data_5LL9
# 
_entry.id   5LL9 
# 
_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   5LL9         pdb_00005ll9 10.2210/pdb5ll9/pdb 
WWPDB D_1200000936 ?            ?                   
# 
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 2024-01-10 
3 'Structure model' 1 2 2024-11-06 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Data collection'        
2 2 'Structure model' 'Database references'    
3 2 'Structure model' 'Derived calculations'   
4 2 'Structure model' 'Refinement description' 
5 3 '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' chem_comp_atom                
2 2 'Structure model' chem_comp_bond                
3 2 'Structure model' database_2                    
4 2 'Structure model' diffrn_radiation_wavelength   
5 2 'Structure model' pdbx_initial_refinement_model 
6 2 'Structure model' struct_conn                   
7 3 'Structure model' pdbx_entry_details            
8 3 'Structure model' pdbx_modification_feature     
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1  2 'Structure model' '_database_2.pdbx_DOI'                
2  2 'Structure model' '_database_2.pdbx_database_accession' 
3  2 'Structure model' '_struct_conn.pdbx_dist_value'        
4  2 'Structure model' '_struct_conn.ptnr1_auth_asym_id'     
5  2 'Structure model' '_struct_conn.ptnr1_auth_comp_id'     
6  2 'Structure model' '_struct_conn.ptnr1_auth_seq_id'      
7  2 'Structure model' '_struct_conn.ptnr1_label_asym_id'    
8  2 'Structure model' '_struct_conn.ptnr1_label_atom_id'    
9  2 'Structure model' '_struct_conn.ptnr1_label_comp_id'    
10 2 'Structure model' '_struct_conn.ptnr1_label_seq_id'     
11 2 'Structure model' '_struct_conn.ptnr2_auth_asym_id'     
12 2 'Structure model' '_struct_conn.ptnr2_auth_comp_id'     
13 2 'Structure model' '_struct_conn.ptnr2_auth_seq_id'      
14 2 'Structure model' '_struct_conn.ptnr2_label_asym_id'    
15 2 'Structure model' '_struct_conn.ptnr2_label_atom_id'    
16 2 'Structure model' '_struct_conn.ptnr2_label_comp_id'    
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        5LL9 
_pdbx_database_status.recvd_initial_deposition_date   2016-07-27 
_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                   DE 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Chemistryselect 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2365-6549 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
'Combinatorial Design of Isoform-Selective N-Alkylated Benzimidazole-Based Inhibitors of Carbonic Anhydrases' 
_citation.year                      2017 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1002/slct.201700531 
_citation.pdbx_database_id_PubMed   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Capkauskaite, E.'   1 ? 
primary 'Linkuviene, V.'     2 ? 
primary 'Smirnov, A.'        3 ? 
primary 'Milinaviciute, G.'  4 ? 
primary 'Timm, D.'           5 ? 
primary 'Kasiliauskaite, A.' 6 ? 
primary 'Manakova, E.'       7 ? 
primary 'Grazulis, S.'       8 ? 
primary 'Matulis, D.'        9 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Carbonic anhydrase 12'                                            29917.318 4    4.2.1.1 ? 
'human carbonic anhydrase XII'                              ? 
2 non-polymer syn 'ZINC ION'                                                         65.409    4    ?       ? 
'4-(1H-benzimidazol-1-ylacetyl)-2-chlorobenzenesulfonamide' ? 
3 non-polymer syn '4-[2-(benzimidazol-1-yl)ethanoyl]-2-chloranyl-benzenesulfonamide' 349.792   4    ?       ? Zn ? 
4 non-polymer syn 1,2-ETHANEDIOL                                                     62.068    11   ?       ? EGL ? 
5 non-polymer syn 'SULFATE ION'                                                      96.063    3    ?       ? SO4 ? 
6 water       nat water                                                              18.015    1211 ?       ? ? ? 
# 
_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 '4-[2-(benzimidazol-1-yl)ethanoyl]-2-chloranyl-benzenesulfonamide' 6YQ 
4 1,2-ETHANEDIOL                                                     EDO 
5 'SULFATE ION'                                                      SO4 
6 water                                                              HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   SER n 
1 3   LYS n 
1 4   TRP n 
1 5   THR n 
1 6   TYR n 
1 7   PHE n 
1 8   GLY n 
1 9   PRO n 
1 10  ASP n 
1 11  GLY n 
1 12  GLU n 
1 13  ASN n 
1 14  SER n 
1 15  TRP n 
1 16  SER n 
1 17  LYS n 
1 18  LYS n 
1 19  TYR n 
1 20  PRO n 
1 21  SER n 
1 22  CYS n 
1 23  GLY n 
1 24  GLY n 
1 25  LEU n 
1 26  LEU n 
1 27  GLN n 
1 28  SER n 
1 29  PRO n 
1 30  ILE n 
1 31  ASP n 
1 32  LEU n 
1 33  HIS n 
1 34  SER n 
1 35  ASP n 
1 36  ILE n 
1 37  LEU n 
1 38  GLN n 
1 39  TYR n 
1 40  ASP n 
1 41  ALA n 
1 42  SER n 
1 43  LEU n 
1 44  THR n 
1 45  PRO n 
1 46  LEU n 
1 47  GLU n 
1 48  PHE n 
1 49  GLN n 
1 50  GLY n 
1 51  TYR n 
1 52  ASN n 
1 53  LEU n 
1 54  SER n 
1 55  ALA n 
1 56  ASN n 
1 57  LYS n 
1 58  GLN n 
1 59  PHE n 
1 60  LEU n 
1 61  LEU n 
1 62  THR n 
1 63  ASN n 
1 64  ASN n 
1 65  GLY n 
1 66  HIS n 
1 67  SER n 
1 68  VAL n 
1 69  LYS n 
1 70  LEU n 
1 71  ASN n 
1 72  LEU n 
1 73  PRO n 
1 74  SER n 
1 75  ASP n 
1 76  MET n 
1 77  HIS n 
1 78  ILE n 
1 79  GLN n 
1 80  GLY n 
1 81  LEU n 
1 82  GLN n 
1 83  SER n 
1 84  ARG n 
1 85  TYR n 
1 86  SER n 
1 87  ALA n 
1 88  THR n 
1 89  GLN n 
1 90  LEU n 
1 91  HIS n 
1 92  LEU n 
1 93  HIS n 
1 94  TRP n 
1 95  GLY n 
1 96  ASN n 
1 97  PRO n 
1 98  ASN n 
1 99  ASP n 
1 100 PRO n 
1 101 HIS n 
1 102 GLY n 
1 103 SER n 
1 104 GLU n 
1 105 HIS n 
1 106 THR n 
1 107 VAL n 
1 108 SER n 
1 109 GLY n 
1 110 GLN n 
1 111 HIS n 
1 112 PHE n 
1 113 ALA n 
1 114 ALA n 
1 115 GLU n 
1 116 LEU n 
1 117 HIS n 
1 118 ILE n 
1 119 VAL n 
1 120 HIS n 
1 121 TYR n 
1 122 ASN n 
1 123 SER n 
1 124 ASP n 
1 125 LEU n 
1 126 TYR n 
1 127 PRO n 
1 128 ASP n 
1 129 ALA n 
1 130 SER n 
1 131 THR n 
1 132 ALA n 
1 133 SER n 
1 134 ASN n 
1 135 LYS n 
1 136 SER n 
1 137 GLU n 
1 138 GLY n 
1 139 LEU n 
1 140 ALA n 
1 141 VAL n 
1 142 LEU n 
1 143 ALA n 
1 144 VAL n 
1 145 LEU n 
1 146 ILE n 
1 147 GLU n 
1 148 MET n 
1 149 GLY n 
1 150 SER n 
1 151 PHE n 
1 152 ASN n 
1 153 PRO n 
1 154 SER n 
1 155 TYR n 
1 156 ASP n 
1 157 LYS n 
1 158 ILE n 
1 159 PHE n 
1 160 SER n 
1 161 HIS n 
1 162 LEU n 
1 163 GLN n 
1 164 HIS n 
1 165 VAL n 
1 166 LYS n 
1 167 TYR n 
1 168 LYS n 
1 169 GLY n 
1 170 GLN n 
1 171 GLU n 
1 172 ALA n 
1 173 PHE n 
1 174 VAL n 
1 175 PRO n 
1 176 GLY n 
1 177 PHE n 
1 178 ASN n 
1 179 ILE n 
1 180 GLU n 
1 181 GLU n 
1 182 LEU n 
1 183 LEU n 
1 184 PRO n 
1 185 GLU n 
1 186 ARG n 
1 187 THR n 
1 188 ALA n 
1 189 GLU n 
1 190 TYR n 
1 191 TYR n 
1 192 ARG n 
1 193 TYR n 
1 194 ARG n 
1 195 GLY n 
1 196 SER n 
1 197 LEU n 
1 198 THR n 
1 199 THR n 
1 200 PRO n 
1 201 PRO n 
1 202 CYS n 
1 203 ASN n 
1 204 PRO n 
1 205 THR n 
1 206 VAL n 
1 207 LEU n 
1 208 TRP n 
1 209 THR n 
1 210 VAL n 
1 211 PHE n 
1 212 ARG n 
1 213 ASN n 
1 214 PRO n 
1 215 VAL n 
1 216 GLN n 
1 217 ILE n 
1 218 SER n 
1 219 GLN n 
1 220 GLU n 
1 221 GLN n 
1 222 LEU n 
1 223 LEU n 
1 224 ALA n 
1 225 LEU n 
1 226 GLU n 
1 227 THR n 
1 228 ALA n 
1 229 LEU n 
1 230 TYR n 
1 231 CYS n 
1 232 THR n 
1 233 HIS n 
1 234 MET n 
1 235 ASP n 
1 236 ASP n 
1 237 PRO n 
1 238 SER n 
1 239 PRO n 
1 240 ARG n 
1 241 GLU n 
1 242 MET n 
1 243 ILE n 
1 244 ASN n 
1 245 ASN n 
1 246 PHE n 
1 247 ARG n 
1 248 GLN n 
1 249 VAL n 
1 250 GLN n 
1 251 LYS n 
1 252 PHE n 
1 253 ASP n 
1 254 GLU n 
1 255 ARG n 
1 256 LEU n 
1 257 VAL n 
1 258 TYR n 
1 259 THR n 
1 260 SER n 
1 261 PHE n 
1 262 SER n 
1 263 GLN n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   263 
_entity_src_gen.gene_src_common_name               Human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 CA12 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_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 
6YQ non-polymer         . '4-[2-(benzimidazol-1-yl)ethanoyl]-2-chloranyl-benzenesulfonamide' ?                 
'C15 H12 Cl N3 O3 S' 349.792 
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 
SO4 non-polymer         . 'SULFATE ION'                                                      ?                 'O4 S -2' 96.063  
THR 'L-peptide linking' y THREONINE                                                          ?                 'C4 H9 N O3' 
119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                                         ?                 'C11 H12 N2 O2' 
204.225 
TYR 'L-peptide linking' y TYROSINE                                                           ?                 'C9 H11 N O3' 
181.189 
VAL 'L-peptide linking' y VALINE                                                             ?                 'C5 H11 N O2' 
117.146 
ZN  non-polymer         . 'ZINC ION'                                                         ?                 'Zn 2' 65.409  
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   SER 2   2   ?   ?   ?   A . n 
A 1 3   LYS 3   3   3   LYS LYS A . n 
A 1 4   TRP 4   4   4   TRP TRP A . n 
A 1 5   THR 5   5   5   THR THR A . n 
A 1 6   TYR 6   6   6   TYR TYR A . n 
A 1 7   PHE 7   7   7   PHE PHE A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   PRO 9   9   9   PRO PRO A . n 
A 1 10  ASP 10  10  10  ASP ASP A . n 
A 1 11  GLY 11  11  11  GLY GLY A . n 
A 1 12  GLU 12  12  12  GLU GLU A . n 
A 1 13  ASN 13  13  13  ASN ASN A . n 
A 1 14  SER 14  14  14  SER SER A . n 
A 1 15  TRP 15  15  15  TRP TRP A . n 
A 1 16  SER 16  16  16  SER SER A . n 
A 1 17  LYS 17  17  17  LYS LYS A . n 
A 1 18  LYS 18  18  18  LYS LYS A . n 
A 1 19  TYR 19  19  19  TYR TYR A . n 
A 1 20  PRO 20  20  20  PRO PRO A . n 
A 1 21  SER 21  21  21  SER SER A . n 
A 1 22  CYS 22  22  22  CYS CYS A . n 
A 1 23  GLY 23  23  23  GLY GLY A . n 
A 1 24  GLY 24  24  24  GLY GLY A . n 
A 1 25  LEU 25  25  25  LEU LEU A . n 
A 1 26  LEU 26  26  26  LEU LEU A . n 
A 1 27  GLN 27  27  27  GLN GLN A . n 
A 1 28  SER 28  28  28  SER SER A . n 
A 1 29  PRO 29  29  29  PRO PRO A . n 
A 1 30  ILE 30  30  30  ILE ILE A . n 
A 1 31  ASP 31  31  31  ASP ASP A . n 
A 1 32  LEU 32  32  32  LEU LEU A . n 
A 1 33  HIS 33  33  33  HIS HIS A . n 
A 1 34  SER 34  34  34  SER SER A . n 
A 1 35  ASP 35  35  35  ASP ASP A . n 
A 1 36  ILE 36  36  36  ILE ILE A . n 
A 1 37  LEU 37  37  37  LEU LEU A . n 
A 1 38  GLN 38  38  38  GLN GLN A . n 
A 1 39  TYR 39  39  39  TYR TYR A . n 
A 1 40  ASP 40  40  40  ASP ASP A . n 
A 1 41  ALA 41  41  41  ALA ALA A . n 
A 1 42  SER 42  42  42  SER SER A . n 
A 1 43  LEU 43  43  43  LEU LEU A . n 
A 1 44  THR 44  44  44  THR THR A . n 
A 1 45  PRO 45  45  45  PRO PRO A . n 
A 1 46  LEU 46  46  46  LEU LEU A . n 
A 1 47  GLU 47  47  47  GLU GLU A . n 
A 1 48  PHE 48  48  48  PHE PHE A . n 
A 1 49  GLN 49  49  49  GLN GLN A . n 
A 1 50  GLY 50  50  50  GLY GLY A . n 
A 1 51  TYR 51  51  51  TYR TYR A . n 
A 1 52  ASN 52  52  52  ASN ASN A . n 
A 1 53  LEU 53  53  53  LEU LEU A . n 
A 1 54  SER 54  54  54  SER SER A . n 
A 1 55  ALA 55  55  55  ALA ALA A . n 
A 1 56  ASN 56  56  56  ASN ASN A . n 
A 1 57  LYS 57  57  57  LYS LYS A . n 
A 1 58  GLN 58  58  58  GLN GLN A . n 
A 1 59  PHE 59  59  59  PHE PHE A . n 
A 1 60  LEU 60  60  60  LEU LEU A . n 
A 1 61  LEU 61  61  61  LEU LEU A . n 
A 1 62  THR 62  62  62  THR THR A . n 
A 1 63  ASN 63  63  63  ASN ASN A . n 
A 1 64  ASN 64  64  64  ASN ASN A . n 
A 1 65  GLY 65  65  65  GLY GLY A . n 
A 1 66  HIS 66  66  66  HIS HIS A . n 
A 1 67  SER 67  67  67  SER SER A . n 
A 1 68  VAL 68  68  68  VAL VAL A . n 
A 1 69  LYS 69  69  69  LYS LYS A . n 
A 1 70  LEU 70  70  70  LEU LEU A . n 
A 1 71  ASN 71  71  71  ASN ASN A . n 
A 1 72  LEU 72  72  72  LEU LEU A . n 
A 1 73  PRO 73  73  73  PRO PRO A . n 
A 1 74  SER 74  74  74  SER SER A . n 
A 1 75  ASP 75  75  75  ASP ASP A . n 
A 1 76  MET 76  76  76  MET MET A . n 
A 1 77  HIS 77  77  77  HIS HIS A . n 
A 1 78  ILE 78  78  78  ILE ILE A . n 
A 1 79  GLN 79  79  79  GLN GLN A . n 
A 1 80  GLY 80  80  80  GLY GLY A . n 
A 1 81  LEU 81  81  81  LEU LEU A . n 
A 1 82  GLN 82  82  82  GLN GLN A . n 
A 1 83  SER 83  83  83  SER SER A . n 
A 1 84  ARG 84  84  84  ARG ARG A . n 
A 1 85  TYR 85  85  85  TYR TYR A . n 
A 1 86  SER 86  86  86  SER SER A . n 
A 1 87  ALA 87  87  87  ALA ALA A . n 
A 1 88  THR 88  88  88  THR THR A . n 
A 1 89  GLN 89  89  89  GLN GLN A . n 
A 1 90  LEU 90  90  90  LEU LEU A . n 
A 1 91  HIS 91  91  91  HIS HIS A . n 
A 1 92  LEU 92  92  92  LEU LEU A . n 
A 1 93  HIS 93  93  93  HIS HIS A . n 
A 1 94  TRP 94  94  94  TRP TRP A . n 
A 1 95  GLY 95  95  95  GLY GLY A . n 
A 1 96  ASN 96  96  96  ASN ASN A . n 
A 1 97  PRO 97  97  97  PRO PRO A . n 
A 1 98  ASN 98  98  98  ASN ASN A . n 
A 1 99  ASP 99  99  99  ASP ASP A . n 
A 1 100 PRO 100 100 100 PRO PRO A . n 
A 1 101 HIS 101 101 101 HIS HIS A . n 
A 1 102 GLY 102 102 102 GLY GLY A . n 
A 1 103 SER 103 103 103 SER SER A . n 
A 1 104 GLU 104 104 104 GLU GLU A . n 
A 1 105 HIS 105 105 105 HIS HIS A . n 
A 1 106 THR 106 106 106 THR THR A . n 
A 1 107 VAL 107 107 107 VAL VAL A . n 
A 1 108 SER 108 108 108 SER SER A . n 
A 1 109 GLY 109 109 109 GLY GLY A . n 
A 1 110 GLN 110 110 110 GLN GLN A . n 
A 1 111 HIS 111 111 111 HIS HIS A . n 
A 1 112 PHE 112 112 112 PHE PHE A . n 
A 1 113 ALA 113 113 113 ALA ALA A . n 
A 1 114 ALA 114 114 114 ALA ALA A . n 
A 1 115 GLU 115 115 115 GLU GLU A . n 
A 1 116 LEU 116 116 116 LEU LEU A . n 
A 1 117 HIS 117 117 117 HIS HIS A . n 
A 1 118 ILE 118 118 118 ILE ILE A . n 
A 1 119 VAL 119 119 119 VAL VAL A . n 
A 1 120 HIS 120 120 120 HIS HIS A . n 
A 1 121 TYR 121 121 121 TYR TYR A . n 
A 1 122 ASN 122 122 122 ASN ASN A . n 
A 1 123 SER 123 123 123 SER SER A . n 
A 1 124 ASP 124 124 124 ASP ASP A . n 
A 1 125 LEU 125 125 125 LEU LEU A . n 
A 1 126 TYR 126 126 126 TYR TYR A . n 
A 1 127 PRO 127 127 127 PRO PRO A . n 
A 1 128 ASP 128 128 128 ASP ASP A . n 
A 1 129 ALA 129 129 129 ALA ALA A . n 
A 1 130 SER 130 130 130 SER SER A . n 
A 1 131 THR 131 131 131 THR THR A . n 
A 1 132 ALA 132 132 132 ALA ALA A . n 
A 1 133 SER 133 133 133 SER SER A . n 
A 1 134 ASN 134 134 134 ASN ASN A . n 
A 1 135 LYS 135 135 135 LYS LYS A . n 
A 1 136 SER 136 136 136 SER SER A . n 
A 1 137 GLU 137 137 137 GLU GLU A . n 
A 1 138 GLY 138 138 138 GLY GLY A . n 
A 1 139 LEU 139 139 139 LEU LEU A . n 
A 1 140 ALA 140 140 140 ALA ALA A . n 
A 1 141 VAL 141 141 141 VAL VAL A . n 
A 1 142 LEU 142 142 142 LEU LEU A . n 
A 1 143 ALA 143 143 143 ALA ALA A . n 
A 1 144 VAL 144 144 144 VAL VAL A . n 
A 1 145 LEU 145 145 145 LEU LEU A . n 
A 1 146 ILE 146 146 146 ILE ILE A . n 
A 1 147 GLU 147 147 147 GLU GLU A . n 
A 1 148 MET 148 148 148 MET MET A . n 
A 1 149 GLY 149 149 149 GLY GLY A . n 
A 1 150 SER 150 150 150 SER SER A . n 
A 1 151 PHE 151 151 151 PHE PHE A . n 
A 1 152 ASN 152 152 152 ASN ASN A . n 
A 1 153 PRO 153 153 153 PRO PRO A . n 
A 1 154 SER 154 154 154 SER SER A . n 
A 1 155 TYR 155 155 155 TYR TYR A . n 
A 1 156 ASP 156 156 156 ASP ASP A . n 
A 1 157 LYS 157 157 157 LYS LYS A . n 
A 1 158 ILE 158 158 158 ILE ILE A . n 
A 1 159 PHE 159 159 159 PHE PHE A . n 
A 1 160 SER 160 160 160 SER SER A . n 
A 1 161 HIS 161 161 161 HIS HIS A . n 
A 1 162 LEU 162 162 162 LEU LEU A . n 
A 1 163 GLN 163 163 163 GLN GLN A . n 
A 1 164 HIS 164 164 164 HIS HIS A . n 
A 1 165 VAL 165 165 165 VAL VAL A . n 
A 1 166 LYS 166 166 166 LYS LYS A . n 
A 1 167 TYR 167 167 167 TYR TYR A . n 
A 1 168 LYS 168 168 168 LYS LYS A . n 
A 1 169 GLY 169 169 169 GLY GLY A . n 
A 1 170 GLN 170 170 170 GLN GLN A . n 
A 1 171 GLU 171 171 171 GLU GLU A . n 
A 1 172 ALA 172 172 172 ALA ALA A . n 
A 1 173 PHE 173 173 173 PHE PHE A . n 
A 1 174 VAL 174 174 174 VAL VAL A . n 
A 1 175 PRO 175 175 175 PRO PRO A . n 
A 1 176 GLY 176 176 176 GLY GLY A . n 
A 1 177 PHE 177 177 177 PHE PHE A . n 
A 1 178 ASN 178 178 178 ASN ASN A . n 
A 1 179 ILE 179 179 179 ILE ILE A . n 
A 1 180 GLU 180 180 180 GLU GLU A . n 
A 1 181 GLU 181 181 181 GLU GLU A . n 
A 1 182 LEU 182 182 182 LEU LEU A . n 
A 1 183 LEU 183 183 183 LEU LEU A . n 
A 1 184 PRO 184 184 184 PRO PRO A . n 
A 1 185 GLU 185 185 185 GLU GLU A . n 
A 1 186 ARG 186 186 186 ARG ARG A . n 
A 1 187 THR 187 187 187 THR THR A . n 
A 1 188 ALA 188 188 188 ALA ALA A . n 
A 1 189 GLU 189 189 189 GLU GLU A . n 
A 1 190 TYR 190 190 190 TYR TYR A . n 
A 1 191 TYR 191 191 191 TYR TYR A . n 
A 1 192 ARG 192 192 192 ARG ARG A . n 
A 1 193 TYR 193 193 193 TYR TYR A . n 
A 1 194 ARG 194 194 194 ARG ARG A . n 
A 1 195 GLY 195 195 195 GLY GLY A . n 
A 1 196 SER 196 196 196 SER SER A . n 
A 1 197 LEU 197 197 197 LEU LEU A . n 
A 1 198 THR 198 198 198 THR THR A . n 
A 1 199 THR 199 199 199 THR THR A . n 
A 1 200 PRO 200 200 200 PRO PRO A . n 
A 1 201 PRO 201 201 201 PRO PRO A . n 
A 1 202 CYS 202 202 202 CYS CYS A . n 
A 1 203 ASN 203 203 203 ASN ASN A . n 
A 1 204 PRO 204 204 204 PRO PRO A . n 
A 1 205 THR 205 205 205 THR THR A . n 
A 1 206 VAL 206 206 206 VAL VAL A . n 
A 1 207 LEU 207 207 207 LEU LEU A . n 
A 1 208 TRP 208 208 208 TRP TRP A . n 
A 1 209 THR 209 209 209 THR THR A . n 
A 1 210 VAL 210 210 210 VAL VAL A . n 
A 1 211 PHE 211 211 211 PHE PHE A . n 
A 1 212 ARG 212 212 212 ARG ARG A . n 
A 1 213 ASN 213 213 213 ASN ASN A . n 
A 1 214 PRO 214 214 214 PRO PRO A . n 
A 1 215 VAL 215 215 215 VAL VAL A . n 
A 1 216 GLN 216 216 216 GLN GLN A . n 
A 1 217 ILE 217 217 217 ILE ILE A . n 
A 1 218 SER 218 218 218 SER SER A . n 
A 1 219 GLN 219 219 219 GLN GLN A . n 
A 1 220 GLU 220 220 220 GLU GLU A . n 
A 1 221 GLN 221 221 221 GLN GLN A . n 
A 1 222 LEU 222 222 222 LEU LEU A . n 
A 1 223 LEU 223 223 223 LEU LEU A . n 
A 1 224 ALA 224 224 224 ALA ALA A . n 
A 1 225 LEU 225 225 225 LEU LEU A . n 
A 1 226 GLU 226 226 226 GLU GLU A . n 
A 1 227 THR 227 227 227 THR THR A . n 
A 1 228 ALA 228 228 228 ALA ALA A . n 
A 1 229 LEU 229 229 229 LEU LEU A . n 
A 1 230 TYR 230 230 230 TYR TYR A . n 
A 1 231 CYS 231 231 231 CYS CYS A . n 
A 1 232 THR 232 232 232 THR THR A . n 
A 1 233 HIS 233 233 233 HIS HIS A . n 
A 1 234 MET 234 234 234 MET MET A . n 
A 1 235 ASP 235 235 235 ASP ASP A . n 
A 1 236 ASP 236 236 236 ASP ASP A . n 
A 1 237 PRO 237 237 237 PRO PRO A . n 
A 1 238 SER 238 238 238 SER SER A . n 
A 1 239 PRO 239 239 239 PRO PRO A . n 
A 1 240 ARG 240 240 240 ARG ARG A . n 
A 1 241 GLU 241 241 241 GLU GLU A . n 
A 1 242 MET 242 242 242 MET MET A . n 
A 1 243 ILE 243 243 243 ILE ILE A . n 
A 1 244 ASN 244 244 244 ASN ASN A . n 
A 1 245 ASN 245 245 245 ASN ASN A . n 
A 1 246 PHE 246 246 246 PHE PHE A . n 
A 1 247 ARG 247 247 247 ARG ARG A . n 
A 1 248 GLN 248 248 248 GLN GLN A . n 
A 1 249 VAL 249 249 249 VAL VAL A . n 
A 1 250 GLN 250 250 250 GLN GLN A . n 
A 1 251 LYS 251 251 251 LYS LYS A . n 
A 1 252 PHE 252 252 252 PHE PHE A . n 
A 1 253 ASP 253 253 253 ASP ASP A . n 
A 1 254 GLU 254 254 254 GLU GLU A . n 
A 1 255 ARG 255 255 255 ARG ARG A . n 
A 1 256 LEU 256 256 256 LEU LEU A . n 
A 1 257 VAL 257 257 257 VAL VAL A . n 
A 1 258 TYR 258 258 258 TYR TYR A . n 
A 1 259 THR 259 259 259 THR THR A . n 
A 1 260 SER 260 260 260 SER SER A . n 
A 1 261 PHE 261 261 261 PHE PHE A . n 
A 1 262 SER 262 262 262 SER SER A . n 
A 1 263 GLN 263 263 263 GLN GLN A . n 
B 1 1   MET 1   1   ?   ?   ?   B . n 
B 1 2   SER 2   2   ?   ?   ?   B . n 
B 1 3   LYS 3   3   3   LYS LYS B . n 
B 1 4   TRP 4   4   4   TRP TRP B . n 
B 1 5   THR 5   5   5   THR THR B . n 
B 1 6   TYR 6   6   6   TYR TYR B . n 
B 1 7   PHE 7   7   7   PHE PHE B . n 
B 1 8   GLY 8   8   8   GLY GLY B . n 
B 1 9   PRO 9   9   9   PRO PRO B . n 
B 1 10  ASP 10  10  10  ASP ASP B . n 
B 1 11  GLY 11  11  11  GLY GLY B . n 
B 1 12  GLU 12  12  12  GLU GLU B . n 
B 1 13  ASN 13  13  13  ASN ASN B . n 
B 1 14  SER 14  14  14  SER SER B . n 
B 1 15  TRP 15  15  15  TRP TRP B . n 
B 1 16  SER 16  16  16  SER SER B . n 
B 1 17  LYS 17  17  17  LYS LYS B . n 
B 1 18  LYS 18  18  18  LYS LYS B . n 
B 1 19  TYR 19  19  19  TYR TYR B . n 
B 1 20  PRO 20  20  20  PRO PRO B . n 
B 1 21  SER 21  21  21  SER SER B . n 
B 1 22  CYS 22  22  22  CYS CYS B . n 
B 1 23  GLY 23  23  23  GLY GLY B . n 
B 1 24  GLY 24  24  24  GLY GLY B . n 
B 1 25  LEU 25  25  25  LEU LEU B . n 
B 1 26  LEU 26  26  26  LEU LEU B . n 
B 1 27  GLN 27  27  27  GLN GLN B . n 
B 1 28  SER 28  28  28  SER SER B . n 
B 1 29  PRO 29  29  29  PRO PRO B . n 
B 1 30  ILE 30  30  30  ILE ILE B . n 
B 1 31  ASP 31  31  31  ASP ASP B . n 
B 1 32  LEU 32  32  32  LEU LEU B . n 
B 1 33  HIS 33  33  33  HIS HIS B . n 
B 1 34  SER 34  34  34  SER SER B . n 
B 1 35  ASP 35  35  35  ASP ASP B . n 
B 1 36  ILE 36  36  36  ILE ILE B . n 
B 1 37  LEU 37  37  37  LEU LEU B . n 
B 1 38  GLN 38  38  38  GLN GLN B . n 
B 1 39  TYR 39  39  39  TYR TYR B . n 
B 1 40  ASP 40  40  40  ASP ASP B . n 
B 1 41  ALA 41  41  41  ALA ALA B . n 
B 1 42  SER 42  42  42  SER SER B . n 
B 1 43  LEU 43  43  43  LEU LEU B . n 
B 1 44  THR 44  44  44  THR THR B . n 
B 1 45  PRO 45  45  45  PRO PRO B . n 
B 1 46  LEU 46  46  46  LEU LEU B . n 
B 1 47  GLU 47  47  47  GLU GLU B . n 
B 1 48  PHE 48  48  48  PHE PHE B . n 
B 1 49  GLN 49  49  49  GLN GLN B . n 
B 1 50  GLY 50  50  50  GLY GLY B . n 
B 1 51  TYR 51  51  51  TYR TYR B . n 
B 1 52  ASN 52  52  52  ASN ASN B . n 
B 1 53  LEU 53  53  53  LEU LEU B . n 
B 1 54  SER 54  54  54  SER SER B . n 
B 1 55  ALA 55  55  55  ALA ALA B . n 
B 1 56  ASN 56  56  56  ASN ASN B . n 
B 1 57  LYS 57  57  57  LYS LYS B . n 
B 1 58  GLN 58  58  58  GLN GLN B . n 
B 1 59  PHE 59  59  59  PHE PHE B . n 
B 1 60  LEU 60  60  60  LEU LEU B . n 
B 1 61  LEU 61  61  61  LEU LEU B . n 
B 1 62  THR 62  62  62  THR THR B . n 
B 1 63  ASN 63  63  63  ASN ASN B . n 
B 1 64  ASN 64  64  64  ASN ASN B . n 
B 1 65  GLY 65  65  65  GLY GLY B . n 
B 1 66  HIS 66  66  66  HIS HIS B . n 
B 1 67  SER 67  67  67  SER SER B . n 
B 1 68  VAL 68  68  68  VAL VAL B . n 
B 1 69  LYS 69  69  69  LYS LYS B . n 
B 1 70  LEU 70  70  70  LEU LEU B . n 
B 1 71  ASN 71  71  71  ASN ASN B . n 
B 1 72  LEU 72  72  72  LEU LEU B . n 
B 1 73  PRO 73  73  73  PRO PRO B . n 
B 1 74  SER 74  74  74  SER SER B . n 
B 1 75  ASP 75  75  75  ASP ASP B . n 
B 1 76  MET 76  76  76  MET MET B . n 
B 1 77  HIS 77  77  77  HIS HIS B . n 
B 1 78  ILE 78  78  78  ILE ILE B . n 
B 1 79  GLN 79  79  79  GLN GLN B . n 
B 1 80  GLY 80  80  80  GLY GLY B . n 
B 1 81  LEU 81  81  81  LEU LEU B . n 
B 1 82  GLN 82  82  82  GLN GLN B . n 
B 1 83  SER 83  83  83  SER SER B . n 
B 1 84  ARG 84  84  84  ARG ARG B . n 
B 1 85  TYR 85  85  85  TYR TYR B . n 
B 1 86  SER 86  86  86  SER SER B . n 
B 1 87  ALA 87  87  87  ALA ALA B . n 
B 1 88  THR 88  88  88  THR THR B . n 
B 1 89  GLN 89  89  89  GLN GLN B . n 
B 1 90  LEU 90  90  90  LEU LEU B . n 
B 1 91  HIS 91  91  91  HIS HIS B . n 
B 1 92  LEU 92  92  92  LEU LEU B . n 
B 1 93  HIS 93  93  93  HIS HIS B . n 
B 1 94  TRP 94  94  94  TRP TRP B . n 
B 1 95  GLY 95  95  95  GLY GLY B . n 
B 1 96  ASN 96  96  96  ASN ASN B . n 
B 1 97  PRO 97  97  97  PRO PRO B . n 
B 1 98  ASN 98  98  98  ASN ASN B . n 
B 1 99  ASP 99  99  99  ASP ASP B . n 
B 1 100 PRO 100 100 100 PRO PRO B . n 
B 1 101 HIS 101 101 101 HIS HIS B . n 
B 1 102 GLY 102 102 102 GLY GLY B . n 
B 1 103 SER 103 103 103 SER SER B . n 
B 1 104 GLU 104 104 104 GLU GLU B . n 
B 1 105 HIS 105 105 105 HIS HIS B . n 
B 1 106 THR 106 106 106 THR THR B . n 
B 1 107 VAL 107 107 107 VAL VAL B . n 
B 1 108 SER 108 108 108 SER SER B . n 
B 1 109 GLY 109 109 109 GLY GLY B . n 
B 1 110 GLN 110 110 110 GLN GLN B . n 
B 1 111 HIS 111 111 111 HIS HIS B . n 
B 1 112 PHE 112 112 112 PHE PHE B . n 
B 1 113 ALA 113 113 113 ALA ALA B . n 
B 1 114 ALA 114 114 114 ALA ALA B . n 
B 1 115 GLU 115 115 115 GLU GLU B . n 
B 1 116 LEU 116 116 116 LEU LEU B . n 
B 1 117 HIS 117 117 117 HIS HIS B . n 
B 1 118 ILE 118 118 118 ILE ILE B . n 
B 1 119 VAL 119 119 119 VAL VAL B . n 
B 1 120 HIS 120 120 120 HIS HIS B . n 
B 1 121 TYR 121 121 121 TYR TYR B . n 
B 1 122 ASN 122 122 122 ASN ASN B . n 
B 1 123 SER 123 123 123 SER SER B . n 
B 1 124 ASP 124 124 124 ASP ASP B . n 
B 1 125 LEU 125 125 125 LEU LEU B . n 
B 1 126 TYR 126 126 126 TYR TYR B . n 
B 1 127 PRO 127 127 127 PRO PRO B . n 
B 1 128 ASP 128 128 128 ASP ASP B . n 
B 1 129 ALA 129 129 129 ALA ALA B . n 
B 1 130 SER 130 130 130 SER SER B . n 
B 1 131 THR 131 131 131 THR THR B . n 
B 1 132 ALA 132 132 132 ALA ALA B . n 
B 1 133 SER 133 133 133 SER SER B . n 
B 1 134 ASN 134 134 134 ASN ASN B . n 
B 1 135 LYS 135 135 135 LYS LYS B . n 
B 1 136 SER 136 136 136 SER SER B . n 
B 1 137 GLU 137 137 137 GLU GLU B . n 
B 1 138 GLY 138 138 138 GLY GLY B . n 
B 1 139 LEU 139 139 139 LEU LEU B . n 
B 1 140 ALA 140 140 140 ALA ALA B . n 
B 1 141 VAL 141 141 141 VAL VAL B . n 
B 1 142 LEU 142 142 142 LEU LEU B . n 
B 1 143 ALA 143 143 143 ALA ALA B . n 
B 1 144 VAL 144 144 144 VAL VAL B . n 
B 1 145 LEU 145 145 145 LEU LEU B . n 
B 1 146 ILE 146 146 146 ILE ILE B . n 
B 1 147 GLU 147 147 147 GLU GLU B . n 
B 1 148 MET 148 148 148 MET MET B . n 
B 1 149 GLY 149 149 149 GLY GLY B . n 
B 1 150 SER 150 150 150 SER SER B . n 
B 1 151 PHE 151 151 151 PHE PHE B . n 
B 1 152 ASN 152 152 152 ASN ASN B . n 
B 1 153 PRO 153 153 153 PRO PRO B . n 
B 1 154 SER 154 154 154 SER SER B . n 
B 1 155 TYR 155 155 155 TYR TYR B . n 
B 1 156 ASP 156 156 156 ASP ASP B . n 
B 1 157 LYS 157 157 157 LYS LYS B . n 
B 1 158 ILE 158 158 158 ILE ILE B . n 
B 1 159 PHE 159 159 159 PHE PHE B . n 
B 1 160 SER 160 160 160 SER SER B . n 
B 1 161 HIS 161 161 161 HIS HIS B . n 
B 1 162 LEU 162 162 162 LEU LEU B . n 
B 1 163 GLN 163 163 163 GLN GLN B . n 
B 1 164 HIS 164 164 164 HIS HIS B . n 
B 1 165 VAL 165 165 165 VAL VAL B . n 
B 1 166 LYS 166 166 166 LYS LYS B . n 
B 1 167 TYR 167 167 167 TYR TYR B . n 
B 1 168 LYS 168 168 168 LYS LYS B . n 
B 1 169 GLY 169 169 169 GLY GLY B . n 
B 1 170 GLN 170 170 170 GLN GLN B . n 
B 1 171 GLU 171 171 171 GLU GLU B . n 
B 1 172 ALA 172 172 172 ALA ALA B . n 
B 1 173 PHE 173 173 173 PHE PHE B . n 
B 1 174 VAL 174 174 174 VAL VAL B . n 
B 1 175 PRO 175 175 175 PRO PRO B . n 
B 1 176 GLY 176 176 176 GLY GLY B . n 
B 1 177 PHE 177 177 177 PHE PHE B . n 
B 1 178 ASN 178 178 178 ASN ASN B . n 
B 1 179 ILE 179 179 179 ILE ILE B . n 
B 1 180 GLU 180 180 180 GLU GLU B . n 
B 1 181 GLU 181 181 181 GLU GLU B . n 
B 1 182 LEU 182 182 182 LEU LEU B . n 
B 1 183 LEU 183 183 183 LEU LEU B . n 
B 1 184 PRO 184 184 184 PRO PRO B . n 
B 1 185 GLU 185 185 185 GLU GLU B . n 
B 1 186 ARG 186 186 186 ARG ARG B . n 
B 1 187 THR 187 187 187 THR THR B . n 
B 1 188 ALA 188 188 188 ALA ALA B . n 
B 1 189 GLU 189 189 189 GLU GLU B . n 
B 1 190 TYR 190 190 190 TYR TYR B . n 
B 1 191 TYR 191 191 191 TYR TYR B . n 
B 1 192 ARG 192 192 192 ARG ARG B . n 
B 1 193 TYR 193 193 193 TYR TYR B . n 
B 1 194 ARG 194 194 194 ARG ARG B . n 
B 1 195 GLY 195 195 195 GLY GLY B . n 
B 1 196 SER 196 196 196 SER SER B . n 
B 1 197 LEU 197 197 197 LEU LEU B . n 
B 1 198 THR 198 198 198 THR THR B . n 
B 1 199 THR 199 199 199 THR THR B . n 
B 1 200 PRO 200 200 200 PRO PRO B . n 
B 1 201 PRO 201 201 201 PRO PRO B . n 
B 1 202 CYS 202 202 202 CYS CYS B . n 
B 1 203 ASN 203 203 203 ASN ASN B . n 
B 1 204 PRO 204 204 204 PRO PRO B . n 
B 1 205 THR 205 205 205 THR THR B . n 
B 1 206 VAL 206 206 206 VAL VAL B . n 
B 1 207 LEU 207 207 207 LEU LEU B . n 
B 1 208 TRP 208 208 208 TRP TRP B . n 
B 1 209 THR 209 209 209 THR THR B . n 
B 1 210 VAL 210 210 210 VAL VAL B . n 
B 1 211 PHE 211 211 211 PHE PHE B . n 
B 1 212 ARG 212 212 212 ARG ARG B . n 
B 1 213 ASN 213 213 213 ASN ASN B . n 
B 1 214 PRO 214 214 214 PRO PRO B . n 
B 1 215 VAL 215 215 215 VAL VAL B . n 
B 1 216 GLN 216 216 216 GLN GLN B . n 
B 1 217 ILE 217 217 217 ILE ILE B . n 
B 1 218 SER 218 218 218 SER SER B . n 
B 1 219 GLN 219 219 219 GLN GLN B . n 
B 1 220 GLU 220 220 220 GLU GLU B . n 
B 1 221 GLN 221 221 221 GLN GLN B . n 
B 1 222 LEU 222 222 222 LEU LEU B . n 
B 1 223 LEU 223 223 223 LEU LEU B . n 
B 1 224 ALA 224 224 224 ALA ALA B . n 
B 1 225 LEU 225 225 225 LEU LEU B . n 
B 1 226 GLU 226 226 226 GLU GLU B . n 
B 1 227 THR 227 227 227 THR THR B . n 
B 1 228 ALA 228 228 228 ALA ALA B . n 
B 1 229 LEU 229 229 229 LEU LEU B . n 
B 1 230 TYR 230 230 230 TYR TYR B . n 
B 1 231 CYS 231 231 231 CYS CYS B . n 
B 1 232 THR 232 232 232 THR THR B . n 
B 1 233 HIS 233 233 233 HIS HIS B . n 
B 1 234 MET 234 234 234 MET MET B . n 
B 1 235 ASP 235 235 235 ASP ASP B . n 
B 1 236 ASP 236 236 236 ASP ASP B . n 
B 1 237 PRO 237 237 237 PRO PRO B . n 
B 1 238 SER 238 238 238 SER SER B . n 
B 1 239 PRO 239 239 239 PRO PRO B . n 
B 1 240 ARG 240 240 240 ARG ARG B . n 
B 1 241 GLU 241 241 241 GLU GLU B . n 
B 1 242 MET 242 242 242 MET MET B . n 
B 1 243 ILE 243 243 243 ILE ILE B . n 
B 1 244 ASN 244 244 244 ASN ASN B . n 
B 1 245 ASN 245 245 245 ASN ASN B . n 
B 1 246 PHE 246 246 246 PHE PHE B . n 
B 1 247 ARG 247 247 247 ARG ARG B . n 
B 1 248 GLN 248 248 248 GLN GLN B . n 
B 1 249 VAL 249 249 249 VAL VAL B . n 
B 1 250 GLN 250 250 250 GLN GLN B . n 
B 1 251 LYS 251 251 251 LYS LYS B . n 
B 1 252 PHE 252 252 252 PHE PHE B . n 
B 1 253 ASP 253 253 253 ASP ASP B . n 
B 1 254 GLU 254 254 254 GLU GLU B . n 
B 1 255 ARG 255 255 255 ARG ARG B . n 
B 1 256 LEU 256 256 256 LEU LEU B . n 
B 1 257 VAL 257 257 257 VAL VAL B . n 
B 1 258 TYR 258 258 258 TYR TYR B . n 
B 1 259 THR 259 259 259 THR THR B . n 
B 1 260 SER 260 260 260 SER SER B . n 
B 1 261 PHE 261 261 261 PHE PHE B . n 
B 1 262 SER 262 262 262 SER SER B . n 
B 1 263 GLN 263 263 263 GLN GLN B . n 
C 1 1   MET 1   1   ?   ?   ?   C . n 
C 1 2   SER 2   2   ?   ?   ?   C . n 
C 1 3   LYS 3   3   3   LYS LYS C . n 
C 1 4   TRP 4   4   4   TRP TRP C . n 
C 1 5   THR 5   5   5   THR THR C . n 
C 1 6   TYR 6   6   6   TYR TYR C . n 
C 1 7   PHE 7   7   7   PHE PHE C . n 
C 1 8   GLY 8   8   8   GLY GLY C . n 
C 1 9   PRO 9   9   9   PRO PRO C . n 
C 1 10  ASP 10  10  10  ASP ASP C . n 
C 1 11  GLY 11  11  11  GLY GLY C . n 
C 1 12  GLU 12  12  12  GLU GLU C . n 
C 1 13  ASN 13  13  13  ASN ASN C . n 
C 1 14  SER 14  14  14  SER SER C . n 
C 1 15  TRP 15  15  15  TRP TRP C . n 
C 1 16  SER 16  16  16  SER SER C . n 
C 1 17  LYS 17  17  17  LYS LYS C . n 
C 1 18  LYS 18  18  18  LYS LYS C . n 
C 1 19  TYR 19  19  19  TYR TYR C . n 
C 1 20  PRO 20  20  20  PRO PRO C . n 
C 1 21  SER 21  21  21  SER SER C . n 
C 1 22  CYS 22  22  22  CYS CYS C . n 
C 1 23  GLY 23  23  23  GLY GLY C . n 
C 1 24  GLY 24  24  24  GLY GLY C . n 
C 1 25  LEU 25  25  25  LEU LEU C . n 
C 1 26  LEU 26  26  26  LEU LEU C . n 
C 1 27  GLN 27  27  27  GLN GLN C . n 
C 1 28  SER 28  28  28  SER SER C . n 
C 1 29  PRO 29  29  29  PRO PRO C . n 
C 1 30  ILE 30  30  30  ILE ILE C . n 
C 1 31  ASP 31  31  31  ASP ASP C . n 
C 1 32  LEU 32  32  32  LEU LEU C . n 
C 1 33  HIS 33  33  33  HIS HIS C . n 
C 1 34  SER 34  34  34  SER SER C . n 
C 1 35  ASP 35  35  35  ASP ASP C . n 
C 1 36  ILE 36  36  36  ILE ILE C . n 
C 1 37  LEU 37  37  37  LEU LEU C . n 
C 1 38  GLN 38  38  38  GLN GLN C . n 
C 1 39  TYR 39  39  39  TYR TYR C . n 
C 1 40  ASP 40  40  40  ASP ASP C . n 
C 1 41  ALA 41  41  41  ALA ALA C . n 
C 1 42  SER 42  42  42  SER SER C . n 
C 1 43  LEU 43  43  43  LEU LEU C . n 
C 1 44  THR 44  44  44  THR THR C . n 
C 1 45  PRO 45  45  45  PRO PRO C . n 
C 1 46  LEU 46  46  46  LEU LEU C . n 
C 1 47  GLU 47  47  47  GLU GLU C . n 
C 1 48  PHE 48  48  48  PHE PHE C . n 
C 1 49  GLN 49  49  49  GLN GLN C . n 
C 1 50  GLY 50  50  50  GLY GLY C . n 
C 1 51  TYR 51  51  51  TYR TYR C . n 
C 1 52  ASN 52  52  52  ASN ASN C . n 
C 1 53  LEU 53  53  53  LEU LEU C . n 
C 1 54  SER 54  54  54  SER SER C . n 
C 1 55  ALA 55  55  55  ALA ALA C . n 
C 1 56  ASN 56  56  56  ASN ASN C . n 
C 1 57  LYS 57  57  57  LYS LYS C . n 
C 1 58  GLN 58  58  58  GLN GLN C . n 
C 1 59  PHE 59  59  59  PHE PHE C . n 
C 1 60  LEU 60  60  60  LEU LEU C . n 
C 1 61  LEU 61  61  61  LEU LEU C . n 
C 1 62  THR 62  62  62  THR THR C . n 
C 1 63  ASN 63  63  63  ASN ASN C . n 
C 1 64  ASN 64  64  64  ASN ASN C . n 
C 1 65  GLY 65  65  65  GLY GLY C . n 
C 1 66  HIS 66  66  66  HIS HIS C . n 
C 1 67  SER 67  67  67  SER SER C . n 
C 1 68  VAL 68  68  68  VAL VAL C . n 
C 1 69  LYS 69  69  69  LYS LYS C . n 
C 1 70  LEU 70  70  70  LEU LEU C . n 
C 1 71  ASN 71  71  71  ASN ASN C . n 
C 1 72  LEU 72  72  72  LEU LEU C . n 
C 1 73  PRO 73  73  73  PRO PRO C . n 
C 1 74  SER 74  74  74  SER SER C . n 
C 1 75  ASP 75  75  75  ASP ASP C . n 
C 1 76  MET 76  76  76  MET MET C . n 
C 1 77  HIS 77  77  77  HIS HIS C . n 
C 1 78  ILE 78  78  78  ILE ILE C . n 
C 1 79  GLN 79  79  79  GLN GLN C . n 
C 1 80  GLY 80  80  80  GLY GLY C . n 
C 1 81  LEU 81  81  81  LEU LEU C . n 
C 1 82  GLN 82  82  82  GLN GLN C . n 
C 1 83  SER 83  83  83  SER SER C . n 
C 1 84  ARG 84  84  84  ARG ARG C . n 
C 1 85  TYR 85  85  85  TYR TYR C . n 
C 1 86  SER 86  86  86  SER SER C . n 
C 1 87  ALA 87  87  87  ALA ALA C . n 
C 1 88  THR 88  88  88  THR THR C . n 
C 1 89  GLN 89  89  89  GLN GLN C . n 
C 1 90  LEU 90  90  90  LEU LEU C . n 
C 1 91  HIS 91  91  91  HIS HIS C . n 
C 1 92  LEU 92  92  92  LEU LEU C . n 
C 1 93  HIS 93  93  93  HIS HIS C . n 
C 1 94  TRP 94  94  94  TRP TRP C . n 
C 1 95  GLY 95  95  95  GLY GLY C . n 
C 1 96  ASN 96  96  96  ASN ASN C . n 
C 1 97  PRO 97  97  97  PRO PRO C . n 
C 1 98  ASN 98  98  98  ASN ASN C . n 
C 1 99  ASP 99  99  99  ASP ASP C . n 
C 1 100 PRO 100 100 100 PRO PRO C . n 
C 1 101 HIS 101 101 101 HIS HIS C . n 
C 1 102 GLY 102 102 102 GLY GLY C . n 
C 1 103 SER 103 103 103 SER SER C . n 
C 1 104 GLU 104 104 104 GLU GLU C . n 
C 1 105 HIS 105 105 105 HIS HIS C . n 
C 1 106 THR 106 106 106 THR THR C . n 
C 1 107 VAL 107 107 107 VAL VAL C . n 
C 1 108 SER 108 108 108 SER SER C . n 
C 1 109 GLY 109 109 109 GLY GLY C . n 
C 1 110 GLN 110 110 110 GLN GLN C . n 
C 1 111 HIS 111 111 111 HIS HIS C . n 
C 1 112 PHE 112 112 112 PHE PHE C . n 
C 1 113 ALA 113 113 113 ALA ALA C . n 
C 1 114 ALA 114 114 114 ALA ALA C . n 
C 1 115 GLU 115 115 115 GLU GLU C . n 
C 1 116 LEU 116 116 116 LEU LEU C . n 
C 1 117 HIS 117 117 117 HIS HIS C . n 
C 1 118 ILE 118 118 118 ILE ILE C . n 
C 1 119 VAL 119 119 119 VAL VAL C . n 
C 1 120 HIS 120 120 120 HIS HIS C . n 
C 1 121 TYR 121 121 121 TYR TYR C . n 
C 1 122 ASN 122 122 122 ASN ASN C . n 
C 1 123 SER 123 123 123 SER SER C . n 
C 1 124 ASP 124 124 124 ASP ASP C . n 
C 1 125 LEU 125 125 125 LEU LEU C . n 
C 1 126 TYR 126 126 126 TYR TYR C . n 
C 1 127 PRO 127 127 127 PRO PRO C . n 
C 1 128 ASP 128 128 128 ASP ASP C . n 
C 1 129 ALA 129 129 129 ALA ALA C . n 
C 1 130 SER 130 130 130 SER SER C . n 
C 1 131 THR 131 131 131 THR THR C . n 
C 1 132 ALA 132 132 132 ALA ALA C . n 
C 1 133 SER 133 133 133 SER SER C . n 
C 1 134 ASN 134 134 134 ASN ASN C . n 
C 1 135 LYS 135 135 135 LYS LYS C . n 
C 1 136 SER 136 136 136 SER SER C . n 
C 1 137 GLU 137 137 137 GLU GLU C . n 
C 1 138 GLY 138 138 138 GLY GLY C . n 
C 1 139 LEU 139 139 139 LEU LEU C . n 
C 1 140 ALA 140 140 140 ALA ALA C . n 
C 1 141 VAL 141 141 141 VAL VAL C . n 
C 1 142 LEU 142 142 142 LEU LEU C . n 
C 1 143 ALA 143 143 143 ALA ALA C . n 
C 1 144 VAL 144 144 144 VAL VAL C . n 
C 1 145 LEU 145 145 145 LEU LEU C . n 
C 1 146 ILE 146 146 146 ILE ILE C . n 
C 1 147 GLU 147 147 147 GLU GLU C . n 
C 1 148 MET 148 148 148 MET MET C . n 
C 1 149 GLY 149 149 149 GLY GLY C . n 
C 1 150 SER 150 150 150 SER SER C . n 
C 1 151 PHE 151 151 151 PHE PHE C . n 
C 1 152 ASN 152 152 152 ASN ASN C . n 
C 1 153 PRO 153 153 153 PRO PRO C . n 
C 1 154 SER 154 154 154 SER SER C . n 
C 1 155 TYR 155 155 155 TYR TYR C . n 
C 1 156 ASP 156 156 156 ASP ASP C . n 
C 1 157 LYS 157 157 157 LYS LYS C . n 
C 1 158 ILE 158 158 158 ILE ILE C . n 
C 1 159 PHE 159 159 159 PHE PHE C . n 
C 1 160 SER 160 160 160 SER SER C . n 
C 1 161 HIS 161 161 161 HIS HIS C . n 
C 1 162 LEU 162 162 162 LEU LEU C . n 
C 1 163 GLN 163 163 163 GLN GLN C . n 
C 1 164 HIS 164 164 164 HIS HIS C . n 
C 1 165 VAL 165 165 165 VAL VAL C . n 
C 1 166 LYS 166 166 166 LYS LYS C . n 
C 1 167 TYR 167 167 167 TYR TYR C . n 
C 1 168 LYS 168 168 168 LYS LYS C . n 
C 1 169 GLY 169 169 169 GLY GLY C . n 
C 1 170 GLN 170 170 170 GLN GLN C . n 
C 1 171 GLU 171 171 171 GLU GLU C . n 
C 1 172 ALA 172 172 172 ALA ALA C . n 
C 1 173 PHE 173 173 173 PHE PHE C . n 
C 1 174 VAL 174 174 174 VAL VAL C . n 
C 1 175 PRO 175 175 175 PRO PRO C . n 
C 1 176 GLY 176 176 176 GLY GLY C . n 
C 1 177 PHE 177 177 177 PHE PHE C . n 
C 1 178 ASN 178 178 178 ASN ASN C . n 
C 1 179 ILE 179 179 179 ILE ILE C . n 
C 1 180 GLU 180 180 180 GLU GLU C . n 
C 1 181 GLU 181 181 181 GLU GLU C . n 
C 1 182 LEU 182 182 182 LEU LEU C . n 
C 1 183 LEU 183 183 183 LEU LEU C . n 
C 1 184 PRO 184 184 184 PRO PRO C . n 
C 1 185 GLU 185 185 185 GLU GLU C . n 
C 1 186 ARG 186 186 186 ARG ARG C . n 
C 1 187 THR 187 187 187 THR THR C . n 
C 1 188 ALA 188 188 188 ALA ALA C . n 
C 1 189 GLU 189 189 189 GLU GLU C . n 
C 1 190 TYR 190 190 190 TYR TYR C . n 
C 1 191 TYR 191 191 191 TYR TYR C . n 
C 1 192 ARG 192 192 192 ARG ARG C . n 
C 1 193 TYR 193 193 193 TYR TYR C . n 
C 1 194 ARG 194 194 194 ARG ARG C . n 
C 1 195 GLY 195 195 195 GLY GLY C . n 
C 1 196 SER 196 196 196 SER SER C . n 
C 1 197 LEU 197 197 197 LEU LEU C . n 
C 1 198 THR 198 198 198 THR THR C . n 
C 1 199 THR 199 199 199 THR THR C . n 
C 1 200 PRO 200 200 200 PRO PRO C . n 
C 1 201 PRO 201 201 201 PRO PRO C . n 
C 1 202 CYS 202 202 202 CYS CYS C . n 
C 1 203 ASN 203 203 203 ASN ASN C . n 
C 1 204 PRO 204 204 204 PRO PRO C . n 
C 1 205 THR 205 205 205 THR THR C . n 
C 1 206 VAL 206 206 206 VAL VAL C . n 
C 1 207 LEU 207 207 207 LEU LEU C . n 
C 1 208 TRP 208 208 208 TRP TRP C . n 
C 1 209 THR 209 209 209 THR THR C . n 
C 1 210 VAL 210 210 210 VAL VAL C . n 
C 1 211 PHE 211 211 211 PHE PHE C . n 
C 1 212 ARG 212 212 212 ARG ARG C . n 
C 1 213 ASN 213 213 213 ASN ASN C . n 
C 1 214 PRO 214 214 214 PRO PRO C . n 
C 1 215 VAL 215 215 215 VAL VAL C . n 
C 1 216 GLN 216 216 216 GLN GLN C . n 
C 1 217 ILE 217 217 217 ILE ILE C . n 
C 1 218 SER 218 218 218 SER SER C . n 
C 1 219 GLN 219 219 219 GLN GLN C . n 
C 1 220 GLU 220 220 220 GLU GLU C . n 
C 1 221 GLN 221 221 221 GLN GLN C . n 
C 1 222 LEU 222 222 222 LEU LEU C . n 
C 1 223 LEU 223 223 223 LEU LEU C . n 
C 1 224 ALA 224 224 224 ALA ALA C . n 
C 1 225 LEU 225 225 225 LEU LEU C . n 
C 1 226 GLU 226 226 226 GLU GLU C . n 
C 1 227 THR 227 227 227 THR THR C . n 
C 1 228 ALA 228 228 228 ALA ALA C . n 
C 1 229 LEU 229 229 229 LEU LEU C . n 
C 1 230 TYR 230 230 230 TYR TYR C . n 
C 1 231 CYS 231 231 231 CYS CYS C . n 
C 1 232 THR 232 232 232 THR THR C . n 
C 1 233 HIS 233 233 233 HIS HIS C . n 
C 1 234 MET 234 234 234 MET MET C . n 
C 1 235 ASP 235 235 235 ASP ASP C . n 
C 1 236 ASP 236 236 236 ASP ASP C . n 
C 1 237 PRO 237 237 237 PRO PRO C . n 
C 1 238 SER 238 238 238 SER SER C . n 
C 1 239 PRO 239 239 239 PRO PRO C . n 
C 1 240 ARG 240 240 240 ARG ARG C . n 
C 1 241 GLU 241 241 241 GLU GLU C . n 
C 1 242 MET 242 242 242 MET MET C . n 
C 1 243 ILE 243 243 243 ILE ILE C . n 
C 1 244 ASN 244 244 244 ASN ASN C . n 
C 1 245 ASN 245 245 245 ASN ASN C . n 
C 1 246 PHE 246 246 246 PHE PHE C . n 
C 1 247 ARG 247 247 247 ARG ARG C . n 
C 1 248 GLN 248 248 248 GLN GLN C . n 
C 1 249 VAL 249 249 249 VAL VAL C . n 
C 1 250 GLN 250 250 250 GLN GLN C . n 
C 1 251 LYS 251 251 251 LYS LYS C . n 
C 1 252 PHE 252 252 252 PHE PHE C . n 
C 1 253 ASP 253 253 253 ASP ASP C . n 
C 1 254 GLU 254 254 254 GLU GLU C . n 
C 1 255 ARG 255 255 255 ARG ARG C . n 
C 1 256 LEU 256 256 256 LEU LEU C . n 
C 1 257 VAL 257 257 257 VAL VAL C . n 
C 1 258 TYR 258 258 258 TYR TYR C . n 
C 1 259 THR 259 259 259 THR THR C . n 
C 1 260 SER 260 260 260 SER SER C . n 
C 1 261 PHE 261 261 261 PHE PHE C . n 
C 1 262 SER 262 262 262 SER SER C . n 
C 1 263 GLN 263 263 263 GLN GLN C . n 
D 1 1   MET 1   1   ?   ?   ?   D . n 
D 1 2   SER 2   2   ?   ?   ?   D . n 
D 1 3   LYS 3   3   3   LYS LYS D . n 
D 1 4   TRP 4   4   4   TRP TRP D . n 
D 1 5   THR 5   5   5   THR THR D . n 
D 1 6   TYR 6   6   6   TYR TYR D . n 
D 1 7   PHE 7   7   7   PHE PHE D . n 
D 1 8   GLY 8   8   8   GLY GLY D . n 
D 1 9   PRO 9   9   9   PRO PRO D . n 
D 1 10  ASP 10  10  10  ASP ASP D . n 
D 1 11  GLY 11  11  11  GLY GLY D . n 
D 1 12  GLU 12  12  12  GLU GLU D . n 
D 1 13  ASN 13  13  13  ASN ASN D . n 
D 1 14  SER 14  14  14  SER SER D . n 
D 1 15  TRP 15  15  15  TRP TRP D . n 
D 1 16  SER 16  16  16  SER SER D . n 
D 1 17  LYS 17  17  17  LYS LYS D . n 
D 1 18  LYS 18  18  18  LYS LYS D . n 
D 1 19  TYR 19  19  19  TYR TYR D . n 
D 1 20  PRO 20  20  20  PRO PRO D . n 
D 1 21  SER 21  21  21  SER SER D . n 
D 1 22  CYS 22  22  22  CYS CYS D . n 
D 1 23  GLY 23  23  23  GLY GLY D . n 
D 1 24  GLY 24  24  24  GLY GLY D . n 
D 1 25  LEU 25  25  25  LEU LEU D . n 
D 1 26  LEU 26  26  26  LEU LEU D . n 
D 1 27  GLN 27  27  27  GLN GLN D . n 
D 1 28  SER 28  28  28  SER SER D . n 
D 1 29  PRO 29  29  29  PRO PRO D . n 
D 1 30  ILE 30  30  30  ILE ILE D . n 
D 1 31  ASP 31  31  31  ASP ASP D . n 
D 1 32  LEU 32  32  32  LEU LEU D . n 
D 1 33  HIS 33  33  33  HIS HIS D . n 
D 1 34  SER 34  34  34  SER SER D . n 
D 1 35  ASP 35  35  35  ASP ASP D . n 
D 1 36  ILE 36  36  36  ILE ILE D . n 
D 1 37  LEU 37  37  37  LEU LEU D . n 
D 1 38  GLN 38  38  38  GLN GLN D . n 
D 1 39  TYR 39  39  39  TYR TYR D . n 
D 1 40  ASP 40  40  40  ASP ASP D . n 
D 1 41  ALA 41  41  41  ALA ALA D . n 
D 1 42  SER 42  42  42  SER SER D . n 
D 1 43  LEU 43  43  43  LEU LEU D . n 
D 1 44  THR 44  44  44  THR THR D . n 
D 1 45  PRO 45  45  45  PRO PRO D . n 
D 1 46  LEU 46  46  46  LEU LEU D . n 
D 1 47  GLU 47  47  47  GLU GLU D . n 
D 1 48  PHE 48  48  48  PHE PHE D . n 
D 1 49  GLN 49  49  49  GLN GLN D . n 
D 1 50  GLY 50  50  50  GLY GLY D . n 
D 1 51  TYR 51  51  51  TYR TYR D . n 
D 1 52  ASN 52  52  52  ASN ASN D . n 
D 1 53  LEU 53  53  53  LEU LEU D . n 
D 1 54  SER 54  54  54  SER SER D . n 
D 1 55  ALA 55  55  55  ALA ALA D . n 
D 1 56  ASN 56  56  56  ASN ASN D . n 
D 1 57  LYS 57  57  57  LYS LYS D . n 
D 1 58  GLN 58  58  58  GLN GLN D . n 
D 1 59  PHE 59  59  59  PHE PHE D . n 
D 1 60  LEU 60  60  60  LEU LEU D . n 
D 1 61  LEU 61  61  61  LEU LEU D . n 
D 1 62  THR 62  62  62  THR THR D . n 
D 1 63  ASN 63  63  63  ASN ASN D . n 
D 1 64  ASN 64  64  64  ASN ASN D . n 
D 1 65  GLY 65  65  65  GLY GLY D . n 
D 1 66  HIS 66  66  66  HIS HIS D . n 
D 1 67  SER 67  67  67  SER SER D . n 
D 1 68  VAL 68  68  68  VAL VAL D . n 
D 1 69  LYS 69  69  69  LYS LYS D . n 
D 1 70  LEU 70  70  70  LEU LEU D . n 
D 1 71  ASN 71  71  71  ASN ASN D . n 
D 1 72  LEU 72  72  72  LEU LEU D . n 
D 1 73  PRO 73  73  73  PRO PRO D . n 
D 1 74  SER 74  74  74  SER SER D . n 
D 1 75  ASP 75  75  75  ASP ASP D . n 
D 1 76  MET 76  76  76  MET MET D . n 
D 1 77  HIS 77  77  77  HIS HIS D . n 
D 1 78  ILE 78  78  78  ILE ILE D . n 
D 1 79  GLN 79  79  79  GLN GLN D . n 
D 1 80  GLY 80  80  80  GLY GLY D . n 
D 1 81  LEU 81  81  81  LEU LEU D . n 
D 1 82  GLN 82  82  82  GLN GLN D . n 
D 1 83  SER 83  83  83  SER SER D . n 
D 1 84  ARG 84  84  84  ARG ARG D . n 
D 1 85  TYR 85  85  85  TYR TYR D . n 
D 1 86  SER 86  86  86  SER SER D . n 
D 1 87  ALA 87  87  87  ALA ALA D . n 
D 1 88  THR 88  88  88  THR THR D . n 
D 1 89  GLN 89  89  89  GLN GLN D . n 
D 1 90  LEU 90  90  90  LEU LEU D . n 
D 1 91  HIS 91  91  91  HIS HIS D . n 
D 1 92  LEU 92  92  92  LEU LEU D . n 
D 1 93  HIS 93  93  93  HIS HIS D . n 
D 1 94  TRP 94  94  94  TRP TRP D . n 
D 1 95  GLY 95  95  95  GLY GLY D . n 
D 1 96  ASN 96  96  96  ASN ASN D . n 
D 1 97  PRO 97  97  97  PRO PRO D . n 
D 1 98  ASN 98  98  98  ASN ASN D . n 
D 1 99  ASP 99  99  99  ASP ASP D . n 
D 1 100 PRO 100 100 100 PRO PRO D . n 
D 1 101 HIS 101 101 101 HIS HIS D . n 
D 1 102 GLY 102 102 102 GLY GLY D . n 
D 1 103 SER 103 103 103 SER SER D . n 
D 1 104 GLU 104 104 104 GLU GLU D . n 
D 1 105 HIS 105 105 105 HIS HIS D . n 
D 1 106 THR 106 106 106 THR THR D . n 
D 1 107 VAL 107 107 107 VAL VAL D . n 
D 1 108 SER 108 108 108 SER SER D . n 
D 1 109 GLY 109 109 109 GLY GLY D . n 
D 1 110 GLN 110 110 110 GLN GLN D . n 
D 1 111 HIS 111 111 111 HIS HIS D . n 
D 1 112 PHE 112 112 112 PHE PHE D . n 
D 1 113 ALA 113 113 113 ALA ALA D . n 
D 1 114 ALA 114 114 114 ALA ALA D . n 
D 1 115 GLU 115 115 115 GLU GLU D . n 
D 1 116 LEU 116 116 116 LEU LEU D . n 
D 1 117 HIS 117 117 117 HIS HIS D . n 
D 1 118 ILE 118 118 118 ILE ILE D . n 
D 1 119 VAL 119 119 119 VAL VAL D . n 
D 1 120 HIS 120 120 120 HIS HIS D . n 
D 1 121 TYR 121 121 121 TYR TYR D . n 
D 1 122 ASN 122 122 122 ASN ASN D . n 
D 1 123 SER 123 123 123 SER SER D . n 
D 1 124 ASP 124 124 124 ASP ASP D . n 
D 1 125 LEU 125 125 125 LEU LEU D . n 
D 1 126 TYR 126 126 126 TYR TYR D . n 
D 1 127 PRO 127 127 127 PRO PRO D . n 
D 1 128 ASP 128 128 128 ASP ASP D . n 
D 1 129 ALA 129 129 129 ALA ALA D . n 
D 1 130 SER 130 130 130 SER SER D . n 
D 1 131 THR 131 131 131 THR THR D . n 
D 1 132 ALA 132 132 132 ALA ALA D . n 
D 1 133 SER 133 133 133 SER SER D . n 
D 1 134 ASN 134 134 134 ASN ASN D . n 
D 1 135 LYS 135 135 135 LYS LYS D . n 
D 1 136 SER 136 136 136 SER SER D . n 
D 1 137 GLU 137 137 137 GLU GLU D . n 
D 1 138 GLY 138 138 138 GLY GLY D . n 
D 1 139 LEU 139 139 139 LEU LEU D . n 
D 1 140 ALA 140 140 140 ALA ALA D . n 
D 1 141 VAL 141 141 141 VAL VAL D . n 
D 1 142 LEU 142 142 142 LEU LEU D . n 
D 1 143 ALA 143 143 143 ALA ALA D . n 
D 1 144 VAL 144 144 144 VAL VAL D . n 
D 1 145 LEU 145 145 145 LEU LEU D . n 
D 1 146 ILE 146 146 146 ILE ILE D . n 
D 1 147 GLU 147 147 147 GLU GLU D . n 
D 1 148 MET 148 148 148 MET MET D . n 
D 1 149 GLY 149 149 149 GLY GLY D . n 
D 1 150 SER 150 150 150 SER SER D . n 
D 1 151 PHE 151 151 151 PHE PHE D . n 
D 1 152 ASN 152 152 152 ASN ASN D . n 
D 1 153 PRO 153 153 153 PRO PRO D . n 
D 1 154 SER 154 154 154 SER SER D . n 
D 1 155 TYR 155 155 155 TYR TYR D . n 
D 1 156 ASP 156 156 156 ASP ASP D . n 
D 1 157 LYS 157 157 157 LYS LYS D . n 
D 1 158 ILE 158 158 158 ILE ILE D . n 
D 1 159 PHE 159 159 159 PHE PHE D . n 
D 1 160 SER 160 160 160 SER SER D . n 
D 1 161 HIS 161 161 161 HIS HIS D . n 
D 1 162 LEU 162 162 162 LEU LEU D . n 
D 1 163 GLN 163 163 163 GLN GLN D . n 
D 1 164 HIS 164 164 164 HIS HIS D . n 
D 1 165 VAL 165 165 165 VAL VAL D . n 
D 1 166 LYS 166 166 166 LYS LYS D . n 
D 1 167 TYR 167 167 167 TYR TYR D . n 
D 1 168 LYS 168 168 168 LYS LYS D . n 
D 1 169 GLY 169 169 169 GLY GLY D . n 
D 1 170 GLN 170 170 170 GLN GLN D . n 
D 1 171 GLU 171 171 171 GLU GLU D . n 
D 1 172 ALA 172 172 172 ALA ALA D . n 
D 1 173 PHE 173 173 173 PHE PHE D . n 
D 1 174 VAL 174 174 174 VAL VAL D . n 
D 1 175 PRO 175 175 175 PRO PRO D . n 
D 1 176 GLY 176 176 176 GLY GLY D . n 
D 1 177 PHE 177 177 177 PHE PHE D . n 
D 1 178 ASN 178 178 178 ASN ASN D . n 
D 1 179 ILE 179 179 179 ILE ILE D . n 
D 1 180 GLU 180 180 180 GLU GLU D . n 
D 1 181 GLU 181 181 181 GLU GLU D . n 
D 1 182 LEU 182 182 182 LEU LEU D . n 
D 1 183 LEU 183 183 183 LEU LEU D . n 
D 1 184 PRO 184 184 184 PRO PRO D . n 
D 1 185 GLU 185 185 185 GLU GLU D . n 
D 1 186 ARG 186 186 186 ARG ARG D . n 
D 1 187 THR 187 187 187 THR THR D . n 
D 1 188 ALA 188 188 188 ALA ALA D . n 
D 1 189 GLU 189 189 189 GLU GLU D . n 
D 1 190 TYR 190 190 190 TYR TYR D . n 
D 1 191 TYR 191 191 191 TYR TYR D . n 
D 1 192 ARG 192 192 192 ARG ARG D . n 
D 1 193 TYR 193 193 193 TYR TYR D . n 
D 1 194 ARG 194 194 194 ARG ARG D . n 
D 1 195 GLY 195 195 195 GLY GLY D . n 
D 1 196 SER 196 196 196 SER SER D . n 
D 1 197 LEU 197 197 197 LEU LEU D . n 
D 1 198 THR 198 198 198 THR THR D . n 
D 1 199 THR 199 199 199 THR THR D . n 
D 1 200 PRO 200 200 200 PRO PRO D . n 
D 1 201 PRO 201 201 201 PRO PRO D . n 
D 1 202 CYS 202 202 202 CYS CYS D . n 
D 1 203 ASN 203 203 203 ASN ASN D . n 
D 1 204 PRO 204 204 204 PRO PRO D . n 
D 1 205 THR 205 205 205 THR THR D . n 
D 1 206 VAL 206 206 206 VAL VAL D . n 
D 1 207 LEU 207 207 207 LEU LEU D . n 
D 1 208 TRP 208 208 208 TRP TRP D . n 
D 1 209 THR 209 209 209 THR THR D . n 
D 1 210 VAL 210 210 210 VAL VAL D . n 
D 1 211 PHE 211 211 211 PHE PHE D . n 
D 1 212 ARG 212 212 212 ARG ARG D . n 
D 1 213 ASN 213 213 213 ASN ASN D . n 
D 1 214 PRO 214 214 214 PRO PRO D . n 
D 1 215 VAL 215 215 215 VAL VAL D . n 
D 1 216 GLN 216 216 216 GLN GLN D . n 
D 1 217 ILE 217 217 217 ILE ILE D . n 
D 1 218 SER 218 218 218 SER SER D . n 
D 1 219 GLN 219 219 219 GLN GLN D . n 
D 1 220 GLU 220 220 220 GLU GLU D . n 
D 1 221 GLN 221 221 221 GLN GLN D . n 
D 1 222 LEU 222 222 222 LEU LEU D . n 
D 1 223 LEU 223 223 223 LEU LEU D . n 
D 1 224 ALA 224 224 224 ALA ALA D . n 
D 1 225 LEU 225 225 225 LEU LEU D . n 
D 1 226 GLU 226 226 226 GLU GLU D . n 
D 1 227 THR 227 227 227 THR THR D . n 
D 1 228 ALA 228 228 228 ALA ALA D . n 
D 1 229 LEU 229 229 229 LEU LEU D . n 
D 1 230 TYR 230 230 230 TYR TYR D . n 
D 1 231 CYS 231 231 231 CYS CYS D . n 
D 1 232 THR 232 232 232 THR THR D . n 
D 1 233 HIS 233 233 233 HIS HIS D . n 
D 1 234 MET 234 234 234 MET MET D . n 
D 1 235 ASP 235 235 235 ASP ASP D . n 
D 1 236 ASP 236 236 236 ASP ASP D . n 
D 1 237 PRO 237 237 237 PRO PRO D . n 
D 1 238 SER 238 238 238 SER SER D . n 
D 1 239 PRO 239 239 239 PRO PRO D . n 
D 1 240 ARG 240 240 240 ARG ARG D . n 
D 1 241 GLU 241 241 241 GLU GLU D . n 
D 1 242 MET 242 242 242 MET MET D . n 
D 1 243 ILE 243 243 243 ILE ILE D . n 
D 1 244 ASN 244 244 244 ASN ASN D . n 
D 1 245 ASN 245 245 245 ASN ASN D . n 
D 1 246 PHE 246 246 246 PHE PHE D . n 
D 1 247 ARG 247 247 247 ARG ARG D . n 
D 1 248 GLN 248 248 248 GLN GLN D . n 
D 1 249 VAL 249 249 249 VAL VAL D . n 
D 1 250 GLN 250 250 250 GLN GLN D . n 
D 1 251 LYS 251 251 251 LYS LYS D . n 
D 1 252 PHE 252 252 252 PHE PHE D . n 
D 1 253 ASP 253 253 253 ASP ASP D . n 
D 1 254 GLU 254 254 254 GLU GLU D . n 
D 1 255 ARG 255 255 255 ARG ARG D . n 
D 1 256 LEU 256 256 256 LEU LEU D . n 
D 1 257 VAL 257 257 257 VAL VAL D . n 
D 1 258 TYR 258 258 258 TYR TYR D . n 
D 1 259 THR 259 259 259 THR THR D . n 
D 1 260 SER 260 260 260 SER SER D . n 
D 1 261 PHE 261 261 261 PHE PHE D . n 
D 1 262 SER 262 262 262 SER SER D . n 
D 1 263 GLN 263 263 263 GLN GLN D . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
E  2 ZN  1   301 4    ZN  ZN  A . 
F  3 6YQ 1   302 3    6YQ E16 A . 
G  4 EDO 1   303 3    EDO EGL A . 
H  4 EDO 1   304 4    EDO EGL A . 
I  4 EDO 1   305 9    EDO EGL A . 
J  4 EDO 1   306 10   EDO EDO A . 
K  2 ZN  1   301 3    ZN  ZN  B . 
L  3 6YQ 1   302 2    6YQ E16 B . 
M  5 SO4 1   303 2    SO4 SO4 B . 
N  4 EDO 1   304 2    EDO EGL B . 
O  4 EDO 1   305 5    EDO EGL B . 
P  2 ZN  1   301 1    ZN  ZN  C . 
Q  3 6YQ 1   302 4    6YQ E16 C . 
R  5 SO4 1   303 3    SO4 SO4 C . 
S  4 EDO 1   304 6    EDO EGL C . 
T  4 EDO 1   305 12   EDO EDO C . 
U  2 ZN  1   301 2    ZN  ZN  D . 
V  3 6YQ 1   302 1    6YQ E16 D . 
W  5 SO4 1   303 1    SO4 SO4 D . 
X  4 EDO 1   304 1    EDO EGL D . 
Y  4 EDO 1   305 7    EDO EGL D . 
Z  4 EDO 1   306 11   EDO EDO D . 
AA 6 HOH 1   401 723  HOH HOH A . 
AA 6 HOH 2   402 872  HOH HOH A . 
AA 6 HOH 3   403 1063 HOH HOH A . 
AA 6 HOH 4   404 1071 HOH HOH A . 
AA 6 HOH 5   405 743  HOH HOH A . 
AA 6 HOH 6   406 314  HOH HOH A . 
AA 6 HOH 7   407 534  HOH HOH A . 
AA 6 HOH 8   408 1082 HOH HOH A . 
AA 6 HOH 9   409 889  HOH HOH A . 
AA 6 HOH 10  410 794  HOH HOH A . 
AA 6 HOH 11  411 830  HOH HOH A . 
AA 6 HOH 12  412 510  HOH HOH A . 
AA 6 HOH 13  413 732  HOH HOH A . 
AA 6 HOH 14  414 83   HOH HOH A . 
AA 6 HOH 15  415 217  HOH HOH A . 
AA 6 HOH 16  416 993  HOH HOH A . 
AA 6 HOH 17  417 4    HOH HOH A . 
AA 6 HOH 18  418 1209 HOH HOH A . 
AA 6 HOH 19  419 624  HOH HOH A . 
AA 6 HOH 20  420 1050 HOH HOH A . 
AA 6 HOH 21  421 245  HOH HOH A . 
AA 6 HOH 22  422 460  HOH HOH A . 
AA 6 HOH 23  423 466  HOH HOH A . 
AA 6 HOH 24  424 119  HOH HOH A . 
AA 6 HOH 25  425 766  HOH HOH A . 
AA 6 HOH 26  426 652  HOH HOH A . 
AA 6 HOH 27  427 211  HOH HOH A . 
AA 6 HOH 28  428 699  HOH HOH A . 
AA 6 HOH 29  429 978  HOH HOH A . 
AA 6 HOH 30  430 626  HOH HOH A . 
AA 6 HOH 31  431 1047 HOH HOH A . 
AA 6 HOH 32  432 721  HOH HOH A . 
AA 6 HOH 33  433 587  HOH HOH A . 
AA 6 HOH 34  434 997  HOH HOH A . 
AA 6 HOH 35  435 1093 HOH HOH A . 
AA 6 HOH 36  436 1079 HOH HOH A . 
AA 6 HOH 37  437 1083 HOH HOH A . 
AA 6 HOH 38  438 1060 HOH HOH A . 
AA 6 HOH 39  439 637  HOH HOH A . 
AA 6 HOH 40  440 482  HOH HOH A . 
AA 6 HOH 41  441 71   HOH HOH A . 
AA 6 HOH 42  442 19   HOH HOH A . 
AA 6 HOH 43  443 61   HOH HOH A . 
AA 6 HOH 44  444 348  HOH HOH A . 
AA 6 HOH 45  445 899  HOH HOH A . 
AA 6 HOH 46  446 102  HOH HOH A . 
AA 6 HOH 47  447 311  HOH HOH A . 
AA 6 HOH 48  448 404  HOH HOH A . 
AA 6 HOH 49  449 85   HOH HOH A . 
AA 6 HOH 50  450 544  HOH HOH A . 
AA 6 HOH 51  451 106  HOH HOH A . 
AA 6 HOH 52  452 816  HOH HOH A . 
AA 6 HOH 53  453 1088 HOH HOH A . 
AA 6 HOH 54  454 58   HOH HOH A . 
AA 6 HOH 55  455 42   HOH HOH A . 
AA 6 HOH 56  456 64   HOH HOH A . 
AA 6 HOH 57  457 585  HOH HOH A . 
AA 6 HOH 58  458 428  HOH HOH A . 
AA 6 HOH 59  459 192  HOH HOH A . 
AA 6 HOH 60  460 21   HOH HOH A . 
AA 6 HOH 61  461 312  HOH HOH A . 
AA 6 HOH 62  462 167  HOH HOH A . 
AA 6 HOH 63  463 1005 HOH HOH A . 
AA 6 HOH 64  464 439  HOH HOH A . 
AA 6 HOH 65  465 697  HOH HOH A . 
AA 6 HOH 66  466 99   HOH HOH A . 
AA 6 HOH 67  467 803  HOH HOH A . 
AA 6 HOH 68  468 1004 HOH HOH A . 
AA 6 HOH 69  469 687  HOH HOH A . 
AA 6 HOH 70  470 233  HOH HOH A . 
AA 6 HOH 71  471 729  HOH HOH A . 
AA 6 HOH 72  472 541  HOH HOH A . 
AA 6 HOH 73  473 400  HOH HOH A . 
AA 6 HOH 74  474 198  HOH HOH A . 
AA 6 HOH 75  475 31   HOH HOH A . 
AA 6 HOH 76  476 523  HOH HOH A . 
AA 6 HOH 77  477 357  HOH HOH A . 
AA 6 HOH 78  478 1003 HOH HOH A . 
AA 6 HOH 79  479 408  HOH HOH A . 
AA 6 HOH 80  480 49   HOH HOH A . 
AA 6 HOH 81  481 793  HOH HOH A . 
AA 6 HOH 82  482 302  HOH HOH A . 
AA 6 HOH 83  483 615  HOH HOH A . 
AA 6 HOH 84  484 396  HOH HOH A . 
AA 6 HOH 85  485 745  HOH HOH A . 
AA 6 HOH 86  486 47   HOH HOH A . 
AA 6 HOH 87  487 1073 HOH HOH A . 
AA 6 HOH 88  488 901  HOH HOH A . 
AA 6 HOH 89  489 722  HOH HOH A . 
AA 6 HOH 90  490 1    HOH HOH A . 
AA 6 HOH 91  491 375  HOH HOH A . 
AA 6 HOH 92  492 338  HOH HOH A . 
AA 6 HOH 93  493 1044 HOH HOH A . 
AA 6 HOH 94  494 904  HOH HOH A . 
AA 6 HOH 95  495 276  HOH HOH A . 
AA 6 HOH 96  496 405  HOH HOH A . 
AA 6 HOH 97  497 795  HOH HOH A . 
AA 6 HOH 98  498 215  HOH HOH A . 
AA 6 HOH 99  499 768  HOH HOH A . 
AA 6 HOH 100 500 183  HOH HOH A . 
AA 6 HOH 101 501 187  HOH HOH A . 
AA 6 HOH 102 502 452  HOH HOH A . 
AA 6 HOH 103 503 702  HOH HOH A . 
AA 6 HOH 104 504 701  HOH HOH A . 
AA 6 HOH 105 505 548  HOH HOH A . 
AA 6 HOH 106 506 1092 HOH HOH A . 
AA 6 HOH 107 507 203  HOH HOH A . 
AA 6 HOH 108 508 185  HOH HOH A . 
AA 6 HOH 109 509 148  HOH HOH A . 
AA 6 HOH 110 510 5    HOH HOH A . 
AA 6 HOH 111 511 902  HOH HOH A . 
AA 6 HOH 112 512 920  HOH HOH A . 
AA 6 HOH 113 513 23   HOH HOH A . 
AA 6 HOH 114 514 844  HOH HOH A . 
AA 6 HOH 115 515 197  HOH HOH A . 
AA 6 HOH 116 516 985  HOH HOH A . 
AA 6 HOH 117 517 87   HOH HOH A . 
AA 6 HOH 118 518 40   HOH HOH A . 
AA 6 HOH 119 519 406  HOH HOH A . 
AA 6 HOH 120 520 353  HOH HOH A . 
AA 6 HOH 121 521 11   HOH HOH A . 
AA 6 HOH 122 522 282  HOH HOH A . 
AA 6 HOH 123 523 1058 HOH HOH A . 
AA 6 HOH 124 524 190  HOH HOH A . 
AA 6 HOH 125 525 771  HOH HOH A . 
AA 6 HOH 126 526 263  HOH HOH A . 
AA 6 HOH 127 527 984  HOH HOH A . 
AA 6 HOH 128 528 1064 HOH HOH A . 
AA 6 HOH 129 529 196  HOH HOH A . 
AA 6 HOH 130 530 588  HOH HOH A . 
AA 6 HOH 131 531 317  HOH HOH A . 
AA 6 HOH 132 532 292  HOH HOH A . 
AA 6 HOH 133 533 603  HOH HOH A . 
AA 6 HOH 134 534 339  HOH HOH A . 
AA 6 HOH 135 535 1070 HOH HOH A . 
AA 6 HOH 136 536 246  HOH HOH A . 
AA 6 HOH 137 537 51   HOH HOH A . 
AA 6 HOH 138 538 999  HOH HOH A . 
AA 6 HOH 139 539 839  HOH HOH A . 
AA 6 HOH 140 540 354  HOH HOH A . 
AA 6 HOH 141 541 315  HOH HOH A . 
AA 6 HOH 142 542 179  HOH HOH A . 
AA 6 HOH 143 543 1078 HOH HOH A . 
AA 6 HOH 144 544 381  HOH HOH A . 
AA 6 HOH 145 545 565  HOH HOH A . 
AA 6 HOH 146 546 767  HOH HOH A . 
AA 6 HOH 147 547 705  HOH HOH A . 
AA 6 HOH 148 548 536  HOH HOH A . 
AA 6 HOH 149 549 989  HOH HOH A . 
AA 6 HOH 150 550 80   HOH HOH A . 
AA 6 HOH 151 551 189  HOH HOH A . 
AA 6 HOH 152 552 165  HOH HOH A . 
AA 6 HOH 153 553 740  HOH HOH A . 
AA 6 HOH 154 554 566  HOH HOH A . 
AA 6 HOH 155 555 1080 HOH HOH A . 
AA 6 HOH 156 556 671  HOH HOH A . 
AA 6 HOH 157 557 789  HOH HOH A . 
AA 6 HOH 158 558 504  HOH HOH A . 
AA 6 HOH 159 559 259  HOH HOH A . 
AA 6 HOH 160 560 673  HOH HOH A . 
AA 6 HOH 161 561 641  HOH HOH A . 
AA 6 HOH 162 562 822  HOH HOH A . 
AA 6 HOH 163 563 352  HOH HOH A . 
AA 6 HOH 164 564 413  HOH HOH A . 
AA 6 HOH 165 565 727  HOH HOH A . 
AA 6 HOH 166 566 113  HOH HOH A . 
AA 6 HOH 167 567 201  HOH HOH A . 
AA 6 HOH 168 568 908  HOH HOH A . 
AA 6 HOH 169 569 519  HOH HOH A . 
AA 6 HOH 170 570 340  HOH HOH A . 
AA 6 HOH 171 571 614  HOH HOH A . 
AA 6 HOH 172 572 1077 HOH HOH A . 
AA 6 HOH 173 573 485  HOH HOH A . 
AA 6 HOH 174 574 698  HOH HOH A . 
AA 6 HOH 175 575 1086 HOH HOH A . 
AA 6 HOH 176 576 134  HOH HOH A . 
AA 6 HOH 177 577 895  HOH HOH A . 
AA 6 HOH 178 578 955  HOH HOH A . 
AA 6 HOH 179 579 996  HOH HOH A . 
AA 6 HOH 180 580 419  HOH HOH A . 
AA 6 HOH 181 581 256  HOH HOH A . 
AA 6 HOH 182 582 913  HOH HOH A . 
AA 6 HOH 183 583 563  HOH HOH A . 
AA 6 HOH 184 584 455  HOH HOH A . 
AA 6 HOH 185 585 258  HOH HOH A . 
AA 6 HOH 186 586 597  HOH HOH A . 
AA 6 HOH 187 587 711  HOH HOH A . 
AA 6 HOH 188 588 242  HOH HOH A . 
AA 6 HOH 189 589 186  HOH HOH A . 
AA 6 HOH 190 590 596  HOH HOH A . 
AA 6 HOH 191 591 991  HOH HOH A . 
AA 6 HOH 192 592 543  HOH HOH A . 
AA 6 HOH 193 593 979  HOH HOH A . 
AA 6 HOH 194 594 559  HOH HOH A . 
AA 6 HOH 195 595 694  HOH HOH A . 
AA 6 HOH 196 596 865  HOH HOH A . 
AA 6 HOH 197 597 1049 HOH HOH A . 
AA 6 HOH 198 598 660  HOH HOH A . 
AA 6 HOH 199 599 628  HOH HOH A . 
AA 6 HOH 200 600 618  HOH HOH A . 
AA 6 HOH 201 601 769  HOH HOH A . 
AA 6 HOH 202 602 310  HOH HOH A . 
AA 6 HOH 203 603 916  HOH HOH A . 
AA 6 HOH 204 604 919  HOH HOH A . 
AA 6 HOH 205 605 1008 HOH HOH A . 
AA 6 HOH 206 606 104  HOH HOH A . 
AA 6 HOH 207 607 554  HOH HOH A . 
AA 6 HOH 208 608 1081 HOH HOH A . 
AA 6 HOH 209 609 385  HOH HOH A . 
AA 6 HOH 210 610 1067 HOH HOH A . 
AA 6 HOH 211 611 674  HOH HOH A . 
AA 6 HOH 212 612 438  HOH HOH A . 
AA 6 HOH 213 613 484  HOH HOH A . 
AA 6 HOH 214 614 986  HOH HOH A . 
AA 6 HOH 215 615 900  HOH HOH A . 
AA 6 HOH 216 616 915  HOH HOH A . 
AA 6 HOH 217 617 1211 HOH HOH A . 
AA 6 HOH 218 618 1066 HOH HOH A . 
AA 6 HOH 219 619 906  HOH HOH A . 
AA 6 HOH 220 620 1068 HOH HOH A . 
AA 6 HOH 221 621 1062 HOH HOH A . 
AA 6 HOH 222 622 1085 HOH HOH A . 
AA 6 HOH 223 623 362  HOH HOH A . 
AA 6 HOH 224 624 893  HOH HOH A . 
AA 6 HOH 225 625 911  HOH HOH A . 
AA 6 HOH 226 626 668  HOH HOH A . 
AA 6 HOH 227 627 663  HOH HOH A . 
AA 6 HOH 228 628 992  HOH HOH A . 
AA 6 HOH 229 629 1075 HOH HOH A . 
AA 6 HOH 230 630 1002 HOH HOH A . 
AA 6 HOH 231 631 778  HOH HOH A . 
AA 6 HOH 232 632 824  HOH HOH A . 
AA 6 HOH 233 633 1089 HOH HOH A . 
AA 6 HOH 234 634 807  HOH HOH A . 
AA 6 HOH 235 635 1087 HOH HOH A . 
AA 6 HOH 236 636 1210 HOH HOH A . 
AA 6 HOH 237 637 853  HOH HOH A . 
AA 6 HOH 238 638 382  HOH HOH A . 
AA 6 HOH 239 639 855  HOH HOH A . 
AA 6 HOH 240 640 594  HOH HOH A . 
AA 6 HOH 241 641 84   HOH HOH A . 
AA 6 HOH 242 642 435  HOH HOH A . 
AA 6 HOH 243 643 1069 HOH HOH A . 
AA 6 HOH 244 644 247  HOH HOH A . 
AA 6 HOH 245 645 1203 HOH HOH A . 
AA 6 HOH 246 646 1009 HOH HOH A . 
AA 6 HOH 247 647 380  HOH HOH A . 
AA 6 HOH 248 648 1059 HOH HOH A . 
AA 6 HOH 249 649 849  HOH HOH A . 
AA 6 HOH 250 650 1057 HOH HOH A . 
AA 6 HOH 251 651 1006 HOH HOH A . 
AA 6 HOH 252 652 708  HOH HOH A . 
AA 6 HOH 253 653 1074 HOH HOH A . 
AA 6 HOH 254 654 1090 HOH HOH A . 
AA 6 HOH 255 655 514  HOH HOH A . 
AA 6 HOH 256 656 1046 HOH HOH A . 
AA 6 HOH 257 657 828  HOH HOH A . 
AA 6 HOH 258 658 1076 HOH HOH A . 
AA 6 HOH 259 659 987  HOH HOH A . 
AA 6 HOH 260 660 1120 HOH HOH A . 
AA 6 HOH 261 661 630  HOH HOH A . 
AA 6 HOH 262 662 1065 HOH HOH A . 
AA 6 HOH 263 663 857  HOH HOH A . 
AA 6 HOH 264 664 646  HOH HOH A . 
AA 6 HOH 265 665 686  HOH HOH A . 
AA 6 HOH 266 666 1137 HOH HOH A . 
AA 6 HOH 267 667 841  HOH HOH A . 
AA 6 HOH 268 668 917  HOH HOH A . 
AA 6 HOH 269 669 1084 HOH HOH A . 
AA 6 HOH 270 670 761  HOH HOH A . 
AA 6 HOH 271 671 1091 HOH HOH A . 
AA 6 HOH 272 672 474  HOH HOH A . 
AA 6 HOH 273 673 1048 HOH HOH A . 
AA 6 HOH 274 674 1061 HOH HOH A . 
AA 6 HOH 275 675 907  HOH HOH A . 
AA 6 HOH 276 676 785  HOH HOH A . 
AA 6 HOH 277 677 988  HOH HOH A . 
BA 6 HOH 1   401 1105 HOH HOH B . 
BA 6 HOH 2   402 884  HOH HOH B . 
BA 6 HOH 3   403 181  HOH HOH B . 
BA 6 HOH 4   404 861  HOH HOH B . 
BA 6 HOH 5   405 368  HOH HOH B . 
BA 6 HOH 6   406 194  HOH HOH B . 
BA 6 HOH 7   407 1100 HOH HOH B . 
BA 6 HOH 8   408 1108 HOH HOH B . 
BA 6 HOH 9   409 833  HOH HOH B . 
BA 6 HOH 10  410 129  HOH HOH B . 
BA 6 HOH 11  411 545  HOH HOH B . 
BA 6 HOH 12  412 498  HOH HOH B . 
BA 6 HOH 13  413 927  HOH HOH B . 
BA 6 HOH 14  414 483  HOH HOH B . 
BA 6 HOH 15  415 842  HOH HOH B . 
BA 6 HOH 16  416 1109 HOH HOH B . 
BA 6 HOH 17  417 180  HOH HOH B . 
BA 6 HOH 18  418 1018 HOH HOH B . 
BA 6 HOH 19  419 1011 HOH HOH B . 
BA 6 HOH 20  420 936  HOH HOH B . 
BA 6 HOH 21  421 801  HOH HOH B . 
BA 6 HOH 22  422 516  HOH HOH B . 
BA 6 HOH 23  423 241  HOH HOH B . 
BA 6 HOH 24  424 422  HOH HOH B . 
BA 6 HOH 25  425 759  HOH HOH B . 
BA 6 HOH 26  426 324  HOH HOH B . 
BA 6 HOH 27  427 762  HOH HOH B . 
BA 6 HOH 28  428 926  HOH HOH B . 
BA 6 HOH 29  429 871  HOH HOH B . 
BA 6 HOH 30  430 656  HOH HOH B . 
BA 6 HOH 31  431 12   HOH HOH B . 
BA 6 HOH 32  432 100  HOH HOH B . 
BA 6 HOH 33  433 363  HOH HOH B . 
BA 6 HOH 34  434 878  HOH HOH B . 
BA 6 HOH 35  435 756  HOH HOH B . 
BA 6 HOH 36  436 537  HOH HOH B . 
BA 6 HOH 37  437 1017 HOH HOH B . 
BA 6 HOH 38  438 77   HOH HOH B . 
BA 6 HOH 39  439 254  HOH HOH B . 
BA 6 HOH 40  440 515  HOH HOH B . 
BA 6 HOH 41  441 296  HOH HOH B . 
BA 6 HOH 42  442 676  HOH HOH B . 
BA 6 HOH 43  443 345  HOH HOH B . 
BA 6 HOH 44  444 261  HOH HOH B . 
BA 6 HOH 45  445 155  HOH HOH B . 
BA 6 HOH 46  446 770  HOH HOH B . 
BA 6 HOH 47  447 683  HOH HOH B . 
BA 6 HOH 48  448 232  HOH HOH B . 
BA 6 HOH 49  449 171  HOH HOH B . 
BA 6 HOH 50  450 859  HOH HOH B . 
BA 6 HOH 51  451 75   HOH HOH B . 
BA 6 HOH 52  452 995  HOH HOH B . 
BA 6 HOH 53  453 366  HOH HOH B . 
BA 6 HOH 54  454 60   HOH HOH B . 
BA 6 HOH 55  455 747  HOH HOH B . 
BA 6 HOH 56  456 57   HOH HOH B . 
BA 6 HOH 57  457 477  HOH HOH B . 
BA 6 HOH 58  458 328  HOH HOH B . 
BA 6 HOH 59  459 72   HOH HOH B . 
BA 6 HOH 60  460 553  HOH HOH B . 
BA 6 HOH 61  461 220  HOH HOH B . 
BA 6 HOH 62  462 308  HOH HOH B . 
BA 6 HOH 63  463 567  HOH HOH B . 
BA 6 HOH 64  464 574  HOH HOH B . 
BA 6 HOH 65  465 56   HOH HOH B . 
BA 6 HOH 66  466 664  HOH HOH B . 
BA 6 HOH 67  467 831  HOH HOH B . 
BA 6 HOH 68  468 837  HOH HOH B . 
BA 6 HOH 69  469 143  HOH HOH B . 
BA 6 HOH 70  470 361  HOH HOH B . 
BA 6 HOH 71  471 670  HOH HOH B . 
BA 6 HOH 72  472 728  HOH HOH B . 
BA 6 HOH 73  473 283  HOH HOH B . 
BA 6 HOH 74  474 18   HOH HOH B . 
BA 6 HOH 75  475 851  HOH HOH B . 
BA 6 HOH 76  476 409  HOH HOH B . 
BA 6 HOH 77  477 493  HOH HOH B . 
BA 6 HOH 78  478 892  HOH HOH B . 
BA 6 HOH 79  479 133  HOH HOH B . 
BA 6 HOH 80  480 825  HOH HOH B . 
BA 6 HOH 81  481 107  HOH HOH B . 
BA 6 HOH 82  482 1096 HOH HOH B . 
BA 6 HOH 83  483 216  HOH HOH B . 
BA 6 HOH 84  484 38   HOH HOH B . 
BA 6 HOH 85  485 62   HOH HOH B . 
BA 6 HOH 86  486 679  HOH HOH B . 
BA 6 HOH 87  487 124  HOH HOH B . 
BA 6 HOH 88  488 970  HOH HOH B . 
BA 6 HOH 89  489 86   HOH HOH B . 
BA 6 HOH 90  490 207  HOH HOH B . 
BA 6 HOH 91  491 108  HOH HOH B . 
BA 6 HOH 92  492 163  HOH HOH B . 
BA 6 HOH 93  493 182  HOH HOH B . 
BA 6 HOH 94  494 1014 HOH HOH B . 
BA 6 HOH 95  495 138  HOH HOH B . 
BA 6 HOH 96  496 7    HOH HOH B . 
BA 6 HOH 97  497 39   HOH HOH B . 
BA 6 HOH 98  498 818  HOH HOH B . 
BA 6 HOH 99  499 862  HOH HOH B . 
BA 6 HOH 100 500 332  HOH HOH B . 
BA 6 HOH 101 501 623  HOH HOH B . 
BA 6 HOH 102 502 117  HOH HOH B . 
BA 6 HOH 103 503 144  HOH HOH B . 
BA 6 HOH 104 504 25   HOH HOH B . 
BA 6 HOH 105 505 804  HOH HOH B . 
BA 6 HOH 106 506 26   HOH HOH B . 
BA 6 HOH 107 507 1010 HOH HOH B . 
BA 6 HOH 108 508 168  HOH HOH B . 
BA 6 HOH 109 509 67   HOH HOH B . 
BA 6 HOH 110 510 427  HOH HOH B . 
BA 6 HOH 111 511 888  HOH HOH B . 
BA 6 HOH 112 512 68   HOH HOH B . 
BA 6 HOH 113 513 589  HOH HOH B . 
BA 6 HOH 114 514 555  HOH HOH B . 
BA 6 HOH 115 515 139  HOH HOH B . 
BA 6 HOH 116 516 436  HOH HOH B . 
BA 6 HOH 117 517 170  HOH HOH B . 
BA 6 HOH 118 518 15   HOH HOH B . 
BA 6 HOH 119 519 178  HOH HOH B . 
BA 6 HOH 120 520 94   HOH HOH B . 
BA 6 HOH 121 521 579  HOH HOH B . 
BA 6 HOH 122 522 792  HOH HOH B . 
BA 6 HOH 123 523 858  HOH HOH B . 
BA 6 HOH 124 524 212  HOH HOH B . 
BA 6 HOH 125 525 136  HOH HOH B . 
BA 6 HOH 126 526 905  HOH HOH B . 
BA 6 HOH 127 527 583  HOH HOH B . 
BA 6 HOH 128 528 6    HOH HOH B . 
BA 6 HOH 129 529 1012 HOH HOH B . 
BA 6 HOH 130 530 224  HOH HOH B . 
BA 6 HOH 131 531 690  HOH HOH B . 
BA 6 HOH 132 532 1103 HOH HOH B . 
BA 6 HOH 133 533 1001 HOH HOH B . 
BA 6 HOH 134 534 285  HOH HOH B . 
BA 6 HOH 135 535 929  HOH HOH B . 
BA 6 HOH 136 536 620  HOH HOH B . 
BA 6 HOH 137 537 903  HOH HOH B . 
BA 6 HOH 138 538 647  HOH HOH B . 
BA 6 HOH 139 539 645  HOH HOH B . 
BA 6 HOH 140 540 97   HOH HOH B . 
BA 6 HOH 141 541 470  HOH HOH B . 
BA 6 HOH 142 542 716  HOH HOH B . 
BA 6 HOH 143 543 1013 HOH HOH B . 
BA 6 HOH 144 544 1024 HOH HOH B . 
BA 6 HOH 145 545 560  HOH HOH B . 
BA 6 HOH 146 546 633  HOH HOH B . 
BA 6 HOH 147 547 52   HOH HOH B . 
BA 6 HOH 148 548 295  HOH HOH B . 
BA 6 HOH 149 549 174  HOH HOH B . 
BA 6 HOH 150 550 176  HOH HOH B . 
BA 6 HOH 151 551 575  HOH HOH B . 
BA 6 HOH 152 552 800  HOH HOH B . 
BA 6 HOH 153 553 780  HOH HOH B . 
BA 6 HOH 154 554 750  HOH HOH B . 
BA 6 HOH 155 555 634  HOH HOH B . 
BA 6 HOH 156 556 1110 HOH HOH B . 
BA 6 HOH 157 557 116  HOH HOH B . 
BA 6 HOH 158 558 1112 HOH HOH B . 
BA 6 HOH 159 559 120  HOH HOH B . 
BA 6 HOH 160 560 50   HOH HOH B . 
BA 6 HOH 161 561 688  HOH HOH B . 
BA 6 HOH 162 562 358  HOH HOH B . 
BA 6 HOH 163 563 65   HOH HOH B . 
BA 6 HOH 164 564 44   HOH HOH B . 
BA 6 HOH 165 565 377  HOH HOH B . 
BA 6 HOH 166 566 35   HOH HOH B . 
BA 6 HOH 167 567 154  HOH HOH B . 
BA 6 HOH 168 568 264  HOH HOH B . 
BA 6 HOH 169 569 313  HOH HOH B . 
BA 6 HOH 170 570 1098 HOH HOH B . 
BA 6 HOH 171 571 444  HOH HOH B . 
BA 6 HOH 172 572 533  HOH HOH B . 
BA 6 HOH 173 573 1123 HOH HOH B . 
BA 6 HOH 174 574 141  HOH HOH B . 
BA 6 HOH 175 575 27   HOH HOH B . 
BA 6 HOH 176 576 631  HOH HOH B . 
BA 6 HOH 177 577 305  HOH HOH B . 
BA 6 HOH 178 578 227  HOH HOH B . 
BA 6 HOH 179 579 147  HOH HOH B . 
BA 6 HOH 180 580 557  HOH HOH B . 
BA 6 HOH 181 581 321  HOH HOH B . 
BA 6 HOH 182 582 350  HOH HOH B . 
BA 6 HOH 183 583 32   HOH HOH B . 
BA 6 HOH 184 584 680  HOH HOH B . 
BA 6 HOH 185 585 1022 HOH HOH B . 
BA 6 HOH 186 586 609  HOH HOH B . 
BA 6 HOH 187 587 128  HOH HOH B . 
BA 6 HOH 188 588 733  HOH HOH B . 
BA 6 HOH 189 589 401  HOH HOH B . 
BA 6 HOH 190 590 423  HOH HOH B . 
BA 6 HOH 191 591 456  HOH HOH B . 
BA 6 HOH 192 592 648  HOH HOH B . 
BA 6 HOH 193 593 230  HOH HOH B . 
BA 6 HOH 194 594 639  HOH HOH B . 
BA 6 HOH 195 595 223  HOH HOH B . 
BA 6 HOH 196 596 506  HOH HOH B . 
BA 6 HOH 197 597 156  HOH HOH B . 
BA 6 HOH 198 598 349  HOH HOH B . 
BA 6 HOH 199 599 91   HOH HOH B . 
BA 6 HOH 200 600 1051 HOH HOH B . 
BA 6 HOH 201 601 475  HOH HOH B . 
BA 6 HOH 202 602 93   HOH HOH B . 
BA 6 HOH 203 603 749  HOH HOH B . 
BA 6 HOH 204 604 930  HOH HOH B . 
BA 6 HOH 205 605 590  HOH HOH B . 
BA 6 HOH 206 606 935  HOH HOH B . 
BA 6 HOH 207 607 629  HOH HOH B . 
BA 6 HOH 208 608 772  HOH HOH B . 
BA 6 HOH 209 609 814  HOH HOH B . 
BA 6 HOH 210 610 852  HOH HOH B . 
BA 6 HOH 211 611 173  HOH HOH B . 
BA 6 HOH 212 612 491  HOH HOH B . 
BA 6 HOH 213 613 551  HOH HOH B . 
BA 6 HOH 214 614 909  HOH HOH B . 
BA 6 HOH 215 615 210  HOH HOH B . 
BA 6 HOH 216 616 145  HOH HOH B . 
BA 6 HOH 217 617 813  HOH HOH B . 
BA 6 HOH 218 618 195  HOH HOH B . 
BA 6 HOH 219 619 454  HOH HOH B . 
BA 6 HOH 220 620 330  HOH HOH B . 
BA 6 HOH 221 621 1106 HOH HOH B . 
BA 6 HOH 222 622 1021 HOH HOH B . 
BA 6 HOH 223 623 395  HOH HOH B . 
BA 6 HOH 224 624 290  HOH HOH B . 
BA 6 HOH 225 625 910  HOH HOH B . 
BA 6 HOH 226 626 714  HOH HOH B . 
BA 6 HOH 227 627 1016 HOH HOH B . 
BA 6 HOH 228 628 564  HOH HOH B . 
BA 6 HOH 229 629 820  HOH HOH B . 
BA 6 HOH 230 630 983  HOH HOH B . 
BA 6 HOH 231 631 593  HOH HOH B . 
BA 6 HOH 232 632 162  HOH HOH B . 
BA 6 HOH 233 633 1104 HOH HOH B . 
BA 6 HOH 234 634 755  HOH HOH B . 
BA 6 HOH 235 635 678  HOH HOH B . 
BA 6 HOH 236 636 689  HOH HOH B . 
BA 6 HOH 237 637 549  HOH HOH B . 
BA 6 HOH 238 638 672  HOH HOH B . 
BA 6 HOH 239 639 1019 HOH HOH B . 
BA 6 HOH 240 640 437  HOH HOH B . 
BA 6 HOH 241 641 658  HOH HOH B . 
BA 6 HOH 242 642 877  HOH HOH B . 
BA 6 HOH 243 643 1097 HOH HOH B . 
BA 6 HOH 244 644 1094 HOH HOH B . 
BA 6 HOH 245 645 471  HOH HOH B . 
BA 6 HOH 246 646 445  HOH HOH B . 
BA 6 HOH 247 647 710  HOH HOH B . 
BA 6 HOH 248 648 1015 HOH HOH B . 
BA 6 HOH 249 649 384  HOH HOH B . 
BA 6 HOH 250 650 1117 HOH HOH B . 
BA 6 HOH 251 651 1111 HOH HOH B . 
BA 6 HOH 252 652 1101 HOH HOH B . 
BA 6 HOH 253 653 922  HOH HOH B . 
BA 6 HOH 254 654 786  HOH HOH B . 
BA 6 HOH 255 655 1118 HOH HOH B . 
BA 6 HOH 256 656 434  HOH HOH B . 
BA 6 HOH 257 657 1052 HOH HOH B . 
BA 6 HOH 258 658 446  HOH HOH B . 
BA 6 HOH 259 659 736  HOH HOH B . 
BA 6 HOH 260 660 1000 HOH HOH B . 
BA 6 HOH 261 661 827  HOH HOH B . 
BA 6 HOH 262 662 1095 HOH HOH B . 
BA 6 HOH 263 663 1173 HOH HOH B . 
BA 6 HOH 264 664 1072 HOH HOH B . 
BA 6 HOH 265 665 1193 HOH HOH B . 
BA 6 HOH 266 666 591  HOH HOH B . 
BA 6 HOH 267 667 459  HOH HOH B . 
BA 6 HOH 268 668 286  HOH HOH B . 
BA 6 HOH 269 669 1116 HOH HOH B . 
BA 6 HOH 270 670 487  HOH HOH B . 
BA 6 HOH 271 671 1195 HOH HOH B . 
BA 6 HOH 272 672 1114 HOH HOH B . 
BA 6 HOH 273 673 307  HOH HOH B . 
BA 6 HOH 274 674 724  HOH HOH B . 
BA 6 HOH 275 675 472  HOH HOH B . 
BA 6 HOH 276 676 291  HOH HOH B . 
BA 6 HOH 277 677 720  HOH HOH B . 
BA 6 HOH 278 678 622  HOH HOH B . 
BA 6 HOH 279 679 709  HOH HOH B . 
BA 6 HOH 280 680 990  HOH HOH B . 
BA 6 HOH 281 681 934  HOH HOH B . 
BA 6 HOH 282 682 898  HOH HOH B . 
BA 6 HOH 283 683 863  HOH HOH B . 
BA 6 HOH 284 684 718  HOH HOH B . 
BA 6 HOH 285 685 344  HOH HOH B . 
BA 6 HOH 286 686 372  HOH HOH B . 
BA 6 HOH 287 687 573  HOH HOH B . 
BA 6 HOH 288 688 568  HOH HOH B . 
BA 6 HOH 289 689 260  HOH HOH B . 
BA 6 HOH 290 690 696  HOH HOH B . 
BA 6 HOH 291 691 925  HOH HOH B . 
BA 6 HOH 292 692 253  HOH HOH B . 
BA 6 HOH 293 693 601  HOH HOH B . 
BA 6 HOH 294 694 840  HOH HOH B . 
BA 6 HOH 295 695 782  HOH HOH B . 
BA 6 HOH 296 696 550  HOH HOH B . 
BA 6 HOH 297 697 731  HOH HOH B . 
BA 6 HOH 298 698 394  HOH HOH B . 
BA 6 HOH 299 699 374  HOH HOH B . 
BA 6 HOH 300 700 644  HOH HOH B . 
BA 6 HOH 301 701 542  HOH HOH B . 
BA 6 HOH 302 702 921  HOH HOH B . 
BA 6 HOH 303 703 823  HOH HOH B . 
BA 6 HOH 304 704 1115 HOH HOH B . 
BA 6 HOH 305 705 748  HOH HOH B . 
BA 6 HOH 306 706 805  HOH HOH B . 
BA 6 HOH 307 707 231  HOH HOH B . 
BA 6 HOH 308 708 1119 HOH HOH B . 
BA 6 HOH 309 709 777  HOH HOH B . 
BA 6 HOH 310 710 351  HOH HOH B . 
BA 6 HOH 311 711 1102 HOH HOH B . 
BA 6 HOH 312 712 923  HOH HOH B . 
BA 6 HOH 313 713 592  HOH HOH B . 
BA 6 HOH 314 714 319  HOH HOH B . 
BA 6 HOH 315 715 642  HOH HOH B . 
BA 6 HOH 316 716 499  HOH HOH B . 
BA 6 HOH 317 717 399  HOH HOH B . 
BA 6 HOH 318 718 659  HOH HOH B . 
BA 6 HOH 319 719 1023 HOH HOH B . 
BA 6 HOH 320 720 681  HOH HOH B . 
BA 6 HOH 321 721 1099 HOH HOH B . 
BA 6 HOH 322 722 870  HOH HOH B . 
BA 6 HOH 323 723 584  HOH HOH B . 
BA 6 HOH 324 724 421  HOH HOH B . 
BA 6 HOH 325 725 267  HOH HOH B . 
BA 6 HOH 326 726 1121 HOH HOH B . 
BA 6 HOH 327 727 924  HOH HOH B . 
BA 6 HOH 328 728 1122 HOH HOH B . 
BA 6 HOH 329 729 1107 HOH HOH B . 
BA 6 HOH 330 730 703  HOH HOH B . 
BA 6 HOH 331 731 602  HOH HOH B . 
BA 6 HOH 332 732 835  HOH HOH B . 
BA 6 HOH 333 733 625  HOH HOH B . 
BA 6 HOH 334 734 869  HOH HOH B . 
CA 6 HOH 1   401 274  HOH HOH C . 
CA 6 HOH 2   402 1036 HOH HOH C . 
CA 6 HOH 3   403 945  HOH HOH C . 
CA 6 HOH 4   404 964  HOH HOH C . 
CA 6 HOH 5   405 848  HOH HOH C . 
CA 6 HOH 6   406 524  HOH HOH C . 
CA 6 HOH 7   407 605  HOH HOH C . 
CA 6 HOH 8   408 323  HOH HOH C . 
CA 6 HOH 9   409 1145 HOH HOH C . 
CA 6 HOH 10  410 799  HOH HOH C . 
CA 6 HOH 11  411 1157 HOH HOH C . 
CA 6 HOH 12  412 1027 HOH HOH C . 
CA 6 HOH 13  413 531  HOH HOH C . 
CA 6 HOH 14  414 734  HOH HOH C . 
CA 6 HOH 15  415 775  HOH HOH C . 
CA 6 HOH 16  416 1147 HOH HOH C . 
CA 6 HOH 17  417 159  HOH HOH C . 
CA 6 HOH 18  418 1025 HOH HOH C . 
CA 6 HOH 19  419 621  HOH HOH C . 
CA 6 HOH 20  420 937  HOH HOH C . 
CA 6 HOH 21  421 420  HOH HOH C . 
CA 6 HOH 22  422 486  HOH HOH C . 
CA 6 HOH 23  423 1158 HOH HOH C . 
CA 6 HOH 24  424 939  HOH HOH C . 
CA 6 HOH 25  425 213  HOH HOH C . 
CA 6 HOH 26  426 299  HOH HOH C . 
CA 6 HOH 27  427 443  HOH HOH C . 
CA 6 HOH 28  428 980  HOH HOH C . 
CA 6 HOH 29  429 1032 HOH HOH C . 
CA 6 HOH 30  430 126  HOH HOH C . 
CA 6 HOH 31  431 598  HOH HOH C . 
CA 6 HOH 32  432 45   HOH HOH C . 
CA 6 HOH 33  433 669  HOH HOH C . 
CA 6 HOH 34  434 505  HOH HOH C . 
CA 6 HOH 35  435 600  HOH HOH C . 
CA 6 HOH 36  436 509  HOH HOH C . 
CA 6 HOH 37  437 838  HOH HOH C . 
CA 6 HOH 38  438 355  HOH HOH C . 
CA 6 HOH 39  439 177  HOH HOH C . 
CA 6 HOH 40  440 802  HOH HOH C . 
CA 6 HOH 41  441 37   HOH HOH C . 
CA 6 HOH 42  442 82   HOH HOH C . 
CA 6 HOH 43  443 735  HOH HOH C . 
CA 6 HOH 44  444 218  HOH HOH C . 
CA 6 HOH 45  445 490  HOH HOH C . 
CA 6 HOH 46  446 737  HOH HOH C . 
CA 6 HOH 47  447 153  HOH HOH C . 
CA 6 HOH 48  448 558  HOH HOH C . 
CA 6 HOH 49  449 875  HOH HOH C . 
CA 6 HOH 50  450 43   HOH HOH C . 
CA 6 HOH 51  451 1020 HOH HOH C . 
CA 6 HOH 52  452 146  HOH HOH C . 
CA 6 HOH 53  453 175  HOH HOH C . 
CA 6 HOH 54  454 965  HOH HOH C . 
CA 6 HOH 55  455 808  HOH HOH C . 
CA 6 HOH 56  456 1028 HOH HOH C . 
CA 6 HOH 57  457 1152 HOH HOH C . 
CA 6 HOH 58  458 643  HOH HOH C . 
CA 6 HOH 59  459 478  HOH HOH C . 
CA 6 HOH 60  460 556  HOH HOH C . 
CA 6 HOH 61  461 627  HOH HOH C . 
CA 6 HOH 62  462 429  HOH HOH C . 
CA 6 HOH 63  463 815  HOH HOH C . 
CA 6 HOH 64  464 572  HOH HOH C . 
CA 6 HOH 65  465 959  HOH HOH C . 
CA 6 HOH 66  466 552  HOH HOH C . 
CA 6 HOH 67  467 28   HOH HOH C . 
CA 6 HOH 68  468 1154 HOH HOH C . 
CA 6 HOH 69  469 70   HOH HOH C . 
CA 6 HOH 70  470 123  HOH HOH C . 
CA 6 HOH 71  471 191  HOH HOH C . 
CA 6 HOH 72  472 963  HOH HOH C . 
CA 6 HOH 73  473 480  HOH HOH C . 
CA 6 HOH 74  474 809  HOH HOH C . 
CA 6 HOH 75  475 36   HOH HOH C . 
CA 6 HOH 76  476 228  HOH HOH C . 
CA 6 HOH 77  477 779  HOH HOH C . 
CA 6 HOH 78  478 262  HOH HOH C . 
CA 6 HOH 79  479 856  HOH HOH C . 
CA 6 HOH 80  480 30   HOH HOH C . 
CA 6 HOH 81  481 763  HOH HOH C . 
CA 6 HOH 82  482 998  HOH HOH C . 
CA 6 HOH 83  483 1053 HOH HOH C . 
CA 6 HOH 84  484 20   HOH HOH C . 
CA 6 HOH 85  485 152  HOH HOH C . 
CA 6 HOH 86  486 966  HOH HOH C . 
CA 6 HOH 87  487 726  HOH HOH C . 
CA 6 HOH 88  488 41   HOH HOH C . 
CA 6 HOH 89  489 1148 HOH HOH C . 
CA 6 HOH 90  490 717  HOH HOH C . 
CA 6 HOH 91  491 960  HOH HOH C . 
CA 6 HOH 92  492 389  HOH HOH C . 
CA 6 HOH 93  493 638  HOH HOH C . 
CA 6 HOH 94  494 790  HOH HOH C . 
CA 6 HOH 95  495 398  HOH HOH C . 
CA 6 HOH 96  496 576  HOH HOH C . 
CA 6 HOH 97  497 1161 HOH HOH C . 
CA 6 HOH 98  498 684  HOH HOH C . 
CA 6 HOH 99  499 127  HOH HOH C . 
CA 6 HOH 100 500 662  HOH HOH C . 
CA 6 HOH 101 501 496  HOH HOH C . 
CA 6 HOH 102 502 250  HOH HOH C . 
CA 6 HOH 103 503 715  HOH HOH C . 
CA 6 HOH 104 504 289  HOH HOH C . 
CA 6 HOH 105 505 149  HOH HOH C . 
CA 6 HOH 106 506 200  HOH HOH C . 
CA 6 HOH 107 507 562  HOH HOH C . 
CA 6 HOH 108 508 407  HOH HOH C . 
CA 6 HOH 109 509 430  HOH HOH C . 
CA 6 HOH 110 510 303  HOH HOH C . 
CA 6 HOH 111 511 110  HOH HOH C . 
CA 6 HOH 112 512 414  HOH HOH C . 
CA 6 HOH 113 513 961  HOH HOH C . 
CA 6 HOH 114 514 891  HOH HOH C . 
CA 6 HOH 115 515 868  HOH HOH C . 
CA 6 HOH 116 516 453  HOH HOH C . 
CA 6 HOH 117 517 255  HOH HOH C . 
CA 6 HOH 118 518 1149 HOH HOH C . 
CA 6 HOH 119 519 24   HOH HOH C . 
CA 6 HOH 120 520 887  HOH HOH C . 
CA 6 HOH 121 521 208  HOH HOH C . 
CA 6 HOH 122 522 209  HOH HOH C . 
CA 6 HOH 123 523 304  HOH HOH C . 
CA 6 HOH 124 524 1166 HOH HOH C . 
CA 6 HOH 125 525 461  HOH HOH C . 
CA 6 HOH 126 526 16   HOH HOH C . 
CA 6 HOH 127 527 1162 HOH HOH C . 
CA 6 HOH 128 528 122  HOH HOH C . 
CA 6 HOH 129 529 76   HOH HOH C . 
CA 6 HOH 130 530 876  HOH HOH C . 
CA 6 HOH 131 531 54   HOH HOH C . 
CA 6 HOH 132 532 249  HOH HOH C . 
CA 6 HOH 133 533 13   HOH HOH C . 
CA 6 HOH 134 534 940  HOH HOH C . 
CA 6 HOH 135 535 946  HOH HOH C . 
CA 6 HOH 136 536 608  HOH HOH C . 
CA 6 HOH 137 537 334  HOH HOH C . 
CA 6 HOH 138 538 161  HOH HOH C . 
CA 6 HOH 139 539 561  HOH HOH C . 
CA 6 HOH 140 540 325  HOH HOH C . 
CA 6 HOH 141 541 268  HOH HOH C . 
CA 6 HOH 142 542 34   HOH HOH C . 
CA 6 HOH 143 543 788  HOH HOH C . 
CA 6 HOH 144 544 525  HOH HOH C . 
CA 6 HOH 145 545 66   HOH HOH C . 
CA 6 HOH 146 546 489  HOH HOH C . 
CA 6 HOH 147 547 867  HOH HOH C . 
CA 6 HOH 148 548 864  HOH HOH C . 
CA 6 HOH 149 549 121  HOH HOH C . 
CA 6 HOH 150 550 424  HOH HOH C . 
CA 6 HOH 151 551 512  HOH HOH C . 
CA 6 HOH 152 552 371  HOH HOH C . 
CA 6 HOH 153 553 956  HOH HOH C . 
CA 6 HOH 154 554 238  HOH HOH C . 
CA 6 HOH 155 555 854  HOH HOH C . 
CA 6 HOH 156 556 236  HOH HOH C . 
CA 6 HOH 157 557 1031 HOH HOH C . 
CA 6 HOH 158 558 356  HOH HOH C . 
CA 6 HOH 159 559 98   HOH HOH C . 
CA 6 HOH 160 560 237  HOH HOH C . 
CA 6 HOH 161 561 586  HOH HOH C . 
CA 6 HOH 162 562 347  HOH HOH C . 
CA 6 HOH 163 563 301  HOH HOH C . 
CA 6 HOH 164 564 981  HOH HOH C . 
CA 6 HOH 165 565 449  HOH HOH C . 
CA 6 HOH 166 566 1160 HOH HOH C . 
CA 6 HOH 167 567 503  HOH HOH C . 
CA 6 HOH 168 568 1142 HOH HOH C . 
CA 6 HOH 169 569 441  HOH HOH C . 
CA 6 HOH 170 570 1045 HOH HOH C . 
CA 6 HOH 171 571 410  HOH HOH C . 
CA 6 HOH 172 572 333  HOH HOH C . 
CA 6 HOH 173 573 89   HOH HOH C . 
CA 6 HOH 174 574 1125 HOH HOH C . 
CA 6 HOH 175 575 1026 HOH HOH C . 
CA 6 HOH 176 576 1164 HOH HOH C . 
CA 6 HOH 177 577 1159 HOH HOH C . 
CA 6 HOH 178 578 500  HOH HOH C . 
CA 6 HOH 179 579 205  HOH HOH C . 
CA 6 HOH 180 580 1030 HOH HOH C . 
CA 6 HOH 181 581 942  HOH HOH C . 
CA 6 HOH 182 582 1167 HOH HOH C . 
CA 6 HOH 183 583 279  HOH HOH C . 
CA 6 HOH 184 584 1130 HOH HOH C . 
CA 6 HOH 185 585 685  HOH HOH C . 
CA 6 HOH 186 586 719  HOH HOH C . 
CA 6 HOH 187 587 613  HOH HOH C . 
CA 6 HOH 188 588 744  HOH HOH C . 
CA 6 HOH 189 589 1156 HOH HOH C . 
CA 6 HOH 190 590 1129 HOH HOH C . 
CA 6 HOH 191 591 896  HOH HOH C . 
CA 6 HOH 192 592 654  HOH HOH C . 
CA 6 HOH 193 593 188  HOH HOH C . 
CA 6 HOH 194 594 958  HOH HOH C . 
CA 6 HOH 195 595 661  HOH HOH C . 
CA 6 HOH 196 596 1033 HOH HOH C . 
CA 6 HOH 197 597 341  HOH HOH C . 
CA 6 HOH 198 598 1113 HOH HOH C . 
CA 6 HOH 199 599 651  HOH HOH C . 
CA 6 HOH 200 600 1151 HOH HOH C . 
CA 6 HOH 201 601 497  HOH HOH C . 
CA 6 HOH 202 602 169  HOH HOH C . 
CA 6 HOH 203 603 798  HOH HOH C . 
CA 6 HOH 204 604 653  HOH HOH C . 
CA 6 HOH 205 605 612  HOH HOH C . 
CA 6 HOH 206 606 947  HOH HOH C . 
CA 6 HOH 207 607 776  HOH HOH C . 
CA 6 HOH 208 608 1029 HOH HOH C . 
CA 6 HOH 209 609 272  HOH HOH C . 
CA 6 HOH 210 610 468  HOH HOH C . 
CA 6 HOH 211 611 582  HOH HOH C . 
CA 6 HOH 212 612 1034 HOH HOH C . 
CA 6 HOH 213 613 1134 HOH HOH C . 
CA 6 HOH 214 614 378  HOH HOH C . 
CA 6 HOH 215 615 894  HOH HOH C . 
CA 6 HOH 216 616 412  HOH HOH C . 
CA 6 HOH 217 617 393  HOH HOH C . 
CA 6 HOH 218 618 1150 HOH HOH C . 
CA 6 HOH 219 619 300  HOH HOH C . 
CA 6 HOH 220 620 1128 HOH HOH C . 
CA 6 HOH 221 621 1054 HOH HOH C . 
CA 6 HOH 222 622 677  HOH HOH C . 
CA 6 HOH 223 623 649  HOH HOH C . 
CA 6 HOH 224 624 1143 HOH HOH C . 
CA 6 HOH 225 625 962  HOH HOH C . 
CA 6 HOH 226 626 1131 HOH HOH C . 
CA 6 HOH 227 627 1141 HOH HOH C . 
CA 6 HOH 228 628 1155 HOH HOH C . 
CA 6 HOH 229 629 1007 HOH HOH C . 
CA 6 HOH 230 630 914  HOH HOH C . 
CA 6 HOH 231 631 954  HOH HOH C . 
CA 6 HOH 232 632 1127 HOH HOH C . 
CA 6 HOH 233 633 476  HOH HOH C . 
CA 6 HOH 234 634 665  HOH HOH C . 
CA 6 HOH 235 635 1124 HOH HOH C . 
CA 6 HOH 236 636 845  HOH HOH C . 
CA 6 HOH 237 637 1055 HOH HOH C . 
CA 6 HOH 238 638 695  HOH HOH C . 
CA 6 HOH 239 639 1035 HOH HOH C . 
CA 6 HOH 240 640 819  HOH HOH C . 
CA 6 HOH 241 641 953  HOH HOH C . 
CA 6 HOH 242 642 873  HOH HOH C . 
CA 6 HOH 243 643 1146 HOH HOH C . 
CA 6 HOH 244 644 1138 HOH HOH C . 
CA 6 HOH 245 645 1139 HOH HOH C . 
CA 6 HOH 246 646 704  HOH HOH C . 
CA 6 HOH 247 647 309  HOH HOH C . 
CA 6 HOH 248 648 1163 HOH HOH C . 
CA 6 HOH 249 649 530  HOH HOH C . 
CA 6 HOH 250 650 599  HOH HOH C . 
CA 6 HOH 251 651 1136 HOH HOH C . 
CA 6 HOH 252 652 931  HOH HOH C . 
CA 6 HOH 253 653 1165 HOH HOH C . 
CA 6 HOH 254 654 806  HOH HOH C . 
CA 6 HOH 255 655 528  HOH HOH C . 
CA 6 HOH 256 656 1197 HOH HOH C . 
CA 6 HOH 257 657 226  HOH HOH C . 
CA 6 HOH 258 658 944  HOH HOH C . 
CA 6 HOH 259 659 547  HOH HOH C . 
CA 6 HOH 260 660 880  HOH HOH C . 
CA 6 HOH 261 661 442  HOH HOH C . 
CA 6 HOH 262 662 546  HOH HOH C . 
CA 6 HOH 263 663 957  HOH HOH C . 
CA 6 HOH 264 664 1132 HOH HOH C . 
CA 6 HOH 265 665 943  HOH HOH C . 
CA 6 HOH 266 666 529  HOH HOH C . 
CA 6 HOH 267 667 1153 HOH HOH C . 
CA 6 HOH 268 668 706  HOH HOH C . 
CA 6 HOH 269 669 1140 HOH HOH C . 
CA 6 HOH 270 670 513  HOH HOH C . 
CA 6 HOH 271 671 1135 HOH HOH C . 
CA 6 HOH 272 672 517  HOH HOH C . 
CA 6 HOH 273 673 595  HOH HOH C . 
CA 6 HOH 274 674 1126 HOH HOH C . 
CA 6 HOH 275 675 783  HOH HOH C . 
CA 6 HOH 276 676 1133 HOH HOH C . 
DA 6 HOH 1   401 418  HOH HOH D . 
DA 6 HOH 2   402 982  HOH HOH D . 
DA 6 HOH 3   403 1208 HOH HOH D . 
DA 6 HOH 4   404 787  HOH HOH D . 
DA 6 HOH 5   405 511  HOH HOH D . 
DA 6 HOH 6   406 462  HOH HOH D . 
DA 6 HOH 7   407 111  HOH HOH D . 
DA 6 HOH 8   408 882  HOH HOH D . 
DA 6 HOH 9   409 266  HOH HOH D . 
DA 6 HOH 10  410 1176 HOH HOH D . 
DA 6 HOH 11  411 532  HOH HOH D . 
DA 6 HOH 12  412 640  HOH HOH D . 
DA 6 HOH 13  413 431  HOH HOH D . 
DA 6 HOH 14  414 738  HOH HOH D . 
DA 6 HOH 15  415 1191 HOH HOH D . 
DA 6 HOH 16  416 270  HOH HOH D . 
DA 6 HOH 17  417 388  HOH HOH D . 
DA 6 HOH 18  418 832  HOH HOH D . 
DA 6 HOH 19  419 1181 HOH HOH D . 
DA 6 HOH 20  420 758  HOH HOH D . 
DA 6 HOH 21  421 784  HOH HOH D . 
DA 6 HOH 22  422 691  HOH HOH D . 
DA 6 HOH 23  423 481  HOH HOH D . 
DA 6 HOH 24  424 886  HOH HOH D . 
DA 6 HOH 25  425 130  HOH HOH D . 
DA 6 HOH 26  426 150  HOH HOH D . 
DA 6 HOH 27  427 753  HOH HOH D . 
DA 6 HOH 28  428 14   HOH HOH D . 
DA 6 HOH 29  429 402  HOH HOH D . 
DA 6 HOH 30  430 1198 HOH HOH D . 
DA 6 HOH 31  431 508  HOH HOH D . 
DA 6 HOH 32  432 294  HOH HOH D . 
DA 6 HOH 33  433 571  HOH HOH D . 
DA 6 HOH 34  434 151  HOH HOH D . 
DA 6 HOH 35  435 1144 HOH HOH D . 
DA 6 HOH 36  436 975  HOH HOH D . 
DA 6 HOH 37  437 912  HOH HOH D . 
DA 6 HOH 38  438 367  HOH HOH D . 
DA 6 HOH 39  439 298  HOH HOH D . 
DA 6 HOH 40  440 928  HOH HOH D . 
DA 6 HOH 41  441 275  HOH HOH D . 
DA 6 HOH 42  442 1041 HOH HOH D . 
DA 6 HOH 43  443 59   HOH HOH D . 
DA 6 HOH 44  444 932  HOH HOH D . 
DA 6 HOH 45  445 329  HOH HOH D . 
DA 6 HOH 46  446 343  HOH HOH D . 
DA 6 HOH 47  447 969  HOH HOH D . 
DA 6 HOH 48  448 797  HOH HOH D . 
DA 6 HOH 49  449 883  HOH HOH D . 
DA 6 HOH 50  450 10   HOH HOH D . 
DA 6 HOH 51  451 754  HOH HOH D . 
DA 6 HOH 52  452 365  HOH HOH D . 
DA 6 HOH 53  453 1194 HOH HOH D . 
DA 6 HOH 54  454 288  HOH HOH D . 
DA 6 HOH 55  455 1202 HOH HOH D . 
DA 6 HOH 56  456 271  HOH HOH D . 
DA 6 HOH 57  457 78   HOH HOH D . 
DA 6 HOH 58  458 199  HOH HOH D . 
DA 6 HOH 59  459 369  HOH HOH D . 
DA 6 HOH 60  460 96   HOH HOH D . 
DA 6 HOH 61  461 619  HOH HOH D . 
DA 6 HOH 62  462 836  HOH HOH D . 
DA 6 HOH 63  463 184  HOH HOH D . 
DA 6 HOH 64  464 977  HOH HOH D . 
DA 6 HOH 65  465 390  HOH HOH D . 
DA 6 HOH 66  466 890  HOH HOH D . 
DA 6 HOH 67  467 636  HOH HOH D . 
DA 6 HOH 68  468 109  HOH HOH D . 
DA 6 HOH 69  469 578  HOH HOH D . 
DA 6 HOH 70  470 938  HOH HOH D . 
DA 6 HOH 71  471 1182 HOH HOH D . 
DA 6 HOH 72  472 713  HOH HOH D . 
DA 6 HOH 73  473 234  HOH HOH D . 
DA 6 HOH 74  474 450  HOH HOH D . 
DA 6 HOH 75  475 55   HOH HOH D . 
DA 6 HOH 76  476 725  HOH HOH D . 
DA 6 HOH 77  477 974  HOH HOH D . 
DA 6 HOH 78  478 115  HOH HOH D . 
DA 6 HOH 79  479 8    HOH HOH D . 
DA 6 HOH 80  480 692  HOH HOH D . 
DA 6 HOH 81  481 17   HOH HOH D . 
DA 6 HOH 82  482 112  HOH HOH D . 
DA 6 HOH 83  483 522  HOH HOH D . 
DA 6 HOH 84  484 9    HOH HOH D . 
DA 6 HOH 85  485 251  HOH HOH D . 
DA 6 HOH 86  486 1201 HOH HOH D . 
DA 6 HOH 87  487 90   HOH HOH D . 
DA 6 HOH 88  488 81   HOH HOH D . 
DA 6 HOH 89  489 33   HOH HOH D . 
DA 6 HOH 90  490 164  HOH HOH D . 
DA 6 HOH 91  491 157  HOH HOH D . 
DA 6 HOH 92  492 74   HOH HOH D . 
DA 6 HOH 93  493 336  HOH HOH D . 
DA 6 HOH 94  494 135  HOH HOH D . 
DA 6 HOH 95  495 1192 HOH HOH D . 
DA 6 HOH 96  496 92   HOH HOH D . 
DA 6 HOH 97  497 280  HOH HOH D . 
DA 6 HOH 98  498 812  HOH HOH D . 
DA 6 HOH 99  499 105  HOH HOH D . 
DA 6 HOH 100 500 320  HOH HOH D . 
DA 6 HOH 101 501 376  HOH HOH D . 
DA 6 HOH 102 502 142  HOH HOH D . 
DA 6 HOH 103 503 48   HOH HOH D . 
DA 6 HOH 104 504 22   HOH HOH D . 
DA 6 HOH 105 505 1178 HOH HOH D . 
DA 6 HOH 106 506 650  HOH HOH D . 
DA 6 HOH 107 507 426  HOH HOH D . 
DA 6 HOH 108 508 114  HOH HOH D . 
DA 6 HOH 109 509 391  HOH HOH D . 
DA 6 HOH 110 510 538  HOH HOH D . 
DA 6 HOH 111 511 118  HOH HOH D . 
DA 6 HOH 112 512 1188 HOH HOH D . 
DA 6 HOH 113 513 29   HOH HOH D . 
DA 6 HOH 114 514 2    HOH HOH D . 
DA 6 HOH 115 515 172  HOH HOH D . 
DA 6 HOH 116 516 125  HOH HOH D . 
DA 6 HOH 117 517 1039 HOH HOH D . 
DA 6 HOH 118 518 527  HOH HOH D . 
DA 6 HOH 119 519 306  HOH HOH D . 
DA 6 HOH 120 520 675  HOH HOH D . 
DA 6 HOH 121 521 447  HOH HOH D . 
DA 6 HOH 122 522 488  HOH HOH D . 
DA 6 HOH 123 523 885  HOH HOH D . 
DA 6 HOH 124 524 834  HOH HOH D . 
DA 6 HOH 125 525 359  HOH HOH D . 
DA 6 HOH 126 526 131  HOH HOH D . 
DA 6 HOH 127 527 140  HOH HOH D . 
DA 6 HOH 128 528 265  HOH HOH D . 
DA 6 HOH 129 529 132  HOH HOH D . 
DA 6 HOH 130 530 387  HOH HOH D . 
DA 6 HOH 131 531 933  HOH HOH D . 
DA 6 HOH 132 532 379  HOH HOH D . 
DA 6 HOH 133 533 73   HOH HOH D . 
DA 6 HOH 134 534 520  HOH HOH D . 
DA 6 HOH 135 535 712  HOH HOH D . 
DA 6 HOH 136 536 1169 HOH HOH D . 
DA 6 HOH 137 537 101  HOH HOH D . 
DA 6 HOH 138 538 635  HOH HOH D . 
DA 6 HOH 139 539 297  HOH HOH D . 
DA 6 HOH 140 540 370  HOH HOH D . 
DA 6 HOH 141 541 707  HOH HOH D . 
DA 6 HOH 142 542 950  HOH HOH D . 
DA 6 HOH 143 543 433  HOH HOH D . 
DA 6 HOH 144 544 222  HOH HOH D . 
DA 6 HOH 145 545 1043 HOH HOH D . 
DA 6 HOH 146 546 69   HOH HOH D . 
DA 6 HOH 147 547 214  HOH HOH D . 
DA 6 HOH 148 548 760  HOH HOH D . 
DA 6 HOH 149 549 693  HOH HOH D . 
DA 6 HOH 150 550 88   HOH HOH D . 
DA 6 HOH 151 551 277  HOH HOH D . 
DA 6 HOH 152 552 204  HOH HOH D . 
DA 6 HOH 153 553 327  HOH HOH D . 
DA 6 HOH 154 554 817  HOH HOH D . 
DA 6 HOH 155 555 616  HOH HOH D . 
DA 6 HOH 156 556 518  HOH HOH D . 
DA 6 HOH 157 557 1184 HOH HOH D . 
DA 6 HOH 158 558 773  HOH HOH D . 
DA 6 HOH 159 559 364  HOH HOH D . 
DA 6 HOH 160 560 416  HOH HOH D . 
DA 6 HOH 161 561 397  HOH HOH D . 
DA 6 HOH 162 562 79   HOH HOH D . 
DA 6 HOH 163 563 501  HOH HOH D . 
DA 6 HOH 164 564 193  HOH HOH D . 
DA 6 HOH 165 565 53   HOH HOH D . 
DA 6 HOH 166 566 1185 HOH HOH D . 
DA 6 HOH 167 567 464  HOH HOH D . 
DA 6 HOH 168 568 63   HOH HOH D . 
DA 6 HOH 169 569 1180 HOH HOH D . 
DA 6 HOH 170 570 941  HOH HOH D . 
DA 6 HOH 171 571 160  HOH HOH D . 
DA 6 HOH 172 572 1037 HOH HOH D . 
DA 6 HOH 173 573 158  HOH HOH D . 
DA 6 HOH 174 574 284  HOH HOH D . 
DA 6 HOH 175 575 3    HOH HOH D . 
DA 6 HOH 176 576 949  HOH HOH D . 
DA 6 HOH 177 577 1172 HOH HOH D . 
DA 6 HOH 178 578 606  HOH HOH D . 
DA 6 HOH 179 579 383  HOH HOH D . 
DA 6 HOH 180 580 373  HOH HOH D . 
DA 6 HOH 181 581 821  HOH HOH D . 
DA 6 HOH 182 582 206  HOH HOH D . 
DA 6 HOH 183 583 494  HOH HOH D . 
DA 6 HOH 184 584 1177 HOH HOH D . 
DA 6 HOH 185 585 1168 HOH HOH D . 
DA 6 HOH 186 586 46   HOH HOH D . 
DA 6 HOH 187 587 897  HOH HOH D . 
DA 6 HOH 188 588 202  HOH HOH D . 
DA 6 HOH 189 589 257  HOH HOH D . 
DA 6 HOH 190 590 781  HOH HOH D . 
DA 6 HOH 191 591 1174 HOH HOH D . 
DA 6 HOH 192 592 95   HOH HOH D . 
DA 6 HOH 193 593 346  HOH HOH D . 
DA 6 HOH 194 594 440  HOH HOH D . 
DA 6 HOH 195 595 607  HOH HOH D . 
DA 6 HOH 196 596 655  HOH HOH D . 
DA 6 HOH 197 597 225  HOH HOH D . 
DA 6 HOH 198 598 403  HOH HOH D . 
DA 6 HOH 199 599 316  HOH HOH D . 
DA 6 HOH 200 600 1207 HOH HOH D . 
DA 6 HOH 201 601 847  HOH HOH D . 
DA 6 HOH 202 602 269  HOH HOH D . 
DA 6 HOH 203 603 335  HOH HOH D . 
DA 6 HOH 204 604 221  HOH HOH D . 
DA 6 HOH 205 605 229  HOH HOH D . 
DA 6 HOH 206 606 581  HOH HOH D . 
DA 6 HOH 207 607 502  HOH HOH D . 
DA 6 HOH 208 608 1056 HOH HOH D . 
DA 6 HOH 209 609 881  HOH HOH D . 
DA 6 HOH 210 610 235  HOH HOH D . 
DA 6 HOH 211 611 451  HOH HOH D . 
DA 6 HOH 212 612 281  HOH HOH D . 
DA 6 HOH 213 613 1186 HOH HOH D . 
DA 6 HOH 214 614 392  HOH HOH D . 
DA 6 HOH 215 615 540  HOH HOH D . 
DA 6 HOH 216 616 751  HOH HOH D . 
DA 6 HOH 217 617 103  HOH HOH D . 
DA 6 HOH 218 618 495  HOH HOH D . 
DA 6 HOH 219 619 342  HOH HOH D . 
DA 6 HOH 220 620 243  HOH HOH D . 
DA 6 HOH 221 621 137  HOH HOH D . 
DA 6 HOH 222 622 666  HOH HOH D . 
DA 6 HOH 223 623 535  HOH HOH D . 
DA 6 HOH 224 624 248  HOH HOH D . 
DA 6 HOH 225 625 617  HOH HOH D . 
DA 6 HOH 226 626 469  HOH HOH D . 
DA 6 HOH 227 627 360  HOH HOH D . 
DA 6 HOH 228 628 219  HOH HOH D . 
DA 6 HOH 229 629 569  HOH HOH D . 
DA 6 HOH 230 630 166  HOH HOH D . 
DA 6 HOH 231 631 293  HOH HOH D . 
DA 6 HOH 232 632 846  HOH HOH D . 
DA 6 HOH 233 633 386  HOH HOH D . 
DA 6 HOH 234 634 967  HOH HOH D . 
DA 6 HOH 235 635 730  HOH HOH D . 
DA 6 HOH 236 636 757  HOH HOH D . 
DA 6 HOH 237 637 457  HOH HOH D . 
DA 6 HOH 238 638 492  HOH HOH D . 
DA 6 HOH 239 639 425  HOH HOH D . 
DA 6 HOH 240 640 952  HOH HOH D . 
DA 6 HOH 241 641 791  HOH HOH D . 
DA 6 HOH 242 642 1190 HOH HOH D . 
DA 6 HOH 243 643 417  HOH HOH D . 
DA 6 HOH 244 644 463  HOH HOH D . 
DA 6 HOH 245 645 948  HOH HOH D . 
DA 6 HOH 246 646 811  HOH HOH D . 
DA 6 HOH 247 647 742  HOH HOH D . 
DA 6 HOH 248 648 879  HOH HOH D . 
DA 6 HOH 249 649 994  HOH HOH D . 
DA 6 HOH 250 650 746  HOH HOH D . 
DA 6 HOH 251 651 765  HOH HOH D . 
DA 6 HOH 252 652 465  HOH HOH D . 
DA 6 HOH 253 653 1189 HOH HOH D . 
DA 6 HOH 254 654 972  HOH HOH D . 
DA 6 HOH 255 655 968  HOH HOH D . 
DA 6 HOH 256 656 610  HOH HOH D . 
DA 6 HOH 257 657 1196 HOH HOH D . 
DA 6 HOH 258 658 1175 HOH HOH D . 
DA 6 HOH 259 659 411  HOH HOH D . 
DA 6 HOH 260 660 774  HOH HOH D . 
DA 6 HOH 261 661 976  HOH HOH D . 
DA 6 HOH 262 662 479  HOH HOH D . 
DA 6 HOH 263 663 1199 HOH HOH D . 
DA 6 HOH 264 664 682  HOH HOH D . 
DA 6 HOH 265 665 448  HOH HOH D . 
DA 6 HOH 266 666 1038 HOH HOH D . 
DA 6 HOH 267 667 810  HOH HOH D . 
DA 6 HOH 268 668 764  HOH HOH D . 
DA 6 HOH 269 669 244  HOH HOH D . 
DA 6 HOH 270 670 322  HOH HOH D . 
DA 6 HOH 271 671 278  HOH HOH D . 
DA 6 HOH 272 672 1206 HOH HOH D . 
DA 6 HOH 273 673 252  HOH HOH D . 
DA 6 HOH 274 674 918  HOH HOH D . 
DA 6 HOH 275 675 331  HOH HOH D . 
DA 6 HOH 276 676 632  HOH HOH D . 
DA 6 HOH 277 677 829  HOH HOH D . 
DA 6 HOH 278 678 657  HOH HOH D . 
DA 6 HOH 279 679 611  HOH HOH D . 
DA 6 HOH 280 680 796  HOH HOH D . 
DA 6 HOH 281 681 1187 HOH HOH D . 
DA 6 HOH 282 682 604  HOH HOH D . 
DA 6 HOH 283 683 1183 HOH HOH D . 
DA 6 HOH 284 684 521  HOH HOH D . 
DA 6 HOH 285 685 971  HOH HOH D . 
DA 6 HOH 286 686 432  HOH HOH D . 
DA 6 HOH 287 687 1171 HOH HOH D . 
DA 6 HOH 288 688 467  HOH HOH D . 
DA 6 HOH 289 689 700  HOH HOH D . 
DA 6 HOH 290 690 473  HOH HOH D . 
DA 6 HOH 291 691 507  HOH HOH D . 
DA 6 HOH 292 692 1040 HOH HOH D . 
DA 6 HOH 293 693 526  HOH HOH D . 
DA 6 HOH 294 694 415  HOH HOH D . 
DA 6 HOH 295 695 951  HOH HOH D . 
DA 6 HOH 296 696 741  HOH HOH D . 
DA 6 HOH 297 697 580  HOH HOH D . 
DA 6 HOH 298 698 1200 HOH HOH D . 
DA 6 HOH 299 699 326  HOH HOH D . 
DA 6 HOH 300 700 860  HOH HOH D . 
DA 6 HOH 301 701 1042 HOH HOH D . 
DA 6 HOH 302 702 318  HOH HOH D . 
DA 6 HOH 303 703 1170 HOH HOH D . 
DA 6 HOH 304 704 539  HOH HOH D . 
DA 6 HOH 305 705 973  HOH HOH D . 
DA 6 HOH 306 706 667  HOH HOH D . 
DA 6 HOH 307 707 458  HOH HOH D . 
DA 6 HOH 308 708 1204 HOH HOH D . 
DA 6 HOH 309 709 240  HOH HOH D . 
DA 6 HOH 310 710 337  HOH HOH D . 
DA 6 HOH 311 711 843  HOH HOH D . 
DA 6 HOH 312 712 1205 HOH HOH D . 
DA 6 HOH 313 713 273  HOH HOH D . 
DA 6 HOH 314 714 739  HOH HOH D . 
DA 6 HOH 315 715 239  HOH HOH D . 
DA 6 HOH 316 716 752  HOH HOH D . 
DA 6 HOH 317 717 287  HOH HOH D . 
DA 6 HOH 318 718 570  HOH HOH D . 
DA 6 HOH 319 719 577  HOH HOH D . 
DA 6 HOH 320 720 850  HOH HOH D . 
DA 6 HOH 321 721 1179 HOH HOH D . 
DA 6 HOH 322 722 866  HOH HOH D . 
DA 6 HOH 323 723 826  HOH HOH D . 
DA 6 HOH 324 724 874  HOH HOH D . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1 1 Y 1 C ASP 235 ? CB  ? C ASP 235 CB  
2 1 Y 1 C ASP 235 ? CG  ? C ASP 235 CG  
3 1 Y 1 C ASP 235 ? OD1 ? C ASP 235 OD1 
4 1 Y 1 C ASP 235 ? OD2 ? C ASP 235 OD2 
# 
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       ? ? ? 3.2.19   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                   108.760 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     5LL9 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     77.298 
_cell.length_a_esd                 ? 
_cell.length_b                     73.887 
_cell.length_b_esd                 ? 
_cell.length_c                     91.285 
_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                         5LL9 
_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                   5LL9 
_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            2.06 
_exptl_crystal.density_method              ? 
_exptl_crystal.density_percent_sol         39.8 
_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), 0.2M ammonium sulfate and 30% 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' 
_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            ? 
_reflns.entry_id                         5LL9 
_reflns.data_reduction_details           ? 
_reflns.data_reduction_method            ? 
_reflns.d_resolution_high                1.450 
_reflns.d_resolution_low                 86.436 
_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                       170401 
_reflns.number_obs                       170401 
_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             99.100 
_reflns.R_free_details                   ? 
_reflns.Rmerge_F_all                     ? 
_reflns.Rmerge_F_obs                     ? 
_reflns.Friedel_coverage                 ? 
_reflns.number_gt                        ? 
_reflns.threshold_expression             ? 
_reflns.pdbx_redundancy                  6.900 
_reflns.pdbx_Rmerge_I_obs                0.045 
_reflns.pdbx_Rmerge_I_all                ? 
_reflns.pdbx_Rsym_value                  0.045 
_reflns.pdbx_netI_over_av_sigmaI         11.350 
_reflns.pdbx_netI_over_sigmaI            21.800 
_reflns.pdbx_res_netI_over_av_sigmaI_2   ? 
_reflns.pdbx_res_netI_over_sigmaI_2      ? 
_reflns.pdbx_chi_squared                 ? 
_reflns.pdbx_scaling_rejects             ? 
_reflns.pdbx_d_res_high_opt              ? 
_reflns.pdbx_d_res_low_opt               ? 
_reflns.pdbx_d_res_opt_method            ? 
_reflns.phase_calculation_details        ? 
_reflns.pdbx_Rrim_I_all                  0.054 
_reflns.pdbx_Rpim_I_all                  0.020 
_reflns.pdbx_d_opt                       ? 
_reflns.pdbx_number_measured_all         1174019 
_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 
1.450 1.530  ? 1.900  ? ? ? ? ? 99.200 ? ? ? ? 0.414 ? ? ? ? ? ? ? ? 6.900 ? ? ? ? ? ? ? 1  1 ? ? 
1.530 1.620  ? 2.800  ? ? ? ? ? 98.500 ? ? ? ? 0.274 ? ? ? ? ? ? ? ? 6.500 ? ? ? ? ? ? ? 2  1 ? ? 
1.620 1.730  ? 4.300  ? ? ? ? ? 99.500 ? ? ? ? 0.180 ? ? ? ? ? ? ? ? 7.000 ? ? ? ? ? ? ? 3  1 ? ? 
1.730 1.870  ? 6.600  ? ? ? ? ? 99.200 ? ? ? ? 0.114 ? ? ? ? ? ? ? ? 7.000 ? ? ? ? ? ? ? 4  1 ? ? 
1.870 2.050  ? 10.100 ? ? ? ? ? 98.900 ? ? ? ? 0.072 ? ? ? ? ? ? ? ? 6.700 ? ? ? ? ? ? ? 5  1 ? ? 
2.050 2.290  ? 14.300 ? ? ? ? ? 99.400 ? ? ? ? 0.050 ? ? ? ? ? ? ? ? 7.100 ? ? ? ? ? ? ? 6  1 ? ? 
2.290 2.650  ? 17.900 ? ? ? ? ? 99.300 ? ? ? ? 0.038 ? ? ? ? ? ? ? ? 7.100 ? ? ? ? ? ? ? 7  1 ? ? 
2.650 3.240  ? 21.300 ? ? ? ? ? 98.700 ? ? ? ? 0.029 ? ? ? ? ? ? ? ? 6.700 ? ? ? ? ? ? ? 8  1 ? ? 
3.240 4.590  ? 25.100 ? ? ? ? ? 99.700 ? ? ? ? 0.022 ? ? ? ? ? ? ? ? 7.200 ? ? ? ? ? ? ? 9  1 ? ? 
4.590 86.436 ? 18.100 ? ? ? ? ? 98.900 ? ? ? ? 0.022 ? ? ? ? ? ? ? ? 6.700 ? ? ? ? ? ? ? 10 1 ? ? 
# 
_refine.aniso_B[1][1]                            -0.2300 
_refine.aniso_B[1][2]                            0.0000 
_refine.aniso_B[1][3]                            0.4100 
_refine.aniso_B[2][2]                            0.2200 
_refine.aniso_B[2][3]                            0.0000 
_refine.aniso_B[3][3]                            0.2700 
_refine.B_iso_max                                69.140 
_refine.B_iso_mean                               17.1770 
_refine.B_iso_min                                5.630 
_refine.correlation_coeff_Fo_to_Fc               0.9700 
_refine.correlation_coeff_Fo_to_Fc_free          0.9590 
_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                                 5LL9 
_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                            1.4500 
_refine.ls_d_res_low                             73.1900 
_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                     153411 
_refine.ls_number_reflns_R_free                  16964 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.0300 
_refine.ls_percent_reflns_R_free                 10.0000 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1742 
_refine.ls_R_factor_R_free                       0.2040 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1710 
_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                       0.0760 
_refine.pdbx_overall_ESU_R_Free                  0.0780 
_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             0.0763 
_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                       1.4500 
_refine_hist.d_res_low                        73.1900 
_refine_hist.pdbx_number_atoms_ligand         155 
_refine_hist.number_atoms_solvent             1211 
_refine_hist.number_atoms_total               9756 
_refine_hist.pdbx_number_residues_total       1044 
_refine_hist.pdbx_B_iso_mean_ligand           24.68 
_refine_hist.pdbx_B_iso_mean_solvent          26.91 
_refine_hist.pdbx_number_atoms_protein        8390 
_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' ? 0.025  0.020  9017  ? r_bond_refined_d       ? ? 
'X-RAY DIFFRACTION' ? 2.287  1.956  12304 ? r_angle_refined_deg    ? ? 
'X-RAY DIFFRACTION' ? 7.298  5.000  1089  ? r_dihedral_angle_1_deg ? ? 
'X-RAY DIFFRACTION' ? 37.525 24.580 452   ? r_dihedral_angle_2_deg ? ? 
'X-RAY DIFFRACTION' ? 12.517 15.000 1398  ? r_dihedral_angle_3_deg ? ? 
'X-RAY DIFFRACTION' ? 16.574 15.000 35    ? r_dihedral_angle_4_deg ? ? 
'X-RAY DIFFRACTION' ? 0.164  0.200  1272  ? r_chiral_restr         ? ? 
'X-RAY DIFFRACTION' ? 0.015  0.021  7152  ? r_gen_planes_refined   ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.4500 
_refine_ls_shell.d_res_low                        1.4880 
_refine_ls_shell.number_reflns_all                12579 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             1253 
_refine_ls_shell.number_reflns_R_work             11326 
_refine_ls_shell.percent_reflns_obs               99.2800 
_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                  0.2980 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.2740 
_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                     5LL9 
_struct.title                        
'Crystal structure of human carbonic anhydrase isozyme XII with 4-(1H-benzimidazol-1-ylacetyl)-2-chlorobenzenesulfonamide' 
_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        5LL9 
_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 4 ? 
I  N N 4 ? 
J  N N 4 ? 
K  N N 2 ? 
L  N N 3 ? 
M  N N 5 ? 
N  N N 4 ? 
O  N N 4 ? 
P  N N 2 ? 
Q  N N 3 ? 
R  N N 5 ? 
S  N N 4 ? 
T  N N 4 ? 
U  N N 2 ? 
V  N N 3 ? 
W  N N 5 ? 
X  N N 4 ? 
Y  N N 4 ? 
Z  N N 4 ? 
AA N N 6 ? 
BA N N 6 ? 
CA N N 6 ? 
DA N N 6 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    CAH12_HUMAN 
_struct_ref.pdbx_db_accession          O43570 
_struct_ref.pdbx_db_isoform            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 5LL9 A 2 ? 263 ? O43570 30 ? 291 ? 2 263 
2 1 5LL9 B 2 ? 263 ? O43570 30 ? 291 ? 2 263 
3 1 5LL9 C 2 ? 263 ? O43570 30 ? 291 ? 2 263 
4 1 5LL9 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 5LL9 MET A 1 ? UNP O43570 ? ? 'initiating methionine' 1 1 
2 5LL9 MET B 1 ? UNP O43570 ? ? 'initiating methionine' 1 2 
3 5LL9 MET C 1 ? UNP O43570 ? ? 'initiating methionine' 1 3 
4 5LL9 MET D 1 ? UNP O43570 ? ? 'initiating methionine' 1 4 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? dimeric 2 
2 author_defined_assembly ? dimeric 2 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,B,E,F,G,H,I,J,K,L,M,N,O,AA,BA 
2 1 C,D,P,Q,R,S,T,U,V,W,X,Y,Z,CA,DA 
# 
_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 GLY B 11  ? LYS B 18  ? GLY B 11  LYS B 18  5 ? 8  
HELX_P HELX_P11 AB2 TYR B 19  ? GLY B 24  ? TYR B 19  GLY B 24  5 ? 6  
HELX_P HELX_P12 AB3 HIS B 33  ? ASP B 35  ? HIS B 33  ASP B 35  5 ? 3  
HELX_P HELX_P13 AB4 ASP B 128 ? SER B 133 ? ASP B 128 SER B 133 1 ? 6  
HELX_P HELX_P14 AB5 ASN B 152 ? SER B 160 ? ASN B 152 SER B 160 1 ? 9  
HELX_P HELX_P15 AB6 HIS B 161 ? VAL B 165 ? HIS B 161 VAL B 165 5 ? 5  
HELX_P HELX_P16 AB7 ASN B 178 ? LEU B 183 ? ASN B 178 LEU B 183 5 ? 6  
HELX_P HELX_P17 AB8 SER B 218 ? ALA B 228 ? SER B 218 ALA B 228 1 ? 11 
HELX_P HELX_P18 AB9 TYR C 19  ? GLY C 24  ? TYR C 19  GLY C 24  5 ? 6  
HELX_P HELX_P19 AC1 HIS C 33  ? ASP C 35  ? HIS C 33  ASP C 35  5 ? 3  
HELX_P HELX_P20 AC2 ASP C 128 ? ASN C 134 ? ASP C 128 ASN C 134 1 ? 7  
HELX_P HELX_P21 AC3 ASN C 152 ? SER C 160 ? ASN C 152 SER C 160 1 ? 9  
HELX_P HELX_P22 AC4 HIS C 161 ? VAL C 165 ? HIS C 161 VAL C 165 5 ? 5  
HELX_P HELX_P23 AC5 ASN C 178 ? LEU C 183 ? ASN C 178 LEU C 183 5 ? 6  
HELX_P HELX_P24 AC6 SER C 218 ? ALA C 228 ? SER C 218 ALA C 228 1 ? 11 
HELX_P HELX_P25 AC7 GLY D 11  ? LYS D 18  ? GLY D 11  LYS D 18  5 ? 8  
HELX_P HELX_P26 AC8 TYR D 19  ? GLY D 24  ? TYR D 19  GLY D 24  5 ? 6  
HELX_P HELX_P27 AC9 HIS D 33  ? ASP D 35  ? HIS D 33  ASP D 35  5 ? 3  
HELX_P HELX_P28 AD1 ASP D 128 ? SER D 133 ? ASP D 128 SER D 133 1 ? 6  
HELX_P HELX_P29 AD2 ASN D 152 ? SER D 160 ? ASN D 152 SER D 160 1 ? 9  
HELX_P HELX_P30 AD3 HIS D 161 ? VAL D 165 ? HIS D 161 VAL D 165 5 ? 5  
HELX_P HELX_P31 AD4 ASN D 178 ? LEU D 183 ? ASN D 178 LEU D 183 5 ? 6  
HELX_P HELX_P32 AD5 SER D 218 ? LEU D 229 ? SER D 218 LEU D 229 1 ? 12 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1  disulf ? ? A CYS 22  SG  ? ? ? 1_555 A CYS 202 SG  ? ? A CYS 22  A CYS 202 1_555 ? ? ? ? ? ? ? 2.047 ? ? 
disulf2  disulf ? ? B CYS 22  SG  ? ? ? 1_555 B CYS 202 SG  ? ? B CYS 22  B CYS 202 1_555 ? ? ? ? ? ? ? 2.036 ? ? 
disulf3  disulf ? ? C CYS 22  SG  ? ? ? 1_555 C CYS 202 SG  ? ? C CYS 22  C CYS 202 1_555 ? ? ? ? ? ? ? 2.072 ? ? 
disulf4  disulf ? ? D CYS 22  SG  ? ? ? 1_555 D CYS 202 SG  ? ? D CYS 22  D CYS 202 1_555 ? ? ? ? ? ? ? 2.054 ? ? 
metalc1  metalc ? ? A HIS 91  NE2 ? ? ? 1_555 E ZN  .   ZN  ? ? A HIS 91  A ZN  301 1_555 ? ? ? ? ? ? ? 2.014 ? ? 
metalc2  metalc ? ? A HIS 93  NE2 ? ? ? 1_555 E ZN  .   ZN  ? ? A HIS 93  A ZN  301 1_555 ? ? ? ? ? ? ? 2.003 ? ? 
metalc3  metalc ? ? A HIS 117 ND1 ? ? ? 1_555 E ZN  .   ZN  ? ? A HIS 117 A ZN  301 1_555 ? ? ? ? ? ? ? 2.003 ? ? 
metalc4  metalc ? ? E ZN  .   ZN  ? ? ? 1_555 F 6YQ .   N10 ? ? A ZN  301 A 6YQ 302 1_555 ? ? ? ? ? ? ? 1.923 ? ? 
metalc5  metalc ? ? B HIS 91  NE2 ? ? ? 1_555 K ZN  .   ZN  ? ? B HIS 91  B ZN  301 1_555 ? ? ? ? ? ? ? 1.989 ? ? 
metalc6  metalc ? ? B HIS 93  NE2 ? ? ? 1_555 K ZN  .   ZN  ? ? B HIS 93  B ZN  301 1_555 ? ? ? ? ? ? ? 1.987 ? ? 
metalc7  metalc ? ? B HIS 117 ND1 ? ? ? 1_555 K ZN  .   ZN  ? ? B HIS 117 B ZN  301 1_555 ? ? ? ? ? ? ? 2.047 ? ? 
metalc8  metalc ? ? K ZN  .   ZN  ? ? ? 1_555 L 6YQ .   N10 ? ? B ZN  301 B 6YQ 302 1_555 ? ? ? ? ? ? ? 1.865 ? ? 
metalc9  metalc ? ? C HIS 91  NE2 ? ? ? 1_555 P ZN  .   ZN  ? ? C HIS 91  C ZN  301 1_555 ? ? ? ? ? ? ? 1.988 ? ? 
metalc10 metalc ? ? C HIS 93  NE2 ? ? ? 1_555 P ZN  .   ZN  ? ? C HIS 93  C ZN  301 1_555 ? ? ? ? ? ? ? 2.022 ? ? 
metalc11 metalc ? ? C HIS 117 ND1 ? ? ? 1_555 P ZN  .   ZN  ? ? C HIS 117 C ZN  301 1_555 ? ? ? ? ? ? ? 1.933 ? ? 
metalc12 metalc ? ? P ZN  .   ZN  ? ? ? 1_555 Q 6YQ .   N10 ? ? C ZN  301 C 6YQ 302 1_555 ? ? ? ? ? ? ? 1.890 ? ? 
metalc13 metalc ? ? D HIS 91  NE2 ? ? ? 1_555 U ZN  .   ZN  ? ? D HIS 91  D ZN  301 1_555 ? ? ? ? ? ? ? 1.981 ? ? 
metalc14 metalc ? ? D HIS 93  NE2 ? ? ? 1_555 U ZN  .   ZN  ? ? D HIS 93  D ZN  301 1_555 ? ? ? ? ? ? ? 2.005 ? ? 
metalc15 metalc ? ? D HIS 117 ND1 ? ? ? 1_555 U ZN  .   ZN  ? ? D HIS 117 D ZN  301 1_555 ? ? ? ? ? ? ? 2.026 ? ? 
metalc16 metalc ? ? U ZN  .   ZN  ? ? ? 1_555 V 6YQ .   N10 ? ? D ZN  301 D 6YQ 302 1_555 ? ? ? ? ? ? ? 1.940 ? ? 
# 
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_555 102.4 ? 
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_555 112.2 ? 
3  NE2 ? A HIS 93  ? A HIS 93  ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS 117 ? A HIS 117 ? 1_555 99.5  ? 
4  NE2 ? A HIS 91  ? A HIS 91  ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 N10 ? F 6YQ .   ? A 6YQ 302 ? 1_555 107.5 ? 
5  NE2 ? A HIS 93  ? A HIS 93  ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 N10 ? F 6YQ .   ? A 6YQ 302 ? 1_555 119.2 ? 
6  ND1 ? A HIS 117 ? A HIS 117 ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 N10 ? F 6YQ .   ? A 6YQ 302 ? 1_555 115.3 ? 
7  NE2 ? B HIS 91  ? B HIS 91  ? 1_555 ZN ? K ZN . ? B ZN 301 ? 1_555 NE2 ? B HIS 93  ? B HIS 93  ? 1_555 104.3 ? 
8  NE2 ? B HIS 91  ? B HIS 91  ? 1_555 ZN ? K ZN . ? B ZN 301 ? 1_555 ND1 ? B HIS 117 ? B HIS 117 ? 1_555 111.9 ? 
9  NE2 ? B HIS 93  ? B HIS 93  ? 1_555 ZN ? K ZN . ? B ZN 301 ? 1_555 ND1 ? B HIS 117 ? B HIS 117 ? 1_555 99.1  ? 
10 NE2 ? B HIS 91  ? B HIS 91  ? 1_555 ZN ? K ZN . ? B ZN 301 ? 1_555 N10 ? L 6YQ .   ? B 6YQ 302 ? 1_555 108.3 ? 
11 NE2 ? B HIS 93  ? B HIS 93  ? 1_555 ZN ? K ZN . ? B ZN 301 ? 1_555 N10 ? L 6YQ .   ? B 6YQ 302 ? 1_555 115.5 ? 
12 ND1 ? B HIS 117 ? B HIS 117 ? 1_555 ZN ? K ZN . ? B ZN 301 ? 1_555 N10 ? L 6YQ .   ? B 6YQ 302 ? 1_555 117.0 ? 
13 NE2 ? C HIS 91  ? C HIS 91  ? 1_555 ZN ? P ZN . ? C ZN 301 ? 1_555 NE2 ? C HIS 93  ? C HIS 93  ? 1_555 102.3 ? 
14 NE2 ? C HIS 91  ? C HIS 91  ? 1_555 ZN ? P ZN . ? C ZN 301 ? 1_555 ND1 ? C HIS 117 ? C HIS 117 ? 1_555 113.1 ? 
15 NE2 ? C HIS 93  ? C HIS 93  ? 1_555 ZN ? P ZN . ? C ZN 301 ? 1_555 ND1 ? C HIS 117 ? C HIS 117 ? 1_555 98.6  ? 
16 NE2 ? C HIS 91  ? C HIS 91  ? 1_555 ZN ? P ZN . ? C ZN 301 ? 1_555 N10 ? Q 6YQ .   ? C 6YQ 302 ? 1_555 108.8 ? 
17 NE2 ? C HIS 93  ? C HIS 93  ? 1_555 ZN ? P ZN . ? C ZN 301 ? 1_555 N10 ? Q 6YQ .   ? C 6YQ 302 ? 1_555 116.7 ? 
18 ND1 ? C HIS 117 ? C HIS 117 ? 1_555 ZN ? P ZN . ? C ZN 301 ? 1_555 N10 ? Q 6YQ .   ? C 6YQ 302 ? 1_555 116.3 ? 
19 NE2 ? D HIS 91  ? D HIS 91  ? 1_555 ZN ? U ZN . ? D ZN 301 ? 1_555 NE2 ? D HIS 93  ? D HIS 93  ? 1_555 102.9 ? 
20 NE2 ? D HIS 91  ? D HIS 91  ? 1_555 ZN ? U ZN . ? D ZN 301 ? 1_555 ND1 ? D HIS 117 ? D HIS 117 ? 1_555 111.7 ? 
21 NE2 ? D HIS 93  ? D HIS 93  ? 1_555 ZN ? U ZN . ? D ZN 301 ? 1_555 ND1 ? D HIS 117 ? D HIS 117 ? 1_555 99.5  ? 
22 NE2 ? D HIS 91  ? D HIS 91  ? 1_555 ZN ? U ZN . ? D ZN 301 ? 1_555 N10 ? V 6YQ .   ? D 6YQ 302 ? 1_555 109.3 ? 
23 NE2 ? D HIS 93  ? D HIS 93  ? 1_555 ZN ? U ZN . ? D ZN 301 ? 1_555 N10 ? V 6YQ .   ? D 6YQ 302 ? 1_555 114.6 ? 
24 ND1 ? D HIS 117 ? D HIS 117 ? 1_555 ZN ? U ZN . ? D ZN 301 ? 1_555 N10 ? V 6YQ .   ? D 6YQ 302 ? 1_555 117.7 ? 
# 
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 3.74  
2 PRO 200 A . ? PRO 200 A PRO 201 A ? PRO 201 A 1 14.11 
3 SER 28  B . ? SER 28  B PRO 29  B ? PRO 29  B 1 0.83  
4 PRO 200 B . ? PRO 200 B PRO 201 B ? PRO 201 B 1 8.73  
5 SER 28  C . ? SER 28  C PRO 29  C ? PRO 29  C 1 -1.40 
6 PRO 200 C . ? PRO 200 C PRO 201 C ? PRO 201 C 1 6.52  
7 SER 28  D . ? SER 28  D PRO 29  D ? PRO 29  D 1 0.14  
8 PRO 200 D . ? PRO 200 D PRO 201 D ? PRO 201 D 1 7.80  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2  ? 
AA2 ? 10 ? 
AA3 ? 6  ? 
AA4 ? 2  ? 
AA5 ? 10 ? 
AA6 ? 6  ? 
AA7 ? 2  ? 
AA8 ? 10 ? 
AA9 ? 6  ? 
AB1 ? 2  ? 
AB2 ? 10 ? 
AB3 ? 6  ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2  ? parallel      
AA2 1 2  ? parallel      
AA2 2 3  ? anti-parallel 
AA2 3 4  ? anti-parallel 
AA2 4 5  ? parallel      
AA2 5 6  ? anti-parallel 
AA2 6 7  ? anti-parallel 
AA2 7 8  ? anti-parallel 
AA2 8 9  ? anti-parallel 
AA2 9 10 ? anti-parallel 
AA3 1 2  ? anti-parallel 
AA3 2 3  ? anti-parallel 
AA3 3 4  ? anti-parallel 
AA3 4 5  ? anti-parallel 
AA3 5 6  ? parallel      
AA4 1 2  ? parallel      
AA5 1 2  ? parallel      
AA5 2 3  ? anti-parallel 
AA5 3 4  ? anti-parallel 
AA5 4 5  ? parallel      
AA5 5 6  ? anti-parallel 
AA5 6 7  ? anti-parallel 
AA5 7 8  ? anti-parallel 
AA5 8 9  ? anti-parallel 
AA5 9 10 ? anti-parallel 
AA6 1 2  ? anti-parallel 
AA6 2 3  ? anti-parallel 
AA6 3 4  ? anti-parallel 
AA6 4 5  ? anti-parallel 
AA6 5 6  ? parallel      
AA7 1 2  ? parallel      
AA8 1 2  ? parallel      
AA8 2 3  ? anti-parallel 
AA8 3 4  ? anti-parallel 
AA8 4 5  ? parallel      
AA8 5 6  ? anti-parallel 
AA8 6 7  ? anti-parallel 
AA8 7 8  ? anti-parallel 
AA8 8 9  ? anti-parallel 
AA8 9 10 ? anti-parallel 
AA9 1 2  ? anti-parallel 
AA9 2 3  ? anti-parallel 
AA9 3 4  ? anti-parallel 
AA9 4 5  ? anti-parallel 
AA9 5 6  ? parallel      
AB1 1 2  ? parallel      
AB2 1 2  ? parallel      
AB2 2 3  ? anti-parallel 
AB2 3 4  ? anti-parallel 
AB2 4 5  ? parallel      
AB2 5 6  ? anti-parallel 
AB2 6 7  ? anti-parallel 
AB2 7 8  ? anti-parallel 
AB2 8 9  ? anti-parallel 
AB2 9 10 ? anti-parallel 
AB3 1 2  ? anti-parallel 
AB3 2 3  ? anti-parallel 
AB3 3 4  ? anti-parallel 
AB3 4 5  ? anti-parallel 
AB3 5 6  ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1  ASP A 31  ? LEU A 32  ? ASP A 31  LEU A 32  
AA1 2  THR A 106 ? VAL A 107 ? THR A 106 VAL A 107 
AA2 1  LEU A 37  ? TYR A 39  ? LEU A 37  TYR A 39  
AA2 2  VAL A 257 ? THR A 259 ? VAL A 257 THR A 259 
AA2 3  TYR A 190 ? GLY A 195 ? TYR A 190 GLY A 195 
AA2 4  VAL A 206 ? PHE A 211 ? VAL A 206 PHE A 211 
AA2 5  LEU A 139 ? MET A 148 ? LEU A 139 MET A 148 
AA2 6  ALA A 114 ? ASN A 122 ? ALA A 114 ASN A 122 
AA2 7  TYR A 85  ? TRP A 94  ? TYR A 85  TRP A 94  
AA2 8  VAL A 68  ? ASN A 71  ? VAL A 68  ASN A 71  
AA2 9  GLN A 58  ? ASN A 63  ? GLN A 58  ASN A 63  
AA2 10 GLU A 171 ? PRO A 175 ? GLU A 171 PRO A 175 
AA3 1  GLU A 47  ? GLN A 49  ? GLU A 47  GLN A 49  
AA3 2  HIS A 77  ? GLN A 79  ? HIS A 77  GLN A 79  
AA3 3  TYR A 85  ? TRP A 94  ? TYR A 85  TRP A 94  
AA3 4  ALA A 114 ? ASN A 122 ? ALA A 114 ASN A 122 
AA3 5  LEU A 139 ? MET A 148 ? LEU A 139 MET A 148 
AA3 6  VAL A 215 ? ILE A 217 ? VAL A 215 ILE A 217 
AA4 1  ASP B 31  ? LEU B 32  ? ASP B 31  LEU B 32  
AA4 2  THR B 106 ? VAL B 107 ? THR B 106 VAL B 107 
AA5 1  LEU B 37  ? TYR B 39  ? LEU B 37  TYR B 39  
AA5 2  VAL B 257 ? THR B 259 ? VAL B 257 THR B 259 
AA5 3  TYR B 190 ? GLY B 195 ? TYR B 190 GLY B 195 
AA5 4  VAL B 206 ? PHE B 211 ? VAL B 206 PHE B 211 
AA5 5  LEU B 139 ? MET B 148 ? LEU B 139 MET B 148 
AA5 6  ALA B 114 ? ASN B 122 ? ALA B 114 ASN B 122 
AA5 7  TYR B 85  ? TRP B 94  ? TYR B 85  TRP B 94  
AA5 8  VAL B 68  ? ASN B 71  ? VAL B 68  ASN B 71  
AA5 9  GLN B 58  ? ASN B 63  ? GLN B 58  ASN B 63  
AA5 10 GLU B 171 ? PRO B 175 ? GLU B 171 PRO B 175 
AA6 1  GLU B 47  ? GLN B 49  ? GLU B 47  GLN B 49  
AA6 2  HIS B 77  ? GLN B 79  ? HIS B 77  GLN B 79  
AA6 3  TYR B 85  ? TRP B 94  ? TYR B 85  TRP B 94  
AA6 4  ALA B 114 ? ASN B 122 ? ALA B 114 ASN B 122 
AA6 5  LEU B 139 ? MET B 148 ? LEU B 139 MET B 148 
AA6 6  VAL B 215 ? ILE B 217 ? VAL B 215 ILE B 217 
AA7 1  ASP C 31  ? LEU C 32  ? ASP C 31  LEU C 32  
AA7 2  THR C 106 ? VAL C 107 ? THR C 106 VAL C 107 
AA8 1  LEU C 37  ? TYR C 39  ? LEU C 37  TYR C 39  
AA8 2  VAL C 257 ? THR C 259 ? VAL C 257 THR C 259 
AA8 3  TYR C 190 ? GLY C 195 ? TYR C 190 GLY C 195 
AA8 4  VAL C 206 ? PHE C 211 ? VAL C 206 PHE C 211 
AA8 5  LEU C 139 ? MET C 148 ? LEU C 139 MET C 148 
AA8 6  ALA C 114 ? ASN C 122 ? ALA C 114 ASN C 122 
AA8 7  TYR C 85  ? TRP C 94  ? TYR C 85  TRP C 94  
AA8 8  VAL C 68  ? ASN C 71  ? VAL C 68  ASN C 71  
AA8 9  GLN C 58  ? ASN C 63  ? GLN C 58  ASN C 63  
AA8 10 GLU C 171 ? PRO C 175 ? GLU C 171 PRO C 175 
AA9 1  GLU C 47  ? GLN C 49  ? GLU C 47  GLN C 49  
AA9 2  HIS C 77  ? GLN C 79  ? HIS C 77  GLN C 79  
AA9 3  TYR C 85  ? TRP C 94  ? TYR C 85  TRP C 94  
AA9 4  ALA C 114 ? ASN C 122 ? ALA C 114 ASN C 122 
AA9 5  LEU C 139 ? MET C 148 ? LEU C 139 MET C 148 
AA9 6  VAL C 215 ? ILE C 217 ? VAL C 215 ILE C 217 
AB1 1  ASP D 31  ? LEU D 32  ? ASP D 31  LEU D 32  
AB1 2  THR D 106 ? VAL D 107 ? THR D 106 VAL D 107 
AB2 1  LEU D 37  ? TYR D 39  ? LEU D 37  TYR D 39  
AB2 2  VAL D 257 ? THR D 259 ? VAL D 257 THR D 259 
AB2 3  TYR D 190 ? GLY D 195 ? TYR D 190 GLY D 195 
AB2 4  VAL D 206 ? PHE D 211 ? VAL D 206 PHE D 211 
AB2 5  LEU D 139 ? MET D 148 ? LEU D 139 MET D 148 
AB2 6  ALA D 114 ? ASN D 122 ? ALA D 114 ASN D 122 
AB2 7  TYR D 85  ? TRP D 94  ? TYR D 85  TRP D 94  
AB2 8  VAL D 68  ? ASN D 71  ? VAL D 68  ASN D 71  
AB2 9  GLN D 58  ? ASN D 63  ? GLN D 58  ASN D 63  
AB2 10 GLU D 171 ? PRO D 175 ? GLU D 171 PRO D 175 
AB3 1  GLU D 47  ? GLN D 49  ? GLU D 47  GLN D 49  
AB3 2  HIS D 77  ? GLN D 79  ? HIS D 77  GLN D 79  
AB3 3  TYR D 85  ? TRP D 94  ? TYR D 85  TRP D 94  
AB3 4  ALA D 114 ? ASN D 122 ? ALA D 114 ASN D 122 
AB3 5  LEU D 139 ? MET D 148 ? LEU D 139 MET D 148 
AB3 6  VAL D 215 ? ILE D 217 ? VAL D 215 ILE D 217 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2  N LEU A 32  ? N LEU A 32  O THR A 106 ? O THR A 106 
AA2 1 2  N GLN A 38  ? N GLN A 38  O THR A 259 ? O THR A 259 
AA2 2 3  O TYR A 258 ? O TYR A 258 N ARG A 192 ? N ARG A 192 
AA2 3 4  N GLY A 195 ? N GLY A 195 O VAL A 206 ? O VAL A 206 
AA2 4 5  O THR A 209 ? O THR A 209 N ALA A 143 ? N ALA A 143 
AA2 5 6  O ILE A 146 ? O ILE A 146 N ALA A 114 ? N ALA A 114 
AA2 6 7  O VAL A 119 ? O VAL A 119 N GLN A 89  ? N GLN A 89  
AA2 7 8  O LEU A 90  ? O LEU A 90  N LEU A 70  ? N LEU A 70  
AA2 8 9  O LYS A 69  ? O LYS A 69  N THR A 62  ? N THR A 62  
AA2 9 10 N LEU A 61  ? N LEU A 61  O ALA A 172 ? O ALA A 172 
AA3 1 2  N GLN A 49  ? N GLN A 49  O HIS A 77  ? O HIS A 77  
AA3 2 3  N ILE A 78  ? N ILE A 78  O TYR A 85  ? O TYR A 85  
AA3 3 4  N GLN A 89  ? N GLN A 89  O VAL A 119 ? O VAL A 119 
AA3 4 5  N ALA A 114 ? N ALA A 114 O ILE A 146 ? O ILE A 146 
AA3 5 6  N GLU A 147 ? N GLU A 147 O VAL A 215 ? O VAL A 215 
AA4 1 2  N LEU B 32  ? N LEU B 32  O THR B 106 ? O THR B 106 
AA5 1 2  N GLN B 38  ? N GLN B 38  O VAL B 257 ? O VAL B 257 
AA5 2 3  O TYR B 258 ? O TYR B 258 N ARG B 192 ? N ARG B 192 
AA5 3 4  N GLY B 195 ? N GLY B 195 O VAL B 206 ? O VAL B 206 
AA5 4 5  O THR B 209 ? O THR B 209 N ALA B 143 ? N ALA B 143 
AA5 5 6  O LEU B 142 ? O LEU B 142 N ILE B 118 ? N ILE B 118 
AA5 6 7  O VAL B 119 ? O VAL B 119 N GLN B 89  ? N GLN B 89  
AA5 7 8  O LEU B 90  ? O LEU B 90  N LEU B 70  ? N LEU B 70  
AA5 8 9  O 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 GLU B 47  ? N GLU B 47  O GLN B 79  ? O GLN B 79  
AA6 2 3  N ILE B 78  ? N ILE B 78  O TYR B 85  ? O TYR B 85  
AA6 3 4  N GLN B 89  ? N GLN B 89  O VAL B 119 ? O VAL B 119 
AA6 4 5  N ILE B 118 ? N ILE B 118 O LEU B 142 ? O LEU B 142 
AA6 5 6  N GLU B 147 ? N GLU B 147 O VAL B 215 ? O VAL B 215 
AA7 1 2  N LEU C 32  ? N LEU C 32  O THR C 106 ? O THR C 106 
AA8 1 2  N GLN C 38  ? N GLN C 38  O VAL C 257 ? O VAL C 257 
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 VAL C 144 ? O VAL C 144 N LEU C 116 ? N LEU C 116 
AA8 6 7  O VAL C 119 ? O VAL C 119 N GLN C 89  ? N GLN C 89  
AA8 7 8  O LEU C 90  ? O LEU C 90  N LEU C 70  ? N LEU C 70  
AA8 8 9  O ASN C 71  ? O ASN C 71  N LEU C 60  ? N LEU C 60  
AA8 9 10 N LEU C 61  ? N LEU C 61  O ALA C 172 ? O ALA C 172 
AA9 1 2  N GLU C 47  ? N GLU C 47  O GLN C 79  ? O GLN C 79  
AA9 2 3  N ILE C 78  ? N ILE C 78  O TYR C 85  ? O TYR C 85  
AA9 3 4  N GLN C 89  ? N GLN C 89  O VAL C 119 ? O VAL C 119 
AA9 4 5  N LEU C 116 ? N LEU C 116 O VAL C 144 ? O VAL C 144 
AA9 5 6  N GLU C 147 ? N GLU C 147 O VAL C 215 ? O VAL C 215 
AB1 1 2  N LEU D 32  ? N LEU D 32  O THR D 106 ? O THR D 106 
AB2 1 2  N GLN D 38  ? N GLN D 38  O VAL D 257 ? O VAL D 257 
AB2 2 3  O TYR D 258 ? O TYR D 258 N ARG D 192 ? N ARG D 192 
AB2 3 4  N GLY D 195 ? N GLY D 195 O VAL D 206 ? O VAL D 206 
AB2 4 5  O THR D 209 ? O THR D 209 N ALA D 143 ? N ALA D 143 
AB2 5 6  O LEU D 142 ? O LEU D 142 N ILE D 118 ? N ILE D 118 
AB2 6 7  O VAL D 119 ? O VAL D 119 N GLN D 89  ? N GLN D 89  
AB2 7 8  O LEU D 90  ? O LEU D 90  N LEU D 70  ? N LEU D 70  
AB2 8 9  O ASN D 71  ? O ASN D 71  N LEU D 60  ? N LEU D 60  
AB2 9 10 N LEU D 61  ? N LEU D 61  O ALA D 172 ? O ALA D 172 
AB3 1 2  N GLN D 49  ? N GLN D 49  O HIS D 77  ? O HIS D 77  
AB3 2 3  N ILE D 78  ? N ILE D 78  O TYR D 85  ? O TYR D 85  
AB3 3 4  N GLN D 89  ? N GLN D 89  O VAL D 119 ? O VAL D 119 
AB3 4 5  N ILE D 118 ? N ILE D 118 O LEU D 142 ? O LEU D 142 
AB3 5 6  N GLU D 147 ? N GLU D 147 O VAL D 215 ? O VAL D 215 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software A ZN  301 ? 4  'binding site for residue ZN A 301'  
AC2 Software A 6YQ 302 ? 15 'binding site for residue 6YQ A 302' 
AC3 Software A EDO 303 ? 6  'binding site for residue EDO A 303' 
AC4 Software A EDO 304 ? 5  'binding site for residue EDO A 304' 
AC5 Software A EDO 305 ? 3  'binding site for residue EDO A 305' 
AC6 Software A EDO 306 ? 6  'binding site for residue EDO A 306' 
AC7 Software B ZN  301 ? 4  'binding site for residue ZN B 301'  
AC8 Software B 6YQ 302 ? 14 'binding site for residue 6YQ B 302' 
AC9 Software B SO4 303 ? 5  'binding site for residue SO4 B 303' 
AD1 Software B EDO 304 ? 8  'binding site for residue EDO B 304' 
AD2 Software B EDO 305 ? 5  'binding site for residue EDO B 305' 
AD3 Software C ZN  301 ? 4  'binding site for residue ZN C 301'  
AD4 Software C 6YQ 302 ? 13 'binding site for residue 6YQ C 302' 
AD5 Software C SO4 303 ? 5  'binding site for residue SO4 C 303' 
AD6 Software C EDO 304 ? 7  'binding site for residue EDO C 304' 
AD7 Software C EDO 305 ? 6  'binding site for residue EDO C 305' 
AD8 Software D ZN  301 ? 4  'binding site for residue ZN D 301'  
AD9 Software D 6YQ 302 ? 12 'binding site for residue 6YQ D 302' 
AE1 Software D SO4 303 ? 5  'binding site for residue SO4 D 303' 
AE2 Software D EDO 304 ? 7  'binding site for residue EDO D 304' 
AE3 Software D EDO 305 ? 8  'binding site for residue EDO D 305' 
AE4 Software D EDO 306 ? 7  'binding site for residue EDO D 306' 
# 
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  6YQ F  .   ? 6YQ A 302 . ? 1_555 ? 
5   AC2 15 HIS A  91  ? HIS A 91  . ? 1_555 ? 
6   AC2 15 HIS A  93  ? HIS A 93  . ? 1_555 ? 
7   AC2 15 HIS A  117 ? HIS A 117 . ? 1_555 ? 
8   AC2 15 SER A  130 ? SER A 130 . ? 1_555 ? 
9   AC2 15 SER A  133 ? SER A 133 . ? 1_555 ? 
10  AC2 15 VAL A  141 ? VAL A 141 . ? 1_555 ? 
11  AC2 15 LEU A  197 ? LEU A 197 . ? 1_555 ? 
12  AC2 15 THR A  198 ? THR A 198 . ? 1_555 ? 
13  AC2 15 THR A  199 ? THR A 199 . ? 1_555 ? 
14  AC2 15 PRO A  201 ? PRO A 201 . ? 1_555 ? 
15  AC2 15 TRP A  208 ? TRP A 208 . ? 1_555 ? 
16  AC2 15 ZN  E  .   ? ZN  A 301 . ? 1_555 ? 
17  AC2 15 EDO G  .   ? EDO A 303 . ? 1_555 ? 
18  AC2 15 EDO H  .   ? EDO A 304 . ? 1_555 ? 
19  AC2 15 HOH AA .   ? HOH A 429 . ? 1_555 ? 
20  AC3 6  ASN A  64  ? ASN A 64  . ? 1_555 ? 
21  AC3 6  HIS A  66  ? HIS A 66  . ? 1_555 ? 
22  AC3 6  GLN A  89  ? GLN A 89  . ? 1_555 ? 
23  AC3 6  6YQ F  .   ? 6YQ A 302 . ? 1_555 ? 
24  AC3 6  EDO H  .   ? EDO A 304 . ? 1_555 ? 
25  AC3 6  HOH AA .   ? HOH A 593 . ? 1_555 ? 
26  AC4 5  ASN A  64  ? ASN A 64  . ? 1_555 ? 
27  AC4 5  LYS A  69  ? LYS A 69  . ? 1_555 ? 
28  AC4 5  GLN A  89  ? GLN A 89  . ? 1_555 ? 
29  AC4 5  6YQ F  .   ? 6YQ A 302 . ? 1_555 ? 
30  AC4 5  EDO G  .   ? EDO A 303 . ? 1_555 ? 
31  AC5 3  ASP A  156 ? ASP A 156 . ? 1_555 ? 
32  AC5 3  SER A  160 ? SER A 160 . ? 1_555 ? 
33  AC5 3  HOH AA .   ? HOH A 463 . ? 1_555 ? 
34  AC6 6  THR A  44  ? THR A 44  . ? 1_555 ? 
35  AC6 6  LEU A  46  ? LEU A 46  . ? 1_555 ? 
36  AC6 6  GLY A  80  ? GLY A 80  . ? 1_555 ? 
37  AC6 6  LEU A  81  ? LEU A 81  . ? 1_555 ? 
38  AC6 6  TYR A  190 ? TYR A 190 . ? 1_555 ? 
39  AC6 6  ARG A  192 ? ARG A 192 . ? 1_555 ? 
40  AC7 4  HIS B  91  ? HIS B 91  . ? 1_555 ? 
41  AC7 4  HIS B  93  ? HIS B 93  . ? 1_555 ? 
42  AC7 4  HIS B  117 ? HIS B 117 . ? 1_555 ? 
43  AC7 4  6YQ L  .   ? 6YQ B 302 . ? 1_555 ? 
44  AC8 14 HIS B  91  ? HIS B 91  . ? 1_555 ? 
45  AC8 14 HIS B  93  ? HIS B 93  . ? 1_555 ? 
46  AC8 14 HIS B  117 ? HIS B 117 . ? 1_555 ? 
47  AC8 14 SER B  130 ? SER B 130 . ? 1_555 ? 
48  AC8 14 VAL B  141 ? VAL B 141 . ? 1_555 ? 
49  AC8 14 LEU B  197 ? LEU B 197 . ? 1_555 ? 
50  AC8 14 THR B  198 ? THR B 198 . ? 1_555 ? 
51  AC8 14 THR B  199 ? THR B 199 . ? 1_555 ? 
52  AC8 14 PRO B  201 ? PRO B 201 . ? 1_555 ? 
53  AC8 14 TRP B  208 ? TRP B 208 . ? 1_555 ? 
54  AC8 14 ZN  K  .   ? ZN  B 301 . ? 1_555 ? 
55  AC8 14 SO4 M  .   ? SO4 B 303 . ? 1_555 ? 
56  AC8 14 EDO N  .   ? EDO B 304 . ? 1_555 ? 
57  AC8 14 HOH BA .   ? HOH B 408 . ? 1_555 ? 
58  AC9 5  ASN B  64  ? ASN B 64  . ? 1_555 ? 
59  AC9 5  LYS B  69  ? LYS B 69  . ? 1_555 ? 
60  AC9 5  6YQ L  .   ? 6YQ B 302 . ? 1_555 ? 
61  AC9 5  EDO N  .   ? EDO B 304 . ? 1_555 ? 
62  AC9 5  HOH BA .   ? HOH B 408 . ? 1_555 ? 
63  AD1 8  ASN B  64  ? ASN B 64  . ? 1_555 ? 
64  AD1 8  HIS B  66  ? HIS B 66  . ? 1_555 ? 
65  AD1 8  GLN B  89  ? GLN B 89  . ? 1_555 ? 
66  AD1 8  HIS B  91  ? HIS B 91  . ? 1_555 ? 
67  AD1 8  6YQ L  .   ? 6YQ B 302 . ? 1_555 ? 
68  AD1 8  SO4 M  .   ? SO4 B 303 . ? 1_555 ? 
69  AD1 8  HOH BA .   ? HOH B 452 . ? 1_555 ? 
70  AD1 8  HOH BA .   ? HOH B 559 . ? 1_555 ? 
71  AD2 5  THR B  44  ? THR B 44  . ? 1_555 ? 
72  AD2 5  LEU B  46  ? LEU B 46  . ? 1_555 ? 
73  AD2 5  GLY B  80  ? GLY B 80  . ? 1_555 ? 
74  AD2 5  TYR B  190 ? TYR B 190 . ? 1_555 ? 
75  AD2 5  ARG B  192 ? ARG B 192 . ? 1_555 ? 
76  AD3 4  HIS C  91  ? HIS C 91  . ? 1_555 ? 
77  AD3 4  HIS C  93  ? HIS C 93  . ? 1_555 ? 
78  AD3 4  HIS C  117 ? HIS C 117 . ? 1_555 ? 
79  AD3 4  6YQ Q  .   ? 6YQ C 302 . ? 1_555 ? 
80  AD4 13 HIS C  91  ? HIS C 91  . ? 1_555 ? 
81  AD4 13 HIS C  93  ? HIS C 93  . ? 1_555 ? 
82  AD4 13 HIS C  117 ? HIS C 117 . ? 1_555 ? 
83  AD4 13 SER C  130 ? SER C 130 . ? 1_555 ? 
84  AD4 13 SER C  133 ? SER C 133 . ? 1_555 ? 
85  AD4 13 VAL C  141 ? VAL C 141 . ? 1_555 ? 
86  AD4 13 LEU C  197 ? LEU C 197 . ? 1_555 ? 
87  AD4 13 THR C  198 ? THR C 198 . ? 1_555 ? 
88  AD4 13 THR C  199 ? THR C 199 . ? 1_555 ? 
89  AD4 13 PRO C  201 ? PRO C 201 . ? 1_555 ? 
90  AD4 13 TRP C  208 ? TRP C 208 . ? 1_555 ? 
91  AD4 13 ZN  P  .   ? ZN  C 301 . ? 1_555 ? 
92  AD4 13 SO4 R  .   ? SO4 C 303 . ? 1_555 ? 
93  AD5 5  ASN C  64  ? ASN C 64  . ? 1_555 ? 
94  AD5 5  LYS C  69  ? LYS C 69  . ? 1_555 ? 
95  AD5 5  6YQ Q  .   ? 6YQ C 302 . ? 1_555 ? 
96  AD5 5  EDO T  .   ? EDO C 305 . ? 1_555 ? 
97  AD5 5  HOH CA .   ? HOH C 564 . ? 1_555 ? 
98  AD6 7  SER C  42  ? SER C 42  . ? 1_555 ? 
99  AD6 7  LEU C  46  ? LEU C 46  . ? 1_555 ? 
100 AD6 7  GLY C  80  ? GLY C 80  . ? 1_555 ? 
101 AD6 7  LEU C  81  ? LEU C 81  . ? 1_555 ? 
102 AD6 7  TYR C  190 ? TYR C 190 . ? 1_555 ? 
103 AD6 7  ARG C  192 ? ARG C 192 . ? 1_555 ? 
104 AD6 7  HOH CA .   ? HOH C 414 . ? 1_555 ? 
105 AD7 6  ASN C  64  ? ASN C 64  . ? 1_555 ? 
106 AD7 6  HIS C  66  ? HIS C 66  . ? 1_555 ? 
107 AD7 6  GLN C  89  ? GLN C 89  . ? 1_555 ? 
108 AD7 6  HIS C  91  ? HIS C 91  . ? 1_555 ? 
109 AD7 6  SO4 R  .   ? SO4 C 303 . ? 1_555 ? 
110 AD7 6  HOH CA .   ? HOH C 564 . ? 1_555 ? 
111 AD8 4  HIS D  91  ? HIS D 91  . ? 1_555 ? 
112 AD8 4  HIS D  93  ? HIS D 93  . ? 1_555 ? 
113 AD8 4  HIS D  117 ? HIS D 117 . ? 1_555 ? 
114 AD8 4  6YQ V  .   ? 6YQ D 302 . ? 1_555 ? 
115 AD9 12 HIS D  91  ? HIS D 91  . ? 1_555 ? 
116 AD9 12 HIS D  93  ? HIS D 93  . ? 1_555 ? 
117 AD9 12 HIS D  117 ? HIS D 117 . ? 1_555 ? 
118 AD9 12 SER D  130 ? SER D 130 . ? 1_555 ? 
119 AD9 12 VAL D  141 ? VAL D 141 . ? 1_555 ? 
120 AD9 12 LEU D  197 ? LEU D 197 . ? 1_555 ? 
121 AD9 12 THR D  198 ? THR D 198 . ? 1_555 ? 
122 AD9 12 THR D  199 ? THR D 199 . ? 1_555 ? 
123 AD9 12 PRO D  201 ? PRO D 201 . ? 1_555 ? 
124 AD9 12 TRP D  208 ? TRP D 208 . ? 1_555 ? 
125 AD9 12 ZN  U  .   ? ZN  D 301 . ? 1_555 ? 
126 AD9 12 SO4 W  .   ? SO4 D 303 . ? 1_555 ? 
127 AE1 5  ASN D  64  ? ASN D 64  . ? 1_555 ? 
128 AE1 5  LYS D  69  ? LYS D 69  . ? 1_555 ? 
129 AE1 5  6YQ V  .   ? 6YQ D 302 . ? 1_555 ? 
130 AE1 5  EDO X  .   ? EDO D 304 . ? 1_555 ? 
131 AE1 5  HOH DA .   ? HOH D 464 . ? 1_555 ? 
132 AE2 7  ASN D  64  ? ASN D 64  . ? 1_555 ? 
133 AE2 7  HIS D  66  ? HIS D 66  . ? 1_555 ? 
134 AE2 7  GLN D  89  ? GLN D 89  . ? 1_555 ? 
135 AE2 7  HIS D  91  ? HIS D 91  . ? 1_555 ? 
136 AE2 7  SO4 W  .   ? SO4 D 303 . ? 1_555 ? 
137 AE2 7  HOH DA .   ? HOH D 402 . ? 1_555 ? 
138 AE2 7  HOH DA .   ? HOH D 487 . ? 1_555 ? 
139 AE3 8  SER D  42  ? SER D 42  . ? 1_555 ? 
140 AE3 8  THR D  44  ? THR D 44  . ? 1_555 ? 
141 AE3 8  LEU D  46  ? LEU D 46  . ? 1_555 ? 
142 AE3 8  GLY D  80  ? GLY D 80  . ? 1_555 ? 
143 AE3 8  TYR D  190 ? TYR D 190 . ? 1_555 ? 
144 AE3 8  ARG D  192 ? ARG D 192 . ? 1_555 ? 
145 AE3 8  HOH DA .   ? HOH D 410 . ? 1_555 ? 
146 AE3 8  HOH DA .   ? HOH D 584 . ? 1_555 ? 
147 AE4 7  GLU D  180 ? GLU D 180 . ? 1_555 ? 
148 AE4 7  GLU D  181 ? GLU D 181 . ? 1_555 ? 
149 AE4 7  LEU D  183 ? LEU D 183 . ? 1_555 ? 
150 AE4 7  HOH DA .   ? HOH D 431 . ? 1_555 ? 
151 AE4 7  HOH DA .   ? HOH D 442 . ? 1_555 ? 
152 AE4 7  HOH DA .   ? HOH D 498 . ? 1_555 ? 
153 AE4 7  HOH DA .   ? HOH D 557 . ? 1_555 ? 
# 
_pdbx_entry_details.entry_id                   5LL9 
_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 CD1 B PHE 252 ? ? O A HOH 629 ? ? 1.81 
2  1 OG  B SER 42  ? ? O B HOH 401 ? ? 1.95 
3  1 OE1 B GLN 82  ? ? O B HOH 402 ? ? 1.97 
4  1 OD2 B ASP 75  ? ? O B HOH 403 ? ? 2.03 
5  1 OD1 D ASN 98  ? ? O D HOH 401 ? ? 2.04 
6  1 O   A HOH 654 ? ? O A HOH 667 ? ? 2.07 
7  1 OD2 C ASP 253 ? A O C HOH 401 ? ? 2.09 
8  1 CE1 B PHE 252 ? ? O A HOH 629 ? ? 2.10 
9  1 OD1 C ASP 253 ? A O C HOH 402 ? ? 2.10 
10 1 OD2 A ASP 253 ? ? O A HOH 401 ? ? 2.13 
11 1 OD2 C ASP 253 ? B O C HOH 403 ? ? 2.15 
12 1 O   A HOH 633 ? ? O B HOH 680 ? ? 2.19 
# 
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 33  ? ? CD2 A HIS 33  ? ? 1.421 1.354 0.067 0.009 N 
2 1 CG A HIS 120 ? ? CD2 A HIS 120 ? ? 1.434 1.354 0.080 0.009 N 
3 1 CG B HIS 91  ? ? CD2 B HIS 91  ? ? 1.430 1.354 0.076 0.009 N 
4 1 CG B HIS 164 ? ? CD2 B HIS 164 ? ? 1.409 1.354 0.055 0.009 N 
5 1 CG D HIS 77  ? ? CD2 D HIS 77  ? ? 1.419 1.354 0.065 0.009 N 
6 1 CG D HIS 91  ? ? CD2 D HIS 91  ? ? 1.419 1.354 0.065 0.009 N 
7 1 CG D HIS 93  ? ? CD2 D HIS 93  ? ? 1.411 1.354 0.057 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             B 
_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             B 
_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             B 
_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                116.35 
_pdbx_validate_rmsd_angle.angle_target_value         120.30 
_pdbx_validate_rmsd_angle.angle_deviation            -3.95 
_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 A 99  ? ? -153.96 71.05   
2  1 ASN A 245 ? ? -94.33  50.03   
3  1 ASP B 99  ? ? -152.97 83.51   
4  1 ASN B 245 ? ? -95.48  57.47   
5  1 GLU B 254 ? ? 76.34   -1.46   
6  1 PHE C 7   ? A -169.39 -157.43 
7  1 THR C 88  ? ? -133.94 -41.92  
8  1 ASP C 99  ? ? -150.29 80.11   
9  1 ASN C 245 ? ? -91.35  54.98   
10 1 ASP C 253 ? A 8.69    111.37  
11 1 ASP D 99  ? ? -154.47 80.34   
12 1 ASN D 245 ? ? -94.44  55.86   
# 
_pdbx_validate_peptide_omega.id               1 
_pdbx_validate_peptide_omega.PDB_model_num    1 
_pdbx_validate_peptide_omega.auth_comp_id_1   SER 
_pdbx_validate_peptide_omega.auth_asym_id_1   D 
_pdbx_validate_peptide_omega.auth_seq_id_1    262 
_pdbx_validate_peptide_omega.PDB_ins_code_1   ? 
_pdbx_validate_peptide_omega.label_alt_id_1   ? 
_pdbx_validate_peptide_omega.auth_comp_id_2   GLN 
_pdbx_validate_peptide_omega.auth_asym_id_2   D 
_pdbx_validate_peptide_omega.auth_seq_id_2    263 
_pdbx_validate_peptide_omega.PDB_ins_code_2   ? 
_pdbx_validate_peptide_omega.label_alt_id_2   ? 
_pdbx_validate_peptide_omega.omega            145.44 
# 
_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 ? B HOH 734 ? 5.83 . 
