data_5LL5
# 
_entry.id   5LL5 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.397 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   5LL5         pdb_00005ll5 10.2210/pdb5ll5/pdb 
WWPDB D_1200000935 ?            ?                   
# 
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 2024-10-16 
# 
_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                        5LL5 
_pdbx_database_status.recvd_initial_deposition_date   2016-07-26 
_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)benzenesulfonamide' ? 
3 non-polymer syn '4-[2-(benzimidazol-1-yl)ethanoyl]benzenesulfonamide' 315.347   4    ?       ? Zn ? 
4 non-polymer syn 1,2-ETHANEDIOL                                        62.068    11   ?       ? EDO ? 
5 water       nat water                                                 18.015    1200 ?       ? ? ? 
# 
_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]benzenesulfonamide' 6YH 
4 1,2-ETHANEDIOL                                        EDO 
5 water                                                 HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   SER n 
1 3   LYS n 
1 4   TRP n 
1 5   THR n 
1 6   TYR n 
1 7   PHE n 
1 8   GLY n 
1 9   PRO n 
1 10  ASP n 
1 11  GLY n 
1 12  GLU n 
1 13  ASN n 
1 14  SER n 
1 15  TRP n 
1 16  SER n 
1 17  LYS n 
1 18  LYS n 
1 19  TYR n 
1 20  PRO n 
1 21  SER n 
1 22  CYS n 
1 23  GLY n 
1 24  GLY n 
1 25  LEU n 
1 26  LEU n 
1 27  GLN n 
1 28  SER n 
1 29  PRO n 
1 30  ILE n 
1 31  ASP n 
1 32  LEU n 
1 33  HIS n 
1 34  SER n 
1 35  ASP n 
1 36  ILE n 
1 37  LEU n 
1 38  GLN n 
1 39  TYR n 
1 40  ASP n 
1 41  ALA n 
1 42  SER n 
1 43  LEU n 
1 44  THR n 
1 45  PRO n 
1 46  LEU n 
1 47  GLU n 
1 48  PHE n 
1 49  GLN n 
1 50  GLY n 
1 51  TYR n 
1 52  ASN n 
1 53  LEU n 
1 54  SER n 
1 55  ALA n 
1 56  ASN n 
1 57  LYS n 
1 58  GLN n 
1 59  PHE n 
1 60  LEU n 
1 61  LEU n 
1 62  THR n 
1 63  ASN n 
1 64  ASN n 
1 65  GLY n 
1 66  HIS n 
1 67  SER n 
1 68  VAL n 
1 69  LYS n 
1 70  LEU n 
1 71  ASN n 
1 72  LEU n 
1 73  PRO n 
1 74  SER n 
1 75  ASP n 
1 76  MET n 
1 77  HIS n 
1 78  ILE n 
1 79  GLN n 
1 80  GLY n 
1 81  LEU n 
1 82  GLN n 
1 83  SER n 
1 84  ARG n 
1 85  TYR n 
1 86  SER n 
1 87  ALA n 
1 88  THR n 
1 89  GLN n 
1 90  LEU n 
1 91  HIS n 
1 92  LEU n 
1 93  HIS n 
1 94  TRP n 
1 95  GLY n 
1 96  ASN n 
1 97  PRO n 
1 98  ASN n 
1 99  ASP n 
1 100 PRO n 
1 101 HIS n 
1 102 GLY n 
1 103 SER n 
1 104 GLU n 
1 105 HIS n 
1 106 THR n 
1 107 VAL n 
1 108 SER n 
1 109 GLY n 
1 110 GLN n 
1 111 HIS n 
1 112 PHE n 
1 113 ALA n 
1 114 ALA n 
1 115 GLU n 
1 116 LEU n 
1 117 HIS n 
1 118 ILE n 
1 119 VAL n 
1 120 HIS n 
1 121 TYR n 
1 122 ASN n 
1 123 SER n 
1 124 ASP n 
1 125 LEU n 
1 126 TYR n 
1 127 PRO n 
1 128 ASP n 
1 129 ALA n 
1 130 SER n 
1 131 THR n 
1 132 ALA n 
1 133 SER n 
1 134 ASN n 
1 135 LYS n 
1 136 SER n 
1 137 GLU n 
1 138 GLY n 
1 139 LEU n 
1 140 ALA n 
1 141 VAL n 
1 142 LEU n 
1 143 ALA n 
1 144 VAL n 
1 145 LEU n 
1 146 ILE n 
1 147 GLU n 
1 148 MET n 
1 149 GLY n 
1 150 SER n 
1 151 PHE n 
1 152 ASN n 
1 153 PRO n 
1 154 SER n 
1 155 TYR n 
1 156 ASP n 
1 157 LYS n 
1 158 ILE n 
1 159 PHE n 
1 160 SER n 
1 161 HIS n 
1 162 LEU n 
1 163 GLN n 
1 164 HIS n 
1 165 VAL n 
1 166 LYS n 
1 167 TYR n 
1 168 LYS n 
1 169 GLY n 
1 170 GLN n 
1 171 GLU n 
1 172 ALA n 
1 173 PHE n 
1 174 VAL n 
1 175 PRO n 
1 176 GLY n 
1 177 PHE n 
1 178 ASN n 
1 179 ILE n 
1 180 GLU n 
1 181 GLU n 
1 182 LEU n 
1 183 LEU n 
1 184 PRO n 
1 185 GLU n 
1 186 ARG n 
1 187 THR n 
1 188 ALA n 
1 189 GLU n 
1 190 TYR n 
1 191 TYR n 
1 192 ARG n 
1 193 TYR n 
1 194 ARG n 
1 195 GLY n 
1 196 SER n 
1 197 LEU n 
1 198 THR n 
1 199 THR n 
1 200 PRO n 
1 201 PRO n 
1 202 CYS n 
1 203 ASN n 
1 204 PRO n 
1 205 THR n 
1 206 VAL n 
1 207 LEU n 
1 208 TRP n 
1 209 THR n 
1 210 VAL n 
1 211 PHE n 
1 212 ARG n 
1 213 ASN n 
1 214 PRO n 
1 215 VAL n 
1 216 GLN n 
1 217 ILE n 
1 218 SER n 
1 219 GLN n 
1 220 GLU n 
1 221 GLN n 
1 222 LEU n 
1 223 LEU n 
1 224 ALA n 
1 225 LEU n 
1 226 GLU n 
1 227 THR n 
1 228 ALA n 
1 229 LEU n 
1 230 TYR n 
1 231 CYS n 
1 232 THR n 
1 233 HIS n 
1 234 MET n 
1 235 ASP n 
1 236 ASP n 
1 237 PRO n 
1 238 SER n 
1 239 PRO n 
1 240 ARG n 
1 241 GLU n 
1 242 MET n 
1 243 ILE n 
1 244 ASN n 
1 245 ASN n 
1 246 PHE n 
1 247 ARG n 
1 248 GLN n 
1 249 VAL n 
1 250 GLN n 
1 251 LYS n 
1 252 PHE n 
1 253 ASP n 
1 254 GLU n 
1 255 ARG n 
1 256 LEU n 
1 257 VAL n 
1 258 TYR n 
1 259 THR n 
1 260 SER n 
1 261 PHE n 
1 262 SER n 
1 263 GLN n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   263 
_entity_src_gen.gene_src_common_name               Human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 CA12 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              Rosetta 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pET21a 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
6YH non-polymer         . '4-[2-(benzimidazol-1-yl)ethanoyl]benzenesulfonamide' ?                 'C15 H13 N3 O3 S' 315.347 
ALA 'L-peptide linking' y ALANINE                                               ?                 'C3 H7 N O2'      89.093  
ARG 'L-peptide linking' y ARGININE                                              ?                 'C6 H15 N4 O2 1'  175.209 
ASN 'L-peptide linking' y ASPARAGINE                                            ?                 'C4 H8 N2 O3'     132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                                       ?                 'C4 H7 N O4'      133.103 
CYS 'L-peptide linking' y CYSTEINE                                              ?                 'C3 H7 N O2 S'    121.158 
EDO non-polymer         . 1,2-ETHANEDIOL                                        'ETHYLENE GLYCOL' 'C2 H6 O2'        62.068  
GLN 'L-peptide linking' y GLUTAMINE                                             ?                 'C5 H10 N2 O3'    146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                       ?                 'C5 H9 N O4'      147.129 
GLY 'peptide linking'   y GLYCINE                                               ?                 'C2 H5 N O2'      75.067  
HIS 'L-peptide linking' y HISTIDINE                                             ?                 'C6 H10 N3 O2 1'  156.162 
HOH non-polymer         . WATER                                                 ?                 'H2 O'            18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                            ?                 'C6 H13 N O2'     131.173 
LEU 'L-peptide linking' y LEUCINE                                               ?                 'C6 H13 N O2'     131.173 
LYS 'L-peptide linking' y LYSINE                                                ?                 'C6 H15 N2 O2 1'  147.195 
MET 'L-peptide linking' y METHIONINE                                            ?                 'C5 H11 N O2 S'   149.211 
PHE 'L-peptide linking' y PHENYLALANINE                                         ?                 'C9 H11 N O2'     165.189 
PRO 'L-peptide linking' y PROLINE                                               ?                 'C5 H9 N O2'      115.130 
SER 'L-peptide linking' y SERINE                                                ?                 'C3 H7 N O3'      105.093 
THR 'L-peptide linking' y THREONINE                                             ?                 'C4 H9 N O3'      119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                            ?                 'C11 H12 N2 O2'   204.225 
TYR 'L-peptide linking' y TYROSINE                                              ?                 'C9 H11 N O3'     181.189 
VAL 'L-peptide linking' y VALINE                                                ?                 'C5 H11 N O2'     117.146 
ZN  non-polymer         . 'ZINC ION'                                            ?                 'Zn 2'            65.409  
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   SER 2   2   ?   ?   ?   A . n 
A 1 3   LYS 3   3   3   LYS LYS A . n 
A 1 4   TRP 4   4   4   TRP TRP A . n 
A 1 5   THR 5   5   5   THR THR A . n 
A 1 6   TYR 6   6   6   TYR TYR A . n 
A 1 7   PHE 7   7   7   PHE PHE A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   PRO 9   9   9   PRO PRO A . n 
A 1 10  ASP 10  10  10  ASP ASP A . n 
A 1 11  GLY 11  11  11  GLY GLY A . n 
A 1 12  GLU 12  12  12  GLU GLU A . n 
A 1 13  ASN 13  13  13  ASN ASN A . n 
A 1 14  SER 14  14  14  SER SER A . n 
A 1 15  TRP 15  15  15  TRP TRP A . n 
A 1 16  SER 16  16  16  SER SER A . n 
A 1 17  LYS 17  17  17  LYS LYS A . n 
A 1 18  LYS 18  18  18  LYS LYS A . n 
A 1 19  TYR 19  19  19  TYR TYR A . n 
A 1 20  PRO 20  20  20  PRO PRO A . n 
A 1 21  SER 21  21  21  SER SER A . n 
A 1 22  CYS 22  22  22  CYS CYS A . n 
A 1 23  GLY 23  23  23  GLY GLY A . n 
A 1 24  GLY 24  24  24  GLY GLY A . n 
A 1 25  LEU 25  25  25  LEU LEU A . n 
A 1 26  LEU 26  26  26  LEU LEU A . n 
A 1 27  GLN 27  27  27  GLN GLN A . n 
A 1 28  SER 28  28  28  SER SER A . n 
A 1 29  PRO 29  29  29  PRO PRO A . n 
A 1 30  ILE 30  30  30  ILE ILE A . n 
A 1 31  ASP 31  31  31  ASP ASP A . n 
A 1 32  LEU 32  32  32  LEU LEU A . n 
A 1 33  HIS 33  33  33  HIS HIS A . n 
A 1 34  SER 34  34  34  SER SER A . n 
A 1 35  ASP 35  35  35  ASP ASP A . n 
A 1 36  ILE 36  36  36  ILE ILE A . n 
A 1 37  LEU 37  37  37  LEU LEU A . n 
A 1 38  GLN 38  38  38  GLN GLN A . n 
A 1 39  TYR 39  39  39  TYR TYR A . n 
A 1 40  ASP 40  40  40  ASP ASP A . n 
A 1 41  ALA 41  41  41  ALA ALA A . n 
A 1 42  SER 42  42  42  SER SER A . n 
A 1 43  LEU 43  43  43  LEU LEU A . n 
A 1 44  THR 44  44  44  THR THR A . n 
A 1 45  PRO 45  45  45  PRO PRO A . n 
A 1 46  LEU 46  46  46  LEU LEU A . n 
A 1 47  GLU 47  47  47  GLU GLU A . n 
A 1 48  PHE 48  48  48  PHE PHE A . n 
A 1 49  GLN 49  49  49  GLN GLN A . n 
A 1 50  GLY 50  50  50  GLY GLY A . n 
A 1 51  TYR 51  51  51  TYR TYR A . n 
A 1 52  ASN 52  52  52  ASN ASN A . n 
A 1 53  LEU 53  53  53  LEU LEU A . n 
A 1 54  SER 54  54  54  SER SER A . n 
A 1 55  ALA 55  55  55  ALA ALA A . n 
A 1 56  ASN 56  56  56  ASN ASN A . n 
A 1 57  LYS 57  57  57  LYS LYS A . n 
A 1 58  GLN 58  58  58  GLN GLN A . n 
A 1 59  PHE 59  59  59  PHE PHE A . n 
A 1 60  LEU 60  60  60  LEU LEU A . n 
A 1 61  LEU 61  61  61  LEU LEU A . n 
A 1 62  THR 62  62  62  THR THR A . n 
A 1 63  ASN 63  63  63  ASN ASN A . n 
A 1 64  ASN 64  64  64  ASN ASN A . n 
A 1 65  GLY 65  65  65  GLY GLY A . n 
A 1 66  HIS 66  66  66  HIS HIS A . n 
A 1 67  SER 67  67  67  SER SER A . n 
A 1 68  VAL 68  68  68  VAL VAL A . n 
A 1 69  LYS 69  69  69  LYS LYS A . n 
A 1 70  LEU 70  70  70  LEU LEU A . n 
A 1 71  ASN 71  71  71  ASN ASN A . n 
A 1 72  LEU 72  72  72  LEU LEU A . n 
A 1 73  PRO 73  73  73  PRO PRO A . n 
A 1 74  SER 74  74  74  SER SER A . n 
A 1 75  ASP 75  75  75  ASP ASP A . n 
A 1 76  MET 76  76  76  MET MET A . n 
A 1 77  HIS 77  77  77  HIS HIS A . n 
A 1 78  ILE 78  78  78  ILE ILE A . n 
A 1 79  GLN 79  79  79  GLN GLN A . n 
A 1 80  GLY 80  80  80  GLY GLY A . n 
A 1 81  LEU 81  81  81  LEU LEU A . n 
A 1 82  GLN 82  82  82  GLN GLN A . n 
A 1 83  SER 83  83  83  SER SER A . n 
A 1 84  ARG 84  84  84  ARG ARG A . n 
A 1 85  TYR 85  85  85  TYR TYR A . n 
A 1 86  SER 86  86  86  SER SER A . n 
A 1 87  ALA 87  87  87  ALA ALA A . n 
A 1 88  THR 88  88  88  THR THR A . n 
A 1 89  GLN 89  89  89  GLN GLN A . n 
A 1 90  LEU 90  90  90  LEU LEU A . n 
A 1 91  HIS 91  91  91  HIS HIS A . n 
A 1 92  LEU 92  92  92  LEU LEU A . n 
A 1 93  HIS 93  93  93  HIS HIS A . n 
A 1 94  TRP 94  94  94  TRP TRP A . n 
A 1 95  GLY 95  95  95  GLY GLY A . n 
A 1 96  ASN 96  96  96  ASN ASN A . n 
A 1 97  PRO 97  97  97  PRO PRO A . n 
A 1 98  ASN 98  98  98  ASN ASN A . n 
A 1 99  ASP 99  99  99  ASP ASP A . n 
A 1 100 PRO 100 100 100 PRO PRO A . n 
A 1 101 HIS 101 101 101 HIS HIS A . n 
A 1 102 GLY 102 102 102 GLY GLY A . n 
A 1 103 SER 103 103 103 SER SER A . n 
A 1 104 GLU 104 104 104 GLU GLU A . n 
A 1 105 HIS 105 105 105 HIS HIS A . n 
A 1 106 THR 106 106 106 THR THR A . n 
A 1 107 VAL 107 107 107 VAL VAL A . n 
A 1 108 SER 108 108 108 SER SER A . n 
A 1 109 GLY 109 109 109 GLY GLY A . n 
A 1 110 GLN 110 110 110 GLN GLN A . n 
A 1 111 HIS 111 111 111 HIS HIS A . n 
A 1 112 PHE 112 112 112 PHE PHE A . n 
A 1 113 ALA 113 113 113 ALA ALA A . n 
A 1 114 ALA 114 114 114 ALA ALA A . n 
A 1 115 GLU 115 115 115 GLU GLU A . n 
A 1 116 LEU 116 116 116 LEU LEU A . n 
A 1 117 HIS 117 117 117 HIS HIS A . n 
A 1 118 ILE 118 118 118 ILE ILE A . n 
A 1 119 VAL 119 119 119 VAL VAL A . n 
A 1 120 HIS 120 120 120 HIS HIS A . n 
A 1 121 TYR 121 121 121 TYR TYR A . n 
A 1 122 ASN 122 122 122 ASN ASN A . n 
A 1 123 SER 123 123 123 SER SER A . n 
A 1 124 ASP 124 124 124 ASP ASP A . n 
A 1 125 LEU 125 125 125 LEU LEU A . n 
A 1 126 TYR 126 126 126 TYR TYR A . n 
A 1 127 PRO 127 127 127 PRO PRO A . n 
A 1 128 ASP 128 128 128 ASP ASP A . n 
A 1 129 ALA 129 129 129 ALA ALA A . n 
A 1 130 SER 130 130 130 SER SER A . n 
A 1 131 THR 131 131 131 THR THR A . n 
A 1 132 ALA 132 132 132 ALA ALA A . n 
A 1 133 SER 133 133 133 SER SER A . n 
A 1 134 ASN 134 134 134 ASN ASN A . n 
A 1 135 LYS 135 135 135 LYS LYS A . n 
A 1 136 SER 136 136 136 SER SER A . n 
A 1 137 GLU 137 137 137 GLU GLU A . n 
A 1 138 GLY 138 138 138 GLY GLY A . n 
A 1 139 LEU 139 139 139 LEU LEU A . n 
A 1 140 ALA 140 140 140 ALA ALA A . n 
A 1 141 VAL 141 141 141 VAL VAL A . n 
A 1 142 LEU 142 142 142 LEU LEU A . n 
A 1 143 ALA 143 143 143 ALA ALA A . n 
A 1 144 VAL 144 144 144 VAL VAL A . n 
A 1 145 LEU 145 145 145 LEU LEU A . n 
A 1 146 ILE 146 146 146 ILE ILE A . n 
A 1 147 GLU 147 147 147 GLU GLU A . n 
A 1 148 MET 148 148 148 MET MET A . n 
A 1 149 GLY 149 149 149 GLY GLY A . n 
A 1 150 SER 150 150 150 SER SER A . n 
A 1 151 PHE 151 151 151 PHE PHE A . n 
A 1 152 ASN 152 152 152 ASN ASN A . n 
A 1 153 PRO 153 153 153 PRO PRO A . n 
A 1 154 SER 154 154 154 SER SER A . n 
A 1 155 TYR 155 155 155 TYR TYR A . n 
A 1 156 ASP 156 156 156 ASP ASP A . n 
A 1 157 LYS 157 157 157 LYS LYS A . n 
A 1 158 ILE 158 158 158 ILE ILE A . n 
A 1 159 PHE 159 159 159 PHE PHE A . n 
A 1 160 SER 160 160 160 SER SER A . n 
A 1 161 HIS 161 161 161 HIS HIS A . n 
A 1 162 LEU 162 162 162 LEU LEU A . n 
A 1 163 GLN 163 163 163 GLN GLN A . n 
A 1 164 HIS 164 164 164 HIS HIS A . n 
A 1 165 VAL 165 165 165 VAL VAL A . n 
A 1 166 LYS 166 166 166 LYS LYS A . n 
A 1 167 TYR 167 167 167 TYR TYR A . n 
A 1 168 LYS 168 168 168 LYS LYS A . n 
A 1 169 GLY 169 169 169 GLY GLY A . n 
A 1 170 GLN 170 170 170 GLN GLN A . n 
A 1 171 GLU 171 171 171 GLU GLU A . n 
A 1 172 ALA 172 172 172 ALA ALA A . n 
A 1 173 PHE 173 173 173 PHE PHE A . n 
A 1 174 VAL 174 174 174 VAL VAL A . n 
A 1 175 PRO 175 175 175 PRO PRO A . n 
A 1 176 GLY 176 176 176 GLY GLY A . n 
A 1 177 PHE 177 177 177 PHE PHE A . n 
A 1 178 ASN 178 178 178 ASN ASN A . n 
A 1 179 ILE 179 179 179 ILE ILE A . n 
A 1 180 GLU 180 180 180 GLU GLU A . n 
A 1 181 GLU 181 181 181 GLU GLU A . n 
A 1 182 LEU 182 182 182 LEU LEU A . n 
A 1 183 LEU 183 183 183 LEU LEU A . n 
A 1 184 PRO 184 184 184 PRO PRO A . n 
A 1 185 GLU 185 185 185 GLU GLU A . n 
A 1 186 ARG 186 186 186 ARG ARG A . n 
A 1 187 THR 187 187 187 THR THR A . n 
A 1 188 ALA 188 188 188 ALA ALA A . n 
A 1 189 GLU 189 189 189 GLU GLU A . n 
A 1 190 TYR 190 190 190 TYR TYR A . n 
A 1 191 TYR 191 191 191 TYR TYR A . n 
A 1 192 ARG 192 192 192 ARG ARG A . n 
A 1 193 TYR 193 193 193 TYR TYR A . n 
A 1 194 ARG 194 194 194 ARG ARG A . n 
A 1 195 GLY 195 195 195 GLY GLY A . n 
A 1 196 SER 196 196 196 SER SER A . n 
A 1 197 LEU 197 197 197 LEU LEU A . n 
A 1 198 THR 198 198 198 THR THR A . n 
A 1 199 THR 199 199 199 THR THR A . n 
A 1 200 PRO 200 200 200 PRO PRO A . n 
A 1 201 PRO 201 201 201 PRO PRO A . n 
A 1 202 CYS 202 202 202 CYS CYS A . n 
A 1 203 ASN 203 203 203 ASN ASN A . n 
A 1 204 PRO 204 204 204 PRO PRO A . n 
A 1 205 THR 205 205 205 THR THR A . n 
A 1 206 VAL 206 206 206 VAL VAL A . n 
A 1 207 LEU 207 207 207 LEU LEU A . n 
A 1 208 TRP 208 208 208 TRP TRP A . n 
A 1 209 THR 209 209 209 THR THR A . n 
A 1 210 VAL 210 210 210 VAL VAL A . n 
A 1 211 PHE 211 211 211 PHE PHE A . n 
A 1 212 ARG 212 212 212 ARG ARG A . n 
A 1 213 ASN 213 213 213 ASN ASN A . n 
A 1 214 PRO 214 214 214 PRO PRO A . n 
A 1 215 VAL 215 215 215 VAL VAL A . n 
A 1 216 GLN 216 216 216 GLN GLN A . n 
A 1 217 ILE 217 217 217 ILE ILE A . n 
A 1 218 SER 218 218 218 SER SER A . n 
A 1 219 GLN 219 219 219 GLN GLN A . n 
A 1 220 GLU 220 220 220 GLU GLU A . n 
A 1 221 GLN 221 221 221 GLN GLN A . n 
A 1 222 LEU 222 222 222 LEU LEU A . n 
A 1 223 LEU 223 223 223 LEU LEU A . n 
A 1 224 ALA 224 224 224 ALA ALA A . n 
A 1 225 LEU 225 225 225 LEU LEU A . n 
A 1 226 GLU 226 226 226 GLU GLU A . n 
A 1 227 THR 227 227 227 THR THR A . n 
A 1 228 ALA 228 228 228 ALA ALA A . n 
A 1 229 LEU 229 229 229 LEU LEU A . n 
A 1 230 TYR 230 230 230 TYR TYR A . n 
A 1 231 CYS 231 231 231 CYS CYS A . n 
A 1 232 THR 232 232 232 THR THR A . n 
A 1 233 HIS 233 233 233 HIS HIS A . n 
A 1 234 MET 234 234 234 MET MET A . n 
A 1 235 ASP 235 235 235 ASP ASP A . n 
A 1 236 ASP 236 236 236 ASP ASP A . n 
A 1 237 PRO 237 237 237 PRO PRO A . n 
A 1 238 SER 238 238 238 SER SER A . n 
A 1 239 PRO 239 239 239 PRO PRO A . n 
A 1 240 ARG 240 240 240 ARG ARG A . n 
A 1 241 GLU 241 241 241 GLU GLU A . n 
A 1 242 MET 242 242 242 MET MET A . n 
A 1 243 ILE 243 243 243 ILE ILE A . n 
A 1 244 ASN 244 244 244 ASN ASN A . n 
A 1 245 ASN 245 245 245 ASN ASN A . n 
A 1 246 PHE 246 246 246 PHE PHE A . n 
A 1 247 ARG 247 247 247 ARG ARG A . n 
A 1 248 GLN 248 248 248 GLN GLN A . n 
A 1 249 VAL 249 249 249 VAL VAL A . n 
A 1 250 GLN 250 250 250 GLN GLN A . n 
A 1 251 LYS 251 251 251 LYS LYS A . n 
A 1 252 PHE 252 252 252 PHE PHE A . n 
A 1 253 ASP 253 253 253 ASP ASP A . n 
A 1 254 GLU 254 254 254 GLU GLU A . n 
A 1 255 ARG 255 255 255 ARG ARG A . n 
A 1 256 LEU 256 256 256 LEU LEU A . n 
A 1 257 VAL 257 257 257 VAL VAL A . n 
A 1 258 TYR 258 258 258 TYR TYR A . n 
A 1 259 THR 259 259 259 THR THR A . n 
A 1 260 SER 260 260 260 SER SER A . n 
A 1 261 PHE 261 261 261 PHE PHE A . n 
A 1 262 SER 262 262 262 SER SER A . n 
A 1 263 GLN 263 263 263 GLN GLN A . n 
B 1 1   MET 1   1   ?   ?   ?   B . n 
B 1 2   SER 2   2   ?   ?   ?   B . n 
B 1 3   LYS 3   3   3   LYS LYS B . n 
B 1 4   TRP 4   4   4   TRP TRP B . n 
B 1 5   THR 5   5   5   THR THR B . n 
B 1 6   TYR 6   6   6   TYR TYR B . n 
B 1 7   PHE 7   7   7   PHE PHE B . n 
B 1 8   GLY 8   8   8   GLY GLY B . n 
B 1 9   PRO 9   9   9   PRO PRO B . n 
B 1 10  ASP 10  10  10  ASP ASP B . n 
B 1 11  GLY 11  11  11  GLY GLY B . n 
B 1 12  GLU 12  12  12  GLU GLU B . n 
B 1 13  ASN 13  13  13  ASN ASN B . n 
B 1 14  SER 14  14  14  SER SER B . n 
B 1 15  TRP 15  15  15  TRP TRP B . n 
B 1 16  SER 16  16  16  SER SER B . n 
B 1 17  LYS 17  17  17  LYS LYS B . n 
B 1 18  LYS 18  18  18  LYS LYS B . n 
B 1 19  TYR 19  19  19  TYR TYR B . n 
B 1 20  PRO 20  20  20  PRO PRO B . n 
B 1 21  SER 21  21  21  SER SER B . n 
B 1 22  CYS 22  22  22  CYS CYS B . n 
B 1 23  GLY 23  23  23  GLY GLY B . n 
B 1 24  GLY 24  24  24  GLY GLY B . n 
B 1 25  LEU 25  25  25  LEU LEU B . n 
B 1 26  LEU 26  26  26  LEU LEU B . n 
B 1 27  GLN 27  27  27  GLN GLN B . n 
B 1 28  SER 28  28  28  SER SER B . n 
B 1 29  PRO 29  29  29  PRO PRO B . n 
B 1 30  ILE 30  30  30  ILE ILE B . n 
B 1 31  ASP 31  31  31  ASP ASP B . n 
B 1 32  LEU 32  32  32  LEU LEU B . n 
B 1 33  HIS 33  33  33  HIS HIS B . n 
B 1 34  SER 34  34  34  SER SER B . n 
B 1 35  ASP 35  35  35  ASP ASP B . n 
B 1 36  ILE 36  36  36  ILE ILE B . n 
B 1 37  LEU 37  37  37  LEU LEU B . n 
B 1 38  GLN 38  38  38  GLN GLN B . n 
B 1 39  TYR 39  39  39  TYR TYR B . n 
B 1 40  ASP 40  40  40  ASP ASP B . n 
B 1 41  ALA 41  41  41  ALA ALA B . n 
B 1 42  SER 42  42  42  SER SER B . n 
B 1 43  LEU 43  43  43  LEU LEU B . n 
B 1 44  THR 44  44  44  THR THR B . n 
B 1 45  PRO 45  45  45  PRO PRO B . n 
B 1 46  LEU 46  46  46  LEU LEU B . n 
B 1 47  GLU 47  47  47  GLU GLU B . n 
B 1 48  PHE 48  48  48  PHE PHE B . n 
B 1 49  GLN 49  49  49  GLN GLN B . n 
B 1 50  GLY 50  50  50  GLY GLY B . n 
B 1 51  TYR 51  51  51  TYR TYR B . n 
B 1 52  ASN 52  52  52  ASN ASN B . n 
B 1 53  LEU 53  53  53  LEU LEU B . n 
B 1 54  SER 54  54  54  SER SER B . n 
B 1 55  ALA 55  55  55  ALA ALA B . n 
B 1 56  ASN 56  56  56  ASN ASN B . n 
B 1 57  LYS 57  57  57  LYS LYS B . n 
B 1 58  GLN 58  58  58  GLN GLN B . n 
B 1 59  PHE 59  59  59  PHE PHE B . n 
B 1 60  LEU 60  60  60  LEU LEU B . n 
B 1 61  LEU 61  61  61  LEU LEU B . n 
B 1 62  THR 62  62  62  THR THR B . n 
B 1 63  ASN 63  63  63  ASN ASN B . n 
B 1 64  ASN 64  64  64  ASN ASN B . n 
B 1 65  GLY 65  65  65  GLY GLY B . n 
B 1 66  HIS 66  66  66  HIS HIS B . n 
B 1 67  SER 67  67  67  SER SER B . n 
B 1 68  VAL 68  68  68  VAL VAL B . n 
B 1 69  LYS 69  69  69  LYS LYS B . n 
B 1 70  LEU 70  70  70  LEU LEU B . n 
B 1 71  ASN 71  71  71  ASN ASN B . n 
B 1 72  LEU 72  72  72  LEU LEU B . n 
B 1 73  PRO 73  73  73  PRO PRO B . n 
B 1 74  SER 74  74  74  SER SER B . n 
B 1 75  ASP 75  75  75  ASP ASP B . n 
B 1 76  MET 76  76  76  MET MET B . n 
B 1 77  HIS 77  77  77  HIS HIS B . n 
B 1 78  ILE 78  78  78  ILE ILE B . n 
B 1 79  GLN 79  79  79  GLN GLN B . n 
B 1 80  GLY 80  80  80  GLY GLY B . n 
B 1 81  LEU 81  81  81  LEU LEU B . n 
B 1 82  GLN 82  82  82  GLN GLN B . n 
B 1 83  SER 83  83  83  SER SER B . n 
B 1 84  ARG 84  84  84  ARG ARG B . n 
B 1 85  TYR 85  85  85  TYR TYR B . n 
B 1 86  SER 86  86  86  SER SER B . n 
B 1 87  ALA 87  87  87  ALA ALA B . n 
B 1 88  THR 88  88  88  THR THR B . n 
B 1 89  GLN 89  89  89  GLN GLN B . n 
B 1 90  LEU 90  90  90  LEU LEU B . n 
B 1 91  HIS 91  91  91  HIS HIS B . n 
B 1 92  LEU 92  92  92  LEU LEU B . n 
B 1 93  HIS 93  93  93  HIS HIS B . n 
B 1 94  TRP 94  94  94  TRP TRP B . n 
B 1 95  GLY 95  95  95  GLY GLY B . n 
B 1 96  ASN 96  96  96  ASN ASN B . n 
B 1 97  PRO 97  97  97  PRO PRO B . n 
B 1 98  ASN 98  98  98  ASN ASN B . n 
B 1 99  ASP 99  99  99  ASP ASP B . n 
B 1 100 PRO 100 100 100 PRO PRO B . n 
B 1 101 HIS 101 101 101 HIS HIS B . n 
B 1 102 GLY 102 102 102 GLY GLY B . n 
B 1 103 SER 103 103 103 SER SER B . n 
B 1 104 GLU 104 104 104 GLU GLU B . n 
B 1 105 HIS 105 105 105 HIS HIS B . n 
B 1 106 THR 106 106 106 THR THR B . n 
B 1 107 VAL 107 107 107 VAL VAL B . n 
B 1 108 SER 108 108 108 SER SER B . n 
B 1 109 GLY 109 109 109 GLY GLY B . n 
B 1 110 GLN 110 110 110 GLN GLN B . n 
B 1 111 HIS 111 111 111 HIS HIS B . n 
B 1 112 PHE 112 112 112 PHE PHE B . n 
B 1 113 ALA 113 113 113 ALA ALA B . n 
B 1 114 ALA 114 114 114 ALA ALA B . n 
B 1 115 GLU 115 115 115 GLU GLU B . n 
B 1 116 LEU 116 116 116 LEU LEU B . n 
B 1 117 HIS 117 117 117 HIS HIS B . n 
B 1 118 ILE 118 118 118 ILE ILE B . n 
B 1 119 VAL 119 119 119 VAL VAL B . n 
B 1 120 HIS 120 120 120 HIS HIS B . n 
B 1 121 TYR 121 121 121 TYR TYR B . n 
B 1 122 ASN 122 122 122 ASN ASN B . n 
B 1 123 SER 123 123 123 SER SER B . n 
B 1 124 ASP 124 124 124 ASP ASP B . n 
B 1 125 LEU 125 125 125 LEU LEU B . n 
B 1 126 TYR 126 126 126 TYR TYR B . n 
B 1 127 PRO 127 127 127 PRO PRO B . n 
B 1 128 ASP 128 128 128 ASP ASP B . n 
B 1 129 ALA 129 129 129 ALA ALA B . n 
B 1 130 SER 130 130 130 SER SER B . n 
B 1 131 THR 131 131 131 THR THR B . n 
B 1 132 ALA 132 132 132 ALA ALA B . n 
B 1 133 SER 133 133 133 SER SER B . n 
B 1 134 ASN 134 134 134 ASN ASN B . n 
B 1 135 LYS 135 135 135 LYS LYS B . n 
B 1 136 SER 136 136 136 SER SER B . n 
B 1 137 GLU 137 137 137 GLU GLU B . n 
B 1 138 GLY 138 138 138 GLY GLY B . n 
B 1 139 LEU 139 139 139 LEU LEU B . n 
B 1 140 ALA 140 140 140 ALA ALA B . n 
B 1 141 VAL 141 141 141 VAL VAL B . n 
B 1 142 LEU 142 142 142 LEU LEU B . n 
B 1 143 ALA 143 143 143 ALA ALA B . n 
B 1 144 VAL 144 144 144 VAL VAL B . n 
B 1 145 LEU 145 145 145 LEU LEU B . n 
B 1 146 ILE 146 146 146 ILE ILE B . n 
B 1 147 GLU 147 147 147 GLU GLU B . n 
B 1 148 MET 148 148 148 MET MET B . n 
B 1 149 GLY 149 149 149 GLY GLY B . n 
B 1 150 SER 150 150 150 SER SER B . n 
B 1 151 PHE 151 151 151 PHE PHE B . n 
B 1 152 ASN 152 152 152 ASN ASN B . n 
B 1 153 PRO 153 153 153 PRO PRO B . n 
B 1 154 SER 154 154 154 SER SER B . n 
B 1 155 TYR 155 155 155 TYR TYR B . n 
B 1 156 ASP 156 156 156 ASP ASP B . n 
B 1 157 LYS 157 157 157 LYS LYS B . n 
B 1 158 ILE 158 158 158 ILE ILE B . n 
B 1 159 PHE 159 159 159 PHE PHE B . n 
B 1 160 SER 160 160 160 SER SER B . n 
B 1 161 HIS 161 161 161 HIS HIS B . n 
B 1 162 LEU 162 162 162 LEU LEU B . n 
B 1 163 GLN 163 163 163 GLN GLN B . n 
B 1 164 HIS 164 164 164 HIS HIS B . n 
B 1 165 VAL 165 165 165 VAL VAL B . n 
B 1 166 LYS 166 166 166 LYS LYS B . n 
B 1 167 TYR 167 167 167 TYR TYR B . n 
B 1 168 LYS 168 168 168 LYS LYS B . n 
B 1 169 GLY 169 169 169 GLY GLY B . n 
B 1 170 GLN 170 170 170 GLN GLN B . n 
B 1 171 GLU 171 171 171 GLU GLU B . n 
B 1 172 ALA 172 172 172 ALA ALA B . n 
B 1 173 PHE 173 173 173 PHE PHE B . n 
B 1 174 VAL 174 174 174 VAL VAL B . n 
B 1 175 PRO 175 175 175 PRO PRO B . n 
B 1 176 GLY 176 176 176 GLY GLY B . n 
B 1 177 PHE 177 177 177 PHE PHE B . n 
B 1 178 ASN 178 178 178 ASN ASN B . n 
B 1 179 ILE 179 179 179 ILE ILE B . n 
B 1 180 GLU 180 180 180 GLU GLU B . n 
B 1 181 GLU 181 181 181 GLU GLU B . n 
B 1 182 LEU 182 182 182 LEU LEU B . n 
B 1 183 LEU 183 183 183 LEU LEU B . n 
B 1 184 PRO 184 184 184 PRO PRO B . n 
B 1 185 GLU 185 185 185 GLU GLU B . n 
B 1 186 ARG 186 186 186 ARG ARG B . n 
B 1 187 THR 187 187 187 THR THR B . n 
B 1 188 ALA 188 188 188 ALA ALA B . n 
B 1 189 GLU 189 189 189 GLU GLU B . n 
B 1 190 TYR 190 190 190 TYR TYR B . n 
B 1 191 TYR 191 191 191 TYR TYR B . n 
B 1 192 ARG 192 192 192 ARG ARG B . n 
B 1 193 TYR 193 193 193 TYR TYR B . n 
B 1 194 ARG 194 194 194 ARG ARG B . n 
B 1 195 GLY 195 195 195 GLY GLY B . n 
B 1 196 SER 196 196 196 SER SER B . n 
B 1 197 LEU 197 197 197 LEU LEU B . n 
B 1 198 THR 198 198 198 THR THR B . n 
B 1 199 THR 199 199 199 THR THR B . n 
B 1 200 PRO 200 200 200 PRO PRO B . n 
B 1 201 PRO 201 201 201 PRO PRO B . n 
B 1 202 CYS 202 202 202 CYS CYS B . n 
B 1 203 ASN 203 203 203 ASN ASN B . n 
B 1 204 PRO 204 204 204 PRO PRO B . n 
B 1 205 THR 205 205 205 THR THR B . n 
B 1 206 VAL 206 206 206 VAL VAL B . n 
B 1 207 LEU 207 207 207 LEU LEU B . n 
B 1 208 TRP 208 208 208 TRP TRP B . n 
B 1 209 THR 209 209 209 THR THR B . n 
B 1 210 VAL 210 210 210 VAL VAL B . n 
B 1 211 PHE 211 211 211 PHE PHE B . n 
B 1 212 ARG 212 212 212 ARG ARG B . n 
B 1 213 ASN 213 213 213 ASN ASN B . n 
B 1 214 PRO 214 214 214 PRO PRO B . n 
B 1 215 VAL 215 215 215 VAL VAL B . n 
B 1 216 GLN 216 216 216 GLN GLN B . n 
B 1 217 ILE 217 217 217 ILE ILE B . n 
B 1 218 SER 218 218 218 SER SER B . n 
B 1 219 GLN 219 219 219 GLN GLN B . n 
B 1 220 GLU 220 220 220 GLU GLU B . n 
B 1 221 GLN 221 221 221 GLN GLN B . n 
B 1 222 LEU 222 222 222 LEU LEU B . n 
B 1 223 LEU 223 223 223 LEU LEU B . n 
B 1 224 ALA 224 224 224 ALA ALA B . n 
B 1 225 LEU 225 225 225 LEU LEU B . n 
B 1 226 GLU 226 226 226 GLU GLU B . n 
B 1 227 THR 227 227 227 THR THR B . n 
B 1 228 ALA 228 228 228 ALA ALA B . n 
B 1 229 LEU 229 229 229 LEU LEU B . n 
B 1 230 TYR 230 230 230 TYR TYR B . n 
B 1 231 CYS 231 231 231 CYS CYS B . n 
B 1 232 THR 232 232 232 THR THR B . n 
B 1 233 HIS 233 233 233 HIS HIS B . n 
B 1 234 MET 234 234 234 MET MET B . n 
B 1 235 ASP 235 235 235 ASP ASP B . n 
B 1 236 ASP 236 236 236 ASP ASP B . n 
B 1 237 PRO 237 237 237 PRO PRO B . n 
B 1 238 SER 238 238 238 SER SER B . n 
B 1 239 PRO 239 239 239 PRO PRO B . n 
B 1 240 ARG 240 240 240 ARG ARG B . n 
B 1 241 GLU 241 241 241 GLU GLU B . n 
B 1 242 MET 242 242 242 MET MET B . n 
B 1 243 ILE 243 243 243 ILE ILE B . n 
B 1 244 ASN 244 244 244 ASN ASN B . n 
B 1 245 ASN 245 245 245 ASN ASN B . n 
B 1 246 PHE 246 246 246 PHE PHE B . n 
B 1 247 ARG 247 247 247 ARG ARG B . n 
B 1 248 GLN 248 248 248 GLN GLN B . n 
B 1 249 VAL 249 249 249 VAL VAL B . n 
B 1 250 GLN 250 250 250 GLN GLN B . n 
B 1 251 LYS 251 251 251 LYS LYS B . n 
B 1 252 PHE 252 252 252 PHE PHE B . n 
B 1 253 ASP 253 253 253 ASP ASP B . n 
B 1 254 GLU 254 254 254 GLU GLU B . n 
B 1 255 ARG 255 255 255 ARG ARG B . n 
B 1 256 LEU 256 256 256 LEU LEU B . n 
B 1 257 VAL 257 257 257 VAL VAL B . n 
B 1 258 TYR 258 258 258 TYR TYR B . n 
B 1 259 THR 259 259 259 THR THR B . n 
B 1 260 SER 260 260 260 SER SER B . n 
B 1 261 PHE 261 261 261 PHE PHE B . n 
B 1 262 SER 262 262 262 SER SER B . n 
B 1 263 GLN 263 263 263 GLN GLN B . n 
C 1 1   MET 1   1   ?   ?   ?   C . n 
C 1 2   SER 2   2   ?   ?   ?   C . n 
C 1 3   LYS 3   3   3   LYS LYS C . n 
C 1 4   TRP 4   4   4   TRP TRP C . n 
C 1 5   THR 5   5   5   THR THR C . n 
C 1 6   TYR 6   6   6   TYR TYR C . n 
C 1 7   PHE 7   7   7   PHE PHE C . n 
C 1 8   GLY 8   8   8   GLY GLY C . n 
C 1 9   PRO 9   9   9   PRO PRO C . n 
C 1 10  ASP 10  10  10  ASP ASP C . n 
C 1 11  GLY 11  11  11  GLY GLY C . n 
C 1 12  GLU 12  12  12  GLU GLU C . n 
C 1 13  ASN 13  13  13  ASN ASN C . n 
C 1 14  SER 14  14  14  SER SER C . n 
C 1 15  TRP 15  15  15  TRP TRP C . n 
C 1 16  SER 16  16  16  SER SER C . n 
C 1 17  LYS 17  17  17  LYS LYS C . n 
C 1 18  LYS 18  18  18  LYS LYS C . n 
C 1 19  TYR 19  19  19  TYR TYR C . n 
C 1 20  PRO 20  20  20  PRO PRO C . n 
C 1 21  SER 21  21  21  SER SER C . n 
C 1 22  CYS 22  22  22  CYS CYS C . n 
C 1 23  GLY 23  23  23  GLY GLY C . n 
C 1 24  GLY 24  24  24  GLY GLY C . n 
C 1 25  LEU 25  25  25  LEU LEU C . n 
C 1 26  LEU 26  26  26  LEU LEU C . n 
C 1 27  GLN 27  27  27  GLN GLN C . n 
C 1 28  SER 28  28  28  SER SER C . n 
C 1 29  PRO 29  29  29  PRO PRO C . n 
C 1 30  ILE 30  30  30  ILE ILE C . n 
C 1 31  ASP 31  31  31  ASP ASP C . n 
C 1 32  LEU 32  32  32  LEU LEU C . n 
C 1 33  HIS 33  33  33  HIS HIS C . n 
C 1 34  SER 34  34  34  SER SER C . n 
C 1 35  ASP 35  35  35  ASP ASP C . n 
C 1 36  ILE 36  36  36  ILE ILE C . n 
C 1 37  LEU 37  37  37  LEU LEU C . n 
C 1 38  GLN 38  38  38  GLN GLN C . n 
C 1 39  TYR 39  39  39  TYR TYR C . n 
C 1 40  ASP 40  40  40  ASP ASP C . n 
C 1 41  ALA 41  41  41  ALA ALA C . n 
C 1 42  SER 42  42  42  SER SER C . n 
C 1 43  LEU 43  43  43  LEU LEU C . n 
C 1 44  THR 44  44  44  THR THR C . n 
C 1 45  PRO 45  45  45  PRO PRO C . n 
C 1 46  LEU 46  46  46  LEU LEU C . n 
C 1 47  GLU 47  47  47  GLU GLU C . n 
C 1 48  PHE 48  48  48  PHE PHE C . n 
C 1 49  GLN 49  49  49  GLN GLN C . n 
C 1 50  GLY 50  50  50  GLY GLY C . n 
C 1 51  TYR 51  51  51  TYR TYR C . n 
C 1 52  ASN 52  52  52  ASN ASN C . n 
C 1 53  LEU 53  53  53  LEU LEU C . n 
C 1 54  SER 54  54  54  SER SER C . n 
C 1 55  ALA 55  55  55  ALA ALA C . n 
C 1 56  ASN 56  56  56  ASN ASN C . n 
C 1 57  LYS 57  57  57  LYS LYS C . n 
C 1 58  GLN 58  58  58  GLN GLN C . n 
C 1 59  PHE 59  59  59  PHE PHE C . n 
C 1 60  LEU 60  60  60  LEU LEU C . n 
C 1 61  LEU 61  61  61  LEU LEU C . n 
C 1 62  THR 62  62  62  THR THR C . n 
C 1 63  ASN 63  63  63  ASN ASN C . n 
C 1 64  ASN 64  64  64  ASN ASN C . n 
C 1 65  GLY 65  65  65  GLY GLY C . n 
C 1 66  HIS 66  66  66  HIS HIS C . n 
C 1 67  SER 67  67  67  SER SER C . n 
C 1 68  VAL 68  68  68  VAL VAL C . n 
C 1 69  LYS 69  69  69  LYS LYS C . n 
C 1 70  LEU 70  70  70  LEU LEU C . n 
C 1 71  ASN 71  71  71  ASN ASN C . n 
C 1 72  LEU 72  72  72  LEU LEU C . n 
C 1 73  PRO 73  73  73  PRO PRO C . n 
C 1 74  SER 74  74  74  SER SER C . n 
C 1 75  ASP 75  75  75  ASP ASP C . n 
C 1 76  MET 76  76  76  MET MET C . n 
C 1 77  HIS 77  77  77  HIS HIS C . n 
C 1 78  ILE 78  78  78  ILE ILE C . n 
C 1 79  GLN 79  79  79  GLN GLN C . n 
C 1 80  GLY 80  80  80  GLY GLY C . n 
C 1 81  LEU 81  81  81  LEU LEU C . n 
C 1 82  GLN 82  82  82  GLN GLN C . n 
C 1 83  SER 83  83  83  SER SER C . n 
C 1 84  ARG 84  84  84  ARG ARG C . n 
C 1 85  TYR 85  85  85  TYR TYR C . n 
C 1 86  SER 86  86  86  SER SER C . n 
C 1 87  ALA 87  87  87  ALA ALA C . n 
C 1 88  THR 88  88  88  THR THR C . n 
C 1 89  GLN 89  89  89  GLN GLN C . n 
C 1 90  LEU 90  90  90  LEU LEU C . n 
C 1 91  HIS 91  91  91  HIS HIS C . n 
C 1 92  LEU 92  92  92  LEU LEU C . n 
C 1 93  HIS 93  93  93  HIS HIS C . n 
C 1 94  TRP 94  94  94  TRP TRP C . n 
C 1 95  GLY 95  95  95  GLY GLY C . n 
C 1 96  ASN 96  96  96  ASN ASN C . n 
C 1 97  PRO 97  97  97  PRO PRO C . n 
C 1 98  ASN 98  98  98  ASN ASN C . n 
C 1 99  ASP 99  99  99  ASP ASP C . n 
C 1 100 PRO 100 100 100 PRO PRO C . n 
C 1 101 HIS 101 101 101 HIS HIS C . n 
C 1 102 GLY 102 102 102 GLY GLY C . n 
C 1 103 SER 103 103 103 SER SER C . n 
C 1 104 GLU 104 104 104 GLU GLU C . n 
C 1 105 HIS 105 105 105 HIS HIS C . n 
C 1 106 THR 106 106 106 THR THR C . n 
C 1 107 VAL 107 107 107 VAL VAL C . n 
C 1 108 SER 108 108 108 SER SER C . n 
C 1 109 GLY 109 109 109 GLY GLY C . n 
C 1 110 GLN 110 110 110 GLN GLN C . n 
C 1 111 HIS 111 111 111 HIS HIS C . n 
C 1 112 PHE 112 112 112 PHE PHE C . n 
C 1 113 ALA 113 113 113 ALA ALA C . n 
C 1 114 ALA 114 114 114 ALA ALA C . n 
C 1 115 GLU 115 115 115 GLU GLU C . n 
C 1 116 LEU 116 116 116 LEU LEU C . n 
C 1 117 HIS 117 117 117 HIS HIS C . n 
C 1 118 ILE 118 118 118 ILE ILE C . n 
C 1 119 VAL 119 119 119 VAL VAL C . n 
C 1 120 HIS 120 120 120 HIS HIS C . n 
C 1 121 TYR 121 121 121 TYR TYR C . n 
C 1 122 ASN 122 122 122 ASN ASN C . n 
C 1 123 SER 123 123 123 SER SER C . n 
C 1 124 ASP 124 124 124 ASP ASP C . n 
C 1 125 LEU 125 125 125 LEU LEU C . n 
C 1 126 TYR 126 126 126 TYR TYR C . n 
C 1 127 PRO 127 127 127 PRO PRO C . n 
C 1 128 ASP 128 128 128 ASP ASP C . n 
C 1 129 ALA 129 129 129 ALA ALA C . n 
C 1 130 SER 130 130 130 SER SER C . n 
C 1 131 THR 131 131 131 THR THR C . n 
C 1 132 ALA 132 132 132 ALA ALA C . n 
C 1 133 SER 133 133 133 SER SER C . n 
C 1 134 ASN 134 134 134 ASN ASN C . n 
C 1 135 LYS 135 135 135 LYS LYS C . n 
C 1 136 SER 136 136 136 SER SER C . n 
C 1 137 GLU 137 137 137 GLU GLU C . n 
C 1 138 GLY 138 138 138 GLY GLY C . n 
C 1 139 LEU 139 139 139 LEU LEU C . n 
C 1 140 ALA 140 140 140 ALA ALA C . n 
C 1 141 VAL 141 141 141 VAL VAL C . n 
C 1 142 LEU 142 142 142 LEU LEU C . n 
C 1 143 ALA 143 143 143 ALA ALA C . n 
C 1 144 VAL 144 144 144 VAL VAL C . n 
C 1 145 LEU 145 145 145 LEU LEU C . n 
C 1 146 ILE 146 146 146 ILE ILE C . n 
C 1 147 GLU 147 147 147 GLU GLU C . n 
C 1 148 MET 148 148 148 MET MET C . n 
C 1 149 GLY 149 149 149 GLY GLY C . n 
C 1 150 SER 150 150 150 SER SER C . n 
C 1 151 PHE 151 151 151 PHE PHE C . n 
C 1 152 ASN 152 152 152 ASN ASN C . n 
C 1 153 PRO 153 153 153 PRO PRO C . n 
C 1 154 SER 154 154 154 SER SER C . n 
C 1 155 TYR 155 155 155 TYR TYR C . n 
C 1 156 ASP 156 156 156 ASP ASP C . n 
C 1 157 LYS 157 157 157 LYS LYS C . n 
C 1 158 ILE 158 158 158 ILE ILE C . n 
C 1 159 PHE 159 159 159 PHE PHE C . n 
C 1 160 SER 160 160 160 SER SER C . n 
C 1 161 HIS 161 161 161 HIS HIS C . n 
C 1 162 LEU 162 162 162 LEU LEU C . n 
C 1 163 GLN 163 163 163 GLN GLN C . n 
C 1 164 HIS 164 164 164 HIS HIS C . n 
C 1 165 VAL 165 165 165 VAL VAL C . n 
C 1 166 LYS 166 166 166 LYS LYS C . n 
C 1 167 TYR 167 167 167 TYR TYR C . n 
C 1 168 LYS 168 168 168 LYS LYS C . n 
C 1 169 GLY 169 169 169 GLY GLY C . n 
C 1 170 GLN 170 170 170 GLN GLN C . n 
C 1 171 GLU 171 171 171 GLU GLU C . n 
C 1 172 ALA 172 172 172 ALA ALA C . n 
C 1 173 PHE 173 173 173 PHE PHE C . n 
C 1 174 VAL 174 174 174 VAL VAL C . n 
C 1 175 PRO 175 175 175 PRO PRO C . n 
C 1 176 GLY 176 176 176 GLY GLY C . n 
C 1 177 PHE 177 177 177 PHE PHE C . n 
C 1 178 ASN 178 178 178 ASN ASN C . n 
C 1 179 ILE 179 179 179 ILE ILE C . n 
C 1 180 GLU 180 180 180 GLU GLU C . n 
C 1 181 GLU 181 181 181 GLU GLU C . n 
C 1 182 LEU 182 182 182 LEU LEU C . n 
C 1 183 LEU 183 183 183 LEU LEU C . n 
C 1 184 PRO 184 184 184 PRO PRO C . n 
C 1 185 GLU 185 185 185 GLU GLU C . n 
C 1 186 ARG 186 186 186 ARG ARG C . n 
C 1 187 THR 187 187 187 THR THR C . n 
C 1 188 ALA 188 188 188 ALA ALA C . n 
C 1 189 GLU 189 189 189 GLU GLU C . n 
C 1 190 TYR 190 190 190 TYR TYR C . n 
C 1 191 TYR 191 191 191 TYR TYR C . n 
C 1 192 ARG 192 192 192 ARG ARG C . n 
C 1 193 TYR 193 193 193 TYR TYR C . n 
C 1 194 ARG 194 194 194 ARG ARG C . n 
C 1 195 GLY 195 195 195 GLY GLY C . n 
C 1 196 SER 196 196 196 SER SER C . n 
C 1 197 LEU 197 197 197 LEU LEU C . n 
C 1 198 THR 198 198 198 THR THR C . n 
C 1 199 THR 199 199 199 THR THR C . n 
C 1 200 PRO 200 200 200 PRO PRO C . n 
C 1 201 PRO 201 201 201 PRO PRO C . n 
C 1 202 CYS 202 202 202 CYS CYS C . n 
C 1 203 ASN 203 203 203 ASN ASN C . n 
C 1 204 PRO 204 204 204 PRO PRO C . n 
C 1 205 THR 205 205 205 THR THR C . n 
C 1 206 VAL 206 206 206 VAL VAL C . n 
C 1 207 LEU 207 207 207 LEU LEU C . n 
C 1 208 TRP 208 208 208 TRP TRP C . n 
C 1 209 THR 209 209 209 THR THR C . n 
C 1 210 VAL 210 210 210 VAL VAL C . n 
C 1 211 PHE 211 211 211 PHE PHE C . n 
C 1 212 ARG 212 212 212 ARG ARG C . n 
C 1 213 ASN 213 213 213 ASN ASN C . n 
C 1 214 PRO 214 214 214 PRO PRO C . n 
C 1 215 VAL 215 215 215 VAL VAL C . n 
C 1 216 GLN 216 216 216 GLN GLN C . n 
C 1 217 ILE 217 217 217 ILE ILE C . n 
C 1 218 SER 218 218 218 SER SER C . n 
C 1 219 GLN 219 219 219 GLN GLN C . n 
C 1 220 GLU 220 220 220 GLU GLU C . n 
C 1 221 GLN 221 221 221 GLN GLN C . n 
C 1 222 LEU 222 222 222 LEU LEU C . n 
C 1 223 LEU 223 223 223 LEU LEU C . n 
C 1 224 ALA 224 224 224 ALA ALA C . n 
C 1 225 LEU 225 225 225 LEU LEU C . n 
C 1 226 GLU 226 226 226 GLU GLU C . n 
C 1 227 THR 227 227 227 THR THR C . n 
C 1 228 ALA 228 228 228 ALA ALA C . n 
C 1 229 LEU 229 229 229 LEU LEU C . n 
C 1 230 TYR 230 230 230 TYR TYR C . n 
C 1 231 CYS 231 231 231 CYS CYS C . n 
C 1 232 THR 232 232 232 THR THR C . n 
C 1 233 HIS 233 233 233 HIS HIS C . n 
C 1 234 MET 234 234 234 MET MET C . n 
C 1 235 ASP 235 235 235 ASP ASP C . n 
C 1 236 ASP 236 236 236 ASP ASP C . n 
C 1 237 PRO 237 237 237 PRO PRO C . n 
C 1 238 SER 238 238 238 SER SER C . n 
C 1 239 PRO 239 239 239 PRO PRO C . n 
C 1 240 ARG 240 240 240 ARG ARG C . n 
C 1 241 GLU 241 241 241 GLU GLU C . n 
C 1 242 MET 242 242 242 MET MET C . n 
C 1 243 ILE 243 243 243 ILE ILE C . n 
C 1 244 ASN 244 244 244 ASN ASN C . n 
C 1 245 ASN 245 245 245 ASN ASN C . n 
C 1 246 PHE 246 246 246 PHE PHE C . n 
C 1 247 ARG 247 247 247 ARG ARG C . n 
C 1 248 GLN 248 248 248 GLN GLN C . n 
C 1 249 VAL 249 249 249 VAL VAL C . n 
C 1 250 GLN 250 250 250 GLN GLN C . n 
C 1 251 LYS 251 251 251 LYS LYS C . n 
C 1 252 PHE 252 252 252 PHE PHE C . n 
C 1 253 ASP 253 253 253 ASP ASP C . n 
C 1 254 GLU 254 254 254 GLU GLU C . n 
C 1 255 ARG 255 255 255 ARG ARG C . n 
C 1 256 LEU 256 256 256 LEU LEU C . n 
C 1 257 VAL 257 257 257 VAL VAL C . n 
C 1 258 TYR 258 258 258 TYR TYR C . n 
C 1 259 THR 259 259 259 THR THR C . n 
C 1 260 SER 260 260 260 SER SER C . n 
C 1 261 PHE 261 261 261 PHE PHE C . n 
C 1 262 SER 262 262 262 SER SER C . n 
C 1 263 GLN 263 263 263 GLN GLN C . n 
D 1 1   MET 1   1   ?   ?   ?   D . n 
D 1 2   SER 2   2   ?   ?   ?   D . n 
D 1 3   LYS 3   3   3   LYS LYS D . n 
D 1 4   TRP 4   4   4   TRP TRP D . n 
D 1 5   THR 5   5   5   THR THR D . n 
D 1 6   TYR 6   6   6   TYR TYR D . n 
D 1 7   PHE 7   7   7   PHE PHE D . n 
D 1 8   GLY 8   8   8   GLY GLY D . n 
D 1 9   PRO 9   9   9   PRO PRO D . n 
D 1 10  ASP 10  10  10  ASP ASP D . n 
D 1 11  GLY 11  11  11  GLY GLY D . n 
D 1 12  GLU 12  12  12  GLU GLU D . n 
D 1 13  ASN 13  13  13  ASN ASN D . n 
D 1 14  SER 14  14  14  SER SER D . n 
D 1 15  TRP 15  15  15  TRP TRP D . n 
D 1 16  SER 16  16  16  SER SER D . n 
D 1 17  LYS 17  17  17  LYS LYS D . n 
D 1 18  LYS 18  18  18  LYS LYS D . n 
D 1 19  TYR 19  19  19  TYR TYR D . n 
D 1 20  PRO 20  20  20  PRO PRO D . n 
D 1 21  SER 21  21  21  SER SER D . n 
D 1 22  CYS 22  22  22  CYS CYS D . n 
D 1 23  GLY 23  23  23  GLY GLY D . n 
D 1 24  GLY 24  24  24  GLY GLY D . n 
D 1 25  LEU 25  25  25  LEU LEU D . n 
D 1 26  LEU 26  26  26  LEU LEU D . n 
D 1 27  GLN 27  27  27  GLN GLN D . n 
D 1 28  SER 28  28  28  SER SER D . n 
D 1 29  PRO 29  29  29  PRO PRO D . n 
D 1 30  ILE 30  30  30  ILE ILE D . n 
D 1 31  ASP 31  31  31  ASP ASP D . n 
D 1 32  LEU 32  32  32  LEU LEU D . n 
D 1 33  HIS 33  33  33  HIS HIS D . n 
D 1 34  SER 34  34  34  SER SER D . n 
D 1 35  ASP 35  35  35  ASP ASP D . n 
D 1 36  ILE 36  36  36  ILE ILE D . n 
D 1 37  LEU 37  37  37  LEU LEU D . n 
D 1 38  GLN 38  38  38  GLN GLN D . n 
D 1 39  TYR 39  39  39  TYR TYR D . n 
D 1 40  ASP 40  40  40  ASP ASP D . n 
D 1 41  ALA 41  41  41  ALA ALA D . n 
D 1 42  SER 42  42  42  SER SER D . n 
D 1 43  LEU 43  43  43  LEU LEU D . n 
D 1 44  THR 44  44  44  THR THR D . n 
D 1 45  PRO 45  45  45  PRO PRO D . n 
D 1 46  LEU 46  46  46  LEU LEU D . n 
D 1 47  GLU 47  47  47  GLU GLU D . n 
D 1 48  PHE 48  48  48  PHE PHE D . n 
D 1 49  GLN 49  49  49  GLN GLN D . n 
D 1 50  GLY 50  50  50  GLY GLY D . n 
D 1 51  TYR 51  51  51  TYR TYR D . n 
D 1 52  ASN 52  52  52  ASN ASN D . n 
D 1 53  LEU 53  53  53  LEU LEU D . n 
D 1 54  SER 54  54  54  SER SER D . n 
D 1 55  ALA 55  55  55  ALA ALA D . n 
D 1 56  ASN 56  56  56  ASN ASN D . n 
D 1 57  LYS 57  57  57  LYS LYS D . n 
D 1 58  GLN 58  58  58  GLN GLN D . n 
D 1 59  PHE 59  59  59  PHE PHE D . n 
D 1 60  LEU 60  60  60  LEU LEU D . n 
D 1 61  LEU 61  61  61  LEU LEU D . n 
D 1 62  THR 62  62  62  THR THR D . n 
D 1 63  ASN 63  63  63  ASN ASN D . n 
D 1 64  ASN 64  64  64  ASN ASN D . n 
D 1 65  GLY 65  65  65  GLY GLY D . n 
D 1 66  HIS 66  66  66  HIS HIS D . n 
D 1 67  SER 67  67  67  SER SER D . n 
D 1 68  VAL 68  68  68  VAL VAL D . n 
D 1 69  LYS 69  69  69  LYS LYS D . n 
D 1 70  LEU 70  70  70  LEU LEU D . n 
D 1 71  ASN 71  71  71  ASN ASN D . n 
D 1 72  LEU 72  72  72  LEU LEU D . n 
D 1 73  PRO 73  73  73  PRO PRO D . n 
D 1 74  SER 74  74  74  SER SER D . n 
D 1 75  ASP 75  75  75  ASP ASP D . n 
D 1 76  MET 76  76  76  MET MET D . n 
D 1 77  HIS 77  77  77  HIS HIS D . n 
D 1 78  ILE 78  78  78  ILE ILE D . n 
D 1 79  GLN 79  79  79  GLN GLN D . n 
D 1 80  GLY 80  80  80  GLY GLY D . n 
D 1 81  LEU 81  81  81  LEU LEU D . n 
D 1 82  GLN 82  82  82  GLN GLN D . n 
D 1 83  SER 83  83  83  SER SER D . n 
D 1 84  ARG 84  84  84  ARG ARG D . n 
D 1 85  TYR 85  85  85  TYR TYR D . n 
D 1 86  SER 86  86  86  SER SER D . n 
D 1 87  ALA 87  87  87  ALA ALA D . n 
D 1 88  THR 88  88  88  THR THR D . n 
D 1 89  GLN 89  89  89  GLN GLN D . n 
D 1 90  LEU 90  90  90  LEU LEU D . n 
D 1 91  HIS 91  91  91  HIS HIS D . n 
D 1 92  LEU 92  92  92  LEU LEU D . n 
D 1 93  HIS 93  93  93  HIS HIS D . n 
D 1 94  TRP 94  94  94  TRP TRP D . n 
D 1 95  GLY 95  95  95  GLY GLY D . n 
D 1 96  ASN 96  96  96  ASN ASN D . n 
D 1 97  PRO 97  97  97  PRO PRO D . n 
D 1 98  ASN 98  98  98  ASN ASN D . n 
D 1 99  ASP 99  99  99  ASP ASP D . n 
D 1 100 PRO 100 100 100 PRO PRO D . n 
D 1 101 HIS 101 101 101 HIS HIS D . n 
D 1 102 GLY 102 102 102 GLY GLY D . n 
D 1 103 SER 103 103 103 SER SER D . n 
D 1 104 GLU 104 104 104 GLU GLU D . n 
D 1 105 HIS 105 105 105 HIS HIS D . n 
D 1 106 THR 106 106 106 THR THR D . n 
D 1 107 VAL 107 107 107 VAL VAL D . n 
D 1 108 SER 108 108 108 SER SER D . n 
D 1 109 GLY 109 109 109 GLY GLY D . n 
D 1 110 GLN 110 110 110 GLN GLN D . n 
D 1 111 HIS 111 111 111 HIS HIS D . n 
D 1 112 PHE 112 112 112 PHE PHE D . n 
D 1 113 ALA 113 113 113 ALA ALA D . n 
D 1 114 ALA 114 114 114 ALA ALA D . n 
D 1 115 GLU 115 115 115 GLU GLU D . n 
D 1 116 LEU 116 116 116 LEU LEU D . n 
D 1 117 HIS 117 117 117 HIS HIS D . n 
D 1 118 ILE 118 118 118 ILE ILE D . n 
D 1 119 VAL 119 119 119 VAL VAL D . n 
D 1 120 HIS 120 120 120 HIS HIS D . n 
D 1 121 TYR 121 121 121 TYR TYR D . n 
D 1 122 ASN 122 122 122 ASN ASN D . n 
D 1 123 SER 123 123 123 SER SER D . n 
D 1 124 ASP 124 124 124 ASP ASP D . n 
D 1 125 LEU 125 125 125 LEU LEU D . n 
D 1 126 TYR 126 126 126 TYR TYR D . n 
D 1 127 PRO 127 127 127 PRO PRO D . n 
D 1 128 ASP 128 128 128 ASP ASP D . n 
D 1 129 ALA 129 129 129 ALA ALA D . n 
D 1 130 SER 130 130 130 SER SER D . n 
D 1 131 THR 131 131 131 THR THR D . n 
D 1 132 ALA 132 132 132 ALA ALA D . n 
D 1 133 SER 133 133 133 SER SER D . n 
D 1 134 ASN 134 134 134 ASN ASN D . n 
D 1 135 LYS 135 135 135 LYS LYS D . n 
D 1 136 SER 136 136 136 SER SER D . n 
D 1 137 GLU 137 137 137 GLU GLU D . n 
D 1 138 GLY 138 138 138 GLY GLY D . n 
D 1 139 LEU 139 139 139 LEU LEU D . n 
D 1 140 ALA 140 140 140 ALA ALA D . n 
D 1 141 VAL 141 141 141 VAL VAL D . n 
D 1 142 LEU 142 142 142 LEU LEU D . n 
D 1 143 ALA 143 143 143 ALA ALA D . n 
D 1 144 VAL 144 144 144 VAL VAL D . n 
D 1 145 LEU 145 145 145 LEU LEU D . n 
D 1 146 ILE 146 146 146 ILE ILE D . n 
D 1 147 GLU 147 147 147 GLU GLU D . n 
D 1 148 MET 148 148 148 MET MET D . n 
D 1 149 GLY 149 149 149 GLY GLY D . n 
D 1 150 SER 150 150 150 SER SER D . n 
D 1 151 PHE 151 151 151 PHE PHE D . n 
D 1 152 ASN 152 152 152 ASN ASN D . n 
D 1 153 PRO 153 153 153 PRO PRO D . n 
D 1 154 SER 154 154 154 SER SER D . n 
D 1 155 TYR 155 155 155 TYR TYR D . n 
D 1 156 ASP 156 156 156 ASP ASP D . n 
D 1 157 LYS 157 157 157 LYS LYS D . n 
D 1 158 ILE 158 158 158 ILE ILE D . n 
D 1 159 PHE 159 159 159 PHE PHE D . n 
D 1 160 SER 160 160 160 SER SER D . n 
D 1 161 HIS 161 161 161 HIS HIS D . n 
D 1 162 LEU 162 162 162 LEU LEU D . n 
D 1 163 GLN 163 163 163 GLN GLN D . n 
D 1 164 HIS 164 164 164 HIS HIS D . n 
D 1 165 VAL 165 165 165 VAL VAL D . n 
D 1 166 LYS 166 166 166 LYS LYS D . n 
D 1 167 TYR 167 167 167 TYR TYR D . n 
D 1 168 LYS 168 168 168 LYS LYS D . n 
D 1 169 GLY 169 169 169 GLY GLY D . n 
D 1 170 GLN 170 170 170 GLN GLN D . n 
D 1 171 GLU 171 171 171 GLU GLU D . n 
D 1 172 ALA 172 172 172 ALA ALA D . n 
D 1 173 PHE 173 173 173 PHE PHE D . n 
D 1 174 VAL 174 174 174 VAL VAL D . n 
D 1 175 PRO 175 175 175 PRO PRO D . n 
D 1 176 GLY 176 176 176 GLY GLY D . n 
D 1 177 PHE 177 177 177 PHE PHE D . n 
D 1 178 ASN 178 178 178 ASN ASN D . n 
D 1 179 ILE 179 179 179 ILE ILE D . n 
D 1 180 GLU 180 180 180 GLU GLU D . n 
D 1 181 GLU 181 181 181 GLU GLU D . n 
D 1 182 LEU 182 182 182 LEU LEU D . n 
D 1 183 LEU 183 183 183 LEU LEU D . n 
D 1 184 PRO 184 184 184 PRO PRO D . n 
D 1 185 GLU 185 185 185 GLU GLU D . n 
D 1 186 ARG 186 186 186 ARG ARG D . n 
D 1 187 THR 187 187 187 THR THR D . n 
D 1 188 ALA 188 188 188 ALA ALA D . n 
D 1 189 GLU 189 189 189 GLU GLU D . n 
D 1 190 TYR 190 190 190 TYR TYR D . n 
D 1 191 TYR 191 191 191 TYR TYR D . n 
D 1 192 ARG 192 192 192 ARG ARG D . n 
D 1 193 TYR 193 193 193 TYR TYR D . n 
D 1 194 ARG 194 194 194 ARG ARG D . n 
D 1 195 GLY 195 195 195 GLY GLY D . n 
D 1 196 SER 196 196 196 SER SER D . n 
D 1 197 LEU 197 197 197 LEU LEU D . n 
D 1 198 THR 198 198 198 THR THR D . n 
D 1 199 THR 199 199 199 THR THR D . n 
D 1 200 PRO 200 200 200 PRO PRO D . n 
D 1 201 PRO 201 201 201 PRO PRO D . n 
D 1 202 CYS 202 202 202 CYS CYS D . n 
D 1 203 ASN 203 203 203 ASN ASN D . n 
D 1 204 PRO 204 204 204 PRO PRO D . n 
D 1 205 THR 205 205 205 THR THR D . n 
D 1 206 VAL 206 206 206 VAL VAL D . n 
D 1 207 LEU 207 207 207 LEU LEU D . n 
D 1 208 TRP 208 208 208 TRP TRP D . n 
D 1 209 THR 209 209 209 THR THR D . n 
D 1 210 VAL 210 210 210 VAL VAL D . n 
D 1 211 PHE 211 211 211 PHE PHE D . n 
D 1 212 ARG 212 212 212 ARG ARG D . n 
D 1 213 ASN 213 213 213 ASN ASN D . n 
D 1 214 PRO 214 214 214 PRO PRO D . n 
D 1 215 VAL 215 215 215 VAL VAL D . n 
D 1 216 GLN 216 216 216 GLN GLN D . n 
D 1 217 ILE 217 217 217 ILE ILE D . n 
D 1 218 SER 218 218 218 SER SER D . n 
D 1 219 GLN 219 219 219 GLN GLN D . n 
D 1 220 GLU 220 220 220 GLU GLU D . n 
D 1 221 GLN 221 221 221 GLN GLN D . n 
D 1 222 LEU 222 222 222 LEU LEU D . n 
D 1 223 LEU 223 223 223 LEU LEU D . n 
D 1 224 ALA 224 224 224 ALA ALA D . n 
D 1 225 LEU 225 225 225 LEU LEU D . n 
D 1 226 GLU 226 226 226 GLU GLU D . n 
D 1 227 THR 227 227 227 THR THR D . n 
D 1 228 ALA 228 228 228 ALA ALA D . n 
D 1 229 LEU 229 229 229 LEU LEU D . n 
D 1 230 TYR 230 230 230 TYR TYR D . n 
D 1 231 CYS 231 231 231 CYS CYS D . n 
D 1 232 THR 232 232 232 THR THR D . n 
D 1 233 HIS 233 233 233 HIS HIS D . n 
D 1 234 MET 234 234 234 MET MET D . n 
D 1 235 ASP 235 235 235 ASP ASP D . n 
D 1 236 ASP 236 236 236 ASP ASP D . n 
D 1 237 PRO 237 237 237 PRO PRO D . n 
D 1 238 SER 238 238 238 SER SER D . n 
D 1 239 PRO 239 239 239 PRO PRO D . n 
D 1 240 ARG 240 240 240 ARG ARG D . n 
D 1 241 GLU 241 241 241 GLU GLU D . n 
D 1 242 MET 242 242 242 MET MET D . n 
D 1 243 ILE 243 243 243 ILE ILE D . n 
D 1 244 ASN 244 244 244 ASN ASN D . n 
D 1 245 ASN 245 245 245 ASN ASN D . n 
D 1 246 PHE 246 246 246 PHE PHE D . n 
D 1 247 ARG 247 247 247 ARG ARG D . n 
D 1 248 GLN 248 248 248 GLN GLN D . n 
D 1 249 VAL 249 249 249 VAL VAL D . n 
D 1 250 GLN 250 250 250 GLN GLN D . n 
D 1 251 LYS 251 251 251 LYS LYS D . n 
D 1 252 PHE 252 252 252 PHE PHE D . n 
D 1 253 ASP 253 253 253 ASP ASP D . n 
D 1 254 GLU 254 254 254 GLU GLU D . n 
D 1 255 ARG 255 255 255 ARG ARG D . n 
D 1 256 LEU 256 256 256 LEU LEU D . n 
D 1 257 VAL 257 257 257 VAL VAL D . n 
D 1 258 TYR 258 258 258 TYR TYR D . n 
D 1 259 THR 259 259 259 THR THR D . n 
D 1 260 SER 260 260 260 SER SER D . n 
D 1 261 PHE 261 261 261 PHE PHE D . n 
D 1 262 SER 262 262 262 SER SER D . n 
D 1 263 GLN 263 263 263 GLN GLN D . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
E  2 ZN  1   301 1    ZN  ZN  A . 
F  3 6YH 1   302 1    6YH E79 A . 
G  4 EDO 1   303 1    EDO EDO A . 
H  4 EDO 1   304 6    EDO EDO A . 
I  4 EDO 1   305 9    EDO EDO A . 
J  2 ZN  1   301 2    ZN  ZN  B . 
K  3 6YH 1   302 2    6YH E79 B . 
L  4 EDO 1   303 2    EDO EDO B . 
M  4 EDO 1   304 4    EDO EDO B . 
N  4 EDO 1   305 7    EDO EDO B . 
O  2 ZN  1   301 3    ZN  ZN  C . 
P  3 6YH 1   302 3    6YH E79 C . 
Q  4 EDO 1   303 10   EDO EDO C . 
R  4 EDO 1   304 11   EDO EDO C . 
S  2 ZN  1   301 4    ZN  ZN  D . 
T  3 6YH 1   302 4    6YH E79 D . 
U  4 EDO 1   303 3    EDO EDO D . 
V  4 EDO 1   304 5    EDO EDO D . 
W  4 EDO 1   305 8    EDO EDO D . 
X  5 HOH 1   401 648  HOH HOH A . 
X  5 HOH 2   402 894  HOH HOH A . 
X  5 HOH 3   403 779  HOH HOH A . 
X  5 HOH 4   404 721  HOH HOH A . 
X  5 HOH 5   405 375  HOH HOH A . 
X  5 HOH 6   406 247  HOH HOH A . 
X  5 HOH 7   407 848  HOH HOH A . 
X  5 HOH 8   408 671  HOH HOH A . 
X  5 HOH 9   409 824  HOH HOH A . 
X  5 HOH 10  410 712  HOH HOH A . 
X  5 HOH 11  411 1107 HOH HOH A . 
X  5 HOH 12  412 416  HOH HOH A . 
X  5 HOH 13  413 1012 HOH HOH A . 
X  5 HOH 14  414 423  HOH HOH A . 
X  5 HOH 15  415 794  HOH HOH A . 
X  5 HOH 16  416 678  HOH HOH A . 
X  5 HOH 17  417 1144 HOH HOH A . 
X  5 HOH 18  418 720  HOH HOH A . 
X  5 HOH 19  419 413  HOH HOH A . 
X  5 HOH 20  420 642  HOH HOH A . 
X  5 HOH 21  421 795  HOH HOH A . 
X  5 HOH 22  422 220  HOH HOH A . 
X  5 HOH 23  423 562  HOH HOH A . 
X  5 HOH 24  424 404  HOH HOH A . 
X  5 HOH 25  425 182  HOH HOH A . 
X  5 HOH 26  426 212  HOH HOH A . 
X  5 HOH 27  427 372  HOH HOH A . 
X  5 HOH 28  428 17   HOH HOH A . 
X  5 HOH 29  429 922  HOH HOH A . 
X  5 HOH 30  430 535  HOH HOH A . 
X  5 HOH 31  431 43   HOH HOH A . 
X  5 HOH 32  432 798  HOH HOH A . 
X  5 HOH 33  433 711  HOH HOH A . 
X  5 HOH 34  434 891  HOH HOH A . 
X  5 HOH 35  435 271  HOH HOH A . 
X  5 HOH 36  436 192  HOH HOH A . 
X  5 HOH 37  437 193  HOH HOH A . 
X  5 HOH 38  438 158  HOH HOH A . 
X  5 HOH 39  439 300  HOH HOH A . 
X  5 HOH 40  440 1105 HOH HOH A . 
X  5 HOH 41  441 103  HOH HOH A . 
X  5 HOH 42  442 294  HOH HOH A . 
X  5 HOH 43  443 14   HOH HOH A . 
X  5 HOH 44  444 943  HOH HOH A . 
X  5 HOH 45  445 71   HOH HOH A . 
X  5 HOH 46  446 692  HOH HOH A . 
X  5 HOH 47  447 145  HOH HOH A . 
X  5 HOH 48  448 422  HOH HOH A . 
X  5 HOH 49  449 61   HOH HOH A . 
X  5 HOH 50  450 962  HOH HOH A . 
X  5 HOH 51  451 391  HOH HOH A . 
X  5 HOH 52  452 542  HOH HOH A . 
X  5 HOH 53  453 60   HOH HOH A . 
X  5 HOH 54  454 983  HOH HOH A . 
X  5 HOH 55  455 293  HOH HOH A . 
X  5 HOH 56  456 84   HOH HOH A . 
X  5 HOH 57  457 202  HOH HOH A . 
X  5 HOH 58  458 169  HOH HOH A . 
X  5 HOH 59  459 303  HOH HOH A . 
X  5 HOH 60  460 236  HOH HOH A . 
X  5 HOH 61  461 652  HOH HOH A . 
X  5 HOH 62  462 687  HOH HOH A . 
X  5 HOH 63  463 1013 HOH HOH A . 
X  5 HOH 64  464 58   HOH HOH A . 
X  5 HOH 65  465 106  HOH HOH A . 
X  5 HOH 66  466 176  HOH HOH A . 
X  5 HOH 67  467 406  HOH HOH A . 
X  5 HOH 68  468 789  HOH HOH A . 
X  5 HOH 69  469 628  HOH HOH A . 
X  5 HOH 70  470 76   HOH HOH A . 
X  5 HOH 71  471 77   HOH HOH A . 
X  5 HOH 72  472 666  HOH HOH A . 
X  5 HOH 73  473 27   HOH HOH A . 
X  5 HOH 74  474 175  HOH HOH A . 
X  5 HOH 75  475 561  HOH HOH A . 
X  5 HOH 76  476 1156 HOH HOH A . 
X  5 HOH 77  477 279  HOH HOH A . 
X  5 HOH 78  478 702  HOH HOH A . 
X  5 HOH 79  479 13   HOH HOH A . 
X  5 HOH 80  480 1106 HOH HOH A . 
X  5 HOH 81  481 471  HOH HOH A . 
X  5 HOH 82  482 56   HOH HOH A . 
X  5 HOH 83  483 710  HOH HOH A . 
X  5 HOH 84  484 568  HOH HOH A . 
X  5 HOH 85  485 96   HOH HOH A . 
X  5 HOH 86  486 691  HOH HOH A . 
X  5 HOH 87  487 39   HOH HOH A . 
X  5 HOH 88  488 357  HOH HOH A . 
X  5 HOH 89  489 392  HOH HOH A . 
X  5 HOH 90  490 330  HOH HOH A . 
X  5 HOH 91  491 633  HOH HOH A . 
X  5 HOH 92  492 760  HOH HOH A . 
X  5 HOH 93  493 277  HOH HOH A . 
X  5 HOH 94  494 536  HOH HOH A . 
X  5 HOH 95  495 288  HOH HOH A . 
X  5 HOH 96  496 551  HOH HOH A . 
X  5 HOH 97  497 964  HOH HOH A . 
X  5 HOH 98  498 199  HOH HOH A . 
X  5 HOH 99  499 295  HOH HOH A . 
X  5 HOH 100 500 699  HOH HOH A . 
X  5 HOH 101 501 346  HOH HOH A . 
X  5 HOH 102 502 166  HOH HOH A . 
X  5 HOH 103 503 33   HOH HOH A . 
X  5 HOH 104 504 581  HOH HOH A . 
X  5 HOH 105 505 443  HOH HOH A . 
X  5 HOH 106 506 19   HOH HOH A . 
X  5 HOH 107 507 953  HOH HOH A . 
X  5 HOH 108 508 455  HOH HOH A . 
X  5 HOH 109 509 414  HOH HOH A . 
X  5 HOH 110 510 641  HOH HOH A . 
X  5 HOH 111 511 611  HOH HOH A . 
X  5 HOH 112 512 66   HOH HOH A . 
X  5 HOH 113 513 717  HOH HOH A . 
X  5 HOH 114 514 8    HOH HOH A . 
X  5 HOH 115 515 366  HOH HOH A . 
X  5 HOH 116 516 627  HOH HOH A . 
X  5 HOH 117 517 24   HOH HOH A . 
X  5 HOH 118 518 469  HOH HOH A . 
X  5 HOH 119 519 213  HOH HOH A . 
X  5 HOH 120 520 425  HOH HOH A . 
X  5 HOH 121 521 993  HOH HOH A . 
X  5 HOH 122 522 326  HOH HOH A . 
X  5 HOH 123 523 729  HOH HOH A . 
X  5 HOH 124 524 546  HOH HOH A . 
X  5 HOH 125 525 1004 HOH HOH A . 
X  5 HOH 126 526 545  HOH HOH A . 
X  5 HOH 127 527 46   HOH HOH A . 
X  5 HOH 128 528 386  HOH HOH A . 
X  5 HOH 129 529 980  HOH HOH A . 
X  5 HOH 130 530 365  HOH HOH A . 
X  5 HOH 131 531 358  HOH HOH A . 
X  5 HOH 132 532 1019 HOH HOH A . 
X  5 HOH 133 533 190  HOH HOH A . 
X  5 HOH 134 534 216  HOH HOH A . 
X  5 HOH 135 535 484  HOH HOH A . 
X  5 HOH 136 536 208  HOH HOH A . 
X  5 HOH 137 537 747  HOH HOH A . 
X  5 HOH 138 538 713  HOH HOH A . 
X  5 HOH 139 539 168  HOH HOH A . 
X  5 HOH 140 540 240  HOH HOH A . 
X  5 HOH 141 541 394  HOH HOH A . 
X  5 HOH 142 542 589  HOH HOH A . 
X  5 HOH 143 543 914  HOH HOH A . 
X  5 HOH 144 544 335  HOH HOH A . 
X  5 HOH 145 545 997  HOH HOH A . 
X  5 HOH 146 546 153  HOH HOH A . 
X  5 HOH 147 547 1003 HOH HOH A . 
X  5 HOH 148 548 877  HOH HOH A . 
X  5 HOH 149 549 957  HOH HOH A . 
X  5 HOH 150 550 533  HOH HOH A . 
X  5 HOH 151 551 287  HOH HOH A . 
X  5 HOH 152 552 688  HOH HOH A . 
X  5 HOH 153 553 30   HOH HOH A . 
X  5 HOH 154 554 167  HOH HOH A . 
X  5 HOH 155 555 832  HOH HOH A . 
X  5 HOH 156 556 473  HOH HOH A . 
X  5 HOH 157 557 315  HOH HOH A . 
X  5 HOH 158 558 907  HOH HOH A . 
X  5 HOH 159 559 987  HOH HOH A . 
X  5 HOH 160 560 917  HOH HOH A . 
X  5 HOH 161 561 191  HOH HOH A . 
X  5 HOH 162 562 911  HOH HOH A . 
X  5 HOH 163 563 307  HOH HOH A . 
X  5 HOH 164 564 275  HOH HOH A . 
X  5 HOH 165 565 452  HOH HOH A . 
X  5 HOH 166 566 1031 HOH HOH A . 
X  5 HOH 167 567 948  HOH HOH A . 
X  5 HOH 168 568 333  HOH HOH A . 
X  5 HOH 169 569 286  HOH HOH A . 
X  5 HOH 170 570 256  HOH HOH A . 
X  5 HOH 171 571 986  HOH HOH A . 
X  5 HOH 172 572 701  HOH HOH A . 
X  5 HOH 173 573 725  HOH HOH A . 
X  5 HOH 174 574 571  HOH HOH A . 
X  5 HOH 175 575 744  HOH HOH A . 
X  5 HOH 176 576 237  HOH HOH A . 
X  5 HOH 177 577 1001 HOH HOH A . 
X  5 HOH 178 578 1155 HOH HOH A . 
X  5 HOH 179 579 862  HOH HOH A . 
X  5 HOH 180 580 582  HOH HOH A . 
X  5 HOH 181 581 1140 HOH HOH A . 
X  5 HOH 182 582 249  HOH HOH A . 
X  5 HOH 183 583 1014 HOH HOH A . 
X  5 HOH 184 584 336  HOH HOH A . 
X  5 HOH 185 585 644  HOH HOH A . 
X  5 HOH 186 586 728  HOH HOH A . 
X  5 HOH 187 587 489  HOH HOH A . 
X  5 HOH 188 588 178  HOH HOH A . 
X  5 HOH 189 589 726  HOH HOH A . 
X  5 HOH 190 590 723  HOH HOH A . 
X  5 HOH 191 591 557  HOH HOH A . 
X  5 HOH 192 592 684  HOH HOH A . 
X  5 HOH 193 593 617  HOH HOH A . 
X  5 HOH 194 594 1136 HOH HOH A . 
X  5 HOH 195 595 906  HOH HOH A . 
X  5 HOH 196 596 1160 HOH HOH A . 
X  5 HOH 197 597 378  HOH HOH A . 
X  5 HOH 198 598 689  HOH HOH A . 
X  5 HOH 199 599 466  HOH HOH A . 
X  5 HOH 200 600 523  HOH HOH A . 
X  5 HOH 201 601 714  HOH HOH A . 
X  5 HOH 202 602 263  HOH HOH A . 
X  5 HOH 203 603 1163 HOH HOH A . 
X  5 HOH 204 604 897  HOH HOH A . 
X  5 HOH 205 605 920  HOH HOH A . 
X  5 HOH 206 606 503  HOH HOH A . 
X  5 HOH 207 607 805  HOH HOH A . 
X  5 HOH 208 608 989  HOH HOH A . 
X  5 HOH 209 609 1162 HOH HOH A . 
X  5 HOH 210 610 1110 HOH HOH A . 
X  5 HOH 211 611 1200 HOH HOH A . 
X  5 HOH 212 612 1011 HOH HOH A . 
X  5 HOH 213 613 791  HOH HOH A . 
X  5 HOH 214 614 1111 HOH HOH A . 
X  5 HOH 215 615 982  HOH HOH A . 
X  5 HOH 216 616 520  HOH HOH A . 
X  5 HOH 217 617 937  HOH HOH A . 
X  5 HOH 218 618 1005 HOH HOH A . 
X  5 HOH 219 619 1006 HOH HOH A . 
X  5 HOH 220 620 1149 HOH HOH A . 
X  5 HOH 221 621 677  HOH HOH A . 
X  5 HOH 222 622 510  HOH HOH A . 
X  5 HOH 223 623 1158 HOH HOH A . 
X  5 HOH 224 624 432  HOH HOH A . 
X  5 HOH 225 625 836  HOH HOH A . 
X  5 HOH 226 626 855  HOH HOH A . 
X  5 HOH 227 627 988  HOH HOH A . 
X  5 HOH 228 628 718  HOH HOH A . 
X  5 HOH 229 629 682  HOH HOH A . 
X  5 HOH 230 630 668  HOH HOH A . 
X  5 HOH 231 631 872  HOH HOH A . 
X  5 HOH 232 632 324  HOH HOH A . 
X  5 HOH 233 633 992  HOH HOH A . 
X  5 HOH 234 634 722  HOH HOH A . 
X  5 HOH 235 635 976  HOH HOH A . 
X  5 HOH 236 636 727  HOH HOH A . 
X  5 HOH 237 637 998  HOH HOH A . 
X  5 HOH 238 638 985  HOH HOH A . 
X  5 HOH 239 639 967  HOH HOH A . 
X  5 HOH 240 640 347  HOH HOH A . 
X  5 HOH 241 641 1150 HOH HOH A . 
X  5 HOH 242 642 1159 HOH HOH A . 
X  5 HOH 243 643 607  HOH HOH A . 
X  5 HOH 244 644 1015 HOH HOH A . 
X  5 HOH 245 645 1161 HOH HOH A . 
X  5 HOH 246 646 1130 HOH HOH A . 
X  5 HOH 247 647 1164 HOH HOH A . 
X  5 HOH 248 648 968  HOH HOH A . 
X  5 HOH 249 649 1009 HOH HOH A . 
X  5 HOH 250 650 478  HOH HOH A . 
X  5 HOH 251 651 1018 HOH HOH A . 
X  5 HOH 252 652 505  HOH HOH A . 
X  5 HOH 253 653 576  HOH HOH A . 
X  5 HOH 254 654 1021 HOH HOH A . 
X  5 HOH 255 655 653  HOH HOH A . 
X  5 HOH 256 656 663  HOH HOH A . 
X  5 HOH 257 657 978  HOH HOH A . 
X  5 HOH 258 658 912  HOH HOH A . 
X  5 HOH 259 659 681  HOH HOH A . 
X  5 HOH 260 660 345  HOH HOH A . 
X  5 HOH 261 661 782  HOH HOH A . 
X  5 HOH 262 662 1154 HOH HOH A . 
X  5 HOH 263 663 588  HOH HOH A . 
X  5 HOH 264 664 974  HOH HOH A . 
X  5 HOH 265 665 515  HOH HOH A . 
X  5 HOH 266 666 1007 HOH HOH A . 
X  5 HOH 267 667 979  HOH HOH A . 
X  5 HOH 268 668 636  HOH HOH A . 
X  5 HOH 269 669 1157 HOH HOH A . 
X  5 HOH 270 670 996  HOH HOH A . 
X  5 HOH 271 671 709  HOH HOH A . 
X  5 HOH 272 672 700  HOH HOH A . 
X  5 HOH 273 673 1135 HOH HOH A . 
Y  5 HOH 1   401 389  HOH HOH B . 
Y  5 HOH 2   402 429  HOH HOH B . 
Y  5 HOH 3   403 1134 HOH HOH B . 
Y  5 HOH 4   404 758  HOH HOH B . 
Y  5 HOH 5   405 707  HOH HOH B . 
Y  5 HOH 6   406 411  HOH HOH B . 
Y  5 HOH 7   407 367  HOH HOH B . 
Y  5 HOH 8   408 1170 HOH HOH B . 
Y  5 HOH 9   409 904  HOH HOH B . 
Y  5 HOH 10  410 558  HOH HOH B . 
Y  5 HOH 11  411 608  HOH HOH B . 
Y  5 HOH 12  412 329  HOH HOH B . 
Y  5 HOH 13  413 245  HOH HOH B . 
Y  5 HOH 14  414 1030 HOH HOH B . 
Y  5 HOH 15  415 1112 HOH HOH B . 
Y  5 HOH 16  416 616  HOH HOH B . 
Y  5 HOH 17  417 972  HOH HOH B . 
Y  5 HOH 18  418 188  HOH HOH B . 
Y  5 HOH 19  419 814  HOH HOH B . 
Y  5 HOH 20  420 955  HOH HOH B . 
Y  5 HOH 21  421 398  HOH HOH B . 
Y  5 HOH 22  422 150  HOH HOH B . 
Y  5 HOH 23  423 7    HOH HOH B . 
Y  5 HOH 24  424 458  HOH HOH B . 
Y  5 HOH 25  425 893  HOH HOH B . 
Y  5 HOH 26  426 1024 HOH HOH B . 
Y  5 HOH 27  427 264  HOH HOH B . 
Y  5 HOH 28  428 355  HOH HOH B . 
Y  5 HOH 29  429 371  HOH HOH B . 
Y  5 HOH 30  430 548  HOH HOH B . 
Y  5 HOH 31  431 302  HOH HOH B . 
Y  5 HOH 32  432 605  HOH HOH B . 
Y  5 HOH 33  433 130  HOH HOH B . 
Y  5 HOH 34  434 479  HOH HOH B . 
Y  5 HOH 35  435 207  HOH HOH B . 
Y  5 HOH 36  436 83   HOH HOH B . 
Y  5 HOH 37  437 291  HOH HOH B . 
Y  5 HOH 38  438 206  HOH HOH B . 
Y  5 HOH 39  439 1167 HOH HOH B . 
Y  5 HOH 40  440 1046 HOH HOH B . 
Y  5 HOH 41  441 461  HOH HOH B . 
Y  5 HOH 42  442 602  HOH HOH B . 
Y  5 HOH 43  443 748  HOH HOH B . 
Y  5 HOH 44  444 734  HOH HOH B . 
Y  5 HOH 45  445 1036 HOH HOH B . 
Y  5 HOH 46  446 538  HOH HOH B . 
Y  5 HOH 47  447 331  HOH HOH B . 
Y  5 HOH 48  448 739  HOH HOH B . 
Y  5 HOH 49  449 577  HOH HOH B . 
Y  5 HOH 50  450 811  HOH HOH B . 
Y  5 HOH 51  451 532  HOH HOH B . 
Y  5 HOH 52  452 741  HOH HOH B . 
Y  5 HOH 53  453 80   HOH HOH B . 
Y  5 HOH 54  454 110  HOH HOH B . 
Y  5 HOH 55  455 171  HOH HOH B . 
Y  5 HOH 56  456 1165 HOH HOH B . 
Y  5 HOH 57  457 580  HOH HOH B . 
Y  5 HOH 58  458 89   HOH HOH B . 
Y  5 HOH 59  459 708  HOH HOH B . 
Y  5 HOH 60  460 754  HOH HOH B . 
Y  5 HOH 61  461 156  HOH HOH B . 
Y  5 HOH 62  462 470  HOH HOH B . 
Y  5 HOH 63  463 737  HOH HOH B . 
Y  5 HOH 64  464 393  HOH HOH B . 
Y  5 HOH 65  465 506  HOH HOH B . 
Y  5 HOH 66  466 941  HOH HOH B . 
Y  5 HOH 67  467 160  HOH HOH B . 
Y  5 HOH 68  468 959  HOH HOH B . 
Y  5 HOH 69  469 1168 HOH HOH B . 
Y  5 HOH 70  470 693  HOH HOH B . 
Y  5 HOH 71  471 31   HOH HOH B . 
Y  5 HOH 72  472 595  HOH HOH B . 
Y  5 HOH 73  473 78   HOH HOH B . 
Y  5 HOH 74  474 164  HOH HOH B . 
Y  5 HOH 75  475 112  HOH HOH B . 
Y  5 HOH 76  476 109  HOH HOH B . 
Y  5 HOH 77  477 138  HOH HOH B . 
Y  5 HOH 78  478 232  HOH HOH B . 
Y  5 HOH 79  479 1026 HOH HOH B . 
Y  5 HOH 80  480 21   HOH HOH B . 
Y  5 HOH 81  481 1147 HOH HOH B . 
Y  5 HOH 82  482 310  HOH HOH B . 
Y  5 HOH 83  483 544  HOH HOH B . 
Y  5 HOH 84  484 1034 HOH HOH B . 
Y  5 HOH 85  485 593  HOH HOH B . 
Y  5 HOH 86  486 526  HOH HOH B . 
Y  5 HOH 87  487 1032 HOH HOH B . 
Y  5 HOH 88  488 267  HOH HOH B . 
Y  5 HOH 89  489 211  HOH HOH B . 
Y  5 HOH 90  490 844  HOH HOH B . 
Y  5 HOH 91  491 361  HOH HOH B . 
Y  5 HOH 92  492 504  HOH HOH B . 
Y  5 HOH 93  493 98   HOH HOH B . 
Y  5 HOH 94  494 672  HOH HOH B . 
Y  5 HOH 95  495 553  HOH HOH B . 
Y  5 HOH 96  496 507  HOH HOH B . 
Y  5 HOH 97  497 81   HOH HOH B . 
Y  5 HOH 98  498 572  HOH HOH B . 
Y  5 HOH 99  499 107  HOH HOH B . 
Y  5 HOH 100 500 74   HOH HOH B . 
Y  5 HOH 101 501 75   HOH HOH B . 
Y  5 HOH 102 502 135  HOH HOH B . 
Y  5 HOH 103 503 543  HOH HOH B . 
Y  5 HOH 104 504 48   HOH HOH B . 
Y  5 HOH 105 505 731  HOH HOH B . 
Y  5 HOH 106 506 63   HOH HOH B . 
Y  5 HOH 107 507 143  HOH HOH B . 
Y  5 HOH 108 508 431  HOH HOH B . 
Y  5 HOH 109 509 59   HOH HOH B . 
Y  5 HOH 110 510 118  HOH HOH B . 
Y  5 HOH 111 511 736  HOH HOH B . 
Y  5 HOH 112 512 706  HOH HOH B . 
Y  5 HOH 113 513 52   HOH HOH B . 
Y  5 HOH 114 514 40   HOH HOH B . 
Y  5 HOH 115 515 108  HOH HOH B . 
Y  5 HOH 116 516 144  HOH HOH B . 
Y  5 HOH 117 517 285  HOH HOH B . 
Y  5 HOH 118 518 619  HOH HOH B . 
Y  5 HOH 119 519 146  HOH HOH B . 
Y  5 HOH 120 520 57   HOH HOH B . 
Y  5 HOH 121 521 15   HOH HOH B . 
Y  5 HOH 122 522 459  HOH HOH B . 
Y  5 HOH 123 523 1173 HOH HOH B . 
Y  5 HOH 124 524 157  HOH HOH B . 
Y  5 HOH 125 525 323  HOH HOH B . 
Y  5 HOH 126 526 306  HOH HOH B . 
Y  5 HOH 127 527 136  HOH HOH B . 
Y  5 HOH 128 528 55   HOH HOH B . 
Y  5 HOH 129 529 888  HOH HOH B . 
Y  5 HOH 130 530 148  HOH HOH B . 
Y  5 HOH 131 531 235  HOH HOH B . 
Y  5 HOH 132 532 225  HOH HOH B . 
Y  5 HOH 133 533 433  HOH HOH B . 
Y  5 HOH 134 534 407  HOH HOH B . 
Y  5 HOH 135 535 796  HOH HOH B . 
Y  5 HOH 136 536 44   HOH HOH B . 
Y  5 HOH 137 537 1022 HOH HOH B . 
Y  5 HOH 138 538 842  HOH HOH B . 
Y  5 HOH 139 539 831  HOH HOH B . 
Y  5 HOH 140 540 499  HOH HOH B . 
Y  5 HOH 141 541 637  HOH HOH B . 
Y  5 HOH 142 542 428  HOH HOH B . 
Y  5 HOH 143 543 500  HOH HOH B . 
Y  5 HOH 144 544 376  HOH HOH B . 
Y  5 HOH 145 545 527  HOH HOH B . 
Y  5 HOH 146 546 120  HOH HOH B . 
Y  5 HOH 147 547 661  HOH HOH B . 
Y  5 HOH 148 548 253  HOH HOH B . 
Y  5 HOH 149 549 777  HOH HOH B . 
Y  5 HOH 150 550 863  HOH HOH B . 
Y  5 HOH 151 551 119  HOH HOH B . 
Y  5 HOH 152 552 298  HOH HOH B . 
Y  5 HOH 153 553 111  HOH HOH B . 
Y  5 HOH 154 554 650  HOH HOH B . 
Y  5 HOH 155 555 567  HOH HOH B . 
Y  5 HOH 156 556 818  HOH HOH B . 
Y  5 HOH 157 557 887  HOH HOH B . 
Y  5 HOH 158 558 843  HOH HOH B . 
Y  5 HOH 159 559 892  HOH HOH B . 
Y  5 HOH 160 560 116  HOH HOH B . 
Y  5 HOH 161 561 85   HOH HOH B . 
Y  5 HOH 162 562 151  HOH HOH B . 
Y  5 HOH 163 563 115  HOH HOH B . 
Y  5 HOH 164 564 511  HOH HOH B . 
Y  5 HOH 165 565 1039 HOH HOH B . 
Y  5 HOH 166 566 239  HOH HOH B . 
Y  5 HOH 167 567 975  HOH HOH B . 
Y  5 HOH 168 568 966  HOH HOH B . 
Y  5 HOH 169 569 137  HOH HOH B . 
Y  5 HOH 170 570 364  HOH HOH B . 
Y  5 HOH 171 571 4    HOH HOH B . 
Y  5 HOH 172 572 370  HOH HOH B . 
Y  5 HOH 173 573 995  HOH HOH B . 
Y  5 HOH 174 574 879  HOH HOH B . 
Y  5 HOH 175 575 586  HOH HOH B . 
Y  5 HOH 176 576 337  HOH HOH B . 
Y  5 HOH 177 577 141  HOH HOH B . 
Y  5 HOH 178 578 2    HOH HOH B . 
Y  5 HOH 179 579 374  HOH HOH B . 
Y  5 HOH 180 580 273  HOH HOH B . 
Y  5 HOH 181 581 328  HOH HOH B . 
Y  5 HOH 182 582 845  HOH HOH B . 
Y  5 HOH 183 583 163  HOH HOH B . 
Y  5 HOH 184 584 380  HOH HOH B . 
Y  5 HOH 185 585 209  HOH HOH B . 
Y  5 HOH 186 586 1025 HOH HOH B . 
Y  5 HOH 187 587 363  HOH HOH B . 
Y  5 HOH 188 588 490  HOH HOH B . 
Y  5 HOH 189 589 497  HOH HOH B . 
Y  5 HOH 190 590 95   HOH HOH B . 
Y  5 HOH 191 591 493  HOH HOH B . 
Y  5 HOH 192 592 827  HOH HOH B . 
Y  5 HOH 193 593 1038 HOH HOH B . 
Y  5 HOH 194 594 387  HOH HOH B . 
Y  5 HOH 195 595 449  HOH HOH B . 
Y  5 HOH 196 596 194  HOH HOH B . 
Y  5 HOH 197 597 453  HOH HOH B . 
Y  5 HOH 198 598 715  HOH HOH B . 
Y  5 HOH 199 599 356  HOH HOH B . 
Y  5 HOH 200 600 32   HOH HOH B . 
Y  5 HOH 201 601 742  HOH HOH B . 
Y  5 HOH 202 602 488  HOH HOH B . 
Y  5 HOH 203 603 161  HOH HOH B . 
Y  5 HOH 204 604 396  HOH HOH B . 
Y  5 HOH 205 605 64   HOH HOH B . 
Y  5 HOH 206 606 787  HOH HOH B . 
Y  5 HOH 207 607 454  HOH HOH B . 
Y  5 HOH 208 608 314  HOH HOH B . 
Y  5 HOH 209 609 1047 HOH HOH B . 
Y  5 HOH 210 610 740  HOH HOH B . 
Y  5 HOH 211 611 981  HOH HOH B . 
Y  5 HOH 212 612 594  HOH HOH B . 
Y  5 HOH 213 613 318  HOH HOH B . 
Y  5 HOH 214 614 1108 HOH HOH B . 
Y  5 HOH 215 615 465  HOH HOH B . 
Y  5 HOH 216 616 377  HOH HOH B . 
Y  5 HOH 217 617 690  HOH HOH B . 
Y  5 HOH 218 618 686  HOH HOH B . 
Y  5 HOH 219 619 86   HOH HOH B . 
Y  5 HOH 220 620 517  HOH HOH B . 
Y  5 HOH 221 621 552  HOH HOH B . 
Y  5 HOH 222 622 829  HOH HOH B . 
Y  5 HOH 223 623 969  HOH HOH B . 
Y  5 HOH 224 624 230  HOH HOH B . 
Y  5 HOH 225 625 928  HOH HOH B . 
Y  5 HOH 226 626 994  HOH HOH B . 
Y  5 HOH 227 627 990  HOH HOH B . 
Y  5 HOH 228 628 685  HOH HOH B . 
Y  5 HOH 229 629 221  HOH HOH B . 
Y  5 HOH 230 630 265  HOH HOH B . 
Y  5 HOH 231 631 625  HOH HOH B . 
Y  5 HOH 232 632 638  HOH HOH B . 
Y  5 HOH 233 633 790  HOH HOH B . 
Y  5 HOH 234 634 599  HOH HOH B . 
Y  5 HOH 235 635 584  HOH HOH B . 
Y  5 HOH 236 636 566  HOH HOH B . 
Y  5 HOH 237 637 327  HOH HOH B . 
Y  5 HOH 238 638 385  HOH HOH B . 
Y  5 HOH 239 639 618  HOH HOH B . 
Y  5 HOH 240 640 308  HOH HOH B . 
Y  5 HOH 241 641 419  HOH HOH B . 
Y  5 HOH 242 642 704  HOH HOH B . 
Y  5 HOH 243 643 970  HOH HOH B . 
Y  5 HOH 244 644 1145 HOH HOH B . 
Y  5 HOH 245 645 991  HOH HOH B . 
Y  5 HOH 246 646 1045 HOH HOH B . 
Y  5 HOH 247 647 873  HOH HOH B . 
Y  5 HOH 248 648 1040 HOH HOH B . 
Y  5 HOH 249 649 613  HOH HOH B . 
Y  5 HOH 250 650 1139 HOH HOH B . 
Y  5 HOH 251 651 1023 HOH HOH B . 
Y  5 HOH 252 652 579  HOH HOH B . 
Y  5 HOH 253 653 1117 HOH HOH B . 
Y  5 HOH 254 654 1172 HOH HOH B . 
Y  5 HOH 255 655 609  HOH HOH B . 
Y  5 HOH 256 656 1171 HOH HOH B . 
Y  5 HOH 257 657 373  HOH HOH B . 
Y  5 HOH 258 658 705  HOH HOH B . 
Y  5 HOH 259 659 951  HOH HOH B . 
Y  5 HOH 260 660 919  HOH HOH B . 
Y  5 HOH 261 661 1020 HOH HOH B . 
Y  5 HOH 262 662 703  HOH HOH B . 
Y  5 HOH 263 663 934  HOH HOH B . 
Y  5 HOH 264 664 1016 HOH HOH B . 
Y  5 HOH 265 665 1041 HOH HOH B . 
Y  5 HOH 266 666 1169 HOH HOH B . 
Y  5 HOH 267 667 462  HOH HOH B . 
Y  5 HOH 268 668 513  HOH HOH B . 
Y  5 HOH 269 669 883  HOH HOH B . 
Y  5 HOH 270 670 719  HOH HOH B . 
Y  5 HOH 271 671 531  HOH HOH B . 
Y  5 HOH 272 672 1033 HOH HOH B . 
Y  5 HOH 273 673 927  HOH HOH B . 
Y  5 HOH 274 674 610  HOH HOH B . 
Y  5 HOH 275 675 424  HOH HOH B . 
Y  5 HOH 276 676 496  HOH HOH B . 
Y  5 HOH 277 677 1035 HOH HOH B . 
Y  5 HOH 278 678 1143 HOH HOH B . 
Y  5 HOH 279 679 1132 HOH HOH B . 
Y  5 HOH 280 680 417  HOH HOH B . 
Y  5 HOH 281 681 929  HOH HOH B . 
Y  5 HOH 282 682 362  HOH HOH B . 
Y  5 HOH 283 683 234  HOH HOH B . 
Y  5 HOH 284 684 903  HOH HOH B . 
Y  5 HOH 285 685 716  HOH HOH B . 
Y  5 HOH 286 686 667  HOH HOH B . 
Y  5 HOH 287 687 950  HOH HOH B . 
Y  5 HOH 288 688 261  HOH HOH B . 
Y  5 HOH 289 689 770  HOH HOH B . 
Y  5 HOH 290 690 651  HOH HOH B . 
Y  5 HOH 291 691 283  HOH HOH B . 
Y  5 HOH 292 692 1043 HOH HOH B . 
Y  5 HOH 293 693 694  HOH HOH B . 
Y  5 HOH 294 694 806  HOH HOH B . 
Y  5 HOH 295 695 838  HOH HOH B . 
Y  5 HOH 296 696 524  HOH HOH B . 
Y  5 HOH 297 697 514  HOH HOH B . 
Y  5 HOH 298 698 521  HOH HOH B . 
Y  5 HOH 299 699 698  HOH HOH B . 
Y  5 HOH 300 700 675  HOH HOH B . 
Y  5 HOH 301 701 925  HOH HOH B . 
Y  5 HOH 302 702 916  HOH HOH B . 
Y  5 HOH 303 703 634  HOH HOH B . 
Y  5 HOH 304 704 901  HOH HOH B . 
Y  5 HOH 305 705 1138 HOH HOH B . 
Y  5 HOH 306 706 343  HOH HOH B . 
Y  5 HOH 307 707 244  HOH HOH B . 
Y  5 HOH 308 708 1113 HOH HOH B . 
Y  5 HOH 309 709 874  HOH HOH B . 
Y  5 HOH 310 710 695  HOH HOH B . 
Y  5 HOH 311 711 696  HOH HOH B . 
Y  5 HOH 312 712 861  HOH HOH B . 
Y  5 HOH 313 713 676  HOH HOH B . 
Y  5 HOH 314 714 475  HOH HOH B . 
Y  5 HOH 315 715 344  HOH HOH B . 
Y  5 HOH 316 716 1137 HOH HOH B . 
Y  5 HOH 317 717 669  HOH HOH B . 
Y  5 HOH 318 718 915  HOH HOH B . 
Y  5 HOH 319 719 977  HOH HOH B . 
Y  5 HOH 320 720 565  HOH HOH B . 
Y  5 HOH 321 721 1166 HOH HOH B . 
Y  5 HOH 322 722 1042 HOH HOH B . 
Y  5 HOH 323 723 875  HOH HOH B . 
Y  5 HOH 324 724 1029 HOH HOH B . 
Z  5 HOH 1   401 229  HOH HOH C . 
Z  5 HOH 2   402 878  HOH HOH C . 
Z  5 HOH 3   403 598  HOH HOH C . 
Z  5 HOH 4   404 870  HOH HOH C . 
Z  5 HOH 5   405 101  HOH HOH C . 
Z  5 HOH 6   406 624  HOH HOH C . 
Z  5 HOH 7   407 766  HOH HOH C . 
Z  5 HOH 8   408 534  HOH HOH C . 
Z  5 HOH 9   409 1096 HOH HOH C . 
Z  5 HOH 10  410 426  HOH HOH C . 
Z  5 HOH 11  411 889  HOH HOH C . 
Z  5 HOH 12  412 1148 HOH HOH C . 
Z  5 HOH 13  413 1088 HOH HOH C . 
Z  5 HOH 14  414 1072 HOH HOH C . 
Z  5 HOH 15  415 332  HOH HOH C . 
Z  5 HOH 16  416 334  HOH HOH C . 
Z  5 HOH 17  417 382  HOH HOH C . 
Z  5 HOH 18  418 596  HOH HOH C . 
Z  5 HOH 19  419 645  HOH HOH C . 
Z  5 HOH 20  420 1087 HOH HOH C . 
Z  5 HOH 21  421 753  HOH HOH C . 
Z  5 HOH 22  422 390  HOH HOH C . 
Z  5 HOH 23  423 772  HOH HOH C . 
Z  5 HOH 24  424 655  HOH HOH C . 
Z  5 HOH 25  425 578  HOH HOH C . 
Z  5 HOH 26  426 231  HOH HOH C . 
Z  5 HOH 27  427 87   HOH HOH C . 
Z  5 HOH 28  428 1073 HOH HOH C . 
Z  5 HOH 29  429 537  HOH HOH C . 
Z  5 HOH 30  430 656  HOH HOH C . 
Z  5 HOH 31  431 65   HOH HOH C . 
Z  5 HOH 32  432 1185 HOH HOH C . 
Z  5 HOH 33  433 635  HOH HOH C . 
Z  5 HOH 34  434 1044 HOH HOH C . 
Z  5 HOH 35  435 233  HOH HOH C . 
Z  5 HOH 36  436 509  HOH HOH C . 
Z  5 HOH 37  437 281  HOH HOH C . 
Z  5 HOH 38  438 1079 HOH HOH C . 
Z  5 HOH 39  439 932  HOH HOH C . 
Z  5 HOH 40  440 896  HOH HOH C . 
Z  5 HOH 41  441 841  HOH HOH C . 
Z  5 HOH 42  442 1123 HOH HOH C . 
Z  5 HOH 43  443 1199 HOH HOH C . 
Z  5 HOH 44  444 405  HOH HOH C . 
Z  5 HOH 45  445 368  HOH HOH C . 
Z  5 HOH 46  446 152  HOH HOH C . 
Z  5 HOH 47  447 154  HOH HOH C . 
Z  5 HOH 48  448 762  HOH HOH C . 
Z  5 HOH 49  449 255  HOH HOH C . 
Z  5 HOH 50  450 900  HOH HOH C . 
Z  5 HOH 51  451 67   HOH HOH C . 
Z  5 HOH 52  452 614  HOH HOH C . 
Z  5 HOH 53  453 781  HOH HOH C . 
Z  5 HOH 54  454 601  HOH HOH C . 
Z  5 HOH 55  455 1071 HOH HOH C . 
Z  5 HOH 56  456 20   HOH HOH C . 
Z  5 HOH 57  457 763  HOH HOH C . 
Z  5 HOH 58  458 512  HOH HOH C . 
Z  5 HOH 59  459 1081 HOH HOH C . 
Z  5 HOH 60  460 36   HOH HOH C . 
Z  5 HOH 61  461 921  HOH HOH C . 
Z  5 HOH 62  462 858  HOH HOH C . 
Z  5 HOH 63  463 864  HOH HOH C . 
Z  5 HOH 64  464 184  HOH HOH C . 
Z  5 HOH 65  465 266  HOH HOH C . 
Z  5 HOH 66  466 1050 HOH HOH C . 
Z  5 HOH 67  467 316  HOH HOH C . 
Z  5 HOH 68  468 342  HOH HOH C . 
Z  5 HOH 69  469 284  HOH HOH C . 
Z  5 HOH 70  470 1085 HOH HOH C . 
Z  5 HOH 71  471 1187 HOH HOH C . 
Z  5 HOH 72  472 187  HOH HOH C . 
Z  5 HOH 73  473 321  HOH HOH C . 
Z  5 HOH 74  474 931  HOH HOH C . 
Z  5 HOH 75  475 351  HOH HOH C . 
Z  5 HOH 76  476 117  HOH HOH C . 
Z  5 HOH 77  477 62   HOH HOH C . 
Z  5 HOH 78  478 660  HOH HOH C . 
Z  5 HOH 79  479 856  HOH HOH C . 
Z  5 HOH 80  480 26   HOH HOH C . 
Z  5 HOH 81  481 140  HOH HOH C . 
Z  5 HOH 82  482 1094 HOH HOH C . 
Z  5 HOH 83  483 41   HOH HOH C . 
Z  5 HOH 84  484 649  HOH HOH C . 
Z  5 HOH 85  485 177  HOH HOH C . 
Z  5 HOH 86  486 801  HOH HOH C . 
Z  5 HOH 87  487 129  HOH HOH C . 
Z  5 HOH 88  488 780  HOH HOH C . 
Z  5 HOH 89  489 630  HOH HOH C . 
Z  5 HOH 90  490 195  HOH HOH C . 
Z  5 HOH 91  491 200  HOH HOH C . 
Z  5 HOH 92  492 104  HOH HOH C . 
Z  5 HOH 93  493 816  HOH HOH C . 
Z  5 HOH 94  494 871  HOH HOH C . 
Z  5 HOH 95  495 270  HOH HOH C . 
Z  5 HOH 96  496 460  HOH HOH C . 
Z  5 HOH 97  497 1051 HOH HOH C . 
Z  5 HOH 98  498 133  HOH HOH C . 
Z  5 HOH 99  499 70   HOH HOH C . 
Z  5 HOH 100 500 5    HOH HOH C . 
Z  5 HOH 101 501 1086 HOH HOH C . 
Z  5 HOH 102 502 1078 HOH HOH C . 
Z  5 HOH 103 503 320  HOH HOH C . 
Z  5 HOH 104 504 54   HOH HOH C . 
Z  5 HOH 105 505 592  HOH HOH C . 
Z  5 HOH 106 506 262  HOH HOH C . 
Z  5 HOH 107 507 492  HOH HOH C . 
Z  5 HOH 108 508 587  HOH HOH C . 
Z  5 HOH 109 509 528  HOH HOH C . 
Z  5 HOH 110 510 743  HOH HOH C . 
Z  5 HOH 111 511 626  HOH HOH C . 
Z  5 HOH 112 512 541  HOH HOH C . 
Z  5 HOH 113 513 359  HOH HOH C . 
Z  5 HOH 114 514 340  HOH HOH C . 
Z  5 HOH 115 515 147  HOH HOH C . 
Z  5 HOH 116 516 1179 HOH HOH C . 
Z  5 HOH 117 517 214  HOH HOH C . 
Z  5 HOH 118 518 183  HOH HOH C . 
Z  5 HOH 119 519 632  HOH HOH C . 
Z  5 HOH 120 520 1181 HOH HOH C . 
Z  5 HOH 121 521 165  HOH HOH C . 
Z  5 HOH 122 522 260  HOH HOH C . 
Z  5 HOH 123 523 895  HOH HOH C . 
Z  5 HOH 124 524 834  HOH HOH C . 
Z  5 HOH 125 525 810  HOH HOH C . 
Z  5 HOH 126 526 485  HOH HOH C . 
Z  5 HOH 127 527 121  HOH HOH C . 
Z  5 HOH 128 528 1080 HOH HOH C . 
Z  5 HOH 129 529 752  HOH HOH C . 
Z  5 HOH 130 530 1084 HOH HOH C . 
Z  5 HOH 131 531 852  HOH HOH C . 
Z  5 HOH 132 532 297  HOH HOH C . 
Z  5 HOH 133 533 134  HOH HOH C . 
Z  5 HOH 134 534 756  HOH HOH C . 
Z  5 HOH 135 535 381  HOH HOH C . 
Z  5 HOH 136 536 72   HOH HOH C . 
Z  5 HOH 137 537 38   HOH HOH C . 
Z  5 HOH 138 538 28   HOH HOH C . 
Z  5 HOH 139 539 185  HOH HOH C . 
Z  5 HOH 140 540 522  HOH HOH C . 
Z  5 HOH 141 541 882  HOH HOH C . 
Z  5 HOH 142 542 933  HOH HOH C . 
Z  5 HOH 143 543 69   HOH HOH C . 
Z  5 HOH 144 544 238  HOH HOH C . 
Z  5 HOH 145 545 282  HOH HOH C . 
Z  5 HOH 146 546 9    HOH HOH C . 
Z  5 HOH 147 547 139  HOH HOH C . 
Z  5 HOH 148 548 215  HOH HOH C . 
Z  5 HOH 149 549 826  HOH HOH C . 
Z  5 HOH 150 550 1074 HOH HOH C . 
Z  5 HOH 151 551 631  HOH HOH C . 
Z  5 HOH 152 552 569  HOH HOH C . 
Z  5 HOH 153 553 1082 HOH HOH C . 
Z  5 HOH 154 554 759  HOH HOH C . 
Z  5 HOH 155 555 800  HOH HOH C . 
Z  5 HOH 156 556 317  HOH HOH C . 
Z  5 HOH 157 557 415  HOH HOH C . 
Z  5 HOH 158 558 792  HOH HOH C . 
Z  5 HOH 159 559 1068 HOH HOH C . 
Z  5 HOH 160 560 248  HOH HOH C . 
Z  5 HOH 161 561 276  HOH HOH C . 
Z  5 HOH 162 562 768  HOH HOH C . 
Z  5 HOH 163 563 924  HOH HOH C . 
Z  5 HOH 164 564 884  HOH HOH C . 
Z  5 HOH 165 565 735  HOH HOH C . 
Z  5 HOH 166 566 560  HOH HOH C . 
Z  5 HOH 167 567 501  HOH HOH C . 
Z  5 HOH 168 568 947  HOH HOH C . 
Z  5 HOH 169 569 965  HOH HOH C . 
Z  5 HOH 170 570 427  HOH HOH C . 
Z  5 HOH 171 571 657  HOH HOH C . 
Z  5 HOH 172 572 451  HOH HOH C . 
Z  5 HOH 173 573 464  HOH HOH C . 
Z  5 HOH 174 574 518  HOH HOH C . 
Z  5 HOH 175 575 575  HOH HOH C . 
Z  5 HOH 176 576 132  HOH HOH C . 
Z  5 HOH 177 577 817  HOH HOH C . 
Z  5 HOH 178 578 771  HOH HOH C . 
Z  5 HOH 179 579 926  HOH HOH C . 
Z  5 HOH 180 580 784  HOH HOH C . 
Z  5 HOH 181 581 597  HOH HOH C . 
Z  5 HOH 182 582 369  HOH HOH C . 
Z  5 HOH 183 583 563  HOH HOH C . 
Z  5 HOH 184 584 606  HOH HOH C . 
Z  5 HOH 185 585 149  HOH HOH C . 
Z  5 HOH 186 586 554  HOH HOH C . 
Z  5 HOH 187 587 491  HOH HOH C . 
Z  5 HOH 188 588 79   HOH HOH C . 
Z  5 HOH 189 589 905  HOH HOH C . 
Z  5 HOH 190 590 1114 HOH HOH C . 
Z  5 HOH 191 591 447  HOH HOH C . 
Z  5 HOH 192 592 1000 HOH HOH C . 
Z  5 HOH 193 593 615  HOH HOH C . 
Z  5 HOH 194 594 923  HOH HOH C . 
Z  5 HOH 195 595 403  HOH HOH C . 
Z  5 HOH 196 596 400  HOH HOH C . 
Z  5 HOH 197 597 918  HOH HOH C . 
Z  5 HOH 198 598 724  HOH HOH C . 
Z  5 HOH 199 599 1183 HOH HOH C . 
Z  5 HOH 200 600 219  HOH HOH C . 
Z  5 HOH 201 601 999  HOH HOH C . 
Z  5 HOH 202 602 830  HOH HOH C . 
Z  5 HOH 203 603 1131 HOH HOH C . 
Z  5 HOH 204 604 808  HOH HOH C . 
Z  5 HOH 205 605 639  HOH HOH C . 
Z  5 HOH 206 606 1174 HOH HOH C . 
Z  5 HOH 207 607 574  HOH HOH C . 
Z  5 HOH 208 608 486  HOH HOH C . 
Z  5 HOH 209 609 410  HOH HOH C . 
Z  5 HOH 210 610 585  HOH HOH C . 
Z  5 HOH 211 611 322  HOH HOH C . 
Z  5 HOH 212 612 961  HOH HOH C . 
Z  5 HOH 213 613 1152 HOH HOH C . 
Z  5 HOH 214 614 498  HOH HOH C . 
Z  5 HOH 215 615 1083 HOH HOH C . 
Z  5 HOH 216 616 658  HOH HOH C . 
Z  5 HOH 217 617 1067 HOH HOH C . 
Z  5 HOH 218 618 1151 HOH HOH C . 
Z  5 HOH 219 619 803  HOH HOH C . 
Z  5 HOH 220 620 338  HOH HOH C . 
Z  5 HOH 221 621 1186 HOH HOH C . 
Z  5 HOH 222 622 1049 HOH HOH C . 
Z  5 HOH 223 623 1064 HOH HOH C . 
Z  5 HOH 224 624 564  HOH HOH C . 
Z  5 HOH 225 625 954  HOH HOH C . 
Z  5 HOH 226 626 1198 HOH HOH C . 
Z  5 HOH 227 627 1055 HOH HOH C . 
Z  5 HOH 228 628 1002 HOH HOH C . 
Z  5 HOH 229 629 408  HOH HOH C . 
Z  5 HOH 230 630 539  HOH HOH C . 
Z  5 HOH 231 631 529  HOH HOH C . 
Z  5 HOH 232 632 1109 HOH HOH C . 
Z  5 HOH 233 633 278  HOH HOH C . 
Z  5 HOH 234 634 474  HOH HOH C . 
Z  5 HOH 235 635 913  HOH HOH C . 
Z  5 HOH 236 636 769  HOH HOH C . 
Z  5 HOH 237 637 622  HOH HOH C . 
Z  5 HOH 238 638 1182 HOH HOH C . 
Z  5 HOH 239 639 1063 HOH HOH C . 
Z  5 HOH 240 640 1175 HOH HOH C . 
Z  5 HOH 241 641 813  HOH HOH C . 
Z  5 HOH 242 642 1075 HOH HOH C . 
Z  5 HOH 243 643 1069 HOH HOH C . 
Z  5 HOH 244 644 1060 HOH HOH C . 
Z  5 HOH 245 645 854  HOH HOH C . 
Z  5 HOH 246 646 1184 HOH HOH C . 
Z  5 HOH 247 647 395  HOH HOH C . 
Z  5 HOH 248 648 902  HOH HOH C . 
Z  5 HOH 249 649 1061 HOH HOH C . 
Z  5 HOH 250 650 809  HOH HOH C . 
Z  5 HOH 251 651 525  HOH HOH C . 
Z  5 HOH 252 652 1066 HOH HOH C . 
Z  5 HOH 253 653 670  HOH HOH C . 
Z  5 HOH 254 654 850  HOH HOH C . 
Z  5 HOH 255 655 936  HOH HOH C . 
Z  5 HOH 256 656 837  HOH HOH C . 
Z  5 HOH 257 657 662  HOH HOH C . 
Z  5 HOH 258 658 430  HOH HOH C . 
Z  5 HOH 259 659 949  HOH HOH C . 
Z  5 HOH 260 660 1178 HOH HOH C . 
Z  5 HOH 261 661 1070 HOH HOH C . 
Z  5 HOH 262 662 1054 HOH HOH C . 
Z  5 HOH 263 663 1056 HOH HOH C . 
Z  5 HOH 264 664 1057 HOH HOH C . 
Z  5 HOH 265 665 773  HOH HOH C . 
Z  5 HOH 266 666 755  HOH HOH C . 
Z  5 HOH 267 667 860  HOH HOH C . 
Z  5 HOH 268 668 1180 HOH HOH C . 
Z  5 HOH 269 669 833  HOH HOH C . 
Z  5 HOH 270 670 1065 HOH HOH C . 
Z  5 HOH 271 671 603  HOH HOH C . 
Z  5 HOH 272 672 971  HOH HOH C . 
Z  5 HOH 273 673 1133 HOH HOH C . 
Z  5 HOH 274 674 1017 HOH HOH C . 
Z  5 HOH 275 675 1177 HOH HOH C . 
Z  5 HOH 276 676 1058 HOH HOH C . 
AA 5 HOH 1   401 750  HOH HOH D . 
AA 5 HOH 2   402 555  HOH HOH D . 
AA 5 HOH 3   403 258  HOH HOH D . 
AA 5 HOH 4   404 1197 HOH HOH D . 
AA 5 HOH 5   405 90   HOH HOH D . 
AA 5 HOH 6   406 640  HOH HOH D . 
AA 5 HOH 7   407 242  HOH HOH D . 
AA 5 HOH 8   408 1193 HOH HOH D . 
AA 5 HOH 9   409 1125 HOH HOH D . 
AA 5 HOH 10  410 804  HOH HOH D . 
AA 5 HOH 11  411 1196 HOH HOH D . 
AA 5 HOH 12  412 292  HOH HOH D . 
AA 5 HOH 13  413 196  HOH HOH D . 
AA 5 HOH 14  414 1048 HOH HOH D . 
AA 5 HOH 15  415 851  HOH HOH D . 
AA 5 HOH 16  416 654  HOH HOH D . 
AA 5 HOH 17  417 401  HOH HOH D . 
AA 5 HOH 18  418 938  HOH HOH D . 
AA 5 HOH 19  419 142  HOH HOH D . 
AA 5 HOH 20  420 1116 HOH HOH D . 
AA 5 HOH 21  421 880  HOH HOH D . 
AA 5 HOH 22  422 3    HOH HOH D . 
AA 5 HOH 23  423 222  HOH HOH D . 
AA 5 HOH 24  424 812  HOH HOH D . 
AA 5 HOH 25  425 783  HOH HOH D . 
AA 5 HOH 26  426 37   HOH HOH D . 
AA 5 HOH 27  427 556  HOH HOH D . 
AA 5 HOH 28  428 876  HOH HOH D . 
AA 5 HOH 29  429 788  HOH HOH D . 
AA 5 HOH 30  430 793  HOH HOH D . 
AA 5 HOH 31  431 1118 HOH HOH D . 
AA 5 HOH 32  432 865  HOH HOH D . 
AA 5 HOH 33  433 228  HOH HOH D . 
AA 5 HOH 34  434 350  HOH HOH D . 
AA 5 HOH 35  435 319  HOH HOH D . 
AA 5 HOH 36  436 114  HOH HOH D . 
AA 5 HOH 37  437 203  HOH HOH D . 
AA 5 HOH 38  438 47   HOH HOH D . 
AA 5 HOH 39  439 172  HOH HOH D . 
AA 5 HOH 40  440 180  HOH HOH D . 
AA 5 HOH 41  441 898  HOH HOH D . 
AA 5 HOH 42  442 217  HOH HOH D . 
AA 5 HOH 43  443 940  HOH HOH D . 
AA 5 HOH 44  444 822  HOH HOH D . 
AA 5 HOH 45  445 251  HOH HOH D . 
AA 5 HOH 46  446 1095 HOH HOH D . 
AA 5 HOH 47  447 339  HOH HOH D . 
AA 5 HOH 48  448 1010 HOH HOH D . 
AA 5 HOH 49  449 1090 HOH HOH D . 
AA 5 HOH 50  450 802  HOH HOH D . 
AA 5 HOH 51  451 481  HOH HOH D . 
AA 5 HOH 52  452 25   HOH HOH D . 
AA 5 HOH 53  453 290  HOH HOH D . 
AA 5 HOH 54  454 620  HOH HOH D . 
AA 5 HOH 55  455 815  HOH HOH D . 
AA 5 HOH 56  456 197  HOH HOH D . 
AA 5 HOH 57  457 22   HOH HOH D . 
AA 5 HOH 58  458 252  HOH HOH D . 
AA 5 HOH 59  459 799  HOH HOH D . 
AA 5 HOH 60  460 305  HOH HOH D . 
AA 5 HOH 61  461 97   HOH HOH D . 
AA 5 HOH 62  462 181  HOH HOH D . 
AA 5 HOH 63  463 16   HOH HOH D . 
AA 5 HOH 64  464 325  HOH HOH D . 
AA 5 HOH 65  465 487  HOH HOH D . 
AA 5 HOH 66  466 383  HOH HOH D . 
AA 5 HOH 67  467 29   HOH HOH D . 
AA 5 HOH 68  468 730  HOH HOH D . 
AA 5 HOH 69  469 519  HOH HOH D . 
AA 5 HOH 70  470 23   HOH HOH D . 
AA 5 HOH 71  471 697  HOH HOH D . 
AA 5 HOH 72  472 353  HOH HOH D . 
AA 5 HOH 73  473 352  HOH HOH D . 
AA 5 HOH 74  474 1076 HOH HOH D . 
AA 5 HOH 75  475 123  HOH HOH D . 
AA 5 HOH 76  476 402  HOH HOH D . 
AA 5 HOH 77  477 434  HOH HOH D . 
AA 5 HOH 78  478 313  HOH HOH D . 
AA 5 HOH 79  479 53   HOH HOH D . 
AA 5 HOH 80  480 296  HOH HOH D . 
AA 5 HOH 81  481 99   HOH HOH D . 
AA 5 HOH 82  482 839  HOH HOH D . 
AA 5 HOH 83  483 869  HOH HOH D . 
AA 5 HOH 84  484 441  HOH HOH D . 
AA 5 HOH 85  485 105  HOH HOH D . 
AA 5 HOH 86  486 418  HOH HOH D . 
AA 5 HOH 87  487 201  HOH HOH D . 
AA 5 HOH 88  488 476  HOH HOH D . 
AA 5 HOH 89  489 457  HOH HOH D . 
AA 5 HOH 90  490 767  HOH HOH D . 
AA 5 HOH 91  491 1092 HOH HOH D . 
AA 5 HOH 92  492 10   HOH HOH D . 
AA 5 HOH 93  493 761  HOH HOH D . 
AA 5 HOH 94  494 289  HOH HOH D . 
AA 5 HOH 95  495 1153 HOH HOH D . 
AA 5 HOH 96  496 51   HOH HOH D . 
AA 5 HOH 97  497 12   HOH HOH D . 
AA 5 HOH 98  498 6    HOH HOH D . 
AA 5 HOH 99  499 93   HOH HOH D . 
AA 5 HOH 100 500 540  HOH HOH D . 
AA 5 HOH 101 501 131  HOH HOH D . 
AA 5 HOH 102 502 42   HOH HOH D . 
AA 5 HOH 103 503 127  HOH HOH D . 
AA 5 HOH 104 504 155  HOH HOH D . 
AA 5 HOH 105 505 226  HOH HOH D . 
AA 5 HOH 106 506 159  HOH HOH D . 
AA 5 HOH 107 507 82   HOH HOH D . 
AA 5 HOH 108 508 126  HOH HOH D . 
AA 5 HOH 109 509 113  HOH HOH D . 
AA 5 HOH 110 510 18   HOH HOH D . 
AA 5 HOH 111 511 573  HOH HOH D . 
AA 5 HOH 112 512 467  HOH HOH D . 
AA 5 HOH 113 513 34   HOH HOH D . 
AA 5 HOH 114 514 732  HOH HOH D . 
AA 5 HOH 115 515 646  HOH HOH D . 
AA 5 HOH 116 516 420  HOH HOH D . 
AA 5 HOH 117 517 272  HOH HOH D . 
AA 5 HOH 118 518 840  HOH HOH D . 
AA 5 HOH 119 519 436  HOH HOH D . 
AA 5 HOH 120 520 128  HOH HOH D . 
AA 5 HOH 121 521 102  HOH HOH D . 
AA 5 HOH 122 522 379  HOH HOH D . 
AA 5 HOH 123 523 444  HOH HOH D . 
AA 5 HOH 124 524 125  HOH HOH D . 
AA 5 HOH 125 525 35   HOH HOH D . 
AA 5 HOH 126 526 91   HOH HOH D . 
AA 5 HOH 127 527 886  HOH HOH D . 
AA 5 HOH 128 528 828  HOH HOH D . 
AA 5 HOH 129 529 100  HOH HOH D . 
AA 5 HOH 130 530 68   HOH HOH D . 
AA 5 HOH 131 531 774  HOH HOH D . 
AA 5 HOH 132 532 1093 HOH HOH D . 
AA 5 HOH 133 533 397  HOH HOH D . 
AA 5 HOH 134 534 348  HOH HOH D . 
AA 5 HOH 135 535 218  HOH HOH D . 
AA 5 HOH 136 536 205  HOH HOH D . 
AA 5 HOH 137 537 591  HOH HOH D . 
AA 5 HOH 138 538 311  HOH HOH D . 
AA 5 HOH 139 539 745  HOH HOH D . 
AA 5 HOH 140 540 946  HOH HOH D . 
AA 5 HOH 141 541 1104 HOH HOH D . 
AA 5 HOH 142 542 162  HOH HOH D . 
AA 5 HOH 143 543 439  HOH HOH D . 
AA 5 HOH 144 544 1142 HOH HOH D . 
AA 5 HOH 145 545 257  HOH HOH D . 
AA 5 HOH 146 546 280  HOH HOH D . 
AA 5 HOH 147 547 547  HOH HOH D . 
AA 5 HOH 148 548 299  HOH HOH D . 
AA 5 HOH 149 549 1191 HOH HOH D . 
AA 5 HOH 150 550 1    HOH HOH D . 
AA 5 HOH 151 551 659  HOH HOH D . 
AA 5 HOH 152 552 821  HOH HOH D . 
AA 5 HOH 153 553 604  HOH HOH D . 
AA 5 HOH 154 554 502  HOH HOH D . 
AA 5 HOH 155 555 477  HOH HOH D . 
AA 5 HOH 156 556 312  HOH HOH D . 
AA 5 HOH 157 557 73   HOH HOH D . 
AA 5 HOH 158 558 45   HOH HOH D . 
AA 5 HOH 159 559 354  HOH HOH D . 
AA 5 HOH 160 560 304  HOH HOH D . 
AA 5 HOH 161 561 939  HOH HOH D . 
AA 5 HOH 162 562 243  HOH HOH D . 
AA 5 HOH 163 563 269  HOH HOH D . 
AA 5 HOH 164 564 173  HOH HOH D . 
AA 5 HOH 165 565 1188 HOH HOH D . 
AA 5 HOH 166 566 268  HOH HOH D . 
AA 5 HOH 167 567 559  HOH HOH D . 
AA 5 HOH 168 568 508  HOH HOH D . 
AA 5 HOH 169 569 122  HOH HOH D . 
AA 5 HOH 170 570 1120 HOH HOH D . 
AA 5 HOH 171 571 349  HOH HOH D . 
AA 5 HOH 172 572 301  HOH HOH D . 
AA 5 HOH 173 573 11   HOH HOH D . 
AA 5 HOH 174 574 1146 HOH HOH D . 
AA 5 HOH 175 575 124  HOH HOH D . 
AA 5 HOH 176 576 409  HOH HOH D . 
AA 5 HOH 177 577 849  HOH HOH D . 
AA 5 HOH 178 578 853  HOH HOH D . 
AA 5 HOH 179 579 50   HOH HOH D . 
AA 5 HOH 180 580 198  HOH HOH D . 
AA 5 HOH 181 581 440  HOH HOH D . 
AA 5 HOH 182 582 88   HOH HOH D . 
AA 5 HOH 183 583 49   HOH HOH D . 
AA 5 HOH 184 584 550  HOH HOH D . 
AA 5 HOH 185 585 647  HOH HOH D . 
AA 5 HOH 186 586 250  HOH HOH D . 
AA 5 HOH 187 587 909  HOH HOH D . 
AA 5 HOH 188 588 674  HOH HOH D . 
AA 5 HOH 189 589 94   HOH HOH D . 
AA 5 HOH 190 590 254  HOH HOH D . 
AA 5 HOH 191 591 823  HOH HOH D . 
AA 5 HOH 192 592 530  HOH HOH D . 
AA 5 HOH 193 593 189  HOH HOH D . 
AA 5 HOH 194 594 963  HOH HOH D . 
AA 5 HOH 195 595 1127 HOH HOH D . 
AA 5 HOH 196 596 1192 HOH HOH D . 
AA 5 HOH 197 597 973  HOH HOH D . 
AA 5 HOH 198 598 388  HOH HOH D . 
AA 5 HOH 199 599 733  HOH HOH D . 
AA 5 HOH 200 600 494  HOH HOH D . 
AA 5 HOH 201 601 174  HOH HOH D . 
AA 5 HOH 202 602 179  HOH HOH D . 
AA 5 HOH 203 603 868  HOH HOH D . 
AA 5 HOH 204 604 227  HOH HOH D . 
AA 5 HOH 205 605 438  HOH HOH D . 
AA 5 HOH 206 606 210  HOH HOH D . 
AA 5 HOH 207 607 1037 HOH HOH D . 
AA 5 HOH 208 608 341  HOH HOH D . 
AA 5 HOH 209 609 456  HOH HOH D . 
AA 5 HOH 210 610 274  HOH HOH D . 
AA 5 HOH 211 611 412  HOH HOH D . 
AA 5 HOH 212 612 246  HOH HOH D . 
AA 5 HOH 213 613 259  HOH HOH D . 
AA 5 HOH 214 614 92   HOH HOH D . 
AA 5 HOH 215 615 785  HOH HOH D . 
AA 5 HOH 216 616 629  HOH HOH D . 
AA 5 HOH 217 617 468  HOH HOH D . 
AA 5 HOH 218 618 600  HOH HOH D . 
AA 5 HOH 219 619 825  HOH HOH D . 
AA 5 HOH 220 620 807  HOH HOH D . 
AA 5 HOH 221 621 945  HOH HOH D . 
AA 5 HOH 222 622 480  HOH HOH D . 
AA 5 HOH 223 623 384  HOH HOH D . 
AA 5 HOH 224 624 764  HOH HOH D . 
AA 5 HOH 225 625 549  HOH HOH D . 
AA 5 HOH 226 626 224  HOH HOH D . 
AA 5 HOH 227 627 570  HOH HOH D . 
AA 5 HOH 228 628 204  HOH HOH D . 
AA 5 HOH 229 629 309  HOH HOH D . 
AA 5 HOH 230 630 583  HOH HOH D . 
AA 5 HOH 231 631 867  HOH HOH D . 
AA 5 HOH 232 632 621  HOH HOH D . 
AA 5 HOH 233 633 643  HOH HOH D . 
AA 5 HOH 234 634 956  HOH HOH D . 
AA 5 HOH 235 635 446  HOH HOH D . 
AA 5 HOH 236 636 942  HOH HOH D . 
AA 5 HOH 237 637 590  HOH HOH D . 
AA 5 HOH 238 638 899  HOH HOH D . 
AA 5 HOH 239 639 450  HOH HOH D . 
AA 5 HOH 240 640 399  HOH HOH D . 
AA 5 HOH 241 641 984  HOH HOH D . 
AA 5 HOH 242 642 746  HOH HOH D . 
AA 5 HOH 243 643 623  HOH HOH D . 
AA 5 HOH 244 644 820  HOH HOH D . 
AA 5 HOH 245 645 1077 HOH HOH D . 
AA 5 HOH 246 646 944  HOH HOH D . 
AA 5 HOH 247 647 1129 HOH HOH D . 
AA 5 HOH 248 648 1103 HOH HOH D . 
AA 5 HOH 249 649 908  HOH HOH D . 
AA 5 HOH 250 650 445  HOH HOH D . 
AA 5 HOH 251 651 819  HOH HOH D . 
AA 5 HOH 252 652 1115 HOH HOH D . 
AA 5 HOH 253 653 1027 HOH HOH D . 
AA 5 HOH 254 654 683  HOH HOH D . 
AA 5 HOH 255 655 786  HOH HOH D . 
AA 5 HOH 256 656 483  HOH HOH D . 
AA 5 HOH 257 657 1126 HOH HOH D . 
AA 5 HOH 258 658 797  HOH HOH D . 
AA 5 HOH 259 659 442  HOH HOH D . 
AA 5 HOH 260 660 1121 HOH HOH D . 
AA 5 HOH 261 661 437  HOH HOH D . 
AA 5 HOH 262 662 857  HOH HOH D . 
AA 5 HOH 263 663 1119 HOH HOH D . 
AA 5 HOH 264 664 738  HOH HOH D . 
AA 5 HOH 265 665 835  HOH HOH D . 
AA 5 HOH 266 666 495  HOH HOH D . 
AA 5 HOH 267 667 757  HOH HOH D . 
AA 5 HOH 268 668 1052 HOH HOH D . 
AA 5 HOH 269 669 186  HOH HOH D . 
AA 5 HOH 270 670 751  HOH HOH D . 
AA 5 HOH 271 671 890  HOH HOH D . 
AA 5 HOH 272 672 360  HOH HOH D . 
AA 5 HOH 273 673 776  HOH HOH D . 
AA 5 HOH 274 674 1141 HOH HOH D . 
AA 5 HOH 275 675 1053 HOH HOH D . 
AA 5 HOH 276 676 778  HOH HOH D . 
AA 5 HOH 277 677 846  HOH HOH D . 
AA 5 HOH 278 678 1062 HOH HOH D . 
AA 5 HOH 279 679 765  HOH HOH D . 
AA 5 HOH 280 680 847  HOH HOH D . 
AA 5 HOH 281 681 1089 HOH HOH D . 
AA 5 HOH 282 682 930  HOH HOH D . 
AA 5 HOH 283 683 1124 HOH HOH D . 
AA 5 HOH 284 684 463  HOH HOH D . 
AA 5 HOH 285 685 435  HOH HOH D . 
AA 5 HOH 286 686 448  HOH HOH D . 
AA 5 HOH 287 687 1097 HOH HOH D . 
AA 5 HOH 288 688 1101 HOH HOH D . 
AA 5 HOH 289 689 472  HOH HOH D . 
AA 5 HOH 290 690 482  HOH HOH D . 
AA 5 HOH 291 691 1190 HOH HOH D . 
AA 5 HOH 292 692 952  HOH HOH D . 
AA 5 HOH 293 693 1122 HOH HOH D . 
AA 5 HOH 294 694 1102 HOH HOH D . 
AA 5 HOH 295 695 665  HOH HOH D . 
AA 5 HOH 296 696 1028 HOH HOH D . 
AA 5 HOH 297 697 960  HOH HOH D . 
AA 5 HOH 298 698 1098 HOH HOH D . 
AA 5 HOH 299 699 749  HOH HOH D . 
AA 5 HOH 300 700 935  HOH HOH D . 
AA 5 HOH 301 701 1176 HOH HOH D . 
AA 5 HOH 302 702 866  HOH HOH D . 
AA 5 HOH 303 703 958  HOH HOH D . 
AA 5 HOH 304 704 241  HOH HOH D . 
AA 5 HOH 305 705 859  HOH HOH D . 
AA 5 HOH 306 706 421  HOH HOH D . 
AA 5 HOH 307 707 516  HOH HOH D . 
AA 5 HOH 308 708 1008 HOH HOH D . 
AA 5 HOH 309 709 1194 HOH HOH D . 
AA 5 HOH 310 710 885  HOH HOH D . 
AA 5 HOH 311 711 223  HOH HOH D . 
AA 5 HOH 312 712 1195 HOH HOH D . 
AA 5 HOH 313 713 1059 HOH HOH D . 
AA 5 HOH 314 714 170  HOH HOH D . 
AA 5 HOH 315 715 1189 HOH HOH D . 
AA 5 HOH 316 716 680  HOH HOH D . 
AA 5 HOH 317 717 664  HOH HOH D . 
AA 5 HOH 318 718 1091 HOH HOH D . 
AA 5 HOH 319 719 612  HOH HOH D . 
AA 5 HOH 320 720 1099 HOH HOH D . 
AA 5 HOH 321 721 910  HOH HOH D . 
AA 5 HOH 322 722 673  HOH HOH D . 
AA 5 HOH 323 723 775  HOH HOH D . 
AA 5 HOH 324 724 679  HOH HOH D . 
AA 5 HOH 325 725 1128 HOH HOH D . 
AA 5 HOH 326 726 881  HOH HOH D . 
AA 5 HOH 327 727 1100 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 A GLU 137 ? CD  ? A GLU 137 CD  
2  1 Y 1 A GLU 137 ? OE1 ? A GLU 137 OE1 
3  1 Y 1 A GLU 137 ? OE2 ? A GLU 137 OE2 
4  1 Y 1 B LYS 135 ? CG  ? B LYS 135 CG  
5  1 Y 1 B LYS 135 ? CD  ? B LYS 135 CD  
6  1 Y 1 B LYS 135 ? CE  ? B LYS 135 CE  
7  1 Y 1 B LYS 135 ? NZ  ? B LYS 135 NZ  
8  1 Y 1 B GLU 254 ? CD  ? B GLU 254 CD  
9  1 Y 1 B GLU 254 ? OE1 ? B GLU 254 OE1 
10 1 Y 1 B GLU 254 ? OE2 ? B GLU 254 OE2 
11 1 Y 1 C LYS 3   ? CD  ? C LYS 3   CD  
12 1 Y 1 C LYS 3   ? CE  ? C LYS 3   CE  
13 1 Y 1 C LYS 3   ? NZ  ? C LYS 3   NZ  
14 1 Y 1 C GLU 47  ? CD  ? C GLU 47  CD  
15 1 Y 1 C GLU 47  ? OE1 ? C GLU 47  OE1 
16 1 Y 1 C GLU 47  ? OE2 ? C GLU 47  OE2 
17 1 Y 1 C ASN 56  ? CG  ? C ASN 56  CG  
18 1 Y 1 C ASN 56  ? OD1 ? C ASN 56  OD1 
19 1 Y 1 C ASN 56  ? ND2 ? C ASN 56  ND2 
20 1 Y 1 C LYS 57  ? CB  ? C LYS 57  CB  
21 1 Y 1 C LYS 57  ? CG  ? C LYS 57  CG  
22 1 Y 1 C LYS 57  ? CD  ? C LYS 57  CD  
23 1 Y 1 C LYS 57  ? CE  ? C LYS 57  CE  
24 1 Y 1 C LYS 57  ? NZ  ? C LYS 57  NZ  
25 1 Y 1 C GLN 219 ? CG  ? C GLN 219 CG  
26 1 Y 1 C GLN 219 ? CD  ? C GLN 219 CD  
27 1 Y 1 C GLN 219 ? OE1 ? C GLN 219 OE1 
28 1 Y 1 C GLN 219 ? NE2 ? C GLN 219 NE2 
29 1 Y 1 C ASP 235 ? CG  ? C ASP 235 CG  
30 1 Y 1 C ASP 235 ? OD1 ? C ASP 235 OD1 
31 1 Y 1 C ASP 235 ? OD2 ? C ASP 235 OD2 
32 1 Y 1 C ARG 240 ? CG  ? C ARG 240 CG  
33 1 Y 1 C ARG 240 ? CD  ? C ARG 240 CD  
34 1 Y 1 C ARG 240 ? NE  ? C ARG 240 NE  
35 1 Y 1 C ARG 240 ? CZ  ? C ARG 240 CZ  
36 1 Y 1 C ARG 240 ? NH1 ? C ARG 240 NH1 
37 1 Y 1 C ARG 240 ? NH2 ? C ARG 240 NH2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement        ? ? ? ? ? ? ? ? ? ? ? REFMAC      ? ? ? 5.6.0117 1 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? SCALA       ? ? ? 3.3.20   2 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? 3.20     3 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? XDS         ? ? ? .        4 
? phasing           ? ? ? ? ? ? ? ? ? ? ? MOLREP      ? ? ? .        5 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   108.960 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     5LL5 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     77.418 
_cell.length_a_esd                 ? 
_cell.length_b                     73.962 
_cell.length_b_esd                 ? 
_cell.length_c                     91.328 
_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                         5LL5 
_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                   5LL5 
_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         39.9 
_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                         5LL5 
_reflns.data_reduction_details           ? 
_reflns.data_reduction_method            ? 
_reflns.d_resolution_high                1.420 
_reflns.d_resolution_low                 86.372 
_reflns.details                          ? 
_reflns.limit_h_max                      ? 
_reflns.limit_h_min                      ? 
_reflns.limit_k_max                      ? 
_reflns.limit_k_min                      ? 
_reflns.limit_l_max                      ? 
_reflns.limit_l_min                      ? 
_reflns.number_all                       ? 
_reflns.number_obs                       181799 
_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             99.200 
_reflns.R_free_details                   ? 
_reflns.Rmerge_F_all                     ? 
_reflns.Rmerge_F_obs                     ? 
_reflns.Friedel_coverage                 ? 
_reflns.number_gt                        ? 
_reflns.threshold_expression             ? 
_reflns.pdbx_redundancy                  6.900 
_reflns.pdbx_Rmerge_I_obs                ? 
_reflns.pdbx_Rmerge_I_all                ? 
_reflns.pdbx_Rsym_value                  0.056 
_reflns.pdbx_netI_over_av_sigmaI         6.385 
_reflns.pdbx_netI_over_sigmaI            15.900 
_reflns.pdbx_res_netI_over_av_sigmaI_2   ? 
_reflns.pdbx_res_netI_over_sigmaI_2      ? 
_reflns.pdbx_chi_squared                 ? 
_reflns.pdbx_scaling_rejects             ? 
_reflns.pdbx_d_res_high_opt              ? 
_reflns.pdbx_d_res_low_opt               ? 
_reflns.pdbx_d_res_opt_method            ? 
_reflns.phase_calculation_details        ? 
_reflns.pdbx_Rrim_I_all                  ? 
_reflns.pdbx_Rpim_I_all                  ? 
_reflns.pdbx_d_opt                       ? 
_reflns.pdbx_number_measured_all         ? 
_reflns.pdbx_diffrn_id                   1 
_reflns.pdbx_ordinal                     1 
_reflns.pdbx_CC_half                     ? 
_reflns.pdbx_R_split                     ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_measured_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.number_unique_obs 
_reflns_shell.percent_possible_all 
_reflns_shell.percent_possible_obs 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_gt 
_reflns_shell.meanI_over_uI_all 
_reflns_shell.meanI_over_uI_gt 
_reflns_shell.number_measured_gt 
_reflns_shell.number_unique_gt 
_reflns_shell.percent_possible_gt 
_reflns_shell.Rmerge_F_gt 
_reflns_shell.Rmerge_I_gt 
_reflns_shell.pdbx_redundancy 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_netI_over_sigmaI_all 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_rejects 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_R_split 
1.420 1.500  ? 2.000  ? ? ? ? ? 99.300 ? ? ? ? 0.388 ? ? ? ? ? ? ? ? 7.000 ? ? ? ? ? ? ? 1  1 ? ? 
1.500 1.590  ? 2.900  ? ? ? ? ? 99.000 ? ? ? ? 0.266 ? ? ? ? ? ? ? ? 6.800 ? ? ? ? ? ? ? 2  1 ? ? 
1.590 1.700  ? 4.200  ? ? ? ? ? 99.200 ? ? ? ? 0.183 ? ? ? ? ? ? ? ? 6.900 ? ? ? ? ? ? ? 3  1 ? ? 
1.700 1.830  ? 6.000  ? ? ? ? ? 99.100 ? ? ? ? 0.124 ? ? ? ? ? ? ? ? 7.000 ? ? ? ? ? ? ? 4  1 ? ? 
1.830 2.010  ? 8.500  ? ? ? ? ? 98.900 ? ? ? ? 0.081 ? ? ? ? ? ? ? ? 6.700 ? ? ? ? ? ? ? 5  1 ? ? 
2.010 2.250  ? 10.700 ? ? ? ? ? 99.500 ? ? ? ? 0.060 ? ? ? ? ? ? ? ? 7.100 ? ? ? ? ? ? ? 6  1 ? ? 
2.250 2.590  ? 11.900 ? ? ? ? ? 98.900 ? ? ? ? 0.050 ? ? ? ? ? ? ? ? 6.800 ? ? ? ? ? ? ? 7  1 ? ? 
2.590 3.180  ? 12.800 ? ? ? ? ? 99.500 ? ? ? ? 0.041 ? ? ? ? ? ? ? ? 7.200 ? ? ? ? ? ? ? 8  1 ? ? 
3.180 4.490  ? 13.200 ? ? ? ? ? 98.900 ? ? ? ? 0.035 ? ? ? ? ? ? ? ? 6.900 ? ? ? ? ? ? ? 9  1 ? ? 
4.490 86.372 ? 10.300 ? ? ? ? ? 99.400 ? ? ? ? 0.038 ? ? ? ? ? ? ? ? 6.800 ? ? ? ? ? ? ? 10 1 ? ? 
# 
_refine.aniso_B[1][1]                            -0.1000 
_refine.aniso_B[1][2]                            0.0000 
_refine.aniso_B[1][3]                            0.1900 
_refine.aniso_B[2][2]                            0.2400 
_refine.aniso_B[2][3]                            0.0000 
_refine.aniso_B[3][3]                            -0.0100 
_refine.B_iso_max                                80.420 
_refine.B_iso_mean                               18.0450 
_refine.B_iso_min                                5.810 
_refine.correlation_coeff_Fo_to_Fc               0.9730 
_refine.correlation_coeff_Fo_to_Fc_free          0.9640 
_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                                 5LL5 
_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                            1.4200 
_refine.ls_d_res_low                             67.7600 
_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                     163738 
_refine.ls_number_reflns_R_free                  18027 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.0700 
_refine.ls_percent_reflns_R_free                 9.9000 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1668 
_refine.ls_R_factor_R_free                       0.1932 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1639 
_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                       0.0690 
_refine.pdbx_overall_ESU_R_Free                  0.0700 
_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             0.0687 
_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                       1.4200 
_refine_hist.d_res_low                        67.7600 
_refine_hist.pdbx_number_atoms_ligand         162 
_refine_hist.number_atoms_solvent             1200 
_refine_hist.number_atoms_total               9718 
_refine_hist.pdbx_number_residues_total       1044 
_refine_hist.pdbx_B_iso_mean_ligand           28.98 
_refine_hist.pdbx_B_iso_mean_solvent          28.22 
_refine_hist.pdbx_number_atoms_protein        8356 
_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' ? 0.026  0.020  9075  ? r_bond_refined_d       ? ? 
'X-RAY DIFFRACTION' ? 2.306  1.958  12404 ? r_angle_refined_deg    ? ? 
'X-RAY DIFFRACTION' ? 7.263  5.000  1107  ? r_dihedral_angle_1_deg ? ? 
'X-RAY DIFFRACTION' ? 36.946 24.600 450   ? r_dihedral_angle_2_deg ? ? 
'X-RAY DIFFRACTION' ? 12.784 15.000 1387  ? r_dihedral_angle_3_deg ? ? 
'X-RAY DIFFRACTION' ? 15.629 15.000 34    ? r_dihedral_angle_4_deg ? ? 
'X-RAY DIFFRACTION' ? 0.168  0.200  1280  ? r_chiral_restr         ? ? 
'X-RAY DIFFRACTION' ? 0.015  0.021  7253  ? r_gen_planes_refined   ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.4200 
_refine_ls_shell.d_res_low                        1.4570 
_refine_ls_shell.number_reflns_all                13369 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             1324 
_refine_ls_shell.number_reflns_R_work             12045 
_refine_ls_shell.percent_reflns_obs               99.3000 
_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                  0.2550 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.2250 
_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                     5LL5 
_struct.title                        
'Crystal structure of human carbonic anhydrase isozyme XII with 4-(1H-benzimidazol-1-ylacetyl)benzenesulfonamide' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        5LL5 
_struct_keywords.text            
'drug design, carbonic anhydrase, benzenesulfonamide, metal-binding, lyase-lyase inhibitor complex, lyase' 
_struct_keywords.pdbx_keywords   LYASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A  N N 1 ? 
B  N N 1 ? 
C  N N 1 ? 
D  N N 1 ? 
E  N N 2 ? 
F  N N 3 ? 
G  N N 4 ? 
H  N N 4 ? 
I  N N 4 ? 
J  N N 2 ? 
K  N N 3 ? 
L  N N 4 ? 
M  N N 4 ? 
N  N N 4 ? 
O  N N 2 ? 
P  N N 3 ? 
Q  N N 4 ? 
R  N N 4 ? 
S  N N 2 ? 
T  N N 3 ? 
U  N N 4 ? 
V  N N 4 ? 
W  N N 4 ? 
X  N N 5 ? 
Y  N N 5 ? 
Z  N N 5 ? 
AA N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    CAH12_HUMAN 
_struct_ref.pdbx_db_accession          O43570 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;SKWTYFGPDGENSWSKKYPSCGGLLQSPIDLHSDILQYDASLTPLEFQGYNLSANKQFLLTNNGHSVKLNLPSDMHIQGL
QSRYSATQLHLHWGNPNDPHGSEHTVSGQHFAAELHIVHYNSDLYPDASTASNKSEGLAVLAVLIEMGSFNPSYDKIFSH
LQHVKYKGQEAFVPGFNIEELLPERTAEYYRYRGSLTTPPCNPTVLWTVFRNPVQISQEQLLALETALYCTHMDDPSPRE
MINNFRQVQKFDERLVYTSFSQ
;
_struct_ref.pdbx_align_begin           30 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 5LL5 A 2 ? 263 ? O43570 30 ? 291 ? 2 263 
2 1 5LL5 B 2 ? 263 ? O43570 30 ? 291 ? 2 263 
3 1 5LL5 C 2 ? 263 ? O43570 30 ? 291 ? 2 263 
4 1 5LL5 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 5LL5 MET A 1 ? UNP O43570 ? ? 'initiating methionine' 1 1 
2 5LL5 MET B 1 ? UNP O43570 ? ? 'initiating methionine' 1 2 
3 5LL5 MET C 1 ? UNP O43570 ? ? 'initiating methionine' 1 3 
4 5LL5 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,X,Y 
2 1 C,D,O,P,Q,R,S,T,U,V,W,Z,AA  
# 
_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  ? LYS A 18  ? GLY A 11  LYS A 18  5 ? 8  
HELX_P HELX_P2  AA2 TYR A 19  ? GLY A 24  ? TYR A 19  GLY A 24  5 ? 6  
HELX_P HELX_P3  AA3 HIS A 33  ? ASP A 35  ? HIS A 33  ASP A 35  5 ? 3  
HELX_P HELX_P4  AA4 ASP A 128 ? SER A 133 ? ASP A 128 SER A 133 1 ? 6  
HELX_P HELX_P5  AA5 ASN A 152 ? SER A 160 ? ASN A 152 SER A 160 1 ? 9  
HELX_P HELX_P6  AA6 HIS A 161 ? LYS A 166 ? HIS A 161 LYS A 166 5 ? 6  
HELX_P HELX_P7  AA7 ASN A 178 ? LEU A 183 ? ASN A 178 LEU A 183 5 ? 6  
HELX_P HELX_P8  AA8 SER A 218 ? ALA A 228 ? SER A 218 ALA A 228 1 ? 11 
HELX_P HELX_P9  AA9 SER B 14  ? LYS B 18  ? SER B 14  LYS B 18  5 ? 5  
HELX_P HELX_P10 AB1 TYR B 19  ? GLY B 24  ? TYR B 19  GLY B 24  5 ? 6  
HELX_P HELX_P11 AB2 HIS B 33  ? ASP B 35  ? HIS B 33  ASP B 35  5 ? 3  
HELX_P HELX_P12 AB3 ASP B 128 ? SER B 133 ? ASP B 128 SER B 133 1 ? 6  
HELX_P HELX_P13 AB4 ASN B 152 ? SER B 160 ? ASN B 152 SER B 160 1 ? 9  
HELX_P HELX_P14 AB5 HIS B 161 ? VAL B 165 ? HIS B 161 VAL B 165 5 ? 5  
HELX_P HELX_P15 AB6 ASN B 178 ? LEU B 183 ? ASN B 178 LEU B 183 5 ? 6  
HELX_P HELX_P16 AB7 SER B 218 ? ALA B 228 ? SER B 218 ALA B 228 1 ? 11 
HELX_P HELX_P17 AB8 PHE C 7   ? ASN C 13  ? PHE C 7   ASN C 13  5 ? 7  
HELX_P HELX_P18 AB9 SER C 14  ? TYR C 19  ? SER C 14  TYR C 19  1 ? 6  
HELX_P HELX_P19 AC1 PRO C 20  ? GLY C 24  ? PRO C 20  GLY C 24  5 ? 5  
HELX_P HELX_P20 AC2 HIS C 33  ? ASP C 35  ? HIS C 33  ASP C 35  5 ? 3  
HELX_P HELX_P21 AC3 ASP C 128 ? SER C 133 ? ASP C 128 SER C 133 1 ? 6  
HELX_P HELX_P22 AC4 ASN C 152 ? SER C 160 ? ASN C 152 SER C 160 1 ? 9  
HELX_P HELX_P23 AC5 HIS C 161 ? VAL C 165 ? HIS C 161 VAL C 165 5 ? 5  
HELX_P HELX_P24 AC6 ASN C 178 ? LEU C 183 ? ASN C 178 LEU C 183 5 ? 6  
HELX_P HELX_P25 AC7 SER C 218 ? ALA C 228 ? SER C 218 ALA C 228 1 ? 11 
HELX_P HELX_P26 AC8 GLY D 11  ? ASN D 13  ? GLY D 11  ASN D 13  5 ? 3  
HELX_P HELX_P27 AC9 SER D 14  ? TYR D 19  ? SER D 14  TYR D 19  1 ? 6  
HELX_P HELX_P28 AD1 PRO D 20  ? GLY D 24  ? PRO D 20  GLY D 24  5 ? 5  
HELX_P HELX_P29 AD2 HIS D 33  ? ASP D 35  ? HIS D 33  ASP D 35  5 ? 3  
HELX_P HELX_P30 AD3 ASP D 128 ? SER D 133 ? ASP D 128 SER D 133 1 ? 6  
HELX_P HELX_P31 AD4 ASN D 152 ? SER D 160 ? ASN D 152 SER D 160 1 ? 9  
HELX_P HELX_P32 AD5 HIS D 161 ? VAL D 165 ? HIS D 161 VAL D 165 5 ? 5  
HELX_P HELX_P33 AD6 ASN D 178 ? LEU D 183 ? ASN D 178 LEU D 183 5 ? 6  
HELX_P HELX_P34 AD7 SER D 218 ? LEU D 229 ? SER D 218 LEU D 229 1 ? 12 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1  disulf ? ? A CYS 22  SG  ? ? ? 1_555 A CYS 202 SG  ? ? A CYS 22  A CYS 202 1_555 ? ? ? ? ? ? ? 2.037 ? ? 
disulf2  disulf ? ? B CYS 22  SG  ? ? ? 1_555 B CYS 202 SG  ? ? B CYS 22  B CYS 202 1_555 ? ? ? ? ? ? ? 2.039 ? ? 
disulf3  disulf ? ? C CYS 22  SG  ? ? ? 1_555 C CYS 202 SG  ? ? C CYS 22  C CYS 202 1_555 ? ? ? ? ? ? ? 2.077 ? ? 
disulf4  disulf ? ? D CYS 22  SG  ? ? ? 1_555 D CYS 202 SG  ? ? D CYS 22  D CYS 202 1_555 ? ? ? ? ? ? ? 2.025 ? ? 
metalc1  metalc ? ? A HIS 91  NE2 ? ? ? 1_555 E ZN  .   ZN  ? ? A HIS 91  A ZN  301 1_555 ? ? ? ? ? ? ? 2.012 ? ? 
metalc2  metalc ? ? A HIS 93  NE2 ? ? ? 1_555 E ZN  .   ZN  ? ? A HIS 93  A ZN  301 1_555 ? ? ? ? ? ? ? 1.997 ? ? 
metalc3  metalc ? ? A HIS 117 ND1 ? ? ? 1_555 E ZN  .   ZN  ? ? A HIS 117 A ZN  301 1_555 ? ? ? ? ? ? ? 2.021 ? ? 
metalc4  metalc ? ? E ZN  .   ZN  ? ? ? 1_555 F 6YH .   S7  ? ? A ZN  301 A 6YH 302 1_555 ? ? ? ? ? ? ? 2.969 ? ? 
metalc5  metalc ? ? E ZN  .   ZN  ? ? ? 1_555 F 6YH .   N10 ? ? A ZN  301 A 6YH 302 1_555 ? ? ? ? ? ? ? 1.906 ? ? 
metalc6  metalc ? ? B HIS 91  NE2 ? ? ? 1_555 J ZN  .   ZN  ? ? B HIS 91  B ZN  301 1_555 ? ? ? ? ? ? ? 1.973 ? ? 
metalc7  metalc ? ? B HIS 93  NE2 ? ? ? 1_555 J ZN  .   ZN  ? ? B HIS 93  B ZN  301 1_555 ? ? ? ? ? ? ? 2.026 ? ? 
metalc8  metalc ? ? B HIS 117 ND1 ? ? ? 1_555 J ZN  .   ZN  ? ? B HIS 117 B ZN  301 1_555 ? ? ? ? ? ? ? 2.047 ? ? 
metalc9  metalc ? ? J ZN  .   ZN  ? ? ? 1_555 K 6YH .   N10 ? ? B ZN  301 B 6YH 302 1_555 ? ? ? ? ? ? ? 1.856 ? ? 
metalc10 metalc ? ? C HIS 91  NE2 ? ? ? 1_555 O ZN  .   ZN  ? ? C HIS 91  C ZN  301 1_555 ? ? ? ? ? ? ? 2.017 ? ? 
metalc11 metalc ? ? C HIS 93  NE2 ? ? ? 1_555 O ZN  .   ZN  ? ? C HIS 93  C ZN  301 1_555 ? ? ? ? ? ? ? 2.008 ? ? 
metalc12 metalc ? ? C HIS 117 ND1 ? ? ? 1_555 O ZN  .   ZN  ? ? C HIS 117 C ZN  301 1_555 ? ? ? ? ? ? ? 2.007 ? ? 
metalc13 metalc ? ? O ZN  .   ZN  ? ? ? 1_555 P 6YH .   S7  ? ? C ZN  301 C 6YH 302 1_555 ? ? ? ? ? ? ? 2.985 ? ? 
metalc14 metalc ? ? O ZN  .   ZN  ? ? ? 1_555 P 6YH .   N10 ? ? C ZN  301 C 6YH 302 1_555 ? ? ? ? ? ? ? 1.909 ? ? 
metalc15 metalc ? ? D HIS 91  NE2 ? ? ? 1_555 S ZN  .   ZN  ? ? D HIS 91  D ZN  301 1_555 ? ? ? ? ? ? ? 2.005 ? ? 
metalc16 metalc ? ? D HIS 93  NE2 ? ? ? 1_555 S ZN  .   ZN  ? ? D HIS 93  D ZN  301 1_555 ? ? ? ? ? ? ? 1.975 ? ? 
metalc17 metalc ? ? D HIS 117 ND1 ? ? ? 1_555 S ZN  .   ZN  ? ? D HIS 117 D ZN  301 1_555 ? ? ? ? ? ? ? 2.015 ? ? 
metalc18 metalc ? ? S ZN  .   ZN  ? ? ? 1_555 T 6YH .   N10 A ? D ZN  301 D 6YH 302 1_555 ? ? ? ? ? ? ? 1.898 ? ? 
metalc19 metalc ? ? S ZN  .   ZN  ? ? ? 1_555 T 6YH .   N10 B ? D ZN  301 D 6YH 302 1_555 ? ? ? ? ? ? ? 1.933 ? ? 
# 
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_555 103.1 ? 
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_555 112.9 ? 
3  NE2 ? A HIS 93  ? A HIS 93  ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS 117 ? A HIS 117 ? 1_555 98.5  ? 
4  NE2 ? A HIS 91  ? A HIS 91  ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 S7  ? F 6YH .   ? A 6YH 302 ? 1_555 99.3  ? 
5  NE2 ? A HIS 93  ? A HIS 93  ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 S7  ? F 6YH .   ? A 6YH 302 ? 1_555 142.5 ? 
6  ND1 ? A HIS 117 ? A HIS 117 ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 S7  ? F 6YH .   ? A 6YH 302 ? 1_555 100.1 ? 
7  NE2 ? A HIS 91  ? A HIS 91  ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 N10 ? F 6YH .   ? A 6YH 302 ? 1_555 108.8 ? 
8  NE2 ? A HIS 93  ? A HIS 93  ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 N10 ? F 6YH .   ? A 6YH 302 ? 1_555 115.3 ? 
9  ND1 ? A HIS 117 ? A HIS 117 ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 N10 ? F 6YH .   ? A 6YH 302 ? 1_555 117.3 ? 
10 S7  ? F 6YH .   ? A 6YH 302 ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 N10 ? F 6YH .   ? A 6YH 302 ? 1_555 27.6  ? 
11 NE2 ? B HIS 91  ? B HIS 91  ? 1_555 ZN ? J ZN . ? B ZN 301 ? 1_555 NE2 ? B HIS 93  ? B HIS 93  ? 1_555 104.9 ? 
12 NE2 ? B HIS 91  ? B HIS 91  ? 1_555 ZN ? J ZN . ? B ZN 301 ? 1_555 ND1 ? B HIS 117 ? B HIS 117 ? 1_555 111.0 ? 
13 NE2 ? B HIS 93  ? B HIS 93  ? 1_555 ZN ? J ZN . ? B ZN 301 ? 1_555 ND1 ? B HIS 117 ? B HIS 117 ? 1_555 99.7  ? 
14 NE2 ? B HIS 91  ? B HIS 91  ? 1_555 ZN ? J ZN . ? B ZN 301 ? 1_555 N10 ? K 6YH .   ? B 6YH 302 ? 1_555 108.9 ? 
15 NE2 ? B HIS 93  ? B HIS 93  ? 1_555 ZN ? J ZN . ? B ZN 301 ? 1_555 N10 ? K 6YH .   ? B 6YH 302 ? 1_555 114.6 ? 
16 ND1 ? B HIS 117 ? B HIS 117 ? 1_555 ZN ? J ZN . ? B ZN 301 ? 1_555 N10 ? K 6YH .   ? B 6YH 302 ? 1_555 116.9 ? 
17 NE2 ? C HIS 91  ? C HIS 91  ? 1_555 ZN ? O ZN . ? C ZN 301 ? 1_555 NE2 ? C HIS 93  ? C HIS 93  ? 1_555 100.7 ? 
18 NE2 ? C HIS 91  ? C HIS 91  ? 1_555 ZN ? O ZN . ? C ZN 301 ? 1_555 ND1 ? C HIS 117 ? C HIS 117 ? 1_555 112.2 ? 
19 NE2 ? C HIS 93  ? C HIS 93  ? 1_555 ZN ? O ZN . ? C ZN 301 ? 1_555 ND1 ? C HIS 117 ? C HIS 117 ? 1_555 99.1  ? 
20 NE2 ? C HIS 91  ? C HIS 91  ? 1_555 ZN ? O ZN . ? C ZN 301 ? 1_555 S7  ? P 6YH .   ? C 6YH 302 ? 1_555 100.3 ? 
21 NE2 ? C HIS 93  ? C HIS 93  ? 1_555 ZN ? O ZN . ? C ZN 301 ? 1_555 S7  ? P 6YH .   ? C 6YH 302 ? 1_555 146.3 ? 
22 ND1 ? C HIS 117 ? C HIS 117 ? 1_555 ZN ? O ZN . ? C ZN 301 ? 1_555 S7  ? P 6YH .   ? C 6YH 302 ? 1_555 97.0  ? 
23 NE2 ? C HIS 91  ? C HIS 91  ? 1_555 ZN ? O ZN . ? C ZN 301 ? 1_555 N10 ? P 6YH .   ? C 6YH 302 ? 1_555 110.2 ? 
24 NE2 ? C HIS 93  ? C HIS 93  ? 1_555 ZN ? O ZN . ? C ZN 301 ? 1_555 N10 ? P 6YH .   ? C 6YH 302 ? 1_555 117.3 ? 
25 ND1 ? C HIS 117 ? C HIS 117 ? 1_555 ZN ? O ZN . ? C ZN 301 ? 1_555 N10 ? P 6YH .   ? C 6YH 302 ? 1_555 116.0 ? 
26 S7  ? P 6YH .   ? C 6YH 302 ? 1_555 ZN ? O ZN . ? C ZN 301 ? 1_555 N10 ? P 6YH .   ? C 6YH 302 ? 1_555 29.5  ? 
27 NE2 ? D HIS 91  ? D HIS 91  ? 1_555 ZN ? S ZN . ? D ZN 301 ? 1_555 NE2 ? D HIS 93  ? D HIS 93  ? 1_555 104.0 ? 
28 NE2 ? D HIS 91  ? D HIS 91  ? 1_555 ZN ? S ZN . ? D ZN 301 ? 1_555 ND1 ? D HIS 117 ? D HIS 117 ? 1_555 112.2 ? 
29 NE2 ? D HIS 93  ? D HIS 93  ? 1_555 ZN ? S ZN . ? D ZN 301 ? 1_555 ND1 ? D HIS 117 ? D HIS 117 ? 1_555 98.4  ? 
30 NE2 ? D HIS 91  ? D HIS 91  ? 1_555 ZN ? S ZN . ? D ZN 301 ? 1_555 N10 A T 6YH .   ? D 6YH 302 ? 1_555 108.4 ? 
31 NE2 ? D HIS 93  ? D HIS 93  ? 1_555 ZN ? S ZN . ? D ZN 301 ? 1_555 N10 A T 6YH .   ? D 6YH 302 ? 1_555 114.2 ? 
32 ND1 ? D HIS 117 ? D HIS 117 ? 1_555 ZN ? S ZN . ? D ZN 301 ? 1_555 N10 A T 6YH .   ? D 6YH 302 ? 1_555 118.5 ? 
33 NE2 ? D HIS 91  ? D HIS 91  ? 1_555 ZN ? S ZN . ? D ZN 301 ? 1_555 N10 B T 6YH .   ? D 6YH 302 ? 1_555 109.4 ? 
34 NE2 ? D HIS 93  ? D HIS 93  ? 1_555 ZN ? S ZN . ? D ZN 301 ? 1_555 N10 B T 6YH .   ? D 6YH 302 ? 1_555 115.0 ? 
35 ND1 ? D HIS 117 ? D HIS 117 ? 1_555 ZN ? S ZN . ? D ZN 301 ? 1_555 N10 B T 6YH .   ? D 6YH 302 ? 1_555 116.9 ? 
36 N10 A T 6YH .   ? D 6YH 302 ? 1_555 ZN ? S ZN . ? D ZN 301 ? 1_555 N10 B T 6YH .   ? D 6YH 302 ? 1_555 1.6   ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 CYS A 22 ? CYS A 202 ? CYS A 22 ? 1_555 CYS A 202 ? 1_555 SG SG . . . None 'Disulfide bridge' 
2 CYS B 22 ? CYS B 202 ? CYS B 22 ? 1_555 CYS B 202 ? 1_555 SG SG . . . None 'Disulfide bridge' 
3 CYS C 22 ? CYS C 202 ? CYS C 22 ? 1_555 CYS C 202 ? 1_555 SG SG . . . None 'Disulfide bridge' 
4 CYS D 22 ? CYS D 202 ? CYS D 22 ? 1_555 CYS D 202 ? 1_555 SG SG . . . None 'Disulfide bridge' 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 SER 28  A . ? SER 28  A PRO 29  A ? PRO 29  A 1 3.03  
2 PRO 200 A . ? PRO 200 A PRO 201 A ? PRO 201 A 1 16.08 
3 SER 28  B . ? SER 28  B PRO 29  B ? PRO 29  B 1 -5.27 
4 PRO 200 B . ? PRO 200 B PRO 201 B ? PRO 201 B 1 8.14  
5 PRO 200 B . ? PRO 200 B PRO 201 B ? PRO 201 B 1 5.15  
6 SER 28  C . ? SER 28  C PRO 29  C ? PRO 29  C 1 2.53  
7 PRO 200 C . ? PRO 200 C PRO 201 C ? PRO 201 C 1 6.76  
8 SER 28  D . ? SER 28  D PRO 29  D ? PRO 29  D 1 0.07  
9 PRO 200 D . ? PRO 200 D PRO 201 D ? PRO 201 D 1 2.62  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2  ? 
AA2 ? 10 ? 
AA3 ? 6  ? 
AA4 ? 2  ? 
AA5 ? 10 ? 
AA6 ? 6  ? 
AA7 ? 2  ? 
AA8 ? 10 ? 
AA9 ? 6  ? 
AB1 ? 2  ? 
AB2 ? 10 ? 
AB3 ? 6  ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2  ? parallel      
AA2 1 2  ? parallel      
AA2 2 3  ? anti-parallel 
AA2 3 4  ? anti-parallel 
AA2 4 5  ? parallel      
AA2 5 6  ? anti-parallel 
AA2 6 7  ? anti-parallel 
AA2 7 8  ? anti-parallel 
AA2 8 9  ? anti-parallel 
AA2 9 10 ? anti-parallel 
AA3 1 2  ? anti-parallel 
AA3 2 3  ? anti-parallel 
AA3 3 4  ? anti-parallel 
AA3 4 5  ? anti-parallel 
AA3 5 6  ? parallel      
AA4 1 2  ? parallel      
AA5 1 2  ? parallel      
AA5 2 3  ? anti-parallel 
AA5 3 4  ? anti-parallel 
AA5 4 5  ? parallel      
AA5 5 6  ? anti-parallel 
AA5 6 7  ? anti-parallel 
AA5 7 8  ? anti-parallel 
AA5 8 9  ? anti-parallel 
AA5 9 10 ? anti-parallel 
AA6 1 2  ? anti-parallel 
AA6 2 3  ? anti-parallel 
AA6 3 4  ? anti-parallel 
AA6 4 5  ? anti-parallel 
AA6 5 6  ? parallel      
AA7 1 2  ? parallel      
AA8 1 2  ? parallel      
AA8 2 3  ? anti-parallel 
AA8 3 4  ? anti-parallel 
AA8 4 5  ? parallel      
AA8 5 6  ? anti-parallel 
AA8 6 7  ? anti-parallel 
AA8 7 8  ? anti-parallel 
AA8 8 9  ? anti-parallel 
AA8 9 10 ? anti-parallel 
AA9 1 2  ? anti-parallel 
AA9 2 3  ? anti-parallel 
AA9 3 4  ? anti-parallel 
AA9 4 5  ? anti-parallel 
AA9 5 6  ? parallel      
AB1 1 2  ? parallel      
AB2 1 2  ? parallel      
AB2 2 3  ? anti-parallel 
AB2 3 4  ? anti-parallel 
AB2 4 5  ? parallel      
AB2 5 6  ? anti-parallel 
AB2 6 7  ? anti-parallel 
AB2 7 8  ? anti-parallel 
AB2 8 9  ? anti-parallel 
AB2 9 10 ? anti-parallel 
AB3 1 2  ? anti-parallel 
AB3 2 3  ? anti-parallel 
AB3 3 4  ? anti-parallel 
AB3 4 5  ? anti-parallel 
AB3 5 6  ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1  ASP A 31  ? LEU A 32  ? ASP A 31  LEU A 32  
AA1 2  THR A 106 ? VAL A 107 ? THR A 106 VAL A 107 
AA2 1  LEU A 37  ? TYR A 39  ? LEU A 37  TYR A 39  
AA2 2  VAL A 257 ? THR A 259 ? VAL A 257 THR A 259 
AA2 3  TYR A 190 ? GLY A 195 ? TYR A 190 GLY A 195 
AA2 4  VAL A 206 ? PHE A 211 ? VAL A 206 PHE A 211 
AA2 5  LEU A 139 ? MET A 148 ? LEU A 139 MET A 148 
AA2 6  ALA A 114 ? ASN A 122 ? ALA A 114 ASN A 122 
AA2 7  TYR A 85  ? TRP A 94  ? TYR A 85  TRP A 94  
AA2 8  VAL A 68  ? ASN A 71  ? VAL A 68  ASN A 71  
AA2 9  GLN A 58  ? ASN A 63  ? GLN A 58  ASN A 63  
AA2 10 GLU A 171 ? PRO A 175 ? GLU A 171 PRO A 175 
AA3 1  GLU A 47  ? GLN A 49  ? GLU A 47  GLN A 49  
AA3 2  HIS A 77  ? GLN A 79  ? HIS A 77  GLN A 79  
AA3 3  TYR A 85  ? TRP A 94  ? TYR A 85  TRP A 94  
AA3 4  ALA A 114 ? ASN A 122 ? ALA A 114 ASN A 122 
AA3 5  LEU A 139 ? MET A 148 ? LEU A 139 MET A 148 
AA3 6  VAL A 215 ? ILE A 217 ? VAL A 215 ILE A 217 
AA4 1  ASP B 31  ? LEU B 32  ? ASP B 31  LEU B 32  
AA4 2  THR B 106 ? VAL B 107 ? THR B 106 VAL B 107 
AA5 1  LEU B 37  ? TYR B 39  ? LEU B 37  TYR B 39  
AA5 2  VAL B 257 ? THR B 259 ? VAL B 257 THR B 259 
AA5 3  TYR B 190 ? GLY B 195 ? TYR B 190 GLY B 195 
AA5 4  VAL B 206 ? PHE B 211 ? VAL B 206 PHE B 211 
AA5 5  LEU B 139 ? MET B 148 ? LEU B 139 MET B 148 
AA5 6  ALA B 114 ? ASN B 122 ? ALA B 114 ASN B 122 
AA5 7  TYR B 85  ? TRP B 94  ? TYR B 85  TRP B 94  
AA5 8  VAL B 68  ? ASN B 71  ? VAL B 68  ASN B 71  
AA5 9  GLN B 58  ? ASN B 63  ? GLN B 58  ASN B 63  
AA5 10 GLU B 171 ? PRO B 175 ? GLU B 171 PRO B 175 
AA6 1  GLU B 47  ? GLN B 49  ? GLU B 47  GLN B 49  
AA6 2  HIS B 77  ? GLN B 79  ? HIS B 77  GLN B 79  
AA6 3  TYR B 85  ? TRP B 94  ? TYR B 85  TRP B 94  
AA6 4  ALA B 114 ? ASN B 122 ? ALA B 114 ASN B 122 
AA6 5  LEU B 139 ? MET B 148 ? LEU B 139 MET B 148 
AA6 6  VAL B 215 ? ILE B 217 ? VAL B 215 ILE B 217 
AA7 1  ASP C 31  ? LEU C 32  ? ASP C 31  LEU C 32  
AA7 2  THR C 106 ? VAL C 107 ? THR C 106 VAL C 107 
AA8 1  LEU C 37  ? TYR C 39  ? LEU C 37  TYR C 39  
AA8 2  VAL C 257 ? THR C 259 ? VAL C 257 THR C 259 
AA8 3  TYR C 190 ? GLY C 195 ? TYR C 190 GLY C 195 
AA8 4  VAL C 206 ? PHE C 211 ? VAL C 206 PHE C 211 
AA8 5  LEU C 139 ? MET C 148 ? LEU C 139 MET C 148 
AA8 6  ALA C 114 ? ASN C 122 ? ALA C 114 ASN C 122 
AA8 7  TYR C 85  ? TRP C 94  ? TYR C 85  TRP C 94  
AA8 8  VAL C 68  ? ASN C 71  ? VAL C 68  ASN C 71  
AA8 9  GLN C 58  ? ASN C 63  ? GLN C 58  ASN C 63  
AA8 10 GLU C 171 ? PRO C 175 ? GLU C 171 PRO C 175 
AA9 1  GLU C 47  ? GLN C 49  ? GLU C 47  GLN C 49  
AA9 2  HIS C 77  ? GLN C 79  ? HIS C 77  GLN C 79  
AA9 3  TYR C 85  ? TRP C 94  ? TYR C 85  TRP C 94  
AA9 4  ALA C 114 ? ASN C 122 ? ALA C 114 ASN C 122 
AA9 5  LEU C 139 ? MET C 148 ? LEU C 139 MET C 148 
AA9 6  VAL C 215 ? ILE C 217 ? VAL C 215 ILE C 217 
AB1 1  ASP D 31  ? LEU D 32  ? ASP D 31  LEU D 32  
AB1 2  THR D 106 ? VAL D 107 ? THR D 106 VAL D 107 
AB2 1  LEU D 37  ? TYR D 39  ? LEU D 37  TYR D 39  
AB2 2  VAL D 257 ? THR D 259 ? VAL D 257 THR D 259 
AB2 3  TYR D 190 ? GLY D 195 ? TYR D 190 GLY D 195 
AB2 4  VAL D 206 ? PHE D 211 ? VAL D 206 PHE D 211 
AB2 5  LEU D 139 ? MET D 148 ? LEU D 139 MET D 148 
AB2 6  ALA D 114 ? ASN D 122 ? ALA D 114 ASN D 122 
AB2 7  TYR D 85  ? TRP D 94  ? TYR D 85  TRP D 94  
AB2 8  VAL D 68  ? ASN D 71  ? VAL D 68  ASN D 71  
AB2 9  GLN D 58  ? ASN D 63  ? GLN D 58  ASN D 63  
AB2 10 GLU D 171 ? PRO D 175 ? GLU D 171 PRO D 175 
AB3 1  GLU D 47  ? GLN D 49  ? GLU D 47  GLN D 49  
AB3 2  HIS D 77  ? GLN D 79  ? HIS D 77  GLN D 79  
AB3 3  TYR D 85  ? TRP D 94  ? TYR D 85  TRP D 94  
AB3 4  ALA D 114 ? ASN D 122 ? ALA D 114 ASN D 122 
AB3 5  LEU D 139 ? MET D 148 ? LEU D 139 MET D 148 
AB3 6  VAL D 215 ? ILE D 217 ? VAL D 215 ILE D 217 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2  N LEU A 32  ? N LEU A 32  O THR A 106 ? O THR A 106 
AA2 1 2  N GLN A 38  ? N GLN A 38  O VAL A 257 ? O VAL A 257 
AA2 2 3  O TYR A 258 ? O TYR A 258 N ARG A 192 ? N ARG A 192 
AA2 3 4  N TYR A 191 ? N TYR A 191 O VAL A 210 ? O VAL A 210 
AA2 4 5  O THR A 209 ? O THR A 209 N ALA A 143 ? N ALA A 143 
AA2 5 6  O 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 GLU A 47  ? N GLU A 47  O GLN A 79  ? O GLN A 79  
AA3 2 3  N ILE A 78  ? N ILE A 78  O TYR A 85  ? O TYR A 85  
AA3 3 4  N GLN A 89  ? N GLN A 89  O VAL A 119 ? O VAL A 119 
AA3 4 5  N ALA A 114 ? N ALA A 114 O ILE A 146 ? O ILE A 146 
AA3 5 6  N GLU A 147 ? N GLU A 147 O VAL A 215 ? O VAL A 215 
AA4 1 2  N LEU B 32  ? N LEU B 32  O THR B 106 ? O THR B 106 
AA5 1 2  N GLN B 38  ? N GLN B 38  O VAL B 257 ? O VAL B 257 
AA5 2 3  O TYR B 258 ? O TYR B 258 N ARG B 192 ? N ARG B 192 
AA5 3 4  N TYR B 191 ? N TYR B 191 O VAL B 210 ? O VAL B 210 
AA5 4 5  O THR B 209 ? O THR B 209 N ALA B 143 ? N ALA B 143 
AA5 5 6  O LEU B 142 ? O LEU B 142 N ILE B 118 ? N ILE B 118 
AA5 6 7  O VAL B 119 ? O VAL B 119 N GLN B 89  ? N GLN B 89  
AA5 7 8  O LEU B 90  ? O LEU B 90  N LEU B 70  ? N LEU B 70  
AA5 8 9  O 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 THR C 259 ? O THR C 259 
AA8 2 3  O TYR C 258 ? O TYR C 258 N ARG C 192 ? N ARG C 192 
AA8 3 4  N GLY C 195 ? N GLY C 195 O VAL C 206 ? O VAL C 206 
AA8 4 5  O THR C 209 ? O THR C 209 N ALA C 143 ? N ALA C 143 
AA8 5 6  O LEU C 142 ? O LEU C 142 N ILE C 118 ? N ILE C 118 
AA8 6 7  O VAL C 119 ? O VAL C 119 N GLN C 89  ? N GLN C 89  
AA8 7 8  O LEU C 90  ? O LEU C 90  N LEU C 70  ? N LEU C 70  
AA8 8 9  O ASN C 71  ? O ASN C 71  N LEU C 60  ? N LEU C 60  
AA8 9 10 N LEU C 61  ? N LEU C 61  O ALA C 172 ? O ALA C 172 
AA9 1 2  N GLN C 49  ? N GLN C 49  O HIS C 77  ? O HIS C 77  
AA9 2 3  N ILE C 78  ? N ILE C 78  O TYR C 85  ? O TYR C 85  
AA9 3 4  N GLN C 89  ? N GLN C 89  O VAL C 119 ? O VAL C 119 
AA9 4 5  N ILE C 118 ? N ILE C 118 O LEU C 142 ? O LEU C 142 
AA9 5 6  N GLU C 147 ? N GLU C 147 O VAL C 215 ? O VAL C 215 
AB1 1 2  N LEU D 32  ? N LEU D 32  O THR D 106 ? O THR D 106 
AB2 1 2  N GLN D 38  ? N GLN D 38  O VAL D 257 ? O VAL D 257 
AB2 2 3  O TYR D 258 ? O TYR D 258 N ARG D 192 ? N ARG D 192 
AB2 3 4  N TYR D 191 ? N TYR D 191 O VAL D 210 ? O VAL D 210 
AB2 4 5  O THR D 209 ? O THR D 209 N ALA D 143 ? N ALA D 143 
AB2 5 6  O 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 6YH 302 ? 13 'binding site for residue 6YH A 302' 
AC3 Software A EDO 303 ? 3  '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 ? 4  'binding site for residue EDO A 305' 
AC6 Software B ZN  301 ? 4  'binding site for residue ZN B 301'  
AC7 Software B 6YH 302 ? 12 'binding site for residue 6YH B 302' 
AC8 Software B EDO 303 ? 6  'binding site for residue EDO B 303' 
AC9 Software B EDO 304 ? 6  'binding site for residue EDO B 304' 
AD1 Software B EDO 305 ? 4  'binding site for residue EDO B 305' 
AD2 Software C ZN  301 ? 4  'binding site for residue ZN C 301'  
AD3 Software C 6YH 302 ? 15 'binding site for residue 6YH C 302' 
AD4 Software C EDO 303 ? 6  'binding site for residue EDO C 303' 
AD5 Software C EDO 304 ? 4  'binding site for residue EDO C 304' 
AD6 Software D ZN  301 ? 4  'binding site for residue ZN D 301'  
AD7 Software D 6YH 302 ? 15 'binding site for residue 6YH D 302' 
AD8 Software D EDO 303 ? 6  'binding site for residue EDO D 303' 
AD9 Software D EDO 304 ? 7  'binding site for residue EDO D 304' 
AE1 Software D EDO 305 ? 6  'binding site for residue EDO D 305' 
# 
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  6YH F  .   ? 6YH A 302 . ? 1_555 ? 
