552  -11.614 -27.403 1.00 23.04 ? 529 HOH D O   1 
HETATM 9608 O  O   . HOH S 5 .   ? 14.166  -11.349 -20.671 1.00 39.79 ? 530 HOH D O   1 
HETATM 9609 O  O   . HOH S 5 .   ? 11.839  9.150   -47.191 1.00 16.42 ? 531 HOH D O   1 
HETATM 9610 O  O   . HOH S 5 .   ? 6.167   -0.257  -58.125 1.00 29.05 ? 532 HOH D O   1 
HETATM 9611 O  O   . HOH S 5 .   ? 7.724   -4.759  -14.571 1.00 25.69 ? 533 HOH D O   1 
HETATM 9612 O  O   . HOH S 5 .   ? 13.811  7.571   -48.296 1.00 13.51 ? 534 HOH D O   1 
HETATM 9613 O  O   . HOH S 5 .   ? 10.923  -0.656  -13.880 1.00 30.80 ? 535 HOH D O   1 
HETATM 9614 O  O   . HOH S 5 .   ? 14.493  17.734  -52.351 1.00 35.38 ? 536 HOH D O   1 
HETATM 9615 O  O   . HOH S 5 .   ? 14.459  2.405   -16.313 1.00 29.62 ? 537 HOH D O   1 
HETATM 9616 O  O   . HOH S 5 .   ? 5.992   -6.455  -57.653 1.00 21.90 ? 538 HOH D O   1 
HETATM 9617 O  O   . HOH S 5 .   ? -2.200  -7.908  -22.597 1.00 18.54 ? 539 HOH D O   1 
HETATM 9618 O  O   . HOH S 5 .   ? 10.370  2.284   -21.449 1.00 17.00 ? 540 HOH D O   1 
HETATM 9619 O  O   . HOH S 5 .   ? -1.899  13.268  -39.330 1.00 24.47 ? 541 HOH D O   1 
HETATM 9620 O  O   . HOH S 5 .   ? -10.506 -4.719  -29.674 1.00 28.12 ? 542 HOH D O   1 
HETATM 9621 O  O   . HOH S 5 .   ? -9.153  11.246  -45.301 1.00 21.77 ? 543 HOH D O   1 
HETATM 9622 O  O   . HOH S 5 .   ? -8.335  -0.225  -51.789 1.00 17.09 ? 544 HOH D O   1 
HETATM 9623 O  O   . HOH S 5 .   ? 1.094   15.605  -59.888 1.00 36.59 ? 545 HOH D O   1 
HETATM 9624 O  O   . HOH S 5 .   ? 4.426   19.114  -51.798 1.00 30.68 ? 546 HOH D O   1 
HETATM 9625 O  O   . HOH S 5 .   ? 1.082   -4.920  -54.565 1.00 20.97 ? 547 HOH D O   1 
HETATM 9626 O  O   . HOH S 5 .   ? 14.842  19.858  -42.794 1.00 33.59 ? 548 HOH D O   1 
HETATM 9627 O  O   . HOH S 5 .   ? 12.791  -9.846  -46.161 1.00 17.00 ? 549 HOH D O   1 
HETATM 9628 O  O   . HOH S 5 .   ? 16.684  10.653  -50.242 1.00 16.88 ? 550 HOH D O   1 
HETATM 9629 O  O   . HOH S 5 .   ? -6.127  -16.876 -36.824 1.00 44.89 ? 551 HOH D O   1 
HETATM 9630 O  O   . HOH S 5 .   ? -9.942  -0.409  -49.575 1.00 17.00 ? 552 HOH D O   1 
HETATM 9631 O  O   . HOH S 5 .   ? 21.413  6.674   -29.696 1.00 14.46 ? 553 HOH D O   1 
HETATM 9632 O  O   . HOH S 5 .   ? 2.707   -0.422  -57.360 1.00 32.76 ? 554 HOH D O   1 
HETATM 9633 O  O   . HOH S 5 .   ? -15.083 -0.596  -35.762 1.00 22.65 ? 555 HOH D O   1 
HETATM 9634 O  O   . HOH S 5 .   ? 19.147  -0.374  -36.851 1.00 19.56 ? 556 HOH D O   1 
HETATM 9635 O  O   . HOH S 5 .   ? -12.198 -4.538  -32.047 1.00 38.16 ? 557 HOH D O   1 
HETATM 9636 O  O   . HOH S 5 .   ? -6.703  0.475   -56.177 1.00 24.16 ? 558 HOH D O   1 