2 1 O ? D HOH 724 ? 5.93 . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A MET 1 ? A MET 1 
2 1 Y 1 A SER 2 ? A SER 2 
3 1 Y 1 B MET 1 ? B MET 1 
4 1 Y 1 B SER 2 ? B SER 2 
5 1 Y 1 C MET 1 ? C MET 1 
6 1 Y 1 C SER 2 ? C SER 2 
7 1 Y 1 D MET 1 ? D MET 1 
8 1 Y 1 D SER 2 ? D SER 2 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
6YQ CL1  CL N N 1   
6YQ C6   C  Y N 2   
6YQ C1   C  Y N 3   
6YQ S7   S  N N 4   
6YQ O9   O  N N 5   
6YQ N10  N  N N 6   
6YQ O8   O  N N 7   
6YQ C5   C  Y N 8   
6YQ C4   C  Y N 9   
6YQ C3   C  Y N 10  
6YQ C2   C  Y N 11  
6YQ C11  C  N N 12  
6YQ O12  O  N N 13  
6YQ C13  C  N N 14  
6YQ N14  N  Y N 15  
6YQ C18  C  Y N 16  
6YQ C20  C  Y N 17  
6YQ C21  C  Y N 18  
6YQ C22  C  Y N 19  
6YQ C23  C  Y N 20  
6YQ C19  C  Y N 21  
6YQ N17  N  Y N 22  
6YQ C16  C  Y N 23  
6YQ H1   H  N N 24  
6YQ H2   H  N N 25  
6YQ H3   H  N N 26  
6YQ H4   H  N N 27  
6YQ H5   H  N N 28  
6YQ H6   H  N N 29  
6YQ H7   H  N N 30  
6YQ H8   H  N N 31  
6YQ H9   H  N N 32  
6YQ H10  H  N N 33  
6YQ H11  H  N N 34  
6YQ H12  H  N N 35  
ALA N    N  N N 36  
ALA CA   C  N S 37  
ALA C    C  N N 38  
ALA O    O  N N 39  
ALA CB   C  N N 40  
ALA OXT  O  N N 41  
ALA H    H  N N 42  
ALA H2   H  N N 43  
ALA HA   H  N N 44  
ALA HB1  H  N N 45  
ALA HB2  H  N N 46  
ALA HB3  H  N N 47  
ALA HXT  H  N N 48  
ARG N    N  N N 49  
ARG CA   C  N S 50  
ARG C    C  N N 51  
ARG O    O  N N 52  
ARG CB   C  N N 53  
ARG CG   C  N N 54  
ARG CD   C  N N 55  
ARG NE   N  N N 56  
ARG CZ   C  N N 57  
ARG NH1  N  N N 58  
ARG NH2  N  N N 59  
ARG OXT  O  N N 60  
ARG H    H  N N 61  
ARG H2   H  N N 62  
ARG HA   H  N N 63  
ARG HB2  H  N N 64  
ARG HB3  H  N N 65  
ARG HG2  H  N N 66  
ARG HG3  H  N N 67  
ARG HD2  H  N N 68  
ARG HD3  H  N N 69  
ARG HE   H  N N 70  
ARG HH11 H  N N 71  
ARG HH12 H  N N 72  
ARG HH21 H  N N 73  
ARG HH22 H  N N 74  
ARG HXT  H  N N 75  
ASN N    N  N N 76  
ASN CA   C  N S 77  
ASN C    C  N N 78  
ASN O    O  N N 79  
ASN CB   C  N N 80  
ASN CG   C  N N 81  
ASN OD1  O  N N 82  
ASN ND2  N  N N 83  
ASN OXT  O  N N 84  
ASN H    H  N N 85  
ASN H2   H  N N 86  
ASN HA   H  N N 87  
ASN HB2  H  N N 88  
ASN HB3  H  N N 89  
ASN HD21 H  N N 90  
ASN HD22 H  N N 91  
ASN HXT  H  N N 92  
ASP N    N  N N 93  
ASP CA   C  N S 94  
ASP C    C  N N 95  
ASP O    O  N N 96  
ASP CB   C  N N 97  
ASP CG   C  N N 98  
ASP OD1  O  N N 99  
ASP OD2  O  N N 100 
ASP OXT  O  N N 101 
ASP H    H  N N 102 
ASP H2   H  N N 103 
ASP HA   H  N N 104 
ASP HB2  H  N N 105 
ASP HB3  H  N N 106 
ASP HD2  H  N N 107 
ASP HXT  H  N N 108 
CYS N    N  N N 109 
CYS CA   C  N R 110 
CYS C    C  N N 111 
CYS O    O  N N 112 
CYS CB   C  N N 113 
CYS SG   S  N N 114 
CYS OXT  O  N N 115 
CYS H    H  N N 116 
CYS H2   H  N N 117 
CYS HA   H  N N 118 
CYS HB2  H  N N 119 
CYS HB3  H  N N 120 
CYS HG   H  N N 121 
CYS HXT  H  N N 122 
EDO C1   C  N N 123 
EDO O1   O  N N 124 
EDO C2   C  N N 125 
EDO O2   O  N N 126 
EDO H11  H  N N 127 
EDO H12  H  N N 128 
EDO HO1  H  N N 129 
EDO H21  H  N N 130 
EDO H22  H  N N 131 
EDO HO2  H  N N 132 
GLN N    N  N N 133 
GLN CA   C  N S 134 
GLN C    C  N N 135 
GLN O    O  N N 136 
GLN CB   C  N N 137 
GLN CG   C  N N 138 
GLN CD   C  N N 139 
GLN OE1  O  N N 140 
GLN NE2  N  N N 141 
GLN OXT  O  N N 142 
GLN H    H  N N 143 
GLN H2   H  N N 144 
GLN HA   H  N N 145 
GLN HB2  H  N N 146 
GLN HB3  H  N N 147 
GLN HG2  H  N N 148 
GLN HG3  H  N N 149 
GLN HE21 H  N N 150 
GLN HE22 H  N N 151 
GLN HXT  H  N N 152 
GLU N    N  N N 153 
GLU CA   C  N S 154 
GLU C    C  N N 155 
GLU O    O  N N 156 
GLU CB   C  N N 157 
GLU CG   C  N N 158 
GLU CD   C  N N 159 
GLU OE1  O  N N 160 
GLU OE2  O  N N 161 
GLU OXT  O  N N 162 
GLU H    H  N N 163 
GLU H2   H  N N 164 
GLU HA   H  N N 165 
GLU HB2  H  N N 166 
GLU HB3  H  N N 167 
GLU HG2  H  N N 168 
GLU HG3  H  N N 169 
GLU HE2  H  N N 170 
GLU HXT  H  N N 171 
GLY N    N  N N 172 
GLY CA   C  N N 173 
GLY C    C  N N 174 
GLY O    O  N N 175 
GLY OXT  O  N N 176 
GLY H    H  N N 177 
GLY H2   H  N N 178 
GLY HA2  H  N N 179 
GLY HA3  H  N N 180 
GLY HXT  H  N N 181 
HIS N    N  N N 182 
HIS CA   C  N S 183 
HIS C    C  N N 184 
HIS O    O  N N 185 
HIS CB   C  N N 186 
HIS CG   C  Y N 187 
HIS ND1  N  Y N 188 
HIS CD2  C  Y N 189 
HIS CE1  C  Y N 190 
HIS NE2  N  Y N 191 
HIS OXT  O  N N 192 
HIS H    H  N N 193 
HIS H2   H  N N 194 
HIS HA   H  N N 195 
HIS HB2  H  N N 196 
HIS HB3  H  N N 197 
HIS HD1  H  N N 198 
HIS HD2  H  N N 199 
HIS HE1  H  N N 200 
HIS HE2  H  N N 201 
HIS HXT  H  N N 202 
HOH O    O  N N 203 
HOH H1   H  N N 204 
HOH H2   H  N N 205 
ILE N    N  N N 206 
ILE CA   C  N S 207 
ILE C    C  N N 208 
ILE O    O  N N 209 
ILE CB   C  N S 210 
ILE CG1  C  N N 211 
ILE CG2  C  N N 212 
ILE CD1  C  N N 213 
ILE OXT  O  N N 214 
ILE H    H  N N 215 
ILE H2   H  N N 216 
ILE HA   H  N N 217 
ILE HB   H  N N 218 
ILE HG12 H  N N 219 
ILE HG13 H  N N 220 
ILE HG21 H  N N 221 
ILE HG22 H  N N 222 
ILE HG23 H  N N 223 
ILE HD11 H  N N 224 
ILE HD12 H  N N 225 
ILE HD13 H  N N 226 
ILE HXT  H  N N 227 
LEU N    N  N N 228 
LEU CA   C  N S 229 
LEU C    C  N N 230 
LEU O    O  N N 231 
LEU CB   C  N N 232 
LEU CG   C  N N 233 
LEU CD1  C  N N 234 
LEU CD2  C  N N 235 
LEU OXT  O  N N 236 
LEU H    H  N N 237 
LEU H2   H  N N 238 
LEU HA   H  N N 239 
LEU HB2  H  N N 240 
LEU HB3  H  N N 241 
LEU HG   H  N N 242 
LEU HD11 H  N N 243 
LEU HD12 H  N N 244 
LEU HD13 H  N N 245 
LEU HD21 H  N N 246 
LEU HD22 H  N N 247 
LEU HD23 H  N N 248 
LEU HXT  H  N N 249 
LYS N    N  N N 250 
LYS CA   C  N S 251 
LYS C    C  N N 252 
LYS O    O  N N 253 
LYS CB   C  N N 254 
LYS CG   C  N N 255 
LYS CD   C  N N 256 
LYS CE   C  N N 257 
LYS NZ   N  N N 258 
LYS OXT  O  N N 259 
LYS H    H  N N 260 
LYS H2   H  N N 261 
LYS HA   H  N N 262 
LYS HB2  H  N N 263 
LYS HB3  H  N N 264 
LYS HG2  H  N N 265 
LYS HG3  H  N N 266 
LYS HD2  H  N N 267 
LYS HD3  H  N N 268 
LYS HE2  H  N N 269 
LYS HE3  H  N N 270 
LYS HZ1  H  N N 271 
LYS HZ2  H  N N 272 
LYS HZ3  H  N N 273 
LYS HXT  H  N N 274 
MET N    N  N N 275 
MET CA   C  N S 276 
MET C    C  N N 277 
MET O    O  N N 278 
MET CB   C  N N 279 
MET CG   C  N N 280 
MET SD   S  N N 281 
MET CE   C  N N 282 
MET OXT  O  N N 283 
MET H    H  N N 284 
MET H2   H  N N 285 
MET HA   H  N N 286 
MET HB2  H  N N 287 
MET HB3  H  N N 288 
MET HG2  H  N N 289 
MET HG3  H  N N 290 
MET HE1  H  N N 291 
MET HE2  H  N N 292 
MET HE3  H  N N 293 
MET HXT  H  N N 294 
PHE N    N  N N 295 
PHE CA   C  N S 296 
PHE C    C  N N 297 
PHE O    O  N N 298 
PHE CB   C  N N 299 
PHE CG   C  Y N 300 
PHE CD1  C  Y N 301 
PHE CD2  C  Y N 302 
PHE CE1  C  Y N 303 
PHE CE2  C  Y N 304 
PHE CZ   C  Y N 305 
PHE OXT  O  N N 306 
PHE H    H  N N 307 
PHE H2   H  N N 308 
PHE HA   H  N N 309 
PHE HB2  H  N N 310 
PHE HB3  H  N N 311 
PHE HD1  H  N N 312 
PHE HD2  H  N N 313 
PHE HE1  H  N N 314 
PHE HE2  H  N N 315 
PHE HZ   H  N N 316 
PHE HXT  H  N N 317 
PRO N    N  N N 318 
PRO CA   C  N S 319 
PRO C    C  N N 320 
PRO O    O  N N 321 
PRO CB   C  N N 322 
PRO CG   C  N N 323 
PRO CD   C  N N 324 
PRO OXT  O  N N 325 
PRO H    H  N N 326 
PRO HA   H  N N 327 
PRO HB2  H  N N 328 
PRO HB3  H  N N 329 
PRO HG2  H  N N 330 
PRO HG3  H  N N 331 
PRO HD2  H  N N 332 
PRO HD3  H  N N 333 
PRO HXT  H  N N 334 
SER N    N  N N 335 
SER CA   C  N S 336 
SER C    C  N N 337 
SER O    O  N N 338 
SER CB   C  N N 339 
SER OG   O  N N 340 
SER OXT  O  N N 341 
SER H    H  N N 342 
SER H2   H  N N 343 
SER HA   H  N N 344 
SER HB2  H  N N 345 
SER HB3  H  N N 346 
SER HG   H  N N 347 
SER HXT  H  N N 348 
SO4 S    S  N N 349 
SO4 O1   O  N N 350 
SO4 O2   O  N N 351 
SO4 O3   O  N N 352 
SO4 O4   O  N N 353 
THR N    N  N N 354 
THR CA   C  N S 355 
THR C    C  N N 356 
THR O    O  N N 357 
THR CB   C  N R 358 
THR OG1  O  N N 359 
THR CG2  C  N N 360 
THR OXT  O  N N 361 
THR H    H  N N 362 
THR H2   H  N N 363 
THR HA   H  N N 364 
THR HB   H  N N 365 
THR HG1  H  N N 366 
THR HG21 H  N N 367 
THR HG22 H  N N 368 
THR HG23 H  N N 369 
THR HXT  H  N N 370 
TRP N    N  N N 371 
TRP CA   C  N S 372 
TRP C    C  N N 373 
TRP O    O  N N 374 
TRP CB   C  N N 375 
TRP CG   C  Y N 376 
TRP CD1  C  Y N 377 
TRP CD2  C  Y N 378 
TRP NE1  N  Y N 379 
TRP CE2  C  Y N 380 
TRP CE3  C  Y N 381 
TRP CZ2  C  Y N 382 
TRP CZ3  C  Y N 383 
TRP CH2  C  Y N 384 
TRP OXT  O  N N 385 
TRP H    H  N N 386 
TRP H2   H  N N 387 
TRP HA   H  N N 388 
TRP HB2  H  N N 389 
TRP HB3  H  N N 390 
TRP HD1  H  N N 391 
TRP HE1  H  N N 392 
TRP HE3  H  N N 393 
TRP HZ2  H  N N 394 
TRP HZ3  H  N N 395 
TRP HH2  H  N N 396 
TRP HXT  H  N N 397 
TYR N    N  N N 398 
TYR CA   C  N S 399 
TYR C    C  N N 400 
TYR O    O  N N 401 
TYR CB   C  N N 402 
TYR CG   C  Y N 403 
TYR CD1  C  Y N 404 
TYR CD2  C  Y N 405 
TYR CE1  C  Y N 406 
TYR CE2  C  Y N 407 
TYR CZ   C  Y N 408 
TYR OH   O  N N 409 
TYR OXT  O  N N 410 
TYR H    H  N N 411 
TYR H2   H  N N 412 
TYR HA   H  N N 413 
TYR HB2  H  N N 414 
TYR HB3  H  N N 415 
TYR HD1  H  N N 416 
TYR HD2  H  N N 417 
TYR HE1  H  N N 418 
TYR HE2  H  N N 419 
TYR HH   H  N N 420 
TYR HXT  H  N N 421 
VAL N    N  N N 422 
VAL CA   C  N S 423 
VAL C    C  N N 424 
VAL O    O  N N 425 
VAL CB   C  N N 426 
VAL CG1  C  N N 427 
VAL CG2  C  N N 428 
VAL OXT  O  N N 429 
VAL H    H  N N 430 
VAL H2   H  N N 431 
VAL HA   H  N N 432 
VAL HB   H  N N 433 
VAL HG11 H  N N 434 
VAL HG12 H  N N 435 
VAL HG13 H  N N 436 
VAL HG21 H  N N 437 
VAL HG22 H  N N 438 
VAL HG23 H  N N 439 
VAL HXT  H  N N 440 
ZN  ZN   ZN N N 441 
# 
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 
6YQ C13 N14  sing N N 1   
6YQ C13 C11  sing N N 2   
6YQ C3  C2   doub Y N 3   
6YQ C3  C4   sing Y N 4   
6YQ C16 N14  sing Y N 5   
6YQ C16 N17  doub Y N 6   
6YQ N14 C18  sing Y N 7   
6YQ C2  C1   sing Y N 8   
6YQ N10 S7   sing N N 9   
6YQ N17 C19  sing Y N 10  
6YQ C18 C19  doub Y N 11  
6YQ C18 C20  sing Y N 12  
6YQ C19 C23  sing Y N 13  
6YQ C20 C21  doub Y N 14  
6YQ C11 C4   sing N N 15  
6YQ C11 O12  doub N N 16  
6YQ C4  C5   doub Y N 17  
6YQ C23 C22  doub Y N 18  
6YQ C21 C22  sing Y N 19  
6YQ C1  S7   sing N N 20  
6YQ C1  C6   doub Y N 21  
6YQ S7  O8   doub N N 22  
6YQ S7  O9   doub N N 23  
6YQ C5  C6   sing Y N 24  
6YQ C6  CL1  sing N N 25  
6YQ N10 H1   sing N N 26  
6YQ N10 H2   sing N N 27  
6YQ C5  H3   sing N N 28  
6YQ C3  H4   sing N N 29  
6YQ C2  H5   sing N N 30  
6YQ C13 H6   sing N N 31  
6YQ C13 H7   sing N N 32  
6YQ C20 H8   sing N N 33  
6YQ C21 H9   sing N N 34  
6YQ C22 H10  sing N N 35  
6YQ C23 H11  sing N N 36  
6YQ C16 H12  sing N N 37  
ALA N   CA   sing N N 38  
ALA N   H    sing N N 39  
ALA N   H2   sing N N 40  
ALA CA  C    sing N N 41  
ALA CA  CB   sing N N 42  
ALA CA  HA   sing N N 43  
ALA C   O    doub N N 44  
ALA C   OXT  sing N N 45  
ALA CB  HB1  sing N N 46  
ALA CB  HB2  sing N N 47  
ALA CB  HB3  sing N N 48  
ALA OXT HXT  sing N N 49  
ARG N   CA   sing N N 50  
ARG N   H    sing N N 51  
ARG N   H2   sing N N 52  
ARG CA  C    sing N N 53  
ARG CA  CB   sing N N 54  
ARG CA  HA   sing N N 55  
ARG C   O    doub N N 56  
ARG C   OXT  sing N N 57  
ARG CB  CG   sing N N 58  
ARG CB  HB2  sing N N 59  
ARG CB  HB3  sing N N 60  
ARG CG  CD   sing N N 61  
ARG CG  HG2  sing N N 62  
ARG CG  HG3  sing N N 63  
ARG CD  NE   sing N N 64  
ARG CD  HD2  sing N N 65  
ARG CD  HD3  sing N N 66  
ARG NE  CZ   sing N N 67  
ARG NE  HE   sing N N 68  
ARG CZ  NH1  sing N N 69  
ARG CZ  NH2  doub N N 70  
ARG NH1 HH11 sing N N 71  
ARG NH1 HH12 sing N N 72  
ARG NH2 HH21 sing N N 73  
ARG NH2 HH22 sing N N 74  
ARG OXT HXT  sing N N 75  
ASN N   CA   sing N N 76  
ASN N   H    sing N N 77  
ASN N   H2   sing N N 78  
ASN CA  C    sing N N 79  
ASN CA  CB   sing N N 80  
ASN CA  HA   sing N N 81  
ASN C   O    doub N N 82  
ASN C   OXT  sing N N 83  
ASN CB  CG   sing N N 84  
ASN CB  HB2  sing N N 85  
ASN CB  HB3  sing N N 86  
ASN CG  OD1  doub N N 87  
ASN CG  ND2  sing N N 88  
ASN ND2 HD21 sing N N 89  
ASN ND2 HD22 sing N N 90  
ASN OXT HXT  sing N N 91  
ASP N   CA   sing N N 92  
ASP N   H    sing N N 93  
ASP N   H2   sing N N 94  
ASP CA  C    sing N N 95  
ASP CA  CB   sing N N 96  
ASP CA  HA   sing N N 97  
ASP C   O    doub N N 98  
ASP C   OXT  sing N N 99  
ASP CB  CG   sing N N 100 
ASP CB  HB2  sing N N 101 
ASP CB  HB3  sing N N 102 
ASP CG  OD1  doub N N 103 
ASP CG  OD2  sing N N 104 
ASP OD2 HD2  sing N N 105 
ASP OXT HXT  sing N N 106 
CYS N   CA   sing N N 107 
CYS N   H    sing N N 108 
CYS N   H2   sing N N 109 
CYS CA  C    sing N N 110 
CYS CA  CB   sing N N 111 
CYS CA  HA   sing N N 112 
CYS C   O    doub N N 113 
CYS C   OXT  sing N N 114 
CYS CB  SG   sing N N 115 
CYS CB  HB2  sing N N 116 
CYS CB  HB3  sing N N 117 
CYS SG  HG   sing N N 118 
CYS OXT HXT  sing N N 119 
EDO C1  O1   sing N N 120 
EDO C1  C2   sing N N 121 
EDO C1  H11  sing N N 122 
EDO C1  H12  sing N N 123 
EDO O1  HO1  sing N N 124 
EDO C2  O2   sing N N 125 
EDO C2  H21  sing N N 126 
EDO C2  H22  sing N N 127 
EDO O2  HO2  sing N N 128 
GLN N   CA   sing N N 129 
GLN N   H    sing N N 130 
GLN N   H2   sing N N 131 
GLN CA  C    sing N N 132 
GLN CA  CB   sing N N 133 
GLN CA  HA   sing N N 134 
GLN C   O    doub N N 135 
GLN C   OXT  sing N N 136 
GLN CB  CG   sing N N 137 
GLN CB  HB2  sing N N 138 
GLN CB  HB3  sing N N 139 
GLN CG  CD   sing N N 140 
GLN CG  HG2  sing N N 141 
GLN CG  HG3  sing N N 142 
GLN CD  OE1  doub N N 143 
GLN CD  NE2  sing N N 144 
GLN NE2 HE21 sing N N 145 
GLN NE2 HE22 sing N N 146 
GLN OXT HXT  sing N N 147 
GLU N   CA   sing N N 148 
GLU N   H    sing N N 149 
GLU N   H2   sing N N 150 
GLU CA  C    sing N N 151 
GLU CA  CB   sing N N 152 
GLU CA  HA   sing N N 153 
GLU C   O    doub N N 154 
GLU C   OXT  sing N N 155 
GLU CB  CG   sing N N 156 
GLU CB  HB2  sing N N 157 
GLU CB  HB3  sing N N 158 
GLU CG  CD   sing N N 159 
GLU CG  HG2  sing N N 160 
GLU CG  HG3  sing N N 161 
GLU CD  OE1  doub N N 162 
GLU CD  OE2  sing N N 163 
GLU OE2 HE2  sing N N 164 
GLU OXT HXT  sing N N 165 
GLY N   CA   sing N N 166 
GLY N   H    sing N N 167 
GLY N   H2   sing N N 168 
GLY CA  C    sing N N 169 
GLY CA  HA2  sing N N 170 
GLY CA  HA3  sing N N 171 
GLY C   O    doub N N 172 
GLY C   OXT  sing N N 173 
GLY OXT HXT  sing N N 174 
HIS N   CA   sing N N 175 
HIS N   H    sing N N 176 
HIS N   H2   sing N N 177 
HIS CA  C    sing N N 178 
HIS CA  CB   sing N N 179 
HIS CA  HA   sing N N 180 
HIS C   O    doub N N 181 
HIS C   OXT  sing N N 182 
HIS CB  CG   sing N N 183 
HIS CB  HB2  sing N N 184 
HIS CB  HB3  sing N N 185 
HIS CG  ND1  sing Y N 186 
HIS CG  CD2  doub Y N 187 
HIS ND1 CE1  doub Y N 188 
HIS ND1 HD1  sing N N 189 
HIS CD2 NE2  sing Y N 190 
HIS CD2 HD2  sing N N 191 
HIS CE1 NE2  sing Y N 192 
HIS CE1 HE1  sing N N 193 
HIS NE2 HE2  sing N N 194 
HIS OXT HXT  sing N N 195 
HOH O   H1   sing N N 196 
HOH O   H2   sing N N 197 
ILE N   CA   sing N N 198 
ILE N   H    sing N N 199 
ILE N   H2   sing N N 200 
ILE CA  C    sing N N 201 
ILE CA  CB   sing N N 202 
ILE CA  HA   sing N N 203 
ILE C   O    doub N N 204 
ILE C   OXT  sing N N 205 
ILE CB  CG1  sing N N 206 
ILE CB  CG2  sing N N 207 
ILE CB  HB   sing N N 208 
ILE CG1 CD1  sing N N 209 
ILE CG1 HG12 sing N N 210 
ILE CG1 HG13 sing N N 211 
ILE CG2 HG21 sing N N 212 
ILE CG2 HG22 sing N N 213 
ILE CG2 HG23 sing N N 214 
ILE CD1 HD11 sing N N 215 
ILE CD1 HD12 sing N N 216 
ILE CD1 HD13 sing N N 217 
ILE OXT HXT  sing N N 218 
LEU N   CA   sing N N 219 
LEU N   H    sing N N 220 
LEU N   H2   sing N N 221 
LEU CA  C    sing N N 222 
LEU CA  CB   sing N N 223 
LEU CA  HA   sing N N 224 
LEU C   O    doub N N 225 
LEU C   OXT  sing N N 226 
LEU CB  CG   sing N N 227 
LEU CB  HB2  sing N N 228 
LEU CB  HB3  sing N N 229 
LEU CG  CD1  sing N N 230 
LEU CG  CD2  sing N N 231 
LEU CG  HG   sing N N 232 
LEU CD1 HD11 sing N N 233 
LEU CD1 HD12 sing N N 234 
LEU CD1 HD13 sing N N 235 
LEU CD2 HD21 sing N N 236 
LEU CD2 HD22 sing N N 237 
LEU CD2 HD23 sing N N 238 
LEU OXT HXT  sing N N 239 
LYS N   CA   sing N N 240 
LYS N   H    sing N N 241 
LYS N   H2   sing N N 242 
LYS CA  C    sing N N 243 
LYS CA  CB   sing N N 244 
LYS CA  HA   sing N N 245 
LYS C   O    doub N N 246 
LYS C   OXT  sing N N 247 
LYS CB  CG   sing N N 248 
LYS CB  HB2  sing N N 249 
LYS CB  HB3  sing N N 250 
LYS CG  CD   sing N N 251 
LYS CG  HG2  sing N N 252 
LYS CG  HG3  sing N N 253 
LYS CD  CE   sing N N 254 
LYS CD  HD2  sing N N 255 
LYS CD  HD3  sing N N 256 
LYS CE  NZ   sing N N 257 
LYS CE  HE2  sing N N 258 
LYS CE  HE3  sing N N 259 
LYS NZ  HZ1  sing N N 260 
LYS NZ  HZ2  sing N N 261 
LYS NZ  HZ3  sing N N 262 
LYS OXT HXT  sing N N 263 
MET N   CA   sing N N 264 
MET N   H    sing N N 265 
MET N   H2   sing N N 266 
MET CA  C    sing N N 267 
MET CA  CB   sing N N 268 
MET CA  HA   sing N N 269 
MET C   O    doub N N 270 
MET C   OXT  sing N N 271 
MET CB  CG   sing N N 272 
MET CB  HB2  sing N N 273 
MET CB  HB3  sing N N 274 
MET CG  SD   sing N N 275 
MET CG  HG2  sing N N 276 
MET CG  HG3  sing N N 277 
MET SD  CE   sing N N 278 
MET CE  HE1  sing N N 279 
MET CE  HE2  sing N N 280 
MET CE  HE3  sing N N 281 
MET OXT HXT  sing N N 282 
PHE N   CA   sing N N 283 
PHE N   H    sing N N 284 
PHE N   H2   sing N N 285 
PHE CA  C    sing N N 286 
PHE CA  CB   sing N N 287 
PHE CA  HA   sing N N 288 
PHE C   O    doub N N 289 
PHE C   OXT  sing N N 290 
PHE CB  CG   sing N N 291 
PHE CB  HB2  sing N N 292 
PHE CB  HB3  sing N N 293 
PHE CG  CD1  doub Y N 294 
PHE CG  CD2  sing Y N 295 
PHE CD1 CE1  sing Y N 296 
PHE CD1 HD1  sing N N 297 
PHE CD2 CE2  doub Y N 298 
PHE CD2 HD2  sing N N 299 
PHE CE1 CZ   doub Y N 300 
PHE CE1 HE1  sing N N 301 
PHE CE2 CZ   sing Y N 302 
PHE CE2 HE2  sing N N 303 
PHE CZ  HZ   sing N N 304 
PHE OXT HXT  sing N N 305 
PRO N   CA   sing N N 306 
PRO N   CD   sing N N 307 
PRO N   H    sing N N 308 
PRO CA  C    sing N N 309 
PRO CA  CB   sing N N 310 
PRO CA  HA   sing N N 311 
PRO C   O    doub N N 312 
PRO C   OXT  sing N N 313 
PRO CB  CG   sing N N 314 
PRO CB  HB2  sing N N 315 
PRO CB  HB3  sing N N 316 
PRO CG  CD   sing N N 317 
PRO CG  HG2  sing N N 318 
PRO CG  HG3  sing N N 319 
PRO CD  HD2  sing N N 320 
PRO CD  HD3  sing N N 321 
PRO OXT HXT  sing N N 322 
SER N   CA   sing N N 323 
SER N   H    sing N N 324 
SER N   H2   sing N N 325 
SER CA  C    sing N N 326 
SER CA  CB   sing N N 327 
SER CA  HA   sing N N 328 
SER C   O    doub N N 329 
SER C   OXT  sing N N 330 
SER CB  OG   sing N N 331 
SER CB  HB2  sing N N 332 
SER CB  HB3  sing N N 333 
SER OG  HG   sing N N 334 
SER OXT HXT  sing N N 335 
SO4 S   O1   doub N N 336 
SO4 S   O2   doub N N 337 
SO4 S   O3   sing N N 338 
SO4 S   O4   sing N N 339 
THR N   CA   sing N N 340 
THR N   H    sing N N 341 
THR N   H2   sing N N 342 
THR CA  C    sing N N 343 
THR CA  CB   sing N N 344 
THR CA  HA   sing N N 345 
THR C   O    doub N N 346 
THR C   OXT  sing N N 347 
THR CB  OG1  sing N N 348 
THR CB  CG2  sing N N 349 
THR CB  HB   sing N N 350 
THR OG1 HG1  sing N N 351 
THR CG2 HG21 sing N N 352 
THR CG2 HG22 sing N N 353 
THR CG2 HG23 sing N N 354 
THR OXT HXT  sing N N 355 
TRP N   CA   sing N N 356 
TRP N   H    sing N N 357 
TRP N   H2   sing N N 358 
TRP CA  C    sing N N 359 
TRP CA  CB   sing N N 360 
TRP CA  HA   sing N N 361 
TRP C   O    doub N N 362 
TRP C   OXT  sing N N 363 
TRP CB  CG   sing N N 364 
TRP CB  HB2  sing N N 365 
TRP CB  HB3  sing N N 366 
TRP CG  CD1  doub Y N 367 
TRP CG  CD2  sing Y N 368 
TRP CD1 NE1  sing Y N 369 
TRP CD1 HD1  sing N N 370 
TRP CD2 CE2  doub Y N 371 
TRP CD2 CE3  sing Y N 372 
TRP NE1 CE2  sing Y N 373 
TRP NE1 HE1  sing N N 374 
TRP CE2 CZ2  sing Y N 375 
TRP CE3 CZ3  doub Y N 376 
TRP CE3 HE3  sing N N 377 
TRP CZ2 CH2  doub Y N 378 
TRP CZ2 HZ2  sing N N 379 
TRP CZ3 CH2  sing Y N 380 
TRP CZ3 HZ3  sing N N 381 
TRP CH2 HH2  sing N N 382 
TRP OXT HXT  sing N N 383 
TYR N   CA   sing N N 384 
TYR N   H    sing N N 385 
TYR N   H2   sing N N 386 
TYR CA  C    sing N N 387 
TYR CA  CB   sing N N 388 
TYR CA  HA   sing N N 389 
TYR C   O    doub N N 390 
TYR C   OXT  sing N N 391 
TYR CB  CG   sing N N 392 
TYR CB  HB2  sing N N 393 
TYR CB  HB3  sing N N 394 
TYR CG  CD1  doub Y N 395 
TYR CG  CD2  sing Y N 396 
TYR CD1 CE1  sing Y N 397 
TYR CD1 HD1  sing N N 398 
TYR CD2 CE2  doub Y N 399 
TYR CD2 HD2  sing N N 400 
TYR CE1 CZ   doub Y N 401 
TYR CE1 HE1  sing N N 402 
TYR CE2 CZ   sing Y N 403 
TYR CE2 HE2  sing N N 404 
TYR CZ  OH   sing N N 405 
TYR OH  HH   sing N N 406 
TYR OXT HXT  sing N N 407 
VAL N   CA   sing N N 408 
VAL N   H    sing N N 409 
VAL N   H2   sing N N 410 
VAL CA  C    sing N N 411 
VAL CA  CB   sing N N 412 
VAL CA  HA   sing N N 413 
VAL C   O    doub N N 414 
VAL C   OXT  sing N N 415 
VAL CB  CG1  sing N N 416 
VAL CB  CG2  sing N N 417 
VAL CB  HB   sing N N 418 
VAL CG1 HG11 sing N N 419 
VAL CG1 HG12 sing N N 420 
VAL CG1 HG13 sing N N 421 
VAL CG2 HG21 sing N N 422 
VAL CG2 HG22 sing N N 423 
VAL CG2 HG23 sing N N 424 
VAL OXT HXT  sing N N 425 
# 
_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                    5LL9 
_atom_sites.fract_transf_matrix[1][1]   0.012937 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.004394 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.013534 
_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]   0.011569 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
# 
loop_
_atom_type.symbol 
C  
CL 
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . LYS A  1 3   ? 17.020  17.259  18.503  1.00 46.79 ? 3   LYS A N   1 
ATOM   2    C  CA  . LYS A  1 3   ? 17.810  16.097  17.989  1.00 41.60 ? 3   LYS A CA  1 
ATOM   3    C  C   . LYS A  1 3   ? 16.949  14.832  17.900  1.00 33.91 ? 3   LYS A C   1 
ATOM   4    O  O   . LYS A  1 3   ? 16.020  14.597  18.701  1.00 36.99 ? 3   LYS A O   1 
ATOM   5    C  CB  . LYS A  1 3   ? 19.027  15.805  18.858  1.00 45.74 ? 3   LYS A CB  1 
ATOM   6    C  CG  . LYS A  1 3   ? 20.136  15.101  18.110  1.00 47.58 ? 3   LYS A CG  1 
ATOM   7    C  CD  . LYS A  1 3   ? 20.951  14.222  19.038  1.00 53.46 ? 3   LYS A CD  1 
ATOM   8    C  CE  . LYS A  1 3   ? 22.373  14.088  18.505  1.00 55.08 ? 3   LYS A CE  1 
ATOM   9    N  NZ  . LYS A  1 3   ? 22.430  13.618  17.087  1.00 50.67 ? 3   LYS A NZ  1 
ATOM   10   N  N   . TRP A  1 4   ? 17.334  13.987  16.958  1.00 21.67 ? 4   TRP A N   1 
ATOM   11   C  CA  . TRP A  1 4   ? 16.456  12.930  16.499  1.00 16.98 ? 4   TRP A CA  1 
ATOM   12   C  C   . TRP A  1 4   ? 16.412  11.810  17.464  1.00 16.92 ? 4   TRP A C   1 
ATOM   13   O  O   . TRP A  1 4   ? 17.413  11.567  18.229  1.00 17.29 ? 4   TRP A O   1 
ATOM   14   C  CB  . TRP A  1 4   ? 16.988  12.478  15.160  1.00 15.03 ? 4   TRP A CB  1 
ATOM   15   C  CG  . TRP A  1 4   ? 18.350  11.862  15.109  1.00 13.92 ? 4   TRP A CG  1 
ATOM   16   C  CD1 . TRP A  1 4   ? 19.585  12.444  14.828  1.00 14.09 ? 4   TRP A CD1 1 
ATOM   17   C  CD2 . TRP A  1 4   ? 18.617  10.424  15.195  1.00 12.74 ? 4   TRP A CD2 1 
ATOM   18   N  NE1 . TRP A  1 4   ? 20.575  11.489  14.791  1.00 15.17 ? 4   TRP A NE1 1 
ATOM   19   C  CE2 . TRP A  1 4   ? 20.045  10.242  15.038  1.00 12.38 ? 4   TRP A CE2 1 
ATOM   20   C  CE3 . TRP A  1 4   ? 17.822  9.324   15.390  1.00 12.38 ? 4   TRP A CE3 1 
ATOM   21   C  CZ2 . TRP A  1 4   ? 20.605  8.956   15.049  1.00 12.68 ? 4   TRP A CZ2 1 
ATOM   22   C  CZ3 . TRP A  1 4   ? 18.378  8.057   15.404  1.00 13.06 ? 4   TRP A CZ3 1 
ATOM   23   C  CH2 . TRP A  1 4   ? 19.737  7.880   15.248  1.00 12.74 ? 4   TRP A CH2 1 
ATOM   24   N  N   . THR A  1 5   ? 15.279  11.135  17.448  1.00 15.67 ? 5   THR A N   1 
ATOM   25   C  CA  . THR A  1 5   ? 15.006  9.977   18.342  1.00 14.82 ? 5   THR A CA  1 
ATOM   26   C  C   . THR A  1 5   ? 14.223  8.880   17.605  1.00 14.11 ? 5   THR A C   1 
ATOM   27   O  O   . THR A  1 5   ? 13.928  8.983   16.418  1.00 13.85 ? 5   THR A O   1 
ATOM   28   C  CB  . THR A  1 5   ? 14.114  10.376  19.554  1.00 18.42 ? 5   THR A CB  1 
ATOM   29   O  OG1 . THR A  1 5   ? 12.839  10.735  19.018  1.00 20.50 ? 5   THR A OG1 1 
ATOM   30   C  CG2 . THR A  1 5   ? 14.706  11.625  20.223  1.00 20.12 ? 5   THR A CG2 1 
ATOM   31   N  N   . TYR A  1 6   ? 13.863  7.789   18.304  1.00 14.20 ? 6   TYR A N   1 
ATOM   32   C  CA  . TYR A  1 6   ? 12.988  6.751   17.722  1.00 14.03 ? 6   TYR A CA  1 
ATOM   33   C  C   . TYR A  1 6   ? 11.576  6.781   18.327  1.00 15.49 ? 6   TYR A C   1 
ATOM   34   O  O   . TYR A  1 6   ? 10.788  5.848   18.269  1.00 15.67 ? 6   TYR A O   1 
ATOM   35   C  CB  . TYR A  1 6   ? 13.595  5.368   17.968  1.00 13.17 ? 6   TYR A CB  1 
ATOM   36   C  CG  . TYR A  1 6   ? 14.870  5.141   17.191  1.00 11.87 ? 6   TYR A CG  1 
ATOM   37   C  CD1 . TYR A  1 6   ? 16.117  5.441   17.706  1.00 11.30 ? 6   TYR A CD1 1 
ATOM   38   C  CD2 . TYR A  1 6   ? 14.814  4.567   15.917  1.00 12.09 ? 6   TYR A CD2 1 
ATOM   39   C  CE1 . TYR A  1 6   ? 17.278  5.181   17.028  1.00 13.17 ? 6   TYR A CE1 1 
ATOM   40   C  CE2 . TYR A  1 6   ? 15.948  4.291   15.190  1.00 11.36 ? 6   TYR A CE2 1 
ATOM   41   C  CZ  . TYR A  1 6   ? 17.183  4.585   15.763  1.00 11.41 ? 6   TYR A CZ  1 
ATOM   42   O  OH  . TYR A  1 6   ? 18.261  4.285   15.032  1.00 12.16 ? 6   TYR A OH  1 
ATOM   43   N  N   . PHE A  1 7   ? 11.242  7.892   19.034  1.00 22.91 ? 7   PHE A N   1 
ATOM   44   C  CA  . PHE A  1 7   ? 9.945   7.964   19.736  1.00 27.94 ? 7   PHE A CA  1 
ATOM   45   C  C   . PHE A  1 7   ? 9.655   9.384   20.133  1.00 33.88 ? 7   PHE A C   1 
ATOM   46   O  O   . PHE A  1 7   ? 10.545  10.071  20.647  1.00 34.89 ? 7   PHE A O   1 
ATOM   47   C  CB  . PHE A  1 7   ? 9.953   7.058   20.997  1.00 33.44 ? 7   PHE A CB  1 
ATOM   48   C  CG  . PHE A  1 7   ? 8.686   7.139   21.879  1.00 40.91 ? 7   PHE A CG  1 
ATOM   49   C  CD1 . PHE A  1 7   ? 8.527   8.140   22.865  1.00 45.29 ? 7   PHE A CD1 1 
ATOM   50   C  CD2 . PHE A  1 7   ? 7.682   6.173   21.776  1.00 41.07 ? 7   PHE A CD2 1 
ATOM   51   C  CE1 . PHE A  1 7   ? 7.380   8.196   23.676  1.00 45.52 ? 7   PHE A CE1 1 
ATOM   52   C  CE2 . PHE A  1 7   ? 6.550   6.227   22.590  1.00 40.68 ? 7   PHE A CE2 1 
ATOM   53   C  CZ  . PHE A  1 7   ? 6.401   7.237   23.536  1.00 48.69 ? 7   PHE A CZ  1 
ATOM   54   N  N   . GLY A  1 8   ? 8.405   9.793   19.897  1.00 29.35 ? 8   GLY A N   1 
ATOM   55   C  CA  . GLY A  1 8   ? 7.855   11.092  20.392  1.00 26.63 ? 8   GLY A CA  1 
ATOM   56   C  C   . GLY A  1 8   ? 7.896   11.950  19.142  1.00 29.12 ? 8   GLY A C   1 
ATOM   57   O  O   . GLY A  1 8   ? 7.923   11.401  17.992  1.00 34.93 ? 8   GLY A O   1 
ATOM   58   N  N   . PRO A  1 9   ? 7.882   13.265  19.297  1.00 26.88 ? 9   PRO A N   1 
ATOM   59   C  CA  . PRO A  1 9   ? 7.748   14.024  18.049  1.00 27.04 ? 9   PRO A CA  1 
ATOM   60   C  C   . PRO A  1 9   ? 9.010   14.152  17.244  1.00 24.11 ? 9   PRO A C   1 
ATOM   61   O  O   . PRO A  1 9   ? 8.956   14.721  16.172  1.00 19.88 ? 9   PRO A O   1 
ATOM   62   C  CB  . PRO A  1 9   ? 7.380   15.447  18.518  1.00 31.91 ? 9   PRO A CB  1 
ATOM   63   C  CG  . PRO A  1 9   ? 7.908   15.555  19.885  1.00 27.22 ? 9   PRO A CG  1 
ATOM   64   C  CD  . PRO A  1 9   ? 7.743   14.157  20.497  1.00 26.69 ? 9   PRO A CD  1 
ATOM   65   N  N   . ASP A  1 10  ? 10.146  13.661  17.739  1.00 21.48 ? 10  ASP A N   1 
ATOM   66   C  CA  . ASP A  1 10  ? 11.397  13.760  16.977  1.00 20.45 ? 10  ASP A CA  1 
ATOM   67   C  C   . ASP A  1 10  ? 11.794  12.422  16.364  1.00 17.45 ? 10  ASP A C   1 
ATOM   68   O  O   . ASP A  1 10  ? 13.004  12.244  15.961  1.00 17.74 ? 10  ASP A O   1 
ATOM   69   C  CB  . ASP A  1 10  ? 12.550  14.305  17.836  1.00 22.58 ? 10  ASP A CB  1 
ATOM   70   C  CG  . ASP A  1 10  ? 12.333  15.774  18.260  1.00 29.22 ? 10  ASP A CG  1 
ATOM   71   O  OD1 . ASP A  1 10  ? 11.978  16.605  17.357  1.00 29.25 ? 10  ASP A OD1 1 
ATOM   72   O  OD2 . ASP A  1 10  ? 12.477  16.051  19.503  1.00 32.37 ? 10  ASP A OD2 1 
ATOM   73   N  N   . GLY A  1 11  ? 10.803  11.530  16.317  1.00 15.94 ? 11  GLY A N   1 
ATOM   74   C  CA  . GLY A  1 11  ? 10.933  10.167  15.849  1.00 14.12 ? 11  GLY A CA  1 
ATOM   75   C  C   . GLY A  1 11  ? 10.964  10.052  14.343  1.00 11.66 ? 11  GLY A C   1 
ATOM   76   O  O   . GLY A  1 11  ? 10.929  11.065  13.585  1.00 11.62 ? 11  GLY A O   1 
ATOM   77   N  N   . GLU A  1 12  ? 11.065  8.793   13.835  1.00 9.50  ? 12  GLU A N   1 
ATOM   78   C  CA  . GLU A  1 12  ? 11.442  8.595   12.466  1.00 8.89  ? 12  GLU A CA  1 
ATOM   79   C  C   . GLU A  1 12  ? 10.564  9.261   11.363  1.00 8.64  ? 12  GLU A C   1 
ATOM   80   O  O   . GLU A  1 12  ? 11.091  9.559   10.331  1.00 8.21  ? 12  GLU A O   1 
ATOM   81   C  CB  . GLU A  1 12  ? 11.601  7.046   12.173  1.00 8.65  ? 12  GLU A CB  1 
ATOM   82   C  CG  . GLU A  1 12  ? 10.262  6.301   12.131  1.00 8.41  ? 12  GLU A CG  1 
ATOM   83   C  CD  . GLU A  1 12  ? 10.597  4.803   12.302  1.00 8.49  ? 12  GLU A CD  1 
ATOM   84   O  OE1 . GLU A  1 12  ? 10.839  4.153   11.320  1.00 8.65  ? 12  GLU A OE1 1 
ATOM   85   O  OE2 . GLU A  1 12  ? 10.503  4.376   13.497  1.00 10.80 ? 12  GLU A OE2 1 
ATOM   86   N  N   . ASN A  1 13  ? 9.283   9.441   11.659  1.00 9.35  ? 13  ASN A N   1 
ATOM   87   C  CA  . ASN A  1 13  ? 8.422   10.047  10.654  1.00 9.83  ? 13  ASN A CA  1 
ATOM   88   C  C   . ASN A  1 13  ? 8.773   11.532  10.473  1.00 9.57  ? 13  ASN A C   1 
ATOM   89   O  O   . ASN A  1 13  ? 8.364   12.073  9.475   1.00 10.16 ? 13  ASN A O   1 
ATOM   90   C  CB  . ASN A  1 13  ? 6.954   9.917   10.950  1.00 10.14 ? 13  ASN A CB  1 
ATOM   91   C  CG  . ASN A  1 13  ? 6.461   8.516   10.822  1.00 10.24 ? 13  ASN A CG  1 
ATOM   92   O  OD1 . ASN A  1 13  ? 7.137   7.639   10.282  1.00 10.26 ? 13  ASN A OD1 1 
ATOM   93   N  ND2 . ASN A  1 13  ? 5.244   8.286   11.327  1.00 9.99  ? 13  ASN A ND2 1 
ATOM   94   N  N   . SER A  1 14  ? 9.480   12.118  11.467  1.00 10.05 ? 14  SER A N   1 
ATOM   95   C  CA  . SER A  1 14  ? 9.850   13.546  11.396  1.00 10.31 ? 14  SER A CA  1 
ATOM   96   C  C   . SER A  1 14  ? 11.308  13.745  11.029  1.00 10.56 ? 14  SER A C   1 
ATOM   97   O  O   . SER A  1 14  ? 11.760  14.867  10.876  1.00 10.34 ? 14  SER A O   1 
ATOM   98   C  CB  . SER A  1 14  ? 9.697   14.149  12.818  1.00 12.26 ? 14  SER A CB  1 
ATOM   99   O  OG  . SER A  1 14  ? 8.265   14.178  12.997  1.00 16.79 ? 14  SER A OG  1 
ATOM   100  N  N   . TRP A  1 15  ? 12.104  12.643  10.829  1.00 10.31 ? 15  TRP A N   1 
ATOM   101  C  CA  . TRP A  1 15  ? 13.505  12.868  10.453  1.00 9.48  ? 15  TRP A CA  1 
ATOM   102  C  C   . TRP A  1 15  ? 13.692  13.653  9.194   1.00 10.24 ? 15  TRP A C   1 
ATOM   103  O  O   . TRP A  1 15  ? 14.636  14.466  9.117   1.00 10.09 ? 15  TRP A O   1 
ATOM   104  C  CB  . TRP A  1 15  ? 14.234  11.525  10.286  1.00 10.54 ? 15  TRP A CB  1 
ATOM   105  C  CG  . TRP A  1 15  ? 14.366  10.691  11.520  1.00 9.43  ? 15  TRP A CG  1 
ATOM   106  C  CD1 . TRP A  1 15  ? 14.139  11.019  12.811  1.00 8.47  ? 15  TRP A CD1 1 
ATOM   107  C  CD2 . TRP A  1 15  ? 14.840  9.296   11.506  1.00 8.95  ? 15  TRP A CD2 1 
ATOM   108  N  NE1 . TRP A  1 15  ? 14.464  9.920   13.680  1.00 9.47  ? 15  TRP A NE1 1 
ATOM   109  C  CE2 . TRP A  1 15  ? 14.875  8.858   12.893  1.00 8.24  ? 15  TRP A CE2 1 
ATOM   110  C  CE3 . TRP A  1 15  ? 15.225  8.433   10.504  1.00 8.38  ? 15  TRP A CE3 1 
ATOM   111  C  CZ2 . TRP A  1 15  ? 15.274  7.566   13.252  1.00 8.62  ? 15  TRP A CZ2 1 
ATOM   112  C  CZ3 . TRP A  1 15  ? 15.623  7.147   10.829  1.00 8.61  ? 15  TRP A CZ3 1 
ATOM   113  C  CH2 . TRP A  1 15  ? 15.663  6.749   12.187  1.00 8.49  ? 15  TRP A CH2 1 
ATOM   114  N  N   . SER A  1 16  ? 12.790  13.536  8.249   1.00 9.53  ? 16  SER A N   1 
ATOM   115  C  CA  . SER A  1 16  ? 12.988  14.186  6.993   1.00 10.12 ? 16  SER A CA  1 
ATOM   116  C  C   . SER A  1 16  ? 12.841  15.718  7.088   1.00 10.51 ? 16  SER A C   1 
ATOM   117  O  O   . SER A  1 16  ? 13.268  16.378  6.118   1.00 10.31 ? 16  SER A O   1 
ATOM   118  C  CB  . SER A  1 16  ? 11.951  13.672  5.993   1.00 10.67 ? 16  SER A CB  1 
ATOM   119  O  OG  . SER A  1 16  ? 10.629  14.060  6.447   1.00 11.89 ? 16  SER A OG  1 
ATOM   120  N  N   . LYS A  1 17  ? 12.344  16.202  8.206   1.00 11.05 ? 17  LYS A N   1 
ATOM   121  C  CA  . LYS A  1 17  ? 12.269  17.723  8.307   1.00 11.06 ? 17  LYS A CA  1 
ATOM   122  C  C   . LYS A  1 17  ? 13.700  18.298  8.346   1.00 12.53 ? 17  LYS A C   1 
ATOM   123  O  O   . LYS A  1 17  ? 14.076  19.187  7.535   1.00 14.07 ? 17  LYS A O   1 
ATOM   124  C  CB  . LYS A  1 17  ? 11.581  18.091  9.588   1.00 11.39 ? 17  LYS A CB  1 
ATOM   125  C  CG  . LYS A  1 17  ? 10.082  17.847  9.582   1.00 16.09 ? 17  LYS A CG  1 
ATOM   126  C  CD  . LYS A  1 17  ? 9.521   17.943  11.026  1.00 18.04 ? 17  LYS A CD  1 
ATOM   127  C  CE  . LYS A  1 17  ? 8.153   17.183  11.123  1.00 20.11 ? 17  LYS A CE  1 
ATOM   128  N  NZ  . LYS A  1 17  ? 7.579   17.510  12.504  1.00 23.33 ? 17  LYS A NZ  1 
ATOM   129  N  N   . LYS A  1 18  ? 14.548  17.729  9.215   1.00 10.70 ? 18  LYS A N   1 
ATOM   130  C  CA  . LYS A  1 18  ? 15.921  18.221  9.342   1.00 12.70 ? 18  LYS A CA  1 
ATOM   131  C  C   . LYS A  1 18  ? 16.896  17.461  8.449   1.00 12.64 ? 18  LYS A C   1 
ATOM   132  O  O   . LYS A  1 18  ? 17.974  17.966  8.060   1.00 14.32 ? 18  LYS A O   1 
ATOM   133  C  CB  . LYS A  1 18  ? 16.412  18.154  10.777  1.00 16.06 ? 18  LYS A CB  1 
ATOM   134  C  CG  . LYS A  1 18  ? 15.624  19.092  11.698  1.00 24.87 ? 18  LYS A CG  1 
ATOM   135  C  CD  . LYS A  1 18  ? 16.402  19.653  12.892  1.00 32.20 ? 18  LYS A CD  1 
ATOM   136  C  CE  . LYS A  1 18  ? 16.806  21.109  12.598  1.00 38.91 ? 18  LYS A CE  1 
ATOM   137  N  NZ  . LYS A  1 18  ? 15.669  22.081  12.661  1.00 38.37 ? 18  LYS A NZ  1 
ATOM   138  N  N   . TYR A  1 19  ? 16.560  16.258  7.988   1.00 10.76 ? 19  TYR A N   1 
ATOM   139  C  CA  . TYR A  1 19  ? 17.479  15.450  7.197   1.00 10.39 ? 19  TYR A CA  1 
ATOM   140  C  C   . TYR A  1 19  ? 16.737  14.997  5.940   1.00 10.69 ? 19  TYR A C   1 
ATOM   141  O  O   . TYR A  1 19  ? 16.042  13.921  5.928   1.00 10.19 ? 19  TYR A O   1 
ATOM   142  C  CB  . TYR A  1 19  ? 17.818  14.208  8.072   1.00 12.13 ? 19  TYR A CB  1 
ATOM   143  C  CG  . TYR A  1 19  ? 18.483  14.554  9.374   1.00 10.88 ? 19  TYR A CG  1 
ATOM   144  C  CD1 . TYR A  1 19  ? 19.871  14.870  9.366   1.00 11.25 ? 19  TYR A CD1 1 
ATOM   145  C  CD2 . TYR A  1 19  ? 17.758  14.615  10.538  1.00 10.68 ? 19  TYR A CD2 1 
ATOM   146  C  CE1 . TYR A  1 19  ? 20.534  15.207  10.552  1.00 11.99 ? 19  TYR A CE1 1 
ATOM   147  C  CE2 . TYR A  1 19  ? 18.399  14.929  11.773  1.00 11.28 ? 19  TYR A CE2 1 
ATOM   148  C  CZ  . TYR A  1 19  ? 19.782  15.235  11.720  1.00 13.53 ? 19  TYR A CZ  1 
ATOM   149  O  OH  . TYR A  1 19  ? 20.465  15.521  12.924  1.00 17.25 ? 19  TYR A OH  1 
ATOM   150  N  N   . PRO A  1 20  ? 16.791  15.756  4.871   1.00 9.60  ? 20  PRO A N   1 
ATOM   151  C  CA  . PRO A  1 20  ? 15.831  15.585  3.817   1.00 10.06 ? 20  PRO A CA  1 
ATOM   152  C  C   . PRO A  1 20  ? 16.064  14.234  3.160   1.00 10.92 ? 20  PRO A C   1 
ATOM   153  O  O   . PRO A  1 20  ? 15.132  13.666  2.526   1.00 10.97 ? 20  PRO A O   1 
ATOM   154  C  CB  . PRO A  1 20  ? 16.139  16.724  2.833   1.00 12.04 ? 20  PRO A CB  1 
ATOM   155  C  CG  . PRO A  1 20  ? 16.770  17.728  3.685   1.00 12.12 ? 20  PRO A CG  1 
ATOM   156  C  CD  . PRO A  1 20  ? 17.538  17.062  4.755   1.00 10.35 ? 20  PRO A CD  1 
ATOM   157  N  N   . SER A  1 21  ? 17.252  13.638  3.177   1.00 10.01 ? 21  SER A N   1 
ATOM   158  C  CA  . SER A  1 21  ? 17.431  12.358  2.519   1.00 9.81  ? 21  SER A CA  1 
ATOM   159  C  C   . SER A  1 21  ? 16.611  11.267  3.220   1.00 8.32  ? 21  SER A C   1 
ATOM   160  O  O   . SER A  1 21  ? 16.373  10.262  2.557   1.00 8.16  ? 21  SER A O   1 
ATOM   161  C  CB  . SER A  1 21  ? 18.942  11.899  2.523   1.00 9.85  ? 21  SER A CB  1 
ATOM   162  O  OG  . SER A  1 21  ? 19.683  12.744  1.567   1.00 11.77 ? 21  SER A OG  1 
ATOM   163  N  N   . CYS A  1 22  ? 16.151  11.497  4.459   1.00 8.61  ? 22  CYS A N   1 
ATOM   164  C  CA  . CYS A  1 22  ? 15.303  10.469  5.119   1.00 9.01  ? 22  CYS A CA  1 
ATOM   165  C  C   . CYS A  1 22  ? 13.954  10.311  4.411   1.00 10.22 ? 22  CYS A C   1 
ATOM   166  O  O   . CYS A  1 22  ? 13.289  9.310   4.634   1.00 9.62  ? 22  CYS A O   1 
ATOM   167  C  CB  . CYS A  1 22  ? 15.116  10.804  6.580   1.00 8.56  ? 22  CYS A CB  1 
ATOM   168  S  SG  . CYS A  1 22  ? 16.727  10.794  7.485   1.00 9.59  ? 22  CYS A SG  1 
ATOM   169  N  N   . GLY A  1 23  ? 13.588  11.282  3.571   1.00 9.81  ? 23  GLY A N   1 
ATOM   170  C  CA  . GLY A  1 23  ? 12.405  11.175  2.701   1.00 9.33  ? 23  GLY A CA  1 
ATOM   171  C  C   . GLY A  1 23  ? 12.688  10.969  1.279   1.00 9.34  ? 23  GLY A C   1 
ATOM   172  O  O   . GLY A  1 23  ? 11.754  11.044  0.448   1.00 10.84 ? 23  GLY A O   1 
ATOM   173  N  N   . GLY A  1 24  ? 13.902  10.656  0.928   1.00 9.16  ? 24  GLY A N   1 
ATOM   174  C  CA  . GLY A  1 24  ? 14.352  10.421  -0.436  1.00 9.48  ? 24  GLY A CA  1 
ATOM   175  C  C   . GLY A  1 24  ? 14.361  9.022   -0.903  1.00 10.97 ? 24  GLY A C   1 
ATOM   176  O  O   . GLY A  1 24  ? 13.613  8.212   -0.312  1.00 12.99 ? 24  GLY A O   1 
ATOM   177  N  N   . LEU A  1 25  ? 15.111  8.757   -1.942  1.00 13.44 ? 25  LEU A N   1 
ATOM   178  C  CA  . LEU A  1 25  ? 15.224  7.460   -2.556  1.00 13.65 ? 25  LEU A CA  1 
ATOM   179  C  C   . LEU A  1 25  ? 16.156  6.527   -1.777  1.00 13.84 ? 25  LEU A C   1 
ATOM   180  O  O   . LEU A  1 25  ? 16.983  6.955   -0.961  1.00 12.73 ? 25  LEU A O   1 
ATOM   181  C  CB  . LEU A  1 25  ? 15.726  7.542   -3.997  1.00 17.19 ? 25  LEU A CB  1 
ATOM   182  C  CG  . LEU A  1 25  ? 14.877  8.495   -4.887  1.00 21.10 ? 25  LEU A CG  1 
ATOM   183  C  CD1 . LEU A  1 25  ? 15.456  8.529   -6.283  1.00 25.58 ? 25  LEU A CD1 1 
ATOM   184  C  CD2 . LEU A  1 25  ? 13.415  8.075   -4.966  1.00 23.31 ? 25  LEU A CD2 1 
ATOM   185  N  N   . LEU A  1 26  ? 16.014  5.241   -2.107  1.00 13.08 ? 26  LEU A N   1 
ATOM   186  C  CA  . LEU A  1 26  ? 16.954  4.150   -1.749  1.00 14.92 ? 26  LEU A CA  1 
ATOM   187  C  C   . LEU A  1 26  ? 16.999  3.995   -0.225  1.00 11.63 ? 26  LEU A C   1 
ATOM   188  O  O   . LEU A  1 26  ? 18.044  3.644   0.304   1.00 12.05 ? 26  LEU A O   1 
ATOM   189  C  CB  . LEU A  1 26  ? 18.419  4.348   -2.259  1.00 17.15 ? 26  LEU A CB  1 
ATOM   190  C  CG  . LEU A  1 26  ? 18.650  4.044   -3.774  1.00 24.35 ? 26  LEU A CG  1 
ATOM   191  C  CD1 . LEU A  1 26  ? 20.151  3.763   -4.064  1.00 25.17 ? 26  LEU A CD1 1 
ATOM   192  C  CD2 . LEU A  1 26  ? 17.716  3.051   -4.470  1.00 24.50 ? 26  LEU A CD2 1 
ATOM   193  N  N   . GLN A  1 27  ? 15.916  4.244   0.504   1.00 10.31 ? 27  GLN A N   1 
ATOM   194  C  CA  . GLN A  1 27  ? 15.996  4.106   1.968   1.00 7.98  ? 27  GLN A CA  1 
ATOM   195  C  C   . GLN A  1 27  ? 16.000  2.672   2.491   1.00 7.87  ? 27  GLN A C   1 
ATOM   196  O  O   . GLN A  1 27  ? 15.338  1.769   1.979   1.00 10.07 ? 27  GLN A O   1 
ATOM   197  C  CB  . GLN A  1 27  ? 14.834  4.830   2.612   1.00 9.55  ? 27  GLN A CB  1 
ATOM   198  C  CG  . GLN A  1 27  ? 14.870  6.346   2.304   1.00 8.06  ? 27  GLN A CG  1 
ATOM   199  C  CD  . GLN A  1 27  ? 16.048  6.989   3.016   1.00 6.98  ? 27  GLN A CD  1 
ATOM   200  O  OE1 . GLN A  1 27  ? 16.047  7.196   4.218   1.00 7.68  ? 27  GLN A OE1 1 
ATOM   201  N  NE2 . GLN A  1 27  ? 17.115  7.231   2.202   1.00 8.95  ? 27  GLN A NE2 1 
ATOM   202  N  N   . SER A  1 28  ? 16.754  2.511   3.565   1.00 7.78  ? 28  SER A N   1 
ATOM   203  C  CA  . SER A  1 28  ? 16.875  1.222   4.290   1.00 7.19  ? 28  SER A CA  1 
ATOM   204  C  C   . SER A  1 28  ? 16.359  1.430   5.713   1.00 7.98  ? 28  SER A C   1 
ATOM   205  O  O   . SER A  1 28  ? 16.227  2.571   6.165   1.00 8.21  ? 28  SER A O   1 
ATOM   206  C  CB  . SER A  1 28  ? 18.373  0.953   4.415   1.00 6.89  ? 28  SER A CB  1 
ATOM   207  O  OG  . SER A  1 28  ? 18.963  0.660   3.160   1.00 7.10  ? 28  SER A OG  1 
ATOM   208  N  N   . PRO A  1 29  ? 15.982  0.396   6.453   1.00 7.77  ? 29  PRO A N   1 
ATOM   209  C  CA  . PRO A  1 29  ? 16.072  -0.995  6.079   1.00 7.74  ? 29  PRO A CA  1 
ATOM   210  C  C   . PRO A  1 29  ? 14.863  -1.458  5.267   1.00 6.88  ? 29  PRO A C   1 
ATOM   211  O  O   . PRO A  1 29  ? 13.925  -0.666  5.021   1.00 8.68  ? 29  PRO A O   1 
ATOM   212  C  CB  . PRO A  1 29  ? 16.096  -1.708  7.478   1.00 7.79  ? 29  PRO A CB  1 
ATOM   213  C  CG  . PRO A  1 29  ? 15.084  -0.864  8.241   1.00 8.46  ? 29  PRO A CG  1 
ATOM   214  C  CD  . PRO A  1 29  ? 15.461  0.615   7.826   1.00 7.26  ? 29  PRO A CD  1 
ATOM   215  N  N   . ILE A  1 30  ? 14.883  -2.714  4.845   1.00 8.04  ? 30  ILE A N   1 
ATOM   216  C  CA  . ILE A  1 30  ? 13.838  -3.263  3.977   1.00 8.86  ? 30  ILE A CA  1 
ATOM   217  C  C   . ILE A  1 30  ? 13.574  -4.700  4.416   1.00 9.00  ? 30  ILE A C   1 
ATOM   218  O  O   . ILE A  1 30  ? 14.327  -5.290  5.182   1.00 9.53  ? 30  ILE A O   1 
ATOM   219  C  CB  . ILE A  1 30  ? 14.275  -3.292  2.506   1.00 9.84  ? 30  ILE A CB  1 
ATOM   220  C  CG1 . ILE A  1 30  ? 15.560  -4.177  2.311   1.00 9.48  ? 30  ILE A CG1 1 
ATOM   221  C  CG2 . ILE A  1 30  ? 14.472  -1.820  2.053   1.00 11.05 ? 30  ILE A CG2 1 
ATOM   222  C  CD1 . ILE A  1 30  ? 15.858  -4.382  0.815   1.00 12.84 ? 30  ILE A CD1 1 
ATOM   223  N  N   . ASP A  1 31  ? 12.417  -5.209  3.997   1.00 9.62  ? 31  ASP A N   1 
ATOM   224  C  CA  . ASP A  1 31  ? 12.096  -6.590  4.175   1.00 9.59  ? 31  ASP A CA  1 
ATOM   225  C  C   . ASP A  1 31  ? 12.696  -7.414  3.045   1.00 10.29 ? 31  ASP A C   1 
ATOM   226  O  O   . ASP A  1 31  ? 12.540  -7.155  1.833   1.00 12.73 ? 31  ASP A O   1 
ATOM   227  C  CB  . ASP A  1 31  ? 10.564  -6.743  4.144   1.00 10.42 ? 31  ASP A CB  1 
ATOM   228  C  CG  . ASP A  1 31  ? 10.127  -8.203  4.398   1.00 11.77 ? 31  ASP A CG  1 
ATOM   229  O  OD1 . ASP A  1 31  ? 10.678  -8.908  5.243   1.00 11.08 ? 31  ASP A OD1 1 
ATOM   230  O  OD2 . ASP A  1 31  ? 9.167   -8.632  3.711   1.00 15.20 ? 31  ASP A OD2 1 
ATOM   231  N  N   . LEU A  1 32  ? 13.432  -8.414  3.453   1.00 10.54 ? 32  LEU A N   1 
ATOM   232  C  CA  . LEU A  1 32  ? 14.066  -9.347  2.534   1.00 11.95 ? 32  LEU A CA  1 
ATOM   233  C  C   . LEU A  1 32  ? 13.159  -10.582 2.314   1.00 12.37 ? 32  LEU A C   1 
ATOM   234  O  O   . LEU A  1 32  ? 13.019  -11.401 3.203   1.00 13.61 ? 32  LEU A O   1 
ATOM   235  C  CB  . LEU A  1 32  ? 15.436  -9.786  3.155   1.00 12.08 ? 32  LEU A CB  1 
ATOM   236  C  CG  . LEU A  1 32  ? 16.344  -8.604  3.510   1.00 12.12 ? 32  LEU A CG  1 
ATOM   237  C  CD1 . LEU A  1 32  ? 17.582  -8.989  4.327   1.00 13.00 ? 32  LEU A CD1 1 
ATOM   238  C  CD2 . LEU A  1 32  ? 16.854  -7.886  2.282   1.00 15.46 ? 32  LEU A CD2 1 
ATOM   239  N  N   . HIS A  1 33  ? 12.471  -10.619 1.185   1.00 18.44 ? 33  HIS A N   1 
ATOM   240  C  CA  . HIS A  1 33  ? 11.492  -11.727 0.968   1.00 18.58 ? 33  HIS A CA  1 
ATOM   241  C  C   . HIS A  1 33  ? 11.643  -12.286 -0.370  1.00 20.06 ? 33  HIS A C   1 
ATOM   242  O  O   . HIS A  1 33  ? 12.167  -11.619 -1.246  1.00 18.60 ? 33  HIS A O   1 
ATOM   243  C  CB  . HIS A  1 33  ? 10.072  -11.267 1.263   1.00 22.11 ? 33  HIS A CB  1 
ATOM   244  C  CG  . HIS A  1 33  ? 9.610   -10.160 0.347   1.00 25.29 ? 33  HIS A CG  1 
ATOM   245  N  ND1 . HIS A  1 33  ? 9.845   -8.851  0.615   1.00 25.75 ? 33  HIS A ND1 1 
ATOM   246  C  CD2 . HIS A  1 33  ? 8.913   -10.206 -0.891  1.00 27.00 ? 33  HIS A CD2 1 
ATOM   247  C  CE1 . HIS A  1 33  ? 9.320   -8.085  -0.417  1.00 30.50 ? 33  HIS A CE1 1 
ATOM   248  N  NE2 . HIS A  1 33  ? 8.806   -8.915  -1.341  1.00 31.55 ? 33  HIS A NE2 1 
ATOM   249  N  N   . SER A  1 34  ? 11.108  -13.490 -0.565  1.00 20.71 ? 34  SER A N   1 
ATOM   250  C  CA  . SER A  1 34  ? 11.542  -14.356 -1.644  1.00 23.87 ? 34  SER A CA  1 
ATOM   251  C  C   . SER A  1 34  ? 11.255  -13.802 -2.998  1.00 24.37 ? 34  SER A C   1 
ATOM   252  O  O   . SER A  1 34  ? 12.074  -14.025 -3.875  1.00 29.15 ? 34  SER A O   1 
ATOM   253  C  CB  . SER A  1 34  ? 10.974  -15.795 -1.490  1.00 32.21 ? 34  SER A CB  1 
ATOM   254  O  OG  . SER A  1 34  ? 9.581   -15.669 -1.370  1.00 39.99 ? 34  SER A OG  1 
ATOM   255  N  N   . ASP A  1 35  ? 10.153  -13.039 -3.129  1.00 28.10 ? 35  ASP A N   1 
ATOM   256  C  CA  . ASP A  1 35  ? 9.668   -12.512 -4.409  1.00 35.34 ? 35  ASP A CA  1 
ATOM   257  C  C   . ASP A  1 35  ? 10.656  -11.560 -5.041  1.00 29.36 ? 35  ASP A C   1 
ATOM   258  O  O   . ASP A  1 35  ? 10.651  -11.324 -6.288  1.00 29.45 ? 35  ASP A O   1 
ATOM   259  C  CB  . ASP A  1 35  ? 8.355   -11.720 -4.209  1.00 39.54 ? 35  ASP A CB  1 
ATOM   260  C  CG  . ASP A  1 35  ? 7.127   -12.617 -4.115  1.00 54.18 ? 35  ASP A CG  1 
ATOM   261  O  OD1 . ASP A  1 35  ? 7.198   -13.806 -4.568  1.00 51.39 ? 35  ASP A OD1 1 
ATOM   262  O  OD2 . ASP A  1 35  ? 6.093   -12.123 -3.583  1.00 54.80 ? 35  ASP A OD2 1 
ATOM   263  N  N   . ILE A  1 36  ? 11.486  -10.952 -4.173  1.00 22.36 ? 36  ILE A N   1 
ATOM   264  C  CA  . ILE A  1 36  ? 12.425  -9.933  -4.617  1.00 21.20 ? 36  ILE A CA  1 
ATOM   265  C  C   . ILE A  1 36  ? 13.870  -10.396 -4.583  1.00 19.37 ? 36  ILE A C   1 
ATOM   266  O  O   . ILE A  1 36  ? 14.716  -9.602  -4.895  1.00 21.18 ? 36  ILE A O   1 
ATOM   267  C  CB  . ILE A  1 36  ? 12.291  -8.605  -3.892  1.00 19.26 ? 36  ILE A CB  1 
ATOM   268  C  CG1 . ILE A  1 36  ? 12.612  -8.838  -2.397  1.00 20.48 ? 36  ILE A CG1 1 
ATOM   269  C  CG2 . ILE A  1 36  ? 10.911  -7.990  -4.224  1.00 22.71 ? 36  ILE A CG2 1 
ATOM   270  C  CD1 . ILE A  1 36  ? 12.836  -7.551  -1.648  1.00 19.59 ? 36  ILE A CD1 1 
ATOM   271  N  N   . LEU A  1 37  ? 14.123  -11.623 -4.238  1.00 19.48 ? 37  LEU A N   1 
ATOM   272  C  CA  . LEU A  1 37  ? 15.537  -12.135 -4.219  1.00 17.33 ? 37  LEU A CA  1 
ATOM   273  C  C   . LEU A  1 37  ? 15.945  -12.688 -5.586  1.00 21.56 ? 37  LEU A C   1 
ATOM   274  O  O   . LEU A  1 37  ? 15.151  -13.395 -6.298  1.00 21.11 ? 37  LEU A O   1 
ATOM   275  C  CB  . LEU A  1 37  ? 15.645  -13.240 -3.170  1.00 19.35 ? 37  LEU A CB  1 
ATOM   276  C  CG  . LEU A  1 37  ? 15.144  -12.805 -1.805  1.00 19.65 ? 37  LEU A CG  1 
ATOM   277  C  CD1 . LEU A  1 37  ? 15.454  -14.009 -0.926  1.00 22.95 ? 37  LEU A CD1 1 
ATOM   278  C  CD2 . LEU A  1 37  ? 15.909  -11.593 -1.315  1.00 16.82 ? 37  LEU A CD2 1 
ATOM   279  N  N   . GLN A  1 38  ? 17.201  -12.453 -5.959  1.00 18.66 ? 38  GLN A N   1 
ATOM   280  C  CA  . GLN A  1 38  ? 17.751  -13.043 -7.226  1.00 20.00 ? 38  GLN A CA  1 
ATOM   281  C  C   . GLN A  1 38  ? 19.196  -13.418 -6.979  1.00 16.99 ? 38  GLN A C   1 
ATOM   282  O  O   . GLN A  1 38  ? 20.020  -12.553 -6.566  1.00 16.96 ? 38  GLN A O   1 
ATOM   283  C  CB  . GLN A  1 38  ? 17.653  -12.015 -8.343  1.00 22.44 ? 38  GLN A CB  1 
ATOM   284  C  CG  . GLN A  1 38  ? 18.092  -12.574 -9.694  1.00 26.78 ? 38  GLN A CG  1 
ATOM   285  C  CD  . GLN A  1 38  ? 17.769  -11.636 -10.837 1.00 32.17 ? 38  GLN A CD  1 
ATOM   286  O  OE1 . GLN A  1 38  ? 16.573  -11.467 -11.212 1.00 34.20 ? 38  GLN A OE1 1 
ATOM   287  N  NE2 . GLN A  1 38  ? 18.818  -11.019 -11.400 1.00 31.92 ? 38  GLN A NE2 1 
ATOM   288  N  N   . TYR A  1 39  ? 19.533  -14.682 -7.280  1.00 17.52 ? 39  TYR A N   1 
ATOM   289  C  CA  . TYR A  1 39  ? 20.857  -15.206 -7.201  1.00 16.30 ? 39  TYR A CA  1 
ATOM   290  C  C   . TYR A  1 39  ? 21.706  -14.443 -8.192  1.00 18.88 ? 39  TYR A C   1 
ATOM   291  O  O   . TYR A  1 39  ? 21.265  -14.194 -9.346  1.00 19.75 ? 39  TYR A O   1 
ATOM   292  C  CB  . TYR A  1 39  ? 20.797  -16.722 -7.549  1.00 19.92 ? 39  TYR A CB  1 
ATOM   293  C  CG  . TYR A  1 39  ? 22.172  -17.303 -7.625  1.00 20.61 ? 39  TYR A CG  1 
ATOM   294  C  CD1 . TYR A  1 39  ? 23.024  -17.272 -6.511  1.00 19.33 ? 39  TYR A CD1 1 
ATOM   295  C  CD2 . TYR A  1 39  ? 22.677  -17.857 -8.839  1.00 20.67 ? 39  TYR A CD2 1 
ATOM   296  C  CE1 . TYR A  1 39  ? 24.287  -17.767 -6.556  1.00 23.29 ? 39  TYR A CE1 1 
ATOM   297  C  CE2 . TYR A  1 39  ? 23.985  -18.306 -8.924  1.00 26.63 ? 39  TYR A CE2 1 
ATOM   298  C  CZ  . TYR A  1 39  ? 24.798  -18.269 -7.779  1.00 26.00 ? 39  TYR A CZ  1 
ATOM   299  O  OH  . TYR A  1 39  ? 26.093  -18.755 -7.827  1.00 28.61 ? 39  TYR A OH  1 
ATOM   300  N  N   . ASP A  1 40  ? 22.840  -13.978 -7.738  1.00 16.50 ? 40  ASP A N   1 
ATOM   301  C  CA  . ASP A  1 40  ? 23.807  -13.382 -8.596  1.00 18.67 ? 40  ASP A CA  1 
ATOM   302  C  C   . ASP A  1 40  ? 25.130  -14.076 -8.337  1.00 20.81 ? 40  ASP A C   1 
ATOM   303  O  O   . ASP A  1 40  ? 25.702  -13.946 -7.325  1.00 17.44 ? 40  ASP A O   1 
ATOM   304  C  CB  . ASP A  1 40  ? 23.902  -11.880 -8.301  1.00 21.04 ? 40  ASP A CB  1 
ATOM   305  C  CG  . ASP A  1 40  ? 24.860  -11.131 -9.266  1.00 25.42 ? 40  ASP A CG  1 
ATOM   306  O  OD1 . ASP A  1 40  ? 25.737  -11.749 -9.850  1.00 29.43 ? 40  ASP A OD1 1 
ATOM   307  O  OD2 . ASP A  1 40  ? 24.655  -9.902  -9.415  1.00 32.19 ? 40  ASP A OD2 1 
ATOM   308  N  N   . ALA A  1 41  ? 25.614  -14.887 -9.309  1.00 25.12 ? 41  ALA A N   1 
ATOM   309  C  CA  . ALA A  1 41  ? 26.977  -15.514 -9.226  1.00 27.25 ? 41  ALA A CA  1 
ATOM   310  C  C   . ALA A  1 41  ? 28.127  -14.531 -9.088  1.00 22.53 ? 41  ALA A C   1 
ATOM   311  O  O   . ALA A  1 41  ? 29.220  -14.910 -8.648  1.00 26.35 ? 41  ALA A O   1 
ATOM   312  C  CB  . ALA A  1 41  ? 27.242  -16.415 -10.452 1.00 26.85 ? 41  ALA A CB  1 
ATOM   313  N  N   . SER A  1 42  ? 27.914  -13.260 -9.393  1.00 25.15 ? 42  SER A N   1 
ATOM   314  C  CA  . SER A  1 42  ? 28.961  -12.240 -9.205  1.00 27.06 ? 42  SER A CA  1 
ATOM   315  C  C   . SER A  1 42  ? 29.302  -11.995 -7.722  1.00 28.85 ? 42  SER A C   1 
ATOM   316  O  O   . SER A  1 42  ? 30.289  -11.329 -7.361  1.00 28.87 ? 42  SER A O   1 
ATOM   317  C  CB  . SER A  1 42  ? 28.500  -10.937 -9.911  1.00 29.70 ? 42  SER A CB  1 
ATOM   318  O  OG  . SER A  1 42  ? 28.170  -9.838  -9.031  1.00 37.80 ? 42  SER A OG  1 
ATOM   319  N  N   . LEU A  1 43  ? 28.439  -12.512 -6.855  1.00 21.03 ? 43  LEU A N   1 
ATOM   320  C  CA  . LEU A  1 43  ? 28.602  -12.234 -5.422  1.00 19.78 ? 43  LEU A CA  1 
ATOM   321  C  C   . LEU A  1 43  ? 29.503  -13.225 -4.720  1.00 19.34 ? 43  LEU A C   1 
ATOM   322  O  O   . LEU A  1 43  ? 29.083  -14.141 -4.000  1.00 21.91 ? 43  LEU A O   1 
ATOM   323  C  CB  . LEU A  1 43  ? 27.206  -12.135 -4.781  1.00 15.82 ? 43  LEU A CB  1 
ATOM   324  C  CG  . LEU A  1 43  ? 26.345  -11.016 -5.308  1.00 17.50 ? 43  LEU A CG  1 
ATOM   325  C  CD1 . LEU A  1 43  ? 24.945  -10.894 -4.643  1.00 14.50 ? 43  LEU A CD1 1 
ATOM   326  C  CD2 . LEU A  1 43  ? 27.022  -9.668  -5.245  1.00 15.92 ? 43  LEU A CD2 1 
ATOM   327  N  N   . THR A  1 44  ? 30.804  -13.010 -4.878  1.00 19.54 ? 44  THR A N   1 
ATOM   328  C  CA  . THR A  1 44  ? 31.840  -13.831 -4.297  1.00 20.40 ? 44  THR A CA  1 
ATOM   329  C  C   . THR A  1 44  ? 32.073  -13.531 -2.788  1.00 19.39 ? 44  THR A C   1 
ATOM   330  O  O   . THR A  1 44  ? 31.532  -12.529 -2.249  1.00 16.36 ? 44  THR A O   1 
ATOM   331  C  CB  . THR A  1 44  ? 33.139  -13.580 -5.141  1.00 22.78 ? 44  THR A CB  1 
ATOM   332  O  OG1 . THR A  1 44  ? 33.483  -12.214 -4.995  1.00 25.77 ? 44  THR A OG1 1 
ATOM   333  C  CG2 . THR A  1 44  ? 32.838  -13.920 -6.629  1.00 31.23 ? 44  THR A CG2 1 
ATOM   334  N  N   . PRO A  1 45  ? 32.748  -14.401 -2.043  1.00 17.83 ? 45  PRO A N   1 
ATOM   335  C  CA  . PRO A  1 45  ? 32.983  -14.155 -0.611  1.00 18.64 ? 45  PRO A CA  1 
ATOM   336  C  C   . PRO A  1 45  ? 33.820  -12.940 -0.274  1.00 17.48 ? 45  PRO A C   1 
ATOM   337  O  O   . PRO A  1 45  ? 34.847  -12.660 -0.944  1.00 21.41 ? 45  PRO A O   1 
ATOM   338  C  CB  . PRO A  1 45  ? 33.687  -15.407 -0.133  1.00 20.47 ? 45  PRO A CB  1 
ATOM   339  C  CG  . PRO A  1 45  ? 33.372  -16.446 -1.174  1.00 20.87 ? 45  PRO A CG  1 
ATOM   340  C  CD  . PRO A  1 45  ? 33.290  -15.713 -2.476  1.00 20.55 ? 45  PRO A CD  1 
ATOM   341  N  N   . LEU A  1 46  ? 33.442  -12.178 0.729   1.00 15.78 ? 46  LEU A N   1 
ATOM   342  C  CA  . LEU A  1 46  ? 34.260  -11.022 1.159   1.00 14.42 ? 46  LEU A CA  1 
ATOM   343  C  C   . LEU A  1 46  ? 35.381  -11.601 2.021   1.00 16.07 ? 46  LEU A C   1 
ATOM   344  O  O   . LEU A  1 46  ? 35.224  -12.663 2.627   1.00 17.63 ? 46  LEU A O   1 
ATOM   345  C  CB  . LEU A  1 46  ? 33.488  -10.050 2.003   1.00 13.99 ? 46  LEU A CB  1 
ATOM   346  C  CG  . LEU A  1 46  ? 32.369  -9.400  1.195   1.00 15.02 ? 46  LEU A CG  1 
ATOM   347  C  CD1 . LEU A  1 46  ? 31.556  -8.564  2.191   1.00 15.18 ? 46  LEU A CD1 1 
ATOM   348  C  CD2 . LEU A  1 46  ? 32.908  -8.569  0.032   1.00 18.74 ? 46  LEU A CD2 1 
ATOM   349  N  N   . GLU A  1 47  ? 36.479  -10.864 2.101   1.00 14.52 ? 47  GLU A N   1 
ATOM   350  C  CA  . GLU A  1 47  ? 37.521  -11.188 3.038   1.00 16.59 ? 47  GLU A CA  1 
ATOM   351  C  C   . GLU A  1 47  ? 37.630  -10.075 4.086   1.00 14.96 ? 47  GLU A C   1 
ATOM   352  O  O   . GLU A  1 47  ? 37.591  -8.877  3.787   1.00 16.98 ? 47  GLU A O   1 
ATOM   353  C  CB  . GLU A  1 47  ? 38.879  -11.323 2.327   1.00 21.08 ? 47  GLU A CB  1 
ATOM   354  C  CG  . GLU A  1 47  ? 38.960  -12.457 1.326   1.00 29.42 ? 47  GLU A CG  1 
ATOM   355  C  CD  . GLU A  1 47  ? 40.372  -12.613 0.747   1.00 40.34 ? 47  GLU A CD  1 
ATOM   356  O  OE1 . GLU A  1 47  ? 40.579  -12.251 -0.439  1.00 47.80 ? 47  GLU A OE1 1 
ATOM   357  O  OE2 . GLU A  1 47  ? 41.277  -13.054 1.482   1.00 45.57 ? 47  GLU A OE2 1 
ATOM   358  N  N   . PHE A  1 48  ? 37.762  -10.459 5.342   1.00 15.09 ? 48  PHE A N   1 
ATOM   359  C  CA  . PHE A  1 48  ? 37.813  -9.558  6.455   1.00 14.26 ? 48  PHE A CA  1 
ATOM   360  C  C   . PHE A  1 48  ? 39.202  -9.380  6.972   1.00 16.94 ? 48  PHE A C   1 
ATOM   361  O  O   . PHE A  1 48  ? 39.764  -10.331 7.530   1.00 20.34 ? 48  PHE A O   1 
ATOM   362  C  CB  . PHE A  1 48  ? 36.834  -10.048 7.554   1.00 15.83 ? 48  PHE A CB  1 
ATOM   363  C  CG  . PHE A  1 48  ? 35.490  -10.420 6.996   1.00 14.57 ? 48  PHE A CG  1 
ATOM   364  C  CD1 . PHE A  1 48  ? 34.646  -9.440  6.531   1.00 14.56 ? 48  PHE A CD1 1 
ATOM   365  C  CD2 . PHE A  1 48  ? 35.105  -11.799 6.822   1.00 15.38 ? 48  PHE A CD2 1 
ATOM   366  C  CE1 . PHE A  1 48  ? 33.446  -9.800  5.865   1.00 15.43 ? 48  PHE A CE1 1 
ATOM   367  C  CE2 . PHE A  1 48  ? 33.895  -12.109 6.228   1.00 14.02 ? 48  PHE A CE2 1 
ATOM   368  C  CZ  . PHE A  1 48  ? 33.044  -11.078 5.730   1.00 14.76 ? 48  PHE A CZ  1 
ATOM   369  N  N   . GLN A  1 49  ? 39.788  -8.247  6.644   1.00 13.26 ? 49  GLN A N   1 
ATOM   370  C  CA  . GLN A  1 49  ? 41.275  -8.099  6.824   1.00 14.85 ? 49  GLN A CA  1 
ATOM   371  C  C   . GLN A  1 49  ? 41.545  -7.138  7.920   1.00 12.40 ? 49  GLN A C   1 
ATOM   372  O  O   . GLN A  1 49  ? 40.862  -6.112  8.100   1.00 13.17 ? 49  GLN A O   1 
ATOM   373  C  CB  . GLN A  1 49  ? 41.900  -7.532  5.554   1.00 15.96 ? 49  GLN A CB  1 
ATOM   374  C  CG  . GLN A  1 49  ? 41.726  -8.520  4.431   1.00 22.71 ? 49  GLN A CG  1 
ATOM   375  C  CD  . GLN A  1 49  ? 42.752  -8.454  3.302   1.00 33.25 ? 49  GLN A CD  1 
ATOM   376  O  OE1 . GLN A  1 49  ? 43.086  -9.517  2.689   1.00 34.47 ? 49  GLN A OE1 1 
ATOM   377  N  NE2 . GLN A  1 49  ? 43.215  -7.222  2.959   1.00 32.25 ? 49  GLN A NE2 1 
ATOM   378  N  N   . GLY A  1 50  ? 42.484  -7.491  8.829   1.00 12.66 ? 50  GLY A N   1 
ATOM   379  C  CA  . GLY A  1 50  ? 42.703  -6.668  9.945   1.00 13.21 ? 50  GLY A CA  1 
ATOM   380  C  C   . GLY A  1 50  ? 41.588  -6.589  11.040  1.00 11.97 ? 50  GLY A C   1 
ATOM   381  O  O   . GLY A  1 50  ? 41.609  -5.726  11.877  1.00 14.87 ? 50  GLY A O   1 
ATOM   382  N  N   . TYR A  1 51  ? 40.708  -7.601  10.978  1.00 13.48 ? 51  TYR A N   1 
ATOM   383  C  CA  . TYR A  1 51  ? 39.630  -7.743  12.029  1.00 13.79 ? 51  TYR A CA  1 
ATOM   384  C  C   . TYR A  1 51  ? 40.177  -8.297  13.348  1.00 14.52 ? 51  TYR A C   1 
ATOM   385  O  O   . TYR A  1 51  ? 39.541  -8.142  14.391  1.00 15.35 ? 51  TYR A O   1 
ATOM   386  C  CB  . TYR A  1 51  ? 38.524  -8.660  11.512  1.00 13.18 ? 51  TYR A CB  1 
ATOM   387  C  CG  . TYR A  1 51  ? 37.483  -7.965  10.662  1.00 12.06 ? 51  TYR A CG  1 
ATOM   388  C  CD1 . TYR A  1 51  ? 37.849  -7.086  9.646   1.00 12.47 ? 51  TYR A CD1 1 
ATOM   389  C  CD2 . TYR A  1 51  ? 36.132  -8.191  10.875  1.00 11.54 ? 51  TYR A CD2 1 
ATOM   390  C  CE1 . TYR A  1 51  ? 36.892  -6.451  8.871   1.00 13.37 ? 51  TYR A CE1 1 
ATOM   391  C  CE2 . TYR A  1 51  ? 35.171  -7.563  10.108  1.00 12.71 ? 51  TYR A CE2 1 
ATOM   392  C  CZ  . TYR A  1 51  ? 35.554  -6.696  9.107   1.00 13.47 ? 51  TYR A CZ  1 
ATOM   393  O  OH  . TYR A  1 51  ? 34.590  -6.075  8.345   1.00 12.84 ? 51  TYR A OH  1 
ATOM   394  N  N   . ASN A  1 52  ? 41.358  -8.940  13.309  1.00 15.60 ? 52  ASN A N   1 
ATOM   395  C  CA  . ASN A  1 52  ? 41.913  -9.453  14.590  1.00 15.92 ? 52  ASN A CA  1 
ATOM   396  C  C   . ASN A  1 52  ? 42.625  -8.373  15.371  1.00 18.47 ? 52  ASN A C   1 
ATOM   397  O  O   . ASN A  1 52  ? 43.847  -8.170  15.249  1.00 21.47 ? 52  ASN A O   1 
ATOM   398  C  CB  . ASN A  1 52  ? 42.801  -10.693 14.328  1.00 17.53 ? 52  ASN A CB  1 
ATOM   399  C  CG  . ASN A  1 52  ? 42.951  -11.619 15.571  1.00 20.83 ? 52  ASN A CG  1 
ATOM   400  O  OD1 . ASN A  1 52  ? 42.523  -11.319 16.686  1.00 21.11 ? 52  ASN A OD1 1 
ATOM   401  N  ND2 . ASN A  1 52  ? 43.689  -12.733 15.371  1.00 30.44 ? 52  ASN A ND2 1 
ATOM   402  N  N   . LEU A  1 53  ? 41.877  -7.561  16.070  1.00 19.13 ? 53  LEU A N   1 
ATOM   403  C  CA  . LEU A  1 53  ? 42.418  -6.363  16.707  1.00 19.93 ? 53  LEU A CA  1 
ATOM   404  C  C   . LEU A  1 53  ? 43.394  -6.722  17.812  1.00 22.31 ? 53  LEU A C   1 
ATOM   405  O  O   . LEU A  1 53  ? 43.145  -7.626  18.621  1.00 23.18 ? 53  LEU A O   1 
ATOM   406  C  CB  . LEU A  1 53  ? 41.355  -5.408  17.251  1.00 16.97 ? 53  LEU A CB  1 
ATOM   407  C  CG  . LEU A  1 53  ? 40.247  -5.047  16.257  1.00 16.56 ? 53  LEU A CG  1 
ATOM   408  C  CD1 . LEU A  1 53  ? 39.241  -4.199  16.999  1.00 15.83 ? 53  LEU A CD1 1 
ATOM   409  C  CD2 . LEU A  1 53  ? 40.859  -4.329  15.032  1.00 19.27 ? 53  LEU A CD2 1 
ATOM   410  N  N   . SER A  1 54  ? 44.520  -6.029  17.726  1.00 22.58 ? 54  SER A N   1 
ATOM   411  C  CA  . SER A  1 54  ? 45.570  -6.181  18.725  1.00 24.58 ? 54  SER A CA  1 
ATOM   412  C  C   . SER A  1 54  ? 44.966  -6.205  20.122  1.00 24.25 ? 54  SER A C   1 
ATOM   413  O  O   . SER A  1 54  ? 44.348  -5.213  20.538  1.00 24.40 ? 54  SER A O   1 
ATOM   414  C  CB  . SER A  1 54  ? 46.509  -4.973  18.598  1.00 22.62 ? 54  SER A CB  1 
ATOM   415  O  OG  . SER A  1 54  ? 47.618  -5.214  19.482  1.00 28.73 ? 54  SER A OG  1 
ATOM   416  N  N   . ALA A  1 55  ? 45.159  -7.280  20.879  1.00 24.90 ? 55  ALA A N   1 
ATOM   417  C  CA  . ALA A  1 55  ? 44.755  -7.182  22.290  1.00 27.60 ? 55  ALA A CA  1 
ATOM   418  C  C   . ALA A  1 55  ? 45.623  -6.190  23.103  1.00 28.33 ? 55  ALA A C   1 
ATOM   419  O  O   . ALA A  1 55  ? 45.341  -5.913  24.233  1.00 29.72 ? 55  ALA A O   1 
ATOM   420  C  CB  . ALA A  1 55  ? 44.714  -8.548  22.973  1.00 33.74 ? 55  ALA A CB  1 
ATOM   421  N  N   . ASN A  1 56  ? 46.658  -5.619  22.487  1.00 29.57 ? 56  ASN A N   1 
ATOM   422  C  CA  . ASN A  1 56  ? 47.437  -4.539  23.161  1.00 28.90 ? 56  ASN A CA  1 
ATOM   423  C  C   . ASN A  1 56  ? 46.987  -3.144  22.796  1.00 30.95 ? 56  ASN A C   1 
ATOM   424  O  O   . ASN A  1 56  ? 47.592  -2.183  23.215  1.00 32.08 ? 56  ASN A O   1 
ATOM   425  C  CB  . ASN A  1 56  ? 48.931  -4.666  22.803  1.00 29.98 ? 56  ASN A CB  1 
ATOM   426  C  CG  . ASN A  1 56  ? 49.514  -5.982  23.264  1.00 33.74 ? 56  ASN A CG  1 
ATOM   427  O  OD1 . ASN A  1 56  ? 49.353  -6.379  24.441  1.00 33.30 ? 56  ASN A OD1 1 
ATOM   428  N  ND2 . ASN A  1 56  ? 50.143  -6.700  22.336  1.00 31.01 ? 56  ASN A ND2 1 
ATOM   429  N  N   . LYS A  1 57  ? 45.962  -3.022  21.937  1.00 25.48 ? 57  LYS A N   1 
ATOM   430  C  CA  . LYS A  1 57  ? 45.334  -1.734  21.661  1.00 22.79 ? 57  LYS A CA  1 
ATOM   431  C  C   . LYS A  1 57  ? 43.977  -1.670  22.381  1.00 20.96 ? 57  LYS A C   1 
ATOM   432  O  O   . LYS A  1 57  ? 43.383  -2.703  22.664  1.00 22.65 ? 57  LYS A O   1 
ATOM   433  C  CB  . LYS A  1 57  ? 45.112  -1.495  20.138  1.00 26.07 ? 57  LYS A CB  1 
ATOM   434  C  CG  . LYS A  1 57  ? 46.347  -1.096  19.323  1.00 33.19 ? 57  LYS A CG  1 
ATOM   435  C  CD  . LYS A  1 57  ? 45.953  -0.861  17.862  1.00 37.09 ? 57  LYS A CD  1 
ATOM   436  C  CE  . LYS A  1 57  ? 45.181  0.462   17.668  1.00 39.34 ? 57  LYS A CE  1 
ATOM   437  N  NZ  . LYS A  1 57  ? 45.181  1.033   16.276  1.00 41.92 ? 57  LYS A NZ  1 
ATOM   438  N  N   . GLN A  1 58  ? 43.530  -0.467  22.683  1.00 21.47 ? 58  GLN A N   1 
ATOM   439  C  CA  . GLN A  1 58  ? 42.143  -0.267  23.198  1.00 21.97 ? 58  GLN A CA  1 
ATOM   440  C  C   . GLN A  1 58  ? 41.273  0.512   22.293  1.00 20.77 ? 58  GLN A C   1 
ATOM   441  O  O   . GLN A  1 58  ? 41.728  1.428   21.606  1.00 22.03 ? 58  GLN A O   1 
ATOM   442  C  CB  . GLN A  1 58  ? 42.157  0.395   24.563  1.00 21.41 ? 58  GLN A CB  1 
ATOM   443  C  CG  . GLN A  1 58  ? 42.599  -0.660  25.531  1.00 23.29 ? 58  GLN A CG  1 
ATOM   444  C  CD  . GLN A  1 58  ? 42.975  -0.072  26.844  1.00 24.68 ? 58  GLN A CD  1 
ATOM   445  O  OE1 . GLN A  1 58  ? 43.524  -0.763  27.684  1.00 25.41 ? 58  GLN A OE1 1 
ATOM   446  N  NE2 . GLN A  1 58  ? 42.797  1.209   26.972  1.00 24.02 ? 58  GLN A NE2 1 
ATOM   447  N  N   . PHE A  1 59  ? 39.970  0.154   22.281  1.00 20.79 ? 59  PHE A N   1 
ATOM   448  C  CA  . PHE A  1 59  ? 39.002  0.789   21.346  1.00 18.49 ? 59  PHE A CA  1 
ATOM   449  C  C   . PHE A  1 59  ? 37.871  1.450   22.090  1.00 15.84 ? 59  PHE A C   1 
ATOM   450  O  O   . PHE A  1 59  ? 37.386  0.854   23.032  1.00 17.00 ? 59  PHE A O   1 
ATOM   451  C  CB  . PHE A  1 59  ? 38.529  -0.278  20.374  1.00 18.41 ? 59  PHE A CB  1 
ATOM   452  C  CG  . PHE A  1 59  ? 39.669  -0.858  19.616  1.00 18.63 ? 59  PHE A CG  1 
ATOM   453  C  CD1 . PHE A  1 59  ? 40.072  -0.230  18.477  1.00 18.61 ? 59  PHE A CD1 1 
ATOM   454  C  CD2 . PHE A  1 59  ? 40.474  -1.881  20.130  1.00 19.12 ? 59  PHE A CD2 1 
ATOM   455  C  CE1 . PHE A  1 59  ? 41.184  -0.657  17.775  1.00 19.49 ? 59  PHE A CE1 1 
ATOM   456  C  CE2 . PHE A  1 59  ? 41.629  -2.316  19.414  1.00 17.05 ? 59  PHE A CE2 1 
ATOM   457  C  CZ  . PHE A  1 59  ? 41.946  -1.697  18.220  1.00 19.44 ? 59  PHE A CZ  1 
ATOM   458  N  N   . LEU A  1 60  ? 37.563  2.693   21.733  1.00 16.80 ? 60  LEU A N   1 
ATOM   459  C  CA  . LEU A  1 60  ? 36.587  3.496   22.472  1.00 16.08 ? 60  LEU A CA  1 
ATOM   460  C  C   . LEU A  1 60  ? 35.119  2.996   22.235  1.00 18.42 ? 60  LEU A C   1 
ATOM   461  O  O   . LEU A  1 60  ? 34.622  3.033   21.111  1.00 16.45 ? 60  LEU A O   1 
ATOM   462  C  CB  . LEU A  1 60  ? 36.682  4.962   22.170  1.00 17.24 ? 60  LEU A CB  1 
ATOM   463  C  CG  . LEU A  1 60  ? 35.907  5.875   23.058  1.00 22.63 ? 60  LEU A CG  1 
ATOM   464  C  CD1 . LEU A  1 60  ? 36.476  5.833   24.500  1.00 24.16 ? 60  LEU A CD1 1 
ATOM   465  C  CD2 . LEU A  1 60  ? 35.913  7.222   22.381  1.00 20.12 ? 60  LEU A CD2 1 
ATOM   466  N  N   . LEU A  1 61  ? 34.459  2.599   23.304  1.00 16.87 ? 61  LEU A N   1 
ATOM   467  C  CA  . LEU A  1 61  ? 33.019  2.309   23.339  1.00 16.80 ? 61  LEU A CA  1 
ATOM   468  C  C   . LEU A  1 61  ? 32.300  3.545   23.834  1.00 15.97 ? 61  LEU A C   1 
ATOM   469  O  O   . LEU A  1 61  ? 32.680  4.148   24.862  1.00 17.26 ? 61  LEU A O   1 
ATOM   470  C  CB  . LEU A  1 61  ? 32.763  1.150   24.251  1.00 17.51 ? 61  LEU A CB  1 
ATOM   471  C  CG  . LEU A  1 61  ? 31.357  0.471   24.147  1.00 17.76 ? 61  LEU A CG  1 
ATOM   472  C  CD1 . LEU A  1 61  ? 31.226  -0.376  22.886  1.00 17.78 ? 61  LEU A CD1 1 
ATOM   473  C  CD2 . LEU A  1 61  ? 31.083  -0.435  25.357  1.00 19.32 ? 61  LEU A CD2 1 
ATOM   474  N  N   A THR A  1 62  ? 31.259  3.993   23.122  0.50 15.04 ? 62  THR A N   1 
ATOM   475  N  N   B THR A  1 62  ? 31.244  3.987   23.131  0.50 15.09 ? 62  THR A N   1 
ATOM   476  C  CA  A THR A  1 62  ? 30.523  5.169   23.527  0.50 15.08 ? 62  THR A CA  1 
ATOM   477  C  CA  B THR A  1 62  ? 30.536  5.205   23.500  0.50 15.06 ? 62  THR A CA  1 
ATOM   478  C  C   A THR A  1 62  ? 29.025  4.866   23.568  0.50 15.82 ? 62  THR A C   1 
ATOM   479  C  C   B THR A  1 62  ? 29.032  5.106   23.391  0.50 16.01 ? 62  THR A C   1 
ATOM   480  O  O   A THR A  1 62  ? 28.524  3.973   22.819  0.50 13.93 ? 62  THR A O   1 
ATOM   481  O  O   B THR A  1 62  ? 28.528  4.538   22.401  0.50 13.80 ? 62  THR A O   1 
ATOM   482  C  CB  A THR A  1 62  ? 30.734  6.405   22.597  0.50 17.06 ? 62  THR A CB  1 
ATOM   483  C  CB  B THR A  1 62  ? 30.922  6.431   22.656  0.50 17.02 ? 62  THR A CB  1 
ATOM   484  O  OG1 A THR A  1 62  ? 32.126  6.715   22.412  0.50 18.94 ? 62  THR A OG1 1 
ATOM   485  O  OG1 B THR A  1 62  ? 30.596  6.223   21.259  0.50 15.78 ? 62  THR A OG1 1 
ATOM   486  C  CG2 A THR A  1 62  ? 29.987  7.667   23.098  0.50 16.66 ? 62  THR A CG2 1 
ATOM   487  C  CG2 B THR A  1 62  ? 32.369  6.738   22.804  0.50 19.46 ? 62  THR A CG2 1 
ATOM   488  N  N   . ASN A  1 63  ? 28.319  5.660   24.363  1.00 14.92 ? 63  ASN A N   1 
ATOM   489  C  CA  . ASN A  1 63  ? 26.861  5.722   24.253  1.00 14.99 ? 63  ASN A CA  1 
ATOM   490  C  C   . ASN A  1 63  ? 26.616  7.103   23.675  1.00 15.33 ? 63  ASN A C   1 
ATOM   491  O  O   . ASN A  1 63  ? 26.898  8.179   24.266  1.00 15.53 ? 63  ASN A O   1 
ATOM   492  C  CB  . ASN A  1 63  ? 26.236  5.548   25.628  1.00 16.11 ? 63  ASN A CB  1 
ATOM   493  C  CG  . ASN A  1 63  ? 24.749  5.872   25.660  1.00 15.65 ? 63  ASN A CG  1 
ATOM   494  O  OD1 . ASN A  1 63  ? 24.199  6.610   24.804  1.00 13.31 ? 63  ASN A OD1 1 
ATOM   495  N  ND2 . ASN A  1 63  ? 24.091  5.358   26.705  1.00 14.55 ? 63  ASN A ND2 1 
ATOM   496  N  N   . ASN A  1 64  ? 26.160  7.160   22.433  1.00 14.82 ? 64  ASN A N   1 
ATOM   497  C  CA  . ASN A  1 64  ? 25.905  8.446   21.766  1.00 15.88 ? 64  ASN A CA  1 
ATOM   498  C  C   . ASN A  1 64  ? 24.457  8.939   21.797  1.00 16.74 ? 64  ASN A C   1 
ATOM   499  O  O   . ASN A  1 64  ? 24.090  9.938   21.127  1.00 18.70 ? 64  ASN A O   1 
ATOM   500  C  CB  . ASN A  1 64  ? 26.416  8.375   20.296  1.00 16.79 ? 64  ASN A CB  1 
ATOM   501  C  CG  . ASN A  1 64  ? 25.519  7.536   19.420  1.00 18.82 ? 64  ASN A CG  1 
ATOM   502  O  OD1 . ASN A  1 64  ? 24.583  6.889   19.874  1.00 16.89 ? 64  ASN A OD1 1 
ATOM   503  N  ND2 . ASN A  1 64  ? 25.798  7.558   18.122  1.00 25.62 ? 64  ASN A ND2 1 
ATOM   504  N  N   . GLY A  1 65  ? 23.684  8.340   22.660  1.00 14.33 ? 65  GLY A N   1 
ATOM   505  C  CA  . GLY A  1 65  ? 22.270  8.638   22.842  1.00 16.80 ? 65  GLY A CA  1 
ATOM   506  C  C   . GLY A  1 65  ? 21.357  7.953   21.825  1.00 16.50 ? 65  GLY A C   1 
ATOM   507  O  O   . GLY A  1 65  ? 20.158  8.036   21.975  1.00 17.52 ? 65  GLY A O   1 
ATOM   508  N  N   . HIS A  1 66  ? 21.915  7.248   20.832  1.00 14.59 ? 66  HIS A N   1 
ATOM   509  C  CA  . HIS A  1 66  ? 21.153  6.519   19.807  1.00 13.83 ? 66  HIS A CA  1 
ATOM   510  C  C   . HIS A  1 66  ? 21.460  5.054   19.788  1.00 11.92 ? 66  HIS A C   1 
ATOM   511  O  O   . HIS A  1 66  ? 20.567  4.287   19.431  1.00 12.46 ? 66  HIS A O   1 
ATOM   512  C  CB  . HIS A  1 66  ? 21.427  7.095   18.429  1.00 13.58 ? 66  HIS A CB  1 
ATOM   513  C  CG  . HIS A  1 66  ? 21.234  8.587   18.330  1.00 13.79 ? 66  HIS A CG  1 
ATOM   514  N  ND1 . HIS A  1 66  ? 20.007  9.176   18.428  1.00 15.66 ? 66  HIS A ND1 1 
ATOM   515  C  CD2 . HIS A  1 66  ? 22.158  9.590   18.074  1.00 14.57 ? 66  HIS A CD2 1 
ATOM   516  C  CE1 . HIS A  1 66  ? 20.175  10.516  18.324  1.00 15.34 ? 66  HIS A CE1 1 
ATOM   517  N  NE2 . HIS A  1 66  ? 21.488  10.749  18.030  1.00 16.42 ? 66  HIS A NE2 1 
ATOM   518  N  N   . SER A  1 67  ? 22.689  4.637   20.117  1.00 11.97 ? 67  SER A N   1 
ATOM   519  C  CA  . SER A  1 67  ? 23.083  3.248   20.133  1.00 12.55 ? 67  SER A CA  1 
ATOM   520  C  C   . SER A  1 67  ? 24.335  3.211   21.022  1.00 11.97 ? 67  SER A C   1 
ATOM   521  O  O   . SER A  1 67  ? 24.723  4.235   21.588  1.00 12.35 ? 67  SER A O   1 
ATOM   522  C  CB  . SER A  1 67  ? 23.442  2.780   18.708  1.00 10.11 ? 67  SER A CB  1 
ATOM   523  O  OG  . SER A  1 67  ? 23.770  1.373   18.674  1.00 13.10 ? 67  SER A OG  1 
ATOM   524  N  N   . VAL A  1 68  ? 24.898  2.012   21.097  1.00 11.20 ? 68  VAL A N   1 
ATOM   525  C  CA  . VAL A  1 68  ? 26.224  1.847   21.709  1.00 12.50 ? 68  VAL A CA  1 
ATOM   526  C  C   . VAL A  1 68  ? 27.150  1.593   20.514  1.00 13.03 ? 68  VAL A C   1 
ATOM   527  O  O   . VAL A  1 68  ? 26.883  0.759   19.679  1.00 13.02 ? 68  VAL A O   1 
ATOM   528  C  CB  . VAL A  1 68  ? 26.217  0.759   22.802  1.00 15.26 ? 68  VAL A CB  1 
ATOM   529  C  CG1 . VAL A  1 68  ? 25.723  -0.578  22.307  1.00 16.18 ? 68  VAL A CG1 1 
ATOM   530  C  CG2 . VAL A  1 68  ? 27.672  0.604   23.257  1.00 18.79 ? 68  VAL A CG2 1 
ATOM   531  N  N   . LYS A  1 69  ? 28.230  2.340   20.472  1.00 12.78 ? 69  LYS A N   1 
ATOM   532  C  CA  . LYS A  1 69  ? 29.146  2.326   19.330  1.00 13.57 ? 69  LYS A CA  1 
ATOM   533  C  C   . LYS A  1 69  ? 30.563  1.975   19.773  1.00 13.20 ? 69  LYS A C   1 
ATOM   534  O  O   . LYS A  1 69  ? 31.008  2.554   20.766  1.00 15.60 ? 69  LYS A O   1 
ATOM   535  C  CB  . LYS A  1 69  ? 29.062  3.567   18.499  1.00 17.04 ? 69  LYS A CB  1 
ATOM   536  C  CG  . LYS A  1 69  ? 29.664  4.818   18.905  1.00 25.32 ? 69  LYS A CG  1 
ATOM   537  C  CD  . LYS A  1 69  ? 29.801  5.764   17.696  1.00 27.80 ? 69  LYS A CD  1 
ATOM   538  C  CE  . LYS A  1 69  ? 30.264  7.112   18.246  1.00 34.01 ? 69  LYS A CE  1 
ATOM   539  N  NZ  . LYS A  1 69  ? 30.498  8.079   17.145  1.00 38.70 ? 69  LYS A NZ  1 
ATOM   540  N  N   . LEU A  1 70  ? 31.202  1.087   19.015  1.00 11.92 ? 70  LEU A N   1 
ATOM   541  C  CA  . LEU A  1 70  ? 32.650  0.802   19.232  1.00 13.18 ? 70  LEU A CA  1 
ATOM   542  C  C   . LEU A  1 70  ? 33.401  1.374   18.090  1.00 11.83 ? 70  LEU A C   1 
ATOM   543  O  O   . LEU A  1 70  ? 33.171  1.011   16.928  1.00 13.19 ? 70  LEU A O   1 
ATOM   544  C  CB  . LEU A  1 70  ? 32.844  -0.671  19.402  1.00 12.19 ? 70  LEU A CB  1 
ATOM   545  C  CG  . LEU A  1 70  ? 34.352  -1.145  19.574  1.00 11.92 ? 70  LEU A CG  1 
ATOM   546  C  CD1 . LEU A  1 70  ? 34.916  -0.683  20.917  1.00 14.54 ? 70  LEU A CD1 1 
ATOM   547  C  CD2 . LEU A  1 70  ? 34.332  -2.661  19.389  1.00 13.62 ? 70  LEU A CD2 1 
ATOM   548  N  N   . ASN A  1 71  ? 34.429  2.222   18.387  1.00 12.61 ? 71  ASN A N   1 
ATOM   549  C  CA  . ASN A  1 71  ? 35.267  2.780   17.331  1.00 14.88 ? 71  ASN A CA  1 
ATOM   550  C  C   . ASN A  1 71  ? 36.218  1.749   16.833  1.00 14.82 ? 71  ASN A C   1 
ATOM   551  O  O   . ASN A  1 71  ? 36.705  0.924   17.624  1.00 15.36 ? 71  ASN A O   1 
ATOM   552  C  CB  . ASN A  1 71  ? 36.043  4.030   17.845  1.00 16.48 ? 71  ASN A CB  1 
ATOM   553  C  CG  . ASN A  1 71  ? 35.167  5.273   17.906  1.00 25.10 ? 71  ASN A CG  1 
ATOM   554  O  OD1 . ASN A  1 71  ? 33.938  5.218   17.692  1.00 27.16 ? 71  ASN A OD1 1 
ATOM   555  N  ND2 . ASN A  1 71  ? 35.785  6.434   18.197  1.00 32.37 ? 71  ASN A ND2 1 
ATOM   556  N  N   . LEU A  1 72  ? 36.415  1.744   15.513  1.00 13.69 ? 72  LEU A N   1 
ATOM   557  C  CA  . LEU A  1 72  ? 37.215  0.721   14.861  1.00 13.77 ? 72  LEU A CA  1 
ATOM   558  C  C   . LEU A  1 72  ? 38.366  1.398   14.134  1.00 14.18 ? 72  LEU A C   1 
ATOM   559  O  O   . LEU A  1 72  ? 38.185  2.499   13.598  1.00 15.64 ? 72  LEU A O   1 
ATOM   560  C  CB  . LEU A  1 72  ? 36.366  -0.145  13.858  1.00 12.13 ? 72  LEU A CB  1 
ATOM   561  C  CG  . LEU A  1 72  ? 35.337  -1.038  14.594  1.00 13.39 ? 72  LEU A CG  1 
ATOM   562  C  CD1 . LEU A  1 72  ? 34.435  -1.679  13.538  1.00 11.63 ? 72  LEU A CD1 1 
ATOM   563  C  CD2 . LEU A  1 72  ? 35.893  -2.092  15.587  1.00 13.30 ? 72  LEU A CD2 1 
ATOM   564  N  N   . PRO A  1 73  ? 39.506  0.672   13.937  1.00 14.65 ? 73  PRO A N   1 
ATOM   565  C  CA  . PRO A  1 73  ? 40.635  1.331   13.218  1.00 15.59 ? 73  PRO A CA  1 
ATOM   566  C  C   . PRO A  1 73  ? 40.559  1.164   11.725  1.00 15.09 ? 73  PRO A C   1 
ATOM   567  O  O   . PRO A  1 73  ? 40.093  0.145   11.240  1.00 17.46 ? 73  PRO A O   1 
ATOM   568  C  CB  . PRO A  1 73  ? 41.844  0.535   13.790  1.00 15.25 ? 73  PRO A CB  1 
ATOM   569  C  CG  . PRO A  1 73  ? 41.324  -0.863  14.024  1.00 15.18 ? 73  PRO A CG  1 
ATOM   570  C  CD  . PRO A  1 73  ? 39.875  -0.649  14.519  1.00 14.51 ? 73  PRO A CD  1 
ATOM   571  N  N   . SER A  1 74  ? 41.128  2.126   11.011  1.00 17.86 ? 74  SER A N   1 
ATOM   572  C  CA  . SER A  1 74  ? 40.994  2.146   9.546   1.00 19.89 ? 74  SER A CA  1 
ATOM   573  C  C   . SER A  1 74  ? 41.908  1.109   8.886   1.00 18.52 ? 74  SER A C   1 
ATOM   574  O  O   . SER A  1 74  ? 41.784  0.871   7.663   1.00 19.50 ? 74  SER A O   1 
ATOM   575  C  CB  . SER A  1 74  ? 41.265  3.502   9.004   1.00 22.65 ? 74  SER A CB  1 
ATOM   576  O  OG  . SER A  1 74  ? 42.584  3.894   9.354   1.00 23.94 ? 74  SER A OG  1 
ATOM   577  N  N   . ASP A  1 75  ? 42.813  0.435   9.623   1.00 18.03 ? 75  ASP A N   1 
ATOM   578  C  CA  . ASP A  1 75  ? 43.519  -0.678  8.952   1.00 19.07 ? 75  ASP A CA  1 
ATOM   579  C  C   . ASP A  1 75  ? 42.644  -1.925  8.863   1.00 16.70 ? 75  ASP A C   1 
ATOM   580  O  O   . ASP A  1 75  ? 42.972  -2.877  8.189   1.00 17.93 ? 75  ASP A O   1 
ATOM   581  C  CB  . ASP A  1 75  ? 44.854  -0.992  9.665   1.00 20.39 ? 75  ASP A CB  1 
ATOM   582  C  CG  . ASP A  1 75  ? 44.606  -1.442  11.062  1.00 25.73 ? 75  ASP A CG  1 
ATOM   583  O  OD1 . ASP A  1 75  ? 44.199  -0.610  11.895  1.00 28.23 ? 75  ASP A OD1 1 
ATOM   584  O  OD2 . ASP A  1 75  ? 44.842  -2.615  11.361  1.00 27.96 ? 75  ASP A OD2 1 
ATOM   585  N  N   . MET A  1 76  ? 41.494  -1.899  9.549   1.00 14.49 ? 76  MET A N   1 
ATOM   586  C  CA  . MET A  1 76  ? 40.489  -2.990  9.405   1.00 13.79 ? 76  MET A CA  1 
ATOM   587  C  C   . MET A  1 76  ? 39.661  -2.710  8.150   1.00 11.93 ? 76  MET A C   1 
ATOM   588  O  O   . MET A  1 76  ? 39.250  -1.568  7.936   1.00 13.35 ? 76  MET A O   1 
ATOM   589  C  CB  . MET A  1 76  ? 39.675  -2.971  10.686  1.00 16.42 ? 76  MET A CB  1 
ATOM   590  C  CG  . MET A  1 76  ? 38.543  -3.866  10.699  1.00 15.94 ? 76  MET A CG  1 
ATOM   591  S  SD  . MET A  1 76  ? 37.773  -3.810  12.346  1.00 16.35 ? 76  MET A SD  1 
ATOM   592  C  CE  . MET A  1 76  ? 36.211  -4.600  11.862  1.00 15.18 ? 76  MET A CE  1 
ATOM   593  N  N   . HIS A  1 77  ? 39.627  -3.681  7.266   1.00 10.55 ? 77  HIS A N   1 
ATOM   594  C  CA  . HIS A  1 77  ? 38.872  -3.442  5.988   1.00 10.93 ? 77  HIS A CA  1 
ATOM   595  C  C   . HIS A  1 77  ? 38.277  -4.630  5.377   1.00 12.06 ? 77  HIS A C   1 
ATOM   596  O  O   . HIS A  1 77  ? 38.618  -5.813  5.699   1.00 12.76 ? 77  HIS A O   1 
ATOM   597  C  CB  . HIS A  1 77  ? 39.757  -2.694  4.966   1.00 13.81 ? 77  HIS A CB  1 
ATOM   598  C  CG  . HIS A  1 77  ? 40.961  -3.516  4.507   1.00 14.81 ? 77  HIS A CG  1 
ATOM   599  N  ND1 . HIS A  1 77  ? 42.162  -3.392  5.109   1.00 17.96 ? 77  HIS A ND1 1 
ATOM   600  C  CD2 . HIS A  1 77  ? 41.117  -4.376  3.480   1.00 16.61 ? 77  HIS A CD2 1 
ATOM   601  C  CE1 . HIS A  1 77  ? 43.046  -4.176  4.488   1.00 17.17 ? 77  HIS A CE1 1 
ATOM   602  N  NE2 . HIS A  1 77  ? 42.445  -4.796  3.504   1.00 17.63 ? 77  HIS A NE2 1 
ATOM   603  N  N   . ILE A  1 78  ? 37.293  -4.397  4.501   1.00 12.65 ? 78  ILE A N   1 
ATOM   604  C  CA  . ILE A  1 78  ? 36.796  -5.453  3.606   1.00 13.73 ? 78  ILE A CA  1 
ATOM   605  C  C   . ILE A  1 78  ? 37.570  -5.522  2.318   1.00 13.49 ? 78  ILE A C   1 
ATOM   606  O  O   . ILE A  1 78  ? 37.804  -4.477  1.743   1.00 13.95 ? 78  ILE A O   1 
ATOM   607  C  CB  . ILE A  1 78  ? 35.320  -5.139  3.221   1.00 13.42 ? 78  ILE A CB  1 
ATOM   608  C  CG1 . ILE A  1 78  ? 34.388  -5.184  4.491   1.00 15.21 ? 78  ILE A CG1 1 
ATOM   609  C  CG2 . ILE A  1 78  ? 34.832  -5.994  2.068   1.00 16.22 ? 78  ILE A CG2 1 
ATOM   610  C  CD1 . ILE A  1 78  ? 33.042  -4.444  4.238   1.00 14.93 ? 78  ILE A CD1 1 
ATOM   611  N  N   . GLN A  1 79  ? 37.950  -6.759  1.919   1.00 13.89 ? 79  GLN A N   1 
ATOM   612  C  CA  . GLN A  1 79  ? 38.486  -7.004  0.589   1.00 16.42 ? 79  GLN A CA  1 
ATOM   613  C  C   . GLN A  1 79  ? 37.450  -7.784  -0.238  1.00 15.00 ? 79  GLN A C   1 
ATOM   614  O  O   . GLN A  1 79  ? 36.788  -8.688  0.283   1.00 17.10 ? 79  GLN A O   1 
ATOM   615  C  CB  . GLN A  1 79  ? 39.777  -7.853  0.856   1.00 21.36 ? 79  GLN A CB  1 
ATOM   616  C  CG  . GLN A  1 79  ? 40.503  -8.331  -0.421  1.00 27.92 ? 79  GLN A CG  1 
ATOM   617  C  CD  . GLN A  1 79  ? 41.475  -7.307  -0.973  1.00 38.40 ? 79  GLN A CD  1 
ATOM   618  O  OE1 . GLN A  1 79  ? 41.664  -6.202  -0.402  1.00 43.75 ? 79  GLN A OE1 1 
ATOM   619  N  NE2 . GLN A  1 79  ? 42.102  -7.656  -2.112  1.00 42.48 ? 79  GLN A NE2 1 
ATOM   620  N  N   . GLY A  1 80  ? 37.338  -7.477  -1.502  1.00 16.53 ? 80  GLY A N   1 
ATOM   621  C  CA  . GLY A  1 80  ? 36.368  -8.217  -2.369  1.00 16.57 ? 80  GLY A CA  1 
ATOM   622  C  C   . GLY A  1 80  ? 35.457  -7.271  -3.114  1.00 17.51 ? 80  GLY A C   1 
ATOM   623  O  O   . GLY A  1 80  ? 34.822  -7.675  -4.102  1.00 21.15 ? 80  GLY A O   1 
ATOM   624  N  N   . LEU A  1 81  ? 35.308  -6.036  -2.632  1.00 15.31 ? 81  LEU A N   1 
ATOM   625  C  CA  . LEU A  1 81  ? 34.524  -5.043  -3.362  1.00 18.34 ? 81  LEU A CA  1 
ATOM   626  C  C   . LEU A  1 81  ? 35.516  -4.358  -4.371  1.00 21.62 ? 81  LEU A C   1 
ATOM   627  O  O   . LEU A  1 81  ? 36.733  -4.624  -4.389  1.00 21.53 ? 81  LEU A O   1 
ATOM   628  C  CB  . LEU A  1 81  ? 33.801  -4.073  -2.423  1.00 16.01 ? 81  LEU A CB  1 
ATOM   629  C  CG  . LEU A  1 81  ? 32.823  -4.765  -1.412  1.00 14.97 ? 81  LEU A CG  1 
ATOM   630  C  CD1 . LEU A  1 81  ? 32.370  -3.819  -0.262  1.00 14.87 ? 81  LEU A CD1 1 
ATOM   631  C  CD2 . LEU A  1 81  ? 31.573  -5.395  -2.140  1.00 17.34 ? 81  LEU A CD2 1 
ATOM   632  N  N   . GLN A  1 82  ? 34.975  -3.528  -5.237  1.00 25.08 ? 82  GLN A N   1 
ATOM   633  C  CA  . GLN A  1 82  ? 35.840  -2.910  -6.241  1.00 24.91 ? 82  GLN A CA  1 
ATOM   634  C  C   . GLN A  1 82  ? 36.846  -1.962  -5.575  1.00 22.62 ? 82  GLN A C   1 
ATOM   635  O  O   . GLN A  1 82  ? 38.031  -1.869  -6.045  1.00 22.53 ? 82  GLN A O   1 
ATOM   636  C  CB  . GLN A  1 82  ? 34.962  -2.072  -7.126  1.00 32.08 ? 82  GLN A CB  1 
ATOM   637  C  CG  . GLN A  1 82  ? 34.086  -2.888  -8.064  1.00 41.25 ? 82  GLN A CG  1 
ATOM   638  C  CD  . GLN A  1 82  ? 34.777  -2.988  -9.399  1.00 45.69 ? 82  GLN A CD  1 
ATOM   639  O  OE1 . GLN A  1 82  ? 34.791  -2.011  -10.173 1.00 45.22 ? 82  GLN A OE1 1 
ATOM   640  N  NE2 . GLN A  1 82  ? 35.438  -4.129  -9.641  1.00 39.94 ? 82  GLN A NE2 1 
ATOM   641  N  N   . SER A  1 83  ? 36.369  -1.241  -4.555  1.00 18.50 ? 83  SER A N   1 
ATOM   642  C  CA  . SER A  1 83  ? 37.262  -0.365  -3.782  1.00 14.30 ? 83  SER A CA  1 
ATOM   643  C  C   . SER A  1 83  ? 37.461  -1.006  -2.431  1.00 13.30 ? 83  SER A C   1 
ATOM   644  O  O   . SER A  1 83  ? 36.634  -1.853  -2.010  1.00 13.01 ? 83  SER A O   1 
ATOM   645  C  CB  . SER A  1 83  ? 36.610  0.970   -3.483  1.00 13.53 ? 83  SER A CB  1 
ATOM   646  O  OG  . SER A  1 83  ? 36.436  1.717   -4.694  1.00 15.28 ? 83  SER A OG  1 
ATOM   647  N  N   . ARG A  1 84  ? 38.520  -0.595  -1.703  1.00 13.19 ? 84  ARG A N   1 
ATOM   648  C  CA  . ARG A  1 84  ? 38.683  -1.033  -0.318  1.00 12.25 ? 84  ARG A CA  1 
ATOM   649  C  C   . ARG A  1 84  ? 37.731  -0.237  0.553   1.00 11.43 ? 84  ARG A C   1 
ATOM   650  O  O   . ARG A  1 84  ? 37.657  1.012   0.393   1.00 10.45 ? 84  ARG A O   1 
ATOM   651  C  CB  . ARG A  1 84  ? 40.139  -0.751  0.092   1.00 11.97 ? 84  ARG A CB  1 
ATOM   652  C  CG  . ARG A  1 84  ? 40.333  -1.035  1.594   1.00 12.49 ? 84  ARG A CG  1 
ATOM   653  C  CD  . ARG A  1 84  ? 41.791  -0.890  2.096   1.00 12.99 ? 84  ARG A CD  1 
ATOM   654  N  NE  . ARG A  1 84  ? 42.589  -1.962  1.602   1.00 14.00 ? 84  ARG A NE  1 
ATOM   655  C  CZ  . ARG A  1 84  ? 43.855  -2.089  1.926   1.00 14.47 ? 84  ARG A CZ  1 
ATOM   656  N  NH1 . ARG A  1 84  ? 44.399  -1.179  2.691   1.00 17.45 ? 84  ARG A NH1 1 
ATOM   657  N  NH2 . ARG A  1 84  ? 44.577  -3.080  1.455   1.00 16.07 ? 84  ARG A NH2 1 
ATOM   658  N  N   . TYR A  1 85  ? 37.028  -0.913  1.480   1.00 10.22 ? 85  TYR A N   1 
ATOM   659  C  CA  . TYR A  1 85  ? 36.174  -0.172  2.421   1.00 10.34 ? 85  TYR A CA  1 
ATOM   660  C  C   . TYR A  1 85  ? 36.752  -0.470  3.804   1.00 10.12 ? 85  TYR A C   1 
ATOM   661  O  O   . TYR A  1 85  ? 36.859  -1.604  4.239   1.00 11.90 ? 85  TYR A O   1 
ATOM   662  C  CB  . TYR A  1 85  ? 34.742  -0.659  2.337   1.00 11.15 ? 85  TYR A CB  1 
ATOM   663  C  CG  . TYR A  1 85  ? 34.015  -0.112  1.141   1.00 9.77  ? 85  TYR A CG  1 
ATOM   664  C  CD1 . TYR A  1 85  ? 34.176  -0.681  -0.118  1.00 10.74 ? 85  TYR A CD1 1 
ATOM   665  C  CD2 . TYR A  1 85  ? 33.176  0.982   1.265   1.00 10.87 ? 85  TYR A CD2 1 
ATOM   666  C  CE1 . TYR A  1 85  ? 33.507  -0.176  -1.218  1.00 10.85 ? 85  TYR A CE1 1 
ATOM   667  C  CE2 . TYR A  1 85  ? 32.507  1.494   0.175   1.00 9.12  ? 85  TYR A CE2 1 
ATOM   668  C  CZ  . TYR A  1 85  ? 32.672  0.915   -1.062  1.00 10.37 ? 85  TYR A CZ  1 
ATOM   669  O  OH  . TYR A  1 85  ? 31.991  1.448   -2.132  1.00 15.31 ? 85  TYR A OH  1 
ATOM   670  N  N   . SER A  1 86  ? 37.147  0.606   4.465   1.00 10.67 ? 86  SER A N   1 
ATOM   671  C  CA  . SER A  1 86  ? 37.858  0.544   5.773   1.00 10.58 ? 86  SER A CA  1 
ATOM   672  C  C   . SER A  1 86  ? 36.840  0.757   6.909   1.00 10.40 ? 86  SER A C   1 
ATOM   673  O  O   . SER A  1 86  ? 35.923  1.532   6.774   1.00 11.78 ? 86  SER A O   1 
ATOM   674  C  CB  . SER A  1 86  ? 38.947  1.611   5.867   1.00 12.60 ? 86  SER A CB  1 
ATOM   675  O  OG  . SER A  1 86  ? 40.001  1.295   4.935   1.00 14.50 ? 86  SER A OG  1 
ATOM   676  N  N   . ALA A  1 87  ? 37.042  0.028   8.030   1.00 10.53 ? 87  ALA A N   1 
ATOM   677  C  CA  . ALA A  1 87  ? 36.110  0.159   9.139   1.00 11.24 ? 87  ALA A CA  1 
ATOM   678  C  C   . ALA A  1 87  ? 36.216  1.502   9.799   1.00 10.71 ? 87  ALA A C   1 
ATOM   679  O  O   . ALA A  1 87  ? 37.320  2.136   9.904   1.00 12.85 ? 87  ALA A O   1 
ATOM   680  C  CB  . ALA A  1 87  ? 36.315  -0.929  10.138  1.00 12.12 ? 87  ALA A CB  1 
ATOM   681  N  N   . THR A  1 88  ? 35.088  1.959   10.315  1.00 10.32 ? 88  THR A N   1 
ATOM   682  C  CA  . THR A  1 88  ? 35.023  3.132   11.195  1.00 11.10 ? 88  THR A CA  1 
ATOM   683  C  C   . THR A  1 88  ? 34.368  2.835   12.560  1.00 10.75 ? 88  THR A C   1 
ATOM   684  O  O   . THR A  1 88  ? 34.797  3.342   13.553  1.00 10.93 ? 88  THR A O   1 
ATOM   685  C  CB  . THR A  1 88  ? 34.358  4.287   10.459  1.00 13.54 ? 88  THR A CB  1 
ATOM   686  O  OG1 . THR A  1 88  ? 34.313  5.427   11.325  1.00 16.58 ? 88  THR A OG1 1 
ATOM   687  C  CG2 . THR A  1 88  ? 32.950  3.997   10.056  1.00 15.07 ? 88  THR A CG2 1 
ATOM   688  N  N   . GLN A  1 89  ? 33.312  2.030   12.622  1.00 10.76 ? 89  GLN A N   1 
ATOM   689  C  CA  . GLN A  1 89  ? 32.636  1.778   13.906  1.00 11.14 ? 89  GLN A CA  1 
ATOM   690  C  C   . GLN A  1 89  ? 31.660  0.617   13.740  1.00 9.76  ? 89  GLN A C   1 
ATOM   691  O  O   . GLN A  1 89  ? 31.271  0.314   12.609  1.00 10.56 ? 89  GLN A O   1 
ATOM   692  C  CB  . GLN A  1 89  ? 31.847  3.001   14.433  1.00 12.43 ? 89  GLN A CB  1 
ATOM   693  C  CG  . GLN A  1 89  ? 30.907  3.596   13.416  1.00 15.61 ? 89  GLN A CG  1 
ATOM   694  C  CD  . GLN A  1 89  ? 29.469  3.429   13.837  1.00 16.22 ? 89  GLN A CD  1 
ATOM   695  O  OE1 . GLN A  1 89  ? 29.091  2.378   14.255  1.00 15.53 ? 89  GLN A OE1 1 
ATOM   696  N  NE2 . GLN A  1 89  ? 28.685  4.428   13.660  1.00 22.72 ? 89  GLN A NE2 1 
ATOM   697  N  N   . LEU A  1 90  ? 31.324  0.018   14.873  1.00 9.63  ? 90  LEU A N   1 
ATOM   698  C  CA  . LEU A  1 90  ? 30.172  -0.912  14.932  1.00 9.38  ? 90  LEU A CA  1 
ATOM   699  C  C   . LEU A  1 90  ? 29.220  -0.501  15.991  1.00 9.00  ? 90  LEU A C   1 
ATOM   700  O  O   . LEU A  1 90  ? 29.564  0.235   16.904  1.00 9.51  ? 90  LEU A O   1 
ATOM   701  C  CB  . LEU A  1 90  ? 30.663  -2.382  15.032  1.00 9.94  ? 90  LEU A CB  1 
ATOM   702  C  CG  . LEU A  1 90  ? 31.414  -2.883  16.307  1.00 11.19 ? 90  LEU A CG  1 
ATOM   703  C  CD1 . LEU A  1 90  ? 30.471  -2.924  17.560  1.00 11.82 ? 90  LEU A CD1 1 
ATOM   704  C  CD2 . LEU A  1 90  ? 32.098  -4.201  15.926  1.00 11.57 ? 90  LEU A CD2 1 
ATOM   705  N  N   . HIS A  1 91  ? 27.952  -0.893  15.778  1.00 8.99  ? 91  HIS A N   1 
ATOM   706  C  CA  . HIS A  1 91  ? 26.899  -0.583  16.763  1.00 8.60  ? 91  HIS A CA  1 
ATOM   707  C  C   . HIS A  1 91  ? 25.736  -1.519  16.515  1.00 8.12  ? 91  HIS A C   1 
ATOM   708  O  O   . HIS A  1 91  ? 25.774  -2.378  15.652  1.00 8.62  ? 91  HIS A O   1 
ATOM   709  C  CB  . HIS A  1 91  ? 26.436  0.886   16.566  1.00 9.75  ? 91  HIS A CB  1 
ATOM   710  C  CG  . HIS A  1 91  ? 25.817  1.123   15.215  1.00 8.71  ? 91  HIS A CG  1 
ATOM   711  N  ND1 . HIS A  1 91  ? 26.540  1.569   14.159  1.00 8.80  ? 91  HIS A ND1 1 
ATOM   712  C  CD2 . HIS A  1 91  ? 24.520  0.832   14.763  1.00 8.40  ? 91  HIS A CD2 1 
ATOM   713  C  CE1 . HIS A  1 91  ? 25.746  1.536   13.022  1.00 8.28  ? 91  HIS A CE1 1 
ATOM   714  N  NE2 . HIS A  1 91  ? 24.530  1.059   13.374  1.00 7.05  ? 91  HIS A NE2 1 
ATOM   715  N  N   . LEU A  1 92  ? 24.753  -1.395  17.433  1.00 8.21  ? 92  LEU A N   1 
ATOM   716  C  CA  . LEU A  1 92  ? 23.650  -2.339  17.407  1.00 8.46  ? 92  LEU A CA  1 
ATOM   717  C  C   . LEU A  1 92  ? 22.284  -1.630  17.426  1.00 8.29  ? 92  LEU A C   1 
ATOM   718  O  O   . LEU A  1 92  ? 22.145  -0.473  17.731  1.00 8.85  ? 92  LEU A O   1 
ATOM   719  C  CB  . LEU A  1 92  ? 23.677  -3.328  18.639  1.00 11.53 ? 92  LEU A CB  1 
ATOM   720  C  CG  . LEU A  1 92  ? 24.932  -4.218  18.547  1.00 11.49 ? 92  LEU A CG  1 
ATOM   721  C  CD1 . LEU A  1 92  ? 25.907  -3.705  19.616  1.00 15.91 ? 92  LEU A CD1 1 
ATOM   722  C  CD2 . LEU A  1 92  ? 24.526  -5.624  18.903  1.00 14.06 ? 92  LEU A CD2 1 
ATOM   723  N  N   . HIS A  1 93  ? 21.256  -2.420  17.063  1.00 7.93  ? 93  HIS A N   1 
ATOM   724  C  CA  . HIS A  1 93  ? 19.816  -1.962  17.137  1.00 7.99  ? 93  HIS A CA  1 
ATOM   725  C  C   . HIS A  1 93  ? 19.032  -3.096  17.742  1.00 8.72  ? 93  HIS A C   1 
ATOM   726  O  O   . HIS A  1 93  ? 19.323  -4.286  17.544  1.00 9.92  ? 93  HIS A O   1 
ATOM   727  C  CB  . HIS A  1 93  ? 19.292  -1.745  15.673  1.00 8.09  ? 93  HIS A CB  1 
ATOM   728  C  CG  . HIS A  1 93  ? 20.068  -0.740  14.909  1.00 7.25  ? 93  HIS A CG  1 
ATOM   729  N  ND1 . HIS A  1 93  ? 19.774  0.595   14.887  1.00 7.56  ? 93  HIS A ND1 1 
ATOM   730  C  CD2 . HIS A  1 93  ? 21.179  -0.899  14.080  1.00 6.51  ? 93  HIS A CD2 1 
ATOM   731  C  CE1 . HIS A  1 93  ? 20.692  1.276   14.093  1.00 7.84  ? 93  HIS A CE1 1 
ATOM   732  N  NE2 . HIS A  1 93  ? 21.481  0.374   13.549  1.00 7.16  ? 93  HIS A NE2 1 
ATOM   733  N  N   . TRP A  1 94  ? 18.085  -2.726  18.619  1.00 8.96  ? 94  TRP A N   1 
ATOM   734  C  CA  . TRP A  1 94  ? 17.336  -3.747  19.388  1.00 8.82  ? 94  TRP A CA  1 
ATOM   735  C  C   . TRP A  1 94  ? 15.960  -3.196  19.763  1.00 9.47  ? 94  TRP A C   1 
ATOM   736  O  O   . TRP A  1 94  ? 15.632  -2.029  19.527  1.00 8.70  ? 94  TRP A O   1 
ATOM   737  C  CB  . TRP A  1 94  ? 18.127  -4.151  20.663  1.00 8.81  ? 94  TRP A CB  1 
ATOM   738  C  CG  . TRP A  1 94  ? 18.442  -3.012  21.588  1.00 8.86  ? 94  TRP A CG  1 
ATOM   739  C  CD1 . TRP A  1 94  ? 17.596  -2.488  22.585  1.00 9.12  ? 94  TRP A CD1 1 
ATOM   740  C  CD2 . TRP A  1 94  ? 19.618  -2.174  21.560  1.00 9.14  ? 94  TRP A CD2 1 
ATOM   741  N  NE1 . TRP A  1 94  ? 18.214  -1.413  23.206  1.00 9.14  ? 94  TRP A NE1 1 
ATOM   742  C  CE2 . TRP A  1 94  ? 19.476  -1.212  22.629  1.00 9.43  ? 94  TRP A CE2 1 
ATOM   743  C  CE3 . TRP A  1 94  ? 20.807  -2.206  20.816  1.00 8.91  ? 94  TRP A CE3 1 
ATOM   744  C  CZ2 . TRP A  1 94  ? 20.445  -0.322  22.963  1.00 9.49  ? 94  TRP A CZ2 1 
ATOM   745  C  CZ3 . TRP A  1 94  ? 21.773  -1.229  21.091  1.00 9.49  ? 94  TRP A CZ3 1 
ATOM   746  C  CH2 . TRP A  1 94  ? 21.606  -0.312  22.153  1.00 9.24  ? 94  TRP A CH2 1 
ATOM   747  N  N   . GLY A  1 95  ? 15.178  -4.100  20.330  1.00 9.09  ? 95  GLY A N   1 
ATOM   748  C  CA  . GLY A  1 95  ? 13.776  -3.795  20.707  1.00 10.71 ? 95  GLY A CA  1 
ATOM   749  C  C   . GLY A  1 95  ? 13.664  -3.492  22.205  1.00 9.58  ? 95  GLY A C   1 
ATOM   750  O  O   . GLY A  1 95  ? 14.316  -2.628  22.752  1.00 9.93  ? 95  GLY A O   1 
ATOM   751  N  N   . ASN A  1 96  ? 12.816  -4.279  22.868  1.00 11.14 ? 96  ASN A N   1 
ATOM   752  C  CA  . ASN A  1 96  ? 12.613  -4.079  24.370  1.00 11.76 ? 96  ASN A CA  1 
ATOM   753  C  C   . ASN A  1 96  ? 12.132  -5.400  24.942  1.00 12.58 ? 96  ASN A C   1 
ATOM   754  O  O   . ASN A  1 96  ? 11.718  -6.297  24.225  1.00 11.49 ? 96  ASN A O   1 
ATOM   755  C  CB  . ASN A  1 96  ? 11.643  -2.920  24.586  1.00 13.45 ? 96  ASN A CB  1 
ATOM   756  C  CG  . ASN A  1 96  ? 10.233  -3.286  24.217  1.00 14.61 ? 96  ASN A CG  1 
ATOM   757  O  OD1 . ASN A  1 96  ? 9.562   -3.903  25.072  1.00 17.57 ? 96  ASN A OD1 1 
ATOM   758  N  ND2 . ASN A  1 96  ? 9.767   -2.994  23.009  1.00 16.21 ? 96  ASN A ND2 1 
ATOM   759  N  N   . PRO A  1 97  ? 12.221  -5.516  26.282  1.00 12.76 ? 97  PRO A N   1 
ATOM   760  C  CA  . PRO A  1 97  ? 11.879  -6.834  26.831  1.00 12.93 ? 97  PRO A CA  1 
ATOM   761  C  C   . PRO A  1 97  ? 10.438  -7.277  26.589  1.00 13.15 ? 97  PRO A C   1 
ATOM   762  O  O   . PRO A  1 97  ? 10.216  -8.481  26.551  1.00 14.04 ? 97  PRO A O   1 
ATOM   763  C  CB  . PRO A  1 97  ? 12.166  -6.694  28.338  1.00 14.34 ? 97  PRO A CB  1 
ATOM   764  C  CG  . PRO A  1 97  ? 13.278  -5.644  28.363  1.00 14.93 ? 97  PRO A CG  1 
ATOM   765  C  CD  . PRO A  1 97  ? 12.886  -4.658  27.276  1.00 14.40 ? 97  PRO A CD  1 
ATOM   766  N  N   . ASN A  1 98  ? 9.501   -6.353  26.478  1.00 12.46 ? 98  ASN A N   1 
ATOM   767  C  CA  . ASN A  1 98  ? 8.120   -6.813  26.154  1.00 16.02 ? 98  ASN A CA  1 
ATOM   768  C  C   . ASN A  1 98  ? 7.891   -7.167  24.709  1.00 14.20 ? 98  ASN A C   1 
ATOM   769  O  O   . ASN A  1 98  ? 6.913   -7.830  24.361  1.00 17.52 ? 98  ASN A O   1 
ATOM   770  C  CB  . ASN A  1 98  ? 7.191   -5.646  26.565  1.00 15.70 ? 98  ASN A CB  1 
ATOM   771  C  CG  . ASN A  1 98  ? 7.052   -5.534  28.071  1.00 24.24 ? 98  ASN A CG  1 
ATOM   772  O  OD1 . ASN A  1 98  ? 7.131   -6.517  28.800  1.00 28.70 ? 98  ASN A OD1 1 
ATOM   773  N  ND2 . ASN A  1 98  ? 6.745   -4.353  28.511  1.00 28.47 ? 98  ASN A ND2 1 
ATOM   774  N  N   . ASP A  1 99  ? 8.834   -6.823  23.834  1.00 12.55 ? 99  ASP A N   1 
ATOM   775  C  CA  . ASP A  1 99  ? 8.695   -7.090  22.391  1.00 12.44 ? 99  ASP A CA  1 
ATOM   776  C  C   . ASP A  1 99  ? 10.111  -7.203  21.768  1.00 11.06 ? 99  ASP A C   1 
ATOM   777  O  O   . ASP A  1 99  ? 10.639  -6.243  21.234  1.00 12.00 ? 99  ASP A O   1 
ATOM   778  C  CB  . ASP A  1 99  ? 7.872   -6.001  21.710  1.00 14.09 ? 99  ASP A CB  1 
ATOM   779  C  CG  . ASP A  1 99  ? 7.363   -6.424  20.336  1.00 16.12 ? 99  ASP A CG  1 
ATOM   780  O  OD1 . ASP A  1 99  ? 7.736   -7.475  19.818  1.00 16.62 ? 99  ASP A OD1 1 
ATOM   781  O  OD2 . ASP A  1 99  ? 6.547   -5.680  19.762  1.00 20.53 ? 99  ASP A OD2 1 
ATOM   782  N  N   . PRO A  1 100 ? 10.801  -8.309  22.099  1.00 11.14 ? 100 PRO A N   1 
ATOM   783  C  CA  . PRO A  1 100 ? 12.266  -8.422  21.863  1.00 10.93 ? 100 PRO A CA  1 
ATOM   784  C  C   . PRO A  1 100 ? 12.591  -8.745  20.441  1.00 11.94 ? 100 PRO A C   1 
ATOM   785  O  O   . PRO A  1 100 ? 13.227  -9.748  20.143  1.00 12.23 ? 100 PRO A O   1 
ATOM   786  C  CB  . PRO A  1 100 ? 12.684  -9.495  22.860  1.00 12.08 ? 100 PRO A CB  1 
ATOM   787  C  CG  . PRO A  1 100 ? 11.469  -10.396 22.922  1.00 12.28 ? 100 PRO A CG  1 
ATOM   788  C  CD  . PRO A  1 100 ? 10.273  -9.455  22.906  1.00 12.13 ? 100 PRO A CD  1 
ATOM   789  N  N   . HIS A  1 101 ? 12.133  -7.893  19.538  1.00 11.39 ? 101 HIS A N   1 
ATOM   790  C  CA  . HIS A  1 101 ? 12.310  -8.167  18.065  1.00 12.83 ? 101 HIS A CA  1 
ATOM   791  C  C   . HIS A  1 101 ? 12.623  -6.902  17.327  1.00 13.44 ? 101 HIS A C   1 
ATOM   792  O  O   . HIS A  1 101 ? 11.824  -6.370  16.520  1.00 17.50 ? 101 HIS A O   1 
ATOM   793  C  CB  . HIS A  1 101 ? 11.004  -8.739  17.469  1.00 14.08 ? 101 HIS A CB  1 
ATOM   794  C  CG  . HIS A  1 101 ? 10.456  -9.854  18.292  1.00 13.42 ? 101 HIS A CG  1 
ATOM   795  N  ND1 . HIS A  1 101 ? 10.985  -11.094 18.282  1.00 15.24 ? 101 HIS A ND1 1 
ATOM   796  C  CD2 . HIS A  1 101 ? 9.416   -9.865  19.205  1.00 14.20 ? 101 HIS A CD2 1 
ATOM   797  C  CE1 . HIS A  1 101 ? 10.309  -11.860 19.191  1.00 14.76 ? 101 HIS A CE1 1 
ATOM   798  N  NE2 . HIS A  1 101 ? 9.393   -11.077 19.779  1.00 14.46 ? 101 HIS A NE2 1 
ATOM   799  N  N   . GLY A  1 102 ? 13.842  -6.427  17.569  1.00 9.42  ? 102 GLY A N   1 
ATOM   800  C  CA  . GLY A  1 102 ? 14.271  -5.094  17.172  1.00 9.57  ? 102 GLY A CA  1 
ATOM   801  C  C   . GLY A  1 102 ? 15.377  -5.086  16.083  1.00 8.88  ? 102 GLY A C   1 
ATOM   802  O  O   . GLY A  1 102 ? 16.075  -4.074  16.035  1.00 8.73  ? 102 GLY A O   1 
ATOM   803  N  N   . SER A  1 103 ? 15.507  -6.120  15.246  1.00 8.81  ? 103 SER A N   1 
ATOM   804  C  CA  . SER A  1 103 ? 16.372  -5.913  14.083  1.00 7.45  ? 103 SER A CA  1 
ATOM   805  C  C   . SER A  1 103 ? 15.800  -4.805  13.195  1.00 8.35  ? 103 SER A C   1 
ATOM   806  O  O   . SER A  1 103 ? 14.610  -4.457  13.291  1.00 9.85  ? 103 SER A O   1 
ATOM   807  C  CB  . SER A  1 103 ? 16.540  -7.202  13.272  1.00 8.70  ? 103 SER A CB  1 
ATOM   808  O  OG  . SER A  1 103 ? 15.312  -7.648  12.660  1.00 8.52  ? 103 SER A OG  1 
ATOM   809  N  N   . GLU A  1 104 ? 16.644  -4.337  12.287  1.00 7.85  ? 104 GLU A N   1 
ATOM   810  C  CA  . GLU A  1 104 ? 16.169  -3.347  11.265  1.00 7.01  ? 104 GLU A CA  1 
ATOM   811  C  C   . GLU A  1 104 ? 15.710  -4.063  10.040  1.00 7.75  ? 104 GLU A C   1 
ATOM   812  O  O   . GLU A  1 104 ? 14.563  -3.858  9.620   1.00 7.76  ? 104 GLU A O   1 
ATOM   813  C  CB  . GLU A  1 104 ? 17.303  -2.369  10.905  1.00 7.17  ? 104 GLU A CB  1 
ATOM   814  C  CG  . GLU A  1 104 ? 17.868  -1.702  12.184  1.00 7.68  ? 104 GLU A CG  1 
ATOM   815  C  CD  . GLU A  1 104 ? 18.240  -0.259  11.922  1.00 8.93  ? 104 GLU A CD  1 
ATOM   816  O  OE1 . GLU A  1 104 ? 19.299  -0.051  11.292  1.00 8.62  ? 104 GLU A OE1 1 
ATOM   817  O  OE2 . GLU A  1 104 ? 17.424  0.646   12.170  1.00 9.14  ? 104 GLU A OE2 1 
ATOM   818  N  N   . HIS A  1 105 ? 16.557  -4.823  9.382   1.00 7.08  ? 105 HIS A N   1 
ATOM   819  C  CA  . HIS A  1 105 ? 16.091  -5.677  8.312   1.00 6.98  ? 105 HIS A CA  1 
ATOM   820  C  C   . HIS A  1 105 ? 15.174  -6.775  8.856   1.00 6.94  ? 105 HIS A C   1 
ATOM   821  O  O   . HIS A  1 105 ? 15.340  -7.283  9.964   1.00 8.18  ? 105 HIS A O   1 
ATOM   822  C  CB  . HIS A  1 105 ? 17.300  -6.290  7.513   1.00 6.83  ? 105 HIS A CB  1 
ATOM   823  C  CG  . HIS A  1 105 ? 18.043  -5.217  6.810   1.00 7.20  ? 105 HIS A CG  1 
ATOM   824  N  ND1 . HIS A  1 105 ? 19.060  -4.490  7.399   1.00 7.97  ? 105 HIS A ND1 1 
ATOM   825  C  CD2 . HIS A  1 105 ? 17.854  -4.709  5.538   1.00 7.54  ? 105 HIS A CD2 1 
ATOM   826  C  CE1 . HIS A  1 105 ? 19.481  -3.535  6.511   1.00 7.95  ? 105 HIS A CE1 1 
ATOM   827  N  NE2 . HIS A  1 105 ? 18.781  -3.701  5.361   1.00 8.27  ? 105 HIS A NE2 1 
ATOM   828  N  N   . THR A  1 106 ? 14.240  -7.184  8.040   1.00 7.51  ? 106 THR A N   1 
ATOM   829  C  CA  . THR A  1 106 ? 13.380  -8.328  8.321   1.00 8.40  ? 106 THR A CA  1 
ATOM   830  C  C   . THR A  1 106 ? 13.543  -9.339  7.222   1.00 8.79  ? 106 THR A C   1 
ATOM   831  O  O   . THR A  1 106 ? 13.996  -9.031  6.102   1.00 9.05  ? 106 THR A O   1 
ATOM   832  C  CB  . THR A  1 106 ? 11.899  -7.903  8.499   1.00 9.42  ? 106 THR A CB  1 
ATOM   833  O  OG1 . THR A  1 106 ? 11.437  -7.301  7.287   1.00 9.34  ? 106 THR A OG1 1 
ATOM   834  C  CG2 . THR A  1 106 ? 11.740  -6.961  9.615   1.00 9.70  ? 106 THR A CG2 1 
ATOM   835  N  N   . VAL A  1 107 ? 13.179  -10.595 7.541   1.00 9.19  ? 107 VAL A N   1 
ATOM   836  C  CA  . VAL A  1 107 ? 13.256  -11.684 6.526   1.00 9.69  ? 107 VAL A CA  1 
ATOM   837  C  C   . VAL A  1 107 ? 11.858  -12.304 6.455   1.00 9.38  ? 107 VAL A C   1 
ATOM   838  O  O   . VAL A  1 107 ? 11.344  -12.776 7.473   1.00 9.72  ? 107 VAL A O   1 
ATOM   839  C  CB  . VAL A  1 107 ? 14.349  -12.736 6.903   1.00 9.67  ? 107 VAL A CB  1 
ATOM   840  C  CG1 . VAL A  1 107 ? 14.295  -13.903 5.890   1.00 11.76 ? 107 VAL A CG1 1 
ATOM   841  C  CG2 . VAL A  1 107 ? 15.776  -12.099 6.981   1.00 12.31 ? 107 VAL A CG2 1 
ATOM   842  N  N   . SER A  1 108 ? 11.288  -12.256 5.269   1.00 10.55 ? 108 SER A N   1 
ATOM   843  C  CA  . SER A  1 108 ? 9.914   -12.776 5.053   1.00 12.36 ? 108 SER A CA  1 
ATOM   844  C  C   . SER A  1 108 ? 8.948   -12.161 6.090   1.00 12.21 ? 108 SER A C   1 
ATOM   845  O  O   . SER A  1 108 ? 8.116   -12.834 6.702   1.00 11.58 ? 108 SER A O   1 
ATOM   846  C  CB  . SER A  1 108 ? 9.946   -14.308 5.159   1.00 13.42 ? 108 SER A CB  1 
ATOM   847  O  OG  . SER A  1 108 ? 10.775  -14.834 4.109   1.00 19.53 ? 108 SER A OG  1 
ATOM   848  N  N   . GLY A  1 109 ? 9.127   -10.864 6.405   1.00 10.11 ? 109 GLY A N   1 
ATOM   849  C  CA  . GLY A  1 109 ? 8.263   -10.118 7.289   1.00 11.58 ? 109 GLY A CA  1 
ATOM   850  C  C   . GLY A  1 109 ? 8.642   -10.191 8.774   1.00 13.04 ? 109 GLY A C   1 
ATOM   851  O  O   . GLY A  1 109 ? 8.033   -9.533  9.597   1.00 15.28 ? 109 GLY A O   1 
ATOM   852  N  N   . GLN A  1 110 ? 9.609   -11.046 9.124   1.00 11.51 ? 110 GLN A N   1 
ATOM   853  C  CA  . GLN A  1 110 ? 9.987   -11.264 10.492  1.00 12.20 ? 110 GLN A CA  1 
ATOM   854  C  C   . GLN A  1 110 ? 11.216  -10.515 11.027  1.00 10.06 ? 110 GLN A C   1 
ATOM   855  O  O   . GLN A  1 110 ? 12.241  -10.547 10.367  1.00 8.87  ? 110 GLN A O   1 
ATOM   856  C  CB  . GLN A  1 110 ? 10.300  -12.753 10.652  1.00 14.19 ? 110 GLN A CB  1 
ATOM   857  C  CG  . GLN A  1 110 ? 9.162   -13.725 10.129  1.00 14.34 ? 110 GLN A CG  1 
ATOM   858  C  CD  . GLN A  1 110 ? 7.757   -13.313 10.597  1.00 15.44 ? 110 GLN A CD  1 
ATOM   859  O  OE1 . GLN A  1 110 ? 7.507   -13.209 11.775  1.00 17.77 ? 110 GLN A OE1 1 
ATOM   860  N  NE2 . GLN A  1 110 ? 6.876   -12.960 9.648   1.00 18.24 ? 110 GLN A NE2 1 
ATOM   861  N  N   . HIS A  1 111 ? 11.080  -9.877  12.176  1.00 11.50 ? 111 HIS A N   1 
ATOM   862  C  CA  . HIS A  1 111 ? 12.180  -9.282  12.833  1.00 11.00 ? 111 HIS A CA  1 
ATOM   863  C  C   . HIS A  1 111 ? 12.975  -10.279 13.547  1.00 12.17 ? 111 HIS A C   1 
ATOM   864  O  O   . HIS A  1 111 ? 12.422  -11.234 14.131  1.00 15.89 ? 111 HIS A O   1 
ATOM   865  C  CB  . HIS A  1 111 ? 11.765  -8.312  13.897  1.00 13.24 ? 111 HIS A CB  1 
ATOM   866  C  CG  . HIS A  1 111 ? 11.380  -6.966  13.357  1.00 12.60 ? 111 HIS A CG  1 
ATOM   867  N  ND1 . HIS A  1 111 ? 10.163  -6.655  12.854  1.00 16.47 ? 111 HIS A ND1 1 
ATOM   868  C  CD2 . HIS A  1 111 ? 12.172  -5.821  13.200  1.00 11.85 ? 111 HIS A CD2 1 
ATOM   869  C  CE1 . HIS A  1 111 ? 10.135  -5.374  12.467  1.00 15.26 ? 111 HIS A CE1 1 
ATOM   870  N  NE2 . HIS A  1 111 ? 11.392  -4.853  12.695  1.00 17.18 ? 111 HIS A NE2 1 
ATOM   871  N  N   . PHE A  1 112 ? 14.282  -10.154 13.500  1.00 10.51 ? 112 PHE A N   1 
ATOM   872  C  CA  . PHE A  1 112 ? 15.155  -10.822 14.462  1.00 9.81  ? 112 PHE A CA  1 
ATOM   873  C  C   . PHE A  1 112 ? 15.226  -10.049 15.769  1.00 9.44  ? 112 PHE A C   1 
ATOM   874  O  O   . PHE A  1 112 ? 14.686  -8.898  15.864  1.00 9.95  ? 112 PHE A O   1 
ATOM   875  C  CB  . PHE A  1 112 ? 16.567  -11.091 13.874  1.00 9.35  ? 112 PHE A CB  1 
ATOM   876  C  CG  . PHE A  1 112 ? 16.568  -12.201 12.859  1.00 11.00 ? 112 PHE A CG  1 
ATOM   877  C  CD1 . PHE A  1 112 ? 15.961  -12.012 11.553  1.00 13.40 ? 112 PHE A CD1 1 
ATOM   878  C  CD2 . PHE A  1 112 ? 17.002  -13.471 13.226  1.00 13.27 ? 112 PHE A CD2 1 
ATOM   879  C  CE1 . PHE A  1 112 ? 15.927  -13.128 10.675  1.00 15.09 ? 112 PHE A CE1 1 
ATOM   880  C  CE2 . PHE A  1 112 ? 17.009  -14.523 12.320  1.00 13.30 ? 112 PHE A CE2 1 
ATOM   881  C  CZ  . PHE A  1 112 ? 16.440  -14.378 11.123  1.00 14.06 ? 112 PHE A CZ  1 
ATOM   882  N  N   . ALA A  1 113 ? 15.882  -10.604 16.807  1.00 9.13  ? 113 ALA A N   1 
ATOM   883  C  CA  . ALA A  1 113 ? 15.883  -9.943  18.131  1.00 9.14  ? 113 ALA A CA  1 
ATOM   884  C  C   . ALA A  1 113 ? 16.625  -8.634  18.084  1.00 8.94  ? 113 ALA A C   1 
ATOM   885  O  O   . ALA A  1 113 ? 16.281  -7.647  18.756  1.00 9.54  ? 113 ALA A O   1 
ATOM   886  C  CB  . ALA A  1 113 ? 16.561  -10.823 19.222  1.00 10.27 ? 113 ALA A CB  1 
ATOM   887  N  N   . ALA A  1 114 ? 17.762  -8.595  17.326  1.00 8.78  ? 114 ALA A N   1 
ATOM   888  C  CA  . ALA A  1 114 ? 18.580  -7.388  17.242  1.00 8.13  ? 114 ALA A CA  1 
ATOM   889  C  C   . ALA A  1 114 ? 19.416  -7.497  15.968  1.00 7.64  ? 114 ALA A C   1 
ATOM   890  O  O   . ALA A  1 114 ? 19.372  -8.496  15.213  1.00 8.96  ? 114 ALA A O   1 
ATOM   891  C  CB  . ALA A  1 114 ? 19.518  -7.379  18.498  1.00 9.91  ? 114 ALA A CB  1 
ATOM   892  N  N   . GLU A  1 115 ? 20.217  -6.449  15.752  1.00 7.73  ? 115 GLU A N   1 
ATOM   893  C  CA  . GLU A  1 115 ? 21.053  -6.434  14.513  1.00 8.84  ? 115 GLU A CA  1 
ATOM   894  C  C   . GLU A  1 115 ? 22.344  -5.627  14.817  1.00 8.15  ? 115 GLU A C   1 
ATOM   895  O  O   . GLU A  1 115 ? 22.321  -4.498  15.470  1.00 8.47  ? 115 GLU A O   1 
ATOM   896  C  CB  . GLU A  1 115 ? 20.256  -5.775  13.378  1.00 8.23  ? 115 GLU A CB  1 
ATOM   897  C  CG  . GLU A  1 115 ? 20.898  -5.839  11.978  1.00 7.53  ? 115 GLU A CG  1 
ATOM   898  C  CD  . GLU A  1 115 ? 19.952  -5.414  10.866  1.00 8.18  ? 115 GLU A CD  1 
ATOM   899  O  OE1 . GLU A  1 115 ? 18.759  -5.722  11.008  1.00 8.31  ? 115 GLU A OE1 1 
ATOM   900  O  OE2 . GLU A  1 115 ? 20.430  -4.951  9.829   1.00 7.49  ? 115 GLU A OE2 1 
ATOM   901  N  N   . LEU A  1 116 ? 23.491  -6.174  14.339  1.00 7.67  ? 116 LEU A N   1 
ATOM   902  C  CA  . LEU A  1 116 ? 24.803  -5.498  14.500  1.00 7.53  ? 116 LEU A CA  1 
ATOM   903  C  C   . LEU A  1 116 ? 25.156  -4.941  13.099  1.00 7.75  ? 116 LEU A C   1 
ATOM   904  O  O   . LEU A  1 116 ? 24.993  -5.648  12.078  1.00 7.22  ? 116 LEU A O   1 
ATOM   905  C  CB  . LEU A  1 116 ? 25.822  -6.566  14.960  1.00 9.27  ? 116 LEU A CB  1 
ATOM   906  C  CG  . LEU A  1 116 ? 27.327  -6.145  14.746  1.00 11.12 ? 116 LEU A CG  1 
ATOM   907  C  CD1 . LEU A  1 116 ? 27.598  -5.196  15.846  1.00 14.52 ? 116 LEU A CD1 1 
ATOM   908  C  CD2 . LEU A  1 116 ? 28.277  -7.368  14.739  1.00 12.90 ? 116 LEU A CD2 1 
ATOM   909  N  N   . HIS A  1 117 ? 25.654  -3.705  13.105  1.00 7.00  ? 117 HIS A N   1 
ATOM   910  C  CA  . HIS A  1 117 ? 26.207  -3.070  11.871  1.00 7.89  ? 117 HIS A CA  1 
ATOM   911  C  C   . HIS A  1 117 ? 27.633  -2.762  12.039  1.00 7.33  ? 117 HIS A C   1 
ATOM   912  O  O   . HIS A  1 117 ? 28.000  -2.127  13.030  1.00 8.29  ? 117 HIS A O   1 
ATOM   913  C  CB  . HIS A  1 117 ? 25.439  -1.785  11.608  1.00 7.99  ? 117 HIS A CB  1 
ATOM   914  C  CG  . HIS A  1 117 ? 24.014  -2.056  11.220  1.00 7.55  ? 117 HIS A CG  1 
ATOM   915  N  ND1 . HIS A  1 117 ? 23.002  -1.105  11.349  1.00 8.11  ? 117 HIS A ND1 1 
ATOM   916  C  CD2 . HIS A  1 117 ? 23.452  -3.145  10.669  1.00 8.07  ? 117 HIS A CD2 1 
ATOM   917  C  CE1 . HIS A  1 117 ? 21.857  -1.642  10.855  1.00 7.47  ? 117 HIS A CE1 1 
ATOM   918  N  NE2 . HIS A  1 117 ? 22.083  -2.878  10.499  1.00 6.95  ? 117 HIS A NE2 1 
ATOM   919  N  N   . ILE A  1 118 ? 28.444  -3.236  11.089  1.00 8.28  ? 118 ILE A N   1 
ATOM   920  C  CA  . ILE A  1 118 ? 29.884  -2.849  11.065  1.00 7.82  ? 118 ILE A CA  1 
ATOM   921  C  C   . ILE A  1 118 ? 30.019  -1.921  9.868   1.00 8.00  ? 118 ILE A C   1 
ATOM   922  O  O   . ILE A  1 118 ? 29.869  -2.299  8.692   1.00 7.76  ? 118 ILE A O   1 
ATOM   923  C  CB  . ILE A  1 118 ? 30.790  -4.073  10.907  1.00 8.57  ? 118 ILE A CB  1 
ATOM   924  C  CG1 . ILE A  1 118 ? 30.456  -5.129  11.929  1.00 9.07  ? 118 ILE A CG1 1 
ATOM   925  C  CG2 . ILE A  1 118 ? 32.277  -3.591  11.084  1.00 9.36  ? 118 ILE A CG2 1 
ATOM   926  C  CD1 . ILE A  1 118 ? 31.311  -6.377  11.796  1.00 11.43 ? 118 ILE A CD1 1 
ATOM   927  N  N   . VAL A  1 119 ? 30.207  -0.657  10.201  1.00 8.03  ? 119 VAL A N   1 
ATOM   928  C  CA  . VAL A  1 119 ? 30.163  0.440   9.177   1.00 9.02  ? 119 VAL A CA  1 
ATOM   929  C  C   . VAL A  1 119 ? 31.588  0.571   8.614   1.00 9.56  ? 119 VAL A C   1 
ATOM   930  O  O   . VAL A  1 119 ? 32.557  0.734   9.426   1.00 10.64 ? 119 VAL A O   1 
ATOM   931  C  CB  . VAL A  1 119 ? 29.701  1.764   9.823   1.00 9.70  ? 119 VAL A CB  1 
ATOM   932  C  CG1 . VAL A  1 119 ? 29.619  2.878   8.792   1.00 10.33 ? 119 VAL A CG1 1 
ATOM   933  C  CG2 . VAL A  1 119 ? 28.318  1.555   10.524  1.00 10.25 ? 119 VAL A CG2 1 
ATOM   934  N  N   . HIS A  1 120 ? 31.694  0.634   7.310   1.00 9.78  ? 120 HIS A N   1 
ATOM   935  C  CA  . HIS A  1 120 ? 33.000  0.925   6.603   1.00 8.83  ? 120 HIS A CA  1 
ATOM   936  C  C   . HIS A  1 120 ? 32.798  2.032   5.613   1.00 10.83 ? 120 HIS A C   1 
ATOM   937  O  O   . HIS A  1 120 ? 31.660  2.269   5.114   1.00 10.21 ? 120 HIS A O   1 
ATOM   938  C  CB  . HIS A  1 120 ? 33.438  -0.292  5.805   1.00 10.11 ? 120 HIS A CB  1 
ATOM   939  C  CG  . HIS A  1 120 ? 33.580  -1.579  6.603   1.00 9.86  ? 120 HIS A CG  1 
ATOM   940  N  ND1 . HIS A  1 120 ? 32.518  -2.287  7.216   1.00 9.09  ? 120 HIS A ND1 1 
ATOM   941  C  CD2 . HIS A  1 120 ? 34.737  -2.378  6.886   1.00 9.03  ? 120 HIS A CD2 1 
ATOM   942  C  CE1 . HIS A  1 120 ? 32.982  -3.414  7.814   1.00 10.14 ? 120 HIS A CE1 1 
ATOM   943  N  NE2 . HIS A  1 120 ? 34.338  -3.533  7.562   1.00 10.17 ? 120 HIS A NE2 1 
ATOM   944  N  N   . TYR A  1 121 ? 33.899  2.708   5.237   1.00 10.93 ? 121 TYR A N   1 
ATOM   945  C  CA  . TYR A  1 121 ? 33.828  3.736   4.202   1.00 10.90 ? 121 TYR A CA  1 
ATOM   946  C  C   . TYR A  1 121 ? 34.819  3.527   3.076   1.00 11.97 ? 121 TYR A C   1 
ATOM   947  O  O   . TYR A  1 121 ? 35.853  2.822   3.345   1.00 11.90 ? 121 TYR A O   1 
ATOM   948  C  CB  . TYR A  1 121 ? 34.047  5.110   4.820   1.00 12.11 ? 121 TYR A CB  1 
ATOM   949  C  CG  . TYR A  1 121 ? 35.479  5.301   5.372   1.00 12.86 ? 121 TYR A CG  1 
ATOM   950  C  CD1 . TYR A  1 121 ? 35.875  4.802   6.632   1.00 12.70 ? 121 TYR A CD1 1 
ATOM   951  C  CD2 . TYR A  1 121 ? 36.433  6.001   4.612   1.00 12.97 ? 121 TYR A CD2 1 
ATOM   952  C  CE1 . TYR A  1 121 ? 37.177  4.964   7.099   1.00 13.69 ? 121 TYR A CE1 1 
ATOM   953  C  CE2 . TYR A  1 121 ? 37.786  6.064   5.043   1.00 14.84 ? 121 TYR A CE2 1 
ATOM   954  C  CZ  . TYR A  1 121 ? 38.092  5.592   6.294   1.00 15.69 ? 121 TYR A CZ  1 
ATOM   955  O  OH  . TYR A  1 121 ? 39.416  5.733   6.807   1.00 19.22 ? 121 TYR A OH  1 
ATOM   956  N  N   . ASN A  1 122 ? 34.582  4.144   1.907   1.00 11.10 ? 122 ASN A N   1 
ATOM   957  C  CA  . ASN A  1 122 ? 35.466  3.870   0.742   1.00 11.87 ? 122 ASN A CA  1 
ATOM   958  C  C   . ASN A  1 122 ? 36.732  4.739   0.969   1.00 12.62 ? 122 ASN A C   1 
ATOM   959  O  O   . ASN A  1 122 ? 36.760  5.930   0.725   1.00 12.07 ? 122 ASN A O   1 
ATOM   960  C  CB  . ASN A  1 122 ? 34.731  4.285   -0.525  1.00 11.01 ? 122 ASN A CB  1 
ATOM   961  C  CG  . ASN A  1 122 ? 35.485  3.935   -1.770  1.00 11.82 ? 122 ASN A CG  1 
ATOM   962  O  OD1 . ASN A  1 122 ? 36.768  3.859   -1.743  1.00 11.27 ? 122 ASN A OD1 1 
ATOM   963  N  ND2 . ASN A  1 122 ? 34.753  3.516   -2.835  1.00 13.80 ? 122 ASN A ND2 1 
ATOM   964  N  N   . SER A  1 123 ? 37.793  4.084   1.467   1.00 11.96 ? 123 SER A N   1 
ATOM   965  C  CA  . SER A  1 123 ? 38.991  4.796   1.836   1.00 12.38 ? 123 SER A CA  1 
ATOM   966  C  C   . SER A  1 123 ? 39.877  4.958   0.561   1.00 12.49 ? 123 SER A C   1 
ATOM   967  O  O   . SER A  1 123 ? 40.874  5.693   0.625   1.00 15.50 ? 123 SER A O   1 
ATOM   968  C  CB  . SER A  1 123 ? 39.701  3.896   2.912   1.00 10.93 ? 123 SER A CB  1 
ATOM   969  O  OG  . SER A  1 123 ? 39.800  2.570   2.560   1.00 13.50 ? 123 SER A OG  1 
ATOM   970  N  N   . ASP A  1 124 ? 39.573  4.281   -0.515  1.00 12.62 ? 124 ASP A N   1 
ATOM   971  C  CA  . ASP A  1 124 ? 40.326  4.461   -1.811  1.00 12.75 ? 124 ASP A CA  1 
ATOM   972  C  C   . ASP A  1 124 ? 39.908  5.807   -2.369  1.00 15.59 ? 124 ASP A C   1 
ATOM   973  O  O   . ASP A  1 124 ? 40.733  6.551   -2.961  1.00 17.18 ? 124 ASP A O   1 
ATOM   974  C  CB  . ASP A  1 124 ? 40.007  3.406   -2.812  1.00 13.94 ? 124 ASP A CB  1 
ATOM   975  C  CG  . ASP A  1 124 ? 40.584  2.118   -2.520  1.00 13.38 ? 124 ASP A CG  1 
ATOM   976  O  OD1 . ASP A  1 124 ? 41.637  2.083   -1.810  1.00 14.67 ? 124 ASP A OD1 1 
ATOM   977  O  OD2 . ASP A  1 124 ? 40.213  1.109   -3.086  1.00 14.26 ? 124 ASP A OD2 1 
ATOM   978  N  N   . LEU A  1 125 ? 38.660  6.208   -2.158  1.00 13.90 ? 125 LEU A N   1 
ATOM   979  C  CA  . LEU A  1 125 ? 38.164  7.469   -2.662  1.00 18.25 ? 125 LEU A CA  1 
ATOM   980  C  C   . LEU A  1 125 ? 38.126  8.617   -1.664  1.00 16.73 ? 125 LEU A C   1 
ATOM   981  O  O   . LEU A  1 125 ? 38.180  9.755   -2.085  1.00 20.84 ? 125 LEU A O   1 
ATOM   982  C  CB  . LEU A  1 125 ? 36.777  7.309   -3.283  1.00 18.64 ? 125 LEU A CB  1 
ATOM   983  C  CG  . LEU A  1 125 ? 36.708  6.293   -4.394  1.00 24.33 ? 125 LEU A CG  1 
ATOM   984  C  CD1 . LEU A  1 125 ? 35.332  6.325   -5.004  1.00 25.46 ? 125 LEU A CD1 1 
ATOM   985  C  CD2 . LEU A  1 125 ? 37.788  6.499   -5.446  1.00 21.77 ? 125 LEU A CD2 1 
ATOM   986  N  N   . TYR A  1 126 ? 37.970  8.320   -0.374  1.00 16.74 ? 126 TYR A N   1 
ATOM   987  C  CA  . TYR A  1 126 ? 37.670  9.384   0.633   1.00 15.73 ? 126 TYR A CA  1 
ATOM   988  C  C   . TYR A  1 126 ? 38.495  9.222   1.913   1.00 18.88 ? 126 TYR A C   1 
ATOM   989  O  O   . TYR A  1 126 ? 38.924  8.125   2.234   1.00 17.98 ? 126 TYR A O   1 
ATOM   990  C  CB  . TYR A  1 126 ? 36.102  9.367   1.031   1.00 16.71 ? 126 TYR A CB  1 
ATOM   991  C  CG  . TYR A  1 126 ? 35.223  9.423   -0.175  1.00 16.21 ? 126 TYR A CG  1 
ATOM   992  C  CD1 . TYR A  1 126 ? 35.198  10.508  -1.036  1.00 20.28 ? 126 TYR A CD1 1 
ATOM   993  C  CD2 . TYR A  1 126 ? 34.409  8.314   -0.474  1.00 17.35 ? 126 TYR A CD2 1 
ATOM   994  C  CE1 . TYR A  1 126 ? 34.407  10.442  -2.159  1.00 17.72 ? 126 TYR A CE1 1 
ATOM   995  C  CE2 . TYR A  1 126 ? 33.632  8.226   -1.627  1.00 18.13 ? 126 TYR A CE2 1 
ATOM   996  C  CZ  . TYR A  1 126 ? 33.624  9.310   -2.453  1.00 20.11 ? 126 TYR A CZ  1 
ATOM   997  O  OH  . TYR A  1 126 ? 32.816  9.239   -3.591  1.00 21.89 ? 126 TYR A OH  1 
ATOM   998  N  N   . PRO A  1 127 ? 38.765  10.343  2.632   1.00 19.60 ? 127 PRO A N   1 
ATOM   999  C  CA  . PRO A  1 127 ? 39.704  10.308  3.787   1.00 20.44 ? 127 PRO A CA  1 
ATOM   1000 C  C   . PRO A  1 127 ? 39.173  9.756   5.086   1.00 21.49 ? 127 PRO A C   1 
ATOM   1001 O  O   . PRO A  1 127 ? 39.949  9.282   5.960   1.00 25.30 ? 127 PRO A O   1 
ATOM   1002 C  CB  . PRO A  1 127 ? 40.112  11.798  3.972   1.00 25.09 ? 127 PRO A CB  1 
ATOM   1003 C  CG  . PRO A  1 127 ? 38.929  12.533  3.386   1.00 21.85 ? 127 PRO A CG  1 
ATOM   1004 C  CD  . PRO A  1 127 ? 38.529  11.735  2.190   1.00 21.19 ? 127 PRO A CD  1 
ATOM   1005 N  N   . ASP A  1 128 ? 37.849  9.765   5.239   1.00 19.84 ? 128 ASP A N   1 
ATOM   1006 C  CA  . ASP A  1 128 ? 37.247  9.365   6.516   1.00 21.46 ? 128 ASP A CA  1 
ATOM   1007 C  C   . ASP A  1 128 ? 35.763  9.119   6.287   1.00 17.89 ? 128 ASP A C   1 
ATOM   1008 O  O   . ASP A  1 128 ? 35.275  9.434   5.195   1.00 17.93 ? 128 ASP A O   1 
ATOM   1009 C  CB  . ASP A  1 128 ? 37.485  10.415  7.660   1.00 23.09 ? 128 ASP A CB  1 
ATOM   1010 C  CG  . ASP A  1 128 ? 37.083  11.838  7.268   1.00 29.40 ? 128 ASP A CG  1 
ATOM   1011 O  OD1 . ASP A  1 128 ? 37.919  12.780  7.478   1.00 33.34 ? 128 ASP A OD1 1 
ATOM   1012 O  OD2 . ASP A  1 128 ? 35.934  12.038  6.770   1.00 25.56 ? 128 ASP A OD2 1 
ATOM   1013 N  N   . ALA A  1 129 ? 35.089  8.504   7.254   1.00 21.28 ? 129 ALA A N   1 
ATOM   1014 C  CA  . ALA A  1 129 ? 33.704  8.139   7.036   1.00 18.96 ? 129 ALA A CA  1 
ATOM   1015 C  C   . ALA A  1 129 ? 32.741  9.308   6.906   1.00 19.39 ? 129 ALA A C   1 
ATOM   1016 O  O   . ALA A  1 129 ? 31.759  9.213   6.181   1.00 18.69 ? 129 ALA A O   1 
ATOM   1017 C  CB  . ALA A  1 129 ? 33.146  7.173   8.094   1.00 22.13 ? 129 ALA A CB  1 
ATOM   1018 N  N   A SER A  1 130 ? 32.976  10.368  7.669   0.50 20.41 ? 130 SER A N   1 
ATOM   1019 N  N   B SER A  1 130 ? 32.977  10.364  7.666   0.50 20.16 ? 130 SER A N   1 
ATOM   1020 C  CA  A SER A  1 130 ? 32.091  11.517  7.622   0.50 19.93 ? 130 SER A CA  1 
ATOM   1021 C  CA  B SER A  1 130 ? 32.053  11.463  7.616   0.50 19.52 ? 130 SER A CA  1 
ATOM   1022 C  C   A SER A  1 130 ? 32.129  12.107  6.221   0.50 18.98 ? 130 SER A C   1 
ATOM   1023 C  C   B SER A  1 130 ? 32.127  12.121  6.236   0.50 18.82 ? 130 SER A C   1 
ATOM   1024 O  O   A SER A  1 130 ? 31.096  12.431  5.652   0.50 19.98 ? 130 SER A O   1 
ATOM   1025 O  O   B SER A  1 130 ? 31.102  12.495  5.689   0.50 19.94 ? 130 SER A O   1 
ATOM   1026 C  CB  A SER A  1 130 ? 32.481  12.546  8.702   0.50 22.00 ? 130 SER A CB  1 
ATOM   1027 C  CB  B SER A  1 130 ? 32.271  12.433  8.795   0.50 21.25 ? 130 SER A CB  1 
ATOM   1028 O  OG  A SER A  1 130 ? 31.966  13.849  8.444   0.50 21.63 ? 130 SER A OG  1 
ATOM   1029 O  OG  B SER A  1 130 ? 33.632  12.844  8.914   0.50 20.91 ? 130 SER A OG  1 
ATOM   1030 N  N   . THR A  1 131 ? 33.309  12.226  5.633   1.00 17.83 ? 131 THR A N   1 
ATOM   1031 C  CA  . THR A  1 131 ? 33.391  12.759  4.325   1.00 18.83 ? 131 THR A CA  1 
ATOM   1032 C  C   . THR A  1 131 ? 32.704  11.824  3.295   1.00 17.86 ? 131 THR A C   1 
ATOM   1033 O  O   . THR A  1 131 ? 32.048  12.273  2.355   1.00 16.78 ? 131 THR A O   1 
ATOM   1034 C  CB  . THR A  1 131 ? 34.849  13.036  3.919   1.00 19.39 ? 131 THR A CB  1 
ATOM   1035 O  OG1 . THR A  1 131 ? 35.395  13.938  4.897   1.00 22.71 ? 131 THR A OG1 1 
ATOM   1036 C  CG2 . THR A  1 131 ? 34.976  13.608  2.488   1.00 20.55 ? 131 THR A CG2 1 
ATOM   1037 N  N   . ALA A  1 132 ? 32.909  10.513  3.445   1.00 17.87 ? 132 ALA A N   1 
ATOM   1038 C  CA  . ALA A  1 132 ? 32.383  9.560   2.490   1.00 15.47 ? 132 ALA A CA  1 
ATOM   1039 C  C   . ALA A  1 132 ? 30.814  9.449   2.534   1.00 13.80 ? 132 ALA A C   1 
ATOM   1040 O  O   . ALA A  1 132 ? 30.235  9.055   1.517   1.00 14.36 ? 132 ALA A O   1 
ATOM   1041 C  CB  . ALA A  1 132 ? 32.929  8.157   2.823   1.00 13.94 ? 132 ALA A CB  1 
ATOM   1042 N  N   . SER A  1 133 ? 30.239  9.837   3.651   1.00 15.64 ? 133 SER A N   1 
ATOM   1043 C  CA  . SER A  1 133 ? 28.861  9.440   3.972   1.00 16.16 ? 133 SER A CA  1 
ATOM   1044 C  C   . SER A  1 133 ? 27.820  10.011  3.022   1.00 17.52 ? 133 SER A C   1 
ATOM   1045 O  O   . SER A  1 133 ? 26.758  9.393   2.821   1.00 15.82 ? 133 SER A O   1 
ATOM   1046 C  CB  . SER A  1 133 ? 28.545  9.819   5.407   1.00 17.79 ? 133 SER A CB  1 
ATOM   1047 O  OG  . SER A  1 133 ? 28.444  11.227  5.529   1.00 19.18 ? 133 SER A OG  1 
ATOM   1048 N  N   . ASN A  1 134 ? 28.082  11.177  2.423   1.00 15.89 ? 134 ASN A N   1 
ATOM   1049 C  CA  . ASN A  1 134 ? 27.206  11.769  1.379   1.00 16.73 ? 134 ASN A CA  1 
ATOM   1050 C  C   . ASN A  1 134 ? 27.721  11.719  -0.039  1.00 17.12 ? 134 ASN A C   1 
ATOM   1051 O  O   . ASN A  1 134 ? 27.233  12.389  -0.975  1.00 20.63 ? 134 ASN A O   1 
ATOM   1052 C  CB  . ASN A  1 134 ? 26.776  13.180  1.787   1.00 18.99 ? 134 ASN A CB  1 
ATOM   1053 C  CG  . ASN A  1 134 ? 27.951  14.148  1.664   1.00 26.01 ? 134 ASN A CG  1 
ATOM   1054 O  OD1 . ASN A  1 134 ? 29.116  13.701  1.648   1.00 21.61 ? 134 ASN A OD1 1 
ATOM   1055 N  ND2 . ASN A  1 134 ? 27.670  15.437  1.577   1.00 23.15 ? 134 ASN A ND2 1 
ATOM   1056 N  N   . LYS A  1 135 ? 28.628  10.798  -0.269  1.00 13.85 ? 135 LYS A N   1 
ATOM   1057 C  CA  . LYS A  1 135 ? 29.205  10.609  -1.580  1.00 15.85 ? 135 LYS A CA  1 
ATOM   1058 C  C   . LYS A  1 135 ? 28.962  9.312   -2.215  1.00 17.40 ? 135 LYS A C   1 
ATOM   1059 O  O   . LYS A  1 135 ? 28.676  8.298   -1.574  1.00 15.32 ? 135 LYS A O   1 
ATOM   1060 C  CB  . LYS A  1 135 ? 30.749  10.972  -1.506  1.00 18.58 ? 135 LYS A CB  1 
ATOM   1061 C  CG  . LYS A  1 135 ? 30.927  12.500  -1.316  1.00 20.87 ? 135 LYS A CG  1 
ATOM   1062 C  CD  . LYS A  1 135 ? 32.326  12.905  -0.886  1.00 24.11 ? 135 LYS A CD  1 
ATOM   1063 C  CE  . LYS A  1 135 ? 32.397  14.344  -0.481  1.00 22.63 ? 135 LYS A CE  1 
ATOM   1064 N  NZ  . LYS A  1 135 ? 31.725  14.589  0.827   1.00 21.77 ? 135 LYS A NZ  1 
ATOM   1065 N  N   . SER A  1 136 ? 29.045  9.329   -3.523  1.00 19.96 ? 136 SER A N   1 
ATOM   1066 C  CA  . SER A  1 136 ? 28.851  8.185   -4.340  1.00 20.18 ? 136 SER A CA  1 
ATOM   1067 C  C   . SER A  1 136 ? 29.790  7.011   -3.907  1.00 17.49 ? 136 SER A C   1 
ATOM   1068 O  O   . SER A  1 136 ? 30.988  7.151   -3.703  1.00 18.46 ? 136 SER A O   1 
ATOM   1069 C  CB  . SER A  1 136 ? 29.249  8.537   -5.768  1.00 25.04 ? 136 SER A CB  1 
ATOM   1070 O  OG  . SER A  1 136 ? 28.953  7.439   -6.595  1.00 36.64 ? 136 SER A OG  1 
ATOM   1071 N  N   . GLU A  1 137 ? 29.187  5.844   -3.779  1.00 21.25 ? 137 GLU A N   1 
ATOM   1072 C  CA  . GLU A  1 137 ? 29.962  4.667   -3.349  1.00 19.67 ? 137 GLU A CA  1 
ATOM   1073 C  C   . GLU A  1 137 ? 30.609  4.852   -1.981  1.00 16.28 ? 137 GLU A C   1 
ATOM   1074 O  O   . GLU A  1 137 ? 31.678  4.292   -1.705  1.00 17.40 ? 137 GLU A O   1 
ATOM   1075 C  CB  . GLU A  1 137 ? 31.025  4.249   -4.353  1.00 23.83 ? 137 GLU A CB  1 
ATOM   1076 C  CG  . GLU A  1 137 ? 30.375  3.770   -5.663  1.00 31.26 ? 137 GLU A CG  1 
ATOM   1077 C  CD  . GLU A  1 137 ? 31.350  2.989   -6.517  1.00 43.68 ? 137 GLU A CD  1 
ATOM   1078 O  OE1 . GLU A  1 137 ? 32.508  3.471   -6.697  1.00 49.43 ? 137 GLU A OE1 1 
ATOM   1079 O  OE2 . GLU A  1 137 ? 30.950  1.885   -6.982  1.00 57.64 ? 137 GLU A OE2 1 
ATOM   1080 N  N   . GLY A  1 138 ? 30.018  5.667   -1.117  1.00 12.40 ? 138 GLY A N   1 
ATOM   1081 C  CA  . GLY A  1 138 ? 30.715  6.094   0.022   1.00 12.14 ? 138 GLY A CA  1 
ATOM   1082 C  C   . GLY A  1 138 ? 30.877  5.052   1.095   1.00 11.65 ? 138 GLY A C   1 
ATOM   1083 O  O   . GLY A  1 138 ? 31.924  5.064   1.775   1.00 11.51 ? 138 GLY A O   1 
ATOM   1084 N  N   . LEU A  1 139 ? 29.820  4.260   1.409   1.00 10.03 ? 139 LEU A N   1 
ATOM   1085 C  CA  . LEU A  1 139 ? 29.816  3.444   2.649   1.00 10.85 ? 139 LEU A CA  1 
ATOM   1086 C  C   . LEU A  1 139 ? 29.463  2.035   2.264   1.00 9.57  ? 139 LEU A C   1 
ATOM   1087 O  O   . LEU A  1 139 ? 28.776  1.751   1.257   1.00 9.60  ? 139 LEU A O   1 
ATOM   1088 C  CB  . LEU A  1 139 ? 28.755  3.944   3.673   1.00 10.85 ? 139 LEU A CB  1 
ATOM   1089 C  CG  . LEU A  1 139 ? 28.951  5.409   4.105   1.00 11.20 ? 139 LEU A CG  1 
ATOM   1090 C  CD1 . LEU A  1 139 ? 27.678  5.815   4.904   1.00 13.00 ? 139 LEU A CD1 1 
ATOM   1091 C  CD2 . LEU A  1 139 ? 30.236  5.484   5.007   1.00 13.60 ? 139 LEU A CD2 1 
ATOM   1092 N  N   . ALA A  1 140 ? 29.887  1.108   3.115   1.00 9.09  ? 140 ALA A N   1 
ATOM   1093 C  CA  . ALA A  1 140 ? 29.514  -0.296  3.019   1.00 8.60  ? 140 ALA A CA  1 
ATOM   1094 C  C   . ALA A  1 140 ? 29.293  -0.782  4.440   1.00 8.10  ? 140 ALA A C   1 
ATOM   1095 O  O   . ALA A  1 140 ? 30.135  -0.598  5.332   1.00 10.47 ? 140 ALA A O   1 
ATOM   1096 C  CB  . ALA A  1 140 ? 30.586  -1.118  2.320   1.00 9.22  ? 140 ALA A CB  1 
ATOM   1097 N  N   . VAL A  1 141 ? 28.144  -1.420  4.659   1.00 8.50  ? 141 VAL A N   1 
ATOM   1098 C  CA  . VAL A  1 141 ? 27.844  -1.975  6.001   1.00 8.72  ? 141 VAL A CA  1 
ATOM   1099 C  C   . VAL A  1 141 ? 27.678  -3.452  5.967   1.00 7.65  ? 141 VAL A C   1 
ATOM   1100 O  O   . VAL A  1 141 ? 27.105  -4.010  5.009   1.00 8.91  ? 141 VAL A O   1 
ATOM   1101 C  CB  . VAL A  1 141 ? 26.549  -1.354  6.547   1.00 9.34  ? 141 VAL A CB  1 
ATOM   1102 C  CG1 . VAL A  1 141 ? 26.205  -1.897  7.960   1.00 9.96  ? 141 VAL A CG1 1 
ATOM   1103 C  CG2 . VAL A  1 141 ? 26.721  0.148   6.632   1.00 9.47  ? 141 VAL A CG2 1 
ATOM   1104 N  N   . LEU A  1 142 ? 28.252  -4.133  6.960   1.00 8.08  ? 142 LEU A N   1 
ATOM   1105 C  CA  . LEU A  1 142 ? 27.977  -5.552  7.174   1.00 7.33  ? 142 LEU A CA  1 
ATOM   1106 C  C   . LEU A  1 142 ? 26.932  -5.604  8.280   1.00 8.46  ? 142 LEU A C   1 
ATOM   1107 O  O   . LEU A  1 142 ? 27.132  -5.041  9.333   1.00 9.21  ? 142 LEU A O   1 
ATOM   1108 C  CB  . LEU A  1 142 ? 29.235  -6.319  7.639   1.00 8.03  ? 142 LEU A CB  1 
ATOM   1109 C  CG  . LEU A  1 142 ? 30.446  -6.109  6.690   1.00 9.26  ? 142 LEU A CG  1 
ATOM   1110 C  CD1 . LEU A  1 142 ? 31.566  -6.944  7.363   1.00 10.34 ? 142 LEU A CD1 1 
ATOM   1111 C  CD2 . LEU A  1 142 ? 30.138  -6.660  5.310   1.00 9.57  ? 142 LEU A CD2 1 
ATOM   1112 N  N   . ALA A  1 143 ? 25.855  -6.360  7.980   1.00 7.12  ? 143 ALA A N   1 
ATOM   1113 C  CA  . ALA A  1 143 ? 24.759  -6.476  8.987   1.00 7.40  ? 143 ALA A CA  1 
ATOM   1114 C  C   . ALA A  1 143 ? 24.644  -7.970  9.417   1.00 7.71  ? 143 ALA A C   1 
ATOM   1115 O  O   . ALA A  1 143 ? 24.590  -8.870  8.550   1.00 8.48  ? 143 ALA A O   1 
ATOM   1116 C  CB  . ALA A  1 143 ? 23.459  -5.991  8.352   1.00 8.87  ? 143 ALA A CB  1 
ATOM   1117 N  N   . VAL A  1 144 ? 24.642  -8.113  10.784  1.00 8.00  ? 144 VAL A N   1 
ATOM   1118 C  CA  . VAL A  1 144 ? 24.471  -9.466  11.310  1.00 8.80  ? 144 VAL A CA  1 
ATOM   1119 C  C   . VAL A  1 144 ? 23.154  -9.465  12.085  1.00 8.38  ? 144 VAL A C   1 
ATOM   1120 O  O   . VAL A  1 144 ? 22.936  -8.651  12.989  1.00 9.50  ? 144 VAL A O   1 
ATOM   1121 C  CB  . VAL A  1 144 ? 25.620  -9.777  12.308  1.00 10.21 ? 144 VAL A CB  1 
ATOM   1122 C  CG1 . VAL A  1 144 ? 25.430  -11.234 12.876  1.00 11.92 ? 144 VAL A CG1 1 
ATOM   1123 C  CG2 . VAL A  1 144 ? 26.990  -9.677  11.551  1.00 10.78 ? 144 VAL A CG2 1 
ATOM   1124 N  N   . LEU A  1 145 ? 22.313  -10.426 11.715  1.00 9.67  ? 145 LEU A N   1 
ATOM   1125 C  CA  . LEU A  1 145 ? 21.061  -10.622 12.422  1.00 9.19  ? 145 LEU A CA  1 
ATOM   1126 C  C   . LEU A  1 145 ? 21.312  -11.437 13.680  1.00 8.38  ? 145 LEU A C   1 
ATOM   1127 O  O   . LEU A  1 145 ? 22.089  -12.408 13.626  1.00 9.93  ? 145 LEU A O   1 
ATOM   1128 C  CB  . LEU A  1 145 ? 20.050  -11.329 11.469  1.00 9.41  ? 145 LEU A CB  1 
ATOM   1129 C  CG  . LEU A  1 145 ? 19.712  -10.611 10.140  1.00 10.65 ? 145 LEU A CG  1 
ATOM   1130 C  CD1 . LEU A  1 145 ? 19.076  -11.568 9.115   1.00 11.46 ? 145 LEU A CD1 1 
ATOM   1131 C  CD2 . LEU A  1 145 ? 18.850  -9.353  10.480  1.00 11.36 ? 145 LEU A CD2 1 
ATOM   1132 N  N   . ILE A  1 146 ? 20.652  -11.067 14.776  1.00 8.56  ? 146 ILE A N   1 
ATOM   1133 C  CA  . ILE A  1 146 ? 20.892  -11.715 16.065  1.00 9.30  ? 146 ILE A CA  1 
ATOM   1134 C  C   . ILE A  1 146 ? 19.615  -12.337 16.628  1.00 10.07 ? 146 ILE A C   1 
ATOM   1135 O  O   . ILE A  1 146 ? 18.593  -11.670 16.638  1.00 10.33 ? 146 ILE A O   1 
ATOM   1136 C  CB  . ILE A  1 146 ? 21.381  -10.630 17.056  1.00 9.59  ? 146 ILE A CB  1 
ATOM   1137 C  CG1 . ILE A  1 146 ? 22.738  -10.028 16.598  1.00 10.06 ? 146 ILE A CG1 1 
ATOM   1138 C  CG2 . ILE A  1 146 ? 21.716  -11.234 18.445  1.00 10.87 ? 146 ILE A CG2 1 
ATOM   1139 C  CD1 . ILE A  1 146 ? 23.096  -8.776  17.397  1.00 10.66 ? 146 ILE A CD1 1 
ATOM   1140 N  N   . GLU A  1 147 ? 19.698  -13.566 17.055  1.00 11.28 ? 147 GLU A N   1 
ATOM   1141 C  CA  . GLU A  1 147 ? 18.526  -14.244 17.684  1.00 10.97 ? 147 GLU A CA  1 
ATOM   1142 C  C   . GLU A  1 147 ? 18.940  -14.771 19.009  1.00 11.68 ? 147 GLU A C   1 
ATOM   1143 O  O   . GLU A  1 147 ? 20.104  -14.861 19.344  1.00 12.33 ? 147 GLU A O   1 
ATOM   1144 C  CB  . GLU A  1 147 ? 17.984  -15.371 16.812  1.00 13.65 ? 147 GLU A CB  1 
ATOM   1145 C  CG  . GLU A  1 147 ? 18.902  -16.549 16.618  1.00 13.96 ? 147 GLU A CG  1 
ATOM   1146 C  CD  . GLU A  1 147 ? 18.479  -17.544 15.572  1.00 16.41 ? 147 GLU A CD  1 
ATOM   1147 O  OE1 . GLU A  1 147 ? 17.500  -17.335 14.801  1.00 17.38 ? 147 GLU A OE1 1 
ATOM   1148 O  OE2 . GLU A  1 147 ? 19.195  -18.562 15.365  1.00 19.51 ? 147 GLU A OE2 1 
ATOM   1149 N  N   . MET A  1 148 ? 17.960  -15.130 19.820  1.00 14.51 ? 148 MET A N   1 
ATOM   1150 C  CA  . MET A  1 148 ? 18.242  -15.598 21.156  1.00 18.12 ? 148 MET A CA  1 
ATOM   1151 C  C   . MET A  1 148 ? 18.598  -17.104 21.033  1.00 16.01 ? 148 MET A C   1 
ATOM   1152 O  O   . MET A  1 148 ? 17.955  -17.823 20.270  1.00 20.49 ? 148 MET A O   1 
ATOM   1153 C  CB  . MET A  1 148 ? 16.868  -15.608 21.806  1.00 21.37 ? 148 MET A CB  1 
ATOM   1154 C  CG  . MET A  1 148 ? 16.826  -14.552 22.739  1.00 24.75 ? 148 MET A CG  1 
ATOM   1155 S  SD  . MET A  1 148 ? 17.756  -15.341 24.062  1.00 40.05 ? 148 MET A SD  1 
ATOM   1156 C  CE  . MET A  1 148 ? 17.093  -16.974 23.937  1.00 12.18 ? 148 MET A CE  1 
ATOM   1157 N  N   . GLY A  1 149 ? 19.591  -17.585 21.767  1.00 15.77 ? 149 GLY A N   1 
ATOM   1158 C  CA  . GLY A  1 149 ? 19.969  -18.978 21.832  1.00 16.88 ? 149 GLY A CA  1 
ATOM   1159 C  C   . GLY A  1 149 ? 21.069  -19.131 22.886  1.00 16.25 ? 149 GLY A C   1 
ATOM   1160 O  O   . GLY A  1 149 ? 20.954  -18.667 24.021  1.00 16.46 ? 149 GLY A O   1 
ATOM   1161 N  N   A SER A  1 150 ? 22.176  -19.691 22.424  0.50 15.24 ? 150 SER A N   1 
ATOM   1162 N  N   B SER A  1 150 ? 22.140  -19.811 22.507  0.50 15.61 ? 150 SER A N   1 
ATOM   1163 C  CA  A SER A  1 150 ? 23.341  -19.860 23.267  0.50 15.72 ? 150 SER A CA  1 
ATOM   1164 C  CA  B SER A  1 150 ? 23.197  -20.071 23.481  0.50 15.98 ? 150 SER A CA  1 
ATOM   1165 C  C   A SER A  1 150 ? 24.048  -18.594 23.741  0.50 16.24 ? 150 SER A C   1 
ATOM   1166 C  C   B SER A  1 150 ? 24.046  -18.830 23.700  0.50 16.01 ? 150 SER A C   1 
ATOM   1167 O  O   A SER A  1 150 ? 24.158  -17.573 23.066  0.50 13.40 ? 150 SER A O   1 
ATOM   1168 O  O   B SER A  1 150 ? 24.207  -18.050 22.730  0.50 13.59 ? 150 SER A O   1 
ATOM   1169 C  CB  A SER A  1 150 ? 24.359  -20.798 22.579  0.50 18.58 ? 150 SER A CB  1 
ATOM   1170 C  CB  B SER A  1 150 ? 24.114  -21.165 22.944  0.50 19.32 ? 150 SER A CB  1 
ATOM   1171 O  OG  A SER A  1 150 ? 23.721  -22.035 22.294  0.50 22.22 ? 150 SER A OG  1 
ATOM   1172 O  OG  B SER A  1 150 ? 24.567  -20.775 21.645  0.50 19.35 ? 150 SER A OG  1 
ATOM   1173 N  N   . PHE A  1 151 ? 24.577  -18.657 24.934  1.00 14.68 ? 151 PHE A N   1 
ATOM   1174 C  CA  . PHE A  1 151 ? 25.541  -17.635 25.333  1.00 15.03 ? 151 PHE A CA  1 
ATOM   1175 C  C   . PHE A  1 151 ? 26.658  -17.452 24.274  1.00 15.64 ? 151 PHE A C   1 
ATOM   1176 O  O   . PHE A  1 151 ? 27.261  -18.472 23.775  1.00 17.11 ? 151 PHE A O   1 
ATOM   1177 C  CB  . PHE A  1 151 ? 26.154  -17.981 26.710  1.00 15.07 ? 151 PHE A CB  1 
ATOM   1178 C  CG  . PHE A  1 151 ? 27.093  -16.997 27.173  1.00 15.19 ? 151 PHE A CG  1 
ATOM   1179 C  CD1 . PHE A  1 151 ? 26.625  -15.752 27.679  1.00 15.24 ? 151 PHE A CD1 1 
ATOM   1180 C  CD2 . PHE A  1 151 ? 28.504  -17.227 27.098  1.00 16.07 ? 151 PHE A CD2 1 
ATOM   1181 C  CE1 . PHE A  1 151 ? 27.531  -14.780 28.062  1.00 16.87 ? 151 PHE A CE1 1 
ATOM   1182 C  CE2 . PHE A  1 151 ? 29.355  -16.234 27.522  1.00 16.03 ? 151 PHE A CE2 1 
ATOM   1183 C  CZ  . PHE A  1 151 ? 28.902  -15.043 28.041  1.00 17.42 ? 151 PHE A CZ  1 
ATOM   1184 N  N   . ASN A  1 152 ? 27.010  -16.212 23.974  1.00 14.06 ? 152 ASN A N   1 
ATOM   1185 C  CA  . ASN A  1 152 ? 28.019  -15.947 22.984  1.00 13.84 ? 152 ASN A CA  1 
ATOM   1186 C  C   . ASN A  1 152 ? 29.172  -15.180 23.637  1.00 14.43 ? 152 ASN A C   1 
ATOM   1187 O  O   . ASN A  1 152 ? 29.118  -13.993 23.948  1.00 14.84 ? 152 ASN A O   1 
ATOM   1188 C  CB  . ASN A  1 152 ? 27.343  -15.135 21.839  1.00 13.53 ? 152 ASN A CB  1 
ATOM   1189 C  CG  . ASN A  1 152 ? 28.257  -15.008 20.629  1.00 13.60 ? 152 ASN A CG  1 
ATOM   1190 O  OD1 . ASN A  1 152 ? 29.432  -14.593 20.760  1.00 13.85 ? 152 ASN A OD1 1 
ATOM   1191 N  ND2 . ASN A  1 152 ? 27.690  -15.242 19.486  1.00 13.40 ? 152 ASN A ND2 1 
ATOM   1192 N  N   . PRO A  1 153 ? 30.278  -15.895 23.891  1.00 15.64 ? 153 PRO A N   1 
ATOM   1193 C  CA  . PRO A  1 153 ? 31.376  -15.219 24.543  1.00 16.00 ? 153 PRO A CA  1 
ATOM   1194 C  C   . PRO A  1 153 ? 31.923  -14.034 23.754  1.00 16.55 ? 153 PRO A C   1 
ATOM   1195 O  O   . PRO A  1 153 ? 32.463  -13.072 24.300  1.00 17.53 ? 153 PRO A O   1 
ATOM   1196 C  CB  . PRO A  1 153 ? 32.461  -16.355 24.580  1.00 18.18 ? 153 PRO A CB  1 
ATOM   1197 C  CG  . PRO A  1 153 ? 31.692  -17.640 24.584  1.00 21.47 ? 153 PRO A CG  1 
ATOM   1198 C  CD  . PRO A  1 153 ? 30.447  -17.365 23.725  1.00 16.40 ? 153 PRO A CD  1 
ATOM   1199 N  N   . SER A  1 154 ? 31.851  -14.137 22.427  1.00 15.66 ? 154 SER A N   1 
ATOM   1200 C  CA  . SER A  1 154 ? 32.473  -12.996 21.668  1.00 15.66 ? 154 SER A CA  1 
ATOM   1201 C  C   . SER A  1 154 ? 31.658  -11.747 21.791  1.00 13.68 ? 154 SER A C   1 
ATOM   1202 O  O   . SER A  1 154 ? 32.182  -10.694 22.000  1.00 14.57 ? 154 SER A O   1 
ATOM   1203 C  CB  . SER A  1 154 ? 32.675  -13.370 20.240  1.00 17.31 ? 154 SER A CB  1 
ATOM   1204 O  OG  . SER A  1 154 ? 33.520  -14.575 20.150  1.00 21.26 ? 154 SER A OG  1 
ATOM   1205 N  N   . TYR A  1 155 ? 30.318  -11.917 21.684  1.00 13.10 ? 155 TYR A N   1 
ATOM   1206 C  CA  . TYR A  1 155 ? 29.491  -10.664 21.961  1.00 13.09 ? 155 TYR A CA  1 
ATOM   1207 C  C   . TYR A  1 155 ? 29.632  -10.118 23.375  1.00 15.60 ? 155 TYR A C   1 
ATOM   1208 O  O   . TYR A  1 155 ? 29.563  -8.942  23.567  1.00 14.13 ? 155 TYR A O   1 
ATOM   1209 C  CB  . TYR A  1 155 ? 28.009  -10.890 21.630  1.00 11.81 ? 155 TYR A CB  1 
ATOM   1210 C  CG  . TYR A  1 155 ? 27.751  -10.728 20.108  1.00 11.97 ? 155 TYR A CG  1 
ATOM   1211 C  CD1 . TYR A  1 155 ? 28.113  -11.750 19.225  1.00 11.45 ? 155 TYR A CD1 1 
ATOM   1212 C  CD2 . TYR A  1 155 ? 27.126  -9.578  19.615  1.00 12.41 ? 155 TYR A CD2 1 
ATOM   1213 C  CE1 . TYR A  1 155 ? 27.939  -11.678 17.825  1.00 11.23 ? 155 TYR A CE1 1 
ATOM   1214 C  CE2 . TYR A  1 155 ? 26.924  -9.488  18.225  1.00 10.74 ? 155 TYR A CE2 1 
ATOM   1215 C  CZ  . TYR A  1 155 ? 27.286  -10.490 17.342  1.00 10.67 ? 155 TYR A CZ  1 
ATOM   1216 O  OH  . TYR A  1 155 ? 27.080  -10.210 15.951  1.00 11.72 ? 155 TYR A OH  1 
ATOM   1217 N  N   . ASP A  1 156 ? 29.948  -11.020 24.340  1.00 14.49 ? 156 ASP A N   1 