5   AC2 13 HIS A  91  ? HIS A 91  . ? 1_555 ? 
6   AC2 13 HIS A  93  ? HIS A 93  . ? 1_555 ? 
7   AC2 13 HIS A  117 ? HIS A 117 . ? 1_555 ? 
8   AC2 13 VAL A  119 ? VAL A 119 . ? 1_555 ? 
9   AC2 13 SER A  133 ? SER A 133 . ? 1_555 ? 
10  AC2 13 LEU A  197 ? LEU A 197 . ? 1_555 ? 
11  AC2 13 THR A  198 ? THR A 198 . ? 1_555 ? 
12  AC2 13 THR A  199 ? THR A 199 . ? 1_555 ? 
13  AC2 13 PRO A  201 ? PRO A 201 . ? 1_555 ? 
14  AC2 13 TRP A  208 ? TRP A 208 . ? 1_555 ? 
15  AC2 13 ZN  E  .   ? ZN  A 301 . ? 1_555 ? 
16  AC2 13 EDO I  .   ? EDO A 305 . ? 1_555 ? 
17  AC2 13 HOH X  .   ? HOH A 440 . ? 1_555 ? 
18  AC3 3  ASP A  156 ? ASP A 156 . ? 1_555 ? 
19  AC3 3  SER A  160 ? SER A 160 . ? 1_555 ? 
20  AC3 3  HOH X  .   ? HOH A 472 . ? 1_555 ? 
21  AC4 5  ASN A  64  ? ASN A 64  . ? 1_555 ? 
22  AC4 5  GLN A  89  ? GLN A 89  . ? 1_555 ? 
23  AC4 5  HIS A  91  ? HIS A 91  . ? 1_555 ? 
24  AC4 5  EDO I  .   ? EDO A 305 . ? 1_555 ? 
25  AC4 5  HOH X  .   ? HOH A 508 . ? 1_555 ? 
26  AC5 4  ASN A  64  ? ASN A 64  . ? 1_555 ? 
27  AC5 4  LYS A  69  ? LYS A 69  . ? 1_555 ? 
28  AC5 4  6YH F  .   ? 6YH A 302 . ? 1_555 ? 
29  AC5 4  EDO H  .   ? EDO A 304 . ? 1_555 ? 
30  AC6 4  HIS B  91  ? HIS B 91  . ? 1_555 ? 
31  AC6 4  HIS B  93  ? HIS B 93  . ? 1_555 ? 
32  AC6 4  HIS B  117 ? HIS B 117 . ? 1_555 ? 
33  AC6 4  6YH K  .   ? 6YH B 302 . ? 1_555 ? 
34  AC7 12 HIS B  91  ? HIS B 91  . ? 1_555 ? 
35  AC7 12 HIS B  93  ? HIS B 93  . ? 1_555 ? 
36  AC7 12 HIS B  117 ? HIS B 117 . ? 1_555 ? 
37  AC7 12 VAL B  119 ? VAL B 119 . ? 1_555 ? 
38  AC7 12 SER B  133 ? SER B 133 . ? 1_555 ? 
39  AC7 12 LEU B  197 ? LEU B 197 . ? 1_555 ? 
40  AC7 12 THR B  198 ? THR B 198 . ? 1_555 ? 
41  AC7 12 THR B  199 ? THR B 199 . ? 1_555 ? 
42  AC7 12 TRP B  208 ? TRP B 208 . ? 1_555 ? 
43  AC7 12 ZN  J  .   ? ZN  B 301 . ? 1_555 ? 
44  AC7 12 EDO N  .   ? EDO B 305 . ? 1_555 ? 
45  AC7 12 HOH Y  .   ? HOH B 614 . ? 1_555 ? 
46  AC8 6  SER B  42  ? SER B 42  . ? 1_555 ? 
47  AC8 6  THR B  44  ? THR B 44  . ? 1_555 ? 
48  AC8 6  LEU B  46  ? LEU B 46  . ? 1_555 ? 
49  AC8 6  GLY B  80  ? GLY B 80  . ? 1_555 ? 
50  AC8 6  TYR B  190 ? TYR B 190 . ? 1_555 ? 
51  AC8 6  ARG B  192 ? ARG B 192 . ? 1_555 ? 
52  AC9 6  ASN B  64  ? ASN B 64  . ? 1_555 ? 
53  AC9 6  GLN B  89  ? GLN B 89  . ? 1_555 ? 
54  AC9 6  HIS B  91  ? HIS B 91  . ? 1_555 ? 
55  AC9 6  EDO N  .   ? EDO B 305 . ? 1_555 ? 
56  AC9 6  HOH Y  .   ? HOH B 452 . ? 1_555 ? 
57  AC9 6  HOH Y  .   ? HOH B 546 . ? 1_555 ? 
58  AD1 4  ASN B  64  ? ASN B 64  . ? 1_555 ? 
59  AD1 4  LYS B  69  ? LYS B 69  . ? 1_555 ? 
60  AD1 4  6YH K  .   ? 6YH B 302 . ? 1_555 ? 
61  AD1 4  EDO M  .   ? EDO B 304 . ? 1_555 ? 
62  AD2 4  HIS C  91  ? HIS C 91  . ? 1_555 ? 
63  AD2 4  HIS C  93  ? HIS C 93  . ? 1_555 ? 
64  AD2 4  HIS C  117 ? HIS C 117 . ? 1_555 ? 
65  AD2 4  6YH P  .   ? 6YH C 302 . ? 1_555 ? 
66  AD3 15 HIS C  91  ? HIS C 91  . ? 1_555 ? 
67  AD3 15 HIS C  93  ? HIS C 93  . ? 1_555 ? 
68  AD3 15 HIS C  117 ? HIS C 117 . ? 1_555 ? 
69  AD3 15 VAL C  119 ? VAL C 119 . ? 1_555 ? 
70  AD3 15 SER C  133 ? SER C 133 . ? 1_555 ? 
71  AD3 15 VAL C  141 ? VAL C 141 . ? 1_555 ? 
72  AD3 15 LEU C  197 ? LEU C 197 . ? 1_555 ? 
73  AD3 15 THR C  198 ? THR C 198 . ? 1_555 ? 
74  AD3 15 THR C  199 ? THR C 199 . ? 1_555 ? 
75  AD3 15 PRO C  201 ? PRO C 201 . ? 1_555 ? 
76  AD3 15 TRP C  208 ? TRP C 208 . ? 1_555 ? 
77  AD3 15 ZN  O  .   ? ZN  C 301 . ? 1_555 ? 
78  AD3 15 EDO Q  .   ? EDO C 303 . ? 1_555 ? 
79  AD3 15 EDO R  .   ? EDO C 304 . ? 1_555 ? 
80  AD3 15 HOH Z  .   ? HOH C 423 . ? 1_555 ? 
81  AD4 6  ASN C  64  ? ASN C 64  . ? 1_555 ? 
82  AD4 6  GLN C  89  ? GLN C 89  . ? 1_555 ? 
83  AD4 6  HIS C  91  ? HIS C 91  . ? 1_555 ? 
84  AD4 6  6YH P  .   ? 6YH C 302 . ? 1_555 ? 
85  AD4 6  EDO R  .   ? EDO C 304 . ? 1_555 ? 
86  AD4 6  HOH Z  .   ? HOH C 507 . ? 1_555 ? 
87  AD5 4  ASN C  64  ? ASN C 64  . ? 1_555 ? 
88  AD5 4  LYS C  69  ? LYS C 69  . ? 1_555 ? 
89  AD5 4  6YH P  .   ? 6YH C 302 . ? 1_555 ? 
90  AD5 4  EDO Q  .   ? EDO C 303 . ? 1_555 ? 
91  AD6 4  HIS D  91  ? HIS D 91  . ? 1_555 ? 
92  AD6 4  HIS D  93  ? HIS D 93  . ? 1_555 ? 
93  AD6 4  HIS D  117 ? HIS D 117 . ? 1_555 ? 
94  AD6 4  6YH T  .   ? 6YH D 302 . ? 1_555 ? 
95  AD7 15 HIS D  91  ? HIS D 91  . ? 1_555 ? 
96  AD7 15 HIS D  93  ? HIS D 93  . ? 1_555 ? 
97  AD7 15 HIS D  117 ? HIS D 117 . ? 1_555 ? 
98  AD7 15 VAL D  119 ? VAL D 119 . ? 1_555 ? 
99  AD7 15 ALA D  129 ? ALA D 129 . ? 1_555 ? 
100 AD7 15 SER D  130 ? SER D 130 . ? 1_555 ? 
101 AD7 15 SER D  133 ? SER D 133 . ? 1_555 ? 
102 AD7 15 LEU D  197 ? LEU D 197 . ? 1_555 ? 
103 AD7 15 THR D  198 ? THR D 198 . ? 1_555 ? 
104 AD7 15 THR D  199 ? THR D 199 . ? 1_555 ? 
105 AD7 15 PRO D  201 ? PRO D 201 . ? 1_555 ? 
106 AD7 15 TRP D  208 ? TRP D 208 . ? 1_555 ? 
107 AD7 15 ZN  S  .   ? ZN  D 301 . ? 1_555 ? 
108 AD7 15 EDO V  .   ? EDO D 304 . ? 1_555 ? 
109 AD7 15 EDO W  .   ? EDO D 305 . ? 1_555 ? 
110 AD8 6  SER D  42  ? SER D 42  . ? 1_555 ? 
111 AD8 6  THR D  44  ? THR D 44  . ? 1_555 ? 
112 AD8 6  LEU D  46  ? LEU D 46  . ? 1_555 ? 
113 AD8 6  GLY D  80  ? GLY D 80  . ? 1_555 ? 
114 AD8 6  TYR D  190 ? TYR D 190 . ? 1_555 ? 
115 AD8 6  ARG D  192 ? ARG D 192 . ? 1_555 ? 
116 AD9 7  ASN D  64  ? ASN D 64  . ? 1_555 ? 
117 AD9 7  GLN D  89  ? GLN D 89  . ? 1_555 ? 
118 AD9 7  HIS D  91  ? HIS D 91  . ? 1_555 ? 
119 AD9 7  6YH T  .   ? 6YH D 302 . ? 1_555 ? 
120 AD9 7  EDO W  .   ? EDO D 305 . ? 1_555 ? 
121 AD9 7  HOH AA .   ? HOH D 496 . ? 1_555 ? 
122 AD9 7  HOH AA .   ? HOH D 541 . ? 1_555 ? 
123 AE1 6  ASN D  64  ? ASN D 64  . ? 1_555 ? 
124 AE1 6  LYS D  69  ? LYS D 69  . ? 1_555 ? 
125 AE1 6  GLN D  89  ? GLN D 89  . ? 1_555 ? 
126 AE1 6  6YH T  .   ? 6YH D 302 . ? 1_555 ? 
127 AE1 6  EDO V  .   ? EDO D 304 . ? 1_555 ? 
128 AE1 6  HOH AA .   ? HOH D 446 . ? 1_555 ? 
# 
_pdbx_entry_details.entry_id                   5LL5 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 O   B HOH 406 ? ? O B HOH 511 ? ? 1.56 
2  1 OG  B SER 42  ? A O B HOH 401 ? ? 1.65 
3  1 OE2 D GLU 147 ? B O D HOH 401 ? ? 1.70 
4  1 OE1 C GLN 58  ? ? O C HOH 401 ? ? 1.77 
5  1 O   D HOH 670 ? ? O D HOH 680 ? ? 1.85 
6  1 O   B HOH 661 ? ? O B HOH 674 ? ? 1.87 
7  1 O   C HOH 645 ? ? O D HOH 667 ? ? 2.07 
8  1 OD2 A ASP 253 ? ? O A HOH 401 ? ? 2.08 
9  1 OE2 B GLU 180 ? B O B HOH 402 ? ? 2.11 
10 1 ND2 B ASN 122 ? ? O B HOH 403 ? ? 2.14 
11 1 OE1 A GLN 79  ? ? O A HOH 402 ? ? 2.16 
12 1 OD2 C ASP 75  ? B O C HOH 402 ? ? 2.17 
13 1 O   C HOH 555 ? ? O D HOH 430 ? ? 2.17 
14 1 O   A SER 74  ? ? O A HOH 403 ? ? 2.18 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    HOH 
_pdbx_validate_symm_contact.auth_seq_id_1     417 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    O 
_pdbx_validate_symm_contact.auth_asym_id_2    B 
_pdbx_validate_symm_contact.auth_comp_id_2    HOH 
_pdbx_validate_symm_contact.auth_seq_id_2     462 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   2_555 
_pdbx_validate_symm_contact.dist              2.13 
# 
loop_
_pdbx_validate_rmsd_bond.id 
_pdbx_validate_rmsd_bond.PDB_model_num 
_pdbx_validate_rmsd_bond.auth_atom_id_1 
_pdbx_validate_rmsd_bond.auth_asym_id_1 
_pdbx_validate_rmsd_bond.auth_comp_id_1 
_pdbx_validate_rmsd_bond.auth_seq_id_1 
_pdbx_validate_rmsd_bond.PDB_ins_code_1 
_pdbx_validate_rmsd_bond.label_alt_id_1 
_pdbx_validate_rmsd_bond.auth_atom_id_2 
_pdbx_validate_rmsd_bond.auth_asym_id_2 
_pdbx_validate_rmsd_bond.auth_comp_id_2 
_pdbx_validate_rmsd_bond.auth_seq_id_2 
_pdbx_validate_rmsd_bond.PDB_ins_code_2 
_pdbx_validate_rmsd_bond.label_alt_id_2 
_pdbx_validate_rmsd_bond.bond_value 
_pdbx_validate_rmsd_bond.bond_target_value 
_pdbx_validate_rmsd_bond.bond_deviation 
_pdbx_validate_rmsd_bond.bond_standard_deviation 
_pdbx_validate_rmsd_bond.linker_flag 
1 1 CG A HIS 33  ? ? CD2 A HIS 33  ? ? 1.419 1.354 0.065 0.009 N 
2 1 CG B HIS 91  ? ? CD2 B HIS 91  ? ? 1.421 1.354 0.067 0.009 N 
3 1 CG B HIS 164 ? ? CD2 B HIS 164 ? ? 1.434 1.354 0.080 0.009 N 
4 1 CG C HIS 93  ? ? CD2 C HIS 93  ? ? 1.427 1.354 0.073 0.009 N 
5 1 CG C HIS 111 ? ? CD2 C HIS 111 ? ? 1.414 1.354 0.060 0.009 N 
6 1 CG D HIS 93  ? ? CD2 D HIS 93  ? ? 1.415 1.354 0.061 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             C 
_pdbx_validate_rmsd_angle.auth_asym_id_1             B 
_pdbx_validate_rmsd_angle.auth_comp_id_1             TYR 
_pdbx_validate_rmsd_angle.auth_seq_id_1              126 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             N 
_pdbx_validate_rmsd_angle.auth_asym_id_2             B 
_pdbx_validate_rmsd_angle.auth_comp_id_2             PRO 
_pdbx_validate_rmsd_angle.auth_seq_id_2              127 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             CA 
_pdbx_validate_rmsd_angle.auth_asym_id_3             B 
_pdbx_validate_rmsd_angle.auth_comp_id_3             PRO 
_pdbx_validate_rmsd_angle.auth_seq_id_3              127 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                132.38 
_pdbx_validate_rmsd_angle.angle_target_value         119.30 
_pdbx_validate_rmsd_angle.angle_deviation            13.08 
_pdbx_validate_rmsd_angle.angle_standard_deviation   1.50 
_pdbx_validate_rmsd_angle.linker_flag                Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ASP A 99  ? ? -152.11 73.56  
2  1 ASN A 245 ? ? -91.07  54.15  
3  1 GLU B 137 ? ? 34.30   44.64  
4  1 CYS B 202 ? ? 72.73   30.37  
5  1 ASN B 245 ? ? -95.29  59.00  
6  1 SER C 54  ? ? -32.63  124.67 
7  1 ASN C 56  ? ? 64.62   -22.04 
8  1 ASN C 245 ? ? -96.16  53.36  
9  1 ASP D 99  ? ? -150.12 83.01  
10 1 ASN D 245 ? ? -94.48  52.40  
# 
_phasing.method   MR 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? C HOH 676 ? 6.08 . 
2 1 O ? D HOH 726 ? 5.88 . 
3 1 O ? D HOH 727 ? 6.16 . 
# 
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 
6YH O12  O  N N 1   
6YH C11  C  N N 2   
6YH C4   C  Y N 3   
6YH C3   C  Y N 4   
6YH C2   C  Y N 5   
6YH C5   C  Y N 6   
6YH C6   C  Y N 7   
6YH C1   C  Y N 8   
6YH S7   S  N N 9   
6YH O9   O  N N 10  
6YH N10  N  N N 11  
6YH O8   O  N N 12  
6YH C13  C  N N 13  
6YH N14  N  Y N 14  
6YH C18  C  Y N 15  
6YH C20  C  Y N 16  
6YH C21  C  Y N 17  
6YH C22  C  Y N 18  
6YH C23  C  Y N 19  
6YH C19  C  Y N 20  
6YH N17  N  Y N 21  
6YH C16  C  Y N 22  
6YH H1   H  N N 23  
6YH H2   H  N N 24  
6YH H3   H  N N 25  
6YH H4   H  N N 26  
6YH H5   H  N N 27  
6YH H6   H  N N 28  
6YH H7   H  N N 29  
6YH H8   H  N N 30  
6YH H9   H  N N 31  
6YH H10  H  N N 32  
6YH H11  H  N N 33  
6YH H12  H  N N 34  
6YH H13  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 
THR N    N  N N 349 
THR CA   C  N S 350 
THR C    C  N N 351 
THR O    O  N N 352 
THR CB   C  N R 353 
THR OG1  O  N N 354 
THR CG2  C  N N 355 
THR OXT  O  N N 356 
THR H    H  N N 357 
THR H2   H  N N 358 
THR HA   H  N N 359 
THR HB   H  N N 360 
THR HG1  H  N N 361 
THR HG21 H  N N 362 
THR HG22 H  N N 363 
THR HG23 H  N N 364 
THR HXT  H  N N 365 
TRP N    N  N N 366 
TRP CA   C  N S 367 
TRP C    C  N N 368 
TRP O    O  N N 369 
TRP CB   C  N N 370 
TRP CG   C  Y N 371 
TRP CD1  C  Y N 372 
TRP CD2  C  Y N 373 
TRP NE1  N  Y N 374 
TRP CE2  C  Y N 375 
TRP CE3  C  Y N 376 
TRP CZ2  C  Y N 377 
TRP CZ3  C  Y N 378 
TRP CH2  C  Y N 379 
TRP OXT  O  N N 380 
TRP H    H  N N 381 
TRP H2   H  N N 382 
TRP HA   H  N N 383 
TRP HB2  H  N N 384 
TRP HB3  H  N N 385 
TRP HD1  H  N N 386 
TRP HE1  H  N N 387 
TRP HE3  H  N N 388 
TRP HZ2  H  N N 389 
TRP HZ3  H  N N 390 
TRP HH2  H  N N 391 
TRP HXT  H  N N 392 
TYR N    N  N N 393 
TYR CA   C  N S 394 
TYR C    C  N N 395 
TYR O    O  N N 396 
TYR CB   C  N N 397 
TYR CG   C  Y N 398 
TYR CD1  C  Y N 399 
TYR CD2  C  Y N 400 
TYR CE1  C  Y N 401 
TYR CE2  C  Y N 402 
TYR CZ   C  Y N 403 
TYR OH   O  N N 404 
TYR OXT  O  N N 405 
TYR H    H  N N 406 
TYR H2   H  N N 407 
TYR HA   H  N N 408 
TYR HB2  H  N N 409 
TYR HB3  H  N N 410 
TYR HD1  H  N N 411 
TYR HD2  H  N N 412 
TYR HE1  H  N N 413 
TYR HE2  H  N N 414 
TYR HH   H  N N 415 
TYR HXT  H  N N 416 
VAL N    N  N N 417 
VAL CA   C  N S 418 
VAL C    C  N N 419 
VAL O    O  N N 420 
VAL CB   C  N N 421 
VAL CG1  C  N N 422 
VAL CG2  C  N N 423 
VAL OXT  O  N N 424 
VAL H    H  N N 425 
VAL H2   H  N N 426 
VAL HA   H  N N 427 
VAL HB   H  N N 428 
VAL HG11 H  N N 429 
VAL HG12 H  N N 430 
VAL HG13 H  N N 431 
VAL HG21 H  N N 432 
VAL HG22 H  N N 433 
VAL HG23 H  N N 434 
VAL HXT  H  N N 435 
ZN  ZN   ZN N N 436 
# 
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 
6YH N17 C16  doub Y N 1   
6YH N17 C19  sing Y N 2   
6YH C16 N14  sing Y N 3   
6YH C19 C23  doub Y N 4   
6YH C19 C18  sing Y N 5   
6YH N14 C18  sing Y N 6   
6YH N14 C13  sing N N 7   
6YH C23 C22  sing Y N 8   
6YH O12 C11  doub N N 9   
6YH C18 C20  doub Y N 10  
6YH C13 C11  sing N N 11  
6YH C11 C4   sing N N 12  
6YH C22 C21  doub Y N 13  
6YH C4  C3   doub Y N 14  
6YH C4  C5   sing Y N 15  
6YH C20 C21  sing Y N 16  
6YH C3  C2   sing Y N 17  
6YH C5  C6   doub Y N 18  
6YH C2  C1   doub Y N 19  
6YH C6  C1   sing Y N 20  
6YH C1  S7   sing N N 21  
6YH N10 S7   sing N N 22  
6YH O8  S7   doub N N 23  
6YH S7  O9   doub N N 24  
6YH C3  H1   sing N N 25  
6YH C2  H2   sing N N 26  
6YH C5  H3   sing N N 27  
6YH C6  H4   sing N N 28  
6YH N10 H5   sing N N 29  
6YH N10 H6   sing N N 30  
6YH C13 H7   sing N N 31  
6YH C13 H8   sing N N 32  
6YH C20 H9   sing N N 33  
6YH C21 H10  sing N N 34  
6YH C22 H11  sing N N 35  
6YH C23 H12  sing N N 36  
6YH C16 H13  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 
THR N   CA   sing N N 336 
THR N   H    sing N N 337 
THR N   H2   sing N N 338 
THR CA  C    sing N N 339 
THR CA  CB   sing N N 340 
THR CA  HA   sing N N 341 
THR C   O    doub N N 342 
THR C   OXT  sing N N 343 
THR CB  OG1  sing N N 344 
THR CB  CG2  sing N N 345 
THR CB  HB   sing N N 346 
THR OG1 HG1  sing N N 347 
THR CG2 HG21 sing N N 348 
THR CG2 HG22 sing N N 349 
THR CG2 HG23 sing N N 350 
THR OXT HXT  sing N N 351 
TRP N   CA   sing N N 352 
TRP N   H    sing N N 353 
TRP N   H2   sing N N 354 
TRP CA  C    sing N N 355 
TRP CA  CB   sing N N 356 
TRP CA  HA   sing N N 357 
TRP C   O    doub N N 358 
TRP C   OXT  sing N N 359 
TRP CB  CG   sing N N 360 
TRP CB  HB2  sing N N 361 
TRP CB  HB3  sing N N 362 
TRP CG  CD1  doub Y N 363 
TRP CG  CD2  sing Y N 364 
TRP CD1 NE1  sing Y N 365 
TRP CD1 HD1  sing N N 366 
TRP CD2 CE2  doub Y N 367 
TRP CD2 CE3  sing Y N 368 
TRP NE1 CE2  sing Y N 369 
TRP NE1 HE1  sing N N 370 
TRP CE2 CZ2  sing Y N 371 
TRP CE3 CZ3  doub Y N 372 
TRP CE3 HE3  sing N N 373 
TRP CZ2 CH2  doub Y N 374 
TRP CZ2 HZ2  sing N N 375 
TRP CZ3 CH2  sing Y N 376 
TRP CZ3 HZ3  sing N N 377 
TRP CH2 HH2  sing N N 378 
TRP OXT HXT  sing N N 379 
TYR N   CA   sing N N 380 
TYR N   H    sing N N 381 
TYR N   H2   sing N N 382 
TYR CA  C    sing N N 383 
TYR CA  CB   sing N N 384 
TYR CA  HA   sing N N 385 
TYR C   O    doub N N 386 
TYR C   OXT  sing N N 387 
TYR CB  CG   sing N N 388 
TYR CB  HB2  sing N N 389 
TYR CB  HB3  sing N N 390 
TYR CG  CD1  doub Y N 391 
TYR CG  CD2  sing Y N 392 
TYR CD1 CE1  sing Y N 393 
TYR CD1 HD1  sing N N 394 
TYR CD2 CE2  doub Y N 395 
TYR CD2 HD2  sing N N 396 
TYR CE1 CZ   doub Y N 397 
TYR CE1 HE1  sing N N 398 
TYR CE2 CZ   sing Y N 399 
TYR CE2 HE2  sing N N 400 
TYR CZ  OH   sing N N 401 
TYR OH  HH   sing N N 402 
TYR OXT HXT  sing N N 403 
VAL N   CA   sing N N 404 
VAL N   H    sing N N 405 
VAL N   H2   sing N N 406 
VAL CA  C    sing N N 407 
VAL CA  CB   sing N N 408 
VAL CA  HA   sing N N 409 
VAL C   O    doub N N 410 
VAL C   OXT  sing N N 411 
VAL CB  CG1  sing N N 412 
VAL CB  CG2  sing N N 413 
VAL CB  HB   sing N N 414 
VAL CG1 HG11 sing N N 415 
VAL CG1 HG12 sing N N 416 
VAL CG1 HG13 sing N N 417 
VAL CG2 HG21 sing N N 418 
VAL CG2 HG22 sing N N 419 
VAL CG2 HG23 sing N N 420 
VAL OXT HXT  sing N N 421 
# 
_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                    5LL5 
_atom_sites.fract_transf_matrix[1][1]   0.012917 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.004438 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.013520 
_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]   0.011578 
_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  
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   ? 16.758  17.307  18.775  1.00 42.18 ? 3   LYS A N   1 
ATOM   2    C  CA  . LYS A  1 3   ? 17.548  16.216  18.152  1.00 40.94 ? 3   LYS A CA  1 
ATOM   3    C  C   . LYS A  1 3   ? 16.658  14.975  17.892  1.00 36.15 ? 3   LYS A C   1 
ATOM   4    O  O   . LYS A  1 3   ? 15.564  14.821  18.470  1.00 37.86 ? 3   LYS A O   1 
ATOM   5    C  CB  . LYS A  1 3   ? 18.713  15.836  19.056  1.00 46.63 ? 3   LYS A CB  1 
ATOM   6    C  CG  . LYS A  1 3   ? 19.927  15.439  18.258  1.00 51.65 ? 3   LYS A CG  1 
ATOM   7    C  CD  . LYS A  1 3   ? 20.457  14.069  18.646  1.00 48.40 ? 3   LYS A CD  1 
ATOM   8    C  CE  . LYS A  1 3   ? 21.793  13.848  17.942  1.00 46.10 ? 3   LYS A CE  1 
ATOM   9    N  NZ  . LYS A  1 3   ? 22.746  14.777  18.599  1.00 54.17 ? 3   LYS A NZ  1 
ATOM   10   N  N   . TRP A  1 4   ? 17.138  14.070  17.058  1.00 21.83 ? 4   TRP A N   1 
ATOM   11   C  CA  . TRP A  1 4   ? 16.252  13.013  16.558  1.00 17.67 ? 4   TRP A CA  1 
ATOM   12   C  C   . TRP A  1 4   ? 16.228  11.883  17.529  1.00 17.09 ? 4   TRP A C   1 
ATOM   13   O  O   . TRP A  1 4   ? 17.237  11.633  18.287  1.00 17.65 ? 4   TRP A O   1 
ATOM   14   C  CB  . TRP A  1 4   ? 16.766  12.566  15.194  1.00 16.11 ? 4   TRP A CB  1 
ATOM   15   C  CG  . TRP A  1 4   ? 18.161  11.914  15.179  1.00 14.44 ? 4   TRP A CG  1 
ATOM   16   C  CD1 . TRP A  1 4   ? 19.367  12.506  14.967  1.00 15.61 ? 4   TRP A CD1 1 
ATOM   17   C  CD2 . TRP A  1 4   ? 18.449  10.494  15.295  1.00 12.61 ? 4   TRP A CD2 1 
ATOM   18   N  NE1 . TRP A  1 4   ? 20.352  11.603  14.928  1.00 15.35 ? 4   TRP A NE1 1 
ATOM   19   C  CE2 . TRP A  1 4   ? 19.870  10.335  15.133  1.00 13.01 ? 4   TRP A CE2 1 
ATOM   20   C  CE3 . TRP A  1 4   ? 17.656  9.351   15.497  1.00 12.00 ? 4   TRP A CE3 1 
ATOM   21   C  CZ2 . TRP A  1 4   ? 20.487  9.079   15.169  1.00 13.63 ? 4   TRP A CZ2 1 
ATOM   22   C  CZ3 . TRP A  1 4   ? 18.266  8.100   15.497  1.00 12.58 ? 4   TRP A CZ3 1 
ATOM   23   C  CH2 . TRP A  1 4   ? 19.670  7.983   15.397  1.00 12.43 ? 4   TRP A CH2 1 
ATOM   24   N  N   . THR A  1 5   ? 15.127  11.177  17.557  1.00 15.95 ? 5   THR A N   1 
ATOM   25   C  CA  . THR A  1 5   ? 14.914  9.990   18.399  1.00 15.28 ? 5   THR A CA  1 
ATOM   26   C  C   . THR A  1 5   ? 14.120  8.876   17.705  1.00 14.61 ? 5   THR A C   1 
ATOM   27   O  O   . THR A  1 5   ? 13.829  9.041   16.519  1.00 14.36 ? 5   THR A O   1 
ATOM   28   C  CB  . THR A  1 5   ? 13.996  10.325  19.628  1.00 16.14 ? 5   THR A CB  1 
ATOM   29   O  OG1 . THR A  1 5   ? 12.676  10.680  19.100  1.00 19.67 ? 5   THR A OG1 1 
ATOM   30   C  CG2 . THR A  1 5   ? 14.473  11.556  20.368  1.00 20.76 ? 5   THR A CG2 1 
ATOM   31   N  N   . TYR A  1 6   ? 13.718  7.782   18.376  1.00 15.22 ? 6   TYR A N   1 
ATOM   32   C  CA  . TYR A  1 6   ? 12.895  6.747   17.793  1.00 15.31 ? 6   TYR A CA  1 
ATOM   33   C  C   . TYR A  1 6   ? 11.449  6.756   18.339  1.00 17.02 ? 6   TYR A C   1 
ATOM   34   O  O   . TYR A  1 6   ? 10.644  5.875   18.150  1.00 16.94 ? 6   TYR A O   1 
ATOM   35   C  CB  . TYR A  1 6   ? 13.488  5.350   18.019  1.00 14.87 ? 6   TYR A CB  1 
ATOM   36   C  CG  . TYR A  1 6   ? 14.760  5.068   17.246  1.00 13.66 ? 6   TYR A CG  1 
ATOM   37   C  CD1 . TYR A  1 6   ? 16.008  5.367   17.783  1.00 12.63 ? 6   TYR A CD1 1 
ATOM   38   C  CD2 . TYR A  1 6   ? 14.712  4.497   15.984  1.00 13.41 ? 6   TYR A CD2 1 
ATOM   39   C  CE1 . TYR A  1 6   ? 17.170  5.111   17.076  1.00 12.21 ? 6   TYR A CE1 1 
ATOM   40   C  CE2 . TYR A  1 6   ? 15.867  4.238   15.271  1.00 11.87 ? 6   TYR A CE2 1 
ATOM   41   C  CZ  . TYR A  1 6   ? 17.091  4.547   15.821  1.00 12.55 ? 6   TYR A CZ  1 
ATOM   42   O  OH  . TYR A  1 6   ? 18.239  4.284   15.106  1.00 14.05 ? 6   TYR A OH  1 
ATOM   43   N  N   A PHE A  1 7   ? 11.138  7.777   19.173  0.50 22.88 ? 7   PHE A N   1 
ATOM   44   N  N   B PHE A  1 7   ? 11.014  7.956   18.744  0.50 22.51 ? 7   PHE A N   1 
ATOM   45   C  CA  A PHE A  1 7   ? 9.817   7.854   19.880  0.50 25.23 ? 7   PHE A CA  1 
ATOM   46   C  CA  B PHE A  1 7   ? 9.717   8.064   19.340  0.50 26.24 ? 7   PHE A CA  1 
ATOM   47   C  C   A PHE A  1 7   ? 9.418   9.290   20.261  0.50 26.04 ? 7   PHE A C   1 
ATOM   48   C  C   B PHE A  1 7   ? 9.250   9.495   19.374  0.50 29.20 ? 7   PHE A C   1 
ATOM   49   O  O   A PHE A  1 7   ? 10.285  10.041  20.704  0.50 20.91 ? 7   PHE A O   1 
ATOM   50   O  O   B PHE A  1 7   ? 9.881   10.413  18.844  0.50 24.82 ? 7   PHE A O   1 
ATOM   51   C  CB  A PHE A  1 7   ? 9.825   6.923   21.115  0.50 29.29 ? 7   PHE A CB  1 
ATOM   52   C  CB  B PHE A  1 7   ? 9.757   7.515   20.778  0.50 29.00 ? 7   PHE A CB  1 
ATOM   53   C  CG  A PHE A  1 7   ? 8.599   7.036   22.015  0.50 31.73 ? 7   PHE A CG  1 
ATOM   54   C  CG  B PHE A  1 7   ? 10.625  8.328   21.704  0.50 29.61 ? 7   PHE A CG  1 
ATOM   55   C  CD1 A PHE A  1 7   ? 7.503   6.221   21.818  0.50 33.05 ? 7   PHE A CD1 1 
ATOM   56   C  CD1 B PHE A  1 7   ? 10.238  9.604   22.080  0.50 33.87 ? 7   PHE A CD1 1 
ATOM   57   C  CD2 A PHE A  1 7   ? 8.574   7.928   23.086  0.50 34.96 ? 7   PHE A CD2 1 
ATOM   58   C  CD2 B PHE A  1 7   ? 11.828  7.828   22.197  0.50 32.00 ? 7   PHE A CD2 1 
ATOM   59   C  CE1 A PHE A  1 7   ? 6.403   6.299   22.646  0.50 32.97 ? 7   PHE A CE1 1 
ATOM   60   C  CE1 B PHE A  1 7   ? 11.026  10.373  22.917  0.50 30.78 ? 7   PHE A CE1 1 
ATOM   61   C  CE2 A PHE A  1 7   ? 7.466   8.014   23.917  0.50 34.30 ? 7   PHE A CE2 1 
ATOM   62   C  CE2 B PHE A  1 7   ? 12.615  8.602   23.033  0.50 34.92 ? 7   PHE A CE2 1 
ATOM   63   C  CZ  A PHE A  1 7   ? 6.385   7.201   23.689  0.50 37.30 ? 7   PHE A CZ  1 
ATOM   64   C  CZ  B PHE A  1 7   ? 12.204  9.881   23.375  0.50 34.27 ? 7   PHE A CZ  1 
ATOM   65   N  N   . GLY A  1 8   ? 8.130   9.656   20.050  1.00 28.61 ? 8   GLY A N   1 
ATOM   66   C  CA  . GLY A  1 8   ? 7.562   11.025  20.380  1.00 26.80 ? 8   GLY A CA  1 
ATOM   67   C  C   . GLY A  1 8   ? 7.718   11.848  19.105  1.00 29.08 ? 8   GLY A C   1 
ATOM   68   O  O   . GLY A  1 8   ? 7.834   11.303  17.970  1.00 32.59 ? 8   GLY A O   1 
ATOM   69   N  N   . PRO A  1 9   ? 7.747   13.141  19.248  1.00 24.03 ? 9   PRO A N   1 
ATOM   70   C  CA  . PRO A  1 9   ? 7.609   13.992  18.078  1.00 24.23 ? 9   PRO A CA  1 
ATOM   71   C  C   . PRO A  1 9   ? 8.839   14.142  17.272  1.00 22.88 ? 9   PRO A C   1 
ATOM   72   O  O   . PRO A  1 9   ? 8.749   14.672  16.168  1.00 20.23 ? 9   PRO A O   1 
ATOM   73   C  CB  . PRO A  1 9   ? 7.167   15.357  18.658  1.00 31.08 ? 9   PRO A CB  1 
ATOM   74   C  CG  . PRO A  1 9   ? 7.573   15.329  20.062  1.00 29.74 ? 9   PRO A CG  1 
ATOM   75   C  CD  . PRO A  1 9   ? 7.446   13.891  20.491  1.00 26.92 ? 9   PRO A CD  1 
ATOM   76   N  N   . ASP A  1 10  ? 9.978   13.641  17.772  1.00 21.54 ? 10  ASP A N   1 
ATOM   77   C  CA  . ASP A  1 10  ? 11.178  13.756  17.016  1.00 21.38 ? 10  ASP A CA  1 
ATOM   78   C  C   . ASP A  1 10  ? 11.652  12.400  16.408  1.00 19.10 ? 10  ASP A C   1 
ATOM   79   O  O   . ASP A  1 10  ? 12.858  12.229  15.972  1.00 17.44 ? 10  ASP A O   1 
ATOM   80   C  CB  . ASP A  1 10  ? 12.300  14.294  17.937  1.00 22.49 ? 10  ASP A CB  1 
ATOM   81   C  CG  . ASP A  1 10  ? 12.078  15.753  18.316  1.00 28.80 ? 10  ASP A CG  1 
ATOM   82   O  OD1 . ASP A  1 10  ? 11.633  16.546  17.423  1.00 30.93 ? 10  ASP A OD1 1 
ATOM   83   O  OD2 . ASP A  1 10  ? 12.306  16.046  19.528  1.00 35.91 ? 10  ASP A OD2 1 
ATOM   84   N  N   . GLY A  1 11  ? 10.652  11.509  16.332  1.00 17.61 ? 11  GLY A N   1 
ATOM   85   C  CA  . GLY A  1 11  ? 10.758  10.068  15.888  1.00 14.73 ? 11  GLY A CA  1 
ATOM   86   C  C   . GLY A  1 11  ? 10.878  10.017  14.392  1.00 12.41 ? 11  GLY A C   1 
ATOM   87   O  O   . GLY A  1 11  ? 10.957  11.008  13.632  1.00 12.42 ? 11  GLY A O   1 
ATOM   88   N  N   . GLU A  1 12  ? 10.954  8.782   13.921  1.00 10.92 ? 12  GLU A N   1 
ATOM   89   C  CA  . GLU A  1 12  ? 11.332  8.531   12.544  1.00 10.03 ? 12  GLU A CA  1 
ATOM   90   C  C   . GLU A  1 12  ? 10.469  9.221   11.418  1.00 9.54  ? 12  GLU A C   1 
ATOM   91   O  O   . GLU A  1 12  ? 11.021  9.570   10.376  1.00 8.74  ? 12  GLU A O   1 
ATOM   92   C  CB  . GLU A  1 12  ? 11.556  7.030   12.278  1.00 10.01 ? 12  GLU A CB  1 
ATOM   93   C  CG  . GLU A  1 12  ? 10.216  6.283   12.208  1.00 9.81  ? 12  GLU A CG  1 
ATOM   94   C  CD  . GLU A  1 12  ? 10.537  4.787   12.329  1.00 8.83  ? 12  GLU A CD  1 
ATOM   95   O  OE1 . GLU A  1 12  ? 10.787  4.129   11.345  1.00 9.62  ? 12  GLU A OE1 1 
ATOM   96   O  OE2 . GLU A  1 12  ? 10.454  4.343   13.504  1.00 10.92 ? 12  GLU A OE2 1 
ATOM   97   N  N   . ASN A  1 13  ? 9.179   9.397   11.675  1.00 10.48 ? 13  ASN A N   1 
ATOM   98   C  CA  . ASN A  1 13  ? 8.367   10.060  10.649  1.00 9.27  ? 13  ASN A CA  1 
ATOM   99   C  C   . ASN A  1 13  ? 8.690   11.521  10.504  1.00 10.40 ? 13  ASN A C   1 
ATOM   100  O  O   . ASN A  1 13  ? 8.273   12.099  9.512   1.00 10.89 ? 13  ASN A O   1 
ATOM   101  C  CB  . ASN A  1 13  ? 6.871   9.955   10.914  1.00 9.15  ? 13  ASN A CB  1 
ATOM   102  C  CG  . ASN A  1 13  ? 6.409   8.510   10.842  1.00 9.52  ? 13  ASN A CG  1 
ATOM   103  O  OD1 . ASN A  1 13  ? 7.088   7.639   10.295  1.00 11.26 ? 13  ASN A OD1 1 
ATOM   104  N  ND2 . ASN A  1 13  ? 5.214   8.285   11.334  1.00 10.22 ? 13  ASN A ND2 1 
ATOM   105  N  N   A SER A  1 14  ? 9.336   12.078  11.555  0.50 9.63  ? 14  SER A N   1 
ATOM   106  N  N   B SER A  1 14  ? 9.502   12.092  11.369  0.50 11.13 ? 14  SER A N   1 
ATOM   107  C  CA  A SER A  1 14  ? 9.793   13.505  11.610  0.50 8.62  ? 14  SER A CA  1 
ATOM   108  C  CA  B SER A  1 14  ? 9.779   13.527  11.232  0.50 10.95 ? 14  SER A CA  1 
ATOM   109  C  C   A SER A  1 14  ? 11.264  13.719  11.212  0.50 9.29  ? 14  SER A C   1 
ATOM   110  C  C   B SER A  1 14  ? 11.271  13.736  10.965  0.50 11.37 ? 14  SER A C   1 
ATOM   111  O  O   A SER A  1 14  ? 11.622  14.880  11.044  0.50 9.30  ? 14  SER A O   1 
ATOM   112  O  O   B SER A  1 14  ? 11.718  14.859  10.780  0.50 11.39 ? 14  SER A O   1 
ATOM   113  C  CB  A SER A  1 14  ? 9.540   14.148  12.975  0.50 9.16  ? 14  SER A CB  1 
ATOM   114  C  CB  B SER A  1 14  ? 9.427   14.250  12.504  0.50 13.33 ? 14  SER A CB  1 
ATOM   115  O  OG  A SER A  1 14  ? 8.124   14.232  13.042  0.50 9.51  ? 14  SER A OG  1 
ATOM   116  O  OG  B SER A  1 14  ? 10.288  13.835  13.516  0.50 18.12 ? 14  SER A OG  1 
ATOM   117  N  N   . TRP A  1 15  ? 12.038  12.663  10.905  1.00 9.87  ? 15  TRP A N   1 
ATOM   118  C  CA  . TRP A  1 15  ? 13.453  12.858  10.549  1.00 9.69  ? 15  TRP A CA  1 
ATOM   119  C  C   . TRP A  1 15  ? 13.634  13.651  9.269   1.00 11.16 ? 15  TRP A C   1 
ATOM   120  O  O   . TRP A  1 15  ? 14.581  14.475  9.187   1.00 10.28 ? 15  TRP A O   1 
ATOM   121  C  CB  . TRP A  1 15  ? 14.157  11.515  10.327  1.00 9.74  ? 15  TRP A CB  1 
ATOM   122  C  CG  . TRP A  1 15  ? 14.305  10.688  11.579  1.00 10.07 ? 15  TRP A CG  1 
ATOM   123  C  CD1 . TRP A  1 15  ? 14.066  10.983  12.879  1.00 10.17 ? 15  TRP A CD1 1 
ATOM   124  C  CD2 . TRP A  1 15  ? 14.727  9.288   11.558  1.00 8.27  ? 15  TRP A CD2 1 
ATOM   125  N  NE1 . TRP A  1 15  ? 14.384  9.917   13.701  1.00 9.49  ? 15  TRP A NE1 1 
ATOM   126  C  CE2 . TRP A  1 15  ? 14.813  8.862   12.948  1.00 8.38  ? 15  TRP A CE2 1 
ATOM   127  C  CE3 . TRP A  1 15  ? 15.162  8.424   10.549  1.00 8.57  ? 15  TRP A CE3 1 
ATOM   128  C  CZ2 . TRP A  1 15  ? 15.217  7.552   13.284  1.00 8.39  ? 15  TRP A CZ2 1 
ATOM   129  C  CZ3 . TRP A  1 15  ? 15.577  7.131   10.901  1.00 8.65  ? 15  TRP A CZ3 1 
ATOM   130  C  CH2 . TRP A  1 15  ? 15.601  6.736   12.253  1.00 8.61  ? 15  TRP A CH2 1 
ATOM   131  N  N   . SER A  1 16  ? 12.750  13.557  8.309   1.00 10.59 ? 16  SER A N   1 
ATOM   132  C  CA  . SER A  1 16  ? 12.914  14.225  7.030   1.00 10.10 ? 16  SER A CA  1 
ATOM   133  C  C   . SER A  1 16  ? 12.774  15.760  7.160   1.00 9.90  ? 16  SER A C   1 
ATOM   134  O  O   . SER A  1 16  ? 13.238  16.405  6.162   1.00 10.75 ? 16  SER A O   1 
ATOM   135  C  CB  . SER A  1 16  ? 11.849  13.734  6.066   1.00 9.96  ? 16  SER A CB  1 
ATOM   136  O  OG  . SER A  1 16  ? 10.581  14.120  6.557   1.00 12.00 ? 16  SER A OG  1 
ATOM   137  N  N   . LYS A  1 17  ? 12.237  16.249  8.260   1.00 9.82  ? 17  LYS A N   1 
ATOM   138  C  CA  . LYS A  1 17  ? 12.210  17.772  8.400   1.00 10.86 ? 17  LYS A CA  1 
ATOM   139  C  C   . LYS A  1 17  ? 13.641  18.322  8.446   1.00 11.59 ? 17  LYS A C   1 
ATOM   140  O  O   . LYS A  1 17  ? 14.028  19.225  7.605   1.00 13.79 ? 17  LYS A O   1 
ATOM   141  C  CB  . LYS A  1 17  ? 11.501  18.124  9.644   1.00 11.74 ? 17  LYS A CB  1 
ATOM   142  C  CG  . LYS A  1 17  ? 9.986   17.888  9.693   1.00 17.76 ? 17  LYS A CG  1 
ATOM   143  C  CD  . LYS A  1 17  ? 9.368   18.038  11.106  1.00 18.68 ? 17  LYS A CD  1 
ATOM   144  C  CE  . LYS A  1 17  ? 8.012   17.231  11.204  1.00 21.11 ? 17  LYS A CE  1 
ATOM   145  N  NZ  . LYS A  1 17  ? 7.472   17.489  12.597  1.00 25.00 ? 17  LYS A NZ  1 
ATOM   146  N  N   A LYS A  1 18  ? 14.523  17.765  9.278   0.50 10.71 ? 18  LYS A N   1 
ATOM   147  N  N   B LYS A  1 18  ? 14.482  17.766  9.345   0.50 10.88 ? 18  LYS A N   1 
ATOM   148  C  CA  A LYS A  1 18  ? 15.869  18.329  9.322   0.50 11.91 ? 18  LYS A CA  1 
ATOM   149  C  CA  B LYS A  1 18  ? 15.862  18.252  9.475   0.50 12.35 ? 18  LYS A CA  1 
ATOM   150  C  C   A LYS A  1 18  ? 16.840  17.597  8.353   0.50 11.30 ? 18  LYS A C   1 
ATOM   151  C  C   B LYS A  1 18  ? 16.889  17.499  8.625   0.50 11.55 ? 18  LYS A C   1 
ATOM   152  O  O   A LYS A  1 18  ? 17.858  18.152  7.836   0.50 12.11 ? 18  LYS A O   1 
ATOM   153  O  O   B LYS A  1 18  ? 18.037  17.942  8.522   0.50 12.55 ? 18  LYS A O   1 
ATOM   154  C  CB  A LYS A  1 18  ? 16.350  18.319  10.765  0.50 14.03 ? 18  LYS A CB  1 
ATOM   155  C  CB  B LYS A  1 18  ? 16.309  18.206  10.930  0.50 15.01 ? 18  LYS A CB  1 
ATOM   156  C  CG  A LYS A  1 18  ? 15.644  19.340  11.680  0.50 15.43 ? 18  LYS A CG  1 
ATOM   157  C  CG  B LYS A  1 18  ? 17.787  18.527  11.095  0.50 16.01 ? 18  LYS A CG  1 
ATOM   158  C  CD  A LYS A  1 18  ? 16.155  20.766  11.396  0.50 16.66 ? 18  LYS A CD  1 
ATOM   159  C  CD  B LYS A  1 18  ? 18.272  18.548  12.547  0.50 19.27 ? 18  LYS A CD  1 
ATOM   160  C  CE  A LYS A  1 18  ? 15.574  21.839  12.339  0.50 19.08 ? 18  LYS A CE  1 
ATOM   161  C  CE  B LYS A  1 18  ? 19.761  18.951  12.642  0.50 21.73 ? 18  LYS A CE  1 
ATOM   162  N  NZ  A LYS A  1 18  ? 16.382  23.084  12.240  0.50 19.92 ? 18  LYS A NZ  1 
ATOM   163  N  NZ  B LYS A  1 18  ? 20.294  18.737  14.022  0.50 28.25 ? 18  LYS A NZ  1 
ATOM   164  N  N   . TYR A  1 19  ? 16.531  16.321  8.088   1.00 11.10 ? 19  TYR A N   1 
ATOM   165  C  CA  . TYR A  1 19  ? 17.412  15.457  7.314   1.00 10.57 ? 19  TYR A CA  1 
ATOM   166  C  C   . TYR A  1 19  ? 16.710  15.008  6.037   1.00 12.35 ? 19  TYR A C   1 
ATOM   167  O  O   . TYR A  1 19  ? 16.036  13.951  5.975   1.00 10.79 ? 19  TYR A O   1 
ATOM   168  C  CB  . TYR A  1 19  ? 17.796  14.253  8.204   1.00 11.59 ? 19  TYR A CB  1 
ATOM   169  C  CG  . TYR A  1 19  ? 18.449  14.617  9.485   1.00 11.16 ? 19  TYR A CG  1 
ATOM   170  C  CD1 . TYR A  1 19  ? 19.842  14.908  9.491   1.00 12.51 ? 19  TYR A CD1 1 
ATOM   171  C  CD2 . TYR A  1 19  ? 17.747  14.657  10.658  1.00 10.78 ? 19  TYR A CD2 1 
ATOM   172  C  CE1 . TYR A  1 19  ? 20.490  15.242  10.701  1.00 13.63 ? 19  TYR A CE1 1 
ATOM   173  C  CE2 . TYR A  1 19  ? 18.358  14.996  11.877  1.00 12.78 ? 19  TYR A CE2 1 
ATOM   174  C  CZ  . TYR A  1 19  ? 19.730  15.292  11.876  1.00 15.65 ? 19  TYR A CZ  1 
ATOM   175  O  OH  . TYR A  1 19  ? 20.374  15.613  13.122  1.00 18.64 ? 19  TYR A OH  1 
ATOM   176  N  N   . PRO A  1 20  ? 16.752  15.782  4.987   1.00 10.34 ? 20  PRO A N   1 
ATOM   177  C  CA  . PRO A  1 20  ? 15.836  15.598  3.888   1.00 10.27 ? 20  PRO A CA  1 
ATOM   178  C  C   . PRO A  1 20  ? 16.092  14.271  3.221   1.00 11.03 ? 20  PRO A C   1 
ATOM   179  O  O   . PRO A  1 20  ? 15.127  13.705  2.583   1.00 11.04 ? 20  PRO A O   1 
ATOM   180  C  CB  . PRO A  1 20  ? 16.170  16.749  2.906   1.00 12.20 ? 20  PRO A CB  1 
ATOM   181  C  CG  . PRO A  1 20  ? 16.856  17.755  3.722   1.00 13.85 ? 20  PRO A CG  1 
ATOM   182  C  CD  . PRO A  1 20  ? 17.472  17.112  4.922   1.00 11.62 ? 20  PRO A CD  1 
ATOM   183  N  N   . SER A  1 21  ? 17.297  13.671  3.224   1.00 10.17 ? 21  SER A N   1 
ATOM   184  C  CA  . SER A  1 21  ? 17.478  12.375  2.602   1.00 10.55 ? 21  SER A CA  1 
ATOM   185  C  C   . SER A  1 21  ? 16.630  11.281  3.298   1.00 8.91  ? 21  SER A C   1 
ATOM   186  O  O   . SER A  1 21  ? 16.367  10.270  2.625   1.00 8.40  ? 21  SER A O   1 
ATOM   187  C  CB  . SER A  1 21  ? 18.999  12.007  2.700   1.00 11.26 ? 21  SER A CB  1 
ATOM   188  O  OG  . SER A  1 21  ? 19.688  12.771  1.692   1.00 13.85 ? 21  SER A OG  1 
ATOM   189  N  N   . CYS A  1 22  ? 16.167  11.511  4.548   1.00 9.22  ? 22  CYS A N   1 
ATOM   190  C  CA  . CYS A  1 22  ? 15.298  10.510  5.162   1.00 9.35  ? 22  CYS A CA  1 
ATOM   191  C  C   . CYS A  1 22  ? 13.978  10.358  4.483   1.00 10.49 ? 22  CYS A C   1 
ATOM   192  O  O   . CYS A  1 22  ? 13.299  9.321   4.684   1.00 10.45 ? 22  CYS A O   1 
ATOM   193  C  CB  . CYS A  1 22  ? 15.092  10.853  6.615   1.00 9.89  ? 22  CYS A CB  1 
ATOM   194  S  SG  . CYS A  1 22  ? 16.694  10.806  7.566   1.00 10.74 ? 22  CYS A SG  1 
ATOM   195  N  N   . GLY A  1 23  ? 13.635  11.310  3.618   1.00 10.42 ? 23  GLY A N   1 
ATOM   196  C  CA  . GLY A  1 23  ? 12.395  11.164  2.781   1.00 10.78 ? 23  GLY A CA  1 
ATOM   197  C  C   . GLY A  1 23  ? 12.696  11.013  1.367   1.00 10.48 ? 23  GLY A C   1 
ATOM   198  O  O   . GLY A  1 23  ? 11.794  11.097  0.508   1.00 11.42 ? 23  GLY A O   1 
ATOM   199  N  N   . GLY A  1 24  ? 13.936  10.753  0.992   1.00 10.26 ? 24  GLY A N   1 
ATOM   200  C  CA  . GLY A  1 24  ? 14.358  10.490  -0.392  1.00 9.71  ? 24  GLY A CA  1 
ATOM   201  C  C   . GLY A  1 24  ? 14.391  9.068   -0.836  1.00 11.07 ? 24  GLY A C   1 
ATOM   202  O  O   . GLY A  1 24  ? 13.663  8.265   -0.228  1.00 12.84 ? 24  GLY A O   1 
ATOM   203  N  N   . LEU A  1 25  ? 15.150  8.783   -1.852  1.00 12.42 ? 25  LEU A N   1 
ATOM   204  C  CA  . LEU A  1 25  ? 15.222  7.504   -2.451  1.00 12.98 ? 25  LEU A CA  1 
ATOM   205  C  C   . LEU A  1 25  ? 16.184  6.600   -1.693  1.00 12.66 ? 25  LEU A C   1 
ATOM   206  O  O   . LEU A  1 25  ? 17.009  7.010   -0.835  1.00 13.48 ? 25  LEU A O   1 
ATOM   207  C  CB  . LEU A  1 25  ? 15.697  7.640   -3.888  1.00 19.47 ? 25  LEU A CB  1 
ATOM   208  C  CG  . LEU A  1 25  ? 14.697  8.454   -4.774  1.00 21.63 ? 25  LEU A CG  1 
ATOM   209  C  CD1 . LEU A  1 25  ? 15.476  8.699   -6.024  1.00 27.21 ? 25  LEU A CD1 1 
ATOM   210  C  CD2 . LEU A  1 25  ? 13.345  7.797   -5.091  1.00 26.71 ? 25  LEU A CD2 1 
ATOM   211  N  N   . LEU A  1 26  ? 16.031  5.311   -2.038  1.00 12.50 ? 26  LEU A N   1 
ATOM   212  C  CA  . LEU A  1 26  ? 17.001  4.253   -1.697  1.00 15.03 ? 26  LEU A CA  1 
ATOM   213  C  C   . LEU A  1 26  ? 17.025  4.033   -0.162  1.00 11.78 ? 26  LEU A C   1 
ATOM   214  O  O   . LEU A  1 26  ? 18.079  3.665   0.394   1.00 13.17 ? 26  LEU A O   1 
ATOM   215  C  CB  . LEU A  1 26  ? 18.445  4.443   -2.225  1.00 15.03 ? 26  LEU A CB  1 
ATOM   216  C  CG  . LEU A  1 26  ? 18.669  4.405   -3.757  1.00 22.45 ? 26  LEU A CG  1 
ATOM   217  C  CD1 . LEU A  1 26  ? 20.190  4.358   -4.055  1.00 23.62 ? 26  LEU A CD1 1 
ATOM   218  C  CD2 . LEU A  1 26  ? 17.983  3.171   -4.401  1.00 23.95 ? 26  LEU A CD2 1 
ATOM   219  N  N   . GLN A  1 27  ? 15.953  4.227   0.537   1.00 10.14 ? 27  GLN A N   1 
ATOM   220  C  CA  . GLN A  1 27  ? 16.029  4.142   2.020   1.00 9.07  ? 27  GLN A CA  1 
ATOM   221  C  C   . GLN A  1 27  ? 15.971  2.684   2.509   1.00 8.82  ? 27  GLN A C   1 
ATOM   222  O  O   . GLN A  1 27  ? 15.332  1.754   1.968   1.00 11.38 ? 27  GLN A O   1 
ATOM   223  C  CB  . GLN A  1 27  ? 14.857  4.860   2.656   1.00 9.11  ? 27  GLN A CB  1 
ATOM   224  C  CG  . GLN A  1 27  ? 14.896  6.389   2.358   1.00 9.27  ? 27  GLN A CG  1 
ATOM   225  C  CD  . GLN A  1 27  ? 16.084  7.018   3.043   1.00 7.34  ? 27  GLN A CD  1 
ATOM   226  O  OE1 . GLN A  1 27  ? 16.065  7.210   4.268   1.00 8.94  ? 27  GLN A OE1 1 
ATOM   227  N  NE2 . GLN A  1 27  ? 17.136  7.271   2.295   1.00 8.27  ? 27  GLN A NE2 1 
ATOM   228  N  N   . SER A  1 28  ? 16.747  2.487   3.577   1.00 8.11  ? 28  SER A N   1 
ATOM   229  C  CA  . SER A  1 28  ? 16.833  1.225   4.293   1.00 8.15  ? 28  SER A CA  1 
ATOM   230  C  C   . SER A  1 28  ? 16.307  1.433   5.731   1.00 8.80  ? 28  SER A C   1 
ATOM   231  O  O   . SER A  1 28  ? 16.195  2.574   6.209   1.00 8.18  ? 28  SER A O   1 
ATOM   232  C  CB  . SER A  1 28  ? 18.344  1.006   4.452   1.00 8.13  ? 28  SER A CB  1 
ATOM   233  O  OG  . SER A  1 28  ? 18.925  0.652   3.190   1.00 8.18  ? 28  SER A OG  1 
ATOM   234  N  N   . PRO A  1 29  ? 15.948  0.375   6.450   1.00 8.41  ? 29  PRO A N   1 
ATOM   235  C  CA  . PRO A  1 29  ? 16.046  -1.025  6.059   1.00 8.39  ? 29  PRO A CA  1 
ATOM   236  C  C   . PRO A  1 29  ? 14.824  -1.486  5.259   1.00 7.47  ? 29  PRO A C   1 
ATOM   237  O  O   . PRO A  1 29  ? 13.874  -0.667  5.075   1.00 8.76  ? 29  PRO A O   1 
ATOM   238  C  CB  . PRO A  1 29  ? 16.051  -1.764  7.437   1.00 8.02  ? 29  PRO A CB  1 
ATOM   239  C  CG  . PRO A  1 29  ? 15.078  -0.906  8.244   1.00 7.88  ? 29  PRO A CG  1 
ATOM   240  C  CD  . PRO A  1 29  ? 15.391  0.544   7.807   1.00 7.50  ? 29  PRO A CD  1 
ATOM   241  N  N   . ILE A  1 30  ? 14.854  -2.760  4.833   1.00 7.63  ? 30  ILE A N   1 
ATOM   242  C  CA  . ILE A  1 30  ? 13.800  -3.297  3.970   1.00 8.44  ? 30  ILE A CA  1 
ATOM   243  C  C   . ILE A  1 30  ? 13.548  -4.723  4.416   1.00 10.19 ? 30  ILE A C   1 
ATOM   244  O  O   . ILE A  1 30  ? 14.301  -5.317  5.216   1.00 9.70  ? 30  ILE A O   1 
ATOM   245  C  CB  . ILE A  1 30  ? 14.234  -3.302  2.481   1.00 9.59  ? 30  ILE A CB  1 
ATOM   246  C  CG1 . ILE A  1 30  ? 15.503  -4.174  2.280   1.00 9.28  ? 30  ILE A CG1 1 
ATOM   247  C  CG2 . ILE A  1 30  ? 14.460  -1.805  2.047   1.00 11.27 ? 30  ILE A CG2 1 
ATOM   248  C  CD1 . ILE A  1 30  ? 15.844  -4.334  0.773   1.00 12.06 ? 30  ILE A CD1 1 
ATOM   249  N  N   . ASP A  1 31  ? 12.396  -5.234  3.967   1.00 9.38  ? 31  ASP A N   1 
ATOM   250  C  CA  . ASP A  1 31  ? 12.075  -6.605  4.162   1.00 9.21  ? 31  ASP A CA  1 
ATOM   251  C  C   . ASP A  1 31  ? 12.672  -7.425  3.039   1.00 10.78 ? 31  ASP A C   1 
ATOM   252  O  O   . ASP A  1 31  ? 12.517  -7.163  1.838   1.00 13.42 ? 31  ASP A O   1 
ATOM   253  C  CB  . ASP A  1 31  ? 10.543  -6.768  4.133   1.00 10.91 ? 31  ASP A CB  1 
ATOM   254  C  CG  . ASP A  1 31  ? 10.129  -8.237  4.331   1.00 13.39 ? 31  ASP A CG  1 
ATOM   255  O  OD1 . ASP A  1 31  ? 10.641  -8.923  5.222   1.00 11.74 ? 31  ASP A OD1 1 
ATOM   256  O  OD2 . ASP A  1 31  ? 9.153   -8.628  3.679   1.00 17.47 ? 31  ASP A OD2 1 
ATOM   257  N  N   . LEU A  1 32  ? 13.416  -8.454  3.395   1.00 11.34 ? 32  LEU A N   1 
ATOM   258  C  CA  . LEU A  1 32  ? 14.043  -9.359  2.464   1.00 12.43 ? 32  LEU A CA  1 
ATOM   259  C  C   . LEU A  1 32  ? 13.140  -10.575 2.264   1.00 14.17 ? 32  LEU A C   1 
ATOM   260  O  O   . LEU A  1 32  ? 12.985  -11.388 3.148   1.00 14.54 ? 32  LEU A O   1 
ATOM   261  C  CB  . LEU A  1 32  ? 15.416  -9.842  3.082   1.00 12.56 ? 32  LEU A CB  1 
ATOM   262  C  CG  . LEU A  1 32  ? 16.307  -8.661  3.465   1.00 11.13 ? 32  LEU A CG  1 
ATOM   263  C  CD1 . LEU A  1 32  ? 17.536  -9.080  4.262   1.00 13.13 ? 32  LEU A CD1 1 
ATOM   264  C  CD2 . LEU A  1 32  ? 16.850  -7.932  2.219   1.00 14.63 ? 32  LEU A CD2 1 
ATOM   265  N  N   . HIS A  1 33  ? 12.462  -10.627 1.131   1.00 19.45 ? 33  HIS A N   1 
ATOM   266  C  CA  . HIS A  1 33  ? 11.491  -11.725 0.944   1.00 20.17 ? 33  HIS A CA  1 
ATOM   267  C  C   . HIS A  1 33  ? 11.647  -12.252 -0.434  1.00 23.92 ? 33  HIS A C   1 
ATOM   268  O  O   . HIS A  1 33  ? 12.106  -11.528 -1.333  1.00 22.76 ? 33  HIS A O   1 
ATOM   269  C  CB  . HIS A  1 33  ? 10.058  -11.256 1.246   1.00 21.89 ? 33  HIS A CB  1 
ATOM   270  C  CG  . HIS A  1 33  ? 9.606   -10.129 0.373   1.00 25.34 ? 33  HIS A CG  1 
ATOM   271  N  ND1 . HIS A  1 33  ? 9.885   -8.841  0.637   1.00 28.20 ? 33  HIS A ND1 1 
ATOM   272  C  CD2 . HIS A  1 33  ? 8.898   -10.152 -0.857  1.00 28.26 ? 33  HIS A CD2 1 
ATOM   273  C  CE1 . HIS A  1 33  ? 9.333   -8.042  -0.362  1.00 29.33 ? 33  HIS A CE1 1 
ATOM   274  N  NE2 . HIS A  1 33  ? 8.783   -8.853  -1.282  1.00 30.67 ? 33  HIS A NE2 1 
ATOM   275  N  N   . SER A  1 34  ? 11.148  -13.478 -0.644  1.00 22.63 ? 34  SER A N   1 
ATOM   276  C  CA  . SER A  1 34  ? 11.643  -14.276 -1.771  1.00 28.44 ? 34  SER A CA  1 
ATOM   277  C  C   . SER A  1 34  ? 11.301  -13.716 -3.140  1.00 30.16 ? 34  SER A C   1 
ATOM   278  O  O   . SER A  1 34  ? 12.092  -13.955 -4.057  1.00 35.02 ? 34  SER A O   1 
ATOM   279  C  CB  . SER A  1 34  ? 11.357  -15.781 -1.630  1.00 36.79 ? 34  SER A CB  1 
ATOM   280  O  OG  . SER A  1 34  ? 9.988   -15.912 -1.472  1.00 44.52 ? 34  SER A OG  1 
ATOM   281  N  N   . ASP A  1 35  ? 10.195  -12.956 -3.237  1.00 32.93 ? 35  ASP A N   1 
ATOM   282  C  CA  . ASP A  1 35  ? 9.694   -12.338 -4.493  1.00 37.42 ? 35  ASP A CA  1 
ATOM   283  C  C   . ASP A  1 35  ? 10.737  -11.462 -5.135  1.00 35.87 ? 35  ASP A C   1 
ATOM   284  O  O   . ASP A  1 35  ? 10.765  -11.289 -6.373  1.00 32.72 ? 35  ASP A O   1 
ATOM   285  C  CB  . ASP A  1 35  ? 8.528   -11.377 -4.200  1.00 41.73 ? 35  ASP A CB  1 
ATOM   286  C  CG  . ASP A  1 35  ? 7.176   -12.017 -4.361  1.00 57.37 ? 35  ASP A CG  1 
ATOM   287  O  OD1 . ASP A  1 35  ? 7.128   -13.138 -4.948  1.00 62.17 ? 35  ASP A OD1 1 
ATOM   288  O  OD2 . ASP A  1 35  ? 6.173   -11.394 -3.883  1.00 61.81 ? 35  ASP A OD2 1 
ATOM   289  N  N   . ILE A  1 36  ? 11.577  -10.861 -4.280  1.00 26.97 ? 36  ILE A N   1 
ATOM   290  C  CA  . ILE A  1 36  ? 12.482  -9.785  -4.718  1.00 25.06 ? 36  ILE A CA  1 
ATOM   291  C  C   . ILE A  1 36  ? 13.920  -10.211 -4.648  1.00 22.35 ? 36  ILE A C   1 
ATOM   292  O  O   . ILE A  1 36  ? 14.790  -9.380  -4.821  1.00 25.64 ? 36  ILE A O   1 
ATOM   293  C  CB  . ILE A  1 36  ? 12.279  -8.480  -3.954  1.00 22.22 ? 36  ILE A CB  1 
ATOM   294  C  CG1 . ILE A  1 36  ? 12.599  -8.687  -2.427  1.00 27.52 ? 36  ILE A CG1 1 
ATOM   295  C  CG2 . ILE A  1 36  ? 10.879  -7.920  -4.226  1.00 25.99 ? 36  ILE A CG2 1 
ATOM   296  C  CD1 . ILE A  1 36  ? 12.718  -7.392  -1.678  1.00 25.35 ? 36  ILE A CD1 1 
ATOM   297  N  N   . LEU A  1 37  ? 14.153  -11.461 -4.361  1.00 23.88 ? 37  LEU A N   1 
ATOM   298  C  CA  . LEU A  1 37  ? 15.557  -11.968 -4.264  1.00 22.67 ? 37  LEU A CA  1 
ATOM   299  C  C   . LEU A  1 37  ? 15.948  -12.471 -5.640  1.00 25.32 ? 37  LEU A C   1 
ATOM   300  O  O   . LEU A  1 37  ? 15.130  -13.100 -6.366  1.00 26.94 ? 37  LEU A O   1 
ATOM   301  C  CB  . LEU A  1 37  ? 15.590  -13.107 -3.238  1.00 22.81 ? 37  LEU A CB  1 
ATOM   302  C  CG  . LEU A  1 37  ? 15.149  -12.797 -1.819  1.00 23.25 ? 37  LEU A CG  1 
ATOM   303  C  CD1 . LEU A  1 37  ? 15.501  -14.071 -1.045  1.00 25.34 ? 37  LEU A CD1 1 
ATOM   304  C  CD2 . LEU A  1 37  ? 15.931  -11.600 -1.317  1.00 18.72 ? 37  LEU A CD2 1 
ATOM   305  N  N   . GLN A  1 38  ? 17.189  -12.260 -6.018  1.00 22.11 ? 38  GLN A N   1 
ATOM   306  C  CA  . GLN A  1 38  ? 17.704  -12.853 -7.247  1.00 23.64 ? 38  GLN A CA  1 
ATOM   307  C  C   . GLN A  1 38  ? 19.153  -13.279 -7.082  1.00 22.38 ? 38  GLN A C   1 
ATOM   308  O  O   . GLN A  1 38  ? 19.999  -12.471 -6.652  1.00 18.46 ? 38  GLN A O   1 
ATOM   309  C  CB  . GLN A  1 38  ? 17.653  -11.848 -8.385  1.00 26.94 ? 38  GLN A CB  1 
ATOM   310  C  CG  . GLN A  1 38  ? 18.112  -12.531 -9.669  1.00 32.75 ? 38  GLN A CG  1 
ATOM   311  C  CD  . GLN A  1 38  ? 17.925  -11.627 -10.814 1.00 35.81 ? 38  GLN A CD  1 
ATOM   312  O  OE1 . GLN A  1 38  ? 16.783  -11.465 -11.277 1.00 42.72 ? 38  GLN A OE1 1 
ATOM   313  N  NE2 . GLN A  1 38  ? 19.009  -10.978 -11.250 1.00 32.18 ? 38  GLN A NE2 1 
ATOM   314  N  N   . TYR A  1 39  ? 19.467  -14.536 -7.400  1.00 21.40 ? 39  TYR A N   1 
ATOM   315  C  CA  . TYR A  1 39  ? 20.759  -15.035 -7.278  1.00 20.77 ? 39  TYR A CA  1 
ATOM   316  C  C   . TYR A  1 39  ? 21.667  -14.265 -8.266  1.00 21.56 ? 39  TYR A C   1 
ATOM   317  O  O   . TYR A  1 39  ? 21.316  -14.034 -9.448  1.00 21.78 ? 39  TYR A O   1 
ATOM   318  C  CB  . TYR A  1 39  ? 20.770  -16.585 -7.594  1.00 21.76 ? 39  TYR A CB  1 
ATOM   319  C  CG  . TYR A  1 39  ? 22.154  -17.174 -7.682  1.00 22.75 ? 39  TYR A CG  1 
ATOM   320  C  CD1 . TYR A  1 39  ? 23.015  -17.181 -6.566  1.00 21.31 ? 39  TYR A CD1 1 
ATOM   321  C  CD2 . TYR A  1 39  ? 22.659  -17.686 -8.895  1.00 26.27 ? 39  TYR A CD2 1 
ATOM   322  C  CE1 . TYR A  1 39  ? 24.277  -17.711 -6.617  1.00 25.95 ? 39  TYR A CE1 1 
ATOM   323  C  CE2 . TYR A  1 39  ? 23.959  -18.152 -8.988  1.00 27.72 ? 39  TYR A CE2 1 
ATOM   324  C  CZ  . TYR A  1 39  ? 24.764  -18.217 -7.864  1.00 27.86 ? 39  TYR A CZ  1 
ATOM   325  O  OH  . TYR A  1 39  ? 26.048  -18.666 -7.996  1.00 32.86 ? 39  TYR A OH  1 
ATOM   326  N  N   . ASP A  1 40  ? 22.828  -13.889 -7.796  1.00 18.83 ? 40  ASP A N   1 
ATOM   327  C  CA  . ASP A  1 40  ? 23.820  -13.264 -8.610  1.00 20.98 ? 40  ASP A CA  1 
ATOM   328  C  C   . ASP A  1 40  ? 25.154  -13.968 -8.330  1.00 24.30 ? 40  ASP A C   1 
ATOM   329  O  O   . ASP A  1 40  ? 25.756  -13.851 -7.275  1.00 20.12 ? 40  ASP A O   1 
ATOM   330  C  CB  . ASP A  1 40  ? 23.805  -11.742 -8.334  1.00 24.17 ? 40  ASP A CB  1 
ATOM   331  C  CG  . ASP A  1 40  ? 24.842  -10.941 -9.164  1.00 31.88 ? 40  ASP A CG  1 
ATOM   332  O  OD1 . ASP A  1 40  ? 25.792  -11.506 -9.723  1.00 33.17 ? 40  ASP A OD1 1 
ATOM   333  O  OD2 . ASP A  1 40  ? 24.673  -9.695  -9.187  1.00 33.63 ? 40  ASP A OD2 1 
ATOM   334  N  N   . ALA A  1 41  ? 25.625  -14.787 -9.297  1.00 26.72 ? 41  ALA A N   1 
ATOM   335  C  CA  . ALA A  1 41  ? 26.966  -15.453 -9.166  1.00 27.47 ? 41  ALA A CA  1 
ATOM   336  C  C   . ALA A  1 41  ? 28.173  -14.490 -9.110  1.00 24.56 ? 41  ALA A C   1 
ATOM   337  O  O   . ALA A  1 41  ? 29.279  -14.895 -8.753  1.00 29.15 ? 41  ALA A O   1 
ATOM   338  C  CB  . ALA A  1 41  ? 27.165  -16.532 -10.253 1.00 32.52 ? 41  ALA A CB  1 
ATOM   339  N  N   . SER A  1 42  ? 27.973  -13.209 -9.383  1.00 26.39 ? 42  SER A N   1 
ATOM   340  C  CA  . SER A  1 42  ? 29.055  -12.194 -9.165  1.00 26.94 ? 42  SER A CA  1 
ATOM   341  C  C   . SER A  1 42  ? 29.394  -11.980 -7.692  1.00 31.15 ? 42  SER A C   1 
ATOM   342  O  O   . SER A  1 42  ? 30.430  -11.398 -7.319  1.00 29.07 ? 42  SER A O   1 
ATOM   343  C  CB  . SER A  1 42  ? 28.640  -10.857 -9.825  1.00 31.37 ? 42  SER A CB  1 
ATOM   344  O  OG  . SER A  1 42  ? 28.349  -9.773  -8.896  1.00 35.74 ? 42  SER A OG  1 
ATOM   345  N  N   . LEU A  1 43  ? 28.515  -12.481 -6.833  1.00 21.61 ? 43  LEU A N   1 
ATOM   346  C  CA  . LEU A  1 43  ? 28.623  -12.167 -5.405  1.00 20.79 ? 43  LEU A CA  1 
ATOM   347  C  C   . LEU A  1 43  ? 29.519  -13.151 -4.681  1.00 21.22 ? 43  LEU A C   1 
ATOM   348  O  O   . LEU A  1 43  ? 29.072  -14.094 -3.989  1.00 22.56 ? 43  LEU A O   1 
ATOM   349  C  CB  . LEU A  1 43  ? 27.194  -12.099 -4.814  1.00 15.45 ? 43  LEU A CB  1 
ATOM   350  C  CG  . LEU A  1 43  ? 26.406  -10.936 -5.288  1.00 16.13 ? 43  LEU A CG  1 
ATOM   351  C  CD1 . LEU A  1 43  ? 25.017  -10.899 -4.627  1.00 15.31 ? 43  LEU A CD1 1 
ATOM   352  C  CD2 . LEU A  1 43  ? 27.090  -9.563  -5.157  1.00 18.28 ? 43  LEU A CD2 1 
ATOM   353  N  N   . THR A  1 44  ? 30.819  -12.948 -4.793  1.00 20.33 ? 44  THR A N   1 
ATOM   354  C  CA  . THR A  1 44  ? 31.787  -13.842 -4.187  1.00 19.87 ? 44  THR A CA  1 
ATOM   355  C  C   . THR A  1 44  ? 32.064  -13.512 -2.712  1.00 18.91 ? 44  THR A C   1 
ATOM   356  O  O   . THR A  1 44  ? 31.584  -12.456 -2.224  1.00 17.12 ? 44  THR A O   1 
ATOM   357  C  CB  . THR A  1 44  ? 33.100  -13.781 -4.993  1.00 23.45 ? 44  THR A CB  1 
ATOM   358  O  OG1 . THR A  1 44  ? 33.435  -12.429 -5.080  1.00 25.36 ? 44  THR A OG1 1 
ATOM   359  C  CG2 . THR A  1 44  ? 32.859  -14.308 -6.426  1.00 30.38 ? 44  THR A CG2 1 
ATOM   360  N  N   . PRO A  1 45  ? 32.771  -14.372 -1.955  1.00 17.75 ? 45  PRO A N   1 
ATOM   361  C  CA  . PRO A  1 45  ? 33.003  -14.092 -0.542  1.00 18.44 ? 45  PRO A CA  1 
ATOM   362  C  C   . PRO A  1 45  ? 33.804  -12.886 -0.303  1.00 18.69 ? 45  PRO A C   1 
ATOM   363  O  O   . PRO A  1 45  ? 34.808  -12.642 -0.966  1.00 23.47 ? 45  PRO A O   1 
ATOM   364  C  CB  . PRO A  1 45  ? 33.736  -15.322 -0.044  1.00 21.35 ? 45  PRO A CB  1 
ATOM   365  C  CG  . PRO A  1 45  ? 33.347  -16.433 -1.054  1.00 20.96 ? 45  PRO A CG  1 
ATOM   366  C  CD  . PRO A  1 45  ? 33.322  -15.698 -2.368  1.00 21.57 ? 45  PRO A CD  1 
ATOM   367  N  N   . LEU A  1 46  ? 33.415  -12.127 0.683   1.00 16.45 ? 46  LEU A N   1 
ATOM   368  C  CA  . LEU A  1 46  ? 34.254  -11.012 1.212   1.00 16.70 ? 46  LEU A CA  1 
ATOM   369  C  C   . LEU A  1 46  ? 35.328  -11.629 2.132   1.00 17.73 ? 46  LEU A C   1 
ATOM   370  O  O   . LEU A  1 46  ? 35.149  -12.703 2.733   1.00 19.56 ? 46  LEU A O   1 
ATOM   371  C  CB  . LEU A  1 46  ? 33.438  -10.033 2.019   1.00 16.27 ? 46  LEU A CB  1 
ATOM   372  C  CG  . LEU A  1 46  ? 32.263  -9.383  1.316   1.00 16.40 ? 46  LEU A CG  1 
ATOM   373  C  CD1 . LEU A  1 46  ? 31.527  -8.529  2.304   1.00 17.55 ? 46  LEU A CD1 1 
ATOM   374  C  CD2 . LEU A  1 46  ? 32.821  -8.545  0.128   1.00 19.13 ? 46  LEU A CD2 1 
ATOM   375  N  N   . GLU A  1 47  ? 36.424  -10.881 2.250   1.00 17.65 ? 47  GLU A N   1 
ATOM   376  C  CA  . GLU A  1 47  ? 37.500  -11.228 3.118   1.00 18.27 ? 47  GLU A CA  1 
ATOM   377  C  C   . GLU A  1 47  ? 37.635  -10.129 4.135   1.00 18.07 ? 47  GLU A C   1 
ATOM   378  O  O   . GLU A  1 47  ? 37.625  -8.905  3.791   1.00 17.95 ? 47  GLU A O   1 
ATOM   379  C  CB  . GLU A  1 47  ? 38.822  -11.366 2.332   1.00 25.91 ? 47  GLU A CB  1 
ATOM   380  C  CG  . GLU A  1 47  ? 38.853  -12.695 1.556   1.00 35.49 ? 47  GLU A CG  1 
ATOM   381  C  CD  . GLU A  1 47  ? 39.921  -12.775 0.456   1.00 46.32 ? 47  GLU A CD  1 
ATOM   382  O  OE1 . GLU A  1 47  ? 39.575  -13.177 -0.696  1.00 50.08 ? 47  GLU A OE1 1 
ATOM   383  O  OE2 . GLU A  1 47  ? 41.099  -12.462 0.745   1.00 53.14 ? 47  GLU A OE2 1 
ATOM   384  N  N   . PHE A  1 48  ? 37.775  -10.505 5.381   1.00 17.18 ? 48  PHE A N   1 
ATOM   385  C  CA  . PHE A  1 48  ? 37.767  -9.608  6.481   1.00 16.83 ? 48  PHE A CA  1 
ATOM   386  C  C   . PHE A  1 48  ? 39.185  -9.491  7.003   1.00 19.94 ? 48  PHE A C   1 
ATOM   387  O  O   . PHE A  1 48  ? 39.686  -10.469 7.621   1.00 22.52 ? 48  PHE A O   1 
ATOM   388  C  CB  . PHE A  1 48  ? 36.766  -10.131 7.555   1.00 18.16 ? 48  PHE A CB  1 
ATOM   389  C  CG  . PHE A  1 48  ? 35.425  -10.455 6.995   1.00 17.40 ? 48  PHE A CG  1 
ATOM   390  C  CD1 . PHE A  1 48  ? 34.556  -9.453  6.557   1.00 16.89 ? 48  PHE A CD1 1 
ATOM   391  C  CD2 . PHE A  1 48  ? 35.044  -11.816 6.831   1.00 17.30 ? 48  PHE A CD2 1 
ATOM   392  C  CE1 . PHE A  1 48  ? 33.307  -9.775  5.942   1.00 16.00 ? 48  PHE A CE1 1 
ATOM   393  C  CE2 . PHE A  1 48  ? 33.839  -12.127 6.213   1.00 17.28 ? 48  PHE A CE2 1 
ATOM   394  C  CZ  . PHE A  1 48  ? 32.951  -11.108 5.731   1.00 15.36 ? 48  PHE A CZ  1 
ATOM   395  N  N   . GLN A  1 49  ? 39.793  -8.344  6.761   1.00 16.23 ? 49  GLN A N   1 
ATOM   396  C  CA  . GLN A  1 49  ? 41.265  -8.145  6.930   1.00 17.25 ? 49  GLN A CA  1 
ATOM   397  C  C   . GLN A  1 49  ? 41.504  -7.165  8.020   1.00 14.75 ? 49  GLN A C   1 
ATOM   398  O  O   . GLN A  1 49  ? 40.822  -6.155  8.227   1.00 14.27 ? 49  GLN A O   1 
ATOM   399  C  CB  . GLN A  1 49  ? 41.860  -7.540  5.659   1.00 17.99 ? 49  GLN A CB  1 
ATOM   400  C  CG  . GLN A  1 49  ? 41.794  -8.548  4.567   1.00 23.13 ? 49  GLN A CG  1 
ATOM   401  C  CD  . GLN A  1 49  ? 42.735  -8.306  3.408   1.00 30.83 ? 49  GLN A CD  1 
ATOM   402  O  OE1 . GLN A  1 49  ? 43.121  -7.138  3.072   1.00 32.73 ? 49  GLN A OE1 1 
ATOM   403  N  NE2 . GLN A  1 49  ? 43.112  -9.419  2.764   1.00 32.53 ? 49  GLN A NE2 1 
ATOM   404  N  N   . GLY A  1 50  ? 42.471  -7.453  8.916   1.00 14.62 ? 50  GLY A N   1 
ATOM   405  C  CA  . GLY A  1 50  ? 42.608  -6.583  10.004  1.00 16.42 ? 50  GLY A CA  1 
ATOM   406  C  C   . GLY A  1 50  ? 41.521  -6.586  11.113  1.00 14.16 ? 50  GLY A C   1 
ATOM   407  O  O   . GLY A  1 50  ? 41.513  -5.748  11.984  1.00 17.57 ? 50  GLY A O   1 
ATOM   408  N  N   . TYR A  1 51  ? 40.680  -7.640  11.079  1.00 14.46 ? 51  TYR A N   1 
ATOM   409  C  CA  . TYR A  1 51  ? 39.597  -7.783  12.065  1.00 17.06 ? 51  TYR A CA  1 
ATOM   410  C  C   . TYR A  1 51  ? 40.089  -8.344  13.386  1.00 16.91 ? 51  TYR A C   1 
ATOM   411  O  O   . TYR A  1 51  ? 39.449  -8.102  14.413  1.00 16.61 ? 51  TYR A O   1 
ATOM   412  C  CB  . TYR A  1 51  ? 38.487  -8.719  11.525  1.00 15.04 ? 51  TYR A CB  1 
ATOM   413  C  CG  . TYR A  1 51  ? 37.447  -7.978  10.703  1.00 13.05 ? 51  TYR A CG  1 
ATOM   414  C  CD1 . TYR A  1 51  ? 36.084  -8.238  10.958  1.00 13.33 ? 51  TYR A CD1 1 
ATOM   415  C  CD2 . TYR A  1 51  ? 37.770  -7.107  9.661   1.00 13.34 ? 51  TYR A CD2 1 
ATOM   416  C  CE1 . TYR A  1 51  ? 35.100  -7.617  10.169  1.00 11.98 ? 51  TYR A CE1 1 
ATOM   417  C  CE2 . TYR A  1 51  ? 36.782  -6.474  8.842   1.00 14.75 ? 51  TYR A CE2 1 
ATOM   418  C  CZ  . TYR A  1 51  ? 35.450  -6.697  9.159   1.00 14.51 ? 51  TYR A CZ  1 
ATOM   419  O  OH  . TYR A  1 51  ? 34.451  -6.020  8.471   1.00 15.08 ? 51  TYR A OH  1 
ATOM   420  N  N   . ASN A  1 52  ? 41.263  -9.007  13.366  1.00 18.01 ? 52  ASN A N   1 
ATOM   421  C  CA  . ASN A  1 52  ? 41.806  -9.558  14.637  1.00 20.01 ? 52  ASN A CA  1 
ATOM   422  C  C   . ASN A  1 52  ? 42.523  -8.446  15.411  1.00 21.44 ? 52  ASN A C   1 
ATOM   423  O  O   . ASN A  1 52  ? 43.760  -8.233  15.246  1.00 25.36 ? 52  ASN A O   1 
ATOM   424  C  CB  . ASN A  1 52  ? 42.691  -10.815 14.377  1.00 20.74 ? 52  ASN A CB  1 
ATOM   425  C  CG  . ASN A  1 52  ? 42.984  -11.639 15.644  1.00 24.67 ? 52  ASN A CG  1 
ATOM   426  O  OD1 . ASN A  1 52  ? 42.352  -11.513 16.681  1.00 21.69 ? 52  ASN A OD1 1 
ATOM   427  N  ND2 . ASN A  1 52  ? 43.973  -12.542 15.522  1.00 30.90 ? 52  ASN A ND2 1 
ATOM   428  N  N   . LEU A  1 53  ? 41.806  -7.645  16.162  1.00 21.56 ? 53  LEU A N   1 
ATOM   429  C  CA  . LEU A  1 53  ? 42.333  -6.432  16.739  1.00 19.13 ? 53  LEU A CA  1 
ATOM   430  C  C   . LEU A  1 53  ? 43.342  -6.784  17.808  1.00 24.51 ? 53  LEU A C   1 
ATOM   431  O  O   . LEU A  1 53  ? 43.124  -7.729  18.557  1.00 25.04 ? 53  LEU A O   1 
ATOM   432  C  CB  . LEU A  1 53  ? 41.266  -5.485  17.321  1.00 19.55 ? 53  LEU A CB  1 
ATOM   433  C  CG  . LEU A  1 53  ? 40.142  -5.131  16.344  1.00 18.07 ? 53  LEU A CG  1 
ATOM   434  C  CD1 . LEU A  1 53  ? 39.171  -4.290  17.116  1.00 18.30 ? 53  LEU A CD1 1 
ATOM   435  C  CD2 . LEU A  1 53  ? 40.613  -4.447  15.050  1.00 20.11 ? 53  LEU A CD2 1 
ATOM   436  N  N   . SER A  1 54  ? 44.471  -6.087  17.732  1.00 21.69 ? 54  SER A N   1 
ATOM   437  C  CA  . SER A  1 54  ? 45.523  -6.261  18.776  1.00 23.70 ? 54  SER A CA  1 
ATOM   438  C  C   . SER A  1 54  ? 44.899  -6.286  20.197  1.00 23.02 ? 54  SER A C   1 
ATOM   439  O  O   . SER A  1 54  ? 44.272  -5.311  20.618  1.00 22.47 ? 54  SER A O   1 
ATOM   440  C  CB  . SER A  1 54  ? 46.493  -5.071  18.666  1.00 25.00 ? 54  SER A CB  1 
ATOM   441  O  OG  . SER A  1 54  ? 47.563  -5.359  19.588  1.00 30.34 ? 54  SER A OG  1 
ATOM   442  N  N   . ALA A  1 55  ? 45.063  -7.379  20.944  1.00 24.80 ? 55  ALA A N   1 
ATOM   443  C  CA  . ALA A  1 55  ? 44.639  -7.308  22.349  1.00 27.06 ? 55  ALA A CA  1 
ATOM   444  C  C   . ALA A  1 55  ? 45.540  -6.371  23.175  1.00 28.66 ? 55  ALA A C   1 
ATOM   445  O  O   . ALA A  1 55  ? 45.280  -6.135  24.331  1.00 31.41 ? 55  ALA A O   1 
ATOM   446  C  CB  . ALA A  1 55  ? 44.569  -8.698  22.992  1.00 33.47 ? 55  ALA A CB  1 
ATOM   447  N  N   . ASN A  1 56  ? 46.572  -5.790  22.549  1.00 30.83 ? 56  ASN A N   1 
ATOM   448  C  CA  . ASN A  1 56  ? 47.385  -4.727  23.230  1.00 29.40 ? 56  ASN A CA  1 
ATOM   449  C  C   . ASN A  1 56  ? 46.947  -3.323  22.851  1.00 32.78 ? 56  ASN A C   1 
ATOM   450  O  O   . ASN A  1 56  ? 47.610  -2.359  23.183  1.00 31.62 ? 56  ASN A O   1 
ATOM   451  C  CB  . ASN A  1 56  ? 48.892  -4.862  22.876  1.00 30.61 ? 56  ASN A CB  1 
ATOM   452  C  CG  . ASN A  1 56  ? 49.465  -6.208  23.232  1.00 37.65 ? 56  ASN A CG  1 
ATOM   453  O  OD1 . ASN A  1 56  ? 49.256  -6.724  24.358  1.00 36.80 ? 56  ASN A OD1 1 
ATOM   454  N  ND2 . ASN A  1 56  ? 50.143  -6.828  22.265  1.00 36.86 ? 56  ASN A ND2 1 
ATOM   455  N  N   . LYS A  1 57  ? 45.873  -3.205  22.056  1.00 26.74 ? 57  LYS A N   1 
ATOM   456  C  CA  . LYS A  1 57  ? 45.280  -1.892  21.747  1.00 25.75 ? 57  LYS A CA  1 
ATOM   457  C  C   . LYS A  1 57  ? 43.905  -1.807  22.448  1.00 22.58 ? 57  LYS A C   1 
ATOM   458  O  O   . LYS A  1 57  ? 43.302  -2.856  22.757  1.00 23.91 ? 57  LYS A O   1 
ATOM   459  C  CB  . LYS A  1 57  ? 45.127  -1.688  20.207  1.00 29.15 ? 57  LYS A CB  1 
ATOM   460  C  CG  . LYS A  1 57  ? 46.377  -1.170  19.518  1.00 38.00 ? 57  LYS A CG  1 
ATOM   461  C  CD  . LYS A  1 57  ? 46.303  -1.441  18.017  1.00 39.26 ? 57  LYS A CD  1 
ATOM   462  C  CE  . LYS A  1 57  ? 45.084  -0.815  17.334  1.00 43.14 ? 57  LYS A CE  1 
ATOM   463  N  NZ  . LYS A  1 57  ? 45.077  0.672   17.332  1.00 41.28 ? 57  LYS A NZ  1 
ATOM   464  N  N   . GLN A  1 58  ? 43.481  -0.589  22.750  1.00 24.89 ? 58  GLN A N   1 
ATOM   465  C  CA  . GLN A  1 58  ? 42.083  -0.375  23.208  1.00 24.78 ? 58  GLN A CA  1 
ATOM   466  C  C   . GLN A  1 58  ? 41.267  0.428   22.303  1.00 24.77 ? 58  GLN A C   1 
ATOM   467  O  O   . GLN A  1 58  ? 41.760  1.311   21.611  1.00 26.35 ? 58  GLN A O   1 
ATOM   468  C  CB  . GLN A  1 58  ? 42.107  0.297   24.560  1.00 24.22 ? 58  GLN A CB  1 
ATOM   469  C  CG  . GLN A  1 58  ? 42.582  -0.721  25.538  1.00 25.36 ? 58  GLN A CG  1 
ATOM   470  C  CD  . GLN A  1 58  ? 42.956  -0.070  26.844  1.00 26.25 ? 58  GLN A CD  1 
ATOM   471  O  OE1 . GLN A  1 58  ? 42.791  1.140   27.019  1.00 30.29 ? 58  GLN A OE1 1 
ATOM   472  N  NE2 . GLN A  1 58  ? 43.486  -0.844  27.721  1.00 25.40 ? 58  GLN A NE2 1 
ATOM   473  N  N   . PHE A  1 59  ? 39.961  0.063   22.273  1.00 22.32 ? 59  PHE A N   1 
ATOM   474  C  CA  . PHE A  1 59  ? 38.997  0.684   21.363  1.00 20.33 ? 59  PHE A CA  1 
ATOM   475  C  C   . PHE A  1 59  ? 37.869  1.300   22.162  1.00 17.55 ? 59  PHE A C   1 
ATOM   476  O  O   . PHE A  1 59  ? 37.411  0.683   23.115  1.00 18.98 ? 59  PHE A O   1 
ATOM   477  C  CB  . PHE A  1 59  ? 38.547  -0.361  20.360  1.00 21.74 ? 59  PHE A CB  1 
ATOM   478  C  CG  . PHE A  1 59  ? 39.695  -0.944  19.609  1.00 19.59 ? 59  PHE A CG  1 
ATOM   479  C  CD1 . PHE A  1 59  ? 40.113  -0.362  18.445  1.00 21.26 ? 59  PHE A CD1 1 
ATOM   480  C  CD2 . PHE A  1 59  ? 40.488  -1.982  20.151  1.00 21.31 ? 59  PHE A CD2 1 
ATOM   481  C  CE1 . PHE A  1 59  ? 41.241  -0.860  17.754  1.00 21.71 ? 59  PHE A CE1 1 
ATOM   482  C  CE2 . PHE A  1 59  ? 41.640  -2.481  19.457  1.00 18.71 ? 59  PHE A CE2 1 
ATOM   483  C  CZ  . PHE A  1 59  ? 41.986  -1.902  18.260  1.00 21.77 ? 59  PHE A CZ  1 
ATOM   484  N  N   . LEU A  1 60  ? 37.514  2.505   21.795  1.00 18.00 ? 60  LEU A N   1 
ATOM   485  C  CA  . LEU A  1 60  ? 36.595  3.333   22.551  1.00 18.58 ? 60  LEU A CA  1 
ATOM   486  C  C   . LEU A  1 60  ? 35.128  2.866   22.318  1.00 20.47 ? 60  LEU A C   1 
ATOM   487  O  O   . LEU A  1 60  ? 34.640  2.923   21.175  1.00 17.42 ? 60  LEU A O   1 
ATOM   488  C  CB  . LEU A  1 60  ? 36.743  4.773   22.226  1.00 20.04 ? 60  LEU A CB  1 
ATOM   489  C  CG  . LEU A  1 60  ? 35.945  5.720   23.050  1.00 24.79 ? 60  LEU A CG  1 
ATOM   490  C  CD1 . LEU A  1 60  ? 36.472  5.690   24.497  1.00 26.52 ? 60  LEU A CD1 1 
ATOM   491  C  CD2 . LEU A  1 60  ? 35.950  7.108   22.395  1.00 24.64 ? 60  LEU A CD2 1 
ATOM   492  N  N   . LEU A  1 61  ? 34.452  2.479   23.368  1.00 17.78 ? 61  LEU A N   1 
ATOM   493  C  CA  . LEU A  1 61  ? 32.991  2.252   23.350  1.00 18.04 ? 61  LEU A CA  1 
ATOM   494  C  C   . LEU A  1 61  ? 32.311  3.498   23.824  1.00 17.71 ? 61  LEU A C   1 
ATOM   495  O  O   . LEU A  1 61  ? 32.661  4.065   24.865  1.00 18.14 ? 61  LEU A O   1 
ATOM   496  C  CB  . LEU A  1 61  ? 32.667  1.102   24.248  1.00 19.53 ? 61  LEU A CB  1 
ATOM   497  C  CG  . LEU A  1 61  ? 31.277  0.401   24.180  1.00 18.86 ? 61  LEU A CG  1 
ATOM   498  C  CD1 . LEU A  1 61  ? 31.215  -0.523  22.941  1.00 17.45 ? 61  LEU A CD1 1 
ATOM   499  C  CD2 . LEU A  1 61  ? 31.075  -0.466  25.410  1.00 20.28 ? 61  LEU A CD2 1 
ATOM   500  N  N   A THR A  1 62  ? 31.296  3.993   23.106  0.50 17.15 ? 62  THR A N   1 
ATOM   501  N  N   B THR A  1 62  ? 31.264  3.908   23.126  0.50 16.66 ? 62  THR A N   1 
ATOM   502  C  CA  A THR A  1 62  ? 30.554  5.180   23.511  0.50 17.57 ? 62  THR A CA  1 
ATOM   503  C  CA  B THR A  1 62  ? 30.493  5.002   23.592  0.50 16.35 ? 62  THR A CA  1 
ATOM   504  C  C   A THR A  1 62  ? 29.040  4.915   23.477  0.50 18.37 ? 62  THR A C   1 
ATOM   505  C  C   B THR A  1 62  ? 28.994  4.769   23.557  0.50 17.13 ? 62  THR A C   1 
ATOM   506  O  O   A THR A  1 62  ? 28.553  4.216   22.574  0.50 18.66 ? 62  THR A O   1 
ATOM   507  O  O   B THR A  1 62  ? 28.476  3.993   22.723  0.50 18.03 ? 62  THR A O   1 
ATOM   508  C  CB  A THR A  1 62  ? 30.799  6.433   22.596  0.50 20.88 ? 62  THR A CB  1 
ATOM   509  C  CB  B THR A  1 62  ? 30.834  6.336   22.878  0.50 18.17 ? 62  THR A CB  1 
ATOM   510  O  OG1 A THR A  1 62  ? 32.202  6.693   22.364  0.50 22.32 ? 62  THR A OG1 1 
ATOM   511  O  OG1 B THR A  1 62  ? 30.557  6.264   21.455  0.50 18.43 ? 62  THR A OG1 1 
ATOM   512  C  CG2 A THR A  1 62  ? 30.111  7.694   23.135  0.50 21.56 ? 62  THR A CG2 1 
ATOM   513  C  CG2 B THR A  1 62  ? 32.315  6.674   23.080  0.50 21.78 ? 62  THR A CG2 1 
ATOM   514  N  N   . ASN A  1 63  ? 28.287  5.514   24.396  1.00 16.54 ? 63  ASN A N   1 
ATOM   515  C  CA  . ASN A  1 63  ? 26.819  5.684   24.217  1.00 15.78 ? 63  ASN A CA  1 
ATOM   516  C  C   . ASN A  1 63  ? 26.621  7.067   23.639  1.00 16.50 ? 63  ASN A C   1 
ATOM   517  O  O   . ASN A  1 63  ? 26.921  8.154   24.228  1.00 17.79 ? 63  ASN A O   1 
ATOM   518  C  CB  . ASN A  1 63  ? 26.186  5.529   25.584  1.00 14.96 ? 63  ASN A CB  1 
ATOM   519  C  CG  . ASN A  1 63  ? 24.688  5.856   25.629  1.00 17.20 ? 63  ASN A CG  1 
ATOM   520  O  OD1 . ASN A  1 63  ? 24.166  6.576   24.783  1.00 16.57 ? 63  ASN A OD1 1 
ATOM   521  N  ND2 . ASN A  1 63  ? 24.002  5.368   26.684  1.00 16.54 ? 63  ASN A ND2 1 
ATOM   522  N  N   . ASN A  1 64  ? 26.080  7.105   22.406  1.00 17.04 ? 64  ASN A N   1 
ATOM   523  C  CA  . ASN A  1 64  ? 25.890  8.384   21.729  1.00 18.16 ? 64  ASN A CA  1 
ATOM   524  C  C   . ASN A  1 64  ? 24.450  8.876   21.777  1.00 17.01 ? 64  ASN A C   1 
ATOM   525  O  O   . ASN A  1 64  ? 24.103  9.860   21.061  1.00 19.66 ? 64  ASN A O   1 
ATOM   526  C  CB  . ASN A  1 64  ? 26.346  8.333   20.239  1.00 18.22 ? 64  ASN A CB  1 
ATOM   527  C  CG  . ASN A  1 64  ? 25.520  7.337   19.413  1.00 19.21 ? 64  ASN A CG  1 
ATOM   528  O  OD1 . ASN A  1 64  ? 24.525  6.802   19.891  1.00 17.00 ? 64  ASN A OD1 1 
ATOM   529  N  ND2 . ASN A  1 64  ? 25.958  7.066   18.178  1.00 23.34 ? 64  ASN A ND2 1 
ATOM   530  N  N   . GLY A  1 65  ? 23.665  8.290   22.664  1.00 16.46 ? 65  GLY A N   1 
ATOM   531  C  CA  . GLY A  1 65  ? 22.288  8.667   22.821  1.00 17.29 ? 65  GLY A CA  1 
ATOM   532  C  C   . GLY A  1 65  ? 21.358  7.953   21.831  1.00 18.52 ? 65  GLY A C   1 
ATOM   533  O  O   . GLY A  1 65  ? 20.154  8.070   22.011  1.00 19.31 ? 65  GLY A O   1 
ATOM   534  N  N   . HIS A  1 66  ? 21.886  7.229   20.835  1.00 15.81 ? 66  HIS A N   1 
ATOM   535  C  CA  . HIS A  1 66  ? 21.084  6.479   19.896  1.00 13.90 ? 66  HIS A CA  1 
ATOM   536  C  C   . HIS A  1 66  ? 21.382  5.000   19.818  1.00 14.32 ? 66  HIS A C   1 
ATOM   537  O  O   . HIS A  1 66  ? 20.496  4.214   19.474  1.00 14.64 ? 66  HIS A O   1 
ATOM   538  C  CB  . HIS A  1 66  ? 21.233  7.054   18.483  1.00 15.09 ? 66  HIS A CB  1 
ATOM   539  C  CG  . HIS A  1 66  ? 21.075  8.544   18.419  1.00 15.72 ? 66  HIS A CG  1 
ATOM   540  N  ND1 . HIS A  1 66  ? 19.841  9.187   18.560  1.00 17.06 ? 66  HIS A ND1 1 
ATOM   541  C  CD2 . HIS A  1 66  ? 22.023  9.535   18.185  1.00 16.10 ? 66  HIS A CD2 1 
ATOM   542  C  CE1 . HIS A  1 66  ? 20.044  10.529  18.477  1.00 16.18 ? 66  HIS A CE1 1 
ATOM   543  N  NE2 . HIS A  1 66  ? 21.355  10.726  18.171  1.00 18.97 ? 66  HIS A NE2 1 
ATOM   544  N  N   . SER A  1 67  ? 22.615  4.587   20.132  1.00 13.91 ? 67  SER A N   1 
ATOM   545  C  CA  . SER A  1 67  ? 23.062  3.192   20.170  1.00 13.79 ? 67  SER A CA  1 
ATOM   546  C  C   . SER A  1 67  ? 24.307  3.143   21.034  1.00 14.24 ? 67  SER A C   1 
ATOM   547  O  O   . SER A  1 67  ? 24.710  4.144   21.602  1.00 14.98 ? 67  SER A O   1 
ATOM   548  C  CB  . SER A  1 67  ? 23.418  2.706   18.780  1.00 12.72 ? 67  SER A CB  1 
ATOM   549  O  OG  . SER A  1 67  ? 23.742  1.290   18.714  1.00 15.22 ? 67  SER A OG  1 
ATOM   550  N  N   . VAL A  1 68  ? 24.845  1.947   21.125  1.00 13.27 ? 68  VAL A N   1 
ATOM   551  C  CA  . VAL A  1 68  ? 26.200  1.804   21.684  1.00 13.44 ? 68  VAL A CA  1 
ATOM   552  C  C   . VAL A  1 68  ? 27.123  1.501   20.509  1.00 14.50 ? 68  VAL A C   1 
ATOM   553  O  O   . VAL A  1 68  ? 26.814  0.656   19.678  1.00 14.95 ? 68  VAL A O   1 
ATOM   554  C  CB  . VAL A  1 68  ? 26.169  0.720   22.803  1.00 15.79 ? 68  VAL A CB  1 
ATOM   555  C  CG1 . VAL A  1 68  ? 25.638  -0.650  22.387  1.00 18.07 ? 68  VAL A CG1 1 
ATOM   556  C  CG2 . VAL A  1 68  ? 27.612  0.517   23.296  1.00 16.59 ? 68  VAL A CG2 1 
ATOM   557  N  N   . LYS A  1 69  ? 28.213  2.267   20.473  1.00 14.50 ? 69  LYS A N   1 
ATOM   558  C  CA  . LYS A  1 69  ? 29.144  2.151   19.337  1.00 14.91 ? 69  LYS A CA  1 
ATOM   559  C  C   . LYS A  1 69  ? 30.567  1.879   19.783  1.00 14.25 ? 69  LYS A C   1 
ATOM   560  O  O   . LYS A  1 69  ? 31.028  2.500   20.769  1.00 18.04 ? 69  LYS A O   1 
ATOM   561  C  CB  . LYS A  1 69  ? 29.089  3.392   18.481  1.00 18.29 ? 69  LYS A CB  1 
ATOM   562  C  CG  . LYS A  1 69  ? 29.548  4.689   18.922  1.00 25.48 ? 69  LYS A CG  1 
ATOM   563  C  CD  . LYS A  1 69  ? 29.818  5.493   17.646  1.00 25.94 ? 69  LYS A CD  1 
ATOM   564  C  CE  . LYS A  1 69  ? 30.484  6.771   18.113  1.00 31.74 ? 69  LYS A CE  1 
ATOM   565  N  NZ  . LYS A  1 69  ? 30.499  7.792   17.011  1.00 31.85 ? 69  LYS A NZ  1 
ATOM   566  N  N   . LEU A  1 70  ? 31.215  0.975   19.086  1.00 13.82 ? 70  LEU A N   1 
ATOM   567  C  CA  . LEU A  1 70  ? 32.668  0.708   19.286  1.00 14.19 ? 70  LEU A CA  1 
ATOM   568  C  C   . LEU A  1 70  ? 33.402  1.303   18.143  1.00 13.08 ? 70  LEU A C   1 
ATOM   569  O  O   . LEU A  1 70  ? 33.172  0.947   16.989  1.00 13.49 ? 70  LEU A O   1 
ATOM   570  C  CB  . LEU A  1 70  ? 32.825  -0.745  19.423  1.00 13.57 ? 70  LEU A CB  1 
ATOM   571  C  CG  . LEU A  1 70  ? 34.325  -1.203  19.659  1.00 13.44 ? 70  LEU A CG  1 
ATOM   572  C  CD1 . LEU A  1 70  ? 34.803  -0.733  21.024  1.00 15.84 ? 70  LEU A CD1 1 
ATOM   573  C  CD2 . LEU A  1 70  ? 34.323  -2.723  19.465  1.00 14.29 ? 70  LEU A CD2 1 
ATOM   574  N  N   . ASN A  1 71  ? 34.427  2.160   18.417  1.00 13.49 ? 71  ASN A N   1 
ATOM   575  C  CA  . ASN A  1 71  ? 35.271  2.680   17.350  1.00 15.00 ? 71  ASN A CA  1 
ATOM   576  C  C   . ASN A  1 71  ? 36.255  1.641   16.907  1.00 16.45 ? 71  ASN A C   1 
ATOM   577  O  O   . ASN A  1 71  ? 36.743  0.829   17.699  1.00 17.57 ? 71  ASN A O   1 
ATOM   578  C  CB  . ASN A  1 71  ? 36.001  3.938   17.847  1.00 17.39 ? 71  ASN A CB  1 
ATOM   579  C  CG  . ASN A  1 71  ? 35.077  5.117   18.020  1.00 27.51 ? 71  ASN A CG  1 
ATOM   580  O  OD1 . ASN A  1 71  ? 33.884  5.049   17.740  1.00 30.76 ? 71  ASN A OD1 1 
ATOM   581  N  ND2 . ASN A  1 71  ? 35.637  6.250   18.493  1.00 36.19 ? 71  ASN A ND2 1 
ATOM   582  N  N   . LEU A  1 72  ? 36.463  1.603   15.573  1.00 14.11 ? 72  LEU A N   1 
ATOM   583  C  CA  . LEU A  1 72  ? 37.289  0.564   14.956  1.00 14.14 ? 72  LEU A CA  1 
ATOM   584  C  C   . LEU A  1 72  ? 38.442  1.284   14.247  1.00 15.38 ? 72  LEU A C   1 
ATOM   585  O  O   . LEU A  1 72  ? 38.285  2.411   13.772  1.00 17.82 ? 72  LEU A O   1 
ATOM   586  C  CB  . LEU A  1 72  ? 36.426  -0.264  13.919  1.00 12.28 ? 72  LEU A CB  1 
ATOM   587  C  CG  . LEU A  1 72  ? 35.351  -1.096  14.658  1.00 13.26 ? 72  LEU A CG  1 
ATOM   588  C  CD1 . LEU A  1 72  ? 34.437  -1.650  13.585  1.00 13.25 ? 72  LEU A CD1 1 
ATOM   589  C  CD2 . LEU A  1 72  ? 35.848  -2.198  15.622  1.00 13.66 ? 72  LEU A CD2 1 
ATOM   590  N  N   . PRO A  1 73  ? 39.577  0.571   14.026  1.00 16.24 ? 73  PRO A N   1 
ATOM   591  C  CA  . PRO A  1 73  ? 40.727  1.258   13.351  1.00 18.33 ? 73  PRO A CA  1 
ATOM   592  C  C   . PRO A  1 73  ? 40.658  1.169   11.834  1.00 16.97 ? 73  PRO A C   1 
ATOM   593  O  O   . PRO A  1 73  ? 40.223  0.159   11.304  1.00 20.12 ? 73  PRO A O   1 
ATOM   594  C  CB  . PRO A  1 73  ? 41.915  0.452   13.889  1.00 19.41 ? 73  PRO A CB  1 
ATOM   595  C  CG  . PRO A  1 73  ? 41.390  -0.972  14.081  1.00 16.62 ? 73  PRO A CG  1 
ATOM   596  C  CD  . PRO A  1 73  ? 39.874  -0.819  14.434  1.00 15.70 ? 73  PRO A CD  1 
ATOM   597  N  N   . SER A  1 74  ? 41.195  2.180   11.147  1.00 22.32 ? 74  SER A N   1 
ATOM   598  C  CA  . SER A  1 74  ? 41.125  2.130   9.698   1.00 24.66 ? 74  SER A CA  1 
ATOM   599  C  C   . SER A  1 74  ? 42.075  1.101   9.076   1.00 22.18 ? 74  SER A C   1 
ATOM   600  O  O   . SER A  1 74  ? 41.956  0.911   7.846   1.00 25.92 ? 74  SER A O   1 
ATOM   601  C  CB  . SER A  1 74  ? 41.429  3.451   9.034   1.00 25.88 ? 74  SER A CB  1 
ATOM   602  O  OG  . SER A  1 74  ? 42.693  3.848   9.561   1.00 26.86 ? 74  SER A OG  1 
ATOM   603  N  N   . ASP A  1 75  ? 42.941  0.393   9.829   1.00 19.48 ? 75  ASP A N   1 
ATOM   604  C  CA  . ASP A  1 75  ? 43.577  -0.758  9.137   1.00 19.11 ? 75  ASP A CA  1 
ATOM   605  C  C   . ASP A  1 75  ? 42.674  -1.977  9.030   1.00 17.59 ? 75  ASP A C   1 
ATOM   606  O  O   . ASP A  1 75  ? 43.004  -2.983  8.374   1.00 18.92 ? 75  ASP A O   1 
ATOM   607  C  CB  . ASP A  1 75  ? 44.930  -1.149  9.826   1.00 20.05 ? 75  ASP A CB  1 
ATOM   608  C  CG  . ASP A  1 75  ? 44.682  -1.679  11.220  1.00 21.98 ? 75  ASP A CG  1 
ATOM   609  O  OD1 . ASP A  1 75  ? 44.278  -0.867  12.100  1.00 28.12 ? 75  ASP A OD1 1 
ATOM   610  O  OD2 . ASP A  1 75  ? 44.927  -2.861  11.428  1.00 29.84 ? 75  ASP A OD2 1 
ATOM   611  N  N   . MET A  1 76  ? 41.476  -1.929  9.662   1.00 16.30 ? 76  MET A N   1 
ATOM   612  C  CA  . MET A  1 76  ? 40.550  -3.024  9.474   1.00 16.00 ? 76  MET A CA  1 
ATOM   613  C  C   . MET A  1 76  ? 39.709  -2.739  8.232   1.00 12.63 ? 76  MET A C   1 
ATOM   614  O  O   . MET A  1 76  ? 39.284  -1.581  8.053   1.00 13.58 ? 76  MET A O   1 
ATOM   615  C  CB  . MET A  1 76  ? 39.694  -3.011  10.700  1.00 18.11 ? 76  MET A CB  1 
ATOM   616  C  CG  . MET A  1 76  ? 38.539  -3.905  10.727  1.00 17.28 ? 76  MET A CG  1 
ATOM   617  S  SD  . MET A  1 76  ? 37.767  -3.848  12.395  1.00 16.34 ? 76  MET A SD  1 
ATOM   618  C  CE  . MET A  1 76  ? 36.201  -4.615  11.983  1.00 17.29 ? 76  MET A CE  1 
ATOM   619  N  N   . HIS A  1 77  ? 39.615  -3.674  7.348   1.00 12.78 ? 77  HIS A N   1 
ATOM   620  C  CA  . HIS A  1 77  ? 38.850  -3.464  6.067   1.00 12.64 ? 77  HIS A CA  1 
ATOM   621  C  C   . HIS A  1 77  ? 38.297  -4.687  5.455   1.00 13.86 ? 77  HIS A C   1 
ATOM   622  O  O   . HIS A  1 77  ? 38.625  -5.846  5.813   1.00 14.34 ? 77  HIS A O   1 
ATOM   623  C  CB  . HIS A  1 77  ? 39.762  -2.727  5.047   1.00 14.91 ? 77  HIS A CB  1 
ATOM   624  C  CG  . HIS A  1 77  ? 40.971  -3.547  4.644   1.00 17.28 ? 77  HIS A CG  1 
ATOM   625  N  ND1 . HIS A  1 77  ? 42.175  -3.353  5.230   1.00 22.08 ? 77  HIS A ND1 1 
ATOM   626  C  CD2 . HIS A  1 77  ? 41.135  -4.494  3.691   1.00 19.47 ? 77  HIS A CD2 1 
ATOM   627  C  CE1 . HIS A  1 77  ? 43.066  -4.169  4.696   1.00 20.47 ? 77  HIS A CE1 1 
ATOM   628  N  NE2 . HIS A  1 77  ? 42.487  -4.888  3.767   1.00 22.96 ? 77  HIS A NE2 1 
ATOM   629  N  N   . ILE A  1 78  ? 37.338  -4.461  4.565   1.00 13.49 ? 78  ILE A N   1 
ATOM   630  C  CA  . ILE A  1 78  ? 36.801  -5.498  3.685   1.00 15.14 ? 78  ILE A CA  1 
ATOM   631  C  C   . ILE A  1 78  ? 37.575  -5.560  2.406   1.00 15.17 ? 78  ILE A C   1 
ATOM   632  O  O   . ILE A  1 78  ? 37.825  -4.511  1.790   1.00 14.56 ? 78  ILE A O   1 
ATOM   633  C  CB  . ILE A  1 78  ? 35.306  -5.137  3.314   1.00 14.90 ? 78  ILE A CB  1 
ATOM   634  C  CG1 . ILE A  1 78  ? 34.398  -5.172  4.547   1.00 19.25 ? 78  ILE A CG1 1 
ATOM   635  C  CG2 . ILE A  1 78  ? 34.893  -6.070  2.199   1.00 20.27 ? 78  ILE A CG2 1 
ATOM   636  C  CD1 . ILE A  1 78  ? 33.083  -4.393  4.232   1.00 17.07 ? 78  ILE A CD1 1 
ATOM   637  N  N   . GLN A  1 79  ? 37.967  -6.782  1.999   1.00 15.83 ? 79  GLN A N   1 
ATOM   638  C  CA  . GLN A  1 79  ? 38.503  -7.017  0.711   1.00 20.62 ? 79  GLN A CA  1 
ATOM   639  C  C   . GLN A  1 79  ? 37.493  -7.805  -0.115  1.00 18.63 ? 79  GLN A C   1 
ATOM   640  O  O   . GLN A  1 79  ? 36.795  -8.664  0.445   1.00 21.23 ? 79  GLN A O   1 
ATOM   641  C  CB  . GLN A  1 79  ? 39.804  -7.821  0.921   1.00 26.00 ? 79  GLN A CB  1 
ATOM   642  C  CG  . GLN A  1 79  ? 40.481  -8.332  -0.365  1.00 31.49 ? 79  GLN A CG  1 
ATOM   643  C  CD  . GLN A  1 79  ? 41.379  -7.259  -0.980  1.00 44.14 ? 79  GLN A CD  1 
ATOM   644  O  OE1 . GLN A  1 79  ? 41.670  -6.230  -0.337  1.00 49.45 ? 79  GLN A OE1 1 
ATOM   645  N  NE2 . GLN A  1 79  ? 41.832  -7.488  -2.230  1.00 42.15 ? 79  GLN A NE2 1 
ATOM   646  N  N   . GLY A  1 80  ? 37.370  -7.524  -1.393  1.00 20.05 ? 80  GLY A N   1 
ATOM   647  C  CA  . GLY A  1 80  ? 36.443  -8.240  -2.256  1.00 20.80 ? 80  GLY A CA  1 
ATOM   648  C  C   . GLY A  1 80  ? 35.473  -7.362  -3.004  1.00 20.44 ? 80  GLY A C   1 
ATOM   649  O  O   . GLY A  1 80  ? 34.855  -7.737  -3.982  1.00 21.56 ? 80  GLY A O   1 
ATOM   650  N  N   . LEU A  1 81  ? 35.318  -6.137  -2.548  1.00 17.70 ? 81  LEU A N   1 
ATOM   651  C  CA  . LEU A  1 81  ? 34.516  -5.149  -3.291  1.00 18.60 ? 81  LEU A CA  1 
ATOM   652  C  C   . LEU A  1 81  ? 35.469  -4.398  -4.258  1.00 20.99 ? 81  LEU A C   1 
ATOM   653  O  O   . LEU A  1 81  ? 36.694  -4.624  -4.244  1.00 21.38 ? 81  LEU A O   1 
ATOM   654  C  CB  . LEU A  1 81  ? 33.818  -4.160  -2.341  1.00 17.31 ? 81  LEU A CB  1 
ATOM   655  C  CG  . LEU A  1 81  ? 32.839  -4.792  -1.330  1.00 16.17 ? 81  LEU A CG  1 
ATOM   656  C  CD1 . LEU A  1 81  ? 32.342  -3.785  -0.292  1.00 16.07 ? 81  LEU A CD1 1 
ATOM   657  C  CD2 . LEU A  1 81  ? 31.655  -5.361  -2.194  1.00 17.04 ? 81  LEU A CD2 1 
ATOM   658  N  N   . GLN A  1 82  ? 34.936  -3.561  -5.110  1.00 23.55 ? 82  GLN A N   1 
ATOM   659  C  CA  . GLN A  1 82  ? 35.832  -2.964  -6.124  1.00 24.54 ? 82  GLN A CA  1 
ATOM   660  C  C   . GLN A  1 82  ? 36.874  -1.982  -5.497  1.00 22.17 ? 82  GLN A C   1 
ATOM   661  O  O   . GLN A  1 82  ? 38.043  -1.928  -5.933  1.00 21.27 ? 82  GLN A O   1 
ATOM   662  C  CB  . GLN A  1 82  ? 35.002  -2.293  -7.161  1.00 28.77 ? 82  GLN A CB  1 
ATOM   663  C  CG  . GLN A  1 82  ? 35.898  -1.577  -8.105  1.00 37.25 ? 82  GLN A CG  1 
ATOM   664  C  CD  . GLN A  1 82  ? 35.145  -0.938  -9.226  1.00 46.01 ? 82  GLN A CD  1 
ATOM   665  O  OE1 . GLN A  1 82  ? 34.822  -1.607  -10.221 1.00 50.42 ? 82  GLN A OE1 1 
ATOM   666  N  NE2 . GLN A  1 82  ? 34.895  0.378   -9.094  1.00 32.44 ? 82  GLN A NE2 1 
ATOM   667  N  N   . SER A  1 83  ? 36.485  -1.274  -4.472  1.00 17.85 ? 83  SER A N   1 
ATOM   668  C  CA  . SER A  1 83  ? 37.422  -0.464  -3.722  1.00 14.38 ? 83  SER A CA  1 
ATOM   669  C  C   . SER A  1 83  ? 37.562  -1.117  -2.362  1.00 14.10 ? 83  SER A C   1 
ATOM   670  O  O   . SER A  1 83  ? 36.699  -1.940  -1.951  1.00 12.79 ? 83  SER A O   1 
ATOM   671  C  CB  . SER A  1 83  ? 36.790  0.881   -3.437  1.00 15.46 ? 83  SER A CB  1 
ATOM   672  O  OG  . SER A  1 83  ? 36.589  1.669   -4.621  1.00 15.92 ? 83  SER A OG  1 
ATOM   673  N  N   . ARG A  1 84  ? 38.608  -0.701  -1.604  1.00 13.27 ? 84  ARG A N   1 
ATOM   674  C  CA  . ARG A  1 84  ? 38.773  -1.160  -0.256  1.00 12.78 ? 84  ARG A CA  1 
ATOM   675  C  C   . ARG A  1 84  ? 37.836  -0.291  0.603   1.00 11.67 ? 84  ARG A C   1 
ATOM   676  O  O   . ARG A  1 84  ? 37.800  0.930   0.458   1.00 12.34 ? 84  ARG A O   1 
ATOM   677  C  CB  . ARG A  1 84  ? 40.219  -0.862  0.177   1.00 13.16 ? 84  ARG A CB  1 
ATOM   678  C  CG  . ARG A  1 84  ? 40.403  -1.187  1.666   1.00 14.97 ? 84  ARG A CG  1 
ATOM   679  C  CD  . ARG A  1 84  ? 41.838  -0.942  2.248   1.00 13.75 ? 84  ARG A CD  1 
ATOM   680  N  NE  . ARG A  1 84  ? 42.682  -2.031  1.780   1.00 15.95 ? 84  ARG A NE  1 
ATOM   681  C  CZ  . ARG A  1 84  ? 43.968  -2.165  2.076   1.00 15.79 ? 84  ARG A CZ  1 
ATOM   682  N  NH1 . ARG A  1 84  ? 44.557  -1.277  2.850   1.00 18.31 ? 84  ARG A NH1 1 
ATOM   683  N  NH2 . ARG A  1 84  ? 44.664  -3.192  1.604   1.00 18.07 ? 84  ARG A NH2 1 
ATOM   684  N  N   . TYR A  1 85  ? 37.060  -0.977  1.514   1.00 11.13 ? 85  TYR A N   1 
ATOM   685  C  CA  . TYR A  1 85  ? 36.286  -0.206  2.479   1.00 10.79 ? 85  TYR A CA  1 
ATOM   686  C  C   . TYR A  1 85  ? 36.838  -0.453  3.865   1.00 10.84 ? 85  TYR A C   1 
ATOM   687  O  O   . TYR A  1 85  ? 36.899  -1.630  4.337   1.00 12.24 ? 85  TYR A O   1 
ATOM   688  C  CB  . TYR A  1 85  ? 34.792  -0.689  2.402   1.00 11.62 ? 85  TYR A CB  1 
ATOM   689  C  CG  . TYR A  1 85  ? 34.093  -0.192  1.196   1.00 9.62  ? 85  TYR A CG  1 
ATOM   690  C  CD1 . TYR A  1 85  ? 33.232  0.913   1.313   1.00 10.22 ? 85  TYR A CD1 1 
ATOM   691  C  CD2 . TYR A  1 85  ? 34.258  -0.811  -0.021  1.00 10.76 ? 85  TYR A CD2 1 
ATOM   692  C  CE1 . TYR A  1 85  ? 32.554  1.408   0.161   1.00 10.25 ? 85  TYR A CE1 1 
ATOM   693  C  CE2 . TYR A  1 85  ? 33.654  -0.312  -1.153  1.00 11.82 ? 85  TYR A CE2 1 
ATOM   694  C  CZ  . TYR A  1 85  ? 32.779  0.789   -1.048  1.00 10.77 ? 85  TYR A CZ  1 
ATOM   695  O  OH  . TYR A  1 85  ? 32.105  1.376   -2.150  1.00 16.28 ? 85  TYR A OH  1 
ATOM   696  N  N   . SER A  1 86  ? 37.198  0.601   4.543   1.00 10.31 ? 86  SER A N   1 
ATOM   697  C  CA  . SER A  1 86  ? 37.887  0.531   5.866   1.00 11.52 ? 86  SER A CA  1 
ATOM   698  C  C   . SER A  1 86  ? 36.867  0.749   6.953   1.00 12.72 ? 86  SER A C   1 
ATOM   699  O  O   . SER A  1 86  ? 35.932  1.530   6.823   1.00 11.90 ? 86  SER A O   1 
ATOM   700  C  CB  . SER A  1 86  ? 38.923  1.676   5.948   1.00 12.94 ? 86  SER A CB  1 
ATOM   701  O  OG  . SER A  1 86  ? 39.964  1.305   5.031   1.00 15.62 ? 86  SER A OG  1 
ATOM   702  N  N   . ALA A  1 87  ? 37.051  0.013   8.069   1.00 12.07 ? 87  ALA A N   1 
ATOM   703  C  CA  . ALA A  1 87  ? 36.095  0.116   9.167   1.00 12.10 ? 87  ALA A CA  1 
ATOM   704  C  C   . ALA A  1 87  ? 36.145  1.456   9.881   1.00 12.66 ? 87  ALA A C   1 
ATOM   705  O  O   . ALA A  1 87  ? 37.236  2.102   9.977   1.00 14.92 ? 87  ALA A O   1 
ATOM   706  C  CB  . ALA A  1 87  ? 36.310  -0.988  10.149  1.00 12.92 ? 87  ALA A CB  1 
ATOM   707  N  N   . THR A  1 88  ? 35.018  1.925   10.387  1.00 11.41 ? 88  THR A N   1 
ATOM   708  C  CA  . THR A  1 88  ? 34.972  3.067   11.290  1.00 11.88 ? 88  THR A CA  1 
ATOM   709  C  C   . THR A  1 88  ? 34.369  2.773   12.647  1.00 11.60 ? 88  THR A C   1 
ATOM   710  O  O   . THR A  1 88  ? 34.849  3.278   13.646  1.00 12.47 ? 88  THR A O   1 
ATOM   711  C  CB  . THR A  1 88  ? 34.322  4.238   10.589  1.00 15.01 ? 88  THR A CB  1 
ATOM   712  O  OG1 . THR A  1 88  ? 34.422  5.442   11.313  1.00 21.19 ? 88  THR A OG1 1 
ATOM   713  C  CG2 . THR A  1 88  ? 32.863  3.955   10.331  1.00 14.34 ? 88  THR A CG2 1 
ATOM   714  N  N   . GLN A  1 89  ? 33.306  1.968   12.762  1.00 11.02 ? 89  GLN A N   1 
ATOM   715  C  CA  . GLN A  1 89  ? 32.633  1.736   14.007  1.00 11.07 ? 89  GLN A CA  1 
ATOM   716  C  C   . GLN A  1 89  ? 31.652  0.597   13.804  1.00 10.98 ? 89  GLN A C   1 
ATOM   717  O  O   . GLN A  1 89  ? 31.271  0.282   12.635  1.00 11.30 ? 89  GLN A O   1 
ATOM   718  C  CB  . GLN A  1 89  ? 31.908  2.897   14.594  1.00 11.98 ? 89  GLN A CB  1 
ATOM   719  C  CG  . GLN A  1 89  ? 30.979  3.691   13.678  1.00 14.54 ? 89  GLN A CG  1 
ATOM   720  C  CD  . GLN A  1 89  ? 29.492  3.360   13.892  1.00 14.31 ? 89  GLN A CD  1 
ATOM   721  O  OE1 . GLN A  1 89  ? 29.133  2.276   14.290  1.00 13.64 ? 89  GLN A OE1 1 
ATOM   722  N  NE2 . GLN A  1 89  ? 28.657  4.275   13.493  1.00 21.88 ? 89  GLN A NE2 1 
ATOM   723  N  N   . LEU A  1 90  ? 31.331  -0.087  14.898  1.00 10.20 ? 90  LEU A N   1 
ATOM   724  C  CA  . LEU A  1 90  ? 30.183  -0.997  14.943  1.00 10.14 ? 90  LEU A CA  1 
ATOM   725  C  C   . LEU A  1 90  ? 29.227  -0.577  15.983  1.00 9.96  ? 90  LEU A C   1 
ATOM   726  O  O   . LEU A  1 90  ? 29.534  0.097   16.928  1.00 10.89 ? 90  LEU A O   1 
ATOM   727  C  CB  . LEU A  1 90  ? 30.651  -2.489  14.997  1.00 11.39 ? 90  LEU A CB  1 
ATOM   728  C  CG  . LEU A  1 90  ? 31.413  -2.893  16.270  1.00 11.90 ? 90  LEU A CG  1 
ATOM   729  C  CD1 . LEU A  1 90  ? 30.498  -2.956  17.508  1.00 12.78 ? 90  LEU A CD1 1 
ATOM   730  C  CD2 . LEU A  1 90  ? 32.014  -4.248  15.914  1.00 12.38 ? 90  LEU A CD2 1 
ATOM   731  N  N   . HIS A  1 91  ? 27.938  -0.992  15.798  1.00 10.10 ? 91  HIS A N   1 
ATOM   732  C  CA  . HIS A  1 91  ? 26.885  -0.642  16.772  1.00 9.66  ? 91  HIS A CA  1 
ATOM   733  C  C   . HIS A  1 91  ? 25.711  -1.616  16.582  1.00 9.08  ? 91  HIS A C   1 
ATOM   734  O  O   . HIS A  1 91  ? 25.737  -2.442  15.686  1.00 9.32  ? 91  HIS A O   1 
ATOM   735  C  CB  . HIS A  1 91  ? 26.457  0.824   16.596  1.00 9.65  ? 91  HIS A CB  1 
ATOM   736  C  CG  . HIS A  1 91  ? 25.821  1.064   15.245  1.00 9.54  ? 91  HIS A CG  1 
ATOM   737  N  ND1 . HIS A  1 91  ? 26.552  1.413   14.199  1.00 9.90  ? 91  HIS A ND1 1 
ATOM   738  C  CD2 . HIS A  1 91  ? 24.533  0.760   14.800  1.00 9.92  ? 91  HIS A CD2 1 
ATOM   739  C  CE1 . HIS A  1 91  ? 25.781  1.431   13.067  1.00 9.37  ? 91  HIS A CE1 1 
ATOM   740  N  NE2 . HIS A  1 91  ? 24.503  1.036   13.434  1.00 8.12  ? 91  HIS A NE2 1 
ATOM   741  N  N   . LEU A  1 92  ? 24.716  -1.502  17.484  1.00 9.82  ? 92  LEU A N   1 
ATOM   742  C  CA  . LEU A  1 92  ? 23.616  -2.399  17.436  1.00 8.39  ? 92  LEU A CA  1 
ATOM   743  C  C   . LEU A  1 92  ? 22.261  -1.710  17.482  1.00 7.88  ? 92  LEU A C   1 
ATOM   744  O  O   . LEU A  1 92  ? 22.113  -0.548  17.797  1.00 9.30  ? 92  LEU A O   1 
ATOM   745  C  CB  . LEU A  1 92  ? 23.654  -3.367  18.653  1.00 12.00 ? 92  LEU A CB  1 
ATOM   746  C  CG  . LEU A  1 92  ? 24.907  -4.251  18.650  1.00 12.42 ? 92  LEU A CG  1 
ATOM   747  C  CD1 . LEU A  1 92  ? 25.909  -3.718  19.650  1.00 17.32 ? 92  LEU A CD1 1 
ATOM   748  C  CD2 . LEU A  1 92  ? 24.483  -5.683  18.909  1.00 15.40 ? 92  LEU A CD2 1 
ATOM   749  N  N   . HIS A  1 93  ? 21.234  -2.496  17.115  1.00 7.87  ? 93  HIS A N   1 
ATOM   750  C  CA  . HIS A  1 93  ? 19.803  -2.033  17.169  1.00 8.30  ? 93  HIS A CA  1 
ATOM   751  C  C   . HIS A  1 93  ? 19.019  -3.155  17.800  1.00 9.02  ? 93  HIS A C   1 
ATOM   752  O  O   . HIS A  1 93  ? 19.297  -4.345  17.545  1.00 9.74  ? 93  HIS A O   1 
ATOM   753  C  CB  . HIS A  1 93  ? 19.272  -1.834  15.705  1.00 8.37  ? 93  HIS A CB  1 
ATOM   754  C  CG  . HIS A  1 93  ? 20.035  -0.810  14.950  1.00 7.88  ? 93  HIS A CG  1 
ATOM   755  N  ND1 . HIS A  1 93  ? 19.713  0.509   14.905  1.00 8.89  ? 93  HIS A ND1 1 
ATOM   756  C  CD2 . HIS A  1 93  ? 21.136  -0.965  14.122  1.00 6.97  ? 93  HIS A CD2 1 
ATOM   757  C  CE1 . HIS A  1 93  ? 20.644  1.198   14.160  1.00 8.03  ? 93  HIS A CE1 1 
ATOM   758  N  NE2 . HIS A  1 93  ? 21.458  0.297   13.607  1.00 8.51  ? 93  HIS A NE2 1 
ATOM   759  N  N   . TRP A  1 94  ? 18.053  -2.812  18.653  1.00 9.76  ? 94  TRP A N   1 
ATOM   760  C  CA  . TRP A  1 94  ? 17.274  -3.816  19.380  1.00 9.46  ? 94  TRP A CA  1 
ATOM   761  C  C   . TRP A  1 94  ? 15.889  -3.267  19.736  1.00 10.19 ? 94  TRP A C   1 
ATOM   762  O  O   . TRP A  1 94  ? 15.591  -2.089  19.531  1.00 9.34  ? 94  TRP A O   1 
ATOM   763  C  CB  . TRP A  1 94  ? 18.022  -4.234  20.687  1.00 9.80  ? 94  TRP A CB  1 
ATOM   764  C  CG  . TRP A  1 94  ? 18.352  -3.110  21.594  1.00 9.65  ? 94  TRP A CG  1 
ATOM   765  C  CD1 . TRP A  1 94  ? 17.535  -2.558  22.622  1.00 10.44 ? 94  TRP A CD1 1 
ATOM   766  C  CD2 . TRP A  1 94  ? 19.551  -2.257  21.575  1.00 10.16 ? 94  TRP A CD2 1 
ATOM   767  N  NE1 . TRP A  1 94  ? 18.144  -1.472  23.237  1.00 11.39 ? 94  TRP A NE1 1 
ATOM   768  C  CE2 . TRP A  1 94  ? 19.416  -1.294  22.674  1.00 12.35 ? 94  TRP A CE2 1 
ATOM   769  C  CE3 . TRP A  1 94  ? 20.721  -2.264  20.851  1.00 10.02 ? 94  TRP A CE3 1 
ATOM   770  C  CZ2 . TRP A  1 94  ? 20.402  -0.349  22.975  1.00 11.37 ? 94  TRP A CZ2 1 
ATOM   771  C  CZ3 . TRP A  1 94  ? 21.703  -1.301  21.093  1.00 10.32 ? 94  TRP A CZ3 1 
ATOM   772  C  CH2 . TRP A  1 94  ? 21.571  -0.352  22.135  1.00 10.91 ? 94  TRP A CH2 1 
ATOM   773  N  N   . GLY A  1 95  ? 15.113  -4.200  20.337  1.00 10.55 ? 95  GLY A N   1 
ATOM   774  C  CA  . GLY A  1 95  ? 13.684  -3.904  20.716  1.00 10.57 ? 95  GLY A CA  1 
ATOM   775  C  C   . GLY A  1 95  ? 13.572  -3.524  22.197  1.00 9.22  ? 95  GLY A C   1 
ATOM   776  O  O   . GLY A  1 95  ? 14.253  -2.685  22.734  1.00 10.16 ? 95  GLY A O   1 
ATOM   777  N  N   . ASN A  1 96  ? 12.742  -4.336  22.862  1.00 11.54 ? 96  ASN A N   1 
ATOM   778  C  CA  . ASN A  1 96  ? 12.558  -4.116  24.335  1.00 10.99 ? 96  ASN A CA  1 
ATOM   779  C  C   . ASN A  1 96  ? 12.054  -5.438  24.909  1.00 13.21 ? 96  ASN A C   1 
ATOM   780  O  O   . ASN A  1 96  ? 11.618  -6.323  24.192  1.00 11.55 ? 96  ASN A O   1 
ATOM   781  C  CB  . ASN A  1 96  ? 11.584  -2.980  24.540  1.00 13.95 ? 96  ASN A CB  1 
ATOM   782  C  CG  . ASN A  1 96  ? 10.133  -3.347  24.255  1.00 16.44 ? 96  ASN A CG  1 
ATOM   783  O  OD1 . ASN A  1 96  ? 9.456   -3.916  25.131  1.00 19.36 ? 96  ASN A OD1 1 
ATOM   784  N  ND2 . ASN A  1 96  ? 9.614   -3.016  23.087  1.00 17.25 ? 96  ASN A ND2 1 
ATOM   785  N  N   . PRO A  1 97  ? 12.105  -5.579  26.276  1.00 13.18 ? 97  PRO A N   1 
ATOM   786  C  CA  . PRO A  1 97  ? 11.795  -6.902  26.826  1.00 13.85 ? 97  PRO A CA  1 
ATOM   787  C  C   . PRO A  1 97  ? 10.339  -7.350  26.606  1.00 14.21 ? 97  PRO A C   1 
ATOM   788  O  O   . PRO A  1 97  ? 10.105  -8.539  26.560  1.00 15.31 ? 97  PRO A O   1 
ATOM   789  C  CB  . PRO A  1 97  ? 12.093  -6.717  28.320  1.00 16.23 ? 97  PRO A CB  1 
ATOM   790  C  CG  . PRO A  1 97  ? 13.165  -5.653  28.325  1.00 16.87 ? 97  PRO A CG  1 
ATOM   791  C  CD  . PRO A  1 97  ? 12.661  -4.666  27.326  1.00 14.95 ? 97  PRO A CD  1 
ATOM   792  N  N   . ASN A  1 98  ? 9.424   -6.413  26.434  1.00 13.14 ? 98  ASN A N   1 
ATOM   793  C  CA  . ASN A  1 98  ? 8.030   -6.847  26.107  1.00 17.14 ? 98  ASN A CA  1 
ATOM   794  C  C   . ASN A  1 98  ? 7.799   -7.238  24.670  1.00 16.34 ? 98  ASN A C   1 
ATOM   795  O  O   . ASN A  1 98  ? 6.788   -7.849  24.300  1.00 18.72 ? 98  ASN A O   1 
ATOM   796  C  CB  . ASN A  1 98  ? 7.088   -5.693  26.428  1.00 17.62 ? 98  ASN A CB  1 
ATOM   797  C  CG  . ASN A  1 98  ? 7.003   -5.411  27.924  1.00 26.83 ? 98  ASN A CG  1 
ATOM   798  O  OD1 . ASN A  1 98  ? 7.074   -6.328  28.756  1.00 32.62 ? 98  ASN A OD1 1 
ATOM   799  N  ND2 . ASN A  1 98  ? 6.813   -4.140  28.267  1.00 28.84 ? 98  ASN A ND2 1 
ATOM   800  N  N   . ASP A  1 99  ? 8.737   -6.867  23.789  1.00 13.69 ? 99  ASP A N   1 
ATOM   801  C  CA  . ASP A  1 99  ? 8.620   -7.137  22.353  1.00 12.69 ? 99  ASP A CA  1 
ATOM   802  C  C   . ASP A  1 99  ? 10.043  -7.249  21.764  1.00 11.85 ? 99  ASP A C   1 
ATOM   803  O  O   . ASP A  1 99  ? 10.504  -6.334  21.094  1.00 12.78 ? 99  ASP A O   1 
ATOM   804  C  CB  . ASP A  1 99  ? 7.788   -6.032  21.611  1.00 14.24 ? 99  ASP A CB  1 
ATOM   805  C  CG  . ASP A  1 99  ? 7.272   -6.487  20.259  1.00 17.55 ? 99  ASP A CG  1 
ATOM   806  O  OD1 . ASP A  1 99  ? 7.594   -7.616  19.838  1.00 18.11 ? 99  ASP A OD1 1 
ATOM   807  O  OD2 . ASP A  1 99  ? 6.538   -5.705  19.617  1.00 23.42 ? 99  ASP A OD2 1 
ATOM   808  N  N   . PRO A  1 100 ? 10.710  -8.347  22.053  1.00 12.23 ? 100 PRO A N   1 
ATOM   809  C  CA  . PRO A  1 100 ? 12.170  -8.449  21.864  1.00 12.14 ? 100 PRO A CA  1 
ATOM   810  C  C   . PRO A  1 100 ? 12.506  -8.820  20.456  1.00 12.85 ? 100 PRO A C   1 
ATOM   811  O  O   . PRO A  1 100 ? 13.171  -9.798  20.172  1.00 13.13 ? 100 PRO A O   1 
ATOM   812  C  CB  . PRO A  1 100 ? 12.586  -9.569  22.817  1.00 13.20 ? 100 PRO A CB  1 
ATOM   813  C  CG  . PRO A  1 100 ? 11.357  -10.453 22.916  1.00 14.32 ? 100 PRO A CG  1 
ATOM   814  C  CD  . PRO A  1 100 ? 10.152  -9.523  22.820  1.00 13.16 ? 100 PRO A CD  1 
ATOM   815  N  N   . HIS A  1 101 ? 12.058  -7.941  19.548  1.00 12.91 ? 101 HIS A N   1 
ATOM   816  C  CA  . HIS A  1 101 ? 12.229  -8.207  18.067  1.00 13.26 ? 101 HIS A CA  1 
ATOM   817  C  C   . HIS A  1 101 ? 12.557  -6.936  17.372  1.00 13.43 ? 101 HIS A C   1 
ATOM   818  O  O   . HIS A  1 101 ? 11.698  -6.409  16.624  1.00 17.20 ? 101 HIS A O   1 
ATOM   819  C  CB  . HIS A  1 101 ? 10.938  -8.788  17.434  1.00 14.53 ? 101 HIS A CB  1 
ATOM   820  C  CG  . HIS A  1 101 ? 10.376  -9.910  18.239  1.00 14.89 ? 101 HIS A CG  1 
ATOM   821  N  ND1 . HIS A  1 101 ? 10.899  -11.158 18.224  1.00 16.85 ? 101 HIS A ND1 1 
ATOM   822  C  CD2 . HIS A  1 101 ? 9.350   -9.899  19.160  1.00 14.96 ? 101 HIS A CD2 1 
ATOM   823  C  CE1 . HIS A  1 101 ? 10.198  -11.932 19.135  1.00 16.59 ? 101 HIS A CE1 1 
ATOM   824  N  NE2 . HIS A  1 101 ? 9.285   -11.130 19.715  1.00 15.79 ? 101 HIS A NE2 1 
ATOM   825  N  N   . GLY A  1 102 ? 13.793  -6.491  17.528  1.00 10.50 ? 102 GLY A N   1 
ATOM   826  C  CA  . GLY A  1 102 ? 14.199  -5.175  17.105  1.00 10.41 ? 102 GLY A CA  1 
ATOM   827  C  C   . GLY A  1 102 ? 15.327  -5.130  16.074  1.00 9.87  ? 102 GLY A C   1 
ATOM   828  O  O   . GLY A  1 102 ? 16.035  -4.103  16.044  1.00 10.31 ? 102 GLY A O   1 
ATOM   829  N  N   . SER A  1 103 ? 15.467  -6.185  15.257  1.00 8.81  ? 103 SER A N   1 
ATOM   830  C  CA  . SER A  1 103 ? 16.285  -5.974  14.050  1.00 8.95  ? 103 SER A CA  1 
ATOM   831  C  C   . SER A  1 103 ? 15.744  -4.873  13.191  1.00 9.41  ? 103 SER A C   1 
ATOM   832  O  O   . SER A  1 103 ? 14.539  -4.525  13.242  1.00 11.47 ? 103 SER A O   1 
ATOM   833  C  CB  . SER A  1 103 ? 16.457  -7.270  13.295  1.00 9.06  ? 103 SER A CB  1 
ATOM   834  O  OG  . SER A  1 103 ? 15.230  -7.689  12.644  1.00 9.21  ? 103 SER A OG  1 
ATOM   835  N  N   . GLU A  1 104 ? 16.593  -4.389  12.301  1.00 9.01  ? 104 GLU A N   1 
ATOM   836  C  CA  . GLU A  1 104 ? 16.135  -3.407  11.320  1.00 8.06  ? 104 GLU A CA  1 
ATOM   837  C  C   . GLU A  1 104 ? 15.671  -4.076  10.039  1.00 8.22  ? 104 GLU A C   1 
ATOM   838  O  O   . GLU A  1 104 ? 14.522  -3.894  9.600   1.00 8.51  ? 104 GLU A O   1 
ATOM   839  C  CB  . GLU A  1 104 ? 17.306  -2.412  10.969  1.00 8.76  ? 104 GLU A CB  1 
ATOM   840  C  CG  . GLU A  1 104 ? 17.832  -1.724  12.238  1.00 8.51  ? 104 GLU A CG  1 
ATOM   841  C  CD  . GLU A  1 104 ? 18.209  -0.306  11.917  1.00 9.42  ? 104 GLU A CD  1 
ATOM   842  O  OE1 . GLU A  1 104 ? 19.294  -0.071  11.336  1.00 10.28 ? 104 GLU A OE1 1 
ATOM   843  O  OE2 . GLU A  1 104 ? 17.363  0.577   12.163  1.00 10.39 ? 104 GLU A OE2 1 
ATOM   844  N  N   . HIS A  1 105 ? 16.533  -4.839  9.396   1.00 7.99  ? 105 HIS A N   1 
ATOM   845  C  CA  . HIS A  1 105 ? 16.049  -5.697  8.304   1.00 8.25  ? 105 HIS A CA  1 
ATOM   846  C  C   . HIS A  1 105 ? 15.143  -6.802  8.847   1.00 8.74  ? 105 HIS A C   1 
ATOM   847  O  O   . HIS A  1 105 ? 15.297  -7.304  9.954   1.00 9.24  ? 105 HIS A O   1 
ATOM   848  C  CB  . HIS A  1 105 ? 17.269  -6.315  7.543   1.00 7.84  ? 105 HIS A CB  1 
ATOM   849  C  CG  . HIS A  1 105 ? 18.006  -5.254  6.807   1.00 8.40  ? 105 HIS A CG  1 
ATOM   850  N  ND1 . HIS A  1 105 ? 19.086  -4.538  7.381   1.00 7.96  ? 105 HIS A ND1 1 
ATOM   851  C  CD2 . HIS A  1 105 ? 17.785  -4.733  5.581   1.00 8.54  ? 105 HIS A CD2 1 
ATOM   852  C  CE1 . HIS A  1 105 ? 19.502  -3.622  6.472   1.00 8.58  ? 105 HIS A CE1 1 
ATOM   853  N  NE2 . HIS A  1 105 ? 18.757  -3.753  5.373   1.00 9.68  ? 105 HIS A NE2 1 
ATOM   854  N  N   . THR A  1 106 ? 14.197  -7.177  8.000   1.00 7.98  ? 106 THR A N   1 
ATOM   855  C  CA  . THR A  1 106 ? 13.338  -8.337  8.300   1.00 9.14  ? 106 THR A CA  1 
ATOM   856  C  C   . THR A  1 106 ? 13.498  -9.349  7.208   1.00 9.09  ? 106 THR A C   1 
ATOM   857  O  O   . THR A  1 106 ? 13.928  -9.053  6.075   1.00 9.36  ? 106 THR A O   1 
ATOM   858  C  CB  . THR A  1 106 ? 11.865  -7.908  8.496   1.00 9.11  ? 106 THR A CB  1 
ATOM   859  O  OG1 . THR A  1 106 ? 11.414  -7.304  7.248   1.00 10.40 ? 106 THR A OG1 1 
ATOM   860  C  CG2 . THR A  1 106 ? 11.703  -6.990  9.589   1.00 11.07 ? 106 THR A CG2 1 
ATOM   861  N  N   . VAL A  1 107 ? 13.144  -10.600 7.522   1.00 10.97 ? 107 VAL A N   1 
ATOM   862  C  CA  . VAL A  1 107 ? 13.220  -11.715 6.517   1.00 10.40 ? 107 VAL A CA  1 
ATOM   863  C  C   . VAL A  1 107 ? 11.840  -12.367 6.406   1.00 10.10 ? 107 VAL A C   1 
ATOM   864  O  O   . VAL A  1 107 ? 11.316  -12.820 7.407   1.00 10.92 ? 107 VAL A O   1 
ATOM   865  C  CB  . VAL A  1 107 ? 14.314  -12.768 6.832   1.00 10.61 ? 107 VAL A CB  1 
ATOM   866  C  CG1 . VAL A  1 107 ? 14.288  -13.896 5.791   1.00 12.48 ? 107 VAL A CG1 1 
ATOM   867  C  CG2 . VAL A  1 107 ? 15.763  -12.138 6.904   1.00 11.47 ? 107 VAL A CG2 1 
ATOM   868  N  N   . SER A  1 108 ? 11.247  -12.259 5.216   1.00 11.09 ? 108 SER A N   1 
ATOM   869  C  CA  . SER A  1 108 ? 9.848   -12.785 4.986   1.00 12.41 ? 108 SER A CA  1 
ATOM   870  C  C   . SER A  1 108 ? 8.946   -12.201 6.047   1.00 13.18 ? 108 SER A C   1 
ATOM   871  O  O   . SER A  1 108 ? 8.065   -12.882 6.612   1.00 13.42 ? 108 SER A O   1 
ATOM   872  C  CB  . SER A  1 108 ? 9.888   -14.319 5.046   1.00 14.28 ? 108 SER A CB  1 
ATOM   873  O  OG  . SER A  1 108 ? 10.711  -14.803 3.971   1.00 19.45 ? 108 SER A OG  1 
ATOM   874  N  N   . GLY A  1 109 ? 9.121   -10.908 6.377   1.00 11.19 ? 109 GLY A N   1 
ATOM   875  C  CA  . GLY A  1 109 ? 8.278   -10.118 7.240   1.00 11.99 ? 109 GLY A CA  1 
ATOM   876  C  C   . GLY A  1 109 ? 8.659   -10.225 8.709   1.00 14.59 ? 109 GLY A C   1 
ATOM   877  O  O   . GLY A  1 109 ? 8.054   -9.542  9.500   1.00 16.88 ? 109 GLY A O   1 
ATOM   878  N  N   . GLN A  1 110 ? 9.569   -11.108 9.086   1.00 12.48 ? 110 GLN A N   1 
ATOM   879  C  CA  . GLN A  1 110 ? 9.945   -11.300 10.466  1.00 12.63 ? 110 GLN A CA  1 
ATOM   880  C  C   . GLN A  1 110 ? 11.175  -10.567 10.980  1.00 11.20 ? 110 GLN A C   1 
ATOM   881  O  O   . GLN A  1 110 ? 12.210  -10.610 10.321  1.00 10.85 ? 110 GLN A O   1 
ATOM   882  C  CB  . GLN A  1 110 ? 10.239  -12.803 10.670  1.00 14.20 ? 110 GLN A CB  1 
ATOM   883  C  CG  . GLN A  1 110 ? 9.112   -13.757 10.127  1.00 14.91 ? 110 GLN A CG  1 
ATOM   884  C  CD  . GLN A  1 110 ? 7.698   -13.285 10.542  1.00 16.22 ? 110 GLN A CD  1 
ATOM   885  O  OE1 . GLN A  1 110 ? 6.856   -12.997 9.641   1.00 23.79 ? 110 GLN A OE1 1 
ATOM   886  N  NE2 . GLN A  1 110 ? 7.434   -13.170 11.765  1.00 18.50 ? 110 GLN A NE2 1 
ATOM   887  N  N   . HIS A  1 111 ? 11.008  -9.934  12.124  1.00 12.26 ? 111 HIS A N   1 
ATOM   888  C  CA  . HIS A  1 111 ? 12.125  -9.346  12.776  1.00 11.16 ? 111 HIS A CA  1 
ATOM   889  C  C   . HIS A  1 111 ? 12.920  -10.354 13.514  1.00 13.84 ? 111 HIS A C   1 
ATOM   890  O  O   . HIS A  1 111 ? 12.346  -11.283 14.085  1.00 17.26 ? 111 HIS A O   1 
ATOM   891  C  CB  . HIS A  1 111 ? 11.710  -8.355  13.840  1.00 14.36 ? 111 HIS A CB  1 
ATOM   892  C  CG  . HIS A  1 111 ? 11.338  -6.996  13.305  1.00 12.98 ? 111 HIS A CG  1 
ATOM   893  N  ND1 . HIS A  1 111 ? 10.106  -6.682  12.784  1.00 16.58 ? 111 HIS A ND1 1 
ATOM   894  C  CD2 . HIS A  1 111 ? 12.119  -5.874  13.164  1.00 12.53 ? 111 HIS A CD2 1 
ATOM   895  C  CE1 . HIS A  1 111 ? 10.063  -5.383  12.420  1.00 16.24 ? 111 HIS A CE1 1 
ATOM   896  N  NE2 . HIS A  1 111 ? 11.329  -4.891  12.611  1.00 17.67 ? 111 HIS A NE2 1 
ATOM   897  N  N   . PHE A  1 112 ? 14.223  -10.240 13.488  1.00 10.64 ? 112 PHE A N   1 
ATOM   898  C  CA  . PHE A  1 112 ? 15.089  -10.913 14.477  1.00 11.25 ? 112 PHE A CA  1 
ATOM   899  C  C   . PHE A  1 112 ? 15.158  -10.137 15.774  1.00 11.12 ? 112 PHE A C   1 
ATOM   900  O  O   . PHE A  1 112 ? 14.650  -8.966  15.895  1.00 10.93 ? 112 PHE A O   1 
ATOM   901  C  CB  . PHE A  1 112 ? 16.495  -11.143 13.822  1.00 11.42 ? 112 PHE A CB  1 
ATOM   902  C  CG  . PHE A  1 112 ? 16.461  -12.247 12.811  1.00 13.26 ? 112 PHE A CG  1 
ATOM   903  C  CD1 . PHE A  1 112 ? 16.915  -13.548 13.100  1.00 13.47 ? 112 PHE A CD1 1 
ATOM   904  C  CD2 . PHE A  1 112 ? 15.861  -11.959 11.545  1.00 14.38 ? 112 PHE A CD2 1 
ATOM   905  C  CE1 . PHE A  1 112 ? 16.848  -14.557 12.125  1.00 14.74 ? 112 PHE A CE1 1 
ATOM   906  C  CE2 . PHE A  1 112 ? 15.754  -12.997 10.593  1.00 19.00 ? 112 PHE A CE2 1 
ATOM   907  C  CZ  . PHE A  1 112 ? 16.236  -14.253 10.925  1.00 17.43 ? 112 PHE A CZ  1 
ATOM   908  N  N   . ALA A  1 113 ? 15.831  -10.670 16.783  1.00 9.48  ? 113 ALA A N   1 
ATOM   909  C  CA  . ALA A  1 113 ? 15.854  -10.029 18.075  1.00 9.83  ? 113 ALA A CA  1 
ATOM   910  C  C   . ALA A  1 113 ? 16.587  -8.694  18.020  1.00 9.94  ? 113 ALA A C   1 
ATOM   911  O  O   . ALA A  1 113 ? 16.219  -7.713  18.740  1.00 9.92  ? 113 ALA A O   1 
ATOM   912  C  CB  . ALA A  1 113 ? 16.519  -10.935 19.147  1.00 10.85 ? 113 ALA A CB  1 
ATOM   913  N  N   . ALA A  1 114 ? 17.722  -8.699  17.292  1.00 8.85  ? 114 ALA A N   1 
ATOM   914  C  CA  . ALA A  1 114 ? 18.554  -7.472  17.267  1.00 9.04  ? 114 ALA A CA  1 
ATOM   915  C  C   . ALA A  1 114 ? 19.374  -7.566  15.998  1.00 8.40  ? 114 ALA A C   1 
ATOM   916  O  O   . ALA A  1 114 ? 19.311  -8.571  15.220  1.00 9.29  ? 114 ALA A O   1 
ATOM   917  C  CB  . ALA A  1 114 ? 19.471  -7.494  18.529  1.00 10.62 ? 114 ALA A CB  1 
ATOM   918  N  N   . GLU A  1 115 ? 20.171  -6.513  15.764  1.00 8.73  ? 115 GLU A N   1 
ATOM   919  C  CA  . GLU A  1 115 ? 20.989  -6.503  14.558  1.00 8.84  ? 115 GLU A CA  1 
ATOM   920  C  C   . GLU A  1 115 ? 22.278  -5.732  14.845  1.00 9.36  ? 115 GLU A C   1 
ATOM   921  O  O   . GLU A  1 115 ? 22.242  -4.634  15.494  1.00 9.61  ? 115 GLU A O   1 
ATOM   922  C  CB  . GLU A  1 115 ? 20.180  -5.843  13.402  1.00 8.91  ? 115 GLU A CB  1 
ATOM   923  C  CG  . GLU A  1 115 ? 20.865  -5.879  12.027  1.00 8.96  ? 115 GLU A CG  1 
ATOM   924  C  CD  . GLU A  1 115 ? 19.915  -5.477  10.925  1.00 9.60  ? 115 GLU A CD  1 
ATOM   925  O  OE1 . GLU A  1 115 ? 18.712  -5.798  11.007  1.00 9.02  ? 115 GLU A OE1 1 
ATOM   926  O  OE2 . GLU A  1 115 ? 20.391  -4.954  9.887   1.00 8.67  ? 115 GLU A OE2 1 
ATOM   927  N  N   . LEU A  1 116 ? 23.420  -6.260  14.396  1.00 8.19  ? 116 LEU A N   1 
ATOM   928  C  CA  . LEU A  1 116 ? 24.754  -5.597  14.521  1.00 8.92  ? 116 LEU A CA  1 
ATOM   929  C  C   . LEU A  1 116 ? 25.108  -5.033  13.135  1.00 8.12  ? 116 LEU A C   1 
ATOM   930  O  O   . LEU A  1 116 ? 24.926  -5.718  12.107  1.00 8.06  ? 116 LEU A O   1 
ATOM   931  C  CB  . LEU A  1 116 ? 25.782  -6.692  14.974  1.00 10.50 ? 116 LEU A CB  1 
ATOM   932  C  CG  . LEU A  1 116 ? 27.303  -6.209  14.751  1.00 10.92 ? 116 LEU A CG  1 
ATOM   933  C  CD1 . LEU A  1 116 ? 27.611  -5.301  15.875  1.00 14.11 ? 116 LEU A CD1 1 
ATOM   934  C  CD2 . LEU A  1 116 ? 28.239  -7.451  14.709  1.00 13.82 ? 116 LEU A CD2 1 
ATOM   935  N  N   . HIS A  1 117 ? 25.623  -3.801  13.140  1.00 7.79  ? 117 HIS A N   1 
ATOM   936  C  CA  . HIS A  1 117 ? 26.149  -3.143  11.926  1.00 8.35  ? 117 HIS A CA  1 
ATOM   937  C  C   . HIS A  1 117 ? 27.601  -2.841  12.094  1.00 8.38  ? 117 HIS A C   1 
ATOM   938  O  O   . HIS A  1 117 ? 27.976  -2.188  13.080  1.00 8.99  ? 117 HIS A O   1 
ATOM   939  C  CB  . HIS A  1 117 ? 25.399  -1.853  11.700  1.00 8.24  ? 117 HIS A CB  1 
ATOM   940  C  CG  . HIS A  1 117 ? 23.967  -2.106  11.272  1.00 7.48  ? 117 HIS A CG  1 
ATOM   941  N  ND1 . HIS A  1 117 ? 22.974  -1.174  11.417  1.00 8.65  ? 117 HIS A ND1 1 
ATOM   942  C  CD2 . HIS A  1 117 ? 23.415  -3.198  10.720  1.00 7.87  ? 117 HIS A CD2 1 
ATOM   943  C  CE1 . HIS A  1 117 ? 21.842  -1.688  10.898  1.00 7.60  ? 117 HIS A CE1 1 
ATOM   944  N  NE2 . HIS A  1 117 ? 22.068  -2.925  10.511  1.00 7.36  ? 117 HIS A NE2 1 
ATOM   945  N  N   . ILE A  1 118 ? 28.393  -3.268  11.114  1.00 9.71  ? 118 ILE A N   1 
ATOM   946  C  CA  . ILE A  1 118 ? 29.850  -2.916  11.094  1.00 8.31  ? 118 ILE A CA  1 
ATOM   947  C  C   . ILE A  1 118 ? 29.995  -1.955  9.906   1.00 8.03  ? 118 ILE A C   1 
ATOM   948  O  O   . ILE A  1 118 ? 29.825  -2.333  8.677   1.00 8.87  ? 118 ILE A O   1 
ATOM   949  C  CB  . ILE A  1 118 ? 30.732  -4.161  10.954  1.00 9.94  ? 118 ILE A CB  1 
ATOM   950  C  CG1 . ILE A  1 118 ? 30.370  -5.232  11.973  1.00 10.50 ? 118 ILE A CG1 1 
ATOM   951  C  CG2 . ILE A  1 118 ? 32.236  -3.697  11.177  1.00 10.66 ? 118 ILE A CG2 1 
ATOM   952  C  CD1 . ILE A  1 118 ? 31.237  -6.454  11.821  1.00 11.58 ? 118 ILE A CD1 1 
ATOM   953  N  N   . VAL A  1 119 ? 30.234  -0.701  10.246  1.00 9.00  ? 119 VAL A N   1 
ATOM   954  C  CA  . VAL A  1 119 ? 30.233  0.424   9.276   1.00 9.54  ? 119 VAL A CA  1 
ATOM   955  C  C   . VAL A  1 119 ? 31.606  0.549   8.646   1.00 10.36 ? 119 VAL A C   1 
ATOM   956  O  O   . VAL A  1 119 ? 32.586  0.694   9.409   1.00 10.53 ? 119 VAL A O   1 
ATOM   957  C  CB  . VAL A  1 119 ? 29.777  1.709   9.931   1.00 9.55  ? 119 VAL A CB  1 
ATOM   958  C  CG1 . VAL A  1 119 ? 29.658  2.787   8.847   1.00 11.31 ? 119 VAL A CG1 1 
ATOM   959  C  CG2 . VAL A  1 119 ? 28.416  1.505   10.655  1.00 10.79 ? 119 VAL A CG2 1 
ATOM   960  N  N   . HIS A  1 120 ? 31.660  0.661   7.335   1.00 9.29  ? 120 HIS A N   1 
ATOM   961  C  CA  . HIS A  1 120 ? 32.999  0.898   6.596   1.00 9.14  ? 120 HIS A CA  1 
ATOM   962  C  C   . HIS A  1 120 ? 32.789  2.029   5.590   1.00 11.01 ? 120 HIS A C   1 
ATOM   963  O  O   . HIS A  1 120 ? 31.655  2.350   5.143   1.00 10.68 ? 120 HIS A O   1 
ATOM   964  C  CB  . HIS A  1 120 ? 33.435  -0.325  5.803   1.00 10.81 ? 120 HIS A CB  1 
ATOM   965  C  CG  . HIS A  1 120 ? 33.563  -1.583  6.609   1.00 10.92 ? 120 HIS A CG  1 
ATOM   966  N  ND1 . HIS A  1 120 ? 32.473  -2.257  7.180   1.00 10.05 ? 120 HIS A ND1 1 
ATOM   967  C  CD2 . HIS A  1 120 ? 34.693  -2.353  6.930   1.00 11.21 ? 120 HIS A CD2 1 
ATOM   968  C  CE1 . HIS A  1 120 ? 32.920  -3.433  7.766   1.00 11.24 ? 120 HIS A CE1 1 
ATOM   969  N  NE2 . HIS A  1 120 ? 34.289  -3.511  7.618   1.00 11.25 ? 120 HIS A NE2 1 
ATOM   970  N  N   . TYR A  1 121 ? 33.877  2.687   5.230   1.00 11.57 ? 121 TYR A N   1 
ATOM   971  C  CA  . TYR A  1 121 ? 33.830  3.677   4.185   1.00 10.80 ? 121 TYR A CA  1 
ATOM   972  C  C   . TYR A  1 121 ? 34.859  3.458   3.072   1.00 12.43 ? 121 TYR A C   1 
ATOM   973  O  O   . TYR A  1 121 ? 35.900  2.742   3.348   1.00 10.64 ? 121 TYR A O   1 
ATOM   974  C  CB  . TYR A  1 121 ? 34.040  5.144   4.774   1.00 12.51 ? 121 TYR A CB  1 
ATOM   975  C  CG  . TYR A  1 121 ? 35.478  5.398   5.315   1.00 14.29 ? 121 TYR A CG  1 
ATOM   976  C  CD1 . TYR A  1 121 ? 36.375  6.143   4.565   1.00 17.09 ? 121 TYR A CD1 1 
ATOM   977  C  CD2 . TYR A  1 121 ? 35.916  4.841   6.491   1.00 15.62 ? 121 TYR A CD2 1 
ATOM   978  C  CE1 . TYR A  1 121 ? 37.743  6.246   5.031   1.00 18.20 ? 121 TYR A CE1 1 
ATOM   979  C  CE2 . TYR A  1 121 ? 37.230  4.984   6.984   1.00 18.55 ? 121 TYR A CE2 1 
ATOM   980  C  CZ  . TYR A  1 121 ? 38.118  5.695   6.225   1.00 21.41 ? 121 TYR A CZ  1 
ATOM   981  O  OH  . TYR A  1 121 ? 39.465  5.825   6.711   1.00 23.15 ? 121 TYR A OH  1 
ATOM   982  N  N   . ASN A  1 122 ? 34.642  4.084   1.891   1.00 10.88 ? 122 ASN A N   1 
ATOM   983  C  CA  . ASN A  1 122 ? 35.555  3.828   0.754   1.00 11.82 ? 122 ASN A CA  1 
ATOM   984  C  C   . ASN A  1 122 ? 36.804  4.697   0.974   1.00 12.53 ? 122 ASN A C   1 
ATOM   985  O  O   . ASN A  1 122 ? 36.819  5.885   0.712   1.00 12.00 ? 122 ASN A O   1 
ATOM   986  C  CB  . ASN A  1 122 ? 34.860  4.263   -0.510  1.00 11.36 ? 122 ASN A CB  1 
ATOM   987  C  CG  . ASN A  1 122 ? 35.601  3.883   -1.727  1.00 12.35 ? 122 ASN A CG  1 
ATOM   988  O  OD1 . ASN A  1 122 ? 36.869  3.833   -1.724  1.00 13.04 ? 122 ASN A OD1 1 
ATOM   989  N  ND2 . ASN A  1 122 ? 34.858  3.480   -2.794  1.00 14.95 ? 122 ASN A ND2 1 
ATOM   990  N  N   . SER A  1 123 ? 37.866  4.034   1.468   1.00 11.29 ? 123 SER A N   1 
ATOM   991  C  CA  . SER A  1 123 ? 39.083  4.780   1.801   1.00 12.11 ? 123 SER A CA  1 
ATOM   992  C  C   . SER A  1 123 ? 39.959  4.877   0.552   1.00 13.37 ? 123 SER A C   1 
ATOM   993  O  O   . SER A  1 123 ? 40.978  5.635   0.654   1.00 15.42 ? 123 SER A O   1 
ATOM   994  C  CB  . SER A  1 123 ? 39.761  4.009   2.947   1.00 13.16 ? 123 SER A CB  1 
ATOM   995  O  OG  . SER A  1 123 ? 39.908  2.628   2.661   1.00 13.34 ? 123 SER A OG  1 
ATOM   996  N  N   . ASP A  1 124 ? 39.691  4.135   -0.512  1.00 12.92 ? 124 ASP A N   1 
ATOM   997  C  CA  . ASP A  1 124 ? 40.449  4.380   -1.777  1.00 13.80 ? 124 ASP A CA  1 
ATOM   998  C  C   . ASP A  1 124 ? 40.045  5.730   -2.333  1.00 16.91 ? 124 ASP A C   1 
ATOM   999  O  O   . ASP A  1 124 ? 40.888  6.433   -2.949  1.00 18.08 ? 124 ASP A O   1 
ATOM   1000 C  CB  . ASP A  1 124 ? 40.135  3.279   -2.761  1.00 14.79 ? 124 ASP A CB  1 
ATOM   1001 C  CG  . ASP A  1 124 ? 40.737  2.015   -2.416  1.00 13.76 ? 124 ASP A CG  1 
ATOM   1002 O  OD1 . ASP A  1 124 ? 41.780  2.009   -1.712  1.00 15.69 ? 124 ASP A OD1 1 
ATOM   1003 O  OD2 . ASP A  1 124 ? 40.349  0.980   -2.940  1.00 13.68 ? 124 ASP A OD2 1 
ATOM   1004 N  N   . LEU A  1 125 ? 38.800  6.172   -2.144  1.00 12.96 ? 125 LEU A N   1 
ATOM   1005 C  CA  . LEU A  1 125 ? 38.290  7.423   -2.798  1.00 16.68 ? 125 LEU A CA  1 
ATOM   1006 C  C   . LEU A  1 125 ? 38.253  8.600   -1.837  1.00 16.81 ? 125 LEU A C   1 
ATOM   1007 O  O   . LEU A  1 125 ? 38.364  9.785   -2.307  1.00 19.66 ? 125 LEU A O   1 
ATOM   1008 C  CB  . LEU A  1 125 ? 36.880  7.196   -3.427  1.00 15.87 ? 125 LEU A CB  1 
ATOM   1009 C  CG  . LEU A  1 125 ? 36.908  6.105   -4.512  1.00 19.80 ? 125 LEU A CG  1 
ATOM   1010 C  CD1 . LEU A  1 125 ? 35.519  6.103   -5.127  1.00 21.15 ? 125 LEU A CD1 1 
ATOM   1011 C  CD2 . LEU A  1 125 ? 38.026  6.365   -5.581  1.00 22.97 ? 125 LEU A CD2 1 
ATOM   1012 N  N   . TYR A  1 126 ? 38.082  8.350   -0.526  1.00 15.97 ? 126 TYR A N   1 
ATOM   1013 C  CA  . TYR A  1 126 ? 37.777  9.404   0.462   1.00 15.99 ? 126 TYR A CA  1 
ATOM   1014 C  C   . TYR A  1 126 ? 38.656  9.267   1.733   1.00 19.80 ? 126 TYR A C   1 
ATOM   1015 O  O   . TYR A  1 126 ? 39.103  8.157   2.097   1.00 19.03 ? 126 TYR A O   1 
ATOM   1016 C  CB  . TYR A  1 126 ? 36.264  9.290   0.884   1.00 16.29 ? 126 TYR A CB  1 
ATOM   1017 C  CG  . TYR A  1 126 ? 35.382  9.295   -0.319  1.00 16.72 ? 126 TYR A CG  1 
ATOM   1018 C  CD1 . TYR A  1 126 ? 35.342  10.404  -1.198  1.00 20.28 ? 126 TYR A CD1 1 
ATOM   1019 C  CD2 . TYR A  1 126 ? 34.605  8.146   -0.633  1.00 18.48 ? 126 TYR A CD2 1 
ATOM   1020 C  CE1 . TYR A  1 126 ? 34.576  10.361  -2.325  1.00 19.64 ? 126 TYR A CE1 1 
ATOM   1021 C  CE2 . TYR A  1 126 ? 33.824  8.090   -1.788  1.00 17.79 ? 126 TYR A CE2 1 
ATOM   1022 C  CZ  . TYR A  1 126 ? 33.812  9.223   -2.623  1.00 19.68 ? 126 TYR A CZ  1 
ATOM   1023 O  OH  . TYR A  1 126 ? 33.035  9.115   -3.782  1.00 22.78 ? 126 TYR A OH  1 
ATOM   1024 N  N   . PRO A  1 127 ? 38.927  10.397  2.431   1.00 20.09 ? 127 PRO A N   1 
ATOM   1025 C  CA  . PRO A  1 127 ? 39.891  10.368  3.519   1.00 23.51 ? 127 PRO A CA  1 
ATOM   1026 C  C   . PRO A  1 127 ? 39.367  9.912   4.851   1.00 24.39 ? 127 PRO A C   1 
ATOM   1027 O  O   . PRO A  1 127 ? 40.137  9.411   5.687   1.00 28.89 ? 127 PRO A O   1 
ATOM   1028 C  CB  . PRO A  1 127 ? 40.303  11.838  3.643   1.00 26.74 ? 127 PRO A CB  1 
ATOM   1029 C  CG  . PRO A  1 127 ? 39.055  12.594  3.220   1.00 22.86 ? 127 PRO A CG  1 
ATOM   1030 C  CD  . PRO A  1 127 ? 38.533  11.769  2.079   1.00 20.85 ? 127 PRO A CD  1 
ATOM   1031 N  N   . ASP A  1 128 ? 38.044  9.998   5.046   1.00 24.19 ? 128 ASP A N   1 
ATOM   1032 C  CA  . ASP A  1 128 ? 37.423  9.530   6.290   1.00 24.48 ? 128 ASP A CA  1 
ATOM   1033 C  C   . ASP A  1 128 ? 35.935  9.248   6.040   1.00 20.07 ? 128 ASP A C   1 
ATOM   1034 O  O   . ASP A  1 128 ? 35.433  9.604   4.982   1.00 20.52 ? 128 ASP A O   1 
ATOM   1035 C  CB  . ASP A  1 128 ? 37.583  10.587  7.391   1.00 30.23 ? 128 ASP A CB  1 
ATOM   1036 C  CG  . ASP A  1 128 ? 37.261  11.965  6.887   1.00 32.76 ? 128 ASP A CG  1 
ATOM   1037 O  OD1 . ASP A  1 128 ? 38.128  12.880  6.977   1.00 42.09 ? 128 ASP A OD1 1 
ATOM   1038 O  OD2 . ASP A  1 128 ? 36.149  12.159  6.363   1.00 32.96 ? 128 ASP A OD2 1 
ATOM   1039 N  N   . ALA A  1 129 ? 35.289  8.588   6.986   1.00 23.69 ? 129 ALA A N   1 
ATOM   1040 C  CA  . ALA A  1 129 ? 33.897  8.216   6.843   1.00 22.28 ? 129 ALA A CA  1 
ATOM   1041 C  C   . ALA A  1 129 ? 32.931  9.417   6.700   1.00 25.13 ? 129 ALA A C   1 
ATOM   1042 O  O   . ALA A  1 129 ? 31.983  9.353   5.931   1.00 22.22 ? 129 ALA A O   1 
ATOM   1043 C  CB  . ALA A  1 129 ? 33.447  7.311   7.995   1.00 25.49 ? 129 ALA A CB  1 
ATOM   1044 N  N   A SER A  1 130 ? 33.211  10.473  7.458   0.50 24.52 ? 130 SER A N   1 
ATOM   1045 N  N   B SER A  1 130 ? 33.140  10.499  7.448   0.50 24.76 ? 130 SER A N   1 
ATOM   1046 C  CA  A SER A  1 130 ? 32.427  11.695  7.370   0.50 26.32 ? 130 SER A CA  1 
ATOM   1047 C  CA  B SER A  1 130 ? 32.230  11.653  7.282   0.50 26.19 ? 130 SER A CA  1 
ATOM   1048 C  C   A SER A  1 130 ? 32.331  12.216  5.933   0.50 26.47 ? 130 SER A C   1 
ATOM   1049 C  C   B SER A  1 130 ? 32.287  12.247  5.843   0.50 25.63 ? 130 SER A C   1 
ATOM   1050 O  O   A SER A  1 130 ? 31.250  12.473  5.418   0.50 25.07 ? 130 SER A O   1 
ATOM   1051 O  O   B SER A  1 130 ? 31.274  12.539  5.196   0.50 21.23 ? 130 SER A O   1 
ATOM   1052 C  CB  A SER A  1 130 ? 33.017  12.774  8.279   0.50 26.22 ? 130 SER A CB  1 
ATOM   1053 C  CB  B SER A  1 130 ? 32.387  12.708  8.414   0.50 27.05 ? 130 SER A CB  1 
ATOM   1054 O  OG  A SER A  1 130 ? 32.233  13.944  8.186   0.50 26.26 ? 130 SER A OG  1 
ATOM   1055 O  OG  B SER A  1 130 ? 33.730  12.909  8.832   0.50 26.74 ? 130 SER A OG  1 
ATOM   1056 N  N   . THR A  1 131 ? 33.480  12.390  5.292   1.00 23.90 ? 131 THR A N   1 
ATOM   1057 C  CA  . THR A  1 131 ? 33.551  12.845  3.933   1.00 24.71 ? 131 THR A CA  1 
ATOM   1058 C  C   . THR A  1 131 ? 32.885  11.845  2.967   1.00 22.12 ? 131 THR A C   1 
ATOM   1059 O  O   . THR A  1 131 ? 32.230  12.238  2.041   1.00 20.66 ? 131 THR A O   1 
ATOM   1060 C  CB  . THR A  1 131 ? 35.019  13.106  3.461   1.00 26.70 ? 131 THR A CB  1 
ATOM   1061 O  OG1 . THR A  1 131 ? 35.654  13.986  4.404   1.00 31.23 ? 131 THR A OG1 1 
ATOM   1062 C  CG2 . THR A  1 131 ? 35.113  13.617  2.032   1.00 26.53 ? 131 THR A CG2 1 
ATOM   1063 N  N   . ALA A  1 132 ? 33.125  10.514  3.131   1.00 20.08 ? 132 ALA A N   1 
ATOM   1064 C  CA  . ALA A  1 132 ? 32.538  9.522   2.247   1.00 17.39 ? 132 ALA A CA  1 
ATOM   1065 C  C   . ALA A  1 132 ? 30.990  9.425   2.337   1.00 17.26 ? 132 ALA A C   1 
ATOM   1066 O  O   . ALA A  1 132 ? 30.418  9.047   1.390   1.00 15.47 ? 132 ALA A O   1 
ATOM   1067 C  CB  . ALA A  1 132 ? 33.079  8.133   2.609   1.00 14.63 ? 132 ALA A CB  1 
ATOM   1068 N  N   . SER A  1 133 ? 30.460  9.806   3.478   1.00 17.52 ? 133 SER A N   1 
ATOM   1069 C  CA  . SER A  1 133 ? 29.094  9.479   3.839   1.00 20.05 ? 133 SER A CA  1 
ATOM   1070 C  C   . SER A  1 133 ? 28.076  10.011  2.898   1.00 19.76 ? 133 SER A C   1 
ATOM   1071 O  O   . SER A  1 133 ? 27.020  9.404   2.784   1.00 21.37 ? 133 SER A O   1 
ATOM   1072 C  CB  . SER A  1 133 ? 28.828  9.927   5.292   1.00 22.90 ? 133 SER A CB  1 
ATOM   1073 O  OG  . SER A  1 133 ? 28.721  11.342  5.426   1.00 27.13 ? 133 SER A OG  1 
ATOM   1074 N  N   . ASN A  1 134 ? 28.302  11.167  2.277   1.00 18.50 ? 134 ASN A N   1 
ATOM   1075 C  CA  . ASN A  1 134 ? 27.377  11.740  1.316   1.00 19.43 ? 134 ASN A CA  1 
ATOM   1076 C  C   . ASN A  1 134 ? 27.839  11.640  -0.109  1.00 19.97 ? 134 ASN A C   1 
ATOM   1077 O  O   . ASN A  1 134 ? 27.371  12.305  -1.023  1.00 24.29 ? 134 ASN A O   1 
ATOM   1078 C  CB  . ASN A  1 134 ? 26.947  13.195  1.755   1.00 22.57 ? 134 ASN A CB  1 
ATOM   1079 C  CG  . ASN A  1 134 ? 28.079  14.173  1.544   1.00 29.55 ? 134 ASN A CG  1 
ATOM   1080 O  OD1 . ASN A  1 134 ? 29.230  13.735  1.441   1.00 32.13 ? 134 ASN A OD1 1 
ATOM   1081 N  ND2 . ASN A  1 134 ? 27.798  15.489  1.546   1.00 28.99 ? 134 ASN A ND2 1 
ATOM   1082 N  N   . LYS A  1 135 ? 28.742  10.698  -0.365  1.00 18.01 ? 135 LYS A N   1 
ATOM   1083 C  CA  . LYS A  1 135 ? 29.321  10.562  -1.628  1.00 19.02 ? 135 LYS A CA  1 
ATOM   1084 C  C   . LYS A  1 135 ? 29.059  9.276   -2.284  1.00 21.04 ? 135 LYS A C   1 
ATOM   1085 O  O   . LYS A  1 135 ? 28.765  8.260   -1.624  1.00 17.85 ? 135 LYS A O   1 
ATOM   1086 C  CB  . LYS A  1 135 ? 30.871  10.881  -1.505  1.00 21.80 ? 135 LYS A CB  1 
ATOM   1087 C  CG  . LYS A  1 135 ? 31.031  12.377  -1.105  1.00 26.04 ? 135 LYS A CG  1 
ATOM   1088 C  CD  . LYS A  1 135 ? 32.402  12.974  -1.336  1.00 28.28 ? 135 LYS A CD  1 
ATOM   1089 C  CE  . LYS A  1 135 ? 32.521  14.342  -0.702  1.00 29.89 ? 135 LYS A CE  1 
ATOM   1090 N  NZ  . LYS A  1 135 ? 31.768  14.481  0.565   1.00 27.99 ? 135 LYS A NZ  1 
ATOM   1091 N  N   . SER A  1 136 ? 29.148  9.296   -3.594  1.00 23.36 ? 136 SER A N   1 
ATOM   1092 C  CA  . SER A  1 136 ? 28.956  8.125   -4.427  1.00 26.87 ? 136 SER A CA  1 
ATOM   1093 C  C   . SER A  1 136 ? 29.905  7.001   -3.978  1.00 20.85 ? 136 SER A C   1 
ATOM   1094 O  O   . SER A  1 136 ? 31.108  7.189   -3.766  1.00 21.79 ? 136 SER A O   1 
ATOM   1095 C  CB  . SER A  1 136 ? 29.276  8.515   -5.892  1.00 30.00 ? 136 SER A CB  1 
ATOM   1096 O  OG  . SER A  1 136 ? 29.784  7.440   -6.725  1.00 41.24 ? 136 SER A OG  1 
ATOM   1097 N  N   . GLU A  1 137 ? 29.326  5.807   -3.877  1.00 21.03 ? 137 GLU A N   1 
ATOM   1098 C  CA  . GLU A  1 137 ? 30.122  4.633   -3.431  1.00 20.37 ? 137 GLU A CA  1 
ATOM   1099 C  C   . GLU A  1 137 ? 30.763  4.828   -2.027  1.00 17.81 ? 137 GLU A C   1 
ATOM   1100 O  O   . GLU A  1 137 ? 31.848  4.281   -1.681  1.00 18.05 ? 137 GLU A O   1 
ATOM   1101 C  CB  . GLU A  1 137 ? 31.186  4.213   -4.460  1.00 29.60 ? 137 GLU A CB  1 
ATOM   1102 C  CG  . GLU A  1 137 ? 30.530  3.933   -5.824  1.00 37.12 ? 137 GLU A CG  1 
ATOM   1103 N  N   . GLY A  1 138 ? 30.100  5.610   -1.157  1.00 13.93 ? 138 GLY A N   1 
ATOM   1104 C  CA  . GLY A  1 138 ? 30.841  6.056   -0.073  1.00 14.29 ? 138 GLY A CA  1 
ATOM   1105 C  C   . GLY A  1 138 ? 30.939  5.015   1.032   1.00 11.63 ? 138 GLY A C   1 
ATOM   1106 O  O   . GLY A  1 138 ? 31.980  5.011   1.718   1.00 11.70 ? 138 GLY A O   1 
ATOM   1107 N  N   . LEU A  1 139 ? 29.840  4.276   1.378   1.00 10.86 ? 139 LEU A N   1 
ATOM   1108 C  CA  . LEU A  1 139 ? 29.819  3.502   2.585   1.00 10.55 ? 139 LEU A CA  1 
ATOM   1109 C  C   . LEU A  1 139 ? 29.482  2.042   2.256   1.00 9.91  ? 139 LEU A C   1 
ATOM   1110 O  O   . LEU A  1 139 ? 28.794  1.751   1.252   1.00 10.58 ? 139 LEU A O   1 
ATOM   1111 C  CB  . LEU A  1 139 ? 28.773  4.043   3.577   1.00 10.88 ? 139 LEU A CB  1 
ATOM   1112 C  CG  . LEU A  1 139 ? 28.957  5.533   3.935   1.00 12.00 ? 139 LEU A CG  1 
ATOM   1113 C  CD1 . LEU A  1 139 ? 27.739  5.956   4.803   1.00 13.20 ? 139 LEU A CD1 1 
ATOM   1114 C  CD2 . LEU A  1 139 ? 30.308  5.656   4.714   1.00 13.80 ? 139 LEU A CD2 1 
ATOM   1115 N  N   . ALA A  1 140 ? 29.929  1.135   3.132   1.00 9.84  ? 140 ALA A N   1 
ATOM   1116 C  CA  . ALA A  1 140 ? 29.527  -0.266  3.091   1.00 9.34  ? 140 ALA A CA  1 
ATOM   1117 C  C   . ALA A  1 140 ? 29.278  -0.696  4.494   1.00 9.71  ? 140 ALA A C   1 
ATOM   1118 O  O   . ALA A  1 140 ? 30.117  -0.564  5.367   1.00 10.95 ? 140 ALA A O   1 
ATOM   1119 C  CB  . ALA A  1 140 ? 30.587  -1.114  2.402   1.00 10.68 ? 140 ALA A CB  1 
ATOM   1120 N  N   . VAL A  1 141 ? 28.131  -1.295  4.727   1.00 9.32  ? 141 VAL A N   1 
ATOM   1121 C  CA  . VAL A  1 141 ? 27.755  -1.778  6.092   1.00 9.38  ? 141 VAL A CA  1 
ATOM   1122 C  C   . VAL A  1 141 ? 27.535  -3.273  6.014   1.00 9.02  ? 141 VAL A C   1 
ATOM   1123 O  O   . VAL A  1 141 ? 26.904  -3.808  5.058   1.00 10.28 ? 141 VAL A O   1 
ATOM   1124 C  CB  . VAL A  1 141 ? 26.521  -1.049  6.638   1.00 8.60  ? 141 VAL A CB  1 
ATOM   1125 C  CG1 . VAL A  1 141 ? 26.228  -1.559  8.083   1.00 10.04 ? 141 VAL A CG1 1 
ATOM   1126 C  CG2 . VAL A  1 141 ? 26.799  0.455   6.675   1.00 10.38 ? 141 VAL A CG2 1 
ATOM   1127 N  N   . LEU A  1 142 ? 28.131  -3.982  6.993   1.00 9.05  ? 142 LEU A N   1 
ATOM   1128 C  CA  . LEU A  1 142 ? 27.837  -5.406  7.188   1.00 8.02  ? 142 LEU A CA  1 