HETATM 9637 O  O   . HOH S 5 .   ? 9.278   17.127  -41.593 1.00 31.27 ? 559 HOH D O   1 
HETATM 9638 O  O   . HOH S 5 .   ? 18.543  16.760  -49.231 1.00 41.13 ? 560 HOH D O   1 
HETATM 9639 O  O   . HOH S 5 .   ? -2.906  22.267  -35.178 1.00 21.68 ? 561 HOH D O   1 
HETATM 9640 O  O   . HOH S 5 .   ? -4.927  -11.234 -28.303 1.00 23.40 ? 562 HOH D O   1 
HETATM 9641 O  O   . HOH S 5 .   ? 19.186  10.016  -35.809 1.00 11.06 ? 563 HOH D O   1 
HETATM 9642 O  O   . HOH S 5 .   ? 15.732  9.815   -48.045 1.00 17.85 ? 564 HOH D O   1 
HETATM 9643 O  O   . HOH S 5 .   ? -20.331 5.833   -51.036 1.00 22.28 ? 565 HOH D O   1 
HETATM 9644 O  O   . HOH S 5 .   ? 2.795   9.331   -24.806 1.00 21.64 ? 566 HOH D O   1 
HETATM 9645 O  O   . HOH S 5 .   ? 1.157   -9.918  -31.278 1.00 14.88 ? 567 HOH D O   1 
HETATM 9646 O  O   . HOH S 5 .   ? 13.832  1.246   -55.832 1.00 22.14 ? 568 HOH D O   1 
HETATM 9647 O  O   . HOH S 5 .   ? 8.726   21.623  -29.655 1.00 20.79 ? 569 HOH D O   1 
HETATM 9648 O  O   . HOH S 5 .   ? -15.519 4.341   -32.055 1.00 39.64 ? 570 HOH D O   1 
HETATM 9649 O  O   . HOH S 5 .   ? -10.017 -1.445  -22.355 1.00 42.12 ? 571 HOH D O   1 
HETATM 9650 O  O   . HOH S 5 .   ? 11.375  3.746   -55.235 1.00 17.66 ? 572 HOH D O   1 
HETATM 9651 O  O   . HOH S 5 .   ? 13.108  13.552  -48.587 1.00 22.03 ? 573 HOH D O   1 
HETATM 9652 O  O   . HOH S 5 .   ? 11.502  19.323  -44.157 1.00 40.68 ? 574 HOH D O   1 
HETATM 9653 O  O   . HOH S 5 .   ? 18.679  -4.659  -18.141 1.00 31.76 ? 575 HOH D O   1 
HETATM 9654 O  O   . HOH S 5 .   ? 22.087  1.201   -25.113 1.00 25.07 ? 576 HOH D O   1 
HETATM 9655 O  O   . HOH S 5 .   ? -12.268 5.527   -53.279 1.00 31.44 ? 577 HOH D O   1 
HETATM 9656 O  O   . HOH S 5 .   ? -16.088 4.304   -40.990 1.00 27.11 ? 578 HOH D O   1 
HETATM 9657 O  O   . HOH S 5 .   ? -1.998  -4.072  -56.044 1.00 34.54 ? 579 HOH D O   1 
HETATM 9658 O  O   . HOH S 5 .   ? -19.869 -0.344  -44.424 1.00 45.48 ? 580 HOH D O   1 
HETATM 9659 O  O   . HOH S 5 .   ? -8.378  18.799  -22.447 1.00 33.86 ? 581 HOH D O   1 
HETATM 9660 O  O   . HOH S 5 .   ? 3.415   -14.166 -17.511 1.00 41.03 ? 582 HOH D O   1 
HETATM 9661 O  O   . HOH S 5 .   ? 10.661  -10.614 -17.049 1.00 26.91 ? 583 HOH D O   1 
HETATM 9662 O  O   . HOH S 5 .   ? 0.015   -12.256 -42.330 1.00 17.95 ? 584 HOH D O   1 
HETATM 9663 O  O   . HOH S 5 .   ? -11.491 12.873  -38.138 1.00 28.64 ? 585 HOH D O   1 
HETATM 9664 O  O   . HOH S 5 .   ? 12.268  1.961   -18.020 1.00 20.73 ? 586 HOH D O   1 
HETATM 9665 O  O   . HOH S 5 .   ? 14.103  16.296  -26.439 1.00 26.01 ? 587 HOH D O   1 