ATOM   1218 C  CA  . ASP A  1 156 ? 30.172  -10.546 25.673  1.00 16.43 ? 156 ASP A CA  1 
ATOM   1219 C  C   . ASP A  1 156 ? 31.449  -9.718  25.786  1.00 15.65 ? 156 ASP A C   1 
ATOM   1220 O  O   . ASP A  1 156 ? 31.548  -8.929  26.740  1.00 16.98 ? 156 ASP A O   1 
ATOM   1221 C  CB  . ASP A  1 156 ? 30.145  -11.700 26.686  1.00 18.28 ? 156 ASP A CB  1 
ATOM   1222 C  CG  . ASP A  1 156 ? 29.116  -11.383 27.794  1.00 21.08 ? 156 ASP A CG  1 
ATOM   1223 O  OD1 . ASP A  1 156 ? 27.965  -10.907 27.471  1.00 18.54 ? 156 ASP A OD1 1 
ATOM   1224 O  OD2 . ASP A  1 156 ? 29.478  -11.462 29.005  1.00 24.85 ? 156 ASP A OD2 1 
ATOM   1225 N  N   . LYS A  1 157 ? 32.368  -9.828  24.796  1.00 14.99 ? 157 LYS A N   1 
ATOM   1226 C  CA  . LYS A  1 157 ? 33.550  -8.930  24.818  1.00 16.82 ? 157 LYS A CA  1 
ATOM   1227 C  C   . LYS A  1 157 ? 33.109  -7.485  24.671  1.00 17.87 ? 157 LYS A C   1 
ATOM   1228 O  O   . LYS A  1 157 ? 33.786  -6.537  25.154  1.00 16.85 ? 157 LYS A O   1 
ATOM   1229 C  CB  . LYS A  1 157 ? 34.625  -9.311  23.789  1.00 17.59 ? 157 LYS A CB  1 
ATOM   1230 C  CG  . LYS A  1 157 ? 35.145  -10.718 24.130  1.00 18.76 ? 157 LYS A CG  1 
ATOM   1231 C  CD  . LYS A  1 157 ? 36.069  -11.283 23.039  1.00 21.92 ? 157 LYS A CD  1 
ATOM   1232 C  CE  . LYS A  1 157 ? 36.527  -12.723 23.344  1.00 22.27 ? 157 LYS A CE  1 
ATOM   1233 N  NZ  . LYS A  1 157 ? 37.243  -13.355 22.185  1.00 21.39 ? 157 LYS A NZ  1 
ATOM   1234 N  N   . ILE A  1 158 ? 31.929  -7.271  24.065  1.00 16.92 ? 158 ILE A N   1 
ATOM   1235 C  CA  . ILE A  1 158 ? 31.355  -5.927  24.053  1.00 18.62 ? 158 ILE A CA  1 
ATOM   1236 C  C   . ILE A  1 158 ? 30.396  -5.748  25.258  1.00 16.79 ? 158 ILE A C   1 
ATOM   1237 O  O   . ILE A  1 158 ? 30.453  -4.703  25.967  1.00 17.97 ? 158 ILE A O   1 
ATOM   1238 C  CB  . ILE A  1 158 ? 30.610  -5.623  22.747  1.00 18.21 ? 158 ILE A CB  1 
ATOM   1239 C  CG1 . ILE A  1 158 ? 31.623  -5.625  21.599  1.00 20.60 ? 158 ILE A CG1 1 
ATOM   1240 C  CG2 . ILE A  1 158 ? 29.930  -4.232  22.805  1.00 17.37 ? 158 ILE A CG2 1 
ATOM   1241 C  CD1 . ILE A  1 158 ? 30.945  -5.797  20.239  1.00 18.72 ? 158 ILE A CD1 1 
ATOM   1242 N  N   . PHE A  1 159 ? 29.477  -6.730  25.414  1.00 14.91 ? 159 PHE A N   1 
ATOM   1243 C  CA  . PHE A  1 159 ? 28.371  -6.510  26.370  1.00 15.73 ? 159 PHE A CA  1 
ATOM   1244 C  C   . PHE A  1 159 ? 28.834  -6.346  27.833  1.00 15.71 ? 159 PHE A C   1 
ATOM   1245 O  O   . PHE A  1 159 ? 28.190  -5.683  28.607  1.00 17.00 ? 159 PHE A O   1 
ATOM   1246 C  CB  . PHE A  1 159 ? 27.351  -7.605  26.321  1.00 14.84 ? 159 PHE A CB  1 
ATOM   1247 C  CG  . PHE A  1 159 ? 26.625  -7.736  24.973  1.00 15.58 ? 159 PHE A CG  1 
ATOM   1248 C  CD1 . PHE A  1 159 ? 26.546  -6.643  24.073  1.00 17.40 ? 159 PHE A CD1 1 
ATOM   1249 C  CD2 . PHE A  1 159 ? 25.987  -8.910  24.654  1.00 15.31 ? 159 PHE A CD2 1 
ATOM   1250 C  CE1 . PHE A  1 159 ? 25.844  -6.796  22.847  1.00 16.62 ? 159 PHE A CE1 1 
ATOM   1251 C  CE2 . PHE A  1 159 ? 25.282  -9.057  23.448  1.00 16.93 ? 159 PHE A CE2 1 
ATOM   1252 C  CZ  . PHE A  1 159 ? 25.212  -7.988  22.557  1.00 16.52 ? 159 PHE A CZ  1 
ATOM   1253 N  N   . SER A  1 160 ? 29.980  -6.910  28.146  1.00 15.94 ? 160 SER A N   1 
ATOM   1254 C  CA  . SER A  1 160 ? 30.490  -6.749  29.531  1.00 19.86 ? 160 SER A CA  1 
ATOM   1255 C  C   . SER A  1 160 ? 30.869  -5.346  29.897  1.00 20.92 ? 160 SER A C   1 
ATOM   1256 O  O   . SER A  1 160 ? 31.036  -5.054  31.085  1.00 23.57 ? 160 SER A O   1 
ATOM   1257 C  CB  . SER A  1 160 ? 31.677  -7.737  29.704  1.00 18.63 ? 160 SER A CB  1 
ATOM   1258 O  OG  . SER A  1 160 ? 32.785  -7.339  28.948  1.00 21.47 ? 160 SER A OG  1 
ATOM   1259 N  N   . HIS A  1 161 ? 30.992  -4.454  28.914  1.00 18.57 ? 161 HIS A N   1 
ATOM   1260 C  CA  . HIS A  1 161 ? 31.306  -3.072  29.191  1.00 20.31 ? 161 HIS A CA  1 
ATOM   1261 C  C   . HIS A  1 161 ? 30.112  -2.179  29.170  1.00 19.50 ? 161 HIS A C   1 
ATOM   1262 O  O   . HIS A  1 161 ? 30.262  -0.962  29.368  1.00 18.31 ? 161 HIS A O   1 
ATOM   1263 C  CB  . HIS A  1 161 ? 32.305  -2.509  28.166  1.00 20.36 ? 161 HIS A CB  1 
ATOM   1264 C  CG  . HIS A  1 161 ? 33.607  -3.242  28.158  1.00 19.95 ? 161 HIS A CG  1 
ATOM   1265 N  ND1 . HIS A  1 161 ? 34.688  -2.852  28.948  1.00 22.59 ? 161 HIS A ND1 1 
ATOM   1266 C  CD2 . HIS A  1 161 ? 33.992  -4.408  27.491  1.00 21.62 ? 161 HIS A CD2 1 
ATOM   1267 C  CE1 . HIS A  1 161 ? 35.736  -3.717  28.730  1.00 23.62 ? 161 HIS A CE1 1 
ATOM   1268 N  NE2 . HIS A  1 161 ? 35.309  -4.683  27.857  1.00 21.02 ? 161 HIS A NE2 1 
ATOM   1269 N  N   . LEU A  1 162 ? 28.900  -2.745  28.936  1.00 17.72 ? 162 LEU A N   1 
ATOM   1270 C  CA  . LEU A  1 162 ? 27.703  -1.877  28.829  1.00 17.56 ? 162 LEU A CA  1 
ATOM   1271 C  C   . LEU A  1 162 ? 27.434  -1.084  30.095  1.00 19.15 ? 162 LEU A C   1 
ATOM   1272 O  O   . LEU A  1 162 ? 26.942  0.044   30.021  1.00 16.29 ? 162 LEU A O   1 
ATOM   1273 C  CB  . LEU A  1 162 ? 26.413  -2.676  28.498  1.00 17.94 ? 162 LEU A CB  1 
ATOM   1274 C  CG  . LEU A  1 162 ? 26.376  -3.340  27.134  1.00 15.53 ? 162 LEU A CG  1 
ATOM   1275 C  CD1 . LEU A  1 162 ? 25.196  -4.344  27.103  1.00 17.18 ? 162 LEU A CD1 1 
ATOM   1276 C  CD2 . LEU A  1 162 ? 26.225  -2.386  25.949  1.00 24.24 ? 162 LEU A CD2 1 
ATOM   1277 N  N   . GLN A  1 163 ? 27.696  -1.693  31.277  1.00 20.88 ? 163 GLN A N   1 
ATOM   1278 C  CA  . GLN A  1 163 ? 27.330  -0.903  32.485  1.00 25.18 ? 163 GLN A CA  1 
ATOM   1279 C  C   . GLN A  1 163 ? 28.184  0.360   32.586  1.00 24.67 ? 163 GLN A C   1 
ATOM   1280 O  O   . GLN A  1 163 ? 27.718  1.371   33.136  1.00 27.52 ? 163 GLN A O   1 
ATOM   1281 C  CB  . GLN A  1 163 ? 27.281  -1.688  33.809  1.00 33.21 ? 163 GLN A CB  1 
ATOM   1282 C  CG  . GLN A  1 163 ? 28.489  -1.569  34.742  1.00 41.21 ? 163 GLN A CG  1 
ATOM   1283 C  CD  . GLN A  1 163 ? 29.657  -2.541  34.465  1.00 45.30 ? 163 GLN A CD  1 
ATOM   1284 O  OE1 . GLN A  1 163 ? 30.271  -3.042  35.423  1.00 34.02 ? 163 GLN A OE1 1 
ATOM   1285 N  NE2 . GLN A  1 163 ? 30.008  -2.766  33.182  1.00 40.73 ? 163 GLN A NE2 1 
ATOM   1286 N  N   . HIS A  1 164 ? 29.352  0.372   31.940  1.00 18.95 ? 164 HIS A N   1 
ATOM   1287 C  CA  . HIS A  1 164 ? 30.170  1.632   31.949  1.00 17.90 ? 164 HIS A CA  1 
ATOM   1288 C  C   . HIS A  1 164 ? 29.753  2.701   31.003  1.00 18.38 ? 164 HIS A C   1 
ATOM   1289 O  O   . HIS A  1 164 ? 30.304  3.773   31.026  1.00 18.78 ? 164 HIS A O   1 
ATOM   1290 C  CB  . HIS A  1 164 ? 31.693  1.393   31.791  1.00 16.25 ? 164 HIS A CB  1 
ATOM   1291 C  CG  . HIS A  1 164 ? 32.318  0.465   32.840  1.00 18.72 ? 164 HIS A CG  1 
ATOM   1292 N  ND1 . HIS A  1 164 ? 32.083  0.550   34.177  1.00 19.30 ? 164 HIS A ND1 1 
ATOM   1293 C  CD2 . HIS A  1 164 ? 33.302  -0.476  32.684  1.00 22.20 ? 164 HIS A CD2 1 
ATOM   1294 C  CE1 . HIS A  1 164 ? 32.807  -0.375  34.820  1.00 17.94 ? 164 HIS A CE1 1 
ATOM   1295 N  NE2 . HIS A  1 164 ? 33.547  -1.007  33.923  1.00 25.26 ? 164 HIS A NE2 1 
ATOM   1296 N  N   . VAL A  1 165 ? 28.836  2.361   30.056  1.00 15.98 ? 165 VAL A N   1 
ATOM   1297 C  CA  . VAL A  1 165 ? 28.379  3.360   29.141  1.00 15.24 ? 165 VAL A CA  1 
ATOM   1298 C  C   . VAL A  1 165 ? 26.846  3.523   29.225  1.00 17.42 ? 165 VAL A C   1 
ATOM   1299 O  O   . VAL A  1 165 ? 26.177  3.840   28.215  1.00 14.74 ? 165 VAL A O   1 
ATOM   1300 C  CB  . VAL A  1 165 ? 28.824  3.040   27.676  1.00 17.85 ? 165 VAL A CB  1 
ATOM   1301 C  CG1 . VAL A  1 165 ? 30.352  3.137   27.536  1.00 15.77 ? 165 VAL A CG1 1 
ATOM   1302 C  CG2 . VAL A  1 165 ? 28.431  1.660   27.175  1.00 16.09 ? 165 VAL A CG2 1 
ATOM   1303 N  N   . LYS A  1 166 ? 26.296  3.402   30.429  1.00 16.77 ? 166 LYS A N   1 
ATOM   1304 C  CA  . LYS A  1 166 ? 24.837  3.528   30.690  1.00 16.69 ? 166 LYS A CA  1 
ATOM   1305 C  C   . LYS A  1 166 ? 24.186  4.798   30.142  1.00 15.48 ? 166 LYS A C   1 
ATOM   1306 O  O   . LYS A  1 166 ? 23.096  4.748   29.621  1.00 17.08 ? 166 LYS A O   1 
ATOM   1307 C  CB  . LYS A  1 166 ? 24.597  3.434   32.203  1.00 18.79 ? 166 LYS A CB  1 
ATOM   1308 C  CG  . LYS A  1 166 ? 23.176  3.460   32.740  1.00 22.04 ? 166 LYS A CG  1 
ATOM   1309 C  CD  . LYS A  1 166 ? 23.062  3.043   34.252  1.00 26.50 ? 166 LYS A CD  1 
ATOM   1310 C  CE  . LYS A  1 166 ? 23.532  1.601   34.487  1.00 30.33 ? 166 LYS A CE  1 
ATOM   1311 N  NZ  . LYS A  1 166 ? 22.532  0.654   33.855  1.00 39.53 ? 166 LYS A NZ  1 
ATOM   1312 N  N   . TYR A  1 167 ? 24.871  5.959   30.261  1.00 15.03 ? 167 TYR A N   1 
ATOM   1313 C  CA  . TYR A  1 167 ? 24.246  7.203   29.901  1.00 14.98 ? 167 TYR A CA  1 
ATOM   1314 C  C   . TYR A  1 167 ? 24.927  7.872   28.717  1.00 15.44 ? 167 TYR A C   1 
ATOM   1315 O  O   . TYR A  1 167 ? 26.137  7.667   28.431  1.00 15.22 ? 167 TYR A O   1 
ATOM   1316 C  CB  . TYR A  1 167 ? 24.290  8.194   31.059  1.00 15.07 ? 167 TYR A CB  1 
ATOM   1317 C  CG  . TYR A  1 167 ? 23.512  7.693   32.274  1.00 15.29 ? 167 TYR A CG  1 
ATOM   1318 C  CD1 . TYR A  1 167 ? 22.112  7.778   32.317  1.00 18.08 ? 167 TYR A CD1 1 
ATOM   1319 C  CD2 . TYR A  1 167 ? 24.191  7.110   33.329  1.00 16.45 ? 167 TYR A CD2 1 
ATOM   1320 C  CE1 . TYR A  1 167 ? 21.401  7.262   33.405  1.00 18.97 ? 167 TYR A CE1 1 
ATOM   1321 C  CE2 . TYR A  1 167 ? 23.486  6.606   34.408  1.00 18.88 ? 167 TYR A CE2 1 
ATOM   1322 C  CZ  . TYR A  1 167 ? 22.121  6.733   34.467  1.00 21.49 ? 167 TYR A CZ  1 
ATOM   1323 O  OH  . TYR A  1 167 ? 21.462  6.209   35.598  1.00 23.15 ? 167 TYR A OH  1 
ATOM   1324 N  N   . LYS A  1 168 ? 24.153  8.706   28.039  1.00 16.82 ? 168 LYS A N   1 
ATOM   1325 C  CA  . LYS A  1 168 ? 24.681  9.442   26.903  1.00 17.20 ? 168 LYS A CA  1 
ATOM   1326 C  C   . LYS A  1 168 ? 25.998  10.209  27.214  1.00 18.06 ? 168 LYS A C   1 
ATOM   1327 O  O   . LYS A  1 168 ? 26.080  10.879  28.276  1.00 19.97 ? 168 LYS A O   1 
ATOM   1328 C  CB  . LYS A  1 168 ? 23.619  10.385  26.346  1.00 20.52 ? 168 LYS A CB  1 
ATOM   1329 C  CG  . LYS A  1 168 ? 24.084  11.125  25.106  1.00 19.44 ? 168 LYS A CG  1 
ATOM   1330 C  CD  . LYS A  1 168 ? 23.038  12.039  24.459  1.00 23.32 ? 168 LYS A CD  1 
ATOM   1331 C  CE  . LYS A  1 168 ? 23.710  12.802  23.324  1.00 26.31 ? 168 LYS A CE  1 
ATOM   1332 N  NZ  . LYS A  1 168 ? 22.644  13.667  22.705  1.00 30.33 ? 168 LYS A NZ  1 
ATOM   1333 N  N   . GLY A  1 169 ? 27.003  10.113  26.350  1.00 17.87 ? 169 GLY A N   1 
ATOM   1334 C  CA  . GLY A  1 169 ? 28.272  10.826  26.572  1.00 19.16 ? 169 GLY A CA  1 
ATOM   1335 C  C   . GLY A  1 169 ? 29.277  9.983   27.328  1.00 21.22 ? 169 GLY A C   1 
ATOM   1336 O  O   . GLY A  1 169 ? 30.483  10.246  27.302  1.00 24.49 ? 169 GLY A O   1 
ATOM   1337 N  N   . GLN A  1 170 ? 28.800  8.916   27.973  1.00 18.01 ? 170 GLN A N   1 
ATOM   1338 C  CA  . GLN A  1 170 ? 29.782  8.004   28.631  1.00 17.09 ? 170 GLN A CA  1 
ATOM   1339 C  C   . GLN A  1 170 ? 30.592  7.150   27.703  1.00 20.21 ? 170 GLN A C   1 
ATOM   1340 O  O   . GLN A  1 170 ? 30.097  6.782   26.601  1.00 17.90 ? 170 GLN A O   1 
ATOM   1341 C  CB  . GLN A  1 170 ? 29.105  7.182   29.711  1.00 17.76 ? 170 GLN A CB  1 
ATOM   1342 C  CG  . GLN A  1 170 ? 28.531  8.044   30.827  1.00 17.76 ? 170 GLN A CG  1 
ATOM   1343 C  CD  . GLN A  1 170 ? 27.979  7.199   31.974  1.00 17.49 ? 170 GLN A CD  1 
ATOM   1344 O  OE1 . GLN A  1 170 ? 27.429  6.108   31.784  1.00 20.16 ? 170 GLN A OE1 1 
ATOM   1345 N  NE2 . GLN A  1 170 ? 28.221  7.661   33.192  1.00 18.02 ? 170 GLN A NE2 1 
ATOM   1346 N  N   A GLU A  1 171 ? 31.843  6.817   28.082  0.50 18.93 ? 171 GLU A N   1 
ATOM   1347 N  N   B GLU A  1 171 ? 31.805  6.779   28.139  0.50 17.99 ? 171 GLU A N   1 
ATOM   1348 C  CA  A GLU A  1 171 ? 32.764  6.056   27.243  0.50 19.38 ? 171 GLU A CA  1 
ATOM   1349 C  CA  B GLU A  1 171 ? 32.680  5.949   27.372  0.50 16.89 ? 171 GLU A CA  1 
ATOM   1350 C  C   A GLU A  1 171 ? 33.601  5.080   28.055  0.50 18.13 ? 171 GLU A C   1 
ATOM   1351 C  C   B GLU A  1 171 ? 33.389  4.869   28.171  0.50 17.23 ? 171 GLU A C   1 
ATOM   1352 O  O   A GLU A  1 171 ? 33.817  5.317   29.249  0.50 18.80 ? 171 GLU A O   1 
ATOM   1353 O  O   B GLU A  1 171 ? 33.341  4.806   29.437  0.50 14.82 ? 171 GLU A O   1 
ATOM   1354 C  CB  A GLU A  1 171 ? 33.678  7.032   26.457  0.50 20.35 ? 171 GLU A CB  1 
ATOM   1355 C  CB  B GLU A  1 171 ? 33.708  6.838   26.643  0.50 17.89 ? 171 GLU A CB  1 
ATOM   1356 C  CG  A GLU A  1 171 ? 32.943  8.238   25.908  0.50 23.27 ? 171 GLU A CG  1 
ATOM   1357 C  CG  B GLU A  1 171 ? 34.635  7.572   27.604  0.50 18.79 ? 171 GLU A CG  1 
ATOM   1358 C  CD  A GLU A  1 171 ? 33.805  9.320   25.264  0.50 25.18 ? 171 GLU A CD  1 
ATOM   1359 C  CD  B GLU A  1 171 ? 35.764  8.290   26.895  0.50 19.24 ? 171 GLU A CD  1 
ATOM   1360 O  OE1 A GLU A  1 171 ? 34.982  9.516   25.674  0.50 25.44 ? 171 GLU A OE1 1 
ATOM   1361 O  OE1 B GLU A  1 171 ? 35.604  8.700   25.719  0.50 21.82 ? 171 GLU A OE1 1 
ATOM   1362 O  OE2 A GLU A  1 171 ? 33.259  10.020  24.388  0.50 23.80 ? 171 GLU A OE2 1 
ATOM   1363 O  OE2 B GLU A  1 171 ? 36.885  8.400   27.500  0.50 17.99 ? 171 GLU A OE2 1 
ATOM   1364 N  N   . ALA A  1 172 ? 34.014  3.979   27.433  1.00 16.98 ? 172 ALA A N   1 
ATOM   1365 C  CA  . ALA A  1 172 ? 34.725  2.848   28.038  1.00 19.22 ? 172 ALA A CA  1 
ATOM   1366 C  C   . ALA A  1 172 ? 35.720  2.426   26.998  1.00 22.00 ? 172 ALA A C   1 
ATOM   1367 O  O   . ALA A  1 172 ? 35.553  2.727   25.794  1.00 21.83 ? 172 ALA A O   1 
ATOM   1368 C  CB  . ALA A  1 172 ? 33.778  1.673   28.350  1.00 22.47 ? 172 ALA A CB  1 
ATOM   1369 N  N   . PHE A  1 173 ? 36.802  1.814   27.436  1.00 19.76 ? 173 PHE A N   1 
ATOM   1370 C  CA  . PHE A  1 173 ? 37.782  1.292   26.540  1.00 19.99 ? 173 PHE A CA  1 
ATOM   1371 C  C   . PHE A  1 173 ? 37.685  -0.214  26.498  1.00 20.63 ? 173 PHE A C   1 
ATOM   1372 O  O   . PHE A  1 173 ? 37.556  -0.874  27.560  1.00 22.59 ? 173 PHE A O   1 
ATOM   1373 C  CB  . PHE A  1 173 ? 39.140  1.726   27.026  1.00 20.56 ? 173 PHE A CB  1 
ATOM   1374 C  CG  . PHE A  1 173 ? 39.443  3.104   26.592  1.00 24.62 ? 173 PHE A CG  1 
ATOM   1375 C  CD1 . PHE A  1 173 ? 39.729  3.384   25.229  1.00 25.02 ? 173 PHE A CD1 1 
ATOM   1376 C  CD2 . PHE A  1 173 ? 39.392  4.147   27.518  1.00 28.53 ? 173 PHE A CD2 1 
ATOM   1377 C  CE1 . PHE A  1 173 ? 40.018  4.695   24.815  1.00 28.30 ? 173 PHE A CE1 1 
ATOM   1378 C  CE2 . PHE A  1 173 ? 39.667  5.449   27.120  1.00 33.02 ? 173 PHE A CE2 1 
ATOM   1379 C  CZ  . PHE A  1 173 ? 39.980  5.738   25.771  1.00 30.42 ? 173 PHE A CZ  1 
ATOM   1380 N  N   . VAL A  1 174 ? 37.676  -0.752  25.271  1.00 18.95 ? 174 VAL A N   1 
ATOM   1381 C  CA  . VAL A  1 174 ? 37.553  -2.180  25.067  1.00 17.52 ? 174 VAL A CA  1 
ATOM   1382 C  C   . VAL A  1 174 ? 38.813  -2.707  24.458  1.00 19.18 ? 174 VAL A C   1 
ATOM   1383 O  O   . VAL A  1 174 ? 39.256  -2.164  23.430  1.00 20.29 ? 174 VAL A O   1 
ATOM   1384 C  CB  . VAL A  1 174 ? 36.375  -2.491  24.104  1.00 18.04 ? 174 VAL A CB  1 
ATOM   1385 C  CG1 . VAL A  1 174 ? 36.275  -3.944  23.897  1.00 17.65 ? 174 VAL A CG1 1 
ATOM   1386 C  CG2 . VAL A  1 174 ? 35.073  -1.983  24.684  1.00 20.13 ? 174 VAL A CG2 1 
ATOM   1387 N  N   . PRO A  1 175 ? 39.407  -3.752  25.078  1.00 19.71 ? 175 PRO A N   1 
ATOM   1388 C  CA  . PRO A  1 175 ? 40.639  -4.222  24.490  1.00 21.29 ? 175 PRO A CA  1 
ATOM   1389 C  C   . PRO A  1 175 ? 40.375  -4.930  23.175  1.00 19.36 ? 175 PRO A C   1 
ATOM   1390 O  O   . PRO A  1 175 ? 39.340  -5.576  23.021  1.00 19.88 ? 175 PRO A O   1 
ATOM   1391 C  CB  . PRO A  1 175 ? 41.190  -5.245  25.519  1.00 22.49 ? 175 PRO A CB  1 
ATOM   1392 C  CG  . PRO A  1 175 ? 40.352  -5.086  26.748  1.00 24.69 ? 175 PRO A CG  1 
ATOM   1393 C  CD  . PRO A  1 175 ? 39.052  -4.361  26.352  1.00 19.64 ? 175 PRO A CD  1 
ATOM   1394 N  N   . GLY A  1 176 ? 41.321  -4.818  22.252  1.00 20.91 ? 176 GLY A N   1 
ATOM   1395 C  CA  . GLY A  1 176 ? 41.217  -5.478  20.983  1.00 18.41 ? 176 GLY A CA  1 
ATOM   1396 C  C   . GLY A  1 176 ? 40.847  -6.946  21.091  1.00 20.94 ? 176 GLY A C   1 
ATOM   1397 O  O   . GLY A  1 176 ? 41.407  -7.728  21.886  1.00 21.19 ? 176 GLY A O   1 
ATOM   1398 N  N   . PHE A  1 177 ? 39.912  -7.372  20.243  1.00 17.61 ? 177 PHE A N   1 
ATOM   1399 C  CA  . PHE A  1 177 ? 39.614  -8.770  20.018  1.00 16.94 ? 177 PHE A CA  1 
ATOM   1400 C  C   . PHE A  1 177 ? 39.293  -9.041  18.545  1.00 15.45 ? 177 PHE A C   1 
ATOM   1401 O  O   . PHE A  1 177 ? 39.279  -8.066  17.781  1.00 15.36 ? 177 PHE A O   1 
ATOM   1402 C  CB  . PHE A  1 177 ? 38.503  -9.306  20.941  1.00 17.97 ? 177 PHE A CB  1 
ATOM   1403 C  CG  . PHE A  1 177 ? 37.110  -8.744  20.631  1.00 16.24 ? 177 PHE A CG  1 
ATOM   1404 C  CD1 . PHE A  1 177 ? 36.796  -7.480  21.085  1.00 15.14 ? 177 PHE A CD1 1 
ATOM   1405 C  CD2 . PHE A  1 177 ? 36.165  -9.471  19.878  1.00 18.13 ? 177 PHE A CD2 1 
ATOM   1406 C  CE1 . PHE A  1 177 ? 35.550  -6.885  20.800  1.00 18.32 ? 177 PHE A CE1 1 
ATOM   1407 C  CE2 . PHE A  1 177 ? 34.924  -8.898  19.610  1.00 17.48 ? 177 PHE A CE2 1 
ATOM   1408 C  CZ  . PHE A  1 177 ? 34.608  -7.624  20.073  1.00 17.41 ? 177 PHE A CZ  1 
ATOM   1409 N  N   . ASN A  1 178 ? 39.106  -10.295 18.130  1.00 15.43 ? 178 ASN A N   1 
ATOM   1410 C  CA  . ASN A  1 178 ? 38.847  -10.614 16.743  1.00 16.00 ? 178 ASN A CA  1 
ATOM   1411 C  C   . ASN A  1 178 ? 37.359  -10.336 16.410  1.00 14.42 ? 178 ASN A C   1 
ATOM   1412 O  O   . ASN A  1 178 ? 36.451  -11.169 16.679  1.00 13.43 ? 178 ASN A O   1 
ATOM   1413 C  CB  . ASN A  1 178 ? 39.170  -12.080 16.477  1.00 17.43 ? 178 ASN A CB  1 
ATOM   1414 C  CG  . ASN A  1 178 ? 39.044  -12.438 15.021  1.00 18.44 ? 178 ASN A CG  1 
ATOM   1415 O  OD1 . ASN A  1 178 ? 38.784  -11.591 14.153  1.00 16.85 ? 178 ASN A OD1 1 
ATOM   1416 N  ND2 . ASN A  1 178 ? 39.180  -13.695 14.723  1.00 21.37 ? 178 ASN A ND2 1 
ATOM   1417 N  N   . ILE A  1 179 ? 37.187  -9.217  15.707  1.00 13.12 ? 179 ILE A N   1 
ATOM   1418 C  CA  . ILE A  1 179 ? 35.815  -8.802  15.337  1.00 13.55 ? 179 ILE A CA  1 
ATOM   1419 C  C   . ILE A  1 179 ? 35.168  -9.831  14.415  1.00 14.77 ? 179 ILE A C   1 
ATOM   1420 O  O   . ILE A  1 179 ? 33.934  -9.930  14.365  1.00 12.84 ? 179 ILE A O   1 
ATOM   1421 C  CB  . ILE A  1 179 ? 35.859  -7.448  14.654  1.00 12.25 ? 179 ILE A CB  1 
ATOM   1422 C  CG1 . ILE A  1 179 ? 36.506  -6.396  15.560  1.00 13.37 ? 179 ILE A CG1 1 
ATOM   1423 C  CG2 . ILE A  1 179 ? 34.445  -7.018  14.187  1.00 13.70 ? 179 ILE A CG2 1 
ATOM   1424 C  CD1 . ILE A  1 179 ? 35.888  -6.203  16.957  1.00 14.29 ? 179 ILE A CD1 1 
ATOM   1425 N  N   . GLU A  1 180 ? 35.930  -10.627 13.667  1.00 13.98 ? 180 GLU A N   1 
ATOM   1426 C  CA  . GLU A  1 180 ? 35.306  -11.643 12.894  1.00 13.31 ? 180 GLU A CA  1 
ATOM   1427 C  C   . GLU A  1 180 ? 34.499  -12.682 13.758  1.00 12.90 ? 180 GLU A C   1 
ATOM   1428 O  O   . GLU A  1 180 ? 33.622  -13.372 13.199  1.00 13.91 ? 180 GLU A O   1 
ATOM   1429 C  CB  . GLU A  1 180 ? 36.354  -12.384 12.049  1.00 15.71 ? 180 GLU A CB  1 
ATOM   1430 C  CG  . GLU A  1 180 ? 35.776  -13.096 10.844  1.00 19.42 ? 180 GLU A CG  1 
ATOM   1431 C  CD  . GLU A  1 180 ? 36.820  -13.582 9.821   1.00 20.48 ? 180 GLU A CD  1 
ATOM   1432 O  OE1 . GLU A  1 180 ? 38.000  -13.290 9.966   1.00 22.22 ? 180 GLU A OE1 1 
ATOM   1433 O  OE2 . GLU A  1 180 ? 36.393  -14.327 8.948   1.00 23.71 ? 180 GLU A OE2 1 
ATOM   1434 N  N   . GLU A  1 181 ? 34.854  -12.733 15.065  1.00 11.95 ? 181 GLU A N   1 
ATOM   1435 C  CA  . GLU A  1 181 ? 34.068  -13.642 15.951  1.00 13.29 ? 181 GLU A CA  1 
ATOM   1436 C  C   . GLU A  1 181 ? 32.573  -13.215 16.054  1.00 12.43 ? 181 GLU A C   1 
ATOM   1437 O  O   . GLU A  1 181 ? 31.749  -13.997 16.507  1.00 14.79 ? 181 GLU A O   1 
ATOM   1438 C  CB  . GLU A  1 181 ? 34.641  -13.741 17.363  1.00 14.04 ? 181 GLU A CB  1 
ATOM   1439 C  CG  . GLU A  1 181 ? 36.071  -14.291 17.463  1.00 16.57 ? 181 GLU A CG  1 
ATOM   1440 C  CD  . GLU A  1 181 ? 36.698  -14.082 18.801  1.00 19.85 ? 181 GLU A CD  1 
ATOM   1441 O  OE1 . GLU A  1 181 ? 36.024  -13.654 19.784  1.00 19.56 ? 181 GLU A OE1 1 
ATOM   1442 O  OE2 . GLU A  1 181 ? 37.931  -14.376 18.875  1.00 20.38 ? 181 GLU A OE2 1 
ATOM   1443 N  N   . LEU A  1 182 ? 32.276  -11.969 15.651  1.00 12.29 ? 182 LEU A N   1 
ATOM   1444 C  CA  . LEU A  1 182 ? 30.894  -11.501 15.719  1.00 10.62 ? 182 LEU A CA  1 
ATOM   1445 C  C   . LEU A  1 182 ? 30.098  -11.847 14.495  1.00 11.59 ? 182 LEU A C   1 
ATOM   1446 O  O   . LEU A  1 182 ? 28.850  -11.656 14.492  1.00 11.58 ? 182 LEU A O   1 
ATOM   1447 C  CB  . LEU A  1 182 ? 30.945  -9.969  15.859  1.00 9.82  ? 182 LEU A CB  1 
ATOM   1448 C  CG  . LEU A  1 182 ? 31.727  -9.391  17.040  1.00 9.60  ? 182 LEU A CG  1 
ATOM   1449 C  CD1 . LEU A  1 182 ? 31.643  -7.861  17.087  1.00 10.90 ? 182 LEU A CD1 1 
ATOM   1450 C  CD2 . LEU A  1 182 ? 31.193  -9.958  18.361  1.00 11.63 ? 182 LEU A CD2 1 
ATOM   1451 N  N   . LEU A  1 183 ? 30.760  -12.359 13.452  1.00 10.89 ? 183 LEU A N   1 
ATOM   1452 C  CA  . LEU A  1 183 ? 30.091  -12.738 12.249  1.00 11.06 ? 183 LEU A CA  1 
ATOM   1453 C  C   . LEU A  1 183 ? 29.496  -14.120 12.346  1.00 12.35 ? 183 LEU A C   1 
ATOM   1454 O  O   . LEU A  1 183 ? 30.051  -14.952 13.060  1.00 13.82 ? 183 LEU A O   1 
ATOM   1455 C  CB  . LEU A  1 183 ? 31.045  -12.642 10.996  1.00 11.47 ? 183 LEU A CB  1 
ATOM   1456 C  CG  . LEU A  1 183 ? 31.711  -11.227 10.920  1.00 12.26 ? 183 LEU A CG  1 
ATOM   1457 C  CD1 . LEU A  1 183 ? 32.646  -11.263 9.690   1.00 15.85 ? 183 LEU A CD1 1 
ATOM   1458 C  CD2 . LEU A  1 183 ? 30.618  -10.158 10.791  1.00 12.83 ? 183 LEU A CD2 1 
ATOM   1459 N  N   . PRO A  1 184 ? 28.456  -14.416 11.622  1.00 10.70 ? 184 PRO A N   1 
ATOM   1460 C  CA  . PRO A  1 184 ? 27.788  -15.700 11.642  1.00 12.18 ? 184 PRO A CA  1 
ATOM   1461 C  C   . PRO A  1 184 ? 28.509  -16.748 10.825  1.00 15.05 ? 184 PRO A C   1 
ATOM   1462 O  O   . PRO A  1 184 ? 29.576  -16.492 10.179  1.00 15.26 ? 184 PRO A O   1 
ATOM   1463 C  CB  . PRO A  1 184 ? 26.361  -15.345 11.083  1.00 12.60 ? 184 PRO A CB  1 
ATOM   1464 C  CG  . PRO A  1 184 ? 26.811  -14.403 9.952   1.00 11.78 ? 184 PRO A CG  1 
ATOM   1465 C  CD  . PRO A  1 184 ? 27.753  -13.483 10.718  1.00 11.07 ? 184 PRO A CD  1 
ATOM   1466 N  N   . GLU A  1 185 ? 27.934  -17.963 10.902  1.00 16.57 ? 185 GLU A N   1 
ATOM   1467 C  CA  . GLU A  1 185 ? 28.380  -19.043 10.021  1.00 17.53 ? 185 GLU A CA  1 
ATOM   1468 C  C   . GLU A  1 185 ? 28.153  -18.768 8.566   1.00 16.70 ? 185 GLU A C   1 
ATOM   1469 O  O   . GLU A  1 185 ? 27.160  -18.065 8.185   1.00 15.87 ? 185 GLU A O   1 
ATOM   1470 C  CB  . GLU A  1 185 ? 27.562  -20.293 10.486  1.00 20.01 ? 185 GLU A CB  1 
ATOM   1471 C  CG  . GLU A  1 185 ? 28.079  -20.761 11.869  1.00 25.63 ? 185 GLU A CG  1 
ATOM   1472 C  CD  . GLU A  1 185 ? 29.603  -20.972 11.839  1.00 35.26 ? 185 GLU A CD  1 
ATOM   1473 O  OE1 . GLU A  1 185 ? 30.074  -21.807 11.015  1.00 34.42 ? 185 GLU A OE1 1 
ATOM   1474 O  OE2 . GLU A  1 185 ? 30.348  -20.273 12.577  1.00 37.91 ? 185 GLU A OE2 1 
ATOM   1475 N  N   . ARG A  1 186 ? 29.072  -19.285 7.705   1.00 15.89 ? 186 ARG A N   1 
ATOM   1476 C  CA  . ARG A  1 186 ? 28.906  -19.228 6.305   1.00 17.72 ? 186 ARG A CA  1 
ATOM   1477 C  C   . ARG A  1 186 ? 28.654  -17.758 5.852   1.00 15.33 ? 186 ARG A C   1 
ATOM   1478 O  O   . ARG A  1 186 ? 27.689  -17.449 5.106   1.00 16.30 ? 186 ARG A O   1 
ATOM   1479 C  CB  . ARG A  1 186 ? 27.832  -20.176 5.771   1.00 19.24 ? 186 ARG A CB  1 
ATOM   1480 C  CG  . ARG A  1 186 ? 28.076  -21.593 6.326   1.00 24.00 ? 186 ARG A CG  1 
ATOM   1481 C  CD  . ARG A  1 186 ? 27.372  -22.694 5.538   1.00 24.80 ? 186 ARG A CD  1 
ATOM   1482 N  NE  . ARG A  1 186 ? 25.939  -22.452 5.358   1.00 26.20 ? 186 ARG A NE  1 
ATOM   1483 C  CZ  . ARG A  1 186 ? 25.035  -22.506 6.325   1.00 26.76 ? 186 ARG A CZ  1 
ATOM   1484 N  NH1 . ARG A  1 186 ? 25.412  -22.834 7.576   1.00 29.16 ? 186 ARG A NH1 1 
ATOM   1485 N  NH2 . ARG A  1 186 ? 23.755  -22.271 6.029   1.00 30.31 ? 186 ARG A NH2 1 
ATOM   1486 N  N   . THR A  1 187 ? 29.638  -16.927 6.144   1.00 12.90 ? 187 THR A N   1 
ATOM   1487 C  CA  . THR A  1 187 ? 29.585  -15.544 5.620   1.00 13.70 ? 187 THR A CA  1 
ATOM   1488 C  C   . THR A  1 187 ? 29.597  -15.406 4.115   1.00 13.52 ? 187 THR A C   1 
ATOM   1489 O  O   . THR A  1 187 ? 29.247  -14.403 3.589   1.00 13.52 ? 187 THR A O   1 
ATOM   1490 C  CB  . THR A  1 187 ? 30.720  -14.684 6.181   1.00 14.61 ? 187 THR A CB  1 
ATOM   1491 O  OG1 . THR A  1 187 ? 31.996  -15.322 5.920   1.00 15.64 ? 187 THR A OG1 1 
ATOM   1492 C  CG2 . THR A  1 187 ? 30.540  -14.425 7.705   1.00 14.38 ? 187 THR A CG2 1 
ATOM   1493 N  N   . ALA A  1 188 ? 29.994  -16.446 3.360   1.00 13.96 ? 188 ALA A N   1 
ATOM   1494 C  CA  . ALA A  1 188 ? 29.764  -16.439 1.877   1.00 14.26 ? 188 ALA A CA  1 
ATOM   1495 C  C   . ALA A  1 188 ? 28.299  -16.310 1.412   1.00 12.18 ? 188 ALA A C   1 
ATOM   1496 O  O   . ALA A  1 188 ? 28.053  -15.912 0.322   1.00 14.02 ? 188 ALA A O   1 
ATOM   1497 C  CB  . ALA A  1 188 ? 30.372  -17.737 1.209   1.00 16.47 ? 188 ALA A CB  1 
ATOM   1498 N  N   . GLU A  1 189 ? 27.367  -16.578 2.354   1.00 13.09 ? 189 GLU A N   1 
ATOM   1499 C  CA  . GLU A  1 189 ? 25.928  -16.531 2.112   1.00 13.23 ? 189 GLU A CA  1 
ATOM   1500 C  C   . GLU A  1 189 ? 25.378  -15.180 2.612   1.00 10.12 ? 189 GLU A C   1 
ATOM   1501 O  O   . GLU A  1 189 ? 25.371  -14.900 3.805   1.00 9.93  ? 189 GLU A O   1 
ATOM   1502 C  CB  . GLU A  1 189 ? 25.183  -17.647 2.810   1.00 14.51 ? 189 GLU A CB  1 
ATOM   1503 C  CG  . GLU A  1 189 ? 25.605  -19.041 2.292   1.00 17.49 ? 189 GLU A CG  1 
ATOM   1504 C  CD  . GLU A  1 189 ? 25.077  -20.197 3.148   1.00 23.55 ? 189 GLU A CD  1 
ATOM   1505 O  OE1 . GLU A  1 189 ? 24.300  -19.979 4.090   1.00 21.61 ? 189 GLU A OE1 1 
ATOM   1506 O  OE2 . GLU A  1 189 ? 25.510  -21.392 2.907   1.00 26.61 ? 189 GLU A OE2 1 
ATOM   1507 N  N   . TYR A  1 190 ? 24.989  -14.315 1.665   1.00 9.52  ? 190 TYR A N   1 
ATOM   1508 C  CA  . TYR A  1 190 ? 24.492  -12.958 2.035   1.00 9.12  ? 190 TYR A CA  1 
ATOM   1509 C  C   . TYR A  1 190 ? 23.515  -12.429 1.018   1.00 10.38 ? 190 TYR A C   1 
ATOM   1510 O  O   . TYR A  1 190 ? 23.463  -12.783 -0.186  1.00 10.29 ? 190 TYR A O   1 
ATOM   1511 C  CB  . TYR A  1 190 ? 25.694  -11.974 2.248   1.00 10.50 ? 190 TYR A CB  1 
ATOM   1512 C  CG  . TYR A  1 190 ? 26.612  -11.838 1.086   1.00 11.38 ? 190 TYR A CG  1 
ATOM   1513 C  CD1 . TYR A  1 190 ? 26.315  -10.943 0.061   1.00 11.53 ? 190 TYR A CD1 1 
ATOM   1514 C  CD2 . TYR A  1 190 ? 27.857  -12.559 1.031   1.00 11.92 ? 190 TYR A CD2 1 
ATOM   1515 C  CE1 . TYR A  1 190 ? 27.178  -10.770 -1.071  1.00 12.80 ? 190 TYR A CE1 1 
ATOM   1516 C  CE2 . TYR A  1 190 ? 28.692  -12.314 -0.063  1.00 10.97 ? 190 TYR A CE2 1 
ATOM   1517 C  CZ  . TYR A  1 190 ? 28.331  -11.450 -1.055  1.00 12.30 ? 190 TYR A CZ  1 
ATOM   1518 O  OH  . TYR A  1 190 ? 29.281  -11.315 -2.097  1.00 14.77 ? 190 TYR A OH  1 
ATOM   1519 N  N   . TYR A  1 191 ? 22.831  -11.394 1.490   1.00 10.04 ? 191 TYR A N   1 
ATOM   1520 C  CA  . TYR A  1 191 ? 21.951  -10.543 0.702   1.00 9.21  ? 191 TYR A CA  1 
ATOM   1521 C  C   . TYR A  1 191 ? 22.724  -9.249  0.365   1.00 9.89  ? 191 TYR A C   1 
ATOM   1522 O  O   . TYR A  1 191 ? 23.469  -8.755  1.246   1.00 9.77  ? 191 TYR A O   1 
ATOM   1523 C  CB  . TYR A  1 191 ? 20.668  -10.132 1.477   1.00 10.57 ? 191 TYR A CB  1 
ATOM   1524 C  CG  . TYR A  1 191 ? 19.840  -11.263 2.055   1.00 10.08 ? 191 TYR A CG  1 
ATOM   1525 C  CD1 . TYR A  1 191 ? 18.803  -11.783 1.313   1.00 10.70 ? 191 TYR A CD1 1 
ATOM   1526 C  CD2 . TYR A  1 191 ? 20.090  -11.662 3.372   1.00 8.97  ? 191 TYR A CD2 1 
ATOM   1527 C  CE1 . TYR A  1 191 ? 17.973  -12.759 1.879   1.00 11.07 ? 191 TYR A CE1 1 
ATOM   1528 C  CE2 . TYR A  1 191 ? 19.290  -12.643 3.956   1.00 10.37 ? 191 TYR A CE2 1 
ATOM   1529 C  CZ  . TYR A  1 191 ? 18.271  -13.138 3.183   1.00 10.20 ? 191 TYR A CZ  1 
ATOM   1530 O  OH  . TYR A  1 191 ? 17.478  -14.169 3.743   1.00 12.86 ? 191 TYR A OH  1 
ATOM   1531 N  N   . ARG A  1 192 ? 22.583  -8.707  -0.803  1.00 9.65  ? 192 ARG A N   1 
ATOM   1532 C  CA  . ARG A  1 192 ? 23.297  -7.467  -1.186  1.00 10.16 ? 192 ARG A CA  1 
ATOM   1533 C  C   . ARG A  1 192 ? 22.332  -6.547  -1.893  1.00 9.60  ? 192 ARG A C   1 
ATOM   1534 O  O   . ARG A  1 192 ? 21.613  -6.994  -2.813  1.00 10.00 ? 192 ARG A O   1 
ATOM   1535 C  CB  . ARG A  1 192 ? 24.396  -7.877  -2.149  1.00 10.63 ? 192 ARG A CB  1 
ATOM   1536 C  CG  . ARG A  1 192 ? 25.007  -6.776  -3.029  1.00 11.84 ? 192 ARG A CG  1 
ATOM   1537 C  CD  . ARG A  1 192 ? 25.842  -5.835  -2.161  1.00 11.73 ? 192 ARG A CD  1 
ATOM   1538 N  NE  . ARG A  1 192 ? 26.781  -6.536  -1.290  1.00 11.62 ? 192 ARG A NE  1 
ATOM   1539 C  CZ  . ARG A  1 192 ? 27.943  -7.037  -1.694  1.00 11.95 ? 192 ARG A CZ  1 
ATOM   1540 N  NH1 . ARG A  1 192 ? 28.310  -6.927  -2.963  1.00 14.44 ? 192 ARG A NH1 1 
ATOM   1541 N  NH2 . ARG A  1 192 ? 28.736  -7.657  -0.831  1.00 12.35 ? 192 ARG A NH2 1 
ATOM   1542 N  N   . TYR A  1 193 ? 22.319  -5.265  -1.486  1.00 8.38  ? 193 TYR A N   1 
ATOM   1543 C  CA  . TYR A  1 193 ? 21.513  -4.268  -2.221  1.00 8.86  ? 193 TYR A CA  1 
ATOM   1544 C  C   . TYR A  1 193 ? 22.149  -2.885  -1.910  1.00 9.24  ? 193 TYR A C   1 
ATOM   1545 O  O   . TYR A  1 193 ? 22.837  -2.659  -0.909  1.00 9.67  ? 193 TYR A O   1 
ATOM   1546 C  CB  . TYR A  1 193 ? 19.995  -4.324  -1.888  1.00 9.28  ? 193 TYR A CB  1 
ATOM   1547 C  CG  . TYR A  1 193 ? 19.632  -3.780  -0.527  1.00 8.03  ? 193 TYR A CG  1 
ATOM   1548 C  CD1 . TYR A  1 193 ? 19.846  -4.523  0.625   1.00 8.24  ? 193 TYR A CD1 1 
ATOM   1549 C  CD2 . TYR A  1 193 ? 19.098  -2.511  -0.384  1.00 8.00  ? 193 TYR A CD2 1 
ATOM   1550 C  CE1 . TYR A  1 193 ? 19.519  -4.037  1.888   1.00 7.99  ? 193 TYR A CE1 1 
ATOM   1551 C  CE2 . TYR A  1 193 ? 18.772  -1.995  0.874   1.00 7.94  ? 193 TYR A CE2 1 
ATOM   1552 C  CZ  . TYR A  1 193 ? 19.038  -2.757  2.058   1.00 6.99  ? 193 TYR A CZ  1 
ATOM   1553 O  OH  . TYR A  1 193 ? 18.660  -2.137  3.227   1.00 7.69  ? 193 TYR A OH  1 
ATOM   1554 N  N   . ARG A  1 194 ? 21.734  -1.938  -2.743  1.00 10.00 ? 194 ARG A N   1 
ATOM   1555 C  CA  . ARG A  1 194 ? 22.133  -0.529  -2.525  1.00 9.43  ? 194 ARG A CA  1 
ATOM   1556 C  C   . ARG A  1 194 ? 21.058  0.122   -1.766  1.00 9.95  ? 194 ARG A C   1 
ATOM   1557 O  O   . ARG A  1 194 ? 19.830  0.115   -2.132  1.00 11.83 ? 194 ARG A O   1 
ATOM   1558 C  CB  . ARG A  1 194 ? 22.205  0.168   -3.923  1.00 13.01 ? 194 ARG A CB  1 
ATOM   1559 C  CG  . ARG A  1 194 ? 23.444  -0.340  -4.608  1.00 16.06 ? 194 ARG A CG  1 
ATOM   1560 C  CD  . ARG A  1 194 ? 24.703  0.408   -4.219  1.00 28.37 ? 194 ARG A CD  1 
ATOM   1561 N  NE  . ARG A  1 194 ? 25.888  -0.217  -4.839  1.00 42.93 ? 194 ARG A NE  1 
ATOM   1562 C  CZ  . ARG A  1 194 ? 27.043  0.412   -5.097  1.00 43.18 ? 194 ARG A CZ  1 
ATOM   1563 N  NH1 . ARG A  1 194 ? 27.171  1.713   -4.807  1.00 46.84 ? 194 ARG A NH1 1 
ATOM   1564 N  NH2 . ARG A  1 194 ? 28.068  -0.272  -5.638  1.00 45.62 ? 194 ARG A NH2 1 
ATOM   1565 N  N   . GLY A  1 195 ? 21.437  0.788   -0.690  1.00 8.69  ? 195 GLY A N   1 
ATOM   1566 C  CA  . GLY A  1 195 ? 20.464  1.533   0.130   1.00 9.83  ? 195 GLY A CA  1 
ATOM   1567 C  C   . GLY A  1 195 ? 21.048  2.671   0.843   1.00 8.50  ? 195 GLY A C   1 
ATOM   1568 O  O   . GLY A  1 195 ? 21.883  3.426   0.307   1.00 9.52  ? 195 GLY A O   1 
ATOM   1569 N  N   . SER A  1 196 ? 20.589  2.918   2.057   1.00 7.86  ? 196 SER A N   1 
ATOM   1570 C  CA  . SER A  1 196 ? 21.002  4.119   2.773   1.00 7.46  ? 196 SER A CA  1 
ATOM   1571 C  C   . SER A  1 196 ? 21.418  3.865   4.200   1.00 7.94  ? 196 SER A C   1 
ATOM   1572 O  O   . SER A  1 196 ? 21.254  2.758   4.732   1.00 7.72  ? 196 SER A O   1 
ATOM   1573 C  CB  . SER A  1 196 ? 19.787  5.059   2.817   1.00 8.25  ? 196 SER A CB  1 
ATOM   1574 O  OG  . SER A  1 196 ? 18.828  4.608   3.770   1.00 8.20  ? 196 SER A OG  1 
ATOM   1575 N  N   . LEU A  1 197 ? 21.952  4.916   4.851   1.00 8.03  ? 197 LEU A N   1 
ATOM   1576 C  CA  . LEU A  1 197 ? 22.034  4.826   6.306   1.00 8.76  ? 197 LEU A CA  1 
ATOM   1577 C  C   . LEU A  1 197 ? 20.625  4.606   6.866   1.00 8.73  ? 197 LEU A C   1 
ATOM   1578 O  O   . LEU A  1 197 ? 19.645  5.241   6.348   1.00 8.53  ? 197 LEU A O   1 
ATOM   1579 C  CB  . LEU A  1 197 ? 22.631  6.142   6.917   1.00 10.64 ? 197 LEU A CB  1 
ATOM   1580 C  CG  . LEU A  1 197 ? 24.113  6.427   6.754   1.00 12.44 ? 197 LEU A CG  1 
ATOM   1581 C  CD1 . LEU A  1 197 ? 24.434  6.976   5.355   1.00 13.94 ? 197 LEU A CD1 1 
ATOM   1582 C  CD2 . LEU A  1 197 ? 24.453  7.562   7.717   1.00 12.54 ? 197 LEU A CD2 1 
ATOM   1583 N  N   . THR A  1 198 ? 20.450  3.858   7.933   1.00 8.02  ? 198 THR A N   1 
ATOM   1584 C  CA  . THR A  1 198 ? 19.126  3.708   8.546   1.00 7.89  ? 198 THR A CA  1 
ATOM   1585 C  C   . THR A  1 198 ? 18.848  4.771   9.600   1.00 8.23  ? 198 THR A C   1 
ATOM   1586 O  O   . THR A  1 198 ? 17.796  4.703   10.296  1.00 9.08  ? 198 THR A O   1 
ATOM   1587 C  CB  . THR A  1 198 ? 18.968  2.311   9.181   1.00 7.63  ? 198 THR A CB  1 
ATOM   1588 O  OG1 . THR A  1 198 ? 19.937  2.224   10.267  1.00 8.60  ? 198 THR A OG1 1 
ATOM   1589 C  CG2 . THR A  1 198 ? 19.188  1.242   8.160   1.00 8.20  ? 198 THR A CG2 1 
ATOM   1590 N  N   . THR A  1 199 ? 19.841  5.659   9.869   1.00 8.97  ? 199 THR A N   1 
ATOM   1591 C  CA  . THR A  1 199 ? 19.726  6.736   10.793  1.00 8.74  ? 199 THR A CA  1 
ATOM   1592 C  C   . THR A  1 199 ? 19.999  8.025   10.014  1.00 9.10  ? 199 THR A C   1 
ATOM   1593 O  O   . THR A  1 199 ? 20.698  7.985   9.010   1.00 9.90  ? 199 THR A O   1 
ATOM   1594 C  CB  . THR A  1 199 ? 20.773  6.685   11.926  1.00 10.37 ? 199 THR A CB  1 
ATOM   1595 O  OG1 . THR A  1 199 ? 22.047  6.564   11.335  1.00 13.24 ? 199 THR A OG1 1 
ATOM   1596 C  CG2 . THR A  1 199 ? 20.525  5.387   12.777  1.00 11.49 ? 199 THR A CG2 1 
ATOM   1597 N  N   . PRO A  1 200 ? 19.515  9.143   10.597  1.00 8.97  ? 200 PRO A N   1 
ATOM   1598 C  CA  . PRO A  1 200 ? 19.863  10.460  9.994   1.00 10.49 ? 200 PRO A CA  1 
ATOM   1599 C  C   . PRO A  1 200 ? 21.384  10.562  9.842   1.00 10.67 ? 200 PRO A C   1 
ATOM   1600 O  O   . PRO A  1 200 ? 22.086  10.104  10.767  1.00 13.48 ? 200 PRO A O   1 
ATOM   1601 C  CB  . PRO A  1 200 ? 19.332  11.443  11.034  1.00 9.91  ? 200 PRO A CB  1 
ATOM   1602 C  CG  . PRO A  1 200 ? 18.098  10.777  11.607  1.00 8.11  ? 200 PRO A CG  1 
ATOM   1603 C  CD  . PRO A  1 200 ? 18.571  9.282   11.712  1.00 9.09  ? 200 PRO A CD  1 
ATOM   1604 N  N   . PRO A  1 201 ? 21.843  11.078  8.745   1.00 9.58  ? 201 PRO A N   1 
ATOM   1605 C  CA  . PRO A  1 201 ? 21.069  11.859  7.717   1.00 9.63  ? 201 PRO A CA  1 
ATOM   1606 C  C   . PRO A  1 201 ? 20.437  10.974  6.639   1.00 9.63  ? 201 PRO A C   1 
ATOM   1607 O  O   . PRO A  1 201 ? 19.970  11.547  5.654   1.00 10.76 ? 201 PRO A O   1 
ATOM   1608 C  CB  . PRO A  1 201 ? 22.109  12.826  7.064   1.00 10.52 ? 201 PRO A CB  1 
ATOM   1609 C  CG  . PRO A  1 201 ? 23.294  12.719  7.978   1.00 12.06 ? 201 PRO A CG  1 
ATOM   1610 C  CD  . PRO A  1 201 ? 23.304  11.301  8.595   1.00 10.75 ? 201 PRO A CD  1 
ATOM   1611 N  N   . CYS A  1 202 ? 20.562  9.626   6.708   1.00 9.29  ? 202 CYS A N   1 
ATOM   1612 C  CA  . CYS A  1 202 ? 19.827  8.663   5.769   1.00 8.65  ? 202 CYS A CA  1 
ATOM   1613 C  C   . CYS A  1 202 ? 20.332  8.796   4.361   1.00 9.37  ? 202 CYS A C   1 
ATOM   1614 O  O   . CYS A  1 202 ? 19.656  8.498   3.410   1.00 9.98  ? 202 CYS A O   1 
ATOM   1615 C  CB  . CYS A  1 202 ? 18.269  8.909   5.773   1.00 9.78  ? 202 CYS A CB  1 
ATOM   1616 S  SG  . CYS A  1 202 ? 17.461  8.888   7.344   1.00 9.16  ? 202 CYS A SG  1 
ATOM   1617 N  N   . ASN A  1 203 ? 21.617  9.180   4.180   1.00 10.25 ? 203 ASN A N   1 
ATOM   1618 C  CA  . ASN A  1 203 ? 22.111  9.289   2.785   1.00 10.56 ? 203 ASN A CA  1 
ATOM   1619 C  C   . ASN A  1 203 ? 22.025  7.984   2.023   1.00 9.55  ? 203 ASN A C   1 
ATOM   1620 O  O   . ASN A  1 203 ? 22.346  6.908   2.644   1.00 8.74  ? 203 ASN A O   1 
ATOM   1621 C  CB  . ASN A  1 203 ? 23.587  9.702   2.826   1.00 13.77 ? 203 ASN A CB  1 
ATOM   1622 C  CG  . ASN A  1 203 ? 23.765  10.951  3.647   1.00 13.80 ? 203 ASN A CG  1 
ATOM   1623 O  OD1 . ASN A  1 203 ? 23.855  10.865  4.859   1.00 16.40 ? 203 ASN A OD1 1 
ATOM   1624 N  ND2 . ASN A  1 203 ? 23.643  12.145  2.953   1.00 18.33 ? 203 ASN A ND2 1 
ATOM   1625 N  N   . PRO A  1 204 ? 21.696  7.983   0.734   1.00 9.73  ? 204 PRO A N   1 
ATOM   1626 C  CA  . PRO A  1 204 ? 21.503  6.742   -0.052  1.00 10.08 ? 204 PRO A CA  1 
ATOM   1627 C  C   . PRO A  1 204 ? 22.858  6.312   -0.644  1.00 9.80  ? 204 PRO A C   1 
ATOM   1628 O  O   . PRO A  1 204 ? 23.029  6.212   -1.839  1.00 12.49 ? 204 PRO A O   1 
ATOM   1629 C  CB  . PRO A  1 204 ? 20.529  7.203   -1.137  1.00 10.10 ? 204 PRO A CB  1 
ATOM   1630 C  CG  . PRO A  1 204 ? 20.901  8.661   -1.378  1.00 10.42 ? 204 PRO A CG  1 
ATOM   1631 C  CD  . PRO A  1 204 ? 21.222  9.234   -0.003  1.00 10.09 ? 204 PRO A CD  1 
ATOM   1632 N  N   . THR A  1 205 ? 23.803  6.049   0.274   1.00 9.95  ? 205 THR A N   1 
ATOM   1633 C  CA  . THR A  1 205 ? 25.168  5.875   -0.214  1.00 10.04 ? 205 THR A CA  1 
ATOM   1634 C  C   . THR A  1 205 ? 25.756  4.579   0.363   1.00 10.89 ? 205 THR A C   1 
ATOM   1635 O  O   . THR A  1 205 ? 26.986  4.413   0.404   1.00 10.43 ? 205 THR A O   1 
ATOM   1636 C  CB  . THR A  1 205 ? 26.043  6.991   0.406   1.00 10.00 ? 205 THR A CB  1 
ATOM   1637 O  OG1 . THR A  1 205 ? 25.831  7.085   1.811   1.00 10.86 ? 205 THR A OG1 1 
ATOM   1638 C  CG2 . THR A  1 205 ? 25.671  8.391   -0.247  1.00 10.76 ? 205 THR A CG2 1 
ATOM   1639 N  N   . VAL A  1 206 ? 24.892  3.654   0.843   1.00 9.11  ? 206 VAL A N   1 
ATOM   1640 C  CA  . VAL A  1 206 ? 25.398  2.407   1.487   1.00 9.19  ? 206 VAL A CA  1 
ATOM   1641 C  C   . VAL A  1 206 ? 25.194  1.192   0.674   1.00 8.74  ? 206 VAL A C   1 
ATOM   1642 O  O   . VAL A  1 206 ? 24.080  0.917   0.202   1.00 10.83 ? 206 VAL A O   1 
ATOM   1643 C  CB  . VAL A  1 206 ? 24.628  2.183   2.851   1.00 9.03  ? 206 VAL A CB  1 
ATOM   1644 C  CG1 . VAL A  1 206 ? 25.090  0.846   3.476   1.00 9.18  ? 206 VAL A CG1 1 
ATOM   1645 C  CG2 . VAL A  1 206 ? 24.859  3.336   3.864   1.00 8.05  ? 206 VAL A CG2 1 
ATOM   1646 N  N   . LEU A  1 207 ? 26.252  0.453   0.450   1.00 8.33  ? 207 LEU A N   1 
ATOM   1647 C  CA  . LEU A  1 207 ? 26.221  -0.876  -0.116  1.00 8.80  ? 207 LEU A CA  1 
ATOM   1648 C  C   . LEU A  1 207 ? 26.028  -1.812  1.049   1.00 8.54  ? 207 LEU A C   1 
ATOM   1649 O  O   . LEU A  1 207 ? 26.892  -1.999  1.947   1.00 9.58  ? 207 LEU A O   1 
ATOM   1650 C  CB  . LEU A  1 207 ? 27.518  -1.188  -0.856  1.00 10.19 ? 207 LEU A CB  1 
ATOM   1651 C  CG  . LEU A  1 207 ? 27.344  -2.504  -1.628  1.00 12.43 ? 207 LEU A CG  1 
ATOM   1652 C  CD1 . LEU A  1 207 ? 26.328  -2.217  -2.792  1.00 15.73 ? 207 LEU A CD1 1 
ATOM   1653 C  CD2 . LEU A  1 207 ? 28.668  -2.984  -2.213  1.00 16.86 ? 207 LEU A CD2 1 
ATOM   1654 N  N   . TRP A  1 208 ? 24.822  -2.383  1.116   1.00 8.42  ? 208 TRP A N   1 
ATOM   1655 C  CA  . TRP A  1 208 ? 24.454  -3.307  2.208   1.00 8.05  ? 208 TRP A CA  1 
ATOM   1656 C  C   . TRP A  1 208 ? 24.852  -4.728  1.919   1.00 8.06  ? 208 TRP A C   1 
ATOM   1657 O  O   . TRP A  1 208 ? 24.597  -5.257  0.825   1.00 9.02  ? 208 TRP A O   1 
ATOM   1658 C  CB  . TRP A  1 208 ? 22.887  -3.260  2.420   1.00 8.62  ? 208 TRP A CB  1 
ATOM   1659 C  CG  . TRP A  1 208 ? 22.542  -2.101  3.246   1.00 7.37  ? 208 TRP A CG  1 
ATOM   1660 C  CD1 . TRP A  1 208 ? 22.050  -0.892  2.820   1.00 7.25  ? 208 TRP A CD1 1 
ATOM   1661 C  CD2 . TRP A  1 208 ? 22.656  -1.923  4.707   1.00 7.17  ? 208 TRP A CD2 1 
ATOM   1662 N  NE1 . TRP A  1 208 ? 21.919  0.012   3.827   1.00 7.76  ? 208 TRP A NE1 1 
ATOM   1663 C  CE2 . TRP A  1 208 ? 22.227  -0.593  5.033   1.00 7.50  ? 208 TRP A CE2 1 
ATOM   1664 C  CE3 . TRP A  1 208 ? 23.055  -2.761  5.754   1.00 8.38  ? 208 TRP A CE3 1 
ATOM   1665 C  CZ2 . TRP A  1 208 ? 22.244  -0.089  6.340   1.00 7.72  ? 208 TRP A CZ2 1 
ATOM   1666 C  CZ3 . TRP A  1 208 ? 23.011  -2.278  7.049   1.00 8.23  ? 208 TRP A CZ3 1 
ATOM   1667 C  CH2 . TRP A  1 208 ? 22.674  -0.926  7.351   1.00 8.51  ? 208 TRP A CH2 1 
ATOM   1668 N  N   . THR A  1 209 ? 25.421  -5.430  2.913   1.00 7.52  ? 209 THR A N   1 
ATOM   1669 C  CA  . THR A  1 209 ? 25.651  -6.873  2.911   1.00 8.07  ? 209 THR A CA  1 
ATOM   1670 C  C   . THR A  1 209 ? 24.969  -7.385  4.189   1.00 8.43  ? 209 THR A C   1 
ATOM   1671 O  O   . THR A  1 209 ? 25.472  -7.064  5.278   1.00 7.91  ? 209 THR A O   1 
ATOM   1672 C  CB  . THR A  1 209 ? 27.167  -7.225  2.894   1.00 7.84  ? 209 THR A CB  1 
ATOM   1673 O  OG1 . THR A  1 209 ? 27.717  -6.650  1.674   1.00 8.35  ? 209 THR A OG1 1 
ATOM   1674 C  CG2 . THR A  1 209 ? 27.397  -8.712  2.977   1.00 10.01 ? 209 THR A CG2 1 
ATOM   1675 N  N   . VAL A  1 210 ? 23.872  -8.141  4.045   1.00 7.34  ? 210 VAL A N   1 
ATOM   1676 C  CA  . VAL A  1 210 ? 23.199  -8.713  5.235   1.00 8.12  ? 210 VAL A CA  1 
ATOM   1677 C  C   . VAL A  1 210 ? 23.484  -10.199 5.150   1.00 7.20  ? 210 VAL A C   1 
ATOM   1678 O  O   . VAL A  1 210 ? 23.110  -10.852 4.203   1.00 9.31  ? 210 VAL A O   1 
ATOM   1679 C  CB  . VAL A  1 210 ? 21.702  -8.400  5.207   1.00 8.39  ? 210 VAL A CB  1 
ATOM   1680 C  CG1 . VAL A  1 210 ? 21.076  -9.000  6.497   1.00 8.93  ? 210 VAL A CG1 1 
ATOM   1681 C  CG2 . VAL A  1 210 ? 21.472  -6.908  5.037   1.00 9.42  ? 210 VAL A CG2 1 
ATOM   1682 N  N   . PHE A  1 211 ? 24.153  -10.722 6.176   1.00 7.51  ? 211 PHE A N   1 
ATOM   1683 C  CA  . PHE A  1 211 ? 24.483  -12.169 6.124   1.00 8.60  ? 211 PHE A CA  1 
ATOM   1684 C  C   . PHE A  1 211 ? 23.216  -12.976 6.257   1.00 8.89  ? 211 PHE A C   1 
ATOM   1685 O  O   . PHE A  1 211 ? 22.264  -12.625 7.028   1.00 9.78  ? 211 PHE A O   1 
ATOM   1686 C  CB  . PHE A  1 211 ? 25.525  -12.493 7.212   1.00 8.20  ? 211 PHE A CB  1 
ATOM   1687 C  CG  . PHE A  1 211 ? 26.831  -11.836 6.952   1.00 7.82  ? 211 PHE A CG  1 
ATOM   1688 C  CD1 . PHE A  1 211 ? 27.611  -12.288 5.904   1.00 8.94  ? 211 PHE A CD1 1 
ATOM   1689 C  CD2 . PHE A  1 211 ? 27.325  -10.806 7.788   1.00 8.61  ? 211 PHE A CD2 1 
ATOM   1690 C  CE1 . PHE A  1 211 ? 28.846  -11.679 5.552   1.00 11.25 ? 211 PHE A CE1 1 
ATOM   1691 C  CE2 . PHE A  1 211 ? 28.576  -10.209 7.451   1.00 9.16  ? 211 PHE A CE2 1 
ATOM   1692 C  CZ  . PHE A  1 211 ? 29.302  -10.654 6.325   1.00 9.95  ? 211 PHE A CZ  1 
ATOM   1693 N  N   . ARG A  1 212 ? 23.191  -14.069 5.503   1.00 8.75  ? 212 ARG A N   1 
ATOM   1694 C  CA  . ARG A  1 212 ? 22.011  -14.937 5.535   1.00 9.78  ? 212 ARG A CA  1 
ATOM   1695 C  C   . ARG A  1 212 ? 21.699  -15.507 6.904   1.00 10.27 ? 212 ARG A C   1 
ATOM   1696 O  O   . ARG A  1 212 ? 20.513  -15.544 7.292   1.00 11.11 ? 212 ARG A O   1 
ATOM   1697 C  CB  . ARG A  1 212 ? 22.204  -16.058 4.522   1.00 11.14 ? 212 ARG A CB  1 
ATOM   1698 C  CG  . ARG A  1 212 ? 20.949  -16.946 4.345   1.00 12.56 ? 212 ARG A CG  1 
ATOM   1699 C  CD  . ARG A  1 212 ? 21.397  -18.276 3.691   1.00 16.82 ? 212 ARG A CD  1 
ATOM   1700 N  NE  . ARG A  1 212 ? 20.254  -19.153 3.451   1.00 23.21 ? 212 ARG A NE  1 
ATOM   1701 C  CZ  . ARG A  1 212 ? 19.853  -20.105 4.288   1.00 30.17 ? 212 ARG A CZ  1 
ATOM   1702 N  NH1 . ARG A  1 212 ? 20.504  -20.311 5.424   1.00 27.49 ? 212 ARG A NH1 1 
ATOM   1703 N  NH2 . ARG A  1 212 ? 18.801  -20.852 3.988   1.00 30.08 ? 212 ARG A NH2 1 
ATOM   1704 N  N   . ASN A  1 213 ? 22.744  -15.962 7.620   1.00 9.81  ? 213 ASN A N   1 
ATOM   1705 C  CA  . ASN A  1 213 ? 22.535  -16.738 8.855   1.00 11.39 ? 213 ASN A CA  1 
ATOM   1706 C  C   . ASN A  1 213 ? 22.664  -15.795 10.040  1.00 11.15 ? 213 ASN A C   1 
ATOM   1707 O  O   . ASN A  1 213 ? 23.621  -14.964 10.124  1.00 10.87 ? 213 ASN A O   1 
ATOM   1708 C  CB  . ASN A  1 213 ? 23.631  -17.839 8.897   1.00 11.72 ? 213 ASN A CB  1 
ATOM   1709 C  CG  . ASN A  1 213 ? 23.511  -18.708 7.653   1.00 14.21 ? 213 ASN A CG  1 
ATOM   1710 O  OD1 . ASN A  1 213 ? 24.501  -18.896 6.904   1.00 17.95 ? 213 ASN A OD1 1 
ATOM   1711 N  ND2 . ASN A  1 213 ? 22.293  -19.058 7.310   1.00 14.08 ? 213 ASN A ND2 1 
ATOM   1712 N  N   . PRO A  1 214 ? 21.804  -15.986 11.049  1.00 10.73 ? 214 PRO A N   1 
ATOM   1713 C  CA  . PRO A  1 214 ? 21.932  -15.168 12.200  1.00 11.17 ? 214 PRO A CA  1 
ATOM   1714 C  C   . PRO A  1 214 ? 23.039  -15.728 13.182  1.00 11.26 ? 214 PRO A C   1 
ATOM   1715 O  O   . PRO A  1 214 ? 23.438  -16.935 13.056  1.00 13.27 ? 214 PRO A O   1 
ATOM   1716 C  CB  . PRO A  1 214 ? 20.545  -15.331 12.910  1.00 12.29 ? 214 PRO A CB  1 
ATOM   1717 C  CG  . PRO A  1 214 ? 20.197  -16.740 12.548  1.00 13.56 ? 214 PRO A CG  1 
ATOM   1718 C  CD  . PRO A  1 214 ? 20.602  -16.813 11.063  1.00 13.20 ? 214 PRO A CD  1 
ATOM   1719 N  N   . VAL A  1 215 ? 23.411  -14.929 14.142  1.00 10.67 ? 215 VAL A N   1 
ATOM   1720 C  CA  . VAL A  1 215 ? 24.149  -15.397 15.344  1.00 11.29 ? 215 VAL A CA  1 
ATOM   1721 C  C   . VAL A  1 215 ? 23.184  -15.534 16.516  1.00 11.83 ? 215 VAL A C   1 
ATOM   1722 O  O   . VAL A  1 215 ? 22.072  -15.013 16.464  1.00 12.23 ? 215 VAL A O   1 
ATOM   1723 C  CB  . VAL A  1 215 ? 25.309  -14.501 15.761  1.00 11.96 ? 215 VAL A CB  1 
ATOM   1724 C  CG1 . VAL A  1 215 ? 26.351  -14.373 14.608  1.00 12.02 ? 215 VAL A CG1 1 
ATOM   1725 C  CG2 . VAL A  1 215 ? 24.821  -13.119 16.159  1.00 11.39 ? 215 VAL A CG2 1 
ATOM   1726 N  N   . GLN A  1 216 ? 23.660  -16.204 17.554  1.00 12.09 ? 216 GLN A N   1 
ATOM   1727 C  CA  . GLN A  1 216 ? 22.907  -16.348 18.851  1.00 12.21 ? 216 GLN A CA  1 
ATOM   1728 C  C   . GLN A  1 216 ? 23.564  -15.710 19.968  1.00 15.08 ? 216 GLN A C   1 
ATOM   1729 O  O   . GLN A  1 216 ? 24.816  -15.774 20.105  1.00 15.14 ? 216 GLN A O   1 
ATOM   1730 C  CB  . GLN A  1 216 ? 22.666  -17.859 19.195  1.00 14.62 ? 216 GLN A CB  1 
ATOM   1731 C  CG  . GLN A  1 216 ? 21.820  -18.524 18.186  1.00 16.31 ? 216 GLN A CG  1 
ATOM   1732 C  CD  . GLN A  1 216 ? 21.414  -19.913 18.571  1.00 26.39 ? 216 GLN A CD  1 
ATOM   1733 O  OE1 . GLN A  1 216 ? 21.929  -20.510 19.555  1.00 28.77 ? 216 GLN A OE1 1 
ATOM   1734 N  NE2 . GLN A  1 216 ? 20.466  -20.444 17.798  1.00 28.09 ? 216 GLN A NE2 1 
ATOM   1735 N  N   . ILE A  1 217 ? 22.770  -15.043 20.826  1.00 10.35 ? 217 ILE A N   1 
ATOM   1736 C  CA  . ILE A  1 217 ? 23.221  -14.587 22.121  1.00 11.84 ? 217 ILE A CA  1 
ATOM   1737 C  C   . ILE A  1 217 ? 22.221  -15.100 23.172  1.00 12.47 ? 217 ILE A C   1 
ATOM   1738 O  O   . ILE A  1 217 ? 21.118  -15.415 22.778  1.00 12.92 ? 217 ILE A O   1 
ATOM   1739 C  CB  . ILE A  1 217 ? 23.381  -13.033 22.169  1.00 11.42 ? 217 ILE A CB  1 
ATOM   1740 C  CG1 . ILE A  1 217 ? 21.980  -12.237 21.981  1.00 13.41 ? 217 ILE A CG1 1 
ATOM   1741 C  CG2 . ILE A  1 217 ? 24.420  -12.515 21.111  1.00 12.50 ? 217 ILE A CG2 1 
ATOM   1742 C  CD1 . ILE A  1 217 ? 22.088  -10.747 22.242  1.00 13.21 ? 217 ILE A CD1 1 
ATOM   1743 N  N   . SER A  1 218 ? 22.650  -15.184 24.446  1.00 13.61 ? 218 SER A N   1 
ATOM   1744 C  CA  . SER A  1 218 ? 21.675  -15.780 25.389  1.00 14.40 ? 218 SER A CA  1 
ATOM   1745 C  C   . SER A  1 218 ? 20.554  -14.825 25.746  1.00 15.19 ? 218 SER A C   1 
ATOM   1746 O  O   . SER A  1 218 ? 20.615  -13.626 25.481  1.00 13.20 ? 218 SER A O   1 
ATOM   1747 C  CB  . SER A  1 218 ? 22.336  -16.120 26.694  1.00 14.32 ? 218 SER A CB  1 
ATOM   1748 O  OG  . SER A  1 218 ? 22.869  -14.964 27.343  1.00 13.31 ? 218 SER A OG  1 
ATOM   1749 N  N   . GLN A  1 219 ? 19.507  -15.405 26.330  1.00 15.32 ? 219 GLN A N   1 
ATOM   1750 C  CA  . GLN A  1 219 ? 18.406  -14.505 26.838  1.00 16.25 ? 219 GLN A CA  1 
ATOM   1751 C  C   . GLN A  1 219 ? 18.939  -13.463 27.788  1.00 15.29 ? 219 GLN A C   1 
ATOM   1752 O  O   . GLN A  1 219 ? 18.489  -12.350 27.771  1.00 14.25 ? 219 GLN A O   1 
ATOM   1753 C  CB  . GLN A  1 219 ? 17.302  -15.355 27.454  1.00 23.28 ? 219 GLN A CB  1 
ATOM   1754 C  CG  . GLN A  1 219 ? 17.642  -16.173 28.655  1.00 24.84 ? 219 GLN A CG  1 
ATOM   1755 C  CD  . GLN A  1 219 ? 16.331  -16.737 29.179  1.00 33.47 ? 219 GLN A CD  1 
ATOM   1756 O  OE1 . GLN A  1 219 ? 15.762  -17.639 28.544  1.00 36.80 ? 219 GLN A OE1 1 
ATOM   1757 N  NE2 . GLN A  1 219 ? 15.787  -16.136 30.286  1.00 34.42 ? 219 GLN A NE2 1 
ATOM   1758 N  N   . GLU A  1 220 ? 19.914  -13.779 28.619  1.00 14.56 ? 220 GLU A N   1 
ATOM   1759 C  CA  . GLU A  1 220 ? 20.406  -12.841 29.555  1.00 14.42 ? 220 GLU A CA  1 
ATOM   1760 C  C   . GLU A  1 220 ? 21.266  -11.745 28.857  1.00 14.63 ? 220 GLU A C   1 
ATOM   1761 O  O   . GLU A  1 220 ? 21.236  -10.568 29.248  1.00 13.41 ? 220 GLU A O   1 
ATOM   1762 C  CB  . GLU A  1 220 ? 21.313  -13.492 30.617  1.00 16.18 ? 220 GLU A CB  1 
ATOM   1763 C  CG  . GLU A  1 220 ? 20.550  -14.512 31.513  1.00 18.70 ? 220 GLU A CG  1 
ATOM   1764 C  CD  . GLU A  1 220 ? 20.296  -15.925 30.913  1.00 23.77 ? 220 GLU A CD  1 
ATOM   1765 O  OE1 . GLU A  1 220 ? 20.778  -16.346 29.801  1.00 21.76 ? 220 GLU A OE1 1 
ATOM   1766 O  OE2 . GLU A  1 220 ? 19.473  -16.624 31.565  1.00 31.12 ? 220 GLU A OE2 1 
ATOM   1767 N  N   . GLN A  1 221 ? 22.032  -12.140 27.821  1.00 13.32 ? 221 GLN A N   1 
ATOM   1768 C  CA  . GLN A  1 221 ? 22.762  -11.115 27.038  1.00 12.44 ? 221 GLN A CA  1 
ATOM   1769 C  C   . GLN A  1 221 ? 21.785  -10.128 26.316  1.00 11.89 ? 221 GLN A C   1 
ATOM   1770 O  O   . GLN A  1 221 ? 22.053  -8.937  26.353  1.00 12.45 ? 221 GLN A O   1 
ATOM   1771 C  CB  . GLN A  1 221 ? 23.587  -11.789 25.957  1.00 12.09 ? 221 GLN A CB  1 
ATOM   1772 C  CG  . GLN A  1 221 ? 24.829  -12.481 26.588  1.00 13.75 ? 221 GLN A CG  1 
ATOM   1773 C  CD  . GLN A  1 221 ? 25.668  -13.177 25.552  1.00 11.96 ? 221 GLN A CD  1 
ATOM   1774 O  OE1 . GLN A  1 221 ? 25.293  -14.078 24.888  1.00 14.27 ? 221 GLN A OE1 1 
ATOM   1775 N  NE2 . GLN A  1 221 ? 26.909  -12.693 25.446  1.00 14.90 ? 221 GLN A NE2 1 
ATOM   1776 N  N   . LEU A  1 222 ? 20.734  -10.708 25.755  1.00 11.48 ? 222 LEU A N   1 
ATOM   1777 C  CA  . LEU A  1 222 ? 19.792  -9.876  25.023  1.00 12.10 ? 222 LEU A CA  1 
ATOM   1778 C  C   . LEU A  1 222 ? 19.109  -8.920  26.002  1.00 11.73 ? 222 LEU A C   1 
ATOM   1779 O  O   . LEU A  1 222 ? 18.896  -7.748  25.761  1.00 11.20 ? 222 LEU A O   1 
ATOM   1780 C  CB  . LEU A  1 222 ? 18.782  -10.724 24.282  1.00 11.22 ? 222 LEU A CB  1 
ATOM   1781 C  CG  . LEU A  1 222 ? 17.645  -9.976  23.619  1.00 12.52 ? 222 LEU A CG  1 
ATOM   1782 C  CD1 . LEU A  1 222 ? 18.218  -9.032  22.496  1.00 12.11 ? 222 LEU A CD1 1 
ATOM   1783 C  CD2 . LEU A  1 222 ? 16.644  -10.953 23.009  1.00 11.98 ? 222 LEU A CD2 1 
ATOM   1784 N  N   . LEU A  1 223 ? 18.690  -9.467  27.186  1.00 11.24 ? 223 LEU A N   1 
ATOM   1785 C  CA  . LEU A  1 223 ? 18.083  -8.560  28.198  1.00 13.01 ? 223 LEU A CA  1 
ATOM   1786 C  C   . LEU A  1 223 ? 19.035  -7.457  28.663  1.00 12.48 ? 223 LEU A C   1 
ATOM   1787 O  O   . LEU A  1 223 ? 18.597  -6.347  28.860  1.00 14.62 ? 223 LEU A O   1 
ATOM   1788 C  CB  . LEU A  1 223 ? 17.703  -9.415  29.413  1.00 14.14 ? 223 LEU A CB  1 
ATOM   1789 C  CG  . LEU A  1 223 ? 17.000  -8.681  30.529  1.00 15.39 ? 223 LEU A CG  1 
ATOM   1790 C  CD1 . LEU A  1 223 ? 15.633  -8.159  29.990  1.00 15.10 ? 223 LEU A CD1 1 
ATOM   1791 C  CD2 . LEU A  1 223 ? 16.799  -9.700  31.690  1.00 18.51 ? 223 LEU A CD2 1 
ATOM   1792 N  N   . ALA A  1 224 ? 20.339  -7.766  28.847  1.00 12.30 ? 224 ALA A N   1 
ATOM   1793 C  CA  . ALA A  1 224 ? 21.283  -6.778  29.212  1.00 12.97 ? 224 ALA A CA  1 
ATOM   1794 C  C   . ALA A  1 224 ? 21.395  -5.673  28.152  1.00 13.99 ? 224 ALA A C   1 
ATOM   1795 O  O   . ALA A  1 224 ? 21.375  -4.512  28.486  1.00 13.64 ? 224 ALA A O   1 
ATOM   1796 C  CB  . ALA A  1 224 ? 22.688  -7.437  29.447  1.00 14.45 ? 224 ALA A CB  1 
ATOM   1797 N  N   . LEU A  1 225 ? 21.483  -6.065  26.894  1.00 12.09 ? 225 LEU A N   1 
ATOM   1798 C  CA  . LEU A  1 225 ? 21.535  -5.034  25.836  1.00 13.88 ? 225 LEU A CA  1 
ATOM   1799 C  C   . LEU A  1 225 ? 20.270  -4.112  25.831  1.00 14.44 ? 225 LEU A C   1 
ATOM   1800 O  O   . LEU A  1 225 ? 20.400  -2.869  25.677  1.00 16.26 ? 225 LEU A O   1 
ATOM   1801 C  CB  . LEU A  1 225 ? 21.657  -5.773  24.489  1.00 12.29 ? 225 LEU A CB  1 
ATOM   1802 C  CG  . LEU A  1 225 ? 21.729  -4.822  23.286  1.00 11.78 ? 225 LEU A CG  1 
ATOM   1803 C  CD1 . LEU A  1 225 ? 22.980  -3.934  23.332  1.00 11.78 ? 225 LEU A CD1 1 
ATOM   1804 C  CD2 . LEU A  1 225 ? 21.653  -5.682  22.055  1.00 12.01 ? 225 LEU A CD2 1 
ATOM   1805 N  N   . GLU A  1 226 ? 19.089  -4.736  26.077  1.00 12.66 ? 226 GLU A N   1 
ATOM   1806 C  CA  . GLU A  1 226 ? 17.823  -3.964  26.097  1.00 12.14 ? 226 GLU A CA  1 
ATOM   1807 C  C   . GLU A  1 226 ? 17.628  -3.076  27.288  1.00 14.32 ? 226 GLU A C   1 
ATOM   1808 O  O   . GLU A  1 226 ? 16.810  -2.220  27.248  1.00 14.32 ? 226 GLU A O   1 
ATOM   1809 C  CB  . GLU A  1 226 ? 16.666  -4.949  26.044  1.00 12.54 ? 226 GLU A CB  1 
ATOM   1810 C  CG  . GLU A  1 226 ? 16.571  -5.737  24.740  1.00 11.89 ? 226 GLU A CG  1 
ATOM   1811 C  CD  . GLU A  1 226 ? 15.639  -6.884  24.788  1.00 13.71 ? 226 GLU A CD  1 
ATOM   1812 O  OE1 . GLU A  1 226 ? 15.395  -7.439  25.938  1.00 13.21 ? 226 GLU A OE1 1 
ATOM   1813 O  OE2 . GLU A  1 226 ? 15.160  -7.390  23.786  1.00 14.38 ? 226 GLU A OE2 1 
ATOM   1814 N  N   . THR A  1 227 ? 18.329  -3.341  28.396  1.00 12.94 ? 227 THR A N   1 
ATOM   1815 C  CA  . THR A  1 227 ? 18.029  -2.717  29.703  1.00 14.72 ? 227 THR A CA  1 
ATOM   1816 C  C   . THR A  1 227 ? 19.208  -1.958  30.233  1.00 16.84 ? 227 THR A C   1 
ATOM   1817 O  O   . THR A  1 227 ? 19.009  -1.208  31.191  1.00 18.44 ? 227 THR A O   1 
ATOM   1818 C  CB  . THR A  1 227 ? 17.585  -3.709  30.784  1.00 16.15 ? 227 THR A CB  1 
ATOM   1819 O  OG1 . THR A  1 227 ? 18.589  -4.695  31.031  1.00 15.19 ? 227 THR A OG1 1 
ATOM   1820 C  CG2 . THR A  1 227 ? 16.287  -4.383  30.384  1.00 17.19 ? 227 THR A CG2 1 
ATOM   1821 N  N   . ALA A  1 228 ? 20.388  -2.021  29.614  1.00 14.60 ? 228 ALA A N   1 
ATOM   1822 C  CA  . ALA A  1 228 ? 21.581  -1.420  30.240  1.00 18.38 ? 228 ALA A CA  1 
ATOM   1823 C  C   . ALA A  1 228 ? 21.694  0.042   29.966  1.00 17.43 ? 228 ALA A C   1 
ATOM   1824 O  O   . ALA A  1 228 ? 22.361  0.791   30.765  1.00 17.64 ? 228 ALA A O   1 
ATOM   1825 C  CB  . ALA A  1 228 ? 22.840  -2.232  29.836  1.00 20.32 ? 228 ALA A CB  1 
ATOM   1826 N  N   . LEU A  1 229 ? 21.057  0.512   28.883  1.00 13.95 ? 229 LEU A N   1 
ATOM   1827 C  CA  . LEU A  1 229 ? 21.364  1.848   28.421  1.00 14.91 ? 229 LEU A CA  1 
ATOM   1828 C  C   . LEU A  1 229 ? 20.226  2.823   28.422  1.00 15.20 ? 229 LEU A C   1 
ATOM   1829 O  O   . LEU A  1 229 ? 19.072  2.442   28.250  1.00 14.22 ? 229 LEU A O   1 
ATOM   1830 C  CB  . LEU A  1 229 ? 21.995  1.790   27.035  1.00 14.01 ? 229 LEU A CB  1 
ATOM   1831 C  CG  . LEU A  1 229 ? 23.065  0.705   26.767  1.00 16.49 ? 229 LEU A CG  1 
ATOM   1832 C  CD1 . LEU A  1 229 ? 23.470  0.743   25.259  1.00 18.47 ? 229 LEU A CD1 1 
ATOM   1833 C  CD2 . LEU A  1 229 ? 24.317  0.885   27.666  1.00 16.66 ? 229 LEU A CD2 1 
ATOM   1834 N  N   . TYR A  1 230 ? 20.571  4.068   28.620  1.00 13.94 ? 230 TYR A N   1 
ATOM   1835 C  CA  . TYR A  1 230 ? 19.715  5.253   28.443  1.00 15.60 ? 230 TYR A CA  1 
ATOM   1836 C  C   . TYR A  1 230 ? 20.168  6.162   27.297  1.00 15.76 ? 230 TYR A C   1 
ATOM   1837 O  O   . TYR A  1 230 ? 21.358  6.283   26.993  1.00 15.25 ? 230 TYR A O   1 
ATOM   1838 C  CB  . TYR A  1 230 ? 19.666  6.141   29.705  1.00 18.92 ? 230 TYR A CB  1 
ATOM   1839 C  CG  . TYR A  1 230 ? 19.014  5.451   30.873  1.00 23.79 ? 230 TYR A CG  1 
ATOM   1840 C  CD1 . TYR A  1 230 ? 19.722  4.488   31.618  1.00 26.80 ? 230 TYR A CD1 1 
ATOM   1841 C  CD2 . TYR A  1 230 ? 17.735  5.781   31.266  1.00 26.03 ? 230 TYR A CD2 1 
ATOM   1842 C  CE1 . TYR A  1 230 ? 19.120  3.864   32.732  1.00 35.38 ? 230 TYR A CE1 1 
ATOM   1843 C  CE2 . TYR A  1 230 ? 17.141  5.153   32.373  1.00 28.99 ? 230 TYR A CE2 1 
ATOM   1844 C  CZ  . TYR A  1 230 ? 17.838  4.216   33.090  1.00 32.47 ? 230 TYR A CZ  1 
ATOM   1845 O  OH  . TYR A  1 230 ? 17.250  3.588   34.187  1.00 39.61 ? 230 TYR A OH  1 
ATOM   1846 N  N   A CYS A  1 231 ? 19.190  6.875   26.716  0.50 15.14 ? 231 CYS A N   1 
ATOM   1847 N  N   B CYS A  1 231 ? 19.194  6.860   26.724  0.50 17.73 ? 231 CYS A N   1 
ATOM   1848 C  CA  A CYS A  1 231 ? 19.406  7.824   25.625  0.50 15.43 ? 231 CYS A CA  1 
ATOM   1849 C  CA  B CYS A  1 231 ? 19.457  7.747   25.628  0.50 19.75 ? 231 CYS A CA  1 
ATOM   1850 C  C   A CYS A  1 231 ? 19.951  9.115   26.179  0.50 15.10 ? 231 CYS A C   1 
ATOM   1851 C  C   B CYS A  1 231 ? 19.635  9.180   26.117  0.50 17.87 ? 231 CYS A C   1 
ATOM   1852 O  O   A CYS A  1 231 ? 20.650  9.876   25.507  0.50 14.69 ? 231 CYS A O   1 
ATOM   1853 O  O   B CYS A  1 231 ? 19.841  10.112  25.324  0.50 17.45 ? 231 CYS A O   1 
ATOM   1854 C  CB  A CYS A  1 231 ? 18.086  8.146   24.871  0.50 13.20 ? 231 CYS A CB  1 
ATOM   1855 C  CB  B CYS A  1 231 ? 18.373  7.617   24.543  0.50 21.39 ? 231 CYS A CB  1 
ATOM   1856 S  SG  A CYS A  1 231 ? 17.523  6.786   23.813  0.50 11.44 ? 231 CYS A SG  1 
ATOM   1857 S  SG  B CYS A  1 231 ? 16.647  7.782   25.032  0.50 27.67 ? 231 CYS A SG  1 
ATOM   1858 N  N   . THR A  1 232 ? 19.607  9.332   27.443  1.00 16.64 ? 232 THR A N   1 
ATOM   1859 C  CA  . THR A  1 232 ? 19.757  10.625  28.085  1.00 18.62 ? 232 THR A CA  1 
ATOM   1860 C  C   . THR A  1 232 ? 21.057  10.731  28.917  1.00 18.50 ? 232 THR A C   1 
ATOM   1861 O  O   . THR A  1 232 ? 21.681  9.719   29.281  1.00 18.11 ? 232 THR A O   1 
ATOM   1862 C  CB  . THR A  1 232 ? 18.522  10.883  28.959  1.00 18.32 ? 232 THR A CB  1 
ATOM   1863 O  OG1 . THR A  1 232 ? 18.208  9.689   29.685  1.00 18.74 ? 232 THR A OG1 1 
ATOM   1864 C  CG2 . THR A  1 232 ? 17.349  11.288  28.100  1.00 20.79 ? 232 THR A CG2 1 
ATOM   1865 N  N   . HIS A  1 233 ? 21.511  11.976  29.198  1.00 19.68 ? 233 HIS A N   1 
ATOM   1866 C  CA  . HIS A  1 233 ? 22.700  12.155  30.062  1.00 21.55 ? 233 HIS A CA  1 
ATOM   1867 C  C   . HIS A  1 233 ? 22.356  11.799  31.494  1.00 22.14 ? 233 HIS A C   1 
ATOM   1868 O  O   . HIS A  1 233 ? 21.179  11.812  31.923  1.00 22.28 ? 233 HIS A O   1 
ATOM   1869 C  CB  . HIS A  1 233 ? 23.151  13.636  30.065  1.00 21.88 ? 233 HIS A CB  1 
ATOM   1870 C  CG  . HIS A  1 233 ? 23.788  14.056  28.754  1.00 28.07 ? 233 HIS A CG  1 
ATOM   1871 N  ND1 . HIS A  1 233 ? 23.129  14.807  27.830  1.00 32.60 ? 233 HIS A ND1 1 
ATOM   1872 C  CD2 . HIS A  1 233 ? 25.041  13.761  28.201  1.00 30.07 ? 233 HIS A CD2 1 
ATOM   1873 C  CE1 . HIS A  1 233 ? 23.925  14.988  26.754  1.00 31.32 ? 233 HIS A CE1 1 
ATOM   1874 N  NE2 . HIS A  1 233 ? 25.076  14.337  26.960  1.00 28.35 ? 233 HIS A NE2 1 
ATOM   1875 N  N   . MET A  1 234 ? 23.380  11.421  32.243  1.00 21.09 ? 234 MET A N   1 
ATOM   1876 C  CA  . MET A  1 234 ? 23.165  11.003  33.617  1.00 23.54 ? 234 MET A CA  1 
ATOM   1877 C  C   . MET A  1 234 ? 22.340  11.979  34.440  1.00 27.44 ? 234 MET A C   1 
ATOM   1878 O  O   . MET A  1 234 ? 21.536  11.549  35.257  1.00 24.22 ? 234 MET A O   1 
ATOM   1879 C  CB  . MET A  1 234 ? 24.512  10.728  34.270  1.00 25.64 ? 234 MET A CB  1 
ATOM   1880 C  CG  . MET A  1 234 ? 24.412  10.103  35.677  1.00 28.08 ? 234 MET A CG  1 
ATOM   1881 S  SD  . MET A  1 234 ? 26.083  9.604   36.248  1.00 35.13 ? 234 MET A SD  1 
ATOM   1882 C  CE  . MET A  1 234 ? 26.923  11.042  35.587  1.00 36.09 ? 234 MET A CE  1 
ATOM   1883 N  N   . ASP A  1 235 ? 22.520  13.293  34.240  1.00 25.49 ? 235 ASP A N   1 
ATOM   1884 C  CA  . ASP A  1 235 ? 21.827  14.236  35.137  1.00 31.96 ? 235 ASP A CA  1 
ATOM   1885 C  C   . ASP A  1 235 ? 20.508  14.696  34.606  1.00 32.46 ? 235 ASP A C   1 
ATOM   1886 O  O   . ASP A  1 235 ? 19.941  15.651  35.101  1.00 32.19 ? 235 ASP A O   1 
ATOM   1887 C  CB  . ASP A  1 235 ? 22.698  15.473  35.398  1.00 40.30 ? 235 ASP A CB  1 
ATOM   1888 C  CG  . ASP A  1 235 ? 22.796  16.401  34.162  1.00 47.43 ? 235 ASP A CG  1 
ATOM   1889 O  OD1 . ASP A  1 235 ? 22.518  15.967  33.000  1.00 55.94 ? 235 ASP A OD1 1 
ATOM   1890 O  OD2 . ASP A  1 235 ? 23.144  17.583  34.365  1.00 54.91 ? 235 ASP A OD2 1 
ATOM   1891 N  N   . ASP A  1 236 ? 20.006  14.037  33.574  1.00 28.81 ? 236 ASP A N   1 
ATOM   1892 C  CA  . ASP A  1 236 ? 18.736  14.389  33.001  1.00 25.97 ? 236 ASP A CA  1 
ATOM   1893 C  C   . ASP A  1 236 ? 17.650  13.997  34.012  1.00 28.40 ? 236 ASP A C   1 
ATOM   1894 O  O   . ASP A  1 236 ? 17.499  12.825  34.362  1.00 27.03 ? 236 ASP A O   1 
ATOM   1895 C  CB  . ASP A  1 236 ? 18.513  13.637  31.652  1.00 25.50 ? 236 ASP A CB  1 
ATOM   1896 C  CG  . ASP A  1 236 ? 17.375  14.208  30.838  1.00 31.70 ? 236 ASP A CG  1 
ATOM   1897 O  OD1 . ASP A  1 236 ? 16.279  14.469  31.381  1.00 34.07 ? 236 ASP A OD1 1 
ATOM   1898 O  OD2 . ASP A  1 236 ? 17.567  14.402  29.622  1.00 27.40 ? 236 ASP A OD2 1 
ATOM   1899 N  N   . PRO A  1 237 ? 16.921  14.990  34.549  1.00 29.01 ? 237 PRO A N   1 
ATOM   1900 C  CA  . PRO A  1 237 ? 15.802  14.654  35.472  1.00 27.62 ? 237 PRO A CA  1 
ATOM   1901 C  C   . PRO A  1 237 ? 14.660  13.825  34.819  1.00 27.62 ? 237 PRO A C   1 
ATOM   1902 O  O   . PRO A  1 237 ? 13.746  13.353  35.518  1.00 29.11 ? 237 PRO A O   1 
ATOM   1903 C  CB  . PRO A  1 237 ? 15.280  16.049  35.933  1.00 31.79 ? 237 PRO A CB  1 
ATOM   1904 C  CG  . PRO A  1 237 ? 15.721  17.000  34.857  1.00 31.50 ? 237 PRO A CG  1 
ATOM   1905 C  CD  . PRO A  1 237 ? 16.840  16.373  34.042  1.00 29.11 ? 237 PRO A CD  1 
ATOM   1906 N  N   . SER A  1 238 ? 14.675  13.641  33.490  1.00 28.28 ? 238 SER A N   1 
ATOM   1907 C  CA  . SER A  1 238 ? 13.663  12.771  32.841  1.00 32.25 ? 238 SER A CA  1 
ATOM   1908 C  C   . SER A  1 238 ? 14.324  11.713  31.955  1.00 25.89 ? 238 SER A C   1 
ATOM   1909 O  O   . SER A  1 238 ? 14.382  11.877  30.714  1.00 27.54 ? 238 SER A O   1 
ATOM   1910 C  CB  . SER A  1 238 ? 12.625  13.588  32.061  1.00 34.20 ? 238 SER A CB  1 
ATOM   1911 O  OG  . SER A  1 238 ? 13.251  14.582  31.290  1.00 42.47 ? 238 SER A OG  1 
ATOM   1912 N  N   . PRO A  1 239 ? 14.788  10.632  32.614  1.00 26.01 ? 239 PRO A N   1 
ATOM   1913 C  CA  . PRO A  1 239 ? 15.582  9.710   31.819  1.00 24.93 ? 239 PRO A CA  1 
ATOM   1914 C  C   . PRO A  1 239 ? 14.728  9.037   30.706  1.00 27.88 ? 239 PRO A C   1 
ATOM   1915 O  O   . PRO A  1 239 ? 13.509  8.937   30.844  1.00 26.66 ? 239 PRO A O   1 
ATOM   1916 C  CB  . PRO A  1 239 ? 16.090  8.735   32.862  1.00 23.59 ? 239 PRO A CB  1 
ATOM   1917 C  CG  . PRO A  1 239 ? 15.093  8.818   34.029  1.00 29.61 ? 239 PRO A CG  1 
ATOM   1918 C  CD  . PRO A  1 239 ? 14.870  10.298  34.051  1.00 24.19 ? 239 PRO A CD  1 
ATOM   1919 N  N   . ARG A  1 240 ? 15.365  8.611   29.603  1.00 22.39 ? 240 ARG A N   1 
ATOM   1920 C  CA  . ARG A  1 240 ? 14.650  7.850   28.559  1.00 22.30 ? 240 ARG A CA  1 
ATOM   1921 C  C   . ARG A  1 240 ? 15.497  6.570   28.359  1.00 18.55 ? 240 ARG A C   1 
ATOM   1922 O  O   . ARG A  1 240 ? 16.683  6.624   28.023  1.00 18.40 ? 240 ARG A O   1 
ATOM   1923 C  CB  . ARG A  1 240 ? 14.485  8.625   27.245  1.00 26.56 ? 240 ARG A CB  1 
ATOM   1924 C  CG  . ARG A  1 240 ? 13.675  9.949   27.270  1.00 31.16 ? 240 ARG A CG  1 
ATOM   1925 C  CD  . ARG A  1 240 ? 13.680  10.622  25.880  1.00 32.79 ? 240 ARG A CD  1 
ATOM   1926 N  NE  . ARG A  1 240 ? 14.833  11.543  25.651  1.00 41.74 ? 240 ARG A NE  1 
ATOM   1927 C  CZ  . ARG A  1 240 ? 15.781  11.438  24.695  1.00 39.64 ? 240 ARG A CZ  1 
ATOM   1928 N  NH1 . ARG A  1 240 ? 15.777  10.438  23.812  1.00 35.52 ? 240 ARG A NH1 1 
ATOM   1929 N  NH2 . ARG A  1 240 ? 16.756  12.366  24.622  1.00 38.94 ? 240 ARG A NH2 1 
ATOM   1930 N  N   . GLU A  1 241 ? 14.911  5.420   28.565  1.00 18.56 ? 241 GLU A N   1 
ATOM   1931 C  CA  . GLU A  1 241 ? 15.628  4.172   28.222  1.00 20.04 ? 241 GLU A CA  1 
ATOM   1932 C  C   . GLU A  1 241 ? 15.961  4.061   26.723  1.00 15.93 ? 241 GLU A C   1 
ATOM   1933 O  O   . GLU A  1 241 ? 15.154  4.489   25.875  1.00 17.33 ? 241 GLU A O   1 
ATOM   1934 C  CB  . GLU A  1 241 ? 14.775  2.996   28.550  1.00 22.03 ? 241 GLU A CB  1 
ATOM   1935 C  CG  . GLU A  1 241 ? 14.575  2.736   30.020  1.00 28.20 ? 241 GLU A CG  1 
ATOM   1936 C  CD  . GLU A  1 241 ? 13.422  1.749   30.338  1.00 34.35 ? 241 GLU A CD  1 
ATOM   1937 O  OE1 . GLU A  1 241 ? 12.618  1.355   29.443  1.00 41.71 ? 241 GLU A OE1 1 
ATOM   1938 O  OE2 . GLU A  1 241 ? 13.312  1.347   31.523  1.00 41.42 ? 241 GLU A OE2 1 
ATOM   1939 N  N   . MET A  1 242 ? 17.137  3.482   26.408  1.00 14.90 ? 242 MET A N   1 
ATOM   1940 C  CA  . MET A  1 242 ? 17.515  3.229   25.026  1.00 12.83 ? 242 MET A CA  1 
ATOM   1941 C  C   . MET A  1 242 ? 16.993  1.848   24.659  1.00 11.58 ? 242 MET A C   1 
ATOM   1942 O  O   . MET A  1 242 ? 17.615  0.818   24.887  1.00 11.33 ? 242 MET A O   1 
ATOM   1943 C  CB  . MET A  1 242 ? 19.044  3.375   24.851  1.00 12.89 ? 242 MET A CB  1 
ATOM   1944 C  CG  . MET A  1 242 ? 19.423  3.137   23.380  1.00 13.29 ? 242 MET A CG  1 
ATOM   1945 S  SD  . MET A  1 242 ? 21.189  3.192   23.133  1.00 13.37 ? 242 MET A SD  1 
ATOM   1946 C  CE  . MET A  1 242 ? 21.528  4.831   23.744  1.00 15.79 ? 242 MET A CE  1 
ATOM   1947 N  N   . ILE A  1 243 ? 15.781  1.877   24.047  1.00 10.72 ? 243 ILE A N   1 
ATOM   1948 C  CA  . ILE A  1 243 ? 15.096  0.697   23.562  1.00 11.19 ? 243 ILE A CA  1 
ATOM   1949 C  C   . ILE A  1 243 ? 14.425  1.020   22.204  1.00 10.48 ? 243 ILE A C   1 
ATOM   1950 O  O   . ILE A  1 243 ? 14.240  2.188   21.835  1.00 11.74 ? 243 ILE A O   1 
ATOM   1951 C  CB  . ILE A  1 243 ? 13.953  0.235   24.512  1.00 12.21 ? 243 ILE A CB  1 
ATOM   1952 C  CG1 . ILE A  1 243 ? 13.006  1.387   24.858  1.00 13.08 ? 243 ILE A CG1 1 
ATOM   1953 C  CG2 . ILE A  1 243 ? 14.555  -0.464  25.748  1.00 15.37 ? 243 ILE A CG2 1 
ATOM   1954 C  CD1 . ILE A  1 243 ? 11.767  1.005   25.705  1.00 12.86 ? 243 ILE A CD1 1 
ATOM   1955 N  N   . ASN A  1 244 ? 14.103  -0.036  21.431  1.00 8.84  ? 244 ASN A N   1 
ATOM   1956 C  CA  . ASN A  1 244 ? 13.367  0.218   20.157  1.00 9.83  ? 244 ASN A CA  1 
ATOM   1957 C  C   . ASN A  1 244 ? 14.093  1.146   19.214  1.00 11.08 ? 244 ASN A C   1 
ATOM   1958 O  O   . ASN A  1 244 ? 13.498  2.002   18.587  1.00 11.17 ? 244 ASN A O   1 
ATOM   1959 C  CB  . ASN A  1 244 ? 11.914  0.617   20.391  1.00 10.76 ? 244 ASN A CB  1 
ATOM   1960 C  CG  . ASN A  1 244 ? 11.228  -0.299  21.318  1.00 11.84 ? 244 ASN A CG  1 
ATOM   1961 O  OD1 . ASN A  1 244 ? 11.401  -1.505  21.291  1.00 13.49 ? 244 ASN A OD1 1 
ATOM   1962 N  ND2 . ASN A  1 244 ? 10.479  0.350   22.273  1.00 14.07 ? 244 ASN A ND2 1 
ATOM   1963 N  N   . ASN A  1 245 ? 15.444  1.008   19.170  1.00 9.26  ? 245 ASN A N   1 
ATOM   1964 C  CA  . ASN A  1 245 ? 16.297  1.963   18.435  1.00 10.03 ? 245 ASN A CA  1 
ATOM   1965 C  C   . ASN A  1 245 ? 16.526  1.373   17.022  1.00 9.10  ? 245 ASN A C   1 
ATOM   1966 O  O   . ASN A  1 245 ? 17.695  1.220   16.626  1.00 9.79  ? 245 ASN A O   1 
ATOM   1967 C  CB  . ASN A  1 245 ? 17.615  2.315   19.165  1.00 9.85  ? 245 ASN A CB  1 
ATOM   1968 C  CG  . ASN A  1 245 ? 18.437  1.098   19.489  1.00 10.65 ? 245 ASN A CG  1 
ATOM   1969 O  OD1 . ASN A  1 245 ? 18.011  -0.023  19.440  1.00 10.82 ? 245 ASN A OD1 1 
ATOM   1970 N  ND2 . ASN A  1 245 ? 19.730  1.363   19.743  1.00 11.39 ? 245 ASN A ND2 1 
ATOM   1971 N  N   . PHE A  1 246 ? 15.470  0.969   16.347  1.00 9.11  ? 246 PHE A N   1 
ATOM   1972 C  CA  . PHE A  1 246 ? 15.522  0.475   14.959  1.00 8.85  ? 246 PHE A CA  1 
ATOM   1973 C  C   . PHE A  1 246 ? 14.507  1.249   14.148  1.00 8.22  ? 246 PHE A C   1 
ATOM   1974 O  O   . PHE A  1 246 ? 13.510  1.731   14.695  1.00 8.83  ? 246 PHE A O   1 
ATOM   1975 C  CB  . PHE A  1 246 ? 15.174  -1.042  14.904  1.00 10.24 ? 246 PHE A CB  1 
ATOM   1976 C  CG  . PHE A  1 246 ? 13.768  -1.365  15.406  1.00 8.99  ? 246 PHE A CG  1 
ATOM   1977 C  CD1 . PHE A  1 246 ? 13.545  -1.604  16.787  1.00 9.32  ? 246 PHE A CD1 1 
ATOM   1978 C  CD2 . PHE A  1 246 ? 12.680  -1.481  14.476  1.00 9.26  ? 246 PHE A CD2 1 
ATOM   1979 C  CE1 . PHE A  1 246 ? 12.263  -1.912  17.257  1.00 9.22  ? 246 PHE A CE1 1 
ATOM   1980 C  CE2 . PHE A  1 246 ? 11.392  -1.798  14.976  1.00 9.94  ? 246 PHE A CE2 1 
ATOM   1981 C  CZ  . PHE A  1 246 ? 11.182  -1.976  16.337  1.00 9.69  ? 246 PHE A CZ  1 
ATOM   1982 N  N   . ARG A  1 247 ? 14.835  1.404   12.875  1.00 7.61  ? 247 ARG A N   1 
ATOM   1983 C  CA  . ARG A  1 247 ? 13.922  2.131   11.920  1.00 7.10  ? 247 ARG A CA  1 
ATOM   1984 C  C   . ARG A  1 247 ? 12.906  1.104   11.369  1.00 7.08  ? 247 ARG A C   1 
ATOM   1985 O  O   . ARG A  1 247 ? 13.306  -0.040  11.088  1.00 8.11  ? 247 ARG A O   1 
ATOM   1986 C  CB  . ARG A  1 247 ? 14.723  2.794   10.821  1.00 7.12  ? 247 ARG A CB  1 
ATOM   1987 C  CG  . ARG A  1 247 ? 13.876  3.766   9.973   1.00 7.19  ? 247 ARG A CG  1 
ATOM   1988 C  CD  . ARG A  1 247 ? 14.708  4.198   8.776   1.00 7.71  ? 247 ARG A CD  1 
ATOM   1989 N  NE  . ARG A  1 247 ? 14.160  5.416   8.176   1.00 7.05  ? 247 ARG A NE  1 
ATOM   1990 C  CZ  . ARG A  1 247 ? 14.596  5.976   7.050   1.00 7.53  ? 247 ARG A CZ  1 
ATOM   1991 N  NH1 . ARG A  1 247 ? 15.604  5.438   6.378   1.00 7.37  ? 247 ARG A NH1 1 
ATOM   1992 N  NH2 . ARG A  1 247 ? 14.025  7.084   6.597   1.00 7.67  ? 247 ARG A NH2 1 
ATOM   1993 N  N   . GLN A  1 248 ? 11.633  1.523   11.221  1.00 7.26  ? 248 GLN A N   1 
ATOM   1994 C  CA  . GLN A  1 248 ? 10.715  0.633   10.450  1.00 6.77  ? 248 GLN A CA  1 
ATOM   1995 C  C   . GLN A  1 248 ? 11.151  0.374   9.011   1.00 7.95  ? 248 GLN A C   1 
ATOM   1996 O  O   . GLN A  1 248 ? 11.887  1.169   8.392   1.00 8.61  ? 248 GLN A O   1 
ATOM   1997 C  CB  . GLN A  1 248 ? 9.351   1.329   10.335  1.00 8.84  ? 248 GLN A CB  1 
ATOM   1998 C  CG  . GLN A  1 248 ? 8.651   1.633   11.679  1.00 8.37  ? 248 GLN A CG  1 
ATOM   1999 C  CD  . GLN A  1 248 ? 8.310   0.424   12.482  1.00 9.66  ? 248 GLN A CD  1 
ATOM   2000 O  OE1 . GLN A  1 248 ? 9.061   0.003   13.352  1.00 9.94  ? 248 GLN A OE1 1 
ATOM   2001 N  NE2 . GLN A  1 248 ? 7.185   -0.221  12.162  1.00 9.63  ? 248 GLN A NE2 1 
ATOM   2002 N  N   . VAL A  1 249 ? 10.801  -0.758  8.487   1.00 7.51  ? 249 VAL A N   1 
ATOM   2003 C  CA  . VAL A  1 249 ? 11.114  -1.065  7.123   1.00 8.10  ? 249 VAL A CA  1 
ATOM   2004 C  C   . VAL A  1 249 ? 10.498  -0.078  6.118   1.00 8.94  ? 249 VAL A C   1 
ATOM   2005 O  O   . VAL A  1 249 ? 9.362   0.437   6.330   1.00 8.81  ? 249 VAL A O   1 
ATOM   2006 C  CB  . VAL A  1 249 ? 10.776  -2.537  6.744   1.00 9.47  ? 249 VAL A CB  1 
ATOM   2007 C  CG1 . VAL A  1 249 ? 11.663  -3.557  7.477   1.00 9.56  ? 249 VAL A CG1 1 
ATOM   2008 C  CG2 . VAL A  1 249 ? 9.317   -2.828  6.899   1.00 13.52 ? 249 VAL A CG2 1 
ATOM   2009 N  N   . GLN A  1 250 ? 11.223  0.141   5.036   1.00 7.65  ? 250 GLN A N   1 
ATOM   2010 C  CA  . GLN A  1 250 ? 10.813  1.101   4.008   1.00 8.86  ? 250 GLN A CA  1 
ATOM   2011 C  C   . GLN A  1 250 ? 10.230  0.361   2.841   1.00 9.18  ? 250 GLN A C   1 
ATOM   2012 O  O   . GLN A  1 250 ? 10.623  -0.759  2.523   1.00 10.59 ? 250 GLN A O   1 
ATOM   2013 C  CB  . GLN A  1 250 ? 12.078  1.869   3.529   1.00 7.67  ? 250 GLN A CB  1 
ATOM   2014 C  CG  . GLN A  1 250 ? 12.941  2.429   4.688   1.00 9.13  ? 250 GLN A CG  1 
ATOM   2015 C  CD  . GLN A  1 250 ? 12.249  3.570   5.382   1.00 8.20  ? 250 GLN A CD  1 
ATOM   2016 O  OE1 . GLN A  1 250 ? 11.897  4.577   4.716   1.00 9.74  ? 250 GLN A OE1 1 
ATOM   2017 N  NE2 . GLN A  1 250 ? 11.887  3.441   6.611   1.00 7.95  ? 250 GLN A NE2 1 
ATOM   2018 N  N   . LYS A  1 251 ? 9.371   1.079   2.035   1.00 8.65  ? 251 LYS A N   1 
ATOM   2019 C  CA  . LYS A  1 251 ? 8.940   0.503   0.739   1.00 10.17 ? 251 LYS A CA  1 
ATOM   2020 C  C   . LYS A  1 251 ? 10.148  0.234   -0.153  1.00 10.47 ? 251 LYS A C   1 
ATOM   2021 O  O   . LYS A  1 251 ? 11.112  1.058   -0.136  1.00 11.72 ? 251 LYS A O   1 
ATOM   2022 C  CB  . LYS A  1 251 ? 7.990   1.465   0.042   1.00 10.16 ? 251 LYS A CB  1 
ATOM   2023 C  CG  . LYS A  1 251 ? 6.632   1.478   0.809   1.00 11.31 ? 251 LYS A CG  1 
ATOM   2024 C  CD  . LYS A  1 251 ? 5.643   2.343   0.091   1.00 11.32 ? 251 LYS A CD  1 
ATOM   2025 C  CE  . LYS A  1 251 ? 4.198   2.158   0.643   1.00 9.42  ? 251 LYS A CE  1 
ATOM   2026 N  NZ  . LYS A  1 251 ? 4.019   2.211   2.139   1.00 9.08  ? 251 LYS A NZ  1 
ATOM   2027 N  N   A PHE A  1 252 ? 10.132  -0.780  -1.024  0.50 13.08 ? 252 PHE A N   1 
ATOM   2028 N  N   B PHE A  1 252 ? 10.069  -0.882  -0.868  0.50 11.40 ? 252 PHE A N   1 
ATOM   2029 C  CA  A PHE A  1 252 ? 11.355  -1.012  -1.846  0.50 15.03 ? 252 PHE A CA  1 
ATOM   2030 C  CA  B PHE A  1 252 ? 11.090  -1.334  -1.782  0.50 12.00 ? 252 PHE A CA  1 
ATOM   2031 C  C   A PHE A  1 252 ? 11.207  -1.286  -3.393  0.50 20.91 ? 252 PHE A C   1 
ATOM   2032 C  C   B PHE A  1 252 ? 10.379  -1.871  -3.005  0.50 14.92 ? 252 PHE A C   1 
ATOM   2033 O  O   A PHE A  1 252 ? 12.157  -1.656  -4.078  0.50 23.62 ? 252 PHE A O   1 
ATOM   2034 O  O   B PHE A  1 252 ? 10.158  -3.033  -3.109  0.50 17.13 ? 252 PHE A O   1 
ATOM   2035 C  CB  A PHE A  1 252 ? 12.259  -1.992  -1.076  0.50 15.21 ? 252 PHE A CB  1 
ATOM   2036 C  CB  B PHE A  1 252 ? 11.840  -2.486  -1.125  0.50 12.02 ? 252 PHE A CB  1 
ATOM   2037 C  CG  A PHE A  1 252 ? 13.535  -2.332  -1.743  0.50 14.94 ? 252 PHE A CG  1 
ATOM   2038 C  CG  B PHE A  1 252 ? 13.078  -2.943  -1.860  0.50 11.80 ? 252 PHE A CG  1 
ATOM   2039 C  CD1 A PHE A  1 252 ? 14.611  -1.494  -1.644  0.50 14.42 ? 252 PHE A CD1 1 
ATOM   2040 C  CD1 B PHE A  1 252 ? 14.240  -2.176  -1.831  0.50 11.34 ? 252 PHE A CD1 1 
ATOM   2041 C  CD2 A PHE A  1 252 ? 13.661  -3.532  -2.416  0.50 15.47 ? 252 PHE A CD2 1 
ATOM   2042 C  CD2 B PHE A  1 252 ? 13.075  -4.172  -2.550  0.50 12.57 ? 252 PHE A CD2 1 
ATOM   2043 C  CE1 A PHE A  1 252 ? 15.828  -1.865  -2.230  0.50 16.49 ? 252 PHE A CE1 1 
ATOM   2044 C  CE1 B PHE A  1 252 ? 15.371  -2.624  -2.456  0.50 11.41 ? 252 PHE A CE1 1 
ATOM   2045 C  CE2 A PHE A  1 252 ? 14.862  -3.941  -2.955  0.50 15.35 ? 252 PHE A CE2 1 
ATOM   2046 C  CE2 B PHE A  1 252 ? 14.243  -4.629  -3.175  0.50 12.04 ? 252 PHE A CE2 1 
ATOM   2047 C  CZ  A PHE A  1 252 ? 15.941  -3.072  -2.912  0.50 15.33 ? 252 PHE A CZ  1 
ATOM   2048 C  CZ  B PHE A  1 252 ? 15.383  -3.851  -3.118  0.50 12.65 ? 252 PHE A CZ  1 
ATOM   2049 N  N   . ASP A  1 253 ? 10.029  -0.984  -3.909  1.00 23.24 ? 253 ASP A N   1 
ATOM   2050 C  CA  . ASP A  1 253 ? 9.360   -1.421  -5.191  1.00 23.15 ? 253 ASP A CA  1 
ATOM   2051 C  C   . ASP A  1 253 ? 10.178  -1.394  -6.495  1.00 22.69 ? 253 ASP A C   1 
ATOM   2052 O  O   . ASP A  1 253 ? 11.005  -0.522  -6.693  1.00 24.21 ? 253 ASP A O   1 
ATOM   2053 C  CB  . ASP A  1 253 ? 8.096   -0.532  -5.373  1.00 27.47 ? 253 ASP A CB  1 
ATOM   2054 C  CG  . ASP A  1 253 ? 7.041   -1.166  -6.289  1.00 34.00 ? 253 ASP A CG  1 
ATOM   2055 O  OD1 . ASP A  1 253 ? 6.849   -2.425  -6.243  1.00 36.26 ? 253 ASP A OD1 1 
ATOM   2056 O  OD2 . ASP A  1 253 ? 6.375   -0.404  -7.040  1.00 36.21 ? 253 ASP A OD2 1 
ATOM   2057 N  N   . GLU A  1 254 ? 9.947   -2.401  -7.341  1.00 24.75 ? 254 GLU A N   1 
ATOM   2058 C  CA  . GLU A  1 254 ? 10.601  -2.525  -8.659  1.00 26.73 ? 254 GLU A CA  1 
ATOM   2059 C  C   . GLU A  1 254 ? 12.104  -2.675  -8.536  1.00 24.38 ? 254 GLU A C   1 
ATOM   2060 O  O   . GLU A  1 254 ? 12.866  -2.271  -9.415  1.00 28.25 ? 254 GLU A O   1 
ATOM   2061 C  CB  . GLU A  1 254 ? 10.222  -1.370  -9.570  1.00 27.85 ? 254 GLU A CB  1 
ATOM   2062 C  CG  . GLU A  1 254 ? 8.691   -1.288  -9.686  1.00 30.48 ? 254 GLU A CG  1 
ATOM   2063 C  CD  . GLU A  1 254 ? 8.221   -0.172  -10.591 1.00 37.85 ? 254 GLU A CD  1 
ATOM   2064 O  OE1 . GLU A  1 254 ? 8.966   0.807   -10.769 1.00 43.64 ? 254 GLU A OE1 1 
ATOM   2065 O  OE2 . GLU A  1 254 ? 7.087   -0.271  -11.112 1.00 41.33 ? 254 GLU A OE2 1 
ATOM   2066 N  N   . ARG A  1 255 ? 12.500  -3.272  -7.431  1.00 24.13 ? 255 ARG A N   1 
ATOM   2067 C  CA  . ARG A  1 255 ? 13.916  -3.516  -7.148  1.00 23.56 ? 255 ARG A CA  1 
ATOM   2068 C  C   . ARG A  1 255 ? 14.136  -4.952  -6.672  1.00 23.92 ? 255 ARG A C   1 
ATOM   2069 O  O   . ARG A  1 255 ? 13.224  -5.644  -6.131  1.00 26.70 ? 255 ARG A O   1 
ATOM   2070 C  CB  . ARG A  1 255 ? 14.454  -2.526  -6.155  1.00 21.44 ? 255 ARG A CB  1 
ATOM   2071 C  CG  . ARG A  1 255 ? 14.321  -1.061  -6.605  1.00 21.82 ? 255 ARG A CG  1 
ATOM   2072 C  CD  . ARG A  1 255 ? 14.862  -0.097  -5.550  1.00 22.38 ? 255 ARG A CD  1 
ATOM   2073 N  NE  . ARG A  1 255 ? 16.279  -0.409  -5.363  1.00 24.01 ? 255 ARG A NE  1 
ATOM   2074 C  CZ  . ARG A  1 255 ? 16.996  -0.110  -4.286  1.00 25.51 ? 255 ARG A CZ  1 
ATOM   2075 N  NH1 . ARG A  1 255 ? 16.444  0.536   -3.271  1.00 23.40 ? 255 ARG A NH1 1 
ATOM   2076 N  NH2 . ARG A  1 255 ? 18.276  -0.456  -4.232  1.00 18.73 ? 255 ARG A NH2 1 
ATOM   2077 N  N   . LEU A  1 256 ? 15.379  -5.378  -6.881  1.00 20.63 ? 256 LEU A N   1 
ATOM   2078 C  CA  . LEU A  1 256 ? 15.819  -6.641  -6.429  1.00 21.74 ? 256 LEU A CA  1 
ATOM   2079 C  C   . LEU A  1 256 ? 16.829  -6.514  -5.272  1.00 17.52 ? 256 LEU A C   1 
ATOM   2080 O  O   . LEU A  1 256 ? 17.592  -5.520  -5.125  1.00 21.01 ? 256 LEU A O   1 
ATOM   2081 C  CB  . LEU A  1 256 ? 16.450  -7.406  -7.618  1.00 24.54 ? 256 LEU A CB  1 
ATOM   2082 C  CG  . LEU A  1 256 ? 15.497  -7.928  -8.731  1.00 28.42 ? 256 LEU A CG  1 
ATOM   2083 C  CD1 . LEU A  1 256 ? 16.286  -8.521  -9.886  1.00 31.22 ? 256 LEU A CD1 1 
ATOM   2084 C  CD2 . LEU A  1 256 ? 14.480  -8.967  -8.243  1.00 27.38 ? 256 LEU A CD2 1 
ATOM   2085 N  N   . VAL A  1 257 ? 16.794  -7.554  -4.452  1.00 19.54 ? 257 VAL A N   1 
ATOM   2086 C  CA  . VAL A  1 257 ? 17.926  -7.858  -3.585  1.00 16.56 ? 257 VAL A CA  1 
ATOM   2087 C  C   . VAL A  1 257 ? 18.638  -9.057  -4.170  1.00 15.67 ? 257 VAL A C   1 
ATOM   2088 O  O   . VAL A  1 257 ? 18.046  -10.157 -4.369  1.00 16.76 ? 257 VAL A O   1 
ATOM   2089 C  CB  . VAL A  1 257 ? 17.425  -8.204  -2.165  1.00 15.58 ? 257 VAL A CB  1 
ATOM   2090 C  CG1 . VAL A  1 257 ? 18.477  -8.759  -1.211  1.00 14.66 ? 257 VAL A CG1 1 
ATOM   2091 C  CG2 . VAL A  1 257 ? 16.750  -7.033  -1.516  1.00 19.11 ? 257 VAL A CG2 1 
ATOM   2092 N  N   . TYR A  1 258 ? 19.942  -8.947  -4.312  1.00 14.42 ? 258 TYR A N   1 
ATOM   2093 C  CA  . TYR A  1 258 ? 20.746  -9.999  -4.899  1.00 13.89 ? 258 TYR A CA  1 
ATOM   2094 C  C   . TYR A  1 258 ? 21.227  -10.867 -3.821  1.00 14.57 ? 258 TYR A C   1 
ATOM   2095 O  O   . TYR A  1 258 ? 21.506  -10.416 -2.697  1.00 15.05 ? 258 TYR A O   1 
ATOM   2096 C  CB  . TYR A  1 258 ? 21.873  -9.378  -5.721  1.00 15.34 ? 258 TYR A CB  1 
ATOM   2097 C  CG  . TYR A  1 258 ? 21.300  -8.502  -6.762  1.00 20.33 ? 258 TYR A CG  1 
ATOM   2098 C  CD1 . TYR A  1 258 ? 20.737  -9.051  -7.912  1.00 17.90 ? 258 TYR A CD1 1 
ATOM   2099 C  CD2 . TYR A  1 258 ? 21.212  -7.140  -6.553  1.00 20.76 ? 258 TYR A CD2 1 
ATOM   2100 C  CE1 . TYR A  1 258 ? 20.125  -8.218  -8.898  1.00 23.54 ? 258 TYR A CE1 1 
ATOM   2101 C  CE2 . TYR A  1 258 ? 20.569  -6.302  -7.489  1.00 23.76 ? 258 TYR A CE2 1 
ATOM   2102 C  CZ  . TYR A  1 258 ? 20.042  -6.850  -8.661  1.00 23.84 ? 258 TYR A CZ  1 
ATOM   2103 O  OH  . TYR A  1 258 ? 19.422  -5.994  -9.578  1.00 28.97 ? 258 TYR A OH  1 
ATOM   2104 N  N   . THR A  1 259 ? 21.303  -12.159 -4.102  1.00 12.87 ? 259 THR A N   1 
ATOM   2105 C  CA  . THR A  1 259 ? 21.784  -13.117 -3.090  1.00 12.87 ? 259 THR A CA  1 
ATOM   2106 C  C   . THR A  1 259 ? 22.985  -13.891 -3.630  1.00 13.16 ? 259 THR A C   1 
ATOM   2107 O  O   . THR A  1 259 ? 23.095  -14.255 -4.859  1.00 13.77 ? 259 THR A O   1 
ATOM   2108 C  CB  . THR A  1 259 ? 20.673  -14.103 -2.622  1.00 11.66 ? 259 THR A CB  1 
ATOM   2109 O  OG1 . THR A  1 259 ? 20.172  -14.756 -3.809  1.00 14.64 ? 259 THR A OG1 1 
ATOM   2110 C  CG2 . THR A  1 259 ? 19.516  -13.328 -1.985  1.00 12.63 ? 259 THR A CG2 1 
ATOM   2111 N  N   . SER A  1 260 ? 23.899  -14.173 -2.715  1.00 13.50 ? 260 SER A N   1 
ATOM   2112 C  CA  . SER A  1 260 ? 25.069  -14.992 -3.113  1.00 14.87 ? 260 SER A CA  1 
ATOM   2113 C  C   . SER A  1 260 ? 24.762  -16.475 -3.077  1.00 16.70 ? 260 SER A C   1 
ATOM   2114 O  O   . SER A  1 260 ? 25.654  -17.282 -3.403  1.00 20.58 ? 260 SER A O   1 
ATOM   2115 C  CB  . SER A  1 260 ? 26.236  -14.686 -2.200  1.00 14.28 ? 260 SER A CB  1 
ATOM   2116 O  OG  . SER A  1 260 ? 25.917  -15.173 -0.895  1.00 14.05 ? 260 SER A OG  1 
ATOM   2117 N  N   . PHE A  1 261 ? 23.551  -16.815 -2.663  1.00 15.25 ? 261 PHE A N   1 
ATOM   2118 C  CA  . PHE A  1 261 ? 23.085  -18.200 -2.549  1.00 19.04 ? 261 PHE A CA  1 
ATOM   2119 C  C   . PHE A  1 261 ? 21.858  -18.368 -3.339  1.00 20.26 ? 261 PHE A C   1 
ATOM   2120 O  O   . PHE A  1 261 ? 20.989  -17.435 -3.554  1.00 19.81 ? 261 PHE A O   1 
ATOM   2121 C  CB  . PHE A  1 261 ? 22.853  -18.544 -1.068  1.00 17.58 ? 261 PHE A CB  1 
ATOM   2122 C  CG  . PHE A  1 261 ? 21.882  -17.623 -0.375  1.00 16.19 ? 261 PHE A CG  1 
ATOM   2123 C  CD1 . PHE A  1 261 ? 20.511  -17.841 -0.338  1.00 15.30 ? 261 PHE A CD1 1 
ATOM   2124 C  CD2 . PHE A  1 261 ? 22.358  -16.454 0.138   1.00 13.06 ? 261 PHE A CD2 1 
ATOM   2125 C  CE1 . PHE A  1 261 ? 19.665  -16.986 0.334   1.00 15.31 ? 261 PHE A CE1 1 
ATOM   2126 C  CE2 . PHE A  1 261 ? 21.508  -15.533 0.813   1.00 14.06 ? 261 PHE A CE2 1 
ATOM   2127 C  CZ  . PHE A  1 261 ? 20.149  -15.782 0.860   1.00 14.97 ? 261 PHE A CZ  1 
ATOM   2128 N  N   . SER A  1 262 ? 21.714  -19.580 -3.848  1.00 28.50 ? 262 SER A N   1 
ATOM   2129 C  CA  . SER A  1 262 ? 20.407  -19.821 -4.418  1.00 31.56 ? 262 SER A CA  1 
ATOM   2130 C  C   . SER A  1 262 ? 19.669  -20.771 -3.480  1.00 40.29 ? 262 SER A C   1 
ATOM   2131 O  O   . SER A  1 262 ? 18.566  -20.467 -3.010  1.00 36.04 ? 262 SER A O   1 
ATOM   2132 C  CB  . SER A  1 262 ? 20.501  -20.315 -5.866  1.00 37.74 ? 262 SER A CB  1 
ATOM   2133 O  OG  . SER A  1 262 ? 20.469  -21.709 -5.919  1.00 38.48 ? 262 SER A OG  1 
ATOM   2134 N  N   . GLN A  1 263 ? 20.327  -21.877 -3.143  1.00 40.10 ? 263 GLN A N   1 
ATOM   2135 C  CA  . GLN A  1 263 ? 19.713  -22.935 -2.339  1.00 44.55 ? 263 GLN A CA  1 
ATOM   2136 C  C   . GLN A  1 263 ? 19.008  -22.385 -1.076  1.00 46.92 ? 263 GLN A C   1 
ATOM   2137 O  O   . GLN A  1 263 ? 19.543  -21.516 -0.369  1.00 45.88 ? 263 GLN A O   1 
ATOM   2138 C  CB  . GLN A  1 263 ? 20.767  -23.977 -1.939  1.00 44.95 ? 263 GLN A CB  1 
ATOM   2139 C  CG  . GLN A  1 263 ? 21.727  -24.347 -3.038  1.00 40.85 ? 263 GLN A CG  1 
ATOM   2140 C  CD  . GLN A  1 263 ? 22.235  -25.778 -2.949  1.00 44.89 ? 263 GLN A CD  1 
ATOM   2141 O  OE1 . GLN A  1 263 ? 23.361  -26.068 -2.432  1.00 41.81 ? 263 GLN A OE1 1 
ATOM   2142 N  NE2 . GLN A  1 263 ? 21.434  -26.692 -3.482  1.00 32.33 ? 263 GLN A NE2 1 
ATOM   2143 N  N   . LYS B  1 3   ? 0.508   18.173  -1.809  1.00 37.14 ? 3   LYS B N   1 
ATOM   2144 C  CA  . LYS B  1 3   ? -0.245  17.176  -2.610  1.00 33.29 ? 3   LYS B CA  1 
ATOM   2145 C  C   . LYS B  1 3   ? 0.381   15.842  -2.212  1.00 25.93 ? 3   LYS B C   1 
ATOM   2146 O  O   . LYS B  1 3   ? 1.229   15.316  -2.936  1.00 24.41 ? 3   LYS B O   1 
ATOM   2147 C  CB  . LYS B  1 3   ? -0.039  17.442  -4.096  1.00 38.29 ? 3   LYS B CB  1 
ATOM   2148 C  CG  . LYS B  1 3   ? 1.366   17.895  -4.455  1.00 43.43 ? 3   LYS B CG  1 
ATOM   2149 C  CD  . LYS B  1 3   ? 1.723   19.245  -3.840  1.00 40.96 ? 3   LYS B CD  1 
ATOM   2150 C  CE  . LYS B  1 3   ? 3.046   19.762  -4.375  1.00 40.75 ? 3   LYS B CE  1 
ATOM   2151 N  NZ  . LYS B  1 3   ? 4.181   18.912  -3.890  1.00 33.81 ? 3   LYS B NZ  1 
ATOM   2152 N  N   . TRP B  1 4   ? 0.004   15.345  -1.023  1.00 16.56 ? 4   TRP B N   1 
ATOM   2153 C  CA  . TRP B  1 4   ? 0.683   14.193  -0.447  1.00 13.48 ? 4   TRP B CA  1 
ATOM   2154 C  C   . TRP B  1 4   ? 0.457   13.019  -1.381  1.00 11.19 ? 4   TRP B C   1 
ATOM   2155 O  O   . TRP B  1 4   ? -0.594  12.883  -2.082  1.00 13.51 ? 4   TRP B O   1 
ATOM   2156 C  CB  . TRP B  1 4   ? 0.233   13.965  1.024   1.00 11.87 ? 4   TRP B CB  1 
ATOM   2157 C  CG  . TRP B  1 4   ? -1.238  13.686  1.219   1.00 11.29 ? 4   TRP B CG  1 
ATOM   2158 C  CD1 . TRP B  1 4   ? -2.276  14.574  1.490   1.00 13.27 ? 4   TRP B CD1 1 
ATOM   2159 C  CD2 . TRP B  1 4   ? -1.859  12.367  1.164   1.00 10.95 ? 4   TRP B CD2 1 
ATOM   2160 N  NE1 . TRP B  1 4   ? -3.459  13.899  1.608   1.00 12.92 ? 4   TRP B NE1 1 
ATOM   2161 C  CE2 . TRP B  1 4   ? -3.255  12.544  1.475   1.00 11.25 ? 4   TRP B CE2 1 
ATOM   2162 C  CE3 . TRP B  1 4   ? -1.346  11.076  1.028   1.00 10.06 ? 4   TRP B CE3 1 
ATOM   2163 C  CZ2 . TRP B  1 4   ? -4.138  11.463  1.586   1.00 10.63 ? 4   TRP B CZ2 1 
ATOM   2164 C  CZ3 . TRP B  1 4   ? -2.246  9.993   1.117   1.00 9.37  ? 4   TRP B CZ3 1 
ATOM   2165 C  CH2 . TRP B  1 4   ? -3.575  10.184  1.361   1.00 10.74 ? 4   TRP B CH2 1 
ATOM   2166 N  N   . THR B  1 5   ? 1.384   12.101  -1.323  1.00 10.26 ? 5   THR B N   1 
ATOM   2167 C  CA  . THR B  1 5   ? 1.319   10.888  -2.139  1.00 9.64  ? 5   THR B CA  1 
ATOM   2168 C  C   . THR B  1 5   ? 1.830   9.687   -1.316  1.00 9.87  ? 5   THR B C   1 
ATOM   2169 O  O   . THR B  1 5   ? 2.188   9.796   -0.111  1.00 9.77  ? 5   THR B O   1 
ATOM   2170 C  CB  . THR B  1 5   ? 2.196   10.947  -3.394  1.00 11.85 ? 5   THR B CB  1 
ATOM   2171 O  OG1 . THR B  1 5   ? 3.549   10.982  -2.889  1.00 11.75 ? 5   THR B OG1 1 
ATOM   2172 C  CG2 . THR B  1 5   ? 1.906   12.272  -4.186  1.00 12.63 ? 5   THR B CG2 1 
ATOM   2173 N  N   . TYR B  1 6   ? 1.988   8.579   -2.017  1.00 9.50  ? 6   TYR B N   1 
ATOM   2174 C  CA  . TYR B  1 6   ? 2.649   7.424   -1.407  1.00 9.66  ? 6   TYR B CA  1 
ATOM   2175 C  C   . TYR B  1 6   ? 4.006   7.052   -1.991  1.00 10.82 ? 6   TYR B C   1 
ATOM   2176 O  O   . TYR B  1 6   ? 4.578   6.000   -1.784  1.00 11.48 ? 6   TYR B O   1 
ATOM   2177 C  CB  . TYR B  1 6   ? 1.774   6.163   -1.508  1.00 8.99  ? 6   TYR B CB  1 
ATOM   2178 C  CG  . TYR B  1 6   ? 0.499   6.233   -0.661  1.00 8.26  ? 6   TYR B CG  1 
ATOM   2179 C  CD1 . TYR B  1 6   ? -0.682  6.795   -1.158  1.00 7.58  ? 6   TYR B CD1 1 
ATOM   2180 C  CD2 . TYR B  1 6   ? 0.485   5.684   0.631   1.00 9.14  ? 6   TYR B CD2 1 
ATOM   2181 C  CE1 . TYR B  1 6   ? -1.835  6.759   -0.382  1.00 7.65  ? 6   TYR B CE1 1 
ATOM   2182 C  CE2 . TYR B  1 6   ? -0.655  5.685   1.426   1.00 8.17  ? 6   TYR B CE2 1 
ATOM   2183 C  CZ  . TYR B  1 6   ? -1.805  6.308   0.940   1.00 6.97  ? 6   TYR B CZ  1 
ATOM   2184 O  OH  . TYR B  1 6   ? -2.945  6.283   1.655   1.00 7.55  ? 6   TYR B OH  1 
ATOM   2185 N  N   . PHE B  1 7   ? 4.512   7.963   -2.837  1.00 12.34 ? 7   PHE B N   1 
ATOM   2186 C  CA  . PHE B  1 7   ? 5.708   7.655   -3.561  1.00 13.94 ? 7   PHE B CA  1 
ATOM   2187 C  C   . PHE B  1 7   ? 6.398   8.924   -3.922  1.00 13.84 ? 7   PHE B C   1 
ATOM   2188 O  O   . PHE B  1 7   ? 5.808   9.786   -4.550  1.00 13.84 ? 7   PHE B O   1 
ATOM   2189 C  CB  . PHE B  1 7   ? 5.476   6.861   -4.896  1.00 19.47 ? 7   PHE B CB  1 
ATOM   2190 C  CG  . PHE B  1 7   ? 6.767   6.560   -5.584  1.00 22.12 ? 7   PHE B CG  1 
ATOM   2191 C  CD1 . PHE B  1 7   ? 7.665   5.585   -5.091  1.00 24.42 ? 7   PHE B CD1 1 
ATOM   2192 C  CD2 . PHE B  1 7   ? 7.160   7.335   -6.691  1.00 31.05 ? 7   PHE B CD2 1 
ATOM   2193 C  CE1 . PHE B  1 7   ? 8.914   5.382   -5.681  1.00 30.60 ? 7   PHE B CE1 1 
ATOM   2194 C  CE2 . PHE B  1 7   ? 8.401   7.131   -7.300  1.00 31.53 ? 7   PHE B CE2 1 
ATOM   2195 C  CZ  . PHE B  1 7   ? 9.258   6.160   -6.797  1.00 30.97 ? 7   PHE B CZ  1 
ATOM   2196 N  N   . GLY B  1 8   ? 7.670   9.038   -3.538  1.00 15.67 ? 8   GLY B N   1 
ATOM   2197 C  CA  . GLY B  1 8   ? 8.507   10.232  -4.003  1.00 15.85 ? 8   GLY B CA  1 
ATOM   2198 C  C   . GLY B  1 8   ? 8.520   11.349  -2.969  1.00 17.29 ? 8   GLY B C   1 
ATOM   2199 O  O   . GLY B  1 8   ? 8.299   11.133  -1.790  1.00 16.27 ? 8   GLY B O   1 
ATOM   2200 N  N   . PRO B  1 9   ? 8.858   12.567  -3.379  1.00 18.03 ? 9   PRO B N   1 
ATOM   2201 C  CA  . PRO B  1 9   ? 9.113   13.588  -2.413  1.00 19.58 ? 9   PRO B CA  1 
ATOM   2202 C  C   . PRO B  1 9   ? 8.017   13.891  -1.473  1.00 20.05 ? 9   PRO B C   1 
ATOM   2203 O  O   . PRO B  1 9   ? 8.300   14.386  -0.388  1.00 19.64 ? 9   PRO B O   1 
ATOM   2204 C  CB  . PRO B  1 9   ? 9.438   14.834  -3.275  1.00 23.35 ? 9   PRO B CB  1 
ATOM   2205 C  CG  . PRO B  1 9   ? 9.979   14.210  -4.501  1.00 22.97 ? 9   PRO B CG  1 
ATOM   2206 C  CD  . PRO B  1 9   ? 9.133   13.010  -4.749  1.00 20.99 ? 9   PRO B CD  1 
ATOM   2207 N  N   . ASP B  1 10  ? 6.754   13.610  -1.852  1.00 15.46 ? 10  ASP B N   1 
ATOM   2208 C  CA  . ASP B  1 10  ? 5.599   13.944  -1.050  1.00 15.67 ? 10  ASP B CA  1 
ATOM   2209 C  C   . ASP B  1 10  ? 5.012   12.655  -0.379  1.00 11.74 ? 10  ASP B C   1 
ATOM   2210 O  O   . ASP B  1 10  ? 3.946   12.731  0.159   1.00 12.26 ? 10  ASP B O   1 
ATOM   2211 C  CB  . ASP B  1 10  ? 4.513   14.688  -1.840  1.00 19.05 ? 10  ASP B CB  1 
ATOM   2212 C  CG  . ASP B  1 10  ? 5.071   16.004  -2.511  1.00 23.08 ? 10  ASP B CG  1 
ATOM   2213 O  OD1 . ASP B  1 10  ? 5.759   16.714  -1.789  1.00 26.48 ? 10  ASP B OD1 1 
ATOM   2214 O  OD2 . ASP B  1 10  ? 4.963   16.153  -3.720  1.00 26.94 ? 10  ASP B OD2 1 
ATOM   2215 N  N   . GLY B  1 11  ? 5.869   11.628  -0.391  1.00 11.23 ? 11  GLY B N   1 
ATOM   2216 C  CA  . GLY B  1 11  ? 5.478   10.267  0.176   1.00 10.63 ? 11  GLY B CA  1 
ATOM   2217 C  C   . GLY B  1 11  ? 5.613   10.268  1.702   1.00 9.49  ? 11  GLY B C   1 
ATOM   2218 O  O   . GLY B  1 11  ? 5.782   11.293  2.379   1.00 8.74  ? 11  GLY B O   1 
ATOM   2219 N  N   . GLU B  1 12  ? 5.345   9.081   2.275   1.00 8.30  ? 12  GLU B N   1 
ATOM   2220 C  CA  . GLU B  1 12  ? 4.981   9.009   3.691   1.00 7.72  ? 12  GLU B CA  1 
ATOM   2221 C  C   . GLU B  1 12  ? 6.000   9.446   4.699   1.00 8.09  ? 12  GLU B C   1 
ATOM   2222 O  O   . GLU B  1 12  ? 5.614   9.897   5.766   1.00 8.17  ? 12  GLU B O   1 
ATOM   2223 C  CB  . GLU B  1 12  ? 4.503   7.575   3.957   1.00 8.09  ? 12  GLU B CB  1 
ATOM   2224 C  CG  . GLU B  1 12  ? 5.624   6.545   4.105   1.00 7.55  ? 12  GLU B CG  1 
ATOM   2225 C  CD  . GLU B  1 12  ? 4.964   5.169   4.073   1.00 7.81  ? 12  GLU B CD  1 
ATOM   2226 O  OE1 . GLU B  1 12  ? 4.630   4.690   5.161   1.00 7.47  ? 12  GLU B OE1 1 
ATOM   2227 O  OE2 . GLU B  1 12  ? 4.948   4.586   2.931   1.00 9.02  ? 12  GLU B OE2 1 
ATOM   2228 N  N   . ASN B  1 13  ? 7.304   9.402   4.339   1.00 8.13  ? 13  ASN B N   1 
ATOM   2229 C  CA  . ASN B  1 13  ? 8.299   9.849   5.310   1.00 8.62  ? 13  ASN B CA  1 
ATOM   2230 C  C   . ASN B  1 13  ? 8.356   11.392  5.398   1.00 9.35  ? 13  ASN B C   1 
ATOM   2231 O  O   . ASN B  1 13  ? 8.910   11.974  6.334   1.00 10.13 ? 13  ASN B O   1 
ATOM   2232 C  CB  . ASN B  1 13  ? 9.670   9.325   4.956   1.00 8.95  ? 13  ASN B CB  1 
ATOM   2233 C  CG  . ASN B  1 13  ? 9.837   7.855   5.232   1.00 9.87  ? 13  ASN B CG  1 
ATOM   2234 O  OD1 . ASN B  1 13  ? 8.930   7.179   5.697   1.00 9.61  ? 13  ASN B OD1 1 
ATOM   2235 N  ND2 . ASN B  1 13  ? 11.008  7.327   4.857   1.00 10.13 ? 13  ASN B ND2 1 
ATOM   2236 N  N   . SER B  1 14  ? 7.657   11.989  4.443   1.00 8.85  ? 14  SER B N   1 
ATOM   2237 C  CA  . SER B  1 14  ? 7.537   13.490  4.373   1.00 8.27  ? 14  SER B CA  1 
ATOM   2238 C  C   . SER B  1 14  ? 6.224   14.064  4.799   1.00 8.20  ? 14  SER B C   1 
ATOM   2239 O  O   . SER B  1 14  ? 6.065   15.276  4.943   1.00 10.21 ? 14  SER B O   1 
ATOM   2240 C  CB  . SER B  1 14  ? 7.812   13.970  2.970   1.00 9.07  ? 14  SER B CB  1 
ATOM   2241 O  OG  . SER B  1 14  ? 9.173   13.755  2.617   1.00 9.71  ? 14  SER B OG  1 
ATOM   2242 N  N   . TRP B  1 15  ? 5.207   13.255  5.054   1.00 7.88  ? 15  TRP B N   1 
ATOM   2243 C  CA  . TRP B  1 15  ? 3.883   13.802  5.399   1.00 8.83  ? 15  TRP B CA  1 
ATOM   2244 C  C   . TRP B  1 15  ? 3.936   14.636  6.630   1.00 9.48  ? 15  TRP B C   1 
ATOM   2245 O  O   . TRP B  1 15  ? 3.238   15.679  6.712   1.00 9.92  ? 15  TRP B O   1 
ATOM   2246 C  CB  . TRP B  1 15  ? 2.944   12.670  5.773   1.00 8.80  ? 15  TRP B CB  1 
ATOM   2247 C  CG  . TRP B  1 15  ? 2.555   11.781  4.635   1.00 8.24  ? 15  TRP B CG  1 
ATOM   2248 C  CD1 . TRP B  1 15  ? 2.770   11.963  3.270   1.00 8.11  ? 15  TRP B CD1 1 
ATOM   2249 C  CD2 . TRP B  1 15  ? 1.771   10.533  4.744   1.00 8.09  ? 15  TRP B CD2 1 
ATOM   2250 N  NE1 . TRP B  1 15  ? 2.171   10.939  2.528   1.00 9.10  ? 15  TRP B NE1 1 
ATOM   2251 C  CE2 . TRP B  1 15  ? 1.589   10.039  3.376   1.00 7.78  ? 15  TRP B CE2 1 
ATOM   2252 C  CE3 . TRP B  1 15  ? 1.193   9.786   5.836   1.00 7.13  ? 15  TRP B CE3 1 
ATOM   2253 C  CZ2 . TRP B  1 15  ? 0.844   8.841   3.085   1.00 8.51  ? 15  TRP B CZ2 1 
ATOM   2254 C  CZ3 . TRP B  1 15  ? 0.474   8.647   5.519   1.00 8.86  ? 15  TRP B CZ3 1 
ATOM   2255 C  CH2 . TRP B  1 15  ? 0.333   8.173   4.188   1.00 8.24  ? 15  TRP B CH2 1 
ATOM   2256 N  N   . SER B  1 16  ? 4.815   14.340  7.605   1.00 8.53  ? 16  SER B N   1 
ATOM   2257 C  CA  . SER B  1 16  ? 4.881   15.145  8.868   1.00 9.15  ? 16  SER B CA  1 
ATOM   2258 C  C   . SER B  1 16  ? 5.346   16.587  8.629   1.00 9.51  ? 16  SER B C   1 
ATOM   2259 O  O   . SER B  1 16  ? 5.176   17.391  9.546   1.00 11.24 ? 16  SER B O   1 
ATOM   2260 C  CB  . SER B  1 16  ? 5.890   14.485  9.867   1.00 11.31 ? 16  SER B CB  1 
ATOM   2261 O  OG  . SER B  1 16  ? 7.190   14.555  9.261   1.00 13.43 ? 16  SER B OG  1 
ATOM   2262 N  N   . LYS B  1 17  ? 5.972   16.817  7.494   1.00 9.49  ? 17  LYS B N   1 
ATOM   2263 C  CA  . LYS B  1 17  ? 6.416   18.223  7.156   1.00 9.89  ? 17  LYS B CA  1 
ATOM   2264 C  C   . LYS B  1 17  ? 5.217   19.105  7.087   1.00 11.21 ? 17  LYS B C   1 
ATOM   2265 O  O   . LYS B  1 17  ? 5.375   20.328  7.352   1.00 11.33 ? 17  LYS B O   1 
ATOM   2266 C  CB  . LYS B  1 17  ? 7.204   18.258  5.807   1.00 8.72  ? 17  LYS B CB  1 
ATOM   2267 C  CG  . LYS B  1 17  ? 8.515   17.440  5.865   1.00 11.30 ? 17  LYS B CG  1 
ATOM   2268 C  CD  . LYS B  1 17  ? 9.119   17.464  4.480   1.00 8.96  ? 17  LYS B CD  1 
ATOM   2269 C  CE  . LYS B  1 17  ? 10.279  16.489  4.275   1.00 10.06 ? 17  LYS B CE  1 
ATOM   2270 N  NZ  . LYS B  1 17  ? 10.862  16.585  2.931   1.00 10.22 ? 17  LYS B NZ  1 
ATOM   2271 N  N   . LYS B  1 18  ? 4.100   18.639  6.520   1.00 10.24 ? 18  LYS B N   1 
ATOM   2272 C  CA  . LYS B  1 18  ? 2.845   19.473  6.352   1.00 9.74  ? 18  LYS B CA  1 
ATOM   2273 C  C   . LYS B  1 18  ? 1.748   19.105  7.371   1.00 10.67 ? 18  LYS B C   1 
ATOM   2274 O  O   . LYS B  1 18  ? 0.821   19.913  7.594   1.00 12.32 ? 18  LYS B O   1 
ATOM   2275 C  CB  . LYS B  1 18  ? 2.304   19.300  4.964   1.00 12.19 ? 18  LYS B CB  1 
ATOM   2276 C  CG  . LYS B  1 18  ? 3.218   19.944  3.910   1.00 14.66 ? 18  LYS B CG  1 
ATOM   2277 C  CD  . LYS B  1 18  ? 2.733   19.692  2.437   1.00 16.29 ? 18  LYS B CD  1 
ATOM   2278 C  CE  . LYS B  1 18  ? 3.335   20.787  1.494   1.00 23.70 ? 18  LYS B CE  1 
ATOM   2279 N  NZ  . LYS B  1 18  ? 2.834   20.498  0.090   1.00 28.29 ? 18  LYS B NZ  1 
ATOM   2280 N  N   . TYR B  1 19  ? 1.823   17.894  7.962   1.00 9.75  ? 19  TYR B N   1 
ATOM   2281 C  CA  . TYR B  1 19  ? 0.770   17.346  8.755   1.00 10.40 ? 19  TYR B CA  1 
ATOM   2282 C  C   . TYR B  1 19  ? 1.399   16.811  10.048  1.00 10.71 ? 19  TYR B C   1 
ATOM   2283 O  O   . TYR B  1 19  ? 1.876   15.634  10.130  1.00 11.15 ? 19  TYR B O   1 
ATOM   2284 C  CB  . TYR B  1 19  ? 0.099   16.157  7.981   1.00 10.47 ? 19  TYR B CB  1 
ATOM   2285 C  CG  . TYR B  1 19  ? -0.509  16.570  6.636   1.00 10.34 ? 19  TYR B CG  1 
ATOM   2286 C  CD1 . TYR B  1 19  ? -1.782  17.183  6.641   1.00 11.30 ? 19  TYR B CD1 1 
ATOM   2287 C  CD2 . TYR B  1 19  ? 0.198   16.423  5.399   1.00 10.63 ? 19  TYR B CD2 1 
ATOM   2288 C  CE1 . TYR B  1 19  ? -2.325  17.585  5.423   1.00 13.03 ? 19  TYR B CE1 1 
ATOM   2289 C  CE2 . TYR B  1 19  ? -0.403  16.856  4.218   1.00 12.88 ? 19  TYR B CE2 1 
ATOM   2290 C  CZ  . TYR B  1 19  ? -1.664  17.372  4.296   1.00 13.67 ? 19  TYR B CZ  1 
ATOM   2291 O  OH  . TYR B  1 19  ? -2.186  17.790  3.052   1.00 18.32 ? 19  TYR B OH  1 
ATOM   2292 N  N   . PRO B  1 20  ? 1.564   17.689  11.043  1.00 10.69 ? 20  PRO B N   1 
ATOM   2293 C  CA  . PRO B  1 20  ? 2.314   17.300  12.229  1.00 13.19 ? 20  PRO B CA  1 
ATOM   2294 C  C   . PRO B  1 20  ? 1.828   16.037  12.911  1.00 11.80 ? 20  PRO B C   1 
ATOM   2295 O  O   . PRO B  1 20  ? 2.723   15.362  13.523  1.00 12.88 ? 20  PRO B O   1 
ATOM   2296 C  CB  . PRO B  1 20  ? 2.184   18.514  13.171  1.00 13.32 ? 20  PRO B CB  1 
ATOM   2297 C  CG  . PRO B  1 20  ? 1.725   19.634  12.253  1.00 14.03 ? 20  PRO B CG  1 
ATOM   2298 C  CD  . PRO B  1 20  ? 1.047   19.083  11.044  1.00 12.43 ? 20  PRO B CD  1 
ATOM   2299 N  N   . SER B  1 21  ? 0.528   15.724  12.886  1.00 10.64 ? 21  SER B N   1 
ATOM   2300 C  CA  . SER B  1 21  ? 0.113   14.543  13.645  1.00 10.65 ? 21  SER B CA  1 
ATOM   2301 C  C   . SER B  1 21  ? 0.707   13.278  12.984  1.00 11.43 ? 21  SER B C   1 
ATOM   2302 O  O   . SER B  1 21  ? 0.723   12.244  13.659  1.00 10.86 ? 21  SER B O   1 
ATOM   2303 C  CB  . SER B  1 21  ? -1.383  14.445  13.701  1.00 11.74 ? 21  SER B CB  1 
ATOM   2304 O  OG  . SER B  1 21  ? -1.870  15.521  14.560  1.00 13.72 ? 21  SER B OG  1 
ATOM   2305 N  N   . CYS B  1 22  ? 1.089   13.321  11.715  1.00 9.78  ? 22  CYS B N   1 
ATOM   2306 C  CA  . CYS B  1 22  ? 1.665   12.105  11.080  1.00 9.68  ? 22  CYS B CA  1 
ATOM   2307 C  C   . CYS B  1 22  ? 3.001   11.766  11.727  1.00 10.67 ? 22  CYS B C   1 
ATOM   2308 O  O   . CYS B  1 22  ? 3.529   10.664  11.523  1.00 11.81 ? 22  CYS B O   1 
ATOM   2309 C  CB  . CYS B  1 22  ? 1.821   12.311  9.541   1.00 9.73  ? 22  CYS B CB  1 
ATOM   2310 S  SG  . CYS B  1 22  ? 0.281   12.639  8.684   1.00 9.97  ? 22  CYS B SG  1 
ATOM   2311 N  N   . GLY B  1 23  ? 3.640   12.727  12.432  1.00 10.31 ? 23  GLY B N   1 
ATOM   2312 C  CA  . GLY B  1 23  ? 4.830   12.436  13.212  1.00 12.09 ? 23  GLY B CA  1 
ATOM   2313 C  C   . GLY B  1 23  ? 4.517   12.341  14.692  1.00 12.60 ? 23  GLY B C   1 
ATOM   2314 O  O   . GLY B  1 23  ? 5.461   12.396  15.534  1.00 15.37 ? 23  GLY B O   1 
ATOM   2315 N  N   . GLY B  1 24  ? 3.275   12.234  15.089  1.00 14.41 ? 24  GLY B N   1 
ATOM   2316 C  CA  . GLY B  1 24  ? 2.922   12.296  16.535  1.00 14.99 ? 24  GLY B CA  1 
ATOM   2317 C  C   . GLY B  1 24  ? 2.716   10.868  17.041  1.00 17.53 ? 24  GLY B C   1 
ATOM   2318 O  O   . GLY B  1 24  ? 3.265   9.914   16.455  1.00 19.90 ? 24  GLY B O   1 
ATOM   2319 N  N   . LEU B  1 25  ? 2.058   10.776  18.162  1.00 19.23 ? 25  LEU B N   1 
ATOM   2320 C  CA  . LEU B  1 25  ? 1.934   9.423   18.707  1.00 20.66 ? 25  LEU B CA  1 
ATOM   2321 C  C   . LEU B  1 25  ? 0.666   8.738   18.167  1.00 17.56 ? 25  LEU B C   1 
ATOM   2322 O  O   . LEU B  1 25  ? -0.177  9.326   17.443  1.00 16.16 ? 25  LEU B O   1 
ATOM   2323 C  CB  . LEU B  1 25  ? 2.052   9.357   20.247  1.00 26.06 ? 25  LEU B CB  1 
ATOM   2324 C  CG  . LEU B  1 25  ? 3.314   9.974   20.925  1.00 25.55 ? 25  LEU B CG  1 
ATOM   2325 C  CD1 . LEU B  1 25  ? 2.998   10.276  22.385  1.00 30.65 ? 25  LEU B CD1 1 
ATOM   2326 C  CD2 . LEU B  1 25  ? 4.590   9.137   20.704  1.00 30.19 ? 25  LEU B CD2 1 
ATOM   2327 N  N   . LEU B  1 26  ? 0.559   7.462   18.543  1.00 17.55 ? 26  LEU B N   1 
ATOM   2328 C  CA  . LEU B  1 26  ? -0.657  6.636   18.300  1.00 16.07 ? 26  LEU B CA  1 
ATOM   2329 C  C   . LEU B  1 26  ? -1.007  6.447   16.821  1.00 11.44 ? 26  LEU B C   1 
ATOM   2330 O  O   . LEU B  1 26  ? -2.166  6.377   16.445  1.00 13.35 ? 26  LEU B O   1 
ATOM   2331 C  CB  . LEU B  1 26  ? -1.920  7.168   19.021  1.00 19.62 ? 26  LEU B CB  1 
ATOM   2332 C  CG  . LEU B  1 26  ? -1.944  7.336   20.593  1.00 27.64 ? 26  LEU B CG  1 
ATOM   2333 C  CD1 . LEU B  1 26  ? -3.355  7.736   21.020  1.00 33.02 ? 26  LEU B CD1 1 
ATOM   2334 C  CD2 . LEU B  1 26  ? -1.447  6.115   21.355  1.00 24.25 ? 26  LEU B CD2 1 
ATOM   2335 N  N   . GLN B  1 27  ? 0.048   6.345   16.025  1.00 11.64 ? 27  GLN B N   1 
ATOM   2336 C  CA  . GLN B  1 27  ? -0.201  6.210   14.547  1.00 10.07 ? 27  GLN B CA  1 
ATOM   2337 C  C   . GLN B  1 27  ? -0.564  4.793   14.117  1.00 9.21  ? 27  GLN B C   1 
ATOM   2338 O  O   . GLN B  1 27  ? -0.131  3.781   14.730  1.00 10.36 ? 27  GLN B O   1 
ATOM   2339 C  CB  . GLN B  1 27  ? 1.065   6.652   13.774  1.00 9.76  ? 27  GLN B CB  1 
ATOM   2340 C  CG  . GLN B  1 27  ? 1.341   8.133   14.128  1.00 10.54 ? 27  GLN B CG  1 
ATOM   2341 C  CD  . GLN B  1 27  ? 0.291   8.990   13.441  1.00 9.46  ? 27  GLN B CD  1 
ATOM   2342 O  OE1 . GLN B  1 27  ? 0.292   9.140   12.198  1.00 10.21 ? 27  GLN B OE1 1 
ATOM   2343 N  NE2 . GLN B  1 27  ? -0.609  9.561   14.216  1.00 9.80  ? 27  GLN B NE2 1 
ATOM   2344 N  N   . SER B  1 28  ? -1.338  4.753   13.059  1.00 8.57  ? 28  SER B N   1 
ATOM   2345 C  CA  . SER B  1 28  ? -1.726  3.540   12.350  1.00 7.75  ? 28  SER B CA  1 
ATOM   2346 C  C   . SER B  1 28  ? -1.189  3.554   10.949  1.00 7.92  ? 28  SER B C   1 
ATOM   2347 O  O   . SER B  1 28  ? -0.927  4.614   10.395  1.00 8.27  ? 28  SER B O   1 
ATOM   2348 C  CB  . SER B  1 28  ? -3.251  3.478   12.353  1.00 9.10  ? 28  SER B CB  1 
ATOM   2349 O  OG  . SER B  1 28  ? -3.763  3.413   13.710  1.00 8.25  ? 28  SER B OG  1 
ATOM   2350 N  N   . PRO B  1 29  ? -1.072  2.384   10.287  1.00 7.25  ? 29  PRO B N   1 
ATOM   2351 C  CA  . PRO B  1 29  ? -1.431  1.034   10.768  1.00 7.69  ? 29  PRO B CA  1 
ATOM   2352 C  C   . PRO B  1 29  ? -0.293  0.439   11.558  1.00 6.68  ? 29  PRO B C   1 
ATOM   2353 O  O   . PRO B  1 29  ? 0.746   1.060   11.761  1.00 8.33  ? 29  PRO B O   1 
ATOM   2354 C  CB  . PRO B  1 29  ? -1.645  0.265   9.434   1.00 7.72  ? 29  PRO B CB  1 
ATOM   2355 C  CG  . PRO B  1 29  ? -0.511  0.878   8.554   1.00 7.49  ? 29  PRO B CG  1 
ATOM   2356 C  CD  . PRO B  1 29  ? -0.590  2.360   8.862   1.00 8.37  ? 29  PRO B CD  1 
ATOM   2357 N  N   . ILE B  1 30  ? -0.564  -0.768  12.046  1.00 7.41  ? 30  ILE B N   1 
ATOM   2358 C  CA  . ILE B  1 30  ? 0.457   -1.515  12.863  1.00 7.68  ? 30  ILE B CA  1 
ATOM   2359 C  C   . ILE B  1 30  ? 0.460   -2.968  12.449  1.00 7.98  ? 30  ILE B C   1 
ATOM   2360 O  O   . ILE B  1 30  ? -0.421  -3.456  11.750  1.00 7.47  ? 30  ILE B O   1 
ATOM   2361 C  CB  . ILE B  1 30  ? 0.101   -1.452  14.349  1.00 8.63  ? 30  ILE B CB  1 
ATOM   2362 C  CG1 . ILE B  1 30  ? -1.298  -1.922  14.651  1.00 8.22  ? 30  ILE B CG1 1 
ATOM   2363 C  CG2 . ILE B  1 30  ? 0.373   -0.016  14.838  1.00 8.77  ? 30  ILE B CG2 1 
ATOM   2364 C  CD1 . ILE B  1 30  ? -1.605  -2.033  16.165  1.00 11.07 ? 30  ILE B CD1 1 
ATOM   2365 N  N   . ASP B  1 31  ? 1.571   -3.610  12.882  1.00 8.16  ? 31  ASP B N   1 
ATOM   2366 C  CA  . ASP B  1 31  ? 1.686   -5.048  12.707  1.00 8.82  ? 31  ASP B CA  1 
ATOM   2367 C  C   . ASP B  1 31  ? 1.082   -5.729  13.935  1.00 10.06 ? 31  ASP B C   1 
ATOM   2368 O  O   . ASP B  1 31  ? 1.466   -5.481  15.060  1.00 11.86 ? 31  ASP B O   1 
ATOM   2369 C  CB  . ASP B  1 31  ? 3.168   -5.474  12.616  1.00 9.62  ? 31  ASP B CB  1 
ATOM   2370 C  CG  . ASP B  1 31  ? 3.277   -6.992  12.480  1.00 11.38 ? 31  ASP B CG  1 
ATOM   2371 O  OD1 . ASP B  1 31  ? 2.760   -7.543  11.541  1.00 10.68 ? 31  ASP B OD1 1 
ATOM   2372 O  OD2 . ASP B  1 31  ? 3.931   -7.575  13.334  1.00 15.03 ? 31  ASP B OD2 1 
ATOM   2373 N  N   . LEU B  1 32  ? 0.137   -6.640  13.619  1.00 9.51  ? 32  LEU B N   1 
ATOM   2374 C  CA  . LEU B  1 32  ? -0.578  -7.369  14.686  1.00 9.36  ? 32  LEU B CA  1 
ATOM   2375 C  C   . LEU B  1 32  ? 0.232   -8.666  14.914  1.00 10.32 ? 32  LEU B C   1 
ATOM   2376 O  O   . LEU B  1 32  ? 0.239   -9.545  14.085  1.00 12.66 ? 32  LEU B O   1 
ATOM   2377 C  CB  . LEU B  1 32  ? -2.008  -7.660  14.187  1.00 10.72 ? 32  LEU B CB  1 
ATOM   2378 C  CG  . LEU B  1 32  ? -2.827  -6.401  13.796  1.00 11.16 ? 32  LEU B CG  1 
ATOM   2379 C  CD1 . LEU B  1 32  ? -4.113  -6.844  13.084  1.00 12.85 ? 32  LEU B CD1 1 
ATOM   2380 C  CD2 . LEU B  1 32  ? -3.073  -5.506  15.024  1.00 13.90 ? 32  LEU B CD2 1 
ATOM   2381 N  N   . HIS B  1 33  ? 0.909   -8.766  16.050  1.00 10.21 ? 33  HIS B N   1 
ATOM   2382 C  CA  . HIS B  1 33  ? 1.766   -9.928  16.373  1.00 11.56 ? 33  HIS B CA  1 
ATOM   2383 C  C   . HIS B  1 33  ? 1.625   -10.249 17.861  1.00 10.31 ? 33  HIS B C   1 
ATOM   2384 O  O   . HIS B  1 33  ? 1.279   -9.404  18.679  1.00 11.30 ? 33  HIS B O   1 
ATOM   2385 C  CB  . HIS B  1 33  ? 3.254   -9.664  15.935  1.00 13.53 ? 33  HIS B CB  1 
ATOM   2386 C  CG  . HIS B  1 33  ? 3.902   -8.485  16.648  1.00 13.75 ? 33  HIS B CG  1 
ATOM   2387 N  ND1 . HIS B  1 33  ? 3.650   -7.206  16.323  1.00 16.36 ? 33  HIS B ND1 1 
ATOM   2388 C  CD2 . HIS B  1 33  ? 4.814   -8.446  17.710  1.00 14.04 ? 33  HIS B CD2 1 
ATOM   2389 C  CE1 . HIS B  1 33  ? 4.380   -6.374  17.147  1.00 20.18 ? 33  HIS B CE1 1 
ATOM   2390 N  NE2 . HIS B  1 33  ? 5.099   -7.159  17.975  1.00 16.85 ? 33  HIS B NE2 1 
ATOM   2391 N  N   . SER B  1 34  ? 2.022   -11.504 18.168  1.00 12.76 ? 34  SER B N   1 
ATOM   2392 C  CA  . SER B  1 34  ? 1.657   -12.079 19.507  1.00 12.61 ? 34  SER B CA  1 
ATOM   2393 C  C   . SER B  1 34  ? 2.111   -11.205 20.677  1.00 11.89 ? 34  SER B C   1 
ATOM   2394 O  O   . SER B  1 34  ? 1.409   -11.061 21.713  1.00 13.05 ? 34  SER B O   1 
ATOM   2395 C  CB  . SER B  1 34  ? 2.251   -13.515 19.607  1.00 14.54 ? 34  SER B CB  1 
ATOM   2396 O  OG  . SER B  1 34  ? 3.634   -13.454 19.508  1.00 18.56 ? 34  SER B OG  1 
ATOM   2397 N  N   . ASP B  1 35  ? 3.313   -10.592 20.606  1.00 11.61 ? 35  ASP B N   1 
ATOM   2398 C  CA  . ASP B  1 35  ? 3.855   -9.958  21.789  1.00 13.01 ? 35  ASP B CA  1 
ATOM   2399 C  C   . ASP B  1 35  ? 3.039   -8.837  22.343  1.00 13.22 ? 35  ASP B C   1 
ATOM   2400 O  O   . ASP B  1 35  ? 3.161   -8.390  23.508  1.00 17.47 ? 35  ASP B O   1 
ATOM   2401 C  CB  . ASP B  1 35  ? 5.253   -9.358  21.464  1.00 14.06 ? 35  ASP B CB  1 
ATOM   2402 C  CG  . ASP B  1 35  ? 6.170   -10.401 20.912  1.00 17.15 ? 35  ASP B CG  1 
ATOM   2403 O  OD1 . ASP B  1 35  ? 5.926   -10.892 19.769  1.00 17.05 ? 35  ASP B OD1 1 
ATOM   2404 O  OD2 . ASP B  1 35  ? 7.144   -10.782 21.654  1.00 15.84 ? 35  ASP B OD2 1 
ATOM   2405 N  N   . ILE B  1 36  ? 2.212   -8.277  21.471  1.00 12.73 ? 36  ILE B N   1 
ATOM   2406 C  CA  . ILE B  1 36  ? 1.446   -7.087  21.850  1.00 13.91 ? 36  ILE B CA  1 
ATOM   2407 C  C   . ILE B  1 36  ? -0.063  -7.302  21.881  1.00 12.54 ? 36  ILE B C   1 
ATOM   2408 O  O   . ILE B  1 36  ? -0.784  -6.335  22.080  1.00 14.79 ? 36  ILE B O   1 
ATOM   2409 C  CB  . ILE B  1 36  ? 1.811   -5.832  20.961  1.00 15.44 ? 36  ILE B CB  1 
ATOM   2410 C  CG1 . ILE B  1 36  ? 1.761   -6.046  19.464  1.00 18.62 ? 36  ILE B CG1 1 
ATOM   2411 C  CG2 . ILE B  1 36  ? 3.239   -5.397  21.299  1.00 20.45 ? 36  ILE B CG2 1 
ATOM   2412 C  CD1 . ILE B  1 36  ? 0.421   -6.304  18.886  1.00 18.41 ? 36  ILE B CD1 1 
ATOM   2413 N  N   . LEU B  1 37  ? -0.477  -8.557  21.701  1.00 11.95 ? 37  LEU B N   1 
ATOM   2414 C  CA  . LEU B  1 37  ? -1.925  -9.000  21.705  1.00 14.08 ? 37  LEU B CA  1 
ATOM   2415 C  C   . LEU B  1 37  ? -2.307  -9.357  23.101  1.00 16.37 ? 37  LEU B C   1 
ATOM   2416 O  O   . LEU B  1 37  ? -1.546  -10.060 23.798  1.00 17.56 ? 37  LEU B O   1 
ATOM   2417 C  CB  . LEU B  1 37  ? -2.172  -10.167 20.790  1.00 13.27 ? 37  LEU B CB  1 
ATOM   2418 C  CG  . LEU B  1 37  ? -1.923  -9.928  19.316  1.00 14.20 ? 37  LEU B CG  1 
ATOM   2419 C  CD1 . LEU B  1 37  ? -2.089  -11.098 18.378  1.00 16.52 ? 37  LEU B CD1 1 
ATOM   2420 C  CD2 . LEU B  1 37  ? -2.711  -8.769  18.756  1.00 14.56 ? 37  LEU B CD2 1 
ATOM   2421 N  N   . GLN B  1 38  ? -3.510  -8.946  23.512  1.00 13.07 ? 38  GLN B N   1 
ATOM   2422 C  CA  . GLN B  1 38  ? -4.018  -9.433  24.844  1.00 15.89 ? 38  GLN B CA  1 
ATOM   2423 C  C   . GLN B  1 38  ? -5.494  -9.615  24.716  1.00 15.89 ? 38  GLN B C   1 
ATOM   2424 O  O   . GLN B  1 38  ? -6.217  -8.688  24.338  1.00 13.29 ? 38  GLN B O   1 
ATOM   2425 C  CB  . GLN B  1 38  ? -3.799  -8.397  25.837  1.00 15.94 ? 38  GLN B CB  1 
ATOM   2426 C  CG  . GLN B  1 38  ? -4.166  -8.881  27.254  1.00 20.10 ? 38  GLN B CG  1 
ATOM   2427 C  CD  . GLN B  1 38  ? -3.622  -7.943  28.265  1.00 25.56 ? 38  GLN B CD  1 
ATOM   2428 O  OE1 . GLN B  1 38  ? -2.397  -7.983  28.537  1.00 37.88 ? 38  GLN B OE1 1 
ATOM   2429 N  NE2 . GLN B  1 38  ? -4.443  -7.086  28.807  1.00 27.20 ? 38  GLN B NE2 1 
ATOM   2430 N  N   . TYR B  1 39  ? -5.956  -10.790 25.141  1.00 14.47 ? 39  TYR B N   1 
ATOM   2431 C  CA  . TYR B  1 39  ? -7.381  -11.064 25.111  1.00 14.63 ? 39  TYR B CA  1 
ATOM   2432 C  C   . TYR B  1 39  ? -8.123  -10.187 26.106  1.00 13.10 ? 39  TYR B C   1 
ATOM   2433 O  O   . TYR B  1 39  ? -7.688  -9.921  27.231  1.00 15.61 ? 39  TYR B O   1 
ATOM   2434 C  CB  . TYR B  1 39  ? -7.600  -12.540 25.512  1.00 14.54 ? 39  TYR B CB  1 
ATOM   2435 C  CG  . TYR B  1 39  ? -9.033  -12.912 25.685  1.00 15.76 ? 39  TYR B CG  1 
ATOM   2436 C  CD1 . TYR B  1 39  ? -9.898  -12.917 24.614  1.00 15.32 ? 39  TYR B CD1 1 
ATOM   2437 C  CD2 . TYR B  1 39  ? -9.554  -13.240 26.971  1.00 17.08 ? 39  TYR B CD2 1 
ATOM   2438 C  CE1 . TYR B  1 39  ? -11.272 -13.222 24.740  1.00 16.91 ? 39  TYR B CE1 1 
ATOM   2439 C  CE2 . TYR B  1 39  ? -10.889 -13.603 27.114  1.00 16.64 ? 39  TYR B CE2 1 
ATOM   2440 C  CZ  . TYR B  1 39  ? -11.750 -13.641 26.008  1.00 16.27 ? 39  TYR B CZ  1 
ATOM   2441 O  OH  . TYR B  1 39  ? -13.058 -13.928 26.175  1.00 17.78 ? 39  TYR B OH  1 
ATOM   2442 N  N   . ASP B  1 40  ? -9.254  -9.654  25.652  1.00 12.61 ? 40  ASP B N   1 
ATOM   2443 C  CA  . ASP B  1 40  ? -10.111 -8.835  26.483  1.00 13.29 ? 40  ASP B CA  1 
ATOM   2444 C  C   . ASP B  1 40  ? -11.538 -9.377  26.330  1.00 14.33 ? 40  ASP B C   1 
ATOM   2445 O  O   . ASP B  1 40  ? -12.223 -9.129  25.337  1.00 13.02 ? 40  ASP B O   1 
ATOM   2446 C  CB  . ASP B  1 40  ? -10.003 -7.369  26.012  1.00 12.94 ? 40  ASP B CB  1 
ATOM   2447 C  CG  . ASP B  1 40  ? -10.811 -6.415  26.849  1.00 16.19 ? 40  ASP B CG  1 
ATOM   2448 O  OD1 . ASP B  1 40  ? -11.637 -6.914  27.677  1.00 17.52 ? 40  ASP B OD1 1 
ATOM   2449 O  OD2 . ASP B  1 40  ? -10.625 -5.158  26.652  1.00 19.89 ? 40  ASP B OD2 1 
ATOM   2450 N  N   . ALA B  1 41  ? -12.093 -10.056 27.368  1.00 12.92 ? 41  ALA B N   1 
ATOM   2451 C  CA  . ALA B  1 41  ? -13.433 -10.612 27.337  1.00 14.79 ? 41  ALA B CA  1 
ATOM   2452 C  C   . ALA B  1 41  ? -14.561 -9.568  27.268  1.00 15.08 ? 41  ALA B C   1 
ATOM   2453 O  O   . ALA B  1 41  ? -15.672 -9.911  26.911  1.00 17.25 ? 41  ALA B O   1 
ATOM   2454 C  CB  . ALA B  1 41  ? -13.599 -11.474 28.593  1.00 15.70 ? 41  ALA B CB  1 
ATOM   2455 N  N   . SER B  1 42  ? -14.244 -8.314  27.585  1.00 16.28 ? 42  SER B N   1 
ATOM   2456 C  CA  . SER B  1 42  ? -15.240 -7.283  27.411  1.00 15.25 ? 42  SER B CA  1 
ATOM   2457 C  C   . SER B  1 42  ? -15.513 -6.825  25.940  1.00 15.43 ? 42  SER B C   1 
ATOM   2458 O  O   . SER B  1 42  ? -16.389 -5.947  25.624  1.00 16.17 ? 42  SER B O   1 
ATOM   2459 C  CB  . SER B  1 42  ? -14.811 -6.038  28.223  1.00 22.89 ? 42  SER B CB  1 
ATOM   2460 O  OG  . SER B  1 42  ? -13.858 -5.227  27.583  1.00 24.53 ? 42  SER B OG  1 
ATOM   2461 N  N   . LEU B  1 43  ? -14.717 -7.346  25.008  1.00 12.76 ? 43  LEU B N   1 
ATOM   2462 C  CA  . LEU B  1 43  ? -14.916 -6.978  23.598  1.00 12.01 ? 43  LEU B CA  1 
ATOM   2463 C  C   . LEU B  1 43  ? -15.979 -7.882  23.024  1.00 11.12 ? 43  LEU B C   1 
ATOM   2464 O  O   . LEU B  1 43  ? -15.772 -8.908  22.338  1.00 13.57 ? 43  LEU B O   1 
ATOM   2465 C  CB  . LEU B  1 43  ? -13.607 -7.141  22.826  1.00 11.03 ? 43  LEU B CB  1 
ATOM   2466 C  CG  . LEU B  1 43  ? -12.527 -6.151  23.227  1.00 11.11 ? 43  LEU B CG  1 
ATOM   2467 C  CD1 . LEU B  1 43  ? -11.216 -6.451  22.503  1.00 12.78 ? 43  LEU B CD1 1 
ATOM   2468 C  CD2 . LEU B  1 43  ? -12.867 -4.665  23.088  1.00 13.45 ? 43  LEU B CD2 1 
ATOM   2469 N  N   . THR B  1 44  ? -17.204 -7.404  23.294  1.00 12.94 ? 44  THR B N   1 
ATOM   2470 C  CA  . THR B  1 44  ? -18.397 -8.109  22.863  1.00 11.91 ? 44  THR B CA  1 
ATOM   2471 C  C   . THR B  1 44  ? -18.768 -7.836  21.387  1.00 10.21 ? 44  THR B C   1 
ATOM   2472 O  O   . THR B  1 44  ? -18.154 -6.981  20.729  1.00 10.52 ? 44  THR B O   1 
ATOM   2473 C  CB  . THR B  1 44  ? -19.577 -7.716  23.800  1.00 13.72 ? 44  THR B CB  1 
ATOM   2474 O  OG1 . THR B  1 44  ? -19.600 -6.312  23.902  1.00 16.62 ? 44  THR B OG1 1 
ATOM   2475 C  CG2 . THR B  1 44  ? -19.345 -8.180  25.285  1.00 15.83 ? 44  THR B CG2 1 
ATOM   2476 N  N   . PRO B  1 45  ? -19.713 -8.560  20.766  1.00 11.88 ? 45  PRO B N   1 
ATOM   2477 C  CA  . PRO B  1 45  ? -19.942 -8.458  19.306  1.00 11.77 ? 45  PRO B CA  1 
ATOM   2478 C  C   . PRO B  1 45  ? -20.507 -7.106  18.913  1.00 13.48 ? 45  PRO B C   1 
ATOM   2479 O  O   . PRO B  1 45  ? -21.312 -6.526  19.674  1.00 13.67 ? 45  PRO B O   1 
ATOM   2480 C  CB  . PRO B  1 45  ? -20.893 -9.625  18.992  1.00 14.93 ? 45  PRO B CB  1 
ATOM   2481 C  CG  . PRO B  1 45  ? -20.558 -10.624 20.078  1.00 15.48 ? 45  PRO B CG  1 
ATOM   2482 C  CD  . PRO B  1 45  ? -20.399 -9.774  21.305  1.00 13.89 ? 45  PRO B CD  1 
ATOM   2483 N  N   . LEU B  1 46  ? -20.034 -6.574  17.794  1.00 11.27 ? 46  LEU B N   1 
ATOM   2484 C  CA  . LEU B  1 46  ? -20.708 -5.387  17.234  1.00 11.83 ? 46  LEU B CA  1 
ATOM   2485 C  C   . LEU B  1 46  ? -21.946 -5.834  16.471  1.00 11.41 ? 46  LEU B C   1 
ATOM   2486 O  O   . LEU B  1 46  ? -22.033 -6.943  15.957  1.00 13.61 ? 46  LEU B O   1 
ATOM   2487 C  CB  . LEU B  1 46  ? -19.710 -4.658  16.265  1.00 12.67 ? 46  LEU B CB  1 
ATOM   2488 C  CG  . LEU B  1 46  ? -18.476 -4.079  17.015  1.00 15.52 ? 46  LEU B CG  1 
ATOM   2489 C  CD1 . LEU B  1 46  ? -17.613 -3.510  15.922  1.00 16.60 ? 46  LEU B CD1 1 
ATOM   2490 C  CD2 . LEU B  1 46  ? -18.876 -3.029  18.061  1.00 17.89 ? 46  LEU B CD2 1 
ATOM   2491 N  N   . GLU B  1 47  ? -22.917 -4.908  16.427  1.00 13.63 ? 47  GLU B N   1 
ATOM   2492 C  CA  . GLU B  1 47  ? -24.017 -5.123  15.533  1.00 15.38 ? 47  GLU B CA  1 
ATOM   2493 C  C   . GLU B  1 47  ? -24.000 -3.998  14.430  1.00 14.27 ? 47  GLU B C   1 
ATOM   2494 O  O   . GLU B  1 47  ? -23.697 -2.820  14.725  1.00 17.29 ? 47  GLU B O   1 
ATOM   2495 C  CB  . GLU B  1 47  ? -25.376 -5.116  16.257  1.00 20.46 ? 47  GLU B CB  1 
ATOM   2496 C  CG  . GLU B  1 47  ? -25.462 -6.128  17.427  1.00 26.06 ? 47  GLU B CG  1 
ATOM   2497 C  CD  . GLU B  1 47  ? -26.827 -6.042  18.151  1.00 31.21 ? 47  GLU B CD  1 
ATOM   2498 O  OE1 . GLU B  1 47  ? -27.135 -5.039  18.883  1.00 38.44 ? 47  GLU B OE1 1 
ATOM   2499 O  OE2 . GLU B  1 47  ? -27.610 -6.967  17.921  1.00 36.47 ? 47  GLU B OE2 1 
ATOM   2500 N  N   . PHE B  1 48  ? -24.339 -4.476  13.247  1.00 14.31 ? 48  PHE B N   1 
ATOM   2501 C  CA  . PHE B  1 48  ? -24.259 -3.611  12.021  1.00 14.63 ? 48  PHE B CA  1 
ATOM   2502 C  C   . PHE B  1 48  ? -25.677 -3.251  11.540  1.00 15.08 ? 48  PHE B C   1 
ATOM   2503 O  O   . PHE B  1 48  ? -26.370 -4.147  11.017  1.00 20.53 ? 48  PHE B O   1 
ATOM   2504 C  CB  . PHE B  1 48  ? -23.440 -4.304  10.940  1.00 15.05 ? 48  PHE B CB  1 
ATOM   2505 C  CG  . PHE B  1 48  ? -22.144 -4.835  11.482  1.00 13.21 ? 48  PHE B CG  1 
ATOM   2506 C  CD1 . PHE B  1 48  ? -21.095 -4.021  11.838  1.00 13.00 ? 48  PHE B CD1 1 
ATOM   2507 C  CD2 . PHE B  1 48  ? -22.011 -6.242  11.669  1.00 14.11 ? 48  PHE B CD2 1 
ATOM   2508 C  CE1 . PHE B  1 48  ? -19.902 -4.543  12.432  1.00 14.29 ? 48  PHE B CE1 1 
ATOM   2509 C  CE2 . PHE B  1 48  ? -20.843 -6.755  12.243  1.00 16.23 ? 48  PHE B CE2 1 
ATOM   2510 C  CZ  . PHE B  1 48  ? -19.806 -5.902  12.624  1.00 15.45 ? 48  PHE B CZ  1 
ATOM   2511 N  N   . GLN B  1 49  ? -26.019 -1.991  11.797  1.00 15.50 ? 49  GLN B N   1 
ATOM   2512 C  CA  . GLN B  1 49  ? -27.411 -1.604  11.637  1.00 16.84 ? 49  GLN B CA  1 
ATOM   2513 C  C   . GLN B  1 49  ? -27.567 -0.710  10.402  1.00 13.58 ? 49  GLN B C   1 
ATOM   2514 O  O   . GLN B  1 49  ? -26.744 0.215   10.227  1.00 14.94 ? 49  GLN B O   1 
ATOM   2515 C  CB  . GLN B  1 49  ? -27.869 -0.867  12.844  1.00 18.96 ? 49  GLN B CB  1 
ATOM   2516 C  CG  . GLN B  1 49  ? -27.692 -1.604  14.132  1.00 27.25 ? 49  GLN B CG  1 
ATOM   2517 C  CD  . GLN B  1 49  ? -28.956 -2.275  14.636  1.00 41.54 ? 49  GLN B CD  1 
ATOM   2518 O  OE1 . GLN B  1 49  ? -29.138 -2.409  15.866  1.00 48.23 ? 49  GLN B OE1 1 
ATOM   2519 N  NE2 . GLN B  1 49  ? -29.847 -2.686  13.713  1.00 35.67 ? 49  GLN B NE2 1 
ATOM   2520 N  N   . GLY B  1 50  ? -28.527 -1.015  9.548   1.00 15.32 ? 50  GLY B N   1 
ATOM   2521 C  CA  . GLY B  1 50  ? -28.793 -0.134  8.395   1.00 12.65 ? 50  GLY B CA  1 
ATOM   2522 C  C   . GLY B  1 50  ? -27.697 -0.307  7.350   1.00 12.95 ? 50  GLY B C   1 
ATOM   2523 O  O   . GLY B  1 50  ? -27.591 0.458   6.422   1.00 14.87 ? 50  GLY B O   1 
ATOM   2524 N  N   . TYR B  1 51  ? -26.981 -1.415  7.478   1.00 11.57 ? 51  TYR B N   1 
ATOM   2525 C  CA  . TYR B  1 51  ? -26.006 -1.778  6.413   1.00 11.95 ? 51  TYR B CA  1 
ATOM   2526 C  C   . TYR B  1 51  ? -26.583 -2.320  5.119   1.00 12.14 ? 51  TYR B C   1 
ATOM   2527 O  O   . TYR B  1 51  ? -25.971 -2.352  4.043   1.00 11.43 ? 51  TYR B O   1 
ATOM   2528 C  CB  . TYR B  1 51  ? -24.967 -2.852  6.958   1.00 11.67 ? 51  TYR B CB  1 
ATOM   2529 C  CG  . TYR B  1 51  ? -23.776 -2.287  7.695   1.00 10.54 ? 51  TYR B CG  1 
ATOM   2530 C  CD1 . TYR B  1 51  ? -23.924 -1.333  8.696   1.00 10.97 ? 51  TYR B CD1 1 
ATOM   2531 C  CD2 . TYR B  1 51  ? -22.497 -2.717  7.389   1.00 11.19 ? 51  TYR B CD2 1 
ATOM   2532 C  CE1 . TYR B  1 51  ? -22.825 -0.826  9.351   1.00 11.18 ? 51  TYR B CE1 1 
ATOM   2533 C  CE2 . TYR B  1 51  ? -21.390 -2.219  8.049   1.00 11.04 ? 51  TYR B CE2 1 
ATOM   2534 C  CZ  . TYR B  1 51  ? -21.556 -1.277  9.032   1.00 11.14 ? 51  TYR B CZ  1 
ATOM   2535 O  OH  . TYR B  1 51  ? -20.462 -0.783  9.695   1.00 13.27 ? 51  TYR B OH  1 
ATOM   2536 N  N   . ASN B  1 52  ? -27.845 -2.817  5.124   1.00 13.13 ? 52  ASN B N   1 
ATOM   2537 C  CA  . ASN B  1 52  ? -28.431 -3.380  3.918   1.00 13.88 ? 52  ASN B CA  1 
ATOM   2538 C  C   . ASN B  1 52  ? -29.089 -2.250  3.119   1.00 15.40 ? 52  ASN B C   1 
ATOM   2539 O  O   . ASN B  1 52  ? -30.280 -1.880  3.313   1.00 16.82 ? 52  ASN B O   1 
ATOM   2540 C  CB  . ASN B  1 52  ? -29.568 -4.366  4.317   1.00 16.71 ? 52  ASN B CB  1 
ATOM   2541 C  CG  . ASN B  1 52  ? -30.129 -5.082  3.159   1.00 19.45 ? 52  ASN B CG  1 
ATOM   2542 O  OD1 . ASN B  1 52  ? -29.831 -4.850  1.995   1.00 24.63 ? 52  ASN B OD1 1 
ATOM   2543 N  ND2 . ASN B  1 52  ? -31.073 -6.000  3.483   1.00 25.22 ? 52  ASN B ND2 1 
ATOM   2544 N  N   . LEU B  1 53  ? -28.271 -1.597  2.285   1.00 13.94 ? 53  LEU B N   1 
ATOM   2545 C  CA  . LEU B  1 53  ? -28.741 -0.366  1.613   1.00 12.08 ? 53  LEU B CA  1 
ATOM   2546 C  C   . LEU B  1 53  ? -29.707 -0.843  0.438   1.00 11.08 ? 53  LEU B C   1 
ATOM   2547 O  O   . LEU B  1 53  ? -29.468 -1.793  -0.292  1.00 12.80 ? 53  LEU B O   1 
ATOM   2548 C  CB  . LEU B  1 53  ? -27.550 0.312   0.949   1.00 12.21 ? 53  LEU B CB  1 
ATOM   2549 C  CG  . LEU B  1 53  ? -26.422 0.653   1.906   1.00 14.27 ? 53  LEU B CG  1 
ATOM   2550 C  CD1 . LEU B  1 53  ? -25.320 1.394   1.117   1.00 14.42 ? 53  LEU B CD1 1 
ATOM   2551 C  CD2 . LEU B  1 53  ? -26.950 1.488   3.033   1.00 14.60 ? 53  LEU B CD2 1 
ATOM   2552 N  N   . SER B  1 54  ? -30.766 -0.038  0.193   1.00 11.19 ? 54  SER B N   1 
ATOM   2553 C  CA  . SER B  1 54  ? -31.681 -0.440  -0.842  1.00 12.64 ? 54  SER B CA  1 
ATOM   2554 C  C   . SER B  1 54  ? -31.078 -0.440  -2.233  1.00 12.57 ? 54  SER B C   1 
ATOM   2555 O  O   . SER B  1 54  ? -30.465 0.614   -2.558  1.00 10.61 ? 54  SER B O   1 
ATOM   2556 C  CB  . SER B  1 54  ? -32.817 0.558   -0.778  1.00 14.54 ? 54  SER B CB  1 
ATOM   2557 O  OG  . SER B  1 54  ? -33.712 0.298   -1.854  1.00 13.04 ? 54  SER B OG  1 
ATOM   2558 N  N   . ALA B  1 55  ? -31.258 -1.497  -3.053  1.00 13.33 ? 55  ALA B N   1 
ATOM   2559 C  CA  . ALA B  1 55  ? -30.800 -1.539  -4.424  1.00 13.21 ? 55  ALA B CA  1 
ATOM   2560 C  C   . ALA B  1 55  ? -31.477 -0.518  -5.308  1.00 11.90 ? 55  ALA B C   1 
ATOM   2561 O  O   . ALA B  1 55  ? -31.050 -0.299  -6.471  1.00 14.32 ? 55  ALA B O   1 
ATOM   2562 C  CB  . ALA B  1 55  ? -31.025 -2.914  -5.037  1.00 16.02 ? 55  ALA B CB  1 
ATOM   2563 N  N   . ASN B  1 56  ? -32.566 0.123   -4.800  1.00 13.60 ? 56  ASN B N   1 
ATOM   2564 C  CA  . ASN B  1 56  ? -33.273 1.080   -5.650  1.00 12.82 ? 56  ASN B CA  1 
ATOM   2565 C  C   . ASN B  1 56  ? -32.771 2.449   -5.335  1.00 11.73 ? 56  ASN B C   1 
ATOM   2566 O  O   . ASN B  1 56  ? -33.111 3.394   -6.036  1.00 14.54 ? 56  ASN B O   1 
ATOM   2567 C  CB  . ASN B  1 56  ? -34.815 1.048   -5.427  1.00 13.66 ? 56  ASN B CB  1 
ATOM   2568 C  CG  . ASN B  1 56  ? -35.406 -0.225  -5.877  1.00 16.90 ? 56  ASN B CG  1 
ATOM   2569 O  OD1 . ASN B  1 56  ? -34.846 -0.994  -6.661  1.00 17.08 ? 56  ASN B OD1 1 
ATOM   2570 N  ND2 . ASN B  1 56  ? -36.620 -0.429  -5.432  1.00 20.48 ? 56  ASN B ND2 1 
ATOM   2571 N  N   . LYS B  1 57  ? -31.906 2.630   -4.325  1.00 12.09 ? 57  LYS B N   1 
ATOM   2572 C  CA  . LYS B  1 57  ? -31.229 3.878   -4.015  1.00 11.97 ? 57  LYS B CA  1 
ATOM   2573 C  C   . LYS B  1 57  ? -29.789 3.775   -4.613  1.00 11.84 ? 57  LYS B C   1 
ATOM   2574 O  O   . LYS B  1 57  ? -29.357 2.682   -5.049  1.00 12.58 ? 57  LYS B O   1 
ATOM   2575 C  CB  . LYS B  1 57  ? -31.091 4.129   -2.517  1.00 12.99 ? 57  LYS B CB  1 
ATOM   2576 C  CG  . LYS B  1 57  ? -32.460 4.589   -1.939  1.00 14.95 ? 57  LYS B CG  1 
ATOM   2577 C  CD  . LYS B  1 57  ? -32.429 4.591   -0.405  1.00 19.60 ? 57  LYS B CD  1 
ATOM   2578 C  CE  . LYS B  1 57  ? -33.433 5.546   0.202   1.00 24.40 ? 57  LYS B CE  1 
ATOM   2579 N  NZ  . LYS B  1 57  ? -33.200 5.830   1.661   1.00 26.39 ? 57  LYS B NZ  1 
ATOM   2580 N  N   . GLN B  1 58  ? -29.142 4.901   -4.675  1.00 11.17 ? 58  GLN B N   1 
ATOM   2581 C  CA  . GLN B  1 58  ? -27.769 4.926   -5.249  1.00 11.93 ? 58  GLN B CA  1 
ATOM   2582 C  C   . GLN B  1 58  ? -26.883 5.838   -4.402  1.00 11.01 ? 58  GLN B C   1 
ATOM   2583 O  O   . GLN B  1 58  ? -27.271 6.788   -3.714  1.00 11.88 ? 58  GLN B O   1 
ATOM   2584 C  CB  . GLN B  1 58  ? -27.692 5.242   -6.736  1.00 18.75 ? 58  GLN B CB  1 
ATOM   2585 C  CG  . GLN B  1 58  ? -28.263 6.538   -7.039  1.00 19.25 ? 58  GLN B CG  1 
ATOM   2586 C  CD  . GLN B  1 58  ? -28.538 6.700   -8.550  1.00 25.02 ? 58  GLN B CD  1 
ATOM   2587 O  OE1 . GLN B  1 58  ? -28.440 5.756   -9.428  1.00 25.39 ? 58  GLN B OE1 1 
ATOM   2588 N  NE2 . GLN B  1 58  ? -28.843 7.965   -8.867  1.00 30.32 ? 58  GLN B NE2 1 
ATOM   2589 N  N   . PHE B  1 59  ? -25.584 5.384   -4.344  1.00 9.36  ? 59  PHE B N   1 
ATOM   2590 C  CA  . PHE B  1 59  ? -24.584 5.959   -3.481  1.00 10.08 ? 59  PHE B CA  1 
ATOM   2591 C  C   . PHE B  1 59  ? -23.370 6.415   -4.269  1.00 7.77  ? 59  PHE B C   1 
ATOM   2592 O  O   . PHE B  1 59  ? -22.992 5.745   -5.226  1.00 9.93  ? 59  PHE B O   1 
ATOM   2593 C  CB  . PHE B  1 59  ? -24.259 4.879   -2.435  1.00 10.40 ? 59  PHE B CB  1 
ATOM   2594 C  CG  . PHE B  1 59  ? -25.496 4.516   -1.633  1.00 11.59 ? 59  PHE B CG  1 
ATOM   2595 C  CD1 . PHE B  1 59  ? -26.394 3.569   -2.141  1.00 10.56 ? 59  PHE B CD1 1 
ATOM   2596 C  CD2 . PHE B  1 59  ? -25.821 5.263   -0.465  1.00 11.06 ? 59  PHE B CD2 1 
ATOM   2597 C  CE1 . PHE B  1 59  ? -27.607 3.363   -1.400  1.00 10.67 ? 59  PHE B CE1 1 
ATOM   2598 C  CE2 . PHE B  1 59  ? -27.054 5.031   0.240   1.00 9.98  ? 59  PHE B CE2 1 
ATOM   2599 C  CZ  . PHE B  1 59  ? -27.864 4.042   -0.253  1.00 10.20 ? 59  PHE B CZ  1 
ATOM   2600 N  N   . LEU B  1 60  ? -22.853 7.569   -3.842  1.00 8.91  ? 60  LEU B N   1 
ATOM   2601 C  CA  . LEU B  1 60  ? -21.807 8.238   -4.619  1.00 9.66  ? 60  LEU B CA  1 
ATOM   2602 C  C   . LEU B  1 60  ? -20.437 7.573   -4.409  1.00 8.45  ? 60  LEU B C   1 
ATOM   2603 O  O   . LEU B  1 60  ? -19.938 7.515   -3.276  1.00 10.05 ? 60  LEU B O   1 
ATOM   2604 C  CB  . LEU B  1 60  ? -21.756 9.705   -4.250  1.00 10.50 ? 60  LEU B CB  1 
ATOM   2605 C  CG  . LEU B  1 60  ? -20.897 10.586  -5.175  1.00 13.31 ? 60  LEU B CG  1 
ATOM   2606 C  CD1 . LEU B  1 60  ? -21.691 10.815  -6.413  1.00 13.55 ? 60  LEU B CD1 1 
ATOM   2607 C  CD2 . LEU B  1 60  ? -20.669 11.915  -4.456  1.00 14.62 ? 60  LEU B CD2 1 
ATOM   2608 N  N   . LEU B  1 61  ? -19.852 7.148   -5.508  1.00 9.54  ? 61  LEU B N   1 
ATOM   2609 C  CA  . LEU B  1 61  ? -18.482 6.634   -5.599  1.00 8.95  ? 61  LEU B CA  1 
ATOM   2610 C  C   . LEU B  1 61  ? -17.598 7.731   -6.182  1.00 9.57  ? 61  LEU B C   1 
ATOM   2611 O  O   . LEU B  1 61  ? -17.953 8.362   -7.159  1.00 11.72 ? 61  LEU B O   1 
ATOM   2612 C  CB  . LEU B  1 61  ? -18.447 5.466   -6.523  1.00 10.44 ? 61  LEU B CB  1 
ATOM   2613 C  CG  . LEU B  1 61  ? -17.165 4.616   -6.576  1.00 10.02 ? 61  LEU B CG  1 
ATOM   2614 C  CD1 . LEU B  1 61  ? -16.952 3.751   -5.288  1.00 10.54 ? 61  LEU B CD1 1 
ATOM   2615 C  CD2 . LEU B  1 61  ? -17.183 3.682   -7.786  1.00 11.73 ? 61  LEU B CD2 1 
ATOM   2616 N  N   . THR B  1 62  ? -16.459 8.007   -5.559  1.00 9.28  ? 62  THR B N   1 
ATOM   2617 C  CA  . THR B  1 62  ? -15.607 9.135   -5.980  1.00 9.92  ? 62  THR B CA  1 
ATOM   2618 C  C   . THR B  1 62  ? -14.153 8.690   -5.929  1.00 10.41 ? 62  THR B C   1 
ATOM   2619 O  O   . THR B  1 62  ? -13.728 7.970   -5.010  1.00 10.19 ? 62  THR B O   1 
ATOM   2620 C  CB  . THR B  1 62  ? -15.664 10.272  -4.971  1.00 11.98 ? 62  THR B CB  1 
ATOM   2621 O  OG1 . THR B  1 62  ? -17.032 10.754  -4.807  1.00 16.47 ? 62  THR B OG1 1 
ATOM   2622 C  CG2 . THR B  1 62  ? -14.856 11.521  -5.499  1.00 17.23 ? 62  THR B CG2 1 
ATOM   2623 N  N   . ASN B  1 63  ? -13.373 9.098   -6.907  1.00 8.74  ? 63  ASN B N   1 
ATOM   2624 C  CA  . ASN B  1 63  ? -11.913 9.024   -6.836  1.00 8.67  ? 63  ASN B CA  1 
ATOM   2625 C  C   . ASN B  1 63  ? -11.449 10.292  -6.238  1.00 8.86  ? 63  ASN B C   1 
ATOM   2626 O  O   . ASN B  1 63  ? -11.609 11.386  -6.808  1.00 7.75  ? 63  ASN B O   1 
ATOM   2627 C  CB  . ASN B  1 63  ? -11.407 8.804   -8.280  1.00 8.59  ? 63  ASN B CB  1 
ATOM   2628 C  CG  . ASN B  1 63  ? -9.921  8.833   -8.392  1.00 8.14  ? 63  ASN B CG  1 
ATOM   2629 O  OD1 . ASN B  1 63  ? -9.212  9.475   -7.568  1.00 7.80  ? 63  ASN B OD1 1 
ATOM   2630 N  ND2 . ASN B  1 63  ? -9.405  8.142   -9.444  1.00 8.35  ? 63  ASN B ND2 1 
ATOM   2631 N  N   . ASN B  1 64  ? -10.863 10.241  -5.048  1.00 9.42  ? 64  ASN B N   1 
ATOM   2632 C  CA  . ASN B  1 64  ? -10.436 11.469  -4.374  1.00 8.90  ? 64  ASN B CA  1 
ATOM   2633 C  C   . ASN B  1 64  ? -8.941  11.848  -4.597  1.00 9.86  ? 64  ASN B C   1 
ATOM   2634 O  O   . ASN B  1 64  ? -8.393  12.700  -3.892  1.00 10.64 ? 64  ASN B O   1 
ATOM   2635 C  CB  . ASN B  1 64  ? -10.782 11.449  -2.857  1.00 11.06 ? 64  ASN B CB  1 
ATOM   2636 C  CG  . ASN B  1 64  ? -9.980  10.439  -2.113  1.00 13.68 ? 64  ASN B CG  1 
ATOM   2637 O  OD1 . ASN B  1 64  ? -9.119  9.781   -2.648  1.00 9.53  ? 64  ASN B OD1 1 
ATOM   2638 N  ND2 . ASN B  1 64  ? -10.320 10.219  -0.816  1.00 16.73 ? 64  ASN B ND2 1 
ATOM   2639 N  N   . GLY B  1 65  ? -8.313  11.152  -5.544  1.00 8.39  ? 65  GLY B N   1 
ATOM   2640 C  CA  . GLY B  1 65  ? -6.874  11.321  -5.771  1.00 9.70  ? 65  GLY B CA  1 
ATOM   2641 C  C   . GLY B  1 65  ? -5.990  10.446  -4.913  1.00 9.03  ? 65  GLY B C   1 
ATOM   2642 O  O   . GLY B  1 65  ? -4.778  10.326  -5.171  1.00 9.03  ? 65  GLY B O   1 
ATOM   2643 N  N   . HIS B  1 66  ? -6.564  9.753   -3.917  1.00 8.28  ? 66  HIS B N   1 
ATOM   2644 C  CA  . HIS B  1 66  ? -5.802  8.852   -3.006  1.00 8.14  ? 66  HIS B CA  1 
ATOM   2645 C  C   . HIS B  1 66  ? -6.353  7.478   -2.855  1.00 8.73  ? 66  HIS B C   1 
ATOM   2646 O  O   . HIS B  1 66  ? -5.554  6.565   -2.496  1.00 8.84  ? 66  HIS B O   1 
ATOM   2647 C  CB  . HIS B  1 66  ? -5.749  9.491   -1.620  1.00 9.12  ? 66  HIS B CB  1 
ATOM   2648 C  CG  . HIS B  1 66  ? -5.161  10.892  -1.643  1.00 10.07 ? 66  HIS B CG  1 
ATOM   2649 N  ND1 . HIS B  1 66  ? -3.842  11.133  -1.856  1.00 11.19 ? 66  HIS B ND1 1 
ATOM   2650 C  CD2 . HIS B  1 66  ? -5.774  12.070  -1.422  1.00 11.06 ? 66  HIS B CD2 1 
ATOM   2651 C  CE1 . HIS B  1 66  ? -3.664  12.496  -1.830  1.00 10.38 ? 66  HIS B CE1 1 
ATOM   2652 N  NE2 . HIS B  1 66  ? -4.843  13.050  -1.524  1.00 12.89 ? 66  HIS B NE2 1 
ATOM   2653 N  N   . SER B  1 67  ? -7.651  7.324   -2.993  1.00 7.59  ? 67  SER B N   1 
ATOM   2654 C  CA  . SER B  1 67  ? -8.340  5.990   -2.961  1.00 7.53  ? 67  SER B CA  1 
ATOM   2655 C  C   . SER B  1 67  ? -9.600  6.186   -3.766  1.00 8.01  ? 67  SER B C   1 
ATOM   2656 O  O   . SER B  1 67  ? -9.861  7.254   -4.396  1.00 9.17  ? 67  SER B O   1 
ATOM   2657 C  CB  . SER B  1 67  ? -8.724  5.652   -1.490  1.00 8.67  ? 67  SER B CB  1 
ATOM   2658 O  OG  . SER B  1 67  ? -9.233  4.368   -1.395  1.00 8.77  ? 67  SER B OG  1 
ATOM   2659 N  N   . VAL B  1 68  ? -10.345 5.070   -3.796  1.00 8.01  ? 68  VAL B N   1 
ATOM   2660 C  CA  . VAL B  1 68  ? -11.728 5.171   -4.325  1.00 8.55  ? 68  VAL B CA  1 
ATOM   2661 C  C   . VAL B  1 68  ? -12.612 5.025   -3.081  1.00 9.13  ? 68  VAL B C   1 
ATOM   2662 O  O   . VAL B  1 68  ? -12.415 4.093   -2.282  1.00 9.63  ? 68  VAL B O   1 
ATOM   2663 C  CB  . VAL B  1 68  ? -11.940 4.074   -5.383  1.00 9.66  ? 68  VAL B CB  1 
ATOM   2664 C  CG1 . VAL B  1 68  ? -11.699 2.675   -4.915  1.00 11.00 ? 68  VAL B CG1 1 
ATOM   2665 C  CG2 . VAL B  1 68  ? -13.338 4.201   -6.030  1.00 13.76 ? 68  VAL B CG2 1 
ATOM   2666 N  N   . LYS B  1 69  ? -13.566 5.950   -2.960  1.00 8.85  ? 69  LYS B N   1 
ATOM   2667 C  CA  . LYS B  1 69  ? -14.480 5.963   -1.768  1.00 9.19  ? 69  LYS B CA  1 
ATOM   2668 C  C   . LYS B  1 69  ? -15.940 5.914   -2.176  1.00 9.25  ? 69  LYS B C   1 
ATOM   2669 O  O   . LYS B  1 69  ? -16.357 6.460   -3.175  1.00 11.05 ? 69  LYS B O   1 
ATOM   2670 C  CB  . LYS B  1 69  ? -14.162 7.197   -0.934  1.00 13.83 ? 69  LYS B CB  1 
ATOM   2671 C  CG  . LYS B  1 69  ? -14.529 8.528   -1.486  1.00 14.82 ? 69  LYS B CG  1 
ATOM   2672 C  CD  . LYS B  1 69  ? -14.663 9.538   -0.270  1.00 17.81 ? 69  LYS B CD  1 
ATOM   2673 C  CE  . LYS B  1 69  ? -14.895 10.862  -0.914  1.00 20.70 ? 69  LYS B CE  1 
ATOM   2674 N  NZ  . LYS B  1 69  ? -14.918 11.840  0.227   1.00 22.00 ? 69  LYS B NZ  1 