ATOM   1129 C  C   . LEU A  1 142 ? 26.784  -5.507  8.258   1.00 8.38  ? 142 LEU A C   1 
ATOM   1130 O  O   . LEU A  1 142 ? 26.949  -4.895  9.328   1.00 9.55  ? 142 LEU A O   1 
ATOM   1131 C  CB  . LEU A  1 142 ? 29.098  -6.208  7.664   1.00 9.16  ? 142 LEU A CB  1 
ATOM   1132 C  CG  . LEU A  1 142 ? 30.256  -6.095  6.716   1.00 10.56 ? 142 LEU A CG  1 
ATOM   1133 C  CD1 . LEU A  1 142 ? 31.401  -6.931  7.425   1.00 12.39 ? 142 LEU A CD1 1 
ATOM   1134 C  CD2 . LEU A  1 142 ? 30.022  -6.558  5.300   1.00 11.08 ? 142 LEU A CD2 1 
ATOM   1135 N  N   . ALA A  1 143 ? 25.757  -6.343  7.967   1.00 8.03  ? 143 ALA A N   1 
ATOM   1136 C  CA  . ALA A  1 143 ? 24.678  -6.544  8.989   1.00 7.61  ? 143 ALA A CA  1 
ATOM   1137 C  C   . ALA A  1 143 ? 24.580  -8.013  9.364   1.00 8.17  ? 143 ALA A C   1 
ATOM   1138 O  O   . ALA A  1 143 ? 24.560  -8.897  8.515   1.00 9.41  ? 143 ALA A O   1 
ATOM   1139 C  CB  . ALA A  1 143 ? 23.334  -6.085  8.433   1.00 9.52  ? 143 ALA A CB  1 
ATOM   1140 N  N   . VAL A  1 144 ? 24.576  -8.193  10.717  1.00 7.54  ? 144 VAL A N   1 
ATOM   1141 C  CA  . VAL A  1 144 ? 24.403  -9.547  11.259  1.00 8.99  ? 144 VAL A CA  1 
ATOM   1142 C  C   . VAL A  1 144 ? 23.078  -9.581  12.036  1.00 8.70  ? 144 VAL A C   1 
ATOM   1143 O  O   . VAL A  1 144 ? 22.839  -8.736  12.958  1.00 9.76  ? 144 VAL A O   1 
ATOM   1144 C  CB  . VAL A  1 144 ? 25.560  -9.828  12.292  1.00 10.55 ? 144 VAL A CB  1 
ATOM   1145 C  CG1 . VAL A  1 144 ? 25.369  -11.299 12.846  1.00 11.65 ? 144 VAL A CG1 1 
ATOM   1146 C  CG2 . VAL A  1 144 ? 26.927  -9.727  11.598  1.00 11.18 ? 144 VAL A CG2 1 
ATOM   1147 N  N   . LEU A  1 145 ? 22.247  -10.503 11.637  1.00 9.80  ? 145 LEU A N   1 
ATOM   1148 C  CA  . LEU A  1 145 ? 20.966  -10.709 12.368  1.00 9.28  ? 145 LEU A CA  1 
ATOM   1149 C  C   . LEU A  1 145 ? 21.237  -11.501 13.634  1.00 10.06 ? 145 LEU A C   1 
ATOM   1150 O  O   . LEU A  1 145 ? 22.012  -12.489 13.611  1.00 10.74 ? 145 LEU A O   1 
ATOM   1151 C  CB  . LEU A  1 145 ? 19.979  -11.404 11.428  1.00 10.31 ? 145 LEU A CB  1 
ATOM   1152 C  CG  . LEU A  1 145 ? 19.690  -10.617 10.128  1.00 11.57 ? 145 LEU A CG  1 
ATOM   1153 C  CD1 . LEU A  1 145 ? 19.037  -11.555 9.135   1.00 13.57 ? 145 LEU A CD1 1 
ATOM   1154 C  CD2 . LEU A  1 145 ? 18.801  -9.386  10.457  1.00 13.56 ? 145 LEU A CD2 1 
ATOM   1155 N  N   . ILE A  1 146 ? 20.573  -11.106 14.723  1.00 9.19  ? 146 ILE A N   1 
ATOM   1156 C  CA  . ILE A  1 146 ? 20.802  -11.788 16.033  1.00 10.38 ? 146 ILE A CA  1 
ATOM   1157 C  C   . ILE A  1 146 ? 19.559  -12.423 16.545  1.00 10.18 ? 146 ILE A C   1 
ATOM   1158 O  O   . ILE A  1 146 ? 18.518  -11.733 16.558  1.00 10.24 ? 146 ILE A O   1 
ATOM   1159 C  CB  . ILE A  1 146 ? 21.294  -10.727 17.009  1.00 10.18 ? 146 ILE A CB  1 
ATOM   1160 C  CG1 . ILE A  1 146 ? 22.669  -10.132 16.552  1.00 11.59 ? 146 ILE A CG1 1 
ATOM   1161 C  CG2 . ILE A  1 146 ? 21.582  -11.322 18.438  1.00 12.40 ? 146 ILE A CG2 1 
ATOM   1162 C  CD1 . ILE A  1 146 ? 23.083  -8.902  17.366  1.00 11.89 ? 146 ILE A CD1 1 
ATOM   1163 N  N   . GLU A  1 147 ? 19.613  -13.693 16.970  1.00 11.74 ? 147 GLU A N   1 
ATOM   1164 C  CA  . GLU A  1 147 ? 18.412  -14.324 17.598  1.00 13.26 ? 147 GLU A CA  1 
ATOM   1165 C  C   . GLU A  1 147 ? 18.839  -14.878 18.926  1.00 14.24 ? 147 GLU A C   1 
ATOM   1166 O  O   . GLU A  1 147 ? 20.019  -14.972 19.260  1.00 14.82 ? 147 GLU A O   1 
ATOM   1167 C  CB  . GLU A  1 147 ? 17.837  -15.441 16.738  1.00 17.30 ? 147 GLU A CB  1 
ATOM   1168 C  CG  . GLU A  1 147 ? 18.809  -16.569 16.550  1.00 15.60 ? 147 GLU A CG  1 
ATOM   1169 C  CD  . GLU A  1 147 ? 18.401  -17.584 15.517  1.00 18.95 ? 147 GLU A CD  1 
ATOM   1170 O  OE1 . GLU A  1 147 ? 17.415  -17.369 14.784  1.00 19.88 ? 147 GLU A OE1 1 
ATOM   1171 O  OE2 . GLU A  1 147 ? 19.131  -18.612 15.371  1.00 23.56 ? 147 GLU A OE2 1 
ATOM   1172 N  N   . MET A  1 148 ? 17.858  -15.267 19.725  1.00 16.38 ? 148 MET A N   1 
ATOM   1173 C  CA  . MET A  1 148 ? 18.136  -15.815 21.057  1.00 18.51 ? 148 MET A CA  1 
ATOM   1174 C  C   . MET A  1 148 ? 18.499  -17.280 20.927  1.00 17.42 ? 148 MET A C   1 
ATOM   1175 O  O   . MET A  1 148 ? 17.925  -18.058 20.178  1.00 22.01 ? 148 MET A O   1 
ATOM   1176 C  CB  . MET A  1 148 ? 16.814  -15.657 21.812  1.00 20.74 ? 148 MET A CB  1 
ATOM   1177 C  CG  . MET A  1 148 ? 16.836  -14.530 22.741  1.00 25.34 ? 148 MET A CG  1 
ATOM   1178 S  SD  . MET A  1 148 ? 17.278  -15.133 24.400  1.00 52.56 ? 148 MET A SD  1 
ATOM   1179 C  CE  . MET A  1 148 ? 17.131  -16.908 24.122  1.00 14.99 ? 148 MET A CE  1 
ATOM   1180 N  N   . GLY A  1 149 ? 19.503  -17.709 21.698  1.00 16.45 ? 149 GLY A N   1 
ATOM   1181 C  CA  . GLY A  1 149 ? 19.872  -19.128 21.726  1.00 18.42 ? 149 GLY A CA  1 
ATOM   1182 C  C   . GLY A  1 149 ? 20.963  -19.290 22.772  1.00 17.79 ? 149 GLY A C   1 
ATOM   1183 O  O   . GLY A  1 149 ? 20.817  -18.809 23.897  1.00 17.69 ? 149 GLY A O   1 
ATOM   1184 N  N   A SER A  1 150 ? 22.069  -19.890 22.345  0.50 18.15 ? 150 SER A N   1 
ATOM   1185 N  N   B SER A  1 150 ? 22.029  -20.019 22.451  0.50 16.33 ? 150 SER A N   1 
ATOM   1186 C  CA  A SER A  1 150 ? 23.245  -19.974 23.170  0.50 17.47 ? 150 SER A CA  1 
ATOM   1187 C  CA  B SER A  1 150 ? 23.066  -20.209 23.456  0.50 16.13 ? 150 SER A CA  1 
ATOM   1188 C  C   A SER A  1 150 ? 23.948  -18.716 23.666  0.50 17.38 ? 150 SER A C   1 
ATOM   1189 C  C   B SER A  1 150 ? 23.909  -18.960 23.650  0.50 15.69 ? 150 SER A C   1 
ATOM   1190 O  O   A SER A  1 150 ? 24.078  -17.700 22.984  0.50 14.47 ? 150 SER A O   1 
ATOM   1191 O  O   B SER A  1 150 ? 24.024  -18.183 22.679  0.50 14.52 ? 150 SER A O   1 
ATOM   1192 C  CB  A SER A  1 150 ? 24.262  -20.882 22.473  0.50 22.28 ? 150 SER A CB  1 
ATOM   1193 C  CB  B SER A  1 150 ? 23.975  -21.346 22.990  0.50 16.52 ? 150 SER A CB  1 
ATOM   1194 O  OG  A SER A  1 150 ? 23.628  -22.118 22.231  0.50 23.87 ? 150 SER A OG  1 
ATOM   1195 O  OG  B SER A  1 150 ? 24.485  -20.961 21.697  0.50 17.15 ? 150 SER A OG  1 
ATOM   1196 N  N   . PHE A  1 151 ? 24.478  -18.780 24.865  1.00 15.43 ? 151 PHE A N   1 
ATOM   1197 C  CA  . PHE A  1 151 ? 25.438  -17.773 25.287  1.00 16.04 ? 151 PHE A CA  1 
ATOM   1198 C  C   . PHE A  1 151 ? 26.554  -17.614 24.261  1.00 16.65 ? 151 PHE A C   1 
ATOM   1199 O  O   . PHE A  1 151 ? 27.093  -18.616 23.726  1.00 19.39 ? 151 PHE A O   1 
ATOM   1200 C  CB  . PHE A  1 151 ? 26.017  -18.078 26.710  1.00 16.40 ? 151 PHE A CB  1 
ATOM   1201 C  CG  . PHE A  1 151 ? 26.960  -17.083 27.161  1.00 16.17 ? 151 PHE A CG  1 
ATOM   1202 C  CD1 . PHE A  1 151 ? 26.530  -15.857 27.682  1.00 17.40 ? 151 PHE A CD1 1 
ATOM   1203 C  CD2 . PHE A  1 151 ? 28.344  -17.329 27.082  1.00 17.94 ? 151 PHE A CD2 1 
ATOM   1204 C  CE1 . PHE A  1 151 ? 27.464  -14.932 28.079  1.00 17.52 ? 151 PHE A CE1 1 
ATOM   1205 C  CE2 . PHE A  1 151 ? 29.263  -16.377 27.508  1.00 17.40 ? 151 PHE A CE2 1 
ATOM   1206 C  CZ  . PHE A  1 151 ? 28.854  -15.194 28.025  1.00 17.73 ? 151 PHE A CZ  1 
ATOM   1207 N  N   . ASN A  1 152 ? 26.876  -16.363 23.921  1.00 14.46 ? 152 ASN A N   1 
ATOM   1208 C  CA  . ASN A  1 152 ? 27.927  -16.035 22.975  1.00 14.31 ? 152 ASN A CA  1 
ATOM   1209 C  C   . ASN A  1 152 ? 29.054  -15.313 23.634  1.00 15.71 ? 152 ASN A C   1 
ATOM   1210 O  O   . ASN A  1 152 ? 28.989  -14.143 23.940  1.00 16.59 ? 152 ASN A O   1 
ATOM   1211 C  CB  . ASN A  1 152 ? 27.232  -15.221 21.812  1.00 14.61 ? 152 ASN A CB  1 
ATOM   1212 C  CG  . ASN A  1 152 ? 28.151  -15.149 20.599  1.00 14.06 ? 152 ASN A CG  1 
ATOM   1213 O  OD1 . ASN A  1 152 ? 29.352  -14.736 20.742  1.00 15.87 ? 152 ASN A OD1 1 
ATOM   1214 N  ND2 . ASN A  1 152 ? 27.554  -15.344 19.418  1.00 13.86 ? 152 ASN A ND2 1 
ATOM   1215 N  N   . PRO A  1 153 ? 30.175  -16.046 23.878  1.00 16.68 ? 153 PRO A N   1 
ATOM   1216 C  CA  . PRO A  1 153 ? 31.282  -15.377 24.519  1.00 16.07 ? 153 PRO A CA  1 
ATOM   1217 C  C   . PRO A  1 153 ? 31.824  -14.136 23.769  1.00 16.58 ? 153 PRO A C   1 
ATOM   1218 O  O   . PRO A  1 153 ? 32.337  -13.149 24.394  1.00 18.31 ? 153 PRO A O   1 
ATOM   1219 C  CB  . PRO A  1 153 ? 32.327  -16.555 24.595  1.00 18.44 ? 153 PRO A CB  1 
ATOM   1220 C  CG  . PRO A  1 153 ? 31.449  -17.790 24.656  1.00 20.82 ? 153 PRO A CG  1 
ATOM   1221 C  CD  . PRO A  1 153 ? 30.305  -17.515 23.724  1.00 18.33 ? 153 PRO A CD  1 
ATOM   1222 N  N   . SER A  1 154 ? 31.745  -14.207 22.435  1.00 16.90 ? 154 SER A N   1 
ATOM   1223 C  CA  . SER A  1 154 ? 32.364  -13.117 21.685  1.00 15.78 ? 154 SER A CA  1 
ATOM   1224 C  C   . SER A  1 154 ? 31.552  -11.848 21.809  1.00 14.09 ? 154 SER A C   1 
ATOM   1225 O  O   . SER A  1 154 ? 32.123  -10.823 21.965  1.00 15.34 ? 154 SER A O   1 
ATOM   1226 C  CB  . SER A  1 154 ? 32.515  -13.495 20.250  1.00 18.31 ? 154 SER A CB  1 
ATOM   1227 O  OG  . SER A  1 154 ? 33.343  -14.710 20.128  1.00 21.35 ? 154 SER A OG  1 
ATOM   1228 N  N   . TYR A  1 155 ? 30.201  -12.007 21.736  1.00 13.22 ? 155 TYR A N   1 
ATOM   1229 C  CA  . TYR A  1 155 ? 29.375  -10.784 21.910  1.00 14.03 ? 155 TYR A CA  1 
ATOM   1230 C  C   . TYR A  1 155 ? 29.562  -10.244 23.328  1.00 15.86 ? 155 TYR A C   1 
ATOM   1231 O  O   . TYR A  1 155 ? 29.463  -9.022  23.527  1.00 15.71 ? 155 TYR A O   1 
ATOM   1232 C  CB  . TYR A  1 155 ? 27.899  -11.020 21.614  1.00 12.93 ? 155 TYR A CB  1 
ATOM   1233 C  CG  . TYR A  1 155 ? 27.648  -10.863 20.114  1.00 13.65 ? 155 TYR A CG  1 
ATOM   1234 C  CD1 . TYR A  1 155 ? 27.089  -9.696  19.600  1.00 13.95 ? 155 TYR A CD1 1 
ATOM   1235 C  CD2 . TYR A  1 155 ? 28.014  -11.856 19.210  1.00 13.07 ? 155 TYR A CD2 1 
ATOM   1236 C  CE1 . TYR A  1 155 ? 26.876  -9.538  18.245  1.00 12.06 ? 155 TYR A CE1 1 
ATOM   1237 C  CE2 . TYR A  1 155 ? 27.802  -11.702 17.842  1.00 12.28 ? 155 TYR A CE2 1 
ATOM   1238 C  CZ  . TYR A  1 155 ? 27.232  -10.538 17.367  1.00 11.71 ? 155 TYR A CZ  1 
ATOM   1239 O  OH  . TYR A  1 155 ? 27.008  -10.358 16.024  1.00 11.51 ? 155 TYR A OH  1 
ATOM   1240 N  N   . ASP A  1 156 ? 29.870  -11.163 24.275  1.00 16.84 ? 156 ASP A N   1 
ATOM   1241 C  CA  . ASP A  1 156 ? 30.102  -10.656 25.606  1.00 18.53 ? 156 ASP A CA  1 
ATOM   1242 C  C   . ASP A  1 156 ? 31.365  -9.851  25.792  1.00 18.13 ? 156 ASP A C   1 
ATOM   1243 O  O   . ASP A  1 156 ? 31.447  -9.085  26.771  1.00 18.36 ? 156 ASP A O   1 
ATOM   1244 C  CB  . ASP A  1 156 ? 30.029  -11.769 26.636  1.00 20.09 ? 156 ASP A CB  1 
ATOM   1245 C  CG  . ASP A  1 156 ? 29.037  -11.409 27.754  1.00 22.32 ? 156 ASP A CG  1 
ATOM   1246 O  OD1 . ASP A  1 156 ? 27.842  -10.956 27.449  1.00 19.63 ? 156 ASP A OD1 1 
ATOM   1247 O  OD2 . ASP A  1 156 ? 29.414  -11.590 28.943  1.00 26.70 ? 156 ASP A OD2 1 
ATOM   1248 N  N   . LYS A  1 157 ? 32.288  -9.915  24.826  1.00 16.46 ? 157 LYS A N   1 
ATOM   1249 C  CA  . LYS A  1 157 ? 33.467  -9.015  24.859  1.00 17.65 ? 157 LYS A CA  1 
ATOM   1250 C  C   . LYS A  1 157 ? 33.036  -7.563  24.696  1.00 17.89 ? 157 LYS A C   1 
ATOM   1251 O  O   . LYS A  1 157 ? 33.699  -6.651  25.195  1.00 18.72 ? 157 LYS A O   1 
ATOM   1252 C  CB  . LYS A  1 157 ? 34.559  -9.416  23.860  1.00 20.61 ? 157 LYS A CB  1 
ATOM   1253 C  CG  . LYS A  1 157 ? 35.113  -10.837 24.201  1.00 20.92 ? 157 LYS A CG  1 
ATOM   1254 C  CD  . LYS A  1 157 ? 35.966  -11.355 23.027  1.00 24.40 ? 157 LYS A CD  1 
ATOM   1255 C  CE  . LYS A  1 157 ? 36.406  -12.792 23.289  1.00 22.25 ? 157 LYS A CE  1 
ATOM   1256 N  NZ  . LYS A  1 157 ? 37.259  -13.321 22.198  1.00 26.16 ? 157 LYS A NZ  1 
ATOM   1257 N  N   . ILE A  1 158 ? 31.847  -7.331  24.112  1.00 18.42 ? 158 ILE A N   1 
ATOM   1258 C  CA  . ILE A  1 158 ? 31.290  -5.970  24.101  1.00 17.35 ? 158 ILE A CA  1 
ATOM   1259 C  C   . ILE A  1 158 ? 30.308  -5.829  25.253  1.00 16.95 ? 158 ILE A C   1 
ATOM   1260 O  O   . ILE A  1 158 ? 30.359  -4.802  26.023  1.00 19.12 ? 158 ILE A O   1 
ATOM   1261 C  CB  . ILE A  1 158 ? 30.460  -5.699  22.808  1.00 18.52 ? 158 ILE A CB  1 
ATOM   1262 C  CG1 . ILE A  1 158 ? 31.426  -5.687  21.633  1.00 22.73 ? 158 ILE A CG1 1 
ATOM   1263 C  CG2 . ILE A  1 158 ? 29.744  -4.327  22.906  1.00 20.78 ? 158 ILE A CG2 1 
ATOM   1264 C  CD1 . ILE A  1 158 ? 30.720  -5.811  20.301  1.00 21.72 ? 158 ILE A CD1 1 
ATOM   1265 N  N   . PHE A  1 159 ? 29.386  -6.804  25.411  1.00 16.40 ? 159 PHE A N   1 
ATOM   1266 C  CA  . PHE A  1 159 ? 28.290  -6.590  26.384  1.00 15.83 ? 159 PHE A CA  1 
ATOM   1267 C  C   . PHE A  1 159 ? 28.747  -6.429  27.850  1.00 16.67 ? 159 PHE A C   1 
ATOM   1268 O  O   . PHE A  1 159 ? 28.066  -5.772  28.632  1.00 18.51 ? 159 PHE A O   1 
ATOM   1269 C  CB  . PHE A  1 159 ? 27.283  -7.717  26.326  1.00 14.97 ? 159 PHE A CB  1 
ATOM   1270 C  CG  . PHE A  1 159 ? 26.531  -7.849  24.972  1.00 16.99 ? 159 PHE A CG  1 
ATOM   1271 C  CD1 . PHE A  1 159 ? 26.438  -6.765  24.058  1.00 17.92 ? 159 PHE A CD1 1 
ATOM   1272 C  CD2 . PHE A  1 159 ? 25.867  -9.042  24.658  1.00 16.32 ? 159 PHE A CD2 1 
ATOM   1273 C  CE1 . PHE A  1 159 ? 25.719  -6.967  22.829  1.00 16.22 ? 159 PHE A CE1 1 
ATOM   1274 C  CE2 . PHE A  1 159 ? 25.177  -9.190  23.475  1.00 18.67 ? 159 PHE A CE2 1 
ATOM   1275 C  CZ  . PHE A  1 159 ? 25.108  -8.159  22.559  1.00 16.60 ? 159 PHE A CZ  1 
ATOM   1276 N  N   . SER A  1 160 ? 29.897  -7.024  28.162  1.00 17.60 ? 160 SER A N   1 
ATOM   1277 C  CA  . SER A  1 160 ? 30.402  -6.875  29.581  1.00 20.47 ? 160 SER A CA  1 
ATOM   1278 C  C   . SER A  1 160 ? 30.784  -5.458  29.932  1.00 23.24 ? 160 SER A C   1 
ATOM   1279 O  O   . SER A  1 160 ? 31.013  -5.144  31.124  1.00 27.13 ? 160 SER A O   1 
ATOM   1280 C  CB  . SER A  1 160 ? 31.541  -7.879  29.795  1.00 20.78 ? 160 SER A CB  1 
ATOM   1281 O  OG  . SER A  1 160 ? 32.650  -7.560  29.021  1.00 22.63 ? 160 SER A OG  1 
ATOM   1282 N  N   . HIS A  1 161 ? 30.915  -4.575  28.950  1.00 19.73 ? 161 HIS A N   1 
ATOM   1283 C  CA  . HIS A  1 161 ? 31.230  -3.196  29.228  1.00 20.98 ? 161 HIS A CA  1 
ATOM   1284 C  C   . HIS A  1 161 ? 30.009  -2.259  29.251  1.00 19.48 ? 161 HIS A C   1 
ATOM   1285 O  O   . HIS A  1 161 ? 30.163  -1.051  29.461  1.00 20.95 ? 161 HIS A O   1 
ATOM   1286 C  CB  . HIS A  1 161 ? 32.275  -2.657  28.208  1.00 21.05 ? 161 HIS A CB  1 
ATOM   1287 C  CG  . HIS A  1 161 ? 33.567  -3.414  28.201  1.00 22.65 ? 161 HIS A CG  1 
ATOM   1288 N  ND1 . HIS A  1 161 ? 34.672  -3.009  28.940  1.00 26.32 ? 161 HIS A ND1 1 
ATOM   1289 C  CD2 . HIS A  1 161 ? 33.925  -4.600  27.556  1.00 21.64 ? 161 HIS A CD2 1 
ATOM   1290 C  CE1 . HIS A  1 161 ? 35.694  -3.871  28.729  1.00 27.81 ? 161 HIS A CE1 1 
ATOM   1291 N  NE2 . HIS A  1 161 ? 35.254  -4.847  27.863  1.00 23.55 ? 161 HIS A NE2 1 
ATOM   1292 N  N   . LEU A  1 162 ? 28.792  -2.816  28.974  1.00 19.01 ? 162 LEU A N   1 
ATOM   1293 C  CA  . LEU A  1 162 ? 27.593  -1.954  28.837  1.00 19.15 ? 162 LEU A CA  1 
ATOM   1294 C  C   . LEU A  1 162 ? 27.344  -1.109  30.085  1.00 20.56 ? 162 LEU A C   1 
ATOM   1295 O  O   . LEU A  1 162 ? 26.903  0.007   29.991  1.00 17.54 ? 162 LEU A O   1 
ATOM   1296 C  CB  . LEU A  1 162 ? 26.296  -2.779  28.492  1.00 18.76 ? 162 LEU A CB  1 
ATOM   1297 C  CG  . LEU A  1 162 ? 26.328  -3.488  27.128  1.00 18.76 ? 162 LEU A CG  1 
ATOM   1298 C  CD1 . LEU A  1 162 ? 25.068  -4.326  26.946  1.00 20.30 ? 162 LEU A CD1 1 
ATOM   1299 C  CD2 . LEU A  1 162 ? 26.388  -2.449  26.042  1.00 23.82 ? 162 LEU A CD2 1 
ATOM   1300 N  N   . GLN A  1 163 ? 27.578  -1.671  31.275  1.00 21.44 ? 163 GLN A N   1 
ATOM   1301 C  CA  . GLN A  1 163 ? 27.173  -0.876  32.418  1.00 23.54 ? 163 GLN A CA  1 
ATOM   1302 C  C   . GLN A  1 163 ? 28.039  0.365   32.548  1.00 23.22 ? 163 GLN A C   1 
ATOM   1303 O  O   . GLN A  1 163 ? 27.534  1.383   33.051  1.00 26.03 ? 163 GLN A O   1 
ATOM   1304 C  CB  . GLN A  1 163 ? 27.100  -1.682  33.718  1.00 30.70 ? 163 GLN A CB  1 
ATOM   1305 C  CG  . GLN A  1 163 ? 26.147  -2.912  33.614  1.00 42.65 ? 163 GLN A CG  1 
ATOM   1306 C  CD  . GLN A  1 163 ? 24.633  -2.615  33.412  1.00 48.40 ? 163 GLN A CD  1 
ATOM   1307 O  OE1 . GLN A  1 163 ? 24.092  -1.602  33.909  1.00 60.18 ? 163 GLN A OE1 1 
ATOM   1308 N  NE2 . GLN A  1 163 ? 23.939  -3.530  32.705  1.00 45.79 ? 163 GLN A NE2 1 
ATOM   1309 N  N   . HIS A  1 164 ? 29.244  0.369   31.961  1.00 18.58 ? 164 HIS A N   1 
ATOM   1310 C  CA  . HIS A  1 164 ? 30.076  1.581   31.982  1.00 19.31 ? 164 HIS A CA  1 
ATOM   1311 C  C   . HIS A  1 164 ? 29.687  2.639   31.028  1.00 20.19 ? 164 HIS A C   1 
ATOM   1312 O  O   . HIS A  1 164 ? 30.282  3.700   30.995  1.00 19.22 ? 164 HIS A O   1 
ATOM   1313 C  CB  . HIS A  1 164 ? 31.582  1.216   31.720  1.00 20.23 ? 164 HIS A CB  1 
ATOM   1314 C  CG  . HIS A  1 164 ? 32.217  0.305   32.769  1.00 21.67 ? 164 HIS A CG  1 
ATOM   1315 N  ND1 . HIS A  1 164 ? 32.087  0.491   34.111  1.00 22.72 ? 164 HIS A ND1 1 
ATOM   1316 C  CD2 . HIS A  1 164 ? 33.116  -0.743  32.604  1.00 29.05 ? 164 HIS A CD2 1 
ATOM   1317 C  CE1 . HIS A  1 164 ? 32.809  -0.444  34.753  1.00 20.16 ? 164 HIS A CE1 1 
ATOM   1318 N  NE2 . HIS A  1 164 ? 33.415  -1.214  33.844  1.00 31.02 ? 164 HIS A NE2 1 
ATOM   1319 N  N   . VAL A  1 165 ? 28.771  2.325   30.080  1.00 17.05 ? 165 VAL A N   1 
ATOM   1320 C  CA  . VAL A  1 165 ? 28.305  3.347   29.147  1.00 16.51 ? 165 VAL A CA  1 
ATOM   1321 C  C   . VAL A  1 165 ? 26.799  3.491   29.222  1.00 18.35 ? 165 VAL A C   1 
ATOM   1322 O  O   . VAL A  1 165 ? 26.134  3.774   28.204  1.00 16.43 ? 165 VAL A O   1 
ATOM   1323 C  CB  . VAL A  1 165 ? 28.716  2.991   27.664  1.00 17.17 ? 165 VAL A CB  1 
ATOM   1324 C  CG1 . VAL A  1 165 ? 30.263  3.130   27.566  1.00 18.01 ? 165 VAL A CG1 1 
ATOM   1325 C  CG2 . VAL A  1 165 ? 28.329  1.582   27.202  1.00 18.12 ? 165 VAL A CG2 1 
ATOM   1326 N  N   . LYS A  1 166 ? 26.236  3.382   30.427  1.00 17.62 ? 166 LYS A N   1 
ATOM   1327 C  CA  . LYS A  1 166 ? 24.793  3.483   30.665  1.00 16.82 ? 166 LYS A CA  1 
ATOM   1328 C  C   . LYS A  1 166 ? 24.162  4.777   30.125  1.00 16.24 ? 166 LYS A C   1 
ATOM   1329 O  O   . LYS A  1 166 ? 23.055  4.743   29.580  1.00 16.72 ? 166 LYS A O   1 
ATOM   1330 C  CB  . LYS A  1 166 ? 24.529  3.423   32.191  1.00 20.96 ? 166 LYS A CB  1 
ATOM   1331 C  CG  . LYS A  1 166 ? 23.093  3.332   32.642  1.00 23.57 ? 166 LYS A CG  1 
ATOM   1332 C  CD  . LYS A  1 166 ? 22.991  3.089   34.191  1.00 25.68 ? 166 LYS A CD  1 
ATOM   1333 C  CE  . LYS A  1 166 ? 23.165  1.584   34.459  1.00 32.66 ? 166 LYS A CE  1 
ATOM   1334 N  NZ  . LYS A  1 166 ? 24.572  1.009   34.448  1.00 33.06 ? 166 LYS A NZ  1 
ATOM   1335 N  N   . TYR A  1 167 ? 24.843  5.937   30.285  1.00 15.50 ? 167 TYR A N   1 
ATOM   1336 C  CA  . TYR A  1 167 ? 24.203  7.194   29.894  1.00 15.36 ? 167 TYR A CA  1 
ATOM   1337 C  C   . TYR A  1 167 ? 24.860  7.871   28.683  1.00 14.73 ? 167 TYR A C   1 
ATOM   1338 O  O   . TYR A  1 167 ? 26.050  7.651   28.416  1.00 16.27 ? 167 TYR A O   1 
ATOM   1339 C  CB  . TYR A  1 167 ? 24.247  8.196   31.033  1.00 15.41 ? 167 TYR A CB  1 
ATOM   1340 C  CG  . TYR A  1 167 ? 23.511  7.656   32.239  1.00 17.90 ? 167 TYR A CG  1 
ATOM   1341 C  CD1 . TYR A  1 167 ? 22.115  7.712   32.301  1.00 19.24 ? 167 TYR A CD1 1 
ATOM   1342 C  CD2 . TYR A  1 167 ? 24.233  7.050   33.299  1.00 17.94 ? 167 TYR A CD2 1 
ATOM   1343 C  CE1 . TYR A  1 167 ? 21.420  7.192   33.399  1.00 21.31 ? 167 TYR A CE1 1 
ATOM   1344 C  CE2 . TYR A  1 167 ? 23.533  6.497   34.387  1.00 22.86 ? 167 TYR A CE2 1 
ATOM   1345 C  CZ  . TYR A  1 167 ? 22.146  6.607   34.434  1.00 25.69 ? 167 TYR A CZ  1 
ATOM   1346 O  OH  . TYR A  1 167 ? 21.453  6.131   35.528  1.00 25.24 ? 167 TYR A OH  1 
ATOM   1347 N  N   . LYS A  1 168 ? 24.119  8.733   28.010  1.00 18.66 ? 168 LYS A N   1 
ATOM   1348 C  CA  . LYS A  1 168 ? 24.646  9.412   26.881  1.00 18.79 ? 168 LYS A CA  1 
ATOM   1349 C  C   . LYS A  1 168 ? 25.963  10.153  27.198  1.00 21.51 ? 168 LYS A C   1 
ATOM   1350 O  O   . LYS A  1 168 ? 26.027  10.807  28.228  1.00 22.15 ? 168 LYS A O   1 
ATOM   1351 C  CB  . LYS A  1 168 ? 23.592  10.398  26.391  1.00 18.94 ? 168 LYS A CB  1 
ATOM   1352 C  CG  . LYS A  1 168 ? 24.042  11.098  25.090  1.00 19.32 ? 168 LYS A CG  1 
ATOM   1353 C  CD  . LYS A  1 168 ? 23.030  12.097  24.555  1.00 27.52 ? 168 LYS A CD  1 
ATOM   1354 C  CE  . LYS A  1 168 ? 23.669  12.792  23.353  1.00 30.16 ? 168 LYS A CE  1 
ATOM   1355 N  NZ  . LYS A  1 168 ? 22.698  13.789  22.825  1.00 37.28 ? 168 LYS A NZ  1 
ATOM   1356 N  N   . GLY A  1 169 ? 26.966  10.078  26.326  1.00 20.60 ? 169 GLY A N   1 
ATOM   1357 C  CA  . GLY A  1 169 ? 28.222  10.772  26.525  1.00 24.06 ? 169 GLY A CA  1 
ATOM   1358 C  C   . GLY A  1 169 ? 29.201  9.913   27.276  1.00 22.79 ? 169 GLY A C   1 
ATOM   1359 O  O   . GLY A  1 169 ? 30.386  10.190  27.266  1.00 26.11 ? 169 GLY A O   1 
ATOM   1360 N  N   . GLN A  1 170 ? 28.734  8.876   27.957  1.00 20.00 ? 170 GLN A N   1 
ATOM   1361 C  CA  . GLN A  1 170 ? 29.736  8.013   28.637  1.00 18.66 ? 170 GLN A CA  1 
ATOM   1362 C  C   . GLN A  1 170 ? 30.556  7.101   27.729  1.00 22.16 ? 170 GLN A C   1 
ATOM   1363 O  O   . GLN A  1 170 ? 30.087  6.754   26.618  1.00 19.93 ? 170 GLN A O   1 
ATOM   1364 C  CB  . GLN A  1 170 ? 29.015  7.210   29.704  1.00 17.91 ? 170 GLN A CB  1 
ATOM   1365 C  CG  . GLN A  1 170 ? 28.440  8.018   30.847  1.00 19.67 ? 170 GLN A CG  1 
ATOM   1366 C  CD  . GLN A  1 170 ? 27.973  7.106   31.971  1.00 20.09 ? 170 GLN A CD  1 
ATOM   1367 O  OE1 . GLN A  1 170 ? 27.419  6.011   31.731  1.00 21.45 ? 170 GLN A OE1 1 
ATOM   1368 N  NE2 . GLN A  1 170 ? 28.158  7.550   33.210  1.00 18.27 ? 170 GLN A NE2 1 
ATOM   1369 N  N   A GLU A  1 171 ? 31.749  6.699   28.169  0.50 20.19 ? 171 GLU A N   1 
ATOM   1370 N  N   B GLU A  1 171 ? 31.758  6.684   28.151  0.50 19.42 ? 171 GLU A N   1 
ATOM   1371 C  CA  A GLU A  1 171 ? 32.670  5.956   27.374  0.50 19.60 ? 171 GLU A CA  1 
ATOM   1372 C  CA  B GLU A  1 171 ? 32.694  5.956   27.333  0.50 19.10 ? 171 GLU A CA  1 
ATOM   1373 C  C   A GLU A  1 171 ? 33.374  4.833   28.162  0.50 18.74 ? 171 GLU A C   1 
ATOM   1374 C  C   B GLU A  1 171 ? 33.552  4.970   28.111  0.50 18.71 ? 171 GLU A C   1 
ATOM   1375 O  O   A GLU A  1 171 ? 33.319  4.755   29.434  0.50 18.78 ? 171 GLU A O   1 
ATOM   1376 O  O   B GLU A  1 171 ? 33.843  5.169   29.308  0.50 19.26 ? 171 GLU A O   1 
ATOM   1377 C  CB  A GLU A  1 171 ? 33.656  6.929   26.662  0.50 21.98 ? 171 GLU A CB  1 
ATOM   1378 C  CB  B GLU A  1 171 ? 33.633  6.932   26.617  0.50 20.29 ? 171 GLU A CB  1 
ATOM   1379 C  CG  A GLU A  1 171 ? 32.947  8.071   25.907  0.50 24.08 ? 171 GLU A CG  1 
ATOM   1380 C  CG  B GLU A  1 171 ? 34.632  7.573   27.573  0.50 20.44 ? 171 GLU A CG  1 
ATOM   1381 C  CD  A GLU A  1 171 ? 33.842  9.174   25.300  0.50 25.44 ? 171 GLU A CD  1 
ATOM   1382 C  CD  B GLU A  1 171 ? 35.804  8.265   26.882  0.50 23.15 ? 171 GLU A CD  1 
ATOM   1383 O  OE1 A GLU A  1 171 ? 35.014  9.382   25.719  0.50 24.82 ? 171 GLU A OE1 1 
ATOM   1384 O  OE1 B GLU A  1 171 ? 35.711  8.607   25.683  0.50 23.81 ? 171 GLU A OE1 1 
ATOM   1385 O  OE2 A GLU A  1 171 ? 33.333  9.886   24.416  0.50 25.22 ? 171 GLU A OE2 1 
ATOM   1386 O  OE2 B GLU A  1 171 ? 36.849  8.477   27.547  0.50 22.53 ? 171 GLU A OE2 1 
ATOM   1387 N  N   . ALA A  1 172 ? 34.001  3.954   27.426  1.00 18.63 ? 172 ALA A N   1 
ATOM   1388 C  CA  . ALA A  1 172 ? 34.692  2.799   28.008  1.00 18.86 ? 172 ALA A CA  1 
ATOM   1389 C  C   . ALA A  1 172 ? 35.708  2.311   27.011  1.00 23.46 ? 172 ALA A C   1 
ATOM   1390 O  O   . ALA A  1 172 ? 35.570  2.581   25.800  1.00 26.08 ? 172 ALA A O   1 
ATOM   1391 C  CB  . ALA A  1 172 ? 33.718  1.677   28.427  1.00 20.81 ? 172 ALA A CB  1 
ATOM   1392 N  N   . PHE A  1 173 ? 36.778  1.681   27.494  1.00 23.70 ? 173 PHE A N   1 
ATOM   1393 C  CA  . PHE A  1 173 ? 37.760  1.107   26.648  1.00 26.55 ? 173 PHE A CA  1 
ATOM   1394 C  C   . PHE A  1 173 ? 37.592  -0.368  26.590  1.00 25.24 ? 173 PHE A C   1 
ATOM   1395 O  O   . PHE A  1 173 ? 37.370  -1.031  27.623  1.00 26.99 ? 173 PHE A O   1 
ATOM   1396 C  CB  . PHE A  1 173 ? 39.129  1.556   27.143  1.00 23.28 ? 173 PHE A CB  1 
ATOM   1397 C  CG  . PHE A  1 173 ? 39.433  2.934   26.646  1.00 26.71 ? 173 PHE A CG  1 
ATOM   1398 C  CD1 . PHE A  1 173 ? 39.722  3.166   25.262  1.00 27.58 ? 173 PHE A CD1 1 
ATOM   1399 C  CD2 . PHE A  1 173 ? 39.324  4.031   27.520  1.00 33.22 ? 173 PHE A CD2 1 
ATOM   1400 C  CE1 . PHE A  1 173 ? 39.974  4.439   24.795  1.00 33.40 ? 173 PHE A CE1 1 
ATOM   1401 C  CE2 . PHE A  1 173 ? 39.578  5.306   27.042  1.00 36.29 ? 173 PHE A CE2 1 
ATOM   1402 C  CZ  . PHE A  1 173 ? 39.902  5.513   25.690  1.00 35.67 ? 173 PHE A CZ  1 
ATOM   1403 N  N   . VAL A  1 174 ? 37.617  -0.896  25.358  1.00 22.41 ? 174 VAL A N   1 
ATOM   1404 C  CA  . VAL A  1 174 ? 37.524  -2.297  25.131  1.00 21.14 ? 174 VAL A CA  1 
ATOM   1405 C  C   . VAL A  1 174 ? 38.816  -2.794  24.515  1.00 22.77 ? 174 VAL A C   1 
ATOM   1406 O  O   . VAL A  1 174 ? 39.227  -2.262  23.471  1.00 22.28 ? 174 VAL A O   1 
ATOM   1407 C  CB  . VAL A  1 174 ? 36.315  -2.616  24.180  1.00 18.88 ? 174 VAL A CB  1 
ATOM   1408 C  CG1 . VAL A  1 174 ? 36.184  -4.073  23.942  1.00 18.96 ? 174 VAL A CG1 1 
ATOM   1409 C  CG2 . VAL A  1 174 ? 35.029  -2.087  24.803  1.00 21.99 ? 174 VAL A CG2 1 
ATOM   1410 N  N   . PRO A  1 175 ? 39.429  -3.848  25.120  1.00 22.59 ? 175 PRO A N   1 
ATOM   1411 C  CA  . PRO A  1 175 ? 40.642  -4.434  24.581  1.00 24.74 ? 175 PRO A CA  1 
ATOM   1412 C  C   . PRO A  1 175 ? 40.365  -5.150  23.275  1.00 21.24 ? 175 PRO A C   1 
ATOM   1413 O  O   . PRO A  1 175 ? 39.295  -5.826  23.107  1.00 20.24 ? 175 PRO A O   1 
ATOM   1414 C  CB  . PRO A  1 175 ? 41.086  -5.454  25.663  1.00 26.57 ? 175 PRO A CB  1 
ATOM   1415 C  CG  . PRO A  1 175 ? 40.269  -5.103  26.872  1.00 26.50 ? 175 PRO A CG  1 
ATOM   1416 C  CD  . PRO A  1 175 ? 38.975  -4.475  26.359  1.00 23.99 ? 175 PRO A CD  1 
ATOM   1417 N  N   . GLY A  1 176 ? 41.295  -5.005  22.358  1.00 22.44 ? 176 GLY A N   1 
ATOM   1418 C  CA  . GLY A  1 176 ? 41.093  -5.593  21.085  1.00 20.54 ? 176 GLY A CA  1 
ATOM   1419 C  C   . GLY A  1 176 ? 40.778  -7.080  21.136  1.00 21.42 ? 176 GLY A C   1 
ATOM   1420 O  O   . GLY A  1 176 ? 41.418  -7.891  21.837  1.00 21.66 ? 176 GLY A O   1 
ATOM   1421 N  N   . PHE A  1 177 ? 39.823  -7.507  20.291  1.00 19.53 ? 177 PHE A N   1 
ATOM   1422 C  CA  . PHE A  1 177 ? 39.540  -8.897  20.060  1.00 19.75 ? 177 PHE A CA  1 
ATOM   1423 C  C   . PHE A  1 177 ? 39.172  -9.148  18.582  1.00 18.35 ? 177 PHE A C   1 
ATOM   1424 O  O   . PHE A  1 177 ? 39.192  -8.155  17.832  1.00 17.07 ? 177 PHE A O   1 
ATOM   1425 C  CB  . PHE A  1 177 ? 38.406  -9.406  21.001  1.00 18.91 ? 177 PHE A CB  1 
ATOM   1426 C  CG  . PHE A  1 177 ? 36.990  -8.819  20.668  1.00 17.52 ? 177 PHE A CG  1 
ATOM   1427 C  CD1 . PHE A  1 177 ? 36.094  -9.611  19.926  1.00 17.54 ? 177 PHE A CD1 1 
ATOM   1428 C  CD2 . PHE A  1 177 ? 36.636  -7.527  21.099  1.00 18.71 ? 177 PHE A CD2 1 
ATOM   1429 C  CE1 . PHE A  1 177 ? 34.806  -9.098  19.637  1.00 19.37 ? 177 PHE A CE1 1 
ATOM   1430 C  CE2 . PHE A  1 177 ? 35.355  -6.995  20.820  1.00 19.86 ? 177 PHE A CE2 1 
ATOM   1431 C  CZ  . PHE A  1 177 ? 34.460  -7.799  20.054  1.00 19.73 ? 177 PHE A CZ  1 
ATOM   1432 N  N   . ASN A  1 178 ? 39.035  -10.404 18.174  1.00 19.13 ? 178 ASN A N   1 
ATOM   1433 C  CA  . ASN A  1 178 ? 38.777  -10.740 16.786  1.00 17.98 ? 178 ASN A CA  1 
ATOM   1434 C  C   . ASN A  1 178 ? 37.265  -10.436 16.436  1.00 17.32 ? 178 ASN A C   1 
ATOM   1435 O  O   . ASN A  1 178 ? 36.351  -11.253 16.708  1.00 15.64 ? 178 ASN A O   1 
ATOM   1436 C  CB  . ASN A  1 178 ? 39.109  -12.202 16.491  1.00 18.45 ? 178 ASN A CB  1 
ATOM   1437 C  CG  . ASN A  1 178 ? 38.961  -12.536 15.037  1.00 21.49 ? 178 ASN A CG  1 
ATOM   1438 O  OD1 . ASN A  1 178 ? 38.731  -11.666 14.184  1.00 18.01 ? 178 ASN A OD1 1 
ATOM   1439 N  ND2 . ASN A  1 178 ? 39.012  -13.788 14.726  1.00 23.22 ? 178 ASN A ND2 1 
ATOM   1440 N  N   . ILE A  1 179 ? 37.083  -9.295  15.765  1.00 14.30 ? 179 ILE A N   1 
ATOM   1441 C  CA  . ILE A  1 179 ? 35.730  -8.861  15.385  1.00 14.88 ? 179 ILE A CA  1 
ATOM   1442 C  C   . ILE A  1 179 ? 35.107  -9.938  14.466  1.00 14.41 ? 179 ILE A C   1 
ATOM   1443 O  O   . ILE A  1 179 ? 33.849  -10.033 14.355  1.00 13.46 ? 179 ILE A O   1 
ATOM   1444 C  CB  . ILE A  1 179 ? 35.806  -7.525  14.673  1.00 14.25 ? 179 ILE A CB  1 
ATOM   1445 C  CG1 . ILE A  1 179 ? 36.422  -6.473  15.592  1.00 15.21 ? 179 ILE A CG1 1 
ATOM   1446 C  CG2 . ILE A  1 179 ? 34.369  -7.105  14.236  1.00 14.63 ? 179 ILE A CG2 1 
ATOM   1447 C  CD1 . ILE A  1 179 ? 35.732  -6.261  16.963  1.00 16.60 ? 179 ILE A CD1 1 
ATOM   1448 N  N   . GLU A  1 180 ? 35.835  -10.795 13.760  1.00 15.21 ? 180 GLU A N   1 
ATOM   1449 C  CA  . GLU A  1 180 ? 35.222  -11.746 12.914  1.00 14.65 ? 180 GLU A CA  1 
ATOM   1450 C  C   . GLU A  1 180 ? 34.402  -12.786 13.758  1.00 14.31 ? 180 GLU A C   1 
ATOM   1451 O  O   . GLU A  1 180 ? 33.531  -13.494 13.209  1.00 15.97 ? 180 GLU A O   1 
ATOM   1452 C  CB  . GLU A  1 180 ? 36.300  -12.482 12.088  1.00 18.66 ? 180 GLU A CB  1 
ATOM   1453 C  CG  . GLU A  1 180 ? 35.735  -13.214 10.854  1.00 23.05 ? 180 GLU A CG  1 
ATOM   1454 C  CD  . GLU A  1 180 ? 36.798  -13.667 9.834   1.00 25.59 ? 180 GLU A CD  1 
ATOM   1455 O  OE1 . GLU A  1 180 ? 37.981  -13.297 9.979   1.00 26.25 ? 180 GLU A OE1 1 
ATOM   1456 O  OE2 . GLU A  1 180 ? 36.398  -14.430 8.959   1.00 29.70 ? 180 GLU A OE2 1 
ATOM   1457 N  N   . GLU A  1 181 ? 34.726  -12.849 15.052  1.00 14.20 ? 181 GLU A N   1 
ATOM   1458 C  CA  . GLU A  1 181 ? 33.974  -13.774 15.889  1.00 14.62 ? 181 GLU A CA  1 
ATOM   1459 C  C   . GLU A  1 181 ? 32.467  -13.332 16.036  1.00 14.49 ? 181 GLU A C   1 
ATOM   1460 O  O   . GLU A  1 181 ? 31.683  -14.144 16.486  1.00 14.56 ? 181 GLU A O   1 
ATOM   1461 C  CB  . GLU A  1 181 ? 34.543  -13.879 17.315  1.00 16.93 ? 181 GLU A CB  1 
ATOM   1462 C  CG  . GLU A  1 181 ? 36.003  -14.358 17.446  1.00 18.65 ? 181 GLU A CG  1 
ATOM   1463 C  CD  . GLU A  1 181 ? 36.600  -14.134 18.825  1.00 23.67 ? 181 GLU A CD  1 
ATOM   1464 O  OE1 . GLU A  1 181 ? 35.907  -13.775 19.845  1.00 22.58 ? 181 GLU A OE1 1 
ATOM   1465 O  OE2 . GLU A  1 181 ? 37.834  -14.452 18.905  1.00 23.55 ? 181 GLU A OE2 1 
ATOM   1466 N  N   . LEU A  1 182 ? 32.170  -12.064 15.694  1.00 12.57 ? 182 LEU A N   1 
ATOM   1467 C  CA  . LEU A  1 182 ? 30.795  -11.591 15.734  1.00 12.69 ? 182 LEU A CA  1 
ATOM   1468 C  C   . LEU A  1 182 ? 30.022  -11.942 14.508  1.00 12.99 ? 182 LEU A C   1 
ATOM   1469 O  O   . LEU A  1 182 ? 28.780  -11.754 14.460  1.00 12.85 ? 182 LEU A O   1 
ATOM   1470 C  CB  . LEU A  1 182 ? 30.841  -10.061 15.843  1.00 11.55 ? 182 LEU A CB  1 
ATOM   1471 C  CG  . LEU A  1 182 ? 31.596  -9.509  17.066  1.00 11.28 ? 182 LEU A CG  1 
ATOM   1472 C  CD1 . LEU A  1 182 ? 31.520  -7.961  17.150  1.00 13.17 ? 182 LEU A CD1 1 
ATOM   1473 C  CD2 . LEU A  1 182 ? 31.081  -10.053 18.368  1.00 12.84 ? 182 LEU A CD2 1 
ATOM   1474 N  N   . LEU A  1 183 ? 30.649  -12.435 13.460  1.00 12.64 ? 183 LEU A N   1 
ATOM   1475 C  CA  . LEU A  1 183 ? 30.013  -12.827 12.242  1.00 13.06 ? 183 LEU A CA  1 
ATOM   1476 C  C   . LEU A  1 183 ? 29.435  -14.222 12.332  1.00 12.92 ? 183 LEU A C   1 
ATOM   1477 O  O   . LEU A  1 183 ? 29.989  -15.034 13.105  1.00 13.49 ? 183 LEU A O   1 
ATOM   1478 C  CB  . LEU A  1 183 ? 31.038  -12.772 11.063  1.00 13.50 ? 183 LEU A CB  1 
ATOM   1479 C  CG  . LEU A  1 183 ? 31.683  -11.346 10.960  1.00 14.26 ? 183 LEU A CG  1 
ATOM   1480 C  CD1 . LEU A  1 183 ? 32.651  -11.399 9.755   1.00 17.38 ? 183 LEU A CD1 1 
ATOM   1481 C  CD2 . LEU A  1 183 ? 30.650  -10.252 10.805  1.00 15.64 ? 183 LEU A CD2 1 
ATOM   1482 N  N   . PRO A  1 184 ? 28.405  -14.509 11.579  1.00 12.60 ? 184 PRO A N   1 
ATOM   1483 C  CA  . PRO A  1 184 ? 27.762  -15.783 11.627  1.00 13.47 ? 184 PRO A CA  1 
ATOM   1484 C  C   . PRO A  1 184 ? 28.513  -16.819 10.779  1.00 16.40 ? 184 PRO A C   1 
ATOM   1485 O  O   . PRO A  1 184 ? 29.555  -16.554 10.120  1.00 15.92 ? 184 PRO A O   1 
ATOM   1486 C  CB  . PRO A  1 184 ? 26.303  -15.434 11.049  1.00 13.64 ? 184 PRO A CB  1 
ATOM   1487 C  CG  . PRO A  1 184 ? 26.718  -14.450 9.931   1.00 12.30 ? 184 PRO A CG  1 
ATOM   1488 C  CD  . PRO A  1 184 ? 27.685  -13.575 10.662  1.00 12.58 ? 184 PRO A CD  1 
ATOM   1489 N  N   . GLU A  1 185 ? 27.913  -18.021 10.833  1.00 19.54 ? 185 GLU A N   1 
ATOM   1490 C  CA  . GLU A  1 185 ? 28.323  -19.132 9.966   1.00 19.49 ? 185 GLU A CA  1 
ATOM   1491 C  C   . GLU A  1 185 ? 28.130  -18.827 8.529   1.00 21.33 ? 185 GLU A C   1 
ATOM   1492 O  O   . GLU A  1 185 ? 27.126  -18.106 8.156   1.00 18.18 ? 185 GLU A O   1 
ATOM   1493 C  CB  . GLU A  1 185 ? 27.348  -20.332 10.298  1.00 23.00 ? 185 GLU A CB  1 
ATOM   1494 C  CG  . GLU A  1 185 ? 27.713  -21.020 11.639  1.00 30.78 ? 185 GLU A CG  1 
ATOM   1495 C  CD  . GLU A  1 185 ? 29.210  -20.969 11.981  1.00 42.62 ? 185 GLU A CD  1 
ATOM   1496 O  OE1 . GLU A  1 185 ? 30.032  -21.646 11.294  1.00 43.90 ? 185 GLU A OE1 1 
ATOM   1497 O  OE2 . GLU A  1 185 ? 29.576  -20.264 12.946  1.00 47.17 ? 185 GLU A OE2 1 
ATOM   1498 N  N   . ARG A  1 186 ? 29.035  -19.342 7.681   1.00 17.47 ? 186 ARG A N   1 
ATOM   1499 C  CA  . ARG A  1 186 ? 28.851  -19.278 6.229   1.00 18.67 ? 186 ARG A CA  1 
ATOM   1500 C  C   . ARG A  1 186 ? 28.564  -17.807 5.787   1.00 15.58 ? 186 ARG A C   1 
ATOM   1501 O  O   . ARG A  1 186 ? 27.620  -17.496 5.021   1.00 16.54 ? 186 ARG A O   1 
ATOM   1502 C  CB  . ARG A  1 186 ? 27.762  -20.200 5.743   1.00 20.32 ? 186 ARG A CB  1 
ATOM   1503 C  CG  . ARG A  1 186 ? 28.148  -21.606 6.252   1.00 26.49 ? 186 ARG A CG  1 
ATOM   1504 C  CD  . ARG A  1 186 ? 27.393  -22.751 5.593   1.00 27.43 ? 186 ARG A CD  1 
ATOM   1505 N  NE  . ARG A  1 186 ? 25.950  -22.512 5.436   1.00 30.53 ? 186 ARG A NE  1 
ATOM   1506 C  CZ  . ARG A  1 186 ? 25.034  -22.575 6.414   1.00 29.76 ? 186 ARG A CZ  1 
ATOM   1507 N  NH1 . ARG A  1 186 ? 25.371  -22.906 7.671   1.00 32.83 ? 186 ARG A NH1 1 
ATOM   1508 N  NH2 . ARG A  1 186 ? 23.750  -22.322 6.130   1.00 35.58 ? 186 ARG A NH2 1 
ATOM   1509 N  N   . THR A  1 187 ? 29.572  -17.026 6.055   1.00 12.86 ? 187 THR A N   1 
ATOM   1510 C  CA  . THR A  1 187 ? 29.542  -15.610 5.589   1.00 13.83 ? 187 THR A CA  1 
ATOM   1511 C  C   . THR A  1 187 ? 29.567  -15.485 4.104   1.00 14.84 ? 187 THR A C   1 
ATOM   1512 O  O   . THR A  1 187 ? 29.211  -14.457 3.603   1.00 15.13 ? 187 THR A O   1 
ATOM   1513 C  CB  . THR A  1 187 ? 30.676  -14.759 6.182   1.00 14.16 ? 187 THR A CB  1 
ATOM   1514 O  OG1 . THR A  1 187 ? 31.946  -15.413 5.948   1.00 17.29 ? 187 THR A OG1 1 
ATOM   1515 C  CG2 . THR A  1 187 ? 30.495  -14.563 7.700   1.00 15.08 ? 187 THR A CG2 1 
ATOM   1516 N  N   . ALA A  1 188 ? 29.958  -16.524 3.331   1.00 14.15 ? 188 ALA A N   1 
ATOM   1517 C  CA  . ALA A  1 188 ? 29.696  -16.529 1.866   1.00 14.40 ? 188 ALA A CA  1 
ATOM   1518 C  C   . ALA A  1 188 ? 28.234  -16.316 1.445   1.00 13.38 ? 188 ALA A C   1 
ATOM   1519 O  O   . ALA A  1 188 ? 28.038  -15.920 0.296   1.00 13.31 ? 188 ALA A O   1 
ATOM   1520 C  CB  . ALA A  1 188 ? 30.218  -17.887 1.216   1.00 16.99 ? 188 ALA A CB  1 
ATOM   1521 N  N   . GLU A  1 189 ? 27.258  -16.586 2.352   1.00 14.20 ? 189 GLU A N   1 
ATOM   1522 C  CA  . GLU A  1 189 ? 25.845  -16.537 2.024   1.00 14.31 ? 189 GLU A CA  1 
ATOM   1523 C  C   . GLU A  1 189 ? 25.332  -15.183 2.572   1.00 12.25 ? 189 GLU A C   1 
ATOM   1524 O  O   . GLU A  1 189 ? 25.327  -14.935 3.787   1.00 11.21 ? 189 GLU A O   1 
ATOM   1525 C  CB  . GLU A  1 189 ? 25.049  -17.701 2.654   1.00 14.20 ? 189 GLU A CB  1 
ATOM   1526 C  CG  . GLU A  1 189 ? 25.538  -19.082 2.211   1.00 18.46 ? 189 GLU A CG  1 
ATOM   1527 C  CD  . GLU A  1 189 ? 25.034  -20.207 3.093   1.00 24.65 ? 189 GLU A CD  1 
ATOM   1528 O  OE1 . GLU A  1 189 ? 24.308  -20.067 4.096   1.00 21.01 ? 189 GLU A OE1 1 
ATOM   1529 O  OE2 . GLU A  1 189 ? 25.496  -21.373 2.858   1.00 29.19 ? 189 GLU A OE2 1 
ATOM   1530 N  N   . TYR A  1 190 ? 24.966  -14.305 1.633   1.00 10.81 ? 190 TYR A N   1 
ATOM   1531 C  CA  . TYR A  1 190 ? 24.460  -12.951 2.008   1.00 9.87  ? 190 TYR A CA  1 
ATOM   1532 C  C   . TYR A  1 190 ? 23.501  -12.394 1.000   1.00 10.47 ? 190 TYR A C   1 
ATOM   1533 O  O   . TYR A  1 190 ? 23.429  -12.765 -0.192  1.00 10.58 ? 190 TYR A O   1 
ATOM   1534 C  CB  . TYR A  1 190 ? 25.641  -11.961 2.243   1.00 11.42 ? 190 TYR A CB  1 
ATOM   1535 C  CG  . TYR A  1 190 ? 26.567  -11.849 1.063   1.00 11.96 ? 190 TYR A CG  1 
ATOM   1536 C  CD1 . TYR A  1 190 ? 26.270  -10.952 0.051   1.00 13.18 ? 190 TYR A CD1 1 
ATOM   1537 C  CD2 . TYR A  1 190 ? 27.792  -12.569 1.001   1.00 12.32 ? 190 TYR A CD2 1 
ATOM   1538 C  CE1 . TYR A  1 190 ? 27.148  -10.735 -1.037  1.00 14.44 ? 190 TYR A CE1 1 
ATOM   1539 C  CE2 . TYR A  1 190 ? 28.688  -12.329 -0.078  1.00 11.25 ? 190 TYR A CE2 1 
ATOM   1540 C  CZ  . TYR A  1 190 ? 28.344  -11.456 -1.063  1.00 12.85 ? 190 TYR A CZ  1 
ATOM   1541 O  OH  . TYR A  1 190 ? 29.288  -11.252 -2.114  1.00 14.30 ? 190 TYR A OH  1 
ATOM   1542 N  N   . TYR A  1 191 ? 22.753  -11.390 1.490   1.00 10.50 ? 191 TYR A N   1 
ATOM   1543 C  CA  . TYR A  1 191 ? 21.989  -10.482 0.657   1.00 9.72  ? 191 TYR A CA  1 
ATOM   1544 C  C   . TYR A  1 191 ? 22.704  -9.202  0.383   1.00 10.33 ? 191 TYR A C   1 
ATOM   1545 O  O   . TYR A  1 191 ? 23.485  -8.755  1.259   1.00 10.43 ? 191 TYR A O   1 
ATOM   1546 C  CB  . TYR A  1 191 ? 20.666  -10.072 1.413   1.00 10.70 ? 191 TYR A CB  1 
ATOM   1547 C  CG  . TYR A  1 191 ? 19.865  -11.248 1.985   1.00 10.63 ? 191 TYR A CG  1 
ATOM   1548 C  CD1 . TYR A  1 191 ? 18.802  -11.776 1.231   1.00 11.03 ? 191 TYR A CD1 1 
ATOM   1549 C  CD2 . TYR A  1 191 ? 20.060  -11.669 3.311   1.00 9.68  ? 191 TYR A CD2 1 
ATOM   1550 C  CE1 . TYR A  1 191 ? 17.942  -12.760 1.781   1.00 11.69 ? 191 TYR A CE1 1 
ATOM   1551 C  CE2 . TYR A  1 191 ? 19.231  -12.675 3.856   1.00 10.97 ? 191 TYR A CE2 1 
ATOM   1552 C  CZ  . TYR A  1 191 ? 18.246  -13.181 3.049   1.00 11.14 ? 191 TYR A CZ  1 
ATOM   1553 O  OH  . TYR A  1 191 ? 17.463  -14.187 3.680   1.00 14.39 ? 191 TYR A OH  1 
ATOM   1554 N  N   . ARG A  1 192 ? 22.534  -8.644  -0.799  1.00 11.27 ? 192 ARG A N   1 
ATOM   1555 C  CA  . ARG A  1 192 ? 23.283  -7.423  -1.177  1.00 10.78 ? 192 ARG A CA  1 
ATOM   1556 C  C   . ARG A  1 192 ? 22.340  -6.502  -1.918  1.00 10.96 ? 192 ARG A C   1 
ATOM   1557 O  O   . ARG A  1 192 ? 21.627  -6.912  -2.835  1.00 11.46 ? 192 ARG A O   1 
ATOM   1558 C  CB  . ARG A  1 192 ? 24.386  -7.829  -2.169  1.00 12.33 ? 192 ARG A CB  1 
ATOM   1559 C  CG  . ARG A  1 192 ? 24.991  -6.713  -2.988  1.00 12.52 ? 192 ARG A CG  1 
ATOM   1560 C  CD  . ARG A  1 192 ? 25.836  -5.757  -2.146  1.00 12.31 ? 192 ARG A CD  1 
ATOM   1561 N  NE  . ARG A  1 192 ? 26.803  -6.405  -1.257  1.00 12.90 ? 192 ARG A NE  1 
ATOM   1562 C  CZ  . ARG A  1 192 ? 27.958  -6.935  -1.652  1.00 12.54 ? 192 ARG A CZ  1 
ATOM   1563 N  NH1 . ARG A  1 192 ? 28.296  -6.931  -2.936  1.00 15.27 ? 192 ARG A NH1 1 
ATOM   1564 N  NH2 . ARG A  1 192 ? 28.775  -7.482  -0.760  1.00 13.45 ? 192 ARG A NH2 1 
ATOM   1565 N  N   . TYR A  1 193 ? 22.314  -5.234  -1.504  1.00 9.39  ? 193 TYR A N   1 
ATOM   1566 C  CA  . TYR A  1 193 ? 21.505  -4.239  -2.210  1.00 9.36  ? 193 TYR A CA  1 
ATOM   1567 C  C   . TYR A  1 193 ? 22.108  -2.833  -1.940  1.00 10.06 ? 193 TYR A C   1 
ATOM   1568 O  O   . TYR A  1 193 ? 22.821  -2.637  -0.940  1.00 9.89  ? 193 TYR A O   1 
ATOM   1569 C  CB  . TYR A  1 193 ? 20.019  -4.330  -1.842  1.00 11.05 ? 193 TYR A CB  1 
ATOM   1570 C  CG  . TYR A  1 193 ? 19.650  -3.792  -0.449  1.00 9.66  ? 193 TYR A CG  1 
ATOM   1571 C  CD1 . TYR A  1 193 ? 19.101  -2.542  -0.366  1.00 9.33  ? 193 TYR A CD1 1 
ATOM   1572 C  CD2 . TYR A  1 193 ? 19.838  -4.542  0.719   1.00 10.15 ? 193 TYR A CD2 1 
ATOM   1573 C  CE1 . TYR A  1 193 ? 18.733  -1.975  0.884   1.00 9.78  ? 193 TYR A CE1 1 
ATOM   1574 C  CE2 . TYR A  1 193 ? 19.531  -4.030  1.953   1.00 9.10  ? 193 TYR A CE2 1 
ATOM   1575 C  CZ  . TYR A  1 193 ? 19.011  -2.755  2.065   1.00 8.82  ? 193 TYR A CZ  1 
ATOM   1576 O  OH  . TYR A  1 193 ? 18.642  -2.130  3.222   1.00 9.00  ? 193 TYR A OH  1 
ATOM   1577 N  N   A ARG A  1 194 ? 21.850  -1.856  -2.768  0.50 10.21 ? 194 ARG A N   1 
ATOM   1578 N  N   B ARG A  1 194 ? 21.621  -1.869  -2.693  0.50 9.95  ? 194 ARG A N   1 
ATOM   1579 C  CA  A ARG A  1 194 ? 22.285  -0.474  -2.466  0.50 10.17 ? 194 ARG A CA  1 
ATOM   1580 C  CA  B ARG A  1 194 ? 21.956  -0.435  -2.553  0.50 10.02 ? 194 ARG A CA  1 
ATOM   1581 C  C   A ARG A  1 194 ? 21.125  0.192   -1.782  0.50 10.69 ? 194 ARG A C   1 
ATOM   1582 C  C   B ARG A  1 194 ? 20.958  0.263   -1.703  0.50 10.68 ? 194 ARG A C   1 
ATOM   1583 O  O   A ARG A  1 194 ? 19.921  0.097   -2.279  0.50 12.23 ? 194 ARG A O   1 
ATOM   1584 O  O   B ARG A  1 194 ? 19.729  0.308   -1.980  0.50 9.82  ? 194 ARG A O   1 
ATOM   1585 C  CB  A ARG A  1 194 ? 22.526  0.270   -3.796  0.50 12.20 ? 194 ARG A CB  1 
ATOM   1586 C  CB  B ARG A  1 194 ? 21.967  0.241   -3.981  0.50 10.33 ? 194 ARG A CB  1 
ATOM   1587 C  CG  A ARG A  1 194 ? 23.644  -0.346  -4.584  0.50 15.63 ? 194 ARG A CG  1 
ATOM   1588 C  CG  B ARG A  1 194 ? 23.359  0.026   -4.605  0.50 13.88 ? 194 ARG A CG  1 
ATOM   1589 C  CD  A ARG A  1 194 ? 24.898  0.406   -4.220  0.50 19.71 ? 194 ARG A CD  1 
ATOM   1590 C  CD  B ARG A  1 194 ? 23.587  0.471   -6.085  0.50 15.47 ? 194 ARG A CD  1 
ATOM   1591 N  NE  A ARG A  1 194 ? 26.082  -0.123  -4.909  0.50 25.80 ? 194 ARG A NE  1 
ATOM   1592 N  NE  B ARG A  1 194 ? 24.806  -0.254  -6.519  0.50 22.89 ? 194 ARG A NE  1 
ATOM   1593 C  CZ  A ARG A  1 194 ? 27.311  0.378   -4.822  0.50 25.77 ? 194 ARG A CZ  1 
ATOM   1594 C  CZ  B ARG A  1 194 ? 26.028  0.286   -6.553  0.50 23.25 ? 194 ARG A CZ  1 
ATOM   1595 N  NH1 A ARG A  1 194 ? 27.556  1.439   -4.060  0.50 26.94 ? 194 ARG A NH1 1 
ATOM   1596 N  NH1 B ARG A  1 194 ? 26.209  1.558   -6.209  0.50 29.59 ? 194 ARG A NH1 1 
ATOM   1597 N  NH2 A ARG A  1 194 ? 28.306  -0.221  -5.470  0.50 29.90 ? 194 ARG A NH2 1 
ATOM   1598 N  NH2 B ARG A  1 194 ? 27.095  -0.434  -6.903  0.50 28.25 ? 194 ARG A NH2 1 
ATOM   1599 N  N   . GLY A  1 195 ? 21.410  0.816   -0.606  1.00 9.82  ? 195 GLY A N   1 
ATOM   1600 C  CA  . GLY A  1 195 ? 20.443  1.512   0.207   1.00 10.98 ? 195 GLY A CA  1 
ATOM   1601 C  C   . GLY A  1 195 ? 21.032  2.703   0.925   1.00 9.26  ? 195 GLY A C   1 
ATOM   1602 O  O   . GLY A  1 195 ? 21.875  3.432   0.393   1.00 9.86  ? 195 GLY A O   1 
ATOM   1603 N  N   . SER A  1 196 ? 20.619  2.882   2.166   1.00 8.37  ? 196 SER A N   1 
ATOM   1604 C  CA  . SER A  1 196 ? 20.922  4.140   2.843   1.00 8.49  ? 196 SER A CA  1 
ATOM   1605 C  C   . SER A  1 196 ? 21.394  3.844   4.284   1.00 8.69  ? 196 SER A C   1 
ATOM   1606 O  O   . SER A  1 196 ? 21.160  2.726   4.860   1.00 8.38  ? 196 SER A O   1 
ATOM   1607 C  CB  . SER A  1 196 ? 19.753  5.099   2.971   1.00 9.02  ? 196 SER A CB  1 
ATOM   1608 O  OG  . SER A  1 196 ? 18.758  4.582   3.917   1.00 9.06  ? 196 SER A OG  1 
ATOM   1609 N  N   . LEU A  1 197 ? 21.914  4.876   4.948   1.00 8.67  ? 197 LEU A N   1 
ATOM   1610 C  CA  . LEU A  1 197 ? 22.005  4.836   6.367   1.00 9.63  ? 197 LEU A CA  1 
ATOM   1611 C  C   . LEU A  1 197 ? 20.576  4.681   6.928   1.00 9.67  ? 197 LEU A C   1 
ATOM   1612 O  O   . LEU A  1 197 ? 19.615  5.311   6.434   1.00 9.22  ? 197 LEU A O   1 
ATOM   1613 C  CB  . LEU A  1 197 ? 22.631  6.118   6.948   1.00 10.87 ? 197 LEU A CB  1 
ATOM   1614 C  CG  . LEU A  1 197 ? 24.109  6.382   6.575   1.00 13.00 ? 197 LEU A CG  1 
ATOM   1615 C  CD1 . LEU A  1 197 ? 24.569  7.720   7.115   1.00 15.33 ? 197 LEU A CD1 1 
ATOM   1616 C  CD2 . LEU A  1 197 ? 24.939  5.305   7.208   1.00 14.57 ? 197 LEU A CD2 1 
ATOM   1617 N  N   . THR A  1 198 ? 20.410  3.973   8.026   1.00 8.73  ? 198 THR A N   1 
ATOM   1618 C  CA  . THR A  1 198 ? 19.088  3.761   8.639   1.00 8.12  ? 198 THR A CA  1 
ATOM   1619 C  C   . THR A  1 198 ? 18.789  4.784   9.721   1.00 9.06  ? 198 THR A C   1 
ATOM   1620 O  O   . THR A  1 198 ? 17.738  4.693   10.391  1.00 8.99  ? 198 THR A O   1 
ATOM   1621 C  CB  . THR A  1 198 ? 18.938  2.344   9.221   1.00 7.87  ? 198 THR A CB  1 
ATOM   1622 O  OG1 . THR A  1 198 ? 19.875  2.224   10.322  1.00 8.87  ? 198 THR A OG1 1 
ATOM   1623 C  CG2 . THR A  1 198 ? 19.149  1.252   8.188   1.00 8.33  ? 198 THR A CG2 1 
ATOM   1624 N  N   . THR A  1 199 ? 19.745  5.710   9.964   1.00 9.16  ? 199 THR A N   1 
ATOM   1625 C  CA  . THR A  1 199 ? 19.564  6.789   10.900  1.00 9.62  ? 199 THR A CA  1 
ATOM   1626 C  C   . THR A  1 199 ? 19.896  8.088   10.151  1.00 10.15 ? 199 THR A C   1 
ATOM   1627 O  O   . THR A  1 199 ? 20.607  8.036   9.127   1.00 10.64 ? 199 THR A O   1 
ATOM   1628 C  CB  . THR A  1 199 ? 20.460  6.779   12.145  1.00 12.93 ? 199 THR A CB  1 
ATOM   1629 O  OG1 . THR A  1 199 ? 21.771  6.946   11.715  1.00 18.09 ? 199 THR A OG1 1 
ATOM   1630 C  CG2 . THR A  1 199 ? 20.376  5.449   12.959  1.00 12.39 ? 199 THR A CG2 1 
ATOM   1631 N  N   . PRO A  1 200 ? 19.375  9.210   10.687  1.00 9.93  ? 200 PRO A N   1 
ATOM   1632 C  CA  . PRO A  1 200 ? 19.776  10.530  10.112  1.00 10.38 ? 200 PRO A CA  1 
ATOM   1633 C  C   . PRO A  1 200 ? 21.337  10.629  9.981   1.00 10.65 ? 200 PRO A C   1 
ATOM   1634 O  O   . PRO A  1 200 ? 22.032  10.084  10.912  1.00 12.89 ? 200 PRO A O   1 
ATOM   1635 C  CB  . PRO A  1 200 ? 19.247  11.501  11.189  1.00 10.58 ? 200 PRO A CB  1 
ATOM   1636 C  CG  . PRO A  1 200 ? 17.999  10.862  11.697  1.00 10.08 ? 200 PRO A CG  1 
ATOM   1637 C  CD  . PRO A  1 200 ? 18.418  9.379   11.804  1.00 10.74 ? 200 PRO A CD  1 
ATOM   1638 N  N   . PRO A  1 201 ? 21.819  11.111  8.854   1.00 10.20 ? 201 PRO A N   1 
ATOM   1639 C  CA  . PRO A  1 201 ? 21.103  11.860  7.835   1.00 9.81  ? 201 PRO A CA  1 
ATOM   1640 C  C   . PRO A  1 201 ? 20.486  11.004  6.730   1.00 9.82  ? 201 PRO A C   1 
ATOM   1641 O  O   . PRO A  1 201 ? 20.011  11.554  5.738   1.00 10.65 ? 201 PRO A O   1 
ATOM   1642 C  CB  . PRO A  1 201 ? 22.162  12.787  7.181   1.00 10.55 ? 201 PRO A CB  1 
ATOM   1643 C  CG  . PRO A  1 201 ? 23.384  12.589  7.995   1.00 14.74 ? 201 PRO A CG  1 
ATOM   1644 C  CD  . PRO A  1 201 ? 23.274  11.289  8.721   1.00 11.01 ? 201 PRO A CD  1 
ATOM   1645 N  N   . CYS A  1 202 ? 20.531  9.663   6.844   1.00 10.40 ? 202 CYS A N   1 
ATOM   1646 C  CA  . CYS A  1 202 ? 19.861  8.715   5.874   1.00 8.88  ? 202 CYS A CA  1 
ATOM   1647 C  C   . CYS A  1 202 ? 20.406  8.771   4.483   1.00 9.26  ? 202 CYS A C   1 
ATOM   1648 O  O   . CYS A  1 202 ? 19.725  8.498   3.512   1.00 9.80  ? 202 CYS A O   1 
ATOM   1649 C  CB  . CYS A  1 202 ? 18.301  8.970   5.820   1.00 9.63  ? 202 CYS A CB  1 
ATOM   1650 S  SG  . CYS A  1 202 ? 17.439  8.915   7.423   1.00 10.11 ? 202 CYS A SG  1 
ATOM   1651 N  N   . ASN A  1 203 ? 21.716  9.099   4.375   1.00 10.26 ? 203 ASN A N   1 
ATOM   1652 C  CA  . ASN A  1 203 ? 22.269  9.268   3.036   1.00 11.32 ? 203 ASN A CA  1 
ATOM   1653 C  C   . ASN A  1 203 ? 22.148  7.970   2.265   1.00 10.86 ? 203 ASN A C   1 
ATOM   1654 O  O   . ASN A  1 203 ? 22.448  6.860   2.798   1.00 9.36  ? 203 ASN A O   1 
ATOM   1655 C  CB  . ASN A  1 203 ? 23.782  9.591   3.125   1.00 13.58 ? 203 ASN A CB  1 
ATOM   1656 C  CG  . ASN A  1 203 ? 24.010  10.789  3.991   1.00 17.24 ? 203 ASN A CG  1 
ATOM   1657 O  OD1 . ASN A  1 203 ? 23.906  10.670  5.227   1.00 20.69 ? 203 ASN A OD1 1 
ATOM   1658 N  ND2 . ASN A  1 203 ? 23.990  11.969  3.353   1.00 25.94 ? 203 ASN A ND2 1 
ATOM   1659 N  N   . PRO A  1 204 ? 21.759  8.042   0.979   1.00 11.13 ? 204 PRO A N   1 
ATOM   1660 C  CA  . PRO A  1 204 ? 21.560  6.869   0.152   1.00 11.35 ? 204 PRO A CA  1 
ATOM   1661 C  C   . PRO A  1 204 ? 22.847  6.394   -0.463  1.00 11.35 ? 204 PRO A C   1 
ATOM   1662 O  O   . PRO A  1 204 ? 22.951  6.260   -1.690  1.00 13.70 ? 204 PRO A O   1 
ATOM   1663 C  CB  . PRO A  1 204 ? 20.575  7.364   -0.968  1.00 12.47 ? 204 PRO A CB  1 
ATOM   1664 C  CG  . PRO A  1 204 ? 20.940  8.863   -1.135  1.00 12.85 ? 204 PRO A CG  1 
ATOM   1665 C  CD  . PRO A  1 204 ? 21.268  9.317   0.288   1.00 11.08 ? 204 PRO A CD  1 
ATOM   1666 N  N   . THR A  1 205 ? 23.823  6.126   0.364   1.00 11.33 ? 205 THR A N   1 
ATOM   1667 C  CA  . THR A  1 205 ? 25.181  5.885   -0.153  1.00 11.42 ? 205 THR A CA  1 
ATOM   1668 C  C   . THR A  1 205 ? 25.759  4.596   0.400   1.00 11.97 ? 205 THR A C   1 
ATOM   1669 O  O   . THR A  1 205 ? 26.989  4.421   0.389   1.00 11.16 ? 205 THR A O   1 
ATOM   1670 C  CB  . THR A  1 205 ? 26.078  7.024   0.388   1.00 11.08 ? 205 THR A CB  1 
ATOM   1671 O  OG1 . THR A  1 205 ? 25.897  7.142   1.778   1.00 11.98 ? 205 THR A OG1 1 
ATOM   1672 C  CG2 . THR A  1 205 ? 25.652  8.401   -0.317  1.00 14.23 ? 205 THR A CG2 1 
ATOM   1673 N  N   . VAL A  1 206 ? 24.898  3.661   0.897   1.00 10.00 ? 206 VAL A N   1 
ATOM   1674 C  CA  . VAL A  1 206 ? 25.394  2.430   1.506   1.00 9.48  ? 206 VAL A CA  1 
ATOM   1675 C  C   . VAL A  1 206 ? 25.223  1.255   0.642   1.00 9.42  ? 206 VAL A C   1 
ATOM   1676 O  O   . VAL A  1 206 ? 24.105  0.926   0.195   1.00 11.38 ? 206 VAL A O   1 
ATOM   1677 C  CB  . VAL A  1 206 ? 24.638  2.216   2.879   1.00 9.06  ? 206 VAL A CB  1 
ATOM   1678 C  CG1 . VAL A  1 206 ? 25.083  0.876   3.495   1.00 9.10  ? 206 VAL A CG1 1 
ATOM   1679 C  CG2 . VAL A  1 206 ? 24.845  3.372   3.831   1.00 9.59  ? 206 VAL A CG2 1 
ATOM   1680 N  N   . LEU A  1 207 ? 26.266  0.487   0.432   1.00 9.45  ? 207 LEU A N   1 
ATOM   1681 C  CA  . LEU A  1 207 ? 26.208  -0.843  -0.146  1.00 10.23 ? 207 LEU A CA  1 
ATOM   1682 C  C   . LEU A  1 207 ? 26.042  -1.807  1.046   1.00 9.62  ? 207 LEU A C   1 
ATOM   1683 O  O   . LEU A  1 207 ? 26.903  -1.930  1.944   1.00 10.52 ? 207 LEU A O   1 
ATOM   1684 C  CB  . LEU A  1 207 ? 27.482  -1.176  -0.897  1.00 12.51 ? 207 LEU A CB  1 
ATOM   1685 C  CG  . LEU A  1 207 ? 27.379  -2.506  -1.622  1.00 14.70 ? 207 LEU A CG  1 
ATOM   1686 C  CD1 . LEU A  1 207 ? 26.458  -2.316  -2.869  1.00 17.96 ? 207 LEU A CD1 1 
ATOM   1687 C  CD2 . LEU A  1 207 ? 28.729  -2.924  -2.179  1.00 20.75 ? 207 LEU A CD2 1 
ATOM   1688 N  N   . TRP A  1 208 ? 24.828  -2.379  1.129   1.00 9.30  ? 208 TRP A N   1 
ATOM   1689 C  CA  . TRP A  1 208 ? 24.436  -3.296  2.259   1.00 8.74  ? 208 TRP A CA  1 
ATOM   1690 C  C   . TRP A  1 208 ? 24.843  -4.713  1.957   1.00 9.09  ? 208 TRP A C   1 
ATOM   1691 O  O   . TRP A  1 208 ? 24.610  -5.235  0.844   1.00 9.46  ? 208 TRP A O   1 
ATOM   1692 C  CB  . TRP A  1 208 ? 22.896  -3.231  2.496   1.00 8.98  ? 208 TRP A CB  1 
ATOM   1693 C  CG  . TRP A  1 208 ? 22.554  -2.070  3.305   1.00 8.33  ? 208 TRP A CG  1 
ATOM   1694 C  CD1 . TRP A  1 208 ? 22.057  -0.842  2.862   1.00 8.15  ? 208 TRP A CD1 1 
ATOM   1695 C  CD2 . TRP A  1 208 ? 22.666  -1.923  4.748   1.00 8.61  ? 208 TRP A CD2 1 
ATOM   1696 N  NE1 . TRP A  1 208 ? 21.884  0.002   3.869   1.00 8.70  ? 208 TRP A NE1 1 
ATOM   1697 C  CE2 . TRP A  1 208 ? 22.228  -0.603  5.076   1.00 8.54  ? 208 TRP A CE2 1 
ATOM   1698 C  CE3 . TRP A  1 208 ? 23.078  -2.785  5.765   1.00 8.82  ? 208 TRP A CE3 1 
ATOM   1699 C  CZ2 . TRP A  1 208 ? 22.228  -0.128  6.386   1.00 9.03  ? 208 TRP A CZ2 1 
ATOM   1700 C  CZ3 . TRP A  1 208 ? 23.070  -2.300  7.067   1.00 8.60  ? 208 TRP A CZ3 1 
ATOM   1701 C  CH2 . TRP A  1 208 ? 22.678  -0.972  7.374   1.00 10.57 ? 208 TRP A CH2 1 
ATOM   1702 N  N   . THR A  1 209 ? 25.402  -5.382  2.974   1.00 8.59  ? 209 THR A N   1 
ATOM   1703 C  CA  . THR A  1 209 ? 25.626  -6.793  2.953   1.00 8.92  ? 209 THR A CA  1 
ATOM   1704 C  C   . THR A  1 209 ? 24.940  -7.342  4.204   1.00 8.80  ? 209 THR A C   1 
ATOM   1705 O  O   . THR A  1 209 ? 25.442  -7.018  5.301   1.00 10.00 ? 209 THR A O   1 
ATOM   1706 C  CB  . THR A  1 209 ? 27.132  -7.194  2.932   1.00 9.07  ? 209 THR A CB  1 
ATOM   1707 O  OG1 . THR A  1 209 ? 27.719  -6.636  1.724   1.00 10.55 ? 209 THR A OG1 1 
ATOM   1708 C  CG2 . THR A  1 209 ? 27.311  -8.708  2.898   1.00 10.65 ? 209 THR A CG2 1 
ATOM   1709 N  N   . VAL A  1 210 ? 23.861  -8.139  4.031   1.00 8.28  ? 210 VAL A N   1 
ATOM   1710 C  CA  . VAL A  1 210 ? 23.180  -8.694  5.216   1.00 8.35  ? 210 VAL A CA  1 
ATOM   1711 C  C   . VAL A  1 210 ? 23.457  -10.181 5.151   1.00 8.03  ? 210 VAL A C   1 
ATOM   1712 O  O   . VAL A  1 210 ? 23.073  -10.832 4.170   1.00 9.59  ? 210 VAL A O   1 
ATOM   1713 C  CB  . VAL A  1 210 ? 21.633  -8.391  5.168   1.00 8.37  ? 210 VAL A CB  1 
ATOM   1714 C  CG1 . VAL A  1 210 ? 21.020  -9.046  6.473   1.00 9.31  ? 210 VAL A CG1 1 
ATOM   1715 C  CG2 . VAL A  1 210 ? 21.345  -6.894  5.002   1.00 9.23  ? 210 VAL A CG2 1 
ATOM   1716 N  N   . PHE A  1 211 ? 24.170  -10.709 6.131   1.00 8.24  ? 211 PHE A N   1 
ATOM   1717 C  CA  . PHE A  1 211 ? 24.446  -12.161 6.083   1.00 8.98  ? 211 PHE A CA  1 
ATOM   1718 C  C   . PHE A  1 211 ? 23.169  -12.951 6.215   1.00 9.19  ? 211 PHE A C   1 
ATOM   1719 O  O   . PHE A  1 211 ? 22.248  -12.614 6.990   1.00 9.54  ? 211 PHE A O   1 
ATOM   1720 C  CB  . PHE A  1 211 ? 25.492  -12.522 7.157   1.00 8.18  ? 211 PHE A CB  1 
ATOM   1721 C  CG  . PHE A  1 211 ? 26.787  -11.850 6.929   1.00 9.03  ? 211 PHE A CG  1 
ATOM   1722 C  CD1 . PHE A  1 211 ? 27.586  -12.296 5.875   1.00 9.61  ? 211 PHE A CD1 1 
ATOM   1723 C  CD2 . PHE A  1 211 ? 27.246  -10.800 7.760   1.00 9.91  ? 211 PHE A CD2 1 
ATOM   1724 C  CE1 . PHE A  1 211 ? 28.815  -11.615 5.596   1.00 12.70 ? 211 PHE A CE1 1 
ATOM   1725 C  CE2 . PHE A  1 211 ? 28.509  -10.180 7.474   1.00 10.30 ? 211 PHE A CE2 1 
ATOM   1726 C  CZ  . PHE A  1 211 ? 29.245  -10.589 6.407   1.00 10.19 ? 211 PHE A CZ  1 
ATOM   1727 N  N   A ARG A  1 212 ? 23.143  -14.059 5.466   0.50 9.64  ? 212 ARG A N   1 
ATOM   1728 N  N   B ARG A  1 212 ? 23.084  -14.046 5.462   0.50 10.05 ? 212 ARG A N   1 
ATOM   1729 C  CA  A ARG A  1 212 ? 22.012  -14.989 5.428   0.50 9.40  ? 212 ARG A CA  1 
ATOM   1730 C  CA  B ARG A  1 212 ? 21.898  -14.904 5.500   0.50 10.07 ? 212 ARG A CA  1 
ATOM   1731 C  C   A ARG A  1 212 ? 21.682  -15.597 6.779   0.50 10.29 ? 212 ARG A C   1 
ATOM   1732 C  C   B ARG A  1 212 ? 21.670  -15.513 6.900   0.50 10.75 ? 212 ARG A C   1 
ATOM   1733 O  O   A ARG A  1 212 ? 20.461  -15.693 7.106   0.50 10.66 ? 212 ARG A O   1 
ATOM   1734 O  O   B ARG A  1 212 ? 20.538  -15.561 7.396   0.50 11.94 ? 212 ARG A O   1 
ATOM   1735 C  CB  A ARG A  1 212 ? 22.225  -16.111 4.408   0.50 9.78  ? 212 ARG A CB  1 
ATOM   1736 C  CB  B ARG A  1 212 ? 21.950  -15.997 4.393   0.50 10.95 ? 212 ARG A CB  1 
ATOM   1737 C  CG  A ARG A  1 212 ? 21.092  -17.117 4.436   0.50 10.70 ? 212 ARG A CG  1 
ATOM   1738 C  CG  B ARG A  1 212 ? 20.639  -16.766 4.220   0.50 12.43 ? 212 ARG A CG  1 
ATOM   1739 C  CD  A ARG A  1 212 ? 21.483  -18.365 3.656   0.50 11.77 ? 212 ARG A CD  1 
ATOM   1740 C  CD  B ARG A  1 212 ? 20.901  -17.981 3.374   0.50 14.85 ? 212 ARG A CD  1 
ATOM   1741 N  NE  A ARG A  1 212 ? 20.331  -19.230 3.425   0.50 12.80 ? 212 ARG A NE  1 
ATOM   1742 N  NE  B ARG A  1 212 ? 19.665  -18.538 2.831   0.50 17.77 ? 212 ARG A NE  1 
ATOM   1743 C  CZ  A ARG A  1 212 ? 19.933  -20.181 4.263   0.50 14.48 ? 212 ARG A CZ  1 
ATOM   1744 C  CZ  B ARG A  1 212 ? 19.610  -19.600 2.035   0.50 18.46 ? 212 ARG A CZ  1 
ATOM   1745 N  NH1 A ARG A  1 212 ? 20.600  -20.397 5.389   0.50 14.89 ? 212 ARG A NH1 1 
ATOM   1746 N  NH1 B ARG A  1 212 ? 20.724  -20.227 1.682   0.50 22.12 ? 212 ARG A NH1 1 
ATOM   1747 N  NH2 A ARG A  1 212 ? 18.869  -20.920 3.976   0.50 16.60 ? 212 ARG A NH2 1 
ATOM   1748 N  NH2 B ARG A  1 212 ? 18.439  -20.036 1.590   0.50 18.87 ? 212 ARG A NH2 1 
ATOM   1749 N  N   . ASN A  1 213 ? 22.735  -15.991 7.517   1.00 10.11 ? 213 ASN A N   1 
ATOM   1750 C  CA  . ASN A  1 213 ? 22.519  -16.761 8.784   1.00 12.32 ? 213 ASN A CA  1 
ATOM   1751 C  C   . ASN A  1 213 ? 22.637  -15.831 9.995   1.00 11.55 ? 213 ASN A C   1 
ATOM   1752 O  O   . ASN A  1 213 ? 23.578  -15.041 10.052  1.00 10.94 ? 213 ASN A O   1 
ATOM   1753 C  CB  . ASN A  1 213 ? 23.558  -17.924 8.795   1.00 13.50 ? 213 ASN A CB  1 
ATOM   1754 C  CG  . ASN A  1 213 ? 23.426  -18.756 7.578   1.00 15.36 ? 213 ASN A CG  1 
ATOM   1755 O  OD1 . ASN A  1 213 ? 22.297  -19.099 7.186   1.00 18.68 ? 213 ASN A OD1 1 
ATOM   1756 N  ND2 . ASN A  1 213 ? 24.516  -18.950 6.836   1.00 16.93 ? 213 ASN A ND2 1 
ATOM   1757 N  N   . PRO A  1 214 ? 21.782  -16.000 11.026  1.00 11.81 ? 214 PRO A N   1 
ATOM   1758 C  CA  . PRO A  1 214 ? 21.880  -15.223 12.206  1.00 11.08 ? 214 PRO A CA  1 
ATOM   1759 C  C   . PRO A  1 214 ? 22.978  -15.784 13.157  1.00 11.53 ? 214 PRO A C   1 
ATOM   1760 O  O   . PRO A  1 214 ? 23.364  -17.010 13.014  1.00 12.51 ? 214 PRO A O   1 
ATOM   1761 C  CB  . PRO A  1 214 ? 20.480  -15.445 12.910  1.00 14.62 ? 214 PRO A CB  1 
ATOM   1762 C  CG  . PRO A  1 214 ? 20.074  -16.777 12.398  1.00 16.38 ? 214 PRO A CG  1 
ATOM   1763 C  CD  . PRO A  1 214 ? 20.575  -16.831 10.972  1.00 14.97 ? 214 PRO A CD  1 
ATOM   1764 N  N   . VAL A  1 215 ? 23.354  -15.005 14.110  1.00 11.31 ? 215 VAL A N   1 
ATOM   1765 C  CA  . VAL A  1 215 ? 24.094  -15.486 15.296  1.00 11.50 ? 215 VAL A CA  1 
ATOM   1766 C  C   . VAL A  1 215 ? 23.116  -15.657 16.446  1.00 12.13 ? 215 VAL A C   1 
ATOM   1767 O  O   . VAL A  1 215 ? 21.998  -15.153 16.381  1.00 12.67 ? 215 VAL A O   1 
ATOM   1768 C  CB  . VAL A  1 215 ? 25.272  -14.580 15.660  1.00 11.84 ? 215 VAL A CB  1 
ATOM   1769 C  CG1 . VAL A  1 215 ? 26.271  -14.451 14.490  1.00 12.19 ? 215 VAL A CG1 1 
ATOM   1770 C  CG2 . VAL A  1 215 ? 24.792  -13.201 16.082  1.00 12.11 ? 215 VAL A CG2 1 
ATOM   1771 N  N   . GLN A  1 216 ? 23.566  -16.344 17.482  1.00 12.98 ? 216 GLN A N   1 
ATOM   1772 C  CA  . GLN A  1 216 ? 22.796  -16.457 18.756  1.00 13.54 ? 216 GLN A CA  1 
ATOM   1773 C  C   . GLN A  1 216 ? 23.441  -15.857 19.883  1.00 15.96 ? 216 GLN A C   1 
ATOM   1774 O  O   . GLN A  1 216 ? 24.655  -15.914 20.007  1.00 15.02 ? 216 GLN A O   1 
ATOM   1775 C  CB  . GLN A  1 216 ? 22.513  -17.959 19.079  1.00 15.44 ? 216 GLN A CB  1 
ATOM   1776 C  CG  . GLN A  1 216 ? 21.743  -18.675 18.063  1.00 17.68 ? 216 GLN A CG  1 
ATOM   1777 C  CD  . GLN A  1 216 ? 21.345  -20.081 18.491  1.00 25.59 ? 216 GLN A CD  1 
ATOM   1778 O  OE1 . GLN A  1 216 ? 21.835  -20.679 19.520  1.00 29.99 ? 216 GLN A OE1 1 
ATOM   1779 N  NE2 . GLN A  1 216 ? 20.393  -20.618 17.720  1.00 31.13 ? 216 GLN A NE2 1 
ATOM   1780 N  N   . ILE A  1 217 ? 22.661  -15.182 20.760  1.00 13.58 ? 217 ILE A N   1 
ATOM   1781 C  CA  . ILE A  1 217 ? 23.071  -14.703 22.082  1.00 13.70 ? 217 ILE A CA  1 
ATOM   1782 C  C   . ILE A  1 217 ? 22.049  -15.243 23.091  1.00 12.58 ? 217 ILE A C   1 
ATOM   1783 O  O   . ILE A  1 217 ? 20.929  -15.565 22.726  1.00 13.26 ? 217 ILE A O   1 
ATOM   1784 C  CB  . ILE A  1 217 ? 23.237  -13.154 22.118  1.00 13.02 ? 217 ILE A CB  1 
ATOM   1785 C  CG1 . ILE A  1 217 ? 21.835  -12.420 21.928  1.00 13.08 ? 217 ILE A CG1 1 
ATOM   1786 C  CG2 . ILE A  1 217 ? 24.296  -12.715 21.050  1.00 14.16 ? 217 ILE A CG2 1 
ATOM   1787 C  CD1 . ILE A  1 217 ? 21.903  -10.963 22.154  1.00 13.82 ? 217 ILE A CD1 1 
ATOM   1788 N  N   . SER A  1 218 ? 22.487  -15.294 24.368  1.00 14.77 ? 218 SER A N   1 
ATOM   1789 C  CA  . SER A  1 218 ? 21.494  -15.910 25.282  1.00 15.03 ? 218 SER A CA  1 
ATOM   1790 C  C   . SER A  1 218 ? 20.422  -14.908 25.672  1.00 15.18 ? 218 SER A C   1 
ATOM   1791 O  O   . SER A  1 218 ? 20.516  -13.695 25.415  1.00 13.45 ? 218 SER A O   1 
ATOM   1792 C  CB  . SER A  1 218 ? 22.192  -16.282 26.554  1.00 14.96 ? 218 SER A CB  1 
ATOM   1793 O  OG  . SER A  1 218 ? 22.639  -15.157 27.286  1.00 16.49 ? 218 SER A OG  1 
ATOM   1794 N  N   . GLN A  1 219 ? 19.373  -15.471 26.313  1.00 17.02 ? 219 GLN A N   1 
ATOM   1795 C  CA  . GLN A  1 219 ? 18.351  -14.547 26.792  1.00 17.63 ? 219 GLN A CA  1 
ATOM   1796 C  C   . GLN A  1 219 ? 18.853  -13.543 27.763  1.00 15.70 ? 219 GLN A C   1 
ATOM   1797 O  O   . GLN A  1 219 ? 18.418  -12.405 27.706  1.00 15.48 ? 219 GLN A O   1 
ATOM   1798 C  CB  . GLN A  1 219 ? 17.202  -15.369 27.359  1.00 22.60 ? 219 GLN A CB  1 
ATOM   1799 C  CG  . GLN A  1 219 ? 17.581  -16.319 28.437  1.00 28.39 ? 219 GLN A CG  1 
ATOM   1800 C  CD  . GLN A  1 219 ? 16.300  -16.942 28.976  1.00 40.88 ? 219 GLN A CD  1 
ATOM   1801 O  OE1 . GLN A  1 219 ? 15.696  -17.795 28.308  1.00 41.53 ? 219 GLN A OE1 1 
ATOM   1802 N  NE2 . GLN A  1 219 ? 15.843  -16.466 30.171  1.00 43.10 ? 219 GLN A NE2 1 
ATOM   1803 N  N   . GLU A  1 220 ? 19.802  -13.872 28.599  1.00 16.06 ? 220 GLU A N   1 
ATOM   1804 C  CA  . GLU A  1 220 ? 20.273  -12.969 29.513  1.00 15.57 ? 220 GLU A CA  1 
ATOM   1805 C  C   . GLU A  1 220 ? 21.134  -11.871 28.814  1.00 16.52 ? 220 GLU A C   1 
ATOM   1806 O  O   . GLU A  1 220 ? 21.070  -10.701 29.173  1.00 15.26 ? 220 GLU A O   1 
ATOM   1807 C  CB  . GLU A  1 220 ? 21.148  -13.638 30.588  1.00 17.12 ? 220 GLU A CB  1 
ATOM   1808 C  CG  . GLU A  1 220 ? 20.372  -14.571 31.521  1.00 21.39 ? 220 GLU A CG  1 
ATOM   1809 C  CD  . GLU A  1 220 ? 20.124  -15.972 30.950  1.00 26.15 ? 220 GLU A CD  1 
ATOM   1810 O  OE1 . GLU A  1 220 ? 20.679  -16.402 29.888  1.00 22.61 ? 220 GLU A OE1 1 
ATOM   1811 O  OE2 . GLU A  1 220 ? 19.322  -16.718 31.574  1.00 32.02 ? 220 GLU A OE2 1 
ATOM   1812 N  N   . GLN A  1 221 ? 21.870  -12.258 27.760  1.00 14.63 ? 221 GLN A N   1 
ATOM   1813 C  CA  . GLN A  1 221 ? 22.644  -11.247 26.995  1.00 13.42 ? 221 GLN A CA  1 
ATOM   1814 C  C   . GLN A  1 221 ? 21.685  -10.251 26.256  1.00 13.37 ? 221 GLN A C   1 
ATOM   1815 O  O   . GLN A  1 221 ? 21.946  -9.077  26.314  1.00 13.20 ? 221 GLN A O   1 
ATOM   1816 C  CB  . GLN A  1 221 ? 23.495  -11.935 25.945  1.00 14.02 ? 221 GLN A CB  1 
ATOM   1817 C  CG  . GLN A  1 221 ? 24.719  -12.672 26.574  1.00 14.20 ? 221 GLN A CG  1 
ATOM   1818 C  CD  . GLN A  1 221 ? 25.532  -13.293 25.488  1.00 11.89 ? 221 GLN A CD  1 
ATOM   1819 O  OE1 . GLN A  1 221 ? 25.145  -14.200 24.837  1.00 14.95 ? 221 GLN A OE1 1 
ATOM   1820 N  NE2 . GLN A  1 221 ? 26.785  -12.869 25.440  1.00 15.17 ? 221 GLN A NE2 1 
ATOM   1821 N  N   . LEU A  1 222 ? 20.637  -10.793 25.691  1.00 12.47 ? 222 LEU A N   1 
ATOM   1822 C  CA  . LEU A  1 222 ? 19.656  -9.946  24.961  1.00 13.02 ? 222 LEU A CA  1 
ATOM   1823 C  C   . LEU A  1 222 ? 18.968  -9.026  25.957  1.00 13.11 ? 222 LEU A C   1 
ATOM   1824 O  O   . LEU A  1 222 ? 18.809  -7.823  25.745  1.00 11.84 ? 222 LEU A O   1 
ATOM   1825 C  CB  . LEU A  1 222 ? 18.633  -10.747 24.214  1.00 12.25 ? 222 LEU A CB  1 
ATOM   1826 C  CG  . LEU A  1 222 ? 17.500  -9.973  23.560  1.00 14.16 ? 222 LEU A CG  1 
ATOM   1827 C  CD1 . LEU A  1 222 ? 18.113  -9.021  22.485  1.00 14.58 ? 222 LEU A CD1 1 
ATOM   1828 C  CD2 . LEU A  1 222 ? 16.549  -10.974 22.965  1.00 15.38 ? 222 LEU A CD2 1 
ATOM   1829 N  N   . LEU A  1 223 ? 18.566  -9.565  27.141  1.00 11.61 ? 223 LEU A N   1 
ATOM   1830 C  CA  . LEU A  1 223 ? 18.022  -8.682  28.206  1.00 12.91 ? 223 LEU A CA  1 
ATOM   1831 C  C   . LEU A  1 223 ? 18.981  -7.596  28.656  1.00 12.98 ? 223 LEU A C   1 
ATOM   1832 O  O   . LEU A  1 223 ? 18.555  -6.468  28.845  1.00 14.87 ? 223 LEU A O   1 
ATOM   1833 C  CB  . LEU A  1 223 ? 17.593  -9.526  29.400  1.00 15.59 ? 223 LEU A CB  1 
ATOM   1834 C  CG  . LEU A  1 223 ? 16.871  -8.789  30.459  1.00 15.62 ? 223 LEU A CG  1 
ATOM   1835 C  CD1 . LEU A  1 223 ? 15.486  -8.310  29.962  1.00 17.04 ? 223 LEU A CD1 1 
ATOM   1836 C  CD2 . LEU A  1 223 ? 16.752  -9.819  31.615  1.00 18.02 ? 223 LEU A CD2 1 
ATOM   1837 N  N   . ALA A  1 224 ? 20.282  -7.917  28.801  1.00 13.57 ? 224 ALA A N   1 
ATOM   1838 C  CA  . ALA A  1 224 ? 21.177  -6.863  29.185  1.00 13.88 ? 224 ALA A CA  1 
ATOM   1839 C  C   . ALA A  1 224 ? 21.301  -5.745  28.166  1.00 15.23 ? 224 ALA A C   1 
ATOM   1840 O  O   . ALA A  1 224 ? 21.313  -4.573  28.517  1.00 15.74 ? 224 ALA A O   1 
ATOM   1841 C  CB  . ALA A  1 224 ? 22.573  -7.492  29.443  1.00 14.94 ? 224 ALA A CB  1 
ATOM   1842 N  N   . LEU A  1 225 ? 21.397  -6.153  26.901  1.00 12.56 ? 225 LEU A N   1 
ATOM   1843 C  CA  . LEU A  1 225 ? 21.434  -5.109  25.871  1.00 14.20 ? 225 LEU A CA  1 
ATOM   1844 C  C   . LEU A  1 225 ? 20.179  -4.223  25.904  1.00 14.16 ? 225 LEU A C   1 
ATOM   1845 O  O   . LEU A  1 225 ? 20.310  -2.985  25.697  1.00 16.36 ? 225 LEU A O   1 
ATOM   1846 C  CB  . LEU A  1 225 ? 21.531  -5.829  24.525  1.00 12.12 ? 225 LEU A CB  1 
ATOM   1847 C  CG  . LEU A  1 225 ? 21.614  -4.917  23.290  1.00 12.67 ? 225 LEU A CG  1 
ATOM   1848 C  CD1 . LEU A  1 225 ? 22.866  -4.032  23.370  1.00 15.08 ? 225 LEU A CD1 1 
ATOM   1849 C  CD2 . LEU A  1 225 ? 21.613  -5.803  22.070  1.00 13.70 ? 225 LEU A CD2 1 
ATOM   1850 N  N   . GLU A  1 226 ? 19.016  -4.859  26.119  1.00 12.89 ? 226 GLU A N   1 
ATOM   1851 C  CA  . GLU A  1 226 ? 17.782  -4.066  26.127  1.00 13.41 ? 226 GLU A CA  1 
ATOM   1852 C  C   . GLU A  1 226 ? 17.583  -3.151  27.279  1.00 16.40 ? 226 GLU A C   1 
ATOM   1853 O  O   . GLU A  1 226 ? 16.761  -2.262  27.242  1.00 16.63 ? 226 GLU A O   1 
ATOM   1854 C  CB  . GLU A  1 226 ? 16.595  -5.031  26.072  1.00 12.70 ? 226 GLU A CB  1 
ATOM   1855 C  CG  . GLU A  1 226 ? 16.488  -5.798  24.720  1.00 11.78 ? 226 GLU A CG  1 
ATOM   1856 C  CD  . GLU A  1 226 ? 15.529  -6.948  24.761  1.00 13.38 ? 226 GLU A CD  1 
ATOM   1857 O  OE1 . GLU A  1 226 ? 15.285  -7.471  25.904  1.00 15.55 ? 226 GLU A OE1 1 
ATOM   1858 O  OE2 . GLU A  1 226 ? 15.035  -7.449  23.742  1.00 15.41 ? 226 GLU A OE2 1 
ATOM   1859 N  N   . THR A  1 227 ? 18.258  -3.443  28.390  1.00 15.02 ? 227 THR A N   1 
ATOM   1860 C  CA  . THR A  1 227 ? 17.944  -2.797  29.687  1.00 15.73 ? 227 THR A CA  1 
ATOM   1861 C  C   . THR A  1 227 ? 19.162  -2.002  30.235  1.00 16.81 ? 227 THR A C   1 
ATOM   1862 O  O   . THR A  1 227 ? 18.990  -1.287  31.245  1.00 18.66 ? 227 THR A O   1 
ATOM   1863 C  CB  . THR A  1 227 ? 17.536  -3.826  30.792  1.00 16.17 ? 227 THR A CB  1 
ATOM   1864 O  OG1 . THR A  1 227 ? 18.571  -4.751  30.999  1.00 16.42 ? 227 THR A OG1 1 
ATOM   1865 C  CG2 . THR A  1 227 ? 16.243  -4.502  30.443  1.00 16.09 ? 227 THR A CG2 1 
ATOM   1866 N  N   . ALA A  1 228 ? 20.337  -2.084  29.624  1.00 15.83 ? 228 ALA A N   1 
ATOM   1867 C  CA  . ALA A  1 228 ? 21.537  -1.480  30.247  1.00 17.93 ? 228 ALA A CA  1 
ATOM   1868 C  C   . ALA A  1 228 ? 21.619  -0.006  30.004  1.00 18.08 ? 228 ALA A C   1 
ATOM   1869 O  O   . ALA A  1 228 ? 22.329  0.711   30.771  1.00 18.50 ? 228 ALA A O   1 
ATOM   1870 C  CB  . ALA A  1 228 ? 22.796  -2.223  29.807  1.00 18.11 ? 228 ALA A CB  1 
ATOM   1871 N  N   . LEU A  1 229 ? 21.008  0.503   28.893  1.00 13.43 ? 229 LEU A N   1 
ATOM   1872 C  CA  . LEU A  1 229 ? 21.314  1.859   28.443  1.00 16.88 ? 229 LEU A CA  1 
ATOM   1873 C  C   . LEU A  1 229 ? 20.188  2.810   28.415  1.00 16.77 ? 229 LEU A C   1 
ATOM   1874 O  O   . LEU A  1 229 ? 19.030  2.426   28.215  1.00 15.12 ? 229 LEU A O   1 
ATOM   1875 C  CB  . LEU A  1 229 ? 21.955  1.797   27.039  1.00 15.82 ? 229 LEU A CB  1 
ATOM   1876 C  CG  . LEU A  1 229 ? 23.005  0.662   26.801  1.00 18.77 ? 229 LEU A CG  1 
ATOM   1877 C  CD1 . LEU A  1 229 ? 23.426  0.720   25.326  1.00 21.83 ? 229 LEU A CD1 1 
ATOM   1878 C  CD2 . LEU A  1 229 ? 24.235  0.851   27.710  1.00 19.12 ? 229 LEU A CD2 1 
ATOM   1879 N  N   . TYR A  1 230 ? 20.518  4.065   28.616  1.00 16.22 ? 230 TYR A N   1 
ATOM   1880 C  CA  . TYR A  1 230 ? 19.636  5.190   28.427  1.00 17.44 ? 230 TYR A CA  1 
ATOM   1881 C  C   . TYR A  1 230 ? 20.084  6.113   27.297  1.00 16.57 ? 230 TYR A C   1 
ATOM   1882 O  O   . TYR A  1 230 ? 21.254  6.220   26.988  1.00 17.05 ? 230 TYR A O   1 
ATOM   1883 C  CB  . TYR A  1 230 ? 19.562  6.066   29.734  1.00 20.85 ? 230 TYR A CB  1 
ATOM   1884 C  CG  . TYR A  1 230 ? 18.940  5.355   30.908  1.00 25.10 ? 230 TYR A CG  1 
ATOM   1885 C  CD1 . TYR A  1 230 ? 17.662  5.679   31.350  1.00 30.41 ? 230 TYR A CD1 1 
ATOM   1886 C  CD2 . TYR A  1 230 ? 19.659  4.365   31.609  1.00 29.81 ? 230 TYR A CD2 1 
ATOM   1887 C  CE1 . TYR A  1 230 ? 17.095  5.047   32.446  1.00 31.74 ? 230 TYR A CE1 1 
ATOM   1888 C  CE2 . TYR A  1 230 ? 19.087  3.724   32.710  1.00 38.75 ? 230 TYR A CE2 1 
ATOM   1889 C  CZ  . TYR A  1 230 ? 17.804  4.083   33.119  1.00 37.65 ? 230 TYR A CZ  1 
ATOM   1890 O  OH  . TYR A  1 230 ? 17.237  3.455   34.224  1.00 40.97 ? 230 TYR A OH  1 
ATOM   1891 N  N   A CYS A  1 231 ? 19.130  6.869   26.742  0.50 16.32 ? 231 CYS A N   1 
ATOM   1892 N  N   B CYS A  1 231 ? 19.124  6.838   26.736  0.50 19.93 ? 231 CYS A N   1 
ATOM   1893 C  CA  A CYS A  1 231 ? 19.377  7.802   25.623  0.50 15.44 ? 231 CYS A CA  1 
ATOM   1894 C  CA  B CYS A  1 231 ? 19.395  7.736   25.623  0.50 20.86 ? 231 CYS A CA  1 
ATOM   1895 C  C   A CYS A  1 231 ? 19.931  9.104   26.144  0.50 15.05 ? 231 CYS A C   1 
ATOM   1896 C  C   B CYS A  1 231 ? 19.623  9.165   26.105  0.50 19.33 ? 231 CYS A C   1 
ATOM   1897 O  O   A CYS A  1 231 ? 20.601  9.879   25.439  0.50 15.20 ? 231 CYS A O   1 
ATOM   1898 O  O   B CYS A  1 231 ? 19.809  10.113  25.336  0.50 20.40 ? 231 CYS A O   1 
ATOM   1899 C  CB  A CYS A  1 231 ? 18.077  8.110   24.855  0.50 12.76 ? 231 CYS A CB  1 
ATOM   1900 C  CB  B CYS A  1 231 ? 18.274  7.658   24.589  0.50 23.51 ? 231 CYS A CB  1 
ATOM   1901 S  SG  A CYS A  1 231 ? 17.519  6.694   23.859  0.50 12.94 ? 231 CYS A SG  1 
ATOM   1902 S  SG  B CYS A  1 231 ? 16.571  7.760   25.158  0.50 28.59 ? 231 CYS A SG  1 
ATOM   1903 N  N   . THR A  1 232 ? 19.611  9.291   27.434  1.00 18.27 ? 232 THR A N   1 
ATOM   1904 C  CA  . THR A  1 232 ? 19.698  10.558  28.110  1.00 18.29 ? 232 THR A CA  1 
ATOM   1905 C  C   . THR A  1 232 ? 20.994  10.663  28.935  1.00 18.93 ? 232 THR A C   1 
ATOM   1906 O  O   . THR A  1 232 ? 21.622  9.649   29.316  1.00 18.87 ? 232 THR A O   1 
ATOM   1907 C  CB  . THR A  1 232 ? 18.443  10.780  28.984  1.00 18.07 ? 232 THR A CB  1 
ATOM   1908 O  OG1 . THR A  1 232 ? 18.095  9.594   29.685  1.00 19.78 ? 232 THR A OG1 1 
ATOM   1909 C  CG2 . THR A  1 232 ? 17.246  11.280  28.114  1.00 19.90 ? 232 THR A CG2 1 
ATOM   1910 N  N   . HIS A  1 233 ? 21.423  11.930  29.156  1.00 20.04 ? 233 HIS A N   1 
ATOM   1911 C  CA  . HIS A  1 233 ? 22.599  12.197  30.017  1.00 24.00 ? 233 HIS A CA  1 
ATOM   1912 C  C   . HIS A  1 233 ? 22.272  11.823  31.460  1.00 21.91 ? 233 HIS A C   1 
ATOM   1913 O  O   . HIS A  1 233 ? 21.072  11.795  31.877  1.00 23.31 ? 233 HIS A O   1 
ATOM   1914 C  CB  . HIS A  1 233 ? 22.954  13.685  29.953  1.00 24.93 ? 233 HIS A CB  1 
ATOM   1915 C  CG  . HIS A  1 233 ? 23.739  14.033  28.712  1.00 29.14 ? 233 HIS A CG  1 
ATOM   1916 N  ND1 . HIS A  1 233 ? 23.192  14.648  27.642  1.00 36.16 ? 233 HIS A ND1 1 
ATOM   1917 C  CD2 . HIS A  1 233 ? 25.067  13.780  28.383  1.00 30.94 ? 233 HIS A CD2 1 
ATOM   1918 C  CE1 . HIS A  1 233 ? 24.120  14.782  26.679  1.00 29.27 ? 233 HIS A CE1 1 
ATOM   1919 N  NE2 . HIS A  1 233 ? 25.269  14.266  27.133  1.00 32.36 ? 233 HIS A NE2 1 
ATOM   1920 N  N   . MET A  1 234 ? 23.326  11.490  32.210  1.00 22.50 ? 234 MET A N   1 
ATOM   1921 C  CA  . MET A  1 234 ? 23.125  11.046  33.583  1.00 24.84 ? 234 MET A CA  1 
ATOM   1922 C  C   . MET A  1 234 ? 22.291  11.979  34.433  1.00 27.79 ? 234 MET A C   1 
ATOM   1923 O  O   . MET A  1 234 ? 21.477  11.528  35.186  1.00 25.71 ? 234 MET A O   1 
ATOM   1924 C  CB  . MET A  1 234 ? 24.443  10.776  34.232  1.00 25.69 ? 234 MET A CB  1 
ATOM   1925 C  CG  . MET A  1 234 ? 24.288  10.047  35.587  1.00 29.34 ? 234 MET A CG  1 
ATOM   1926 S  SD  . MET A  1 234 ? 25.955  9.659   36.228  1.00 38.37 ? 234 MET A SD  1 
ATOM   1927 C  CE  . MET A  1 234 ? 26.758  11.095  35.535  1.00 36.13 ? 234 MET A CE  1 
ATOM   1928 N  N   . ASP A  1 235 ? 22.445  13.286  34.252  1.00 27.60 ? 235 ASP A N   1 
ATOM   1929 C  CA  . ASP A  1 235 ? 21.708  14.198  35.103  1.00 33.12 ? 235 ASP A CA  1 
ATOM   1930 C  C   . ASP A  1 235 ? 20.372  14.673  34.541  1.00 34.22 ? 235 ASP A C   1 
ATOM   1931 O  O   . ASP A  1 235 ? 19.794  15.616  35.063  1.00 31.67 ? 235 ASP A O   1 
ATOM   1932 C  CB  . ASP A  1 235 ? 22.587  15.414  35.365  1.00 39.70 ? 235 ASP A CB  1 
ATOM   1933 C  CG  . ASP A  1 235 ? 22.801  16.256  34.099  1.00 49.30 ? 235 ASP A CG  1 
ATOM   1934 O  OD1 . ASP A  1 235 ? 22.510  15.794  32.954  1.00 54.35 ? 235 ASP A OD1 1 
ATOM   1935 O  OD2 . ASP A  1 235 ? 23.261  17.404  34.257  1.00 52.69 ? 235 ASP A OD2 1 
ATOM   1936 N  N   . ASP A  1 236 ? 19.852  14.032  33.494  1.00 31.10 ? 236 ASP A N   1 
ATOM   1937 C  CA  . ASP A  1 236 ? 18.585  14.393  32.927  1.00 29.62 ? 236 ASP A CA  1 
ATOM   1938 C  C   . ASP A  1 236 ? 17.516  14.004  33.934  1.00 31.29 ? 236 ASP A C   1 
ATOM   1939 O  O   . ASP A  1 236 ? 17.407  12.829  34.304  1.00 30.64 ? 236 ASP A O   1 
ATOM   1940 C  CB  . ASP A  1 236 ? 18.354  13.641  31.610  1.00 29.34 ? 236 ASP A CB  1 
ATOM   1941 C  CG  . ASP A  1 236 ? 17.224  14.239  30.775  1.00 34.67 ? 236 ASP A CG  1 
ATOM   1942 O  OD1 . ASP A  1 236 ? 16.123  14.577  31.283  1.00 35.64 ? 236 ASP A OD1 1 
ATOM   1943 O  OD2 . ASP A  1 236 ? 17.429  14.346  29.559  1.00 32.19 ? 236 ASP A OD2 1 
ATOM   1944 N  N   . PRO A  1 237 ? 16.734  14.980  34.421  1.00 33.35 ? 237 PRO A N   1 
ATOM   1945 C  CA  . PRO A  1 237 ? 15.613  14.659  35.347  1.00 34.74 ? 237 PRO A CA  1 
ATOM   1946 C  C   . PRO A  1 237 ? 14.481  13.801  34.723  1.00 34.45 ? 237 PRO A C   1 
ATOM   1947 O  O   . PRO A  1 237 ? 13.570  13.324  35.425  1.00 32.07 ? 237 PRO A O   1 
ATOM   1948 C  CB  . PRO A  1 237 ? 15.079  16.064  35.749  1.00 35.40 ? 237 PRO A CB  1 
ATOM   1949 C  CG  . PRO A  1 237 ? 15.392  16.914  34.547  1.00 40.52 ? 237 PRO A CG  1 
ATOM   1950 C  CD  . PRO A  1 237 ? 16.704  16.393  33.979  1.00 33.66 ? 237 PRO A CD  1 
ATOM   1951 N  N   . SER A  1 238 ? 14.527  13.603  33.405  1.00 33.83 ? 238 SER A N   1 
ATOM   1952 C  CA  . SER A  1 238 ? 13.493  12.797  32.712  1.00 35.59 ? 238 SER A CA  1 
ATOM   1953 C  C   . SER A  1 238 ? 14.205  11.740  31.836  1.00 29.11 ? 238 SER A C   1 
ATOM   1954 O  O   . SER A  1 238 ? 14.373  11.942  30.618  1.00 27.00 ? 238 SER A O   1 
ATOM   1955 C  CB  . SER A  1 238 ? 12.524  13.699  31.943  1.00 35.62 ? 238 SER A CB  1 
ATOM   1956 O  OG  . SER A  1 238 ? 13.141  14.929  31.552  1.00 47.86 ? 238 SER A OG  1 
ATOM   1957 N  N   . PRO A  1 239 ? 14.640  10.645  32.488  1.00 27.53 ? 239 PRO A N   1 
ATOM   1958 C  CA  . PRO A  1 239 ? 15.491  9.740   31.726  1.00 27.11 ? 239 PRO A CA  1 
ATOM   1959 C  C   . PRO A  1 239 ? 14.654  8.906   30.744  1.00 28.58 ? 239 PRO A C   1 
ATOM   1960 O  O   . PRO A  1 239 ? 13.477  8.606   31.023  1.00 29.84 ? 239 PRO A O   1 
ATOM   1961 C  CB  . PRO A  1 239 ? 16.107  8.860   32.791  1.00 26.91 ? 239 PRO A CB  1 
ATOM   1962 C  CG  . PRO A  1 239 ? 15.183  8.945   33.977  1.00 35.08 ? 239 PRO A CG  1 
ATOM   1963 C  CD  . PRO A  1 239 ? 14.711  10.370  33.929  1.00 26.12 ? 239 PRO A CD  1 
ATOM   1964 N  N   . ARG A  1 240 ? 15.289  8.492   29.644  1.00 24.44 ? 240 ARG A N   1 
ATOM   1965 C  CA  . ARG A  1 240 ? 14.601  7.704   28.611  1.00 24.60 ? 240 ARG A CA  1 
ATOM   1966 C  C   . ARG A  1 240 ? 15.474  6.475   28.387  1.00 21.21 ? 240 ARG A C   1 
ATOM   1967 O  O   . ARG A  1 240 ? 16.639  6.572   28.072  1.00 20.68 ? 240 ARG A O   1 
ATOM   1968 C  CB  . ARG A  1 240 ? 14.418  8.482   27.315  1.00 27.31 ? 240 ARG A CB  1 
ATOM   1969 C  CG  . ARG A  1 240 ? 13.655  9.833   27.410  1.00 34.46 ? 240 ARG A CG  1 
ATOM   1970 C  CD  . ARG A  1 240 ? 13.505  10.528  26.045  1.00 35.17 ? 240 ARG A CD  1 
ATOM   1971 N  NE  . ARG A  1 240 ? 14.557  11.521  25.688  1.00 40.58 ? 240 ARG A NE  1 
ATOM   1972 C  CZ  . ARG A  1 240 ? 15.521  11.398  24.743  1.00 38.27 ? 240 ARG A CZ  1 
ATOM   1973 N  NH1 . ARG A  1 240 ? 15.653  10.300  23.987  1.00 37.05 ? 240 ARG A NH1 1 
ATOM   1974 N  NH2 . ARG A  1 240 ? 16.368  12.413  24.526  1.00 37.79 ? 240 ARG A NH2 1 
ATOM   1975 N  N   . GLU A  1 241 ? 14.910  5.334   28.575  1.00 19.77 ? 241 GLU A N   1 
ATOM   1976 C  CA  . GLU A  1 241 ? 15.572  4.071   28.227  1.00 20.41 ? 241 GLU A CA  1 
ATOM   1977 C  C   . GLU A  1 241 ? 15.890  4.017   26.737  1.00 17.18 ? 241 GLU A C   1 
ATOM   1978 O  O   . GLU A  1 241 ? 15.107  4.443   25.874  1.00 18.04 ? 241 GLU A O   1 
ATOM   1979 C  CB  . GLU A  1 241 ? 14.668  2.906   28.537  1.00 23.45 ? 241 GLU A CB  1 
ATOM   1980 C  CG  . GLU A  1 241 ? 14.229  2.773   29.981  1.00 30.36 ? 241 GLU A CG  1 
ATOM   1981 C  CD  . GLU A  1 241 ? 13.144  1.679   30.163  1.00 34.18 ? 241 GLU A CD  1 
ATOM   1982 O  OE1 . GLU A  1 241 ? 12.126  1.632   29.420  1.00 44.15 ? 241 GLU A OE1 1 
ATOM   1983 O  OE2 . GLU A  1 241 ? 13.282  0.835   31.063  1.00 42.51 ? 241 GLU A OE2 1 
ATOM   1984 N  N   . MET A  1 242 ? 17.062  3.456   26.444  1.00 14.58 ? 242 MET A N   1 
ATOM   1985 C  CA  . MET A  1 242 ? 17.458  3.176   25.051  1.00 11.95 ? 242 MET A CA  1 
ATOM   1986 C  C   . MET A  1 242 ? 16.900  1.809   24.650  1.00 12.02 ? 242 MET A C   1 
ATOM   1987 O  O   . MET A  1 242 ? 17.499  0.774   24.859  1.00 12.35 ? 242 MET A O   1 
ATOM   1988 C  CB  . MET A  1 242 ? 19.011  3.301   24.853  1.00 13.05 ? 242 MET A CB  1 
ATOM   1989 C  CG  . MET A  1 242 ? 19.335  3.128   23.352  1.00 13.21 ? 242 MET A CG  1 
ATOM   1990 S  SD  . MET A  1 242 ? 21.129  3.134   23.170  1.00 14.37 ? 242 MET A SD  1 
ATOM   1991 C  CE  . MET A  1 242 ? 21.443  4.836   23.698  1.00 15.16 ? 242 MET A CE  1 
ATOM   1992 N  N   . ILE A  1 243 ? 15.711  1.848   24.030  1.00 12.64 ? 243 ILE A N   1 
ATOM   1993 C  CA  . ILE A  1 243 ? 14.994  0.640   23.575  1.00 12.71 ? 243 ILE A CA  1 
ATOM   1994 C  C   . ILE A  1 243 ? 14.370  0.989   22.192  1.00 11.09 ? 243 ILE A C   1 
ATOM   1995 O  O   . ILE A  1 243 ? 14.159  2.161   21.858  1.00 12.67 ? 243 ILE A O   1 
ATOM   1996 C  CB  . ILE A  1 243 ? 13.826  0.238   24.519  1.00 14.41 ? 243 ILE A CB  1 
ATOM   1997 C  CG1 . ILE A  1 243 ? 12.902  1.410   24.853  1.00 15.25 ? 243 ILE A CG1 1 
ATOM   1998 C  CG2 . ILE A  1 243 ? 14.407  -0.430  25.811  1.00 17.61 ? 243 ILE A CG2 1 
ATOM   1999 C  CD1 . ILE A  1 243 ? 11.640  0.975   25.640  1.00 14.87 ? 243 ILE A CD1 1 
ATOM   2000 N  N   . ASN A  1 244 ? 14.037  -0.032  21.409  1.00 9.70  ? 244 ASN A N   1 
ATOM   2001 C  CA  . ASN A  1 244 ? 13.280  0.146   20.168  1.00 10.01 ? 244 ASN A CA  1 
ATOM   2002 C  C   . ASN A  1 244 ? 14.036  1.079   19.234  1.00 10.81 ? 244 ASN A C   1 
ATOM   2003 O  O   . ASN A  1 244 ? 13.447  1.910   18.538  1.00 11.04 ? 244 ASN A O   1 
ATOM   2004 C  CB  . ASN A  1 244 ? 11.825  0.573   20.416  1.00 10.99 ? 244 ASN A CB  1 
ATOM   2005 C  CG  . ASN A  1 244 ? 11.166  -0.346  21.359  1.00 11.72 ? 244 ASN A CG  1 
ATOM   2006 O  OD1 . ASN A  1 244 ? 11.258  -1.562  21.252  1.00 13.65 ? 244 ASN A OD1 1 
ATOM   2007 N  ND2 . ASN A  1 244 ? 10.371  0.279   22.262  1.00 15.18 ? 244 ASN A ND2 1 
ATOM   2008 N  N   . ASN A  1 245 ? 15.403  0.967   19.223  1.00 9.96  ? 245 ASN A N   1 
ATOM   2009 C  CA  . ASN A  1 245 ? 16.257  1.900   18.440  1.00 10.18 ? 245 ASN A CA  1 
ATOM   2010 C  C   . ASN A  1 245 ? 16.472  1.315   17.072  1.00 9.20  ? 245 ASN A C   1 
ATOM   2011 O  O   . ASN A  1 245 ? 17.652  1.157   16.638  1.00 10.26 ? 245 ASN A O   1 
ATOM   2012 C  CB  . ASN A  1 245 ? 17.565  2.227   19.141  1.00 10.18 ? 245 ASN A CB  1 
ATOM   2013 C  CG  . ASN A  1 245 ? 18.386  1.022   19.500  1.00 10.86 ? 245 ASN A CG  1 
ATOM   2014 O  OD1 . ASN A  1 245 ? 17.957  -0.102  19.464  1.00 11.82 ? 245 ASN A OD1 1 
ATOM   2015 N  ND2 . ASN A  1 245 ? 19.680  1.302   19.782  1.00 12.90 ? 245 ASN A ND2 1 
ATOM   2016 N  N   . PHE A  1 246 ? 15.409  0.969   16.344  1.00 8.32  ? 246 PHE A N   1 
ATOM   2017 C  CA  . PHE A  1 246 ? 15.499  0.471   14.958  1.00 8.42  ? 246 PHE A CA  1 
ATOM   2018 C  C   . PHE A  1 246 ? 14.466  1.236   14.145  1.00 8.50  ? 246 PHE A C   1 
ATOM   2019 O  O   . PHE A  1 246 ? 13.477  1.728   14.700  1.00 9.14  ? 246 PHE A O   1 
ATOM   2020 C  CB  . PHE A  1 246 ? 15.167  -1.069  14.902  1.00 9.63  ? 246 PHE A CB  1 
ATOM   2021 C  CG  . PHE A  1 246 ? 13.741  -1.414  15.429  1.00 8.11  ? 246 PHE A CG  1 
ATOM   2022 C  CD1 . PHE A  1 246 ? 12.665  -1.552  14.506  1.00 9.48  ? 246 PHE A CD1 1 
ATOM   2023 C  CD2 . PHE A  1 246 ? 13.494  -1.615  16.776  1.00 9.11  ? 246 PHE A CD2 1 
ATOM   2024 C  CE1 . PHE A  1 246 ? 11.343  -1.848  14.968  1.00 9.83  ? 246 PHE A CE1 1 
ATOM   2025 C  CE2 . PHE A  1 246 ? 12.232  -1.928  17.267  1.00 10.00 ? 246 PHE A CE2 1 
ATOM   2026 C  CZ  . PHE A  1 246 ? 11.123  -2.009  16.347  1.00 9.59  ? 246 PHE A CZ  1 
ATOM   2027 N  N   . ARG A  1 247 ? 14.773  1.345   12.864  1.00 8.05  ? 247 ARG A N   1 
ATOM   2028 C  CA  . ARG A  1 247 ? 13.830  2.058   11.926  1.00 8.50  ? 247 ARG A CA  1 
ATOM   2029 C  C   . ARG A  1 247 ? 12.841  1.038   11.377  1.00 8.27  ? 247 ARG A C   1 
ATOM   2030 O  O   . ARG A  1 247 ? 13.232  -0.073  11.107  1.00 8.68  ? 247 ARG A O   1 
ATOM   2031 C  CB  . ARG A  1 247 ? 14.646  2.739   10.840  1.00 8.20  ? 247 ARG A CB  1 
ATOM   2032 C  CG  . ARG A  1 247 ? 13.848  3.754   9.978   1.00 8.58  ? 247 ARG A CG  1 
ATOM   2033 C  CD  . ARG A  1 247 ? 14.719  4.212   8.765   1.00 9.03  ? 247 ARG A CD  1 
ATOM   2034 N  NE  . ARG A  1 247 ? 14.070  5.387   8.194   1.00 8.21  ? 247 ARG A NE  1 
ATOM   2035 C  CZ  . ARG A  1 247 ? 14.578  5.977   7.091   1.00 8.19  ? 247 ARG A CZ  1 
ATOM   2036 N  NH1 . ARG A  1 247 ? 15.601  5.434   6.442   1.00 8.71  ? 247 ARG A NH1 1 
ATOM   2037 N  NH2 . ARG A  1 247 ? 14.030  7.105   6.685   1.00 8.48  ? 247 ARG A NH2 1 
ATOM   2038 N  N   . GLN A  1 248 ? 11.579  1.466   11.208  1.00 8.55  ? 248 GLN A N   1 
ATOM   2039 C  CA  . GLN A  1 248 ? 10.663  0.624   10.410  1.00 7.89  ? 248 GLN A CA  1 
ATOM   2040 C  C   . GLN A  1 248 ? 11.122  0.374   9.000   1.00 8.43  ? 248 GLN A C   1 
ATOM   2041 O  O   . GLN A  1 248 ? 11.828  1.147   8.389   1.00 8.72  ? 248 GLN A O   1 
ATOM   2042 C  CB  . GLN A  1 248 ? 9.293   1.316   10.333  1.00 8.52  ? 248 GLN A CB  1 
ATOM   2043 C  CG  . GLN A  1 248 ? 8.605   1.589   11.688  1.00 8.21  ? 248 GLN A CG  1 
ATOM   2044 C  CD  . GLN A  1 248 ? 8.253   0.368   12.497  1.00 9.53  ? 248 GLN A CD  1 
ATOM   2045 O  OE1 . GLN A  1 248 ? 8.993   -0.030  13.398  1.00 10.74 ? 248 GLN A OE1 1 
ATOM   2046 N  NE2 . GLN A  1 248 ? 7.170   -0.280  12.109  1.00 11.14 ? 248 GLN A NE2 1 
ATOM   2047 N  N   . VAL A  1 249 ? 10.769  -0.787  8.445   1.00 8.24  ? 249 VAL A N   1 
ATOM   2048 C  CA  . VAL A  1 249 ? 11.082  -1.130  7.083   1.00 8.76  ? 249 VAL A CA  1 
ATOM   2049 C  C   . VAL A  1 249 ? 10.487  -0.101  6.100   1.00 10.32 ? 249 VAL A C   1 
ATOM   2050 O  O   . VAL A  1 249 ? 9.319   0.405   6.316   1.00 9.36  ? 249 VAL A O   1 
ATOM   2051 C  CB  . VAL A  1 249 ? 10.740  -2.545  6.683   1.00 11.03 ? 249 VAL A CB  1 
ATOM   2052 C  CG1 . VAL A  1 249 ? 11.650  -3.518  7.459   1.00 10.32 ? 249 VAL A CG1 1 
ATOM   2053 C  CG2 . VAL A  1 249 ? 9.286   -2.806  6.865   1.00 14.07 ? 249 VAL A CG2 1 
ATOM   2054 N  N   . GLN A  1 250 ? 11.202  0.134   5.018   1.00 8.35  ? 250 GLN A N   1 
ATOM   2055 C  CA  . GLN A  1 250 ? 10.803  1.089   4.016   1.00 9.07  ? 250 GLN A CA  1 
ATOM   2056 C  C   . GLN A  1 250 ? 10.195  0.376   2.835   1.00 9.82  ? 250 GLN A C   1 
ATOM   2057 O  O   . GLN A  1 250 ? 10.574  -0.725  2.504   1.00 11.59 ? 250 GLN A O   1 
ATOM   2058 C  CB  . GLN A  1 250 ? 12.055  1.867   3.579   1.00 9.14  ? 250 GLN A CB  1 
ATOM   2059 C  CG  . GLN A  1 250 ? 12.914  2.474   4.713   1.00 8.63  ? 250 GLN A CG  1 
ATOM   2060 C  CD  . GLN A  1 250 ? 12.156  3.560   5.391   1.00 8.87  ? 250 GLN A CD  1 
ATOM   2061 O  OE1 . GLN A  1 250 ? 11.889  4.616   4.756   1.00 10.31 ? 250 GLN A OE1 1 
ATOM   2062 N  NE2 . GLN A  1 250 ? 11.809  3.408   6.632   1.00 8.42  ? 250 GLN A NE2 1 
ATOM   2063 N  N   . LYS A  1 251 ? 9.371   1.118   2.041   1.00 9.66  ? 251 LYS A N   1 
ATOM   2064 C  CA  . LYS A  1 251 ? 8.938   0.525   0.741   1.00 11.74 ? 251 LYS A CA  1 
ATOM   2065 C  C   . LYS A  1 251 ? 10.138  0.264   -0.154  1.00 11.82 ? 251 LYS A C   1 
ATOM   2066 O  O   . LYS A  1 251 ? 11.099  1.101   -0.133  1.00 12.38 ? 251 LYS A O   1 
ATOM   2067 C  CB  . LYS A  1 251 ? 7.982   1.462   0.055   1.00 11.69 ? 251 LYS A CB  1 
ATOM   2068 C  CG  . LYS A  1 251 ? 6.647   1.462   0.797   1.00 13.22 ? 251 LYS A CG  1 
ATOM   2069 C  CD  . LYS A  1 251 ? 5.649   2.358   0.157   1.00 13.41 ? 251 LYS A CD  1 
ATOM   2070 C  CE  . LYS A  1 251 ? 4.200   2.122   0.587   1.00 10.66 ? 251 LYS A CE  1 
ATOM   2071 N  NZ  . LYS A  1 251 ? 3.979   2.196   2.075   1.00 8.74  ? 251 LYS A NZ  1 
ATOM   2072 N  N   A PHE A  1 252 ? 10.062  -0.830  -0.905  0.50 13.84 ? 252 PHE A N   1 
ATOM   2073 N  N   B PHE A  1 252 ? 10.090  -0.773  -1.006  0.50 14.34 ? 252 PHE A N   1 
ATOM   2074 C  CA  A PHE A  1 252 ? 11.139  -1.174  -1.797  0.50 14.73 ? 252 PHE A CA  1 
ATOM   2075 C  CA  B PHE A  1 252 ? 11.293  -1.094  -1.832  0.50 15.11 ? 252 PHE A CA  1 
ATOM   2076 C  C   A PHE A  1 252 ? 10.444  -1.822  -2.988  0.50 18.24 ? 252 PHE A C   1 
ATOM   2077 C  C   B PHE A  1 252 ? 11.204  -1.253  -3.378  0.50 20.00 ? 252 PHE A C   1 
ATOM   2078 O  O   A PHE A  1 252 ? 10.163  -2.972  -2.984  0.50 17.96 ? 252 PHE A O   1 
ATOM   2079 O  O   B PHE A  1 252 ? 12.162  -1.668  -4.029  0.50 20.89 ? 252 PHE A O   1 
ATOM   2080 C  CB  A PHE A  1 252 ? 12.035  -2.130  -1.021  0.50 17.61 ? 252 PHE A CB  1 
ATOM   2081 C  CB  B PHE A  1 252 ? 11.893  -2.376  -1.270  0.50 16.77 ? 252 PHE A CB  1 
ATOM   2082 C  CG  A PHE A  1 252 ? 13.241  -2.640  -1.776  0.50 19.03 ? 252 PHE A CG  1 
ATOM   2083 C  CG  B PHE A  1 252 ? 13.263  -2.735  -1.852  0.50 17.36 ? 252 PHE A CG  1 
ATOM   2084 C  CD1 A PHE A  1 252 ? 14.429  -1.936  -1.766  0.50 17.93 ? 252 PHE A CD1 1 
ATOM   2085 C  CD1 B PHE A  1 252 ? 14.330  -1.856  -1.738  0.50 16.14 ? 252 PHE A CD1 1 
ATOM   2086 C  CD2 A PHE A  1 252 ? 13.171  -3.852  -2.457  0.50 20.05 ? 252 PHE A CD2 1 
ATOM   2087 C  CD2 B PHE A  1 252 ? 13.458  -3.936  -2.514  0.50 19.17 ? 252 PHE A CD2 1 
ATOM   2088 C  CE1 A PHE A  1 252 ? 15.541  -2.437  -2.435  0.50 18.92 ? 252 PHE A CE1 1 
ATOM   2089 C  CE1 B PHE A  1 252 ? 15.578  -2.191  -2.261  0.50 17.61 ? 252 PHE A CE1 1 
ATOM   2090 C  CE2 A PHE A  1 252 ? 14.293  -4.361  -3.111  0.50 20.42 ? 252 PHE A CE2 1 
ATOM   2091 C  CE2 B PHE A  1 252 ? 14.729  -4.281  -3.000  0.50 16.99 ? 252 PHE A CE2 1 
ATOM   2092 C  CZ  A PHE A  1 252 ? 15.472  -3.656  -3.080  0.50 20.54 ? 252 PHE A CZ  1 
ATOM   2093 C  CZ  B PHE A  1 252 ? 15.774  -3.393  -2.883  0.50 18.31 ? 252 PHE A CZ  1 
ATOM   2094 N  N   . ASP A  1 253 ? 10.037  -0.954  -3.889  1.00 25.34 ? 253 ASP A N   1 
ATOM   2095 C  CA  . ASP A  1 253 ? 9.375   -1.324  -5.182  1.00 25.86 ? 253 ASP A CA  1 
ATOM   2096 C  C   . ASP A  1 253 ? 10.209  -1.250  -6.455  1.00 26.53 ? 253 ASP A C   1 
ATOM   2097 O  O   . ASP A  1 253 ? 11.043  -0.335  -6.663  1.00 26.78 ? 253 ASP A O   1 
ATOM   2098 C  CB  . ASP A  1 253 ? 8.068   -0.479  -5.348  1.00 31.93 ? 253 ASP A CB  1 
ATOM   2099 C  CG  . ASP A  1 253 ? 7.039   -1.128  -6.341  1.00 39.51 ? 253 ASP A CG  1 
ATOM   2100 O  OD1 . ASP A  1 253 ? 6.793   -2.391  -6.256  1.00 37.72 ? 253 ASP A OD1 1 
ATOM   2101 O  OD2 . ASP A  1 253 ? 6.461   -0.375  -7.186  1.00 41.38 ? 253 ASP A OD2 1 
ATOM   2102 N  N   . GLU A  1 254 ? 9.946   -2.266  -7.307  1.00 30.09 ? 254 GLU A N   1 
ATOM   2103 C  CA  . GLU A  1 254 ? 10.600  -2.396  -8.622  1.00 29.93 ? 254 GLU A CA  1 
ATOM   2104 C  C   . GLU A  1 254 ? 12.105  -2.529  -8.468  1.00 28.27 ? 254 GLU A C   1 
ATOM   2105 O  O   . GLU A  1 254 ? 12.882  -2.110  -9.312  1.00 30.31 ? 254 GLU A O   1 
ATOM   2106 C  CB  . GLU A  1 254 ? 10.194  -1.243  -9.531  1.00 33.64 ? 254 GLU A CB  1 
ATOM   2107 C  CG  . GLU A  1 254 ? 8.699   -1.359  -9.750  1.00 37.68 ? 254 GLU A CG  1 
ATOM   2108 C  CD  . GLU A  1 254 ? 8.132   -0.303  -10.661 1.00 46.61 ? 254 GLU A CD  1 
ATOM   2109 O  OE1 . GLU A  1 254 ? 8.723   0.783   -10.767 1.00 39.91 ? 254 GLU A OE1 1 
ATOM   2110 O  OE2 . GLU A  1 254 ? 7.059   -0.564  -11.234 1.00 50.29 ? 254 GLU A OE2 1 
ATOM   2111 N  N   . ARG A  1 255 ? 12.470  -3.180  -7.381  1.00 25.59 ? 255 ARG A N   1 
ATOM   2112 C  CA  . ARG A  1 255 ? 13.909  -3.459  -7.108  1.00 26.81 ? 255 ARG A CA  1 
ATOM   2113 C  C   . ARG A  1 255 ? 14.164  -4.900  -6.645  1.00 26.99 ? 255 ARG A C   1 
ATOM   2114 O  O   . ARG A  1 255 ? 13.282  -5.614  -6.079  1.00 27.91 ? 255 ARG A O   1 
ATOM   2115 C  CB  . ARG A  1 255 ? 14.477  -2.465  -6.127  1.00 22.62 ? 255 ARG A CB  1 
ATOM   2116 C  CG  . ARG A  1 255 ? 14.382  -1.012  -6.598  1.00 25.31 ? 255 ARG A CG  1 
ATOM   2117 C  CD  . ARG A  1 255 ? 14.899  0.023   -5.537  1.00 24.38 ? 255 ARG A CD  1 
ATOM   2118 N  NE  . ARG A  1 255 ? 16.324  -0.272  -5.333  1.00 27.95 ? 255 ARG A NE  1 
ATOM   2119 C  CZ  . ARG A  1 255 ? 17.021  -0.036  -4.226  1.00 26.49 ? 255 ARG A CZ  1 
ATOM   2120 N  NH1 . ARG A  1 255 ? 16.448  0.530   -3.175  1.00 26.55 ? 255 ARG A NH1 1 
ATOM   2121 N  NH2 . ARG A  1 255 ? 18.308  -0.366  -4.177  1.00 18.82 ? 255 ARG A NH2 1 
ATOM   2122 N  N   . LEU A  1 256 ? 15.396  -5.321  -6.910  1.00 22.47 ? 256 LEU A N   1 
ATOM   2123 C  CA  . LEU A  1 256 ? 15.883  -6.563  -6.458  1.00 23.42 ? 256 LEU A CA  1 
ATOM   2124 C  C   . LEU A  1 256 ? 16.936  -6.370  -5.306  1.00 16.94 ? 256 LEU A C   1 
ATOM   2125 O  O   . LEU A  1 256 ? 17.735  -5.377  -5.215  1.00 21.25 ? 256 LEU A O   1 
ATOM   2126 C  CB  . LEU A  1 256 ? 16.469  -7.358  -7.656  1.00 27.30 ? 256 LEU A CB  1 
ATOM   2127 C  CG  . LEU A  1 256 ? 15.494  -7.812  -8.784  1.00 30.28 ? 256 LEU A CG  1 
ATOM   2128 C  CD1 . LEU A  1 256 ? 16.290  -8.376  -9.934  1.00 27.84 ? 256 LEU A CD1 1 
ATOM   2129 C  CD2 . LEU A  1 256 ? 14.533  -8.932  -8.336  1.00 31.58 ? 256 LEU A CD2 1 
ATOM   2130 N  N   . VAL A  1 257 ? 16.848  -7.372  -4.449  1.00 21.58 ? 257 VAL A N   1 
ATOM   2131 C  CA  . VAL A  1 257 ? 17.963  -7.774  -3.613  1.00 16.40 ? 257 VAL A CA  1 
ATOM   2132 C  C   . VAL A  1 257 ? 18.703  -8.946  -4.165  1.00 16.11 ? 257 VAL A C   1 
ATOM   2133 O  O   . VAL A  1 257 ? 18.124  -10.073 -4.377  1.00 18.76 ? 257 VAL A O   1 
ATOM   2134 C  CB  . VAL A  1 257 ? 17.477  -8.107  -2.188  1.00 17.34 ? 257 VAL A CB  1 
ATOM   2135 C  CG1 . VAL A  1 257 ? 18.579  -8.616  -1.224  1.00 17.48 ? 257 VAL A CG1 1 
ATOM   2136 C  CG2 . VAL A  1 257 ? 16.810  -6.922  -1.587  1.00 19.87 ? 257 VAL A CG2 1 
ATOM   2137 N  N   . TYR A  1 258 ? 19.984  -8.816  -4.335  1.00 15.87 ? 258 TYR A N   1 
ATOM   2138 C  CA  . TYR A  1 258 ? 20.769  -9.898  -4.945  1.00 16.19 ? 258 TYR A CA  1 
ATOM   2139 C  C   . TYR A  1 258 ? 21.231  -10.786 -3.850  1.00 16.18 ? 258 TYR A C   1 
ATOM   2140 O  O   . TYR A  1 258 ? 21.500  -10.316 -2.705  1.00 14.94 ? 258 TYR A O   1 
ATOM   2141 C  CB  . TYR A  1 258 ? 21.928  -9.286  -5.750  1.00 17.24 ? 258 TYR A CB  1 
ATOM   2142 C  CG  . TYR A  1 258 ? 21.327  -8.395  -6.779  1.00 21.29 ? 258 TYR A CG  1 
ATOM   2143 C  CD1 . TYR A  1 258 ? 20.840  -8.931  -7.952  1.00 20.02 ? 258 TYR A CD1 1 
ATOM   2144 C  CD2 . TYR A  1 258 ? 21.187  -7.049  -6.538  1.00 21.50 ? 258 TYR A CD2 1 
ATOM   2145 C  CE1 . TYR A  1 258 ? 20.236  -8.112  -8.928  1.00 25.79 ? 258 TYR A CE1 1 
ATOM   2146 C  CE2 . TYR A  1 258 ? 20.577  -6.210  -7.466  1.00 25.22 ? 258 TYR A CE2 1 
ATOM   2147 C  CZ  . TYR A  1 258 ? 20.098  -6.753  -8.645  1.00 25.66 ? 258 TYR A CZ  1 
ATOM   2148 O  OH  . TYR A  1 258 ? 19.510  -5.896  -9.566  1.00 29.96 ? 258 TYR A OH  1 
ATOM   2149 N  N   . THR A  1 259 ? 21.276  -12.104 -4.079  1.00 13.83 ? 259 THR A N   1 
ATOM   2150 C  CA  . THR A  1 259 ? 21.739  -13.073 -3.076  1.00 14.10 ? 259 THR A CA  1 
ATOM   2151 C  C   . THR A  1 259 ? 22.964  -13.807 -3.607  1.00 13.40 ? 259 THR A C   1 
ATOM   2152 O  O   . THR A  1 259 ? 23.096  -14.111 -4.885  1.00 15.51 ? 259 THR A O   1 
ATOM   2153 C  CB  . THR A  1 259 ? 20.612  -14.084 -2.684  1.00 14.21 ? 259 THR A CB  1 
ATOM   2154 O  OG1 . THR A  1 259 ? 20.193  -14.700 -3.903  1.00 17.12 ? 259 THR A OG1 1 
ATOM   2155 C  CG2 . THR A  1 259 ? 19.472  -13.338 -2.042  1.00 15.29 ? 259 THR A CG2 1 
ATOM   2156 N  N   . SER A  1 260 ? 23.896  -14.111 -2.741  1.00 12.87 ? 260 SER A N   1 
ATOM   2157 C  CA  . SER A  1 260 ? 25.050  -14.925 -3.165  1.00 15.10 ? 260 SER A CA  1 
ATOM   2158 C  C   . SER A  1 260 ? 24.716  -16.408 -3.180  1.00 16.55 ? 260 SER A C   1 
ATOM   2159 O  O   . SER A  1 260 ? 25.596  -17.204 -3.458  1.00 18.46 ? 260 SER A O   1 
ATOM   2160 C  CB  . SER A  1 260 ? 26.222  -14.642 -2.269  1.00 15.19 ? 260 SER A CB  1 
ATOM   2161 O  OG  . SER A  1 260 ? 25.929  -15.109 -0.942  1.00 13.60 ? 260 SER A OG  1 
ATOM   2162 N  N   . PHE A  1 261 ? 23.493  -16.766 -2.800  1.00 16.41 ? 261 PHE A N   1 
ATOM   2163 C  CA  . PHE A  1 261 ? 23.010  -18.180 -2.699  1.00 16.88 ? 261 PHE A CA  1 
ATOM   2164 C  C   . PHE A  1 261 ? 21.765  -18.296 -3.519  1.00 20.89 ? 261 PHE A C   1 
ATOM   2165 O  O   . PHE A  1 261 ? 20.962  -17.365 -3.693  1.00 21.15 ? 261 PHE A O   1 
ATOM   2166 C  CB  . PHE A  1 261 ? 22.811  -18.540 -1.218  1.00 17.68 ? 261 PHE A CB  1 
ATOM   2167 C  CG  . PHE A  1 261 ? 21.884  -17.605 -0.511  1.00 18.20 ? 261 PHE A CG  1 
ATOM   2168 C  CD1 . PHE A  1 261 ? 20.515  -17.843 -0.431  1.00 16.52 ? 261 PHE A CD1 1 
ATOM   2169 C  CD2 . PHE A  1 261 ? 22.377  -16.415 0.059   1.00 15.03 ? 261 PHE A CD2 1 
ATOM   2170 C  CE1 . PHE A  1 261 ? 19.646  -16.992 0.156   1.00 17.02 ? 261 PHE A CE1 1 
ATOM   2171 C  CE2 . PHE A  1 261 ? 21.503  -15.542 0.654   1.00 14.01 ? 261 PHE A CE2 1 
ATOM   2172 C  CZ  . PHE A  1 261 ? 20.134  -15.810 0.712   1.00 15.03 ? 261 PHE A CZ  1 
ATOM   2173 N  N   . SER A  1 262 ? 21.548  -19.501 -4.040  1.00 28.72 ? 262 SER A N   1 
ATOM   2174 C  CA  . SER A  1 262 ? 20.290  -19.741 -4.745  1.00 32.61 ? 262 SER A CA  1 
ATOM   2175 C  C   . SER A  1 262 ? 19.483  -20.728 -3.934  1.00 39.45 ? 262 SER A C   1 
ATOM   2176 O  O   . SER A  1 262 ? 18.285  -20.569 -3.758  1.00 45.91 ? 262 SER A O   1 
ATOM   2177 C  CB  . SER A  1 262 ? 20.559  -20.278 -6.134  1.00 32.34 ? 262 SER A CB  1 
ATOM   2178 O  OG  . SER A  1 262 ? 21.399  -21.406 -6.055  1.00 40.08 ? 262 SER A OG  1 
ATOM   2179 N  N   . GLN A  1 263 ? 20.183  -21.748 -3.446  1.00 46.55 ? 263 GLN A N   1 
ATOM   2180 C  CA  . GLN A  1 263 ? 19.640  -22.772 -2.573  1.00 48.97 ? 263 GLN A CA  1 
ATOM   2181 C  C   . GLN A  1 263 ? 19.860  -22.245 -1.123  1.00 58.67 ? 263 GLN A C   1 
ATOM   2182 O  O   . GLN A  1 263 ? 18.894  -21.825 -0.493  1.00 50.04 ? 263 GLN A O   1 
ATOM   2183 C  CB  . GLN A  1 263 ? 20.285  -24.177 -2.863  1.00 49.61 ? 263 GLN A CB  1 
ATOM   2184 C  CG  . GLN A  1 263 ? 21.797  -24.316 -2.576  1.00 45.47 ? 263 GLN A CG  1 
ATOM   2185 C  CD  . GLN A  1 263 ? 22.394  -25.723 -2.770  1.00 46.82 ? 263 GLN A CD  1 
ATOM   2186 O  OE1 . GLN A  1 263 ? 23.525  -25.988 -2.321  1.00 45.09 ? 263 GLN A OE1 1 
ATOM   2187 N  NE2 . GLN A  1 263 ? 21.666  -26.620 -3.439  1.00 31.03 ? 263 GLN A NE2 1 
ATOM   2188 O  OXT . GLN A  1 263 ? 20.976  -22.181 -0.553  1.00 63.40 ? 263 GLN A OXT 1 
ATOM   2189 N  N   . LYS B  1 3   ? -0.343  18.109  -1.619  1.00 46.08 ? 3   LYS B N   1 
ATOM   2190 C  CA  . LYS B  1 3   ? -0.279  17.178  -2.784  1.00 36.95 ? 3   LYS B CA  1 
ATOM   2191 C  C   . LYS B  1 3   ? 0.393   15.898  -2.273  1.00 28.47 ? 3   LYS B C   1 
ATOM   2192 O  O   . LYS B  1 3   ? 1.281   15.370  -2.970  1.00 26.39 ? 3   LYS B O   1 
ATOM   2193 C  CB  . LYS B  1 3   ? 0.623   17.773  -3.840  1.00 38.89 ? 3   LYS B CB  1 
ATOM   2194 C  CG  . LYS B  1 3   ? 1.754   18.478  -3.143  1.00 41.30 ? 3   LYS B CG  1 
ATOM   2195 C  CD  . LYS B  1 3   ? 2.000   19.887  -3.679  1.00 45.19 ? 3   LYS B CD  1 
ATOM   2196 C  CE  . LYS B  1 3   ? 3.242   19.882  -4.544  1.00 41.58 ? 3   LYS B CE  1 
ATOM   2197 N  NZ  . LYS B  1 3   ? 4.303   18.953  -3.985  1.00 34.83 ? 3   LYS B NZ  1 
ATOM   2198 N  N   . TRP B  1 4   ? 0.047   15.442  -1.048  1.00 17.64 ? 4   TRP B N   1 
ATOM   2199 C  CA  . TRP B  1 4   ? 0.764   14.272  -0.473  1.00 13.74 ? 4   TRP B CA  1 
ATOM   2200 C  C   . TRP B  1 4   ? 0.538   13.057  -1.383  1.00 11.66 ? 4   TRP B C   1 
ATOM   2201 O  O   . TRP B  1 4   ? -0.566  12.961  -2.059  1.00 13.68 ? 4   TRP B O   1 
ATOM   2202 C  CB  . TRP B  1 4   ? 0.318   14.029  0.995   1.00 12.43 ? 4   TRP B CB  1 
ATOM   2203 C  CG  . TRP B  1 4   ? -1.173  13.728  1.218   1.00 11.15 ? 4   TRP B CG  1 
ATOM   2204 C  CD1 . TRP B  1 4   ? -2.221  14.595  1.476   1.00 12.08 ? 4   TRP B CD1 1 
ATOM   2205 C  CD2 . TRP B  1 4   ? -1.801  12.407  1.183   1.00 9.82  ? 4   TRP B CD2 1 
ATOM   2206 N  NE1 . TRP B  1 4   ? -3.393  13.913  1.576   1.00 12.74 ? 4   TRP B NE1 1 
ATOM   2207 C  CE2 . TRP B  1 4   ? -3.183  12.591  1.398   1.00 10.33 ? 4   TRP B CE2 1 
ATOM   2208 C  CE3 . TRP B  1 4   ? -1.291  11.092  0.977   1.00 10.03 ? 4   TRP B CE3 1 
ATOM   2209 C  CZ2 . TRP B  1 4   ? -4.054  11.520  1.499   1.00 11.10 ? 4   TRP B CZ2 1 
ATOM   2210 C  CZ3 . TRP B  1 4   ? -2.165  10.027  1.030   1.00 9.03  ? 4   TRP B CZ3 1 
ATOM   2211 C  CH2 . TRP B  1 4   ? -3.493  10.251  1.283   1.00 10.04 ? 4   TRP B CH2 1 
ATOM   2212 N  N   . THR B  1 5   ? 1.454   12.098  -1.325  1.00 10.32 ? 5   THR B N   1 
ATOM   2213 C  CA  . THR B  1 5   ? 1.322   10.890  -2.149  1.00 10.22 ? 5   THR B CA  1 
ATOM   2214 C  C   . THR B  1 5   ? 1.859   9.683   -1.326  1.00 10.48 ? 5   THR B C   1 
ATOM   2215 O  O   . THR B  1 5   ? 2.232   9.817   -0.125  1.00 9.52  ? 5   THR B O   1 
ATOM   2216 C  CB  . THR B  1 5   ? 2.232   10.968  -3.398  1.00 11.85 ? 5   THR B CB  1 
ATOM   2217 O  OG1 . THR B  1 5   ? 3.605   11.001  -2.885  1.00 12.66 ? 5   THR B OG1 1 
ATOM   2218 C  CG2 . THR B  1 5   ? 1.941   12.286  -4.189  1.00 13.19 ? 5   THR B CG2 1 
ATOM   2219 N  N   . TYR B  1 6   ? 1.969   8.547   -1.983  1.00 10.92 ? 6   TYR B N   1 
ATOM   2220 C  CA  . TYR B  1 6   ? 2.598   7.376   -1.423  1.00 9.62  ? 6   TYR B CA  1 
ATOM   2221 C  C   . TYR B  1 6   ? 3.953   7.039   -2.000  1.00 10.84 ? 6   TYR B C   1 
ATOM   2222 O  O   . TYR B  1 6   ? 4.556   6.001   -1.740  1.00 11.79 ? 6   TYR B O   1 
ATOM   2223 C  CB  . TYR B  1 6   ? 1.712   6.166   -1.571  1.00 9.63  ? 6   TYR B CB  1 
ATOM   2224 C  CG  . TYR B  1 6   ? 0.434   6.268   -0.729  1.00 7.99  ? 6   TYR B CG  1 
ATOM   2225 C  CD1 . TYR B  1 6   ? 0.435   5.698   0.582   1.00 8.49  ? 6   TYR B CD1 1 
ATOM   2226 C  CD2 . TYR B  1 6   ? -0.751  6.799   -1.189  1.00 8.04  ? 6   TYR B CD2 1 
ATOM   2227 C  CE1 . TYR B  1 6   ? -0.700  5.678   1.361   1.00 8.04  ? 6   TYR B CE1 1 
ATOM   2228 C  CE2 . TYR B  1 6   ? -1.895  6.764   -0.377  1.00 8.64  ? 6   TYR B CE2 1 
ATOM   2229 C  CZ  . TYR B  1 6   ? -1.864  6.249   0.914   1.00 7.30  ? 6   TYR B CZ  1 
ATOM   2230 O  OH  . TYR B  1 6   ? -2.997  6.232   1.629   1.00 8.68  ? 6   TYR B OH  1 
ATOM   2231 N  N   . PHE B  1 7   ? 4.511   7.958   -2.810  1.00 12.71 ? 7   PHE B N   1 
ATOM   2232 C  CA  . PHE B  1 7   ? 5.713   7.629   -3.543  1.00 15.12 ? 7   PHE B CA  1 
ATOM   2233 C  C   . PHE B  1 7   ? 6.409   8.894   -3.924  1.00 17.07 ? 7   PHE B C   1 
ATOM   2234 O  O   . PHE B  1 7   ? 5.835   9.748   -4.518  1.00 15.30 ? 7   PHE B O   1 
ATOM   2235 C  CB  . PHE B  1 7   ? 5.442   6.818   -4.866  1.00 19.36 ? 7   PHE B CB  1 
ATOM   2236 C  CG  . PHE B  1 7   ? 6.717   6.501   -5.600  1.00 23.85 ? 7   PHE B CG  1 
ATOM   2237 C  CD1 . PHE B  1 7   ? 7.610   5.513   -5.119  1.00 28.28 ? 7   PHE B CD1 1 
ATOM   2238 C  CD2 . PHE B  1 7   ? 7.100   7.235   -6.732  1.00 30.24 ? 7   PHE B CD2 1 
ATOM   2239 C  CE1 . PHE B  1 7   ? 8.820   5.241   -5.754  1.00 32.67 ? 7   PHE B CE1 1 
ATOM   2240 C  CE2 . PHE B  1 7   ? 8.311   6.955   -7.393  1.00 32.39 ? 7   PHE B CE2 1 
ATOM   2241 C  CZ  . PHE B  1 7   ? 9.159   5.974   -6.904  1.00 33.73 ? 7   PHE B CZ  1 
ATOM   2242 N  N   . GLY B  1 8   ? 7.683   8.979   -3.573  1.00 16.80 ? 8   GLY B N   1 
ATOM   2243 C  CA  . GLY B  1 8   ? 8.545   10.140  -3.995  1.00 17.35 ? 8   GLY B CA  1 
ATOM   2244 C  C   . GLY B  1 8   ? 8.576   11.233  -2.940  1.00 19.16 ? 8   GLY B C   1 
ATOM   2245 O  O   . GLY B  1 8   ? 8.341   11.008  -1.741  1.00 18.65 ? 8   GLY B O   1 
ATOM   2246 N  N   . PRO B  1 9   ? 8.943   12.455  -3.331  1.00 18.93 ? 9   PRO B N   1 
ATOM   2247 C  CA  . PRO B  1 9   ? 9.154   13.525  -2.360  1.00 19.14 ? 9   PRO B CA  1 
ATOM   2248 C  C   . PRO B  1 9   ? 8.087   13.842  -1.442  1.00 18.62 ? 9   PRO B C   1 
ATOM   2249 O  O   . PRO B  1 9   ? 8.347   14.409  -0.392  1.00 20.93 ? 9   PRO B O   1 
ATOM   2250 C  CB  . PRO B  1 9   ? 9.513   14.743  -3.237  1.00 22.11 ? 9   PRO B CB  1 
ATOM   2251 C  CG  . PRO B  1 9   ? 9.966   14.077  -4.491  1.00 22.02 ? 9   PRO B CG  1 
ATOM   2252 C  CD  . PRO B  1 9   ? 9.194   12.875  -4.716  1.00 20.91 ? 9   PRO B CD  1 
ATOM   2253 N  N   . ASP B  1 10  ? 6.817   13.536  -1.788  1.00 16.40 ? 10  ASP B N   1 
ATOM   2254 C  CA  . ASP B  1 10  ? 5.682   13.879  -0.972  1.00 16.26 ? 10  ASP B CA  1 
ATOM   2255 C  C   . ASP B  1 10  ? 5.083   12.625  -0.353  1.00 11.76 ? 10  ASP B C   1 
ATOM   2256 O  O   . ASP B  1 10  ? 3.946   12.703  0.108   1.00 12.27 ? 10  ASP B O   1 
ATOM   2257 C  CB  . ASP B  1 10  ? 4.603   14.693  -1.786  1.00 18.25 ? 10  ASP B CB  1 
ATOM   2258 C  CG  . ASP B  1 10  ? 5.214   15.981  -2.396  1.00 25.69 ? 10  ASP B CG  1 
ATOM   2259 O  OD1 . ASP B  1 10  ? 5.956   16.680  -1.642  1.00 27.72 ? 10  ASP B OD1 1 
ATOM   2260 O  OD2 . ASP B  1 10  ? 5.080   16.163  -3.615  1.00 31.82 ? 10  ASP B OD2 1 
ATOM   2261 N  N   . GLY B  1 11  ? 5.879   11.553  -0.356  1.00 12.45 ? 11  GLY B N   1 
ATOM   2262 C  CA  . GLY B  1 11  ? 5.549   10.263  0.218   1.00 10.46 ? 11  GLY B CA  1 
ATOM   2263 C  C   . GLY B  1 11  ? 5.578   10.245  1.732   1.00 10.15 ? 11  GLY B C   1 
ATOM   2264 O  O   . GLY B  1 11  ? 5.799   11.274  2.393   1.00 8.93  ? 11  GLY B O   1 
ATOM   2265 N  N   . GLU B  1 12  ? 5.337   9.068   2.320   1.00 8.30  ? 12  GLU B N   1 
ATOM   2266 C  CA  . GLU B  1 12  ? 4.926   9.015   3.682   1.00 8.31  ? 12  GLU B CA  1 
ATOM   2267 C  C   . GLU B  1 12  ? 5.957   9.442   4.719   1.00 8.13  ? 12  GLU B C   1 
ATOM   2268 O  O   . GLU B  1 12  ? 5.574   9.908   5.798   1.00 8.53  ? 12  GLU B O   1 
ATOM   2269 C  CB  . GLU B  1 12  ? 4.496   7.562   4.050   1.00 8.89  ? 12  GLU B CB  1 
ATOM   2270 C  CG  . GLU B  1 12  ? 5.596   6.514   4.124   1.00 8.85  ? 12  GLU B CG  1 
ATOM   2271 C  CD  . GLU B  1 12  ? 4.959   5.155   4.059   1.00 8.44  ? 12  GLU B CD  1 
ATOM   2272 O  OE1 . GLU B  1 12  ? 4.591   4.685   5.134   1.00 8.63  ? 12  GLU B OE1 1 
ATOM   2273 O  OE2 . GLU B  1 12  ? 4.922   4.592   2.931   1.00 9.46  ? 12  GLU B OE2 1 
ATOM   2274 N  N   . ASN B  1 13  ? 7.261   9.383   4.349   1.00 9.21  ? 13  ASN B N   1 
ATOM   2275 C  CA  . ASN B  1 13  ? 8.268   9.863   5.328   1.00 9.19  ? 13  ASN B CA  1 
ATOM   2276 C  C   . ASN B  1 13  ? 8.304   11.396  5.367   1.00 9.68  ? 13  ASN B C   1 
ATOM   2277 O  O   . ASN B  1 13  ? 8.886   11.962  6.318   1.00 10.27 ? 13  ASN B O   1 
ATOM   2278 C  CB  . ASN B  1 13  ? 9.660   9.352   5.015   1.00 9.80  ? 13  ASN B CB  1 
ATOM   2279 C  CG  . ASN B  1 13  ? 9.822   7.865   5.260   1.00 9.87  ? 13  ASN B CG  1 
ATOM   2280 O  OD1 . ASN B  1 13  ? 8.889   7.204   5.716   1.00 9.63  ? 13  ASN B OD1 1 
ATOM   2281 N  ND2 . ASN B  1 13  ? 10.987  7.329   4.896   1.00 9.63  ? 13  ASN B ND2 1 
ATOM   2282 N  N   . SER B  1 14  ? 7.611   12.001  4.402   1.00 8.98  ? 14  SER B N   1 
ATOM   2283 C  CA  . SER B  1 14  ? 7.512   13.496  4.393   1.00 8.57  ? 14  SER B CA  1 
ATOM   2284 C  C   . SER B  1 14  ? 6.211   14.058  4.807   1.00 9.02  ? 14  SER B C   1 
ATOM   2285 O  O   . SER B  1 14  ? 6.084   15.292  4.958   1.00 10.27 ? 14  SER B O   1 
ATOM   2286 C  CB  . SER B  1 14  ? 7.813   14.003  2.988   1.00 9.40  ? 14  SER B CB  1 
ATOM   2287 O  OG  . SER B  1 14  ? 9.179   13.753  2.642   1.00 9.67  ? 14  SER B OG  1 
ATOM   2288 N  N   . TRP B  1 15  ? 5.190   13.231  5.034   1.00 8.25  ? 15  TRP B N   1 
ATOM   2289 C  CA  . TRP B  1 15  ? 3.886   13.787  5.449   1.00 8.89  ? 15  TRP B CA  1 
ATOM   2290 C  C   . TRP B  1 15  ? 3.959   14.654  6.643   1.00 9.06  ? 15  TRP B C   1 
ATOM   2291 O  O   . TRP B  1 15  ? 3.228   15.683  6.720   1.00 9.84  ? 15  TRP B O   1 
ATOM   2292 C  CB  . TRP B  1 15  ? 2.905   12.668  5.804   1.00 8.97  ? 15  TRP B CB  1 
ATOM   2293 C  CG  . TRP B  1 15  ? 2.497   11.770  4.670   1.00 8.35  ? 15  TRP B CG  1 
ATOM   2294 C  CD1 . TRP B  1 15  ? 2.759   11.930  3.311   1.00 8.95  ? 15  TRP B CD1 1 
ATOM   2295 C  CD2 . TRP B  1 15  ? 1.726   10.526  4.769   1.00 8.51  ? 15  TRP B CD2 1 
ATOM   2296 N  NE1 . TRP B  1 15  ? 2.216   10.897  2.588   1.00 9.14  ? 15  TRP B NE1 1 
ATOM   2297 C  CE2 . TRP B  1 15  ? 1.585   10.022  3.402   1.00 8.31  ? 15  TRP B CE2 1 
ATOM   2298 C  CE3 . TRP B  1 15  ? 1.161   9.811   5.813   1.00 7.69  ? 15  TRP B CE3 1 
ATOM   2299 C  CZ2 . TRP B  1 15  ? 0.904   8.851   3.122   1.00 9.11  ? 15  TRP B CZ2 1 
ATOM   2300 C  CZ3 . TRP B  1 15  ? 0.477   8.631   5.518   1.00 8.48  ? 15  TRP B CZ3 1 
ATOM   2301 C  CH2 . TRP B  1 15  ? 0.352   8.165   4.204   1.00 8.83  ? 15  TRP B CH2 1 
ATOM   2302 N  N   . SER B  1 16  ? 4.778   14.343  7.635   1.00 9.32  ? 16  SER B N   1 
ATOM   2303 C  CA  . SER B  1 16  ? 4.877   15.141  8.867   1.00 10.14 ? 16  SER B CA  1 
ATOM   2304 C  C   . SER B  1 16  ? 5.334   16.607  8.647   1.00 9.50  ? 16  SER B C   1 
ATOM   2305 O  O   . SER B  1 16  ? 5.126   17.411  9.571   1.00 11.14 ? 16  SER B O   1 
ATOM   2306 C  CB  . SER B  1 16  ? 5.885   14.473  9.859   1.00 11.98 ? 16  SER B CB  1 
ATOM   2307 O  OG  . SER B  1 16  ? 7.180   14.593  9.315   1.00 13.45 ? 16  SER B OG  1 
ATOM   2308 N  N   . LYS B  1 17  ? 5.931   16.850  7.498   1.00 9.99  ? 17  LYS B N   1 
ATOM   2309 C  CA  . LYS B  1 17  ? 6.384   18.230  7.195   1.00 10.83 ? 17  LYS B CA  1 
ATOM   2310 C  C   . LYS B  1 17  ? 5.172   19.103  7.095   1.00 11.48 ? 17  LYS B C   1 
ATOM   2311 O  O   . LYS B  1 17  ? 5.343   20.349  7.402   1.00 12.02 ? 17  LYS B O   1 
ATOM   2312 C  CB  . LYS B  1 17  ? 7.168   18.270  5.881   1.00 9.03  ? 17  LYS B CB  1 
ATOM   2313 C  CG  . LYS B  1 17  ? 8.485   17.413  5.889   1.00 12.12 ? 17  LYS B CG  1 
ATOM   2314 C  CD  . LYS B  1 17  ? 9.059   17.415  4.479   1.00 10.56 ? 17  LYS B CD  1 
ATOM   2315 C  CE  . LYS B  1 17  ? 10.260  16.476  4.254   1.00 9.55  ? 17  LYS B CE  1 
ATOM   2316 N  NZ  . LYS B  1 17  ? 10.860  16.621  2.960   1.00 10.52 ? 17  LYS B NZ  1 
ATOM   2317 N  N   . LYS B  1 18  ? 4.034   18.638  6.518   1.00 10.62 ? 18  LYS B N   1 
ATOM   2318 C  CA  . LYS B  1 18  ? 2.820   19.516  6.392   1.00 10.03 ? 18  LYS B CA  1 
ATOM   2319 C  C   . LYS B  1 18  ? 1.748   19.101  7.371   1.00 10.87 ? 18  LYS B C   1 
ATOM   2320 O  O   . LYS B  1 18  ? 0.818   19.922  7.581   1.00 13.12 ? 18  LYS B O   1 
ATOM   2321 C  CB  . LYS B  1 18  ? 2.252   19.405  5.020   1.00 11.74 ? 18  LYS B CB  1 
ATOM   2322 C  CG  . LYS B  1 18  ? 3.139   20.056  3.941   1.00 16.03 ? 18  LYS B CG  1 
ATOM   2323 C  CD  . LYS B  1 18  ? 2.641   19.794  2.477   1.00 17.64 ? 18  LYS B CD  1 
ATOM   2324 C  CE  . LYS B  1 18  ? 3.408   20.669  1.475   1.00 22.68 ? 18  LYS B CE  1 
ATOM   2325 N  NZ  . LYS B  1 18  ? 2.657   20.541  0.134   1.00 24.33 ? 18  LYS B NZ  1 
ATOM   2326 N  N   . TYR B  1 19  ? 1.780   17.879  7.939   1.00 9.25  ? 19  TYR B N   1 
ATOM   2327 C  CA  . TYR B  1 19  ? 0.720   17.352  8.771   1.00 11.64 ? 19  TYR B CA  1 
ATOM   2328 C  C   . TYR B  1 19  ? 1.321   16.847  10.065  1.00 10.78 ? 19  TYR B C   1 
ATOM   2329 O  O   . TYR B  1 19  ? 1.767   15.659  10.147  1.00 10.81 ? 19  TYR B O   1 
ATOM   2330 C  CB  . TYR B  1 19  ? 0.018   16.194  7.982   1.00 11.29 ? 19  TYR B CB  1 
ATOM   2331 C  CG  . TYR B  1 19  ? -0.582  16.601  6.659   1.00 10.26 ? 19  TYR B CG  1 
ATOM   2332 C  CD1 . TYR B  1 19  ? -1.820  17.225  6.628   1.00 11.67 ? 19  TYR B CD1 1 
ATOM   2333 C  CD2 . TYR B  1 19  ? 0.112   16.439  5.478   1.00 11.91 ? 19  TYR B CD2 1 
ATOM   2334 C  CE1 . TYR B  1 19  ? -2.364  17.644  5.442   1.00 13.86 ? 19  TYR B CE1 1 
ATOM   2335 C  CE2 . TYR B  1 19  ? -0.429  16.847  4.287   1.00 13.17 ? 19  TYR B CE2 1 
ATOM   2336 C  CZ  . TYR B  1 19  ? -1.669  17.451  4.273   1.00 13.26 ? 19  TYR B CZ  1 
ATOM   2337 O  OH  . TYR B  1 19  ? -2.199  17.856  3.080   1.00 18.13 ? 19  TYR B OH  1 
ATOM   2338 N  N   . PRO B  1 20  ? 1.466   17.717  11.050  1.00 11.28 ? 20  PRO B N   1 
ATOM   2339 C  CA  . PRO B  1 20  ? 2.232   17.352  12.257  1.00 12.51 ? 20  PRO B CA  1 
ATOM   2340 C  C   . PRO B  1 20  ? 1.757   16.057  12.936  1.00 12.33 ? 20  PRO B C   1 
ATOM   2341 O  O   . PRO B  1 20  ? 2.641   15.388  13.501  1.00 13.13 ? 20  PRO B O   1 
ATOM   2342 C  CB  . PRO B  1 20  ? 2.103   18.578  13.200  1.00 15.72 ? 20  PRO B CB  1 
ATOM   2343 C  CG  . PRO B  1 20  ? 1.626   19.624  12.265  1.00 15.54 ? 20  PRO B CG  1 
ATOM   2344 C  CD  . PRO B  1 20  ? 1.018   19.127  11.021  1.00 12.79 ? 20  PRO B CD  1 
ATOM   2345 N  N   . SER B  1 21  ? 0.459   15.801  12.930  1.00 11.60 ? 21  SER B N   1 
ATOM   2346 C  CA  . SER B  1 21  ? 0.049   14.551  13.613  1.00 11.72 ? 21  SER B CA  1 
ATOM   2347 C  C   . SER B  1 21  ? 0.638   13.304  12.969  1.00 11.64 ? 21  SER B C   1 
ATOM   2348 O  O   . SER B  1 21  ? 0.635   12.295  13.653  1.00 10.92 ? 21  SER B O   1 
ATOM   2349 C  CB  . SER B  1 21  ? -1.416  14.386  13.639  1.00 11.98 ? 21  SER B CB  1 
ATOM   2350 O  OG  . SER B  1 21  ? -2.002  15.458  14.407  1.00 15.30 ? 21  SER B OG  1 
ATOM   2351 N  N   . CYS B  1 22  ? 1.023   13.311  11.718  1.00 10.27 ? 22  CYS B N   1 
ATOM   2352 C  CA  . CYS B  1 22  ? 1.631   12.130  11.095  1.00 9.67  ? 22  CYS B CA  1 
ATOM   2353 C  C   . CYS B  1 22  ? 2.935   11.742  11.744  1.00 10.92 ? 22  CYS B C   1 
ATOM   2354 O  O   . CYS B  1 22  ? 3.428   10.647  11.507  1.00 11.75 ? 22  CYS B O   1 
ATOM   2355 C  CB  . CYS B  1 22  ? 1.803   12.392  9.541   1.00 10.05 ? 22  CYS B CB  1 
ATOM   2356 S  SG  . CYS B  1 22  ? 0.248   12.663  8.666   1.00 10.40 ? 22  CYS B SG  1 
ATOM   2357 N  N   . GLY B  1 23  ? 3.610   12.693  12.430  1.00 11.69 ? 23  GLY B N   1 
ATOM   2358 C  CA  . GLY B  1 23  ? 4.785   12.450  13.244  1.00 12.43 ? 23  GLY B CA  1 
ATOM   2359 C  C   . GLY B  1 23  ? 4.469   12.380  14.706  1.00 13.29 ? 23  GLY B C   1 
ATOM   2360 O  O   . GLY B  1 23  ? 5.435   12.375  15.522  1.00 15.15 ? 23  GLY B O   1 
ATOM   2361 N  N   . GLY B  1 24  ? 3.230   12.230  15.096  1.00 13.46 ? 24  GLY B N   1 
ATOM   2362 C  CA  . GLY B  1 24  ? 2.854   12.254  16.533  1.00 13.87 ? 24  GLY B CA  1 
ATOM   2363 C  C   . GLY B  1 24  ? 2.666   10.813  17.006  1.00 16.28 ? 24  GLY B C   1 
ATOM   2364 O  O   . GLY B  1 24  ? 3.214   9.886   16.411  1.00 18.47 ? 24  GLY B O   1 
ATOM   2365 N  N   . LEU B  1 25  ? 2.080   10.725  18.158  1.00 19.02 ? 25  LEU B N   1 
ATOM   2366 C  CA  . LEU B  1 25  ? 1.918   9.342   18.713  1.00 19.60 ? 25  LEU B CA  1 
ATOM   2367 C  C   . LEU B  1 25  ? 0.646   8.669   18.129  1.00 18.75 ? 25  LEU B C   1 
ATOM   2368 O  O   . LEU B  1 25  ? -0.201  9.307   17.406  1.00 15.83 ? 25  LEU B O   1 
ATOM   2369 C  CB  . LEU B  1 25  ? 1.862   9.386   20.232  1.00 25.94 ? 25  LEU B CB  1 
ATOM   2370 C  CG  . LEU B  1 25  ? 3.119   9.941   20.945  1.00 25.83 ? 25  LEU B CG  1 
ATOM   2371 C  CD1 . LEU B  1 25  ? 2.850   10.214  22.417  1.00 33.60 ? 25  LEU B CD1 1 
ATOM   2372 C  CD2 . LEU B  1 25  ? 4.369   9.098   20.762  1.00 30.63 ? 25  LEU B CD2 1 
ATOM   2373 N  N   . LEU B  1 26  ? 0.490   7.397   18.538  1.00 19.24 ? 26  LEU B N   1 
ATOM   2374 C  CA  . LEU B  1 26  ? -0.760  6.662   18.282  1.00 17.24 ? 26  LEU B CA  1 
ATOM   2375 C  C   . LEU B  1 26  ? -1.059  6.436   16.793  1.00 10.46 ? 26  LEU B C   1 
ATOM   2376 O  O   . LEU B  1 26  ? -2.217  6.424   16.386  1.00 12.34 ? 26  LEU B O   1 
ATOM   2377 C  CB  . LEU B  1 26  ? -2.032  7.285   18.905  1.00 19.05 ? 26  LEU B CB  1 
ATOM   2378 C  CG  . LEU B  1 26  ? -2.009  7.457   20.514  1.00 23.76 ? 26  LEU B CG  1 
ATOM   2379 C  CD1 . LEU B  1 26  ? -3.262  8.172   20.984  1.00 31.81 ? 26  LEU B CD1 1 
ATOM   2380 C  CD2 . LEU B  1 26  ? -1.974  6.088   21.138  1.00 26.79 ? 26  LEU B CD2 1 
ATOM   2381 N  N   . GLN B  1 27  ? 0.005   6.269   16.022  1.00 11.62 ? 27  GLN B N   1 
ATOM   2382 C  CA  . GLN B  1 27  ? -0.228  6.154   14.508  1.00 10.87 ? 27  GLN B CA  1 
ATOM   2383 C  C   . GLN B  1 27  ? -0.597  4.778   14.072  1.00 11.04 ? 27  GLN B C   1 
ATOM   2384 O  O   . GLN B  1 27  ? -0.168  3.755   14.661  1.00 11.66 ? 27  GLN B O   1 
ATOM   2385 C  CB  . GLN B  1 27  ? 1.012   6.625   13.751  1.00 10.87 ? 27  GLN B CB  1 
ATOM   2386 C  CG  . GLN B  1 27  ? 1.256   8.097   14.076  1.00 11.66 ? 27  GLN B CG  1 
ATOM   2387 C  CD  . GLN B  1 27  ? 0.184   8.979   13.442  1.00 10.02 ? 27  GLN B CD  1 
ATOM   2388 O  OE1 . GLN B  1 27  ? 0.187   9.117   12.175  1.00 9.93  ? 27  GLN B OE1 1 
ATOM   2389 N  NE2 . GLN B  1 27  ? -0.701  9.546   14.199  1.00 10.56 ? 27  GLN B NE2 1 
ATOM   2390 N  N   . SER B  1 28  ? -1.405  4.728   13.037  1.00 8.66  ? 28  SER B N   1 
ATOM   2391 C  CA  . SER B  1 28  ? -1.730  3.486   12.344  1.00 8.39  ? 28  SER B CA  1 
ATOM   2392 C  C   . SER B  1 28  ? -1.206  3.483   10.943  1.00 8.92  ? 28  SER B C   1 
ATOM   2393 O  O   . SER B  1 28  ? -0.931  4.542   10.366  1.00 8.71  ? 28  SER B O   1 
ATOM   2394 C  CB  . SER B  1 28  ? -3.243  3.458   12.285  1.00 8.20  ? 28  SER B CB  1 
ATOM   2395 O  OG  . SER B  1 28  ? -3.789  3.349   13.658  1.00 9.83  ? 28  SER B OG  1 
ATOM   2396 N  N   . PRO B  1 29  ? -1.150  2.354   10.250  1.00 7.64  ? 29  PRO B N   1 
ATOM   2397 C  CA  . PRO B  1 29  ? -1.464  1.002   10.754  1.00 8.51  ? 29  PRO B CA  1 
ATOM   2398 C  C   . PRO B  1 29  ? -0.322  0.409   11.541  1.00 7.27  ? 29  PRO B C   1 
ATOM   2399 O  O   . PRO B  1 29  ? 0.706   1.000   11.747  1.00 8.20  ? 29  PRO B O   1 
ATOM   2400 C  CB  . PRO B  1 29  ? -1.694  0.226   9.411   1.00 8.82  ? 29  PRO B CB  1 
ATOM   2401 C  CG  . PRO B  1 29  ? -0.565  0.826   8.520   1.00 8.21  ? 29  PRO B CG  1 
ATOM   2402 C  CD  . PRO B  1 29  ? -0.641  2.273   8.854   1.00 8.78  ? 29  PRO B CD  1 
ATOM   2403 N  N   . ILE B  1 30  ? -0.594  -0.817  12.003  1.00 8.00  ? 30  ILE B N   1 
ATOM   2404 C  CA  . ILE B  1 30  ? 0.410   -1.583  12.820  1.00 7.86  ? 30  ILE B CA  1 
ATOM   2405 C  C   . ILE B  1 30  ? 0.398   -3.038  12.420  1.00 8.14  ? 30  ILE B C   1 
ATOM   2406 O  O   . ILE B  1 30  ? -0.472  -3.529  11.708  1.00 7.72  ? 30  ILE B O   1 
ATOM   2407 C  CB  . ILE B  1 30  ? 0.096   -1.489  14.329  1.00 8.83  ? 30  ILE B CB  1 
ATOM   2408 C  CG1 . ILE B  1 30  ? -1.339  -2.007  14.611  1.00 10.18 ? 30  ILE B CG1 1 
ATOM   2409 C  CG2 . ILE B  1 30  ? 0.284   0.000   14.833  1.00 10.53 ? 30  ILE B CG2 1 
ATOM   2410 C  CD1 . ILE B  1 30  ? -1.605  -2.177  16.109  1.00 12.39 ? 30  ILE B CD1 1 
ATOM   2411 N  N   . ASP B  1 31  ? 1.497   -3.663  12.851  1.00 8.69  ? 31  ASP B N   1 
ATOM   2412 C  CA  . ASP B  1 31  ? 1.635   -5.094  12.666  1.00 9.76  ? 31  ASP B CA  1 
ATOM   2413 C  C   . ASP B  1 31  ? 1.003   -5.814  13.849  1.00 11.90 ? 31  ASP B C   1 
ATOM   2414 O  O   . ASP B  1 31  ? 1.416   -5.632  15.008  1.00 12.87 ? 31  ASP B O   1 
ATOM   2415 C  CB  . ASP B  1 31  ? 3.124   -5.497  12.595  1.00 9.71  ? 31  ASP B CB  1 
ATOM   2416 C  CG  . ASP B  1 31  ? 3.238   -7.021  12.415  1.00 12.87 ? 31  ASP B CG  1 
ATOM   2417 O  OD1 . ASP B  1 31  ? 2.742   -7.612  11.465  1.00 11.44 ? 31  ASP B OD1 1 
ATOM   2418 O  OD2 . ASP B  1 31  ? 3.911   -7.665  13.276  1.00 16.64 ? 31  ASP B OD2 1 
ATOM   2419 N  N   . LEU B  1 32  ? 0.065   -6.716  13.564  1.00 9.99  ? 32  LEU B N   1 
ATOM   2420 C  CA  . LEU B  1 32  ? -0.611  -7.470  14.649  1.00 11.64 ? 32  LEU B CA  1 
ATOM   2421 C  C   . LEU B  1 32  ? 0.174   -8.738  14.863  1.00 12.04 ? 32  LEU B C   1 
ATOM   2422 O  O   . LEU B  1 32  ? 0.238   -9.618  14.015  1.00 13.79 ? 32  LEU B O   1 
ATOM   2423 C  CB  . LEU B  1 32  ? -2.044  -7.790  14.108  1.00 12.53 ? 32  LEU B CB  1 
ATOM   2424 C  CG  . LEU B  1 32  ? -2.850  -6.497  13.798  1.00 14.27 ? 32  LEU B CG  1 
ATOM   2425 C  CD1 . LEU B  1 32  ? -4.094  -6.880  12.970  1.00 16.85 ? 32  LEU B CD1 1 
ATOM   2426 C  CD2 . LEU B  1 32  ? -3.190  -5.561  14.987  1.00 16.19 ? 32  LEU B CD2 1 
ATOM   2427 N  N   . HIS B  1 33  ? 0.830   -8.832  16.024  1.00 12.00 ? 33  HIS B N   1 
ATOM   2428 C  CA  . HIS B  1 33  ? 1.689   -10.000 16.341  1.00 12.65 ? 33  HIS B CA  1 
ATOM   2429 C  C   . HIS B  1 33  ? 1.568   -10.304 17.821  1.00 10.76 ? 33  HIS B C   1 
ATOM   2430 O  O   . HIS B  1 33  ? 1.212   -9.490  18.638  1.00 11.83 ? 33  HIS B O   1 
ATOM   2431 C  CB  . HIS B  1 33  ? 3.202   -9.771  15.924  1.00 14.37 ? 33  HIS B CB  1 
ATOM   2432 C  CG  . HIS B  1 33  ? 3.889   -8.604  16.607  1.00 14.26 ? 33  HIS B CG  1 
ATOM   2433 N  ND1 . HIS B  1 33  ? 3.631   -7.323  16.329  1.00 17.61 ? 33  HIS B ND1 1 
ATOM   2434 C  CD2 . HIS B  1 33  ? 4.823   -8.585  17.643  1.00 14.02 ? 33  HIS B CD2 1 
ATOM   2435 C  CE1 . HIS B  1 33  ? 4.371   -6.516  17.181  1.00 19.67 ? 33  HIS B CE1 1 
ATOM   2436 N  NE2 . HIS B  1 33  ? 5.084   -7.313  17.953  1.00 18.15 ? 33  HIS B NE2 1 
ATOM   2437 N  N   . SER B  1 34  ? 1.939   -11.565 18.140  1.00 13.73 ? 34  SER B N   1 