HETATM 9666 O  O   . HOH S 5 .   ? -8.248  8.610   -55.858 1.00 33.15 ? 588 HOH D O   1 
HETATM 9667 O  O   . HOH S 5 .   ? 11.354  -10.548 -43.839 1.00 23.26 ? 589 HOH D O   1 
HETATM 9668 O  O   . HOH S 5 .   ? 18.799  -7.789  -40.215 1.00 24.87 ? 590 HOH D O   1 
HETATM 9669 O  O   . HOH S 5 .   ? -11.188 12.202  -30.982 1.00 33.99 ? 591 HOH D O   1 
HETATM 9670 O  O   . HOH S 5 .   ? -13.615 12.308  -32.554 1.00 45.86 ? 592 HOH D O   1 
HETATM 9671 O  O   . HOH S 5 .   ? -11.709 -7.513  -36.732 1.00 32.91 ? 593 HOH D O   1 
HETATM 9672 O  O   . HOH S 5 .   ? -0.256  -12.800 -45.472 1.00 17.11 ? 594 HOH D O   1 
HETATM 9673 O  O   . HOH S 5 .   ? -2.437  13.756  -56.751 1.00 26.87 ? 595 HOH D O   1 
HETATM 9674 O  O   . HOH S 5 .   ? -16.006 2.988   -38.063 1.00 39.10 ? 596 HOH D O   1 
HETATM 9675 O  O   . HOH S 5 .   ? 13.258  11.482  -46.762 1.00 19.77 ? 597 HOH D O   1 
HETATM 9676 O  O   . HOH S 5 .   ? 8.736   17.661  -27.456 1.00 22.52 ? 598 HOH D O   1 
HETATM 9677 O  O   . HOH S 5 .   ? 15.376  -6.753  -17.689 1.00 42.46 ? 599 HOH D O   1 
HETATM 9678 O  O   . HOH S 5 .   ? -15.695 9.639   -47.291 1.00 25.57 ? 600 HOH D O   1 
HETATM 9679 O  O   . HOH S 5 .   ? -5.624  -11.048 -31.008 1.00 27.86 ? 601 HOH D O   1 
HETATM 9680 O  O   . HOH S 5 .   ? 0.188   0.223   -56.968 1.00 31.22 ? 602 HOH D O   1 
HETATM 9681 O  O   . HOH S 5 .   ? -17.264 8.515   -50.107 1.00 30.85 ? 603 HOH D O   1 
HETATM 9682 O  O   . HOH S 5 .   ? 23.702  10.271  -41.602 1.00 21.31 ? 604 HOH D O   1 
HETATM 9683 O  O   . HOH S 5 .   ? -3.879  9.974   -17.487 1.00 25.48 ? 605 HOH D O   1 
HETATM 9684 O  O   . HOH S 5 .   ? 8.686   -13.704 -29.885 1.00 29.05 ? 606 HOH D O   1 
HETATM 9685 O  O   . HOH S 5 .   ? 19.114  12.855  -58.254 1.00 35.19 ? 607 HOH D O   1 
HETATM 9686 O  O   . HOH S 5 .   ? 2.488   1.169   -20.180 1.00 39.51 ? 608 HOH D O   1 
HETATM 9687 O  O   . HOH S 5 .   ? 22.331  3.445   -23.479 1.00 21.53 ? 609 HOH D O   1 
HETATM 9688 O  O   . HOH S 5 .   ? -9.139  -5.527  -22.818 1.00 41.83 ? 610 HOH D O   1 
HETATM 9689 O  O   . HOH S 5 .   ? 20.828  -4.244  -28.817 1.00 32.82 ? 611 HOH D O   1 
HETATM 9690 O  O   . HOH S 5 .   ? -16.815 4.017   -51.978 1.00 32.08 ? 612 HOH D O   1 
HETATM 9691 O  O   . HOH S 5 .   ? 1.369   -0.213  -12.164 1.00 31.39 ? 613 HOH D O   1 
HETATM 9692 O  O   . HOH S 5 .   ? 10.138  16.261  -48.348 1.00 42.40 ? 614 HOH D O   1 
HETATM 9693 O  O   . HOH S 5 .   ? 17.444  18.752  -42.959 1.00 33.96 ? 615 HOH D O   1 
HETATM 9694 O  O   . HOH S 5 .   ? 0.756   12.994  -40.498 1.00 25.38 ? 616 HOH D O   1 
HETATM 9695 O  O   . HOH S 5 .   ? -2.551  -0.229  -16.837 1.00 27.50 ? 617 HOH D O   1 