ATOM   2675 N  N   . LEU B  1 70  ? -16.732 5.223   -1.346  1.00 8.37  ? 70  LEU B N   1 
ATOM   2676 C  CA  . LEU B  1 70  ? -18.195 5.146   -1.526  1.00 7.94  ? 70  LEU B CA  1 
ATOM   2677 C  C   . LEU B  1 70  ? -18.721 5.862   -0.327  1.00 8.51  ? 70  LEU B C   1 
ATOM   2678 O  O   . LEU B  1 70  ? -18.525 5.501   0.822   1.00 8.75  ? 70  LEU B O   1 
ATOM   2679 C  CB  . LEU B  1 70  ? -18.587 3.667   -1.558  1.00 8.83  ? 70  LEU B CB  1 
ATOM   2680 C  CG  . LEU B  1 70  ? -20.121 3.464   -1.706  1.00 9.43  ? 70  LEU B CG  1 
ATOM   2681 C  CD1 . LEU B  1 70  ? -20.558 3.949   -3.084  1.00 11.14 ? 70  LEU B CD1 1 
ATOM   2682 C  CD2 . LEU B  1 70  ? -20.462 1.980   -1.476  1.00 11.87 ? 70  LEU B CD2 1 
ATOM   2683 N  N   . ASN B  1 71  ? -19.583 6.899   -0.546  1.00 9.29  ? 71  ASN B N   1 
ATOM   2684 C  CA  . ASN B  1 71  ? -20.277 7.605   0.575   1.00 9.83  ? 71  ASN B CA  1 
ATOM   2685 C  C   . ASN B  1 71  ? -21.440 6.732   1.062   1.00 10.32 ? 71  ASN B C   1 
ATOM   2686 O  O   . ASN B  1 71  ? -22.070 5.958   0.309   1.00 11.69 ? 71  ASN B O   1 
ATOM   2687 C  CB  . ASN B  1 71  ? -20.860 8.940   0.014   1.00 10.66 ? 71  ASN B CB  1 
ATOM   2688 C  CG  . ASN B  1 71  ? -19.807 9.986   -0.217  1.00 14.75 ? 71  ASN B CG  1 
ATOM   2689 O  OD1 . ASN B  1 71  ? -18.627 9.796   0.040   1.00 16.58 ? 71  ASN B OD1 1 
ATOM   2690 N  ND2 . ASN B  1 71  ? -20.294 11.174  -0.655  1.00 18.08 ? 71  ASN B ND2 1 
ATOM   2691 N  N   . LEU B  1 72  ? -21.593 6.803   2.357   1.00 11.19 ? 72  LEU B N   1 
ATOM   2692 C  CA  . LEU B  1 72  ? -22.576 5.938   3.003   1.00 10.45 ? 72  LEU B CA  1 
ATOM   2693 C  C   . LEU B  1 72  ? -23.523 6.872   3.812   1.00 11.24 ? 72  LEU B C   1 
ATOM   2694 O  O   . LEU B  1 72  ? -23.148 7.953   4.281   1.00 11.71 ? 72  LEU B O   1 
ATOM   2695 C  CB  . LEU B  1 72  ? -21.817 5.045   4.042   1.00 11.30 ? 72  LEU B CB  1 
ATOM   2696 C  CG  . LEU B  1 72  ? -20.877 4.043   3.299   1.00 10.91 ? 72  LEU B CG  1 
ATOM   2697 C  CD1 . LEU B  1 72  ? -19.973 3.403   4.368   1.00 11.59 ? 72  LEU B CD1 1 
ATOM   2698 C  CD2 . LEU B  1 72  ? -21.620 3.043   2.467   1.00 11.10 ? 72  LEU B CD2 1 
ATOM   2699 N  N   . PRO B  1 73  ? -24.757 6.383   4.036   1.00 11.69 ? 73  PRO B N   1 
ATOM   2700 C  CA  . PRO B  1 73  ? -25.791 7.214   4.671   1.00 13.58 ? 73  PRO B CA  1 
ATOM   2701 C  C   . PRO B  1 73  ? -25.665 7.160   6.172   1.00 16.12 ? 73  PRO B C   1 
ATOM   2702 O  O   . PRO B  1 73  ? -25.170 6.136   6.750   1.00 15.36 ? 73  PRO B O   1 
ATOM   2703 C  CB  . PRO B  1 73  ? -27.067 6.541   4.208   1.00 12.96 ? 73  PRO B CB  1 
ATOM   2704 C  CG  . PRO B  1 73  ? -26.710 5.015   4.135   1.00 13.16 ? 73  PRO B CG  1 
ATOM   2705 C  CD  . PRO B  1 73  ? -25.326 5.143   3.499   1.00 12.12 ? 73  PRO B CD  1 
ATOM   2706 N  N   . SER B  1 74  ? -26.081 8.226   6.820   1.00 18.45 ? 74  SER B N   1 
ATOM   2707 C  CA  . SER B  1 74  ? -25.828 8.278   8.279   1.00 19.24 ? 74  SER B CA  1 
ATOM   2708 C  C   . SER B  1 74  ? -26.794 7.412   9.089   1.00 15.92 ? 74  SER B C   1 
ATOM   2709 O  O   . SER B  1 74  ? -26.464 7.185   10.293  1.00 19.45 ? 74  SER B O   1 
ATOM   2710 C  CB  . SER B  1 74  ? -25.862 9.708   8.814   1.00 24.68 ? 74  SER B CB  1 
ATOM   2711 O  OG  . SER B  1 74  ? -27.120 10.291  8.511   1.00 26.01 ? 74  SER B OG  1 
ATOM   2712 N  N   . ASP B  1 75  ? -27.767 6.794   8.424   1.00 17.48 ? 75  ASP B N   1 
ATOM   2713 C  CA  . ASP B  1 75  ? -28.694 5.871   9.142   1.00 20.33 ? 75  ASP B CA  1 
ATOM   2714 C  C   . ASP B  1 75  ? -28.011 4.508   9.352   1.00 20.61 ? 75  ASP B C   1 
ATOM   2715 O  O   . ASP B  1 75  ? -28.488 3.649   10.069  1.00 19.30 ? 75  ASP B O   1 
ATOM   2716 C  CB  . ASP B  1 75  ? -30.023 5.761   8.398   1.00 23.84 ? 75  ASP B CB  1 
ATOM   2717 C  CG  . ASP B  1 75  ? -29.945 4.939   7.119   1.00 36.46 ? 75  ASP B CG  1 
ATOM   2718 O  OD1 . ASP B  1 75  ? -29.642 5.478   6.007   1.00 30.66 ? 75  ASP B OD1 1 
ATOM   2719 O  OD2 . ASP B  1 75  ? -30.270 3.710   7.214   1.00 45.53 ? 75  ASP B OD2 1 
ATOM   2720 N  N   . MET B  1 76  ? -26.852 4.360   8.711   1.00 16.99 ? 76  MET B N   1 
ATOM   2721 C  CA  . MET B  1 76  ? -26.051 3.143   8.825   1.00 15.34 ? 76  MET B CA  1 
ATOM   2722 C  C   . MET B  1 76  ? -25.125 3.369   10.014  1.00 14.18 ? 76  MET B C   1 
ATOM   2723 O  O   . MET B  1 76  ? -24.442 4.403   10.181  1.00 14.03 ? 76  MET B O   1 
ATOM   2724 C  CB  . MET B  1 76  ? -25.350 2.963   7.467   1.00 15.23 ? 76  MET B CB  1 
ATOM   2725 C  CG  . MET B  1 76  ? -24.303 1.898   7.476   1.00 17.35 ? 76  MET B CG  1 
ATOM   2726 S  SD  . MET B  1 76  ? -23.655 1.717   5.751   1.00 15.15 ? 76  MET B SD  1 
ATOM   2727 C  CE  . MET B  1 76  ? -22.191 0.820   6.229   1.00 13.49 ? 76  MET B CE  1 
ATOM   2728 N  N   . HIS B  1 77  ? -25.145 2.415   10.987  1.00 13.51 ? 77  HIS B N   1 
ATOM   2729 C  CA  . HIS B  1 77  ? -24.353 2.606   12.221  1.00 15.07 ? 77  HIS B CA  1 
ATOM   2730 C  C   . HIS B  1 77  ? -23.892 1.327   12.844  1.00 12.32 ? 77  HIS B C   1 
ATOM   2731 O  O   . HIS B  1 77  ? -24.342 0.286   12.442  1.00 14.63 ? 77  HIS B O   1 
ATOM   2732 C  CB  . HIS B  1 77  ? -25.069 3.500   13.285  1.00 20.05 ? 77  HIS B CB  1 
ATOM   2733 C  CG  . HIS B  1 77  ? -26.391 2.958   13.696  1.00 23.71 ? 77  HIS B CG  1 
ATOM   2734 N  ND1 . HIS B  1 77  ? -27.530 3.043   12.907  1.00 23.27 ? 77  HIS B ND1 1 
ATOM   2735 C  CD2 . HIS B  1 77  ? -26.760 2.288   14.877  1.00 27.65 ? 77  HIS B CD2 1 
ATOM   2736 C  CE1 . HIS B  1 77  ? -28.551 2.404   13.566  1.00 25.35 ? 77  HIS B CE1 1 
ATOM   2737 N  NE2 . HIS B  1 77  ? -28.082 1.963   14.767  1.00 26.64 ? 77  HIS B NE2 1 
ATOM   2738 N  N   . ILE B  1 78  ? -22.898 1.470   13.661  1.00 13.83 ? 78  ILE B N   1 
ATOM   2739 C  CA  . ILE B  1 78  ? -22.471 0.316   14.513  1.00 17.48 ? 78  ILE B CA  1 
ATOM   2740 C  C   . ILE B  1 78  ? -23.155 0.488   15.845  1.00 18.65 ? 78  ILE B C   1 
ATOM   2741 O  O   . ILE B  1 78  ? -23.142 1.612   16.401  1.00 20.37 ? 78  ILE B O   1 
ATOM   2742 C  CB  . ILE B  1 78  ? -20.981 0.437   14.786  1.00 18.11 ? 78  ILE B CB  1 
ATOM   2743 C  CG1 . ILE B  1 78  ? -20.120 0.252   13.542  1.00 21.79 ? 78  ILE B CG1 1 
ATOM   2744 C  CG2 . ILE B  1 78  ? -20.514 -0.615  15.840  1.00 17.60 ? 78  ILE B CG2 1 
ATOM   2745 C  CD1 . ILE B  1 78  ? -18.697 0.814   13.712  1.00 17.68 ? 78  ILE B CD1 1 
ATOM   2746 N  N   . GLN B  1 79  ? -23.751 -0.607  16.325  1.00 18.63 ? 79  GLN B N   1 
ATOM   2747 C  CA  . GLN B  1 79  ? -24.372 -0.763  17.702  1.00 21.90 ? 79  GLN B CA  1 
ATOM   2748 C  C   . GLN B  1 79  ? -23.347 -1.643  18.502  1.00 20.20 ? 79  GLN B C   1 
ATOM   2749 O  O   . GLN B  1 79  ? -22.858 -2.675  17.968  1.00 19.53 ? 79  GLN B O   1 
ATOM   2750 C  CB  . GLN B  1 79  ? -25.748 -1.454  17.499  1.00 22.61 ? 79  GLN B CB  1 
ATOM   2751 C  CG  . GLN B  1 79  ? -26.579 -1.812  18.758  1.00 34.34 ? 79  GLN B CG  1 
ATOM   2752 C  CD  . GLN B  1 79  ? -26.937 -0.618  19.640  1.00 35.26 ? 79  GLN B CD  1 
ATOM   2753 O  OE1 . GLN B  1 79  ? -27.300 0.440   19.159  1.00 36.53 ? 79  GLN B OE1 1 
ATOM   2754 N  NE2 . GLN B  1 79  ? -26.869 -0.813  20.959  1.00 40.77 ? 79  GLN B NE2 1 
ATOM   2755 N  N   . GLY B  1 80  ? -23.006 -1.228  19.715  1.00 21.62 ? 80  GLY B N   1 
ATOM   2756 C  CA  . GLY B  1 80  ? -22.158 -2.081  20.560  1.00 22.60 ? 80  GLY B CA  1 
ATOM   2757 C  C   . GLY B  1 80  ? -20.990 -1.318  21.128  1.00 20.92 ? 80  GLY B C   1 
ATOM   2758 O  O   . GLY B  1 80  ? -20.382 -1.733  22.162  1.00 20.58 ? 80  GLY B O   1 
ATOM   2759 N  N   . LEU B  1 81  ? -20.665 -0.162  20.519  1.00 18.37 ? 81  LEU B N   1 
ATOM   2760 C  CA  . LEU B  1 81  ? -19.625 0.678   21.113  1.00 17.91 ? 81  LEU B CA  1 
ATOM   2761 C  C   . LEU B  1 81  ? -20.287 1.536   22.229  1.00 21.24 ? 81  LEU B C   1 
ATOM   2762 O  O   . LEU B  1 81  ? -21.521 1.452   22.457  1.00 21.14 ? 81  LEU B O   1 
ATOM   2763 C  CB  . LEU B  1 81  ? -18.853 1.553   20.059  1.00 19.43 ? 81  LEU B CB  1 
ATOM   2764 C  CG  . LEU B  1 81  ? -18.116 0.697   19.022  1.00 17.73 ? 81  LEU B CG  1 
ATOM   2765 C  CD1 . LEU B  1 81  ? -17.565 1.547   17.885  1.00 18.51 ? 81  LEU B CD1 1 
ATOM   2766 C  CD2 . LEU B  1 81  ? -16.899 0.100   19.813  1.00 17.78 ? 81  LEU B CD2 1 
ATOM   2767 N  N   . GLN B  1 82  ? -19.541 2.380   22.900  1.00 19.45 ? 82  GLN B N   1 
ATOM   2768 C  CA  . GLN B  1 82  ? -20.209 3.135   24.030  1.00 25.81 ? 82  GLN B CA  1 
ATOM   2769 C  C   . GLN B  1 82  ? -20.886 4.408   23.569  1.00 29.22 ? 82  GLN B C   1 
ATOM   2770 O  O   . GLN B  1 82  ? -21.486 5.098   24.378  1.00 29.91 ? 82  GLN B O   1 
ATOM   2771 C  CB  . GLN B  1 82  ? -19.226 3.480   25.105  1.00 29.32 ? 82  GLN B CB  1 
ATOM   2772 C  CG  . GLN B  1 82  ? -17.796 3.095   24.784  1.00 42.37 ? 82  GLN B CG  1 
ATOM   2773 C  CD  . GLN B  1 82  ? -17.023 2.765   26.059  1.00 43.93 ? 82  GLN B CD  1 
ATOM   2774 O  OE1 . GLN B  1 82  ? -17.321 1.784   26.767  1.00 48.37 ? 82  GLN B OE1 1 
ATOM   2775 N  NE2 . GLN B  1 82  ? -16.056 3.604   26.374  1.00 40.82 ? 82  GLN B NE2 1 
ATOM   2776 N  N   . SER B  1 83  ? -20.743 4.725   22.274  1.00 25.74 ? 83  SER B N   1 
ATOM   2777 C  CA  . SER B  1 83  ? -21.618 5.705   21.546  1.00 23.40 ? 83  SER B CA  1 
ATOM   2778 C  C   . SER B  1 83  ? -22.041 5.058   20.269  1.00 23.87 ? 83  SER B C   1 
ATOM   2779 O  O   . SER B  1 83  ? -21.447 4.072   19.880  1.00 20.28 ? 83  SER B O   1 
ATOM   2780 C  CB  . SER B  1 83  ? -20.836 6.982   21.188  1.00 28.58 ? 83  SER B CB  1 
ATOM   2781 O  OG  . SER B  1 83  ? -20.564 7.729   22.334  1.00 31.55 ? 83  SER B OG  1 
ATOM   2782 N  N   A ARG B  1 84  ? -23.089 5.586   19.616  0.50 21.62 ? 84  ARG B N   1 
ATOM   2783 N  N   B ARG B  1 84  ? -23.071 5.594   19.631  0.50 23.45 ? 84  ARG B N   1 
ATOM   2784 C  CA  A ARG B  1 84  ? -23.465 5.162   18.267  0.50 19.80 ? 84  ARG B CA  1 
ATOM   2785 C  CA  B ARG B  1 84  ? -23.422 5.160   18.316  0.50 22.42 ? 84  ARG B CA  1 
ATOM   2786 C  C   A ARG B  1 84  ? -22.468 5.806   17.298  0.50 18.86 ? 84  ARG B C   1 
ATOM   2787 C  C   B ARG B  1 84  ? -22.378 5.784   17.381  0.50 20.76 ? 84  ARG B C   1 
ATOM   2788 O  O   A ARG B  1 84  ? -22.189 7.003   17.330  0.50 18.99 ? 84  ARG B O   1 
ATOM   2789 O  O   B ARG B  1 84  ? -21.974 6.939   17.536  0.50 20.92 ? 84  ARG B O   1 
ATOM   2790 C  CB  A ARG B  1 84  ? -24.905 5.570   17.893  0.50 21.96 ? 84  ARG B CB  1 
ATOM   2791 C  CB  B ARG B  1 84  ? -24.810 5.656   17.972  0.50 26.65 ? 84  ARG B CB  1 
ATOM   2792 C  CG  A ARG B  1 84  ? -25.144 5.503   16.377  0.50 21.76 ? 84  ARG B CG  1 
ATOM   2793 C  CG  B ARG B  1 84  ? -24.996 5.756   16.485  0.50 29.01 ? 84  ARG B CG  1 
ATOM   2794 C  CD  A ARG B  1 84  ? -26.491 6.076   15.923  0.50 22.02 ? 84  ARG B CD  1 
ATOM   2795 C  CD  B ARG B  1 84  ? -26.455 5.604   16.175  0.50 31.14 ? 84  ARG B CD  1 
ATOM   2796 N  NE  A ARG B  1 84  ? -26.616 6.203   14.464  0.50 20.16 ? 84  ARG B NE  1 
ATOM   2797 N  NE  B ARG B  1 84  ? -27.104 6.887   15.955  0.50 32.95 ? 84  ARG B NE  1 
ATOM   2798 C  CZ  A ARG B  1 84  ? -27.740 6.056   13.779  0.50 19.30 ? 84  ARG B CZ  1 
ATOM   2799 C  CZ  B ARG B  1 84  ? -28.410 6.945   15.750  0.50 31.66 ? 84  ARG B CZ  1 
ATOM   2800 N  NH1 A ARG B  1 84  ? -28.867 5.752   14.396  0.50 18.86 ? 84  ARG B NH1 1 
ATOM   2801 N  NH1 B ARG B  1 84  ? -29.064 5.791   15.788  0.50 26.74 ? 84  ARG B NH1 1 
ATOM   2802 N  NH2 A ARG B  1 84  ? -27.748 6.157   12.473  0.50 17.63 ? 84  ARG B NH2 1 
ATOM   2803 N  NH2 B ARG B  1 84  ? -29.034 8.103   15.528  0.50 31.63 ? 84  ARG B NH2 1 
ATOM   2804 N  N   . TYR B  1 85  ? -21.889 4.964   16.455  1.00 17.48 ? 85  TYR B N   1 
ATOM   2805 C  CA  . TYR B  1 85  ? -21.026 5.506   15.370  1.00 14.37 ? 85  TYR B CA  1 
ATOM   2806 C  C   . TYR B  1 85  ? -21.740 5.323   14.142  1.00 12.78 ? 85  TYR B C   1 
ATOM   2807 O  O   . TYR B  1 85  ? -22.114 4.205   13.807  1.00 15.67 ? 85  TYR B O   1 
ATOM   2808 C  CB  . TYR B  1 85  ? -19.651 4.792   15.388  1.00 13.05 ? 85  TYR B CB  1 
ATOM   2809 C  CG  . TYR B  1 85  ? -18.785 5.317   16.458  1.00 14.48 ? 85  TYR B CG  1 
ATOM   2810 C  CD1 . TYR B  1 85  ? -18.945 4.851   17.787  1.00 17.31 ? 85  TYR B CD1 1 
ATOM   2811 C  CD2 . TYR B  1 85  ? -17.785 6.220   16.211  1.00 13.70 ? 85  TYR B CD2 1 
ATOM   2812 C  CE1 . TYR B  1 85  ? -18.110 5.310   18.766  1.00 16.68 ? 85  TYR B CE1 1 
ATOM   2813 C  CE2 . TYR B  1 85  ? -16.941 6.686   17.154  1.00 15.46 ? 85  TYR B CE2 1 
ATOM   2814 C  CZ  . TYR B  1 85  ? -17.093 6.257   18.483  1.00 17.90 ? 85  TYR B CZ  1 
ATOM   2815 O  OH  . TYR B  1 85  ? -16.245 6.724   19.466  1.00 23.55 ? 85  TYR B OH  1 
ATOM   2816 N  N   . SER B  1 86  ? -21.924 6.413   13.371  1.00 13.86 ? 86  SER B N   1 
ATOM   2817 C  CA  . SER B  1 86  ? -22.639 6.299   12.085  1.00 13.10 ? 86  SER B CA  1 
ATOM   2818 C  C   . SER B  1 86  ? -21.631 6.342   10.907  1.00 9.67  ? 86  SER B C   1 
ATOM   2819 O  O   . SER B  1 86  ? -20.596 7.061   10.996  1.00 12.90 ? 86  SER B O   1 
ATOM   2820 C  CB  . SER B  1 86  ? -23.676 7.437   11.807  1.00 18.27 ? 86  SER B CB  1 
ATOM   2821 O  OG  . SER B  1 86  ? -24.725 7.437   12.843  1.00 22.38 ? 86  SER B OG  1 
ATOM   2822 N  N   . ALA B  1 87  ? -22.046 5.619   9.912   1.00 11.35 ? 87  ALA B N   1 
ATOM   2823 C  CA  . ALA B  1 87  ? -21.160 5.424   8.674   1.00 11.27 ? 87  ALA B CA  1 
ATOM   2824 C  C   . ALA B  1 87  ? -20.996 6.777   8.018   1.00 12.58 ? 87  ALA B C   1 
ATOM   2825 O  O   . ALA B  1 87  ? -21.943 7.649   7.995   1.00 13.67 ? 87  ALA B O   1 
ATOM   2826 C  CB  . ALA B  1 87  ? -21.745 4.440   7.734   1.00 17.19 ? 87  ALA B CB  1 
ATOM   2827 N  N   . THR B  1 88  ? -19.815 6.985   7.381   1.00 11.55 ? 88  THR B N   1 
ATOM   2828 C  CA  . THR B  1 88  ? -19.684 8.110   6.448   1.00 11.70 ? 88  THR B CA  1 
ATOM   2829 C  C   . THR B  1 88  ? -19.149 7.737   5.075   1.00 10.11 ? 88  THR B C   1 
ATOM   2830 O  O   . THR B  1 88  ? -19.620 8.240   4.067   1.00 10.50 ? 88  THR B O   1 
ATOM   2831 C  CB  . THR B  1 88  ? -18.899 9.213   7.076   1.00 11.83 ? 88  THR B CB  1 
ATOM   2832 O  OG1 . THR B  1 88  ? -18.899 10.350  6.102   1.00 16.80 ? 88  THR B OG1 1 
ATOM   2833 C  CG2 . THR B  1 88  ? -17.426 8.772   7.530   1.00 12.19 ? 88  THR B CG2 1 
ATOM   2834 N  N   . GLN B  1 89  ? -18.155 6.794   5.032   1.00 9.11  ? 89  GLN B N   1 
ATOM   2835 C  CA  . GLN B  1 89  ? -17.663 6.361   3.721   1.00 8.44  ? 89  GLN B CA  1 
ATOM   2836 C  C   . GLN B  1 89  ? -16.882 5.082   3.928   1.00 6.83  ? 89  GLN B C   1 
ATOM   2837 O  O   . GLN B  1 89  ? -16.479 4.734   5.056   1.00 8.19  ? 89  GLN B O   1 
ATOM   2838 C  CB  . GLN B  1 89  ? -16.742 7.454   3.099   1.00 8.61  ? 89  GLN B CB  1 
ATOM   2839 C  CG  . GLN B  1 89  ? -15.627 7.848   4.059   1.00 12.03 ? 89  GLN B CG  1 
ATOM   2840 C  CD  . GLN B  1 89  ? -14.301 7.381   3.601   1.00 10.19 ? 89  GLN B CD  1 
ATOM   2841 O  OE1 . GLN B  1 89  ? -14.168 6.245   3.170   1.00 11.66 ? 89  GLN B OE1 1 
ATOM   2842 N  NE2 . GLN B  1 89  ? -13.315 8.249   3.613   1.00 16.59 ? 89  GLN B NE2 1 
ATOM   2843 N  N   . LEU B  1 90  ? -16.737 4.344   2.833   1.00 6.39  ? 90  LEU B N   1 
ATOM   2844 C  CA  . LEU B  1 90  ? -15.745 3.259   2.819   1.00 7.40  ? 90  LEU B CA  1 
ATOM   2845 C  C   . LEU B  1 90  ? -14.785 3.472   1.672   1.00 8.30  ? 90  LEU B C   1 
ATOM   2846 O  O   . LEU B  1 90  ? -15.070 4.133   0.711   1.00 7.76  ? 90  LEU B O   1 
ATOM   2847 C  CB  . LEU B  1 90  ? -16.433 1.826   2.806   1.00 8.05  ? 90  LEU B CB  1 
ATOM   2848 C  CG  . LEU B  1 90  ? -17.375 1.546   1.660   1.00 8.33  ? 90  LEU B CG  1 
ATOM   2849 C  CD1 . LEU B  1 90  ? -16.673 1.190   0.361   1.00 9.16  ? 90  LEU B CD1 1 
ATOM   2850 C  CD2 . LEU B  1 90  ? -18.236 0.381   2.035   1.00 9.50  ? 90  LEU B CD2 1 
ATOM   2851 N  N   . HIS B  1 91  ? -13.596 2.856   1.789   1.00 6.99  ? 91  HIS B N   1 
ATOM   2852 C  CA  . HIS B  1 91  ? -12.591 2.992   0.700   1.00 6.70  ? 91  HIS B CA  1 
ATOM   2853 C  C   . HIS B  1 91  ? -11.600 1.842   0.926   1.00 6.24  ? 91  HIS B C   1 
ATOM   2854 O  O   . HIS B  1 91  ? -11.692 1.035   1.860   1.00 6.67  ? 91  HIS B O   1 
ATOM   2855 C  CB  . HIS B  1 91  ? -11.885 4.386   0.823   1.00 6.44  ? 91  HIS B CB  1 
ATOM   2856 C  CG  . HIS B  1 91  ? -11.162 4.536   2.149   1.00 5.88  ? 91  HIS B CG  1 
ATOM   2857 N  ND1 . HIS B  1 91  ? -11.717 5.113   3.277   1.00 6.68  ? 91  HIS B ND1 1 
ATOM   2858 C  CD2 . HIS B  1 91  ? -9.871  4.065   2.545   1.00 6.56  ? 91  HIS B CD2 1 
ATOM   2859 C  CE1 . HIS B  1 91  ? -10.854 5.020   4.317   1.00 6.57  ? 91  HIS B CE1 1 
ATOM   2860 N  NE2 . HIS B  1 91  ? -9.708  4.364   3.869   1.00 5.63  ? 91  HIS B NE2 1 
ATOM   2861 N  N   . LEU B  1 92  ? -10.638 1.812   -0.011  1.00 6.32  ? 92  LEU B N   1 
ATOM   2862 C  CA  . LEU B  1 92  ? -9.675  0.693   -0.021  1.00 6.37  ? 92  LEU B CA  1 
ATOM   2863 C  C   . LEU B  1 92  ? -8.220  1.143   -0.119  1.00 6.27  ? 92  LEU B C   1 
ATOM   2864 O  O   . LEU B  1 92  ? -7.916  2.292   -0.460  1.00 6.67  ? 92  LEU B O   1 
ATOM   2865 C  CB  . LEU B  1 92  ? -9.963  -0.248  -1.149  1.00 7.97  ? 92  LEU B CB  1 
ATOM   2866 C  CG  . LEU B  1 92  ? -11.392 -0.951  -1.067  1.00 7.76  ? 92  LEU B CG  1 
ATOM   2867 C  CD1 . LEU B  1 92  ? -12.346 -0.338  -1.965  1.00 12.90 ? 92  LEU B CD1 1 
ATOM   2868 C  CD2 . LEU B  1 92  ? -11.250 -2.402  -1.380  1.00 9.94  ? 92  LEU B CD2 1 
ATOM   2869 N  N   . HIS B  1 93  ? -7.360  0.179   0.218   1.00 5.98  ? 93  HIS B N   1 
ATOM   2870 C  CA  . HIS B  1 93  ? -5.884  0.372   0.030   1.00 5.99  ? 93  HIS B CA  1 
ATOM   2871 C  C   . HIS B  1 93  ? -5.376  -0.866  -0.595  1.00 6.72  ? 93  HIS B C   1 
ATOM   2872 O  O   . HIS B  1 93  ? -5.823  -1.949  -0.280  1.00 6.89  ? 93  HIS B O   1 
ATOM   2873 C  CB  . HIS B  1 93  ? -5.221  0.541   1.383   1.00 6.62  ? 93  HIS B CB  1 
ATOM   2874 C  CG  . HIS B  1 93  ? -5.714  1.721   2.158   1.00 6.84  ? 93  HIS B CG  1 
ATOM   2875 N  ND1 . HIS B  1 93  ? -5.131  2.995   2.142   1.00 7.52  ? 93  HIS B ND1 1 
ATOM   2876 C  CD2 . HIS B  1 93  ? -6.758  1.805   3.096   1.00 6.57  ? 93  HIS B CD2 1 
ATOM   2877 C  CE1 . HIS B  1 93  ? -5.812  3.871   2.955   1.00 8.15  ? 93  HIS B CE1 1 
ATOM   2878 N  NE2 . HIS B  1 93  ? -6.822  3.170   3.550   1.00 6.44  ? 93  HIS B NE2 1 
ATOM   2879 N  N   . TRP B  1 94  ? -4.440  -0.752  -1.516  1.00 5.79  ? 94  TRP B N   1 
ATOM   2880 C  CA  . TRP B  1 94  ? -3.947  -1.889  -2.337  1.00 5.81  ? 94  TRP B CA  1 
ATOM   2881 C  C   . TRP B  1 94  ? -2.533  -1.658  -2.807  1.00 6.22  ? 94  TRP B C   1 
ATOM   2882 O  O   . TRP B  1 94  ? -1.927  -0.609  -2.587  1.00 6.44  ? 94  TRP B O   1 
ATOM   2883 C  CB  . TRP B  1 94  ? -4.916  -2.150  -3.475  1.00 6.47  ? 94  TRP B CB  1 
ATOM   2884 C  CG  . TRP B  1 94  ? -5.014  -0.972  -4.412  1.00 6.37  ? 94  TRP B CG  1 
ATOM   2885 C  CD1 . TRP B  1 94  ? -4.231  -0.711  -5.531  1.00 6.98  ? 94  TRP B CD1 1 
ATOM   2886 C  CD2 . TRP B  1 94  ? -6.041  0.085   -4.356  1.00 6.27  ? 94  TRP B CD2 1 
ATOM   2887 N  NE1 . TRP B  1 94  ? -4.680  0.462   -6.149  1.00 6.90  ? 94  TRP B NE1 1 
ATOM   2888 C  CE2 . TRP B  1 94  ? -5.812  0.942   -5.478  1.00 6.56  ? 94  TRP B CE2 1 
ATOM   2889 C  CE3 . TRP B  1 94  ? -7.121  0.366   -3.511  1.00 6.80  ? 94  TRP B CE3 1 
ATOM   2890 C  CZ2 . TRP B  1 94  ? -6.609  2.040   -5.742  1.00 6.74  ? 94  TRP B CZ2 1 
ATOM   2891 C  CZ3 . TRP B  1 94  ? -7.903  1.525   -3.752  1.00 7.90  ? 94  TRP B CZ3 1 
ATOM   2892 C  CH2 . TRP B  1 94  ? -7.628  2.366   -4.839  1.00 7.06  ? 94  TRP B CH2 1 
ATOM   2893 N  N   . GLY B  1 95  ? -2.038  -2.682  -3.504  1.00 5.90  ? 95  GLY B N   1 
ATOM   2894 C  CA  . GLY B  1 95  ? -0.597  -2.659  -3.909  1.00 7.07  ? 95  GLY B CA  1 
ATOM   2895 C  C   . GLY B  1 95  ? -0.536  -2.388  -5.402  1.00 6.52  ? 95  GLY B C   1 
ATOM   2896 O  O   . GLY B  1 95  ? -1.052  -1.361  -5.895  1.00 7.70  ? 95  GLY B O   1 
ATOM   2897 N  N   . ASN B  1 96  ? 0.009   -3.303  -6.195  1.00 7.88  ? 96  ASN B N   1 
ATOM   2898 C  CA  . ASN B  1 96  ? 0.088   -3.064  -7.654  1.00 9.17  ? 96  ASN B CA  1 
ATOM   2899 C  C   . ASN B  1 96  ? 0.094   -4.381  -8.393  1.00 10.11 ? 96  ASN B C   1 
ATOM   2900 O  O   . ASN B  1 96  ? 0.246   -5.402  -7.748  1.00 8.72  ? 96  ASN B O   1 
ATOM   2901 C  CB  . ASN B  1 96  ? 1.351   -2.253  -8.028  1.00 11.27 ? 96  ASN B CB  1 
ATOM   2902 C  CG  . ASN B  1 96  ? 2.650   -3.019  -7.775  1.00 12.09 ? 96  ASN B CG  1 
ATOM   2903 O  OD1 . ASN B  1 96  ? 3.036   -3.796  -8.644  1.00 17.46 ? 96  ASN B OD1 1 
ATOM   2904 N  ND2 . ASN B  1 96  ? 3.314   -2.839  -6.713  1.00 12.36 ? 96  ASN B ND2 1 
ATOM   2905 N  N   . PRO B  1 97  ? -0.013  -4.406  -9.750  1.00 9.66  ? 97  PRO B N   1 
ATOM   2906 C  CA  . PRO B  1 97  ? -0.197  -5.680  -10.443 1.00 11.62 ? 97  PRO B CA  1 
ATOM   2907 C  C   . PRO B  1 97  ? 0.955   -6.684  -10.255 1.00 10.10 ? 97  PRO B C   1 
ATOM   2908 O  O   . PRO B  1 97  ? 0.699   -7.901  -10.315 1.00 12.26 ? 97  PRO B O   1 
ATOM   2909 C  CB  . PRO B  1 97  ? -0.253  -5.248  -11.913 1.00 12.40 ? 97  PRO B CB  1 
ATOM   2910 C  CG  . PRO B  1 97  ? -1.009  -3.930  -11.808 1.00 10.99 ? 97  PRO B CG  1 
ATOM   2911 C  CD  . PRO B  1 97  ? -0.239  -3.281  -10.668 1.00 11.75 ? 97  PRO B CD  1 
ATOM   2912 N  N   . ASN B  1 98  ? 2.160   -6.169  -10.054 1.00 8.92  ? 98  ASN B N   1 
ATOM   2913 C  CA  . ASN B  1 98  ? 3.334   -7.057  -9.927  1.00 11.41 ? 98  ASN B CA  1 
ATOM   2914 C  C   . ASN B  1 98  ? 3.631   -7.337  -8.472  1.00 14.94 ? 98  ASN B C   1 
ATOM   2915 O  O   . ASN B  1 98  ? 4.577   -8.086  -8.142  1.00 19.39 ? 98  ASN B O   1 
ATOM   2916 C  CB  . ASN B  1 98  ? 4.501   -6.318  -10.594 1.00 11.95 ? 98  ASN B CB  1 
ATOM   2917 C  CG  . ASN B  1 98  ? 4.291   -6.139  -12.077 1.00 12.86 ? 98  ASN B CG  1 
ATOM   2918 O  OD1 . ASN B  1 98  ? 4.075   -7.120  -12.830 1.00 12.94 ? 98  ASN B OD1 1 
ATOM   2919 N  ND2 . ASN B  1 98  ? 4.191   -4.889  -12.501 1.00 12.73 ? 98  ASN B ND2 1 
ATOM   2920 N  N   . ASP B  1 99  ? 2.910   -6.734  -7.549  1.00 11.84 ? 99  ASP B N   1 
ATOM   2921 C  CA  . ASP B  1 99  ? 3.145   -7.053  -6.091  1.00 11.81 ? 99  ASP B CA  1 
ATOM   2922 C  C   . ASP B  1 99  ? 1.769   -6.761  -5.439  1.00 9.42  ? 99  ASP B C   1 
ATOM   2923 O  O   . ASP B  1 99  ? 1.532   -5.660  -4.891  1.00 9.27  ? 99  ASP B O   1 
ATOM   2924 C  CB  . ASP B  1 99  ? 4.204   -6.118  -5.474  1.00 15.12 ? 99  ASP B CB  1 
ATOM   2925 C  CG  . ASP B  1 99  ? 4.447   -6.366  -3.942  1.00 18.48 ? 99  ASP B CG  1 
ATOM   2926 O  OD1 . ASP B  1 99  ? 3.991   -7.363  -3.468  1.00 20.71 ? 99  ASP B OD1 1 
ATOM   2927 O  OD2 . ASP B  1 99  ? 4.950   -5.430  -3.263  1.00 25.31 ? 99  ASP B OD2 1 
ATOM   2928 N  N   . PRO B  1 100 ? 0.843   -7.728  -5.491  1.00 7.98  ? 100 PRO B N   1 
ATOM   2929 C  CA  . PRO B  1 100 ? -0.533  -7.524  -4.922  1.00 9.45  ? 100 PRO B CA  1 
ATOM   2930 C  C   . PRO B  1 100 ? -0.517  -7.743  -3.410  1.00 9.59  ? 100 PRO B C   1 
ATOM   2931 O  O   . PRO B  1 100 ? -1.112  -8.672  -2.907  1.00 11.37 ? 100 PRO B O   1 
ATOM   2932 C  CB  . PRO B  1 100 ? -1.404  -8.515  -5.719  1.00 10.67 ? 100 PRO B CB  1 
ATOM   2933 C  CG  . PRO B  1 100 ? -0.348  -9.578  -6.054  1.00 10.57 ? 100 PRO B CG  1 
ATOM   2934 C  CD  . PRO B  1 100 ? 0.933   -8.947  -6.339  1.00 9.75  ? 100 PRO B CD  1 
ATOM   2935 N  N   . HIS B  1 101 ? 0.172   -6.879  -2.687  1.00 9.58  ? 101 HIS B N   1 
ATOM   2936 C  CA  . HIS B  1 101 ? 0.357   -7.049  -1.241  1.00 10.69 ? 101 HIS B CA  1 
ATOM   2937 C  C   . HIS B  1 101 ? 0.328   -5.740  -0.567  1.00 10.57 ? 101 HIS B C   1 
ATOM   2938 O  O   . HIS B  1 101 ? 1.266   -5.305  0.163   1.00 13.78 ? 101 HIS B O   1 
ATOM   2939 C  CB  . HIS B  1 101 ? 1.633   -7.824  -0.824  1.00 12.41 ? 101 HIS B CB  1 
ATOM   2940 C  CG  . HIS B  1 101 ? 1.711   -9.144  -1.424  1.00 15.11 ? 101 HIS B CG  1 
ATOM   2941 N  ND1 . HIS B  1 101 ? 1.071   -10.231 -0.929  1.00 20.41 ? 101 HIS B ND1 1 
ATOM   2942 C  CD2 . HIS B  1 101 ? 2.275   -9.528  -2.635  1.00 14.29 ? 101 HIS B CD2 1 
ATOM   2943 C  CE1 . HIS B  1 101 ? 1.287   -11.292 -1.807  1.00 17.76 ? 101 HIS B CE1 1 
ATOM   2944 N  NE2 . HIS B  1 101 ? 2.013   -10.864 -2.805  1.00 20.41 ? 101 HIS B NE2 1 
ATOM   2945 N  N   . GLY B  1 102 ? -0.815  -5.104  -0.645  1.00 8.14  ? 102 GLY B N   1 
ATOM   2946 C  CA  . GLY B  1 102 ? -1.000  -3.689  -0.218  1.00 8.18  ? 102 GLY B CA  1 
ATOM   2947 C  C   . GLY B  1 102 ? -1.970  -3.462  0.918   1.00 7.07  ? 102 GLY B C   1 
ATOM   2948 O  O   . GLY B  1 102 ? -2.461  -2.341  1.042   1.00 8.44  ? 102 GLY B O   1 
ATOM   2949 N  N   . SER B  1 103 ? -2.192  -4.458  1.823   1.00 6.71  ? 103 SER B N   1 
ATOM   2950 C  CA  . SER B  1 103 ? -2.918  -4.083  3.012   1.00 6.54  ? 103 SER B CA  1 
ATOM   2951 C  C   . SER B  1 103 ? -2.140  -3.105  3.874   1.00 7.40  ? 103 SER B C   1 
ATOM   2952 O  O   . SER B  1 103 ? -0.880  -2.998  3.742   1.00 8.83  ? 103 SER B O   1 
ATOM   2953 C  CB  . SER B  1 103 ? -3.273  -5.343  3.870   1.00 6.70  ? 103 SER B CB  1 
ATOM   2954 O  OG  . SER B  1 103 ? -2.051  -5.904  4.432   1.00 7.21  ? 103 SER B OG  1 
ATOM   2955 N  N   . GLU B  1 104 ? -2.819  -2.354  4.741   1.00 6.40  ? 104 GLU B N   1 
ATOM   2956 C  CA  . GLU B  1 104 ? -2.148  -1.447  5.666   1.00 6.48  ? 104 GLU B CA  1 
ATOM   2957 C  C   . GLU B  1 104 ? -1.703  -2.162  6.928   1.00 6.79  ? 104 GLU B C   1 
ATOM   2958 O  O   . GLU B  1 104 ? -0.525  -2.213  7.274   1.00 7.56  ? 104 GLU B O   1 
ATOM   2959 C  CB  . GLU B  1 104 ? -3.013  -0.208  5.986   1.00 6.67  ? 104 GLU B CB  1 
ATOM   2960 C  CG  . GLU B  1 104 ? -3.492  0.457   4.709   1.00 7.34  ? 104 GLU B CG  1 
ATOM   2961 C  CD  . GLU B  1 104 ? -3.572  1.949   4.974   1.00 6.36  ? 104 GLU B CD  1 
ATOM   2962 O  OE1 . GLU B  1 104 ? -4.573  2.406   5.590   1.00 7.32  ? 104 GLU B OE1 1 
ATOM   2963 O  OE2 . GLU B  1 104 ? -2.641  2.690   4.663   1.00 7.63  ? 104 GLU B OE2 1 
ATOM   2964 N  N   . HIS B  1 105 ? -2.643  -2.772  7.652   1.00 7.36  ? 105 HIS B N   1 
ATOM   2965 C  CA  . HIS B  1 105 ? -2.248  -3.623  8.780   1.00 7.77  ? 105 HIS B CA  1 
ATOM   2966 C  C   . HIS B  1 105 ? -1.639  -4.869  8.244   1.00 7.87  ? 105 HIS B C   1 
ATOM   2967 O  O   . HIS B  1 105 ? -1.998  -5.387  7.159   1.00 7.71  ? 105 HIS B O   1 
ATOM   2968 C  CB  . HIS B  1 105 ? -3.515  -3.956  9.604   1.00 7.29  ? 105 HIS B CB  1 
ATOM   2969 C  CG  . HIS B  1 105 ? -4.053  -2.780  10.309  1.00 7.75  ? 105 HIS B CG  1 
ATOM   2970 N  ND1 . HIS B  1 105 ? -4.975  -1.958  9.729   1.00 7.73  ? 105 HIS B ND1 1 
ATOM   2971 C  CD2 . HIS B  1 105 ? -3.722  -2.236  11.542  1.00 7.29  ? 105 HIS B CD2 1 
ATOM   2972 C  CE1 . HIS B  1 105 ? -5.205  -0.949  10.572  1.00 8.01  ? 105 HIS B CE1 1 
ATOM   2973 N  NE2 . HIS B  1 105 ? -4.449  -1.121  11.694  1.00 8.03  ? 105 HIS B NE2 1 
ATOM   2974 N  N   . THR B  1 106 ? -0.641  -5.372  9.008   1.00 8.13  ? 106 THR B N   1 
ATOM   2975 C  CA  . THR B  1 106 ? -0.050  -6.682  8.747   1.00 8.64  ? 106 THR B CA  1 
ATOM   2976 C  C   . THR B  1 106 ? -0.322  -7.605  9.920   1.00 7.68  ? 106 THR B C   1 
ATOM   2977 O  O   . THR B  1 106 ? -0.672  -7.145  10.958  1.00 8.74  ? 106 THR B O   1 
ATOM   2978 C  CB  . THR B  1 106 ? 1.445   -6.507  8.403   1.00 8.94  ? 106 THR B CB  1 
ATOM   2979 O  OG1 . THR B  1 106 ? 2.125   -5.873  9.508   1.00 9.06  ? 106 THR B OG1 1 
ATOM   2980 C  CG2 . THR B  1 106 ? 1.555   -5.616  7.190   1.00 10.21 ? 106 THR B CG2 1 
ATOM   2981 N  N   . VAL B  1 107 ? -0.221  -8.928  9.629   1.00 9.95  ? 107 VAL B N   1 
ATOM   2982 C  CA  . VAL B  1 107 ? -0.419  -9.885  10.686  1.00 10.54 ? 107 VAL B CA  1 
ATOM   2983 C  C   . VAL B  1 107 ? 0.809   -10.779 10.729  1.00 9.54  ? 107 VAL B C   1 
ATOM   2984 O  O   . VAL B  1 107 ? 1.184   -11.332 9.706   1.00 11.99 ? 107 VAL B O   1 
ATOM   2985 C  CB  . VAL B  1 107 ? -1.738  -10.738 10.452  1.00 11.14 ? 107 VAL B CB  1 
ATOM   2986 C  CG1 . VAL B  1 107 ? -1.809  -11.749 11.601  1.00 12.61 ? 107 VAL B CG1 1 
ATOM   2987 C  CG2 . VAL B  1 107 ? -3.011  -9.833  10.478  1.00 12.09 ? 107 VAL B CG2 1 
ATOM   2988 N  N   . SER B  1 108 ? 1.462   -10.722 11.872  1.00 10.76 ? 108 SER B N   1 
ATOM   2989 C  CA  . SER B  1 108 ? 2.752   -11.500 12.065  1.00 11.93 ? 108 SER B CA  1 
ATOM   2990 C  C   . SER B  1 108 ? 3.709   -11.193 10.885  1.00 11.88 ? 108 SER B C   1 
ATOM   2991 O  O   . SER B  1 108 ? 4.310   -12.097 10.263  1.00 13.68 ? 108 SER B O   1 
ATOM   2992 C  CB  . SER B  1 108 ? 2.480   -13.014 12.248  1.00 13.43 ? 108 SER B CB  1 
ATOM   2993 O  OG  . SER B  1 108 ? 1.628   -13.215 13.340  1.00 16.16 ? 108 SER B OG  1 
ATOM   2994 N  N   . GLY B  1 109 ? 3.829   -9.920  10.542  1.00 12.87 ? 109 GLY B N   1 
ATOM   2995 C  CA  . GLY B  1 109 ? 4.718   -9.434  9.531   1.00 12.22 ? 109 GLY B CA  1 
ATOM   2996 C  C   . GLY B  1 109 ? 4.307   -9.547  8.037   1.00 15.63 ? 109 GLY B C   1 
ATOM   2997 O  O   . GLY B  1 109 ? 5.066   -9.095  7.162   1.00 19.28 ? 109 GLY B O   1 
ATOM   2998 N  N   . GLN B  1 110 ? 3.136   -10.109 7.783   1.00 14.18 ? 110 GLN B N   1 
ATOM   2999 C  CA  . GLN B  1 110 ? 2.735   -10.418 6.399   1.00 16.86 ? 110 GLN B CA  1 
ATOM   3000 C  C   . GLN B  1 110 ? 1.597   -9.425  6.001   1.00 11.82 ? 110 GLN B C   1 
ATOM   3001 O  O   . GLN B  1 110 ? 0.592   -9.192  6.760   1.00 10.83 ? 110 GLN B O   1 
ATOM   3002 C  CB  . GLN B  1 110 ? 2.155   -11.861 6.310   1.00 20.20 ? 110 GLN B CB  1 
ATOM   3003 C  CG  . GLN B  1 110 ? 2.965   -13.019 7.029   1.00 20.51 ? 110 GLN B CG  1 
ATOM   3004 C  CD  . GLN B  1 110 ? 4.321   -13.316 6.374   1.00 28.55 ? 110 GLN B CD  1 
ATOM   3005 O  OE1 . GLN B  1 110 ? 4.554   -13.035 5.218   1.00 30.90 ? 110 GLN B OE1 1 
ATOM   3006 N  NE2 . GLN B  1 110 ? 5.208   -13.921 7.135   1.00 42.85 ? 110 GLN B NE2 1 
ATOM   3007 N  N   . HIS B  1 111 ? 1.760   -8.862  4.819   1.00 10.95 ? 111 HIS B N   1 
ATOM   3008 C  CA  . HIS B  1 111 ? 0.684   -8.155  4.128   1.00 10.37 ? 111 HIS B CA  1 
ATOM   3009 C  C   . HIS B  1 111 ? -0.327  -9.055  3.515   1.00 11.28 ? 111 HIS B C   1 
ATOM   3010 O  O   . HIS B  1 111 ? 0.021   -10.143 2.944   1.00 14.87 ? 111 HIS B O   1 
ATOM   3011 C  CB  . HIS B  1 111 ? 1.161   -7.315  2.965   1.00 12.52 ? 111 HIS B CB  1 
ATOM   3012 C  CG  . HIS B  1 111 ? 1.867   -6.098  3.391   1.00 11.60 ? 111 HIS B CG  1 
ATOM   3013 N  ND1 . HIS B  1 111 ? 1.238   -4.820  3.522   1.00 12.00 ? 111 HIS B ND1 1 
ATOM   3014 C  CD2 . HIS B  1 111 ? 3.199   -5.935  3.775   1.00 13.47 ? 111 HIS B CD2 1 
ATOM   3015 C  CE1 . HIS B  1 111 ? 2.179   -3.929  3.960   1.00 13.13 ? 111 HIS B CE1 1 
ATOM   3016 N  NE2 . HIS B  1 111 ? 3.386   -4.577  4.076   1.00 16.71 ? 111 HIS B NE2 1 
ATOM   3017 N  N   . PHE B  1 112 ? -1.575  -8.631  3.579   1.00 9.25  ? 112 PHE B N   1 
ATOM   3018 C  CA  . PHE B  1 112 ? -2.643  -9.165  2.772   1.00 8.87  ? 112 PHE B CA  1 
ATOM   3019 C  C   . PHE B  1 112 ? -2.672  -8.401  1.447   1.00 7.08  ? 112 PHE B C   1 
ATOM   3020 O  O   . PHE B  1 112 ? -1.942  -7.410  1.301   1.00 7.65  ? 112 PHE B O   1 
ATOM   3021 C  CB  . PHE B  1 112 ? -3.958  -9.117  3.537   1.00 11.00 ? 112 PHE B CB  1 
ATOM   3022 C  CG  . PHE B  1 112 ? -4.067  -10.206 4.577   1.00 12.04 ? 112 PHE B CG  1 
ATOM   3023 C  CD1 . PHE B  1 112 ? -3.473  -10.027 5.821   1.00 14.54 ? 112 PHE B CD1 1 
ATOM   3024 C  CD2 . PHE B  1 112 ? -4.729  -11.368 4.218   1.00 14.35 ? 112 PHE B CD2 1 
ATOM   3025 C  CE1 . PHE B  1 112 ? -3.579  -11.115 6.784   1.00 16.25 ? 112 PHE B CE1 1 
ATOM   3026 C  CE2 . PHE B  1 112 ? -4.864  -12.408 5.110   1.00 19.03 ? 112 PHE B CE2 1 
ATOM   3027 C  CZ  . PHE B  1 112 ? -4.279  -12.233 6.343   1.00 15.86 ? 112 PHE B CZ  1 
ATOM   3028 N  N   . ALA B  1 113 ? -3.505  -8.822  0.491   1.00 7.28  ? 113 ALA B N   1 
ATOM   3029 C  CA  . ALA B  1 113 ? -3.508  -8.224  -0.821  1.00 7.53  ? 113 ALA B CA  1 
ATOM   3030 C  C   . ALA B  1 113 ? -4.007  -6.789  -0.747  1.00 7.26  ? 113 ALA B C   1 
ATOM   3031 O  O   . ALA B  1 113 ? -3.498  -5.952  -1.490  1.00 8.28  ? 113 ALA B O   1 
ATOM   3032 C  CB  . ALA B  1 113 ? -4.362  -9.050  -1.785  1.00 8.37  ? 113 ALA B CB  1 
ATOM   3033 N  N   . ALA B  1 114 ? -5.038  -6.539  0.048   1.00 7.25  ? 114 ALA B N   1 
ATOM   3034 C  CA  . ALA B  1 114 ? -5.616  -5.158  0.086   1.00 6.33  ? 114 ALA B CA  1 
ATOM   3035 C  C   . ALA B  1 114 ? -6.372  -5.078  1.431   1.00 6.44  ? 114 ALA B C   1 
ATOM   3036 O  O   . ALA B  1 114 ? -6.360  -5.986  2.266   1.00 6.55  ? 114 ALA B O   1 
ATOM   3037 C  CB  . ALA B  1 114 ? -6.589  -4.994  -1.110  1.00 6.89  ? 114 ALA B CB  1 
ATOM   3038 N  N   . GLU B  1 115 ? -7.004  -3.922  1.647   1.00 6.17  ? 115 GLU B N   1 
ATOM   3039 C  CA  . GLU B  1 115 ? -7.714  -3.679  2.899   1.00 6.10  ? 115 GLU B CA  1 
ATOM   3040 C  C   . GLU B  1 115 ? -8.843  -2.720  2.658   1.00 6.81  ? 115 GLU B C   1 
ATOM   3041 O  O   . GLU B  1 115 ? -8.701  -1.718  1.936   1.00 7.35  ? 115 GLU B O   1 
ATOM   3042 C  CB  . GLU B  1 115 ? -6.746  -3.160  3.935   1.00 6.41  ? 115 GLU B CB  1 
ATOM   3043 C  CG  . GLU B  1 115 ? -7.327  -3.013  5.366   1.00 6.99  ? 115 GLU B CG  1 
ATOM   3044 C  CD  . GLU B  1 115 ? -6.230  -2.740  6.426   1.00 7.53  ? 115 GLU B CD  1 
ATOM   3045 O  OE1 . GLU B  1 115 ? -5.056  -3.208  6.199   1.00 7.26  ? 115 GLU B OE1 1 
ATOM   3046 O  OE2 . GLU B  1 115 ? -6.471  -2.110  7.463   1.00 7.44  ? 115 GLU B OE2 1 
ATOM   3047 N  N   . LEU B  1 116 ? -10.026 -3.019  3.228   1.00 6.37  ? 116 LEU B N   1 
ATOM   3048 C  CA  . LEU B  1 116 ? -11.220 -2.163  3.177   1.00 6.87  ? 116 LEU B CA  1 
ATOM   3049 C  C   . LEU B  1 116 ? -11.346 -1.477  4.515   1.00 7.36  ? 116 LEU B C   1 
ATOM   3050 O  O   . LEU B  1 116 ? -11.198 -2.099  5.615   1.00 7.07  ? 116 LEU B O   1 
ATOM   3051 C  CB  . LEU B  1 116 ? -12.464 -3.100  3.037   1.00 8.01  ? 116 LEU B CB  1 
ATOM   3052 C  CG  . LEU B  1 116 ? -13.794 -2.278  3.083   1.00 8.01  ? 116 LEU B CG  1 
ATOM   3053 C  CD1 . LEU B  1 116 ? -14.106 -1.414  1.875   1.00 9.49  ? 116 LEU B CD1 1 
ATOM   3054 C  CD2 . LEU B  1 116 ? -14.912 -3.315  3.273   1.00 8.84  ? 116 LEU B CD2 1 
ATOM   3055 N  N   . HIS B  1 117 ? -11.584 -0.198  4.465   1.00 6.21  ? 117 HIS B N   1 
ATOM   3056 C  CA  . HIS B  1 117 ? -11.905 0.625   5.673   1.00 7.19  ? 117 HIS B CA  1 
ATOM   3057 C  C   . HIS B  1 117 ? -13.306 1.196   5.588   1.00 7.18  ? 117 HIS B C   1 
ATOM   3058 O  O   . HIS B  1 117 ? -13.642 1.826   4.580   1.00 7.03  ? 117 HIS B O   1 
ATOM   3059 C  CB  . HIS B  1 117 ? -10.933 1.795   5.798   1.00 6.31  ? 117 HIS B CB  1 
ATOM   3060 C  CG  . HIS B  1 117 ? -9.573  1.322   6.170   1.00 5.94  ? 117 HIS B CG  1 
ATOM   3061 N  ND1 . HIS B  1 117 ? -8.432  2.041   5.907   1.00 6.30  ? 117 HIS B ND1 1 
ATOM   3062 C  CD2 . HIS B  1 117 ? -9.160  0.110   6.690   1.00 6.75  ? 117 HIS B CD2 1 
ATOM   3063 C  CE1 . HIS B  1 117 ? -7.339  1.352   6.317   1.00 7.14  ? 117 HIS B CE1 1 
ATOM   3064 N  NE2 . HIS B  1 117 ? -7.799  0.151   6.784   1.00 6.16  ? 117 HIS B NE2 1 
ATOM   3065 N  N   . ILE B  1 118 ? -14.141 0.839   6.581   1.00 7.43  ? 118 ILE B N   1 
ATOM   3066 C  CA  . ILE B  1 118 ? -15.467 1.501   6.629   1.00 7.71  ? 118 ILE B CA  1 
ATOM   3067 C  C   . ILE B  1 118 ? -15.449 2.480   7.774   1.00 8.09  ? 118 ILE B C   1 
ATOM   3068 O  O   . ILE B  1 118 ? -15.258 2.110   8.961   1.00 7.89  ? 118 ILE B O   1 
ATOM   3069 C  CB  . ILE B  1 118 ? -16.568 0.437   6.862   1.00 7.64  ? 118 ILE B CB  1 
ATOM   3070 C  CG1 . ILE B  1 118 ? -16.469 -0.760  5.903   1.00 7.92  ? 118 ILE B CG1 1 
ATOM   3071 C  CG2 . ILE B  1 118 ? -17.993 1.142   6.775   1.00 8.80  ? 118 ILE B CG2 1 
ATOM   3072 C  CD1 . ILE B  1 118 ? -17.537 -1.877  6.169   1.00 10.71 ? 118 ILE B CD1 1 
ATOM   3073 N  N   . VAL B  1 119 ? -15.429 3.796   7.480   1.00 8.31  ? 119 VAL B N   1 
ATOM   3074 C  CA  . VAL B  1 119 ? -15.220 4.873   8.420   1.00 8.19  ? 119 VAL B CA  1 
ATOM   3075 C  C   . VAL B  1 119 ? -16.563 5.315   8.990   1.00 9.06  ? 119 VAL B C   1 
ATOM   3076 O  O   . VAL B  1 119 ? -17.482 5.579   8.212   1.00 9.92  ? 119 VAL B O   1 
ATOM   3077 C  CB  . VAL B  1 119 ? -14.562 6.090   7.686   1.00 8.59  ? 119 VAL B CB  1 
ATOM   3078 C  CG1 . VAL B  1 119 ? -14.232 7.251   8.638   1.00 10.30 ? 119 VAL B CG1 1 
ATOM   3079 C  CG2 . VAL B  1 119 ? -13.243 5.616   6.949   1.00 8.94  ? 119 VAL B CG2 1 
ATOM   3080 N  N   . HIS B  1 120 ? -16.533 5.413   10.320  1.00 9.52  ? 120 HIS B N   1 
ATOM   3081 C  CA  . HIS B  1 120 ? -17.704 5.929   11.060  1.00 10.77 ? 120 HIS B CA  1 
ATOM   3082 C  C   . HIS B  1 120 ? -17.248 7.025   11.967  1.00 10.53 ? 120 HIS B C   1 
ATOM   3083 O  O   . HIS B  1 120 ? -16.114 7.176   12.412  1.00 11.85 ? 120 HIS B O   1 
ATOM   3084 C  CB  . HIS B  1 120 ? -18.339 4.777   11.913  1.00 10.58 ? 120 HIS B CB  1 
ATOM   3085 C  CG  . HIS B  1 120 ? -18.720 3.565   11.198  1.00 10.50 ? 120 HIS B CG  1 
ATOM   3086 N  ND1 . HIS B  1 120 ? -17.764 2.696   10.627  1.00 10.76 ? 120 HIS B ND1 1 
ATOM   3087 C  CD2 . HIS B  1 120 ? -19.935 2.925   11.066  1.00 10.74 ? 120 HIS B CD2 1 
ATOM   3088 C  CE1 . HIS B  1 120 ? -18.410 1.637   10.120  1.00 11.78 ? 120 HIS B CE1 1 
ATOM   3089 N  NE2 . HIS B  1 120 ? -19.773 1.768   10.391  1.00 13.15 ? 120 HIS B NE2 1 
ATOM   3090 N  N   . TYR B  1 121 ? -18.224 7.899   12.326  1.00 13.30 ? 121 TYR B N   1 
ATOM   3091 C  CA  . TYR B  1 121 ? -17.932 8.941   13.233  1.00 15.68 ? 121 TYR B CA  1 
ATOM   3092 C  C   . TYR B  1 121 ? -18.996 8.914   14.368  1.00 16.24 ? 121 TYR B C   1 
ATOM   3093 O  O   . TYR B  1 121 ? -20.086 8.405   14.208  1.00 16.72 ? 121 TYR B O   1 
ATOM   3094 C  CB  . TYR B  1 121 ? -17.968 10.336  12.512  1.00 16.85 ? 121 TYR B CB  1 
ATOM   3095 C  CG  . TYR B  1 121 ? -19.376 10.731  12.034  1.00 16.41 ? 121 TYR B CG  1 
ATOM   3096 C  CD1 . TYR B  1 121 ? -19.867 10.233  10.896  1.00 17.70 ? 121 TYR B CD1 1 
ATOM   3097 C  CD2 . TYR B  1 121 ? -20.159 11.598  12.821  1.00 17.85 ? 121 TYR B CD2 1 
ATOM   3098 C  CE1 . TYR B  1 121 ? -21.129 10.562  10.406  1.00 17.54 ? 121 TYR B CE1 1 
ATOM   3099 C  CE2 . TYR B  1 121 ? -21.426 11.947  12.345  1.00 17.88 ? 121 TYR B CE2 1 
ATOM   3100 C  CZ  . TYR B  1 121 ? -21.900 11.414  11.140  1.00 20.97 ? 121 TYR B CZ  1 
ATOM   3101 O  OH  . TYR B  1 121 ? -23.157 11.623  10.539  1.00 25.81 ? 121 TYR B OH  1 
ATOM   3102 N  N   . ASN B  1 122 ? -18.592 9.482   15.451  1.00 17.22 ? 122 ASN B N   1 
ATOM   3103 C  CA  . ASN B  1 122 ? -19.478 9.557   16.625  1.00 20.46 ? 122 ASN B CA  1 
ATOM   3104 C  C   . ASN B  1 122 ? -20.673 10.541  16.439  1.00 18.54 ? 122 ASN B C   1 
ATOM   3105 O  O   . ASN B  1 122 ? -20.463 11.708  16.643  1.00 21.91 ? 122 ASN B O   1 
ATOM   3106 C  CB  . ASN B  1 122 ? -18.618 9.891   17.807  1.00 21.72 ? 122 ASN B CB  1 
ATOM   3107 C  CG  . ASN B  1 122 ? -19.382 9.739   19.129  1.00 28.68 ? 122 ASN B CG  1 
ATOM   3108 O  OD1 . ASN B  1 122 ? -20.615 9.869   19.169  1.00 24.23 ? 122 ASN B OD1 1 
ATOM   3109 N  ND2 . ASN B  1 122 ? -18.656 9.392   20.187  1.00 28.09 ? 122 ASN B ND2 1 
ATOM   3110 N  N   . SER B  1 123 ? -21.798 10.011  15.994  1.00 23.47 ? 123 SER B N   1 
ATOM   3111 C  CA  . SER B  1 123 ? -22.972 10.853  15.593  1.00 24.32 ? 123 SER B CA  1 
ATOM   3112 C  C   . SER B  1 123 ? -23.778 11.264  16.844  1.00 30.72 ? 123 SER B C   1 
ATOM   3113 O  O   . SER B  1 123 ? -24.676 12.132  16.738  1.00 27.33 ? 123 SER B O   1 
ATOM   3114 C  CB  . SER B  1 123 ? -23.838 10.205  14.511  1.00 28.39 ? 123 SER B CB  1 
ATOM   3115 O  OG  . SER B  1 123 ? -24.169 8.851   14.832  1.00 27.34 ? 123 SER B OG  1 
ATOM   3116 N  N   . ASP B  1 124 ? -23.482 10.641  17.991  1.00 28.15 ? 124 ASP B N   1 
ATOM   3117 C  CA  . ASP B  1 124 ? -24.038 11.071  19.280  1.00 32.03 ? 124 ASP B CA  1 
ATOM   3118 C  C   . ASP B  1 124 ? -23.470 12.432  19.643  1.00 31.75 ? 124 ASP B C   1 
ATOM   3119 O  O   . ASP B  1 124 ? -24.224 13.299  20.117  1.00 32.32 ? 124 ASP B O   1 
ATOM   3120 C  CB  . ASP B  1 124 ? -23.819 10.033  20.405  1.00 30.79 ? 124 ASP B CB  1 
ATOM   3121 C  CG  . ASP B  1 124 ? -24.718 8.814   20.282  1.00 33.47 ? 124 ASP B CG  1 
ATOM   3122 O  OD1 . ASP B  1 124 ? -25.733 8.829   19.513  1.00 35.71 ? 124 ASP B OD1 1 
ATOM   3123 O  OD2 . ASP B  1 124 ? -24.437 7.796   20.991  1.00 35.83 ? 124 ASP B OD2 1 
ATOM   3124 N  N   . LEU B  1 125 ? -22.203 12.659  19.316  1.00 30.34 ? 125 LEU B N   1 
ATOM   3125 C  CA  . LEU B  1 125 ? -21.455 13.874  19.692  1.00 24.49 ? 125 LEU B CA  1 
ATOM   3126 C  C   . LEU B  1 125 ? -21.160 14.890  18.589  1.00 31.92 ? 125 LEU B C   1 
ATOM   3127 O  O   . LEU B  1 125 ? -20.923 16.077  18.900  1.00 33.99 ? 125 LEU B O   1 
ATOM   3128 C  CB  . LEU B  1 125 ? -20.168 13.577  20.404  1.00 28.68 ? 125 LEU B CB  1 
ATOM   3129 C  CG  . LEU B  1 125 ? -20.243 12.557  21.536  1.00 30.66 ? 125 LEU B CG  1 
ATOM   3130 C  CD1 . LEU B  1 125 ? -18.868 12.395  22.125  1.00 27.37 ? 125 LEU B CD1 1 
ATOM   3131 C  CD2 . LEU B  1 125 ? -21.219 12.978  22.648  1.00 28.86 ? 125 LEU B CD2 1 
ATOM   3132 N  N   . TYR B  1 126 ? -21.132 14.441  17.321  1.00 29.46 ? 126 TYR B N   1 
ATOM   3133 C  CA  . TYR B  1 126 ? -20.640 15.315  16.238  1.00 27.44 ? 126 TYR B CA  1 
ATOM   3134 C  C   . TYR B  1 126 ? -21.566 15.256  15.094  1.00 24.25 ? 126 TYR B C   1 
ATOM   3135 O  O   . TYR B  1 126 ? -22.256 14.211  14.842  1.00 26.97 ? 126 TYR B O   1 
ATOM   3136 C  CB  . TYR B  1 126 ? -19.174 14.981  15.779  1.00 27.24 ? 126 TYR B CB  1 
ATOM   3137 C  CG  . TYR B  1 126 ? -18.249 14.921  16.942  1.00 27.89 ? 126 TYR B CG  1 
ATOM   3138 C  CD1 . TYR B  1 126 ? -17.790 16.100  17.556  1.00 32.55 ? 126 TYR B CD1 1 
ATOM   3139 C  CD2 . TYR B  1 126 ? -17.834 13.665  17.490  1.00 27.68 ? 126 TYR B CD2 1 
ATOM   3140 C  CE1 . TYR B  1 126 ? -16.998 16.056  18.709  1.00 31.54 ? 126 TYR B CE1 1 
ATOM   3141 C  CE2 . TYR B  1 126 ? -17.038 13.606  18.619  1.00 29.99 ? 126 TYR B CE2 1 
ATOM   3142 C  CZ  . TYR B  1 126 ? -16.591 14.806  19.226  1.00 32.71 ? 126 TYR B CZ  1 
ATOM   3143 O  OH  . TYR B  1 126 ? -15.773 14.754  20.348  1.00 31.11 ? 126 TYR B OH  1 
ATOM   3144 N  N   . PRO B  1 127 ? -21.638 16.405  14.365  1.00 31.05 ? 127 PRO B N   1 
ATOM   3145 C  CA  . PRO B  1 127 ? -22.572 16.606  13.298  1.00 29.36 ? 127 PRO B CA  1 
ATOM   3146 C  C   . PRO B  1 127 ? -22.187 15.928  11.964  1.00 28.32 ? 127 PRO B C   1 
ATOM   3147 O  O   . PRO B  1 127 ? -23.059 15.673  11.141  1.00 32.34 ? 127 PRO B O   1 
ATOM   3148 C  CB  . PRO B  1 127 ? -22.595 18.145  13.155  1.00 27.45 ? 127 PRO B CB  1 
ATOM   3149 C  CG  . PRO B  1 127 ? -21.259 18.587  13.666  1.00 32.64 ? 127 PRO B CG  1 
ATOM   3150 C  CD  . PRO B  1 127 ? -21.013 17.668  14.807  1.00 30.21 ? 127 PRO B CD  1 
ATOM   3151 N  N   . ASP B  1 128 ? -20.886 15.643  11.770  1.00 26.02 ? 128 ASP B N   1 
ATOM   3152 C  CA  . ASP B  1 128 ? -20.383 15.071  10.540  1.00 25.17 ? 128 ASP B CA  1 
ATOM   3153 C  C   . ASP B  1 128 ? -18.999 14.561  10.856  1.00 23.31 ? 128 ASP B C   1 
ATOM   3154 O  O   . ASP B  1 128 ? -18.419 14.891  11.891  1.00 27.45 ? 128 ASP B O   1 
ATOM   3155 C  CB  . ASP B  1 128 ? -20.283 16.185  9.467   1.00 28.70 ? 128 ASP B CB  1 
ATOM   3156 C  CG  . ASP B  1 128 ? -19.456 17.365  9.914   1.00 31.22 ? 128 ASP B CG  1 
ATOM   3157 O  OD1 . ASP B  1 128 ? -19.958 18.196  10.696  1.00 39.22 ? 128 ASP B OD1 1 
ATOM   3158 O  OD2 . ASP B  1 128 ? -18.326 17.531  9.415   1.00 34.77 ? 128 ASP B OD2 1 
ATOM   3159 N  N   . ALA B  1 129 ? -18.469 13.727  9.954   1.00 24.37 ? 129 ALA B N   1 
ATOM   3160 C  CA  . ALA B  1 129 ? -17.157 13.107  10.116  1.00 22.29 ? 129 ALA B CA  1 
ATOM   3161 C  C   . ALA B  1 129 ? -15.983 14.081  10.052  1.00 22.14 ? 129 ALA B C   1 
ATOM   3162 O  O   . ALA B  1 129 ? -14.989 13.853  10.717  1.00 21.41 ? 129 ALA B O   1 
ATOM   3163 C  CB  . ALA B  1 129 ? -16.969 11.997  9.037   1.00 22.33 ? 129 ALA B CB  1 
ATOM   3164 N  N   A SER B  1 130 ? -16.123 15.170  9.277   0.50 23.66 ? 130 SER B N   1 
ATOM   3165 N  N   B SER B  1 130 ? -16.081 15.172  9.275   0.50 24.69 ? 130 SER B N   1 
ATOM   3166 C  CA  A SER B  1 130 ? -15.006 16.123  9.111   0.50 25.16 ? 130 SER B CA  1 
ATOM   3167 C  CA  B SER B  1 130 ? -14.938 16.117  9.189   0.50 26.81 ? 130 SER B CA  1 
ATOM   3168 C  C   A SER B  1 130 ? -14.709 16.882  10.409  0.50 25.76 ? 130 SER B C   1 
ATOM   3169 C  C   B SER B  1 130 ? -14.692 16.781  10.531  0.50 27.08 ? 130 SER B C   1 
ATOM   3170 O  O   A SER B  1 130 ? -13.531 17.122  10.729  0.50 24.30 ? 130 SER B O   1 
ATOM   3171 O  O   B SER B  1 130 ? -13.551 16.877  11.007  0.50 27.32 ? 130 SER B O   1 
ATOM   3172 C  CB  A SER B  1 130 ? -15.207 17.097  7.920   0.50 24.92 ? 130 SER B CB  1 
ATOM   3173 C  CB  B SER B  1 130 ? -15.130 17.199  8.110   0.50 27.24 ? 130 SER B CB  1 
ATOM   3174 O  OG  A SER B  1 130 ? -15.514 16.413  6.702   0.50 22.22 ? 130 SER B OG  1 
ATOM   3175 O  OG  B SER B  1 130 ? -14.043 18.114  8.096   0.50 28.23 ? 130 SER B OG  1 
ATOM   3176 N  N   . THR B  1 131 ? -15.778 17.253  11.129  1.00 28.91 ? 131 THR B N   1 
ATOM   3177 C  CA  . THR B  1 131 ? -15.728 17.844  12.456  1.00 28.86 ? 131 THR B CA  1 
ATOM   3178 C  C   . THR B  1 131 ? -15.227 16.858  13.487  1.00 26.16 ? 131 THR B C   1 
ATOM   3179 O  O   . THR B  1 131 ? -14.392 17.237  14.314  1.00 27.68 ? 131 THR B O   1 
ATOM   3180 C  CB  . THR B  1 131 ? -17.140 18.383  12.862  1.00 33.34 ? 131 THR B CB  1 
ATOM   3181 O  OG1 . THR B  1 131 ? -17.560 19.324  11.876  1.00 34.50 ? 131 THR B OG1 1 
ATOM   3182 C  CG2 . THR B  1 131 ? -17.101 19.118  14.215  1.00 35.44 ? 131 THR B CG2 1 
ATOM   3183 N  N   . ALA B  1 132 ? -15.688 15.580  13.407  1.00 28.63 ? 132 ALA B N   1 
ATOM   3184 C  CA  . ALA B  1 132 ? -15.264 14.496  14.346  1.00 25.33 ? 132 ALA B CA  1 
ATOM   3185 C  C   . ALA B  1 132 ? -13.766 14.130  14.234  1.00 22.80 ? 132 ALA B C   1 
ATOM   3186 O  O   . ALA B  1 132 ? -13.210 13.656  15.234  1.00 23.36 ? 132 ALA B O   1 
ATOM   3187 C  CB  . ALA B  1 132 ? -16.102 13.234  14.200  1.00 23.91 ? 132 ALA B CB  1 
ATOM   3188 N  N   . SER B  1 133 ? -13.157 14.436  13.089  1.00 23.96 ? 133 SER B N   1 
ATOM   3189 C  CA  . SER B  1 133 ? -11.894 13.778  12.662  1.00 25.62 ? 133 SER B CA  1 
ATOM   3190 C  C   . SER B  1 133 ? -10.702 14.192  13.499  1.00 29.61 ? 133 SER B C   1 
ATOM   3191 O  O   . SER B  1 133 ? -9.744  13.438  13.701  1.00 24.29 ? 133 SER B O   1 
ATOM   3192 C  CB  . SER B  1 133 ? -11.612 13.989  11.162  1.00 26.30 ? 133 SER B CB  1 
ATOM   3193 O  OG  . SER B  1 133 ? -11.279 15.371  10.870  1.00 31.56 ? 133 SER B OG  1 
ATOM   3194 N  N   . ASN B  1 134 ? -10.725 15.453  13.930  1.00 32.52 ? 134 ASN B N   1 
ATOM   3195 C  CA  . ASN B  1 134 ? -9.614  15.964  14.692  1.00 32.16 ? 134 ASN B CA  1 
ATOM   3196 C  C   . ASN B  1 134 ? -9.935  16.052  16.158  1.00 30.23 ? 134 ASN B C   1 
ATOM   3197 O  O   . ASN B  1 134 ? -9.198  16.732  16.889  1.00 35.22 ? 134 ASN B O   1 
ATOM   3198 C  CB  . ASN B  1 134 ? -9.066  17.276  14.127  1.00 29.76 ? 134 ASN B CB  1 
ATOM   3199 C  CG  . ASN B  1 134 ? -10.076 18.407  14.196  1.00 30.32 ? 134 ASN B CG  1 
ATOM   3200 O  OD1 . ASN B  1 134 ? -11.268 18.181  14.339  1.00 33.94 ? 134 ASN B OD1 1 
ATOM   3201 N  ND2 . ASN B  1 134 ? -9.588  19.636  14.068  1.00 33.37 ? 134 ASN B ND2 1 
ATOM   3202 N  N   . LYS B  1 135 ? -10.971 15.324  16.577  1.00 30.60 ? 135 LYS B N   1 
ATOM   3203 C  CA  . LYS B  1 135 ? -11.553 15.406  17.935  1.00 36.85 ? 135 LYS B CA  1 
ATOM   3204 C  C   . LYS B  1 135 ? -11.691 14.071  18.715  1.00 37.95 ? 135 LYS B C   1 
ATOM   3205 O  O   . LYS B  1 135 ? -11.713 12.991  18.099  1.00 32.46 ? 135 LYS B O   1 
ATOM   3206 C  CB  . LYS B  1 135 ? -12.884 16.220  17.896  1.00 36.81 ? 135 LYS B CB  1 
ATOM   3207 C  CG  . LYS B  1 135 ? -12.632 17.687  17.535  1.00 40.86 ? 135 LYS B CG  1 
ATOM   3208 C  CD  . LYS B  1 135 ? -13.889 18.513  17.297  1.00 43.92 ? 135 LYS B CD  1 
ATOM   3209 C  CE  . LYS B  1 135 ? -13.477 19.869  16.704  1.00 41.98 ? 135 LYS B CE  1 
ATOM   3210 N  NZ  . LYS B  1 135 ? -13.309 19.867  15.203  1.00 38.98 ? 135 LYS B NZ  1 
ATOM   3211 N  N   . SER B  1 136 ? -11.740 14.109  20.060  1.00 38.66 ? 136 SER B N   1 
ATOM   3212 C  CA  . SER B  1 136 ? -11.575 12.861  20.863  1.00 32.38 ? 136 SER B CA  1 
ATOM   3213 C  C   . SER B  1 136 ? -12.717 11.888  20.794  1.00 38.08 ? 136 SER B C   1 
ATOM   3214 O  O   . SER B  1 136 ? -13.877 12.287  20.902  1.00 35.37 ? 136 SER B O   1 
ATOM   3215 C  CB  . SER B  1 136 ? -11.254 13.133  22.364  1.00 48.56 ? 136 SER B CB  1 
ATOM   3216 O  OG  . SER B  1 136 ? -11.599 11.997  23.219  1.00 47.70 ? 136 SER B OG  1 
ATOM   3217 N  N   . GLU B  1 137 ? -12.391 10.608  20.632  1.00 27.12 ? 137 GLU B N   1 
ATOM   3218 C  CA  . GLU B  1 137 ? -13.423 9.579   20.383  1.00 37.14 ? 137 GLU B CA  1 
ATOM   3219 C  C   . GLU B  1 137 ? -14.190 9.879   19.061  1.00 28.47 ? 137 GLU B C   1 
ATOM   3220 O  O   . GLU B  1 137 ? -15.373 9.560   18.892  1.00 31.63 ? 137 GLU B O   1 
ATOM   3221 C  CB  . GLU B  1 137 ? -14.442 9.488   21.553  1.00 38.14 ? 137 GLU B CB  1 
ATOM   3222 C  CG  . GLU B  1 137 ? -13.852 9.491   22.969  1.00 48.80 ? 137 GLU B CG  1 
ATOM   3223 C  CD  . GLU B  1 137 ? -12.963 8.288   23.257  1.00 53.18 ? 137 GLU B CD  1 
ATOM   3224 O  OE1 . GLU B  1 137 ? -13.492 7.146   23.363  1.00 57.52 ? 137 GLU B OE1 1 
ATOM   3225 O  OE2 . GLU B  1 137 ? -11.730 8.496   23.399  1.00 56.00 ? 137 GLU B OE2 1 
ATOM   3226 N  N   . GLY B  1 138 ? -13.548 10.505  18.109  1.00 22.72 ? 138 GLY B N   1 
ATOM   3227 C  CA  . GLY B  1 138 ? -14.351 10.998  16.995  1.00 19.35 ? 138 GLY B CA  1 
ATOM   3228 C  C   . GLY B  1 138 ? -14.681 9.951   15.941  1.00 17.33 ? 138 GLY B C   1 
ATOM   3229 O  O   . GLY B  1 138 ? -15.723 10.002  15.333  1.00 16.78 ? 138 GLY B O   1 
ATOM   3230 N  N   . LEU B  1 139 ? -13.731 9.030   15.656  1.00 13.13 ? 139 LEU B N   1 
ATOM   3231 C  CA  . LEU B  1 139 ? -13.940 8.117   14.564  1.00 13.09 ? 139 LEU B CA  1 
ATOM   3232 C  C   . LEU B  1 139 ? -13.823 6.650   15.015  1.00 10.88 ? 139 LEU B C   1 
ATOM   3233 O  O   . LEU B  1 139 ? -13.091 6.362   15.988  1.00 13.01 ? 139 LEU B O   1 
ATOM   3234 C  CB  . LEU B  1 139 ? -12.828 8.382   13.523  1.00 14.06 ? 139 LEU B CB  1 
ATOM   3235 C  CG  . LEU B  1 139 ? -12.902 9.767   12.912  1.00 13.38 ? 139 LEU B CG  1 
ATOM   3236 C  CD1 . LEU B  1 139 ? -11.724 9.900   11.946  1.00 14.88 ? 139 LEU B CD1 1 
ATOM   3237 C  CD2 . LEU B  1 139 ? -14.217 9.888   12.146  1.00 14.86 ? 139 LEU B CD2 1 
ATOM   3238 N  N   . ALA B  1 140 ? -14.468 5.779   14.301  1.00 12.03 ? 140 ALA B N   1 
ATOM   3239 C  CA  . ALA B  1 140 ? -14.252 4.360   14.483  1.00 10.94 ? 140 ALA B CA  1 
ATOM   3240 C  C   . ALA B  1 140 ? -14.242 3.755   13.082  1.00 11.10 ? 140 ALA B C   1 
ATOM   3241 O  O   . ALA B  1 140 ? -15.105 3.991   12.198  1.00 12.50 ? 140 ALA B O   1 
ATOM   3242 C  CB  . ALA B  1 140 ? -15.378 3.734   15.271  1.00 12.09 ? 140 ALA B CB  1 
ATOM   3243 N  N   . VAL B  1 141 ? -13.195 2.940   12.824  1.00 9.25  ? 141 VAL B N   1 
ATOM   3244 C  CA  . VAL B  1 141 ? -13.076 2.320   11.498  1.00 9.04  ? 141 VAL B CA  1 
ATOM   3245 C  C   . VAL B  1 141 ? -13.167 0.842   11.649  1.00 8.61  ? 141 VAL B C   1 
ATOM   3246 O  O   . VAL B  1 141 ? -12.563 0.280   12.647  1.00 11.01 ? 141 VAL B O   1 
ATOM   3247 C  CB  . VAL B  1 141 ? -11.721 2.706   10.852  1.00 9.05  ? 141 VAL B CB  1 
ATOM   3248 C  CG1 . VAL B  1 141 ? -11.535 2.054   9.471   1.00 10.51 ? 141 VAL B CG1 1 
ATOM   3249 C  CG2 . VAL B  1 141 ? -11.651 4.244   10.691  1.00 9.98  ? 141 VAL B CG2 1 
ATOM   3250 N  N   . LEU B  1 142 ? -13.913 0.191   10.783  1.00 8.23  ? 142 LEU B N   1 
ATOM   3251 C  CA  . LEU B  1 142 ? -13.884 -1.269  10.646  1.00 8.80  ? 142 LEU B CA  1 
ATOM   3252 C  C   . LEU B  1 142 ? -12.933 -1.577  9.498   1.00 9.63  ? 142 LEU B C   1 
ATOM   3253 O  O   . LEU B  1 142 ? -13.123 -1.067  8.382   1.00 9.97  ? 142 LEU B O   1 
ATOM   3254 C  CB  . LEU B  1 142 ? -15.211 -1.860  10.334  1.00 9.01  ? 142 LEU B CB  1 
ATOM   3255 C  CG  . LEU B  1 142 ? -16.397 -1.522  11.214  1.00 10.22 ? 142 LEU B CG  1 
ATOM   3256 C  CD1 . LEU B  1 142 ? -17.658 -2.142  10.679  1.00 12.15 ? 142 LEU B CD1 1 
ATOM   3257 C  CD2 . LEU B  1 142 ? -16.091 -1.941  12.683  1.00 10.83 ? 142 LEU B CD2 1 
ATOM   3258 N  N   . ALA B  1 143 ? -11.924 -2.455  9.725   1.00 8.53  ? 143 ALA B N   1 
ATOM   3259 C  CA  . ALA B  1 143 ? -10.993 -2.827  8.692   1.00 7.45  ? 143 ALA B CA  1 
ATOM   3260 C  C   . ALA B  1 143 ? -11.157 -4.277  8.355   1.00 7.04  ? 143 ALA B C   1 
ATOM   3261 O  O   . ALA B  1 143 ? -11.231 -5.162  9.291   1.00 8.01  ? 143 ALA B O   1 
ATOM   3262 C  CB  . ALA B  1 143 ? -9.576  -2.559  9.192   1.00 8.83  ? 143 ALA B CB  1 
ATOM   3263 N  N   . VAL B  1 144 ? -11.234 -4.575  7.049   1.00 6.72  ? 144 VAL B N   1 
ATOM   3264 C  CA  . VAL B  1 144 ? -11.290 -5.931  6.520   1.00 7.12  ? 144 VAL B CA  1 
ATOM   3265 C  C   . VAL B  1 144 ? -10.053 -6.204  5.696   1.00 8.37  ? 144 VAL B C   1 
ATOM   3266 O  O   . VAL B  1 144 ? -9.748  -5.481  4.736   1.00 8.27  ? 144 VAL B O   1 
ATOM   3267 C  CB  . VAL B  1 144 ? -12.577 -6.152  5.671   1.00 6.61  ? 144 VAL B CB  1 
ATOM   3268 C  CG1 . VAL B  1 144 ? -12.613 -7.575  5.149   1.00 8.77  ? 144 VAL B CG1 1 
ATOM   3269 C  CG2 . VAL B  1 144 ? -13.828 -5.820  6.449   1.00 7.91  ? 144 VAL B CG2 1 
ATOM   3270 N  N   . LEU B  1 145 ? -9.336  -7.241  6.117   1.00 6.97  ? 145 LEU B N   1 
ATOM   3271 C  CA  . LEU B  1 145 ? -8.205  -7.739  5.380   1.00 7.64  ? 145 LEU B CA  1 
ATOM   3272 C  C   . LEU B  1 145 ? -8.674  -8.514  4.199   1.00 7.36  ? 145 LEU B C   1 
ATOM   3273 O  O   . LEU B  1 145 ? -9.600  -9.339  4.253   1.00 8.30  ? 145 LEU B O   1 
ATOM   3274 C  CB  . LEU B  1 145 ? -7.295  -8.576  6.328   1.00 8.14  ? 145 LEU B CB  1 
ATOM   3275 C  CG  . LEU B  1 145 ? -6.811  -7.824  7.571   1.00 8.78  ? 145 LEU B CG  1 
ATOM   3276 C  CD1 . LEU B  1 145 ? -6.180  -8.808  8.594   1.00 11.63 ? 145 LEU B CD1 1 
ATOM   3277 C  CD2 . LEU B  1 145 ? -5.694  -6.882  7.173   1.00 12.00 ? 145 LEU B CD2 1 
ATOM   3278 N  N   . ILE B  1 146 ? -8.081  -8.269  3.040   1.00 7.53  ? 146 ILE B N   1 
ATOM   3279 C  CA  . ILE B  1 146 ? -8.492  -8.868  1.772   1.00 7.70  ? 146 ILE B CA  1 
ATOM   3280 C  C   . ILE B  1 146 ? -7.366  -9.762  1.211   1.00 7.79  ? 146 ILE B C   1 
ATOM   3281 O  O   . ILE B  1 146 ? -6.235  -9.255  1.043   1.00 8.39  ? 146 ILE B O   1 
ATOM   3282 C  CB  . ILE B  1 146 ? -8.896  -7.797  0.759   1.00 7.47  ? 146 ILE B CB  1 
ATOM   3283 C  CG1 . ILE B  1 146 ? -10.054 -6.971  1.289   1.00 8.91  ? 146 ILE B CG1 1 
ATOM   3284 C  CG2 . ILE B  1 146 ? -9.187  -8.481  -0.591  1.00 9.04  ? 146 ILE B CG2 1 
ATOM   3285 C  CD1 . ILE B  1 146 ? -10.384 -5.735  0.448   1.00 9.79  ? 146 ILE B CD1 1 
ATOM   3286 N  N   A GLU B  1 147 ? -7.631  -11.033 0.970   0.50 8.18  ? 147 GLU B N   1 
ATOM   3287 N  N   B GLU B  1 147 ? -7.669  -11.016 0.930   0.50 7.89  ? 147 GLU B N   1 
ATOM   3288 C  CA  A GLU B  1 147 ? -6.649  -11.896 0.327   0.50 9.46  ? 147 GLU B CA  1 
ATOM   3289 C  CA  B GLU B  1 147 ? -6.723  -11.985 0.389   0.50 8.90  ? 147 GLU B CA  1 
ATOM   3290 C  C   A GLU B  1 147 ? -7.081  -12.295 -1.074  0.50 9.42  ? 147 GLU B C   1 
ATOM   3291 C  C   B GLU B  1 147 ? -7.091  -12.356 -1.047  0.50 9.02  ? 147 GLU B C   1 
ATOM   3292 O  O   A GLU B  1 147 ? -8.257  -12.302 -1.428  0.50 10.04 ? 147 GLU B O   1 
ATOM   3293 O  O   B GLU B  1 147 ? -8.262  -12.399 -1.398  0.50 9.60  ? 147 GLU B O   1 
ATOM   3294 C  CB  A GLU B  1 147 ? -6.389  -13.153 1.202   0.50 11.77 ? 147 GLU B CB  1 
ATOM   3295 C  CB  B GLU B  1 147 ? -6.808  -13.239 1.296   0.50 10.19 ? 147 GLU B CB  1 
ATOM   3296 C  CG  A GLU B  1 147 ? -7.577  -14.093 1.334   0.50 15.10 ? 147 GLU B CG  1 
ATOM   3297 C  CG  B GLU B  1 147 ? -5.853  -14.376 0.955   0.50 11.76 ? 147 GLU B CG  1 
ATOM   3298 C  CD  A GLU B  1 147 ? -7.350  -15.314 2.320   0.50 16.26 ? 147 GLU B CD  1 
ATOM   3299 C  CD  B GLU B  1 147 ? -5.605  -15.324 2.135   0.50 14.65 ? 147 GLU B CD  1 
ATOM   3300 O  OE1 A GLU B  1 147 ? -6.225  -15.456 2.829   0.50 17.70 ? 147 GLU B OE1 1 
ATOM   3301 O  OE1 B GLU B  1 147 ? -4.744  -16.209 1.956   0.50 19.58 ? 147 GLU B OE1 1 
ATOM   3302 O  OE2 A GLU B  1 147 ? -8.274  -16.154 2.544   0.50 18.24 ? 147 GLU B OE2 1 
ATOM   3303 O  OE2 B GLU B  1 147 ? -6.174  -15.121 3.252   0.50 17.19 ? 147 GLU B OE2 1 
ATOM   3304 N  N   . MET B  1 148 ? -6.095  -12.601 -1.891  1.00 8.43  ? 148 MET B N   1 
ATOM   3305 C  CA  . MET B  1 148 ? -6.326  -13.149 -3.205  1.00 8.64  ? 148 MET B CA  1 
ATOM   3306 C  C   . MET B  1 148 ? -6.899  -14.585 -3.081  1.00 8.84  ? 148 MET B C   1 
ATOM   3307 O  O   . MET B  1 148 ? -6.338  -15.437 -2.384  1.00 9.83  ? 148 MET B O   1 
ATOM   3308 C  CB  . MET B  1 148 ? -5.010  -13.205 -4.004  1.00 8.45  ? 148 MET B CB  1 
ATOM   3309 C  CG  . MET B  1 148 ? -5.258  -13.543 -5.435  1.00 9.88  ? 148 MET B CG  1 
ATOM   3310 S  SD  . MET B  1 148 ? -3.717  -13.672 -6.398  1.00 10.87 ? 148 MET B SD  1 
ATOM   3311 C  CE  . MET B  1 148 ? -3.189  -11.934 -6.494  1.00 10.51 ? 148 MET B CE  1 
ATOM   3312 N  N   . GLY B  1 149 ? -8.065  -14.705 -3.730  1.00 8.13  ? 149 GLY B N   1 
ATOM   3313 C  CA  . GLY B  1 149 ? -8.818  -15.967 -3.560  1.00 8.89  ? 149 GLY B CA  1 
ATOM   3314 C  C   . GLY B  1 149 ? -9.909  -16.054 -4.629  1.00 7.60  ? 149 GLY B C   1 
ATOM   3315 O  O   . GLY B  1 149 ? -9.720  -15.775 -5.838  1.00 9.47  ? 149 GLY B O   1 
ATOM   3316 N  N   . SER B  1 150 ? -11.070 -16.512 -4.177  1.00 8.52  ? 150 SER B N   1 
ATOM   3317 C  CA  . SER B  1 150 ? -12.262 -16.582 -5.080  1.00 9.22  ? 150 SER B CA  1 
ATOM   3318 C  C   . SER B  1 150 ? -12.805 -15.220 -5.446  1.00 9.27  ? 150 SER B C   1 
ATOM   3319 O  O   . SER B  1 150 ? -12.722 -14.249 -4.660  1.00 10.09 ? 150 SER B O   1 
ATOM   3320 C  CB  . SER B  1 150 ? -13.376 -17.329 -4.317  1.00 9.57  ? 150 SER B CB  1 
ATOM   3321 O  OG  . SER B  1 150 ? -12.980 -18.730 -4.119  1.00 10.52 ? 150 SER B OG  1 
ATOM   3322 N  N   . PHE B  1 151 ? -13.378 -15.202 -6.633  1.00 9.05  ? 151 PHE B N   1 
ATOM   3323 C  CA  . PHE B  1 151 ? -14.183 -14.072 -7.045  1.00 9.31  ? 151 PHE B CA  1 
ATOM   3324 C  C   . PHE B  1 151 ? -15.213 -13.741 -5.999  1.00 9.58  ? 151 PHE B C   1 
ATOM   3325 O  O   . PHE B  1 151 ? -15.915 -14.603 -5.436  1.00 11.47 ? 151 PHE B O   1 
ATOM   3326 C  CB  . PHE B  1 151 ? -14.847 -14.385 -8.377  1.00 9.11  ? 151 PHE B CB  1 
ATOM   3327 C  CG  . PHE B  1 151 ? -15.689 -13.253 -8.927  1.00 10.03 ? 151 PHE B CG  1 
ATOM   3328 C  CD1 . PHE B  1 151 ? -15.061 -12.169 -9.571  1.00 11.86 ? 151 PHE B CD1 1 
ATOM   3329 C  CD2 . PHE B  1 151 ? -17.042 -13.295 -8.736  1.00 10.26 ? 151 PHE B CD2 1 
ATOM   3330 C  CE1 . PHE B  1 151 ? -15.849 -11.120 -10.027 1.00 11.17 ? 151 PHE B CE1 1 
ATOM   3331 C  CE2 . PHE B  1 151 ? -17.876 -12.218 -9.172  1.00 11.35 ? 151 PHE B CE2 1 
ATOM   3332 C  CZ  . PHE B  1 151 ? -17.230 -11.161 -9.824  1.00 10.29 ? 151 PHE B CZ  1 
ATOM   3333 N  N   . ASN B  1 152 ? -15.440 -12.426 -5.753  1.00 7.84  ? 152 ASN B N   1 
ATOM   3334 C  CA  . ASN B  1 152 ? -16.343 -11.999 -4.737  1.00 8.49  ? 152 ASN B CA  1 
ATOM   3335 C  C   . ASN B  1 152 ? -17.426 -11.104 -5.350  1.00 9.63  ? 152 ASN B C   1 
ATOM   3336 O  O   . ASN B  1 152 ? -17.171 -9.896  -5.657  1.00 8.66  ? 152 ASN B O   1 
ATOM   3337 C  CB  . ASN B  1 152 ? -15.529 -11.211 -3.644  1.00 8.22  ? 152 ASN B CB  1 
ATOM   3338 C  CG  . ASN B  1 152 ? -16.366 -10.926 -2.413  1.00 8.37  ? 152 ASN B CG  1 
ATOM   3339 O  OD1 . ASN B  1 152 ? -17.487 -10.406 -2.515  1.00 9.26  ? 152 ASN B OD1 1 
ATOM   3340 N  ND2 . ASN B  1 152 ? -15.805 -11.234 -1.207  1.00 8.96  ? 152 ASN B ND2 1 
ATOM   3341 N  N   . PRO B  1 153 ? -18.639 -11.597 -5.595  1.00 9.57  ? 153 PRO B N   1 
ATOM   3342 C  CA  . PRO B  1 153 ? -19.669 -10.787 -6.263  1.00 9.62  ? 153 PRO B CA  1 
ATOM   3343 C  C   . PRO B  1 153 ? -20.009 -9.579  -5.419  1.00 11.29 ? 153 PRO B C   1 
ATOM   3344 O  O   . PRO B  1 153 ? -20.439 -8.537  -6.034  1.00 11.70 ? 153 PRO B O   1 
ATOM   3345 C  CB  . PRO B  1 153 ? -20.872 -11.764 -6.325  1.00 12.52 ? 153 PRO B CB  1 
ATOM   3346 C  CG  . PRO B  1 153 ? -20.285 -13.159 -6.181  1.00 15.00 ? 153 PRO B CG  1 
ATOM   3347 C  CD  . PRO B  1 153 ? -19.067 -13.002 -5.340  1.00 11.63 ? 153 PRO B CD  1 
ATOM   3348 N  N   . SER B  1 154 ? -19.907 -9.603  -4.111  1.00 9.67  ? 154 SER B N   1 
ATOM   3349 C  CA  . SER B  1 154 ? -20.277 -8.410  -3.349  1.00 9.63  ? 154 SER B CA  1 
ATOM   3350 C  C   . SER B  1 154 ? -19.284 -7.253  -3.550  1.00 10.52 ? 154 SER B C   1 
ATOM   3351 O  O   . SER B  1 154 ? -19.682 -6.095  -3.752  1.00 9.28  ? 154 SER B O   1 
ATOM   3352 C  CB  . SER B  1 154 ? -20.429 -8.719  -1.834  1.00 12.55 ? 154 SER B CB  1 
ATOM   3353 O  OG  . SER B  1 154 ? -21.360 -9.778  -1.677  1.00 15.87 ? 154 SER B OG  1 
ATOM   3354 N  N   . TYR B  1 155 ? -17.970 -7.550  -3.442  1.00 9.19  ? 155 TYR B N   1 
ATOM   3355 C  CA  . TYR B  1 155 ? -16.998 -6.507  -3.788  1.00 8.80  ? 155 TYR B CA  1 
ATOM   3356 C  C   . TYR B  1 155 ? -17.147 -6.065  -5.218  1.00 8.22  ? 155 TYR B C   1 
ATOM   3357 O  O   . TYR B  1 155 ? -16.795 -4.895  -5.528  1.00 8.01  ? 155 TYR B O   1 
ATOM   3358 C  CB  . TYR B  1 155 ? -15.564 -7.010  -3.456  1.00 8.41  ? 155 TYR B CB  1 
ATOM   3359 C  CG  . TYR B  1 155 ? -15.177 -6.886  -1.982  1.00 7.80  ? 155 TYR B CG  1 
ATOM   3360 C  CD1 . TYR B  1 155 ? -15.595 -7.802  -1.022  1.00 7.45  ? 155 TYR B CD1 1 
ATOM   3361 C  CD2 . TYR B  1 155 ? -14.438 -5.768  -1.511  1.00 8.44  ? 155 TYR B CD2 1 
ATOM   3362 C  CE1 . TYR B  1 155 ? -15.302 -7.642  0.308   1.00 8.59  ? 155 TYR B CE1 1 
ATOM   3363 C  CE2 . TYR B  1 155 ? -14.097 -5.619  -0.194  1.00 8.26  ? 155 TYR B CE2 1 
ATOM   3364 C  CZ  . TYR B  1 155 ? -14.587 -6.567  0.743   1.00 8.72  ? 155 TYR B CZ  1 
ATOM   3365 O  OH  . TYR B  1 155 ? -14.241 -6.381  2.085   1.00 9.00  ? 155 TYR B OH  1 
ATOM   3366 N  N   . ASP B  1 156 ? -17.629 -6.919  -6.127  1.00 7.93  ? 156 ASP B N   1 
ATOM   3367 C  CA  . ASP B  1 156 ? -17.729 -6.503  -7.490  1.00 8.68  ? 156 ASP B CA  1 
ATOM   3368 C  C   . ASP B  1 156 ? -18.807 -5.463  -7.657  1.00 7.93  ? 156 ASP B C   1 
ATOM   3369 O  O   . ASP B  1 156 ? -18.800 -4.784  -8.706  1.00 10.24 ? 156 ASP B O   1 
ATOM   3370 C  CB  . ASP B  1 156 ? -17.930 -7.688  -8.489  1.00 10.21 ? 156 ASP B CB  1 
ATOM   3371 C  CG  . ASP B  1 156 ? -17.009 -7.590  -9.688  1.00 13.06 ? 156 ASP B CG  1 
ATOM   3372 O  OD1 . ASP B  1 156 ? -15.797 -7.364  -9.484  1.00 10.95 ? 156 ASP B OD1 1 
ATOM   3373 O  OD2 . ASP B  1 156 ? -17.491 -7.723  -10.835 1.00 16.42 ? 156 ASP B OD2 1 
ATOM   3374 N  N   . LYS B  1 157 ? -19.704 -5.348  -6.647  1.00 9.73  ? 157 LYS B N   1 
ATOM   3375 C  CA  . LYS B  1 157 ? -20.782 -4.312  -6.784  1.00 10.21 ? 157 LYS B CA  1 
ATOM   3376 C  C   . LYS B  1 157 ? -20.042 -2.962  -6.766  1.00 9.82  ? 157 LYS B C   1 
ATOM   3377 O  O   . LYS B  1 157 ? -20.576 -1.964  -7.331  1.00 11.48 ? 157 LYS B O   1 
ATOM   3378 C  CB  . LYS B  1 157 ? -21.825 -4.466  -5.674  1.00 12.04 ? 157 LYS B CB  1 
ATOM   3379 C  CG  . LYS B  1 157 ? -22.693 -5.693  -5.921  1.00 13.63 ? 157 LYS B CG  1 
ATOM   3380 C  CD  . LYS B  1 157 ? -23.608 -6.078  -4.731  1.00 19.29 ? 157 LYS B CD  1 
ATOM   3381 C  CE  . LYS B  1 157 ? -24.353 -7.372  -5.092  1.00 20.79 ? 157 LYS B CE  1 
ATOM   3382 N  NZ  . LYS B  1 157 ? -25.133 -7.898  -3.895  1.00 24.85 ? 157 LYS B NZ  1 
ATOM   3383 N  N   . ILE B  1 158 ? -18.833 -2.877  -6.180  1.00 9.41  ? 158 ILE B N   1 
ATOM   3384 C  CA  . ILE B  1 158 ? -18.043 -1.650  -6.186  1.00 9.86  ? 158 ILE B CA  1 
ATOM   3385 C  C   . ILE B  1 158 ? -17.144 -1.717  -7.420  1.00 9.56  ? 158 ILE B C   1 
ATOM   3386 O  O   . ILE B  1 158 ? -17.095 -0.736  -8.186  1.00 9.64  ? 158 ILE B O   1 
ATOM   3387 C  CB  . ILE B  1 158 ? -17.201 -1.485  -4.932  1.00 9.99  ? 158 ILE B CB  1 
ATOM   3388 C  CG1 . ILE B  1 158 ? -18.160 -1.250  -3.768  1.00 11.69 ? 158 ILE B CG1 1 
ATOM   3389 C  CG2 . ILE B  1 158 ? -16.240 -0.254  -5.101  1.00 10.56 ? 158 ILE B CG2 1 
ATOM   3390 C  CD1 . ILE B  1 158 ? -17.519 -1.387  -2.407  1.00 15.23 ? 158 ILE B CD1 1 
ATOM   3391 N  N   . PHE B  1 159 ? -16.358 -2.795  -7.644  1.00 8.57  ? 159 PHE B N   1 
ATOM   3392 C  CA  . PHE B  1 159 ? -15.359 -2.815  -8.673  1.00 9.20  ? 159 PHE B CA  1 
ATOM   3393 C  C   . PHE B  1 159 ? -15.863 -2.690  -10.080 1.00 10.71 ? 159 PHE B C   1 
ATOM   3394 O  O   . PHE B  1 159 ? -15.122 -2.257  -10.955 1.00 11.69 ? 159 PHE B O   1 
ATOM   3395 C  CB  . PHE B  1 159 ? -14.505 -4.106  -8.564  1.00 10.26 ? 159 PHE B CB  1 
ATOM   3396 C  CG  . PHE B  1 159 ? -13.777 -4.288  -7.219  1.00 10.71 ? 159 PHE B CG  1 
ATOM   3397 C  CD1 . PHE B  1 159 ? -13.429 -3.206  -6.407  1.00 10.62 ? 159 PHE B CD1 1 
ATOM   3398 C  CD2 . PHE B  1 159 ? -13.432 -5.563  -6.779  1.00 11.97 ? 159 PHE B CD2 1 
ATOM   3399 C  CE1 . PHE B  1 159 ? -12.760 -3.400  -5.199  1.00 11.37 ? 159 PHE B CE1 1 
ATOM   3400 C  CE2 . PHE B  1 159 ? -12.768 -5.758  -5.575  1.00 11.37 ? 159 PHE B CE2 1 
ATOM   3401 C  CZ  . PHE B  1 159 ? -12.433 -4.676  -4.780  1.00 12.09 ? 159 PHE B CZ  1 
ATOM   3402 N  N   . SER B  1 160 ? -17.109 -3.065  -10.301 1.00 11.44 ? 160 SER B N   1 
ATOM   3403 C  CA  . SER B  1 160 ? -17.699 -2.978  -11.659 1.00 11.70 ? 160 SER B CA  1 
ATOM   3404 C  C   . SER B  1 160 ? -17.870 -1.561  -12.094 1.00 12.43 ? 160 SER B C   1 
ATOM   3405 O  O   . SER B  1 160 ? -18.150 -1.329  -13.306 1.00 15.62 ? 160 SER B O   1 
ATOM   3406 C  CB  . SER B  1 160 ? -19.039 -3.720  -11.716 1.00 12.39 ? 160 SER B CB  1 
ATOM   3407 O  OG  . SER B  1 160 ? -19.956 -3.195  -10.768 1.00 14.54 ? 160 SER B OG  1 
ATOM   3408 N  N   . HIS B  1 161 ? -17.698 -0.600  -11.161 1.00 11.41 ? 161 HIS B N   1 
ATOM   3409 C  CA  . HIS B  1 161 ? -17.811 0.845   -11.526 1.00 12.30 ? 161 HIS B CA  1 
ATOM   3410 C  C   . HIS B  1 161 ? -16.446 1.526   -11.664 1.00 13.54 ? 161 HIS B C   1 
ATOM   3411 O  O   . HIS B  1 161 ? -16.457 2.737   -11.942 1.00 13.60 ? 161 HIS B O   1 
ATOM   3412 C  CB  . HIS B  1 161 ? -18.641 1.594   -10.509 1.00 14.59 ? 161 HIS B CB  1 
ATOM   3413 C  CG  . HIS B  1 161 ? -20.081 1.147   -10.438 1.00 13.79 ? 161 HIS B CG  1 
ATOM   3414 N  ND1 . HIS B  1 161 ? -21.057 1.691   -11.279 1.00 15.45 ? 161 HIS B ND1 1 
ATOM   3415 C  CD2 . HIS B  1 161 ? -20.677 0.096   -9.760  1.00 14.55 ? 161 HIS B CD2 1 
ATOM   3416 C  CE1 . HIS B  1 161 ? -22.239 1.052   -11.036 1.00 14.53 ? 161 HIS B CE1 1 
ATOM   3417 N  NE2 . HIS B  1 161 ? -21.996 0.052   -10.121 1.00 14.56 ? 161 HIS B NE2 1 
ATOM   3418 N  N   . LEU B  1 162 ? -15.310 0.824   -11.574 1.00 13.28 ? 162 LEU B N   1 
ATOM   3419 C  CA  . LEU B  1 162 ? -14.006 1.537   -11.456 1.00 14.40 ? 162 LEU B CA  1 
ATOM   3420 C  C   . LEU B  1 162 ? -13.714 2.252   -12.748 1.00 16.37 ? 162 LEU B C   1 
ATOM   3421 O  O   . LEU B  1 162 ? -13.114 3.299   -12.663 1.00 15.86 ? 162 LEU B O   1 
ATOM   3422 C  CB  . LEU B  1 162 ? -12.897 0.561   -11.160 1.00 15.27 ? 162 LEU B CB  1 
ATOM   3423 C  CG  . LEU B  1 162 ? -12.917 -0.144  -9.794  1.00 15.58 ? 162 LEU B CG  1 
ATOM   3424 C  CD1 . LEU B  1 162 ? -11.985 -1.337  -9.863  1.00 14.55 ? 162 LEU B CD1 1 
ATOM   3425 C  CD2 . LEU B  1 162 ? -12.492 0.849   -8.724  1.00 20.99 ? 162 LEU B CD2 1 
ATOM   3426 N  N   . GLN B  1 163 ? -14.139 1.751   -13.906 1.00 15.02 ? 163 GLN B N   1 
ATOM   3427 C  CA  . GLN B  1 163 ? -13.739 2.462   -15.122 1.00 14.47 ? 163 GLN B CA  1 
ATOM   3428 C  C   . GLN B  1 163 ? -14.480 3.768   -15.326 1.00 16.69 ? 163 GLN B C   1 
ATOM   3429 O  O   . GLN B  1 163 ? -14.269 4.455   -16.371 1.00 18.89 ? 163 GLN B O   1 
ATOM   3430 C  CB  . GLN B  1 163 ? -13.860 1.573   -16.399 1.00 18.68 ? 163 GLN B CB  1 
ATOM   3431 C  CG  . GLN B  1 163 ? -12.945 0.321   -16.466 1.00 19.09 ? 163 GLN B CG  1 
ATOM   3432 C  CD  . GLN B  1 163 ? -11.414 0.600   -16.386 1.00 22.77 ? 163 GLN B CD  1 
ATOM   3433 O  OE1 . GLN B  1 163 ? -10.949 1.672   -16.632 1.00 27.41 ? 163 GLN B OE1 1 
ATOM   3434 N  NE2 . GLN B  1 163 ? -10.628 -0.451  -15.983 1.00 26.84 ? 163 GLN B NE2 1 
ATOM   3435 N  N   . HIS B  1 164 ? -15.389 4.091   -14.444 1.00 15.30 ? 164 HIS B N   1 
ATOM   3436 C  CA  . HIS B  1 164 ? -16.121 5.359   -14.433 1.00 14.19 ? 164 HIS B CA  1 
ATOM   3437 C  C   . HIS B  1 164 ? -15.653 6.413   -13.428 1.00 13.34 ? 164 HIS B C   1 
ATOM   3438 O  O   . HIS B  1 164 ? -16.156 7.530   -13.281 1.00 13.48 ? 164 HIS B O   1 
ATOM   3439 C  CB  . HIS B  1 164 ? -17.627 5.008   -14.383 1.00 17.13 ? 164 HIS B CB  1 
ATOM   3440 C  CG  . HIS B  1 164 ? -17.912 3.828   -15.344 1.00 18.12 ? 164 HIS B CG  1 
ATOM   3441 N  ND1 . HIS B  1 164 ? -17.490 3.863   -16.658 1.00 22.64 ? 164 HIS B ND1 1 
ATOM   3442 C  CD2 . HIS B  1 164 ? -18.351 2.510   -15.111 1.00 22.85 ? 164 HIS B CD2 1 
ATOM   3443 C  CE1 . HIS B  1 164 ? -17.751 2.664   -17.248 1.00 22.14 ? 164 HIS B CE1 1 
ATOM   3444 N  NE2 . HIS B  1 164 ? -18.303 1.848   -16.320 1.00 24.59 ? 164 HIS B NE2 1 
ATOM   3445 N  N   . VAL B  1 165 ? -14.647 6.007   -12.616 1.00 11.14 ? 165 VAL B N   1 
ATOM   3446 C  CA  . VAL B  1 165 ? -14.054 6.921   -11.622 1.00 11.26 ? 165 VAL B CA  1 
ATOM   3447 C  C   . VAL B  1 165 ? -12.535 6.817   -11.798 1.00 8.88  ? 165 VAL B C   1 
ATOM   3448 O  O   . VAL B  1 165 ? -11.791 6.899   -10.828 1.00 8.89  ? 165 VAL B O   1 
ATOM   3449 C  CB  . VAL B  1 165 ? -14.501 6.635   -10.140 1.00 11.36 ? 165 VAL B CB  1 
ATOM   3450 C  CG1 . VAL B  1 165 ? -15.948 7.072   -10.014 1.00 13.68 ? 165 VAL B CG1 1 
ATOM   3451 C  CG2 . VAL B  1 165 ? -14.312 5.173   -9.723  1.00 10.87 ? 165 VAL B CG2 1 
ATOM   3452 N  N   . LYS B  1 166 ? -12.065 6.675   -13.053 1.00 9.88  ? 166 LYS B N   1 
ATOM   3453 C  CA  . LYS B  1 166 ? -10.648 6.452   -13.316 1.00 10.09 ? 166 LYS B CA  1 
ATOM   3454 C  C   . LYS B  1 166 ? -9.795  7.611   -12.838 1.00 9.86  ? 166 LYS B C   1 
ATOM   3455 O  O   . LYS B  1 166 ? -8.643  7.387   -12.417 1.00 9.64  ? 166 LYS B O   1 
ATOM   3456 C  CB  . LYS B  1 166 ? -10.319 6.298   -14.801 1.00 11.75 ? 166 LYS B CB  1 
ATOM   3457 C  CG  . LYS B  1 166 ? -10.907 5.008   -15.371 1.00 13.36 ? 166 LYS B CG  1 
ATOM   3458 C  CD  . LYS B  1 166 ? -10.549 4.797   -16.864 1.00 16.85 ? 166 LYS B CD  1 
ATOM   3459 C  CE  . LYS B  1 166 ? -9.079  4.498   -17.064 1.00 17.62 ? 166 LYS B CE  1 
ATOM   3460 N  NZ  . LYS B  1 166 ? -8.774  3.179   -16.403 1.00 16.45 ? 166 LYS B NZ  1 
ATOM   3461 N  N   . TYR B  1 167 ? -10.329 8.873   -12.830 1.00 9.19  ? 167 TYR B N   1 
ATOM   3462 C  CA  . TYR B  1 167 ? -9.454  10.019  -12.561 1.00 8.60  ? 167 TYR B CA  1 
ATOM   3463 C  C   . TYR B  1 167 ? -9.944  10.821  -11.355 1.00 8.34  ? 167 TYR B C   1 
ATOM   3464 O  O   . TYR B  1 167 ? -11.164 10.775  -10.985 1.00 8.45  ? 167 TYR B O   1 
ATOM   3465 C  CB  . TYR B  1 167 ? -9.449  10.994  -13.803 1.00 9.95  ? 167 TYR B CB  1 
ATOM   3466 C  CG  . TYR B  1 167 ? -9.061  10.188  -15.073 1.00 10.46 ? 167 TYR B CG  1 
ATOM   3467 C  CD1 . TYR B  1 167 ? -7.761  9.811   -15.237 1.00 11.85 ? 167 TYR B CD1 1 
ATOM   3468 C  CD2 . TYR B  1 167 ? -9.987  9.837   -16.068 1.00 12.55 ? 167 TYR B CD2 1 
ATOM   3469 C  CE1 . TYR B  1 167 ? -7.378  9.078   -16.383 1.00 12.02 ? 167 TYR B CE1 1 
ATOM   3470 C  CE2 . TYR B  1 167 ? -9.647  9.117   -17.239 1.00 12.26 ? 167 TYR B CE2 1 
ATOM   3471 C  CZ  . TYR B  1 167 ? -8.336  8.730   -17.338 1.00 13.00 ? 167 TYR B CZ  1 
ATOM   3472 O  OH  . TYR B  1 167 ? -7.966  7.942   -18.457 1.00 15.71 ? 167 TYR B OH  1 
ATOM   3473 N  N   . LYS B  1 168 ? -9.016  11.544  -10.723 1.00 8.13  ? 168 LYS B N   1 
ATOM   3474 C  CA  . LYS B  1 168 ? -9.302  12.375  -9.552  1.00 9.43  ? 168 LYS B CA  1 
ATOM   3475 C  C   . LYS B  1 168 ? -10.480 13.271  -9.861  1.00 10.12 ? 168 LYS B C   1 
ATOM   3476 O  O   . LYS B  1 168 ? -10.573 13.951  -10.914 1.00 11.34 ? 168 LYS B O   1 
ATOM   3477 C  CB  . LYS B  1 168 ? -8.100  13.266  -9.235  1.00 10.48 ? 168 LYS B CB  1 
ATOM   3478 C  CG  . LYS B  1 168 ? -8.383  14.041  -7.947  1.00 9.86  ? 168 LYS B CG  1 
ATOM   3479 C  CD  . LYS B  1 168 ? -7.181  14.791  -7.488  1.00 13.06 ? 168 LYS B CD  1 
ATOM   3480 C  CE  . LYS B  1 168 ? -7.511  15.614  -6.200  1.00 17.48 ? 168 LYS B CE  1 
ATOM   3481 N  NZ  . LYS B  1 168 ? -6.291  16.352  -5.690  1.00 24.13 ? 168 LYS B NZ  1 
ATOM   3482 N  N   . GLY B  1 169 ? -11.416 13.268  -8.933  1.00 9.01  ? 169 GLY B N   1 
ATOM   3483 C  CA  . GLY B  1 169 ? -12.605 14.173  -8.982  1.00 10.98 ? 169 GLY B CA  1 
ATOM   3484 C  C   . GLY B  1 169 ? -13.802 13.565  -9.625  1.00 12.01 ? 169 GLY B C   1 
ATOM   3485 O  O   . GLY B  1 169 ? -14.942 14.130  -9.541  1.00 14.32 ? 169 GLY B O   1 
ATOM   3486 N  N   . GLN B  1 170 ? -13.638 12.423  -10.306 1.00 9.51  ? 170 GLN B N   1 
ATOM   3487 C  CA  . GLN B  1 170 ? -14.736 11.795  -10.996 1.00 10.71 ? 170 GLN B CA  1 
ATOM   3488 C  C   . GLN B  1 170 ? -15.644 11.092  -9.952  1.00 10.34 ? 170 GLN B C   1 
ATOM   3489 O  O   . GLN B  1 170 ? -15.187 10.630  -8.925  1.00 11.59 ? 170 GLN B O   1 
ATOM   3490 C  CB  . GLN B  1 170 ? -14.203 10.842  -12.055 1.00 9.42  ? 170 GLN B CB  1 
ATOM   3491 C  CG  . GLN B  1 170 ? -13.522 11.647  -13.216 1.00 12.11 ? 170 GLN B CG  1 
ATOM   3492 C  CD  . GLN B  1 170 ? -13.270 10.750  -14.386 1.00 12.34 ? 170 GLN B CD  1 
ATOM   3493 O  OE1 . GLN B  1 170 ? -12.867 9.575   -14.269 1.00 12.39 ? 170 GLN B OE1 1 
ATOM   3494 N  NE2 . GLN B  1 170 ? -13.396 11.328  -15.594 1.00 16.37 ? 170 GLN B NE2 1 
ATOM   3495 N  N   . GLU B  1 171 ? -16.893 11.093  -10.306 1.00 11.95 ? 171 GLU B N   1 
ATOM   3496 C  CA  . GLU B  1 171 ? -17.935 10.539  -9.438  1.00 12.15 ? 171 GLU B CA  1 
ATOM   3497 C  C   . GLU B  1 171 ? -18.826 9.599   -10.242 1.00 12.89 ? 171 GLU B C   1 
ATOM   3498 O  O   . GLU B  1 171 ? -19.035 9.775   -11.476 1.00 14.70 ? 171 GLU B O   1 
ATOM   3499 C  CB  . GLU B  1 171 ? -18.814 11.684  -8.922  1.00 15.67 ? 171 GLU B CB  1 
ATOM   3500 C  CG  . GLU B  1 171 ? -18.167 12.591  -7.888  1.00 18.81 ? 171 GLU B CG  1 
ATOM   3501 C  CD  . GLU B  1 171 ? -19.094 13.758  -7.571  1.00 23.69 ? 171 GLU B CD  1 
ATOM   3502 O  OE1 . GLU B  1 171 ? -19.936 14.083  -8.445  1.00 32.37 ? 171 GLU B OE1 1 
ATOM   3503 O  OE2 . GLU B  1 171 ? -18.884 14.303  -6.516  1.00 28.66 ? 171 GLU B OE2 1 
ATOM   3504 N  N   . ALA B  1 172 ? -19.407 8.573   -9.610  1.00 11.19 ? 172 ALA B N   1 
ATOM   3505 C  CA  . ALA B  1 172 ? -20.291 7.615   -10.289 1.00 11.80 ? 172 ALA B CA  1 
ATOM   3506 C  C   . ALA B  1 172 ? -21.282 7.231   -9.162  1.00 12.03 ? 172 ALA B C   1 
ATOM   3507 O  O   . ALA B  1 172 ? -21.067 7.581   -7.976  1.00 13.72 ? 172 ALA B O   1 
ATOM   3508 C  CB  . ALA B  1 172 ? -19.528 6.403   -10.754 1.00 12.25 ? 172 ALA B CB  1 
ATOM   3509 N  N   . PHE B  1 173 ? -22.400 6.628   -9.540  1.00 12.87 ? 173 PHE B N   1 
ATOM   3510 C  CA  . PHE B  1 173 ? -23.402 6.085   -8.607  1.00 11.14 ? 173 PHE B CA  1 
ATOM   3511 C  C   . PHE B  1 173 ? -23.426 4.580   -8.654  1.00 12.85 ? 173 PHE B C   1 
ATOM   3512 O  O   . PHE B  1 173 ? -23.315 3.947   -9.710  1.00 16.34 ? 173 PHE B O   1 
ATOM   3513 C  CB  . PHE B  1 173 ? -24.798 6.663   -8.995  1.00 13.98 ? 173 PHE B CB  1 
ATOM   3514 C  CG  . PHE B  1 173 ? -25.039 8.054   -8.479  1.00 15.74 ? 173 PHE B CG  1 
ATOM   3515 C  CD1 . PHE B  1 173 ? -25.064 8.301   -7.119  1.00 17.55 ? 173 PHE B CD1 1 
ATOM   3516 C  CD2 . PHE B  1 173 ? -25.393 9.081   -9.348  1.00 21.00 ? 173 PHE B CD2 1 
ATOM   3517 C  CE1 . PHE B  1 173 ? -25.296 9.552   -6.584  1.00 21.17 ? 173 PHE B CE1 1 
ATOM   3518 C  CE2 . PHE B  1 173 ? -25.656 10.352  -8.838  1.00 21.43 ? 173 PHE B CE2 1 
ATOM   3519 C  CZ  . PHE B  1 173 ? -25.594 10.592  -7.452  1.00 22.62 ? 173 PHE B CZ  1 
ATOM   3520 N  N   . VAL B  1 174 ? -23.437 4.046   -7.442  1.00 11.58 ? 174 VAL B N   1 
ATOM   3521 C  CA  . VAL B  1 174 ? -23.453 2.580   -7.209  1.00 11.85 ? 174 VAL B CA  1 
ATOM   3522 C  C   . VAL B  1 174 ? -24.815 2.263   -6.566  1.00 11.26 ? 174 VAL B C   1 
ATOM   3523 O  O   . VAL B  1 174 ? -25.154 2.835   -5.529  1.00 12.67 ? 174 VAL B O   1 
ATOM   3524 C  CB  . VAL B  1 174 ? -22.345 2.164   -6.225  1.00 11.21 ? 174 VAL B CB  1 
ATOM   3525 C  CG1 . VAL B  1 174 ? -22.402 0.669   -5.890  1.00 11.90 ? 174 VAL B CG1 1 
ATOM   3526 C  CG2 . VAL B  1 174 ? -20.962 2.423   -6.929  1.00 12.49 ? 174 VAL B CG2 1 
ATOM   3527 N  N   . PRO B  1 175 ? -25.595 1.348   -7.233  1.00 10.18 ? 175 PRO B N   1 
ATOM   3528 C  CA  . PRO B  1 175 ? -26.865 0.950   -6.544  1.00 10.60 ? 175 PRO B CA  1 
ATOM   3529 C  C   . PRO B  1 175 ? -26.523 0.447   -5.114  1.00 10.51 ? 175 PRO B C   1 
ATOM   3530 O  O   . PRO B  1 175 ? -25.518 -0.254  -4.884  1.00 11.83 ? 175 PRO B O   1 
ATOM   3531 C  CB  . PRO B  1 175 ? -27.417 -0.129  -7.467  1.00 10.71 ? 175 PRO B CB  1 
ATOM   3532 C  CG  . PRO B  1 175 ? -26.868 0.178   -8.840  1.00 11.11 ? 175 PRO B CG  1 
ATOM   3533 C  CD  . PRO B  1 175 ? -25.431 0.746   -8.552  1.00 10.46 ? 175 PRO B CD  1 
ATOM   3534 N  N   . GLY B  1 176 ? -27.469 0.585   -4.201  1.00 12.25 ? 176 GLY B N   1 
ATOM   3535 C  CA  . GLY B  1 176 ? -27.313 0.091   -2.827  1.00 12.07 ? 176 GLY B CA  1 
ATOM   3536 C  C   . GLY B  1 176 ? -27.240 -1.448  -2.850  1.00 11.90 ? 176 GLY B C   1 
ATOM   3537 O  O   . GLY B  1 176 ? -27.778 -2.156  -3.726  1.00 11.68 ? 176 GLY B O   1 
ATOM   3538 N  N   . PHE B  1 177 ? -26.454 -1.924  -1.850  1.00 10.96 ? 177 PHE B N   1 
ATOM   3539 C  CA  . PHE B  1 177 ? -26.373 -3.386  -1.634  1.00 10.89 ? 177 PHE B CA  1 
ATOM   3540 C  C   . PHE B  1 177 ? -26.051 -3.507  -0.190  1.00 10.86 ? 177 PHE B C   1 
ATOM   3541 O  O   . PHE B  1 177 ? -25.928 -2.547  0.580   1.00 11.18 ? 177 PHE B O   1 
ATOM   3542 C  CB  . PHE B  1 177 ? -25.304 -4.074  -2.553  1.00 11.79 ? 177 PHE B CB  1 
ATOM   3543 C  CG  . PHE B  1 177 ? -23.875 -3.643  -2.291  1.00 12.67 ? 177 PHE B CG  1 
ATOM   3544 C  CD1 . PHE B  1 177 ? -23.390 -2.436  -2.793  1.00 12.44 ? 177 PHE B CD1 1 
ATOM   3545 C  CD2 . PHE B  1 177 ? -23.053 -4.483  -1.521  1.00 14.22 ? 177 PHE B CD2 1 
ATOM   3546 C  CE1 . PHE B  1 177 ? -22.034 -2.036  -2.563  1.00 12.66 ? 177 PHE B CE1 1 
ATOM   3547 C  CE2 . PHE B  1 177 ? -21.737 -4.109  -1.296  1.00 11.70 ? 177 PHE B CE2 1 
ATOM   3548 C  CZ  . PHE B  1 177 ? -21.225 -2.932  -1.830  1.00 11.75 ? 177 PHE B CZ  1 
ATOM   3549 N  N   . ASN B  1 178 ? -26.060 -4.809  0.259   1.00 12.86 ? 178 ASN B N   1 
ATOM   3550 C  CA  . ASN B  1 178 ? -25.851 -5.044  1.638   1.00 12.39 ? 178 ASN B CA  1 
ATOM   3551 C  C   . ASN B  1 178 ? -24.329 -5.010  1.981   1.00 11.89 ? 178 ASN B C   1 
ATOM   3552 O  O   . ASN B  1 178 ? -23.594 -5.910  1.689   1.00 12.54 ? 178 ASN B O   1 
ATOM   3553 C  CB  . ASN B  1 178 ? -26.519 -6.400  2.087   1.00 13.36 ? 178 ASN B CB  1 
ATOM   3554 C  CG  . ASN B  1 178 ? -26.319 -6.686  3.520   1.00 13.47 ? 178 ASN B CG  1 
ATOM   3555 O  OD1 . ASN B  1 178 ? -25.879 -5.908  4.306   1.00 13.58 ? 178 ASN B OD1 1 
ATOM   3556 N  ND2 . ASN B  1 178 ? -26.632 -8.003  3.877   1.00 17.68 ? 178 ASN B ND2 1 
ATOM   3557 N  N   . ILE B  1 179 ? -23.985 -3.915  2.606   1.00 10.70 ? 179 ILE B N   1 
ATOM   3558 C  CA  . ILE B  1 179 ? -22.557 -3.648  2.998   1.00 11.59 ? 179 ILE B CA  1 
ATOM   3559 C  C   . ILE B  1 179 ? -22.029 -4.758  3.873   1.00 12.05 ? 179 ILE B C   1 
ATOM   3560 O  O   . ILE B  1 179 ? -20.792 -5.011  3.938   1.00 11.02 ? 179 ILE B O   1 
ATOM   3561 C  CB  . ILE B  1 179 ? -22.370 -2.254  3.587   1.00 9.82  ? 179 ILE B CB  1 
ATOM   3562 C  CG1 . ILE B  1 179 ? -22.924 -1.159  2.639   1.00 9.88  ? 179 ILE B CG1 1 
ATOM   3563 C  CG2 . ILE B  1 179 ? -20.874 -1.992  3.980   1.00 10.82 ? 179 ILE B CG2 1 
ATOM   3564 C  CD1 . ILE B  1 179 ? -22.254 -1.157  1.262   1.00 11.33 ? 179 ILE B CD1 1 
ATOM   3565 N  N   . GLU B  1 180 ? -22.904 -5.349  4.689   1.00 11.07 ? 180 GLU B N   1 
ATOM   3566 C  CA  . GLU B  1 180 ? -22.400 -6.437  5.529   1.00 11.86 ? 180 GLU B CA  1 
ATOM   3567 C  C   . GLU B  1 180 ? -21.816 -7.538  4.706   1.00 10.75 ? 180 GLU B C   1 
ATOM   3568 O  O   . GLU B  1 180 ? -21.002 -8.324  5.299   1.00 11.70 ? 180 GLU B O   1 
ATOM   3569 C  CB  . GLU B  1 180 ? -23.527 -6.913  6.472   1.00 15.34 ? 180 GLU B CB  1 
ATOM   3570 C  CG  . GLU B  1 180 ? -22.956 -7.559  7.746   1.00 17.79 ? 180 GLU B CG  1 
ATOM   3571 C  CD  . GLU B  1 180 ? -24.054 -7.886  8.787   1.00 19.20 ? 180 GLU B CD  1 
ATOM   3572 O  OE1 . GLU B  1 180 ? -25.230 -7.489  8.538   1.00 20.42 ? 180 GLU B OE1 1 
ATOM   3573 O  OE2 . GLU B  1 180 ? -23.681 -8.528  9.769   1.00 23.82 ? 180 GLU B OE2 1 
ATOM   3574 N  N   . GLU B  1 181 ? -22.192 -7.731  3.435   1.00 10.69 ? 181 GLU B N   1 
ATOM   3575 C  CA  . GLU B  1 181 ? -21.599 -8.763  2.594   1.00 10.52 ? 181 GLU B CA  1 
ATOM   3576 C  C   . GLU B  1 181 ? -20.080 -8.521  2.364   1.00 11.35 ? 181 GLU B C   1 
ATOM   3577 O  O   . GLU B  1 181 ? -19.414 -9.400  1.834   1.00 13.57 ? 181 GLU B O   1 
ATOM   3578 C  CB  . GLU B  1 181 ? -22.288 -8.757  1.213   1.00 12.99 ? 181 GLU B CB  1 
ATOM   3579 C  CG  . GLU B  1 181 ? -23.766 -9.156  1.234   1.00 15.91 ? 181 GLU B CG  1 
ATOM   3580 C  CD  . GLU B  1 181 ? -24.429 -8.977  -0.110  1.00 19.87 ? 181 GLU B CD  1 
ATOM   3581 O  OE1 . GLU B  1 181 ? -23.786 -8.572  -1.149  1.00 21.72 ? 181 GLU B OE1 1 
ATOM   3582 O  OE2 . GLU B  1 181 ? -25.707 -9.106  -0.196  1.00 21.06 ? 181 GLU B OE2 1 
ATOM   3583 N  N   . LEU B  1 182 ? -19.609 -7.324  2.681   1.00 9.77  ? 182 LEU B N   1 
ATOM   3584 C  CA  . LEU B  1 182 ? -18.182 -7.069  2.483   1.00 9.62  ? 182 LEU B CA  1 
ATOM   3585 C  C   . LEU B  1 182 ? -17.407 -7.558  3.705   1.00 8.68  ? 182 LEU B C   1 
ATOM   3586 O  O   . LEU B  1 182 ? -16.165 -7.495  3.705   1.00 9.64  ? 182 LEU B O   1 
ATOM   3587 C  CB  . LEU B  1 182 ? -17.945 -5.549  2.337   1.00 9.38  ? 182 LEU B CB  1 
ATOM   3588 C  CG  . LEU B  1 182 ? -18.623 -4.916  1.092   1.00 8.06  ? 182 LEU B CG  1 
ATOM   3589 C  CD1 . LEU B  1 182 ? -18.308 -3.399  1.077   1.00 9.30  ? 182 LEU B CD1 1 
ATOM   3590 C  CD2 . LEU B  1 182 ? -18.250 -5.594  -0.187  1.00 9.31  ? 182 LEU B CD2 1 
ATOM   3591 N  N   . LEU B  1 183 ? -18.068 -7.830  4.858   1.00 9.64  ? 183 LEU B N   1 
ATOM   3592 C  CA  . LEU B  1 183 ? -17.404 -8.247  6.088   1.00 9.16  ? 183 LEU B CA  1 
ATOM   3593 C  C   . LEU B  1 183 ? -17.138 -9.777  6.042   1.00 9.73  ? 183 LEU B C   1 
ATOM   3594 O  O   . LEU B  1 183 ? -17.799 -10.531 5.383   1.00 11.62 ? 183 LEU B O   1 
ATOM   3595 C  CB  . LEU B  1 183 ? -18.296 -7.964  7.311   1.00 10.98 ? 183 LEU B CB  1 
ATOM   3596 C  CG  . LEU B  1 183 ? -18.661 -6.475  7.396   1.00 11.49 ? 183 LEU B CG  1 
ATOM   3597 C  CD1 . LEU B  1 183 ? -19.450 -6.187  8.733   1.00 15.17 ? 183 LEU B CD1 1 
ATOM   3598 C  CD2 . LEU B  1 183 ? -17.529 -5.501  7.352   1.00 12.92 ? 183 LEU B CD2 1 
ATOM   3599 N  N   . PRO B  1 184 ? -16.096 -10.219 6.791   1.00 9.43  ? 184 PRO B N   1 
ATOM   3600 C  CA  . PRO B  1 184 ? -15.718 -11.638 6.761   1.00 11.41 ? 184 PRO B CA  1 
ATOM   3601 C  C   . PRO B  1 184 ? -16.580 -12.430 7.671   1.00 13.14 ? 184 PRO B C   1 
ATOM   3602 O  O   . PRO B  1 184 ? -17.513 -11.967 8.306   1.00 14.05 ? 184 PRO B O   1 
ATOM   3603 C  CB  . PRO B  1 184 ? -14.273 -11.607 7.356   1.00 12.04 ? 184 PRO B CB  1 
ATOM   3604 C  CG  . PRO B  1 184 ? -14.358 -10.401 8.384   1.00 11.88 ? 184 PRO B CG  1 
ATOM   3605 C  CD  . PRO B  1 184 ? -15.226 -9.397  7.653   1.00 10.28 ? 184 PRO B CD  1 
ATOM   3606 N  N   . GLU B  1 185 ? -16.276 -13.709 7.627   1.00 13.37 ? 185 GLU B N   1 
ATOM   3607 C  CA  . GLU B  1 185 ? -16.797 -14.666 8.633   1.00 15.04 ? 185 GLU B CA  1 
ATOM   3608 C  C   . GLU B  1 185 ? -16.417 -14.339 10.061  1.00 14.53 ? 185 GLU B C   1 
ATOM   3609 O  O   . GLU B  1 185 ? -15.307 -13.818 10.349  1.00 14.65 ? 185 GLU B O   1 
ATOM   3610 C  CB  . GLU B  1 185 ? -16.307 -16.034 8.260   1.00 18.01 ? 185 GLU B CB  1 
ATOM   3611 C  CG  . GLU B  1 185 ? -16.950 -16.526 7.006   1.00 23.97 ? 185 GLU B CG  1 
ATOM   3612 C  CD  . GLU B  1 185 ? -16.651 -17.997 6.728   1.00 34.66 ? 185 GLU B CD  1 
ATOM   3613 O  OE1 . GLU B  1 185 ? -15.618 -18.531 7.243   1.00 42.05 ? 185 GLU B OE1 1 
ATOM   3614 O  OE2 . GLU B  1 185 ? -17.470 -18.608 5.986   1.00 47.18 ? 185 GLU B OE2 1 
ATOM   3615 N  N   . ARG B  1 186 ? -17.363 -14.577 10.977  1.00 15.50 ? 186 ARG B N   1 
ATOM   3616 C  CA  . ARG B  1 186 ? -17.100 -14.499 12.407  1.00 15.88 ? 186 ARG B CA  1 
ATOM   3617 C  C   . ARG B  1 186 ? -16.634 -13.102 12.819  1.00 12.09 ? 186 ARG B C   1 
ATOM   3618 O  O   . ARG B  1 186 ? -15.530 -12.898 13.406  1.00 13.09 ? 186 ARG B O   1 
ATOM   3619 C  CB  . ARG B  1 186 ? -16.120 -15.578 12.929  1.00 18.24 ? 186 ARG B CB  1 
ATOM   3620 C  CG  . ARG B  1 186 ? -16.662 -17.004 12.791  1.00 22.92 ? 186 ARG B CG  1 
ATOM   3621 C  CD  . ARG B  1 186 ? -15.645 -18.041 13.322  1.00 25.05 ? 186 ARG B CD  1 
ATOM   3622 N  NE  . ARG B  1 186 ? -14.480 -18.247 12.429  1.00 28.43 ? 186 ARG B NE  1 
ATOM   3623 C  CZ  . ARG B  1 186 ? -14.541 -18.801 11.218  1.00 32.62 ? 186 ARG B CZ  1 
ATOM   3624 N  NH1 . ARG B  1 186 ? -15.720 -19.190 10.722  1.00 38.59 ? 186 ARG B NH1 1 
ATOM   3625 N  NH2 . ARG B  1 186 ? -13.433 -18.934 10.483  1.00 38.32 ? 186 ARG B NH2 1 
ATOM   3626 N  N   . THR B  1 187 ? -17.480 -12.122 12.484  1.00 11.37 ? 187 THR B N   1 
ATOM   3627 C  CA  . THR B  1 187 ? -17.146 -10.795 12.877  1.00 10.73 ? 187 THR B CA  1 
ATOM   3628 C  C   . THR B  1 187 ? -17.011 -10.567 14.379  1.00 10.54 ? 187 THR B C   1 
ATOM   3629 O  O   . THR B  1 187 ? -16.482 -9.557  14.821  1.00 11.77 ? 187 THR B O   1 
ATOM   3630 C  CB  . THR B  1 187 ? -18.173 -9.770  12.303  1.00 10.24 ? 187 THR B CB  1 
ATOM   3631 O  OG1 . THR B  1 187 ? -19.515 -10.241 12.621  1.00 12.82 ? 187 THR B OG1 1 
ATOM   3632 C  CG2 . THR B  1 187 ? -18.011 -9.682  10.718  1.00 13.67 ? 187 THR B CG2 1 
ATOM   3633 N  N   . ALA B  1 188 ? -17.486 -11.530 15.182  1.00 11.14 ? 188 ALA B N   1 
ATOM   3634 C  CA  . ALA B  1 188 ? -17.277 -11.411 16.576  1.00 10.68 ? 188 ALA B CA  1 
ATOM   3635 C  C   . ALA B  1 188 ? -15.787 -11.493 17.009  1.00 9.45  ? 188 ALA B C   1 
ATOM   3636 O  O   . ALA B  1 188 ? -15.467 -11.079 18.100  1.00 11.08 ? 188 ALA B O   1 
ATOM   3637 C  CB  . ALA B  1 188 ? -18.047 -12.530 17.346  1.00 12.66 ? 188 ALA B CB  1 
ATOM   3638 N  N   . GLU B  1 189 ? -14.941 -12.035 16.115  1.00 10.66 ? 189 GLU B N   1 
ATOM   3639 C  CA  . GLU B  1 189 ? -13.480 -12.148 16.362  1.00 9.74  ? 189 GLU B CA  1 
ATOM   3640 C  C   . GLU B  1 189 ? -12.733 -10.909 15.739  1.00 9.11  ? 189 GLU B C   1 
ATOM   3641 O  O   . GLU B  1 189 ? -12.754 -10.791 14.436  1.00 9.56  ? 189 GLU B O   1 
ATOM   3642 C  CB  . GLU B  1 189 ? -12.975 -13.455 15.819  1.00 11.90 ? 189 GLU B CB  1 
ATOM   3643 C  CG  . GLU B  1 189 ? -13.794 -14.606 16.450  1.00 14.71 ? 189 GLU B CG  1 
ATOM   3644 C  CD  . GLU B  1 189 ? -13.348 -15.923 15.983  1.00 20.53 ? 189 GLU B CD  1 
ATOM   3645 O  OE1 . GLU B  1 189 ? -12.175 -16.063 15.641  1.00 23.61 ? 189 GLU B OE1 1 
ATOM   3646 O  OE2 . GLU B  1 189 ? -14.180 -16.905 16.010  1.00 26.70 ? 189 GLU B OE2 1 
ATOM   3647 N  N   . TYR B  1 190 ? -12.218 -10.064 16.594  1.00 7.85  ? 190 TYR B N   1 
ATOM   3648 C  CA  . TYR B  1 190 ? -11.535 -8.843  16.057  1.00 8.19  ? 190 TYR B CA  1 
ATOM   3649 C  C   . TYR B  1 190 ? -10.461 -8.392  16.977  1.00 9.17  ? 190 TYR B C   1 
ATOM   3650 O  O   . TYR B  1 190 ? -10.376 -8.801  18.160  1.00 9.87  ? 190 TYR B O   1 
ATOM   3651 C  CB  . TYR B  1 190 ? -12.575 -7.735  15.717  1.00 8.04  ? 190 TYR B CB  1 
ATOM   3652 C  CG  . TYR B  1 190 ? -13.410 -7.356  16.980  1.00 7.59  ? 190 TYR B CG  1 
ATOM   3653 C  CD1 . TYR B  1 190 ? -12.899 -6.478  17.957  1.00 8.02  ? 190 TYR B CD1 1 
ATOM   3654 C  CD2 . TYR B  1 190 ? -14.712 -7.851  17.177  1.00 7.82  ? 190 TYR B CD2 1 
ATOM   3655 C  CE1 . TYR B  1 190 ? -13.714 -6.043  19.086  1.00 8.39  ? 190 TYR B CE1 1 
ATOM   3656 C  CE2 . TYR B  1 190 ? -15.470 -7.505  18.343  1.00 8.90  ? 190 TYR B CE2 1 
ATOM   3657 C  CZ  . TYR B  1 190 ? -14.947 -6.598  19.222  1.00 8.62  ? 190 TYR B CZ  1 
ATOM   3658 O  OH  . TYR B  1 190 ? -15.669 -6.169  20.328  1.00 11.06 ? 190 TYR B OH  1 
ATOM   3659 N  N   . TYR B  1 191 ? -9.542  -7.552  16.421  1.00 9.13  ? 191 TYR B N   1 
ATOM   3660 C  CA  . TYR B  1 191 ? -8.534  -6.838  17.128  1.00 8.07  ? 191 TYR B CA  1 
ATOM   3661 C  C   . TYR B  1 191 ? -9.045  -5.415  17.318  1.00 9.34  ? 191 TYR B C   1 
ATOM   3662 O  O   . TYR B  1 191 ? -9.681  -4.836  16.446  1.00 8.81  ? 191 TYR B O   1 
ATOM   3663 C  CB  . TYR B  1 191 ? -7.271  -6.739  16.232  1.00 8.90  ? 191 TYR B CB  1 
ATOM   3664 C  CG  . TYR B  1 191 ? -6.674  -8.008  15.683  1.00 8.96  ? 191 TYR B CG  1 
ATOM   3665 C  CD1 . TYR B  1 191 ? -5.694  -8.674  16.441  1.00 9.19  ? 191 TYR B CD1 1 
ATOM   3666 C  CD2 . TYR B  1 191 ? -7.032  -8.503  14.438  1.00 8.41  ? 191 TYR B CD2 1 
ATOM   3667 C  CE1 . TYR B  1 191 ? -5.118  -9.833  15.899  1.00 9.48  ? 191 TYR B CE1 1 
ATOM   3668 C  CE2 . TYR B  1 191 ? -6.439  -9.647  13.902  1.00 10.48 ? 191 TYR B CE2 1 
ATOM   3669 C  CZ  . TYR B  1 191 ? -5.458  -10.252 14.668  1.00 10.32 ? 191 TYR B CZ  1 
ATOM   3670 O  OH  . TYR B  1 191 ? -4.894  -11.381 14.019  1.00 14.03 ? 191 TYR B OH  1 
ATOM   3671 N  N   . ARG B  1 192 ? -8.766  -4.857  18.448  1.00 8.56  ? 192 ARG B N   1 
ATOM   3672 C  CA  . ARG B  1 192 ? -9.198  -3.512  18.803  1.00 8.32  ? 192 ARG B CA  1 
ATOM   3673 C  C   . ARG B  1 192 ? -8.071  -2.686  19.393  1.00 9.25  ? 192 ARG B C   1 
ATOM   3674 O  O   . ARG B  1 192 ? -7.356  -3.156  20.313  1.00 10.09 ? 192 ARG B O   1 
ATOM   3675 C  CB  . ARG B  1 192 ? -10.313 -3.633  19.888  1.00 10.41 ? 192 ARG B CB  1 
ATOM   3676 C  CG  . ARG B  1 192 ? -10.618 -2.324  20.646  1.00 11.45 ? 192 ARG B CG  1 
ATOM   3677 C  CD  . ARG B  1 192 ? -11.346 -1.229  19.794  1.00 11.33 ? 192 ARG B CD  1 
ATOM   3678 N  NE  . ARG B  1 192 ? -12.454 -1.772  18.994  1.00 11.93 ? 192 ARG B NE  1 
ATOM   3679 C  CZ  . ARG B  1 192 ? -13.647 -2.118  19.478  1.00 11.91 ? 192 ARG B CZ  1 
ATOM   3680 N  NH1 . ARG B  1 192 ? -13.905 -1.982  20.770  1.00 13.97 ? 192 ARG B NH1 1 
ATOM   3681 N  NH2 . ARG B  1 192 ? -14.584 -2.602  18.669  1.00 12.68 ? 192 ARG B NH2 1 
ATOM   3682 N  N   . TYR B  1 193 ? -7.850  -1.467  18.924  1.00 8.63  ? 193 TYR B N   1 
ATOM   3683 C  CA  . TYR B  1 193 ? -6.786  -0.647  19.459  1.00 10.72 ? 193 TYR B CA  1 
ATOM   3684 C  C   . TYR B  1 193 ? -7.042  0.815   19.172  1.00 10.15 ? 193 TYR B C   1 
ATOM   3685 O  O   . TYR B  1 193 ? -7.882  1.113   18.315  1.00 10.83 ? 193 TYR B O   1 
ATOM   3686 C  CB  . TYR B  1 193 ? -5.357  -1.116  18.985  1.00 10.57 ? 193 TYR B CB  1 
ATOM   3687 C  CG  . TYR B  1 193 ? -5.001  -0.668  17.576  1.00 8.32  ? 193 TYR B CG  1 
ATOM   3688 C  CD1 . TYR B  1 193 ? -5.423  -1.394  16.469  1.00 9.10  ? 193 TYR B CD1 1 
ATOM   3689 C  CD2 . TYR B  1 193 ? -4.242  0.477   17.360  1.00 9.79  ? 193 TYR B CD2 1 
ATOM   3690 C  CE1 . TYR B  1 193 ? -5.100  -0.989  15.181  1.00 8.03  ? 193 TYR B CE1 1 
ATOM   3691 C  CE2 . TYR B  1 193 ? -3.912  0.886   16.077  1.00 8.64  ? 193 TYR B CE2 1 
ATOM   3692 C  CZ  . TYR B  1 193 ? -4.343  0.150   14.992  1.00 7.99  ? 193 TYR B CZ  1 
ATOM   3693 O  OH  . TYR B  1 193 ? -4.009  0.570   13.723  1.00 8.76  ? 193 TYR B OH  1 
ATOM   3694 N  N   . ARG B  1 194 ? -6.314  1.686   19.863  1.00 12.06 ? 194 ARG B N   1 
ATOM   3695 C  CA  . ARG B  1 194 ? -6.455  3.146   19.673  1.00 13.23 ? 194 ARG B CA  1 
ATOM   3696 C  C   . ARG B  1 194 ? -5.393  3.546   18.719  1.00 12.05 ? 194 ARG B C   1 
ATOM   3697 O  O   . ARG B  1 194 ? -4.209  3.306   18.903  1.00 12.39 ? 194 ARG B O   1 
ATOM   3698 C  CB  . ARG B  1 194 ? -6.058  3.840   21.018  1.00 17.18 ? 194 ARG B CB  1 
ATOM   3699 C  CG  . ARG B  1 194 ? -7.014  3.423   22.095  1.00 22.88 ? 194 ARG B CG  1 
ATOM   3700 C  CD  . ARG B  1 194 ? -8.283  4.175   21.865  1.00 29.67 ? 194 ARG B CD  1 
ATOM   3701 N  NE  . ARG B  1 194 ? -9.044  4.315   23.116  1.00 43.56 ? 194 ARG B NE  1 
ATOM   3702 C  CZ  . ARG B  1 194 ? -10.131 5.073   23.243  1.00 46.76 ? 194 ARG B CZ  1 
ATOM   3703 N  NH1 . ARG B  1 194 ? -10.565 5.815   22.213  1.00 42.24 ? 194 ARG B NH1 1 
ATOM   3704 N  NH2 . ARG B  1 194 ? -10.789 5.081   24.398  1.00 50.18 ? 194 ARG B NH2 1 
ATOM   3705 N  N   . GLY B  1 195 ? -5.792  4.223   17.647  1.00 11.30 ? 195 GLY B N   1 
ATOM   3706 C  CA  . GLY B  1 195 ? -4.749  4.702   16.694  1.00 11.58 ? 195 GLY B CA  1 
ATOM   3707 C  C   . GLY B  1 195 ? -5.181  5.950   15.994  1.00 11.29 ? 195 GLY B C   1 
ATOM   3708 O  O   . GLY B  1 195 ? -5.871  6.799   16.528  1.00 11.40 ? 195 GLY B O   1 
ATOM   3709 N  N   . SER B  1 196 ? -4.898  5.936   14.703  1.00 10.04 ? 196 SER B N   1 
ATOM   3710 C  CA  . SER B  1 196 ? -4.971  7.217   13.959  1.00 9.69  ? 196 SER B CA  1 
ATOM   3711 C  C   . SER B  1 196 ? -5.522  6.973   12.536  1.00 8.61  ? 196 SER B C   1 
ATOM   3712 O  O   . SER B  1 196 ? -5.685  5.851   12.019  1.00 9.73  ? 196 SER B O   1 
ATOM   3713 C  CB  . SER B  1 196 ? -3.579  7.872   13.766  1.00 10.12 ? 196 SER B CB  1 
ATOM   3714 O  OG  . SER B  1 196 ? -2.791  7.217   12.752  1.00 8.96  ? 196 SER B OG  1 
ATOM   3715 N  N   . LEU B  1 197 ? -5.909  8.065   11.893  1.00 9.49  ? 197 LEU B N   1 
ATOM   3716 C  CA  . LEU B  1 197 ? -6.077  7.960   10.417  1.00 8.74  ? 197 LEU B CA  1 
ATOM   3717 C  C   . LEU B  1 197 ? -4.728  7.527   9.809   1.00 7.09  ? 197 LEU B C   1 
ATOM   3718 O  O   . LEU B  1 197 ? -3.671  7.948   10.272  1.00 8.48  ? 197 LEU B O   1 
ATOM   3719 C  CB  . LEU B  1 197 ? -6.324  9.396   9.811   1.00 9.40  ? 197 LEU B CB  1 
ATOM   3720 C  CG  . LEU B  1 197 ? -7.736  9.940   9.786   1.00 11.61 ? 197 LEU B CG  1 
ATOM   3721 C  CD1 . LEU B  1 197 ? -8.320  10.188  11.112  1.00 16.11 ? 197 LEU B CD1 1 
ATOM   3722 C  CD2 . LEU B  1 197 ? -7.703  11.289  8.979   1.00 11.41 ? 197 LEU B CD2 1 
ATOM   3723 N  N   . THR B  1 198 ? -4.826  6.646   8.767   1.00 7.79  ? 198 THR B N   1 
ATOM   3724 C  CA  . THR B  1 198 ? -3.570  6.183   8.122   1.00 7.21  ? 198 THR B CA  1 
ATOM   3725 C  C   . THR B  1 198 ? -3.150  7.086   6.985   1.00 7.27  ? 198 THR B C   1 
ATOM   3726 O  O   . THR B  1 198 ? -2.154  6.842   6.328   1.00 7.79  ? 198 THR B O   1 
ATOM   3727 C  CB  . THR B  1 198 ? -3.707  4.746   7.596   1.00 7.06  ? 198 THR B CB  1 
ATOM   3728 O  OG1 . THR B  1 198 ? -4.713  4.795   6.571   1.00 8.08  ? 198 THR B OG1 1 
ATOM   3729 C  CG2 . THR B  1 198 ? -4.156  3.797   8.667   1.00 8.13  ? 198 THR B CG2 1 
ATOM   3730 N  N   . THR B  1 199 ? -3.938  8.188   6.783   1.00 8.64  ? 199 THR B N   1 
ATOM   3731 C  CA  . THR B  1 199 ? -3.627  9.163   5.728   1.00 8.15  ? 199 THR B CA  1 
ATOM   3732 C  C   . THR B  1 199 ? -3.508  10.509  6.444   1.00 8.29  ? 199 THR B C   1 
ATOM   3733 O  O   . THR B  1 199 ? -4.182  10.729  7.461   1.00 10.01 ? 199 THR B O   1 
ATOM   3734 C  CB  . THR B  1 199 ? -4.772  9.241   4.669   1.00 8.33  ? 199 THR B CB  1 
ATOM   3735 O  OG1 . THR B  1 199 ? -6.017  9.387   5.369   1.00 14.26 ? 199 THR B OG1 1 
ATOM   3736 C  CG2 . THR B  1 199 ? -4.888  7.885   4.017   1.00 8.82  ? 199 THR B CG2 1 
ATOM   3737 N  N   . PRO B  1 200 ? -2.785  11.436  5.843   1.00 8.41  ? 200 PRO B N   1 
ATOM   3738 C  CA  . PRO B  1 200 ? -2.832  12.809  6.353   1.00 9.26  ? 200 PRO B CA  1 
ATOM   3739 C  C   . PRO B  1 200 ? -4.288  13.299  6.500   1.00 10.63 ? 200 PRO B C   1 
ATOM   3740 O  O   . PRO B  1 200 ? -5.076  13.018  5.615   1.00 10.41 ? 200 PRO B O   1 
ATOM   3741 C  CB  . PRO B  1 200 ? -2.141  13.594  5.224   1.00 8.77  ? 200 PRO B CB  1 
ATOM   3742 C  CG  . PRO B  1 200 ? -1.060  12.640  4.755   1.00 8.58  ? 200 PRO B CG  1 
ATOM   3743 C  CD  . PRO B  1 200 ? -1.882  11.313  4.685   1.00 8.74  ? 200 PRO B CD  1 
ATOM   3744 N  N   . PRO B  1 201 ? -4.595  14.034  7.559   1.00 10.58 ? 201 PRO B N   1 
ATOM   3745 C  CA  . PRO B  1 201 ? -3.673  14.609  8.559   1.00 11.42 ? 201 PRO B CA  1 
ATOM   3746 C  C   . PRO B  1 201 ? -3.296  13.672  9.703   1.00 11.02 ? 201 PRO B C   1 
ATOM   3747 O  O   . PRO B  1 201 ? -2.692  14.079  10.652  1.00 10.11 ? 201 PRO B O   1 
ATOM   3748 C  CB  . PRO B  1 201 ? -4.501  15.785  9.138   1.00 11.96 ? 201 PRO B CB  1 
ATOM   3749 C  CG  . PRO B  1 201 ? -5.582  15.970  8.149   1.00 15.17 ? 201 PRO B CG  1 
ATOM   3750 C  CD  . PRO B  1 201 ? -5.956  14.568  7.708   1.00 12.40 ? 201 PRO B CD  1 
ATOM   3751 N  N   . CYS B  1 202 ? -3.654  12.379  9.607   1.00 9.62  ? 202 CYS B N   1 
ATOM   3752 C  CA  . CYS B  1 202 ? -3.158  11.331  10.588  1.00 10.42 ? 202 CYS B CA  1 
ATOM   3753 C  C   . CYS B  1 202 ? -3.595  11.595  12.070  1.00 10.10 ? 202 CYS B C   1 
ATOM   3754 O  O   . CYS B  1 202 ? -2.906  11.184  12.995  1.00 10.59 ? 202 CYS B O   1 
ATOM   3755 C  CB  . CYS B  1 202 ? -1.615  11.290  10.558  1.00 9.84  ? 202 CYS B CB  1 
ATOM   3756 S  SG  . CYS B  1 202 ? -0.794  10.939  8.997   1.00 9.65  ? 202 CYS B SG  1 
ATOM   3757 N  N   . ASN B  1 203 ? -4.727  12.232  12.253  1.00 12.77 ? 203 ASN B N   1 
ATOM   3758 C  CA  . ASN B  1 203 ? -5.178  12.505  13.586  1.00 16.19 ? 203 ASN B CA  1 
ATOM   3759 C  C   . ASN B  1 203 ? -5.295  11.236  14.403  1.00 15.01 ? 203 ASN B C   1 
ATOM   3760 O  O   . ASN B  1 203 ? -5.882  10.256  13.944  1.00 12.22 ? 203 ASN B O   1 
ATOM   3761 C  CB  . ASN B  1 203 ? -6.498  13.235  13.535  1.00 19.60 ? 203 ASN B CB  1 
ATOM   3762 C  CG  . ASN B  1 203 ? -6.437  14.410  12.551  1.00 22.19 ? 203 ASN B CG  1 
ATOM   3763 O  OD1 . ASN B  1 203 ? -6.505  14.199  11.348  1.00 23.75 ? 203 ASN B OD1 1 
ATOM   3764 N  ND2 . ASN B  1 203 ? -6.145  15.582  13.051  1.00 29.18 ? 203 ASN B ND2 1 
ATOM   3765 N  N   . PRO B  1 204 ? -4.875  11.299  15.649  1.00 13.86 ? 204 PRO B N   1 
ATOM   3766 C  CA  . PRO B  1 204 ? -4.893  10.097  16.518  1.00 14.88 ? 204 PRO B CA  1 
ATOM   3767 C  C   . PRO B  1 204 ? -6.250  9.899   17.206  1.00 15.51 ? 204 PRO B C   1 
ATOM   3768 O  O   . PRO B  1 204 ? -6.304  9.865   18.515  1.00 15.80 ? 204 PRO B O   1 
ATOM   3769 C  CB  . PRO B  1 204 ? -3.790  10.378  17.533  1.00 13.68 ? 204 PRO B CB  1 
ATOM   3770 C  CG  . PRO B  1 204 ? -3.702  11.939  17.577  1.00 15.51 ? 204 PRO B CG  1 
ATOM   3771 C  CD  . PRO B  1 204 ? -4.088  12.423  16.195  1.00 16.45 ? 204 PRO B CD  1 
ATOM   3772 N  N   . THR B  1 205 ? -7.302  9.825   16.405  1.00 11.76 ? 205 THR B N   1 
ATOM   3773 C  CA  . THR B  1 205 ? -8.632  9.912   16.903  1.00 13.77 ? 205 THR B CA  1 
ATOM   3774 C  C   . THR B  1 205 ? -9.521  8.749   16.501  1.00 11.72 ? 205 THR B C   1 
ATOM   3775 O  O   . THR B  1 205 ? -10.707 8.825   16.560  1.00 14.41 ? 205 THR B O   1 
ATOM   3776 C  CB  . THR B  1 205 ? -9.282  11.169  16.339  1.00 14.03 ? 205 THR B CB  1 
ATOM   3777 O  OG1 . THR B  1 205 ? -9.113  11.136  14.922  1.00 14.68 ? 205 THR B OG1 1 
ATOM   3778 C  CG2 . THR B  1 205 ? -8.549  12.403  16.900  1.00 17.44 ? 205 THR B CG2 1 
ATOM   3779 N  N   . VAL B  1 206 ? -8.849  7.642   16.099  1.00 10.02 ? 206 VAL B N   1 
ATOM   3780 C  CA  . VAL B  1 206 ? -9.553  6.460   15.624  1.00 11.50 ? 206 VAL B CA  1 
ATOM   3781 C  C   . VAL B  1 206 ? -9.550  5.215   16.579  1.00 9.56  ? 206 VAL B C   1 
ATOM   3782 O  O   . VAL B  1 206 ? -8.473  4.804   17.021  1.00 11.46 ? 206 VAL B O   1 
ATOM   3783 C  CB  . VAL B  1 206 ? -8.961  6.023   14.227  1.00 9.24  ? 206 VAL B CB  1 
ATOM   3784 C  CG1 . VAL B  1 206 ? -9.719  4.820   13.737  1.00 11.31 ? 206 VAL B CG1 1 
ATOM   3785 C  CG2 . VAL B  1 206 ? -9.020  7.130   13.169  1.00 11.35 ? 206 VAL B CG2 1 
ATOM   3786 N  N   . LEU B  1 207 ? -10.733 4.745   16.829  1.00 10.10 ? 207 LEU B N   1 
ATOM   3787 C  CA  . LEU B  1 207 ? -10.937 3.442   17.502  1.00 10.63 ? 207 LEU B CA  1 
ATOM   3788 C  C   . LEU B  1 207 ? -10.951 2.424   16.346  1.00 8.96  ? 207 LEU B C   1 
ATOM   3789 O  O   . LEU B  1 207 ? -11.899 2.365   15.568  1.00 10.43 ? 207 LEU B O   1 
ATOM   3790 C  CB  . LEU B  1 207 ? -12.297 3.434   18.230  1.00 13.49 ? 207 LEU B CB  1 
ATOM   3791 C  CG  . LEU B  1 207 ? -12.362 2.255   19.195  1.00 18.15 ? 207 LEU B CG  1 
ATOM   3792 C  CD1 . LEU B  1 207 ? -11.439 2.421   20.407  1.00 24.72 ? 207 LEU B CD1 1 
ATOM   3793 C  CD2 . LEU B  1 207 ? -13.814 2.126   19.609  1.00 22.54 ? 207 LEU B CD2 1 
ATOM   3794 N  N   . TRP B  1 208 ? -9.871  1.619   16.259  1.00 8.61  ? 208 TRP B N   1 
ATOM   3795 C  CA  . TRP B  1 208 ? -9.718  0.608   15.207  1.00 8.70  ? 208 TRP B CA  1 
ATOM   3796 C  C   . TRP B  1 208 ? -10.358 -0.693  15.631  1.00 8.94  ? 208 TRP B C   1 
ATOM   3797 O  O   . TRP B  1 208 ? -10.082 -1.181  16.761  1.00 9.77  ? 208 TRP B O   1 
ATOM   3798 C  CB  . TRP B  1 208 ? -8.220  0.358   14.875  1.00 8.15  ? 208 TRP B CB  1 
ATOM   3799 C  CG  . TRP B  1 208 ? -7.731  1.450   13.946  1.00 8.53  ? 208 TRP B CG  1 
ATOM   3800 C  CD1 . TRP B  1 208 ? -7.046  2.586   14.320  1.00 8.96  ? 208 TRP B CD1 1 
ATOM   3801 C  CD2 . TRP B  1 208 ? -7.876  1.494   12.502  1.00 8.23  ? 208 TRP B CD2 1 
ATOM   3802 N  NE1 . TRP B  1 208 ? -6.799  3.385   13.211  1.00 8.97  ? 208 TRP B NE1 1 
ATOM   3803 C  CE2 . TRP B  1 208 ? -7.296  2.766   12.070  1.00 8.10  ? 208 TRP B CE2 1 
ATOM   3804 C  CE3 . TRP B  1 208 ? -8.440  0.672   11.561  1.00 8.49  ? 208 TRP B CE3 1 
ATOM   3805 C  CZ2 . TRP B  1 208 ? -7.321  3.160   10.730  1.00 7.37  ? 208 TRP B CZ2 1 
ATOM   3806 C  CZ3 . TRP B  1 208 ? -8.477  1.071   10.248  1.00 8.36  ? 208 TRP B CZ3 1 
ATOM   3807 C  CH2 . TRP B  1 208 ? -7.884  2.252   9.824   1.00 7.98  ? 208 TRP B CH2 1 
ATOM   3808 N  N   . THR B  1 209 ? -11.082 -1.334  14.726  1.00 8.63  ? 209 THR B N   1 
ATOM   3809 C  CA  . THR B  1 209 ? -11.534 -2.726  14.813  1.00 8.38  ? 209 THR B CA  1 
ATOM   3810 C  C   . THR B  1 209 ? -11.055 -3.402  13.558  1.00 8.58  ? 209 THR B C   1 
ATOM   3811 O  O   . THR B  1 209 ? -11.554 -3.061  12.475  1.00 8.49  ? 209 THR B O   1 
ATOM   3812 C  CB  . THR B  1 209 ? -13.074 -2.791  14.929  1.00 9.02  ? 209 THR B CB  1 
ATOM   3813 O  OG1 . THR B  1 209 ? -13.449 -2.080  16.088  1.00 9.72  ? 209 THR B OG1 1 
ATOM   3814 C  CG2 . THR B  1 209 ? -13.556 -4.241  15.049  1.00 8.32  ? 209 THR B CG2 1 
ATOM   3815 N  N   . VAL B  1 210 ? -10.107 -4.337  13.622  1.00 8.37  ? 210 VAL B N   1 
ATOM   3816 C  CA  . VAL B  1 210 ? -9.652  -5.106  12.453  1.00 7.64  ? 210 VAL B CA  1 
ATOM   3817 C  C   . VAL B  1 210 ? -10.231 -6.500  12.639  1.00 7.64  ? 210 VAL B C   1 
ATOM   3818 O  O   . VAL B  1 210 ? -9.923  -7.154  13.640  1.00 8.37  ? 210 VAL B O   1 
ATOM   3819 C  CB  . VAL B  1 210 ? -8.100  -5.135  12.432  1.00 8.27  ? 210 VAL B CB  1 
ATOM   3820 C  CG1 . VAL B  1 210 ? -7.623  -5.893  11.219  1.00 8.37  ? 210 VAL B CG1 1 
ATOM   3821 C  CG2 . VAL B  1 210 ? -7.501  -3.726  12.456  1.00 9.42  ? 210 VAL B CG2 1 
ATOM   3822 N  N   . PHE B  1 211 ? -11.045 -6.948  11.737  1.00 7.11  ? 211 PHE B N   1 
ATOM   3823 C  CA  . PHE B  1 211 ? -11.566 -8.324  11.864  1.00 7.79  ? 211 PHE B CA  1 
ATOM   3824 C  C   . PHE B  1 211 ? -10.482 -9.363  11.756  1.00 7.85  ? 211 PHE B C   1 
ATOM   3825 O  O   . PHE B  1 211 ? -9.474  -9.203  10.969  1.00 8.85  ? 211 PHE B O   1 
ATOM   3826 C  CB  . PHE B  1 211 ? -12.698 -8.549  10.864  1.00 8.48  ? 211 PHE B CB  1 
ATOM   3827 C  CG  . PHE B  1 211 ? -13.870 -7.641  11.151  1.00 8.72  ? 211 PHE B CG  1 
ATOM   3828 C  CD1 . PHE B  1 211 ? -14.634 -7.850  12.295  1.00 10.05 ? 211 PHE B CD1 1 
ATOM   3829 C  CD2 . PHE B  1 211 ? -14.231 -6.619  10.320  1.00 9.97  ? 211 PHE B CD2 1 
ATOM   3830 C  CE1 . PHE B  1 211 ? -15.727 -7.047  12.628  1.00 10.86 ? 211 PHE B CE1 1 
ATOM   3831 C  CE2 . PHE B  1 211 ? -15.322 -5.771  10.658  1.00 11.41 ? 211 PHE B CE2 1 
ATOM   3832 C  CZ  . PHE B  1 211 ? -16.096 -5.979  11.801  1.00 11.78 ? 211 PHE B CZ  1 
ATOM   3833 N  N   . ARG B  1 212 ? -10.604 -10.423 12.539  1.00 8.13  ? 212 ARG B N   1 
ATOM   3834 C  CA  . ARG B  1 212 ? -9.567  -11.427 12.513  1.00 8.43  ? 212 ARG B CA  1 
ATOM   3835 C  C   . ARG B  1 212 ? -9.491  -12.143 11.170  1.00 9.34  ? 212 ARG B C   1 
ATOM   3836 O  O   . ARG B  1 212 ? -8.371  -12.456 10.748  1.00 11.13 ? 212 ARG B O   1 
ATOM   3837 C  CB  . ARG B  1 212 ? -9.892  -12.444 13.623  1.00 8.57  ? 212 ARG B CB  1 
ATOM   3838 C  CG  . ARG B  1 212 ? -8.816  -13.534 13.726  1.00 9.83  ? 212 ARG B CG  1 
ATOM   3839 C  CD  . ARG B  1 212 ? -9.327  -14.684 14.663  1.00 12.26 ? 212 ARG B CD  1 
ATOM   3840 N  NE  . ARG B  1 212 ? -8.183  -15.521 15.011  1.00 14.50 ? 212 ARG B NE  1 
ATOM   3841 C  CZ  . ARG B  1 212 ? -8.212  -16.520 15.888  1.00 15.88 ? 212 ARG B CZ  1 
ATOM   3842 N  NH1 . ARG B  1 212 ? -9.332  -16.816 16.517  1.00 15.11 ? 212 ARG B NH1 1 
ATOM   3843 N  NH2 . ARG B  1 212 ? -7.106  -17.220 16.116  1.00 17.69 ? 212 ARG B NH2 1 
ATOM   3844 N  N   . ASN B  1 213 ? -10.639 -12.441 10.538  1.00 8.93  ? 213 ASN B N   1 
ATOM   3845 C  CA  . ASN B  1 213 ? -10.619 -13.266 9.349   1.00 10.24 ? 213 ASN B CA  1 
ATOM   3846 C  C   . ASN B  1 213 ? -10.622 -12.359 8.120   1.00 10.80 ? 213 ASN B C   1 
ATOM   3847 O  O   . ASN B  1 213 ? -11.382 -11.354 8.046   1.00 9.24  ? 213 ASN B O   1 
ATOM   3848 C  CB  . ASN B  1 213 ? -11.845 -14.193 9.351   1.00 14.06 ? 213 ASN B CB  1 
ATOM   3849 C  CG  . ASN B  1 213 ? -11.811 -15.147 10.568  1.00 17.24 ? 213 ASN B CG  1 
ATOM   3850 O  OD1 . ASN B  1 213 ? -10.765 -15.721 10.839  1.00 21.22 ? 213 ASN B OD1 1 
ATOM   3851 N  ND2 . ASN B  1 213 ? -12.878 -15.239 11.293  1.00 18.09 ? 213 ASN B ND2 1 
ATOM   3852 N  N   . PRO B  1 214 ? -9.850  -12.689 7.102   1.00 10.15 ? 214 PRO B N   1 
ATOM   3853 C  CA  . PRO B  1 214 ? -9.930  -11.989 5.816   1.00 9.89  ? 214 PRO B CA  1 
ATOM   3854 C  C   . PRO B  1 214 ? -11.102 -12.397 4.972   1.00 10.18 ? 214 PRO B C   1 
ATOM   3855 O  O   . PRO B  1 214 ? -11.714 -13.513 5.179   1.00 11.06 ? 214 PRO B O   1 
ATOM   3856 C  CB  . PRO B  1 214 ? -8.587  -12.385 5.140   1.00 10.77 ? 214 PRO B CB  1 
ATOM   3857 C  CG  . PRO B  1 214 ? -8.425  -13.837 5.572   1.00 13.13 ? 214 PRO B CG  1 
ATOM   3858 C  CD  . PRO B  1 214 ? -8.857  -13.791 7.072   1.00 11.34 ? 214 PRO B CD  1 
ATOM   3859 N  N   . VAL B  1 215 ? -11.419 -11.573 4.020   1.00 9.18  ? 215 VAL B N   1 
ATOM   3860 C  CA  . VAL B  1 215 ? -12.264 -11.977 2.880   1.00 7.98  ? 215 VAL B CA  1 
ATOM   3861 C  C   . VAL B  1 215 ? -11.423 -12.274 1.648   1.00 8.11  ? 215 VAL B C   1 
ATOM   3862 O  O   . VAL B  1 215 ? -10.211 -11.928 1.676   1.00 9.10  ? 215 VAL B O   1 
ATOM   3863 C  CB  . VAL B  1 215 ? -13.299 -10.918 2.524   1.00 8.50  ? 215 VAL B CB  1 
ATOM   3864 C  CG1 . VAL B  1 215 ? -14.252 -10.662 3.711   1.00 9.29  ? 215 VAL B CG1 1 
ATOM   3865 C  CG2 . VAL B  1 215 ? -12.635 -9.596  1.995   1.00 8.98  ? 215 VAL B CG2 1 
ATOM   3866 N  N   . GLN B  1 216 ? -11.941 -12.929 0.641   1.00 8.24  ? 216 GLN B N   1 
ATOM   3867 C  CA  . GLN B  1 216 ? -11.219 -13.160 -0.620  1.00 8.22  ? 216 GLN B CA  1 
ATOM   3868 C  C   . GLN B  1 216 ? -11.834 -12.406 -1.772  1.00 8.02  ? 216 GLN B C   1 
ATOM   3869 O  O   . GLN B  1 216 ? -13.081 -12.246 -1.857  1.00 9.77  ? 216 GLN B O   1 
ATOM   3870 C  CB  . GLN B  1 216 ? -11.330 -14.652 -1.034  1.00 10.37 ? 216 GLN B CB  1 
ATOM   3871 C  CG  . GLN B  1 216 ? -10.515 -15.535 -0.046  1.00 10.82 ? 216 GLN B CG  1 
ATOM   3872 C  CD  . GLN B  1 216 ? -10.550 -17.011 -0.468  1.00 12.72 ? 216 GLN B CD  1 
ATOM   3873 O  OE1 . GLN B  1 216 ? -11.079 -17.472 -1.503  1.00 11.38 ? 216 GLN B OE1 1 
ATOM   3874 N  NE2 . GLN B  1 216 ? -10.003 -17.780 0.418   1.00 19.37 ? 216 GLN B NE2 1 
ATOM   3875 N  N   . ILE B  1 217 ? -10.994 -11.828 -2.642  1.00 7.45  ? 217 ILE B N   1 
ATOM   3876 C  CA  . ILE B  1 217 ? -11.428 -11.373 -3.962  1.00 7.45  ? 217 ILE B CA  1 
ATOM   3877 C  C   . ILE B  1 217 ? -10.456 -11.979 -4.981  1.00 7.34  ? 217 ILE B C   1 
ATOM   3878 O  O   . ILE B  1 217 ? -9.346  -12.415 -4.583  1.00 7.20  ? 217 ILE B O   1 
ATOM   3879 C  CB  . ILE B  1 217 ? -11.433 -9.800  -4.045  1.00 7.63  ? 217 ILE B CB  1 
ATOM   3880 C  CG1 . ILE B  1 217 ? -10.029 -9.233  -4.038  1.00 8.42  ? 217 ILE B CG1 1 
ATOM   3881 C  CG2 . ILE B  1 217 ? -12.332 -9.243  -2.950  1.00 8.44  ? 217 ILE B CG2 1 
ATOM   3882 C  CD1 . ILE B  1 217 ? -10.025 -7.665  -4.188  1.00 10.08 ? 217 ILE B CD1 1 
ATOM   3883 N  N   . SER B  1 218 ? -10.845 -12.037 -6.254  1.00 7.06  ? 218 SER B N   1 
ATOM   3884 C  CA  . SER B  1 218 ? -9.943  -12.764 -7.139  1.00 6.96  ? 218 SER B CA  1 
ATOM   3885 C  C   . SER B  1 218 ? -8.776  -11.975 -7.618  1.00 8.91  ? 218 SER B C   1 
ATOM   3886 O  O   . SER B  1 218 ? -8.721  -10.721 -7.540  1.00 8.51  ? 218 SER B O   1 
ATOM   3887 C  CB  . SER B  1 218 ? -10.707 -13.269 -8.382  1.00 7.74  ? 218 SER B CB  1 
ATOM   3888 O  OG  . SER B  1 218 ? -11.202 -12.172 -9.179  1.00 9.26  ? 218 SER B OG  1 
ATOM   3889 N  N   . GLN B  1 219 ? -7.820  -12.662 -8.246  1.00 9.78  ? 219 GLN B N   1 
ATOM   3890 C  CA  . GLN B  1 219 ? -6.703  -11.991 -8.907  1.00 10.59 ? 219 GLN B CA  1 
ATOM   3891 C  C   . GLN B  1 219 ? -7.221  -10.992 -9.967  1.00 10.38 ? 219 GLN B C   1 
ATOM   3892 O  O   . GLN B  1 219 ? -6.609  -9.922  -10.106 1.00 8.76  ? 219 GLN B O   1 
ATOM   3893 C  CB  . GLN B  1 219 ? -5.795  -13.037 -9.579  1.00 12.47 ? 219 GLN B CB  1 
ATOM   3894 C  CG  . GLN B  1 219 ? -4.467  -12.411 -10.111 1.00 16.76 ? 219 GLN B CG  1 
ATOM   3895 C  CD  . GLN B  1 219 ? -4.516  -11.784 -11.491 1.00 19.48 ? 219 GLN B CD  1 
ATOM   3896 O  OE1 . GLN B  1 219 ? -3.655  -10.975 -11.849 1.00 21.48 ? 219 GLN B OE1 1 
ATOM   3897 N  NE2 . GLN B  1 219 ? -5.441  -12.230 -12.312 1.00 19.93 ? 219 GLN B NE2 1 
ATOM   3898 N  N   . GLU B  1 220 ? -8.244  -11.365 -10.703 1.00 10.30 ? 220 GLU B N   1 
ATOM   3899 C  CA  . GLU B  1 220 ? -8.730  -10.450 -11.744 1.00 10.21 ? 220 GLU B CA  1 
ATOM   3900 C  C   . GLU B  1 220 ? -9.401  -9.228  -11.107 1.00 10.62 ? 220 GLU B C   1 
ATOM   3901 O  O   . GLU B  1 220 ? -9.262  -8.114  -11.674 1.00 9.58  ? 220 GLU B O   1 
ATOM   3902 C  CB  . GLU B  1 220 ? -9.778  -11.174 -12.615 1.00 11.81 ? 220 GLU B CB  1 
ATOM   3903 C  CG  . GLU B  1 220 ? -9.157  -12.326 -13.485 1.00 12.51 ? 220 GLU B CG  1 
ATOM   3904 C  CD  . GLU B  1 220 ? -8.892  -13.653 -12.752 1.00 17.05 ? 220 GLU B CD  1 
ATOM   3905 O  OE1 . GLU B  1 220 ? -9.229  -13.815 -11.579 1.00 15.18 ? 220 GLU B OE1 1 
ATOM   3906 O  OE2 . GLU B  1 220 ? -8.318  -14.570 -13.394 1.00 22.41 ? 220 GLU B OE2 1 
ATOM   3907 N  N   . GLN B  1 221 ? -10.044 -9.361  -9.954  1.00 8.18  ? 221 GLN B N   1 
ATOM   3908 C  CA  . GLN B  1 221 ? -10.626 -8.202  -9.255  1.00 8.08  ? 221 GLN B CA  1 
ATOM   3909 C  C   . GLN B  1 221 ? -9.526  -7.379  -8.750  1.00 7.98  ? 221 GLN B C   1 
ATOM   3910 O  O   . GLN B  1 221 ? -9.563  -6.127  -8.930  1.00 8.40  ? 221 GLN B O   1 
ATOM   3911 C  CB  . GLN B  1 221 ? -11.504 -8.668  -8.110  1.00 7.99  ? 221 GLN B CB  1 
ATOM   3912 C  CG  . GLN B  1 221 ? -12.806 -9.256  -8.633  1.00 7.86  ? 221 GLN B CG  1 
ATOM   3913 C  CD  . GLN B  1 221 ? -13.678 -9.686  -7.492  1.00 7.16  ? 221 GLN B CD  1 
ATOM   3914 O  OE1 . GLN B  1 221 ? -13.394 -10.660 -6.773  1.00 8.98  ? 221 GLN B OE1 1 
ATOM   3915 N  NE2 . GLN B  1 221 ? -14.841 -9.052  -7.324  1.00 7.98  ? 221 GLN B NE2 1 
ATOM   3916 N  N   . LEU B  1 222 ? -8.503  -7.968  -8.144  1.00 8.12  ? 222 LEU B N   1 
ATOM   3917 C  CA  . LEU B  1 222 ? -7.355  -7.124  -7.683  1.00 7.91  ? 222 LEU B CA  1 
ATOM   3918 C  C   . LEU B  1 222 ? -6.741  -6.400  -8.903  1.00 8.48  ? 222 LEU B C   1 
ATOM   3919 O  O   . LEU B  1 222 ? -6.287  -5.245  -8.759  1.00 8.26  ? 222 LEU B O   1 
ATOM   3920 C  CB  . LEU B  1 222 ? -6.331  -8.059  -7.022  1.00 9.18  ? 222 LEU B CB  1 
ATOM   3921 C  CG  . LEU B  1 222 ? -6.699  -8.405  -5.605  1.00 8.48  ? 222 LEU B CG  1 
ATOM   3922 C  CD1 . LEU B  1 222 ? -6.013  -9.690  -5.023  1.00 10.07 ? 222 LEU B CD1 1 
ATOM   3923 C  CD2 . LEU B  1 222 ? -6.355  -7.210  -4.655  1.00 9.48  ? 222 LEU B CD2 1 
ATOM   3924 N  N   . LEU B  1 223 ? -6.570  -7.125  -10.024 1.00 8.38  ? 223 LEU B N   1 
ATOM   3925 C  CA  . LEU B  1 223 ? -5.886  -6.491  -11.159 1.00 8.76  ? 223 LEU B CA  1 
ATOM   3926 C  C   . LEU B  1 223 ? -6.722  -5.300  -11.620 1.00 9.45  ? 223 LEU B C   1 
ATOM   3927 O  O   . LEU B  1 223 ? -6.128  -4.259  -12.015 1.00 9.58  ? 223 LEU B O   1 
ATOM   3928 C  CB  . LEU B  1 223 ? -5.730  -7.532  -12.319 1.00 11.76 ? 223 LEU B CB  1 
ATOM   3929 C  CG  . LEU B  1 223 ? -4.888  -6.939  -13.482 1.00 11.10 ? 223 LEU B CG  1 
ATOM   3930 C  CD1 . LEU B  1 223 ? -3.473  -6.619  -12.958 1.00 12.92 ? 223 LEU B CD1 1 
ATOM   3931 C  CD2 . LEU B  1 223 ? -4.901  -7.936  -14.642 1.00 14.00 ? 223 LEU B CD2 1 
ATOM   3932 N  N   . ALA B  1 224 ? -8.026  -5.415  -11.684 1.00 9.44  ? 224 ALA B N   1 
ATOM   3933 C  CA  . ALA B  1 224 ? -8.864  -4.266  -12.084 1.00 9.41  ? 224 ALA B CA  1 
ATOM   3934 C  C   . ALA B  1 224 ? -8.649  -3.132  -11.071 1.00 10.13 ? 224 ALA B C   1 
ATOM   3935 O  O   . ALA B  1 224 ? -8.417  -1.993  -11.471 1.00 10.56 ? 224 ALA B O   1 
ATOM   3936 C  CB  . ALA B  1 224 ? -10.340 -4.644  -12.139 1.00 11.05 ? 224 ALA B CB  1 
ATOM   3937 N  N   . LEU B  1 225 ? -8.674  -3.380  -9.766  1.00 9.74  ? 225 LEU B N   1 
ATOM   3938 C  CA  . LEU B  1 225 ? -8.477  -2.345  -8.747  1.00 9.10  ? 225 LEU B CA  1 
ATOM   3939 C  C   . LEU B  1 225 ? -7.133  -1.659  -8.924  1.00 9.66  ? 225 LEU B C   1 
ATOM   3940 O  O   . LEU B  1 225 ? -7.018  -0.448  -8.751  1.00 10.44 ? 225 LEU B O   1 
ATOM   3941 C  CB  . LEU B  1 225 ? -8.620  -3.015  -7.345  1.00 8.24  ? 225 LEU B CB  1 
ATOM   3942 C  CG  . LEU B  1 225 ? -8.508  -2.026  -6.181  1.00 8.53  ? 225 LEU B CG  1 
ATOM   3943 C  CD1 . LEU B  1 225 ? -9.571  -0.926  -6.223  1.00 9.76  ? 225 LEU B CD1 1 
ATOM   3944 C  CD2 . LEU B  1 225 ? -8.633  -2.794  -4.900  1.00 9.94  ? 225 LEU B CD2 1 
ATOM   3945 N  N   . GLU B  1 226 ? -6.110  -2.466  -9.239  1.00 8.53  ? 226 GLU B N   1 
ATOM   3946 C  CA  . GLU B  1 226 ? -4.719  -1.981  -9.327  1.00 9.08  ? 226 GLU B CA  1 
ATOM   3947 C  C   . GLU B  1 226 ? -4.394  -1.293  -10.679 1.00 8.58  ? 226 GLU B C   1 
ATOM   3948 O  O   . GLU B  1 226 ? -3.280  -0.713  -10.746 1.00 11.73 ? 226 GLU B O   1 
ATOM   3949 C  CB  . GLU B  1 226 ? -3.745  -3.175  -9.148  1.00 8.26  ? 226 GLU B CB  1 
ATOM   3950 C  CG  . GLU B  1 226 ? -3.803  -3.843  -7.774  1.00 9.13  ? 226 GLU B CG  1 
ATOM   3951 C  CD  . GLU B  1 226 ? -3.455  -5.288  -7.802  1.00 9.76  ? 226 GLU B CD  1 
ATOM   3952 O  OE1 . GLU B  1 226 ? -3.228  -5.911  -8.901  1.00 9.22  ? 226 GLU B OE1 1 
ATOM   3953 O  OE2 . GLU B  1 226 ? -3.488  -5.899  -6.718  1.00 10.08 ? 226 GLU B OE2 1 
ATOM   3954 N  N   . THR B  1 227 ? -5.243  -1.421  -11.651 1.00 8.60  ? 227 THR B N   1 
ATOM   3955 C  CA  . THR B  1 227 ? -4.969  -0.825  -12.962 1.00 8.94  ? 227 THR B CA  1 
ATOM   3956 C  C   . THR B  1 227 ? -5.937  0.207   -13.399 1.00 10.39 ? 227 THR B C   1 
ATOM   3957 O  O   . THR B  1 227 ? -5.618  0.918   -14.381 1.00 12.01 ? 227 THR B O   1 
ATOM   3958 C  CB  . THR B  1 227 ? -4.901  -1.895  -14.116 1.00 9.44  ? 227 THR B CB  1 
ATOM   3959 O  OG1 . THR B  1 227 ? -6.140  -2.612  -14.224 1.00 10.09 ? 227 THR B OG1 1 
ATOM   3960 C  CG2 . THR B  1 227 ? -3.691  -2.920  -13.876 1.00 8.91  ? 227 THR B CG2 1 
ATOM   3961 N  N   . ALA B  1 228 ? -7.092  0.299   -12.755 1.00 8.98  ? 228 ALA B N   1 
ATOM   3962 C  CA  . ALA B  1 228 ? -8.163  1.170   -13.322 1.00 9.84  ? 228 ALA B CA  1 
ATOM   3963 C  C   . ALA B  1 228 ? -7.909  2.639   -12.989 1.00 10.59 ? 228 ALA B C   1 
ATOM   3964 O  O   . ALA B  1 228 ? -8.491  3.495   -13.649 1.00 11.40 ? 228 ALA B O   1 
ATOM   3965 C  CB  . ALA B  1 228 ? -9.500  0.780   -12.791 1.00 10.23 ? 228 ALA B CB  1 
ATOM   3966 N  N   . LEU B  1 229 ? -7.246  2.944   -11.910 1.00 9.40  ? 229 LEU B N   1 
ATOM   3967 C  CA  . LEU B  1 229 ? -7.370  4.283   -11.271 1.00 8.50  ? 229 LEU B CA  1 
ATOM   3968 C  C   . LEU B  1 229 ? -6.078  5.035   -11.304 1.00 8.34  ? 229 LEU B C   1 
ATOM   3969 O  O   . LEU B  1 229 ? -5.001  4.503   -11.266 1.00 8.47  ? 229 LEU B O   1 
ATOM   3970 C  CB  . LEU B  1 229 ? -7.870  4.212   -9.796  1.00 9.97  ? 229 LEU B CB  1 
ATOM   3971 C  CG  . LEU B  1 229 ? -9.102  3.284   -9.632  1.00 10.01 ? 229 LEU B CG  1 
ATOM   3972 C  CD1 . LEU B  1 229 ? -9.368  3.147   -8.129  1.00 12.47 ? 229 LEU B CD1 1 
ATOM   3973 C  CD2 . LEU B  1 229 ? -10.274 3.915   -10.311 1.00 14.31 ? 229 LEU B CD2 1 
ATOM   3974 N  N   . TYR B  1 230 ? -6.252  6.337   -11.371 1.00 8.56  ? 230 TYR B N   1 
ATOM   3975 C  CA  . TYR B  1 230 ? -5.205  7.381   -11.407 1.00 8.44  ? 230 TYR B CA  1 
ATOM   3976 C  C   . TYR B  1 230 ? -5.382  8.350   -10.243 1.00 8.59  ? 230 TYR B C   1 
ATOM   3977 O  O   . TYR B  1 230 ? -6.554  8.715   -9.910  1.00 8.62  ? 230 TYR B O   1 
ATOM   3978 C  CB  . TYR B  1 230 ? -5.160  8.138   -12.759 1.00 8.60  ? 230 TYR B CB  1 
ATOM   3979 C  CG  . TYR B  1 230 ? -4.611  7.170   -13.781 1.00 8.66  ? 230 TYR B CG  1 
ATOM   3980 C  CD1 . TYR B  1 230 ? -5.433  6.220   -14.370 1.00 9.57  ? 230 TYR B CD1 1 
ATOM   3981 C  CD2 . TYR B  1 230 ? -3.255  7.133   -14.068 1.00 11.48 ? 230 TYR B CD2 1 
ATOM   3982 C  CE1 . TYR B  1 230 ? -4.929  5.299   -15.270 1.00 11.13 ? 230 TYR B CE1 1 
ATOM   3983 C  CE2 . TYR B  1 230 ? -2.742  6.216   -14.967 1.00 11.52 ? 230 TYR B CE2 1 
ATOM   3984 C  CZ  . TYR B  1 230 ? -3.583  5.302   -15.564 1.00 11.93 ? 230 TYR B CZ  1 
ATOM   3985 O  OH  . TYR B  1 230 ? -3.075  4.389   -16.459 1.00 16.91 ? 230 TYR B OH  1 
ATOM   3986 N  N   . CYS B  1 231 ? -4.303  8.809   -9.607  1.00 8.41  ? 231 CYS B N   1 
ATOM   3987 C  CA  . CYS B  1 231 ? -4.320  9.818   -8.587  1.00 8.70  ? 231 CYS B CA  1 
ATOM   3988 C  C   . CYS B  1 231 ? -4.606  11.211  -9.157  1.00 9.30  ? 231 CYS B C   1 
ATOM   3989 O  O   . CYS B  1 231 ? -4.950  12.122  -8.447  1.00 10.77 ? 231 CYS B O   1 
ATOM   3990 C  CB  . CYS B  1 231 ? -2.962  9.939   -7.913  1.00 9.07  ? 231 CYS B CB  1 
ATOM   3991 S  SG  . CYS B  1 231 ? -2.480  8.389   -7.050  1.00 10.34 ? 231 CYS B SG  1 
ATOM   3992 N  N   . THR B  1 232 ? -4.419  11.300  -10.474 1.00 8.71  ? 232 THR B N   1 
ATOM   3993 C  CA  . THR B  1 232 ? -4.414  12.625  -11.141 1.00 8.86  ? 232 THR B CA  1 
ATOM   3994 C  C   . THR B  1 232 ? -5.723  12.859  -11.904 1.00 9.44  ? 232 THR B C   1 
ATOM   3995 O  O   . THR B  1 232 ? -6.485  11.950  -12.268 1.00 10.42 ? 232 THR B O   1 
ATOM   3996 C  CB  . THR B  1 232 ? -3.188  12.668  -12.116 1.00 8.56  ? 232 THR B CB  1 
ATOM   3997 O  OG1 . THR B  1 232 ? -3.011  11.391  -12.750 1.00 9.39  ? 232 THR B OG1 1 
ATOM   3998 C  CG2 . THR B  1 232 ? -1.922  12.992  -11.314 1.00 10.54 ? 232 THR B CG2 1 
ATOM   3999 N  N   . HIS B  1 233 ? -5.960  14.151  -12.192 1.00 9.34  ? 233 HIS B N   1 
ATOM   4000 C  CA  . HIS B  1 233 ? -7.067  14.477  -13.079 1.00 10.37 ? 233 HIS B CA  1 
ATOM   4001 C  C   . HIS B  1 233 ? -6.988  13.945  -14.515 1.00 9.05  ? 233 HIS B C   1 
ATOM   4002 O  O   . HIS B  1 233 ? -5.874  13.693  -15.007 1.00 9.82  ? 233 HIS B O   1 
ATOM   4003 C  CB  . HIS B  1 233 ? -7.280  15.997  -13.154 1.00 11.18 ? 233 HIS B CB  1 
ATOM   4004 C  CG  . HIS B  1 233 ? -7.697  16.581  -11.852 1.00 13.25 ? 233 HIS B CG  1 
ATOM   4005 N  ND1 . HIS B  1 233 ? -6.878  17.309  -11.076 1.00 20.39 ? 233 HIS B ND1 1 
ATOM   4006 C  CD2 . HIS B  1 233 ? -8.856  16.475  -11.177 1.00 15.46 ? 233 HIS B CD2 1 
ATOM   4007 C  CE1 . HIS B  1 233 ? -7.512  17.689  -9.962  1.00 21.01 ? 233 HIS B CE1 1 
ATOM   4008 N  NE2 . HIS B  1 233 ? -8.709  17.209  -10.013 1.00 18.32 ? 233 HIS B NE2 1 
ATOM   4009 N  N   . MET B  1 234 ? -8.135  13.810  -15.202 1.00 9.73  ? 234 MET B N   1 
ATOM   4010 C  CA  . MET B  1 234 ? -8.204  13.276  -16.569 1.00 10.25 ? 234 MET B CA  1 
ATOM   4011 C  C   . MET B  1 234 ? -7.314  14.081  -17.531 1.00 10.21 ? 234 MET B C   1 
ATOM   4012 O  O   . MET B  1 234 ? -6.687  13.508  -18.438 1.00 11.55 ? 234 MET B O   1 
ATOM   4013 C  CB  . MET B  1 234 ? -9.629  13.341  -17.042 1.00 11.91 ? 234 MET B CB  1 
ATOM   4014 C  CG  . MET B  1 234 ? -9.816  12.711  -18.423 1.00 13.47 ? 234 MET B CG  1 
ATOM   4015 S  SD  . MET B  1 234 ? -11.653 12.433  -18.648 1.00 20.45 ? 234 MET B SD  1 
ATOM   4016 C  CE  . MET B  1 234 ? -11.617 11.527  -20.251 1.00 20.76 ? 234 MET B CE  1 
ATOM   4017 N  N   . ASP B  1 235 ? -7.140  15.376  -17.250 1.00 11.06 ? 235 ASP B N   1 
ATOM   4018 C  CA  . ASP B  1 235 ? -6.299  16.201  -18.193 1.00 12.94 ? 235 ASP B CA  1 
ATOM   4019 C  C   . ASP B  1 235 ? -4.935  16.450  -17.683 1.00 12.93 ? 235 ASP B C   1 
ATOM   4020 O  O   . ASP B  1 235 ? -4.228  17.324  -18.264 1.00 15.69 ? 235 ASP B O   1 
ATOM   4021 C  CB  . ASP B  1 235 ? -7.005  17.522  -18.511 1.00 15.10 ? 235 ASP B CB  1 
ATOM   4022 C  CG  . ASP B  1 235 ? -7.113  18.411  -17.300 1.00 21.40 ? 235 ASP B CG  1 
ATOM   4023 O  OD1 . ASP B  1 235 ? -6.749  18.038  -16.139 1.00 19.32 ? 235 ASP B OD1 1 
ATOM   4024 O  OD2 . ASP B  1 235 ? -7.663  19.557  -17.520 1.00 24.42 ? 235 ASP B OD2 1 
ATOM   4025 N  N   . ASP B  1 236 ? -4.415  15.683  -16.700 1.00 10.39 ? 236 ASP B N   1 
ATOM   4026 C  CA  . ASP B  1 236 ? -3.120  16.026  -16.151 1.00 10.49 ? 236 ASP B CA  1 
ATOM   4027 C  C   . ASP B  1 236 ? -2.016  15.534  -17.099 1.00 11.54 ? 236 ASP B C   1 
ATOM   4028 O  O   . ASP B  1 236 ? -1.984  14.348  -17.489 1.00 11.15 ? 236 ASP B O   1 
ATOM   4029 C  CB  . ASP B  1 236 ? -2.942  15.299  -14.764 1.00 10.69 ? 236 ASP B CB  1 
ATOM   4030 C  CG  . ASP B  1 236 ? -1.804  15.935  -13.974 1.00 13.40 ? 236 ASP B CG  1 
ATOM   4031 O  OD1 . ASP B  1 236 ? -0.662  16.086  -14.477 1.00 13.29 ? 236 ASP B OD1 1 
ATOM   4032 O  OD2 . ASP B  1 236 ? -1.960  16.264  -12.797 1.00 14.54 ? 236 ASP B OD2 1 
ATOM   4033 N  N   . PRO B  1 237 ? -1.034  16.378  -17.499 1.00 10.57 ? 237 PRO B N   1 
ATOM   4034 C  CA  . PRO B  1 237 ? 0.002   15.914  -18.398 1.00 11.01 ? 237 PRO B CA  1 
ATOM   4035 C  C   . PRO B  1 237 ? 1.120   15.095  -17.683 1.00 10.65 ? 237 PRO B C   1 
ATOM   4036 O  O   . PRO B  1 237 ? 2.029   14.581  -18.358 1.00 10.42 ? 237 PRO B O   1 
ATOM   4037 C  CB  . PRO B  1 237 ? 0.524   17.261  -18.965 1.00 12.01 ? 237 PRO B CB  1 
ATOM   4038 C  CG  . PRO B  1 237 ? 0.364   18.199  -17.758 1.00 11.22 ? 237 PRO B CG  1 
ATOM   4039 C  CD  . PRO B  1 237 ? -1.029  17.848  -17.310 1.00 10.18 ? 237 PRO B CD  1 
ATOM   4040 N  N   A SER B  1 238 ? 0.994   14.886  -16.341 0.50 10.68 ? 238 SER B N   1 
ATOM   4041 N  N   B SER B  1 238 ? 1.079   14.898  -16.338 0.50 10.13 ? 238 SER B N   1 
ATOM   4042 C  CA  A SER B  1 238 ? 1.900   14.069  -15.519 0.50 10.99 ? 238 SER B CA  1 
ATOM   4043 C  CA  B SER B  1 238 ? 1.954   13.927  -15.661 0.50 10.30 ? 238 SER B CA  1 
ATOM   4044 C  C   A SER B  1 238 ? 1.129   12.977  -14.776 0.50 9.87  ? 238 SER B C   1 
ATOM   4045 C  C   B SER B  1 238 ? 1.066   13.017  -14.832 0.50 9.57  ? 238 SER B C   1 
ATOM   4046 O  O   A SER B  1 238 ? 1.112   12.972  -13.560 0.50 11.10 ? 238 SER B O   1 
ATOM   4047 O  O   B SER B  1 238 ? 0.837   13.207  -13.651 0.50 10.45 ? 238 SER B O   1 
ATOM   4048 C  CB  A SER B  1 238 ? 2.602   14.933  -14.478 0.50 12.15 ? 238 SER B CB  1 
ATOM   4049 C  CB  B SER B  1 238 ? 2.973   14.576  -14.765 0.50 10.66 ? 238 SER B CB  1 
ATOM   4050 O  OG  A SER B  1 238 ? 3.710   14.198  -13.987 0.50 16.29 ? 238 SER B OG  1 
ATOM   4051 O  OG  B SER B  1 238 ? 3.533   15.746  -15.350 0.50 12.30 ? 238 SER B OG  1 
ATOM   4052 N  N   . PRO B  1 239 ? 0.467   12.083  -15.529 1.00 9.40  ? 239 PRO B N   1 
ATOM   4053 C  CA  . PRO B  1 239 ? -0.405  11.083  -14.830 1.00 10.24 ? 239 PRO B CA  1 
ATOM   4054 C  C   . PRO B  1 239 ? 0.366   10.244  -13.850 1.00 10.02 ? 239 PRO B C   1 
ATOM   4055 O  O   . PRO B  1 239 ? 1.544   9.906   -14.007 1.00 11.25 ? 239 PRO B O   1 
ATOM   4056 C  CB  . PRO B  1 239 ? -0.911  10.196  -15.957 1.00 11.61 ? 239 PRO B CB  1 
ATOM   4057 C  CG  . PRO B  1 239 ? -0.246  10.620  -17.222 1.00 14.21 ? 239 PRO B CG  1 
ATOM   4058 C  CD  . PRO B  1 239 ? 0.541   11.888  -17.001 1.00 10.71 ? 239 PRO B CD  1 
ATOM   4059 N  N   . ARG B  1 240 ? -0.332  9.884   -12.755 1.00 8.69  ? 240 ARG B N   1 
ATOM   4060 C  CA  . ARG B  1 240 ? 0.223   9.018   -11.740 1.00 8.78  ? 240 ARG B CA  1 
ATOM   4061 C  C   . ARG B  1 240 ? -0.799  7.896   -11.422 1.00 9.05  ? 240 ARG B C   1 
ATOM   4062 O  O   . ARG B  1 240 ? -1.939  8.170   -11.093 1.00 9.83  ? 240 ARG B O   1 
ATOM   4063 C  CB  . ARG B  1 240 ? 0.522   9.783   -10.462 1.00 8.85  ? 240 ARG B CB  1 
ATOM   4064 C  CG  . ARG B  1 240 ? 1.723   10.730  -10.634 1.00 10.76 ? 240 ARG B CG  1 
ATOM   4065 C  CD  . ARG B  1 240 ? 1.921   11.528  -9.336  1.00 13.15 ? 240 ARG B CD  1 
ATOM   4066 N  NE  . ARG B  1 240 ? 0.867   12.499  -9.048  1.00 14.34 ? 240 ARG B NE  1 
ATOM   4067 C  CZ  . ARG B  1 240 ? -0.001  12.366  -8.025  1.00 13.17 ? 240 ARG B CZ  1 
ATOM   4068 N  NH1 . ARG B  1 240 ? 0.026   11.273  -7.267  1.00 12.28 ? 240 ARG B NH1 1 
ATOM   4069 N  NH2 . ARG B  1 240 ? -0.904  13.283  -7.809  1.00 15.86 ? 240 ARG B NH2 1 
ATOM   4070 N  N   . GLU B  1 241 ? -0.397  6.663   -11.612 1.00 9.68  ? 241 GLU B N   1 
ATOM   4071 C  CA  . GLU B  1 241 ? -1.267  5.525   -11.308 1.00 9.46  ? 241 GLU B CA  1 
ATOM   4072 C  C   . GLU B  1 241 ? -1.545  5.477   -9.797  1.00 8.33  ? 241 GLU B C   1 
ATOM   4073 O  O   . GLU B  1 241 ? -0.676  5.679   -8.947  1.00 9.15  ? 241 GLU B O   1 
ATOM   4074 C  CB  . GLU B  1 241 ? -0.550  4.258   -11.693 1.00 12.14 ? 241 GLU B CB  1 
ATOM   4075 C  CG  . GLU B  1 241 ? -0.394  4.158   -13.206 1.00 13.19 ? 241 GLU B CG  1 
ATOM   4076 C  CD  . GLU B  1 241 ? 0.477   2.975   -13.596 1.00 18.06 ? 241 GLU B CD  1 
ATOM   4077 O  OE1 . GLU B  1 241 ? 1.478   2.721   -12.883 1.00 23.17 ? 241 GLU B OE1 1 
ATOM   4078 O  OE2 . GLU B  1 241 ? 0.074   2.257   -14.514 1.00 23.74 ? 241 GLU B OE2 1 
ATOM   4079 N  N   . MET B  1 242 ? -2.800  5.113   -9.481  1.00 7.44  ? 242 MET B N   1 
ATOM   4080 C  CA  . MET B  1 242 ? -3.164  4.926   -8.027  1.00 7.63  ? 242 MET B CA  1 
ATOM   4081 C  C   . MET B  1 242 ? -2.887  3.455   -7.634  1.00 6.86  ? 242 MET B C   1 
ATOM   4082 O  O   . MET B  1 242 ? -3.691  2.576   -7.877  1.00 7.31  ? 242 MET B O   1 
ATOM   4083 C  CB  . MET B  1 242 ? -4.602  5.314   -7.889  1.00 8.42  ? 242 MET B CB  1 
ATOM   4084 C  CG  . MET B  1 242 ? -4.987  5.250   -6.376  1.00 8.16  ? 242 MET B CG  1 
ATOM   4085 S  SD  . MET B  1 242 ? -6.732  5.635   -6.070  1.00 8.10  ? 242 MET B SD  1 
ATOM   4086 C  CE  . MET B  1 242 ? -6.828  7.339   -6.673  1.00 9.42  ? 242 MET B CE  1 
ATOM   4087 N  N   . ILE B  1 243 ? -1.661  3.311   -7.179  1.00 7.05  ? 243 ILE B N   1 
ATOM   4088 C  CA  . ILE B  1 243 ? -1.108  2.013   -6.766  1.00 7.18  ? 243 ILE B CA  1 
ATOM   4089 C  C   . ILE B  1 243 ? -0.352  2.225   -5.470  1.00 7.33  ? 243 ILE B C   1 
ATOM   4090 O  O   . ILE B  1 243 ? 0.106   3.347   -5.148  1.00 7.53  ? 243 ILE B O   1 
ATOM   4091 C  CB  . ILE B  1 243 ? -0.167  1.397   -7.864  1.00 9.39  ? 243 ILE B CB  1 
ATOM   4092 C  CG1 . ILE B  1 243 ? 0.958   2.416   -8.182  1.00 9.55  ? 243 ILE B CG1 1 
ATOM   4093 C  CG2 . ILE B  1 243 ? -0.977  0.966   -9.028  1.00 8.89  ? 243 ILE B CG2 1 
ATOM   4094 C  CD1 . ILE B  1 243 ? 1.943   1.810   -9.177  1.00 12.65 ? 243 ILE B CD1 1 
ATOM   4095 N  N   . ASN B  1 244 ? -0.181  1.105   -4.725  1.00 7.00  ? 244 ASN B N   1 
ATOM   4096 C  CA  . ASN B  1 244 ? 0.641   1.113   -3.529  1.00 7.47  ? 244 ASN B CA  1 
ATOM   4097 C  C   . ASN B  1 244 ? 0.267   2.217   -2.554  1.00 7.43  ? 244 ASN B C   1 
ATOM   4098 O  O   . ASN B  1 244 ? 1.037   2.867   -1.925  1.00 7.49  ? 244 ASN B O   1 
ATOM   4099 C  CB  . ASN B  1 244 ? 2.161   1.234   -3.846  1.00 8.69  ? 244 ASN B CB  1 
ATOM   4100 C  CG  . ASN B  1 244 ? 2.547   0.174   -4.852  1.00 9.69  ? 244 ASN B CG  1 
ATOM   4101 O  OD1 . ASN B  1 244 ? 2.171   -0.999  -4.794  1.00 11.21 ? 244 ASN B OD1 1 
ATOM   4102 N  ND2 . ASN B  1 244 ? 3.320   0.625   -5.842  1.00 12.90 ? 244 ASN B ND2 1 
ATOM   4103 N  N   . ASN B  1 245 ? -1.080  2.376   -2.405  1.00 6.83  ? 245 ASN B N   1 
ATOM   4104 C  CA  . ASN B  1 245 ? -1.654  3.436   -1.612  1.00 6.26  ? 245 ASN B CA  1 
ATOM   4105 C  C   . ASN B  1 245 ? -1.944  2.896   -0.224  1.00 6.32  ? 245 ASN B C   1 
ATOM   4106 O  O   . ASN B  1 245 ? -3.029  3.009   0.347   1.00 7.29  ? 245 ASN B O   1 
ATOM   4107 C  CB  . ASN B  1 245 ? -2.961  4.028   -2.284  1.00 6.81  ? 245 ASN B CB  1 
ATOM   4108 C  CG  . ASN B  1 245 ? -4.036  3.052   -2.438  1.00 6.69  ? 245 ASN B CG  1 
ATOM   4109 O  OD1 . ASN B  1 245 ? -3.836  1.839   -2.460  1.00 7.28  ? 245 ASN B OD1 1 
ATOM   4110 N  ND2 . ASN B  1 245 ? -5.266  3.603   -2.658  1.00 7.08  ? 245 ASN B ND2 1 
ATOM   4111 N  N   . PHE B  1 246 ? -0.899  2.395   0.417   1.00 5.83  ? 246 PHE B N   1 
ATOM   4112 C  CA  . PHE B  1 246 ? -0.919  1.930   1.852   1.00 6.22  ? 246 PHE B CA  1 
ATOM   4113 C  C   . PHE B  1 246 ? 0.266   2.554   2.586   1.00 6.51  ? 246 PHE B C   1 
ATOM   4114 O  O   . PHE B  1 246 ? 1.336   2.741   1.967   1.00 6.55  ? 246 PHE B O   1 
ATOM   4115 C  CB  . PHE B  1 246 ? -0.844  0.356   1.923   1.00 7.55  ? 246 PHE B CB  1 
ATOM   4116 C  CG  . PHE B  1 246 ? 0.411   -0.243  1.303   1.00 6.90  ? 246 PHE B CG  1 
ATOM   4117 C  CD1 . PHE B  1 246 ? 0.490   -0.494  -0.055  1.00 7.93  ? 246 PHE B CD1 1 
ATOM   4118 C  CD2 . PHE B  1 246 ? 1.497   -0.582  2.090   1.00 7.91  ? 246 PHE B CD2 1 
ATOM   4119 C  CE1 . PHE B  1 246 ? 1.631   -1.053  -0.616  1.00 8.32  ? 246 PHE B CE1 1 
ATOM   4120 C  CE2 . PHE B  1 246 ? 2.630   -1.140  1.545   1.00 8.51  ? 246 PHE B CE2 1 
ATOM   4121 C  CZ  . PHE B  1 246 ? 2.703   -1.383  0.188   1.00 8.41  ? 246 PHE B CZ  1 
ATOM   4122 N  N   . ARG B  1 247 ? 0.093   2.851   3.833   1.00 6.16  ? 247 ARG B N   1 
ATOM   4123 C  CA  . ARG B  1 247 ? 1.196   3.377   4.697   1.00 6.31  ? 247 ARG B CA  1 
ATOM   4124 C  C   . ARG B  1 247 ? 1.941   2.188   5.273   1.00 6.63  ? 247 ARG B C   1 
ATOM   4125 O  O   . ARG B  1 247 ? 1.316   1.173   5.646   1.00 7.19  ? 247 ARG B O   1 
ATOM   4126 C  CB  . ARG B  1 247 ? 0.606   4.254   5.806   1.00 6.46  ? 247 ARG B CB  1 
ATOM   4127 C  CG  . ARG B  1 247 ? 1.594   5.133   6.532   1.00 6.34  ? 247 ARG B CG  1 
ATOM   4128 C  CD  . ARG B  1 247 ? 0.908   5.753   7.724   1.00 7.69  ? 247 ARG B CD  1 
ATOM   4129 N  NE  . ARG B  1 247 ? 1.774   6.842   8.283   1.00 7.40  ? 247 ARG B NE  1 
ATOM   4130 C  CZ  . ARG B  1 247 ? 1.479   7.557   9.376   1.00 7.33  ? 247 ARG B CZ  1 
ATOM   4131 N  NH1 . ARG B  1 247 ? 0.375   7.259   10.081  1.00 8.15  ? 247 ARG B NH1 1 