ATOM   2438 C  CA  . SER B  1 34  ? 1.575   -12.118 19.488  1.00 14.03 ? 34  SER B CA  1 
ATOM   2439 C  C   . SER B  1 34  ? 2.065   -11.317 20.635  1.00 13.57 ? 34  SER B C   1 
ATOM   2440 O  O   . SER B  1 34  ? 1.338   -11.163 21.653  1.00 14.57 ? 34  SER B O   1 
ATOM   2441 C  CB  . SER B  1 34  ? 2.080   -13.569 19.576  1.00 16.71 ? 34  SER B CB  1 
ATOM   2442 O  OG  . SER B  1 34  ? 3.481   -13.620 19.479  1.00 21.71 ? 34  SER B OG  1 
ATOM   2443 N  N   . ASP B  1 35  ? 3.269   -10.719 20.573  1.00 13.19 ? 35  ASP B N   1 
ATOM   2444 C  CA  . ASP B  1 35  ? 3.782   -10.072 21.761  1.00 14.92 ? 35  ASP B CA  1 
ATOM   2445 C  C   . ASP B  1 35  ? 2.955   -8.918  22.274  1.00 15.62 ? 35  ASP B C   1 
ATOM   2446 O  O   . ASP B  1 35  ? 3.053   -8.457  23.445  1.00 19.43 ? 35  ASP B O   1 
ATOM   2447 C  CB  . ASP B  1 35  ? 5.213   -9.474  21.486  1.00 15.61 ? 35  ASP B CB  1 
ATOM   2448 C  CG  . ASP B  1 35  ? 6.119   -10.494 20.888  1.00 19.41 ? 35  ASP B CG  1 
ATOM   2449 O  OD1 . ASP B  1 35  ? 5.862   -11.014 19.770  1.00 17.51 ? 35  ASP B OD1 1 
ATOM   2450 O  OD2 . ASP B  1 35  ? 7.160   -10.879 21.573  1.00 17.25 ? 35  ASP B OD2 1 
ATOM   2451 N  N   . ILE B  1 36  ? 2.106   -8.340  21.432  1.00 13.05 ? 36  ILE B N   1 
ATOM   2452 C  CA  . ILE B  1 36  ? 1.412   -7.151  21.836  1.00 13.94 ? 36  ILE B CA  1 
ATOM   2453 C  C   . ILE B  1 36  ? -0.120  -7.362  21.823  1.00 12.85 ? 36  ILE B C   1 
ATOM   2454 O  O   . ILE B  1 36  ? -0.857  -6.438  22.030  1.00 14.91 ? 36  ILE B O   1 
ATOM   2455 C  CB  . ILE B  1 36  ? 1.806   -5.904  20.929  1.00 15.62 ? 36  ILE B CB  1 
ATOM   2456 C  CG1 . ILE B  1 36  ? 1.670   -6.152  19.420  1.00 19.21 ? 36  ILE B CG1 1 
ATOM   2457 C  CG2 . ILE B  1 36  ? 3.284   -5.528  21.255  1.00 20.40 ? 36  ILE B CG2 1 
ATOM   2458 C  CD1 . ILE B  1 36  ? 0.288   -6.351  18.953  1.00 18.68 ? 36  ILE B CD1 1 
ATOM   2459 N  N   . LEU B  1 37  ? -0.523  -8.615  21.742  1.00 12.95 ? 37  LEU B N   1 
ATOM   2460 C  CA  . LEU B  1 37  ? -1.973  -9.006  21.730  1.00 14.86 ? 37  LEU B CA  1 
ATOM   2461 C  C   . LEU B  1 37  ? -2.354  -9.363  23.161  1.00 16.59 ? 37  LEU B C   1 
ATOM   2462 O  O   . LEU B  1 37  ? -1.591  -9.995  23.865  1.00 19.01 ? 37  LEU B O   1 
ATOM   2463 C  CB  . LEU B  1 37  ? -2.282  -10.215 20.855  1.00 14.53 ? 37  LEU B CB  1 
ATOM   2464 C  CG  . LEU B  1 37  ? -1.975  -9.999  19.350  1.00 15.70 ? 37  LEU B CG  1 
ATOM   2465 C  CD1 . LEU B  1 37  ? -2.231  -11.244 18.518  1.00 16.22 ? 37  LEU B CD1 1 
ATOM   2466 C  CD2 . LEU B  1 37  ? -2.664  -8.800  18.776  1.00 15.12 ? 37  LEU B CD2 1 
ATOM   2467 N  N   . GLN B  1 38  ? -3.570  -8.997  23.532  1.00 14.44 ? 38  GLN B N   1 
ATOM   2468 C  CA  . GLN B  1 38  ? -4.103  -9.470  24.840  1.00 13.98 ? 38  GLN B CA  1 
ATOM   2469 C  C   . GLN B  1 38  ? -5.589  -9.650  24.738  1.00 14.81 ? 38  GLN B C   1 
ATOM   2470 O  O   . GLN B  1 38  ? -6.319  -8.726  24.328  1.00 12.94 ? 38  GLN B O   1 
ATOM   2471 C  CB  . GLN B  1 38  ? -3.815  -8.453  25.849  1.00 16.30 ? 38  GLN B CB  1 
ATOM   2472 C  CG  . GLN B  1 38  ? -4.227  -8.825  27.280  1.00 20.15 ? 38  GLN B CG  1 
ATOM   2473 C  CD  . GLN B  1 38  ? -3.684  -7.799  28.216  1.00 23.56 ? 38  GLN B CD  1 
ATOM   2474 O  OE1 . GLN B  1 38  ? -2.460  -7.766  28.422  1.00 33.36 ? 38  GLN B OE1 1 
ATOM   2475 N  NE2 . GLN B  1 38  ? -4.526  -6.987  28.811  1.00 25.30 ? 38  GLN B NE2 1 
ATOM   2476 N  N   . TYR B  1 39  ? -6.073  -10.802 25.178  1.00 13.77 ? 39  TYR B N   1 
ATOM   2477 C  CA  . TYR B  1 39  ? -7.489  -11.086 25.091  1.00 12.69 ? 39  TYR B CA  1 
ATOM   2478 C  C   . TYR B  1 39  ? -8.234  -10.181 26.063  1.00 12.24 ? 39  TYR B C   1 
ATOM   2479 O  O   . TYR B  1 39  ? -7.782  -9.886  27.205  1.00 14.21 ? 39  TYR B O   1 
ATOM   2480 C  CB  . TYR B  1 39  ? -7.644  -12.560 25.570  1.00 12.97 ? 39  TYR B CB  1 
ATOM   2481 C  CG  . TYR B  1 39  ? -9.093  -12.955 25.723  1.00 13.16 ? 39  TYR B CG  1 
ATOM   2482 C  CD1 . TYR B  1 39  ? -9.976  -12.918 24.687  1.00 14.42 ? 39  TYR B CD1 1 
ATOM   2483 C  CD2 . TYR B  1 39  ? -9.628  -13.375 26.995  1.00 16.58 ? 39  TYR B CD2 1 
ATOM   2484 C  CE1 . TYR B  1 39  ? -11.316 -13.248 24.822  1.00 15.70 ? 39  TYR B CE1 1 
ATOM   2485 C  CE2 . TYR B  1 39  ? -10.962 -13.709 27.126  1.00 15.44 ? 39  TYR B CE2 1 
ATOM   2486 C  CZ  . TYR B  1 39  ? -11.802 -13.667 26.056  1.00 15.80 ? 39  TYR B CZ  1 
ATOM   2487 O  OH  . TYR B  1 39  ? -13.138 -13.981 26.113  1.00 18.62 ? 39  TYR B OH  1 
ATOM   2488 N  N   . ASP B  1 40  ? -9.357  -9.647  25.614  1.00 12.10 ? 40  ASP B N   1 
ATOM   2489 C  CA  . ASP B  1 40  ? -10.235 -8.804  26.453  1.00 12.49 ? 40  ASP B CA  1 
ATOM   2490 C  C   . ASP B  1 40  ? -11.637 -9.353  26.304  1.00 14.03 ? 40  ASP B C   1 
ATOM   2491 O  O   . ASP B  1 40  ? -12.301 -9.137  25.261  1.00 12.82 ? 40  ASP B O   1 
ATOM   2492 C  CB  . ASP B  1 40  ? -10.082 -7.365  25.967  1.00 13.65 ? 40  ASP B CB  1 
ATOM   2493 C  CG  . ASP B  1 40  ? -10.888 -6.393  26.796  1.00 16.52 ? 40  ASP B CG  1 
ATOM   2494 O  OD1 . ASP B  1 40  ? -11.740 -6.869  27.559  1.00 17.92 ? 40  ASP B OD1 1 
ATOM   2495 O  OD2 . ASP B  1 40  ? -10.759 -5.151  26.560  1.00 21.09 ? 40  ASP B OD2 1 
ATOM   2496 N  N   . ALA B  1 41  ? -12.207 -10.066 27.296  1.00 13.51 ? 41  ALA B N   1 
ATOM   2497 C  CA  . ALA B  1 41  ? -13.528 -10.602 27.276  1.00 15.45 ? 41  ALA B CA  1 
ATOM   2498 C  C   . ALA B  1 41  ? -14.657 -9.602  27.194  1.00 15.59 ? 41  ALA B C   1 
ATOM   2499 O  O   . ALA B  1 41  ? -15.773 -9.982  26.826  1.00 18.04 ? 41  ALA B O   1 
ATOM   2500 C  CB  . ALA B  1 41  ? -13.651 -11.442 28.584  1.00 16.20 ? 41  ALA B CB  1 
ATOM   2501 N  N   A SER B  1 42  ? -14.332 -8.326  27.456  0.50 15.50 ? 42  SER B N   1 
ATOM   2502 N  N   B SER B  1 42  ? -14.372 -8.344  27.467  0.50 16.37 ? 42  SER B N   1 
ATOM   2503 C  CA  A SER B  1 42  ? -15.284 -7.225  27.315  0.50 15.37 ? 42  SER B CA  1 
ATOM   2504 C  CA  B SER B  1 42  ? -15.422 -7.388  27.332  0.50 16.29 ? 42  SER B CA  1 
ATOM   2505 C  C   A SER B  1 42  ? -15.510 -6.727  25.865  0.50 14.39 ? 42  SER B C   1 
ATOM   2506 C  C   B SER B  1 42  ? -15.672 -6.953  25.875  0.50 15.48 ? 42  SER B C   1 
ATOM   2507 O  O   A SER B  1 42  ? -16.309 -5.766  25.583  0.50 13.20 ? 42  SER B O   1 
ATOM   2508 O  O   B SER B  1 42  ? -16.656 -6.245  25.598  0.50 15.60 ? 42  SER B O   1 
ATOM   2509 C  CB  A SER B  1 42  ? -14.807 -6.030  28.159  0.50 17.55 ? 42  SER B CB  1 
ATOM   2510 C  CB  B SER B  1 42  ? -15.072 -6.189  28.191  0.50 20.62 ? 42  SER B CB  1 
ATOM   2511 O  OG  A SER B  1 42  ? -14.019 -5.129  27.446  0.50 16.27 ? 42  SER B OG  1 
ATOM   2512 O  OG  B SER B  1 42  ? -15.009 -6.629  29.542  0.50 18.13 ? 42  SER B OG  1 
ATOM   2513 N  N   . LEU B  1 43  ? -14.805 -7.357  24.936  1.00 13.84 ? 43  LEU B N   1 
ATOM   2514 C  CA  . LEU B  1 43  ? -15.050 -7.060  23.496  1.00 13.68 ? 43  LEU B CA  1 
ATOM   2515 C  C   . LEU B  1 43  ? -16.102 -7.916  22.897  1.00 12.48 ? 43  LEU B C   1 
ATOM   2516 O  O   . LEU B  1 43  ? -15.841 -8.908  22.240  1.00 14.40 ? 43  LEU B O   1 
ATOM   2517 C  CB  . LEU B  1 43  ? -13.719 -7.211  22.771  1.00 13.38 ? 43  LEU B CB  1 
ATOM   2518 C  CG  . LEU B  1 43  ? -12.615 -6.206  23.162  1.00 12.38 ? 43  LEU B CG  1 
ATOM   2519 C  CD1 . LEU B  1 43  ? -11.302 -6.488  22.397  1.00 13.89 ? 43  LEU B CD1 1 
ATOM   2520 C  CD2 . LEU B  1 43  ? -12.936 -4.698  22.993  1.00 14.54 ? 43  LEU B CD2 1 
ATOM   2521 N  N   . THR B  1 44  ? -17.335 -7.469  23.152  1.00 13.85 ? 44  THR B N   1 
ATOM   2522 C  CA  . THR B  1 44  ? -18.510 -8.210  22.726  1.00 13.33 ? 44  THR B CA  1 
ATOM   2523 C  C   . THR B  1 44  ? -18.849 -7.916  21.250  1.00 12.12 ? 44  THR B C   1 
ATOM   2524 O  O   . THR B  1 44  ? -18.251 -7.027  20.646  1.00 11.83 ? 44  THR B O   1 
ATOM   2525 C  CB  . THR B  1 44  ? -19.709 -7.783  23.629  1.00 15.46 ? 44  THR B CB  1 
ATOM   2526 O  OG1 . THR B  1 44  ? -19.743 -6.387  23.710  1.00 18.89 ? 44  THR B OG1 1 
ATOM   2527 C  CG2 . THR B  1 44  ? -19.495 -8.275  25.060  1.00 16.93 ? 44  THR B CG2 1 
ATOM   2528 N  N   . PRO B  1 45  ? -19.776 -8.653  20.631  1.00 13.42 ? 45  PRO B N   1 
ATOM   2529 C  CA  . PRO B  1 45  ? -19.949 -8.487  19.218  1.00 13.31 ? 45  PRO B CA  1 
ATOM   2530 C  C   . PRO B  1 45  ? -20.568 -7.173  18.808  1.00 13.18 ? 45  PRO B C   1 
ATOM   2531 O  O   . PRO B  1 45  ? -21.447 -6.625  19.507  1.00 16.31 ? 45  PRO B O   1 
ATOM   2532 C  CB  . PRO B  1 45  ? -20.826 -9.650  18.820  1.00 15.88 ? 45  PRO B CB  1 
ATOM   2533 C  CG  . PRO B  1 45  ? -20.568 -10.723 19.902  1.00 15.15 ? 45  PRO B CG  1 
ATOM   2534 C  CD  . PRO B  1 45  ? -20.497 -9.863  21.107  1.00 13.82 ? 45  PRO B CD  1 
ATOM   2535 N  N   . LEU B  1 46  ? -20.084 -6.621  17.693  1.00 13.05 ? 46  LEU B N   1 
ATOM   2536 C  CA  . LEU B  1 46  ? -20.739 -5.415  17.196  1.00 13.58 ? 46  LEU B CA  1 
ATOM   2537 C  C   . LEU B  1 46  ? -22.027 -5.819  16.485  1.00 12.48 ? 46  LEU B C   1 
ATOM   2538 O  O   . LEU B  1 46  ? -22.142 -6.937  15.921  1.00 14.45 ? 46  LEU B O   1 
ATOM   2539 C  CB  . LEU B  1 46  ? -19.824 -4.679  16.200  1.00 14.94 ? 46  LEU B CB  1 
ATOM   2540 C  CG  . LEU B  1 46  ? -18.506 -4.046  16.684  1.00 18.80 ? 46  LEU B CG  1 
ATOM   2541 C  CD1 . LEU B  1 46  ? -17.693 -3.572  15.456  1.00 18.43 ? 46  LEU B CD1 1 
ATOM   2542 C  CD2 . LEU B  1 46  ? -18.770 -2.948  17.670  1.00 22.73 ? 46  LEU B CD2 1 
ATOM   2543 N  N   . GLU B  1 47  ? -22.960 -4.853  16.557  1.00 16.46 ? 47  GLU B N   1 
ATOM   2544 C  CA  . GLU B  1 47  ? -24.135 -4.979  15.747  1.00 17.83 ? 47  GLU B CA  1 
ATOM   2545 C  C   . GLU B  1 47  ? -24.099 -3.976  14.576  1.00 15.47 ? 47  GLU B C   1 
ATOM   2546 O  O   . GLU B  1 47  ? -23.782 -2.790  14.820  1.00 17.97 ? 47  GLU B O   1 
ATOM   2547 C  CB  . GLU B  1 47  ? -25.368 -4.666  16.593  1.00 27.80 ? 47  GLU B CB  1 
ATOM   2548 C  CG  . GLU B  1 47  ? -25.557 -5.610  17.782  1.00 33.46 ? 47  GLU B CG  1 
ATOM   2549 C  CD  . GLU B  1 47  ? -26.986 -5.579  18.267  1.00 43.74 ? 47  GLU B CD  1 
ATOM   2550 O  OE1 . GLU B  1 47  ? -27.425 -4.527  18.855  1.00 47.79 ? 47  GLU B OE1 1 
ATOM   2551 O  OE2 . GLU B  1 47  ? -27.640 -6.611  17.986  1.00 42.58 ? 47  GLU B OE2 1 
ATOM   2552 N  N   . PHE B  1 48  ? -24.401 -4.516  13.415  1.00 15.61 ? 48  PHE B N   1 
ATOM   2553 C  CA  . PHE B  1 48  ? -24.380 -3.731  12.115  1.00 16.02 ? 48  PHE B CA  1 
ATOM   2554 C  C   . PHE B  1 48  ? -25.805 -3.305  11.776  1.00 19.16 ? 48  PHE B C   1 
ATOM   2555 O  O   . PHE B  1 48  ? -26.589 -4.229  11.439  1.00 23.44 ? 48  PHE B O   1 
ATOM   2556 C  CB  . PHE B  1 48  ? -23.665 -4.474  11.012  1.00 17.92 ? 48  PHE B CB  1 
ATOM   2557 C  CG  . PHE B  1 48  ? -22.319 -4.980  11.474  1.00 15.75 ? 48  PHE B CG  1 
ATOM   2558 C  CD1 . PHE B  1 48  ? -21.217 -4.199  11.515  1.00 14.26 ? 48  PHE B CD1 1 
ATOM   2559 C  CD2 . PHE B  1 48  ? -22.142 -6.354  11.824  1.00 16.23 ? 48  PHE B CD2 1 
ATOM   2560 C  CE1 . PHE B  1 48  ? -20.003 -4.670  12.072  1.00 14.41 ? 48  PHE B CE1 1 
ATOM   2561 C  CE2 . PHE B  1 48  ? -20.923 -6.820  12.309  1.00 16.94 ? 48  PHE B CE2 1 
ATOM   2562 C  CZ  . PHE B  1 48  ? -19.859 -5.971  12.398  1.00 15.40 ? 48  PHE B CZ  1 
ATOM   2563 N  N   A GLN B  1 49  ? -26.158 -2.028  11.861  0.50 16.00 ? 49  GLN B N   1 
ATOM   2564 N  N   B GLN B  1 49  ? -26.082 -1.965  11.971  0.50 14.84 ? 49  GLN B N   1 
ATOM   2565 C  CA  A GLN B  1 49  ? -27.556 -1.780  11.586  0.50 16.33 ? 49  GLN B CA  1 
ATOM   2566 C  CA  B GLN B  1 49  ? -27.437 -1.335  11.828  0.50 15.29 ? 49  GLN B CA  1 
ATOM   2567 C  C   A GLN B  1 49  ? -27.614 -0.760  10.500  0.50 15.32 ? 49  GLN B C   1 
ATOM   2568 C  C   B GLN B  1 49  ? -27.600 -0.629  10.446  0.50 14.31 ? 49  GLN B C   1 
ATOM   2569 O  O   A GLN B  1 49  ? -26.801 0.194   10.469  0.50 15.66 ? 49  GLN B O   1 
ATOM   2570 O  O   B GLN B  1 49  ? -26.811 0.242   10.097  0.50 12.83 ? 49  GLN B O   1 
ATOM   2571 C  CB  A GLN B  1 49  ? -28.248 -1.250  12.801  0.50 14.94 ? 49  GLN B CB  1 
ATOM   2572 C  CB  B GLN B  1 49  ? -27.756 -0.373  12.978  0.50 15.46 ? 49  GLN B CB  1 
ATOM   2573 C  CG  A GLN B  1 49  ? -28.090 -2.137  14.008  0.50 17.21 ? 49  GLN B CG  1 
ATOM   2574 C  CG  B GLN B  1 49  ? -27.863 -1.129  14.293  0.50 17.78 ? 49  GLN B CG  1 
ATOM   2575 C  CD  A GLN B  1 49  ? -29.120 -3.249  14.139  0.50 23.84 ? 49  GLN B CD  1 
ATOM   2576 C  CD  B GLN B  1 49  ? -27.802 -0.261  15.537  0.50 18.39 ? 49  GLN B CD  1 
ATOM   2577 O  OE1 A GLN B  1 49  ? -28.884 -4.302  14.777  0.50 27.49 ? 49  GLN B OE1 1 
ATOM   2578 O  OE1 B GLN B  1 49  ? -27.416 0.913   15.513  0.50 18.63 ? 49  GLN B OE1 1 
ATOM   2579 N  NE2 A GLN B  1 49  ? -30.280 -3.028  13.558  0.50 22.49 ? 49  GLN B NE2 1 
ATOM   2580 N  NE2 B GLN B  1 49  ? -28.168 -0.876  16.687  0.50 22.53 ? 49  GLN B NE2 1 
ATOM   2581 N  N   . GLY B  1 50  ? -28.581 -1.005  9.645   1.00 16.22 ? 50  GLY B N   1 
ATOM   2582 C  CA  . GLY B  1 50  ? -28.815 -0.202  8.441   1.00 13.99 ? 50  GLY B CA  1 
ATOM   2583 C  C   . GLY B  1 50  ? -27.726 -0.432  7.386   1.00 14.70 ? 50  GLY B C   1 
ATOM   2584 O  O   . GLY B  1 50  ? -27.650 0.320   6.431   1.00 15.82 ? 50  GLY B O   1 
ATOM   2585 N  N   . TYR B  1 51  ? -26.984 -1.526  7.538   1.00 13.25 ? 51  TYR B N   1 
ATOM   2586 C  CA  . TYR B  1 51  ? -26.004 -1.886  6.463   1.00 13.36 ? 51  TYR B CA  1 
ATOM   2587 C  C   . TYR B  1 51  ? -26.593 -2.396  5.177   1.00 12.72 ? 51  TYR B C   1 
ATOM   2588 O  O   . TYR B  1 51  ? -26.002 -2.391  4.109   1.00 12.60 ? 51  TYR B O   1 
ATOM   2589 C  CB  . TYR B  1 51  ? -24.964 -2.945  6.988   1.00 12.99 ? 51  TYR B CB  1 
ATOM   2590 C  CG  . TYR B  1 51  ? -23.751 -2.350  7.684   1.00 10.76 ? 51  TYR B CG  1 
ATOM   2591 C  CD1 . TYR B  1 51  ? -22.472 -2.801  7.375   1.00 10.65 ? 51  TYR B CD1 1 
ATOM   2592 C  CD2 . TYR B  1 51  ? -23.879 -1.386  8.670   1.00 10.95 ? 51  TYR B CD2 1 
ATOM   2593 C  CE1 . TYR B  1 51  ? -21.361 -2.302  8.016   1.00 10.60 ? 51  TYR B CE1 1 
ATOM   2594 C  CE2 . TYR B  1 51  ? -22.767 -0.884  9.317   1.00 10.58 ? 51  TYR B CE2 1 
ATOM   2595 C  CZ  . TYR B  1 51  ? -21.515 -1.349  8.980   1.00 11.04 ? 51  TYR B CZ  1 
ATOM   2596 O  OH  . TYR B  1 51  ? -20.377 -0.859  9.614   1.00 11.97 ? 51  TYR B OH  1 
ATOM   2597 N  N   . ASN B  1 52  ? -27.858 -2.923  5.203   1.00 13.47 ? 52  ASN B N   1 
ATOM   2598 C  CA  . ASN B  1 52  ? -28.457 -3.450  4.031   1.00 13.11 ? 52  ASN B CA  1 
ATOM   2599 C  C   . ASN B  1 52  ? -29.096 -2.326  3.213   1.00 16.37 ? 52  ASN B C   1 
ATOM   2600 O  O   . ASN B  1 52  ? -30.275 -2.019  3.364   1.00 16.74 ? 52  ASN B O   1 
ATOM   2601 C  CB  . ASN B  1 52  ? -29.556 -4.467  4.465   1.00 16.40 ? 52  ASN B CB  1 
ATOM   2602 C  CG  . ASN B  1 52  ? -30.135 -5.164  3.321   1.00 18.92 ? 52  ASN B CG  1 
ATOM   2603 O  OD1 . ASN B  1 52  ? -29.808 -4.948  2.151   1.00 26.89 ? 52  ASN B OD1 1 
ATOM   2604 N  ND2 . ASN B  1 52  ? -31.205 -5.973  3.622   1.00 23.36 ? 52  ASN B ND2 1 
ATOM   2605 N  N   . LEU B  1 53  ? -28.305 -1.689  2.375   1.00 14.22 ? 53  LEU B N   1 
ATOM   2606 C  CA  . LEU B  1 53  ? -28.738 -0.469  1.631   1.00 13.68 ? 53  LEU B CA  1 
ATOM   2607 C  C   . LEU B  1 53  ? -29.715 -0.946  0.478   1.00 13.24 ? 53  LEU B C   1 
ATOM   2608 O  O   . LEU B  1 53  ? -29.482 -1.914  -0.232  1.00 14.01 ? 53  LEU B O   1 
ATOM   2609 C  CB  . LEU B  1 53  ? -27.490 0.185   0.980   1.00 12.84 ? 53  LEU B CB  1 
ATOM   2610 C  CG  . LEU B  1 53  ? -26.436 0.601   2.052   1.00 14.07 ? 53  LEU B CG  1 
ATOM   2611 C  CD1 . LEU B  1 53  ? -25.307 1.259   1.190   1.00 15.88 ? 53  LEU B CD1 1 
ATOM   2612 C  CD2 . LEU B  1 53  ? -26.951 1.524   3.089   1.00 14.98 ? 53  LEU B CD2 1 
ATOM   2613 N  N   . SER B  1 54  ? -30.784 -0.164  0.274   1.00 12.92 ? 54  SER B N   1 
ATOM   2614 C  CA  . SER B  1 54  ? -31.710 -0.535  -0.760  1.00 13.31 ? 54  SER B CA  1 
ATOM   2615 C  C   . SER B  1 54  ? -31.097 -0.592  -2.150  1.00 13.07 ? 54  SER B C   1 
ATOM   2616 O  O   . SER B  1 54  ? -30.484 0.437   -2.543  1.00 11.33 ? 54  SER B O   1 
ATOM   2617 C  CB  . SER B  1 54  ? -32.814 0.453   -0.700  1.00 13.66 ? 54  SER B CB  1 
ATOM   2618 O  OG  . SER B  1 54  ? -33.750 0.147   -1.748  1.00 13.98 ? 54  SER B OG  1 
ATOM   2619 N  N   . ALA B  1 55  ? -31.311 -1.656  -2.959  1.00 13.70 ? 55  ALA B N   1 
ATOM   2620 C  CA  . ALA B  1 55  ? -30.870 -1.646  -4.305  1.00 13.23 ? 55  ALA B CA  1 
ATOM   2621 C  C   . ALA B  1 55  ? -31.544 -0.660  -5.234  1.00 13.77 ? 55  ALA B C   1 
ATOM   2622 O  O   . ALA B  1 55  ? -31.094 -0.437  -6.376  1.00 16.08 ? 55  ALA B O   1 
ATOM   2623 C  CB  . ALA B  1 55  ? -31.000 -3.096  -4.895  1.00 17.86 ? 55  ALA B CB  1 
ATOM   2624 N  N   . ASN B  1 56  ? -32.612 -0.067  -4.701  1.00 13.85 ? 56  ASN B N   1 
ATOM   2625 C  CA  . ASN B  1 56  ? -33.294 0.923   -5.520  1.00 14.18 ? 56  ASN B CA  1 
ATOM   2626 C  C   . ASN B  1 56  ? -32.761 2.288   -5.277  1.00 13.19 ? 56  ASN B C   1 
ATOM   2627 O  O   . ASN B  1 56  ? -33.092 3.218   -6.023  1.00 15.65 ? 56  ASN B O   1 
ATOM   2628 C  CB  . ASN B  1 56  ? -34.856 0.929   -5.352  1.00 14.76 ? 56  ASN B CB  1 
ATOM   2629 C  CG  . ASN B  1 56  ? -35.463 -0.353  -5.779  1.00 18.16 ? 56  ASN B CG  1 
ATOM   2630 O  OD1 . ASN B  1 56  ? -34.926 -1.156  -6.534  1.00 17.02 ? 56  ASN B OD1 1 
ATOM   2631 N  ND2 . ASN B  1 56  ? -36.717 -0.501  -5.376  1.00 19.43 ? 56  ASN B ND2 1 
ATOM   2632 N  N   . LYS B  1 57  ? -31.915 2.466   -4.258  1.00 12.97 ? 57  LYS B N   1 
ATOM   2633 C  CA  . LYS B  1 57  ? -31.246 3.735   -3.966  1.00 12.68 ? 57  LYS B CA  1 
ATOM   2634 C  C   . LYS B  1 57  ? -29.831 3.645   -4.548  1.00 12.06 ? 57  LYS B C   1 
ATOM   2635 O  O   . LYS B  1 57  ? -29.408 2.577   -5.017  1.00 13.16 ? 57  LYS B O   1 
ATOM   2636 C  CB  . LYS B  1 57  ? -31.153 3.966   -2.444  1.00 12.69 ? 57  LYS B CB  1 
ATOM   2637 C  CG  . LYS B  1 57  ? -32.513 4.519   -1.868  1.00 15.33 ? 57  LYS B CG  1 
ATOM   2638 C  CD  . LYS B  1 57  ? -32.479 4.642   -0.351  1.00 20.02 ? 57  LYS B CD  1 
ATOM   2639 C  CE  . LYS B  1 57  ? -33.355 5.715   0.246   1.00 30.11 ? 57  LYS B CE  1 
ATOM   2640 N  NZ  . LYS B  1 57  ? -33.251 5.749   1.736   1.00 33.55 ? 57  LYS B NZ  1 
ATOM   2641 N  N   . GLN B  1 58  ? -29.215 4.795   -4.662  1.00 11.45 ? 58  GLN B N   1 
ATOM   2642 C  CA  . GLN B  1 58  ? -27.828 4.858   -5.254  1.00 11.59 ? 58  GLN B CA  1 
ATOM   2643 C  C   . GLN B  1 58  ? -26.965 5.776   -4.397  1.00 11.98 ? 58  GLN B C   1 
ATOM   2644 O  O   . GLN B  1 58  ? -27.374 6.712   -3.708  1.00 13.48 ? 58  GLN B O   1 
ATOM   2645 C  CB  . GLN B  1 58  ? -27.860 5.204   -6.712  1.00 16.26 ? 58  GLN B CB  1 
ATOM   2646 C  CG  . GLN B  1 58  ? -28.256 6.545   -7.014  1.00 18.40 ? 58  GLN B CG  1 
ATOM   2647 C  CD  . GLN B  1 58  ? -28.701 6.609   -8.518  1.00 21.28 ? 58  GLN B CD  1 
ATOM   2648 O  OE1 . GLN B  1 58  ? -28.456 5.703   -9.373  1.00 22.52 ? 58  GLN B OE1 1 
ATOM   2649 N  NE2 . GLN B  1 58  ? -29.360 7.703   -8.832  1.00 27.33 ? 58  GLN B NE2 1 
ATOM   2650 N  N   . PHE B  1 59  ? -25.664 5.368   -4.314  1.00 10.31 ? 59  PHE B N   1 
ATOM   2651 C  CA  . PHE B  1 59  ? -24.674 5.910   -3.436  1.00 9.68  ? 59  PHE B CA  1 
ATOM   2652 C  C   . PHE B  1 59  ? -23.458 6.367   -4.215  1.00 8.22  ? 59  PHE B C   1 
ATOM   2653 O  O   . PHE B  1 59  ? -23.053 5.684   -5.185  1.00 9.69  ? 59  PHE B O   1 
ATOM   2654 C  CB  . PHE B  1 59  ? -24.323 4.839   -2.357  1.00 11.25 ? 59  PHE B CB  1 
ATOM   2655 C  CG  . PHE B  1 59  ? -25.561 4.470   -1.561  1.00 11.37 ? 59  PHE B CG  1 
ATOM   2656 C  CD1 . PHE B  1 59  ? -26.442 3.476   -2.076  1.00 11.03 ? 59  PHE B CD1 1 
ATOM   2657 C  CD2 . PHE B  1 59  ? -25.849 5.177   -0.436  1.00 11.35 ? 59  PHE B CD2 1 
ATOM   2658 C  CE1 . PHE B  1 59  ? -27.653 3.230   -1.340  1.00 12.11 ? 59  PHE B CE1 1 
ATOM   2659 C  CE2 . PHE B  1 59  ? -27.105 4.935   0.255   1.00 12.01 ? 59  PHE B CE2 1 
ATOM   2660 C  CZ  . PHE B  1 59  ? -27.966 3.936   -0.211  1.00 11.23 ? 59  PHE B CZ  1 
ATOM   2661 N  N   . LEU B  1 60  ? -22.935 7.511   -3.805  1.00 9.39  ? 60  LEU B N   1 
ATOM   2662 C  CA  . LEU B  1 60  ? -21.874 8.151   -4.616  1.00 10.01 ? 60  LEU B CA  1 
ATOM   2663 C  C   . LEU B  1 60  ? -20.490 7.535   -4.379  1.00 8.75  ? 60  LEU B C   1 
ATOM   2664 O  O   . LEU B  1 60  ? -20.002 7.521   -3.239  1.00 9.97  ? 60  LEU B O   1 
ATOM   2665 C  CB  . LEU B  1 60  ? -21.854 9.599   -4.189  1.00 10.88 ? 60  LEU B CB  1 
ATOM   2666 C  CG  . LEU B  1 60  ? -20.990 10.528  -5.074  1.00 14.47 ? 60  LEU B CG  1 
ATOM   2667 C  CD1 . LEU B  1 60  ? -21.713 10.736  -6.369  1.00 14.21 ? 60  LEU B CD1 1 
ATOM   2668 C  CD2 . LEU B  1 60  ? -20.760 11.893  -4.336  1.00 15.44 ? 60  LEU B CD2 1 
ATOM   2669 N  N   . LEU B  1 61  ? -19.910 7.104   -5.475  1.00 9.47  ? 61  LEU B N   1 
ATOM   2670 C  CA  . LEU B  1 61  ? -18.523 6.576   -5.559  1.00 8.48  ? 61  LEU B CA  1 
ATOM   2671 C  C   . LEU B  1 61  ? -17.638 7.658   -6.118  1.00 9.59  ? 61  LEU B C   1 
ATOM   2672 O  O   . LEU B  1 61  ? -18.017 8.311   -7.096  1.00 11.37 ? 61  LEU B O   1 
ATOM   2673 C  CB  . LEU B  1 61  ? -18.485 5.376   -6.482  1.00 10.18 ? 61  LEU B CB  1 
ATOM   2674 C  CG  . LEU B  1 61  ? -17.204 4.578   -6.503  1.00 10.01 ? 61  LEU B CG  1 
ATOM   2675 C  CD1 . LEU B  1 61  ? -17.044 3.788   -5.187  1.00 11.62 ? 61  LEU B CD1 1 
ATOM   2676 C  CD2 . LEU B  1 61  ? -17.179 3.638   -7.680  1.00 12.02 ? 61  LEU B CD2 1 
ATOM   2677 N  N   . THR B  1 62  ? -16.523 7.964   -5.480  1.00 9.50  ? 62  THR B N   1 
ATOM   2678 C  CA  . THR B  1 62  ? -15.680 9.111   -5.931  1.00 10.32 ? 62  THR B CA  1 
ATOM   2679 C  C   . THR B  1 62  ? -14.218 8.656   -5.859  1.00 10.08 ? 62  THR B C   1 
ATOM   2680 O  O   . THR B  1 62  ? -13.764 7.972   -4.913  1.00 10.67 ? 62  THR B O   1 
ATOM   2681 C  CB  . THR B  1 62  ? -15.772 10.270  -4.963  1.00 13.69 ? 62  THR B CB  1 
ATOM   2682 O  OG1 . THR B  1 62  ? -17.143 10.734  -4.786  1.00 17.72 ? 62  THR B OG1 1 
ATOM   2683 C  CG2 . THR B  1 62  ? -14.964 11.562  -5.458  1.00 15.97 ? 62  THR B CG2 1 
ATOM   2684 N  N   . ASN B  1 63  ? -13.439 9.069   -6.849  1.00 8.25  ? 63  ASN B N   1 
ATOM   2685 C  CA  . ASN B  1 63  ? -11.962 8.990   -6.759  1.00 8.46  ? 63  ASN B CA  1 
ATOM   2686 C  C   . ASN B  1 63  ? -11.491 10.254  -6.158  1.00 8.94  ? 63  ASN B C   1 
ATOM   2687 O  O   . ASN B  1 63  ? -11.683 11.375  -6.723  1.00 8.55  ? 63  ASN B O   1 
ATOM   2688 C  CB  . ASN B  1 63  ? -11.511 8.836   -8.210  1.00 9.17  ? 63  ASN B CB  1 
ATOM   2689 C  CG  . ASN B  1 63  ? -10.006 8.879   -8.324  1.00 7.82  ? 63  ASN B CG  1 
ATOM   2690 O  OD1 . ASN B  1 63  ? -9.271  9.447   -7.513  1.00 8.32  ? 63  ASN B OD1 1 
ATOM   2691 N  ND2 . ASN B  1 63  ? -9.466  8.159   -9.353  1.00 8.37  ? 63  ASN B ND2 1 
ATOM   2692 N  N   . ASN B  1 64  ? -10.883 10.183  -4.966  1.00 9.48  ? 64  ASN B N   1 
ATOM   2693 C  CA  . ASN B  1 64  ? -10.482 11.419  -4.263  1.00 9.86  ? 64  ASN B CA  1 
ATOM   2694 C  C   . ASN B  1 64  ? -9.011  11.785  -4.472  1.00 10.61 ? 64  ASN B C   1 
ATOM   2695 O  O   . ASN B  1 64  ? -8.478  12.636  -3.774  1.00 11.66 ? 64  ASN B O   1 
ATOM   2696 C  CB  . ASN B  1 64  ? -10.809 11.380  -2.752  1.00 10.09 ? 64  ASN B CB  1 
ATOM   2697 C  CG  . ASN B  1 64  ? -9.997  10.365  -2.019  1.00 12.23 ? 64  ASN B CG  1 
ATOM   2698 O  OD1 . ASN B  1 64  ? -9.164  9.702   -2.578  1.00 9.61  ? 64  ASN B OD1 1 
ATOM   2699 N  ND2 . ASN B  1 64  ? -10.319 10.127  -0.709  1.00 13.57 ? 64  ASN B ND2 1 
ATOM   2700 N  N   . GLY B  1 65  ? -8.392  11.110  -5.442  1.00 9.27  ? 65  GLY B N   1 
ATOM   2701 C  CA  . GLY B  1 65  ? -6.984  11.344  -5.682  1.00 10.01 ? 65  GLY B CA  1 
ATOM   2702 C  C   . GLY B  1 65  ? -6.083  10.407  -4.917  1.00 9.87  ? 65  GLY B C   1 
ATOM   2703 O  O   . GLY B  1 65  ? -4.882  10.321  -5.176  1.00 9.41  ? 65  GLY B O   1 
ATOM   2704 N  N   . HIS B  1 66  ? -6.621  9.727   -3.853  1.00 8.79  ? 66  HIS B N   1 
ATOM   2705 C  CA  . HIS B  1 66  ? -5.801  8.851   -2.968  1.00 8.36  ? 66  HIS B CA  1 
ATOM   2706 C  C   . HIS B  1 66  ? -6.372  7.472   -2.839  1.00 8.97  ? 66  HIS B C   1 
ATOM   2707 O  O   . HIS B  1 66  ? -5.605  6.540   -2.512  1.00 9.66  ? 66  HIS B O   1 
ATOM   2708 C  CB  . HIS B  1 66  ? -5.700  9.500   -1.575  1.00 10.15 ? 66  HIS B CB  1 
ATOM   2709 C  CG  . HIS B  1 66  ? -5.143  10.901  -1.619  1.00 10.54 ? 66  HIS B CG  1 
ATOM   2710 N  ND1 . HIS B  1 66  ? -3.822  11.156  -1.890  1.00 10.36 ? 66  HIS B ND1 1 
ATOM   2711 C  CD2 . HIS B  1 66  ? -5.757  12.060  -1.395  1.00 12.20 ? 66  HIS B CD2 1 
ATOM   2712 C  CE1 . HIS B  1 66  ? -3.664  12.512  -1.834  1.00 10.47 ? 66  HIS B CE1 1 
ATOM   2713 N  NE2 . HIS B  1 66  ? -4.835  13.046  -1.521  1.00 12.60 ? 66  HIS B NE2 1 
ATOM   2714 N  N   . SER B  1 67  ? -7.682  7.319   -2.977  1.00 7.64  ? 67  SER B N   1 
ATOM   2715 C  CA  . SER B  1 67  ? -8.383  6.005   -2.934  1.00 7.74  ? 67  SER B CA  1 
ATOM   2716 C  C   . SER B  1 67  ? -9.654  6.176   -3.775  1.00 8.34  ? 67  SER B C   1 
ATOM   2717 O  O   . SER B  1 67  ? -9.892  7.220   -4.373  1.00 9.31  ? 67  SER B O   1 
ATOM   2718 C  CB  . SER B  1 67  ? -8.739  5.660   -1.472  1.00 9.32  ? 67  SER B CB  1 
ATOM   2719 O  OG  . SER B  1 67  ? -9.302  4.350   -1.371  1.00 9.43  ? 67  SER B OG  1 
ATOM   2720 N  N   . VAL B  1 68  ? -10.424 5.078   -3.760  1.00 8.97  ? 68  VAL B N   1 
ATOM   2721 C  CA  . VAL B  1 68  ? -11.774 5.186   -4.293  1.00 9.46  ? 68  VAL B CA  1 
ATOM   2722 C  C   . VAL B  1 68  ? -12.686 5.009   -3.056  1.00 9.82  ? 68  VAL B C   1 
ATOM   2723 O  O   . VAL B  1 68  ? -12.474 4.065   -2.248  1.00 9.28  ? 68  VAL B O   1 
ATOM   2724 C  CB  . VAL B  1 68  ? -11.979 4.113   -5.387  1.00 10.59 ? 68  VAL B CB  1 
ATOM   2725 C  CG1 . VAL B  1 68  ? -11.703 2.709   -4.940  1.00 10.74 ? 68  VAL B CG1 1 
ATOM   2726 C  CG2 . VAL B  1 68  ? -13.379 4.233   -6.022  1.00 13.85 ? 68  VAL B CG2 1 
ATOM   2727 N  N   . LYS B  1 69  ? -13.660 5.922   -2.950  1.00 10.02 ? 69  LYS B N   1 
ATOM   2728 C  CA  . LYS B  1 69  ? -14.550 5.974   -1.719  1.00 10.33 ? 69  LYS B CA  1 
ATOM   2729 C  C   . LYS B  1 69  ? -15.990 5.883   -2.142  1.00 10.46 ? 69  LYS B C   1 
ATOM   2730 O  O   . LYS B  1 69  ? -16.429 6.457   -3.129  1.00 11.28 ? 69  LYS B O   1 
ATOM   2731 C  CB  . LYS B  1 69  ? -14.230 7.181   -0.877  1.00 15.64 ? 69  LYS B CB  1 
ATOM   2732 C  CG  . LYS B  1 69  ? -14.662 8.503   -1.382  1.00 19.06 ? 69  LYS B CG  1 
ATOM   2733 C  CD  . LYS B  1 69  ? -14.713 9.516   -0.174  1.00 20.15 ? 69  LYS B CD  1 
ATOM   2734 C  CE  . LYS B  1 69  ? -14.945 10.832  -0.839  1.00 23.09 ? 69  LYS B CE  1 
ATOM   2735 N  NZ  . LYS B  1 69  ? -14.955 11.884  0.230   1.00 25.91 ? 69  LYS B NZ  1 
ATOM   2736 N  N   . LEU B  1 70  ? -16.781 5.197   -1.316  1.00 8.96  ? 70  LEU B N   1 
ATOM   2737 C  CA  . LEU B  1 70  ? -18.250 5.126   -1.493  1.00 8.55  ? 70  LEU B CA  1 
ATOM   2738 C  C   . LEU B  1 70  ? -18.806 5.834   -0.308  1.00 8.83  ? 70  LEU B C   1 
ATOM   2739 O  O   . LEU B  1 70  ? -18.581 5.474   0.879   1.00 9.43  ? 70  LEU B O   1 
ATOM   2740 C  CB  . LEU B  1 70  ? -18.639 3.696   -1.428  1.00 8.85  ? 70  LEU B CB  1 
ATOM   2741 C  CG  . LEU B  1 70  ? -20.190 3.453   -1.648  1.00 9.42  ? 70  LEU B CG  1 
ATOM   2742 C  CD1 . LEU B  1 70  ? -20.603 3.869   -3.047  1.00 11.12 ? 70  LEU B CD1 1 
ATOM   2743 C  CD2 . LEU B  1 70  ? -20.499 1.956   -1.466  1.00 11.31 ? 70  LEU B CD2 1 
ATOM   2744 N  N   . ASN B  1 71  ? -19.643 6.882   -0.540  1.00 10.34 ? 71  ASN B N   1 
ATOM   2745 C  CA  . ASN B  1 71  ? -20.370 7.610   0.620   1.00 10.99 ? 71  ASN B CA  1 
ATOM   2746 C  C   . ASN B  1 71  ? -21.515 6.721   1.120   1.00 10.90 ? 71  ASN B C   1 
ATOM   2747 O  O   . ASN B  1 71  ? -22.160 5.994   0.347   1.00 13.23 ? 71  ASN B O   1 
ATOM   2748 C  CB  . ASN B  1 71  ? -20.926 8.942   0.047   1.00 11.90 ? 71  ASN B CB  1 
ATOM   2749 C  CG  . ASN B  1 71  ? -19.867 9.979   -0.171  1.00 14.46 ? 71  ASN B CG  1 
ATOM   2750 O  OD1 . ASN B  1 71  ? -18.681 9.826   0.127   1.00 16.18 ? 71  ASN B OD1 1 
ATOM   2751 N  ND2 . ASN B  1 71  ? -20.385 11.160  -0.559  1.00 19.70 ? 71  ASN B ND2 1 
ATOM   2752 N  N   . LEU B  1 72  ? -21.638 6.763   2.452   1.00 10.46 ? 72  LEU B N   1 
ATOM   2753 C  CA  . LEU B  1 72  ? -22.615 5.904   3.072   1.00 12.63 ? 72  LEU B CA  1 
ATOM   2754 C  C   . LEU B  1 72  ? -23.596 6.823   3.850   1.00 11.43 ? 72  LEU B C   1 
ATOM   2755 O  O   . LEU B  1 72  ? -23.256 7.927   4.275   1.00 11.80 ? 72  LEU B O   1 
ATOM   2756 C  CB  . LEU B  1 72  ? -21.870 4.973   4.041   1.00 11.57 ? 72  LEU B CB  1 
ATOM   2757 C  CG  . LEU B  1 72  ? -20.948 3.961   3.341   1.00 11.31 ? 72  LEU B CG  1 
ATOM   2758 C  CD1 . LEU B  1 72  ? -20.041 3.293   4.418   1.00 11.25 ? 72  LEU B CD1 1 
ATOM   2759 C  CD2 . LEU B  1 72  ? -21.658 2.928   2.543   1.00 11.69 ? 72  LEU B CD2 1 
ATOM   2760 N  N   . PRO B  1 73  ? -24.852 6.299   4.014   1.00 11.86 ? 73  PRO B N   1 
ATOM   2761 C  CA  . PRO B  1 73  ? -25.900 7.140   4.609   1.00 12.58 ? 73  PRO B CA  1 
ATOM   2762 C  C   . PRO B  1 73  ? -25.822 7.156   6.121   1.00 14.65 ? 73  PRO B C   1 
ATOM   2763 O  O   . PRO B  1 73  ? -25.304 6.191   6.748   1.00 16.32 ? 73  PRO B O   1 
ATOM   2764 C  CB  . PRO B  1 73  ? -27.148 6.429   4.120   1.00 13.59 ? 73  PRO B CB  1 
ATOM   2765 C  CG  . PRO B  1 73  ? -26.767 4.952   4.133   1.00 12.25 ? 73  PRO B CG  1 
ATOM   2766 C  CD  . PRO B  1 73  ? -25.387 5.056   3.497   1.00 12.52 ? 73  PRO B CD  1 
ATOM   2767 N  N   . SER B  1 74  ? -26.328 8.231   6.740   1.00 18.78 ? 74  SER B N   1 
ATOM   2768 C  CA  . SER B  1 74  ? -26.089 8.307   8.230   1.00 21.41 ? 74  SER B CA  1 
ATOM   2769 C  C   . SER B  1 74  ? -26.996 7.386   9.009   1.00 20.45 ? 74  SER B C   1 
ATOM   2770 O  O   . SER B  1 74  ? -26.682 7.214   10.184  1.00 26.93 ? 74  SER B O   1 
ATOM   2771 C  CB  . SER B  1 74  ? -26.309 9.709   8.800   1.00 23.99 ? 74  SER B CB  1 
ATOM   2772 O  OG  . SER B  1 74  ? -27.520 10.214  8.281   1.00 27.38 ? 74  SER B OG  1 
ATOM   2773 N  N   . ASP B  1 75  ? -28.012 6.798   8.366   1.00 17.32 ? 75  ASP B N   1 
ATOM   2774 C  CA  . ASP B  1 75  ? -28.918 5.798   9.024   1.00 18.94 ? 75  ASP B CA  1 
ATOM   2775 C  C   . ASP B  1 75  ? -28.217 4.381   9.125   1.00 19.94 ? 75  ASP B C   1 
ATOM   2776 O  O   . ASP B  1 75  ? -28.794 3.381   9.588   1.00 22.61 ? 75  ASP B O   1 
ATOM   2777 C  CB  . ASP B  1 75  ? -30.335 5.731   8.415   1.00 23.02 ? 75  ASP B CB  1 
ATOM   2778 C  CG  . ASP B  1 75  ? -30.351 5.388   6.921   1.00 30.18 ? 75  ASP B CG  1 
ATOM   2779 O  OD1 . ASP B  1 75  ? -31.451 5.431   6.324   1.00 33.37 ? 75  ASP B OD1 1 
ATOM   2780 O  OD2 . ASP B  1 75  ? -29.292 5.084   6.338   1.00 28.07 ? 75  ASP B OD2 1 
ATOM   2781 N  N   . MET B  1 76  ? -26.947 4.312   8.697   1.00 17.18 ? 76  MET B N   1 
ATOM   2782 C  CA  . MET B  1 76  ? -26.100 3.107   8.849   1.00 15.20 ? 76  MET B CA  1 
ATOM   2783 C  C   . MET B  1 76  ? -25.202 3.308   10.054  1.00 13.33 ? 76  MET B C   1 
ATOM   2784 O  O   . MET B  1 76  ? -24.518 4.366   10.250  1.00 13.97 ? 76  MET B O   1 
ATOM   2785 C  CB  . MET B  1 76  ? -25.379 2.978   7.535   1.00 15.35 ? 76  MET B CB  1 
ATOM   2786 C  CG  . MET B  1 76  ? -24.440 1.820   7.492   1.00 17.28 ? 76  MET B CG  1 
ATOM   2787 S  SD  . MET B  1 76  ? -23.719 1.709   5.779   1.00 14.90 ? 76  MET B SD  1 
ATOM   2788 C  CE  . MET B  1 76  ? -22.284 0.736   6.231   1.00 11.39 ? 76  MET B CE  1 
ATOM   2789 N  N   . HIS B  1 77  ? -25.261 2.346   11.010  1.00 13.85 ? 77  HIS B N   1 
ATOM   2790 C  CA  . HIS B  1 77  ? -24.532 2.530   12.236  1.00 14.41 ? 77  HIS B CA  1 
ATOM   2791 C  C   . HIS B  1 77  ? -23.927 1.257   12.783  1.00 12.76 ? 77  HIS B C   1 
ATOM   2792 O  O   . HIS B  1 77  ? -24.341 0.189   12.359  1.00 13.94 ? 77  HIS B O   1 
ATOM   2793 C  CB  . HIS B  1 77  ? -25.476 3.079   13.421  1.00 19.47 ? 77  HIS B CB  1 
ATOM   2794 C  CG  . HIS B  1 77  ? -26.381 4.340   13.129  1.00 24.30 ? 77  HIS B CG  1 
ATOM   2795 N  ND1 . HIS B  1 77  ? -26.062 5.581   13.566  1.00 34.19 ? 77  HIS B ND1 1 
ATOM   2796 C  CD2 . HIS B  1 77  ? -27.683 4.418   12.639  1.00 30.61 ? 77  HIS B CD2 1 
ATOM   2797 C  CE1 . HIS B  1 77  ? -27.074 6.445   13.234  1.00 27.86 ? 77  HIS B CE1 1 
ATOM   2798 N  NE2 . HIS B  1 77  ? -28.065 5.726   12.681  1.00 29.71 ? 77  HIS B NE2 1 
ATOM   2799 N  N   . ILE B  1 78  ? -22.992 1.433   13.665  1.00 12.63 ? 78  ILE B N   1 
ATOM   2800 C  CA  . ILE B  1 78  ? -22.540 0.280   14.480  1.00 17.42 ? 78  ILE B CA  1 
ATOM   2801 C  C   . ILE B  1 78  ? -22.913 0.511   15.911  1.00 21.13 ? 78  ILE B C   1 
ATOM   2802 O  O   . ILE B  1 78  ? -22.729 1.641   16.402  1.00 22.73 ? 78  ILE B O   1 
ATOM   2803 C  CB  . ILE B  1 78  ? -21.009 -0.029  14.292  1.00 17.39 ? 78  ILE B CB  1 
ATOM   2804 C  CG1 . ILE B  1 78  ? -20.076 1.146   14.476  1.00 20.47 ? 78  ILE B CG1 1 
ATOM   2805 C  CG2 . ILE B  1 78  ? -20.766 -0.696  12.906  1.00 18.05 ? 78  ILE B CG2 1 
ATOM   2806 C  CD1 . ILE B  1 78  ? -18.617 0.712   14.127  1.00 19.94 ? 78  ILE B CD1 1 
ATOM   2807 N  N   . GLN B  1 79  ? -23.421 -0.578  16.522  1.00 24.40 ? 79  GLN B N   1 
ATOM   2808 C  CA  . GLN B  1 79  ? -23.972 -0.617  17.904  1.00 29.96 ? 79  GLN B CA  1 
ATOM   2809 C  C   . GLN B  1 79  ? -23.087 -1.635  18.624  1.00 26.43 ? 79  GLN B C   1 
ATOM   2810 O  O   . GLN B  1 79  ? -22.754 -2.712  18.103  1.00 24.70 ? 79  GLN B O   1 
ATOM   2811 C  CB  . GLN B  1 79  ? -25.426 -1.119  17.881  1.00 33.69 ? 79  GLN B CB  1 
ATOM   2812 C  CG  . GLN B  1 79  ? -26.245 -1.027  19.219  1.00 41.72 ? 79  GLN B CG  1 
ATOM   2813 C  CD  . GLN B  1 79  ? -26.939 0.343   19.447  1.00 44.56 ? 79  GLN B CD  1 
ATOM   2814 O  OE1 . GLN B  1 79  ? -28.181 0.451   19.316  1.00 48.91 ? 79  GLN B OE1 1 
ATOM   2815 N  NE2 . GLN B  1 79  ? -26.140 1.400   19.792  1.00 40.04 ? 79  GLN B NE2 1 
ATOM   2816 N  N   . GLY B  1 80  ? -22.832 -1.335  19.858  1.00 32.30 ? 80  GLY B N   1 
ATOM   2817 C  CA  . GLY B  1 80  ? -22.074 -2.277  20.631  1.00 30.26 ? 80  GLY B CA  1 
ATOM   2818 C  C   . GLY B  1 80  ? -21.031 -1.428  21.244  1.00 28.73 ? 80  GLY B C   1 
ATOM   2819 O  O   . GLY B  1 80  ? -20.564 -1.751  22.358  1.00 24.47 ? 80  GLY B O   1 
ATOM   2820 N  N   . LEU B  1 81  ? -20.706 -0.318  20.550  1.00 27.48 ? 81  LEU B N   1 
ATOM   2821 C  CA  . LEU B  1 81  ? -19.745 0.659   21.160  1.00 25.91 ? 81  LEU B CA  1 
ATOM   2822 C  C   . LEU B  1 81  ? -20.446 1.513   22.227  1.00 27.38 ? 81  LEU B C   1 
ATOM   2823 O  O   . LEU B  1 81  ? -21.664 1.377   22.449  1.00 26.53 ? 81  LEU B O   1 
ATOM   2824 C  CB  . LEU B  1 81  ? -18.928 1.517   20.152  1.00 27.16 ? 81  LEU B CB  1 
ATOM   2825 C  CG  . LEU B  1 81  ? -18.163 0.732   19.071  1.00 23.58 ? 81  LEU B CG  1 
ATOM   2826 C  CD1 . LEU B  1 81  ? -17.557 1.663   18.023  1.00 23.30 ? 81  LEU B CD1 1 
ATOM   2827 C  CD2 . LEU B  1 81  ? -16.988 0.043   19.743  1.00 24.00 ? 81  LEU B CD2 1 
ATOM   2828 N  N   . GLN B  1 82  ? -19.748 2.394   22.891  1.00 22.58 ? 82  GLN B N   1 
ATOM   2829 C  CA  . GLN B  1 82  ? -20.422 3.015   24.088  1.00 26.76 ? 82  GLN B CA  1 
ATOM   2830 C  C   . GLN B  1 82  ? -21.160 4.264   23.638  1.00 33.48 ? 82  GLN B C   1 
ATOM   2831 O  O   . GLN B  1 82  ? -21.705 4.970   24.498  1.00 32.19 ? 82  GLN B O   1 
ATOM   2832 C  CB  . GLN B  1 82  ? -19.377 3.435   25.089  1.00 28.39 ? 82  GLN B CB  1 
ATOM   2833 C  CG  . GLN B  1 82  ? -18.735 2.270   25.866  1.00 30.68 ? 82  GLN B CG  1 
ATOM   2834 C  CD  . GLN B  1 82  ? -17.627 2.802   26.796  1.00 30.54 ? 82  GLN B CD  1 
ATOM   2835 O  OE1 . GLN B  1 82  ? -17.808 3.025   28.052  1.00 26.71 ? 82  GLN B OE1 1 
ATOM   2836 N  NE2 . GLN B  1 82  ? -16.504 3.137   26.168  1.00 28.72 ? 82  GLN B NE2 1 
ATOM   2837 N  N   . SER B  1 83  ? -21.075 4.585   22.321  1.00 28.80 ? 83  SER B N   1 
ATOM   2838 C  CA  . SER B  1 83  ? -22.026 5.511   21.658  1.00 26.13 ? 83  SER B CA  1 
ATOM   2839 C  C   . SER B  1 83  ? -22.359 4.825   20.353  1.00 25.72 ? 83  SER B C   1 
ATOM   2840 O  O   . SER B  1 83  ? -21.682 3.902   19.990  1.00 20.77 ? 83  SER B O   1 
ATOM   2841 C  CB  . SER B  1 83  ? -21.395 6.856   21.305  1.00 31.27 ? 83  SER B CB  1 
ATOM   2842 O  OG  . SER B  1 83  ? -21.230 7.655   22.450  1.00 33.46 ? 83  SER B OG  1 
ATOM   2843 N  N   . ARG B  1 84  ? -23.384 5.300   19.660  1.00 25.05 ? 84  ARG B N   1 
ATOM   2844 C  CA  . ARG B  1 84  ? -23.657 4.793   18.332  1.00 25.28 ? 84  ARG B CA  1 
ATOM   2845 C  C   . ARG B  1 84  ? -22.686 5.533   17.385  1.00 26.31 ? 84  ARG B C   1 
ATOM   2846 O  O   . ARG B  1 84  ? -22.424 6.741   17.496  1.00 23.50 ? 84  ARG B O   1 
ATOM   2847 C  CB  . ARG B  1 84  ? -25.095 5.042   17.952  1.00 28.52 ? 84  ARG B CB  1 
ATOM   2848 C  CG  . ARG B  1 84  ? -25.697 3.785   17.392  1.00 32.74 ? 84  ARG B CG  1 
ATOM   2849 C  CD  . ARG B  1 84  ? -27.111 3.975   16.855  1.00 26.63 ? 84  ARG B CD  1 
ATOM   2850 N  NE  . ARG B  1 84  ? -27.482 5.283   16.317  1.00 36.07 ? 84  ARG B NE  1 
ATOM   2851 C  CZ  . ARG B  1 84  ? -28.751 5.554   16.002  1.00 34.52 ? 84  ARG B CZ  1 
ATOM   2852 N  NH1 . ARG B  1 84  ? -29.667 4.606   16.201  1.00 39.75 ? 84  ARG B NH1 1 
ATOM   2853 N  NH2 . ARG B  1 84  ? -29.100 6.770   15.529  1.00 41.95 ? 84  ARG B NH2 1 
ATOM   2854 N  N   . TYR B  1 85  ? -22.147 4.783   16.430  1.00 18.94 ? 85  TYR B N   1 
ATOM   2855 C  CA  . TYR B  1 85  ? -21.215 5.387   15.462  1.00 16.14 ? 85  TYR B CA  1 
ATOM   2856 C  C   . TYR B  1 85  ? -21.947 5.279   14.213  1.00 14.27 ? 85  TYR B C   1 
ATOM   2857 O  O   . TYR B  1 85  ? -22.447 4.246   13.867  1.00 17.54 ? 85  TYR B O   1 
ATOM   2858 C  CB  . TYR B  1 85  ? -19.855 4.713   15.377  1.00 15.72 ? 85  TYR B CB  1 
ATOM   2859 C  CG  . TYR B  1 85  ? -18.952 5.140   16.456  1.00 17.57 ? 85  TYR B CG  1 
ATOM   2860 C  CD1 . TYR B  1 85  ? -17.957 6.065   16.218  1.00 17.56 ? 85  TYR B CD1 1 
ATOM   2861 C  CD2 . TYR B  1 85  ? -19.129 4.658   17.748  1.00 21.70 ? 85  TYR B CD2 1 
ATOM   2862 C  CE1 . TYR B  1 85  ? -17.142 6.482   17.237  1.00 20.71 ? 85  TYR B CE1 1 
ATOM   2863 C  CE2 . TYR B  1 85  ? -18.314 5.075   18.762  1.00 22.04 ? 85  TYR B CE2 1 
ATOM   2864 C  CZ  . TYR B  1 85  ? -17.324 5.988   18.491  1.00 23.33 ? 85  TYR B CZ  1 
ATOM   2865 O  OH  . TYR B  1 85  ? -16.518 6.398   19.503  1.00 25.00 ? 85  TYR B OH  1 
ATOM   2866 N  N   . SER B  1 86  ? -22.008 6.398   13.464  1.00 14.15 ? 86  SER B N   1 
ATOM   2867 C  CA  . SER B  1 86  ? -22.708 6.360   12.175  1.00 15.43 ? 86  SER B CA  1 
ATOM   2868 C  C   . SER B  1 86  ? -21.646 6.310   10.963  1.00 10.72 ? 86  SER B C   1 
ATOM   2869 O  O   . SER B  1 86  ? -20.598 6.968   11.105  1.00 13.68 ? 86  SER B O   1 
ATOM   2870 C  CB  . SER B  1 86  ? -23.534 7.630   11.995  1.00 20.07 ? 86  SER B CB  1 
ATOM   2871 O  OG  . SER B  1 86  ? -24.803 7.513   12.602  1.00 30.71 ? 86  SER B OG  1 
ATOM   2872 N  N   . ALA B  1 87  ? -22.053 5.589   9.971   1.00 12.77 ? 87  ALA B N   1 
ATOM   2873 C  CA  . ALA B  1 87  ? -21.207 5.406   8.721   1.00 12.44 ? 87  ALA B CA  1 
ATOM   2874 C  C   . ALA B  1 87  ? -21.041 6.719   8.042   1.00 14.26 ? 87  ALA B C   1 
ATOM   2875 O  O   . ALA B  1 87  ? -22.000 7.565   8.033   1.00 14.89 ? 87  ALA B O   1 
ATOM   2876 C  CB  . ALA B  1 87  ? -21.716 4.350   7.871   1.00 15.41 ? 87  ALA B CB  1 
ATOM   2877 N  N   . THR B  1 88  ? -19.864 6.952   7.478   1.00 11.90 ? 88  THR B N   1 
ATOM   2878 C  CA  . THR B  1 88  ? -19.755 8.092   6.554   1.00 13.07 ? 88  THR B CA  1 
ATOM   2879 C  C   . THR B  1 88  ? -19.257 7.694   5.175   1.00 10.24 ? 88  THR B C   1 
ATOM   2880 O  O   . THR B  1 88  ? -19.715 8.164   4.159   1.00 10.50 ? 88  THR B O   1 
ATOM   2881 C  CB  . THR B  1 88  ? -18.893 9.144   7.111   1.00 13.07 ? 88  THR B CB  1 
ATOM   2882 O  OG1 . THR B  1 88  ? -19.011 10.286  6.165   1.00 21.90 ? 88  THR B OG1 1 
ATOM   2883 C  CG2 . THR B  1 88  ? -17.460 8.689   7.477   1.00 11.90 ? 88  THR B CG2 1 
ATOM   2884 N  N   . GLN B  1 89  ? -18.284 6.723   5.107   1.00 9.42  ? 89  GLN B N   1 
ATOM   2885 C  CA  . GLN B  1 89  ? -17.786 6.304   3.786   1.00 9.31  ? 89  GLN B CA  1 
ATOM   2886 C  C   . GLN B  1 89  ? -16.989 5.024   3.957   1.00 7.95  ? 89  GLN B C   1 
ATOM   2887 O  O   . GLN B  1 89  ? -16.560 4.704   5.096   1.00 8.50  ? 89  GLN B O   1 
ATOM   2888 C  CB  . GLN B  1 89  ? -16.869 7.398   3.130   1.00 9.10  ? 89  GLN B CB  1 
ATOM   2889 C  CG  . GLN B  1 89  ? -15.719 7.852   4.036   1.00 11.32 ? 89  GLN B CG  1 
ATOM   2890 C  CD  . GLN B  1 89  ? -14.382 7.291   3.632   1.00 10.21 ? 89  GLN B CD  1 
ATOM   2891 O  OE1 . GLN B  1 89  ? -14.221 6.170   3.272   1.00 10.04 ? 89  GLN B OE1 1 
ATOM   2892 N  NE2 . GLN B  1 89  ? -13.392 8.138   3.617   1.00 16.13 ? 89  GLN B NE2 1 
ATOM   2893 N  N   . LEU B  1 90  ? -16.820 4.319   2.879   1.00 6.78  ? 90  LEU B N   1 
ATOM   2894 C  CA  . LEU B  1 90  ? -15.815 3.202   2.844   1.00 7.46  ? 90  LEU B CA  1 
ATOM   2895 C  C   . LEU B  1 90  ? -14.835 3.444   1.693   1.00 7.91  ? 90  LEU B C   1 
ATOM   2896 O  O   . LEU B  1 90  ? -15.158 4.085   0.722   1.00 7.73  ? 90  LEU B O   1 
ATOM   2897 C  CB  . LEU B  1 90  ? -16.480 1.756   2.799   1.00 7.32  ? 90  LEU B CB  1 
ATOM   2898 C  CG  . LEU B  1 90  ? -17.468 1.501   1.729   1.00 7.65  ? 90  LEU B CG  1 
ATOM   2899 C  CD1 . LEU B  1 90  ? -16.758 1.180   0.394   1.00 9.07  ? 90  LEU B CD1 1 
ATOM   2900 C  CD2 . LEU B  1 90  ? -18.307 0.278   2.108   1.00 8.58  ? 90  LEU B CD2 1 
ATOM   2901 N  N   . HIS B  1 91  ? -13.629 2.830   1.808   1.00 7.01  ? 91  HIS B N   1 
ATOM   2902 C  CA  . HIS B  1 91  ? -12.650 2.957   0.724   1.00 7.31  ? 91  HIS B CA  1 
ATOM   2903 C  C   . HIS B  1 91  ? -11.682 1.797   0.883   1.00 6.96  ? 91  HIS B C   1 
ATOM   2904 O  O   . HIS B  1 91  ? -11.760 0.990   1.841   1.00 6.70  ? 91  HIS B O   1 
ATOM   2905 C  CB  . HIS B  1 91  ? -11.955 4.347   0.857   1.00 6.54  ? 91  HIS B CB  1 
ATOM   2906 C  CG  . HIS B  1 91  ? -11.232 4.495   2.147   1.00 6.40  ? 91  HIS B CG  1 
ATOM   2907 N  ND1 . HIS B  1 91  ? -11.773 5.040   3.293   1.00 6.90  ? 91  HIS B ND1 1 
ATOM   2908 C  CD2 . HIS B  1 91  ? -9.943  4.036   2.529   1.00 6.92  ? 91  HIS B CD2 1 
ATOM   2909 C  CE1 . HIS B  1 91  ? -10.930 4.963   4.341   1.00 6.90  ? 91  HIS B CE1 1 
ATOM   2910 N  NE2 . HIS B  1 91  ? -9.773  4.307   3.890   1.00 6.12  ? 91  HIS B NE2 1 
ATOM   2911 N  N   . LEU B  1 92  ? -10.707 1.742   -0.012  1.00 6.60  ? 92  LEU B N   1 
ATOM   2912 C  CA  . LEU B  1 92  ? -9.734  0.645   -0.042  1.00 6.34  ? 92  LEU B CA  1 
ATOM   2913 C  C   . LEU B  1 92  ? -8.275  1.101   -0.151  1.00 6.29  ? 92  LEU B C   1 
ATOM   2914 O  O   . LEU B  1 92  ? -7.995  2.250   -0.504  1.00 7.08  ? 92  LEU B O   1 
ATOM   2915 C  CB  . LEU B  1 92  ? -10.043 -0.281  -1.148  1.00 8.10  ? 92  LEU B CB  1 
ATOM   2916 C  CG  . LEU B  1 92  ? -11.476 -0.999  -1.113  1.00 8.38  ? 92  LEU B CG  1 
ATOM   2917 C  CD1 . LEU B  1 92  ? -12.479 -0.409  -1.974  1.00 13.48 ? 92  LEU B CD1 1 
ATOM   2918 C  CD2 . LEU B  1 92  ? -11.340 -2.447  -1.373  1.00 12.13 ? 92  LEU B CD2 1 
ATOM   2919 N  N   . HIS B  1 93  ? -7.394  0.175   0.227   1.00 7.09  ? 93  HIS B N   1 
ATOM   2920 C  CA  . HIS B  1 93  ? -5.932  0.315   0.004   1.00 6.49  ? 93  HIS B CA  1 
ATOM   2921 C  C   . HIS B  1 93  ? -5.431  -0.900  -0.647  1.00 6.97  ? 93  HIS B C   1 
ATOM   2922 O  O   . HIS B  1 93  ? -5.915  -2.008  -0.349  1.00 7.41  ? 93  HIS B O   1 
ATOM   2923 C  CB  . HIS B  1 93  ? -5.280  0.447   1.346   1.00 6.49  ? 93  HIS B CB  1 
ATOM   2924 C  CG  . HIS B  1 93  ? -5.765  1.632   2.124   1.00 6.30  ? 93  HIS B CG  1 
ATOM   2925 N  ND1 . HIS B  1 93  ? -5.187  2.914   2.067   1.00 6.67  ? 93  HIS B ND1 1 
ATOM   2926 C  CD2 . HIS B  1 93  ? -6.796  1.714   3.006   1.00 6.07  ? 93  HIS B CD2 1 
ATOM   2927 C  CE1 . HIS B  1 93  ? -5.854  3.784   2.889   1.00 7.65  ? 93  HIS B CE1 1 
ATOM   2928 N  NE2 . HIS B  1 93  ? -6.875  3.093   3.467   1.00 5.81  ? 93  HIS B NE2 1 
ATOM   2929 N  N   . TRP B  1 94  ? -4.469  -0.798  -1.568  1.00 6.35  ? 94  TRP B N   1 
ATOM   2930 C  CA  . TRP B  1 94  ? -3.991  -1.951  -2.382  1.00 6.10  ? 94  TRP B CA  1 
ATOM   2931 C  C   . TRP B  1 94  ? -2.564  -1.689  -2.856  1.00 5.97  ? 94  TRP B C   1 
ATOM   2932 O  O   . TRP B  1 94  ? -1.950  -0.631  -2.602  1.00 6.38  ? 94  TRP B O   1 
ATOM   2933 C  CB  . TRP B  1 94  ? -4.956  -2.226  -3.521  1.00 6.87  ? 94  TRP B CB  1 
ATOM   2934 C  CG  . TRP B  1 94  ? -5.082  -1.018  -4.475  1.00 6.91  ? 94  TRP B CG  1 
ATOM   2935 C  CD1 . TRP B  1 94  ? -4.277  -0.737  -5.556  1.00 7.15  ? 94  TRP B CD1 1 
ATOM   2936 C  CD2 . TRP B  1 94  ? -6.081  0.044   -4.384  1.00 6.89  ? 94  TRP B CD2 1 
ATOM   2937 N  NE1 . TRP B  1 94  ? -4.729  0.411   -6.177  1.00 7.83  ? 94  TRP B NE1 1 
ATOM   2938 C  CE2 . TRP B  1 94  ? -5.860  0.901   -5.503  1.00 6.85  ? 94  TRP B CE2 1 
ATOM   2939 C  CE3 . TRP B  1 94  ? -7.153  0.312   -3.543  1.00 7.22  ? 94  TRP B CE3 1 
ATOM   2940 C  CZ2 . TRP B  1 94  ? -6.661  2.036   -5.738  1.00 7.52  ? 94  TRP B CZ2 1 
ATOM   2941 C  CZ3 . TRP B  1 94  ? -7.914  1.474   -3.736  1.00 7.24  ? 94  TRP B CZ3 1 
ATOM   2942 C  CH2 . TRP B  1 94  ? -7.675  2.329   -4.863  1.00 7.36  ? 94  TRP B CH2 1 
ATOM   2943 N  N   . GLY B  1 95  ? -2.045  -2.736  -3.505  1.00 6.81  ? 95  GLY B N   1 
ATOM   2944 C  CA  . GLY B  1 95  ? -0.629  -2.749  -3.984  1.00 7.95  ? 95  GLY B CA  1 
ATOM   2945 C  C   . GLY B  1 95  ? -0.600  -2.417  -5.451  1.00 7.70  ? 95  GLY B C   1 
ATOM   2946 O  O   . GLY B  1 95  ? -1.072  -1.398  -5.943  1.00 8.98  ? 95  GLY B O   1 
ATOM   2947 N  N   . ASN B  1 96  ? -0.049  -3.331  -6.251  1.00 8.46  ? 96  ASN B N   1 
ATOM   2948 C  CA  . ASN B  1 96  ? 0.062   -3.098  -7.688  1.00 9.62  ? 96  ASN B CA  1 
ATOM   2949 C  C   . ASN B  1 96  ? 0.071   -4.440  -8.383  1.00 9.98  ? 96  ASN B C   1 
ATOM   2950 O  O   . ASN B  1 96  ? 0.255   -5.456  -7.743  1.00 9.00  ? 96  ASN B O   1 
ATOM   2951 C  CB  . ASN B  1 96  ? 1.340   -2.275  -8.005  1.00 11.29 ? 96  ASN B CB  1 
ATOM   2952 C  CG  . ASN B  1 96  ? 2.670   -3.010  -7.773  1.00 13.28 ? 96  ASN B CG  1 
ATOM   2953 O  OD1 . ASN B  1 96  ? 3.051   -3.834  -8.642  1.00 17.80 ? 96  ASN B OD1 1 
ATOM   2954 N  ND2 . ASN B  1 96  ? 3.327   -2.849  -6.693  1.00 14.05 ? 96  ASN B ND2 1 
ATOM   2955 N  N   . PRO B  1 97  ? -0.031  -4.455  -9.759  1.00 10.01 ? 97  PRO B N   1 
ATOM   2956 C  CA  . PRO B  1 97  ? -0.183  -5.712  -10.435 1.00 12.21 ? 97  PRO B CA  1 
ATOM   2957 C  C   . PRO B  1 97  ? 0.991   -6.673  -10.277 1.00 10.40 ? 97  PRO B C   1 
ATOM   2958 O  O   . PRO B  1 97  ? 0.749   -7.931  -10.341 1.00 13.03 ? 97  PRO B O   1 
ATOM   2959 C  CB  . PRO B  1 97  ? -0.281  -5.280  -11.917 1.00 12.88 ? 97  PRO B CB  1 
ATOM   2960 C  CG  . PRO B  1 97  ? -0.988  -3.887  -11.805 1.00 12.87 ? 97  PRO B CG  1 
ATOM   2961 C  CD  . PRO B  1 97  ? -0.218  -3.309  -10.671 1.00 11.98 ? 97  PRO B CD  1 
ATOM   2962 N  N   . ASN B  1 98  ? 2.173   -6.147  -10.059 1.00 9.32  ? 98  ASN B N   1 
ATOM   2963 C  CA  . ASN B  1 98  ? 3.338   -7.019  -9.930  1.00 11.77 ? 98  ASN B CA  1 
ATOM   2964 C  C   . ASN B  1 98  ? 3.620   -7.337  -8.488  1.00 14.98 ? 98  ASN B C   1 
ATOM   2965 O  O   . ASN B  1 98  ? 4.607   -7.997  -8.193  1.00 18.74 ? 98  ASN B O   1 
ATOM   2966 C  CB  . ASN B  1 98  ? 4.541   -6.293  -10.620 1.00 12.22 ? 98  ASN B CB  1 
ATOM   2967 C  CG  . ASN B  1 98  ? 4.336   -6.103  -12.111 1.00 11.52 ? 98  ASN B CG  1 
ATOM   2968 O  OD1 . ASN B  1 98  ? 4.204   -7.080  -12.854 1.00 13.02 ? 98  ASN B OD1 1 
ATOM   2969 N  ND2 . ASN B  1 98  ? 4.182   -4.821  -12.522 1.00 13.81 ? 98  ASN B ND2 1 
ATOM   2970 N  N   . ASP B  1 99  ? 2.945   -6.742  -7.549  1.00 12.84 ? 99  ASP B N   1 
ATOM   2971 C  CA  . ASP B  1 99  ? 3.140   -7.021  -6.086  1.00 12.87 ? 99  ASP B CA  1 
ATOM   2972 C  C   . ASP B  1 99  ? 1.763   -6.769  -5.427  1.00 10.11 ? 99  ASP B C   1 
ATOM   2973 O  O   . ASP B  1 99  ? 1.541   -5.661  -4.880  1.00 10.28 ? 99  ASP B O   1 
ATOM   2974 C  CB  . ASP B  1 99  ? 4.180   -6.059  -5.461  1.00 16.64 ? 99  ASP B CB  1 
ATOM   2975 C  CG  . ASP B  1 99  ? 4.467   -6.387  -3.980  1.00 20.61 ? 99  ASP B CG  1 
ATOM   2976 O  OD1 . ASP B  1 99  ? 3.961   -7.455  -3.556  1.00 22.63 ? 99  ASP B OD1 1 
ATOM   2977 O  OD2 . ASP B  1 99  ? 5.043   -5.502  -3.300  1.00 28.17 ? 99  ASP B OD2 1 
ATOM   2978 N  N   . PRO B  1 100 ? 0.854   -7.752  -5.522  1.00 9.52  ? 100 PRO B N   1 
ATOM   2979 C  CA  . PRO B  1 100 ? -0.521  -7.568  -4.934  1.00 10.35 ? 100 PRO B CA  1 
ATOM   2980 C  C   . PRO B  1 100 ? -0.490  -7.792  -3.451  1.00 10.21 ? 100 PRO B C   1 
ATOM   2981 O  O   . PRO B  1 100 ? -1.106  -8.732  -2.947  1.00 11.33 ? 100 PRO B O   1 
ATOM   2982 C  CB  . PRO B  1 100 ? -1.405  -8.570  -5.755  1.00 11.81 ? 100 PRO B CB  1 
ATOM   2983 C  CG  . PRO B  1 100 ? -0.343  -9.629  -6.138  1.00 11.39 ? 100 PRO B CG  1 
ATOM   2984 C  CD  . PRO B  1 100 ? 0.958   -8.960  -6.336  1.00 11.87 ? 100 PRO B CD  1 
ATOM   2985 N  N   . HIS B  1 101 ? 0.169   -6.938  -2.717  1.00 10.23 ? 101 HIS B N   1 
ATOM   2986 C  CA  . HIS B  1 101 ? 0.379   -7.086  -1.260  1.00 10.74 ? 101 HIS B CA  1 
ATOM   2987 C  C   . HIS B  1 101 ? 0.306   -5.759  -0.639  1.00 10.78 ? 101 HIS B C   1 
ATOM   2988 O  O   . HIS B  1 101 ? 1.223   -5.328  0.102   1.00 15.05 ? 101 HIS B O   1 
ATOM   2989 C  CB  . HIS B  1 101 ? 1.680   -7.836  -0.867  1.00 12.16 ? 101 HIS B CB  1 
ATOM   2990 C  CG  . HIS B  1 101 ? 1.716   -9.156  -1.444  1.00 15.24 ? 101 HIS B CG  1 
ATOM   2991 N  ND1 . HIS B  1 101 ? 1.063   -10.239 -0.950  1.00 21.11 ? 101 HIS B ND1 1 
ATOM   2992 C  CD2 . HIS B  1 101 ? 2.294   -9.550  -2.637  1.00 14.68 ? 101 HIS B CD2 1 
ATOM   2993 C  CE1 . HIS B  1 101 ? 1.280   -11.288 -1.793  1.00 20.15 ? 101 HIS B CE1 1 
ATOM   2994 N  NE2 . HIS B  1 101 ? 2.011   -10.870 -2.809  1.00 21.33 ? 101 HIS B NE2 1 
ATOM   2995 N  N   . GLY B  1 102 ? -0.863  -5.137  -0.670  1.00 9.41  ? 102 GLY B N   1 
ATOM   2996 C  CA  . GLY B  1 102 ? -1.017  -3.741  -0.273  1.00 8.97  ? 102 GLY B CA  1 
ATOM   2997 C  C   . GLY B  1 102 ? -2.000  -3.513  0.895   1.00 7.76  ? 102 GLY B C   1 
ATOM   2998 O  O   . GLY B  1 102 ? -2.483  -2.391  1.035   1.00 8.27  ? 102 GLY B O   1 
ATOM   2999 N  N   . SER B  1 103 ? -2.243  -4.501  1.772   1.00 7.81  ? 103 SER B N   1 
ATOM   3000 C  CA  . SER B  1 103 ? -2.923  -4.133  2.980   1.00 6.94  ? 103 SER B CA  1 
ATOM   3001 C  C   . SER B  1 103 ? -2.166  -3.151  3.826   1.00 7.72  ? 103 SER B C   1 
ATOM   3002 O  O   . SER B  1 103 ? -0.917  -3.050  3.708   1.00 9.18  ? 103 SER B O   1 
ATOM   3003 C  CB  . SER B  1 103 ? -3.305  -5.380  3.813   1.00 7.09  ? 103 SER B CB  1 
ATOM   3004 O  OG  . SER B  1 103 ? -2.084  -5.950  4.415   1.00 7.59  ? 103 SER B OG  1 
ATOM   3005 N  N   . GLU B  1 104 ? -2.837  -2.424  4.706   1.00 6.96  ? 104 GLU B N   1 
ATOM   3006 C  CA  . GLU B  1 104 ? -2.223  -1.514  5.624   1.00 7.15  ? 104 GLU B CA  1 
ATOM   3007 C  C   . GLU B  1 104 ? -1.757  -2.220  6.905   1.00 6.97  ? 104 GLU B C   1 
ATOM   3008 O  O   . GLU B  1 104 ? -0.581  -2.255  7.228   1.00 8.25  ? 104 GLU B O   1 
ATOM   3009 C  CB  . GLU B  1 104 ? -3.091  -0.289  5.984   1.00 6.96  ? 104 GLU B CB  1 
ATOM   3010 C  CG  . GLU B  1 104 ? -3.540  0.429   4.694   1.00 7.37  ? 104 GLU B CG  1 
ATOM   3011 C  CD  . GLU B  1 104 ? -3.618  1.895   4.972   1.00 7.30  ? 104 GLU B CD  1 
ATOM   3012 O  OE1 . GLU B  1 104 ? -4.586  2.359   5.581   1.00 8.51  ? 104 GLU B OE1 1 
ATOM   3013 O  OE2 . GLU B  1 104 ? -2.676  2.612   4.647   1.00 8.54  ? 104 GLU B OE2 1 
ATOM   3014 N  N   . HIS B  1 105 ? -2.721  -2.842  7.596   1.00 7.89  ? 105 HIS B N   1 
ATOM   3015 C  CA  . HIS B  1 105 ? -2.326  -3.679  8.729   1.00 7.70  ? 105 HIS B CA  1 
ATOM   3016 C  C   . HIS B  1 105 ? -1.705  -4.944  8.181   1.00 8.88  ? 105 HIS B C   1 
ATOM   3017 O  O   . HIS B  1 105 ? -2.056  -5.441  7.108   1.00 8.45  ? 105 HIS B O   1 
ATOM   3018 C  CB  . HIS B  1 105 ? -3.570  -4.024  9.544   1.00 7.93  ? 105 HIS B CB  1 
ATOM   3019 C  CG  . HIS B  1 105 ? -4.130  -2.855  10.258  1.00 8.32  ? 105 HIS B CG  1 
ATOM   3020 N  ND1 . HIS B  1 105 ? -5.045  -2.051  9.688   1.00 8.19  ? 105 HIS B ND1 1 
ATOM   3021 C  CD2 . HIS B  1 105 ? -3.804  -2.308  11.500  1.00 7.77  ? 105 HIS B CD2 1 
ATOM   3022 C  CE1 . HIS B  1 105 ? -5.287  -0.995  10.512  1.00 8.43  ? 105 HIS B CE1 1 
ATOM   3023 N  NE2 . HIS B  1 105 ? -4.528  -1.167  11.655  1.00 9.01  ? 105 HIS B NE2 1 
ATOM   3024 N  N   . THR B  1 106 ? -0.714  -5.468  8.975   1.00 9.29  ? 106 THR B N   1 
ATOM   3025 C  CA  . THR B  1 106 ? -0.095  -6.787  8.667   1.00 9.06  ? 106 THR B CA  1 
ATOM   3026 C  C   . THR B  1 106 ? -0.337  -7.698  9.829   1.00 8.98  ? 106 THR B C   1 
ATOM   3027 O  O   . THR B  1 106 ? -0.708  -7.249  10.891  1.00 9.37  ? 106 THR B O   1 
ATOM   3028 C  CB  . THR B  1 106 ? 1.385   -6.561  8.383   1.00 9.50  ? 106 THR B CB  1 
ATOM   3029 O  OG1 . THR B  1 106 ? 2.071   -5.964  9.508   1.00 10.43 ? 106 THR B OG1 1 
ATOM   3030 C  CG2 . THR B  1 106 ? 1.563   -5.681  7.128   1.00 11.74 ? 106 THR B CG2 1 
ATOM   3031 N  N   . VAL B  1 107 ? -0.216  -9.000  9.568   1.00 11.09 ? 107 VAL B N   1 
ATOM   3032 C  CA  . VAL B  1 107 ? -0.446  -9.982  10.631  1.00 12.67 ? 107 VAL B CA  1 
ATOM   3033 C  C   . VAL B  1 107 ? 0.748   -10.872 10.639  1.00 11.48 ? 107 VAL B C   1 
ATOM   3034 O  O   . VAL B  1 107 ? 1.141   -11.456 9.647   1.00 12.93 ? 107 VAL B O   1 
ATOM   3035 C  CB  . VAL B  1 107 ? -1.728  -10.860 10.353  1.00 11.56 ? 107 VAL B CB  1 
ATOM   3036 C  CG1 . VAL B  1 107 ? -1.846  -11.871 11.522  1.00 14.35 ? 107 VAL B CG1 1 
ATOM   3037 C  CG2 . VAL B  1 107 ? -3.027  -10.015 10.376  1.00 13.84 ? 107 VAL B CG2 1 
ATOM   3038 N  N   . SER B  1 108 ? 1.383   -10.809 11.826  1.00 12.71 ? 108 SER B N   1 
ATOM   3039 C  CA  . SER B  1 108 ? 2.691   -11.556 12.022  1.00 14.43 ? 108 SER B CA  1 
ATOM   3040 C  C   . SER B  1 108 ? 3.600   -11.272 10.846  1.00 13.65 ? 108 SER B C   1 
ATOM   3041 O  O   . SER B  1 108 ? 4.231   -12.168 10.228  1.00 15.24 ? 108 SER B O   1 
ATOM   3042 C  CB  . SER B  1 108 ? 2.436   -13.073 12.175  1.00 17.03 ? 108 SER B CB  1 
ATOM   3043 O  OG  . SER B  1 108 ? 1.628   -13.281 13.318  1.00 16.98 ? 108 SER B OG  1 
ATOM   3044 N  N   . GLY B  1 109 ? 3.714   -9.996  10.484  1.00 14.27 ? 109 GLY B N   1 
ATOM   3045 C  CA  . GLY B  1 109 ? 4.649   -9.548  9.510   1.00 13.87 ? 109 GLY B CA  1 
ATOM   3046 C  C   . GLY B  1 109 ? 4.217   -9.638  8.035   1.00 15.63 ? 109 GLY B C   1 
ATOM   3047 O  O   . GLY B  1 109 ? 4.995   -9.159  7.197   1.00 20.66 ? 109 GLY B O   1 
ATOM   3048 N  N   . GLN B  1 110 ? 3.067   -10.203 7.755   1.00 15.35 ? 110 GLN B N   1 
ATOM   3049 C  CA  . GLN B  1 110 ? 2.656   -10.530 6.334   1.00 15.24 ? 110 GLN B CA  1 
ATOM   3050 C  C   . GLN B  1 110 ? 1.545   -9.507  5.919   1.00 11.99 ? 110 GLN B C   1 
ATOM   3051 O  O   . GLN B  1 110 ? 0.569   -9.274  6.674   1.00 11.06 ? 110 GLN B O   1 
ATOM   3052 C  CB  . GLN B  1 110 ? 2.049   -11.930 6.296   1.00 17.63 ? 110 GLN B CB  1 
ATOM   3053 C  CG  . GLN B  1 110 ? 2.931   -13.101 6.977   1.00 18.06 ? 110 GLN B CG  1 
ATOM   3054 C  CD  . GLN B  1 110 ? 4.366   -13.040 6.447   1.00 25.76 ? 110 GLN B CD  1 
ATOM   3055 O  OE1 . GLN B  1 110 ? 4.589   -13.255 5.252   1.00 26.48 ? 110 GLN B OE1 1 
ATOM   3056 N  NE2 . GLN B  1 110 ? 5.339   -12.654 7.336   1.00 28.47 ? 110 GLN B NE2 1 
ATOM   3057 N  N   . HIS B  1 111 ? 1.708   -8.952  4.726   1.00 11.97 ? 111 HIS B N   1 
ATOM   3058 C  CA  . HIS B  1 111 ? 0.653   -8.174  4.086   1.00 10.57 ? 111 HIS B CA  1 
ATOM   3059 C  C   . HIS B  1 111 ? -0.334  -9.088  3.473   1.00 11.07 ? 111 HIS B C   1 
ATOM   3060 O  O   . HIS B  1 111 ? 0.029   -10.176 2.893   1.00 15.44 ? 111 HIS B O   1 
ATOM   3061 C  CB  . HIS B  1 111 ? 1.150   -7.345  2.909   1.00 12.53 ? 111 HIS B CB  1 
ATOM   3062 C  CG  . HIS B  1 111 ? 1.860   -6.130  3.321   1.00 12.05 ? 111 HIS B CG  1 
ATOM   3063 N  ND1 . HIS B  1 111 ? 1.232   -4.942  3.559   1.00 13.16 ? 111 HIS B ND1 1 
ATOM   3064 C  CD2 . HIS B  1 111 ? 3.201   -5.947  3.650   1.00 14.86 ? 111 HIS B CD2 1 
ATOM   3065 C  CE1 . HIS B  1 111 ? 2.172   -4.019  3.957   1.00 13.70 ? 111 HIS B CE1 1 
ATOM   3066 N  NE2 . HIS B  1 111 ? 3.367   -4.619  4.049   1.00 16.80 ? 111 HIS B NE2 1 
ATOM   3067 N  N   . PHE B  1 112 ? -1.597  -8.711  3.508   1.00 8.79  ? 112 PHE B N   1 
ATOM   3068 C  CA  . PHE B  1 112 ? -2.661  -9.180  2.703   1.00 9.35  ? 112 PHE B CA  1 
ATOM   3069 C  C   . PHE B  1 112 ? -2.673  -8.440  1.376   1.00 7.36  ? 112 PHE B C   1 
ATOM   3070 O  O   . PHE B  1 112 ? -1.943  -7.449  1.206   1.00 8.88  ? 112 PHE B O   1 
ATOM   3071 C  CB  . PHE B  1 112 ? -3.995  -9.172  3.467   1.00 11.29 ? 112 PHE B CB  1 
ATOM   3072 C  CG  . PHE B  1 112 ? -4.082  -10.258 4.489   1.00 11.30 ? 112 PHE B CG  1 
ATOM   3073 C  CD1 . PHE B  1 112 ? -4.752  -11.372 4.170   1.00 15.42 ? 112 PHE B CD1 1 
ATOM   3074 C  CD2 . PHE B  1 112 ? -3.446  -10.122 5.731   1.00 14.92 ? 112 PHE B CD2 1 
ATOM   3075 C  CE1 . PHE B  1 112 ? -4.817  -12.460 5.068   1.00 19.83 ? 112 PHE B CE1 1 
ATOM   3076 C  CE2 . PHE B  1 112 ? -3.570  -11.211 6.662   1.00 17.78 ? 112 PHE B CE2 1 
ATOM   3077 C  CZ  . PHE B  1 112 ? -4.223  -12.335 6.256   1.00 17.51 ? 112 PHE B CZ  1 
ATOM   3078 N  N   . ALA B  1 113 ? -3.485  -8.875  0.422   1.00 7.89  ? 113 ALA B N   1 
ATOM   3079 C  CA  . ALA B  1 113 ? -3.516  -8.249  -0.906  1.00 8.14  ? 113 ALA B CA  1 
ATOM   3080 C  C   . ALA B  1 113 ? -4.018  -6.841  -0.810  1.00 7.68  ? 113 ALA B C   1 
ATOM   3081 O  O   . ALA B  1 113 ? -3.533  -5.975  -1.567  1.00 8.17  ? 113 ALA B O   1 
ATOM   3082 C  CB  . ALA B  1 113 ? -4.391  -9.103  -1.806  1.00 9.44  ? 113 ALA B CB  1 
ATOM   3083 N  N   . ALA B  1 114 ? -5.060  -6.595  0.030   1.00 7.21  ? 114 ALA B N   1 
ATOM   3084 C  CA  . ALA B  1 114 ? -5.678  -5.233  0.037   1.00 6.41  ? 114 ALA B CA  1 
ATOM   3085 C  C   . ALA B  1 114 ? -6.414  -5.147  1.366   1.00 6.48  ? 114 ALA B C   1 
ATOM   3086 O  O   . ALA B  1 114 ? -6.380  -6.047  2.221   1.00 6.75  ? 114 ALA B O   1 
ATOM   3087 C  CB  . ALA B  1 114 ? -6.646  -5.047  -1.153  1.00 6.90  ? 114 ALA B CB  1 
ATOM   3088 N  N   . GLU B  1 115 ? -7.046  -3.990  1.573   1.00 6.14  ? 115 GLU B N   1 
ATOM   3089 C  CA  . GLU B  1 115 ? -7.778  -3.730  2.820   1.00 6.06  ? 115 GLU B CA  1 
ATOM   3090 C  C   . GLU B  1 115 ? -8.920  -2.814  2.588   1.00 7.30  ? 115 GLU B C   1 
ATOM   3091 O  O   . GLU B  1 115 ? -8.762  -1.785  1.881   1.00 7.86  ? 115 GLU B O   1 
ATOM   3092 C  CB  . GLU B  1 115 ? -6.811  -3.215  3.884   1.00 7.18  ? 115 GLU B CB  1 
ATOM   3093 C  CG  . GLU B  1 115 ? -7.335  -3.104  5.288   1.00 8.14  ? 115 GLU B CG  1 
ATOM   3094 C  CD  . GLU B  1 115 ? -6.265  -2.803  6.343   1.00 7.89  ? 115 GLU B CD  1 
ATOM   3095 O  OE1 . GLU B  1 115 ? -6.521  -2.181  7.392   1.00 7.62  ? 115 GLU B OE1 1 
ATOM   3096 O  OE2 . GLU B  1 115 ? -5.116  -3.296  6.162   1.00 8.07  ? 115 GLU B OE2 1 
ATOM   3097 N  N   . LEU B  1 116 ? -10.083 -3.110  3.188   1.00 6.13  ? 116 LEU B N   1 
ATOM   3098 C  CA  . LEU B  1 116 ? -11.295 -2.261  3.121   1.00 6.62  ? 116 LEU B CA  1 
ATOM   3099 C  C   . LEU B  1 116 ? -11.413 -1.559  4.448   1.00 6.83  ? 116 LEU B C   1 
ATOM   3100 O  O   . LEU B  1 116 ? -11.256 -2.209  5.550   1.00 6.67  ? 116 LEU B O   1 
ATOM   3101 C  CB  . LEU B  1 116 ? -12.544 -3.131  2.949   1.00 8.14  ? 116 LEU B CB  1 
ATOM   3102 C  CG  . LEU B  1 116 ? -13.877 -2.375  3.116   1.00 7.76  ? 116 LEU B CG  1 
ATOM   3103 C  CD1 . LEU B  1 116 ? -14.150 -1.577  1.856   1.00 9.55  ? 116 LEU B CD1 1 
ATOM   3104 C  CD2 . LEU B  1 116 ? -14.971 -3.423  3.260   1.00 8.96  ? 116 LEU B CD2 1 
ATOM   3105 N  N   . HIS B  1 117 ? -11.646 -0.256  4.452   1.00 6.23  ? 117 HIS B N   1 
ATOM   3106 C  CA  . HIS B  1 117 ? -11.979 0.507   5.643   1.00 6.37  ? 117 HIS B CA  1 
ATOM   3107 C  C   . HIS B  1 117 ? -13.372 1.076   5.575   1.00 7.02  ? 117 HIS B C   1 
ATOM   3108 O  O   . HIS B  1 117 ? -13.736 1.724   4.565   1.00 7.20  ? 117 HIS B O   1 
ATOM   3109 C  CB  . HIS B  1 117 ? -11.035 1.689   5.766   1.00 6.65  ? 117 HIS B CB  1 
ATOM   3110 C  CG  . HIS B  1 117 ? -9.641  1.235   6.143   1.00 6.53  ? 117 HIS B CG  1 
ATOM   3111 N  ND1 . HIS B  1 117 ? -8.509  1.971   5.869   1.00 6.25  ? 117 HIS B ND1 1 
ATOM   3112 C  CD2 . HIS B  1 117 ? -9.214  0.046   6.657   1.00 7.20  ? 117 HIS B CD2 1 
ATOM   3113 C  CE1 . HIS B  1 117 ? -7.431  1.308   6.296   1.00 6.94  ? 117 HIS B CE1 1 
ATOM   3114 N  NE2 . HIS B  1 117 ? -7.839  0.106   6.779   1.00 6.70  ? 117 HIS B NE2 1 
ATOM   3115 N  N   . ILE B  1 118 ? -14.173 0.834   6.650   1.00 7.73  ? 118 ILE B N   1 
ATOM   3116 C  CA  . ILE B  1 118 ? -15.541 1.435   6.690   1.00 7.76  ? 118 ILE B CA  1 
ATOM   3117 C  C   . ILE B  1 118 ? -15.511 2.402   7.828   1.00 7.48  ? 118 ILE B C   1 
ATOM   3118 O  O   . ILE B  1 118 ? -15.282 2.039   9.018   1.00 7.90  ? 118 ILE B O   1 
ATOM   3119 C  CB  . ILE B  1 118 ? -16.609 0.333   6.924   1.00 7.87  ? 118 ILE B CB  1 
ATOM   3120 C  CG1 . ILE B  1 118 ? -16.509 -0.834  5.964   1.00 8.15  ? 118 ILE B CG1 1 
ATOM   3121 C  CG2 . ILE B  1 118 ? -17.984 1.094   6.877   1.00 9.97  ? 118 ILE B CG2 1 
ATOM   3122 C  CD1 . ILE B  1 118 ? -17.531 -2.022  6.206   1.00 10.48 ? 118 ILE B CD1 1 
ATOM   3123 N  N   . VAL B  1 119 ? -15.548 3.721   7.506   1.00 8.32  ? 119 VAL B N   1 
ATOM   3124 C  CA  . VAL B  1 119 ? -15.279 4.823   8.454   1.00 8.71  ? 119 VAL B CA  1 
ATOM   3125 C  C   . VAL B  1 119 ? -16.659 5.258   9.040   1.00 8.18  ? 119 VAL B C   1 
ATOM   3126 O  O   . VAL B  1 119 ? -17.632 5.470   8.296   1.00 9.81  ? 119 VAL B O   1 
ATOM   3127 C  CB  . VAL B  1 119 ? -14.681 6.047   7.671   1.00 9.32  ? 119 VAL B CB  1 
ATOM   3128 C  CG1 . VAL B  1 119 ? -14.312 7.165   8.600   1.00 10.96 ? 119 VAL B CG1 1 
ATOM   3129 C  CG2 . VAL B  1 119 ? -13.414 5.566   6.853   1.00 10.31 ? 119 VAL B CG2 1 
ATOM   3130 N  N   . HIS B  1 120 ? -16.619 5.392   10.362  1.00 9.24  ? 120 HIS B N   1 
ATOM   3131 C  CA  . HIS B  1 120 ? -17.794 5.884   11.134  1.00 10.86 ? 120 HIS B CA  1 
ATOM   3132 C  C   . HIS B  1 120 ? -17.297 6.977   12.069  1.00 10.19 ? 120 HIS B C   1 
ATOM   3133 O  O   . HIS B  1 120 ? -16.165 7.137   12.475  1.00 11.57 ? 120 HIS B O   1 
ATOM   3134 C  CB  . HIS B  1 120 ? -18.403 4.718   11.989  1.00 11.17 ? 120 HIS B CB  1 
ATOM   3135 C  CG  . HIS B  1 120 ? -18.754 3.496   11.278  1.00 9.78  ? 120 HIS B CG  1 
ATOM   3136 N  ND1 . HIS B  1 120 ? -17.759 2.619   10.746  1.00 10.89 ? 120 HIS B ND1 1 
ATOM   3137 C  CD2 . HIS B  1 120 ? -19.970 2.869   11.034  1.00 10.67 ? 120 HIS B CD2 1 
ATOM   3138 C  CE1 . HIS B  1 120 ? -18.366 1.576   10.190  1.00 11.49 ? 120 HIS B CE1 1 
ATOM   3139 N  NE2 . HIS B  1 120 ? -19.767 1.687   10.377  1.00 12.03 ? 120 HIS B NE2 1 
ATOM   3140 N  N   . TYR B  1 121 ? -18.287 7.827   12.508  1.00 13.68 ? 121 TYR B N   1 
ATOM   3141 C  CA  . TYR B  1 121 ? -18.018 8.872   13.425  1.00 17.24 ? 121 TYR B CA  1 
ATOM   3142 C  C   . TYR B  1 121 ? -19.113 8.767   14.584  1.00 19.49 ? 121 TYR B C   1 
ATOM   3143 O  O   . TYR B  1 121 ? -20.174 8.188   14.401  1.00 18.87 ? 121 TYR B O   1 
ATOM   3144 C  CB  . TYR B  1 121 ? -18.108 10.252  12.713  1.00 18.90 ? 121 TYR B CB  1 
ATOM   3145 C  CG  . TYR B  1 121 ? -19.496 10.617  12.178  1.00 18.79 ? 121 TYR B CG  1 
ATOM   3146 C  CD1 . TYR B  1 121 ? -20.336 11.500  12.864  1.00 25.94 ? 121 TYR B CD1 1 
ATOM   3147 C  CD2 . TYR B  1 121 ? -19.949 10.096  10.970  1.00 20.09 ? 121 TYR B CD2 1 
ATOM   3148 C  CE1 . TYR B  1 121 ? -21.582 11.839  12.356  1.00 26.41 ? 121 TYR B CE1 1 
ATOM   3149 C  CE2 . TYR B  1 121 ? -21.210 10.424  10.468  1.00 24.53 ? 121 TYR B CE2 1 
ATOM   3150 C  CZ  . TYR B  1 121 ? -22.017 11.304  11.165  1.00 27.99 ? 121 TYR B CZ  1 
ATOM   3151 O  OH  . TYR B  1 121 ? -23.260 11.652  10.696  1.00 33.74 ? 121 TYR B OH  1 
ATOM   3152 N  N   . ASN B  1 122 ? -18.799 9.340   15.697  1.00 20.59 ? 122 ASN B N   1 
ATOM   3153 C  CA  . ASN B  1 122 ? -19.841 9.299   16.766  1.00 20.60 ? 122 ASN B CA  1 
ATOM   3154 C  C   . ASN B  1 122 ? -21.045 10.265  16.488  1.00 21.52 ? 122 ASN B C   1 
ATOM   3155 O  O   . ASN B  1 122 ? -20.867 11.475  16.686  1.00 22.78 ? 122 ASN B O   1 
ATOM   3156 C  CB  . ASN B  1 122 ? -19.195 9.682   18.067  1.00 25.06 ? 122 ASN B CB  1 
ATOM   3157 C  CG  . ASN B  1 122 ? -20.131 9.497   19.260  1.00 28.38 ? 122 ASN B CG  1 
ATOM   3158 O  OD1 . ASN B  1 122 ? -21.378 9.612   19.167  1.00 30.04 ? 122 ASN B OD1 1 
ATOM   3159 N  ND2 . ASN B  1 122 ? -19.531 9.089   20.365  1.00 32.13 ? 122 ASN B ND2 1 
ATOM   3160 N  N   . SER B  1 123 ? -22.160 9.750   15.974  1.00 26.50 ? 123 SER B N   1 
ATOM   3161 C  CA  . SER B  1 123 ? -23.270 10.652  15.621  1.00 26.25 ? 123 SER B CA  1 
ATOM   3162 C  C   . SER B  1 123 ? -24.038 11.103  16.866  1.00 35.24 ? 123 SER B C   1 
ATOM   3163 O  O   . SER B  1 123 ? -24.871 12.048  16.749  1.00 33.27 ? 123 SER B O   1 
ATOM   3164 C  CB  . SER B  1 123 ? -24.221 10.032  14.597  1.00 29.39 ? 123 SER B CB  1 
ATOM   3165 O  OG  . SER B  1 123 ? -24.333 8.656   14.822  1.00 30.59 ? 123 SER B OG  1 
ATOM   3166 N  N   . ASP B  1 124 ? -23.799 10.427  18.002  1.00 30.64 ? 124 ASP B N   1 
ATOM   3167 C  CA  . ASP B  1 124 ? -24.410 10.824  19.291  1.00 33.21 ? 124 ASP B CA  1 
ATOM   3168 C  C   . ASP B  1 124 ? -23.900 12.219  19.695  1.00 36.46 ? 124 ASP B C   1 
ATOM   3169 O  O   . ASP B  1 124 ? -24.623 13.059  20.275  1.00 28.87 ? 124 ASP B O   1 
ATOM   3170 C  CB  . ASP B  1 124 ? -24.140 9.758   20.405  1.00 32.51 ? 124 ASP B CB  1 
ATOM   3171 C  CG  . ASP B  1 124 ? -25.028 8.470   20.277  1.00 39.02 ? 124 ASP B CG  1 
ATOM   3172 O  OD1 . ASP B  1 124 ? -26.019 8.505   19.495  1.00 41.79 ? 124 ASP B OD1 1 
ATOM   3173 O  OD2 . ASP B  1 124 ? -24.761 7.425   20.975  1.00 36.64 ? 124 ASP B OD2 1 
ATOM   3174 N  N   . LEU B  1 125 ? -22.642 12.455  19.390  1.00 31.19 ? 125 LEU B N   1 
ATOM   3175 C  CA  . LEU B  1 125 ? -21.835 13.641  19.783  1.00 30.96 ? 125 LEU B CA  1 
ATOM   3176 C  C   . LEU B  1 125 ? -21.530 14.656  18.703  1.00 34.53 ? 125 LEU B C   1 
ATOM   3177 O  O   . LEU B  1 125 ? -21.288 15.847  18.992  1.00 38.36 ? 125 LEU B O   1 
ATOM   3178 C  CB  . LEU B  1 125 ? -20.518 13.135  20.480  1.00 25.57 ? 125 LEU B CB  1 
ATOM   3179 C  CG  . LEU B  1 125 ? -20.333 12.796  21.990  1.00 31.05 ? 125 LEU B CG  1 
ATOM   3180 C  CD1 . LEU B  1 125 ? -19.738 11.422  22.303  1.00 29.89 ? 125 LEU B CD1 1 
ATOM   3181 C  CD2 . LEU B  1 125 ? -19.494 13.860  22.683  1.00 25.24 ? 125 LEU B CD2 1 
ATOM   3182 N  N   . TYR B  1 126 ? -21.605 14.257  17.431  1.00 32.09 ? 126 TYR B N   1 
ATOM   3183 C  CA  . TYR B  1 126 ? -21.178 15.200  16.368  1.00 30.21 ? 126 TYR B CA  1 
ATOM   3184 C  C   . TYR B  1 126 ? -22.081 15.141  15.198  1.00 34.20 ? 126 TYR B C   1 
ATOM   3185 O  O   . TYR B  1 126 ? -22.693 14.053  14.914  1.00 31.13 ? 126 TYR B O   1 
ATOM   3186 C  CB  . TYR B  1 126 ? -19.668 14.980  15.991  1.00 36.53 ? 126 TYR B CB  1 
ATOM   3187 C  CG  . TYR B  1 126 ? -18.835 14.846  17.247  1.00 34.33 ? 126 TYR B CG  1 
ATOM   3188 C  CD1 . TYR B  1 126 ? -18.628 15.961  18.105  1.00 41.90 ? 126 TYR B CD1 1 
ATOM   3189 C  CD2 . TYR B  1 126 ? -18.305 13.603  17.640  1.00 34.26 ? 126 TYR B CD2 1 
ATOM   3190 C  CE1 . TYR B  1 126 ? -17.933 15.822  19.305  1.00 39.23 ? 126 TYR B CE1 1 
ATOM   3191 C  CE2 . TYR B  1 126 ? -17.602 13.466  18.820  1.00 31.50 ? 126 TYR B CE2 1 
ATOM   3192 C  CZ  . TYR B  1 126 ? -17.408 14.554  19.663  1.00 36.43 ? 126 TYR B CZ  1 
ATOM   3193 O  OH  . TYR B  1 126 ? -16.696 14.390  20.867  1.00 31.71 ? 126 TYR B OH  1 
ATOM   3194 N  N   . PRO B  1 127 ? -22.183 16.305  14.500  1.00 39.65 ? 127 PRO B N   1 
ATOM   3195 C  CA  . PRO B  1 127 ? -22.951 16.679  13.304  1.00 40.88 ? 127 PRO B CA  1 
ATOM   3196 C  C   . PRO B  1 127 ? -22.523 15.975  11.993  1.00 39.01 ? 127 PRO B C   1 
ATOM   3197 O  O   . PRO B  1 127 ? -23.355 15.755  11.090  1.00 46.86 ? 127 PRO B O   1 
ATOM   3198 C  CB  . PRO B  1 127 ? -22.701 18.204  13.200  1.00 40.32 ? 127 PRO B CB  1 
ATOM   3199 C  CG  . PRO B  1 127 ? -21.403 18.453  13.933  1.00 41.64 ? 127 PRO B CG  1 
ATOM   3200 C  CD  . PRO B  1 127 ? -21.447 17.465  15.062  1.00 41.35 ? 127 PRO B CD  1 
ATOM   3201 N  N   . ASP B  1 128 ? -21.254 15.573  11.930  1.00 37.68 ? 128 ASP B N   1 
ATOM   3202 C  CA  . ASP B  1 128 ? -20.678 14.918  10.789  1.00 31.18 ? 128 ASP B CA  1 
ATOM   3203 C  C   . ASP B  1 128 ? -19.269 14.440  11.217  1.00 31.39 ? 128 ASP B C   1 
ATOM   3204 O  O   . ASP B  1 128 ? -18.802 14.685  12.368  1.00 31.15 ? 128 ASP B O   1 
ATOM   3205 C  CB  . ASP B  1 128 ? -20.543 15.949  9.669   1.00 37.15 ? 128 ASP B CB  1 
ATOM   3206 C  CG  . ASP B  1 128 ? -19.652 17.102  10.054  1.00 36.61 ? 128 ASP B CG  1 
ATOM   3207 O  OD1 . ASP B  1 128 ? -19.899 17.706  11.108  1.00 49.70 ? 128 ASP B OD1 1 
ATOM   3208 O  OD2 . ASP B  1 128 ? -18.713 17.432  9.294   1.00 46.22 ? 128 ASP B OD2 1 
ATOM   3209 N  N   . ALA B  1 129 ? -18.635 13.734  10.272  1.00 31.44 ? 129 ALA B N   1 
ATOM   3210 C  CA  . ALA B  1 129 ? -17.388 13.055  10.418  1.00 29.19 ? 129 ALA B CA  1 
ATOM   3211 C  C   . ALA B  1 129 ? -16.228 14.053  10.459  1.00 34.21 ? 129 ALA B C   1 
ATOM   3212 O  O   . ALA B  1 129 ? -15.304 13.896  11.266  1.00 32.38 ? 129 ALA B O   1 
ATOM   3213 C  CB  . ALA B  1 129 ? -17.218 12.092  9.226   1.00 34.68 ? 129 ALA B CB  1 
ATOM   3214 N  N   . SER B  1 130 ? -16.282 15.104  9.614   1.00 37.97 ? 130 SER B N   1 
ATOM   3215 C  CA  . SER B  1 130 ? -15.298 16.228  9.737   1.00 42.58 ? 130 SER B CA  1 
ATOM   3216 C  C   . SER B  1 130 ? -15.157 16.795  11.173  1.00 44.60 ? 130 SER B C   1 
ATOM   3217 O  O   . SER B  1 130 ? -14.040 16.964  11.655  1.00 44.67 ? 130 SER B O   1 
ATOM   3218 C  CB  . SER B  1 130 ? -15.623 17.380  8.776   1.00 46.92 ? 130 SER B CB  1 
ATOM   3219 O  OG  . SER B  1 130 ? -14.760 17.377  7.667   1.00 53.07 ? 130 SER B OG  1 
ATOM   3220 N  N   . THR B  1 131 ? -16.283 17.061  11.846  1.00 41.06 ? 131 THR B N   1 
ATOM   3221 C  CA  . THR B  1 131 ? -16.293 17.629  13.187  1.00 40.25 ? 131 THR B CA  1 
ATOM   3222 C  C   . THR B  1 131 ? -15.758 16.631  14.204  1.00 35.00 ? 131 THR B C   1 
ATOM   3223 O  O   . THR B  1 131 ? -15.107 17.008  15.168  1.00 36.15 ? 131 THR B O   1 
ATOM   3224 C  CB  . THR B  1 131 ? -17.769 18.016  13.542  1.00 46.68 ? 131 THR B CB  1 
ATOM   3225 O  OG1 . THR B  1 131 ? -18.207 19.007  12.615  1.00 51.07 ? 131 THR B OG1 1 
ATOM   3226 C  CG2 . THR B  1 131 ? -17.978 18.562  15.001  1.00 41.50 ? 131 THR B CG2 1 
ATOM   3227 N  N   . ALA B  1 132 ? -16.055 15.330  13.967  1.00 36.31 ? 132 ALA B N   1 
ATOM   3228 C  CA  . ALA B  1 132 ? -15.694 14.221  14.912  1.00 30.60 ? 132 ALA B CA  1 
ATOM   3229 C  C   . ALA B  1 132 ? -14.155 13.888  14.966  1.00 27.90 ? 132 ALA B C   1 
ATOM   3230 O  O   . ALA B  1 132 ? -13.610 13.315  15.931  1.00 23.07 ? 132 ALA B O   1 
ATOM   3231 C  CB  . ALA B  1 132 ? -16.492 12.975  14.547  1.00 34.26 ? 132 ALA B CB  1 
ATOM   3232 N  N   . SER B  1 133 ? -13.542 14.287  13.882  1.00 26.23 ? 133 SER B N   1 
ATOM   3233 C  CA  . SER B  1 133 ? -12.205 13.839  13.578  1.00 28.63 ? 133 SER B CA  1 
ATOM   3234 C  C   . SER B  1 133 ? -11.087 14.346  14.501  1.00 28.15 ? 133 SER B C   1 
ATOM   3235 O  O   . SER B  1 133 ? -10.016 13.728  14.532  1.00 22.03 ? 133 SER B O   1 
ATOM   3236 C  CB  . SER B  1 133 ? -11.971 14.103  12.111  1.00 26.23 ? 133 SER B CB  1 
ATOM   3237 O  OG  . SER B  1 133 ? -11.738 15.494  11.851  1.00 31.42 ? 133 SER B OG  1 
ATOM   3238 N  N   . ASN B  1 134 ? -11.292 15.422  15.288  1.00 29.74 ? 134 ASN B N   1 
ATOM   3239 C  CA  . ASN B  1 134 ? -10.294 15.797  16.299  1.00 32.94 ? 134 ASN B CA  1 
ATOM   3240 C  C   . ASN B  1 134 ? -10.673 15.460  17.678  1.00 41.90 ? 134 ASN B C   1 
ATOM   3241 O  O   . ASN B  1 134 ? -9.930  15.787  18.615  1.00 48.06 ? 134 ASN B O   1 
ATOM   3242 C  CB  . ASN B  1 134 ? -9.991  17.289  16.317  1.00 37.01 ? 134 ASN B CB  1 
ATOM   3243 C  CG  . ASN B  1 134 ? -9.978  17.851  14.958  1.00 42.45 ? 134 ASN B CG  1 
ATOM   3244 O  OD1 . ASN B  1 134 ? -9.101  17.531  14.159  1.00 46.29 ? 134 ASN B OD1 1 
ATOM   3245 N  ND2 . ASN B  1 134 ? -10.981 18.634  14.647  1.00 33.82 ? 134 ASN B ND2 1 
ATOM   3246 N  N   . LYS B  1 135 ? -11.803 14.795  17.846  1.00 39.76 ? 135 LYS B N   1 
ATOM   3247 C  CA  . LYS B  1 135 ? -12.260 14.534  19.218  1.00 42.00 ? 135 LYS B CA  1 
ATOM   3248 C  C   . LYS B  1 135 ? -11.873 13.132  19.572  1.00 41.28 ? 135 LYS B C   1 
ATOM   3249 O  O   . LYS B  1 135 ? -11.880 12.233  18.695  1.00 32.92 ? 135 LYS B O   1 
ATOM   3250 C  CB  . LYS B  1 135 ? -13.757 14.773  19.359  1.00 46.57 ? 135 LYS B CB  1 
ATOM   3251 N  N   . SER B  1 136 ? -11.491 12.941  20.830  1.00 40.05 ? 136 SER B N   1 
ATOM   3252 C  CA  . SER B  1 136 ? -11.109 11.630  21.320  1.00 46.22 ? 136 SER B CA  1 
ATOM   3253 C  C   . SER B  1 136 ? -12.186 10.618  20.910  1.00 37.76 ? 136 SER B C   1 
ATOM   3254 O  O   . SER B  1 136 ? -13.388 10.887  21.059  1.00 37.13 ? 136 SER B O   1 
ATOM   3255 C  CB  . SER B  1 136 ? -10.942 11.616  22.866  1.00 54.93 ? 136 SER B CB  1 
ATOM   3256 O  OG  . SER B  1 136 ? -12.203 11.651  23.551  1.00 47.53 ? 136 SER B OG  1 
ATOM   3257 N  N   . GLU B  1 137 ? -11.720 9.477   20.387  1.00 37.17 ? 137 GLU B N   1 
ATOM   3258 C  CA  . GLU B  1 137 ? -12.584 8.403   19.756  1.00 38.79 ? 137 GLU B CA  1 
ATOM   3259 C  C   . GLU B  1 137 ? -13.808 8.979   19.014  1.00 32.92 ? 137 GLU B C   1 
ATOM   3260 O  O   . GLU B  1 137 ? -14.920 8.416   19.089  1.00 30.29 ? 137 GLU B O   1 
ATOM   3261 C  CB  . GLU B  1 137 ? -12.967 7.285   20.763  1.00 44.43 ? 137 GLU B CB  1 
ATOM   3262 C  CG  . GLU B  1 137 ? -13.911 7.748   21.879  1.00 54.18 ? 137 GLU B CG  1 
ATOM   3263 C  CD  . GLU B  1 137 ? -13.541 7.253   23.283  1.00 60.31 ? 137 GLU B CD  1 
ATOM   3264 O  OE1 . GLU B  1 137 ? -13.327 6.015   23.455  1.00 52.04 ? 137 GLU B OE1 1 
ATOM   3265 O  OE2 . GLU B  1 137 ? -13.488 8.123   24.209  1.00 55.83 ? 137 GLU B OE2 1 
ATOM   3266 N  N   . GLY B  1 138 ? -13.603 10.042  18.228  1.00 19.92 ? 138 GLY B N   1 
ATOM   3267 C  CA  . GLY B  1 138 ? -14.638 10.615  17.458  1.00 21.70 ? 138 GLY B CA  1 
ATOM   3268 C  C   . GLY B  1 138 ? -14.882 9.644   16.312  1.00 14.80 ? 138 GLY B C   1 
ATOM   3269 O  O   . GLY B  1 138 ? -15.949 9.729   15.648  1.00 19.69 ? 138 GLY B O   1 
ATOM   3270 N  N   . LEU B  1 139 ? -13.818 8.879   15.888  1.00 16.32 ? 139 LEU B N   1 
ATOM   3271 C  CA  . LEU B  1 139 ? -13.990 7.982   14.696  1.00 14.11 ? 139 LEU B CA  1 
ATOM   3272 C  C   . LEU B  1 139 ? -13.843 6.523   15.061  1.00 12.80 ? 139 LEU B C   1 
ATOM   3273 O  O   . LEU B  1 139 ? -13.099 6.209   15.965  1.00 13.18 ? 139 LEU B O   1 
ATOM   3274 C  CB  . LEU B  1 139 ? -12.990 8.353   13.569  1.00 13.52 ? 139 LEU B CB  1 
ATOM   3275 C  CG  . LEU B  1 139 ? -12.998 9.810   13.132  1.00 14.50 ? 139 LEU B CG  1 
ATOM   3276 C  CD1 . LEU B  1 139 ? -11.777 9.994   12.184  1.00 13.68 ? 139 LEU B CD1 1 
ATOM   3277 C  CD2 . LEU B  1 139 ? -14.328 10.081  12.481  1.00 16.13 ? 139 LEU B CD2 1 
ATOM   3278 N  N   . ALA B  1 140 ? -14.546 5.661   14.370  1.00 11.05 ? 140 ALA B N   1 
ATOM   3279 C  CA  . ALA B  1 140 ? -14.336 4.190   14.534  1.00 11.08 ? 140 ALA B CA  1 
ATOM   3280 C  C   . ALA B  1 140 ? -14.242 3.720   13.060  1.00 10.99 ? 140 ALA B C   1 
ATOM   3281 O  O   . ALA B  1 140 ? -15.154 3.943   12.206  1.00 12.79 ? 140 ALA B O   1 
ATOM   3282 C  CB  . ALA B  1 140 ? -15.521 3.529   15.246  1.00 12.89 ? 140 ALA B CB  1 
ATOM   3283 N  N   . VAL B  1 141 ? -13.138 3.015   12.787  1.00 9.16  ? 141 VAL B N   1 
ATOM   3284 C  CA  . VAL B  1 141 ? -13.010 2.457   11.450  1.00 9.03  ? 141 VAL B CA  1 
ATOM   3285 C  C   . VAL B  1 141 ? -12.973 0.928   11.573  1.00 8.69  ? 141 VAL B C   1 
ATOM   3286 O  O   . VAL B  1 141 ? -12.219 0.394   12.440  1.00 10.22 ? 141 VAL B O   1 
ATOM   3287 C  CB  . VAL B  1 141 ? -11.709 3.006   10.782  1.00 8.95  ? 141 VAL B CB  1 
ATOM   3288 C  CG1 . VAL B  1 141 ? -11.580 2.406   9.359   1.00 9.87  ? 141 VAL B CG1 1 
ATOM   3289 C  CG2 . VAL B  1 141 ? -11.730 4.560   10.707  1.00 9.43  ? 141 VAL B CG2 1 
ATOM   3290 N  N   . LEU B  1 142 ? -13.768 0.276   10.724  1.00 7.85  ? 142 LEU B N   1 
ATOM   3291 C  CA  . LEU B  1 142 ? -13.677 -1.190  10.649  1.00 8.62  ? 142 LEU B CA  1 
ATOM   3292 C  C   . LEU B  1 142 ? -12.751 -1.516  9.504   1.00 9.09  ? 142 LEU B C   1 
ATOM   3293 O  O   . LEU B  1 142 ? -12.905 -0.951  8.402   1.00 9.69  ? 142 LEU B O   1 
ATOM   3294 C  CB  . LEU B  1 142 ? -15.043 -1.794  10.336  1.00 8.59  ? 142 LEU B CB  1 
ATOM   3295 C  CG  . LEU B  1 142 ? -16.221 -1.475  11.199  1.00 11.61 ? 142 LEU B CG  1 
ATOM   3296 C  CD1 . LEU B  1 142 ? -17.470 -2.173  10.691  1.00 14.25 ? 142 LEU B CD1 1 
ATOM   3297 C  CD2 . LEU B  1 142 ? -15.946 -1.795  12.648  1.00 12.36 ? 142 LEU B CD2 1 
ATOM   3298 N  N   . ALA B  1 143 ? -11.843 -2.452  9.697   1.00 7.79  ? 143 ALA B N   1 
ATOM   3299 C  CA  . ALA B  1 143 ? -10.944 -2.888  8.653   1.00 7.46  ? 143 ALA B CA  1 
ATOM   3300 C  C   . ALA B  1 143 ? -11.107 -4.356  8.294   1.00 7.15  ? 143 ALA B C   1 
ATOM   3301 O  O   . ALA B  1 143 ? -11.215 -5.240  9.224   1.00 8.06  ? 143 ALA B O   1 
ATOM   3302 C  CB  . ALA B  1 143 ? -9.482  -2.709  9.154   1.00 9.01  ? 143 ALA B CB  1 
ATOM   3303 N  N   . VAL B  1 144 ? -11.224 -4.658  7.021   1.00 6.70  ? 144 VAL B N   1 
ATOM   3304 C  CA  . VAL B  1 144 ? -11.340 -6.008  6.519   1.00 7.50  ? 144 VAL B CA  1 
ATOM   3305 C  C   . VAL B  1 144 ? -10.105 -6.294  5.672   1.00 7.78  ? 144 VAL B C   1 
ATOM   3306 O  O   . VAL B  1 144 ? -9.790  -5.571  4.716   1.00 7.53  ? 144 VAL B O   1 
ATOM   3307 C  CB  . VAL B  1 144 ? -12.606 -6.197  5.679   1.00 7.35  ? 144 VAL B CB  1 
ATOM   3308 C  CG1 . VAL B  1 144 ? -12.652 -7.662  5.183   1.00 8.32  ? 144 VAL B CG1 1 
ATOM   3309 C  CG2 . VAL B  1 144 ? -13.860 -5.863  6.487   1.00 8.94  ? 144 VAL B CG2 1 
ATOM   3310 N  N   . LEU B  1 145 ? -9.364  -7.320  6.068   1.00 8.23  ? 145 LEU B N   1 
ATOM   3311 C  CA  . LEU B  1 145 ? -8.225  -7.830  5.309   1.00 7.47  ? 145 LEU B CA  1 
ATOM   3312 C  C   . LEU B  1 145 ? -8.699  -8.596  4.126   1.00 7.80  ? 145 LEU B C   1 
ATOM   3313 O  O   . LEU B  1 145 ? -9.644  -9.389  4.207   1.00 8.12  ? 145 LEU B O   1 
ATOM   3314 C  CB  . LEU B  1 145 ? -7.358  -8.690  6.259   1.00 8.91  ? 145 LEU B CB  1 
ATOM   3315 C  CG  . LEU B  1 145 ? -6.818  -7.912  7.484   1.00 9.84  ? 145 LEU B CG  1 
ATOM   3316 C  CD1 . LEU B  1 145 ? -6.263  -8.957  8.503   1.00 11.80 ? 145 LEU B CD1 1 
ATOM   3317 C  CD2 . LEU B  1 145 ? -5.718  -6.962  7.124   1.00 12.21 ? 145 LEU B CD2 1 
ATOM   3318 N  N   . ILE B  1 146 ? -8.113  -8.345  2.961   1.00 7.60  ? 146 ILE B N   1 
ATOM   3319 C  CA  . ILE B  1 146 ? -8.501  -8.966  1.701   1.00 8.27  ? 146 ILE B CA  1 
ATOM   3320 C  C   . ILE B  1 146 ? -7.382  -9.835  1.153   1.00 7.94  ? 146 ILE B C   1 
ATOM   3321 O  O   . ILE B  1 146 ? -6.241  -9.303  0.962   1.00 8.47  ? 146 ILE B O   1 
ATOM   3322 C  CB  . ILE B  1 146 ? -8.887  -7.866  0.688   1.00 8.31  ? 146 ILE B CB  1 
ATOM   3323 C  CG1 . ILE B  1 146 ? -10.086 -7.060  1.199   1.00 9.92  ? 146 ILE B CG1 1 
ATOM   3324 C  CG2 . ILE B  1 146 ? -9.203  -8.520  -0.666  1.00 8.85  ? 146 ILE B CG2 1 
ATOM   3325 C  CD1 . ILE B  1 146 ? -10.416 -5.782  0.368   1.00 10.88 ? 146 ILE B CD1 1 
ATOM   3326 N  N   A GLU B  1 147 ? -7.612  -11.120 0.930   0.50 8.36  ? 147 GLU B N   1 
ATOM   3327 N  N   B GLU B  1 147 ? -7.724  -11.077 0.842   0.50 7.90  ? 147 GLU B N   1 
ATOM   3328 C  CA  A GLU B  1 147 ? -6.567  -11.979 0.385   0.50 9.56  ? 147 GLU B CA  1 
ATOM   3329 C  CA  B GLU B  1 147 ? -6.767  -12.041 0.305   0.50 8.99  ? 147 GLU B CA  1 
ATOM   3330 C  C   A GLU B  1 147 ? -7.034  -12.385 -1.028  0.50 8.88  ? 147 GLU B C   1 
ATOM   3331 C  C   B GLU B  1 147 ? -7.088  -12.346 -1.145  0.50 8.68  ? 147 GLU B C   1 
ATOM   3332 O  O   A GLU B  1 147 ? -8.256  -12.451 -1.315  0.50 9.12  ? 147 GLU B O   1 
ATOM   3333 O  O   B GLU B  1 147 ? -8.254  -12.316 -1.610  0.50 8.54  ? 147 GLU B O   1 
ATOM   3334 C  CB  A GLU B  1 147 ? -6.414  -13.247 1.251   0.50 12.22 ? 147 GLU B CB  1 
ATOM   3335 C  CB  B GLU B  1 147 ? -6.927  -13.321 1.189   0.50 10.70 ? 147 GLU B CB  1 
ATOM   3336 C  CG  A GLU B  1 147 ? -7.606  -14.196 1.258   0.50 15.38 ? 147 GLU B CG  1 
ATOM   3337 C  CG  B GLU B  1 147 ? -5.937  -14.442 0.882   0.50 11.13 ? 147 GLU B CG  1 
ATOM   3338 C  CD  A GLU B  1 147 ? -7.436  -15.347 2.244   0.50 16.03 ? 147 GLU B CD  1 
ATOM   3339 C  CD  B GLU B  1 147 ? -5.704  -15.412 2.045   0.50 14.14 ? 147 GLU B CD  1 
ATOM   3340 O  OE1 A GLU B  1 147 ? -6.355  -15.486 2.842   0.50 18.15 ? 147 GLU B OE1 1 
ATOM   3341 O  OE1 B GLU B  1 147 ? -6.155  -15.133 3.176   0.50 15.98 ? 147 GLU B OE1 1 
ATOM   3342 O  OE2 A GLU B  1 147 ? -8.401  -16.122 2.421   0.50 18.42 ? 147 GLU B OE2 1 
ATOM   3343 O  OE2 B GLU B  1 147 ? -5.054  -16.453 1.808   0.50 20.37 ? 147 GLU B OE2 1 
ATOM   3344 N  N   . MET B  1 148 ? -6.070  -12.670 -1.910  1.00 8.90  ? 148 MET B N   1 
ATOM   3345 C  CA  . MET B  1 148 ? -6.316  -13.164 -3.240  1.00 8.79  ? 148 MET B CA  1 
ATOM   3346 C  C   . MET B  1 148 ? -6.905  -14.575 -3.170  1.00 8.85  ? 148 MET B C   1 
ATOM   3347 O  O   . MET B  1 148 ? -6.348  -15.457 -2.483  1.00 10.08 ? 148 MET B O   1 
ATOM   3348 C  CB  . MET B  1 148 ? -5.003  -13.200 -4.050  1.00 8.52  ? 148 MET B CB  1 
ATOM   3349 C  CG  . MET B  1 148 ? -5.234  -13.501 -5.507  1.00 9.76  ? 148 MET B CG  1 
ATOM   3350 S  SD  . MET B  1 148 ? -3.695  -13.679 -6.451  1.00 11.46 ? 148 MET B SD  1 
ATOM   3351 C  CE  . MET B  1 148 ? -3.243  -11.937 -6.516  1.00 9.99  ? 148 MET B CE  1 
ATOM   3352 N  N   . GLY B  1 149 ? -8.076  -14.701 -3.798  1.00 8.08  ? 149 GLY B N   1 
ATOM   3353 C  CA  . GLY B  1 149 ? -8.764  -16.007 -3.693  1.00 9.02  ? 149 GLY B CA  1 
ATOM   3354 C  C   . GLY B  1 149 ? -9.888  -16.087 -4.696  1.00 7.37  ? 149 GLY B C   1 
ATOM   3355 O  O   . GLY B  1 149 ? -9.714  -15.775 -5.893  1.00 9.44  ? 149 GLY B O   1 
ATOM   3356 N  N   . SER B  1 150 ? -11.060 -16.525 -4.221  1.00 7.73  ? 150 SER B N   1 
ATOM   3357 C  CA  . SER B  1 150 ? -12.213 -16.616 -5.110  1.00 9.31  ? 150 SER B CA  1 
ATOM   3358 C  C   . SER B  1 150 ? -12.765 -15.225 -5.478  1.00 9.14  ? 150 SER B C   1 
ATOM   3359 O  O   . SER B  1 150 ? -12.746 -14.268 -4.686  1.00 9.94  ? 150 SER B O   1 
ATOM   3360 C  CB  . SER B  1 150 ? -13.331 -17.339 -4.403  1.00 8.31  ? 150 SER B CB  1 
ATOM   3361 O  OG  . SER B  1 150 ? -12.970 -18.732 -4.180  1.00 9.87  ? 150 SER B OG  1 
ATOM   3362 N  N   . PHE B  1 151 ? -13.397 -15.215 -6.658  1.00 9.08  ? 151 PHE B N   1 
ATOM   3363 C  CA  . PHE B  1 151 ? -14.220 -14.088 -7.085  1.00 9.38  ? 151 PHE B CA  1 
ATOM   3364 C  C   . PHE B  1 151 ? -15.254 -13.775 -6.076  1.00 10.17 ? 151 PHE B C   1 
ATOM   3365 O  O   . PHE B  1 151 ? -15.918 -14.657 -5.500  1.00 11.62 ? 151 PHE B O   1 
ATOM   3366 C  CB  . PHE B  1 151 ? -14.884 -14.410 -8.430  1.00 9.65  ? 151 PHE B CB  1 
ATOM   3367 C  CG  . PHE B  1 151 ? -15.733 -13.263 -8.979  1.00 9.73  ? 151 PHE B CG  1 
ATOM   3368 C  CD1 . PHE B  1 151 ? -15.117 -12.160 -9.622  1.00 11.62 ? 151 PHE B CD1 1 
ATOM   3369 C  CD2 . PHE B  1 151 ? -17.126 -13.295 -8.804  1.00 10.98 ? 151 PHE B CD2 1 
ATOM   3370 C  CE1 . PHE B  1 151 ? -15.926 -11.101 -10.047 1.00 11.47 ? 151 PHE B CE1 1 
ATOM   3371 C  CE2 . PHE B  1 151 ? -17.902 -12.186 -9.266  1.00 11.45 ? 151 PHE B CE2 1 
ATOM   3372 C  CZ  . PHE B  1 151 ? -17.272 -11.154 -9.847  1.00 10.89 ? 151 PHE B CZ  1 
ATOM   3373 N  N   . ASN B  1 152 ? -15.456 -12.454 -5.787  1.00 8.56  ? 152 ASN B N   1 
ATOM   3374 C  CA  . ASN B  1 152 ? -16.381 -12.022 -4.765  1.00 8.61  ? 152 ASN B CA  1 
ATOM   3375 C  C   . ASN B  1 152 ? -17.465 -11.119 -5.351  1.00 9.94  ? 152 ASN B C   1 
ATOM   3376 O  O   . ASN B  1 152 ? -17.176 -9.975  -5.734  1.00 9.05  ? 152 ASN B O   1 
ATOM   3377 C  CB  . ASN B  1 152 ? -15.582 -11.249 -3.661  1.00 8.11  ? 152 ASN B CB  1 
ATOM   3378 C  CG  . ASN B  1 152 ? -16.395 -11.023 -2.458  1.00 8.56  ? 152 ASN B CG  1 
ATOM   3379 O  OD1 . ASN B  1 152 ? -17.504 -10.489 -2.525  1.00 9.78  ? 152 ASN B OD1 1 
ATOM   3380 N  ND2 . ASN B  1 152 ? -15.836 -11.271 -1.291  1.00 9.80  ? 152 ASN B ND2 1 
ATOM   3381 N  N   . PRO B  1 153 ? -18.662 -11.631 -5.590  1.00 9.75  ? 153 PRO B N   1 
ATOM   3382 C  CA  . PRO B  1 153 ? -19.701 -10.836 -6.278  1.00 9.81  ? 153 PRO B CA  1 
ATOM   3383 C  C   . PRO B  1 153 ? -20.081 -9.621  -5.468  1.00 11.06 ? 153 PRO B C   1 
ATOM   3384 O  O   . PRO B  1 153 ? -20.469 -8.591  -6.046  1.00 12.30 ? 153 PRO B O   1 
ATOM   3385 C  CB  . PRO B  1 153 ? -20.897 -11.797 -6.319  1.00 12.58 ? 153 PRO B CB  1 
ATOM   3386 C  CG  . PRO B  1 153 ? -20.294 -13.193 -6.207  1.00 17.40 ? 153 PRO B CG  1 
ATOM   3387 C  CD  . PRO B  1 153 ? -19.038 -13.067 -5.370  1.00 11.59 ? 153 PRO B CD  1 
ATOM   3388 N  N   . SER B  1 154 ? -19.951 -9.617  -4.141  1.00 9.81  ? 154 SER B N   1 
ATOM   3389 C  CA  . SER B  1 154 ? -20.335 -8.429  -3.373  1.00 10.03 ? 154 SER B CA  1 
ATOM   3390 C  C   . SER B  1 154 ? -19.345 -7.276  -3.593  1.00 9.73  ? 154 SER B C   1 
ATOM   3391 O  O   . SER B  1 154 ? -19.719 -6.113  -3.795  1.00 9.77  ? 154 SER B O   1 
ATOM   3392 C  CB  . SER B  1 154 ? -20.473 -8.781  -1.863  1.00 12.29 ? 154 SER B CB  1 
ATOM   3393 O  OG  . SER B  1 154 ? -21.447 -9.824  -1.713  1.00 17.14 ? 154 SER B OG  1 
ATOM   3394 N  N   . TYR B  1 155 ? -18.023 -7.583  -3.467  1.00 8.72  ? 155 TYR B N   1 
ATOM   3395 C  CA  . TYR B  1 155 ? -17.030 -6.532  -3.802  1.00 8.10  ? 155 TYR B CA  1 
ATOM   3396 C  C   . TYR B  1 155 ? -17.180 -6.116  -5.234  1.00 7.87  ? 155 TYR B C   1 
ATOM   3397 O  O   . TYR B  1 155 ? -16.843 -4.940  -5.547  1.00 8.10  ? 155 TYR B O   1 
ATOM   3398 C  CB  . TYR B  1 155 ? -15.585 -7.015  -3.477  1.00 8.07  ? 155 TYR B CB  1 
ATOM   3399 C  CG  . TYR B  1 155 ? -15.213 -6.931  -2.012  1.00 7.80  ? 155 TYR B CG  1 
ATOM   3400 C  CD1 . TYR B  1 155 ? -14.472 -5.818  -1.565  1.00 8.51  ? 155 TYR B CD1 1 
ATOM   3401 C  CD2 . TYR B  1 155 ? -15.598 -7.883  -1.067  1.00 7.63  ? 155 TYR B CD2 1 
ATOM   3402 C  CE1 . TYR B  1 155 ? -14.162 -5.672  -0.212  1.00 9.29  ? 155 TYR B CE1 1 
ATOM   3403 C  CE2 . TYR B  1 155 ? -15.335 -7.703  0.288   1.00 8.67  ? 155 TYR B CE2 1 
ATOM   3404 C  CZ  . TYR B  1 155 ? -14.611 -6.623  0.688   1.00 9.06  ? 155 TYR B CZ  1 
ATOM   3405 O  OH  . TYR B  1 155 ? -14.302 -6.466  2.035   1.00 9.93  ? 155 TYR B OH  1 
ATOM   3406 N  N   . ASP B  1 156 ? -17.633 -6.958  -6.143  1.00 7.94  ? 156 ASP B N   1 
ATOM   3407 C  CA  . ASP B  1 156 ? -17.760 -6.567  -7.529  1.00 8.39  ? 156 ASP B CA  1 
ATOM   3408 C  C   . ASP B  1 156 ? -18.837 -5.508  -7.667  1.00 8.95  ? 156 ASP B C   1 
ATOM   3409 O  O   . ASP B  1 156 ? -18.817 -4.830  -8.706  1.00 10.99 ? 156 ASP B O   1 
ATOM   3410 C  CB  . ASP B  1 156 ? -17.901 -7.762  -8.535  1.00 10.17 ? 156 ASP B CB  1 
ATOM   3411 C  CG  . ASP B  1 156 ? -16.990 -7.590  -9.723  1.00 11.20 ? 156 ASP B CG  1 
ATOM   3412 O  OD1 . ASP B  1 156 ? -15.790 -7.345  -9.523  1.00 10.30 ? 156 ASP B OD1 1 
ATOM   3413 O  OD2 . ASP B  1 156 ? -17.477 -7.635  -10.858 1.00 17.32 ? 156 ASP B OD2 1 
ATOM   3414 N  N   . LYS B  1 157 ? -19.748 -5.365  -6.703  1.00 9.75  ? 157 LYS B N   1 
ATOM   3415 C  CA  . LYS B  1 157 ? -20.804 -4.326  -6.815  1.00 10.56 ? 157 LYS B CA  1 
ATOM   3416 C  C   . LYS B  1 157 ? -20.055 -3.002  -6.779  1.00 9.79  ? 157 LYS B C   1 
ATOM   3417 O  O   . LYS B  1 157 ? -20.602 -2.029  -7.352  1.00 11.95 ? 157 LYS B O   1 
ATOM   3418 C  CB  . LYS B  1 157 ? -21.830 -4.479  -5.742  1.00 11.39 ? 157 LYS B CB  1 
ATOM   3419 C  CG  . LYS B  1 157 ? -22.694 -5.741  -5.986  1.00 14.42 ? 157 LYS B CG  1 
ATOM   3420 C  CD  . LYS B  1 157 ? -23.558 -6.113  -4.763  1.00 18.99 ? 157 LYS B CD  1 
ATOM   3421 C  CE  . LYS B  1 157 ? -24.424 -7.355  -5.105  1.00 24.95 ? 157 LYS B CE  1 
ATOM   3422 N  NZ  . LYS B  1 157 ? -25.080 -7.880  -3.823  1.00 27.34 ? 157 LYS B NZ  1 
ATOM   3423 N  N   . ILE B  1 158 ? -18.857 -2.879  -6.165  1.00 9.25  ? 158 ILE B N   1 
ATOM   3424 C  CA  . ILE B  1 158 ? -18.054 -1.625  -6.207  1.00 10.32 ? 158 ILE B CA  1 
ATOM   3425 C  C   . ILE B  1 158 ? -17.154 -1.704  -7.423  1.00 10.33 ? 158 ILE B C   1 
ATOM   3426 O  O   . ILE B  1 158 ? -17.126 -0.742  -8.218  1.00 10.49 ? 158 ILE B O   1 
ATOM   3427 C  CB  . ILE B  1 158 ? -17.231 -1.496  -4.928  1.00 11.60 ? 158 ILE B CB  1 
ATOM   3428 C  CG1 . ILE B  1 158 ? -18.178 -1.319  -3.757  1.00 13.11 ? 158 ILE B CG1 1 
ATOM   3429 C  CG2 . ILE B  1 158 ? -16.228 -0.275  -5.034  1.00 12.42 ? 158 ILE B CG2 1 
ATOM   3430 C  CD1 . ILE B  1 158 ? -17.456 -1.487  -2.404  1.00 15.19 ? 158 ILE B CD1 1 
ATOM   3431 N  N   . PHE B  1 159 ? -16.410 -2.818  -7.694  1.00 9.42  ? 159 PHE B N   1 
ATOM   3432 C  CA  . PHE B  1 159 ? -15.385 -2.815  -8.688  1.00 10.51 ? 159 PHE B CA  1 
ATOM   3433 C  C   . PHE B  1 159 ? -15.943 -2.698  -10.092 1.00 11.08 ? 159 PHE B C   1 
ATOM   3434 O  O   . PHE B  1 159 ? -15.206 -2.237  -11.002 1.00 12.48 ? 159 PHE B O   1 
ATOM   3435 C  CB  . PHE B  1 159 ? -14.517 -4.077  -8.597  1.00 10.58 ? 159 PHE B CB  1 
ATOM   3436 C  CG  . PHE B  1 159 ? -13.854 -4.299  -7.242  1.00 10.91 ? 159 PHE B CG  1 
ATOM   3437 C  CD1 . PHE B  1 159 ? -13.424 -3.243  -6.423  1.00 13.47 ? 159 PHE B CD1 1 
ATOM   3438 C  CD2 . PHE B  1 159 ? -13.522 -5.612  -6.799  1.00 11.60 ? 159 PHE B CD2 1 
ATOM   3439 C  CE1 . PHE B  1 159 ? -12.720 -3.453  -5.195  1.00 12.07 ? 159 PHE B CE1 1 
ATOM   3440 C  CE2 . PHE B  1 159 ? -12.846 -5.750  -5.584  1.00 11.38 ? 159 PHE B CE2 1 
ATOM   3441 C  CZ  . PHE B  1 159 ? -12.402 -4.729  -4.788  1.00 12.26 ? 159 PHE B CZ  1 
ATOM   3442 N  N   . SER B  1 160 ? -17.175 -3.070  -10.313 1.00 11.66 ? 160 SER B N   1 
ATOM   3443 C  CA  . SER B  1 160 ? -17.733 -2.941  -11.651 1.00 12.05 ? 160 SER B CA  1 
ATOM   3444 C  C   . SER B  1 160 ? -17.885 -1.524  -12.059 1.00 13.20 ? 160 SER B C   1 
ATOM   3445 O  O   . SER B  1 160 ? -18.064 -1.310  -13.277 1.00 16.16 ? 160 SER B O   1 
ATOM   3446 C  CB  . SER B  1 160 ? -19.093 -3.702  -11.688 1.00 13.64 ? 160 SER B CB  1 
ATOM   3447 O  OG  . SER B  1 160 ? -20.045 -3.178  -10.841 1.00 15.59 ? 160 SER B OG  1 
ATOM   3448 N  N   . HIS B  1 161 ? -17.752 -0.531  -11.170 1.00 11.75 ? 161 HIS B N   1 
ATOM   3449 C  CA  . HIS B  1 161 ? -17.883 0.915   -11.510 1.00 12.33 ? 161 HIS B CA  1 
ATOM   3450 C  C   . HIS B  1 161 ? -16.540 1.596   -11.657 1.00 14.62 ? 161 HIS B C   1 
ATOM   3451 O  O   . HIS B  1 161 ? -16.541 2.808   -11.929 1.00 14.04 ? 161 HIS B O   1 
ATOM   3452 C  CB  . HIS B  1 161 ? -18.716 1.649   -10.476 1.00 13.47 ? 161 HIS B CB  1 
ATOM   3453 C  CG  . HIS B  1 161 ? -20.131 1.158   -10.432 1.00 14.24 ? 161 HIS B CG  1 
ATOM   3454 N  ND1 . HIS B  1 161 ? -21.108 1.723   -11.209 1.00 17.54 ? 161 HIS B ND1 1 
ATOM   3455 C  CD2 . HIS B  1 161 ? -20.738 0.122   -9.717  1.00 14.26 ? 161 HIS B CD2 1 
ATOM   3456 C  CE1 . HIS B  1 161 ? -22.287 1.064   -11.017 1.00 16.12 ? 161 HIS B CE1 1 
ATOM   3457 N  NE2 . HIS B  1 161 ? -22.065 0.071   -10.121 1.00 14.36 ? 161 HIS B NE2 1 
ATOM   3458 N  N   . LEU B  1 162 ? -15.420 0.877   -11.533 1.00 14.90 ? 162 LEU B N   1 
ATOM   3459 C  CA  . LEU B  1 162 ? -14.110 1.554   -11.434 1.00 14.67 ? 162 LEU B CA  1 
ATOM   3460 C  C   . LEU B  1 162 ? -13.822 2.299   -12.725 1.00 16.60 ? 162 LEU B C   1 
ATOM   3461 O  O   . LEU B  1 162 ? -13.208 3.383   -12.634 1.00 15.37 ? 162 LEU B O   1 
ATOM   3462 C  CB  . LEU B  1 162 ? -13.028 0.505   -11.209 1.00 16.67 ? 162 LEU B CB  1 
ATOM   3463 C  CG  . LEU B  1 162 ? -13.060 -0.121  -9.812  1.00 16.50 ? 162 LEU B CG  1 
ATOM   3464 C  CD1 . LEU B  1 162 ? -11.980 -1.158  -9.741  1.00 18.40 ? 162 LEU B CD1 1 
ATOM   3465 C  CD2 . LEU B  1 162 ? -12.866 0.943   -8.693  1.00 22.05 ? 162 LEU B CD2 1 
ATOM   3466 N  N   . GLN B  1 163 ? -14.266 1.804   -13.895 1.00 17.19 ? 163 GLN B N   1 
ATOM   3467 C  CA  . GLN B  1 163 ? -13.857 2.511   -15.117 1.00 16.26 ? 163 GLN B CA  1 
ATOM   3468 C  C   . GLN B  1 163 ? -14.608 3.816   -15.322 1.00 17.74 ? 163 GLN B C   1 
ATOM   3469 O  O   . GLN B  1 163 ? -14.314 4.498   -16.309 1.00 20.11 ? 163 GLN B O   1 
ATOM   3470 C  CB  . GLN B  1 163 ? -13.950 1.586   -16.390 1.00 20.47 ? 163 GLN B CB  1 
ATOM   3471 C  CG  . GLN B  1 163 ? -13.007 0.340   -16.398 1.00 23.80 ? 163 GLN B CG  1 
ATOM   3472 C  CD  . GLN B  1 163 ? -11.496 0.589   -16.331 1.00 26.62 ? 163 GLN B CD  1 
ATOM   3473 O  OE1 . GLN B  1 163 ? -11.049 1.639   -16.641 1.00 28.30 ? 163 GLN B OE1 1 
ATOM   3474 N  NE2 . GLN B  1 163 ? -10.695 -0.458  -15.894 1.00 28.06 ? 163 GLN B NE2 1 
ATOM   3475 N  N   . HIS B  1 164 ? -15.500 4.175   -14.438 1.00 16.01 ? 164 HIS B N   1 
ATOM   3476 C  CA  . HIS B  1 164 ? -16.219 5.424   -14.399 1.00 16.32 ? 164 HIS B CA  1 
ATOM   3477 C  C   . HIS B  1 164 ? -15.719 6.456   -13.381 1.00 14.16 ? 164 HIS B C   1 
ATOM   3478 O  O   . HIS B  1 164 ? -16.206 7.557   -13.241 1.00 14.56 ? 164 HIS B O   1 
ATOM   3479 C  CB  . HIS B  1 164 ? -17.709 5.041   -14.333 1.00 20.21 ? 164 HIS B CB  1 
ATOM   3480 C  CG  . HIS B  1 164 ? -17.966 3.831   -15.276 1.00 23.18 ? 164 HIS B CG  1 
ATOM   3481 N  ND1 . HIS B  1 164 ? -17.603 3.867   -16.630 1.00 30.86 ? 164 HIS B ND1 1 
ATOM   3482 C  CD2 . HIS B  1 164 ? -18.389 2.484   -15.026 1.00 26.32 ? 164 HIS B CD2 1 
ATOM   3483 C  CE1 . HIS B  1 164 ? -17.854 2.637   -17.212 1.00 28.48 ? 164 HIS B CE1 1 
ATOM   3484 N  NE2 . HIS B  1 164 ? -18.357 1.797   -16.250 1.00 29.33 ? 164 HIS B NE2 1 
ATOM   3485 N  N   . VAL B  1 165 ? -14.716 6.024   -12.575 1.00 12.28 ? 165 VAL B N   1 
ATOM   3486 C  CA  . VAL B  1 165 ? -14.131 6.936   -11.607 1.00 11.50 ? 165 VAL B CA  1 
ATOM   3487 C  C   . VAL B  1 165 ? -12.612 6.855   -11.793 1.00 9.79  ? 165 VAL B C   1 
ATOM   3488 O  O   . VAL B  1 165 ? -11.842 6.876   -10.822 1.00 10.65 ? 165 VAL B O   1 
ATOM   3489 C  CB  . VAL B  1 165 ? -14.577 6.663   -10.136 1.00 12.10 ? 165 VAL B CB  1 
ATOM   3490 C  CG1 . VAL B  1 165 ? -16.050 7.108   -9.946  1.00 14.69 ? 165 VAL B CG1 1 
ATOM   3491 C  CG2 . VAL B  1 165 ? -14.330 5.226   -9.691  1.00 12.15 ? 165 VAL B CG2 1 
ATOM   3492 N  N   . LYS B  1 166 ? -12.120 6.751   -13.019 1.00 9.47  ? 166 LYS B N   1 
ATOM   3493 C  CA  . LYS B  1 166 ? -10.691 6.493   -13.268 1.00 10.35 ? 166 LYS B CA  1 
ATOM   3494 C  C   . LYS B  1 166 ? -9.845  7.661   -12.784 1.00 9.54  ? 166 LYS B C   1 
ATOM   3495 O  O   . LYS B  1 166 ? -8.702  7.425   -12.390 1.00 10.04 ? 166 LYS B O   1 
ATOM   3496 C  CB  . LYS B  1 166 ? -10.462 6.328   -14.769 1.00 11.35 ? 166 LYS B CB  1 
ATOM   3497 C  CG  . LYS B  1 166 ? -10.946 5.006   -15.336 1.00 13.51 ? 166 LYS B CG  1 
ATOM   3498 C  CD  . LYS B  1 166 ? -10.586 4.848   -16.821 1.00 16.17 ? 166 LYS B CD  1 
ATOM   3499 C  CE  . LYS B  1 166 ? -9.114  4.582   -17.020 1.00 16.96 ? 166 LYS B CE  1 
ATOM   3500 N  NZ  . LYS B  1 166 ? -8.751  3.253   -16.401 1.00 16.75 ? 166 LYS B NZ  1 
ATOM   3501 N  N   . TYR B  1 167 ? -10.380 8.877   -12.789 1.00 9.60  ? 167 TYR B N   1 
ATOM   3502 C  CA  . TYR B  1 167 ? -9.528  10.030  -12.529 1.00 9.53  ? 167 TYR B CA  1 
ATOM   3503 C  C   . TYR B  1 167 ? -9.989  10.868  -11.311 1.00 8.75  ? 167 TYR B C   1 
ATOM   3504 O  O   . TYR B  1 167 ? -11.182 10.820  -10.925 1.00 8.97  ? 167 TYR B O   1 
ATOM   3505 C  CB  . TYR B  1 167 ? -9.528  10.994  -13.767 1.00 9.53  ? 167 TYR B CB  1 
ATOM   3506 C  CG  . TYR B  1 167 ? -9.098  10.236  -15.028 1.00 9.54  ? 167 TYR B CG  1 
ATOM   3507 C  CD1 . TYR B  1 167 ? -7.784  9.834   -15.187 1.00 11.82 ? 167 TYR B CD1 1 
ATOM   3508 C  CD2 . TYR B  1 167 ? -10.031 9.919   -16.035 1.00 12.00 ? 167 TYR B CD2 1 
ATOM   3509 C  CE1 . TYR B  1 167 ? -7.381  9.093   -16.317 1.00 12.08 ? 167 TYR B CE1 1 
ATOM   3510 C  CE2 . TYR B  1 167 ? -9.656  9.191   -17.185 1.00 12.66 ? 167 TYR B CE2 1 
ATOM   3511 C  CZ  . TYR B  1 167 ? -8.347  8.776   -17.274 1.00 13.54 ? 167 TYR B CZ  1 
ATOM   3512 O  OH  . TYR B  1 167 ? -8.021  7.994   -18.398 1.00 16.28 ? 167 TYR B OH  1 
ATOM   3513 N  N   . LYS B  1 168 ? -9.037  11.553  -10.689 1.00 8.83  ? 168 LYS B N   1 
ATOM   3514 C  CA  . LYS B  1 168 ? -9.346  12.371  -9.505  1.00 10.00 ? 168 LYS B CA  1 
ATOM   3515 C  C   . LYS B  1 168 ? -10.551 13.302  -9.759  1.00 10.79 ? 168 LYS B C   1 
ATOM   3516 O  O   . LYS B  1 168 ? -10.684 13.958  -10.802 1.00 11.36 ? 168 LYS B O   1 
ATOM   3517 C  CB  . LYS B  1 168 ? -8.138  13.223  -9.141  1.00 10.90 ? 168 LYS B CB  1 
ATOM   3518 C  CG  . LYS B  1 168 ? -8.425  14.027  -7.895  1.00 11.07 ? 168 LYS B CG  1 
ATOM   3519 C  CD  . LYS B  1 168 ? -7.183  14.740  -7.475  1.00 14.24 ? 168 LYS B CD  1 
ATOM   3520 C  CE  . LYS B  1 168 ? -7.553  15.522  -6.205  1.00 19.55 ? 168 LYS B CE  1 
ATOM   3521 N  NZ  . LYS B  1 168 ? -6.417  16.284  -5.598  1.00 27.90 ? 168 LYS B NZ  1 
ATOM   3522 N  N   . GLY B  1 169 ? -11.475 13.287  -8.817  1.00 10.02 ? 169 GLY B N   1 
ATOM   3523 C  CA  . GLY B  1 169 ? -12.708 14.131  -8.813  1.00 12.07 ? 169 GLY B CA  1 
ATOM   3524 C  C   . GLY B  1 169 ? -13.832 13.505  -9.508  1.00 12.49 ? 169 GLY B C   1 
ATOM   3525 O  O   . GLY B  1 169 ? -14.969 14.067  -9.448  1.00 15.61 ? 169 GLY B O   1 
ATOM   3526 N  N   . GLN B  1 170 ? -13.662 12.404  -10.218 1.00 9.36  ? 170 GLN B N   1 
ATOM   3527 C  CA  . GLN B  1 170 ? -14.757 11.827  -10.940 1.00 10.84 ? 170 GLN B CA  1 
ATOM   3528 C  C   . GLN B  1 170 ? -15.679 11.052  -9.909  1.00 11.18 ? 170 GLN B C   1 
ATOM   3529 O  O   . GLN B  1 170 ? -15.216 10.587  -8.890  1.00 11.80 ? 170 GLN B O   1 
ATOM   3530 C  CB  . GLN B  1 170 ? -14.270 10.870  -12.017 1.00 10.14 ? 170 GLN B CB  1 
ATOM   3531 C  CG  . GLN B  1 170 ? -13.557 11.684  -13.146 1.00 11.58 ? 170 GLN B CG  1 
ATOM   3532 C  CD  . GLN B  1 170 ? -13.308 10.792  -14.307 1.00 12.36 ? 170 GLN B CD  1 
ATOM   3533 O  OE1 . GLN B  1 170 ? -12.964 9.608   -14.249 1.00 12.60 ? 170 GLN B OE1 1 
ATOM   3534 N  NE2 . GLN B  1 170 ? -13.443 11.407  -15.529 1.00 17.49 ? 170 GLN B NE2 1 
ATOM   3535 N  N   . GLU B  1 171 ? -16.935 11.030  -10.236 1.00 11.75 ? 171 GLU B N   1 
ATOM   3536 C  CA  . GLU B  1 171 ? -18.000 10.453  -9.376  1.00 12.74 ? 171 GLU B CA  1 
ATOM   3537 C  C   . GLU B  1 171 ? -18.905 9.517   -10.209 1.00 13.29 ? 171 GLU B C   1 
ATOM   3538 O  O   . GLU B  1 171 ? -19.117 9.726   -11.452 1.00 16.02 ? 171 GLU B O   1 
ATOM   3539 C  CB  . GLU B  1 171 ? -18.874 11.640  -8.920  1.00 17.11 ? 171 GLU B CB  1 
ATOM   3540 C  CG  . GLU B  1 171 ? -18.266 12.554  -7.904  1.00 18.78 ? 171 GLU B CG  1 
ATOM   3541 C  CD  . GLU B  1 171 ? -19.232 13.672  -7.547  1.00 21.47 ? 171 GLU B CD  1 
ATOM   3542 O  OE1 . GLU B  1 171 ? -20.207 13.898  -8.303  1.00 29.91 ? 171 GLU B OE1 1 
ATOM   3543 O  OE2 . GLU B  1 171 ? -19.016 14.329  -6.512  1.00 24.94 ? 171 GLU B OE2 1 
ATOM   3544 N  N   . ALA B  1 172 ? -19.425 8.484   -9.595  1.00 13.59 ? 172 ALA B N   1 
ATOM   3545 C  CA  . ALA B  1 172 ? -20.312 7.441   -10.204 1.00 13.36 ? 172 ALA B CA  1 
ATOM   3546 C  C   . ALA B  1 172 ? -21.317 7.080   -9.101  1.00 12.62 ? 172 ALA B C   1 
ATOM   3547 O  O   . ALA B  1 172 ? -21.144 7.480   -7.922  1.00 15.64 ? 172 ALA B O   1 
ATOM   3548 C  CB  . ALA B  1 172 ? -19.536 6.257   -10.701 1.00 14.47 ? 172 ALA B CB  1 
ATOM   3549 N  N   . PHE B  1 173 ? -22.461 6.561   -9.503  1.00 13.53 ? 173 PHE B N   1 
ATOM   3550 C  CA  . PHE B  1 173 ? -23.464 6.071   -8.553  1.00 11.55 ? 173 PHE B CA  1 
ATOM   3551 C  C   . PHE B  1 173 ? -23.512 4.552   -8.582  1.00 12.71 ? 173 PHE B C   1 
ATOM   3552 O  O   . PHE B  1 173 ? -23.454 3.932   -9.662  1.00 18.07 ? 173 PHE B O   1 
ATOM   3553 C  CB  . PHE B  1 173 ? -24.851 6.620   -8.969  1.00 15.24 ? 173 PHE B CB  1 
ATOM   3554 C  CG  . PHE B  1 173 ? -25.116 7.970   -8.406  1.00 18.09 ? 173 PHE B CG  1 
ATOM   3555 C  CD1 . PHE B  1 173 ? -25.225 8.172   -7.015  1.00 20.43 ? 173 PHE B CD1 1 
ATOM   3556 C  CD2 . PHE B  1 173 ? -25.345 9.041   -9.254  1.00 22.38 ? 173 PHE B CD2 1 
ATOM   3557 C  CE1 . PHE B  1 173 ? -25.481 9.418   -6.436  1.00 21.22 ? 173 PHE B CE1 1 
ATOM   3558 C  CE2 . PHE B  1 173 ? -25.591 10.321  -8.706  1.00 23.37 ? 173 PHE B CE2 1 
ATOM   3559 C  CZ  . PHE B  1 173 ? -25.678 10.511  -7.306  1.00 25.94 ? 173 PHE B CZ  1 
ATOM   3560 N  N   . VAL B  1 174 ? -23.555 3.982   -7.401  1.00 11.75 ? 174 VAL B N   1 
ATOM   3561 C  CA  . VAL B  1 174 ? -23.501 2.528   -7.173  1.00 12.80 ? 174 VAL B CA  1 
ATOM   3562 C  C   . VAL B  1 174 ? -24.873 2.190   -6.529  1.00 11.56 ? 174 VAL B C   1 
ATOM   3563 O  O   . VAL B  1 174 ? -25.211 2.733   -5.444  1.00 12.68 ? 174 VAL B O   1 
ATOM   3564 C  CB  . VAL B  1 174 ? -22.367 2.134   -6.219  1.00 11.87 ? 174 VAL B CB  1 
ATOM   3565 C  CG1 . VAL B  1 174 ? -22.445 0.653   -5.888  1.00 13.52 ? 174 VAL B CG1 1 
ATOM   3566 C  CG2 . VAL B  1 174 ? -21.021 2.470   -6.866  1.00 14.83 ? 174 VAL B CG2 1 
ATOM   3567 N  N   . PRO B  1 175 ? -25.659 1.296   -7.182  1.00 10.50 ? 175 PRO B N   1 
ATOM   3568 C  CA  . PRO B  1 175 ? -26.862 0.883   -6.469  1.00 11.33 ? 175 PRO B CA  1 
ATOM   3569 C  C   . PRO B  1 175 ? -26.589 0.336   -5.064  1.00 11.03 ? 175 PRO B C   1 
ATOM   3570 O  O   . PRO B  1 175 ? -25.570 -0.362  -4.831  1.00 11.86 ? 175 PRO B O   1 
ATOM   3571 C  CB  . PRO B  1 175 ? -27.423 -0.201  -7.393  1.00 12.90 ? 175 PRO B CB  1 
ATOM   3572 C  CG  . PRO B  1 175 ? -26.903 0.122   -8.804  1.00 12.63 ? 175 PRO B CG  1 
ATOM   3573 C  CD  . PRO B  1 175 ? -25.482 0.649   -8.472  1.00 11.52 ? 175 PRO B CD  1 
ATOM   3574 N  N   . GLY B  1 176 ? -27.490 0.478   -4.149  1.00 12.84 ? 176 GLY B N   1 
ATOM   3575 C  CA  . GLY B  1 176 ? -27.337 -0.047  -2.795  1.00 11.84 ? 176 GLY B CA  1 
ATOM   3576 C  C   . GLY B  1 176 ? -27.251 -1.589  -2.802  1.00 12.39 ? 176 GLY B C   1 
ATOM   3577 O  O   . GLY B  1 176 ? -27.804 -2.272  -3.642  1.00 12.81 ? 176 GLY B O   1 
ATOM   3578 N  N   . PHE B  1 177 ? -26.450 -2.080  -1.842  1.00 12.32 ? 177 PHE B N   1 
ATOM   3579 C  CA  . PHE B  1 177 ? -26.381 -3.533  -1.592  1.00 11.75 ? 177 PHE B CA  1 
ATOM   3580 C  C   . PHE B  1 177 ? -26.099 -3.628  -0.135  1.00 10.98 ? 177 PHE B C   1 
ATOM   3581 O  O   . PHE B  1 177 ? -25.903 -2.683  0.605   1.00 11.47 ? 177 PHE B O   1 
ATOM   3582 C  CB  . PHE B  1 177 ? -25.312 -4.193  -2.505  1.00 12.80 ? 177 PHE B CB  1 
ATOM   3583 C  CG  . PHE B  1 177 ? -23.880 -3.749  -2.244  1.00 11.92 ? 177 PHE B CG  1 
ATOM   3584 C  CD1 . PHE B  1 177 ? -23.047 -4.542  -1.424  1.00 13.66 ? 177 PHE B CD1 1 
ATOM   3585 C  CD2 . PHE B  1 177 ? -23.415 -2.599  -2.827  1.00 11.74 ? 177 PHE B CD2 1 
ATOM   3586 C  CE1 . PHE B  1 177 ? -21.743 -4.137  -1.199  1.00 12.38 ? 177 PHE B CE1 1 
ATOM   3587 C  CE2 . PHE B  1 177 ? -22.068 -2.158  -2.627  1.00 12.33 ? 177 PHE B CE2 1 
ATOM   3588 C  CZ  . PHE B  1 177 ? -21.282 -2.994  -1.825  1.00 12.21 ? 177 PHE B CZ  1 
ATOM   3589 N  N   . ASN B  1 178 ? -26.088 -4.903  0.317   1.00 12.39 ? 178 ASN B N   1 
ATOM   3590 C  CA  . ASN B  1 178 ? -25.866 -5.166  1.689   1.00 12.30 ? 178 ASN B CA  1 
ATOM   3591 C  C   . ASN B  1 178 ? -24.362 -5.121  2.008   1.00 11.61 ? 178 ASN B C   1 
ATOM   3592 O  O   . ASN B  1 178 ? -23.618 -6.019  1.656   1.00 13.41 ? 178 ASN B O   1 
ATOM   3593 C  CB  . ASN B  1 178 ? -26.540 -6.512  2.114   1.00 14.32 ? 178 ASN B CB  1 
ATOM   3594 C  CG  . ASN B  1 178 ? -26.335 -6.787  3.526   1.00 14.27 ? 178 ASN B CG  1 
ATOM   3595 O  OD1 . ASN B  1 178 ? -25.938 -6.009  4.361   1.00 14.50 ? 178 ASN B OD1 1 
ATOM   3596 N  ND2 . ASN B  1 178 ? -26.708 -8.082  3.867   1.00 19.06 ? 178 ASN B ND2 1 
ATOM   3597 N  N   . ILE B  1 179 ? -24.016 -4.031  2.653   1.00 10.90 ? 179 ILE B N   1 
ATOM   3598 C  CA  . ILE B  1 179 ? -22.578 -3.795  3.055   1.00 10.52 ? 179 ILE B CA  1 
ATOM   3599 C  C   . ILE B  1 179 ? -22.053 -4.872  3.940   1.00 11.86 ? 179 ILE B C   1 
ATOM   3600 O  O   . ILE B  1 179 ? -20.826 -5.119  3.974   1.00 11.38 ? 179 ILE B O   1 
ATOM   3601 C  CB  . ILE B  1 179 ? -22.384 -2.413  3.679   1.00 10.98 ? 179 ILE B CB  1 
ATOM   3602 C  CG1 . ILE B  1 179 ? -22.880 -1.314  2.695   1.00 11.27 ? 179 ILE B CG1 1 
ATOM   3603 C  CG2 . ILE B  1 179 ? -20.892 -2.157  3.995   1.00 11.05 ? 179 ILE B CG2 1 
ATOM   3604 C  CD1 . ILE B  1 179 ? -22.296 -1.321  1.256   1.00 11.59 ? 179 ILE B CD1 1 
ATOM   3605 N  N   A GLU B  1 180 ? -22.882 -5.391  4.832   0.50 10.73 ? 180 GLU B N   1 
ATOM   3606 N  N   B GLU B  1 180 ? -22.926 -5.613  4.639   0.50 11.50 ? 180 GLU B N   1 
ATOM   3607 C  CA  A GLU B  1 180 ? -22.406 -6.502  5.606   0.50 11.72 ? 180 GLU B CA  1 
ATOM   3608 C  CA  B GLU B  1 180 ? -22.458 -6.753  5.487   0.50 12.84 ? 180 GLU B CA  1 
ATOM   3609 C  C   A GLU B  1 180 ? -21.833 -7.650  4.746   0.50 10.97 ? 180 GLU B C   1 
ATOM   3610 C  C   B GLU B  1 180 ? -21.864 -7.879  4.680   0.50 11.56 ? 180 GLU B C   1 
ATOM   3611 O  O   A GLU B  1 180 ? -20.951 -8.311  5.336   0.50 11.57 ? 180 GLU B O   1 
ATOM   3612 O  O   B GLU B  1 180 ? -21.079 -8.765  5.122   0.50 11.47 ? 180 GLU B O   1 
ATOM   3613 C  CB  A GLU B  1 180 ? -23.445 -6.970  6.646   0.50 13.30 ? 180 GLU B CB  1 
ATOM   3614 C  CB  B GLU B  1 180 ? -23.624 -7.316  6.306   0.50 15.25 ? 180 GLU B CB  1 
ATOM   3615 C  CG  A GLU B  1 180 ? -22.904 -7.770  7.812   0.50 14.02 ? 180 GLU B CG  1 
ATOM   3616 C  CG  B GLU B  1 180 ? -23.930 -6.489  7.578   0.50 17.18 ? 180 GLU B CG  1 
ATOM   3617 C  CD  A GLU B  1 180 ? -23.962 -8.018  8.927   0.50 13.84 ? 180 GLU B CD  1 
ATOM   3618 C  CD  B GLU B  1 180 ? -25.184 -7.015  8.278   0.50 22.77 ? 180 GLU B CD  1 
ATOM   3619 O  OE1 A GLU B  1 180 ? -25.058 -7.417  8.892   0.50 16.12 ? 180 GLU B OE1 1 
ATOM   3620 O  OE1 B GLU B  1 180 ? -25.351 -8.248  8.324   0.50 21.35 ? 180 GLU B OE1 1 
ATOM   3621 O  OE2 A GLU B  1 180 ? -23.623 -8.772  9.837   0.50 16.95 ? 180 GLU B OE2 1 
ATOM   3622 O  OE2 B GLU B  1 180 ? -26.003 -6.189  8.743   0.50 25.86 ? 180 GLU B OE2 1 
ATOM   3623 N  N   . GLU B  1 181 ? -22.204 -7.875  3.435   1.00 10.70 ? 181 GLU B N   1 
ATOM   3624 C  CA  . GLU B  1 181 ? -21.629 -8.880  2.557   1.00 10.77 ? 181 GLU B CA  1 
ATOM   3625 C  C   . GLU B  1 181 ? -20.109 -8.619  2.303   1.00 11.96 ? 181 GLU B C   1 
ATOM   3626 O  O   . GLU B  1 181 ? -19.439 -9.536  1.764   1.00 12.72 ? 181 GLU B O   1 
ATOM   3627 C  CB  . GLU B  1 181 ? -22.299 -8.940  1.194   1.00 13.86 ? 181 GLU B CB  1 
ATOM   3628 C  CG  . GLU B  1 181 ? -23.741 -9.318  1.252   1.00 16.73 ? 181 GLU B CG  1 
ATOM   3629 C  CD  . GLU B  1 181 ? -24.436 -9.082  -0.059  1.00 21.08 ? 181 GLU B CD  1 
ATOM   3630 O  OE1 . GLU B  1 181 ? -23.824 -8.665  -1.130  1.00 23.09 ? 181 GLU B OE1 1 
ATOM   3631 O  OE2 . GLU B  1 181 ? -25.716 -9.230  -0.082  1.00 22.22 ? 181 GLU B OE2 1 
ATOM   3632 N  N   . LEU B  1 182 ? -19.629 -7.421  2.673   1.00 10.23 ? 182 LEU B N   1 
ATOM   3633 C  CA  . LEU B  1 182 ? -18.180 -7.132  2.464   1.00 9.94  ? 182 LEU B CA  1 
ATOM   3634 C  C   . LEU B  1 182 ? -17.414 -7.612  3.688   1.00 9.16  ? 182 LEU B C   1 
ATOM   3635 O  O   . LEU B  1 182 ? -16.173 -7.598  3.688   1.00 9.54  ? 182 LEU B O   1 
ATOM   3636 C  CB  . LEU B  1 182 ? -17.991 -5.601  2.319   1.00 9.03  ? 182 LEU B CB  1 
ATOM   3637 C  CG  . LEU B  1 182 ? -18.673 -4.984  1.086   1.00 7.49  ? 182 LEU B CG  1 
ATOM   3638 C  CD1 . LEU B  1 182 ? -18.350 -3.459  1.030   1.00 8.87  ? 182 LEU B CD1 1 
ATOM   3639 C  CD2 . LEU B  1 182 ? -18.361 -5.610  -0.212  1.00 8.42  ? 182 LEU B CD2 1 
ATOM   3640 N  N   . LEU B  1 183 ? -18.082 -7.974  4.784   1.00 10.36 ? 183 LEU B N   1 
ATOM   3641 C  CA  . LEU B  1 183 ? -17.398 -8.384  6.015   1.00 9.66  ? 183 LEU B CA  1 
ATOM   3642 C  C   . LEU B  1 183 ? -17.132 -9.889  5.975   1.00 10.14 ? 183 LEU B C   1 
ATOM   3643 O  O   . LEU B  1 183 ? -17.812 -10.645 5.311   1.00 11.48 ? 183 LEU B O   1 
ATOM   3644 C  CB  . LEU B  1 183 ? -18.294 -8.071  7.266   1.00 12.68 ? 183 LEU B CB  1 
ATOM   3645 C  CG  . LEU B  1 183 ? -18.721 -6.596  7.315   1.00 12.72 ? 183 LEU B CG  1 
ATOM   3646 C  CD1 . LEU B  1 183 ? -19.632 -6.389  8.593   1.00 18.39 ? 183 LEU B CD1 1 
ATOM   3647 C  CD2 . LEU B  1 183 ? -17.564 -5.664  7.257   1.00 14.44 ? 183 LEU B CD2 1 
ATOM   3648 N  N   . PRO B  1 184 ? -16.115 -10.327 6.750   1.00 9.34  ? 184 PRO B N   1 
ATOM   3649 C  CA  . PRO B  1 184 ? -15.738 -11.761 6.746   1.00 10.97 ? 184 PRO B CA  1 
ATOM   3650 C  C   . PRO B  1 184 ? -16.646 -12.546 7.630   1.00 13.77 ? 184 PRO B C   1 
ATOM   3651 O  O   . PRO B  1 184 ? -17.555 -12.064 8.269   1.00 15.31 ? 184 PRO B O   1 
ATOM   3652 C  CB  . PRO B  1 184 ? -14.325 -11.720 7.389   1.00 13.07 ? 184 PRO B CB  1 
ATOM   3653 C  CG  . PRO B  1 184 ? -14.382 -10.515 8.307   1.00 12.46 ? 184 PRO B CG  1 
ATOM   3654 C  CD  . PRO B  1 184 ? -15.230 -9.531  7.598   1.00 9.72  ? 184 PRO B CD  1 
ATOM   3655 N  N   . GLU B  1 185 ? -16.299 -13.830 7.613   1.00 14.95 ? 185 GLU B N   1 
ATOM   3656 C  CA  . GLU B  1 185 ? -16.862 -14.758 8.618   1.00 16.37 ? 185 GLU B CA  1 
ATOM   3657 C  C   . GLU B  1 185 ? -16.460 -14.450 10.013  1.00 15.69 ? 185 GLU B C   1 
ATOM   3658 O  O   . GLU B  1 185 ? -15.296 -13.944 10.293  1.00 15.25 ? 185 GLU B O   1 
ATOM   3659 C  CB  . GLU B  1 185 ? -16.396 -16.169 8.277   1.00 19.56 ? 185 GLU B CB  1 
ATOM   3660 C  CG  . GLU B  1 185 ? -16.942 -16.626 6.935   1.00 24.67 ? 185 GLU B CG  1 
ATOM   3661 C  CD  . GLU B  1 185 ? -16.427 -18.020 6.517   1.00 38.22 ? 185 GLU B CD  1 
ATOM   3662 O  OE1 . GLU B  1 185 ? -16.954 -18.548 5.500   1.00 47.42 ? 185 GLU B OE1 1 
ATOM   3663 O  OE2 . GLU B  1 185 ? -15.480 -18.577 7.143   1.00 43.49 ? 185 GLU B OE2 1 
ATOM   3664 N  N   . ARG B  1 186 ? -17.408 -14.656 10.919  1.00 15.51 ? 186 ARG B N   1 
ATOM   3665 C  CA  . ARG B  1 186 ? -17.130 -14.624 12.356  1.00 16.29 ? 186 ARG B CA  1 
ATOM   3666 C  C   . ARG B  1 186 ? -16.670 -13.209 12.763  1.00 13.04 ? 186 ARG B C   1 
ATOM   3667 O  O   . ARG B  1 186 ? -15.592 -12.995 13.315  1.00 13.69 ? 186 ARG B O   1 
ATOM   3668 C  CB  . ARG B  1 186 ? -16.121 -15.697 12.784  1.00 17.80 ? 186 ARG B CB  1 
ATOM   3669 C  CG  . ARG B  1 186 ? -16.732 -17.117 12.789  1.00 24.65 ? 186 ARG B CG  1 
ATOM   3670 C  CD  . ARG B  1 186 ? -15.719 -18.202 13.251  1.00 25.71 ? 186 ARG B CD  1 
ATOM   3671 N  NE  . ARG B  1 186 ? -14.544 -18.401 12.404  1.00 30.41 ? 186 ARG B NE  1 
ATOM   3672 C  CZ  . ARG B  1 186 ? -14.601 -18.831 11.140  1.00 34.39 ? 186 ARG B CZ  1 
ATOM   3673 N  NH1 . ARG B  1 186 ? -15.784 -19.080 10.571  1.00 40.98 ? 186 ARG B NH1 1 
ATOM   3674 N  NH2 . ARG B  1 186 ? -13.483 -18.972 10.427  1.00 38.55 ? 186 ARG B NH2 1 
ATOM   3675 N  N   . THR B  1 187 ? -17.510 -12.241 12.422  1.00 11.83 ? 187 THR B N   1 
ATOM   3676 C  CA  . THR B  1 187 ? -17.213 -10.883 12.805  1.00 10.42 ? 187 THR B CA  1 
ATOM   3677 C  C   . THR B  1 187 ? -17.065 -10.665 14.303  1.00 11.18 ? 187 THR B C   1 
ATOM   3678 O  O   . THR B  1 187 ? -16.537 -9.651  14.729  1.00 11.77 ? 187 THR B O   1 
ATOM   3679 C  CB  . THR B  1 187 ? -18.211 -9.852  12.270  1.00 10.95 ? 187 THR B CB  1 
ATOM   3680 O  OG1 . THR B  1 187 ? -19.547 -10.319 12.539  1.00 13.35 ? 187 THR B OG1 1 
ATOM   3681 C  CG2 . THR B  1 187 ? -18.042 -9.780  10.713  1.00 12.89 ? 187 THR B CG2 1 
ATOM   3682 N  N   . ALA B  1 188 ? -17.521 -11.630 15.123  1.00 11.02 ? 188 ALA B N   1 
ATOM   3683 C  CA  . ALA B  1 188 ? -17.332 -11.491 16.512  1.00 10.82 ? 188 ALA B CA  1 
ATOM   3684 C  C   . ALA B  1 188 ? -15.861 -11.558 16.930  1.00 9.90  ? 188 ALA B C   1 
ATOM   3685 O  O   . ALA B  1 188 ? -15.556 -11.144 18.046  1.00 11.32 ? 188 ALA B O   1 
ATOM   3686 C  CB  . ALA B  1 188 ? -18.123 -12.614 17.276  1.00 12.69 ? 188 ALA B CB  1 
ATOM   3687 N  N   A GLU B  1 189 ? -15.008 -12.109 16.065  0.50 10.43 ? 189 GLU B N   1 
ATOM   3688 N  N   B GLU B  1 189 ? -15.019 -12.105 16.069  0.50 11.32 ? 189 GLU B N   1 
ATOM   3689 C  CA  A GLU B  1 189 ? -13.549 -12.200 16.309  0.50 9.40  ? 189 GLU B CA  1 
ATOM   3690 C  CA  B GLU B  1 189 ? -13.588 -12.155 16.328  0.50 10.75 ? 189 GLU B CA  1 
ATOM   3691 C  C   A GLU B  1 189 ? -12.774 -11.033 15.656  0.50 9.69  ? 189 GLU B C   1 
ATOM   3692 C  C   B GLU B  1 189 ? -12.890 -10.966 15.669  0.50 10.75 ? 189 GLU B C   1 
ATOM   3693 O  O   A GLU B  1 189 ? -12.693 -10.947 14.375  0.50 9.27  ? 189 GLU B O   1 
ATOM   3694 O  O   B GLU B  1 189 ? -12.915 -10.838 14.406  0.50 10.77 ? 189 GLU B O   1 
ATOM   3695 C  CB  A GLU B  1 189 ? -12.999 -13.572 15.849  0.50 10.53 ? 189 GLU B CB  1 
ATOM   3696 C  CB  B GLU B  1 189 ? -13.016 -13.456 15.783  0.50 13.36 ? 189 GLU B CB  1 
ATOM   3697 C  CG  A GLU B  1 189 ? -13.732 -14.751 16.521  0.50 12.05 ? 189 GLU B CG  1 
ATOM   3698 C  CG  B GLU B  1 189 ? -13.788 -14.703 16.186  0.50 17.17 ? 189 GLU B CG  1 
ATOM   3699 C  CD  A GLU B  1 189 ? -13.353 -16.067 15.911  0.50 13.02 ? 189 GLU B CD  1 
ATOM   3700 C  CD  B GLU B  1 189 ? -12.973 -15.879 15.779  0.50 20.28 ? 189 GLU B CD  1 
ATOM   3701 O  OE1 A GLU B  1 189 ? -12.121 -16.297 15.596  0.50 12.11 ? 189 GLU B OE1 1 
ATOM   3702 O  OE1 B GLU B  1 189 ? -12.391 -16.518 16.703  0.50 24.54 ? 189 GLU B OE1 1 
ATOM   3703 O  OE2 A GLU B  1 189 ? -14.284 -16.916 15.821  0.50 15.25 ? 189 GLU B OE2 1 
ATOM   3704 O  OE2 B GLU B  1 189 ? -12.857 -16.085 14.540  0.50 19.84 ? 189 GLU B OE2 1 
ATOM   3705 N  N   . TYR B  1 190 ? -12.275 -10.161 16.507  1.00 8.84  ? 190 TYR B N   1 
ATOM   3706 C  CA  . TYR B  1 190 ? -11.595 -8.955  15.996  1.00 8.37  ? 190 TYR B CA  1 
ATOM   3707 C  C   . TYR B  1 190 ? -10.494 -8.511  16.908  1.00 9.40  ? 190 TYR B C   1 
ATOM   3708 O  O   . TYR B  1 190 ? -10.451 -8.854  18.096  1.00 9.91  ? 190 TYR B O   1 
ATOM   3709 C  CB  . TYR B  1 190 ? -12.623 -7.825  15.659  1.00 8.03  ? 190 TYR B CB  1 
ATOM   3710 C  CG  . TYR B  1 190 ? -13.454 -7.427  16.939  1.00 7.93  ? 190 TYR B CG  1 
ATOM   3711 C  CD1 . TYR B  1 190 ? -12.952 -6.529  17.871  1.00 8.35  ? 190 TYR B CD1 1 
ATOM   3712 C  CD2 . TYR B  1 190 ? -14.767 -7.946  17.119  1.00 8.79  ? 190 TYR B CD2 1 
ATOM   3713 C  CE1 . TYR B  1 190 ? -13.789 -6.102  18.964  1.00 8.50  ? 190 TYR B CE1 1 
ATOM   3714 C  CE2 . TYR B  1 190 ? -15.546 -7.581  18.261  1.00 10.02 ? 190 TYR B CE2 1 
ATOM   3715 C  CZ  . TYR B  1 190 ? -15.047 -6.687  19.120  1.00 9.13  ? 190 TYR B CZ  1 
ATOM   3716 O  OH  . TYR B  1 190 ? -15.755 -6.194  20.222  1.00 10.66 ? 190 TYR B OH  1 
ATOM   3717 N  N   . TYR B  1 191 ? -9.609  -7.648  16.367  1.00 8.98  ? 191 TYR B N   1 
ATOM   3718 C  CA  . TYR B  1 191 ? -8.591  -6.933  17.065  1.00 8.86  ? 191 TYR B CA  1 
ATOM   3719 C  C   . TYR B  1 191 ? -9.102  -5.505  17.264  1.00 9.38  ? 191 TYR B C   1 
ATOM   3720 O  O   . TYR B  1 191 ? -9.750  -4.909  16.404  1.00 9.50  ? 191 TYR B O   1 
ATOM   3721 C  CB  . TYR B  1 191 ? -7.273  -6.842  16.245  1.00 8.66  ? 191 TYR B CB  1 
ATOM   3722 C  CG  . TYR B  1 191 ? -6.726  -8.124  15.697  1.00 9.17  ? 191 TYR B CG  1 
ATOM   3723 C  CD1 . TYR B  1 191 ? -5.696  -8.758  16.405  1.00 10.00 ? 191 TYR B CD1 1 
ATOM   3724 C  CD2 . TYR B  1 191 ? -7.081  -8.557  14.460  1.00 9.22  ? 191 TYR B CD2 1 
ATOM   3725 C  CE1 . TYR B  1 191 ? -5.163  -9.932  15.892  1.00 10.77 ? 191 TYR B CE1 1 
ATOM   3726 C  CE2 . TYR B  1 191 ? -6.527  -9.707  13.881  1.00 10.54 ? 191 TYR B CE2 1 
ATOM   3727 C  CZ  . TYR B  1 191 ? -5.543  -10.373 14.617  1.00 9.94  ? 191 TYR B CZ  1 
ATOM   3728 O  OH  . TYR B  1 191 ? -4.937  -11.512 14.064  1.00 14.45 ? 191 TYR B OH  1 
ATOM   3729 N  N   . ARG B  1 192 ? -8.850  -4.902  18.416  1.00 8.67  ? 192 ARG B N   1 
ATOM   3730 C  CA  . ARG B  1 192 ? -9.281  -3.527  18.746  1.00 9.31  ? 192 ARG B CA  1 
ATOM   3731 C  C   . ARG B  1 192 ? -8.123  -2.760  19.312  1.00 9.43  ? 192 ARG B C   1 
ATOM   3732 O  O   . ARG B  1 192 ? -7.439  -3.239  20.249  1.00 9.83  ? 192 ARG B O   1 
ATOM   3733 C  CB  . ARG B  1 192 ? -10.397 -3.657  19.827  1.00 11.30 ? 192 ARG B CB  1 
ATOM   3734 C  CG  . ARG B  1 192 ? -10.742 -2.400  20.568  1.00 13.08 ? 192 ARG B CG  1 
ATOM   3735 C  CD  . ARG B  1 192 ? -11.388 -1.332  19.667  1.00 13.68 ? 192 ARG B CD  1 
ATOM   3736 N  NE  . ARG B  1 192 ? -12.569 -1.821  18.928  1.00 13.80 ? 192 ARG B NE  1 
ATOM   3737 C  CZ  . ARG B  1 192 ? -13.791 -2.159  19.391  1.00 14.47 ? 192 ARG B CZ  1 
ATOM   3738 N  NH1 . ARG B  1 192 ? -14.047 -2.059  20.739  1.00 17.11 ? 192 ARG B NH1 1 
ATOM   3739 N  NH2 . ARG B  1 192 ? -14.751 -2.608  18.601  1.00 15.38 ? 192 ARG B NH2 1 
ATOM   3740 N  N   . TYR B  1 193 ? -7.883  -1.564  18.851  1.00 9.50  ? 193 TYR B N   1 
ATOM   3741 C  CA  . TYR B  1 193 ? -6.848  -0.766  19.416  1.00 10.85 ? 193 TYR B CA  1 
ATOM   3742 C  C   . TYR B  1 193 ? -7.057  0.720   19.166  1.00 11.24 ? 193 TYR B C   1 
ATOM   3743 O  O   . TYR B  1 193 ? -7.848  1.062   18.264  1.00 10.97 ? 193 TYR B O   1 
ATOM   3744 C  CB  . TYR B  1 193 ? -5.445  -1.236  18.950  1.00 11.17 ? 193 TYR B CB  1 
ATOM   3745 C  CG  . TYR B  1 193 ? -5.083  -0.768  17.492  1.00 9.79  ? 193 TYR B CG  1 
ATOM   3746 C  CD1 . TYR B  1 193 ? -4.265  0.397   17.293  1.00 10.83 ? 193 TYR B CD1 1 