HETATM 9696 O  O   . HOH S 5 .   ? 23.690  19.295  -46.915 1.00 31.10 ? 618 HOH D O   1 
HETATM 9697 O  O   . HOH S 5 .   ? 11.417  10.356  -61.466 1.00 40.01 ? 619 HOH D O   1 
HETATM 9698 O  O   . HOH S 5 .   ? 5.294   9.330   -23.818 1.00 23.02 ? 620 HOH D O   1 
HETATM 9699 O  O   . HOH S 5 .   ? 16.434  24.342  -34.142 1.00 26.06 ? 621 HOH D O   1 
HETATM 9700 O  O   . HOH S 5 .   ? 13.924  -11.340 -38.792 1.00 40.14 ? 622 HOH D O   1 
HETATM 9701 O  O   . HOH S 5 .   ? -17.052 -4.158  -36.336 1.00 32.30 ? 623 HOH D O   1 
HETATM 9702 O  O   . HOH S 5 .   ? 17.532  -14.267 -25.944 1.00 40.21 ? 624 HOH D O   1 
HETATM 9703 O  O   . HOH S 5 .   ? 22.681  -1.770  -40.072 1.00 28.23 ? 625 HOH D O   1 
HETATM 9704 O  O   . HOH S 5 .   ? -8.378  19.370  -25.958 1.00 35.71 ? 626 HOH D O   1 
HETATM 9705 O  O   . HOH S 5 .   ? 13.869  -10.845 -27.757 1.00 40.44 ? 627 HOH D O   1 
HETATM 9706 O  O   . HOH S 5 .   ? 27.524  12.956  -47.216 1.00 28.37 ? 628 HOH D O   1 
HETATM 9707 O  O   . HOH S 5 .   ? 10.146  -10.983 -20.426 1.00 36.54 ? 629 HOH D O   1 
HETATM 9708 O  O   . HOH S 5 .   ? 7.351   -4.073  -58.451 1.00 31.66 ? 630 HOH D O   1 
HETATM 9709 O  O   . HOH S 5 .   ? -15.087 6.975   -40.759 1.00 36.11 ? 631 HOH D O   1 
HETATM 9710 O  O   . HOH S 5 .   ? 4.340   17.320  -49.124 1.00 38.36 ? 632 HOH D O   1 
HETATM 9711 O  O   . HOH S 5 .   ? -3.032  -12.234 -45.476 1.00 25.15 ? 633 HOH D O   1 
HETATM 9712 O  O   . HOH S 5 .   ? -15.992 10.270  -54.740 1.00 28.63 ? 634 HOH D O   1 
HETATM 9713 O  O   . HOH S 5 .   ? 20.872  -1.207  -42.119 1.00 25.63 ? 635 HOH D O   1 
HETATM 9714 O  O   . HOH S 5 .   ? -22.053 6.362   -49.144 1.00 26.18 ? 636 HOH D O   1 
HETATM 9715 O  O   . HOH S 5 .   ? -2.663  -14.751 -39.491 1.00 37.00 ? 637 HOH D O   1 
HETATM 9716 O  O   . HOH S 5 .   ? 14.326  -11.610 -47.652 1.00 28.71 ? 638 HOH D O   1 
HETATM 9717 O  O   . HOH S 5 .   ? 20.715  4.161   -46.929 1.00 21.76 ? 639 HOH D O   1 
HETATM 9718 O  O   . HOH S 5 .   ? 23.251  12.159  -50.921 1.00 36.08 ? 640 HOH D O   1 
HETATM 9719 O  O   . HOH S 5 .   ? 1.981   -7.486  -55.784 1.00 23.49 ? 641 HOH D O   1 
HETATM 9720 O  O   . HOH S 5 .   ? 0.801   -3.263  -56.371 1.00 36.24 ? 642 HOH D O   1 
HETATM 9721 O  O   . HOH S 5 .   ? 22.419  -7.703  -27.657 1.00 23.45 ? 643 HOH D O   1 
HETATM 9722 O  O   . HOH S 5 .   ? 12.397  -12.506 -56.718 1.00 26.20 ? 644 HOH D O   1 
HETATM 9723 O  O   . HOH S 5 .   ? 3.490   -6.531  -58.154 1.00 24.36 ? 645 HOH D O   1 
HETATM 9724 O  O   . HOH S 5 .   ? -6.776  -9.445  -27.036 1.00 30.85 ? 646 HOH D O   1 
HETATM 9725 O  O   . HOH S 5 .   ? -3.027  -9.851  -21.055 1.00 29.34 ? 647 HOH D O   1 