ATOM   4132 N  NH2 . ARG B  1 247 ? 2.229   8.594   9.741   1.00 8.10  ? 247 ARG B NH2 1 
ATOM   4133 N  N   . GLN B  1 248 ? 3.250   2.357   5.514   1.00 6.51  ? 248 GLN B N   1 
ATOM   4134 C  CA  . GLN B  1 248 ? 3.996   1.329   6.299   1.00 7.20  ? 248 GLN B CA  1 
ATOM   4135 C  C   . GLN B  1 248 ? 3.505   1.279   7.708   1.00 7.01  ? 248 GLN B C   1 
ATOM   4136 O  O   . GLN B  1 248 ? 2.986   2.248   8.238   1.00 7.13  ? 248 GLN B O   1 
ATOM   4137 C  CB  . GLN B  1 248 ? 5.505   1.680   6.325   1.00 7.34  ? 248 GLN B CB  1 
ATOM   4138 C  CG  . GLN B  1 248 ? 6.192   1.687   4.932   1.00 7.62  ? 248 GLN B CG  1 
ATOM   4139 C  CD  . GLN B  1 248 ? 6.182   0.309   4.306   1.00 8.32  ? 248 GLN B CD  1 
ATOM   4140 O  OE1 . GLN B  1 248 ? 5.271   -0.036  3.559   1.00 7.03  ? 248 GLN B OE1 1 
ATOM   4141 N  NE2 . GLN B  1 248 ? 7.190   -0.507  4.612   1.00 8.70  ? 248 GLN B NE2 1 
ATOM   4142 N  N   . VAL B  1 249 ? 3.721   0.120   8.366   1.00 7.09  ? 249 VAL B N   1 
ATOM   4143 C  CA  . VAL B  1 249 ? 3.317   -0.045  9.773   1.00 7.66  ? 249 VAL B CA  1 
ATOM   4144 C  C   . VAL B  1 249 ? 4.174   0.830   10.665  1.00 7.68  ? 249 VAL B C   1 
ATOM   4145 O  O   . VAL B  1 249 ? 5.326   1.192   10.285  1.00 8.04  ? 249 VAL B O   1 
ATOM   4146 C  CB  . VAL B  1 249 ? 3.361   -1.488  10.244  1.00 8.58  ? 249 VAL B CB  1 
ATOM   4147 C  CG1 . VAL B  1 249 ? 2.269   -2.326  9.531   1.00 8.82  ? 249 VAL B CG1 1 
ATOM   4148 C  CG2 . VAL B  1 249 ? 4.755   -2.154  10.082  1.00 9.00  ? 249 VAL B CG2 1 
ATOM   4149 N  N   . GLN B  1 250 ? 3.586   1.209   11.789  1.00 7.64  ? 250 GLN B N   1 
ATOM   4150 C  CA  . GLN B  1 250 ? 4.114   2.217   12.716  1.00 8.03  ? 250 GLN B CA  1 
ATOM   4151 C  C   . GLN B  1 250 ? 4.621   1.604   13.974  1.00 8.63  ? 250 GLN B C   1 
ATOM   4152 O  O   . GLN B  1 250 ? 4.163   0.528   14.396  1.00 10.78 ? 250 GLN B O   1 
ATOM   4153 C  CB  . GLN B  1 250 ? 3.007   3.246   13.087  1.00 8.09  ? 250 GLN B CB  1 
ATOM   4154 C  CG  . GLN B  1 250 ? 2.394   3.891   11.842  1.00 9.02  ? 250 GLN B CG  1 
ATOM   4155 C  CD  . GLN B  1 250 ? 3.288   4.832   11.093  1.00 9.24  ? 250 GLN B CD  1 
ATOM   4156 O  OE1 . GLN B  1 250 ? 3.707   5.834   11.668  1.00 10.38 ? 250 GLN B OE1 1 
ATOM   4157 N  NE2 . GLN B  1 250 ? 3.579   4.537   9.837   1.00 8.22  ? 250 GLN B NE2 1 
ATOM   4158 N  N   . LYS B  1 251 ? 5.561   2.316   14.645  1.00 8.36  ? 251 LYS B N   1 
ATOM   4159 C  CA  . LYS B  1 251 ? 6.004   1.834   15.994  1.00 9.98  ? 251 LYS B CA  1 
ATOM   4160 C  C   . LYS B  1 251 ? 4.773   1.788   16.950  1.00 10.35 ? 251 LYS B C   1 
ATOM   4161 O  O   . LYS B  1 251 ? 3.803   2.603   16.848  1.00 10.02 ? 251 LYS B O   1 
ATOM   4162 C  CB  . LYS B  1 251 ? 7.005   2.848   16.650  1.00 11.83 ? 251 LYS B CB  1 
ATOM   4163 C  CG  . LYS B  1 251 ? 8.375   2.919   15.963  1.00 11.65 ? 251 LYS B CG  1 
ATOM   4164 C  CD  . LYS B  1 251 ? 9.190   1.749   16.467  1.00 10.54 ? 251 LYS B CD  1 
ATOM   4165 C  CE  . LYS B  1 251 ? 10.674  1.721   16.051  1.00 10.39 ? 251 LYS B CE  1 
ATOM   4166 N  NZ  . LYS B  1 251 ? 10.863  1.862   14.539  1.00 9.25  ? 251 LYS B NZ  1 
ATOM   4167 N  N   . PHE B  1 252 ? 4.799   0.875   17.886  1.00 12.23 ? 252 PHE B N   1 
ATOM   4168 C  CA  . PHE B  1 252 ? 3.707   0.785   18.828  1.00 14.57 ? 252 PHE B CA  1 
ATOM   4169 C  C   . PHE B  1 252 ? 3.583   1.920   19.896  1.00 19.33 ? 252 PHE B C   1 
ATOM   4170 O  O   . PHE B  1 252 ? 2.504   2.121   20.399  1.00 23.94 ? 252 PHE B O   1 
ATOM   4171 C  CB  . PHE B  1 252 ? 3.709   -0.574  19.508  1.00 13.41 ? 252 PHE B CB  1 
ATOM   4172 C  CG  . PHE B  1 252 ? 3.037   -1.622  18.697  1.00 13.24 ? 252 PHE B CG  1 
ATOM   4173 C  CD1 . PHE B  1 252 ? 3.674   -2.165  17.598  1.00 15.37 ? 252 PHE B CD1 1 
ATOM   4174 C  CD2 . PHE B  1 252 ? 1.752   -2.026  18.998  1.00 13.65 ? 252 PHE B CD2 1 
ATOM   4175 C  CE1 . PHE B  1 252 ? 3.052   -3.122  16.828  1.00 15.30 ? 252 PHE B CE1 1 
ATOM   4176 C  CE2 . PHE B  1 252 ? 1.121   -2.983  18.233  1.00 14.30 ? 252 PHE B CE2 1 
ATOM   4177 C  CZ  . PHE B  1 252 ? 1.772   -3.532  17.145  1.00 13.44 ? 252 PHE B CZ  1 
ATOM   4178 N  N   . ASP B  1 253 ? 4.619   2.637   20.256  1.00 22.34 ? 253 ASP B N   1 
ATOM   4179 C  CA  . ASP B  1 253 ? 4.521   3.612   21.328  1.00 22.71 ? 253 ASP B CA  1 
ATOM   4180 C  C   . ASP B  1 253 ? 3.902   3.052   22.651  1.00 25.02 ? 253 ASP B C   1 
ATOM   4181 O  O   . ASP B  1 253 ? 3.146   3.743   23.255  1.00 26.00 ? 253 ASP B O   1 
ATOM   4182 C  CB  . ASP B  1 253 ? 3.733   4.832   20.853  1.00 26.66 ? 253 ASP B CB  1 
ATOM   4183 C  CG  . ASP B  1 253 ? 4.340   5.520   19.611  1.00 34.70 ? 253 ASP B CG  1 
ATOM   4184 O  OD1 . ASP B  1 253 ? 5.532   5.396   19.373  1.00 31.85 ? 253 ASP B OD1 1 
ATOM   4185 O  OD2 . ASP B  1 253 ? 3.585   6.190   18.894  1.00 30.53 ? 253 ASP B OD2 1 
ATOM   4186 N  N   . GLU B  1 254 ? 4.248   1.814   23.042  1.00 22.41 ? 254 GLU B N   1 
ATOM   4187 C  CA  . GLU B  1 254 ? 3.790   1.166   24.300  1.00 26.11 ? 254 GLU B CA  1 
ATOM   4188 C  C   . GLU B  1 254 ? 2.312   0.645   24.248  1.00 24.63 ? 254 GLU B C   1 
ATOM   4189 O  O   . GLU B  1 254 ? 1.837   -0.010  25.197  1.00 24.81 ? 254 GLU B O   1 
ATOM   4190 C  CB  . GLU B  1 254 ? 4.047   2.067   25.554  1.00 27.63 ? 254 GLU B CB  1 
ATOM   4191 C  CG  . GLU B  1 254 ? 5.510   2.531   25.660  1.00 35.64 ? 254 GLU B CG  1 
ATOM   4192 C  CD  . GLU B  1 254 ? 5.676   3.748   26.582  1.00 50.36 ? 254 GLU B CD  1 
ATOM   4193 O  OE1 . GLU B  1 254 ? 5.610   4.913   26.084  1.00 56.40 ? 254 GLU B OE1 1 
ATOM   4194 O  OE2 . GLU B  1 254 ? 5.841   3.545   27.817  1.00 57.84 ? 254 GLU B OE2 1 
ATOM   4195 N  N   . ARG B  1 255 ? 1.617   0.849   23.136  1.00 21.51 ? 255 ARG B N   1 
ATOM   4196 C  CA  . ARG B  1 255 ? 0.237   0.296   23.059  1.00 19.98 ? 255 ARG B CA  1 
ATOM   4197 C  C   . ARG B  1 255 ? 0.195   -1.304  23.081  1.00 22.39 ? 255 ARG B C   1 
ATOM   4198 O  O   . ARG B  1 255 ? 1.115   -1.987  22.616  1.00 23.12 ? 255 ARG B O   1 
ATOM   4199 C  CB  . ARG B  1 255 ? -0.370  0.868   21.719  1.00 19.91 ? 255 ARG B CB  1 
ATOM   4200 C  CG  . ARG B  1 255 ? -0.787  2.360   21.666  1.00 23.35 ? 255 ARG B CG  1 
ATOM   4201 C  CD  . ARG B  1 255 ? -1.208  2.817   20.208  1.00 17.55 ? 255 ARG B CD  1 
ATOM   4202 N  NE  . ARG B  1 255 ? -0.101  2.868   19.252  1.00 21.68 ? 255 ARG B NE  1 
ATOM   4203 C  CZ  . ARG B  1 255 ? -0.250  3.065   17.943  1.00 20.79 ? 255 ARG B CZ  1 
ATOM   4204 N  NH1 . ARG B  1 255 ? -1.462  3.235   17.427  1.00 14.81 ? 255 ARG B NH1 1 
ATOM   4205 N  NH2 . ARG B  1 255 ? 0.810   3.094   17.146  1.00 16.36 ? 255 ARG B NH2 1 
ATOM   4206 N  N   . LEU B  1 256 ? -0.894  -1.899  23.601  1.00 18.82 ? 256 LEU B N   1 
ATOM   4207 C  CA  . LEU B  1 256 ? -1.268  -3.265  23.303  1.00 18.00 ? 256 LEU B CA  1 
ATOM   4208 C  C   . LEU B  1 256 ? -2.500  -3.189  22.335  1.00 16.09 ? 256 LEU B C   1 
ATOM   4209 O  O   . LEU B  1 256 ? -3.185  -2.150  22.216  1.00 16.42 ? 256 LEU B O   1 
ATOM   4210 C  CB  . LEU B  1 256 ? -1.715  -3.981  24.576  1.00 21.24 ? 256 LEU B CB  1 
ATOM   4211 C  CG  . LEU B  1 256 ? -0.729  -3.990  25.747  1.00 25.74 ? 256 LEU B CG  1 
ATOM   4212 C  CD1 . LEU B  1 256 ? -1.368  -4.916  26.781  1.00 26.38 ? 256 LEU B CD1 1 
ATOM   4213 C  CD2 . LEU B  1 256 ? 0.610   -4.506  25.226  1.00 26.19 ? 256 LEU B CD2 1 
ATOM   4214 N  N   . VAL B  1 257 ? -2.733  -4.303  21.675  1.00 12.87 ? 257 VAL B N   1 
ATOM   4215 C  CA  . VAL B  1 257 ? -3.871  -4.539  20.846  1.00 12.28 ? 257 VAL B CA  1 
ATOM   4216 C  C   . VAL B  1 257 ? -4.677  -5.572  21.592  1.00 12.50 ? 257 VAL B C   1 
ATOM   4217 O  O   . VAL B  1 257 ? -4.170  -6.687  21.947  1.00 12.59 ? 257 VAL B O   1 
ATOM   4218 C  CB  . VAL B  1 257 ? -3.465  -5.061  19.467  1.00 12.38 ? 257 VAL B CB  1 
ATOM   4219 C  CG1 . VAL B  1 257 ? -4.644  -5.494  18.642  1.00 12.29 ? 257 VAL B CG1 1 
ATOM   4220 C  CG2 . VAL B  1 257 ? -2.628  -4.010  18.746  1.00 12.77 ? 257 VAL B CG2 1 
ATOM   4221 N  N   . TYR B  1 258 ? -5.940  -5.263  21.792  1.00 10.81 ? 258 TYR B N   1 
ATOM   4222 C  CA  . TYR B  1 258 ? -6.838  -6.184  22.526  1.00 11.69 ? 258 TYR B CA  1 
ATOM   4223 C  C   . TYR B  1 258 ? -7.650  -7.087  21.594  1.00 10.95 ? 258 TYR B C   1 
ATOM   4224 O  O   . TYR B  1 258 ? -8.072  -6.649  20.489  1.00 12.49 ? 258 TYR B O   1 
ATOM   4225 C  CB  . TYR B  1 258 ? -7.746  -5.267  23.396  1.00 13.79 ? 258 TYR B CB  1 
ATOM   4226 C  CG  . TYR B  1 258 ? -6.949  -4.412  24.297  1.00 16.88 ? 258 TYR B CG  1 
ATOM   4227 C  CD1 . TYR B  1 258 ? -6.389  -4.980  25.480  1.00 16.80 ? 258 TYR B CD1 1 
ATOM   4228 C  CD2 . TYR B  1 258 ? -6.572  -3.096  23.922  1.00 16.00 ? 258 TYR B CD2 1 
ATOM   4229 C  CE1 . TYR B  1 258 ? -5.586  -4.231  26.292  1.00 19.09 ? 258 TYR B CE1 1 
ATOM   4230 C  CE2 . TYR B  1 258 ? -5.750  -2.326  24.723  1.00 18.26 ? 258 TYR B CE2 1 
ATOM   4231 C  CZ  . TYR B  1 258 ? -5.256  -2.912  25.912  1.00 19.88 ? 258 TYR B CZ  1 
ATOM   4232 O  OH  . TYR B  1 258 ? -4.464  -2.065  26.644  1.00 23.53 ? 258 TYR B OH  1 
ATOM   4233 N  N   . THR B  1 259 ? -7.830  -8.371  21.895  1.00 10.69 ? 259 THR B N   1 
ATOM   4234 C  CA  . THR B  1 259 ? -8.473  -9.286  21.000  1.00 11.79 ? 259 THR B CA  1 
ATOM   4235 C  C   . THR B  1 259 ? -9.773  -9.807  21.635  1.00 11.78 ? 259 THR B C   1 
ATOM   4236 O  O   . THR B  1 259 ? -9.839  -10.067 22.873  1.00 12.67 ? 259 THR B O   1 
ATOM   4237 C  CB  . THR B  1 259 ? -7.606  -10.465 20.571  1.00 12.56 ? 259 THR B CB  1 
ATOM   4238 O  OG1 . THR B  1 259 ? -7.115  -11.167 21.759  1.00 14.64 ? 259 THR B OG1 1 
ATOM   4239 C  CG2 . THR B  1 259 ? -6.314  -9.936  19.819  1.00 11.75 ? 259 THR B CG2 1 
ATOM   4240 N  N   . SER B  1 260 ? -10.774 -9.986  20.813  1.00 10.18 ? 260 SER B N   1 
ATOM   4241 C  CA  . SER B  1 260 ? -12.079 -10.531 21.365  1.00 10.59 ? 260 SER B CA  1 
ATOM   4242 C  C   . SER B  1 260 ? -12.028 -12.047 21.346  1.00 13.57 ? 260 SER B C   1 
ATOM   4243 O  O   . SER B  1 260 ? -13.041 -12.699 21.694  1.00 14.78 ? 260 SER B O   1 
ATOM   4244 C  CB  . SER B  1 260 ? -13.206 -10.033 20.413  1.00 10.61 ? 260 SER B CB  1 
ATOM   4245 O  OG  . SER B  1 260 ? -13.097 -10.615 19.188  1.00 11.29 ? 260 SER B OG  1 
ATOM   4246 N  N   . PHE B  1 261 ? -10.930 -12.634 20.857  1.00 12.20 ? 261 PHE B N   1 
ATOM   4247 C  CA  . PHE B  1 261 ? -10.733 -14.089 20.747  1.00 13.10 ? 261 PHE B CA  1 
ATOM   4248 C  C   . PHE B  1 261 ? -9.502  -14.390 21.569  1.00 14.89 ? 261 PHE B C   1 
ATOM   4249 O  O   . PHE B  1 261 ? -8.550  -13.645 21.704  1.00 13.72 ? 261 PHE B O   1 
ATOM   4250 C  CB  . PHE B  1 261 ? -10.537 -14.521 19.292  1.00 12.22 ? 261 PHE B CB  1 
ATOM   4251 C  CG  . PHE B  1 261 ? -9.489  -13.754 18.561  1.00 13.45 ? 261 PHE B CG  1 
ATOM   4252 C  CD1 . PHE B  1 261 ? -9.815  -12.548 17.973  1.00 12.85 ? 261 PHE B CD1 1 
ATOM   4253 C  CD2 . PHE B  1 261 ? -8.226  -14.275 18.372  1.00 15.61 ? 261 PHE B CD2 1 
ATOM   4254 C  CE1 . PHE B  1 261 ? -8.832  -11.852 17.257  1.00 14.89 ? 261 PHE B CE1 1 
ATOM   4255 C  CE2 . PHE B  1 261 ? -7.250  -13.578 17.685  1.00 16.00 ? 261 PHE B CE2 1 
ATOM   4256 C  CZ  . PHE B  1 261 ? -7.566  -12.336 17.121  1.00 15.48 ? 261 PHE B CZ  1 
ATOM   4257 N  N   . SER B  1 262 ? -9.582  -15.515 22.280  1.00 16.47 ? 262 SER B N   1 
ATOM   4258 C  CA  . SER B  1 262 ? -8.492  -15.795 23.174  1.00 20.06 ? 262 SER B CA  1 
ATOM   4259 C  C   . SER B  1 262 ? -7.495  -16.675 22.504  1.00 22.75 ? 262 SER B C   1 
ATOM   4260 O  O   . SER B  1 262 ? -6.462  -16.914 23.087  1.00 26.29 ? 262 SER B O   1 
ATOM   4261 C  CB  . SER B  1 262 ? -8.945  -16.450 24.465  1.00 25.46 ? 262 SER B CB  1 
ATOM   4262 O  OG  . SER B  1 262 ? -9.516  -17.712 24.149  1.00 29.12 ? 262 SER B OG  1 
ATOM   4263 N  N   . GLN B  1 263 ? -7.848  -17.297 21.384  1.00 26.76 ? 263 GLN B N   1 
ATOM   4264 C  CA  . GLN B  1 263 ? -6.997  -18.281 20.685  1.00 28.02 ? 263 GLN B CA  1 
ATOM   4265 C  C   . GLN B  1 263 ? -7.625  -18.456 19.324  1.00 24.94 ? 263 GLN B C   1 
ATOM   4266 O  O   . GLN B  1 263 ? -6.964  -19.031 18.409  1.00 24.23 ? 263 GLN B O   1 
ATOM   4267 C  CB  . GLN B  1 263 ? -6.816  -19.663 21.406  1.00 28.53 ? 263 GLN B CB  1 
ATOM   4268 C  CG  . GLN B  1 263 ? -8.088  -20.457 21.698  1.00 33.67 ? 263 GLN B CG  1 
ATOM   4269 C  CD  . GLN B  1 263 ? -7.794  -21.801 22.352  1.00 33.99 ? 263 GLN B CD  1 
ATOM   4270 O  OE1 . GLN B  1 263 ? -7.232  -22.720 21.723  1.00 29.91 ? 263 GLN B OE1 1 
ATOM   4271 N  NE2 . GLN B  1 263 ? -8.211  -21.946 23.595  1.00 33.37 ? 263 GLN B NE2 1 
ATOM   4272 O  OXT . GLN B  1 263 ? -8.767  -17.972 19.207  1.00 20.27 ? 263 GLN B OXT 1 
ATOM   4273 N  N   . LYS C  1 3   ? 33.888  17.664  -25.438 1.00 39.67 ? 3   LYS C N   1 
ATOM   4274 C  CA  . LYS C  1 3   ? 32.752  17.386  -24.499 1.00 39.16 ? 3   LYS C CA  1 
ATOM   4275 C  C   . LYS C  1 3   ? 31.696  16.441  -25.135 1.00 38.88 ? 3   LYS C C   1 
ATOM   4276 O  O   . LYS C  1 3   ? 30.564  16.294  -24.625 1.00 41.67 ? 3   LYS C O   1 
ATOM   4277 C  CB  . LYS C  1 3   ? 32.091  18.679  -24.014 1.00 47.33 ? 3   LYS C CB  1 
ATOM   4278 C  CG  . LYS C  1 3   ? 30.997  19.184  -24.940 1.00 50.89 ? 3   LYS C CG  1 
ATOM   4279 C  CD  . LYS C  1 3   ? 30.229  20.350  -24.356 1.00 63.62 ? 3   LYS C CD  1 
ATOM   4280 C  CE  . LYS C  1 3   ? 30.740  21.684  -24.873 1.00 65.69 ? 3   LYS C CE  1 
ATOM   4281 N  NZ  . LYS C  1 3   ? 29.607  22.646  -24.838 1.00 63.19 ? 3   LYS C NZ  1 
ATOM   4282 N  N   . TRP C  1 4   ? 32.065  15.771  -26.225 1.00 25.28 ? 4   TRP C N   1 
ATOM   4283 C  CA  . TRP C  1 4   ? 31.091  14.839  -26.799 1.00 21.27 ? 4   TRP C CA  1 
ATOM   4284 C  C   . TRP C  1 4   ? 30.955  13.659  -25.842 1.00 20.03 ? 4   TRP C C   1 
ATOM   4285 O  O   . TRP C  1 4   ? 31.865  13.327  -25.022 1.00 20.18 ? 4   TRP C O   1 
ATOM   4286 C  CB  . TRP C  1 4   ? 31.511  14.466  -28.247 1.00 17.24 ? 4   TRP C CB  1 
ATOM   4287 C  CG  . TRP C  1 4   ? 32.858  13.809  -28.318 1.00 15.96 ? 4   TRP C CG  1 
ATOM   4288 C  CD1 . TRP C  1 4   ? 34.108  14.351  -28.542 1.00 14.63 ? 4   TRP C CD1 1 
ATOM   4289 C  CD2 . TRP C  1 4   ? 33.147  12.365  -28.149 1.00 13.12 ? 4   TRP C CD2 1 
ATOM   4290 N  NE1 . TRP C  1 4   ? 35.105  13.403  -28.514 1.00 16.38 ? 4   TRP C NE1 1 
ATOM   4291 C  CE2 . TRP C  1 4   ? 34.588  12.169  -28.306 1.00 15.50 ? 4   TRP C CE2 1 
ATOM   4292 C  CE3 . TRP C  1 4   ? 32.320  11.210  -27.936 1.00 14.13 ? 4   TRP C CE3 1 
ATOM   4293 C  CZ2 . TRP C  1 4   ? 35.192  10.898  -28.250 1.00 15.21 ? 4   TRP C CZ2 1 
ATOM   4294 C  CZ3 . TRP C  1 4   ? 32.943  9.955   -27.835 1.00 13.55 ? 4   TRP C CZ3 1 
ATOM   4295 C  CH2 . TRP C  1 4   ? 34.331  9.786   -27.979 1.00 15.92 ? 4   TRP C CH2 1 
ATOM   4296 N  N   . THR C  1 5   ? 29.801  13.002  -25.912 1.00 17.87 ? 5   THR C N   1 
ATOM   4297 C  CA  . THR C  1 5   ? 29.501  11.905  -25.005 1.00 18.09 ? 5   THR C CA  1 
ATOM   4298 C  C   . THR C  1 5   ? 28.730  10.797  -25.741 1.00 17.18 ? 5   THR C C   1 
ATOM   4299 O  O   . THR C  1 5   ? 28.499  10.835  -26.995 1.00 16.28 ? 5   THR C O   1 
ATOM   4300 C  CB  . THR C  1 5   ? 28.556  12.352  -23.847 1.00 21.24 ? 5   THR C CB  1 
ATOM   4301 O  OG1 . THR C  1 5   ? 27.298  12.671  -24.418 1.00 23.19 ? 5   THR C OG1 1 
ATOM   4302 C  CG2 . THR C  1 5   ? 29.140  13.625  -23.107 1.00 23.07 ? 5   THR C CG2 1 
ATOM   4303 N  N   . TYR C  1 6   ? 28.261  9.799   -24.995 1.00 18.65 ? 6   TYR C N   1 
ATOM   4304 C  CA  . TYR C  1 6   ? 27.398  8.726   -25.549 1.00 18.43 ? 6   TYR C CA  1 
ATOM   4305 C  C   . TYR C  1 6   ? 25.969  8.793   -24.981 1.00 20.65 ? 6   TYR C C   1 
ATOM   4306 O  O   . TYR C  1 6   ? 25.189  7.842   -25.094 1.00 22.18 ? 6   TYR C O   1 
ATOM   4307 C  CB  . TYR C  1 6   ? 27.966  7.323   -25.379 1.00 16.28 ? 6   TYR C CB  1 
ATOM   4308 C  CG  . TYR C  1 6   ? 29.260  7.068   -26.136 1.00 17.56 ? 6   TYR C CG  1 
ATOM   4309 C  CD1 . TYR C  1 6   ? 30.536  7.298   -25.538 1.00 16.27 ? 6   TYR C CD1 1 
ATOM   4310 C  CD2 . TYR C  1 6   ? 29.233  6.487   -27.401 1.00 15.30 ? 6   TYR C CD2 1 
ATOM   4311 C  CE1 . TYR C  1 6   ? 31.745  7.049   -26.179 1.00 15.47 ? 6   TYR C CE1 1 
ATOM   4312 C  CE2 . TYR C  1 6   ? 30.415  6.253   -28.078 1.00 14.66 ? 6   TYR C CE2 1 
ATOM   4313 C  CZ  . TYR C  1 6   ? 31.649  6.482   -27.501 1.00 13.74 ? 6   TYR C CZ  1 
ATOM   4314 O  OH  . TYR C  1 6   ? 32.789  6.139   -28.196 1.00 14.65 ? 6   TYR C OH  1 
ATOM   4315 N  N   A PHE C  1 7   ? 25.416  10.001  -24.664 0.50 20.21 ? 7   PHE C N   1 
ATOM   4316 N  N   B PHE C  1 7   ? 25.580  9.881   -24.261 0.50 24.49 ? 7   PHE C N   1 
ATOM   4317 C  CA  A PHE C  1 7   ? 24.006  10.154  -24.238 0.50 23.53 ? 7   PHE C CA  1 
ATOM   4318 C  CA  B PHE C  1 7   ? 24.312  10.024  -23.468 0.50 28.76 ? 7   PHE C CA  1 
ATOM   4319 C  C   A PHE C  1 7   ? 23.635  11.609  -24.214 0.50 25.20 ? 7   PHE C C   1 
ATOM   4320 C  C   B PHE C  1 7   ? 23.898  11.514  -23.282 0.50 29.46 ? 7   PHE C C   1 
ATOM   4321 O  O   A PHE C  1 7   ? 24.327  12.430  -24.777 0.50 20.83 ? 7   PHE C O   1 
ATOM   4322 O  O   B PHE C  1 7   ? 24.770  12.357  -23.068 0.50 32.38 ? 7   PHE C O   1 
ATOM   4323 C  CB  A PHE C  1 7   ? 23.855  9.752   -22.783 0.50 22.07 ? 7   PHE C CB  1 
ATOM   4324 C  CB  B PHE C  1 7   ? 24.428  9.331   -22.065 0.50 29.75 ? 7   PHE C CB  1 
ATOM   4325 C  CG  A PHE C  1 7   ? 24.708  10.593  -21.860 0.50 22.33 ? 7   PHE C CG  1 
ATOM   4326 C  CG  B PHE C  1 7   ? 23.146  9.376   -21.241 0.50 30.90 ? 7   PHE C CG  1 
ATOM   4327 C  CD1 A PHE C  1 7   ? 24.190  11.784  -21.329 0.50 21.14 ? 7   PHE C CD1 1 
ATOM   4328 C  CD1 B PHE C  1 7   ? 22.145  8.449   -21.430 0.50 31.67 ? 7   PHE C CD1 1 
ATOM   4329 C  CD2 A PHE C  1 7   ? 26.007  10.231  -21.571 0.50 22.23 ? 7   PHE C CD2 1 
ATOM   4330 C  CD2 B PHE C  1 7   ? 22.946  10.370  -20.287 0.50 31.56 ? 7   PHE C CD2 1 
ATOM   4331 C  CE1 A PHE C  1 7   ? 24.946  12.594  -20.499 0.50 19.95 ? 7   PHE C CE1 1 
ATOM   4332 C  CE1 B PHE C  1 7   ? 20.988  8.503   -20.684 0.50 29.31 ? 7   PHE C CE1 1 
ATOM   4333 C  CE2 A PHE C  1 7   ? 26.779  11.040  -20.729 0.50 21.09 ? 7   PHE C CE2 1 
ATOM   4334 C  CE2 B PHE C  1 7   ? 21.774  10.427  -19.550 0.50 32.62 ? 7   PHE C CE2 1 
ATOM   4335 C  CZ  A PHE C  1 7   ? 26.256  12.228  -20.231 0.50 19.69 ? 7   PHE C CZ  1 
ATOM   4336 C  CZ  B PHE C  1 7   ? 20.803  9.485   -19.746 0.50 30.17 ? 7   PHE C CZ  1 
ATOM   4337 N  N   . GLY C  1 8   ? 22.542  11.896  -23.375 1.00 30.81 ? 8   GLY C N   1 
ATOM   4338 C  CA  . GLY C  1 8   ? 22.179  13.273  -23.078 1.00 26.39 ? 8   GLY C CA  1 
ATOM   4339 C  C   . GLY C  1 8   ? 22.005  14.035  -24.373 1.00 28.84 ? 8   GLY C C   1 
ATOM   4340 O  O   . GLY C  1 8   ? 21.587  13.406  -25.425 1.00 35.00 ? 8   GLY C O   1 
ATOM   4341 N  N   . PRO C  1 9   ? 22.334  15.348  -24.412 1.00 26.09 ? 9   PRO C N   1 
ATOM   4342 C  CA  . PRO C  1 9   ? 22.279  16.087  -25.696 1.00 23.58 ? 9   PRO C CA  1 
ATOM   4343 C  C   . PRO C  1 9   ? 23.598  16.168  -26.430 1.00 21.27 ? 9   PRO C C   1 
ATOM   4344 O  O   . PRO C  1 9   ? 23.621  16.771  -27.493 1.00 20.63 ? 9   PRO C O   1 
ATOM   4345 C  CB  . PRO C  1 9   ? 21.864  17.563  -25.268 1.00 25.70 ? 9   PRO C CB  1 
ATOM   4346 C  CG  . PRO C  1 9   ? 22.476  17.641  -23.887 1.00 23.11 ? 9   PRO C CG  1 
ATOM   4347 C  CD  . PRO C  1 9   ? 22.292  16.284  -23.240 1.00 26.77 ? 9   PRO C CD  1 
ATOM   4348 N  N   . ASP C  1 10  ? 24.693  15.655  -25.852 1.00 21.02 ? 10  ASP C N   1 
ATOM   4349 C  CA  . ASP C  1 10  ? 26.009  15.718  -26.560 1.00 20.29 ? 10  ASP C CA  1 
ATOM   4350 C  C   . ASP C  1 10  ? 26.417  14.364  -27.116 1.00 17.75 ? 10  ASP C C   1 
ATOM   4351 O  O   . ASP C  1 10  ? 27.596  14.186  -27.483 1.00 18.36 ? 10  ASP C O   1 
ATOM   4352 C  CB  . ASP C  1 10  ? 27.121  16.268  -25.642 1.00 22.39 ? 10  ASP C CB  1 
ATOM   4353 C  CG  . ASP C  1 10  ? 26.890  17.755  -25.295 1.00 29.03 ? 10  ASP C CG  1 
ATOM   4354 O  OD1 . ASP C  1 10  ? 26.507  18.522  -26.221 1.00 30.73 ? 10  ASP C OD1 1 
ATOM   4355 O  OD2 . ASP C  1 10  ? 27.045  18.103  -24.094 1.00 29.86 ? 10  ASP C OD2 1 
ATOM   4356 N  N   . GLY C  1 11  ? 25.410  13.505  -27.244 1.00 22.16 ? 11  GLY C N   1 
ATOM   4357 C  CA  . GLY C  1 11  ? 25.578  12.060  -27.597 1.00 15.62 ? 11  GLY C CA  1 
ATOM   4358 C  C   . GLY C  1 11  ? 25.647  11.920  -29.126 1.00 11.83 ? 11  GLY C C   1 
ATOM   4359 O  O   . GLY C  1 11  ? 25.694  12.904  -29.877 1.00 11.88 ? 11  GLY C O   1 
ATOM   4360 N  N   . GLU C  1 12  ? 25.678  10.636  -29.551 1.00 11.36 ? 12  GLU C N   1 
ATOM   4361 C  CA  . GLU C  1 12  ? 26.116  10.388  -30.920 1.00 10.11 ? 12  GLU C CA  1 
ATOM   4362 C  C   . GLU C  1 12  ? 25.247  11.059  -32.006 1.00 11.42 ? 12  GLU C C   1 
ATOM   4363 O  O   . GLU C  1 12  ? 25.768  11.322  -33.109 1.00 9.80  ? 12  GLU C O   1 
ATOM   4364 C  CB  . GLU C  1 12  ? 26.277  8.888   -31.206 1.00 9.72  ? 12  GLU C CB  1 
ATOM   4365 C  CG  . GLU C  1 12  ? 24.930  8.152   -31.308 1.00 9.75  ? 12  GLU C CG  1 
ATOM   4366 C  CD  . GLU C  1 12  ? 25.153  6.683   -31.038 1.00 8.91  ? 12  GLU C CD  1 
ATOM   4367 O  OE1 . GLU C  1 12  ? 25.472  5.901   -31.958 1.00 9.49  ? 12  GLU C OE1 1 
ATOM   4368 O  OE2 . GLU C  1 12  ? 25.135  6.277   -29.832 1.00 11.70 ? 12  GLU C OE2 1 
ATOM   4369 N  N   . ASN C  1 13  ? 23.938  11.221  -31.778 1.00 9.47  ? 13  ASN C N   1 
ATOM   4370 C  CA  . ASN C  1 13  ? 23.153  11.835  -32.850 1.00 10.13 ? 13  ASN C CA  1 
ATOM   4371 C  C   . ASN C  1 13  ? 23.475  13.306  -33.044 1.00 9.49  ? 13  ASN C C   1 
ATOM   4372 O  O   . ASN C  1 13  ? 23.120  13.851  -34.047 1.00 10.42 ? 13  ASN C O   1 
ATOM   4373 C  CB  . ASN C  1 13  ? 21.626  11.684  -32.574 1.00 10.17 ? 13  ASN C CB  1 
ATOM   4374 C  CG  . ASN C  1 13  ? 21.162  10.231  -32.667 1.00 11.44 ? 13  ASN C CG  1 
ATOM   4375 O  OD1 . ASN C  1 13  ? 21.842  9.328   -33.265 1.00 11.03 ? 13  ASN C OD1 1 
ATOM   4376 N  ND2 . ASN C  1 13  ? 19.993  10.001  -32.141 1.00 10.38 ? 13  ASN C ND2 1 
ATOM   4377 N  N   A SER C  1 14  ? 24.114  13.904  -32.025 0.50 9.43  ? 14  SER C N   1 
ATOM   4378 N  N   B SER C  1 14  ? 24.107  13.969  -32.072 0.50 10.29 ? 14  SER C N   1 
ATOM   4379 C  CA  A SER C  1 14  ? 24.492  15.301  -32.057 0.50 9.84  ? 14  SER C CA  1 
ATOM   4380 C  CA  B SER C  1 14  ? 24.463  15.375  -32.264 0.50 11.26 ? 14  SER C CA  1 
ATOM   4381 C  C   A SER C  1 14  ? 25.919  15.537  -32.543 0.50 10.28 ? 14  SER C C   1 
ATOM   4382 C  C   B SER C  1 14  ? 25.987  15.554  -32.440 0.50 11.57 ? 14  SER C C   1 
ATOM   4383 O  O   A SER C  1 14  ? 26.243  16.683  -32.903 0.50 8.56  ? 14  SER C O   1 
ATOM   4384 O  O   B SER C  1 14  ? 26.476  16.668  -32.440 0.50 11.09 ? 14  SER C O   1 
ATOM   4385 C  CB  A SER C  1 14  ? 24.305  15.974  -30.669 0.50 10.02 ? 14  SER C CB  1 
ATOM   4386 C  CB  B SER C  1 14  ? 24.087  16.181  -31.021 0.50 13.18 ? 14  SER C CB  1 
ATOM   4387 O  OG  A SER C  1 14  ? 22.923  16.053  -30.425 0.50 9.40  ? 14  SER C OG  1 
ATOM   4388 O  OG  B SER C  1 14  ? 24.807  15.629  -29.958 0.50 14.30 ? 14  SER C OG  1 
ATOM   4389 N  N   . TRP C  1 15  ? 26.745  14.485  -32.570 1.00 9.60  ? 15  TRP C N   1 
ATOM   4390 C  CA  . TRP C  1 15  ? 28.145  14.664  -32.960 1.00 10.09 ? 15  TRP C CA  1 
ATOM   4391 C  C   . TRP C  1 15  ? 28.319  15.465  -34.227 1.00 9.89  ? 15  TRP C C   1 
ATOM   4392 O  O   . TRP C  1 15  ? 29.276  16.272  -34.317 1.00 10.48 ? 15  TRP C O   1 
ATOM   4393 C  CB  . TRP C  1 15  ? 28.880  13.329  -33.190 1.00 8.89  ? 15  TRP C CB  1 
ATOM   4394 C  CG  . TRP C  1 15  ? 29.041  12.492  -31.946 1.00 8.64  ? 15  TRP C CG  1 
ATOM   4395 C  CD1 . TRP C  1 15  ? 28.801  12.848  -30.618 1.00 9.69  ? 15  TRP C CD1 1 
ATOM   4396 C  CD2 . TRP C  1 15  ? 29.495  11.110  -31.894 1.00 9.05  ? 15  TRP C CD2 1 
ATOM   4397 N  NE1 . TRP C  1 15  ? 29.071  11.789  -29.780 1.00 9.52  ? 15  TRP C NE1 1 
ATOM   4398 C  CE2 . TRP C  1 15  ? 29.495  10.718  -30.490 1.00 9.82  ? 15  TRP C CE2 1 
ATOM   4399 C  CE3 . TRP C  1 15  ? 29.896  10.196  -32.844 1.00 8.82  ? 15  TRP C CE3 1 
ATOM   4400 C  CZ2 . TRP C  1 15  ? 29.886  9.455   -30.087 1.00 9.57  ? 15  TRP C CZ2 1 
ATOM   4401 C  CZ3 . TRP C  1 15  ? 30.285  8.922   -32.429 1.00 8.45  ? 15  TRP C CZ3 1 
ATOM   4402 C  CH2 . TRP C  1 15  ? 30.276  8.561   -31.078 1.00 9.67  ? 15  TRP C CH2 1 
ATOM   4403 N  N   . SER C  1 16  ? 27.461  15.266  -35.248 1.00 9.75  ? 16  SER C N   1 
ATOM   4404 C  CA  . SER C  1 16  ? 27.652  15.929  -36.540 1.00 9.35  ? 16  SER C CA  1 
ATOM   4405 C  C   . SER C  1 16  ? 27.565  17.448  -36.415 1.00 10.69 ? 16  SER C C   1 
ATOM   4406 O  O   . SER C  1 16  ? 27.962  18.123  -37.367 1.00 10.83 ? 16  SER C O   1 
ATOM   4407 C  CB  . SER C  1 16  ? 26.596  15.450  -37.537 1.00 10.30 ? 16  SER C CB  1 
ATOM   4408 O  OG  . SER C  1 16  ? 25.292  15.832  -37.038 1.00 11.51 ? 16  SER C OG  1 
ATOM   4409 N  N   A LYS C  1 17  ? 26.980  17.985  -35.351 0.50 10.05 ? 17  LYS C N   1 
ATOM   4410 N  N   B LYS C  1 17  ? 27.058  17.950  -35.298 0.50 10.79 ? 17  LYS C N   1 
ATOM   4411 C  CA  A LYS C  1 17  ? 26.969  19.483  -35.180 0.50 10.20 ? 17  LYS C CA  1 
ATOM   4412 C  CA  B LYS C  1 17  ? 26.933  19.422  -35.190 0.50 11.75 ? 17  LYS C CA  1 
ATOM   4413 C  C   A LYS C  1 17  ? 28.455  19.991  -35.213 0.50 9.89  ? 17  LYS C C   1 
ATOM   4414 C  C   B LYS C  1 17  ? 28.294  20.087  -35.029 0.50 11.80 ? 17  LYS C C   1 
ATOM   4415 O  O   A LYS C  1 17  ? 28.895  20.831  -36.076 0.50 9.23  ? 17  LYS C O   1 
ATOM   4416 O  O   B LYS C  1 17  ? 28.410  21.204  -35.517 0.50 13.23 ? 17  LYS C O   1 
ATOM   4417 C  CB  A LYS C  1 17  ? 26.239  19.845  -33.836 0.50 9.56  ? 17  LYS C CB  1 
ATOM   4418 C  CB  B LYS C  1 17  ? 25.995  19.836  -34.055 0.50 11.48 ? 17  LYS C CB  1 
ATOM   4419 C  CG  A LYS C  1 17  ? 24.764  19.362  -33.742 0.50 10.42 ? 17  LYS C CG  1 
ATOM   4420 C  CG  B LYS C  1 17  ? 24.524  19.673  -34.422 0.50 11.79 ? 17  LYS C CG  1 
ATOM   4421 C  CD  A LYS C  1 17  ? 24.066  19.801  -32.426 0.50 10.70 ? 17  LYS C CD  1 
ATOM   4422 C  CD  B LYS C  1 17  ? 23.610  19.987  -33.255 0.50 13.06 ? 17  LYS C CD  1 
ATOM   4423 C  CE  A LYS C  1 17  ? 22.782  19.033  -32.119 0.50 12.07 ? 17  LYS C CE  1 
ATOM   4424 C  CE  B LYS C  1 17  ? 23.747  21.472  -32.925 0.50 14.51 ? 17  LYS C CE  1 
ATOM   4425 N  NZ  A LYS C  1 17  ? 22.379  19.239  -30.700 0.50 13.69 ? 17  LYS C NZ  1 
ATOM   4426 N  NZ  B LYS C  1 17  ? 23.198  21.592  -31.557 0.50 16.07 ? 17  LYS C NZ  1 
ATOM   4427 N  N   . LYS C  1 18  ? 29.252  19.490  -34.296 1.00 11.77 ? 18  LYS C N   1 
ATOM   4428 C  CA  . LYS C  1 18  ? 30.657  19.980  -34.172 1.00 12.11 ? 18  LYS C CA  1 
ATOM   4429 C  C   . LYS C  1 18  ? 31.613  19.245  -35.044 1.00 14.41 ? 18  LYS C C   1 
ATOM   4430 O  O   . LYS C  1 18  ? 32.699  19.747  -35.290 1.00 16.33 ? 18  LYS C O   1 
ATOM   4431 C  CB  . LYS C  1 18  ? 31.067  19.890  -32.721 1.00 15.41 ? 18  LYS C CB  1 
ATOM   4432 C  CG  . LYS C  1 18  ? 30.388  20.979  -31.870 1.00 23.64 ? 18  LYS C CG  1 
ATOM   4433 C  CD  . LYS C  1 18  ? 31.161  22.314  -31.675 1.00 29.49 ? 18  LYS C CD  1 
ATOM   4434 C  CE  . LYS C  1 18  ? 30.223  23.422  -31.189 1.00 32.70 ? 18  LYS C CE  1 
ATOM   4435 N  NZ  . LYS C  1 18  ? 28.927  23.189  -31.961 1.00 31.94 ? 18  LYS C NZ  1 
ATOM   4436 N  N   . TYR C  1 19  ? 31.263  18.030  -35.536 1.00 11.71 ? 19  TYR C N   1 
ATOM   4437 C  CA  . TYR C  1 19  ? 32.170  17.143  -36.263 1.00 10.99 ? 19  TYR C CA  1 
ATOM   4438 C  C   . TYR C  1 19  ? 31.454  16.699  -37.529 1.00 10.41 ? 19  TYR C C   1 
ATOM   4439 O  O   . TYR C  1 19  ? 30.742  15.604  -37.533 1.00 11.18 ? 19  TYR C O   1 
ATOM   4440 C  CB  . TYR C  1 19  ? 32.518  15.939  -35.354 1.00 11.05 ? 19  TYR C CB  1 
ATOM   4441 C  CG  . TYR C  1 19  ? 33.141  16.345  -34.050 1.00 12.19 ? 19  TYR C CG  1 
ATOM   4442 C  CD1 . TYR C  1 19  ? 34.528  16.621  -33.980 1.00 13.01 ? 19  TYR C CD1 1 
ATOM   4443 C  CD2 . TYR C  1 19  ? 32.390  16.404  -32.909 1.00 10.67 ? 19  TYR C CD2 1 
ATOM   4444 C  CE1 . TYR C  1 19  ? 35.141  17.016  -32.791 1.00 14.74 ? 19  TYR C CE1 1 
ATOM   4445 C  CE2 . TYR C  1 19  ? 32.986  16.713  -31.672 1.00 12.16 ? 19  TYR C CE2 1 
ATOM   4446 C  CZ  . TYR C  1 19  ? 34.342  17.083  -31.634 1.00 14.41 ? 19  TYR C CZ  1 
ATOM   4447 O  OH  . TYR C  1 19  ? 34.915  17.392  -30.343 1.00 18.74 ? 19  TYR C OH  1 
ATOM   4448 N  N   . PRO C  1 20  ? 31.503  17.495  -38.596 1.00 10.05 ? 20  PRO C N   1 
ATOM   4449 C  CA  . PRO C  1 20  ? 30.599  17.301  -39.671 1.00 10.51 ? 20  PRO C CA  1 
ATOM   4450 C  C   . PRO C  1 20  ? 30.804  15.869  -40.295 1.00 11.27 ? 20  PRO C C   1 
ATOM   4451 O  O   . PRO C  1 20  ? 29.864  15.323  -40.923 1.00 10.95 ? 20  PRO C O   1 
ATOM   4452 C  CB  . PRO C  1 20  ? 30.957  18.417  -40.716 1.00 12.17 ? 20  PRO C CB  1 
ATOM   4453 C  CG  . PRO C  1 20  ? 31.669  19.444  -39.845 1.00 14.34 ? 20  PRO C CG  1 
ATOM   4454 C  CD  . PRO C  1 20  ? 32.284  18.771  -38.684 1.00 11.85 ? 20  PRO C CD  1 
ATOM   4455 N  N   . SER C  1 21  ? 32.011  15.313  -40.200 1.00 11.10 ? 21  SER C N   1 
ATOM   4456 C  CA  . SER C  1 21  ? 32.206  14.002  -40.865 1.00 10.14 ? 21  SER C CA  1 
ATOM   4457 C  C   . SER C  1 21  ? 31.372  12.930  -40.187 1.00 10.04 ? 21  SER C C   1 
ATOM   4458 O  O   . SER C  1 21  ? 31.121  11.908  -40.835 1.00 10.47 ? 21  SER C O   1 
ATOM   4459 C  CB  . SER C  1 21  ? 33.709  13.566  -40.835 1.00 11.46 ? 21  SER C CB  1 
ATOM   4460 O  OG  . SER C  1 21  ? 34.396  14.397  -41.787 1.00 13.45 ? 21  SER C OG  1 
ATOM   4461 N  N   . CYS C  1 22  ? 30.884  13.157  -38.964 1.00 9.36  ? 22  CYS C N   1 
ATOM   4462 C  CA  . CYS C  1 22  ? 29.990  12.130  -38.341 1.00 9.69  ? 22  CYS C CA  1 
ATOM   4463 C  C   . CYS C  1 22  ? 28.652  12.014  -39.038 1.00 10.91 ? 22  CYS C C   1 
ATOM   4464 O  O   . CYS C  1 22  ? 27.954  10.999  -38.769 1.00 10.52 ? 22  CYS C O   1 
ATOM   4465 C  CB  . CYS C  1 22  ? 29.829  12.479  -36.874 1.00 9.81  ? 22  CYS C CB  1 
ATOM   4466 S  SG  . CYS C  1 22  ? 31.325  12.574  -35.874 1.00 10.61 ? 22  CYS C SG  1 
ATOM   4467 N  N   . GLY C  1 23  ? 28.268  12.962  -39.896 1.00 10.87 ? 23  GLY C N   1 
ATOM   4468 C  CA  . GLY C  1 23  ? 27.064  12.852  -40.725 1.00 10.35 ? 23  GLY C CA  1 
ATOM   4469 C  C   . GLY C  1 23  ? 27.427  12.576  -42.168 1.00 10.38 ? 23  GLY C C   1 
ATOM   4470 O  O   . GLY C  1 23  ? 26.530  12.666  -43.031 1.00 10.66 ? 23  GLY C O   1 
ATOM   4471 N  N   . GLY C  1 24  ? 28.691  12.221  -42.462 1.00 9.88  ? 24  GLY C N   1 
ATOM   4472 C  CA  . GLY C  1 24  ? 29.143  12.002  -43.839 1.00 9.99  ? 24  GLY C CA  1 
ATOM   4473 C  C   . GLY C  1 24  ? 29.172  10.569  -44.315 1.00 10.70 ? 24  GLY C C   1 
ATOM   4474 O  O   . GLY C  1 24  ? 28.462  9.743   -43.730 1.00 12.45 ? 24  GLY C O   1 
ATOM   4475 N  N   . LEU C  1 25  ? 29.965  10.301  -45.324 1.00 11.86 ? 25  LEU C N   1 
ATOM   4476 C  CA  . LEU C  1 25  ? 29.992  8.973   -45.934 1.00 12.59 ? 25  LEU C CA  1 
ATOM   4477 C  C   . LEU C  1 25  ? 30.910  8.101   -45.096 1.00 12.61 ? 25  LEU C C   1 
ATOM   4478 O  O   . LEU C  1 25  ? 31.741  8.522   -44.204 1.00 12.13 ? 25  LEU C O   1 
ATOM   4479 C  CB  . LEU C  1 25  ? 30.653  9.063   -47.324 1.00 15.48 ? 25  LEU C CB  1 
ATOM   4480 C  CG  . LEU C  1 25  ? 29.846  10.013  -48.281 1.00 18.35 ? 25  LEU C CG  1 
ATOM   4481 C  CD1 . LEU C  1 25  ? 30.515  10.047  -49.665 1.00 19.72 ? 25  LEU C CD1 1 
ATOM   4482 C  CD2 . LEU C  1 25  ? 28.406  9.545   -48.409 1.00 22.49 ? 25  LEU C CD2 1 
ATOM   4483 N  N   . LEU C  1 26  ? 30.801  6.795   -45.388 1.00 13.68 ? 26  LEU C N   1 
ATOM   4484 C  CA  . LEU C  1 26  ? 31.754  5.756   -44.969 1.00 13.21 ? 26  LEU C CA  1 
ATOM   4485 C  C   . LEU C  1 26  ? 31.770  5.604   -43.452 1.00 11.46 ? 26  LEU C C   1 
ATOM   4486 O  O   . LEU C  1 26  ? 32.820  5.190   -42.905 1.00 13.45 ? 26  LEU C O   1 
ATOM   4487 C  CB  . LEU C  1 26  ? 33.230  5.939   -45.421 1.00 15.37 ? 26  LEU C CB  1 
ATOM   4488 C  CG  . LEU C  1 26  ? 33.617  5.870   -46.886 1.00 22.03 ? 26  LEU C CG  1 
ATOM   4489 C  CD1 . LEU C  1 26  ? 35.109  5.506   -47.030 1.00 22.82 ? 26  LEU C CD1 1 
ATOM   4490 C  CD2 . LEU C  1 26  ? 32.679  5.037   -47.742 1.00 22.52 ? 26  LEU C CD2 1 
ATOM   4491 N  N   . GLN C  1 27  ? 30.639  5.835   -42.750 1.00 8.95  ? 27  GLN C N   1 
ATOM   4492 C  CA  . GLN C  1 27  ? 30.677  5.733   -41.311 1.00 8.97  ? 27  GLN C CA  1 
ATOM   4493 C  C   . GLN C  1 27  ? 30.711  4.345   -40.744 1.00 9.17  ? 27  GLN C C   1 
ATOM   4494 O  O   . GLN C  1 27  ? 30.111  3.404   -41.262 1.00 9.92  ? 27  GLN C O   1 
ATOM   4495 C  CB  . GLN C  1 27  ? 29.511  6.479   -40.704 1.00 8.25  ? 27  GLN C CB  1 
ATOM   4496 C  CG  . GLN C  1 27  ? 29.591  7.993   -41.028 1.00 8.43  ? 27  GLN C CG  1 
ATOM   4497 C  CD  . GLN C  1 27  ? 30.728  8.648   -40.308 1.00 7.61  ? 27  GLN C CD  1 
ATOM   4498 O  OE1 . GLN C  1 27  ? 30.724  8.891   -39.106 1.00 9.17  ? 27  GLN C OE1 1 
ATOM   4499 N  NE2 . GLN C  1 27  ? 31.792  8.884   -41.119 1.00 8.83  ? 27  GLN C NE2 1 
ATOM   4500 N  N   . SER C  1 28  ? 31.478  4.163   -39.684 1.00 8.19  ? 28  SER C N   1 
ATOM   4501 C  CA  . SER C  1 28  ? 31.621  2.906   -38.894 1.00 7.87  ? 28  SER C CA  1 
ATOM   4502 C  C   . SER C  1 28  ? 31.010  3.128   -37.521 1.00 8.20  ? 28  SER C C   1 
ATOM   4503 O  O   . SER C  1 28  ? 30.890  4.272   -37.047 1.00 9.03  ? 28  SER C O   1 
ATOM   4504 C  CB  . SER C  1 28  ? 33.091  2.588   -38.691 1.00 8.30  ? 28  SER C CB  1 
ATOM   4505 O  OG  . SER C  1 28  ? 33.633  2.254   -40.006 1.00 9.56  ? 28  SER C OG  1 
ATOM   4506 N  N   . PRO C  1 29  ? 30.658  2.092   -36.769 1.00 7.13  ? 29  PRO C N   1 
ATOM   4507 C  CA  . PRO C  1 29  ? 30.763  0.718   -37.118 1.00 6.67  ? 29  PRO C CA  1 
ATOM   4508 C  C   . PRO C  1 29  ? 29.554  0.219   -37.942 1.00 7.50  ? 29  PRO C C   1 
ATOM   4509 O  O   . PRO C  1 29  ? 28.614  0.994   -38.209 1.00 8.62  ? 29  PRO C O   1 
ATOM   4510 C  CB  . PRO C  1 29  ? 30.798  -0.030  -35.745 1.00 7.77  ? 29  PRO C CB  1 
ATOM   4511 C  CG  . PRO C  1 29  ? 29.786  0.827   -35.005 1.00 8.75  ? 29  PRO C CG  1 
ATOM   4512 C  CD  . PRO C  1 29  ? 30.054  2.269   -35.407 1.00 7.43  ? 29  PRO C CD  1 
ATOM   4513 N  N   . ILE C  1 30  ? 29.599  -1.046  -38.326 1.00 7.77  ? 30  ILE C N   1 
ATOM   4514 C  CA  . ILE C  1 30  ? 28.552  -1.629  -39.179 1.00 7.99  ? 30  ILE C CA  1 
ATOM   4515 C  C   . ILE C  1 30  ? 28.243  -3.051  -38.707 1.00 8.18  ? 30  ILE C C   1 
ATOM   4516 O  O   . ILE C  1 30  ? 29.019  -3.664  -37.916 1.00 8.86  ? 30  ILE C O   1 
ATOM   4517 C  CB  . ILE C  1 30  ? 29.030  -1.690  -40.660 1.00 8.01  ? 30  ILE C CB  1 
ATOM   4518 C  CG1 . ILE C  1 30  ? 30.285  -2.573  -40.817 1.00 8.82  ? 30  ILE C CG1 1 
ATOM   4519 C  CG2 . ILE C  1 30  ? 29.210  -0.236  -41.175 1.00 9.06  ? 30  ILE C CG2 1 
ATOM   4520 C  CD1 . ILE C  1 30  ? 30.608  -2.802  -42.299 1.00 10.17 ? 30  ILE C CD1 1 
ATOM   4521 N  N   . ASP C  1 31  ? 27.099  -3.573  -39.166 1.00 9.85  ? 31  ASP C N   1 
ATOM   4522 C  CA  . ASP C  1 31  ? 26.794  -4.986  -38.975 1.00 9.65  ? 31  ASP C CA  1 
ATOM   4523 C  C   . ASP C  1 31  ? 27.430  -5.799  -40.058 1.00 8.97  ? 31  ASP C C   1 
ATOM   4524 O  O   . ASP C  1 31  ? 27.272  -5.530  -41.277 1.00 10.90 ? 31  ASP C O   1 
ATOM   4525 C  CB  . ASP C  1 31  ? 25.284  -5.193  -39.136 1.00 10.16 ? 31  ASP C CB  1 
ATOM   4526 C  CG  . ASP C  1 31  ? 24.857  -6.636  -38.839 1.00 11.06 ? 31  ASP C CG  1 
ATOM   4527 O  OD1 . ASP C  1 31  ? 25.342  -7.249  -37.876 1.00 11.84 ? 31  ASP C OD1 1 
ATOM   4528 O  OD2 . ASP C  1 31  ? 23.934  -7.102  -39.575 1.00 15.69 ? 31  ASP C OD2 1 
ATOM   4529 N  N   . LEU C  1 32  ? 28.122  -6.853  -39.625 1.00 9.69  ? 32  LEU C N   1 
ATOM   4530 C  CA  . LEU C  1 32  ? 28.791  -7.793  -40.512 1.00 10.70 ? 32  LEU C CA  1 
ATOM   4531 C  C   . LEU C  1 32  ? 27.894  -9.018  -40.707 1.00 12.62 ? 32  LEU C C   1 
ATOM   4532 O  O   . LEU C  1 32  ? 27.735  -9.826  -39.807 1.00 13.71 ? 32  LEU C O   1 
ATOM   4533 C  CB  . LEU C  1 32  ? 30.150  -8.264  -39.893 1.00 11.13 ? 32  LEU C CB  1 
ATOM   4534 C  CG  . LEU C  1 32  ? 31.054  -7.086  -39.439 1.00 10.78 ? 32  LEU C CG  1 
ATOM   4535 C  CD1 . LEU C  1 32  ? 32.281  -7.542  -38.588 1.00 13.10 ? 32  LEU C CD1 1 
ATOM   4536 C  CD2 . LEU C  1 32  ? 31.499  -6.292  -40.689 1.00 12.77 ? 32  LEU C CD2 1 
ATOM   4537 N  N   . HIS C  1 33  ? 27.271  -9.136  -41.848 1.00 16.56 ? 33  HIS C N   1 
ATOM   4538 C  CA  . HIS C  1 33  ? 26.255  -10.234 -42.092 1.00 19.01 ? 33  HIS C CA  1 
ATOM   4539 C  C   . HIS C  1 33  ? 26.458  -10.869 -43.434 1.00 17.77 ? 33  HIS C C   1 
ATOM   4540 O  O   . HIS C  1 33  ? 27.033  -10.234 -44.306 1.00 16.13 ? 33  HIS C O   1 
ATOM   4541 C  CB  . HIS C  1 33  ? 24.833  -9.738  -41.844 1.00 21.15 ? 33  HIS C CB  1 
ATOM   4542 C  CG  . HIS C  1 33  ? 24.410  -8.687  -42.782 1.00 21.20 ? 33  HIS C CG  1 
ATOM   4543 N  ND1 . HIS C  1 33  ? 23.708  -8.977  -43.904 1.00 24.67 ? 33  HIS C ND1 1 
ATOM   4544 C  CD2 . HIS C  1 33  ? 24.616  -7.298  -42.769 1.00 23.63 ? 33  HIS C CD2 1 
ATOM   4545 C  CE1 . HIS C  1 33  ? 23.500  -7.831  -44.597 1.00 23.95 ? 33  HIS C CE1 1 
ATOM   4546 N  NE2 . HIS C  1 33  ? 24.052  -6.806  -43.914 1.00 24.48 ? 33  HIS C NE2 1 
ATOM   4547 N  N   A SER C  1 34  ? 25.940  -12.088 -43.606 0.50 19.61 ? 34  SER C N   1 
ATOM   4548 N  N   B SER C  1 34  ? 26.015  -12.126 -43.660 0.50 19.14 ? 34  SER C N   1 
ATOM   4549 C  CA  A SER C  1 34  ? 26.328  -12.947 -44.700 0.50 21.74 ? 34  SER C CA  1 
ATOM   4550 C  CA  B SER C  1 34  ? 26.483  -12.902 -44.842 0.50 20.54 ? 34  SER C CA  1 
ATOM   4551 C  C   A SER C  1 34  ? 26.161  -12.359 -46.081 0.50 19.46 ? 34  SER C C   1 
ATOM   4552 C  C   B SER C  1 34  ? 26.203  -12.288 -46.174 0.50 19.33 ? 34  SER C C   1 
ATOM   4553 O  O   A SER C  1 34  ? 27.064  -12.530 -46.920 0.50 21.07 ? 34  SER C O   1 
ATOM   4554 O  O   B SER C  1 34  ? 27.048  -12.382 -47.086 0.50 20.70 ? 34  SER C O   1 
ATOM   4555 C  CB  A SER C  1 34  ? 25.560  -14.278 -44.600 0.50 22.10 ? 34  SER C CB  1 
ATOM   4556 C  CB  B SER C  1 34  ? 25.923  -14.344 -44.850 0.50 21.81 ? 34  SER C CB  1 
ATOM   4557 O  OG  A SER C  1 34  ? 24.173  -14.061 -44.711 0.50 25.08 ? 34  SER C OG  1 
ATOM   4558 O  OG  B SER C  1 34  ? 26.054  -14.886 -43.564 0.50 22.52 ? 34  SER C OG  1 
ATOM   4559 N  N   . ASP C  1 35  ? 25.041  -11.637 -46.290 1.00 19.60 ? 35  ASP C N   1 
ATOM   4560 C  CA  . ASP C  1 35  ? 24.588  -11.117 -47.601 1.00 24.54 ? 35  ASP C CA  1 
ATOM   4561 C  C   . ASP C  1 35  ? 25.494  -10.061 -48.172 1.00 19.30 ? 35  ASP C C   1 
ATOM   4562 O  O   . ASP C  1 35  ? 25.495  -9.787  -49.405 1.00 23.30 ? 35  ASP C O   1 
ATOM   4563 C  CB  . ASP C  1 35  ? 23.112  -10.612 -47.580 1.00 31.63 ? 35  ASP C CB  1 
ATOM   4564 C  CG  . ASP C  1 35  ? 22.112  -11.700 -47.141 1.00 43.74 ? 35  ASP C CG  1 
ATOM   4565 O  OD1 . ASP C  1 35  ? 22.386  -12.909 -47.364 1.00 40.57 ? 35  ASP C OD1 1 
ATOM   4566 O  OD2 . ASP C  1 35  ? 21.042  -11.345 -46.558 1.00 48.24 ? 35  ASP C OD2 1 
ATOM   4567 N  N   . ILE C  1 36  ? 26.381  -9.504  -47.324 1.00 16.70 ? 36  ILE C N   1 
ATOM   4568 C  CA  . ILE C  1 36  ? 27.261  -8.466  -47.771 1.00 14.59 ? 36  ILE C CA  1 
ATOM   4569 C  C   . ILE C  1 36  ? 28.750  -8.885  -47.723 1.00 13.96 ? 36  ILE C C   1 
ATOM   4570 O  O   . ILE C  1 36  ? 29.589  -8.090  -48.006 1.00 16.00 ? 36  ILE C O   1 
ATOM   4571 C  CB  . ILE C  1 36  ? 27.090  -7.121  -47.037 1.00 15.25 ? 36  ILE C CB  1 
ATOM   4572 C  CG1 . ILE C  1 36  ? 27.357  -7.262  -45.544 1.00 15.71 ? 36  ILE C CG1 1 
ATOM   4573 C  CG2 . ILE C  1 36  ? 25.696  -6.528  -47.368 1.00 17.96 ? 36  ILE C CG2 1 
ATOM   4574 C  CD1 . ILE C  1 36  ? 27.612  -5.959  -44.747 1.00 15.67 ? 36  ILE C CD1 1 
ATOM   4575 N  N   . LEU C  1 37  ? 29.018  -10.129 -47.434 1.00 16.29 ? 37  LEU C N   1 
ATOM   4576 C  CA  . LEU C  1 37  ? 30.431  -10.602 -47.328 1.00 15.59 ? 37  LEU C CA  1 
ATOM   4577 C  C   . LEU C  1 37  ? 30.860  -11.140 -48.643 1.00 17.31 ? 37  LEU C C   1 
ATOM   4578 O  O   . LEU C  1 37  ? 30.070  -11.830 -49.394 1.00 18.75 ? 37  LEU C O   1 
ATOM   4579 C  CB  . LEU C  1 37  ? 30.576  -11.761 -46.310 1.00 16.40 ? 37  LEU C CB  1 
ATOM   4580 C  CG  . LEU C  1 37  ? 30.096  -11.453 -44.917 1.00 15.61 ? 37  LEU C CG  1 
ATOM   4581 C  CD1 . LEU C  1 37  ? 30.301  -12.625 -44.022 1.00 16.36 ? 37  LEU C CD1 1 
ATOM   4582 C  CD2 . LEU C  1 37  ? 30.873  -10.231 -44.365 1.00 16.37 ? 37  LEU C CD2 1 
ATOM   4583 N  N   . GLN C  1 38  ? 32.084  -10.838 -49.018 1.00 14.41 ? 38  GLN C N   1 
ATOM   4584 C  CA  . GLN C  1 38  ? 32.652  -11.403 -50.252 1.00 16.55 ? 38  GLN C CA  1 
ATOM   4585 C  C   . GLN C  1 38  ? 34.090  -11.789 -49.991 1.00 15.58 ? 38  GLN C C   1 
ATOM   4586 O  O   . GLN C  1 38  ? 34.914  -10.933 -49.613 1.00 13.20 ? 38  GLN C O   1 
ATOM   4587 C  CB  . GLN C  1 38  ? 32.593  -10.374 -51.363 1.00 17.07 ? 38  GLN C CB  1 
ATOM   4588 C  CG  . GLN C  1 38  ? 33.008  -10.982 -52.700 1.00 20.23 ? 38  GLN C CG  1 
ATOM   4589 C  CD  . GLN C  1 38  ? 32.612  -10.091 -53.817 1.00 26.55 ? 38  GLN C CD  1 
ATOM   4590 O  OE1 . GLN C  1 38  ? 31.418  -10.056 -54.293 1.00 33.28 ? 38  GLN C OE1 1 
ATOM   4591 N  NE2 . GLN C  1 38  ? 33.544  -9.302  -54.212 1.00 19.12 ? 38  GLN C NE2 1 
ATOM   4592 N  N   . TYR C  1 39  ? 34.467  -13.054 -50.287 1.00 15.76 ? 39  TYR C N   1 
ATOM   4593 C  CA  . TYR C  1 39  ? 35.852  -13.427 -50.218 1.00 16.97 ? 39  TYR C CA  1 
ATOM   4594 C  C   . TYR C  1 39  ? 36.754  -12.625 -51.153 1.00 16.45 ? 39  TYR C C   1 
ATOM   4595 O  O   . TYR C  1 39  ? 36.388  -12.374 -52.332 1.00 18.54 ? 39  TYR C O   1 
ATOM   4596 C  CB  . TYR C  1 39  ? 35.934  -14.966 -50.600 1.00 18.37 ? 39  TYR C CB  1 
ATOM   4597 C  CG  . TYR C  1 39  ? 37.375  -15.413 -50.767 1.00 18.83 ? 39  TYR C CG  1 
ATOM   4598 C  CD1 . TYR C  1 39  ? 38.188  -15.530 -49.651 1.00 20.48 ? 39  TYR C CD1 1 
ATOM   4599 C  CD2 . TYR C  1 39  ? 37.890  -15.754 -52.059 1.00 20.11 ? 39  TYR C CD2 1 
ATOM   4600 C  CE1 . TYR C  1 39  ? 39.512  -15.914 -49.784 1.00 23.91 ? 39  TYR C CE1 1 
ATOM   4601 C  CE2 . TYR C  1 39  ? 39.219  -16.162 -52.187 1.00 21.91 ? 39  TYR C CE2 1 
ATOM   4602 C  CZ  . TYR C  1 39  ? 40.011  -16.240 -51.062 1.00 23.42 ? 39  TYR C CZ  1 
ATOM   4603 O  OH  . TYR C  1 39  ? 41.336  -16.651 -51.244 1.00 23.03 ? 39  TYR C OH  1 
ATOM   4604 N  N   . ASP C  1 40  ? 37.951  -12.231 -50.696 1.00 16.16 ? 40  ASP C N   1 
ATOM   4605 C  CA  . ASP C  1 40  ? 38.855  -11.398 -51.501 1.00 18.26 ? 40  ASP C CA  1 
ATOM   4606 C  C   . ASP C  1 40  ? 40.257  -12.039 -51.290 1.00 17.84 ? 40  ASP C C   1 
ATOM   4607 O  O   . ASP C  1 40  ? 40.843  -11.984 -50.188 1.00 18.44 ? 40  ASP C O   1 
ATOM   4608 C  CB  . ASP C  1 40  ? 38.805  -9.967  -50.936 1.00 17.56 ? 40  ASP C CB  1 
ATOM   4609 C  CG  . ASP C  1 40  ? 39.802  -8.949  -51.589 1.00 22.78 ? 40  ASP C CG  1 
ATOM   4610 O  OD1 . ASP C  1 40  ? 40.676  -9.309  -52.328 1.00 20.13 ? 40  ASP C OD1 1 
ATOM   4611 O  OD2 . ASP C  1 40  ? 39.669  -7.719  -51.322 1.00 25.87 ? 40  ASP C OD2 1 
ATOM   4612 N  N   . ALA C  1 41  ? 40.826  -12.588 -52.395 1.00 19.10 ? 41  ALA C N   1 
ATOM   4613 C  CA  . ALA C  1 41  ? 42.161  -13.244 -52.316 1.00 17.97 ? 41  ALA C CA  1 
ATOM   4614 C  C   . ALA C  1 41  ? 43.287  -12.264 -51.982 1.00 17.35 ? 41  ALA C C   1 
ATOM   4615 O  O   . ALA C  1 41  ? 44.413  -12.667 -51.634 1.00 18.92 ? 41  ALA C O   1 
ATOM   4616 C  CB  . ALA C  1 41  ? 42.443  -13.992 -53.634 1.00 19.99 ? 41  ALA C CB  1 
ATOM   4617 N  N   . SER C  1 42  ? 43.058  -10.946 -52.048 1.00 17.33 ? 42  SER C N   1 
ATOM   4618 C  CA  . SER C  1 42  ? 44.124  -10.055 -51.720 1.00 17.41 ? 42  SER C CA  1 
ATOM   4619 C  C   . SER C  1 42  ? 44.430  -10.008 -50.205 1.00 17.16 ? 42  SER C C   1 
ATOM   4620 O  O   . SER C  1 42  ? 45.423  -9.397  -49.763 1.00 19.56 ? 42  SER C O   1 
ATOM   4621 C  CB  . SER C  1 42  ? 43.842  -8.635  -52.263 1.00 19.08 ? 42  SER C CB  1 
ATOM   4622 O  OG  . SER C  1 42  ? 42.994  -7.902  -51.346 1.00 20.60 ? 42  SER C OG  1 
ATOM   4623 N  N   . LEU C  1 43  ? 43.497  -10.627 -49.433 1.00 15.77 ? 43  LEU C N   1 
ATOM   4624 C  CA  . LEU C  1 43  ? 43.527  -10.436 -47.969 1.00 14.98 ? 43  LEU C CA  1 
ATOM   4625 C  C   . LEU C  1 43  ? 44.389  -11.500 -47.326 1.00 16.77 ? 43  LEU C C   1 
ATOM   4626 O  O   . LEU C  1 43  ? 43.912  -12.446 -46.691 1.00 17.85 ? 43  LEU C O   1 
ATOM   4627 C  CB  . LEU C  1 43  ? 42.100  -10.452 -47.423 1.00 14.62 ? 43  LEU C CB  1 
ATOM   4628 C  CG  . LEU C  1 43  ? 41.317  -9.217  -47.923 1.00 13.26 ? 43  LEU C CG  1 
ATOM   4629 C  CD1 . LEU C  1 43  ? 39.894  -9.343  -47.307 1.00 14.25 ? 43  LEU C CD1 1 
ATOM   4630 C  CD2 . LEU C  1 43  ? 41.913  -7.855  -47.668 1.00 15.44 ? 43  LEU C CD2 1 
ATOM   4631 N  N   . THR C  1 44  ? 45.686  -11.313 -47.544 1.00 18.19 ? 44  THR C N   1 
ATOM   4632 C  CA  . THR C  1 44  ? 46.752  -12.163 -46.944 1.00 18.10 ? 44  THR C CA  1 
ATOM   4633 C  C   . THR C  1 44  ? 46.958  -11.905 -45.415 1.00 20.03 ? 44  THR C C   1 
ATOM   4634 O  O   . THR C  1 44  ? 46.495  -10.885 -44.907 1.00 16.97 ? 44  THR C O   1 
ATOM   4635 C  CB  . THR C  1 44  ? 48.069  -11.935 -47.770 1.00 18.55 ? 44  THR C CB  1 
ATOM   4636 O  OG1 . THR C  1 44  ? 48.287  -10.531 -47.908 1.00 21.87 ? 44  THR C OG1 1 
ATOM   4637 C  CG2 . THR C  1 44  ? 47.874  -12.505 -49.113 1.00 22.24 ? 44  THR C CG2 1 
ATOM   4638 N  N   . PRO C  1 45  ? 47.701  -12.749 -44.675 1.00 18.78 ? 45  PRO C N   1 
ATOM   4639 C  CA  . PRO C  1 45  ? 47.887  -12.530 -43.232 1.00 18.48 ? 45  PRO C CA  1 
ATOM   4640 C  C   . PRO C  1 45  ? 48.700  -11.302 -42.941 1.00 21.19 ? 45  PRO C C   1 
ATOM   4641 O  O   . PRO C  1 45  ? 49.714  -11.105 -43.589 1.00 23.44 ? 45  PRO C O   1 
ATOM   4642 C  CB  . PRO C  1 45  ? 48.658  -13.774 -42.801 1.00 21.32 ? 45  PRO C CB  1 
ATOM   4643 C  CG  . PRO C  1 45  ? 48.215  -14.832 -43.756 1.00 18.52 ? 45  PRO C CG  1 
ATOM   4644 C  CD  . PRO C  1 45  ? 48.097  -14.136 -45.071 1.00 19.01 ? 45  PRO C CD  1 
ATOM   4645 N  N   . LEU C  1 46  ? 48.293  -10.480 -41.964 1.00 16.70 ? 46  LEU C N   1 
ATOM   4646 C  CA  . LEU C  1 46  ? 49.061  -9.334  -41.497 1.00 19.59 ? 46  LEU C CA  1 
ATOM   4647 C  C   . LEU C  1 46  ? 50.159  -9.867  -40.582 1.00 18.69 ? 46  LEU C C   1 
ATOM   4648 O  O   . LEU C  1 46  ? 49.995  -10.915 -39.987 1.00 20.04 ? 46  LEU C O   1 
ATOM   4649 C  CB  . LEU C  1 46  ? 48.198  -8.405  -40.686 1.00 18.45 ? 46  LEU C CB  1 
ATOM   4650 C  CG  . LEU C  1 46  ? 47.090  -7.792  -41.539 1.00 19.27 ? 46  LEU C CG  1 
ATOM   4651 C  CD1 . LEU C  1 46  ? 46.237  -6.871  -40.673 1.00 21.13 ? 46  LEU C CD1 1 
ATOM   4652 C  CD2 . LEU C  1 46  ? 47.633  -7.104  -42.804 1.00 20.98 ? 46  LEU C CD2 1 
ATOM   4653 N  N   . GLU C  1 47  ? 51.230  -9.109  -40.485 1.00 19.85 ? 47  GLU C N   1 
ATOM   4654 C  CA  . GLU C  1 47  ? 52.250  -9.326  -39.456 1.00 19.91 ? 47  GLU C CA  1 
ATOM   4655 C  C   . GLU C  1 47  ? 52.304  -8.196  -38.482 1.00 17.81 ? 47  GLU C C   1 
ATOM   4656 O  O   . GLU C  1 47  ? 52.202  -6.991  -38.912 1.00 17.93 ? 47  GLU C O   1 
ATOM   4657 C  CB  . GLU C  1 47  ? 53.627  -9.437  -40.154 1.00 27.03 ? 47  GLU C CB  1 
ATOM   4658 C  CG  . GLU C  1 47  ? 53.702  -10.514 -41.250 1.00 31.94 ? 47  GLU C CG  1 
ATOM   4659 C  CD  . GLU C  1 47  ? 53.891  -11.943 -40.713 1.00 47.61 ? 47  GLU C CD  1 
ATOM   4660 O  OE1 . GLU C  1 47  ? 54.796  -12.166 -39.845 1.00 56.30 ? 47  GLU C OE1 1 
ATOM   4661 O  OE2 . GLU C  1 47  ? 53.141  -12.855 -41.164 1.00 48.23 ? 47  GLU C OE2 1 
ATOM   4662 N  N   . PHE C  1 48  ? 52.508  -8.504  -37.202 1.00 17.01 ? 48  PHE C N   1 
ATOM   4663 C  CA  . PHE C  1 48  ? 52.472  -7.534  -36.135 1.00 17.88 ? 48  PHE C CA  1 
ATOM   4664 C  C   . PHE C  1 48  ? 53.877  -7.416  -35.644 1.00 17.65 ? 48  PHE C C   1 
ATOM   4665 O  O   . PHE C  1 48  ? 54.382  -8.304  -34.991 1.00 22.51 ? 48  PHE C O   1 
ATOM   4666 C  CB  . PHE C  1 48  ? 51.432  -7.965  -35.048 1.00 17.41 ? 48  PHE C CB  1 
ATOM   4667 C  CG  . PHE C  1 48  ? 50.132  -8.447  -35.680 1.00 17.97 ? 48  PHE C CG  1 
ATOM   4668 C  CD1 . PHE C  1 48  ? 49.327  -7.518  -36.227 1.00 18.61 ? 48  PHE C CD1 1 
ATOM   4669 C  CD2 . PHE C  1 48  ? 49.788  -9.780  -35.798 1.00 16.81 ? 48  PHE C CD2 1 
ATOM   4670 C  CE1 . PHE C  1 48  ? 48.197  -7.907  -36.887 1.00 16.86 ? 48  PHE C CE1 1 
ATOM   4671 C  CE2 . PHE C  1 48  ? 48.614  -10.185 -36.385 1.00 19.02 ? 48  PHE C CE2 1 
ATOM   4672 C  CZ  . PHE C  1 48  ? 47.804  -9.217  -36.911 1.00 16.64 ? 48  PHE C CZ  1 
ATOM   4673 N  N   . GLN C  1 49  ? 54.434  -6.260  -35.890 1.00 17.30 ? 49  GLN C N   1 
ATOM   4674 C  CA  . GLN C  1 49  ? 55.879  -6.023  -35.587 1.00 18.53 ? 49  GLN C CA  1 
ATOM   4675 C  C   . GLN C  1 49  ? 56.099  -5.116  -34.459 1.00 18.20 ? 49  GLN C C   1 
ATOM   4676 O  O   . GLN C  1 49  ? 55.474  -4.098  -34.368 1.00 16.74 ? 49  GLN C O   1 
ATOM   4677 C  CB  . GLN C  1 49  ? 56.525  -5.466  -36.841 1.00 20.42 ? 49  GLN C CB  1 
ATOM   4678 C  CG  . GLN C  1 49  ? 56.366  -6.582  -37.862 1.00 25.65 ? 49  GLN C CG  1 
ATOM   4679 C  CD  . GLN C  1 49  ? 57.240  -6.478  -39.076 1.00 37.35 ? 49  GLN C CD  1 
ATOM   4680 O  OE1 . GLN C  1 49  ? 57.631  -5.372  -39.494 1.00 41.69 ? 49  GLN C OE1 1 
ATOM   4681 N  NE2 . GLN C  1 49  ? 57.525  -7.643  -39.695 1.00 40.84 ? 49  GLN C NE2 1 
ATOM   4682 N  N   . GLY C  1 50  ? 57.078  -5.445  -33.573 1.00 17.09 ? 50  GLY C N   1 
ATOM   4683 C  CA  . GLY C  1 50  ? 57.309  -4.501  -32.534 1.00 19.30 ? 50  GLY C CA  1 
ATOM   4684 C  C   . GLY C  1 50  ? 56.261  -4.534  -31.443 1.00 18.24 ? 50  GLY C C   1 
ATOM   4685 O  O   . GLY C  1 50  ? 56.214  -3.661  -30.592 1.00 19.36 ? 50  GLY C O   1 
ATOM   4686 N  N   . TYR C  1 51  ? 55.402  -5.549  -31.445 1.00 17.40 ? 51  TYR C N   1 
ATOM   4687 C  CA  . TYR C  1 51  ? 54.285  -5.615  -30.463 1.00 17.54 ? 51  TYR C CA  1 
ATOM   4688 C  C   . TYR C  1 51  ? 54.694  -6.117  -29.103 1.00 17.81 ? 51  TYR C C   1 
ATOM   4689 O  O   . TYR C  1 51  ? 54.038  -5.900  -28.132 1.00 17.08 ? 51  TYR C O   1 
ATOM   4690 C  CB  . TYR C  1 51  ? 53.088  -6.527  -30.975 1.00 15.73 ? 51  TYR C CB  1 
ATOM   4691 C  CG  . TYR C  1 51  ? 52.094  -5.840  -31.894 1.00 14.79 ? 51  TYR C CG  1 
ATOM   4692 C  CD1 . TYR C  1 51  ? 52.490  -5.009  -32.945 1.00 13.19 ? 51  TYR C CD1 1 
ATOM   4693 C  CD2 . TYR C  1 51  ? 50.739  -6.040  -31.704 1.00 14.41 ? 51  TYR C CD2 1 
ATOM   4694 C  CE1 . TYR C  1 51  ? 51.550  -4.406  -33.770 1.00 14.95 ? 51  TYR C CE1 1 
ATOM   4695 C  CE2 . TYR C  1 51  ? 49.804  -5.447  -32.517 1.00 15.37 ? 51  TYR C CE2 1 
ATOM   4696 C  CZ  . TYR C  1 51  ? 50.208  -4.629  -33.535 1.00 16.51 ? 51  TYR C CZ  1 
ATOM   4697 O  OH  . TYR C  1 51  ? 49.230  -4.060  -34.318 1.00 16.55 ? 51  TYR C OH  1 
ATOM   4698 N  N   . ASN C  1 52  ? 55.874  -6.774  -29.047 1.00 20.31 ? 52  ASN C N   1 
ATOM   4699 C  CA  . ASN C  1 52  ? 56.338  -7.338  -27.746 1.00 21.17 ? 52  ASN C CA  1 
ATOM   4700 C  C   . ASN C  1 52  ? 57.069  -6.242  -26.951 1.00 22.81 ? 52  ASN C C   1 
ATOM   4701 O  O   . ASN C  1 52  ? 58.266  -6.030  -27.148 1.00 25.45 ? 52  ASN C O   1 
ATOM   4702 C  CB  . ASN C  1 52  ? 57.218  -8.553  -28.015 1.00 22.46 ? 52  ASN C CB  1 
ATOM   4703 C  CG  . ASN C  1 52  ? 57.581  -9.277  -26.723 1.00 25.40 ? 52  ASN C CG  1 
ATOM   4704 O  OD1 . ASN C  1 52  ? 56.870  -9.225  -25.730 1.00 24.55 ? 52  ASN C OD1 1 
ATOM   4705 N  ND2 . ASN C  1 52  ? 58.765  -9.886  -26.715 1.00 30.85 ? 52  ASN C ND2 1 
ATOM   4706 N  N   . LEU C  1 53  ? 56.293  -5.545  -26.118 1.00 20.24 ? 53  LEU C N   1 
ATOM   4707 C  CA  . LEU C  1 53  ? 56.795  -4.342  -25.457 1.00 24.40 ? 53  LEU C CA  1 
ATOM   4708 C  C   . LEU C  1 53  ? 57.451  -4.835  -24.131 1.00 22.26 ? 53  LEU C C   1 
ATOM   4709 O  O   . LEU C  1 53  ? 56.879  -5.618  -23.332 1.00 22.70 ? 53  LEU C O   1 
ATOM   4710 C  CB  . LEU C  1 53  ? 55.670  -3.334  -25.187 1.00 20.15 ? 53  LEU C CB  1 
ATOM   4711 C  CG  . LEU C  1 53  ? 54.729  -2.976  -26.359 1.00 18.59 ? 53  LEU C CG  1 
ATOM   4712 C  CD1 . LEU C  1 53  ? 53.679  -2.026  -25.739 1.00 20.44 ? 53  LEU C CD1 1 
ATOM   4713 C  CD2 . LEU C  1 53  ? 55.429  -2.183  -27.490 1.00 21.53 ? 53  LEU C CD2 1 
ATOM   4714 N  N   . SER C  1 54  ? 58.633  -4.339  -23.852 1.00 26.69 ? 54  SER C N   1 
ATOM   4715 C  CA  . SER C  1 54  ? 59.343  -4.769  -22.620 1.00 29.25 ? 54  SER C CA  1 
ATOM   4716 C  C   . SER C  1 54  ? 58.596  -4.470  -21.318 1.00 31.61 ? 54  SER C C   1 
ATOM   4717 O  O   . SER C  1 54  ? 58.068  -3.350  -21.118 1.00 31.13 ? 54  SER C O   1 
ATOM   4718 C  CB  . SER C  1 54  ? 60.695  -4.101  -22.545 1.00 26.97 ? 54  SER C CB  1 
ATOM   4719 O  OG  . SER C  1 54  ? 61.440  -4.452  -23.707 1.00 32.77 ? 54  SER C OG  1 
ATOM   4720 N  N   . ALA C  1 55  ? 58.604  -5.447  -20.416 1.00 30.42 ? 55  ALA C N   1 
ATOM   4721 C  CA  . ALA C  1 55  ? 57.996  -5.325  -19.047 1.00 31.91 ? 55  ALA C CA  1 
ATOM   4722 C  C   . ALA C  1 55  ? 58.606  -4.160  -18.240 1.00 34.56 ? 55  ALA C C   1 
ATOM   4723 O  O   . ALA C  1 55  ? 57.923  -3.612  -17.320 1.00 27.75 ? 55  ALA C O   1 
ATOM   4724 C  CB  . ALA C  1 55  ? 58.144  -6.639  -18.283 1.00 29.79 ? 55  ALA C CB  1 
ATOM   4725 N  N   . ASN C  1 56  ? 59.848  -3.754  -18.584 1.00 29.11 ? 56  ASN C N   1 
ATOM   4726 C  CA  . ASN C  1 56  ? 60.481  -2.706  -17.784 1.00 29.10 ? 56  ASN C CA  1 
ATOM   4727 C  C   . ASN C  1 56  ? 60.263  -1.309  -18.415 1.00 29.67 ? 56  ASN C C   1 
ATOM   4728 O  O   . ASN C  1 56  ? 60.704  -0.282  -17.855 1.00 25.33 ? 56  ASN C O   1 
ATOM   4729 C  CB  . ASN C  1 56  ? 61.955  -3.049  -17.417 1.00 32.00 ? 56  ASN C CB  1 
ATOM   4730 C  CG  . ASN C  1 56  ? 62.899  -2.954  -18.619 1.00 33.93 ? 56  ASN C CG  1 
ATOM   4731 O  OD1 . ASN C  1 56  ? 62.446  -2.738  -19.764 1.00 33.74 ? 56  ASN C OD1 1 
ATOM   4732 N  ND2 . ASN C  1 56  ? 64.219  -3.057  -18.364 1.00 30.30 ? 56  ASN C ND2 1 
ATOM   4733 N  N   . LYS C  1 57  ? 59.538  -1.289  -19.571 1.00 25.97 ? 57  LYS C N   1 
ATOM   4734 C  CA  . LYS C  1 57  ? 59.032  -0.020  -20.145 1.00 26.11 ? 57  LYS C CA  1 
ATOM   4735 C  C   . LYS C  1 57  ? 57.662  0.198   -19.639 1.00 25.42 ? 57  LYS C C   1 
ATOM   4736 O  O   . LYS C  1 57  ? 57.030  -0.710  -19.005 1.00 21.13 ? 57  LYS C O   1 
ATOM   4737 C  CB  . LYS C  1 57  ? 59.027  -0.077  -21.669 1.00 27.17 ? 57  LYS C CB  1 
ATOM   4738 C  CG  . LYS C  1 57  ? 60.423  -0.168  -22.214 1.00 32.01 ? 57  LYS C CG  1 
ATOM   4739 C  CD  . LYS C  1 57  ? 60.258  0.068   -23.700 1.00 33.93 ? 57  LYS C CD  1 
ATOM   4740 C  CE  . LYS C  1 57  ? 61.595  -0.080  -24.418 1.00 39.11 ? 57  LYS C CE  1 
ATOM   4741 N  NZ  . LYS C  1 57  ? 61.438  0.313   -25.860 1.00 46.25 ? 57  LYS C NZ  1 
ATOM   4742 N  N   . GLN C  1 58  ? 57.200  1.446   -19.775 1.00 23.90 ? 58  GLN C N   1 
ATOM   4743 C  CA  . GLN C  1 58  ? 55.817  1.730   -19.396 1.00 22.44 ? 58  GLN C CA  1 
ATOM   4744 C  C   . GLN C  1 58  ? 55.186  2.687   -20.416 1.00 19.97 ? 58  GLN C C   1 
ATOM   4745 O  O   . GLN C  1 58  ? 55.871  3.464   -21.142 1.00 19.27 ? 58  GLN C O   1 
ATOM   4746 C  CB  . GLN C  1 58  ? 55.784  2.281   -17.957 1.00 22.71 ? 58  GLN C CB  1 
ATOM   4747 C  CG  . GLN C  1 58  ? 56.396  3.699   -17.882 1.00 22.95 ? 58  GLN C CG  1 
ATOM   4748 C  CD  . GLN C  1 58  ? 56.337  4.334   -16.465 1.00 24.47 ? 58  GLN C CD  1 
ATOM   4749 O  OE1 . GLN C  1 58  ? 55.961  3.642   -15.523 1.00 24.90 ? 58  GLN C OE1 1 
ATOM   4750 N  NE2 . GLN C  1 58  ? 56.619  5.657   -16.341 1.00 20.02 ? 58  GLN C NE2 1 
ATOM   4751 N  N   . PHE C  1 59  ? 53.854  2.614   -20.361 1.00 22.27 ? 59  PHE C N   1 
ATOM   4752 C  CA  . PHE C  1 59  ? 52.921  3.162   -21.365 1.00 19.37 ? 59  PHE C CA  1 
ATOM   4753 C  C   . PHE C  1 59  ? 51.802  3.834   -20.650 1.00 18.05 ? 59  PHE C C   1 
ATOM   4754 O  O   . PHE C  1 59  ? 51.279  3.325   -19.690 1.00 20.53 ? 59  PHE C O   1 
ATOM   4755 C  CB  . PHE C  1 59  ? 52.556  1.992   -22.360 1.00 20.03 ? 59  PHE C CB  1 
ATOM   4756 C  CG  . PHE C  1 59  ? 53.775  1.420   -23.007 1.00 18.86 ? 59  PHE C CG  1 
ATOM   4757 C  CD1 . PHE C  1 59  ? 54.361  2.059   -24.103 1.00 18.29 ? 59  PHE C CD1 1 
ATOM   4758 C  CD2 . PHE C  1 59  ? 54.453  0.313   -22.417 1.00 19.42 ? 59  PHE C CD2 1 
ATOM   4759 C  CE1 . PHE C  1 59  ? 55.569  1.589   -24.651 1.00 20.18 ? 59  PHE C CE1 1 
ATOM   4760 C  CE2 . PHE C  1 59  ? 55.667  -0.086  -22.889 1.00 19.93 ? 59  PHE C CE2 1 
ATOM   4761 C  CZ  . PHE C  1 59  ? 56.215  0.503   -23.993 1.00 17.10 ? 59  PHE C CZ  1 
ATOM   4762 N  N   . LEU C  1 60  ? 51.469  5.045   -21.086 1.00 17.06 ? 60  LEU C N   1 
ATOM   4763 C  CA  . LEU C  1 60  ? 50.607  5.925   -20.332 1.00 16.70 ? 60  LEU C CA  1 
ATOM   4764 C  C   . LEU C  1 60  ? 49.187  5.403   -20.604 1.00 17.79 ? 60  LEU C C   1 
ATOM   4765 O  O   . LEU C  1 60  ? 48.710  5.354   -21.815 1.00 18.79 ? 60  LEU C O   1 
ATOM   4766 C  CB  . LEU C  1 60  ? 50.731  7.374   -20.869 1.00 15.31 ? 60  LEU C CB  1 
ATOM   4767 C  CG  . LEU C  1 60  ? 49.870  8.427   -20.185 1.00 19.65 ? 60  LEU C CG  1 
ATOM   4768 C  CD1 . LEU C  1 60  ? 50.378  8.554   -18.731 1.00 21.55 ? 60  LEU C CD1 1 
ATOM   4769 C  CD2 . LEU C  1 60  ? 50.016  9.769   -20.905 1.00 23.12 ? 60  LEU C CD2 1 
ATOM   4770 N  N   . LEU C  1 61  ? 48.436  5.142   -19.551 1.00 16.52 ? 61  LEU C N   1 
ATOM   4771 C  CA  . LEU C  1 61  ? 46.983  4.814   -19.569 1.00 17.88 ? 61  LEU C CA  1 
ATOM   4772 C  C   . LEU C  1 61  ? 46.201  6.070   -19.156 1.00 18.84 ? 61  LEU C C   1 
ATOM   4773 O  O   . LEU C  1 61  ? 46.534  6.701   -18.127 1.00 20.25 ? 61  LEU C O   1 
ATOM   4774 C  CB  . LEU C  1 61  ? 46.839  3.679   -18.588 1.00 18.77 ? 61  LEU C CB  1 
ATOM   4775 C  CG  . LEU C  1 61  ? 45.466  3.067   -18.560 1.00 21.13 ? 61  LEU C CG  1 
ATOM   4776 C  CD1 . LEU C  1 61  ? 45.390  2.120   -19.774 1.00 23.01 ? 61  LEU C CD1 1 
ATOM   4777 C  CD2 . LEU C  1 61  ? 45.268  2.242   -17.294 1.00 22.14 ? 61  LEU C CD2 1 
ATOM   4778 N  N   . THR C  1 62  ? 45.210  6.462   -19.904 1.00 14.71 ? 62  THR C N   1 
ATOM   4779 C  CA  . THR C  1 62  ? 44.505  7.702   -19.684 1.00 15.55 ? 62  THR C CA  1 
ATOM   4780 C  C   . THR C  1 62  ? 43.029  7.447   -19.736 1.00 17.15 ? 62  THR C C   1 
ATOM   4781 O  O   . THR C  1 62  ? 42.504  6.761   -20.681 1.00 18.54 ? 62  THR C O   1 
ATOM   4782 C  CB  . THR C  1 62  ? 44.735  8.745   -20.813 1.00 17.73 ? 62  THR C CB  1 
ATOM   4783 O  OG1 . THR C  1 62  ? 46.125  9.025   -20.867 1.00 20.10 ? 62  THR C OG1 1 
ATOM   4784 C  CG2 . THR C  1 62  ? 43.876  10.126  -20.508 1.00 17.98 ? 62  THR C CG2 1 
ATOM   4785 N  N   . ASN C  1 63  ? 42.309  7.917   -18.729 1.00 19.04 ? 63  ASN C N   1 
ATOM   4786 C  CA  . ASN C  1 63  ? 40.931  8.073   -18.871 1.00 16.60 ? 63  ASN C CA  1 
ATOM   4787 C  C   . ASN C  1 63  ? 40.624  9.386   -19.521 1.00 20.86 ? 63  ASN C C   1 
ATOM   4788 O  O   . ASN C  1 63  ? 40.764  10.443  -18.870 1.00 18.66 ? 63  ASN C O   1 
ATOM   4789 C  CB  . ASN C  1 63  ? 40.286  7.966   -17.474 1.00 18.01 ? 63  ASN C CB  1 
ATOM   4790 C  CG  . ASN C  1 63  ? 38.761  8.232   -17.461 1.00 17.19 ? 63  ASN C CG  1 
ATOM   4791 O  OD1 . ASN C  1 63  ? 38.188  8.877   -18.328 1.00 17.73 ? 63  ASN C OD1 1 
ATOM   4792 N  ND2 . ASN C  1 63  ? 38.104  7.826   -16.353 1.00 14.85 ? 63  ASN C ND2 1 
ATOM   4793 N  N   . ASN C  1 64  ? 40.216  9.341   -20.796 1.00 17.76 ? 64  ASN C N   1 
ATOM   4794 C  CA  . ASN C  1 64  ? 39.864  10.591  -21.463 1.00 20.77 ? 64  ASN C CA  1 
ATOM   4795 C  C   . ASN C  1 64  ? 38.444  10.999  -21.425 1.00 20.32 ? 64  ASN C C   1 
ATOM   4796 O  O   . ASN C  1 64  ? 38.032  11.900  -22.196 1.00 21.85 ? 64  ASN C O   1 
ATOM   4797 C  CB  . ASN C  1 64  ? 40.443  10.558  -22.911 1.00 18.79 ? 64  ASN C CB  1 
ATOM   4798 C  CG  . ASN C  1 64  ? 39.784  9.482   -23.720 1.00 17.78 ? 64  ASN C CG  1 
ATOM   4799 O  OD1 . ASN C  1 64  ? 38.678  9.065   -23.368 1.00 17.83 ? 64  ASN C OD1 1 
ATOM   4800 N  ND2 . ASN C  1 64  ? 40.487  8.940   -24.739 1.00 22.89 ? 64  ASN C ND2 1 
ATOM   4801 N  N   . GLY C  1 65  ? 37.637  10.381  -20.554 1.00 20.63 ? 65  GLY C N   1 
ATOM   4802 C  CA  . GLY C  1 65  ? 36.219  10.734  -20.457 1.00 21.61 ? 65  GLY C CA  1 
ATOM   4803 C  C   . GLY C  1 65  ? 35.331  9.980   -21.432 1.00 21.34 ? 65  GLY C C   1 
ATOM   4804 O  O   . GLY C  1 65  ? 34.140  9.904   -21.270 1.00 26.00 ? 65  GLY C O   1 
ATOM   4805 N  N   . HIS C  1 66  ? 35.977  9.337   -22.413 1.00 17.42 ? 66  HIS C N   1 
ATOM   4806 C  CA  . HIS C  1 66  ? 35.260  8.604   -23.472 1.00 20.05 ? 66  HIS C CA  1 
ATOM   4807 C  C   . HIS C  1 66  ? 35.598  7.158   -23.424 1.00 15.43 ? 66  HIS C C   1 
ATOM   4808 O  O   . HIS C  1 66  ? 34.772  6.270   -23.759 1.00 18.19 ? 66  HIS C O   1 
ATOM   4809 C  CB  . HIS C  1 66  ? 35.717  9.145   -24.803 1.00 19.37 ? 66  HIS C CB  1 
ATOM   4810 C  CG  . HIS C  1 66  ? 35.535  10.612  -24.936 1.00 21.65 ? 66  HIS C CG  1 
ATOM   4811 N  ND1 . HIS C  1 66  ? 36.576  11.497  -25.127 1.00 21.04 ? 66  HIS C ND1 1 
ATOM   4812 C  CD2 . HIS C  1 66  ? 34.367  11.372  -24.855 1.00 18.11 ? 66  HIS C CD2 1 
ATOM   4813 C  CE1 . HIS C  1 66  ? 36.054  12.738  -25.201 1.00 20.70 ? 66  HIS C CE1 1 
ATOM   4814 N  NE2 . HIS C  1 66  ? 34.699  12.653  -25.015 1.00 25.73 ? 66  HIS C NE2 1 
ATOM   4815 N  N   . SER C  1 67  ? 36.781  6.866   -23.022 1.00 17.12 ? 67  SER C N   1 
ATOM   4816 C  CA  . SER C  1 67  ? 37.242  5.479   -22.925 1.00 12.97 ? 67  SER C CA  1 
ATOM   4817 C  C   . SER C  1 67  ? 38.471  5.475   -22.035 1.00 17.23 ? 67  SER C C   1 
ATOM   4818 O  O   . SER C  1 67  ? 38.776  6.556   -21.500 1.00 19.14 ? 67  SER C O   1 
ATOM   4819 C  CB  . SER C  1 67  ? 37.599  4.950   -24.315 1.00 13.73 ? 67  SER C CB  1 
ATOM   4820 O  OG  . SER C  1 67  ? 38.021  3.599   -24.264 1.00 15.41 ? 67  SER C OG  1 
ATOM   4821 N  N   . VAL C  1 68  ? 39.117  4.288   -21.928 1.00 14.79 ? 68  VAL C N   1 
ATOM   4822 C  CA  . VAL C  1 68  ? 40.466  4.176   -21.367 1.00 17.26 ? 68  VAL C CA  1 
ATOM   4823 C  C   . VAL C  1 68  ? 41.392  3.849   -22.533 1.00 18.38 ? 68  VAL C C   1 
ATOM   4824 O  O   . VAL C  1 68  ? 41.095  2.887   -23.302 1.00 16.95 ? 68  VAL C O   1 
ATOM   4825 C  CB  . VAL C  1 68  ? 40.508  3.111   -20.186 1.00 16.15 ? 68  VAL C CB  1 
ATOM   4826 C  CG1 . VAL C  1 68  ? 40.299  1.665   -20.593 1.00 17.35 ? 68  VAL C CG1 1 
ATOM   4827 C  CG2 . VAL C  1 68  ? 41.817  3.260   -19.385 1.00 18.44 ? 68  VAL C CG2 1 
ATOM   4828 N  N   . LYS C  1 69  ? 42.472  4.638   -22.695 1.00 17.27 ? 69  LYS C N   1 
ATOM   4829 C  CA  . LYS C  1 69  ? 43.398  4.450   -23.816 1.00 15.50 ? 69  LYS C CA  1 
ATOM   4830 C  C   . LYS C  1 69  ? 44.784  4.205   -23.255 1.00 18.52 ? 69  LYS C C   1 
ATOM   4831 O  O   . LYS C  1 69  ? 45.142  4.701   -22.186 1.00 20.19 ? 69  LYS C O   1 
ATOM   4832 C  CB  . LYS C  1 69  ? 43.306  5.589   -24.767 1.00 22.57 ? 69  LYS C CB  1 
ATOM   4833 C  CG  . LYS C  1 69  ? 43.902  6.873   -24.266 1.00 26.40 ? 69  LYS C CG  1 
ATOM   4834 C  CD  . LYS C  1 69  ? 44.157  7.863   -25.383 1.00 28.25 ? 69  LYS C CD  1 
ATOM   4835 C  CE  . LYS C  1 69  ? 44.610  9.127   -24.653 1.00 29.38 ? 69  LYS C CE  1 
ATOM   4836 N  NZ  . LYS C  1 69  ? 44.954  10.213  -25.592 1.00 32.37 ? 69  LYS C NZ  1 
ATOM   4837 N  N   . LEU C  1 70  ? 45.527  3.351   -23.928 1.00 15.39 ? 70  LEU C N   1 
ATOM   4838 C  CA  . LEU C  1 70  ? 46.908  3.097   -23.664 1.00 15.07 ? 70  LEU C CA  1 
ATOM   4839 C  C   . LEU C  1 70  ? 47.682  3.623   -24.805 1.00 13.87 ? 70  LEU C C   1 
ATOM   4840 O  O   . LEU C  1 70  ? 47.520  3.167   -25.972 1.00 14.31 ? 70  LEU C O   1 
ATOM   4841 C  CB  . LEU C  1 70  ? 47.136  1.574   -23.497 1.00 14.95 ? 70  LEU C CB  1 
ATOM   4842 C  CG  . LEU C  1 70  ? 48.542  1.121   -23.146 1.00 17.69 ? 70  LEU C CG  1 
ATOM   4843 C  CD1 . LEU C  1 70  ? 48.857  1.581   -21.698 1.00 16.85 ? 70  LEU C CD1 1 
ATOM   4844 C  CD2 . LEU C  1 70  ? 48.736  -0.416  -23.269 1.00 16.01 ? 70  LEU C CD2 1 
ATOM   4845 N  N   . ASN C  1 71  ? 48.622  4.533   -24.535 1.00 15.29 ? 71  ASN C N   1 
ATOM   4846 C  CA  . ASN C  1 71  ? 49.470  5.017   -25.571 1.00 15.69 ? 71  ASN C CA  1 
ATOM   4847 C  C   . ASN C  1 71  ? 50.447  3.883   -25.989 1.00 16.40 ? 71  ASN C C   1 
ATOM   4848 O  O   . ASN C  1 71  ? 50.925  3.071   -25.178 1.00 17.40 ? 71  ASN C O   1 
ATOM   4849 C  CB  . ASN C  1 71  ? 50.215  6.311   -25.109 1.00 15.32 ? 71  ASN C CB  1 
ATOM   4850 C  CG  . ASN C  1 71  ? 49.299  7.544   -25.103 1.00 23.44 ? 71  ASN C CG  1 
ATOM   4851 O  OD1 . ASN C  1 71  ? 48.111  7.471   -25.468 1.00 22.38 ? 71  ASN C OD1 1 
ATOM   4852 N  ND2 . ASN C  1 71  ? 49.889  8.730   -24.805 1.00 24.00 ? 71  ASN C ND2 1 
ATOM   4853 N  N   . LEU C  1 72  ? 50.719  3.803   -27.309 1.00 13.89 ? 72  LEU C N   1 
ATOM   4854 C  CA  . LEU C  1 72  ? 51.557  2.766   -27.869 1.00 14.62 ? 72  LEU C CA  1 
ATOM   4855 C  C   . LEU C  1 72  ? 52.707  3.408   -28.690 1.00 12.94 ? 72  LEU C C   1 
ATOM   4856 O  O   . LEU C  1 72  ? 52.546  4.517   -29.213 1.00 16.58 ? 72  LEU C O   1 
ATOM   4857 C  CB  . LEU C  1 72  ? 50.782  1.941   -28.889 1.00 13.66 ? 72  LEU C CB  1 
ATOM   4858 C  CG  . LEU C  1 72  ? 49.749  1.107   -28.135 1.00 15.01 ? 72  LEU C CG  1 
ATOM   4859 C  CD1 . LEU C  1 72  ? 48.791  0.454   -29.161 1.00 15.43 ? 72  LEU C CD1 1 
ATOM   4860 C  CD2 . LEU C  1 72  ? 50.324  0.011   -27.285 1.00 17.09 ? 72  LEU C CD2 1 
ATOM   4861 N  N   . PRO C  1 73  ? 53.882  2.784   -28.762 1.00 17.21 ? 73  PRO C N   1 
ATOM   4862 C  CA  . PRO C  1 73  ? 55.024  3.381   -29.424 1.00 17.31 ? 73  PRO C CA  1 
ATOM   4863 C  C   . PRO C  1 73  ? 55.049  3.196   -30.962 1.00 19.48 ? 73  PRO C C   1 
ATOM   4864 O  O   . PRO C  1 73  ? 54.572  2.164   -31.421 1.00 19.54 ? 73  PRO C O   1 
ATOM   4865 C  CB  . PRO C  1 73  ? 56.208  2.648   -28.757 1.00 19.33 ? 73  PRO C CB  1 
ATOM   4866 C  CG  . PRO C  1 73  ? 55.711  1.224   -28.635 1.00 18.31 ? 73  PRO C CG  1 
ATOM   4867 C  CD  . PRO C  1 73  ? 54.220  1.428   -28.267 1.00 15.63 ? 73  PRO C CD  1 
ATOM   4868 N  N   . SER C  1 74  ? 55.530  4.211   -31.691 1.00 18.92 ? 74  SER C N   1 
ATOM   4869 C  CA  . SER C  1 74  ? 55.418  4.286   -33.152 1.00 21.49 ? 74  SER C CA  1 
ATOM   4870 C  C   . SER C  1 74  ? 56.302  3.255   -33.837 1.00 24.83 ? 74  SER C C   1 
ATOM   4871 O  O   . SER C  1 74  ? 56.155  2.990   -35.031 1.00 23.48 ? 74  SER C O   1 
ATOM   4872 C  CB  . SER C  1 74  ? 55.653  5.724   -33.674 1.00 27.40 ? 74  SER C CB  1 
ATOM   4873 O  OG  . SER C  1 74  ? 56.941  6.223   -33.374 1.00 26.94 ? 74  SER C OG  1 
ATOM   4874 N  N   . ASP C  1 75  ? 57.249  2.660   -33.107 1.00 22.61 ? 75  ASP C N   1 
ATOM   4875 C  CA  . ASP C  1 75  ? 58.033  1.591   -33.744 1.00 23.04 ? 75  ASP C CA  1 
ATOM   4876 C  C   . ASP C  1 75  ? 57.197  0.263   -33.769 1.00 21.83 ? 75  ASP C C   1 
ATOM   4877 O  O   . ASP C  1 75  ? 57.540  -0.704  -34.448 1.00 22.83 ? 75  ASP C O   1 
ATOM   4878 C  CB  . ASP C  1 75  ? 59.432  1.425   -33.094 1.00 28.22 ? 75  ASP C CB  1 
ATOM   4879 C  CG  . ASP C  1 75  ? 59.308  0.966   -31.701 1.00 33.75 ? 75  ASP C CG  1 
ATOM   4880 O  OD1 . ASP C  1 75  ? 58.947  1.830   -30.856 1.00 37.22 ? 75  ASP C OD1 1 
ATOM   4881 O  OD2 . ASP C  1 75  ? 59.520  -0.254  -31.483 1.00 35.91 ? 75  ASP C OD2 1 
ATOM   4882 N  N   . MET C  1 76  ? 56.029  0.218   -33.123 1.00 18.38 ? 76  MET C N   1 
ATOM   4883 C  CA  . MET C  1 76  ? 55.137  -0.925  -33.282 1.00 17.08 ? 76  MET C CA  1 
ATOM   4884 C  C   . MET C  1 76  ? 54.288  -0.769  -34.594 1.00 14.93 ? 76  MET C C   1 
ATOM   4885 O  O   . MET C  1 76  ? 53.859  0.352   -34.842 1.00 15.74 ? 76  MET C O   1 
ATOM   4886 C  CB  . MET C  1 76  ? 54.259  -0.843  -32.073 1.00 21.46 ? 76  MET C CB  1 
ATOM   4887 C  CG  . MET C  1 76  ? 53.186  -1.804  -31.932 1.00 21.52 ? 76  MET C CG  1 
ATOM   4888 S  SD  . MET C  1 76  ? 52.438  -1.679  -30.289 1.00 19.49 ? 76  MET C SD  1 
ATOM   4889 C  CE  . MET C  1 76  ? 50.811  -2.369  -30.810 1.00 16.66 ? 76  MET C CE  1 
ATOM   4890 N  N   . HIS C  1 77  ? 54.224  -1.770  -35.427 1.00 13.00 ? 77  HIS C N   1 
ATOM   4891 C  CA  . HIS C  1 77  ? 53.535  -1.567  -36.761 1.00 16.66 ? 77  HIS C CA  1 
ATOM   4892 C  C   . HIS C  1 77  ? 52.962  -2.797  -37.348 1.00 16.32 ? 77  HIS C C   1 
ATOM   4893 O  O   . HIS C  1 77  ? 53.293  -3.915  -37.045 1.00 14.29 ? 77  HIS C O   1 
ATOM   4894 C  CB  . HIS C  1 77  ? 54.367  -0.777  -37.793 1.00 19.01 ? 77  HIS C CB  1 
ATOM   4895 C  CG  . HIS C  1 77  ? 55.634  -1.490  -38.169 1.00 19.71 ? 77  HIS C CG  1 
ATOM   4896 N  ND1 . HIS C  1 77  ? 56.833  -1.284  -37.529 1.00 21.91 ? 77  HIS C ND1 1 
ATOM   4897 C  CD2 . HIS C  1 77  ? 55.870  -2.420  -39.168 1.00 22.06 ? 77  HIS C CD2 1 
ATOM   4898 C  CE1 . HIS C  1 77  ? 57.752  -2.084  -38.078 1.00 24.23 ? 77  HIS C CE1 1 
ATOM   4899 N  NE2 . HIS C  1 77  ? 57.188  -2.754  -39.114 1.00 24.06 ? 77  HIS C NE2 1 
ATOM   4900 N  N   . ILE C  1 78  ? 51.997  -2.581  -38.247 1.00 15.99 ? 78  ILE C N   1 
ATOM   4901 C  CA  . ILE C  1 78  ? 51.509  -3.648  -39.088 1.00 14.56 ? 78  ILE C CA  1 
ATOM   4902 C  C   . ILE C  1 78  ? 52.247  -3.700  -40.432 1.00 15.13 ? 78  ILE C C   1 
ATOM   4903 O  O   . ILE C  1 78  ? 52.477  -2.667  -41.013 1.00 16.92 ? 78  ILE C O   1 
ATOM   4904 C  CB  . ILE C  1 78  ? 49.984  -3.337  -39.456 1.00 17.24 ? 78  ILE C CB  1 
ATOM   4905 C  CG1 . ILE C  1 78  ? 49.126  -3.268  -38.193 1.00 17.39 ? 78  ILE C CG1 1 
ATOM   4906 C  CG2 . ILE C  1 78  ? 49.452  -4.355  -40.450 1.00 17.70 ? 78  ILE C CG2 1 
ATOM   4907 C  CD1 . ILE C  1 78  ? 47.762  -2.613  -38.451 1.00 17.09 ? 78  ILE C CD1 1 
ATOM   4908 N  N   . GLN C  1 79  ? 52.622  -4.897  -40.845 1.00 17.31 ? 79  GLN C N   1 
ATOM   4909 C  CA  . GLN C  1 79  ? 53.258  -5.192  -42.081 1.00 22.07 ? 79  GLN C CA  1 
ATOM   4910 C  C   . GLN C  1 79  ? 52.253  -6.052  -42.862 1.00 19.54 ? 79  GLN C C   1 
ATOM   4911 O  O   . GLN C  1 79  ? 51.605  -6.951  -42.276 1.00 19.81 ? 79  GLN C O   1 
ATOM   4912 C  CB  . GLN C  1 79  ? 54.499  -6.030  -41.697 1.00 26.56 ? 79  GLN C CB  1 
ATOM   4913 C  CG  . GLN C  1 79  ? 55.163  -6.668  -42.905 1.00 32.91 ? 79  GLN C CG  1 
ATOM   4914 C  CD  . GLN C  1 79  ? 56.189  -5.736  -43.504 1.00 39.93 ? 79  GLN C CD  1 
ATOM   4915 O  OE1 . GLN C  1 79  ? 55.857  -4.645  -43.989 1.00 45.11 ? 79  GLN C OE1 1 
ATOM   4916 N  NE2 . GLN C  1 79  ? 57.457  -6.155  -43.459 1.00 45.33 ? 79  GLN C NE2 1 
ATOM   4917 N  N   . GLY C  1 80  ? 52.088  -5.725  -44.149 1.00 18.14 ? 80  GLY C N   1 
ATOM   4918 C  CA  . GLY C  1 80  ? 51.196  -6.424  -45.082 1.00 19.93 ? 80  GLY C CA  1 
ATOM   4919 C  C   . GLY C  1 80  ? 50.149  -5.574  -45.773 1.00 21.70 ? 80  GLY C C   1 
ATOM   4920 O  O   . GLY C  1 80  ? 49.468  -6.049  -46.718 1.00 24.02 ? 80  GLY C O   1 
ATOM   4921 N  N   . LEU C  1 81  ? 50.011  -4.303  -45.351 1.00 20.56 ? 81  LEU C N   1 
ATOM   4922 C  CA  . LEU C  1 81  ? 49.111  -3.406  -46.012 1.00 20.72 ? 81  LEU C CA  1 
ATOM   4923 C  C   . LEU C  1 81  ? 49.919  -2.599  -47.077 1.00 20.40 ? 81  LEU C C   1 
ATOM   4924 O  O   . LEU C  1 81  ? 51.133  -2.742  -47.125 1.00 23.21 ? 81  LEU C O   1 
ATOM   4925 C  CB  . LEU C  1 81  ? 48.435  -2.487  -45.018 1.00 17.40 ? 81  LEU C CB  1 
ATOM   4926 C  CG  . LEU C  1 81  ? 47.546  -3.175  -43.994 1.00 17.59 ? 81  LEU C CG  1 
ATOM   4927 C  CD1 . LEU C  1 81  ? 47.133  -2.269  -42.855 1.00 17.42 ? 81  LEU C CD1 1 
ATOM   4928 C  CD2 . LEU C  1 81  ? 46.273  -3.697  -44.719 1.00 17.13 ? 81  LEU C CD2 1 
ATOM   4929 N  N   . GLN C  1 82  ? 49.256  -1.749  -47.842 1.00 24.49 ? 82  GLN C N   1 
ATOM   4930 C  CA  . GLN C  1 82  ? 49.965  -1.089  -48.937 1.00 24.07 ? 82  GLN C CA  1 
ATOM   4931 C  C   . GLN C  1 82  ? 50.958  0.000   -48.463 1.00 24.79 ? 82  GLN C C   1 
ATOM   4932 O  O   . GLN C  1 82  ? 51.846  0.366   -49.206 1.00 26.65 ? 82  GLN C O   1 
ATOM   4933 C  CB  . GLN C  1 82  ? 48.982  -0.622  -50.034 1.00 30.01 ? 82  GLN C CB  1 
ATOM   4934 C  CG  . GLN C  1 82  ? 48.449  -1.759  -50.953 1.00 34.18 ? 82  GLN C CG  1 
ATOM   4935 C  CD  . GLN C  1 82  ? 49.412  -2.251  -52.071 1.00 36.67 ? 82  GLN C CD  1 
ATOM   4936 O  OE1 . GLN C  1 82  ? 50.423  -1.633  -52.424 1.00 37.22 ? 82  GLN C OE1 1 
ATOM   4937 N  NE2 . GLN C  1 82  ? 49.081  -3.401  -52.616 1.00 43.69 ? 82  GLN C NE2 1 
ATOM   4938 N  N   . SER C  1 83  ? 50.848  0.475   -47.217 1.00 19.45 ? 83  SER C N   1 
ATOM   4939 C  CA  . SER C  1 83  ? 51.757  1.377   -46.574 1.00 16.42 ? 83  SER C CA  1 
ATOM   4940 C  C   . SER C  1 83  ? 52.005  0.774   -45.201 1.00 17.48 ? 83  SER C C   1 
ATOM   4941 O  O   . SER C  1 83  ? 51.238  -0.053  -44.705 1.00 13.69 ? 83  SER C O   1 
ATOM   4942 C  CB  . SER C  1 83  ? 51.156  2.745   -46.329 1.00 18.77 ? 83  SER C CB  1 
ATOM   4943 O  OG  . SER C  1 83  ? 50.803  3.422   -47.524 1.00 23.34 ? 83  SER C OG  1 
ATOM   4944 N  N   . ARG C  1 84  ? 53.091  1.178   -44.548 1.00 15.12 ? 84  ARG C N   1 
ATOM   4945 C  CA  . ARG C  1 84  ? 53.264  0.929   -43.125 1.00 14.39 ? 84  ARG C CA  1 
ATOM   4946 C  C   . ARG C  1 84  ? 52.334  1.740   -42.293 1.00 12.31 ? 84  ARG C C   1 
ATOM   4947 O  O   . ARG C  1 84  ? 52.209  2.951   -42.442 1.00 13.93 ? 84  ARG C O   1 
ATOM   4948 C  CB  . ARG C  1 84  ? 54.736  1.239   -42.704 1.00 14.12 ? 84  ARG C CB  1 
ATOM   4949 C  CG  . ARG C  1 84  ? 54.925  0.960   -41.179 1.00 15.87 ? 84  ARG C CG  1 
ATOM   4950 C  CD  . ARG C  1 84  ? 56.336  1.181   -40.660 1.00 15.25 ? 84  ARG C CD  1 
ATOM   4951 N  NE  . ARG C  1 84  ? 57.167  0.157   -41.256 1.00 14.79 ? 84  ARG C NE  1 
ATOM   4952 C  CZ  . ARG C  1 84  ? 58.491  0.009   -40.912 1.00 18.86 ? 84  ARG C CZ  1 
ATOM   4953 N  NH1 . ARG C  1 84  ? 59.050  0.912   -40.120 1.00 19.06 ? 84  ARG C NH1 1 
ATOM   4954 N  NH2 . ARG C  1 84  ? 59.190  -0.991  -41.411 1.00 20.87 ? 84  ARG C NH2 1 
ATOM   4955 N  N   . TYR C  1 85  ? 51.658  1.029   -41.339 1.00 13.10 ? 85  TYR C N   1 
ATOM   4956 C  CA  . TYR C  1 85  ? 50.833  1.690   -40.329 1.00 12.70 ? 85  TYR C CA  1 
ATOM   4957 C  C   . TYR C  1 85  ? 51.459  1.430   -39.004 1.00 13.48 ? 85  TYR C C   1 
ATOM   4958 O  O   . TYR C  1 85  ? 51.583  0.275   -38.607 1.00 11.66 ? 85  TYR C O   1 
ATOM   4959 C  CB  . TYR C  1 85  ? 49.399  1.016   -40.414 1.00 12.70 ? 85  TYR C CB  1 
ATOM   4960 C  CG  . TYR C  1 85  ? 48.651  1.603   -41.633 1.00 10.82 ? 85  TYR C CG  1 
ATOM   4961 C  CD1 . TYR C  1 85  ? 47.851  2.740   -41.455 1.00 11.05 ? 85  TYR C CD1 1 
ATOM   4962 C  CD2 . TYR C  1 85  ? 48.707  0.968   -42.865 1.00 12.98 ? 85  TYR C CD2 1 
ATOM   4963 C  CE1 . TYR C  1 85  ? 47.141  3.270   -42.523 1.00 12.93 ? 85  TYR C CE1 1 
ATOM   4964 C  CE2 . TYR C  1 85  ? 48.025  1.527   -43.967 1.00 13.06 ? 85  TYR C CE2 1 
ATOM   4965 C  CZ  . TYR C  1 85  ? 47.231  2.629   -43.757 1.00 12.65 ? 85  TYR C CZ  1 
ATOM   4966 O  OH  . TYR C  1 85  ? 46.540  3.109   -44.905 1.00 15.60 ? 85  TYR C OH  1 
ATOM   4967 N  N   . SER C  1 86  ? 51.832  2.526   -38.329 1.00 13.98 ? 86  SER C N   1 
ATOM   4968 C  CA  . SER C  1 86  ? 52.443  2.513   -36.984 1.00 14.19 ? 86  SER C CA  1 
ATOM   4969 C  C   . SER C  1 86  ? 51.394  2.722   -35.891 1.00 14.45 ? 86  SER C C   1 
ATOM   4970 O  O   . SER C  1 86  ? 50.515  3.600   -36.017 1.00 15.33 ? 86  SER C O   1 
ATOM   4971 C  CB  . SER C  1 86  ? 53.601  3.531   -36.911 1.00 16.98 ? 86  SER C CB  1 
ATOM   4972 O  OG  . SER C  1 86  ? 54.530  3.231   -37.913 1.00 15.88 ? 86  SER C OG  1 
ATOM   4973 N  N   . ALA C  1 87  ? 51.593  2.036   -34.771 1.00 14.81 ? 87  ALA C N   1 
ATOM   4974 C  CA  . ALA C  1 87  ? 50.707  2.190   -33.608 1.00 13.50 ? 87  ALA C CA  1 
ATOM   4975 C  C   . ALA C  1 87  ? 50.697  3.575   -33.018 1.00 14.86 ? 87  ALA C C   1 
ATOM   4976 O  O   . ALA C  1 87  ? 51.740  4.292   -32.997 1.00 14.49 ? 87  ALA C O   1 
ATOM   4977 C  CB  . ALA C  1 87  ? 51.036  1.132   -32.581 1.00 15.08 ? 87  ALA C CB  1 
ATOM   4978 N  N   . THR C  1 88  ? 49.561  3.908   -32.392 1.00 12.73 ? 88  THR C N   1 
ATOM   4979 C  CA  . THR C  1 88  ? 49.411  5.163   -31.647 1.00 14.46 ? 88  THR C CA  1 
ATOM   4980 C  C   . THR C  1 88  ? 48.760  4.902   -30.299 1.00 14.97 ? 88  THR C C   1 
ATOM   4981 O  O   . THR C  1 88  ? 49.244  5.469   -29.308 1.00 13.56 ? 88  THR C O   1 
ATOM   4982 C  CB  . THR C  1 88  ? 48.756  6.313   -32.420 1.00 15.35 ? 88  THR C CB  1 
ATOM   4983 O  OG1 . THR C  1 88  ? 48.689  7.482   -31.576 1.00 15.92 ? 88  THR C OG1 1 
ATOM   4984 C  CG2 . THR C  1 88  ? 47.378  5.970   -33.040 1.00 14.51 ? 88  THR C CG2 1 
ATOM   4985 N  N   . GLN C  1 89  ? 47.716  4.038   -30.201 1.00 14.07 ? 89  GLN C N   1 
ATOM   4986 C  CA  . GLN C  1 89  ? 47.018  3.853   -28.905 1.00 13.47 ? 89  GLN C CA  1 
ATOM   4987 C  C   . GLN C  1 89  ? 46.107  2.642   -29.138 1.00 12.89 ? 89  GLN C C   1 
ATOM   4988 O  O   . GLN C  1 89  ? 45.766  2.320   -30.323 1.00 13.85 ? 89  GLN C O   1 
ATOM   4989 C  CB  . GLN C  1 89  ? 46.266  5.129   -28.476 1.00 16.98 ? 89  GLN C CB  1 
ATOM   4990 C  CG  . GLN C  1 89  ? 45.311  5.669   -29.536 1.00 19.79 ? 89  GLN C CG  1 
ATOM   4991 C  CD  . GLN C  1 89  ? 43.859  5.485   -29.123 1.00 17.47 ? 89  GLN C CD  1 
ATOM   4992 O  OE1 . GLN C  1 89  ? 43.069  6.407   -29.094 1.00 31.58 ? 89  GLN C OE1 1 
ATOM   4993 N  NE2 . GLN C  1 89  ? 43.561  4.344   -28.718 1.00 16.70 ? 89  GLN C NE2 1 
ATOM   4994 N  N   . LEU C  1 90  ? 45.737  2.034   -28.025 1.00 13.97 ? 90  LEU C N   1 
ATOM   4995 C  CA  . LEU C  1 90  ? 44.591  1.186   -28.045 1.00 12.61 ? 90  LEU C CA  1 
ATOM   4996 C  C   . LEU C  1 90  ? 43.600  1.660   -27.031 1.00 13.43 ? 90  LEU C C   1 
ATOM   4997 O  O   . LEU C  1 90  ? 43.938  2.411   -26.076 1.00 14.67 ? 90  LEU C O   1 
ATOM   4998 C  CB  . LEU C  1 90  ? 45.013  -0.256  -27.879 1.00 12.80 ? 90  LEU C CB  1 
ATOM   4999 C  CG  . LEU C  1 90  ? 45.751  -0.629  -26.543 1.00 13.52 ? 90  LEU C CG  1 
ATOM   5000 C  CD1 . LEU C  1 90  ? 44.853  -0.722  -25.278 1.00 14.39 ? 90  LEU C CD1 1 
ATOM   5001 C  CD2 . LEU C  1 90  ? 46.391  -2.004  -26.724 1.00 13.30 ? 90  LEU C CD2 1 
ATOM   5002 N  N   . HIS C  1 91  ? 42.361  1.218   -27.220 1.00 12.02 ? 91  HIS C N   1 
ATOM   5003 C  CA  . HIS C  1 91  ? 41.335  1.480   -26.260 1.00 11.55 ? 91  HIS C CA  1 
ATOM   5004 C  C   . HIS C  1 91  ? 40.196  0.471   -26.419 1.00 10.89 ? 91  HIS C C   1 
ATOM   5005 O  O   . HIS C  1 91  ? 40.250  -0.399  -27.234 1.00 12.28 ? 91  HIS C O   1 
ATOM   5006 C  CB  . HIS C  1 91  ? 40.814  2.910   -26.490 1.00 11.09 ? 91  HIS C CB  1 
ATOM   5007 C  CG  . HIS C  1 91  ? 40.216  3.089   -27.852 1.00 11.83 ? 91  HIS C CG  1 
ATOM   5008 N  ND1 . HIS C  1 91  ? 40.953  3.497   -28.902 1.00 13.20 ? 91  HIS C ND1 1 
ATOM   5009 C  CD2 . HIS C  1 91  ? 38.952  2.812   -28.296 1.00 11.58 ? 91  HIS C CD2 1 
ATOM   5010 C  CE1 . HIS C  1 91  ? 40.206  3.501   -30.018 1.00 11.43 ? 91  HIS C CE1 1 
ATOM   5011 N  NE2 . HIS C  1 91  ? 38.976  2.995   -29.698 1.00 9.86  ? 91  HIS C NE2 1 
ATOM   5012 N  N   . LEU C  1 92  ? 39.164  0.621   -25.565 1.00 12.16 ? 92  LEU C N   1 
ATOM   5013 C  CA  . LEU C  1 92  ? 38.044  -0.314  -25.523 1.00 13.45 ? 92  LEU C CA  1 
ATOM   5014 C  C   . LEU C  1 92  ? 36.706  0.385   -25.577 1.00 9.83  ? 92  LEU C C   1 
ATOM   5015 O  O   . LEU C  1 92  ? 36.524  1.577   -25.307 1.00 11.82 ? 92  LEU C O   1 
ATOM   5016 C  CB  . LEU C  1 92  ? 38.098  -1.282  -24.278 1.00 12.65 ? 92  LEU C CB  1 
ATOM   5017 C  CG  . LEU C  1 92  ? 39.363  -2.140  -24.354 1.00 14.61 ? 92  LEU C CG  1 
ATOM   5018 C  CD1 . LEU C  1 92  ? 40.376  -1.638  -23.368 1.00 19.08 ? 92  LEU C CD1 1 
ATOM   5019 C  CD2 . LEU C  1 92  ? 39.004  -3.527  -24.083 1.00 16.35 ? 92  LEU C CD2 1 
ATOM   5020 N  N   . HIS C  1 93  ? 35.711  -0.438  -25.975 1.00 12.27 ? 93  HIS C N   1 
ATOM   5021 C  CA  . HIS C  1 93  ? 34.306  -0.052  -25.944 1.00 10.61 ? 93  HIS C CA  1 
ATOM   5022 C  C   . HIS C  1 93  ? 33.495  -1.154  -25.260 1.00 10.73 ? 93  HIS C C   1 
ATOM   5023 O  O   . HIS C  1 93  ? 33.707  -2.297  -25.565 1.00 11.10 ? 93  HIS C O   1 
ATOM   5024 C  CB  . HIS C  1 93  ? 33.772  0.152   -27.439 1.00 11.03 ? 93  HIS C CB  1 
ATOM   5025 C  CG  . HIS C  1 93  ? 34.540  1.164   -28.206 1.00 8.66  ? 93  HIS C CG  1 
ATOM   5026 N  ND1 . HIS C  1 93  ? 34.249  2.474   -28.187 1.00 11.26 ? 93  HIS C ND1 1 
ATOM   5027 C  CD2 . HIS C  1 93  ? 35.657  0.998   -29.043 1.00 9.89  ? 93  HIS C CD2 1 
ATOM   5028 C  CE1 . HIS C  1 93  ? 35.154  3.131   -29.012 1.00 9.61  ? 93  HIS C CE1 1 
ATOM   5029 N  NE2 . HIS C  1 93  ? 35.955  2.222   -29.537 1.00 8.70  ? 93  HIS C NE2 1 
ATOM   5030 N  N   . TRP C  1 94  ? 32.568  -0.762  -24.361 1.00 11.94 ? 94  TRP C N   1 
ATOM   5031 C  CA  . TRP C  1 94  ? 31.749  -1.759  -23.679 1.00 11.79 ? 94  TRP C CA  1 
ATOM   5032 C  C   . TRP C  1 94  ? 30.313  -1.228  -23.451 1.00 10.67 ? 94  TRP C C   1 
ATOM   5033 O  O   . TRP C  1 94  ? 29.940  -0.082  -23.815 1.00 11.27 ? 94  TRP C O   1 
ATOM   5034 C  CB  . TRP C  1 94  ? 32.540  -2.145  -22.352 1.00 13.02 ? 94  TRP C CB  1 
ATOM   5035 C  CG  . TRP C  1 94  ? 32.805  -0.965  -21.448 1.00 14.62 ? 94  TRP C CG  1 
ATOM   5036 C  CD1 . TRP C  1 94  ? 31.976  -0.456  -20.452 1.00 14.44 ? 94  TRP C CD1 1 
ATOM   5037 C  CD2 . TRP C  1 94  ? 33.996  -0.102  -21.428 1.00 12.99 ? 94  TRP C CD2 1 
ATOM   5038 N  NE1 . TRP C  1 94  ? 32.555  0.626   -19.839 1.00 13.04 ? 94  TRP C NE1 1 
ATOM   5039 C  CE2 . TRP C  1 94  ? 33.766  0.891   -20.376 1.00 13.58 ? 94  TRP C CE2 1 
ATOM   5040 C  CE3 . TRP C  1 94  ? 35.180  -0.055  -22.149 1.00 14.61 ? 94  TRP C CE3 1 
ATOM   5041 C  CZ2 . TRP C  1 94  ? 34.694  1.874   -20.079 1.00 15.49 ? 94  TRP C CZ2 1 
ATOM   5042 C  CZ3 . TRP C  1 94  ? 36.108  0.942   -21.838 1.00 13.35 ? 94  TRP C CZ3 1 
ATOM   5043 C  CH2 . TRP C  1 94  ? 35.869  1.881   -20.828 1.00 15.43 ? 94  TRP C CH2 1 
ATOM   5044 N  N   . GLY C  1 95  ? 29.547  -2.111  -22.769 1.00 12.94 ? 95  GLY C N   1 
ATOM   5045 C  CA  . GLY C  1 95  ? 28.162  -1.765  -22.446 1.00 14.04 ? 95  GLY C CA  1 
ATOM   5046 C  C   . GLY C  1 95  ? 27.993  -1.452  -20.936 1.00 12.99 ? 95  GLY C C   1 
ATOM   5047 O  O   . GLY C  1 95  ? 28.651  -0.528  -20.379 1.00 13.53 ? 95  GLY C O   1 
ATOM   5048 N  N   . ASN C  1 96  ? 27.009  -2.132  -20.347 1.00 15.75 ? 96  ASN C N   1 
ATOM   5049 C  CA  . ASN C  1 96  ? 26.809  -1.923  -18.880 1.00 14.64 ? 96  ASN C CA  1 
ATOM   5050 C  C   . ASN C  1 96  ? 26.429  -3.246  -18.241 1.00 16.12 ? 96  ASN C C   1 
ATOM   5051 O  O   . ASN C  1 96  ? 26.060  -4.187  -18.881 1.00 17.34 ? 96  ASN C O   1 
ATOM   5052 C  CB  . ASN C  1 96  ? 25.821  -0.798  -18.626 1.00 17.63 ? 96  ASN C CB  1 
ATOM   5053 C  CG  . ASN C  1 96  ? 24.413  -1.183  -18.976 1.00 21.97 ? 96  ASN C CG  1 
ATOM   5054 O  OD1 . ASN C  1 96  ? 23.710  -1.776  -18.136 1.00 24.99 ? 96  ASN C OD1 1 
ATOM   5055 N  ND2 . ASN C  1 96  ? 23.959  -0.821  -20.160 1.00 26.36 ? 96  ASN C ND2 1 
ATOM   5056 N  N   . PRO C  1 97  ? 26.391  -3.300  -16.897 1.00 19.56 ? 97  PRO C N   1 
ATOM   5057 C  CA  . PRO C  1 97  ? 26.136  -4.653  -16.320 1.00 16.24 ? 97  PRO C CA  1 
ATOM   5058 C  C   . PRO C  1 97  ? 24.703  -5.238  -16.545 1.00 17.98 ? 97  PRO C C   1 
ATOM   5059 O  O   . PRO C  1 97  ? 24.543  -6.459  -16.513 1.00 20.24 ? 97  PRO C O   1 
ATOM   5060 C  CB  . PRO C  1 97  ? 26.476  -4.474  -14.823 1.00 20.12 ? 97  PRO C CB  1 
ATOM   5061 C  CG  . PRO C  1 97  ? 27.277  -3.200  -14.803 1.00 18.73 ? 97  PRO C CG  1 
ATOM   5062 C  CD  . PRO C  1 97  ? 26.845  -2.296  -15.905 1.00 18.99 ? 97  PRO C CD  1 
ATOM   5063 N  N   . ASN C  1 98  ? 23.776  -4.343  -16.757 1.00 17.64 ? 98  ASN C N   1 
ATOM   5064 C  CA  . ASN C  1 98  ? 22.365  -4.716  -17.078 1.00 21.73 ? 98  ASN C CA  1 
ATOM   5065 C  C   . ASN C  1 98  ? 22.122  -5.073  -18.535 1.00 21.44 ? 98  ASN C C   1 
ATOM   5066 O  O   . ASN C  1 98  ? 21.080  -5.615  -18.841 1.00 23.00 ? 98  ASN C O   1 
ATOM   5067 C  CB  . ASN C  1 98  ? 21.464  -3.551  -16.739 1.00 21.73 ? 98  ASN C CB  1 
ATOM   5068 C  CG  . ASN C  1 98  ? 21.310  -3.388  -15.241 1.00 26.70 ? 98  ASN C CG  1 
ATOM   5069 O  OD1 . ASN C  1 98  ? 21.377  -4.364  -14.491 1.00 31.32 ? 98  ASN C OD1 1 
ATOM   5070 N  ND2 . ASN C  1 98  ? 21.146  -2.160  -14.808 1.00 36.52 ? 98  ASN C ND2 1 
ATOM   5071 N  N   . ASP C  1 99  ? 23.069  -4.718  -19.423 1.00 21.04 ? 99  ASP C N   1 
ATOM   5072 C  CA  . ASP C  1 99  ? 23.025  -5.077  -20.885 1.00 17.05 ? 99  ASP C CA  1 
ATOM   5073 C  C   . ASP C  1 99  ? 24.490  -5.189  -21.357 1.00 15.43 ? 99  ASP C C   1 
ATOM   5074 O  O   . ASP C  1 99  ? 24.983  -4.225  -21.991 1.00 15.54 ? 99  ASP C O   1 
ATOM   5075 C  CB  . ASP C  1 99  ? 22.280  -3.965  -21.631 1.00 17.32 ? 99  ASP C CB  1 
ATOM   5076 C  CG  . ASP C  1 99  ? 21.737  -4.423  -23.001 1.00 17.14 ? 99  ASP C CG  1 
ATOM   5077 O  OD1 . ASP C  1 99  ? 21.790  -5.613  -23.265 1.00 18.32 ? 99  ASP C OD1 1 
ATOM   5078 O  OD2 . ASP C  1 99  ? 21.415  -3.555  -23.824 1.00 21.73 ? 99  ASP C OD2 1 
ATOM   5079 N  N   . PRO C  1 100 ? 25.126  -6.303  -21.082 1.00 13.30 ? 100 PRO C N   1 
ATOM   5080 C  CA  . PRO C  1 100 ? 26.584  -6.408  -21.229 1.00 14.99 ? 100 PRO C CA  1 
ATOM   5081 C  C   . PRO C  1 100 ? 26.977  -6.801  -22.658 1.00 14.86 ? 100 PRO C C   1 
ATOM   5082 O  O   . PRO C  1 100 ? 27.585  -7.815  -22.921 1.00 15.87 ? 100 PRO C O   1 
ATOM   5083 C  CB  . PRO C  1 100 ? 26.983  -7.456  -20.217 1.00 16.39 ? 100 PRO C CB  1 
ATOM   5084 C  CG  . PRO C  1 100 ? 25.773  -8.369  -20.083 1.00 17.67 ? 100 PRO C CG  1 
ATOM   5085 C  CD  . PRO C  1 100 ? 24.596  -7.456  -20.311 1.00 16.31 ? 100 PRO C CD  1 
ATOM   5086 N  N   . HIS C  1 101 ? 26.575  -5.933  -23.609 1.00 13.20 ? 101 HIS C N   1 
ATOM   5087 C  CA  . HIS C  1 101 ? 26.781  -6.238  -25.066 1.00 13.28 ? 101 HIS C CA  1 
ATOM   5088 C  C   . HIS C  1 101 ? 27.082  -4.946  -25.748 1.00 15.87 ? 101 HIS C C   1 
ATOM   5089 O  O   . HIS C  1 101 ? 26.245  -4.466  -26.478 1.00 16.62 ? 101 HIS C O   1 
ATOM   5090 C  CB  . HIS C  1 101 ? 25.481  -6.800  -25.681 1.00 15.32 ? 101 HIS C CB  1 
ATOM   5091 C  CG  . HIS C  1 101 ? 24.876  -7.943  -24.871 1.00 16.82 ? 101 HIS C CG  1 
ATOM   5092 N  ND1 . HIS C  1 101 ? 25.418  -9.195  -24.805 1.00 16.83 ? 101 HIS C ND1 1 
ATOM   5093 C  CD2 . HIS C  1 101 ? 23.839  -7.913  -23.924 1.00 16.37 ? 101 HIS C CD2 1 
ATOM   5094 C  CE1 . HIS C  1 101 ? 24.702  -9.921  -23.904 1.00 19.49 ? 101 HIS C CE1 1 
ATOM   5095 N  NE2 . HIS C  1 101 ? 23.740  -9.133  -23.405 1.00 18.19 ? 101 HIS C NE2 1 
ATOM   5096 N  N   . GLY C  1 102 ? 28.328  -4.496  -25.596 1.00 12.96 ? 102 GLY C N   1 
ATOM   5097 C  CA  . GLY C  1 102 ? 28.777  -3.220  -26.023 1.00 13.05 ? 102 GLY C CA  1 
ATOM   5098 C  C   . GLY C  1 102 ? 29.948  -3.196  -27.014 1.00 9.59  ? 102 GLY C C   1 
ATOM   5099 O  O   . GLY C  1 102 ? 30.563  -2.143  -27.110 1.00 11.08 ? 102 GLY C O   1 
ATOM   5100 N  N   . SER C  1 103 ? 30.013  -4.217  -27.842 1.00 10.03 ? 103 SER C N   1 
ATOM   5101 C  CA  . SER C  1 103 ? 30.898  -4.078  -28.997 1.00 10.34 ? 103 SER C CA  1 
ATOM   5102 C  C   . SER C  1 103 ? 30.343  -3.011  -29.942 1.00 10.77 ? 103 SER C C   1 
ATOM   5103 O  O   . SER C  1 103 ? 29.126  -2.631  -29.912 1.00 10.73 ? 103 SER C O   1 
ATOM   5104 C  CB  . SER C  1 103 ? 31.057  -5.395  -29.707 1.00 10.01 ? 103 SER C CB  1 
ATOM   5105 O  OG  . SER C  1 103 ? 29.818  -5.821  -30.394 1.00 10.35 ? 103 SER C OG  1 
ATOM   5106 N  N   . GLU C  1 104 ? 31.217  -2.535  -30.822 1.00 9.59  ? 104 GLU C N   1 
ATOM   5107 C  CA  . GLU C  1 104 ? 30.794  -1.607  -31.835 1.00 9.40  ? 104 GLU C CA  1 
ATOM   5108 C  C   . GLU C  1 104 ? 30.303  -2.305  -33.070 1.00 10.87 ? 104 GLU C C   1 
ATOM   5109 O  O   . GLU C  1 104 ? 29.133  -2.113  -33.518 1.00 8.57  ? 104 GLU C O   1 
ATOM   5110 C  CB  . GLU C  1 104 ? 31.919  -0.601  -32.176 1.00 9.43  ? 104 GLU C CB  1 
ATOM   5111 C  CG  . GLU C  1 104 ? 32.491  0.091   -30.914 1.00 10.43 ? 104 GLU C CG  1 
ATOM   5112 C  CD  . GLU C  1 104 ? 32.778  1.541   -31.220 1.00 9.74  ? 104 GLU C CD  1 
ATOM   5113 O  OE1 . GLU C  1 104 ? 33.845  1.763   -31.870 1.00 10.57 ? 104 GLU C OE1 1 
ATOM   5114 O  OE2 . GLU C  1 104 ? 32.000  2.475   -30.986 1.00 10.06 ? 104 GLU C OE2 1 
ATOM   5115 N  N   . HIS C  1 105 ? 31.129  -3.113  -33.720 1.00 8.62  ? 105 HIS C N   1 
ATOM   5116 C  CA  . HIS C  1 105 ? 30.685  -4.011  -34.803 1.00 8.14  ? 105 HIS C CA  1 
ATOM   5117 C  C   . HIS C  1 105 ? 29.788  -5.062  -34.272 1.00 8.80  ? 105 HIS C C   1 
ATOM   5118 O  O   . HIS C  1 105 ? 29.926  -5.527  -33.126 1.00 10.07 ? 105 HIS C O   1 
ATOM   5119 C  CB  . HIS C  1 105 ? 31.916  -4.582  -35.541 1.00 8.54  ? 105 HIS C CB  1 
ATOM   5120 C  CG  . HIS C  1 105 ? 32.665  -3.543  -36.244 1.00 8.63  ? 105 HIS C CG  1 
ATOM   5121 N  ND1 . HIS C  1 105 ? 33.693  -2.846  -35.644 1.00 8.39  ? 105 HIS C ND1 1 
ATOM   5122 C  CD2 . HIS C  1 105 ? 32.488  -3.035  -37.492 1.00 7.57  ? 105 HIS C CD2 1 
ATOM   5123 C  CE1 . HIS C  1 105 ? 34.149  -1.908  -36.544 1.00 8.52  ? 105 HIS C CE1 1 
ATOM   5124 N  NE2 . HIS C  1 105 ? 33.427  -2.067  -37.699 1.00 8.73  ? 105 HIS C NE2 1 
ATOM   5125 N  N   . THR C  1 106 ? 28.831  -5.439  -35.086 1.00 8.34  ? 106 THR C N   1 
ATOM   5126 C  CA  . THR C  1 106 ? 28.013  -6.620  -34.748 1.00 9.48  ? 106 THR C CA  1 
ATOM   5127 C  C   . THR C  1 106 ? 28.183  -7.661  -35.848 1.00 10.24 ? 106 THR C C   1 
ATOM   5128 O  O   . THR C  1 106 ? 28.605  -7.370  -36.976 1.00 9.40  ? 106 THR C O   1 
ATOM   5129 C  CB  . THR C  1 106 ? 26.503  -6.187  -34.637 1.00 9.64  ? 106 THR C CB  1 
ATOM   5130 O  OG1 . THR C  1 106 ? 26.076  -5.565  -35.865 1.00 10.46 ? 106 THR C OG1 1 
ATOM   5131 C  CG2 . THR C  1 106 ? 26.327  -5.198  -33.546 1.00 10.34 ? 106 THR C CG2 1 
ATOM   5132 N  N   . VAL C  1 107 ? 27.821  -8.907  -35.509 1.00 11.07 ? 107 VAL C N   1 
ATOM   5133 C  CA  . VAL C  1 107 ? 27.906  -9.956  -36.478 1.00 11.28 ? 107 VAL C CA  1 
ATOM   5134 C  C   . VAL C  1 107 ? 26.489  -10.592 -36.554 1.00 12.10 ? 107 VAL C C   1 
ATOM   5135 O  O   . VAL C  1 107 ? 25.982  -11.060 -35.506 1.00 12.04 ? 107 VAL C O   1 
ATOM   5136 C  CB  . VAL C  1 107 ? 28.950  -11.003 -36.021 1.00 14.69 ? 107 VAL C CB  1 
ATOM   5137 C  CG1 . VAL C  1 107 ? 29.007  -12.129 -37.045 1.00 14.28 ? 107 VAL C CG1 1 
ATOM   5138 C  CG2 . VAL C  1 107 ? 30.362  -10.316 -35.793 1.00 13.91 ? 107 VAL C CG2 1 
ATOM   5139 N  N   . SER C  1 108 ? 25.913  -10.565 -37.747 1.00 11.31 ? 108 SER C N   1 
ATOM   5140 C  CA  . SER C  1 108 ? 24.521  -11.058 -37.986 1.00 13.32 ? 108 SER C CA  1 
ATOM   5141 C  C   . SER C  1 108 ? 23.575  -10.454 -36.957 1.00 12.01 ? 108 SER C C   1 
ATOM   5142 O  O   . SER C  1 108 ? 22.755  -11.138 -36.340 1.00 12.60 ? 108 SER C O   1 
ATOM   5143 C  CB  . SER C  1 108 ? 24.450  -12.609 -37.871 1.00 14.16 ? 108 SER C CB  1 
ATOM   5144 O  OG  . SER C  1 108 ? 25.372  -13.182 -38.728 1.00 19.34 ? 108 SER C OG  1 
ATOM   5145 N  N   . GLY C  1 109 ? 23.785  -9.165  -36.705 1.00 10.95 ? 109 GLY C N   1 
ATOM   5146 C  CA  . GLY C  1 109 ? 22.944  -8.429  -35.841 1.00 12.41 ? 109 GLY C CA  1 
ATOM   5147 C  C   . GLY C  1 109 ? 23.278  -8.459  -34.355 1.00 12.90 ? 109 GLY C C   1 
ATOM   5148 O  O   . GLY C  1 109 ? 22.648  -7.766  -33.568 1.00 15.31 ? 109 GLY C O   1 
ATOM   5149 N  N   . GLN C  1 110 ? 24.257  -9.271  -33.951 1.00 12.71 ? 110 GLN C N   1 
ATOM   5150 C  CA  . GLN C  1 110 ? 24.522  -9.563  -32.538 1.00 13.47 ? 110 GLN C CA  1 
ATOM   5151 C  C   . GLN C  1 110 ? 25.769  -8.758  -32.063 1.00 11.52 ? 110 GLN C C   1 
ATOM   5152 O  O   . GLN C  1 110 ? 26.809  -8.803  -32.753 1.00 11.45 ? 110 GLN C O   1 
ATOM   5153 C  CB  . GLN C  1 110 ? 24.837  -11.090 -32.348 1.00 15.30 ? 110 GLN C CB  1 
ATOM   5154 C  CG  . GLN C  1 110 ? 23.734  -11.967 -32.960 1.00 15.92 ? 110 GLN C CG  1 
ATOM   5155 C  CD  . GLN C  1 110 ? 22.325  -11.527 -32.529 1.00 15.77 ? 110 GLN C CD  1 
ATOM   5156 O  OE1 . GLN C  1 110 ? 21.483  -11.244 -33.450 1.00 21.74 ? 110 GLN C OE1 1 
ATOM   5157 N  NE2 . GLN C  1 110 ? 22.074  -11.397 -31.245 1.00 15.54 ? 110 GLN C NE2 1 
ATOM   5158 N  N   . HIS C  1 111 ? 25.609  -8.038  -30.938 1.00 13.43 ? 111 HIS C N   1 
ATOM   5159 C  CA  . HIS C  1 111 ? 26.753  -7.433  -30.258 1.00 12.13 ? 111 HIS C CA  1 
ATOM   5160 C  C   . HIS C  1 111 ? 27.577  -8.480  -29.557 1.00 13.08 ? 111 HIS C C   1 
ATOM   5161 O  O   . HIS C  1 111 ? 27.021  -9.485  -29.060 1.00 16.80 ? 111 HIS C O   1 
ATOM   5162 C  CB  . HIS C  1 111 ? 26.337  -6.421  -29.196 1.00 12.70 ? 111 HIS C CB  1 
ATOM   5163 C  CG  . HIS C  1 111 ? 25.881  -5.156  -29.765 1.00 12.28 ? 111 HIS C CG  1 
ATOM   5164 N  ND1 . HIS C  1 111 ? 26.690  -4.062  -29.945 1.00 11.59 ? 111 HIS C ND1 1 
ATOM   5165 C  CD2 . HIS C  1 111 ? 24.656  -4.821  -30.300 1.00 12.75 ? 111 HIS C CD2 1 
ATOM   5166 C  CE1 . HIS C  1 111 ? 25.955  -3.092  -30.499 1.00 10.63 ? 111 HIS C CE1 1 
ATOM   5167 N  NE2 . HIS C  1 111 ? 24.704  -3.554  -30.661 1.00 15.14 ? 111 HIS C NE2 1 
ATOM   5168 N  N   . PHE C  1 112 ? 28.856  -8.270  -29.515 1.00 12.11 ? 112 PHE C N   1 
ATOM   5169 C  CA  . PHE C  1 112 ? 29.710  -8.906  -28.501 1.00 13.06 ? 112 PHE C CA  1 
ATOM   5170 C  C   . PHE C  1 112 ? 29.734  -8.143  -27.220 1.00 12.07 ? 112 PHE C C   1 
ATOM   5171 O  O   . PHE C  1 112 ? 29.226  -7.030  -27.175 1.00 11.92 ? 112 PHE C O   1 
ATOM   5172 C  CB  . PHE C  1 112 ? 31.097  -9.168  -29.109 1.00 14.10 ? 112 PHE C CB  1 
ATOM   5173 C  CG  . PHE C  1 112 ? 31.096  -10.341 -30.062 1.00 15.56 ? 112 PHE C CG  1 
ATOM   5174 C  CD1 . PHE C  1 112 ? 30.516  -10.298 -31.393 1.00 15.53 ? 112 PHE C CD1 1 
ATOM   5175 C  CD2 . PHE C  1 112 ? 31.603  -11.558 -29.627 1.00 16.84 ? 112 PHE C CD2 1 
ATOM   5176 C  CE1 . PHE C  1 112 ? 30.529  -11.470 -32.217 1.00 19.42 ? 112 PHE C CE1 1 
ATOM   5177 C  CE2 . PHE C  1 112 ? 31.616  -12.692 -30.413 1.00 18.84 ? 112 PHE C CE2 1 
ATOM   5178 C  CZ  . PHE C  1 112 ? 31.069  -12.683 -31.682 1.00 19.44 ? 112 PHE C CZ  1 
ATOM   5179 N  N   . ALA C  1 113 ? 30.380  -8.688  -26.117 1.00 12.23 ? 113 ALA C N   1 
ATOM   5180 C  CA  . ALA C  1 113 ? 30.415  -7.981  -24.856 1.00 13.27 ? 113 ALA C CA  1 
ATOM   5181 C  C   . ALA C  1 113 ? 31.120  -6.662  -24.892 1.00 10.85 ? 113 ALA C C   1 
ATOM   5182 O  O   . ALA C  1 113 ? 30.694  -5.693  -24.274 1.00 13.56 ? 113 ALA C O   1 
ATOM   5183 C  CB  . ALA C  1 113 ? 31.033  -8.845  -23.761 1.00 14.64 ? 113 ALA C CB  1 
ATOM   5184 N  N   . ALA C  1 114 ? 32.260  -6.606  -25.625 1.00 11.37 ? 114 ALA C N   1 
ATOM   5185 C  CA  . ALA C  1 114 ? 33.079  -5.429  -25.690 1.00 11.07 ? 114 ALA C CA  1 
ATOM   5186 C  C   . ALA C  1 114 ? 33.966  -5.557  -26.961 1.00 10.35 ? 114 ALA C C   1 
ATOM   5187 O  O   . ALA C  1 114 ? 33.859  -6.502  -27.693 1.00 11.30 ? 114 ALA C O   1 
ATOM   5188 C  CB  . ALA C  1 114 ? 33.946  -5.382  -24.411 1.00 12.92 ? 114 ALA C CB  1 
ATOM   5189 N  N   . GLU C  1 115 ? 34.712  -4.507  -27.256 1.00 10.71 ? 115 GLU C N   1 
ATOM   5190 C  CA  . GLU C  1 115 ? 35.525  -4.533  -28.463 1.00 11.65 ? 115 GLU C CA  1 
ATOM   5191 C  C   . GLU C  1 115 ? 36.810  -3.717  -28.116 1.00 9.55  ? 115 GLU C C   1 
ATOM   5192 O  O   . GLU C  1 115 ? 36.792  -2.588  -27.514 1.00 10.79 ? 115 GLU C O   1 
ATOM   5193 C  CB  . GLU C  1 115 ? 34.747  -3.891  -29.618 1.00 10.14 ? 115 GLU C CB  1 
ATOM   5194 C  CG  . GLU C  1 115 ? 35.446  -4.034  -30.997 1.00 9.81  ? 115 GLU C CG  1 
ATOM   5195 C  CD  . GLU C  1 115 ? 34.512  -3.632  -32.124 1.00 10.13 ? 115 GLU C CD  1 
ATOM   5196 O  OE1 . GLU C  1 115 ? 35.043  -3.187  -33.154 1.00 10.32 ? 115 GLU C OE1 1 
ATOM   5197 O  OE2 . GLU C  1 115 ? 33.297  -3.942  -32.016 1.00 10.96 ? 115 GLU C OE2 1 
ATOM   5198 N  N   . LEU C  1 116 ? 37.958  -4.313  -28.535 1.00 11.36 ? 116 LEU C N   1 
ATOM   5199 C  CA  . LEU C  1 116 ? 39.241  -3.623  -28.415 1.00 11.20 ? 116 LEU C CA  1 
ATOM   5200 C  C   . LEU C  1 116 ? 39.699  -3.031  -29.802 1.00 9.44  ? 116 LEU C C   1 
ATOM   5201 O  O   . LEU C  1 116 ? 39.550  -3.808  -30.834 1.00 11.37 ? 116 LEU C O   1 
ATOM   5202 C  CB  . LEU C  1 116 ? 40.289  -4.642  -27.944 1.00 12.35 ? 116 LEU C CB  1 
ATOM   5203 C  CG  . LEU C  1 116 ? 41.761  -4.181  -28.007 1.00 12.79 ? 116 LEU C CG  1 
ATOM   5204 C  CD1 . LEU C  1 116 ? 42.088  -3.224  -26.876 1.00 15.36 ? 116 LEU C CD1 1 
ATOM   5205 C  CD2 . LEU C  1 116 ? 42.686  -5.349  -28.242 1.00 13.84 ? 116 LEU C CD2 1 
ATOM   5206 N  N   . HIS C  1 117 ? 40.180  -1.801  -29.789 1.00 11.14 ? 117 HIS C N   1 
ATOM   5207 C  CA  . HIS C  1 117 ? 40.691  -1.161  -31.019 1.00 9.75  ? 117 HIS C CA  1 
ATOM   5208 C  C   . HIS C  1 117 ? 42.168  -0.914  -30.796 1.00 10.70 ? 117 HIS C C   1 
ATOM   5209 O  O   . HIS C  1 117 ? 42.506  -0.206  -29.872 1.00 11.40 ? 117 HIS C O   1 
ATOM   5210 C  CB  . HIS C  1 117 ? 39.912  0.112   -31.318 1.00 10.86 ? 117 HIS C CB  1 
ATOM   5211 C  CG  . HIS C  1 117 ? 38.524  -0.177  -31.797 1.00 9.59  ? 117 HIS C CG  1 
ATOM   5212 N  ND1 . HIS C  1 117 ? 37.543  0.776   -31.629 1.00 10.68 ? 117 HIS C ND1 1 
ATOM   5213 C  CD2 . HIS C  1 117 ? 38.005  -1.349  -32.364 1.00 11.37 ? 117 HIS C CD2 1 
ATOM   5214 C  CE1 . HIS C  1 117 ? 36.374  0.136   -32.209 1.00 10.96 ? 117 HIS C CE1 1 
ATOM   5215 N  NE2 . HIS C  1 117 ? 36.665  -1.106  -32.625 1.00 10.07 ? 117 HIS C NE2 1 
ATOM   5216 N  N   . ILE C  1 118 ? 42.944  -1.288  -31.781 1.00 10.43 ? 118 ILE C N   1 
ATOM   5217 C  CA  . ILE C  1 118 ? 44.392  -0.911  -31.782 1.00 11.96 ? 118 ILE C CA  1 
ATOM   5218 C  C   . ILE C  1 118 ? 44.627  -0.006  -32.977 1.00 9.31  ? 118 ILE C C   1 
ATOM   5219 O  O   . ILE C  1 118 ? 44.481  -0.494  -34.179 1.00 10.08 ? 118 ILE C O   1 
ATOM   5220 C  CB  . ILE C  1 118 ? 45.275  -2.162  -31.917 1.00 13.47 ? 118 ILE C CB  1 
ATOM   5221 C  CG1 . ILE C  1 118 ? 44.907  -3.234  -30.875 1.00 14.90 ? 118 ILE C CG1 1 
ATOM   5222 C  CG2 . ILE C  1 118 ? 46.762  -1.663  -31.733 1.00 13.06 ? 118 ILE C CG2 1 
ATOM   5223 C  CD1 . ILE C  1 118 ? 45.826  -4.438  -30.913 1.00 16.69 ? 118 ILE C CD1 1 
ATOM   5224 N  N   . VAL C  1 119 ? 44.819  1.284   -32.709 1.00 11.11 ? 119 VAL C N   1 
ATOM   5225 C  CA  . VAL C  1 119 ? 44.719  2.332   -33.724 1.00 10.23 ? 119 VAL C CA  1 
ATOM   5226 C  C   . VAL C  1 119 ? 46.126  2.558   -34.226 1.00 12.66 ? 119 VAL C C   1 
ATOM   5227 O  O   . VAL C  1 119 ? 47.117  2.708   -33.430 1.00 11.93 ? 119 VAL C O   1 
ATOM   5228 C  CB  . VAL C  1 119 ? 44.238  3.656   -33.103 1.00 10.42 ? 119 VAL C CB  1 
ATOM   5229 C  CG1 . VAL C  1 119 ? 44.169  4.717   -34.209 1.00 12.51 ? 119 VAL C CG1 1 
ATOM   5230 C  CG2 . VAL C  1 119 ? 42.858  3.467   -32.371 1.00 12.71 ? 119 VAL C CG2 1 
ATOM   5231 N  N   . HIS C  1 120 ? 46.272  2.519   -35.546 1.00 11.52 ? 120 HIS C N   1 
ATOM   5232 C  CA  . HIS C  1 120 ? 47.581  2.786   -36.276 1.00 12.26 ? 120 HIS C CA  1 
ATOM   5233 C  C   . HIS C  1 120 ? 47.398  3.917   -37.270 1.00 12.82 ? 120 HIS C C   1 
ATOM   5234 O  O   . HIS C  1 120 ? 46.300  4.191   -37.723 1.00 10.58 ? 120 HIS C O   1 
ATOM   5235 C  CB  . HIS C  1 120 ? 48.017  1.552   -37.040 1.00 12.57 ? 120 HIS C CB  1 
ATOM   5236 C  CG  . HIS C  1 120 ? 48.204  0.328   -36.224 1.00 12.27 ? 120 HIS C CG  1 
ATOM   5237 N  ND1 . HIS C  1 120 ? 47.148  -0.346  -35.653 1.00 11.70 ? 120 HIS C ND1 1 
ATOM   5238 C  CD2 . HIS C  1 120 ? 49.354  -0.380  -35.885 1.00 13.48 ? 120 HIS C CD2 1 
ATOM   5239 C  CE1 . HIS C  1 120 ? 47.605  -1.486  -35.096 1.00 10.98 ? 120 HIS C CE1 1 
ATOM   5240 N  NE2 . HIS C  1 120 ? 48.968  -1.484  -35.171 1.00 12.35 ? 120 HIS C NE2 1 
ATOM   5241 N  N   . TYR C  1 121 ? 48.503  4.583   -37.676 1.00 12.12 ? 121 TYR C N   1 
ATOM   5242 C  CA  . TYR C  1 121 ? 48.440  5.661   -38.612 1.00 14.62 ? 121 TYR C CA  1 
ATOM   5243 C  C   . TYR C  1 121 ? 49.434  5.372   -39.696 1.00 13.36 ? 121 TYR C C   1 
ATOM   5244 O  O   . TYR C  1 121 ? 50.443  4.680   -39.474 1.00 13.35 ? 121 TYR C O   1 
ATOM   5245 C  CB  . TYR C  1 121 ? 48.738  7.007   -37.912 1.00 14.68 ? 121 TYR C CB  1 
ATOM   5246 C  CG  . TYR C  1 121 ? 50.136  7.216   -37.430 1.00 15.61 ? 121 TYR C CG  1 
ATOM   5247 C  CD1 . TYR C  1 121 ? 50.597  6.690   -36.186 1.00 14.51 ? 121 TYR C CD1 1 
ATOM   5248 C  CD2 . TYR C  1 121 ? 51.011  8.022   -38.208 1.00 15.14 ? 121 TYR C CD2 1 
ATOM   5249 C  CE1 . TYR C  1 121 ? 51.890  6.912   -35.756 1.00 16.59 ? 121 TYR C CE1 1 
ATOM   5250 C  CE2 . TYR C  1 121 ? 52.349  8.209   -37.793 1.00 14.76 ? 121 TYR C CE2 1 
ATOM   5251 C  CZ  . TYR C  1 121 ? 52.752  7.663   -36.592 1.00 18.75 ? 121 TYR C CZ  1 
ATOM   5252 O  OH  . TYR C  1 121 ? 54.058  7.832   -36.119 1.00 21.04 ? 121 TYR C OH  1 
ATOM   5253 N  N   . ASN C  1 122 ? 49.193  5.954   -40.843 1.00 13.67 ? 122 ASN C N   1 
ATOM   5254 C  CA  . ASN C  1 122 ? 50.069  5.736   -42.012 1.00 12.97 ? 122 ASN C CA  1 
ATOM   5255 C  C   . ASN C  1 122 ? 51.336  6.587   -41.887 1.00 13.59 ? 122 ASN C C   1 
ATOM   5256 O  O   . ASN C  1 122 ? 51.290  7.783   -42.148 1.00 15.66 ? 122 ASN C O   1 
ATOM   5257 C  CB  . ASN C  1 122 ? 49.296  6.172   -43.238 1.00 15.60 ? 122 ASN C CB  1 
ATOM   5258 C  CG  . ASN C  1 122 ? 49.974  5.780   -44.503 1.00 15.80 ? 122 ASN C CG  1 
ATOM   5259 O  OD1 . ASN C  1 122 ? 51.245  5.764   -44.564 1.00 14.85 ? 122 ASN C OD1 1 
ATOM   5260 N  ND2 . ASN C  1 122 ? 49.182  5.408   -45.535 1.00 18.00 ? 122 ASN C ND2 1 
ATOM   5261 N  N   . SER C  1 123 ? 52.358  5.942   -41.398 1.00 14.42 ? 123 SER C N   1 
ATOM   5262 C  CA  . SER C  1 123 ? 53.602  6.663   -41.077 1.00 15.11 ? 123 SER C CA  1 
ATOM   5263 C  C   . SER C  1 123 ? 54.455  6.839   -42.311 1.00 16.44 ? 123 SER C C   1 
ATOM   5264 O  O   . SER C  1 123 ? 55.384  7.642   -42.270 1.00 16.39 ? 123 SER C O   1 
ATOM   5265 C  CB  . SER C  1 123 ? 54.337  5.891   -40.009 1.00 14.83 ? 123 SER C CB  1 
ATOM   5266 O  OG  . SER C  1 123 ? 54.508  4.535   -40.246 1.00 14.15 ? 123 SER C OG  1 
ATOM   5267 N  N   . ASP C  1 124 ? 54.169  6.143   -43.395 1.00 14.61 ? 124 ASP C N   1 
ATOM   5268 C  CA  . ASP C  1 124 ? 54.828  6.445   -44.689 1.00 14.67 ? 124 ASP C CA  1 
ATOM   5269 C  C   . ASP C  1 124 ? 54.383  7.777   -45.259 1.00 20.08 ? 124 ASP C C   1 
ATOM   5270 O  O   . ASP C  1 124 ? 55.185  8.405   -45.964 1.00 23.52 ? 124 ASP C O   1 
ATOM   5271 C  CB  . ASP C  1 124 ? 54.532  5.334   -45.692 1.00 15.21 ? 124 ASP C CB  1 
ATOM   5272 C  CG  . ASP C  1 124 ? 55.183  4.043   -45.360 1.00 15.54 ? 124 ASP C CG  1 
ATOM   5273 O  OD1 . ASP C  1 124 ? 56.225  3.976   -44.596 1.00 16.54 ? 124 ASP C OD1 1 
ATOM   5274 O  OD2 . ASP C  1 124 ? 54.787  3.012   -45.892 1.00 14.59 ? 124 ASP C OD2 1 
ATOM   5275 N  N   . LEU C  1 125 ? 53.154  8.202   -45.003 1.00 14.22 ? 125 LEU C N   1 
ATOM   5276 C  CA  . LEU C  1 125 ? 52.643  9.457   -45.496 1.00 16.87 ? 125 LEU C CA  1 
ATOM   5277 C  C   . LEU C  1 125 ? 52.668  10.583  -44.460 1.00 17.43 ? 125 LEU C C   1 
ATOM   5278 O  O   . LEU C  1 125 ? 52.750  11.726  -44.822 1.00 21.03 ? 125 LEU C O   1 
ATOM   5279 C  CB  . LEU C  1 125 ? 51.209  9.271   -45.986 1.00 18.57 ? 125 LEU C CB  1 
ATOM   5280 C  CG  . LEU C  1 125 ? 51.006  8.344   -47.181 1.00 24.18 ? 125 LEU C CG  1 
ATOM   5281 C  CD1 . LEU C  1 125 ? 49.550  8.293   -47.589 1.00 23.65 ? 125 LEU C CD1 1 
ATOM   5282 C  CD2 . LEU C  1 125 ? 51.908  8.681   -48.351 1.00 22.05 ? 125 LEU C CD2 1 
ATOM   5283 N  N   . TYR C  1 126 ? 52.509  10.248  -43.194 1.00 15.46 ? 126 TYR C N   1 
ATOM   5284 C  CA  . TYR C  1 126 ? 52.213  11.282  -42.204 1.00 15.32 ? 126 TYR C CA  1 
ATOM   5285 C  C   . TYR C  1 126 ? 53.073  11.162  -40.938 1.00 16.39 ? 126 TYR C C   1 
ATOM   5286 O  O   . TYR C  1 126 ? 53.465  10.047  -40.559 1.00 16.27 ? 126 TYR C O   1 
ATOM   5287 C  CB  . TYR C  1 126 ? 50.730  11.203  -41.731 1.00 14.70 ? 126 TYR C CB  1 
ATOM   5288 C  CG  . TYR C  1 126 ? 49.789  11.251  -42.938 1.00 16.50 ? 126 TYR C CG  1 
ATOM   5289 C  CD1 . TYR C  1 126 ? 49.778  12.345  -43.858 1.00 17.95 ? 126 TYR C CD1 1 
ATOM   5290 C  CD2 . TYR C  1 126 ? 48.891  10.182  -43.211 1.00 18.58 ? 126 TYR C CD2 1 
ATOM   5291 C  CE1 . TYR C  1 126 ? 48.944  12.342  -44.960 1.00 17.64 ? 126 TYR C CE1 1 
ATOM   5292 C  CE2 . TYR C  1 126 ? 48.126  10.146  -44.350 1.00 20.01 ? 126 TYR C CE2 1 
ATOM   5293 C  CZ  . TYR C  1 126 ? 48.121  11.223  -45.211 1.00 19.89 ? 126 TYR C CZ  1 
ATOM   5294 O  OH  . TYR C  1 126 ? 47.254  11.273  -46.314 1.00 18.47 ? 126 TYR C OH  1 
ATOM   5295 N  N   . PRO C  1 127 ? 53.303  12.319  -40.229 1.00 16.54 ? 127 PRO C N   1 
ATOM   5296 C  CA  . PRO C  1 127 ? 54.273  12.241  -39.163 1.00 20.93 ? 127 PRO C CA  1 
ATOM   5297 C  C   . PRO C  1 127 ? 53.714  11.690  -37.880 1.00 20.13 ? 127 PRO C C   1 
ATOM   5298 O  O   . PRO C  1 127 ? 54.478  11.302  -36.965 1.00 22.32 ? 127 PRO C O   1 
ATOM   5299 C  CB  . PRO C  1 127 ? 54.641  13.727  -38.922 1.00 22.05 ? 127 PRO C CB  1 
ATOM   5300 C  CG  . PRO C  1 127 ? 53.581  14.558  -39.560 1.00 21.28 ? 127 PRO C CG  1 
ATOM   5301 C  CD  . PRO C  1 127 ? 53.049  13.702  -40.704 1.00 20.78 ? 127 PRO C CD  1 
ATOM   5302 N  N   . ASP C  1 128 ? 52.398  11.741  -37.725 1.00 19.15 ? 128 ASP C N   1 
ATOM   5303 C  CA  . ASP C  1 128 ? 51.821  11.345  -36.416 1.00 21.27 ? 128 ASP C CA  1 
ATOM   5304 C  C   . ASP C  1 128 ? 50.336  11.046  -36.681 1.00 19.92 ? 128 ASP C C   1 
ATOM   5305 O  O   . ASP C  1 128 ? 49.768  11.470  -37.723 1.00 18.23 ? 128 ASP C O   1 
ATOM   5306 C  CB  . ASP C  1 128 ? 51.987  12.452  -35.291 1.00 22.80 ? 128 ASP C CB  1 
ATOM   5307 C  CG  . ASP C  1 128 ? 51.657  13.858  -35.774 1.00 29.53 ? 128 ASP C CG  1 
ATOM   5308 O  OD1 . ASP C  1 128 ? 52.568  14.733  -35.779 1.00 34.10 ? 128 ASP C OD1 1 
ATOM   5309 O  OD2 . ASP C  1 128 ? 50.522  14.106  -36.240 1.00 26.93 ? 128 ASP C OD2 1 
ATOM   5310 N  N   . ALA C  1 129 ? 49.669  10.457  -35.698 1.00 19.95 ? 129 ALA C N   1 
ATOM   5311 C  CA  . ALA C  1 129 ? 48.266  10.036  -35.845 1.00 19.72 ? 129 ALA C CA  1 
ATOM   5312 C  C   . ALA C  1 129 ? 47.252  11.181  -35.963 1.00 21.22 ? 129 ALA C C   1 
ATOM   5313 O  O   . ALA C  1 129 ? 46.320  11.115  -36.732 1.00 19.38 ? 129 ALA C O   1 
ATOM   5314 C  CB  . ALA C  1 129 ? 47.877  9.156   -34.669 1.00 24.93 ? 129 ALA C CB  1 
ATOM   5315 N  N   A SER C  1 130 ? 47.468  12.228  -35.205 0.50 22.05 ? 130 SER C N   1 
ATOM   5316 N  N   B SER C  1 130 ? 47.463  12.230  -35.198 0.50 21.39 ? 130 SER C N   1 
ATOM   5317 C  CA  A SER C  1 130 ? 46.592  13.391  -35.301 0.50 22.96 ? 130 SER C CA  1 
ATOM   5318 C  CA  B SER C  1 130 ? 46.573  13.389  -35.298 0.50 21.80 ? 130 SER C CA  1 
ATOM   5319 C  C   A SER C  1 130 ? 46.630  13.997  -36.688 0.50 20.43 ? 130 SER C C   1 
ATOM   5320 C  C   B SER C  1 130 ? 46.627  14.020  -36.681 0.50 19.84 ? 130 SER C C   1 
ATOM   5321 O  O   A SER C  1 130 ? 45.582  14.266  -37.257 0.50 21.40 ? 130 SER C O   1 
ATOM   5322 O  O   B SER C  1 130 ? 45.586  14.322  -37.245 0.50 20.54 ? 130 SER C O   1 
ATOM   5323 C  CB  A SER C  1 130 ? 46.954  14.429  -34.234 0.50 25.89 ? 130 SER C CB  1 
ATOM   5324 C  CB  B SER C  1 130 ? 46.820  14.419  -34.170 0.50 23.74 ? 130 SER C CB  1 
ATOM   5325 O  OG  A SER C  1 130 ? 46.657  13.925  -32.948 0.50 28.28 ? 130 SER C OG  1 
ATOM   5326 O  OG  B SER C  1 130 ? 48.196  14.685  -33.946 0.50 23.00 ? 130 SER C OG  1 
ATOM   5327 N  N   . THR C  1 131 ? 47.830  14.246  -37.239 1.00 19.79 ? 131 THR C N   1 
ATOM   5328 C  CA  . THR C  1 131 ? 47.922  14.723  -38.673 1.00 17.73 ? 131 THR C CA  1 
ATOM   5329 C  C   . THR C  1 131 ? 47.255  13.734  -39.683 1.00 15.46 ? 131 THR C C   1 
ATOM   5330 O  O   . THR C  1 131 ? 46.631  14.133  -40.638 1.00 17.59 ? 131 THR C O   1 
ATOM   5331 C  CB  . THR C  1 131 ? 49.383  14.928  -39.084 1.00 19.61 ? 131 THR C CB  1 
ATOM   5332 O  OG1 . THR C  1 131 ? 49.965  15.817  -38.125 1.00 22.19 ? 131 THR C OG1 1 
ATOM   5333 C  CG2 . THR C  1 131 ? 49.531  15.433  -40.474 1.00 18.81 ? 131 THR C CG2 1 
ATOM   5334 N  N   . ALA C  1 132 ? 47.480  12.453  -39.429 1.00 16.38 ? 132 ALA C N   1 
ATOM   5335 C  CA  . ALA C  1 132 ? 46.974  11.424  -40.335 1.00 16.24 ? 132 ALA C CA  1 
ATOM   5336 C  C   . ALA C  1 132 ? 45.422  11.284  -40.291 1.00 15.36 ? 132 ALA C C   1 
ATOM   5337 O  O   . ALA C  1 132 ? 44.837  10.944  -41.282 1.00 15.36 ? 132 ALA C O   1 
ATOM   5338 C  CB  . ALA C  1 132 ? 47.549  10.084  -39.927 1.00 14.69 ? 132 ALA C CB  1 
ATOM   5339 N  N   . SER C  1 133 ? 44.830  11.654  -39.147 1.00 15.74 ? 133 SER C N   1 
ATOM   5340 C  CA  . SER C  1 133 ? 43.424  11.218  -38.858 1.00 17.19 ? 133 SER C CA  1 
ATOM   5341 C  C   . SER C  1 133 ? 42.420  11.785  -39.803 1.00 19.31 ? 133 SER C C   1 
ATOM   5342 O  O   . SER C  1 133 ? 41.415  11.149  -40.141 1.00 16.51 ? 133 SER C O   1 
ATOM   5343 C  CB  . SER C  1 133 ? 43.123  11.467  -37.361 1.00 18.50 ? 133 SER C CB  1 
ATOM   5344 O  OG  . SER C  1 133 ? 43.207  12.895  -37.138 1.00 23.24 ? 133 SER C OG  1 
ATOM   5345 N  N   . ASN C  1 134 ? 42.680  12.969  -40.327 1.00 16.71 ? 134 ASN C N   1 
ATOM   5346 C  CA  . ASN C  1 134 ? 41.771  13.534  -41.307 1.00 18.52 ? 134 ASN C CA  1 
ATOM   5347 C  C   . ASN C  1 134 ? 42.242  13.523  -42.754 1.00 17.60 ? 134 ASN C C   1 
ATOM   5348 O  O   . ASN C  1 134 ? 41.730  14.227  -43.573 1.00 22.19 ? 134 ASN C O   1 
ATOM   5349 C  CB  . ASN C  1 134 ? 41.356  14.960  -40.857 1.00 18.85 ? 134 ASN C CB  1 
ATOM   5350 C  CG  . ASN C  1 134 ? 42.510  15.950  -40.946 1.00 25.87 ? 134 ASN C CG  1 
ATOM   5351 O  OD1 . ASN C  1 134 ? 43.664  15.551  -40.980 1.00 24.97 ? 134 ASN C OD1 1 
ATOM   5352 N  ND2 . ASN C  1 134 ? 42.181  17.243  -40.998 1.00 25.17 ? 134 ASN C ND2 1 
ATOM   5353 N  N   . LYS C  1 135 ? 43.148  12.626  -43.117 1.00 17.11 ? 135 LYS C N   1 
ATOM   5354 C  CA  . LYS C  1 135 ? 43.801  12.629  -44.349 1.00 17.52 ? 135 LYS C CA  1 
ATOM   5355 C  C   . LYS C  1 135 ? 43.675  11.297  -45.002 1.00 17.38 ? 135 LYS C C   1 
ATOM   5356 O  O   . LYS C  1 135 ? 43.473  10.241  -44.348 1.00 18.11 ? 135 LYS C O   1 
ATOM   5357 C  CB  . LYS C  1 135 ? 45.293  13.021  -44.146 1.00 19.66 ? 135 LYS C CB  1 
ATOM   5358 C  CG  . LYS C  1 135 ? 45.392  14.494  -43.732 1.00 20.75 ? 135 LYS C CG  1 
ATOM   5359 C  CD  . LYS C  1 135 ? 46.832  14.988  -43.752 1.00 20.92 ? 135 LYS C CD  1 
ATOM   5360 C  CE  . LYS C  1 135 ? 46.894  16.374  -43.182 1.00 22.02 ? 135 LYS C CE  1 
ATOM   5361 N  NZ  . LYS C  1 135 ? 46.229  16.585  -41.853 1.00 22.20 ? 135 LYS C NZ  1 
ATOM   5362 N  N   . SER C  1 136 ? 43.783  11.297  -46.323 1.00 18.29 ? 136 SER C N   1 
ATOM   5363 C  CA  . SER C  1 136 ? 43.564  10.108  -47.129 1.00 17.46 ? 136 SER C CA  1 
ATOM   5364 C  C   . SER C  1 136 ? 44.447  8.937   -46.652 1.00 16.51 ? 136 SER C C   1 
ATOM   5365 O  O   . SER C  1 136 ? 45.676  9.113   -46.426 1.00 18.06 ? 136 SER C O   1 
ATOM   5366 C  CB  . SER C  1 136 ? 43.985  10.422  -48.556 1.00 20.75 ? 136 SER C CB  1 
ATOM   5367 O  OG  . SER C  1 136 ? 43.716  9.280   -49.320 1.00 26.38 ? 136 SER C OG  1 
ATOM   5368 N  N   . GLU C  1 137 ? 43.840  7.762   -46.528 1.00 17.31 ? 137 GLU C N   1 
ATOM   5369 C  CA  . GLU C  1 137 ? 44.605  6.567   -46.079 1.00 17.77 ? 137 GLU C CA  1 
ATOM   5370 C  C   . GLU C  1 137 ? 45.306  6.741   -44.757 1.00 17.19 ? 137 GLU C C   1 
ATOM   5371 O  O   . GLU C  1 137 ? 46.363  6.122   -44.471 1.00 16.13 ? 137 GLU C O   1 
ATOM   5372 C  CB  . GLU C  1 137 ? 45.582  6.068   -47.136 1.00 19.56 ? 137 GLU C CB  1 
ATOM   5373 C  CG  . GLU C  1 137 ? 44.839  5.570   -48.346 1.00 26.75 ? 137 GLU C CG  1 
ATOM   5374 C  CD  . GLU C  1 137 ? 45.738  5.298   -49.568 1.00 32.05 ? 137 GLU C CD  1 
ATOM   5375 O  OE1 . GLU C  1 137 ? 46.960  5.627   -49.573 1.00 41.49 ? 137 GLU C OE1 1 
ATOM   5376 O  OE2 . GLU C  1 137 ? 45.182  4.829   -50.574 1.00 34.67 ? 137 GLU C OE2 1 
ATOM   5377 N  N   . GLY C  1 138 ? 44.725  7.553   -43.873 1.00 12.88 ? 138 GLY C N   1 
ATOM   5378 C  CA  . GLY C  1 138 ? 45.458  7.966   -42.731 1.00 13.24 ? 138 GLY C CA  1 
ATOM   5379 C  C   . GLY C  1 138 ? 45.569  6.935   -41.642 1.00 12.31 ? 138 GLY C C   1 
ATOM   5380 O  O   . GLY C  1 138 ? 46.558  6.906   -40.865 1.00 14.20 ? 138 GLY C O   1 
ATOM   5381 N  N   . LEU C  1 139 ? 44.529  6.071   -41.474 1.00 11.26 ? 139 LEU C N   1 
ATOM   5382 C  CA  . LEU C  1 139 ? 44.464  5.203   -40.308 1.00 10.61 ? 139 LEU C CA  1 
ATOM   5383 C  C   . LEU C  1 139 ? 44.147  3.757   -40.627 1.00 10.53 ? 139 LEU C C   1 
ATOM   5384 O  O   . LEU C  1 139 ? 43.508  3.533   -41.641 1.00 9.97  ? 139 LEU C O   1 
ATOM   5385 C  CB  . LEU C  1 139 ? 43.449  5.731   -39.248 1.00 10.87 ? 139 LEU C CB  1 
ATOM   5386 C  CG  . LEU C  1 139 ? 43.650  7.155   -38.739 1.00 12.53 ? 139 LEU C CG  1 
ATOM   5387 C  CD1 . LEU C  1 139 ? 42.366  7.585   -37.992 1.00 14.54 ? 139 LEU C CD1 1 
ATOM   5388 C  CD2 . LEU C  1 139 ? 44.884  7.284   -37.849 1.00 14.08 ? 139 LEU C CD2 1 
ATOM   5389 N  N   . ALA C  1 140 ? 44.552  2.829   -39.769 1.00 9.81  ? 140 ALA C N   1 
ATOM   5390 C  CA  . ALA C  1 140 ? 44.165  1.404   -39.896 1.00 9.63  ? 140 ALA C CA  1 
ATOM   5391 C  C   . ALA C  1 140 ? 43.933  0.931   -38.488 1.00 10.65 ? 140 ALA C C   1 
ATOM   5392 O  O   . ALA C  1 140 ? 44.713  1.179   -37.589 1.00 10.85 ? 140 ALA C O   1 
ATOM   5393 C  CB  . ALA C  1 140 ? 45.267  0.583   -40.528 1.00 10.81 ? 140 ALA C CB  1 
ATOM   5394 N  N   . VAL C  1 141 ? 42.783  0.291   -38.225 1.00 10.08 ? 141 VAL C N   1 
ATOM   5395 C  CA  . VAL C  1 141 ? 42.445  -0.189  -36.889 1.00 10.82 ? 141 VAL C CA  1 
ATOM   5396 C  C   . VAL C  1 141 ? 42.370  -1.691  -36.933 1.00 9.87  ? 141 VAL C C   1 
ATOM   5397 O  O   . VAL C  1 141 ? 41.781  -2.310  -37.844 1.00 11.20 ? 141 VAL C O   1 
ATOM   5398 C  CB  . VAL C  1 141 ? 41.142  0.443   -36.345 1.00 9.95  ? 141 VAL C CB  1 
ATOM   5399 C  CG1 . VAL C  1 141 ? 40.816  -0.132  -34.924 1.00 13.00 ? 141 VAL C CG1 1 
ATOM   5400 C  CG2 . VAL C  1 141 ? 41.222  1.925   -36.270 1.00 11.78 ? 141 VAL C CG2 1 
ATOM   5401 N  N   . LEU C  1 142 ? 42.906  -2.330  -35.904 1.00 10.51 ? 142 LEU C N   1 
ATOM   5402 C  CA  . LEU C  1 142 ? 42.700  -3.725  -35.710 1.00 10.56 ? 142 LEU C CA  1 
ATOM   5403 C  C   . LEU C  1 142 ? 41.619  -3.856  -34.610 1.00 10.67 ? 142 LEU C C   1 
ATOM   5404 O  O   . LEU C  1 142 ? 41.777  -3.237  -33.489 1.00 11.59 ? 142 LEU C O   1 
ATOM   5405 C  CB  . LEU C  1 142 ? 43.912  -4.474  -35.200 1.00 12.72 ? 142 LEU C CB  1 
ATOM   5406 C  CG  . LEU C  1 142 ? 45.158  -4.344  -36.042 1.00 12.78 ? 142 LEU C CG  1 
ATOM   5407 C  CD1 . LEU C  1 142 ? 46.226  -5.175  -35.370 1.00 14.56 ? 142 LEU C CD1 1 
ATOM   5408 C  CD2 . LEU C  1 142 ? 44.886  -4.856  -37.445 1.00 14.20 ? 142 LEU C CD2 1 
ATOM   5409 N  N   . ALA C  1 143 ? 40.523  -4.557  -34.911 1.00 9.82  ? 143 ALA C N   1 
ATOM   5410 C  CA  . ALA C  1 143 ? 39.433  -4.669  -33.956 1.00 9.31  ? 143 ALA C CA  1 
ATOM   5411 C  C   . ALA C  1 143 ? 39.273  -6.132  -33.531 1.00 10.05 ? 143 ALA C C   1 
ATOM   5412 O  O   . ALA C  1 143 ? 39.247  -7.089  -34.300 1.00 11.07 ? 143 ALA C O   1 
ATOM   5413 C  CB  . ALA C  1 143 ? 38.107  -4.221  -34.595 1.00 10.41 ? 143 ALA C CB  1 
ATOM   5414 N  N   . VAL C  1 144 ? 39.223  -6.260  -32.187 1.00 10.49 ? 144 VAL C N   1 
ATOM   5415 C  CA  . VAL C  1 144 ? 39.029  -7.590  -31.572 1.00 10.93 ? 144 VAL C CA  1 
ATOM   5416 C  C   . VAL C  1 144 ? 37.680  -7.618  -30.790 1.00 10.59 ? 144 VAL C C   1 
ATOM   5417 O  O   . VAL C  1 144 ? 37.448  -6.783  -29.938 1.00 12.51 ? 144 VAL C O   1 
ATOM   5418 C  CB  . VAL C  1 144 ? 40.161  -7.896  -30.568 1.00 12.47 ? 144 VAL C CB  1 
ATOM   5419 C  CG1 . VAL C  1 144 ? 39.983  -9.340  -30.042 1.00 14.75 ? 144 VAL C CG1 1 
ATOM   5420 C  CG2 . VAL C  1 144 ? 41.552  -7.893  -31.305 1.00 12.82 ? 144 VAL C CG2 1 
ATOM   5421 N  N   . LEU C  1 145 ? 36.848  -8.595  -31.174 1.00 11.87 ? 145 LEU C N   1 
ATOM   5422 C  CA  . LEU C  1 145 ? 35.522  -8.761  -30.515 1.00 13.00 ? 145 LEU C CA  1 
ATOM   5423 C  C   . LEU C  1 145 ? 35.836  -9.528  -29.203 1.00 14.06 ? 145 LEU C C   1 
ATOM   5424 O  O   . LEU C  1 145 ? 36.628  -10.475 -29.225 1.00 15.67 ? 145 LEU C O   1 
ATOM   5425 C  CB  . LEU C  1 145 ? 34.573  -9.529  -31.445 1.00 12.53 ? 145 LEU C CB  1 
ATOM   5426 C  CG  . LEU C  1 145 ? 34.327  -8.831  -32.797 1.00 12.96 ? 145 LEU C CG  1 
ATOM   5427 C  CD1 . LEU C  1 145 ? 33.684  -9.775  -33.818 1.00 12.54 ? 145 LEU C CD1 1 
ATOM   5428 C  CD2 . LEU C  1 145 ? 33.477  -7.587  -32.541 1.00 13.90 ? 145 LEU C CD2 1 
ATOM   5429 N  N   . ILE C  1 146 ? 35.119  -9.147  -28.151 1.00 12.08 ? 146 ILE C N   1 
ATOM   5430 C  CA  . ILE C  1 146 ? 35.397  -9.667  -26.722 1.00 12.32 ? 146 ILE C CA  1 
ATOM   5431 C  C   . ILE C  1 146 ? 34.089  -10.287 -26.277 1.00 15.98 ? 146 ILE C C   1 
ATOM   5432 O  O   . ILE C  1 146 ? 33.047  -9.615  -26.264 1.00 14.28 ? 146 ILE C O   1 
ATOM   5433 C  CB  . ILE C  1 146 ? 35.840  -8.548  -25.766 1.00 13.83 ? 146 ILE C CB  1 
ATOM   5434 C  CG1 . ILE C  1 146 ? 37.221  -7.963  -26.177 1.00 13.28 ? 146 ILE C CG1 1 
ATOM   5435 C  CG2 . ILE C  1 146 ? 36.054  -9.199  -24.355 1.00 14.58 ? 146 ILE C CG2 1 
ATOM   5436 C  CD1 . ILE C  1 146 ? 37.608  -6.609  -25.565 1.00 14.72 ? 146 ILE C CD1 1 
ATOM   5437 N  N   . GLU C  1 147 ? 34.169  -11.546 -25.837 1.00 16.80 ? 147 GLU C N   1 
ATOM   5438 C  CA  . GLU C  1 147 ? 33.038  -12.212 -25.157 1.00 18.74 ? 147 GLU C CA  1 
ATOM   5439 C  C   . GLU C  1 147 ? 33.423  -12.728 -23.761 1.00 19.16 ? 147 GLU C C   1 
ATOM   5440 O  O   . GLU C  1 147 ? 34.617  -12.823 -23.397 1.00 19.61 ? 147 GLU C O   1 
ATOM   5441 C  CB  . GLU C  1 147 ? 32.443  -13.317 -26.036 1.00 18.46 ? 147 GLU C CB  1 
ATOM   5442 C  CG  . GLU C  1 147 ? 33.427  -14.494 -26.215 1.00 20.36 ? 147 GLU C CG  1 
ATOM   5443 C  CD  . GLU C  1 147 ? 32.970  -15.568 -27.182 1.00 22.32 ? 147 GLU C CD  1 
ATOM   5444 O  OE1 . GLU C  1 147 ? 31.984  -15.369 -27.953 1.00 26.53 ? 147 GLU C OE1 1 
ATOM   5445 O  OE2 . GLU C  1 147 ? 33.650  -16.621 -27.261 1.00 28.19 ? 147 GLU C OE2 1 
ATOM   5446 N  N   . MET C  1 148 ? 32.398  -12.962 -22.962 1.00 21.03 ? 148 MET C N   1 
ATOM   5447 C  CA  . MET C  1 148 ? 32.646  -13.535 -21.638 1.00 24.60 ? 148 MET C CA  1 
ATOM   5448 C  C   . MET C  1 148 ? 33.059  -15.004 -21.772 1.00 24.02 ? 148 MET C C   1 
ATOM   5449 O  O   . MET C  1 148 ? 32.482  -15.788 -22.532 1.00 25.07 ? 148 MET C O   1 
ATOM   5450 C  CB  . MET C  1 148 ? 31.384  -13.431 -20.786 1.00 29.77 ? 148 MET C CB  1 
ATOM   5451 C  CG  . MET C  1 148 ? 31.363  -12.308 -19.779 1.00 40.32 ? 148 MET C CG  1 
ATOM   5452 S  SD  . MET C  1 148 ? 30.029  -12.530 -18.536 1.00 56.15 ? 148 MET C SD  1 
ATOM   5453 C  CE  . MET C  1 148 ? 28.560  -12.208 -19.552 1.00 48.73 ? 148 MET C CE  1 
ATOM   5454 N  N   . GLY C  1 149 ? 34.054  -15.391 -20.975 1.00 22.51 ? 149 GLY C N   1 
ATOM   5455 C  CA  . GLY C  1 149 ? 34.384  -16.839 -20.880 1.00 24.24 ? 149 GLY C CA  1 
ATOM   5456 C  C   . GLY C  1 149 ? 35.506  -16.967 -19.840 1.00 24.34 ? 149 GLY C C   1 
ATOM   5457 O  O   . GLY C  1 149 ? 35.415  -16.422 -18.736 1.00 22.76 ? 149 GLY C O   1 
ATOM   5458 N  N   . SER C  1 150 ? 36.599  -17.596 -20.269 1.00 24.96 ? 150 SER C N   1 
ATOM   5459 C  CA  . SER C  1 150 ? 37.810  -17.843 -19.426 1.00 26.74 ? 150 SER C CA  1 
ATOM   5460 C  C   . SER C  1 150 ? 38.503  -16.535 -19.028 1.00 30.56 ? 150 SER C C   1 
ATOM   5461 O  O   . SER C  1 150 ? 38.595  -15.589 -19.852 1.00 24.43 ? 150 SER C O   1 
ATOM   5462 C  CB  . SER C  1 150 ? 38.844  -18.684 -20.208 1.00 29.10 ? 150 SER C CB  1 
ATOM   5463 O  OG  . SER C  1 150 ? 38.486  -20.067 -20.257 1.00 35.50 ? 150 SER C OG  1 
ATOM   5464 N  N   . PHE C  1 151 ? 39.072  -16.513 -17.818 1.00 25.52 ? 151 PHE C N   1 
ATOM   5465 C  CA  . PHE C  1 151 ? 39.929  -15.380 -17.346 1.00 23.93 ? 151 PHE C CA  1 
ATOM   5466 C  C   . PHE C  1 151 ? 41.056  -15.149 -18.342 1.00 25.61 ? 151 PHE C C   1 
ATOM   5467 O  O   . PHE C  1 151 ? 41.693  -16.098 -18.795 1.00 23.43 ? 151 PHE C O   1 
ATOM   5468 C  CB  . PHE C  1 151 ? 40.532  -15.667 -15.912 1.00 24.37 ? 151 PHE C CB  1 
ATOM   5469 C  CG  . PHE C  1 151 ? 41.482  -14.606 -15.420 1.00 22.15 ? 151 PHE C CG  1 
ATOM   5470 C  CD1 . PHE C  1 151 ? 41.002  -13.372 -15.011 1.00 23.97 ? 151 PHE C CD1 1 
ATOM   5471 C  CD2 . PHE C  1 151 ? 42.856  -14.837 -15.392 1.00 23.88 ? 151 PHE C CD2 1 
ATOM   5472 C  CE1 . PHE C  1 151 ? 41.882  -12.368 -14.561 1.00 21.32 ? 151 PHE C CE1 1 
ATOM   5473 C  CE2 . PHE C  1 151 ? 43.728  -13.850 -14.959 1.00 24.37 ? 151 PHE C CE2 1 
ATOM   5474 C  CZ  . PHE C  1 151 ? 43.246  -12.607 -14.544 1.00 24.15 ? 151 PHE C CZ  1 
ATOM   5475 N  N   . ASN C  1 152 ? 41.339  -13.875 -18.636 1.00 22.43 ? 152 ASN C N   1 
ATOM   5476 C  CA  . ASN C  1 152 ? 42.406  -13.566 -19.578 1.00 19.65 ? 152 ASN C CA  1 
ATOM   5477 C  C   . ASN C  1 152 ? 43.560  -12.788 -18.992 1.00 19.36 ? 152 ASN C C   1 
ATOM   5478 O  O   . ASN C  1 152 ? 43.470  -11.556 -18.668 1.00 20.75 ? 152 ASN C O   1 
ATOM   5479 C  CB  . ASN C  1 152 ? 41.769  -12.779 -20.754 1.00 17.95 ? 152 ASN C CB  1 
ATOM   5480 C  CG  . ASN C  1 152 ? 42.702  -12.657 -21.924 1.00 18.95 ? 152 ASN C CG  1 
ATOM   5481 O  OD1 . ASN C  1 152 ? 43.893  -12.310 -21.778 1.00 17.98 ? 152 ASN C OD1 1 
ATOM   5482 N  ND2 . ASN C  1 152 ? 42.175  -12.907 -23.148 1.00 18.68 ? 152 ASN C ND2 1 
ATOM   5483 N  N   . PRO C  1 153 ? 44.691  -13.482 -18.727 1.00 21.98 ? 153 PRO C N   1 
ATOM   5484 C  CA  . PRO C  1 153 ? 45.765  -12.802 -18.044 1.00 22.25 ? 153 PRO C CA  1 
ATOM   5485 C  C   . PRO C  1 153 ? 46.368  -11.633 -18.834 1.00 20.61 ? 153 PRO C C   1 
ATOM   5486 O  O   . PRO C  1 153 ? 46.806  -10.642 -18.229 1.00 23.64 ? 153 PRO C O   1 
ATOM   5487 C  CB  . PRO C  1 153 ? 46.763  -13.917 -17.714 1.00 24.16 ? 153 PRO C CB  1 
ATOM   5488 C  CG  . PRO C  1 153 ? 46.394  -15.074 -18.564 1.00 25.63 ? 153 PRO C CG  1 
ATOM   5489 C  CD  . PRO C  1 153 ? 44.964  -14.915 -19.039 1.00 22.11 ? 153 PRO C CD  1 
ATOM   5490 N  N   . SER C  1 154 ? 46.245  -11.670 -20.170 1.00 22.91 ? 154 SER C N   1 
ATOM   5491 C  CA  . SER C  1 154 ? 46.811  -10.600 -20.982 1.00 21.08 ? 154 SER C CA  1 
ATOM   5492 C  C   . SER C  1 154 ? 45.959  -9.359  -20.866 1.00 18.00 ? 154 SER C C   1 
ATOM   5493 O  O   . SER C  1 154 ? 46.503  -8.279  -20.655 1.00 18.04 ? 154 SER C O   1 
ATOM   5494 C  CB  . SER C  1 154 ? 47.009  -11.099 -22.374 1.00 24.21 ? 154 SER C CB  1 
ATOM   5495 O  OG  . SER C  1 154 ? 47.782  -12.304 -22.302 1.00 27.01 ? 154 SER C OG  1 
ATOM   5496 N  N   . TYR C  1 155 ? 44.612  -9.502  -20.916 1.00 19.48 ? 155 TYR C N   1 
ATOM   5497 C  CA  . TYR C  1 155 ? 43.743  -8.351  -20.730 1.00 20.47 ? 155 TYR C CA  1 
ATOM   5498 C  C   . TYR C  1 155 ? 43.897  -7.799  -19.350 1.00 19.09 ? 155 TYR C C   1 
ATOM   5499 O  O   . TYR C  1 155 ? 43.719  -6.558  -19.103 1.00 19.27 ? 155 TYR C O   1 
ATOM   5500 C  CB  . TYR C  1 155 ? 42.243  -8.608  -21.090 1.00 19.11 ? 155 TYR C CB  1 
ATOM   5501 C  CG  . TYR C  1 155 ? 42.029  -8.538  -22.650 1.00 18.94 ? 155 TYR C CG  1 
ATOM   5502 C  CD1 . TYR C  1 155 ? 42.463  -9.568  -23.483 1.00 16.90 ? 155 TYR C CD1 1 
ATOM   5503 C  CD2 . TYR C  1 155 ? 41.496  -7.356  -23.244 1.00 16.83 ? 155 TYR C CD2 1 
ATOM   5504 C  CE1 . TYR C  1 155 ? 42.295  -9.473  -24.913 1.00 18.94 ? 155 TYR C CE1 1 
ATOM   5505 C  CE2 . TYR C  1 155 ? 41.328  -7.244  -24.630 1.00 16.77 ? 155 TYR C CE2 1 
ATOM   5506 C  CZ  . TYR C  1 155 ? 41.762  -8.301  -25.434 1.00 16.40 ? 155 TYR C CZ  1 
ATOM   5507 O  OH  . TYR C  1 155 ? 41.609  -8.163  -26.849 1.00 16.85 ? 155 TYR C OH  1 
ATOM   5508 N  N   . ASP C  1 156 ? 44.243  -8.658  -18.394 1.00 20.64 ? 156 ASP C N   1 
ATOM   5509 C  CA  . ASP C  1 156 ? 44.383  -8.155  -17.031 1.00 24.74 ? 156 ASP C CA  1 
ATOM   5510 C  C   . ASP C  1 156 ? 45.565  -7.252  -16.826 1.00 23.02 ? 156 ASP C C   1 
ATOM   5511 O  O   . ASP C  1 156 ? 45.604  -6.520  -15.829 1.00 25.03 ? 156 ASP C O   1 
ATOM   5512 C  CB  . ASP C  1 156 ? 44.392  -9.276  -15.975 1.00 24.86 ? 156 ASP C CB  1 
ATOM   5513 C  CG  . ASP C  1 156 ? 43.355  -8.997  -14.847 1.00 31.36 ? 156 ASP C CG  1 
ATOM   5514 O  OD1 . ASP C  1 156 ? 42.168  -8.666  -15.164 1.00 26.42 ? 156 ASP C OD1 1 
ATOM   5515 O  OD2 . ASP C  1 156 ? 43.754  -9.034  -13.639 1.00 33.30 ? 156 ASP C OD2 1 
ATOM   5516 N  N   . LYS C  1 157 ? 46.488  -7.211  -17.784 1.00 20.30 ? 157 LYS C N   1 
ATOM   5517 C  CA  . LYS C  1 157 ? 47.664  -6.312  -17.676 1.00 21.86 ? 157 LYS C CA  1 
ATOM   5518 C  C   . LYS C  1 157 ? 47.180  -4.903  -17.823 1.00 23.91 ? 157 LYS C C   1 
ATOM   5519 O  O   . LYS C  1 157 ? 47.747  -3.975  -17.234 1.00 26.29 ? 157 LYS C O   1 
ATOM   5520 C  CB  . LYS C  1 157 ? 48.701  -6.720  -18.688 1.00 22.71 ? 157 LYS C CB  1 
ATOM   5521 C  CG  . LYS C  1 157 ? 49.084  -8.199  -18.454 1.00 27.76 ? 157 LYS C CG  1 
ATOM   5522 C  CD  . LYS C  1 157 ? 50.358  -8.663  -19.103 1.00 30.04 ? 157 LYS C CD  1 
ATOM   5523 C  CE  . LYS C  1 157 ? 50.315  -10.187 -19.055 1.00 29.99 ? 157 LYS C CE  1 
ATOM   5524 N  NZ  . LYS C  1 157 ? 51.353  -10.816 -19.927 1.00 26.87 ? 157 LYS C NZ  1 
ATOM   5525 N  N   . ILE C  1 158 ? 46.080  -4.758  -18.550 1.00 20.61 ? 158 ILE C N   1 
ATOM   5526 C  CA  . ILE C  1 158 ? 45.445  -3.455  -18.593 1.00 22.21 ? 158 ILE C CA  1 
ATOM   5527 C  C   . ILE C  1 158 ? 44.482  -3.276  -17.410 1.00 20.17 ? 158 ILE C C   1 
ATOM   5528 O  O   . ILE C  1 158 ? 44.498  -2.195  -16.714 1.00 18.08 ? 158 ILE C O   1 
ATOM   5529 C  CB  . ILE C  1 158 ? 44.684  -3.246  -19.954 1.00 18.57 ? 158 ILE C CB  1 
ATOM   5530 C  CG1 . ILE C  1 158 ? 45.713  -3.278  -21.068 1.00 22.26 ? 158 ILE C CG1 1 
ATOM   5531 C  CG2 . ILE C  1 158 ? 43.947  -1.895  -19.827 1.00 20.53 ? 158 ILE C CG2 1 
ATOM   5532 C  CD1 . ILE C  1 158 ? 45.154  -3.394  -22.473 1.00 24.23 ? 158 ILE C CD1 1 
ATOM   5533 N  N   . PHE C  1 159 ? 43.567  -4.223  -17.251 1.00 19.26 ? 159 PHE C N   1 
ATOM   5534 C  CA  . PHE C  1 159 ? 42.414  -4.056  -16.365 1.00 17.63 ? 159 PHE C CA  1 
ATOM   5535 C  C   . PHE C  1 159 ? 42.822  -3.903  -14.904 1.00 20.37 ? 159 PHE C C   1 
ATOM   5536 O  O   . PHE C  1 159 ? 42.028  -3.310  -14.126 1.00 18.89 ? 159 PHE C O   1 
ATOM   5537 C  CB  . PHE C  1 159 ? 41.384  -5.203  -16.446 1.00 18.71 ? 159 PHE C CB  1 
ATOM   5538 C  CG  . PHE C  1 159 ? 40.743  -5.422  -17.820 1.00 20.29 ? 159 PHE C CG  1 
ATOM   5539 C  CD1 . PHE C  1 159 ? 40.595  -4.356  -18.789 1.00 23.05 ? 159 PHE C CD1 1 
ATOM   5540 C  CD2 . PHE C  1 159 ? 40.228  -6.679  -18.103 1.00 20.09 ? 159 PHE C CD2 1 
ATOM   5541 C  CE1 . PHE C  1 159 ? 39.990  -4.651  -20.021 1.00 20.06 ? 159 PHE C CE1 1 
ATOM   5542 C  CE2 . PHE C  1 159 ? 39.581  -6.940  -19.353 1.00 23.41 ? 159 PHE C CE2 1 
ATOM   5543 C  CZ  . PHE C  1 159 ? 39.500  -5.940  -20.285 1.00 19.12 ? 159 PHE C CZ  1 
ATOM   5544 N  N   . SER C  1 160 ? 44.020  -4.414  -14.583 1.00 19.04 ? 160 SER C N   1 
ATOM   5545 C  CA  . SER C  1 160 ? 44.488  -4.366  -13.182 1.00 20.08 ? 160 SER C CA  1 
ATOM   5546 C  C   . SER C  1 160 ? 44.911  -2.971  -12.798 1.00 24.09 ? 160 SER C C   1 
ATOM   5547 O  O   . SER C  1 160 ? 45.198  -2.770  -11.615 1.00 24.09 ? 160 SER C O   1 
ATOM   5548 C  CB  . SER C  1 160 ? 45.588  -5.358  -12.922 1.00 25.10 ? 160 SER C CB  1 
ATOM   5549 O  OG  . SER C  1 160 ? 46.716  -5.120  -13.766 1.00 24.13 ? 160 SER C OG  1 
ATOM   5550 N  N   . HIS C  1 161 ? 44.903  -2.013  -13.747 1.00 19.21 ? 161 HIS C N   1 
ATOM   5551 C  CA  . HIS C  1 161 ? 45.151  -0.570  -13.518 1.00 18.90 ? 161 HIS C CA  1 
ATOM   5552 C  C   . HIS C  1 161 ? 44.004  0.361   -13.544 1.00 16.57 ? 161 HIS C C   1 
ATOM   5553 O  O   . HIS C  1 161 ? 44.166  1.605   -13.362 1.00 17.59 ? 161 HIS C O   1 
ATOM   5554 C  CB  . HIS C  1 161 ? 46.264  -0.133  -14.528 1.00 21.57 ? 161 HIS C CB  1 
ATOM   5555 C  CG  . HIS C  1 161 ? 47.574  -0.845  -14.260 1.00 24.36 ? 161 HIS C CG  1 
ATOM   5556 N  ND1 . HIS C  1 161 ? 48.494  -0.334  -13.402 1.00 29.67 ? 161 HIS C ND1 1 
ATOM   5557 C  CD2 . HIS C  1 161 ? 48.009  -2.120  -14.610 1.00 24.57 ? 161 HIS C CD2 1 
ATOM   5558 C  CE1 . HIS C  1 161 ? 49.504  -1.230  -13.256 1.00 28.75 ? 161 HIS C CE1 1 
ATOM   5559 N  NE2 . HIS C  1 161 ? 49.208  -2.324  -13.974 1.00 27.59 ? 161 HIS C NE2 1 
ATOM   5560 N  N   . LEU C  1 162 ? 42.807  -0.151  -13.870 1.00 16.73 ? 162 LEU C N   1 
ATOM   5561 C  CA  . LEU C  1 162 ? 41.652  0.736   -14.024 1.00 16.83 ? 162 LEU C CA  1 
ATOM   5562 C  C   . LEU C  1 162 ? 41.349  1.580   -12.802 1.00 15.11 ? 162 LEU C C   1 
ATOM   5563 O  O   . LEU C  1 162 ? 40.929  2.691   -12.983 1.00 15.73 ? 162 LEU C O   1 
ATOM   5564 C  CB  . LEU C  1 162 ? 40.392  -0.044  -14.466 1.00 17.68 ? 162 LEU C CB  1 
ATOM   5565 C  CG  . LEU C  1 162 ? 40.609  -0.811  -15.784 1.00 21.19 ? 162 LEU C CG  1 
ATOM   5566 C  CD1 . LEU C  1 162 ? 39.392  -1.680  -15.999 1.00 23.57 ? 162 LEU C CD1 1 
ATOM   5567 C  CD2 . LEU C  1 162 ? 40.850  0.204   -16.879 1.00 26.60 ? 162 LEU C CD2 1 
ATOM   5568 N  N   . GLN C  1 163 ? 41.588  1.082   -11.556 1.00 15.51 ? 163 GLN C N   1 
ATOM   5569 C  CA  . GLN C  1 163 ? 41.213  1.903   -10.413 1.00 16.28 ? 163 GLN C CA  1 
ATOM   5570 C  C   . GLN C  1 163 ? 42.215  3.071   -10.200 1.00 14.73 ? 163 GLN C C   1 
ATOM   5571 O  O   . GLN C  1 163 ? 41.970  3.921   -9.322  1.00 19.65 ? 163 GLN C O   1 
ATOM   5572 C  CB  . GLN C  1 163 ? 41.184  1.026   -9.143  1.00 16.10 ? 163 GLN C CB  1 
ATOM   5573 C  CG  . GLN C  1 163 ? 40.083  -0.098  -9.114  1.00 18.38 ? 163 GLN C CG  1 
ATOM   5574 C  CD  . GLN C  1 163 ? 38.648  0.382   -9.170  1.00 21.75 ? 163 GLN C CD  1 
ATOM   5575 O  OE1 . GLN C  1 163 ? 38.252  1.385   -8.603  1.00 21.47 ? 163 GLN C OE1 1 
ATOM   5576 N  NE2 . GLN C  1 163 ? 37.818  -0.403  -9.900  1.00 23.63 ? 163 GLN C NE2 1 
ATOM   5577 N  N   . HIS C  1 164 ? 43.279  3.129   -10.979 1.00 15.91 ? 164 HIS C N   1 
ATOM   5578 C  CA  . HIS C  1 164 ? 44.140  4.305   -10.940 1.00 17.72 ? 164 HIS C CA  1 
ATOM   5579 C  C   . HIS C  1 164 ? 43.716  5.444   -11.836 1.00 21.20 ? 164 HIS C C   1 
ATOM   5580 O  O   . HIS C  1 164 ? 44.241  6.574   -11.729 1.00 20.92 ? 164 HIS C O   1 
ATOM   5581 C  CB  . HIS C  1 164 ? 45.575  3.930   -11.214 1.00 19.28 ? 164 HIS C CB  1 
ATOM   5582 C  CG  . HIS C  1 164 ? 46.102  2.860   -10.291 1.00 16.95 ? 164 HIS C CG  1 
ATOM   5583 N  ND1 . HIS C  1 164 ? 46.171  3.056   -8.935  1.00 20.88 ? 164 HIS C ND1 1 
ATOM   5584 C  CD2 . HIS C  1 164 ? 46.508  1.564   -10.526 1.00 17.63 ? 164 HIS C CD2 1 
ATOM   5585 C  CE1 . HIS C  1 164 ? 46.629  1.918   -8.348  1.00 16.30 ? 164 HIS C CE1 1 
ATOM   5586 N  NE2 . HIS C  1 164 ? 46.801  0.992   -9.296  1.00 17.61 ? 164 HIS C NE2 1 
ATOM   5587 N  N   . VAL C  1 165 ? 42.756  5.169   -12.722 1.00 19.76 ? 165 VAL C N   1 
ATOM   5588 C  CA  . VAL C  1 165 ? 42.284  6.141   -13.682 1.00 18.53 ? 165 VAL C CA  1 