ATOM   3747 C  CD2 . TYR B  1 193 ? -5.478  -1.521  16.375  1.00 10.00 ? 193 TYR B CD2 1 
ATOM   3748 C  CE1 . TYR B  1 193 ? -3.948  0.786   16.032  1.00 9.51  ? 193 TYR B CE1 1 
ATOM   3749 C  CE2 . TYR B  1 193 ? -5.168  -1.099  15.072  1.00 8.52  ? 193 TYR B CE2 1 
ATOM   3750 C  CZ  . TYR B  1 193 ? -4.420  0.068   14.946  1.00 9.22  ? 193 TYR B CZ  1 
ATOM   3751 O  OH  . TYR B  1 193 ? -4.044  0.489   13.673  1.00 9.93  ? 193 TYR B OH  1 
ATOM   3752 N  N   . ARG B  1 194 ? -6.292  1.546   19.865  1.00 12.52 ? 194 ARG B N   1 
ATOM   3753 C  CA  . ARG B  1 194 ? -6.427  3.018   19.681  1.00 12.50 ? 194 ARG B CA  1 
ATOM   3754 C  C   . ARG B  1 194 ? -5.372  3.462   18.727  1.00 11.31 ? 194 ARG B C   1 
ATOM   3755 O  O   . ARG B  1 194 ? -4.188  3.183   18.906  1.00 12.99 ? 194 ARG B O   1 
ATOM   3756 C  CB  . ARG B  1 194 ? -6.080  3.710   21.045  1.00 15.84 ? 194 ARG B CB  1 
ATOM   3757 C  CG  . ARG B  1 194 ? -7.059  3.304   22.158  1.00 23.59 ? 194 ARG B CG  1 
ATOM   3758 C  CD  . ARG B  1 194 ? -8.332  4.135   22.065  1.00 34.03 ? 194 ARG B CD  1 
ATOM   3759 N  NE  . ARG B  1 194 ? -8.902  4.523   23.379  1.00 44.73 ? 194 ARG B NE  1 
ATOM   3760 C  CZ  . ARG B  1 194 ? -10.196 4.812   23.571  1.00 50.48 ? 194 ARG B CZ  1 
ATOM   3761 N  NH1 . ARG B  1 194 ? -11.067 4.778   22.562  1.00 45.57 ? 194 ARG B NH1 1 
ATOM   3762 N  NH2 . ARG B  1 194 ? -10.637 5.126   24.779  1.00 61.56 ? 194 ARG B NH2 1 
ATOM   3763 N  N   . GLY B  1 195 ? -5.806  4.161   17.628  1.00 11.02 ? 195 GLY B N   1 
ATOM   3764 C  CA  . GLY B  1 195 ? -4.790  4.598   16.619  1.00 11.62 ? 195 GLY B CA  1 
ATOM   3765 C  C   . GLY B  1 195 ? -5.216  5.890   15.996  1.00 11.26 ? 195 GLY B C   1 
ATOM   3766 O  O   . GLY B  1 195 ? -5.853  6.750   16.517  1.00 11.88 ? 195 GLY B O   1 
ATOM   3767 N  N   . SER B  1 196 ? -4.911  5.936   14.679  1.00 10.37 ? 196 SER B N   1 
ATOM   3768 C  CA  . SER B  1 196 ? -5.032  7.179   13.959  1.00 10.38 ? 196 SER B CA  1 
ATOM   3769 C  C   . SER B  1 196 ? -5.608  6.900   12.525  1.00 9.45  ? 196 SER B C   1 
ATOM   3770 O  O   . SER B  1 196 ? -5.709  5.761   11.990  1.00 10.05 ? 196 SER B O   1 
ATOM   3771 C  CB  . SER B  1 196 ? -3.662  7.868   13.714  1.00 9.84  ? 196 SER B CB  1 
ATOM   3772 O  OG  . SER B  1 196 ? -2.850  7.156   12.740  1.00 9.38  ? 196 SER B OG  1 
ATOM   3773 N  N   . LEU B  1 197 ? -5.896  8.022   11.853  1.00 8.52  ? 197 LEU B N   1 
ATOM   3774 C  CA  . LEU B  1 197 ? -6.099  7.949   10.381  1.00 8.60  ? 197 LEU B CA  1 
ATOM   3775 C  C   . LEU B  1 197 ? -4.798  7.540   9.770   1.00 8.32  ? 197 LEU B C   1 
ATOM   3776 O  O   . LEU B  1 197 ? -3.710  7.941   10.218  1.00 8.32  ? 197 LEU B O   1 
ATOM   3777 C  CB  . LEU B  1 197 ? -6.446  9.368   9.838   1.00 10.80 ? 197 LEU B CB  1 
ATOM   3778 C  CG  . LEU B  1 197 ? -7.781  9.934   10.332  1.00 13.12 ? 197 LEU B CG  1 
ATOM   3779 C  CD1 . LEU B  1 197 ? -7.904  11.333  9.764   1.00 16.87 ? 197 LEU B CD1 1 
ATOM   3780 C  CD2 . LEU B  1 197 ? -8.995  9.103   10.022  1.00 14.86 ? 197 LEU B CD2 1 
ATOM   3781 N  N   . THR B  1 198 ? -4.858  6.678   8.712   1.00 8.02  ? 198 THR B N   1 
ATOM   3782 C  CA  . THR B  1 198 ? -3.606  6.209   8.083   1.00 7.70  ? 198 THR B CA  1 
ATOM   3783 C  C   . THR B  1 198 ? -3.136  7.076   6.930   1.00 7.59  ? 198 THR B C   1 
ATOM   3784 O  O   . THR B  1 198 ? -2.186  6.736   6.273   1.00 7.98  ? 198 THR B O   1 
ATOM   3785 C  CB  . THR B  1 198 ? -3.717  4.776   7.569   1.00 7.04  ? 198 THR B CB  1 
ATOM   3786 O  OG1 . THR B  1 198 ? -4.693  4.737   6.497   1.00 7.69  ? 198 THR B OG1 1 
ATOM   3787 C  CG2 . THR B  1 198 ? -4.136  3.777   8.642   1.00 8.80  ? 198 THR B CG2 1 
ATOM   3788 N  N   . THR B  1 199 ? -3.899  8.204   6.693   1.00 9.35  ? 199 THR B N   1 
ATOM   3789 C  CA  . THR B  1 199 ? -3.464  9.174   5.685   1.00 8.47  ? 199 THR B CA  1 
ATOM   3790 C  C   . THR B  1 199 ? -3.412  10.519  6.400   1.00 9.28  ? 199 THR B C   1 
ATOM   3791 O  O   . THR B  1 199 ? -4.086  10.661  7.434   1.00 9.67  ? 199 THR B O   1 
ATOM   3792 C  CB  . THR B  1 199 ? -4.448  9.314   4.524   1.00 9.08  ? 199 THR B CB  1 
ATOM   3793 O  OG1 . THR B  1 199 ? -5.646  9.899   4.960   1.00 13.99 ? 199 THR B OG1 1 
ATOM   3794 C  CG2 . THR B  1 199 ? -4.772  7.931   3.970   1.00 9.79  ? 199 THR B CG2 1 
ATOM   3795 N  N   . PRO B  1 200 ? -2.711  11.506  5.824   1.00 8.62  ? 200 PRO B N   1 
ATOM   3796 C  CA  . PRO B  1 200 ? -2.870  12.862  6.317   1.00 9.84  ? 200 PRO B CA  1 
ATOM   3797 C  C   . PRO B  1 200 ? -4.364  13.208  6.464   1.00 9.40  ? 200 PRO B C   1 
ATOM   3798 O  O   . PRO B  1 200 ? -5.125  12.872  5.610   1.00 10.81 ? 200 PRO B O   1 
ATOM   3799 C  CB  . PRO B  1 200 ? -2.187  13.647  5.192   1.00 9.40  ? 200 PRO B CB  1 
ATOM   3800 C  CG  . PRO B  1 200 ? -1.084  12.765  4.744   1.00 8.80  ? 200 PRO B CG  1 
ATOM   3801 C  CD  . PRO B  1 200 ? -1.820  11.427  4.636   1.00 9.12  ? 200 PRO B CD  1 
ATOM   3802 N  N   A PRO B  1 201 ? -4.765  13.901  7.530   0.50 8.91  ? 201 PRO B N   1 
ATOM   3803 N  N   B PRO B  1 201 ? -4.719  13.962  7.514   0.50 10.29 ? 201 PRO B N   1 
ATOM   3804 C  CA  A PRO B  1 201 ? -3.955  14.553  8.563   0.50 9.22  ? 201 PRO B CA  1 
ATOM   3805 C  CA  B PRO B  1 201 ? -3.767  14.577  8.482   0.50 10.83 ? 201 PRO B CA  1 
ATOM   3806 C  C   A PRO B  1 201 ? -3.517  13.684  9.720   0.50 9.59  ? 201 PRO B C   1 
ATOM   3807 C  C   B PRO B  1 201 ? -3.295  13.652  9.590   0.50 10.75 ? 201 PRO B C   1 
ATOM   3808 O  O   A PRO B  1 201 ? -2.993  14.137  10.725  0.50 7.93  ? 201 PRO B O   1 
ATOM   3809 O  O   B PRO B  1 201 ? -2.591  14.087  10.468  0.50 10.82 ? 201 PRO B O   1 
ATOM   3810 C  CB  A PRO B  1 201 ? -4.857  15.740  9.024   0.50 9.25  ? 201 PRO B CB  1 
ATOM   3811 C  CB  B PRO B  1 201 ? -4.567  15.790  9.061   0.50 11.57 ? 201 PRO B CB  1 
ATOM   3812 C  CG  A PRO B  1 201 ? -6.214  15.155  8.845   0.50 8.08  ? 201 PRO B CG  1 
ATOM   3813 C  CG  B PRO B  1 201 ? -5.724  15.931  8.115   0.50 11.83 ? 201 PRO B CG  1 
ATOM   3814 C  CD  A PRO B  1 201 ? -6.190  14.232  7.646   0.50 8.84  ? 201 PRO B CD  1 
ATOM   3815 C  CD  B PRO B  1 201 ? -6.041  14.605  7.534   0.50 11.01 ? 201 PRO B CD  1 
ATOM   3816 N  N   . CYS B  1 202 ? -3.736  12.379  9.599   1.00 9.64  ? 202 CYS B N   1 
ATOM   3817 C  CA  . CYS B  1 202 ? -3.209  11.371  10.588  1.00 10.29 ? 202 CYS B CA  1 
ATOM   3818 C  C   . CYS B  1 202 ? -3.708  11.573  12.062  1.00 10.04 ? 202 CYS B C   1 
ATOM   3819 O  O   . CYS B  1 202 ? -2.988  11.207  12.984  1.00 10.94 ? 202 CYS B O   1 
ATOM   3820 C  CB  . CYS B  1 202 ? -1.660  11.329  10.612  1.00 10.98 ? 202 CYS B CB  1 
ATOM   3821 S  SG  . CYS B  1 202 ? -0.851  10.978  9.000   1.00 9.90  ? 202 CYS B SG  1 
ATOM   3822 N  N   . ASN B  1 203 ? -4.903  12.106  12.165  1.00 13.02 ? 203 ASN B N   1 
ATOM   3823 C  CA  . ASN B  1 203 ? -5.429  12.472  13.485  1.00 14.30 ? 203 ASN B CA  1 
ATOM   3824 C  C   . ASN B  1 203 ? -5.418  11.201  14.320  1.00 15.43 ? 203 ASN B C   1 
ATOM   3825 O  O   . ASN B  1 203 ? -5.941  10.189  13.899  1.00 13.80 ? 203 ASN B O   1 
ATOM   3826 C  CB  . ASN B  1 203 ? -6.841  12.956  13.349  1.00 15.93 ? 203 ASN B CB  1 
ATOM   3827 C  CG  . ASN B  1 203 ? -6.932  14.309  12.627  1.00 22.95 ? 203 ASN B CG  1 
ATOM   3828 O  OD1 . ASN B  1 203 ? -5.941  14.803  12.106  1.00 24.61 ? 203 ASN B OD1 1 
ATOM   3829 N  ND2 . ASN B  1 203 ? -8.083  14.901  12.617  1.00 21.59 ? 203 ASN B ND2 1 
ATOM   3830 N  N   . PRO B  1 204 ? -4.935  11.263  15.578  1.00 13.38 ? 204 PRO B N   1 
ATOM   3831 C  CA  . PRO B  1 204 ? -4.906  10.064  16.484  1.00 15.54 ? 204 PRO B CA  1 
ATOM   3832 C  C   . PRO B  1 204 ? -6.234  9.879   17.186  1.00 16.31 ? 204 PRO B C   1 
ATOM   3833 O  O   . PRO B  1 204 ? -6.264  9.838   18.475  1.00 17.95 ? 204 PRO B O   1 
ATOM   3834 C  CB  . PRO B  1 204 ? -3.760  10.391  17.463  1.00 14.12 ? 204 PRO B CB  1 
ATOM   3835 C  CG  . PRO B  1 204 ? -3.847  11.910  17.582  1.00 14.30 ? 204 PRO B CG  1 
ATOM   3836 C  CD  . PRO B  1 204 ? -4.239  12.419  16.147  1.00 14.64 ? 204 PRO B CD  1 
ATOM   3837 N  N   . THR B  1 205 ? -7.316  9.774   16.424  1.00 14.37 ? 205 THR B N   1 
ATOM   3838 C  CA  . THR B  1 205 ? -8.619  9.869   16.990  1.00 14.73 ? 205 THR B CA  1 
ATOM   3839 C  C   . THR B  1 205 ? -9.523  8.709   16.534  1.00 13.23 ? 205 THR B C   1 
ATOM   3840 O  O   . THR B  1 205 ? -10.748 8.762   16.635  1.00 14.38 ? 205 THR B O   1 
ATOM   3841 C  CB  . THR B  1 205 ? -9.325  11.147  16.493  1.00 16.83 ? 205 THR B CB  1 
ATOM   3842 O  OG1 . THR B  1 205 ? -9.201  11.172  15.049  1.00 15.04 ? 205 THR B OG1 1 
ATOM   3843 C  CG2 . THR B  1 205 ? -8.566  12.353  17.141  1.00 18.36 ? 205 THR B CG2 1 
ATOM   3844 N  N   . VAL B  1 206 ? -8.845  7.609   16.101  1.00 11.72 ? 206 VAL B N   1 
ATOM   3845 C  CA  . VAL B  1 206 ? -9.582  6.378   15.651  1.00 12.20 ? 206 VAL B CA  1 
ATOM   3846 C  C   . VAL B  1 206 ? -9.558  5.167   16.643  1.00 10.59 ? 206 VAL B C   1 
ATOM   3847 O  O   . VAL B  1 206 ? -8.518  4.797   17.064  1.00 13.43 ? 206 VAL B O   1 
ATOM   3848 C  CB  . VAL B  1 206 ? -9.024  5.957   14.253  1.00 10.43 ? 206 VAL B CB  1 
ATOM   3849 C  CG1 . VAL B  1 206 ? -9.754  4.670   13.839  1.00 11.06 ? 206 VAL B CG1 1 
ATOM   3850 C  CG2 . VAL B  1 206 ? -9.087  7.061   13.221  1.00 11.92 ? 206 VAL B CG2 1 
ATOM   3851 N  N   . LEU B  1 207 ? -10.768 4.688   16.900  1.00 9.86  ? 207 LEU B N   1 
ATOM   3852 C  CA  . LEU B  1 207 ? -10.934 3.340   17.508  1.00 11.17 ? 207 LEU B CA  1 
ATOM   3853 C  C   . LEU B  1 207 ? -10.961 2.341   16.289  1.00 9.57  ? 207 LEU B C   1 
ATOM   3854 O  O   . LEU B  1 207 ? -11.910 2.338   15.568  1.00 10.30 ? 207 LEU B O   1 
ATOM   3855 C  CB  . LEU B  1 207 ? -12.274 3.335   18.256  1.00 16.85 ? 207 LEU B CB  1 
ATOM   3856 C  CG  . LEU B  1 207 ? -12.330 2.149   19.228  1.00 22.73 ? 207 LEU B CG  1 
ATOM   3857 C  CD1 . LEU B  1 207 ? -11.335 2.320   20.365  1.00 28.69 ? 207 LEU B CD1 1 
ATOM   3858 C  CD2 . LEU B  1 207 ? -13.754 2.067   19.755  1.00 25.76 ? 207 LEU B CD2 1 
ATOM   3859 N  N   . TRP B  1 208 ? -9.930  1.540   16.211  1.00 10.16 ? 208 TRP B N   1 
ATOM   3860 C  CA  . TRP B  1 208 ? -9.774  0.553   15.110  1.00 9.33  ? 208 TRP B CA  1 
ATOM   3861 C  C   . TRP B  1 208 ? -10.390 -0.758  15.530  1.00 9.87  ? 208 TRP B C   1 
ATOM   3862 O  O   . TRP B  1 208 ? -10.101 -1.251  16.681  1.00 10.72 ? 208 TRP B O   1 
ATOM   3863 C  CB  . TRP B  1 208 ? -8.269  0.329   14.777  1.00 8.40  ? 208 TRP B CB  1 
ATOM   3864 C  CG  . TRP B  1 208 ? -7.755  1.425   13.892  1.00 8.11  ? 208 TRP B CG  1 
ATOM   3865 C  CD1 . TRP B  1 208 ? -7.048  2.557   14.226  1.00 9.52  ? 208 TRP B CD1 1 
ATOM   3866 C  CD2 . TRP B  1 208 ? -7.949  1.470   12.468  1.00 8.37  ? 208 TRP B CD2 1 
ATOM   3867 N  NE1 . TRP B  1 208 ? -6.823  3.330   13.124  1.00 8.84  ? 208 TRP B NE1 1 
ATOM   3868 C  CE2 . TRP B  1 208 ? -7.351  2.696   12.013  1.00 7.82  ? 208 TRP B CE2 1 
ATOM   3869 C  CE3 . TRP B  1 208 ? -8.590  0.598   11.519  1.00 8.48  ? 208 TRP B CE3 1 
ATOM   3870 C  CZ2 . TRP B  1 208 ? -7.378  3.080   10.699  1.00 7.59  ? 208 TRP B CZ2 1 
ATOM   3871 C  CZ3 . TRP B  1 208 ? -8.619  1.025   10.191  1.00 8.44  ? 208 TRP B CZ3 1 
ATOM   3872 C  CH2 . TRP B  1 208 ? -7.958  2.214   9.790   1.00 8.14  ? 208 TRP B CH2 1 
ATOM   3873 N  N   . THR B  1 209 ? -11.144 -1.377  14.627  1.00 8.90  ? 209 THR B N   1 
ATOM   3874 C  CA  . THR B  1 209 ? -11.568 -2.766  14.790  1.00 8.73  ? 209 THR B CA  1 
ATOM   3875 C  C   . THR B  1 209 ? -11.056 -3.475  13.514  1.00 9.13  ? 209 THR B C   1 
ATOM   3876 O  O   . THR B  1 209 ? -11.535 -3.156  12.414  1.00 9.33  ? 209 THR B O   1 
ATOM   3877 C  CB  . THR B  1 209 ? -13.072 -2.842  14.851  1.00 9.05  ? 209 THR B CB  1 
ATOM   3878 O  OG1 . THR B  1 209 ? -13.511 -2.165  16.036  1.00 9.65  ? 209 THR B OG1 1 
ATOM   3879 C  CG2 . THR B  1 209 ? -13.586 -4.265  14.977  1.00 9.15  ? 209 THR B CG2 1 
ATOM   3880 N  N   . VAL B  1 210 ? -10.140 -4.444  13.622  1.00 8.70  ? 210 VAL B N   1 
ATOM   3881 C  CA  . VAL B  1 210 ? -9.679  -5.206  12.455  1.00 7.93  ? 210 VAL B CA  1 
ATOM   3882 C  C   . VAL B  1 210 ? -10.252 -6.595  12.609  1.00 8.05  ? 210 VAL B C   1 
ATOM   3883 O  O   . VAL B  1 210 ? -9.937  -7.263  13.631  1.00 8.92  ? 210 VAL B O   1 
ATOM   3884 C  CB  . VAL B  1 210 ? -8.095  -5.232  12.412  1.00 8.31  ? 210 VAL B CB  1 
ATOM   3885 C  CG1 . VAL B  1 210 ? -7.644  -6.007  11.210  1.00 9.37  ? 210 VAL B CG1 1 
ATOM   3886 C  CG2 . VAL B  1 210 ? -7.520  -3.805  12.404  1.00 9.86  ? 210 VAL B CG2 1 
ATOM   3887 N  N   . PHE B  1 211 ? -11.075 -7.022  11.681  1.00 7.34  ? 211 PHE B N   1 
ATOM   3888 C  CA  . PHE B  1 211 ? -11.580 -8.404  11.836  1.00 7.64  ? 211 PHE B CA  1 
ATOM   3889 C  C   . PHE B  1 211 ? -10.516 -9.427  11.736  1.00 8.64  ? 211 PHE B C   1 
ATOM   3890 O  O   . PHE B  1 211 ? -9.516  -9.277  10.934  1.00 8.76  ? 211 PHE B O   1 
ATOM   3891 C  CB  . PHE B  1 211 ? -12.727 -8.599  10.810  1.00 8.34  ? 211 PHE B CB  1 
ATOM   3892 C  CG  . PHE B  1 211 ? -13.913 -7.693  11.110  1.00 8.94  ? 211 PHE B CG  1 
ATOM   3893 C  CD1 . PHE B  1 211 ? -14.228 -6.557  10.306  1.00 10.96 ? 211 PHE B CD1 1 
ATOM   3894 C  CD2 . PHE B  1 211 ? -14.732 -7.969  12.244  1.00 9.25  ? 211 PHE B CD2 1 
ATOM   3895 C  CE1 . PHE B  1 211 ? -15.278 -5.704  10.687  1.00 12.21 ? 211 PHE B CE1 1 
ATOM   3896 C  CE2 . PHE B  1 211 ? -15.796 -7.139  12.594  1.00 10.53 ? 211 PHE B CE2 1 
ATOM   3897 C  CZ  . PHE B  1 211 ? -16.100 -5.996  11.766  1.00 12.17 ? 211 PHE B CZ  1 
ATOM   3898 N  N   . ARG B  1 212 ? -10.662 -10.509 12.527  1.00 8.45  ? 212 ARG B N   1 
ATOM   3899 C  CA  . ARG B  1 212 ? -9.621  -11.550 12.452  1.00 9.01  ? 212 ARG B CA  1 
ATOM   3900 C  C   . ARG B  1 212 ? -9.540  -12.245 11.107  1.00 9.06  ? 212 ARG B C   1 
ATOM   3901 O  O   . ARG B  1 212 ? -8.407  -12.512 10.713  1.00 10.79 ? 212 ARG B O   1 
ATOM   3902 C  CB  . ARG B  1 212 ? -9.960  -12.573 13.574  1.00 9.65  ? 212 ARG B CB  1 
ATOM   3903 C  CG  . ARG B  1 212 ? -8.832  -13.579 13.734  1.00 10.90 ? 212 ARG B CG  1 
ATOM   3904 C  CD  . ARG B  1 212 ? -9.366  -14.754 14.600  1.00 13.06 ? 212 ARG B CD  1 
ATOM   3905 N  NE  . ARG B  1 212 ? -8.255  -15.621 14.985  1.00 15.76 ? 212 ARG B NE  1 
ATOM   3906 C  CZ  . ARG B  1 212 ? -8.328  -16.597 15.883  1.00 16.90 ? 212 ARG B CZ  1 
ATOM   3907 N  NH1 . ARG B  1 212 ? -9.471  -16.849 16.505  1.00 16.04 ? 212 ARG B NH1 1 
ATOM   3908 N  NH2 . ARG B  1 212 ? -7.253  -17.324 16.159  1.00 18.94 ? 212 ARG B NH2 1 
ATOM   3909 N  N   . ASN B  1 213 ? -10.686 -12.535 10.456  1.00 8.46  ? 213 ASN B N   1 
ATOM   3910 C  CA  . ASN B  1 213 ? -10.667 -13.357 9.303   1.00 10.51 ? 213 ASN B CA  1 
ATOM   3911 C  C   . ASN B  1 213 ? -10.672 -12.449 8.054   1.00 11.60 ? 213 ASN B C   1 
ATOM   3912 O  O   . ASN B  1 213 ? -11.393 -11.457 7.999   1.00 9.88  ? 213 ASN B O   1 
ATOM   3913 C  CB  . ASN B  1 213 ? -11.839 -14.332 9.292   1.00 12.52 ? 213 ASN B CB  1 
ATOM   3914 C  CG  . ASN B  1 213 ? -11.826 -15.233 10.533  1.00 15.55 ? 213 ASN B CG  1 
ATOM   3915 O  OD1 . ASN B  1 213 ? -10.792 -15.854 10.757  1.00 21.37 ? 213 ASN B OD1 1 
ATOM   3916 N  ND2 . ASN B  1 213 ? -12.889 -15.263 11.293  1.00 18.60 ? 213 ASN B ND2 1 
ATOM   3917 N  N   . PRO B  1 214 ? -9.864  -12.779 7.059   1.00 11.10 ? 214 PRO B N   1 
ATOM   3918 C  CA  . PRO B  1 214 ? -9.913  -12.086 5.755   1.00 10.30 ? 214 PRO B CA  1 
ATOM   3919 C  C   . PRO B  1 214 ? -11.130 -12.483 4.926   1.00 10.03 ? 214 PRO B C   1 
ATOM   3920 O  O   . PRO B  1 214 ? -11.720 -13.576 5.102   1.00 11.81 ? 214 PRO B O   1 
ATOM   3921 C  CB  . PRO B  1 214 ? -8.591  -12.451 5.105   1.00 11.37 ? 214 PRO B CB  1 
ATOM   3922 C  CG  . PRO B  1 214 ? -8.443  -13.897 5.527   1.00 14.10 ? 214 PRO B CG  1 
ATOM   3923 C  CD  . PRO B  1 214 ? -8.857  -13.871 7.038   1.00 13.28 ? 214 PRO B CD  1 
ATOM   3924 N  N   . VAL B  1 215 ? -11.407 -11.671 3.942   1.00 8.75  ? 215 VAL B N   1 
ATOM   3925 C  CA  . VAL B  1 215 ? -12.260 -12.082 2.832   1.00 8.35  ? 215 VAL B CA  1 
ATOM   3926 C  C   . VAL B  1 215 ? -11.418 -12.338 1.637   1.00 7.94  ? 215 VAL B C   1 
ATOM   3927 O  O   . VAL B  1 215 ? -10.208 -11.974 1.628   1.00 9.55  ? 215 VAL B O   1 
ATOM   3928 C  CB  . VAL B  1 215 ? -13.279 -10.991 2.507   1.00 8.73  ? 215 VAL B CB  1 
ATOM   3929 C  CG1 . VAL B  1 215 ? -14.225 -10.752 3.691   1.00 9.64  ? 215 VAL B CG1 1 
ATOM   3930 C  CG2 . VAL B  1 215 ? -12.639 -9.658  1.966   1.00 8.46  ? 215 VAL B CG2 1 
ATOM   3931 N  N   . GLN B  1 216 ? -11.924 -12.969 0.603   1.00 7.22  ? 216 GLN B N   1 
ATOM   3932 C  CA  . GLN B  1 216 ? -11.217 -13.200 -0.683  1.00 7.33  ? 216 GLN B CA  1 
ATOM   3933 C  C   . GLN B  1 216 ? -11.854 -12.377 -1.808  1.00 8.02  ? 216 GLN B C   1 
ATOM   3934 O  O   . GLN B  1 216 ? -13.111 -12.292 -1.903  1.00 9.10  ? 216 GLN B O   1 
ATOM   3935 C  CB  . GLN B  1 216 ? -11.324 -14.682 -1.145  1.00 9.32  ? 216 GLN B CB  1 
ATOM   3936 C  CG  . GLN B  1 216 ? -10.603 -15.575 -0.114  1.00 10.41 ? 216 GLN B CG  1 
ATOM   3937 C  CD  . GLN B  1 216 ? -10.591 -17.058 -0.534  1.00 13.45 ? 216 GLN B CD  1 
ATOM   3938 O  OE1 . GLN B  1 216 ? -11.065 -17.498 -1.586  1.00 11.50 ? 216 GLN B OE1 1 
ATOM   3939 N  NE2 . GLN B  1 216 ? -9.969  -17.817 0.329   1.00 19.92 ? 216 GLN B NE2 1 
ATOM   3940 N  N   . ILE B  1 217 ? -11.005 -11.889 -2.712  1.00 7.56  ? 217 ILE B N   1 
ATOM   3941 C  CA  . ILE B  1 217 ? -11.454 -11.401 -4.016  1.00 7.60  ? 217 ILE B CA  1 
ATOM   3942 C  C   . ILE B  1 217 ? -10.468 -12.034 -4.997  1.00 7.42  ? 217 ILE B C   1 
ATOM   3943 O  O   . ILE B  1 217 ? -9.342  -12.439 -4.649  1.00 7.63  ? 217 ILE B O   1 
ATOM   3944 C  CB  . ILE B  1 217 ? -11.469 -9.833  -4.094  1.00 7.54  ? 217 ILE B CB  1 
ATOM   3945 C  CG1 . ILE B  1 217 ? -10.071 -9.241  -4.088  1.00 7.49  ? 217 ILE B CG1 1 
ATOM   3946 C  CG2 . ILE B  1 217 ? -12.391 -9.272  -3.010  1.00 9.02  ? 217 ILE B CG2 1 
ATOM   3947 C  CD1 . ILE B  1 217 ? -10.042 -7.665  -4.252  1.00 10.35 ? 217 ILE B CD1 1 
ATOM   3948 N  N   . SER B  1 218 ? -10.824 -12.074 -6.286  1.00 7.41  ? 218 SER B N   1 
ATOM   3949 C  CA  . SER B  1 218 ? -9.947  -12.800 -7.235  1.00 8.28  ? 218 SER B CA  1 
ATOM   3950 C  C   . SER B  1 218 ? -8.783  -12.041 -7.655  1.00 9.36  ? 218 SER B C   1 
ATOM   3951 O  O   . SER B  1 218 ? -8.745  -10.760 -7.571  1.00 9.39  ? 218 SER B O   1 
ATOM   3952 C  CB  . SER B  1 218 ? -10.745 -13.321 -8.445  1.00 9.20  ? 218 SER B CB  1 
ATOM   3953 O  OG  . SER B  1 218 ? -11.189 -12.182 -9.209  1.00 9.79  ? 218 SER B OG  1 
ATOM   3954 N  N   . GLN B  1 219 ? -7.821  -12.705 -8.305  1.00 10.18 ? 219 GLN B N   1 
ATOM   3955 C  CA  . GLN B  1 219 ? -6.716  -12.013 -8.966  1.00 9.96  ? 219 GLN B CA  1 
ATOM   3956 C  C   . GLN B  1 219 ? -7.245  -10.993 -9.991  1.00 10.17 ? 219 GLN B C   1 
ATOM   3957 O  O   . GLN B  1 219 ? -6.617  -9.898  -10.129 1.00 10.60 ? 219 GLN B O   1 
ATOM   3958 C  CB  . GLN B  1 219 ? -5.779  -13.049 -9.623  1.00 12.17 ? 219 GLN B CB  1 
ATOM   3959 C  CG  . GLN B  1 219 ? -4.440  -12.373 -10.099 1.00 17.22 ? 219 GLN B CG  1 
ATOM   3960 C  CD  . GLN B  1 219 ? -4.491  -11.765 -11.505 1.00 19.84 ? 219 GLN B CD  1 
ATOM   3961 O  OE1 . GLN B  1 219 ? -3.610  -10.973 -11.836 1.00 21.72 ? 219 GLN B OE1 1 
ATOM   3962 N  NE2 . GLN B  1 219 ? -5.424  -12.180 -12.355 1.00 20.59 ? 219 GLN B NE2 1 
ATOM   3963 N  N   . GLU B  1 220 ? -8.283  -11.365 -10.705 1.00 10.60 ? 220 GLU B N   1 
ATOM   3964 C  CA  . GLU B  1 220 ? -8.764  -10.458 -11.784 1.00 10.50 ? 220 GLU B CA  1 
ATOM   3965 C  C   . GLU B  1 220 ? -9.386  -9.250  -11.164 1.00 10.18 ? 220 GLU B C   1 
ATOM   3966 O  O   . GLU B  1 220 ? -9.273  -8.119  -11.720 1.00 10.45 ? 220 GLU B O   1 
ATOM   3967 C  CB  . GLU B  1 220 ? -9.764  -11.175 -12.704 1.00 12.65 ? 220 GLU B CB  1 
ATOM   3968 C  CG  . GLU B  1 220 ? -9.144  -12.323 -13.553 1.00 14.46 ? 220 GLU B CG  1 
ATOM   3969 C  CD  . GLU B  1 220 ? -8.867  -13.604 -12.800 1.00 18.82 ? 220 GLU B CD  1 
ATOM   3970 O  OE1 . GLU B  1 220 ? -9.258  -13.723 -11.622 1.00 15.84 ? 220 GLU B OE1 1 
ATOM   3971 O  OE2 . GLU B  1 220 ? -8.261  -14.511 -13.408 1.00 23.61 ? 220 GLU B OE2 1 
ATOM   3972 N  N   . GLN B  1 221 ? -10.062 -9.404  -10.001 1.00 8.10  ? 221 GLN B N   1 
ATOM   3973 C  CA  . GLN B  1 221 ? -10.653 -8.204  -9.335  1.00 8.27  ? 221 GLN B CA  1 
ATOM   3974 C  C   . GLN B  1 221 ? -9.538  -7.392  -8.766  1.00 8.44  ? 221 GLN B C   1 
ATOM   3975 O  O   . GLN B  1 221 ? -9.581  -6.128  -8.957  1.00 8.83  ? 221 GLN B O   1 
ATOM   3976 C  CB  . GLN B  1 221 ? -11.535 -8.671  -8.166  1.00 8.20  ? 221 GLN B CB  1 
ATOM   3977 C  CG  . GLN B  1 221 ? -12.825 -9.298  -8.671  1.00 8.17  ? 221 GLN B CG  1 
ATOM   3978 C  CD  . GLN B  1 221 ? -13.712 -9.751  -7.529  1.00 8.00  ? 221 GLN B CD  1 
ATOM   3979 O  OE1 . GLN B  1 221 ? -13.397 -10.692 -6.782  1.00 9.08  ? 221 GLN B OE1 1 
ATOM   3980 N  NE2 . GLN B  1 221 ? -14.869 -9.069  -7.375  1.00 8.31  ? 221 GLN B NE2 1 
ATOM   3981 N  N   . LEU B  1 222 ? -8.511  -7.975  -8.189  1.00 8.21  ? 222 LEU B N   1 
ATOM   3982 C  CA  . LEU B  1 222 ? -7.360  -7.149  -7.738  1.00 7.83  ? 222 LEU B CA  1 
ATOM   3983 C  C   . LEU B  1 222 ? -6.738  -6.430  -8.929  1.00 8.25  ? 222 LEU B C   1 
ATOM   3984 O  O   . LEU B  1 222 ? -6.333  -5.263  -8.791  1.00 8.76  ? 222 LEU B O   1 
ATOM   3985 C  CB  . LEU B  1 222 ? -6.313  -8.076  -7.031  1.00 9.25  ? 222 LEU B CB  1 
ATOM   3986 C  CG  . LEU B  1 222 ? -6.754  -8.418  -5.595  1.00 8.93  ? 222 LEU B CG  1 
ATOM   3987 C  CD1 . LEU B  1 222 ? -6.053  -9.698  -5.084  1.00 10.19 ? 222 LEU B CD1 1 
ATOM   3988 C  CD2 . LEU B  1 222 ? -6.433  -7.204  -4.686  1.00 10.68 ? 222 LEU B CD2 1 
ATOM   3989 N  N   . LEU B  1 223 ? -6.548  -7.120  -10.069 1.00 8.83  ? 223 LEU B N   1 
ATOM   3990 C  CA  . LEU B  1 223 ? -5.883  -6.490  -11.213 1.00 9.32  ? 223 LEU B CA  1 
ATOM   3991 C  C   . LEU B  1 223 ? -6.710  -5.299  -11.671 1.00 9.27  ? 223 LEU B C   1 
ATOM   3992 O  O   . LEU B  1 223 ? -6.105  -4.270  -12.023 1.00 9.54  ? 223 LEU B O   1 
ATOM   3993 C  CB  . LEU B  1 223 ? -5.726  -7.536  -12.373 1.00 10.20 ? 223 LEU B CB  1 
ATOM   3994 C  CG  . LEU B  1 223 ? -4.923  -6.941  -13.544 1.00 11.16 ? 223 LEU B CG  1 
ATOM   3995 C  CD1 . LEU B  1 223 ? -3.507  -6.663  -13.185 1.00 12.27 ? 223 LEU B CD1 1 
ATOM   3996 C  CD2 . LEU B  1 223 ? -5.004  -8.007  -14.668 1.00 14.26 ? 223 LEU B CD2 1 
ATOM   3997 N  N   . ALA B  1 224 ? -8.044  -5.424  -11.717 1.00 9.51  ? 224 ALA B N   1 
ATOM   3998 C  CA  . ALA B  1 224 ? -8.871  -4.260  -12.085 1.00 9.88  ? 224 ALA B CA  1 
ATOM   3999 C  C   . ALA B  1 224 ? -8.664  -3.143  -11.106 1.00 9.69  ? 224 ALA B C   1 
ATOM   4000 O  O   . ALA B  1 224 ? -8.435  -1.975  -11.523 1.00 11.08 ? 224 ALA B O   1 
ATOM   4001 C  CB  . ALA B  1 224 ? -10.332 -4.626  -12.138 1.00 11.70 ? 224 ALA B CB  1 
ATOM   4002 N  N   . LEU B  1 225 ? -8.704  -3.410  -9.799  1.00 9.16  ? 225 LEU B N   1 
ATOM   4003 C  CA  . LEU B  1 225 ? -8.501  -2.346  -8.827  1.00 8.95  ? 225 LEU B CA  1 
ATOM   4004 C  C   . LEU B  1 225 ? -7.124  -1.678  -8.944  1.00 8.75  ? 225 LEU B C   1 
ATOM   4005 O  O   . LEU B  1 225 ? -7.024  -0.470  -8.752  1.00 10.42 ? 225 LEU B O   1 
ATOM   4006 C  CB  . LEU B  1 225 ? -8.704  -3.002  -7.407  1.00 9.08  ? 225 LEU B CB  1 
ATOM   4007 C  CG  . LEU B  1 225 ? -8.509  -2.036  -6.222  1.00 8.66  ? 225 LEU B CG  1 
ATOM   4008 C  CD1 . LEU B  1 225 ? -9.521  -0.908  -6.229  1.00 9.08  ? 225 LEU B CD1 1 
ATOM   4009 C  CD2 . LEU B  1 225 ? -8.593  -2.844  -4.888  1.00 9.97  ? 225 LEU B CD2 1 
ATOM   4010 N  N   . GLU B  1 226 ? -6.110  -2.465  -9.284  1.00 9.18  ? 226 GLU B N   1 
ATOM   4011 C  CA  . GLU B  1 226 ? -4.776  -2.000  -9.364  1.00 9.56  ? 226 GLU B CA  1 
ATOM   4012 C  C   . GLU B  1 226 ? -4.446  -1.274  -10.682 1.00 8.78  ? 226 GLU B C   1 
ATOM   4013 O  O   . GLU B  1 226 ? -3.333  -0.688  -10.723 1.00 11.76 ? 226 GLU B O   1 
ATOM   4014 C  CB  . GLU B  1 226 ? -3.801  -3.225  -9.203  1.00 9.07  ? 226 GLU B CB  1 
ATOM   4015 C  CG  . GLU B  1 226 ? -3.842  -3.885  -7.841  1.00 9.17  ? 226 GLU B CG  1 
ATOM   4016 C  CD  . GLU B  1 226 ? -3.474  -5.314  -7.833  1.00 10.64 ? 226 GLU B CD  1 
ATOM   4017 O  OE1 . GLU B  1 226 ? -3.247  -5.911  -8.923  1.00 10.18 ? 226 GLU B OE1 1 
ATOM   4018 O  OE2 . GLU B  1 226 ? -3.490  -5.948  -6.756  1.00 10.74 ? 226 GLU B OE2 1 
ATOM   4019 N  N   . THR B  1 227 ? -5.233  -1.460  -11.694 1.00 9.05  ? 227 THR B N   1 
ATOM   4020 C  CA  . THR B  1 227 ? -4.933  -0.823  -12.981 1.00 9.77  ? 227 THR B CA  1 
ATOM   4021 C  C   . THR B  1 227 ? -5.965  0.191   -13.427 1.00 10.91 ? 227 THR B C   1 
ATOM   4022 O  O   . THR B  1 227 ? -5.611  0.948   -14.376 1.00 11.80 ? 227 THR B O   1 
ATOM   4023 C  CB  . THR B  1 227 ? -4.882  -1.905  -14.120 1.00 9.85  ? 227 THR B CB  1 
ATOM   4024 O  OG1 . THR B  1 227 ? -6.114  -2.613  -14.212 1.00 10.55 ? 227 THR B OG1 1 
ATOM   4025 C  CG2 . THR B  1 227 ? -3.699  -2.930  -13.904 1.00 10.82 ? 227 THR B CG2 1 
ATOM   4026 N  N   . ALA B  1 228 ? -7.110  0.315   -12.770 1.00 9.20  ? 228 ALA B N   1 
ATOM   4027 C  CA  . ALA B  1 228 ? -8.152  1.183   -13.308 1.00 10.74 ? 228 ALA B CA  1 
ATOM   4028 C  C   . ALA B  1 228 ? -7.940  2.647   -12.983 1.00 10.78 ? 228 ALA B C   1 
ATOM   4029 O  O   . ALA B  1 228 ? -8.505  3.492   -13.686 1.00 12.06 ? 228 ALA B O   1 
ATOM   4030 C  CB  . ALA B  1 228 ? -9.514  0.772   -12.816 1.00 11.02 ? 228 ALA B CB  1 
ATOM   4031 N  N   . LEU B  1 229 ? -7.286  2.983   -11.882 1.00 9.94  ? 229 LEU B N   1 
ATOM   4032 C  CA  . LEU B  1 229 ? -7.417  4.270   -11.271 1.00 8.79  ? 229 LEU B CA  1 
ATOM   4033 C  C   . LEU B  1 229 ? -6.110  5.048   -11.260 1.00 7.91  ? 229 LEU B C   1 
ATOM   4034 O  O   . LEU B  1 229 ? -5.025  4.511   -11.226 1.00 8.42  ? 229 LEU B O   1 
ATOM   4035 C  CB  . LEU B  1 229 ? -7.885  4.150   -9.790  1.00 10.05 ? 229 LEU B CB  1 
ATOM   4036 C  CG  . LEU B  1 229 ? -9.148  3.297   -9.613  1.00 9.93  ? 229 LEU B CG  1 
ATOM   4037 C  CD1 . LEU B  1 229 ? -9.493  3.206   -8.137  1.00 13.18 ? 229 LEU B CD1 1 
ATOM   4038 C  CD2 . LEU B  1 229 ? -10.291 3.874   -10.295 1.00 12.07 ? 229 LEU B CD2 1 
ATOM   4039 N  N   . TYR B  1 230 ? -6.275  6.364   -11.354 1.00 8.34  ? 230 TYR B N   1 
ATOM   4040 C  CA  . TYR B  1 230 ? -5.223  7.437   -11.347 1.00 8.31  ? 230 TYR B CA  1 
ATOM   4041 C  C   . TYR B  1 230 ? -5.402  8.385   -10.174 1.00 8.05  ? 230 TYR B C   1 
ATOM   4042 O  O   . TYR B  1 230 ? -6.561  8.759   -9.890  1.00 9.07  ? 230 TYR B O   1 
ATOM   4043 C  CB  . TYR B  1 230 ? -5.224  8.171   -12.756 1.00 9.04  ? 230 TYR B CB  1 
ATOM   4044 C  CG  . TYR B  1 230 ? -4.691  7.213   -13.778 1.00 9.54  ? 230 TYR B CG  1 
ATOM   4045 C  CD1 . TYR B  1 230 ? -3.330  7.212   -14.067 1.00 11.25 ? 230 TYR B CD1 1 
ATOM   4046 C  CD2 . TYR B  1 230 ? -5.532  6.286   -14.398 1.00 10.58 ? 230 TYR B CD2 1 
ATOM   4047 C  CE1 . TYR B  1 230 ? -2.794  6.209   -14.898 1.00 12.51 ? 230 TYR B CE1 1 
ATOM   4048 C  CE2 . TYR B  1 230 ? -4.981  5.278   -15.251 1.00 11.85 ? 230 TYR B CE2 1 
ATOM   4049 C  CZ  . TYR B  1 230 ? -3.654  5.284   -15.478 1.00 11.79 ? 230 TYR B CZ  1 
ATOM   4050 O  OH  . TYR B  1 230 ? -3.119  4.304   -16.342 1.00 16.03 ? 230 TYR B OH  1 
ATOM   4051 N  N   . CYS B  1 231 ? -4.339  8.824   -9.576  1.00 8.98  ? 231 CYS B N   1 
ATOM   4052 C  CA  . CYS B  1 231 ? -4.364  9.830   -8.552  1.00 9.19  ? 231 CYS B CA  1 
ATOM   4053 C  C   . CYS B  1 231 ? -4.692  11.231  -9.123  1.00 9.32  ? 231 CYS B C   1 
ATOM   4054 O  O   . CYS B  1 231 ? -4.995  12.181  -8.400  1.00 11.55 ? 231 CYS B O   1 
ATOM   4055 C  CB  . CYS B  1 231 ? -3.014  9.989   -7.896  1.00 9.13  ? 231 CYS B CB  1 
ATOM   4056 S  SG  . CYS B  1 231 ? -2.506  8.405   -7.017  1.00 10.72 ? 231 CYS B SG  1 
ATOM   4057 N  N   . THR B  1 232 ? -4.461  11.369  -10.428 1.00 9.92  ? 232 THR B N   1 
ATOM   4058 C  CA  . THR B  1 232 ? -4.466  12.707  -11.102 1.00 9.49  ? 232 THR B CA  1 
ATOM   4059 C  C   . THR B  1 232 ? -5.740  12.905  -11.894 1.00 9.53  ? 232 THR B C   1 
ATOM   4060 O  O   . THR B  1 232 ? -6.505  11.981  -12.218 1.00 10.36 ? 232 THR B O   1 
ATOM   4061 C  CB  . THR B  1 232 ? -3.211  12.717  -12.083 1.00 8.76  ? 232 THR B CB  1 
ATOM   4062 O  OG1 . THR B  1 232 ? -3.058  11.419  -12.678 1.00 10.27 ? 232 THR B OG1 1 
ATOM   4063 C  CG2 . THR B  1 232 ? -1.975  13.026  -11.239 1.00 11.19 ? 232 THR B CG2 1 
ATOM   4064 N  N   . HIS B  1 233 ? -6.011  14.186  -12.178 1.00 10.27 ? 233 HIS B N   1 
ATOM   4065 C  CA  . HIS B  1 233 ? -7.145  14.515  -13.014 1.00 10.77 ? 233 HIS B CA  1 
ATOM   4066 C  C   . HIS B  1 233 ? -7.025  14.036  -14.460 1.00 10.49 ? 233 HIS B C   1 
ATOM   4067 O  O   . HIS B  1 233 ? -5.912  13.755  -14.950 1.00 10.36 ? 233 HIS B O   1 
ATOM   4068 C  CB  . HIS B  1 233 ? -7.273  16.032  -13.067 1.00 12.72 ? 233 HIS B CB  1 
ATOM   4069 C  CG  . HIS B  1 233 ? -7.733  16.609  -11.746 1.00 13.71 ? 233 HIS B CG  1 
ATOM   4070 N  ND1 . HIS B  1 233 ? -6.959  17.354  -10.969 1.00 22.67 ? 233 HIS B ND1 1 
ATOM   4071 C  CD2 . HIS B  1 233 ? -8.904  16.476  -11.091 1.00 16.90 ? 233 HIS B CD2 1 
ATOM   4072 C  CE1 . HIS B  1 233 ? -7.626  17.739  -9.874  1.00 21.73 ? 233 HIS B CE1 1 
ATOM   4073 N  NE2 . HIS B  1 233 ? -8.796  17.208  -9.930  1.00 18.04 ? 233 HIS B NE2 1 
ATOM   4074 N  N   . MET B  1 234 ? -8.169  13.872  -15.116 1.00 10.85 ? 234 MET B N   1 
ATOM   4075 C  CA  . MET B  1 234 ? -8.258  13.339  -16.513 1.00 10.70 ? 234 MET B CA  1 
ATOM   4076 C  C   . MET B  1 234 ? -7.334  14.128  -17.458 1.00 11.94 ? 234 MET B C   1 
ATOM   4077 O  O   . MET B  1 234 ? -6.709  13.528  -18.357 1.00 12.46 ? 234 MET B O   1 
ATOM   4078 C  CB  . MET B  1 234 ? -9.700  13.385  -16.969 1.00 12.80 ? 234 MET B CB  1 
ATOM   4079 C  CG  . MET B  1 234 ? -9.878  12.718  -18.311 1.00 13.62 ? 234 MET B CG  1 
ATOM   4080 S  SD  . MET B  1 234 ? -11.666 12.459  -18.585 1.00 21.38 ? 234 MET B SD  1 
ATOM   4081 C  CE  . MET B  1 234 ? -11.609 11.595  -20.148 1.00 21.49 ? 234 MET B CE  1 
ATOM   4082 N  N   . ASP B  1 235 ? -7.211  15.432  -17.204 1.00 12.09 ? 235 ASP B N   1 
ATOM   4083 C  CA  . ASP B  1 235 ? -6.334  16.239  -18.145 1.00 13.20 ? 235 ASP B CA  1 
ATOM   4084 C  C   . ASP B  1 235 ? -4.931  16.511  -17.607 1.00 14.70 ? 235 ASP B C   1 
ATOM   4085 O  O   . ASP B  1 235 ? -4.194  17.324  -18.174 1.00 17.54 ? 235 ASP B O   1 
ATOM   4086 C  CB  . ASP B  1 235 ? -7.031  17.571  -18.444 1.00 18.00 ? 235 ASP B CB  1 
ATOM   4087 C  CG  . ASP B  1 235 ? -7.163  18.458  -17.221 1.00 23.59 ? 235 ASP B CG  1 
ATOM   4088 O  OD1 . ASP B  1 235 ? -6.878  18.055  -16.047 1.00 22.28 ? 235 ASP B OD1 1 
ATOM   4089 O  OD2 . ASP B  1 235 ? -7.604  19.636  -17.407 1.00 29.12 ? 235 ASP B OD2 1 
ATOM   4090 N  N   . ASP B  1 236 ? -4.408  15.799  -16.625 1.00 11.74 ? 236 ASP B N   1 
ATOM   4091 C  CA  . ASP B  1 236 ? -3.121  16.063  -16.116 1.00 10.96 ? 236 ASP B CA  1 
ATOM   4092 C  C   . ASP B  1 236 ? -2.032  15.543  -17.090 1.00 11.28 ? 236 ASP B C   1 
ATOM   4093 O  O   . ASP B  1 236 ? -1.978  14.367  -17.415 1.00 12.93 ? 236 ASP B O   1 
ATOM   4094 C  CB  . ASP B  1 236 ? -2.973  15.343  -14.733 1.00 11.56 ? 236 ASP B CB  1 
ATOM   4095 C  CG  . ASP B  1 236 ? -1.846  15.957  -13.934 1.00 13.59 ? 236 ASP B CG  1 
ATOM   4096 O  OD1 . ASP B  1 236 ? -0.729  16.193  -14.428 1.00 14.32 ? 236 ASP B OD1 1 
ATOM   4097 O  OD2 . ASP B  1 236 ? -2.020  16.277  -12.734 1.00 15.39 ? 236 ASP B OD2 1 
ATOM   4098 N  N   . PRO B  1 237 ? -1.036  16.396  -17.497 1.00 11.94 ? 237 PRO B N   1 
ATOM   4099 C  CA  . PRO B  1 237 ? -0.012  15.927  -18.364 1.00 12.66 ? 237 PRO B CA  1 
ATOM   4100 C  C   . PRO B  1 237 ? 1.111   15.122  -17.656 1.00 11.11 ? 237 PRO B C   1 
ATOM   4101 O  O   . PRO B  1 237 ? 2.057   14.600  -18.307 1.00 13.53 ? 237 PRO B O   1 
ATOM   4102 C  CB  . PRO B  1 237 ? 0.573   17.271  -18.901 1.00 12.77 ? 237 PRO B CB  1 
ATOM   4103 C  CG  . PRO B  1 237 ? 0.400   18.195  -17.694 1.00 11.96 ? 237 PRO B CG  1 
ATOM   4104 C  CD  . PRO B  1 237 ? -1.025  17.860  -17.258 1.00 13.00 ? 237 PRO B CD  1 
ATOM   4105 N  N   A SER B  1 238 ? 1.056   14.902  -16.325 0.50 10.94 ? 238 SER B N   1 
ATOM   4106 N  N   B SER B  1 238 ? 0.959   14.977  -16.326 0.50 11.34 ? 238 SER B N   1 
ATOM   4107 C  CA  A SER B  1 238 ? 1.984   13.960  -15.612 0.50 11.04 ? 238 SER B CA  1 
ATOM   4108 C  CA  B SER B  1 238 ? 1.817   14.169  -15.460 0.50 11.41 ? 238 SER B CA  1 
ATOM   4109 C  C   A SER B  1 238 ? 1.166   12.988  -14.770 0.50 10.77 ? 238 SER B C   1 
ATOM   4110 C  C   B SER B  1 238 ? 0.953   13.127  -14.725 0.50 10.74 ? 238 SER B C   1 
ATOM   4111 O  O   A SER B  1 238 ? 1.124   13.046  -13.537 0.50 11.51 ? 238 SER B O   1 
ATOM   4112 O  O   B SER B  1 238 ? 0.750   13.222  -13.497 0.50 11.48 ? 238 SER B O   1 
ATOM   4113 C  CB  A SER B  1 238 ? 2.942   14.674  -14.682 0.50 13.11 ? 238 SER B CB  1 
ATOM   4114 C  CB  B SER B  1 238 ? 2.561   15.054  -14.437 0.50 12.74 ? 238 SER B CB  1 
ATOM   4115 O  OG  A SER B  1 238 ? 3.573   15.796  -15.280 0.50 15.05 ? 238 SER B OG  1 
ATOM   4116 O  OG  B SER B  1 238 ? 3.707   14.286  -14.061 0.50 17.02 ? 238 SER B OG  1 
ATOM   4117 N  N   . PRO B  1 239 ? 0.472   12.117  -15.463 1.00 9.63  ? 239 PRO B N   1 
ATOM   4118 C  CA  . PRO B  1 239 ? -0.404  11.128  -14.767 1.00 10.19 ? 239 PRO B CA  1 
ATOM   4119 C  C   . PRO B  1 239 ? 0.330   10.297  -13.797 1.00 10.80 ? 239 PRO B C   1 
ATOM   4120 O  O   . PRO B  1 239 ? 1.509   9.965   -13.936 1.00 11.71 ? 239 PRO B O   1 
ATOM   4121 C  CB  . PRO B  1 239 ? -0.941  10.217  -15.883 1.00 11.98 ? 239 PRO B CB  1 
ATOM   4122 C  CG  . PRO B  1 239 ? -0.135  10.586  -17.074 1.00 14.48 ? 239 PRO B CG  1 
ATOM   4123 C  CD  . PRO B  1 239 ? 0.550   11.910  -16.911 1.00 11.00 ? 239 PRO B CD  1 
ATOM   4124 N  N   . ARG B  1 240 ? -0.405  9.943   -12.723 1.00 9.80  ? 240 ARG B N   1 
ATOM   4125 C  CA  . ARG B  1 240 ? 0.190   9.044   -11.688 1.00 9.80  ? 240 ARG B CA  1 
ATOM   4126 C  C   . ARG B  1 240 ? -0.812  7.946   -11.364 1.00 8.51  ? 240 ARG B C   1 
ATOM   4127 O  O   . ARG B  1 240 ? -1.971  8.240   -11.059 1.00 10.42 ? 240 ARG B O   1 
ATOM   4128 C  CB  . ARG B  1 240 ? 0.468   9.815   -10.434 1.00 9.70  ? 240 ARG B CB  1 
ATOM   4129 C  CG  . ARG B  1 240 ? 1.646   10.755  -10.626 1.00 11.21 ? 240 ARG B CG  1 
ATOM   4130 C  CD  . ARG B  1 240 ? 1.884   11.481  -9.313  1.00 12.32 ? 240 ARG B CD  1 
ATOM   4131 N  NE  . ARG B  1 240 ? 0.824   12.464  -8.999  1.00 13.84 ? 240 ARG B NE  1 
ATOM   4132 C  CZ  . ARG B  1 240 ? -0.048  12.352  -7.965  1.00 15.39 ? 240 ARG B CZ  1 
ATOM   4133 N  NH1 . ARG B  1 240 ? -0.012  11.278  -7.157  1.00 13.31 ? 240 ARG B NH1 1 
ATOM   4134 N  NH2 . ARG B  1 240 ? -0.926  13.301  -7.795  1.00 16.08 ? 240 ARG B NH2 1 
ATOM   4135 N  N   . GLU B  1 241 ? -0.462  6.703   -11.551 1.00 9.79  ? 241 GLU B N   1 
ATOM   4136 C  CA  . GLU B  1 241 ? -1.324  5.541   -11.277 1.00 9.92  ? 241 GLU B CA  1 
ATOM   4137 C  C   . GLU B  1 241 ? -1.561  5.483   -9.768  1.00 9.24  ? 241 GLU B C   1 
ATOM   4138 O  O   . GLU B  1 241 ? -0.683  5.709   -8.946  1.00 9.60  ? 241 GLU B O   1 
ATOM   4139 C  CB  . GLU B  1 241 ? -0.591  4.267   -11.677 1.00 12.47 ? 241 GLU B CB  1 
ATOM   4140 C  CG  . GLU B  1 241 ? -0.419  4.127   -13.171 1.00 13.18 ? 241 GLU B CG  1 
ATOM   4141 C  CD  . GLU B  1 241 ? 0.423   2.944   -13.568 1.00 18.15 ? 241 GLU B CD  1 
ATOM   4142 O  OE1 . GLU B  1 241 ? 1.406   2.648   -12.845 1.00 26.06 ? 241 GLU B OE1 1 
ATOM   4143 O  OE2 . GLU B  1 241 ? 0.122   2.323   -14.571 1.00 26.60 ? 241 GLU B OE2 1 
ATOM   4144 N  N   . MET B  1 242 ? -2.830  5.148   -9.451  1.00 7.77  ? 242 MET B N   1 
ATOM   4145 C  CA  . MET B  1 242 ? -3.190  4.916   -8.005  1.00 8.29  ? 242 MET B CA  1 
ATOM   4146 C  C   . MET B  1 242 ? -2.923  3.422   -7.630  1.00 7.47  ? 242 MET B C   1 
ATOM   4147 O  O   . MET B  1 242 ? -3.744  2.546   -7.886  1.00 7.90  ? 242 MET B O   1 
ATOM   4148 C  CB  . MET B  1 242 ? -4.638  5.284   -7.877  1.00 8.04  ? 242 MET B CB  1 
ATOM   4149 C  CG  . MET B  1 242 ? -5.042  5.240   -6.376  1.00 8.64  ? 242 MET B CG  1 
ATOM   4150 S  SD  . MET B  1 242 ? -6.780  5.611   -6.049  1.00 8.78  ? 242 MET B SD  1 
ATOM   4151 C  CE  . MET B  1 242 ? -6.907  7.344   -6.577  1.00 9.08  ? 242 MET B CE  1 
ATOM   4152 N  N   . ILE B  1 243 ? -1.688  3.294   -7.144  1.00 7.59  ? 243 ILE B N   1 
ATOM   4153 C  CA  . ILE B  1 243 ? -1.138  2.001   -6.766  1.00 7.95  ? 243 ILE B CA  1 
ATOM   4154 C  C   . ILE B  1 243 ? -0.377  2.178   -5.482  1.00 7.09  ? 243 ILE B C   1 
ATOM   4155 O  O   . ILE B  1 243 ? 0.069   3.294   -5.150  1.00 7.82  ? 243 ILE B O   1 
ATOM   4156 C  CB  . ILE B  1 243 ? -0.212  1.399   -7.862  1.00 8.99  ? 243 ILE B CB  1 
ATOM   4157 C  CG1 . ILE B  1 243 ? 0.881   2.393   -8.252  1.00 9.31  ? 243 ILE B CG1 1 
ATOM   4158 C  CG2 . ILE B  1 243 ? -1.000  0.916   -9.072  1.00 8.73  ? 243 ILE B CG2 1 
ATOM   4159 C  CD1 . ILE B  1 243 ? 1.921   1.798   -9.211  1.00 12.76 ? 243 ILE B CD1 1 
ATOM   4160 N  N   . ASN B  1 244 ? -0.194  1.053   -4.734  1.00 7.43  ? 244 ASN B N   1 
ATOM   4161 C  CA  . ASN B  1 244 ? 0.625   1.103   -3.512  1.00 7.33  ? 244 ASN B CA  1 
ATOM   4162 C  C   . ASN B  1 244 ? 0.209   2.203   -2.591  1.00 6.88  ? 244 ASN B C   1 
ATOM   4163 O  O   . ASN B  1 244 ? 1.002   2.837   -1.950  1.00 7.50  ? 244 ASN B O   1 
ATOM   4164 C  CB  . ASN B  1 244 ? 2.153   1.196   -3.844  1.00 8.82  ? 244 ASN B CB  1 
ATOM   4165 C  CG  . ASN B  1 244 ? 2.513   0.155   -4.835  1.00 9.90  ? 244 ASN B CG  1 
ATOM   4166 O  OD1 . ASN B  1 244 ? 2.135   -1.011  -4.834  1.00 11.46 ? 244 ASN B OD1 1 
ATOM   4167 N  ND2 . ASN B  1 244 ? 3.314   0.642   -5.845  1.00 13.60 ? 244 ASN B ND2 1 
ATOM   4168 N  N   . ASN B  1 245 ? -1.123  2.353   -2.423  1.00 7.43  ? 245 ASN B N   1 
ATOM   4169 C  CA  . ASN B  1 245 ? -1.710  3.422   -1.599  1.00 6.67  ? 245 ASN B CA  1 
ATOM   4170 C  C   . ASN B  1 245 ? -1.976  2.879   -0.219  1.00 7.49  ? 245 ASN B C   1 
ATOM   4171 O  O   . ASN B  1 245 ? -3.094  2.973   0.331   1.00 7.50  ? 245 ASN B O   1 
ATOM   4172 C  CB  . ASN B  1 245 ? -2.994  4.003   -2.260  1.00 7.16  ? 245 ASN B CB  1 
ATOM   4173 C  CG  . ASN B  1 245 ? -4.072  3.017   -2.412  1.00 7.42  ? 245 ASN B CG  1 
ATOM   4174 O  OD1 . ASN B  1 245 ? -3.853  1.821   -2.476  1.00 7.86  ? 245 ASN B OD1 1 
ATOM   4175 N  ND2 . ASN B  1 245 ? -5.320  3.554   -2.615  1.00 7.83  ? 245 ASN B ND2 1 
ATOM   4176 N  N   . PHE B  1 246 ? -0.912  2.414   0.424   1.00 6.02  ? 246 PHE B N   1 
ATOM   4177 C  CA  . PHE B  1 246 ? -0.973  1.927   1.835   1.00 6.88  ? 246 PHE B CA  1 
ATOM   4178 C  C   . PHE B  1 246 ? 0.224   2.528   2.549   1.00 6.80  ? 246 PHE B C   1 
ATOM   4179 O  O   . PHE B  1 246 ? 1.307   2.733   1.966   1.00 7.73  ? 246 PHE B O   1 
ATOM   4180 C  CB  . PHE B  1 246 ? -0.907  0.350   1.878   1.00 7.64  ? 246 PHE B CB  1 
ATOM   4181 C  CG  . PHE B  1 246 ? 0.355   -0.249  1.267   1.00 7.97  ? 246 PHE B CG  1 
ATOM   4182 C  CD1 . PHE B  1 246 ? 1.461   -0.617  2.120   1.00 8.61  ? 246 PHE B CD1 1 
ATOM   4183 C  CD2 . PHE B  1 246 ? 0.447   -0.523  -0.116  1.00 7.63  ? 246 PHE B CD2 1 
ATOM   4184 C  CE1 . PHE B  1 246 ? 2.599   -1.167  1.559   1.00 9.72  ? 246 PHE B CE1 1 
ATOM   4185 C  CE2 . PHE B  1 246 ? 1.638   -1.077  -0.660  1.00 8.43  ? 246 PHE B CE2 1 
ATOM   4186 C  CZ  . PHE B  1 246 ? 2.731   -1.390  0.202   1.00 8.61  ? 246 PHE B CZ  1 
ATOM   4187 N  N   . ARG B  1 247 ? 0.069   2.815   3.809   1.00 6.49  ? 247 ARG B N   1 
ATOM   4188 C  CA  . ARG B  1 247 ? 1.188   3.316   4.680   1.00 7.11  ? 247 ARG B CA  1 
ATOM   4189 C  C   . ARG B  1 247 ? 1.911   2.141   5.272   1.00 6.67  ? 247 ARG B C   1 
ATOM   4190 O  O   . ARG B  1 247 ? 1.282   1.160   5.635   1.00 7.54  ? 247 ARG B O   1 
ATOM   4191 C  CB  . ARG B  1 247 ? 0.562   4.175   5.776   1.00 8.08  ? 247 ARG B CB  1 
ATOM   4192 C  CG  . ARG B  1 247 ? 1.542   5.096   6.520   1.00 7.43  ? 247 ARG B CG  1 
ATOM   4193 C  CD  . ARG B  1 247 ? 0.828   5.720   7.716   1.00 8.28  ? 247 ARG B CD  1 
ATOM   4194 N  NE  . ARG B  1 247 ? 1.715   6.798   8.288   1.00 8.08  ? 247 ARG B NE  1 
ATOM   4195 C  CZ  . ARG B  1 247 ? 1.399   7.525   9.353   1.00 8.84  ? 247 ARG B CZ  1 
ATOM   4196 N  NH1 . ARG B  1 247 ? 0.299   7.266   10.059  1.00 8.83  ? 247 ARG B NH1 1 
ATOM   4197 N  NH2 . ARG B  1 247 ? 2.151   8.580   9.748   1.00 9.77  ? 247 ARG B NH2 1 
ATOM   4198 N  N   . GLN B  1 248 ? 3.223   2.293   5.471   1.00 6.96  ? 248 GLN B N   1 
ATOM   4199 C  CA  . GLN B  1 248 ? 4.000   1.303   6.286   1.00 8.03  ? 248 GLN B CA  1 
ATOM   4200 C  C   . GLN B  1 248 ? 3.490   1.223   7.713   1.00 7.10  ? 248 GLN B C   1 
ATOM   4201 O  O   . GLN B  1 248 ? 2.951   2.186   8.252   1.00 7.95  ? 248 GLN B O   1 
ATOM   4202 C  CB  . GLN B  1 248 ? 5.484   1.661   6.330   1.00 7.18  ? 248 GLN B CB  1 
ATOM   4203 C  CG  . GLN B  1 248 ? 6.171   1.665   4.924   1.00 8.36  ? 248 GLN B CG  1 
ATOM   4204 C  CD  . GLN B  1 248 ? 6.144   0.304   4.273   1.00 8.49  ? 248 GLN B CD  1 
ATOM   4205 O  OE1 . GLN B  1 248 ? 5.272   -0.048  3.481   1.00 9.22  ? 248 GLN B OE1 1 
ATOM   4206 N  NE2 . GLN B  1 248 ? 7.149   -0.511  4.609   1.00 9.74  ? 248 GLN B NE2 1 
ATOM   4207 N  N   . VAL B  1 249 ? 3.691   0.035   8.327   1.00 7.50  ? 249 VAL B N   1 
ATOM   4208 C  CA  . VAL B  1 249 ? 3.267   -0.053  9.717   1.00 8.55  ? 249 VAL B CA  1 
ATOM   4209 C  C   . VAL B  1 249 ? 4.125   0.804   10.637  1.00 9.06  ? 249 VAL B C   1 
ATOM   4210 O  O   . VAL B  1 249 ? 5.286   1.179   10.289  1.00 8.23  ? 249 VAL B O   1 
ATOM   4211 C  CB  . VAL B  1 249 ? 3.320   -1.499  10.220  1.00 9.24  ? 249 VAL B CB  1 
ATOM   4212 C  CG1 . VAL B  1 249 ? 2.234   -2.392  9.521   1.00 8.76  ? 249 VAL B CG1 1 
ATOM   4213 C  CG2 . VAL B  1 249 ? 4.702   -2.149  10.063  1.00 10.32 ? 249 VAL B CG2 1 
ATOM   4214 N  N   . GLN B  1 250 ? 3.567   1.165   11.762  1.00 8.56  ? 250 GLN B N   1 
ATOM   4215 C  CA  . GLN B  1 250 ? 4.076   2.182   12.702  1.00 8.59  ? 250 GLN B CA  1 
ATOM   4216 C  C   . GLN B  1 250 ? 4.604   1.586   13.955  1.00 9.52  ? 250 GLN B C   1 
ATOM   4217 O  O   . GLN B  1 250 ? 4.153   0.501   14.375  1.00 10.76 ? 250 GLN B O   1 
ATOM   4218 C  CB  . GLN B  1 250 ? 2.975   3.186   13.092  1.00 8.03  ? 250 GLN B CB  1 
ATOM   4219 C  CG  . GLN B  1 250 ? 2.326   3.856   11.846  1.00 8.24  ? 250 GLN B CG  1 
ATOM   4220 C  CD  . GLN B  1 250 ? 3.240   4.772   11.067  1.00 9.15  ? 250 GLN B CD  1 
ATOM   4221 O  OE1 . GLN B  1 250 ? 3.642   5.818   11.630  1.00 11.06 ? 250 GLN B OE1 1 
ATOM   4222 N  NE2 . GLN B  1 250 ? 3.535   4.486   9.823   1.00 8.77  ? 250 GLN B NE2 1 
ATOM   4223 N  N   . LYS B  1 251 ? 5.531   2.290   14.631  1.00 9.21  ? 251 LYS B N   1 
ATOM   4224 C  CA  . LYS B  1 251 ? 5.936   1.832   15.957  1.00 9.99  ? 251 LYS B CA  1 
ATOM   4225 C  C   . LYS B  1 251 ? 4.676   1.715   16.888  1.00 11.33 ? 251 LYS B C   1 
ATOM   4226 O  O   . LYS B  1 251 ? 3.732   2.551   16.847  1.00 10.58 ? 251 LYS B O   1 
ATOM   4227 C  CB  . LYS B  1 251 ? 6.930   2.843   16.597  1.00 11.33 ? 251 LYS B CB  1 
ATOM   4228 C  CG  . LYS B  1 251 ? 8.322   2.882   15.980  1.00 12.00 ? 251 LYS B CG  1 
ATOM   4229 C  CD  . LYS B  1 251 ? 9.165   1.754   16.520  1.00 11.66 ? 251 LYS B CD  1 
ATOM   4230 C  CE  . LYS B  1 251 ? 10.623  1.802   16.088  1.00 11.05 ? 251 LYS B CE  1 
ATOM   4231 N  NZ  . LYS B  1 251 ? 10.789  1.829   14.573  1.00 9.61  ? 251 LYS B NZ  1 
ATOM   4232 N  N   . PHE B  1 252 ? 4.728   0.752   17.846  1.00 12.29 ? 252 PHE B N   1 
ATOM   4233 C  CA  . PHE B  1 252 ? 3.649   0.667   18.814  1.00 14.32 ? 252 PHE B CA  1 
ATOM   4234 C  C   . PHE B  1 252 ? 3.490   1.753   19.852  1.00 20.25 ? 252 PHE B C   1 
ATOM   4235 O  O   . PHE B  1 252 ? 2.394   1.952   20.381  1.00 21.95 ? 252 PHE B O   1 
ATOM   4236 C  CB  . PHE B  1 252 ? 3.859   -0.648  19.545  1.00 18.39 ? 252 PHE B CB  1 
ATOM   4237 C  CG  . PHE B  1 252 ? 3.234   -1.720  18.733  1.00 21.86 ? 252 PHE B CG  1 
ATOM   4238 C  CD1 . PHE B  1 252 ? 1.856   -2.020  18.898  1.00 28.35 ? 252 PHE B CD1 1 
ATOM   4239 C  CD2 . PHE B  1 252 ? 3.945   -2.347  17.676  1.00 29.31 ? 252 PHE B CD2 1 
ATOM   4240 C  CE1 . PHE B  1 252 ? 1.287   -2.956  18.035  1.00 27.81 ? 252 PHE B CE1 1 
ATOM   4241 C  CE2 . PHE B  1 252 ? 3.329   -3.319  16.820  1.00 24.94 ? 252 PHE B CE2 1 
ATOM   4242 C  CZ  . PHE B  1 252 ? 1.993   -3.555  16.997  1.00 27.26 ? 252 PHE B CZ  1 
ATOM   4243 N  N   . ASP B  1 253 ? 4.564   2.451   20.247  1.00 20.59 ? 253 ASP B N   1 
ATOM   4244 C  CA  . ASP B  1 253 ? 4.480   3.501   21.271  1.00 24.05 ? 253 ASP B CA  1 
ATOM   4245 C  C   . ASP B  1 253 ? 3.887   2.948   22.597  1.00 23.97 ? 253 ASP B C   1 
ATOM   4246 O  O   . ASP B  1 253 ? 3.102   3.691   23.201  1.00 23.06 ? 253 ASP B O   1 
ATOM   4247 C  CB  . ASP B  1 253 ? 3.702   4.717   20.748  1.00 25.32 ? 253 ASP B CB  1 
ATOM   4248 C  CG  . ASP B  1 253 ? 4.414   5.437   19.558  1.00 29.14 ? 253 ASP B CG  1 
ATOM   4249 O  OD1 . ASP B  1 253 ? 5.630   5.219   19.389  1.00 28.53 ? 253 ASP B OD1 1 
ATOM   4250 O  OD2 . ASP B  1 253 ? 3.689   6.183   18.818  1.00 30.51 ? 253 ASP B OD2 1 
ATOM   4251 N  N   . GLU B  1 254 ? 4.210   1.672   22.992  1.00 22.50 ? 254 GLU B N   1 
ATOM   4252 C  CA  . GLU B  1 254 ? 3.721   1.048   24.260  1.00 23.37 ? 254 GLU B CA  1 
ATOM   4253 C  C   . GLU B  1 254 ? 2.238   0.583   24.222  1.00 22.59 ? 254 GLU B C   1 
ATOM   4254 O  O   . GLU B  1 254 ? 1.744   0.016   25.204  1.00 21.96 ? 254 GLU B O   1 
ATOM   4255 C  CB  . GLU B  1 254 ? 3.983   1.946   25.524  1.00 28.79 ? 254 GLU B CB  1 
ATOM   4256 C  CG  . GLU B  1 254 ? 5.487   2.151   25.802  1.00 38.93 ? 254 GLU B CG  1 
ATOM   4257 N  N   . ARG B  1 255 ? 1.558   0.750   23.094  1.00 21.52 ? 255 ARG B N   1 
ATOM   4258 C  CA  . ARG B  1 255 ? 0.187   0.227   22.977  1.00 20.22 ? 255 ARG B CA  1 
ATOM   4259 C  C   . ARG B  1 255 ? 0.152   -1.354  23.017  1.00 18.82 ? 255 ARG B C   1 
ATOM   4260 O  O   . ARG B  1 255 ? 1.081   -2.026  22.532  1.00 21.33 ? 255 ARG B O   1 
ATOM   4261 C  CB  . ARG B  1 255 ? -0.407  0.714   21.607  1.00 19.05 ? 255 ARG B CB  1 
ATOM   4262 C  CG  . ARG B  1 255 ? -0.724  2.190   21.582  1.00 22.50 ? 255 ARG B CG  1 
ATOM   4263 C  CD  . ARG B  1 255 ? -1.250  2.615   20.164  1.00 18.93 ? 255 ARG B CD  1 
ATOM   4264 N  NE  . ARG B  1 255 ? -0.136  2.684   19.212  1.00 21.85 ? 255 ARG B NE  1 
ATOM   4265 C  CZ  . ARG B  1 255 ? -0.265  2.959   17.917  1.00 19.85 ? 255 ARG B CZ  1 
ATOM   4266 N  NH1 . ARG B  1 255 ? -1.467  3.179   17.412  1.00 16.13 ? 255 ARG B NH1 1 
ATOM   4267 N  NH2 . ARG B  1 255 ? 0.801   3.011   17.130  1.00 16.19 ? 255 ARG B NH2 1 
ATOM   4268 N  N   . LEU B  1 256 ? -0.974  -1.917  23.558  1.00 16.64 ? 256 LEU B N   1 
ATOM   4269 C  CA  . LEU B  1 256 ? -1.363  -3.288  23.263  1.00 15.62 ? 256 LEU B CA  1 
ATOM   4270 C  C   . LEU B  1 256 ? -2.552  -3.229  22.246  1.00 14.91 ? 256 LEU B C   1 
ATOM   4271 O  O   . LEU B  1 256 ? -3.205  -2.196  22.107  1.00 16.05 ? 256 LEU B O   1 
ATOM   4272 C  CB  . LEU B  1 256 ? -1.781  -3.985  24.561  1.00 20.63 ? 256 LEU B CB  1 
ATOM   4273 C  CG  . LEU B  1 256 ? -0.692  -4.063  25.640  1.00 20.96 ? 256 LEU B CG  1 
ATOM   4274 C  CD1 . LEU B  1 256 ? -1.308  -4.920  26.748  1.00 25.48 ? 256 LEU B CD1 1 
ATOM   4275 C  CD2 . LEU B  1 256 ? 0.596   -4.675  25.088  1.00 23.54 ? 256 LEU B CD2 1 
ATOM   4276 N  N   . VAL B  1 257 ? -2.801  -4.346  21.641  1.00 13.33 ? 257 VAL B N   1 
ATOM   4277 C  CA  . VAL B  1 257 ? -3.921  -4.618  20.762  1.00 12.91 ? 257 VAL B CA  1 
ATOM   4278 C  C   . VAL B  1 257 ? -4.781  -5.632  21.518  1.00 12.51 ? 257 VAL B C   1 
ATOM   4279 O  O   . VAL B  1 257 ? -4.285  -6.721  21.891  1.00 13.34 ? 257 VAL B O   1 
ATOM   4280 C  CB  . VAL B  1 257 ? -3.456  -5.165  19.431  1.00 12.22 ? 257 VAL B CB  1 
ATOM   4281 C  CG1 . VAL B  1 257 ? -4.618  -5.535  18.580  1.00 12.29 ? 257 VAL B CG1 1 
ATOM   4282 C  CG2 . VAL B  1 257 ? -2.622  -4.118  18.659  1.00 12.96 ? 257 VAL B CG2 1 
ATOM   4283 N  N   . TYR B  1 258 ? -6.041  -5.359  21.745  1.00 11.72 ? 258 TYR B N   1 
ATOM   4284 C  CA  . TYR B  1 258 ? -6.930  -6.257  22.473  1.00 12.16 ? 258 TYR B CA  1 
ATOM   4285 C  C   . TYR B  1 258 ? -7.715  -7.112  21.547  1.00 11.87 ? 258 TYR B C   1 
ATOM   4286 O  O   . TYR B  1 258 ? -8.104  -6.686  20.436  1.00 13.31 ? 258 TYR B O   1 
ATOM   4287 C  CB  . TYR B  1 258 ? -7.845  -5.365  23.304  1.00 14.69 ? 258 TYR B CB  1 
ATOM   4288 C  CG  . TYR B  1 258 ? -7.048  -4.501  24.237  1.00 16.49 ? 258 TYR B CG  1 
ATOM   4289 C  CD1 . TYR B  1 258 ? -6.521  -5.062  25.426  1.00 18.43 ? 258 TYR B CD1 1 
ATOM   4290 C  CD2 . TYR B  1 258 ? -6.656  -3.216  23.868  1.00 16.96 ? 258 TYR B CD2 1 
ATOM   4291 C  CE1 . TYR B  1 258 ? -5.701  -4.304  26.235  1.00 20.61 ? 258 TYR B CE1 1 
ATOM   4292 C  CE2 . TYR B  1 258 ? -5.842  -2.416  24.666  1.00 20.64 ? 258 TYR B CE2 1 
ATOM   4293 C  CZ  . TYR B  1 258 ? -5.347  -2.986  25.850  1.00 22.01 ? 258 TYR B CZ  1 
ATOM   4294 O  OH  . TYR B  1 258 ? -4.538  -2.112  26.558  1.00 22.82 ? 258 TYR B OH  1 
ATOM   4295 N  N   . THR B  1 259 ? -7.882  -8.387  21.858  1.00 11.40 ? 259 THR B N   1 
ATOM   4296 C  CA  . THR B  1 259 ? -8.536  -9.298  20.977  1.00 11.10 ? 259 THR B CA  1 
ATOM   4297 C  C   . THR B  1 259 ? -9.861  -9.825  21.580  1.00 10.51 ? 259 THR B C   1 
ATOM   4298 O  O   . THR B  1 259 ? -9.911  -10.084 22.835  1.00 12.47 ? 259 THR B O   1 
ATOM   4299 C  CB  . THR B  1 259 ? -7.682  -10.485 20.551  1.00 12.17 ? 259 THR B CB  1 
ATOM   4300 O  OG1 . THR B  1 259 ? -7.218  -11.257 21.701  1.00 13.40 ? 259 THR B OG1 1 
ATOM   4301 C  CG2 . THR B  1 259 ? -6.318  -10.005 19.893  1.00 13.31 ? 259 THR B CG2 1 
ATOM   4302 N  N   . SER B  1 260 ? -10.863 -10.032 20.783  1.00 9.56  ? 260 SER B N   1 
ATOM   4303 C  CA  . SER B  1 260 ? -12.145 -10.582 21.289  1.00 10.76 ? 260 SER B CA  1 
ATOM   4304 C  C   . SER B  1 260 ? -12.074 -12.107 21.323  1.00 12.10 ? 260 SER B C   1 
ATOM   4305 O  O   . SER B  1 260 ? -13.110 -12.743 21.702  1.00 13.44 ? 260 SER B O   1 
ATOM   4306 C  CB  . SER B  1 260 ? -13.292 -10.089 20.381  1.00 10.92 ? 260 SER B CB  1 
ATOM   4307 O  OG  . SER B  1 260 ? -13.145 -10.728 19.124  1.00 10.86 ? 260 SER B OG  1 
ATOM   4308 N  N   . PHE B  1 261 ? -10.993 -12.687 20.831  1.00 12.71 ? 261 PHE B N   1 
ATOM   4309 C  CA  . PHE B  1 261 ? -10.805 -14.119 20.738  1.00 13.38 ? 261 PHE B CA  1 
ATOM   4310 C  C   . PHE B  1 261 ? -9.578  -14.444 21.594  1.00 13.99 ? 261 PHE B C   1 
ATOM   4311 O  O   . PHE B  1 261 ? -8.633  -13.689 21.677  1.00 13.56 ? 261 PHE B O   1 
ATOM   4312 C  CB  . PHE B  1 261 ? -10.600 -14.603 19.278  1.00 12.61 ? 261 PHE B CB  1 
ATOM   4313 C  CG  . PHE B  1 261 ? -9.578  -13.864 18.497  1.00 14.00 ? 261 PHE B CG  1 
ATOM   4314 C  CD1 . PHE B  1 261 ? -8.285  -14.364 18.376  1.00 15.69 ? 261 PHE B CD1 1 
ATOM   4315 C  CD2 . PHE B  1 261 ? -9.860  -12.606 17.931  1.00 12.67 ? 261 PHE B CD2 1 
ATOM   4316 C  CE1 . PHE B  1 261 ? -7.324  -13.664 17.679  1.00 14.59 ? 261 PHE B CE1 1 
ATOM   4317 C  CE2 . PHE B  1 261 ? -8.886  -11.931 17.241  1.00 14.22 ? 261 PHE B CE2 1 
ATOM   4318 C  CZ  . PHE B  1 261 ? -7.609  -12.446 17.069  1.00 14.64 ? 261 PHE B CZ  1 
ATOM   4319 N  N   . SER B  1 262 ? -9.652  -15.590 22.307  1.00 16.40 ? 262 SER B N   1 
ATOM   4320 C  CA  . SER B  1 262 ? -8.554  -15.881 23.206  1.00 19.34 ? 262 SER B CA  1 
ATOM   4321 C  C   . SER B  1 262 ? -7.603  -16.832 22.546  1.00 20.48 ? 262 SER B C   1 
ATOM   4322 O  O   . SER B  1 262 ? -6.519  -17.006 23.107  1.00 23.03 ? 262 SER B O   1 
ATOM   4323 C  CB  . SER B  1 262 ? -9.059  -16.473 24.532  1.00 22.83 ? 262 SER B CB  1 
ATOM   4324 O  OG  . SER B  1 262 ? -9.643  -17.735 24.225  1.00 24.28 ? 262 SER B OG  1 
ATOM   4325 N  N   . GLN B  1 263 ? -8.006  -17.538 21.469  1.00 22.08 ? 263 GLN B N   1 
ATOM   4326 C  CA  . GLN B  1 263 ? -7.111  -18.414 20.738  1.00 24.97 ? 263 GLN B CA  1 
ATOM   4327 C  C   . GLN B  1 263 ? -7.669  -18.550 19.349  1.00 23.73 ? 263 GLN B C   1 
ATOM   4328 O  O   . GLN B  1 263 ? -6.978  -19.123 18.468  1.00 25.34 ? 263 GLN B O   1 
ATOM   4329 C  CB  . GLN B  1 263 ? -6.916  -19.810 21.413  1.00 23.86 ? 263 GLN B CB  1 
ATOM   4330 C  CG  . GLN B  1 263 ? -8.244  -20.586 21.583  1.00 29.50 ? 263 GLN B CG  1 
ATOM   4331 C  CD  . GLN B  1 263 ? -8.167  -21.763 22.548  1.00 37.61 ? 263 GLN B CD  1 
ATOM   4332 O  OE1 . GLN B  1 263 ? -7.288  -21.836 23.375  1.00 39.85 ? 263 GLN B OE1 1 
ATOM   4333 N  NE2 . GLN B  1 263 ? -9.133  -22.664 22.456  1.00 45.83 ? 263 GLN B NE2 1 
ATOM   4334 O  OXT . GLN B  1 263 ? -8.798  -18.091 19.123  1.00 20.11 ? 263 GLN B OXT 1 
ATOM   4335 N  N   A LYS C  1 3   ? 34.169  17.416  -25.050 0.50 29.12 ? 3   LYS C N   1 
ATOM   4336 N  N   B LYS C  1 3   ? 34.055  18.887  -26.611 0.50 33.92 ? 3   LYS C N   1 
ATOM   4337 C  CA  A LYS C  1 3   ? 32.912  17.209  -24.249 0.50 25.60 ? 3   LYS C CA  1 
ATOM   4338 C  CA  B LYS C  1 3   ? 33.250  17.929  -25.773 0.50 30.78 ? 3   LYS C CA  1 
ATOM   4339 C  C   A LYS C  1 3   ? 31.788  16.417  -24.952 0.50 26.32 ? 3   LYS C C   1 
ATOM   4340 C  C   B LYS C  1 3   ? 32.188  17.101  -26.526 0.50 28.32 ? 3   LYS C C   1 
ATOM   4341 O  O   A LYS C  1 3   ? 30.671  16.357  -24.467 0.50 25.18 ? 3   LYS C O   1 
ATOM   4342 O  O   B LYS C  1 3   ? 31.488  17.602  -27.431 0.50 27.28 ? 3   LYS C O   1 
ATOM   4343 C  CB  A LYS C  1 3   ? 32.344  18.543  -23.785 0.50 28.21 ? 3   LYS C CB  1 
ATOM   4344 C  CB  B LYS C  1 3   ? 32.639  18.587  -24.521 0.50 33.18 ? 3   LYS C CB  1 
ATOM   4345 C  CG  A LYS C  1 3   ? 30.964  18.388  -23.176 0.50 26.94 ? 3   LYS C CG  1 
ATOM   4346 C  CG  B LYS C  1 3   ? 31.546  19.618  -24.750 0.50 33.68 ? 3   LYS C CG  1 
ATOM   4347 N  N   . TRP C  1 4   ? 32.084  15.823  -26.110 1.00 25.36 ? 4   TRP C N   1 
ATOM   4348 C  CA  . TRP C  1 4   ? 31.129  14.879  -26.713 1.00 19.39 ? 4   TRP C CA  1 
ATOM   4349 C  C   . TRP C  1 4   ? 31.013  13.727  -25.780 1.00 18.28 ? 4   TRP C C   1 
ATOM   4350 O  O   . TRP C  1 4   ? 31.980  13.428  -24.994 1.00 18.52 ? 4   TRP C O   1 
ATOM   4351 C  CB  . TRP C  1 4   ? 31.606  14.471  -28.155 1.00 16.51 ? 4   TRP C CB  1 
ATOM   4352 C  CG  . TRP C  1 4   ? 32.957  13.851  -28.209 1.00 14.17 ? 4   TRP C CG  1 
ATOM   4353 C  CD1 . TRP C  1 4   ? 34.217  14.424  -28.428 1.00 14.83 ? 4   TRP C CD1 1 
ATOM   4354 C  CD2 . TRP C  1 4   ? 33.240  12.427  -28.033 1.00 13.09 ? 4   TRP C CD2 1 
ATOM   4355 N  NE1 . TRP C  1 4   ? 35.189  13.485  -28.417 1.00 15.53 ? 4   TRP C NE1 1 
ATOM   4356 C  CE2 . TRP C  1 4   ? 34.666  12.242  -28.189 1.00 13.81 ? 4   TRP C CE2 1 
ATOM   4357 C  CE3 . TRP C  1 4   ? 32.417  11.302  -27.823 1.00 13.74 ? 4   TRP C CE3 1 
ATOM   4358 C  CZ2 . TRP C  1 4   ? 35.251  10.965  -28.125 1.00 14.47 ? 4   TRP C CZ2 1 
ATOM   4359 C  CZ3 . TRP C  1 4   ? 33.009  10.052  -27.824 1.00 13.58 ? 4   TRP C CZ3 1 
ATOM   4360 C  CH2 . TRP C  1 4   ? 34.371  9.876   -27.913 1.00 15.45 ? 4   TRP C CH2 1 
ATOM   4361 N  N   . THR C  1 5   ? 29.851  13.078  -25.778 1.00 17.51 ? 5   THR C N   1 
ATOM   4362 C  CA  . THR C  1 5   ? 29.625  11.975  -24.879 1.00 16.39 ? 5   THR C CA  1 
ATOM   4363 C  C   . THR C  1 5   ? 28.874  10.849  -25.633 1.00 15.39 ? 5   THR C C   1 
ATOM   4364 O  O   . THR C  1 5   ? 28.638  10.929  -26.884 1.00 15.75 ? 5   THR C O   1 
ATOM   4365 C  CB  . THR C  1 5   ? 28.674  12.355  -23.720 1.00 20.49 ? 5   THR C CB  1 
ATOM   4366 O  OG1 . THR C  1 5   ? 27.389  12.663  -24.298 1.00 20.78 ? 5   THR C OG1 1 
ATOM   4367 C  CG2 . THR C  1 5   ? 29.218  13.607  -23.021 1.00 20.81 ? 5   THR C CG2 1 
ATOM   4368 N  N   . TYR C  1 6   ? 28.442  9.783   -24.940 1.00 17.43 ? 6   TYR C N   1 
ATOM   4369 C  CA  . TYR C  1 6   ? 27.548  8.744   -25.463 1.00 18.56 ? 6   TYR C CA  1 
ATOM   4370 C  C   . TYR C  1 6   ? 26.095  8.801   -24.953 1.00 18.31 ? 6   TYR C C   1 
ATOM   4371 O  O   . TYR C  1 6   ? 25.361  7.819   -24.992 1.00 22.13 ? 6   TYR C O   1 
ATOM   4372 C  CB  . TYR C  1 6   ? 28.057  7.334   -25.275 1.00 16.50 ? 6   TYR C CB  1 
ATOM   4373 C  CG  . TYR C  1 6   ? 29.385  7.042   -26.015 1.00 16.63 ? 6   TYR C CG  1 
ATOM   4374 C  CD1 . TYR C  1 6   ? 30.634  7.300   -25.430 1.00 15.28 ? 6   TYR C CD1 1 
ATOM   4375 C  CD2 . TYR C  1 6   ? 29.381  6.493   -27.292 1.00 15.34 ? 6   TYR C CD2 1 
ATOM   4376 C  CE1 . TYR C  1 6   ? 31.820  7.018   -26.110 1.00 15.48 ? 6   TYR C CE1 1 
ATOM   4377 C  CE2 . TYR C  1 6   ? 30.556  6.212   -27.969 1.00 14.09 ? 6   TYR C CE2 1 
ATOM   4378 C  CZ  . TYR C  1 6   ? 31.773  6.469   -27.385 1.00 13.69 ? 6   TYR C CZ  1 
ATOM   4379 O  OH  . TYR C  1 6   ? 32.920  6.180   -28.100 1.00 16.00 ? 6   TYR C OH  1 
ATOM   4380 N  N   . PHE C  1 7   ? 25.616  9.969   -24.426 1.00 25.15 ? 7   PHE C N   1 
ATOM   4381 C  CA  . PHE C  1 7   ? 24.178  10.111  -23.908 1.00 32.78 ? 7   PHE C CA  1 
ATOM   4382 C  C   . PHE C  1 7   ? 23.677  11.584  -24.006 1.00 36.65 ? 7   PHE C C   1 
ATOM   4383 O  O   . PHE C  1 7   ? 24.322  12.377  -24.700 1.00 32.02 ? 7   PHE C O   1 
ATOM   4384 C  CB  . PHE C  1 7   ? 24.133  9.689   -22.458 1.00 37.54 ? 7   PHE C CB  1 
ATOM   4385 C  CG  . PHE C  1 7   ? 24.903  10.626  -21.598 1.00 39.13 ? 7   PHE C CG  1 
ATOM   4386 C  CD1 . PHE C  1 7   ? 24.285  11.788  -21.089 1.00 40.14 ? 7   PHE C CD1 1 
ATOM   4387 C  CD2 . PHE C  1 7   ? 26.273  10.429  -21.383 1.00 40.45 ? 7   PHE C CD2 1 
ATOM   4388 C  CE1 . PHE C  1 7   ? 25.016  12.704  -20.332 1.00 40.41 ? 7   PHE C CE1 1 
ATOM   4389 C  CE2 . PHE C  1 7   ? 27.010  11.345  -20.628 1.00 41.38 ? 7   PHE C CE2 1 
ATOM   4390 C  CZ  . PHE C  1 7   ? 26.384  12.485  -20.117 1.00 37.37 ? 7   PHE C CZ  1 
ATOM   4391 N  N   . GLY C  1 8   ? 22.614  11.950  -23.250 1.00 37.15 ? 8   GLY C N   1 
ATOM   4392 C  CA  . GLY C  1 8   ? 22.076  13.354  -23.019 1.00 26.14 ? 8   GLY C CA  1 
ATOM   4393 C  C   . GLY C  1 8   ? 22.102  14.075  -24.340 1.00 29.45 ? 8   GLY C C   1 
ATOM   4394 O  O   . GLY C  1 8   ? 21.854  13.412  -25.414 1.00 34.77 ? 8   GLY C O   1 
ATOM   4395 N  N   . PRO C  1 9   ? 22.426  15.371  -24.326 1.00 25.60 ? 9   PRO C N   1 
ATOM   4396 C  CA  . PRO C  1 9   ? 22.358  16.122  -25.577 1.00 25.78 ? 9   PRO C CA  1 
ATOM   4397 C  C   . PRO C  1 9   ? 23.679  16.206  -26.323 1.00 20.24 ? 9   PRO C C   1 
ATOM   4398 O  O   . PRO C  1 9   ? 23.701  16.767  -27.411 1.00 21.60 ? 9   PRO C O   1 
ATOM   4399 C  CB  . PRO C  1 9   ? 21.904  17.545  -25.106 1.00 27.23 ? 9   PRO C CB  1 
ATOM   4400 C  CG  . PRO C  1 9   ? 22.489  17.633  -23.691 1.00 28.65 ? 9   PRO C CG  1 
ATOM   4401 C  CD  . PRO C  1 9   ? 22.461  16.249  -23.104 1.00 26.93 ? 9   PRO C CD  1 
ATOM   4402 N  N   . ASP C  1 10  ? 24.770  15.709  -25.718 1.00 21.36 ? 10  ASP C N   1 
ATOM   4403 C  CA  . ASP C  1 10  ? 26.061  15.728  -26.440 1.00 21.67 ? 10  ASP C CA  1 
ATOM   4404 C  C   . ASP C  1 10  ? 26.500  14.380  -26.995 1.00 17.81 ? 10  ASP C C   1 
ATOM   4405 O  O   . ASP C  1 10  ? 27.685  14.183  -27.404 1.00 16.65 ? 10  ASP C O   1 
ATOM   4406 C  CB  . ASP C  1 10  ? 27.216  16.320  -25.587 1.00 24.09 ? 10  ASP C CB  1 
ATOM   4407 C  CG  . ASP C  1 10  ? 26.965  17.789  -25.231 1.00 31.46 ? 10  ASP C CG  1 
ATOM   4408 O  OD1 . ASP C  1 10  ? 26.644  18.535  -26.162 1.00 32.21 ? 10  ASP C OD1 1 
ATOM   4409 O  OD2 . ASP C  1 10  ? 27.031  18.154  -24.027 1.00 34.98 ? 10  ASP C OD2 1 
ATOM   4410 N  N   . GLY C  1 11  ? 25.527  13.485  -27.072 1.00 19.56 ? 11  GLY C N   1 
ATOM   4411 C  CA  . GLY C  1 11  ? 25.670  12.067  -27.521 1.00 15.23 ? 11  GLY C CA  1 
ATOM   4412 C  C   . GLY C  1 11  ? 25.739  11.945  -29.061 1.00 12.97 ? 11  GLY C C   1 
ATOM   4413 O  O   . GLY C  1 11  ? 25.807  12.916  -29.814 1.00 12.11 ? 11  GLY C O   1 
ATOM   4414 N  N   . GLU C  1 12  ? 25.811  10.687  -29.522 1.00 11.41 ? 12  GLU C N   1 
ATOM   4415 C  CA  . GLU C  1 12  ? 26.220  10.433  -30.867 1.00 10.61 ? 12  GLU C CA  1 
ATOM   4416 C  C   . GLU C  1 12  ? 25.339  11.053  -31.939 1.00 10.96 ? 12  GLU C C   1 
ATOM   4417 O  O   . GLU C  1 12  ? 25.903  11.394  -33.009 1.00 9.07  ? 12  GLU C O   1 
ATOM   4418 C  CB  . GLU C  1 12  ? 26.428  8.909   -31.086 1.00 10.63 ? 12  GLU C CB  1 
ATOM   4419 C  CG  . GLU C  1 12  ? 25.046  8.174   -31.185 1.00 9.56  ? 12  GLU C CG  1 
ATOM   4420 C  CD  . GLU C  1 12  ? 25.296  6.687   -30.969 1.00 9.89  ? 12  GLU C CD  1 
ATOM   4421 O  OE1 . GLU C  1 12  ? 25.596  5.944   -31.919 1.00 9.60  ? 12  GLU C OE1 1 
ATOM   4422 O  OE2 . GLU C  1 12  ? 25.281  6.271   -29.775 1.00 11.83 ? 12  GLU C OE2 1 
ATOM   4423 N  N   . ASN C  1 13  ? 24.046  11.230  -31.745 1.00 10.47 ? 13  ASN C N   1 
ATOM   4424 C  CA  . ASN C  1 13  ? 23.296  11.875  -32.788 1.00 9.90  ? 13  ASN C CA  1 
ATOM   4425 C  C   . ASN C  1 13  ? 23.628  13.352  -32.953 1.00 9.51  ? 13  ASN C C   1 
ATOM   4426 O  O   . ASN C  1 13  ? 23.220  13.915  -33.974 1.00 10.23 ? 13  ASN C O   1 
ATOM   4427 C  CB  . ASN C  1 13  ? 21.778  11.709  -32.519 1.00 9.43  ? 13  ASN C CB  1 
ATOM   4428 C  CG  . ASN C  1 13  ? 21.311  10.296  -32.641 1.00 10.47 ? 13  ASN C CG  1 
ATOM   4429 O  OD1 . ASN C  1 13  ? 21.997  9.398   -33.193 1.00 10.62 ? 13  ASN C OD1 1 
ATOM   4430 N  ND2 . ASN C  1 13  ? 20.132  10.084  -32.084 1.00 10.30 ? 13  ASN C ND2 1 
ATOM   4431 N  N   A SER C  1 14  ? 24.243  13.934  -31.916 0.50 9.19  ? 14  SER C N   1 
ATOM   4432 N  N   B SER C  1 14  ? 24.301  13.989  -32.002 0.50 10.13 ? 14  SER C N   1 
ATOM   4433 C  CA  A SER C  1 14  ? 24.662  15.358  -31.910 0.50 9.13  ? 14  SER C CA  1 
ATOM   4434 C  CA  B SER C  1 14  ? 24.673  15.434  -32.194 0.50 10.49 ? 14  SER C CA  1 
ATOM   4435 C  C   A SER C  1 14  ? 26.084  15.594  -32.419 0.50 9.88  ? 14  SER C C   1 
ATOM   4436 C  C   B SER C  1 14  ? 26.164  15.615  -32.420 0.50 11.05 ? 14  SER C C   1 
ATOM   4437 O  O   A SER C  1 14  ? 26.373  16.734  -32.764 0.50 9.09  ? 14  SER C O   1 
ATOM   4438 O  O   B SER C  1 14  ? 26.639  16.726  -32.467 0.50 11.51 ? 14  SER C O   1 
ATOM   4439 C  CB  A SER C  1 14  ? 24.398  15.980  -30.528 0.50 9.59  ? 14  SER C CB  1 
ATOM   4440 C  CB  B SER C  1 14  ? 24.311  16.212  -30.952 0.50 12.04 ? 14  SER C CB  1 
ATOM   4441 O  OG  A SER C  1 14  ? 23.013  16.080  -30.356 0.50 9.15  ? 14  SER C OG  1 
ATOM   4442 O  OG  B SER C  1 14  ? 25.032  15.622  -29.889 0.50 13.82 ? 14  SER C OG  1 
ATOM   4443 N  N   . TRP C  1 15  ? 26.912  14.536  -32.531 1.00 9.90  ? 15  TRP C N   1 
ATOM   4444 C  CA  . TRP C  1 15  ? 28.332  14.708  -32.891 1.00 9.81  ? 15  TRP C CA  1 
ATOM   4445 C  C   . TRP C  1 15  ? 28.503  15.535  -34.140 1.00 9.32  ? 15  TRP C C   1 
ATOM   4446 O  O   . TRP C  1 15  ? 29.455  16.315  -34.218 1.00 10.32 ? 15  TRP C O   1 
ATOM   4447 C  CB  . TRP C  1 15  ? 29.011  13.358  -33.082 1.00 8.90  ? 15  TRP C CB  1 
ATOM   4448 C  CG  . TRP C  1 15  ? 29.171  12.548  -31.823 1.00 8.50  ? 15  TRP C CG  1 
ATOM   4449 C  CD1 . TRP C  1 15  ? 28.926  12.919  -30.486 1.00 9.85  ? 15  TRP C CD1 1 
ATOM   4450 C  CD2 . TRP C  1 15  ? 29.631  11.160  -31.766 1.00 8.62  ? 15  TRP C CD2 1 
ATOM   4451 N  NE1 . TRP C  1 15  ? 29.196  11.823  -29.625 1.00 10.24 ? 15  TRP C NE1 1 
ATOM   4452 C  CE2 . TRP C  1 15  ? 29.643  10.751  -30.367 1.00 9.27  ? 15  TRP C CE2 1 
ATOM   4453 C  CE3 . TRP C  1 15  ? 30.034  10.196  -32.782 1.00 8.22  ? 15  TRP C CE3 1 
ATOM   4454 C  CZ2 . TRP C  1 15  ? 30.008  9.474   -30.000 1.00 9.20  ? 15  TRP C CZ2 1 
ATOM   4455 C  CZ3 . TRP C  1 15  ? 30.414  8.934   -32.358 1.00 8.21  ? 15  TRP C CZ3 1 
ATOM   4456 C  CH2 . TRP C  1 15  ? 30.396  8.581   -30.991 1.00 8.73  ? 15  TRP C CH2 1 
ATOM   4457 N  N   . SER C  1 16  ? 27.634  15.363  -35.158 1.00 10.02 ? 16  SER C N   1 
ATOM   4458 C  CA  . SER C  1 16  ? 27.850  16.003  -36.468 1.00 10.27 ? 16  SER C CA  1 
ATOM   4459 C  C   . SER C  1 16  ? 27.717  17.511  -36.323 1.00 10.99 ? 16  SER C C   1 
ATOM   4460 O  O   . SER C  1 16  ? 28.162  18.149  -37.278 1.00 11.68 ? 16  SER C O   1 
ATOM   4461 C  CB  . SER C  1 16  ? 26.793  15.545  -37.453 1.00 10.38 ? 16  SER C CB  1 
ATOM   4462 O  OG  . SER C  1 16  ? 25.487  15.899  -36.947 1.00 11.24 ? 16  SER C OG  1 
ATOM   4463 N  N   . LYS C  1 17  ? 27.162  18.025  -35.226 1.00 10.61 ? 17  LYS C N   1 
ATOM   4464 C  CA  . LYS C  1 17  ? 27.091  19.536  -35.123 1.00 10.98 ? 17  LYS C CA  1 
ATOM   4465 C  C   . LYS C  1 17  ? 28.503  20.134  -35.073 1.00 11.60 ? 17  LYS C C   1 
ATOM   4466 O  O   . LYS C  1 17  ? 28.909  21.013  -35.867 1.00 14.01 ? 17  LYS C O   1 
ATOM   4467 C  CB  . LYS C  1 17  ? 26.320  19.891  -33.883 1.00 12.10 ? 17  LYS C CB  1 
ATOM   4468 C  CG  . LYS C  1 17  ? 24.800  19.588  -33.963 1.00 16.15 ? 17  LYS C CG  1 
ATOM   4469 C  CD  . LYS C  1 17  ? 24.148  19.926  -32.630 1.00 20.24 ? 17  LYS C CD  1 
ATOM   4470 C  CE  . LYS C  1 17  ? 24.275  21.467  -32.524 1.00 26.89 ? 17  LYS C CE  1 
ATOM   4471 N  NZ  . LYS C  1 17  ? 23.108  21.997  -31.749 1.00 30.55 ? 17  LYS C NZ  1 
ATOM   4472 N  N   . LYS C  1 18  ? 29.360  19.569  -34.227 1.00 11.24 ? 18  LYS C N   1 
ATOM   4473 C  CA  . LYS C  1 18  ? 30.739  20.066  -34.077 1.00 13.37 ? 18  LYS C CA  1 
ATOM   4474 C  C   . LYS C  1 18  ? 31.709  19.306  -34.955 1.00 15.90 ? 18  LYS C C   1 
ATOM   4475 O  O   . LYS C  1 18  ? 32.805  19.782  -35.222 1.00 17.72 ? 18  LYS C O   1 
ATOM   4476 C  CB  . LYS C  1 18  ? 31.199  19.991  -32.621 1.00 15.94 ? 18  LYS C CB  1 
ATOM   4477 C  CG  . LYS C  1 18  ? 30.561  21.039  -31.702 1.00 27.51 ? 18  LYS C CG  1 
ATOM   4478 C  CD  . LYS C  1 18  ? 31.255  22.439  -31.764 1.00 33.50 ? 18  LYS C CD  1 
ATOM   4479 C  CE  . LYS C  1 18  ? 30.361  23.497  -31.159 1.00 37.45 ? 18  LYS C CE  1 
ATOM   4480 N  NZ  . LYS C  1 18  ? 29.058  23.274  -31.894 1.00 34.84 ? 18  LYS C NZ  1 
ATOM   4481 N  N   . TYR C  1 19  ? 31.389  18.079  -35.388 1.00 12.73 ? 19  TYR C N   1 
ATOM   4482 C  CA  . TYR C  1 19  ? 32.304  17.240  -36.116 1.00 11.41 ? 19  TYR C CA  1 
ATOM   4483 C  C   . TYR C  1 19  ? 31.643  16.806  -37.415 1.00 10.91 ? 19  TYR C C   1 
ATOM   4484 O  O   . TYR C  1 19  ? 30.940  15.736  -37.420 1.00 11.17 ? 19  TYR C O   1 
ATOM   4485 C  CB  . TYR C  1 19  ? 32.679  16.012  -35.258 1.00 11.22 ? 19  TYR C CB  1 
ATOM   4486 C  CG  . TYR C  1 19  ? 33.305  16.432  -33.921 1.00 12.14 ? 19  TYR C CG  1 
ATOM   4487 C  CD1 . TYR C  1 19  ? 34.677  16.700  -33.856 1.00 12.02 ? 19  TYR C CD1 1 
ATOM   4488 C  CD2 . TYR C  1 19  ? 32.548  16.470  -32.753 1.00 12.13 ? 19  TYR C CD2 1 
ATOM   4489 C  CE1 . TYR C  1 19  ? 35.278  17.070  -32.644 1.00 15.50 ? 19  TYR C CE1 1 
ATOM   4490 C  CE2 . TYR C  1 19  ? 33.122  16.775  -31.541 1.00 14.15 ? 19  TYR C CE2 1 
ATOM   4491 C  CZ  . TYR C  1 19  ? 34.456  17.106  -31.487 1.00 16.15 ? 19  TYR C CZ  1 
ATOM   4492 O  OH  . TYR C  1 19  ? 35.121  17.421  -30.244 1.00 20.33 ? 19  TYR C OH  1 
ATOM   4493 N  N   . PRO C  1 20  ? 31.717  17.553  -38.484 1.00 10.49 ? 20  PRO C N   1 
ATOM   4494 C  CA  . PRO C  1 20  ? 30.842  17.339  -39.592 1.00 11.02 ? 20  PRO C CA  1 
ATOM   4495 C  C   . PRO C  1 20  ? 31.009  15.936  -40.208 1.00 11.03 ? 20  PRO C C   1 
ATOM   4496 O  O   . PRO C  1 20  ? 30.094  15.407  -40.827 1.00 10.85 ? 20  PRO C O   1 
ATOM   4497 C  CB  . PRO C  1 20  ? 31.215  18.438  -40.640 1.00 12.68 ? 20  PRO C CB  1 
ATOM   4498 C  CG  . PRO C  1 20  ? 31.899  19.460  -39.778 1.00 17.30 ? 20  PRO C CG  1 
ATOM   4499 C  CD  . PRO C  1 20  ? 32.524  18.806  -38.614 1.00 12.54 ? 20  PRO C CD  1 
ATOM   4500 N  N   . SER C  1 21  ? 32.185  15.359  -40.093 1.00 10.08 ? 21  SER C N   1 
ATOM   4501 C  CA  . SER C  1 21  ? 32.399  14.033  -40.738 1.00 9.66  ? 21  SER C CA  1 
ATOM   4502 C  C   . SER C  1 21  ? 31.528  12.971  -40.098 1.00 10.41 ? 21  SER C C   1 
ATOM   4503 O  O   . SER C  1 21  ? 31.300  11.961  -40.723 1.00 10.93 ? 21  SER C O   1 
ATOM   4504 C  CB  . SER C  1 21  ? 33.898  13.600  -40.686 1.00 10.53 ? 21  SER C CB  1 
ATOM   4505 O  OG  . SER C  1 21  ? 34.607  14.432  -41.628 1.00 13.38 ? 21  SER C OG  1 
ATOM   4506 N  N   . CYS C  1 22  ? 31.061  13.200  -38.885 1.00 9.79  ? 22  CYS C N   1 
ATOM   4507 C  CA  . CYS C  1 22  ? 30.194  12.207  -38.216 1.00 9.86  ? 22  CYS C CA  1 
ATOM   4508 C  C   . CYS C  1 22  ? 28.843  12.070  -38.903 1.00 11.03 ? 22  CYS C C   1 
ATOM   4509 O  O   . CYS C  1 22  ? 28.161  11.005  -38.717 1.00 10.15 ? 22  CYS C O   1 
ATOM   4510 C  CB  . CYS C  1 22  ? 29.995  12.576  -36.752 1.00 10.99 ? 22  CYS C CB  1 
ATOM   4511 S  SG  . CYS C  1 22  ? 31.502  12.606  -35.762 1.00 11.01 ? 22  CYS C SG  1 
ATOM   4512 N  N   . GLY C  1 23  ? 28.504  12.996  -39.786 1.00 10.26 ? 23  GLY C N   1 
ATOM   4513 C  CA  . GLY C  1 23  ? 27.281  12.881  -40.617 1.00 11.04 ? 23  GLY C CA  1 
ATOM   4514 C  C   . GLY C  1 23  ? 27.631  12.644  -42.076 1.00 10.85 ? 23  GLY C C   1 
ATOM   4515 O  O   . GLY C  1 23  ? 26.759  12.719  -42.911 1.00 10.66 ? 23  GLY C O   1 
ATOM   4516 N  N   . GLY C  1 24  ? 28.888  12.286  -42.374 1.00 10.29 ? 24  GLY C N   1 
ATOM   4517 C  CA  . GLY C  1 24  ? 29.313  12.110  -43.752 1.00 10.68 ? 24  GLY C CA  1 
ATOM   4518 C  C   . GLY C  1 24  ? 29.324  10.684  -44.226 1.00 11.34 ? 24  GLY C C   1 
ATOM   4519 O  O   . GLY C  1 24  ? 28.672  9.823   -43.610 1.00 13.15 ? 24  GLY C O   1 
ATOM   4520 N  N   . LEU C  1 25  ? 30.127  10.410  -45.215 1.00 13.13 ? 25  LEU C N   1 
ATOM   4521 C  CA  . LEU C  1 25  ? 30.240  9.096   -45.822 1.00 13.64 ? 25  LEU C CA  1 
ATOM   4522 C  C   . LEU C  1 25  ? 31.141  8.190   -44.987 1.00 13.01 ? 25  LEU C C   1 
ATOM   4523 O  O   . LEU C  1 25  ? 31.960  8.592   -44.103 1.00 11.35 ? 25  LEU C O   1 
ATOM   4524 C  CB  . LEU C  1 25  ? 30.849  9.219   -47.257 1.00 17.38 ? 25  LEU C CB  1 
ATOM   4525 C  CG  . LEU C  1 25  ? 29.982  10.124  -48.190 1.00 21.90 ? 25  LEU C CG  1 
ATOM   4526 C  CD1 . LEU C  1 25  ? 30.598  10.153  -49.604 1.00 24.45 ? 25  LEU C CD1 1 
ATOM   4527 C  CD2 . LEU C  1 25  ? 28.545  9.593   -48.256 1.00 25.67 ? 25  LEU C CD2 1 
ATOM   4528 N  N   . LEU C  1 26  ? 31.018  6.883   -45.303 1.00 13.40 ? 26  LEU C N   1 
ATOM   4529 C  CA  . LEU C  1 26  ? 31.999  5.809   -44.897 1.00 13.59 ? 26  LEU C CA  1 
ATOM   4530 C  C   . LEU C  1 26  ? 31.993  5.656   -43.362 1.00 11.27 ? 26  LEU C C   1 
ATOM   4531 O  O   . LEU C  1 26  ? 33.010  5.242   -42.771 1.00 12.92 ? 26  LEU C O   1 
ATOM   4532 C  CB  . LEU C  1 26  ? 33.437  6.048   -45.394 1.00 14.03 ? 26  LEU C CB  1 
ATOM   4533 C  CG  . LEU C  1 26  ? 33.714  5.972   -46.906 1.00 21.79 ? 26  LEU C CG  1 
ATOM   4534 C  CD1 . LEU C  1 26  ? 35.241  5.925   -47.131 1.00 25.70 ? 26  LEU C CD1 1 
ATOM   4535 C  CD2 . LEU C  1 26  ? 32.912  4.961   -47.744 1.00 22.83 ? 26  LEU C CD2 1 
ATOM   4536 N  N   . GLN C  1 27  ? 30.873  5.880   -42.688 1.00 9.07  ? 27  GLN C N   1 
ATOM   4537 C  CA  . GLN C  1 27  ? 30.882  5.779   -41.226 1.00 8.88  ? 27  GLN C CA  1 
ATOM   4538 C  C   . GLN C  1 27  ? 30.877  4.374   -40.696 1.00 9.37  ? 27  GLN C C   1 
ATOM   4539 O  O   . GLN C  1 27  ? 30.218  3.445   -41.205 1.00 11.23 ? 27  GLN C O   1 
ATOM   4540 C  CB  . GLN C  1 27  ? 29.704  6.550   -40.613 1.00 8.61  ? 27  GLN C CB  1 
ATOM   4541 C  CG  . GLN C  1 27  ? 29.768  8.084   -40.898 1.00 8.57  ? 27  GLN C CG  1 
ATOM   4542 C  CD  . GLN C  1 27  ? 30.960  8.692   -40.234 1.00 7.61  ? 27  GLN C CD  1 
ATOM   4543 O  OE1 . GLN C  1 27  ? 30.924  8.944   -39.045 1.00 9.10  ? 27  GLN C OE1 1 
ATOM   4544 N  NE2 . GLN C  1 27  ? 32.021  8.916   -40.993 1.00 9.17  ? 27  GLN C NE2 1 
ATOM   4545 N  N   . SER C  1 28  ? 31.624  4.193   -39.630 1.00 8.36  ? 28  SER C N   1 
ATOM   4546 C  CA  . SER C  1 28  ? 31.742  2.929   -38.844 1.00 7.73  ? 28  SER C CA  1 
ATOM   4547 C  C   . SER C  1 28  ? 31.161  3.129   -37.443 1.00 7.94  ? 28  SER C C   1 
ATOM   4548 O  O   . SER C  1 28  ? 31.035  4.279   -36.990 1.00 8.86  ? 28  SER C O   1 
ATOM   4549 C  CB  . SER C  1 28  ? 33.266  2.644   -38.651 1.00 8.32  ? 28  SER C CB  1 
ATOM   4550 O  OG  . SER C  1 28  ? 33.799  2.353   -39.959 1.00 9.03  ? 28  SER C OG  1 
ATOM   4551 N  N   . PRO C  1 29  ? 30.786  2.093   -36.728 1.00 7.62  ? 29  PRO C N   1 
ATOM   4552 C  CA  . PRO C  1 29  ? 30.902  0.707   -37.096 1.00 7.35  ? 29  PRO C CA  1 
ATOM   4553 C  C   . PRO C  1 29  ? 29.702  0.250   -37.896 1.00 7.80  ? 29  PRO C C   1 
ATOM   4554 O  O   . PRO C  1 29  ? 28.756  1.001   -38.189 1.00 8.99  ? 29  PRO C O   1 
ATOM   4555 C  CB  . PRO C  1 29  ? 30.937  0.014   -35.715 1.00 7.86  ? 29  PRO C CB  1 
ATOM   4556 C  CG  . PRO C  1 29  ? 29.900  0.848   -34.925 1.00 9.43  ? 29  PRO C CG  1 
ATOM   4557 C  CD  . PRO C  1 29  ? 30.167  2.302   -35.375 1.00 8.25  ? 29  PRO C CD  1 
ATOM   4558 N  N   . ILE C  1 30  ? 29.742  -1.016  -38.310 1.00 8.08  ? 30  ILE C N   1 
ATOM   4559 C  CA  . ILE C  1 30  ? 28.717  -1.623  -39.147 1.00 8.48  ? 30  ILE C CA  1 
ATOM   4560 C  C   . ILE C  1 30  ? 28.443  -3.063  -38.636 1.00 8.84  ? 30  ILE C C   1 
ATOM   4561 O  O   . ILE C  1 30  ? 29.188  -3.647  -37.862 1.00 9.02  ? 30  ILE C O   1 
ATOM   4562 C  CB  . ILE C  1 30  ? 29.181  -1.685  -40.651 1.00 7.99  ? 30  ILE C CB  1 
ATOM   4563 C  CG1 . ILE C  1 30  ? 30.470  -2.513  -40.782 1.00 8.96  ? 30  ILE C CG1 1 
ATOM   4564 C  CG2 . ILE C  1 30  ? 29.349  -0.264  -41.178 1.00 9.78  ? 30  ILE C CG2 1 
ATOM   4565 C  CD1 . ILE C  1 30  ? 30.839  -2.778  -42.247 1.00 11.23 ? 30  ILE C CD1 1 
ATOM   4566 N  N   . ASP C  1 31  ? 27.281  -3.562  -39.135 1.00 9.54  ? 31  ASP C N   1 
ATOM   4567 C  CA  . ASP C  1 31  ? 26.934  -4.972  -38.936 1.00 9.52  ? 31  ASP C CA  1 
ATOM   4568 C  C   . ASP C  1 31  ? 27.564  -5.787  -40.057 1.00 9.99  ? 31  ASP C C   1 
ATOM   4569 O  O   . ASP C  1 31  ? 27.453  -5.516  -41.323 1.00 12.71 ? 31  ASP C O   1 
ATOM   4570 C  CB  . ASP C  1 31  ? 25.425  -5.172  -39.085 1.00 11.06 ? 31  ASP C CB  1 
ATOM   4571 C  CG  . ASP C  1 31  ? 25.048  -6.638  -38.796 1.00 11.85 ? 31  ASP C CG  1 
ATOM   4572 O  OD1 . ASP C  1 31  ? 25.482  -7.197  -37.802 1.00 12.31 ? 31  ASP C OD1 1 
ATOM   4573 O  OD2 . ASP C  1 31  ? 24.193  -7.160  -39.562 1.00 17.38 ? 31  ASP C OD2 1 
ATOM   4574 N  N   . LEU C  1 32  ? 28.282  -6.824  -39.635 1.00 10.07 ? 32  LEU C N   1 
ATOM   4575 C  CA  . LEU C  1 32  ? 28.925  -7.793  -40.570 1.00 11.89 ? 32  LEU C CA  1 
ATOM   4576 C  C   . LEU C  1 32  ? 28.026  -9.041  -40.752 1.00 12.48 ? 32  LEU C C   1 
ATOM   4577 O  O   . LEU C  1 32  ? 27.832  -9.782  -39.787 1.00 13.92 ? 32  LEU C O   1 
ATOM   4578 C  CB  . LEU C  1 32  ? 30.288  -8.224  -39.895 1.00 12.67 ? 32  LEU C CB  1 
ATOM   4579 C  CG  . LEU C  1 32  ? 31.202  -7.070  -39.484 1.00 12.16 ? 32  LEU C CG  1 
ATOM   4580 C  CD1 . LEU C  1 32  ? 32.431  -7.568  -38.724 1.00 14.81 ? 32  LEU C CD1 1 
ATOM   4581 C  CD2 . LEU C  1 32  ? 31.618  -6.304  -40.721 1.00 13.26 ? 32  LEU C CD2 1 
ATOM   4582 N  N   . HIS C  1 33  ? 27.441  -9.184  -41.910 1.00 15.15 ? 33  HIS C N   1 
ATOM   4583 C  CA  . HIS C  1 33  ? 26.445  -10.259 -42.096 1.00 16.15 ? 33  HIS C CA  1 
ATOM   4584 C  C   . HIS C  1 33  ? 26.672  -10.886 -43.448 1.00 16.70 ? 33  HIS C C   1 
ATOM   4585 O  O   . HIS C  1 33  ? 27.230  -10.248 -44.316 1.00 16.58 ? 33  HIS C O   1 
ATOM   4586 C  CB  . HIS C  1 33  ? 25.040  -9.807  -41.875 1.00 19.51 ? 33  HIS C CB  1 
ATOM   4587 C  CG  . HIS C  1 33  ? 24.626  -8.705  -42.748 1.00 20.36 ? 33  HIS C CG  1 
ATOM   4588 N  ND1 . HIS C  1 33  ? 23.919  -8.930  -43.866 1.00 24.71 ? 33  HIS C ND1 1 
ATOM   4589 C  CD2 . HIS C  1 33  ? 24.864  -7.331  -42.682 1.00 22.03 ? 33  HIS C CD2 1 
ATOM   4590 C  CE1 . HIS C  1 33  ? 23.689  -7.757  -44.476 1.00 23.45 ? 33  HIS C CE1 1 
ATOM   4591 N  NE2 . HIS C  1 33  ? 24.257  -6.779  -43.749 1.00 25.09 ? 33  HIS C NE2 1 
ATOM   4592 N  N   A SER C  1 34  ? 26.136  -12.098 -43.638 0.50 18.53 ? 34  SER C N   1 
ATOM   4593 N  N   B SER C  1 34  ? 26.264  -12.157 -43.684 0.50 18.02 ? 34  SER C N   1 
ATOM   4594 C  CA  A SER C  1 34  ? 26.592  -12.973 -44.716 0.50 20.93 ? 34  SER C CA  1 
ATOM   4595 C  CA  B SER C  1 34  ? 26.792  -12.916 -44.887 0.50 18.50 ? 34  SER C CA  1 
ATOM   4596 C  C   A SER C  1 34  ? 26.442  -12.377 -46.068 0.50 19.73 ? 34  SER C C   1 
ATOM   4597 C  C   B SER C  1 34  ? 26.476  -12.291 -46.197 0.50 19.28 ? 34  SER C C   1 
ATOM   4598 O  O   A SER C  1 34  ? 27.354  -12.519 -46.905 0.50 20.26 ? 34  SER C O   1 
ATOM   4599 O  O   B SER C  1 34  ? 27.277  -12.313 -47.144 0.50 19.40 ? 34  SER C O   1 
ATOM   4600 C  CB  A SER C  1 34  ? 25.836  -14.306 -44.682 0.50 22.43 ? 34  SER C CB  1 
ATOM   4601 C  CB  B SER C  1 34  ? 26.328  -14.392 -44.910 0.50 20.83 ? 34  SER C CB  1 
ATOM   4602 O  OG  A SER C  1 34  ? 24.448  -14.076 -44.659 0.50 27.31 ? 34  SER C OG  1 
ATOM   4603 O  OG  B SER C  1 34  ? 26.395  -14.899 -43.598 0.50 22.93 ? 34  SER C OG  1 
ATOM   4604 N  N   . ASP C  1 35  ? 25.310  -11.686 -46.277 1.00 19.70 ? 35  ASP C N   1 
ATOM   4605 C  CA  . ASP C  1 35  ? 24.940  -11.247 -47.627 1.00 25.17 ? 35  ASP C CA  1 
ATOM   4606 C  C   . ASP C  1 35  ? 25.750  -10.093 -48.153 1.00 21.51 ? 35  ASP C C   1 
ATOM   4607 O  O   . ASP C  1 35  ? 25.676  -9.767  -49.340 1.00 26.54 ? 35  ASP C O   1 
ATOM   4608 C  CB  . ASP C  1 35  ? 23.434  -11.120 -47.840 1.00 36.75 ? 35  ASP C CB  1 
ATOM   4609 C  CG  . ASP C  1 35  ? 22.924  -9.754  -47.581 1.00 48.31 ? 35  ASP C CG  1 
ATOM   4610 O  OD1 . ASP C  1 35  ? 23.012  -9.305  -46.422 1.00 57.99 ? 35  ASP C OD1 1 
ATOM   4611 O  OD2 . ASP C  1 35  ? 22.430  -9.115  -48.541 1.00 65.71 ? 35  ASP C OD2 1 
ATOM   4612 N  N   . ILE C  1 36  ? 26.625  -9.501  -47.308 1.00 16.46 ? 36  ILE C N   1 
ATOM   4613 C  CA  . ILE C  1 36  ? 27.479  -8.424  -47.785 1.00 16.20 ? 36  ILE C CA  1 
ATOM   4614 C  C   . ILE C  1 36  ? 28.953  -8.823  -47.727 1.00 14.52 ? 36  ILE C C   1 
ATOM   4615 O  O   . ILE C  1 36  ? 29.785  -7.992  -47.987 1.00 17.74 ? 36  ILE C O   1 
ATOM   4616 C  CB  . ILE C  1 36  ? 27.342  -7.111  -47.026 1.00 14.89 ? 36  ILE C CB  1 
ATOM   4617 C  CG1 . ILE C  1 36  ? 27.560  -7.284  -45.507 1.00 17.44 ? 36  ILE C CG1 1 
ATOM   4618 C  CG2 . ILE C  1 36  ? 25.923  -6.579  -47.292 1.00 17.24 ? 36  ILE C CG2 1 
ATOM   4619 C  CD1 . ILE C  1 36  ? 27.666  -5.943  -44.724 1.00 17.41 ? 36  ILE C CD1 1 
ATOM   4620 N  N   . LEU C  1 37  ? 29.230  -10.087 -47.435 1.00 16.68 ? 37  LEU C N   1 
ATOM   4621 C  CA  . LEU C  1 37  ? 30.658  -10.540 -47.364 1.00 16.04 ? 37  LEU C CA  1 
ATOM   4622 C  C   . LEU C  1 37  ? 31.112  -11.087 -48.688 1.00 18.81 ? 37  LEU C C   1 
ATOM   4623 O  O   . LEU C  1 37  ? 30.304  -11.700 -49.454 1.00 20.83 ? 37  LEU C O   1 
ATOM   4624 C  CB  . LEU C  1 37  ? 30.828  -11.692 -46.385 1.00 15.93 ? 37  LEU C CB  1 
ATOM   4625 C  CG  . LEU C  1 37  ? 30.299  -11.412 -44.989 1.00 16.70 ? 37  LEU C CG  1 
ATOM   4626 C  CD1 . LEU C  1 37  ? 30.494  -12.649 -44.144 1.00 18.32 ? 37  LEU C CD1 1 
ATOM   4627 C  CD2 . LEU C  1 37  ? 31.048  -10.180 -44.367 1.00 18.18 ? 37  LEU C CD2 1 
ATOM   4628 N  N   . GLN C  1 38  ? 32.332  -10.798 -49.070 1.00 15.71 ? 38  GLN C N   1 
ATOM   4629 C  CA  . GLN C  1 38  ? 32.884  -11.346 -50.314 1.00 16.25 ? 38  GLN C CA  1 
ATOM   4630 C  C   . GLN C  1 38  ? 34.337  -11.736 -50.021 1.00 13.99 ? 38  GLN C C   1 
ATOM   4631 O  O   . GLN C  1 38  ? 35.173  -10.877 -49.621 1.00 13.68 ? 38  GLN C O   1 
ATOM   4632 C  CB  . GLN C  1 38  ? 32.899  -10.279 -51.378 1.00 15.11 ? 38  GLN C CB  1 
ATOM   4633 C  CG  . GLN C  1 38  ? 33.389  -10.840 -52.751 1.00 19.84 ? 38  GLN C CG  1 
ATOM   4634 C  CD  . GLN C  1 38  ? 33.057  -9.883  -53.838 1.00 23.51 ? 38  GLN C CD  1 
ATOM   4635 O  OE1 . GLN C  1 38  ? 33.904  -9.175  -54.267 1.00 25.09 ? 38  GLN C OE1 1 
ATOM   4636 N  NE2 . GLN C  1 38  ? 31.754  -9.820  -54.232 1.00 28.37 ? 38  GLN C NE2 1 
ATOM   4637 N  N   . TYR C  1 39  ? 34.716  -12.994 -50.331 1.00 13.50 ? 39  TYR C N   1 
ATOM   4638 C  CA  . TYR C  1 39  ? 36.112  -13.371 -50.238 1.00 14.81 ? 39  TYR C CA  1 
ATOM   4639 C  C   . TYR C  1 39  ? 36.986  -12.581 -51.160 1.00 15.57 ? 39  TYR C C   1 
ATOM   4640 O  O   . TYR C  1 39  ? 36.625  -12.281 -52.348 1.00 16.90 ? 39  TYR C O   1 
ATOM   4641 C  CB  . TYR C  1 39  ? 36.184  -14.907 -50.633 1.00 16.59 ? 39  TYR C CB  1 
ATOM   4642 C  CG  . TYR C  1 39  ? 37.617  -15.348 -50.772 1.00 18.98 ? 39  TYR C CG  1 
ATOM   4643 C  CD1 . TYR C  1 39  ? 38.421  -15.447 -49.678 1.00 19.27 ? 39  TYR C CD1 1 
ATOM   4644 C  CD2 . TYR C  1 39  ? 38.137  -15.673 -52.035 1.00 19.76 ? 39  TYR C CD2 1 
ATOM   4645 C  CE1 . TYR C  1 39  ? 39.726  -15.835 -49.826 1.00 22.74 ? 39  TYR C CE1 1 
ATOM   4646 C  CE2 . TYR C  1 39  ? 39.442  -16.101 -52.216 1.00 21.86 ? 39  TYR C CE2 1 
ATOM   4647 C  CZ  . TYR C  1 39  ? 40.229  -16.178 -51.098 1.00 21.28 ? 39  TYR C CZ  1 
ATOM   4648 O  OH  . TYR C  1 39  ? 41.547  -16.585 -51.273 1.00 21.54 ? 39  TYR C OH  1 
ATOM   4649 N  N   . ASP C  1 40  ? 38.162  -12.165 -50.686 1.00 15.48 ? 40  ASP C N   1 
ATOM   4650 C  CA  . ASP C  1 40  ? 39.109  -11.333 -51.484 1.00 17.71 ? 40  ASP C CA  1 
ATOM   4651 C  C   . ASP C  1 40  ? 40.507  -11.948 -51.261 1.00 17.78 ? 40  ASP C C   1 
ATOM   4652 O  O   . ASP C  1 40  ? 41.073  -11.966 -50.177 1.00 16.99 ? 40  ASP C O   1 
ATOM   4653 C  CB  . ASP C  1 40  ? 39.028  -9.890  -50.930 1.00 17.27 ? 40  ASP C CB  1 
ATOM   4654 C  CG  . ASP C  1 40  ? 40.015  -8.944  -51.582 1.00 22.84 ? 40  ASP C CG  1 
ATOM   4655 O  OD1 . ASP C  1 40  ? 40.881  -9.403  -52.350 1.00 17.71 ? 40  ASP C OD1 1 
ATOM   4656 O  OD2 . ASP C  1 40  ? 39.924  -7.725  -51.316 1.00 25.42 ? 40  ASP C OD2 1 
ATOM   4657 N  N   . ALA C  1 41  ? 41.096  -12.494 -52.346 1.00 17.23 ? 41  ALA C N   1 
ATOM   4658 C  CA  . ALA C  1 41  ? 42.431  -13.190 -52.258 1.00 16.79 ? 41  ALA C CA  1 
ATOM   4659 C  C   . ALA C  1 41  ? 43.534  -12.255 -51.942 1.00 16.00 ? 41  ALA C C   1 
ATOM   4660 O  O   . ALA C  1 41  ? 44.634  -12.659 -51.603 1.00 17.33 ? 41  ALA C O   1 
ATOM   4661 C  CB  . ALA C  1 41  ? 42.720  -13.856 -53.611 1.00 17.32 ? 41  ALA C CB  1 
ATOM   4662 N  N   . SER C  1 42  ? 43.307  -10.944 -52.008 1.00 16.76 ? 42  SER C N   1 
ATOM   4663 C  CA  . SER C  1 42  ? 44.362  -10.006 -51.697 1.00 16.08 ? 42  SER C CA  1 
ATOM   4664 C  C   . SER C  1 42  ? 44.629  -9.947  -50.156 1.00 17.09 ? 42  SER C C   1 
ATOM   4665 O  O   . SER C  1 42  ? 45.634  -9.369  -49.738 1.00 17.22 ? 42  SER C O   1 
ATOM   4666 C  CB  . SER C  1 42  ? 44.128  -8.578  -52.198 1.00 18.19 ? 42  SER C CB  1 
ATOM   4667 O  OG  . SER C  1 42  ? 43.195  -7.844  -51.342 1.00 19.64 ? 42  SER C OG  1 
ATOM   4668 N  N   . LEU C  1 43  ? 43.709  -10.531 -49.373 1.00 16.37 ? 43  LEU C N   1 
ATOM   4669 C  CA  . LEU C  1 43  ? 43.750  -10.384 -47.913 1.00 15.15 ? 43  LEU C CA  1 
ATOM   4670 C  C   . LEU C  1 43  ? 44.609  -11.426 -47.225 1.00 14.73 ? 43  LEU C C   1 
ATOM   4671 O  O   . LEU C  1 43  ? 44.116  -12.377 -46.610 1.00 16.60 ? 43  LEU C O   1 
ATOM   4672 C  CB  . LEU C  1 43  ? 42.311  -10.423 -47.359 1.00 14.48 ? 43  LEU C CB  1 
ATOM   4673 C  CG  . LEU C  1 43  ? 41.460  -9.224  -47.891 1.00 14.29 ? 43  LEU C CG  1 
ATOM   4674 C  CD1 . LEU C  1 43  ? 40.012  -9.283  -47.293 1.00 13.88 ? 43  LEU C CD1 1 
ATOM   4675 C  CD2 . LEU C  1 43  ? 42.071  -7.821  -47.760 1.00 15.03 ? 43  LEU C CD2 1 
ATOM   4676 N  N   . THR C  1 44  ? 45.917  -11.237 -47.431 1.00 18.68 ? 44  THR C N   1 
ATOM   4677 C  CA  . THR C  1 44  ? 46.936  -12.153 -46.909 1.00 17.02 ? 44  THR C CA  1 
ATOM   4678 C  C   . THR C  1 44  ? 47.144  -11.866 -45.416 1.00 20.51 ? 44  THR C C   1 
ATOM   4679 O  O   . THR C  1 44  ? 46.692  -10.809 -44.906 1.00 17.53 ? 44  THR C O   1 
ATOM   4680 C  CB  . THR C  1 44  ? 48.252  -11.951 -47.744 1.00 20.08 ? 44  THR C CB  1 
ATOM   4681 O  OG1 . THR C  1 44  ? 48.536  -10.546 -47.863 1.00 22.52 ? 44  THR C OG1 1 
ATOM   4682 C  CG2 . THR C  1 44  ? 48.027  -12.526 -49.137 1.00 22.42 ? 44  THR C CG2 1 
ATOM   4683 N  N   . PRO C  1 45  ? 47.905  -12.687 -44.701 1.00 19.11 ? 45  PRO C N   1 
ATOM   4684 C  CA  . PRO C  1 45  ? 48.069  -12.513 -43.234 1.00 18.62 ? 45  PRO C CA  1 
ATOM   4685 C  C   . PRO C  1 45  ? 48.871  -11.255 -42.943 1.00 21.15 ? 45  PRO C C   1 
ATOM   4686 O  O   . PRO C  1 45  ? 49.824  -10.968 -43.643 1.00 22.67 ? 45  PRO C O   1 
ATOM   4687 C  CB  . PRO C  1 45  ? 48.840  -13.775 -42.850 1.00 20.88 ? 45  PRO C CB  1 
ATOM   4688 C  CG  . PRO C  1 45  ? 48.390  -14.799 -43.872 1.00 20.30 ? 45  PRO C CG  1 
ATOM   4689 C  CD  . PRO C  1 45  ? 48.302  -14.039 -45.162 1.00 20.10 ? 45  PRO C CD  1 
ATOM   4690 N  N   . LEU C  1 46  ? 48.486  -10.427 -41.951 1.00 17.34 ? 46  LEU C N   1 
ATOM   4691 C  CA  . LEU C  1 46  ? 49.257  -9.295  -41.476 1.00 19.20 ? 46  LEU C CA  1 
ATOM   4692 C  C   . LEU C  1 46  ? 50.369  -9.852  -40.561 1.00 17.55 ? 46  LEU C C   1 
ATOM   4693 O  O   . LEU C  1 46  ? 50.166  -10.881 -39.937 1.00 19.53 ? 46  LEU C O   1 
ATOM   4694 C  CB  . LEU C  1 46  ? 48.362  -8.347  -40.677 1.00 18.31 ? 46  LEU C CB  1 
ATOM   4695 C  CG  . LEU C  1 46  ? 47.253  -7.772  -41.544 1.00 19.33 ? 46  LEU C CG  1 
ATOM   4696 C  CD1 . LEU C  1 46  ? 46.423  -6.963  -40.562 1.00 21.43 ? 46  LEU C CD1 1 
ATOM   4697 C  CD2 . LEU C  1 46  ? 47.823  -7.058  -42.772 1.00 21.61 ? 46  LEU C CD2 1 
ATOM   4698 N  N   . GLU C  1 47  ? 51.432  -9.090  -40.464 1.00 19.33 ? 47  GLU C N   1 
ATOM   4699 C  CA  . GLU C  1 47  ? 52.453  -9.327  -39.439 1.00 19.12 ? 47  GLU C CA  1 
ATOM   4700 C  C   . GLU C  1 47  ? 52.491  -8.199  -38.471 1.00 19.50 ? 47  GLU C C   1 
ATOM   4701 O  O   . GLU C  1 47  ? 52.465  -7.007  -38.865 1.00 19.66 ? 47  GLU C O   1 
ATOM   4702 C  CB  . GLU C  1 47  ? 53.814  -9.376  -40.135 1.00 27.85 ? 47  GLU C CB  1 
ATOM   4703 C  CG  . GLU C  1 47  ? 53.864  -10.430 -41.219 1.00 35.05 ? 47  GLU C CG  1 
ATOM   4704 N  N   . PHE C  1 48  ? 52.653  -8.513  -37.201 1.00 17.80 ? 48  PHE C N   1 
ATOM   4705 C  CA  . PHE C  1 48  ? 52.607  -7.524  -36.139 1.00 18.97 ? 48  PHE C CA  1 
ATOM   4706 C  C   . PHE C  1 48  ? 54.045  -7.419  -35.621 1.00 18.47 ? 48  PHE C C   1 
ATOM   4707 O  O   . PHE C  1 48  ? 54.561  -8.360  -35.030 1.00 24.78 ? 48  PHE C O   1 
ATOM   4708 C  CB  . PHE C  1 48  ? 51.565  -7.954  -35.041 1.00 18.70 ? 48  PHE C CB  1 
ATOM   4709 C  CG  . PHE C  1 48  ? 50.259  -8.405  -35.655 1.00 17.91 ? 48  PHE C CG  1 
ATOM   4710 C  CD1 . PHE C  1 48  ? 49.416  -7.465  -36.170 1.00 17.88 ? 48  PHE C CD1 1 
ATOM   4711 C  CD2 . PHE C  1 48  ? 49.954  -9.765  -35.809 1.00 15.60 ? 48  PHE C CD2 1 
ATOM   4712 C  CE1 . PHE C  1 48  ? 48.261  -7.912  -36.833 1.00 17.46 ? 48  PHE C CE1 1 
ATOM   4713 C  CE2 . PHE C  1 48  ? 48.793  -10.226 -36.380 1.00 17.56 ? 48  PHE C CE2 1 
ATOM   4714 C  CZ  . PHE C  1 48  ? 47.957  -9.246  -36.894 1.00 16.47 ? 48  PHE C CZ  1 
ATOM   4715 N  N   . GLN C  1 49  ? 54.623  -6.296  -35.918 1.00 17.40 ? 49  GLN C N   1 
ATOM   4716 C  CA  . GLN C  1 49  ? 56.056  -6.052  -35.627 1.00 21.59 ? 49  GLN C CA  1 
ATOM   4717 C  C   . GLN C  1 49  ? 56.283  -5.130  -34.463 1.00 21.49 ? 49  GLN C C   1 
ATOM   4718 O  O   . GLN C  1 49  ? 55.658  -4.088  -34.391 1.00 17.61 ? 49  GLN C O   1 
ATOM   4719 C  CB  . GLN C  1 49  ? 56.731  -5.534  -36.904 1.00 22.93 ? 49  GLN C CB  1 
ATOM   4720 C  CG  . GLN C  1 49  ? 56.651  -6.614  -37.979 1.00 28.02 ? 49  GLN C CG  1 
ATOM   4721 C  CD  . GLN C  1 49  ? 57.611  -6.418  -39.138 1.00 40.87 ? 49  GLN C CD  1 
ATOM   4722 O  OE1 . GLN C  1 49  ? 58.052  -5.279  -39.460 1.00 45.53 ? 49  GLN C OE1 1 
ATOM   4723 N  NE2 . GLN C  1 49  ? 57.930  -7.530  -39.807 1.00 39.05 ? 49  GLN C NE2 1 
ATOM   4724 N  N   . GLY C  1 50  ? 57.248  -5.467  -33.546 1.00 18.60 ? 50  GLY C N   1 
ATOM   4725 C  CA  . GLY C  1 50  ? 57.506  -4.604  -32.443 1.00 19.11 ? 50  GLY C CA  1 
ATOM   4726 C  C   . GLY C  1 50  ? 56.396  -4.563  -31.418 1.00 19.11 ? 50  GLY C C   1 
ATOM   4727 O  O   . GLY C  1 50  ? 56.354  -3.635  -30.584 1.00 18.61 ? 50  GLY C O   1 
ATOM   4728 N  N   . TYR C  1 51  ? 55.535  -5.556  -31.466 1.00 18.64 ? 51  TYR C N   1 
ATOM   4729 C  CA  . TYR C  1 51  ? 54.413  -5.666  -30.487 1.00 18.77 ? 51  TYR C CA  1 
ATOM   4730 C  C   . TYR C  1 51  ? 54.869  -6.157  -29.104 1.00 17.94 ? 51  TYR C C   1 
ATOM   4731 O  O   . TYR C  1 51  ? 54.169  -5.983  -28.126 1.00 17.07 ? 51  TYR C O   1 
ATOM   4732 C  CB  . TYR C  1 51  ? 53.295  -6.574  -31.028 1.00 16.37 ? 51  TYR C CB  1 
ATOM   4733 C  CG  . TYR C  1 51  ? 52.258  -5.892  -31.907 1.00 14.87 ? 51  TYR C CG  1 
ATOM   4734 C  CD1 . TYR C  1 51  ? 50.895  -6.126  -31.723 1.00 13.77 ? 51  TYR C CD1 1 
ATOM   4735 C  CD2 . TYR C  1 51  ? 52.632  -5.045  -32.937 1.00 15.58 ? 51  TYR C CD2 1 
ATOM   4736 C  CE1 . TYR C  1 51  ? 49.937  -5.526  -32.526 1.00 16.26 ? 51  TYR C CE1 1 
ATOM   4737 C  CE2 . TYR C  1 51  ? 51.677  -4.437  -33.744 1.00 15.96 ? 51  TYR C CE2 1 
ATOM   4738 C  CZ  . TYR C  1 51  ? 50.337  -4.683  -33.542 1.00 16.24 ? 51  TYR C CZ  1 
ATOM   4739 O  OH  . TYR C  1 51  ? 49.392  -4.074  -34.349 1.00 16.96 ? 51  TYR C OH  1 
ATOM   4740 N  N   . ASN C  1 52  ? 56.064  -6.782  -29.045 1.00 19.87 ? 52  ASN C N   1 
ATOM   4741 C  CA  . ASN C  1 52  ? 56.467  -7.367  -27.764 1.00 22.56 ? 52  ASN C CA  1 
ATOM   4742 C  C   . ASN C  1 52  ? 57.180  -6.317  -26.925 1.00 26.59 ? 52  ASN C C   1 
ATOM   4743 O  O   . ASN C  1 52  ? 58.412  -6.168  -27.029 1.00 27.43 ? 52  ASN C O   1 
ATOM   4744 C  CB  . ASN C  1 52  ? 57.393  -8.550  -28.038 1.00 23.45 ? 52  ASN C CB  1 
ATOM   4745 C  CG  . ASN C  1 52  ? 57.728  -9.288  -26.787 1.00 30.11 ? 52  ASN C CG  1 
ATOM   4746 O  OD1 . ASN C  1 52  ? 57.044  -9.183  -25.763 1.00 27.69 ? 52  ASN C OD1 1 
ATOM   4747 N  ND2 . ASN C  1 52  ? 58.861  -9.972  -26.823 1.00 34.72 ? 52  ASN C ND2 1 
ATOM   4748 N  N   . LEU C  1 53  ? 56.426  -5.597  -26.105 1.00 23.52 ? 53  LEU C N   1 
ATOM   4749 C  CA  . LEU C  1 53  ? 56.974  -4.388  -25.557 1.00 31.38 ? 53  LEU C CA  1 
ATOM   4750 C  C   . LEU C  1 53  ? 57.738  -4.779  -24.286 1.00 31.03 ? 53  LEU C C   1 
ATOM   4751 O  O   . LEU C  1 53  ? 57.181  -5.541  -23.439 1.00 28.69 ? 53  LEU C O   1 
ATOM   4752 C  CB  . LEU C  1 53  ? 55.863  -3.338  -25.299 1.00 25.00 ? 53  LEU C CB  1 
ATOM   4753 C  CG  . LEU C  1 53  ? 54.948  -2.836  -26.452 1.00 22.81 ? 53  LEU C CG  1 
ATOM   4754 C  CD1 . LEU C  1 53  ? 53.904  -1.961  -25.753 1.00 19.71 ? 53  LEU C CD1 1 
ATOM   4755 C  CD2 . LEU C  1 53  ? 55.579  -2.021  -27.594 1.00 24.15 ? 53  LEU C CD2 1 
ATOM   4756 N  N   . SER C  1 54  ? 58.938  -4.195  -24.231 1.00 39.48 ? 54  SER C N   1 
ATOM   4757 C  CA  . SER C  1 54  ? 60.032  -4.218  -23.201 1.00 51.54 ? 54  SER C CA  1 
ATOM   4758 C  C   . SER C  1 54  ? 59.451  -4.344  -21.801 1.00 61.02 ? 54  SER C C   1 
ATOM   4759 O  O   . SER C  1 54  ? 58.644  -3.512  -21.381 1.00 50.14 ? 54  SER C O   1 
ATOM   4760 C  CB  . SER C  1 54  ? 60.786  -2.887  -23.253 1.00 57.96 ? 54  SER C CB  1 
ATOM   4761 O  OG  . SER C  1 54  ? 62.135  -3.032  -23.655 1.00 44.63 ? 54  SER C OG  1 
ATOM   4762 N  N   . ALA C  1 55  ? 59.887  -5.352  -21.060 1.00 65.85 ? 55  ALA C N   1 
ATOM   4763 C  CA  . ALA C  1 55  ? 59.641  -5.366  -19.637 1.00 65.97 ? 55  ALA C CA  1 
ATOM   4764 C  C   . ALA C  1 55  ? 60.239  -4.042  -19.193 1.00 64.84 ? 55  ALA C C   1 
ATOM   4765 O  O   . ALA C  1 55  ? 60.919  -3.379  -19.979 1.00 45.97 ? 55  ALA C O   1 
ATOM   4766 C  CB  . ALA C  1 55  ? 60.375  -6.527  -18.989 1.00 63.13 ? 55  ALA C CB  1 
ATOM   4767 N  N   . ASN C  1 56  ? 59.984  -3.637  -17.958 1.00 63.03 ? 56  ASN C N   1 
ATOM   4768 C  CA  . ASN C  1 56  ? 60.610  -2.428  -17.446 1.00 30.00 ? 56  ASN C CA  1 
ATOM   4769 C  C   . ASN C  1 56  ? 60.187  -1.152  -18.175 1.00 38.15 ? 56  ASN C C   1 
ATOM   4770 O  O   . ASN C  1 56  ? 60.314  -0.059  -17.626 1.00 31.51 ? 56  ASN C O   1 
ATOM   4771 C  CB  . ASN C  1 56  ? 62.131  -2.566  -17.512 1.00 20.00 ? 56  ASN C CB  1 
ATOM   4772 N  N   . LYS C  1 57  ? 59.702  -1.290  -19.408 1.00 28.83 ? 57  LYS C N   1 
ATOM   4773 C  CA  . LYS C  1 57  ? 59.194  -0.146  -20.164 1.00 31.84 ? 57  LYS C CA  1 
ATOM   4774 C  C   . LYS C  1 57  ? 57.825  0.190   -19.608 1.00 28.77 ? 57  LYS C C   1 
ATOM   4775 O  O   . LYS C  1 57  ? 57.184  -0.720  -19.012 1.00 23.88 ? 57  LYS C O   1 
ATOM   4776 N  N   . GLN C  1 58  ? 57.386  1.450   -19.772 1.00 31.36 ? 58  GLN C N   1 
ATOM   4777 C  CA  . GLN C  1 58  ? 56.178  1.970   -19.157 1.00 33.65 ? 58  GLN C CA  1 
ATOM   4778 C  C   . GLN C  1 58  ? 55.449  2.684   -20.291 1.00 24.06 ? 58  GLN C C   1 
ATOM   4779 O  O   . GLN C  1 58  ? 56.095  3.426   -21.037 1.00 22.62 ? 58  GLN C O   1 
ATOM   4780 C  CB  . GLN C  1 58  ? 56.605  3.064   -18.150 1.00 35.54 ? 58  GLN C CB  1 
ATOM   4781 C  CG  . GLN C  1 58  ? 56.116  2.882   -16.737 1.00 49.93 ? 58  GLN C CG  1 
ATOM   4782 C  CD  . GLN C  1 58  ? 56.454  4.079   -15.825 1.00 45.08 ? 58  GLN C CD  1 
ATOM   4783 O  OE1 . GLN C  1 58  ? 56.381  3.931   -14.604 1.00 61.10 ? 58  GLN C OE1 1 
ATOM   4784 N  NE2 . GLN C  1 58  ? 56.827  5.270   -16.403 1.00 35.26 ? 58  GLN C NE2 1 
ATOM   4785 N  N   . PHE C  1 59  ? 54.112  2.524   -20.308 1.00 27.51 ? 59  PHE C N   1 
ATOM   4786 C  CA  . PHE C  1 59  ? 53.207  3.097   -21.336 1.00 25.97 ? 59  PHE C CA  1 
ATOM   4787 C  C   . PHE C  1 59  ? 52.093  3.803   -20.645 1.00 21.72 ? 59  PHE C C   1 
ATOM   4788 O  O   . PHE C  1 59  ? 51.546  3.297   -19.657 1.00 24.87 ? 59  PHE C O   1 
ATOM   4789 C  CB  . PHE C  1 59  ? 52.798  1.965   -22.300 1.00 22.60 ? 59  PHE C CB  1 
ATOM   4790 C  CG  . PHE C  1 59  ? 54.009  1.370   -22.935 1.00 22.57 ? 59  PHE C CG  1 
ATOM   4791 C  CD1 . PHE C  1 59  ? 54.570  1.988   -24.064 1.00 20.34 ? 59  PHE C CD1 1 
ATOM   4792 C  CD2 . PHE C  1 59  ? 54.671  0.302   -22.315 1.00 23.82 ? 59  PHE C CD2 1 
ATOM   4793 C  CE1 . PHE C  1 59  ? 55.751  1.487   -24.615 1.00 23.41 ? 59  PHE C CE1 1 
ATOM   4794 C  CE2 . PHE C  1 59  ? 55.844  -0.158  -22.819 1.00 23.43 ? 59  PHE C CE2 1 
ATOM   4795 C  CZ  . PHE C  1 59  ? 56.379  0.419   -23.960 1.00 20.39 ? 59  PHE C CZ  1 
ATOM   4796 N  N   . LEU C  1 60  ? 51.798  5.015   -21.068 1.00 19.73 ? 60  LEU C N   1 
ATOM   4797 C  CA  . LEU C  1 60  ? 50.876  5.859   -20.349 1.00 19.07 ? 60  LEU C CA  1 
ATOM   4798 C  C   . LEU C  1 60  ? 49.430  5.357   -20.588 1.00 22.63 ? 60  LEU C C   1 
ATOM   4799 O  O   . LEU C  1 60  ? 48.977  5.246   -21.751 1.00 20.65 ? 60  LEU C O   1 
ATOM   4800 C  CB  . LEU C  1 60  ? 51.011  7.300   -20.844 1.00 20.41 ? 60  LEU C CB  1 
ATOM   4801 C  CG  . LEU C  1 60  ? 50.109  8.339   -20.193 1.00 22.99 ? 60  LEU C CG  1 
ATOM   4802 C  CD1 . LEU C  1 60  ? 50.533  8.520   -18.741 1.00 21.41 ? 60  LEU C CD1 1 
ATOM   4803 C  CD2 . LEU C  1 60  ? 50.282  9.656   -20.943 1.00 23.40 ? 60  LEU C CD2 1 
ATOM   4804 N  N   . LEU C  1 61  ? 48.721  5.054   -19.518 1.00 20.58 ? 61  LEU C N   1 
ATOM   4805 C  CA  . LEU C  1 61  ? 47.262  4.735   -19.541 1.00 20.21 ? 61  LEU C CA  1 
ATOM   4806 C  C   . LEU C  1 61  ? 46.469  5.959   -19.116 1.00 23.66 ? 61  LEU C C   1 
ATOM   4807 O  O   . LEU C  1 61  ? 46.808  6.572   -18.100 1.00 26.28 ? 61  LEU C O   1 
ATOM   4808 C  CB  . LEU C  1 61  ? 47.053  3.529   -18.652 1.00 20.83 ? 61  LEU C CB  1 
ATOM   4809 C  CG  . LEU C  1 61  ? 45.653  2.905   -18.623 1.00 22.73 ? 61  LEU C CG  1 
ATOM   4810 C  CD1 . LEU C  1 61  ? 45.522  1.972   -19.848 1.00 23.39 ? 61  LEU C CD1 1 
ATOM   4811 C  CD2 . LEU C  1 61  ? 45.521  2.132   -17.297 1.00 25.75 ? 61  LEU C CD2 1 
ATOM   4812 N  N   . THR C  1 62  ? 45.409  6.305   -19.805 1.00 17.80 ? 62  THR C N   1 
ATOM   4813 C  CA  . THR C  1 62  ? 44.739  7.588   -19.630 1.00 17.90 ? 62  THR C CA  1 
ATOM   4814 C  C   . THR C  1 62  ? 43.280  7.287   -19.657 1.00 23.45 ? 62  THR C C   1 
ATOM   4815 O  O   . THR C  1 62  ? 42.760  6.642   -20.593 1.00 22.73 ? 62  THR C O   1 
ATOM   4816 C  CB  . THR C  1 62  ? 44.936  8.634   -20.762 1.00 22.80 ? 62  THR C CB  1 
ATOM   4817 O  OG1 . THR C  1 62  ? 46.306  8.984   -20.792 1.00 23.35 ? 62  THR C OG1 1 
ATOM   4818 C  CG2 . THR C  1 62  ? 44.103  9.991   -20.453 1.00 24.29 ? 62  THR C CG2 1 
ATOM   4819 N  N   . ASN C  1 63  ? 42.559  7.762   -18.674 1.00 22.09 ? 63  ASN C N   1 
ATOM   4820 C  CA  . ASN C  1 63  ? 41.167  7.918   -18.859 1.00 19.01 ? 63  ASN C CA  1 
ATOM   4821 C  C   . ASN C  1 63  ? 40.897  9.249   -19.483 1.00 22.20 ? 63  ASN C C   1 
ATOM   4822 O  O   . ASN C  1 63  ? 41.142  10.287  -18.852 1.00 22.74 ? 63  ASN C O   1 
ATOM   4823 C  CB  . ASN C  1 63  ? 40.537  7.821   -17.456 1.00 17.85 ? 63  ASN C CB  1 
ATOM   4824 C  CG  . ASN C  1 63  ? 39.003  8.094   -17.437 1.00 19.95 ? 63  ASN C CG  1 
ATOM   4825 O  OD1 . ASN C  1 63  ? 38.416  8.762   -18.297 1.00 19.24 ? 63  ASN C OD1 1 
ATOM   4826 N  ND2 . ASN C  1 63  ? 38.363  7.666   -16.341 1.00 16.98 ? 63  ASN C ND2 1 
ATOM   4827 N  N   . ASN C  1 64  ? 40.458  9.245   -20.746 1.00 21.16 ? 64  ASN C N   1 
ATOM   4828 C  CA  . ASN C  1 64  ? 40.174  10.512  -21.455 1.00 23.12 ? 64  ASN C CA  1 
ATOM   4829 C  C   . ASN C  1 64  ? 38.735  10.926  -21.398 1.00 20.22 ? 64  ASN C C   1 
ATOM   4830 O  O   . ASN C  1 64  ? 38.248  11.782  -22.201 1.00 22.30 ? 64  ASN C O   1 
ATOM   4831 C  CB  . ASN C  1 64  ? 40.717  10.423  -22.908 1.00 20.44 ? 64  ASN C CB  1 
ATOM   4832 C  CG  . ASN C  1 64  ? 39.992  9.396   -23.728 1.00 20.79 ? 64  ASN C CG  1 
ATOM   4833 O  OD1 . ASN C  1 64  ? 38.893  8.959   -23.356 1.00 19.48 ? 64  ASN C OD1 1 
ATOM   4834 N  ND2 . ASN C  1 64  ? 40.644  8.914   -24.796 1.00 25.95 ? 64  ASN C ND2 1 
ATOM   4835 N  N   . GLY C  1 65  ? 37.968  10.325  -20.475 1.00 21.20 ? 65  GLY C N   1 
ATOM   4836 C  CA  . GLY C  1 65  ? 36.555  10.638  -20.396 1.00 21.45 ? 65  GLY C CA  1 
ATOM   4837 C  C   . GLY C  1 65  ? 35.643  9.899   -21.375 1.00 23.59 ? 65  GLY C C   1 
ATOM   4838 O  O   . GLY C  1 65  ? 34.434  9.944   -21.234 1.00 25.90 ? 65  GLY C O   1 
ATOM   4839 N  N   . HIS C  1 66  ? 36.259  9.226   -22.356 1.00 18.97 ? 66  HIS C N   1 
ATOM   4840 C  CA  . HIS C  1 66  ? 35.523  8.493   -23.383 1.00 19.11 ? 66  HIS C CA  1 
ATOM   4841 C  C   . HIS C  1 66  ? 35.840  7.026   -23.342 1.00 14.31 ? 66  HIS C C   1 
ATOM   4842 O  O   . HIS C  1 66  ? 34.971  6.191   -23.659 1.00 18.09 ? 66  HIS C O   1 
ATOM   4843 C  CB  . HIS C  1 66  ? 35.823  9.051   -24.752 1.00 15.87 ? 66  HIS C CB  1 
ATOM   4844 C  CG  . HIS C  1 66  ? 35.613  10.516  -24.823 1.00 19.37 ? 66  HIS C CG  1 
ATOM   4845 N  ND1 . HIS C  1 66  ? 36.640  11.395  -25.026 1.00 22.07 ? 66  HIS C ND1 1 
ATOM   4846 C  CD2 . HIS C  1 66  ? 34.454  11.259  -24.704 1.00 16.98 ? 66  HIS C CD2 1 
ATOM   4847 C  CE1 . HIS C  1 66  ? 36.138  12.623  -25.060 1.00 17.73 ? 66  HIS C CE1 1 
ATOM   4848 N  NE2 . HIS C  1 66  ? 34.785  12.537  -24.841 1.00 22.05 ? 66  HIS C NE2 1 
ATOM   4849 N  N   . SER C  1 67  ? 37.053  6.675   -23.012 1.00 17.77 ? 67  SER C N   1 
ATOM   4850 C  CA  . SER C  1 67  ? 37.498  5.329   -22.924 1.00 15.99 ? 67  SER C CA  1 
ATOM   4851 C  C   . SER C  1 67  ? 38.743  5.304   -22.008 1.00 18.13 ? 67  SER C C   1 
ATOM   4852 O  O   . SER C  1 67  ? 39.067  6.359   -21.416 1.00 19.34 ? 67  SER C O   1 
ATOM   4853 C  CB  . SER C  1 67  ? 37.872  4.767   -24.370 1.00 16.25 ? 67  SER C CB  1 
ATOM   4854 O  OG  . SER C  1 67  ? 38.253  3.424   -24.342 1.00 16.62 ? 67  SER C OG  1 
ATOM   4855 N  N   . VAL C  1 68  ? 39.343  4.143   -21.901 1.00 17.23 ? 68  VAL C N   1 
ATOM   4856 C  CA  . VAL C  1 68  ? 40.652  4.034   -21.325 1.00 18.37 ? 68  VAL C CA  1 
ATOM   4857 C  C   . VAL C  1 68  ? 41.598  3.665   -22.461 1.00 20.21 ? 68  VAL C C   1 
ATOM   4858 O  O   . VAL C  1 68  ? 41.358  2.691   -23.218 1.00 17.73 ? 68  VAL C O   1 
ATOM   4859 C  CB  . VAL C  1 68  ? 40.621  3.035   -20.110 1.00 18.48 ? 68  VAL C CB  1 
ATOM   4860 C  CG1 . VAL C  1 68  ? 40.342  1.561   -20.490 1.00 17.67 ? 68  VAL C CG1 1 
ATOM   4861 C  CG2 . VAL C  1 68  ? 41.992  3.074   -19.421 1.00 20.08 ? 68  VAL C CG2 1 
ATOM   4862 N  N   . LYS C  1 69  ? 42.689  4.419   -22.551 1.00 19.77 ? 69  LYS C N   1 
ATOM   4863 C  CA  . LYS C  1 69  ? 43.612  4.301   -23.699 1.00 18.95 ? 69  LYS C CA  1 
ATOM   4864 C  C   . LYS C  1 69  ? 44.995  4.084   -23.205 1.00 20.38 ? 69  LYS C C   1 
ATOM   4865 O  O   . LYS C  1 69  ? 45.404  4.626   -22.116 1.00 22.01 ? 69  LYS C O   1 
ATOM   4866 C  CB  . LYS C  1 69  ? 43.487  5.435   -24.679 1.00 24.32 ? 69  LYS C CB  1 
ATOM   4867 C  CG  . LYS C  1 69  ? 44.025  6.747   -24.242 1.00 29.95 ? 69  LYS C CG  1 
ATOM   4868 C  CD  . LYS C  1 69  ? 44.383  7.626   -25.437 1.00 30.73 ? 69  LYS C CD  1 
ATOM   4869 C  CE  . LYS C  1 69  ? 44.831  8.966   -24.857 1.00 32.52 ? 69  LYS C CE  1 
ATOM   4870 N  NZ  . LYS C  1 69  ? 44.974  10.003  -25.922 1.00 29.66 ? 69  LYS C NZ  1 
ATOM   4871 N  N   . LEU C  1 70  ? 45.701  3.204   -23.873 1.00 16.40 ? 70  LEU C N   1 
ATOM   4872 C  CA  . LEU C  1 70  ? 47.106  2.963   -23.608 1.00 15.96 ? 70  LEU C CA  1 
ATOM   4873 C  C   . LEU C  1 70  ? 47.895  3.533   -24.784 1.00 17.02 ? 70  LEU C C   1 
ATOM   4874 O  O   . LEU C  1 70  ? 47.721  3.111   -25.949 1.00 15.47 ? 70  LEU C O   1 
ATOM   4875 C  CB  . LEU C  1 70  ? 47.368  1.490   -23.464 1.00 13.92 ? 70  LEU C CB  1 
ATOM   4876 C  CG  . LEU C  1 70  ? 48.797  1.070   -23.138 1.00 17.19 ? 70  LEU C CG  1 
ATOM   4877 C  CD1 . LEU C  1 70  ? 49.092  1.531   -21.692 1.00 17.67 ? 70  LEU C CD1 1 
ATOM   4878 C  CD2 . LEU C  1 70  ? 48.872  -0.449  -23.172 1.00 14.96 ? 70  LEU C CD2 1 
ATOM   4879 N  N   . ASN C  1 71  ? 48.818  4.459   -24.525 1.00 17.35 ? 71  ASN C N   1 
ATOM   4880 C  CA  . ASN C  1 71  ? 49.681  4.979   -25.539 1.00 17.71 ? 71  ASN C CA  1 
ATOM   4881 C  C   . ASN C  1 71  ? 50.663  3.859   -25.977 1.00 17.76 ? 71  ASN C C   1 
ATOM   4882 O  O   . ASN C  1 71  ? 51.138  3.019   -25.168 1.00 18.52 ? 71  ASN C O   1 
ATOM   4883 C  CB  . ASN C  1 71  ? 50.377  6.223   -25.008 1.00 16.75 ? 71  ASN C CB  1 
ATOM   4884 C  CG  . ASN C  1 71  ? 49.495  7.458   -25.056 1.00 23.96 ? 71  ASN C CG  1 
ATOM   4885 O  OD1 . ASN C  1 71  ? 48.324  7.426   -25.476 1.00 22.85 ? 71  ASN C OD1 1 
ATOM   4886 N  ND2 . ASN C  1 71  ? 50.080  8.612   -24.643 1.00 26.43 ? 71  ASN C ND2 1 
ATOM   4887 N  N   . LEU C  1 72  ? 50.954  3.800   -27.296 1.00 15.44 ? 72  LEU C N   1 
ATOM   4888 C  CA  . LEU C  1 72  ? 51.803  2.733   -27.839 1.00 16.22 ? 72  LEU C CA  1 
ATOM   4889 C  C   . LEU C  1 72  ? 52.919  3.396   -28.657 1.00 15.22 ? 72  LEU C C   1 
ATOM   4890 O  O   . LEU C  1 72  ? 52.756  4.516   -29.138 1.00 15.98 ? 72  LEU C O   1 
ATOM   4891 C  CB  . LEU C  1 72  ? 50.986  1.905   -28.855 1.00 13.23 ? 72  LEU C CB  1 
ATOM   4892 C  CG  . LEU C  1 72  ? 49.954  0.963   -28.157 1.00 15.73 ? 72  LEU C CG  1 
ATOM   4893 C  CD1 . LEU C  1 72  ? 49.063  0.297   -29.209 1.00 16.01 ? 72  LEU C CD1 1 
ATOM   4894 C  CD2 . LEU C  1 72  ? 50.555  -0.077  -27.214 1.00 18.28 ? 72  LEU C CD2 1 
ATOM   4895 N  N   . PRO C  1 73  ? 54.103  2.776   -28.715 1.00 19.13 ? 73  PRO C N   1 
ATOM   4896 C  CA  . PRO C  1 73  ? 55.247  3.416   -29.335 1.00 18.09 ? 73  PRO C CA  1 
ATOM   4897 C  C   . PRO C  1 73  ? 55.242  3.224   -30.880 1.00 20.82 ? 73  PRO C C   1 
ATOM   4898 O  O   . PRO C  1 73  ? 54.728  2.214   -31.351 1.00 19.89 ? 73  PRO C O   1 
ATOM   4899 C  CB  . PRO C  1 73  ? 56.429  2.675   -28.673 1.00 19.29 ? 73  PRO C CB  1 
ATOM   4900 C  CG  . PRO C  1 73  ? 55.967  1.234   -28.576 1.00 19.19 ? 73  PRO C CG  1 
ATOM   4901 C  CD  . PRO C  1 73  ? 54.453  1.394   -28.288 1.00 16.73 ? 73  PRO C CD  1 
ATOM   4902 N  N   . SER C  1 74  ? 55.732  4.223   -31.591 1.00 22.86 ? 74  SER C N   1 
ATOM   4903 C  CA  . SER C  1 74  ? 55.734  4.258   -33.061 1.00 21.53 ? 74  SER C CA  1 
ATOM   4904 C  C   . SER C  1 74  ? 56.614  3.192   -33.735 1.00 25.04 ? 74  SER C C   1 
ATOM   4905 O  O   . SER C  1 74  ? 56.483  2.929   -34.954 1.00 23.78 ? 74  SER C O   1 
ATOM   4906 C  CB  . SER C  1 74  ? 55.943  5.684   -33.611 1.00 27.92 ? 74  SER C CB  1 
ATOM   4907 O  OG  . SER C  1 74  ? 57.224  6.174   -33.301 1.00 30.64 ? 74  SER C OG  1 
ATOM   4908 N  N   A ASP C  1 75  ? 57.565  2.645   -33.009 0.50 21.51 ? 75  ASP C N   1 
ATOM   4909 N  N   B ASP C  1 75  ? 57.471  2.489   -32.973 0.50 23.89 ? 75  ASP C N   1 
ATOM   4910 C  CA  A ASP C  1 75  ? 58.284  1.588   -33.646 0.50 21.20 ? 75  ASP C CA  1 
ATOM   4911 C  CA  B ASP C  1 75  ? 58.233  1.320   -33.527 0.50 23.43 ? 75  ASP C CA  1 
ATOM   4912 C  C   A ASP C  1 75  ? 57.393  0.323   -33.848 0.50 19.74 ? 75  ASP C C   1 
ATOM   4913 C  C   B ASP C  1 75  ? 57.434  0.045   -33.624 0.50 20.79 ? 75  ASP C C   1 
ATOM   4914 O  O   A ASP C  1 75  ? 57.737  -0.445  -34.762 0.50 18.60 ? 75  ASP C O   1 
ATOM   4915 O  O   B ASP C  1 75  ? 57.818  -1.024  -34.138 0.50 18.26 ? 75  ASP C O   1 
ATOM   4916 C  CB  A ASP C  1 75  ? 59.645  1.318   -32.988 0.50 20.93 ? 75  ASP C CB  1 
ATOM   4917 C  CB  B ASP C  1 75  ? 59.528  1.064   -32.770 0.50 26.94 ? 75  ASP C CB  1 
ATOM   4918 C  CG  A ASP C  1 75  ? 59.495  1.010   -31.550 0.50 19.97 ? 75  ASP C CG  1 
ATOM   4919 C  CG  B ASP C  1 75  ? 60.416  2.234   -32.810 0.50 27.27 ? 75  ASP C CG  1 
ATOM   4920 O  OD1 A ASP C  1 75  ? 59.151  1.960   -30.814 0.50 21.19 ? 75  ASP C OD1 1 
ATOM   4921 O  OD1 B ASP C  1 75  ? 60.474  2.896   -33.879 0.50 31.09 ? 75  ASP C OD1 1 
ATOM   4922 O  OD2 A ASP C  1 75  ? 59.663  -0.153  -31.191 0.50 22.19 ? 75  ASP C OD2 1 
ATOM   4923 O  OD2 B ASP C  1 75  ? 60.992  2.534   -31.742 0.50 30.36 ? 75  ASP C OD2 1 
ATOM   4924 N  N   . MET C  1 76  ? 56.250  0.153   -33.114 1.00 18.06 ? 76  MET C N   1 
ATOM   4925 C  CA  . MET C  1 76  ? 55.333  -0.964  -33.263 1.00 17.24 ? 76  MET C CA  1 
ATOM   4926 C  C   . MET C  1 76  ? 54.475  -0.722  -34.522 1.00 15.34 ? 76  MET C C   1 
ATOM   4927 O  O   . MET C  1 76  ? 54.091  0.419   -34.740 1.00 17.84 ? 76  MET C O   1 
ATOM   4928 C  CB  . MET C  1 76  ? 54.460  -0.875  -32.072 1.00 20.68 ? 76  MET C CB  1 
ATOM   4929 C  CG  . MET C  1 76  ? 53.437  -1.914  -31.947 1.00 20.38 ? 76  MET C CG  1 
ATOM   4930 S  SD  . MET C  1 76  ? 52.607  -1.678  -30.373 1.00 19.61 ? 76  MET C SD  1 
ATOM   4931 C  CE  . MET C  1 76  ? 51.023  -2.478  -30.835 1.00 16.29 ? 76  MET C CE  1 
ATOM   4932 N  N   . HIS C  1 77  ? 54.435  -1.737  -35.343 1.00 14.68 ? 77  HIS C N   1 
ATOM   4933 C  CA  . HIS C  1 77  ? 53.766  -1.574  -36.711 1.00 16.52 ? 77  HIS C CA  1 
ATOM   4934 C  C   . HIS C  1 77  ? 53.203  -2.786  -37.286 1.00 16.69 ? 77  HIS C C   1 
ATOM   4935 O  O   . HIS C  1 77  ? 53.516  -3.920  -36.956 1.00 15.93 ? 77  HIS C O   1 
ATOM   4936 C  CB  . HIS C  1 77  ? 54.597  -0.788  -37.733 1.00 20.27 ? 77  HIS C CB  1 
ATOM   4937 C  CG  . HIS C  1 77  ? 55.854  -1.487  -38.121 1.00 22.21 ? 77  HIS C CG  1 
ATOM   4938 N  ND1 . HIS C  1 77  ? 57.054  -1.259  -37.500 1.00 25.32 ? 77  HIS C ND1 1 
ATOM   4939 C  CD2 . HIS C  1 77  ? 56.067  -2.450  -39.055 1.00 23.47 ? 77  HIS C CD2 1 
ATOM   4940 C  CE1 . HIS C  1 77  ? 57.967  -2.023  -38.048 1.00 21.95 ? 77  HIS C CE1 1 
ATOM   4941 N  NE2 . HIS C  1 77  ? 57.396  -2.749  -39.035 1.00 24.43 ? 77  HIS C NE2 1 
ATOM   4942 N  N   . ILE C  1 78  ? 52.210  -2.551  -38.165 1.00 15.83 ? 78  ILE C N   1 
ATOM   4943 C  CA  . ILE C  1 78  ? 51.712  -3.638  -39.028 1.00 17.12 ? 78  ILE C CA  1 
ATOM   4944 C  C   . ILE C  1 78  ? 52.445  -3.715  -40.376 1.00 16.72 ? 78  ILE C C   1 
ATOM   4945 O  O   . ILE C  1 78  ? 52.663  -2.691  -40.985 1.00 17.94 ? 78  ILE C O   1 
ATOM   4946 C  CB  . ILE C  1 78  ? 50.222  -3.293  -39.387 1.00 16.76 ? 78  ILE C CB  1 
ATOM   4947 C  CG1 . ILE C  1 78  ? 49.328  -3.198  -38.158 1.00 19.59 ? 78  ILE C CG1 1 
ATOM   4948 C  CG2 . ILE C  1 78  ? 49.652  -4.309  -40.397 1.00 18.06 ? 78  ILE C CG2 1 
ATOM   4949 C  CD1 . ILE C  1 78  ? 47.915  -2.596  -38.453 1.00 17.91 ? 78  ILE C CD1 1 
ATOM   4950 N  N   . GLN C  1 79  ? 52.887  -4.913  -40.740 1.00 18.63 ? 79  GLN C N   1 
ATOM   4951 C  CA  . GLN C  1 79  ? 53.454  -5.181  -42.019 1.00 22.14 ? 79  GLN C CA  1 
ATOM   4952 C  C   . GLN C  1 79  ? 52.429  -5.964  -42.808 1.00 20.32 ? 79  GLN C C   1 
ATOM   4953 O  O   . GLN C  1 79  ? 51.777  -6.878  -42.255 1.00 20.26 ? 79  GLN C O   1 
ATOM   4954 C  CB  . GLN C  1 79  ? 54.692  -6.078  -41.759 1.00 26.94 ? 79  GLN C CB  1 
ATOM   4955 C  CG  . GLN C  1 79  ? 55.499  -6.370  -43.021 1.00 34.64 ? 79  GLN C CG  1 
ATOM   4956 C  CD  . GLN C  1 79  ? 56.326  -5.151  -43.417 1.00 41.26 ? 79  GLN C CD  1 
ATOM   4957 O  OE1 . GLN C  1 79  ? 57.260  -4.730  -42.681 1.00 48.66 ? 79  GLN C OE1 1 
ATOM   4958 N  NE2 . GLN C  1 79  ? 55.975  -4.545  -44.549 1.00 48.70 ? 79  GLN C NE2 1 
ATOM   4959 N  N   . GLY C  1 80  ? 52.303  -5.697  -44.096 1.00 18.73 ? 80  GLY C N   1 
ATOM   4960 C  CA  . GLY C  1 80  ? 51.402  -6.425  -44.984 1.00 21.78 ? 80  GLY C CA  1 
ATOM   4961 C  C   . GLY C  1 80  ? 50.370  -5.590  -45.728 1.00 23.39 ? 80  GLY C C   1 
ATOM   4962 O  O   . GLY C  1 80  ? 49.686  -6.077  -46.692 1.00 25.60 ? 80  GLY C O   1 
ATOM   4963 N  N   . LEU C  1 81  ? 50.240  -4.320  -45.336 1.00 21.65 ? 81  LEU C N   1 
ATOM   4964 C  CA  . LEU C  1 81  ? 49.336  -3.421  -46.019 1.00 22.37 ? 81  LEU C CA  1 
ATOM   4965 C  C   . LEU C  1 81  ? 50.139  -2.620  -47.081 1.00 22.97 ? 81  LEU C C   1 
ATOM   4966 O  O   . LEU C  1 81  ? 51.368  -2.779  -47.152 1.00 25.08 ? 81  LEU C O   1 
ATOM   4967 C  CB  . LEU C  1 81  ? 48.680  -2.453  -45.010 1.00 19.68 ? 81  LEU C CB  1 
ATOM   4968 C  CG  . LEU C  1 81  ? 47.814  -3.132  -43.963 1.00 17.37 ? 81  LEU C CG  1 
ATOM   4969 C  CD1 . LEU C  1 81  ? 47.341  -2.217  -42.831 1.00 17.56 ? 81  LEU C CD1 1 
ATOM   4970 C  CD2 . LEU C  1 81  ? 46.527  -3.632  -44.704 1.00 18.60 ? 81  LEU C CD2 1 
ATOM   4971 N  N   . GLN C  1 82  ? 49.514  -1.727  -47.814 1.00 24.84 ? 82  GLN C N   1 
ATOM   4972 C  CA  . GLN C  1 82  ? 50.273  -1.064  -48.879 1.00 27.13 ? 82  GLN C CA  1 
ATOM   4973 C  C   . GLN C  1 82  ? 51.273  -0.022  -48.361 1.00 27.71 ? 82  GLN C C   1 
ATOM   4974 O  O   . GLN C  1 82  ? 52.223  0.305   -49.063 1.00 26.01 ? 82  GLN C O   1 
ATOM   4975 C  CB  . GLN C  1 82  ? 49.363  -0.535  -50.008 1.00 34.91 ? 82  GLN C CB  1 
ATOM   4976 C  CG  . GLN C  1 82  ? 48.717  -1.630  -50.881 1.00 38.96 ? 82  GLN C CG  1 
ATOM   4977 C  CD  . GLN C  1 82  ? 49.581  -2.193  -52.030 1.00 40.44 ? 82  GLN C CD  1 
ATOM   4978 O  OE1 . GLN C  1 82  ? 49.186  -3.190  -52.627 1.00 50.27 ? 82  GLN C OE1 1 
ATOM   4979 N  NE2 . GLN C  1 82  ? 50.741  -1.579  -52.347 1.00 34.42 ? 82  GLN C NE2 1 
ATOM   4980 N  N   . SER C  1 83  ? 51.076  0.482   -47.134 1.00 21.52 ? 83  SER C N   1 
ATOM   4981 C  CA  . SER C  1 83  ? 52.010  1.410   -46.434 1.00 18.00 ? 83  SER C CA  1 
ATOM   4982 C  C   . SER C  1 83  ? 52.253  0.797   -45.102 1.00 17.65 ? 83  SER C C   1 
ATOM   4983 O  O   . SER C  1 83  ? 51.524  -0.076  -44.689 1.00 15.73 ? 83  SER C O   1 
ATOM   4984 C  CB  . SER C  1 83  ? 51.438  2.779   -46.191 1.00 19.83 ? 83  SER C CB  1 
ATOM   4985 O  OG  . SER C  1 83  ? 51.091  3.447   -47.395 1.00 24.06 ? 83  SER C OG  1 
ATOM   4986 N  N   . ARG C  1 84  ? 53.360  1.153   -44.426 1.00 15.78 ? 84  ARG C N   1 
ATOM   4987 C  CA  . ARG C  1 84  ? 53.512  0.899   -43.007 1.00 14.74 ? 84  ARG C CA  1 
ATOM   4988 C  C   . ARG C  1 84  ? 52.591  1.704   -42.197 1.00 13.36 ? 84  ARG C C   1 
ATOM   4989 O  O   . ARG C  1 84  ? 52.479  2.896   -42.374 1.00 15.12 ? 84  ARG C O   1 
ATOM   4990 C  CB  . ARG C  1 84  ? 54.992  1.198   -42.630 1.00 14.54 ? 84  ARG C CB  1 
ATOM   4991 C  CG  . ARG C  1 84  ? 55.147  0.967   -41.075 1.00 14.84 ? 84  ARG C CG  1 
ATOM   4992 C  CD  . ARG C  1 84  ? 56.594  1.136   -40.601 1.00 15.82 ? 84  ARG C CD  1 
ATOM   4993 N  NE  . ARG C  1 84  ? 57.377  0.070   -41.169 1.00 16.06 ? 84  ARG C NE  1 
ATOM   4994 C  CZ  . ARG C  1 84  ? 58.713  -0.078  -40.848 1.00 19.51 ? 84  ARG C CZ  1 
ATOM   4995 N  NH1 . ARG C  1 84  ? 59.297  0.835   -40.106 1.00 21.42 ? 84  ARG C NH1 1 
ATOM   4996 N  NH2 . ARG C  1 84  ? 59.392  -1.081  -41.322 1.00 19.84 ? 84  ARG C NH2 1 
ATOM   4997 N  N   . TYR C  1 85  ? 51.879  0.998   -41.282 1.00 13.26 ? 85  TYR C N   1 
ATOM   4998 C  CA  . TYR C  1 85  ? 51.065  1.714   -40.305 1.00 13.79 ? 85  TYR C CA  1 
ATOM   4999 C  C   . TYR C  1 85  ? 51.677  1.451   -38.932 1.00 13.41 ? 85  TYR C C   1 
ATOM   5000 O  O   . TYR C  1 85  ? 51.811  0.297   -38.554 1.00 12.92 ? 85  TYR C O   1 
ATOM   5001 C  CB  . TYR C  1 85  ? 49.586  1.136   -40.373 1.00 15.20 ? 85  TYR C CB  1 
ATOM   5002 C  CG  . TYR C  1 85  ? 48.849  1.693   -41.584 1.00 13.04 ? 85  TYR C CG  1 
ATOM   5003 C  CD1 . TYR C  1 85  ? 48.029  2.816   -41.440 1.00 12.40 ? 85  TYR C CD1 1 
ATOM   5004 C  CD2 . TYR C  1 85  ? 48.967  1.100   -42.840 1.00 15.16 ? 85  TYR C CD2 1 
ATOM   5005 C  CE1 . TYR C  1 85  ? 47.314  3.286   -42.551 1.00 13.22 ? 85  TYR C CE1 1 
ATOM   5006 C  CE2 . TYR C  1 85  ? 48.237  1.578   -43.920 1.00 15.06 ? 85  TYR C CE2 1 
ATOM   5007 C  CZ  . TYR C  1 85  ? 47.472  2.674   -43.768 1.00 13.67 ? 85  TYR C CZ  1 
ATOM   5008 O  OH  . TYR C  1 85  ? 46.794  3.117   -44.912 1.00 15.95 ? 85  TYR C OH  1 
ATOM   5009 N  N   . SER C  1 86  ? 52.013  2.532   -38.266 1.00 14.96 ? 86  SER C N   1 
ATOM   5010 C  CA  . SER C  1 86  ? 52.621  2.481   -36.957 1.00 15.20 ? 86  SER C CA  1 
ATOM   5011 C  C   . SER C  1 86  ? 51.599  2.713   -35.835 1.00 16.05 ? 86  SER C C   1 
ATOM   5012 O  O   . SER C  1 86  ? 50.728  3.601   -35.942 1.00 15.81 ? 86  SER C O   1 
ATOM   5013 C  CB  . SER C  1 86  ? 53.772  3.522   -36.850 1.00 17.92 ? 86  SER C CB  1 
ATOM   5014 O  OG  . SER C  1 86  ? 54.761  3.237   -37.859 1.00 16.75 ? 86  SER C OG  1 
ATOM   5015 N  N   . ALA C  1 87  ? 51.827  2.034   -34.723 1.00 14.95 ? 87  ALA C N   1 
ATOM   5016 C  CA  . ALA C  1 87  ? 50.922  2.197   -33.596 1.00 14.63 ? 87  ALA C CA  1 
ATOM   5017 C  C   . ALA C  1 87  ? 50.940  3.571   -32.952 1.00 15.61 ? 87  ALA C C   1 
ATOM   5018 O  O   . ALA C  1 87  ? 51.963  4.272   -32.905 1.00 15.63 ? 87  ALA C O   1 
ATOM   5019 C  CB  . ALA C  1 87  ? 51.194  1.141   -32.566 1.00 15.91 ? 87  ALA C CB  1 
ATOM   5020 N  N   . THR C  1 88  ? 49.769  3.966   -32.442 1.00 13.70 ? 88  THR C N   1 
ATOM   5021 C  CA  . THR C  1 88  ? 49.567  5.144   -31.617 1.00 13.92 ? 88  THR C CA  1 
ATOM   5022 C  C   . THR C  1 88  ? 48.958  4.867   -30.257 1.00 15.40 ? 88  THR C C   1 
ATOM   5023 O  O   . THR C  1 88  ? 49.445  5.412   -29.258 1.00 15.95 ? 88  THR C O   1 
ATOM   5024 C  CB  . THR C  1 88  ? 48.989  6.303   -32.394 1.00 15.92 ? 88  THR C CB  1 
ATOM   5025 O  OG1 . THR C  1 88  ? 48.917  7.458   -31.540 1.00 17.98 ? 88  THR C OG1 1 
ATOM   5026 C  CG2 . THR C  1 88  ? 47.597  5.978   -32.950 1.00 15.62 ? 88  THR C CG2 1 
ATOM   5027 N  N   . GLN C  1 89  ? 47.925  4.016   -30.137 1.00 14.67 ? 89  GLN C N   1 
ATOM   5028 C  CA  . GLN C  1 89  ? 47.249  3.819   -28.844 1.00 14.29 ? 89  GLN C CA  1 
ATOM   5029 C  C   . GLN C  1 89  ? 46.316  2.630   -29.077 1.00 13.21 ? 89  GLN C C   1 
ATOM   5030 O  O   . GLN C  1 89  ? 45.929  2.315   -30.279 1.00 13.17 ? 89  GLN C O   1 
ATOM   5031 C  CB  . GLN C  1 89  ? 46.511  5.053   -28.360 1.00 16.36 ? 89  GLN C CB  1 
ATOM   5032 C  CG  . GLN C  1 89  ? 45.545  5.755   -29.317 1.00 18.96 ? 89  GLN C CG  1 
ATOM   5033 C  CD  . GLN C  1 89  ? 44.075  5.375   -29.086 1.00 16.77 ? 89  GLN C CD  1 
ATOM   5034 O  OE1 . GLN C  1 89  ? 43.762  4.275   -28.720 1.00 16.78 ? 89  GLN C OE1 1 
ATOM   5035 N  NE2 . GLN C  1 89  ? 43.218  6.290   -29.303 1.00 25.64 ? 89  GLN C NE2 1 
ATOM   5036 N  N   . LEU C  1 90  ? 45.938  1.960   -27.983 1.00 12.77 ? 90  LEU C N   1 
ATOM   5037 C  CA  . LEU C  1 90  ? 44.791  1.101   -28.029 1.00 13.03 ? 90  LEU C CA  1 
ATOM   5038 C  C   . LEU C  1 90  ? 43.803  1.530   -27.010 1.00 13.55 ? 90  LEU C C   1 
ATOM   5039 O  O   . LEU C  1 90  ? 44.095  2.334   -26.093 1.00 15.33 ? 90  LEU C O   1 
ATOM   5040 C  CB  . LEU C  1 90  ? 45.219  -0.341  -27.873 1.00 13.92 ? 90  LEU C CB  1 
ATOM   5041 C  CG  . LEU C  1 90  ? 45.950  -0.723  -26.541 1.00 15.59 ? 90  LEU C CG  1 
ATOM   5042 C  CD1 . LEU C  1 90  ? 44.971  -0.861  -25.383 1.00 16.11 ? 90  LEU C CD1 1 
ATOM   5043 C  CD2 . LEU C  1 90  ? 46.511  -2.092  -26.795 1.00 13.91 ? 90  LEU C CD2 1 
ATOM   5044 N  N   . HIS C  1 91  ? 42.554  1.084   -27.150 1.00 11.28 ? 91  HIS C N   1 
ATOM   5045 C  CA  . HIS C  1 91  ? 41.501  1.456   -26.226 1.00 12.02 ? 91  HIS C CA  1 
ATOM   5046 C  C   . HIS C  1 91  ? 40.348  0.460   -26.380 1.00 11.50 ? 91  HIS C C   1 
ATOM   5047 O  O   . HIS C  1 91  ? 40.377  -0.430  -27.216 1.00 12.12 ? 91  HIS C O   1 
ATOM   5048 C  CB  . HIS C  1 91  ? 41.067  2.892   -26.467 1.00 12.56 ? 91  HIS C CB  1 
ATOM   5049 C  CG  . HIS C  1 91  ? 40.455  3.040   -27.798 1.00 11.70 ? 91  HIS C CG  1 
ATOM   5050 N  ND1 . HIS C  1 91  ? 41.157  3.491   -28.887 1.00 12.53 ? 91  HIS C ND1 1 
ATOM   5051 C  CD2 . HIS C  1 91  ? 39.175  2.737   -28.207 1.00 11.54 ? 91  HIS C CD2 1 
ATOM   5052 C  CE1 . HIS C  1 91  ? 40.341  3.445   -29.961 1.00 11.48 ? 91  HIS C CE1 1 
ATOM   5053 N  NE2 . HIS C  1 91  ? 39.166  2.922   -29.598 1.00 10.72 ? 91  HIS C NE2 1 
ATOM   5054 N  N   . LEU C  1 92  ? 39.319  0.563   -25.487 1.00 12.61 ? 92  LEU C N   1 
ATOM   5055 C  CA  . LEU C  1 92  ? 38.232  -0.409  -25.531 1.00 13.29 ? 92  LEU C CA  1 