HETATM 9726 O  O   . HOH S 5 .   ? 5.256   -2.494  -59.100 1.00 27.02 ? 648 HOH D O   1 
HETATM 9727 O  O   . HOH S 5 .   ? 22.831  7.705   -42.681 1.00 26.35 ? 649 HOH D O   1 
HETATM 9728 O  O   . HOH S 5 .   ? 5.865   18.401  -36.048 1.00 32.45 ? 650 HOH D O   1 
HETATM 9729 O  O   . HOH S 5 .   ? -4.475  -14.548 -46.646 1.00 35.65 ? 651 HOH D O   1 
HETATM 9730 O  O   . HOH S 5 .   ? -3.855  -8.767  -18.788 1.00 24.60 ? 652 HOH D O   1 
HETATM 9731 O  O   . HOH S 5 .   ? 10.031  -11.993 -33.325 1.00 30.03 ? 653 HOH D O   1 
HETATM 9732 O  O   . HOH S 5 .   ? -11.446 -2.699  -49.724 1.00 31.00 ? 654 HOH D O   1 
HETATM 9733 O  O   . HOH S 5 .   ? -8.213  -10.640 -41.889 1.00 37.38 ? 655 HOH D O   1 
HETATM 9734 O  O   . HOH S 5 .   ? 20.970  11.694  -52.415 1.00 30.76 ? 656 HOH D O   1 
HETATM 9735 O  O   . HOH S 5 .   ? 19.850  -5.929  -42.084 1.00 22.81 ? 657 HOH D O   1 
HETATM 9736 O  O   . HOH S 5 .   ? -6.349  -9.123  -53.063 1.00 27.64 ? 658 HOH D O   1 
HETATM 9737 O  O   . HOH S 5 .   ? 7.332   20.483  -33.558 1.00 36.90 ? 659 HOH D O   1 
HETATM 9738 O  O   . HOH S 5 .   ? -2.682  21.929  -25.957 1.00 32.27 ? 660 HOH D O   1 
HETATM 9739 O  O   . HOH S 5 .   ? -4.983  -13.281 -27.206 1.00 36.27 ? 661 HOH D O   1 
HETATM 9740 O  O   . HOH S 5 .   ? 10.750  3.776   -19.258 1.00 21.84 ? 662 HOH D O   1 
HETATM 9741 O  O   . HOH S 5 .   ? -6.571  -12.690 -46.212 1.00 39.46 ? 663 HOH D O   1 
HETATM 9742 O  O   . HOH S 5 .   ? 12.080  20.740  -32.521 1.00 26.26 ? 664 HOH D O   1 
HETATM 9743 O  O   . HOH S 5 .   ? 12.701  -13.905 -31.736 1.00 37.75 ? 665 HOH D O   1 
HETATM 9744 O  O   . HOH S 5 .   ? 18.803  7.710   -53.073 1.00 31.95 ? 666 HOH D O   1 
HETATM 9745 O  O   . HOH S 5 .   ? 5.926   -14.523 -13.531 1.00 53.49 ? 667 HOH D O   1 
HETATM 9746 O  O   . HOH S 5 .   ? 7.102   -8.548  -59.137 1.00 21.20 ? 668 HOH D O   1 
HETATM 9747 O  O   . HOH S 5 .   ? -5.606  -15.281 -29.246 1.00 42.84 ? 669 HOH D O   1 
HETATM 9748 O  O   . HOH S 5 .   ? 27.951  13.161  -49.930 1.00 31.89 ? 670 HOH D O   1 
HETATM 9749 O  O   . HOH S 5 .   ? 11.834  6.024   -19.713 1.00 29.48 ? 671 HOH D O   1 
HETATM 9750 O  O   . HOH S 5 .   ? -6.545  -8.750  -18.390 1.00 27.17 ? 672 HOH D O   1 
HETATM 9751 O  O   . HOH S 5 .   ? -4.771  23.615  -27.120 1.00 34.12 ? 673 HOH D O   1 
HETATM 9752 O  O   . HOH S 5 .   ? -7.962  23.829  -27.871 1.00 30.06 ? 674 HOH D O   1 
HETATM 9753 O  O   . HOH S 5 .   ? 1.304   -19.706 -39.189 1.00 26.28 ? 675 HOH D O   1 
HETATM 9754 O  O   . HOH S 5 .   ? -4.397  -14.064 -41.687 1.00 32.20 ? 676 HOH D O   1 
# 