ATOM   5589 C  C   . VAL C  1 165 ? 40.766  6.294   -13.649 1.00 19.11 ? 165 VAL C C   1 
ATOM   5590 O  O   . VAL C  1 165 ? 40.079  6.500   -14.683 1.00 16.11 ? 165 VAL C O   1 
ATOM   5591 C  CB  . VAL C  1 165 ? 42.909  5.900   -15.100 1.00 19.04 ? 165 VAL C CB  1 
ATOM   5592 C  CG1 . VAL C  1 165 ? 44.412  6.158   -15.047 1.00 18.58 ? 165 VAL C CG1 1 
ATOM   5593 C  CG2 . VAL C  1 165 ? 42.650  4.448   -15.559 1.00 19.92 ? 165 VAL C CG2 1 
ATOM   5594 N  N   . LYS C  1 166 ? 40.186  6.263   -12.446 1.00 17.31 ? 166 LYS C N   1 
ATOM   5595 C  CA  . LYS C  1 166 ? 38.769  6.297   -12.362 1.00 16.79 ? 166 LYS C CA  1 
ATOM   5596 C  C   . LYS C  1 166 ? 38.104  7.518   -12.929 1.00 18.04 ? 166 LYS C C   1 
ATOM   5597 O  O   . LYS C  1 166 ? 36.955  7.430   -13.359 1.00 18.78 ? 166 LYS C O   1 
ATOM   5598 C  CB  . LYS C  1 166 ? 38.247  6.035   -10.896 1.00 19.16 ? 166 LYS C CB  1 
ATOM   5599 C  CG  . LYS C  1 166 ? 38.703  4.723   -10.353 1.00 23.28 ? 166 LYS C CG  1 
ATOM   5600 C  CD  . LYS C  1 166 ? 38.105  4.497   -8.936  1.00 24.52 ? 166 LYS C CD  1 
ATOM   5601 C  CE  . LYS C  1 166 ? 36.586  4.319   -8.957  1.00 23.37 ? 166 LYS C CE  1 
ATOM   5602 N  NZ  . LYS C  1 166 ? 36.206  2.940   -9.403  1.00 22.86 ? 166 LYS C NZ  1 
ATOM   5603 N  N   . TYR C  1 167 ? 38.773  8.642   -12.918 1.00 16.96 ? 167 TYR C N   1 
ATOM   5604 C  CA  . TYR C  1 167 ? 38.093  9.853   -13.295 1.00 18.11 ? 167 TYR C CA  1 
ATOM   5605 C  C   . TYR C  1 167 ? 38.683  10.400  -14.546 1.00 18.18 ? 167 TYR C C   1 
ATOM   5606 O  O   . TYR C  1 167 ? 39.912  10.239  -14.799 1.00 23.09 ? 167 TYR C O   1 
ATOM   5607 C  CB  . TYR C  1 167 ? 38.174  10.944  -12.200 1.00 18.91 ? 167 TYR C CB  1 
ATOM   5608 C  CG  . TYR C  1 167 ? 37.562  10.509  -10.880 1.00 20.20 ? 167 TYR C CG  1 
ATOM   5609 C  CD1 . TYR C  1 167 ? 36.182  10.501  -10.702 1.00 22.21 ? 167 TYR C CD1 1 
ATOM   5610 C  CD2 . TYR C  1 167 ? 38.397  10.077  -9.824  1.00 20.63 ? 167 TYR C CD2 1 
ATOM   5611 C  CE1 . TYR C  1 167 ? 35.615  10.118  -9.479  1.00 26.10 ? 167 TYR C CE1 1 
ATOM   5612 C  CE2 . TYR C  1 167 ? 37.858  9.630   -8.618  1.00 24.23 ? 167 TYR C CE2 1 
ATOM   5613 C  CZ  . TYR C  1 167 ? 36.471  9.675   -8.448  1.00 26.80 ? 167 TYR C CZ  1 
ATOM   5614 O  OH  . TYR C  1 167 ? 35.922  9.259   -7.241  1.00 32.75 ? 167 TYR C OH  1 
ATOM   5615 N  N   . LYS C  1 168 ? 37.837  11.221  -15.198 1.00 19.53 ? 168 LYS C N   1 
ATOM   5616 C  CA  . LYS C  1 168 ? 38.195  11.800  -16.441 1.00 20.48 ? 168 LYS C CA  1 
ATOM   5617 C  C   . LYS C  1 168 ? 39.417  12.635  -16.247 1.00 23.84 ? 168 LYS C C   1 
ATOM   5618 O  O   . LYS C  1 168 ? 39.466  13.490  -15.308 1.00 23.81 ? 168 LYS C O   1 
ATOM   5619 C  CB  . LYS C  1 168 ? 37.048  12.694  -16.988 1.00 22.79 ? 168 LYS C CB  1 
ATOM   5620 C  CG  . LYS C  1 168 ? 37.456  13.412  -18.267 1.00 24.50 ? 168 LYS C CG  1 
ATOM   5621 C  CD  . LYS C  1 168 ? 36.305  14.223  -18.820 1.00 28.59 ? 168 LYS C CD  1 
ATOM   5622 C  CE  . LYS C  1 168 ? 36.914  15.390  -19.545 1.00 34.76 ? 168 LYS C CE  1 
ATOM   5623 N  NZ  . LYS C  1 168 ? 37.020  15.175  -20.995 1.00 36.07 ? 168 LYS C NZ  1 
ATOM   5624 N  N   . GLY C  1 169 ? 40.394  12.421  -17.123 1.00 21.53 ? 169 GLY C N   1 
ATOM   5625 C  CA  . GLY C  1 169 ? 41.587  13.229  -17.117 1.00 22.80 ? 169 GLY C CA  1 
ATOM   5626 C  C   . GLY C  1 169 ? 42.720  12.546  -16.384 1.00 21.14 ? 169 GLY C C   1 
ATOM   5627 O  O   . GLY C  1 169 ? 43.858  12.948  -16.492 1.00 24.96 ? 169 GLY C O   1 
ATOM   5628 N  N   . GLN C  1 170 ? 42.430  11.527  -15.569 1.00 18.66 ? 170 GLN C N   1 
ATOM   5629 C  CA  . GLN C  1 170 ? 43.467  10.889  -14.847 1.00 17.65 ? 170 GLN C CA  1 
ATOM   5630 C  C   . GLN C  1 170 ? 44.298  9.970   -15.661 1.00 20.47 ? 170 GLN C C   1 
ATOM   5631 O  O   . GLN C  1 170 ? 43.800  9.399   -16.678 1.00 19.95 ? 170 GLN C O   1 
ATOM   5632 C  CB  . GLN C  1 170 ? 42.883  10.061  -13.662 1.00 18.78 ? 170 GLN C CB  1 
ATOM   5633 C  CG  . GLN C  1 170 ? 42.268  10.993  -12.605 1.00 17.58 ? 170 GLN C CG  1 
ATOM   5634 C  CD  . GLN C  1 170 ? 41.779  10.238  -11.354 1.00 20.41 ? 170 GLN C CD  1 
ATOM   5635 O  OE1 . GLN C  1 170 ? 41.287  9.079   -11.435 1.00 18.51 ? 170 GLN C OE1 1 
ATOM   5636 N  NE2 . GLN C  1 170 ? 41.990  10.853  -10.141 1.00 22.90 ? 170 GLN C NE2 1 
ATOM   5637 N  N   . GLU C  1 171 ? 45.540  9.835   -15.244 1.00 20.30 ? 171 GLU C N   1 
ATOM   5638 C  CA  . GLU C  1 171 ? 46.540  9.060   -15.986 1.00 22.40 ? 171 GLU C CA  1 
ATOM   5639 C  C   . GLU C  1 171 ? 47.330  8.174   -15.067 1.00 23.06 ? 171 GLU C C   1 
ATOM   5640 O  O   . GLU C  1 171 ? 47.562  8.547   -13.874 1.00 23.29 ? 171 GLU C O   1 
ATOM   5641 C  CB  . GLU C  1 171 ? 47.535  9.997   -16.740 1.00 22.27 ? 171 GLU C CB  1 
ATOM   5642 C  CG  . GLU C  1 171 ? 46.885  10.867  -17.813 1.00 26.56 ? 171 GLU C CG  1 
ATOM   5643 C  CD  . GLU C  1 171 ? 47.762  11.969  -18.361 1.00 29.90 ? 171 GLU C CD  1 
ATOM   5644 O  OE1 . GLU C  1 171 ? 48.896  12.102  -17.865 1.00 28.42 ? 171 GLU C OE1 1 
ATOM   5645 O  OE2 . GLU C  1 171 ? 47.260  12.663  -19.299 1.00 33.76 ? 171 GLU C OE2 1 
ATOM   5646 N  N   . ALA C  1 172 ? 47.848  7.095   -15.628 1.00 19.29 ? 172 ALA C N   1 
ATOM   5647 C  CA  . ALA C  1 172 ? 48.702  6.162   -14.893 1.00 20.92 ? 172 ALA C CA  1 
ATOM   5648 C  C   . ALA C  1 172 ? 49.546  5.393   -15.837 1.00 25.74 ? 172 ALA C C   1 
ATOM   5649 O  O   . ALA C  1 172 ? 49.279  5.360   -17.025 1.00 28.97 ? 172 ALA C O   1 
ATOM   5650 C  CB  . ALA C  1 172 ? 47.865  5.257   -14.003 1.00 20.98 ? 172 ALA C CB  1 
ATOM   5651 N  N   . PHE C  1 173 ? 50.639  4.827   -15.369 1.00 25.66 ? 173 PHE C N   1 
ATOM   5652 C  CA  . PHE C  1 173 ? 51.454  3.939   -16.234 1.00 24.71 ? 173 PHE C CA  1 
ATOM   5653 C  C   . PHE C  1 173 ? 51.128  2.438   -16.057 1.00 26.13 ? 173 PHE C C   1 
ATOM   5654 O  O   . PHE C  1 173 ? 50.693  1.991   -14.983 1.00 24.34 ? 173 PHE C O   1 
ATOM   5655 C  CB  . PHE C  1 173 ? 52.940  4.228   -16.222 1.00 20.94 ? 173 PHE C CB  1 
ATOM   5656 C  CG  . PHE C  1 173 ? 53.351  5.595   -16.808 1.00 21.29 ? 173 PHE C CG  1 
ATOM   5657 C  CD1 . PHE C  1 173 ? 53.397  6.739   -15.993 1.00 23.14 ? 173 PHE C CD1 1 
ATOM   5658 C  CD2 . PHE C  1 173 ? 53.743  5.724   -18.152 1.00 24.49 ? 173 PHE C CD2 1 
ATOM   5659 C  CE1 . PHE C  1 173 ? 53.771  7.982   -16.538 1.00 23.91 ? 173 PHE C CE1 1 
ATOM   5660 C  CE2 . PHE C  1 173 ? 54.112  6.963   -18.708 1.00 25.65 ? 173 PHE C CE2 1 
ATOM   5661 C  CZ  . PHE C  1 173 ? 54.138  8.094   -17.892 1.00 24.12 ? 173 PHE C CZ  1 
ATOM   5662 N  N   . VAL C  1 174 ? 51.174  1.752   -17.187 1.00 21.91 ? 174 VAL C N   1 
ATOM   5663 C  CA  . VAL C  1 174 ? 51.009  0.277   -17.289 1.00 24.59 ? 174 VAL C CA  1 
ATOM   5664 C  C   . VAL C  1 174 ? 52.368  -0.225  -17.777 1.00 24.83 ? 174 VAL C C   1 
ATOM   5665 O  O   . VAL C  1 174 ? 52.911  0.291   -18.754 1.00 26.54 ? 174 VAL C O   1 
ATOM   5666 C  CB  . VAL C  1 174 ? 49.900  -0.128  -18.320 1.00 22.67 ? 174 VAL C CB  1 
ATOM   5667 C  CG1 . VAL C  1 174 ? 49.989  -1.629  -18.645 1.00 26.20 ? 174 VAL C CG1 1 
ATOM   5668 C  CG2 . VAL C  1 174 ? 48.499  0.269   -17.792 1.00 29.67 ? 174 VAL C CG2 1 
ATOM   5669 N  N   . PRO C  1 175 ? 52.948  -1.258  -17.101 1.00 26.09 ? 175 PRO C N   1 
ATOM   5670 C  CA  . PRO C  1 175 ? 54.199  -1.838  -17.639 1.00 21.91 ? 175 PRO C CA  1 
ATOM   5671 C  C   . PRO C  1 175 ? 53.950  -2.472  -19.011 1.00 25.13 ? 175 PRO C C   1 
ATOM   5672 O  O   . PRO C  1 175 ? 52.873  -2.934  -19.239 1.00 24.15 ? 175 PRO C O   1 
ATOM   5673 C  CB  . PRO C  1 175 ? 54.600  -2.925  -16.603 1.00 25.02 ? 175 PRO C CB  1 
ATOM   5674 C  CG  . PRO C  1 175 ? 53.631  -2.793  -15.480 1.00 25.30 ? 175 PRO C CG  1 
ATOM   5675 C  CD  . PRO C  1 175 ? 52.540  -1.809  -15.790 1.00 23.25 ? 175 PRO C CD  1 
ATOM   5676 N  N   . GLY C  1 176 ? 54.967  -2.528  -19.849 1.00 21.86 ? 176 GLY C N   1 
ATOM   5677 C  CA  . GLY C  1 176 ? 54.936  -3.178  -21.129 1.00 24.56 ? 176 GLY C CA  1 
ATOM   5678 C  C   . GLY C  1 176 ? 54.562  -4.633  -20.995 1.00 26.51 ? 176 GLY C C   1 
ATOM   5679 O  O   . GLY C  1 176 ? 54.763  -5.279  -19.948 1.00 22.86 ? 176 GLY C O   1 
ATOM   5680 N  N   . PHE C  1 177 ? 54.015  -5.141  -22.102 1.00 23.07 ? 177 PHE C N   1 
ATOM   5681 C  CA  . PHE C  1 177 ? 53.733  -6.610  -22.237 1.00 21.09 ? 177 PHE C CA  1 
ATOM   5682 C  C   . PHE C  1 177 ? 53.568  -6.814  -23.767 1.00 21.66 ? 177 PHE C C   1 
ATOM   5683 O  O   . PHE C  1 177 ? 53.631  -5.843  -24.514 1.00 21.22 ? 177 PHE C O   1 
ATOM   5684 C  CB  . PHE C  1 177 ? 52.534  -7.010  -21.374 1.00 22.75 ? 177 PHE C CB  1 
ATOM   5685 C  CG  . PHE C  1 177 ? 51.217  -6.466  -21.853 1.00 25.01 ? 177 PHE C CG  1 
ATOM   5686 C  CD1 . PHE C  1 177 ? 50.838  -5.170  -21.520 1.00 23.93 ? 177 PHE C CD1 1 
ATOM   5687 C  CD2 . PHE C  1 177 ? 50.366  -7.230  -22.645 1.00 24.05 ? 177 PHE C CD2 1 
ATOM   5688 C  CE1 . PHE C  1 177 ? 49.631  -4.636  -21.962 1.00 27.99 ? 177 PHE C CE1 1 
ATOM   5689 C  CE2 . PHE C  1 177 ? 49.131  -6.705  -23.108 1.00 23.93 ? 177 PHE C CE2 1 
ATOM   5690 C  CZ  . PHE C  1 177 ? 48.765  -5.419  -22.751 1.00 25.40 ? 177 PHE C CZ  1 
ATOM   5691 N  N   . ASN C  1 178 ? 53.354  -8.037  -24.235 1.00 22.99 ? 178 ASN C N   1 
ATOM   5692 C  CA  . ASN C  1 178 ? 53.276  -8.297  -25.646 1.00 20.55 ? 178 ASN C CA  1 
ATOM   5693 C  C   . ASN C  1 178 ? 51.817  -8.083  -26.114 1.00 20.09 ? 178 ASN C C   1 
ATOM   5694 O  O   . ASN C  1 178 ? 50.900  -8.777  -25.725 1.00 18.14 ? 178 ASN C O   1 
ATOM   5695 C  CB  . ASN C  1 178 ? 53.665  -9.734  -25.844 1.00 21.10 ? 178 ASN C CB  1 
ATOM   5696 C  CG  . ASN C  1 178 ? 53.575  -10.132 -27.288 1.00 20.14 ? 178 ASN C CG  1 
ATOM   5697 O  OD1 . ASN C  1 178 ? 53.431  -9.273  -28.208 1.00 18.61 ? 178 ASN C OD1 1 
ATOM   5698 N  ND2 . ASN C  1 178 ? 53.603  -11.455 -27.517 1.00 22.16 ? 178 ASN C ND2 1 
ATOM   5699 N  N   . ILE C  1 179 ? 51.642  -6.982  -26.871 1.00 19.71 ? 179 ILE C N   1 
ATOM   5700 C  CA  . ILE C  1 179 ? 50.309  -6.542  -27.288 1.00 18.00 ? 179 ILE C CA  1 
ATOM   5701 C  C   . ILE C  1 179 ? 49.709  -7.599  -28.165 1.00 18.43 ? 179 ILE C C   1 
ATOM   5702 O  O   . ILE C  1 179 ? 48.453  -7.714  -28.192 1.00 16.24 ? 179 ILE C O   1 
ATOM   5703 C  CB  . ILE C  1 179 ? 50.453  -5.185  -27.986 1.00 16.03 ? 179 ILE C CB  1 
ATOM   5704 C  CG1 . ILE C  1 179 ? 51.019  -4.065  -27.040 1.00 17.21 ? 179 ILE C CG1 1 
ATOM   5705 C  CG2 . ILE C  1 179 ? 49.085  -4.702  -28.522 1.00 15.88 ? 179 ILE C CG2 1 
ATOM   5706 C  CD1 . ILE C  1 179 ? 50.350  -3.927  -25.667 1.00 18.20 ? 179 ILE C CD1 1 
ATOM   5707 N  N   . GLU C  1 180 ? 50.525  -8.411  -28.795 1.00 17.64 ? 180 GLU C N   1 
ATOM   5708 C  CA  . GLU C  1 180 ? 49.995  -9.498  -29.623 1.00 17.67 ? 180 GLU C CA  1 
ATOM   5709 C  C   . GLU C  1 180 ? 49.150  -10.514 -28.812 1.00 19.40 ? 180 GLU C C   1 
ATOM   5710 O  O   . GLU C  1 180 ? 48.311  -11.221 -29.384 1.00 17.35 ? 180 GLU C O   1 
ATOM   5711 C  CB  . GLU C  1 180 ? 51.074  -10.181 -30.418 1.00 19.43 ? 180 GLU C CB  1 
ATOM   5712 C  CG  . GLU C  1 180 ? 50.497  -11.049 -31.515 1.00 22.16 ? 180 GLU C CG  1 
ATOM   5713 C  CD  . GLU C  1 180 ? 51.543  -11.497 -32.534 1.00 27.98 ? 180 GLU C CD  1 
ATOM   5714 O  OE1 . GLU C  1 180 ? 52.761  -11.177 -32.384 1.00 26.97 ? 180 GLU C OE1 1 
ATOM   5715 O  OE2 . GLU C  1 180 ? 51.114  -12.239 -33.451 1.00 27.92 ? 180 GLU C OE2 1 
ATOM   5716 N  N   . GLU C  1 181 ? 49.380  -10.588 -27.508 1.00 15.31 ? 181 GLU C N   1 
ATOM   5717 C  CA  . GLU C  1 181 ? 48.560  -11.451 -26.622 1.00 18.25 ? 181 GLU C CA  1 
ATOM   5718 C  C   . GLU C  1 181 ? 47.093  -11.037 -26.556 1.00 18.47 ? 181 GLU C C   1 
ATOM   5719 O  O   . GLU C  1 181 ? 46.252  -11.831 -26.128 1.00 19.16 ? 181 GLU C O   1 
ATOM   5720 C  CB  . GLU C  1 181 ? 49.162  -11.445 -25.210 1.00 21.02 ? 181 GLU C CB  1 
ATOM   5721 C  CG  . GLU C  1 181 ? 50.495  -12.198 -25.042 1.00 25.35 ? 181 GLU C CG  1 
ATOM   5722 C  CD  . GLU C  1 181 ? 51.120  -11.911 -23.682 1.00 24.00 ? 181 GLU C CD  1 
ATOM   5723 O  OE1 . GLU C  1 181 ? 50.384  -11.549 -22.701 1.00 25.63 ? 181 GLU C OE1 1 
ATOM   5724 O  OE2 . GLU C  1 181 ? 52.383  -11.983 -23.559 1.00 27.81 ? 181 GLU C OE2 1 
ATOM   5725 N  N   . LEU C  1 182 ? 46.828  -9.784  -26.969 1.00 16.01 ? 182 LEU C N   1 
ATOM   5726 C  CA  . LEU C  1 182 ? 45.442  -9.287  -26.977 1.00 14.87 ? 182 LEU C CA  1 
ATOM   5727 C  C   . LEU C  1 182 ? 44.658  -9.735  -28.185 1.00 15.19 ? 182 LEU C C   1 
ATOM   5728 O  O   . LEU C  1 182 ? 43.417  -9.607  -28.212 1.00 15.61 ? 182 LEU C O   1 
ATOM   5729 C  CB  . LEU C  1 182 ? 45.463  -7.745  -26.834 1.00 15.52 ? 182 LEU C CB  1 
ATOM   5730 C  CG  . LEU C  1 182 ? 46.098  -7.130  -25.595 1.00 15.24 ? 182 LEU C CG  1 
ATOM   5731 C  CD1 . LEU C  1 182 ? 46.043  -5.621  -25.690 1.00 16.70 ? 182 LEU C CD1 1 
ATOM   5732 C  CD2 . LEU C  1 182 ? 45.572  -7.691  -24.208 1.00 15.45 ? 182 LEU C CD2 1 
ATOM   5733 N  N   . LEU C  1 183 ? 45.355  -10.299 -29.210 1.00 15.48 ? 183 LEU C N   1 
ATOM   5734 C  CA  . LEU C  1 183 ? 44.743  -10.729 -30.458 1.00 16.49 ? 183 LEU C CA  1 
ATOM   5735 C  C   . LEU C  1 183 ? 44.185  -12.129 -30.303 1.00 17.63 ? 183 LEU C C   1 
ATOM   5736 O  O   . LEU C  1 183 ? 44.695  -12.934 -29.445 1.00 20.25 ? 183 LEU C O   1 
ATOM   5737 C  CB  . LEU C  1 183 ? 45.716  -10.651 -31.652 1.00 17.89 ? 183 LEU C CB  1 
ATOM   5738 C  CG  . LEU C  1 183 ? 46.360  -9.276  -31.816 1.00 15.92 ? 183 LEU C CG  1 
ATOM   5739 C  CD1 . LEU C  1 183 ? 47.221  -9.326  -33.087 1.00 20.25 ? 183 LEU C CD1 1 
ATOM   5740 C  CD2 . LEU C  1 183 ? 45.290  -8.225  -31.929 1.00 19.17 ? 183 LEU C CD2 1 
ATOM   5741 N  N   . PRO C  1 184 ? 43.177  -12.463 -31.117 1.00 15.68 ? 184 PRO C N   1 
ATOM   5742 C  CA  . PRO C  1 184 ? 42.511  -13.755 -31.055 1.00 17.50 ? 184 PRO C CA  1 
ATOM   5743 C  C   . PRO C  1 184 ? 43.274  -14.850 -31.788 1.00 19.67 ? 184 PRO C C   1 
ATOM   5744 O  O   . PRO C  1 184 ? 44.320  -14.607 -32.417 1.00 19.17 ? 184 PRO C O   1 
ATOM   5745 C  CB  . PRO C  1 184 ? 41.130  -13.476 -31.694 1.00 17.52 ? 184 PRO C CB  1 
ATOM   5746 C  CG  . PRO C  1 184 ? 41.473  -12.473 -32.747 1.00 15.03 ? 184 PRO C CG  1 
ATOM   5747 C  CD  . PRO C  1 184 ? 42.461  -11.544 -32.042 1.00 14.09 ? 184 PRO C CD  1 
ATOM   5748 N  N   . GLU C  1 185 ? 42.724  -16.058 -31.697 1.00 20.57 ? 185 GLU C N   1 
ATOM   5749 C  CA  . GLU C  1 185 ? 43.156  -17.166 -32.520 1.00 25.14 ? 185 GLU C CA  1 
ATOM   5750 C  C   . GLU C  1 185 ? 42.925  -16.907 -34.011 1.00 22.38 ? 185 GLU C C   1 
ATOM   5751 O  O   . GLU C  1 185 ? 41.969  -16.146 -34.441 1.00 22.26 ? 185 GLU C O   1 
ATOM   5752 C  CB  . GLU C  1 185 ? 42.396  -18.436 -32.114 1.00 30.42 ? 185 GLU C CB  1 
ATOM   5753 C  CG  . GLU C  1 185 ? 42.736  -18.934 -30.691 1.00 35.87 ? 185 GLU C CG  1 
ATOM   5754 C  CD  . GLU C  1 185 ? 43.831  -19.992 -30.637 1.00 49.10 ? 185 GLU C CD  1 
ATOM   5755 O  OE1 . GLU C  1 185 ? 44.727  -19.985 -31.510 1.00 44.03 ? 185 GLU C OE1 1 
ATOM   5756 O  OE2 . GLU C  1 185 ? 43.803  -20.839 -29.699 1.00 52.94 ? 185 GLU C OE2 1 
ATOM   5757 N  N   A ARG C  1 186 ? 43.726  -17.583 -34.835 0.50 21.31 ? 186 ARG C N   1 
ATOM   5758 N  N   B ARG C  1 186 ? 43.863  -17.428 -34.797 0.50 19.16 ? 186 ARG C N   1 
ATOM   5759 C  CA  A ARG C  1 186 ? 43.655  -17.443 -36.301 0.50 21.32 ? 186 ARG C CA  1 
ATOM   5760 C  CA  B ARG C  1 186 ? 43.754  -17.378 -36.254 0.50 18.86 ? 186 ARG C CA  1 
ATOM   5761 C  C   A ARG C  1 186 ? 43.514  -15.989 -36.803 0.50 19.33 ? 186 ARG C C   1 
ATOM   5762 C  C   B ARG C  1 186 ? 43.527  -15.983 -36.792 0.50 17.75 ? 186 ARG C C   1 
ATOM   5763 O  O   A ARG C  1 186 ? 42.594  -15.673 -37.580 0.50 21.21 ? 186 ARG C O   1 
ATOM   5764 O  O   B ARG C  1 186 ? 42.602  -15.708 -37.580 0.50 19.57 ? 186 ARG C O   1 
ATOM   5765 C  CB  A ARG C  1 186 ? 42.586  -18.378 -36.898 0.50 23.36 ? 186 ARG C CB  1 
ATOM   5766 C  CB  B ARG C  1 186 ? 42.719  -18.367 -36.704 0.50 18.64 ? 186 ARG C CB  1 
ATOM   5767 C  CG  A ARG C  1 186 ? 42.936  -19.878 -36.781 0.50 27.53 ? 186 ARG C CG  1 
ATOM   5768 C  CG  B ARG C  1 186 ? 43.131  -19.725 -36.173 0.50 18.74 ? 186 ARG C CG  1 
ATOM   5769 C  CD  A ARG C  1 186 ? 41.911  -20.832 -37.425 0.50 27.36 ? 186 ARG C CD  1 
ATOM   5770 C  CD  B ARG C  1 186 ? 42.125  -20.795 -36.560 0.50 19.56 ? 186 ARG C CD  1 
ATOM   5771 N  NE  A ARG C  1 186 ? 40.524  -20.499 -37.026 0.50 30.72 ? 186 ARG C NE  1 
ATOM   5772 N  NE  B ARG C  1 186 ? 40.973  -20.681 -35.649 0.50 21.61 ? 186 ARG C NE  1 
ATOM   5773 C  CZ  A ARG C  1 186 ? 39.385  -21.034 -37.493 0.50 31.07 ? 186 ARG C CZ  1 
ATOM   5774 C  CZ  B ARG C  1 186 ? 40.994  -21.081 -34.395 0.50 19.92 ? 186 ARG C CZ  1 
ATOM   5775 N  NH1 A ARG C  1 186 ? 39.364  -21.952 -38.452 0.50 28.75 ? 186 ARG C NH1 1 
ATOM   5776 N  NH1 B ARG C  1 186 ? 42.080  -21.662 -33.923 0.50 22.33 ? 186 ARG C NH1 1 
ATOM   5777 N  NH2 A ARG C  1 186 ? 38.232  -20.582 -37.021 0.50 26.86 ? 186 ARG C NH2 1 
ATOM   5778 N  NH2 B ARG C  1 186 ? 39.934  -20.911 -33.614 0.50 24.47 ? 186 ARG C NH2 1 
ATOM   5779 N  N   . THR C  1 187 ? 44.472  -15.137 -36.449 1.00 18.31 ? 187 THR C N   1 
ATOM   5780 C  CA  . THR C  1 187 ? 44.447  -13.775 -36.978 1.00 17.61 ? 187 THR C CA  1 
ATOM   5781 C  C   . THR C  1 187 ? 44.366  -13.689 -38.533 1.00 17.59 ? 187 THR C C   1 
ATOM   5782 O  O   . THR C  1 187 ? 44.010  -12.655 -39.052 1.00 15.58 ? 187 THR C O   1 
ATOM   5783 C  CB  . THR C  1 187 ? 45.519  -12.857 -36.401 1.00 19.07 ? 187 THR C CB  1 
ATOM   5784 O  OG1 . THR C  1 187 ? 46.799  -13.437 -36.631 1.00 22.24 ? 187 THR C OG1 1 
ATOM   5785 C  CG2 . THR C  1 187 ? 45.327  -12.685 -34.884 1.00 18.51 ? 187 THR C CG2 1 
ATOM   5786 N  N   . ALA C  1 188 ? 44.731  -14.763 -39.265 1.00 16.19 ? 188 ALA C N   1 
ATOM   5787 C  CA  . ALA C  1 188 ? 44.600  -14.754 -40.696 1.00 16.29 ? 188 ALA C CA  1 
ATOM   5788 C  C   . ALA C  1 188 ? 43.089  -14.621 -41.235 1.00 13.84 ? 188 ALA C C   1 
ATOM   5789 O  O   . ALA C  1 188 ? 42.841  -14.262 -42.433 1.00 14.98 ? 188 ALA C O   1 
ATOM   5790 C  CB  . ALA C  1 188 ? 45.376  -15.939 -41.341 1.00 18.83 ? 188 ALA C CB  1 
ATOM   5791 N  N   . GLU C  1 189 ? 42.148  -14.869 -40.320 1.00 15.70 ? 189 GLU C N   1 
ATOM   5792 C  CA  . GLU C  1 189 ? 40.729  -14.821 -40.618 1.00 17.10 ? 189 GLU C CA  1 
ATOM   5793 C  C   . GLU C  1 189 ? 40.125  -13.499 -40.167 1.00 13.70 ? 189 GLU C C   1 
ATOM   5794 O  O   . GLU C  1 189 ? 40.120  -13.230 -38.949 1.00 14.52 ? 189 GLU C O   1 
ATOM   5795 C  CB  . GLU C  1 189 ? 39.979  -15.962 -39.956 1.00 19.17 ? 189 GLU C CB  1 
ATOM   5796 C  CG  . GLU C  1 189 ? 40.457  -17.325 -40.448 1.00 23.39 ? 189 GLU C CG  1 
ATOM   5797 C  CD  . GLU C  1 189 ? 39.964  -18.477 -39.543 1.00 27.66 ? 189 GLU C CD  1 
ATOM   5798 O  OE1 . GLU C  1 189 ? 39.055  -18.305 -38.665 1.00 25.88 ? 189 GLU C OE1 1 
ATOM   5799 O  OE2 . GLU C  1 189 ? 40.531  -19.576 -39.700 1.00 29.79 ? 189 GLU C OE2 1 
ATOM   5800 N  N   . TYR C  1 190 ? 39.783  -12.661 -41.156 1.00 12.42 ? 190 TYR C N   1 
ATOM   5801 C  CA  . TYR C  1 190 ? 39.263  -11.326 -40.766 1.00 11.64 ? 190 TYR C CA  1 
ATOM   5802 C  C   . TYR C  1 190 ? 38.356  -10.746 -41.832 1.00 11.75 ? 190 TYR C C   1 
ATOM   5803 O  O   . TYR C  1 190 ? 38.334  -11.154 -42.969 1.00 11.87 ? 190 TYR C O   1 
ATOM   5804 C  CB  . TYR C  1 190 ? 40.474  -10.377 -40.505 1.00 12.80 ? 190 TYR C CB  1 
ATOM   5805 C  CG  . TYR C  1 190 ? 41.433  -10.185 -41.690 1.00 13.31 ? 190 TYR C CG  1 
ATOM   5806 C  CD1 . TYR C  1 190 ? 41.184  -9.231  -42.715 1.00 13.48 ? 190 TYR C CD1 1 
ATOM   5807 C  CD2 . TYR C  1 190 ? 42.587  -10.931 -41.756 1.00 14.19 ? 190 TYR C CD2 1 
ATOM   5808 C  CE1 . TYR C  1 190 ? 42.105  -9.074  -43.805 1.00 12.14 ? 190 TYR C CE1 1 
ATOM   5809 C  CE2 . TYR C  1 190 ? 43.482  -10.747 -42.792 1.00 12.82 ? 190 TYR C CE2 1 
ATOM   5810 C  CZ  . TYR C  1 190 ? 43.242  -9.865  -43.777 1.00 14.44 ? 190 TYR C CZ  1 
ATOM   5811 O  OH  . TYR C  1 190 ? 44.160  -9.672  -44.791 1.00 14.98 ? 190 TYR C OH  1 
ATOM   5812 N  N   . TYR C  1 191 ? 37.559  -9.743  -41.383 1.00 10.30 ? 191 TYR C N   1 
ATOM   5813 C  CA  . TYR C  1 191 ? 36.754  -8.872  -42.247 1.00 10.09 ? 191 TYR C CA  1 
ATOM   5814 C  C   . TYR C  1 191 ? 37.546  -7.612  -42.557 1.00 9.34  ? 191 TYR C C   1 
ATOM   5815 O  O   . TYR C  1 191 ? 38.267  -7.107  -41.640 1.00 10.65 ? 191 TYR C O   1 
ATOM   5816 C  CB  . TYR C  1 191 ? 35.473  -8.521  -41.489 1.00 10.03 ? 191 TYR C CB  1 
ATOM   5817 C  CG  . TYR C  1 191 ? 34.648  -9.670  -40.952 1.00 10.12 ? 191 TYR C CG  1 
ATOM   5818 C  CD1 . TYR C  1 191 ? 33.583  -10.195 -41.717 1.00 10.67 ? 191 TYR C CD1 1 
ATOM   5819 C  CD2 . TYR C  1 191 ? 34.820  -10.058 -39.582 1.00 9.83  ? 191 TYR C CD2 1 
ATOM   5820 C  CE1 . TYR C  1 191 ? 32.791  -11.165 -41.131 1.00 11.14 ? 191 TYR C CE1 1 
ATOM   5821 C  CE2 . TYR C  1 191 ? 33.980  -11.017 -38.990 1.00 10.64 ? 191 TYR C CE2 1 
ATOM   5822 C  CZ  . TYR C  1 191 ? 33.018  -11.567 -39.821 1.00 11.43 ? 191 TYR C CZ  1 
ATOM   5823 O  OH  . TYR C  1 191 ? 32.152  -12.517 -39.232 1.00 14.83 ? 191 TYR C OH  1 
ATOM   5824 N  N   . ARG C  1 192 ? 37.381  -7.094  -43.777 1.00 9.50  ? 192 ARG C N   1 
ATOM   5825 C  CA  . ARG C  1 192 ? 38.067  -5.855  -44.125 1.00 9.52  ? 192 ARG C CA  1 
ATOM   5826 C  C   . ARG C  1 192 ? 37.092  -4.913  -44.840 1.00 10.09 ? 192 ARG C C   1 
ATOM   5827 O  O   . ARG C  1 192 ? 36.352  -5.349  -45.794 1.00 10.67 ? 192 ARG C O   1 
ATOM   5828 C  CB  . ARG C  1 192 ? 39.162  -6.235  -45.120 1.00 10.89 ? 192 ARG C CB  1 
ATOM   5829 C  CG  . ARG C  1 192 ? 39.823  -5.053  -45.894 1.00 10.27 ? 192 ARG C CG  1 
ATOM   5830 C  CD  . ARG C  1 192 ? 40.578  -4.075  -45.005 1.00 11.48 ? 192 ARG C CD  1 
ATOM   5831 N  NE  . ARG C  1 192 ? 41.539  -4.721  -44.115 1.00 11.01 ? 192 ARG C NE  1 
ATOM   5832 C  CZ  . ARG C  1 192 ? 42.707  -5.228  -44.501 1.00 12.47 ? 192 ARG C CZ  1 
ATOM   5833 N  NH1 . ARG C  1 192 ? 43.073  -5.178  -45.774 1.00 13.64 ? 192 ARG C NH1 1 
ATOM   5834 N  NH2 . ARG C  1 192 ? 43.509  -5.791  -43.607 1.00 13.58 ? 192 ARG C NH2 1 
ATOM   5835 N  N   . TYR C  1 193 ? 37.088  -3.643  -44.409 1.00 8.71  ? 193 TYR C N   1 
ATOM   5836 C  CA  . TYR C  1 193 ? 36.337  -2.674  -45.207 1.00 8.90  ? 193 TYR C CA  1 
ATOM   5837 C  C   . TYR C  1 193 ? 36.885  -1.273  -44.963 1.00 8.11  ? 193 TYR C C   1 
ATOM   5838 O  O   . TYR C  1 193 ? 37.565  -1.062  -43.925 1.00 9.32  ? 193 TYR C O   1 
ATOM   5839 C  CB  . TYR C  1 193 ? 34.790  -2.747  -44.907 1.00 8.98  ? 193 TYR C CB  1 
ATOM   5840 C  CG  . TYR C  1 193 ? 34.397  -2.186  -43.547 1.00 7.39  ? 193 TYR C CG  1 
ATOM   5841 C  CD1 . TYR C  1 193 ? 34.622  -2.931  -42.402 1.00 7.76  ? 193 TYR C CD1 1 
ATOM   5842 C  CD2 . TYR C  1 193 ? 33.881  -0.908  -43.496 1.00 7.86  ? 193 TYR C CD2 1 
ATOM   5843 C  CE1 . TYR C  1 193 ? 34.263  -2.367  -41.115 1.00 7.08  ? 193 TYR C CE1 1 
ATOM   5844 C  CE2 . TYR C  1 193 ? 33.502  -0.360  -42.243 1.00 7.94  ? 193 TYR C CE2 1 
ATOM   5845 C  CZ  . TYR C  1 193 ? 33.712  -1.104  -41.077 1.00 7.68  ? 193 TYR C CZ  1 
ATOM   5846 O  OH  . TYR C  1 193 ? 33.375  -0.479  -39.877 1.00 7.97  ? 193 TYR C OH  1 
ATOM   5847 N  N   . ARG C  1 194 ? 36.572  -0.351  -45.861 1.00 9.68  ? 194 ARG C N   1 
ATOM   5848 C  CA  . ARG C  1 194 ? 36.997  1.040   -45.632 1.00 9.32  ? 194 ARG C CA  1 
ATOM   5849 C  C   . ARG C  1 194 ? 35.877  1.741   -44.871 1.00 9.63  ? 194 ARG C C   1 
ATOM   5850 O  O   . ARG C  1 194 ? 34.670  1.720   -45.254 1.00 10.25 ? 194 ARG C O   1 
ATOM   5851 C  CB  . ARG C  1 194 ? 37.073  1.750   -46.970 1.00 12.69 ? 194 ARG C CB  1 
ATOM   5852 C  CG  . ARG C  1 194 ? 38.294  1.236   -47.736 1.00 16.05 ? 194 ARG C CG  1 
ATOM   5853 C  CD  . ARG C  1 194 ? 38.636  2.054   -48.998 1.00 27.79 ? 194 ARG C CD  1 
ATOM   5854 N  NE  . ARG C  1 194 ? 39.816  1.431   -49.599 1.00 38.43 ? 194 ARG C NE  1 
ATOM   5855 C  CZ  . ARG C  1 194 ? 41.067  1.666   -49.206 1.00 51.75 ? 194 ARG C CZ  1 
ATOM   5856 N  NH1 . ARG C  1 194 ? 41.310  2.544   -48.248 1.00 45.04 ? 194 ARG C NH1 1 
ATOM   5857 N  NH2 . ARG C  1 194 ? 42.083  1.046   -49.790 1.00 53.37 ? 194 ARG C NH2 1 
ATOM   5858 N  N   . GLY C  1 195 ? 36.244  2.381   -43.783 1.00 8.59  ? 195 GLY C N   1 
ATOM   5859 C  CA  . GLY C  1 195 ? 35.248  3.125   -42.948 1.00 9.18  ? 195 GLY C CA  1 
ATOM   5860 C  C   . GLY C  1 195 ? 35.820  4.305   -42.276 1.00 8.24  ? 195 GLY C C   1 
ATOM   5861 O  O   . GLY C  1 195 ? 36.623  5.061   -42.857 1.00 10.11 ? 195 GLY C O   1 
ATOM   5862 N  N   . SER C  1 196 ? 35.319  4.558   -41.065 1.00 9.15  ? 196 SER C N   1 
ATOM   5863 C  CA  . SER C  1 196 ? 35.630  5.831   -40.371 1.00 8.99  ? 196 SER C CA  1 
ATOM   5864 C  C   . SER C  1 196 ? 36.097  5.569   -38.954 1.00 8.70  ? 196 SER C C   1 
ATOM   5865 O  O   . SER C  1 196 ? 35.968  4.471   -38.393 1.00 8.97  ? 196 SER C O   1 
ATOM   5866 C  CB  . SER C  1 196 ? 34.397  6.760   -40.323 1.00 8.48  ? 196 SER C CB  1 
ATOM   5867 O  OG  . SER C  1 196 ? 33.409  6.281   -39.361 1.00 8.54  ? 196 SER C OG  1 
ATOM   5868 N  N   . LEU C  1 197 ? 36.593  6.620   -38.325 1.00 9.35  ? 197 LEU C N   1 
ATOM   5869 C  CA  . LEU C  1 197 ? 36.636  6.584   -36.858 1.00 10.17 ? 197 LEU C CA  1 
ATOM   5870 C  C   . LEU C  1 197 ? 35.205  6.382   -36.329 1.00 9.19  ? 197 LEU C C   1 
ATOM   5871 O  O   . LEU C  1 197 ? 34.271  6.936   -36.851 1.00 10.09 ? 197 LEU C O   1 
ATOM   5872 C  CB  . LEU C  1 197 ? 37.199  7.923   -36.194 1.00 10.86 ? 197 LEU C CB  1 
ATOM   5873 C  CG  . LEU C  1 197 ? 38.695  8.173   -36.398 1.00 11.91 ? 197 LEU C CG  1 
ATOM   5874 C  CD1 . LEU C  1 197 ? 38.989  8.695   -37.764 1.00 13.33 ? 197 LEU C CD1 1 
ATOM   5875 C  CD2 . LEU C  1 197 ? 39.028  9.257   -35.463 1.00 12.26 ? 197 LEU C CD2 1 
ATOM   5876 N  N   . THR C  1 198 ? 35.076  5.642   -35.263 1.00 8.52  ? 198 THR C N   1 
ATOM   5877 C  CA  . THR C  1 198 ? 33.722  5.516   -34.661 1.00 8.52  ? 198 THR C CA  1 
ATOM   5878 C  C   . THR C  1 198 ? 33.427  6.553   -33.564 1.00 10.12 ? 198 THR C C   1 
ATOM   5879 O  O   . THR C  1 198 ? 32.374  6.529   -32.901 1.00 9.73  ? 198 THR C O   1 
ATOM   5880 C  CB  . THR C  1 198 ? 33.578  4.155   -34.030 1.00 9.07  ? 198 THR C CB  1 
ATOM   5881 O  OG1 . THR C  1 198 ? 34.483  4.056   -32.952 1.00 9.13  ? 198 THR C OG1 1 
ATOM   5882 C  CG2 . THR C  1 198 ? 33.826  2.928   -34.994 1.00 8.47  ? 198 THR C CG2 1 
ATOM   5883 N  N   . THR C  1 199 ? 34.417  7.425   -33.317 1.00 10.68 ? 199 THR C N   1 
ATOM   5884 C  CA  . THR C  1 199 ? 34.287  8.575   -32.419 1.00 10.52 ? 199 THR C CA  1 
ATOM   5885 C  C   . THR C  1 199 ? 34.498  9.826   -33.232 1.00 10.83 ? 199 THR C C   1 
ATOM   5886 O  O   . THR C  1 199 ? 35.194  9.827   -34.242 1.00 11.32 ? 199 THR C O   1 
ATOM   5887 C  CB  . THR C  1 199 ? 35.333  8.530   -31.273 1.00 12.42 ? 199 THR C CB  1 
ATOM   5888 O  OG1 . THR C  1 199 ? 36.619  8.384   -31.883 1.00 14.51 ? 199 THR C OG1 1 
ATOM   5889 C  CG2 . THR C  1 199 ? 35.195  7.211   -30.500 1.00 12.86 ? 199 THR C CG2 1 
ATOM   5890 N  N   . PRO C  1 200 ? 34.088  10.975  -32.680 1.00 10.28 ? 200 PRO C N   1 
ATOM   5891 C  CA  . PRO C  1 200 ? 34.461  12.239  -33.333 1.00 11.14 ? 200 PRO C CA  1 
ATOM   5892 C  C   . PRO C  1 200 ? 35.970  12.307  -33.472 1.00 11.98 ? 200 PRO C C   1 
ATOM   5893 O  O   . PRO C  1 200 ? 36.688  11.833  -32.556 1.00 13.37 ? 200 PRO C O   1 
ATOM   5894 C  CB  . PRO C  1 200 ? 33.924  13.280  -32.318 1.00 10.28 ? 200 PRO C CB  1 
ATOM   5895 C  CG  . PRO C  1 200 ? 32.733  12.575  -31.664 1.00 10.50 ? 200 PRO C CG  1 
ATOM   5896 C  CD  . PRO C  1 200 ? 33.115  11.137  -31.587 1.00 10.03 ? 200 PRO C CD  1 
ATOM   5897 N  N   . PRO C  1 201 ? 36.436  12.879  -34.554 1.00 11.26 ? 201 PRO C N   1 
ATOM   5898 C  CA  . PRO C  1 201 ? 35.677  13.585  -35.598 1.00 11.30 ? 201 PRO C CA  1 
ATOM   5899 C  C   . PRO C  1 201 ? 35.088  12.740  -36.748 1.00 9.96  ? 201 PRO C C   1 
ATOM   5900 O  O   . PRO C  1 201 ? 34.574  13.253  -37.715 1.00 11.65 ? 201 PRO C O   1 
ATOM   5901 C  CB  . PRO C  1 201 ? 36.718  14.588  -36.183 1.00 11.57 ? 201 PRO C CB  1 
ATOM   5902 C  CG  . PRO C  1 201 ? 37.838  14.611  -35.147 1.00 13.92 ? 201 PRO C CG  1 
ATOM   5903 C  CD  . PRO C  1 201 ? 37.910  13.156  -34.667 1.00 13.68 ? 201 PRO C CD  1 
ATOM   5904 N  N   . CYS C  1 202 ? 35.153  11.408  -36.569 1.00 10.13 ? 202 CYS C N   1 
ATOM   5905 C  CA  . CYS C  1 202 ? 34.462  10.452  -37.477 1.00 10.70 ? 202 CYS C CA  1 
ATOM   5906 C  C   . CYS C  1 202 ? 34.999  10.465  -38.887 1.00 10.19 ? 202 CYS C C   1 
ATOM   5907 O  O   . CYS C  1 202 ? 34.306  10.106  -39.851 1.00 10.76 ? 202 CYS C O   1 
ATOM   5908 C  CB  . CYS C  1 202 ? 32.904  10.709  -37.560 1.00 10.24 ? 202 CYS C CB  1 
ATOM   5909 S  SG  . CYS C  1 202 ? 32.048  10.635  -35.984 1.00 10.23 ? 202 CYS C SG  1 
ATOM   5910 N  N   . ASN C  1 203 ? 36.295  10.842  -39.109 1.00 11.09 ? 203 ASN C N   1 
ATOM   5911 C  CA  . ASN C  1 203 ? 36.797  11.007  -40.463 1.00 12.16 ? 203 ASN C CA  1 
ATOM   5912 C  C   . ASN C  1 203 ? 36.740  9.636   -41.190 1.00 10.13 ? 203 ASN C C   1 
ATOM   5913 O  O   . ASN C  1 203 ? 36.992  8.588   -40.547 1.00 9.38  ? 203 ASN C O   1 
ATOM   5914 C  CB  . ASN C  1 203 ? 38.244  11.553  -40.462 1.00 13.41 ? 203 ASN C CB  1 
ATOM   5915 C  CG  . ASN C  1 203 ? 38.390  12.763  -39.543 1.00 13.92 ? 203 ASN C CG  1 
ATOM   5916 O  OD1 . ASN C  1 203 ? 38.473  12.638  -38.308 1.00 15.13 ? 203 ASN C OD1 1 
ATOM   5917 N  ND2 . ASN C  1 203 ? 38.269  13.906  -40.148 1.00 18.74 ? 203 ASN C ND2 1 
ATOM   5918 N  N   . PRO C  1 204 ? 36.437  9.670   -42.471 1.00 10.86 ? 204 PRO C N   1 
ATOM   5919 C  CA  . PRO C  1 204 ? 36.236  8.430   -43.258 1.00 10.50 ? 204 PRO C CA  1 
ATOM   5920 C  C   . PRO C  1 204 ? 37.601  7.974   -43.793 1.00 10.56 ? 204 PRO C C   1 
ATOM   5921 O  O   . PRO C  1 204 ? 37.768  7.807   -45.030 1.00 12.95 ? 204 PRO C O   1 
ATOM   5922 C  CB  . PRO C  1 204 ? 35.267  8.838   -44.386 1.00 11.64 ? 204 PRO C CB  1 
ATOM   5923 C  CG  . PRO C  1 204 ? 35.704  10.323  -44.570 1.00 10.82 ? 204 PRO C CG  1 
ATOM   5924 C  CD  . PRO C  1 204 ? 35.932  10.875  -43.183 1.00 11.66 ? 204 PRO C CD  1 
ATOM   5925 N  N   . THR C  1 205 ? 38.526  7.773   -42.856 1.00 10.33 ? 205 THR C N   1 
ATOM   5926 C  CA  . THR C  1 205 ? 39.960  7.600   -43.191 1.00 11.88 ? 205 THR C CA  1 
ATOM   5927 C  C   . THR C  1 205 ? 40.536  6.282   -42.605 1.00 11.81 ? 205 THR C C   1 
ATOM   5928 O  O   . THR C  1 205 ? 41.796  6.073   -42.575 1.00 12.47 ? 205 THR C O   1 
ATOM   5929 C  CB  . THR C  1 205 ? 40.759  8.776   -42.627 1.00 11.57 ? 205 THR C CB  1 
ATOM   5930 O  OG1 . THR C  1 205 ? 40.482  8.801   -41.243 1.00 12.48 ? 205 THR C OG1 1 
ATOM   5931 C  CG2 . THR C  1 205 ? 40.341  10.065  -43.376 1.00 13.98 ? 205 THR C CG2 1 
ATOM   5932 N  N   . VAL C  1 206 ? 39.662  5.342   -42.153 1.00 10.68 ? 206 VAL C N   1 
ATOM   5933 C  CA  . VAL C  1 206 ? 40.099  4.141   -41.473 1.00 9.95  ? 206 VAL C CA  1 
ATOM   5934 C  C   . VAL C  1 206 ? 39.977  2.906   -42.327 1.00 9.25  ? 206 VAL C C   1 
ATOM   5935 O  O   . VAL C  1 206 ? 38.874  2.585   -42.838 1.00 10.96 ? 206 VAL C O   1 
ATOM   5936 C  CB  . VAL C  1 206 ? 39.291  3.930   -40.187 1.00 8.26  ? 206 VAL C CB  1 
ATOM   5937 C  CG1 . VAL C  1 206 ? 39.763  2.588   -39.536 1.00 8.35  ? 206 VAL C CG1 1 
ATOM   5938 C  CG2 . VAL C  1 206 ? 39.556  5.104   -39.219 1.00 8.63  ? 206 VAL C CG2 1 
ATOM   5939 N  N   . LEU C  1 207 ? 41.070  2.163   -42.505 1.00 9.38  ? 207 LEU C N   1 
ATOM   5940 C  CA  . LEU C  1 207 ? 40.987  0.819   -43.069 1.00 10.39 ? 207 LEU C CA  1 
ATOM   5941 C  C   . LEU C  1 207 ? 40.737  -0.122  -41.906 1.00 9.15  ? 207 LEU C C   1 
ATOM   5942 O  O   . LEU C  1 207 ? 41.600  -0.330  -40.993 1.00 8.92  ? 207 LEU C O   1 
ATOM   5943 C  CB  . LEU C  1 207 ? 42.307  0.487   -43.774 1.00 12.96 ? 207 LEU C CB  1 
ATOM   5944 C  CG  . LEU C  1 207 ? 42.290  -0.794  -44.570 1.00 15.14 ? 207 LEU C CG  1 
ATOM   5945 C  CD1 . LEU C  1 207 ? 41.430  -0.597  -45.816 1.00 20.05 ? 207 LEU C CD1 1 
ATOM   5946 C  CD2 . LEU C  1 207 ? 43.708  -1.088  -45.094 1.00 23.71 ? 207 LEU C CD2 1 
ATOM   5947 N  N   . TRP C  1 208 ? 39.555  -0.721  -41.875 1.00 9.34  ? 208 TRP C N   1 
ATOM   5948 C  CA  . TRP C  1 208 ? 39.180  -1.637  -40.739 1.00 9.05  ? 208 TRP C CA  1 
ATOM   5949 C  C   . TRP C  1 208 ? 39.571  -3.041  -41.000 1.00 8.37  ? 208 TRP C C   1 
ATOM   5950 O  O   . TRP C  1 208 ? 39.348  -3.567  -42.149 1.00 9.05  ? 208 TRP C O   1 
ATOM   5951 C  CB  . TRP C  1 208 ? 37.634  -1.576  -40.569 1.00 8.84  ? 208 TRP C CB  1 
ATOM   5952 C  CG  . TRP C  1 208 ? 37.219  -0.388  -39.800 1.00 8.04  ? 208 TRP C CG  1 
ATOM   5953 C  CD1 . TRP C  1 208 ? 36.760  0.802   -40.289 1.00 7.49  ? 208 TRP C CD1 1 
ATOM   5954 C  CD2 . TRP C  1 208 ? 37.327  -0.210  -38.343 1.00 7.43  ? 208 TRP C CD2 1 
ATOM   5955 N  NE1 . TRP C  1 208 ? 36.607  1.692   -39.276 1.00 8.69  ? 208 TRP C NE1 1 
ATOM   5956 C  CE2 . TRP C  1 208 ? 36.881  1.129   -38.071 1.00 7.96  ? 208 TRP C CE2 1 
ATOM   5957 C  CE3 . TRP C  1 208 ? 37.693  -1.057  -37.282 1.00 8.65  ? 208 TRP C CE3 1 
ATOM   5958 C  CZ2 . TRP C  1 208 ? 36.900  1.675   -36.746 1.00 7.84  ? 208 TRP C CZ2 1 
ATOM   5959 C  CZ3 . TRP C  1 208 ? 37.626  -0.534  -35.986 1.00 8.41  ? 208 TRP C CZ3 1 
ATOM   5960 C  CH2 . TRP C  1 208 ? 37.235  0.798   -35.723 1.00 8.32  ? 208 TRP C CH2 1 
ATOM   5961 N  N   . THR C  1 209 ? 40.123  -3.705  -39.985 1.00 9.28  ? 209 THR C N   1 
ATOM   5962 C  CA  . THR C  1 209 ? 40.346  -5.127  -39.933 1.00 9.10  ? 209 THR C CA  1 
ATOM   5963 C  C   . THR C  1 209 ? 39.702  -5.635  -38.685 1.00 9.95  ? 209 THR C C   1 
ATOM   5964 O  O   . THR C  1 209 ? 40.157  -5.288  -37.587 1.00 10.09 ? 209 THR C O   1 
ATOM   5965 C  CB  . THR C  1 209 ? 41.867  -5.439  -39.909 1.00 10.16 ? 209 THR C CB  1 
ATOM   5966 O  OG1 . THR C  1 209 ? 42.416  -4.961  -41.143 1.00 10.47 ? 209 THR C OG1 1 
ATOM   5967 C  CG2 . THR C  1 209 ? 42.086  -6.959  -39.851 1.00 10.08 ? 209 THR C CG2 1 
ATOM   5968 N  N   . VAL C  1 210 ? 38.635  -6.414  -38.862 1.00 9.71  ? 210 VAL C N   1 
ATOM   5969 C  CA  . VAL C  1 210 ? 37.923  -6.939  -37.672 1.00 10.25 ? 210 VAL C CA  1 
ATOM   5970 C  C   . VAL C  1 210 ? 38.202  -8.410  -37.662 1.00 9.98  ? 210 VAL C C   1 
ATOM   5971 O  O   . VAL C  1 210 ? 37.891  -9.154  -38.636 1.00 11.38 ? 210 VAL C O   1 
ATOM   5972 C  CB  . VAL C  1 210 ? 36.386  -6.692  -37.749 1.00 9.58  ? 210 VAL C CB  1 
ATOM   5973 C  CG1 . VAL C  1 210 ? 35.677  -7.272  -36.491 1.00 10.22 ? 210 VAL C CG1 1 
ATOM   5974 C  CG2 . VAL C  1 210 ? 36.091  -5.220  -37.961 1.00 10.66 ? 210 VAL C CG2 1 
ATOM   5975 N  N   . PHE C  1 211 ? 38.864  -8.892  -36.597 1.00 10.65 ? 211 PHE C N   1 
ATOM   5976 C  CA  . PHE C  1 211 ? 39.135  -10.319 -36.688 1.00 11.38 ? 211 PHE C CA  1 
ATOM   5977 C  C   . PHE C  1 211 ? 37.874  -11.201 -36.578 1.00 12.10 ? 211 PHE C C   1 
ATOM   5978 O  O   . PHE C  1 211 ? 36.973  -10.864 -35.841 1.00 11.68 ? 211 PHE C O   1 
ATOM   5979 C  CB  . PHE C  1 211 ? 40.165  -10.724 -35.625 1.00 11.28 ? 211 PHE C CB  1 
ATOM   5980 C  CG  . PHE C  1 211 ? 41.526  -10.112 -35.882 1.00 9.90  ? 211 PHE C CG  1 
ATOM   5981 C  CD1 . PHE C  1 211 ? 42.324  -10.572 -36.909 1.00 12.09 ? 211 PHE C CD1 1 
ATOM   5982 C  CD2 . PHE C  1 211 ? 41.994  -9.076  -35.076 1.00 11.76 ? 211 PHE C CD2 1 
ATOM   5983 C  CE1 . PHE C  1 211 ? 43.555  -9.900  -37.145 1.00 12.07 ? 211 PHE C CE1 1 
ATOM   5984 C  CE2 . PHE C  1 211 ? 43.230  -8.409  -35.322 1.00 11.18 ? 211 PHE C CE2 1 
ATOM   5985 C  CZ  . PHE C  1 211 ? 43.990  -8.842  -36.315 1.00 11.44 ? 211 PHE C CZ  1 
ATOM   5986 N  N   . ARG C  1 212 ? 37.867  -12.332 -37.242 1.00 12.44 ? 212 ARG C N   1 
ATOM   5987 C  CA  . ARG C  1 212 ? 36.680  -13.187 -37.354 1.00 13.59 ? 212 ARG C CA  1 
ATOM   5988 C  C   . ARG C  1 212 ? 36.395  -13.820 -35.944 1.00 12.82 ? 212 ARG C C   1 
ATOM   5989 O  O   . ARG C  1 212 ? 35.235  -13.911 -35.537 1.00 15.58 ? 212 ARG C O   1 
ATOM   5990 C  CB  . ARG C  1 212 ? 36.934  -14.358 -38.299 1.00 14.61 ? 212 ARG C CB  1 
ATOM   5991 C  CG  . ARG C  1 212 ? 35.655  -15.175 -38.607 1.00 18.67 ? 212 ARG C CG  1 
ATOM   5992 C  CD  . ARG C  1 212 ? 36.110  -16.559 -39.088 1.00 24.61 ? 212 ARG C CD  1 
ATOM   5993 N  NE  . ARG C  1 212 ? 35.028  -17.498 -39.348 1.00 27.11 ? 212 ARG C NE  1 
ATOM   5994 C  CZ  . ARG C  1 212 ? 34.718  -18.559 -38.578 1.00 37.05 ? 212 ARG C CZ  1 
ATOM   5995 N  NH1 . ARG C  1 212 ? 35.412  -18.870 -37.469 1.00 35.21 ? 212 ARG C NH1 1 
ATOM   5996 N  NH2 . ARG C  1 212 ? 33.698  -19.348 -38.936 1.00 39.02 ? 212 ARG C NH2 1 
ATOM   5997 N  N   . ASN C  1 213 ? 37.448  -14.237 -35.204 1.00 14.03 ? 213 ASN C N   1 
ATOM   5998 C  CA  . ASN C  1 213 ? 37.278  -14.957 -33.901 1.00 14.43 ? 213 ASN C CA  1 
ATOM   5999 C  C   . ASN C  1 213 ? 37.423  -14.035 -32.700 1.00 14.81 ? 213 ASN C C   1 
ATOM   6000 O  O   . ASN C  1 213 ? 38.279  -13.184 -32.701 1.00 14.45 ? 213 ASN C O   1 
ATOM   6001 C  CB  . ASN C  1 213 ? 38.310  -16.117 -33.812 1.00 16.91 ? 213 ASN C CB  1 
ATOM   6002 C  CG  . ASN C  1 213 ? 38.286  -16.988 -35.054 1.00 17.79 ? 213 ASN C CG  1 
ATOM   6003 O  OD1 . ASN C  1 213 ? 39.318  -17.180 -35.716 1.00 22.73 ? 213 ASN C OD1 1 
ATOM   6004 N  ND2 . ASN C  1 213 ? 37.144  -17.499 -35.415 1.00 19.57 ? 213 ASN C ND2 1 
ATOM   6005 N  N   . PRO C  1 214 ? 36.490  -14.104 -31.723 1.00 13.39 ? 214 PRO C N   1 
ATOM   6006 C  CA  . PRO C  1 214 ? 36.561  -13.280 -30.534 1.00 15.76 ? 214 PRO C CA  1 
ATOM   6007 C  C   . PRO C  1 214 ? 37.604  -13.778 -29.557 1.00 15.61 ? 214 PRO C C   1 
ATOM   6008 O  O   . PRO C  1 214 ? 38.090  -14.935 -29.718 1.00 20.03 ? 214 PRO C O   1 
ATOM   6009 C  CB  . PRO C  1 214 ? 35.198  -13.486 -29.852 1.00 15.60 ? 214 PRO C CB  1 
ATOM   6010 C  CG  . PRO C  1 214 ? 34.835  -14.894 -30.279 1.00 16.75 ? 214 PRO C CG  1 
ATOM   6011 C  CD  . PRO C  1 214 ? 35.351  -15.065 -31.682 1.00 17.87 ? 214 PRO C CD  1 
ATOM   6012 N  N   . VAL C  1 215 ? 38.014  -12.907 -28.642 1.00 14.80 ? 215 VAL C N   1 
ATOM   6013 C  CA  . VAL C  1 215 ? 38.702  -13.345 -27.392 1.00 15.89 ? 215 VAL C CA  1 
ATOM   6014 C  C   . VAL C  1 215 ? 37.709  -13.434 -26.231 1.00 17.20 ? 215 VAL C C   1 
ATOM   6015 O  O   . VAL C  1 215 ? 36.548  -12.976 -26.314 1.00 17.85 ? 215 VAL C O   1 
ATOM   6016 C  CB  . VAL C  1 215 ? 39.873  -12.447 -27.005 1.00 16.75 ? 215 VAL C CB  1 
ATOM   6017 C  CG1 . VAL C  1 215 ? 41.018  -12.505 -28.083 1.00 19.14 ? 215 VAL C CG1 1 
ATOM   6018 C  CG2 . VAL C  1 215 ? 39.444  -10.998 -26.616 1.00 16.86 ? 215 VAL C CG2 1 
ATOM   6019 N  N   . GLN C  1 216 ? 38.155  -14.082 -25.154 1.00 17.08 ? 216 GLN C N   1 
ATOM   6020 C  CA  . GLN C  1 216 ? 37.429  -14.235 -23.892 1.00 20.79 ? 216 GLN C CA  1 
ATOM   6021 C  C   . GLN C  1 216 ? 38.081  -13.500 -22.753 1.00 19.93 ? 216 GLN C C   1 
ATOM   6022 O  O   . GLN C  1 216 ? 39.329  -13.496 -22.668 1.00 21.34 ? 216 GLN C O   1 
ATOM   6023 C  CB  . GLN C  1 216 ? 37.330  -15.713 -23.545 1.00 20.74 ? 216 GLN C CB  1 
ATOM   6024 C  CG  . GLN C  1 216 ? 36.545  -16.420 -24.579 1.00 23.30 ? 216 GLN C CG  1 
ATOM   6025 C  CD  . GLN C  1 216 ? 35.929  -17.694 -24.123 1.00 30.77 ? 216 GLN C CD  1 
ATOM   6026 O  OE1 . GLN C  1 216 ? 36.274  -18.267 -23.058 1.00 29.78 ? 216 GLN C OE1 1 
ATOM   6027 N  NE2 . GLN C  1 216 ? 34.979  -18.162 -24.926 1.00 31.07 ? 216 GLN C NE2 1 
ATOM   6028 N  N   . ILE C  1 217 ? 37.266  -12.903 -21.890 1.00 19.89 ? 217 ILE C N   1 
ATOM   6029 C  CA  . ILE C  1 217 ? 37.615  -12.360 -20.606 1.00 18.35 ? 217 ILE C CA  1 
ATOM   6030 C  C   . ILE C  1 217 ? 36.577  -12.907 -19.582 1.00 19.46 ? 217 ILE C C   1 
ATOM   6031 O  O   . ILE C  1 217 ? 35.426  -13.273 -19.944 1.00 21.31 ? 217 ILE C O   1 
ATOM   6032 C  CB  . ILE C  1 217 ? 37.728  -10.784 -20.585 1.00 20.44 ? 217 ILE C CB  1 
ATOM   6033 C  CG1 . ILE C  1 217 ? 36.362  -10.100 -20.852 1.00 17.09 ? 217 ILE C CG1 1 
ATOM   6034 C  CG2 . ILE C  1 217 ? 38.764  -10.319 -21.632 1.00 18.95 ? 217 ILE C CG2 1 
ATOM   6035 C  CD1 . ILE C  1 217 ? 36.398  -8.587  -20.677 1.00 17.73 ? 217 ILE C CD1 1 
ATOM   6036 N  N   . SER C  1 218 ? 36.999  -13.017 -18.312 1.00 21.38 ? 218 SER C N   1 
ATOM   6037 C  CA  . SER C  1 218 ? 36.040  -13.559 -17.365 1.00 22.39 ? 218 SER C CA  1 
ATOM   6038 C  C   . SER C  1 218 ? 34.890  -12.565 -17.138 1.00 24.50 ? 218 SER C C   1 
ATOM   6039 O  O   . SER C  1 218 ? 34.984  -11.293 -17.336 1.00 21.88 ? 218 SER C O   1 
ATOM   6040 C  CB  . SER C  1 218 ? 36.749  -13.915 -16.022 1.00 20.66 ? 218 SER C CB  1 
ATOM   6041 O  OG  . SER C  1 218 ? 37.137  -12.740 -15.343 1.00 22.42 ? 218 SER C OG  1 
ATOM   6042 N  N   . GLN C  1 219 ? 33.810  -13.120 -16.584 1.00 26.46 ? 219 GLN C N   1 
ATOM   6043 C  CA  . GLN C  1 219 ? 32.753  -12.351 -15.980 1.00 25.77 ? 219 GLN C CA  1 
ATOM   6044 C  C   . GLN C  1 219 ? 33.235  -11.249 -15.058 1.00 23.10 ? 219 GLN C C   1 
ATOM   6045 O  O   . GLN C  1 219 ? 32.735  -10.090 -15.071 1.00 24.66 ? 219 GLN C O   1 
ATOM   6046 C  CB  . GLN C  1 219 ? 31.941  -13.390 -15.223 1.00 37.06 ? 219 GLN C CB  1 
ATOM   6047 C  CG  . GLN C  1 219 ? 30.690  -12.962 -14.495 1.00 49.75 ? 219 GLN C CG  1 
ATOM   6048 C  CD  . GLN C  1 219 ? 30.548  -13.762 -13.195 1.00 59.98 ? 219 GLN C CD  1 
ATOM   6049 O  OE1 . GLN C  1 219 ? 31.151  -13.413 -12.167 1.00 60.30 ? 219 GLN C OE1 1 
ATOM   6050 N  NE2 . GLN C  1 219 ? 29.776  -14.856 -13.241 1.00 62.36 ? 219 GLN C NE2 1 
ATOM   6051 N  N   . GLU C  1 220 ? 34.226  -11.557 -14.207 1.00 24.44 ? 220 GLU C N   1 
ATOM   6052 C  CA  . GLU C  1 220 ? 34.714  -10.572 -13.275 1.00 25.50 ? 220 GLU C CA  1 
ATOM   6053 C  C   . GLU C  1 220 ? 35.456  -9.438  -13.947 1.00 18.09 ? 220 GLU C C   1 
ATOM   6054 O  O   . GLU C  1 220 ? 35.336  -8.249  -13.537 1.00 23.69 ? 220 GLU C O   1 
ATOM   6055 C  CB  . GLU C  1 220 ? 35.612  -11.226 -12.219 1.00 26.63 ? 220 GLU C CB  1 
ATOM   6056 C  CG  . GLU C  1 220 ? 34.982  -12.526 -11.639 1.00 38.30 ? 220 GLU C CG  1 
ATOM   6057 C  CD  . GLU C  1 220 ? 35.282  -13.864 -12.401 1.00 42.58 ? 220 GLU C CD  1 
ATOM   6058 O  OE1 . GLU C  1 220 ? 34.490  -14.371 -13.251 1.00 40.39 ? 220 GLU C OE1 1 
ATOM   6059 O  OE2 . GLU C  1 220 ? 36.330  -14.491 -12.107 1.00 58.36 ? 220 GLU C OE2 1 
ATOM   6060 N  N   . GLN C  1 221 ? 36.292  -9.807  -14.910 1.00 22.30 ? 221 GLN C N   1 
ATOM   6061 C  CA  . GLN C  1 221 ? 37.028  -8.850  -15.758 1.00 21.08 ? 221 GLN C CA  1 
ATOM   6062 C  C   . GLN C  1 221 ? 36.121  -7.924  -16.575 1.00 16.01 ? 221 GLN C C   1 
ATOM   6063 O  O   . GLN C  1 221 ? 36.269  -6.670  -16.469 1.00 17.09 ? 221 GLN C O   1 
ATOM   6064 C  CB  . GLN C  1 221 ? 37.982  -9.579  -16.690 1.00 19.65 ? 221 GLN C CB  1 
ATOM   6065 C  CG  . GLN C  1 221 ? 39.222  -10.191 -16.008 1.00 18.03 ? 221 GLN C CG  1 
ATOM   6066 C  CD  . GLN C  1 221 ? 40.063  -10.816 -17.057 1.00 19.16 ? 221 GLN C CD  1 
ATOM   6067 O  OE1 . GLN C  1 221 ? 39.601  -11.742 -17.752 1.00 19.52 ? 221 GLN C OE1 1 
ATOM   6068 N  NE2 . GLN C  1 221 ? 41.253  -10.320 -17.220 1.00 20.55 ? 221 GLN C NE2 1 
ATOM   6069 N  N   . LEU C  1 222 ? 35.089  -8.507  -17.179 1.00 19.57 ? 222 LEU C N   1 
ATOM   6070 C  CA  . LEU C  1 222 ? 34.043  -7.660  -17.796 1.00 16.66 ? 222 LEU C CA  1 
ATOM   6071 C  C   . LEU C  1 222 ? 33.323  -6.714  -16.889 1.00 16.37 ? 222 LEU C C   1 
ATOM   6072 O  O   . LEU C  1 222 ? 33.182  -5.526  -17.173 1.00 16.18 ? 222 LEU C O   1 
ATOM   6073 C  CB  . LEU C  1 222 ? 33.035  -8.546  -18.483 1.00 16.60 ? 222 LEU C CB  1 
ATOM   6074 C  CG  . LEU C  1 222 ? 31.964  -7.824  -19.333 1.00 17.29 ? 222 LEU C CG  1 
ATOM   6075 C  CD1 . LEU C  1 222 ? 32.510  -6.861  -20.384 1.00 17.57 ? 222 LEU C CD1 1 
ATOM   6076 C  CD2 . LEU C  1 222 ? 31.086  -8.897  -19.970 1.00 18.82 ? 222 LEU C CD2 1 
ATOM   6077 N  N   . LEU C  1 223 ? 32.826  -7.213  -15.711 1.00 19.63 ? 223 LEU C N   1 
ATOM   6078 C  CA  . LEU C  1 223 ? 32.287  -6.328  -14.649 1.00 17.76 ? 223 LEU C CA  1 
ATOM   6079 C  C   . LEU C  1 223 ? 33.210  -5.202  -14.198 1.00 16.84 ? 223 LEU C C   1 
ATOM   6080 O  O   . LEU C  1 223 ? 32.789  -4.039  -14.068 1.00 17.75 ? 223 LEU C O   1 
ATOM   6081 C  CB  . LEU C  1 223 ? 31.783  -7.196  -13.448 1.00 21.17 ? 223 LEU C CB  1 
ATOM   6082 C  CG  . LEU C  1 223 ? 30.868  -6.401  -12.505 1.00 25.74 ? 223 LEU C CG  1 
ATOM   6083 C  CD1 . LEU C  1 223 ? 29.609  -5.750  -13.158 1.00 25.37 ? 223 LEU C CD1 1 
ATOM   6084 C  CD2 . LEU C  1 223 ? 30.471  -7.375  -11.378 1.00 23.54 ? 223 LEU C CD2 1 
ATOM   6085 N  N   . ALA C  1 224 ? 34.482  -5.528  -13.979 1.00 20.47 ? 224 ALA C N   1 
ATOM   6086 C  CA  . ALA C  1 224 ? 35.507  -4.494  -13.614 1.00 20.42 ? 224 ALA C CA  1 
ATOM   6087 C  C   . ALA C  1 224 ? 35.532  -3.427  -14.660 1.00 17.07 ? 224 ALA C C   1 
ATOM   6088 O  O   . ALA C  1 224 ? 35.463  -2.188  -14.392 1.00 22.39 ? 224 ALA C O   1 
ATOM   6089 C  CB  . ALA C  1 224 ? 36.930  -5.102  -13.430 1.00 21.77 ? 224 ALA C CB  1 
ATOM   6090 N  N   . LEU C  1 225 ? 35.615  -3.865  -15.930 1.00 19.34 ? 225 LEU C N   1 
ATOM   6091 C  CA  . LEU C  1 225 ? 35.724  -2.868  -17.028 1.00 19.18 ? 225 LEU C CA  1 
ATOM   6092 C  C   . LEU C  1 225 ? 34.509  -2.020  -17.082 1.00 16.03 ? 225 LEU C C   1 
ATOM   6093 O  O   . LEU C  1 225 ? 34.589  -0.792  -17.254 1.00 19.26 ? 225 LEU C O   1 
ATOM   6094 C  CB  . LEU C  1 225 ? 35.942  -3.624  -18.376 1.00 17.94 ? 225 LEU C CB  1 
ATOM   6095 C  CG  . LEU C  1 225 ? 35.971  -2.761  -19.628 1.00 18.24 ? 225 LEU C CG  1 
ATOM   6096 C  CD1 . LEU C  1 225 ? 37.134  -1.780  -19.533 1.00 19.33 ? 225 LEU C CD1 1 
ATOM   6097 C  CD2 . LEU C  1 225 ? 36.081  -3.600  -20.887 1.00 17.66 ? 225 LEU C CD2 1 
ATOM   6098 N  N   . GLU C  1 226 ? 33.322  -2.649  -16.908 1.00 17.30 ? 226 GLU C N   1 
ATOM   6099 C  CA  . GLU C  1 226 ? 32.075  -1.860  -16.971 1.00 16.96 ? 226 GLU C CA  1 
ATOM   6100 C  C   . GLU C  1 226 ? 31.782  -0.979  -15.756 1.00 19.34 ? 226 GLU C C   1 
ATOM   6101 O  O   . GLU C  1 226 ? 30.972  -0.097  -15.823 1.00 21.08 ? 226 GLU C O   1 
ATOM   6102 C  CB  . GLU C  1 226 ? 30.857  -2.773  -17.119 1.00 19.13 ? 226 GLU C CB  1 
ATOM   6103 C  CG  . GLU C  1 226 ? 30.859  -3.632  -18.399 1.00 19.41 ? 226 GLU C CG  1 
ATOM   6104 C  CD  . GLU C  1 226 ? 29.970  -4.846  -18.287 1.00 21.38 ? 226 GLU C CD  1 
ATOM   6105 O  OE1 . GLU C  1 226 ? 29.635  -5.328  -17.123 1.00 20.97 ? 226 GLU C OE1 1 
ATOM   6106 O  OE2 . GLU C  1 226 ? 29.525  -5.383  -19.327 1.00 20.43 ? 226 GLU C OE2 1 
ATOM   6107 N  N   . THR C  1 227 ? 32.525  -1.189  -14.696 1.00 21.32 ? 227 THR C N   1 
ATOM   6108 C  CA  . THR C  1 227 ? 32.159  -0.536  -13.420 1.00 22.58 ? 227 THR C CA  1 
ATOM   6109 C  C   . THR C  1 227 ? 33.304  0.293   -12.808 1.00 23.65 ? 227 THR C C   1 
ATOM   6110 O  O   . THR C  1 227 ? 33.094  0.933   -11.771 1.00 24.99 ? 227 THR C O   1 
ATOM   6111 C  CB  . THR C  1 227 ? 31.605  -1.549  -12.347 1.00 22.72 ? 227 THR C CB  1 
ATOM   6112 O  OG1 . THR C  1 227 ? 32.565  -2.576  -12.064 1.00 24.76 ? 227 THR C OG1 1 
ATOM   6113 C  CG2 . THR C  1 227 ? 30.216  -2.166  -12.801 1.00 23.17 ? 227 THR C CG2 1 
ATOM   6114 N  N   . ALA C  1 228 ? 34.468  0.286   -13.450 1.00 21.82 ? 228 ALA C N   1 
ATOM   6115 C  CA  . ALA C  1 228 ? 35.632  0.895   -12.825 1.00 19.32 ? 228 ALA C CA  1 
ATOM   6116 C  C   . ALA C  1 228 ? 35.714  2.386   -13.053 1.00 22.79 ? 228 ALA C C   1 
ATOM   6117 O  O   . ALA C  1 228 ? 36.280  3.080   -12.199 1.00 22.13 ? 228 ALA C O   1 
ATOM   6118 C  CB  . ALA C  1 228 ? 36.909  0.220   -13.266 1.00 22.27 ? 228 ALA C CB  1 
ATOM   6119 N  N   . LEU C  1 229 ? 35.183  2.919   -14.175 1.00 16.70 ? 229 LEU C N   1 
ATOM   6120 C  CA  . LEU C  1 229 ? 35.449  4.301   -14.555 1.00 16.60 ? 229 LEU C CA  1 
ATOM   6121 C  C   . LEU C  1 229 ? 34.259  5.205   -14.560 1.00 19.87 ? 229 LEU C C   1 
ATOM   6122 O  O   . LEU C  1 229 ? 33.114  4.836   -14.863 1.00 17.83 ? 229 LEU C O   1 
ATOM   6123 C  CB  . LEU C  1 229 ? 36.078  4.340   -15.977 1.00 15.58 ? 229 LEU C CB  1 
ATOM   6124 C  CG  . LEU C  1 229 ? 37.185  3.276   -16.200 1.00 14.89 ? 229 LEU C CG  1 
ATOM   6125 C  CD1 . LEU C  1 229 ? 37.734  3.355   -17.645 1.00 20.22 ? 229 LEU C CD1 1 
ATOM   6126 C  CD2 . LEU C  1 229 ? 38.414  3.486   -15.269 1.00 14.93 ? 229 LEU C CD2 1 
ATOM   6127 N  N   . TYR C  1 230 ? 34.532  6.454   -14.298 1.00 21.90 ? 230 TYR C N   1 
ATOM   6128 C  CA  . TYR C  1 230 ? 33.587  7.463   -14.514 1.00 22.19 ? 230 TYR C CA  1 
ATOM   6129 C  C   . TYR C  1 230 ? 33.980  8.227   -15.732 1.00 21.89 ? 230 TYR C C   1 
ATOM   6130 O  O   . TYR C  1 230 ? 35.121  8.279   -16.133 1.00 25.30 ? 230 TYR C O   1 
ATOM   6131 C  CB  . TYR C  1 230 ? 33.561  8.422   -13.305 1.00 24.03 ? 230 TYR C CB  1 
ATOM   6132 C  CG  . TYR C  1 230 ? 33.121  7.824   -11.987 1.00 26.70 ? 230 TYR C CG  1 
ATOM   6133 C  CD1 . TYR C  1 230 ? 31.763  7.630   -11.654 1.00 28.12 ? 230 TYR C CD1 1 
ATOM   6134 C  CD2 . TYR C  1 230 ? 34.083  7.566   -11.010 1.00 32.77 ? 230 TYR C CD2 1 
ATOM   6135 C  CE1 . TYR C  1 230 ? 31.402  7.170   -10.378 1.00 32.77 ? 230 TYR C CE1 1 
ATOM   6136 C  CE2 . TYR C  1 230 ? 33.745  7.122   -9.734  1.00 32.74 ? 230 TYR C CE2 1 
ATOM   6137 C  CZ  . TYR C  1 230 ? 32.426  6.924   -9.405  1.00 32.93 ? 230 TYR C CZ  1 
ATOM   6138 O  OH  . TYR C  1 230 ? 32.209  6.473   -8.081  1.00 37.16 ? 230 TYR C OH  1 
ATOM   6139 N  N   A CYS C  1 231 ? 33.021  8.894   -16.343 0.50 22.42 ? 231 CYS C N   1 
ATOM   6140 N  N   B CYS C  1 231 ? 32.987  8.890   -16.300 0.50 20.97 ? 231 CYS C N   1 
ATOM   6141 C  CA  A CYS C  1 231 ? 33.397  9.778   -17.411 0.50 24.99 ? 231 CYS C CA  1 
ATOM   6142 C  CA  B CYS C  1 231 ? 33.235  9.745   -17.424 0.50 22.74 ? 231 CYS C CA  1 
ATOM   6143 C  C   A CYS C  1 231 ? 33.897  11.104  -16.859 0.50 26.76 ? 231 CYS C C   1 
ATOM   6144 C  C   B CYS C  1 231 ? 33.295  11.244  -17.002 0.50 23.60 ? 231 CYS C C   1 
ATOM   6145 O  O   A CYS C  1 231 ? 34.727  11.742  -17.484 0.50 28.40 ? 231 CYS C O   1 
ATOM   6146 O  O   B CYS C  1 231 ? 33.345  12.126  -17.827 0.50 22.33 ? 231 CYS C O   1 
ATOM   6147 C  CB  A CYS C  1 231 ? 32.208  10.104  -18.288 0.50 24.15 ? 231 CYS C CB  1 
ATOM   6148 C  CB  B CYS C  1 231 ? 32.204  9.487   -18.518 0.50 22.15 ? 231 CYS C CB  1 
ATOM   6149 S  SG  A CYS C  1 231 ? 31.848  8.879   -19.541 0.50 24.36 ? 231 CYS C SG  1 
ATOM   6150 S  SG  B CYS C  1 231 ? 30.463  9.885   -18.114 0.50 20.03 ? 231 CYS C SG  1 
ATOM   6151 N  N   . THR C  1 232 ? 33.350  11.488  -15.701 1.00 23.87 ? 232 THR C N   1 
ATOM   6152 C  CA  . THR C  1 232 ? 33.405  12.845  -15.143 1.00 23.38 ? 232 THR C CA  1 
ATOM   6153 C  C   . THR C  1 232 ? 34.742  13.071  -14.402 1.00 25.17 ? 232 THR C C   1 
ATOM   6154 O  O   . THR C  1 232 ? 35.442  12.075  -13.985 1.00 21.31 ? 232 THR C O   1 
ATOM   6155 C  CB  . THR C  1 232 ? 32.220  13.033  -14.151 1.00 24.37 ? 232 THR C CB  1 
ATOM   6156 O  OG1 . THR C  1 232 ? 32.096  11.815  -13.335 1.00 23.25 ? 232 THR C OG1 1 
ATOM   6157 C  CG2 . THR C  1 232 ? 30.925  13.277  -14.952 1.00 28.96 ? 232 THR C CG2 1 
ATOM   6158 N  N   . HIS C  1 233 ? 35.050  14.373  -14.145 1.00 23.41 ? 233 HIS C N   1 
ATOM   6159 C  CA  . HIS C  1 233 ? 36.270  14.727  -13.324 1.00 25.92 ? 233 HIS C CA  1 
ATOM   6160 C  C   . HIS C  1 233 ? 36.055  14.385  -11.876 1.00 22.30 ? 233 HIS C C   1 
ATOM   6161 O  O   . HIS C  1 233 ? 34.878  14.338  -11.412 1.00 25.99 ? 233 HIS C O   1 
ATOM   6162 C  CB  . HIS C  1 233 ? 36.560  16.215  -13.415 1.00 26.09 ? 233 HIS C CB  1 
ATOM   6163 C  CG  . HIS C  1 233 ? 37.080  16.603  -14.768 1.00 31.11 ? 233 HIS C CG  1 
ATOM   6164 N  ND1 . HIS C  1 233 ? 36.284  17.170  -15.734 1.00 32.40 ? 233 HIS C ND1 1 
ATOM   6165 C  CD2 . HIS C  1 233 ? 38.332  16.420  -15.339 1.00 28.59 ? 233 HIS C CD2 1 
ATOM   6166 C  CE1 . HIS C  1 233 ? 37.019  17.367  -16.846 1.00 32.79 ? 233 HIS C CE1 1 
ATOM   6167 N  NE2 . HIS C  1 233 ? 38.266  16.889  -16.616 1.00 29.07 ? 233 HIS C NE2 1 
ATOM   6168 N  N   . MET C  1 234 ? 37.152  14.103  -11.193 1.00 28.81 ? 234 MET C N   1 
ATOM   6169 C  CA  . MET C  1 234 ? 37.168  13.818  -9.714  1.00 34.13 ? 234 MET C CA  1 
ATOM   6170 C  C   . MET C  1 234 ? 36.365  14.836  -8.852  1.00 38.59 ? 234 MET C C   1 
ATOM   6171 O  O   . MET C  1 234 ? 35.641  14.439  -7.940  1.00 41.18 ? 234 MET C O   1 
ATOM   6172 C  CB  . MET C  1 234 ? 38.601  13.734  -9.210  1.00 32.96 ? 234 MET C CB  1 
ATOM   6173 C  CG  . MET C  1 234 ? 38.734  13.027  -7.853  1.00 41.57 ? 234 MET C CG  1 
ATOM   6174 S  SD  . MET C  1 234 ? 40.460  12.919  -7.366  1.00 46.53 ? 234 MET C SD  1 
ATOM   6175 C  CE  . MET C  1 234 ? 40.638  11.259  -6.665  1.00 46.73 ? 234 MET C CE  1 
ATOM   6176 N  N   . ASP C  1 235 ? 36.490  16.127  -9.166  1.00 39.53 ? 235 ASP C N   1 
ATOM   6177 C  CA  . ASP C  1 235 ? 35.757  17.153  -8.447  1.00 48.02 ? 235 ASP C CA  1 
ATOM   6178 C  C   . ASP C  1 235 ? 34.230  17.025  -8.526  1.00 50.30 ? 235 ASP C C   1 
ATOM   6179 O  O   . ASP C  1 235 ? 33.570  17.320  -7.514  1.00 51.62 ? 235 ASP C O   1 
ATOM   6180 N  N   . ASP C  1 236 ? 33.706  16.615  -9.696  1.00 45.23 ? 236 ASP C N   1 
ATOM   6181 C  CA  . ASP C  1 236 ? 32.258  16.607  -10.018 1.00 44.15 ? 236 ASP C CA  1 
ATOM   6182 C  C   . ASP C  1 236 ? 31.333  16.043  -8.889  1.00 44.21 ? 236 ASP C C   1 
ATOM   6183 O  O   . ASP C  1 236 ? 31.385  14.847  -8.594  1.00 39.96 ? 236 ASP C O   1 
ATOM   6184 C  CB  . ASP C  1 236 ? 32.013  15.904  -11.402 1.00 38.80 ? 236 ASP C CB  1 
ATOM   6185 C  CG  . ASP C  1 236 ? 30.807  16.455  -12.130 1.00 42.24 ? 236 ASP C CG  1 
ATOM   6186 O  OD1 . ASP C  1 236 ? 29.806  16.770  -11.427 1.00 43.42 ? 236 ASP C OD1 1 
ATOM   6187 O  OD2 . ASP C  1 236 ? 30.820  16.588  -13.388 1.00 35.94 ? 236 ASP C OD2 1 
ATOM   6188 N  N   . PRO C  1 237 ? 30.494  16.909  -8.251  1.00 45.59 ? 237 PRO C N   1 
ATOM   6189 C  CA  . PRO C  1 237 ? 29.531  16.352  -7.266  1.00 44.95 ? 237 PRO C CA  1 
ATOM   6190 C  C   . PRO C  1 237 ? 28.385  15.554  -7.953  1.00 44.90 ? 237 PRO C C   1 
ATOM   6191 O  O   . PRO C  1 237 ? 27.511  14.990  -7.277  1.00 35.03 ? 237 PRO C O   1 
ATOM   6192 C  CB  . PRO C  1 237 ? 28.993  17.593  -6.538  1.00 43.95 ? 237 PRO C CB  1 
ATOM   6193 C  CG  . PRO C  1 237 ? 29.228  18.731  -7.478  1.00 43.88 ? 237 PRO C CG  1 
ATOM   6194 C  CD  . PRO C  1 237 ? 30.461  18.388  -8.278  1.00 43.98 ? 237 PRO C CD  1 
ATOM   6195 N  N   . SER C  1 238 ? 28.432  15.504  -9.289  1.00 42.18 ? 238 SER C N   1 
ATOM   6196 C  CA  . SER C  1 238 ? 27.435  14.825  -10.096 1.00 41.64 ? 238 SER C CA  1 
ATOM   6197 C  C   . SER C  1 238 ? 28.072  13.714  -10.957 1.00 33.66 ? 238 SER C C   1 
ATOM   6198 O  O   . SER C  1 238 ? 27.992  13.757  -12.192 1.00 31.46 ? 238 SER C O   1 
ATOM   6199 C  CB  . SER C  1 238 ? 26.730  15.862  -10.968 1.00 46.17 ? 238 SER C CB  1 
ATOM   6200 O  OG  . SER C  1 238 ? 25.405  15.448  -11.257 1.00 53.46 ? 238 SER C OG  1 
ATOM   6201 N  N   . PRO C  1 239 ? 28.697  12.698  -10.311 1.00 29.42 ? 239 PRO C N   1 
ATOM   6202 C  CA  . PRO C  1 239 ? 29.424  11.746  -11.127 1.00 26.99 ? 239 PRO C CA  1 
ATOM   6203 C  C   . PRO C  1 239 ? 28.598  10.864  -12.043 1.00 30.55 ? 239 PRO C C   1 
ATOM   6204 O  O   . PRO C  1 239 ? 27.410  10.545  -11.745 1.00 31.36 ? 239 PRO C O   1 
ATOM   6205 C  CB  . PRO C  1 239 ? 30.081  10.799  -10.113 1.00 27.90 ? 239 PRO C CB  1 
ATOM   6206 C  CG  . PRO C  1 239 ? 29.357  11.007  -8.821  1.00 26.58 ? 239 PRO C CG  1 
ATOM   6207 C  CD  . PRO C  1 239 ? 28.949  12.460  -8.869  1.00 28.31 ? 239 PRO C CD  1 
ATOM   6208 N  N   A ARG C  1 240 ? 29.250  10.409  -13.107 0.50 26.61 ? 240 ARG C N   1 
ATOM   6209 N  N   B ARG C  1 240 ? 29.241  10.405  -13.115 0.50 27.26 ? 240 ARG C N   1 
ATOM   6210 C  CA  A ARG C  1 240 ? 28.581  9.558   -14.088 0.50 26.43 ? 240 ARG C CA  1 
ATOM   6211 C  CA  B ARG C  1 240 ? 28.555  9.570   -14.112 0.50 27.22 ? 240 ARG C CA  1 
ATOM   6212 C  C   A ARG C  1 240 ? 29.484  8.414   -14.510 0.50 23.78 ? 240 ARG C C   1 
ATOM   6213 C  C   B ARG C  1 240 ? 29.461  8.432   -14.557 0.50 24.26 ? 240 ARG C C   1 
ATOM   6214 O  O   A ARG C  1 240 ? 30.672  8.591   -14.794 0.50 24.59 ? 240 ARG C O   1 
ATOM   6215 O  O   B ARG C  1 240 ? 30.635  8.637   -14.889 0.50 24.95 ? 240 ARG C O   1 
ATOM   6216 C  CB  A ARG C  1 240 ? 28.160  10.393  -15.292 0.50 25.29 ? 240 ARG C CB  1 
ATOM   6217 C  CB  B ARG C  1 240 ? 28.124  10.440  -15.297 0.50 26.85 ? 240 ARG C CB  1 
ATOM   6218 C  CG  A ARG C  1 240 ? 27.748  9.531   -16.466 0.50 27.51 ? 240 ARG C CG  1 
ATOM   6219 C  CG  B ARG C  1 240 ? 27.062  9.809   -16.186 0.50 30.34 ? 240 ARG C CG  1 
ATOM   6220 C  CD  A ARG C  1 240 ? 27.352  10.379  -17.655 0.50 28.79 ? 240 ARG C CD  1 
ATOM   6221 C  CD  B ARG C  1 240 ? 26.445  10.876  -17.090 0.50 33.08 ? 240 ARG C CD  1 
ATOM   6222 N  NE  A ARG C  1 240 ? 26.045  11.001  -17.468 0.50 31.90 ? 240 ARG C NE  1 
ATOM   6223 N  NE  B ARG C  1 240 ? 26.001  12.043  -16.321 0.50 33.24 ? 240 ARG C NE  1 
ATOM   6224 C  CZ  A ARG C  1 240 ? 24.891  10.370  -17.626 0.50 31.48 ? 240 ARG C CZ  1 
ATOM   6225 C  CZ  B ARG C  1 240 ? 26.530  13.263  -16.405 0.50 34.51 ? 240 ARG C CZ  1 
ATOM   6226 N  NH1 A ARG C  1 240 ? 24.880  9.076   -17.966 0.50 34.36 ? 240 ARG C NH1 1 
ATOM   6227 N  NH1 B ARG C  1 240 ? 27.541  13.502  -17.229 0.50 32.19 ? 240 ARG C NH1 1 
ATOM   6228 N  NH2 A ARG C  1 240 ? 23.754  11.035  -17.444 0.50 31.55 ? 240 ARG C NH2 1 
ATOM   6229 N  NH2 B ARG C  1 240 ? 26.043  14.242  -15.644 0.50 34.25 ? 240 ARG C NH2 1 
ATOM   6230 N  N   . GLU C  1 241 ? 28.900  7.223   -14.553 1.00 24.26 ? 241 GLU C N   1 
ATOM   6231 C  CA  . GLU C  1 241 ? 29.603  6.011   -14.871 1.00 20.62 ? 241 GLU C CA  1 
ATOM   6232 C  C   . GLU C  1 241 ? 30.025  6.039   -16.387 1.00 20.04 ? 241 GLU C C   1 
ATOM   6233 O  O   . GLU C  1 241 ? 29.254  6.557   -17.251 1.00 19.26 ? 241 GLU C O   1 
ATOM   6234 C  CB  . GLU C  1 241 ? 28.684  4.814   -14.704 1.00 25.99 ? 241 GLU C CB  1 
ATOM   6235 C  CG  . GLU C  1 241 ? 28.041  4.648   -13.338 1.00 31.78 ? 241 GLU C CG  1 
ATOM   6236 C  CD  . GLU C  1 241 ? 27.508  3.237   -13.156 1.00 40.54 ? 241 GLU C CD  1 
ATOM   6237 O  OE1 . GLU C  1 241 ? 26.619  2.806   -13.917 1.00 37.86 ? 241 GLU C OE1 1 
ATOM   6238 O  OE2 . GLU C  1 241 ? 27.990  2.530   -12.251 1.00 51.62 ? 241 GLU C OE2 1 
ATOM   6239 N  N   . MET C  1 242 ? 31.244  5.588   -16.647 1.00 17.55 ? 242 MET C N   1 
ATOM   6240 C  CA  . MET C  1 242 ? 31.696  5.363   -18.092 1.00 17.01 ? 242 MET C CA  1 
ATOM   6241 C  C   . MET C  1 242 ? 31.209  3.954   -18.540 1.00 16.11 ? 242 MET C C   1 
ATOM   6242 O  O   . MET C  1 242 ? 31.779  2.921   -18.264 1.00 14.89 ? 242 MET C O   1 
ATOM   6243 C  CB  . MET C  1 242 ? 33.227  5.493   -18.234 1.00 15.51 ? 242 MET C CB  1 
ATOM   6244 C  CG  . MET C  1 242 ? 33.573  5.496   -19.750 1.00 16.49 ? 242 MET C CG  1 
ATOM   6245 S  SD  . MET C  1 242 ? 35.349  5.410   -19.969 1.00 17.57 ? 242 MET C SD  1 
ATOM   6246 C  CE  . MET C  1 242 ? 35.800  7.070   -19.383 1.00 16.83 ? 242 MET C CE  1 
ATOM   6247 N  N   . ILE C  1 243 ? 30.059  3.967   -19.185 1.00 15.48 ? 243 ILE C N   1 
ATOM   6248 C  CA  . ILE C  1 243 ? 29.348  2.780   -19.639 1.00 14.29 ? 243 ILE C CA  1 
ATOM   6249 C  C   . ILE C  1 243 ? 28.756  3.119   -21.035 1.00 12.59 ? 243 ILE C C   1 
ATOM   6250 O  O   . ILE C  1 243 ? 28.529  4.262   -21.410 1.00 13.84 ? 243 ILE C O   1 
ATOM   6251 C  CB  . ILE C  1 243 ? 28.179  2.308   -18.681 1.00 14.89 ? 243 ILE C CB  1 
ATOM   6252 C  CG1 . ILE C  1 243 ? 27.247  3.441   -18.401 1.00 17.53 ? 243 ILE C CG1 1 
ATOM   6253 C  CG2 . ILE C  1 243 ? 28.794  1.651   -17.456 1.00 16.51 ? 243 ILE C CG2 1 
ATOM   6254 C  CD1 . ILE C  1 243 ? 26.072  3.028   -17.474 1.00 20.40 ? 243 ILE C CD1 1 
ATOM   6255 N  N   . ASN C  1 244 ? 28.493  2.040   -21.759 1.00 12.89 ? 244 ASN C N   1 
ATOM   6256 C  CA  . ASN C  1 244 ? 27.803  2.117   -23.111 1.00 13.41 ? 244 ASN C CA  1 
ATOM   6257 C  C   . ASN C  1 244 ? 28.536  3.080   -24.057 1.00 12.51 ? 244 ASN C C   1 
ATOM   6258 O  O   . ASN C  1 244 ? 27.950  3.913   -24.694 1.00 13.33 ? 244 ASN C O   1 
ATOM   6259 C  CB  . ASN C  1 244 ? 26.311  2.560   -22.979 1.00 15.20 ? 244 ASN C CB  1 
ATOM   6260 C  CG  . ASN C  1 244 ? 25.544  1.772   -21.951 1.00 16.61 ? 244 ASN C CG  1 
ATOM   6261 O  OD1 . ASN C  1 244 ? 25.677  0.574   -21.878 1.00 17.40 ? 244 ASN C OD1 1 
ATOM   6262 N  ND2 . ASN C  1 244 ? 24.810  2.559   -21.043 1.00 17.59 ? 244 ASN C ND2 1 
ATOM   6263 N  N   . ASN C  1 245 ? 29.862  2.980   -23.999 1.00 13.13 ? 245 ASN C N   1 
ATOM   6264 C  CA  . ASN C  1 245 ? 30.675  3.893   -24.811 1.00 12.07 ? 245 ASN C CA  1 
ATOM   6265 C  C   . ASN C  1 245 ? 31.003  3.319   -26.184 1.00 11.48 ? 245 ASN C C   1 
ATOM   6266 O  O   . ASN C  1 245 ? 32.167  3.232   -26.580 1.00 13.75 ? 245 ASN C O   1 
ATOM   6267 C  CB  . ASN C  1 245 ? 31.949  4.302   -24.042 1.00 13.51 ? 245 ASN C CB  1 
ATOM   6268 C  CG  . ASN C  1 245 ? 32.800  3.130   -23.701 1.00 13.38 ? 245 ASN C CG  1 
ATOM   6269 O  OD1 . ASN C  1 245 ? 32.436  1.957   -23.637 1.00 15.13 ? 245 ASN C OD1 1 
ATOM   6270 N  ND2 . ASN C  1 245 ? 34.076  3.475   -23.425 1.00 14.96 ? 245 ASN C ND2 1 
ATOM   6271 N  N   . PHE C  1 246 ? 29.922  2.944   -26.886 1.00 11.06 ? 246 PHE C N   1 
ATOM   6272 C  CA  . PHE C  1 246 ? 30.035  2.416   -28.244 1.00 10.31 ? 246 PHE C CA  1 
ATOM   6273 C  C   . PHE C  1 246 ? 29.065  3.172   -29.076 1.00 9.85  ? 246 PHE C C   1 
ATOM   6274 O  O   . PHE C  1 246 ? 28.014  3.637   -28.577 1.00 11.27 ? 246 PHE C O   1 
ATOM   6275 C  CB  . PHE C  1 246 ? 29.705  0.871   -28.297 1.00 10.92 ? 246 PHE C CB  1 
ATOM   6276 C  CG  . PHE C  1 246 ? 28.284  0.505   -27.821 1.00 11.16 ? 246 PHE C CG  1 
ATOM   6277 C  CD1 . PHE C  1 246 ? 27.994  0.365   -26.441 1.00 13.38 ? 246 PHE C CD1 1 
ATOM   6278 C  CD2 . PHE C  1 246 ? 27.256  0.404   -28.733 1.00 11.23 ? 246 PHE C CD2 1 
ATOM   6279 C  CE1 . PHE C  1 246 ? 26.669  0.126   -26.006 1.00 12.99 ? 246 PHE C CE1 1 
ATOM   6280 C  CE2 . PHE C  1 246 ? 25.958  0.175   -28.313 1.00 12.89 ? 246 PHE C CE2 1 
ATOM   6281 C  CZ  . PHE C  1 246 ? 25.653  -0.038  -26.965 1.00 12.83 ? 246 PHE C CZ  1 
ATOM   6282 N  N   . ARG C  1 247 ? 29.389  3.278   -30.367 1.00 8.62  ? 247 ARG C N   1 
ATOM   6283 C  CA  . ARG C  1 247 ? 28.473  3.912   -31.307 1.00 8.67  ? 247 ARG C CA  1 
ATOM   6284 C  C   . ARG C  1 247 ? 27.498  2.834   -31.872 1.00 9.22  ? 247 ARG C C   1 
ATOM   6285 O  O   . ARG C  1 247 ? 27.881  1.691   -32.120 1.00 8.82  ? 247 ARG C O   1 
ATOM   6286 C  CB  . ARG C  1 247 ? 29.297  4.536   -32.467 1.00 8.47  ? 247 ARG C CB  1 
ATOM   6287 C  CG  . ARG C  1 247 ? 28.516  5.553   -33.291 1.00 7.74  ? 247 ARG C CG  1 
ATOM   6288 C  CD  . ARG C  1 247 ? 29.330  6.004   -34.524 1.00 7.44  ? 247 ARG C CD  1 
ATOM   6289 N  NE  . ARG C  1 247 ? 28.785  7.193   -35.151 1.00 8.42  ? 247 ARG C NE  1 
ATOM   6290 C  CZ  . ARG C  1 247 ? 29.246  7.697   -36.289 1.00 7.87  ? 247 ARG C CZ  1 
ATOM   6291 N  NH1 . ARG C  1 247 ? 30.262  7.115   -36.914 1.00 8.95  ? 247 ARG C NH1 1 
ATOM   6292 N  NH2 . ARG C  1 247 ? 28.689  8.783   -36.798 1.00 9.04  ? 247 ARG C NH2 1 
ATOM   6293 N  N   . GLN C  1 248 ? 26.244  3.251   -32.105 1.00 8.24  ? 248 GLN C N   1 
ATOM   6294 C  CA  . GLN C  1 248 ? 25.296  2.397   -32.807 1.00 8.25  ? 248 GLN C CA  1 
ATOM   6295 C  C   . GLN C  1 248 ? 25.801  2.095   -34.224 1.00 7.76  ? 248 GLN C C   1 
ATOM   6296 O  O   . GLN C  1 248 ? 26.490  2.906   -34.853 1.00 8.61  ? 248 GLN C O   1 
ATOM   6297 C  CB  . GLN C  1 248 ? 23.912  3.139   -32.950 1.00 8.79  ? 248 GLN C CB  1 
ATOM   6298 C  CG  . GLN C  1 248 ? 23.268  3.503   -31.580 1.00 8.89  ? 248 GLN C CG  1 
ATOM   6299 C  CD  . GLN C  1 248 ? 22.924  2.264   -30.762 1.00 9.57  ? 248 GLN C CD  1 
ATOM   6300 O  OE1 . GLN C  1 248 ? 23.599  1.880   -29.801 1.00 12.07 ? 248 GLN C OE1 1 
ATOM   6301 N  NE2 . GLN C  1 248 ? 21.796  1.574   -31.158 1.00 11.12 ? 248 GLN C NE2 1 
ATOM   6302 N  N   . VAL C  1 249 ? 25.406  0.935   -34.772 1.00 8.18  ? 249 VAL C N   1 
ATOM   6303 C  CA  . VAL C  1 249 ? 25.766  0.593   -36.150 1.00 9.59  ? 249 VAL C CA  1 
ATOM   6304 C  C   . VAL C  1 249 ? 25.181  1.581   -37.162 1.00 10.25 ? 249 VAL C C   1 
ATOM   6305 O  O   . VAL C  1 249 ? 24.073  2.114   -36.924 1.00 9.72  ? 249 VAL C O   1 
ATOM   6306 C  CB  . VAL C  1 249 ? 25.433  -0.846  -36.575 1.00 12.13 ? 249 VAL C CB  1 
ATOM   6307 C  CG1 . VAL C  1 249 ? 26.245  -1.859  -35.737 1.00 11.03 ? 249 VAL C CG1 1 
ATOM   6308 C  CG2 . VAL C  1 249 ? 23.993  -1.060  -36.419 1.00 12.72 ? 249 VAL C CG2 1 
ATOM   6309 N  N   . GLN C  1 250 ? 25.895  1.793   -38.242 1.00 7.90  ? 250 GLN C N   1 
ATOM   6310 C  CA  . GLN C  1 250 ? 25.495  2.734   -39.264 1.00 8.89  ? 250 GLN C CA  1 
ATOM   6311 C  C   . GLN C  1 250 ? 24.946  1.980   -40.432 1.00 8.99  ? 250 GLN C C   1 
ATOM   6312 O  O   . GLN C  1 250 ? 25.346  0.827   -40.698 1.00 11.22 ? 250 GLN C O   1 
ATOM   6313 C  CB  . GLN C  1 250 ? 26.773  3.454   -39.757 1.00 7.77  ? 250 GLN C CB  1 
ATOM   6314 C  CG  . GLN C  1 250 ? 27.617  4.066   -38.572 1.00 8.32  ? 250 GLN C CG  1 
ATOM   6315 C  CD  . GLN C  1 250 ? 26.890  5.229   -37.933 1.00 7.73  ? 250 GLN C CD  1 
ATOM   6316 O  OE1 . GLN C  1 250 ? 26.613  6.245   -38.655 1.00 9.60  ? 250 GLN C OE1 1 
ATOM   6317 N  NE2 . GLN C  1 250 ? 26.609  5.153   -36.658 1.00 8.73  ? 250 GLN C NE2 1 
ATOM   6318 N  N   . LYS C  1 251 ? 24.110  2.690   -41.231 1.00 8.99  ? 251 LYS C N   1 
ATOM   6319 C  CA  . LYS C  1 251 ? 23.657  2.082   -42.523 1.00 9.46  ? 251 LYS C CA  1 
ATOM   6320 C  C   . LYS C  1 251 ? 24.882  1.805   -43.400 1.00 11.12 ? 251 LYS C C   1 
ATOM   6321 O  O   . LYS C  1 251 ? 25.846  2.610   -43.370 1.00 11.48 ? 251 LYS C O   1 
ATOM   6322 C  CB  . LYS C  1 251 ? 22.684  3.020   -43.230 1.00 10.87 ? 251 LYS C CB  1 
ATOM   6323 C  CG  . LYS C  1 251 ? 21.329  3.003   -42.462 1.00 10.66 ? 251 LYS C CG  1 
ATOM   6324 C  CD  . LYS C  1 251 ? 20.420  3.968   -43.108 1.00 11.21 ? 251 LYS C CD  1 
ATOM   6325 C  CE  . LYS C  1 251 ? 18.911  3.667   -42.731 1.00 10.39 ? 251 LYS C CE  1 
ATOM   6326 N  NZ  . LYS C  1 251 ? 18.721  3.772   -41.239 1.00 9.24  ? 251 LYS C NZ  1 
ATOM   6327 N  N   A PHE C  1 252 ? 24.765  0.865   -44.333 0.50 12.63 ? 252 PHE C N   1 
ATOM   6328 N  N   B PHE C  1 252 ? 24.838  0.670   -44.095 0.50 10.92 ? 252 PHE C N   1 
ATOM   6329 C  CA  A PHE C  1 252 ? 25.902  0.382   -45.139 0.50 14.30 ? 252 PHE C CA  1 
ATOM   6330 C  CA  B PHE C  1 252 ? 25.928  0.292   -45.005 0.50 10.74 ? 252 PHE C CA  1 
ATOM   6331 C  C   A PHE C  1 252 ? 25.587  0.214   -46.660 0.50 18.90 ? 252 PHE C C   1 
ATOM   6332 C  C   B PHE C  1 252 ? 25.213  -0.382  -46.199 0.50 11.94 ? 252 PHE C C   1 
ATOM   6333 O  O   A PHE C  1 252 ? 26.471  -0.117  -47.474 0.50 22.68 ? 252 PHE C O   1 
ATOM   6334 O  O   B PHE C  1 252 ? 24.831  -1.513  -46.146 0.50 14.68 ? 252 PHE C O   1 
ATOM   6335 C  CB  A PHE C  1 252 ? 26.409  -0.921  -44.530 0.50 14.40 ? 252 PHE C CB  1 
ATOM   6336 C  CB  B PHE C  1 252 ? 26.903  -0.594  -44.219 0.50 10.90 ? 252 PHE C CB  1 
ATOM   6337 C  CG  A PHE C  1 252 ? 27.716  -1.383  -45.074 0.50 12.37 ? 252 PHE C CG  1 
ATOM   6338 C  CG  B PHE C  1 252 ? 28.194  -0.952  -44.935 0.50 9.98  ? 252 PHE C CG  1 
ATOM   6339 C  CD1 A PHE C  1 252 ? 28.844  -0.568  -45.017 0.50 10.69 ? 252 PHE C CD1 1 
ATOM   6340 C  CD1 B PHE C  1 252 ? 29.307  -0.144  -44.849 0.50 9.48  ? 252 PHE C CD1 1 
ATOM   6341 C  CD2 A PHE C  1 252 ? 27.828  -2.652  -45.614 0.50 12.59 ? 252 PHE C CD2 1 
ATOM   6342 C  CD2 B PHE C  1 252 ? 28.314  -2.188  -45.569 0.50 11.81 ? 252 PHE C CD2 1 
ATOM   6343 C  CE1 A PHE C  1 252 ? 30.065  -0.992  -45.483 0.50 11.76 ? 252 PHE C CE1 1 
ATOM   6344 C  CE1 B PHE C  1 252 ? 30.517  -0.533  -45.429 0.50 9.97  ? 252 PHE C CE1 1 
ATOM   6345 C  CE2 A PHE C  1 252 ? 29.077  -3.096  -46.097 0.50 13.02 ? 252 PHE C CE2 1 
ATOM   6346 C  CE2 B PHE C  1 252 ? 29.518  -2.585  -46.129 0.50 12.01 ? 252 PHE C CE2 1 
ATOM   6347 C  CZ  A PHE C  1 252 ? 30.199  -2.257  -46.002 0.50 12.05 ? 252 PHE C CZ  1 
ATOM   6348 C  CZ  B PHE C  1 252 ? 30.618  -1.761  -46.041 0.50 9.69  ? 252 PHE C CZ  1 
ATOM   6349 N  N   A ASP C  1 253 ? 24.347  0.466   -47.044 0.50 23.24 ? 253 ASP C N   1 
ATOM   6350 N  N   B ASP C  1 253 ? 24.996  0.412   -47.236 0.50 15.59 ? 253 ASP C N   1 
ATOM   6351 C  CA  A ASP C  1 253 ? 23.925  0.551   -48.483 0.50 22.45 ? 253 ASP C CA  1 
ATOM   6352 C  CA  B ASP C  1 253 ? 24.088  0.011   -48.340 0.50 16.90 ? 253 ASP C CA  1 
ATOM   6353 C  C   A ASP C  1 253 ? 24.861  0.157   -49.695 0.50 20.29 ? 253 ASP C C   1 
ATOM   6354 C  C   B ASP C  1 253 ? 24.831  0.086   -49.656 0.50 17.00 ? 253 ASP C C   1 
ATOM   6355 O  O   A ASP C  1 253 ? 25.838  0.890   -49.977 0.50 22.00 ? 253 ASP C O   1 
ATOM   6356 O  O   B ASP C  1 253 ? 25.673  0.982   -49.925 0.50 19.83 ? 253 ASP C O   1 
ATOM   6357 C  CB  A ASP C  1 253 ? 23.373  1.971   -48.654 0.50 26.89 ? 253 ASP C CB  1 
ATOM   6358 C  CB  B ASP C  1 253 ? 22.821  0.880   -48.320 0.50 20.24 ? 253 ASP C CB  1 
ATOM   6359 C  CG  A ASP C  1 253 ? 22.437  2.370   -47.479 0.50 25.92 ? 253 ASP C CG  1 
ATOM   6360 C  CG  B ASP C  1 253 ? 21.725  0.323   -49.202 0.50 22.94 ? 253 ASP C CG  1 
ATOM   6361 O  OD1 A ASP C  1 253 ? 21.596  1.510   -47.117 0.50 31.29 ? 253 ASP C OD1 1 
ATOM   6362 O  OD1 B ASP C  1 253 ? 21.287  -0.836  -48.979 0.50 24.97 ? 253 ASP C OD1 1 
ATOM   6363 O  OD2 A ASP C  1 253 ? 22.559  3.484   -46.873 0.50 25.26 ? 253 ASP C OD2 1 
ATOM   6364 O  OD2 B ASP C  1 253 ? 21.324  1.054   -50.116 0.50 25.14 ? 253 ASP C OD2 1 
ATOM   6365 N  N   . GLU C  1 254 ? 24.551  -0.938  -50.414 1.00 20.13 ? 254 GLU C N   1 
ATOM   6366 C  CA  . GLU C  1 254 ? 25.190  -1.214  -51.691 1.00 22.58 ? 254 GLU C CA  1 
ATOM   6367 C  C   . GLU C  1 254 ? 26.729  -1.281  -51.576 1.00 22.15 ? 254 GLU C C   1 
ATOM   6368 O  O   . GLU C  1 254 ? 27.461  -0.760  -52.455 1.00 22.89 ? 254 GLU C O   1 
ATOM   6369 C  CB  . GLU C  1 254 ? 24.728  -0.196  -52.756 1.00 26.81 ? 254 GLU C CB  1 
ATOM   6370 C  CG  . GLU C  1 254 ? 23.217  -0.273  -53.057 1.00 28.50 ? 254 GLU C CG  1 
ATOM   6371 C  CD  . GLU C  1 254 ? 22.817  0.536   -54.264 1.00 39.03 ? 254 GLU C CD  1 
ATOM   6372 O  OE1 . GLU C  1 254 ? 23.704  0.866   -55.102 1.00 44.22 ? 254 GLU C OE1 1 
ATOM   6373 O  OE2 . GLU C  1 254 ? 21.597  0.832   -54.381 1.00 48.30 ? 254 GLU C OE2 1 
ATOM   6374 N  N   . ARG C  1 255 ? 27.192  -1.815  -50.441 1.00 18.14 ? 255 ARG C N   1 
ATOM   6375 C  CA  . ARG C  1 255 ? 28.638  -2.033  -50.219 1.00 18.23 ? 255 ARG C CA  1 
ATOM   6376 C  C   . ARG C  1 255 ? 28.896  -3.428  -49.687 1.00 16.91 ? 255 ARG C C   1 
ATOM   6377 O  O   . ARG C  1 255 ? 28.009  -4.155  -49.115 1.00 18.47 ? 255 ARG C O   1 
ATOM   6378 C  CB  . ARG C  1 255 ? 29.256  -1.004  -49.257 1.00 17.16 ? 255 ARG C CB  1 
ATOM   6379 C  CG  . ARG C  1 255 ? 29.034  0.472   -49.665 1.00 19.05 ? 255 ARG C CG  1 
ATOM   6380 C  CD  . ARG C  1 255 ? 29.685  1.448   -48.671 1.00 18.91 ? 255 ARG C CD  1 
ATOM   6381 N  NE  . ARG C  1 255 ? 31.064  1.056   -48.491 1.00 17.85 ? 255 ARG C NE  1 
ATOM   6382 C  CZ  . ARG C  1 255 ? 31.793  1.316   -47.421 1.00 19.06 ? 255 ARG C CZ  1 
ATOM   6383 N  NH1 . ARG C  1 255 ? 31.271  2.006   -46.420 1.00 16.07 ? 255 ARG C NH1 1 
ATOM   6384 N  NH2 . ARG C  1 255 ? 33.041  0.902   -47.359 1.00 14.86 ? 255 ARG C NH2 1 
ATOM   6385 N  N   . LEU C  1 256 ? 30.186  -3.830  -49.839 1.00 15.17 ? 256 LEU C N   1 
ATOM   6386 C  CA  . LEU C  1 256 ? 30.585  -5.157  -49.414 1.00 15.09 ? 256 LEU C CA  1 
ATOM   6387 C  C   . LEU C  1 256 ? 31.583  -5.066  -48.233 1.00 14.52 ? 256 LEU C C   1 
ATOM   6388 O  O   . LEU C  1 256 ? 32.271  -4.077  -48.067 1.00 15.69 ? 256 LEU C O   1 
ATOM   6389 C  CB  . LEU C  1 256 ? 31.199  -5.917  -50.585 1.00 17.27 ? 256 LEU C CB  1 
ATOM   6390 C  CG  . LEU C  1 256 ? 30.253  -6.332  -51.772 1.00 21.97 ? 256 LEU C CG  1 
ATOM   6391 C  CD1 . LEU C  1 256 ? 31.081  -6.898  -52.909 1.00 23.37 ? 256 LEU C CD1 1 
ATOM   6392 C  CD2 . LEU C  1 256 ? 29.248  -7.374  -51.354 1.00 23.52 ? 256 LEU C CD2 1 
ATOM   6393 N  N   . VAL C  1 257 ? 31.594  -6.121  -47.412 1.00 14.86 ? 257 VAL C N   1 
ATOM   6394 C  CA  . VAL C  1 257 ? 32.715  -6.336  -46.504 1.00 13.47 ? 257 VAL C CA  1 
ATOM   6395 C  C   . VAL C  1 257 ? 33.460  -7.503  -47.073 1.00 13.44 ? 257 VAL C C   1 
ATOM   6396 O  O   . VAL C  1 257 ? 32.869  -8.598  -47.375 1.00 13.85 ? 257 VAL C O   1 
ATOM   6397 C  CB  . VAL C  1 257 ? 32.190  -6.712  -45.154 1.00 13.90 ? 257 VAL C CB  1 
ATOM   6398 C  CG1 . VAL C  1 257 ? 33.280  -7.152  -44.194 1.00 14.33 ? 257 VAL C CG1 1 
ATOM   6399 C  CG2 . VAL C  1 257 ? 31.493  -5.500  -44.533 1.00 16.09 ? 257 VAL C CG2 1 
ATOM   6400 N  N   . TYR C  1 258 ? 34.772  -7.338  -47.212 1.00 12.55 ? 258 TYR C N   1 
ATOM   6401 C  CA  . TYR C  1 258 ? 35.631  -8.369  -47.856 1.00 12.56 ? 258 TYR C CA  1 
ATOM   6402 C  C   . TYR C  1 258 ? 36.158  -9.283  -46.759 1.00 12.69 ? 258 TYR C C   1 
ATOM   6403 O  O   . TYR C  1 258 ? 36.456  -8.849  -45.652 1.00 13.23 ? 258 TYR C O   1 
ATOM   6404 C  CB  . TYR C  1 258 ? 36.687  -7.708  -48.732 1.00 15.45 ? 258 TYR C CB  1 
ATOM   6405 C  CG  . TYR C  1 258 ? 36.090  -6.843  -49.731 1.00 16.84 ? 258 TYR C CG  1 
ATOM   6406 C  CD1 . TYR C  1 258 ? 35.594  -7.392  -50.906 1.00 17.56 ? 258 TYR C CD1 1 
ATOM   6407 C  CD2 . TYR C  1 258 ? 35.973  -5.458  -49.514 1.00 19.00 ? 258 TYR C CD2 1 
ATOM   6408 C  CE1 . TYR C  1 258 ? 34.993  -6.579  -51.882 1.00 18.47 ? 258 TYR C CE1 1 
ATOM   6409 C  CE2 . TYR C  1 258 ? 35.351  -4.623  -50.484 1.00 20.41 ? 258 TYR C CE2 1 
ATOM   6410 C  CZ  . TYR C  1 258 ? 34.857  -5.186  -51.666 1.00 24.02 ? 258 TYR C CZ  1 
ATOM   6411 O  OH  . TYR C  1 258 ? 34.218  -4.342  -52.629 1.00 24.35 ? 258 TYR C OH  1 
ATOM   6412 N  N   . THR C  1 259 ? 36.290  -10.587 -47.040 1.00 12.32 ? 259 THR C N   1 
ATOM   6413 C  CA  . THR C  1 259 ? 36.708  -11.477 -46.033 1.00 13.12 ? 259 THR C CA  1 
ATOM   6414 C  C   . THR C  1 259 ? 37.922  -12.280 -46.522 1.00 13.78 ? 259 THR C C   1 
ATOM   6415 O  O   . THR C  1 259 ? 38.036  -12.580 -47.726 1.00 14.57 ? 259 THR C O   1 
ATOM   6416 C  CB  . THR C  1 259 ? 35.596  -12.473 -45.664 1.00 14.04 ? 259 THR C CB  1 
ATOM   6417 O  OG1 . THR C  1 259 ? 35.170  -13.257 -46.828 1.00 15.93 ? 259 THR C OG1 1 
ATOM   6418 C  CG2 . THR C  1 259 ? 34.415  -11.711 -45.034 1.00 13.88 ? 259 THR C CG2 1 
ATOM   6419 N  N   . SER C  1 260 ? 38.829  -12.556 -45.550 1.00 13.76 ? 260 SER C N   1 
ATOM   6420 C  CA  . SER C  1 260 ? 40.065  -13.286 -45.933 1.00 15.67 ? 260 SER C CA  1 
ATOM   6421 C  C   . SER C  1 260 ? 39.715  -14.749 -45.978 1.00 18.46 ? 260 SER C C   1 
ATOM   6422 O  O   . SER C  1 260 ? 40.595  -15.576 -46.292 1.00 22.20 ? 260 SER C O   1 
ATOM   6423 C  CB  . SER C  1 260 ? 41.153  -13.014 -44.907 1.00 15.21 ? 260 SER C CB  1 
ATOM   6424 O  OG  . SER C  1 260 ? 40.757  -13.560 -43.688 1.00 15.40 ? 260 SER C OG  1 
ATOM   6425 N  N   . PHE C  1 261 ? 38.506  -15.111 -45.588 1.00 17.93 ? 261 PHE C N   1 
ATOM   6426 C  CA  . PHE C  1 261 ? 38.130  -16.495 -45.415 1.00 19.69 ? 261 PHE C CA  1 
ATOM   6427 C  C   . PHE C  1 261 ? 36.965  -16.746 -46.306 1.00 20.03 ? 261 PHE C C   1 
ATOM   6428 O  O   . PHE C  1 261 ? 36.124  -15.892 -46.624 1.00 22.70 ? 261 PHE C O   1 
ATOM   6429 C  CB  . PHE C  1 261 ? 37.791  -16.819 -43.945 1.00 18.61 ? 261 PHE C CB  1 
ATOM   6430 C  CG  . PHE C  1 261 ? 36.737  -15.914 -43.368 1.00 19.54 ? 261 PHE C CG  1 
ATOM   6431 C  CD1 . PHE C  1 261 ? 37.130  -14.740 -42.761 1.00 16.38 ? 261 PHE C CD1 1 
ATOM   6432 C  CD2 . PHE C  1 261 ? 35.395  -16.229 -43.402 1.00 19.07 ? 261 PHE C CD2 1 
ATOM   6433 C  CE1 . PHE C  1 261 ? 36.184  -13.888 -42.176 1.00 16.70 ? 261 PHE C CE1 1 
ATOM   6434 C  CE2 . PHE C  1 261 ? 34.437  -15.394 -42.852 1.00 18.88 ? 261 PHE C CE2 1 
ATOM   6435 C  CZ  . PHE C  1 261 ? 34.842  -14.182 -42.243 1.00 19.30 ? 261 PHE C CZ  1 
ATOM   6436 N  N   . SER C  1 262 ? 36.872  -17.953 -46.816 1.00 27.84 ? 262 SER C N   1 
ATOM   6437 C  CA  . SER C  1 262 ? 35.621  -18.215 -47.513 1.00 34.12 ? 262 SER C CA  1 
ATOM   6438 C  C   . SER C  1 262 ? 34.582  -18.961 -46.670 1.00 42.54 ? 262 SER C C   1 
ATOM   6439 O  O   . SER C  1 262 ? 33.386  -18.596 -46.546 1.00 42.55 ? 262 SER C O   1 
ATOM   6440 C  CB  . SER C  1 262 ? 35.911  -19.103 -48.682 1.00 29.40 ? 262 SER C CB  1 
ATOM   6441 O  OG  . SER C  1 262 ? 34.698  -19.796 -48.978 1.00 29.37 ? 262 SER C OG  1 
ATOM   6442 N  N   . GLN C  1 263 ? 35.047  -20.056 -46.126 1.00 41.58 ? 263 GLN C N   1 
ATOM   6443 C  CA  . GLN C  1 263 ? 34.151  -21.040 -45.567 1.00 43.97 ? 263 GLN C CA  1 
ATOM   6444 C  C   . GLN C  1 263 ? 33.928  -20.841 -44.052 1.00 48.42 ? 263 GLN C C   1 
ATOM   6445 O  O   . GLN C  1 263 ? 34.482  -19.899 -43.447 1.00 46.28 ? 263 GLN C O   1 
ATOM   6446 C  CB  . GLN C  1 263 ? 34.733  -22.413 -45.895 1.00 38.52 ? 263 GLN C CB  1 
ATOM   6447 C  CG  . GLN C  1 263 ? 36.191  -22.551 -45.457 1.00 33.52 ? 263 GLN C CG  1 
ATOM   6448 C  CD  . GLN C  1 263 ? 36.793  -23.904 -45.765 1.00 29.58 ? 263 GLN C CD  1 
ATOM   6449 O  OE1 . GLN C  1 263 ? 37.905  -24.224 -45.309 1.00 28.80 ? 263 GLN C OE1 1 
ATOM   6450 N  NE2 . GLN C  1 263 ? 36.089  -24.698 -46.565 1.00 21.86 ? 263 GLN C NE2 1 
ATOM   6451 N  N   . LYS D  1 3   ? 14.149  19.617  -45.146 1.00 36.91 ? 3   LYS D N   1 
ATOM   6452 C  CA  . LYS D  1 3   ? 14.440  18.729  -46.285 1.00 27.06 ? 3   LYS D CA  1 
ATOM   6453 C  C   . LYS D  1 3   ? 15.161  17.464  -45.756 1.00 23.48 ? 3   LYS D C   1 
ATOM   6454 O  O   . LYS D  1 3   ? 16.064  16.919  -46.412 1.00 20.66 ? 3   LYS D O   1 
ATOM   6455 C  CB  . LYS D  1 3   ? 15.371  19.413  -47.272 1.00 29.00 ? 3   LYS D CB  1 
ATOM   6456 C  CG  . LYS D  1 3   ? 16.344  20.356  -46.585 1.00 35.21 ? 3   LYS D CG  1 
ATOM   6457 C  CD  . LYS D  1 3   ? 17.033  21.274  -47.582 1.00 37.06 ? 3   LYS D CD  1 
ATOM   6458 C  CE  . LYS D  1 3   ? 18.082  20.470  -48.296 1.00 31.48 ? 3   LYS D CE  1 
ATOM   6459 N  NZ  . LYS D  1 3   ? 19.276  20.458  -47.402 1.00 27.34 ? 3   LYS D NZ  1 
ATOM   6460 N  N   . TRP D  1 4   ? 14.747  16.992  -44.553 1.00 15.02 ? 4   TRP D N   1 
ATOM   6461 C  CA  . TRP D  1 4   ? 15.428  15.854  -43.947 1.00 13.09 ? 4   TRP D CA  1 
ATOM   6462 C  C   . TRP D  1 4   ? 15.175  14.647  -44.834 1.00 12.12 ? 4   TRP D C   1 
ATOM   6463 O  O   . TRP D  1 4   ? 14.163  14.551  -45.547 1.00 13.28 ? 4   TRP D O   1 
ATOM   6464 C  CB  . TRP D  1 4   ? 14.987  15.617  -42.504 1.00 13.02 ? 4   TRP D CB  1 
ATOM   6465 C  CG  . TRP D  1 4   ? 13.546  15.353  -42.323 1.00 11.43 ? 4   TRP D CG  1 
ATOM   6466 C  CD1 . TRP D  1 4   ? 12.506  16.268  -42.108 1.00 11.70 ? 4   TRP D CD1 1 
ATOM   6467 C  CD2 . TRP D  1 4   ? 12.912  14.001  -42.273 1.00 11.17 ? 4   TRP D CD2 1 
ATOM   6468 N  NE1 . TRP D  1 4   ? 11.312  15.587  -41.939 1.00 12.51 ? 4   TRP D NE1 1 
ATOM   6469 C  CE2 . TRP D  1 4   ? 11.508  14.232  -42.058 1.00 11.10 ? 4   TRP D CE2 1 
ATOM   6470 C  CE3 . TRP D  1 4   ? 13.374  12.690  -42.428 1.00 11.09 ? 4   TRP D CE3 1 
ATOM   6471 C  CZ2 . TRP D  1 4   ? 10.627  13.171  -41.880 1.00 10.66 ? 4   TRP D CZ2 1 
ATOM   6472 C  CZ3 . TRP D  1 4   ? 12.462  11.601  -42.275 1.00 10.36 ? 4   TRP D CZ3 1 
ATOM   6473 C  CH2 . TRP D  1 4   ? 11.142  11.838  -42.004 1.00 11.24 ? 4   TRP D CH2 1 
ATOM   6474 N  N   . THR D  1 5   ? 16.156  13.728  -44.780 1.00 10.59 ? 5   THR D N   1 
ATOM   6475 C  CA  . THR D  1 5   ? 16.109  12.524  -45.601 1.00 11.35 ? 5   THR D CA  1 
ATOM   6476 C  C   . THR D  1 5   ? 16.638  11.350  -44.743 1.00 10.83 ? 5   THR D C   1 
ATOM   6477 O  O   . THR D  1 5   ? 16.982  11.476  -43.561 1.00 10.80 ? 5   THR D O   1 
ATOM   6478 C  CB  . THR D  1 5   ? 17.007  12.589  -46.895 1.00 12.50 ? 5   THR D CB  1 
ATOM   6479 O  OG1 . THR D  1 5   ? 18.362  12.584  -46.402 1.00 12.07 ? 5   THR D OG1 1 
ATOM   6480 C  CG2 . THR D  1 5   ? 16.666  13.844  -47.742 1.00 13.72 ? 5   THR D CG2 1 
ATOM   6481 N  N   . TYR D  1 6   ? 16.734  10.173  -45.384 1.00 9.97  ? 6   TYR D N   1 
ATOM   6482 C  CA  . TYR D  1 6   ? 17.397  9.023   -44.821 1.00 9.82  ? 6   TYR D CA  1 
ATOM   6483 C  C   . TYR D  1 6   ? 18.736  8.654   -45.389 1.00 10.11 ? 6   TYR D C   1 
ATOM   6484 O  O   . TYR D  1 6   ? 19.339  7.574   -45.109 1.00 11.75 ? 6   TYR D O   1 
ATOM   6485 C  CB  . TYR D  1 6   ? 16.483  7.778   -44.978 1.00 8.96  ? 6   TYR D CB  1 
ATOM   6486 C  CG  . TYR D  1 6   ? 15.214  7.890   -44.072 1.00 8.70  ? 6   TYR D CG  1 
ATOM   6487 C  CD1 . TYR D  1 6   ? 15.224  7.353   -42.766 1.00 8.47  ? 6   TYR D CD1 1 
ATOM   6488 C  CD2 . TYR D  1 6   ? 14.008  8.471   -44.533 1.00 8.15  ? 6   TYR D CD2 1 
ATOM   6489 C  CE1 . TYR D  1 6   ? 14.071  7.351   -41.974 1.00 7.92  ? 6   TYR D CE1 1 
ATOM   6490 C  CE2 . TYR D  1 6   ? 12.878  8.496   -43.754 1.00 8.36  ? 6   TYR D CE2 1 
ATOM   6491 C  CZ  . TYR D  1 6   ? 12.911  7.965   -42.463 1.00 6.53  ? 6   TYR D CZ  1 
ATOM   6492 O  OH  . TYR D  1 6   ? 11.776  7.995   -41.720 1.00 7.89  ? 6   TYR D OH  1 
ATOM   6493 N  N   . PHE D  1 7   ? 19.201  9.487   -46.333 1.00 12.28 ? 7   PHE D N   1 
ATOM   6494 C  CA  . PHE D  1 7   ? 20.428  9.166   -47.061 1.00 14.29 ? 7   PHE D CA  1 
ATOM   6495 C  C   . PHE D  1 7   ? 21.186  10.452  -47.395 1.00 14.58 ? 7   PHE D C   1 
ATOM   6496 O  O   . PHE D  1 7   ? 20.588  11.308  -48.056 1.00 16.34 ? 7   PHE D O   1 
ATOM   6497 C  CB  . PHE D  1 7   ? 20.083  8.514   -48.394 1.00 16.79 ? 7   PHE D CB  1 
ATOM   6498 C  CG  . PHE D  1 7   ? 21.307  8.059   -49.129 1.00 24.08 ? 7   PHE D CG  1 
ATOM   6499 C  CD1 . PHE D  1 7   ? 22.163  7.081   -48.598 1.00 24.12 ? 7   PHE D CD1 1 
ATOM   6500 C  CD2 . PHE D  1 7   ? 21.645  8.688   -50.345 1.00 27.85 ? 7   PHE D CD2 1 
ATOM   6501 C  CE1 . PHE D  1 7   ? 23.319  6.676   -49.290 1.00 30.73 ? 7   PHE D CE1 1 
ATOM   6502 C  CE2 . PHE D  1 7   ? 22.795  8.305   -51.022 1.00 33.77 ? 7   PHE D CE2 1 
ATOM   6503 C  CZ  . PHE D  1 7   ? 23.619  7.298   -50.511 1.00 29.26 ? 7   PHE D CZ  1 
ATOM   6504 N  N   . GLY D  1 8   ? 22.466  10.531  -47.016 1.00 16.45 ? 8   GLY D N   1 
ATOM   6505 C  CA  . GLY D  1 8   ? 23.320  11.660  -47.550 1.00 19.10 ? 8   GLY D CA  1 
ATOM   6506 C  C   . GLY D  1 8   ? 23.369  12.744  -46.516 1.00 18.85 ? 8   GLY D C   1 
ATOM   6507 O  O   . GLY D  1 8   ? 23.077  12.531  -45.336 1.00 17.21 ? 8   GLY D O   1 
ATOM   6508 N  N   . PRO D  1 9   ? 23.667  13.961  -46.919 1.00 18.23 ? 9   PRO D N   1 
ATOM   6509 C  CA  . PRO D  1 9   ? 24.019  14.936  -45.926 1.00 19.10 ? 9   PRO D CA  1 
ATOM   6510 C  C   . PRO D  1 9   ? 22.910  15.375  -45.006 1.00 19.31 ? 9   PRO D C   1 
ATOM   6511 O  O   . PRO D  1 9   ? 23.230  15.869  -43.936 1.00 20.09 ? 9   PRO D O   1 
ATOM   6512 C  CB  . PRO D  1 9   ? 24.540  16.145  -46.760 1.00 21.91 ? 9   PRO D CB  1 
ATOM   6513 C  CG  . PRO D  1 9   ? 24.752  15.640  -48.132 1.00 22.89 ? 9   PRO D CG  1 
ATOM   6514 C  CD  . PRO D  1 9   ? 23.996  14.333  -48.315 1.00 19.96 ? 9   PRO D CD  1 
ATOM   6515 N  N   . ASP D  1 10  ? 21.631  15.169  -45.383 1.00 15.42 ? 10  ASP D N   1 
ATOM   6516 C  CA  . ASP D  1 10  ? 20.460  15.489  -44.565 1.00 14.50 ? 10  ASP D CA  1 
ATOM   6517 C  C   . ASP D  1 10  ? 19.847  14.226  -43.888 1.00 11.71 ? 10  ASP D C   1 
ATOM   6518 O  O   . ASP D  1 10  ? 18.745  14.339  -43.350 1.00 12.85 ? 10  ASP D O   1 
ATOM   6519 C  CB  . ASP D  1 10  ? 19.383  16.236  -45.348 1.00 17.32 ? 10  ASP D CB  1 
ATOM   6520 C  CG  . ASP D  1 10  ? 19.957  17.522  -45.986 1.00 23.11 ? 10  ASP D CG  1 
ATOM   6521 O  OD1 . ASP D  1 10  ? 20.627  18.238  -45.250 1.00 25.83 ? 10  ASP D OD1 1 
ATOM   6522 O  OD2 . ASP D  1 10  ? 19.822  17.638  -47.202 1.00 25.91 ? 10  ASP D OD2 1 
ATOM   6523 N  N   . GLY D  1 11  ? 20.651  13.160  -43.900 1.00 10.78 ? 11  GLY D N   1 
ATOM   6524 C  CA  . GLY D  1 11  ? 20.275  11.877  -43.305 1.00 9.18  ? 11  GLY D CA  1 
ATOM   6525 C  C   . GLY D  1 11  ? 20.327  11.871  -41.780 1.00 9.38  ? 11  GLY D C   1 
ATOM   6526 O  O   . GLY D  1 11  ? 20.520  12.927  -41.100 1.00 8.67  ? 11  GLY D O   1 
ATOM   6527 N  N   . GLU D  1 12  ? 20.082  10.710  -41.169 1.00 8.10  ? 12  GLU D N   1 
ATOM   6528 C  CA  . GLU D  1 12  ? 19.710  10.684  -39.783 1.00 7.86  ? 12  GLU D CA  1 
ATOM   6529 C  C   . GLU D  1 12  ? 20.721  11.144  -38.795 1.00 7.58  ? 12  GLU D C   1 
ATOM   6530 O  O   . GLU D  1 12  ? 20.331  11.609  -37.739 1.00 7.49  ? 12  GLU D O   1 
ATOM   6531 C  CB  . GLU D  1 12  ? 19.225  9.257   -39.386 1.00 7.60  ? 12  GLU D CB  1 
ATOM   6532 C  CG  . GLU D  1 12  ? 20.325  8.217   -39.283 1.00 8.25  ? 12  GLU D CG  1 
ATOM   6533 C  CD  . GLU D  1 12  ? 19.724  6.806   -39.300 1.00 8.32  ? 12  GLU D CD  1 
ATOM   6534 O  OE1 . GLU D  1 12  ? 19.346  6.334   -38.183 1.00 8.82  ? 12  GLU D OE1 1 
ATOM   6535 O  OE2 . GLU D  1 12  ? 19.663  6.254   -40.422 1.00 9.31  ? 12  GLU D OE2 1 
ATOM   6536 N  N   . ASN D  1 13  ? 22.025  11.025  -39.108 1.00 7.90  ? 13  ASN D N   1 
ATOM   6537 C  CA  . ASN D  1 13  ? 23.026  11.528  -38.187 1.00 8.07  ? 13  ASN D CA  1 
ATOM   6538 C  C   . ASN D  1 13  ? 23.104  13.081  -38.162 1.00 8.19  ? 13  ASN D C   1 
ATOM   6539 O  O   . ASN D  1 13  ? 23.713  13.607  -37.239 1.00 9.49  ? 13  ASN D O   1 
ATOM   6540 C  CB  . ASN D  1 13  ? 24.404  10.983  -38.561 1.00 8.67  ? 13  ASN D CB  1 
ATOM   6541 C  CG  . ASN D  1 13  ? 24.580  9.517   -38.228 1.00 8.35  ? 13  ASN D CG  1 
ATOM   6542 O  OD1 . ASN D  1 13  ? 23.658  8.854   -37.728 1.00 9.10  ? 13  ASN D OD1 1 
ATOM   6543 N  ND2 . ASN D  1 13  ? 25.762  8.993   -38.576 1.00 9.90  ? 13  ASN D ND2 1 
ATOM   6544 N  N   . SER D  1 14  ? 22.404  13.717  -39.090 1.00 8.38  ? 14  SER D N   1 
ATOM   6545 C  CA  . SER D  1 14  ? 22.360  15.207  -39.194 1.00 8.76  ? 14  SER D CA  1 
ATOM   6546 C  C   . SER D  1 14  ? 21.030  15.718  -38.743 1.00 9.17  ? 14  SER D C   1 
ATOM   6547 O  O   . SER D  1 14  ? 20.875  16.919  -38.656 1.00 10.52 ? 14  SER D O   1 
ATOM   6548 C  CB  . SER D  1 14  ? 22.626  15.676  -40.627 1.00 8.96  ? 14  SER D CB  1 
ATOM   6549 O  OG  . SER D  1 14  ? 23.976  15.343  -40.911 1.00 10.38 ? 14  SER D OG  1 
ATOM   6550 N  N   . TRP D  1 15  ? 20.007  14.891  -38.440 1.00 7.89  ? 15  TRP D N   1 
ATOM   6551 C  CA  . TRP D  1 15  ? 18.724  15.496  -38.061 1.00 8.13  ? 15  TRP D CA  1 
ATOM   6552 C  C   . TRP D  1 15  ? 18.795  16.401  -36.870 1.00 8.45  ? 15  TRP D C   1 
ATOM   6553 O  O   . TRP D  1 15  ? 18.015  17.390  -36.846 1.00 8.24  ? 15  TRP D O   1 
ATOM   6554 C  CB  . TRP D  1 15  ? 17.729  14.353  -37.682 1.00 8.90  ? 15  TRP D CB  1 
ATOM   6555 C  CG  . TRP D  1 15  ? 17.304  13.463  -38.853 1.00 8.94  ? 15  TRP D CG  1 
ATOM   6556 C  CD1 . TRP D  1 15  ? 17.533  13.621  -40.192 1.00 7.84  ? 15  TRP D CD1 1 
ATOM   6557 C  CD2 . TRP D  1 15  ? 16.533  12.247  -38.715 1.00 8.28  ? 15  TRP D CD2 1 
ATOM   6558 N  NE1 . TRP D  1 15  ? 16.972  12.582  -40.951 1.00 8.44  ? 15  TRP D NE1 1 
ATOM   6559 C  CE2 . TRP D  1 15  ? 16.355  11.755  -40.071 1.00 7.39  ? 15  TRP D CE2 1 
ATOM   6560 C  CE3 . TRP D  1 15  ? 15.971  11.537  -37.620 1.00 7.76  ? 15  TRP D CE3 1 
ATOM   6561 C  CZ2 . TRP D  1 15  ? 15.641  10.552  -40.361 1.00 7.53  ? 15  TRP D CZ2 1 
ATOM   6562 C  CZ3 . TRP D  1 15  ? 15.239  10.372  -37.890 1.00 7.29  ? 15  TRP D CZ3 1 
ATOM   6563 C  CH2 . TRP D  1 15  ? 15.075  9.914   -39.249 1.00 7.12  ? 15  TRP D CH2 1 
ATOM   6564 N  N   . SER D  1 16  ? 19.651  16.059  -35.919 1.00 8.71  ? 16  SER D N   1 
ATOM   6565 C  CA  . SER D  1 16  ? 19.714  16.908  -34.672 1.00 8.91  ? 16  SER D CA  1 
ATOM   6566 C  C   . SER D  1 16  ? 20.229  18.331  -34.977 1.00 9.64  ? 16  SER D C   1 
ATOM   6567 O  O   . SER D  1 16  ? 20.004  19.170  -34.096 1.00 11.08 ? 16  SER D O   1 
ATOM   6568 C  CB  . SER D  1 16  ? 20.644  16.255  -33.734 1.00 9.69  ? 16  SER D CB  1 
ATOM   6569 O  OG  . SER D  1 16  ? 21.973  16.346  -34.256 1.00 14.13 ? 16  SER D OG  1 
ATOM   6570 N  N   . LYS D  1 17  ? 20.803  18.573  -36.150 1.00 9.78  ? 17  LYS D N   1 
ATOM   6571 C  CA  . LYS D  1 17  ? 21.267  19.946  -36.434 1.00 9.84  ? 17  LYS D CA  1 
ATOM   6572 C  C   . LYS D  1 17  ? 20.077  20.840  -36.583 1.00 10.33 ? 17  LYS D C   1 
ATOM   6573 O  O   . LYS D  1 17  ? 20.198  22.067  -36.292 1.00 9.42  ? 17  LYS D O   1 
ATOM   6574 C  CB  . LYS D  1 17  ? 21.995  19.940  -37.759 1.00 9.15  ? 17  LYS D CB  1 
ATOM   6575 C  CG  . LYS D  1 17  ? 23.285  19.078  -37.767 1.00 10.85 ? 17  LYS D CG  1 
ATOM   6576 C  CD  . LYS D  1 17  ? 23.891  19.101  -39.190 1.00 10.32 ? 17  LYS D CD  1 
ATOM   6577 C  CE  . LYS D  1 17  ? 25.039  18.155  -39.327 1.00 10.73 ? 17  LYS D CE  1 
ATOM   6578 N  NZ  . LYS D  1 17  ? 25.673  18.326  -40.707 1.00 12.07 ? 17  LYS D NZ  1 
ATOM   6579 N  N   . LYS D  1 18  ? 18.931  20.373  -37.036 1.00 9.74  ? 18  LYS D N   1 
ATOM   6580 C  CA  . LYS D  1 18  ? 17.678  21.194  -37.185 1.00 9.15  ? 18  LYS D CA  1 
ATOM   6581 C  C   . LYS D  1 18  ? 16.582  20.820  -36.196 1.00 9.96  ? 18  LYS D C   1 
ATOM   6582 O  O   . LYS D  1 18  ? 15.668  21.613  -36.049 1.00 12.01 ? 18  LYS D O   1 
ATOM   6583 C  CB  . LYS D  1 18  ? 17.103  21.046  -38.578 1.00 12.02 ? 18  LYS D CB  1 
ATOM   6584 C  CG  . LYS D  1 18  ? 17.986  21.704  -39.708 1.00 15.35 ? 18  LYS D CG  1 
ATOM   6585 C  CD  . LYS D  1 18  ? 17.389  21.454  -41.109 1.00 17.19 ? 18  LYS D CD  1 
ATOM   6586 C  CE  . LYS D  1 18  ? 18.160  22.213  -42.207 1.00 20.82 ? 18  LYS D CE  1 
ATOM   6587 N  NZ  . LYS D  1 18  ? 17.619  21.627  -43.490 1.00 24.06 ? 18  LYS D NZ  1 
ATOM   6588 N  N   . TYR D  1 19  ? 16.682  19.632  -35.586 1.00 10.18 ? 19  TYR D N   1 
ATOM   6589 C  CA  . TYR D  1 19  ? 15.559  19.090  -34.778 1.00 9.04  ? 19  TYR D CA  1 
ATOM   6590 C  C   . TYR D  1 19  ? 16.203  18.618  -33.496 1.00 9.73  ? 19  TYR D C   1 
ATOM   6591 O  O   . TYR D  1 19  ? 16.684  17.476  -33.417 1.00 9.78  ? 19  TYR D O   1 
ATOM   6592 C  CB  . TYR D  1 19  ? 14.876  17.905  -35.543 1.00 9.50  ? 19  TYR D CB  1 
ATOM   6593 C  CG  . TYR D  1 19  ? 14.296  18.323  -36.820 1.00 8.53  ? 19  TYR D CG  1 
ATOM   6594 C  CD1 . TYR D  1 19  ? 13.096  19.043  -36.869 1.00 10.03 ? 19  TYR D CD1 1 
ATOM   6595 C  CD2 . TYR D  1 19  ? 14.982  18.085  -38.038 1.00 10.41 ? 19  TYR D CD2 1 
ATOM   6596 C  CE1 . TYR D  1 19  ? 12.524  19.416  -38.078 1.00 11.22 ? 19  TYR D CE1 1 
ATOM   6597 C  CE2 . TYR D  1 19  ? 14.425  18.501  -39.266 1.00 10.33 ? 19  TYR D CE2 1 
ATOM   6598 C  CZ  . TYR D  1 19  ? 13.234  19.167  -39.247 1.00 12.57 ? 19  TYR D CZ  1 
ATOM   6599 O  OH  . TYR D  1 19  ? 12.641  19.547  -40.463 1.00 15.02 ? 19  TYR D OH  1 
ATOM   6600 N  N   . PRO D  1 20  ? 16.373  19.472  -32.467 1.00 10.29 ? 20  PRO D N   1 
ATOM   6601 C  CA  . PRO D  1 20  ? 17.147  19.070  -31.317 1.00 10.78 ? 20  PRO D CA  1 
ATOM   6602 C  C   . PRO D  1 20  ? 16.677  17.836  -30.574 1.00 9.40  ? 20  PRO D C   1 
ATOM   6603 O  O   . PRO D  1 20  ? 17.543  17.156  -29.996 1.00 9.89  ? 20  PRO D O   1 
ATOM   6604 C  CB  . PRO D  1 20  ? 17.076  20.292  -30.327 1.00 11.60 ? 20  PRO D CB  1 
ATOM   6605 C  CG  . PRO D  1 20  ? 16.480  21.325  -31.115 1.00 13.20 ? 20  PRO D CG  1 
ATOM   6606 C  CD  . PRO D  1 20  ? 15.911  20.876  -32.450 1.00 10.58 ? 20  PRO D CD  1 
ATOM   6607 N  N   . SER D  1 21  ? 15.367  17.534  -30.607 1.00 10.27 ? 21  SER D N   1 
ATOM   6608 C  CA  . SER D  1 21  ? 14.978  16.302  -29.881 1.00 9.50  ? 21  SER D CA  1 
ATOM   6609 C  C   . SER D  1 21  ? 15.536  15.035  -30.530 1.00 8.98  ? 21  SER D C   1 
ATOM   6610 O  O   . SER D  1 21  ? 15.621  14.047  -29.826 1.00 9.95  ? 21  SER D O   1 
ATOM   6611 C  CB  . SER D  1 21  ? 13.483  16.203  -29.875 1.00 9.22  ? 21  SER D CB  1 
ATOM   6612 O  OG  . SER D  1 21  ? 12.963  17.252  -28.969 1.00 12.35 ? 21  SER D OG  1 
ATOM   6613 N  N   . CYS D  1 22  ? 15.905  15.104  -31.813 1.00 9.91  ? 22  CYS D N   1 
ATOM   6614 C  CA  . CYS D  1 22  ? 16.535  13.942  -32.455 1.00 8.71  ? 22  CYS D CA  1 
ATOM   6615 C  C   . CYS D  1 22  ? 17.891  13.633  -31.827 1.00 10.58 ? 22  CYS D C   1 
ATOM   6616 O  O   . CYS D  1 22  ? 18.388  12.511  -32.041 1.00 9.82  ? 22  CYS D O   1 
ATOM   6617 C  CB  . CYS D  1 22  ? 16.695  14.159  -33.947 1.00 9.78  ? 22  CYS D CB  1 
ATOM   6618 S  SG  . CYS D  1 22  ? 15.129  14.427  -34.825 1.00 9.15  ? 22  CYS D SG  1 
ATOM   6619 N  N   . GLY D  1 23  ? 18.505  14.578  -31.081 1.00 11.09 ? 23  GLY D N   1 
ATOM   6620 C  CA  . GLY D  1 23  ? 19.718  14.326  -30.303 1.00 11.24 ? 23  GLY D CA  1 
ATOM   6621 C  C   . GLY D  1 23  ? 19.483  14.302  -28.797 1.00 13.27 ? 23  GLY D C   1 
ATOM   6622 O  O   . GLY D  1 23  ? 20.466  14.317  -27.979 1.00 14.53 ? 23  GLY D O   1 
ATOM   6623 N  N   . GLY D  1 24  ? 18.247  14.200  -28.389 1.00 12.00 ? 24  GLY D N   1 
ATOM   6624 C  CA  . GLY D  1 24  ? 17.900  14.094  -26.945 1.00 15.16 ? 24  GLY D CA  1 
ATOM   6625 C  C   . GLY D  1 24  ? 17.665  12.693  -26.467 1.00 16.17 ? 24  GLY D C   1 
ATOM   6626 O  O   . GLY D  1 24  ? 18.148  11.734  -27.028 1.00 17.01 ? 24  GLY D O   1 
ATOM   6627 N  N   . LEU D  1 25  ? 17.074  12.613  -25.314 1.00 15.04 ? 25  LEU D N   1 
ATOM   6628 C  CA  . LEU D  1 25  ? 16.857  11.341  -24.708 1.00 15.82 ? 25  LEU D CA  1 
ATOM   6629 C  C   . LEU D  1 25  ? 15.599  10.610  -25.243 1.00 13.35 ? 25  LEU D C   1 
ATOM   6630 O  O   . LEU D  1 25  ? 14.739  11.167  -25.936 1.00 13.37 ? 25  LEU D O   1 
ATOM   6631 C  CB  . LEU D  1 25  ? 16.727  11.543  -23.178 1.00 18.19 ? 25  LEU D CB  1 
ATOM   6632 C  CG  . LEU D  1 25  ? 18.020  12.070  -22.482 1.00 19.15 ? 25  LEU D CG  1 
ATOM   6633 C  CD1 . LEU D  1 25  ? 17.656  12.375  -21.032 1.00 24.43 ? 25  LEU D CD1 1 
ATOM   6634 C  CD2 . LEU D  1 25  ? 19.165  11.051  -22.562 1.00 21.83 ? 25  LEU D CD2 1 
ATOM   6635 N  N   . LEU D  1 26  ? 15.547  9.312   -24.897 1.00 12.93 ? 26  LEU D N   1 
ATOM   6636 C  CA  . LEU D  1 26  ? 14.302  8.495   -25.072 1.00 12.66 ? 26  LEU D CA  1 
ATOM   6637 C  C   . LEU D  1 26  ? 13.867  8.309   -26.495 1.00 9.54  ? 26  LEU D C   1 
ATOM   6638 O  O   . LEU D  1 26  ? 12.701  8.451   -26.871 1.00 10.60 ? 26  LEU D O   1 
ATOM   6639 C  CB  . LEU D  1 26  ? 13.129  8.999   -24.239 1.00 15.72 ? 26  LEU D CB  1 
ATOM   6640 C  CG  . LEU D  1 26  ? 13.593  9.266   -22.763 1.00 17.67 ? 26  LEU D CG  1 
ATOM   6641 C  CD1 . LEU D  1 26  ? 12.353  9.676   -22.018 1.00 20.16 ? 26  LEU D CD1 1 
ATOM   6642 C  CD2 . LEU D  1 26  ? 14.239  8.043   -22.059 1.00 18.52 ? 26  LEU D CD2 1 
ATOM   6643 N  N   . GLN D  1 27  ? 14.879  8.084   -27.360 1.00 9.46  ? 27  GLN D N   1 
ATOM   6644 C  CA  . GLN D  1 27  ? 14.586  8.005   -28.826 1.00 8.74  ? 27  GLN D CA  1 
ATOM   6645 C  C   . GLN D  1 27  ? 14.157  6.626   -29.270 1.00 8.90  ? 27  GLN D C   1 
ATOM   6646 O  O   . GLN D  1 27  ? 14.556  5.607   -28.660 1.00 9.43  ? 27  GLN D O   1 
ATOM   6647 C  CB  . GLN D  1 27  ? 15.811  8.446   -29.669 1.00 7.94  ? 27  GLN D CB  1 
ATOM   6648 C  CG  . GLN D  1 27  ? 16.186  9.897   -29.343 1.00 8.66  ? 27  GLN D CG  1 
ATOM   6649 C  CD  . GLN D  1 27  ? 15.149  10.750  -30.012 1.00 8.44  ? 27  GLN D CD  1 
ATOM   6650 O  OE1 . GLN D  1 27  ? 15.204  10.966  -31.261 1.00 8.48  ? 27  GLN D OE1 1 
ATOM   6651 N  NE2 . GLN D  1 27  ? 14.235  11.373  -29.235 1.00 9.28  ? 27  GLN D NE2 1 
ATOM   6652 N  N   . SER D  1 28  ? 13.425  6.589   -30.346 1.00 7.49  ? 28  SER D N   1 
ATOM   6653 C  CA  . SER D  1 28  ? 13.000  5.329   -30.987 1.00 7.73  ? 28  SER D CA  1 
ATOM   6654 C  C   . SER D  1 28  ? 13.505  5.350   -32.388 1.00 7.96  ? 28  SER D C   1 
ATOM   6655 O  O   . SER D  1 28  ? 13.823  6.368   -32.979 1.00 7.83  ? 28  SER D O   1 
ATOM   6656 C  CB  . SER D  1 28  ? 11.488  5.361   -31.033 1.00 7.96  ? 28  SER D CB  1 
ATOM   6657 O  OG  . SER D  1 28  ? 10.978  5.262   -29.709 1.00 8.19  ? 28  SER D OG  1 
ATOM   6658 N  N   . PRO D  1 29  ? 13.630  4.188   -33.051 1.00 7.31  ? 29  PRO D N   1 
ATOM   6659 C  CA  . PRO D  1 29  ? 13.303  2.826   -32.518 1.00 7.84  ? 29  PRO D CA  1 
ATOM   6660 C  C   . PRO D  1 29  ? 14.420  2.235   -31.696 1.00 8.59  ? 29  PRO D C   1 
ATOM   6661 O  O   . PRO D  1 29  ? 15.438  2.874   -31.510 1.00 8.91  ? 29  PRO D O   1 
ATOM   6662 C  CB  . PRO D  1 29  ? 13.075  1.995   -33.821 1.00 8.09  ? 29  PRO D CB  1 
ATOM   6663 C  CG  . PRO D  1 29  ? 14.189  2.598   -34.751 1.00 7.40  ? 29  PRO D CG  1 
ATOM   6664 C  CD  . PRO D  1 29  ? 14.175  4.106   -34.433 1.00 8.16  ? 29  PRO D CD  1 
ATOM   6665 N  N   . ILE D  1 30  ? 14.167  1.015   -31.193 1.00 7.21  ? 30  ILE D N   1 
ATOM   6666 C  CA  . ILE D  1 30  ? 15.154  0.267   -30.348 1.00 9.13  ? 30  ILE D CA  1 
ATOM   6667 C  C   . ILE D  1 30  ? 15.135  -1.167  -30.785 1.00 8.05  ? 30  ILE D C   1 
ATOM   6668 O  O   . ILE D  1 30  ? 14.231  -1.619  -31.467 1.00 8.03  ? 30  ILE D O   1 
ATOM   6669 C  CB  . ILE D  1 30  ? 14.840  0.467   -28.855 1.00 9.52  ? 30  ILE D CB  1 
ATOM   6670 C  CG1 . ILE D  1 30  ? 13.409  -0.049  -28.551 1.00 11.19 ? 30  ILE D CG1 1 
ATOM   6671 C  CG2 . ILE D  1 30  ? 15.063  1.904   -28.395 1.00 9.83  ? 30  ILE D CG2 1 
ATOM   6672 C  CD1 . ILE D  1 30  ? 13.127  -0.207  -27.069 1.00 13.59 ? 30  ILE D CD1 1 
ATOM   6673 N  N   . ASP D  1 31  ? 16.186  -1.836  -30.334 1.00 8.67  ? 31  ASP D N   1 
ATOM   6674 C  CA  . ASP D  1 31  ? 16.289  -3.306  -30.491 1.00 9.71  ? 31  ASP D CA  1 
ATOM   6675 C  C   . ASP D  1 31  ? 15.668  -3.991  -29.287 1.00 11.32 ? 31  ASP D C   1 
ATOM   6676 O  O   . ASP D  1 31  ? 16.104  -3.785  -28.178 1.00 13.00 ? 31  ASP D O   1 
ATOM   6677 C  CB  . ASP D  1 31  ? 17.772  -3.714  -30.567 1.00 11.57 ? 31  ASP D CB  1 
ATOM   6678 C  CG  . ASP D  1 31  ? 17.895  -5.248  -30.695 1.00 13.02 ? 31  ASP D CG  1 
ATOM   6679 O  OD1 . ASP D  1 31  ? 17.355  -5.797  -31.651 1.00 11.12 ? 31  ASP D OD1 1 
ATOM   6680 O  OD2 . ASP D  1 31  ? 18.532  -5.831  -29.850 1.00 16.75 ? 31  ASP D OD2 1 
ATOM   6681 N  N   . LEU D  1 32  ? 14.770  -4.917  -29.574 1.00 10.25 ? 32  LEU D N   1 
ATOM   6682 C  CA  . LEU D  1 32  ? 13.990  -5.556  -28.495 1.00 11.10 ? 32  LEU D CA  1 
ATOM   6683 C  C   . LEU D  1 32  ? 14.752  -6.872  -28.207 1.00 12.31 ? 32  LEU D C   1 
ATOM   6684 O  O   . LEU D  1 32  ? 14.819  -7.741  -29.086 1.00 12.03 ? 32  LEU D O   1 
ATOM   6685 C  CB  . LEU D  1 32  ? 12.576  -5.870  -29.012 1.00 10.80 ? 32  LEU D CB  1 
ATOM   6686 C  CG  . LEU D  1 32  ? 11.825  -4.580  -29.352 1.00 11.67 ? 32  LEU D CG  1 
ATOM   6687 C  CD1 . LEU D  1 32  ? 10.526  -4.949  -30.070 1.00 12.12 ? 32  LEU D CD1 1 
ATOM   6688 C  CD2 . LEU D  1 32  ? 11.566  -3.692  -28.121 1.00 13.61 ? 32  LEU D CD2 1 
ATOM   6689 N  N   . HIS D  1 33  ? 15.482  -6.964  -27.073 1.00 11.80 ? 33  HIS D N   1 
ATOM   6690 C  CA  . HIS D  1 33  ? 16.265  -8.131  -26.789 1.00 11.74 ? 33  HIS D CA  1 
ATOM   6691 C  C   . HIS D  1 33  ? 16.188  -8.470  -25.324 1.00 12.34 ? 33  HIS D C   1 
ATOM   6692 O  O   . HIS D  1 33  ? 15.904  -7.574  -24.500 1.00 12.41 ? 33  HIS D O   1 
ATOM   6693 C  CB  . HIS D  1 33  ? 17.743  -7.980  -27.303 1.00 13.98 ? 33  HIS D CB  1 
ATOM   6694 C  CG  . HIS D  1 33  ? 18.512  -6.909  -26.611 1.00 12.80 ? 33  HIS D CG  1 
ATOM   6695 N  ND1 . HIS D  1 33  ? 18.432  -5.588  -26.914 1.00 16.00 ? 33  HIS D ND1 1 
ATOM   6696 C  CD2 . HIS D  1 33  ? 19.393  -6.997  -25.526 1.00 12.92 ? 33  HIS D CD2 1 
ATOM   6697 C  CE1 . HIS D  1 33  ? 19.264  -4.902  -26.096 1.00 18.86 ? 33  HIS D CE1 1 
ATOM   6698 N  NE2 . HIS D  1 33  ? 19.828  -5.773  -25.258 1.00 16.07 ? 33  HIS D NE2 1 
ATOM   6699 N  N   . SER D  1 34  ? 16.513  -9.759  -25.054 1.00 12.89 ? 34  SER D N   1 
ATOM   6700 C  CA  . SER D  1 34  ? 16.152  -10.339 -23.687 1.00 13.13 ? 34  SER D CA  1 
ATOM   6701 C  C   . SER D  1 34  ? 16.665  -9.526  -22.519 1.00 13.33 ? 34  SER D C   1 
ATOM   6702 O  O   . SER D  1 34  ? 15.899  -9.333  -21.528 1.00 13.94 ? 34  SER D O   1 
ATOM   6703 C  CB  . SER D  1 34  ? 16.657  -11.770 -23.703 1.00 16.37 ? 34  SER D CB  1 
ATOM   6704 O  OG  . SER D  1 34  ? 18.053  -11.709 -23.749 1.00 20.70 ? 34  SER D OG  1 
ATOM   6705 N  N   . ASP D  1 35  ? 17.879  -8.951  -22.572 1.00 11.82 ? 35  ASP D N   1 
ATOM   6706 C  CA  . ASP D  1 35  ? 18.444  -8.390  -21.354 1.00 12.89 ? 35  ASP D CA  1 
ATOM   6707 C  C   . ASP D  1 35  ? 17.649  -7.200  -20.860 1.00 14.05 ? 35  ASP D C   1 
ATOM   6708 O  O   . ASP D  1 35  ? 17.701  -6.861  -19.677 1.00 15.69 ? 35  ASP D O   1 
ATOM   6709 C  CB  . ASP D  1 35  ? 19.902  -7.866  -21.584 1.00 15.92 ? 35  ASP D CB  1 
ATOM   6710 C  CG  . ASP D  1 35  ? 20.783  -8.844  -22.186 1.00 19.54 ? 35  ASP D CG  1 
ATOM   6711 O  OD1 . ASP D  1 35  ? 21.739  -9.253  -21.458 1.00 17.24 ? 35  ASP D OD1 1 
ATOM   6712 O  OD2 . ASP D  1 35  ? 20.537  -9.192  -23.376 1.00 19.32 ? 35  ASP D OD2 1 
ATOM   6713 N  N   . ILE D  1 36  ? 16.897  -6.548  -21.790 1.00 12.44 ? 36  ILE D N   1 
ATOM   6714 C  CA  . ILE D  1 36  ? 16.163  -5.299  -21.455 1.00 11.95 ? 36  ILE D CA  1 
ATOM   6715 C  C   . ILE D  1 36  ? 14.677  -5.507  -21.360 1.00 13.43 ? 36  ILE D C   1 
ATOM   6716 O  O   . ILE D  1 36  ? 13.967  -4.469  -21.166 1.00 14.61 ? 36  ILE D O   1 
ATOM   6717 C  CB  . ILE D  1 36  ? 16.625  -4.064  -22.288 1.00 13.88 ? 36  ILE D CB  1 
ATOM   6718 C  CG1 . ILE D  1 36  ? 16.505  -4.327  -23.781 1.00 14.65 ? 36  ILE D CG1 1 
ATOM   6719 C  CG2 . ILE D  1 36  ? 18.081  -3.700  -21.886 1.00 16.83 ? 36  ILE D CG2 1 
ATOM   6720 C  CD1 . ILE D  1 36  ? 15.090  -4.501  -24.335 1.00 15.89 ? 36  ILE D CD1 1 
ATOM   6721 N  N   . LEU D  1 37  ? 14.204  -6.773  -21.430 1.00 11.53 ? 37  LEU D N   1 
ATOM   6722 C  CA  . LEU D  1 37  ? 12.751  -7.078  -21.351 1.00 12.12 ? 37  LEU D CA  1 
ATOM   6723 C  C   . LEU D  1 37  ? 12.339  -7.411  -19.959 1.00 14.48 ? 37  LEU D C   1 
ATOM   6724 O  O   . LEU D  1 37  ? 13.066  -8.099  -19.243 1.00 15.81 ? 37  LEU D O   1 
ATOM   6725 C  CB  . LEU D  1 37  ? 12.399  -8.262  -22.225 1.00 12.31 ? 37  LEU D CB  1 
ATOM   6726 C  CG  . LEU D  1 37  ? 12.655  -8.032  -23.753 1.00 11.88 ? 37  LEU D CG  1 
ATOM   6727 C  CD1 . LEU D  1 37  ? 12.352  -9.281  -24.540 1.00 16.26 ? 37  LEU D CD1 1 
ATOM   6728 C  CD2 . LEU D  1 37  ? 12.017  -6.862  -24.423 1.00 12.61 ? 37  LEU D CD2 1 
ATOM   6729 N  N   . GLN D  1 38  ? 11.204  -6.867  -19.533 1.00 11.28 ? 38  GLN D N   1 
ATOM   6730 C  CA  . GLN D  1 38  ? 10.734  -7.220  -18.200 1.00 13.57 ? 38  GLN D CA  1 
ATOM   6731 C  C   . GLN D  1 38  ? 9.225   -7.397  -18.269 1.00 12.38 ? 38  GLN D C   1 
ATOM   6732 O  O   . GLN D  1 38  ? 8.494   -6.503  -18.669 1.00 11.93 ? 38  GLN D O   1 
ATOM   6733 C  CB  . GLN D  1 38  ? 11.049  -6.120  -17.265 1.00 15.47 ? 38  GLN D CB  1 
ATOM   6734 C  CG  . GLN D  1 38  ? 10.659  -6.526  -15.851 1.00 21.17 ? 38  GLN D CG  1 
ATOM   6735 C  CD  . GLN D  1 38  ? 11.323  -5.619  -14.901 1.00 24.09 ? 38  GLN D CD  1 
ATOM   6736 O  OE1 . GLN D  1 38  ? 12.509  -5.754  -14.651 1.00 29.77 ? 38  GLN D OE1 1 
ATOM   6737 N  NE2 . GLN D  1 38  ? 10.579  -4.689  -14.357 1.00 26.01 ? 38  GLN D NE2 1 
ATOM   6738 N  N   . TYR D  1 39  ? 8.728   -8.526  -17.763 1.00 12.43 ? 39  TYR D N   1 
ATOM   6739 C  CA  . TYR D  1 39  ? 7.278   -8.776  -17.762 1.00 11.11 ? 39  TYR D CA  1 
ATOM   6740 C  C   . TYR D  1 39  ? 6.575   -7.808  -16.793 1.00 11.27 ? 39  TYR D C   1 
ATOM   6741 O  O   . TYR D  1 39  ? 7.093   -7.541  -15.702 1.00 12.82 ? 39  TYR D O   1 
ATOM   6742 C  CB  . TYR D  1 39  ? 7.022   -10.263 -17.375 1.00 12.24 ? 39  TYR D CB  1 
ATOM   6743 C  CG  . TYR D  1 39  ? 5.553   -10.511 -17.059 1.00 12.94 ? 39  TYR D CG  1 
ATOM   6744 C  CD1 . TYR D  1 39  ? 4.606   -10.528 -18.061 1.00 13.81 ? 39  TYR D CD1 1 
ATOM   6745 C  CD2 . TYR D  1 39  ? 5.121   -10.723 -15.704 1.00 13.21 ? 39  TYR D CD2 1 
ATOM   6746 C  CE1 . TYR D  1 39  ? 3.248   -10.761 -17.778 1.00 13.97 ? 39  TYR D CE1 1 
ATOM   6747 C  CE2 . TYR D  1 39  ? 3.777   -10.920 -15.452 1.00 11.70 ? 39  TYR D CE2 1 
ATOM   6748 C  CZ  . TYR D  1 39  ? 2.883   -10.959 -16.420 1.00 12.06 ? 39  TYR D CZ  1 
ATOM   6749 O  OH  . TYR D  1 39  ? 1.508   -11.170 -16.230 1.00 17.07 ? 39  TYR D OH  1 
ATOM   6750 N  N   . ASP D  1 40  ? 5.429   -7.260  -17.232 1.00 11.56 ? 40  ASP D N   1 
ATOM   6751 C  CA  . ASP D  1 40  ? 4.677   -6.312  -16.381 1.00 11.86 ? 40  ASP D CA  1 
ATOM   6752 C  C   . ASP D  1 40  ? 3.289   -6.738  -16.444 1.00 11.27 ? 40  ASP D C   1 
ATOM   6753 O  O   . ASP D  1 40  ? 2.585   -6.634  -17.495 1.00 10.86 ? 40  ASP D O   1 
ATOM   6754 C  CB  . ASP D  1 40  ? 4.888   -4.922  -16.964 1.00 11.50 ? 40  ASP D CB  1 
ATOM   6755 C  CG  . ASP D  1 40  ? 4.173   -3.840  -16.178 1.00 17.23 ? 40  ASP D CG  1 
ATOM   6756 O  OD1 . ASP D  1 40  ? 3.393   -4.101  -15.236 1.00 13.07 ? 40  ASP D OD1 1 
ATOM   6757 O  OD2 . ASP D  1 40  ? 4.396   -2.635  -16.531 1.00 19.58 ? 40  ASP D OD2 1 
ATOM   6758 N  N   . ALA D  1 41  ? 2.751   -7.218  -15.271 1.00 9.53  ? 41  ALA D N   1 
ATOM   6759 C  CA  . ALA D  1 41  ? 1.313   -7.644  -15.202 1.00 10.73 ? 41  ALA D CA  1 
ATOM   6760 C  C   . ALA D  1 41  ? 0.271   -6.529  -15.372 1.00 11.45 ? 41  ALA D C   1 
ATOM   6761 O  O   . ALA D  1 41  ? -0.893  -6.778  -15.664 1.00 12.97 ? 41  ALA D O   1 
ATOM   6762 C  CB  . ALA D  1 41  ? 1.124   -8.380  -13.873 1.00 11.68 ? 41  ALA D CB  1 
ATOM   6763 N  N   . SER D  1 42  ? 0.744   -5.300  -15.372 1.00 10.87 ? 42  SER D N   1 
ATOM   6764 C  CA  . SER D  1 42  ? -0.148  -4.139  -15.582 1.00 13.27 ? 42  SER D CA  1 
ATOM   6765 C  C   . SER D  1 42  ? -0.561  -4.004  -17.059 1.00 15.00 ? 42  SER D C   1 
ATOM   6766 O  O   . SER D  1 42  ? -1.441  -3.179  -17.410 1.00 16.60 ? 42  SER D O   1 
ATOM   6767 C  CB  . SER D  1 42  ? 0.424   -2.855  -14.965 1.00 15.38 ? 42  SER D CB  1 
ATOM   6768 O  OG  . SER D  1 42  ? 1.375   -2.316  -15.855 1.00 18.67 ? 42  SER D OG  1 
ATOM   6769 N  N   . LEU D  1 43  ? 0.137   -4.711  -17.967 1.00 12.81 ? 43  LEU D N   1 
ATOM   6770 C  CA  . LEU D  1 43  ? -0.059  -4.536  -19.407 1.00 14.09 ? 43  LEU D CA  1 
ATOM   6771 C  C   . LEU D  1 43  ? -1.146  -5.413  -19.851 1.00 13.13 ? 43  LEU D C   1 
ATOM   6772 O  O   . LEU D  1 43  ? -1.014  -6.502  -20.360 1.00 13.37 ? 43  LEU D O   1 
ATOM   6773 C  CB  . LEU D  1 43  ? 1.246   -4.797  -20.146 1.00 12.06 ? 43  LEU D CB  1 
ATOM   6774 C  CG  . LEU D  1 43  ? 2.415   -3.861  -19.817 1.00 12.98 ? 43  LEU D CG  1 
ATOM   6775 C  CD1 . LEU D  1 43  ? 3.579   -4.270  -20.699 1.00 12.92 ? 43  LEU D CD1 1 
ATOM   6776 C  CD2 . LEU D  1 43  ? 2.069   -2.398  -20.041 1.00 15.83 ? 43  LEU D CD2 1 
ATOM   6777 N  N   . THR D  1 44  ? -2.374  -4.867  -19.669 1.00 15.30 ? 44  THR D N   1 
ATOM   6778 C  CA  . THR D  1 44  ? -3.574  -5.593  -19.996 1.00 14.61 ? 44  THR D CA  1 
ATOM   6779 C  C   . THR D  1 44  ? -3.937  -5.416  -21.502 1.00 13.42 ? 44  THR D C   1 
ATOM   6780 O  O   . THR D  1 44  ? -3.352  -4.545  -22.130 1.00 12.33 ? 44  THR D O   1 
ATOM   6781 C  CB  . THR D  1 44  ? -4.759  -5.042  -19.094 1.00 12.91 ? 44  THR D CB  1 
ATOM   6782 O  OG1 . THR D  1 44  ? -4.778  -3.643  -19.179 1.00 18.77 ? 44  THR D OG1 1 
ATOM   6783 C  CG2 . THR D  1 44  ? -4.459  -5.282  -17.570 1.00 20.71 ? 44  THR D CG2 1 
ATOM   6784 N  N   . PRO D  1 45  ? -4.908  -6.149  -22.045 1.00 13.96 ? 45  PRO D N   1 
ATOM   6785 C  CA  . PRO D  1 45  ? -5.159  -6.138  -23.517 1.00 14.37 ? 45  PRO D CA  1 
ATOM   6786 C  C   . PRO D  1 45  ? -5.759  -4.784  -23.967 1.00 14.11 ? 45  PRO D C   1 
ATOM   6787 O  O   . PRO D  1 45  ? -6.626  -4.226  -23.297 1.00 16.95 ? 45  PRO D O   1 
ATOM   6788 C  CB  . PRO D  1 45  ? -6.155  -7.248  -23.701 1.00 15.86 ? 45  PRO D CB  1 
ATOM   6789 C  CG  . PRO D  1 45  ? -5.884  -8.134  -22.474 1.00 15.81 ? 45  PRO D CG  1 
ATOM   6790 C  CD  . PRO D  1 45  ? -5.659  -7.197  -21.357 1.00 14.50 ? 45  PRO D CD  1 
ATOM   6791 N  N   . LEU D  1 46  ? -5.258  -4.253  -25.073 1.00 13.84 ? 46  LEU D N   1 
ATOM   6792 C  CA  . LEU D  1 46  ? -5.905  -3.068  -25.652 1.00 13.24 ? 46  LEU D CA  1 
ATOM   6793 C  C   . LEU D  1 46  ? -7.135  -3.463  -26.394 1.00 13.92 ? 46  LEU D C   1 
ATOM   6794 O  O   . LEU D  1 46  ? -7.288  -4.571  -26.895 1.00 15.34 ? 46  LEU D O   1 
ATOM   6795 C  CB  . LEU D  1 46  ? -4.967  -2.481  -26.663 1.00 14.77 ? 46  LEU D CB  1 
ATOM   6796 C  CG  . LEU D  1 46  ? -3.669  -1.918  -26.021 1.00 15.74 ? 46  LEU D CG  1 
ATOM   6797 C  CD1 . LEU D  1 46  ? -2.702  -1.413  -27.102 1.00 18.05 ? 46  LEU D CD1 1 
ATOM   6798 C  CD2 . LEU D  1 46  ? -4.002  -0.827  -24.944 1.00 17.09 ? 46  LEU D CD2 1 
ATOM   6799 N  N   . GLU D  1 47  ? -8.048  -2.505  -26.461 1.00 14.12 ? 47  GLU D N   1 
ATOM   6800 C  CA  . GLU D  1 47  ? -9.203  -2.636  -27.266 1.00 14.39 ? 47  GLU D CA  1 
ATOM   6801 C  C   . GLU D  1 47  ? -9.157  -1.584  -28.435 1.00 12.46 ? 47  GLU D C   1 
ATOM   6802 O  O   . GLU D  1 47  ? -8.817  -0.369  -28.233 1.00 15.93 ? 47  GLU D O   1 
ATOM   6803 C  CB  . GLU D  1 47  ? -10.521 -2.483  -26.464 1.00 19.63 ? 47  GLU D CB  1 
ATOM   6804 C  CG  . GLU D  1 47  ? -10.990 -3.799  -25.760 1.00 29.03 ? 47  GLU D CG  1 
ATOM   6805 C  CD  . GLU D  1 47  ? -12.345 -3.660  -25.044 1.00 35.09 ? 47  GLU D CD  1 
ATOM   6806 O  OE1 . GLU D  1 47  ? -13.169 -2.812  -25.481 1.00 44.60 ? 47  GLU D OE1 1 
ATOM   6807 O  OE2 . GLU D  1 47  ? -12.554 -4.340  -24.016 1.00 45.05 ? 47  GLU D OE2 1 
ATOM   6808 N  N   . PHE D  1 48  ? -9.530  -2.111  -29.600 1.00 14.25 ? 48  PHE D N   1 
ATOM   6809 C  CA  . PHE D  1 48  ? -9.486  -1.318  -30.868 1.00 14.12 ? 48  PHE D CA  1 
ATOM   6810 C  C   . PHE D  1 48  ? -10.907 -1.010  -31.257 1.00 15.74 ? 48  PHE D C   1 
ATOM   6811 O  O   . PHE D  1 48  ? -11.621 -1.885  -31.786 1.00 19.57 ? 48  PHE D O   1 
ATOM   6812 C  CB  . PHE D  1 48  ? -8.723  -2.096  -31.969 1.00 14.30 ? 48  PHE D CB  1 
ATOM   6813 C  CG  . PHE D  1 48  ? -7.458  -2.680  -31.469 1.00 13.12 ? 48  PHE D CG  1 
ATOM   6814 C  CD1 . PHE D  1 48  ? -6.380  -1.896  -31.202 1.00 12.89 ? 48  PHE D CD1 1 
ATOM   6815 C  CD2 . PHE D  1 48  ? -7.362  -4.090  -31.226 1.00 14.43 ? 48  PHE D CD2 1 
ATOM   6816 C  CE1 . PHE D  1 48  ? -5.216  -2.410  -30.603 1.00 16.22 ? 48  PHE D CE1 1 
ATOM   6817 C  CE2 . PHE D  1 48  ? -6.169  -4.637  -30.683 1.00 15.30 ? 48  PHE D CE2 1 
ATOM   6818 C  CZ  . PHE D  1 48  ? -5.098  -3.750  -30.387 1.00 13.64 ? 48  PHE D CZ  1 
ATOM   6819 N  N   . GLN D  1 49  ? -11.232 0.275   -31.107 1.00 13.08 ? 49  GLN D N   1 
ATOM   6820 C  CA  . GLN D  1 49  ? -12.614 0.754   -31.242 1.00 15.18 ? 49  GLN D CA  1 
ATOM   6821 C  C   . GLN D  1 49  ? -12.695 1.593   -32.486 1.00 12.85 ? 49  GLN D C   1 
ATOM   6822 O  O   . GLN D  1 49  ? -11.897 2.498   -32.765 1.00 13.58 ? 49  GLN D O   1 
ATOM   6823 C  CB  . GLN D  1 49  ? -13.043 1.602   -30.052 1.00 17.39 ? 49  GLN D CB  1 
ATOM   6824 C  CG  . GLN D  1 49  ? -12.782 1.031   -28.657 1.00 24.34 ? 49  GLN D CG  1 
ATOM   6825 C  CD  . GLN D  1 49  ? -13.592 -0.235  -28.308 1.00 33.71 ? 49  GLN D CD  1 
ATOM   6826 O  OE1 . GLN D  1 49  ? -14.360 -0.774  -29.116 1.00 40.32 ? 49  GLN D OE1 1 
ATOM   6827 N  NE2 . GLN D  1 49  ? -13.441 -0.696  -27.042 1.00 38.24 ? 49  GLN D NE2 1 
ATOM   6828 N  N   . GLY D  1 50  ? -13.717 1.322   -33.272 1.00 11.94 ? 50  GLY D N   1 
ATOM   6829 C  CA  . GLY D  1 50  ? -13.984 2.101   -34.432 1.00 12.22 ? 50  GLY D CA  1 
ATOM   6830 C  C   . GLY D  1 50  ? -12.984 1.874   -35.589 1.00 11.43 ? 50  GLY D C   1 
ATOM   6831 O  O   . GLY D  1 50  ? -12.907 2.687   -36.493 1.00 11.98 ? 50  GLY D O   1 
ATOM   6832 N  N   . TYR D  1 51  ? -12.299 0.746   -35.483 1.00 10.62 ? 51  TYR D N   1 
ATOM   6833 C  CA  . TYR D  1 51  ? -11.299 0.350   -36.566 1.00 10.87 ? 51  TYR D CA  1 
ATOM   6834 C  C   . TYR D  1 51  ? -11.938 -0.195  -37.848 1.00 10.81 ? 51  TYR D C   1 
ATOM   6835 O  O   . TYR D  1 51  ? -11.309 -0.282  -38.915 1.00 10.64 ? 51  TYR D O   1 
ATOM   6836 C  CB  . TYR D  1 51  ? -10.313 -0.733  -36.042 1.00 9.82  ? 51  TYR D CB  1 
ATOM   6837 C  CG  . TYR D  1 51  ? -9.108  -0.177  -35.313 1.00 9.67  ? 51  TYR D CG  1 
ATOM   6838 C  CD1 . TYR D  1 51  ? -9.250  0.816   -34.354 1.00 10.24 ? 51  TYR D CD1 1 
ATOM   6839 C  CD2 . TYR D  1 51  ? -7.829  -0.647  -35.583 1.00 10.30 ? 51  TYR D CD2 1 
ATOM   6840 C  CE1 . TYR D  1 51  ? -8.154  1.326   -33.684 1.00 11.16 ? 51  TYR D CE1 1 
ATOM   6841 C  CE2 . TYR D  1 51  ? -6.726  -0.142  -34.918 1.00 10.30 ? 51  TYR D CE2 1 
ATOM   6842 C  CZ  . TYR D  1 51  ? -6.895  0.844   -33.969 1.00 11.86 ? 51  TYR D CZ  1 
ATOM   6843 O  OH  . TYR D  1 51  ? -5.807  1.357   -33.299 1.00 11.83 ? 51  TYR D OH  1 
ATOM   6844 N  N   . ASN D  1 52  ? -13.237 -0.602  -37.799 1.00 11.67 ? 52  ASN D N   1 
ATOM   6845 C  CA  . ASN D  1 52  ? -13.862 -1.153  -38.931 1.00 12.80 ? 52  ASN D CA  1 
ATOM   6846 C  C   . ASN D  1 52  ? -14.488 -0.074  -39.756 1.00 14.33 ? 52  ASN D C   1 
ATOM   6847 O  O   . ASN D  1 52  ? -15.625 0.326   -39.516 1.00 16.63 ? 52  ASN D O   1 
ATOM   6848 C  CB  . ASN D  1 52  ? -14.875 -2.222  -38.465 1.00 14.15 ? 52  ASN D CB  1 
ATOM   6849 C  CG  . ASN D  1 52  ? -15.485 -2.983  -39.616 1.00 17.49 ? 52  ASN D CG  1 
ATOM   6850 O  OD1 . ASN D  1 52  ? -15.270 -2.734  -40.743 1.00 18.57 ? 52  ASN D OD1 1 
ATOM   6851 N  ND2 . ASN D  1 52  ? -16.415 -3.859  -39.281 1.00 21.52 ? 52  ASN D ND2 1 
ATOM   6852 N  N   . LEU D  1 53  ? -13.722 0.507   -40.669 1.00 12.44 ? 53  LEU D N   1 
ATOM   6853 C  CA  . LEU D  1 53  ? -14.130 1.691   -41.468 1.00 11.44 ? 53  LEU D CA  1 
ATOM   6854 C  C   . LEU D  1 53  ? -15.089 1.232   -42.585 1.00 13.51 ? 53  LEU D C   1 
ATOM   6855 O  O   . LEU D  1 53  ? -14.834 0.230   -43.248 1.00 13.46 ? 53  LEU D O   1 
ATOM   6856 C  CB  . LEU D  1 53  ? -12.898 2.397   -42.049 1.00 12.38 ? 53  LEU D CB  1 
ATOM   6857 C  CG  . LEU D  1 53  ? -11.873 2.794   -40.924 1.00 13.18 ? 53  LEU D CG  1 
ATOM   6858 C  CD1 . LEU D  1 53  ? -10.719 3.515   -41.629 1.00 14.05 ? 53  LEU D CD1 1 
ATOM   6859 C  CD2 . LEU D  1 53  ? -12.483 3.705   -39.879 1.00 14.86 ? 53  LEU D CD2 1 
ATOM   6860 N  N   . SER D  1 54  ? -16.091 2.061   -42.827 1.00 12.66 ? 54  SER D N   1 
ATOM   6861 C  CA  . SER D  1 54  ? -17.073 1.673   -43.844 1.00 13.75 ? 54  SER D CA  1 
ATOM   6862 C  C   . SER D  1 54  ? -16.426 1.649   -45.243 1.00 12.73 ? 54  SER D C   1 
ATOM   6863 O  O   . SER D  1 54  ? -15.823 2.649   -45.649 1.00 13.53 ? 54  SER D O   1 
ATOM   6864 C  CB  . SER D  1 54  ? -18.218 2.670   -43.858 1.00 14.11 ? 54  SER D CB  1 
ATOM   6865 O  OG  . SER D  1 54  ? -19.148 2.235   -44.852 1.00 15.97 ? 54  SER D OG  1 
ATOM   6866 N  N   . ALA D  1 55  ? -16.741 0.605   -45.971 1.00 15.73 ? 55  ALA D N   1 
ATOM   6867 C  CA  . ALA D  1 55  ? -16.331 0.469   -47.368 1.00 18.36 ? 55  ALA D CA  1 
ATOM   6868 C  C   . ALA D  1 55  ? -16.998 1.530   -48.214 1.00 16.24 ? 55  ALA D C   1 
ATOM   6869 O  O   . ALA D  1 55  ? -16.613 1.788   -49.386 1.00 18.85 ? 55  ALA D O   1 
ATOM   6870 C  CB  . ALA D  1 55  ? -16.752 -0.925  -47.916 1.00 21.53 ? 55  ALA D CB  1 
ATOM   6871 N  N   . ASN D  1 56  ? -18.067 2.188   -47.742 1.00 16.75 ? 56  ASN D N   1 
ATOM   6872 C  CA  . ASN D  1 56  ? -18.663 3.305   -48.448 1.00 17.11 ? 56  ASN D CA  1 
ATOM   6873 C  C   . ASN D  1 56  ? -18.124 4.718   -48.145 1.00 17.94 ? 56  ASN D C   1 
ATOM   6874 O  O   . ASN D  1 56  ? -18.570 5.755   -48.727 1.00 19.20 ? 56  ASN D O   1 
ATOM   6875 C  CB  . ASN D  1 56  ? -20.218 3.371   -48.185 1.00 23.34 ? 56  ASN D CB  1 
ATOM   6876 C  CG  . ASN D  1 56  ? -20.992 2.306   -48.924 1.00 32.57 ? 56  ASN D CG  1 
ATOM   6877 O  OD1 . ASN D  1 56  ? -20.528 1.746   -49.917 1.00 32.95 ? 56  ASN D OD1 1 
ATOM   6878 N  ND2 . ASN D  1 56  ? -22.233 2.051   -48.460 1.00 38.30 ? 56  ASN D ND2 1 
ATOM   6879 N  N   A LYS D  1 57  ? -17.140 4.753   -47.265 0.50 15.24 ? 57  LYS D N   1 
ATOM   6880 N  N   B LYS D  1 57  ? -17.169 4.798   -47.233 0.50 14.73 ? 57  LYS D N   1 
ATOM   6881 C  CA  A LYS D  1 57  ? -16.464 5.975   -46.929 0.50 15.01 ? 57  LYS D CA  1 
ATOM   6882 C  CA  B LYS D  1 57  ? -16.502 6.062   -47.016 0.50 13.97 ? 57  LYS D CA  1 
ATOM   6883 C  C   A LYS D  1 57  ? -15.047 5.866   -47.510 0.50 14.92 ? 57  LYS D C   1 
ATOM   6884 C  C   B LYS D  1 57  ? -15.126 5.901   -47.654 0.50 14.78 ? 57  LYS D C   1 
ATOM   6885 O  O   A LYS D  1 57  ? -14.622 4.778   -47.899 0.50 14.90 ? 57  LYS D O   1 
ATOM   6886 O  O   B LYS D  1 57  ? -14.792 4.812   -48.165 0.50 13.74 ? 57  LYS D O   1 
ATOM   6887 C  CB  A LYS D  1 57  ? -16.433 6.105   -45.421 0.50 15.01 ? 57  LYS D CB  1 
ATOM   6888 C  CB  B LYS D  1 57  ? -16.360 6.371   -45.526 0.50 13.57 ? 57  LYS D CB  1 
ATOM   6889 C  CG  A LYS D  1 57  ? -17.845 6.249   -44.889 0.50 15.32 ? 57  LYS D CG  1 
ATOM   6890 C  CG  B LYS D  1 57  ? -17.640 6.909   -44.888 0.50 13.05 ? 57  LYS D CG  1 
ATOM   6891 C  CD  A LYS D  1 57  ? -17.861 6.627   -43.420 0.50 16.38 ? 57  LYS D CD  1 
ATOM   6892 C  CD  B LYS D  1 57  ? -17.377 7.261   -43.436 0.50 14.69 ? 57  LYS D CD  1 
ATOM   6893 C  CE  A LYS D  1 57  ? -19.151 7.380   -43.110 0.50 19.06 ? 57  LYS D CE  1 
ATOM   6894 C  CE  B LYS D  1 57  ? -18.635 7.780   -42.747 0.50 16.40 ? 57  LYS D CE  1 
ATOM   6895 N  NZ  A LYS D  1 57  ? -19.233 8.778   -43.645 0.50 19.40 ? 57  LYS D NZ  1 
ATOM   6896 N  NZ  B LYS D  1 57  ? -18.511 8.015   -41.304 0.50 17.25 ? 57  LYS D NZ  1 
ATOM   6897 N  N   . GLN D  1 58  ? -14.414 7.006   -47.679 1.00 13.89 ? 58  GLN D N   1 
ATOM   6898 C  CA  . GLN D  1 58  ? -13.086 6.958   -48.307 1.00 15.24 ? 58  GLN D CA  1 
ATOM   6899 C  C   . GLN D  1 58  ? -12.146 7.823   -47.487 1.00 12.54 ? 58  GLN D C   1 
ATOM   6900 O  O   . GLN D  1 58  ? -12.502 8.757   -46.775 1.00 13.43 ? 58  GLN D O   1 
ATOM   6901 C  CB  . GLN D  1 58  ? -13.164 7.279   -49.781 1.00 21.13 ? 58  GLN D CB  1 
ATOM   6902 C  CG  . GLN D  1 58  ? -13.546 8.659   -50.025 1.00 20.57 ? 58  GLN D CG  1 
ATOM   6903 C  CD  . GLN D  1 58  ? -13.674 8.945   -51.535 1.00 23.68 ? 58  GLN D CD  1 
ATOM   6904 O  OE1 . GLN D  1 58  ? -13.484 8.060   -52.415 1.00 23.05 ? 58  GLN D OE1 1 
ATOM   6905 N  NE2 . GLN D  1 58  ? -13.931 10.236  -51.824 1.00 23.64 ? 58  GLN D NE2 1 
ATOM   6906 N  N   . PHE D  1 59  ? -10.882 7.387   -47.519 1.00 11.20 ? 59  PHE D N   1 
ATOM   6907 C  CA  . PHE D  1 59  ? -9.805  7.906   -46.621 1.00 10.84 ? 59  PHE D CA  1 
ATOM   6908 C  C   . PHE D  1 59  ? -8.646  8.314   -47.473 1.00 9.33  ? 59  PHE D C   1 
ATOM   6909 O  O   . PHE D  1 59  ? -8.285  7.646   -48.426 1.00 11.49 ? 59  PHE D O   1 
ATOM   6910 C  CB  . PHE D  1 59  ? -9.481  6.791   -45.609 1.00 10.77 ? 59  PHE D CB  1 
ATOM   6911 C  CG  . PHE D  1 59  ? -10.680 6.494   -44.776 1.00 10.37 ? 59  PHE D CG  1 
ATOM   6912 C  CD1 . PHE D  1 59  ? -11.628 5.573   -45.263 1.00 11.55 ? 59  PHE D CD1 1 
ATOM   6913 C  CD2 . PHE D  1 59  ? -10.938 7.256   -43.610 1.00 11.78 ? 59  PHE D CD2 1 
ATOM   6914 C  CE1 . PHE D  1 59  ? -12.840 5.359   -44.519 1.00 11.33 ? 59  PHE D CE1 1 
ATOM   6915 C  CE2 . PHE D  1 59  ? -12.136 7.078   -42.908 1.00 12.33 ? 59  PHE D CE2 1 
ATOM   6916 C  CZ  . PHE D  1 59  ? -13.058 6.131   -43.342 1.00 11.74 ? 59  PHE D CZ  1 
ATOM   6917 N  N   . LEU D  1 60  ? -7.999  9.430   -47.119 1.00 10.11 ? 60  LEU D N   1 
ATOM   6918 C  CA  . LEU D  1 60  ? -6.989  10.053  -47.985 1.00 11.91 ? 60  LEU D CA  1 
ATOM   6919 C  C   . LEU D  1 60  ? -5.631  9.416   -47.765 1.00 11.32 ? 60  LEU D C   1 
ATOM   6920 O  O   . LEU D  1 60  ? -5.086  9.353   -46.659 1.00 11.45 ? 60  LEU D O   1 
ATOM   6921 C  CB  . LEU D  1 60  ? -6.886  11.519  -47.592 1.00 13.48 ? 60  LEU D CB  1 
ATOM   6922 C  CG  . LEU D  1 60  ? -6.137  12.377  -48.575 1.00 14.88 ? 60  LEU D CG  1 
ATOM   6923 C  CD1 . LEU D  1 60  ? -6.820  12.523  -49.906 1.00 16.85 ? 60  LEU D CD1 1 
ATOM   6924 C  CD2 . LEU D  1 60  ? -5.869  13.706  -47.903 1.00 18.93 ? 60  LEU D CD2 1 
ATOM   6925 N  N   . LEU D  1 61  ? -5.101  8.934   -48.865 1.00 10.58 ? 61  LEU D N   1 
ATOM   6926 C  CA  . LEU D  1 61  ? -3.712  8.405   -48.948 1.00 10.69 ? 61  LEU D CA  1 
ATOM   6927 C  C   . LEU D  1 61  ? -2.823  9.472   -49.546 1.00 10.05 ? 61  LEU D C   1 
ATOM   6928 O  O   . LEU D  1 61  ? -3.186  10.099  -50.575 1.00 12.73 ? 61  LEU D O   1 
ATOM   6929 C  CB  . LEU D  1 61  ? -3.667  7.180   -49.840 1.00 12.19 ? 61  LEU D CB  1 
ATOM   6930 C  CG  . LEU D  1 61  ? -2.432  6.295   -49.847 1.00 11.44 ? 61  LEU D CG  1 
ATOM   6931 C  CD1 . LEU D  1 61  ? -2.331  5.564   -48.516 1.00 11.21 ? 61  LEU D CD1 1 
ATOM   6932 C  CD2 . LEU D  1 61  ? -2.456  5.284   -51.036 1.00 11.88 ? 61  LEU D CD2 1 
ATOM   6933 N  N   . THR D  1 62  ? -1.663  9.724   -48.914 1.00 10.83 ? 62  THR D N   1 
ATOM   6934 C  CA  . THR D  1 62  ? -0.807  10.802  -49.428 1.00 11.81 ? 62  THR D CA  1 
ATOM   6935 C  C   . THR D  1 62  ? 0.675   10.340  -49.345 1.00 10.92 ? 62  THR D C   1 
ATOM   6936 O  O   . THR D  1 62  ? 1.123   9.646   -48.389 1.00 11.11 ? 62  THR D O   1 
ATOM   6937 C  CB  . THR D  1 62  ? -0.877  12.006  -48.479 1.00 14.33 ? 62  THR D CB  1 
ATOM   6938 O  OG1 . THR D  1 62  ? -2.218  12.481  -48.277 1.00 19.03 ? 62  THR D OG1 1 
ATOM   6939 C  CG2 . THR D  1 62  ? -0.076  13.258  -48.974 1.00 17.47 ? 62  THR D CG2 1 
ATOM   6940 N  N   . ASN D  1 63  ? 1.413   10.737  -50.347 1.00 11.14 ? 63  ASN D N   1 
ATOM   6941 C  CA  . ASN D  1 63  ? 2.887   10.675  -50.280 1.00 10.60 ? 63  ASN D CA  1 
ATOM   6942 C  C   . ASN D  1 63  ? 3.421   11.937  -49.691 1.00 11.01 ? 63  ASN D C   1 
ATOM   6943 O  O   . ASN D  1 63  ? 3.256   13.037  -50.273 1.00 11.59 ? 63  ASN D O   1 
ATOM   6944 C  CB  . ASN D  1 63  ? 3.365   10.397  -51.750 1.00 12.28 ? 63  ASN D CB  1 
ATOM   6945 C  CG  . ASN D  1 63  ? 4.912   10.459  -51.907 1.00 10.11 ? 63  ASN D CG  1 
ATOM   6946 O  OD1 . ASN D  1 63  ? 5.598   11.004  -51.023 1.00 10.05 ? 63  ASN D OD1 1 
ATOM   6947 N  ND2 . ASN D  1 63  ? 5.408   9.793   -52.910 1.00 10.95 ? 63  ASN D ND2 1 
ATOM   6948 N  N   . ASN D  1 64  ? 3.999   11.883  -48.522 1.00 10.57 ? 64  ASN D N   1 
ATOM   6949 C  CA  . ASN D  1 64  ? 4.390   13.119  -47.834 1.00 11.07 ? 64  ASN D CA  1 
ATOM   6950 C  C   . ASN D  1 64  ? 5.899   13.468  -48.054 1.00 10.45 ? 64  ASN D C   1 
ATOM   6951 O  O   . ASN D  1 64  ? 6.449   14.352  -47.308 1.00 13.01 ? 64  ASN D O   1 
ATOM   6952 C  CB  . ASN D  1 64  ? 4.068   13.120  -46.357 1.00 12.64 ? 64  ASN D CB  1 
ATOM   6953 C  CG  . ASN D  1 64  ? 4.824   12.081  -45.589 1.00 13.78 ? 64  ASN D CG  1 
ATOM   6954 O  OD1 . ASN D  1 64  ? 5.687   11.387  -46.119 1.00 10.74 ? 64  ASN D OD1 1 
ATOM   6955 N  ND2 . ASN D  1 64  ? 4.506   11.960  -44.278 1.00 17.18 ? 64  ASN D ND2 1 
ATOM   6956 N  N   . GLY D  1 65  ? 6.511   12.730  -48.961 1.00 10.04 ? 65  GLY D N   1 
ATOM   6957 C  CA  . GLY D  1 65  ? 7.952   12.897  -49.193 1.00 10.73 ? 65  GLY D CA  1 
ATOM   6958 C  C   . GLY D  1 65  ? 8.819   11.968  -48.345 1.00 11.37 ? 65  GLY D C   1 
ATOM   6959 O  O   . GLY D  1 65  ? 10.014  11.852  -48.609 1.00 11.55 ? 65  GLY D O   1 
ATOM   6960 N  N   . HIS D  1 66  ? 8.219   11.328  -47.339 1.00 10.04 ? 66  HIS D N   1 
ATOM   6961 C  CA  . HIS D  1 66  ? 9.031   10.492  -46.413 1.00 9.61  ? 66  HIS D CA  1 
ATOM   6962 C  C   . HIS D  1 66  ? 8.470   9.106   -46.227 1.00 9.74  ? 66  HIS D C   1 
ATOM   6963 O  O   . HIS D  1 66  ? 9.200   8.168   -45.900 1.00 9.02  ? 66  HIS D O   1 
ATOM   6964 C  CB  . HIS D  1 66  ? 9.122   11.185  -45.018 1.00 11.14 ? 66  HIS D CB  1 
ATOM   6965 C  CG  . HIS D  1 66  ? 9.665   12.599  -45.080 1.00 11.88 ? 66  HIS D CG  1 
ATOM   6966 N  ND1 . HIS D  1 66  ? 10.986  12.868  -45.290 1.00 13.13 ? 66  HIS D ND1 1 
ATOM   6967 C  CD2 . HIS D  1 66  ? 9.024   13.778  -44.895 1.00 12.04 ? 66  HIS D CD2 1 
ATOM   6968 C  CE1 . HIS D  1 66  ? 11.135  14.261  -45.254 1.00 11.84 ? 66  HIS D CE1 1 
ATOM   6969 N  NE2 . HIS D  1 66  ? 9.949   14.794  -45.025 1.00 13.43 ? 66  HIS D NE2 1 
ATOM   6970 N  N   . SER D  1 67  ? 7.153   8.970   -46.407 1.00 10.07 ? 67  SER D N   1 
ATOM   6971 C  CA  . SER D  1 67  ? 6.472   7.661   -46.359 1.00 9.40  ? 67  SER D CA  1 
ATOM   6972 C  C   . SER D  1 67  ? 5.188   7.824   -47.159 1.00 10.74 ? 67  SER D C   1 
ATOM   6973 O  O   . SER D  1 67  ? 4.941   8.856   -47.735 1.00 11.02 ? 67  SER D O   1 
ATOM   6974 C  CB  . SER D  1 67  ? 6.105   7.333   -44.897 1.00 9.35  ? 67  SER D CB  1 
ATOM   6975 O  OG  . SER D  1 67  ? 5.558   6.041   -44.740 1.00 9.06  ? 67  SER D OG  1 
ATOM   6976 N  N   . VAL D  1 68  ? 4.367   6.778   -47.110 1.00 9.47  ? 68  VAL D N   1 
ATOM   6977 C  CA  . VAL D  1 68  ? 2.982   6.833   -47.633 1.00 10.55 ? 68  VAL D CA  1 
ATOM   6978 C  C   . VAL D  1 68  ? 2.117   6.762   -46.376 1.00 9.88  ? 68  VAL D C   1 
ATOM   6979 O  O   . VAL D  1 68  ? 2.290   5.916   -45.536 1.00 9.51  ? 68  VAL D O   1 
ATOM   6980 C  CB  . VAL D  1 68  ? 2.759   5.757   -48.687 1.00 11.05 ? 68  VAL D CB  1 
ATOM   6981 C  CG1 . VAL D  1 68  ? 2.967   4.347   -48.204 1.00 11.56 ? 68  VAL D CG1 1 
ATOM   6982 C  CG2 . VAL D  1 68  ? 1.320   5.862   -49.206 1.00 13.70 ? 68  VAL D CG2 1 
ATOM   6983 N  N   . LYS D  1 69  ? 1.151   7.686   -46.325 1.00 10.04 ? 69  LYS D N   1 
ATOM   6984 C  CA  . LYS D  1 69  ? 0.297   7.764   -45.158 1.00 10.24 ? 69  LYS D CA  1 
ATOM   6985 C  C   . LYS D  1 69  ? -1.180  7.736   -45.488 1.00 9.43  ? 69  LYS D C   1 
ATOM   6986 O  O   . LYS D  1 69  ? -1.572  8.205   -46.514 1.00 10.91 ? 69  LYS D O   1 
ATOM   6987 C  CB  . LYS D  1 69  ? 0.673   9.002   -44.340 1.00 14.09 ? 69  LYS D CB  1 
ATOM   6988 C  CG  . LYS D  1 69  ? 0.215   10.296  -44.770 1.00 18.52 ? 69  LYS D CG  1 
ATOM   6989 C  CD  . LYS D  1 69  ? 0.228   11.268  -43.505 1.00 17.74 ? 69  LYS D CD  1 
ATOM   6990 C  CE  . LYS D  1 69  ? -0.218  12.559  -44.133 1.00 19.93 ? 69  LYS D CE  1 
ATOM   6991 N  NZ  . LYS D  1 69  ? 0.014   13.674  -43.168 1.00 21.35 ? 69  LYS D NZ  1 
ATOM   6992 N  N   . LEU D  1 70  ? -1.956  7.025   -44.710 1.00 8.45  ? 70  LEU D N   1 
ATOM   6993 C  CA  . LEU D  1 70  ? -3.398  6.974   -44.822 1.00 8.87  ? 70  LEU D CA  1 
ATOM   6994 C  C   . LEU D  1 70  ? -3.948  7.742   -43.605 1.00 7.89  ? 70  LEU D C   1 
ATOM   6995 O  O   . LEU D  1 70  ? -3.758  7.404   -42.440 1.00 9.36  ? 70  LEU D O   1 
ATOM   6996 C  CB  . LEU D  1 70  ? -3.827  5.517   -44.761 1.00 9.89  ? 70  LEU D CB  1 
ATOM   6997 C  CG  . LEU D  1 70  ? -5.348  5.344   -44.977 1.00 9.25  ? 70  LEU D CG  1 
ATOM   6998 C  CD1 . LEU D  1 70  ? -5.763  5.830   -46.393 1.00 9.63  ? 70  LEU D CD1 1 
ATOM   6999 C  CD2 . LEU D  1 70  ? -5.757  3.845   -44.794 1.00 11.77 ? 70  LEU D CD2 1 
ATOM   7000 N  N   . ASN D  1 71  ? -4.759  8.749   -43.922 1.00 9.47  ? 71  ASN D N   1 
ATOM   7001 C  CA  . ASN D  1 71  ? -5.461  9.460   -42.851 1.00 9.31  ? 71  ASN D CA  1 
ATOM   7002 C  C   . ASN D  1 71  ? -6.579  8.621   -42.248 1.00 9.83  ? 71  ASN D C   1 
ATOM   7003 O  O   . ASN D  1 71  ? -7.288  7.880   -42.970 1.00 11.47 ? 71  ASN D O   1 
ATOM   7004 C  CB  . ASN D  1 71  ? -6.067  10.764  -43.378 1.00 11.37 ? 71  ASN D CB  1 
ATOM   7005 C  CG  . ASN D  1 71  ? -5.033  11.834  -43.542 1.00 13.27 ? 71  ASN D CG  1 
ATOM   7006 O  OD1 . ASN D  1 71  ? -3.867  11.668  -43.273 1.00 18.80 ? 71  ASN D OD1 1 
ATOM   7007 N  ND2 . ASN D  1 71  ? -5.487  12.993  -44.089 1.00 17.72 ? 71  ASN D ND2 1 
ATOM   7008 N  N   . LEU D  1 72  ? -6.729  8.734   -40.949 1.00 8.51  ? 72  LEU D N   1 
ATOM   7009 C  CA  . LEU D  1 72  ? -7.714  7.955   -40.228 1.00 9.73  ? 72  LEU D CA  1 
ATOM   7010 C  C   . LEU D  1 72  ? -8.644  8.890   -39.387 1.00 10.40 ? 72  LEU D C   1 
ATOM   7011 O  O   . LEU D  1 72  ? -8.245  10.000  -39.036 1.00 11.68 ? 72  LEU D O   1 
ATOM   7012 C  CB  . LEU D  1 72  ? -6.984  7.019   -39.220 1.00 10.50 ? 72  LEU D CB  1 
ATOM   7013 C  CG  . LEU D  1 72  ? -6.111  5.963   -39.948 1.00 9.95  ? 72  LEU D CG  1 
ATOM   7014 C  CD1 . LEU D  1 72  ? -5.245  5.269   -38.881 1.00 9.83  ? 72  LEU D CD1 1 
ATOM   7015 C  CD2 . LEU D  1 72  ? -6.931  4.954   -40.724 1.00 10.85 ? 72  LEU D CD2 1 
ATOM   7016 N  N   . PRO D  1 73  ? -9.865  8.462   -39.152 1.00 10.59 ? 73  PRO D N   1 
ATOM   7017 C  CA  . PRO D  1 73  ? -10.881 9.304   -38.455 1.00 12.17 ? 73  PRO D CA  1 
ATOM   7018 C  C   . PRO D  1 73  ? -10.705 9.271   -36.940 1.00 13.15 ? 73  PRO D C   1 
ATOM   7019 O  O   . PRO D  1 73  ? -10.266 8.249   -36.345 1.00 12.91 ? 73  PRO D O   1 
ATOM   7020 C  CB  . PRO D  1 73  ? -12.164 8.677   -38.925 1.00 11.30 ? 73  PRO D CB  1 
ATOM   7021 C  CG  . PRO D  1 73  ? -11.821 7.165   -38.933 1.00 13.19 ? 73  PRO D CG  1 
ATOM   7022 C  CD  . PRO D  1 73  ? -10.465 7.191   -39.675 1.00 11.05 ? 73  PRO D CD  1 
ATOM   7023 N  N   . SER D  1 74  ? -11.018 10.388  -36.266 1.00 15.20 ? 74  SER D N   1 
ATOM   7024 C  CA  . SER D  1 74  ? -10.717 10.467  -34.840 1.00 15.31 ? 74  SER D CA  1 
ATOM   7025 C  C   . SER D  1 74  ? -11.695 9.655   -33.999 1.00 14.37 ? 74  SER D C   1 
ATOM   7026 O  O   . SER D  1 74  ? -11.426 9.473   -32.804 1.00 17.37 ? 74  SER D O   1 
ATOM   7027 C  CB  . SER D  1 74  ? -10.632 11.938  -34.387 1.00 18.79 ? 74  SER D CB  1 
ATOM   7028 O  OG  . SER D  1 74  ? -11.900 12.543  -34.678 1.00 20.01 ? 74  SER D OG  1 
ATOM   7029 N  N   . ASP D  1 75  ? -12.746 9.154   -34.609 1.00 14.72 ? 75  ASP D N   1 
ATOM   7030 C  CA  . ASP D  1 75  ? -13.622 8.243   -33.908 1.00 17.40 ? 75  ASP D CA  1 
ATOM   7031 C  C   . ASP D  1 75  ? -13.005 6.864   -33.683 1.00 18.00 ? 75  ASP D C   1 
ATOM   7032 O  O   . ASP D  1 75  ? -13.456 6.100   -32.820 1.00 18.32 ? 75  ASP D O   1 
ATOM   7033 C  CB  . ASP D  1 75  ? -15.041 8.226   -34.539 1.00 23.13 ? 75  ASP D CB  1 
ATOM   7034 C  CG  . ASP D  1 75  ? -15.199 7.251   -35.659 1.00 36.12 ? 75  ASP D CG  1 
ATOM   7035 O  OD1 . ASP D  1 75  ? -14.846 7.519   -36.859 1.00 41.04 ? 75  ASP D OD1 1 
ATOM   7036 O  OD2 . ASP D  1 75  ? -15.785 6.174   -35.333 1.00 50.82 ? 75  ASP D OD2 1 
ATOM   7037 N  N   . MET D  1 76  ? -11.971 6.554   -34.450 1.00 13.09 ? 76  MET D N   1 
ATOM   7038 C  CA  . MET D  1 76  ? -11.248 5.311   -34.279 1.00 13.52 ? 76  MET D CA  1 
ATOM   7039 C  C   . MET D  1 76  ? -10.291 5.560   -33.094 1.00 12.04 ? 76  MET D C   1 
ATOM   7040 O  O   . MET D  1 76  ? -9.607  6.560   -32.975 1.00 12.54 ? 76  MET D O   1 
ATOM   7041 C  CB  . MET D  1 76  ? -10.544 5.036   -35.624 1.00 15.80 ? 76  MET D CB  1 
ATOM   7042 C  CG  . MET D  1 76  ? -9.532  3.979   -35.578 1.00 16.89 ? 76  MET D CG  1 
ATOM   7043 S  SD  . MET D  1 76  ? -8.932  3.812   -37.301 1.00 14.32 ? 76  MET D SD  1 
ATOM   7044 C  CE  . MET D  1 76  ? -7.494  2.790   -36.923 1.00 13.95 ? 76  MET D CE  1 
ATOM   7045 N  N   . HIS D  1 77  ? -10.308 4.653   -32.119 1.00 11.48 ? 77  HIS D N   1 