ATOM   5056 C  C   . LEU C  1 92  ? 36.880  0.326   -25.552 1.00 9.54  ? 92  LEU C C   1 
ATOM   5057 O  O   . LEU C  1 92  ? 36.714  1.520   -25.258 1.00 12.86 ? 92  LEU C O   1 
ATOM   5058 C  CB  . LEU C  1 92  ? 38.252  -1.366  -24.275 1.00 13.08 ? 92  LEU C CB  1 
ATOM   5059 C  CG  . LEU C  1 92  ? 39.488  -2.281  -24.333 1.00 14.54 ? 92  LEU C CG  1 
ATOM   5060 C  CD1 . LEU C  1 92  ? 40.500  -1.804  -23.330 1.00 19.72 ? 92  LEU C CD1 1 
ATOM   5061 C  CD2 . LEU C  1 92  ? 39.159  -3.709  -24.131 1.00 17.40 ? 92  LEU C CD2 1 
ATOM   5062 N  N   . HIS C  1 93  ? 35.871  -0.510  -25.958 1.00 11.49 ? 93  HIS C N   1 
ATOM   5063 C  CA  . HIS C  1 93  ? 34.431  -0.116  -25.892 1.00 9.86  ? 93  HIS C CA  1 
ATOM   5064 C  C   . HIS C  1 93  ? 33.649  -1.228  -25.199 1.00 10.34 ? 93  HIS C C   1 
ATOM   5065 O  O   . HIS C  1 93  ? 33.857  -2.361  -25.458 1.00 11.72 ? 93  HIS C O   1 
ATOM   5066 C  CB  . HIS C  1 93  ? 33.909  0.101   -27.336 1.00 11.00 ? 93  HIS C CB  1 
ATOM   5067 C  CG  . HIS C  1 93  ? 34.685  1.112   -28.120 1.00 9.19  ? 93  HIS C CG  1 
ATOM   5068 N  ND1 . HIS C  1 93  ? 34.396  2.446   -28.144 1.00 10.92 ? 93  HIS C ND1 1 
ATOM   5069 C  CD2 . HIS C  1 93  ? 35.823  0.942   -28.964 1.00 10.21 ? 93  HIS C CD2 1 
ATOM   5070 C  CE1 . HIS C  1 93  ? 35.282  3.105   -28.973 1.00 10.84 ? 93  HIS C CE1 1 
ATOM   5071 N  NE2 . HIS C  1 93  ? 36.161  2.180   -29.439 1.00 9.79  ? 93  HIS C NE2 1 
ATOM   5072 N  N   . TRP C  1 94  ? 32.712  -0.842  -24.321 1.00 10.68 ? 94  TRP C N   1 
ATOM   5073 C  CA  . TRP C  1 94  ? 31.909  -1.839  -23.652 1.00 11.50 ? 94  TRP C CA  1 
ATOM   5074 C  C   . TRP C  1 94  ? 30.483  -1.292  -23.416 1.00 11.05 ? 94  TRP C C   1 
ATOM   5075 O  O   . TRP C  1 94  ? 30.123  -0.162  -23.788 1.00 10.99 ? 94  TRP C O   1 
ATOM   5076 C  CB  . TRP C  1 94  ? 32.657  -2.239  -22.313 1.00 12.27 ? 94  TRP C CB  1 
ATOM   5077 C  CG  . TRP C  1 94  ? 32.940  -1.059  -21.417 1.00 12.73 ? 94  TRP C CG  1 
ATOM   5078 C  CD1 . TRP C  1 94  ? 32.121  -0.524  -20.428 1.00 13.17 ? 94  TRP C CD1 1 
ATOM   5079 C  CD2 . TRP C  1 94  ? 34.144  -0.220  -21.412 1.00 11.34 ? 94  TRP C CD2 1 
ATOM   5080 N  NE1 . TRP C  1 94  ? 32.718  0.551   -19.826 1.00 12.82 ? 94  TRP C NE1 1 
ATOM   5081 C  CE2 . TRP C  1 94  ? 33.934  0.787   -20.370 1.00 13.00 ? 94  TRP C CE2 1 
ATOM   5082 C  CE3 . TRP C  1 94  ? 35.326  -0.204  -22.133 1.00 11.99 ? 94  TRP C CE3 1 
ATOM   5083 C  CZ2 . TRP C  1 94  ? 34.880  1.757   -20.082 1.00 14.61 ? 94  TRP C CZ2 1 
ATOM   5084 C  CZ3 . TRP C  1 94  ? 36.275  0.779   -21.834 1.00 12.62 ? 94  TRP C CZ3 1 
ATOM   5085 C  CH2 . TRP C  1 94  ? 36.053  1.731   -20.835 1.00 15.56 ? 94  TRP C CH2 1 
ATOM   5086 N  N   . GLY C  1 95  ? 29.710  -2.182  -22.734 1.00 12.38 ? 95  GLY C N   1 
ATOM   5087 C  CA  . GLY C  1 95  ? 28.278  -1.892  -22.435 1.00 13.23 ? 95  GLY C CA  1 
ATOM   5088 C  C   . GLY C  1 95  ? 28.128  -1.540  -20.927 1.00 13.47 ? 95  GLY C C   1 
ATOM   5089 O  O   . GLY C  1 95  ? 28.736  -0.582  -20.414 1.00 13.49 ? 95  GLY C O   1 
ATOM   5090 N  N   . ASN C  1 96  ? 27.172  -2.264  -20.309 1.00 14.71 ? 96  ASN C N   1 
ATOM   5091 C  CA  . ASN C  1 96  ? 26.974  -2.008  -18.861 1.00 14.75 ? 96  ASN C CA  1 
ATOM   5092 C  C   . ASN C  1 96  ? 26.539  -3.326  -18.234 1.00 15.14 ? 96  ASN C C   1 
ATOM   5093 O  O   . ASN C  1 96  ? 26.180  -4.272  -18.896 1.00 16.35 ? 96  ASN C O   1 
ATOM   5094 C  CB  . ASN C  1 96  ? 25.977  -0.891  -18.642 1.00 15.80 ? 96  ASN C CB  1 
ATOM   5095 C  CG  . ASN C  1 96  ? 24.543  -1.261  -18.934 1.00 22.35 ? 96  ASN C CG  1 
ATOM   5096 O  OD1 . ASN C  1 96  ? 23.842  -1.783  -18.049 1.00 22.93 ? 96  ASN C OD1 1 
ATOM   5097 N  ND2 . ASN C  1 96  ? 24.075  -0.951  -20.109 1.00 22.94 ? 96  ASN C ND2 1 
ATOM   5098 N  N   . PRO C  1 97  ? 26.545  -3.438  -16.865 1.00 18.36 ? 97  PRO C N   1 
ATOM   5099 C  CA  . PRO C  1 97  ? 26.248  -4.793  -16.317 1.00 17.68 ? 97  PRO C CA  1 
ATOM   5100 C  C   . PRO C  1 97  ? 24.817  -5.329  -16.518 1.00 17.45 ? 97  PRO C C   1 
ATOM   5101 O  O   . PRO C  1 97  ? 24.586  -6.527  -16.516 1.00 20.37 ? 97  PRO C O   1 
ATOM   5102 C  CB  . PRO C  1 97  ? 26.414  -4.560  -14.799 1.00 19.44 ? 97  PRO C CB  1 
ATOM   5103 C  CG  . PRO C  1 97  ? 27.425  -3.485  -14.756 1.00 18.87 ? 97  PRO C CG  1 
ATOM   5104 C  CD  . PRO C  1 97  ? 27.075  -2.519  -15.816 1.00 20.28 ? 97  PRO C CD  1 
ATOM   5105 N  N   . ASN C  1 98  ? 23.928  -4.405  -16.738 1.00 16.45 ? 98  ASN C N   1 
ATOM   5106 C  CA  . ASN C  1 98  ? 22.504  -4.753  -17.041 1.00 21.47 ? 98  ASN C CA  1 
ATOM   5107 C  C   . ASN C  1 98  ? 22.318  -5.152  -18.506 1.00 21.92 ? 98  ASN C C   1 
ATOM   5108 O  O   . ASN C  1 98  ? 21.330  -5.777  -18.849 1.00 23.78 ? 98  ASN C O   1 
ATOM   5109 C  CB  . ASN C  1 98  ? 21.587  -3.580  -16.758 1.00 22.74 ? 98  ASN C CB  1 
ATOM   5110 C  CG  . ASN C  1 98  ? 21.485  -3.274  -15.272 1.00 28.30 ? 98  ASN C CG  1 
ATOM   5111 O  OD1 . ASN C  1 98  ? 21.549  -4.176  -14.472 1.00 32.57 ? 98  ASN C OD1 1 
ATOM   5112 N  ND2 . ASN C  1 98  ? 21.365  -2.010  -14.928 1.00 36.33 ? 98  ASN C ND2 1 
ATOM   5113 N  N   . ASP C  1 99  ? 23.252  -4.743  -19.378 1.00 19.66 ? 99  ASP C N   1 
ATOM   5114 C  CA  . ASP C  1 99  ? 23.168  -5.108  -20.838 1.00 17.28 ? 99  ASP C CA  1 
ATOM   5115 C  C   . ASP C  1 99  ? 24.641  -5.213  -21.317 1.00 15.62 ? 99  ASP C C   1 
ATOM   5116 O  O   . ASP C  1 99  ? 25.133  -4.275  -21.979 1.00 15.85 ? 99  ASP C O   1 
ATOM   5117 C  CB  . ASP C  1 99  ? 22.382  -4.029  -21.599 1.00 16.30 ? 99  ASP C CB  1 
ATOM   5118 C  CG  . ASP C  1 99  ? 21.875  -4.489  -22.984 1.00 16.90 ? 99  ASP C CG  1 
ATOM   5119 O  OD1 . ASP C  1 99  ? 22.002  -5.651  -23.260 1.00 19.41 ? 99  ASP C OD1 1 
ATOM   5120 O  OD2 . ASP C  1 99  ? 21.558  -3.625  -23.816 1.00 19.44 ? 99  ASP C OD2 1 
ATOM   5121 N  N   . PRO C  1 100 ? 25.263  -6.357  -21.042 1.00 15.56 ? 100 PRO C N   1 
ATOM   5122 C  CA  . PRO C  1 100 ? 26.741  -6.448  -21.179 1.00 14.24 ? 100 PRO C CA  1 
ATOM   5123 C  C   . PRO C  1 100 ? 27.098  -6.856  -22.628 1.00 14.24 ? 100 PRO C C   1 
ATOM   5124 O  O   . PRO C  1 100 ? 27.725  -7.865  -22.900 1.00 14.84 ? 100 PRO C O   1 
ATOM   5125 C  CB  . PRO C  1 100 ? 27.120  -7.566  -20.202 1.00 16.64 ? 100 PRO C CB  1 
ATOM   5126 C  CG  . PRO C  1 100 ? 25.914  -8.387  -20.018 1.00 17.68 ? 100 PRO C CG  1 
ATOM   5127 C  CD  . PRO C  1 100 ? 24.706  -7.560  -20.351 1.00 16.68 ? 100 PRO C CD  1 
ATOM   5128 N  N   . HIS C  1 101 ? 26.668  -6.007  -23.577 1.00 13.34 ? 101 HIS C N   1 
ATOM   5129 C  CA  . HIS C  1 101 ? 26.851  -6.291  -25.036 1.00 13.78 ? 101 HIS C CA  1 
ATOM   5130 C  C   . HIS C  1 101 ? 27.199  -4.963  -25.704 1.00 14.90 ? 101 HIS C C   1 
ATOM   5131 O  O   . HIS C  1 101 ? 26.378  -4.446  -26.460 1.00 18.08 ? 101 HIS C O   1 
ATOM   5132 C  CB  . HIS C  1 101 ? 25.531  -6.828  -25.610 1.00 16.24 ? 101 HIS C CB  1 
ATOM   5133 C  CG  . HIS C  1 101 ? 24.977  -7.971  -24.850 1.00 16.04 ? 101 HIS C CG  1 
ATOM   5134 N  ND1 . HIS C  1 101 ? 25.574  -9.195  -24.807 1.00 17.25 ? 101 HIS C ND1 1 
ATOM   5135 C  CD2 . HIS C  1 101 ? 23.981  -7.983  -23.860 1.00 17.67 ? 101 HIS C CD2 1 
ATOM   5136 C  CE1 . HIS C  1 101 ? 24.892  -10.000 -23.947 1.00 19.12 ? 101 HIS C CE1 1 
ATOM   5137 N  NE2 . HIS C  1 101 ? 23.940  -9.246  -23.356 1.00 18.03 ? 101 HIS C NE2 1 
ATOM   5138 N  N   . GLY C  1 102 ? 28.455  -4.510  -25.563 1.00 12.43 ? 102 GLY C N   1 
ATOM   5139 C  CA  . GLY C  1 102 ? 28.915  -3.217  -26.001 1.00 12.98 ? 102 GLY C CA  1 
ATOM   5140 C  C   . GLY C  1 102 ? 30.040  -3.172  -26.982 1.00 10.71 ? 102 GLY C C   1 
ATOM   5141 O  O   . GLY C  1 102 ? 30.703  -2.136  -27.089 1.00 11.39 ? 102 GLY C O   1 
ATOM   5142 N  N   . SER C  1 103 ? 30.171  -4.220  -27.770 1.00 11.01 ? 103 SER C N   1 
ATOM   5143 C  CA  . SER C  1 103 ? 31.048  -4.081  -28.953 1.00 10.21 ? 103 SER C CA  1 
ATOM   5144 C  C   . SER C  1 103 ? 30.477  -2.991  -29.907 1.00 11.38 ? 103 SER C C   1 
ATOM   5145 O  O   . SER C  1 103 ? 29.274  -2.615  -29.866 1.00 11.92 ? 103 SER C O   1 
ATOM   5146 C  CB  . SER C  1 103 ? 31.182  -5.444  -29.681 1.00 9.89  ? 103 SER C CB  1 
ATOM   5147 O  OG  . SER C  1 103 ? 29.949  -5.811  -30.363 1.00 9.99  ? 103 SER C OG  1 
ATOM   5148 N  N   . GLU C  1 104 ? 31.350  -2.542  -30.798 1.00 9.76  ? 104 GLU C N   1 
ATOM   5149 C  CA  . GLU C  1 104 ? 30.931  -1.600  -31.820 1.00 9.52  ? 104 GLU C CA  1 
ATOM   5150 C  C   . GLU C  1 104 ? 30.462  -2.277  -33.037 1.00 9.07  ? 104 GLU C C   1 
ATOM   5151 O  O   . GLU C  1 104 ? 29.295  -2.090  -33.483 1.00 8.89  ? 104 GLU C O   1 
ATOM   5152 C  CB  . GLU C  1 104 ? 32.063  -0.576  -32.117 1.00 9.07  ? 104 GLU C CB  1 
ATOM   5153 C  CG  . GLU C  1 104 ? 32.639  0.121   -30.853 1.00 10.60 ? 104 GLU C CG  1 
ATOM   5154 C  CD  . GLU C  1 104 ? 32.953  1.535   -31.205 1.00 10.33 ? 104 GLU C CD  1 
ATOM   5155 O  OE1 . GLU C  1 104 ? 34.014  1.747   -31.825 1.00 10.65 ? 104 GLU C OE1 1 
ATOM   5156 O  OE2 . GLU C  1 104 ? 32.119  2.439   -30.970 1.00 10.06 ? 104 GLU C OE2 1 
ATOM   5157 N  N   . HIS C  1 105 ? 31.316  -3.098  -33.671 1.00 8.25  ? 105 HIS C N   1 
ATOM   5158 C  CA  . HIS C  1 105 ? 30.838  -3.933  -34.765 1.00 8.96  ? 105 HIS C CA  1 
ATOM   5159 C  C   . HIS C  1 105 ? 29.948  -5.013  -34.252 1.00 8.07  ? 105 HIS C C   1 
ATOM   5160 O  O   . HIS C  1 105 ? 30.083  -5.534  -33.119 1.00 9.43  ? 105 HIS C O   1 
ATOM   5161 C  CB  . HIS C  1 105 ? 32.096  -4.529  -35.446 1.00 8.91  ? 105 HIS C CB  1 
ATOM   5162 C  CG  . HIS C  1 105 ? 32.853  -3.522  -36.214 1.00 8.86  ? 105 HIS C CG  1 
ATOM   5163 N  ND1 . HIS C  1 105 ? 33.874  -2.810  -35.670 1.00 9.15  ? 105 HIS C ND1 1 
ATOM   5164 C  CD2 . HIS C  1 105 ? 32.650  -2.997  -37.502 1.00 8.55  ? 105 HIS C CD2 1 
ATOM   5165 C  CE1 . HIS C  1 105 ? 34.358  -1.899  -36.604 1.00 8.98  ? 105 HIS C CE1 1 
ATOM   5166 N  NE2 . HIS C  1 105 ? 33.606  -2.030  -37.728 1.00 8.92  ? 105 HIS C NE2 1 
ATOM   5167 N  N   . THR C  1 106 ? 28.979  -5.418  -35.059 1.00 8.35  ? 106 THR C N   1 
ATOM   5168 C  CA  . THR C  1 106 ? 28.128  -6.578  -34.707 1.00 9.56  ? 106 THR C CA  1 
ATOM   5169 C  C   . THR C  1 106 ? 28.295  -7.600  -35.816 1.00 10.69 ? 106 THR C C   1 
ATOM   5170 O  O   . THR C  1 106 ? 28.767  -7.321  -36.931 1.00 9.97  ? 106 THR C O   1 
ATOM   5171 C  CB  . THR C  1 106 ? 26.638  -6.121  -34.576 1.00 10.15 ? 106 THR C CB  1 
ATOM   5172 O  OG1 . THR C  1 106 ? 26.187  -5.586  -35.841 1.00 11.22 ? 106 THR C OG1 1 
ATOM   5173 C  CG2 . THR C  1 106 ? 26.459  -5.117  -33.477 1.00 10.72 ? 106 THR C CG2 1 
ATOM   5174 N  N   . VAL C  1 107 ? 27.940  -8.858  -35.492 1.00 11.43 ? 107 VAL C N   1 
ATOM   5175 C  CA  . VAL C  1 107 ? 28.010  -9.929  -36.475 1.00 11.17 ? 107 VAL C CA  1 
ATOM   5176 C  C   . VAL C  1 107 ? 26.631  -10.570 -36.564 1.00 11.84 ? 107 VAL C C   1 
ATOM   5177 O  O   . VAL C  1 107 ? 26.112  -11.024 -35.549 1.00 12.51 ? 107 VAL C O   1 
ATOM   5178 C  CB  . VAL C  1 107 ? 29.062  -10.990 -36.030 1.00 12.66 ? 107 VAL C CB  1 
ATOM   5179 C  CG1 . VAL C  1 107 ? 29.043  -12.226 -36.980 1.00 14.27 ? 107 VAL C CG1 1 
ATOM   5180 C  CG2 . VAL C  1 107 ? 30.485  -10.315 -35.876 1.00 13.13 ? 107 VAL C CG2 1 
ATOM   5181 N  N   . SER C  1 108 ? 26.047  -10.555 -37.747 1.00 11.88 ? 108 SER C N   1 
ATOM   5182 C  CA  . SER C  1 108 ? 24.688  -11.090 -37.944 1.00 13.58 ? 108 SER C CA  1 
ATOM   5183 C  C   . SER C  1 108 ? 23.726  -10.474 -36.927 1.00 12.97 ? 108 SER C C   1 
ATOM   5184 O  O   . SER C  1 108 ? 22.854  -11.141 -36.379 1.00 14.08 ? 108 SER C O   1 
ATOM   5185 C  CB  . SER C  1 108 ? 24.652  -12.637 -37.805 1.00 14.82 ? 108 SER C CB  1 
ATOM   5186 O  OG  . SER C  1 108 ? 25.485  -13.137 -38.829 1.00 18.80 ? 108 SER C OG  1 
ATOM   5187 N  N   . GLY C  1 109 ? 23.910  -9.183  -36.640 1.00 11.88 ? 109 GLY C N   1 
ATOM   5188 C  CA  . GLY C  1 109 ? 23.048  -8.381  -35.845 1.00 12.23 ? 109 GLY C CA  1 
ATOM   5189 C  C   . GLY C  1 109 ? 23.411  -8.418  -34.368 1.00 13.06 ? 109 GLY C C   1 
ATOM   5190 O  O   . GLY C  1 109 ? 22.809  -7.655  -33.581 1.00 16.93 ? 109 GLY C O   1 
ATOM   5191 N  N   . GLN C  1 110 ? 24.371  -9.256  -33.960 1.00 12.82 ? 110 GLN C N   1 
ATOM   5192 C  CA  . GLN C  1 110 ? 24.640  -9.488  -32.542 1.00 13.74 ? 110 GLN C CA  1 
ATOM   5193 C  C   . GLN C  1 110 ? 25.863  -8.718  -32.050 1.00 12.03 ? 110 GLN C C   1 
ATOM   5194 O  O   . GLN C  1 110 ? 26.923  -8.776  -32.723 1.00 11.79 ? 110 GLN C O   1 
ATOM   5195 C  CB  . GLN C  1 110 ? 24.962  -10.998 -32.281 1.00 16.09 ? 110 GLN C CB  1 
ATOM   5196 C  CG  . GLN C  1 110 ? 23.870  -11.933 -32.839 1.00 17.43 ? 110 GLN C CG  1 
ATOM   5197 C  CD  . GLN C  1 110 ? 22.454  -11.519 -32.401 1.00 16.78 ? 110 GLN C CD  1 
ATOM   5198 O  OE1 . GLN C  1 110 ? 22.178  -11.391 -31.187 1.00 20.98 ? 110 GLN C OE1 1 
ATOM   5199 N  NE2 . GLN C  1 110 ? 21.569  -11.247 -33.424 1.00 19.85 ? 110 GLN C NE2 1 
ATOM   5200 N  N   . HIS C  1 111 ? 25.712  -8.024  -30.905 1.00 13.46 ? 111 HIS C N   1 
ATOM   5201 C  CA  . HIS C  1 111 ? 26.874  -7.431  -30.272 1.00 13.38 ? 111 HIS C CA  1 
ATOM   5202 C  C   . HIS C  1 111 ? 27.668  -8.465  -29.555 1.00 14.87 ? 111 HIS C C   1 
ATOM   5203 O  O   . HIS C  1 111 ? 27.083  -9.452  -29.033 1.00 18.28 ? 111 HIS C O   1 
ATOM   5204 C  CB  . HIS C  1 111 ? 26.532  -6.382  -29.201 1.00 13.37 ? 111 HIS C CB  1 
ATOM   5205 C  CG  . HIS C  1 111 ? 26.044  -5.138  -29.762 1.00 13.05 ? 111 HIS C CG  1 
ATOM   5206 N  ND1 . HIS C  1 111 ? 26.821  -4.015  -29.965 1.00 12.91 ? 111 HIS C ND1 1 
ATOM   5207 C  CD2 . HIS C  1 111 ? 24.767  -4.843  -30.294 1.00 14.11 ? 111 HIS C CD2 1 
ATOM   5208 C  CE1 . HIS C  1 111 ? 26.048  -3.067  -30.566 1.00 14.09 ? 111 HIS C CE1 1 
ATOM   5209 N  NE2 . HIS C  1 111 ? 24.778  -3.571  -30.696 1.00 17.48 ? 111 HIS C NE2 1 
ATOM   5210 N  N   . PHE C  1 112 ? 28.962  -8.274  -29.488 1.00 12.32 ? 112 PHE C N   1 
ATOM   5211 C  CA  . PHE C  1 112 ? 29.814  -8.988  -28.516 1.00 13.16 ? 112 PHE C CA  1 
ATOM   5212 C  C   . PHE C  1 112 ? 29.855  -8.200  -27.222 1.00 13.19 ? 112 PHE C C   1 
ATOM   5213 O  O   . PHE C  1 112 ? 29.307  -7.116  -27.156 1.00 12.79 ? 112 PHE C O   1 
ATOM   5214 C  CB  . PHE C  1 112 ? 31.212  -9.243  -29.144 1.00 14.71 ? 112 PHE C CB  1 
ATOM   5215 C  CG  . PHE C  1 112 ? 31.215  -10.389 -30.118 1.00 15.19 ? 112 PHE C CG  1 
ATOM   5216 C  CD1 . PHE C  1 112 ? 31.717  -11.647 -29.709 1.00 17.64 ? 112 PHE C CD1 1 
ATOM   5217 C  CD2 . PHE C  1 112 ? 30.631  -10.307 -31.446 1.00 16.01 ? 112 PHE C CD2 1 
ATOM   5218 C  CE1 . PHE C  1 112 ? 31.720  -12.718 -30.598 1.00 19.16 ? 112 PHE C CE1 1 
ATOM   5219 C  CE2 . PHE C  1 112 ? 30.605  -11.462 -32.290 1.00 20.38 ? 112 PHE C CE2 1 
ATOM   5220 C  CZ  . PHE C  1 112 ? 31.207  -12.642 -31.846 1.00 20.30 ? 112 PHE C CZ  1 
ATOM   5221 N  N   . ALA C  1 113 ? 30.480  -8.746  -26.148 1.00 13.94 ? 113 ALA C N   1 
ATOM   5222 C  CA  . ALA C  1 113 ? 30.538  -8.029  -24.910 1.00 12.55 ? 113 ALA C CA  1 
ATOM   5223 C  C   . ALA C  1 113 ? 31.254  -6.728  -24.935 1.00 11.12 ? 113 ALA C C   1 
ATOM   5224 O  O   . ALA C  1 113 ? 30.853  -5.763  -24.306 1.00 12.59 ? 113 ALA C O   1 
ATOM   5225 C  CB  . ALA C  1 113 ? 31.087  -8.939  -23.792 1.00 14.55 ? 113 ALA C CB  1 
ATOM   5226 N  N   . ALA C  1 114 ? 32.368  -6.695  -25.681 1.00 11.54 ? 114 ALA C N   1 
ATOM   5227 C  CA  . ALA C  1 114 ? 33.194  -5.513  -25.736 1.00 11.24 ? 114 ALA C CA  1 
ATOM   5228 C  C   . ALA C  1 114 ? 34.081  -5.634  -26.953 1.00 10.10 ? 114 ALA C C   1 
ATOM   5229 O  O   . ALA C  1 114 ? 33.994  -6.625  -27.689 1.00 11.55 ? 114 ALA C O   1 
ATOM   5230 C  CB  . ALA C  1 114 ? 34.009  -5.460  -24.424 1.00 12.38 ? 114 ALA C CB  1 
ATOM   5231 N  N   . GLU C  1 115 ? 34.810  -4.552  -27.250 1.00 10.88 ? 115 GLU C N   1 
ATOM   5232 C  CA  . GLU C  1 115 ? 35.671  -4.597  -28.419 1.00 11.77 ? 115 GLU C CA  1 
ATOM   5233 C  C   . GLU C  1 115 ? 36.962  -3.785  -28.084 1.00 9.42  ? 115 GLU C C   1 
ATOM   5234 O  O   . GLU C  1 115 ? 36.917  -2.643  -27.505 1.00 11.12 ? 115 GLU C O   1 
ATOM   5235 C  CB  . GLU C  1 115 ? 34.931  -3.953  -29.596 1.00 10.99 ? 115 GLU C CB  1 
ATOM   5236 C  CG  . GLU C  1 115 ? 35.626  -4.076  -30.981 1.00 10.82 ? 115 GLU C CG  1 
ATOM   5237 C  CD  . GLU C  1 115 ? 34.678  -3.684  -32.071 1.00 9.99  ? 115 GLU C CD  1 
ATOM   5238 O  OE1 . GLU C  1 115 ? 35.164  -3.198  -33.130 1.00 9.97  ? 115 GLU C OE1 1 
ATOM   5239 O  OE2 . GLU C  1 115 ? 33.470  -3.969  -31.994 1.00 11.34 ? 115 GLU C OE2 1 
ATOM   5240 N  N   . LEU C  1 116 ? 38.117  -4.364  -28.534 1.00 10.27 ? 116 LEU C N   1 
ATOM   5241 C  CA  . LEU C  1 116 ? 39.390  -3.658  -28.380 1.00 10.55 ? 116 LEU C CA  1 
ATOM   5242 C  C   . LEU C  1 116 ? 39.800  -3.080  -29.774 1.00 9.98  ? 116 LEU C C   1 
ATOM   5243 O  O   . LEU C  1 116 ? 39.721  -3.840  -30.800 1.00 10.67 ? 116 LEU C O   1 
ATOM   5244 C  CB  . LEU C  1 116 ? 40.442  -4.706  -27.957 1.00 12.96 ? 116 LEU C CB  1 
ATOM   5245 C  CG  . LEU C  1 116 ? 41.907  -4.213  -28.023 1.00 12.58 ? 116 LEU C CG  1 
ATOM   5246 C  CD1 . LEU C  1 116 ? 42.237  -3.337  -26.863 1.00 15.58 ? 116 LEU C CD1 1 
ATOM   5247 C  CD2 . LEU C  1 116 ? 42.872  -5.401  -28.240 1.00 15.70 ? 116 LEU C CD2 1 
ATOM   5248 N  N   . HIS C  1 117 ? 40.305  -1.861  -29.759 1.00 10.70 ? 117 HIS C N   1 
ATOM   5249 C  CA  . HIS C  1 117 ? 40.811  -1.242  -31.029 1.00 10.31 ? 117 HIS C CA  1 
ATOM   5250 C  C   . HIS C  1 117 ? 42.270  -0.942  -30.801 1.00 11.98 ? 117 HIS C C   1 
ATOM   5251 O  O   . HIS C  1 117 ? 42.610  -0.227  -29.864 1.00 11.40 ? 117 HIS C O   1 
ATOM   5252 C  CB  . HIS C  1 117 ? 40.064  0.037   -31.300 1.00 10.98 ? 117 HIS C CB  1 
ATOM   5253 C  CG  . HIS C  1 117 ? 38.692  -0.222  -31.747 1.00 9.18  ? 117 HIS C CG  1 
ATOM   5254 N  ND1 . HIS C  1 117 ? 37.705  0.702   -31.622 1.00 10.75 ? 117 HIS C ND1 1 
ATOM   5255 C  CD2 . HIS C  1 117 ? 38.179  -1.354  -32.328 1.00 10.40 ? 117 HIS C CD2 1 
ATOM   5256 C  CE1 . HIS C  1 117 ? 36.583  0.151   -32.115 1.00 10.24 ? 117 HIS C CE1 1 
ATOM   5257 N  NE2 . HIS C  1 117 ? 36.829  -1.084  -32.561 1.00 9.73  ? 117 HIS C NE2 1 
ATOM   5258 N  N   . ILE C  1 118 ? 43.090  -1.328  -31.751 1.00 10.39 ? 118 ILE C N   1 
ATOM   5259 C  CA  . ILE C  1 118 ? 44.551  -0.987  -31.773 1.00 11.42 ? 118 ILE C CA  1 
ATOM   5260 C  C   . ILE C  1 118 ? 44.778  -0.057  -32.953 1.00 10.30 ? 118 ILE C C   1 
ATOM   5261 O  O   . ILE C  1 118 ? 44.624  -0.479  -34.183 1.00 10.35 ? 118 ILE C O   1 
ATOM   5262 C  CB  . ILE C  1 118 ? 45.429  -2.256  -31.891 1.00 11.27 ? 118 ILE C CB  1 
ATOM   5263 C  CG1 . ILE C  1 118 ? 45.072  -3.259  -30.865 1.00 12.86 ? 118 ILE C CG1 1 
ATOM   5264 C  CG2 . ILE C  1 118 ? 46.921  -1.780  -31.671 1.00 12.73 ? 118 ILE C CG2 1 
ATOM   5265 C  CD1 . ILE C  1 118 ? 45.911  -4.538  -30.878 1.00 15.61 ? 118 ILE C CD1 1 
ATOM   5266 N  N   . VAL C  1 119 ? 45.027  1.199   -32.678 1.00 11.66 ? 119 VAL C N   1 
ATOM   5267 C  CA  . VAL C  1 119 ? 44.942  2.317   -33.643 1.00 10.97 ? 119 VAL C CA  1 
ATOM   5268 C  C   . VAL C  1 119 ? 46.328  2.560   -34.184 1.00 12.84 ? 119 VAL C C   1 
ATOM   5269 O  O   . VAL C  1 119 ? 47.327  2.691   -33.402 1.00 12.93 ? 119 VAL C O   1 
ATOM   5270 C  CB  . VAL C  1 119 ? 44.465  3.602   -33.020 1.00 11.16 ? 119 VAL C CB  1 
ATOM   5271 C  CG1 . VAL C  1 119 ? 44.293  4.721   -34.071 1.00 12.22 ? 119 VAL C CG1 1 
ATOM   5272 C  CG2 . VAL C  1 119 ? 43.084  3.367   -32.316 1.00 13.55 ? 119 VAL C CG2 1 
ATOM   5273 N  N   . HIS C  1 120 ? 46.447  2.587   -35.512 1.00 11.53 ? 120 HIS C N   1 
ATOM   5274 C  CA  . HIS C  1 120 ? 47.771  2.835   -36.238 1.00 13.36 ? 120 HIS C CA  1 
ATOM   5275 C  C   . HIS C  1 120 ? 47.600  3.956   -37.190 1.00 14.61 ? 120 HIS C C   1 
ATOM   5276 O  O   . HIS C  1 120 ? 46.516  4.197   -37.711 1.00 12.44 ? 120 HIS C O   1 
ATOM   5277 C  CB  . HIS C  1 120 ? 48.210  1.606   -36.974 1.00 12.76 ? 120 HIS C CB  1 
ATOM   5278 C  CG  . HIS C  1 120 ? 48.352  0.357   -36.171 1.00 12.63 ? 120 HIS C CG  1 
ATOM   5279 N  ND1 . HIS C  1 120 ? 47.284  -0.357  -35.646 1.00 12.68 ? 120 HIS C ND1 1 
ATOM   5280 C  CD2 . HIS C  1 120 ? 49.488  -0.352  -35.815 1.00 14.97 ? 120 HIS C CD2 1 
ATOM   5281 C  CE1 . HIS C  1 120 ? 47.721  -1.494  -35.080 1.00 13.48 ? 120 HIS C CE1 1 
ATOM   5282 N  NE2 . HIS C  1 120 ? 49.092  -1.488  -35.127 1.00 13.96 ? 120 HIS C NE2 1 
ATOM   5283 N  N   . TYR C  1 121 ? 48.729  4.614   -37.562 1.00 14.25 ? 121 TYR C N   1 
ATOM   5284 C  CA  . TYR C  1 121 ? 48.657  5.696   -38.527 1.00 16.59 ? 121 TYR C CA  1 
ATOM   5285 C  C   . TYR C  1 121 ? 49.630  5.374   -39.669 1.00 15.17 ? 121 TYR C C   1 
ATOM   5286 O  O   . TYR C  1 121 ? 50.660  4.642   -39.433 1.00 14.09 ? 121 TYR C O   1 
ATOM   5287 C  CB  . TYR C  1 121 ? 48.939  7.004   -37.862 1.00 16.38 ? 121 TYR C CB  1 
ATOM   5288 C  CG  . TYR C  1 121 ? 50.354  7.221   -37.368 1.00 15.99 ? 121 TYR C CG  1 
ATOM   5289 C  CD1 . TYR C  1 121 ? 51.264  7.989   -38.128 1.00 16.67 ? 121 TYR C CD1 1 
ATOM   5290 C  CD2 . TYR C  1 121 ? 50.763  6.704   -36.127 1.00 16.35 ? 121 TYR C CD2 1 
ATOM   5291 C  CE1 . TYR C  1 121 ? 52.595  8.127   -37.669 1.00 17.01 ? 121 TYR C CE1 1 
ATOM   5292 C  CE2 . TYR C  1 121 ? 52.097  6.846   -35.673 1.00 18.54 ? 121 TYR C CE2 1 
ATOM   5293 C  CZ  . TYR C  1 121 ? 52.983  7.587   -36.460 1.00 20.12 ? 121 TYR C CZ  1 
ATOM   5294 O  OH  . TYR C  1 121 ? 54.309  7.771   -35.995 1.00 21.08 ? 121 TYR C OH  1 
ATOM   5295 N  N   . ASN C  1 122 ? 49.413  6.034   -40.811 1.00 15.36 ? 122 ASN C N   1 
ATOM   5296 C  CA  . ASN C  1 122 ? 50.295  5.799   -41.958 1.00 14.21 ? 122 ASN C CA  1 
ATOM   5297 C  C   . ASN C  1 122 ? 51.576  6.651   -41.851 1.00 14.94 ? 122 ASN C C   1 
ATOM   5298 O  O   . ASN C  1 122 ? 51.563  7.819   -42.127 1.00 15.44 ? 122 ASN C O   1 
ATOM   5299 C  CB  . ASN C  1 122 ? 49.560  6.172   -43.179 1.00 16.81 ? 122 ASN C CB  1 
ATOM   5300 C  CG  . ASN C  1 122 ? 50.266  5.791   -44.416 1.00 16.51 ? 122 ASN C CG  1 
ATOM   5301 O  OD1 . ASN C  1 122 ? 51.520  5.722   -44.492 1.00 16.76 ? 122 ASN C OD1 1 
ATOM   5302 N  ND2 . ASN C  1 122 ? 49.464  5.531   -45.464 1.00 19.74 ? 122 ASN C ND2 1 
ATOM   5303 N  N   . SER C  1 123 ? 52.608  5.969   -41.383 1.00 15.29 ? 123 SER C N   1 
ATOM   5304 C  CA  . SER C  1 123 ? 53.836  6.700   -41.034 1.00 16.16 ? 123 SER C CA  1 
ATOM   5305 C  C   . SER C  1 123 ? 54.702  6.887   -42.260 1.00 18.45 ? 123 SER C C   1 
ATOM   5306 O  O   . SER C  1 123 ? 55.645  7.689   -42.212 1.00 17.91 ? 123 SER C O   1 
ATOM   5307 C  CB  . SER C  1 123 ? 54.511  5.916   -39.919 1.00 15.33 ? 123 SER C CB  1 
ATOM   5308 O  OG  . SER C  1 123 ? 54.717  4.597   -40.206 1.00 14.86 ? 123 SER C OG  1 
ATOM   5309 N  N   . ASP C  1 124 ? 54.426  6.190   -43.340 1.00 16.35 ? 124 ASP C N   1 
ATOM   5310 C  CA  . ASP C  1 124 ? 55.110  6.469   -44.620 1.00 15.66 ? 124 ASP C CA  1 
ATOM   5311 C  C   . ASP C  1 124 ? 54.691  7.796   -45.203 1.00 19.93 ? 124 ASP C C   1 
ATOM   5312 O  O   . ASP C  1 124 ? 55.488  8.398   -45.956 1.00 23.51 ? 124 ASP C O   1 
ATOM   5313 C  CB  . ASP C  1 124 ? 54.829  5.389   -45.617 1.00 16.09 ? 124 ASP C CB  1 
ATOM   5314 C  CG  . ASP C  1 124 ? 55.469  4.056   -45.295 1.00 17.22 ? 124 ASP C CG  1 
ATOM   5315 O  OD1 . ASP C  1 124 ? 56.504  3.982   -44.515 1.00 17.52 ? 124 ASP C OD1 1 
ATOM   5316 O  OD2 . ASP C  1 124 ? 55.032  3.036   -45.791 1.00 16.30 ? 124 ASP C OD2 1 
ATOM   5317 N  N   . LEU C  1 125 ? 53.477  8.229   -44.907 1.00 15.38 ? 125 LEU C N   1 
ATOM   5318 C  CA  . LEU C  1 125 ? 52.916  9.439   -45.440 1.00 18.92 ? 125 LEU C CA  1 
ATOM   5319 C  C   . LEU C  1 125 ? 52.930  10.592  -44.447 1.00 20.91 ? 125 LEU C C   1 
ATOM   5320 O  O   . LEU C  1 125 ? 53.023  11.753  -44.837 1.00 21.73 ? 125 LEU C O   1 
ATOM   5321 C  CB  . LEU C  1 125 ? 51.462  9.226   -45.930 1.00 20.01 ? 125 LEU C CB  1 
ATOM   5322 C  CG  . LEU C  1 125 ? 51.199  8.279   -47.107 1.00 23.32 ? 125 LEU C CG  1 
ATOM   5323 C  CD1 . LEU C  1 125 ? 49.752  8.379   -47.564 1.00 30.80 ? 125 LEU C CD1 1 
ATOM   5324 C  CD2 . LEU C  1 125 ? 52.139  8.556   -48.270 1.00 24.24 ? 125 LEU C CD2 1 
ATOM   5325 N  N   . TYR C  1 126 ? 52.803  10.249  -43.180 1.00 17.38 ? 126 TYR C N   1 
ATOM   5326 C  CA  . TYR C  1 126 ? 52.485  11.272  -42.181 1.00 17.05 ? 126 TYR C CA  1 
ATOM   5327 C  C   . TYR C  1 126 ? 53.350  11.161  -40.946 1.00 17.16 ? 126 TYR C C   1 
ATOM   5328 O  O   . TYR C  1 126 ? 53.731  10.095  -40.586 1.00 16.42 ? 126 TYR C O   1 
ATOM   5329 C  CB  . TYR C  1 126 ? 50.984  11.225  -41.760 1.00 17.44 ? 126 TYR C CB  1 
ATOM   5330 C  CG  . TYR C  1 126 ? 50.071  11.261  -42.927 1.00 19.51 ? 126 TYR C CG  1 
ATOM   5331 C  CD1 . TYR C  1 126 ? 50.057  12.372  -43.809 1.00 21.49 ? 126 TYR C CD1 1 
ATOM   5332 C  CD2 . TYR C  1 126 ? 49.185  10.195  -43.180 1.00 19.73 ? 126 TYR C CD2 1 
ATOM   5333 C  CE1 . TYR C  1 126 ? 49.228  12.382  -44.902 1.00 22.60 ? 126 TYR C CE1 1 
ATOM   5334 C  CE2 . TYR C  1 126 ? 48.396  10.208  -44.299 1.00 20.20 ? 126 TYR C CE2 1 
ATOM   5335 C  CZ  . TYR C  1 126 ? 48.433  11.281  -45.148 1.00 21.65 ? 126 TYR C CZ  1 
ATOM   5336 O  OH  . TYR C  1 126 ? 47.564  11.298  -46.245 1.00 21.53 ? 126 TYR C OH  1 
ATOM   5337 N  N   . PRO C  1 127 ? 53.625  12.321  -40.263 1.00 18.88 ? 127 PRO C N   1 
ATOM   5338 C  CA  . PRO C  1 127 ? 54.575  12.261  -39.155 1.00 21.24 ? 127 PRO C CA  1 
ATOM   5339 C  C   . PRO C  1 127 ? 54.037  11.726  -37.843 1.00 22.62 ? 127 PRO C C   1 
ATOM   5340 O  O   . PRO C  1 127 ? 54.797  11.263  -36.959 1.00 23.02 ? 127 PRO C O   1 
ATOM   5341 C  CB  . PRO C  1 127 ? 54.903  13.750  -38.902 1.00 23.41 ? 127 PRO C CB  1 
ATOM   5342 C  CG  . PRO C  1 127 ? 53.887  14.548  -39.623 1.00 23.60 ? 127 PRO C CG  1 
ATOM   5343 C  CD  . PRO C  1 127 ? 53.248  13.689  -40.667 1.00 21.66 ? 127 PRO C CD  1 
ATOM   5344 N  N   . ASP C  1 128 ? 52.739  11.818  -37.671 1.00 20.64 ? 128 ASP C N   1 
ATOM   5345 C  CA  . ASP C  1 128 ? 52.155  11.405  -36.419 1.00 22.07 ? 128 ASP C CA  1 
ATOM   5346 C  C   . ASP C  1 128 ? 50.676  11.110  -36.638 1.00 19.50 ? 128 ASP C C   1 
ATOM   5347 O  O   . ASP C  1 128 ? 50.073  11.442  -37.709 1.00 18.93 ? 128 ASP C O   1 
ATOM   5348 C  CB  . ASP C  1 128 ? 52.374  12.486  -35.318 1.00 23.73 ? 128 ASP C CB  1 
ATOM   5349 C  CG  . ASP C  1 128 ? 51.934  13.900  -35.748 1.00 28.97 ? 128 ASP C CG  1 
ATOM   5350 O  OD1 . ASP C  1 128 ? 52.763  14.841  -35.668 1.00 36.30 ? 128 ASP C OD1 1 
ATOM   5351 O  OD2 . ASP C  1 128 ? 50.804  14.118  -36.213 1.00 29.72 ? 128 ASP C OD2 1 
ATOM   5352 N  N   . ALA C  1 129 ? 50.039  10.586  -35.596 1.00 20.29 ? 129 ALA C N   1 
ATOM   5353 C  CA  . ALA C  1 129 ? 48.694  10.114  -35.777 1.00 20.79 ? 129 ALA C CA  1 
ATOM   5354 C  C   . ALA C  1 129 ? 47.669  11.270  -35.849 1.00 23.69 ? 129 ALA C C   1 
ATOM   5355 O  O   . ALA C  1 129 ? 46.696  11.237  -36.613 1.00 22.37 ? 129 ALA C O   1 
ATOM   5356 C  CB  . ALA C  1 129 ? 48.359  9.205   -34.605 1.00 25.04 ? 129 ALA C CB  1 
ATOM   5357 N  N   . SER C  1 130 ? 47.956  12.317  -35.127 1.00 26.04 ? 130 SER C N   1 
ATOM   5358 C  CA  . SER C  1 130 ? 47.162  13.520  -35.202 1.00 28.51 ? 130 SER C CA  1 
ATOM   5359 C  C   . SER C  1 130 ? 47.124  14.093  -36.614 1.00 26.80 ? 130 SER C C   1 
ATOM   5360 O  O   . SER C  1 130 ? 46.072  14.370  -37.122 1.00 28.80 ? 130 SER C O   1 
ATOM   5361 C  CB  . SER C  1 130 ? 47.715  14.522  -34.180 1.00 31.03 ? 130 SER C CB  1 
ATOM   5362 O  OG  . SER C  1 130 ? 47.147  15.803  -34.424 1.00 43.54 ? 130 SER C OG  1 
ATOM   5363 N  N   . THR C  1 131 ? 48.292  14.275  -37.266 1.00 21.87 ? 131 THR C N   1 
ATOM   5364 C  CA  . THR C  1 131 ? 48.320  14.762  -38.652 1.00 21.11 ? 131 THR C CA  1 
ATOM   5365 C  C   . THR C  1 131 ? 47.598  13.792  -39.584 1.00 17.70 ? 131 THR C C   1 
ATOM   5366 O  O   . THR C  1 131 ? 46.975  14.202  -40.559 1.00 19.09 ? 131 THR C O   1 
ATOM   5367 C  CB  . THR C  1 131 ? 49.783  14.960  -39.115 1.00 22.42 ? 131 THR C CB  1 
ATOM   5368 O  OG1 . THR C  1 131 ? 50.424  15.845  -38.177 1.00 25.33 ? 131 THR C OG1 1 
ATOM   5369 C  CG2 . THR C  1 131 ? 49.860  15.532  -40.493 1.00 22.09 ? 131 THR C CG2 1 
ATOM   5370 N  N   . ALA C  1 132 ? 47.821  12.496  -39.326 1.00 18.87 ? 132 ALA C N   1 
ATOM   5371 C  CA  . ALA C  1 132 ? 47.306  11.439  -40.240 1.00 19.87 ? 132 ALA C CA  1 
ATOM   5372 C  C   . ALA C  1 132 ? 45.762  11.343  -40.145 1.00 17.31 ? 132 ALA C C   1 
ATOM   5373 O  O   . ALA C  1 132 ? 45.157  11.019  -41.156 1.00 16.76 ? 132 ALA C O   1 
ATOM   5374 C  CB  . ALA C  1 132 ? 47.891  10.113  -39.869 1.00 16.17 ? 132 ALA C CB  1 
ATOM   5375 N  N   . SER C  1 133 ? 45.164  11.725  -38.994 1.00 17.52 ? 133 SER C N   1 
ATOM   5376 C  CA  . SER C  1 133 ? 43.789  11.245  -38.728 1.00 20.35 ? 133 SER C CA  1 
ATOM   5377 C  C   . SER C  1 133 ? 42.782  11.818  -39.680 1.00 21.32 ? 133 SER C C   1 
ATOM   5378 O  O   . SER C  1 133 ? 41.772  11.160  -39.994 1.00 19.79 ? 133 SER C O   1 
ATOM   5379 C  CB  . SER C  1 133 ? 43.476  11.459  -37.216 1.00 21.36 ? 133 SER C CB  1 
ATOM   5380 O  OG  . SER C  1 133 ? 43.517  12.876  -36.975 1.00 26.10 ? 133 SER C OG  1 
ATOM   5381 N  N   . ASN C  1 134 ? 42.976  13.009  -40.206 1.00 20.02 ? 134 ASN C N   1 
ATOM   5382 C  CA  . ASN C  1 134 ? 42.021  13.571  -41.155 1.00 21.88 ? 134 ASN C CA  1 
ATOM   5383 C  C   . ASN C  1 134 ? 42.492  13.514  -42.563 1.00 18.58 ? 134 ASN C C   1 
ATOM   5384 O  O   . ASN C  1 134 ? 42.013  14.241  -43.432 1.00 24.24 ? 134 ASN C O   1 
ATOM   5385 C  CB  . ASN C  1 134 ? 41.654  15.007  -40.769 1.00 22.54 ? 134 ASN C CB  1 
ATOM   5386 C  CG  . ASN C  1 134 ? 42.867  15.933  -40.693 1.00 27.80 ? 134 ASN C CG  1 
ATOM   5387 O  OD1 . ASN C  1 134 ? 44.014  15.517  -40.796 1.00 26.85 ? 134 ASN C OD1 1 
ATOM   5388 N  ND2 . ASN C  1 134 ? 42.587  17.220  -40.532 1.00 30.13 ? 134 ASN C ND2 1 
ATOM   5389 N  N   . LYS C  1 135 ? 43.457  12.650  -42.894 1.00 19.18 ? 135 LYS C N   1 
ATOM   5390 C  CA  . LYS C  1 135 ? 44.015  12.647  -44.202 1.00 20.15 ? 135 LYS C CA  1 
ATOM   5391 C  C   . LYS C  1 135 ? 43.904  11.346  -44.881 1.00 17.94 ? 135 LYS C C   1 
ATOM   5392 O  O   . LYS C  1 135 ? 43.720  10.256  -44.232 1.00 18.06 ? 135 LYS C O   1 
ATOM   5393 C  CB  . LYS C  1 135 ? 45.548  13.018  -44.127 1.00 22.59 ? 135 LYS C CB  1 
ATOM   5394 C  CG  . LYS C  1 135 ? 45.743  14.391  -43.517 1.00 24.30 ? 135 LYS C CG  1 
ATOM   5395 C  CD  . LYS C  1 135 ? 47.185  14.869  -43.538 1.00 24.55 ? 135 LYS C CD  1 
ATOM   5396 C  CE  . LYS C  1 135 ? 47.168  16.345  -43.193 1.00 23.81 ? 135 LYS C CE  1 
ATOM   5397 N  NZ  . LYS C  1 135 ? 46.508  16.699  -41.854 1.00 26.35 ? 135 LYS C NZ  1 
ATOM   5398 N  N   . SER C  1 136 ? 44.059  11.367  -46.198 1.00 19.58 ? 136 SER C N   1 
ATOM   5399 C  CA  . SER C  1 136 ? 43.857  10.234  -47.024 1.00 19.08 ? 136 SER C CA  1 
ATOM   5400 C  C   . SER C  1 136 ? 44.722  9.049   -46.569 1.00 18.87 ? 136 SER C C   1 
ATOM   5401 O  O   . SER C  1 136 ? 45.930  9.198   -46.305 1.00 21.55 ? 136 SER C O   1 
ATOM   5402 C  CB  . SER C  1 136 ? 44.215  10.605  -48.443 1.00 24.80 ? 136 SER C CB  1 
ATOM   5403 O  OG  . SER C  1 136 ? 44.008  9.482   -49.247 1.00 31.23 ? 136 SER C OG  1 
ATOM   5404 N  N   . GLU C  1 137 ? 44.103  7.873   -46.459 1.00 17.67 ? 137 GLU C N   1 
ATOM   5405 C  CA  . GLU C  1 137 ? 44.804  6.663   -46.050 1.00 17.77 ? 137 GLU C CA  1 
ATOM   5406 C  C   . GLU C  1 137 ? 45.524  6.841   -44.765 1.00 17.54 ? 137 GLU C C   1 
ATOM   5407 O  O   . GLU C  1 137 ? 46.547  6.170   -44.501 1.00 17.85 ? 137 GLU C O   1 
ATOM   5408 C  CB  . GLU C  1 137 ? 45.764  6.132   -47.109 1.00 19.59 ? 137 GLU C CB  1 
ATOM   5409 C  CG  . GLU C  1 137 ? 45.035  5.822   -48.409 1.00 26.96 ? 137 GLU C CG  1 
ATOM   5410 C  CD  . GLU C  1 137 ? 45.986  5.373   -49.550 1.00 32.98 ? 137 GLU C CD  1 
ATOM   5411 O  OE1 . GLU C  1 137 ? 45.508  4.689   -50.483 1.00 36.74 ? 137 GLU C OE1 1 
ATOM   5412 O  OE2 . GLU C  1 137 ? 47.211  5.684   -49.506 1.00 38.90 ? 137 GLU C OE2 1 
ATOM   5413 N  N   . GLY C  1 138 ? 44.948  7.602   -43.845 1.00 15.34 ? 138 GLY C N   1 
ATOM   5414 C  CA  . GLY C  1 138 ? 45.678  8.067   -42.679 1.00 16.27 ? 138 GLY C CA  1 
ATOM   5415 C  C   . GLY C  1 138 ? 45.824  6.972   -41.634 1.00 14.09 ? 138 GLY C C   1 
ATOM   5416 O  O   . GLY C  1 138 ? 46.798  6.955   -40.846 1.00 15.44 ? 138 GLY C O   1 
ATOM   5417 N  N   . LEU C  1 139 ? 44.784  6.086   -41.479 1.00 11.90 ? 139 LEU C N   1 
ATOM   5418 C  CA  . LEU C  1 139 ? 44.653  5.259   -40.275 1.00 11.36 ? 139 LEU C CA  1 
ATOM   5419 C  C   . LEU C  1 139 ? 44.345  3.821   -40.643 1.00 11.10 ? 139 LEU C C   1 
ATOM   5420 O  O   . LEU C  1 139 ? 43.693  3.577   -41.652 1.00 12.05 ? 139 LEU C O   1 
ATOM   5421 C  CB  . LEU C  1 139 ? 43.624  5.753   -39.210 1.00 11.95 ? 139 LEU C CB  1 
ATOM   5422 C  CG  . LEU C  1 139 ? 43.813  7.153   -38.745 1.00 12.49 ? 139 LEU C CG  1 
ATOM   5423 C  CD1 . LEU C  1 139 ? 42.546  7.672   -38.041 1.00 16.50 ? 139 LEU C CD1 1 
ATOM   5424 C  CD2 . LEU C  1 139 ? 45.047  7.322   -37.907 1.00 15.25 ? 139 LEU C CD2 1 
ATOM   5425 N  N   . ALA C  1 140 ? 44.748  2.910   -39.771 1.00 10.26 ? 140 ALA C N   1 
ATOM   5426 C  CA  . ALA C  1 140 ? 44.398  1.478   -39.861 1.00 10.79 ? 140 ALA C CA  1 
ATOM   5427 C  C   . ALA C  1 140 ? 44.090  1.040   -38.471 1.00 11.52 ? 140 ALA C C   1 
ATOM   5428 O  O   . ALA C  1 140 ? 44.898  1.222   -37.568 1.00 11.72 ? 140 ALA C O   1 
ATOM   5429 C  CB  . ALA C  1 140 ? 45.529  0.648   -40.462 1.00 12.43 ? 140 ALA C CB  1 
ATOM   5430 N  N   . VAL C  1 141 ? 42.946  0.420   -38.196 1.00 10.23 ? 141 VAL C N   1 
ATOM   5431 C  CA  . VAL C  1 141 ? 42.591  -0.011  -36.822 1.00 11.21 ? 141 VAL C CA  1 
ATOM   5432 C  C   . VAL C  1 141 ? 42.429  -1.506  -36.903 1.00 9.41  ? 141 VAL C C   1 
ATOM   5433 O  O   . VAL C  1 141 ? 41.745  -2.034  -37.827 1.00 10.81 ? 141 VAL C O   1 
ATOM   5434 C  CB  . VAL C  1 141 ? 41.324  0.712   -36.303 1.00 9.80  ? 141 VAL C CB  1 
ATOM   5435 C  CG1 . VAL C  1 141 ? 40.991  0.258   -34.875 1.00 12.86 ? 141 VAL C CG1 1 
ATOM   5436 C  CG2 . VAL C  1 141 ? 41.533  2.190   -36.227 1.00 11.46 ? 141 VAL C CG2 1 
ATOM   5437 N  N   . LEU C  1 142 ? 42.949  -2.223  -35.880 1.00 10.11 ? 142 LEU C N   1 
ATOM   5438 C  CA  . LEU C  1 142 ? 42.730  -3.597  -35.730 1.00 10.41 ? 142 LEU C CA  1 
ATOM   5439 C  C   . LEU C  1 142 ? 41.628  -3.760  -34.655 1.00 10.33 ? 142 LEU C C   1 
ATOM   5440 O  O   . LEU C  1 142 ? 41.801  -3.106  -33.560 1.00 11.59 ? 142 LEU C O   1 
ATOM   5441 C  CB  . LEU C  1 142 ? 43.983  -4.351  -35.184 1.00 11.60 ? 142 LEU C CB  1 
ATOM   5442 C  CG  . LEU C  1 142 ? 45.230  -4.253  -36.040 1.00 11.25 ? 142 LEU C CG  1 
ATOM   5443 C  CD1 . LEU C  1 142 ? 46.298  -5.081  -35.355 1.00 13.60 ? 142 LEU C CD1 1 
ATOM   5444 C  CD2 . LEU C  1 142 ? 44.935  -4.785  -37.437 1.00 12.57 ? 142 LEU C CD2 1 
ATOM   5445 N  N   . ALA C  1 143 ? 40.591  -4.535  -34.891 1.00 10.11 ? 143 ALA C N   1 
ATOM   5446 C  CA  . ALA C  1 143 ? 39.477  -4.669  -33.917 1.00 9.98  ? 143 ALA C CA  1 
ATOM   5447 C  C   . ALA C  1 143 ? 39.379  -6.134  -33.522 1.00 9.90  ? 143 ALA C C   1 
ATOM   5448 O  O   . ALA C  1 143 ? 39.353  -7.052  -34.330 1.00 11.00 ? 143 ALA C O   1 
ATOM   5449 C  CB  . ALA C  1 143 ? 38.155  -4.227  -34.535 1.00 11.20 ? 143 ALA C CB  1 
ATOM   5450 N  N   . VAL C  1 144 ? 39.324  -6.289  -32.189 1.00 11.38 ? 144 VAL C N   1 
ATOM   5451 C  CA  . VAL C  1 144 ? 39.137  -7.619  -31.593 1.00 11.70 ? 144 VAL C CA  1 
ATOM   5452 C  C   . VAL C  1 144 ? 37.824  -7.678  -30.818 1.00 11.38 ? 144 VAL C C   1 
ATOM   5453 O  O   . VAL C  1 144 ? 37.552  -6.845  -29.944 1.00 12.20 ? 144 VAL C O   1 
ATOM   5454 C  CB  . VAL C  1 144 ? 40.281  -7.936  -30.583 1.00 11.87 ? 144 VAL C CB  1 
ATOM   5455 C  CG1 . VAL C  1 144 ? 40.140  -9.358  -30.053 1.00 14.73 ? 144 VAL C CG1 1 
ATOM   5456 C  CG2 . VAL C  1 144 ? 41.653  -7.830  -31.286 1.00 13.13 ? 144 VAL C CG2 1 
ATOM   5457 N  N   . LEU C  1 145 ? 37.006  -8.634  -31.203 1.00 11.98 ? 145 LEU C N   1 
ATOM   5458 C  CA  . LEU C  1 145 ? 35.708  -8.838  -30.548 1.00 13.50 ? 145 LEU C CA  1 
ATOM   5459 C  C   . LEU C  1 145 ? 35.984  -9.574  -29.214 1.00 14.83 ? 145 LEU C C   1 
ATOM   5460 O  O   . LEU C  1 145 ? 36.767  -10.546 -29.227 1.00 16.10 ? 145 LEU C O   1 
ATOM   5461 C  CB  . LEU C  1 145 ? 34.747  -9.587  -31.456 1.00 13.10 ? 145 LEU C CB  1 
ATOM   5462 C  CG  . LEU C  1 145 ? 34.456  -8.826  -32.754 1.00 14.48 ? 145 LEU C CG  1 
ATOM   5463 C  CD1 . LEU C  1 145 ? 33.897  -9.769  -33.819 1.00 15.14 ? 145 LEU C CD1 1 
ATOM   5464 C  CD2 . LEU C  1 145 ? 33.486  -7.673  -32.486 1.00 15.69 ? 145 LEU C CD2 1 
ATOM   5465 N  N   . ILE C  1 146 ? 35.268  -9.185  -28.182 1.00 12.02 ? 146 ILE C N   1 
ATOM   5466 C  CA  . ILE C  1 146 ? 35.524  -9.772  -26.787 1.00 13.78 ? 146 ILE C CA  1 
ATOM   5467 C  C   . ILE C  1 146 ? 34.231  -10.436 -26.336 1.00 16.27 ? 146 ILE C C   1 
ATOM   5468 O  O   . ILE C  1 146 ? 33.187  -9.780  -26.325 1.00 15.19 ? 146 ILE C O   1 
ATOM   5469 C  CB  . ILE C  1 146 ? 35.997  -8.681  -25.828 1.00 14.10 ? 146 ILE C CB  1 
ATOM   5470 C  CG1 . ILE C  1 146 ? 37.356  -8.077  -26.265 1.00 13.69 ? 146 ILE C CG1 1 
ATOM   5471 C  CG2 . ILE C  1 146 ? 36.194  -9.333  -24.414 1.00 14.74 ? 146 ILE C CG2 1 
ATOM   5472 C  CD1 . ILE C  1 146 ? 37.750  -6.846  -25.513 1.00 14.46 ? 146 ILE C CD1 1 
ATOM   5473 N  N   . GLU C  1 147 ? 34.270  -11.724 -25.958 1.00 19.64 ? 147 GLU C N   1 
ATOM   5474 C  CA  . GLU C  1 147 ? 33.122  -12.368 -25.269 1.00 20.29 ? 147 GLU C CA  1 
ATOM   5475 C  C   . GLU C  1 147 ? 33.524  -12.937 -23.916 1.00 21.77 ? 147 GLU C C   1 
ATOM   5476 O  O   . GLU C  1 147 ? 34.692  -13.002 -23.571 1.00 20.72 ? 147 GLU C O   1 
ATOM   5477 C  CB  . GLU C  1 147 ? 32.615  -13.473 -26.138 1.00 18.56 ? 147 GLU C CB  1 
ATOM   5478 C  CG  . GLU C  1 147 ? 33.634  -14.593 -26.356 1.00 22.48 ? 147 GLU C CG  1 
ATOM   5479 C  CD  . GLU C  1 147 ? 33.156  -15.645 -27.357 1.00 24.73 ? 147 GLU C CD  1 
ATOM   5480 O  OE1 . GLU C  1 147 ? 32.144  -15.487 -28.087 1.00 24.11 ? 147 GLU C OE1 1 
ATOM   5481 O  OE2 . GLU C  1 147 ? 33.817  -16.704 -27.472 1.00 29.90 ? 147 GLU C OE2 1 
ATOM   5482 N  N   . MET C  1 148 ? 32.528  -13.323 -23.168 1.00 25.87 ? 148 MET C N   1 
ATOM   5483 C  CA  . MET C  1 148 ? 32.795  -13.859 -21.842 1.00 25.75 ? 148 MET C CA  1 
ATOM   5484 C  C   . MET C  1 148 ? 33.193  -15.251 -21.932 1.00 24.15 ? 148 MET C C   1 
ATOM   5485 O  O   . MET C  1 148 ? 32.622  -16.022 -22.703 1.00 25.88 ? 148 MET C O   1 
ATOM   5486 C  CB  . MET C  1 148 ? 31.534  -13.704 -21.039 1.00 29.93 ? 148 MET C CB  1 
ATOM   5487 C  CG  . MET C  1 148 ? 31.427  -12.499 -20.153 1.00 30.42 ? 148 MET C CG  1 
ATOM   5488 S  SD  . MET C  1 148 ? 30.633  -13.157 -18.671 1.00 67.44 ? 148 MET C SD  1 
ATOM   5489 C  CE  . MET C  1 148 ? 29.760  -11.729 -18.045 1.00 39.83 ? 148 MET C CE  1 
ATOM   5490 N  N   . GLY C  1 149 ? 34.193  -15.628 -21.113 1.00 27.62 ? 149 GLY C N   1 
ATOM   5491 C  CA  . GLY C  1 149 ? 34.549  -17.058 -20.973 1.00 27.76 ? 149 GLY C CA  1 
ATOM   5492 C  C   . GLY C  1 149 ? 35.672  -17.149 -19.929 1.00 25.28 ? 149 GLY C C   1 
ATOM   5493 O  O   . GLY C  1 149 ? 35.571  -16.605 -18.816 1.00 26.07 ? 149 GLY C O   1 
ATOM   5494 N  N   . SER C  1 150 ? 36.793  -17.745 -20.337 1.00 28.90 ? 150 SER C N   1 
ATOM   5495 C  CA  . SER C  1 150 ? 37.998  -17.937 -19.477 1.00 28.41 ? 150 SER C CA  1 
ATOM   5496 C  C   . SER C  1 150 ? 38.664  -16.637 -19.055 1.00 29.95 ? 150 SER C C   1 
ATOM   5497 O  O   . SER C  1 150 ? 38.747  -15.708 -19.875 1.00 25.45 ? 150 SER C O   1 
ATOM   5498 C  CB  . SER C  1 150 ? 39.072  -18.704 -20.263 1.00 32.54 ? 150 SER C CB  1 
ATOM   5499 O  OG  . SER C  1 150 ? 38.695  -20.046 -20.462 1.00 35.33 ? 150 SER C OG  1 
ATOM   5500 N  N   . PHE C  1 151 ? 39.200  -16.580 -17.837 1.00 24.00 ? 151 PHE C N   1 
ATOM   5501 C  CA  . PHE C  1 151 ? 40.039  -15.456 -17.388 1.00 24.75 ? 151 PHE C CA  1 
ATOM   5502 C  C   . PHE C  1 151 ? 41.168  -15.285 -18.386 1.00 25.14 ? 151 PHE C C   1 
ATOM   5503 O  O   . PHE C  1 151 ? 41.779  -16.292 -18.778 1.00 27.30 ? 151 PHE C O   1 
ATOM   5504 C  CB  . PHE C  1 151 ? 40.648  -15.736 -15.961 1.00 25.43 ? 151 PHE C CB  1 
ATOM   5505 C  CG  . PHE C  1 151 ? 41.640  -14.692 -15.479 1.00 24.60 ? 151 PHE C CG  1 
ATOM   5506 C  CD1 . PHE C  1 151 ? 41.219  -13.422 -15.007 1.00 25.93 ? 151 PHE C CD1 1 
ATOM   5507 C  CD2 . PHE C  1 151 ? 43.011  -14.957 -15.485 1.00 24.68 ? 151 PHE C CD2 1 
ATOM   5508 C  CE1 . PHE C  1 151 ? 42.138  -12.442 -14.552 1.00 23.92 ? 151 PHE C CE1 1 
ATOM   5509 C  CE2 . PHE C  1 151 ? 43.914  -13.996 -15.044 1.00 22.19 ? 151 PHE C CE2 1 
ATOM   5510 C  CZ  . PHE C  1 151 ? 43.484  -12.727 -14.571 1.00 23.51 ? 151 PHE C CZ  1 
ATOM   5511 N  N   . ASN C  1 152 ? 41.497  -14.035 -18.716 1.00 26.41 ? 152 ASN C N   1 
ATOM   5512 C  CA  . ASN C  1 152 ? 42.578  -13.774 -19.667 1.00 21.28 ? 152 ASN C CA  1 
ATOM   5513 C  C   . ASN C  1 152 ? 43.705  -12.940 -19.010 1.00 21.30 ? 152 ASN C C   1 
ATOM   5514 O  O   . ASN C  1 152 ? 43.560  -11.716 -18.642 1.00 22.67 ? 152 ASN C O   1 
ATOM   5515 C  CB  . ASN C  1 152 ? 41.924  -13.037 -20.897 1.00 23.01 ? 152 ASN C CB  1 
ATOM   5516 C  CG  . ASN C  1 152 ? 42.862  -12.873 -22.036 1.00 21.37 ? 152 ASN C CG  1 
ATOM   5517 O  OD1 . ASN C  1 152 ? 44.003  -12.408 -21.859 1.00 21.49 ? 152 ASN C OD1 1 
ATOM   5518 N  ND2 . ASN C  1 152 ? 42.370  -13.153 -23.267 1.00 23.53 ? 152 ASN C ND2 1 
ATOM   5519 N  N   . PRO C  1 153 ? 44.867  -13.594 -18.728 1.00 21.32 ? 153 PRO C N   1 
ATOM   5520 C  CA  . PRO C  1 153 ? 45.970  -12.965 -18.076 1.00 23.95 ? 153 PRO C CA  1 
ATOM   5521 C  C   . PRO C  1 153 ? 46.498  -11.754 -18.833 1.00 23.14 ? 153 PRO C C   1 
ATOM   5522 O  O   . PRO C  1 153 ? 46.950  -10.798 -18.206 1.00 25.31 ? 153 PRO C O   1 
ATOM   5523 C  CB  . PRO C  1 153 ? 47.013  -14.129 -17.944 1.00 23.62 ? 153 PRO C CB  1 
ATOM   5524 C  CG  . PRO C  1 153 ? 46.229  -15.365 -18.138 1.00 25.70 ? 153 PRO C CG  1 
ATOM   5525 C  CD  . PRO C  1 153 ? 45.072  -15.033 -19.056 1.00 23.31 ? 153 PRO C CD  1 
ATOM   5526 N  N   . SER C  1 154 ? 46.405  -11.780 -20.189 1.00 22.63 ? 154 SER C N   1 
ATOM   5527 C  CA  . SER C  1 154 ? 46.993  -10.736 -21.028 1.00 20.48 ? 154 SER C CA  1 
ATOM   5528 C  C   . SER C  1 154 ? 46.130  -9.457  -20.906 1.00 16.92 ? 154 SER C C   1 
ATOM   5529 O  O   . SER C  1 154 ? 46.683  -8.337  -20.728 1.00 19.56 ? 154 SER C O   1 
ATOM   5530 C  CB  . SER C  1 154 ? 47.157  -11.245 -22.440 1.00 23.77 ? 154 SER C CB  1 
ATOM   5531 O  OG  . SER C  1 154 ? 48.030  -12.411 -22.387 1.00 23.91 ? 154 SER C OG  1 
ATOM   5532 N  N   . TYR C  1 155 ? 44.779  -9.662  -20.964 1.00 21.23 ? 155 TYR C N   1 
ATOM   5533 C  CA  . TYR C  1 155 ? 43.869  -8.520  -20.767 1.00 22.65 ? 155 TYR C CA  1 
ATOM   5534 C  C   . TYR C  1 155 ? 43.997  -7.926  -19.399 1.00 20.62 ? 155 TYR C C   1 
ATOM   5535 O  O   . TYR C  1 155 ? 43.887  -6.682  -19.192 1.00 21.19 ? 155 TYR C O   1 
ATOM   5536 C  CB  . TYR C  1 155 ? 42.380  -8.777  -21.172 1.00 20.72 ? 155 TYR C CB  1 
ATOM   5537 C  CG  . TYR C  1 155 ? 42.194  -8.660  -22.690 1.00 18.55 ? 155 TYR C CG  1 
ATOM   5538 C  CD1 . TYR C  1 155 ? 41.659  -7.477  -23.245 1.00 17.93 ? 155 TYR C CD1 1 
ATOM   5539 C  CD2 . TYR C  1 155 ? 42.544  -9.727  -23.537 1.00 18.15 ? 155 TYR C CD2 1 
ATOM   5540 C  CE1 . TYR C  1 155 ? 41.479  -7.375  -24.638 1.00 18.28 ? 155 TYR C CE1 1 
ATOM   5541 C  CE2 . TYR C  1 155 ? 42.461  -9.615  -24.955 1.00 17.58 ? 155 TYR C CE2 1 
ATOM   5542 C  CZ  . TYR C  1 155 ? 41.862  -8.435  -25.479 1.00 17.61 ? 155 TYR C CZ  1 
ATOM   5543 O  OH  . TYR C  1 155 ? 41.761  -8.262  -26.862 1.00 16.58 ? 155 TYR C OH  1 
ATOM   5544 N  N   . ASP C  1 156 ? 44.362  -8.766  -18.428 1.00 22.13 ? 156 ASP C N   1 
ATOM   5545 C  CA  . ASP C  1 156 ? 44.521  -8.263  -17.050 1.00 24.95 ? 156 ASP C CA  1 
ATOM   5546 C  C   . ASP C  1 156 ? 45.751  -7.368  -16.869 1.00 22.98 ? 156 ASP C C   1 
ATOM   5547 O  O   . ASP C  1 156 ? 45.809  -6.554  -15.918 1.00 25.12 ? 156 ASP C O   1 
ATOM   5548 C  CB  . ASP C  1 156 ? 44.477  -9.411  -16.051 1.00 26.44 ? 156 ASP C CB  1 
ATOM   5549 C  CG  . ASP C  1 156 ? 43.504  -9.126  -14.940 1.00 30.58 ? 156 ASP C CG  1 
ATOM   5550 O  OD1 . ASP C  1 156 ? 42.279  -8.785  -15.210 1.00 26.24 ? 156 ASP C OD1 1 
ATOM   5551 O  OD2 . ASP C  1 156 ? 43.983  -9.181  -13.766 1.00 35.54 ? 156 ASP C OD2 1 
ATOM   5552 N  N   . LYS C  1 157 ? 46.652  -7.363  -17.874 1.00 21.99 ? 157 LYS C N   1 
ATOM   5553 C  CA  . LYS C  1 157 ? 47.804  -6.458  -17.829 1.00 22.86 ? 157 LYS C CA  1 
ATOM   5554 C  C   . LYS C  1 157 ? 47.338  -5.022  -17.981 1.00 24.33 ? 157 LYS C C   1 
ATOM   5555 O  O   . LYS C  1 157 ? 48.023  -4.075  -17.499 1.00 28.52 ? 157 LYS C O   1 
ATOM   5556 C  CB  . LYS C  1 157 ? 48.879  -6.914  -18.808 1.00 27.74 ? 157 LYS C CB  1 
ATOM   5557 C  CG  . LYS C  1 157 ? 49.286  -8.355  -18.438 1.00 28.26 ? 157 LYS C CG  1 
ATOM   5558 C  CD  . LYS C  1 157 ? 50.511  -8.873  -19.151 1.00 32.38 ? 157 LYS C CD  1 
ATOM   5559 C  CE  . LYS C  1 157 ? 50.526  -10.402 -19.075 1.00 34.08 ? 157 LYS C CE  1 
ATOM   5560 N  NZ  . LYS C  1 157 ? 51.503  -11.029 -20.024 1.00 34.13 ? 157 LYS C NZ  1 
ATOM   5561 N  N   . ILE C  1 158 ? 46.148  -4.878  -18.609 1.00 21.21 ? 158 ILE C N   1 
ATOM   5562 C  CA  . ILE C  1 158 ? 45.483  -3.572  -18.597 1.00 22.47 ? 158 ILE C CA  1 
ATOM   5563 C  C   . ILE C  1 158 ? 44.550  -3.417  -17.412 1.00 19.39 ? 158 ILE C C   1 
ATOM   5564 O  O   . ILE C  1 158 ? 44.583  -2.329  -16.699 1.00 19.74 ? 158 ILE C O   1 
ATOM   5565 C  CB  . ILE C  1 158 ? 44.738  -3.379  -19.957 1.00 18.89 ? 158 ILE C CB  1 
ATOM   5566 C  CG1 . ILE C  1 158 ? 45.831  -3.242  -20.984 1.00 22.82 ? 158 ILE C CG1 1 
ATOM   5567 C  CG2 . ILE C  1 158 ? 43.939  -2.064  -19.963 1.00 19.67 ? 158 ILE C CG2 1 
ATOM   5568 C  CD1 . ILE C  1 158 ? 45.386  -3.499  -22.410 1.00 26.48 ? 158 ILE C CD1 1 
ATOM   5569 N  N   . PHE C  1 159 ? 43.666  -4.394  -17.268 1.00 21.86 ? 159 PHE C N   1 
ATOM   5570 C  CA  . PHE C  1 159 ? 42.540  -4.201  -16.373 1.00 21.10 ? 159 PHE C CA  1 
ATOM   5571 C  C   . PHE C  1 159 ? 42.962  -3.990  -14.920 1.00 21.77 ? 159 PHE C C   1 
ATOM   5572 O  O   . PHE C  1 159 ? 42.210  -3.384  -14.132 1.00 22.57 ? 159 PHE C O   1 
ATOM   5573 C  CB  . PHE C  1 159 ? 41.509  -5.334  -16.460 1.00 19.58 ? 159 PHE C CB  1 
ATOM   5574 C  CG  . PHE C  1 159 ? 40.853  -5.542  -17.826 1.00 20.47 ? 159 PHE C CG  1 
ATOM   5575 C  CD1 . PHE C  1 159 ? 40.701  -4.526  -18.765 1.00 22.88 ? 159 PHE C CD1 1 
ATOM   5576 C  CD2 . PHE C  1 159 ? 40.374  -6.795  -18.143 1.00 20.45 ? 159 PHE C CD2 1 
ATOM   5577 C  CE1 . PHE C  1 159 ? 40.086  -4.778  -19.991 1.00 21.10 ? 159 PHE C CE1 1 
ATOM   5578 C  CE2 . PHE C  1 159 ? 39.768  -7.055  -19.350 1.00 25.51 ? 159 PHE C CE2 1 
ATOM   5579 C  CZ  . PHE C  1 159 ? 39.618  -6.046  -20.280 1.00 19.42 ? 159 PHE C CZ  1 
ATOM   5580 N  N   . SER C  1 160 ? 44.146  -4.518  -14.604 1.00 21.37 ? 160 SER C N   1 
ATOM   5581 C  CA  . SER C  1 160 ? 44.673  -4.464  -13.221 1.00 21.70 ? 160 SER C CA  1 
ATOM   5582 C  C   . SER C  1 160 ? 45.116  -3.073  -12.815 1.00 25.29 ? 160 SER C C   1 
ATOM   5583 O  O   . SER C  1 160 ? 45.414  -2.848  -11.627 1.00 25.65 ? 160 SER C O   1 
ATOM   5584 C  CB  . SER C  1 160 ? 45.801  -5.487  -13.060 1.00 25.60 ? 160 SER C CB  1 
ATOM   5585 O  OG  . SER C  1 160 ? 46.969  -5.169  -13.839 1.00 23.91 ? 160 SER C OG  1 
ATOM   5586 N  N   . HIS C  1 161 ? 45.074  -2.116  -13.733 1.00 19.24 ? 161 HIS C N   1 
ATOM   5587 C  CA  . HIS C  1 161 ? 45.374  -0.694  -13.519 1.00 21.39 ? 161 HIS C CA  1 
ATOM   5588 C  C   . HIS C  1 161 ? 44.227  0.223   -13.517 1.00 16.30 ? 161 HIS C C   1 
ATOM   5589 O  O   . HIS C  1 161 ? 44.400  1.438   -13.333 1.00 20.01 ? 161 HIS C O   1 
ATOM   5590 C  CB  . HIS C  1 161 ? 46.498  -0.230  -14.478 1.00 25.14 ? 161 HIS C CB  1 
ATOM   5591 C  CG  . HIS C  1 161 ? 47.761  -1.014  -14.259 1.00 28.09 ? 161 HIS C CG  1 
ATOM   5592 N  ND1 . HIS C  1 161 ? 48.789  -0.559  -13.452 1.00 33.57 ? 161 HIS C ND1 1 
ATOM   5593 C  CD2 . HIS C  1 161 ? 48.074  -2.334  -14.596 1.00 27.68 ? 161 HIS C CD2 1 
ATOM   5594 C  CE1 . HIS C  1 161 ? 49.732  -1.540  -13.355 1.00 31.59 ? 161 HIS C CE1 1 
ATOM   5595 N  NE2 . HIS C  1 161 ? 49.277  -2.633  -14.011 1.00 31.08 ? 161 HIS C NE2 1 
ATOM   5596 N  N   . LEU C  1 162 ? 43.000  -0.327  -13.804 1.00 17.73 ? 162 LEU C N   1 
ATOM   5597 C  CA  . LEU C  1 162 ? 41.849  0.552   -13.993 1.00 17.85 ? 162 LEU C CA  1 
ATOM   5598 C  C   . LEU C  1 162 ? 41.520  1.415   -12.794 1.00 16.20 ? 162 LEU C C   1 
ATOM   5599 O  O   . LEU C  1 162 ? 41.143  2.592   -12.986 1.00 16.35 ? 162 LEU C O   1 
ATOM   5600 C  CB  . LEU C  1 162 ? 40.582  -0.221  -14.413 1.00 18.74 ? 162 LEU C CB  1 
ATOM   5601 C  CG  . LEU C  1 162 ? 40.735  -0.949  -15.734 1.00 23.02 ? 162 LEU C CG  1 
ATOM   5602 C  CD1 . LEU C  1 162 ? 39.527  -1.842  -15.895 1.00 25.12 ? 162 LEU C CD1 1 
ATOM   5603 C  CD2 . LEU C  1 162 ? 41.004  0.017   -16.880 1.00 27.47 ? 162 LEU C CD2 1 
ATOM   5604 N  N   . GLN C  1 163 ? 41.791  0.885   -11.570 1.00 16.74 ? 163 GLN C N   1 
ATOM   5605 C  CA  . GLN C  1 163 ? 41.411  1.683   -10.407 1.00 17.72 ? 163 GLN C CA  1 
ATOM   5606 C  C   . GLN C  1 163 ? 42.362  2.916   -10.190 1.00 16.58 ? 163 GLN C C   1 
ATOM   5607 O  O   . GLN C  1 163 ? 42.095  3.769   -9.319  1.00 20.85 ? 163 GLN C O   1 
ATOM   5608 C  CB  . GLN C  1 163 ? 41.366  0.840   -9.111  1.00 18.07 ? 163 GLN C CB  1 
ATOM   5609 C  CG  . GLN C  1 163 ? 40.382  -0.350  -9.074  1.00 21.85 ? 163 GLN C CG  1 
ATOM   5610 C  CD  . GLN C  1 163 ? 38.936  0.105   -9.222  1.00 24.15 ? 163 GLN C CD  1 
ATOM   5611 O  OE1 . GLN C  1 163 ? 38.493  1.122   -8.674  1.00 23.64 ? 163 GLN C OE1 1 
ATOM   5612 N  NE2 . GLN C  1 163 ? 38.175  -0.651  -10.050 1.00 24.41 ? 163 GLN C NE2 1 
ATOM   5613 N  N   . HIS C  1 164 ? 43.430  3.067   -10.975 1.00 17.15 ? 164 HIS C N   1 
ATOM   5614 C  CA  . HIS C  1 164 ? 44.326  4.208   -10.878 1.00 19.52 ? 164 HIS C CA  1 
ATOM   5615 C  C   . HIS C  1 164 ? 43.951  5.287   -11.818 1.00 21.16 ? 164 HIS C C   1 
ATOM   5616 O  O   . HIS C  1 164 ? 44.463  6.419   -11.739 1.00 20.49 ? 164 HIS C O   1 
ATOM   5617 C  CB  . HIS C  1 164 ? 45.762  3.782   -11.171 1.00 21.15 ? 164 HIS C CB  1 
ATOM   5618 C  CG  . HIS C  1 164 ? 46.262  2.742   -10.240 1.00 16.93 ? 164 HIS C CG  1 
ATOM   5619 N  ND1 . HIS C  1 164 ? 46.277  2.912   -8.886  1.00 21.89 ? 164 HIS C ND1 1 
ATOM   5620 C  CD2 . HIS C  1 164 ? 46.696  1.433   -10.461 1.00 17.35 ? 164 HIS C CD2 1 
ATOM   5621 C  CE1 . HIS C  1 164 ? 46.706  1.761   -8.296  1.00 18.42 ? 164 HIS C CE1 1 
ATOM   5622 N  NE2 . HIS C  1 164 ? 46.900  0.848   -9.230  1.00 18.63 ? 164 HIS C NE2 1 
ATOM   5623 N  N   . VAL C  1 165 ? 43.003  4.986   -12.726 1.00 20.34 ? 165 VAL C N   1 
ATOM   5624 C  CA  . VAL C  1 165 ? 42.550  6.000   -13.673 1.00 19.18 ? 165 VAL C CA  1 
ATOM   5625 C  C   . VAL C  1 165 ? 41.044  6.166   -13.646 1.00 18.96 ? 165 VAL C C   1 
ATOM   5626 O  O   . VAL C  1 165 ? 40.341  6.383   -14.698 1.00 19.66 ? 165 VAL C O   1 
ATOM   5627 C  CB  . VAL C  1 165 ? 43.136  5.745   -15.096 1.00 19.28 ? 165 VAL C CB  1 
ATOM   5628 C  CG1 . VAL C  1 165 ? 44.664  6.003   -15.046 1.00 20.59 ? 165 VAL C CG1 1 
ATOM   5629 C  CG2 . VAL C  1 165 ? 42.826  4.317   -15.539 1.00 18.88 ? 165 VAL C CG2 1 
ATOM   5630 N  N   . LYS C  1 166 ? 40.477  6.152   -12.455 1.00 18.16 ? 166 LYS C N   1 
ATOM   5631 C  CA  . LYS C  1 166 ? 39.043  6.190   -12.389 1.00 17.68 ? 166 LYS C CA  1 
ATOM   5632 C  C   . LYS C  1 166 ? 38.337  7.410   -12.919 1.00 19.69 ? 166 LYS C C   1 
ATOM   5633 O  O   . LYS C  1 166 ? 37.166  7.324   -13.341 1.00 20.03 ? 166 LYS C O   1 
ATOM   5634 C  CB  . LYS C  1 166 ? 38.540  5.905   -10.933 1.00 19.43 ? 166 LYS C CB  1 
ATOM   5635 C  CG  . LYS C  1 166 ? 38.885  4.561   -10.426 1.00 21.12 ? 166 LYS C CG  1 
ATOM   5636 C  CD  . LYS C  1 166 ? 38.430  4.385   -8.978  1.00 24.56 ? 166 LYS C CD  1 
ATOM   5637 C  CE  . LYS C  1 166 ? 36.934  4.294   -8.803  1.00 23.91 ? 166 LYS C CE  1 
ATOM   5638 N  NZ  . LYS C  1 166 ? 36.423  2.989   -9.313  1.00 22.81 ? 166 LYS C NZ  1 
ATOM   5639 N  N   . TYR C  1 167 ? 38.992  8.555   -12.905 1.00 17.61 ? 167 TYR C N   1 
ATOM   5640 C  CA  . TYR C  1 167 ? 38.306  9.753   -13.253 1.00 18.66 ? 167 TYR C CA  1 
ATOM   5641 C  C   . TYR C  1 167 ? 38.903  10.302  -14.548 1.00 19.16 ? 167 TYR C C   1 
ATOM   5642 O  O   . TYR C  1 167 ? 40.141  10.104  -14.785 1.00 20.29 ? 167 TYR C O   1 
ATOM   5643 C  CB  . TYR C  1 167 ? 38.425  10.818  -12.148 1.00 21.69 ? 167 TYR C CB  1 
ATOM   5644 C  CG  . TYR C  1 167 ? 37.806  10.397  -10.835 1.00 19.35 ? 167 TYR C CG  1 
ATOM   5645 C  CD1 . TYR C  1 167 ? 36.427  10.474  -10.626 1.00 21.73 ? 167 TYR C CD1 1 
ATOM   5646 C  CD2 . TYR C  1 167 ? 38.638  9.929   -9.765  1.00 21.30 ? 167 TYR C CD2 1 
ATOM   5647 C  CE1 . TYR C  1 167 ? 35.891  10.099  -9.374  1.00 26.22 ? 167 TYR C CE1 1 
ATOM   5648 C  CE2 . TYR C  1 167 ? 38.093  9.501   -8.557  1.00 22.48 ? 167 TYR C CE2 1 
ATOM   5649 C  CZ  . TYR C  1 167 ? 36.730  9.625   -8.361  1.00 25.07 ? 167 TYR C CZ  1 
ATOM   5650 O  OH  . TYR C  1 167 ? 36.180  9.229   -7.146  1.00 29.65 ? 167 TYR C OH  1 
ATOM   5651 N  N   . LYS C  1 168 ? 38.038  11.085  -15.230 1.00 19.92 ? 168 LYS C N   1 
ATOM   5652 C  CA  . LYS C  1 168 ? 38.397  11.734  -16.497 1.00 22.03 ? 168 LYS C CA  1 
ATOM   5653 C  C   . LYS C  1 168 ? 39.615  12.571  -16.274 1.00 27.07 ? 168 LYS C C   1 
ATOM   5654 O  O   . LYS C  1 168 ? 39.617  13.417  -15.324 1.00 26.62 ? 168 LYS C O   1 
ATOM   5655 C  CB  . LYS C  1 168 ? 37.285  12.693  -16.974 1.00 23.94 ? 168 LYS C CB  1 
ATOM   5656 C  CG  . LYS C  1 168 ? 37.678  13.480  -18.247 1.00 25.91 ? 168 LYS C CG  1 
ATOM   5657 C  CD  . LYS C  1 168 ? 36.466  14.230  -18.776 1.00 28.28 ? 168 LYS C CD  1 
ATOM   5658 C  CE  . LYS C  1 168 ? 36.557  14.420  -20.282 1.00 40.69 ? 168 LYS C CE  1 
ATOM   5659 N  NZ  . LYS C  1 168 ? 37.426  15.544  -20.725 1.00 43.27 ? 168 LYS C NZ  1 
ATOM   5660 N  N   . GLY C  1 169 ? 40.641  12.344  -17.085 1.00 25.04 ? 169 GLY C N   1 
ATOM   5661 C  CA  . GLY C  1 169 ? 41.854  13.098  -17.086 1.00 25.16 ? 169 GLY C CA  1 
ATOM   5662 C  C   . GLY C  1 169 ? 42.951  12.441  -16.346 1.00 25.51 ? 169 GLY C C   1 
ATOM   5663 O  O   . GLY C  1 169 ? 44.120  12.825  -16.454 1.00 28.01 ? 169 GLY C O   1 
ATOM   5664 N  N   . GLN C  1 170 ? 42.610  11.448  -15.520 1.00 20.77 ? 170 GLN C N   1 
ATOM   5665 C  CA  . GLN C  1 170 ? 43.662  10.736  -14.812 1.00 20.77 ? 170 GLN C CA  1 
ATOM   5666 C  C   . GLN C  1 170 ? 44.515  9.836   -15.655 1.00 24.78 ? 170 GLN C C   1 
ATOM   5667 O  O   . GLN C  1 170 ? 44.039  9.262   -16.657 1.00 23.27 ? 170 GLN C O   1 
ATOM   5668 C  CB  . GLN C  1 170 ? 43.156  9.896   -13.589 1.00 21.01 ? 170 GLN C CB  1 
ATOM   5669 C  CG  . GLN C  1 170 ? 42.642  10.803  -12.482 1.00 20.63 ? 170 GLN C CG  1 
ATOM   5670 C  CD  . GLN C  1 170 ? 42.173  9.991   -11.283 1.00 23.69 ? 170 GLN C CD  1 
ATOM   5671 O  OE1 . GLN C  1 170 ? 41.532  8.949   -11.411 1.00 19.91 ? 170 GLN C OE1 1 
ATOM   5672 N  NE2 . GLN C  1 170 ? 42.549  10.443  -10.095 1.00 28.50 ? 170 GLN C NE2 1 
ATOM   5673 N  N   . GLU C  1 171 ? 45.754  9.715   -15.236 1.00 20.69 ? 171 GLU C N   1 
ATOM   5674 C  CA  . GLU C  1 171 ? 46.804  8.882   -15.893 1.00 23.24 ? 171 GLU C CA  1 
ATOM   5675 C  C   . GLU C  1 171 ? 47.593  7.934   -15.012 1.00 22.35 ? 171 GLU C C   1 
ATOM   5676 O  O   . GLU C  1 171 ? 47.806  8.203   -13.826 1.00 25.46 ? 171 GLU C O   1 
ATOM   5677 C  CB  . GLU C  1 171 ? 47.854  9.804   -16.613 1.00 26.05 ? 171 GLU C CB  1 
ATOM   5678 C  CG  . GLU C  1 171 ? 47.293  10.749  -17.661 1.00 30.68 ? 171 GLU C CG  1 
ATOM   5679 C  CD  . GLU C  1 171 ? 48.269  11.851  -18.073 1.00 32.93 ? 171 GLU C CD  1 
ATOM   5680 O  OE1 . GLU C  1 171 ? 49.415  11.858  -17.544 1.00 34.03 ? 171 GLU C OE1 1 
ATOM   5681 O  OE2 . GLU C  1 171 ? 47.818  12.669  -18.931 1.00 39.27 ? 171 GLU C OE2 1 
ATOM   5682 N  N   . ALA C  1 172 ? 48.106  6.874   -15.589 1.00 20.68 ? 172 ALA C N   1 
ATOM   5683 C  CA  . ALA C  1 172 ? 48.980  5.907   -14.899 1.00 20.44 ? 172 ALA C CA  1 
ATOM   5684 C  C   . ALA C  1 172 ? 49.855  5.181   -15.878 1.00 29.64 ? 172 ALA C C   1 
ATOM   5685 O  O   . ALA C  1 172 ? 49.516  5.082   -17.052 1.00 33.19 ? 172 ALA C O   1 
ATOM   5686 C  CB  . ALA C  1 172 ? 48.176  4.888   -14.051 1.00 26.09 ? 172 ALA C CB  1 
ATOM   5687 N  N   A PHE C  1 173 ? 50.976  4.607   -15.421 0.50 27.38 ? 173 PHE C N   1 
ATOM   5688 N  N   B PHE C  1 173 ? 51.008  4.753   -15.421 0.50 28.61 ? 173 PHE C N   1 
ATOM   5689 C  CA  A PHE C  1 173 ? 52.017  3.948   -16.283 0.50 26.99 ? 173 PHE C CA  1 
ATOM   5690 C  CA  B PHE C  1 173 ? 51.795  3.892   -16.239 0.50 29.34 ? 173 PHE C CA  1 
ATOM   5691 C  C   A PHE C  1 173 ? 52.094  2.388   -16.220 0.50 28.95 ? 173 PHE C C   1 
ATOM   5692 C  C   B PHE C  1 173 ? 51.333  2.444   -16.012 0.50 26.94 ? 173 PHE C C   1 
ATOM   5693 O  O   A PHE C  1 173 ? 52.843  1.826   -15.382 0.50 28.09 ? 173 PHE C O   1 
ATOM   5694 O  O   B PHE C  1 173 ? 50.862  2.047   -14.940 0.50 20.30 ? 173 PHE C O   1 
ATOM   5695 C  CB  A PHE C  1 173 ? 53.403  4.549   -16.025 0.50 25.54 ? 173 PHE C CB  1 
ATOM   5696 C  CB  B PHE C  1 173 ? 53.292  4.155   -16.093 0.50 31.49 ? 173 PHE C CB  1 
ATOM   5697 C  CG  A PHE C  1 173 ? 53.658  5.884   -16.699 0.50 22.39 ? 173 PHE C CG  1 
ATOM   5698 C  CG  B PHE C  1 173 ? 53.771  5.453   -16.756 0.50 34.06 ? 173 PHE C CG  1 
ATOM   5699 C  CD1 A PHE C  1 173 ? 53.978  5.955   -18.044 0.50 23.59 ? 173 PHE C CD1 1 
ATOM   5700 C  CD1 B PHE C  1 173 ? 54.208  5.458   -18.085 0.50 36.01 ? 173 PHE C CD1 1 
ATOM   5701 C  CD2 A PHE C  1 173 ? 53.628  7.071   -15.960 0.50 21.08 ? 173 PHE C CD2 1 
ATOM   5702 C  CD2 B PHE C  1 173 ? 53.833  6.645   -16.041 0.50 35.72 ? 173 PHE C CD2 1 
ATOM   5703 C  CE1 A PHE C  1 173 ? 54.231  7.172   -18.663 0.50 22.37 ? 173 PHE C CE1 1 
ATOM   5704 C  CE1 B PHE C  1 173 ? 54.667  6.620   -18.688 0.50 36.44 ? 173 PHE C CE1 1 
ATOM   5705 C  CE2 A PHE C  1 173 ? 53.879  8.292   -16.573 0.50 21.23 ? 173 PHE C CE2 1 
ATOM   5706 C  CE2 B PHE C  1 173 ? 54.287  7.814   -16.645 0.50 35.81 ? 173 PHE C CE2 1 
ATOM   5707 C  CZ  A PHE C  1 173 ? 54.193  8.341   -17.924 0.50 20.75 ? 173 PHE C CZ  1 
ATOM   5708 C  CZ  B PHE C  1 173 ? 54.701  7.804   -17.968 0.50 36.91 ? 173 PHE C CZ  1 
ATOM   5709 N  N   . VAL C  1 174 ? 51.330  1.733   -17.121 1.00 26.15 ? 174 VAL C N   1 
ATOM   5710 C  CA  . VAL C  1 174 ? 51.161  0.273   -17.175 1.00 29.90 ? 174 VAL C CA  1 
ATOM   5711 C  C   . VAL C  1 174 ? 52.519  -0.235  -17.675 1.00 30.18 ? 174 VAL C C   1 
ATOM   5712 O  O   . VAL C  1 174 ? 53.051  0.307   -18.659 1.00 30.12 ? 174 VAL C O   1 
ATOM   5713 C  CB  . VAL C  1 174 ? 50.016  -0.122  -18.191 1.00 29.67 ? 174 VAL C CB  1 
ATOM   5714 C  CG1 . VAL C  1 174 ? 50.051  -1.630  -18.530 1.00 30.65 ? 174 VAL C CG1 1 
ATOM   5715 C  CG2 . VAL C  1 174 ? 48.636  0.305   -17.646 1.00 37.33 ? 174 VAL C CG2 1 
ATOM   5716 N  N   . PRO C  1 175 ? 53.101  -1.283  -17.018 1.00 29.47 ? 175 PRO C N   1 
ATOM   5717 C  CA  . PRO C  1 175 ? 54.352  -1.812  -17.632 1.00 26.82 ? 175 PRO C CA  1 
ATOM   5718 C  C   . PRO C  1 175 ? 54.103  -2.513  -18.985 1.00 28.49 ? 175 PRO C C   1 
ATOM   5719 O  O   . PRO C  1 175 ? 53.005  -2.969  -19.242 1.00 29.05 ? 175 PRO C O   1 
ATOM   5720 C  CB  . PRO C  1 175 ? 54.892  -2.824  -16.598 1.00 32.94 ? 175 PRO C CB  1 
ATOM   5721 C  CG  . PRO C  1 175 ? 53.848  -2.928  -15.518 1.00 35.62 ? 175 PRO C CG  1 
ATOM   5722 C  CD  . PRO C  1 175 ? 52.730  -1.930  -15.734 1.00 31.29 ? 175 PRO C CD  1 
ATOM   5723 N  N   . GLY C  1 176 ? 55.133  -2.567  -19.801 1.00 23.23 ? 176 GLY C N   1 
ATOM   5724 C  CA  . GLY C  1 176 ? 55.150  -3.223  -21.111 1.00 28.88 ? 176 GLY C CA  1 
ATOM   5725 C  C   . GLY C  1 176 ? 54.746  -4.682  -20.988 1.00 29.42 ? 176 GLY C C   1 
ATOM   5726 O  O   . GLY C  1 176 ? 54.892  -5.315  -19.921 1.00 28.27 ? 176 GLY C O   1 
ATOM   5727 N  N   . PHE C  1 177 ? 54.161  -5.179  -22.075 1.00 29.35 ? 177 PHE C N   1 
ATOM   5728 C  CA  . PHE C  1 177 ? 53.796  -6.615  -22.235 1.00 20.54 ? 177 PHE C CA  1 
ATOM   5729 C  C   . PHE C  1 177 ? 53.651  -6.813  -23.784 1.00 23.47 ? 177 PHE C C   1 
ATOM   5730 O  O   . PHE C  1 177 ? 53.788  -5.852  -24.570 1.00 22.57 ? 177 PHE C O   1 
ATOM   5731 C  CB  . PHE C  1 177 ? 52.588  -7.062  -21.402 1.00 25.82 ? 177 PHE C CB  1 
ATOM   5732 C  CG  . PHE C  1 177 ? 51.273  -6.502  -21.879 1.00 26.36 ? 177 PHE C CG  1 
ATOM   5733 C  CD1 . PHE C  1 177 ? 50.436  -7.245  -22.688 1.00 24.62 ? 177 PHE C CD1 1 
ATOM   5734 C  CD2 . PHE C  1 177 ? 50.889  -5.205  -21.489 1.00 26.62 ? 177 PHE C CD2 1 
ATOM   5735 C  CE1 . PHE C  1 177 ? 49.233  -6.711  -23.132 1.00 26.83 ? 177 PHE C CE1 1 
ATOM   5736 C  CE2 . PHE C  1 177 ? 49.666  -4.679  -21.880 1.00 27.79 ? 177 PHE C CE2 1 
ATOM   5737 C  CZ  . PHE C  1 177 ? 48.851  -5.454  -22.716 1.00 26.80 ? 177 PHE C CZ  1 
ATOM   5738 N  N   . ASN C  1 178 ? 53.500  -8.067  -24.220 1.00 20.61 ? 178 ASN C N   1 
ATOM   5739 C  CA  . ASN C  1 178 ? 53.446  -8.352  -25.649 1.00 19.19 ? 178 ASN C CA  1 
ATOM   5740 C  C   . ASN C  1 178 ? 51.973  -8.168  -26.106 1.00 19.47 ? 178 ASN C C   1 
ATOM   5741 O  O   . ASN C  1 178 ? 51.059  -8.896  -25.721 1.00 19.71 ? 178 ASN C O   1 
ATOM   5742 C  CB  . ASN C  1 178 ? 53.829  -9.787  -25.837 1.00 21.37 ? 178 ASN C CB  1 
ATOM   5743 C  CG  . ASN C  1 178 ? 53.742  -10.197 -27.283 1.00 22.80 ? 178 ASN C CG  1 
ATOM   5744 O  OD1 . ASN C  1 178 ? 53.617  -9.360  -28.202 1.00 22.11 ? 178 ASN C OD1 1 
ATOM   5745 N  ND2 . ASN C  1 178 ? 53.827  -11.503 -27.510 1.00 24.07 ? 178 ASN C ND2 1 
ATOM   5746 N  N   . ILE C  1 179 ? 51.812  -7.072  -26.864 1.00 18.11 ? 179 ILE C N   1 
ATOM   5747 C  CA  . ILE C  1 179 ? 50.473  -6.623  -27.285 1.00 15.89 ? 179 ILE C CA  1 
ATOM   5748 C  C   . ILE C  1 179 ? 49.856  -7.714  -28.138 1.00 17.79 ? 179 ILE C C   1 
ATOM   5749 O  O   . ILE C  1 179 ? 48.600  -7.768  -28.220 1.00 16.69 ? 179 ILE C O   1 
ATOM   5750 C  CB  . ILE C  1 179 ? 50.612  -5.264  -27.973 1.00 15.79 ? 179 ILE C CB  1 
ATOM   5751 C  CG1 . ILE C  1 179 ? 51.199  -4.193  -27.038 1.00 17.07 ? 179 ILE C CG1 1 
ATOM   5752 C  CG2 . ILE C  1 179 ? 49.214  -4.829  -28.490 1.00 16.04 ? 179 ILE C CG2 1 
ATOM   5753 C  CD1 . ILE C  1 179 ? 50.517  -3.970  -25.653 1.00 17.95 ? 179 ILE C CD1 1 
ATOM   5754 N  N   . GLU C  1 180 ? 50.663  -8.523  -28.805 1.00 16.41 ? 180 GLU C N   1 
ATOM   5755 C  CA  . GLU C  1 180 ? 50.139  -9.609  -29.642 1.00 18.04 ? 180 GLU C CA  1 
ATOM   5756 C  C   . GLU C  1 180 ? 49.367  -10.635 -28.835 1.00 21.23 ? 180 GLU C C   1 
ATOM   5757 O  O   . GLU C  1 180 ? 48.516  -11.332 -29.406 1.00 18.13 ? 180 GLU C O   1 
ATOM   5758 C  CB  . GLU C  1 180 ? 51.244  -10.232 -30.487 1.00 21.15 ? 180 GLU C CB  1 
ATOM   5759 C  CG  . GLU C  1 180 ? 50.666  -10.999 -31.658 1.00 24.76 ? 180 GLU C CG  1 
ATOM   5760 C  CD  . GLU C  1 180 ? 51.746  -11.549 -32.607 1.00 31.38 ? 180 GLU C CD  1 
ATOM   5761 O  OE1 . GLU C  1 180 ? 52.943  -11.308 -32.367 1.00 26.87 ? 180 GLU C OE1 1 
ATOM   5762 O  OE2 . GLU C  1 180 ? 51.337  -12.290 -33.526 1.00 29.21 ? 180 GLU C OE2 1 
ATOM   5763 N  N   . GLU C  1 181 ? 49.542  -10.645 -27.510 1.00 19.02 ? 181 GLU C N   1 
ATOM   5764 C  CA  . GLU C  1 181 ? 48.763  -11.595 -26.711 1.00 19.75 ? 181 GLU C CA  1 
ATOM   5765 C  C   . GLU C  1 181 ? 47.274  -11.158 -26.599 1.00 19.56 ? 181 GLU C C   1 
ATOM   5766 O  O   . GLU C  1 181 ? 46.442  -11.944 -26.172 1.00 19.57 ? 181 GLU C O   1 
ATOM   5767 C  CB  . GLU C  1 181 ? 49.303  -11.659 -25.275 1.00 20.54 ? 181 GLU C CB  1 
ATOM   5768 C  CG  . GLU C  1 181 ? 50.718  -12.227 -25.122 1.00 23.66 ? 181 GLU C CG  1 
ATOM   5769 C  CD  . GLU C  1 181 ? 51.293  -11.958 -23.733 1.00 25.83 ? 181 GLU C CD  1 
ATOM   5770 O  OE1 . GLU C  1 181 ? 50.542  -11.580 -22.790 1.00 26.80 ? 181 GLU C OE1 1 
ATOM   5771 O  OE2 . GLU C  1 181 ? 52.552  -12.090 -23.528 1.00 28.59 ? 181 GLU C OE2 1 
ATOM   5772 N  N   . LEU C  1 182 ? 46.959  -9.898  -26.981 1.00 17.32 ? 182 LEU C N   1 
ATOM   5773 C  CA  . LEU C  1 182 ? 45.529  -9.378  -27.000 1.00 15.02 ? 182 LEU C CA  1 
ATOM   5774 C  C   . LEU C  1 182 ? 44.750  -9.803  -28.213 1.00 16.40 ? 182 LEU C C   1 
ATOM   5775 O  O   . LEU C  1 182 ? 43.506  -9.720  -28.278 1.00 16.21 ? 182 LEU C O   1 
ATOM   5776 C  CB  . LEU C  1 182 ? 45.542  -7.852  -26.859 1.00 16.07 ? 182 LEU C CB  1 
ATOM   5777 C  CG  . LEU C  1 182 ? 46.217  -7.258  -25.628 1.00 15.51 ? 182 LEU C CG  1 
ATOM   5778 C  CD1 . LEU C  1 182 ? 46.216  -5.721  -25.626 1.00 16.23 ? 182 LEU C CD1 1 
ATOM   5779 C  CD2 . LEU C  1 182 ? 45.666  -7.773  -24.257 1.00 16.85 ? 182 LEU C CD2 1 
ATOM   5780 N  N   . LEU C  1 183 ? 45.497  -10.353 -29.185 1.00 17.10 ? 183 LEU C N   1 
ATOM   5781 C  CA  . LEU C  1 183 ? 44.889  -10.777 -30.438 1.00 16.84 ? 183 LEU C CA  1 
ATOM   5782 C  C   . LEU C  1 183 ? 44.323  -12.202 -30.308 1.00 18.13 ? 183 LEU C C   1 
ATOM   5783 O  O   . LEU C  1 183 ? 44.782  -13.005 -29.434 1.00 20.71 ? 183 LEU C O   1 
ATOM   5784 C  CB  . LEU C  1 183 ? 45.877  -10.690 -31.640 1.00 18.34 ? 183 LEU C CB  1 
ATOM   5785 C  CG  . LEU C  1 183 ? 46.504  -9.312  -31.764 1.00 17.74 ? 183 LEU C CG  1 
ATOM   5786 C  CD1 . LEU C  1 183 ? 47.454  -9.365  -32.969 1.00 21.77 ? 183 LEU C CD1 1 
ATOM   5787 C  CD2 . LEU C  1 183 ? 45.502  -8.200  -31.910 1.00 20.74 ? 183 LEU C CD2 1 
ATOM   5788 N  N   . PRO C  1 184 ? 43.350  -12.543 -31.128 1.00 16.62 ? 184 PRO C N   1 
ATOM   5789 C  CA  . PRO C  1 184 ? 42.667  -13.814 -31.064 1.00 18.05 ? 184 PRO C CA  1 
ATOM   5790 C  C   . PRO C  1 184 ? 43.407  -14.878 -31.848 1.00 23.13 ? 184 PRO C C   1 
ATOM   5791 O  O   . PRO C  1 184 ? 44.426  -14.604 -32.459 1.00 20.62 ? 184 PRO C O   1 
ATOM   5792 C  CB  . PRO C  1 184 ? 41.302  -13.494 -31.696 1.00 19.26 ? 184 PRO C CB  1 
ATOM   5793 C  CG  . PRO C  1 184 ? 41.702  -12.482 -32.735 1.00 15.58 ? 184 PRO C CG  1 
ATOM   5794 C  CD  . PRO C  1 184 ? 42.664  -11.574 -32.034 1.00 15.03 ? 184 PRO C CD  1 
ATOM   5795 N  N   . GLU C  1 185 ? 42.906  -16.103 -31.728 1.00 22.63 ? 185 GLU C N   1 
ATOM   5796 C  CA  . GLU C  1 185 ? 43.407  -17.197 -32.523 1.00 26.02 ? 185 GLU C CA  1 
ATOM   5797 C  C   . GLU C  1 185 ? 43.137  -16.910 -34.021 1.00 21.86 ? 185 GLU C C   1 
ATOM   5798 O  O   . GLU C  1 185 ? 42.100  -16.223 -34.430 1.00 23.15 ? 185 GLU C O   1 
ATOM   5799 C  CB  . GLU C  1 185 ? 42.653  -18.483 -32.154 1.00 30.50 ? 185 GLU C CB  1 
ATOM   5800 C  CG  . GLU C  1 185 ? 43.029  -19.009 -30.775 1.00 36.25 ? 185 GLU C CG  1 
ATOM   5801 C  CD  . GLU C  1 185 ? 44.434  -19.577 -30.740 1.00 51.04 ? 185 GLU C CD  1 
ATOM   5802 O  OE1 . GLU C  1 185 ? 45.396  -18.776 -30.901 1.00 57.19 ? 185 GLU C OE1 1 
ATOM   5803 O  OE2 . GLU C  1 185 ? 44.573  -20.820 -30.535 1.00 56.14 ? 185 GLU C OE2 1 
ATOM   5804 N  N   . ARG C  1 186 ? 44.034  -17.448 -34.837 1.00 22.55 ? 186 ARG C N   1 
ATOM   5805 C  CA  . ARG C  1 186 ? 43.947  -17.342 -36.291 1.00 22.51 ? 186 ARG C CA  1 
ATOM   5806 C  C   . ARG C  1 186 ? 43.678  -15.971 -36.833 1.00 18.63 ? 186 ARG C C   1 
ATOM   5807 O  O   . ARG C  1 186 ? 42.682  -15.713 -37.573 1.00 20.11 ? 186 ARG C O   1 
ATOM   5808 C  CB  . ARG C  1 186 ? 42.920  -18.341 -36.787 1.00 22.83 ? 186 ARG C CB  1 
ATOM   5809 C  CG  . ARG C  1 186 ? 43.434  -19.745 -36.478 1.00 26.83 ? 186 ARG C CG  1 
ATOM   5810 C  CD  . ARG C  1 186 ? 42.370  -20.833 -36.627 1.00 31.98 ? 186 ARG C CD  1 
ATOM   5811 N  NE  . ARG C  1 186 ? 41.709  -20.988 -35.330 1.00 39.46 ? 186 ARG C NE  1 
ATOM   5812 C  CZ  . ARG C  1 186 ? 40.401  -20.872 -35.119 1.00 41.21 ? 186 ARG C CZ  1 
ATOM   5813 N  NH1 . ARG C  1 186 ? 39.577  -20.624 -36.126 1.00 40.90 ? 186 ARG C NH1 1 
ATOM   5814 N  NH2 . ARG C  1 186 ? 39.916  -21.017 -33.892 1.00 44.61 ? 186 ARG C NH2 1 
ATOM   5815 N  N   . THR C  1 187 ? 44.613  -15.117 -36.492 1.00 19.51 ? 187 THR C N   1 
ATOM   5816 C  CA  . THR C  1 187 ? 44.576  -13.757 -37.045 1.00 17.40 ? 187 THR C CA  1 
ATOM   5817 C  C   . THR C  1 187 ? 44.548  -13.669 -38.583 1.00 17.44 ? 187 THR C C   1 
ATOM   5818 O  O   . THR C  1 187 ? 44.202  -12.660 -39.116 1.00 17.02 ? 187 THR C O   1 
ATOM   5819 C  CB  . THR C  1 187 ? 45.658  -12.845 -36.487 1.00 18.01 ? 187 THR C CB  1 
ATOM   5820 O  OG1 . THR C  1 187 ? 46.967  -13.429 -36.698 1.00 22.84 ? 187 THR C OG1 1 
ATOM   5821 C  CG2 . THR C  1 187 ? 45.481  -12.659 -34.937 1.00 18.37 ? 187 THR C CG2 1 
ATOM   5822 N  N   . ALA C  1 188 ? 44.957  -14.743 -39.294 1.00 16.63 ? 188 ALA C N   1 
ATOM   5823 C  CA  . ALA C  1 188 ? 44.777  -14.720 -40.730 1.00 17.78 ? 188 ALA C CA  1 
ATOM   5824 C  C   . ALA C  1 188 ? 43.291  -14.593 -41.241 1.00 15.35 ? 188 ALA C C   1 
ATOM   5825 O  O   . ALA C  1 188 ? 43.039  -14.254 -42.445 1.00 15.94 ? 188 ALA C O   1 
ATOM   5826 C  CB  . ALA C  1 188 ? 45.450  -15.970 -41.354 1.00 19.99 ? 188 ALA C CB  1 
ATOM   5827 N  N   . GLU C  1 189 ? 42.349  -14.912 -40.375 1.00 16.53 ? 189 GLU C N   1 
ATOM   5828 C  CA  . GLU C  1 189 ? 40.918  -14.821 -40.640 1.00 16.23 ? 189 GLU C CA  1 
ATOM   5829 C  C   . GLU C  1 189 ? 40.366  -13.437 -40.191 1.00 13.81 ? 189 GLU C C   1 
ATOM   5830 O  O   . GLU C  1 189 ? 40.323  -13.161 -38.965 1.00 15.67 ? 189 GLU C O   1 
ATOM   5831 C  CB  . GLU C  1 189 ? 40.134  -15.925 -39.905 1.00 17.26 ? 189 GLU C CB  1 
ATOM   5832 C  CG  . GLU C  1 189 ? 40.590  -17.304 -40.392 1.00 22.74 ? 189 GLU C CG  1 
ATOM   5833 C  CD  . GLU C  1 189 ? 40.086  -18.488 -39.542 1.00 28.48 ? 189 GLU C CD  1 
ATOM   5834 O  OE1 . GLU C  1 189 ? 39.197  -18.387 -38.616 1.00 27.99 ? 189 GLU C OE1 1 
ATOM   5835 O  OE2 . GLU C  1 189 ? 40.645  -19.583 -39.778 1.00 31.02 ? 189 GLU C OE2 1 
ATOM   5836 N  N   . TYR C  1 190 ? 39.977  -12.625 -41.160 1.00 12.81 ? 190 TYR C N   1 
ATOM   5837 C  CA  . TYR C  1 190 ? 39.466  -11.318 -40.766 1.00 12.22 ? 190 TYR C CA  1 
ATOM   5838 C  C   . TYR C  1 190 ? 38.576  -10.751 -41.833 1.00 11.51 ? 190 TYR C C   1 
ATOM   5839 O  O   . TYR C  1 190 ? 38.587  -11.118 -43.004 1.00 13.56 ? 190 TYR C O   1 
ATOM   5840 C  CB  . TYR C  1 190 ? 40.658  -10.347 -40.509 1.00 12.50 ? 190 TYR C CB  1 
ATOM   5841 C  CG  . TYR C  1 190 ? 41.607  -10.174 -41.672 1.00 13.18 ? 190 TYR C CG  1 
ATOM   5842 C  CD1 . TYR C  1 190 ? 41.369  -9.201  -42.690 1.00 13.62 ? 190 TYR C CD1 1 
ATOM   5843 C  CD2 . TYR C  1 190 ? 42.803  -10.947 -41.750 1.00 14.09 ? 190 TYR C CD2 1 
ATOM   5844 C  CE1 . TYR C  1 190 ? 42.317  -9.002  -43.765 1.00 12.00 ? 190 TYR C CE1 1 
ATOM   5845 C  CE2 . TYR C  1 190 ? 43.732  -10.706 -42.795 1.00 13.71 ? 190 TYR C CE2 1 
ATOM   5846 C  CZ  . TYR C  1 190 ? 43.466  -9.800  -43.781 1.00 14.33 ? 190 TYR C CZ  1 
ATOM   5847 O  OH  . TYR C  1 190 ? 44.387  -9.586  -44.800 1.00 14.10 ? 190 TYR C OH  1 
ATOM   5848 N  N   . TYR C  1 191 ? 37.764  -9.745  -41.406 1.00 10.60 ? 191 TYR C N   1 
ATOM   5849 C  CA  . TYR C  1 191 ? 36.998  -8.870  -42.266 1.00 10.83 ? 191 TYR C CA  1 
ATOM   5850 C  C   . TYR C  1 191 ? 37.739  -7.575  -42.548 1.00 11.08 ? 191 TYR C C   1 
ATOM   5851 O  O   . TYR C  1 191 ? 38.442  -7.047  -41.622 1.00 10.88 ? 191 TYR C O   1 
ATOM   5852 C  CB  . TYR C  1 191 ? 35.706  -8.494  -41.528 1.00 10.80 ? 191 TYR C CB  1 
ATOM   5853 C  CG  . TYR C  1 191 ? 34.869  -9.621  -40.973 1.00 11.33 ? 191 TYR C CG  1 
ATOM   5854 C  CD1 . TYR C  1 191 ? 33.786  -10.163 -41.720 1.00 11.09 ? 191 TYR C CD1 1 
ATOM   5855 C  CD2 . TYR C  1 191 ? 35.043  -10.046 -39.613 1.00 11.05 ? 191 TYR C CD2 1 
ATOM   5856 C  CE1 . TYR C  1 191 ? 32.992  -11.149 -41.178 1.00 11.62 ? 191 TYR C CE1 1 
ATOM   5857 C  CE2 . TYR C  1 191 ? 34.179  -10.997 -39.053 1.00 11.90 ? 191 TYR C CE2 1 
ATOM   5858 C  CZ  . TYR C  1 191 ? 33.181  -11.510 -39.856 1.00 13.06 ? 191 TYR C CZ  1 
ATOM   5859 O  OH  . TYR C  1 191 ? 32.320  -12.483 -39.291 1.00 15.94 ? 191 TYR C OH  1 
ATOM   5860 N  N   . ARG C  1 192 ? 37.600  -7.026  -43.752 1.00 10.28 ? 192 ARG C N   1 
ATOM   5861 C  CA  . ARG C  1 192 ? 38.277  -5.781  -44.147 1.00 10.70 ? 192 ARG C CA  1 
ATOM   5862 C  C   . ARG C  1 192 ? 37.285  -4.856  -44.824 1.00 10.66 ? 192 ARG C C   1 
ATOM   5863 O  O   . ARG C  1 192 ? 36.548  -5.281  -45.784 1.00 9.75  ? 192 ARG C O   1 
ATOM   5864 C  CB  . ARG C  1 192 ? 39.399  -6.171  -45.114 1.00 10.98 ? 192 ARG C CB  1 
ATOM   5865 C  CG  . ARG C  1 192 ? 40.030  -4.980  -45.872 1.00 10.97 ? 192 ARG C CG  1 
ATOM   5866 C  CD  . ARG C  1 192 ? 40.806  -3.956  -45.021 1.00 13.02 ? 192 ARG C CD  1 
ATOM   5867 N  NE  . ARG C  1 192 ? 41.757  -4.600  -44.104 1.00 12.13 ? 192 ARG C NE  1 
ATOM   5868 C  CZ  . ARG C  1 192 ? 42.913  -5.159  -44.467 1.00 13.84 ? 192 ARG C CZ  1 
ATOM   5869 N  NH1 . ARG C  1 192 ? 43.284  -5.167  -45.740 1.00 14.68 ? 192 ARG C NH1 1 
ATOM   5870 N  NH2 . ARG C  1 192 ? 43.705  -5.713  -43.556 1.00 14.45 ? 192 ARG C NH2 1 
ATOM   5871 N  N   . TYR C  1 193 ? 37.265  -3.577  -44.410 1.00 9.03  ? 193 TYR C N   1 
ATOM   5872 C  CA  . TYR C  1 193 ? 36.491  -2.600  -45.206 1.00 9.66  ? 193 TYR C CA  1 
ATOM   5873 C  C   . TYR C  1 193 ? 37.060  -1.198  -44.934 1.00 8.56  ? 193 TYR C C   1 
ATOM   5874 O  O   . TYR C  1 193 ? 37.764  -1.012  -43.897 1.00 9.79  ? 193 TYR C O   1 
ATOM   5875 C  CB  . TYR C  1 193 ? 34.976  -2.638  -44.947 1.00 9.29  ? 193 TYR C CB  1 
ATOM   5876 C  CG  . TYR C  1 193 ? 34.595  -2.097  -43.551 1.00 8.73  ? 193 TYR C CG  1 
ATOM   5877 C  CD1 . TYR C  1 193 ? 34.048  -0.831  -43.440 1.00 8.81  ? 193 TYR C CD1 1 
ATOM   5878 C  CD2 . TYR C  1 193 ? 34.799  -2.843  -42.354 1.00 8.22  ? 193 TYR C CD2 1 
ATOM   5879 C  CE1 . TYR C  1 193 ? 33.698  -0.309  -42.212 1.00 8.60  ? 193 TYR C CE1 1 
ATOM   5880 C  CE2 . TYR C  1 193 ? 34.440  -2.298  -41.122 1.00 7.75  ? 193 TYR C CE2 1 
ATOM   5881 C  CZ  . TYR C  1 193 ? 33.890  -1.033  -41.057 1.00 7.71  ? 193 TYR C CZ  1 
ATOM   5882 O  OH  . TYR C  1 193 ? 33.528  -0.460  -39.850 1.00 8.80  ? 193 TYR C OH  1 
ATOM   5883 N  N   . ARG C  1 194 ? 36.744  -0.244  -45.797 1.00 9.74  ? 194 ARG C N   1 
ATOM   5884 C  CA  . ARG C  1 194 ? 37.196  1.129   -45.586 1.00 10.20 ? 194 ARG C CA  1 
ATOM   5885 C  C   . ARG C  1 194 ? 36.075  1.818   -44.819 1.00 11.24 ? 194 ARG C C   1 
ATOM   5886 O  O   . ARG C  1 194 ? 34.875  1.794   -45.233 1.00 11.31 ? 194 ARG C O   1 
ATOM   5887 C  CB  . ARG C  1 194 ? 37.272  1.844   -46.943 1.00 13.04 ? 194 ARG C CB  1 
ATOM   5888 C  CG  . ARG C  1 194 ? 38.486  1.314   -47.650 1.00 15.99 ? 194 ARG C CG  1 
ATOM   5889 C  CD  . ARG C  1 194 ? 38.925  2.082   -48.940 1.00 28.29 ? 194 ARG C CD  1 
ATOM   5890 N  NE  . ARG C  1 194 ? 40.141  1.460   -49.452 1.00 40.46 ? 194 ARG C NE  1 
ATOM   5891 C  CZ  . ARG C  1 194 ? 41.374  1.732   -49.031 1.00 55.46 ? 194 ARG C CZ  1 
ATOM   5892 N  NH1 . ARG C  1 194 ? 41.590  2.651   -48.097 1.00 53.05 ? 194 ARG C NH1 1 
ATOM   5893 N  NH2 . ARG C  1 194 ? 42.401  1.088   -49.566 1.00 58.44 ? 194 ARG C NH2 1 
ATOM   5894 N  N   . GLY C  1 195 ? 36.407  2.446   -43.710 1.00 9.70  ? 195 GLY C N   1 
ATOM   5895 C  CA  . GLY C  1 195 ? 35.409  3.202   -42.916 1.00 9.58  ? 195 GLY C CA  1 
ATOM   5896 C  C   . GLY C  1 195 ? 35.982  4.368   -42.216 1.00 8.90  ? 195 GLY C C   1 
ATOM   5897 O  O   . GLY C  1 195 ? 36.811  5.128   -42.745 1.00 9.98  ? 195 GLY C O   1 
ATOM   5898 N  N   . SER C  1 196 ? 35.493  4.581   -40.988 1.00 9.14  ? 196 SER C N   1 
ATOM   5899 C  CA  . SER C  1 196 ? 35.813  5.823   -40.275 1.00 9.16  ? 196 SER C CA  1 
ATOM   5900 C  C   . SER C  1 196 ? 36.237  5.574   -38.848 1.00 9.02  ? 196 SER C C   1 
ATOM   5901 O  O   . SER C  1 196 ? 36.095  4.444   -38.276 1.00 9.22  ? 196 SER C O   1 
ATOM   5902 C  CB  . SER C  1 196 ? 34.573  6.816   -40.250 1.00 9.10  ? 196 SER C CB  1 
ATOM   5903 O  OG  . SER C  1 196 ? 33.607  6.344   -39.285 1.00 9.12  ? 196 SER C OG  1 
ATOM   5904 N  N   . LEU C  1 197 ? 36.750  6.610   -38.235 1.00 9.14  ? 197 LEU C N   1 
ATOM   5905 C  CA  . LEU C  1 197 ? 36.777  6.628   -36.774 1.00 9.94  ? 197 LEU C CA  1 
ATOM   5906 C  C   . LEU C  1 197 ? 35.361  6.458   -36.228 1.00 8.47  ? 197 LEU C C   1 
ATOM   5907 O  O   . LEU C  1 197 ? 34.411  7.047   -36.794 1.00 9.54  ? 197 LEU C O   1 
ATOM   5908 C  CB  . LEU C  1 197 ? 37.405  7.947   -36.180 1.00 10.68 ? 197 LEU C CB  1 
ATOM   5909 C  CG  . LEU C  1 197 ? 38.912  8.077   -36.458 1.00 13.31 ? 197 LEU C CG  1 
ATOM   5910 C  CD1 . LEU C  1 197 ? 39.264  9.398   -35.828 1.00 17.46 ? 197 LEU C CD1 1 
ATOM   5911 C  CD2 . LEU C  1 197 ? 39.685  6.989   -35.810 1.00 18.13 ? 197 LEU C CD2 1 
ATOM   5912 N  N   . THR C  1 198 ? 35.200  5.707   -35.147 1.00 9.68  ? 198 THR C N   1 
ATOM   5913 C  CA  . THR C  1 198 ? 33.874  5.548   -34.540 1.00 9.20  ? 198 THR C CA  1 
ATOM   5914 C  C   . THR C  1 198 ? 33.601  6.565   -33.451 1.00 10.80 ? 198 THR C C   1 
ATOM   5915 O  O   . THR C  1 198 ? 32.525  6.520   -32.806 1.00 9.67  ? 198 THR C O   1 
ATOM   5916 C  CB  . THR C  1 198 ? 33.738  4.153   -33.942 1.00 10.82 ? 198 THR C CB  1 
ATOM   5917 O  OG1 . THR C  1 198 ? 34.638  4.032   -32.852 1.00 9.71  ? 198 THR C OG1 1 
ATOM   5918 C  CG2 . THR C  1 198 ? 34.011  2.969   -34.912 1.00 10.13 ? 198 THR C CG2 1 
ATOM   5919 N  N   . THR C  1 199 ? 34.541  7.497   -33.245 1.00 10.11 ? 199 THR C N   1 
ATOM   5920 C  CA  . THR C  1 199 ? 34.372  8.654   -32.325 1.00 10.08 ? 199 THR C CA  1 
ATOM   5921 C  C   . THR C  1 199 ? 34.671  9.889   -33.093 1.00 12.13 ? 199 THR C C   1 
ATOM   5922 O  O   . THR C  1 199 ? 35.406  9.869   -34.066 1.00 12.25 ? 199 THR C O   1 
ATOM   5923 C  CB  . THR C  1 199 ? 35.361  8.612   -31.143 1.00 13.25 ? 199 THR C CB  1 
ATOM   5924 O  OG1 . THR C  1 199 ? 36.695  8.508   -31.666 1.00 17.57 ? 199 THR C OG1 1 
ATOM   5925 C  CG2 . THR C  1 199 ? 35.169  7.286   -30.344 1.00 12.70 ? 199 THR C CG2 1 
ATOM   5926 N  N   . PRO C  1 200 ? 34.211  11.046  -32.576 1.00 10.59 ? 200 PRO C N   1 
ATOM   5927 C  CA  . PRO C  1 200 ? 34.613  12.311  -33.212 1.00 11.04 ? 200 PRO C CA  1 
ATOM   5928 C  C   . PRO C  1 200 ? 36.120  12.381  -33.314 1.00 12.93 ? 200 PRO C C   1 
ATOM   5929 O  O   . PRO C  1 200 ? 36.806  11.936  -32.368 1.00 13.54 ? 200 PRO C O   1 
ATOM   5930 C  CB  . PRO C  1 200 ? 34.121  13.321  -32.166 1.00 11.19 ? 200 PRO C CB  1 
ATOM   5931 C  CG  . PRO C  1 200 ? 32.865  12.681  -31.597 1.00 11.70 ? 200 PRO C CG  1 
ATOM   5932 C  CD  . PRO C  1 200 ? 33.245  11.227  -31.488 1.00 11.18 ? 200 PRO C CD  1 
ATOM   5933 N  N   . PRO C  1 201 ? 36.613  12.922  -34.395 1.00 10.91 ? 201 PRO C N   1 
ATOM   5934 C  CA  . PRO C  1 201 ? 35.889  13.609  -35.494 1.00 11.45 ? 201 PRO C CA  1 
ATOM   5935 C  C   . PRO C  1 201 ? 35.279  12.758  -36.616 1.00 10.22 ? 201 PRO C C   1 
ATOM   5936 O  O   . PRO C  1 201 ? 34.794  13.295  -37.595 1.00 12.05 ? 201 PRO C O   1 
ATOM   5937 C  CB  . PRO C  1 201 ? 36.888  14.628  -36.055 1.00 11.47 ? 201 PRO C CB  1 
ATOM   5938 C  CG  . PRO C  1 201 ? 38.006  14.646  -35.039 1.00 14.16 ? 201 PRO C CG  1 
ATOM   5939 C  CD  . PRO C  1 201 ? 38.079  13.180  -34.481 1.00 12.77 ? 201 PRO C CD  1 
ATOM   5940 N  N   . CYS C  1 202 ? 35.321  11.447  -36.399 1.00 10.56 ? 202 CYS C N   1 
ATOM   5941 C  CA  . CYS C  1 202 ? 34.676  10.502  -37.346 1.00 10.81 ? 202 CYS C CA  1 
ATOM   5942 C  C   . CYS C  1 202 ? 35.207  10.523  -38.761 1.00 10.28 ? 202 CYS C C   1 
ATOM   5943 O  O   . CYS C  1 202 ? 34.527  10.178  -39.710 1.00 10.16 ? 202 CYS C O   1 
ATOM   5944 C  CB  . CYS C  1 202 ? 33.102  10.689  -37.444 1.00 10.57 ? 202 CYS C CB  1 
ATOM   5945 S  SG  . CYS C  1 202 ? 32.240  10.668  -35.869 1.00 10.85 ? 202 CYS C SG  1 
ATOM   5946 N  N   . ASN C  1 203 ? 36.519  10.854  -38.902 1.00 11.40 ? 203 ASN C N   1 
ATOM   5947 C  CA  . ASN C  1 203 ? 37.074  10.961  -40.244 1.00 10.71 ? 203 ASN C CA  1 
ATOM   5948 C  C   . ASN C  1 203 ? 36.997  9.639   -40.990 1.00 11.00 ? 203 ASN C C   1 
ATOM   5949 O  O   . ASN C  1 203 ? 37.264  8.596   -40.413 1.00 10.61 ? 203 ASN C O   1 
ATOM   5950 C  CB  . ASN C  1 203 ? 38.539  11.428  -40.173 1.00 13.55 ? 203 ASN C CB  1 
ATOM   5951 C  CG  . ASN C  1 203 ? 38.677  12.669  -39.299 1.00 15.00 ? 203 ASN C CG  1 
ATOM   5952 O  OD1 . ASN C  1 203 ? 38.709  12.559  -38.077 1.00 18.58 ? 203 ASN C OD1 1 
ATOM   5953 N  ND2 . ASN C  1 203 ? 38.581  13.818  -39.922 1.00 19.59 ? 203 ASN C ND2 1 
ATOM   5954 N  N   . PRO C  1 204 ? 36.655  9.710   -42.265 1.00 10.57 ? 204 PRO C N   1 
ATOM   5955 C  CA  . PRO C  1 204 ? 36.458  8.472   -43.109 1.00 11.53 ? 204 PRO C CA  1 
ATOM   5956 C  C   . PRO C  1 204 ? 37.796  8.045   -43.652 1.00 10.69 ? 204 PRO C C   1 
ATOM   5957 O  O   . PRO C  1 204 ? 37.920  7.848   -44.880 1.00 13.72 ? 204 PRO C O   1 
ATOM   5958 C  CB  . PRO C  1 204 ? 35.481  8.939   -44.233 1.00 12.27 ? 204 PRO C CB  1 
ATOM   5959 C  CG  . PRO C  1 204 ? 35.878  10.435  -44.358 1.00 12.29 ? 204 PRO C CG  1 
ATOM   5960 C  CD  . PRO C  1 204 ? 36.212  10.965  -42.961 1.00 12.17 ? 204 PRO C CD  1 
ATOM   5961 N  N   . THR C  1 205 ? 38.742  7.833   -42.777 1.00 10.54 ? 205 THR C N   1 
ATOM   5962 C  CA  . THR C  1 205 ? 40.146  7.629   -43.162 1.00 13.32 ? 205 THR C CA  1 
ATOM   5963 C  C   . THR C  1 205 ? 40.709  6.331   -42.574 1.00 13.00 ? 205 THR C C   1 
ATOM   5964 O  O   . THR C  1 205 ? 41.960  6.092   -42.532 1.00 13.70 ? 205 THR C O   1 
ATOM   5965 C  CB  . THR C  1 205 ? 40.979  8.797   -42.567 1.00 12.27 ? 205 THR C CB  1 
ATOM   5966 O  OG1 . THR C  1 205 ? 40.758  8.842   -41.172 1.00 14.24 ? 205 THR C OG1 1 
ATOM   5967 C  CG2 . THR C  1 205 ? 40.558  10.130  -43.316 1.00 14.79 ? 205 THR C CG2 1 
ATOM   5968 N  N   . VAL C  1 206 ? 39.838  5.422   -42.102 1.00 11.73 ? 206 VAL C N   1 
ATOM   5969 C  CA  . VAL C  1 206 ? 40.286  4.181   -41.442 1.00 10.56 ? 206 VAL C CA  1 
ATOM   5970 C  C   . VAL C  1 206 ? 40.178  2.931   -42.305 1.00 10.18 ? 206 VAL C C   1 
ATOM   5971 O  O   . VAL C  1 206 ? 39.075  2.605   -42.821 1.00 12.83 ? 206 VAL C O   1 
ATOM   5972 C  CB  . VAL C  1 206 ? 39.496  3.952   -40.100 1.00 10.04 ? 206 VAL C CB  1 
ATOM   5973 C  CG1 . VAL C  1 206 ? 39.924  2.579   -39.516 1.00 10.06 ? 206 VAL C CG1 1 
ATOM   5974 C  CG2 . VAL C  1 206 ? 39.725  5.110   -39.146 1.00 10.28 ? 206 VAL C CG2 1 
ATOM   5975 N  N   . LEU C  1 207 ? 41.270  2.197   -42.496 1.00 9.45  ? 207 LEU C N   1 
ATOM   5976 C  CA  . LEU C  1 207 ? 41.175  0.849   -43.019 1.00 9.86  ? 207 LEU C CA  1 
ATOM   5977 C  C   . LEU C  1 207 ? 40.921  -0.113  -41.880 1.00 9.74  ? 207 LEU C C   1 
ATOM   5978 O  O   . LEU C  1 207 ? 41.810  -0.257  -40.995 1.00 9.95  ? 207 LEU C O   1 
ATOM   5979 C  CB  . LEU C  1 207 ? 42.523  0.573   -43.724 1.00 12.45 ? 207 LEU C CB  1 
ATOM   5980 C  CG  . LEU C  1 207 ? 42.506  -0.709  -44.539 1.00 16.38 ? 207 LEU C CG  1 
ATOM   5981 C  CD1 . LEU C  1 207 ? 41.665  -0.529  -45.823 1.00 21.20 ? 207 LEU C CD1 1 
ATOM   5982 C  CD2 . LEU C  1 207 ? 43.926  -0.979  -45.032 1.00 24.59 ? 207 LEU C CD2 1 
ATOM   5983 N  N   . TRP C  1 208 ? 39.739  -0.699  -41.833 1.00 8.82  ? 208 TRP C N   1 
ATOM   5984 C  CA  . TRP C  1 208 ? 39.382  -1.610  -40.721 1.00 8.74  ? 208 TRP C CA  1 
ATOM   5985 C  C   . TRP C  1 208 ? 39.750  -3.023  -40.966 1.00 9.51  ? 208 TRP C C   1 
ATOM   5986 O  O   . TRP C  1 208 ? 39.556  -3.547  -42.108 1.00 10.15 ? 208 TRP C O   1 
ATOM   5987 C  CB  . TRP C  1 208 ? 37.833  -1.568  -40.520 1.00 8.51  ? 208 TRP C CB  1 
ATOM   5988 C  CG  . TRP C  1 208 ? 37.406  -0.347  -39.750 1.00 8.31  ? 208 TRP C CG  1 
ATOM   5989 C  CD1 . TRP C  1 208 ? 36.933  0.849   -40.204 1.00 8.90  ? 208 TRP C CD1 1 
ATOM   5990 C  CD2 . TRP C  1 208 ? 37.523  -0.197  -38.288 1.00 8.01  ? 208 TRP C CD2 1 
ATOM   5991 N  NE1 . TRP C  1 208 ? 36.748  1.685   -39.179 1.00 9.07  ? 208 TRP C NE1 1 
ATOM   5992 C  CE2 . TRP C  1 208 ? 37.103  1.124   -38.020 1.00 8.17  ? 208 TRP C CE2 1 
ATOM   5993 C  CE3 . TRP C  1 208 ? 37.924  -1.025  -37.252 1.00 9.81  ? 208 TRP C CE3 1 
ATOM   5994 C  CZ2 . TRP C  1 208 ? 37.079  1.648   -36.704 1.00 9.23  ? 208 TRP C CZ2 1 
ATOM   5995 C  CZ3 . TRP C  1 208 ? 37.843  -0.537  -35.925 1.00 9.50  ? 208 TRP C CZ3 1 
ATOM   5996 C  CH2 . TRP C  1 208 ? 37.436  0.799   -35.660 1.00 9.91  ? 208 TRP C CH2 1 
ATOM   5997 N  N   . THR C  1 209 ? 40.321  -3.656  -39.958 1.00 9.72  ? 209 THR C N   1 
ATOM   5998 C  CA  . THR C  1 209 ? 40.504  -5.122  -39.922 1.00 9.66  ? 209 THR C CA  1 
ATOM   5999 C  C   . THR C  1 209 ? 39.842  -5.634  -38.708 1.00 11.33 ? 209 THR C C   1 
ATOM   6000 O  O   . THR C  1 209 ? 40.299  -5.248  -37.570 1.00 11.90 ? 209 THR C O   1 
ATOM   6001 C  CB  . THR C  1 209 ? 42.026  -5.460  -39.904 1.00 10.25 ? 209 THR C CB  1 
ATOM   6002 O  OG1 . THR C  1 209 ? 42.628  -4.901  -41.083 1.00 10.45 ? 209 THR C OG1 1 
ATOM   6003 C  CG2 . THR C  1 209 ? 42.268  -6.984  -39.873 1.00 10.70 ? 209 THR C CG2 1 
ATOM   6004 N  N   . VAL C  1 210 ? 38.763  -6.435  -38.895 1.00 10.41 ? 210 VAL C N   1 
ATOM   6005 C  CA  . VAL C  1 210 ? 38.065  -6.944  -37.706 1.00 9.83  ? 210 VAL C CA  1 
ATOM   6006 C  C   . VAL C  1 210 ? 38.371  -8.416  -37.713 1.00 11.23 ? 210 VAL C C   1 
ATOM   6007 O  O   . VAL C  1 210 ? 37.992  -9.137  -38.646 1.00 11.29 ? 210 VAL C O   1 
ATOM   6008 C  CB  . VAL C  1 210 ? 36.543  -6.728  -37.769 1.00 9.61  ? 210 VAL C CB  1 
ATOM   6009 C  CG1 . VAL C  1 210 ? 35.809  -7.275  -36.514 1.00 10.34 ? 210 VAL C CG1 1 
ATOM   6010 C  CG2 . VAL C  1 210 ? 36.208  -5.258  -37.998 1.00 11.29 ? 210 VAL C CG2 1 
ATOM   6011 N  N   . PHE C  1 211 ? 39.015  -8.911  -36.633 1.00 10.65 ? 211 PHE C N   1 
ATOM   6012 C  CA  . PHE C  1 211 ? 39.305  -10.363 -36.712 1.00 11.82 ? 211 PHE C CA  1 
ATOM   6013 C  C   . PHE C  1 211 ? 38.045  -11.189 -36.648 1.00 13.19 ? 211 PHE C C   1 
ATOM   6014 O  O   . PHE C  1 211 ? 37.109  -10.863 -35.884 1.00 12.89 ? 211 PHE C O   1 
ATOM   6015 C  CB  . PHE C  1 211 ? 40.374  -10.775 -35.661 1.00 12.38 ? 211 PHE C CB  1 
ATOM   6016 C  CG  . PHE C  1 211 ? 41.699  -10.106 -35.890 1.00 11.40 ? 211 PHE C CG  1 
ATOM   6017 C  CD1 . PHE C  1 211 ? 42.526  -10.542 -36.931 1.00 13.29 ? 211 PHE C CD1 1 
ATOM   6018 C  CD2 . PHE C  1 211 ? 42.122  -9.069  -35.076 1.00 13.60 ? 211 PHE C CD2 1 
ATOM   6019 C  CE1 . PHE C  1 211 ? 43.754  -9.844  -37.150 1.00 14.66 ? 211 PHE C CE1 1 
ATOM   6020 C  CE2 . PHE C  1 211 ? 43.339  -8.380  -35.308 1.00 13.40 ? 211 PHE C CE2 1 
ATOM   6021 C  CZ  . PHE C  1 211 ? 44.138  -8.783  -36.354 1.00 13.14 ? 211 PHE C CZ  1 
ATOM   6022 N  N   . ARG C  1 212 ? 38.005  -12.275 -37.398 1.00 13.27 ? 212 ARG C N   1 
ATOM   6023 C  CA  . ARG C  1 212 ? 36.862  -13.186 -37.348 1.00 14.31 ? 212 ARG C CA  1 
ATOM   6024 C  C   . ARG C  1 212 ? 36.560  -13.755 -35.938 1.00 14.06 ? 212 ARG C C   1 
ATOM   6025 O  O   . ARG C  1 212 ? 35.413  -13.776 -35.520 1.00 15.88 ? 212 ARG C O   1 
ATOM   6026 C  CB  . ARG C  1 212 ? 37.081  -14.353 -38.344 1.00 15.01 ? 212 ARG C CB  1 
ATOM   6027 C  CG  . ARG C  1 212 ? 35.790  -15.155 -38.627 1.00 17.91 ? 212 ARG C CG  1 
ATOM   6028 C  CD  . ARG C  1 212 ? 36.267  -16.463 -39.222 1.00 24.53 ? 212 ARG C CD  1 
ATOM   6029 N  NE  . ARG C  1 212 ? 35.212  -17.460 -39.404 1.00 27.83 ? 212 ARG C NE  1 
ATOM   6030 C  CZ  . ARG C  1 212 ? 35.024  -18.509 -38.608 1.00 31.13 ? 212 ARG C CZ  1 
ATOM   6031 N  NH1 . ARG C  1 212 ? 35.809  -18.698 -37.558 1.00 33.76 ? 212 ARG C NH1 1 
ATOM   6032 N  NH2 . ARG C  1 212 ? 34.045  -19.370 -38.858 1.00 37.15 ? 212 ARG C NH2 1 
ATOM   6033 N  N   . ASN C  1 213 ? 37.619  -14.238 -35.271 1.00 14.35 ? 213 ASN C N   1 
ATOM   6034 C  CA  . ASN C  1 213 ? 37.432  -14.987 -33.987 1.00 15.45 ? 213 ASN C CA  1 
ATOM   6035 C  C   . ASN C  1 213 ? 37.539  -14.052 -32.777 1.00 14.76 ? 213 ASN C C   1 
ATOM   6036 O  O   . ASN C  1 213 ? 38.407  -13.219 -32.711 1.00 14.38 ? 213 ASN C O   1 
ATOM   6037 C  CB  . ASN C  1 213 ? 38.514  -16.107 -33.909 1.00 17.56 ? 213 ASN C CB  1 
ATOM   6038 C  CG  . ASN C  1 213 ? 38.458  -16.985 -35.139 1.00 19.54 ? 213 ASN C CG  1 
ATOM   6039 O  OD1 . ASN C  1 213 ? 37.373  -17.483 -35.533 1.00 23.24 ? 213 ASN C OD1 1 
ATOM   6040 N  ND2 . ASN C  1 213 ? 39.588  -17.138 -35.816 1.00 20.35 ? 213 ASN C ND2 1 
ATOM   6041 N  N   . PRO C  1 214 ? 36.623  -14.176 -31.791 1.00 14.95 ? 214 PRO C N   1 
ATOM   6042 C  CA  . PRO C  1 214 ? 36.677  -13.347 -30.621 1.00 16.07 ? 214 PRO C CA  1 
ATOM   6043 C  C   . PRO C  1 214 ? 37.742  -13.831 -29.602 1.00 16.56 ? 214 PRO C C   1 
ATOM   6044 O  O   . PRO C  1 214 ? 38.231  -14.992 -29.774 1.00 19.01 ? 214 PRO C O   1 
ATOM   6045 C  CB  . PRO C  1 214 ? 35.293  -13.524 -29.995 1.00 18.03 ? 214 PRO C CB  1 
ATOM   6046 C  CG  . PRO C  1 214 ? 34.885  -14.895 -30.439 1.00 20.58 ? 214 PRO C CG  1 
ATOM   6047 C  CD  . PRO C  1 214 ? 35.453  -15.072 -31.814 1.00 19.08 ? 214 PRO C CD  1 
ATOM   6048 N  N   . VAL C  1 215 ? 38.160  -12.958 -28.683 1.00 15.12 ? 215 VAL C N   1 
ATOM   6049 C  CA  . VAL C  1 215 ? 38.866  -13.453 -27.488 1.00 16.90 ? 215 VAL C CA  1 
ATOM   6050 C  C   . VAL C  1 215 ? 37.852  -13.541 -26.324 1.00 19.02 ? 215 VAL C C   1 
ATOM   6051 O  O   . VAL C  1 215 ? 36.729  -13.032 -26.395 1.00 18.79 ? 215 VAL C O   1 
ATOM   6052 C  CB  . VAL C  1 215 ? 39.994  -12.546 -27.059 1.00 18.26 ? 215 VAL C CB  1 
ATOM   6053 C  CG1 . VAL C  1 215 ? 41.128  -12.501 -28.135 1.00 19.75 ? 215 VAL C CG1 1 
ATOM   6054 C  CG2 . VAL C  1 215 ? 39.517  -11.153 -26.589 1.00 16.16 ? 215 VAL C CG2 1 
ATOM   6055 N  N   . GLN C  1 216 ? 38.290  -14.186 -25.228 1.00 19.75 ? 216 GLN C N   1 
ATOM   6056 C  CA  . GLN C  1 216 ? 37.490  -14.387 -24.003 1.00 20.55 ? 216 GLN C CA  1 
ATOM   6057 C  C   . GLN C  1 216 ? 38.163  -13.718 -22.836 1.00 21.70 ? 216 GLN C C   1 
ATOM   6058 O  O   . GLN C  1 216 ? 39.392  -13.732 -22.716 1.00 21.73 ? 216 GLN C O   1 
ATOM   6059 C  CB  . GLN C  1 216 ? 37.389  -15.852 -23.688 1.00 22.39 ? 216 GLN C CB  1 
ATOM   6060 C  CG  . GLN C  1 216 ? 36.565  -16.673 -24.616 1.00 25.85 ? 216 GLN C CG  1 
ATOM   6061 C  CD  . GLN C  1 216 ? 36.627  -18.142 -24.166 1.00 38.18 ? 216 GLN C CD  1 
ATOM   6062 O  OE1 . GLN C  1 216 ? 36.416  -18.467 -22.984 1.00 38.78 ? 216 GLN C OE1 1 
ATOM   6063 N  NE2 . GLN C  1 216 ? 36.995  -19.034 -25.097 1.00 43.50 ? 216 GLN C NE2 1 
ATOM   6064 N  N   . ILE C  1 217 ? 37.346  -13.055 -22.041 1.00 21.72 ? 217 ILE C N   1 
ATOM   6065 C  CA  . ILE C  1 217 ? 37.650  -12.512 -20.738 1.00 19.72 ? 217 ILE C CA  1 
ATOM   6066 C  C   . ILE C  1 217 ? 36.603  -13.086 -19.738 1.00 20.26 ? 217 ILE C C   1 
ATOM   6067 O  O   . ILE C  1 217 ? 35.501  -13.489 -20.133 1.00 21.62 ? 217 ILE C O   1 
ATOM   6068 C  CB  . ILE C  1 217 ? 37.793  -10.945 -20.687 1.00 19.74 ? 217 ILE C CB  1 
ATOM   6069 C  CG1 . ILE C  1 217 ? 36.435  -10.221 -20.923 1.00 16.67 ? 217 ILE C CG1 1 
ATOM   6070 C  CG2 . ILE C  1 217 ? 38.902  -10.448 -21.667 1.00 20.56 ? 217 ILE C CG2 1 
ATOM   6071 C  CD1 . ILE C  1 217 ? 36.539  -8.768  -20.612 1.00 20.53 ? 217 ILE C CD1 1 
ATOM   6072 N  N   . SER C  1 218 ? 37.010  -13.182 -18.456 1.00 24.84 ? 218 SER C N   1 
ATOM   6073 C  CA  . SER C  1 218 ? 36.085  -13.815 -17.470 1.00 24.44 ? 218 SER C CA  1 
ATOM   6074 C  C   . SER C  1 218 ? 34.941  -12.823 -17.233 1.00 25.75 ? 218 SER C C   1 
ATOM   6075 O  O   . SER C  1 218 ? 35.093  -11.581 -17.457 1.00 24.26 ? 218 SER C O   1 
ATOM   6076 C  CB  . SER C  1 218 ? 36.812  -14.087 -16.134 1.00 21.27 ? 218 SER C CB  1 
ATOM   6077 O  OG  . SER C  1 218 ? 37.220  -12.900 -15.439 1.00 24.57 ? 218 SER C OG  1 
ATOM   6078 N  N   . GLN C  1 219 ? 33.794  -13.339 -16.760 1.00 26.82 ? 219 GLN C N   1 
ATOM   6079 C  CA  . GLN C  1 219 ? 32.817  -12.444 -16.135 1.00 27.59 ? 219 GLN C CA  1 
ATOM   6080 C  C   . GLN C  1 219 ? 33.358  -11.389 -15.191 1.00 24.83 ? 219 GLN C C   1 
ATOM   6081 O  O   . GLN C  1 219 ? 32.898  -10.255 -15.205 1.00 24.28 ? 219 GLN C O   1 
ATOM   6082 C  CB  . GLN C  1 219 ? 31.650  -13.240 -15.461 1.00 35.00 ? 219 GLN C CB  1 
ATOM   6083 N  N   . GLU C  1 220 ? 34.307  -11.727 -14.304 1.00 26.29 ? 220 GLU C N   1 
ATOM   6084 C  CA  . GLU C  1 220 ? 34.787  -10.743 -13.384 1.00 26.33 ? 220 GLU C CA  1 
ATOM   6085 C  C   . GLU C  1 220 ? 35.586  -9.656  -14.054 1.00 19.64 ? 220 GLU C C   1 
ATOM   6086 O  O   . GLU C  1 220 ? 35.553  -8.498  -13.629 1.00 21.48 ? 220 GLU C O   1 
ATOM   6087 C  CB  . GLU C  1 220 ? 35.605  -11.418 -12.237 1.00 29.92 ? 220 GLU C CB  1 
ATOM   6088 C  CG  . GLU C  1 220 ? 34.967  -12.747 -11.735 1.00 39.14 ? 220 GLU C CG  1 
ATOM   6089 C  CD  . GLU C  1 220 ? 35.263  -14.051 -12.554 1.00 43.78 ? 220 GLU C CD  1 
ATOM   6090 O  OE1 . GLU C  1 220 ? 34.513  -14.473 -13.485 1.00 38.52 ? 220 GLU C OE1 1 
ATOM   6091 O  OE2 . GLU C  1 220 ? 36.244  -14.744 -12.214 1.00 58.31 ? 220 GLU C OE2 1 
ATOM   6092 N  N   . GLN C  1 221 ? 36.394  -10.049 -15.066 1.00 23.37 ? 221 GLN C N   1 
ATOM   6093 C  CA  . GLN C  1 221 ? 37.159  -9.045  -15.860 1.00 21.02 ? 221 GLN C CA  1 
ATOM   6094 C  C   . GLN C  1 221 ? 36.212  -8.092  -16.616 1.00 15.92 ? 221 GLN C C   1 
ATOM   6095 O  O   . GLN C  1 221 ? 36.382  -6.887  -16.510 1.00 18.06 ? 221 GLN C O   1 
ATOM   6096 C  CB  . GLN C  1 221 ? 38.102  -9.689  -16.825 1.00 20.41 ? 221 GLN C CB  1 
ATOM   6097 C  CG  . GLN C  1 221 ? 39.331  -10.315 -16.123 1.00 18.56 ? 221 GLN C CG  1 
ATOM   6098 C  CD  . GLN C  1 221 ? 40.219  -10.901 -17.150 1.00 18.33 ? 221 GLN C CD  1 
ATOM   6099 O  OE1 . GLN C  1 221 ? 39.776  -11.865 -17.795 1.00 19.32 ? 221 GLN C OE1 1 
ATOM   6100 N  NE2 . GLN C  1 221 ? 41.444  -10.430 -17.245 1.00 20.95 ? 221 GLN C NE2 1 
ATOM   6101 N  N   . LEU C  1 222 ? 35.176  -8.694  -17.223 1.00 18.68 ? 222 LEU C N   1 
ATOM   6102 C  CA  . LEU C  1 222 ? 34.095  -7.859  -17.888 1.00 16.86 ? 222 LEU C CA  1 
ATOM   6103 C  C   . LEU C  1 222 ? 33.385  -6.855  -16.967 1.00 15.69 ? 222 LEU C C   1 
ATOM   6104 O  O   . LEU C  1 222 ? 33.319  -5.633  -17.174 1.00 16.90 ? 222 LEU C O   1 
ATOM   6105 C  CB  . LEU C  1 222 ? 33.092  -8.710  -18.593 1.00 17.70 ? 222 LEU C CB  1 
ATOM   6106 C  CG  . LEU C  1 222 ? 32.050  -7.900  -19.415 1.00 17.74 ? 222 LEU C CG  1 
ATOM   6107 C  CD1 . LEU C  1 222 ? 32.708  -6.991  -20.465 1.00 18.40 ? 222 LEU C CD1 1 
ATOM   6108 C  CD2 . LEU C  1 222 ? 31.118  -8.948  -20.040 1.00 18.94 ? 222 LEU C CD2 1 
ATOM   6109 N  N   . LEU C  1 223 ? 32.920  -7.361  -15.775 1.00 19.81 ? 223 LEU C N   1 
ATOM   6110 C  CA  . LEU C  1 223 ? 32.383  -6.504  -14.715 1.00 19.76 ? 223 LEU C CA  1 
ATOM   6111 C  C   . LEU C  1 223 ? 33.254  -5.394  -14.231 1.00 16.99 ? 223 LEU C C   1 
ATOM   6112 O  O   . LEU C  1 223 ? 32.871  -4.231  -14.034 1.00 18.06 ? 223 LEU C O   1 
ATOM   6113 C  CB  . LEU C  1 223 ? 31.939  -7.423  -13.564 1.00 23.28 ? 223 LEU C CB  1 
ATOM   6114 C  CG  . LEU C  1 223 ? 31.042  -6.676  -12.601 1.00 27.65 ? 223 LEU C CG  1 
ATOM   6115 C  CD1 . LEU C  1 223 ? 29.813  -6.017  -13.252 1.00 25.07 ? 223 LEU C CD1 1 
ATOM   6116 C  CD2 . LEU C  1 223 ? 30.632  -7.651  -11.493 1.00 28.98 ? 223 LEU C CD2 1 
ATOM   6117 N  N   . ALA C  1 224 ? 34.533  -5.745  -14.049 1.00 18.53 ? 224 ALA C N   1 
ATOM   6118 C  CA  . ALA C  1 224 ? 35.559  -4.803  -13.658 1.00 19.21 ? 224 ALA C CA  1 
ATOM   6119 C  C   . ALA C  1 224 ? 35.686  -3.667  -14.661 1.00 16.29 ? 224 ALA C C   1 
ATOM   6120 O  O   . ALA C  1 224 ? 35.652  -2.455  -14.342 1.00 19.29 ? 224 ALA C O   1 
ATOM   6121 C  CB  . ALA C  1 224 ? 36.934  -5.560  -13.505 1.00 22.94 ? 224 ALA C CB  1 
ATOM   6122 N  N   . LEU C  1 225 ? 35.767  -4.086  -15.956 1.00 16.68 ? 225 LEU C N   1 
ATOM   6123 C  CA  . LEU C  1 225 ? 35.884  -3.037  -16.988 1.00 18.47 ? 225 LEU C CA  1 
ATOM   6124 C  C   . LEU C  1 225 ? 34.660  -2.164  -16.994 1.00 15.01 ? 225 LEU C C   1 
ATOM   6125 O  O   . LEU C  1 225 ? 34.776  -0.956  -17.149 1.00 17.74 ? 225 LEU C O   1 
ATOM   6126 C  CB  . LEU C  1 225 ? 36.058  -3.683  -18.370 1.00 17.76 ? 225 LEU C CB  1 
ATOM   6127 C  CG  . LEU C  1 225 ? 36.115  -2.765  -19.591 1.00 16.62 ? 225 LEU C CG  1 
ATOM   6128 C  CD1 . LEU C  1 225 ? 37.373  -1.907  -19.481 1.00 18.66 ? 225 LEU C CD1 1 
ATOM   6129 C  CD2 . LEU C  1 225 ? 36.160  -3.609  -20.807 1.00 16.09 ? 225 LEU C CD2 1 
ATOM   6130 N  N   . GLU C  1 226 ? 33.457  -2.791  -16.860 1.00 16.17 ? 226 GLU C N   1 
ATOM   6131 C  CA  . GLU C  1 226 ? 32.207  -1.991  -16.913 1.00 17.65 ? 226 GLU C CA  1 
ATOM   6132 C  C   . GLU C  1 226 ? 31.933  -1.075  -15.743 1.00 19.12 ? 226 GLU C C   1 
ATOM   6133 O  O   . GLU C  1 226 ? 31.099  -0.164  -15.793 1.00 20.25 ? 226 GLU C O   1 
ATOM   6134 C  CB  . GLU C  1 226 ? 31.012  -2.936  -17.009 1.00 16.80 ? 226 GLU C CB  1 
ATOM   6135 C  CG  . GLU C  1 226 ? 30.963  -3.690  -18.370 1.00 16.80 ? 226 GLU C CG  1 
ATOM   6136 C  CD  . GLU C  1 226 ? 30.052  -4.898  -18.290 1.00 17.77 ? 226 GLU C CD  1 
ATOM   6137 O  OE1 . GLU C  1 226 ? 29.761  -5.348  -17.161 1.00 19.81 ? 226 GLU C OE1 1 
ATOM   6138 O  OE2 . GLU C  1 226 ? 29.629  -5.396  -19.353 1.00 18.46 ? 226 GLU C OE2 1 
ATOM   6139 N  N   . THR C  1 227 ? 32.645  -1.329  -14.638 1.00 18.94 ? 227 THR C N   1 
ATOM   6140 C  CA  . THR C  1 227 ? 32.275  -0.662  -13.338 1.00 19.27 ? 227 THR C CA  1 
ATOM   6141 C  C   . THR C  1 227 ? 33.428  0.170   -12.751 1.00 22.01 ? 227 THR C C   1 
ATOM   6142 O  O   . THR C  1 227 ? 33.226  0.815   -11.722 1.00 23.62 ? 227 THR C O   1 
ATOM   6143 C  CB  . THR C  1 227 ? 31.754  -1.699  -12.256 1.00 18.09 ? 227 THR C CB  1 
ATOM   6144 O  OG1 . THR C  1 227 ? 32.777  -2.667  -11.990 1.00 21.18 ? 227 THR C OG1 1 
ATOM   6145 C  CG2 . THR C  1 227 ? 30.447  -2.376  -12.738 1.00 23.29 ? 227 THR C CG2 1 
ATOM   6146 N  N   . ALA C  1 228 ? 34.575  0.159   -13.416 1.00 20.00 ? 228 ALA C N   1 
ATOM   6147 C  CA  . ALA C  1 228 ? 35.789  0.744   -12.833 1.00 18.23 ? 228 ALA C CA  1 
ATOM   6148 C  C   . ALA C  1 228 ? 35.870  2.248   -13.015 1.00 22.06 ? 228 ALA C C   1 
ATOM   6149 O  O   . ALA C  1 228 ? 36.452  2.961   -12.189 1.00 20.69 ? 228 ALA C O   1 
ATOM   6150 C  CB  . ALA C  1 228 ? 37.084  0.059   -13.316 1.00 21.02 ? 228 ALA C CB  1 
ATOM   6151 N  N   . LEU C  1 229 ? 35.344  2.802   -14.128 1.00 16.31 ? 229 LEU C N   1 
ATOM   6152 C  CA  . LEU C  1 229 ? 35.625  4.181   -14.513 1.00 18.29 ? 229 LEU C CA  1 
ATOM   6153 C  C   . LEU C  1 229 ? 34.466  5.081   -14.562 1.00 18.95 ? 229 LEU C C   1 
ATOM   6154 O  O   . LEU C  1 229 ? 33.295  4.701   -14.829 1.00 17.02 ? 229 LEU C O   1 
ATOM   6155 C  CB  . LEU C  1 229 ? 36.286  4.242   -15.906 1.00 16.33 ? 229 LEU C CB  1 
ATOM   6156 C  CG  . LEU C  1 229 ? 37.394  3.211   -16.157 1.00 15.30 ? 229 LEU C CG  1 
ATOM   6157 C  CD1 . LEU C  1 229 ? 37.904  3.355   -17.617 1.00 18.78 ? 229 LEU C CD1 1 
ATOM   6158 C  CD2 . LEU C  1 229 ? 38.581  3.381   -15.195 1.00 16.43 ? 229 LEU C CD2 1 
ATOM   6159 N  N   . TYR C  1 230 ? 34.737  6.314   -14.250 1.00 21.83 ? 230 TYR C N   1 
ATOM   6160 C  CA  . TYR C  1 230 ? 33.803  7.327   -14.470 1.00 22.61 ? 230 TYR C CA  1 
ATOM   6161 C  C   . TYR C  1 230 ? 34.232  8.108   -15.677 1.00 23.41 ? 230 TYR C C   1 
ATOM   6162 O  O   . TYR C  1 230 ? 35.392  8.141   -16.050 1.00 26.55 ? 230 TYR C O   1 
ATOM   6163 C  CB  . TYR C  1 230 ? 33.782  8.315   -13.283 1.00 24.92 ? 230 TYR C CB  1 
ATOM   6164 C  CG  . TYR C  1 230 ? 33.372  7.768   -11.953 1.00 29.45 ? 230 TYR C CG  1 
ATOM   6165 C  CD1 . TYR C  1 230 ? 32.004  7.654   -11.580 1.00 28.97 ? 230 TYR C CD1 1 
ATOM   6166 C  CD2 . TYR C  1 230 ? 34.348  7.461   -11.012 1.00 30.27 ? 230 TYR C CD2 1 
ATOM   6167 C  CE1 . TYR C  1 230 ? 31.652  7.233   -10.297 1.00 32.58 ? 230 TYR C CE1 1 
ATOM   6168 C  CE2 . TYR C  1 230 ? 34.014  7.061   -9.713  1.00 33.72 ? 230 TYR C CE2 1 
ATOM   6169 C  CZ  . TYR C  1 230 ? 32.682  6.960   -9.358  1.00 33.58 ? 230 TYR C CZ  1 
ATOM   6170 O  OH  . TYR C  1 230 ? 32.434  6.547   -8.041  1.00 34.35 ? 230 TYR C OH  1 
ATOM   6171 N  N   A CYS C  1 231 ? 33.247  8.776   -16.269 0.50 22.93 ? 231 CYS C N   1 
ATOM   6172 N  N   B CYS C  1 231 ? 33.281  8.790   -16.296 0.50 24.27 ? 231 CYS C N   1 
ATOM   6173 C  CA  A CYS C  1 231 ? 33.477  9.632   -17.400 0.50 23.30 ? 231 CYS C CA  1 
ATOM   6174 C  CA  B CYS C  1 231 ? 33.620  9.684   -17.366 0.50 25.37 ? 231 CYS C CA  1 
ATOM   6175 C  C   A CYS C  1 231 ? 33.541  11.125  -16.972 0.50 25.03 ? 231 CYS C C   1 
ATOM   6176 C  C   B CYS C  1 231 ? 34.108  11.003  -16.837 0.50 27.79 ? 231 CYS C C   1 
ATOM   6177 O  O   A CYS C  1 231 ? 33.630  12.011  -17.787 0.50 23.89 ? 231 CYS C O   1 
ATOM   6178 O  O   B CYS C  1 231 ? 34.886  11.682  -17.515 0.50 27.64 ? 231 CYS C O   1 
ATOM   6179 C  CB  A CYS C  1 231 ? 32.408  9.379   -18.486 0.50 21.45 ? 231 CYS C CB  1 
ATOM   6180 C  CB  B CYS C  1 231 ? 32.380  10.046  -18.160 0.50 24.40 ? 231 CYS C CB  1 
ATOM   6181 S  SG  A CYS C  1 231 ? 30.680  9.780   -18.099 0.50 20.42 ? 231 CYS C SG  1 
ATOM   6182 S  SG  B CYS C  1 231 ? 32.049  8.950   -19.511 0.50 23.37 ? 231 CYS C SG  1 
ATOM   6183 N  N   . THR C  1 232 ? 33.554  11.382  -15.669 1.00 25.64 ? 232 THR C N   1 
ATOM   6184 C  CA  . THR C  1 232 ? 33.617  12.760  -15.139 1.00 24.65 ? 232 THR C CA  1 
ATOM   6185 C  C   . THR C  1 232 ? 34.956  13.002  -14.357 1.00 26.21 ? 232 THR C C   1 
ATOM   6186 O  O   . THR C  1 232 ? 35.654  12.055  -13.966 1.00 21.64 ? 232 THR C O   1 
ATOM   6187 C  CB  . THR C  1 232 ? 32.438  12.975  -14.223 1.00 26.10 ? 232 THR C CB  1 
ATOM   6188 O  OG1 . THR C  1 232 ? 32.297  11.783  -13.403 1.00 25.09 ? 232 THR C OG1 1 
ATOM   6189 C  CG2 . THR C  1 232 ? 31.161  13.260  -15.040 1.00 27.62 ? 232 THR C CG2 1 
ATOM   6190 N  N   . HIS C  1 233 ? 35.304  14.290  -14.116 1.00 26.81 ? 233 HIS C N   1 
ATOM   6191 C  CA  . HIS C  1 233 ? 36.555  14.634  -13.323 1.00 27.33 ? 233 HIS C CA  1 
ATOM   6192 C  C   . HIS C  1 233 ? 36.320  14.319  -11.869 1.00 23.92 ? 233 HIS C C   1 
ATOM   6193 O  O   . HIS C  1 233 ? 35.166  14.242  -11.392 1.00 27.16 ? 233 HIS C O   1 
ATOM   6194 C  CB  . HIS C  1 233 ? 36.929  16.104  -13.467 1.00 31.00 ? 233 HIS C CB  1 
ATOM   6195 C  CG  . HIS C  1 233 ? 37.605  16.410  -14.789 1.00 34.45 ? 233 HIS C CG  1 
ATOM   6196 N  ND1 . HIS C  1 233 ? 36.917  16.804  -15.899 1.00 39.52 ? 233 HIS C ND1 1 
ATOM   6197 C  CD2 . HIS C  1 233 ? 38.937  16.351  -15.157 1.00 36.08 ? 233 HIS C CD2 1 
ATOM   6198 C  CE1 . HIS C  1 233 ? 37.787  16.998  -16.908 1.00 33.73 ? 233 HIS C CE1 1 
ATOM   6199 N  NE2 . HIS C  1 233 ? 39.015  16.727  -16.460 1.00 41.13 ? 233 HIS C NE2 1 
ATOM   6200 N  N   . MET C  1 234 ? 37.395  14.003  -11.180 1.00 30.90 ? 234 MET C N   1 
ATOM   6201 C  CA  . MET C  1 234 ? 37.344  13.655  -9.755  1.00 34.44 ? 234 MET C CA  1 
ATOM   6202 C  C   . MET C  1 234 ? 36.550  14.700  -8.914  1.00 41.42 ? 234 MET C C   1 
ATOM   6203 O  O   . MET C  1 234 ? 35.617  14.356  -8.153  1.00 43.08 ? 234 MET C O   1 
ATOM   6204 C  CB  . MET C  1 234 ? 38.760  13.521  -9.242  1.00 34.44 ? 234 MET C CB  1 
ATOM   6205 C  CG  . MET C  1 234 ? 38.845  13.027  -7.806  1.00 38.52 ? 234 MET C CG  1 
ATOM   6206 S  SD  . MET C  1 234 ? 40.515  13.213  -7.170  1.00 45.42 ? 234 MET C SD  1 
ATOM   6207 C  CE  . MET C  1 234 ? 41.105  11.521  -7.248  1.00 34.95 ? 234 MET C CE  1 
ATOM   6208 N  N   . ASP C  1 235 ? 36.871  15.963  -9.129  1.00 44.66 ? 235 ASP C N   1 
ATOM   6209 C  CA  . ASP C  1 235 ? 36.128  17.080  -8.548  1.00 48.27 ? 235 ASP C CA  1 
ATOM   6210 C  C   . ASP C  1 235 ? 34.586  17.067  -8.675  1.00 48.58 ? 235 ASP C C   1 
ATOM   6211 O  O   . ASP C  1 235 ? 33.930  17.517  -7.754  1.00 50.31 ? 235 ASP C O   1 
ATOM   6212 C  CB  . ASP C  1 235 ? 36.673  18.406  -9.088  1.00 63.91 ? 235 ASP C CB  1 
ATOM   6213 N  N   . ASP C  1 236 ? 34.032  16.585  -9.800  1.00 44.01 ? 236 ASP C N   1 
ATOM   6214 C  CA  . ASP C  1 236 ? 32.578  16.621  -10.131 1.00 45.25 ? 236 ASP C CA  1 
ATOM   6215 C  C   . ASP C  1 236 ? 31.593  16.039  -9.054  1.00 46.96 ? 236 ASP C C   1 
ATOM   6216 O  O   . ASP C  1 236 ? 31.625  14.827  -8.767  1.00 44.16 ? 236 ASP C O   1 
ATOM   6217 C  CB  . ASP C  1 236 ? 32.343  15.952  -11.520 1.00 38.87 ? 236 ASP C CB  1 
ATOM   6218 C  CG  . ASP C  1 236 ? 31.064  16.418  -12.193 1.00 41.41 ? 236 ASP C CG  1 
ATOM   6219 O  OD1 . ASP C  1 236 ? 30.144  16.881  -11.469 1.00 48.38 ? 236 ASP C OD1 1 
ATOM   6220 O  OD2 . ASP C  1 236 ? 30.947  16.341  -13.456 1.00 37.26 ? 236 ASP C OD2 1 
ATOM   6221 N  N   . PRO C  1 237 ? 30.705  16.899  -8.454  1.00 52.58 ? 237 PRO C N   1 
ATOM   6222 C  CA  . PRO C  1 237 ? 29.734  16.395  -7.441  1.00 49.83 ? 237 PRO C CA  1 
ATOM   6223 C  C   . PRO C  1 237 ? 28.563  15.555  -8.046  1.00 47.16 ? 237 PRO C C   1 
ATOM   6224 O  O   . PRO C  1 237 ? 27.741  14.991  -7.294  1.00 42.78 ? 237 PRO C O   1 
ATOM   6225 C  CB  . PRO C  1 237 ? 29.203  17.683  -6.765  1.00 52.00 ? 237 PRO C CB  1 
ATOM   6226 C  CG  . PRO C  1 237 ? 29.984  18.817  -7.359  1.00 52.05 ? 237 PRO C CG  1 
ATOM   6227 C  CD  . PRO C  1 237 ? 30.546  18.351  -8.668  1.00 50.29 ? 237 PRO C CD  1 
ATOM   6228 N  N   . SER C  1 238 ? 28.498  15.481  -9.380  1.00 43.48 ? 238 SER C N   1 
ATOM   6229 C  CA  . SER C  1 238 ? 27.541  14.588  -10.046 1.00 42.96 ? 238 SER C CA  1 
ATOM   6230 C  C   . SER C  1 238 ? 28.252  13.595  -10.950 1.00 35.38 ? 238 SER C C   1 
ATOM   6231 O  O   . SER C  1 238 ? 28.182  13.726  -12.163 1.00 33.03 ? 238 SER C O   1 
ATOM   6232 C  CB  . SER C  1 238 ? 26.508  15.387  -10.851 1.00 46.98 ? 238 SER C CB  1 
ATOM   6233 O  OG  . SER C  1 238 ? 25.778  16.268  -9.997  1.00 51.73 ? 238 SER C OG  1 
ATOM   6234 N  N   . PRO C  1 239 ? 28.931  12.592  -10.369 1.00 34.49 ? 239 PRO C N   1 
ATOM   6235 C  CA  . PRO C  1 239 ? 29.735  11.696  -11.189 1.00 30.60 ? 239 PRO C CA  1 
ATOM   6236 C  C   . PRO C  1 239 ? 28.873  10.828  -12.111 1.00 32.93 ? 239 PRO C C   1 
ATOM   6237 O  O   . PRO C  1 239 ? 27.724  10.485  -11.774 1.00 33.83 ? 239 PRO C O   1 
ATOM   6238 C  CB  . PRO C  1 239 ? 30.423  10.773  -10.154 1.00 32.69 ? 239 PRO C CB  1 
ATOM   6239 C  CG  . PRO C  1 239 ? 29.490  10.800  -8.990  1.00 34.95 ? 239 PRO C CG  1 
ATOM   6240 C  CD  . PRO C  1 239 ? 29.024  12.228  -8.940  1.00 32.72 ? 239 PRO C CD  1 
ATOM   6241 N  N   . ARG C  1 240 ? 29.443  10.453  -13.249 1.00 30.33 ? 240 ARG C N   1 
ATOM   6242 C  CA  . ARG C  1 240 ? 28.733  9.550   -14.146 1.00 29.97 ? 240 ARG C CA  1 
ATOM   6243 C  C   . ARG C  1 240 ? 29.648  8.393   -14.519 1.00 26.64 ? 240 ARG C C   1 
ATOM   6244 O  O   . ARG C  1 240 ? 30.839  8.604   -14.798 1.00 25.88 ? 240 ARG C O   1 
ATOM   6245 C  CB  . ARG C  1 240 ? 28.244  10.313  -15.376 1.00 32.47 ? 240 ARG C CB  1 
ATOM   6246 N  N   . GLU C  1 241 ? 29.074  7.183   -14.521 1.00 23.64 ? 241 GLU C N   1 
ATOM   6247 C  CA  . GLU C  1 241 ? 29.796  5.963   -14.912 1.00 22.46 ? 241 GLU C CA  1 
ATOM   6248 C  C   . GLU C  1 241 ? 30.208  6.022   -16.424 1.00 20.23 ? 241 GLU C C   1 
ATOM   6249 O  O   . GLU C  1 241 ? 29.452  6.550   -17.270 1.00 20.82 ? 241 GLU C O   1 
ATOM   6250 C  CB  . GLU C  1 241 ? 28.940  4.737   -14.695 1.00 25.38 ? 241 GLU C CB  1 
ATOM   6251 C  CG  . GLU C  1 241 ? 28.295  4.709   -13.310 1.00 29.59 ? 241 GLU C CG  1 
ATOM   6252 C  CD  . GLU C  1 241 ? 27.538  3.425   -12.971 1.00 38.82 ? 241 GLU C CD  1 
ATOM   6253 O  OE1 . GLU C  1 241 ? 26.933  2.739   -13.844 1.00 36.04 ? 241 GLU C OE1 1 
ATOM   6254 O  OE2 . GLU C  1 241 ? 27.506  3.100   -11.759 1.00 48.66 ? 241 GLU C OE2 1 
ATOM   6255 N  N   . MET C  1 242 ? 31.425  5.605   -16.702 1.00 17.63 ? 242 MET C N   1 
ATOM   6256 C  CA  . MET C  1 242 ? 31.884  5.300   -18.119 1.00 16.14 ? 242 MET C CA  1 
ATOM   6257 C  C   . MET C  1 242 ? 31.365  3.892   -18.508 1.00 14.97 ? 242 MET C C   1 
ATOM   6258 O  O   . MET C  1 242 ? 31.928  2.852   -18.228 1.00 15.85 ? 242 MET C O   1 
ATOM   6259 C  CB  . MET C  1 242 ? 33.388  5.396   -18.234 1.00 14.37 ? 242 MET C CB  1 
ATOM   6260 C  CG  . MET C  1 242 ? 33.795  5.283   -19.729 1.00 16.59 ? 242 MET C CG  1 
ATOM   6261 S  SD  . MET C  1 242 ? 35.546  5.280   -19.935 1.00 17.90 ? 242 MET C SD  1 
ATOM   6262 C  CE  . MET C  1 242 ? 36.023  6.934   -19.370 1.00 17.83 ? 242 MET C CE  1 
ATOM   6263 N  N   . ILE C  1 243 ? 30.202  3.889   -19.152 1.00 14.99 ? 243 ILE C N   1 
ATOM   6264 C  CA  . ILE C  1 243 ? 29.485  2.707   -19.618 1.00 14.36 ? 243 ILE C CA  1 
ATOM   6265 C  C   . ILE C  1 243 ? 28.910  3.016   -21.006 1.00 13.67 ? 243 ILE C C   1 
ATOM   6266 O  O   . ILE C  1 243 ? 28.706  4.162   -21.350 1.00 13.11 ? 243 ILE C O   1 
ATOM   6267 C  CB  . ILE C  1 243 ? 28.322  2.268   -18.630 1.00 15.00 ? 243 ILE C CB  1 
ATOM   6268 C  CG1 . ILE C  1 243 ? 27.395  3.467   -18.350 1.00 15.42 ? 243 ILE C CG1 1 
ATOM   6269 C  CG2 . ILE C  1 243 ? 28.928  1.601   -17.363 1.00 16.19 ? 243 ILE C CG2 1 
ATOM   6270 C  CD1 . ILE C  1 243 ? 26.187  3.050   -17.489 1.00 17.11 ? 243 ILE C CD1 1 
ATOM   6271 N  N   . ASN C  1 244 ? 28.628  1.924   -21.728 1.00 11.65 ? 244 ASN C N   1 
ATOM   6272 C  CA  . ASN C  1 244 ? 27.912  2.092   -23.054 1.00 12.36 ? 244 ASN C CA  1 
ATOM   6273 C  C   . ASN C  1 244 ? 28.653  3.053   -23.972 1.00 11.96 ? 244 ASN C C   1 
ATOM   6274 O  O   . ASN C  1 244 ? 28.095  3.888   -24.635 1.00 12.53 ? 244 ASN C O   1 
ATOM   6275 C  CB  . ASN C  1 244 ? 26.490  2.559   -22.873 1.00 13.37 ? 244 ASN C CB  1 
ATOM   6276 C  CG  . ASN C  1 244 ? 25.734  1.709   -21.906 1.00 14.41 ? 244 ASN C CG  1 
ATOM   6277 O  OD1 . ASN C  1 244 ? 25.822  0.503   -21.903 1.00 15.56 ? 244 ASN C OD1 1 
ATOM   6278 N  ND2 . ASN C  1 244 ? 24.992  2.442   -21.023 1.00 16.46 ? 244 ASN C ND2 1 
ATOM   6279 N  N   . ASN C  1 245 ? 29.975  2.876   -23.972 1.00 12.07 ? 245 ASN C N   1 
ATOM   6280 C  CA  . ASN C  1 245 ? 30.856  3.857   -24.738 1.00 11.96 ? 245 ASN C CA  1 
ATOM   6281 C  C   . ASN C  1 245 ? 31.181  3.314   -26.124 1.00 10.68 ? 245 ASN C C   1 
ATOM   6282 O  O   . ASN C  1 245 ? 32.336  3.163   -26.546 1.00 13.38 ? 245 ASN C O   1 
ATOM   6283 C  CB  . ASN C  1 245 ? 32.112  4.214   -23.929 1.00 12.39 ? 245 ASN C CB  1 
ATOM   6284 C  CG  . ASN C  1 245 ? 32.980  3.035   -23.632 1.00 13.51 ? 245 ASN C CG  1 
ATOM   6285 O  OD1 . ASN C  1 245 ? 32.601  1.883   -23.574 1.00 13.51 ? 245 ASN C OD1 1 
ATOM   6286 N  ND2 . ASN C  1 245 ? 34.247  3.362   -23.341 1.00 14.62 ? 245 ASN C ND2 1 
ATOM   6287 N  N   . PHE C  1 246 ? 30.113  2.950   -26.861 1.00 10.24 ? 246 PHE C N   1 
ATOM   6288 C  CA  . PHE C  1 246 ? 30.217  2.378   -28.227 1.00 9.92  ? 246 PHE C CA  1 
ATOM   6289 C  C   . PHE C  1 246 ? 29.241  3.151   -29.026 1.00 9.44  ? 246 PHE C C   1 
ATOM   6290 O  O   . PHE C  1 246 ? 28.217  3.661   -28.543 1.00 10.49 ? 246 PHE C O   1 
ATOM   6291 C  CB  . PHE C  1 246 ? 29.870  0.843   -28.224 1.00 10.37 ? 246 PHE C CB  1 
ATOM   6292 C  CG  . PHE C  1 246 ? 28.447  0.497   -27.788 1.00 10.97 ? 246 PHE C CG  1 
ATOM   6293 C  CD1 . PHE C  1 246 ? 27.382  0.413   -28.716 1.00 11.26 ? 246 PHE C CD1 1 
ATOM   6294 C  CD2 . PHE C  1 246 ? 28.163  0.305   -26.412 1.00 11.80 ? 246 PHE C CD2 1 
ATOM   6295 C  CE1 . PHE C  1 246 ? 26.058  0.154   -28.267 1.00 12.23 ? 246 PHE C CE1 1 
ATOM   6296 C  CE2 . PHE C  1 246 ? 26.848  0.054   -25.999 1.00 11.70 ? 246 PHE C CE2 1 
ATOM   6297 C  CZ  . PHE C  1 246 ? 25.802  -0.044  -26.900 1.00 11.69 ? 246 PHE C CZ  1 
ATOM   6298 N  N   . ARG C  1 247 ? 29.535  3.300   -30.303 1.00 8.06  ? 247 ARG C N   1 
ATOM   6299 C  CA  . ARG C  1 247 ? 28.583  3.907   -31.257 1.00 9.27  ? 247 ARG C CA  1 
ATOM   6300 C  C   . ARG C  1 247 ? 27.619  2.905   -31.814 1.00 8.28  ? 247 ARG C C   1 
ATOM   6301 O  O   . ARG C  1 247 ? 28.062  1.752   -32.070 1.00 9.19  ? 247 ARG C O   1 
ATOM   6302 C  CB  . ARG C  1 247 ? 29.426  4.560   -32.401 1.00 9.09  ? 247 ARG C CB  1 
ATOM   6303 C  CG  . ARG C  1 247 ? 28.668  5.591   -33.261 1.00 8.59  ? 247 ARG C CG  1 
ATOM   6304 C  CD  . ARG C  1 247 ? 29.506  6.027   -34.475 1.00 7.97  ? 247 ARG C CD  1 
ATOM   6305 N  NE  . ARG C  1 247 ? 28.888  7.133   -35.124 1.00 8.09  ? 247 ARG C NE  1 
ATOM   6306 C  CZ  . ARG C  1 247 ? 29.416  7.719   -36.228 1.00 8.41  ? 247 ARG C CZ  1 
ATOM   6307 N  NH1 . ARG C  1 247 ? 30.470  7.118   -36.819 1.00 8.94  ? 247 ARG C NH1 1 
ATOM   6308 N  NH2 . ARG C  1 247 ? 28.873  8.870   -36.661 1.00 8.37  ? 247 ARG C NH2 1 
ATOM   6309 N  N   . GLN C  1 248 ? 26.369  3.297   -32.064 1.00 7.97  ? 248 GLN C N   1 
ATOM   6310 C  CA  . GLN C  1 248 ? 25.446  2.417   -32.776 1.00 8.18  ? 248 GLN C CA  1 
ATOM   6311 C  C   . GLN C  1 248 ? 25.911  2.107   -34.201 1.00 8.12  ? 248 GLN C C   1 
ATOM   6312 O  O   . GLN C  1 248 ? 26.618  2.914   -34.808 1.00 9.13  ? 248 GLN C O   1 
ATOM   6313 C  CB  . GLN C  1 248 ? 24.062  3.093   -32.865 1.00 9.45  ? 248 GLN C CB  1 
ATOM   6314 C  CG  . GLN C  1 248 ? 23.381  3.448   -31.525 1.00 8.57  ? 248 GLN C CG  1 
ATOM   6315 C  CD  . GLN C  1 248 ? 23.009  2.243   -30.688 1.00 10.69 ? 248 GLN C CD  1 
ATOM   6316 O  OE1 . GLN C  1 248 ? 23.724  1.860   -29.758 1.00 12.44 ? 248 GLN C OE1 1 
ATOM   6317 N  NE2 . GLN C  1 248 ? 21.895  1.598   -31.053 1.00 13.12 ? 248 GLN C NE2 1 
ATOM   6318 N  N   . VAL C  1 249 ? 25.531  0.965   -34.742 1.00 9.31  ? 249 VAL C N   1 
ATOM   6319 C  CA  . VAL C  1 249 ? 25.925  0.663   -36.103 1.00 10.30 ? 249 VAL C CA  1 
ATOM   6320 C  C   . VAL C  1 249 ? 25.330  1.631   -37.109 1.00 10.65 ? 249 VAL C C   1 
ATOM   6321 O  O   . VAL C  1 249 ? 24.199  2.130   -36.915 1.00 10.39 ? 249 VAL C O   1 
ATOM   6322 C  CB  . VAL C  1 249 ? 25.576  -0.780  -36.527 1.00 11.60 ? 249 VAL C CB  1 
ATOM   6323 C  CG1 . VAL C  1 249 ? 26.401  -1.813  -35.733 1.00 11.82 ? 249 VAL C CG1 1 
ATOM   6324 C  CG2 . VAL C  1 249 ? 24.133  -1.075  -36.382 1.00 12.10 ? 249 VAL C CG2 1 
ATOM   6325 N  N   . GLN C  1 250 ? 26.043  1.838   -38.181 1.00 9.03  ? 250 GLN C N   1 
ATOM   6326 C  CA  . GLN C  1 250 ? 25.657  2.782   -39.218 1.00 9.73  ? 250 GLN C CA  1 
ATOM   6327 C  C   . GLN C  1 250 ? 25.081  2.036   -40.406 1.00 10.08 ? 250 GLN C C   1 
ATOM   6328 O  O   . GLN C  1 250 ? 25.479  0.894   -40.706 1.00 11.43 ? 250 GLN C O   1 
ATOM   6329 C  CB  . GLN C  1 250 ? 26.925  3.505   -39.703 1.00 9.54  ? 250 GLN C CB  1 
ATOM   6330 C  CG  . GLN C  1 250 ? 27.748  4.106   -38.535 1.00 8.61  ? 250 GLN C CG  1 
ATOM   6331 C  CD  . GLN C  1 250 ? 27.061  5.260   -37.879 1.00 8.82  ? 250 GLN C CD  1 
ATOM   6332 O  OE1 . GLN C  1 250 ? 26.815  6.289   -38.581 1.00 10.02 ? 250 GLN C OE1 1 
ATOM   6333 N  NE2 . GLN C  1 250 ? 26.709  5.157   -36.610 1.00 9.09  ? 250 GLN C NE2 1 
ATOM   6334 N  N   . LYS C  1 251 ? 24.251  2.770   -41.207 1.00 9.19  ? 251 LYS C N   1 
ATOM   6335 C  CA  . LYS C  1 251 ? 23.820  2.168   -42.485 1.00 10.19 ? 251 LYS C CA  1 
ATOM   6336 C  C   . LYS C  1 251 ? 25.063  1.923   -43.357 1.00 10.88 ? 251 LYS C C   1 
ATOM   6337 O  O   . LYS C  1 251 ? 26.028  2.732   -43.354 1.00 12.15 ? 251 LYS C O   1 
ATOM   6338 C  CB  . LYS C  1 251 ? 22.823  3.065   -43.198 1.00 10.53 ? 251 LYS C CB  1 
ATOM   6339 C  CG  . LYS C  1 251 ? 21.449  3.092   -42.416 1.00 10.98 ? 251 LYS C CG  1 
ATOM   6340 C  CD  . LYS C  1 251 ? 20.490  4.012   -43.124 1.00 11.64 ? 251 LYS C CD  1 
ATOM   6341 C  CE  . LYS C  1 251 ? 19.027  3.734   -42.710 1.00 9.91  ? 251 LYS C CE  1 
ATOM   6342 N  NZ  . LYS C  1 251 ? 18.848  3.839   -41.187 1.00 9.15  ? 251 LYS C NZ  1 
ATOM   6343 N  N   . PHE C  1 252 ? 24.979  0.864   -44.163 1.00 12.40 ? 252 PHE C N   1 
ATOM   6344 C  CA  . PHE C  1 252 ? 26.078  0.467   -45.030 1.00 11.85 ? 252 PHE C CA  1 
ATOM   6345 C  C   . PHE C  1 252 ? 25.400  -0.151  -46.240 1.00 17.04 ? 252 PHE C C   1 
ATOM   6346 O  O   . PHE C  1 252 ? 24.985  -1.320  -46.148 1.00 22.42 ? 252 PHE C O   1 
ATOM   6347 C  CB  . PHE C  1 252 ? 26.871  -0.614  -44.297 1.00 14.59 ? 252 PHE C CB  1 
ATOM   6348 C  CG  . PHE C  1 252 ? 28.149  -1.064  -44.969 1.00 12.75 ? 252 PHE C CG  1 
ATOM   6349 C  CD1 . PHE C  1 252 ? 29.285  -0.300  -44.862 1.00 11.57 ? 252 PHE C CD1 1 
ATOM   6350 C  CD2 . PHE C  1 252 ? 28.204  -2.345  -45.565 1.00 15.92 ? 252 PHE C CD2 1 
ATOM   6351 C  CE1 . PHE C  1 252 ? 30.502  -0.717  -45.397 1.00 13.38 ? 252 PHE C CE1 1 
ATOM   6352 C  CE2 . PHE C  1 252 ? 29.453  -2.781  -46.092 1.00 15.46 ? 252 PHE C CE2 1 
ATOM   6353 C  CZ  . PHE C  1 252 ? 30.564  -1.983  -45.999 1.00 13.42 ? 252 PHE C CZ  1 
ATOM   6354 N  N   . ASP C  1 253 ? 25.143  0.666   -47.211 1.00 23.28 ? 253 ASP C N   1 
ATOM   6355 C  CA  . ASP C  1 253 ? 24.304  0.274   -48.338 1.00 23.89 ? 253 ASP C CA  1 
ATOM   6356 C  C   . ASP C  1 253 ? 25.054  0.196   -49.628 1.00 18.74 ? 253 ASP C C   1 
ATOM   6357 O  O   . ASP C  1 253 ? 25.906  1.043   -49.906 1.00 20.74 ? 253 ASP C O   1 
ATOM   6358 C  CB  . ASP C  1 253 ? 23.120  1.245   -48.435 1.00 30.93 ? 253 ASP C CB  1 
ATOM   6359 C  CG  . ASP C  1 253 ? 21.969  0.687   -49.276 1.00 36.48 ? 253 ASP C CG  1 
ATOM   6360 O  OD1 . ASP C  1 253 ? 21.523  -0.492  -49.052 1.00 35.85 ? 253 ASP C OD1 1 
ATOM   6361 O  OD2 . ASP C  1 253 ? 21.545  1.443   -50.159 1.00 37.26 ? 253 ASP C OD2 1 
ATOM   6362 N  N   A GLU C  1 254 ? 24.739  -0.871  -50.365 0.50 21.62 ? 254 GLU C N   1 
ATOM   6363 N  N   B GLU C  1 254 ? 24.729  -0.814  -50.415 0.50 21.03 ? 254 GLU C N   1 