ATOM   7046 C  CA  . HIS D  1 77  ? -9.488  4.883   -30.917 1.00 12.17 ? 77  HIS D CA  1 
ATOM   7047 C  C   . HIS D  1 77  ? -9.007  3.669   -30.241 1.00 12.41 ? 77  HIS D C   1 
ATOM   7048 O  O   . HIS D  1 77  ? -9.567  2.622   -30.480 1.00 12.83 ? 77  HIS D O   1 
ATOM   7049 C  CB  . HIS D  1 77  ? -10.205 5.885   -29.947 1.00 17.10 ? 77  HIS D CB  1 
ATOM   7050 C  CG  . HIS D  1 77  ? -11.460 5.391   -29.328 1.00 19.82 ? 77  HIS D CG  1 
ATOM   7051 N  ND1 . HIS D  1 77  ? -12.659 5.406   -29.977 1.00 22.61 ? 77  HIS D ND1 1 
ATOM   7052 C  CD2 . HIS D  1 77  ? -11.694 4.847   -28.038 1.00 24.08 ? 77  HIS D CD2 1 
ATOM   7053 C  CE1 . HIS D  1 77  ? -13.638 4.840   -29.137 1.00 22.59 ? 77  HIS D CE1 1 
ATOM   7054 N  NE2 . HIS D  1 77  ? -13.033 4.513   -27.963 1.00 25.15 ? 77  HIS D NE2 1 
ATOM   7055 N  N   . ILE D  1 78  ? -7.995  3.810   -29.411 1.00 11.86 ? 78  ILE D N   1 
ATOM   7056 C  CA  . ILE D  1 78  ? -7.571  2.746   -28.494 1.00 13.98 ? 78  ILE D CA  1 
ATOM   7057 C  C   . ILE D  1 78  ? -8.123  3.011   -27.087 1.00 16.16 ? 78  ILE D C   1 
ATOM   7058 O  O   . ILE D  1 78  ? -7.924  4.145   -26.513 1.00 16.91 ? 78  ILE D O   1 
ATOM   7059 C  CB  . ILE D  1 78  ? -6.058  2.645   -28.377 1.00 15.25 ? 78  ILE D CB  1 
ATOM   7060 C  CG1 . ILE D  1 78  ? -5.293  2.351   -29.704 1.00 16.89 ? 78  ILE D CG1 1 
ATOM   7061 C  CG2 . ILE D  1 78  ? -5.654  1.624   -27.319 1.00 20.18 ? 78  ILE D CG2 1 
ATOM   7062 C  CD1 . ILE D  1 78  ? -3.860  2.916   -29.530 1.00 16.92 ? 78  ILE D CD1 1 
ATOM   7063 N  N   . GLN D  1 79  ? -8.470  1.915   -26.458 1.00 17.40 ? 79  GLN D N   1 
ATOM   7064 C  CA  . GLN D  1 79  ? -8.839  1.874   -25.051 1.00 21.73 ? 79  GLN D CA  1 
ATOM   7065 C  C   . GLN D  1 79  ? -7.907  0.992   -24.250 1.00 21.53 ? 79  GLN D C   1 
ATOM   7066 O  O   . GLN D  1 79  ? -7.473  -0.099  -24.740 1.00 22.80 ? 79  GLN D O   1 
ATOM   7067 C  CB  . GLN D  1 79  ? -10.252 1.302   -24.987 1.00 23.33 ? 79  GLN D CB  1 
ATOM   7068 C  CG  . GLN D  1 79  ? -11.299 2.401   -25.233 1.00 31.51 ? 79  GLN D CG  1 
ATOM   7069 C  CD  . GLN D  1 79  ? -11.157 3.619   -24.266 1.00 36.60 ? 79  GLN D CD  1 
ATOM   7070 O  OE1 . GLN D  1 79  ? -10.970 3.457   -23.055 1.00 47.78 ? 79  GLN D OE1 1 
ATOM   7071 N  NE2 . GLN D  1 79  ? -11.237 4.834   -24.812 1.00 37.62 ? 79  GLN D NE2 1 
ATOM   7072 N  N   . GLY D  1 80  ? -7.556  1.389   -23.033 1.00 20.14 ? 80  GLY D N   1 
ATOM   7073 C  CA  . GLY D  1 80  ? -6.635  0.567   -22.278 1.00 19.38 ? 80  GLY D CA  1 
ATOM   7074 C  C   . GLY D  1 80  ? -5.482  1.304   -21.696 1.00 20.75 ? 80  GLY D C   1 
ATOM   7075 O  O   . GLY D  1 80  ? -4.888  0.852   -20.768 1.00 24.34 ? 80  GLY D O   1 
ATOM   7076 N  N   . LEU D  1 81  ? -5.106  2.461   -22.292 1.00 16.24 ? 81  LEU D N   1 
ATOM   7077 C  CA  . LEU D  1 81  ? -3.946  3.162   -21.854 1.00 17.28 ? 81  LEU D CA  1 
ATOM   7078 C  C   . LEU D  1 81  ? -4.384  4.156   -20.748 1.00 13.91 ? 81  LEU D C   1 
ATOM   7079 O  O   . LEU D  1 81  ? -5.582  4.143   -20.402 1.00 17.15 ? 81  LEU D O   1 
ATOM   7080 C  CB  . LEU D  1 81  ? -3.313  3.902   -23.036 1.00 15.83 ? 81  LEU D CB  1 
ATOM   7081 C  CG  . LEU D  1 81  ? -2.922  2.941   -24.184 1.00 16.52 ? 81  LEU D CG  1 
ATOM   7082 C  CD1 . LEU D  1 81  ? -2.516  3.818   -25.406 1.00 19.06 ? 81  LEU D CD1 1 
ATOM   7083 C  CD2 . LEU D  1 81  ? -1.710  2.138   -23.664 1.00 16.12 ? 81  LEU D CD2 1 
ATOM   7084 N  N   . GLN D  1 82  ? -3.494  5.019   -20.271 1.00 14.50 ? 82  GLN D N   1 
ATOM   7085 C  CA  . GLN D  1 82  ? -3.845  5.946   -19.175 1.00 14.15 ? 82  GLN D CA  1 
ATOM   7086 C  C   . GLN D  1 82  ? -4.853  7.029   -19.641 1.00 14.23 ? 82  GLN D C   1 
ATOM   7087 O  O   . GLN D  1 82  ? -5.404  7.701   -18.829 1.00 16.45 ? 82  GLN D O   1 
ATOM   7088 C  CB  . GLN D  1 82  ? -2.566  6.591   -18.572 1.00 14.38 ? 82  GLN D CB  1 
ATOM   7089 C  CG  . GLN D  1 82  ? -2.160  7.929   -19.204 1.00 18.48 ? 82  GLN D CG  1 
ATOM   7090 C  CD  . GLN D  1 82  ? -1.663  7.803   -20.661 1.00 18.90 ? 82  GLN D CD  1 
ATOM   7091 O  OE1 . GLN D  1 82  ? -1.328  6.711   -21.158 1.00 21.26 ? 82  GLN D OE1 1 
ATOM   7092 N  NE2 . GLN D  1 82  ? -1.493  8.949   -21.306 1.00 20.01 ? 82  GLN D NE2 1 
ATOM   7093 N  N   . SER D  1 83  ? -5.046  7.189   -20.951 1.00 13.55 ? 83  SER D N   1 
ATOM   7094 C  CA  . SER D  1 83  ? -5.957  8.232   -21.558 1.00 12.79 ? 83  SER D CA  1 
ATOM   7095 C  C   . SER D  1 83  ? -6.559  7.627   -22.835 1.00 14.12 ? 83  SER D C   1 
ATOM   7096 O  O   . SER D  1 83  ? -5.898  6.683   -23.399 1.00 13.11 ? 83  SER D O   1 
ATOM   7097 C  CB  . SER D  1 83  ? -5.170  9.473   -21.978 1.00 12.37 ? 83  SER D CB  1 
ATOM   7098 O  OG  . SER D  1 83  ? -4.578  10.137  -20.858 1.00 13.38 ? 83  SER D OG  1 
ATOM   7099 N  N   . ARG D  1 84  ? -7.646  8.122   -23.393 1.00 11.71 ? 84  ARG D N   1 
ATOM   7100 C  CA  . ARG D  1 84  ? -8.094  7.727   -24.732 1.00 13.48 ? 84  ARG D CA  1 
ATOM   7101 C  C   . ARG D  1 84  ? -7.101  8.363   -25.760 1.00 12.23 ? 84  ARG D C   1 
ATOM   7102 O  O   . ARG D  1 84  ? -6.805  9.573   -25.765 1.00 12.74 ? 84  ARG D O   1 
ATOM   7103 C  CB  . ARG D  1 84  ? -9.465  8.325   -25.035 1.00 14.76 ? 84  ARG D CB  1 
ATOM   7104 C  CG  . ARG D  1 84  ? -9.932  8.057   -26.449 1.00 17.92 ? 84  ARG D CG  1 
ATOM   7105 C  CD  . ARG D  1 84  ? -11.411 8.434   -26.706 1.00 19.79 ? 84  ARG D CD  1 
ATOM   7106 N  NE  . ARG D  1 84  ? -11.492 8.557   -28.164 1.00 24.40 ? 84  ARG D NE  1 
ATOM   7107 C  CZ  . ARG D  1 84  ? -12.637 8.479   -28.869 1.00 25.50 ? 84  ARG D CZ  1 
ATOM   7108 N  NH1 . ARG D  1 84  ? -13.826 8.376   -28.210 1.00 29.63 ? 84  ARG D NH1 1 
ATOM   7109 N  NH2 . ARG D  1 84  ? -12.631 8.550   -30.216 1.00 23.25 ? 84  ARG D NH2 1 
ATOM   7110 N  N   . TYR D  1 85  ? -6.634  7.487   -26.647 1.00 11.38 ? 85  TYR D N   1 
ATOM   7111 C  CA  . TYR D  1 85  ? -5.866  7.935   -27.797 1.00 10.55 ? 85  TYR D CA  1 
ATOM   7112 C  C   . TYR D  1 85  ? -6.668  7.647   -29.038 1.00 11.36 ? 85  TYR D C   1 
ATOM   7113 O  O   . TYR D  1 85  ? -7.123  6.528   -29.316 1.00 12.60 ? 85  TYR D O   1 
ATOM   7114 C  CB  . TYR D  1 85  ? -4.544  7.149   -27.774 1.00 9.87  ? 85  TYR D CB  1 
ATOM   7115 C  CG  . TYR D  1 85  ? -3.517  7.684   -26.804 1.00 9.29  ? 85  TYR D CG  1 
ATOM   7116 C  CD1 . TYR D  1 85  ? -3.498  7.228   -25.435 1.00 9.26  ? 85  TYR D CD1 1 
ATOM   7117 C  CD2 . TYR D  1 85  ? -2.542  8.589   -27.192 1.00 9.76  ? 85  TYR D CD2 1 
ATOM   7118 C  CE1 . TYR D  1 85  ? -2.575  7.658   -24.541 1.00 9.97  ? 85  TYR D CE1 1 
ATOM   7119 C  CE2 . TYR D  1 85  ? -1.627  9.091   -26.275 1.00 9.62  ? 85  TYR D CE2 1 
ATOM   7120 C  CZ  . TYR D  1 85  ? -1.649  8.632   -24.941 1.00 10.84 ? 85  TYR D CZ  1 
ATOM   7121 O  OH  . TYR D  1 85  ? -0.719  9.066   -24.010 1.00 11.04 ? 85  TYR D OH  1 
ATOM   7122 N  N   . SER D  1 86  ? -6.818  8.703   -29.844 1.00 10.61 ? 86  SER D N   1 
ATOM   7123 C  CA  . SER D  1 86  ? -7.623  8.634   -31.039 1.00 10.51 ? 86  SER D CA  1 
ATOM   7124 C  C   . SER D  1 86  ? -6.675  8.572   -32.302 1.00 9.34  ? 86  SER D C   1 
ATOM   7125 O  O   . SER D  1 86  ? -5.622  9.214   -32.340 1.00 10.30 ? 86  SER D O   1 
ATOM   7126 C  CB  . SER D  1 86  ? -8.478  9.932   -31.208 1.00 11.27 ? 86  SER D CB  1 
ATOM   7127 O  OG  . SER D  1 86  ? -9.421  9.937   -30.090 1.00 13.40 ? 86  SER D OG  1 
ATOM   7128 N  N   . ALA D  1 87  ? -7.141  7.816   -33.261 1.00 9.39  ? 87  ALA D N   1 
ATOM   7129 C  CA  . ALA D  1 87  ? -6.283  7.652   -34.484 1.00 10.18 ? 87  ALA D CA  1 
ATOM   7130 C  C   . ALA D  1 87  ? -6.137  8.935   -35.252 1.00 10.71 ? 87  ALA D C   1 
ATOM   7131 O  O   . ALA D  1 87  ? -7.093  9.767   -35.326 1.00 12.12 ? 87  ALA D O   1 
ATOM   7132 C  CB  . ALA D  1 87  ? -6.870  6.593   -35.334 1.00 10.99 ? 87  ALA D CB  1 
ATOM   7133 N  N   . THR D  1 88  ? -4.985  9.081   -35.940 1.00 10.48 ? 88  THR D N   1 
ATOM   7134 C  CA  . THR D  1 88  ? -4.759  10.167  -36.868 1.00 8.95  ? 88  THR D CA  1 
ATOM   7135 C  C   . THR D  1 88  ? -4.289  9.696   -38.249 1.00 9.22  ? 88  THR D C   1 
ATOM   7136 O  O   . THR D  1 88  ? -4.775  10.157  -39.247 1.00 10.06 ? 88  THR D O   1 
ATOM   7137 C  CB  . THR D  1 88  ? -3.894  11.252  -36.259 1.00 11.35 ? 88  THR D CB  1 
ATOM   7138 O  OG1 . THR D  1 88  ? -3.797  12.336  -37.203 1.00 14.10 ? 88  THR D OG1 1 
ATOM   7139 C  CG2 . THR D  1 88  ? -2.478  10.787  -35.820 1.00 12.34 ? 88  THR D CG2 1 
ATOM   7140 N  N   . GLN D  1 89  ? -3.374  8.711   -38.279 1.00 9.06  ? 89  GLN D N   1 
ATOM   7141 C  CA  . GLN D  1 89  ? -2.902  8.252   -39.584 1.00 8.48  ? 89  GLN D CA  1 
ATOM   7142 C  C   . GLN D  1 89  ? -2.117  6.966   -39.356 1.00 6.91  ? 89  GLN D C   1 
ATOM   7143 O  O   . GLN D  1 89  ? -1.681  6.674   -38.255 1.00 8.26  ? 89  GLN D O   1 
ATOM   7144 C  CB  . GLN D  1 89  ? -1.943  9.298   -40.283 1.00 8.90  ? 89  GLN D CB  1 
ATOM   7145 C  CG  . GLN D  1 89  ? -0.807  9.785   -39.413 1.00 11.97 ? 89  GLN D CG  1 
ATOM   7146 C  CD  . GLN D  1 89  ? 0.508   9.255   -39.842 1.00 12.13 ? 89  GLN D CD  1 
ATOM   7147 O  OE1 . GLN D  1 89  ? 0.617   8.109   -40.202 1.00 12.53 ? 89  GLN D OE1 1 
ATOM   7148 N  NE2 . GLN D  1 89  ? 1.499   10.101  -39.843 1.00 17.42 ? 89  GLN D NE2 1 
ATOM   7149 N  N   . LEU D  1 90  ? -1.998  6.177   -40.452 1.00 7.32  ? 90  LEU D N   1 
ATOM   7150 C  CA  . LEU D  1 90  ? -1.012  5.090   -40.478 1.00 6.98  ? 90  LEU D CA  1 
ATOM   7151 C  C   . LEU D  1 90  ? -0.017  5.286   -41.659 1.00 6.20  ? 90  LEU D C   1 
ATOM   7152 O  O   . LEU D  1 90  ? -0.332  5.942   -42.603 1.00 7.70  ? 90  LEU D O   1 
ATOM   7153 C  CB  . LEU D  1 90  ? -1.698  3.766   -40.476 1.00 6.71  ? 90  LEU D CB  1 
ATOM   7154 C  CG  . LEU D  1 90  ? -2.628  3.367   -41.604 1.00 6.48  ? 90  LEU D CG  1 
ATOM   7155 C  CD1 . LEU D  1 90  ? -1.928  3.053   -42.946 1.00 7.90  ? 90  LEU D CD1 1 
ATOM   7156 C  CD2 . LEU D  1 90  ? -3.524  2.203   -41.173 1.00 8.02  ? 90  LEU D CD2 1 
ATOM   7157 N  N   . HIS D  1 91  ? 1.158   4.695   -41.487 1.00 6.69  ? 91  HIS D N   1 
ATOM   7158 C  CA  . HIS D  1 91  ? 2.152   4.762   -42.548 1.00 6.80  ? 91  HIS D CA  1 
ATOM   7159 C  C   . HIS D  1 91  ? 3.094   3.598   -42.334 1.00 6.83  ? 91  HIS D C   1 
ATOM   7160 O  O   . HIS D  1 91  ? 3.006   2.865   -41.379 1.00 6.84  ? 91  HIS D O   1 
ATOM   7161 C  CB  . HIS D  1 91  ? 2.883   6.130   -42.500 1.00 7.22  ? 91  HIS D CB  1 
ATOM   7162 C  CG  . HIS D  1 91  ? 3.629   6.347   -41.198 1.00 6.24  ? 91  HIS D CG  1 
ATOM   7163 N  ND1 . HIS D  1 91  ? 3.067   6.902   -40.089 1.00 7.45  ? 91  HIS D ND1 1 
ATOM   7164 C  CD2 . HIS D  1 91  ? 4.884   5.833   -40.781 1.00 7.63  ? 91  HIS D CD2 1 
ATOM   7165 C  CE1 . HIS D  1 91  ? 3.948   6.863   -39.062 1.00 5.96  ? 91  HIS D CE1 1 
ATOM   7166 N  NE2 . HIS D  1 91  ? 5.077   6.148   -39.477 1.00 6.14  ? 91  HIS D NE2 1 
ATOM   7167 N  N   . LEU D  1 92  ? 4.052   3.503   -43.262 1.00 7.22  ? 92  LEU D N   1 
ATOM   7168 C  CA  . LEU D  1 92  ? 4.997   2.371   -43.274 1.00 7.19  ? 92  LEU D CA  1 
ATOM   7169 C  C   . LEU D  1 92  ? 6.460   2.856   -43.385 1.00 6.59  ? 92  LEU D C   1 
ATOM   7170 O  O   . LEU D  1 92  ? 6.784   3.945   -43.768 1.00 7.59  ? 92  LEU D O   1 
ATOM   7171 C  CB  . LEU D  1 92  ? 4.677   1.440   -44.418 1.00 8.97  ? 92  LEU D CB  1 
ATOM   7172 C  CG  . LEU D  1 92  ? 3.282   0.744   -44.262 1.00 9.60  ? 92  LEU D CG  1 
ATOM   7173 C  CD1 . LEU D  1 92  ? 2.348   1.397   -45.243 1.00 14.31 ? 92  LEU D CD1 1 
ATOM   7174 C  CD2 . LEU D  1 92  ? 3.397   -0.733  -44.483 1.00 12.33 ? 92  LEU D CD2 1 
ATOM   7175 N  N   . HIS D  1 93  ? 7.310   1.902   -43.040 1.00 7.51  ? 93  HIS D N   1 
ATOM   7176 C  CA  . HIS D  1 93  ? 8.820   2.074   -43.249 1.00 6.96  ? 93  HIS D CA  1 
ATOM   7177 C  C   . HIS D  1 93  ? 9.321   0.828   -43.835 1.00 7.23  ? 93  HIS D C   1 
ATOM   7178 O  O   . HIS D  1 93  ? 8.837   -0.274  -43.527 1.00 7.15  ? 93  HIS D O   1 
ATOM   7179 C  CB  . HIS D  1 93  ? 9.498   2.233   -41.874 1.00 6.69  ? 93  HIS D CB  1 
ATOM   7180 C  CG  . HIS D  1 93  ? 9.009   3.414   -41.095 1.00 6.83  ? 93  HIS D CG  1 
ATOM   7181 N  ND1 . HIS D  1 93  ? 9.597   4.658   -41.187 1.00 7.74  ? 93  HIS D ND1 1 
ATOM   7182 C  CD2 . HIS D  1 93  ? 7.913   3.589   -40.224 1.00 6.90  ? 93  HIS D CD2 1 
ATOM   7183 C  CE1 . HIS D  1 93  ? 8.946   5.554   -40.392 1.00 8.11  ? 93  HIS D CE1 1 
ATOM   7184 N  NE2 . HIS D  1 93  ? 7.929   4.925   -39.773 1.00 6.59  ? 93  HIS D NE2 1 
ATOM   7185 N  N   . TRP D  1 94  ? 10.256  0.935   -44.759 1.00 6.25  ? 94  TRP D N   1 
ATOM   7186 C  CA  . TRP D  1 94  ? 10.724  -0.259  -45.578 1.00 6.44  ? 94  TRP D CA  1 
ATOM   7187 C  C   . TRP D  1 94  ? 12.162  -0.007  -46.052 1.00 6.09  ? 94  TRP D C   1 
ATOM   7188 O  O   . TRP D  1 94  ? 12.787  1.026   -45.834 1.00 7.25  ? 94  TRP D O   1 
ATOM   7189 C  CB  . TRP D  1 94  ? 9.742   -0.539  -46.711 1.00 7.24  ? 94  TRP D CB  1 
ATOM   7190 C  CG  . TRP D  1 94  ? 9.653   0.610   -47.708 1.00 7.15  ? 94  TRP D CG  1 
ATOM   7191 C  CD1 . TRP D  1 94  ? 10.472  0.908   -48.814 1.00 7.18  ? 94  TRP D CD1 1 
ATOM   7192 C  CD2 . TRP D  1 94  ? 8.649   1.688   -47.622 1.00 6.72  ? 94  TRP D CD2 1 
ATOM   7193 N  NE1 . TRP D  1 94  ? 10.030  2.055   -49.452 1.00 7.16  ? 94  TRP D NE1 1 
ATOM   7194 C  CE2 . TRP D  1 94  ? 8.883   2.552   -48.772 1.00 6.72  ? 94  TRP D CE2 1 
ATOM   7195 C  CE3 . TRP D  1 94  ? 7.554   1.967   -46.808 1.00 7.53  ? 94  TRP D CE3 1 
ATOM   7196 C  CZ2 . TRP D  1 94  ? 8.065   3.695   -49.043 1.00 6.73  ? 94  TRP D CZ2 1 
ATOM   7197 C  CZ3 . TRP D  1 94  ? 6.773   3.110   -47.078 1.00 6.78  ? 94  TRP D CZ3 1 
ATOM   7198 C  CH2 . TRP D  1 94  ? 7.036   3.987   -48.138 1.00 7.45  ? 94  TRP D CH2 1 
ATOM   7199 N  N   . GLY D  1 95  ? 12.663  -1.099  -46.653 1.00 6.70  ? 95  GLY D N   1 
ATOM   7200 C  CA  . GLY D  1 95  ? 14.072  -1.152  -47.146 1.00 8.62  ? 95  GLY D CA  1 
ATOM   7201 C  C   . GLY D  1 95  ? 14.149  -0.867  -48.637 1.00 7.92  ? 95  GLY D C   1 
ATOM   7202 O  O   . GLY D  1 95  ? 13.624  0.124   -49.184 1.00 7.82  ? 95  GLY D O   1 
ATOM   7203 N  N   . ASN D  1 96  ? 14.720  -1.864  -49.385 1.00 8.60  ? 96  ASN D N   1 
ATOM   7204 C  CA  . ASN D  1 96  ? 14.807  -1.613  -50.855 1.00 11.05 ? 96  ASN D CA  1 
ATOM   7205 C  C   . ASN D  1 96  ? 14.902  -2.995  -51.482 1.00 11.79 ? 96  ASN D C   1 
ATOM   7206 O  O   . ASN D  1 96  ? 15.061  -3.982  -50.763 1.00 11.21 ? 96  ASN D O   1 
ATOM   7207 C  CB  . ASN D  1 96  ? 16.054  -0.735  -51.186 1.00 12.09 ? 96  ASN D CB  1 
ATOM   7208 C  CG  . ASN D  1 96  ? 17.356  -1.448  -50.923 1.00 12.77 ? 96  ASN D CG  1 
ATOM   7209 O  OD1 . ASN D  1 96  ? 17.763  -2.213  -51.783 1.00 19.66 ? 96  ASN D OD1 1 
ATOM   7210 N  ND2 . ASN D  1 96  ? 17.973  -1.288  -49.792 1.00 13.02 ? 96  ASN D ND2 1 
ATOM   7211 N  N   . PRO D  1 97  ? 14.799  -3.062  -52.834 1.00 12.91 ? 97  PRO D N   1 
ATOM   7212 C  CA  . PRO D  1 97  ? 14.761  -4.379  -53.441 1.00 15.57 ? 97  PRO D CA  1 
ATOM   7213 C  C   . PRO D  1 97  ? 15.994  -5.241  -53.129 1.00 17.30 ? 97  PRO D C   1 
ATOM   7214 O  O   . PRO D  1 97  ? 15.843  -6.454  -52.972 1.00 24.30 ? 97  PRO D O   1 
ATOM   7215 C  CB  . PRO D  1 97  ? 14.565  -4.066  -54.924 1.00 16.51 ? 97  PRO D CB  1 
ATOM   7216 C  CG  . PRO D  1 97  ? 13.976  -2.712  -54.993 1.00 17.12 ? 97  PRO D CG  1 
ATOM   7217 C  CD  . PRO D  1 97  ? 14.579  -2.010  -53.786 1.00 14.05 ? 97  PRO D CD  1 
ATOM   7218 N  N   . ASN D  1 98  ? 17.150  -4.630  -52.933 1.00 16.83 ? 98  ASN D N   1 
ATOM   7219 C  CA  . ASN D  1 98  ? 18.371  -5.379  -52.673 1.00 22.49 ? 98  ASN D CA  1 
ATOM   7220 C  C   . ASN D  1 98  ? 18.579  -5.653  -51.180 1.00 23.18 ? 98  ASN D C   1 
ATOM   7221 O  O   . ASN D  1 98  ? 19.567  -6.285  -50.755 1.00 22.87 ? 98  ASN D O   1 
ATOM   7222 C  CB  . ASN D  1 98  ? 19.591  -4.636  -53.252 1.00 24.80 ? 98  ASN D CB  1 
ATOM   7223 C  CG  . ASN D  1 98  ? 19.485  -4.385  -54.767 1.00 33.57 ? 98  ASN D CG  1 
ATOM   7224 O  OD1 . ASN D  1 98  ? 18.961  -5.207  -55.541 1.00 39.20 ? 98  ASN D OD1 1 
ATOM   7225 N  ND2 . ASN D  1 98  ? 19.976  -3.207  -55.189 1.00 40.59 ? 98  ASN D ND2 1 
ATOM   7226 N  N   . ASP D  1 99  ? 17.734  -5.086  -50.322 1.00 15.32 ? 99  ASP D N   1 
ATOM   7227 C  CA  . ASP D  1 99  ? 17.909  -5.366  -48.899 1.00 14.24 ? 99  ASP D CA  1 
ATOM   7228 C  C   . ASP D  1 99  ? 16.491  -5.154  -48.300 1.00 11.52 ? 99  ASP D C   1 
ATOM   7229 O  O   . ASP D  1 99  ? 16.188  -4.060  -47.764 1.00 11.06 ? 99  ASP D O   1 
ATOM   7230 C  CB  . ASP D  1 99  ? 18.914  -4.356  -48.260 1.00 16.02 ? 99  ASP D CB  1 
ATOM   7231 C  CG  . ASP D  1 99  ? 19.073  -4.566  -46.742 1.00 19.06 ? 99  ASP D CG  1 
ATOM   7232 O  OD1 . ASP D  1 99  ? 18.690  -5.667  -46.311 1.00 18.55 ? 99  ASP D OD1 1 
ATOM   7233 O  OD2 . ASP D  1 99  ? 19.504  -3.643  -45.982 1.00 25.92 ? 99  ASP D OD2 1 
ATOM   7234 N  N   . PRO D  1 100 ? 15.597  -6.111  -48.412 1.00 12.81 ? 100 PRO D N   1 
ATOM   7235 C  CA  . PRO D  1 100 ? 14.195  -5.967  -47.935 1.00 11.33 ? 100 PRO D CA  1 
ATOM   7236 C  C   . PRO D  1 100 ? 14.151  -6.221  -46.431 1.00 10.19 ? 100 PRO D C   1 
ATOM   7237 O  O   . PRO D  1 100 ? 13.539  -7.136  -45.934 1.00 11.36 ? 100 PRO D O   1 
ATOM   7238 C  CB  . PRO D  1 100 ? 13.402  -7.025  -48.739 1.00 13.44 ? 100 PRO D CB  1 
ATOM   7239 C  CG  . PRO D  1 100 ? 14.457  -8.053  -49.010 1.00 12.78 ? 100 PRO D CG  1 
ATOM   7240 C  CD  . PRO D  1 100 ? 15.817  -7.409  -49.091 1.00 13.36 ? 100 PRO D CD  1 
ATOM   7241 N  N   . HIS D  1 101 ? 14.838  -5.371  -45.691 1.00 10.47 ? 101 HIS D N   1 
ATOM   7242 C  CA  . HIS D  1 101 ? 14.990  -5.492  -44.208 1.00 10.60 ? 101 HIS D CA  1 
ATOM   7243 C  C   . HIS D  1 101 ? 14.947  -4.130  -43.562 1.00 10.85 ? 101 HIS D C   1 
ATOM   7244 O  O   . HIS D  1 101 ? 15.911  -3.683  -42.905 1.00 13.70 ? 101 HIS D O   1 
ATOM   7245 C  CB  . HIS D  1 101 ? 16.301  -6.278  -43.809 1.00 13.11 ? 101 HIS D CB  1 
ATOM   7246 C  CG  . HIS D  1 101 ? 16.366  -7.655  -44.472 1.00 13.22 ? 101 HIS D CG  1 
ATOM   7247 N  ND1 . HIS D  1 101 ? 15.737  -8.757  -43.997 1.00 17.80 ? 101 HIS D ND1 1 
ATOM   7248 C  CD2 . HIS D  1 101 ? 16.972  -8.033  -45.645 1.00 13.69 ? 101 HIS D CD2 1 
ATOM   7249 C  CE1 . HIS D  1 101 ? 15.928  -9.789  -44.847 1.00 16.96 ? 101 HIS D CE1 1 
ATOM   7250 N  NE2 . HIS D  1 101 ? 16.674  -9.362  -45.849 1.00 19.56 ? 101 HIS D NE2 1 
ATOM   7251 N  N   . GLY D  1 102 ? 13.819  -3.465  -43.734 1.00 8.65  ? 102 GLY D N   1 
ATOM   7252 C  CA  . GLY D  1 102 ? 13.653  -2.074  -43.368 1.00 8.75  ? 102 GLY D CA  1 
ATOM   7253 C  C   . GLY D  1 102 ? 12.685  -1.810  -42.239 1.00 8.02  ? 102 GLY D C   1 
ATOM   7254 O  O   . GLY D  1 102 ? 12.188  -0.720  -42.105 1.00 9.06  ? 102 GLY D O   1 
ATOM   7255 N  N   . SER D  1 103 ? 12.437  -2.784  -41.358 1.00 8.26  ? 103 SER D N   1 
ATOM   7256 C  CA  . SER D  1 103 ? 11.664  -2.414  -40.159 1.00 7.53  ? 103 SER D CA  1 
ATOM   7257 C  C   . SER D  1 103 ? 12.518  -1.424  -39.321 1.00 7.33  ? 103 SER D C   1 
ATOM   7258 O  O   . SER D  1 103 ? 13.774  -1.385  -39.439 1.00 8.26  ? 103 SER D O   1 
ATOM   7259 C  CB  . SER D  1 103 ? 11.348  -3.636  -39.279 1.00 7.61  ? 103 SER D CB  1 
ATOM   7260 O  OG  . SER D  1 103 ? 12.509  -4.229  -38.711 1.00 8.38  ? 103 SER D OG  1 
ATOM   7261 N  N   . GLU D  1 104 ? 11.838  -0.636  -38.453 1.00 6.70  ? 104 GLU D N   1 
ATOM   7262 C  CA  . GLU D  1 104 ? 12.537  0.255   -37.566 1.00 7.02  ? 104 GLU D CA  1 
ATOM   7263 C  C   . GLU D  1 104 ? 12.958  -0.451  -36.315 1.00 6.86  ? 104 GLU D C   1 
ATOM   7264 O  O   . GLU D  1 104 ? 14.120  -0.456  -35.941 1.00 8.18  ? 104 GLU D O   1 
ATOM   7265 C  CB  . GLU D  1 104 ? 11.625  1.450   -37.265 1.00 7.07  ? 104 GLU D CB  1 
ATOM   7266 C  CG  . GLU D  1 104 ? 11.220  2.175   -38.555 1.00 7.44  ? 104 GLU D CG  1 
ATOM   7267 C  CD  . GLU D  1 104 ? 11.141  3.673   -38.289 1.00 7.87  ? 104 GLU D CD  1 
ATOM   7268 O  OE1 . GLU D  1 104 ? 10.179  4.108   -37.669 1.00 7.78  ? 104 GLU D OE1 1 
ATOM   7269 O  OE2 . GLU D  1 104 ? 12.093  4.396   -38.655 1.00 8.27  ? 104 GLU D OE2 1 
ATOM   7270 N  N   . HIS D  1 105 ? 12.007  -1.030  -35.564 1.00 6.64  ? 105 HIS D N   1 
ATOM   7271 C  CA  . HIS D  1 105 ? 12.340  -1.900  -34.433 1.00 7.61  ? 105 HIS D CA  1 
ATOM   7272 C  C   . HIS D  1 105 ? 12.945  -3.138  -34.974 1.00 7.54  ? 105 HIS D C   1 
ATOM   7273 O  O   . HIS D  1 105 ? 12.587  -3.692  -36.011 1.00 7.92  ? 105 HIS D O   1 
ATOM   7274 C  CB  . HIS D  1 105 ? 11.047  -2.171  -33.567 1.00 6.73  ? 105 HIS D CB  1 
ATOM   7275 C  CG  . HIS D  1 105 ? 10.565  -0.943  -32.894 1.00 8.06  ? 105 HIS D CG  1 
ATOM   7276 N  ND1 . HIS D  1 105 ? 9.682   -0.103  -33.471 1.00 8.13  ? 105 HIS D ND1 1 
ATOM   7277 C  CD2 . HIS D  1 105 ? 10.908  -0.395  -31.654 1.00 7.79  ? 105 HIS D CD2 1 
ATOM   7278 C  CE1 . HIS D  1 105 ? 9.481   0.962   -32.601 1.00 7.87  ? 105 HIS D CE1 1 
ATOM   7279 N  NE2 . HIS D  1 105 ? 10.236  0.772   -31.531 1.00 8.91  ? 105 HIS D NE2 1 
ATOM   7280 N  N   . THR D  1 106 ? 13.888  -3.654  -34.167 1.00 8.41  ? 106 THR D N   1 
ATOM   7281 C  CA  . THR D  1 106 ? 14.530  -4.970  -34.464 1.00 8.83  ? 106 THR D CA  1 
ATOM   7282 C  C   . THR D  1 106 ? 14.263  -5.910  -33.266 1.00 8.84  ? 106 THR D C   1 
ATOM   7283 O  O   . THR D  1 106 ? 13.960  -5.436  -32.169 1.00 9.09  ? 106 THR D O   1 
ATOM   7284 C  CB  . THR D  1 106 ? 16.060  -4.789  -34.784 1.00 9.51  ? 106 THR D CB  1 
ATOM   7285 O  OG1 . THR D  1 106 ? 16.730  -4.131  -33.631 1.00 10.18 ? 106 THR D OG1 1 
ATOM   7286 C  CG2 . THR D  1 106 ? 16.287  -3.868  -36.015 1.00 10.54 ? 106 THR D CG2 1 
ATOM   7287 N  N   . VAL D  1 107 ? 14.374  -7.212  -33.523 1.00 9.80  ? 107 VAL D N   1 
ATOM   7288 C  CA  . VAL D  1 107 ? 14.133  -8.203  -32.437 1.00 10.68 ? 107 VAL D CA  1 
ATOM   7289 C  C   . VAL D  1 107 ? 15.387  -9.044  -32.453 1.00 11.06 ? 107 VAL D C   1 
ATOM   7290 O  O   . VAL D  1 107 ? 15.801  -9.615  -33.435 1.00 13.49 ? 107 VAL D O   1 
ATOM   7291 C  CB  . VAL D  1 107 ? 12.873  -9.071  -32.711 1.00 9.88  ? 107 VAL D CB  1 
ATOM   7292 C  CG1 . VAL D  1 107 ? 12.749  -10.037 -31.564 1.00 13.98 ? 107 VAL D CG1 1 
ATOM   7293 C  CG2 . VAL D  1 107 ? 11.647  -8.131  -32.636 1.00 12.35 ? 107 VAL D CG2 1 
ATOM   7294 N  N   . SER D  1 108 ? 16.039  -9.001  -31.303 1.00 10.87 ? 108 SER D N   1 
ATOM   7295 C  CA  . SER D  1 108 ? 17.324  -9.756  -31.062 1.00 11.95 ? 108 SER D CA  1 
ATOM   7296 C  C   . SER D  1 108 ? 18.275  -9.446  -32.230 1.00 12.11 ? 108 SER D C   1 
ATOM   7297 O  O   . SER D  1 108 ? 18.909  -10.362 -32.855 1.00 13.41 ? 108 SER D O   1 
ATOM   7298 C  CB  . SER D  1 108 ? 16.998  -11.296 -30.940 1.00 12.45 ? 108 SER D CB  1 
ATOM   7299 O  OG  . SER D  1 108 ? 16.219  -11.511 -29.805 1.00 17.66 ? 108 SER D OG  1 
ATOM   7300 N  N   . GLY D  1 109 ? 18.374  -8.156  -32.556 1.00 11.50 ? 109 GLY D N   1 
ATOM   7301 C  CA  . GLY D  1 109 ? 19.291  -7.689  -33.592 1.00 12.14 ? 109 GLY D CA  1 
ATOM   7302 C  C   . GLY D  1 109 ? 18.848  -7.835  -35.084 1.00 14.00 ? 109 GLY D C   1 
ATOM   7303 O  O   . GLY D  1 109 ? 19.610  -7.441  -35.976 1.00 17.82 ? 109 GLY D O   1 
ATOM   7304 N  N   A GLN D  1 110 ? 17.683  -8.401  -35.330 0.50 12.93 ? 110 GLN D N   1 
ATOM   7305 N  N   B GLN D  1 110 ? 17.684  -8.375  -35.343 0.50 14.21 ? 110 GLN D N   1 
ATOM   7306 C  CA  A GLN D  1 110 ? 17.224  -8.767  -36.680 0.50 12.63 ? 110 GLN D CA  1 
ATOM   7307 C  CA  B GLN D  1 110 ? 17.282  -8.692  -36.705 0.50 14.90 ? 110 GLN D CA  1 
ATOM   7308 C  C   A GLN D  1 110 ? 16.127  -7.767  -37.149 0.50 9.72  ? 110 GLN D C   1 
ATOM   7309 C  C   B GLN D  1 110 ? 16.150  -7.741  -37.142 0.50 10.76 ? 110 GLN D C   1 
ATOM   7310 O  O   A GLN D  1 110 ? 15.143  -7.526  -36.401 0.50 9.41  ? 110 GLN D O   1 
ATOM   7311 O  O   B GLN D  1 110 ? 15.174  -7.518  -36.386 0.50 10.24 ? 110 GLN D O   1 
ATOM   7312 C  CB  A GLN D  1 110 ? 16.620  -10.179 -36.726 0.50 13.31 ? 110 GLN D CB  1 
ATOM   7313 C  CB  B GLN D  1 110 ? 16.757  -10.115 -36.796 0.50 18.10 ? 110 GLN D CB  1 
ATOM   7314 C  CG  A GLN D  1 110 ? 17.560  -11.262 -36.139 0.50 13.17 ? 110 GLN D CG  1 
ATOM   7315 C  CG  B GLN D  1 110 ? 17.575  -11.060 -35.912 0.50 21.95 ? 110 GLN D CG  1 
ATOM   7316 C  CD  A GLN D  1 110 ? 18.964  -11.168 -36.696 0.50 14.40 ? 110 GLN D CD  1 
ATOM   7317 C  CD  B GLN D  1 110 ? 17.287  -12.503 -36.170 0.50 26.20 ? 110 GLN D CD  1 
ATOM   7318 O  OE1 A GLN D  1 110 ? 19.150  -11.359 -37.873 0.50 15.37 ? 110 GLN D OE1 1 
ATOM   7319 O  OE1 B GLN D  1 110 ? 16.406  -13.117 -35.529 0.50 33.43 ? 110 GLN D OE1 1 
ATOM   7320 N  NE2 A GLN D  1 110 ? 19.962  -10.873 -35.811 0.50 13.98 ? 110 GLN D NE2 1 
ATOM   7321 N  NE2 B GLN D  1 110 ? 18.043  -13.073 -37.076 0.50 26.75 ? 110 GLN D NE2 1 
ATOM   7322 N  N   . HIS D  1 111 ? 16.324  -7.169  -38.322 1.00 10.26 ? 111 HIS D N   1 
ATOM   7323 C  CA  . HIS D  1 111 ? 15.213  -6.466  -38.993 1.00 10.19 ? 111 HIS D CA  1 
ATOM   7324 C  C   . HIS D  1 111 ? 14.204  -7.381  -39.537 1.00 12.07 ? 111 HIS D C   1 
ATOM   7325 O  O   . HIS D  1 111 ? 14.504  -8.509  -40.032 1.00 14.07 ? 111 HIS D O   1 
ATOM   7326 C  CB  . HIS D  1 111 ? 15.707  -5.662  -40.167 1.00 10.95 ? 111 HIS D CB  1 
ATOM   7327 C  CG  . HIS D  1 111 ? 16.444  -4.413  -39.795 1.00 10.17 ? 111 HIS D CG  1 
ATOM   7328 N  ND1 . HIS D  1 111 ? 15.831  -3.188  -39.580 1.00 10.45 ? 111 HIS D ND1 1 
ATOM   7329 C  CD2 . HIS D  1 111 ? 17.803  -4.212  -39.506 1.00 11.84 ? 111 HIS D CD2 1 
ATOM   7330 C  CE1 . HIS D  1 111 ? 16.755  -2.284  -39.210 1.00 9.47  ? 111 HIS D CE1 1 
ATOM   7331 N  NE2 . HIS D  1 111 ? 17.960  -2.879  -39.174 1.00 13.46 ? 111 HIS D NE2 1 
ATOM   7332 N  N   . PHE D  1 112 ? 12.969  -6.958  -39.468 1.00 8.36  ? 112 PHE D N   1 
ATOM   7333 C  CA  . PHE D  1 112 ? 11.887  -7.526  -40.269 1.00 9.10  ? 112 PHE D CA  1 
ATOM   7334 C  C   . PHE D  1 112 ? 11.897  -6.758  -41.633 1.00 8.33  ? 112 PHE D C   1 
ATOM   7335 O  O   . PHE D  1 112 ? 12.659  -5.764  -41.803 1.00 7.68  ? 112 PHE D O   1 
ATOM   7336 C  CB  . PHE D  1 112 ? 10.540  -7.400  -39.560 1.00 9.98  ? 112 PHE D CB  1 
ATOM   7337 C  CG  . PHE D  1 112 ? 10.389  -8.473  -38.505 1.00 11.23 ? 112 PHE D CG  1 
ATOM   7338 C  CD1 . PHE D  1 112 ? 10.976  -8.379  -37.233 1.00 12.68 ? 112 PHE D CD1 1 
ATOM   7339 C  CD2 . PHE D  1 112 ? 9.774   -9.645  -38.852 1.00 13.65 ? 112 PHE D CD2 1 
ATOM   7340 C  CE1 . PHE D  1 112 ? 10.851  -9.430  -36.320 1.00 15.12 ? 112 PHE D CE1 1 
ATOM   7341 C  CE2 . PHE D  1 112 ? 9.648   -10.682 -37.962 1.00 16.15 ? 112 PHE D CE2 1 
ATOM   7342 C  CZ  . PHE D  1 112 ? 10.179  -10.585 -36.695 1.00 15.03 ? 112 PHE D CZ  1 
ATOM   7343 N  N   . ALA D  1 113 ? 11.076  -7.210  -42.585 1.00 7.81  ? 113 ALA D N   1 
ATOM   7344 C  CA  . ALA D  1 113 ? 11.055  -6.584  -43.932 1.00 9.04  ? 113 ALA D CA  1 
ATOM   7345 C  C   . ALA D  1 113 ? 10.575  -5.134  -43.898 1.00 8.10  ? 113 ALA D C   1 
ATOM   7346 O  O   . ALA D  1 113 ? 11.107  -4.310  -44.630 1.00 8.39  ? 113 ALA D O   1 
ATOM   7347 C  CB  . ALA D  1 113 ? 10.180  -7.372  -44.918 1.00 9.65  ? 113 ALA D CB  1 
ATOM   7348 N  N   . ALA D  1 114 ? 9.558   -4.870  -43.097 1.00 6.89  ? 114 ALA D N   1 
ATOM   7349 C  CA  . ALA D  1 114 ? 8.988   -3.500  -43.101 1.00 6.79  ? 114 ALA D CA  1 
ATOM   7350 C  C   . ALA D  1 114 ? 8.260   -3.380  -41.756 1.00 6.87  ? 114 ALA D C   1 
ATOM   7351 O  O   . ALA D  1 114 ? 8.239   -4.277  -40.862 1.00 7.02  ? 114 ALA D O   1 
ATOM   7352 C  CB  . ALA D  1 114 ? 8.014   -3.320  -44.254 1.00 7.20  ? 114 ALA D CB  1 
ATOM   7353 N  N   . GLU D  1 115 ? 7.637   -2.202  -41.566 1.00 6.93  ? 115 GLU D N   1 
ATOM   7354 C  CA  . GLU D  1 115 ? 6.917   -1.953  -40.267 1.00 7.08  ? 115 GLU D CA  1 
ATOM   7355 C  C   . GLU D  1 115 ? 5.761   -0.983  -40.558 1.00 6.69  ? 115 GLU D C   1 
ATOM   7356 O  O   . GLU D  1 115 ? 5.911   -0.016  -41.292 1.00 7.59  ? 115 GLU D O   1 
ATOM   7357 C  CB  . GLU D  1 115 ? 7.886   -1.394  -39.248 1.00 7.05  ? 115 GLU D CB  1 
ATOM   7358 C  CG  . GLU D  1 115 ? 7.337   -1.236  -37.838 1.00 6.99  ? 115 GLU D CG  1 
ATOM   7359 C  CD  . GLU D  1 115 ? 8.434   -0.990  -36.785 1.00 6.99  ? 115 GLU D CD  1 
ATOM   7360 O  OE1 . GLU D  1 115 ? 9.571   -1.481  -37.008 1.00 7.95  ? 115 GLU D OE1 1 
ATOM   7361 O  OE2 . GLU D  1 115 ? 8.154   -0.311  -35.744 1.00 7.49  ? 115 GLU D OE2 1 
ATOM   7362 N  N   . LEU D  1 116 ? 4.606   -1.286  -39.950 1.00 6.73  ? 116 LEU D N   1 
ATOM   7363 C  CA  . LEU D  1 116 ? 3.424   -0.376  -39.969 1.00 6.71  ? 116 LEU D CA  1 
ATOM   7364 C  C   . LEU D  1 116 ? 3.287   0.359   -38.672 1.00 7.13  ? 116 LEU D C   1 
ATOM   7365 O  O   . LEU D  1 116 ? 3.451   -0.247  -37.588 1.00 7.56  ? 116 LEU D O   1 
ATOM   7366 C  CB  . LEU D  1 116 ? 2.154   -1.298  -40.138 1.00 7.54  ? 116 LEU D CB  1 
ATOM   7367 C  CG  . LEU D  1 116 ? 0.822   -0.504  -40.034 1.00 8.28  ? 116 LEU D CG  1 
ATOM   7368 C  CD1 . LEU D  1 116 ? 0.624   0.338   -41.266 1.00 8.92  ? 116 LEU D CD1 1 
ATOM   7369 C  CD2 . LEU D  1 116 ? -0.305  -1.482  -39.874 1.00 8.88  ? 116 LEU D CD2 1 
ATOM   7370 N  N   . HIS D  1 117 ? 3.108   1.687   -38.764 1.00 6.75  ? 117 HIS D N   1 
ATOM   7371 C  CA  . HIS D  1 117 ? 2.779   2.501   -37.546 1.00 6.59  ? 117 HIS D CA  1 
ATOM   7372 C  C   . HIS D  1 117 ? 1.412   3.080   -37.670 1.00 6.70  ? 117 HIS D C   1 
ATOM   7373 O  O   . HIS D  1 117 ? 1.085   3.760   -38.639 1.00 7.84  ? 117 HIS D O   1 
ATOM   7374 C  CB  . HIS D  1 117 ? 3.777   3.649   -37.454 1.00 6.61  ? 117 HIS D CB  1 
ATOM   7375 C  CG  . HIS D  1 117 ? 5.141   3.146   -37.113 1.00 6.32  ? 117 HIS D CG  1 
ATOM   7376 N  ND1 . HIS D  1 117 ? 6.287   3.869   -37.395 1.00 6.48  ? 117 HIS D ND1 1 
ATOM   7377 C  CD2 . HIS D  1 117 ? 5.561   1.962   -36.485 1.00 7.47  ? 117 HIS D CD2 1 
ATOM   7378 C  CE1 . HIS D  1 117 ? 7.396   3.157   -36.912 1.00 7.92  ? 117 HIS D CE1 1 
ATOM   7379 N  NE2 . HIS D  1 117 ? 6.946   1.945   -36.441 1.00 7.19  ? 117 HIS D NE2 1 
ATOM   7380 N  N   . ILE D  1 118 ? 0.592   2.721   -36.682 1.00 7.61  ? 118 ILE D N   1 
ATOM   7381 C  CA  . ILE D  1 118 ? -0.742  3.386   -36.604 1.00 7.52  ? 118 ILE D CA  1 
ATOM   7382 C  C   . ILE D  1 118 ? -0.679  4.419   -35.520 1.00 6.79  ? 118 ILE D C   1 
ATOM   7383 O  O   . ILE D  1 118 ? -0.521  4.083   -34.293 1.00 7.47  ? 118 ILE D O   1 
ATOM   7384 C  CB  . ILE D  1 118 ? -1.868  2.368   -36.322 1.00 8.03  ? 118 ILE D CB  1 
ATOM   7385 C  CG1 . ILE D  1 118 ? -1.804  1.175   -37.348 1.00 7.67  ? 118 ILE D CG1 1 
ATOM   7386 C  CG2 . ILE D  1 118 ? -3.204  3.138   -36.408 1.00 8.69  ? 118 ILE D CG2 1 
ATOM   7387 C  CD1 . ILE D  1 118 ? -2.841  0.038   -36.968 1.00 9.58  ? 118 ILE D CD1 1 
ATOM   7388 N  N   . VAL D  1 119 ? -0.624  5.717   -35.918 1.00 7.62  ? 119 VAL D N   1 
ATOM   7389 C  CA  . VAL D  1 119 ? -0.384  6.779   -34.939 1.00 7.65  ? 119 VAL D CA  1 
ATOM   7390 C  C   . VAL D  1 119 ? -1.719  7.317   -34.384 1.00 7.15  ? 119 VAL D C   1 
ATOM   7391 O  O   . VAL D  1 119 ? -2.682  7.557   -35.128 1.00 8.37  ? 119 VAL D O   1 
ATOM   7392 C  CB  . VAL D  1 119 ? 0.293   7.939   -35.719 1.00 6.87  ? 119 VAL D CB  1 
ATOM   7393 C  CG1 . VAL D  1 119 ? 0.679   9.067   -34.749 1.00 8.26  ? 119 VAL D CG1 1 
ATOM   7394 C  CG2 . VAL D  1 119 ? 1.538   7.446   -36.422 1.00 7.56  ? 119 VAL D CG2 1 
ATOM   7395 N  N   . HIS D  1 120 ? -1.707  7.468   -33.062 1.00 7.86  ? 120 HIS D N   1 
ATOM   7396 C  CA  . HIS D  1 120 ? -2.834  8.040   -32.294 1.00 7.97  ? 120 HIS D CA  1 
ATOM   7397 C  C   . HIS D  1 120 ? -2.346  9.153   -31.438 1.00 8.61  ? 120 HIS D C   1 
ATOM   7398 O  O   . HIS D  1 120 ? -1.184  9.215   -31.013 1.00 9.55  ? 120 HIS D O   1 
ATOM   7399 C  CB  . HIS D  1 120 ? -3.427  6.912   -31.335 1.00 8.88  ? 120 HIS D CB  1 
ATOM   7400 C  CG  . HIS D  1 120 ? -3.899  5.663   -32.012 1.00 8.19  ? 120 HIS D CG  1 
ATOM   7401 N  ND1 . HIS D  1 120 ? -3.005  4.779   -32.618 1.00 8.57  ? 120 HIS D ND1 1 
ATOM   7402 C  CD2 . HIS D  1 120 ? -5.140  5.097   -32.115 1.00 9.51  ? 120 HIS D CD2 1 
ATOM   7403 C  CE1 . HIS D  1 120 ? -3.708  3.720   -33.083 1.00 8.60  ? 120 HIS D CE1 1 
ATOM   7404 N  NE2 . HIS D  1 120 ? -5.033  3.909   -32.808 1.00 9.22  ? 120 HIS D NE2 1 
ATOM   7405 N  N   . TYR D  1 121 ? -3.286  10.102  -31.125 1.00 8.80  ? 121 TYR D N   1 
ATOM   7406 C  CA  . TYR D  1 121 ? -2.937  11.206  -30.247 1.00 9.31  ? 121 TYR D CA  1 
ATOM   7407 C  C   . TYR D  1 121 ? -3.880  11.209  -29.005 1.00 7.98  ? 121 TYR D C   1 
ATOM   7408 O  O   . TYR D  1 121 ? -4.974  10.668  -29.040 1.00 9.32  ? 121 TYR D O   1 
ATOM   7409 C  CB  . TYR D  1 121 ? -3.075  12.535  -31.043 1.00 9.93  ? 121 TYR D CB  1 
ATOM   7410 C  CG  . TYR D  1 121 ? -4.433  12.975  -31.386 1.00 9.62  ? 121 TYR D CG  1 
ATOM   7411 C  CD1 . TYR D  1 121 ? -5.099  12.465  -32.471 1.00 11.85 ? 121 TYR D CD1 1 
ATOM   7412 C  CD2 . TYR D  1 121 ? -5.073  13.870  -30.543 1.00 10.85 ? 121 TYR D CD2 1 
ATOM   7413 C  CE1 . TYR D  1 121 ? -6.402  12.807  -32.808 1.00 12.05 ? 121 TYR D CE1 1 
ATOM   7414 C  CE2 . TYR D  1 121 ? -6.405  14.256  -30.825 1.00 12.27 ? 121 TYR D CE2 1 
ATOM   7415 C  CZ  . TYR D  1 121 ? -7.030  13.723  -31.941 1.00 14.34 ? 121 TYR D CZ  1 
ATOM   7416 O  OH  . TYR D  1 121 ? -8.327  14.052  -32.314 1.00 19.31 ? 121 TYR D OH  1 
ATOM   7417 N  N   . ASN D  1 122 ? -3.369  11.844  -27.947 1.00 9.45  ? 122 ASN D N   1 
ATOM   7418 C  CA  . ASN D  1 122 ? -4.091  11.919  -26.635 1.00 9.79  ? 122 ASN D CA  1 
ATOM   7419 C  C   . ASN D  1 122 ? -5.225  12.966  -26.807 1.00 10.39 ? 122 ASN D C   1 
ATOM   7420 O  O   . ASN D  1 122 ? -4.973  14.151  -26.587 1.00 11.38 ? 122 ASN D O   1 
ATOM   7421 C  CB  . ASN D  1 122 ? -3.083  12.259  -25.541 1.00 9.08  ? 122 ASN D CB  1 
ATOM   7422 C  CG  . ASN D  1 122 ? -3.688  12.112  -24.168 1.00 10.13 ? 122 ASN D CG  1 
ATOM   7423 O  OD1 . ASN D  1 122 ? -4.926  12.202  -24.020 1.00 11.06 ? 122 ASN D OD1 1 
ATOM   7424 N  ND2 . ASN D  1 122 ? -2.829  11.819  -23.178 1.00 11.58 ? 122 ASN D ND2 1 
ATOM   7425 N  N   . SER D  1 123 ? -6.397  12.454  -27.163 1.00 10.41 ? 123 SER D N   1 
ATOM   7426 C  CA  . SER D  1 123 ? -7.573  13.323  -27.357 1.00 11.98 ? 123 SER D CA  1 
ATOM   7427 C  C   . SER D  1 123 ? -8.180  13.740  -26.009 1.00 12.36 ? 123 SER D C   1 
ATOM   7428 O  O   . SER D  1 123 ? -9.052  14.625  -26.036 1.00 13.94 ? 123 SER D O   1 
ATOM   7429 C  CB  . SER D  1 123 ? -8.569  12.666  -28.285 1.00 12.41 ? 123 SER D CB  1 
ATOM   7430 O  OG  . SER D  1 123 ? -8.835  11.310  -27.891 1.00 13.77 ? 123 SER D OG  1 
ATOM   7431 N  N   . ASP D  1 124 ? -7.740  13.166  -24.894 1.00 11.31 ? 124 ASP D N   1 
ATOM   7432 C  CA  . ASP D  1 124 ? -8.229  13.653  -23.566 1.00 12.47 ? 124 ASP D CA  1 
ATOM   7433 C  C   . ASP D  1 124 ? -7.541  14.986  -23.297 1.00 14.55 ? 124 ASP D C   1 
ATOM   7434 O  O   . ASP D  1 124 ? -8.124  15.854  -22.585 1.00 16.96 ? 124 ASP D O   1 
ATOM   7435 C  CB  . ASP D  1 124 ? -7.894  12.672  -22.428 1.00 11.98 ? 124 ASP D CB  1 
ATOM   7436 C  CG  . ASP D  1 124 ? -8.804  11.443  -22.469 1.00 11.99 ? 124 ASP D CG  1 
ATOM   7437 O  OD1 . ASP D  1 124 ? -9.821  11.489  -23.208 1.00 14.09 ? 124 ASP D OD1 1 
ATOM   7438 O  OD2 . ASP D  1 124 ? -8.509  10.436  -21.796 1.00 13.57 ? 124 ASP D OD2 1 
ATOM   7439 N  N   . LEU D  1 125 ? -6.328  15.166  -23.750 1.00 12.51 ? 125 LEU D N   1 
ATOM   7440 C  CA  . LEU D  1 125 ? -5.492  16.337  -23.414 1.00 13.67 ? 125 LEU D CA  1 
ATOM   7441 C  C   . LEU D  1 125 ? -5.420  17.350  -24.541 1.00 14.41 ? 125 LEU D C   1 
ATOM   7442 O  O   . LEU D  1 125 ? -5.269  18.573  -24.264 1.00 15.54 ? 125 LEU D O   1 
ATOM   7443 C  CB  . LEU D  1 125 ? -4.074  15.954  -22.995 1.00 13.49 ? 125 LEU D CB  1 
ATOM   7444 C  CG  . LEU D  1 125 ? -3.815  15.539  -21.558 1.00 14.15 ? 125 LEU D CG  1 
ATOM   7445 C  CD1 . LEU D  1 125 ? -4.725  14.419  -21.184 1.00 15.69 ? 125 LEU D CD1 1 
ATOM   7446 C  CD2 . LEU D  1 125 ? -2.383  15.055  -21.408 1.00 14.07 ? 125 LEU D CD2 1 
ATOM   7447 N  N   . TYR D  1 126 ? -5.438  16.877  -25.778 1.00 12.73 ? 126 TYR D N   1 
ATOM   7448 C  CA  . TYR D  1 126 ? -5.137  17.684  -26.954 1.00 12.17 ? 126 TYR D CA  1 
ATOM   7449 C  C   . TYR D  1 126 ? -6.192  17.660  -28.018 1.00 13.31 ? 126 TYR D C   1 
ATOM   7450 O  O   . TYR D  1 126 ? -6.865  16.659  -28.207 1.00 13.22 ? 126 TYR D O   1 
ATOM   7451 C  CB  . TYR D  1 126 ? -3.726  17.246  -27.528 1.00 10.83 ? 126 TYR D CB  1 
ATOM   7452 C  CG  . TYR D  1 126 ? -2.676  17.254  -26.449 1.00 11.01 ? 126 TYR D CG  1 
ATOM   7453 C  CD1 . TYR D  1 126 ? -2.326  18.432  -25.798 1.00 10.78 ? 126 TYR D CD1 1 
ATOM   7454 C  CD2 . TYR D  1 126 ? -2.077  16.072  -26.038 1.00 11.68 ? 126 TYR D CD2 1 
ATOM   7455 C  CE1 . TYR D  1 126 ? -1.388  18.426  -24.774 1.00 11.64 ? 126 TYR D CE1 1 
ATOM   7456 C  CE2 . TYR D  1 126 ? -1.146  16.056  -25.022 1.00 11.03 ? 126 TYR D CE2 1 
ATOM   7457 C  CZ  . TYR D  1 126 ? -0.799  17.231  -24.388 1.00 11.12 ? 126 TYR D CZ  1 
ATOM   7458 O  OH  . TYR D  1 126 ? 0.140   17.215  -23.366 1.00 11.86 ? 126 TYR D OH  1 
ATOM   7459 N  N   . PRO D  1 127 ? -6.313  18.795  -28.756 1.00 14.37 ? 127 PRO D N   1 
ATOM   7460 C  CA  . PRO D  1 127 ? -7.419  18.893  -29.710 1.00 16.31 ? 127 PRO D CA  1 
ATOM   7461 C  C   . PRO D  1 127 ? -7.164  18.260  -31.013 1.00 17.12 ? 127 PRO D C   1 
ATOM   7462 O  O   . PRO D  1 127 ? -8.107  18.070  -31.792 1.00 21.70 ? 127 PRO D O   1 
ATOM   7463 C  CB  . PRO D  1 127 ? -7.535  20.413  -29.925 1.00 18.46 ? 127 PRO D CB  1 
ATOM   7464 C  CG  . PRO D  1 127 ? -6.178  20.943  -29.550 1.00 17.03 ? 127 PRO D CG  1 
ATOM   7465 C  CD  . PRO D  1 127 ? -5.717  20.092  -28.390 1.00 15.81 ? 127 PRO D CD  1 
ATOM   7466 N  N   . ASP D  1 128 ? -5.920  17.933  -31.330 1.00 15.01 ? 128 ASP D N   1 
ATOM   7467 C  CA  . ASP D  1 128 ? -5.535  17.328  -32.563 1.00 16.20 ? 128 ASP D CA  1 
ATOM   7468 C  C   . ASP D  1 128 ? -4.105  16.799  -32.514 1.00 16.23 ? 128 ASP D C   1 
ATOM   7469 O  O   . ASP D  1 128 ? -3.363  17.073  -31.571 1.00 14.69 ? 128 ASP D O   1 
ATOM   7470 C  CB  . ASP D  1 128 ? -5.615  18.363  -33.714 1.00 18.20 ? 128 ASP D CB  1 
ATOM   7471 C  CG  . ASP D  1 128 ? -4.662  19.501  -33.474 1.00 16.66 ? 128 ASP D CG  1 
ATOM   7472 O  OD1 . ASP D  1 128 ? -4.975  20.443  -32.681 1.00 23.18 ? 128 ASP D OD1 1 
ATOM   7473 O  OD2 . ASP D  1 128 ? -3.602  19.458  -34.043 1.00 20.53 ? 128 ASP D OD2 1 
ATOM   7474 N  N   . ALA D  1 129 ? -3.693  15.979  -33.459 1.00 15.41 ? 129 ALA D N   1 
ATOM   7475 C  CA  . ALA D  1 129 ? -2.467  15.297  -33.414 1.00 14.71 ? 129 ALA D CA  1 
ATOM   7476 C  C   . ALA D  1 129 ? -1.204  16.187  -33.525 1.00 15.24 ? 129 ALA D C   1 
ATOM   7477 O  O   . ALA D  1 129 ? -0.167  15.976  -32.926 1.00 15.28 ? 129 ALA D O   1 
ATOM   7478 C  CB  . ALA D  1 129 ? -2.462  14.285  -34.561 1.00 19.78 ? 129 ALA D CB  1 
ATOM   7479 N  N   . SER D  1 130 ? -1.268  17.190  -34.426 1.00 15.74 ? 130 SER D N   1 
ATOM   7480 C  CA  . SER D  1 130 ? -0.122  18.087  -34.560 1.00 14.40 ? 130 SER D CA  1 
ATOM   7481 C  C   . SER D  1 130 ? 0.105   18.844  -33.207 1.00 12.20 ? 130 SER D C   1 
ATOM   7482 O  O   . SER D  1 130 ? 1.242   18.936  -32.743 1.00 13.95 ? 130 SER D O   1 
ATOM   7483 C  CB  . SER D  1 130 ? -0.336  19.115  -35.712 1.00 14.39 ? 130 SER D CB  1 
ATOM   7484 O  OG  . SER D  1 130 ? -0.379  18.406  -36.937 1.00 19.82 ? 130 SER D OG  1 
ATOM   7485 N  N   . THR D  1 131 ? -0.964  19.315  -32.599 1.00 13.00 ? 131 THR D N   1 
ATOM   7486 C  CA  . THR D  1 131 ? -0.794  19.974  -31.283 1.00 11.69 ? 131 THR D CA  1 
ATOM   7487 C  C   . THR D  1 131 ? -0.183  18.999  -30.269 1.00 12.23 ? 131 THR D C   1 
ATOM   7488 O  O   . THR D  1 131 ? 0.663   19.333  -29.401 1.00 13.27 ? 131 THR D O   1 
ATOM   7489 C  CB  . THR D  1 131 ? -2.082  20.534  -30.748 1.00 14.06 ? 131 THR D CB  1 
ATOM   7490 O  OG1 . THR D  1 131 ? -2.642  21.501  -31.700 1.00 17.91 ? 131 THR D OG1 1 
ATOM   7491 C  CG2 . THR D  1 131 ? -1.966  21.243  -29.332 1.00 15.07 ? 131 THR D CG2 1 
ATOM   7492 N  N   . ALA D  1 132 ? -0.671  17.779  -30.310 1.00 11.13 ? 132 ALA D N   1 
ATOM   7493 C  CA  . ALA D  1 132 ? -0.261  16.777  -29.357 1.00 10.52 ? 132 ALA D CA  1 
ATOM   7494 C  C   . ALA D  1 132 ? 1.213   16.338  -29.471 1.00 10.01 ? 132 ALA D C   1 
ATOM   7495 O  O   . ALA D  1 132 ? 1.873   15.867  -28.533 1.00 10.48 ? 132 ALA D O   1 
ATOM   7496 C  CB  . ALA D  1 132 ? -1.115  15.496  -29.523 1.00 9.38  ? 132 ALA D CB  1 
ATOM   7497 N  N   . SER D  1 133 ? 1.726   16.433  -30.719 1.00 10.73 ? 133 SER D N   1 
ATOM   7498 C  CA  . SER D  1 133 ? 2.966   15.779  -31.113 1.00 11.85 ? 133 SER D CA  1 
ATOM   7499 C  C   . SER D  1 133 ? 4.221   16.160  -30.306 1.00 12.50 ? 133 SER D C   1 
ATOM   7500 O  O   . SER D  1 133 ? 5.189   15.428  -30.105 1.00 12.51 ? 133 SER D O   1 
ATOM   7501 C  CB  . SER D  1 133 ? 3.239   15.942  -32.610 1.00 12.59 ? 133 SER D CB  1 
ATOM   7502 O  OG  . SER D  1 133 ? 3.656   17.292  -32.888 1.00 15.57 ? 133 SER D OG  1 
ATOM   7503 N  N   . ASN D  1 134 ? 4.278   17.435  -29.813 1.00 10.70 ? 134 ASN D N   1 
ATOM   7504 C  CA  . ASN D  1 134 ? 5.415   17.891  -29.020 1.00 12.58 ? 134 ASN D CA  1 
ATOM   7505 C  C   . ASN D  1 134 ? 5.112   18.108  -27.568 1.00 11.72 ? 134 ASN D C   1 
ATOM   7506 O  O   . ASN D  1 134 ? 5.885   18.743  -26.840 1.00 13.64 ? 134 ASN D O   1 
ATOM   7507 C  CB  . ASN D  1 134 ? 6.079   19.158  -29.637 1.00 13.23 ? 134 ASN D CB  1 
ATOM   7508 C  CG  . ASN D  1 134 ? 5.186   20.386  -29.450 1.00 16.02 ? 134 ASN D CG  1 
ATOM   7509 O  OD1 . ASN D  1 134 ? 3.978   20.288  -29.289 1.00 13.45 ? 134 ASN D OD1 1 
ATOM   7510 N  ND2 . ASN D  1 134 ? 5.808   21.558  -29.420 1.00 15.74 ? 134 ASN D ND2 1 
ATOM   7511 N  N   . LYS D  1 135 ? 4.037   17.446  -27.125 1.00 10.86 ? 135 LYS D N   1 
ATOM   7512 C  CA  . LYS D  1 135 ? 3.557   17.678  -25.747 1.00 11.70 ? 135 LYS D CA  1 
ATOM   7513 C  C   . LYS D  1 135 ? 3.507   16.384  -24.936 1.00 11.71 ? 135 LYS D C   1 
ATOM   7514 O  O   . LYS D  1 135 ? 3.440   15.250  -25.467 1.00 11.20 ? 135 LYS D O   1 
ATOM   7515 C  CB  . LYS D  1 135 ? 2.178   18.379  -25.760 1.00 12.01 ? 135 LYS D CB  1 
ATOM   7516 C  CG  . LYS D  1 135 ? 2.376   19.838  -26.266 1.00 13.72 ? 135 LYS D CG  1 
ATOM   7517 C  CD  . LYS D  1 135 ? 1.063   20.620  -26.282 1.00 15.76 ? 135 LYS D CD  1 
ATOM   7518 C  CE  . LYS D  1 135 ? 1.245   21.927  -27.055 1.00 14.68 ? 135 LYS D CE  1 
ATOM   7519 N  NZ  . LYS D  1 135 ? 1.644   21.782  -28.526 1.00 13.48 ? 135 LYS D NZ  1 
ATOM   7520 N  N   . SER D  1 136 ? 3.528   16.576  -23.627 1.00 11.56 ? 136 SER D N   1 
ATOM   7521 C  CA  . SER D  1 136 ? 3.570   15.444  -22.677 1.00 11.83 ? 136 SER D CA  1 
ATOM   7522 C  C   . SER D  1 136 ? 2.455   14.432  -22.947 1.00 11.43 ? 136 SER D C   1 
ATOM   7523 O  O   . SER D  1 136 ? 1.277   14.766  -23.090 1.00 10.95 ? 136 SER D O   1 
ATOM   7524 C  CB  . SER D  1 136 ? 3.346   16.066  -21.267 1.00 14.11 ? 136 SER D CB  1 
ATOM   7525 O  OG  . SER D  1 136 ? 3.672   14.993  -20.380 1.00 20.10 ? 136 SER D OG  1 
ATOM   7526 N  N   . GLU D  1 137 ? 2.819   13.124  -22.956 1.00 11.62 ? 137 GLU D N   1 
ATOM   7527 C  CA  . GLU D  1 137 ? 1.820   12.102  -23.208 1.00 11.05 ? 137 GLU D CA  1 
ATOM   7528 C  C   . GLU D  1 137 ? 1.039   12.232  -24.535 1.00 10.44 ? 137 GLU D C   1 
ATOM   7529 O  O   . GLU D  1 137 ? -0.063  11.741  -24.662 1.00 11.78 ? 137 GLU D O   1 
ATOM   7530 C  CB  . GLU D  1 137 ? 0.821   11.907  -22.014 1.00 13.10 ? 137 GLU D CB  1 
ATOM   7531 C  CG  . GLU D  1 137 ? 1.490   11.949  -20.623 1.00 15.62 ? 137 GLU D CG  1 
ATOM   7532 C  CD  . GLU D  1 137 ? 2.355   10.706  -20.273 1.00 19.65 ? 137 GLU D CD  1 
ATOM   7533 O  OE1 . GLU D  1 137 ? 2.203   9.640   -20.875 1.00 22.78 ? 137 GLU D OE1 1 
ATOM   7534 O  OE2 . GLU D  1 137 ? 3.310   10.877  -19.469 1.00 30.62 ? 137 GLU D OE2 1 
ATOM   7535 N  N   . GLY D  1 138 ? 1.625   12.930  -25.537 1.00 9.64  ? 138 GLY D N   1 
ATOM   7536 C  CA  . GLY D  1 138 ? 0.832   13.270  -26.622 1.00 10.29 ? 138 GLY D CA  1 
ATOM   7537 C  C   . GLY D  1 138 ? 0.402   12.176  -27.577 1.00 9.03  ? 138 GLY D C   1 
ATOM   7538 O  O   . GLY D  1 138 ? -0.620  12.303  -28.251 1.00 9.14  ? 138 GLY D O   1 
ATOM   7539 N  N   . LEU D  1 139 ? 1.273   11.155  -27.742 1.00 8.37  ? 139 LEU D N   1 
ATOM   7540 C  CA  . LEU D  1 139 ? 1.007   10.179  -28.895 1.00 8.58  ? 139 LEU D CA  1 
ATOM   7541 C  C   . LEU D  1 139 ? 1.154   8.748   -28.386 1.00 7.82  ? 139 LEU D C   1 
ATOM   7542 O  O   . LEU D  1 139 ? 1.908   8.503   -27.423 1.00 8.58  ? 139 LEU D O   1 
ATOM   7543 C  CB  . LEU D  1 139 ? 2.051   10.404  -30.039 1.00 9.77  ? 139 LEU D CB  1 
ATOM   7544 C  CG  . LEU D  1 139 ? 2.018   11.806  -30.697 1.00 9.28  ? 139 LEU D CG  1 
ATOM   7545 C  CD1 . LEU D  1 139 ? 3.293   11.951  -31.548 1.00 11.30 ? 139 LEU D CD1 1 
ATOM   7546 C  CD2 . LEU D  1 139 ? 0.767   11.998  -31.544 1.00 11.09 ? 139 LEU D CD2 1 
ATOM   7547 N  N   . ALA D  1 140 ? 0.462   7.862   -29.110 1.00 7.88  ? 140 ALA D N   1 
ATOM   7548 C  CA  . ALA D  1 140 ? 0.667   6.423   -28.874 1.00 7.48  ? 140 ALA D CA  1 
ATOM   7549 C  C   . ALA D  1 140 ? 0.667   5.789   -30.234 1.00 7.38  ? 140 ALA D C   1 
ATOM   7550 O  O   . ALA D  1 140 ? -0.174  6.102   -31.050 1.00 8.90  ? 140 ALA D O   1 
ATOM   7551 C  CB  . ALA D  1 140 ? -0.520  5.875   -28.041 1.00 10.06 ? 140 ALA D CB  1 
ATOM   7552 N  N   . VAL D  1 141 ? 1.667   4.950   -30.501 1.00 7.98  ? 141 VAL D N   1 
ATOM   7553 C  CA  . VAL D  1 141 ? 1.732   4.242   -31.764 1.00 8.52  ? 141 VAL D CA  1 
ATOM   7554 C  C   . VAL D  1 141 ? 1.547   2.752   -31.553 1.00 8.10  ? 141 VAL D C   1 
ATOM   7555 O  O   . VAL D  1 141 ? 2.093   2.181   -30.582 1.00 8.95  ? 141 VAL D O   1 
ATOM   7556 C  CB  . VAL D  1 141 ? 3.094   4.527   -32.434 1.00 8.56  ? 141 VAL D CB  1 
ATOM   7557 C  CG1 . VAL D  1 141 ? 3.191   3.787   -33.807 1.00 10.48 ? 141 VAL D CG1 1 
ATOM   7558 C  CG2 . VAL D  1 141 ? 3.231   6.028   -32.619 1.00 10.26 ? 141 VAL D CG2 1 
ATOM   7559 N  N   . LEU D  1 142 ? 0.811   2.120   -32.458 1.00 7.72  ? 142 LEU D N   1 
ATOM   7560 C  CA  . LEU D  1 142 ? 0.793   0.675   -32.551 1.00 8.29  ? 142 LEU D CA  1 
ATOM   7561 C  C   . LEU D  1 142 ? 1.730   0.340   -33.712 1.00 8.17  ? 142 LEU D C   1 
ATOM   7562 O  O   . LEU D  1 142 ? 1.534   0.810   -34.838 1.00 9.99  ? 142 LEU D O   1 
ATOM   7563 C  CB  . LEU D  1 142 ? -0.607  0.142   -32.891 1.00 9.56  ? 142 LEU D CB  1 
ATOM   7564 C  CG  . LEU D  1 142 ? -1.700  0.500   -31.897 1.00 9.62  ? 142 LEU D CG  1 
ATOM   7565 C  CD1 . LEU D  1 142 ? -3.006  -0.142  -32.372 1.00 10.22 ? 142 LEU D CD1 1 
ATOM   7566 C  CD2 . LEU D  1 142 ? -1.350  0.051   -30.438 1.00 11.42 ? 142 LEU D CD2 1 
ATOM   7567 N  N   . ALA D  1 143 ? 2.702   -0.507  -33.408 1.00 8.14  ? 143 ALA D N   1 
ATOM   7568 C  CA  . ALA D  1 143 ? 3.701   -0.907  -34.450 1.00 7.58  ? 143 ALA D CA  1 
ATOM   7569 C  C   . ALA D  1 143 ? 3.506   -2.419  -34.729 1.00 7.60  ? 143 ALA D C   1 
ATOM   7570 O  O   . ALA D  1 143 ? 3.417   -3.271  -33.852 1.00 8.40  ? 143 ALA D O   1 
ATOM   7571 C  CB  . ALA D  1 143 ? 5.083   -0.668  -33.889 1.00 8.32  ? 143 ALA D CB  1 
ATOM   7572 N  N   . VAL D  1 144 ? 3.421   -2.657  -36.035 1.00 6.55  ? 144 VAL D N   1 
ATOM   7573 C  CA  . VAL D  1 144 ? 3.289   -4.054  -36.567 1.00 7.70  ? 144 VAL D CA  1 
ATOM   7574 C  C   . VAL D  1 144 ? 4.535   -4.371  -37.385 1.00 7.33  ? 144 VAL D C   1 
ATOM   7575 O  O   . VAL D  1 144 ? 4.826   -3.708  -38.364 1.00 8.44  ? 144 VAL D O   1 
ATOM   7576 C  CB  . VAL D  1 144 ? 2.031   -4.275  -37.379 1.00 8.27  ? 144 VAL D CB  1 
ATOM   7577 C  CG1 . VAL D  1 144 ? 1.934   -5.721  -37.819 1.00 9.59  ? 144 VAL D CG1 1 
ATOM   7578 C  CG2 . VAL D  1 144 ? 0.780   -3.820  -36.569 1.00 8.47  ? 144 VAL D CG2 1 
ATOM   7579 N  N   . LEU D  1 145 ? 5.268   -5.394  -36.921 1.00 7.50  ? 145 LEU D N   1 
ATOM   7580 C  CA  . LEU D  1 145 ? 6.446   -5.861  -37.658 1.00 7.68  ? 145 LEU D CA  1 
ATOM   7581 C  C   . LEU D  1 145 ? 5.945   -6.684  -38.825 1.00 7.06  ? 145 LEU D C   1 
ATOM   7582 O  O   . LEU D  1 145 ? 4.984   -7.498  -38.716 1.00 7.87  ? 145 LEU D O   1 
ATOM   7583 C  CB  . LEU D  1 145 ? 7.295   -6.732  -36.746 1.00 8.23  ? 145 LEU D CB  1 
ATOM   7584 C  CG  . LEU D  1 145 ? 7.829   -6.007  -35.567 1.00 9.32  ? 145 LEU D CG  1 
ATOM   7585 C  CD1 . LEU D  1 145 ? 8.321   -7.022  -34.508 1.00 10.45 ? 145 LEU D CD1 1 
ATOM   7586 C  CD2 . LEU D  1 145 ? 8.944   -5.056  -35.935 1.00 11.89 ? 145 LEU D CD2 1 
ATOM   7587 N  N   . ILE D  1 146 ? 6.519   -6.487  -40.008 1.00 6.91  ? 146 ILE D N   1 
ATOM   7588 C  CA  . ILE D  1 146 ? 6.055   -7.119  -41.262 1.00 7.54  ? 146 ILE D CA  1 
ATOM   7589 C  C   . ILE D  1 146 ? 7.172   -8.019  -41.837 1.00 8.06  ? 146 ILE D C   1 
ATOM   7590 O  O   . ILE D  1 146 ? 8.282   -7.523  -42.106 1.00 8.23  ? 146 ILE D O   1 
ATOM   7591 C  CB  . ILE D  1 146 ? 5.702   -6.065  -42.323 1.00 7.92  ? 146 ILE D CB  1 
ATOM   7592 C  CG1 . ILE D  1 146 ? 4.544   -5.180  -41.822 1.00 9.11  ? 146 ILE D CG1 1 
ATOM   7593 C  CG2 . ILE D  1 146 ? 5.309   -6.772  -43.658 1.00 8.17  ? 146 ILE D CG2 1 
ATOM   7594 C  CD1 . ILE D  1 146 ? 4.203   -3.957  -42.685 1.00 9.51  ? 146 ILE D CD1 1 
ATOM   7595 N  N   A GLU D  1 147 ? 6.910   -9.319  -41.977 0.50 8.04  ? 147 GLU D N   1 
ATOM   7596 N  N   B GLU D  1 147 ? 6.823   -9.291  -42.005 0.50 7.46  ? 147 GLU D N   1 
ATOM   7597 C  CA  A GLU D  1 147 ? 7.929   -10.278 -42.452 0.50 9.44  ? 147 GLU D CA  1 
ATOM   7598 C  CA  B GLU D  1 147 ? 7.709   -10.280 -42.554 0.50 8.19  ? 147 GLU D CA  1 
ATOM   7599 C  C   A GLU D  1 147 ? 7.510   -10.681 -43.857 0.50 8.33  ? 147 GLU D C   1 
ATOM   7600 C  C   B GLU D  1 147 ? 7.430   -10.563 -44.029 0.50 7.63  ? 147 GLU D C   1 
ATOM   7601 O  O   A GLU D  1 147 ? 6.323   -10.829 -44.116 0.50 8.16  ? 147 GLU D O   1 
ATOM   7602 O  O   B GLU D  1 147 ? 6.294   -10.558 -44.510 0.50 7.03  ? 147 GLU D O   1 
ATOM   7603 C  CB  A GLU D  1 147 ? 7.986   -11.505 -41.488 0.50 10.63 ? 147 GLU D CB  1 
ATOM   7604 C  CB  B GLU D  1 147 ? 7.527   -11.560 -41.719 0.50 8.28  ? 147 GLU D CB  1 
ATOM   7605 C  CG  A GLU D  1 147 ? 7.055   -12.706 -41.830 0.50 15.76 ? 147 GLU D CG  1 
ATOM   7606 C  CG  B GLU D  1 147 ? 8.537   -12.663 -42.029 0.50 9.02  ? 147 GLU D CG  1 
ATOM   7607 C  CD  A GLU D  1 147 ? 6.978   -13.685 -40.674 0.50 14.60 ? 147 GLU D CD  1 
ATOM   7608 C  CD  B GLU D  1 147 ? 8.827   -13.567 -40.852 0.50 11.88 ? 147 GLU D CD  1 
ATOM   7609 O  OE1 A GLU D  1 147 ? 7.935   -13.727 -39.872 0.50 16.16 ? 147 GLU D OE1 1 
ATOM   7610 O  OE1 B GLU D  1 147 ? 8.293   -13.310 -39.752 0.50 14.45 ? 147 GLU D OE1 1 
ATOM   7611 O  OE2 A GLU D  1 147 ? 5.960   -14.396 -40.554 0.50 17.52 ? 147 GLU D OE2 1 
ATOM   7612 O  OE2 B GLU D  1 147 ? 9.596   -14.534 -41.030 0.50 15.43 ? 147 GLU D OE2 1 
ATOM   7613 N  N   . MET D  1 148 ? 8.484   -10.861 -44.786 1.00 8.49  ? 148 MET D N   1 
ATOM   7614 C  CA  . MET D  1 148 ? 8.231   -11.449 -46.137 1.00 8.99  ? 148 MET D CA  1 
ATOM   7615 C  C   . MET D  1 148 ? 7.643   -12.868 -46.000 1.00 8.21  ? 148 MET D C   1 
ATOM   7616 O  O   . MET D  1 148 ? 8.227   -13.715 -45.345 1.00 9.94  ? 148 MET D O   1 
ATOM   7617 C  CB  . MET D  1 148 ? 9.559   -11.489 -46.911 1.00 8.97  ? 148 MET D CB  1 
ATOM   7618 C  CG  . MET D  1 148 ? 9.340   -11.947 -48.298 1.00 10.21 ? 148 MET D CG  1 
ATOM   7619 S  SD  . MET D  1 148 ? 10.851  -11.983 -49.321 1.00 12.10 ? 148 MET D SD  1 
ATOM   7620 C  CE  . MET D  1 148 ? 11.290  -10.217 -49.366 1.00 12.82 ? 148 MET D CE  1 
ATOM   7621 N  N   . GLY D  1 149 ? 6.493   -12.976 -46.624 1.00 8.41  ? 149 GLY D N   1 
ATOM   7622 C  CA  . GLY D  1 149 ? 5.707   -14.222 -46.502 1.00 8.53  ? 149 GLY D CA  1 
ATOM   7623 C  C   . GLY D  1 149 ? 4.607   -14.335 -47.532 1.00 7.40  ? 149 GLY D C   1 
ATOM   7624 O  O   . GLY D  1 149 ? 4.807   -14.125 -48.723 1.00 7.39  ? 149 GLY D O   1 
ATOM   7625 N  N   . SER D  1 150 ? 3.409   -14.697 -47.076 1.00 9.21  ? 150 SER D N   1 
ATOM   7626 C  CA  . SER D  1 150 ? 2.233   -14.832 -47.966 1.00 8.47  ? 150 SER D CA  1 
ATOM   7627 C  C   . SER D  1 150 ? 1.668   -13.455 -48.355 1.00 8.75  ? 150 SER D C   1 
ATOM   7628 O  O   . SER D  1 150 ? 1.750   -12.496 -47.544 1.00 9.96  ? 150 SER D O   1 
ATOM   7629 C  CB  . SER D  1 150 ? 1.169   -15.597 -47.199 1.00 9.29  ? 150 SER D CB  1 
ATOM   7630 O  OG  . SER D  1 150 ? 1.563   -17.016 -47.105 1.00 10.41 ? 150 SER D OG  1 
ATOM   7631 N  N   . PHE D  1 151 ? 1.094   -13.454 -49.566 1.00 8.99  ? 151 PHE D N   1 
ATOM   7632 C  CA  . PHE D  1 151 ? 0.272   -12.339 -50.002 1.00 9.07  ? 151 PHE D CA  1 
ATOM   7633 C  C   . PHE D  1 151 ? -0.772  -11.974 -48.914 1.00 9.47  ? 151 PHE D C   1 
ATOM   7634 O  O   . PHE D  1 151 ? -1.423  -12.871 -48.329 1.00 11.87 ? 151 PHE D O   1 
ATOM   7635 C  CB  . PHE D  1 151 ? -0.382  -12.667 -51.314 1.00 9.62  ? 151 PHE D CB  1 
ATOM   7636 C  CG  . PHE D  1 151 ? -1.236  -11.534 -51.860 1.00 10.94 ? 151 PHE D CG  1 
ATOM   7637 C  CD1 . PHE D  1 151 ? -0.626  -10.442 -52.517 1.00 12.08 ? 151 PHE D CD1 1 
ATOM   7638 C  CD2 . PHE D  1 151 ? -2.584  -11.604 -51.712 1.00 12.59 ? 151 PHE D CD2 1 
ATOM   7639 C  CE1 . PHE D  1 151 ? -1.401  -9.340  -52.966 1.00 11.98 ? 151 PHE D CE1 1 
ATOM   7640 C  CE2 . PHE D  1 151 ? -3.373  -10.531 -52.103 1.00 11.72 ? 151 PHE D CE2 1 
ATOM   7641 C  CZ  . PHE D  1 151 ? -2.783  -9.466  -52.782 1.00 11.13 ? 151 PHE D CZ  1 
ATOM   7642 N  N   . ASN D  1 152 ? -0.938  -10.656 -48.685 1.00 9.00  ? 152 ASN D N   1 
ATOM   7643 C  CA  . ASN D  1 152 ? -1.819  -10.192 -47.683 1.00 8.59  ? 152 ASN D CA  1 
ATOM   7644 C  C   . ASN D  1 152 ? -2.887  -9.277  -48.284 1.00 9.52  ? 152 ASN D C   1 
ATOM   7645 O  O   . ASN D  1 152 ? -2.602  -8.111  -48.722 1.00 9.77  ? 152 ASN D O   1 
ATOM   7646 C  CB  . ASN D  1 152 ? -1.017  -9.418  -46.611 1.00 7.58  ? 152 ASN D CB  1 
ATOM   7647 C  CG  . ASN D  1 152 ? -1.826  -9.141  -45.329 1.00 8.39  ? 152 ASN D CG  1 
ATOM   7648 O  OD1 . ASN D  1 152 ? -2.936  -8.590  -45.462 1.00 9.76  ? 152 ASN D OD1 1 
ATOM   7649 N  ND2 . ASN D  1 152 ? -1.268  -9.394  -44.162 1.00 9.12  ? 152 ASN D ND2 1 
ATOM   7650 N  N   . PRO D  1 153 ? -4.112  -9.843  -48.472 1.00 10.68 ? 153 PRO D N   1 
ATOM   7651 C  CA  . PRO D  1 153 ? -5.119  -9.020  -49.156 1.00 10.24 ? 153 PRO D CA  1 
ATOM   7652 C  C   . PRO D  1 153 ? -5.537  -7.789  -48.396 1.00 10.96 ? 153 PRO D C   1 
ATOM   7653 O  O   . PRO D  1 153 ? -5.895  -6.811  -49.052 1.00 11.97 ? 153 PRO D O   1 
ATOM   7654 C  CB  . PRO D  1 153 ? -6.354  -9.974  -49.324 1.00 12.05 ? 153 PRO D CB  1 
ATOM   7655 C  CG  . PRO D  1 153 ? -5.775  -11.324 -49.130 1.00 16.01 ? 153 PRO D CG  1 
ATOM   7656 C  CD  . PRO D  1 153 ? -4.588  -11.227 -48.179 1.00 11.61 ? 153 PRO D CD  1 
ATOM   7657 N  N   . SER D  1 154 ? -5.365  -7.787  -47.080 1.00 10.76 ? 154 SER D N   1 
ATOM   7658 C  CA  . SER D  1 154 ? -5.758  -6.576  -46.360 1.00 10.77 ? 154 SER D CA  1 
ATOM   7659 C  C   . SER D  1 154 ? -4.718  -5.470  -46.569 1.00 11.73 ? 154 SER D C   1 
ATOM   7660 O  O   . SER D  1 154 ? -5.119  -4.310  -46.808 1.00 10.82 ? 154 SER D O   1 
ATOM   7661 C  CB  . SER D  1 154 ? -5.868  -6.887  -44.909 1.00 11.28 ? 154 SER D CB  1 
ATOM   7662 O  OG  . SER D  1 154 ? -6.868  -7.877  -44.655 1.00 13.61 ? 154 SER D OG  1 
ATOM   7663 N  N   . TYR D  1 155 ? -3.390  -5.786  -46.444 1.00 9.49  ? 155 TYR D N   1 
ATOM   7664 C  CA  . TYR D  1 155 ? -2.396  -4.737  -46.762 1.00 9.79  ? 155 TYR D CA  1 
ATOM   7665 C  C   . TYR D  1 155 ? -2.527  -4.335  -48.225 1.00 8.94  ? 155 TYR D C   1 
ATOM   7666 O  O   . TYR D  1 155 ? -2.259  -3.171  -48.589 1.00 9.63  ? 155 TYR D O   1 
ATOM   7667 C  CB  . TYR D  1 155 ? -0.963  -5.209  -46.425 1.00 8.65  ? 155 TYR D CB  1 
ATOM   7668 C  CG  . TYR D  1 155 ? -0.627  -5.084  -45.007 1.00 8.08  ? 155 TYR D CG  1 
ATOM   7669 C  CD1 . TYR D  1 155 ? -1.047  -5.999  -44.053 1.00 8.47  ? 155 TYR D CD1 1 
ATOM   7670 C  CD2 . TYR D  1 155 ? 0.119   -3.927  -44.571 1.00 8.84  ? 155 TYR D CD2 1 
ATOM   7671 C  CE1 . TYR D  1 155 ? -0.762  -5.836  -42.699 1.00 8.71  ? 155 TYR D CE1 1 
ATOM   7672 C  CE2 . TYR D  1 155 ? 0.462   -3.777  -43.204 1.00 8.96  ? 155 TYR D CE2 1 
ATOM   7673 C  CZ  . TYR D  1 155 ? -0.022  -4.752  -42.267 1.00 9.55  ? 155 TYR D CZ  1 
ATOM   7674 O  OH  . TYR D  1 155 ? 0.238   -4.627  -40.910 1.00 9.33  ? 155 TYR D OH  1 
ATOM   7675 N  N   . ASP D  1 156 ? -2.965  -5.228  -49.132 1.00 9.43  ? 156 ASP D N   1 
ATOM   7676 C  CA  . ASP D  1 156 ? -3.130  -4.807  -50.517 1.00 9.95  ? 156 ASP D CA  1 
ATOM   7677 C  C   . ASP D  1 156 ? -4.227  -3.729  -50.740 1.00 9.05  ? 156 ASP D C   1 
ATOM   7678 O  O   . ASP D  1 156 ? -4.196  -3.063  -51.780 1.00 10.01 ? 156 ASP D O   1 
ATOM   7679 C  CB  . ASP D  1 156 ? -3.340  -6.001  -51.440 1.00 11.35 ? 156 ASP D CB  1 
ATOM   7680 C  CG  . ASP D  1 156 ? -2.514  -5.898  -52.699 1.00 14.12 ? 156 ASP D CG  1 
ATOM   7681 O  OD1 . ASP D  1 156 ? -1.286  -5.698  -52.595 1.00 12.42 ? 156 ASP D OD1 1 
ATOM   7682 O  OD2 . ASP D  1 156 ? -3.094  -5.996  -53.800 1.00 14.06 ? 156 ASP D OD2 1 
ATOM   7683 N  N   . LYS D  1 157 ? -5.163  -3.596  -49.766 1.00 9.97  ? 157 LYS D N   1 
ATOM   7684 C  CA  . LYS D  1 157 ? -6.167  -2.551  -49.893 1.00 11.15 ? 157 LYS D CA  1 
ATOM   7685 C  C   . LYS D  1 157 ? -5.456  -1.192  -49.845 1.00 12.37 ? 157 LYS D C   1 
ATOM   7686 O  O   . LYS D  1 157 ? -5.986  -0.205  -50.409 1.00 13.25 ? 157 LYS D O   1 
ATOM   7687 C  CB  . LYS D  1 157 ? -7.192  -2.707  -48.753 1.00 11.72 ? 157 LYS D CB  1 
ATOM   7688 C  CG  . LYS D  1 157 ? -8.033  -3.974  -48.934 1.00 12.84 ? 157 LYS D CG  1 
ATOM   7689 C  CD  . LYS D  1 157 ? -8.880  -4.292  -47.684 1.00 18.55 ? 157 LYS D CD  1 
ATOM   7690 C  CE  . LYS D  1 157 ? -9.688  -5.608  -47.889 1.00 18.49 ? 157 LYS D CE  1 
ATOM   7691 N  NZ  . LYS D  1 157 ? -10.422 -6.114  -46.631 1.00 20.29 ? 157 LYS D NZ  1 
ATOM   7692 N  N   . ILE D  1 158 ? -4.260  -1.112  -49.267 1.00 10.22 ? 158 ILE D N   1 
ATOM   7693 C  CA  . ILE D  1 158 ? -3.480  0.136   -49.302 1.00 11.71 ? 158 ILE D CA  1 
ATOM   7694 C  C   . ILE D  1 158 ? -2.609  0.060   -50.509 1.00 9.84  ? 158 ILE D C   1 
ATOM   7695 O  O   . ILE D  1 158 ? -2.529  0.977   -51.337 1.00 9.88  ? 158 ILE D O   1 
ATOM   7696 C  CB  . ILE D  1 158 ? -2.633  0.244   -48.036 1.00 10.94 ? 158 ILE D CB  1 
ATOM   7697 C  CG1 . ILE D  1 158 ? -3.515  0.503   -46.773 1.00 13.83 ? 158 ILE D CG1 1 
ATOM   7698 C  CG2 . ILE D  1 158 ? -1.572  1.353   -48.161 1.00 11.06 ? 158 ILE D CG2 1 
ATOM   7699 C  CD1 . ILE D  1 158 ? -2.779  0.266   -45.494 1.00 16.04 ? 158 ILE D CD1 1 
ATOM   7700 N  N   . PHE D  1 159 ? -1.888  -1.088  -50.688 1.00 10.11 ? 159 PHE D N   1 
ATOM   7701 C  CA  . PHE D  1 159 ? -0.854  -1.094  -51.729 1.00 10.38 ? 159 PHE D CA  1 
ATOM   7702 C  C   . PHE D  1 159 ? -1.334  -0.964  -53.140 1.00 10.47 ? 159 PHE D C   1 
ATOM   7703 O  O   . PHE D  1 159 ? -0.608  -0.506  -54.048 1.00 10.62 ? 159 PHE D O   1 
ATOM   7704 C  CB  . PHE D  1 159 ? 0.051   -2.350  -51.637 1.00 9.18  ? 159 PHE D CB  1 
ATOM   7705 C  CG  . PHE D  1 159 ? 0.762   -2.571  -50.301 1.00 9.98  ? 159 PHE D CG  1 
ATOM   7706 C  CD1 . PHE D  1 159 ? 1.163   -1.529  -49.470 1.00 11.62 ? 159 PHE D CD1 1 
ATOM   7707 C  CD2 . PHE D  1 159 ? 1.072   -3.870  -49.911 1.00 9.54  ? 159 PHE D CD2 1 
ATOM   7708 C  CE1 . PHE D  1 159 ? 1.825   -1.790  -48.272 1.00 12.97 ? 159 PHE D CE1 1 
ATOM   7709 C  CE2 . PHE D  1 159 ? 1.731   -4.132  -48.721 1.00 10.39 ? 159 PHE D CE2 1 
ATOM   7710 C  CZ  . PHE D  1 159 ? 2.109   -3.091  -47.899 1.00 10.69 ? 159 PHE D CZ  1 
ATOM   7711 N  N   . SER D  1 160 ? -2.589  -1.401  -53.408 1.00 11.23 ? 160 SER D N   1 
ATOM   7712 C  CA  . SER D  1 160 ? -3.070  -1.218  -54.801 1.00 10.95 ? 160 SER D CA  1 
ATOM   7713 C  C   . SER D  1 160 ? -3.216  0.187   -55.271 1.00 10.89 ? 160 SER D C   1 
ATOM   7714 O  O   . SER D  1 160 ? -3.277  0.395   -56.487 1.00 13.85 ? 160 SER D O   1 
ATOM   7715 C  CB  . SER D  1 160 ? -4.423  -1.926  -54.948 1.00 12.79 ? 160 SER D CB  1 
ATOM   7716 O  OG  . SER D  1 160 ? -5.392  -1.328  -54.067 1.00 14.39 ? 160 SER D OG  1 
ATOM   7717 N  N   . HIS D  1 161 ? -3.138  1.140   -54.343 1.00 10.46 ? 161 HIS D N   1 
ATOM   7718 C  CA  . HIS D  1 161 ? -3.205  2.544   -54.643 1.00 11.92 ? 161 HIS D CA  1 
ATOM   7719 C  C   . HIS D  1 161 ? -1.880  3.221   -54.808 1.00 12.00 ? 161 HIS D C   1 
ATOM   7720 O  O   . HIS D  1 161 ? -1.865  4.429   -55.149 1.00 12.10 ? 161 HIS D O   1 
ATOM   7721 C  CB  . HIS D  1 161 ? -4.027  3.304   -53.532 1.00 12.88 ? 161 HIS D CB  1 
ATOM   7722 C  CG  . HIS D  1 161 ? -5.410  2.867   -53.464 1.00 14.72 ? 161 HIS D CG  1 
ATOM   7723 N  ND1 . HIS D  1 161 ? -6.392  3.458   -54.248 1.00 17.47 ? 161 HIS D ND1 1 
ATOM   7724 C  CD2 . HIS D  1 161 ? -6.032  1.877   -52.719 1.00 14.12 ? 161 HIS D CD2 1 
ATOM   7725 C  CE1 . HIS D  1 161 ? -7.580  2.862   -53.995 1.00 16.39 ? 161 HIS D CE1 1 
ATOM   7726 N  NE2 . HIS D  1 161 ? -7.368  1.874   -53.065 1.00 16.05 ? 161 HIS D NE2 1 
ATOM   7727 N  N   . LEU D  1 162 ? -0.750  2.506   -54.621 1.00 12.53 ? 162 LEU D N   1 
ATOM   7728 C  CA  . LEU D  1 162 ? 0.567   3.187   -54.582 1.00 13.13 ? 162 LEU D CA  1 
ATOM   7729 C  C   . LEU D  1 162 ? 0.874   3.880   -55.879 1.00 14.39 ? 162 LEU D C   1 
ATOM   7730 O  O   . LEU D  1 162 ? 1.541   4.917   -55.903 1.00 15.44 ? 162 LEU D O   1 
ATOM   7731 C  CB  . LEU D  1 162 ? 1.643   2.104   -54.276 1.00 14.99 ? 162 LEU D CB  1 
ATOM   7732 C  CG  . LEU D  1 162 ? 1.671   1.490   -52.843 1.00 15.09 ? 162 LEU D CG  1 
ATOM   7733 C  CD1 . LEU D  1 162 ? 2.658   0.305   -52.888 1.00 16.62 ? 162 LEU D CD1 1 
ATOM   7734 C  CD2 . LEU D  1 162 ? 2.160   2.514   -51.813 1.00 17.69 ? 162 LEU D CD2 1 
ATOM   7735 N  N   . GLN D  1 163 ? 0.424   3.251   -56.974 1.00 16.70 ? 163 GLN D N   1 
ATOM   7736 C  CA  . GLN D  1 163 ? 0.716   3.871   -58.272 1.00 19.13 ? 163 GLN D CA  1 
ATOM   7737 C  C   . GLN D  1 163 ? 0.047   5.220   -58.569 1.00 19.28 ? 163 GLN D C   1 
ATOM   7738 O  O   . GLN D  1 163 ? 0.310   5.805   -59.621 1.00 23.18 ? 163 GLN D O   1 
ATOM   7739 C  CB  . GLN D  1 163 ? 0.448   2.879   -59.426 1.00 23.29 ? 163 GLN D CB  1 
ATOM   7740 C  CG  . GLN D  1 163 ? 1.521   1.750   -59.601 1.00 30.56 ? 163 GLN D CG  1 
ATOM   7741 C  CD  . GLN D  1 163 ? 3.030   2.153   -59.600 1.00 30.98 ? 163 GLN D CD  1 
ATOM   7742 O  OE1 . GLN D  1 163 ? 3.481   3.110   -60.274 1.00 36.91 ? 163 GLN D OE1 1 
ATOM   7743 N  NE2 . GLN D  1 163 ? 3.825   1.352   -58.884 1.00 27.18 ? 163 GLN D NE2 1 
ATOM   7744 N  N   . HIS D  1 164 ? -0.861  5.651   -57.709 1.00 15.67 ? 164 HIS D N   1 
ATOM   7745 C  CA  . HIS D  1 164 ? -1.516  6.965   -57.740 1.00 15.65 ? 164 HIS D CA  1 
ATOM   7746 C  C   . HIS D  1 164 ? -0.963  8.003   -56.840 1.00 15.29 ? 164 HIS D C   1 
ATOM   7747 O  O   . HIS D  1 164 ? -1.462  9.157   -56.774 1.00 16.52 ? 164 HIS D O   1 
ATOM   7748 C  CB  . HIS D  1 164 ? -3.026  6.784   -57.513 1.00 17.45 ? 164 HIS D CB  1 
ATOM   7749 C  CG  . HIS D  1 164 ? -3.651  5.812   -58.503 1.00 21.90 ? 164 HIS D CG  1 
ATOM   7750 N  ND1 . HIS D  1 164 ? -3.928  6.144   -59.772 1.00 26.01 ? 164 HIS D ND1 1 
ATOM   7751 C  CD2 . HIS D  1 164 ? -4.006  4.472   -58.359 1.00 29.16 ? 164 HIS D CD2 1 
ATOM   7752 C  CE1 . HIS D  1 164 ? -4.451  5.076   -60.432 1.00 26.16 ? 164 HIS D CE1 1 
ATOM   7753 N  NE2 . HIS D  1 164 ? -4.498  4.052   -59.568 1.00 33.92 ? 164 HIS D NE2 1 
ATOM   7754 N  N   . VAL D  1 165 ? 0.061   7.620   -56.032 1.00 12.95 ? 165 VAL D N   1 
ATOM   7755 C  CA  . VAL D  1 165 ? 0.702   8.561   -55.135 1.00 12.62 ? 165 VAL D CA  1 
ATOM   7756 C  C   . VAL D  1 165 ? 2.248   8.480   -55.277 1.00 12.24 ? 165 VAL D C   1 
ATOM   7757 O  O   . VAL D  1 165 ? 2.976   8.593   -54.232 1.00 12.36 ? 165 VAL D O   1 
ATOM   7758 C  CB  . VAL D  1 165 ? 0.295   8.365   -53.628 1.00 14.94 ? 165 VAL D CB  1 
ATOM   7759 C  CG1 . VAL D  1 165 ? -1.189  8.745   -53.394 1.00 15.33 ? 165 VAL D CG1 1 
ATOM   7760 C  CG2 . VAL D  1 165 ? 0.521   6.912   -53.144 1.00 13.49 ? 165 VAL D CG2 1 
ATOM   7761 N  N   . LYS D  1 166 ? 2.685   8.310   -56.533 1.00 12.31 ? 166 LYS D N   1 
ATOM   7762 C  CA  . LYS D  1 166 ? 4.059   8.070   -56.750 1.00 12.40 ? 166 LYS D CA  1 
ATOM   7763 C  C   . LYS D  1 166 ? 4.951   9.207   -56.276 1.00 13.26 ? 166 LYS D C   1 
ATOM   7764 O  O   . LYS D  1 166 ? 6.073   8.956   -55.813 1.00 13.33 ? 166 LYS D O   1 
ATOM   7765 C  CB  . LYS D  1 166 ? 4.224   7.801   -58.237 1.00 14.07 ? 166 LYS D CB  1 
ATOM   7766 C  CG  . LYS D  1 166 ? 5.611   7.726   -58.783 1.00 17.87 ? 166 LYS D CG  1 
ATOM   7767 C  CD  . LYS D  1 166 ? 5.654   7.311   -60.275 1.00 22.79 ? 166 LYS D CD  1 
ATOM   7768 C  CE  . LYS D  1 166 ? 5.130   5.873   -60.518 1.00 22.98 ? 166 LYS D CE  1 
ATOM   7769 N  NZ  . LYS D  1 166 ? 5.821   4.638   -59.948 1.00 25.99 ? 166 LYS D NZ  1 
ATOM   7770 N  N   . TYR D  1 167 ? 4.510   10.444  -56.440 1.00 13.72 ? 167 TYR D N   1 
ATOM   7771 C  CA  . TYR D  1 167 ? 5.365   11.581  -56.126 1.00 13.09 ? 167 TYR D CA  1 
ATOM   7772 C  C   . TYR D  1 167 ? 4.895   12.424  -54.915 1.00 12.27 ? 167 TYR D C   1 
ATOM   7773 O  O   . TYR D  1 167 ? 3.679   12.402  -54.520 1.00 12.21 ? 167 TYR D O   1 
ATOM   7774 C  CB  . TYR D  1 167 ? 5.488   12.480  -57.365 1.00 13.75 ? 167 TYR D CB  1 
ATOM   7775 C  CG  . TYR D  1 167 ? 6.064   11.776  -58.571 1.00 14.62 ? 167 TYR D CG  1 
ATOM   7776 C  CD1 . TYR D  1 167 ? 7.446   11.581  -58.656 1.00 19.74 ? 167 TYR D CD1 1 
ATOM   7777 C  CD2 . TYR D  1 167 ? 5.227   11.359  -59.596 1.00 19.82 ? 167 TYR D CD2 1 
ATOM   7778 C  CE1 . TYR D  1 167 ? 7.989   11.022  -59.806 1.00 20.99 ? 167 TYR D CE1 1 
ATOM   7779 C  CE2 . TYR D  1 167 ? 5.718   10.806  -60.769 1.00 21.22 ? 167 TYR D CE2 1 
ATOM   7780 C  CZ  . TYR D  1 167 ? 7.111   10.603  -60.854 1.00 25.42 ? 167 TYR D CZ  1 
ATOM   7781 O  OH  . TYR D  1 167 ? 7.619   9.981   -62.018 1.00 29.12 ? 167 TYR D OH  1 
ATOM   7782 N  N   . LYS D  1 168 ? 5.803   13.102  -54.250 1.00 12.51 ? 168 LYS D N   1 
ATOM   7783 C  CA  . LYS D  1 168 ? 5.496   13.925  -53.084 1.00 13.21 ? 168 LYS D CA  1 
ATOM   7784 C  C   . LYS D  1 168 ? 4.339   14.843  -53.345 1.00 14.60 ? 168 LYS D C   1 
ATOM   7785 O  O   . LYS D  1 168 ? 4.275   15.498  -54.463 1.00 15.13 ? 168 LYS D O   1 
ATOM   7786 C  CB  . LYS D  1 168 ? 6.706   14.805  -52.640 1.00 13.71 ? 168 LYS D CB  1 
ATOM   7787 C  CG  . LYS D  1 168 ? 6.427   15.566  -51.386 1.00 16.43 ? 168 LYS D CG  1 
ATOM   7788 C  CD  . LYS D  1 168 ? 7.659   16.265  -50.900 1.00 16.71 ? 168 LYS D CD  1 
ATOM   7789 C  CE  . LYS D  1 168 ? 7.360   17.264  -49.803 1.00 22.22 ? 168 LYS D CE  1 
ATOM   7790 N  NZ  . LYS D  1 168 ? 8.637   17.627  -49.095 1.00 27.44 ? 168 LYS D NZ  1 
ATOM   7791 N  N   . GLY D  1 169 ? 3.412   14.862  -52.394 1.00 14.43 ? 169 GLY D N   1 
ATOM   7792 C  CA  . GLY D  1 169 ? 2.240   15.746  -52.553 1.00 15.96 ? 169 GLY D CA  1 
ATOM   7793 C  C   . GLY D  1 169 ? 1.002   15.127  -53.202 1.00 19.25 ? 169 GLY D C   1 
ATOM   7794 O  O   . GLY D  1 169 ? -0.106  15.673  -53.100 1.00 21.01 ? 169 GLY D O   1 
ATOM   7795 N  N   . GLN D  1 170 ? 1.158   14.017  -53.927 1.00 14.37 ? 170 GLN D N   1 
ATOM   7796 C  CA  . GLN D  1 170 ? 0.083   13.294  -54.631 1.00 14.98 ? 170 GLN D CA  1 
ATOM   7797 C  C   . GLN D  1 170 ? -0.806  12.581  -53.576 1.00 15.27 ? 170 GLN D C   1 
ATOM   7798 O  O   . GLN D  1 170 ? -0.339  12.197  -52.475 1.00 15.58 ? 170 GLN D O   1 
ATOM   7799 C  CB  . GLN D  1 170 ? 0.612   12.387  -55.689 1.00 13.50 ? 170 GLN D CB  1 
ATOM   7800 C  CG  . GLN D  1 170 ? 1.289   13.175  -56.846 1.00 16.02 ? 170 GLN D CG  1 
ATOM   7801 C  CD  . GLN D  1 170 ? 1.628   12.256  -58.011 1.00 19.17 ? 170 GLN D CD  1 
ATOM   7802 O  OE1 . GLN D  1 170 ? 1.955   11.093  -57.853 1.00 17.03 ? 170 GLN D OE1 1 
ATOM   7803 N  NE2 . GLN D  1 170 ? 1.442   12.759  -59.246 1.00 20.90 ? 170 GLN D NE2 1 
ATOM   7804 N  N   . GLU D  1 171 ? -2.078  12.500  -53.924 1.00 16.73 ? 171 GLU D N   1 
ATOM   7805 C  CA  . GLU D  1 171 ? -3.116  12.065  -52.976 1.00 15.73 ? 171 GLU D CA  1 
ATOM   7806 C  C   . GLU D  1 171 ? -4.051  11.133  -53.757 1.00 16.82 ? 171 GLU D C   1 
ATOM   7807 O  O   . GLU D  1 171 ? -4.219  11.236  -54.981 1.00 17.56 ? 171 GLU D O   1 
ATOM   7808 C  CB  . GLU D  1 171 ? -3.929  13.258  -52.473 1.00 20.28 ? 171 GLU D CB  1 
ATOM   7809 C  CG  . GLU D  1 171 ? -3.230  14.184  -51.501 1.00 24.39 ? 171 GLU D CG  1 
ATOM   7810 C  CD  . GLU D  1 171 ? -4.120  15.362  -51.102 1.00 28.12 ? 171 GLU D CD  1 
ATOM   7811 O  OE1 . GLU D  1 171 ? -5.147  15.562  -51.766 1.00 36.19 ? 171 GLU D OE1 1 
ATOM   7812 O  OE2 . GLU D  1 171 ? -3.778  16.020  -50.116 1.00 34.82 ? 171 GLU D OE2 1 
ATOM   7813 N  N   . ALA D  1 172 ? -4.589  10.134  -53.078 1.00 14.39 ? 172 ALA D N   1 
ATOM   7814 C  CA  . ALA D  1 172 ? -5.553  9.210   -53.638 1.00 13.96 ? 172 ALA D CA  1 
ATOM   7815 C  C   . ALA D  1 172 ? -6.555  8.875   -52.547 1.00 14.05 ? 172 ALA D C   1 
ATOM   7816 O  O   . ALA D  1 172 ? -6.243  9.049   -51.382 1.00 16.11 ? 172 ALA D O   1 
ATOM   7817 C  CB  . ALA D  1 172 ? -4.882  7.937   -54.126 1.00 15.77 ? 172 ALA D CB  1 
ATOM   7818 N  N   . PHE D  1 173 ? -7.737  8.371   -52.931 1.00 13.26 ? 173 PHE D N   1 
ATOM   7819 C  CA  . PHE D  1 173 ? -8.686  7.913   -51.889 1.00 12.80 ? 173 PHE D CA  1 
ATOM   7820 C  C   . PHE D  1 173 ? -8.732  6.447   -51.867 1.00 13.80 ? 173 PHE D C   1 
ATOM   7821 O  O   . PHE D  1 173 ? -8.715  5.791   -52.896 1.00 16.01 ? 173 PHE D O   1 
ATOM   7822 C  CB  . PHE D  1 173 ? -10.102 8.417   -52.235 1.00 14.67 ? 173 PHE D CB  1 
ATOM   7823 C  CG  . PHE D  1 173 ? -10.339 9.837   -51.776 1.00 16.01 ? 173 PHE D CG  1 
ATOM   7824 C  CD1 . PHE D  1 173 ? -10.283 10.160  -50.387 1.00 18.53 ? 173 PHE D CD1 1 
ATOM   7825 C  CD2 . PHE D  1 173 ? -10.628 10.854  -52.672 1.00 21.59 ? 173 PHE D CD2 1 
ATOM   7826 C  CE1 . PHE D  1 173 ? -10.495 11.452  -49.926 1.00 22.41 ? 173 PHE D CE1 1 
ATOM   7827 C  CE2 . PHE D  1 173 ? -10.867 12.183  -52.183 1.00 23.01 ? 173 PHE D CE2 1 
ATOM   7828 C  CZ  . PHE D  1 173 ? -10.755 12.474  -50.832 1.00 23.01 ? 173 PHE D CZ  1 
ATOM   7829 N  N   . VAL D  1 174 ? -8.808  5.963   -50.652 1.00 12.06 ? 174 VAL D N   1 
ATOM   7830 C  CA  . VAL D  1 174 ? -8.861  4.558   -50.384 1.00 12.40 ? 174 VAL D CA  1 
ATOM   7831 C  C   . VAL D  1 174 ? -10.206 4.234   -49.694 1.00 12.49 ? 174 VAL D C   1 
ATOM   7832 O  O   . VAL D  1 174 ? -10.524 4.863   -48.661 1.00 13.20 ? 174 VAL D O   1 
ATOM   7833 C  CB  . VAL D  1 174 ? -7.736  4.162   -49.393 1.00 13.36 ? 174 VAL D CB  1 
ATOM   7834 C  CG1 . VAL D  1 174 ? -7.833  2.698   -48.971 1.00 12.71 ? 174 VAL D CG1 1 
ATOM   7835 C  CG2 . VAL D  1 174 ? -6.355  4.471   -50.008 1.00 14.02 ? 174 VAL D CG2 1 
ATOM   7836 N  N   . PRO D  1 175 ? -11.027 3.304   -50.309 1.00 11.33 ? 175 PRO D N   1 
ATOM   7837 C  CA  . PRO D  1 175 ? -12.255 2.934   -49.580 1.00 11.89 ? 175 PRO D CA  1 
ATOM   7838 C  C   . PRO D  1 175 ? -12.011 2.414   -48.183 1.00 12.47 ? 175 PRO D C   1 
ATOM   7839 O  O   . PRO D  1 175 ? -11.002 1.761   -47.932 1.00 12.69 ? 175 PRO D O   1 
ATOM   7840 C  CB  . PRO D  1 175 ? -12.856 1.792   -50.407 1.00 13.24 ? 175 PRO D CB  1 
ATOM   7841 C  CG  . PRO D  1 175 ? -12.305 1.972   -51.746 1.00 15.98 ? 175 PRO D CG  1 
ATOM   7842 C  CD  . PRO D  1 175 ? -10.876 2.581   -51.568 1.00 13.04 ? 175 PRO D CD  1 
ATOM   7843 N  N   . GLY D  1 176 ? -12.903 2.656   -47.217 1.00 11.29 ? 176 GLY D N   1 
ATOM   7844 C  CA  . GLY D  1 176 ? -12.681 2.090   -45.896 1.00 10.90 ? 176 GLY D CA  1 
ATOM   7845 C  C   . GLY D  1 176 ? -12.605 0.583   -45.852 1.00 11.78 ? 176 GLY D C   1 
ATOM   7846 O  O   . GLY D  1 176 ? -13.246 -0.118  -46.688 1.00 13.37 ? 176 GLY D O   1 
ATOM   7847 N  N   . PHE D  1 177 ? -11.865 0.135   -44.874 1.00 11.75 ? 177 PHE D N   1 
ATOM   7848 C  CA  . PHE D  1 177 ? -11.792 -1.320  -44.580 1.00 11.19 ? 177 PHE D CA  1 
ATOM   7849 C  C   . PHE D  1 177 ? -11.504 -1.497  -43.127 1.00 12.08 ? 177 PHE D C   1 
ATOM   7850 O  O   . PHE D  1 177 ? -11.318 -0.517  -42.401 1.00 11.54 ? 177 PHE D O   1 
ATOM   7851 C  CB  . PHE D  1 177 ? -10.775 -2.076  -45.485 1.00 12.86 ? 177 PHE D CB  1 
ATOM   7852 C  CG  . PHE D  1 177 ? -9.328  -1.707  -45.245 1.00 11.57 ? 177 PHE D CG  1 
ATOM   7853 C  CD1 . PHE D  1 177 ? -8.769  -0.586  -45.876 1.00 13.35 ? 177 PHE D CD1 1 
ATOM   7854 C  CD2 . PHE D  1 177 ? -8.516  -2.532  -44.434 1.00 14.92 ? 177 PHE D CD2 1 
ATOM   7855 C  CE1 . PHE D  1 177 ? -7.424  -0.229  -45.632 1.00 13.04 ? 177 PHE D CE1 1 
ATOM   7856 C  CE2 . PHE D  1 177 ? -7.162  -2.170  -44.242 1.00 12.59 ? 177 PHE D CE2 1 
ATOM   7857 C  CZ  . PHE D  1 177 ? -6.644  -1.065  -44.861 1.00 14.03 ? 177 PHE D CZ  1 
ATOM   7858 N  N   . ASN D  1 178 ? -11.525 -2.736  -42.608 1.00 12.57 ? 178 ASN D N   1 
ATOM   7859 C  CA  . ASN D  1 178 ? -11.329 -2.892  -41.206 1.00 12.83 ? 178 ASN D CA  1 
ATOM   7860 C  C   . ASN D  1 178 ? -9.809  -2.899  -40.969 1.00 12.42 ? 178 ASN D C   1 
ATOM   7861 O  O   . ASN D  1 178 ? -9.104  -3.902  -41.296 1.00 12.35 ? 178 ASN D O   1 
ATOM   7862 C  CB  . ASN D  1 178 ? -11.918 -4.289  -40.825 1.00 13.87 ? 178 ASN D CB  1 
ATOM   7863 C  CG  . ASN D  1 178 ? -11.758 -4.568  -39.375 1.00 13.10 ? 178 ASN D CG  1 
ATOM   7864 O  OD1 . ASN D  1 178 ? -11.366 -3.741  -38.568 1.00 12.95 ? 178 ASN D OD1 1 
ATOM   7865 N  ND2 . ASN D  1 178 ? -12.187 -5.801  -38.973 1.00 19.55 ? 178 ASN D ND2 1 
ATOM   7866 N  N   . ILE D  1 179 ? -9.357  -1.835  -40.350 1.00 11.07 ? 179 ILE D N   1 
ATOM   7867 C  CA  . ILE D  1 179 ? -7.941  -1.657  -40.039 1.00 10.82 ? 179 ILE D CA  1 
ATOM   7868 C  C   . ILE D  1 179 ? -7.438  -2.728  -39.085 1.00 11.65 ? 179 ILE D C   1 
ATOM   7869 O  O   . ILE D  1 179 ? -6.234  -2.978  -39.011 1.00 10.99 ? 179 ILE D O   1 
ATOM   7870 C  CB  . ILE D  1 179 ? -7.768  -0.207  -39.516 1.00 10.90 ? 179 ILE D CB  1 
ATOM   7871 C  CG1 . ILE D  1 179 ? -8.257  0.835   -40.499 1.00 10.37 ? 179 ILE D CG1 1 
ATOM   7872 C  CG2 . ILE D  1 179 ? -6.273  0.065   -39.086 1.00 10.04 ? 179 ILE D CG2 1 
ATOM   7873 C  CD1 . ILE D  1 179 ? -7.608  0.764   -41.879 1.00 13.94 ? 179 ILE D CD1 1 
ATOM   7874 N  N   . GLU D  1 180 ? -8.318  -3.394  -38.284 1.00 11.16 ? 180 GLU D N   1 
ATOM   7875 C  CA  . GLU D  1 180 ? -7.858  -4.456  -37.405 1.00 12.03 ? 180 GLU D CA  1 
ATOM   7876 C  C   . GLU D  1 180 ? -7.319  -5.634  -38.254 1.00 10.46 ? 180 GLU D C   1 
ATOM   7877 O  O   . GLU D  1 180 ? -6.505  -6.420  -37.681 1.00 11.81 ? 180 GLU D O   1 
ATOM   7878 C  CB  . GLU D  1 180 ? -9.018  -4.899  -36.421 1.00 15.81 ? 180 GLU D CB  1 
ATOM   7879 C  CG  . GLU D  1 180 ? -8.517  -5.681  -35.225 1.00 21.32 ? 180 GLU D CG  1 
ATOM   7880 C  CD  . GLU D  1 180 ? -9.579  -5.798  -34.123 1.00 21.77 ? 180 GLU D CD  1 
ATOM   7881 O  OE1 . GLU D  1 180 ? -10.662 -5.188  -34.229 1.00 21.65 ? 180 GLU D OE1 1 
ATOM   7882 O  OE2 . GLU D  1 180 ? -9.210  -6.458  -33.172 1.00 26.33 ? 180 GLU D OE2 1 
ATOM   7883 N  N   . GLU D  1 181 ? -7.697  -5.694  -39.557 1.00 10.51 ? 181 GLU D N   1 
ATOM   7884 C  CA  . GLU D  1 181 ? -7.117  -6.763  -40.424 1.00 10.38 ? 181 GLU D CA  1 
ATOM   7885 C  C   . GLU D  1 181 ? -5.610  -6.561  -40.673 1.00 11.53 ? 181 GLU D C   1 
ATOM   7886 O  O   . GLU D  1 181 ? -4.918  -7.525  -41.100 1.00 11.47 ? 181 GLU D O   1 
ATOM   7887 C  CB  . GLU D  1 181 ? -7.782  -6.714  -41.725 1.00 12.22 ? 181 GLU D CB  1 
ATOM   7888 C  CG  . GLU D  1 181 ? -9.232  -7.180  -41.688 1.00 13.22 ? 181 GLU D CG  1 
ATOM   7889 C  CD  . GLU D  1 181 ? -9.904  -6.990  -43.068 1.00 17.37 ? 181 GLU D CD  1 
ATOM   7890 O  OE1 . GLU D  1 181 ? -9.216  -6.776  -44.075 1.00 18.84 ? 181 GLU D OE1 1 
ATOM   7891 O  OE2 . GLU D  1 181 ? -11.155 -7.048  -43.144 1.00 18.15 ? 181 GLU D OE2 1 
ATOM   7892 N  N   . LEU D  1 182 ? -5.076  -5.378  -40.360 1.00 10.60 ? 182 LEU D N   1 
ATOM   7893 C  CA  . LEU D  1 182 ? -3.637  -5.138  -40.440 1.00 9.37  ? 182 LEU D CA  1 
ATOM   7894 C  C   . LEU D  1 182 ? -2.886  -5.570  -39.227 1.00 9.70  ? 182 LEU D C   1 
ATOM   7895 O  O   . LEU D  1 182 ? -1.646  -5.590  -39.254 1.00 9.79  ? 182 LEU D O   1 
ATOM   7896 C  CB  . LEU D  1 182 ? -3.380  -3.606  -40.652 1.00 9.52  ? 182 LEU D CB  1 
ATOM   7897 C  CG  . LEU D  1 182 ? -4.032  -3.000  -41.885 1.00 9.17  ? 182 LEU D CG  1 
ATOM   7898 C  CD1 . LEU D  1 182 ? -3.696  -1.474  -42.017 1.00 10.04 ? 182 LEU D CD1 1 
ATOM   7899 C  CD2 . LEU D  1 182 ? -3.769  -3.710  -43.198 1.00 9.18  ? 182 LEU D CD2 1 
ATOM   7900 N  N   . LEU D  1 183 ? -3.530  -5.894  -38.102 1.00 10.18 ? 183 LEU D N   1 
ATOM   7901 C  CA  . LEU D  1 183 ? -2.896  -6.288  -36.912 1.00 10.36 ? 183 LEU D CA  1 
ATOM   7902 C  C   . LEU D  1 183 ? -2.607  -7.812  -36.895 1.00 9.04  ? 183 LEU D C   1 
ATOM   7903 O  O   . LEU D  1 183 ? -3.290  -8.585  -37.563 1.00 11.32 ? 183 LEU D O   1 
ATOM   7904 C  CB  . LEU D  1 183 ? -3.820  -5.982  -35.698 1.00 11.60 ? 183 LEU D CB  1 
ATOM   7905 C  CG  . LEU D  1 183 ? -4.117  -4.469  -35.543 1.00 12.45 ? 183 LEU D CG  1 
ATOM   7906 C  CD1 . LEU D  1 183 ? -4.871  -4.143  -34.235 1.00 13.14 ? 183 LEU D CD1 1 
ATOM   7907 C  CD2 . LEU D  1 183 ? -2.925  -3.541  -35.630 1.00 13.74 ? 183 LEU D CD2 1 
ATOM   7908 N  N   . PRO D  1 184 ? -1.616  -8.212  -36.164 1.00 10.35 ? 184 PRO D N   1 
ATOM   7909 C  CA  . PRO D  1 184 ? -1.230  -9.672  -36.060 1.00 11.71 ? 184 PRO D CA  1 
ATOM   7910 C  C   . PRO D  1 184 ? -2.088  -10.475 -35.114 1.00 13.78 ? 184 PRO D C   1 
ATOM   7911 O  O   . PRO D  1 184 ? -3.004  -9.954  -34.454 1.00 13.88 ? 184 PRO D O   1 
ATOM   7912 C  CB  . PRO D  1 184 ? 0.233   -9.561  -35.529 1.00 12.51 ? 184 PRO D CB  1 
ATOM   7913 C  CG  . PRO D  1 184 ? 0.180   -8.303  -34.618 1.00 12.31 ? 184 PRO D CG  1 
ATOM   7914 C  CD  . PRO D  1 184 ? -0.727  -7.368  -35.379 1.00 10.06 ? 184 PRO D CD  1 
ATOM   7915 N  N   A GLU D  1 185 ? -1.777  -11.776 -35.103 0.50 15.07 ? 185 GLU D N   1 
ATOM   7916 N  N   B GLU D  1 185 ? -1.769  -11.767 -35.071 0.50 14.93 ? 185 GLU D N   1 
ATOM   7917 C  CA  A GLU D  1 185 ? -2.303  -12.682 -34.110 0.50 16.46 ? 185 GLU D CA  1 
ATOM   7918 C  CA  B GLU D  1 185 ? -2.388  -12.621 -34.103 0.50 16.09 ? 185 GLU D CA  1 
ATOM   7919 C  C   A GLU D  1 185 ? -1.957  -12.249 -32.699 0.50 14.28 ? 185 GLU D C   1 
ATOM   7920 C  C   B GLU D  1 185 ? -1.962  -12.258 -32.703 0.50 14.05 ? 185 GLU D C   1 
ATOM   7921 O  O   A GLU D  1 185 ? -0.877  -11.689 -32.445 0.50 14.95 ? 185 GLU D O   1 
ATOM   7922 O  O   B GLU D  1 185 ? -0.845  -11.751 -32.463 0.50 14.45 ? 185 GLU D O   1 
ATOM   7923 C  CB  A GLU D  1 185 ? -1.739  -14.094 -34.360 0.50 17.94 ? 185 GLU D CB  1 
ATOM   7924 C  CB  B GLU D  1 185 ? -2.022  -14.075 -34.406 0.50 17.58 ? 185 GLU D CB  1 
ATOM   7925 C  CG  A GLU D  1 185 ? -2.191  -14.710 -35.675 0.50 19.36 ? 185 GLU D CG  1 
ATOM   7926 C  CG  B GLU D  1 185 ? -2.395  -14.462 -35.813 0.50 18.78 ? 185 GLU D CG  1 
ATOM   7927 C  CD  A GLU D  1 185 ? -1.891  -16.215 -35.763 0.50 23.41 ? 185 GLU D CD  1 
ATOM   7928 C  CD  B GLU D  1 185 ? -3.881  -14.398 -36.030 0.50 23.01 ? 185 GLU D CD  1 
ATOM   7929 O  OE1 A GLU D  1 185 ? -2.393  -16.987 -34.930 0.50 26.39 ? 185 GLU D OE1 1 
ATOM   7930 O  OE1 B GLU D  1 185 ? -4.622  -15.132 -35.352 0.50 25.45 ? 185 GLU D OE1 1 
ATOM   7931 O  OE2 A GLU D  1 185 ? -1.145  -16.622 -36.678 0.50 29.69 ? 185 GLU D OE2 1 
ATOM   7932 O  OE2 B GLU D  1 185 ? -4.333  -13.626 -36.881 0.50 27.81 ? 185 GLU D OE2 1 
ATOM   7933 N  N   . ARG D  1 186 ? -2.861  -12.541 -31.744 1.00 13.60 ? 186 ARG D N   1 
ATOM   7934 C  CA  . ARG D  1 186 ? -2.552  -12.443 -30.324 1.00 14.34 ? 186 ARG D CA  1 
ATOM   7935 C  C   . ARG D  1 186 ? -2.064  -11.057 -29.951 1.00 11.72 ? 186 ARG D C   1 
ATOM   7936 O  O   . ARG D  1 186 ? -0.963  -10.868 -29.363 1.00 12.70 ? 186 ARG D O   1 
ATOM   7937 C  CB  . ARG D  1 186 ? -1.613  -13.571 -29.859 1.00 17.87 ? 186 ARG D CB  1 
ATOM   7938 C  CG  . ARG D  1 186 ? -2.226  -14.950 -30.102 1.00 22.23 ? 186 ARG D CG  1 
ATOM   7939 C  CD  . ARG D  1 186 ? -1.346  -16.103 -29.587 1.00 26.87 ? 186 ARG D CD  1 
ATOM   7940 N  NE  . ARG D  1 186 ? -0.240  -16.278 -30.520 1.00 30.50 ? 186 ARG D NE  1 
ATOM   7941 C  CZ  . ARG D  1 186 ? -0.377  -16.767 -31.769 1.00 35.48 ? 186 ARG D CZ  1 
ATOM   7942 N  NH1 . ARG D  1 186 ? -1.581  -17.134 -32.223 1.00 34.18 ? 186 ARG D NH1 1 
ATOM   7943 N  NH2 . ARG D  1 186 ? 0.687   -16.862 -32.575 1.00 38.48 ? 186 ARG D NH2 1 
ATOM   7944 N  N   . THR D  1 187 ? -2.892  -10.068 -30.318 1.00 11.32 ? 187 THR D N   1 
ATOM   7945 C  CA  . THR D  1 187 ? -2.531  -8.703  -29.959 1.00 12.98 ? 187 THR D CA  1 
ATOM   7946 C  C   . THR D  1 187 ? -2.414  -8.423  -28.461 1.00 12.49 ? 187 THR D C   1 
ATOM   7947 O  O   . THR D  1 187 ? -1.823  -7.370  -28.045 1.00 12.80 ? 187 THR D O   1 
ATOM   7948 C  CB  . THR D  1 187 ? -3.535  -7.707  -30.541 1.00 11.81 ? 187 THR D CB  1 
ATOM   7949 O  OG1 . THR D  1 187 ? -4.876  -8.045  -30.098 1.00 16.11 ? 187 THR D OG1 1 
ATOM   7950 C  CG2 . THR D  1 187 ? -3.506  -7.697  -32.143 1.00 13.80 ? 187 THR D CG2 1 
ATOM   7951 N  N   . ALA D  1 188 ? -2.905  -9.321  -27.594 1.00 12.52 ? 188 ALA D N   1 
ATOM   7952 C  CA  . ALA D  1 188 ? -2.676  -9.138  -26.205 1.00 11.56 ? 188 ALA D CA  1 
ATOM   7953 C  C   . ALA D  1 188 ? -1.183  -9.252  -25.781 1.00 10.64 ? 188 ALA D C   1 
ATOM   7954 O  O   . ALA D  1 188 ? -0.785  -8.911  -24.664 1.00 11.56 ? 188 ALA D O   1 
ATOM   7955 C  CB  . ALA D  1 188 ? -3.492  -10.205 -25.392 1.00 12.69 ? 188 ALA D CB  1 
ATOM   7956 N  N   . GLU D  1 189 ? -0.401  -9.849  -26.678 1.00 11.69 ? 189 GLU D N   1 
ATOM   7957 C  CA  . GLU D  1 189 ? 1.060   -10.054 -26.444 1.00 11.46 ? 189 GLU D CA  1 
ATOM   7958 C  C   . GLU D  1 189 ? 1.853   -8.927  -27.203 1.00 8.05  ? 189 GLU D C   1 
ATOM   7959 O  O   . GLU D  1 189 ? 1.824   -8.822  -28.441 1.00 10.46 ? 189 GLU D O   1 
ATOM   7960 C  CB  . GLU D  1 189 ? 1.473   -11.392 -27.052 1.00 12.45 ? 189 GLU D CB  1 
ATOM   7961 C  CG  . GLU D  1 189 ? 0.665   -12.480 -26.320 1.00 13.95 ? 189 GLU D CG  1 
ATOM   7962 C  CD  . GLU D  1 189 ? 1.115   -13.876 -26.767 1.00 20.70 ? 189 GLU D CD  1 
ATOM   7963 O  OE1 . GLU D  1 189 ? 2.218   -14.092 -27.286 1.00 19.38 ? 189 GLU D OE1 1 
ATOM   7964 O  OE2 . GLU D  1 189 ? 0.317   -14.823 -26.498 1.00 25.12 ? 189 GLU D OE2 1 
ATOM   7965 N  N   . TYR D  1 190 ? 2.500   -8.133  -26.357 1.00 8.94  ? 190 TYR D N   1 
ATOM   7966 C  CA  . TYR D  1 190 ? 3.176   -6.913  -26.924 1.00 8.36  ? 190 TYR D CA  1 
ATOM   7967 C  C   . TYR D  1 190 ? 4.237   -6.443  -26.039 1.00 9.53  ? 190 TYR D C   1 
ATOM   7968 O  O   . TYR D  1 190 ? 4.351   -6.796  -24.838 1.00 9.73  ? 190 TYR D O   1 
ATOM   7969 C  CB  . TYR D  1 190 ? 2.163   -5.776  -27.179 1.00 9.13  ? 190 TYR D CB  1 
ATOM   7970 C  CG  . TYR D  1 190 ? 1.353   -5.330  -25.965 1.00 9.69  ? 190 TYR D CG  1 
ATOM   7971 C  CD1 . TYR D  1 190 ? 1.907   -4.428  -25.073 1.00 9.48  ? 190 TYR D CD1 1 
ATOM   7972 C  CD2 . TYR D  1 190 ? 0.039   -5.807  -25.794 1.00 9.36  ? 190 TYR D CD2 1 
ATOM   7973 C  CE1 . TYR D  1 190 ? 1.193   -3.998  -23.948 1.00 10.31 ? 190 TYR D CE1 1 
ATOM   7974 C  CE2 . TYR D  1 190 ? -0.701  -5.358  -24.642 1.00 10.80 ? 190 TYR D CE2 1 
ATOM   7975 C  CZ  . TYR D  1 190 ? -0.096  -4.477  -23.768 1.00 11.44 ? 190 TYR D CZ  1 
ATOM   7976 O  OH  . TYR D  1 190 ? -0.855  -3.987  -22.658 1.00 10.89 ? 190 TYR D OH  1 
ATOM   7977 N  N   . TYR D  1 191 ? 5.123   -5.630  -26.650 1.00 8.32  ? 191 TYR D N   1 
ATOM   7978 C  CA  . TYR D  1 191 ? 6.163   -4.900  -25.977 1.00 8.58  ? 191 TYR D CA  1 
ATOM   7979 C  C   . TYR D  1 191 ? 5.694   -3.431  -25.789 1.00 7.76  ? 191 TYR D C   1 
ATOM   7980 O  O   . TYR D  1 191 ? 5.002   -2.896  -26.704 1.00 8.85  ? 191 TYR D O   1 
ATOM   7981 C  CB  . TYR D  1 191 ? 7.413   -4.797  -26.911 1.00 8.01  ? 191 TYR D CB  1 
ATOM   7982 C  CG  . TYR D  1 191 ? 7.966   -6.106  -27.400 1.00 8.35  ? 191 TYR D CG  1 
ATOM   7983 C  CD1 . TYR D  1 191 ? 8.970   -6.790  -26.684 1.00 9.31  ? 191 TYR D CD1 1 
ATOM   7984 C  CD2 . TYR D  1 191 ? 7.521   -6.633  -28.648 1.00 9.58  ? 191 TYR D CD2 1 
ATOM   7985 C  CE1 . TYR D  1 191 ? 9.456   -7.984  -27.189 1.00 9.75  ? 191 TYR D CE1 1 
ATOM   7986 C  CE2 . TYR D  1 191 ? 8.094   -7.848  -29.156 1.00 9.98  ? 191 TYR D CE2 1 
ATOM   7987 C  CZ  . TYR D  1 191 ? 9.089   -8.448  -28.399 1.00 9.98  ? 191 TYR D CZ  1 
ATOM   7988 O  OH  . TYR D  1 191 ? 9.662   -9.609  -28.882 1.00 12.83 ? 191 TYR D OH  1 
ATOM   7989 N  N   . ARG D  1 192 ? 6.030   -2.832  -24.647 1.00 9.36  ? 192 ARG D N   1 
ATOM   7990 C  CA  . ARG D  1 192 ? 5.609   -1.448  -24.357 1.00 8.89  ? 192 ARG D CA  1 
ATOM   7991 C  C   . ARG D  1 192 ? 6.810   -0.662  -23.821 1.00 7.74  ? 192 ARG D C   1 
ATOM   7992 O  O   . ARG D  1 192 ? 7.523   -1.098  -22.918 1.00 9.93  ? 192 ARG D O   1 
ATOM   7993 C  CB  . ARG D  1 192 ? 4.537   -1.506  -23.254 1.00 9.49  ? 192 ARG D CB  1 
ATOM   7994 C  CG  . ARG D  1 192 ? 4.236   -0.238  -22.457 1.00 13.47 ? 192 ARG D CG  1 
ATOM   7995 C  CD  . ARG D  1 192 ? 3.544   0.752   -23.377 1.00 13.50 ? 192 ARG D CD  1 
ATOM   7996 N  NE  . ARG D  1 192 ? 2.384   0.268   -24.119 1.00 14.53 ? 192 ARG D NE  1 
ATOM   7997 C  CZ  . ARG D  1 192 ? 1.206   -0.129  -23.624 1.00 14.18 ? 192 ARG D CZ  1 
ATOM   7998 N  NH1 . ARG D  1 192 ? 0.934   0.066   -22.278 1.00 18.67 ? 192 ARG D NH1 1 
ATOM   7999 N  NH2 . ARG D  1 192 ? 0.267   -0.677  -24.414 1.00 14.05 ? 192 ARG D NH2 1 
ATOM   8000 N  N   . TYR D  1 193 ? 7.024   0.504   -24.414 1.00 8.71  ? 193 TYR D N   1 
ATOM   8001 C  CA  . TYR D  1 193 ? 8.084   1.342   -23.815 1.00 8.26  ? 193 TYR D CA  1 
ATOM   8002 C  C   . TYR D  1 193 ? 7.803   2.806   -24.147 1.00 8.39  ? 193 TYR D C   1 
ATOM   8003 O  O   . TYR D  1 193 ? 7.014   3.133   -25.023 1.00 9.25  ? 193 TYR D O   1 
ATOM   8004 C  CB  . TYR D  1 193 ? 9.499   0.936   -24.329 1.00 9.63  ? 193 TYR D CB  1 
ATOM   8005 C  CG  . TYR D  1 193 ? 9.829   1.306   -25.775 1.00 8.90  ? 193 TYR D CG  1 
ATOM   8006 C  CD1 . TYR D  1 193 ? 9.365   0.540   -26.867 1.00 8.92  ? 193 TYR D CD1 1 
ATOM   8007 C  CD2 . TYR D  1 193 ? 10.573  2.412   -26.007 1.00 9.40  ? 193 TYR D CD2 1 
ATOM   8008 C  CE1 . TYR D  1 193 ? 9.615   0.958   -28.160 1.00 9.29  ? 193 TYR D CE1 1 
ATOM   8009 C  CE2 . TYR D  1 193 ? 10.868  2.851   -27.310 1.00 8.43  ? 193 TYR D CE2 1 
ATOM   8010 C  CZ  . TYR D  1 193 ? 10.387  2.122   -28.358 1.00 8.36  ? 193 TYR D CZ  1 
ATOM   8011 O  OH  . TYR D  1 193 ? 10.689  2.523   -29.645 1.00 8.42  ? 193 TYR D OH  1 
ATOM   8012 N  N   . ARG D  1 194 ? 8.569   3.625   -23.491 1.00 8.80  ? 194 ARG D N   1 
ATOM   8013 C  CA  . ARG D  1 194 ? 8.471   5.153   -23.666 1.00 9.40  ? 194 ARG D CA  1 
ATOM   8014 C  C   . ARG D  1 194 ? 9.516   5.581   -24.635 1.00 8.25  ? 194 ARG D C   1 
ATOM   8015 O  O   . ARG D  1 194 ? 10.726  5.323   -24.465 1.00 10.38 ? 194 ARG D O   1 
ATOM   8016 C  CB  . ARG D  1 194 ? 8.721   5.884   -22.336 1.00 12.31 ? 194 ARG D CB  1 
ATOM   8017 C  CG  . ARG D  1 194 ? 7.680   5.523   -21.283 1.00 16.46 ? 194 ARG D CG  1 
ATOM   8018 C  CD  . ARG D  1 194 ? 6.451   6.333   -21.543 1.00 23.32 ? 194 ARG D CD  1 
ATOM   8019 N  NE  . ARG D  1 194 ? 5.454   6.006   -20.511 1.00 31.96 ? 194 ARG D NE  1 
ATOM   8020 C  CZ  . ARG D  1 194 ? 4.407   6.787   -20.268 1.00 35.32 ? 194 ARG D CZ  1 
ATOM   8021 N  NH1 . ARG D  1 194 ? 4.266   7.923   -20.943 1.00 31.74 ? 194 ARG D NH1 1 
ATOM   8022 N  NH2 . ARG D  1 194 ? 3.511   6.421   -19.356 1.00 38.39 ? 194 ARG D NH2 1 
ATOM   8023 N  N   . GLY D  1 195 ? 9.069   6.218   -25.705 1.00 8.39  ? 195 GLY D N   1 
ATOM   8024 C  CA  . GLY D  1 195 ? 10.047  6.683   -26.699 1.00 8.61  ? 195 GLY D CA  1 
ATOM   8025 C  C   . GLY D  1 195 ? 9.587   7.907   -27.402 1.00 9.11  ? 195 GLY D C   1 
ATOM   8026 O  O   . GLY D  1 195 ? 9.003   8.833   -26.859 1.00 9.56  ? 195 GLY D O   1 
ATOM   8027 N  N   . SER D  1 196 ? 9.913   7.931   -28.669 1.00 7.70  ? 196 SER D N   1 
ATOM   8028 C  CA  . SER D  1 196 ? 9.852   9.203   -29.419 1.00 8.96  ? 196 SER D CA  1 
ATOM   8029 C  C   . SER D  1 196 ? 9.267   8.959   -30.818 1.00 8.52  ? 196 SER D C   1 
ATOM   8030 O  O   . SER D  1 196 ? 9.111   7.786   -31.311 1.00 8.03  ? 196 SER D O   1 
ATOM   8031 C  CB  . SER D  1 196 ? 11.290  9.772   -29.566 1.00 9.49  ? 196 SER D CB  1 
ATOM   8032 O  OG  . SER D  1 196 ? 12.028  9.091   -30.637 1.00 8.16  ? 196 SER D OG  1 
ATOM   8033 N  N   . LEU D  1 197 ? 8.961   10.016  -31.528 1.00 8.16  ? 197 LEU D N   1 
ATOM   8034 C  CA  . LEU D  1 197 ? 8.780   9.896   -33.005 1.00 7.92  ? 197 LEU D CA  1 
ATOM   8035 C  C   . LEU D  1 197 ? 10.079  9.356   -33.618 1.00 7.15  ? 197 LEU D C   1 
ATOM   8036 O  O   . LEU D  1 197 ? 11.170  9.751   -33.197 1.00 8.65  ? 197 LEU D O   1 
ATOM   8037 C  CB  . LEU D  1 197 ? 8.534   11.340  -33.617 1.00 8.34  ? 197 LEU D CB  1 
ATOM   8038 C  CG  . LEU D  1 197 ? 7.133   11.908  -33.518 1.00 10.04 ? 197 LEU D CG  1 
ATOM   8039 C  CD1 . LEU D  1 197 ? 6.840   12.429  -32.103 1.00 12.60 ? 197 LEU D CD1 1 
ATOM   8040 C  CD2 . LEU D  1 197 ? 7.017   13.053  -34.543 1.00 11.80 ? 197 LEU D CD2 1 
ATOM   8041 N  N   . THR D  1 198 ? 9.965   8.476   -34.596 1.00 7.42  ? 198 THR D N   1 
ATOM   8042 C  CA  . THR D  1 198 ? 11.193  8.039   -35.275 1.00 8.14  ? 198 THR D CA  1 
ATOM   8043 C  C   . THR D  1 198 ? 11.615  8.863   -36.424 1.00 7.51  ? 198 THR D C   1 
ATOM   8044 O  O   . THR D  1 198 ? 12.645  8.573   -37.093 1.00 8.77  ? 198 THR D O   1 
ATOM   8045 C  CB  . THR D  1 198 ? 11.062  6.605   -35.789 1.00 6.46  ? 198 THR D CB  1 
ATOM   8046 O  OG1 . THR D  1 198 ? 10.064  6.617   -36.798 1.00 6.58  ? 198 THR D OG1 1 
ATOM   8047 C  CG2 . THR D  1 198 ? 10.609  5.611   -34.677 1.00 7.86  ? 198 THR D CG2 1 
ATOM   8048 N  N   . THR D  1 199 ? 10.857  9.917   -36.649 1.00 7.70  ? 199 THR D N   1 
ATOM   8049 C  CA  . THR D  1 199 ? 11.198  10.928  -37.676 1.00 7.85  ? 199 THR D CA  1 
ATOM   8050 C  C   . THR D  1 199 ? 11.316  12.267  -36.997 1.00 8.27  ? 199 THR D C   1 
ATOM   8051 O  O   . THR D  1 199 ? 10.615  12.509  -36.032 1.00 9.08  ? 199 THR D O   1 
ATOM   8052 C  CB  . THR D  1 199 ? 10.027  10.994  -38.692 1.00 9.31  ? 199 THR D CB  1 
ATOM   8053 O  OG1 . THR D  1 199 ? 8.773   11.164  -38.017 1.00 12.60 ? 199 THR D OG1 1 
ATOM   8054 C  CG2 . THR D  1 199 ? 9.887   9.657   -39.469 1.00 10.24 ? 199 THR D CG2 1 
ATOM   8055 N  N   . PRO D  1 200 ? 12.010  13.208  -37.656 1.00 8.43  ? 200 PRO D N   1 
ATOM   8056 C  CA  . PRO D  1 200 ? 11.987  14.584  -37.137 1.00 8.76  ? 200 PRO D CA  1 
ATOM   8057 C  C   . PRO D  1 200 ? 10.551  15.078  -36.944 1.00 8.91  ? 200 PRO D C   1 
ATOM   8058 O  O   . PRO D  1 200 ? 9.703   14.843  -37.799 1.00 10.16 ? 200 PRO D O   1 
ATOM   8059 C  CB  . PRO D  1 200 ? 12.677  15.343  -38.309 1.00 7.53  ? 200 PRO D CB  1 
ATOM   8060 C  CG  . PRO D  1 200 ? 13.718  14.336  -38.766 1.00 8.80  ? 200 PRO D CG  1 
ATOM   8061 C  CD  . PRO D  1 200 ? 12.904  13.001  -38.836 1.00 7.83  ? 200 PRO D CD  1 
ATOM   8062 N  N   . PRO D  1 201 ? 10.277  15.817  -35.863 1.00 8.62  ? 201 PRO D N   1 
ATOM   8063 C  CA  . PRO D  1 201 ? 11.259  16.324  -34.939 1.00 8.26  ? 201 PRO D CA  1 
ATOM   8064 C  C   . PRO D  1 201 ? 11.669  15.438  -33.788 1.00 9.64  ? 201 PRO D C   1 
ATOM   8065 O  O   . PRO D  1 201 ? 12.300  15.864  -32.844 1.00 9.66  ? 201 PRO D O   1 
ATOM   8066 C  CB  . PRO D  1 201 ? 10.530  17.587  -34.381 1.00 9.69  ? 201 PRO D CB  1 
ATOM   8067 C  CG  . PRO D  1 201 ? 9.408   17.867  -35.287 1.00 10.91 ? 201 PRO D CG  1 
ATOM   8068 C  CD  . PRO D  1 201 ? 8.968   16.500  -35.705 1.00 9.99  ? 201 PRO D CD  1 
ATOM   8069 N  N   . CYS D  1 202 ? 11.264  14.153  -33.822 1.00 8.46  ? 202 CYS D N   1 
ATOM   8070 C  CA  . CYS D  1 202 ? 11.788  13.185  -32.873 1.00 9.16  ? 202 CYS D CA  1 
ATOM   8071 C  C   . CYS D  1 202 ? 11.349  13.443  -31.413 1.00 8.57  ? 202 CYS D C   1 
ATOM   8072 O  O   . CYS D  1 202 ? 12.020  13.048  -30.491 1.00 8.74  ? 202 CYS D O   1 
ATOM   8073 C  CB  . CYS D  1 202 ? 13.329  13.056  -32.877 1.00 9.17  ? 202 CYS D CB  1 
ATOM   8074 S  SG  . CYS D  1 202 ? 14.075  12.695  -34.498 1.00 8.88  ? 202 CYS D SG  1 
ATOM   8075 N  N   . ASN D  1 203 ? 10.198  14.039  -31.262 1.00 9.67  ? 203 ASN D N   1 
ATOM   8076 C  CA  . ASN D  1 203 ? 9.828   14.443  -29.897 1.00 9.91  ? 203 ASN D CA  1 
ATOM   8077 C  C   . ASN D  1 203 ? 9.669   13.212  -29.048 1.00 9.42  ? 203 ASN D C   1 
ATOM   8078 O  O   . ASN D  1 203 ? 9.058   12.211  -29.512 1.00 8.73  ? 203 ASN D O   1 
ATOM   8079 C  CB  . ASN D  1 203 ? 8.512   15.222  -29.908 1.00 11.07 ? 203 ASN D CB  1 
ATOM   8080 C  CG  . ASN D  1 203 ? 8.574   16.355  -30.916 1.00 13.78 ? 203 ASN D CG  1 
ATOM   8081 O  OD1 . ASN D  1 203 ? 8.444   16.168  -32.118 1.00 12.71 ? 203 ASN D OD1 1 
ATOM   8082 N  ND2 . ASN D  1 203 ? 8.953   17.486  -30.418 1.00 16.24 ? 203 ASN D ND2 1 
ATOM   8083 N  N   . PRO D  1 204 ? 10.121  13.247  -27.797 1.00 9.49  ? 204 PRO D N   1 
ATOM   8084 C  CA  . PRO D  1 204 ? 10.000  12.079  -26.893 1.00 9.27  ? 204 PRO D CA  1 
ATOM   8085 C  C   . PRO D  1 204 ? 8.617   11.958  -26.196 1.00 9.44  ? 204 PRO D C   1 
ATOM   8086 O  O   . PRO D  1 204 ? 8.535   12.094  -24.920 1.00 11.36 ? 204 PRO D O   1 
ATOM   8087 C  CB  . PRO D  1 204 ? 11.166  12.290  -25.876 1.00 9.43  ? 204 PRO D CB  1 
ATOM   8088 C  CG  . PRO D  1 204 ? 11.205  13.821  -25.775 1.00 10.10 ? 204 PRO D CG  1 
ATOM   8089 C  CD  . PRO D  1 204 ? 10.993  14.296  -27.206 1.00 9.31  ? 204 PRO D CD  1 
ATOM   8090 N  N   . THR D  1 205 ? 7.591   11.812  -27.016 1.00 8.35  ? 205 THR D N   1 
ATOM   8091 C  CA  . THR D  1 205 ? 6.220   11.975  -26.601 1.00 8.98  ? 205 THR D CA  1 
ATOM   8092 C  C   . THR D  1 205 ? 5.366   10.763  -26.937 1.00 9.43  ? 205 THR D C   1 
ATOM   8093 O  O   . THR D  1 205 ? 4.148   10.873  -26.914 1.00 9.36  ? 205 THR D O   1 
ATOM   8094 C  CB  . THR D  1 205 ? 5.590   13.196  -27.276 1.00 10.02 ? 205 THR D CB  1 
ATOM   8095 O  OG1 . THR D  1 205 ? 5.767   13.052  -28.724 1.00 11.72 ? 205 THR D OG1 1 
ATOM   8096 C  CG2 . THR D  1 205 ? 6.298   14.567  -26.799 1.00 10.27 ? 205 THR D CG2 1 
ATOM   8097 N  N   . VAL D  1 206 ? 6.019   9.656   -27.272 1.00 8.94  ? 206 VAL D N   1 
ATOM   8098 C  CA  . VAL D  1 206 ? 5.305   8.511   -27.807 1.00 9.11  ? 206 VAL D CA  1 
ATOM   8099 C  C   . VAL D  1 206 ? 5.334   7.315   -26.829 1.00 8.33  ? 206 VAL D C   1 
ATOM   8100 O  O   . VAL D  1 206 ? 6.381   6.887   -26.428 1.00 9.57  ? 206 VAL D O   1 
ATOM   8101 C  CB  . VAL D  1 206 ? 5.936   8.060   -29.146 1.00 8.20  ? 206 VAL D CB  1 
ATOM   8102 C  CG1 . VAL D  1 206 ? 5.145   6.902   -29.677 1.00 8.90  ? 206 VAL D CG1 1 
ATOM   8103 C  CG2 . VAL D  1 206 ? 5.888   9.163   -30.179 1.00 10.25 ? 206 VAL D CG2 1 
ATOM   8104 N  N   . LEU D  1 207 ? 4.140   6.790   -26.551 1.00 8.36  ? 207 LEU D N   1 
ATOM   8105 C  CA  . LEU D  1 207 ? 4.007   5.504   -25.815 1.00 9.48  ? 207 LEU D CA  1 
ATOM   8106 C  C   . LEU D  1 207 ? 3.910   4.476   -26.939 1.00 7.38  ? 207 LEU D C   1 
ATOM   8107 O  O   . LEU D  1 207 ? 2.971   4.441   -27.725 1.00 8.69  ? 207 LEU D O   1 
ATOM   8108 C  CB  . LEU D  1 207 ? 2.712   5.535   -25.018 1.00 12.62 ? 207 LEU D CB  1 
ATOM   8109 C  CG  . LEU D  1 207 ? 2.570   4.287   -24.085 1.00 16.11 ? 207 LEU D CG  1 
ATOM   8110 C  CD1 . LEU D  1 207 ? 3.770   4.242   -23.114 1.00 18.42 ? 207 LEU D CD1 1 
ATOM   8111 C  CD2 . LEU D  1 207 ? 1.223   4.448   -23.388 1.00 21.85 ? 207 LEU D CD2 1 
ATOM   8112 N  N   . TRP D  1 208 ? 4.927   3.651   -26.998 1.00 7.87  ? 208 TRP D N   1 
ATOM   8113 C  CA  . TRP D  1 208 ? 5.015   2.618   -28.031 1.00 7.60  ? 208 TRP D CA  1 
ATOM   8114 C  C   . TRP D  1 208 ? 4.452   1.293   -27.599 1.00 7.95  ? 208 TRP D C   1 
ATOM   8115 O  O   . TRP D  1 208 ? 4.751   0.848   -26.447 1.00 9.24  ? 208 TRP D O   1 
ATOM   8116 C  CB  . TRP D  1 208 ? 6.548   2.394   -28.406 1.00 7.74  ? 208 TRP D CB  1 
ATOM   8117 C  CG  . TRP D  1 208 ? 7.038   3.449   -29.341 1.00 8.85  ? 208 TRP D CG  1 
ATOM   8118 C  CD1 . TRP D  1 208 ? 7.733   4.607   -29.036 1.00 9.55  ? 208 TRP D CD1 1 
ATOM   8119 C  CD2 . TRP D  1 208 ? 6.854   3.478   -30.789 1.00 8.30  ? 208 TRP D CD2 1 
ATOM   8120 N  NE1 . TRP D  1 208 ? 7.997   5.330   -30.169 1.00 8.72  ? 208 TRP D NE1 1 
ATOM   8121 C  CE2 . TRP D  1 208 ? 7.499   4.704   -31.256 1.00 8.05  ? 208 TRP D CE2 1 
ATOM   8122 C  CE3 . TRP D  1 208 ? 6.254   2.633   -31.707 1.00 8.30  ? 208 TRP D CE3 1 
ATOM   8123 C  CZ2 . TRP D  1 208 ? 7.522   5.053   -32.587 1.00 7.70  ? 208 TRP D CZ2 1 
ATOM   8124 C  CZ3 . TRP D  1 208 ? 6.286   2.995   -33.054 1.00 8.75  ? 208 TRP D CZ3 1 
ATOM   8125 C  CH2 . TRP D  1 208 ? 6.907   4.173   -33.480 1.00 8.91  ? 208 TRP D CH2 1 
ATOM   8126 N  N   . THR D  1 209 ? 3.696   0.667   -28.508 1.00 7.36  ? 209 THR D N   1 
ATOM   8127 C  CA  . THR D  1 209 ? 3.215   -0.701  -28.323 1.00 7.60  ? 209 THR D CA  1 
ATOM   8128 C  C   . THR D  1 209 ? 3.687   -1.413  -29.615 1.00 7.43  ? 209 THR D C   1 
ATOM   8129 O  O   . THR D  1 209 ? 3.220   -1.082  -30.691 1.00 8.65  ? 209 THR D O   1 
ATOM   8130 C  CB  . THR D  1 209 ? 1.694   -0.748  -28.266 1.00 9.16  ? 209 THR D CB  1 
ATOM   8131 O  OG1 . THR D  1 209 ? 1.343   -0.027  -27.050 1.00 9.26  ? 209 THR D OG1 1 
ATOM   8132 C  CG2 . THR D  1 209 ? 1.210   -2.201  -27.964 1.00 9.54  ? 209 THR D CG2 1 
ATOM   8133 N  N   . VAL D  1 210 ? 4.594   -2.399  -29.513 1.00 7.89  ? 210 VAL D N   1 
ATOM   8134 C  CA  . VAL D  1 210 ? 5.033   -3.209  -30.637 1.00 8.48  ? 210 VAL D CA  1 
ATOM   8135 C  C   . VAL D  1 210 ? 4.425   -4.603  -30.419 1.00 7.65  ? 210 VAL D C   1 
ATOM   8136 O  O   . VAL D  1 210 ? 4.748   -5.225  -29.440 1.00 8.37  ? 210 VAL D O   1 
ATOM   8137 C  CB  . VAL D  1 210 ? 6.567   -3.236  -30.680 1.00 7.95  ? 210 VAL D CB  1 
ATOM   8138 C  CG1 . VAL D  1 210 ? 6.974   -4.047  -31.926 1.00 8.33  ? 210 VAL D CG1 1 
ATOM   8139 C  CG2 . VAL D  1 210 ? 7.198   -1.838  -30.792 1.00 9.05  ? 210 VAL D CG2 1 
ATOM   8140 N  N   . PHE D  1 211 ? 3.610   -5.076  -31.339 1.00 7.80  ? 211 PHE D N   1 
ATOM   8141 C  CA  . PHE D  1 211 ? 3.038   -6.373  -31.134 1.00 8.08  ? 211 PHE D CA  1 
ATOM   8142 C  C   . PHE D  1 211 ? 4.139   -7.432  -31.234 1.00 8.65  ? 211 PHE D C   1 
ATOM   8143 O  O   . PHE D  1 211 ? 5.087   -7.367  -31.993 1.00 9.41  ? 211 PHE D O   1 
ATOM   8144 C  CB  . PHE D  1 211 ? 1.916   -6.619  -32.131 1.00 8.42  ? 211 PHE D CB  1 
ATOM   8145 C  CG  . PHE D  1 211 ? 0.754   -5.692  -31.880 1.00 9.02  ? 211 PHE D CG  1 
ATOM   8146 C  CD1 . PHE D  1 211 ? -0.054  -5.897  -30.738 1.00 9.80  ? 211 PHE D CD1 1 
ATOM   8147 C  CD2 . PHE D  1 211 ? 0.421   -4.660  -32.770 1.00 10.63 ? 211 PHE D CD2 1 
ATOM   8148 C  CE1 . PHE D  1 211 ? -1.059  -4.991  -30.399 1.00 10.35 ? 211 PHE D CE1 1 
ATOM   8149 C  CE2 . PHE D  1 211 ? -0.642  -3.812  -32.443 1.00 9.71  ? 211 PHE D CE2 1 
ATOM   8150 C  CZ  . PHE D  1 211 ? -1.415  -3.974  -31.285 1.00 10.68 ? 211 PHE D CZ  1 
ATOM   8151 N  N   . ARG D  1 212 ? 4.005   -8.487  -30.409 1.00 8.66  ? 212 ARG D N   1 
ATOM   8152 C  CA  . ARG D  1 212 ? 4.987   -9.577  -30.413 1.00 9.60  ? 212 ARG D CA  1 
ATOM   8153 C  C   . ARG D  1 212 ? 5.048   -10.293 -31.723 1.00 10.26 ? 212 ARG D C   1 
ATOM   8154 O  O   . ARG D  1 212 ? 6.168   -10.617 -32.227 1.00 11.66 ? 212 ARG D O   1 
ATOM   8155 C  CB  . ARG D  1 212 ? 4.612   -10.558 -29.267 1.00 10.31 ? 212 ARG D CB  1 
ATOM   8156 C  CG  . ARG D  1 212 ? 5.654   -11.693 -29.200 1.00 10.36 ? 212 ARG D CG  1 
ATOM   8157 C  CD  . ARG D  1 212 ? 5.145   -12.729 -28.204 1.00 13.53 ? 212 ARG D CD  1 
ATOM   8158 N  NE  . ARG D  1 212 ? 6.198   -13.681 -27.860 1.00 15.31 ? 212 ARG D NE  1 
ATOM   8159 C  CZ  . ARG D  1 212 ? 6.042   -14.711 -27.036 1.00 18.61 ? 212 ARG D CZ  1 
ATOM   8160 N  NH1 . ARG D  1 212 ? 4.868   -14.933 -26.462 1.00 20.74 ? 212 ARG D NH1 1 
ATOM   8161 N  NH2 . ARG D  1 212 ? 7.062   -15.520 -26.786 1.00 22.48 ? 212 ARG D NH2 1 
ATOM   8162 N  N   . ASN D  1 213 ? 3.919   -10.567 -32.315 1.00 9.88  ? 213 ASN D N   1 
ATOM   8163 C  CA  . ASN D  1 213 ? 3.881   -11.360 -33.560 1.00 10.67 ? 213 ASN D CA  1 
ATOM   8164 C  C   . ASN D  1 213 ? 3.884   -10.476 -34.818 1.00 10.90 ? 213 ASN D C   1 
ATOM   8165 O  O   . ASN D  1 213 ? 3.154   -9.467  -34.857 1.00 10.93 ? 213 ASN D O   1 
ATOM   8166 C  CB  . ASN D  1 213 ? 2.622   -12.270 -33.561 1.00 12.84 ? 213 ASN D CB  1 
ATOM   8167 C  CG  . ASN D  1 213 ? 2.679   -13.260 -32.431 1.00 14.52 ? 213 ASN D CG  1 
ATOM   8168 O  OD1 . ASN D  1 213 ? 3.692   -13.946 -32.254 1.00 19.15 ? 213 ASN D OD1 1 
ATOM   8169 N  ND2 . ASN D  1 213 ? 1.670   -13.238 -31.623 1.00 17.95 ? 213 ASN D ND2 1 
ATOM   8170 N  N   . PRO D  1 214 ? 4.618   -10.850 -35.830 1.00 9.74  ? 214 PRO D N   1 
ATOM   8171 C  CA  . PRO D  1 214 ? 4.531   -10.147 -37.089 1.00 9.32  ? 214 PRO D CA  1 
ATOM   8172 C  C   . PRO D  1 214 ? 3.370   -10.530 -37.946 1.00 8.89  ? 214 PRO D C   1 
ATOM   8173 O  O   . PRO D  1 214 ? 2.729   -11.561 -37.699 1.00 10.69 ? 214 PRO D O   1 
ATOM   8174 C  CB  . PRO D  1 214 ? 5.896   -10.509 -37.810 1.00 9.60  ? 214 PRO D CB  1 
ATOM   8175 C  CG  . PRO D  1 214 ? 6.076   -11.953 -37.346 1.00 12.32 ? 214 PRO D CG  1 
ATOM   8176 C  CD  . PRO D  1 214 ? 5.649   -11.954 -35.861 1.00 11.10 ? 214 PRO D CD  1 
ATOM   8177 N  N   . VAL D  1 215 ? 3.053   -9.718  -38.954 1.00 8.06  ? 215 VAL D N   1 
ATOM   8178 C  CA  . VAL D  1 215 ? 2.221   -10.208 -40.078 1.00 8.27  ? 215 VAL D CA  1 
ATOM   8179 C  C   . VAL D  1 215 ? 3.119   -10.494 -41.279 1.00 7.78  ? 215 VAL D C   1 
ATOM   8180 O  O   . VAL D  1 215 ? 4.323   -10.173 -41.220 1.00 8.81  ? 215 VAL D O   1 
ATOM   8181 C  CB  . VAL D  1 215 ? 1.191   -9.104  -40.463 1.00 8.27  ? 215 VAL D CB  1 
ATOM   8182 C  CG1 . VAL D  1 215 ? 0.251   -8.813  -39.256 1.00 10.51 ? 215 VAL D CG1 1 
ATOM   8183 C  CG2 . VAL D  1 215 ? 1.869   -7.821  -41.076 1.00 8.86  ? 215 VAL D CG2 1 
ATOM   8184 N  N   . GLN D  1 216 ? 2.562   -11.034 -42.321 1.00 7.57  ? 216 GLN D N   1 
ATOM   8185 C  CA  . GLN D  1 216 ? 3.280   -11.326 -43.535 1.00 8.27  ? 216 GLN D CA  1 
ATOM   8186 C  C   . GLN D  1 216 ? 2.659   -10.550 -44.695 1.00 9.08  ? 216 GLN D C   1 
ATOM   8187 O  O   . GLN D  1 216 ? 1.423   -10.427 -44.823 1.00 9.16  ? 216 GLN D O   1 
ATOM   8188 C  CB  . GLN D  1 216 ? 3.159   -12.823 -43.951 1.00 9.54  ? 216 GLN D CB  1 
ATOM   8189 C  CG  . GLN D  1 216 ? 4.020   -13.670 -43.018 1.00 10.81 ? 216 GLN D CG  1 
ATOM   8190 C  CD  . GLN D  1 216 ? 3.940   -15.163 -43.359 1.00 12.20 ? 216 GLN D CD  1 
ATOM   8191 O  OE1 . GLN D  1 216 ? 3.454   -15.606 -44.373 1.00 12.13 ? 216 GLN D OE1 1 
ATOM   8192 N  NE2 . GLN D  1 216 ? 4.529   -15.943 -42.430 1.00 16.92 ? 216 GLN D NE2 1 
ATOM   8193 N  N   . ILE D  1 217 ? 3.500   -10.089 -45.597 1.00 8.12  ? 217 ILE D N   1 
ATOM   8194 C  CA  . ILE D  1 217 ? 3.087   -9.661  -46.955 1.00 8.00  ? 217 ILE D CA  1 
ATOM   8195 C  C   . ILE D  1 217 ? 4.063   -10.298 -47.939 1.00 7.89  ? 217 ILE D C   1 
ATOM   8196 O  O   . ILE D  1 217 ? 5.163   -10.758 -47.512 1.00 7.75  ? 217 ILE D O   1 
ATOM   8197 C  CB  . ILE D  1 217 ? 3.098   -8.091  -47.131 1.00 7.62  ? 217 ILE D CB  1 
ATOM   8198 C  CG1 . ILE D  1 217 ? 4.530   -7.568  -47.089 1.00 7.79  ? 217 ILE D CG1 1 
ATOM   8199 C  CG2 . ILE D  1 217 ? 2.169   -7.402  -46.114 1.00 9.69  ? 217 ILE D CG2 1 
ATOM   8200 C  CD1 . ILE D  1 217 ? 4.578   -5.994  -47.388 1.00 10.12 ? 217 ILE D CD1 1 
ATOM   8201 N  N   . SER D  1 218 ? 3.652   -10.430 -49.179 1.00 7.24  ? 218 SER D N   1 
ATOM   8202 C  CA  . SER D  1 218 ? 4.541   -11.167 -50.125 1.00 7.90  ? 218 SER D CA  1 
ATOM   8203 C  C   . SER D  1 218 ? 5.714   -10.419 -50.628 1.00 8.04  ? 218 SER D C   1 
ATOM   8204 O  O   . SER D  1 218 ? 5.772   -9.149  -50.539 1.00 9.00  ? 218 SER D O   1 
ATOM   8205 C  CB  . SER D  1 218 ? 3.705   -11.708 -51.312 1.00 7.89  ? 218 SER D CB  1 
ATOM   8206 O  OG  . SER D  1 218 ? 3.332   -10.603 -52.132 1.00 8.87  ? 218 SER D OG  1 
ATOM   8207 N  N   A GLN D  1 219 ? 6.647   -11.153 -51.230 0.50 9.16  ? 219 GLN D N   1 
ATOM   8208 N  N   B GLN D  1 219 ? 6.685   -11.138 -51.171 0.50 8.57  ? 219 GLN D N   1 
ATOM   8209 C  CA  A GLN D  1 219 ? 7.761   -10.548 -51.937 0.50 9.64  ? 219 GLN D CA  1 
ATOM   8210 C  CA  B GLN D  1 219 ? 7.794   -10.465 -51.790 0.50 8.55  ? 219 GLN D CA  1 
ATOM   8211 C  C   A GLN D  1 219 ? 7.281   -9.494  -52.913 0.50 9.33  ? 219 GLN D C   1 
ATOM   8212 C  C   B GLN D  1 219 ? 7.357   -9.544  -52.961 0.50 8.81  ? 219 GLN D C   1 
ATOM   8213 O  O   A GLN D  1 219 ? 7.811   -8.365  -52.999 0.50 8.66  ? 219 GLN D O   1 
ATOM   8214 O  O   B GLN D  1 219 ? 8.008   -8.503  -53.185 0.50 8.84  ? 219 GLN D O   1 
ATOM   8215 C  CB  A GLN D  1 219 ? 8.424   -11.573 -52.846 0.50 11.89 ? 219 GLN D CB  1 
ATOM   8216 C  CB  B GLN D  1 219 ? 8.812   -11.446 -52.346 0.50 9.67  ? 219 GLN D CB  1 
ATOM   8217 C  CG  A GLN D  1 219 ? 9.735   -11.111 -53.559 0.50 14.74 ? 219 GLN D CG  1 
ATOM   8218 C  CG  B GLN D  1 219 ? 10.108  -10.820 -52.981 0.50 10.71 ? 219 GLN D CG  1 
ATOM   8219 C  CD  A GLN D  1 219 ? 10.409  -9.802  -52.991 0.50 18.16 ? 219 GLN D CD  1 
ATOM   8220 C  CD  B GLN D  1 219 ? 9.996   -10.271 -54.414 0.50 10.61 ? 219 GLN D CD  1 
ATOM   8221 O  OE1 A GLN D  1 219 ? 10.537  -9.635  -51.785 0.50 25.10 ? 219 GLN D OE1 1 
ATOM   8222 O  OE1 B GLN D  1 219 ? 9.085   -10.643 -55.149 0.50 12.08 ? 219 GLN D OE1 1 
ATOM   8223 N  NE2 A GLN D  1 219 ? 10.799  -8.855  -53.874 0.50 16.61 ? 219 GLN D NE2 1 
ATOM   8224 N  NE2 B GLN D  1 219 ? 10.918  -9.362  -54.784 0.50 11.85 ? 219 GLN D NE2 1 
ATOM   8225 N  N   . GLU D  1 220 ? 6.266   -9.868  -53.651 1.00 8.53  ? 220 GLU D N   1 
ATOM   8226 C  CA  . GLU D  1 220 ? 5.798   -8.990  -54.721 1.00 8.85  ? 220 GLU D CA  1 
ATOM   8227 C  C   . GLU D  1 220 ? 5.184   -7.709  -54.108 1.00 8.81  ? 220 GLU D C   1 
ATOM   8228 O  O   . GLU D  1 220 ? 5.349   -6.650  -54.703 1.00 9.86  ? 220 GLU D O   1 
ATOM   8229 C  CB  . GLU D  1 220 ? 4.804   -9.681  -55.652 1.00 9.92  ? 220 GLU D CB  1 
ATOM   8230 C  CG  . GLU D  1 220 ? 5.431   -10.836 -56.441 1.00 10.78 ? 220 GLU D CG  1 
ATOM   8231 C  CD  . GLU D  1 220 ? 5.602   -12.134 -55.680 1.00 16.07 ? 220 GLU D CD  1 
ATOM   8232 O  OE1 . GLU D  1 220 ? 5.172   -12.323 -54.542 1.00 15.24 ? 220 GLU D OE1 1 
ATOM   8233 O  OE2 . GLU D  1 220 ? 6.211   -13.068 -56.341 1.00 22.99 ? 220 GLU D OE2 1 
ATOM   8234 N  N   . GLN D  1 221 ? 4.451   -7.804  -52.962 1.00 8.42  ? 221 GLN D N   1 
ATOM   8235 C  CA  . GLN D  1 221 ? 3.953   -6.622  -52.319 1.00 9.16  ? 221 GLN D CA  1 
ATOM   8236 C  C   . GLN D  1 221 ? 5.055   -5.804  -51.807 1.00 8.57  ? 221 GLN D C   1 
ATOM   8237 O  O   . GLN D  1 221 ? 5.050   -4.579  -52.002 1.00 9.59  ? 221 GLN D O   1 
ATOM   8238 C  CB  . GLN D  1 221 ? 3.034   -7.018  -51.198 1.00 8.94  ? 221 GLN D CB  1 
ATOM   8239 C  CG  . GLN D  1 221 ? 1.696   -7.662  -51.701 1.00 8.60  ? 221 GLN D CG  1 
ATOM   8240 C  CD  . GLN D  1 221 ? 0.864   -8.068  -50.563 1.00 8.28  ? 221 GLN D CD  1 
ATOM   8241 O  OE1 . GLN D  1 221 ? 1.170   -8.974  -49.749 1.00 9.29  ? 221 GLN D OE1 1 
ATOM   8242 N  NE2 . GLN D  1 221 ? -0.256  -7.387  -50.409 1.00 9.14  ? 221 GLN D NE2 1 
ATOM   8243 N  N   . LEU D  1 222 ? 6.109   -6.398  -51.208 1.00 7.94  ? 222 LEU D N   1 
ATOM   8244 C  CA  . LEU D  1 222 ? 7.241   -5.618  -50.736 1.00 8.21  ? 222 LEU D CA  1 
ATOM   8245 C  C   . LEU D  1 222 ? 7.927   -4.916  -51.892 1.00 9.54  ? 222 LEU D C   1 
ATOM   8246 O  O   . LEU D  1 222 ? 8.354   -3.762  -51.780 1.00 9.60  ? 222 LEU D O   1 
ATOM   8247 C  CB  . LEU D  1 222 ? 8.217   -6.541  -50.043 1.00 9.43  ? 222 LEU D CB  1 
ATOM   8248 C  CG  . LEU D  1 222 ? 7.883   -6.758  -48.603 1.00 11.16 ? 222 LEU D CG  1 
ATOM   8249 C  CD1 . LEU D  1 222 ? 8.552   -8.024  -48.055 1.00 12.03 ? 222 LEU D CD1 1 
ATOM   8250 C  CD2 . LEU D  1 222 ? 8.288   -5.618  -47.661 1.00 12.14 ? 222 LEU D CD2 1 
ATOM   8251 N  N   . LEU D  1 223 ? 8.082   -5.614  -53.023 1.00 8.85  ? 223 LEU D N   1 
ATOM   8252 C  CA  . LEU D  1 223 ? 8.836   -5.018  -54.133 1.00 8.94  ? 223 LEU D CA  1 
ATOM   8253 C  C   . LEU D  1 223 ? 8.004   -3.831  -54.676 1.00 9.23  ? 223 LEU D C   1 
ATOM   8254 O  O   . LEU D  1 223 ? 8.593   -2.816  -55.101 1.00 10.13 ? 223 LEU D O   1 
ATOM   8255 C  CB  . LEU D  1 223 ? 9.104   -6.081  -55.295 1.00 9.30  ? 223 LEU D CB  1 
ATOM   8256 C  CG  . LEU D  1 223 ? 9.851   -5.496  -56.495 1.00 10.73 ? 223 LEU D CG  1 
ATOM   8257 C  CD1 . LEU D  1 223 ? 11.299  -5.102  -56.020 1.00 13.23 ? 223 LEU D CD1 1 
ATOM   8258 C  CD2 . LEU D  1 223 ? 9.873   -6.594  -57.591 1.00 11.00 ? 223 LEU D CD2 1 
ATOM   8259 N  N   . ALA D  1 224 ? 6.700   -3.979  -54.732 1.00 10.26 ? 224 ALA D N   1 
ATOM   8260 C  CA  . ALA D  1 224 ? 5.850   -2.824  -55.233 1.00 10.78 ? 224 ALA D CA  1 
ATOM   8261 C  C   . ALA D  1 224 ? 6.034   -1.659  -54.253 1.00 10.94 ? 224 ALA D C   1 
ATOM   8262 O  O   . ALA D  1 224 ? 6.263   -0.537  -54.645 1.00 11.51 ? 224 ALA D O   1 
ATOM   8263 C  CB  . ALA D  1 224 ? 4.392   -3.268  -55.364 1.00 11.30 ? 224 ALA D CB  1 
ATOM   8264 N  N   . LEU D  1 225 ? 5.968   -1.910  -52.959 1.00 8.92  ? 225 LEU D N   1 
ATOM   8265 C  CA  . LEU D  1 225 ? 6.167   -0.842  -51.951 1.00 10.31 ? 225 LEU D CA  1 
ATOM   8266 C  C   . LEU D  1 225 ? 7.515   -0.163  -52.110 1.00 10.88 ? 225 LEU D C   1 
ATOM   8267 O  O   . LEU D  1 225 ? 7.618   1.048   -52.049 1.00 11.76 ? 225 LEU D O   1 
ATOM   8268 C  CB  . LEU D  1 225 ? 6.009   -1.478  -50.593 1.00 9.49  ? 225 LEU D CB  1 
ATOM   8269 C  CG  . LEU D  1 225 ? 6.113   -0.468  -49.429 1.00 11.17 ? 225 LEU D CG  1 
ATOM   8270 C  CD1 . LEU D  1 225 ? 5.108   0.726   -49.476 1.00 13.04 ? 225 LEU D CD1 1 
ATOM   8271 C  CD2 . LEU D  1 225 ? 5.953   -1.211  -48.090 1.00 10.98 ? 225 LEU D CD2 1 
ATOM   8272 N  N   . GLU D  1 226 ? 8.557   -0.980  -52.326 1.00 9.83  ? 226 GLU D N   1 
ATOM   8273 C  CA  . GLU D  1 226 ? 9.926   -0.484  -52.390 1.00 10.27 ? 226 GLU D CA  1 
ATOM   8274 C  C   . GLU D  1 226 ? 10.243  0.246   -53.717 1.00 11.90 ? 226 GLU D C   1 
ATOM   8275 O  O   . GLU D  1 226 ? 11.286  0.902   -53.757 1.00 14.18 ? 226 GLU D O   1 
ATOM   8276 C  CB  . GLU D  1 226 ? 10.851  -1.745  -52.320 1.00 9.72  ? 226 GLU D CB  1 
ATOM   8277 C  CG  . GLU D  1 226 ? 10.914  -2.331  -50.905 1.00 9.98  ? 226 GLU D CG  1 
ATOM   8278 C  CD  . GLU D  1 226 ? 11.265  -3.806  -50.936 1.00 11.20 ? 226 GLU D CD  1 
ATOM   8279 O  OE1 . GLU D  1 226 ? 11.554  -4.419  -51.996 1.00 10.88 ? 226 GLU D OE1 1 
ATOM   8280 O  OE2 . GLU D  1 226 ? 11.268  -4.392  -49.851 1.00 11.91 ? 226 GLU D OE2 1 
ATOM   8281 N  N   . THR D  1 227 ? 9.429   0.078   -54.762 1.00 10.69 ? 227 THR D N   1 
ATOM   8282 C  CA  . THR D  1 227 ? 9.742   0.646   -56.062 1.00 10.69 ? 227 THR D CA  1 
ATOM   8283 C  C   . THR D  1 227 ? 8.709   1.646   -56.512 1.00 11.35 ? 227 THR D C   1 
ATOM   8284 O  O   . THR D  1 227 ? 8.942   2.309   -57.553 1.00 13.82 ? 227 THR D O   1 
ATOM   8285 C  CB  . THR D  1 227 ? 9.920   -0.450  -57.156 1.00 12.18 ? 227 THR D CB  1 
ATOM   8286 O  OG1 . THR D  1 227 ? 8.730   -1.157  -57.329 1.00 12.37 ? 227 THR D OG1 1 
ATOM   8287 C  CG2 . THR D  1 227 ? 11.092  -1.368  -56.854 1.00 13.62 ? 227 THR D CG2 1 
ATOM   8288 N  N   . ALA D  1 228 ? 7.609   1.796   -55.810 1.00 11.10 ? 228 ALA D N   1 
ATOM   8289 C  CA  . ALA D  1 228 ? 6.520   2.629   -56.332 1.00 11.78 ? 228 ALA D CA  1 
ATOM   8290 C  C   . ALA D  1 228 ? 6.756   4.085   -56.157 1.00 12.49 ? 228 ALA D C   1 
ATOM   8291 O  O   . ALA D  1 228 ? 6.193   4.848   -56.953 1.00 14.28 ? 228 ALA D O   1 
ATOM   8292 C  CB  . ALA D  1 228 ? 5.173   2.240   -55.719 1.00 13.37 ? 228 ALA D CB  1 
ATOM   8293 N  N   . LEU D  1 229 ? 7.435   4.509   -55.108 1.00 10.95 ? 229 LEU D N   1 
ATOM   8294 C  CA  . LEU D  1 229 ? 7.319   5.899   -54.661 1.00 10.74 ? 229 LEU D CA  1 
ATOM   8295 C  C   . LEU D  1 229 ? 8.629   6.635   -54.774 1.00 11.00 ? 229 LEU D C   1 
ATOM   8296 O  O   . LEU D  1 229 ? 9.715   6.049   -54.640 1.00 10.25 ? 229 LEU D O   1 
ATOM   8297 C  CB  . LEU D  1 229 ? 6.848   5.972   -53.174 1.00 11.05 ? 229 LEU D CB  1 
ATOM   8298 C  CG  . LEU D  1 229 ? 5.576   5.123   -52.836 1.00 12.92 ? 229 LEU D CG  1 
ATOM   8299 C  CD1 . LEU D  1 229 ? 5.207   5.176   -51.346 1.00 15.08 ? 229 LEU D CD1 1 
ATOM   8300 C  CD2 . LEU D  1 229 ? 4.413   5.528   -53.773 1.00 14.41 ? 229 LEU D CD2 1 
ATOM   8301 N  N   . TYR D  1 230 ? 8.435   7.949   -54.946 1.00 10.71 ? 230 TYR D N   1 
ATOM   8302 C  CA  . TYR D  1 230 ? 9.546   8.900   -54.872 1.00 11.06 ? 230 TYR D CA  1 
ATOM   8303 C  C   . TYR D  1 230 ? 9.358   9.871   -53.699 1.00 10.34 ? 230 TYR D C   1 
ATOM   8304 O  O   . TYR D  1 230 ? 8.249   10.292  -53.393 1.00 11.25 ? 230 TYR D O   1 
ATOM   8305 C  CB  . TYR D  1 230 ? 9.671   9.700   -56.213 1.00 10.65 ? 230 TYR D CB  1 
ATOM   8306 C  CG  . TYR D  1 230 ? 10.174  8.873   -57.335 1.00 13.77 ? 230 TYR D CG  1 
ATOM   8307 C  CD1 . TYR D  1 230 ? 9.327   7.977   -57.998 1.00 16.60 ? 230 TYR D CD1 1 
ATOM   8308 C  CD2 . TYR D  1 230 ? 11.520  8.896   -57.623 1.00 15.82 ? 230 TYR D CD2 1 
ATOM   8309 C  CE1 . TYR D  1 230 ? 9.849   7.134   -58.995 1.00 21.54 ? 230 TYR D CE1 1 
ATOM   8310 C  CE2 . TYR D  1 230 ? 12.063  8.045   -58.622 1.00 20.13 ? 230 TYR D CE2 1 
ATOM   8311 C  CZ  . TYR D  1 230 ? 11.207  7.188   -59.292 1.00 23.54 ? 230 TYR D CZ  1 
ATOM   8312 O  OH  . TYR D  1 230 ? 11.681  6.323   -60.253 1.00 26.00 ? 230 TYR D OH  1 
ATOM   8313 N  N   . CYS D  1 231 ? 10.469  10.303  -53.111 1.00 11.85 ? 231 CYS D N   1 
ATOM   8314 C  CA  . CYS D  1 231 ? 10.435  11.343  -52.127 1.00 10.66 ? 231 CYS D CA  1 
ATOM   8315 C  C   . CYS D  1 231 ? 10.219  12.791  -52.628 1.00 10.07 ? 231 CYS D C   1 
ATOM   8316 O  O   . CYS D  1 231 ? 9.877   13.650  -51.898 1.00 12.71 ? 231 CYS D O   1 
ATOM   8317 C  CB  . CYS D  1 231 ? 11.781  11.427  -51.419 1.00 12.64 ? 231 CYS D CB  1 
ATOM   8318 S  SG  . CYS D  1 231 ? 12.305  9.938   -50.489 1.00 12.97 ? 231 CYS D SG  1 
ATOM   8319 N  N   . THR D  1 232 ? 10.417  12.888  -53.931 1.00 10.76 ? 232 THR D N   1 
ATOM   8320 C  CA  . THR D  1 232 ? 10.436  14.230  -54.617 1.00 13.14 ? 232 THR D CA  1 
ATOM   8321 C  C   . THR D  1 232 ? 9.162   14.455  -55.387 1.00 14.49 ? 232 THR D C   1 
ATOM   8322 O  O   . THR D  1 232 ? 8.366   13.555  -55.728 1.00 14.55 ? 232 THR D O   1 
ATOM   8323 C  CB  . THR D  1 232 ? 11.697  14.217  -55.543 1.00 12.66 ? 232 THR D CB  1 
ATOM   8324 O  OG1 . THR D  1 232 ? 11.773  12.935  -56.182 1.00 11.87 ? 232 THR D OG1 1 
ATOM   8325 C  CG2 . THR D  1 232 ? 12.941  14.487  -54.789 1.00 13.85 ? 232 THR D CG2 1 
ATOM   8326 N  N   . HIS D  1 233 ? 8.903   15.757  -55.583 1.00 14.32 ? 233 HIS D N   1 
ATOM   8327 C  CA  . HIS D  1 233 ? 7.860   16.158  -56.480 1.00 14.02 ? 233 HIS D CA  1 
ATOM   8328 C  C   . HIS D  1 233 ? 8.078   15.715  -57.884 1.00 15.05 ? 233 HIS D C   1 
ATOM   8329 O  O   . HIS D  1 233 ? 9.199   15.507  -58.314 1.00 16.72 ? 233 HIS D O   1 
ATOM   8330 C  CB  . HIS D  1 233 ? 7.739   17.716  -56.453 1.00 16.76 ? 233 HIS D CB  1 
ATOM   8331 C  CG  . HIS D  1 233 ? 7.202   18.222  -55.159 1.00 16.97 ? 233 HIS D CG  1 
ATOM   8332 N  ND1 . HIS D  1 233 ? 7.960   18.926  -54.252 1.00 22.81 ? 233 HIS D ND1 1 
ATOM   8333 C  CD2 . HIS D  1 233 ? 5.935   18.119  -54.600 1.00 19.72 ? 233 HIS D CD2 1 
ATOM   8334 C  CE1 . HIS D  1 233 ? 7.186   19.207  -53.156 1.00 22.59 ? 233 HIS D CE1 1 
ATOM   8335 N  NE2 . HIS D  1 233 ? 5.965   18.728  -53.381 1.00 21.12 ? 233 HIS D NE2 1 
ATOM   8336 N  N   . MET D  1 234 ? 6.980   15.572  -58.607 1.00 18.54 ? 234 MET D N   1 
ATOM   8337 C  CA  . MET D  1 234 ? 6.999   15.081  -59.989 1.00 18.11 ? 234 MET D CA  1 
ATOM   8338 C  C   . MET D  1 234 ? 7.951   15.888  -60.856 1.00 23.88 ? 234 MET D C   1 
ATOM   8339 O  O   . MET D  1 234 ? 8.704   15.351  -61.678 1.00 24.79 ? 234 MET D O   1 
ATOM   8340 C  CB  . MET D  1 234 ? 5.578   15.095  -60.507 1.00 24.49 ? 234 MET D CB  1 
ATOM   8341 C  CG  . MET D  1 234 ? 5.471   14.571  -61.921 1.00 29.71 ? 234 MET D CG  1 
ATOM   8342 S  SD  . MET D  1 234 ? 3.706   14.409  -62.275 1.00 42.37 ? 234 MET D SD  1 
ATOM   8343 C  CE  . MET D  1 234 ? 3.797   13.214  -63.610 1.00 38.95 ? 234 MET D CE  1 
ATOM   8344 N  N   . ASP D  1 235 ? 8.034   17.187  -60.579 1.00 21.86 ? 235 ASP D N   1 
ATOM   8345 C  CA  . ASP D  1 235 ? 8.853   18.037  -61.463 1.00 25.37 ? 235 ASP D CA  1 
ATOM   8346 C  C   . ASP D  1 235 ? 10.273  18.292  -60.947 1.00 24.90 ? 235 ASP D C   1 
ATOM   8347 O  O   . ASP D  1 235 ? 10.992  19.132  -61.485 1.00 25.00 ? 235 ASP D O   1 
ATOM   8348 C  CB  . ASP D  1 235 ? 8.053   19.346  -61.741 1.00 28.70 ? 235 ASP D CB  1 
ATOM   8349 C  CG  . ASP D  1 235 ? 7.903   20.225  -60.468 1.00 33.04 ? 235 ASP D CG  1 
ATOM   8350 O  OD1 . ASP D  1 235 ? 8.285   19.778  -59.352 1.00 31.76 ? 235 ASP D OD1 1 
ATOM   8351 O  OD2 . ASP D  1 235 ? 7.403   21.372  -60.564 1.00 34.09 ? 235 ASP D OD2 1 
ATOM   8352 N  N   . ASP D  1 236 ? 10.748  17.591  -59.909 1.00 21.19 ? 236 ASP D N   1 
ATOM   8353 C  CA  . ASP D  1 236 ? 12.064  17.770  -59.423 1.00 21.30 ? 236 ASP D CA  1 
ATOM   8354 C  C   . ASP D  1 236 ? 13.043  17.236  -60.477 1.00 21.25 ? 236 ASP D C   1 
ATOM   8355 O  O   . ASP D  1 236 ? 12.884  16.098  -60.925 1.00 22.69 ? 236 ASP D O   1 
ATOM   8356 C  CB  . ASP D  1 236 ? 12.239  16.970  -58.093 1.00 20.06 ? 236 ASP D CB  1 
ATOM   8357 C  CG  . ASP D  1 236 ? 13.389  17.474  -57.253 1.00 22.50 ? 236 ASP D CG  1 
ATOM   8358 O  OD1 . ASP D  1 236 ? 14.507  17.593  -57.788 1.00 23.46 ? 236 ASP D OD1 1 
ATOM   8359 O  OD2 . ASP D  1 236 ? 13.177  17.744  -56.053 1.00 22.11 ? 236 ASP D OD2 1 
ATOM   8360 N  N   . PRO D  1 237 ? 14.047  18.061  -60.852 1.00 25.99 ? 237 PRO D N   1 
ATOM   8361 C  CA  . PRO D  1 237 ? 15.088  17.601  -61.778 1.00 25.27 ? 237 PRO D CA  1 
ATOM   8362 C  C   . PRO D  1 237 ? 16.041  16.572  -61.151 1.00 25.00 ? 237 PRO D C   1 
ATOM   8363 O  O   . PRO D  1 237 ? 16.833  15.938  -61.879 1.00 23.01 ? 237 PRO D O   1 
ATOM   8364 C  CB  . PRO D  1 237 ? 15.841  18.916  -62.086 1.00 28.06 ? 237 PRO D CB  1 
ATOM   8365 C  CG  . PRO D  1 237 ? 15.803  19.670  -60.775 1.00 26.54 ? 237 PRO D CG  1 
ATOM   8366 C  CD  . PRO D  1 237 ? 14.343  19.424  -60.316 1.00 26.14 ? 237 PRO D CD  1 
ATOM   8367 N  N   . SER D  1 238 ? 15.951  16.361  -59.828 1.00 21.22 ? 238 SER D N   1 
ATOM   8368 C  CA  . SER D  1 238 ? 16.851  15.455  -59.128 1.00 19.96 ? 238 SER D CA  1 
ATOM   8369 C  C   . SER D  1 238 ? 15.981  14.431  -58.331 1.00 17.69 ? 238 SER D C   1 
ATOM   8370 O  O   . SER D  1 238 ? 15.890  14.515  -57.138 1.00 16.36 ? 238 SER D O   1 
ATOM   8371 C  CB  . SER D  1 238 ? 17.762  16.236  -58.202 1.00 27.34 ? 238 SER D CB  1 
ATOM   8372 O  OG  . SER D  1 238 ? 18.756  15.384  -57.672 1.00 35.57 ? 238 SER D OG  1 
ATOM   8373 N  N   . PRO D  1 239 ? 15.311  13.523  -59.062 1.00 18.27 ? 239 PRO D N   1 
ATOM   8374 C  CA  . PRO D  1 239 ? 14.423  12.531  -58.350 1.00 15.53 ? 239 PRO D CA  1 
ATOM   8375 C  C   . PRO D  1 239 ? 15.154  11.666  -57.357 1.00 14.91 ? 239 PRO D C   1 
ATOM   8376 O  O   . PRO D  1 239 ? 16.308  11.270  -57.527 1.00 17.77 ? 239 PRO D O   1 
ATOM   8377 C  CB  . PRO D  1 239 ? 13.810  11.649  -59.451 1.00 18.62 ? 239 PRO D CB  1 
ATOM   8378 C  CG  . PRO D  1 239 ? 14.448  12.057  -60.707 1.00 21.35 ? 239 PRO D CG  1 
ATOM   8379 C  CD  . PRO D  1 239 ? 15.466  13.146  -60.482 1.00 20.70 ? 239 PRO D CD  1 
ATOM   8380 N  N   . ARG D  1 240 ? 14.461  11.360  -56.251 1.00 14.09 ? 240 ARG D N   1 
ATOM   8381 C  CA  . ARG D  1 240 ? 15.047  10.475  -55.234 1.00 11.78 ? 240 ARG D CA  1 
ATOM   8382 C  C   . ARG D  1 240 ? 14.008  9.373   -54.892 1.00 11.49 ? 240 ARG D C   1 
ATOM   8383 O  O   . ARG D  1 240 ? 12.845  9.725   -54.515 1.00 11.53 ? 240 ARG D O   1 
ATOM   8384 C  CB  . ARG D  1 240 ? 15.311  11.244  -53.962 1.00 12.62 ? 240 ARG D CB  1 
ATOM   8385 C  CG  . ARG D  1 240 ? 16.553  12.171  -54.113 1.00 14.86 ? 240 ARG D CG  1 
ATOM   8386 C  CD  . ARG D  1 240 ? 16.798  12.870  -52.785 1.00 18.19 ? 240 ARG D CD  1 
ATOM   8387 N  NE  . ARG D  1 240 ? 15.790  13.905  -52.492 1.00 18.49 ? 240 ARG D NE  1 
ATOM   8388 C  CZ  . ARG D  1 240 ? 14.863  13.832  -51.523 1.00 21.08 ? 240 ARG D CZ  1 
ATOM   8389 N  NH1 . ARG D  1 240 ? 14.831  12.826  -50.650 1.00 16.62 ? 240 ARG D NH1 1 
ATOM   8390 N  NH2 . ARG D  1 240 ? 14.031  14.850  -51.350 1.00 21.39 ? 240 ARG D NH2 1 
ATOM   8391 N  N   . GLU D  1 241 ? 14.408  8.106   -55.033 1.00 11.55 ? 241 GLU D N   1 
ATOM   8392 C  CA  . GLU D  1 241 ? 13.534  6.979   -54.697 1.00 11.76 ? 241 GLU D CA  1 
ATOM   8393 C  C   . GLU D  1 241 ? 13.234  6.940   -53.223 1.00 11.04 ? 241 GLU D C   1 
ATOM   8394 O  O   . GLU D  1 241 ? 14.099  7.160   -52.345 1.00 10.62 ? 241 GLU D O   1 
ATOM   8395 C  CB  . GLU D  1 241 ? 14.217  5.682   -55.068 1.00 13.60 ? 241 GLU D CB  1 
ATOM   8396 C  CG  . GLU D  1 241 ? 14.397  5.566   -56.592 1.00 17.48 ? 241 GLU D CG  1 
ATOM   8397 C  CD  . GLU D  1 241 ? 15.051  4.305   -57.019 1.00 24.28 ? 241 GLU D CD  1 
ATOM   8398 O  OE1 . GLU D  1 241 ? 15.545  3.492   -56.191 1.00 31.37 ? 241 GLU D OE1 1 
ATOM   8399 O  OE2 . GLU D  1 241 ? 15.072  4.132   -58.233 1.00 34.14 ? 241 GLU D OE2 1 
ATOM   8400 N  N   . MET D  1 242 ? 11.956  6.551   -52.892 1.00 9.42  ? 242 MET D N   1 
ATOM   8401 C  CA  . MET D  1 242 ? 11.592  6.490   -51.451 1.00 9.42  ? 242 MET D CA  1 
ATOM   8402 C  C   . MET D  1 242 ? 11.902  5.044   -50.987 1.00 8.88  ? 242 MET D C   1 
ATOM   8403 O  O   . MET D  1 242 ? 11.073  4.139   -51.132 1.00 8.85  ? 242 MET D O   1 
ATOM   8404 C  CB  . MET D  1 242 ? 10.130  6.829   -51.254 1.00 9.92  ? 242 MET D CB  1 
ATOM   8405 C  CG  . MET D  1 242 ? 9.815   6.896   -49.746 1.00 10.67 ? 242 MET D CG  1 
ATOM   8406 S  SD  . MET D  1 242 ? 8.051   7.203   -49.423 1.00 9.23  ? 242 MET D SD  1 
ATOM   8407 C  CE  . MET D  1 242 ? 7.980   8.896   -50.089 1.00 10.22 ? 242 MET D CE  1 
ATOM   8408 N  N   . ILE D  1 243 ? 13.120  4.828   -50.520 1.00 9.29  ? 243 ILE D N   1 
ATOM   8409 C  CA  . ILE D  1 243 ? 13.661  3.544   -50.135 1.00 9.05  ? 243 ILE D CA  1 
ATOM   8410 C  C   . ILE D  1 243 ? 14.369  3.788   -48.801 1.00 8.34  ? 243 ILE D C   1 
ATOM   8411 O  O   . ILE D  1 243 ? 14.877  4.875   -48.492 1.00 8.55  ? 243 ILE D O   1 
ATOM   8412 C  CB  . ILE D  1 243 ? 14.640  2.907   -51.149 1.00 9.77  ? 243 ILE D CB  1 
ATOM   8413 C  CG1 . ILE D  1 243 ? 15.768  3.926   -51.514 1.00 11.18 ? 243 ILE D CG1 1 
ATOM   8414 C  CG2 . ILE D  1 243 ? 13.852  2.465   -52.360 1.00 12.32 ? 243 ILE D CG2 1 
ATOM   8415 C  CD1 . ILE D  1 243 ? 16.773  3.349   -52.492 1.00 13.02 ? 243 ILE D CD1 1 
ATOM   8416 N  N   . ASN D  1 244 ? 14.521  2.664   -48.072 1.00 6.82  ? 244 ASN D N   1 
ATOM   8417 C  CA  . ASN D  1 244 ? 15.323  2.702   -46.846 1.00 7.36  ? 244 ASN D CA  1 
ATOM   8418 C  C   . ASN D  1 244 ? 14.919  3.800   -45.884 1.00 7.96  ? 244 ASN D C   1 
ATOM   8419 O  O   . ASN D  1 244 ? 15.746  4.469   -45.248 1.00 8.46  ? 244 ASN D O   1 
ATOM   8420 C  CB  . ASN D  1 244 ? 16.839  2.856   -47.160 1.00 8.61  ? 244 ASN D CB  1 
ATOM   8421 C  CG  . ASN D  1 244 ? 17.276  1.759   -48.053 1.00 10.91 ? 244 ASN D CG  1 
ATOM   8422 O  OD1 . ASN D  1 244 ? 16.850  0.563   -47.946 1.00 10.22 ? 244 ASN D OD1 1 
ATOM   8423 N  ND2 . ASN D  1 244 ? 18.086  2.179   -49.059 1.00 12.55 ? 244 ASN D ND2 1 
ATOM   8424 N  N   . ASN D  1 245 ? 13.604  3.991   -45.718 1.00 7.42  ? 245 ASN D N   1 
ATOM   8425 C  CA  . ASN D  1 245 ? 13.083  5.058   -44.898 1.00 7.12  ? 245 ASN D CA  1 
ATOM   8426 C  C   . ASN D  1 245 ? 12.791  4.595   -43.470 1.00 7.48  ? 245 ASN D C   1 
ATOM   8427 O  O   . ASN D  1 245 ? 11.665  4.740   -42.973 1.00 8.60  ? 245 ASN D O   1 
ATOM   8428 C  CB  . ASN D  1 245 ? 11.787  5.662   -45.572 1.00 7.11  ? 245 ASN D CB  1 
ATOM   8429 C  CG  . ASN D  1 245 ? 10.673  4.668   -45.799 1.00 8.14  ? 245 ASN D CG  1 
ATOM   8430 O  OD1 . ASN D  1 245 ? 10.859  3.512   -45.716 1.00 7.73  ? 245 ASN D OD1 1 
ATOM   8431 N  ND2 . ASN D  1 245 ? 9.440   5.191   -45.997 1.00 8.42  ? 245 ASN D ND2 1 
ATOM   8432 N  N   . PHE D  1 246 ? 13.822  4.047   -42.830 1.00 6.96  ? 246 PHE D N   1 
ATOM   8433 C  CA  . PHE D  1 246 ? 13.775  3.609   -41.445 1.00 6.92  ? 246 PHE D CA  1 
ATOM   8434 C  C   . PHE D  1 246 ? 14.945  4.243   -40.770 1.00 7.44  ? 246 PHE D C   1 
ATOM   8435 O  O   . PHE D  1 246 ? 16.020  4.395   -41.364 1.00 8.40  ? 246 PHE D O   1 
ATOM   8436 C  CB  . PHE D  1 246 ? 13.813  2.043   -41.421 1.00 7.24  ? 246 PHE D CB  1 
ATOM   8437 C  CG  . PHE D  1 246 ? 15.094  1.390   -41.970 1.00 7.35  ? 246 PHE D CG  1 
ATOM   8438 C  CD1 . PHE D  1 246 ? 15.193  1.130   -43.340 1.00 7.62  ? 246 PHE D CD1 1 
ATOM   8439 C  CD2 . PHE D  1 246 ? 16.143  1.050   -41.092 1.00 7.61  ? 246 PHE D CD2 1 
ATOM   8440 C  CE1 . PHE D  1 246 ? 16.333  0.547   -43.876 1.00 7.05  ? 246 PHE D CE1 1 
ATOM   8441 C  CE2 . PHE D  1 246 ? 17.297  0.473   -41.614 1.00 8.30  ? 246 PHE D CE2 1 
ATOM   8442 C  CZ  . PHE D  1 246 ? 17.406  0.255   -43.008 1.00 8.53  ? 246 PHE D CZ  1 
ATOM   8443 N  N   . ARG D  1 247 ? 14.800  4.534   -39.499 1.00 6.97  ? 247 ARG D N   1 
ATOM   8444 C  CA  . ARG D  1 247 ? 15.891  5.031   -38.658 1.00 6.53  ? 247 ARG D CA  1 
ATOM   8445 C  C   . ARG D  1 247 ? 16.618  3.831   -38.042 1.00 7.33  ? 247 ARG D C   1 
ATOM   8446 O  O   . ARG D  1 247 ? 15.988  2.818   -37.706 1.00 7.24  ? 247 ARG D O   1 
ATOM   8447 C  CB  . ARG D  1 247 ? 15.307  5.902   -37.526 1.00 6.26  ? 247 ARG D CB  1 
ATOM   8448 C  CG  . ARG D  1 247 ? 16.300  6.834   -36.840 1.00 6.51  ? 247 ARG D CG  1 
ATOM   8449 C  CD  . ARG D  1 247 ? 15.592  7.552   -35.685 1.00 7.67  ? 247 ARG D CD  1 
ATOM   8450 N  NE  . ARG D  1 247 ? 16.420  8.635   -35.157 1.00 7.57  ? 247 ARG D NE  1 
ATOM   8451 C  CZ  . ARG D  1 247 ? 16.159  9.313   -34.044 1.00 8.30  ? 247 ARG D CZ  1 
ATOM   8452 N  NH1 . ARG D  1 247 ? 15.087  9.026   -33.319 1.00 8.87  ? 247 ARG D NH1 1 
ATOM   8453 N  NH2 . ARG D  1 247 ? 16.977  10.282  -33.653 1.00 7.91  ? 247 ARG D NH2 1 
ATOM   8454 N  N   . GLN D  1 248 ? 17.940  3.993   -37.842 1.00 7.12  ? 248 GLN D N   1 
ATOM   8455 C  CA  . GLN D  1 248 ? 18.692  3.014   -37.013 1.00 7.39  ? 248 GLN D CA  1 
ATOM   8456 C  C   . GLN D  1 248 ? 18.176  2.943   -35.576 1.00 7.24  ? 248 GLN D C   1 
ATOM   8457 O  O   . GLN D  1 248 ? 17.654  3.958   -35.040 1.00 7.08  ? 248 GLN D O   1 
ATOM   8458 C  CB  . GLN D  1 248 ? 20.190  3.452   -36.984 1.00 7.01  ? 248 GLN D CB  1 
ATOM   8459 C  CG  . GLN D  1 248 ? 20.874  3.353   -38.363 1.00 8.19  ? 248 GLN D CG  1 
ATOM   8460 C  CD  . GLN D  1 248 ? 20.828  1.944   -38.983 1.00 8.10  ? 248 GLN D CD  1 
ATOM   8461 O  OE1 . GLN D  1 248 ? 19.935  1.591   -39.761 1.00 9.47  ? 248 GLN D OE1 1 
ATOM   8462 N  NE2 . GLN D  1 248 ? 21.861  1.162   -38.690 1.00 9.76  ? 248 GLN D NE2 1 
ATOM   8463 N  N   . VAL D  1 249 ? 18.410  1.808   -34.935 1.00 7.35  ? 249 VAL D N   1 
ATOM   8464 C  CA  . VAL D  1 249 ? 18.017  1.706   -33.510 1.00 8.21  ? 249 VAL D CA  1 
ATOM   8465 C  C   . VAL D  1 249 ? 18.902  2.600   -32.611 1.00 8.86  ? 249 VAL D C   1 
ATOM   8466 O  O   . VAL D  1 249 ? 20.016  2.990   -32.988 1.00 8.83  ? 249 VAL D O   1 
ATOM   8467 C  CB  . VAL D  1 249 ? 18.038  0.259   -32.949 1.00 8.24  ? 249 VAL D CB  1 
ATOM   8468 C  CG1 . VAL D  1 249 ? 16.970  -0.614  -33.646 1.00 9.31  ? 249 VAL D CG1 1 
ATOM   8469 C  CG2 . VAL D  1 249 ? 19.463  -0.355  -33.030 1.00 9.56  ? 249 VAL D CG2 1 
ATOM   8470 N  N   . GLN D  1 250 ? 18.320  3.012   -31.527 1.00 7.90  ? 250 GLN D N   1 
ATOM   8471 C  CA  . GLN D  1 250 ? 18.888  4.027   -30.577 1.00 8.67  ? 250 GLN D CA  1 
ATOM   8472 C  C   . GLN D  1 250 ? 19.366  3.461   -29.270 1.00 9.22  ? 250 GLN D C   1 
ATOM   8473 O  O   . GLN D  1 250 ? 18.926  2.377   -28.825 1.00 10.21 ? 250 GLN D O   1 
ATOM   8474 C  CB  . GLN D  1 250 ? 17.720  5.008   -30.250 1.00 7.66  ? 250 GLN D CB  1 
ATOM   8475 C  CG  . GLN D  1 250 ? 17.086  5.658   -31.526 1.00 8.81  ? 250 GLN D CG  1 
ATOM   8476 C  CD  . GLN D  1 250 ? 18.034  6.550   -32.272 1.00 8.32  ? 250 GLN D CD  1 
ATOM   8477 O  OE1 . GLN D  1 250 ? 18.493  7.563   -31.701 1.00 9.75  ? 250 GLN D OE1 1 
ATOM   8478 N  NE2 . GLN D  1 250 ? 18.272  6.297   -33.529 1.00 8.09  ? 250 GLN D NE2 1 
ATOM   8479 N  N   . LYS D  1 251 ? 20.205  4.242   -28.606 1.00 8.54  ? 251 LYS D N   1 
ATOM   8480 C  CA  . LYS D  1 251 ? 20.610  3.855   -27.228 1.00 10.33 ? 251 LYS D CA  1 
ATOM   8481 C  C   . LYS D  1 251 ? 19.374  3.762   -26.300 1.00 8.95  ? 251 LYS D C   1 
ATOM   8482 O  O   . LYS D  1 251 ? 18.383  4.506   -26.416 1.00 10.41 ? 251 LYS D O   1 
ATOM   8483 C  CB  . LYS D  1 251 ? 21.510  4.971   -26.724 1.00 10.44 ? 251 LYS D CB  1 
ATOM   8484 C  CG  . LYS D  1 251 ? 22.877  4.988   -27.389 1.00 11.71 ? 251 LYS D CG  1 
ATOM   8485 C  CD  . LYS D  1 251 ? 23.718  3.883   -26.786 1.00 11.66 ? 251 LYS D CD  1 
ATOM   8486 C  CE  . LYS D  1 251 ? 25.201  3.873   -27.201 1.00 12.50 ? 251 LYS D CE  1 
ATOM   8487 N  NZ  . LYS D  1 251 ? 25.361  3.811   -28.694 1.00 11.36 ? 251 LYS D NZ  1 
ATOM   8488 N  N   . PHE D  1 252 ? 19.446  2.816   -25.396 1.00 10.53 ? 252 PHE D N   1 
ATOM   8489 C  CA  . PHE D  1 252 ? 18.373  2.690   -24.434 1.00 11.27 ? 252 PHE D CA  1 
ATOM   8490 C  C   . PHE D  1 252 ? 18.218  3.814   -23.420 1.00 13.99 ? 252 PHE D C   1 
ATOM   8491 O  O   . PHE D  1 252 ? 17.119  4.020   -22.883 1.00 14.07 ? 252 PHE D O   1 
ATOM   8492 C  CB  . PHE D  1 252 ? 18.531  1.319   -23.696 1.00 13.38 ? 252 PHE D CB  1 
ATOM   8493 C  CG  . PHE D  1 252 ? 17.960  0.216   -24.535 1.00 16.56 ? 252 PHE D CG  1 
ATOM   8494 C  CD1 . PHE D  1 252 ? 16.612  -0.111  -24.390 1.00 19.60 ? 252 PHE D CD1 1 
ATOM   8495 C  CD2 . PHE D  1 252 ? 18.752  -0.432  -25.515 1.00 20.45 ? 252 PHE D CD2 1 
ATOM   8496 C  CE1 . PHE D  1 252 ? 16.042  -1.058  -25.224 1.00 22.57 ? 252 PHE D CE1 1 
ATOM   8497 C  CE2 . PHE D  1 252 ? 18.157  -1.421  -26.376 1.00 20.30 ? 252 PHE D CE2 1 
ATOM   8498 C  CZ  . PHE D  1 252 ? 16.825  -1.676  -26.201 1.00 21.66 ? 252 PHE D CZ  1 
ATOM   8499 N  N   . ASP D  1 253 ? 19.302  4.562   -23.031 1.00 13.96 ? 253 ASP D N   1 
ATOM   8500 C  CA  . ASP D  1 253 ? 19.082  5.676   -22.037 1.00 15.50 ? 253 ASP D CA  1 
ATOM   8501 C  C   . ASP D  1 253 ? 18.414  5.184   -20.730 1.00 15.66 ? 253 ASP D C   1 
ATOM   8502 O  O   . ASP D  1 253 ? 17.543  5.868   -20.178 1.00 18.15 ? 253 ASP D O   1 