ATOM   6364 C  CA  A GLU C  1 254 ? 25.351  -1.213  -51.644 0.50 22.34 ? 254 GLU C CA  1 
ATOM   6365 C  CA  B GLU C  1 254 ? 25.403  -1.013  -51.672 0.50 21.38 ? 254 GLU C CA  1 
ATOM   6366 C  C   A GLU C  1 254 ? 26.878  -1.345  -51.566 0.50 21.44 ? 254 GLU C C   1 
ATOM   6367 C  C   B GLU C  1 254 ? 26.919  -1.050  -51.476 0.50 19.74 ? 254 GLU C C   1 
ATOM   6368 O  O   A GLU C  1 254 ? 27.603  -1.077  -52.540 0.50 24.24 ? 254 GLU C O   1 
ATOM   6369 O  O   B GLU C  1 254 ? 27.669  -0.445  -52.297 0.50 17.19 ? 254 GLU C O   1 
ATOM   6370 C  CB  A GLU C  1 254 ? 24.924  -0.198  -52.722 0.50 25.01 ? 254 GLU C CB  1 
ATOM   6371 C  CB  B GLU C  1 254 ? 25.005  0.098   -52.663 0.50 24.09 ? 254 GLU C CB  1 
ATOM   6372 C  CG  A GLU C  1 254 ? 23.419  -0.217  -52.910 0.50 24.60 ? 254 GLU C CG  1 
ATOM   6373 C  CG  B GLU C  1 254 ? 23.494  0.185   -52.862 0.50 25.26 ? 254 GLU C CG  1 
ATOM   6374 C  CD  A GLU C  1 254 ? 22.938  0.575   -54.120 0.50 28.23 ? 254 GLU C CD  1 
ATOM   6375 C  CD  B GLU C  1 254 ? 22.906  -1.003  -53.631 0.50 28.79 ? 254 GLU C CD  1 
ATOM   6376 O  OE1 A GLU C  1 254 ? 23.729  0.825   -55.046 0.50 30.66 ? 254 GLU C OE1 1 
ATOM   6377 O  OE1 B GLU C  1 254 ? 23.473  -1.424  -54.649 0.50 29.55 ? 254 GLU C OE1 1 
ATOM   6378 O  OE2 A GLU C  1 254 ? 21.752  0.949   -54.138 0.50 30.37 ? 254 GLU C OE2 1 
ATOM   6379 O  OE2 B GLU C  1 254 ? 21.847  -1.515  -53.248 0.50 32.30 ? 254 GLU C OE2 1 
ATOM   6380 N  N   . ARG C  1 255 ? 27.352  -1.710  -50.386 1.00 19.18 ? 255 ARG C N   1 
ATOM   6381 C  CA  . ARG C  1 255 ? 28.799  -1.920  -50.171 1.00 17.73 ? 255 ARG C CA  1 
ATOM   6382 C  C   . ARG C  1 255 ? 29.069  -3.359  -49.660 1.00 16.79 ? 255 ARG C C   1 
ATOM   6383 O  O   . ARG C  1 255 ? 28.182  -4.056  -49.098 1.00 19.23 ? 255 ARG C O   1 
ATOM   6384 C  CB  . ARG C  1 255 ? 29.356  -0.896  -49.158 1.00 16.66 ? 255 ARG C CB  1 
ATOM   6385 C  CG  . ARG C  1 255 ? 29.271  0.557   -49.655 1.00 17.88 ? 255 ARG C CG  1 
ATOM   6386 C  CD  . ARG C  1 255 ? 29.912  1.539   -48.677 1.00 17.03 ? 255 ARG C CD  1 
ATOM   6387 N  NE  . ARG C  1 255 ? 31.304  1.150   -48.463 1.00 17.73 ? 255 ARG C NE  1 
ATOM   6388 C  CZ  . ARG C  1 255 ? 32.009  1.428   -47.373 1.00 18.36 ? 255 ARG C CZ  1 
ATOM   6389 N  NH1 . ARG C  1 255 ? 31.470  2.120   -46.379 1.00 16.83 ? 255 ARG C NH1 1 
ATOM   6390 N  NH2 . ARG C  1 255 ? 33.263  1.021   -47.284 1.00 14.90 ? 255 ARG C NH2 1 
ATOM   6391 N  N   . LEU C  1 256 ? 30.341  -3.786  -49.862 1.00 16.32 ? 256 LEU C N   1 
ATOM   6392 C  CA  . LEU C  1 256 ? 30.774  -5.105  -49.459 1.00 16.22 ? 256 LEU C CA  1 
ATOM   6393 C  C   . LEU C  1 256 ? 31.798  -5.000  -48.251 1.00 14.45 ? 256 LEU C C   1 
ATOM   6394 O  O   . LEU C  1 256 ? 32.465  -3.989  -48.053 1.00 16.03 ? 256 LEU C O   1 
ATOM   6395 C  CB  . LEU C  1 256 ? 31.453  -5.870  -50.613 1.00 18.47 ? 256 LEU C CB  1 
ATOM   6396 C  CG  . LEU C  1 256 ? 30.498  -6.214  -51.764 1.00 24.52 ? 256 LEU C CG  1 
ATOM   6397 C  CD1 . LEU C  1 256 ? 31.309  -6.642  -52.971 1.00 24.41 ? 256 LEU C CD1 1 
ATOM   6398 C  CD2 . LEU C  1 256 ? 29.490  -7.280  -51.410 1.00 23.50 ? 256 LEU C CD2 1 
ATOM   6399 N  N   . VAL C  1 257 ? 31.802  -6.066  -47.468 1.00 16.14 ? 257 VAL C N   1 
ATOM   6400 C  CA  . VAL C  1 257 ? 32.902  -6.271  -46.555 1.00 14.25 ? 257 VAL C CA  1 
ATOM   6401 C  C   . VAL C  1 257 ? 33.698  -7.436  -47.099 1.00 12.44 ? 257 VAL C C   1 
ATOM   6402 O  O   . VAL C  1 257 ? 33.130  -8.551  -47.410 1.00 13.43 ? 257 VAL C O   1 
ATOM   6403 C  CB  . VAL C  1 257 ? 32.397  -6.608  -45.165 1.00 14.04 ? 257 VAL C CB  1 
ATOM   6404 C  CG1 . VAL C  1 257 ? 33.510  -7.037  -44.227 1.00 14.95 ? 257 VAL C CG1 1 
ATOM   6405 C  CG2 . VAL C  1 257 ? 31.636  -5.420  -44.598 1.00 16.65 ? 257 VAL C CG2 1 
ATOM   6406 N  N   . TYR C  1 258 ? 34.989  -7.260  -47.241 1.00 11.47 ? 258 TYR C N   1 
ATOM   6407 C  CA  . TYR C  1 258 ? 35.814  -8.337  -47.886 1.00 13.01 ? 258 TYR C CA  1 
ATOM   6408 C  C   . TYR C  1 258 ? 36.338  -9.229  -46.780 1.00 12.48 ? 258 TYR C C   1 
ATOM   6409 O  O   . TYR C  1 258 ? 36.669  -8.806  -45.656 1.00 14.64 ? 258 TYR C O   1 
ATOM   6410 C  CB  . TYR C  1 258 ? 36.930  -7.661  -48.666 1.00 14.23 ? 258 TYR C CB  1 
ATOM   6411 C  CG  . TYR C  1 258 ? 36.332  -6.794  -49.690 1.00 16.38 ? 258 TYR C CG  1 
ATOM   6412 C  CD1 . TYR C  1 258 ? 35.840  -7.343  -50.879 1.00 17.17 ? 258 TYR C CD1 1 
ATOM   6413 C  CD2 . TYR C  1 258 ? 36.220  -5.425  -49.476 1.00 17.72 ? 258 TYR C CD2 1 
ATOM   6414 C  CE1 . TYR C  1 258 ? 35.232  -6.526  -51.855 1.00 18.57 ? 258 TYR C CE1 1 
ATOM   6415 C  CE2 . TYR C  1 258 ? 35.594  -4.585  -50.426 1.00 18.46 ? 258 TYR C CE2 1 
ATOM   6416 C  CZ  . TYR C  1 258 ? 35.124  -5.122  -51.630 1.00 20.73 ? 258 TYR C CZ  1 
ATOM   6417 O  OH  . TYR C  1 258 ? 34.467  -4.293  -52.620 1.00 23.81 ? 258 TYR C OH  1 
ATOM   6418 N  N   . THR C  1 259 ? 36.442  -10.528 -47.067 1.00 12.11 ? 259 THR C N   1 
ATOM   6419 C  CA  . THR C  1 259 ? 36.891  -11.402 -46.061 1.00 12.76 ? 259 THR C CA  1 
ATOM   6420 C  C   . THR C  1 259 ? 38.150  -12.197 -46.528 1.00 12.57 ? 259 THR C C   1 
ATOM   6421 O  O   . THR C  1 259 ? 38.275  -12.497 -47.733 1.00 13.96 ? 259 THR C O   1 
ATOM   6422 C  CB  . THR C  1 259 ? 35.804  -12.416 -45.701 1.00 13.88 ? 259 THR C CB  1 
ATOM   6423 O  OG1 . THR C  1 259 ? 35.404  -13.206 -46.857 1.00 15.73 ? 259 THR C OG1 1 
ATOM   6424 C  CG2 . THR C  1 259 ? 34.559  -11.737 -45.082 1.00 14.76 ? 259 THR C CG2 1 
ATOM   6425 N  N   . SER C  1 260 ? 39.037  -12.562 -45.561 1.00 13.22 ? 260 SER C N   1 
ATOM   6426 C  CA  . SER C  1 260 ? 40.263  -13.277 -45.945 1.00 14.35 ? 260 SER C CA  1 
ATOM   6427 C  C   . SER C  1 260 ? 39.953  -14.750 -45.980 1.00 18.12 ? 260 SER C C   1 
ATOM   6428 O  O   . SER C  1 260 ? 40.840  -15.561 -46.338 1.00 21.27 ? 260 SER C O   1 
ATOM   6429 C  CB  . SER C  1 260 ? 41.345  -12.947 -44.953 1.00 14.78 ? 260 SER C CB  1 
ATOM   6430 O  OG  . SER C  1 260 ? 40.945  -13.558 -43.749 1.00 15.26 ? 260 SER C OG  1 
ATOM   6431 N  N   . PHE C  1 261 ? 38.754  -15.109 -45.557 1.00 17.44 ? 261 PHE C N   1 
ATOM   6432 C  CA  . PHE C  1 261 ? 38.347  -16.489 -45.414 1.00 19.66 ? 261 PHE C CA  1 
ATOM   6433 C  C   . PHE C  1 261 ? 37.237  -16.727 -46.353 1.00 21.65 ? 261 PHE C C   1 
ATOM   6434 O  O   . PHE C  1 261 ? 36.357  -15.874 -46.716 1.00 22.03 ? 261 PHE C O   1 
ATOM   6435 C  CB  . PHE C  1 261 ? 37.938  -16.860 -43.943 1.00 19.13 ? 261 PHE C CB  1 
ATOM   6436 C  CG  . PHE C  1 261 ? 36.923  -15.917 -43.358 1.00 18.36 ? 261 PHE C CG  1 
ATOM   6437 C  CD1 . PHE C  1 261 ? 35.580  -16.188 -43.436 1.00 17.71 ? 261 PHE C CD1 1 
ATOM   6438 C  CD2 . PHE C  1 261 ? 37.336  -14.722 -42.734 1.00 16.73 ? 261 PHE C CD2 1 
ATOM   6439 C  CE1 . PHE C  1 261 ? 34.649  -15.355 -42.882 1.00 19.76 ? 261 PHE C CE1 1 
ATOM   6440 C  CE2 . PHE C  1 261 ? 36.413  -13.841 -42.195 1.00 15.87 ? 261 PHE C CE2 1 
ATOM   6441 C  CZ  . PHE C  1 261 ? 35.038  -14.137 -42.267 1.00 20.46 ? 261 PHE C CZ  1 
ATOM   6442 N  N   . SER C  1 262 ? 37.225  -17.945 -46.866 1.00 28.05 ? 262 SER C N   1 
ATOM   6443 C  CA  . SER C  1 262 ? 35.933  -18.348 -47.410 1.00 38.96 ? 262 SER C CA  1 
ATOM   6444 C  C   . SER C  1 262 ? 35.666  -19.590 -46.632 1.00 39.37 ? 262 SER C C   1 
ATOM   6445 O  O   . SER C  1 262 ? 36.633  -20.364 -46.456 1.00 52.68 ? 262 SER C O   1 
ATOM   6446 C  CB  . SER C  1 262 ? 36.077  -18.824 -48.811 1.00 38.07 ? 262 SER C CB  1 
ATOM   6447 O  OG  . SER C  1 262 ? 35.030  -19.758 -48.926 1.00 29.98 ? 262 SER C OG  1 
ATOM   6448 N  N   . GLN C  1 263 ? 34.430  -19.847 -46.205 1.00 47.30 ? 263 GLN C N   1 
ATOM   6449 C  CA  . GLN C  1 263 ? 34.240  -20.973 -45.281 1.00 51.48 ? 263 GLN C CA  1 
ATOM   6450 C  C   . GLN C  1 263 ? 34.822  -20.431 -43.941 1.00 54.11 ? 263 GLN C C   1 
ATOM   6451 O  O   . GLN C  1 263 ? 34.490  -19.303 -43.635 1.00 52.88 ? 263 GLN C O   1 
ATOM   6452 C  CB  . GLN C  1 263 ? 34.920  -22.300 -45.822 1.00 38.95 ? 263 GLN C CB  1 
ATOM   6453 C  CG  . GLN C  1 263 ? 36.438  -22.460 -45.515 1.00 35.01 ? 263 GLN C CG  1 
ATOM   6454 C  CD  . GLN C  1 263 ? 37.034  -23.835 -45.744 1.00 29.92 ? 263 GLN C CD  1 
ATOM   6455 O  OE1 . GLN C  1 263 ? 38.143  -24.114 -45.294 1.00 28.59 ? 263 GLN C OE1 1 
ATOM   6456 N  NE2 . GLN C  1 263 ? 36.320  -24.700 -46.462 1.00 22.76 ? 263 GLN C NE2 1 
ATOM   6457 O  OXT . GLN C  1 263 ? 35.631  -20.967 -43.141 1.00 64.65 ? 263 GLN C OXT 1 
ATOM   6458 N  N   . LYS D  1 3   ? 14.309  19.753  -45.249 1.00 36.52 ? 3   LYS D N   1 
ATOM   6459 C  CA  . LYS D  1 3   ? 14.726  18.840  -46.317 1.00 28.95 ? 3   LYS D CA  1 
ATOM   6460 C  C   . LYS D  1 3   ? 15.405  17.550  -45.757 1.00 23.08 ? 3   LYS D C   1 
ATOM   6461 O  O   . LYS D  1 3   ? 16.270  16.996  -46.470 1.00 22.10 ? 3   LYS D O   1 
ATOM   6462 C  CB  . LYS D  1 3   ? 15.753  19.548  -47.205 1.00 30.71 ? 3   LYS D CB  1 
ATOM   6463 C  CG  . LYS D  1 3   ? 16.614  20.536  -46.448 1.00 36.43 ? 3   LYS D CG  1 
ATOM   6464 C  CD  . LYS D  1 3   ? 17.258  21.564  -47.389 1.00 41.48 ? 3   LYS D CD  1 
ATOM   6465 C  CE  . LYS D  1 3   ? 18.267  20.827  -48.246 1.00 35.97 ? 3   LYS D CE  1 
ATOM   6466 N  NZ  . LYS D  1 3   ? 19.453  20.544  -47.366 1.00 28.59 ? 3   LYS D NZ  1 
ATOM   6467 N  N   . TRP D  1 4   ? 15.021  17.094  -44.505 1.00 15.42 ? 4   TRP D N   1 
ATOM   6468 C  CA  . TRP D  1 4   ? 15.681  15.910  -43.919 1.00 14.04 ? 4   TRP D CA  1 
ATOM   6469 C  C   . TRP D  1 4   ? 15.405  14.713  -44.841 1.00 12.23 ? 4   TRP D C   1 
ATOM   6470 O  O   . TRP D  1 4   ? 14.396  14.631  -45.562 1.00 12.65 ? 4   TRP D O   1 
ATOM   6471 C  CB  . TRP D  1 4   ? 15.202  15.712  -42.487 1.00 12.20 ? 4   TRP D CB  1 
ATOM   6472 C  CG  . TRP D  1 4   ? 13.762  15.484  -42.329 1.00 11.27 ? 4   TRP D CG  1 
ATOM   6473 C  CD1 . TRP D  1 4   ? 12.714  16.358  -42.114 1.00 12.12 ? 4   TRP D CD1 1 
ATOM   6474 C  CD2 . TRP D  1 4   ? 13.149  14.121  -42.256 1.00 11.00 ? 4   TRP D CD2 1 
ATOM   6475 N  NE1 . TRP D  1 4   ? 11.529  15.687  -41.929 1.00 12.70 ? 4   TRP D NE1 1 
ATOM   6476 C  CE2 . TRP D  1 4   ? 11.742  14.338  -42.057 1.00 11.04 ? 4   TRP D CE2 1 
ATOM   6477 C  CE3 . TRP D  1 4   ? 13.650  12.790  -42.428 1.00 11.27 ? 4   TRP D CE3 1 
ATOM   6478 C  CZ2 . TRP D  1 4   ? 10.866  13.282  -41.900 1.00 11.84 ? 4   TRP D CZ2 1 
ATOM   6479 C  CZ3 . TRP D  1 4   ? 12.706  11.720  -42.287 1.00 10.94 ? 4   TRP D CZ3 1 
ATOM   6480 C  CH2 . TRP D  1 4   ? 11.395  11.965  -42.033 1.00 12.03 ? 4   TRP D CH2 1 
ATOM   6481 N  N   . THR D  1 5   ? 16.326  13.793  -44.776 1.00 11.14 ? 5   THR D N   1 
ATOM   6482 C  CA  . THR D  1 5   ? 16.295  12.561  -45.592 1.00 11.28 ? 5   THR D CA  1 
ATOM   6483 C  C   . THR D  1 5   ? 16.834  11.377  -44.752 1.00 10.77 ? 5   THR D C   1 
ATOM   6484 O  O   . THR D  1 5   ? 17.165  11.547  -43.545 1.00 10.14 ? 5   THR D O   1 
ATOM   6485 C  CB  . THR D  1 5   ? 17.209  12.632  -46.850 1.00 13.65 ? 5   THR D CB  1 
ATOM   6486 O  OG1 . THR D  1 5   ? 18.561  12.619  -46.350 1.00 13.33 ? 5   THR D OG1 1 
ATOM   6487 C  CG2 . THR D  1 5   ? 16.913  13.949  -47.706 1.00 14.23 ? 5   THR D CG2 1 
ATOM   6488 N  N   . TYR D  1 6   ? 16.916  10.170  -45.351 1.00 10.40 ? 6   TYR D N   1 
ATOM   6489 C  CA  . TYR D  1 6   ? 17.566  9.056   -44.789 1.00 10.01 ? 6   TYR D CA  1 
ATOM   6490 C  C   . TYR D  1 6   ? 18.900  8.689   -45.329 1.00 10.06 ? 6   TYR D C   1 
ATOM   6491 O  O   . TYR D  1 6   ? 19.485  7.636   -45.056 1.00 11.36 ? 6   TYR D O   1 
ATOM   6492 C  CB  . TYR D  1 6   ? 16.614  7.832   -44.970 1.00 10.19 ? 6   TYR D CB  1 
ATOM   6493 C  CG  . TYR D  1 6   ? 15.333  7.922   -44.098 1.00 9.45  ? 6   TYR D CG  1 
ATOM   6494 C  CD1 . TYR D  1 6   ? 15.332  7.392   -42.775 1.00 9.52  ? 6   TYR D CD1 1 
ATOM   6495 C  CD2 . TYR D  1 6   ? 14.199  8.520   -44.552 1.00 8.16  ? 6   TYR D CD2 1 
ATOM   6496 C  CE1 . TYR D  1 6   ? 14.217  7.400   -41.971 1.00 8.29  ? 6   TYR D CE1 1 
ATOM   6497 C  CE2 . TYR D  1 6   ? 13.036  8.550   -43.761 1.00 8.93  ? 6   TYR D CE2 1 
ATOM   6498 C  CZ  . TYR D  1 6   ? 13.073  7.997   -42.439 1.00 7.43  ? 6   TYR D CZ  1 
ATOM   6499 O  OH  . TYR D  1 6   ? 11.899  8.027   -41.724 1.00 8.87  ? 6   TYR D OH  1 
ATOM   6500 N  N   . PHE D  1 7   ? 19.392  9.547   -46.239 1.00 12.16 ? 7   PHE D N   1 
ATOM   6501 C  CA  . PHE D  1 7   ? 20.622  9.198   -46.970 1.00 15.20 ? 7   PHE D CA  1 
ATOM   6502 C  C   . PHE D  1 7   ? 21.381  10.471  -47.336 1.00 15.52 ? 7   PHE D C   1 
ATOM   6503 O  O   . PHE D  1 7   ? 20.780  11.351  -47.951 1.00 16.22 ? 7   PHE D O   1 
ATOM   6504 C  CB  . PHE D  1 7   ? 20.300  8.461   -48.302 1.00 18.50 ? 7   PHE D CB  1 
ATOM   6505 C  CG  . PHE D  1 7   ? 21.535  8.046   -49.034 1.00 24.73 ? 7   PHE D CG  1 
ATOM   6506 C  CD1 . PHE D  1 7   ? 22.351  7.015   -48.539 1.00 27.17 ? 7   PHE D CD1 1 
ATOM   6507 C  CD2 . PHE D  1 7   ? 21.973  8.813   -50.154 1.00 28.44 ? 7   PHE D CD2 1 
ATOM   6508 C  CE1 . PHE D  1 7   ? 23.546  6.674   -49.189 1.00 32.87 ? 7   PHE D CE1 1 
ATOM   6509 C  CE2 . PHE D  1 7   ? 23.154  8.467   -50.812 1.00 35.67 ? 7   PHE D CE2 1 
ATOM   6510 C  CZ  . PHE D  1 7   ? 23.927  7.398   -50.337 1.00 33.14 ? 7   PHE D CZ  1 
ATOM   6511 N  N   . GLY D  1 8   ? 22.689  10.498  -47.049 1.00 16.11 ? 8   GLY D N   1 
ATOM   6512 C  CA  . GLY D  1 8   ? 23.536  11.645  -47.479 1.00 17.24 ? 8   GLY D CA  1 
ATOM   6513 C  C   . GLY D  1 8   ? 23.563  12.738  -46.441 1.00 16.68 ? 8   GLY D C   1 
ATOM   6514 O  O   . GLY D  1 8   ? 23.271  12.502  -45.252 1.00 16.41 ? 8   GLY D O   1 
ATOM   6515 N  N   A PRO D  1 9   ? 23.978  13.961  -46.760 0.50 16.45 ? 9   PRO D N   1 
ATOM   6516 N  N   B PRO D  1 9   ? 23.840  13.968  -46.936 0.50 18.04 ? 9   PRO D N   1 
ATOM   6517 C  CA  A PRO D  1 9   ? 24.254  14.979  -45.680 0.50 15.57 ? 9   PRO D CA  1 
ATOM   6518 C  CA  B PRO D  1 9   ? 24.208  15.001  -46.054 0.50 16.77 ? 9   PRO D CA  1 
ATOM   6519 C  C   A PRO D  1 9   ? 23.053  15.522  -44.870 0.50 15.85 ? 9   PRO D C   1 
ATOM   6520 C  C   B PRO D  1 9   ? 23.193  15.325  -44.997 0.50 15.36 ? 9   PRO D C   1 
ATOM   6521 O  O   A PRO D  1 9   ? 23.189  16.199  -43.824 0.50 15.21 ? 9   PRO D O   1 
ATOM   6522 O  O   B PRO D  1 9   ? 23.678  15.610  -43.897 0.50 16.05 ? 9   PRO D O   1 
ATOM   6523 C  CB  A PRO D  1 9   ? 24.990  16.123  -46.440 0.50 17.39 ? 9   PRO D CB  1 
ATOM   6524 C  CB  B PRO D  1 9   ? 24.553  16.195  -46.999 0.50 17.50 ? 9   PRO D CB  1 
ATOM   6525 C  CG  A PRO D  1 9   ? 25.167  15.634  -47.835 0.50 14.17 ? 9   PRO D CG  1 
ATOM   6526 C  CG  B PRO D  1 9   ? 23.932  15.885  -48.306 0.50 19.48 ? 9   PRO D CG  1 
ATOM   6527 C  CD  A PRO D  1 9   ? 24.598  14.252  -48.059 0.50 15.44 ? 9   PRO D CD  1 
ATOM   6528 C  CD  B PRO D  1 9   ? 24.020  14.373  -48.356 0.50 18.04 ? 9   PRO D CD  1 
ATOM   6529 N  N   . ASP D  1 10  ? 21.849  15.199  -45.306 1.00 13.97 ? 10  ASP D N   1 
ATOM   6530 C  CA  . ASP D  1 10  ? 20.707  15.528  -44.529 1.00 14.04 ? 10  ASP D CA  1 
ATOM   6531 C  C   . ASP D  1 10  ? 20.080  14.277  -43.848 1.00 11.84 ? 10  ASP D C   1 
ATOM   6532 O  O   . ASP D  1 10  ? 18.989  14.402  -43.323 1.00 11.79 ? 10  ASP D O   1 
ATOM   6533 C  CB  . ASP D  1 10  ? 19.642  16.323  -45.312 1.00 15.70 ? 10  ASP D CB  1 
ATOM   6534 C  CG  . ASP D  1 10  ? 20.231  17.605  -45.979 1.00 22.28 ? 10  ASP D CG  1 
ATOM   6535 O  OD1 . ASP D  1 10  ? 20.966  18.304  -45.283 1.00 24.62 ? 10  ASP D OD1 1 
ATOM   6536 O  OD2 . ASP D  1 10  ? 20.017  17.749  -47.202 1.00 27.67 ? 10  ASP D OD2 1 
ATOM   6537 N  N   . GLY D  1 11  ? 20.868  13.234  -43.802 1.00 11.51 ? 11  GLY D N   1 
ATOM   6538 C  CA  . GLY D  1 11  ? 20.418  11.916  -43.237 1.00 9.85  ? 11  GLY D CA  1 
ATOM   6539 C  C   . GLY D  1 11  ? 20.562  11.931  -41.717 1.00 9.09  ? 11  GLY D C   1 
ATOM   6540 O  O   . GLY D  1 11  ? 20.703  12.981  -41.029 1.00 9.08  ? 11  GLY D O   1 
ATOM   6541 N  N   . GLU D  1 12  ? 20.254  10.789  -41.136 1.00 8.14  ? 12  GLU D N   1 
ATOM   6542 C  CA  . GLU D  1 12  ? 19.897  10.718  -39.733 1.00 8.05  ? 12  GLU D CA  1 
ATOM   6543 C  C   . GLU D  1 12  ? 20.900  11.159  -38.727 1.00 8.59  ? 12  GLU D C   1 
ATOM   6544 O  O   . GLU D  1 12  ? 20.513  11.617  -37.658 1.00 7.54  ? 12  GLU D O   1 
ATOM   6545 C  CB  . GLU D  1 12  ? 19.407  9.307   -39.312 1.00 7.92  ? 12  GLU D CB  1 
ATOM   6546 C  CG  . GLU D  1 12  ? 20.492  8.257   -39.242 1.00 8.24  ? 12  GLU D CG  1 
ATOM   6547 C  CD  . GLU D  1 12  ? 19.877  6.885   -39.270 1.00 8.26  ? 12  GLU D CD  1 
ATOM   6548 O  OE1 . GLU D  1 12  ? 19.467  6.390   -38.200 1.00 9.45  ? 12  GLU D OE1 1 
ATOM   6549 O  OE2 . GLU D  1 12  ? 19.768  6.310   -40.368 1.00 10.07 ? 12  GLU D OE2 1 
ATOM   6550 N  N   . ASN D  1 13  ? 22.194  11.124  -39.070 1.00 8.27  ? 13  ASN D N   1 
ATOM   6551 C  CA  . ASN D  1 13  ? 23.190  11.582  -38.090 1.00 8.20  ? 13  ASN D CA  1 
ATOM   6552 C  C   . ASN D  1 13  ? 23.233  13.122  -38.125 1.00 8.78  ? 13  ASN D C   1 
ATOM   6553 O  O   . ASN D  1 13  ? 23.867  13.664  -37.203 1.00 9.49  ? 13  ASN D O   1 
ATOM   6554 C  CB  . ASN D  1 13  ? 24.592  11.040  -38.437 1.00 8.67  ? 13  ASN D CB  1 
ATOM   6555 C  CG  . ASN D  1 13  ? 24.733  9.568   -38.165 1.00 8.44  ? 13  ASN D CG  1 
ATOM   6556 O  OD1 . ASN D  1 13  ? 23.825  8.918   -37.671 1.00 9.37  ? 13  ASN D OD1 1 
ATOM   6557 N  ND2 . ASN D  1 13  ? 25.902  9.021   -38.516 1.00 10.31 ? 13  ASN D ND2 1 
ATOM   6558 N  N   . SER D  1 14  ? 22.552  13.756  -39.101 1.00 8.14  ? 14  SER D N   1 
ATOM   6559 C  CA  . SER D  1 14  ? 22.519  15.222  -39.136 1.00 8.04  ? 14  SER D CA  1 
ATOM   6560 C  C   . SER D  1 14  ? 21.191  15.767  -38.715 1.00 8.80  ? 14  SER D C   1 
ATOM   6561 O  O   . SER D  1 14  ? 21.041  17.001  -38.607 1.00 9.28  ? 14  SER D O   1 
ATOM   6562 C  CB  . SER D  1 14  ? 22.812  15.696  -40.562 1.00 9.09  ? 14  SER D CB  1 
ATOM   6563 O  OG  . SER D  1 14  ? 24.166  15.404  -40.861 1.00 11.20 ? 14  SER D OG  1 
ATOM   6564 N  N   . TRP D  1 15  ? 20.147  14.961  -38.442 1.00 8.06  ? 15  TRP D N   1 
ATOM   6565 C  CA  . TRP D  1 15  ? 18.865  15.558  -38.056 1.00 8.56  ? 15  TRP D CA  1 
ATOM   6566 C  C   . TRP D  1 15  ? 18.936  16.456  -36.859 1.00 8.36  ? 15  TRP D C   1 
ATOM   6567 O  O   . TRP D  1 15  ? 18.191  17.453  -36.818 1.00 8.64  ? 15  TRP D O   1 
ATOM   6568 C  CB  . TRP D  1 15  ? 17.854  14.425  -37.658 1.00 8.58  ? 15  TRP D CB  1 
ATOM   6569 C  CG  . TRP D  1 15  ? 17.473  13.536  -38.820 1.00 8.94  ? 15  TRP D CG  1 
ATOM   6570 C  CD1 . TRP D  1 15  ? 17.725  13.681  -40.144 1.00 8.14  ? 15  TRP D CD1 1 
ATOM   6571 C  CD2 . TRP D  1 15  ? 16.687  12.323  -38.707 1.00 7.89  ? 15  TRP D CD2 1 
ATOM   6572 N  NE1 . TRP D  1 15  ? 17.143  12.668  -40.877 1.00 9.58  ? 15  TRP D NE1 1 
ATOM   6573 C  CE2 . TRP D  1 15  ? 16.515  11.811  -40.038 1.00 7.35  ? 15  TRP D CE2 1 
ATOM   6574 C  CE3 . TRP D  1 15  ? 16.116  11.629  -37.603 1.00 8.55  ? 15  TRP D CE3 1 
ATOM   6575 C  CZ2 . TRP D  1 15  ? 15.838  10.588  -40.313 1.00 8.33  ? 15  TRP D CZ2 1 
ATOM   6576 C  CZ3 . TRP D  1 15  ? 15.404  10.424  -37.898 1.00 9.33  ? 15  TRP D CZ3 1 
ATOM   6577 C  CH2 . TRP D  1 15  ? 15.249  9.953   -39.226 1.00 7.85  ? 15  TRP D CH2 1 
ATOM   6578 N  N   . SER D  1 16  ? 19.782  16.131  -35.885 1.00 8.53  ? 16  SER D N   1 
ATOM   6579 C  CA  . SER D  1 16  ? 19.884  16.930  -34.620 1.00 8.91  ? 16  SER D CA  1 
ATOM   6580 C  C   . SER D  1 16  ? 20.359  18.365  -34.946 1.00 9.64  ? 16  SER D C   1 
ATOM   6581 O  O   . SER D  1 16  ? 20.155  19.217  -34.079 1.00 10.72 ? 16  SER D O   1 
ATOM   6582 C  CB  . SER D  1 16  ? 20.860  16.295  -33.643 1.00 10.93 ? 16  SER D CB  1 
ATOM   6583 O  OG  . SER D  1 16  ? 22.177  16.415  -34.213 1.00 14.79 ? 16  SER D OG  1 
ATOM   6584 N  N   . LYS D  1 17  ? 20.956  18.587  -36.116 1.00 9.30  ? 17  LYS D N   1 
ATOM   6585 C  CA  . LYS D  1 17  ? 21.456  19.979  -36.428 1.00 10.74 ? 17  LYS D CA  1 
ATOM   6586 C  C   . LYS D  1 17  ? 20.269  20.907  -36.535 1.00 11.38 ? 17  LYS D C   1 
ATOM   6587 O  O   . LYS D  1 17  ? 20.379  22.126  -36.224 1.00 11.07 ? 17  LYS D O   1 
ATOM   6588 C  CB  . LYS D  1 17  ? 22.190  20.037  -37.736 1.00 9.49  ? 17  LYS D CB  1 
ATOM   6589 C  CG  . LYS D  1 17  ? 23.461  19.154  -37.738 1.00 10.69 ? 17  LYS D CG  1 
ATOM   6590 C  CD  . LYS D  1 17  ? 24.063  19.147  -39.170 1.00 10.36 ? 17  LYS D CD  1 
ATOM   6591 C  CE  . LYS D  1 17  ? 25.233  18.185  -39.291 1.00 9.94  ? 17  LYS D CE  1 
ATOM   6592 N  NZ  . LYS D  1 17  ? 25.873  18.391  -40.631 1.00 11.46 ? 17  LYS D NZ  1 
ATOM   6593 N  N   . LYS D  1 18  ? 19.105  20.445  -36.979 1.00 9.63  ? 18  LYS D N   1 
ATOM   6594 C  CA  . LYS D  1 18  ? 17.859  21.282  -37.157 1.00 9.77  ? 18  LYS D CA  1 
ATOM   6595 C  C   . LYS D  1 18  ? 16.772  20.915  -36.145 1.00 11.27 ? 18  LYS D C   1 
ATOM   6596 O  O   . LYS D  1 18  ? 15.873  21.743  -35.944 1.00 12.80 ? 18  LYS D O   1 
ATOM   6597 C  CB  . LYS D  1 18  ? 17.300  21.115  -38.562 1.00 10.83 ? 18  LYS D CB  1 
ATOM   6598 C  CG  . LYS D  1 18  ? 18.205  21.802  -39.680 1.00 14.10 ? 18  LYS D CG  1 
ATOM   6599 C  CD  . LYS D  1 18  ? 17.553  21.621  -41.046 1.00 16.35 ? 18  LYS D CD  1 
ATOM   6600 C  CE  . LYS D  1 18  ? 18.311  22.484  -42.079 1.00 21.13 ? 18  LYS D CE  1 
ATOM   6601 N  NZ  . LYS D  1 18  ? 17.847  21.925  -43.403 1.00 25.98 ? 18  LYS D NZ  1 
ATOM   6602 N  N   . TYR D  1 19  ? 16.845  19.733  -35.582 1.00 9.83  ? 19  TYR D N   1 
ATOM   6603 C  CA  . TYR D  1 19  ? 15.688  19.196  -34.809 1.00 9.82  ? 19  TYR D CA  1 
ATOM   6604 C  C   . TYR D  1 19  ? 16.350  18.701  -33.520 1.00 9.43  ? 19  TYR D C   1 
ATOM   6605 O  O   . TYR D  1 19  ? 16.815  17.524  -33.403 1.00 9.81  ? 19  TYR D O   1 
ATOM   6606 C  CB  . TYR D  1 19  ? 15.052  18.001  -35.539 1.00 9.70  ? 19  TYR D CB  1 
ATOM   6607 C  CG  . TYR D  1 19  ? 14.449  18.415  -36.804 1.00 9.42  ? 19  TYR D CG  1 
ATOM   6608 C  CD1 . TYR D  1 19  ? 13.216  19.119  -36.863 1.00 10.81 ? 19  TYR D CD1 1 
ATOM   6609 C  CD2 . TYR D  1 19  ? 15.127  18.179  -38.036 1.00 10.17 ? 19  TYR D CD2 1 
ATOM   6610 C  CE1 . TYR D  1 19  ? 12.698  19.508  -38.098 1.00 11.51 ? 19  TYR D CE1 1 
ATOM   6611 C  CE2 . TYR D  1 19  ? 14.583  18.579  -39.225 1.00 10.59 ? 19  TYR D CE2 1 
ATOM   6612 C  CZ  . TYR D  1 19  ? 13.404  19.252  -39.257 1.00 12.52 ? 19  TYR D CZ  1 
ATOM   6613 O  OH  . TYR D  1 19  ? 12.799  19.620  -40.459 1.00 16.62 ? 19  TYR D OH  1 
ATOM   6614 N  N   . PRO D  1 20  ? 16.477  19.550  -32.469 1.00 10.54 ? 20  PRO D N   1 
ATOM   6615 C  CA  . PRO D  1 20  ? 17.305  19.179  -31.326 1.00 10.31 ? 20  PRO D CA  1 
ATOM   6616 C  C   . PRO D  1 20  ? 16.820  17.925  -30.576 1.00 10.03 ? 20  PRO D C   1 
ATOM   6617 O  O   . PRO D  1 20  ? 17.665  17.250  -29.957 1.00 10.89 ? 20  PRO D O   1 
ATOM   6618 C  CB  . PRO D  1 20  ? 17.222  20.447  -30.364 1.00 12.20 ? 20  PRO D CB  1 
ATOM   6619 C  CG  . PRO D  1 20  ? 16.495  21.395  -31.112 1.00 13.77 ? 20  PRO D CG  1 
ATOM   6620 C  CD  . PRO D  1 20  ? 16.010  20.962  -32.455 1.00 9.24  ? 20  PRO D CD  1 
ATOM   6621 N  N   . SER D  1 21  ? 15.514  17.656  -30.621 1.00 10.03 ? 21  SER D N   1 
ATOM   6622 C  CA  . SER D  1 21  ? 15.140  16.441  -29.853 1.00 10.28 ? 21  SER D CA  1 
ATOM   6623 C  C   . SER D  1 21  ? 15.691  15.176  -30.511 1.00 9.43  ? 21  SER D C   1 
ATOM   6624 O  O   . SER D  1 21  ? 15.714  14.168  -29.823 1.00 10.43 ? 21  SER D O   1 
ATOM   6625 C  CB  . SER D  1 21  ? 13.594  16.312  -29.803 1.00 10.72 ? 21  SER D CB  1 
ATOM   6626 O  OG  . SER D  1 21  ? 13.033  17.359  -28.982 1.00 14.56 ? 21  SER D OG  1 
ATOM   6627 N  N   . CYS D  1 22  ? 16.106  15.185  -31.787 1.00 10.25 ? 22  CYS D N   1 
ATOM   6628 C  CA  . CYS D  1 22  ? 16.649  13.984  -32.409 1.00 8.70  ? 22  CYS D CA  1 
ATOM   6629 C  C   . CYS D  1 22  ? 17.997  13.683  -31.782 1.00 11.09 ? 22  CYS D C   1 
ATOM   6630 O  O   . CYS D  1 22  ? 18.509  12.579  -31.968 1.00 10.29 ? 22  CYS D O   1 
ATOM   6631 C  CB  . CYS D  1 22  ? 16.827  14.159  -33.918 1.00 10.98 ? 22  CYS D CB  1 
ATOM   6632 S  SG  . CYS D  1 22  ? 15.270  14.485  -34.815 1.00 9.41  ? 22  CYS D SG  1 
ATOM   6633 N  N   . GLY D  1 23  ? 18.661  14.634  -31.070 1.00 10.76 ? 23  GLY D N   1 
ATOM   6634 C  CA  . GLY D  1 23  ? 19.872  14.370  -30.263 1.00 11.89 ? 23  GLY D CA  1 
ATOM   6635 C  C   . GLY D  1 23  ? 19.585  14.299  -28.778 1.00 13.37 ? 23  GLY D C   1 
ATOM   6636 O  O   . GLY D  1 23  ? 20.571  14.322  -27.953 1.00 14.18 ? 23  GLY D O   1 
ATOM   6637 N  N   . GLY D  1 24  ? 18.338  14.252  -28.377 1.00 11.63 ? 24  GLY D N   1 
ATOM   6638 C  CA  . GLY D  1 24  ? 17.948  14.225  -26.898 1.00 14.67 ? 24  GLY D CA  1 
ATOM   6639 C  C   . GLY D  1 24  ? 17.759  12.790  -26.441 1.00 15.29 ? 24  GLY D C   1 
ATOM   6640 O  O   . GLY D  1 24  ? 18.204  11.829  -27.029 1.00 16.43 ? 24  GLY D O   1 
ATOM   6641 N  N   . LEU D  1 25  ? 17.151  12.667  -25.299 1.00 15.55 ? 25  LEU D N   1 
ATOM   6642 C  CA  . LEU D  1 25  ? 16.993  11.379  -24.654 1.00 15.13 ? 25  LEU D CA  1 
ATOM   6643 C  C   . LEU D  1 25  ? 15.735  10.681  -25.233 1.00 13.12 ? 25  LEU D C   1 
ATOM   6644 O  O   . LEU D  1 25  ? 14.854  11.255  -25.914 1.00 13.72 ? 25  LEU D O   1 
ATOM   6645 C  CB  . LEU D  1 25  ? 16.851  11.540  -23.090 1.00 19.15 ? 25  LEU D CB  1 
ATOM   6646 C  CG  . LEU D  1 25  ? 18.149  12.166  -22.439 1.00 19.63 ? 25  LEU D CG  1 
ATOM   6647 C  CD1 . LEU D  1 25  ? 17.761  12.564  -21.015 1.00 22.93 ? 25  LEU D CD1 1 
ATOM   6648 C  CD2 . LEU D  1 25  ? 19.181  11.050  -22.487 1.00 23.28 ? 25  LEU D CD2 1 
ATOM   6649 N  N   . LEU D  1 26  ? 15.642  9.405   -24.828 1.00 13.05 ? 26  LEU D N   1 
ATOM   6650 C  CA  . LEU D  1 26  ? 14.434  8.541   -25.064 1.00 13.28 ? 26  LEU D CA  1 
ATOM   6651 C  C   . LEU D  1 26  ? 14.012  8.413   -26.497 1.00 10.50 ? 26  LEU D C   1 
ATOM   6652 O  O   . LEU D  1 26  ? 12.807  8.501   -26.897 1.00 11.47 ? 26  LEU D O   1 
ATOM   6653 C  CB  . LEU D  1 26  ? 13.279  9.081   -24.256 1.00 16.33 ? 26  LEU D CB  1 
ATOM   6654 C  CG  . LEU D  1 26  ? 13.567  9.401   -22.799 1.00 20.02 ? 26  LEU D CG  1 
ATOM   6655 C  CD1 . LEU D  1 26  ? 12.223  9.701   -22.188 1.00 21.58 ? 26  LEU D CD1 1 
ATOM   6656 C  CD2 . LEU D  1 26  ? 14.251  8.232   -22.079 1.00 22.23 ? 26  LEU D CD2 1 
ATOM   6657 N  N   . GLN D  1 27  ? 15.007  8.176   -27.327 1.00 9.65  ? 27  GLN D N   1 
ATOM   6658 C  CA  . GLN D  1 27  ? 14.716  8.084   -28.802 1.00 8.83  ? 27  GLN D CA  1 
ATOM   6659 C  C   . GLN D  1 27  ? 14.312  6.665   -29.242 1.00 9.33  ? 27  GLN D C   1 
ATOM   6660 O  O   . GLN D  1 27  ? 14.691  5.673   -28.607 1.00 10.23 ? 27  GLN D O   1 
ATOM   6661 C  CB  . GLN D  1 27  ? 15.967  8.490   -29.597 1.00 9.44  ? 27  GLN D CB  1 
ATOM   6662 C  CG  . GLN D  1 27  ? 16.326  9.977   -29.343 1.00 10.02 ? 27  GLN D CG  1 
ATOM   6663 C  CD  . GLN D  1 27  ? 15.250  10.881  -29.971 1.00 9.43  ? 27  GLN D CD  1 
ATOM   6664 O  OE1 . GLN D  1 27  ? 15.294  11.060  -31.239 1.00 8.95  ? 27  GLN D OE1 1 
ATOM   6665 N  NE2 . GLN D  1 27  ? 14.307  11.467  -29.207 1.00 10.29 ? 27  GLN D NE2 1 
ATOM   6666 N  N   . SER D  1 28  ? 13.566  6.659   -30.316 1.00 7.46  ? 28  SER D N   1 
ATOM   6667 C  CA  . SER D  1 28  ? 13.143  5.375   -30.949 1.00 7.17  ? 28  SER D CA  1 
ATOM   6668 C  C   . SER D  1 28  ? 13.682  5.339   -32.380 1.00 7.64  ? 28  SER D C   1 
ATOM   6669 O  O   . SER D  1 28  ? 13.957  6.418   -32.945 1.00 8.06  ? 28  SER D O   1 
ATOM   6670 C  CB  . SER D  1 28  ? 11.622  5.394   -30.995 1.00 7.55  ? 28  SER D CB  1 
ATOM   6671 O  OG  . SER D  1 28  ? 11.106  5.352   -29.669 1.00 8.15  ? 28  SER D OG  1 
ATOM   6672 N  N   . PRO D  1 29  ? 13.791  4.205   -33.029 1.00 7.11  ? 29  PRO D N   1 
ATOM   6673 C  CA  . PRO D  1 29  ? 13.417  2.880   -32.471 1.00 7.83  ? 29  PRO D CA  1 
ATOM   6674 C  C   . PRO D  1 29  ? 14.558  2.275   -31.653 1.00 7.77  ? 29  PRO D C   1 
ATOM   6675 O  O   . PRO D  1 29  ? 15.590  2.903   -31.503 1.00 8.76  ? 29  PRO D O   1 
ATOM   6676 C  CB  . PRO D  1 29  ? 13.181  2.072   -33.814 1.00 8.39  ? 29  PRO D CB  1 
ATOM   6677 C  CG  . PRO D  1 29  ? 14.318  2.628   -34.677 1.00 7.37  ? 29  PRO D CG  1 
ATOM   6678 C  CD  . PRO D  1 29  ? 14.332  4.124   -34.428 1.00 7.13  ? 29  PRO D CD  1 
ATOM   6679 N  N   . ILE D  1 30  ? 14.297  1.058   -31.148 1.00 7.53  ? 30  ILE D N   1 
ATOM   6680 C  CA  . ILE D  1 30  ? 15.265  0.347   -30.308 1.00 8.66  ? 30  ILE D CA  1 
ATOM   6681 C  C   . ILE D  1 30  ? 15.243  -1.114  -30.715 1.00 8.53  ? 30  ILE D C   1 
ATOM   6682 O  O   . ILE D  1 30  ? 14.360  -1.577  -31.438 1.00 8.10  ? 30  ILE D O   1 
ATOM   6683 C  CB  . ILE D  1 30  ? 14.955  0.476   -28.797 1.00 8.90  ? 30  ILE D CB  1 
ATOM   6684 C  CG1 . ILE D  1 30  ? 13.481  0.016   -28.504 1.00 9.66  ? 30  ILE D CG1 1 
ATOM   6685 C  CG2 . ILE D  1 30  ? 15.177  1.948   -28.313 1.00 10.80 ? 30  ILE D CG2 1 
ATOM   6686 C  CD1 . ILE D  1 30  ? 13.216  -0.127  -27.008 1.00 12.24 ? 30  ILE D CD1 1 
ATOM   6687 N  N   . ASP D  1 31  ? 16.327  -1.787  -30.267 1.00 9.10  ? 31  ASP D N   1 
ATOM   6688 C  CA  . ASP D  1 31  ? 16.414  -3.240  -30.428 1.00 9.50  ? 31  ASP D CA  1 
ATOM   6689 C  C   . ASP D  1 31  ? 15.782  -3.932  -29.226 1.00 11.30 ? 31  ASP D C   1 
ATOM   6690 O  O   . ASP D  1 31  ? 16.203  -3.746  -28.113 1.00 13.95 ? 31  ASP D O   1 
ATOM   6691 C  CB  . ASP D  1 31  ? 17.896  -3.677  -30.544 1.00 11.05 ? 31  ASP D CB  1 
ATOM   6692 C  CG  . ASP D  1 31  ? 18.022  -5.202  -30.700 1.00 13.96 ? 31  ASP D CG  1 
ATOM   6693 O  OD1 . ASP D  1 31  ? 17.467  -5.763  -31.619 1.00 11.88 ? 31  ASP D OD1 1 
ATOM   6694 O  OD2 . ASP D  1 31  ? 18.651  -5.773  -29.790 1.00 15.72 ? 31  ASP D OD2 1 
ATOM   6695 N  N   . LEU D  1 32  ? 14.906  -4.863  -29.536 1.00 10.05 ? 32  LEU D N   1 
ATOM   6696 C  CA  . LEU D  1 32  ? 14.151  -5.539  -28.452 1.00 10.15 ? 32  LEU D CA  1 
ATOM   6697 C  C   . LEU D  1 32  ? 14.943  -6.835  -28.210 1.00 11.11 ? 32  LEU D C   1 
ATOM   6698 O  O   . LEU D  1 32  ? 14.969  -7.763  -29.057 1.00 13.04 ? 32  LEU D O   1 
ATOM   6699 C  CB  . LEU D  1 32  ? 12.709  -5.851  -28.961 1.00 10.80 ? 32  LEU D CB  1 
ATOM   6700 C  CG  . LEU D  1 32  ? 11.966  -4.526  -29.362 1.00 11.57 ? 32  LEU D CG  1 
ATOM   6701 C  CD1 . LEU D  1 32  ? 10.661  -4.921  -30.063 1.00 13.49 ? 32  LEU D CD1 1 
ATOM   6702 C  CD2 . LEU D  1 32  ? 11.637  -3.634  -28.136 1.00 14.46 ? 32  LEU D CD2 1 
ATOM   6703 N  N   . HIS D  1 33  ? 15.609  -6.907  -27.061 1.00 11.67 ? 33  HIS D N   1 
ATOM   6704 C  CA  . HIS D  1 33  ? 16.383  -8.119  -26.808 1.00 11.77 ? 33  HIS D CA  1 
ATOM   6705 C  C   . HIS D  1 33  ? 16.314  -8.437  -25.300 1.00 11.63 ? 33  HIS D C   1 
ATOM   6706 O  O   . HIS D  1 33  ? 16.049  -7.559  -24.449 1.00 12.08 ? 33  HIS D O   1 
ATOM   6707 C  CB  . HIS D  1 33  ? 17.884  -7.979  -27.258 1.00 13.27 ? 33  HIS D CB  1 
ATOM   6708 C  CG  . HIS D  1 33  ? 18.661  -6.909  -26.565 1.00 13.13 ? 33  HIS D CG  1 
ATOM   6709 N  ND1 . HIS D  1 33  ? 18.548  -5.573  -26.877 1.00 14.93 ? 33  HIS D ND1 1 
ATOM   6710 C  CD2 . HIS D  1 33  ? 19.487  -6.977  -25.451 1.00 14.04 ? 33  HIS D CD2 1 
ATOM   6711 C  CE1 . HIS D  1 33  ? 19.373  -4.886  -26.042 1.00 19.16 ? 33  HIS D CE1 1 
ATOM   6712 N  NE2 . HIS D  1 33  ? 19.951  -5.774  -25.215 1.00 16.76 ? 33  HIS D NE2 1 
ATOM   6713 N  N   . SER D  1 34  ? 16.609  -9.733  -25.006 1.00 12.75 ? 34  SER D N   1 
ATOM   6714 C  CA  . SER D  1 34  ? 16.271  -10.306 -23.674 1.00 13.70 ? 34  SER D CA  1 
ATOM   6715 C  C   . SER D  1 34  ? 16.776  -9.523  -22.491 1.00 14.01 ? 34  SER D C   1 
ATOM   6716 O  O   . SER D  1 34  ? 15.994  -9.320  -21.545 1.00 13.84 ? 34  SER D O   1 
ATOM   6717 C  CB  . SER D  1 34  ? 16.759  -11.738 -23.654 1.00 16.94 ? 34  SER D CB  1 
ATOM   6718 O  OG  . SER D  1 34  ? 18.122  -11.687 -23.583 1.00 21.78 ? 34  SER D OG  1 
ATOM   6719 N  N   . ASP D  1 35  ? 18.029  -9.003  -22.462 1.00 12.31 ? 35  ASP D N   1 
ATOM   6720 C  CA  . ASP D  1 35  ? 18.503  -8.332  -21.276 1.00 13.43 ? 35  ASP D CA  1 
ATOM   6721 C  C   . ASP D  1 35  ? 17.739  -7.140  -20.851 1.00 13.78 ? 35  ASP D C   1 
ATOM   6722 O  O   . ASP D  1 35  ? 17.809  -6.714  -19.683 1.00 16.80 ? 35  ASP D O   1 
ATOM   6723 C  CB  . ASP D  1 35  ? 20.016  -7.850  -21.487 1.00 15.76 ? 35  ASP D CB  1 
ATOM   6724 C  CG  . ASP D  1 35  ? 20.890  -8.871  -22.181 1.00 18.47 ? 35  ASP D CG  1 
ATOM   6725 O  OD1 . ASP D  1 35  ? 21.866  -9.320  -21.549 1.00 16.62 ? 35  ASP D OD1 1 
ATOM   6726 O  OD2 . ASP D  1 35  ? 20.641  -9.200  -23.359 1.00 20.82 ? 35  ASP D OD2 1 
ATOM   6727 N  N   . ILE D  1 36  ? 16.976  -6.498  -21.804 1.00 11.61 ? 36  ILE D N   1 
ATOM   6728 C  CA  . ILE D  1 36  ? 16.299  -5.267  -21.412 1.00 11.80 ? 36  ILE D CA  1 
ATOM   6729 C  C   . ILE D  1 36  ? 14.804  -5.430  -21.293 1.00 12.13 ? 36  ILE D C   1 
ATOM   6730 O  O   . ILE D  1 36  ? 14.095  -4.414  -21.129 1.00 14.06 ? 36  ILE D O   1 
ATOM   6731 C  CB  . ILE D  1 36  ? 16.732  -4.058  -22.240 1.00 13.97 ? 36  ILE D CB  1 
ATOM   6732 C  CG1 . ILE D  1 36  ? 16.580  -4.295  -23.760 1.00 15.87 ? 36  ILE D CG1 1 
ATOM   6733 C  CG2 . ILE D  1 36  ? 18.201  -3.745  -21.872 1.00 17.14 ? 36  ILE D CG2 1 
ATOM   6734 C  CD1 . ILE D  1 36  ? 15.184  -4.440  -24.282 1.00 15.07 ? 36  ILE D CD1 1 
ATOM   6735 N  N   . LEU D  1 37  ? 14.330  -6.688  -21.408 1.00 11.95 ? 37  LEU D N   1 
ATOM   6736 C  CA  . LEU D  1 37  ? 12.857  -6.994  -21.329 1.00 12.74 ? 37  LEU D CA  1 
ATOM   6737 C  C   . LEU D  1 37  ? 12.488  -7.317  -19.909 1.00 14.07 ? 37  LEU D C   1 
ATOM   6738 O  O   . LEU D  1 37  ? 13.251  -7.987  -19.184 1.00 15.54 ? 37  LEU D O   1 
ATOM   6739 C  CB  . LEU D  1 37  ? 12.469  -8.191  -22.182 1.00 13.18 ? 37  LEU D CB  1 
ATOM   6740 C  CG  . LEU D  1 37  ? 12.775  -8.011  -23.676 1.00 13.20 ? 37  LEU D CG  1 
ATOM   6741 C  CD1 . LEU D  1 37  ? 12.417  -9.250  -24.410 1.00 17.33 ? 37  LEU D CD1 1 
ATOM   6742 C  CD2 . LEU D  1 37  ? 12.063  -6.826  -24.287 1.00 13.82 ? 37  LEU D CD2 1 
ATOM   6743 N  N   . GLN D  1 38  ? 11.344  -6.822  -19.507 1.00 12.61 ? 38  GLN D N   1 
ATOM   6744 C  CA  . GLN D  1 38  ? 10.836  -7.175  -18.156 1.00 13.07 ? 38  GLN D CA  1 
ATOM   6745 C  C   . GLN D  1 38  ? 9.326   -7.370  -18.220 1.00 12.07 ? 38  GLN D C   1 
ATOM   6746 O  O   . GLN D  1 38  ? 8.611   -6.447  -18.642 1.00 11.76 ? 38  GLN D O   1 
ATOM   6747 C  CB  . GLN D  1 38  ? 11.166  -6.069  -17.236 1.00 14.88 ? 38  GLN D CB  1 
ATOM   6748 C  CG  . GLN D  1 38  ? 10.801  -6.500  -15.797 1.00 20.43 ? 38  GLN D CG  1 
ATOM   6749 C  CD  . GLN D  1 38  ? 11.379  -5.566  -14.832 1.00 21.92 ? 38  GLN D CD  1 
ATOM   6750 O  OE1 . GLN D  1 38  ? 12.586  -5.625  -14.588 1.00 26.64 ? 38  GLN D OE1 1 
ATOM   6751 N  NE2 . GLN D  1 38  ? 10.604  -4.649  -14.339 1.00 24.92 ? 38  GLN D NE2 1 
ATOM   6752 N  N   . TYR D  1 39  ? 8.773   -8.496  -17.728 1.00 12.09 ? 39  TYR D N   1 
ATOM   6753 C  CA  . TYR D  1 39  ? 7.318   -8.755  -17.750 1.00 11.32 ? 39  TYR D CA  1 
ATOM   6754 C  C   . TYR D  1 39  ? 6.650   -7.755  -16.773 1.00 11.18 ? 39  TYR D C   1 
ATOM   6755 O  O   . TYR D  1 39  ? 7.182   -7.505  -15.701 1.00 12.72 ? 39  TYR D O   1 
ATOM   6756 C  CB  . TYR D  1 39  ? 7.136   -10.197 -17.239 1.00 12.27 ? 39  TYR D CB  1 
ATOM   6757 C  CG  . TYR D  1 39  ? 5.656   -10.467 -16.979 1.00 12.37 ? 39  TYR D CG  1 
ATOM   6758 C  CD1 . TYR D  1 39  ? 4.679   -10.534 -18.019 1.00 14.33 ? 39  TYR D CD1 1 
ATOM   6759 C  CD2 . TYR D  1 39  ? 5.200   -10.664 -15.647 1.00 13.07 ? 39  TYR D CD2 1 
ATOM   6760 C  CE1 . TYR D  1 39  ? 3.318   -10.720 -17.767 1.00 13.28 ? 39  TYR D CE1 1 
ATOM   6761 C  CE2 . TYR D  1 39  ? 3.861   -10.883 -15.417 1.00 13.86 ? 39  TYR D CE2 1 
ATOM   6762 C  CZ  . TYR D  1 39  ? 2.939   -10.882 -16.408 1.00 13.12 ? 39  TYR D CZ  1 
ATOM   6763 O  OH  . TYR D  1 39  ? 1.594   -11.125 -16.231 1.00 15.68 ? 39  TYR D OH  1 
ATOM   6764 N  N   . ASP D  1 40  ? 5.512   -7.188  -17.182 1.00 10.89 ? 40  ASP D N   1 
ATOM   6765 C  CA  . ASP D  1 40  ? 4.725   -6.277  -16.332 1.00 10.61 ? 40  ASP D CA  1 
ATOM   6766 C  C   . ASP D  1 40  ? 3.334   -6.715  -16.446 1.00 11.21 ? 40  ASP D C   1 
ATOM   6767 O  O   . ASP D  1 40  ? 2.653   -6.605  -17.491 1.00 11.57 ? 40  ASP D O   1 
ATOM   6768 C  CB  . ASP D  1 40  ? 4.966   -4.883  -16.917 1.00 11.52 ? 40  ASP D CB  1 
ATOM   6769 C  CG  . ASP D  1 40  ? 4.270   -3.797  -16.175 1.00 17.15 ? 40  ASP D CG  1 
ATOM   6770 O  OD1 . ASP D  1 40  ? 3.456   -4.045  -15.247 1.00 13.43 ? 40  ASP D OD1 1 
ATOM   6771 O  OD2 . ASP D  1 40  ? 4.452   -2.613  -16.562 1.00 19.86 ? 40  ASP D OD2 1 
ATOM   6772 N  N   . ALA D  1 41  ? 2.816   -7.187  -15.265 1.00 9.72  ? 41  ALA D N   1 
ATOM   6773 C  CA  . ALA D  1 41  ? 1.423   -7.617  -15.226 1.00 11.99 ? 41  ALA D CA  1 
ATOM   6774 C  C   . ALA D  1 41  ? 0.363   -6.485  -15.340 1.00 11.65 ? 41  ALA D C   1 
ATOM   6775 O  O   . ALA D  1 41  ? -0.813  -6.766  -15.581 1.00 13.78 ? 41  ALA D O   1 
ATOM   6776 C  CB  . ALA D  1 41  ? 1.192   -8.351  -13.905 1.00 13.08 ? 41  ALA D CB  1 
ATOM   6777 N  N   . SER D  1 42  ? 0.818   -5.226  -15.364 1.00 11.22 ? 42  SER D N   1 
ATOM   6778 C  CA  . SER D  1 42  ? -0.057  -4.077  -15.561 1.00 12.90 ? 42  SER D CA  1 
ATOM   6779 C  C   . SER D  1 42  ? -0.486  -3.927  -17.020 1.00 13.64 ? 42  SER D C   1 
ATOM   6780 O  O   . SER D  1 42  ? -1.324  -3.041  -17.344 1.00 16.87 ? 42  SER D O   1 
ATOM   6781 C  CB  . SER D  1 42  ? 0.510   -2.801  -14.951 1.00 15.47 ? 42  SER D CB  1 
ATOM   6782 O  OG  . SER D  1 42  ? 1.427   -2.242  -15.860 1.00 18.58 ? 42  SER D OG  1 
ATOM   6783 N  N   . LEU D  1 43  ? 0.214   -4.670  -17.912 1.00 12.78 ? 43  LEU D N   1 
ATOM   6784 C  CA  . LEU D  1 43  ? 0.049   -4.482  -19.351 1.00 14.08 ? 43  LEU D CA  1 
ATOM   6785 C  C   . LEU D  1 43  ? -1.033  -5.365  -19.799 1.00 12.66 ? 43  LEU D C   1 
ATOM   6786 O  O   . LEU D  1 43  ? -0.920  -6.442  -20.351 1.00 13.16 ? 43  LEU D O   1 
ATOM   6787 C  CB  . LEU D  1 43  ? 1.395   -4.775  -20.056 1.00 11.20 ? 43  LEU D CB  1 
ATOM   6788 C  CG  . LEU D  1 43  ? 2.481   -3.799  -19.777 1.00 12.83 ? 43  LEU D CG  1 
ATOM   6789 C  CD1 . LEU D  1 43  ? 3.709   -4.297  -20.568 1.00 13.12 ? 43  LEU D CD1 1 
ATOM   6790 C  CD2 . LEU D  1 43  ? 2.180   -2.300  -20.047 1.00 15.67 ? 43  LEU D CD2 1 
ATOM   6791 N  N   . THR D  1 44  ? -2.262  -4.788  -19.664 1.00 13.70 ? 44  THR D N   1 
ATOM   6792 C  CA  . THR D  1 44  ? -3.492  -5.467  -20.009 1.00 14.15 ? 44  THR D CA  1 
ATOM   6793 C  C   . THR D  1 44  ? -3.850  -5.298  -21.519 1.00 12.76 ? 44  THR D C   1 
ATOM   6794 O  O   . THR D  1 44  ? -3.264  -4.436  -22.150 1.00 12.53 ? 44  THR D O   1 
ATOM   6795 C  CB  . THR D  1 44  ? -4.663  -4.897  -19.097 1.00 12.64 ? 44  THR D CB  1 
ATOM   6796 O  OG1 . THR D  1 44  ? -4.661  -3.502  -19.148 1.00 19.39 ? 44  THR D OG1 1 
ATOM   6797 C  CG2 . THR D  1 44  ? -4.387  -5.208  -17.575 1.00 18.93 ? 44  THR D CG2 1 
ATOM   6798 N  N   . PRO D  1 45  ? -4.817  -6.036  -22.041 1.00 14.00 ? 45  PRO D N   1 
ATOM   6799 C  CA  . PRO D  1 45  ? -5.043  -6.010  -23.518 1.00 14.38 ? 45  PRO D CA  1 
ATOM   6800 C  C   . PRO D  1 45  ? -5.662  -4.719  -23.972 1.00 16.01 ? 45  PRO D C   1 
ATOM   6801 O  O   . PRO D  1 45  ? -6.513  -4.147  -23.290 1.00 18.96 ? 45  PRO D O   1 
ATOM   6802 C  CB  . PRO D  1 45  ? -5.997  -7.177  -23.746 1.00 17.49 ? 45  PRO D CB  1 
ATOM   6803 C  CG  . PRO D  1 45  ? -5.776  -8.083  -22.496 1.00 16.88 ? 45  PRO D CG  1 
ATOM   6804 C  CD  . PRO D  1 45  ? -5.557  -7.118  -21.373 1.00 15.92 ? 45  PRO D CD  1 
ATOM   6805 N  N   . LEU D  1 46  ? -5.146  -4.178  -25.067 1.00 14.11 ? 46  LEU D N   1 
ATOM   6806 C  CA  . LEU D  1 46  ? -5.742  -2.988  -25.671 1.00 14.06 ? 46  LEU D CA  1 
ATOM   6807 C  C   . LEU D  1 46  ? -7.024  -3.384  -26.358 1.00 13.41 ? 46  LEU D C   1 
ATOM   6808 O  O   . LEU D  1 46  ? -7.210  -4.526  -26.849 1.00 15.08 ? 46  LEU D O   1 
ATOM   6809 C  CB  . LEU D  1 46  ? -4.843  -2.390  -26.725 1.00 16.08 ? 46  LEU D CB  1 
ATOM   6810 C  CG  . LEU D  1 46  ? -3.559  -1.793  -26.143 1.00 16.94 ? 46  LEU D CG  1 
ATOM   6811 C  CD1 . LEU D  1 46  ? -2.632  -1.390  -27.280 1.00 21.22 ? 46  LEU D CD1 1 
ATOM   6812 C  CD2 . LEU D  1 46  ? -3.794  -0.536  -25.311 1.00 22.27 ? 46  LEU D CD2 1 
ATOM   6813 N  N   . GLU D  1 47  ? -7.931  -2.413  -26.388 1.00 14.18 ? 47  GLU D N   1 
ATOM   6814 C  CA  . GLU D  1 47  ? -9.088  -2.578  -27.204 1.00 14.83 ? 47  GLU D CA  1 
ATOM   6815 C  C   . GLU D  1 47  ? -9.060  -1.547  -28.389 1.00 13.79 ? 47  GLU D C   1 
ATOM   6816 O  O   . GLU D  1 47  ? -8.722  -0.339  -28.193 1.00 15.28 ? 47  GLU D O   1 
ATOM   6817 C  CB  . GLU D  1 47  ? -10.431 -2.452  -26.404 1.00 21.73 ? 47  GLU D CB  1 
ATOM   6818 C  CG  . GLU D  1 47  ? -10.779 -3.584  -25.382 1.00 29.90 ? 47  GLU D CG  1 
ATOM   6819 C  CD  . GLU D  1 47  ? -12.264 -3.536  -24.935 1.00 41.37 ? 47  GLU D CD  1 
ATOM   6820 O  OE1 . GLU D  1 47  ? -13.093 -2.849  -25.624 1.00 46.30 ? 47  GLU D OE1 1 
ATOM   6821 O  OE2 . GLU D  1 47  ? -12.594 -4.140  -23.877 1.00 46.81 ? 47  GLU D OE2 1 
ATOM   6822 N  N   . PHE D  1 48  ? -9.394  -2.067  -29.542 1.00 14.08 ? 48  PHE D N   1 
ATOM   6823 C  CA  . PHE D  1 48  ? -9.350  -1.294  -30.796 1.00 15.37 ? 48  PHE D CA  1 
ATOM   6824 C  C   . PHE D  1 48  ? -10.767 -0.918  -31.125 1.00 17.69 ? 48  PHE D C   1 
ATOM   6825 O  O   . PHE D  1 48  ? -11.495 -1.791  -31.566 1.00 20.21 ? 48  PHE D O   1 
ATOM   6826 C  CB  . PHE D  1 48  ? -8.644  -2.148  -31.908 1.00 14.84 ? 48  PHE D CB  1 
ATOM   6827 C  CG  . PHE D  1 48  ? -7.342  -2.693  -31.448 1.00 14.60 ? 48  PHE D CG  1 
ATOM   6828 C  CD1 . PHE D  1 48  ? -6.281  -1.898  -31.208 1.00 13.34 ? 48  PHE D CD1 1 
ATOM   6829 C  CD2 . PHE D  1 48  ? -7.220  -4.058  -31.137 1.00 15.90 ? 48  PHE D CD2 1 
ATOM   6830 C  CE1 . PHE D  1 48  ? -5.099  -2.345  -30.673 1.00 15.53 ? 48  PHE D CE1 1 
ATOM   6831 C  CE2 . PHE D  1 48  ? -6.023  -4.561  -30.607 1.00 14.59 ? 48  PHE D CE2 1 
ATOM   6832 C  CZ  . PHE D  1 48  ? -4.932  -3.688  -30.383 1.00 12.70 ? 48  PHE D CZ  1 
ATOM   6833 N  N   . GLN D  1 49  ? -11.116 0.361   -31.033 1.00 13.58 ? 49  GLN D N   1 
ATOM   6834 C  CA  . GLN D  1 49  ? -12.509 0.798   -31.221 1.00 16.57 ? 49  GLN D CA  1 
ATOM   6835 C  C   . GLN D  1 49  ? -12.602 1.612   -32.471 1.00 13.73 ? 49  GLN D C   1 
ATOM   6836 O  O   . GLN D  1 49  ? -11.832 2.548   -32.722 1.00 13.60 ? 49  GLN D O   1 
ATOM   6837 C  CB  . GLN D  1 49  ? -12.988 1.690   -30.074 1.00 20.23 ? 49  GLN D CB  1 
ATOM   6838 C  CG  . GLN D  1 49  ? -12.815 1.133   -28.634 1.00 26.96 ? 49  GLN D CG  1 
ATOM   6839 C  CD  . GLN D  1 49  ? -13.573 -0.179  -28.304 1.00 39.29 ? 49  GLN D CD  1 
ATOM   6840 O  OE1 . GLN D  1 49  ? -14.089 -0.870  -29.187 1.00 46.49 ? 49  GLN D OE1 1 
ATOM   6841 N  NE2 . GLN D  1 49  ? -13.607 -0.540  -27.001 1.00 40.82 ? 49  GLN D NE2 1 
ATOM   6842 N  N   . GLY D  1 50  ? -13.628 1.338   -33.275 1.00 12.35 ? 50  GLY D N   1 
ATOM   6843 C  CA  . GLY D  1 50  ? -13.860 2.115   -34.441 1.00 12.95 ? 50  GLY D CA  1 
ATOM   6844 C  C   . GLY D  1 50  ? -12.843 1.845   -35.561 1.00 11.18 ? 50  GLY D C   1 
ATOM   6845 O  O   . GLY D  1 50  ? -12.741 2.683   -36.465 1.00 12.32 ? 50  GLY D O   1 
ATOM   6846 N  N   . TYR D  1 51  ? -12.162 0.702   -35.448 1.00 10.20 ? 51  TYR D N   1 
ATOM   6847 C  CA  . TYR D  1 51  ? -11.147 0.342   -36.510 1.00 11.09 ? 51  TYR D CA  1 
ATOM   6848 C  C   . TYR D  1 51  ? -11.806 -0.191  -37.787 1.00 11.13 ? 51  TYR D C   1 
ATOM   6849 O  O   . TYR D  1 51  ? -11.197 -0.282  -38.844 1.00 10.87 ? 51  TYR D O   1 
ATOM   6850 C  CB  . TYR D  1 51  ? -10.157 -0.720  -35.961 1.00 10.77 ? 51  TYR D CB  1 
ATOM   6851 C  CG  . TYR D  1 51  ? -8.951  -0.158  -35.250 1.00 9.39  ? 51  TYR D CG  1 
ATOM   6852 C  CD1 . TYR D  1 51  ? -7.676  -0.628  -35.533 1.00 10.81 ? 51  TYR D CD1 1 
ATOM   6853 C  CD2 . TYR D  1 51  ? -9.086  0.832   -34.288 1.00 11.72 ? 51  TYR D CD2 1 
ATOM   6854 C  CE1 . TYR D  1 51  ? -6.567  -0.122  -34.882 1.00 10.90 ? 51  TYR D CE1 1 
ATOM   6855 C  CE2 . TYR D  1 51  ? -7.984  1.345   -33.632 1.00 11.15 ? 51  TYR D CE2 1 
ATOM   6856 C  CZ  . TYR D  1 51  ? -6.728  0.864   -33.933 1.00 11.97 ? 51  TYR D CZ  1 
ATOM   6857 O  OH  . TYR D  1 51  ? -5.629  1.372   -33.282 1.00 12.16 ? 51  TYR D OH  1 
ATOM   6858 N  N   . ASN D  1 52  ? -13.132 -0.585  -37.721 1.00 13.23 ? 52  ASN D N   1 
ATOM   6859 C  CA  . ASN D  1 52  ? -13.758 -1.173  -38.859 1.00 13.57 ? 52  ASN D CA  1 
ATOM   6860 C  C   . ASN D  1 52  ? -14.364 -0.070  -39.678 1.00 14.30 ? 52  ASN D C   1 
ATOM   6861 O  O   . ASN D  1 52  ? -15.534 0.361   -39.519 1.00 16.31 ? 52  ASN D O   1 
ATOM   6862 C  CB  . ASN D  1 52  ? -14.824 -2.152  -38.416 1.00 15.19 ? 52  ASN D CB  1 
ATOM   6863 C  CG  . ASN D  1 52  ? -15.386 -2.936  -39.550 1.00 18.11 ? 52  ASN D CG  1 
ATOM   6864 O  OD1 . ASN D  1 52  ? -15.179 -2.642  -40.663 1.00 18.31 ? 52  ASN D OD1 1 
ATOM   6865 N  ND2 . ASN D  1 52  ? -16.288 -3.842  -39.225 1.00 24.29 ? 52  ASN D ND2 1 
ATOM   6866 N  N   . LEU D  1 53  ? -13.584 0.482   -40.584 1.00 12.01 ? 53  LEU D N   1 
ATOM   6867 C  CA  . LEU D  1 53  ? -14.003 1.668   -41.383 1.00 12.49 ? 53  LEU D CA  1 
ATOM   6868 C  C   . LEU D  1 53  ? -14.956 1.220   -42.516 1.00 14.50 ? 53  LEU D C   1 
ATOM   6869 O  O   . LEU D  1 53  ? -14.709 0.199   -43.163 1.00 14.57 ? 53  LEU D O   1 
ATOM   6870 C  CB  . LEU D  1 53  ? -12.775 2.378   -41.990 1.00 14.21 ? 53  LEU D CB  1 
ATOM   6871 C  CG  . LEU D  1 53  ? -11.699 2.745   -40.946 1.00 14.31 ? 53  LEU D CG  1 
ATOM   6872 C  CD1 . LEU D  1 53  ? -10.533 3.422   -41.639 1.00 16.52 ? 53  LEU D CD1 1 
ATOM   6873 C  CD2 . LEU D  1 53  ? -12.171 3.618   -39.795 1.00 15.33 ? 53  LEU D CD2 1 
ATOM   6874 N  N   . SER D  1 54  ? -15.947 2.027   -42.757 1.00 13.36 ? 54  SER D N   1 
ATOM   6875 C  CA  . SER D  1 54  ? -16.957 1.623   -43.743 1.00 14.66 ? 54  SER D CA  1 
ATOM   6876 C  C   . SER D  1 54  ? -16.326 1.630   -45.157 1.00 14.57 ? 54  SER D C   1 
ATOM   6877 O  O   . SER D  1 54  ? -15.741 2.655   -45.582 1.00 13.49 ? 54  SER D O   1 
ATOM   6878 C  CB  . SER D  1 54  ? -18.125 2.605   -43.689 1.00 14.98 ? 54  SER D CB  1 
ATOM   6879 O  OG  . SER D  1 54  ? -18.987 2.221   -44.799 1.00 16.77 ? 54  SER D OG  1 
ATOM   6880 N  N   . ALA D  1 55  ? -16.671 0.565   -45.877 1.00 16.53 ? 55  ALA D N   1 
ATOM   6881 C  CA  . ALA D  1 55  ? -16.243 0.413   -47.317 1.00 18.81 ? 55  ALA D CA  1 
ATOM   6882 C  C   . ALA D  1 55  ? -16.903 1.467   -48.205 1.00 18.05 ? 55  ALA D C   1 
ATOM   6883 O  O   . ALA D  1 55  ? -16.471 1.717   -49.329 1.00 19.88 ? 55  ALA D O   1 
ATOM   6884 C  CB  . ALA D  1 55  ? -16.532 -1.005  -47.857 1.00 22.18 ? 55  ALA D CB  1 
ATOM   6885 N  N   . ASN D  1 56  ? -17.941 2.167   -47.728 1.00 18.20 ? 56  ASN D N   1 
ATOM   6886 C  CA  . ASN D  1 56  ? -18.529 3.282   -48.422 1.00 18.80 ? 56  ASN D CA  1 
ATOM   6887 C  C   . ASN D  1 56  ? -18.022 4.676   -48.113 1.00 20.42 ? 56  ASN D C   1 
ATOM   6888 O  O   . ASN D  1 56  ? -18.405 5.680   -48.741 1.00 20.93 ? 56  ASN D O   1 
ATOM   6889 C  CB  . ASN D  1 56  ? -20.056 3.285   -48.101 1.00 23.01 ? 56  ASN D CB  1 
ATOM   6890 C  CG  . ASN D  1 56  ? -20.840 2.277   -48.889 1.00 33.98 ? 56  ASN D CG  1 
ATOM   6891 O  OD1 . ASN D  1 56  ? -20.384 1.755   -49.900 1.00 30.90 ? 56  ASN D OD1 1 
ATOM   6892 N  ND2 . ASN D  1 56  ? -22.100 2.068   -48.475 1.00 41.14 ? 56  ASN D ND2 1 
ATOM   6893 N  N   . LYS D  1 57  ? -17.077 4.743   -47.178 1.00 16.27 ? 57  LYS D N   1 
ATOM   6894 C  CA  . LYS D  1 57  ? -16.411 5.979   -46.924 1.00 15.31 ? 57  LYS D CA  1 
ATOM   6895 C  C   . LYS D  1 57  ? -14.967 5.851   -47.490 1.00 14.89 ? 57  LYS D C   1 
ATOM   6896 O  O   . LYS D  1 57  ? -14.606 4.757   -48.008 1.00 14.46 ? 57  LYS D O   1 
ATOM   6897 C  CB  . LYS D  1 57  ? -16.329 6.203   -45.424 1.00 16.60 ? 57  LYS D CB  1 
ATOM   6898 C  CG  . LYS D  1 57  ? -17.702 6.531   -44.814 1.00 18.48 ? 57  LYS D CG  1 
ATOM   6899 C  CD  . LYS D  1 57  ? -17.460 6.928   -43.365 1.00 24.17 ? 57  LYS D CD  1 
ATOM   6900 C  CE  . LYS D  1 57  ? -18.709 7.503   -42.720 1.00 27.26 ? 57  LYS D CE  1 
ATOM   6901 N  NZ  . LYS D  1 57  ? -18.505 7.738   -41.247 1.00 28.26 ? 57  LYS D NZ  1 
ATOM   6902 N  N   . GLN D  1 58  ? -14.327 7.021   -47.603 1.00 16.45 ? 58  GLN D N   1 
ATOM   6903 C  CA  . GLN D  1 58  ? -12.990 6.950   -48.246 1.00 16.00 ? 58  GLN D CA  1 
ATOM   6904 C  C   . GLN D  1 58  ? -12.068 7.819   -47.408 1.00 13.64 ? 58  GLN D C   1 
ATOM   6905 O  O   . GLN D  1 58  ? -12.418 8.758   -46.734 1.00 15.09 ? 58  GLN D O   1 
ATOM   6906 C  CB  . GLN D  1 58  ? -12.993 7.302   -49.721 1.00 20.40 ? 58  GLN D CB  1 
ATOM   6907 C  CG  . GLN D  1 58  ? -13.564 8.608   -49.980 1.00 21.61 ? 58  GLN D CG  1 
ATOM   6908 C  CD  . GLN D  1 58  ? -13.615 8.950   -51.501 1.00 25.88 ? 58  GLN D CD  1 
ATOM   6909 O  OE1 . GLN D  1 58  ? -13.333 8.114   -52.400 1.00 25.40 ? 58  GLN D OE1 1 
ATOM   6910 N  NE2 . GLN D  1 58  ? -13.827 10.253  -51.751 1.00 26.96 ? 58  GLN D NE2 1 
ATOM   6911 N  N   . PHE D  1 59  ? -10.789 7.427   -47.436 1.00 11.28 ? 59  PHE D N   1 
ATOM   6912 C  CA  . PHE D  1 59  ? -9.702  7.965   -46.547 1.00 11.28 ? 59  PHE D CA  1 
ATOM   6913 C  C   . PHE D  1 59  ? -8.537  8.329   -47.395 1.00 10.26 ? 59  PHE D C   1 
ATOM   6914 O  O   . PHE D  1 59  ? -8.210  7.661   -48.391 1.00 11.92 ? 59  PHE D O   1 
ATOM   6915 C  CB  . PHE D  1 59  ? -9.392  6.838   -45.554 1.00 11.78 ? 59  PHE D CB  1 
ATOM   6916 C  CG  . PHE D  1 59  ? -10.601 6.541   -44.703 1.00 12.28 ? 59  PHE D CG  1 
ATOM   6917 C  CD1 . PHE D  1 59  ? -11.532 5.538   -45.147 1.00 12.00 ? 59  PHE D CD1 1 
ATOM   6918 C  CD2 . PHE D  1 59  ? -10.901 7.312   -43.543 1.00 13.66 ? 59  PHE D CD2 1 
ATOM   6919 C  CE1 . PHE D  1 59  ? -12.753 5.300   -44.425 1.00 11.86 ? 59  PHE D CE1 1 
ATOM   6920 C  CE2 . PHE D  1 59  ? -12.072 7.058   -42.889 1.00 12.95 ? 59  PHE D CE2 1 
ATOM   6921 C  CZ  . PHE D  1 59  ? -12.987 6.096   -43.264 1.00 13.29 ? 59  PHE D CZ  1 
ATOM   6922 N  N   . LEU D  1 60  ? -7.939  9.473   -47.078 1.00 10.24 ? 60  LEU D N   1 
ATOM   6923 C  CA  . LEU D  1 60  ? -6.873  10.063  -47.876 1.00 11.17 ? 60  LEU D CA  1 
ATOM   6924 C  C   . LEU D  1 60  ? -5.531  9.417   -47.694 1.00 10.83 ? 60  LEU D C   1 
ATOM   6925 O  O   . LEU D  1 60  ? -4.979  9.384   -46.578 1.00 10.98 ? 60  LEU D O   1 
ATOM   6926 C  CB  . LEU D  1 60  ? -6.800  11.560  -47.506 1.00 13.18 ? 60  LEU D CB  1 
ATOM   6927 C  CG  . LEU D  1 60  ? -6.062  12.335  -48.526 1.00 16.36 ? 60  LEU D CG  1 
ATOM   6928 C  CD1 . LEU D  1 60  ? -6.865  12.448  -49.814 1.00 17.94 ? 60  LEU D CD1 1 
ATOM   6929 C  CD2 . LEU D  1 60  ? -5.833  13.697  -47.901 1.00 19.58 ? 60  LEU D CD2 1 
ATOM   6930 N  N   . LEU D  1 61  ? -4.959  8.972   -48.776 1.00 11.23 ? 61  LEU D N   1 
ATOM   6931 C  CA  . LEU D  1 61  ? -3.582  8.465   -48.858 1.00 10.33 ? 61  LEU D CA  1 
ATOM   6932 C  C   . LEU D  1 61  ? -2.692  9.518   -49.458 1.00 11.71 ? 61  LEU D C   1 
ATOM   6933 O  O   . LEU D  1 61  ? -3.052  10.124  -50.496 1.00 13.17 ? 61  LEU D O   1 
ATOM   6934 C  CB  . LEU D  1 61  ? -3.613  7.162   -49.695 1.00 12.29 ? 61  LEU D CB  1 
ATOM   6935 C  CG  . LEU D  1 61  ? -2.334  6.347   -49.755 1.00 12.47 ? 61  LEU D CG  1 
ATOM   6936 C  CD1 . LEU D  1 61  ? -2.187  5.598   -48.463 1.00 11.90 ? 61  LEU D CD1 1 
ATOM   6937 C  CD2 . LEU D  1 61  ? -2.425  5.394   -50.938 1.00 13.45 ? 61  LEU D CD2 1 
ATOM   6938 N  N   . THR D  1 62  ? -1.548  9.789   -48.840 1.00 11.43 ? 62  THR D N   1 
ATOM   6939 C  CA  . THR D  1 62  ? -0.701  10.914  -49.291 1.00 11.66 ? 62  THR D CA  1 
ATOM   6940 C  C   . THR D  1 62  ? 0.754   10.418  -49.257 1.00 12.21 ? 62  THR D C   1 
ATOM   6941 O  O   . THR D  1 62  ? 1.209   9.734   -48.311 1.00 12.36 ? 62  THR D O   1 
ATOM   6942 C  CB  . THR D  1 62  ? -0.754  12.082  -48.296 1.00 15.20 ? 62  THR D CB  1 
ATOM   6943 O  OG1 . THR D  1 62  ? -2.102  12.551  -48.127 1.00 21.58 ? 62  THR D OG1 1 
ATOM   6944 C  CG2 . THR D  1 62  ? 0.010   13.303  -48.889 1.00 18.48 ? 62  THR D CG2 1 
ATOM   6945 N  N   . ASN D  1 63  ? 1.518   10.789  -50.251 1.00 10.52 ? 63  ASN D N   1 
ATOM   6946 C  CA  . ASN D  1 63  ? 3.002   10.735  -50.176 1.00 10.68 ? 63  ASN D CA  1 
ATOM   6947 C  C   . ASN D  1 63  ? 3.512   12.014  -49.573 1.00 11.95 ? 63  ASN D C   1 
ATOM   6948 O  O   . ASN D  1 63  ? 3.383   13.131  -50.174 1.00 12.59 ? 63  ASN D O   1 
ATOM   6949 C  CB  . ASN D  1 63  ? 3.476   10.480  -51.646 1.00 12.58 ? 63  ASN D CB  1 
ATOM   6950 C  CG  . ASN D  1 63  ? 4.999   10.548  -51.773 1.00 12.24 ? 63  ASN D CG  1 
ATOM   6951 O  OD1 . ASN D  1 63  ? 5.692   11.109  -50.923 1.00 10.84 ? 63  ASN D OD1 1 
ATOM   6952 N  ND2 . ASN D  1 63  ? 5.518   9.867   -52.801 1.00 11.27 ? 63  ASN D ND2 1 
ATOM   6953 N  N   . ASN D  1 64  ? 4.095   11.964  -48.379 1.00 11.73 ? 64  ASN D N   1 
ATOM   6954 C  CA  . ASN D  1 64  ? 4.503   13.205  -47.691 1.00 12.38 ? 64  ASN D CA  1 
ATOM   6955 C  C   . ASN D  1 64  ? 5.971   13.547  -47.921 1.00 11.56 ? 64  ASN D C   1 
ATOM   6956 O  O   . ASN D  1 64  ? 6.515   14.424  -47.210 1.00 13.14 ? 64  ASN D O   1 
ATOM   6957 C  CB  . ASN D  1 64  ? 4.148   13.172  -46.196 1.00 12.84 ? 64  ASN D CB  1 
ATOM   6958 C  CG  . ASN D  1 64  ? 4.901   12.102  -45.449 1.00 14.43 ? 64  ASN D CG  1 
ATOM   6959 O  OD1 . ASN D  1 64  ? 5.824   11.489  -45.958 1.00 11.82 ? 64  ASN D OD1 1 
ATOM   6960 N  ND2 . ASN D  1 64  ? 4.542   11.909  -44.136 1.00 16.31 ? 64  ASN D ND2 1 
ATOM   6961 N  N   . GLY D  1 65  ? 6.578   12.807  -48.872 1.00 11.31 ? 65  GLY D N   1 
ATOM   6962 C  CA  . GLY D  1 65  ? 8.023   12.964  -49.123 1.00 11.11 ? 65  GLY D CA  1 
ATOM   6963 C  C   . GLY D  1 65  ? 8.920   12.059  -48.269 1.00 12.31 ? 65  GLY D C   1 
ATOM   6964 O  O   . GLY D  1 65  ? 10.125  11.947  -48.543 1.00 11.70 ? 65  GLY D O   1 
ATOM   6965 N  N   . HIS D  1 66  ? 8.314   11.381  -47.272 1.00 11.51 ? 66  HIS D N   1 
ATOM   6966 C  CA  . HIS D  1 66  ? 9.125   10.575  -46.349 1.00 9.97  ? 66  HIS D CA  1 
ATOM   6967 C  C   . HIS D  1 66  ? 8.581   9.147   -46.156 1.00 9.31  ? 66  HIS D C   1 
ATOM   6968 O  O   . HIS D  1 66  ? 9.339   8.227   -45.823 1.00 10.06 ? 66  HIS D O   1 
ATOM   6969 C  CB  . HIS D  1 66  ? 9.239   11.252  -44.955 1.00 10.91 ? 66  HIS D CB  1 
ATOM   6970 C  CG  . HIS D  1 66  ? 9.826   12.669  -45.036 1.00 10.82 ? 66  HIS D CG  1 
ATOM   6971 N  ND1 . HIS D  1 66  ? 11.162  12.897  -45.278 1.00 12.33 ? 66  HIS D ND1 1 
ATOM   6972 C  CD2 . HIS D  1 66  ? 9.215   13.856  -44.844 1.00 12.22 ? 66  HIS D CD2 1 
ATOM   6973 C  CE1 . HIS D  1 66  ? 11.322  14.252  -45.269 1.00 12.76 ? 66  HIS D CE1 1 
ATOM   6974 N  NE2 . HIS D  1 66  ? 10.137  14.811  -45.008 1.00 13.81 ? 66  HIS D NE2 1 
ATOM   6975 N  N   . SER D  1 67  ? 7.249   9.014   -46.337 1.00 9.62  ? 67  SER D N   1 
ATOM   6976 C  CA  . SER D  1 67  ? 6.575   7.708   -46.304 1.00 9.46  ? 67  SER D CA  1 
ATOM   6977 C  C   . SER D  1 67  ? 5.279   7.878   -47.080 1.00 10.42 ? 67  SER D C   1 
ATOM   6978 O  O   . SER D  1 67  ? 5.023   8.950   -47.667 1.00 10.55 ? 67  SER D O   1 
ATOM   6979 C  CB  . SER D  1 67  ? 6.215   7.414   -44.834 1.00 10.05 ? 67  SER D CB  1 
ATOM   6980 O  OG  . SER D  1 67  ? 5.685   6.126   -44.649 1.00 9.67  ? 67  SER D OG  1 
ATOM   6981 N  N   . VAL D  1 68  ? 4.477   6.840   -47.042 1.00 9.77  ? 68  VAL D N   1 
ATOM   6982 C  CA  . VAL D  1 68  ? 3.094   6.916   -47.562 1.00 11.09 ? 68  VAL D CA  1 
ATOM   6983 C  C   . VAL D  1 68  ? 2.212   6.818   -46.321 1.00 10.17 ? 68  VAL D C   1 
ATOM   6984 O  O   . VAL D  1 68  ? 2.379   5.939   -45.502 1.00 9.37  ? 68  VAL D O   1 
ATOM   6985 C  CB  . VAL D  1 68  ? 2.847   5.833   -48.591 1.00 11.61 ? 68  VAL D CB  1 
ATOM   6986 C  CG1 . VAL D  1 68  ? 3.051   4.399   -48.106 1.00 12.15 ? 68  VAL D CG1 1 
ATOM   6987 C  CG2 . VAL D  1 68  ? 1.395   5.949   -49.140 1.00 13.87 ? 68  VAL D CG2 1 
ATOM   6988 N  N   . LYS D  1 69  ? 1.251   7.748   -46.228 1.00 10.34 ? 69  LYS D N   1 
ATOM   6989 C  CA  . LYS D  1 69  ? 0.383   7.807   -45.011 1.00 10.97 ? 69  LYS D CA  1 
ATOM   6990 C  C   . LYS D  1 69  ? -1.081  7.761   -45.402 1.00 9.82  ? 69  LYS D C   1 
ATOM   6991 O  O   . LYS D  1 69  ? -1.453  8.275   -46.457 1.00 11.83 ? 69  LYS D O   1 
ATOM   6992 C  CB  . LYS D  1 69  ? 0.812   9.035   -44.221 1.00 15.58 ? 69  LYS D CB  1 
ATOM   6993 C  CG  . LYS D  1 69  ? 0.208   10.304  -44.565 1.00 19.15 ? 69  LYS D CG  1 
ATOM   6994 C  CD  . LYS D  1 69  ? 0.293   11.287  -43.315 1.00 17.22 ? 69  LYS D CD  1 
ATOM   6995 C  CE  . LYS D  1 69  ? 0.066   12.590  -44.065 1.00 21.18 ? 69  LYS D CE  1 
ATOM   6996 N  NZ  . LYS D  1 69  ? 0.016   13.784  -43.162 1.00 22.76 ? 69  LYS D NZ  1 
ATOM   6997 N  N   . LEU D  1 70  ? -1.863  7.078   -44.596 1.00 8.81  ? 70  LEU D N   1 
ATOM   6998 C  CA  . LEU D  1 70  ? -3.309  7.010   -44.728 1.00 8.95  ? 70  LEU D CA  1 
ATOM   6999 C  C   . LEU D  1 70  ? -3.878  7.772   -43.576 1.00 8.86  ? 70  LEU D C   1 
ATOM   7000 O  O   . LEU D  1 70  ? -3.664  7.417   -42.394 1.00 9.78  ? 70  LEU D O   1 
ATOM   7001 C  CB  . LEU D  1 70  ? -3.764  5.537   -44.719 1.00 9.42  ? 70  LEU D CB  1 
ATOM   7002 C  CG  . LEU D  1 70  ? -5.269  5.331   -44.892 1.00 9.35  ? 70  LEU D CG  1 
ATOM   7003 C  CD1 . LEU D  1 70  ? -5.720  5.829   -46.307 1.00 11.89 ? 70  LEU D CD1 1 
ATOM   7004 C  CD2 . LEU D  1 70  ? -5.634  3.860   -44.696 1.00 11.56 ? 70  LEU D CD2 1 
ATOM   7005 N  N   . ASN D  1 71  ? -4.702  8.779   -43.864 1.00 10.31 ? 71  ASN D N   1 
ATOM   7006 C  CA  . ASN D  1 71  ? -5.398  9.516   -42.772 1.00 10.13 ? 71  ASN D CA  1 
ATOM   7007 C  C   . ASN D  1 71  ? -6.497  8.660   -42.187 1.00 10.99 ? 71  ASN D C   1 
ATOM   7008 O  O   . ASN D  1 71  ? -7.192  7.899   -42.891 1.00 12.35 ? 71  ASN D O   1 
ATOM   7009 C  CB  . ASN D  1 71  ? -5.993  10.843  -43.296 1.00 12.82 ? 71  ASN D CB  1 
ATOM   7010 C  CG  . ASN D  1 71  ? -4.970  11.877  -43.519 1.00 14.02 ? 71  ASN D CG  1 
ATOM   7011 O  OD1 . ASN D  1 71  ? -3.822  11.700  -43.265 1.00 18.71 ? 71  ASN D OD1 1 
ATOM   7012 N  ND2 . ASN D  1 71  ? -5.438  13.064  -44.001 1.00 18.26 ? 71  ASN D ND2 1 
ATOM   7013 N  N   . LEU D  1 72  ? -6.633  8.770   -40.891 1.00 9.76  ? 72  LEU D N   1 
ATOM   7014 C  CA  . LEU D  1 72  ? -7.630  8.009   -40.157 1.00 10.04 ? 72  LEU D CA  1 
ATOM   7015 C  C   . LEU D  1 72  ? -8.594  8.907   -39.336 1.00 10.75 ? 72  LEU D C   1 
ATOM   7016 O  O   . LEU D  1 72  ? -8.201  10.031  -38.996 1.00 11.58 ? 72  LEU D O   1 
ATOM   7017 C  CB  . LEU D  1 72  ? -6.908  7.054   -39.122 1.00 9.36  ? 72  LEU D CB  1 
ATOM   7018 C  CG  . LEU D  1 72  ? -6.032  6.028   -39.829 1.00 10.30 ? 72  LEU D CG  1 
ATOM   7019 C  CD1 . LEU D  1 72  ? -5.109  5.342   -38.789 1.00 10.09 ? 72  LEU D CD1 1 
ATOM   7020 C  CD2 . LEU D  1 72  ? -6.804  4.989   -40.609 1.00 11.54 ? 72  LEU D CD2 1 
ATOM   7021 N  N   . PRO D  1 73  ? -9.822  8.466   -39.120 1.00 11.23 ? 73  PRO D N   1 
ATOM   7022 C  CA  . PRO D  1 73  ? -10.824 9.323   -38.403 1.00 12.59 ? 73  PRO D CA  1 
ATOM   7023 C  C   . PRO D  1 73  ? -10.612 9.349   -36.886 1.00 13.51 ? 73  PRO D C   1 
ATOM   7024 O  O   . PRO D  1 73  ? -10.225 8.323   -36.311 1.00 13.88 ? 73  PRO D O   1 
ATOM   7025 C  CB  . PRO D  1 73  ? -12.126 8.675   -38.831 1.00 13.18 ? 73  PRO D CB  1 
ATOM   7026 C  CG  . PRO D  1 73  ? -11.784 7.182   -38.889 1.00 12.17 ? 73  PRO D CG  1 
ATOM   7027 C  CD  . PRO D  1 73  ? -10.416 7.188   -39.609 1.00 11.52 ? 73  PRO D CD  1 
ATOM   7028 N  N   . SER D  1 74  ? -10.879 10.472  -36.217 1.00 15.86 ? 74  SER D N   1 
ATOM   7029 C  CA  . SER D  1 74  ? -10.688 10.511  -34.784 1.00 16.05 ? 74  SER D CA  1 
ATOM   7030 C  C   . SER D  1 74  ? -11.704 9.679   -34.014 1.00 15.64 ? 74  SER D C   1 
ATOM   7031 O  O   . SER D  1 74  ? -11.384 9.455   -32.816 1.00 18.60 ? 74  SER D O   1 
ATOM   7032 C  CB  . SER D  1 74  ? -10.700 11.972  -34.293 1.00 20.06 ? 74  SER D CB  1 
ATOM   7033 O  OG  . SER D  1 74  ? -11.914 12.613  -34.693 1.00 22.11 ? 74  SER D OG  1 
ATOM   7034 N  N   . ASP D  1 75  ? -12.793 9.193   -34.633 1.00 15.66 ? 75  ASP D N   1 
ATOM   7035 C  CA  . ASP D  1 75  ? -13.634 8.279   -33.929 1.00 19.14 ? 75  ASP D CA  1 
ATOM   7036 C  C   . ASP D  1 75  ? -12.997 6.920   -33.695 1.00 17.43 ? 75  ASP D C   1 
ATOM   7037 O  O   . ASP D  1 75  ? -13.373 6.185   -32.785 1.00 18.77 ? 75  ASP D O   1 
ATOM   7038 C  CB  . ASP D  1 75  ? -15.038 8.197   -34.550 1.00 24.61 ? 75  ASP D CB  1 
ATOM   7039 C  CG  . ASP D  1 75  ? -15.146 7.241   -35.719 1.00 38.34 ? 75  ASP D CG  1 
ATOM   7040 O  OD1 . ASP D  1 75  ? -14.669 7.508   -36.870 1.00 39.24 ? 75  ASP D OD1 1 
ATOM   7041 O  OD2 . ASP D  1 75  ? -15.793 6.189   -35.474 1.00 54.67 ? 75  ASP D OD2 1 
ATOM   7042 N  N   . MET D  1 76  ? -11.927 6.616   -34.430 1.00 13.34 ? 76  MET D N   1 
ATOM   7043 C  CA  . MET D  1 76  ? -11.177 5.363   -34.228 1.00 14.36 ? 76  MET D CA  1 
ATOM   7044 C  C   . MET D  1 76  ? -10.184 5.637   -33.057 1.00 11.85 ? 76  MET D C   1 
ATOM   7045 O  O   . MET D  1 76  ? -9.514  6.658   -32.943 1.00 12.41 ? 76  MET D O   1 
ATOM   7046 C  CB  . MET D  1 76  ? -10.513 5.073   -35.582 1.00 15.57 ? 76  MET D CB  1 
ATOM   7047 C  CG  . MET D  1 76  ? -9.483  4.001   -35.484 1.00 14.44 ? 76  MET D CG  1 
ATOM   7048 S  SD  . MET D  1 76  ? -8.812  3.817   -37.225 1.00 14.56 ? 76  MET D SD  1 
ATOM   7049 C  CE  . MET D  1 76  ? -7.362  2.834   -36.899 1.00 13.30 ? 76  MET D CE  1 
ATOM   7050 N  N   . HIS D  1 77  ? -10.192 4.709   -32.092 1.00 11.87 ? 77  HIS D N   1 
ATOM   7051 C  CA  . HIS D  1 77  ? -9.394  4.927   -30.879 1.00 12.41 ? 77  HIS D CA  1 
ATOM   7052 C  C   . HIS D  1 77  ? -8.928  3.692   -30.196 1.00 12.02 ? 77  HIS D C   1 
ATOM   7053 O  O   . HIS D  1 77  ? -9.468  2.640   -30.485 1.00 13.96 ? 77  HIS D O   1 
ATOM   7054 C  CB  . HIS D  1 77  ? -10.172 5.886   -29.901 1.00 17.32 ? 77  HIS D CB  1 
ATOM   7055 C  CG  . HIS D  1 77  ? -11.405 5.348   -29.335 1.00 19.92 ? 77  HIS D CG  1 
ATOM   7056 N  ND1 . HIS D  1 77  ? -12.618 5.425   -29.989 1.00 20.10 ? 77  HIS D ND1 1 
ATOM   7057 C  CD2 . HIS D  1 77  ? -11.667 4.803   -28.072 1.00 22.88 ? 77  HIS D CD2 1 
ATOM   7058 C  CE1 . HIS D  1 77  ? -13.600 4.845   -29.177 1.00 22.78 ? 77  HIS D CE1 1 
ATOM   7059 N  NE2 . HIS D  1 77  ? -13.008 4.488   -28.013 1.00 24.63 ? 77  HIS D NE2 1 
ATOM   7060 N  N   . ILE D  1 78  ? -7.938  3.842   -29.317 1.00 12.45 ? 78  ILE D N   1 
ATOM   7061 C  CA  . ILE D  1 78  ? -7.539  2.738   -28.461 1.00 14.42 ? 78  ILE D CA  1 
ATOM   7062 C  C   . ILE D  1 78  ? -8.064  3.021   -27.041 1.00 15.31 ? 78  ILE D C   1 
ATOM   7063 O  O   . ILE D  1 78  ? -7.873  4.159   -26.517 1.00 16.58 ? 78  ILE D O   1 
ATOM   7064 C  CB  . ILE D  1 78  ? -5.998  2.662   -28.405 1.00 14.82 ? 78  ILE D CB  1 
ATOM   7065 C  CG1 . ILE D  1 78  ? -5.291  2.278   -29.709 1.00 19.34 ? 78  ILE D CG1 1 
ATOM   7066 C  CG2 . ILE D  1 78  ? -5.546  1.750   -27.283 1.00 19.06 ? 78  ILE D CG2 1 
ATOM   7067 C  CD1 . ILE D  1 78  ? -3.810  2.863   -29.519 1.00 20.53 ? 78  ILE D CD1 1 
ATOM   7068 N  N   . GLN D  1 79  ? -8.433  1.944   -26.393 1.00 16.86 ? 79  GLN D N   1 
ATOM   7069 C  CA  . GLN D  1 79  ? -8.695  1.949   -24.945 1.00 19.44 ? 79  GLN D CA  1 
ATOM   7070 C  C   . GLN D  1 79  ? -7.792  1.037   -24.179 1.00 20.65 ? 79  GLN D C   1 
ATOM   7071 O  O   . GLN D  1 79  ? -7.327  -0.023  -24.705 1.00 20.44 ? 79  GLN D O   1 
ATOM   7072 C  CB  . GLN D  1 79  ? -10.147 1.510   -24.742 1.00 24.93 ? 79  GLN D CB  1 
ATOM   7073 C  CG  . GLN D  1 79  ? -11.202 2.624   -24.957 1.00 33.83 ? 79  GLN D CG  1 
ATOM   7074 C  CD  . GLN D  1 79  ? -10.893 3.957   -24.203 1.00 42.57 ? 79  GLN D CD  1 
ATOM   7075 O  OE1 . GLN D  1 79  ? -11.060 5.064   -24.756 1.00 44.36 ? 79  GLN D OE1 1 
ATOM   7076 N  NE2 . GLN D  1 79  ? -10.442 3.852   -22.936 1.00 44.20 ? 79  GLN D NE2 1 
ATOM   7077 N  N   . GLY D  1 80  ? -7.420  1.455   -22.968 1.00 19.80 ? 80  GLY D N   1 
ATOM   7078 C  CA  . GLY D  1 80  ? -6.553  0.619   -22.209 1.00 19.52 ? 80  GLY D CA  1 
ATOM   7079 C  C   . GLY D  1 80  ? -5.400  1.366   -21.673 1.00 21.66 ? 80  GLY D C   1 
ATOM   7080 O  O   . GLY D  1 80  ? -4.750  0.920   -20.755 1.00 25.03 ? 80  GLY D O   1 
ATOM   7081 N  N   . LEU D  1 81  ? -5.045  2.516   -22.256 1.00 17.24 ? 81  LEU D N   1 
ATOM   7082 C  CA  . LEU D  1 81  ? -3.883  3.205   -21.766 1.00 17.40 ? 81  LEU D CA  1 
ATOM   7083 C  C   . LEU D  1 81  ? -4.350  4.235   -20.714 1.00 14.20 ? 81  LEU D C   1 
ATOM   7084 O  O   . LEU D  1 81  ? -5.505  4.181   -20.305 1.00 16.42 ? 81  LEU D O   1 
ATOM   7085 C  CB  . LEU D  1 81  ? -3.202  3.952   -22.925 1.00 15.59 ? 81  LEU D CB  1 
ATOM   7086 C  CG  . LEU D  1 81  ? -2.727  3.024   -24.071 1.00 15.07 ? 81  LEU D CG  1 
ATOM   7087 C  CD1 . LEU D  1 81  ? -2.240  3.954   -25.208 1.00 18.39 ? 81  LEU D CD1 1 
ATOM   7088 C  CD2 . LEU D  1 81  ? -1.564  2.175   -23.532 1.00 15.65 ? 81  LEU D CD2 1 
ATOM   7089 N  N   . GLN D  1 82  ? -3.459  5.101   -20.265 1.00 13.88 ? 82  GLN D N   1 
ATOM   7090 C  CA  . GLN D  1 82  ? -3.822  6.036   -19.150 1.00 13.15 ? 82  GLN D CA  1 
ATOM   7091 C  C   . GLN D  1 82  ? -4.828  7.093   -19.563 1.00 14.19 ? 82  GLN D C   1 
ATOM   7092 O  O   . GLN D  1 82  ? -5.395  7.712   -18.703 1.00 15.44 ? 82  GLN D O   1 
ATOM   7093 C  CB  . GLN D  1 82  ? -2.571  6.655   -18.565 1.00 14.96 ? 82  GLN D CB  1 
ATOM   7094 C  CG  . GLN D  1 82  ? -2.115  8.003   -19.171 1.00 16.80 ? 82  GLN D CG  1 
ATOM   7095 C  CD  . GLN D  1 82  ? -1.561  7.852   -20.593 1.00 20.44 ? 82  GLN D CD  1 
ATOM   7096 O  OE1 . GLN D  1 82  ? -1.307  6.744   -21.089 1.00 20.19 ? 82  GLN D OE1 1 
ATOM   7097 N  NE2 . GLN D  1 82  ? -1.362  9.005   -21.251 1.00 20.42 ? 82  GLN D NE2 1 
ATOM   7098 N  N   . SER D  1 83  ? -5.022  7.277   -20.869 1.00 12.89 ? 83  SER D N   1 
ATOM   7099 C  CA  . SER D  1 83  ? -5.969  8.308   -21.443 1.00 12.60 ? 83  SER D CA  1 
ATOM   7100 C  C   . SER D  1 83  ? -6.519  7.667   -22.753 1.00 12.58 ? 83  SER D C   1 
ATOM   7101 O  O   . SER D  1 83  ? -5.856  6.688   -23.272 1.00 12.44 ? 83  SER D O   1 
ATOM   7102 C  CB  . SER D  1 83  ? -5.203  9.558   -21.958 1.00 12.25 ? 83  SER D CB  1 
ATOM   7103 O  OG  . SER D  1 83  ? -4.626  10.237  -20.830 1.00 12.93 ? 83  SER D OG  1 
ATOM   7104 N  N   A ARG D  1 84  ? -7.603  8.172   -23.352 0.50 11.42 ? 84  ARG D N   1 
ATOM   7105 N  N   B ARG D  1 84  ? -7.614  8.168   -23.353 0.50 12.61 ? 84  ARG D N   1 
ATOM   7106 C  CA  A ARG D  1 84  ? -8.048  7.783   -24.676 0.50 12.24 ? 84  ARG D CA  1 
ATOM   7107 C  CA  B ARG D  1 84  ? -8.028  7.745   -24.687 0.50 14.22 ? 84  ARG D CA  1 
ATOM   7108 C  C   A ARG D  1 84  ? -7.077  8.387   -25.694 0.50 11.70 ? 84  ARG D C   1 
ATOM   7109 C  C   B ARG D  1 84  ? -7.080  8.379   -25.699 0.50 12.84 ? 84  ARG D C   1 
ATOM   7110 O  O   A ARG D  1 84  ? -6.792  9.609   -25.679 0.50 11.60 ? 84  ARG D O   1 
ATOM   7111 O  O   B ARG D  1 84  ? -6.816  9.604   -25.687 0.50 12.39 ? 84  ARG D O   1 
ATOM   7112 C  CB  A ARG D  1 84  ? -9.444  8.349   -24.957 0.50 11.98 ? 84  ARG D CB  1 
ATOM   7113 C  CB  B ARG D  1 84  ? -9.465  8.147   -25.065 0.50 16.32 ? 84  ARG D CB  1 
ATOM   7114 C  CG  A ARG D  1 84  ? -9.917  8.262   -26.420 0.50 11.96 ? 84  ARG D CG  1 
ATOM   7115 C  CG  B ARG D  1 84  ? -9.780  7.838   -26.554 0.50 19.13 ? 84  ARG D CG  1 
ATOM   7116 C  CD  A ARG D  1 84  ? -11.396 8.711   -26.716 0.50 13.55 ? 84  ARG D CD  1 
ATOM   7117 C  CD  B ARG D  1 84  ? -11.201 8.079   -27.083 0.50 22.39 ? 84  ARG D CD  1 
ATOM   7118 N  NE  A ARG D  1 84  ? -11.489 8.732   -28.171 0.50 13.16 ? 84  ARG D NE  1 
ATOM   7119 N  NE  B ARG D  1 84  ? -12.276 7.596   -26.216 0.50 28.99 ? 84  ARG D NE  1 
ATOM   7120 C  CZ  A ARG D  1 84  ? -12.598 8.505   -28.903 0.50 13.24 ? 84  ARG D CZ  1 
ATOM   7121 C  CZ  B ARG D  1 84  ? -13.581 7.886   -26.412 0.50 31.16 ? 84  ARG D CZ  1 
ATOM   7122 N  NH1 A ARG D  1 84  ? -13.790 8.269   -28.323 0.50 15.15 ? 84  ARG D NH1 1 
ATOM   7123 N  NH1 B ARG D  1 84  ? -13.954 8.646   -27.422 0.50 31.95 ? 84  ARG D NH1 1 
ATOM   7124 N  NH2 A ARG D  1 84  ? -12.555 8.560   -30.254 0.50 12.46 ? 84  ARG D NH2 1 
ATOM   7125 N  NH2 B ARG D  1 84  ? -14.509 7.449   -25.585 0.50 29.59 ? 84  ARG D NH2 1 
ATOM   7126 N  N   . TYR D  1 85  ? -6.607  7.521   -26.603 1.00 11.06 ? 85  TYR D N   1 
ATOM   7127 C  CA  . TYR D  1 85  ? -5.815  7.999   -27.763 1.00 10.28 ? 85  TYR D CA  1 
ATOM   7128 C  C   . TYR D  1 85  ? -6.649  7.737   -28.984 1.00 12.02 ? 85  TYR D C   1 
ATOM   7129 O  O   . TYR D  1 85  ? -7.096  6.646   -29.293 1.00 13.52 ? 85  TYR D O   1 
ATOM   7130 C  CB  . TYR D  1 85  ? -4.487  7.229   -27.781 1.00 10.30 ? 85  TYR D CB  1 
ATOM   7131 C  CG  . TYR D  1 85  ? -3.493  7.719   -26.788 1.00 9.13  ? 85  TYR D CG  1 
ATOM   7132 C  CD1 . TYR D  1 85  ? -2.511  8.639   -27.145 1.00 9.46  ? 85  TYR D CD1 1 
ATOM   7133 C  CD2 . TYR D  1 85  ? -3.495  7.285   -25.424 1.00 10.50 ? 85  TYR D CD2 1 
ATOM   7134 C  CE1 . TYR D  1 85  ? -1.576  9.127   -26.229 1.00 9.81  ? 85  TYR D CE1 1 
ATOM   7135 C  CE2 . TYR D  1 85  ? -2.567  7.732   -24.539 1.00 10.48 ? 85  TYR D CE2 1 
ATOM   7136 C  CZ  . TYR D  1 85  ? -1.643  8.705   -24.924 1.00 10.34 ? 85  TYR D CZ  1 
ATOM   7137 O  OH  . TYR D  1 85  ? -0.701  9.105   -23.996 1.00 11.86 ? 85  TYR D OH  1 
ATOM   7138 N  N   . SER D  1 86  ? -6.772  8.770   -29.817 1.00 9.52  ? 86  SER D N   1 
ATOM   7139 C  CA  . SER D  1 86  ? -7.590  8.688   -31.045 1.00 10.51 ? 86  SER D CA  1 
ATOM   7140 C  C   . SER D  1 86  ? -6.651  8.642   -32.304 1.00 8.83  ? 86  SER D C   1 
ATOM   7141 O  O   . SER D  1 86  ? -5.563  9.254   -32.308 1.00 8.97  ? 86  SER D O   1 
ATOM   7142 C  CB  . SER D  1 86  ? -8.414  9.981   -31.181 1.00 11.93 ? 86  SER D CB  1 
ATOM   7143 O  OG  . SER D  1 86  ? -9.377  9.969   -30.065 1.00 13.85 ? 86  SER D OG  1 
ATOM   7144 N  N   . ALA D  1 87  ? -7.083  7.840   -33.254 1.00 9.99  ? 87  ALA D N   1 
ATOM   7145 C  CA  . ALA D  1 87  ? -6.230  7.707   -34.460 1.00 10.19 ? 87  ALA D CA  1 
ATOM   7146 C  C   . ALA D  1 87  ? -6.070  8.965   -35.232 1.00 10.35 ? 87  ALA D C   1 
ATOM   7147 O  O   . ALA D  1 87  ? -7.009  9.820   -35.283 1.00 11.64 ? 87  ALA D O   1 
ATOM   7148 C  CB  . ALA D  1 87  ? -6.772  6.645   -35.333 1.00 10.86 ? 87  ALA D CB  1 
ATOM   7149 N  N   . THR D  1 88  ? -4.936  9.101   -35.878 1.00 9.88  ? 88  THR D N   1 
ATOM   7150 C  CA  . THR D  1 88  ? -4.669  10.246  -36.792 1.00 10.08 ? 88  THR D CA  1 
ATOM   7151 C  C   . THR D  1 88  ? -4.228  9.734   -38.173 1.00 9.70  ? 88  THR D C   1 
ATOM   7152 O  O   . THR D  1 88  ? -4.684  10.216  -39.206 1.00 10.39 ? 88  THR D O   1 
ATOM   7153 C  CB  . THR D  1 88  ? -3.803  11.335  -36.177 1.00 11.81 ? 88  THR D CB  1 
ATOM   7154 O  OG1 . THR D  1 88  ? -3.762  12.413  -37.127 1.00 14.22 ? 88  THR D OG1 1 
ATOM   7155 C  CG2 . THR D  1 88  ? -2.394  10.884  -35.798 1.00 11.94 ? 88  THR D CG2 1 
ATOM   7156 N  N   . GLN D  1 89  ? -3.315  8.756   -38.253 1.00 9.16  ? 89  GLN D N   1 
ATOM   7157 C  CA  . GLN D  1 89  ? -2.817  8.313   -39.569 1.00 9.36  ? 89  GLN D CA  1 
ATOM   7158 C  C   . GLN D  1 89  ? -2.035  7.023   -39.341 1.00 7.89  ? 89  GLN D C   1 
ATOM   7159 O  O   . GLN D  1 89  ? -1.611  6.737   -38.202 1.00 7.93  ? 89  GLN D O   1 
ATOM   7160 C  CB  . GLN D  1 89  ? -1.906  9.364   -40.233 1.00 9.63  ? 89  GLN D CB  1 
ATOM   7161 C  CG  . GLN D  1 89  ? -0.701  9.815   -39.370 1.00 12.24 ? 89  GLN D CG  1 
ATOM   7162 C  CD  . GLN D  1 89  ? 0.590   9.270   -39.764 1.00 12.05 ? 89  GLN D CD  1 
ATOM   7163 O  OE1 . GLN D  1 89  ? 0.709   8.155   -40.084 1.00 11.49 ? 89  GLN D OE1 1 
ATOM   7164 N  NE2 . GLN D  1 89  ? 1.594   10.118  -39.806 1.00 18.84 ? 89  GLN D NE2 1 
ATOM   7165 N  N   . LEU D  1 90  ? -1.900  6.251   -40.405 1.00 7.13  ? 90  LEU D N   1 
ATOM   7166 C  CA  . LEU D  1 90  ? -0.912  5.157   -40.398 1.00 7.07  ? 90  LEU D CA  1 
ATOM   7167 C  C   . LEU D  1 90  ? 0.042   5.337   -41.589 1.00 6.84  ? 90  LEU D C   1 
ATOM   7168 O  O   . LEU D  1 90  ? -0.244  6.001   -42.574 1.00 8.32  ? 90  LEU D O   1 
ATOM   7169 C  CB  . LEU D  1 90  ? -1.598  3.768   -40.397 1.00 7.70  ? 90  LEU D CB  1 
ATOM   7170 C  CG  . LEU D  1 90  ? -2.547  3.410   -41.495 1.00 7.55  ? 90  LEU D CG  1 
ATOM   7171 C  CD1 . LEU D  1 90  ? -1.801  2.988   -42.765 1.00 9.69  ? 90  LEU D CD1 1 
ATOM   7172 C  CD2 . LEU D  1 90  ? -3.396  2.214   -41.069 1.00 9.26  ? 90  LEU D CD2 1 
ATOM   7173 N  N   . HIS D  1 91  ? 1.212   4.712   -41.440 1.00 7.07  ? 91  HIS D N   1 
ATOM   7174 C  CA  . HIS D  1 91  ? 2.232   4.843   -42.489 1.00 7.09  ? 91  HIS D CA  1 
ATOM   7175 C  C   . HIS D  1 91  ? 3.204   3.682   -42.274 1.00 7.32  ? 91  HIS D C   1 
ATOM   7176 O  O   . HIS D  1 91  ? 3.110   2.896   -41.332 1.00 6.73  ? 91  HIS D O   1 
ATOM   7177 C  CB  . HIS D  1 91  ? 2.969   6.217   -42.426 1.00 7.30  ? 91  HIS D CB  1 
ATOM   7178 C  CG  . HIS D  1 91  ? 3.726   6.379   -41.131 1.00 6.17  ? 91  HIS D CG  1 
ATOM   7179 N  ND1 . HIS D  1 91  ? 3.177   6.961   -40.044 1.00 7.60  ? 91  HIS D ND1 1 
ATOM   7180 C  CD2 . HIS D  1 91  ? 4.993   5.954   -40.739 1.00 6.69  ? 91  HIS D CD2 1 
ATOM   7181 C  CE1 . HIS D  1 91  ? 4.037   6.878   -39.025 1.00 7.03  ? 91  HIS D CE1 1 
ATOM   7182 N  NE2 . HIS D  1 91  ? 5.143   6.204   -39.417 1.00 7.01  ? 91  HIS D NE2 1 
ATOM   7183 N  N   . LEU D  1 92  ? 4.167   3.573   -43.195 1.00 7.63  ? 92  LEU D N   1 
ATOM   7184 C  CA  . LEU D  1 92  ? 5.103   2.431   -43.195 1.00 7.23  ? 92  LEU D CA  1 
ATOM   7185 C  C   . LEU D  1 92  ? 6.569   2.874   -43.373 1.00 7.36  ? 92  LEU D C   1 
ATOM   7186 O  O   . LEU D  1 92  ? 6.910   4.003   -43.717 1.00 8.12  ? 92  LEU D O   1 
ATOM   7187 C  CB  . LEU D  1 92  ? 4.746   1.495   -44.366 1.00 9.00  ? 92  LEU D CB  1 
ATOM   7188 C  CG  . LEU D  1 92  ? 3.344   0.855   -44.273 1.00 9.39  ? 92  LEU D CG  1 
ATOM   7189 C  CD1 . LEU D  1 92  ? 2.381   1.511   -45.159 1.00 13.93 ? 92  LEU D CD1 1 
ATOM   7190 C  CD2 . LEU D  1 92  ? 3.455   -0.637  -44.399 1.00 12.69 ? 92  LEU D CD2 1 
ATOM   7191 N  N   . HIS D  1 93  ? 7.416   1.942   -43.000 1.00 7.15  ? 93  HIS D N   1 
ATOM   7192 C  CA  . HIS D  1 93  ? 8.910   2.094   -43.191 1.00 7.86  ? 93  HIS D CA  1 
ATOM   7193 C  C   . HIS D  1 93  ? 9.419   0.841   -43.848 1.00 7.75  ? 93  HIS D C   1 
ATOM   7194 O  O   . HIS D  1 93  ? 8.917   -0.273  -43.504 1.00 7.24  ? 93  HIS D O   1 
ATOM   7195 C  CB  . HIS D  1 93  ? 9.581   2.249   -41.834 1.00 7.83  ? 93  HIS D CB  1 
ATOM   7196 C  CG  . HIS D  1 93  ? 9.133   3.429   -41.068 1.00 7.34  ? 93  HIS D CG  1 
ATOM   7197 N  ND1 . HIS D  1 93  ? 9.711   4.692   -41.163 1.00 7.80  ? 93  HIS D ND1 1 
ATOM   7198 C  CD2 . HIS D  1 93  ? 8.027   3.564   -40.196 1.00 6.82  ? 93  HIS D CD2 1 
ATOM   7199 C  CE1 . HIS D  1 93  ? 9.036   5.587   -40.357 1.00 7.91  ? 93  HIS D CE1 1 
ATOM   7200 N  NE2 . HIS D  1 93  ? 7.997   4.942   -39.736 1.00 6.47  ? 93  HIS D NE2 1 
ATOM   7201 N  N   . TRP D  1 94  ? 10.365  0.942   -44.788 1.00 6.75  ? 94  TRP D N   1 
ATOM   7202 C  CA  . TRP D  1 94  ? 10.873  -0.273  -45.544 1.00 7.00  ? 94  TRP D CA  1 
ATOM   7203 C  C   . TRP D  1 94  ? 12.294  -0.001  -45.975 1.00 7.22  ? 94  TRP D C   1 
ATOM   7204 O  O   . TRP D  1 94  ? 12.873  1.071   -45.787 1.00 7.75  ? 94  TRP D O   1 
ATOM   7205 C  CB  . TRP D  1 94  ? 9.866   -0.523  -46.678 1.00 7.55  ? 94  TRP D CB  1 
ATOM   7206 C  CG  . TRP D  1 94  ? 9.733   0.667   -47.659 1.00 7.46  ? 94  TRP D CG  1 
ATOM   7207 C  CD1 . TRP D  1 94  ? 10.575  0.944   -48.756 1.00 8.73  ? 94  TRP D CD1 1 
ATOM   7208 C  CD2 . TRP D  1 94  ? 8.742   1.740   -47.607 1.00 7.90  ? 94  TRP D CD2 1 
ATOM   7209 N  NE1 . TRP D  1 94  ? 10.164  2.137   -49.372 1.00 8.28  ? 94  TRP D NE1 1 
ATOM   7210 C  CE2 . TRP D  1 94  ? 8.994   2.610   -48.730 1.00 7.82  ? 94  TRP D CE2 1 
ATOM   7211 C  CE3 . TRP D  1 94  ? 7.679   2.075   -46.761 1.00 8.60  ? 94  TRP D CE3 1 
ATOM   7212 C  CZ2 . TRP D  1 94  ? 8.203   3.776   -48.971 1.00 7.82  ? 94  TRP D CZ2 1 
ATOM   7213 C  CZ3 . TRP D  1 94  ? 6.914   3.210   -47.031 1.00 7.94  ? 94  TRP D CZ3 1 
ATOM   7214 C  CH2 . TRP D  1 94  ? 7.156   4.040   -48.123 1.00 7.91  ? 94  TRP D CH2 1 
ATOM   7215 N  N   . GLY D  1 95  ? 12.794  -1.035  -46.631 1.00 7.34  ? 95  GLY D N   1 
ATOM   7216 C  CA  . GLY D  1 95  ? 14.206  -1.103  -47.131 1.00 8.58  ? 95  GLY D CA  1 
ATOM   7217 C  C   . GLY D  1 95  ? 14.280  -0.807  -48.644 1.00 8.23  ? 95  GLY D C   1 
ATOM   7218 O  O   . GLY D  1 95  ? 13.760  0.209   -49.142 1.00 9.16  ? 95  GLY D O   1 
ATOM   7219 N  N   . ASN D  1 96  ? 14.835  -1.790  -49.385 1.00 9.68  ? 96  ASN D N   1 
ATOM   7220 C  CA  . ASN D  1 96  ? 14.949  -1.568  -50.826 1.00 12.13 ? 96  ASN D CA  1 
ATOM   7221 C  C   . ASN D  1 96  ? 15.088  -2.943  -51.429 1.00 12.45 ? 96  ASN D C   1 
ATOM   7222 O  O   . ASN D  1 96  ? 15.214  -3.915  -50.694 1.00 11.56 ? 96  ASN D O   1 
ATOM   7223 C  CB  . ASN D  1 96  ? 16.179  -0.673  -51.119 1.00 13.11 ? 96  ASN D CB  1 
ATOM   7224 C  CG  . ASN D  1 96  ? 17.464  -1.354  -50.897 1.00 14.57 ? 96  ASN D CG  1 
ATOM   7225 O  OD1 . ASN D  1 96  ? 17.874  -2.068  -51.811 1.00 21.71 ? 96  ASN D OD1 1 
ATOM   7226 N  ND2 . ASN D  1 96  ? 18.120  -1.179  -49.789 1.00 14.94 ? 96  ASN D ND2 1 
ATOM   7227 N  N   . PRO D  1 97  ? 14.973  -3.000  -52.799 1.00 14.07 ? 97  PRO D N   1 
ATOM   7228 C  CA  . PRO D  1 97  ? 14.906  -4.332  -53.431 1.00 17.46 ? 97  PRO D CA  1 
ATOM   7229 C  C   . PRO D  1 97  ? 16.114  -5.180  -53.152 1.00 17.16 ? 97  PRO D C   1 
ATOM   7230 O  O   . PRO D  1 97  ? 15.926  -6.387  -53.023 1.00 23.48 ? 97  PRO D O   1 
ATOM   7231 C  CB  . PRO D  1 97  ? 14.626  -4.012  -54.911 1.00 18.00 ? 97  PRO D CB  1 
ATOM   7232 C  CG  . PRO D  1 97  ? 14.092  -2.582  -54.912 1.00 17.44 ? 97  PRO D CG  1 
ATOM   7233 C  CD  . PRO D  1 97  ? 14.737  -1.889  -53.713 1.00 14.89 ? 97  PRO D CD  1 
ATOM   7234 N  N   . ASN D  1 98  ? 17.272  -4.586  -52.919 1.00 18.36 ? 98  ASN D N   1 
ATOM   7235 C  CA  . ASN D  1 98  ? 18.485  -5.330  -52.646 1.00 22.04 ? 98  ASN D CA  1 
ATOM   7236 C  C   . ASN D  1 98  ? 18.702  -5.596  -51.161 1.00 24.69 ? 98  ASN D C   1 
ATOM   7237 O  O   . ASN D  1 98  ? 19.667  -6.263  -50.773 1.00 23.10 ? 98  ASN D O   1 
ATOM   7238 C  CB  . ASN D  1 98  ? 19.707  -4.558  -53.215 1.00 26.98 ? 98  ASN D CB  1 
ATOM   7239 C  CG  . ASN D  1 98  ? 19.550  -4.164  -54.712 1.00 35.94 ? 98  ASN D CG  1 
ATOM   7240 O  OD1 . ASN D  1 98  ? 19.005  -4.910  -55.547 1.00 38.42 ? 98  ASN D OD1 1 
ATOM   7241 N  ND2 . ASN D  1 98  ? 20.041  -2.977  -55.044 1.00 42.82 ? 98  ASN D ND2 1 
ATOM   7242 N  N   . ASP D  1 99  ? 17.908  -4.979  -50.284 1.00 17.05 ? 99  ASP D N   1 
ATOM   7243 C  CA  . ASP D  1 99  ? 18.028  -5.273  -48.891 1.00 16.11 ? 99  ASP D CA  1 
ATOM   7244 C  C   . ASP D  1 99  ? 16.605  -5.067  -48.261 1.00 13.73 ? 99  ASP D C   1 
ATOM   7245 O  O   . ASP D  1 99  ? 16.322  -3.942  -47.722 1.00 12.64 ? 99  ASP D O   1 
ATOM   7246 C  CB  . ASP D  1 99  ? 18.995  -4.278  -48.229 1.00 16.50 ? 99  ASP D CB  1 
ATOM   7247 C  CG  . ASP D  1 99  ? 19.191  -4.557  -46.744 1.00 20.66 ? 99  ASP D CG  1 
ATOM   7248 O  OD1 . ASP D  1 99  ? 18.776  -5.640  -46.296 1.00 20.62 ? 99  ASP D OD1 1 
ATOM   7249 O  OD2 . ASP D  1 99  ? 19.653  -3.662  -45.973 1.00 28.13 ? 99  ASP D OD2 1 
ATOM   7250 N  N   . PRO D  1 100 ? 15.729  -6.062  -48.350 1.00 12.72 ? 100 PRO D N   1 
ATOM   7251 C  CA  . PRO D  1 100 ? 14.303  -5.906  -47.940 1.00 11.55 ? 100 PRO D CA  1 
ATOM   7252 C  C   . PRO D  1 100 ? 14.285  -6.149  -46.419 1.00 9.87  ? 100 PRO D C   1 
ATOM   7253 O  O   . PRO D  1 100 ? 13.681  -7.098  -45.894 1.00 11.75 ? 100 PRO D O   1 
ATOM   7254 C  CB  . PRO D  1 100 ? 13.583  -6.992  -48.763 1.00 13.53 ? 100 PRO D CB  1 
ATOM   7255 C  CG  . PRO D  1 100 ? 14.648  -8.064  -48.907 1.00 13.54 ? 100 PRO D CG  1 
ATOM   7256 C  CD  . PRO D  1 100 ? 15.965  -7.385  -49.035 1.00 15.03 ? 100 PRO D CD  1 
ATOM   7257 N  N   . HIS D  1 101 ? 14.993  -5.306  -45.640 1.00 11.19 ? 101 HIS D N   1 
ATOM   7258 C  CA  . HIS D  1 101 ? 15.137  -5.445  -44.170 1.00 10.69 ? 101 HIS D CA  1 
ATOM   7259 C  C   . HIS D  1 101 ? 15.068  -4.095  -43.515 1.00 10.95 ? 101 HIS D C   1 
ATOM   7260 O  O   . HIS D  1 101 ? 16.010  -3.640  -42.880 1.00 14.08 ? 101 HIS D O   1 
ATOM   7261 C  CB  . HIS D  1 101 ? 16.457  -6.169  -43.818 1.00 13.38 ? 101 HIS D CB  1 
ATOM   7262 C  CG  . HIS D  1 101 ? 16.531  -7.540  -44.436 1.00 15.26 ? 101 HIS D CG  1 
ATOM   7263 N  ND1 . HIS D  1 101 ? 15.952  -8.660  -43.877 1.00 21.15 ? 101 HIS D ND1 1 
ATOM   7264 C  CD2 . HIS D  1 101 ? 17.096  -7.944  -45.650 1.00 14.96 ? 101 HIS D CD2 1 
ATOM   7265 C  CE1 . HIS D  1 101 ? 16.165  -9.719  -44.713 1.00 21.58 ? 101 HIS D CE1 1 
ATOM   7266 N  NE2 . HIS D  1 101 ? 16.840  -9.273  -45.801 1.00 22.88 ? 101 HIS D NE2 1 
ATOM   7267 N  N   . GLY D  1 102 ? 13.941  -3.434  -43.679 1.00 8.73  ? 102 GLY D N   1 
ATOM   7268 C  CA  . GLY D  1 102 ? 13.775  -2.042  -43.323 1.00 9.55  ? 102 GLY D CA  1 
ATOM   7269 C  C   . GLY D  1 102 ? 12.838  -1.770  -42.174 1.00 8.71  ? 102 GLY D C   1 
ATOM   7270 O  O   . GLY D  1 102 ? 12.295  -0.658  -42.091 1.00 9.37  ? 102 GLY D O   1 
ATOM   7271 N  N   . SER D  1 103 ? 12.548  -2.756  -41.316 1.00 8.33  ? 103 SER D N   1 
ATOM   7272 C  CA  . SER D  1 103 ? 11.826  -2.353  -40.109 1.00 7.88  ? 103 SER D CA  1 
ATOM   7273 C  C   . SER D  1 103 ? 12.639  -1.410  -39.248 1.00 8.16  ? 103 SER D C   1 
ATOM   7274 O  O   . SER D  1 103 ? 13.881  -1.340  -39.376 1.00 9.37  ? 103 SER D O   1 
ATOM   7275 C  CB  . SER D  1 103 ? 11.467  -3.573  -39.236 1.00 7.58  ? 103 SER D CB  1 
ATOM   7276 O  OG  . SER D  1 103 ? 12.675  -4.173  -38.642 1.00 8.31  ? 103 SER D OG  1 
ATOM   7277 N  N   . GLU D  1 104 ? 11.956  -0.614  -38.421 1.00 7.71  ? 104 GLU D N   1 
ATOM   7278 C  CA  . GLU D  1 104 ? 12.628  0.281   -37.520 1.00 8.08  ? 104 GLU D CA  1 
ATOM   7279 C  C   . GLU D  1 104 ? 13.083  -0.431  -36.271 1.00 6.94  ? 104 GLU D C   1 
ATOM   7280 O  O   . GLU D  1 104 ? 14.237  -0.417  -35.921 1.00 8.07  ? 104 GLU D O   1 
ATOM   7281 C  CB  . GLU D  1 104 ? 11.727  1.486   -37.212 1.00 7.65  ? 104 GLU D CB  1 
ATOM   7282 C  CG  . GLU D  1 104 ? 11.320  2.212   -38.514 1.00 7.58  ? 104 GLU D CG  1 
ATOM   7283 C  CD  . GLU D  1 104 ? 11.256  3.692   -38.240 1.00 8.47  ? 104 GLU D CD  1 
ATOM   7284 O  OE1 . GLU D  1 104 ? 10.270  4.147   -37.655 1.00 9.43  ? 104 GLU D OE1 1 
ATOM   7285 O  OE2 . GLU D  1 104 ? 12.211  4.438   -38.634 1.00 8.66  ? 104 GLU D OE2 1 
ATOM   7286 N  N   . HIS D  1 105 ? 12.117  -0.959  -35.515 1.00 7.33  ? 105 HIS D N   1 
ATOM   7287 C  CA  . HIS D  1 105 ? 12.464  -1.838  -34.397 1.00 8.09  ? 105 HIS D CA  1 
ATOM   7288 C  C   . HIS D  1 105 ? 13.069  -3.091  -34.934 1.00 7.54  ? 105 HIS D C   1 
ATOM   7289 O  O   . HIS D  1 105 ? 12.714  -3.624  -35.975 1.00 8.02  ? 105 HIS D O   1 
ATOM   7290 C  CB  . HIS D  1 105 ? 11.192  -2.147  -33.569 1.00 7.52  ? 105 HIS D CB  1 
ATOM   7291 C  CG  . HIS D  1 105 ? 10.690  -0.924  -32.865 1.00 7.67  ? 105 HIS D CG  1 
ATOM   7292 N  ND1 . HIS D  1 105 ? 9.797   -0.090  -33.467 1.00 8.50  ? 105 HIS D ND1 1 
ATOM   7293 C  CD2 . HIS D  1 105 ? 11.042  -0.351  -31.657 1.00 8.22  ? 105 HIS D CD2 1 
ATOM   7294 C  CE1 . HIS D  1 105 ? 9.565   0.989   -32.600 1.00 8.68  ? 105 HIS D CE1 1 
ATOM   7295 N  NE2 . HIS D  1 105 ? 10.327  0.801   -31.501 1.00 9.13  ? 105 HIS D NE2 1 
ATOM   7296 N  N   . THR D  1 106 ? 13.997  -3.624  -34.139 1.00 8.52  ? 106 THR D N   1 
ATOM   7297 C  CA  . THR D  1 106 ? 14.656  -4.966  -34.419 1.00 8.66  ? 106 THR D CA  1 
ATOM   7298 C  C   . THR D  1 106 ? 14.395  -5.903  -33.244 1.00 9.26  ? 106 THR D C   1 
ATOM   7299 O  O   . THR D  1 106 ? 14.065  -5.427  -32.169 1.00 9.09  ? 106 THR D O   1 
ATOM   7300 C  CB  . THR D  1 106 ? 16.139  -4.755  -34.732 1.00 8.76  ? 106 THR D CB  1 
ATOM   7301 O  OG1 . THR D  1 106 ? 16.827  -4.129  -33.598 1.00 10.65 ? 106 THR D OG1 1 
ATOM   7302 C  CG2 . THR D  1 106 ? 16.386  -3.842  -35.963 1.00 9.34  ? 106 THR D CG2 1 
ATOM   7303 N  N   . VAL D  1 107 ? 14.477  -7.217  -33.520 1.00 10.62 ? 107 VAL D N   1 
ATOM   7304 C  CA  . VAL D  1 107 ? 14.261  -8.179  -32.419 1.00 12.36 ? 107 VAL D CA  1 
ATOM   7305 C  C   . VAL D  1 107 ? 15.500  -8.999  -32.370 1.00 12.40 ? 107 VAL D C   1 
ATOM   7306 O  O   . VAL D  1 107 ? 15.870  -9.601  -33.381 1.00 12.81 ? 107 VAL D O   1 
ATOM   7307 C  CB  . VAL D  1 107 ? 12.982  -8.994  -32.640 1.00 11.12 ? 107 VAL D CB  1 
ATOM   7308 C  CG1 . VAL D  1 107 ? 12.872  -10.021 -31.536 1.00 14.40 ? 107 VAL D CG1 1 
ATOM   7309 C  CG2 . VAL D  1 107 ? 11.754  -8.064  -32.616 1.00 12.83 ? 107 VAL D CG2 1 
ATOM   7310 N  N   . SER D  1 108 ? 16.149  -8.973  -31.215 1.00 13.18 ? 108 SER D N   1 
ATOM   7311 C  CA  . SER D  1 108 ? 17.427  -9.743  -31.016 1.00 13.35 ? 108 SER D CA  1 
ATOM   7312 C  C   . SER D  1 108 ? 18.352  -9.485  -32.174 1.00 13.45 ? 108 SER D C   1 
ATOM   7313 O  O   . SER D  1 108 ? 19.006  -10.374 -32.785 1.00 14.30 ? 108 SER D O   1 
ATOM   7314 C  CB  . SER D  1 108 ? 17.149  -11.252 -30.907 1.00 14.57 ? 108 SER D CB  1 
ATOM   7315 O  OG  . SER D  1 108 ? 16.347  -11.485 -29.795 1.00 19.28 ? 108 SER D OG  1 
ATOM   7316 N  N   . GLY D  1 109 ? 18.466  -8.195  -32.488 1.00 12.11 ? 109 GLY D N   1 
ATOM   7317 C  CA  . GLY D  1 109 ? 19.349  -7.665  -33.544 1.00 14.24 ? 109 GLY D CA  1 
ATOM   7318 C  C   . GLY D  1 109 ? 18.971  -7.846  -35.016 1.00 15.29 ? 109 GLY D C   1 
ATOM   7319 O  O   . GLY D  1 109 ? 19.758  -7.456  -35.907 1.00 19.07 ? 109 GLY D O   1 
ATOM   7320 N  N   A GLN D  1 110 ? 17.818  -8.414  -35.321 0.50 13.53 ? 110 GLN D N   1 
ATOM   7321 N  N   B GLN D  1 110 ? 17.770  -8.306  -35.245 0.50 14.92 ? 110 GLN D N   1 
ATOM   7322 C  CA  A GLN D  1 110 ? 17.425  -8.690  -36.711 0.50 13.86 ? 110 GLN D CA  1 
ATOM   7323 C  CA  B GLN D  1 110 ? 17.299  -8.646  -36.562 0.50 16.08 ? 110 GLN D CA  1 
ATOM   7324 C  C   A GLN D  1 110 ? 16.292  -7.741  -37.091 0.50 11.41 ? 110 GLN D C   1 
ATOM   7325 C  C   B GLN D  1 110 ? 16.229  -7.687  -37.061 0.50 12.24 ? 110 GLN D C   1 
ATOM   7326 O  O   A GLN D  1 110 ? 15.323  -7.543  -36.329 0.50 11.00 ? 110 GLN D O   1 
ATOM   7327 O  O   B GLN D  1 110 ? 15.204  -7.463  -36.372 0.50 10.86 ? 110 GLN D O   1 
ATOM   7328 C  CB  A GLN D  1 110 ? 16.876  -10.135 -36.887 0.50 12.88 ? 110 GLN D CB  1 
ATOM   7329 C  CB  B GLN D  1 110 ? 16.649  -10.020 -36.490 0.50 17.07 ? 110 GLN D CB  1 
ATOM   7330 C  CG  A GLN D  1 110 ? 17.685  -11.225 -36.162 0.50 13.53 ? 110 GLN D CG  1 
ATOM   7331 C  CG  B GLN D  1 110 ? 17.480  -11.014 -35.661 0.50 23.64 ? 110 GLN D CG  1 
ATOM   7332 C  CD  A GLN D  1 110 ? 19.113  -11.189 -36.548 0.50 14.30 ? 110 GLN D CD  1 
ATOM   7333 C  CD  B GLN D  1 110 ? 17.331  -12.413 -36.175 0.50 26.53 ? 110 GLN D CD  1 
ATOM   7334 O  OE1 A GLN D  1 110 ? 20.013  -10.900 -35.714 0.50 15.81 ? 110 GLN D OE1 1 
ATOM   7335 O  OE1 B GLN D  1 110 ? 16.511  -13.202 -35.671 0.50 33.75 ? 110 GLN D OE1 1 
ATOM   7336 N  NE2 A GLN D  1 110 ? 19.345  -11.455 -37.789 0.50 14.16 ? 110 GLN D NE2 1 
ATOM   7337 N  NE2 B GLN D  1 110 ? 18.084  -12.725 -37.202 0.50 26.38 ? 110 GLN D NE2 1 
ATOM   7338 N  N   . HIS D  1 111 ? 16.424  -7.176  -38.280 1.00 10.73 ? 111 HIS D N   1 
ATOM   7339 C  CA  . HIS D  1 111 ? 15.331  -6.441  -38.911 1.00 10.20 ? 111 HIS D CA  1 
ATOM   7340 C  C   . HIS D  1 111 ? 14.329  -7.340  -39.475 1.00 12.43 ? 111 HIS D C   1 
ATOM   7341 O  O   . HIS D  1 111 ? 14.672  -8.427  -40.000 1.00 16.26 ? 111 HIS D O   1 
ATOM   7342 C  CB  . HIS D  1 111 ? 15.872  -5.635  -40.099 1.00 12.56 ? 111 HIS D CB  1 
ATOM   7343 C  CG  . HIS D  1 111 ? 16.593  -4.417  -39.694 1.00 10.41 ? 111 HIS D CG  1 
ATOM   7344 N  ND1 . HIS D  1 111 ? 15.979  -3.173  -39.491 1.00 11.63 ? 111 HIS D ND1 1 
ATOM   7345 C  CD2 . HIS D  1 111 ? 17.958  -4.213  -39.463 1.00 13.03 ? 111 HIS D CD2 1 
ATOM   7346 C  CE1 . HIS D  1 111 ? 16.921  -2.256  -39.137 1.00 12.97 ? 111 HIS D CE1 1 
ATOM   7347 N  NE2 . HIS D  1 111 ? 18.140  -2.886  -39.102 1.00 15.17 ? 111 HIS D NE2 1 
ATOM   7348 N  N   . PHE D  1 112 ? 13.075  -6.920  -39.471 1.00 9.01  ? 112 PHE D N   1 
ATOM   7349 C  CA  . PHE D  1 112 ? 12.018  -7.520  -40.270 1.00 9.58  ? 112 PHE D CA  1 
ATOM   7350 C  C   . PHE D  1 112 ? 12.022  -6.730  -41.611 1.00 8.80  ? 112 PHE D C   1 
ATOM   7351 O  O   . PHE D  1 112 ? 12.789  -5.723  -41.765 1.00 8.75  ? 112 PHE D O   1 
ATOM   7352 C  CB  . PHE D  1 112 ? 10.688  -7.392  -39.495 1.00 10.61 ? 112 PHE D CB  1 
ATOM   7353 C  CG  . PHE D  1 112 ? 10.532  -8.490  -38.478 1.00 9.99  ? 112 PHE D CG  1 
ATOM   7354 C  CD1 . PHE D  1 112 ? 9.889   -9.645  -38.834 1.00 14.18 ? 112 PHE D CD1 1 
ATOM   7355 C  CD2 . PHE D  1 112 ? 11.103  -8.401  -37.210 1.00 13.36 ? 112 PHE D CD2 1 
ATOM   7356 C  CE1 . PHE D  1 112 ? 9.754   -10.684 -37.950 1.00 17.13 ? 112 PHE D CE1 1 
ATOM   7357 C  CE2 . PHE D  1 112 ? 10.980  -9.451  -36.309 1.00 15.29 ? 112 PHE D CE2 1 
ATOM   7358 C  CZ  . PHE D  1 112 ? 10.293  -10.593 -36.685 1.00 14.89 ? 112 PHE D CZ  1 
ATOM   7359 N  N   . ALA D  1 113 ? 11.184  -7.169  -42.572 1.00 7.72  ? 113 ALA D N   1 
ATOM   7360 C  CA  . ALA D  1 113 ? 11.205  -6.565  -43.892 1.00 9.45  ? 113 ALA D CA  1 
ATOM   7361 C  C   . ALA D  1 113 ? 10.725  -5.117  -43.841 1.00 8.18  ? 113 ALA D C   1 
ATOM   7362 O  O   . ALA D  1 113 ? 11.226  -4.275  -44.618 1.00 8.62  ? 113 ALA D O   1 
ATOM   7363 C  CB  . ALA D  1 113 ? 10.332  -7.331  -44.884 1.00 9.19  ? 113 ALA D CB  1 
ATOM   7364 N  N   . ALA D  1 114 ? 9.670   -4.839  -43.063 1.00 7.34  ? 114 ALA D N   1 
ATOM   7365 C  CA  . ALA D  1 114 ? 9.087   -3.492  -43.069 1.00 7.39  ? 114 ALA D CA  1 
ATOM   7366 C  C   . ALA D  1 114 ? 8.319   -3.366  -41.717 1.00 7.37  ? 114 ALA D C   1 
ATOM   7367 O  O   . ALA D  1 114 ? 8.341   -4.267  -40.837 1.00 7.20  ? 114 ALA D O   1 
ATOM   7368 C  CB  . ALA D  1 114 ? 8.168   -3.285  -44.257 1.00 7.82  ? 114 ALA D CB  1 
ATOM   7369 N  N   . GLU D  1 115 ? 7.696   -2.196  -41.537 1.00 6.56  ? 115 GLU D N   1 
ATOM   7370 C  CA  . GLU D  1 115 ? 6.996   -1.921  -40.226 1.00 6.98  ? 115 GLU D CA  1 
ATOM   7371 C  C   . GLU D  1 115 ? 5.864   -0.951  -40.523 1.00 6.43  ? 115 GLU D C   1 
ATOM   7372 O  O   . GLU D  1 115 ? 6.022   0.024   -41.268 1.00 7.29  ? 115 GLU D O   1 
ATOM   7373 C  CB  . GLU D  1 115 ? 7.978   -1.324  -39.206 1.00 6.94  ? 115 GLU D CB  1 
ATOM   7374 C  CG  . GLU D  1 115 ? 7.436   -1.195  -37.832 1.00 8.10  ? 115 GLU D CG  1 
ATOM   7375 C  CD  . GLU D  1 115 ? 8.523   -0.964  -36.800 1.00 7.28  ? 115 GLU D CD  1 
ATOM   7376 O  OE1 . GLU D  1 115 ? 9.662   -1.428  -37.019 1.00 8.08  ? 115 GLU D OE1 1 
ATOM   7377 O  OE2 . GLU D  1 115 ? 8.241   -0.315  -35.771 1.00 8.30  ? 115 GLU D OE2 1 
ATOM   7378 N  N   . LEU D  1 116 ? 4.708   -1.226  -39.928 1.00 6.39  ? 116 LEU D N   1 
ATOM   7379 C  CA  . LEU D  1 116 ? 3.530   -0.332  -39.944 1.00 7.06  ? 116 LEU D CA  1 
ATOM   7380 C  C   . LEU D  1 116 ? 3.430   0.340   -38.619 1.00 7.28  ? 116 LEU D C   1 
ATOM   7381 O  O   . LEU D  1 116 ? 3.575   -0.273  -37.535 1.00 7.24  ? 116 LEU D O   1 
ATOM   7382 C  CB  . LEU D  1 116 ? 2.254   -1.229  -40.134 1.00 7.51  ? 116 LEU D CB  1 
ATOM   7383 C  CG  . LEU D  1 116 ? 0.925   -0.477  -40.015 1.00 7.88  ? 116 LEU D CG  1 
ATOM   7384 C  CD1 . LEU D  1 116 ? 0.724   0.370   -41.246 1.00 9.18  ? 116 LEU D CD1 1 
ATOM   7385 C  CD2 . LEU D  1 116 ? -0.202  -1.481  -39.824 1.00 8.43  ? 116 LEU D CD2 1 
ATOM   7386 N  N   . HIS D  1 117 ? 3.197   1.660   -38.713 1.00 7.25  ? 117 HIS D N   1 
ATOM   7387 C  CA  . HIS D  1 117 ? 2.886   2.489   -37.509 1.00 6.39  ? 117 HIS D CA  1 
ATOM   7388 C  C   . HIS D  1 117 ? 1.489   3.060   -37.644 1.00 7.39  ? 117 HIS D C   1 
ATOM   7389 O  O   . HIS D  1 117 ? 1.145   3.705   -38.617 1.00 8.16  ? 117 HIS D O   1 
ATOM   7390 C  CB  . HIS D  1 117 ? 3.878   3.676   -37.492 1.00 7.22  ? 117 HIS D CB  1 
ATOM   7391 C  CG  . HIS D  1 117 ? 5.240   3.184   -37.107 1.00 6.40  ? 117 HIS D CG  1 
ATOM   7392 N  ND1 . HIS D  1 117 ? 6.419   3.883   -37.388 1.00 6.33  ? 117 HIS D ND1 1 
ATOM   7393 C  CD2 . HIS D  1 117 ? 5.660   1.997   -36.498 1.00 7.09  ? 117 HIS D CD2 1 
ATOM   7394 C  CE1 . HIS D  1 117 ? 7.469   3.185   -36.947 1.00 7.02  ? 117 HIS D CE1 1 
ATOM   7395 N  NE2 . HIS D  1 117 ? 7.033   1.998   -36.398 1.00 6.27  ? 117 HIS D NE2 1 
ATOM   7396 N  N   . ILE D  1 118 ? 0.700   2.776   -36.617 1.00 6.93  ? 118 ILE D N   1 
ATOM   7397 C  CA  . ILE D  1 118 ? -0.651  3.422   -36.534 1.00 7.49  ? 118 ILE D CA  1 
ATOM   7398 C  C   . ILE D  1 118 ? -0.586  4.440   -35.438 1.00 7.71  ? 118 ILE D C   1 
ATOM   7399 O  O   . ILE D  1 118 ? -0.397  4.088   -34.211 1.00 7.14  ? 118 ILE D O   1 
ATOM   7400 C  CB  . ILE D  1 118 ? -1.754  2.368   -36.232 1.00 7.82  ? 118 ILE D CB  1 
ATOM   7401 C  CG1 . ILE D  1 118 ? -1.631  1.148   -37.175 1.00 7.77  ? 118 ILE D CG1 1 
ATOM   7402 C  CG2 . ILE D  1 118 ? -3.106  3.091   -36.330 1.00 9.23  ? 118 ILE D CG2 1 
ATOM   7403 C  CD1 . ILE D  1 118 ? -2.697  0.082   -36.917 1.00 10.17 ? 118 ILE D CD1 1 
ATOM   7404 N  N   . VAL D  1 119 ? -0.609  5.727   -35.833 1.00 7.29  ? 119 VAL D N   1 
ATOM   7405 C  CA  . VAL D  1 119 ? -0.343  6.853   -34.920 1.00 7.91  ? 119 VAL D CA  1 
ATOM   7406 C  C   . VAL D  1 119 ? -1.689  7.335   -34.353 1.00 7.69  ? 119 VAL D C   1 
ATOM   7407 O  O   . VAL D  1 119 ? -2.668  7.552   -35.064 1.00 8.43  ? 119 VAL D O   1 
ATOM   7408 C  CB  . VAL D  1 119 ? 0.350   8.005   -35.713 1.00 7.42  ? 119 VAL D CB  1 
ATOM   7409 C  CG1 . VAL D  1 119 ? 0.731   9.092   -34.754 1.00 8.64  ? 119 VAL D CG1 1 
ATOM   7410 C  CG2 . VAL D  1 119 ? 1.569   7.459   -36.469 1.00 8.42  ? 119 VAL D CG2 1 
ATOM   7411 N  N   . HIS D  1 120 ? -1.643  7.519   -33.021 1.00 8.28  ? 120 HIS D N   1 
ATOM   7412 C  CA  . HIS D  1 120 ? -2.782  8.082   -32.252 1.00 9.00  ? 120 HIS D CA  1 
ATOM   7413 C  C   . HIS D  1 120 ? -2.280  9.171   -31.361 1.00 8.06  ? 120 HIS D C   1 
ATOM   7414 O  O   . HIS D  1 120 ? -1.084  9.275   -30.963 1.00 9.64  ? 120 HIS D O   1 
ATOM   7415 C  CB  . HIS D  1 120 ? -3.339  6.957   -31.303 1.00 8.86  ? 120 HIS D CB  1 
ATOM   7416 C  CG  . HIS D  1 120 ? -3.802  5.689   -31.990 1.00 8.55  ? 120 HIS D CG  1 
ATOM   7417 N  ND1 . HIS D  1 120 ? -2.896  4.767   -32.529 1.00 9.18  ? 120 HIS D ND1 1 
ATOM   7418 C  CD2 . HIS D  1 120 ? -5.053  5.132   -32.122 1.00 9.38  ? 120 HIS D CD2 1 
ATOM   7419 C  CE1 . HIS D  1 120 ? -3.628  3.720   -33.010 1.00 9.66  ? 120 HIS D CE1 1 
ATOM   7420 N  NE2 . HIS D  1 120 ? -4.950  3.936   -32.806 1.00 9.96  ? 120 HIS D NE2 1 
ATOM   7421 N  N   . TYR D  1 121 ? -3.238  10.088  -31.045 1.00 8.73  ? 121 TYR D N   1 
ATOM   7422 C  CA  . TYR D  1 121 ? -2.881  11.226  -30.188 1.00 9.83  ? 121 TYR D CA  1 
ATOM   7423 C  C   . TYR D  1 121 ? -3.807  11.243  -28.950 1.00 9.40  ? 121 TYR D C   1 
ATOM   7424 O  O   . TYR D  1 121 ? -4.945  10.719  -28.973 1.00 9.60  ? 121 TYR D O   1 
ATOM   7425 C  CB  . TYR D  1 121 ? -2.995  12.574  -30.937 1.00 10.05 ? 121 TYR D CB  1 
ATOM   7426 C  CG  . TYR D  1 121 ? -4.370  13.031  -31.271 1.00 10.40 ? 121 TYR D CG  1 
ATOM   7427 C  CD1 . TYR D  1 121 ? -5.028  13.993  -30.493 1.00 12.33 ? 121 TYR D CD1 1 
ATOM   7428 C  CD2 . TYR D  1 121 ? -5.039  12.553  -32.377 1.00 12.09 ? 121 TYR D CD2 1 
ATOM   7429 C  CE1 . TYR D  1 121 ? -6.335  14.320  -30.800 1.00 13.26 ? 121 TYR D CE1 1 
ATOM   7430 C  CE2 . TYR D  1 121 ? -6.344  12.914  -32.693 1.00 13.02 ? 121 TYR D CE2 1 
ATOM   7431 C  CZ  . TYR D  1 121 ? -6.950  13.832  -31.864 1.00 14.83 ? 121 TYR D CZ  1 
ATOM   7432 O  OH  . TYR D  1 121 ? -8.250  14.146  -32.283 1.00 21.69 ? 121 TYR D OH  1 
ATOM   7433 N  N   . ASN D  1 122 ? -3.307  11.886  -27.900 1.00 9.36  ? 122 ASN D N   1 
ATOM   7434 C  CA  . ASN D  1 122 ? -4.046  12.021  -26.600 1.00 9.37  ? 122 ASN D CA  1 
ATOM   7435 C  C   . ASN D  1 122 ? -5.168  13.014  -26.747 1.00 10.58 ? 122 ASN D C   1 
ATOM   7436 O  O   . ASN D  1 122 ? -4.913  14.216  -26.528 1.00 11.46 ? 122 ASN D O   1 
ATOM   7437 C  CB  . ASN D  1 122 ? -3.033  12.302  -25.485 1.00 9.70  ? 122 ASN D CB  1 
ATOM   7438 C  CG  . ASN D  1 122 ? -3.648  12.159  -24.123 1.00 10.09 ? 122 ASN D CG  1 
ATOM   7439 O  OD1 . ASN D  1 122 ? -4.892  12.323  -23.970 1.00 10.77 ? 122 ASN D OD1 1 
ATOM   7440 N  ND2 . ASN D  1 122 ? -2.805  11.807  -23.149 1.00 11.72 ? 122 ASN D ND2 1 
ATOM   7441 N  N   . SER D  1 123 ? -6.345  12.484  -27.032 1.00 9.69  ? 123 SER D N   1 
ATOM   7442 C  CA  . SER D  1 123 ? -7.522  13.355  -27.274 1.00 11.64 ? 123 SER D CA  1 
ATOM   7443 C  C   . SER D  1 123 ? -8.147  13.792  -25.951 1.00 12.56 ? 123 SER D C   1 
ATOM   7444 O  O   . SER D  1 123 ? -9.006  14.683  -25.974 1.00 13.20 ? 123 SER D O   1 
ATOM   7445 C  CB  . SER D  1 123 ? -8.550  12.793  -28.217 1.00 11.05 ? 123 SER D CB  1 
ATOM   7446 O  OG  . SER D  1 123 ? -8.762  11.409  -27.904 1.00 12.78 ? 123 SER D OG  1 
ATOM   7447 N  N   . ASP D  1 124 ? -7.761  13.221  -24.837 1.00 11.75 ? 124 ASP D N   1 
ATOM   7448 C  CA  . ASP D  1 124 ? -8.275  13.714  -23.509 1.00 12.13 ? 124 ASP D CA  1 
ATOM   7449 C  C   . ASP D  1 124 ? -7.533  15.027  -23.201 1.00 14.75 ? 124 ASP D C   1 
ATOM   7450 O  O   . ASP D  1 124 ? -8.074  15.875  -22.452 1.00 16.93 ? 124 ASP D O   1 
ATOM   7451 C  CB  . ASP D  1 124 ? -7.950  12.702  -22.419 1.00 13.34 ? 124 ASP D CB  1 
ATOM   7452 C  CG  . ASP D  1 124 ? -8.844  11.477  -22.462 1.00 12.97 ? 124 ASP D CG  1 
ATOM   7453 O  OD1 . ASP D  1 124 ? -9.855  11.479  -23.200 1.00 14.12 ? 124 ASP D OD1 1 
ATOM   7454 O  OD2 . ASP D  1 124 ? -8.508  10.516  -21.743 1.00 14.22 ? 124 ASP D OD2 1 
ATOM   7455 N  N   . LEU D  1 125 ? -6.317  15.191  -23.665 1.00 11.80 ? 125 LEU D N   1 
ATOM   7456 C  CA  . LEU D  1 125 ? -5.494  16.350  -23.339 1.00 14.45 ? 125 LEU D CA  1 
ATOM   7457 C  C   . LEU D  1 125 ? -5.447  17.373  -24.476 1.00 14.39 ? 125 LEU D C   1 
ATOM   7458 O  O   . LEU D  1 125 ? -5.286  18.619  -24.167 1.00 15.60 ? 125 LEU D O   1 
ATOM   7459 C  CB  . LEU D  1 125 ? -4.072  16.005  -22.960 1.00 13.65 ? 125 LEU D CB  1 
ATOM   7460 C  CG  . LEU D  1 125 ? -3.800  15.532  -21.526 1.00 15.33 ? 125 LEU D CG  1 
ATOM   7461 C  CD1 . LEU D  1 125 ? -4.703  14.405  -21.098 1.00 17.42 ? 125 LEU D CD1 1 
ATOM   7462 C  CD2 . LEU D  1 125 ? -2.361  15.078  -21.432 1.00 16.21 ? 125 LEU D CD2 1 
ATOM   7463 N  N   . TYR D  1 126 ? -5.488  16.962  -25.763 1.00 12.34 ? 126 TYR D N   1 
ATOM   7464 C  CA  . TYR D  1 126 ? -5.082  17.841  -26.857 1.00 13.09 ? 126 TYR D CA  1 
ATOM   7465 C  C   . TYR D  1 126 ? -6.143  17.786  -27.944 1.00 15.06 ? 126 TYR D C   1 
ATOM   7466 O  O   . TYR D  1 126 ? -6.808  16.768  -28.129 1.00 15.14 ? 126 TYR D O   1 
ATOM   7467 C  CB  . TYR D  1 126 ? -3.734  17.334  -27.434 1.00 12.01 ? 126 TYR D CB  1 
ATOM   7468 C  CG  . TYR D  1 126 ? -2.677  17.362  -26.399 1.00 10.67 ? 126 TYR D CG  1 
ATOM   7469 C  CD1 . TYR D  1 126 ? -2.354  18.537  -25.690 1.00 12.25 ? 126 TYR D CD1 1 
ATOM   7470 C  CD2 . TYR D  1 126 ? -2.028  16.146  -25.973 1.00 10.40 ? 126 TYR D CD2 1 
ATOM   7471 C  CE1 . TYR D  1 126 ? -1.433  18.498  -24.636 1.00 11.20 ? 126 TYR D CE1 1 
ATOM   7472 C  CE2 . TYR D  1 126 ? -1.070  16.107  -24.964 1.00 11.12 ? 126 TYR D CE2 1 
ATOM   7473 C  CZ  . TYR D  1 126 ? -0.784  17.289  -24.255 1.00 11.90 ? 126 TYR D CZ  1 
ATOM   7474 O  OH  . TYR D  1 126 ? 0.107   17.263  -23.217 1.00 12.30 ? 126 TYR D OH  1 
ATOM   7475 N  N   . PRO D  1 127 ? -6.290  18.910  -28.693 1.00 15.24 ? 127 PRO D N   1 
ATOM   7476 C  CA  . PRO D  1 127 ? -7.436  18.990  -29.602 1.00 15.63 ? 127 PRO D CA  1 
ATOM   7477 C  C   . PRO D  1 127 ? -7.145  18.363  -30.897 1.00 17.84 ? 127 PRO D C   1 
ATOM   7478 O  O   . PRO D  1 127 ? -8.036  18.118  -31.703 1.00 21.20 ? 127 PRO D O   1 
ATOM   7479 C  CB  . PRO D  1 127 ? -7.535  20.548  -29.754 1.00 16.26 ? 127 PRO D CB  1 
ATOM   7480 C  CG  . PRO D  1 127 ? -6.160  21.056  -29.474 1.00 17.16 ? 127 PRO D CG  1 
ATOM   7481 C  CD  . PRO D  1 127 ? -5.659  20.201  -28.364 1.00 16.94 ? 127 PRO D CD  1 
ATOM   7482 N  N   . ASP D  1 128 ? -5.881  18.066  -31.175 1.00 15.16 ? 128 ASP D N   1 
ATOM   7483 C  CA  . ASP D  1 128 ? -5.506  17.480  -32.415 1.00 14.30 ? 128 ASP D CA  1 
ATOM   7484 C  C   . ASP D  1 128 ? -4.086  16.917  -32.418 1.00 14.50 ? 128 ASP D C   1 
ATOM   7485 O  O   . ASP D  1 128 ? -3.317  17.185  -31.486 1.00 14.41 ? 128 ASP D O   1 
ATOM   7486 C  CB  . ASP D  1 128 ? -5.631  18.610  -33.493 1.00 17.10 ? 128 ASP D CB  1 
ATOM   7487 C  CG  . ASP D  1 128 ? -4.603  19.730  -33.292 1.00 17.15 ? 128 ASP D CG  1 
ATOM   7488 O  OD1 . ASP D  1 128 ? -4.942  20.736  -32.563 1.00 21.34 ? 128 ASP D OD1 1 
ATOM   7489 O  OD2 . ASP D  1 128 ? -3.527  19.626  -33.865 1.00 20.65 ? 128 ASP D OD2 1 
ATOM   7490 N  N   . ALA D  1 129 ? -3.686  16.084  -33.375 1.00 13.76 ? 129 ALA D N   1 
ATOM   7491 C  CA  . ALA D  1 129 ? -2.437  15.384  -33.332 1.00 14.47 ? 129 ALA D CA  1 
ATOM   7492 C  C   . ALA D  1 129 ? -1.197  16.293  -33.455 1.00 13.63 ? 129 ALA D C   1 
ATOM   7493 O  O   . ALA D  1 129 ? -0.157  16.066  -32.839 1.00 13.91 ? 129 ALA D O   1 
ATOM   7494 C  CB  . ALA D  1 129 ? -2.420  14.385  -34.484 1.00 17.34 ? 129 ALA D CB  1 
ATOM   7495 N  N   A SER D  1 130 ? -1.290  17.348  -34.292 0.50 14.91 ? 130 SER D N   1 
ATOM   7496 N  N   B SER D  1 130 ? -1.321  17.345  -34.289 0.50 16.08 ? 130 SER D N   1 
ATOM   7497 C  CA  A SER D  1 130 ? -0.141  18.234  -34.418 0.50 13.60 ? 130 SER D CA  1 
ATOM   7498 C  CA  B SER D  1 130 ? -0.213  18.272  -34.440 0.50 15.48 ? 130 SER D CA  1 
ATOM   7499 C  C   A SER D  1 130 ? 0.114   18.989  -33.087 0.50 11.94 ? 130 SER D C   1 
ATOM   7500 C  C   B SER D  1 130 ? 0.096   18.976  -33.101 0.50 12.87 ? 130 SER D C   1 
ATOM   7501 O  O   A SER D  1 130 ? 1.276   19.070  -32.611 0.50 12.86 ? 130 SER D O   1 
ATOM   7502 O  O   B SER D  1 130 ? 1.266   19.015  -32.642 0.50 13.93 ? 130 SER D O   1 
ATOM   7503 C  CB  A SER D  1 130 ? -0.357  19.221  -35.587 0.50 13.43 ? 130 SER D CB  1 
ATOM   7504 C  CB  B SER D  1 130 ? -0.569  19.318  -35.513 0.50 16.72 ? 130 SER D CB  1 
ATOM   7505 O  OG  A SER D  1 130 ? -0.298  18.542  -36.819 0.50 14.28 ? 130 SER D OG  1 
ATOM   7506 O  OG  B SER D  1 130 ? 0.541   20.161  -35.726 0.50 20.93 ? 130 SER D OG  1 
ATOM   7507 N  N   . THR D  1 131 ? -0.941  19.454  -32.434 1.00 13.28 ? 131 THR D N   1 
ATOM   7508 C  CA  . THR D  1 131 ? -0.777  20.084  -31.108 1.00 12.27 ? 131 THR D CA  1 
ATOM   7509 C  C   . THR D  1 131 ? -0.196  19.080  -30.096 1.00 12.92 ? 131 THR D C   1 
ATOM   7510 O  O   . THR D  1 131 ? 0.667   19.405  -29.288 1.00 14.06 ? 131 THR D O   1 
ATOM   7511 C  CB  . THR D  1 131 ? -2.084  20.610  -30.621 1.00 13.74 ? 131 THR D CB  1 
ATOM   7512 O  OG1 . THR D  1 131 ? -2.626  21.635  -31.549 1.00 17.47 ? 131 THR D OG1 1 
ATOM   7513 C  CG2 . THR D  1 131 ? -1.934  21.297  -29.204 1.00 14.55 ? 131 THR D CG2 1 
ATOM   7514 N  N   . ALA D  1 132 ? -0.654  17.841  -30.174 1.00 11.42 ? 132 ALA D N   1 
ATOM   7515 C  CA  . ALA D  1 132 ? -0.214  16.851  -29.214 1.00 10.44 ? 132 ALA D CA  1 
ATOM   7516 C  C   . ALA D  1 132 ? 1.241   16.394  -29.347 1.00 9.47  ? 132 ALA D C   1 
ATOM   7517 O  O   . ALA D  1 132 ? 1.931   15.927  -28.429 1.00 10.71 ? 132 ALA D O   1 
ATOM   7518 C  CB  . ALA D  1 132 ? -1.100  15.578  -29.429 1.00 10.23 ? 132 ALA D CB  1 
ATOM   7519 N  N   . SER D  1 133 ? 1.738   16.552  -30.598 1.00 10.86 ? 133 SER D N   1 
ATOM   7520 C  CA  . SER D  1 133 ? 2.948   15.880  -30.997 1.00 11.28 ? 133 SER D CA  1 
ATOM   7521 C  C   . SER D  1 133 ? 4.225   16.259  -30.234 1.00 12.09 ? 133 SER D C   1 
ATOM   7522 O  O   . SER D  1 133 ? 5.170   15.482  -30.097 1.00 13.54 ? 133 SER D O   1 
ATOM   7523 C  CB  . SER D  1 133 ? 3.238   16.019  -32.532 1.00 14.20 ? 133 SER D CB  1 
ATOM   7524 O  OG  . SER D  1 133 ? 3.610   17.371  -32.841 1.00 18.17 ? 133 SER D OG  1 
ATOM   7525 N  N   . ASN D  1 134 ? 4.314   17.529  -29.738 1.00 11.52 ? 134 ASN D N   1 
ATOM   7526 C  CA  . ASN D  1 134 ? 5.406   17.963  -28.952 1.00 12.69 ? 134 ASN D CA  1 
ATOM   7527 C  C   . ASN D  1 134 ? 5.128   18.187  -27.485 1.00 13.96 ? 134 ASN D C   1 
ATOM   7528 O  O   . ASN D  1 134 ? 5.919   18.802  -26.782 1.00 14.68 ? 134 ASN D O   1 
ATOM   7529 C  CB  . ASN D  1 134 ? 6.072   19.228  -29.584 1.00 14.95 ? 134 ASN D CB  1 
ATOM   7530 C  CG  . ASN D  1 134 ? 5.181   20.450  -29.428 1.00 17.99 ? 134 ASN D CG  1 
ATOM   7531 O  OD1 . ASN D  1 134 ? 3.937   20.364  -29.245 1.00 17.50 ? 134 ASN D OD1 1 
ATOM   7532 N  ND2 . ASN D  1 134 ? 5.846   21.616  -29.331 1.00 17.27 ? 134 ASN D ND2 1 
ATOM   7533 N  N   . LYS D  1 135 ? 4.075   17.528  -27.030 1.00 12.37 ? 135 LYS D N   1 
ATOM   7534 C  CA  . LYS D  1 135 ? 3.620   17.752  -25.627 1.00 11.83 ? 135 LYS D CA  1 
ATOM   7535 C  C   . LYS D  1 135 ? 3.542   16.454  -24.855 1.00 12.46 ? 135 LYS D C   1 
ATOM   7536 O  O   . LYS D  1 135 ? 3.493   15.328  -25.416 1.00 11.97 ? 135 LYS D O   1 
ATOM   7537 C  CB  . LYS D  1 135 ? 2.245   18.454  -25.654 1.00 12.58 ? 135 LYS D CB  1 
ATOM   7538 C  CG  . LYS D  1 135 ? 2.427   19.942  -26.109 1.00 14.95 ? 135 LYS D CG  1 
ATOM   7539 C  CD  . LYS D  1 135 ? 1.082   20.663  -26.213 1.00 16.67 ? 135 LYS D CD  1 
ATOM   7540 C  CE  . LYS D  1 135 ? 1.284   22.005  -26.950 1.00 15.33 ? 135 LYS D CE  1 
ATOM   7541 N  NZ  . LYS D  1 135 ? 1.675   21.876  -28.421 1.00 16.17 ? 135 LYS D NZ  1 
ATOM   7542 N  N   . SER D  1 136 ? 3.552   16.650  -23.509 1.00 12.45 ? 136 SER D N   1 
ATOM   7543 C  CA  . SER D  1 136 ? 3.575   15.503  -22.599 1.00 12.72 ? 136 SER D CA  1 
ATOM   7544 C  C   . SER D  1 136 ? 2.463   14.494  -22.883 1.00 11.82 ? 136 SER D C   1 
ATOM   7545 O  O   . SER D  1 136 ? 1.270   14.854  -23.024 1.00 11.26 ? 136 SER D O   1 
ATOM   7546 C  CB  . SER D  1 136 ? 3.408   16.108  -21.192 1.00 15.05 ? 136 SER D CB  1 
ATOM   7547 O  OG  . SER D  1 136 ? 3.660   15.027  -20.289 1.00 19.47 ? 136 SER D OG  1 
ATOM   7548 N  N   . GLU D  1 137 ? 2.839   13.206  -22.884 1.00 11.84 ? 137 GLU D N   1 
ATOM   7549 C  CA  . GLU D  1 137 ? 1.868   12.178  -23.129 1.00 11.12 ? 137 GLU D CA  1 
ATOM   7550 C  C   . GLU D  1 137 ? 1.070   12.280  -24.439 1.00 10.64 ? 137 GLU D C   1 
ATOM   7551 O  O   . GLU D  1 137 ? -0.020  11.803  -24.592 1.00 11.34 ? 137 GLU D O   1 
ATOM   7552 C  CB  . GLU D  1 137 ? 0.859   12.025  -21.923 1.00 13.28 ? 137 GLU D CB  1 
ATOM   7553 C  CG  . GLU D  1 137 ? 1.495   11.981  -20.559 1.00 15.89 ? 137 GLU D CG  1 
ATOM   7554 C  CD  . GLU D  1 137 ? 2.330   10.734  -20.293 1.00 20.27 ? 137 GLU D CD  1 
ATOM   7555 O  OE1 . GLU D  1 137 ? 2.161   9.655   -20.929 1.00 23.55 ? 137 GLU D OE1 1 
ATOM   7556 O  OE2 . GLU D  1 137 ? 3.251   10.856  -19.455 1.00 29.95 ? 137 GLU D OE2 1 
ATOM   7557 N  N   . GLY D  1 138 ? 1.656   12.945  -25.436 1.00 10.46 ? 138 GLY D N   1 
ATOM   7558 C  CA  . GLY D  1 138 ? 0.910   13.358  -26.551 1.00 10.57 ? 138 GLY D CA  1 
ATOM   7559 C  C   . GLY D  1 138 ? 0.489   12.252  -27.511 1.00 8.73  ? 138 GLY D C   1 
ATOM   7560 O  O   . GLY D  1 138 ? -0.544  12.336  -28.131 1.00 9.27  ? 138 GLY D O   1 
ATOM   7561 N  N   . LEU D  1 139 ? 1.344   11.237  -27.687 1.00 9.00  ? 139 LEU D N   1 
ATOM   7562 C  CA  . LEU D  1 139 ? 1.094   10.246  -28.834 1.00 9.37  ? 139 LEU D CA  1 
ATOM   7563 C  C   . LEU D  1 139 ? 1.217   8.799   -28.321 1.00 8.36  ? 139 LEU D C   1 
ATOM   7564 O  O   . LEU D  1 139 ? 2.000   8.534   -27.359 1.00 8.74  ? 139 LEU D O   1 
ATOM   7565 C  CB  . LEU D  1 139 ? 2.183   10.447  -29.955 1.00 9.66  ? 139 LEU D CB  1 
ATOM   7566 C  CG  . LEU D  1 139 ? 2.181   11.853  -30.580 1.00 9.80  ? 139 LEU D CG  1 
ATOM   7567 C  CD1 . LEU D  1 139 ? 3.393   12.032  -31.546 1.00 12.26 ? 139 LEU D CD1 1 
ATOM   7568 C  CD2 . LEU D  1 139 ? 0.850   12.124  -31.354 1.00 12.68 ? 139 LEU D CD2 1 
ATOM   7569 N  N   . ALA D  1 140 ? 0.509   7.912   -29.025 1.00 8.89  ? 140 ALA D N   1 
ATOM   7570 C  CA  . ALA D  1 140 ? 0.697   6.487   -28.783 1.00 8.08  ? 140 ALA D CA  1 
ATOM   7571 C  C   . ALA D  1 140 ? 0.741   5.899   -30.171 1.00 8.32  ? 140 ALA D C   1 
ATOM   7572 O  O   . ALA D  1 140 ? -0.169  6.146   -30.991 1.00 9.01  ? 140 ALA D O   1 
ATOM   7573 C  CB  . ALA D  1 140 ? -0.453  5.894   -27.969 1.00 9.60  ? 140 ALA D CB  1 
ATOM   7574 N  N   . VAL D  1 141 ? 1.786   5.116   -30.444 1.00 8.24  ? 141 VAL D N   1 
ATOM   7575 C  CA  . VAL D  1 141 ? 1.922   4.462   -31.717 1.00 7.98  ? 141 VAL D CA  1 
ATOM   7576 C  C   . VAL D  1 141 ? 1.824   2.966   -31.571 1.00 8.04  ? 141 VAL D C   1 
ATOM   7577 O  O   . VAL D  1 141 ? 2.454   2.408   -30.632 1.00 8.90  ? 141 VAL D O   1 
ATOM   7578 C  CB  . VAL D  1 141 ? 3.222   4.904   -32.452 1.00 7.36  ? 141 VAL D CB  1 
ATOM   7579 C  CG1 . VAL D  1 141 ? 3.296   4.235   -33.849 1.00 8.33  ? 141 VAL D CG1 1 
ATOM   7580 C  CG2 . VAL D  1 141 ? 3.262   6.423   -32.551 1.00 8.10  ? 141 VAL D CG2 1 
ATOM   7581 N  N   . LEU D  1 142 ? 1.076   2.325   -32.453 1.00 7.86  ? 142 LEU D N   1 
ATOM   7582 C  CA  . LEU D  1 142 ? 1.102   0.845   -32.514 1.00 7.37  ? 142 LEU D CA  1 
ATOM   7583 C  C   . LEU D  1 142 ? 2.018   0.452   -33.670 1.00 8.26  ? 142 LEU D C   1 
ATOM   7584 O  O   . LEU D  1 142 ? 1.939   0.994   -34.777 1.00 9.49  ? 142 LEU D O   1 
ATOM   7585 C  CB  . LEU D  1 142 ? -0.274  0.307   -32.822 1.00 8.41  ? 142 LEU D CB  1 
ATOM   7586 C  CG  . LEU D  1 142 ? -1.400  0.713   -31.870 1.00 9.36  ? 142 LEU D CG  1 
ATOM   7587 C  CD1 . LEU D  1 142 ? -2.695  0.026   -32.364 1.00 10.69 ? 142 LEU D CD1 1 
ATOM   7588 C  CD2 . LEU D  1 142 ? -1.056  0.378   -30.394 1.00 11.59 ? 142 LEU D CD2 1 
ATOM   7589 N  N   . ALA D  1 143 ? 2.953   -0.460  -33.380 1.00 8.38  ? 143 ALA D N   1 
ATOM   7590 C  CA  . ALA D  1 143 ? 3.905   -0.943  -34.407 1.00 7.70  ? 143 ALA D CA  1 
ATOM   7591 C  C   . ALA D  1 143 ? 3.652   -2.414  -34.681 1.00 8.24  ? 143 ALA D C   1 
ATOM   7592 O  O   . ALA D  1 143 ? 3.567   -3.256  -33.779 1.00 8.69  ? 143 ALA D O   1 
ATOM   7593 C  CB  . ALA D  1 143 ? 5.299   -0.718  -33.892 1.00 8.03  ? 143 ALA D CB  1 
ATOM   7594 N  N   . VAL D  1 144 ? 3.527   -2.663  -35.986 1.00 6.90  ? 144 VAL D N   1 
ATOM   7595 C  CA  . VAL D  1 144 ? 3.369   -4.062  -36.485 1.00 7.83  ? 144 VAL D CA  1 
ATOM   7596 C  C   . VAL D  1 144 ? 4.602   -4.357  -37.318 1.00 7.55  ? 144 VAL D C   1 
ATOM   7597 O  O   . VAL D  1 144 ? 4.907   -3.712  -38.330 1.00 7.89  ? 144 VAL D O   1 
ATOM   7598 C  CB  . VAL D  1 144 ? 2.112   -4.231  -37.312 1.00 8.06  ? 144 VAL D CB  1 
ATOM   7599 C  CG1 . VAL D  1 144 ? 2.021   -5.706  -37.778 1.00 9.39  ? 144 VAL D CG1 1 
ATOM   7600 C  CG2 . VAL D  1 144 ? 0.862   -3.823  -36.526 1.00 9.00  ? 144 VAL D CG2 1 
ATOM   7601 N  N   . LEU D  1 145 ? 5.377   -5.383  -36.896 1.00 7.46  ? 145 LEU D N   1 
ATOM   7602 C  CA  . LEU D  1 145 ? 6.538   -5.857  -37.655 1.00 8.42  ? 145 LEU D CA  1 
ATOM   7603 C  C   . LEU D  1 145 ? 6.060   -6.698  -38.829 1.00 8.45  ? 145 LEU D C   1 
ATOM   7604 O  O   . LEU D  1 145 ? 5.105   -7.481  -38.697 1.00 8.33  ? 145 LEU D O   1 
ATOM   7605 C  CB  . LEU D  1 145 ? 7.413   -6.723  -36.758 1.00 8.97  ? 145 LEU D CB  1 
ATOM   7606 C  CG  . LEU D  1 145 ? 7.944   -5.979  -35.575 1.00 10.35 ? 145 LEU D CG  1 
ATOM   7607 C  CD1 . LEU D  1 145 ? 8.444   -6.963  -34.480 1.00 11.84 ? 145 LEU D CD1 1 
ATOM   7608 C  CD2 . LEU D  1 145 ? 9.043   -5.035  -35.952 1.00 13.49 ? 145 LEU D CD2 1 
ATOM   7609 N  N   . ILE D  1 146 ? 6.619   -6.478  -40.010 1.00 8.27  ? 146 ILE D N   1 
ATOM   7610 C  CA  . ILE D  1 146 ? 6.166   -7.106  -41.224 1.00 8.43  ? 146 ILE D CA  1 
ATOM   7611 C  C   . ILE D  1 146 ? 7.278   -7.983  -41.789 1.00 8.24  ? 146 ILE D C   1 
ATOM   7612 O  O   . ILE D  1 146 ? 8.394   -7.471  -42.048 1.00 8.32  ? 146 ILE D O   1 
ATOM   7613 C  CB  . ILE D  1 146 ? 5.805   -6.070  -42.285 1.00 7.69  ? 146 ILE D CB  1 
ATOM   7614 C  CG1 . ILE D  1 146 ? 4.646   -5.205  -41.803 1.00 8.84  ? 146 ILE D CG1 1 
ATOM   7615 C  CG2 . ILE D  1 146 ? 5.458   -6.737  -43.648 1.00 8.56  ? 146 ILE D CG2 1 
ATOM   7616 C  CD1 . ILE D  1 146 ? 4.367   -3.968  -42.695 1.00 9.83  ? 146 ILE D CD1 1 
ATOM   7617 N  N   A GLU D  1 147 ? 6.949   -9.267  -41.965 0.50 8.30  ? 147 GLU D N   1 
ATOM   7618 N  N   B GLU D  1 147 ? 7.019   -9.267  -41.986 0.50 9.12  ? 147 GLU D N   1 
ATOM   7619 C  CA  A GLU D  1 147 ? 7.833   -10.300 -42.502 0.50 8.73  ? 147 GLU D CA  1 
ATOM   7620 C  CA  B GLU D  1 147 ? 8.056   -10.205 -42.474 0.50 10.08 ? 147 GLU D CA  1 
ATOM   7621 C  C   A GLU D  1 147 ? 7.536   -10.566 -43.994 0.50 8.28  ? 147 GLU D C   1 
ATOM   7622 C  C   B GLU D  1 147 ? 7.629   -10.657 -43.834 0.50 9.09  ? 147 GLU D C   1 
ATOM   7623 O  O   A GLU D  1 147 ? 6.387   -10.536 -44.456 0.50 7.40  ? 147 GLU D O   1 
ATOM   7624 O  O   B GLU D  1 147 ? 6.456   -10.849 -44.046 0.50 8.48  ? 147 GLU D O   1 
ATOM   7625 C  CB  A GLU D  1 147 ? 7.664   -11.622 -41.711 0.50 8.61  ? 147 GLU D CB  1 
ATOM   7626 C  CB  B GLU D  1 147 ? 8.096   -11.395 -41.466 0.50 11.89 ? 147 GLU D CB  1 
ATOM   7627 C  CG  A GLU D  1 147 ? 8.820   -12.591 -41.909 0.50 10.94 ? 147 GLU D CG  1 
ATOM   7628 C  CG  B GLU D  1 147 ? 8.345   -12.819 -41.920 0.50 16.59 ? 147 GLU D CG  1 
ATOM   7629 C  CD  A GLU D  1 147 ? 8.872   -13.680 -40.854 0.50 12.29 ? 147 GLU D CD  1 
ATOM   7630 C  CD  B GLU D  1 147 ? 8.038   -13.807 -40.788 0.50 19.47 ? 147 GLU D CD  1 
ATOM   7631 O  OE1 A GLU D  1 147 ? 8.038   -13.655 -39.925 0.50 13.57 ? 147 GLU D OE1 1 
ATOM   7632 O  OE1 B GLU D  1 147 ? 8.734   -13.764 -39.748 0.50 17.18 ? 147 GLU D OE1 1 
ATOM   7633 O  OE2 A GLU D  1 147 ? 9.750   -14.563 -40.957 0.50 18.05 ? 147 GLU D OE2 1 
ATOM   7634 O  OE2 B GLU D  1 147 ? 7.084   -14.600 -40.922 0.50 19.72 ? 147 GLU D OE2 1 
ATOM   7635 N  N   . MET D  1 148 ? 8.585   -10.870 -44.767 1.00 9.47  ? 148 MET D N   1 
ATOM   7636 C  CA  . MET D  1 148 ? 8.356   -11.433 -46.097 1.00 9.48  ? 148 MET D CA  1 
ATOM   7637 C  C   . MET D  1 148 ? 7.767   -12.814 -45.984 1.00 8.69  ? 148 MET D C   1 
ATOM   7638 O  O   . MET D  1 148 ? 8.337   -13.688 -45.325 1.00 9.84  ? 148 MET D O   1 
ATOM   7639 C  CB  . MET D  1 148 ? 9.670   -11.447 -46.885 1.00 9.45  ? 148 MET D CB  1 
ATOM   7640 C  CG  . MET D  1 148 ? 9.454   -11.880 -48.278 1.00 10.71 ? 148 MET D CG  1 
ATOM   7641 S  SD  . MET D  1 148 ? 11.011  -11.943 -49.270 1.00 12.39 ? 148 MET D SD  1 
ATOM   7642 C  CE  . MET D  1 148 ? 11.519  -10.202 -49.247 1.00 12.83 ? 148 MET D CE  1 
ATOM   7643 N  N   . GLY D  1 149 ? 6.603   -12.983 -46.608 1.00 8.55  ? 149 GLY D N   1 
ATOM   7644 C  CA  . GLY D  1 149 ? 5.825   -14.211 -46.439 1.00 8.81  ? 149 GLY D CA  1 
ATOM   7645 C  C   . GLY D  1 149 ? 4.757   -14.307 -47.511 1.00 8.70  ? 149 GLY D C   1 
ATOM   7646 O  O   . GLY D  1 149 ? 4.938   -14.106 -48.691 1.00 9.25  ? 149 GLY D O   1 
ATOM   7647 N  N   . SER D  1 150 ? 3.544   -14.667 -47.060 1.00 9.40  ? 150 SER D N   1 
ATOM   7648 C  CA  . SER D  1 150 ? 2.358   -14.810 -47.949 1.00 9.50  ? 150 SER D CA  1 
ATOM   7649 C  C   . SER D  1 150 ? 1.783   -13.466 -48.321 1.00 9.70  ? 150 SER D C   1 
ATOM   7650 O  O   . SER D  1 150 ? 1.865   -12.508 -47.537 1.00 9.64  ? 150 SER D O   1 
ATOM   7651 C  CB  . SER D  1 150 ? 1.308   -15.603 -47.196 1.00 10.01 ? 150 SER D CB  1 
ATOM   7652 O  OG  . SER D  1 150 ? 1.740   -17.000 -47.092 1.00 10.80 ? 150 SER D OG  1 
ATOM   7653 N  N   . PHE D  1 151 ? 1.184   -13.428 -49.515 1.00 10.25 ? 151 PHE D N   1 
ATOM   7654 C  CA  . PHE D  1 151 ? 0.408   -12.280 -49.956 1.00 9.00  ? 151 PHE D CA  1 
ATOM   7655 C  C   . PHE D  1 151 ? -0.661  -11.942 -48.923 1.00 10.44 ? 151 PHE D C   1 
ATOM   7656 O  O   . PHE D  1 151 ? -1.312  -12.827 -48.351 1.00 11.20 ? 151 PHE D O   1 
ATOM   7657 C  CB  . PHE D  1 151 ? -0.241  -12.643 -51.295 1.00 9.35  ? 151 PHE D CB  1 
ATOM   7658 C  CG  . PHE D  1 151 ? -1.087  -11.498 -51.814 1.00 10.66 ? 151 PHE D CG  1 
ATOM   7659 C  CD1 . PHE D  1 151 ? -0.528  -10.426 -52.480 1.00 12.74 ? 151 PHE D CD1 1 
ATOM   7660 C  CD2 . PHE D  1 151 ? -2.443  -11.569 -51.653 1.00 12.28 ? 151 PHE D CD2 1 
ATOM   7661 C  CE1 . PHE D  1 151 ? -1.366  -9.313  -52.921 1.00 11.64 ? 151 PHE D CE1 1 
ATOM   7662 C  CE2 . PHE D  1 151 ? -3.259  -10.550 -52.072 1.00 11.70 ? 151 PHE D CE2 1 
ATOM   7663 C  CZ  . PHE D  1 151 ? -2.710  -9.455  -52.708 1.00 11.59 ? 151 PHE D CZ  1 
ATOM   7664 N  N   . ASN D  1 152 ? -0.828  -10.638 -48.662 1.00 9.08  ? 152 ASN D N   1 
ATOM   7665 C  CA  . ASN D  1 152 ? -1.698  -10.193 -47.615 1.00 10.07 ? 152 ASN D CA  1 
ATOM   7666 C  C   . ASN D  1 152 ? -2.769  -9.303  -48.261 1.00 11.03 ? 152 ASN D C   1 
ATOM   7667 O  O   . ASN D  1 152 ? -2.493  -8.127  -48.643 1.00 10.27 ? 152 ASN D O   1 
ATOM   7668 C  CB  . ASN D  1 152 ? -0.901  -9.406  -46.558 1.00 9.05  ? 152 ASN D CB  1 
ATOM   7669 C  CG  . ASN D  1 152 ? -1.695  -9.106  -45.289 1.00 8.90  ? 152 ASN D CG  1 
ATOM   7670 O  OD1 . ASN D  1 152 ? -2.812  -8.573  -45.414 1.00 10.29 ? 152 ASN D OD1 1 
ATOM   7671 N  ND2 . ASN D  1 152 ? -1.159  -9.377  -44.143 1.00 9.39  ? 152 ASN D ND2 1 
ATOM   7672 N  N   . PRO D  1 153 ? -4.020  -9.833  -48.422 1.00 11.37 ? 153 PRO D N   1 