ATOM   8503 C  CB  . ASP D  1 253 ? 18.236  6.841   -22.623 1.00 15.95 ? 253 ASP D CB  1 
ATOM   8504 C  CG  . ASP D  1 253 ? 18.940  7.555   -23.810 1.00 17.66 ? 253 ASP D CG  1 
ATOM   8505 O  OD1 . ASP D  1 253 ? 20.199  7.492   -23.959 1.00 18.59 ? 253 ASP D OD1 1 
ATOM   8506 O  OD2 . ASP D  1 253 ? 18.216  8.206   -24.568 1.00 18.32 ? 253 ASP D OD2 1 
ATOM   8507 N  N   . GLU D  1 254 ? 18.853  3.982   -20.317 1.00 15.95 ? 254 GLU D N   1 
ATOM   8508 C  CA  . GLU D  1 254 ? 18.399  3.303   -19.058 1.00 17.81 ? 254 GLU D CA  1 
ATOM   8509 C  C   . GLU D  1 254 ? 16.965  2.763   -19.084 1.00 17.66 ? 254 GLU D C   1 
ATOM   8510 O  O   . GLU D  1 254 ? 16.517  2.203   -18.046 1.00 17.62 ? 254 GLU D O   1 
ATOM   8511 C  CB  . GLU D  1 254 ? 18.548  4.233   -17.826 1.00 20.95 ? 254 GLU D CB  1 
ATOM   8512 C  CG  . GLU D  1 254 ? 20.000  4.664   -17.645 1.00 28.47 ? 254 GLU D CG  1 
ATOM   8513 C  CD  . GLU D  1 254 ? 20.122  5.637   -16.474 1.00 40.74 ? 254 GLU D CD  1 
ATOM   8514 O  OE1 . GLU D  1 254 ? 20.039  5.139   -15.314 1.00 40.57 ? 254 GLU D OE1 1 
ATOM   8515 O  OE2 . GLU D  1 254 ? 20.252  6.877   -16.702 1.00 44.99 ? 254 GLU D OE2 1 
ATOM   8516 N  N   . ARG D  1 255 ? 16.253  2.855   -20.199 1.00 15.25 ? 255 ARG D N   1 
ATOM   8517 C  CA  . ARG D  1 255 ? 14.889  2.292   -20.301 1.00 14.03 ? 255 ARG D CA  1 
ATOM   8518 C  C   . ARG D  1 255 ? 14.930  0.763   -20.275 1.00 14.75 ? 255 ARG D C   1 
ATOM   8519 O  O   . ARG D  1 255 ? 15.878  0.102   -20.797 1.00 16.37 ? 255 ARG D O   1 
ATOM   8520 C  CB  . ARG D  1 255 ? 14.244  2.670   -21.667 1.00 13.95 ? 255 ARG D CB  1 
ATOM   8521 C  CG  . ARG D  1 255 ? 13.854  4.137   -21.682 1.00 12.82 ? 255 ARG D CG  1 
ATOM   8522 C  CD  . ARG D  1 255 ? 13.438  4.521   -23.140 1.00 12.95 ? 255 ARG D CD  1 
ATOM   8523 N  NE  . ARG D  1 255 ? 14.561  4.522   -24.075 1.00 13.53 ? 255 ARG D NE  1 
ATOM   8524 C  CZ  . ARG D  1 255 ? 14.466  4.847   -25.360 1.00 13.12 ? 255 ARG D CZ  1 
ATOM   8525 N  NH1 . ARG D  1 255 ? 13.293  5.191   -25.877 1.00 10.47 ? 255 ARG D NH1 1 
ATOM   8526 N  NH2 . ARG D  1 255 ? 15.546  4.828   -26.130 1.00 11.66 ? 255 ARG D NH2 1 
ATOM   8527 N  N   . LEU D  1 256 ? 13.861  0.164   -19.682 1.00 14.36 ? 256 LEU D N   1 
ATOM   8528 C  CA  . LEU D  1 256 ? 13.488  -1.171  -19.979 1.00 12.93 ? 256 LEU D CA  1 
ATOM   8529 C  C   . LEU D  1 256 ? 12.292  -1.166  -20.922 1.00 12.57 ? 256 LEU D C   1 
ATOM   8530 O  O   . LEU D  1 256 ? 11.621  -0.137  -21.203 1.00 14.07 ? 256 LEU D O   1 
ATOM   8531 C  CB  . LEU D  1 256 ? 13.057  -1.875  -18.720 1.00 14.94 ? 256 LEU D CB  1 
ATOM   8532 C  CG  . LEU D  1 256 ? 14.157  -1.872  -17.678 1.00 14.06 ? 256 LEU D CG  1 
ATOM   8533 C  CD1 . LEU D  1 256 ? 13.510  -2.490  -16.405 1.00 18.90 ? 256 LEU D CD1 1 
ATOM   8534 C  CD2 . LEU D  1 256 ? 15.416  -2.618  -18.105 1.00 20.38 ? 256 LEU D CD2 1 
ATOM   8535 N  N   . VAL D  1 257 ? 12.102  -2.295  -21.552 1.00 11.92 ? 257 VAL D N   1 
ATOM   8536 C  CA  . VAL D  1 257 ? 10.931  -2.576  -22.415 1.00 12.33 ? 257 VAL D CA  1 
ATOM   8537 C  C   . VAL D  1 257 ? 10.086  -3.588  -21.668 1.00 12.37 ? 257 VAL D C   1 
ATOM   8538 O  O   . VAL D  1 257 ? 10.537  -4.645  -21.240 1.00 12.73 ? 257 VAL D O   1 
ATOM   8539 C  CB  . VAL D  1 257 ? 11.261  -3.176  -23.820 1.00 12.79 ? 257 VAL D CB  1 
ATOM   8540 C  CG1 . VAL D  1 257 ? 10.013  -3.614  -24.555 1.00 11.37 ? 257 VAL D CG1 1 
ATOM   8541 C  CG2 . VAL D  1 257 ? 12.041  -2.135  -24.587 1.00 11.10 ? 257 VAL D CG2 1 
ATOM   8542 N  N   . TYR D  1 258 ? 8.846   -3.230  -21.409 1.00 11.31 ? 258 TYR D N   1 
ATOM   8543 C  CA  . TYR D  1 258 ? 7.914   -4.056  -20.620 1.00 10.72 ? 258 TYR D CA  1 
ATOM   8544 C  C   . TYR D  1 258 ? 7.070   -4.915  -21.498 1.00 11.18 ? 258 TYR D C   1 
ATOM   8545 O  O   . TYR D  1 258 ? 6.730   -4.520  -22.607 1.00 11.47 ? 258 TYR D O   1 
ATOM   8546 C  CB  . TYR D  1 258 ? 7.042   -3.123  -19.696 1.00 12.37 ? 258 TYR D CB  1 
ATOM   8547 C  CG  . TYR D  1 258 ? 7.907   -2.291  -18.799 1.00 13.37 ? 258 TYR D CG  1 
ATOM   8548 C  CD1 . TYR D  1 258 ? 8.403   -2.842  -17.608 1.00 15.54 ? 258 TYR D CD1 1 
ATOM   8549 C  CD2 . TYR D  1 258 ? 8.355   -1.012  -19.212 1.00 15.72 ? 258 TYR D CD2 1 
ATOM   8550 C  CE1 . TYR D  1 258 ? 9.299   -2.123  -16.833 1.00 15.63 ? 258 TYR D CE1 1 
ATOM   8551 C  CE2 . TYR D  1 258 ? 9.206   -0.276  -18.396 1.00 16.58 ? 258 TYR D CE2 1 
ATOM   8552 C  CZ  . TYR D  1 258 ? 9.674   -0.843  -17.227 1.00 16.35 ? 258 TYR D CZ  1 
ATOM   8553 O  OH  . TYR D  1 258 ? 10.548  -0.020  -16.464 1.00 17.29 ? 258 TYR D OH  1 
ATOM   8554 N  N   . THR D  1 259 ? 6.872   -6.189  -21.113 1.00 10.40 ? 259 THR D N   1 
ATOM   8555 C  CA  . THR D  1 259 ? 6.169   -7.074  -21.978 1.00 9.61  ? 259 THR D CA  1 
ATOM   8556 C  C   . THR D  1 259 ? 4.899   -7.570  -21.271 1.00 10.45 ? 259 THR D C   1 
ATOM   8557 O  O   . THR D  1 259 ? 4.864   -7.720  -20.015 1.00 11.27 ? 259 THR D O   1 
ATOM   8558 C  CB  . THR D  1 259 ? 7.013   -8.319  -22.371 1.00 9.67  ? 259 THR D CB  1 
ATOM   8559 O  OG1 . THR D  1 259 ? 7.508   -8.947  -21.170 1.00 11.19 ? 259 THR D OG1 1 
ATOM   8560 C  CG2 . THR D  1 259 ? 8.319   -7.864  -23.146 1.00 10.58 ? 259 THR D CG2 1 
ATOM   8561 N  N   . SER D  1 260 ? 3.919   -7.892  -22.075 1.00 10.60 ? 260 SER D N   1 
ATOM   8562 C  CA  . SER D  1 260 ? 2.630   -8.483  -21.539 1.00 11.29 ? 260 SER D CA  1 
ATOM   8563 C  C   . SER D  1 260 ? 2.701   -10.019 -21.508 1.00 13.47 ? 260 SER D C   1 
ATOM   8564 O  O   . SER D  1 260 ? 1.680   -10.721 -21.188 1.00 15.62 ? 260 SER D O   1 
ATOM   8565 C  CB  . SER D  1 260 ? 1.494   -7.944  -22.374 1.00 13.00 ? 260 SER D CB  1 
ATOM   8566 O  OG  . SER D  1 260 ? 1.594   -8.513  -23.673 1.00 12.82 ? 260 SER D OG  1 
ATOM   8567 N  N   . PHE D  1 261 ? 3.870   -10.577 -21.787 1.00 13.34 ? 261 PHE D N   1 
ATOM   8568 C  CA  . PHE D  1 261 ? 4.038   -12.038 -21.951 1.00 14.70 ? 261 PHE D CA  1 
ATOM   8569 C  C   . PHE D  1 261 ? 5.369   -12.329 -21.316 1.00 16.70 ? 261 PHE D C   1 
ATOM   8570 O  O   . PHE D  1 261 ? 6.222   -11.495 -21.109 1.00 14.87 ? 261 PHE D O   1 
ATOM   8571 C  CB  . PHE D  1 261 ? 4.022   -12.518 -23.407 1.00 14.71 ? 261 PHE D CB  1 
ATOM   8572 C  CG  . PHE D  1 261 ? 5.065   -11.831 -24.257 1.00 14.33 ? 261 PHE D CG  1 
ATOM   8573 C  CD1 . PHE D  1 261 ? 6.385   -12.352 -24.411 1.00 16.09 ? 261 PHE D CD1 1 
ATOM   8574 C  CD2 . PHE D  1 261 ? 4.784   -10.571 -24.856 1.00 14.39 ? 261 PHE D CD2 1 
ATOM   8575 C  CE1 . PHE D  1 261 ? 7.359   -11.680 -25.161 1.00 17.54 ? 261 PHE D CE1 1 
ATOM   8576 C  CE2 . PHE D  1 261 ? 5.808   -9.939  -25.594 1.00 16.28 ? 261 PHE D CE2 1 
ATOM   8577 C  CZ  . PHE D  1 261 ? 7.051   -10.471 -25.777 1.00 16.02 ? 261 PHE D CZ  1 
ATOM   8578 N  N   . SER D  1 262 ? 5.555   -13.600 -20.926 1.00 23.73 ? 262 SER D N   1 
ATOM   8579 C  CA  . SER D  1 262 ? 6.880   -14.062 -20.477 1.00 29.96 ? 262 SER D CA  1 
ATOM   8580 C  C   . SER D  1 262 ? 7.356   -15.062 -21.534 1.00 31.68 ? 262 SER D C   1 
ATOM   8581 O  O   . SER D  1 262 ? 8.536   -15.052 -21.972 1.00 34.78 ? 262 SER D O   1 
ATOM   8582 C  CB  . SER D  1 262 ? 6.787   -14.732 -19.129 1.00 33.92 ? 262 SER D CB  1 
ATOM   8583 O  OG  . SER D  1 262 ? 5.956   -14.010 -18.256 1.00 34.51 ? 262 SER D OG  1 
ATOM   8584 N  N   . GLN D  1 263 ? 6.435   -15.974 -21.791 1.00 39.37 ? 263 GLN D N   1 
ATOM   8585 C  CA  . GLN D  1 263 ? 6.109   -16.651 -23.069 1.00 50.93 ? 263 GLN D CA  1 
ATOM   8586 C  C   . GLN D  1 263 ? 7.204   -17.237 -23.981 1.00 57.57 ? 263 GLN D C   1 
ATOM   8587 O  O   . GLN D  1 263 ? 8.407   -17.011 -23.746 1.00 65.52 ? 263 GLN D O   1 
ATOM   8588 C  CB  . GLN D  1 263 ? 5.005   -15.893 -23.844 1.00 48.01 ? 263 GLN D CB  1 
ATOM   8589 C  CG  . GLN D  1 263 ? 3.562   -16.370 -23.600 1.00 45.97 ? 263 GLN D CG  1 
ATOM   8590 C  CD  . GLN D  1 263 ? 2.815   -15.616 -22.484 1.00 50.96 ? 263 GLN D CD  1 
ATOM   8591 O  OE1 . GLN D  1 263 ? 3.321   -15.453 -21.346 1.00 41.78 ? 263 GLN D OE1 1 
ATOM   8592 N  NE2 . GLN D  1 263 ? 1.582   -15.147 -22.810 1.00 53.10 ? 263 GLN D NE2 1 
ATOM   8593 O  OXT . GLN D  1 263 ? 6.873   -17.963 -24.943 1.00 59.83 ? 263 GLN D OXT 1 
HETATM 8594 ZN ZN  . ZN  E  2 .   ? 22.929  0.704   12.205  1.00 8.09  ? 301 ZN  A ZN  1 
HETATM 8595 CL CL1 . 6YQ F  3 .   ? 26.000  3.255   7.610   1.00 15.10 ? 302 6YQ A CL1 1 
HETATM 8596 C  C6  . 6YQ F  3 .   ? 25.737  4.107   9.080   1.00 13.67 ? 302 6YQ A C6  1 
HETATM 8597 C  C1  . 6YQ F  3 .   ? 24.700  3.749   10.008  1.00 12.30 ? 302 6YQ A C1  1 
HETATM 8598 S  S7  . 6YQ F  3 .   ? 23.678  2.295   9.731   1.00 12.10 ? 302 6YQ A S7  1 
HETATM 8599 O  O9  . 6YQ F  3 .   ? 22.916  2.484   8.501   1.00 9.88  ? 302 6YQ A O9  1 
HETATM 8600 N  N10 . 6YQ F  3 .   ? 22.762  2.184   10.988  1.00 10.75 ? 302 6YQ A N10 1 
HETATM 8601 O  O8  . 6YQ F  3 .   ? 24.649  1.114   9.772   1.00 11.20 ? 302 6YQ A O8  1 
HETATM 8602 C  C5  . 6YQ F  3 .   ? 26.584  5.229   9.416   1.00 15.73 ? 302 6YQ A C5  1 
HETATM 8603 C  C4  . 6YQ F  3 .   ? 26.388  5.908   10.556  1.00 19.17 ? 302 6YQ A C4  1 
HETATM 8604 C  C3  . 6YQ F  3 .   ? 25.377  5.606   11.488  1.00 17.82 ? 302 6YQ A C3  1 
HETATM 8605 C  C2  . 6YQ F  3 .   ? 24.530  4.492   11.243  1.00 13.53 ? 302 6YQ A C2  1 
HETATM 8606 C  C11 . 6YQ F  3 .   ? 27.295  7.077   10.719  1.00 24.85 ? 302 6YQ A C11 1 
HETATM 8607 O  O12 . 6YQ F  3 .   ? 28.230  7.159   9.922   1.00 27.83 ? 302 6YQ A O12 1 
HETATM 8608 C  C13 . 6YQ F  3 .   ? 26.904  8.139   11.694  1.00 29.45 ? 302 6YQ A C13 1 
HETATM 8609 N  N14 . 6YQ F  3 .   ? 27.669  9.361   11.526  1.00 27.61 ? 302 6YQ A N14 1 
HETATM 8610 C  C18 . 6YQ F  3 .   ? 27.632  10.297  10.542  1.00 29.74 ? 302 6YQ A C18 1 
HETATM 8611 C  C20 . 6YQ F  3 .   ? 26.807  10.448  9.398   1.00 28.48 ? 302 6YQ A C20 1 
HETATM 8612 C  C21 . 6YQ F  3 .   ? 27.004  11.552  8.552   1.00 27.42 ? 302 6YQ A C21 1 
HETATM 8613 C  C22 . 6YQ F  3 .   ? 27.999  12.510  8.836   1.00 28.93 ? 302 6YQ A C22 1 
HETATM 8614 C  C23 . 6YQ F  3 .   ? 28.818  12.354  9.975   1.00 29.21 ? 302 6YQ A C23 1 
HETATM 8615 C  C19 . 6YQ F  3 .   ? 28.620  11.234  10.822  1.00 30.41 ? 302 6YQ A C19 1 
HETATM 8616 N  N17 . 6YQ F  3 .   ? 29.301  10.896  11.954  1.00 33.62 ? 302 6YQ A N17 1 
HETATM 8617 C  C16 . 6YQ F  3 .   ? 28.695  9.736   12.381  1.00 36.06 ? 302 6YQ A C16 1 
HETATM 8618 C  C1  . EDO G  4 .   ? 23.564  5.374   15.467  1.00 22.39 ? 303 EDO A C1  1 
HETATM 8619 O  O1  . EDO G  4 .   ? 23.968  6.673   15.930  1.00 24.62 ? 303 EDO A O1  1 
HETATM 8620 C  C2  . EDO G  4 .   ? 24.720  4.746   14.707  1.00 29.95 ? 303 EDO A C2  1 
HETATM 8621 O  O2  . EDO G  4 .   ? 26.011  5.285   14.883  1.00 28.70 ? 303 EDO A O2  1 
HETATM 8622 C  C1  . EDO H  4 .   ? 27.713  9.656   16.192  1.00 37.80 ? 304 EDO A C1  1 
HETATM 8623 O  O1  . EDO H  4 .   ? 28.209  9.494   17.496  1.00 36.10 ? 304 EDO A O1  1 
HETATM 8624 C  C2  . EDO H  4 .   ? 28.152  8.345   15.575  1.00 28.69 ? 304 EDO A C2  1 
HETATM 8625 O  O2  . EDO H  4 .   ? 27.188  7.531   14.951  1.00 30.45 ? 304 EDO A O2  1 
HETATM 8626 C  C1  . EDO I  4 .   ? 26.307  -8.676  29.963  1.00 22.40 ? 305 EDO A C1  1 
HETATM 8627 O  O1  . EDO I  4 .   ? 25.959  -9.733  29.074  1.00 25.38 ? 305 EDO A O1  1 
HETATM 8628 C  C2  . EDO I  4 .   ? 27.252  -9.166  31.076  1.00 26.64 ? 305 EDO A C2  1 
HETATM 8629 O  O2  . EDO I  4 .   ? 28.561  -9.442  30.585  1.00 25.92 ? 305 EDO A O2  1 
HETATM 8630 C  C1  . EDO J  4 .   ? 31.712  -9.128  -3.267  1.00 29.25 ? 306 EDO A C1  1 
HETATM 8631 O  O1  . EDO J  4 .   ? 30.447  -8.825  -2.607  1.00 17.02 ? 306 EDO A O1  1 
HETATM 8632 C  C2  . EDO J  4 .   ? 31.598  -9.011  -4.780  1.00 26.56 ? 306 EDO A C2  1 
HETATM 8633 O  O2  . EDO J  4 .   ? 30.743  -7.942  -5.172  1.00 36.52 ? 306 EDO A O2  1 
HETATM 8634 ZN ZN  . ZN  K  2 .   ? -8.114  3.805   4.919   1.00 6.78  ? 301 ZN  B ZN  1 
HETATM 8635 CL CL1 . 6YQ L  3 .   ? -10.367 6.962   9.551   1.00 15.89 ? 302 6YQ B CL1 1 
HETATM 8636 C  C6  . 6YQ L  3 .   ? -9.991  7.760   8.049   1.00 15.22 ? 302 6YQ B C6  1 
HETATM 8637 C  C1  . 6YQ L  3 .   ? -9.119  7.270   7.067   1.00 12.28 ? 302 6YQ B C1  1 
HETATM 8638 S  S7  . 6YQ L  3 .   ? -8.364  5.628   7.301   1.00 9.72  ? 302 6YQ B S7  1 
HETATM 8639 O  O9  . 6YQ L  3 .   ? -7.562  5.715   8.503   1.00 7.76  ? 302 6YQ B O9  1 
HETATM 8640 N  N10 . 6YQ L  3 .   ? -7.550  5.258   5.943   1.00 10.62 ? 302 6YQ B N10 1 
HETATM 8641 O  O8  . 6YQ L  3 .   ? -9.514  4.764   7.341   1.00 9.87  ? 302 6YQ B O8  1 
HETATM 8642 C  C5  . 6YQ L  3 .   ? -10.575 8.994   7.856   1.00 16.77 ? 302 6YQ B C5  1 
HETATM 8643 C  C4  . 6YQ L  3 .   ? -10.375 9.751   6.729   1.00 16.77 ? 302 6YQ B C4  1 
HETATM 8644 C  C3  . 6YQ L  3 .   ? -9.530  9.291   5.706   1.00 15.71 ? 302 6YQ B C3  1 
HETATM 8645 C  C2  . 6YQ L  3 .   ? -8.900  8.005   5.898   1.00 15.38 ? 302 6YQ B C2  1 
HETATM 8646 C  C11 . 6YQ L  3 .   ? -11.064 11.103  6.694   1.00 22.79 ? 302 6YQ B C11 1 
HETATM 8647 O  O12 . 6YQ L  3 .   ? -11.710 11.487  7.733   1.00 25.41 ? 302 6YQ B O12 1 
HETATM 8648 C  C13 . 6YQ L  3 .   ? -10.838 11.983  5.511   1.00 27.15 ? 302 6YQ B C13 1 
HETATM 8649 N  N14 . 6YQ L  3 .   ? -11.410 13.294  5.868   1.00 31.82 ? 302 6YQ B N14 1 
HETATM 8650 C  C18 . 6YQ L  3 .   ? -10.801 14.367  6.448   1.00 33.32 ? 302 6YQ B C18 1 
HETATM 8651 C  C20 . 6YQ L  3 .   ? -9.462  14.580  6.770   1.00 33.03 ? 302 6YQ B C20 1 
HETATM 8652 C  C21 . 6YQ L  3 .   ? -9.135  15.850  7.320   1.00 34.61 ? 302 6YQ B C21 1 
HETATM 8653 C  C22 . 6YQ L  3 .   ? -10.121 16.867  7.503   1.00 37.73 ? 302 6YQ B C22 1 
HETATM 8654 C  C23 . 6YQ L  3 .   ? -11.470 16.630  7.151   1.00 37.31 ? 302 6YQ B C23 1 
HETATM 8655 C  C19 . 6YQ L  3 .   ? -11.754 15.365  6.622   1.00 31.86 ? 302 6YQ B C19 1 
HETATM 8656 N  N17 . 6YQ L  3 .   ? -12.962 14.896  6.220   1.00 31.97 ? 302 6YQ B N17 1 
HETATM 8657 C  C16 . 6YQ L  3 .   ? -12.742 13.620  5.778   1.00 31.79 ? 302 6YQ B C16 1 
HETATM 8658 S  S   . SO4 M  5 .   ? -11.747 12.217  1.761   1.00 41.23 ? 303 SO4 B S   1 
HETATM 8659 O  O1  . SO4 M  5 .   ? -11.023 13.532  1.888   1.00 43.33 ? 303 SO4 B O1  1 
HETATM 8660 O  O2  . SO4 M  5 .   ? -12.108 12.128  0.304   1.00 28.74 ? 303 SO4 B O2  1 
HETATM 8661 O  O3  . SO4 M  5 .   ? -10.955 11.058  2.302   1.00 33.18 ? 303 SO4 B O3  1 
HETATM 8662 O  O4  . SO4 M  5 .   ? -13.056 12.183  2.528   1.00 43.85 ? 303 SO4 B O4  1 
HETATM 8663 C  C1  . EDO N  4 .   ? -9.566  7.940   2.753   1.00 22.43 ? 304 EDO B C1  1 
HETATM 8664 O  O1  . EDO N  4 .   ? -10.632 8.400   2.019   1.00 19.82 ? 304 EDO B O1  1 
HETATM 8665 C  C2  . EDO N  4 .   ? -8.430  7.395   1.924   1.00 21.23 ? 304 EDO B C2  1 
HETATM 8666 O  O2  . EDO N  4 .   ? -7.908  8.386   1.085   1.00 22.17 ? 304 EDO B O2  1 
HETATM 8667 C  C1  . EDO O  4 .   ? -17.563 -3.637  21.543  1.00 20.21 ? 305 EDO B C1  1 
HETATM 8668 O  O1  . EDO O  4 .   ? -16.378 -3.624  20.678  1.00 18.84 ? 305 EDO B O1  1 
HETATM 8669 C  C2  . EDO O  4 .   ? -17.084 -3.430  22.967  1.00 23.93 ? 305 EDO B C2  1 
HETATM 8670 O  O2  . EDO O  4 .   ? -16.068 -2.468  23.019  1.00 27.18 ? 305 EDO B O2  1 
HETATM 8671 ZN ZN  . ZN  P  2 .   ? 37.436  2.552   -30.874 1.00 10.38 ? 301 ZN  C ZN  1 
HETATM 8672 CL CL1 . 6YQ Q  3 .   ? 40.548  5.009   -35.473 1.00 14.93 ? 302 6YQ C CL1 1 
HETATM 8673 C  C6  . 6YQ Q  3 .   ? 40.309  5.920   -34.022 1.00 14.27 ? 302 6YQ C C6  1 
HETATM 8674 C  C1  . 6YQ Q  3 .   ? 39.324  5.536   -33.080 1.00 13.62 ? 302 6YQ C C1  1 
HETATM 8675 S  S7  . 6YQ Q  3 .   ? 38.254  4.095   -33.339 1.00 12.54 ? 302 6YQ C S7  1 
HETATM 8676 O  O9  . 6YQ Q  3 .   ? 37.485  4.224   -34.592 1.00 10.59 ? 302 6YQ C O9  1 
HETATM 8677 N  N10 . 6YQ Q  3 .   ? 37.176  3.969   -32.098 1.00 12.77 ? 302 6YQ C N10 1 
HETATM 8678 O  O8  . 6YQ Q  3 .   ? 39.124  2.935   -33.313 1.00 11.85 ? 302 6YQ C O8  1 
HETATM 8679 C  C5  . 6YQ Q  3 .   ? 41.171  6.974   -33.775 1.00 18.60 ? 302 6YQ C C5  1 
HETATM 8680 C  C4  . 6YQ Q  3 .   ? 41.021  7.699   -32.606 1.00 20.09 ? 302 6YQ C C4  1 
HETATM 8681 C  C3  . 6YQ Q  3 .   ? 40.040  7.372   -31.683 1.00 17.61 ? 302 6YQ C C3  1 
HETATM 8682 C  C2  . 6YQ Q  3 .   ? 39.185  6.270   -31.896 1.00 15.30 ? 302 6YQ C C2  1 
HETATM 8683 C  C11 . 6YQ Q  3 .   ? 41.898  8.851   -32.364 1.00 23.21 ? 302 6YQ C C11 1 
HETATM 8684 O  O12 . 6YQ Q  3 .   ? 42.819  8.971   -33.176 1.00 28.75 ? 302 6YQ C O12 1 
HETATM 8685 C  C13 . 6YQ Q  3 .   ? 41.567  9.872   -31.317 1.00 26.83 ? 302 6YQ C C13 1 
HETATM 8686 N  N14 . 6YQ Q  3 .   ? 42.345  11.095  -31.572 1.00 29.48 ? 302 6YQ C N14 1 
HETATM 8687 C  C18 . 6YQ Q  3 .   ? 42.213  12.045  -32.521 1.00 28.99 ? 302 6YQ C C18 1 
HETATM 8688 C  C20 . 6YQ Q  3 .   ? 41.279  12.244  -33.543 1.00 26.20 ? 302 6YQ C C20 1 
HETATM 8689 C  C21 . 6YQ Q  3 .   ? 41.457  13.422  -34.339 1.00 26.60 ? 302 6YQ C C21 1 
HETATM 8690 C  C22 . 6YQ Q  3 .   ? 42.509  14.329  -34.147 1.00 30.34 ? 302 6YQ C C22 1 
HETATM 8691 C  C23 . 6YQ Q  3 .   ? 43.430  14.091  -33.131 1.00 28.92 ? 302 6YQ C C23 1 
HETATM 8692 C  C19 . 6YQ Q  3 .   ? 43.240  12.961  -32.342 1.00 33.52 ? 302 6YQ C C19 1 
HETATM 8693 N  N17 . 6YQ Q  3 .   ? 44.029  12.560  -31.326 1.00 34.35 ? 302 6YQ C N17 1 
HETATM 8694 C  C16 . 6YQ Q  3 .   ? 43.460  11.421  -30.869 1.00 40.70 ? 302 6YQ C C16 1 
HETATM 8695 S  S   . SO4 R  5 .   ? 42.316  10.746  -27.376 1.00 69.14 ? 303 SO4 C S   1 
HETATM 8696 O  O1  . SO4 R  5 .   ? 41.733  12.028  -27.863 1.00 68.14 ? 303 SO4 C O1  1 
HETATM 8697 O  O2  . SO4 R  5 .   ? 41.533  9.617   -27.982 1.00 48.09 ? 303 SO4 C O2  1 
HETATM 8698 O  O3  . SO4 R  5 .   ? 43.713  10.607  -27.842 1.00 68.97 ? 303 SO4 C O3  1 
HETATM 8699 O  O4  . SO4 R  5 .   ? 42.345  10.820  -25.869 1.00 52.51 ? 303 SO4 C O4  1 
HETATM 8700 C  C1  . EDO S  4 .   ? 46.080  -7.218  -47.665 1.00 24.66 ? 304 EDO C C1  1 
HETATM 8701 O  O1  . EDO S  4 .   ? 45.359  -6.033  -47.965 1.00 24.71 ? 304 EDO C O1  1 
HETATM 8702 C  C2  . EDO S  4 .   ? 46.456  -7.311  -46.184 1.00 23.88 ? 304 EDO C C2  1 
HETATM 8703 O  O2  . EDO S  4 .   ? 45.256  -7.178  -45.404 1.00 17.23 ? 304 EDO C O2  1 
HETATM 8704 C  C1  . EDO T  4 .   ? 37.862  7.331   -27.559 1.00 32.17 ? 305 EDO C C1  1 
HETATM 8705 O  O1  . EDO T  4 .   ? 38.263  8.700   -27.203 1.00 33.05 ? 305 EDO C O1  1 
HETATM 8706 C  C2  . EDO T  4 .   ? 39.038  6.468   -28.044 1.00 35.37 ? 305 EDO C C2  1 
HETATM 8707 O  O2  . EDO T  4 .   ? 40.382  7.041   -27.975 1.00 29.17 ? 305 EDO C O2  1 
HETATM 8708 ZN ZN  . ZN  U  2 .   ? 6.640   5.597   -38.392 1.00 7.07  ? 301 ZN  D ZN  1 
HETATM 8709 CL CL1 . 6YQ V  3 .   ? 4.462   8.841   -33.778 1.00 12.54 ? 302 6YQ D CL1 1 
HETATM 8710 C  C6  . 6YQ V  3 .   ? 4.719   9.645   -35.277 1.00 11.62 ? 302 6YQ D C6  1 
HETATM 8711 C  C1  . 6YQ V  3 .   ? 5.617   9.117   -36.275 1.00 10.27 ? 302 6YQ D C1  1 
HETATM 8712 S  S7  . 6YQ V  3 .   ? 6.378   7.469   -36.039 1.00 9.41  ? 302 6YQ D S7  1 
HETATM 8713 O  O9  . 6YQ V  3 .   ? 7.209   7.541   -34.856 1.00 8.19  ? 302 6YQ D O9  1 
HETATM 8714 N  N10 . 6YQ V  3 .   ? 7.275   7.117   -37.367 1.00 8.97  ? 302 6YQ D N10 1 
HETATM 8715 O  O8  . 6YQ V  3 .   ? 5.210   6.537   -36.005 1.00 8.71  ? 302 6YQ D O8  1 
HETATM 8716 C  C5  . 6YQ V  3 .   ? 4.123   10.821  -35.487 1.00 14.09 ? 302 6YQ D C5  1 
HETATM 8717 C  C4  . 6YQ V  3 .   ? 4.335   11.590  -36.581 1.00 15.43 ? 302 6YQ D C4  1 
HETATM 8718 C  C3  . 6YQ V  3 .   ? 5.166   11.114  -37.596 1.00 14.42 ? 302 6YQ D C3  1 
HETATM 8719 C  C2  . 6YQ V  3 .   ? 5.834   9.867   -37.452 1.00 14.26 ? 302 6YQ D C2  1 
HETATM 8720 C  C11 . 6YQ V  3 .   ? 3.647   12.923  -36.644 1.00 19.07 ? 302 6YQ D C11 1 
HETATM 8721 O  O12 . 6YQ V  3 .   ? 3.011   13.317  -35.634 1.00 22.65 ? 302 6YQ D O12 1 
HETATM 8722 C  C13 . 6YQ V  3 .   ? 3.929   13.756  -37.818 1.00 19.67 ? 302 6YQ D C13 1 
HETATM 8723 N  N14 . 6YQ V  3 .   ? 3.379   15.116  -37.510 1.00 23.57 ? 302 6YQ D N14 1 
HETATM 8724 C  C18 . 6YQ V  3 .   ? 4.017   16.217  -37.042 1.00 23.71 ? 302 6YQ D C18 1 
HETATM 8725 C  C20 . 6YQ V  3 .   ? 5.357   16.422  -36.715 1.00 23.98 ? 302 6YQ D C20 1 
HETATM 8726 C  C21 . 6YQ V  3 .   ? 5.763   17.737  -36.326 1.00 26.27 ? 302 6YQ D C21 1 
HETATM 8727 C  C22 . 6YQ V  3 .   ? 4.802   18.784  -36.205 1.00 22.68 ? 302 6YQ D C22 1 
HETATM 8728 C  C23 . 6YQ V  3 .   ? 3.459   18.492  -36.495 1.00 21.98 ? 302 6YQ D C23 1 
HETATM 8729 C  C19 . 6YQ V  3 .   ? 3.086   17.222  -36.892 1.00 21.24 ? 302 6YQ D C19 1 
HETATM 8730 N  N17 . 6YQ V  3 .   ? 1.837   16.771  -37.218 1.00 22.88 ? 302 6YQ D N17 1 
HETATM 8731 C  C16 . 6YQ V  3 .   ? 2.045   15.466  -37.590 1.00 25.89 ? 302 6YQ D C16 1 
HETATM 8732 S  S   . SO4 W  5 .   ? 3.123   13.997  -41.608 1.00 35.38 ? 303 SO4 D S   1 
HETATM 8733 O  O1  . SO4 W  5 .   ? 4.031   15.184  -41.402 1.00 40.33 ? 303 SO4 D O1  1 
HETATM 8734 O  O2  . SO4 W  5 .   ? 2.742   13.903  -43.083 1.00 32.53 ? 303 SO4 D O2  1 
HETATM 8735 O  O3  . SO4 W  5 .   ? 3.787   12.748  -41.079 1.00 28.69 ? 303 SO4 D O3  1 
HETATM 8736 O  O4  . SO4 W  5 .   ? 1.829   14.254  -40.889 1.00 35.91 ? 303 SO4 D O4  1 
HETATM 8737 C  C1  . EDO X  4 .   ? 5.474   9.411   -41.126 1.00 20.35 ? 304 EDO D C1  1 
HETATM 8738 O  O1  . EDO X  4 .   ? 4.283   10.136  -41.348 1.00 19.89 ? 304 EDO D O1  1 
HETATM 8739 C  C2  . EDO X  4 .   ? 6.755   9.646   -41.973 1.00 20.19 ? 304 EDO D C2  1 
HETATM 8740 O  O2  . EDO X  4 .   ? 6.735   10.927  -42.456 1.00 28.63 ? 304 EDO D O2  1 
HETATM 8741 C  C1  . EDO Y  4 .   ? -2.728  -1.424  -21.630 1.00 24.32 ? 305 EDO D C1  1 
HETATM 8742 O  O1  . EDO Y  4 .   ? -1.622  -1.527  -22.509 1.00 22.86 ? 305 EDO D O1  1 
HETATM 8743 C  C2  . EDO Y  4 .   ? -2.105  -1.140  -20.271 1.00 26.96 ? 305 EDO D C2  1 
HETATM 8744 O  O2  . EDO Y  4 .   ? -1.225  -0.016  -20.224 1.00 32.20 ? 305 EDO D O2  1 
HETATM 8745 C  C1  . EDO Z  4 .   ? -5.601  -9.578  -38.441 1.00 34.60 ? 306 EDO D C1  1 
HETATM 8746 O  O1  . EDO Z  4 .   ? -6.503  -9.153  -37.375 1.00 28.99 ? 306 EDO D O1  1 
HETATM 8747 C  C2  . EDO Z  4 .   ? -6.083  -10.612 -39.472 1.00 36.12 ? 306 EDO D C2  1 
HETATM 8748 O  O2  . EDO Z  4 .   ? -5.870  -10.055 -40.807 1.00 32.16 ? 306 EDO D O2  1 
HETATM 8749 O  O   . HOH AA 6 .   ? 4.773   -0.377  -8.446  1.00 27.13 ? 401 HOH A O   1 
HETATM 8750 O  O   . HOH AA 6 .   ? 34.837  -11.110 -3.507  1.00 35.36 ? 402 HOH A O   1 
HETATM 8751 O  O   . HOH AA 6 .   ? 42.866  -9.946  19.152  1.00 34.28 ? 403 HOH A O   1 
HETATM 8752 O  O   . HOH AA 6 .   ? 42.496  -0.212  5.641   1.00 39.10 ? 404 HOH A O   1 
HETATM 8753 O  O   . HOH AA 6 .   ? 18.305  -3.363  -5.924  1.00 30.79 ? 405 HOH A O   1 
HETATM 8754 O  O   . HOH AA 6 .   ? 43.670  -4.175  12.880  1.00 24.96 ? 406 HOH A O   1 
HETATM 8755 O  O   . HOH AA 6 .   ? 10.993  12.504  20.292  1.00 23.82 ? 407 HOH A O   1 
HETATM 8756 O  O   . HOH AA 6 .   ? 26.076  2.696   -2.773  1.00 29.98 ? 408 HOH A O   1 
HETATM 8757 O  O   . HOH AA 6 .   ? 41.534  2.577   19.369  1.00 33.48 ? 409 HOH A O   1 
HETATM 8758 O  O   . HOH AA 6 .   ? 5.987   -3.914  -8.130  1.00 28.64 ? 410 HOH A O   1 
HETATM 8759 O  O   . HOH AA 6 .   ? 9.907   -14.671 1.706   1.00 28.65 ? 411 HOH A O   1 
HETATM 8760 O  O   . HOH AA 6 .   ? 11.209  3.480   19.192  1.00 24.76 ? 412 HOH A O   1 
HETATM 8761 O  O   . HOH AA 6 .   ? 41.595  6.172   5.498   1.00 26.47 ? 413 HOH A O   1 
HETATM 8762 O  O   . HOH AA 6 .   ? 14.416  -9.827  26.055  1.00 14.86 ? 414 HOH A O   1 
HETATM 8763 O  O   . HOH AA 6 .   ? 7.749   -8.156  11.769  1.00 21.72 ? 415 HOH A O   1 
HETATM 8764 O  O   . HOH AA 6 .   ? 27.752  -21.786 1.666   1.00 35.25 ? 416 HOH A O   1 
HETATM 8765 O  O   . HOH AA 6 .   ? 17.816  3.246   12.689  1.00 9.60  ? 417 HOH A O   1 
HETATM 8766 O  O   . HOH AA 6 .   ? 32.671  6.596   12.979  1.00 30.79 ? 418 HOH A O   1 
HETATM 8767 O  O   . HOH AA 6 .   ? 37.246  7.375   29.881  1.00 27.60 ? 419 HOH A O   1 
HETATM 8768 O  O   . HOH AA 6 .   ? 5.884   -3.415  20.895  1.00 27.09 ? 420 HOH A O   1 
HETATM 8769 O  O   . HOH AA 6 .   ? 12.728  -12.336 16.496  1.00 19.41 ? 421 HOH A O   1 
HETATM 8770 O  O   . HOH AA 6 .   ? 27.885  3.945   33.646  1.00 26.24 ? 422 HOH A O   1 
HETATM 8771 O  O   . HOH AA 6 .   ? 27.719  -20.940 24.558  1.00 26.97 ? 423 HOH A O   1 
HETATM 8772 O  O   . HOH AA 6 .   ? 9.208   11.523  0.905   1.00 12.82 ? 424 HOH A O   1 
HETATM 8773 O  O   . HOH AA 6 .   ? 18.712  10.513  34.717  1.00 28.34 ? 425 HOH A O   1 
HETATM 8774 O  O   . HOH AA 6 .   ? 11.736  10.071  22.998  1.00 33.44 ? 426 HOH A O   1 
HETATM 8775 O  O   . HOH AA 6 .   ? 41.113  -10.316 9.796   1.00 17.27 ? 427 HOH A O   1 
HETATM 8776 O  O   . HOH AA 6 .   ? 39.560  -12.567 19.892  1.00 22.65 ? 428 HOH A O   1 
HETATM 8777 O  O   . HOH AA 6 .   ? 23.833  8.434   11.862  1.00 21.80 ? 429 HOH A O   1 
HETATM 8778 O  O   . HOH AA 6 .   ? 20.612  -18.817 28.883  1.00 33.26 ? 430 HOH A O   1 
HETATM 8779 O  O   . HOH AA 6 .   ? 37.114  15.779  4.101   1.00 33.13 ? 431 HOH A O   1 
HETATM 8780 O  O   . HOH AA 6 .   ? 34.809  0.443   -9.178  1.00 26.56 ? 432 HOH A O   1 
HETATM 8781 O  O   . HOH AA 6 .   ? 10.960  -4.770  -5.071  1.00 32.21 ? 433 HOH A O   1 
HETATM 8782 O  O   . HOH AA 6 .   ? 39.353  -3.691  -7.448  1.00 33.62 ? 434 HOH A O   1 
HETATM 8783 O  O   . HOH AA 6 .   ? 5.173   1.475   -10.539 1.00 39.95 ? 435 HOH A O   1 
HETATM 8784 O  O   . HOH AA 6 .   ? 33.426  15.472  6.926   1.00 45.14 ? 436 HOH A O   1 
HETATM 8785 O  O   . HOH AA 6 .   ? 29.388  -16.758 14.907  1.00 27.00 ? 437 HOH A O   1 
HETATM 8786 O  O   . HOH AA 6 .   ? 18.719  20.519  8.318   1.00 27.53 ? 438 HOH A O   1 
HETATM 8787 O  O   . HOH AA 6 .   ? 32.812  6.739   15.804  1.00 38.54 ? 439 HOH A O   1 
HETATM 8788 O  O   . HOH AA 6 .   ? 32.198  -17.003 10.309  1.00 27.36 ? 440 HOH A O   1 
HETATM 8789 O  O   . HOH AA 6 .   ? 10.542  6.282   15.378  1.00 12.11 ? 441 HOH A O   1 
HETATM 8790 O  O   . HOH AA 6 .   ? 28.507  -4.213  2.455   1.00 10.78 ? 442 HOH A O   1 
HETATM 8791 O  O   . HOH AA 6 .   ? 19.571  -0.490  26.597  1.00 14.95 ? 443 HOH A O   1 
HETATM 8792 O  O   . HOH AA 6 .   ? 19.375  9.837   32.130  1.00 20.40 ? 444 HOH A O   1 
HETATM 8793 O  O   . HOH AA 6 .   ? 13.767  16.425  11.738  1.00 16.64 ? 445 HOH A O   1 
HETATM 8794 O  O   . HOH AA 6 .   ? 12.626  14.545  2.141   1.00 13.58 ? 446 HOH A O   1 
HETATM 8795 O  O   . HOH AA 6 .   ? 38.462  4.237   11.129  1.00 20.05 ? 447 HOH A O   1 
HETATM 8796 O  O   . HOH AA 6 .   ? 5.034   -9.237  25.671  1.00 27.40 ? 448 HOH A O   1 
HETATM 8797 O  O   . HOH AA 6 .   ? 17.290  0.434   28.450  1.00 17.18 ? 449 HOH A O   1 
HETATM 8798 O  O   . HOH AA 6 .   ? 34.201  1.219   -6.113  1.00 27.56 ? 450 HOH A O   1 
HETATM 8799 O  O   . HOH AA 6 .   ? 41.965  2.390   0.966   1.00 14.70 ? 451 HOH A O   1 
HETATM 8800 O  O   . HOH AA 6 .   ? 47.149  -3.540  10.316  1.00 30.26 ? 452 HOH A O   1 
HETATM 8801 O  O   . HOH AA 6 .   ? 24.916  14.076  33.281  1.00 36.79 ? 453 HOH A O   1 
HETATM 8802 O  O   . HOH AA 6 .   ? 10.437  -3.449  2.666   1.00 13.30 ? 454 HOH A O   1 
HETATM 8803 O  O   . HOH AA 6 .   ? 10.318  4.755   8.739   1.00 10.26 ? 455 HOH A O   1 
HETATM 8804 O  O   . HOH AA 6 .   ? 19.432  14.103  4.966   1.00 12.86 ? 456 HOH A O   1 
HETATM 8805 O  O   . HOH AA 6 .   ? 13.335  14.114  14.032  1.00 23.69 ? 457 HOH A O   1 
HETATM 8806 O  O   . HOH AA 6 .   ? 41.977  2.362   29.282  1.00 27.33 ? 458 HOH A O   1 
HETATM 8807 O  O   . HOH AA 6 .   ? 31.535  5.644   32.554  1.00 25.51 ? 459 HOH A O   1 
HETATM 8808 O  O   . HOH AA 6 .   ? 15.215  -6.754  21.149  1.00 10.98 ? 460 HOH A O   1 
HETATM 8809 O  O   . HOH AA 6 .   ? 39.272  -15.746 16.955  1.00 28.29 ? 461 HOH A O   1 
HETATM 8810 O  O   . HOH AA 6 .   ? 18.052  -15.087 6.232   1.00 17.66 ? 462 HOH A O   1 
HETATM 8811 O  O   . HOH AA 6 .   ? 24.411  -11.625 30.256  1.00 25.20 ? 463 HOH A O   1 
HETATM 8812 O  O   . HOH AA 6 .   ? 32.951  5.071   20.218  1.00 23.18 ? 464 HOH A O   1 
HETATM 8813 O  O   . HOH AA 6 .   ? 33.713  -13.366 26.694  1.00 28.32 ? 465 HOH A O   1 
HETATM 8814 O  O   . HOH AA 6 .   ? 5.581   -12.024 13.285  1.00 16.78 ? 466 HOH A O   1 
HETATM 8815 O  O   . HOH AA 6 .   ? 34.590  3.524   31.485  1.00 30.48 ? 467 HOH A O   1 
HETATM 8816 O  O   . HOH AA 6 .   ? 23.873  -15.899 29.694  1.00 24.49 ? 468 HOH A O   1 
HETATM 8817 O  O   . HOH AA 6 .   ? 45.157  -4.412  7.660   1.00 26.61 ? 469 HOH A O   1 
HETATM 8818 O  O   . HOH AA 6 .   ? 36.167  -6.905  26.425  1.00 21.97 ? 470 HOH A O   1 
HETATM 8819 O  O   . HOH AA 6 .   ? 19.923  14.102  28.277  1.00 25.44 ? 471 HOH A O   1 
HETATM 8820 O  O   . HOH AA 6 .   ? 22.350  7.115   -4.324  1.00 28.77 ? 472 HOH A O   1 
HETATM 8821 O  O   . HOH AA 6 .   ? 25.938  12.453  5.628   1.00 22.22 ? 473 HOH A O   1 
HETATM 8822 O  O   . HOH AA 6 .   ? 15.888  -11.857 27.086  1.00 19.01 ? 474 HOH A O   1 
HETATM 8823 O  O   . HOH AA 6 .   ? 12.434  -2.630  10.992  1.00 9.07  ? 475 HOH A O   1 
HETATM 8824 O  O   . HOH AA 6 .   ? 38.862  -5.759  -3.101  1.00 24.82 ? 476 HOH A O   1 
HETATM 8825 O  O   . HOH AA 6 .   ? 33.108  -14.744 3.485   1.00 19.91 ? 477 HOH A O   1 
HETATM 8826 O  O   . HOH AA 6 .   ? 35.662  14.656  8.589   1.00 42.36 ? 478 HOH A O   1 
HETATM 8827 O  O   . HOH AA 6 .   ? 38.110  -7.503  24.536  1.00 23.95 ? 479 HOH A O   1 
HETATM 8828 O  O   . HOH AA 6 .   ? 11.305  5.227   2.117   1.00 11.62 ? 480 HOH A O   1 
HETATM 8829 O  O   . HOH AA 6 .   ? 35.056  -0.689  30.597  1.00 28.57 ? 481 HOH A O   1 
HETATM 8830 O  O   . HOH AA 6 .   ? 13.860  1.574   -0.327  1.00 18.12 ? 482 HOH A O   1 
HETATM 8831 O  O   . HOH AA 6 .   ? 26.476  5.385   -3.849  1.00 26.67 ? 483 HOH A O   1 
HETATM 8832 O  O   . HOH AA 6 .   ? 19.488  -18.331 26.326  1.00 23.02 ? 484 HOH A O   1 
HETATM 8833 O  O   . HOH AA 6 .   ? 32.096  -16.862 20.717  1.00 33.01 ? 485 HOH A O   1 
HETATM 8834 O  O   . HOH AA 6 .   ? 23.075  -12.291 9.751   1.00 10.94 ? 486 HOH A O   1 
HETATM 8835 O  O   . HOH AA 6 .   ? 9.461   -4.963  16.680  1.00 32.53 ? 487 HOH A O   1 
HETATM 8836 O  O   . HOH AA 6 .   ? 16.803  -13.617 30.766  1.00 21.29 ? 488 HOH A O   1 
HETATM 8837 O  O   . HOH AA 6 .   ? 11.005  -5.214  0.611   1.00 21.79 ? 489 HOH A O   1 
HETATM 8838 O  O   . HOH AA 6 .   ? 8.676   2.920   7.321   1.00 8.09  ? 490 HOH A O   1 
HETATM 8839 O  O   . HOH AA 6 .   ? 25.983  11.202  31.016  1.00 23.42 ? 491 HOH A O   1 
HETATM 8840 O  O   . HOH AA 6 .   ? 40.015  -12.059 11.726  1.00 20.13 ? 492 HOH A O   1 
HETATM 8841 O  O   . HOH AA 6 .   ? 21.442  -11.741 -10.929 1.00 36.69 ? 493 HOH A O   1 
HETATM 8842 O  O   . HOH AA 6 .   ? 6.480   15.791  15.564  1.00 35.14 ? 494 HOH A O   1 
HETATM 8843 O  O   . HOH AA 6 .   ? 31.422  -13.154 2.346   1.00 21.25 ? 495 HOH A O   1 
HETATM 8844 O  O   . HOH AA 6 .   ? 28.569  2.282   -1.454  1.00 20.01 ? 496 HOH A O   1 
HETATM 8845 O  O   . HOH AA 6 .   ? 23.903  12.187  0.194   1.00 27.85 ? 497 HOH A O   1 
HETATM 8846 O  O   . HOH AA 6 .   ? 18.924  11.788  -0.924  1.00 17.53 ? 498 HOH A O   1 
HETATM 8847 O  O   . HOH AA 6 .   ? 20.088  -19.825 8.809   1.00 29.36 ? 499 HOH A O   1 
HETATM 8848 O  O   . HOH AA 6 .   ? 8.823   -6.390  7.508   1.00 19.20 ? 500 HOH A O   1 
HETATM 8849 O  O   . HOH AA 6 .   ? 12.037  -10.432 27.329  1.00 16.56 ? 501 HOH A O   1 
HETATM 8850 O  O   . HOH AA 6 .   ? 31.961  -12.158 30.046  1.00 40.67 ? 502 HOH A O   1 
HETATM 8851 O  O   . HOH AA 6 .   ? 16.598  -18.483 12.434  1.00 40.76 ? 503 HOH A O   1 
HETATM 8852 O  O   . HOH AA 6 .   ? 27.802  -4.779  31.209  1.00 26.23 ? 504 HOH A O   1 
HETATM 8853 O  O   . HOH AA 6 .   ? 42.420  5.593   -4.955  1.00 24.21 ? 505 HOH A O   1 
HETATM 8854 O  O   . HOH AA 6 .   ? 6.493   0.422   -13.741 1.00 39.57 ? 506 HOH A O   1 
HETATM 8855 O  O   . HOH AA 6 .   ? 20.668  -9.806  31.864  1.00 19.29 ? 507 HOH A O   1 
HETATM 8856 O  O   . HOH AA 6 .   ? 29.905  -15.635 -1.741  1.00 20.17 ? 508 HOH A O   1 
HETATM 8857 O  O   . HOH AA 6 .   ? 36.837  -4.399  -0.894  1.00 16.15 ? 509 HOH A O   1 
HETATM 8858 O  O   . HOH AA 6 .   ? 11.058  11.141  8.034   1.00 9.91  ? 510 HOH A O   1 
HETATM 8859 O  O   . HOH AA 6 .   ? 20.694  17.710  7.495   1.00 32.19 ? 511 HOH A O   1 
HETATM 8860 O  O   . HOH AA 6 .   ? 12.144  5.241   28.880  1.00 37.27 ? 512 HOH A O   1 
HETATM 8861 O  O   . HOH AA 6 .   ? 6.094   11.714  7.891   1.00 10.57 ? 513 HOH A O   1 
HETATM 8862 O  O   . HOH AA 6 .   ? 31.205  -20.929 8.457   1.00 27.17 ? 514 HOH A O   1 
HETATM 8863 O  O   . HOH AA 6 .   ? 17.071  0.652   -0.548  1.00 17.84 ? 515 HOH A O   1 
HETATM 8864 O  O   . HOH AA 6 .   ? 13.009  5.751   24.598  1.00 28.16 ? 516 HOH A O   1 
HETATM 8865 O  O   . HOH AA 6 .   ? 7.395   4.996   11.164  1.00 9.55  ? 517 HOH A O   1 
HETATM 8866 O  O   . HOH AA 6 .   ? 17.614  9.511   -0.005  1.00 11.78 ? 518 HOH A O   1 
HETATM 8867 O  O   . HOH AA 6 .   ? 15.106  -15.919 15.146  1.00 20.32 ? 519 HOH A O   1 
HETATM 8868 O  O   . HOH AA 6 .   ? 29.134  -14.909 16.983  1.00 18.44 ? 520 HOH A O   1 
HETATM 8869 O  O   . HOH AA 6 .   ? 11.993  7.504   8.633   1.00 8.92  ? 521 HOH A O   1 
HETATM 8870 O  O   . HOH AA 6 .   ? 7.531   -6.766  2.382   1.00 22.33 ? 522 HOH A O   1 
HETATM 8871 O  O   . HOH AA 6 .   ? 25.749  -18.495 12.634  1.00 22.46 ? 523 HOH A O   1 
HETATM 8872 O  O   . HOH AA 6 .   ? 13.932  1.786   -2.960  1.00 22.56 ? 524 HOH A O   1 
HETATM 8873 O  O   . HOH AA 6 .   ? 18.459  -15.708 34.035  1.00 22.53 ? 525 HOH A O   1 
HETATM 8874 O  O   . HOH AA 6 .   ? 11.902  -15.354 8.510   1.00 21.89 ? 526 HOH A O   1 
HETATM 8875 O  O   . HOH AA 6 .   ? 18.362  12.455  20.753  1.00 31.29 ? 527 HOH A O   1 
HETATM 8876 O  O   . HOH AA 6 .   ? 39.729  -1.752  29.167  1.00 40.53 ? 528 HOH A O   1 
HETATM 8877 O  O   . HOH AA 6 .   ? 13.677  -12.469 20.831  1.00 18.76 ? 529 HOH A O   1 
HETATM 8878 O  O   . HOH AA 6 .   ? 30.229  14.719  4.135   1.00 32.21 ? 530 HOH A O   1 
HETATM 8879 O  O   . HOH AA 6 .   ? 27.369  -5.525  -5.260  1.00 20.52 ? 531 HOH A O   1 
HETATM 8880 O  O   . HOH AA 6 .   ? 9.568   -2.516  10.364  1.00 20.31 ? 532 HOH A O   1 
HETATM 8881 O  O   . HOH AA 6 .   ? 15.485  -15.748 2.439   1.00 30.36 ? 533 HOH A O   1 
HETATM 8882 O  O   . HOH AA 6 .   ? 7.477   -2.097  -0.897  1.00 23.31 ? 534 HOH A O   1 
HETATM 8883 O  O   . HOH AA 6 .   ? 37.289  10.351  24.096  1.00 34.47 ? 535 HOH A O   1 
HETATM 8884 O  O   . HOH AA 6 .   ? 20.728  -2.704  -5.313  1.00 22.68 ? 536 HOH A O   1 
HETATM 8885 O  O   . HOH AA 6 .   ? 8.893   3.826   2.709   1.00 12.60 ? 537 HOH A O   1 
HETATM 8886 O  O   . HOH AA 6 .   ? 36.863  5.213   14.248  1.00 30.66 ? 538 HOH A O   1 
HETATM 8887 O  O   . HOH AA 6 .   ? 20.322  15.552  1.697   1.00 31.61 ? 539 HOH A O   1 
HETATM 8888 O  O   . HOH AA 6 .   ? 20.769  4.099   16.445  1.00 19.53 ? 540 HOH A O   1 
HETATM 8889 O  O   . HOH AA 6 .   ? 11.226  9.675   -2.037  1.00 20.30 ? 541 HOH A O   1 
HETATM 8890 O  O   . HOH AA 6 .   ? 15.238  -14.339 19.250  1.00 17.23 ? 542 HOH A O   1 
HETATM 8891 O  O   . HOH AA 6 .   ? 37.941  10.593  -4.843  1.00 32.30 ? 543 HOH A O   1 
HETATM 8892 O  O   . HOH AA 6 .   ? 32.385  7.598   30.852  1.00 21.31 ? 544 HOH A O   1 
HETATM 8893 O  O   . HOH AA 6 .   ? 26.191  -18.394 20.653  1.00 20.29 ? 545 HOH A O   1 
HETATM 8894 O  O   . HOH AA 6 .   ? 38.190  -13.276 5.844   1.00 28.43 ? 546 HOH A O   1 
HETATM 8895 O  O   . HOH AA 6 .   ? 14.060  -16.026 26.843  1.00 34.19 ? 547 HOH A O   1 
HETATM 8896 O  O   . HOH AA 6 .   ? 8.190   -10.543 26.357  1.00 25.67 ? 548 HOH A O   1 
HETATM 8897 O  O   . HOH AA 6 .   ? 11.469  1.517   -4.182  1.00 36.84 ? 549 HOH A O   1 
HETATM 8898 O  O   . HOH AA 6 .   ? 11.497  8.016   1.664   1.00 12.40 ? 550 HOH A O   1 
HETATM 8899 O  O   . HOH AA 6 .   ? 15.798  4.637   21.682  1.00 17.51 ? 551 HOH A O   1 
HETATM 8900 O  O   . HOH AA 6 .   ? 23.300  3.224   -2.231  1.00 14.71 ? 552 HOH A O   1 
HETATM 8901 O  O   . HOH AA 6 .   ? 44.152  -9.780  8.138   1.00 26.84 ? 553 HOH A O   1 
HETATM 8902 O  O   . HOH AA 6 .   ? 43.550  -9.384  11.435  1.00 21.97 ? 554 HOH A O   1 
HETATM 8903 O  O   . HOH AA 6 .   ? 27.674  14.936  -2.345  1.00 36.33 ? 555 HOH A O   1 
HETATM 8904 O  O   . HOH AA 6 .   ? 11.509  2.360   -6.656  1.00 34.23 ? 556 HOH A O   1 
HETATM 8905 O  O   . HOH AA 6 .   ? 9.718   17.159  14.744  1.00 31.43 ? 557 HOH A O   1 
HETATM 8906 O  O   . HOH AA 6 .   ? 10.168  -4.059  19.343  1.00 21.98 ? 558 HOH A O   1 
HETATM 8907 O  O   . HOH AA 6 .   ? 16.688  10.826  -3.291  1.00 20.12 ? 559 HOH A O   1 
HETATM 8908 O  O   . HOH AA 6 .   ? 10.091  3.257   22.302  1.00 26.76 ? 560 HOH A O   1 
HETATM 8909 O  O   . HOH AA 6 .   ? 6.648   -9.940  4.452   1.00 28.81 ? 561 HOH A O   1 
HETATM 8910 O  O   . HOH AA 6 .   ? 24.482  -21.609 18.601  1.00 39.81 ? 562 HOH A O   1 
HETATM 8911 O  O   . HOH AA 6 .   ? 14.688  7.154   21.056  1.00 25.00 ? 563 HOH A O   1 
HETATM 8912 O  O   . HOH AA 6 .   ? 24.027  -20.927 26.726  1.00 28.52 ? 564 HOH A O   1 
HETATM 8913 O  O   . HOH AA 6 .   ? 8.446   -0.124  24.350  1.00 27.64 ? 565 HOH A O   1 
HETATM 8914 O  O   . HOH AA 6 .   ? 25.678  -15.927 6.631   1.00 11.96 ? 566 HOH A O   1 
HETATM 8915 O  O   . HOH AA 6 .   ? 26.099  -17.853 17.411  1.00 18.44 ? 567 HOH A O   1 
HETATM 8916 O  O   . HOH AA 6 .   ? 9.529   -5.327  -1.367  1.00 28.14 ? 568 HOH A O   1 
HETATM 8917 O  O   . HOH AA 6 .   ? 7.738   -1.753  15.325  1.00 30.85 ? 569 HOH A O   1 
HETATM 8918 O  O   . HOH AA 6 .   ? 13.961  4.415   -4.067  1.00 22.41 ? 570 HOH A O   1 
HETATM 8919 O  O   . HOH AA 6 .   ? 17.974  10.031  21.812  1.00 28.82 ? 571 HOH A O   1 
HETATM 8920 O  O   . HOH AA 6 .   ? 15.123  -17.273 19.595  1.00 28.19 ? 572 HOH A O   1 
HETATM 8921 O  O   . HOH AA 6 .   ? 31.389  -18.905 4.250   1.00 24.02 ? 573 HOH A O   1 
HETATM 8922 O  O   . HOH AA 6 .   ? 27.390  -15.991 -5.585  1.00 25.09 ? 574 HOH A O   1 
HETATM 8923 O  O   . HOH AA 6 .   ? 23.690  -21.713 -3.251  1.00 35.70 ? 575 HOH A O   1 
HETATM 8924 O  O   . HOH AA 6 .   ? 7.723   9.250   14.178  1.00 17.66 ? 576 HOH A O   1 
HETATM 8925 O  O   . HOH AA 6 .   ? 17.186  -3.771  -8.604  1.00 33.41 ? 577 HOH A O   1 
HETATM 8926 O  O   . HOH AA 6 .   ? 20.152  12.096  37.829  1.00 29.10 ? 578 HOH A O   1 
HETATM 8927 O  O   . HOH AA 6 .   ? 23.288  11.817  13.614  1.00 40.91 ? 579 HOH A O   1 
HETATM 8928 O  O   . HOH AA 6 .   ? 17.615  8.026   19.776  1.00 26.49 ? 580 HOH A O   1 
HETATM 8929 O  O   . HOH AA 6 .   ? 39.159  3.934   19.548  1.00 24.66 ? 581 HOH A O   1 
HETATM 8930 O  O   . HOH AA 6 .   ? 33.232  17.061  1.534   1.00 39.64 ? 582 HOH A O   1 
HETATM 8931 O  O   . HOH AA 6 .   ? 17.607  -16.755 -8.221  1.00 28.50 ? 583 HOH A O   1 
HETATM 8932 O  O   . HOH AA 6 .   ? 36.435  7.683   9.788   1.00 31.34 ? 584 HOH A O   1 
HETATM 8933 O  O   . HOH AA 6 .   ? 13.198  5.062   -0.429  1.00 19.99 ? 585 HOH A O   1 
HETATM 8934 O  O   . HOH AA 6 .   ? 7.380   -0.807  8.201   1.00 29.14 ? 586 HOH A O   1 
HETATM 8935 O  O   . HOH AA 6 .   ? 9.245   -11.149 14.174  1.00 29.76 ? 587 HOH A O   1 
HETATM 8936 O  O   . HOH AA 6 .   ? 23.710  14.869  4.209   1.00 25.66 ? 588 HOH A O   1 
HETATM 8937 O  O   . HOH AA 6 .   ? 18.145  5.625   20.611  1.00 15.78 ? 589 HOH A O   1 
HETATM 8938 O  O   . HOH AA 6 .   ? 29.561  11.877  -5.054  1.00 23.60 ? 590 HOH A O   1 
HETATM 8939 O  O   . HOH AA 6 .   ? 9.087   2.176   -8.081  1.00 36.63 ? 591 HOH A O   1 
HETATM 8940 O  O   . HOH AA 6 .   ? 12.523  4.672   22.138  1.00 25.20 ? 592 HOH A O   1 
HETATM 8941 O  O   . HOH AA 6 .   ? 24.436  9.292   14.461  1.00 37.80 ? 593 HOH A O   1 
HETATM 8942 O  O   . HOH AA 6 .   ? 38.645  -15.364 12.238  1.00 28.58 ? 594 HOH A O   1 
HETATM 8943 O  O   . HOH AA 6 .   ? 29.837  10.170  33.794  1.00 27.77 ? 595 HOH A O   1 
HETATM 8944 O  O   . HOH AA 6 .   ? 36.567  1.398   30.444  1.00 30.40 ? 596 HOH A O   1 
HETATM 8945 O  O   . HOH AA 6 .   ? 7.946   -7.016  16.813  1.00 26.35 ? 597 HOH A O   1 
HETATM 8946 O  O   . HOH AA 6 .   ? 32.333  -18.112 7.127   1.00 29.37 ? 598 HOH A O   1 
HETATM 8947 O  O   . HOH AA 6 .   ? 27.284  5.774   35.417  1.00 21.73 ? 599 HOH A O   1 
HETATM 8948 O  O   . HOH AA 6 .   ? 39.798  -11.954 23.142  1.00 30.85 ? 600 HOH A O   1 
HETATM 8949 O  O   . HOH AA 6 .   ? 24.747  16.247  2.063   1.00 28.68 ? 601 HOH A O   1 
HETATM 8950 O  O   . HOH AA 6 .   ? 14.255  -1.958  28.944  1.00 23.26 ? 602 HOH A O   1 
HETATM 8951 O  O   . HOH AA 6 .   ? 22.229  -19.092 15.100  1.00 26.53 ? 603 HOH A O   1 
HETATM 8952 O  O   . HOH AA 6 .   ? 16.057  -0.301  31.023  1.00 34.72 ? 604 HOH A O   1 
HETATM 8953 O  O   . HOH AA 6 .   ? 28.140  -23.977 8.511   1.00 37.08 ? 605 HOH A O   1 
HETATM 8954 O  O   . HOH AA 6 .   ? 15.095  -13.608 16.668  1.00 15.93 ? 606 HOH A O   1 
HETATM 8955 O  O   . HOH AA 6 .   ? 24.722  -28.518 -1.058  1.00 26.49 ? 607 HOH A O   1 
HETATM 8956 O  O   . HOH AA 6 .   ? 25.267  11.029  -2.994  1.00 35.97 ? 608 HOH A O   1 
HETATM 8957 O  O   . HOH AA 6 .   ? 6.203   -2.982  13.298  1.00 20.72 ? 609 HOH A O   1 
HETATM 8958 O  O   . HOH AA 6 .   ? 29.273  -6.206  33.430  1.00 36.39 ? 610 HOH A O   1 
HETATM 8959 O  O   . HOH AA 6 .   ? 20.037  -7.216  32.300  1.00 22.28 ? 611 HOH A O   1 
HETATM 8960 O  O   . HOH AA 6 .   ? 34.911  10.224  10.189  1.00 33.69 ? 612 HOH A O   1 
HETATM 8961 O  O   . HOH AA 6 .   ? 17.671  -6.250  33.673  1.00 32.05 ? 613 HOH A O   1 
HETATM 8962 O  O   . HOH AA 6 .   ? 8.726   3.963   19.870  1.00 38.99 ? 614 HOH A O   1 
HETATM 8963 O  O   . HOH AA 6 .   ? 23.956  -15.466 -12.019 1.00 36.46 ? 615 HOH A O   1 
HETATM 8964 O  O   . HOH AA 6 .   ? 23.738  -19.330 16.733  1.00 29.04 ? 616 HOH A O   1 
HETATM 8965 O  O   . HOH AA 6 .   ? 18.632  16.541  15.412  1.00 41.59 ? 617 HOH A O   1 
HETATM 8966 O  O   . HOH AA 6 .   ? 33.969  -3.959  32.131  1.00 39.47 ? 618 HOH A O   1 
HETATM 8967 O  O   . HOH AA 6 .   ? 10.137  3.065   -2.595  1.00 31.78 ? 619 HOH A O   1 
HETATM 8968 O  O   . HOH AA 6 .   ? 34.202  -10.307 28.354  1.00 38.24 ? 620 HOH A O   1 
HETATM 8969 O  O   . HOH AA 6 .   ? 15.949  13.937  -0.721  1.00 35.08 ? 621 HOH A O   1 
HETATM 8970 O  O   . HOH AA 6 .   ? 26.472  -19.691 -1.167  1.00 34.47 ? 622 HOH A O   1 
HETATM 8971 O  O   . HOH AA 6 .   ? 40.165  -3.626  -2.104  1.00 32.09 ? 623 HOH A O   1 
HETATM 8972 O  O   . HOH AA 6 .   ? 4.419   13.483  19.562  1.00 34.00 ? 624 HOH A O   1 
HETATM 8973 O  O   . HOH AA 6 .   ? 46.032  1.347   25.582  1.00 34.68 ? 625 HOH A O   1 
HETATM 8974 O  O   . HOH AA 6 .   ? 28.846  -18.524 20.607  1.00 21.03 ? 626 HOH A O   1 
HETATM 8975 O  O   . HOH AA 6 .   ? 30.432  -17.414 18.746  1.00 30.91 ? 627 HOH A O   1 
HETATM 8976 O  O   . HOH AA 6 .   ? 17.378  -16.882 -3.001  1.00 35.42 ? 628 HOH A O   1 
HETATM 8977 O  O   . HOH AA 6 .   ? 5.040   -3.341  17.472  1.00 27.81 ? 629 HOH A O   1 
HETATM 8978 O  O   . HOH AA 6 .   ? 13.107  -14.524 12.760  1.00 27.09 ? 630 HOH A O   1 
HETATM 8979 O  O   . HOH AA 6 .   ? 10.866  -14.556 17.152  1.00 32.39 ? 631 HOH A O   1 
HETATM 8980 O  O   . HOH AA 6 .   ? 27.824  -21.285 15.018  1.00 40.64 ? 632 HOH A O   1 
HETATM 8981 O  O   . HOH AA 6 .   ? 8.050   2.074   -3.529  1.00 34.25 ? 633 HOH A O   1 
HETATM 8982 O  O   . HOH AA 6 .   ? 42.331  -13.736 12.102  1.00 34.58 ? 634 HOH A O   1 
HETATM 8983 O  O   . HOH AA 6 .   ? 19.090  -20.041 11.995  1.00 34.52 ? 635 HOH A O   1 
HETATM 8984 O  O   . HOH AA 6 .   ? 27.517  11.417  22.561  1.00 40.90 ? 636 HOH A O   1 
HETATM 8985 O  O   . HOH AA 6 .   ? 7.098   -5.880  5.153   1.00 28.57 ? 637 HOH A O   1 
HETATM 8986 O  O   . HOH AA 6 .   ? 13.517  25.251  12.998  1.00 24.39 ? 638 HOH A O   1 
HETATM 8987 O  O   . HOH AA 6 .   ? 33.700  -17.450 2.802   1.00 29.32 ? 639 HOH A O   1 
HETATM 8988 O  O   . HOH AA 6 .   ? 13.274  13.588  -2.110  1.00 32.12 ? 640 HOH A O   1 
HETATM 8989 O  O   . HOH AA 6 .   ? 14.641  -12.390 29.515  1.00 18.01 ? 641 HOH A O   1 
HETATM 8990 O  O   . HOH AA 6 .   ? 23.525  -9.949  32.497  1.00 25.60 ? 642 HOH A O   1 
HETATM 8991 O  O   . HOH AA 6 .   ? 39.495  -9.826  24.744  1.00 35.53 ? 643 HOH A O   1 
HETATM 8992 O  O   . HOH AA 6 .   ? 7.883   6.702   15.533  1.00 18.50 ? 644 HOH A O   1 
HETATM 8993 O  O   . HOH AA 6 .   ? 43.338  -4.751  28.803  1.00 33.32 ? 645 HOH A O   1 
HETATM 8994 O  O   . HOH AA 6 .   ? 23.528  -4.262  -5.688  1.00 39.25 ? 646 HOH A O   1 
HETATM 8995 O  O   . HOH AA 6 .   ? 36.266  -2.578  36.717  1.00 23.72 ? 647 HOH A O   1 
HETATM 8996 O  O   . HOH AA 6 .   ? 12.959  18.736  12.988  1.00 33.06 ? 648 HOH A O   1 
HETATM 8997 O  O   . HOH AA 6 .   ? 24.377  -20.945 11.730  1.00 32.85 ? 649 HOH A O   1 
HETATM 8998 O  O   . HOH AA 6 .   ? 50.874  -9.483  27.049  1.00 35.47 ? 650 HOH A O   1 
HETATM 8999 O  O   . HOH AA 6 .   ? 32.529  -14.829 28.268  1.00 32.35 ? 651 HOH A O   1 
HETATM 9000 O  O   . HOH AA 6 .   ? 30.274  -18.115 -2.723  1.00 25.99 ? 652 HOH A O   1 
HETATM 9001 O  O   . HOH AA 6 .   ? 8.075   -4.855  9.486   1.00 31.50 ? 653 HOH A O   1 
HETATM 9002 O  O   . HOH AA 6 .   ? 11.239  5.208   -2.424  1.00 35.77 ? 654 HOH A O   1 
HETATM 9003 O  O   . HOH AA 6 .   ? 16.306  -16.564 7.930   1.00 28.00 ? 655 HOH A O   1 
HETATM 9004 O  O   . HOH AA 6 .   ? 36.458  13.650  -1.000  1.00 33.04 ? 656 HOH A O   1 
HETATM 9005 O  O   . HOH AA 6 .   ? 36.027  -14.515 26.497  1.00 37.56 ? 657 HOH A O   1 
HETATM 9006 O  O   . HOH AA 6 .   ? 14.972  -13.956 25.515  1.00 29.54 ? 658 HOH A O   1 
HETATM 9007 O  O   . HOH AA 6 .   ? 19.615  21.840  10.529  1.00 40.33 ? 659 HOH A O   1 
HETATM 9008 O  O   . HOH AA 6 .   ? 5.790   -17.891 -5.865  1.00 42.20 ? 660 HOH A O   1 
HETATM 9009 O  O   . HOH AA 6 .   ? 21.295  16.085  5.072   1.00 23.18 ? 661 HOH A O   1 
HETATM 9010 O  O   . HOH AA 6 .   ? 39.107  -4.141  30.311  1.00 38.01 ? 662 HOH A O   1 
HETATM 9011 O  O   . HOH AA 6 .   ? 4.604   13.686  22.458  1.00 35.20 ? 663 HOH A O   1 
HETATM 9012 O  O   . HOH AA 6 .   ? 25.786  14.930  6.273   1.00 35.11 ? 664 HOH A O   1 
HETATM 9013 O  O   . HOH AA 6 .   ? 21.020  11.843  -2.783  1.00 31.99 ? 665 HOH A O   1 
HETATM 9014 O  O   . HOH AA 6 .   ? 13.586  16.499  38.925  1.00 31.23 ? 666 HOH A O   1 
HETATM 9015 O  O   . HOH AA 6 .   ? 11.905  5.304   -4.383  1.00 30.68 ? 667 HOH A O   1 
HETATM 9016 O  O   . HOH AA 6 .   ? 25.033  -18.354 30.136  1.00 31.56 ? 668 HOH A O   1 
HETATM 9017 O  O   . HOH AA 6 .   ? 30.740  -21.111 3.136   1.00 32.88 ? 669 HOH A O   1 
HETATM 9018 O  O   . HOH AA 6 .   ? 11.476  -13.017 25.998  1.00 24.56 ? 670 HOH A O   1 
HETATM 9019 O  O   . HOH AA 6 .   ? 14.726  4.462   -6.676  1.00 36.28 ? 671 HOH A O   1 
HETATM 9020 O  O   . HOH AA 6 .   ? 19.041  10.146  -4.594  1.00 26.34 ? 672 HOH A O   1 
HETATM 9021 O  O   . HOH AA 6 .   ? 13.831  -17.114 7.471   1.00 29.82 ? 673 HOH A O   1 
HETATM 9022 O  O   . HOH AA 6 .   ? 22.767  16.308  7.835   1.00 44.81 ? 674 HOH A O   1 
HETATM 9023 O  O   . HOH AA 6 .   ? 21.617  2.405   -7.001  1.00 33.05 ? 675 HOH A O   1 
HETATM 9024 O  O   . HOH AA 6 .   ? 4.820   17.759  19.468  1.00 31.52 ? 676 HOH A O   1 
HETATM 9025 O  O   . HOH AA 6 .   ? 18.558  6.378   -6.973  1.00 32.67 ? 677 HOH A O   1 
HETATM 9026 O  O   . HOH BA 6 .   ? -13.524 -3.442  26.862  1.00 39.65 ? 401 HOH B O   1 
HETATM 9027 O  O   . HOH BA 6 .   ? -17.738 3.071   28.200  1.00 26.04 ? 402 HOH B O   1 
HETATM 9028 O  O   . HOH BA 6 .   ? -29.296 2.551   5.865   1.00 21.47 ? 403 HOH B O   1 
HETATM 9029 O  O   . HOH BA 6 .   ? 3.198   0.984   -12.810 1.00 34.28 ? 404 HOH B O   1 
HETATM 9030 O  O   . HOH BA 6 .   ? -27.548 3.568   -10.158 1.00 30.52 ? 405 HOH B O   1 
HETATM 9031 O  O   . HOH BA 6 .   ? -27.620 -3.998  8.859   1.00 19.09 ? 406 HOH B O   1 
HETATM 9032 O  O   . HOH BA 6 .   ? -1.568  18.002  14.448  1.00 34.88 ? 407 HOH B O   1 
HETATM 9033 O  O   . HOH BA 6 .   ? -13.973 11.119  4.601   1.00 32.02 ? 408 HOH B O   1 
HETATM 9034 O  O   . HOH BA 6 .   ? 3.412   18.231  -15.635 1.00 30.68 ? 409 HOH B O   1 
HETATM 9035 O  O   . HOH BA 6 .   ? -0.098  16.678  -11.150 1.00 18.74 ? 410 HOH B O   1 
HETATM 9036 O  O   . HOH BA 6 .   ? -3.561  19.016  -20.015 1.00 26.19 ? 411 HOH B O   1 
HETATM 9037 O  O   . HOH BA 6 .   ? -3.662  13.881  -7.160  1.00 22.69 ? 412 HOH B O   1 
HETATM 9038 O  O   . HOH BA 6 .   ? -14.987 5.897   26.226  1.00 30.18 ? 413 HOH B O   1 
HETATM 9039 O  O   . HOH BA 6 .   ? -21.454 -9.735  10.002  1.00 32.40 ? 414 HOH B O   1 
HETATM 9040 O  O   . HOH BA 6 .   ? -19.896 -7.781  -11.663 1.00 28.45 ? 415 HOH B O   1 
HETATM 9041 O  O   . HOH BA 6 .   ? -18.777 6.528   23.691  1.00 40.29 ? 416 HOH B O   1 
HETATM 9042 O  O   . HOH BA 6 .   ? -4.138  -17.794 22.535  1.00 21.68 ? 417 HOH B O   1 
HETATM 9043 O  O   . HOH BA 6 .   ? -26.259 9.221   16.580  1.00 38.42 ? 418 HOH B O   1 
HETATM 9044 O  O   . HOH BA 6 .   ? 1.883   17.154  0.116   1.00 30.75 ? 419 HOH B O   1 
HETATM 9045 O  O   . HOH BA 6 .   ? -12.085 -17.629 13.176  1.00 32.59 ? 420 HOH B O   1 
HETATM 9046 O  O   . HOH BA 6 .   ? -15.685 16.137  -8.093  1.00 25.29 ? 421 HOH B O   1 
HETATM 9047 O  O   . HOH BA 6 .   ? 7.214   -11.516 24.131  1.00 27.65 ? 422 HOH B O   1 
HETATM 9048 O  O   . HOH BA 6 .   ? -13.549 7.471   -15.610 1.00 19.91 ? 423 HOH B O   1 
HETATM 9049 O  O   . HOH BA 6 .   ? -27.142 -3.561  -5.803  1.00 26.36 ? 424 HOH B O   1 
HETATM 9050 O  O   . HOH BA 6 .   ? -13.804 -14.956 28.432  1.00 20.29 ? 425 HOH B O   1 
HETATM 9051 O  O   . HOH BA 6 .   ? -5.807  -11.732 -14.830 1.00 24.95 ? 426 HOH B O   1 
HETATM 9052 O  O   . HOH BA 6 .   ? -9.418  -20.104 25.181  1.00 33.97 ? 427 HOH B O   1 
HETATM 9053 O  O   . HOH BA 6 .   ? -25.438 3.284   -11.105 1.00 31.54 ? 428 HOH B O   1 
HETATM 9054 O  O   . HOH BA 6 .   ? -32.905 -1.523  -8.350  1.00 27.04 ? 429 HOH B O   1 
HETATM 9055 O  O   . HOH BA 6 .   ? -7.405  -7.595  28.424  1.00 25.88 ? 430 HOH B O   1 
HETATM 9056 O  O   . HOH BA 6 .   ? -2.584  5.254   4.051   1.00 8.95  ? 431 HOH B O   1 
HETATM 9057 O  O   . HOH BA 6 .   ? -5.837  -12.595 11.875  1.00 16.01 ? 432 HOH B O   1 
HETATM 9058 O  O   . HOH BA 6 .   ? -26.723 -6.984  -1.391  1.00 20.83 ? 433 HOH B O   1 
HETATM 9059 O  O   . HOH BA 6 .   ? -17.571 13.369  -4.423  1.00 29.51 ? 434 HOH B O   1 
HETATM 9060 O  O   . HOH BA 6 .   ? -4.353  -19.295 18.098  1.00 29.92 ? 435 HOH B O   1 
HETATM 9061 O  O   . HOH BA 6 .   ? -13.760 4.544   -18.967 1.00 33.26 ? 436 HOH B O   1 
HETATM 9062 O  O   . HOH BA 6 .   ? -29.060 1.137   17.086  1.00 41.35 ? 437 HOH B O   1 
HETATM 9063 O  O   . HOH BA 6 .   ? -4.401  11.295  -15.003 1.00 13.78 ? 438 HOH B O   1 
HETATM 9064 O  O   . HOH BA 6 .   ? 8.897   16.663  0.828   1.00 18.70 ? 439 HOH B O   1 
HETATM 9065 O  O   . HOH BA 6 .   ? -20.165 -11.801 8.287   1.00 28.40 ? 440 HOH B O   1 
HETATM 9066 O  O   . HOH BA 6 .   ? -20.913 -4.907  22.067  1.00 20.42 ? 441 HOH B O   1 
HETATM 9067 O  O   . HOH BA 6 .   ? -27.206 -9.885  1.860   1.00 23.98 ? 442 HOH B O   1 
HETATM 9068 O  O   . HOH BA 6 .   ? -29.905 -4.401  -0.627  1.00 20.43 ? 443 HOH B O   1 
HETATM 9069 O  O   . HOH BA 6 .   ? -17.735 -10.150 28.577  1.00 21.23 ? 444 HOH B O   1 
HETATM 9070 O  O   . HOH BA 6 .   ? 1.735   6.577   -8.248  1.00 16.85 ? 445 HOH B O   1 
HETATM 9071 O  O   . HOH BA 6 .   ? -20.187 -11.717 0.763   1.00 34.49 ? 446 HOH B O   1 
HETATM 9072 O  O   . HOH BA 6 .   ? -1.669  20.455  8.382   1.00 31.71 ? 447 HOH B O   1 
HETATM 9073 O  O   . HOH BA 6 .   ? 6.959   -11.428 17.366  1.00 22.12 ? 448 HOH B O   1 
HETATM 9074 O  O   . HOH BA 6 .   ? -7.358  11.689  5.184   1.00 22.07 ? 449 HOH B O   1 
HETATM 9075 O  O   . HOH BA 6 .   ? -8.745  16.180  10.586  1.00 36.25 ? 450 HOH B O   1 
HETATM 9076 O  O   . HOH BA 6 .   ? 5.888   -9.395  13.461  1.00 13.88 ? 451 HOH B O   1 
HETATM 9077 O  O   . HOH BA 6 .   ? -7.719  10.911  1.958   1.00 36.18 ? 452 HOH B O   1 
HETATM 9078 O  O   . HOH BA 6 .   ? 1.288   0.470   -16.103 1.00 27.38 ? 453 HOH B O   1 
HETATM 9079 O  O   . HOH BA 6 .   ? -13.879 0.435   15.261  1.00 11.21 ? 454 HOH B O   1 
HETATM 9080 O  O   . HOH BA 6 .   ? 3.272   5.463   16.331  1.00 20.28 ? 455 HOH B O   1 
HETATM 9081 O  O   . HOH BA 6 .   ? 5.228   6.370   0.946   1.00 10.74 ? 456 HOH B O   1 
HETATM 9082 O  O   . HOH BA 6 .   ? 3.784   -2.240  22.757  1.00 23.85 ? 457 HOH B O   1 
HETATM 9083 O  O   . HOH BA 6 .   ? -3.627  -8.558  -9.117  1.00 17.94 ? 458 HOH B O   1 
HETATM 9084 O  O   . HOH BA 6 .   ? -4.152  16.045  -11.257 1.00 12.70 ? 459 HOH B O   1 
HETATM 9085 O  O   . HOH BA 6 .   ? -5.949  -16.463 5.571   1.00 25.22 ? 460 HOH B O   1 
HETATM 9086 O  O   . HOH BA 6 .   ? 3.780   3.528   -2.482  1.00 16.53 ? 461 HOH B O   1 
HETATM 9087 O  O   . HOH BA 6 .   ? -21.861 1.639   18.809  1.00 25.64 ? 462 HOH B O   1 
HETATM 9088 O  O   . HOH BA 6 .   ? 1.070   18.060  -13.880 1.00 24.09 ? 463 HOH B O   1 
HETATM 9089 O  O   . HOH BA 6 .   ? -16.965 11.355  1.909   1.00 23.54 ? 464 HOH B O   1 
HETATM 9090 O  O   . HOH BA 6 .   ? 3.762   -2.095  13.921  1.00 14.87 ? 465 HOH B O   1 
HETATM 9091 O  O   . HOH BA 6 .   ? 5.301   16.151  13.441  1.00 25.71 ? 466 HOH B O   1 
HETATM 9092 O  O   . HOH BA 6 .   ? -6.291  -18.127 -2.180  1.00 27.86 ? 467 HOH B O   1 
HETATM 9093 O  O   . HOH BA 6 .   ? -6.016  11.394  20.719  1.00 33.24 ? 468 HOH B O   1 
HETATM 9094 O  O   . HOH BA 6 .   ? 9.137   7.144   8.388   1.00 12.33 ? 469 HOH B O   1 
HETATM 9095 O  O   . HOH BA 6 .   ? -2.908  -12.701 15.296  1.00 26.47 ? 470 HOH B O   1 
HETATM 9096 O  O   . HOH BA 6 .   ? -20.206 -12.180 -2.143  1.00 26.32 ? 471 HOH B O   1 
HETATM 9097 O  O   . HOH BA 6 .   ? -19.362 -0.639  -16.199 1.00 23.35 ? 472 HOH B O   1 
HETATM 9098 O  O   . HOH BA 6 .   ? 7.991   11.871  14.729  1.00 20.92 ? 473 HOH B O   1 
HETATM 9099 O  O   . HOH BA 6 .   ? -10.305 -8.879  8.299   1.00 8.57  ? 474 HOH B O   1 
HETATM 9100 O  O   . HOH BA 6 .   ? -8.120  -1.482  -16.010 1.00 32.44 ? 475 HOH B O   1 
HETATM 9101 O  O   . HOH BA 6 .   ? -17.675 -16.498 -6.254  1.00 26.40 ? 476 HOH B O   1 
HETATM 9102 O  O   . HOH BA 6 .   ? 4.777   -5.892  8.935   1.00 23.19 ? 477 HOH B O   1 
HETATM 9103 O  O   . HOH BA 6 .   ? -14.586 -13.373 24.002  1.00 27.24 ? 478 HOH B O   1 
HETATM 9104 O  O   . HOH BA 6 .   ? 5.680   12.488  -4.330  1.00 17.23 ? 479 HOH B O   1 
HETATM 9105 O  O   . HOH BA 6 .   ? -8.842  14.714  -2.123  1.00 30.30 ? 480 HOH B O   1 
HETATM 9106 O  O   . HOH BA 6 .   ? -18.365 -7.995  16.185  1.00 15.76 ? 481 HOH B O   1 
HETATM 9107 O  O   . HOH BA 6 .   ? -5.055  18.028  -7.441  1.00 39.04 ? 482 HOH B O   1 
HETATM 9108 O  O   . HOH BA 6 .   ? -17.513 -12.509 3.534   1.00 20.86 ? 483 HOH B O   1 
HETATM 9109 O  O   . HOH BA 6 .   ? -7.840  -15.500 -7.794  1.00 12.24 ? 484 HOH B O   1 
HETATM 9110 O  O   . HOH BA 6 .   ? -16.974 -10.321 20.339  1.00 14.79 ? 485 HOH B O   1 
HETATM 9111 O  O   . HOH BA 6 .   ? -5.207  14.193  -4.423  1.00 28.88 ? 486 HOH B O   1 
HETATM 9112 O  O   . HOH BA 6 .   ? 4.518   6.488   14.190  1.00 12.61 ? 487 HOH B O   1 
HETATM 9113 O  O   . HOH BA 6 .   ? -0.382  4.146   -16.826 1.00 21.52 ? 488 HOH B O   1 
HETATM 9114 O  O   . HOH BA 6 .   ? -22.969 -2.165  -8.639  1.00 13.61 ? 489 HOH B O   1 
HETATM 9115 O  O   . HOH BA 6 .   ? -1.230  14.519  17.023  1.00 21.00 ? 490 HOH B O   1 
HETATM 9116 O  O   . HOH BA 6 .   ? -14.046 -14.679 6.005   1.00 18.06 ? 491 HOH B O   1 
HETATM 9117 O  O   . HOH BA 6 .   ? -10.498 14.290  -13.627 1.00 15.10 ? 492 HOH B O   1 
HETATM 9118 O  O   . HOH BA 6 .   ? 2.741   -13.274 15.840  1.00 17.93 ? 493 HOH B O   1 
HETATM 9119 O  O   . HOH BA 6 .   ? -23.236 -8.825  14.371  1.00 30.49 ? 494 HOH B O   1 
HETATM 9120 O  O   . HOH BA 6 .   ? -24.707 -2.410  -6.371  1.00 14.93 ? 495 HOH B O   1 
HETATM 9121 O  O   . HOH BA 6 .   ? 1.755   -1.526  5.852   1.00 8.01  ? 496 HOH B O   1 
HETATM 9122 O  O   . HOH BA 6 .   ? -17.046 -10.712 1.394   1.00 13.87 ? 497 HOH B O   1 
HETATM 9123 O  O   . HOH BA 6 .   ? -0.219  -13.100 22.562  1.00 31.53 ? 498 HOH B O   1 
HETATM 9124 O  O   . HOH BA 6 .   ? -5.272  15.758  -1.639  1.00 39.48 ? 499 HOH B O   1 
HETATM 9125 O  O   . HOH BA 6 .   ? -26.944 -6.077  6.830   1.00 19.36 ? 500 HOH B O   1 
HETATM 9126 O  O   . HOH BA 6 .   ? 4.026   -2.389  -3.321  1.00 27.66 ? 501 HOH B O   1 
HETATM 9127 O  O   . HOH BA 6 .   ? -12.419 -13.539 -11.227 1.00 16.47 ? 502 HOH B O   1 
HETATM 9128 O  O   . HOH BA 6 .   ? -9.055  -7.848  -14.401 1.00 15.36 ? 503 HOH B O   1 
HETATM 9129 O  O   . HOH BA 6 .   ? -2.876  -5.291  -4.084  1.00 8.56  ? 504 HOH B O   1 
HETATM 9130 O  O   . HOH BA 6 .   ? -16.429 -12.256 25.693  1.00 23.52 ? 505 HOH B O   1 
HETATM 9131 O  O   . HOH BA 6 .   ? 8.115   4.602   5.188   1.00 8.88  ? 506 HOH B O   1 
HETATM 9132 O  O   . HOH BA 6 .   ? -0.893  18.028  0.635   1.00 32.70 ? 507 HOH B O   1 
HETATM 9133 O  O   . HOH BA 6 .   ? -3.826  12.451  -18.251 1.00 17.78 ? 508 HOH B O   1 
HETATM 9134 O  O   . HOH BA 6 .   ? -1.069  5.827   -4.937  1.00 10.87 ? 509 HOH B O   1 
HETATM 9135 O  O   . HOH BA 6 .   ? -1.436  13.989  -4.460  1.00 24.86 ? 510 HOH B O   1 
HETATM 9136 O  O   . HOH BA 6 .   ? -16.801 -16.821 16.855  1.00 36.61 ? 511 HOH B O   1 
HETATM 9137 O  O   . HOH BA 6 .   ? -5.527  1.564   -9.906  1.00 9.18  ? 512 HOH B O   1 
HETATM 9138 O  O   . HOH BA 6 .   ? 4.843   -9.674  -12.128 1.00 24.08 ? 513 HOH B O   1 
HETATM 9139 O  O   . HOH BA 6 .   ? 4.741   16.886  3.135   1.00 25.66 ? 514 HOH B O   1 
HETATM 9140 O  O   . HOH BA 6 .   ? -21.857 -8.620  -8.401  1.00 16.89 ? 515 HOH B O   1 
HETATM 9141 O  O   . HOH BA 6 .   ? -17.645 -3.794  26.816  1.00 26.47 ? 516 HOH B O   1 
HETATM 9142 O  O   . HOH BA 6 .   ? -17.785 9.271   -2.598  1.00 16.10 ? 517 HOH B O   1 
HETATM 9143 O  O   . HOH BA 6 .   ? 5.393   5.547   7.679   1.00 9.96  ? 518 HOH B O   1 
HETATM 9144 O  O   . HOH BA 6 .   ? -23.069 9.681   6.489   1.00 17.28 ? 519 HOH B O   1 
HETATM 9145 O  O   . HOH BA 6 .   ? 4.183   10.085  -6.773  1.00 16.69 ? 520 HOH B O   1 
HETATM 9146 O  O   . HOH BA 6 .   ? -24.074 0.966   21.031  1.00 28.31 ? 521 HOH B O   1 
HETATM 9147 O  O   . HOH BA 6 .   ? -16.883 6.145   -18.112 1.00 36.26 ? 522 HOH B O   1 
HETATM 9148 O  O   . HOH BA 6 .   ? -12.810 -19.316 16.100  1.00 38.72 ? 523 HOH B O   1 
HETATM 9149 O  O   . HOH BA 6 .   ? 5.459   -8.254  -1.285  1.00 23.00 ? 524 HOH B O   1 
HETATM 9150 O  O   . HOH BA 6 .   ? 1.420   14.392  -11.188 1.00 15.53 ? 525 HOH B O   1 
HETATM 9151 O  O   . HOH BA 6 .   ? 5.430   19.900  10.723  1.00 20.25 ? 526 HOH B O   1 
HETATM 9152 O  O   . HOH BA 6 .   ? -6.167  2.305   -16.876 1.00 24.74 ? 527 HOH B O   1 
HETATM 9153 O  O   . HOH BA 6 .   ? 6.648   3.358   9.117   1.00 7.31  ? 528 HOH B O   1 
HETATM 9154 O  O   . HOH BA 6 .   ? -6.472  -11.424 29.248  1.00 29.14 ? 529 HOH B O   1 
HETATM 9155 O  O   . HOH BA 6 .   ? -20.385 -9.387  15.138  1.00 18.52 ? 530 HOH B O   1 
HETATM 9156 O  O   . HOH BA 6 .   ? -26.885 -7.223  10.779  1.00 31.23 ? 531 HOH B O   1 
HETATM 9157 O  O   . HOH BA 6 .   ? -4.780  -12.662 22.159  1.00 33.31 ? 532 HOH B O   1 
HETATM 9158 O  O   . HOH BA 6 .   ? 4.061   -14.874 9.979   1.00 34.41 ? 533 HOH B O   1 
HETATM 9159 O  O   . HOH BA 6 .   ? -27.433 6.918   -11.772 1.00 22.01 ? 534 HOH B O   1 
HETATM 9160 O  O   . HOH BA 6 .   ? -13.603 -6.846  -11.154 1.00 18.19 ? 535 HOH B O   1 
HETATM 9161 O  O   . HOH BA 6 .   ? -11.986 7.540   18.705  1.00 35.05 ? 536 HOH B O   1 
HETATM 9162 O  O   . HOH BA 6 .   ? 6.680   0.593   22.332  1.00 29.54 ? 537 HOH B O   1 
HETATM 9163 O  O   . HOH BA 6 .   ? -14.596 -14.279 19.963  1.00 32.01 ? 538 HOH B O   1 
HETATM 9164 O  O   . HOH BA 6 .   ? -14.550 13.845  -16.090 1.00 26.11 ? 539 HOH B O   1 
HETATM 9165 O  O   . HOH BA 6 .   ? -0.463  12.001  16.200  1.00 14.68 ? 540 HOH B O   1 
HETATM 9166 O  O   . HOH BA 6 .   ? -21.871 -2.248  -12.614 1.00 29.85 ? 541 HOH B O   1 
HETATM 9167 O  O   . HOH BA 6 .   ? 9.288   7.085   -2.297  1.00 28.58 ? 542 HOH B O   1 
HETATM 9168 O  O   . HOH BA 6 .   ? -11.453 -17.391 21.300  1.00 61.42 ? 543 HOH B O   1 
HETATM 9169 O  O   . HOH BA 6 .   ? -5.063  -15.010 -12.646 1.00 36.38 ? 544 HOH B O   1 
HETATM 9170 O  O   . HOH BA 6 .   ? -23.743 -7.596  20.639  1.00 30.85 ? 545 HOH B O   1 
HETATM 9171 O  O   . HOH BA 6 .   ? -31.870 5.446   -7.538  1.00 22.05 ? 546 HOH B O   1 
HETATM 9172 O  O   . HOH BA 6 .   ? -3.491  2.197   -11.922 1.00 11.33 ? 547 HOH B O   1 
HETATM 9173 O  O   . HOH BA 6 .   ? -4.469  0.358   21.894  1.00 19.69 ? 548 HOH B O   1 
HETATM 9174 O  O   . HOH BA 6 .   ? 2.263   5.133   -5.610  1.00 16.58 ? 549 HOH B O   1 
HETATM 9175 O  O   . HOH BA 6 .   ? -1.194  -0.568  -12.667 1.00 16.18 ? 550 HOH B O   1 
HETATM 9176 O  O   . HOH BA 6 .   ? -35.410 7.110   2.903   1.00 26.53 ? 551 HOH B O   1 
HETATM 9177 O  O   . HOH BA 6 .   ? -19.815 -15.825 10.247  1.00 26.81 ? 552 HOH B O   1 
HETATM 9178 O  O   . HOH BA 6 .   ? -19.870 12.872  7.624   1.00 23.93 ? 553 HOH B O   1 
HETATM 9179 O  O   . HOH BA 6 .   ? -14.276 -2.285  -13.679 1.00 23.29 ? 554 HOH B O   1 
HETATM 9180 O  O   . HOH BA 6 .   ? -20.925 -11.166 5.535   1.00 32.66 ? 555 HOH B O   1 
HETATM 9181 O  O   . HOH BA 6 .   ? -28.281 7.592   19.166  1.00 52.66 ? 556 HOH B O   1 
HETATM 9182 O  O   . HOH BA 6 .   ? -1.980  -11.387 -3.043  1.00 14.38 ? 557 HOH B O   1 
HETATM 9183 O  O   . HOH BA 6 .   ? -16.950 9.670   -14.996 1.00 37.20 ? 558 HOH B O   1 
HETATM 9184 O  O   . HOH BA 6 .   ? -5.532  6.586   0.479   1.00 11.82 ? 559 HOH B O   1 
HETATM 9185 O  O   . HOH BA 6 .   ? 6.633   4.809   13.745  1.00 11.40 ? 560 HOH B O   1 
HETATM 9186 O  O   . HOH BA 6 .   ? -29.186 7.372   -1.672  1.00 30.07 ? 561 HOH B O   1 
HETATM 9187 O  O   . HOH BA 6 .   ? -25.379 -7.140  13.211  1.00 26.23 ? 562 HOH B O   1 
HETATM 9188 O  O   . HOH BA 6 .   ? 1.654   8.948   -6.883  1.00 13.62 ? 563 HOH B O   1 
HETATM 9189 O  O   . HOH BA 6 .   ? -1.507  16.655  11.066  1.00 12.42 ? 564 HOH B O   1 
HETATM 9190 O  O   . HOH BA 6 .   ? -1.505  -9.726  -10.122 1.00 19.28 ? 565 HOH B O   1 
HETATM 9191 O  O   . HOH BA 6 .   ? -3.087  7.239   -3.795  1.00 11.82 ? 566 HOH B O   1 
HETATM 9192 O  O   . HOH BA 6 .   ? 0.600   8.133   -4.489  1.00 18.02 ? 567 HOH B O   1 
HETATM 9193 O  O   . HOH BA 6 .   ? -15.992 -0.339  -14.921 1.00 19.84 ? 568 HOH B O   1 
HETATM 9194 O  O   . HOH BA 6 .   ? -17.601 12.681  -12.592 1.00 24.31 ? 569 HOH B O   1 
HETATM 9195 O  O   . HOH BA 6 .   ? -8.246  -18.969 3.112   1.00 31.65 ? 570 HOH B O   1 
HETATM 9196 O  O   . HOH BA 6 .   ? -26.597 10.499  5.138   1.00 25.29 ? 571 HOH B O   1 
HETATM 9197 O  O   . HOH BA 6 .   ? 4.073   -9.229  3.147   1.00 19.26 ? 572 HOH B O   1 
HETATM 9198 O  O   . HOH BA 6 .   ? 4.045   11.206  -13.425 1.00 29.56 ? 573 HOH B O   1 
HETATM 9199 O  O   . HOH BA 6 .   ? -1.850  9.582   -3.242  1.00 14.22 ? 574 HOH B O   1 
HETATM 9200 O  O   . HOH BA 6 .   ? 5.063   9.229   14.311  1.00 13.18 ? 575 HOH B O   1 
HETATM 9201 O  O   . HOH BA 6 .   ? -29.818 -2.906  7.226   1.00 24.06 ? 576 HOH B O   1 
HETATM 9202 O  O   . HOH BA 6 .   ? -2.650  -0.255  25.317  1.00 22.87 ? 577 HOH B O   1 
HETATM 9203 O  O   . HOH BA 6 .   ? 2.322   6.161   -12.439 1.00 18.65 ? 578 HOH B O   1 
HETATM 9204 O  O   . HOH BA 6 .   ? 4.333   3.330   -5.956  1.00 19.31 ? 579 HOH B O   1 
HETATM 9205 O  O   . HOH BA 6 .   ? -20.828 -0.368  -13.834 1.00 27.41 ? 580 HOH B O   1 
HETATM 9206 O  O   . HOH BA 6 .   ? -26.133 -9.571  6.259   1.00 24.99 ? 581 HOH B O   1 
HETATM 9207 O  O   . HOH BA 6 .   ? -0.875  16.038  -8.708  1.00 23.00 ? 582 HOH B O   1 
HETATM 9208 O  O   . HOH BA 6 .   ? 4.312   8.194   7.717   1.00 9.42  ? 583 HOH B O   1 
HETATM 9209 O  O   . HOH BA 6 .   ? -20.495 11.990  -12.658 1.00 33.17 ? 584 HOH B O   1 
HETATM 9210 O  O   . HOH BA 6 .   ? -8.493  -16.670 9.290   1.00 37.52 ? 585 HOH B O   1 
HETATM 9211 O  O   . HOH BA 6 .   ? -8.216  -16.344 -10.555 1.00 35.31 ? 586 HOH B O   1 
HETATM 9212 O  O   . HOH BA 6 .   ? -24.181 8.983   -1.670  1.00 16.77 ? 587 HOH B O   1 
HETATM 9213 O  O   . HOH BA 6 .   ? -2.798  1.581   -14.682 1.00 20.37 ? 588 HOH B O   1 
HETATM 9214 O  O   . HOH BA 6 .   ? -5.954  -15.444 13.137  1.00 25.13 ? 589 HOH B O   1 
HETATM 9215 O  O   . HOH BA 6 .   ? -32.490 -3.816  -1.788  1.00 26.27 ? 590 HOH B O   1 
HETATM 9216 O  O   . HOH BA 6 .   ? -31.079 2.317   1.887   1.00 24.48 ? 591 HOH B O   1 
HETATM 9217 O  O   . HOH BA 6 .   ? 4.062   -4.763  0.798   1.00 30.47 ? 592 HOH B O   1 
HETATM 9218 O  O   . HOH BA 6 .   ? -30.805 7.266   -4.241  1.00 23.33 ? 593 HOH B O   1 
HETATM 9219 O  O   . HOH BA 6 .   ? 6.031   -6.020  14.646  1.00 22.04 ? 594 HOH B O   1 
HETATM 9220 O  O   . HOH BA 6 .   ? 7.082   -0.956  17.826  1.00 22.14 ? 595 HOH B O   1 
HETATM 9221 O  O   . HOH BA 6 .   ? 1.216   13.253  19.481  1.00 26.89 ? 596 HOH B O   1 
HETATM 9222 O  O   . HOH BA 6 .   ? -14.654 -14.019 0.838   1.00 17.01 ? 597 HOH B O   1 
HETATM 9223 O  O   . HOH BA 6 .   ? 0.022   -13.669 8.368   1.00 31.65 ? 598 HOH B O   1 
HETATM 9224 O  O   . HOH BA 6 .   ? 8.755   8.867   1.846   1.00 15.34 ? 599 HOH B O   1 
HETATM 9225 O  O   . HOH BA 6 .   ? -0.491  -0.011  26.984  1.00 39.71 ? 600 HOH B O   1 
HETATM 9226 O  O   . HOH BA 6 .   ? -14.500 -11.055 23.886  1.00 29.64 ? 601 HOH B O   1 
HETATM 9227 O  O   . HOH BA 6 .   ? -13.359 -11.855 11.725  1.00 12.00 ? 602 HOH B O   1 
HETATM 9228 O  O   . HOH BA 6 .   ? -9.786  7.276   19.777  1.00 32.61 ? 603 HOH B O   1 
HETATM 9229 O  O   . HOH BA 6 .   ? -16.208 -5.818  -12.684 1.00 23.84 ? 604 HOH B O   1 
HETATM 9230 O  O   . HOH BA 6 .   ? -22.800 6.070   -12.411 1.00 20.71 ? 605 HOH B O   1 
HETATM 9231 O  O   . HOH BA 6 .   ? -13.030 -17.129 6.904   1.00 32.31 ? 606 HOH B O   1 
HETATM 9232 O  O   . HOH BA 6 .   ? 3.790   -16.042 18.071  1.00 37.39 ? 607 HOH B O   1 
HETATM 9233 O  O   . HOH BA 6 .   ? -11.179 -15.777 3.332   1.00 26.45 ? 608 HOH B O   1 
HETATM 9234 O  O   . HOH BA 6 .   ? -10.376 -10.465 29.759  1.00 19.80 ? 609 HOH B O   1 
HETATM 9235 O  O   . HOH BA 6 .   ? -33.599 3.051   2.684   1.00 34.33 ? 610 HOH B O   1 
HETATM 9236 O  O   . HOH BA 6 .   ? 4.377   -2.087  6.461   1.00 14.18 ? 611 HOH B O   1 
HETATM 9237 O  O   . HOH BA 6 .   ? -6.917  7.007   19.321  1.00 22.74 ? 612 HOH B O   1 
HETATM 9238 O  O   . HOH BA 6 .   ? 3.400   15.268  1.645   1.00 25.16 ? 613 HOH B O   1 
HETATM 9239 O  O   . HOH BA 6 .   ? -32.012 -6.432  6.290   1.00 29.89 ? 614 HOH B O   1 
HETATM 9240 O  O   . HOH BA 6 .   ? -3.290  -12.443 -0.849  1.00 16.85 ? 615 HOH B O   1 
HETATM 9241 O  O   . HOH BA 6 .   ? -2.047  11.682  -5.120  1.00 16.82 ? 616 HOH B O   1 
HETATM 9242 O  O   . HOH BA 6 .   ? -4.256  -13.121 26.011  1.00 26.49 ? 617 HOH B O   1 
HETATM 9243 O  O   . HOH BA 6 .   ? -19.617 -13.561 14.533  1.00 20.01 ? 618 HOH B O   1 
HETATM 9244 O  O   . HOH BA 6 .   ? -23.257 11.521  -1.109  1.00 19.85 ? 619 HOH B O   1 
HETATM 9245 O  O   . HOH BA 6 .   ? -12.407 -0.529  22.968  1.00 21.41 ? 620 HOH B O   1 
HETATM 9246 O  O   . HOH BA 6 .   ? -27.418 -6.067  -4.699  1.00 34.15 ? 621 HOH B O   1 
HETATM 9247 O  O   . HOH BA 6 .   ? -13.932 9.446   -17.918 1.00 36.09 ? 622 HOH B O   1 
HETATM 9248 O  O   . HOH BA 6 .   ? -9.510  16.783  -15.958 1.00 24.00 ? 623 HOH B O   1 
HETATM 9249 O  O   . HOH BA 6 .   ? 7.764   -3.278  3.468   1.00 19.08 ? 624 HOH B O   1 
HETATM 9250 O  O   . HOH BA 6 .   ? -25.159 -4.326  21.101  1.00 38.12 ? 625 HOH B O   1 
HETATM 9251 O  O   . HOH BA 6 .   ? 3.431   21.392  9.461   1.00 20.63 ? 626 HOH B O   1 
HETATM 9252 O  O   . HOH BA 6 .   ? -29.563 8.520   6.358   1.00 36.54 ? 627 HOH B O   1 
HETATM 9253 O  O   . HOH BA 6 .   ? -5.724  18.295  11.689  1.00 33.35 ? 628 HOH B O   1 
HETATM 9254 O  O   . HOH BA 6 .   ? 6.317   7.743   17.561  1.00 34.31 ? 629 HOH B O   1 
HETATM 9255 O  O   . HOH BA 6 .   ? -5.840  14.935  3.248   1.00 34.42 ? 630 HOH B O   1 
HETATM 9256 O  O   . HOH BA 6 .   ? -20.260 -13.153 11.651  1.00 31.49 ? 631 HOH B O   1 
HETATM 9257 O  O   . HOH BA 6 .   ? -14.944 -14.623 -2.503  1.00 17.27 ? 632 HOH B O   1 
HETATM 9258 O  O   . HOH BA 6 .   ? -2.607  -12.988 23.923  1.00 33.69 ? 633 HOH B O   1 
HETATM 9259 O  O   . HOH BA 6 .   ? -2.610  -10.720 -14.796 1.00 27.70 ? 634 HOH B O   1 
HETATM 9260 O  O   . HOH BA 6 .   ? -10.916 17.016  -7.791  1.00 27.59 ? 635 HOH B O   1 
HETATM 9261 O  O   . HOH BA 6 .   ? -5.996  15.737  16.182  1.00 29.04 ? 636 HOH B O   1 
HETATM 9262 O  O   . HOH BA 6 .   ? -17.277 -16.554 3.618   1.00 43.08 ? 637 HOH B O   1 
HETATM 9263 O  O   . HOH BA 6 .   ? -34.776 -2.613  -2.396  1.00 31.04 ? 638 HOH B O   1 
HETATM 9264 O  O   . HOH BA 6 .   ? -0.026  21.756  0.503   1.00 43.44 ? 639 HOH B O   1 
HETATM 9265 O  O   . HOH BA 6 .   ? -20.291 -4.139  26.079  1.00 25.13 ? 640 HOH B O   1 
HETATM 9266 O  O   . HOH BA 6 .   ? 4.149   14.796  -10.920 1.00 30.70 ? 641 HOH B O   1 
HETATM 9267 O  O   . HOH BA 6 .   ? -18.065 13.262  -1.477  1.00 34.55 ? 642 HOH B O   1 
HETATM 9268 O  O   . HOH BA 6 .   ? -13.699 13.721  -2.009  1.00 37.02 ? 643 HOH B O   1 
HETATM 9269 O  O   . HOH BA 6 .   ? -2.548  17.162  -1.482  1.00 34.94 ? 644 HOH B O   1 
HETATM 9270 O  O   . HOH BA 6 .   ? -24.593 -1.132  -11.516 1.00 20.34 ? 645 HOH B O   1 
HETATM 9271 O  O   . HOH BA 6 .   ? 5.969   -2.473  1.642   1.00 26.87 ? 646 HOH B O   1 
HETATM 9272 O  O   . HOH BA 6 .   ? -0.543  -12.620 15.591  1.00 35.48 ? 647 HOH B O   1 
HETATM 9273 O  O   . HOH BA 6 .   ? -29.284 9.460   -6.072  1.00 37.40 ? 648 HOH B O   1 
HETATM 9274 O  O   . HOH BA 6 .   ? 1.374   -0.397  -12.146 1.00 25.91 ? 649 HOH B O   1 
HETATM 9275 O  O   . HOH BA 6 .   ? -9.563  -18.034 12.707  1.00 41.84 ? 650 HOH B O   1 
HETATM 9276 O  O   . HOH BA 6 .   ? -15.483 21.083  10.175  1.00 39.01 ? 651 HOH B O   1 
HETATM 9277 O  O   . HOH BA 6 .   ? 0.334   3.982   24.833  1.00 39.34 ? 652 HOH B O   1 
HETATM 9278 O  O   . HOH BA 6 .   ? 2.255   15.885  16.715  1.00 44.45 ? 653 HOH B O   1 
HETATM 9279 O  O   . HOH BA 6 .   ? 11.562  14.577  -0.234  1.00 28.71 ? 654 HOH B O   1 
HETATM 9280 O  O   . HOH BA 6 .   ? -13.191 -16.929 19.172  1.00 38.53 ? 655 HOH B O   1 
HETATM 9281 O  O   . HOH BA 6 .   ? 7.690   1.373   19.883  1.00 23.93 ? 656 HOH B O   1 
HETATM 9282 O  O   . HOH BA 6 .   ? 2.382   6.996   23.597  1.00 42.65 ? 657 HOH B O   1 
HETATM 9283 O  O   . HOH BA 6 .   ? -8.965  1.610   -19.383 1.00 31.86 ? 658 HOH B O   1 
HETATM 9284 O  O   . HOH BA 6 .   ? -21.432 -6.588  -9.886  1.00 28.75 ? 659 HOH B O   1 
HETATM 9285 O  O   . HOH BA 6 .   ? 7.740   -16.158 7.731   1.00 45.95 ? 660 HOH B O   1 
HETATM 9286 O  O   . HOH BA 6 .   ? -1.156  -13.104 4.224   1.00 46.86 ? 661 HOH B O   1 
HETATM 9287 O  O   . HOH BA 6 .   ? -8.685  17.709  -3.608  1.00 38.17 ? 662 HOH B O   1 
HETATM 9288 O  O   . HOH BA 6 .   ? -12.281 -19.815 24.465  1.00 27.58 ? 663 HOH B O   1 
HETATM 9289 O  O   . HOH BA 6 .   ? -31.648 0.088   5.937   1.00 35.28 ? 664 HOH B O   1 
HETATM 9290 O  O   . HOH BA 6 .   ? -14.887 -0.243  28.414  1.00 33.13 ? 665 HOH B O   1 
HETATM 9291 O  O   . HOH BA 6 .   ? -17.599 -14.173 -2.251  1.00 26.21 ? 666 HOH B O   1 
HETATM 9292 O  O   . HOH BA 6 .   ? 12.286  11.441  -3.757  1.00 28.21 ? 667 HOH B O   1 
HETATM 9293 O  O   . HOH BA 6 .   ? -0.301  -13.251 -4.307  1.00 27.00 ? 668 HOH B O   1 
HETATM 9294 O  O   . HOH BA 6 .   ? -12.891 14.102  -4.736  1.00 34.76 ? 669 HOH B O   1 
HETATM 9295 O  O   . HOH BA 6 .   ? -23.333 -4.425  -10.107 1.00 31.03 ? 670 HOH B O   1 
HETATM 9296 O  O   . HOH BA 6 .   ? -13.481 8.046   26.917  1.00 37.07 ? 671 HOH B O   1 
HETATM 9297 O  O   . HOH BA 6 .   ? -22.258 12.320  -10.725 1.00 34.80 ? 672 HOH B O   1 
HETATM 9298 O  O   . HOH BA 6 .   ? -12.723 -9.096  -12.563 1.00 21.77 ? 673 HOH B O   1 
HETATM 9299 O  O   . HOH BA 6 .   ? 1.085   22.599  10.137  1.00 29.01 ? 674 HOH B O   1 
HETATM 9300 O  O   . HOH BA 6 .   ? -10.845 15.131  -5.284  1.00 34.66 ? 675 HOH B O   1 
HETATM 9301 O  O   . HOH BA 6 .   ? -8.216  -5.466  -15.433 1.00 23.25 ? 676 HOH B O   1 
HETATM 9302 O  O   . HOH BA 6 .   ? 7.662   7.444   -0.153  1.00 19.76 ? 677 HOH B O   1 
HETATM 9303 O  O   . HOH BA 6 .   ? 5.137   12.102  -11.231 1.00 36.79 ? 678 HOH B O   1 
HETATM 9304 O  O   . HOH BA 6 .   ? -23.819 -10.829 5.371   1.00 36.00 ? 679 HOH B O   1 
HETATM 9305 O  O   . HOH BA 6 .   ? 5.877   2.305   -3.623  1.00 26.19 ? 680 HOH B O   1 
HETATM 9306 O  O   . HOH BA 6 .   ? -12.429 17.225  -11.460 1.00 38.21 ? 681 HOH B O   1 
HETATM 9307 O  O   . HOH BA 6 .   ? -29.207 -7.413  6.638   1.00 28.22 ? 682 HOH B O   1 
HETATM 9308 O  O   . HOH BA 6 .   ? -18.560 -13.740 -0.002  1.00 31.67 ? 683 HOH B O   1 
HETATM 9309 O  O   . HOH BA 6 .   ? -16.622 -14.190 27.796  1.00 23.29 ? 684 HOH B O   1 
HETATM 9310 O  O   . HOH BA 6 .   ? -11.507 -8.232  -14.899 1.00 26.44 ? 685 HOH B O   1 
HETATM 9311 O  O   . HOH BA 6 .   ? -3.700  16.216  -8.682  1.00 26.42 ? 686 HOH B O   1 
HETATM 9312 O  O   . HOH BA 6 .   ? 2.435   -11.239 -11.600 1.00 36.14 ? 687 HOH B O   1 
HETATM 9313 O  O   . HOH BA 6 .   ? 8.191   10.630  -7.650  1.00 35.03 ? 688 HOH B O   1 
HETATM 9314 O  O   . HOH BA 6 .   ? -21.399 -11.849 15.963  1.00 23.05 ? 689 HOH B O   1 
HETATM 9315 O  O   . HOH BA 6 .   ? 4.420   -12.010 24.713  1.00 35.66 ? 690 HOH B O   1 
HETATM 9316 O  O   . HOH BA 6 .   ? -29.454 7.172   1.083   1.00 31.99 ? 691 HOH B O   1 
HETATM 9317 O  O   . HOH BA 6 .   ? 7.669   -9.350  15.764  1.00 18.24 ? 692 HOH B O   1 
HETATM 9318 O  O   . HOH BA 6 .   ? -3.463  -17.510 19.760  1.00 25.49 ? 693 HOH B O   1 
HETATM 9319 O  O   . HOH BA 6 .   ? 4.405   15.439  18.018  1.00 34.18 ? 694 HOH B O   1 
HETATM 9320 O  O   . HOH BA 6 .   ? -21.573 10.150  -14.665 1.00 35.02 ? 695 HOH B O   1 
HETATM 9321 O  O   . HOH BA 6 .   ? 2.029   -15.820 16.538  1.00 29.74 ? 696 HOH B O   1 
HETATM 9322 O  O   . HOH BA 6 .   ? -19.266 -16.346 -3.769  1.00 30.00 ? 697 HOH B O   1 
HETATM 9323 O  O   . HOH BA 6 .   ? 5.461   -13.117 15.815  1.00 23.84 ? 698 HOH B O   1 
HETATM 9324 O  O   . HOH BA 6 .   ? -15.617 -14.520 3.620   1.00 28.23 ? 699 HOH B O   1 
HETATM 9325 O  O   . HOH BA 6 .   ? -4.530  -13.774 9.637   1.00 27.08 ? 700 HOH B O   1 
HETATM 9326 O  O   . HOH BA 6 .   ? -29.249 -5.997  -2.716  1.00 38.50 ? 701 HOH B O   1 
HETATM 9327 O  O   . HOH BA 6 .   ? 5.783   -0.531  -2.587  1.00 24.54 ? 702 HOH B O   1 
HETATM 9328 O  O   . HOH BA 6 .   ? -15.256 -16.964 -0.867  1.00 32.41 ? 703 HOH B O   1 
HETATM 9329 O  O   . HOH BA 6 .   ? -15.144 11.133  -19.483 1.00 38.99 ? 704 HOH B O   1 
HETATM 9330 O  O   . HOH BA 6 .   ? -18.616 -11.693 23.880  1.00 27.99 ? 705 HOH B O   1 
HETATM 9331 O  O   . HOH BA 6 .   ? -10.961 17.098  -18.683 1.00 33.03 ? 706 HOH B O   1 
HETATM 9332 O  O   . HOH BA 6 .   ? 5.006   -7.242  1.122   1.00 19.78 ? 707 HOH B O   1 
HETATM 9333 O  O   . HOH BA 6 .   ? -7.777  18.469  10.273  1.00 36.64 ? 708 HOH B O   1 
HETATM 9334 O  O   . HOH BA 6 .   ? -22.784 -12.400 1.471   1.00 36.88 ? 709 HOH B O   1 
HETATM 9335 O  O   . HOH BA 6 .   ? -17.799 -12.665 21.399  1.00 24.58 ? 710 HOH B O   1 
HETATM 9336 O  O   . HOH BA 6 .   ? 1.520   -15.214 23.137  1.00 31.64 ? 711 HOH B O   1 
HETATM 9337 O  O   . HOH BA 6 .   ? -3.055  15.201  18.790  1.00 30.54 ? 712 HOH B O   1 
HETATM 9338 O  O   . HOH BA 6 .   ? -3.742  -14.604 17.276  1.00 31.40 ? 713 HOH B O   1 
HETATM 9339 O  O   . HOH BA 6 .   ? -0.600  -12.114 -8.807  1.00 22.79 ? 714 HOH B O   1 
HETATM 9340 O  O   . HOH BA 6 .   ? -0.828  24.012  6.946   1.00 33.12 ? 715 HOH B O   1 
HETATM 9341 O  O   . HOH BA 6 .   ? -3.940  1.810   24.141  1.00 26.02 ? 716 HOH B O   1 
HETATM 9342 O  O   . HOH BA 6 .   ? -20.878 -10.670 -9.988  1.00 24.07 ? 717 HOH B O   1 
HETATM 9343 O  O   . HOH BA 6 .   ? 5.554   9.787   -9.139  1.00 32.65 ? 718 HOH B O   1 
HETATM 9344 O  O   . HOH BA 6 .   ? -2.303  11.013  21.173  1.00 63.05 ? 719 HOH B O   1 
HETATM 9345 O  O   . HOH BA 6 .   ? 3.894   6.230   -9.882  1.00 29.35 ? 720 HOH B O   1 
HETATM 9346 O  O   . HOH BA 6 .   ? -1.735  20.202  13.152  1.00 37.02 ? 721 HOH B O   1 
HETATM 9347 O  O   . HOH BA 6 .   ? -19.038 -15.913 15.411  1.00 30.07 ? 722 HOH B O   1 
HETATM 9348 O  O   . HOH BA 6 .   ? -2.971  18.915  10.780  1.00 28.66 ? 723 HOH B O   1 
HETATM 9349 O  O   . HOH BA 6 .   ? -12.859 -14.291 30.917  1.00 20.30 ? 724 HOH B O   1 
HETATM 9350 O  O   . HOH BA 6 .   ? -7.804  -9.928  -15.827 1.00 19.49 ? 725 HOH B O   1 
HETATM 9351 O  O   . HOH BA 6 .   ? -1.975  -15.424 11.147  1.00 30.14 ? 726 HOH B O   1 
HETATM 9352 O  O   . HOH BA 6 .   ? -10.248 -13.109 30.574  1.00 22.10 ? 727 HOH B O   1 
HETATM 9353 O  O   . HOH BA 6 .   ? -2.403  -14.459 8.915   1.00 36.09 ? 728 HOH B O   1 
HETATM 9354 O  O   . HOH BA 6 .   ? -21.634 -14.640 -3.029  1.00 38.32 ? 729 HOH B O   1 
HETATM 9355 O  O   . HOH BA 6 .   ? 12.717  11.433  -6.385  1.00 31.14 ? 730 HOH B O   1 
HETATM 9356 O  O   . HOH BA 6 .   ? -4.136  19.267  8.234   1.00 35.57 ? 731 HOH B O   1 
HETATM 9357 O  O   . HOH BA 6 .   ? -21.997 -13.371 -9.481  1.00 30.98 ? 732 HOH B O   1 
HETATM 9358 O  O   . HOH BA 6 .   ? -21.831 -13.491 18.215  1.00 35.35 ? 733 HOH B O   1 
HETATM 9359 O  O   . HOH BA 6 .   ? -17.382 -18.065 0.186   1.00 39.60 ? 734 HOH B O   1 
HETATM 9360 O  O   . HOH CA 6 .   ? 20.542  4.025   -46.976 1.00 27.46 ? 401 HOH C O   1 
HETATM 9361 O  O   . HOH CA 6 .   ? 20.253  1.016   -45.577 1.00 25.25 ? 402 HOH C O   1 
HETATM 9362 O  O   . HOH CA 6 .   ? 19.700  1.155   -51.514 1.00 26.36 ? 403 HOH C O   1 
HETATM 9363 O  O   . HOH CA 6 .   ? 32.755  13.044  -8.483  1.00 27.85 ? 404 HOH C O   1 
HETATM 9364 O  O   . HOH CA 6 .   ? 20.649  -2.008  -50.861 1.00 33.12 ? 405 HOH C O   1 
HETATM 9365 O  O   . HOH CA 6 .   ? 50.530  -4.518  -54.109 1.00 34.64 ? 406 HOH C O   1 
HETATM 9366 O  O   . HOH CA 6 .   ? 25.470  14.641  -23.223 1.00 29.88 ? 407 HOH C O   1 
HETATM 9367 O  O   . HOH CA 6 .   ? 47.329  -1.352  -9.497  1.00 25.39 ? 408 HOH C O   1 
HETATM 9368 O  O   . HOH CA 6 .   ? 34.061  -5.100  -54.937 1.00 38.67 ? 409 HOH C O   1 
HETATM 9369 O  O   . HOH CA 6 .   ? 26.175  -8.205  -15.816 1.00 29.77 ? 410 HOH C O   1 
HETATM 9370 O  O   . HOH CA 6 .   ? 38.350  -13.479 -13.163 1.00 36.77 ? 411 HOH C O   1 
HETATM 9371 O  O   . HOH CA 6 .   ? 58.147  -4.176  -41.625 1.00 39.86 ? 412 HOH C O   1 
HETATM 9372 O  O   . HOH CA 6 .   ? 58.436  -1.817  -29.856 1.00 29.97 ? 413 HOH C O   1 
HETATM 9373 O  O   . HOH CA 6 .   ? 43.770  -5.846  -50.143 1.00 24.50 ? 414 HOH C O   1 
HETATM 9374 O  O   . HOH CA 6 .   ? 33.474  18.004  -27.915 1.00 37.01 ? 415 HOH C O   1 
HETATM 9375 O  O   . HOH CA 6 .   ? 56.928  -8.145  -23.144 1.00 35.92 ? 416 HOH C O   1 
HETATM 9376 O  O   . HOH CA 6 .   ? 27.282  25.097  -32.264 1.00 15.42 ? 417 HOH C O   1 
HETATM 9377 O  O   . HOH CA 6 .   ? 27.906  15.802  -29.419 1.00 26.77 ? 418 HOH C O   1 
HETATM 9378 O  O   . HOH CA 6 .   ? 33.215  12.255  -11.087 1.00 24.25 ? 419 HOH C O   1 
HETATM 9379 O  O   . HOH CA 6 .   ? 28.389  18.150  -31.637 1.00 16.81 ? 420 HOH C O   1 
HETATM 9380 O  O   . HOH CA 6 .   ? 22.146  -8.930  -39.634 1.00 27.79 ? 421 HOH C O   1 
HETATM 9381 O  O   . HOH CA 6 .   ? 33.129  -1.787  -48.866 1.00 24.06 ? 422 HOH C O   1 
HETATM 9382 O  O   . HOH CA 6 .   ? 42.259  -9.755  -11.666 1.00 41.72 ? 423 HOH C O   1 
HETATM 9383 O  O   . HOH CA 6 .   ? 20.392  17.841  -29.828 1.00 29.12 ? 424 HOH C O   1 
HETATM 9384 O  O   . HOH CA 6 .   ? 22.263  -6.407  -31.407 1.00 22.20 ? 425 HOH C O   1 
HETATM 9385 O  O   . HOH CA 6 .   ? 46.942  9.102   -27.108 1.00 26.04 ? 426 HOH C O   1 
HETATM 9386 O  O   . HOH CA 6 .   ? 52.607  4.826   -48.762 1.00 26.13 ? 427 HOH C O   1 
HETATM 9387 O  O   . HOH CA 6 .   ? 38.435  10.258  -31.438 1.00 24.35 ? 428 HOH C O   1 
HETATM 9388 O  O   . HOH CA 6 .   ? 56.265  7.904   -37.500 1.00 48.19 ? 429 HOH C O   1 
HETATM 9389 O  O   . HOH CA 6 .   ? 35.508  -13.784 -54.338 1.00 22.40 ? 430 HOH C O   1 
HETATM 9390 O  O   . HOH CA 6 .   ? 53.631  -10.071 -22.302 1.00 24.90 ? 431 HOH C O   1 
HETATM 9391 O  O   . HOH CA 6 .   ? 32.397  5.077   -30.549 1.00 12.22 ? 432 HOH C O   1 
HETATM 9392 O  O   . HOH CA 6 .   ? 53.783  -13.318 -25.328 1.00 29.67 ? 433 HOH C O   1 
HETATM 9393 O  O   . HOH CA 6 .   ? 51.130  8.312   -31.041 1.00 27.35 ? 434 HOH C O   1 
HETATM 9394 O  O   . HOH CA 6 .   ? 46.824  11.456  -21.638 1.00 32.46 ? 435 HOH C O   1 
HETATM 9395 O  O   . HOH CA 6 .   ? 25.833  5.348   -24.014 1.00 30.99 ? 436 HOH C O   1 
HETATM 9396 O  O   . HOH CA 6 .   ? 47.446  -13.724 -29.347 1.00 35.37 ? 437 HOH C O   1 
HETATM 9397 O  O   . HOH CA 6 .   ? 56.594  4.450   -41.876 1.00 19.97 ? 438 HOH C O   1 
HETATM 9398 O  O   . HOH CA 6 .   ? 27.242  -10.315 -26.553 1.00 23.83 ? 439 HOH C O   1 
HETATM 9399 O  O   . HOH CA 6 .   ? 51.832  -4.991  -17.926 1.00 29.91 ? 440 HOH C O   1 
HETATM 9400 O  O   . HOH CA 6 .   ? 25.180  -1.828  -40.570 1.00 11.90 ? 441 HOH C O   1 
HETATM 9401 O  O   . HOH CA 6 .   ? 25.247  8.202   -27.993 1.00 16.33 ? 442 HOH C O   1 
HETATM 9402 O  O   . HOH CA 6 .   ? 28.497  -7.735  -16.978 1.00 24.60 ? 443 HOH C O   1 
HETATM 9403 O  O   . HOH CA 6 .   ? 56.238  3.842   -12.877 1.00 16.48 ? 444 HOH C O   1 
HETATM 9404 O  O   . HOH CA 6 .   ? 46.490  8.181   -11.456 1.00 22.09 ? 445 HOH C O   1 
HETATM 9405 O  O   . HOH CA 6 .   ? 59.666  -2.743  -25.727 1.00 31.30 ? 446 HOH C O   1 
HETATM 9406 O  O   . HOH CA 6 .   ? 23.943  13.072  -42.506 1.00 13.19 ? 447 HOH C O   1 
HETATM 9407 O  O   . HOH CA 6 .   ? 56.397  9.110   -40.282 1.00 28.81 ? 448 HOH C O   1 
HETATM 9408 O  O   . HOH CA 6 .   ? 42.917  -1.078  -10.716 1.00 30.60 ? 449 HOH C O   1 
HETATM 9409 O  O   . HOH CA 6 .   ? 43.184  -2.517  -40.380 1.00 11.53 ? 450 HOH C O   1 
HETATM 9410 O  O   . HOH CA 6 .   ? 52.270  1.304   -12.934 1.00 32.04 ? 451 HOH C O   1 
HETATM 9411 O  O   . HOH CA 6 .   ? 23.853  8.872   -34.971 1.00 13.18 ? 452 HOH C O   1 
HETATM 9412 O  O   . HOH CA 6 .   ? 28.451  3.228   -43.461 1.00 16.25 ? 453 HOH C O   1 
HETATM 9413 O  O   . HOH CA 6 .   ? 26.257  7.094   -14.110 1.00 31.66 ? 454 HOH C O   1 
HETATM 9414 O  O   . HOH CA 6 .   ? 44.395  -14.983 -50.277 1.00 28.58 ? 455 HOH C O   1 
HETATM 9415 O  O   . HOH CA 6 .   ? 59.562  -7.870  -21.066 1.00 42.17 ? 456 HOH C O   1 
HETATM 9416 O  O   . HOH CA 6 .   ? 53.079  14.370  -44.487 1.00 38.06 ? 457 HOH C O   1 
HETATM 9417 O  O   . HOH CA 6 .   ? 39.694  14.094  -12.699 1.00 29.92 ? 458 HOH C O   1 
HETATM 9418 O  O   . HOH CA 6 .   ? 35.088  6.042   -26.805 1.00 21.69 ? 459 HOH C O   1 
HETATM 9419 O  O   . HOH CA 6 .   ? 61.863  -1.089  -32.508 1.00 26.20 ? 460 HOH C O   1 
HETATM 9420 O  O   . HOH CA 6 .   ? 36.075  -9.845  -53.456 1.00 35.43 ? 461 HOH C O   1 
HETATM 9421 O  O   . HOH CA 6 .   ? 21.942  -0.913  -23.666 1.00 24.76 ? 462 HOH C O   1 
HETATM 9422 O  O   . HOH CA 6 .   ? 47.614  -8.932  -51.269 1.00 29.96 ? 463 HOH C O   1 
HETATM 9423 O  O   . HOH CA 6 .   ? 44.794  16.629  -38.777 1.00 32.02 ? 464 HOH C O   1 
HETATM 9424 O  O   . HOH CA 6 .   ? 48.594  -13.150 -33.789 1.00 29.10 ? 465 HOH C O   1 
HETATM 9425 O  O   . HOH CA 6 .   ? 22.512  -2.118  -31.318 1.00 27.43 ? 466 HOH C O   1 
HETATM 9426 O  O   . HOH CA 6 .   ? 25.998  6.850   -41.217 1.00 10.78 ? 467 HOH C O   1 
HETATM 9427 O  O   . HOH CA 6 .   ? 48.144  16.999  -35.344 1.00 43.28 ? 468 HOH C O   1 
HETATM 9428 O  O   . HOH CA 6 .   ? 29.535  -4.810  -21.996 1.00 15.73 ? 469 HOH C O   1 
HETATM 9429 O  O   . HOH CA 6 .   ? 32.741  -13.429 -36.755 1.00 17.52 ? 470 HOH C O   1 
HETATM 9430 O  O   . HOH CA 6 .   ? 27.343  16.192  -41.379 1.00 13.46 ? 471 HOH C O   1 
HETATM 9431 O  O   . HOH CA 6 .   ? 32.961  16.351  -15.031 1.00 37.48 ? 472 HOH C O   1 
HETATM 9432 O  O   . HOH CA 6 .   ? 22.874  -11.528 -44.276 1.00 32.55 ? 473 HOH C O   1 
HETATM 9433 O  O   . HOH CA 6 .   ? 35.199  16.986  -41.754 1.00 28.53 ? 474 HOH C O   1 
HETATM 9434 O  O   . HOH CA 6 .   ? 34.128  15.827  -38.449 1.00 10.28 ? 475 HOH C O   1 
HETATM 9435 O  O   . HOH CA 6 .   ? 43.611  3.984   -44.317 1.00 19.74 ? 476 HOH C O   1 
HETATM 9436 O  O   . HOH CA 6 .   ? 41.978  7.054   -9.758  1.00 36.83 ? 477 HOH C O   1 
HETATM 9437 O  O   . HOH CA 6 .   ? 46.985  7.305   -22.798 1.00 20.82 ? 478 HOH C O   1 
HETATM 9438 O  O   . HOH CA 6 .   ? 24.623  -13.117 -41.449 1.00 24.09 ? 479 HOH C O   1 
HETATM 9439 O  O   . HOH CA 6 .   ? 26.639  9.308   -34.736 1.00 11.39 ? 480 HOH C O   1 
HETATM 9440 O  O   . HOH CA 6 .   ? 54.721  1.332   -14.747 1.00 28.78 ? 481 HOH C O   1 
HETATM 9441 O  O   . HOH CA 6 .   ? 38.764  2.255   -6.057  1.00 20.08 ? 482 HOH C O   1 
HETATM 9442 O  O   . HOH CA 6 .   ? 27.182  7.388   -18.838 1.00 34.58 ? 483 HOH C O   1 
HETATM 9443 O  O   . HOH CA 6 .   ? 26.994  -0.901  -32.158 1.00 9.67  ? 484 HOH C O   1 
HETATM 9444 O  O   . HOH CA 6 .   ? 51.471  -2.536  -43.570 1.00 21.28 ? 485 HOH C O   1 
HETATM 9445 O  O   . HOH CA 6 .   ? 35.523  -21.435 -51.017 1.00 25.26 ? 486 HOH C O   1 
HETATM 9446 O  O   . HOH CA 6 .   ? 24.276  -3.824  -44.775 1.00 23.84 ? 487 HOH C O   1 
HETATM 9447 O  O   . HOH CA 6 .   ? 24.956  6.421   -34.603 1.00 10.39 ? 488 HOH C O   1 
HETATM 9448 O  O   . HOH CA 6 .   ? 63.529  -1.889  -22.141 1.00 35.50 ? 489 HOH C O   1 
HETATM 9449 O  O   . HOH CA 6 .   ? 25.818  -3.596  -42.577 1.00 17.90 ? 490 HOH C O   1 
HETATM 9450 O  O   . HOH CA 6 .   ? 46.770  1.811   -47.316 1.00 35.01 ? 491 HOH C O   1 
HETATM 9451 O  O   . HOH CA 6 .   ? 47.041  -14.766 -32.067 1.00 30.84 ? 492 HOH C O   1 
HETATM 9452 O  O   . HOH CA 6 .   ? 25.944  5.364   -43.419 1.00 28.60 ? 493 HOH C O   1 
HETATM 9453 O  O   . HOH CA 6 .   ? 42.240  16.716  -44.646 1.00 32.16 ? 494 HOH C O   1 
HETATM 9454 O  O   . HOH CA 6 .   ? 40.604  14.225  -37.565 1.00 25.56 ? 495 HOH C O   1 
HETATM 9455 O  O   . HOH CA 6 .   ? 47.886  -12.912 -39.112 1.00 26.57 ? 496 HOH C O   1 
HETATM 9456 O  O   . HOH CA 6 .   ? 38.339  17.330  -10.824 1.00 34.58 ? 497 HOH C O   1 
HETATM 9457 O  O   . HOH CA 6 .   ? 54.540  -9.909  -30.698 1.00 23.49 ? 498 HOH C O   1 
HETATM 9458 O  O   . HOH CA 6 .   ? 20.096  -10.132 -29.794 1.00 19.10 ? 499 HOH C O   1 
HETATM 9459 O  O   . HOH CA 6 .   ? 24.834  4.621   -45.797 1.00 30.56 ? 500 HOH C O   1 
HETATM 9460 O  O   . HOH CA 6 .   ? 52.859  6.269   -31.426 1.00 19.96 ? 501 HOH C O   1 
HETATM 9461 O  O   . HOH CA 6 .   ? 41.127  7.342   -46.852 1.00 22.17 ? 502 HOH C O   1 
HETATM 9462 O  O   . HOH CA 6 .   ? 39.084  -26.515 -44.300 1.00 22.54 ? 503 HOH C O   1 
HETATM 9463 O  O   . HOH CA 6 .   ? 44.680  -14.134 -44.498 1.00 19.15 ? 504 HOH C O   1 
HETATM 9464 O  O   . HOH CA 6 .   ? 33.734  1.720   -16.464 1.00 17.66 ? 505 HOH C O   1 
HETATM 9465 O  O   . HOH CA 6 .   ? 41.417  -8.397  -54.836 1.00 19.41 ? 506 HOH C O   1 
HETATM 9466 O  O   . HOH CA 6 .   ? 37.130  8.632   -47.596 1.00 24.42 ? 507 HOH C O   1 
HETATM 9467 O  O   . HOH CA 6 .   ? 51.150  7.246   -28.365 1.00 24.98 ? 508 HOH C O   1 
HETATM 9468 O  O   . HOH CA 6 .   ? 30.111  6.536   -21.502 1.00 25.61 ? 509 HOH C O   1 
HETATM 9469 O  O   . HOH CA 6 .   ? 40.346  -16.517 -30.022 1.00 25.98 ? 510 HOH C O   1 
HETATM 9470 O  O   . HOH CA 6 .   ? 23.447  -4.687  -35.767 1.00 17.00 ? 511 HOH C O   1 
HETATM 9471 O  O   . HOH CA 6 .   ? 59.822  -2.100  -35.180 1.00 31.48 ? 512 HOH C O   1 
HETATM 9472 O  O   . HOH CA 6 .   ? 40.833  4.043   -45.959 1.00 35.77 ? 513 HOH C O   1 
HETATM 9473 O  O   . HOH CA 6 .   ? 46.117  -18.878 -33.645 1.00 31.41 ? 514 HOH C O   1 
HETATM 9474 O  O   . HOH CA 6 .   ? 49.034  2.273   -12.602 1.00 33.67 ? 515 HOH C O   1 
HETATM 9475 O  O   . HOH CA 6 .   ? 25.502  -3.256  -48.208 1.00 26.87 ? 516 HOH C O   1 
HETATM 9476 O  O   . HOH CA 6 .   ? 46.850  -13.111 -52.911 1.00 20.87 ? 517 HOH C O   1 
HETATM 9477 O  O   . HOH CA 6 .   ? 59.120  3.337   -20.505 1.00 35.11 ? 518 HOH C O   1 
HETATM 9478 O  O   . HOH CA 6 .   ? 20.854  13.452  -35.629 1.00 8.81  ? 519 HOH C O   1 
HETATM 9479 O  O   . HOH CA 6 .   ? 24.505  19.056  -28.893 1.00 33.18 ? 520 HOH C O   1 
HETATM 9480 O  O   . HOH CA 6 .   ? 26.457  -13.626 -34.501 1.00 20.95 ? 521 HOH C O   1 
HETATM 9481 O  O   . HOH CA 6 .   ? 22.355  0.291   -27.856 1.00 22.30 ? 522 HOH C O   1 
HETATM 9482 O  O   . HOH CA 6 .   ? 28.028  -10.511 -22.295 1.00 21.23 ? 523 HOH C O   1 
HETATM 9483 O  O   . HOH CA 6 .   ? 32.493  0.337   -50.797 1.00 36.21 ? 524 HOH C O   1 
HETATM 9484 O  O   . HOH CA 6 .   ? 46.154  -11.361 -40.371 1.00 23.12 ? 525 HOH C O   1 
HETATM 9485 O  O   . HOH CA 6 .   ? 23.350  4.666   -35.996 1.00 7.49  ? 526 HOH C O   1 
HETATM 9486 O  O   . HOH CA 6 .   ? 43.683  -14.757 -27.560 1.00 32.92 ? 527 HOH C O   1 
HETATM 9487 O  O   . HOH CA 6 .   ? 37.705  -10.461 -33.157 1.00 14.51 ? 528 HOH C O   1 
HETATM 9488 O  O   . HOH CA 6 .   ? 31.811  2.327   -43.679 1.00 15.21 ? 529 HOH C O   1 
HETATM 9489 O  O   . HOH CA 6 .   ? 30.208  -9.879  -16.292 1.00 38.76 ? 530 HOH C O   1 
HETATM 9490 O  O   . HOH CA 6 .   ? 22.112  6.750   -32.165 1.00 9.50  ? 531 HOH C O   1 
HETATM 9491 O  O   . HOH CA 6 .   ? 55.693  -8.247  -32.496 1.00 20.72 ? 532 HOH C O   1 
HETATM 9492 O  O   . HOH CA 6 .   ? 25.810  12.912  -35.441 1.00 10.66 ? 533 HOH C O   1 
HETATM 9493 O  O   . HOH CA 6 .   ? 29.119  9.148   -22.384 1.00 28.01 ? 534 HOH C O   1 
HETATM 9494 O  O   . HOH CA 6 .   ? 49.892  -9.387  -45.884 1.00 30.83 ? 535 HOH C O   1 
HETATM 9495 O  O   . HOH CA 6 .   ? 54.208  9.590   -33.910 1.00 30.91 ? 536 HOH C O   1 
HETATM 9496 O  O   . HOH CA 6 .   ? 24.775  -1.862  -23.531 1.00 22.85 ? 537 HOH C O   1 
HETATM 9497 O  O   . HOH CA 6 .   ? 33.590  13.339  -44.284 1.00 15.81 ? 538 HOH C O   1 
HETATM 9498 O  O   . HOH CA 6 .   ? 46.883  -16.213 -35.431 1.00 33.74 ? 539 HOH C O   1 
HETATM 9499 O  O   . HOH CA 6 .   ? 26.062  11.261  -45.443 1.00 22.38 ? 540 HOH C O   1 
HETATM 9500 O  O   . HOH CA 6 .   ? 35.690  -1.322  -48.371 1.00 19.87 ? 541 HOH C O   1 
HETATM 9501 O  O   . HOH CA 6 .   ? 32.415  11.144  -43.247 1.00 11.47 ? 542 HOH C O   1 
HETATM 9502 O  O   . HOH CA 6 .   ? 34.642  -7.389  -10.918 1.00 28.36 ? 543 HOH C O   1 
HETATM 9503 O  O   . HOH CA 6 .   ? 52.597  8.686   -23.935 1.00 27.77 ? 544 HOH C O   1 
HETATM 9504 O  O   . HOH CA 6 .   ? 23.640  5.433   -40.625 1.00 12.08 ? 545 HOH C O   1 
HETATM 9505 O  O   . HOH CA 6 .   ? 31.296  2.650   -14.612 1.00 22.68 ? 546 HOH C O   1 
HETATM 9506 O  O   . HOH CA 6 .   ? 49.119  -5.395  -49.478 1.00 41.44 ? 547 HOH C O   1 
HETATM 9507 O  O   . HOH CA 6 .   ? 43.945  13.717  -47.843 1.00 33.09 ? 548 HOH C O   1 
HETATM 9508 O  O   . HOH CA 6 .   ? 24.149  -0.807  -32.878 1.00 19.61 ? 549 HOH C O   1 
HETATM 9509 O  O   . HOH CA 6 .   ? 43.626  -12.862 -25.632 1.00 23.53 ? 550 HOH C O   1 
HETATM 9510 O  O   . HOH CA 6 .   ? 39.387  17.887  -41.008 1.00 25.59 ? 551 HOH C O   1 
HETATM 9511 O  O   . HOH CA 6 .   ? 22.317  -5.298  -41.111 1.00 23.91 ? 552 HOH C O   1 
HETATM 9512 O  O   . HOH CA 6 .   ? 47.815  18.797  -40.938 1.00 36.53 ? 553 HOH C O   1 
HETATM 9513 O  O   . HOH CA 6 .   ? 38.152  4.914   -45.286 1.00 18.14 ? 554 HOH C O   1 
HETATM 9514 O  O   . HOH CA 6 .   ? 38.985  -19.738 -46.033 1.00 35.46 ? 555 HOH C O   1 
HETATM 9515 O  O   . HOH CA 6 .   ? 28.975  5.901   -47.421 1.00 18.33 ? 556 HOH C O   1 
HETATM 9516 O  O   . HOH CA 6 .   ? 22.152  -13.859 -35.614 1.00 34.71 ? 557 HOH C O   1 
HETATM 9517 O  O   . HOH CA 6 .   ? 29.655  -12.364 -23.622 1.00 23.02 ? 558 HOH C O   1 
HETATM 9518 O  O   . HOH CA 6 .   ? 22.456  10.938  -29.319 1.00 16.28 ? 559 HOH C O   1 
HETATM 9519 O  O   . HOH CA 6 .   ? 22.265  -0.642  -44.102 1.00 21.67 ? 560 HOH C O   1 
HETATM 9520 O  O   . HOH CA 6 .   ? 48.098  -10.719 -15.647 1.00 30.24 ? 561 HOH C O   1 
HETATM 9521 O  O   . HOH CA 6 .   ? 40.815  4.046   -6.667  1.00 21.76 ? 562 HOH C O   1 
HETATM 9522 O  O   . HOH CA 6 .   ? 39.697  -11.966 -54.991 1.00 24.15 ? 563 HOH C O   1 
HETATM 9523 O  O   . HOH CA 6 .   ? 39.069  10.995  -28.793 1.00 34.12 ? 564 HOH C O   1 
HETATM 9524 O  O   . HOH CA 6 .   ? 19.571  -7.652  -17.410 1.00 30.01 ? 565 HOH C O   1 
HETATM 9525 O  O   . HOH CA 6 .   ? 38.760  -2.705  -11.415 1.00 34.19 ? 566 HOH C O   1 
HETATM 9526 O  O   . HOH CA 6 .   ? 52.928  -11.329 -36.622 1.00 29.24 ? 567 HOH C O   1 
HETATM 9527 O  O   . HOH CA 6 .   ? 28.082  -10.620 -51.153 1.00 42.44 ? 568 HOH C O   1 
HETATM 9528 O  O   . HOH CA 6 .   ? 53.552  -3.994  -45.989 1.00 32.50 ? 569 HOH C O   1 
HETATM 9529 O  O   . HOH CA 6 .   ? 41.466  9.260   -7.750  1.00 29.34 ? 570 HOH C O   1 
HETATM 9530 O  O   . HOH CA 6 .   ? 29.456  -13.896 -27.863 1.00 28.68 ? 571 HOH C O   1 
HETATM 9531 O  O   . HOH CA 6 .   ? 31.426  12.513  -46.578 1.00 21.40 ? 572 HOH C O   1 
HETATM 9532 O  O   . HOH CA 6 .   ? 26.290  9.589   -41.765 1.00 13.18 ? 573 HOH C O   1 
HETATM 9533 O  O   . HOH CA 6 .   ? 37.804  14.191  -29.360 1.00 42.42 ? 574 HOH C O   1 
HETATM 9534 O  O   . HOH CA 6 .   ? 35.564  19.356  -35.809 1.00 53.78 ? 575 HOH C O   1 
HETATM 9535 O  O   . HOH CA 6 .   ? 43.346  -19.746 -40.533 1.00 32.84 ? 576 HOH C O   1 
HETATM 9536 O  O   . HOH CA 6 .   ? 40.066  -7.766  -13.310 1.00 37.68 ? 577 HOH C O   1 
HETATM 9537 O  O   . HOH CA 6 .   ? 42.079  -4.056  -48.311 1.00 19.94 ? 578 HOH C O   1 
HETATM 9538 O  O   . HOH CA 6 .   ? 28.014  6.610   -43.845 1.00 19.43 ? 579 HOH C O   1 
HETATM 9539 O  O   . HOH CA 6 .   ? 46.455  -0.891  -47.477 1.00 32.16 ? 580 HOH C O   1 
HETATM 9540 O  O   . HOH CA 6 .   ? 24.417  5.481   -21.224 1.00 31.94 ? 581 HOH C O   1 
HETATM 9541 O  O   . HOH CA 6 .   ? 37.488  -20.791 -40.417 1.00 47.83 ? 582 HOH C O   1 
HETATM 9542 O  O   . HOH CA 6 .   ? 40.746  -15.526 -25.080 1.00 21.55 ? 583 HOH C O   1 
HETATM 9543 O  O   . HOH CA 6 .   ? 35.132  20.199  -26.360 1.00 47.35 ? 584 HOH C O   1 
HETATM 9544 O  O   . HOH CA 6 .   ? 62.722  0.594   -19.854 1.00 35.10 ? 585 HOH C O   1 
HETATM 9545 O  O   . HOH CA 6 .   ? 58.111  -7.280  -30.949 1.00 25.27 ? 586 HOH C O   1 
HETATM 9546 O  O   . HOH CA 6 .   ? 23.795  -9.187  -28.871 1.00 27.40 ? 587 HOH C O   1 
HETATM 9547 O  O   . HOH CA 6 .   ? 31.976  -2.298  -51.676 1.00 28.34 ? 588 HOH C O   1 
HETATM 9548 O  O   . HOH CA 6 .   ? 38.438  -18.907 -16.146 1.00 40.55 ? 589 HOH C O   1 
HETATM 9549 O  O   . HOH CA 6 .   ? 27.014  6.827   -21.143 1.00 31.64 ? 590 HOH C O   1 
HETATM 9550 O  O   . HOH CA 6 .   ? 42.358  -14.195 -48.571 1.00 33.22 ? 591 HOH C O   1 
HETATM 9551 O  O   . HOH CA 6 .   ? 48.488  11.292  -24.106 1.00 30.38 ? 592 HOH C O   1 
HETATM 9552 O  O   . HOH CA 6 .   ? 28.610  3.393   -46.265 1.00 20.08 ? 593 HOH C O   1 
HETATM 9553 O  O   . HOH CA 6 .   ? 50.313  -4.579  -15.787 1.00 39.57 ? 594 HOH C O   1 
HETATM 9554 O  O   . HOH CA 6 .   ? 40.641  -16.203 -21.972 1.00 28.71 ? 595 HOH C O   1 
HETATM 9555 O  O   . HOH CA 6 .   ? 44.305  18.280  -43.439 1.00 37.59 ? 596 HOH C O   1 
HETATM 9556 O  O   . HOH CA 6 .   ? 38.452  16.605  -38.815 1.00 22.00 ? 597 HOH C O   1 
HETATM 9557 O  O   . HOH CA 6 .   ? 56.461  7.730   -14.155 1.00 30.38 ? 598 HOH C O   1 
HETATM 9558 O  O   . HOH CA 6 .   ? 54.613  -2.045  -44.881 1.00 33.63 ? 599 HOH C O   1 
HETATM 9559 O  O   . HOH CA 6 .   ? 51.781  12.809  -47.468 1.00 33.04 ? 600 HOH C O   1 
HETATM 9560 O  O   . HOH CA 6 .   ? 38.580  13.842  -43.152 1.00 26.15 ? 601 HOH C O   1 
HETATM 9561 O  O   . HOH CA 6 .   ? 40.430  -14.082 -36.065 1.00 15.97 ? 602 HOH C O   1 
HETATM 9562 O  O   . HOH CA 6 .   ? 51.880  5.602   -12.722 1.00 26.19 ? 603 HOH C O   1 
HETATM 9563 O  O   . HOH CA 6 .   ? 51.360  9.896   -33.253 1.00 26.72 ? 604 HOH C O   1 
HETATM 9564 O  O   . HOH CA 6 .   ? 22.798  2.550   -18.761 1.00 28.17 ? 605 HOH C O   1 
HETATM 9565 O  O   . HOH CA 6 .   ? 58.664  -7.933  -34.324 1.00 29.79 ? 606 HOH C O   1 
HETATM 9566 O  O   . HOH CA 6 .   ? 26.226  3.203   -47.345 1.00 32.68 ? 607 HOH C O   1 
HETATM 9567 O  O   . HOH CA 6 .   ? 55.568  6.754   -29.977 1.00 29.08 ? 608 HOH C O   1 
HETATM 9568 O  O   . HOH CA 6 .   ? 49.508  12.240  -32.618 1.00 24.43 ? 609 HOH C O   1 
HETATM 9569 O  O   . HOH CA 6 .   ? 32.284  7.620   -22.517 1.00 29.93 ? 610 HOH C O   1 
HETATM 9570 O  O   . HOH CA 6 .   ? 46.525  -16.996 -38.081 1.00 25.43 ? 611 HOH C O   1 
HETATM 9571 O  O   . HOH CA 6 .   ? 50.527  -13.675 -19.049 1.00 42.59 ? 612 HOH C O   1 
HETATM 9572 O  O   . HOH CA 6 .   ? 26.457  3.997   -49.903 1.00 40.59 ? 613 HOH C O   1 
HETATM 9573 O  O   . HOH CA 6 .   ? 29.589  -11.707 -26.286 1.00 21.05 ? 614 HOH C O   1 
HETATM 9574 O  O   . HOH CA 6 .   ? 27.490  2.381   -52.174 1.00 31.97 ? 615 HOH C O   1 
HETATM 9575 O  O   . HOH CA 6 .   ? 53.729  7.018   -27.745 1.00 27.24 ? 616 HOH C O   1 
HETATM 9576 O  O   . HOH CA 6 .   ? 53.344  6.044   -23.402 1.00 23.52 ? 617 HOH C O   1 
HETATM 9577 O  O   . HOH CA 6 .   ? 22.831  -4.655  -26.426 1.00 30.85 ? 618 HOH C O   1 
HETATM 9578 O  O   . HOH CA 6 .   ? 20.877  -1.157  -29.780 1.00 20.37 ? 619 HOH C O   1 
HETATM 9579 O  O   . HOH CA 6 .   ? 31.958  10.187  -23.591 1.00 30.56 ? 620 HOH C O   1 
HETATM 9580 O  O   . HOH CA 6 .   ? 54.101  -9.346  -19.164 1.00 39.63 ? 621 HOH C O   1 
HETATM 9581 O  O   . HOH CA 6 .   ? 20.997  -0.108  -21.265 1.00 25.03 ? 622 HOH C O   1 
HETATM 9582 O  O   . HOH CA 6 .   ? 27.599  -12.562 -29.962 1.00 29.55 ? 623 HOH C O   1 
HETATM 9583 O  O   . HOH CA 6 .   ? 29.880  -13.974 -51.859 1.00 40.66 ? 624 HOH C O   1 
HETATM 9584 O  O   . HOH CA 6 .   ? 31.611  -15.213 -18.781 1.00 29.39 ? 625 HOH C O   1 
HETATM 9585 O  O   . HOH CA 6 .   ? 34.271  20.613  -30.541 1.00 46.97 ? 626 HOH C O   1 
HETATM 9586 O  O   . HOH CA 6 .   ? 28.291  -12.889 -40.923 1.00 41.30 ? 627 HOH C O   1 
HETATM 9587 O  O   . HOH CA 6 .   ? 43.295  -16.076 -21.723 1.00 35.15 ? 628 HOH C O   1 
HETATM 9588 O  O   . HOH CA 6 .   ? 53.541  -2.708  -53.357 1.00 31.44 ? 629 HOH C O   1 
HETATM 9589 O  O   . HOH CA 6 .   ? 32.951  4.205   -10.760 1.00 41.94 ? 630 HOH C O   1 
HETATM 9590 O  O   . HOH CA 6 .   ? 56.063  12.056  -42.301 1.00 36.64 ? 631 HOH C O   1 
HETATM 9591 O  O   . HOH CA 6 .   ? 27.336  20.519  -30.415 1.00 32.85 ? 632 HOH C O   1 
HETATM 9592 O  O   . HOH CA 6 .   ? 53.934  5.024   -25.944 1.00 26.63 ? 633 HOH C O   1 
HETATM 9593 O  O   . HOH CA 6 .   ? 42.557  -5.720  -54.173 1.00 23.14 ? 634 HOH C O   1 
HETATM 9594 O  O   . HOH CA 6 .   ? 36.793  15.437  -26.032 1.00 34.56 ? 635 HOH C O   1 
HETATM 9595 O  O   . HOH CA 6 .   ? 51.086  -6.410  -52.970 1.00 37.58 ? 636 HOH C O   1 
HETATM 9596 O  O   . HOH CA 6 .   ? 23.572  3.641   -51.357 1.00 42.68 ? 637 HOH C O   1 
HETATM 9597 O  O   . HOH CA 6 .   ? 35.325  1.257   -50.182 1.00 37.55 ? 638 HOH C O   1 
HETATM 9598 O  O   . HOH CA 6 .   ? 40.070  -1.975  -48.215 1.00 42.56 ? 639 HOH C O   1 
HETATM 9599 O  O   . HOH CA 6 .   ? 29.434  -10.321 -13.403 1.00 35.76 ? 640 HOH C O   1 
HETATM 9600 O  O   . HOH CA 6 .   ? 25.456  -12.780 -25.811 1.00 35.96 ? 641 HOH C O   1 
HETATM 9601 O  O   . HOH CA 6 .   ? 59.751  -5.781  -14.865 1.00 30.86 ? 642 HOH C O   1 
HETATM 9602 O  O   . HOH CA 6 .   ? 56.455  -11.503 -30.007 1.00 32.61 ? 643 HOH C O   1 
HETATM 9603 O  O   . HOH CA 6 .   ? 40.075  12.230  -46.788 1.00 41.46 ? 644 HOH C O   1 
HETATM 9604 O  O   . HOH CA 6 .   ? 31.789  16.850  -43.902 1.00 35.76 ? 645 HOH C O   1 
HETATM 9605 O  O   . HOH CA 6 .   ? 27.882  15.226  -45.625 1.00 33.01 ? 646 HOH C O   1 
HETATM 9606 O  O   . HOH CA 6 .   ? 22.476  8.636   -27.799 1.00 19.16 ? 647 HOH C O   1 
HETATM 9607 O  O   . HOH CA 6 .   ? 48.527  -15.624 -39.763 1.00 32.79 ? 648 HOH C O   1 
HETATM 9608 O  O   . HOH CA 6 .   ? 21.848  -4.098  -38.003 1.00 23.66 ? 649 HOH C O   1 
HETATM 9609 O  O   . HOH CA 6 .   ? 28.344  26.817  -30.421 1.00 21.57 ? 650 HOH C O   1 
HETATM 9610 O  O   . HOH CA 6 .   ? 37.784  16.435  -43.191 1.00 36.73 ? 651 HOH C O   1 
HETATM 9611 O  O   . HOH CA 6 .   ? 61.800  -6.723  -16.724 1.00 29.85 ? 652 HOH C O   1 
HETATM 9612 O  O   . HOH CA 6 .   ? 38.169  -3.069  -48.692 1.00 32.53 ? 653 HOH C O   1 
HETATM 9613 O  O   . HOH CA 6 .   ? 45.042  -16.301 -45.570 1.00 29.31 ? 654 HOH C O   1 
HETATM 9614 O  O   . HOH CA 6 .   ? 21.570  -15.967 -50.093 1.00 30.35 ? 655 HOH C O   1 
HETATM 9615 O  O   . HOH CA 6 .   ? 20.575  4.878   -51.643 1.00 39.49 ? 656 HOH C O   1 
HETATM 9616 O  O   . HOH CA 6 .   ? 41.833  -10.648 -56.357 1.00 22.84 ? 657 HOH C O   1 
HETATM 9617 O  O   . HOH CA 6 .   ? 35.896  13.534  -45.883 1.00 31.79 ? 658 HOH C O   1 
HETATM 9618 O  O   . HOH CA 6 .   ? 30.905  -14.993 -35.464 1.00 30.81 ? 659 HOH C O   1 
HETATM 9619 O  O   . HOH CA 6 .   ? 34.416  23.274  -33.154 1.00 38.86 ? 660 HOH C O   1 
HETATM 9620 O  O   . HOH CA 6 .   ? 35.964  17.840  -38.275 1.00 23.81 ? 661 HOH C O   1 
HETATM 9621 O  O   . HOH CA 6 .   ? 46.973  -12.818 -14.270 1.00 35.04 ? 662 HOH C O   1 
HETATM 9622 O  O   . HOH CA 6 .   ? 50.318  -13.129 -16.172 1.00 39.36 ? 663 HOH C O   1 
HETATM 9623 O  O   . HOH CA 6 .   ? 34.211  9.187   -47.981 1.00 30.84 ? 664 HOH C O   1 
HETATM 9624 O  O   . HOH CA 6 .   ? 19.080  15.945  -21.222 1.00 32.26 ? 665 HOH C O   1 
HETATM 9625 O  O   . HOH CA 6 .   ? 40.290  16.692  -36.829 1.00 27.84 ? 666 HOH C O   1 
HETATM 9626 O  O   . HOH CA 6 .   ? 50.790  15.869  -44.038 1.00 40.27 ? 667 HOH C O   1 
HETATM 9627 O  O   . HOH CA 6 .   ? 40.366  -15.162 -56.241 1.00 24.97 ? 668 HOH C O   1 
HETATM 9628 O  O   . HOH CA 6 .   ? 31.848  14.947  -45.667 1.00 35.53 ? 669 HOH C O   1 
HETATM 9629 O  O   . HOH CA 6 .   ? 48.875  -11.180 -52.556 1.00 22.00 ? 670 HOH C O   1 
HETATM 9630 O  O   . HOH CA 6 .   ? 26.652  6.720   -47.776 1.00 36.03 ? 671 HOH C O   1 
HETATM 9631 O  O   . HOH CA 6 .   ? 35.536  19.476  -40.324 1.00 38.65 ? 672 HOH C O   1 
HETATM 9632 O  O   . HOH CA 6 .   ? 33.978  11.770  -47.729 1.00 26.53 ? 673 HOH C O   1 
HETATM 9633 O  O   . HOH CA 6 .   ? 37.710  18.344  -34.392 1.00 43.06 ? 674 HOH C O   1 
HETATM 9634 O  O   . HOH CA 6 .   ? 51.132  -12.644 -51.520 1.00 32.24 ? 675 HOH C O   1 
HETATM 9635 O  O   . HOH CA 6 .   ? 33.119  7.806   -50.376 1.00 36.51 ? 676 HOH C O   1 
HETATM 9636 O  O   . HOH DA 6 .   ? 17.626  -6.688  -55.968 1.00 27.30 ? 401 HOH D O   1 
HETATM 9637 O  O   . HOH DA 6 .   ? 6.987   12.968  -41.354 1.00 29.29 ? 402 HOH D O   1 
HETATM 9638 O  O   . HOH DA 6 .   ? 4.199   -14.882 -16.878 1.00 41.32 ? 403 HOH D O   1 
HETATM 9639 O  O   . HOH DA 6 .   ? 15.082  18.040  -54.585 1.00 41.11 ? 404 HOH D O   1 
HETATM 9640 O  O   . HOH DA 6 .   ? -7.799  3.512   -21.190 1.00 24.58 ? 405 HOH D O   1 
HETATM 9641 O  O   . HOH DA 6 .   ? 14.207  19.769  -42.671 1.00 31.76 ? 406 HOH D O   1 
HETATM 9642 O  O   . HOH DA 6 .   ? -12.842 -1.808  -33.944 1.00 15.94 ? 407 HOH D O   1 
HETATM 9643 O  O   . HOH DA 6 .   ? 5.925   16.305  -45.837 1.00 39.31 ? 408 HOH D O   1 
HETATM 9644 O  O   . HOH DA 6 .   ? -14.604 4.724   -37.022 1.00 21.49 ? 409 HOH D O   1 
HETATM 9645 O  O   . HOH DA 6 .   ? -0.148  -0.148  -17.919 1.00 35.31 ? 410 HOH D O   1 
HETATM 9646 O  O   . HOH DA 6 .   ? 10.973  -0.553  -14.008 1.00 29.09 ? 411 HOH D O   1 
HETATM 9647 O  O   . HOH DA 6 .   ? 14.223  -8.388  -52.572 1.00 27.20 ? 412 HOH D O   1 
HETATM 9648 O  O   . HOH DA 6 .   ? 14.441  -11.942 -34.395 1.00 29.19 ? 413 HOH D O   1 
HETATM 9649 O  O   . HOH DA 6 .   ? 4.221   -0.814  -14.745 1.00 31.19 ? 414 HOH D O   1 
HETATM 9650 O  O   . HOH DA 6 .   ? -1.923  13.256  -38.679 1.00 33.81 ? 415 HOH D O   1 
HETATM 9651 O  O   . HOH DA 6 .   ? 12.581  19.761  -29.307 1.00 23.72 ? 416 HOH D O   1 
HETATM 9652 O  O   . HOH DA 6 .   ? 22.856  13.696  -28.683 1.00 22.73 ? 417 HOH D O   1 
HETATM 9653 O  O   . HOH DA 6 .   ? 11.191  15.533  -50.735 1.00 24.32 ? 418 HOH D O   1 
HETATM 9654 O  O   . HOH DA 6 .   ? -14.196 3.188   -26.079 1.00 34.78 ? 419 HOH D O   1 
HETATM 9655 O  O   . HOH DA 6 .   ? -6.048  13.595  -37.302 1.00 31.49 ? 420 HOH D O   1 
HETATM 9656 O  O   . HOH DA 6 .   ? 21.823  -9.535  -18.893 1.00 32.74 ? 421 HOH D O   1 
HETATM 9657 O  O   . HOH DA 6 .   ? -5.789  19.431  -21.875 1.00 30.77 ? 422 HOH D O   1 
HETATM 9658 O  O   . HOH DA 6 .   ? -0.196  -10.387 -18.029 1.00 29.49 ? 423 HOH D O   1 
HETATM 9659 O  O   . HOH DA 6 .   ? -10.043 15.105  -30.667 1.00 28.47 ? 424 HOH D O   1 
HETATM 9660 O  O   . HOH DA 6 .   ? -10.555 11.655  -25.959 1.00 17.36 ? 425 HOH D O   1 
HETATM 9661 O  O   . HOH DA 6 .   ? 7.476   13.419  -38.314 1.00 18.94 ? 426 HOH D O   1 
HETATM 9662 O  O   . HOH DA 6 .   ? -18.891 5.517   -40.610 1.00 29.58 ? 427 HOH D O   1 
HETATM 9663 O  O   . HOH DA 6 .   ? 12.175  6.977   -39.335 1.00 8.23  ? 428 HOH D O   1 
HETATM 9664 O  O   . HOH DA 6 .   ? 11.842  -7.025  -52.095 1.00 22.18 ? 429 HOH D O   1 
HETATM 9665 O  O   . HOH DA 6 .   ? 21.448  -10.966 -39.077 1.00 31.85 ? 430 HOH D O   1 
HETATM 9666 O  O   . HOH DA 6 .   ? -5.626  -9.822  -34.506 1.00 25.23 ? 431 HOH D O   1 
HETATM 9667 O  O   . HOH DA 6 .   ? 10.935  17.632  -54.686 1.00 20.04 ? 432 HOH D O   1 
HETATM 9668 O  O   . HOH DA 6 .   ? 14.562  -13.403 -30.571 1.00 34.65 ? 433 HOH D O   1 
HETATM 9669 O  O   . HOH DA 6 .   ? 20.452  -7.621  -29.665 1.00 19.84 ? 434 HOH D O   1 
HETATM 9670 O  O   . HOH DA 6 .   ? -3.936  23.718  -31.091 1.00 34.84 ? 435 HOH D O   1 
HETATM 9671 O  O   . HOH DA 6 .   ? 2.058   -15.349 -29.612 1.00 24.78 ? 436 HOH D O   1 
HETATM 9672 O  O   . HOH DA 6 .   ? -6.186  5.191   -56.231 1.00 23.06 ? 437 HOH D O   1 
HETATM 9673 O  O   . HOH DA 6 .   ? -1.892  -9.086  -16.474 1.00 22.32 ? 438 HOH D O   1 
HETATM 9674 O  O   . HOH DA 6 .   ? -15.397 -2.344  -43.520 1.00 20.91 ? 439 HOH D O   1 
HETATM 9675 O  O   . HOH DA 6 .   ? 0.758   -12.013 -13.830 1.00 33.06 ? 440 HOH D O   1 
HETATM 9676 O  O   . HOH DA 6 .   ? -6.263  4.254   -24.399 1.00 21.73 ? 441 HOH D O   1 
HETATM 9677 O  O   . HOH DA 6 .   ? -2.956  -10.554 -39.316 1.00 21.75 ? 442 HOH D O   1 
HETATM 9678 O  O   . HOH DA 6 .   ? 19.926  7.953   -42.452 1.00 10.52 ? 443 HOH D O   1 
HETATM 9679 O  O   . HOH DA 6 .   ? -10.064 15.254  -20.860 1.00 20.32 ? 444 HOH D O   1 
HETATM 9680 O  O   . HOH DA 6 .   ? 19.332  -3.981  -34.197 1.00 25.61 ? 445 HOH D O   1 
HETATM 9681 O  O   . HOH DA 6 .   ? 17.938  7.322   -27.070 1.00 14.87 ? 446 HOH D O   1 
HETATM 9682 O  O   . HOH DA 6 .   ? -14.396 7.775   -25.673 1.00 31.64 ? 447 HOH D O   1 
HETATM 9683 O  O   . HOH DA 6 .   ? 4.344   13.017  -18.252 1.00 35.99 ? 448 HOH D O   1 
HETATM 9684 O  O   . HOH DA 6 .   ? -5.818  -10.315 -44.945 1.00 29.15 ? 449 HOH D O   1 
HETATM 9685 O  O   . HOH DA 6 .   ? 16.381  0.189   -37.419 1.00 8.76  ? 450 HOH D O   1 
HETATM 9686 O  O   . HOH DA 6 .   ? -2.137  11.034  -58.564 1.00 30.94 ? 451 HOH D O   1 
HETATM 9687 O  O   . HOH DA 6 .   ? 8.285   -16.372 -44.987 1.00 22.31 ? 452 HOH D O   1 
HETATM 9688 O  O   . HOH DA 6 .   ? 15.929  1.928   -59.501 1.00 36.37 ? 453 HOH D O   1 
HETATM 9689 O  O   . HOH DA 6 .   ? 1.007   9.030   -59.287 1.00 23.75 ? 454 HOH D O   1 
HETATM 9690 O  O   . HOH DA 6 .   ? 11.471  -11.015 -27.476 1.00 33.45 ? 455 HOH D O   1 
HETATM 9691 O  O   . HOH DA 6 .   ? 18.486  5.102   -45.739 1.00 17.66 ? 456 HOH D O   1 
HETATM 9692 O  O   . HOH DA 6 .   ? 8.635   -10.688 -31.141 1.00 15.93 ? 457 HOH D O   1 
HETATM 9693 O  O   . HOH DA 6 .   ? 10.616  13.178  -58.606 1.00 18.75 ? 458 HOH D O   1 
HETATM 9694 O  O   . HOH DA 6 .   ? -12.652 -7.810  -41.032 1.00 20.02 ? 459 HOH D O   1 
HETATM 9695 O  O   . HOH DA 6 .   ? 8.953   3.210   -52.959 1.00 11.90 ? 460 HOH D O   1 
HETATM 9696 O  O   . HOH DA 6 .   ? -7.208  -3.194  -53.337 1.00 29.71 ? 461 HOH D O   1 
HETATM 9697 O  O   . HOH DA 6 .   ? -10.243 5.248   -55.065 1.00 34.20 ? 462 HOH D O   1 
HETATM 9698 O  O   . HOH DA 6 .   ? 18.968  11.623  -50.207 1.00 18.33 ? 463 HOH D O   1 
HETATM 9699 O  O   . HOH DA 6 .   ? 0.877   12.779  -38.815 1.00 28.98 ? 464 HOH D O   1 
HETATM 9700 O  O   . HOH DA 6 .   ? -12.297 -4.911  -44.374 1.00 20.16 ? 465 HOH D O   1 
HETATM 9701 O  O   . HOH DA 6 .   ? -11.623 11.238  -46.087 1.00 31.59 ? 466 HOH D O   1 
HETATM 9702 O  O   . HOH DA 6 .   ? -5.793  -5.631  -53.750 1.00 28.82 ? 467 HOH D O   1 
HETATM 9703 O  O   . HOH DA 6 .   ? 4.523   15.934  -57.142 1.00 21.20 ? 468 HOH D O   1 
HETATM 9704 O  O   . HOH DA 6 .   ? 1.521   7.652   -22.613 1.00 33.25 ? 469 HOH D O   1 
HETATM 9705 O  O   . HOH DA 6 .   ? 20.070  21.601  -32.861 1.00 26.99 ? 470 HOH D O   1 
HETATM 9706 O  O   . HOH DA 6 .   ? -9.446  5.469   -22.020 1.00 38.86 ? 471 HOH D O   1 
HETATM 9707 O  O   . HOH DA 6 .   ? 19.489  18.640  -40.256 1.00 22.98 ? 472 HOH D O   1 
HETATM 9708 O  O   . HOH DA 6 .   ? -2.927  11.092  -46.037 1.00 17.94 ? 473 HOH D O   1 
HETATM 9709 O  O   . HOH DA 6 .   ? -3.137  -14.757 -49.307 1.00 29.57 ? 474 HOH D O   1 
HETATM 9710 O  O   . HOH DA 6 .   ? -6.841  10.987  -19.584 1.00 13.03 ? 475 HOH D O   1 
HETATM 9711 O  O   . HOH DA 6 .   ? -6.332  -2.521  -21.179 1.00 24.21 ? 476 HOH D O   1 
HETATM 9712 O  O   . HOH DA 6 .   ? 1.196   -17.383 -26.903 1.00 39.40 ? 477 HOH D O   1 
HETATM 9713 O  O   . HOH DA 6 .   ? 20.439  14.028  -47.790 1.00 16.47 ? 478 HOH D O   1 
HETATM 9714 O  O   . HOH DA 6 .   ? 0.941   2.510   -27.998 1.00 9.22  ? 479 HOH D O   1 
HETATM 9715 O  O   . HOH DA 6 .   ? 8.690   -14.612 -37.376 1.00 26.46 ? 480 HOH D O   1 
HETATM 9716 O  O   . HOH DA 6 .   ? 20.130  7.314   -35.749 1.00 10.76 ? 481 HOH D O   1 
HETATM 9717 O  O   . HOH DA 6 .   ? 18.401  -0.249  -29.405 1.00 14.10 ? 482 HOH D O   1 
HETATM 9718 O  O   . HOH DA 6 .   ? 6.305   17.985  -32.993 1.00 21.58 ? 483 HOH D O   1 
HETATM 9719 O  O   . HOH DA 6 .   ? 6.609   -13.934 -50.783 1.00 9.52  ? 484 HOH D O   1 
HETATM 9720 O  O   . HOH DA 6 .   ? 20.173  -6.953  -44.394 1.00 27.06 ? 485 HOH D O   1 
HETATM 9721 O  O   . HOH DA 6 .   ? 5.915   -14.681 -33.687 1.00 39.30 ? 486 HOH D O   1 
HETATM 9722 O  O   . HOH DA 6 .   ? 9.313   8.211   -42.918 1.00 11.37 ? 487 HOH D O   1 
HETATM 9723 O  O   . HOH DA 6 .   ? 19.239  8.391   -29.189 1.00 14.02 ? 488 HOH D O   1 
HETATM 9724 O  O   . HOH DA 6 .   ? 11.800  -3.659  -47.209 1.00 9.95  ? 489 HOH D O   1 
HETATM 9725 O  O   . HOH DA 6 .   ? -8.072  11.833  -36.853 1.00 17.80 ? 490 HOH D O   1 
HETATM 9726 O  O   . HOH DA 6 .   ? 10.274  2.256   -21.351 1.00 15.37 ? 491 HOH D O   1 
HETATM 9727 O  O   . HOH DA 6 .   ? 19.727  11.100  -29.189 1.00 13.78 ? 492 HOH D O   1 
HETATM 9728 O  O   . HOH DA 6 .   ? 16.546  8.083   -51.493 1.00 18.56 ? 493 HOH D O   1 
HETATM 9729 O  O   . HOH DA 6 .   ? 0.362   -12.669 -36.841 1.00 14.74 ? 494 HOH D O   1 
HETATM 9730 O  O   . HOH DA 6 .   ? 16.270  0.949   -55.423 1.00 31.81 ? 495 HOH D O   1 
HETATM 9731 O  O   . HOH DA 6 .   ? -2.546  -8.809  -41.656 1.00 15.63 ? 496 HOH D O   1 
HETATM 9732 O  O   . HOH DA 6 .   ? -5.754  -6.974  -27.717 1.00 18.85 ? 497 HOH D O   1 
HETATM 9733 O  O   . HOH DA 6 .   ? -8.412  -10.675 -41.672 1.00 38.14 ? 498 HOH D O   1 
HETATM 9734 O  O   . HOH DA 6 .   ? -3.561  -5.696  -26.696 1.00 17.02 ? 499 HOH D O   1 
HETATM 9735 O  O   . HOH DA 6 .   ? -12.383 -3.826  -36.006 1.00 18.97 ? 500 HOH D O   1 
HETATM 9736 O  O   . HOH DA 6 .   ? 18.561  -0.224  -20.244 1.00 23.11 ? 501 HOH D O   1 
HETATM 9737 O  O   . HOH DA 6 .   ? 19.090  4.744   -49.233 1.00 17.77 ? 502 HOH D O   1 
HETATM 9738 O  O   . HOH DA 6 .   ? 21.327  5.097   -34.204 1.00 8.48  ? 503 HOH D O   1 
HETATM 9739 O  O   . HOH DA 6 .   ? 4.299   -6.953  -34.741 1.00 9.39  ? 504 HOH D O   1 
HETATM 9740 O  O   . HOH DA 6 .   ? -0.032  -12.202 -22.780 1.00 34.72 ? 505 HOH D O   1 
HETATM 9741 O  O   . HOH DA 6 .   ? -9.202  -4.939  -22.576 1.00 37.50 ? 506 HOH D O   1 
HETATM 9742 O  O   . HOH DA 6 .   ? -2.267  11.514  -20.204 1.00 20.83 ? 507 HOH D O   1 
HETATM 9743 O  O   . HOH DA 6 .   ? 5.775   -6.456  -57.436 1.00 16.21 ? 508 HOH D O   1 
HETATM 9744 O  O   . HOH DA 6 .   ? 20.126  -1.174  -39.857 1.00 26.16 ? 509 HOH D O   1 
HETATM 9745 O  O   . HOH DA 6 .   ? 13.224  15.725  -47.881 1.00 23.34 ? 510 HOH D O   1 
HETATM 9746 O  O   . HOH DA 6 .   ? -7.255  -6.977  -51.471 1.00 18.77 ? 511 HOH D O   1 
HETATM 9747 O  O   . HOH DA 6 .   ? -2.722  15.138  -47.630 1.00 40.12 ? 512 HOH D O   1 
HETATM 9748 O  O   . HOH DA 6 .   ? 22.828  6.250   -38.241 1.00 9.35  ? 513 HOH D O   1 
HETATM 9749 O  O   . HOH DA 6 .   ? 13.377  18.400  -32.460 1.00 10.34 ? 514 HOH D O   1 
HETATM 9750 O  O   . HOH DA 6 .   ? 23.783  18.329  -42.759 1.00 16.71 ? 515 HOH D O   1 
HETATM 9751 O  O   . HOH DA 6 .   ? -2.255  -7.890  -22.430 1.00 16.36 ? 516 HOH D O   1 
HETATM 9752 O  O   . HOH DA 6 .   ? -2.116  -4.278  -55.764 1.00 34.36 ? 517 HOH D O   1 
HETATM 9753 O  O   . HOH DA 6 .   ? 3.111   -13.721 -39.419 1.00 25.48 ? 518 HOH D O   1 
HETATM 9754 O  O   . HOH DA 6 .   ? 5.448   12.182  -22.951 1.00 21.21 ? 519 HOH D O   1 
HETATM 9755 O  O   . HOH DA 6 .   ? -8.244  13.398  -44.287 1.00 26.50 ? 520 HOH D O   1 
HETATM 9756 O  O   . HOH DA 6 .   ? -12.432 5.552   -53.070 1.00 31.02 ? 521 HOH D O   1 
HETATM 9757 O  O   . HOH DA 6 .   ? 13.142  22.320  -35.069 1.00 32.14 ? 522 HOH D O   1 
HETATM 9758 O  O   . HOH DA 6 .   ? -10.592 -4.702  -29.613 1.00 26.89 ? 523 HOH D O   1 
HETATM 9759 O  O   . HOH DA 6 .   ? -0.655  19.139  -21.493 1.00 30.27 ? 524 HOH D O   1 
HETATM 9760 O  O   . HOH DA 6 .   ? 17.370  -11.494 -27.251 1.00 23.15 ? 525 HOH D O   1 
HETATM 9761 O  O   . HOH DA 6 .   ? -10.107 -0.478  -49.359 1.00 15.30 ? 526 HOH D O   1 
HETATM 9762 O  O   . HOH DA 6 .   ? 16.445  10.560  -50.307 1.00 15.34 ? 527 HOH D O   1 
HETATM 9763 O  O   . HOH DA 6 .   ? 0.752   -5.205  -54.456 1.00 23.72 ? 528 HOH D O   1 
HETATM 9764 O  O   . HOH DA 6 .   ? -12.961 8.464   -55.141 1.00 22.79 ? 529 HOH D O   1 
HETATM 9765 O  O   . HOH DA 6 .   ? -13.946 -1.376  -49.098 1.00 22.48 ? 530 HOH D O   1 
HETATM 9766 O  O   . HOH DA 6 .   ? -9.814  16.057  -28.328 1.00 26.68 ? 531 HOH D O   1 
HETATM 9767 O  O   . HOH DA 6 .   ? 10.934  13.709  -61.208 1.00 22.52 ? 532 HOH D O   1 
HETATM 9768 O  O   . HOH DA 6 .   ? 13.671  7.413   -48.349 1.00 12.10 ? 533 HOH D O   1 
HETATM 9769 O  O   . HOH DA 6 .   ? 18.655  -0.795  -46.268 1.00 27.11 ? 534 HOH D O   1 
HETATM 9770 O  O   . HOH DA 6 .   ? -8.522  -0.274  -51.629 1.00 14.49 ? 535 HOH D O   1 
HETATM 9771 O  O   . HOH DA 6 .   ? 20.303  15.927  -49.386 1.00 35.56 ? 536 HOH D O   1 
HETATM 9772 O  O   . HOH DA 6 .   ? 12.593  -9.791  -46.038 1.00 14.65 ? 537 HOH D O   1 
HETATM 9773 O  O   . HOH DA 6 .   ? 8.261   -9.305  -13.835 1.00 30.14 ? 538 HOH D O   1 
HETATM 9774 O  O   . HOH DA 6 .   ? 8.952   -10.101 -57.916 1.00 19.83 ? 539 HOH D O   1 
HETATM 9775 O  O   . HOH DA 6 .   ? 0.658   -8.242  -18.792 1.00 17.75 ? 540 HOH D O   1 
HETATM 9776 O  O   . HOH DA 6 .   ? 11.469  21.911  -61.673 1.00 31.74 ? 541 HOH D O   1 
HETATM 9777 O  O   . HOH DA 6 .   ? 21.647  -9.675  -25.935 1.00 28.10 ? 542 HOH D O   1 
HETATM 9778 O  O   . HOH DA 6 .   ? -3.042  21.951  -35.271 1.00 20.32 ? 543 HOH D O   1 
HETATM 9779 O  O   . HOH DA 6 .   ? 18.736  -3.510  -43.073 1.00 19.56 ? 544 HOH D O   1 
HETATM 9780 O  O   . HOH DA 6 .   ? 14.124  17.533  -52.262 1.00 30.51 ? 545 HOH D O   1 
HETATM 9781 O  O   . HOH DA 6 .   ? 11.175  3.662   -55.100 1.00 13.71 ? 546 HOH D O   1 
HETATM 9782 O  O   . HOH DA 6 .   ? -9.911  8.265   -20.627 1.00 20.72 ? 547 HOH D O   1 
HETATM 9783 O  O   . HOH DA 6 .   ? -2.289  13.142  -41.433 1.00 29.27 ? 548 HOH D O   1 
HETATM 9784 O  O   . HOH DA 6 .   ? -12.303 -4.803  -31.945 1.00 34.96 ? 549 HOH D O   1 
HETATM 9785 O  O   . HOH DA 6 .   ? 14.485  13.793  -27.237 1.00 13.19 ? 550 HOH D O   1 
HETATM 9786 O  O   . HOH DA 6 .   ? 17.082  7.461   -55.749 1.00 19.97 ? 551 HOH D O   1 
HETATM 9787 O  O   . HOH DA 6 .   ? 12.187  1.800   -17.907 1.00 17.43 ? 552 HOH D O   1 
HETATM 9788 O  O   . HOH DA 6 .   ? 5.886   21.293  -25.581 1.00 18.86 ? 553 HOH D O   1 
HETATM 9789 O  O   . HOH DA 6 .   ? -2.427  -14.407 -25.871 1.00 34.13 ? 554 HOH D O   1 
HETATM 9790 O  O   . HOH DA 6 .   ? 18.785  -13.208 -32.922 1.00 29.81 ? 555 HOH D O   1 
HETATM 9791 O  O   . HOH DA 6 .   ? 23.897  8.453   -45.689 1.00 29.77 ? 556 HOH D O   1 
HETATM 9792 O  O   . HOH DA 6 .   ? -9.298  -8.777  -37.796 1.00 40.85 ? 557 HOH D O   1 
HETATM 9793 O  O   . HOH DA 6 .   ? -13.429 12.414  -32.270 1.00 35.32 ? 558 HOH D O   1 
HETATM 9794 O  O   . HOH DA 6 .   ? -5.338  -13.775 -32.456 1.00 24.08 ? 559 HOH D O   1 
HETATM 9795 O  O   . HOH DA 6 .   ? -8.258  8.431   -55.740 1.00 28.04 ? 560 HOH D O   1 
HETATM 9796 O  O   . HOH DA 6 .   ? 14.249  2.456   -16.321 1.00 24.64 ? 561 HOH D O   1 
HETATM 9797 O  O   . HOH DA 6 .   ? 19.042  -0.375  -36.674 1.00 13.79 ? 562 HOH D O   1 
HETATM 9798 O  O   . HOH DA 6 .   ? 20.840  9.490   -25.907 1.00 25.29 ? 563 HOH D O   1 
HETATM 9799 O  O   . HOH DA 6 .   ? 7.955   9.068   -24.204 1.00 19.32 ? 564 HOH D O   1 
HETATM 9800 O  O   . HOH DA 6 .   ? 11.677  8.781   -47.204 1.00 12.58 ? 565 HOH D O   1 
HETATM 9801 O  O   . HOH DA 6 .   ? -6.685  -7.763  -32.791 1.00 33.06 ? 566 HOH D O   1 
HETATM 9802 O  O   . HOH DA 6 .   ? 16.239  14.999  -23.958 1.00 25.04 ? 567 HOH D O   1 
HETATM 9803 O  O   . HOH DA 6 .   ? 21.302  6.681   -29.644 1.00 11.94 ? 568 HOH D O   1 
HETATM 9804 O  O   . HOH DA 6 .   ? -15.560 4.373   -31.904 1.00 33.18 ? 569 HOH D O   1 
HETATM 9805 O  O   . HOH DA 6 .   ? 22.882  6.483   -23.722 1.00 24.06 ? 570 HOH D O   1 
HETATM 9806 O  O   . HOH DA 6 .   ? 17.072  6.673   -48.972 1.00 17.54 ? 571 HOH D O   1 
HETATM 9807 O  O   . HOH DA 6 .   ? -8.865  -6.536  -28.300 1.00 33.70 ? 572 HOH D O   1 
HETATM 9808 O  O   . HOH DA 6 .   ? 2.600   9.367   -24.758 1.00 16.12 ? 573 HOH D O   1 
HETATM 9809 O  O   . HOH DA 6 .   ? -0.004  0.120   -56.800 1.00 24.15 ? 574 HOH D O   1 
HETATM 9810 O  O   . HOH DA 6 .   ? 19.036  9.951   -35.762 1.00 9.11  ? 575 HOH D O   1 
HETATM 9811 O  O   . HOH DA 6 .   ? 18.407  -4.538  -18.114 1.00 27.64 ? 576 HOH D O   1 
HETATM 9812 O  O   . HOH DA 6 .   ? 9.534   -13.480 -55.451 1.00 39.26 ? 577 HOH D O   1 
HETATM 9813 O  O   . HOH DA 6 .   ? -12.275 -9.276  -44.607 1.00 32.79 ? 578 HOH D O   1 
HETATM 9814 O  O   . HOH DA 6 .   ? 21.948  1.397   -25.060 1.00 21.04 ? 579 HOH D O   1 
HETATM 9815 O  O   . HOH DA 6 .   ? -16.375 4.302   -41.011 1.00 21.30 ? 580 HOH D O   1 
HETATM 9816 O  O   . HOH DA 6 .   ? 16.420  19.581  -56.897 1.00 28.93 ? 581 HOH D O   1 
HETATM 9817 O  O   . HOH DA 6 .   ? 12.886  11.151  -46.650 1.00 15.95 ? 582 HOH D O   1 
HETATM 9818 O  O   . HOH DA 6 .   ? 5.927   -0.306  -57.762 1.00 26.92 ? 583 HOH D O   1 
HETATM 9819 O  O   . HOH DA 6 .   ? -1.368  2.706   -19.224 1.00 39.12 ? 584 HOH D O   1 
HETATM 9820 O  O   . HOH DA 6 .   ? 16.802  18.743  -43.481 1.00 33.07 ? 585 HOH D O   1 
HETATM 9821 O  O   . HOH DA 6 .   ? 1.146   -9.931  -31.130 1.00 11.70 ? 586 HOH D O   1 
HETATM 9822 O  O   . HOH DA 6 .   ? 13.934  -11.350 -20.801 1.00 40.85 ? 587 HOH D O   1 
HETATM 9823 O  O   . HOH DA 6 .   ? 21.162  2.369   -21.048 1.00 23.03 ? 588 HOH D O   1 
HETATM 9824 O  O   . HOH DA 6 .   ? 10.536  -10.600 -16.815 1.00 23.19 ? 589 HOH D O   1 
HETATM 9825 O  O   . HOH DA 6 .   ? 0.618   15.530  -59.584 1.00 28.82 ? 590 HOH D O   1 
HETATM 9826 O  O   . HOH DA 6 .   ? 15.018  6.089   -18.747 1.00 35.45 ? 591 HOH D O   1 
HETATM 9827 O  O   . HOH DA 6 .   ? 15.360  9.720   -47.910 1.00 14.86 ? 592 HOH D O   1 
HETATM 9828 O  O   . HOH DA 6 .   ? 22.071  3.716   -23.348 1.00 21.00 ? 593 HOH D O   1 
HETATM 9829 O  O   . HOH DA 6 .   ? 16.326  15.918  -54.623 1.00 23.85 ? 594 HOH D O   1 
HETATM 9830 O  O   . HOH DA 6 .   ? -6.984  0.231   -55.946 1.00 26.03 ? 595 HOH D O   1 
HETATM 9831 O  O   . HOH DA 6 .   ? 7.513   -4.952  -14.420 1.00 24.87 ? 596 HOH D O   1 
HETATM 9832 O  O   . HOH DA 6 .   ? 8.706   21.607  -29.774 1.00 16.87 ? 597 HOH D O   1 
HETATM 9833 O  O   . HOH DA 6 .   ? 18.323  22.928  -34.213 1.00 22.83 ? 598 HOH D O   1 
HETATM 9834 O  O   . HOH DA 6 .   ? 18.579  -7.653  -40.132 1.00 17.15 ? 599 HOH D O   1 
HETATM 9835 O  O   . HOH DA 6 .   ? 5.209   -18.498 -20.938 1.00 52.43 ? 600 HOH D O   1 
HETATM 9836 O  O   . HOH DA 6 .   ? -12.335 9.977   -23.269 1.00 22.70 ? 601 HOH D O   1 
HETATM 9837 O  O   . HOH DA 6 .   ? 13.502  1.083   -55.674 1.00 19.84 ? 602 HOH D O   1 
HETATM 9838 O  O   . HOH DA 6 .   ? -2.574  -0.566  -16.661 1.00 24.80 ? 603 HOH D O   1 
HETATM 9839 O  O   . HOH DA 6 .   ? -4.964  -11.362 -28.117 1.00 21.44 ? 604 HOH D O   1 
HETATM 9840 O  O   . HOH DA 6 .   ? -0.143  -12.193 -42.093 1.00 16.29 ? 605 HOH D O   1 
HETATM 9841 O  O   . HOH DA 6 .   ? -12.687 -4.438  -47.518 1.00 24.60 ? 606 HOH D O   1 
HETATM 9842 O  O   . HOH DA 6 .   ? 3.919   18.608  -51.244 1.00 27.27 ? 607 HOH D O   1 
HETATM 9843 O  O   . HOH DA 6 .   ? 1.242   -15.144 -35.733 1.00 31.02 ? 608 HOH D O   1 
HETATM 9844 O  O   . HOH DA 6 .   ? 2.707   21.360  -31.875 1.00 32.88 ? 609 HOH D O   1 
HETATM 9845 O  O   . HOH DA 6 .   ? 13.900  16.250  -26.343 1.00 19.55 ? 610 HOH D O   1 
HETATM 9846 O  O   . HOH DA 6 .   ? -15.193 -0.642  -35.574 1.00 20.41 ? 611 HOH D O   1 
HETATM 9847 O  O   . HOH DA 6 .   ? 9.180   20.042  -31.909 1.00 16.79 ? 612 HOH D O   1 
HETATM 9848 O  O   . HOH DA 6 .   ? -20.115 -0.573  -44.975 1.00 39.49 ? 613 HOH D O   1 
HETATM 9849 O  O   . HOH DA 6 .   ? -14.413 9.501   -44.623 1.00 30.07 ? 614 HOH D O   1 
HETATM 9850 O  O   . HOH DA 6 .   ? 2.619   -0.775  -57.192 1.00 31.89 ? 615 HOH D O   1 
HETATM 9851 O  O   . HOH DA 6 .   ? 0.595   24.089  -30.089 1.00 31.91 ? 616 HOH D O   1 
HETATM 9852 O  O   . HOH DA 6 .   ? 23.499  10.442  -41.629 1.00 13.91 ? 617 HOH D O   1 
HETATM 9853 O  O   . HOH DA 6 .   ? -9.624  0.544   -54.521 1.00 24.60 ? 618 HOH D O   1 
HETATM 9854 O  O   . HOH DA 6 .   ? -15.930 9.560   -47.251 1.00 23.63 ? 619 HOH D O   1 
HETATM 9855 O  O   . HOH DA 6 .   ? -9.336  10.979  -44.922 1.00 16.67 ? 620 HOH D O   1 
HETATM 9856 O  O   . HOH DA 6 .   ? 11.188  -10.588 -43.505 1.00 16.76 ? 621 HOH D O   1 
HETATM 9857 O  O   . HOH DA 6 .   ? -14.327 10.484  -36.809 1.00 28.18 ? 622 HOH D O   1 
HETATM 9858 O  O   . HOH DA 6 .   ? -2.722  13.730  -56.603 1.00 24.09 ? 623 HOH D O   1 
HETATM 9859 O  O   . HOH DA 6 .   ? 8.667   17.685  -27.361 1.00 19.97 ? 624 HOH D O   1 
HETATM 9860 O  O   . HOH DA 6 .   ? 2.063   11.171  -61.745 1.00 35.53 ? 625 HOH D O   1 
HETATM 9861 O  O   . HOH DA 6 .   ? -3.988  9.935   -17.347 1.00 18.35 ? 626 HOH D O   1 
HETATM 9862 O  O   . HOH DA 6 .   ? -17.314 -4.145  -36.399 1.00 29.86 ? 627 HOH D O   1 
HETATM 9863 O  O   . HOH DA 6 .   ? 12.707  13.248  -48.520 1.00 20.07 ? 628 HOH D O   1 
HETATM 9864 O  O   . HOH DA 6 .   ? -5.640  -11.211 -30.938 1.00 26.23 ? 629 HOH D O   1 
HETATM 9865 O  O   . HOH DA 6 .   ? -0.356  -12.855 -45.272 1.00 16.36 ? 630 HOH D O   1 
HETATM 9866 O  O   . HOH DA 6 .   ? 18.145  16.932  -41.843 1.00 28.13 ? 631 HOH D O   1 
HETATM 9867 O  O   . HOH DA 6 .   ? -17.393 8.161   -50.208 1.00 31.38 ? 632 HOH D O   1 
HETATM 9868 O  O   . HOH DA 6 .   ? 2.471   1.728   -20.210 1.00 25.73 ? 633 HOH D O   1 
HETATM 9869 O  O   . HOH DA 6 .   ? 18.869  17.840  -27.316 1.00 37.24 ? 634 HOH D O   1 
HETATM 9870 O  O   . HOH DA 6 .   ? 16.188  24.059  -34.265 1.00 26.46 ? 635 HOH D O   1 
HETATM 9871 O  O   . HOH DA 6 .   ? 4.154   24.048  -28.597 1.00 25.43 ? 636 HOH D O   1 
HETATM 9872 O  O   . HOH DA 6 .   ? -11.772 12.721  -38.176 1.00 27.27 ? 637 HOH D O   1 
HETATM 9873 O  O   . HOH DA 6 .   ? -8.862  16.489  -34.364 1.00 35.83 ? 638 HOH D O   1 
HETATM 9874 O  O   . HOH DA 6 .   ? -11.626 -7.450  -36.393 1.00 27.90 ? 639 HOH D O   1 
HETATM 9875 O  O   . HOH DA 6 .   ? 5.404   18.610  -59.138 1.00 30.17 ? 640 HOH D O   1 
HETATM 9876 O  O   . HOH DA 6 .   ? -10.795 19.405  -30.929 1.00 28.44 ? 641 HOH D O   1 
HETATM 9877 O  O   . HOH DA 6 .   ? -11.545 12.202  -30.465 1.00 32.37 ? 642 HOH D O   1 
HETATM 9878 O  O   . HOH DA 6 .   ? 22.516  -1.696  -39.835 1.00 22.52 ? 643 HOH D O   1 
HETATM 9879 O  O   . HOH DA 6 .   ? 5.162   9.366   -23.603 1.00 22.24 ? 644 HOH D O   1 
HETATM 9880 O  O   . HOH DA 6 .   ? -18.062 -1.922  -44.599 1.00 33.93 ? 645 HOH D O   1 
HETATM 9881 O  O   . HOH DA 6 .   ? 20.736  -4.039  -28.450 1.00 24.81 ? 646 HOH D O   1 
HETATM 9882 O  O   . HOH DA 6 .   ? 26.381  15.965  -43.568 1.00 26.88 ? 647 HOH D O   1 
HETATM 9883 O  O   . HOH DA 6 .   ? -16.210 3.256   -38.428 1.00 29.98 ? 648 HOH D O   1 
HETATM 9884 O  O   . HOH DA 6 .   ? 9.095   17.063  -40.031 1.00 41.78 ? 649 HOH D O   1 
HETATM 9885 O  O   . HOH DA 6 .   ? 8.752   -13.590 -29.809 1.00 31.00 ? 650 HOH D O   1 
HETATM 9886 O  O   . HOH DA 6 .   ? -16.519 4.192   -51.527 1.00 42.15 ? 651 HOH D O   1 
HETATM 9887 O  O   . HOH DA 6 .   ? -2.762  -14.620 -39.525 1.00 26.18 ? 652 HOH D O   1 
HETATM 9888 O  O   . HOH DA 6 .   ? 7.267   19.997  -47.374 1.00 48.05 ? 653 HOH D O   1 
HETATM 9889 O  O   . HOH DA 6 .   ? 13.562  -11.417 -38.951 1.00 42.48 ? 654 HOH D O   1 
HETATM 9890 O  O   . HOH DA 6 .   ? 13.927  -10.687 -27.581 1.00 36.76 ? 655 HOH D O   1 
HETATM 9891 O  O   . HOH DA 6 .   ? -3.715  -11.920 -42.511 1.00 35.70 ? 656 HOH D O   1 
HETATM 9892 O  O   . HOH DA 6 .   ? 17.973  -0.015  -54.309 1.00 32.93 ? 657 HOH D O   1 
HETATM 9893 O  O   . HOH DA 6 .   ? 8.533   -13.155 -16.275 1.00 33.19 ? 658 HOH D O   1 
HETATM 9894 O  O   . HOH DA 6 .   ? 6.742   -15.350 -30.731 1.00 36.53 ? 659 HOH D O   1 
HETATM 9895 O  O   . HOH DA 6 .   ? 20.238  -2.912  -36.640 1.00 39.87 ? 660 HOH D O   1 
HETATM 9896 O  O   . HOH DA 6 .   ? 10.207  -10.927 -20.430 1.00 28.93 ? 661 HOH D O   1 
HETATM 9897 O  O   . HOH DA 6 .   ? -2.960  -12.532 -45.230 1.00 24.39 ? 662 HOH D O   1 
HETATM 9898 O  O   . HOH DA 6 .   ? 19.783  -14.631 -34.475 1.00 40.30 ? 663 HOH D O   1 
HETATM 9899 O  O   . HOH DA 6 .   ? 4.669   -16.440 -30.002 1.00 35.87 ? 664 HOH D O   1 
HETATM 9900 O  O   . HOH DA 6 .   ? 27.026  13.023  -47.244 1.00 24.97 ? 665 HOH D O   1 
HETATM 9901 O  O   . HOH DA 6 .   ? -15.272 6.945   -40.464 1.00 25.34 ? 666 HOH D O   1 
HETATM 9902 O  O   . HOH DA 6 .   ? -14.853 -5.187  -36.419 1.00 34.20 ? 667 HOH D O   1 
HETATM 9903 O  O   . HOH DA 6 .   ? -8.658  19.176  -26.139 1.00 34.08 ? 668 HOH D O   1 
HETATM 9904 O  O   . HOH DA 6 .   ? 7.040   -4.161  -58.372 1.00 25.15 ? 669 HOH D O   1 
HETATM 9905 O  O   . HOH DA 6 .   ? 22.156  -7.451  -27.434 1.00 20.02 ? 670 HOH D O   1 
HETATM 9906 O  O   . HOH DA 6 .   ? 1.916   -7.494  -55.531 1.00 22.42 ? 671 HOH D O   1 
HETATM 9907 O  O   . HOH DA 6 .   ? 11.677  -16.634 -21.027 1.00 38.31 ? 672 HOH D O   1 
HETATM 9908 O  O   . HOH DA 6 .   ? 14.281  -11.700 -47.351 1.00 25.82 ? 673 HOH D O   1 
HETATM 9909 O  O   . HOH DA 6 .   ? -16.260 10.131  -54.658 1.00 29.81 ? 674 HOH D O   1 
HETATM 9910 O  O   . HOH DA 6 .   ? 22.363  8.984   -43.470 1.00 21.00 ? 675 HOH D O   1 
HETATM 9911 O  O   . HOH DA 6 .   ? 20.576  -1.252  -42.020 1.00 23.75 ? 676 HOH D O   1 
HETATM 9912 O  O   . HOH DA 6 .   ? 10.109  19.910  -27.866 1.00 27.82 ? 677 HOH D O   1 
HETATM 9913 O  O   . HOH DA 6 .   ? 17.952  16.223  -50.543 1.00 34.45 ? 678 HOH D O   1 
HETATM 9914 O  O   . HOH DA 6 .   ? 11.991  -12.503 -56.606 1.00 24.85 ? 679 HOH D O   1 
HETATM 9915 O  O   . HOH DA 6 .   ? -22.315 6.368   -49.229 1.00 24.41 ? 680 HOH D O   1 
HETATM 9916 O  O   . HOH DA 6 .   ? 11.166  17.873  -52.009 1.00 36.11 ? 681 HOH D O   1 
HETATM 9917 O  O   . HOH DA 6 .   ? 3.806   16.857  -49.096 1.00 35.86 ? 682 HOH D O   1 
HETATM 9918 O  O   . HOH DA 6 .   ? -15.593 -7.679  -38.539 1.00 47.63 ? 683 HOH D O   1 
HETATM 9919 O  O   . HOH DA 6 .   ? -6.616  7.719   -57.402 1.00 26.85 ? 684 HOH D O   1 
HETATM 9920 O  O   . HOH DA 6 .   ? 0.591   6.548   -16.732 1.00 29.39 ? 685 HOH D O   1 
HETATM 9921 O  O   . HOH DA 6 .   ? 3.142   -6.727  -57.985 1.00 22.17 ? 686 HOH D O   1 
HETATM 9922 O  O   . HOH DA 6 .   ? 23.124  11.949  -51.024 1.00 37.54 ? 687 HOH D O   1 
HETATM 9923 O  O   . HOH DA 6 .   ? 4.965   -2.452  -59.050 1.00 24.97 ? 688 HOH D O   1 
HETATM 9924 O  O   . HOH DA 6 .   ? 0.555   -3.552  -56.338 1.00 31.36 ? 689 HOH D O   1 
HETATM 9925 O  O   . HOH DA 6 .   ? -3.131  -9.880  -20.949 1.00 23.84 ? 690 HOH D O   1 
HETATM 9926 O  O   . HOH DA 6 .   ? -4.672  -14.587 -46.653 1.00 35.34 ? 691 HOH D O   1 
HETATM 9927 O  O   . HOH DA 6 .   ? -1.238  -12.482 -39.221 1.00 24.32 ? 692 HOH D O   1 
HETATM 9928 O  O   . HOH DA 6 .   ? -14.753 9.325   -42.129 1.00 29.32 ? 693 HOH D O   1 
HETATM 9929 O  O   . HOH DA 6 .   ? -6.910  -9.405  -26.797 1.00 24.10 ? 694 HOH D O   1 
HETATM 9930 O  O   . HOH DA 6 .   ? 19.909  -11.247 -27.359 1.00 31.85 ? 695 HOH D O   1 
HETATM 9931 O  O   . HOH DA 6 .   ? 14.426  -10.905 -51.265 1.00 29.99 ? 696 HOH D O   1 
HETATM 9932 O  O   . HOH DA 6 .   ? -3.934  -8.841  -18.517 1.00 22.10 ? 697 HOH D O   1 
HETATM 9933 O  O   . HOH DA 6 .   ? 4.975   21.951  -33.505 1.00 31.06 ? 698 HOH D O   1 
HETATM 9934 O  O   . HOH DA 6 .   ? 10.022  -11.988 -33.127 1.00 27.10 ? 699 HOH D O   1 
HETATM 9935 O  O   . HOH DA 6 .   ? -7.943  -6.354  -18.128 1.00 33.19 ? 700 HOH D O   1 
HETATM 9936 O  O   . HOH DA 6 .   ? -4.470  -14.074 -41.493 1.00 36.23 ? 701 HOH D O   1 
HETATM 9937 O  O   . HOH DA 6 .   ? 19.733  -5.739  -41.869 1.00 20.03 ? 702 HOH D O   1 
HETATM 9938 O  O   . HOH DA 6 .   ? 20.653  11.648  -52.394 1.00 35.69 ? 703 HOH D O   1 
HETATM 9939 O  O   . HOH DA 6 .   ? 1.224   -19.659 -38.835 1.00 28.58 ? 704 HOH D O   1 
HETATM 9940 O  O   . HOH DA 6 .   ? 5.169   -15.666 -36.260 1.00 38.07 ? 705 HOH D O   1 
HETATM 9941 O  O   . HOH DA 6 .   ? -14.819 -4.239  -45.575 1.00 36.56 ? 706 HOH D O   1 
HETATM 9942 O  O   . HOH DA 6 .   ? -6.504  -9.075  -52.972 1.00 28.36 ? 707 HOH D O   1 
HETATM 9943 O  O   . HOH DA 6 .   ? -5.571  -15.159 -29.128 1.00 44.30 ? 708 HOH D O   1 
HETATM 9944 O  O   . HOH DA 6 .   ? 10.560  3.846   -19.096 1.00 21.90 ? 709 HOH D O   1 
HETATM 9945 O  O   . HOH DA 6 .   ? 11.903  20.689  -32.482 1.00 16.36 ? 710 HOH D O   1 
HETATM 9946 O  O   . HOH DA 6 .   ? 18.626  7.882   -53.125 1.00 36.97 ? 711 HOH D O   1 
HETATM 9947 O  O   . HOH DA 6 .   ? 12.269  13.072  -22.299 1.00 41.61 ? 712 HOH D O   1 
HETATM 9948 O  O   . HOH DA 6 .   ? 7.201   20.395  -33.763 1.00 18.63 ? 713 HOH D O   1 
HETATM 9949 O  O   . HOH DA 6 .   ? 14.565  -12.394 -54.515 1.00 26.92 ? 714 HOH D O   1 
HETATM 9950 O  O   . HOH DA 6 .   ? 6.925   -8.572  -58.851 1.00 21.11 ? 715 HOH D O   1 
HETATM 9951 O  O   . HOH DA 6 .   ? 27.582  12.937  -49.769 1.00 31.83 ? 716 HOH D O   1 
HETATM 9952 O  O   . HOH DA 6 .   ? -6.678  -8.786  -18.129 1.00 22.02 ? 717 HOH D O   1 
HETATM 9953 O  O   . HOH DA 6 .   ? 11.803  6.140   -19.512 1.00 26.11 ? 718 HOH D O   1 
HETATM 9954 O  O   . HOH DA 6 .   ? 10.010  8.558   -19.464 1.00 28.76 ? 719 HOH D O   1 
HETATM 9955 O  O   . HOH DA 6 .   ? -7.330  -11.835 -52.245 1.00 37.66 ? 720 HOH D O   1 
HETATM 9956 O  O   . HOH DA 6 .   ? -4.876  -11.576 -22.059 1.00 38.42 ? 721 HOH D O   1 
HETATM 9957 O  O   . HOH DA 6 .   ? -8.096  -10.151 -20.150 1.00 39.02 ? 722 HOH D O   1 
HETATM 9958 O  O   . HOH DA 6 .   ? -7.216  -10.943 -24.404 1.00 34.43 ? 723 HOH D O   1 
HETATM 9959 O  O   . HOH DA 6 .   ? -9.356  -11.963 -50.241 1.00 35.17 ? 724 HOH D O   1 
# 