ATOM   7673 C  CA  . PRO D  1 153 ? -5.038  -9.034  -49.116 1.00 11.26 ? 153 PRO D CA  1 
ATOM   7674 C  C   . PRO D  1 153 ? -5.431  -7.740  -48.365 1.00 10.97 ? 153 PRO D C   1 
ATOM   7675 O  O   . PRO D  1 153 ? -5.816  -6.792  -48.997 1.00 12.90 ? 153 PRO D O   1 
ATOM   7676 C  CB  . PRO D  1 153 ? -6.263  -9.999  -49.190 1.00 13.82 ? 153 PRO D CB  1 
ATOM   7677 C  CG  . PRO D  1 153 ? -5.712  -11.359 -48.985 1.00 18.25 ? 153 PRO D CG  1 
ATOM   7678 C  CD  . PRO D  1 153 ? -4.485  -11.203 -48.065 1.00 13.57 ? 153 PRO D CD  1 
ATOM   7679 N  N   . SER D  1 154 ? -5.264  -7.738  -47.057 1.00 10.03 ? 154 SER D N   1 
ATOM   7680 C  CA  . SER D  1 154 ? -5.679  -6.546  -46.307 1.00 10.82 ? 154 SER D CA  1 
ATOM   7681 C  C   . SER D  1 154 ? -4.645  -5.443  -46.511 1.00 11.22 ? 154 SER D C   1 
ATOM   7682 O  O   . SER D  1 154 ? -5.001  -4.269  -46.779 1.00 11.00 ? 154 SER D O   1 
ATOM   7683 C  CB  . SER D  1 154 ? -5.791  -6.895  -44.838 1.00 11.39 ? 154 SER D CB  1 
ATOM   7684 O  OG  . SER D  1 154 ? -6.802  -7.877  -44.637 1.00 15.31 ? 154 SER D OG  1 
ATOM   7685 N  N   . TYR D  1 155 ? -3.316  -5.776  -46.414 1.00 9.67  ? 155 TYR D N   1 
ATOM   7686 C  CA  . TYR D  1 155 ? -2.328  -4.724  -46.698 1.00 9.67  ? 155 TYR D CA  1 
ATOM   7687 C  C   . TYR D  1 155 ? -2.403  -4.307  -48.157 1.00 9.18  ? 155 TYR D C   1 
ATOM   7688 O  O   . TYR D  1 155 ? -2.095  -3.121  -48.533 1.00 9.96  ? 155 TYR D O   1 
ATOM   7689 C  CB  . TYR D  1 155 ? -0.859  -5.152  -46.418 1.00 8.32  ? 155 TYR D CB  1 
ATOM   7690 C  CG  . TYR D  1 155 ? -0.508  -5.013  -44.954 1.00 7.83  ? 155 TYR D CG  1 
ATOM   7691 C  CD1 . TYR D  1 155 ? 0.239   -3.937  -44.498 1.00 8.53  ? 155 TYR D CD1 1 
ATOM   7692 C  CD2 . TYR D  1 155 ? -0.955  -5.941  -44.021 1.00 8.56  ? 155 TYR D CD2 1 
ATOM   7693 C  CE1 . TYR D  1 155 ? 0.545   -3.797  -43.156 1.00 9.31  ? 155 TYR D CE1 1 
ATOM   7694 C  CE2 . TYR D  1 155 ? -0.652  -5.811  -42.678 1.00 8.93  ? 155 TYR D CE2 1 
ATOM   7695 C  CZ  . TYR D  1 155 ? 0.096   -4.738  -42.247 1.00 9.24  ? 155 TYR D CZ  1 
ATOM   7696 O  OH  . TYR D  1 155 ? 0.394   -4.621  -40.907 1.00 9.94  ? 155 TYR D OH  1 
ATOM   7697 N  N   . ASP D  1 156 ? -2.856  -5.210  -49.071 1.00 9.51  ? 156 ASP D N   1 
ATOM   7698 C  CA  . ASP D  1 156 ? -2.985  -4.803  -50.426 1.00 10.40 ? 156 ASP D CA  1 
ATOM   7699 C  C   . ASP D  1 156 ? -4.105  -3.694  -50.682 1.00 9.47  ? 156 ASP D C   1 
ATOM   7700 O  O   . ASP D  1 156 ? -4.069  -3.046  -51.715 1.00 11.60 ? 156 ASP D O   1 
ATOM   7701 C  CB  . ASP D  1 156 ? -3.229  -6.018  -51.363 1.00 11.08 ? 156 ASP D CB  1 
ATOM   7702 C  CG  . ASP D  1 156 ? -2.415  -5.908  -52.635 1.00 13.24 ? 156 ASP D CG  1 
ATOM   7703 O  OD1 . ASP D  1 156 ? -1.192  -5.697  -52.514 1.00 12.19 ? 156 ASP D OD1 1 
ATOM   7704 O  OD2 . ASP D  1 156 ? -2.985  -5.980  -53.745 1.00 16.21 ? 156 ASP D OD2 1 
ATOM   7705 N  N   . LYS D  1 157 ? -5.026  -3.589  -49.722 1.00 10.80 ? 157 LYS D N   1 
ATOM   7706 C  CA  . LYS D  1 157 ? -6.053  -2.504  -49.831 1.00 12.76 ? 157 LYS D CA  1 
ATOM   7707 C  C   . LYS D  1 157 ? -5.332  -1.154  -49.753 1.00 12.63 ? 157 LYS D C   1 
ATOM   7708 O  O   . LYS D  1 157 ? -5.864  -0.160  -50.379 1.00 13.86 ? 157 LYS D O   1 
ATOM   7709 C  CB  . LYS D  1 157 ? -7.095  -2.663  -48.764 1.00 12.60 ? 157 LYS D CB  1 
ATOM   7710 C  CG  . LYS D  1 157 ? -7.926  -3.971  -48.962 1.00 14.41 ? 157 LYS D CG  1 
ATOM   7711 C  CD  . LYS D  1 157 ? -8.808  -4.225  -47.715 1.00 19.69 ? 157 LYS D CD  1 
ATOM   7712 C  CE  . LYS D  1 157 ? -9.616  -5.528  -47.876 1.00 22.92 ? 157 LYS D CE  1 
ATOM   7713 N  NZ  . LYS D  1 157 ? -10.299 -6.073  -46.628 1.00 25.06 ? 157 LYS D NZ  1 
ATOM   7714 N  N   . ILE D  1 158 ? -4.115  -1.070  -49.186 1.00 11.23 ? 158 ILE D N   1 
ATOM   7715 C  CA  . ILE D  1 158 ? -3.314  0.188   -49.234 1.00 11.70 ? 158 ILE D CA  1 
ATOM   7716 C  C   . ILE D  1 158 ? -2.459  0.108   -50.491 1.00 10.72 ? 158 ILE D C   1 
ATOM   7717 O  O   . ILE D  1 158 ? -2.391  1.043   -51.280 1.00 11.29 ? 158 ILE D O   1 
ATOM   7718 C  CB  . ILE D  1 158 ? -2.468  0.325   -47.948 1.00 12.77 ? 158 ILE D CB  1 
ATOM   7719 C  CG1 . ILE D  1 158 ? -3.382  0.503   -46.719 1.00 14.45 ? 158 ILE D CG1 1 
ATOM   7720 C  CG2 . ILE D  1 158 ? -1.441  1.448   -48.144 1.00 12.31 ? 158 ILE D CG2 1 
ATOM   7721 C  CD1 . ILE D  1 158 ? -2.633  0.301   -45.456 1.00 16.19 ? 158 ILE D CD1 1 
ATOM   7722 N  N   . PHE D  1 159 ? -1.742  -1.045  -50.668 1.00 10.60 ? 159 PHE D N   1 
ATOM   7723 C  CA  . PHE D  1 159 ? -0.680  -1.020  -51.673 1.00 11.08 ? 159 PHE D CA  1 
ATOM   7724 C  C   . PHE D  1 159 ? -1.189  -0.935  -53.104 1.00 11.16 ? 159 PHE D C   1 
ATOM   7725 O  O   . PHE D  1 159 ? -0.490  -0.466  -53.962 1.00 12.03 ? 159 PHE D O   1 
ATOM   7726 C  CB  . PHE D  1 159 ? 0.189   -2.332  -51.602 1.00 9.54  ? 159 PHE D CB  1 
ATOM   7727 C  CG  . PHE D  1 159 ? 0.891   -2.550  -50.259 1.00 10.24 ? 159 PHE D CG  1 
ATOM   7728 C  CD1 . PHE D  1 159 ? 1.308   -1.545  -49.480 1.00 12.70 ? 159 PHE D CD1 1 
ATOM   7729 C  CD2 . PHE D  1 159 ? 1.142   -3.868  -49.871 1.00 12.32 ? 159 PHE D CD2 1 
ATOM   7730 C  CE1 . PHE D  1 159 ? 1.974   -1.828  -48.246 1.00 12.26 ? 159 PHE D CE1 1 
ATOM   7731 C  CE2 . PHE D  1 159 ? 1.820   -4.112  -48.681 1.00 11.78 ? 159 PHE D CE2 1 
ATOM   7732 C  CZ  . PHE D  1 159 ? 2.236   -3.119  -47.867 1.00 12.38 ? 159 PHE D CZ  1 
ATOM   7733 N  N   . SER D  1 160 ? -2.443  -1.321  -53.364 1.00 11.85 ? 160 SER D N   1 
ATOM   7734 C  CA  . SER D  1 160 ? -2.954  -1.158  -54.734 1.00 11.37 ? 160 SER D CA  1 
ATOM   7735 C  C   . SER D  1 160 ? -3.088  0.239   -55.171 1.00 12.25 ? 160 SER D C   1 
ATOM   7736 O  O   . SER D  1 160 ? -3.171  0.425   -56.395 1.00 14.96 ? 160 SER D O   1 
ATOM   7737 C  CB  . SER D  1 160 ? -4.312  -1.890  -54.825 1.00 14.07 ? 160 SER D CB  1 
ATOM   7738 O  OG  . SER D  1 160 ? -5.291  -1.262  -53.996 1.00 15.20 ? 160 SER D OG  1 
ATOM   7739 N  N   . HIS D  1 161 ? -2.996  1.230   -54.268 1.00 10.75 ? 161 HIS D N   1 
ATOM   7740 C  CA  . HIS D  1 161 ? -3.080  2.633   -54.583 1.00 11.39 ? 161 HIS D CA  1 
ATOM   7741 C  C   . HIS D  1 161 ? -1.731  3.284   -54.702 1.00 12.19 ? 161 HIS D C   1 
ATOM   7742 O  O   . HIS D  1 161 ? -1.681  4.490   -55.034 1.00 13.72 ? 161 HIS D O   1 
ATOM   7743 C  CB  . HIS D  1 161 ? -3.923  3.389   -53.512 1.00 12.03 ? 161 HIS D CB  1 
ATOM   7744 C  CG  . HIS D  1 161 ? -5.290  2.943   -53.421 1.00 13.77 ? 161 HIS D CG  1 
ATOM   7745 N  ND1 . HIS D  1 161 ? -6.301  3.535   -54.173 1.00 17.62 ? 161 HIS D ND1 1 
ATOM   7746 C  CD2 . HIS D  1 161 ? -5.872  1.898   -52.690 1.00 14.80 ? 161 HIS D CD2 1 
ATOM   7747 C  CE1 . HIS D  1 161 ? -7.480  2.889   -53.915 1.00 17.85 ? 161 HIS D CE1 1 
ATOM   7748 N  NE2 . HIS D  1 161 ? -7.212  1.864   -53.015 1.00 16.27 ? 161 HIS D NE2 1 
ATOM   7749 N  N   . LEU D  1 162 ? -0.590  2.551   -54.562 1.00 12.04 ? 162 LEU D N   1 
ATOM   7750 C  CA  . LEU D  1 162 ? 0.706   3.284   -54.494 1.00 13.73 ? 162 LEU D CA  1 
ATOM   7751 C  C   . LEU D  1 162 ? 1.005   3.948   -55.811 1.00 14.55 ? 162 LEU D C   1 
ATOM   7752 O  O   . LEU D  1 162 ? 1.646   5.008   -55.832 1.00 16.06 ? 162 LEU D O   1 
ATOM   7753 C  CB  . LEU D  1 162 ? 1.774   2.189   -54.220 1.00 14.70 ? 162 LEU D CB  1 
ATOM   7754 C  CG  . LEU D  1 162 ? 1.819   1.578   -52.804 1.00 16.48 ? 162 LEU D CG  1 
ATOM   7755 C  CD1 . LEU D  1 162 ? 2.822   0.408   -52.856 1.00 18.73 ? 162 LEU D CD1 1 
ATOM   7756 C  CD2 . LEU D  1 162 ? 2.270   2.681   -51.837 1.00 19.80 ? 162 LEU D CD2 1 
ATOM   7757 N  N   A GLN D  1 163 ? 0.564   3.335   -56.912 0.50 16.26 ? 163 GLN D N   1 
ATOM   7758 N  N   B GLN D  1 163 ? 0.540   3.361   -56.930 0.50 16.90 ? 163 GLN D N   1 
ATOM   7759 C  CA  A GLN D  1 163 ? 0.863   3.958   -58.199 0.50 16.74 ? 163 GLN D CA  1 
ATOM   7760 C  CA  B GLN D  1 163 ? 0.711   3.980   -58.285 0.50 18.05 ? 163 GLN D CA  1 
ATOM   7761 C  C   A GLN D  1 163 ? 0.068   5.226   -58.543 0.50 16.60 ? 163 GLN D C   1 
ATOM   7762 C  C   B GLN D  1 163 ? 0.171   5.425   -58.443 0.50 17.77 ? 163 GLN D C   1 
ATOM   7763 O  O   A GLN D  1 163 ? 0.214   5.647   -59.684 0.50 17.09 ? 163 GLN D O   1 
ATOM   7764 O  O   B GLN D  1 163 ? 0.598   6.231   -59.272 0.50 19.65 ? 163 GLN D O   1 
ATOM   7765 C  CB  A GLN D  1 163 ? 0.702   2.981   -59.383 0.50 18.47 ? 163 GLN D CB  1 
ATOM   7766 C  CB  B GLN D  1 163 ? 0.089   3.063   -59.377 0.50 19.57 ? 163 GLN D CB  1 
ATOM   7767 C  CG  A GLN D  1 163 ? 1.661   1.808   -59.480 0.50 18.91 ? 163 GLN D CG  1 
ATOM   7768 C  CG  B GLN D  1 163 ? -1.202  2.331   -59.010 0.50 23.98 ? 163 GLN D CG  1 
ATOM   7769 C  CD  A GLN D  1 163 ? 3.156   2.158   -59.509 0.50 17.90 ? 163 GLN D CD  1 
ATOM   7770 C  CD  B GLN D  1 163 ? -1.593  1.304   -60.081 0.50 24.95 ? 163 GLN D CD  1 
ATOM   7771 O  OE1 A GLN D  1 163 ? 3.571   3.128   -60.141 0.50 21.03 ? 163 GLN D OE1 1 
ATOM   7772 O  OE1 B GLN D  1 163 ? -1.382  0.103   -59.904 0.50 30.64 ? 163 GLN D OE1 1 
ATOM   7773 N  NE2 A GLN D  1 163 ? 3.957   1.294   -58.931 0.50 20.02 ? 163 GLN D NE2 1 
ATOM   7774 N  NE2 B GLN D  1 163 ? -2.173  1.773   -61.181 0.50 24.52 ? 163 GLN D NE2 1 
ATOM   7775 N  N   . HIS D  1 164 ? -0.796  5.739   -57.634 1.00 15.29 ? 164 HIS D N   1 
ATOM   7776 C  CA  . HIS D  1 164 ? -1.413  7.044   -57.671 1.00 15.87 ? 164 HIS D CA  1 
ATOM   7777 C  C   . HIS D  1 164 ? -0.864  8.056   -56.728 1.00 18.60 ? 164 HIS D C   1 
ATOM   7778 O  O   . HIS D  1 164 ? -1.336  9.199   -56.661 1.00 18.17 ? 164 HIS D O   1 
ATOM   7779 C  CB  . HIS D  1 164 ? -2.908  6.816   -57.474 1.00 18.16 ? 164 HIS D CB  1 
ATOM   7780 C  CG  . HIS D  1 164 ? -3.497  5.839   -58.506 1.00 22.74 ? 164 HIS D CG  1 
ATOM   7781 N  ND1 . HIS D  1 164 ? -3.723  6.184   -59.764 1.00 27.97 ? 164 HIS D ND1 1 
ATOM   7782 C  CD2 . HIS D  1 164 ? -3.828  4.477   -58.405 1.00 31.61 ? 164 HIS D CD2 1 
ATOM   7783 C  CE1 . HIS D  1 164 ? -4.232  5.118   -60.468 1.00 27.59 ? 164 HIS D CE1 1 
ATOM   7784 N  NE2 . HIS D  1 164 ? -4.265  4.067   -59.646 1.00 35.07 ? 164 HIS D NE2 1 
ATOM   7785 N  N   . VAL D  1 165 ? 0.165   7.665   -55.942 1.00 13.66 ? 165 VAL D N   1 
ATOM   7786 C  CA  . VAL D  1 165 ? 0.801   8.615   -55.018 1.00 12.86 ? 165 VAL D CA  1 
ATOM   7787 C  C   . VAL D  1 165 ? 2.319   8.539   -55.177 1.00 12.98 ? 165 VAL D C   1 
ATOM   7788 O  O   . VAL D  1 165 ? 3.073   8.666   -54.162 1.00 12.17 ? 165 VAL D O   1 
ATOM   7789 C  CB  . VAL D  1 165 ? 0.334   8.398   -53.488 1.00 14.97 ? 165 VAL D CB  1 
ATOM   7790 C  CG1 . VAL D  1 165 ? -1.148  8.778   -53.275 1.00 15.17 ? 165 VAL D CG1 1 
ATOM   7791 C  CG2 . VAL D  1 165 ? 0.608   6.955   -53.035 1.00 13.57 ? 165 VAL D CG2 1 
ATOM   7792 N  N   . LYS D  1 166 ? 2.806   8.360   -56.421 1.00 12.40 ? 166 LYS D N   1 
ATOM   7793 C  CA  . LYS D  1 166 ? 4.196   8.137   -56.656 1.00 12.72 ? 166 LYS D CA  1 
ATOM   7794 C  C   . LYS D  1 166 ? 5.058   9.319   -56.209 1.00 12.18 ? 166 LYS D C   1 
ATOM   7795 O  O   . LYS D  1 166 ? 6.198   9.119   -55.748 1.00 12.49 ? 166 LYS D O   1 
ATOM   7796 C  CB  . LYS D  1 166 ? 4.423   7.913   -58.154 1.00 14.01 ? 166 LYS D CB  1 
ATOM   7797 C  CG  . LYS D  1 166 ? 3.780   6.585   -58.569 1.00 17.46 ? 166 LYS D CG  1 
ATOM   7798 C  CD  . LYS D  1 166 ? 3.943   6.209   -60.074 1.00 21.15 ? 166 LYS D CD  1 
ATOM   7799 C  CE  . LYS D  1 166 ? 5.384   5.911   -60.391 1.00 22.88 ? 166 LYS D CE  1 
ATOM   7800 N  NZ  . LYS D  1 166 ? 5.908   4.638   -59.783 1.00 21.86 ? 166 LYS D NZ  1 
ATOM   7801 N  N   . TYR D  1 167 ? 4.557   10.543  -56.299 1.00 14.02 ? 167 TYR D N   1 
ATOM   7802 C  CA  . TYR D  1 167 ? 5.440   11.698  -55.956 1.00 13.70 ? 167 TYR D CA  1 
ATOM   7803 C  C   . TYR D  1 167 ? 4.989   12.530  -54.785 1.00 12.36 ? 167 TYR D C   1 
ATOM   7804 O  O   . TYR D  1 167 ? 3.765   12.512  -54.447 1.00 12.63 ? 167 TYR D O   1 
ATOM   7805 C  CB  . TYR D  1 167 ? 5.511   12.597  -57.202 1.00 15.74 ? 167 TYR D CB  1 
ATOM   7806 C  CG  . TYR D  1 167 ? 6.114   11.876  -58.379 1.00 17.93 ? 167 TYR D CG  1 
ATOM   7807 C  CD1 . TYR D  1 167 ? 7.478   11.678  -58.437 1.00 22.39 ? 167 TYR D CD1 1 
ATOM   7808 C  CD2 . TYR D  1 167 ? 5.327   11.351  -59.402 1.00 22.87 ? 167 TYR D CD2 1 
ATOM   7809 C  CE1 . TYR D  1 167 ? 8.058   11.000  -59.481 1.00 24.90 ? 167 TYR D CE1 1 
ATOM   7810 C  CE2 . TYR D  1 167 ? 5.904   10.667  -60.460 1.00 26.16 ? 167 TYR D CE2 1 
ATOM   7811 C  CZ  . TYR D  1 167 ? 7.277   10.499  -60.488 1.00 28.43 ? 167 TYR D CZ  1 
ATOM   7812 O  OH  . TYR D  1 167 ? 7.911   9.831   -61.507 1.00 31.46 ? 167 TYR D OH  1 
ATOM   7813 N  N   . LYS D  1 168 ? 5.952   13.230  -54.154 1.00 11.79 ? 168 LYS D N   1 
ATOM   7814 C  CA  . LYS D  1 168 ? 5.618   14.056  -52.966 1.00 13.26 ? 168 LYS D CA  1 
ATOM   7815 C  C   . LYS D  1 168 ? 4.444   14.938  -53.219 1.00 14.20 ? 168 LYS D C   1 
ATOM   7816 O  O   . LYS D  1 168 ? 4.382   15.618  -54.252 1.00 16.51 ? 168 LYS D O   1 
ATOM   7817 C  CB  . LYS D  1 168 ? 6.810   14.926  -52.559 1.00 13.05 ? 168 LYS D CB  1 
ATOM   7818 C  CG  . LYS D  1 168 ? 6.508   15.697  -51.305 1.00 14.82 ? 168 LYS D CG  1 
ATOM   7819 C  CD  . LYS D  1 168 ? 7.756   16.419  -50.853 1.00 17.23 ? 168 LYS D CD  1 
ATOM   7820 C  CE  . LYS D  1 168 ? 7.418   17.380  -49.734 1.00 22.80 ? 168 LYS D CE  1 
ATOM   7821 N  NZ  . LYS D  1 168 ? 8.641   17.834  -49.011 1.00 28.48 ? 168 LYS D NZ  1 
ATOM   7822 N  N   . GLY D  1 169 ? 3.511   14.976  -52.290 1.00 14.32 ? 169 GLY D N   1 
ATOM   7823 C  CA  . GLY D  1 169 ? 2.319   15.829  -52.414 1.00 16.85 ? 169 GLY D CA  1 
ATOM   7824 C  C   . GLY D  1 169 ? 1.105   15.197  -53.073 1.00 17.76 ? 169 GLY D C   1 
ATOM   7825 O  O   . GLY D  1 169 ? -0.034  15.716  -52.996 1.00 20.85 ? 169 GLY D O   1 
ATOM   7826 N  N   . GLN D  1 170 ? 1.299   14.101  -53.826 1.00 13.68 ? 170 GLN D N   1 
ATOM   7827 C  CA  . GLN D  1 170 ? 0.218   13.380  -54.518 1.00 14.11 ? 170 GLN D CA  1 
ATOM   7828 C  C   . GLN D  1 170 ? -0.677  12.654  -53.465 1.00 14.98 ? 170 GLN D C   1 
ATOM   7829 O  O   . GLN D  1 170 ? -0.213  12.213  -52.362 1.00 14.87 ? 170 GLN D O   1 
ATOM   7830 C  CB  . GLN D  1 170 ? 0.744   12.463  -55.588 1.00 13.92 ? 170 GLN D CB  1 
ATOM   7831 C  CG  . GLN D  1 170 ? 1.425   13.303  -56.728 1.00 15.01 ? 170 GLN D CG  1 
ATOM   7832 C  CD  . GLN D  1 170 ? 1.760   12.398  -57.887 1.00 19.36 ? 170 GLN D CD  1 
ATOM   7833 O  OE1 . GLN D  1 170 ? 1.987   11.210  -57.732 1.00 17.18 ? 170 GLN D OE1 1 
ATOM   7834 N  NE2 . GLN D  1 170 ? 1.655   12.925  -59.125 1.00 21.56 ? 170 GLN D NE2 1 
ATOM   7835 N  N   . GLU D  1 171 ? -1.953  12.642  -53.790 1.00 16.12 ? 171 GLU D N   1 
ATOM   7836 C  CA  . GLU D  1 171 ? -3.018  12.143  -52.893 1.00 16.08 ? 171 GLU D CA  1 
ATOM   7837 C  C   . GLU D  1 171 ? -3.974  11.227  -53.669 1.00 16.94 ? 171 GLU D C   1 
ATOM   7838 O  O   . GLU D  1 171 ? -4.105  11.298  -54.932 1.00 18.08 ? 171 GLU D O   1 
ATOM   7839 C  CB  . GLU D  1 171 ? -3.868  13.279  -52.355 1.00 19.91 ? 171 GLU D CB  1 
ATOM   7840 C  CG  . GLU D  1 171 ? -3.138  14.267  -51.516 1.00 23.55 ? 171 GLU D CG  1 
ATOM   7841 C  CD  . GLU D  1 171 ? -4.077  15.394  -51.035 1.00 28.00 ? 171 GLU D CD  1 
ATOM   7842 O  OE1 . GLU D  1 171 ? -5.108  15.613  -51.672 1.00 35.85 ? 171 GLU D OE1 1 
ATOM   7843 O  OE2 . GLU D  1 171 ? -3.753  16.019  -50.018 1.00 31.94 ? 171 GLU D OE2 1 
ATOM   7844 N  N   . ALA D  1 172 ? -4.551  10.276  -52.975 1.00 14.12 ? 172 ALA D N   1 
ATOM   7845 C  CA  . ALA D  1 172 ? -5.517  9.334   -53.544 1.00 14.46 ? 172 ALA D CA  1 
ATOM   7846 C  C   . ALA D  1 172 ? -6.464  8.902   -52.466 1.00 13.78 ? 172 ALA D C   1 
ATOM   7847 O  O   . ALA D  1 172 ? -6.177  9.127   -51.289 1.00 17.52 ? 172 ALA D O   1 
ATOM   7848 C  CB  . ALA D  1 172 ? -4.817  8.149   -54.149 1.00 16.17 ? 172 ALA D CB  1 
ATOM   7849 N  N   . PHE D  1 173 ? -7.615  8.356   -52.820 1.00 13.00 ? 173 PHE D N   1 
ATOM   7850 C  CA  . PHE D  1 173 ? -8.603  7.949   -51.821 1.00 13.39 ? 173 PHE D CA  1 
ATOM   7851 C  C   . PHE D  1 173 ? -8.658  6.459   -51.804 1.00 14.90 ? 173 PHE D C   1 
ATOM   7852 O  O   . PHE D  1 173 ? -8.654  5.797   -52.866 1.00 16.12 ? 173 PHE D O   1 
ATOM   7853 C  CB  . PHE D  1 173 ? -9.999  8.495   -52.175 1.00 15.09 ? 173 PHE D CB  1 
ATOM   7854 C  CG  . PHE D  1 173 ? -10.220 9.919   -51.699 1.00 16.95 ? 173 PHE D CG  1 
ATOM   7855 C  CD1 . PHE D  1 173 ? -10.198 10.230  -50.294 1.00 21.35 ? 173 PHE D CD1 1 
ATOM   7856 C  CD2 . PHE D  1 173 ? -10.573 10.939  -52.600 1.00 24.69 ? 173 PHE D CD2 1 
ATOM   7857 C  CE1 . PHE D  1 173 ? -10.440 11.542  -49.815 1.00 22.06 ? 173 PHE D CE1 1 
ATOM   7858 C  CE2 . PHE D  1 173 ? -10.805 12.253  -52.093 1.00 22.03 ? 173 PHE D CE2 1 
ATOM   7859 C  CZ  . PHE D  1 173 ? -10.720 12.551  -50.722 1.00 23.50 ? 173 PHE D CZ  1 
ATOM   7860 N  N   . VAL D  1 174 ? -8.691  5.960   -50.602 1.00 12.78 ? 174 VAL D N   1 
ATOM   7861 C  CA  . VAL D  1 174 ? -8.766  4.552   -50.339 1.00 12.84 ? 174 VAL D CA  1 
ATOM   7862 C  C   . VAL D  1 174 ? -10.108 4.266   -49.654 1.00 13.33 ? 174 VAL D C   1 
ATOM   7863 O  O   . VAL D  1 174 ? -10.423 4.856   -48.610 1.00 13.80 ? 174 VAL D O   1 
ATOM   7864 C  CB  . VAL D  1 174 ? -7.627  4.136   -49.373 1.00 12.36 ? 174 VAL D CB  1 
ATOM   7865 C  CG1 . VAL D  1 174 ? -7.723  2.663   -48.970 1.00 12.38 ? 174 VAL D CG1 1 
ATOM   7866 C  CG2 . VAL D  1 174 ? -6.253  4.465   -50.035 1.00 14.61 ? 174 VAL D CG2 1 
ATOM   7867 N  N   . PRO D  1 175 ? -10.913 3.317   -50.198 1.00 11.86 ? 175 PRO D N   1 
ATOM   7868 C  CA  . PRO D  1 175 ? -12.133 2.971   -49.495 1.00 12.45 ? 175 PRO D CA  1 
ATOM   7869 C  C   . PRO D  1 175 ? -11.858 2.403   -48.120 1.00 12.58 ? 175 PRO D C   1 
ATOM   7870 O  O   . PRO D  1 175 ? -10.838 1.733   -47.854 1.00 12.61 ? 175 PRO D O   1 
ATOM   7871 C  CB  . PRO D  1 175 ? -12.759 1.859   -50.357 1.00 13.69 ? 175 PRO D CB  1 
ATOM   7872 C  CG  . PRO D  1 175 ? -12.225 2.120   -51.719 1.00 15.03 ? 175 PRO D CG  1 
ATOM   7873 C  CD  . PRO D  1 175 ? -10.778 2.628   -51.474 1.00 13.38 ? 175 PRO D CD  1 
ATOM   7874 N  N   . GLY D  1 176 ? -12.749 2.688   -47.167 1.00 12.47 ? 176 GLY D N   1 
ATOM   7875 C  CA  . GLY D  1 176 ? -12.567 2.112   -45.859 1.00 11.41 ? 176 GLY D CA  1 
ATOM   7876 C  C   . GLY D  1 176 ? -12.462 0.586   -45.828 1.00 12.03 ? 176 GLY D C   1 
ATOM   7877 O  O   . GLY D  1 176 ? -13.110 -0.109  -46.606 1.00 14.36 ? 176 GLY D O   1 
ATOM   7878 N  N   . PHE D  1 177 ? -11.711 0.090   -44.863 1.00 11.34 ? 177 PHE D N   1 
ATOM   7879 C  CA  . PHE D  1 177 ? -11.686 -1.354  -44.569 1.00 12.05 ? 177 PHE D CA  1 
ATOM   7880 C  C   . PHE D  1 177 ? -11.359 -1.531  -43.103 1.00 12.72 ? 177 PHE D C   1 
ATOM   7881 O  O   . PHE D  1 177 ? -11.184 -0.549  -42.370 1.00 12.85 ? 177 PHE D O   1 
ATOM   7882 C  CB  . PHE D  1 177 ? -10.679 -2.081  -45.475 1.00 12.93 ? 177 PHE D CB  1 
ATOM   7883 C  CG  . PHE D  1 177 ? -9.190  -1.684  -45.242 1.00 12.18 ? 177 PHE D CG  1 
ATOM   7884 C  CD1 . PHE D  1 177 ? -8.381  -2.543  -44.417 1.00 14.44 ? 177 PHE D CD1 1 
ATOM   7885 C  CD2 . PHE D  1 177 ? -8.680  -0.518  -45.808 1.00 13.71 ? 177 PHE D CD2 1 
ATOM   7886 C  CE1 . PHE D  1 177 ? -7.027  -2.210  -44.219 1.00 11.26 ? 177 PHE D CE1 1 
ATOM   7887 C  CE2 . PHE D  1 177 ? -7.325  -0.171  -45.588 1.00 12.89 ? 177 PHE D CE2 1 
ATOM   7888 C  CZ  . PHE D  1 177 ? -6.557  -1.044  -44.802 1.00 13.42 ? 177 PHE D CZ  1 
ATOM   7889 N  N   . ASN D  1 178 ? -11.360 -2.769  -42.594 1.00 13.59 ? 178 ASN D N   1 
ATOM   7890 C  CA  . ASN D  1 178 ? -11.190 -2.944  -41.187 1.00 14.26 ? 178 ASN D CA  1 
ATOM   7891 C  C   . ASN D  1 178 ? -9.683  -2.894  -40.923 1.00 12.42 ? 178 ASN D C   1 
ATOM   7892 O  O   . ASN D  1 178 ? -9.002  -3.888  -41.232 1.00 12.56 ? 178 ASN D O   1 
ATOM   7893 C  CB  . ASN D  1 178 ? -11.840 -4.316  -40.729 1.00 13.75 ? 178 ASN D CB  1 
ATOM   7894 C  CG  . ASN D  1 178 ? -11.657 -4.540  -39.302 1.00 13.63 ? 178 ASN D CG  1 
ATOM   7895 O  OD1 . ASN D  1 178 ? -11.238 -3.708  -38.525 1.00 13.58 ? 178 ASN D OD1 1 
ATOM   7896 N  ND2 . ASN D  1 178 ? -12.006 -5.806  -38.853 1.00 20.26 ? 178 ASN D ND2 1 
ATOM   7897 N  N   . ILE D  1 179 ? -9.236  -1.810  -40.297 1.00 11.49 ? 179 ILE D N   1 
ATOM   7898 C  CA  . ILE D  1 179 ? -7.828  -1.686  -39.972 1.00 10.90 ? 179 ILE D CA  1 
ATOM   7899 C  C   . ILE D  1 179 ? -7.339  -2.762  -39.039 1.00 12.24 ? 179 ILE D C   1 
ATOM   7900 O  O   . ILE D  1 179 ? -6.121  -3.014  -38.937 1.00 10.93 ? 179 ILE D O   1 
ATOM   7901 C  CB  . ILE D  1 179 ? -7.654  -0.238  -39.419 1.00 11.18 ? 179 ILE D CB  1 
ATOM   7902 C  CG1 . ILE D  1 179 ? -8.109  0.840   -40.387 1.00 11.88 ? 179 ILE D CG1 1 
ATOM   7903 C  CG2 . ILE D  1 179 ? -6.168  0.026   -39.029 1.00 10.23 ? 179 ILE D CG2 1 
ATOM   7904 C  CD1 . ILE D  1 179 ? -7.479  0.737   -41.786 1.00 13.64 ? 179 ILE D CD1 1 
ATOM   7905 N  N   . GLU D  1 180 ? -8.201  -3.408  -38.227 1.00 11.49 ? 180 GLU D N   1 
ATOM   7906 C  CA  . GLU D  1 180 ? -7.715  -4.482  -37.381 1.00 13.13 ? 180 GLU D CA  1 
ATOM   7907 C  C   . GLU D  1 180 ? -7.180  -5.670  -38.211 1.00 10.56 ? 180 GLU D C   1 
ATOM   7908 O  O   . GLU D  1 180 ? -6.390  -6.440  -37.636 1.00 12.55 ? 180 GLU D O   1 
ATOM   7909 C  CB  . GLU D  1 180 ? -8.851  -4.996  -36.447 1.00 15.98 ? 180 GLU D CB  1 
ATOM   7910 C  CG  . GLU D  1 180 ? -8.370  -5.684  -35.192 1.00 22.93 ? 180 GLU D CG  1 
ATOM   7911 C  CD  . GLU D  1 180 ? -9.457  -5.792  -34.110 1.00 25.01 ? 180 GLU D CD  1 
ATOM   7912 O  OE1 . GLU D  1 180 ? -10.575 -5.210  -34.214 1.00 23.94 ? 180 GLU D OE1 1 
ATOM   7913 O  OE2 . GLU D  1 180 ? -9.071  -6.412  -33.130 1.00 28.55 ? 180 GLU D OE2 1 
ATOM   7914 N  N   . GLU D  1 181 ? -7.569  -5.748  -39.485 1.00 11.32 ? 181 GLU D N   1 
ATOM   7915 C  CA  . GLU D  1 181 ? -6.977  -6.784  -40.358 1.00 11.18 ? 181 GLU D CA  1 
ATOM   7916 C  C   . GLU D  1 181 ? -5.488  -6.572  -40.581 1.00 11.58 ? 181 GLU D C   1 
ATOM   7917 O  O   . GLU D  1 181 ? -4.793  -7.502  -41.051 1.00 12.68 ? 181 GLU D O   1 
ATOM   7918 C  CB  . GLU D  1 181 ? -7.655  -6.767  -41.683 1.00 12.98 ? 181 GLU D CB  1 
ATOM   7919 C  CG  . GLU D  1 181 ? -9.105  -7.226  -41.673 1.00 13.47 ? 181 GLU D CG  1 
ATOM   7920 C  CD  . GLU D  1 181 ? -9.755  -7.041  -43.047 1.00 18.39 ? 181 GLU D CD  1 
ATOM   7921 O  OE1 . GLU D  1 181 ? -9.108  -6.741  -44.110 1.00 21.86 ? 181 GLU D OE1 1 
ATOM   7922 O  OE2 . GLU D  1 181 ? -11.051 -7.140  -43.141 1.00 19.73 ? 181 GLU D OE2 1 
ATOM   7923 N  N   . LEU D  1 182 ? -4.964  -5.400  -40.332 1.00 10.12 ? 182 LEU D N   1 
ATOM   7924 C  CA  . LEU D  1 182 ? -3.484  -5.162  -40.408 1.00 10.08 ? 182 LEU D CA  1 
ATOM   7925 C  C   . LEU D  1 182 ? -2.754  -5.607  -39.181 1.00 10.47 ? 182 LEU D C   1 
ATOM   7926 O  O   . LEU D  1 182 ? -1.524  -5.581  -39.210 1.00 10.21 ? 182 LEU D O   1 
ATOM   7927 C  CB  . LEU D  1 182 ? -3.248  -3.618  -40.620 1.00 9.57  ? 182 LEU D CB  1 
ATOM   7928 C  CG  . LEU D  1 182 ? -3.955  -3.017  -41.808 1.00 9.38  ? 182 LEU D CG  1 
ATOM   7929 C  CD1 . LEU D  1 182 ? -3.610  -1.516  -41.945 1.00 10.33 ? 182 LEU D CD1 1 
ATOM   7930 C  CD2 . LEU D  1 182 ? -3.666  -3.703  -43.102 1.00 9.43  ? 182 LEU D CD2 1 
ATOM   7931 N  N   . LEU D  1 183 ? -3.411  -5.910  -38.053 1.00 10.83 ? 183 LEU D N   1 
ATOM   7932 C  CA  . LEU D  1 183 ? -2.774  -6.347  -36.840 1.00 10.89 ? 183 LEU D CA  1 
ATOM   7933 C  C   . LEU D  1 183 ? -2.496  -7.813  -36.851 1.00 10.38 ? 183 LEU D C   1 
ATOM   7934 O  O   . LEU D  1 183 ? -3.183  -8.569  -37.540 1.00 11.57 ? 183 LEU D O   1 
ATOM   7935 C  CB  . LEU D  1 183 ? -3.731  -6.036  -35.658 1.00 12.19 ? 183 LEU D CB  1 
ATOM   7936 C  CG  . LEU D  1 183 ? -4.056  -4.511  -35.529 1.00 12.74 ? 183 LEU D CG  1 
ATOM   7937 C  CD1 . LEU D  1 183 ? -4.916  -4.197  -34.252 1.00 14.51 ? 183 LEU D CD1 1 
ATOM   7938 C  CD2 . LEU D  1 183 ? -2.841  -3.606  -35.484 1.00 14.51 ? 183 LEU D CD2 1 
ATOM   7939 N  N   . PRO D  1 184 ? -1.495  -8.214  -36.096 1.00 10.71 ? 184 PRO D N   1 
ATOM   7940 C  CA  . PRO D  1 184 ? -1.104  -9.639  -36.006 1.00 11.85 ? 184 PRO D CA  1 
ATOM   7941 C  C   . PRO D  1 184 ? -1.969  -10.449 -35.088 1.00 12.85 ? 184 PRO D C   1 
ATOM   7942 O  O   . PRO D  1 184 ? -2.853  -9.951  -34.397 1.00 14.08 ? 184 PRO D O   1 
ATOM   7943 C  CB  . PRO D  1 184 ? 0.355   -9.556  -35.466 1.00 11.73 ? 184 PRO D CB  1 
ATOM   7944 C  CG  . PRO D  1 184 ? 0.289   -8.342  -34.510 1.00 12.91 ? 184 PRO D CG  1 
ATOM   7945 C  CD  . PRO D  1 184 ? -0.587  -7.383  -35.282 1.00 10.72 ? 184 PRO D CD  1 
ATOM   7946 N  N   A GLU D  1 185 ? -1.695  -11.760 -35.102 0.50 13.29 ? 185 GLU D N   1 
ATOM   7947 N  N   B GLU D  1 185 ? -1.583  -11.730 -35.038 0.50 13.38 ? 185 GLU D N   1 
ATOM   7948 C  CA  A GLU D  1 185 ? -2.307  -12.625 -34.104 0.50 14.45 ? 185 GLU D CA  1 
ATOM   7949 C  CA  B GLU D  1 185 ? -2.105  -12.645 -34.052 0.50 14.82 ? 185 GLU D CA  1 
ATOM   7950 C  C   A GLU D  1 185 ? -1.839  -12.293 -32.698 0.50 13.37 ? 185 GLU D C   1 
ATOM   7951 C  C   B GLU D  1 185 ? -1.822  -12.211 -32.630 0.50 13.80 ? 185 GLU D C   1 
ATOM   7952 O  O   A GLU D  1 185 ? -0.661  -11.858 -32.486 0.50 12.80 ? 185 GLU D O   1 
ATOM   7953 O  O   B GLU D  1 185 ? -0.784  -11.595 -32.324 0.50 13.18 ? 185 GLU D O   1 
ATOM   7954 C  CB  A GLU D  1 185 ? -2.024  -14.099 -34.390 0.50 15.97 ? 185 GLU D CB  1 
ATOM   7955 C  CB  B GLU D  1 185 ? -1.569  -14.043 -34.335 0.50 17.08 ? 185 GLU D CB  1 
ATOM   7956 C  CG  A GLU D  1 185 ? -2.414  -14.499 -35.778 0.50 16.75 ? 185 GLU D CG  1 
ATOM   7957 C  CG  B GLU D  1 185 ? -2.140  -14.575 -35.636 0.50 18.44 ? 185 GLU D CG  1 
ATOM   7958 C  CD  A GLU D  1 185 ? -1.883  -15.871 -36.162 0.50 22.19 ? 185 GLU D CD  1 
ATOM   7959 C  CD  B GLU D  1 185 ? -3.651  -14.606 -35.654 0.50 24.16 ? 185 GLU D CD  1 
ATOM   7960 O  OE1 A GLU D  1 185 ? -1.376  -16.587 -35.283 0.50 24.65 ? 185 GLU D OE1 1 
ATOM   7961 O  OE1 B GLU D  1 185 ? -4.217  -15.404 -34.918 0.50 27.52 ? 185 GLU D OE1 1 
ATOM   7962 O  OE2 A GLU D  1 185 ? -1.973  -16.210 -37.379 0.50 25.38 ? 185 GLU D OE2 1 
ATOM   7963 O  OE2 B GLU D  1 185 ? -4.280  -13.839 -36.402 0.50 27.18 ? 185 GLU D OE2 1 
ATOM   7964 N  N   . ARG D  1 186 ? -2.759  -12.499 -31.738 1.00 13.13 ? 186 ARG D N   1 
ATOM   7965 C  CA  . ARG D  1 186 ? -2.441  -12.374 -30.295 1.00 14.32 ? 186 ARG D CA  1 
ATOM   7966 C  C   . ARG D  1 186 ? -1.956  -10.993 -29.911 1.00 13.32 ? 186 ARG D C   1 
ATOM   7967 O  O   . ARG D  1 186 ? -0.875  -10.789 -29.336 1.00 13.10 ? 186 ARG D O   1 
ATOM   7968 C  CB  . ARG D  1 186 ? -1.494  -13.498 -29.787 1.00 17.36 ? 186 ARG D CB  1 
ATOM   7969 C  CG  . ARG D  1 186 ? -2.174  -14.852 -30.036 1.00 23.23 ? 186 ARG D CG  1 
ATOM   7970 C  CD  . ARG D  1 186 ? -1.342  -16.046 -29.542 1.00 28.83 ? 186 ARG D CD  1 
ATOM   7971 N  NE  . ARG D  1 186 ? -0.196  -16.237 -30.410 1.00 30.93 ? 186 ARG D NE  1 
ATOM   7972 C  CZ  . ARG D  1 186 ? -0.258  -16.792 -31.644 1.00 34.32 ? 186 ARG D CZ  1 
ATOM   7973 N  NH1 . ARG D  1 186 ? -1.429  -17.240 -32.131 1.00 32.77 ? 186 ARG D NH1 1 
ATOM   7974 N  NH2 . ARG D  1 186 ? 0.841   -16.889 -32.397 1.00 34.79 ? 186 ARG D NH2 1 
ATOM   7975 N  N   . THR D  1 187 ? -2.795  -10.048 -30.273 1.00 11.45 ? 187 THR D N   1 
ATOM   7976 C  CA  . THR D  1 187 ? -2.440  -8.672  -29.911 1.00 12.06 ? 187 THR D CA  1 
ATOM   7977 C  C   . THR D  1 187 ? -2.313  -8.365  -28.427 1.00 13.11 ? 187 THR D C   1 
ATOM   7978 O  O   . THR D  1 187 ? -1.713  -7.367  -28.047 1.00 13.16 ? 187 THR D O   1 
ATOM   7979 C  CB  . THR D  1 187 ? -3.428  -7.664  -30.510 1.00 12.09 ? 187 THR D CB  1 
ATOM   7980 O  OG1 . THR D  1 187 ? -4.774  -8.021  -30.136 1.00 14.65 ? 187 THR D OG1 1 
ATOM   7981 C  CG2 . THR D  1 187 ? -3.379  -7.663  -32.073 1.00 13.51 ? 187 THR D CG2 1 
ATOM   7982 N  N   . ALA D  1 188 ? -2.785  -9.279  -27.541 1.00 11.69 ? 188 ALA D N   1 
ATOM   7983 C  CA  . ALA D  1 188 ? -2.563  -9.024  -26.132 1.00 12.10 ? 188 ALA D CA  1 
ATOM   7984 C  C   . ALA D  1 188 ? -1.067  -9.157  -25.741 1.00 11.82 ? 188 ALA D C   1 
ATOM   7985 O  O   . ALA D  1 188 ? -0.693  -8.843  -24.645 1.00 11.75 ? 188 ALA D O   1 
ATOM   7986 C  CB  . ALA D  1 188 ? -3.387  -10.070 -25.326 1.00 13.41 ? 188 ALA D CB  1 
ATOM   7987 N  N   . GLU D  1 189 ? -0.282  -9.784  -26.624 1.00 11.75 ? 189 GLU D N   1 
ATOM   7988 C  CA  . GLU D  1 189 ? 1.147   -9.976  -26.387 1.00 10.94 ? 189 GLU D CA  1 
ATOM   7989 C  C   . GLU D  1 189 ? 1.933   -8.858  -27.163 1.00 9.44  ? 189 GLU D C   1 
ATOM   7990 O  O   . GLU D  1 189 ? 1.940   -8.777  -28.404 1.00 9.70  ? 189 GLU D O   1 
ATOM   7991 C  CB  . GLU D  1 189 ? 1.570   -11.289 -26.976 1.00 11.70 ? 189 GLU D CB  1 
ATOM   7992 C  CG  . GLU D  1 189 ? 0.888   -12.412 -26.153 1.00 14.60 ? 189 GLU D CG  1 
ATOM   7993 C  CD  . GLU D  1 189 ? 1.208   -13.793 -26.742 1.00 18.58 ? 189 GLU D CD  1 
ATOM   7994 O  OE1 . GLU D  1 189 ? 2.313   -14.056 -27.178 1.00 19.42 ? 189 GLU D OE1 1 
ATOM   7995 O  OE2 . GLU D  1 189 ? 0.322   -14.721 -26.650 1.00 26.12 ? 189 GLU D OE2 1 
ATOM   7996 N  N   . TYR D  1 190 ? 2.568   -8.061  -26.346 1.00 8.79  ? 190 TYR D N   1 
ATOM   7997 C  CA  . TYR D  1 190 ? 3.285   -6.866  -26.885 1.00 8.77  ? 190 TYR D CA  1 
ATOM   7998 C  C   . TYR D  1 190 ? 4.364   -6.425  -26.012 1.00 9.38  ? 190 TYR D C   1 
ATOM   7999 O  O   . TYR D  1 190 ? 4.447   -6.763  -24.800 1.00 9.92  ? 190 TYR D O   1 
ATOM   8000 C  CB  . TYR D  1 190 ? 2.262   -5.706  -27.153 1.00 10.20 ? 190 TYR D CB  1 
ATOM   8001 C  CG  . TYR D  1 190 ? 1.465   -5.249  -25.936 1.00 9.33  ? 190 TYR D CG  1 
ATOM   8002 C  CD1 . TYR D  1 190 ? 2.009   -4.360  -25.017 1.00 9.84  ? 190 TYR D CD1 1 
ATOM   8003 C  CD2 . TYR D  1 190 ? 0.159   -5.685  -25.727 1.00 9.52  ? 190 TYR D CD2 1 
ATOM   8004 C  CE1 . TYR D  1 190 ? 1.286   -3.928  -23.918 1.00 10.42 ? 190 TYR D CE1 1 
ATOM   8005 C  CE2 . TYR D  1 190 ? -0.578  -5.259  -24.631 1.00 10.57 ? 190 TYR D CE2 1 
ATOM   8006 C  CZ  . TYR D  1 190 ? -0.009  -4.379  -23.727 1.00 10.51 ? 190 TYR D CZ  1 
ATOM   8007 O  OH  . TYR D  1 190 ? -0.713  -3.937  -22.627 1.00 11.32 ? 190 TYR D OH  1 
ATOM   8008 N  N   . TYR D  1 191 ? 5.245   -5.589  -26.602 1.00 9.28  ? 191 TYR D N   1 
ATOM   8009 C  CA  . TYR D  1 191 ? 6.251   -4.828  -25.961 1.00 9.02  ? 191 TYR D CA  1 
ATOM   8010 C  C   . TYR D  1 191 ? 5.813   -3.372  -25.792 1.00 8.68  ? 191 TYR D C   1 
ATOM   8011 O  O   . TYR D  1 191 ? 5.128   -2.818  -26.678 1.00 9.54  ? 191 TYR D O   1 
ATOM   8012 C  CB  . TYR D  1 191 ? 7.502   -4.750  -26.898 1.00 8.63  ? 191 TYR D CB  1 
ATOM   8013 C  CG  . TYR D  1 191 ? 8.085   -6.076  -27.355 1.00 8.93  ? 191 TYR D CG  1 
ATOM   8014 C  CD1 . TYR D  1 191 ? 9.094   -6.736  -26.651 1.00 9.80  ? 191 TYR D CD1 1 
ATOM   8015 C  CD2 . TYR D  1 191 ? 7.672   -6.587  -28.570 1.00 9.61  ? 191 TYR D CD2 1 
ATOM   8016 C  CE1 . TYR D  1 191 ? 9.633   -7.945  -27.107 1.00 10.69 ? 191 TYR D CE1 1 
ATOM   8017 C  CE2 . TYR D  1 191 ? 8.237   -7.783  -29.056 1.00 10.92 ? 191 TYR D CE2 1 
ATOM   8018 C  CZ  . TYR D  1 191 ? 9.225   -8.398  -28.307 1.00 10.31 ? 191 TYR D CZ  1 
ATOM   8019 O  OH  . TYR D  1 191 ? 9.770   -9.583  -28.815 1.00 13.56 ? 191 TYR D OH  1 
ATOM   8020 N  N   . ARG D  1 192 ? 6.129   -2.754  -24.655 1.00 9.32  ? 192 ARG D N   1 
ATOM   8021 C  CA  . ARG D  1 192 ? 5.696   -1.367  -24.363 1.00 8.93  ? 192 ARG D CA  1 
ATOM   8022 C  C   . ARG D  1 192 ? 6.897   -0.619  -23.811 1.00 8.11  ? 192 ARG D C   1 
ATOM   8023 O  O   . ARG D  1 192 ? 7.587   -1.078  -22.895 1.00 10.11 ? 192 ARG D O   1 
ATOM   8024 C  CB  . ARG D  1 192 ? 4.636   -1.473  -23.293 1.00 10.67 ? 192 ARG D CB  1 
ATOM   8025 C  CG  . ARG D  1 192 ? 4.332   -0.203  -22.511 1.00 13.74 ? 192 ARG D CG  1 
ATOM   8026 C  CD  . ARG D  1 192 ? 3.597   0.806   -23.381 1.00 13.21 ? 192 ARG D CD  1 
ATOM   8027 N  NE  . ARG D  1 192 ? 2.469   0.228   -24.145 1.00 15.73 ? 192 ARG D NE  1 
ATOM   8028 C  CZ  . ARG D  1 192 ? 1.262   -0.054  -23.651 1.00 15.75 ? 192 ARG D CZ  1 
ATOM   8029 N  NH1 . ARG D  1 192 ? 1.021   0.131   -22.359 1.00 18.49 ? 192 ARG D NH1 1 
ATOM   8030 N  NH2 . ARG D  1 192 ? 0.320   -0.570  -24.430 1.00 15.98 ? 192 ARG D NH2 1 
ATOM   8031 N  N   . TYR D  1 193 ? 7.155   0.566   -24.365 1.00 8.50  ? 193 TYR D N   1 
ATOM   8032 C  CA  . TYR D  1 193 ? 8.177   1.389   -23.752 1.00 8.81  ? 193 TYR D CA  1 
ATOM   8033 C  C   . TYR D  1 193 ? 7.940   2.871   -24.103 1.00 8.77  ? 193 TYR D C   1 
ATOM   8034 O  O   . TYR D  1 193 ? 7.121   3.198   -24.973 1.00 9.27  ? 193 TYR D O   1 
ATOM   8035 C  CB  . TYR D  1 193 ? 9.584   0.947   -24.261 1.00 8.89  ? 193 TYR D CB  1 
ATOM   8036 C  CG  . TYR D  1 193 ? 9.920   1.328   -25.719 1.00 7.95  ? 193 TYR D CG  1 
ATOM   8037 C  CD1 . TYR D  1 193 ? 10.710  2.442   -25.965 1.00 8.79  ? 193 TYR D CD1 1 
ATOM   8038 C  CD2 . TYR D  1 193 ? 9.461   0.568   -26.796 1.00 8.36  ? 193 TYR D CD2 1 
ATOM   8039 C  CE1 . TYR D  1 193 ? 10.993  2.873   -27.275 1.00 8.45  ? 193 TYR D CE1 1 
ATOM   8040 C  CE2 . TYR D  1 193 ? 9.725   0.972   -28.085 1.00 8.70  ? 193 TYR D CE2 1 
ATOM   8041 C  CZ  . TYR D  1 193 ? 10.485  2.121   -28.292 1.00 8.67  ? 193 TYR D CZ  1 
ATOM   8042 O  OH  . TYR D  1 193 ? 10.818  2.544   -29.588 1.00 9.09  ? 193 TYR D OH  1 
ATOM   8043 N  N   . ARG D  1 194 ? 8.671   3.715   -23.443 1.00 9.53  ? 194 ARG D N   1 
ATOM   8044 C  CA  . ARG D  1 194 ? 8.572   5.221   -23.638 1.00 9.82  ? 194 ARG D CA  1 
ATOM   8045 C  C   . ARG D  1 194 ? 9.637   5.664   -24.561 1.00 8.84  ? 194 ARG D C   1 
ATOM   8046 O  O   . ARG D  1 194 ? 10.838  5.373   -24.424 1.00 10.45 ? 194 ARG D O   1 
ATOM   8047 C  CB  . ARG D  1 194 ? 8.819   5.908   -22.309 1.00 13.42 ? 194 ARG D CB  1 
ATOM   8048 C  CG  . ARG D  1 194 ? 7.810   5.551   -21.261 1.00 17.50 ? 194 ARG D CG  1 
ATOM   8049 C  CD  . ARG D  1 194 ? 6.658   6.441   -21.475 1.00 21.91 ? 194 ARG D CD  1 
ATOM   8050 N  NE  . ARG D  1 194 ? 5.628   6.094   -20.522 1.00 31.18 ? 194 ARG D NE  1 
ATOM   8051 C  CZ  . ARG D  1 194 ? 4.536   6.825   -20.381 1.00 33.82 ? 194 ARG D CZ  1 
ATOM   8052 N  NH1 . ARG D  1 194 ? 4.422   7.931   -21.124 1.00 31.43 ? 194 ARG D NH1 1 
ATOM   8053 N  NH2 . ARG D  1 194 ? 3.592   6.431   -19.518 1.00 34.73 ? 194 ARG D NH2 1 
ATOM   8054 N  N   . GLY D  1 195 ? 9.199   6.275   -25.656 1.00 7.95  ? 195 GLY D N   1 
ATOM   8055 C  CA  . GLY D  1 195 ? 10.139  6.757   -26.672 1.00 8.21  ? 195 GLY D CA  1 
ATOM   8056 C  C   . GLY D  1 195 ? 9.684   7.975   -27.384 1.00 9.09  ? 195 GLY D C   1 
ATOM   8057 O  O   . GLY D  1 195 ? 9.120   8.911   -26.865 1.00 9.47  ? 195 GLY D O   1 
ATOM   8058 N  N   . SER D  1 196 ? 10.074  8.000   -28.662 1.00 7.85  ? 196 SER D N   1 
ATOM   8059 C  CA  . SER D  1 196 ? 9.986   9.238   -29.431 1.00 8.48  ? 196 SER D CA  1 
ATOM   8060 C  C   . SER D  1 196 ? 9.374   8.981   -30.824 1.00 7.93  ? 196 SER D C   1 
ATOM   8061 O  O   . SER D  1 196 ? 9.270   7.798   -31.319 1.00 7.91  ? 196 SER D O   1 
ATOM   8062 C  CB  . SER D  1 196 ? 11.379  9.863   -29.636 1.00 9.15  ? 196 SER D CB  1 
ATOM   8063 O  OG  . SER D  1 196 ? 12.150  9.141   -30.629 1.00 8.89  ? 196 SER D OG  1 
ATOM   8064 N  N   A LEU D  1 197 ? 9.084   10.059  -31.538 0.50 8.70  ? 197 LEU D N   1 
ATOM   8065 N  N   B LEU D  1 197 ? 9.098   10.062  -31.538 0.50 8.02  ? 197 LEU D N   1 
ATOM   8066 C  CA  A LEU D  1 197 ? 8.897   9.914   -32.986 0.50 8.69  ? 197 LEU D CA  1 
ATOM   8067 C  CA  B LEU D  1 197 ? 8.920   9.935   -32.989 0.50 7.63  ? 197 LEU D CA  1 
ATOM   8068 C  C   A LEU D  1 197 ? 10.207  9.439   -33.596 0.50 8.00  ? 197 LEU D C   1 
ATOM   8069 C  C   B LEU D  1 197 ? 10.219  9.438   -33.596 0.50 7.37  ? 197 LEU D C   1 
ATOM   8070 O  O   A LEU D  1 197 ? 11.306  9.835   -33.172 0.50 8.98  ? 197 LEU D O   1 
ATOM   8071 O  O   B LEU D  1 197 ? 11.328  9.820   -33.174 0.50 8.14  ? 197 LEU D O   1 
ATOM   8072 C  CB  A LEU D  1 197 ? 8.594   11.301  -33.615 0.50 9.71  ? 197 LEU D CB  1 
ATOM   8073 C  CB  B LEU D  1 197 ? 8.675   11.349  -33.603 0.50 7.52  ? 197 LEU D CB  1 
ATOM   8074 C  CG  A LEU D  1 197 ? 7.178   11.878  -33.505 0.50 11.47 ? 197 LEU D CG  1 
ATOM   8075 C  CG  B LEU D  1 197 ? 7.360   12.041  -33.227 0.50 8.11  ? 197 LEU D CG  1 
ATOM   8076 C  CD1 A LEU D  1 197 ? 6.818   12.241  -32.070 0.50 13.32 ? 197 LEU D CD1 1 
ATOM   8077 C  CD1 B LEU D  1 197 ? 7.200   13.429  -33.852 0.50 9.46  ? 197 LEU D CD1 1 
ATOM   8078 C  CD2 A LEU D  1 197 ? 7.184   13.118  -34.418 0.50 13.74 ? 197 LEU D CD2 1 
ATOM   8079 C  CD2 B LEU D  1 197 ? 6.199   11.172  -33.696 0.50 7.73  ? 197 LEU D CD2 1 
ATOM   8080 N  N   . THR D  1 198 ? 10.111  8.563   -34.589 1.00 7.96  ? 198 THR D N   1 
ATOM   8081 C  CA  . THR D  1 198 ? 11.336  8.096   -35.269 1.00 8.45  ? 198 THR D CA  1 
ATOM   8082 C  C   . THR D  1 198 ? 11.770  8.939   -36.441 1.00 7.81  ? 198 THR D C   1 
ATOM   8083 O  O   . THR D  1 198 ? 12.759  8.604   -37.119 1.00 8.63  ? 198 THR D O   1 
ATOM   8084 C  CB  . THR D  1 198 ? 11.202  6.643   -35.741 1.00 7.12  ? 198 THR D CB  1 
ATOM   8085 O  OG1 . THR D  1 198 ? 10.228  6.646   -36.775 1.00 7.30  ? 198 THR D OG1 1 
ATOM   8086 C  CG2 . THR D  1 198 ? 10.746  5.720   -34.642 1.00 9.08  ? 198 THR D CG2 1 
ATOM   8087 N  N   . THR D  1 199 ? 11.051  10.025  -36.664 1.00 8.68  ? 199 THR D N   1 
ATOM   8088 C  CA  . THR D  1 199 ? 11.418  11.013  -37.687 1.00 8.70  ? 199 THR D CA  1 
ATOM   8089 C  C   . THR D  1 199 ? 11.533  12.343  -37.021 1.00 8.95  ? 199 THR D C   1 
ATOM   8090 O  O   . THR D  1 199 ? 10.838  12.552  -36.010 1.00 9.16  ? 199 THR D O   1 
ATOM   8091 C  CB  . THR D  1 199 ? 10.307  11.102  -38.769 1.00 9.71  ? 199 THR D CB  1 
ATOM   8092 O  OG1 . THR D  1 199 ? 9.041   11.440  -38.193 1.00 13.87 ? 199 THR D OG1 1 
ATOM   8093 C  CG2 . THR D  1 199 ? 10.120  9.757   -39.485 1.00 10.64 ? 199 THR D CG2 1 
ATOM   8094 N  N   . PRO D  1 200 ? 12.243  13.299  -37.652 1.00 8.17  ? 200 PRO D N   1 
ATOM   8095 C  CA  . PRO D  1 200 ? 12.143  14.645  -37.155 1.00 8.76  ? 200 PRO D CA  1 
ATOM   8096 C  C   . PRO D  1 200 ? 10.695  15.076  -36.973 1.00 9.89  ? 200 PRO D C   1 
ATOM   8097 O  O   . PRO D  1 200 ? 9.889   14.773  -37.822 1.00 10.83 ? 200 PRO D O   1 
ATOM   8098 C  CB  . PRO D  1 200 ? 12.799  15.429  -38.309 1.00 8.23  ? 200 PRO D CB  1 
ATOM   8099 C  CG  . PRO D  1 200 ? 13.907  14.478  -38.783 1.00 8.20  ? 200 PRO D CG  1 
ATOM   8100 C  CD  . PRO D  1 200 ? 13.131  13.153  -38.830 1.00 7.84  ? 200 PRO D CD  1 
ATOM   8101 N  N   . PRO D  1 201 ? 10.389  15.865  -35.937 1.00 9.10  ? 201 PRO D N   1 
ATOM   8102 C  CA  . PRO D  1 201 ? 11.310  16.419  -34.963 1.00 9.03  ? 201 PRO D CA  1 
ATOM   8103 C  C   . PRO D  1 201 ? 11.712  15.538  -33.851 1.00 9.19  ? 201 PRO D C   1 
ATOM   8104 O  O   . PRO D  1 201 ? 12.372  15.990  -32.885 1.00 9.20  ? 201 PRO D O   1 
ATOM   8105 C  CB  . PRO D  1 201 ? 10.543  17.666  -34.402 1.00 9.61  ? 201 PRO D CB  1 
ATOM   8106 C  CG  . PRO D  1 201 ? 9.343   17.782  -35.194 1.00 13.83 ? 201 PRO D CG  1 
ATOM   8107 C  CD  . PRO D  1 201 ? 9.045   16.449  -35.804 1.00 11.13 ? 201 PRO D CD  1 
ATOM   8108 N  N   . CYS D  1 202 ? 11.353  14.238  -33.889 1.00 9.15  ? 202 CYS D N   1 
ATOM   8109 C  CA  . CYS D  1 202 ? 11.896  13.255  -32.902 1.00 9.54  ? 202 CYS D CA  1 
ATOM   8110 C  C   . CYS D  1 202 ? 11.430  13.506  -31.424 1.00 9.20  ? 202 CYS D C   1 
ATOM   8111 O  O   . CYS D  1 202 ? 12.106  13.121  -30.487 1.00 9.49  ? 202 CYS D O   1 
ATOM   8112 C  CB  . CYS D  1 202 ? 13.440  13.095  -32.856 1.00 8.49  ? 202 CYS D CB  1 
ATOM   8113 S  SG  . CYS D  1 202 ? 14.204  12.795  -34.485 1.00 9.07  ? 202 CYS D SG  1 
ATOM   8114 N  N   . ASN D  1 203 ? 10.264  14.086  -31.314 1.00 10.08 ? 203 ASN D N   1 
ATOM   8115 C  CA  . ASN D  1 203 ? 9.850   14.480  -29.954 1.00 10.16 ? 203 ASN D CA  1 
ATOM   8116 C  C   . ASN D  1 203 ? 9.690   13.282  -29.107 1.00 10.37 ? 203 ASN D C   1 
ATOM   8117 O  O   . ASN D  1 203 ? 9.134   12.258  -29.537 1.00 9.48  ? 203 ASN D O   1 
ATOM   8118 C  CB  . ASN D  1 203 ? 8.518   15.208  -30.024 1.00 10.82 ? 203 ASN D CB  1 
ATOM   8119 C  CG  . ASN D  1 203 ? 8.611   16.382  -31.000 1.00 13.04 ? 203 ASN D CG  1 
ATOM   8120 O  OD1 . ASN D  1 203 ? 8.485   16.228  -32.207 1.00 17.11 ? 203 ASN D OD1 1 
ATOM   8121 N  ND2 . ASN D  1 203 ? 8.919   17.484  -30.491 1.00 18.31 ? 203 ASN D ND2 1 
ATOM   8122 N  N   . PRO D  1 204 ? 10.128  13.334  -27.842 1.00 9.25  ? 204 PRO D N   1 
ATOM   8123 C  CA  . PRO D  1 204 ? 10.076  12.117  -26.960 1.00 10.18 ? 204 PRO D CA  1 
ATOM   8124 C  C   . PRO D  1 204 ? 8.698   11.996  -26.221 1.00 10.13 ? 204 PRO D C   1 
ATOM   8125 O  O   . PRO D  1 204 ? 8.620   12.123  -24.932 1.00 11.22 ? 204 PRO D O   1 
ATOM   8126 C  CB  . PRO D  1 204 ? 11.243  12.325  -25.946 1.00 10.90 ? 204 PRO D CB  1 
ATOM   8127 C  CG  . PRO D  1 204 ? 11.286  13.842  -25.885 1.00 10.17 ? 204 PRO D CG  1 
ATOM   8128 C  CD  . PRO D  1 204 ? 11.058  14.367  -27.297 1.00 10.39 ? 204 PRO D CD  1 
ATOM   8129 N  N   . THR D  1 205 ? 7.662   11.873  -27.018 1.00 8.91  ? 205 THR D N   1 
ATOM   8130 C  CA  . THR D  1 205 ? 6.292   12.026  -26.574 1.00 9.35  ? 205 THR D CA  1 
ATOM   8131 C  C   . THR D  1 205 ? 5.473   10.803  -26.905 1.00 9.04  ? 205 THR D C   1 
ATOM   8132 O  O   . THR D  1 205 ? 4.242   10.893  -26.908 1.00 9.28  ? 205 THR D O   1 
ATOM   8133 C  CB  . THR D  1 205 ? 5.665   13.258  -27.224 1.00 9.93  ? 205 THR D CB  1 
ATOM   8134 O  OG1 . THR D  1 205 ? 5.831   13.130  -28.649 1.00 10.44 ? 205 THR D OG1 1 
ATOM   8135 C  CG2 . THR D  1 205 ? 6.312   14.618  -26.738 1.00 10.26 ? 205 THR D CG2 1 
ATOM   8136 N  N   . VAL D  1 206 ? 6.159   9.702   -27.294 1.00 8.44  ? 206 VAL D N   1 
ATOM   8137 C  CA  . VAL D  1 206 ? 5.417   8.535   -27.769 1.00 8.98  ? 206 VAL D CA  1 
ATOM   8138 C  C   . VAL D  1 206 ? 5.449   7.360   -26.752 1.00 8.70  ? 206 VAL D C   1 
ATOM   8139 O  O   . VAL D  1 206 ? 6.510   6.927   -26.390 1.00 9.63  ? 206 VAL D O   1 
ATOM   8140 C  CB  . VAL D  1 206 ? 5.999   8.029   -29.125 1.00 7.63  ? 206 VAL D CB  1 
ATOM   8141 C  CG1 . VAL D  1 206 ? 5.220   6.818   -29.611 1.00 9.10  ? 206 VAL D CG1 1 
ATOM   8142 C  CG2 . VAL D  1 206 ? 5.916   9.108   -30.187 1.00 9.71  ? 206 VAL D CG2 1 
ATOM   8143 N  N   . LEU D  1 207 ? 4.255   6.865   -26.512 1.00 8.37  ? 207 LEU D N   1 
ATOM   8144 C  CA  . LEU D  1 207 ? 4.154   5.584   -25.793 1.00 9.51  ? 207 LEU D CA  1 
ATOM   8145 C  C   . LEU D  1 207 ? 4.023   4.533   -26.926 1.00 8.32  ? 207 LEU D C   1 
ATOM   8146 O  O   . LEU D  1 207 ? 3.080   4.509   -27.694 1.00 9.27  ? 207 LEU D O   1 
ATOM   8147 C  CB  . LEU D  1 207 ? 2.868   5.596   -24.975 1.00 12.06 ? 207 LEU D CB  1 
ATOM   8148 C  CG  . LEU D  1 207 ? 2.746   4.362   -24.104 1.00 15.00 ? 207 LEU D CG  1 
ATOM   8149 C  CD1 . LEU D  1 207 ? 3.884   4.262   -23.094 1.00 15.75 ? 207 LEU D CD1 1 
ATOM   8150 C  CD2 . LEU D  1 207 ? 1.399   4.479   -23.426 1.00 21.52 ? 207 LEU D CD2 1 
ATOM   8151 N  N   . TRP D  1 208 ? 5.036   3.702   -26.951 1.00 7.66  ? 208 TRP D N   1 
ATOM   8152 C  CA  . TRP D  1 208 ? 5.133   2.679   -28.017 1.00 8.03  ? 208 TRP D CA  1 
ATOM   8153 C  C   . TRP D  1 208 ? 4.555   1.364   -27.579 1.00 8.05  ? 208 TRP D C   1 
ATOM   8154 O  O   . TRP D  1 208 ? 4.894   0.881   -26.461 1.00 9.76  ? 208 TRP D O   1 
ATOM   8155 C  CB  . TRP D  1 208 ? 6.620   2.430   -28.396 1.00 8.06  ? 208 TRP D CB  1 
ATOM   8156 C  CG  . TRP D  1 208 ? 7.182   3.468   -29.302 1.00 8.46  ? 208 TRP D CG  1 
ATOM   8157 C  CD1 . TRP D  1 208 ? 7.898   4.615   -28.971 1.00 9.13  ? 208 TRP D CD1 1 
ATOM   8158 C  CD2 . TRP D  1 208 ? 6.981   3.472   -30.738 1.00 8.10  ? 208 TRP D CD2 1 
ATOM   8159 N  NE1 . TRP D  1 208 ? 8.113   5.351   -30.153 1.00 8.38  ? 208 TRP D NE1 1 
ATOM   8160 C  CE2 . TRP D  1 208 ? 7.593   4.706   -31.232 1.00 7.87  ? 208 TRP D CE2 1 
ATOM   8161 C  CE3 . TRP D  1 208 ? 6.293   2.644   -31.661 1.00 8.88  ? 208 TRP D CE3 1 
ATOM   8162 C  CZ2 . TRP D  1 208 ? 7.549   5.069   -32.577 1.00 9.05  ? 208 TRP D CZ2 1 
ATOM   8163 C  CZ3 . TRP D  1 208 ? 6.294   3.024   -33.020 1.00 8.96  ? 208 TRP D CZ3 1 
ATOM   8164 C  CH2 . TRP D  1 208 ? 6.939   4.211   -33.466 1.00 9.89  ? 208 TRP D CH2 1 
ATOM   8165 N  N   . THR D  1 209 ? 3.804   0.742   -28.473 1.00 7.36  ? 209 THR D N   1 
ATOM   8166 C  CA  . THR D  1 209 ? 3.346   -0.682  -28.302 1.00 7.40  ? 209 THR D CA  1 
ATOM   8167 C  C   . THR D  1 209 ? 3.806   -1.395  -29.592 1.00 7.90  ? 209 THR D C   1 
ATOM   8168 O  O   . THR D  1 209 ? 3.344   -1.021  -30.695 1.00 8.86  ? 209 THR D O   1 
ATOM   8169 C  CB  . THR D  1 209 ? 1.836   -0.722  -28.214 1.00 8.79  ? 209 THR D CB  1 
ATOM   8170 O  OG1 . THR D  1 209 ? 1.433   0.065   -27.042 1.00 9.46  ? 209 THR D OG1 1 
ATOM   8171 C  CG2 . THR D  1 209 ? 1.319   -2.192  -27.972 1.00 9.20  ? 209 THR D CG2 1 
ATOM   8172 N  N   . VAL D  1 210 ? 4.712   -2.351  -29.433 1.00 7.46  ? 210 VAL D N   1 
ATOM   8173 C  CA  . VAL D  1 210 ? 5.158   -3.158  -30.574 1.00 7.56  ? 210 VAL D CA  1 
ATOM   8174 C  C   . VAL D  1 210 ? 4.561   -4.568  -30.403 1.00 8.08  ? 210 VAL D C   1 
ATOM   8175 O  O   . VAL D  1 210 ? 4.862   -5.196  -29.370 1.00 8.43  ? 210 VAL D O   1 
ATOM   8176 C  CB  . VAL D  1 210 ? 6.709   -3.198  -30.684 1.00 7.24  ? 210 VAL D CB  1 
ATOM   8177 C  CG1 . VAL D  1 210 ? 7.150   -4.019  -31.887 1.00 8.60  ? 210 VAL D CG1 1 
ATOM   8178 C  CG2 . VAL D  1 210 ? 7.298   -1.807  -30.701 1.00 8.69  ? 210 VAL D CG2 1 
ATOM   8179 N  N   . PHE D  1 211 ? 3.732   -5.043  -31.334 1.00 8.30  ? 211 PHE D N   1 
ATOM   8180 C  CA  . PHE D  1 211 ? 3.137   -6.376  -31.117 1.00 8.88  ? 211 PHE D CA  1 
ATOM   8181 C  C   . PHE D  1 211 ? 4.277   -7.394  -31.184 1.00 9.22  ? 211 PHE D C   1 
ATOM   8182 O  O   . PHE D  1 211 ? 5.235   -7.231  -31.939 1.00 9.86  ? 211 PHE D O   1 
ATOM   8183 C  CB  . PHE D  1 211 ? 2.005   -6.597  -32.075 1.00 9.38  ? 211 PHE D CB  1 
ATOM   8184 C  CG  . PHE D  1 211 ? 0.853   -5.663  -31.815 1.00 10.18 ? 211 PHE D CG  1 
ATOM   8185 C  CD1 . PHE D  1 211 ? 0.092   -5.801  -30.661 1.00 9.86  ? 211 PHE D CD1 1 
ATOM   8186 C  CD2 . PHE D  1 211 ? 0.557   -4.618  -32.675 1.00 11.16 ? 211 PHE D CD2 1 
ATOM   8187 C  CE1 . PHE D  1 211 ? -0.957  -4.933  -30.393 1.00 11.62 ? 211 PHE D CE1 1 
ATOM   8188 C  CE2 . PHE D  1 211 ? -0.493  -3.748  -32.410 1.00 10.89 ? 211 PHE D CE2 1 
ATOM   8189 C  CZ  . PHE D  1 211 ? -1.247  -3.909  -31.269 1.00 11.60 ? 211 PHE D CZ  1 
ATOM   8190 N  N   . ARG D  1 212 ? 4.078   -8.497  -30.402 1.00 9.66  ? 212 ARG D N   1 
ATOM   8191 C  CA  . ARG D  1 212 ? 5.101   -9.585  -30.341 1.00 10.06 ? 212 ARG D CA  1 
ATOM   8192 C  C   . ARG D  1 212 ? 5.150   -10.292 -31.678 1.00 10.15 ? 212 ARG D C   1 
ATOM   8193 O  O   . ARG D  1 212 ? 6.252   -10.654 -32.165 1.00 11.22 ? 212 ARG D O   1 
ATOM   8194 C  CB  . ARG D  1 212 ? 4.711   -10.564 -29.230 1.00 10.80 ? 212 ARG D CB  1 
ATOM   8195 C  CG  . ARG D  1 212 ? 5.783   -11.678 -29.152 1.00 11.39 ? 212 ARG D CG  1 
ATOM   8196 C  CD  . ARG D  1 212 ? 5.247   -12.735 -28.155 1.00 14.09 ? 212 ARG D CD  1 
ATOM   8197 N  NE  . ARG D  1 212 ? 6.346   -13.677 -27.809 1.00 16.37 ? 212 ARG D NE  1 
ATOM   8198 C  CZ  . ARG D  1 212 ? 6.172   -14.650 -26.910 1.00 18.95 ? 212 ARG D CZ  1 
ATOM   8199 N  NH1 . ARG D  1 212 ? 4.998   -14.860 -26.371 1.00 19.76 ? 212 ARG D NH1 1 
ATOM   8200 N  NH2 . ARG D  1 212 ? 7.218   -15.419 -26.595 1.00 24.48 ? 212 ARG D NH2 1 
ATOM   8201 N  N   . ASN D  1 213 ? 4.032   -10.519 -32.324 1.00 10.31 ? 213 ASN D N   1 
ATOM   8202 C  CA  . ASN D  1 213 ? 4.020   -11.389 -33.515 1.00 11.53 ? 213 ASN D CA  1 
ATOM   8203 C  C   . ASN D  1 213 ? 4.027   -10.468 -34.757 1.00 11.21 ? 213 ASN D C   1 
ATOM   8204 O  O   . ASN D  1 213 ? 3.285   -9.477  -34.812 1.00 10.33 ? 213 ASN D O   1 
ATOM   8205 C  CB  . ASN D  1 213 ? 2.733   -12.227 -33.493 1.00 13.59 ? 213 ASN D CB  1 
ATOM   8206 C  CG  . ASN D  1 213 ? 2.733   -13.235 -32.355 1.00 16.36 ? 213 ASN D CG  1 
ATOM   8207 O  OD1 . ASN D  1 213 ? 1.803   -13.240 -31.508 1.00 20.71 ? 213 ASN D OD1 1 
ATOM   8208 N  ND2 . ASN D  1 213 ? 3.803   -13.955 -32.253 1.00 18.58 ? 213 ASN D ND2 1 
ATOM   8209 N  N   . PRO D  1 214 ? 4.732   -10.828 -35.797 1.00 10.42 ? 214 PRO D N   1 
ATOM   8210 C  CA  . PRO D  1 214 ? 4.692   -10.111 -37.061 1.00 10.53 ? 214 PRO D CA  1 
ATOM   8211 C  C   . PRO D  1 214 ? 3.500   -10.530 -37.905 1.00 9.62  ? 214 PRO D C   1 
ATOM   8212 O  O   . PRO D  1 214 ? 2.861   -11.556 -37.634 1.00 11.38 ? 214 PRO D O   1 
ATOM   8213 C  CB  . PRO D  1 214 ? 6.006   -10.560 -37.761 1.00 10.43 ? 214 PRO D CB  1 
ATOM   8214 C  CG  . PRO D  1 214 ? 6.074   -12.027 -37.367 1.00 12.58 ? 214 PRO D CG  1 
ATOM   8215 C  CD  . PRO D  1 214 ? 5.757   -11.935 -35.818 1.00 11.92 ? 214 PRO D CD  1 
ATOM   8216 N  N   . VAL D  1 215 ? 3.205   -9.757  -38.949 1.00 9.21  ? 215 VAL D N   1 
ATOM   8217 C  CA  . VAL D  1 215 ? 2.306   -10.197 -40.041 1.00 8.98  ? 215 VAL D CA  1 
ATOM   8218 C  C   . VAL D  1 215 ? 3.207   -10.465 -41.248 1.00 8.71  ? 215 VAL D C   1 
ATOM   8219 O  O   . VAL D  1 215 ? 4.456   -10.164 -41.168 1.00 9.48  ? 215 VAL D O   1 
ATOM   8220 C  CB  . VAL D  1 215 ? 1.277   -9.093  -40.426 1.00 8.61  ? 215 VAL D CB  1 
ATOM   8221 C  CG1 . VAL D  1 215 ? 0.414   -8.779  -39.217 1.00 10.45 ? 215 VAL D CG1 1 
ATOM   8222 C  CG2 . VAL D  1 215 ? 1.967   -7.805  -41.019 1.00 10.31 ? 215 VAL D CG2 1 
ATOM   8223 N  N   . GLN D  1 216 ? 2.658   -11.063 -42.284 1.00 8.12  ? 216 GLN D N   1 
ATOM   8224 C  CA  . GLN D  1 216 ? 3.414   -11.347 -43.503 1.00 8.23  ? 216 GLN D CA  1 
ATOM   8225 C  C   . GLN D  1 216 ? 2.824   -10.530 -44.647 1.00 8.69  ? 216 GLN D C   1 
ATOM   8226 O  O   . GLN D  1 216 ? 1.561   -10.412 -44.752 1.00 9.50  ? 216 GLN D O   1 
ATOM   8227 C  CB  . GLN D  1 216 ? 3.293   -12.839 -43.902 1.00 10.44 ? 216 GLN D CB  1 
ATOM   8228 C  CG  . GLN D  1 216 ? 4.090   -13.700 -42.946 1.00 10.54 ? 216 GLN D CG  1 
ATOM   8229 C  CD  . GLN D  1 216 ? 4.048   -15.162 -43.343 1.00 12.51 ? 216 GLN D CD  1 
ATOM   8230 O  OE1 . GLN D  1 216 ? 3.549   -15.599 -44.348 1.00 11.26 ? 216 GLN D OE1 1 
ATOM   8231 N  NE2 . GLN D  1 216 ? 4.700   -15.942 -42.452 1.00 16.39 ? 216 GLN D NE2 1 
ATOM   8232 N  N   . ILE D  1 217 ? 3.624   -10.045 -45.559 1.00 8.13  ? 217 ILE D N   1 
ATOM   8233 C  CA  . ILE D  1 217 ? 3.167   -9.610  -46.910 1.00 8.14  ? 217 ILE D CA  1 
ATOM   8234 C  C   . ILE D  1 217 ? 4.151   -10.313 -47.906 1.00 8.13  ? 217 ILE D C   1 
ATOM   8235 O  O   . ILE D  1 217 ? 5.293   -10.696 -47.480 1.00 8.78  ? 217 ILE D O   1 
ATOM   8236 C  CB  . ILE D  1 217 ? 3.202   -8.053  -47.078 1.00 7.98  ? 217 ILE D CB  1 
ATOM   8237 C  CG1 . ILE D  1 217 ? 4.651   -7.542  -47.073 1.00 8.97  ? 217 ILE D CG1 1 
ATOM   8238 C  CG2 . ILE D  1 217 ? 2.376   -7.372  -45.970 1.00 9.57  ? 217 ILE D CG2 1 
ATOM   8239 C  CD1 . ILE D  1 217 ? 4.651   -5.956  -47.293 1.00 11.25 ? 217 ILE D CD1 1 
ATOM   8240 N  N   . SER D  1 218 ? 3.793   -10.387 -49.164 1.00 7.71  ? 218 SER D N   1 
ATOM   8241 C  CA  . SER D  1 218 ? 4.680   -11.113 -50.093 1.00 8.24  ? 218 SER D CA  1 
ATOM   8242 C  C   . SER D  1 218 ? 5.857   -10.333 -50.578 1.00 9.50  ? 218 SER D C   1 
ATOM   8243 O  O   . SER D  1 218 ? 5.904   -9.104  -50.510 1.00 10.14 ? 218 SER D O   1 
ATOM   8244 C  CB  . SER D  1 218 ? 3.860   -11.611 -51.268 1.00 9.31  ? 218 SER D CB  1 
ATOM   8245 O  OG  . SER D  1 218 ? 3.437   -10.547 -52.083 1.00 10.19 ? 218 SER D OG  1 
ATOM   8246 N  N   . GLN D  1 219 ? 6.809   -11.072 -51.134 1.00 9.11  ? 219 GLN D N   1 
ATOM   8247 C  CA  . GLN D  1 219 ? 7.916   -10.431 -51.846 1.00 10.39 ? 219 GLN D CA  1 
ATOM   8248 C  C   . GLN D  1 219 ? 7.415   -9.489  -52.922 1.00 10.56 ? 219 GLN D C   1 
ATOM   8249 O  O   . GLN D  1 219 ? 7.998   -8.395  -53.056 1.00 10.85 ? 219 GLN D O   1 
ATOM   8250 C  CB  . GLN D  1 219 ? 8.814   -11.510 -52.485 1.00 13.99 ? 219 GLN D CB  1 
ATOM   8251 C  CG  . GLN D  1 219 ? 10.166  -10.906 -52.980 1.00 17.46 ? 219 GLN D CG  1 
ATOM   8252 C  CD  . GLN D  1 219 ? 10.159  -10.259 -54.303 1.00 22.28 ? 219 GLN D CD  1 
ATOM   8253 O  OE1 . GLN D  1 219 ? 10.941  -9.247  -54.519 1.00 26.16 ? 219 GLN D OE1 1 
ATOM   8254 N  NE2 . GLN D  1 219 ? 9.278   -10.716 -55.162 1.00 22.92 ? 219 GLN D NE2 1 
ATOM   8255 N  N   . GLU D  1 220 ? 6.397   -9.833  -53.644 1.00 9.78  ? 220 GLU D N   1 
ATOM   8256 C  CA  . GLU D  1 220 ? 5.924   -8.933  -54.695 1.00 10.98 ? 220 GLU D CA  1 
ATOM   8257 C  C   . GLU D  1 220 ? 5.300   -7.664  -54.077 1.00 10.32 ? 220 GLU D C   1 
ATOM   8258 O  O   . GLU D  1 220 ? 5.500   -6.579  -54.639 1.00 11.17 ? 220 GLU D O   1 
ATOM   8259 C  CB  . GLU D  1 220 ? 4.870   -9.672  -55.552 1.00 10.81 ? 220 GLU D CB  1 
ATOM   8260 C  CG  . GLU D  1 220 ? 5.555   -10.769 -56.397 1.00 13.15 ? 220 GLU D CG  1 
ATOM   8261 C  CD  . GLU D  1 220 ? 5.788   -12.082 -55.666 1.00 18.03 ? 220 GLU D CD  1 
ATOM   8262 O  OE1 . GLU D  1 220 ? 5.339   -12.313 -54.512 1.00 17.89 ? 220 GLU D OE1 1 
ATOM   8263 O  OE2 . GLU D  1 220 ? 6.479   -12.953 -56.305 1.00 27.47 ? 220 GLU D OE2 1 
ATOM   8264 N  N   . GLN D  1 221 ? 4.579   -7.758  -52.925 1.00 8.81  ? 221 GLN D N   1 
ATOM   8265 C  CA  . GLN D  1 221 ? 4.049   -6.541  -52.285 1.00 9.19  ? 221 GLN D CA  1 
ATOM   8266 C  C   . GLN D  1 221 ? 5.171   -5.717  -51.732 1.00 9.20  ? 221 GLN D C   1 
ATOM   8267 O  O   . GLN D  1 221 ? 5.174   -4.477  -51.955 1.00 10.40 ? 221 GLN D O   1 
ATOM   8268 C  CB  . GLN D  1 221 ? 3.168   -6.953  -51.136 1.00 9.67  ? 221 GLN D CB  1 
ATOM   8269 C  CG  . GLN D  1 221 ? 1.852   -7.565  -51.672 1.00 9.36  ? 221 GLN D CG  1 
ATOM   8270 C  CD  . GLN D  1 221 ? 0.967   -7.989  -50.484 1.00 8.12  ? 221 GLN D CD  1 
ATOM   8271 O  OE1 . GLN D  1 221 ? 1.275   -8.932  -49.710 1.00 9.21  ? 221 GLN D OE1 1 
ATOM   8272 N  NE2 . GLN D  1 221 ? -0.203  -7.352  -50.338 1.00 9.50  ? 221 GLN D NE2 1 
ATOM   8273 N  N   . LEU D  1 222 ? 6.232   -6.337  -51.170 1.00 9.10  ? 222 LEU D N   1 
ATOM   8274 C  CA  . LEU D  1 222 ? 7.377   -5.572  -50.708 1.00 9.92  ? 222 LEU D CA  1 
ATOM   8275 C  C   . LEU D  1 222 ? 8.061   -4.865  -51.871 1.00 10.64 ? 222 LEU D C   1 
ATOM   8276 O  O   . LEU D  1 222 ? 8.486   -3.695  -51.740 1.00 10.00 ? 222 LEU D O   1 
ATOM   8277 C  CB  . LEU D  1 222 ? 8.378   -6.524  -50.025 1.00 9.71  ? 222 LEU D CB  1 
ATOM   8278 C  CG  . LEU D  1 222 ? 8.062   -6.699  -48.564 1.00 10.49 ? 222 LEU D CG  1 
ATOM   8279 C  CD1 . LEU D  1 222 ? 8.700   -7.961  -48.047 1.00 12.21 ? 222 LEU D CD1 1 
ATOM   8280 C  CD2 . LEU D  1 222 ? 8.444   -5.512  -47.636 1.00 12.00 ? 222 LEU D CD2 1 
ATOM   8281 N  N   . LEU D  1 223 ? 8.232   -5.544  -53.001 1.00 9.97  ? 223 LEU D N   1 
ATOM   8282 C  CA  . LEU D  1 223 ? 8.957   -4.944  -54.113 1.00 10.74 ? 223 LEU D CA  1 
ATOM   8283 C  C   . LEU D  1 223 ? 8.116   -3.758  -54.637 1.00 10.87 ? 223 LEU D C   1 
ATOM   8284 O  O   . LEU D  1 223 ? 8.704   -2.757  -55.062 1.00 11.04 ? 223 LEU D O   1 
ATOM   8285 C  CB  . LEU D  1 223 ? 9.176   -6.003  -55.247 1.00 11.02 ? 223 LEU D CB  1 
ATOM   8286 C  CG  . LEU D  1 223 ? 9.973   -5.480  -56.486 1.00 13.01 ? 223 LEU D CG  1 
ATOM   8287 C  CD1 . LEU D  1 223 ? 11.365  -4.999  -56.055 1.00 16.24 ? 223 LEU D CD1 1 
ATOM   8288 C  CD2 . LEU D  1 223 ? 10.032  -6.626  -57.522 1.00 13.99 ? 223 LEU D CD2 1 
ATOM   8289 N  N   . ALA D  1 224 ? 6.810   -3.900  -54.652 1.00 11.34 ? 224 ALA D N   1 
ATOM   8290 C  CA  . ALA D  1 224 ? 5.971   -2.768  -55.102 1.00 11.46 ? 224 ALA D CA  1 
ATOM   8291 C  C   . ALA D  1 224 ? 6.149   -1.573  -54.172 1.00 11.83 ? 224 ALA D C   1 
ATOM   8292 O  O   . ALA D  1 224 ? 6.396   -0.467  -54.607 1.00 12.98 ? 224 ALA D O   1 
ATOM   8293 C  CB  . ALA D  1 224 ? 4.510   -3.151  -55.196 1.00 11.85 ? 224 ALA D CB  1 
ATOM   8294 N  N   . LEU D  1 225 ? 6.110   -1.824  -52.853 1.00 9.49  ? 225 LEU D N   1 
ATOM   8295 C  CA  . LEU D  1 225 ? 6.320   -0.801  -51.805 1.00 10.99 ? 225 LEU D CA  1 
ATOM   8296 C  C   . LEU D  1 225 ? 7.673   -0.111  -52.022 1.00 11.77 ? 225 LEU D C   1 
ATOM   8297 O  O   . LEU D  1 225 ? 7.779   1.124   -51.958 1.00 13.39 ? 225 LEU D O   1 
ATOM   8298 C  CB  . LEU D  1 225 ? 6.084   -1.453  -50.470 1.00 11.57 ? 225 LEU D CB  1 
ATOM   8299 C  CG  . LEU D  1 225 ? 6.223   -0.405  -49.340 1.00 11.07 ? 225 LEU D CG  1 
ATOM   8300 C  CD1 . LEU D  1 225 ? 5.208   0.737   -49.411 1.00 11.82 ? 225 LEU D CD1 1 
ATOM   8301 C  CD2 . LEU D  1 225 ? 6.129   -1.091  -47.972 1.00 12.02 ? 225 LEU D CD2 1 
ATOM   8302 N  N   . GLU D  1 226 ? 8.701   -0.887  -52.288 1.00 10.30 ? 226 GLU D N   1 
ATOM   8303 C  CA  . GLU D  1 226 ? 10.070  -0.429  -52.377 1.00 11.53 ? 226 GLU D CA  1 
ATOM   8304 C  C   . GLU D  1 226 ? 10.384  0.263   -53.642 1.00 11.45 ? 226 GLU D C   1 
ATOM   8305 O  O   . GLU D  1 226 ? 11.445  0.901   -53.702 1.00 14.47 ? 226 GLU D O   1 
ATOM   8306 C  CB  . GLU D  1 226 ? 11.007  -1.708  -52.254 1.00 10.38 ? 226 GLU D CB  1 
ATOM   8307 C  CG  . GLU D  1 226 ? 11.028  -2.297  -50.846 1.00 9.38  ? 226 GLU D CG  1 
ATOM   8308 C  CD  . GLU D  1 226 ? 11.367  -3.731  -50.879 1.00 12.20 ? 226 GLU D CD  1 
ATOM   8309 O  OE1 . GLU D  1 226 ? 11.674  -4.356  -51.952 1.00 11.44 ? 226 GLU D OE1 1 
ATOM   8310 O  OE2 . GLU D  1 226 ? 11.427  -4.300  -49.826 1.00 12.48 ? 226 GLU D OE2 1 
ATOM   8311 N  N   . THR D  1 227 ? 9.576   0.149   -54.653 1.00 11.54 ? 227 THR D N   1 
ATOM   8312 C  CA  . THR D  1 227 ? 9.908   0.722   -55.998 1.00 11.72 ? 227 THR D CA  1 
ATOM   8313 C  C   . THR D  1 227 ? 8.865   1.715   -56.457 1.00 11.62 ? 227 THR D C   1 
ATOM   8314 O  O   . THR D  1 227 ? 9.153   2.418   -57.485 1.00 14.84 ? 227 THR D O   1 
ATOM   8315 C  CB  . THR D  1 227 ? 10.062  -0.381  -57.096 1.00 14.12 ? 227 THR D CB  1 
ATOM   8316 O  OG1 . THR D  1 227 ? 8.858   -1.118  -57.228 1.00 13.02 ? 227 THR D OG1 1 
ATOM   8317 C  CG2 . THR D  1 227 ? 11.221  -1.297  -56.778 1.00 15.07 ? 227 THR D CG2 1 
ATOM   8318 N  N   . ALA D  1 228 ? 7.745   1.882   -55.812 1.00 11.15 ? 228 ALA D N   1 
ATOM   8319 C  CA  . ALA D  1 228 ? 6.655   2.717   -56.311 1.00 12.90 ? 228 ALA D CA  1 
ATOM   8320 C  C   . ALA D  1 228 ? 6.895   4.190   -56.133 1.00 13.11 ? 228 ALA D C   1 
ATOM   8321 O  O   . ALA D  1 228 ? 6.354   4.971   -56.909 1.00 15.19 ? 228 ALA D O   1 
ATOM   8322 C  CB  . ALA D  1 228 ? 5.318   2.295   -55.711 1.00 16.51 ? 228 ALA D CB  1 
ATOM   8323 N  N   . LEU D  1 229 ? 7.548   4.574   -55.080 1.00 11.97 ? 229 LEU D N   1 
ATOM   8324 C  CA  . LEU D  1 229 ? 7.488   5.971   -54.572 1.00 11.82 ? 229 LEU D CA  1 
ATOM   8325 C  C   . LEU D  1 229 ? 8.779   6.736   -54.644 1.00 11.36 ? 229 LEU D C   1 
ATOM   8326 O  O   . LEU D  1 229 ? 9.871   6.199   -54.515 1.00 10.84 ? 229 LEU D O   1 
ATOM   8327 C  CB  . LEU D  1 229 ? 7.031   5.991   -53.082 1.00 11.69 ? 229 LEU D CB  1 
ATOM   8328 C  CG  . LEU D  1 229 ? 5.749   5.131   -52.847 1.00 12.65 ? 229 LEU D CG  1 
ATOM   8329 C  CD1 . LEU D  1 229 ? 5.379   5.086   -51.361 1.00 13.93 ? 229 LEU D CD1 1 
ATOM   8330 C  CD2 . LEU D  1 229 ? 4.552   5.673   -53.628 1.00 15.76 ? 229 LEU D CD2 1 
ATOM   8331 N  N   . TYR D  1 230 ? 8.577   8.034   -54.854 1.00 11.50 ? 230 TYR D N   1 
ATOM   8332 C  CA  . TYR D  1 230 ? 9.673   9.001   -54.776 1.00 12.42 ? 230 TYR D CA  1 
ATOM   8333 C  C   . TYR D  1 230 ? 9.492   9.956   -53.594 1.00 11.37 ? 230 TYR D C   1 
ATOM   8334 O  O   . TYR D  1 230 ? 8.341   10.371  -53.284 1.00 11.35 ? 230 TYR D O   1 
ATOM   8335 C  CB  . TYR D  1 230 ? 9.787   9.780   -56.121 1.00 11.60 ? 230 TYR D CB  1 
ATOM   8336 C  CG  . TYR D  1 230 ? 10.281  8.933   -57.227 1.00 13.80 ? 230 TYR D CG  1 
ATOM   8337 C  CD1 . TYR D  1 230 ? 11.624  8.943   -57.532 1.00 14.98 ? 230 TYR D CD1 1 
ATOM   8338 C  CD2 . TYR D  1 230 ? 9.404   8.011   -57.875 1.00 16.51 ? 230 TYR D CD2 1 
ATOM   8339 C  CE1 . TYR D  1 230 ? 12.137  8.056   -58.515 1.00 18.67 ? 230 TYR D CE1 1 
ATOM   8340 C  CE2 . TYR D  1 230 ? 9.906   7.085   -58.819 1.00 20.80 ? 230 TYR D CE2 1 
ATOM   8341 C  CZ  . TYR D  1 230 ? 11.248  7.169   -59.149 1.00 21.68 ? 230 TYR D CZ  1 
ATOM   8342 O  OH  . TYR D  1 230 ? 11.749  6.269   -60.105 1.00 25.47 ? 230 TYR D OH  1 
ATOM   8343 N  N   . CYS D  1 231 ? 10.607  10.443  -53.084 1.00 12.73 ? 231 CYS D N   1 
ATOM   8344 C  CA  . CYS D  1 231 ? 10.562  11.433  -52.012 1.00 11.10 ? 231 CYS D CA  1 
ATOM   8345 C  C   . CYS D  1 231 ? 10.338  12.857  -52.529 1.00 10.53 ? 231 CYS D C   1 
ATOM   8346 O  O   . CYS D  1 231 ? 9.952   13.768  -51.800 1.00 13.82 ? 231 CYS D O   1 
ATOM   8347 C  CB  . CYS D  1 231 ? 11.891  11.542  -51.298 1.00 11.94 ? 231 CYS D CB  1 
ATOM   8348 S  SG  . CYS D  1 231 ? 12.439  10.044  -50.415 1.00 12.95 ? 231 CYS D SG  1 
ATOM   8349 N  N   . THR D  1 232 ? 10.591  13.007  -53.832 1.00 12.90 ? 232 THR D N   1 
ATOM   8350 C  CA  . THR D  1 232 ? 10.552  14.334  -54.476 1.00 13.13 ? 232 THR D CA  1 
ATOM   8351 C  C   . THR D  1 232 ? 9.291   14.541  -55.236 1.00 15.11 ? 232 THR D C   1 
ATOM   8352 O  O   . THR D  1 232 ? 8.485   13.672  -55.551 1.00 13.59 ? 232 THR D O   1 
ATOM   8353 C  CB  . THR D  1 232 ? 11.809  14.347  -55.410 1.00 14.80 ? 232 THR D CB  1 
ATOM   8354 O  OG1 . THR D  1 232 ? 11.908  13.068  -56.105 1.00 15.09 ? 232 THR D OG1 1 
ATOM   8355 C  CG2 . THR D  1 232 ? 13.047  14.572  -54.667 1.00 15.54 ? 232 THR D CG2 1 
ATOM   8356 N  N   . HIS D  1 233 ? 9.059   15.840  -55.490 1.00 16.58 ? 233 HIS D N   1 
ATOM   8357 C  CA  . HIS D  1 233 ? 7.970   16.265  -56.306 1.00 16.18 ? 233 HIS D CA  1 
ATOM   8358 C  C   . HIS D  1 233 ? 8.214   15.843  -57.730 1.00 17.23 ? 233 HIS D C   1 
ATOM   8359 O  O   . HIS D  1 233 ? 9.359   15.619  -58.159 1.00 19.27 ? 233 HIS D O   1 
ATOM   8360 C  CB  . HIS D  1 233 ? 7.888   17.833  -56.282 1.00 19.77 ? 233 HIS D CB  1 
ATOM   8361 C  CG  . HIS D  1 233 ? 7.381   18.346  -54.990 1.00 19.55 ? 233 HIS D CG  1 
ATOM   8362 N  ND1 . HIS D  1 233 ? 8.171   18.994  -54.085 1.00 26.20 ? 233 HIS D ND1 1 
ATOM   8363 C  CD2 . HIS D  1 233 ? 6.130   18.238  -54.407 1.00 23.51 ? 233 HIS D CD2 1 
ATOM   8364 C  CE1 . HIS D  1 233 ? 7.420   19.297  -52.984 1.00 27.24 ? 233 HIS D CE1 1 
ATOM   8365 N  NE2 . HIS D  1 233 ? 6.193   18.839  -53.179 1.00 23.38 ? 233 HIS D NE2 1 
ATOM   8366 N  N   . MET D  1 234 ? 7.097   15.677  -58.384 1.00 20.63 ? 234 MET D N   1 
ATOM   8367 C  CA  . MET D  1 234 ? 7.047   15.248  -59.774 1.00 21.22 ? 234 MET D CA  1 
ATOM   8368 C  C   . MET D  1 234 ? 8.000   16.011  -60.721 1.00 28.54 ? 234 MET D C   1 
ATOM   8369 O  O   . MET D  1 234 ? 8.678   15.416  -61.545 1.00 27.67 ? 234 MET D O   1 
ATOM   8370 C  CB  . MET D  1 234 ? 5.618   15.342  -60.232 1.00 21.64 ? 234 MET D CB  1 
ATOM   8371 C  CG  . MET D  1 234 ? 5.433   14.658  -61.578 1.00 35.10 ? 234 MET D CG  1 
ATOM   8372 S  SD  . MET D  1 234 ? 3.710   14.645  -62.082 1.00 43.02 ? 234 MET D SD  1 
ATOM   8373 C  CE  . MET D  1 234 ? 3.837   13.331  -63.315 1.00 43.56 ? 234 MET D CE  1 
ATOM   8374 N  N   . ASP D  1 235 ? 8.160   17.312  -60.482 1.00 25.05 ? 235 ASP D N   1 
ATOM   8375 C  CA  . ASP D  1 235 ? 9.012   18.141  -61.350 1.00 30.50 ? 235 ASP D CA  1 
ATOM   8376 C  C   . ASP D  1 235 ? 10.454  18.372  -60.855 1.00 30.25 ? 235 ASP D C   1 
ATOM   8377 O  O   . ASP D  1 235 ? 11.192  19.210  -61.373 1.00 32.73 ? 235 ASP D O   1 
ATOM   8378 C  CB  . ASP D  1 235 ? 8.309   19.507  -61.585 1.00 36.58 ? 235 ASP D CB  1 
ATOM   8379 C  CG  . ASP D  1 235 ? 8.269   20.360  -60.316 1.00 38.46 ? 235 ASP D CG  1 
ATOM   8380 O  OD1 . ASP D  1 235 ? 8.726   19.866  -59.244 1.00 40.46 ? 235 ASP D OD1 1 
ATOM   8381 O  OD2 . ASP D  1 235 ? 7.799   21.526  -60.374 1.00 36.88 ? 235 ASP D OD2 1 
ATOM   8382 N  N   . ASP D  1 236 ? 10.907  17.627  -59.858 1.00 25.71 ? 236 ASP D N   1 
ATOM   8383 C  CA  . ASP D  1 236 ? 12.216  17.847  -59.346 1.00 26.63 ? 236 ASP D CA  1 
ATOM   8384 C  C   . ASP D  1 236 ? 13.133  17.288  -60.425 1.00 26.36 ? 236 ASP D C   1 
ATOM   8385 O  O   . ASP D  1 236 ? 12.959  16.133  -60.892 1.00 24.22 ? 236 ASP D O   1 
ATOM   8386 C  CB  . ASP D  1 236 ? 12.384  17.124  -57.983 1.00 23.57 ? 236 ASP D CB  1 
ATOM   8387 C  CG  . ASP D  1 236 ? 13.560  17.591  -57.214 1.00 26.56 ? 236 ASP D CG  1 
ATOM   8388 O  OD1 . ASP D  1 236 ? 14.686  17.669  -57.729 1.00 27.39 ? 236 ASP D OD1 1 
ATOM   8389 O  OD2 . ASP D  1 236 ? 13.428  17.870  -55.976 1.00 26.87 ? 236 ASP D OD2 1 
ATOM   8390 N  N   . PRO D  1 237 ? 14.096  18.118  -60.841 1.00 28.79 ? 237 PRO D N   1 
ATOM   8391 C  CA  . PRO D  1 237 ? 15.084  17.654  -61.759 1.00 27.11 ? 237 PRO D CA  1 
ATOM   8392 C  C   . PRO D  1 237 ? 16.089  16.704  -61.076 1.00 26.90 ? 237 PRO D C   1 
ATOM   8393 O  O   . PRO D  1 237 ? 16.915  16.069  -61.797 1.00 23.68 ? 237 PRO D O   1 
ATOM   8394 C  CB  . PRO D  1 237 ? 15.739  18.969  -62.182 1.00 29.12 ? 237 PRO D CB  1 
ATOM   8395 C  CG  . PRO D  1 237 ? 15.791  19.770  -60.902 1.00 31.52 ? 237 PRO D CG  1 
ATOM   8396 C  CD  . PRO D  1 237 ? 14.421  19.479  -60.310 1.00 29.31 ? 237 PRO D CD  1 
ATOM   8397 N  N   A SER D  1 238 ? 15.989  16.510  -59.743 0.50 23.99 ? 238 SER D N   1 
ATOM   8398 N  N   B SER D  1 238 ? 16.016  16.552  -59.734 0.50 23.66 ? 238 SER D N   1 
ATOM   8399 C  CA  A SER D  1 238 ? 16.898  15.612  -59.022 0.50 22.57 ? 238 SER D CA  1 
ATOM   8400 C  CA  B SER D  1 238 ? 16.859  15.601  -59.003 0.50 21.84 ? 238 SER D CA  1 
ATOM   8401 C  C   A SER D  1 238 ? 16.143  14.525  -58.235 0.50 19.58 ? 238 SER D C   1 
ATOM   8402 C  C   B SER D  1 238 ? 15.966  14.619  -58.231 0.50 19.03 ? 238 SER D C   1 
ATOM   8403 O  O   A SER D  1 238 ? 16.212  14.523  -57.023 0.50 17.56 ? 238 SER D O   1 
ATOM   8404 O  O   B SER D  1 238 ? 15.738  14.786  -57.044 0.50 16.62 ? 238 SER D O   1 
ATOM   8405 C  CB  A SER D  1 238 ? 17.742  16.386  -58.013 0.50 25.46 ? 238 SER D CB  1 
ATOM   8406 C  CB  B SER D  1 238 ? 17.812  16.301  -58.038 0.50 23.54 ? 238 SER D CB  1 
ATOM   8407 O  OG  A SER D  1 238 ? 18.795  15.575  -57.551 0.50 28.36 ? 238 SER D OG  1 
ATOM   8408 O  OG  B SER D  1 238 ? 18.687  17.130  -58.786 0.50 25.07 ? 238 SER D OG  1 
ATOM   8409 N  N   . PRO D  1 239 ? 15.438  13.621  -58.934 1.00 18.93 ? 239 PRO D N   1 
ATOM   8410 C  CA  . PRO D  1 239 ? 14.536  12.648  -58.221 1.00 18.19 ? 239 PRO D CA  1 
ATOM   8411 C  C   . PRO D  1 239 ? 15.257  11.797  -57.244 1.00 16.50 ? 239 PRO D C   1 
ATOM   8412 O  O   . PRO D  1 239 ? 16.390  11.422  -57.413 1.00 16.30 ? 239 PRO D O   1 
ATOM   8413 C  CB  . PRO D  1 239 ? 13.940  11.758  -59.309 1.00 18.04 ? 239 PRO D CB  1 
ATOM   8414 C  CG  . PRO D  1 239 ? 14.676  12.051  -60.577 1.00 20.39 ? 239 PRO D CG  1 
ATOM   8415 C  CD  . PRO D  1 239 ? 15.492  13.330  -60.391 1.00 20.78 ? 239 PRO D CD  1 
ATOM   8416 N  N   . ARG D  1 240 ? 14.580  11.476  -56.140 1.00 15.23 ? 240 ARG D N   1 
ATOM   8417 C  CA  . ARG D  1 240 ? 15.186  10.589  -55.142 1.00 12.80 ? 240 ARG D CA  1 
ATOM   8418 C  C   . ARG D  1 240 ? 14.126  9.501   -54.786 1.00 12.35 ? 240 ARG D C   1 
ATOM   8419 O  O   . ARG D  1 240 ? 12.960  9.825   -54.427 1.00 12.74 ? 240 ARG D O   1 
ATOM   8420 C  CB  . ARG D  1 240 ? 15.433  11.336  -53.861 1.00 13.19 ? 240 ARG D CB  1 
ATOM   8421 C  CG  . ARG D  1 240 ? 16.581  12.330  -54.053 1.00 17.32 ? 240 ARG D CG  1 
ATOM   8422 C  CD  . ARG D  1 240 ? 16.895  13.022  -52.717 1.00 19.19 ? 240 ARG D CD  1 
ATOM   8423 N  NE  . ARG D  1 240 ? 15.869  14.029  -52.450 1.00 21.01 ? 240 ARG D NE  1 
ATOM   8424 C  CZ  . ARG D  1 240 ? 14.936  13.950  -51.474 1.00 23.18 ? 240 ARG D CZ  1 
ATOM   8425 N  NH1 . ARG D  1 240 ? 14.921  12.914  -50.625 1.00 17.05 ? 240 ARG D NH1 1 
ATOM   8426 N  NH2 . ARG D  1 240 ? 14.069  14.950  -51.329 1.00 19.96 ? 240 ARG D NH2 1 
ATOM   8427 N  N   . GLU D  1 241 ? 14.485  8.241   -54.944 1.00 12.01 ? 241 GLU D N   1 
ATOM   8428 C  CA  . GLU D  1 241 ? 13.563  7.097   -54.613 1.00 12.79 ? 241 GLU D CA  1 
ATOM   8429 C  C   . GLU D  1 241 ? 13.335  7.041   -53.141 1.00 11.18 ? 241 GLU D C   1 
ATOM   8430 O  O   . GLU D  1 241 ? 14.210  7.262   -52.303 1.00 11.90 ? 241 GLU D O   1 
ATOM   8431 C  CB  . GLU D  1 241 ? 14.281  5.825   -55.041 1.00 14.15 ? 241 GLU D CB  1 
ATOM   8432 C  CG  . GLU D  1 241 ? 14.397  5.707   -56.591 1.00 17.26 ? 241 GLU D CG  1 
ATOM   8433 C  CD  . GLU D  1 241 ? 15.287  4.596   -56.918 1.00 25.28 ? 241 GLU D CD  1 
ATOM   8434 O  OE1 . GLU D  1 241 ? 16.465  4.650   -56.488 1.00 30.49 ? 241 GLU D OE1 1 
ATOM   8435 O  OE2 . GLU D  1 241 ? 14.816  3.663   -57.576 1.00 30.44 ? 241 GLU D OE2 1 
ATOM   8436 N  N   . MET D  1 242 ? 12.079  6.711   -52.807 1.00 9.17  ? 242 MET D N   1 
ATOM   8437 C  CA  . MET D  1 242 ? 11.738  6.552   -51.376 1.00 9.58  ? 242 MET D CA  1 
ATOM   8438 C  C   . MET D  1 242 ? 12.029  5.087   -50.914 1.00 8.87  ? 242 MET D C   1 
ATOM   8439 O  O   . MET D  1 242 ? 11.202  4.190   -51.124 1.00 8.86  ? 242 MET D O   1 
ATOM   8440 C  CB  . MET D  1 242 ? 10.277  6.946   -51.180 1.00 9.46  ? 242 MET D CB  1 
ATOM   8441 C  CG  . MET D  1 242 ? 9.920   6.973   -49.648 1.00 9.65  ? 242 MET D CG  1 
ATOM   8442 S  SD  . MET D  1 242 ? 8.169   7.267   -49.345 1.00 9.68  ? 242 MET D SD  1 
ATOM   8443 C  CE  . MET D  1 242 ? 8.084   8.923   -50.025 1.00 11.57 ? 242 MET D CE  1 
ATOM   8444 N  N   . ILE D  1 243 ? 13.264  4.903   -50.461 1.00 8.85  ? 243 ILE D N   1 
ATOM   8445 C  CA  . ILE D  1 243 ? 13.783  3.603   -50.053 1.00 8.97  ? 243 ILE D CA  1 
ATOM   8446 C  C   . ILE D  1 243 ? 14.521  3.834   -48.722 1.00 7.82  ? 243 ILE D C   1 
ATOM   8447 O  O   . ILE D  1 243 ? 14.972  4.928   -48.437 1.00 9.02  ? 243 ILE D O   1 
ATOM   8448 C  CB  . ILE D  1 243 ? 14.747  2.981   -51.127 1.00 10.08 ? 243 ILE D CB  1 
ATOM   8449 C  CG1 . ILE D  1 243 ? 15.892  4.030   -51.453 1.00 11.06 ? 243 ILE D CG1 1 
ATOM   8450 C  CG2 . ILE D  1 243 ? 13.948  2.548   -52.348 1.00 12.86 ? 243 ILE D CG2 1 
ATOM   8451 C  CD1 . ILE D  1 243 ? 16.918  3.476   -52.375 1.00 13.77 ? 243 ILE D CD1 1 
ATOM   8452 N  N   . ASN D  1 244 ? 14.665  2.725   -47.979 1.00 8.04  ? 244 ASN D N   1 
ATOM   8453 C  CA  . ASN D  1 244 ? 15.469  2.751   -46.748 1.00 7.41  ? 244 ASN D CA  1 
ATOM   8454 C  C   . ASN D  1 244 ? 15.063  3.840   -45.806 1.00 8.22  ? 244 ASN D C   1 
ATOM   8455 O  O   . ASN D  1 244 ? 15.896  4.532   -45.215 1.00 8.24  ? 244 ASN D O   1 
ATOM   8456 C  CB  . ASN D  1 244 ? 17.002  2.848   -47.046 1.00 9.96  ? 244 ASN D CB  1 
ATOM   8457 C  CG  . ASN D  1 244 ? 17.394  1.766   -48.000 1.00 10.46 ? 244 ASN D CG  1 
ATOM   8458 O  OD1 . ASN D  1 244 ? 16.981  0.609   -47.933 1.00 11.19 ? 244 ASN D OD1 1 
ATOM   8459 N  ND2 . ASN D  1 244 ? 18.221  2.220   -49.025 1.00 13.03 ? 244 ASN D ND2 1 
ATOM   8460 N  N   . ASN D  1 245 ? 13.756  4.019   -45.653 1.00 7.46  ? 245 ASN D N   1 
ATOM   8461 C  CA  . ASN D  1 245 ? 13.188  5.130   -44.860 1.00 7.17  ? 245 ASN D CA  1 
ATOM   8462 C  C   . ASN D  1 245 ? 12.908  4.664   -43.433 1.00 8.22  ? 245 ASN D C   1 
ATOM   8463 O  O   . ASN D  1 245 ? 11.782  4.787   -42.907 1.00 8.61  ? 245 ASN D O   1 
ATOM   8464 C  CB  . ASN D  1 245 ? 11.907  5.730   -45.513 1.00 8.22  ? 245 ASN D CB  1 
ATOM   8465 C  CG  . ASN D  1 245 ? 10.798  4.740   -45.713 1.00 7.63  ? 245 ASN D CG  1 
ATOM   8466 O  OD1 . ASN D  1 245 ? 10.984  3.560   -45.679 1.00 9.14  ? 245 ASN D OD1 1 
ATOM   8467 N  ND2 . ASN D  1 245 ? 9.575   5.233   -45.885 1.00 8.92  ? 245 ASN D ND2 1 
ATOM   8468 N  N   . PHE D  1 246 ? 13.930  4.097   -42.837 1.00 7.15  ? 246 PHE D N   1 
ATOM   8469 C  CA  . PHE D  1 246 ? 13.897  3.683   -41.412 1.00 6.77  ? 246 PHE D CA  1 
ATOM   8470 C  C   . PHE D  1 246 ? 15.081  4.276   -40.729 1.00 7.44  ? 246 PHE D C   1 
ATOM   8471 O  O   . PHE D  1 246 ? 16.169  4.431   -41.305 1.00 8.19  ? 246 PHE D O   1 
ATOM   8472 C  CB  . PHE D  1 246 ? 13.953  2.089   -41.359 1.00 7.22  ? 246 PHE D CB  1 
ATOM   8473 C  CG  . PHE D  1 246 ? 15.198  1.447   -41.925 1.00 7.47  ? 246 PHE D CG  1 
ATOM   8474 C  CD1 . PHE D  1 246 ? 16.266  1.112   -41.088 1.00 8.76  ? 246 PHE D CD1 1 
ATOM   8475 C  CD2 . PHE D  1 246 ? 15.286  1.153   -43.317 1.00 7.80  ? 246 PHE D CD2 1 
ATOM   8476 C  CE1 . PHE D  1 246 ? 17.419  0.546   -41.618 1.00 9.09  ? 246 PHE D CE1 1 
ATOM   8477 C  CE2 . PHE D  1 246 ? 16.469  0.566   -43.858 1.00 7.84  ? 246 PHE D CE2 1 
ATOM   8478 C  CZ  . PHE D  1 246 ? 17.529  0.273   -42.973 1.00 9.17  ? 246 PHE D CZ  1 
ATOM   8479 N  N   . ARG D  1 247 ? 14.953  4.589   -39.453 1.00 7.30  ? 247 ARG D N   1 
ATOM   8480 C  CA  . ARG D  1 247 ? 16.047  5.106   -38.636 1.00 7.97  ? 247 ARG D CA  1 
ATOM   8481 C  C   . ARG D  1 247 ? 16.753  3.903   -37.983 1.00 7.84  ? 247 ARG D C   1 
ATOM   8482 O  O   . ARG D  1 247 ? 16.102  2.883   -37.660 1.00 7.91  ? 247 ARG D O   1 
ATOM   8483 C  CB  . ARG D  1 247 ? 15.404  5.989   -37.522 1.00 7.61  ? 247 ARG D CB  1 
ATOM   8484 C  CG  . ARG D  1 247 ? 16.420  6.849   -36.769 1.00 7.90  ? 247 ARG D CG  1 
ATOM   8485 C  CD  . ARG D  1 247 ? 15.722  7.562   -35.648 1.00 7.86  ? 247 ARG D CD  1 
ATOM   8486 N  NE  . ARG D  1 247 ? 16.552  8.654   -35.140 1.00 7.28  ? 247 ARG D NE  1 
ATOM   8487 C  CZ  . ARG D  1 247 ? 16.301  9.350   -34.036 1.00 8.41  ? 247 ARG D CZ  1 
ATOM   8488 N  NH1 . ARG D  1 247 ? 15.231  9.078   -33.301 1.00 8.55  ? 247 ARG D NH1 1 
ATOM   8489 N  NH2 . ARG D  1 247 ? 17.126  10.320  -33.664 1.00 8.07  ? 247 ARG D NH2 1 
ATOM   8490 N  N   . GLN D  1 248 ? 18.085  4.047   -37.761 1.00 6.95  ? 248 GLN D N   1 
ATOM   8491 C  CA  . GLN D  1 248 ? 18.831  3.038   -36.964 1.00 7.53  ? 248 GLN D CA  1 
ATOM   8492 C  C   . GLN D  1 248 ? 18.318  3.006   -35.530 1.00 7.23  ? 248 GLN D C   1 
ATOM   8493 O  O   . GLN D  1 248 ? 17.793  4.009   -34.997 1.00 7.56  ? 248 GLN D O   1 
ATOM   8494 C  CB  . GLN D  1 248 ? 20.330  3.420   -36.926 1.00 7.13  ? 248 GLN D CB  1 
ATOM   8495 C  CG  . GLN D  1 248 ? 21.003  3.385   -38.323 1.00 8.30  ? 248 GLN D CG  1 
ATOM   8496 C  CD  . GLN D  1 248 ? 20.920  2.001   -38.967 1.00 9.16  ? 248 GLN D CD  1 
ATOM   8497 O  OE1 . GLN D  1 248 ? 20.024  1.644   -39.725 1.00 10.23 ? 248 GLN D OE1 1 
ATOM   8498 N  NE2 . GLN D  1 248 ? 21.950  1.176   -38.646 1.00 10.41 ? 248 GLN D NE2 1 
ATOM   8499 N  N   . VAL D  1 249 ? 18.531  1.852   -34.909 1.00 7.42  ? 249 VAL D N   1 
ATOM   8500 C  CA  . VAL D  1 249 ? 18.165  1.763   -33.478 1.00 8.61  ? 249 VAL D CA  1 
ATOM   8501 C  C   . VAL D  1 249 ? 19.044  2.639   -32.582 1.00 9.03  ? 249 VAL D C   1 
ATOM   8502 O  O   . VAL D  1 249 ? 20.163  3.026   -32.966 1.00 8.29  ? 249 VAL D O   1 
ATOM   8503 C  CB  . VAL D  1 249 ? 18.180  0.330   -32.944 1.00 8.41  ? 249 VAL D CB  1 
ATOM   8504 C  CG1 . VAL D  1 249 ? 17.080  -0.502  -33.636 1.00 9.28  ? 249 VAL D CG1 1 
ATOM   8505 C  CG2 . VAL D  1 249 ? 19.578  -0.336  -33.035 1.00 9.31  ? 249 VAL D CG2 1 
ATOM   8506 N  N   . GLN D  1 250 ? 18.447  3.036   -31.473 1.00 8.41  ? 250 GLN D N   1 
ATOM   8507 C  CA  . GLN D  1 250 ? 18.989  4.078   -30.535 1.00 9.20  ? 250 GLN D CA  1 
ATOM   8508 C  C   . GLN D  1 250 ? 19.491  3.512   -29.208 1.00 9.84  ? 250 GLN D C   1 
ATOM   8509 O  O   . GLN D  1 250 ? 19.027  2.439   -28.782 1.00 10.50 ? 250 GLN D O   1 
ATOM   8510 C  CB  . GLN D  1 250 ? 17.861  5.083   -30.216 1.00 8.82  ? 250 GLN D CB  1 
ATOM   8511 C  CG  . GLN D  1 250 ? 17.248  5.699   -31.484 1.00 8.62  ? 250 GLN D CG  1 
ATOM   8512 C  CD  . GLN D  1 250 ? 18.184  6.591   -32.228 1.00 8.85  ? 250 GLN D CD  1 
ATOM   8513 O  OE1 . GLN D  1 250 ? 18.596  7.646   -31.670 1.00 10.22 ? 250 GLN D OE1 1 
ATOM   8514 N  NE2 . GLN D  1 250 ? 18.417  6.315   -33.477 1.00 8.93  ? 250 GLN D NE2 1 
ATOM   8515 N  N   . LYS D  1 251 ? 20.362  4.282   -28.566 1.00 9.58  ? 251 LYS D N   1 
ATOM   8516 C  CA  . LYS D  1 251 ? 20.750  3.897   -27.190 1.00 10.04 ? 251 LYS D CA  1 
ATOM   8517 C  C   . LYS D  1 251 ? 19.509  3.769   -26.264 1.00 9.59  ? 251 LYS D C   1 
ATOM   8518 O  O   . LYS D  1 251 ? 18.496  4.550   -26.356 1.00 9.79  ? 251 LYS D O   1 
ATOM   8519 C  CB  . LYS D  1 251 ? 21.662  4.977   -26.628 1.00 10.96 ? 251 LYS D CB  1 
ATOM   8520 C  CG  . LYS D  1 251 ? 23.051  4.955   -27.318 1.00 12.29 ? 251 LYS D CG  1 
ATOM   8521 C  CD  . LYS D  1 251 ? 23.872  3.744   -26.784 1.00 11.26 ? 251 LYS D CD  1 
ATOM   8522 C  CE  . LYS D  1 251 ? 25.381  3.856   -27.148 1.00 12.47 ? 251 LYS D CE  1 
ATOM   8523 N  NZ  . LYS D  1 251 ? 25.558  3.753   -28.654 1.00 11.13 ? 251 LYS D NZ  1 
ATOM   8524 N  N   . PHE D  1 252 ? 19.576  2.819   -25.350 1.00 11.06 ? 252 PHE D N   1 
ATOM   8525 C  CA  . PHE D  1 252 ? 18.499  2.633   -24.405 1.00 11.73 ? 252 PHE D CA  1 
ATOM   8526 C  C   . PHE D  1 252 ? 18.341  3.800   -23.366 1.00 15.89 ? 252 PHE D C   1 
ATOM   8527 O  O   . PHE D  1 252 ? 17.249  4.057   -22.886 1.00 15.41 ? 252 PHE D O   1 
ATOM   8528 C  CB  . PHE D  1 252 ? 18.622  1.288   -23.718 1.00 14.75 ? 252 PHE D CB  1 
ATOM   8529 C  CG  . PHE D  1 252 ? 17.987  0.209   -24.509 1.00 16.33 ? 252 PHE D CG  1 
ATOM   8530 C  CD1 . PHE D  1 252 ? 16.648  -0.076  -24.341 1.00 19.46 ? 252 PHE D CD1 1 
ATOM   8531 C  CD2 . PHE D  1 252 ? 18.696  -0.446  -25.497 1.00 22.88 ? 252 PHE D CD2 1 
ATOM   8532 C  CE1 . PHE D  1 252 ? 16.037  -1.043  -25.104 1.00 20.91 ? 252 PHE D CE1 1 
ATOM   8533 C  CE2 . PHE D  1 252 ? 18.093  -1.416  -26.266 1.00 19.30 ? 252 PHE D CE2 1 
ATOM   8534 C  CZ  . PHE D  1 252 ? 16.760  -1.715  -26.069 1.00 18.54 ? 252 PHE D CZ  1 
ATOM   8535 N  N   . ASP D  1 253 ? 19.391  4.541   -22.985 1.00 13.39 ? 253 ASP D N   1 
ATOM   8536 C  CA  . ASP D  1 253 ? 19.209  5.660   -22.024 1.00 17.15 ? 253 ASP D CA  1 
ATOM   8537 C  C   . ASP D  1 253 ? 18.589  5.167   -20.688 1.00 17.06 ? 253 ASP D C   1 
ATOM   8538 O  O   . ASP D  1 253 ? 17.761  5.847   -20.131 1.00 19.22 ? 253 ASP D O   1 
ATOM   8539 C  CB  . ASP D  1 253 ? 18.378  6.811   -22.624 1.00 19.40 ? 253 ASP D CB  1 
ATOM   8540 C  CG  . ASP D  1 253 ? 19.108  7.525   -23.781 1.00 20.16 ? 253 ASP D CG  1 
ATOM   8541 O  OD1 . ASP D  1 253 ? 20.359  7.418   -23.888 1.00 20.16 ? 253 ASP D OD1 1 
ATOM   8542 O  OD2 . ASP D  1 253 ? 18.372  8.177   -24.549 1.00 20.09 ? 253 ASP D OD2 1 
ATOM   8543 N  N   . GLU D  1 254 ? 18.992  3.949   -20.299 1.00 17.80 ? 254 GLU D N   1 
ATOM   8544 C  CA  . GLU D  1 254 ? 18.569  3.280   -19.017 1.00 18.23 ? 254 GLU D CA  1 
ATOM   8545 C  C   . GLU D  1 254 ? 17.110  2.782   -19.014 1.00 18.61 ? 254 GLU D C   1 
ATOM   8546 O  O   . GLU D  1 254 ? 16.626  2.254   -17.959 1.00 19.88 ? 254 GLU D O   1 
ATOM   8547 C  CB  . GLU D  1 254 ? 18.734  4.252   -17.807 1.00 20.85 ? 254 GLU D CB  1 
ATOM   8548 C  CG  . GLU D  1 254 ? 20.192  4.354   -17.327 1.00 28.80 ? 254 GLU D CG  1 
ATOM   8549 C  CD  . GLU D  1 254 ? 20.266  5.250   -16.061 1.00 43.14 ? 254 GLU D CD  1 
ATOM   8550 O  OE1 . GLU D  1 254 ? 20.171  4.727   -14.910 1.00 50.94 ? 254 GLU D OE1 1 
ATOM   8551 O  OE2 . GLU D  1 254 ? 20.341  6.500   -16.228 1.00 51.59 ? 254 GLU D OE2 1 
ATOM   8552 N  N   . ARG D  1 255 ? 16.373  2.892   -20.118 1.00 15.36 ? 255 ARG D N   1 
ATOM   8553 C  CA  . ARG D  1 255 ? 15.020  2.308   -20.249 1.00 14.76 ? 255 ARG D CA  1 
ATOM   8554 C  C   . ARG D  1 255 ? 15.022  0.803   -20.225 1.00 15.32 ? 255 ARG D C   1 
ATOM   8555 O  O   . ARG D  1 255 ? 15.950  0.135   -20.750 1.00 17.22 ? 255 ARG D O   1 
ATOM   8556 C  CB  . ARG D  1 255 ? 14.400  2.738   -21.634 1.00 14.76 ? 255 ARG D CB  1 
ATOM   8557 C  CG  . ARG D  1 255 ? 13.993  4.190   -21.641 1.00 15.87 ? 255 ARG D CG  1 
ATOM   8558 C  CD  . ARG D  1 255 ? 13.568  4.617   -23.054 1.00 15.37 ? 255 ARG D CD  1 
ATOM   8559 N  NE  . ARG D  1 255 ? 14.655  4.562   -24.014 1.00 14.32 ? 255 ARG D NE  1 
ATOM   8560 C  CZ  . ARG D  1 255 ? 14.567  4.876   -25.313 1.00 13.53 ? 255 ARG D CZ  1 
ATOM   8561 N  NH1 . ARG D  1 255 ? 13.370  5.217   -25.858 1.00 11.22 ? 255 ARG D NH1 1 
ATOM   8562 N  NH2 . ARG D  1 255 ? 15.712  4.931   -26.087 1.00 14.08 ? 255 ARG D NH2 1 
ATOM   8563 N  N   . LEU D  1 256 ? 13.931  0.217   -19.678 1.00 14.34 ? 256 LEU D N   1 
ATOM   8564 C  CA  . LEU D  1 256 ? 13.606  -1.167  -19.924 1.00 13.13 ? 256 LEU D CA  1 
ATOM   8565 C  C   . LEU D  1 256 ? 12.414  -1.156  -20.906 1.00 13.03 ? 256 LEU D C   1 
ATOM   8566 O  O   . LEU D  1 256 ? 11.748  -0.096  -21.145 1.00 14.72 ? 256 LEU D O   1 
ATOM   8567 C  CB  . LEU D  1 256 ? 13.162  -1.888  -18.658 1.00 14.78 ? 256 LEU D CB  1 
ATOM   8568 C  CG  . LEU D  1 256 ? 14.217  -1.844  -17.586 1.00 15.62 ? 256 LEU D CG  1 
ATOM   8569 C  CD1 . LEU D  1 256 ? 13.673  -2.534  -16.312 1.00 17.11 ? 256 LEU D CD1 1 
ATOM   8570 C  CD2 . LEU D  1 256 ? 15.519  -2.497  -18.070 1.00 20.45 ? 256 LEU D CD2 1 
ATOM   8571 N  N   . VAL D  1 257 ? 12.225  -2.291  -21.523 1.00 11.55 ? 257 VAL D N   1 
ATOM   8572 C  CA  . VAL D  1 257 ? 11.057  -2.550  -22.365 1.00 11.92 ? 257 VAL D CA  1 
ATOM   8573 C  C   . VAL D  1 257 ? 10.206  -3.568  -21.637 1.00 11.97 ? 257 VAL D C   1 
ATOM   8574 O  O   . VAL D  1 257 ? 10.662  -4.640  -21.230 1.00 13.70 ? 257 VAL D O   1 
ATOM   8575 C  CB  . VAL D  1 257 ? 11.383  -3.130  -23.780 1.00 11.70 ? 257 VAL D CB  1 
ATOM   8576 C  CG1 . VAL D  1 257 ? 10.136  -3.538  -24.528 1.00 13.61 ? 257 VAL D CG1 1 
ATOM   8577 C  CG2 . VAL D  1 257 ? 12.191  -2.094  -24.556 1.00 12.50 ? 257 VAL D CG2 1 
ATOM   8578 N  N   . TYR D  1 258 ? 8.962   -3.189  -21.405 1.00 10.68 ? 258 TYR D N   1 
ATOM   8579 C  CA  . TYR D  1 258 ? 8.058   -4.021  -20.595 1.00 10.08 ? 258 TYR D CA  1 
ATOM   8580 C  C   . TYR D  1 258 ? 7.214   -4.885  -21.438 1.00 10.92 ? 258 TYR D C   1 
ATOM   8581 O  O   . TYR D  1 258 ? 6.800   -4.498  -22.575 1.00 12.11 ? 258 TYR D O   1 
ATOM   8582 C  CB  . TYR D  1 258 ? 7.188   -3.101  -19.669 1.00 12.91 ? 258 TYR D CB  1 
ATOM   8583 C  CG  . TYR D  1 258 ? 8.069   -2.240  -18.805 1.00 13.13 ? 258 TYR D CG  1 
ATOM   8584 C  CD1 . TYR D  1 258 ? 8.579   -2.720  -17.612 1.00 13.96 ? 258 TYR D CD1 1 
ATOM   8585 C  CD2 . TYR D  1 258 ? 8.447   -0.969  -19.214 1.00 13.13 ? 258 TYR D CD2 1 
ATOM   8586 C  CE1 . TYR D  1 258 ? 9.412   -1.946  -16.824 1.00 15.37 ? 258 TYR D CE1 1 
ATOM   8587 C  CE2 . TYR D  1 258 ? 9.276   -0.184  -18.446 1.00 16.15 ? 258 TYR D CE2 1 
ATOM   8588 C  CZ  . TYR D  1 258 ? 9.758   -0.674  -17.251 1.00 17.05 ? 258 TYR D CZ  1 
ATOM   8589 O  OH  . TYR D  1 258 ? 10.586  0.139   -16.516 1.00 18.67 ? 258 TYR D OH  1 
ATOM   8590 N  N   . THR D  1 259 ? 6.999   -6.154  -21.057 1.00 10.16 ? 259 THR D N   1 
ATOM   8591 C  CA  . THR D  1 259 ? 6.291   -7.044  -21.953 1.00 9.50  ? 259 THR D CA  1 
ATOM   8592 C  C   . THR D  1 259 ? 4.986   -7.544  -21.265 1.00 9.50  ? 259 THR D C   1 
ATOM   8593 O  O   . THR D  1 259 ? 4.925   -7.677  -19.978 1.00 10.15 ? 259 THR D O   1 
ATOM   8594 C  CB  . THR D  1 259 ? 7.139   -8.269  -22.367 1.00 10.58 ? 259 THR D CB  1 
ATOM   8595 O  OG1 . THR D  1 259 ? 7.598   -8.941  -21.145 1.00 13.31 ? 259 THR D OG1 1 
ATOM   8596 C  CG2 . THR D  1 259 ? 8.423   -7.778  -23.090 1.00 12.12 ? 259 THR D CG2 1 
ATOM   8597 N  N   . SER D  1 260 ? 3.998   -7.858  -22.045 1.00 10.30 ? 260 SER D N   1 
ATOM   8598 C  CA  . SER D  1 260 ? 2.746   -8.420  -21.492 1.00 10.36 ? 260 SER D CA  1 
ATOM   8599 C  C   . SER D  1 260 ? 2.838   -9.936  -21.498 1.00 11.89 ? 260 SER D C   1 
ATOM   8600 O  O   . SER D  1 260 ? 1.843   -10.597 -21.207 1.00 15.20 ? 260 SER D O   1 
ATOM   8601 C  CB  . SER D  1 260 ? 1.573   -7.960  -22.293 1.00 11.58 ? 260 SER D CB  1 
ATOM   8602 O  OG  . SER D  1 260 ? 1.716   -8.442  -23.630 1.00 11.94 ? 260 SER D OG  1 
ATOM   8603 N  N   . PHE D  1 261 ? 3.985   -10.500 -21.794 1.00 12.37 ? 261 PHE D N   1 
ATOM   8604 C  CA  . PHE D  1 261 ? 4.150   -11.968 -21.899 1.00 15.05 ? 261 PHE D CA  1 
ATOM   8605 C  C   . PHE D  1 261 ? 5.477   -12.282 -21.245 1.00 16.39 ? 261 PHE D C   1 
ATOM   8606 O  O   . PHE D  1 261 ? 6.321   -11.461 -21.045 1.00 15.45 ? 261 PHE D O   1 
ATOM   8607 C  CB  . PHE D  1 261 ? 4.111   -12.460 -23.352 1.00 15.74 ? 261 PHE D CB  1 
ATOM   8608 C  CG  . PHE D  1 261 ? 5.139   -11.766 -24.201 1.00 14.94 ? 261 PHE D CG  1 
ATOM   8609 C  CD1 . PHE D  1 261 ? 6.441   -12.270 -24.311 1.00 15.74 ? 261 PHE D CD1 1 
ATOM   8610 C  CD2 . PHE D  1 261 ? 4.876   -10.511 -24.868 1.00 14.36 ? 261 PHE D CD2 1 
ATOM   8611 C  CE1 . PHE D  1 261 ? 7.429   -11.653 -25.071 1.00 16.23 ? 261 PHE D CE1 1 
ATOM   8612 C  CE2 . PHE D  1 261 ? 5.932   -9.912  -25.600 1.00 14.46 ? 261 PHE D CE2 1 
ATOM   8613 C  CZ  . PHE D  1 261 ? 7.184   -10.410 -25.699 1.00 14.08 ? 261 PHE D CZ  1 
ATOM   8614 N  N   . SER D  1 262 ? 5.697   -13.557 -20.839 1.00 23.13 ? 262 SER D N   1 
ATOM   8615 C  CA  . SER D  1 262 ? 7.031   -13.976 -20.374 1.00 29.75 ? 262 SER D CA  1 
ATOM   8616 C  C   . SER D  1 262 ? 7.632   -14.972 -21.365 1.00 36.12 ? 262 SER D C   1 
ATOM   8617 O  O   . SER D  1 262 ? 8.848   -14.952 -21.699 1.00 34.00 ? 262 SER D O   1 
ATOM   8618 C  CB  . SER D  1 262 ? 6.926   -14.624 -19.006 1.00 36.90 ? 262 SER D CB  1 
ATOM   8619 O  OG  . SER D  1 262 ? 6.094   -13.845 -18.220 1.00 40.71 ? 262 SER D OG  1 
ATOM   8620 N  N   . GLN D  1 263 ? 6.711   -15.833 -21.769 1.00 40.75 ? 263 GLN D N   1 
ATOM   8621 C  CA  . GLN D  1 263 ? 6.717   -16.804 -22.872 1.00 61.37 ? 263 GLN D CA  1 
ATOM   8622 C  C   . GLN D  1 263 ? 8.023   -17.438 -23.433 1.00 71.84 ? 263 GLN D C   1 
ATOM   8623 O  O   . GLN D  1 263 ? 7.953   -18.234 -24.382 1.00 78.34 ? 263 GLN D O   1 
ATOM   8624 C  CB  . GLN D  1 263 ? 5.730   -16.347 -23.973 1.00 56.52 ? 263 GLN D CB  1 
ATOM   8625 C  CG  . GLN D  1 263 ? 4.303   -16.919 -23.855 1.00 58.41 ? 263 GLN D CG  1 
ATOM   8626 C  CD  . GLN D  1 263 ? 3.343   -16.123 -22.947 1.00 60.00 ? 263 GLN D CD  1 
ATOM   8627 O  OE1 . GLN D  1 263 ? 3.662   -15.778 -21.788 1.00 49.84 ? 263 GLN D OE1 1 
ATOM   8628 N  NE2 . GLN D  1 263 ? 2.130   -15.855 -23.471 1.00 61.03 ? 263 GLN D NE2 1 
ATOM   8629 O  OXT . GLN D  1 263 ? 9.149   -17.222 -22.947 1.00 80.42 ? 263 GLN D OXT 1 
HETATM 8630 ZN ZN  . ZN  E  2 .   ? 22.903  0.654   12.276  1.00 8.54  ? 301 ZN  A ZN  1 
HETATM 8631 O  O12 . 6YH F  3 .   ? 27.604  7.522   11.045  1.00 31.81 ? 302 6YH A O12 1 
HETATM 8632 C  C11 . 6YH F  3 .   ? 26.390  7.543   11.060  1.00 31.22 ? 302 6YH A C11 1 
HETATM 8633 C  C4  . 6YH F  3 .   ? 25.703  6.261   10.842  1.00 25.79 ? 302 6YH A C4  1 
HETATM 8634 C  C3  . 6YH F  3 .   ? 24.305  6.177   10.856  1.00 26.56 ? 302 6YH A C3  1 
HETATM 8635 C  C2  . 6YH F  3 .   ? 23.678  4.935   10.631  1.00 20.90 ? 302 6YH A C2  1 
HETATM 8636 C  C5  . 6YH F  3 .   ? 26.504  5.156   10.477  1.00 21.52 ? 302 6YH A C5  1 
HETATM 8637 C  C6  . 6YH F  3 .   ? 25.870  3.920   10.247  1.00 18.92 ? 302 6YH A C6  1 
HETATM 8638 C  C1  . 6YH F  3 .   ? 24.454  3.883   10.291  1.00 17.10 ? 302 6YH A C1  1 
HETATM 8639 S  S7  . 6YH F  3 .   ? 23.583  2.354   9.939   1.00 14.29 ? 302 6YH A S7  1 
HETATM 8640 O  O9  . 6YH F  3 .   ? 22.897  2.496   8.602   1.00 11.60 ? 302 6YH A O9  1 
HETATM 8641 N  N10 . 6YH F  3 .   ? 22.604  2.146   11.129  1.00 12.46 ? 302 6YH A N10 1 
HETATM 8642 O  O8  . 6YH F  3 .   ? 24.636  1.260   9.951   1.00 13.85 ? 302 6YH A O8  1 
HETATM 8643 C  C13 . 6YH F  3 .   ? 25.607  8.830   11.182  1.00 34.97 ? 302 6YH A C13 1 
HETATM 8644 N  N14 . 6YH F  3 .   ? 26.443  10.044  11.330  1.00 39.83 ? 302 6YH A N14 1 
HETATM 8645 C  C18 . 6YH F  3 .   ? 26.891  10.814  10.293  1.00 36.25 ? 302 6YH A C18 1 
HETATM 8646 C  C20 . 6YH F  3 .   ? 26.711  10.671  8.920   1.00 32.65 ? 302 6YH A C20 1 
HETATM 8647 C  C21 . 6YH F  3 .   ? 27.269  11.656  8.061   1.00 36.93 ? 302 6YH A C21 1 
HETATM 8648 C  C22 . 6YH F  3 .   ? 28.049  12.711  8.571   1.00 36.08 ? 302 6YH A C22 1 
HETATM 8649 C  C23 . 6YH F  3 .   ? 28.228  12.836  9.961   1.00 39.46 ? 302 6YH A C23 1 
HETATM 8650 C  C19 . 6YH F  3 .   ? 27.628  11.872  10.817  1.00 44.20 ? 302 6YH A C19 1 
HETATM 8651 N  N17 . 6YH F  3 .   ? 27.661  11.786  12.192  1.00 44.19 ? 302 6YH A N17 1 
HETATM 8652 C  C16 . 6YH F  3 .   ? 26.921  10.655  12.476  1.00 44.21 ? 302 6YH A C16 1 
HETATM 8653 C  C1  . EDO G  4 .   ? 26.159  -8.784  30.013  1.00 27.46 ? 303 EDO A C1  1 
HETATM 8654 O  O1  . EDO G  4 .   ? 25.819  -9.871  29.128  1.00 29.09 ? 303 EDO A O1  1 
HETATM 8655 C  C2  . EDO G  4 .   ? 27.066  -9.232  31.152  1.00 28.96 ? 303 EDO A C2  1 
HETATM 8656 O  O2  . EDO G  4 .   ? 28.413  -9.498  30.652  1.00 28.78 ? 303 EDO A O2  1 
HETATM 8657 C  C1  . EDO H  4 .   ? 25.067  4.694   14.210  1.00 25.38 ? 304 EDO A C1  1 
HETATM 8658 O  O1  . EDO H  4 .   ? 26.042  5.158   15.112  1.00 28.39 ? 304 EDO A O1  1 
HETATM 8659 C  C2  . EDO H  4 .   ? 23.858  4.272   15.072  1.00 25.26 ? 304 EDO A C2  1 
HETATM 8660 O  O2  . EDO H  4 .   ? 23.289  5.412   15.698  1.00 28.79 ? 304 EDO A O2  1 
HETATM 8661 C  C1  . EDO I  4 .   ? 27.544  9.681   15.844  1.00 42.66 ? 305 EDO A C1  1 
HETATM 8662 O  O1  . EDO I  4 .   ? 27.953  9.833   17.211  1.00 40.21 ? 305 EDO A O1  1 
HETATM 8663 C  C2  . EDO I  4 .   ? 27.995  8.302   15.329  1.00 37.89 ? 305 EDO A C2  1 
HETATM 8664 O  O2  . EDO I  4 .   ? 26.904  7.585   14.706  1.00 34.41 ? 305 EDO A O2  1 
HETATM 8665 ZN ZN  . ZN  J  2 .   ? -8.170  3.735   4.887   1.00 6.82  ? 301 ZN  B ZN  1 
HETATM 8666 O  O12 . 6YH K  3 .   ? -11.395 11.459  6.109   1.00 29.24 ? 302 6YH B O12 1 
HETATM 8667 C  C11 . 6YH K  3 .   ? -10.219 11.247  6.001   1.00 26.42 ? 302 6YH B C11 1 
HETATM 8668 C  C4  . 6YH K  3 .   ? -9.783  9.823   6.261   1.00 15.59 ? 302 6YH B C4  1 
HETATM 8669 C  C3  . 6YH K  3 .   ? -10.731 8.920   6.671   1.00 16.35 ? 302 6YH B C3  1 
HETATM 8670 C  C2  . 6YH K  3 .   ? -10.332 7.551   6.883   1.00 13.31 ? 302 6YH B C2  1 
HETATM 8671 C  C5  . 6YH K  3 .   ? -8.420  9.524   6.150   1.00 16.11 ? 302 6YH B C5  1 
HETATM 8672 C  C6  . 6YH K  3 .   ? -7.967  8.218   6.440   1.00 13.90 ? 302 6YH B C6  1 
HETATM 8673 C  C1  . 6YH K  3 .   ? -8.945  7.323   6.832   1.00 11.04 ? 302 6YH B C1  1 
HETATM 8674 S  S7  . 6YH K  3 .   ? -8.393  5.639   7.211   1.00 10.32 ? 302 6YH B S7  1 
HETATM 8675 O  O9  . 6YH K  3 .   ? -7.582  5.778   8.456   1.00 9.48  ? 302 6YH B O9  1 
HETATM 8676 N  N10 . 6YH K  3 .   ? -7.555  5.159   5.907   1.00 10.83 ? 302 6YH B N10 1 
HETATM 8677 O  O8  . 6YH K  3 .   ? -9.580  4.814   7.313   1.00 10.81 ? 302 6YH B O8  1 
HETATM 8678 C  C13 . 6YH K  3 .   ? -9.222  12.356  5.751   1.00 36.54 ? 302 6YH B C13 1 
HETATM 8679 N  N14 . 6YH K  3 .   ? -9.838  13.700  5.756   1.00 48.03 ? 302 6YH B N14 1 
HETATM 8680 C  C18 . 6YH K  3 .   ? -10.138 14.436  6.863   1.00 48.10 ? 302 6YH B C18 1 
HETATM 8681 C  C20 . 6YH K  3 .   ? -9.939  14.152  8.231   1.00 43.59 ? 302 6YH B C20 1 
HETATM 8682 C  C21 . 6YH K  3 .   ? -10.340 15.142  9.174   1.00 52.33 ? 302 6YH B C21 1 
HETATM 8683 C  C22 . 6YH K  3 .   ? -10.948 16.358  8.734   1.00 48.78 ? 302 6YH B C22 1 
HETATM 8684 C  C23 . 6YH K  3 .   ? -11.141 16.616  7.350   1.00 52.60 ? 302 6YH B C23 1 
HETATM 8685 C  C19 . 6YH K  3 .   ? -10.715 15.622  6.442   1.00 56.61 ? 302 6YH B C19 1 
HETATM 8686 N  N17 . 6YH K  3 .   ? -10.783 15.637  5.077   1.00 55.36 ? 302 6YH B N17 1 
HETATM 8687 C  C16 . 6YH K  3 .   ? -10.248 14.442  4.674   1.00 55.96 ? 302 6YH B C16 1 
HETATM 8688 C  C1  . EDO L  4 .   ? -17.743 -3.789  21.437  1.00 23.49 ? 303 EDO B C1  1 
HETATM 8689 O  O1  . EDO L  4 .   ? -16.636 -3.646  20.449  1.00 27.76 ? 303 EDO B O1  1 
HETATM 8690 C  C2  . EDO L  4 .   ? -17.208 -3.686  22.827  1.00 29.67 ? 303 EDO B C2  1 
HETATM 8691 O  O2  . EDO L  4 .   ? -16.376 -2.525  22.956  1.00 31.06 ? 303 EDO B O2  1 
HETATM 8692 C  C1  . EDO M  4 .   ? -9.540  7.895   2.940   1.00 15.31 ? 304 EDO B C1  1 
HETATM 8693 O  O1  . EDO M  4 .   ? -10.645 8.346   2.172   1.00 18.61 ? 304 EDO B O1  1 
HETATM 8694 C  C2  . EDO M  4 .   ? -8.601  7.193   1.998   1.00 15.50 ? 304 EDO B C2  1 
HETATM 8695 O  O2  . EDO M  4 .   ? -7.834  8.165   1.263   1.00 17.33 ? 304 EDO B O2  1 
HETATM 8696 C  C1  . EDO N  4 .   ? -12.092 11.913  2.083   1.00 24.66 ? 305 EDO B C1  1 
HETATM 8697 O  O1  . EDO N  4 .   ? -11.113 10.944  2.558   1.00 25.72 ? 305 EDO B O1  1 
HETATM 8698 C  C2  . EDO N  4 .   ? -12.105 12.109  0.563   1.00 20.17 ? 305 EDO B C2  1 
HETATM 8699 O  O2  . EDO N  4 .   ? -11.679 13.497  0.428   1.00 29.74 ? 305 EDO B O2  1 
HETATM 8700 ZN ZN  . ZN  O  2 .   ? 37.595  2.530   -30.800 1.00 10.52 ? 301 ZN  C ZN  1 
HETATM 8701 O  O12 . 6YH P  3 .   ? 42.910  8.815   -33.488 1.00 43.03 ? 302 6YH C O12 1 
HETATM 8702 C  C11 . 6YH P  3 .   ? 42.137  8.762   -32.495 1.00 37.20 ? 302 6YH C C11 1 
HETATM 8703 C  C4  . 6YH P  3 .   ? 41.145  7.658   -32.515 1.00 30.88 ? 302 6YH C C4  1 
HETATM 8704 C  C3  . 6YH P  3 .   ? 39.873  7.688   -31.915 1.00 32.30 ? 302 6YH C C3  1 
HETATM 8705 C  C2  . 6YH P  3 .   ? 38.992  6.555   -32.082 1.00 28.12 ? 302 6YH C C2  1 
HETATM 8706 C  C5  . 6YH P  3 .   ? 41.518  6.595   -33.308 1.00 29.75 ? 302 6YH C C5  1 
HETATM 8707 C  C6  . 6YH P  3 .   ? 40.666  5.520   -33.529 1.00 27.06 ? 302 6YH C C6  1 
HETATM 8708 C  C1  . 6YH P  3 .   ? 39.429  5.531   -32.924 1.00 20.01 ? 302 6YH C C1  1 
HETATM 8709 S  S7  . 6YH P  3 .   ? 38.387  4.071   -33.231 1.00 16.66 ? 302 6YH C S7  1 
HETATM 8710 O  O9  . 6YH P  3 .   ? 37.658  4.231   -34.520 1.00 13.16 ? 302 6YH C O9  1 
HETATM 8711 N  N10 . 6YH P  3 .   ? 37.316  3.977   -32.014 1.00 13.19 ? 302 6YH C N10 1 
HETATM 8712 O  O8  . 6YH P  3 .   ? 39.356  2.938   -33.233 1.00 16.13 ? 302 6YH C O8  1 
HETATM 8713 C  C13 . 6YH P  3 .   ? 42.131  9.878   -31.476 1.00 46.70 ? 302 6YH C C13 1 
HETATM 8714 N  N14 . 6YH P  3 .   ? 43.046  10.968  -31.908 1.00 55.24 ? 302 6YH C N14 1 
HETATM 8715 C  C18 . 6YH P  3 .   ? 42.716  12.067  -32.634 1.00 52.70 ? 302 6YH C C18 1 
HETATM 8716 C  C20 . 6YH P  3 .   ? 41.463  12.489  -33.129 1.00 41.68 ? 302 6YH C C20 1 
HETATM 8717 C  C21 . 6YH P  3 .   ? 41.453  13.702  -33.855 1.00 40.24 ? 302 6YH C C21 1 
HETATM 8718 C  C22 . 6YH P  3 .   ? 42.632  14.471  -34.040 1.00 42.15 ? 302 6YH C C22 1 
HETATM 8719 C  C23 . 6YH P  3 .   ? 43.859  14.024  -33.537 1.00 41.67 ? 302 6YH C C23 1 
HETATM 8720 C  C19 . 6YH P  3 .   ? 43.875  12.806  -32.849 1.00 53.08 ? 302 6YH C C19 1 
HETATM 8721 N  N17 . 6YH P  3 .   ? 44.948  12.188  -32.297 1.00 50.07 ? 302 6YH C N17 1 
HETATM 8722 C  C16 . 6YH P  3 .   ? 44.417  11.060  -31.728 1.00 57.84 ? 302 6YH C C16 1 
HETATM 8723 C  C1  . EDO Q  4 .   ? 38.803  6.172   -28.338 1.00 38.15 ? 303 EDO C C1  1 
HETATM 8724 O  O1  . EDO Q  4 .   ? 37.900  6.903   -27.519 1.00 36.25 ? 303 EDO C O1  1 
HETATM 8725 C  C2  . EDO Q  4 .   ? 40.179  6.852   -28.495 1.00 32.31 ? 303 EDO C C2  1 
HETATM 8726 O  O2  . EDO Q  4 .   ? 40.771  6.778   -27.191 1.00 41.05 ? 303 EDO C O2  1 
HETATM 8727 C  C1  . EDO R  4 .   ? 42.145  11.895  -27.098 1.00 44.87 ? 304 EDO C C1  1 
HETATM 8728 O  O1  . EDO R  4 .   ? 42.441  11.502  -25.749 1.00 46.07 ? 304 EDO C O1  1 
HETATM 8729 C  C2  . EDO R  4 .   ? 42.636  10.735  -27.995 1.00 40.18 ? 304 EDO C C2  1 
HETATM 8730 O  O2  . EDO R  4 .   ? 41.616  9.719   -28.250 1.00 39.00 ? 304 EDO C O2  1 
HETATM 8731 ZN ZN  . ZN  S  2 .   ? 6.745   5.615   -38.365 1.00 7.20  ? 301 ZN  D ZN  1 
HETATM 8732 O  O12 A 6YH T  3 .   ? 4.499   13.679  -38.098 0.50 37.54 ? 302 6YH D O12 1 
HETATM 8733 O  O12 B 6YH T  3 .   ? 3.036   13.080  -35.344 0.50 18.62 ? 302 6YH D O12 1 
HETATM 8734 C  C11 A 6YH T  3 .   ? 4.009   12.982  -37.206 0.50 34.73 ? 302 6YH D C11 1 
HETATM 8735 C  C11 B 6YH T  3 .   ? 3.731   12.839  -36.347 0.50 18.69 ? 302 6YH D C11 1 
HETATM 8736 C  C4  A 6YH T  3 .   ? 4.658   11.653  -36.966 0.50 29.23 ? 302 6YH D C4  1 
HETATM 8737 C  C4  B 6YH T  3 .   ? 4.466   11.552  -36.385 0.50 16.45 ? 302 6YH D C4  1 
HETATM 8738 C  C3  A 6YH T  3 .   ? 3.899   10.635  -36.381 0.50 26.06 ? 302 6YH D C3  1 
HETATM 8739 C  C3  B 6YH T  3 .   ? 4.016   10.553  -35.519 0.50 16.43 ? 302 6YH D C3  1 
HETATM 8740 C  C2  A 6YH T  3 .   ? 4.478   9.400   -36.105 0.50 22.91 ? 302 6YH D C2  1 
HETATM 8741 C  C2  B 6YH T  3 .   ? 4.693   9.352   -35.450 0.50 13.39 ? 302 6YH D C2  1 
HETATM 8742 C  C5  A 6YH T  3 .   ? 6.019   11.424  -37.277 0.50 27.13 ? 302 6YH D C5  1 
HETATM 8743 C  C5  B 6YH T  3 .   ? 5.603   11.378  -37.194 0.50 16.11 ? 302 6YH D C5  1 
HETATM 8744 C  C6  A 6YH T  3 .   ? 6.588   10.158  -37.018 0.50 22.83 ? 302 6YH D C6  1 
HETATM 8745 C  C6  B 6YH T  3 .   ? 6.299   10.138  -37.130 0.50 14.44 ? 302 6YH D C6  1 
HETATM 8746 C  C1  A 6YH T  3 .   ? 5.824   9.166   -36.406 0.50 18.38 ? 302 6YH D C1  1 
HETATM 8747 C  C1  B 6YH T  3 .   ? 5.819   9.154   -36.267 0.50 11.38 ? 302 6YH D C1  1 
HETATM 8748 S  S7  A 6YH T  3 .   ? 6.503   7.515   -36.036 0.50 15.65 ? 302 6YH D S7  1 
HETATM 8749 S  S7  B 6YH T  3 .   ? 6.508   7.504   -36.029 0.50 10.20 ? 302 6YH D S7  1 
HETATM 8750 O  O9  A 6YH T  3 .   ? 7.405   7.610   -34.723 0.50 14.79 ? 302 6YH D O9  1 
HETATM 8751 O  O9  B 6YH T  3 .   ? 7.359   7.569   -34.771 0.50 8.55  ? 302 6YH D O9  1 
HETATM 8752 N  N10 A 6YH T  3 .   ? 7.396   7.101   -37.380 0.50 13.06 ? 302 6YH D N10 1 
HETATM 8753 N  N10 B 6YH T  3 .   ? 7.404   7.099   -37.316 0.50 8.38  ? 302 6YH D N10 1 
HETATM 8754 O  O8  A 6YH T  3 .   ? 5.290   6.611   -35.898 0.50 15.74 ? 302 6YH D O8  1 
HETATM 8755 O  O8  B 6YH T  3 .   ? 5.308   6.616   -35.902 0.50 9.58  ? 302 6YH D O8  1 
HETATM 8756 C  C13 A 6YH T  3 .   ? 2.828   13.394  -36.279 0.50 42.84 ? 302 6YH D C13 1 
HETATM 8757 C  C13 B 6YH T  3 .   ? 3.980   13.769  -37.500 0.50 18.86 ? 302 6YH D C13 1 
HETATM 8758 N  N14 A 6YH T  3 .   ? 2.402   14.818  -36.187 0.50 45.91 ? 302 6YH D N14 1 
HETATM 8759 N  N14 B 6YH T  3 .   ? 3.448   15.136  -37.296 0.50 19.35 ? 302 6YH D N14 1 
HETATM 8760 C  C18 A 6YH T  3 .   ? 3.236   15.889  -36.092 0.50 48.26 ? 302 6YH D C18 1 
HETATM 8761 C  C18 B 6YH T  3 .   ? 4.108   16.249  -36.899 0.50 19.95 ? 302 6YH D C18 1 
HETATM 8762 C  C20 A 6YH T  3 .   ? 4.643   15.920  -36.052 0.50 49.36 ? 302 6YH D C20 1 
HETATM 8763 C  C20 B 6YH T  3 .   ? 5.450   16.445  -36.587 0.50 18.54 ? 302 6YH D C20 1 
HETATM 8764 C  C21 A 6YH T  3 .   ? 5.260   17.188  -35.962 0.50 51.45 ? 302 6YH D C21 1 
HETATM 8765 C  C21 B 6YH T  3 .   ? 5.854   17.745  -36.224 0.50 19.59 ? 302 6YH D C21 1 
HETATM 8766 C  C22 A 6YH T  3 .   ? 4.474   18.379  -35.921 0.50 54.68 ? 302 6YH D C22 1 
HETATM 8767 C  C22 B 6YH T  3 .   ? 4.937   18.836  -36.159 0.50 18.21 ? 302 6YH D C22 1 
HETATM 8768 C  C23 A 6YH T  3 .   ? 3.062   18.311  -35.962 0.50 50.68 ? 302 6YH D C23 1 
HETATM 8769 C  C23 B 6YH T  3 .   ? 3.571   18.569  -36.426 0.50 17.07 ? 302 6YH D C23 1 
HETATM 8770 C  C19 A 6YH T  3 .   ? 2.483   17.036  -36.051 0.50 47.88 ? 302 6YH D C19 1 
HETATM 8771 C  C19 B 6YH T  3 .   ? 3.196   17.265  -36.784 0.50 17.09 ? 302 6YH D C19 1 
HETATM 8772 N  N17 A 6YH T  3 .   ? 1.167   16.713  -36.111 0.50 48.81 ? 302 6YH D N17 1 
HETATM 8773 N  N17 B 6YH T  3 .   ? 1.948   16.817  -37.133 0.50 17.47 ? 302 6YH D N17 1 
HETATM 8774 C  C16 A 6YH T  3 .   ? 1.136   15.342  -36.201 0.50 46.39 ? 302 6YH D C16 1 
HETATM 8775 C  C16 B 6YH T  3 .   ? 2.133   15.496  -37.415 0.50 19.77 ? 302 6YH D C16 1 
HETATM 8776 C  C1  . EDO U  4 .   ? -2.693  -1.339  -21.664 1.00 23.69 ? 303 EDO D C1  1 
HETATM 8777 O  O1  . EDO U  4 .   ? -1.643  -1.470  -22.687 1.00 23.53 ? 303 EDO D O1  1 
HETATM 8778 C  C2  . EDO U  4 .   ? -2.094  -1.121  -20.264 1.00 24.29 ? 303 EDO D C2  1 
HETATM 8779 O  O2  . EDO U  4 .   ? -1.135  -0.018  -20.253 1.00 31.31 ? 303 EDO D O2  1 
HETATM 8780 C  C1  . EDO V  4 .   ? 5.361   9.760   -40.530 1.00 18.12 ? 304 EDO D C1  1 
HETATM 8781 O  O1  . EDO V  4 .   ? 4.294   10.205  -41.317 1.00 20.45 ? 304 EDO D O1  1 
HETATM 8782 C  C2  . EDO V  4 .   ? 6.474   9.049   -41.303 1.00 19.15 ? 304 EDO D C2  1 
HETATM 8783 O  O2  . EDO V  4 .   ? 7.147   10.019  -42.160 1.00 20.30 ? 304 EDO D O2  1 
HETATM 8784 C  C1  A EDO W  4 .   ? 1.762   13.190  -40.909 0.50 26.22 ? 305 EDO D C1  1 
HETATM 8785 C  C1  B EDO W  4 .   ? 1.375   13.012  -40.414 0.50 22.83 ? 305 EDO D C1  1 
HETATM 8786 O  O1  A EDO W  4 .   ? 1.510   13.120  -39.477 0.50 32.76 ? 305 EDO D O1  1 
HETATM 8787 O  O1  B EDO W  4 .   ? 1.122   12.916  -38.957 0.50 20.46 ? 305 EDO D O1  1 
HETATM 8788 C  C2  A EDO W  4 .   ? 3.043   13.864  -41.465 0.50 20.16 ? 305 EDO D C2  1 
HETATM 8789 C  C2  B EDO W  4 .   ? 2.690   13.690  -40.949 0.50 22.52 ? 305 EDO D C2  1 
HETATM 8790 O  O2  A EDO W  4 .   ? 2.831   13.946  -42.887 0.50 20.42 ? 305 EDO D O2  1 
HETATM 8791 O  O2  B EDO W  4 .   ? 3.888   12.876  -40.825 0.50 19.58 ? 305 EDO D O2  1 
HETATM 8792 O  O   . HOH X  5 .   ? 4.766   -0.439  -8.397  1.00 29.58 ? 401 HOH A O   1 
HETATM 8793 O  O   . HOH X  5 .   ? 41.229  -4.306  0.547   1.00 33.68 ? 402 HOH A O   1 
HETATM 8794 O  O   . HOH X  5 .   ? 42.234  -0.178  5.983   1.00 31.67 ? 403 HOH A O   1 
HETATM 8795 O  O   . HOH X  5 .   ? 18.254  -3.230  -5.809  1.00 31.84 ? 404 HOH A O   1 
HETATM 8796 O  O   . HOH X  5 .   ? 5.976   -3.932  -7.984  1.00 35.38 ? 405 HOH A O   1 
HETATM 8797 O  O   . HOH X  5 .   ? 43.689  -4.344  13.007  1.00 26.18 ? 406 HOH A O   1 
HETATM 8798 O  O   . HOH X  5 .   ? 18.626  10.636  34.635  1.00 31.60 ? 407 HOH A O   1 
HETATM 8799 O  O   . HOH X  5 .   ? 27.858  -2.796  -6.390  1.00 35.98 ? 408 HOH A O   1 
HETATM 8800 O  O   . HOH X  5 .   ? 42.709  -10.157 19.158  1.00 29.46 ? 409 HOH A O   1 
HETATM 8801 O  O   . HOH X  5 .   ? 9.896   -14.700 1.569   1.00 27.57 ? 410 HOH A O   1 
HETATM 8802 O  O   . HOH X  5 .   ? 36.701  6.340   12.008  1.00 36.61 ? 411 HOH A O   1 
HETATM 8803 O  O   . HOH X  5 .   ? 10.827  12.505  20.328  1.00 24.13 ? 412 HOH A O   1 
HETATM 8804 O  O   . HOH X  5 .   ? 27.769  -21.741 1.759   1.00 35.53 ? 413 HOH A O   1 
HETATM 8805 O  O   . HOH X  5 .   ? 39.363  -12.723 19.994  1.00 25.25 ? 414 HOH A O   1 
HETATM 8806 O  O   . HOH X  5 .   ? 27.871  3.844   33.638  1.00 28.75 ? 415 HOH A O   1 
HETATM 8807 O  O   . HOH X  5 .   ? 37.194  7.524   29.892  1.00 30.57 ? 416 HOH A O   1 
HETATM 8808 O  O   . HOH X  5 .   ? 18.614  20.588  8.247   1.00 32.59 ? 417 HOH A O   1 
HETATM 8809 O  O   . HOH X  5 .   ? 11.766  2.158   -6.712  1.00 38.27 ? 418 HOH A O   1 
HETATM 8810 O  O   . HOH X  5 .   ? 38.049  -7.621  24.511  1.00 25.66 ? 419 HOH A O   1 
HETATM 8811 O  O   . HOH X  5 .   ? 33.544  -13.505 26.681  1.00 29.70 ? 420 HOH A O   1 
HETATM 8812 O  O   . HOH X  5 .   ? 19.677  13.989  28.268  1.00 29.11 ? 421 HOH A O   1 
HETATM 8813 O  O   . HOH X  5 .   ? 32.107  -16.959 20.677  1.00 30.80 ? 422 HOH A O   1 
HETATM 8814 O  O   . HOH X  5 .   ? 37.546  15.819  4.406   1.00 40.06 ? 423 HOH A O   1 
HETATM 8815 O  O   . HOH X  5 .   ? 12.678  -12.359 16.476  1.00 21.42 ? 424 HOH A O   1 
HETATM 8816 O  O   . HOH X  5 .   ? 14.240  -9.896  26.026  1.00 15.59 ? 425 HOH A O   1 
HETATM 8817 O  O   . HOH X  5 .   ? 7.742   -8.222  11.774  1.00 25.83 ? 426 HOH A O   1 
HETATM 8818 O  O   . HOH X  5 .   ? 10.953  -4.654  -5.247  1.00 37.45 ? 427 HOH A O   1 
HETATM 8819 O  O   . HOH X  5 .   ? 17.781  3.136   12.734  1.00 10.35 ? 428 HOH A O   1 
HETATM 8820 O  O   . HOH X  5 .   ? 34.280  3.602   31.631  1.00 33.51 ? 429 HOH A O   1 
HETATM 8821 O  O   . HOH X  5 .   ? 32.197  -16.903 10.176  1.00 34.16 ? 430 HOH A O   1 
HETATM 8822 O  O   . HOH X  5 .   ? 41.087  -10.337 9.887   1.00 20.59 ? 431 HOH A O   1 
HETATM 8823 O  O   . HOH X  5 .   ? 47.229  -3.622  10.315  1.00 31.05 ? 432 HOH A O   1 
HETATM 8824 O  O   . HOH X  5 .   ? 26.735  5.137   -3.818  1.00 30.21 ? 433 HOH A O   1 
HETATM 8825 O  O   . HOH X  5 .   ? 29.265  -16.963 14.814  1.00 27.51 ? 434 HOH A O   1 
HETATM 8826 O  O   . HOH X  5 .   ? 9.189   11.509  0.985   1.00 14.19 ? 435 HOH A O   1 
HETATM 8827 O  O   . HOH X  5 .   ? 18.012  -15.091 6.182   1.00 17.78 ? 436 HOH A O   1 
HETATM 8828 O  O   . HOH X  5 .   ? 13.839  1.640   -0.266  1.00 20.56 ? 437 HOH A O   1 
HETATM 8829 O  O   . HOH X  5 .   ? 10.261  4.719   8.773   1.00 12.20 ? 438 HOH A O   1 
HETATM 8830 O  O   . HOH X  5 .   ? 5.513   -12.105 13.320  1.00 20.60 ? 439 HOH A O   1 
HETATM 8831 O  O   . HOH X  5 .   ? 29.634  6.933   12.711  1.00 34.84 ? 440 HOH A O   1 
HETATM 8832 O  O   . HOH X  5 .   ? 13.645  16.455  11.868  1.00 17.32 ? 441 HOH A O   1 
HETATM 8833 O  O   . HOH X  5 .   ? 19.249  9.785   32.112  1.00 24.39 ? 442 HOH A O   1 
HETATM 8834 O  O   . HOH X  5 .   ? 15.131  -6.855  21.056  1.00 11.99 ? 443 HOH A O   1 
HETATM 8835 O  O   . HOH X  5 .   ? 45.172  -4.410  7.631   1.00 30.43 ? 444 HOH A O   1 
HETATM 8836 O  O   . HOH X  5 .   ? 10.433  -3.419  2.677   1.00 13.67 ? 445 HOH A O   1 
HETATM 8837 O  O   . HOH X  5 .   ? 6.411   15.895  15.578  1.00 36.18 ? 446 HOH A O   1 
HETATM 8838 O  O   . HOH X  5 .   ? 12.604  14.610  2.226   1.00 14.03 ? 447 HOH A O   1 
HETATM 8839 O  O   . HOH X  5 .   ? 32.796  5.042   20.306  1.00 24.14 ? 448 HOH A O   1 
HETATM 8840 O  O   . HOH X  5 .   ? 28.462  -4.174  2.561   1.00 12.32 ? 449 HOH A O   1 
HETATM 8841 O  O   . HOH X  5 .   ? 9.302   -5.150  16.613  1.00 36.53 ? 450 HOH A O   1 
HETATM 8842 O  O   . HOH X  5 .   ? 4.893   -9.210  25.674  1.00 27.64 ? 451 HOH A O   1 
HETATM 8843 O  O   . HOH X  5 .   ? 39.940  -12.071 11.795  1.00 24.85 ? 452 HOH A O   1 
HETATM 8844 O  O   . HOH X  5 .   ? 14.058  1.792   -2.987  1.00 25.06 ? 453 HOH A O   1 
HETATM 8845 O  O   . HOH X  5 .   ? 35.033  -11.180 -3.283  1.00 30.71 ? 454 HOH A O   1 
HETATM 8846 O  O   . HOH X  5 .   ? 27.628  -21.132 24.579  1.00 29.55 ? 455 HOH A O   1 
HETATM 8847 O  O   . HOH X  5 .   ? 23.009  -12.409 9.702   1.00 11.14 ? 456 HOH A O   1 
HETATM 8848 O  O   . HOH X  5 .   ? 13.181  14.131  14.060  1.00 22.60 ? 457 HOH A O   1 
HETATM 8849 O  O   . HOH X  5 .   ? 36.114  -7.026  26.385  1.00 22.19 ? 458 HOH A O   1 
HETATM 8850 O  O   . HOH X  5 .   ? 15.852  -11.947 26.934  1.00 20.85 ? 459 HOH A O   1 
HETATM 8851 O  O   . HOH X  5 .   ? 36.803  -4.408  -0.730  1.00 20.51 ? 460 HOH A O   1 
HETATM 8852 O  O   . HOH X  5 .   ? 20.410  -18.910 28.866  1.00 37.93 ? 461 HOH A O   1 
HETATM 8853 O  O   . HOH X  5 .   ? 11.056  3.357   19.098  1.00 24.94 ? 462 HOH A O   1 
HETATM 8854 O  O   . HOH X  5 .   ? 32.658  -0.037  -4.412  1.00 45.96 ? 463 HOH A O   1 
HETATM 8855 O  O   . HOH X  5 .   ? 19.407  14.134  5.107   1.00 12.91 ? 464 HOH A O   1 
HETATM 8856 O  O   . HOH X  5 .   ? 10.496  6.263   15.436  1.00 13.48 ? 465 HOH A O   1 
HETATM 8857 O  O   . HOH X  5 .   ? 11.903  -10.434 27.336  1.00 16.78 ? 466 HOH A O   1 
HETATM 8858 O  O   . HOH X  5 .   ? 34.363  1.271   -6.143  1.00 31.35 ? 467 HOH A O   1 
HETATM 8859 O  O   . HOH X  5 .   ? 35.003  -0.923  30.668  1.00 29.65 ? 468 HOH A O   1 
HETATM 8860 O  O   . HOH X  5 .   ? 38.896  -5.685  -3.028  1.00 23.82 ? 469 HOH A O   1 
HETATM 8861 O  O   . HOH X  5 .   ? 12.383  -2.667  10.986  1.00 9.77  ? 470 HOH A O   1 
HETATM 8862 O  O   . HOH X  5 .   ? 30.472  -8.831  -2.564  1.00 18.08 ? 471 HOH A O   1 
HETATM 8863 O  O   . HOH X  5 .   ? 24.230  -11.751 30.317  1.00 26.96 ? 472 HOH A O   1 
HETATM 8864 O  O   . HOH X  5 .   ? 11.332  5.281   2.158   1.00 11.72 ? 473 HOH A O   1 
HETATM 8865 O  O   . HOH X  5 .   ? 31.431  5.606   32.594  1.00 26.93 ? 474 HOH A O   1 
HETATM 8866 O  O   . HOH X  5 .   ? 39.033  -15.937 16.938  1.00 30.25 ? 475 HOH A O   1 
HETATM 8867 O  O   . HOH X  5 .   ? 18.315  12.548  20.636  1.00 36.18 ? 476 HOH A O   1 
HETATM 8868 O  O   . HOH X  5 .   ? 17.065  0.664   -0.506  1.00 18.28 ? 477 HOH A O   1 
HETATM 8869 O  O   . HOH X  5 .   ? 24.085  11.998  0.612   1.00 29.24 ? 478 HOH A O   1 
HETATM 8870 O  O   . HOH X  5 .   ? 42.110  2.326   1.050   1.00 16.92 ? 479 HOH A O   1 
HETATM 8871 O  O   . HOH X  5 .   ? 30.739  14.630  10.389  1.00 44.28 ? 480 HOH A O   1 
HETATM 8872 O  O   . HOH X  5 .   ? 9.465   16.985  14.866  1.00 34.68 ? 481 HOH A O   1 
HETATM 8873 O  O   . HOH X  5 .   ? 8.800   -6.464  7.434   1.00 20.14 ? 482 HOH A O   1 
HETATM 8874 O  O   . HOH X  5 .   ? 22.495  7.373   -4.173  1.00 28.92 ? 483 HOH A O   1 
HETATM 8875 O  O   . HOH X  5 .   ? 15.026  -16.005 14.995  1.00 22.25 ? 484 HOH A O   1 
HETATM 8876 O  O   . HOH X  5 .   ? 29.887  -15.546 -1.789  1.00 21.53 ? 485 HOH A O   1 
HETATM 8877 O  O   . HOH X  5 .   ? 5.322   16.076  13.594  1.00 27.50 ? 486 HOH A O   1 
HETATM 8878 O  O   . HOH X  5 .   ? 19.503  -0.518  26.638  1.00 14.67 ? 487 HOH A O   1 
HETATM 8879 O  O   . HOH X  5 .   ? 25.893  11.166  30.964  1.00 24.64 ? 488 HOH A O   1 
HETATM 8880 O  O   . HOH X  5 .   ? 23.789  -16.199 29.572  1.00 25.33 ? 489 HOH A O   1 
HETATM 8881 O  O   . HOH X  5 .   ? 25.643  -18.505 12.538  1.00 21.42 ? 490 HOH A O   1 
HETATM 8882 O  O   . HOH X  5 .   ? 19.353  -18.438 26.217  1.00 25.18 ? 491 HOH A O   1 
HETATM 8883 O  O   . HOH X  5 .   ? 42.579  5.380   -4.888  1.00 26.38 ? 492 HOH A O   1 
HETATM 8884 O  O   . HOH X  5 .   ? 18.864  11.900  -0.821  1.00 21.95 ? 493 HOH A O   1 
HETATM 8885 O  O   . HOH X  5 .   ? 6.005   -3.342  20.992  1.00 30.77 ? 494 HOH A O   1 
HETATM 8886 O  O   . HOH X  5 .   ? 33.061  -14.731 3.484   1.00 21.77 ? 495 HOH A O   1 
HETATM 8887 O  O   . HOH X  5 .   ? 28.623  2.269   -1.484  1.00 27.89 ? 496 HOH A O   1 
HETATM 8888 O  O   . HOH X  5 .   ? 31.150  -20.942 8.548   1.00 30.39 ? 497 HOH A O   1 
HETATM 8889 O  O   . HOH X  5 .   ? 38.932  2.195   -6.043  1.00 19.74 ? 498 HOH A O   1 
HETATM 8890 O  O   . HOH X  5 .   ? 11.028  -5.139  0.617   1.00 24.03 ? 499 HOH A O   1 
HETATM 8891 O  O   . HOH X  5 .   ? 20.665  17.726  7.599   1.00 32.01 ? 500 HOH A O   1 
HETATM 8892 O  O   . HOH X  5 .   ? 36.709  5.207   14.438  1.00 32.91 ? 501 HOH A O   1 
HETATM 8893 O  O   . HOH X  5 .   ? 7.348   4.994   11.182  1.00 10.54 ? 502 HOH A O   1 
HETATM 8894 O  O   . HOH X  5 .   ? 8.656   2.941   7.313   1.00 8.60  ? 503 HOH A O   1 
HETATM 8895 O  O   . HOH X  5 .   ? 10.052  -4.132  19.412  1.00 27.13 ? 504 HOH A O   1 
HETATM 8896 O  O   . HOH X  5 .   ? 31.399  -13.183 2.333   1.00 21.52 ? 505 HOH A O   1 
HETATM 8897 O  O   . HOH X  5 .   ? 11.029  11.182  8.059   1.00 10.09 ? 506 HOH A O   1 
HETATM 8898 O  O   . HOH X  5 .   ? 24.861  14.232  33.009  1.00 37.02 ? 507 HOH A O   1 
HETATM 8899 O  O   . HOH X  5 .   ? 20.718  4.063   16.440  1.00 19.42 ? 508 HOH A O   1 
HETATM 8900 O  O   . HOH X  5 .   ? 29.013  -14.948 16.966  1.00 18.88 ? 509 HOH A O   1 
HETATM 8901 O  O   . HOH X  5 .   ? 7.470   -6.720  2.439   1.00 23.76 ? 510 HOH A O   1 
HETATM 8902 O  O   . HOH X  5 .   ? 28.015  -21.295 15.070  1.00 44.70 ? 511 HOH A O   1 
HETATM 8903 O  O   . HOH X  5 .   ? 17.133  0.326   28.412  1.00 18.85 ? 512 HOH A O   1 
HETATM 8904 O  O   . HOH X  5 .   ? 11.465  1.480   -4.184  1.00 34.35 ? 513 HOH A O   1 
HETATM 8905 O  O   . HOH X  5 .   ? 17.641  9.612   0.114   1.00 11.37 ? 514 HOH A O   1 
HETATM 8906 O  O   . HOH X  5 .   ? 7.726   -1.715  15.307  1.00 27.65 ? 515 HOH A O   1 
HETATM 8907 O  O   . HOH X  5 .   ? 24.020  -22.216 18.531  1.00 37.95 ? 516 HOH A O   1 
HETATM 8908 O  O   . HOH X  5 .   ? 11.935  7.495   8.649   1.00 10.85 ? 517 HOH A O   1 
HETATM 8909 O  O   . HOH X  5 .   ? 11.856  -15.408 8.475   1.00 23.65 ? 518 HOH A O   1 
HETATM 8910 O  O   . HOH X  5 .   ? 20.567  -9.916  31.869  1.00 20.63 ? 519 HOH A O   1 
HETATM 8911 O  O   . HOH X  5 .   ? 12.083  5.048   28.854  1.00 37.43 ? 520 HOH A O   1 
HETATM 8912 O  O   . HOH X  5 .   ? 12.935  5.776   24.585  1.00 35.38 ? 521 HOH A O   1 
HETATM 8913 O  O   . HOH X  5 .   ? 8.038   -10.480 26.210  1.00 28.58 ? 522 HOH A O   1 
HETATM 8914 O  O   . HOH X  5 .   ? 32.551  -16.164 12.534  1.00 38.57 ? 523 HOH A O   1 
HETATM 8915 O  O   . HOH X  5 .   ? 39.674  -12.083 23.105  1.00 35.85 ? 524 HOH A O   1 
HETATM 8916 O  O   . HOH X  5 .   ? 19.896  -19.769 8.598   1.00 31.42 ? 525 HOH A O   1 
HETATM 8917 O  O   . HOH X  5 .   ? 27.411  -5.464  -5.237  1.00 22.55 ? 526 HOH A O   1 
HETATM 8918 O  O   . HOH X  5 .   ? 8.889   3.866   2.724   1.00 13.85 ? 527 HOH A O   1 
HETATM 8919 O  O   . HOH X  5 .   ? 38.557  4.164   11.508  1.00 26.23 ? 528 HOH A O   1 
HETATM 8920 O  O   . HOH X  5 .   ? 9.595   -5.374  -1.504  1.00 34.19 ? 529 HOH A O   1 
HETATM 8921 O  O   . HOH X  5 .   ? 26.008  -18.579 20.632  1.00 21.38 ? 530 HOH A O   1 
HETATM 8922 O  O   . HOH X  5 .   ? 13.650  -12.549 20.872  1.00 21.70 ? 531 HOH A O   1 
HETATM 8923 O  O   . HOH X  5 .   ? 15.903  -0.345  30.900  1.00 39.81 ? 532 HOH A O   1 
HETATM 8924 O  O   . HOH X  5 .   ? 14.165  4.424   -4.045  1.00 21.82 ? 533 HOH A O   1 
HETATM 8925 O  O   . HOH X  5 .   ? 43.488  -9.359  11.570  1.00 25.38 ? 534 HOH A O   1 
HETATM 8926 O  O   . HOH X  5 .   ? 26.025  -17.848 17.372  1.00 20.11 ? 535 HOH A O   1 
HETATM 8927 O  O   . HOH X  5 .   ? 20.764  -2.757  -5.301  1.00 26.11 ? 536 HOH A O   1 
HETATM 8928 O  O   . HOH X  5 .   ? 18.295  -15.704 34.074  1.00 27.21 ? 537 HOH A O   1 
HETATM 8929 O  O   . HOH X  5 .   ? 7.961   -12.879 -1.408  1.00 37.46 ? 538 HOH A O   1 
HETATM 8930 O  O   . HOH X  5 .   ? 11.522  8.016   1.698   1.00 12.58 ? 539 HOH A O   1 
HETATM 8931 O  O   . HOH X  5 .   ? 15.765  4.561   21.637  1.00 18.75 ? 540 HOH A O   1 
HETATM 8932 O  O   . HOH X  5 .   ? 11.261  9.702   -1.975  1.00 21.65 ? 541 HOH A O   1 
HETATM 8933 O  O   . HOH X  5 .   ? 17.492  8.041   19.812  1.00 21.64 ? 542 HOH A O   1 
HETATM 8934 O  O   . HOH X  5 .   ? 24.668  -7.262  -7.609  1.00 39.77 ? 543 HOH A O   1 
HETATM 8935 O  O   . HOH X  5 .   ? 32.382  7.620   30.845  1.00 20.13 ? 544 HOH A O   1 
HETATM 8936 O  O   . HOH X  5 .   ? 37.808  10.513  -5.061  1.00 28.29 ? 545 HOH A O   1 
HETATM 8937 O  O   . HOH X  5 .   ? 7.661   9.210   14.142  1.00 17.36 ? 546 HOH A O   1 
HETATM 8938 O  O   . HOH X  5 .   ? 16.708  -18.378 12.155  1.00 35.19 ? 547 HOH A O   1 
HETATM 8939 O  O   . HOH X  5 .   ? 12.261  -17.032 5.015   1.00 34.90 ? 548 HOH A O   1 
HETATM 8940 O  O   . HOH X  5 .   ? 17.181  -3.649  -8.495  1.00 35.38 ? 549 HOH A O   1 
HETATM 8941 O  O   . HOH X  5 .   ? 39.401  -3.747  -7.764  1.00 36.27 ? 550 HOH A O   1 
HETATM 8942 O  O   . HOH X  5 .   ? 9.574   -2.615  10.380  1.00 20.00 ? 551 HOH A O   1 
HETATM 8943 O  O   . HOH X  5 .   ? 8.432   -0.028  24.421  1.00 25.71 ? 552 HOH A O   1 
HETATM 8944 O  O   . HOH X  5 .   ? 16.498  10.915  -3.328  1.00 22.85 ? 553 HOH A O   1 
HETATM 8945 O  O   . HOH X  5 .   ? 25.596  -15.938 6.520   1.00 13.30 ? 554 HOH A O   1 
HETATM 8946 O  O   . HOH X  5 .   ? 9.080   -11.057 14.020  1.00 30.42 ? 555 HOH A O   1 
HETATM 8947 O  O   . HOH X  5 .   ? 22.000  -19.156 15.147  1.00 24.91 ? 556 HOH A O   1 
HETATM 8948 O  O   . HOH X  5 .   ? 29.749  11.787  -5.018  1.00 27.92 ? 557 HOH A O   1 
HETATM 8949 O  O   . HOH X  5 .   ? 6.690   -10.012 4.469   1.00 30.34 ? 558 HOH A O   1 
HETATM 8950 O  O   . HOH X  5 .   ? 45.323  1.558   21.970  1.00 37.13 ? 559 HOH A O   1 
HETATM 8951 O  O   . HOH X  5 .   ? 29.647  10.002  33.845  1.00 32.31 ? 560 HOH A O   1 
HETATM 8952 O  O   . HOH X  5 .   ? 23.271  3.243   -2.193  1.00 17.25 ? 561 HOH A O   1 
HETATM 8953 O  O   . HOH X  5 .   ? 17.382  -16.477 -8.155  1.00 35.39 ? 562 HOH A O   1 
HETATM 8954 O  O   . HOH X  5 .   ? 18.097  5.469   20.639  1.00 18.87 ? 563 HOH A O   1 
HETATM 8955 O  O   . HOH X  5 .   ? 24.039  -21.045 26.709  1.00 28.82 ? 564 HOH A O   1 
HETATM 8956 O  O   . HOH X  5 .   ? 9.047   2.116   -8.149  1.00 41.28 ? 565 HOH A O   1 
HETATM 8957 O  O   . HOH X  5 .   ? 45.789  1.545   12.916  1.00 36.14 ? 566 HOH A O   1 
HETATM 8958 O  O   . HOH X  5 .   ? 26.851  13.569  24.729  1.00 34.18 ? 567 HOH A O   1 
HETATM 8959 O  O   . HOH X  5 .   ? 31.431  -18.914 4.284   1.00 24.24 ? 568 HOH A O   1 
HETATM 8960 O  O   . HOH X  5 .   ? 15.067  -14.488 19.097  1.00 18.48 ? 569 HOH A O   1 
HETATM 8961 O  O   . HOH X  5 .   ? 7.367   -2.068  -0.860  1.00 24.24 ? 570 HOH A O   1 
HETATM 8962 O  O   . HOH X  5 .   ? 44.932  -4.136  15.538  1.00 32.90 ? 571 HOH A O   1 
HETATM 8963 O  O   . HOH X  5 .   ? 23.706  14.743  4.390   1.00 31.10 ? 572 HOH A O   1 
HETATM 8964 O  O   . HOH X  5 .   ? 23.477  -21.671 -3.374  1.00 32.29 ? 573 HOH A O   1 
HETATM 8965 O  O   . HOH X  5 .   ? 12.468  4.601   22.146  1.00 24.17 ? 574 HOH A O   1 
HETATM 8966 O  O   . HOH X  5 .   ? 44.119  -9.809  8.118   1.00 29.30 ? 575 HOH A O   1 
HETATM 8967 O  O   . HOH X  5 .   ? 16.720  -13.680 30.788  1.00 21.02 ? 576 HOH A O   1 
HETATM 8968 O  O   . HOH X  5 .   ? 25.483  10.998  -2.942  1.00 39.60 ? 577 HOH A O   1 
HETATM 8969 O  O   . HOH X  5 .   ? 18.489  16.309  15.357  1.00 44.49 ? 578 HOH A O   1 
HETATM 8970 O  O   . HOH X  5 .   ? 27.515  -4.699  31.388  1.00 30.50 ? 579 HOH A O   1 
HETATM 8971 O  O   . HOH X  5 .   ? 35.167  10.491  9.901   1.00 35.92 ? 580 HOH A O   1 
HETATM 8972 O  O   . HOH X  5 .   ? 45.980  -9.474  16.866  1.00 34.87 ? 581 HOH A O   1 
HETATM 8973 O  O   . HOH X  5 .   ? 14.839  7.200   21.115  1.00 23.08 ? 582 HOH A O   1 
HETATM 8974 O  O   . HOH X  5 .   ? 32.042  -2.701  -4.951  1.00 38.50 ? 583 HOH A O   1 
HETATM 8975 O  O   . HOH X  5 .   ? 13.172  5.084   -0.290  1.00 20.29 ? 584 HOH A O   1 
HETATM 8976 O  O   . HOH X  5 .   ? 38.038  -13.504 5.751   1.00 29.47 ? 585 HOH A O   1 
HETATM 8977 O  O   . HOH X  5 .   ? 32.167  -18.215 7.089   1.00 30.52 ? 586 HOH A O   1 
HETATM 8978 O  O   . HOH X  5 .   ? 10.004  3.290   22.152  1.00 25.68 ? 587 HOH A O   1 
HETATM 8979 O  O   . HOH X  5 .   ? 39.225  3.893   19.693  1.00 25.53 ? 588 HOH A O   1 
HETATM 8980 O  O   . HOH X  5 .   ? 27.355  -15.969 -5.667  1.00 27.41 ? 589 HOH A O   1 
HETATM 8981 O  O   . HOH X  5 .   ? 24.104  -15.374 -11.891 1.00 34.80 ? 590 HOH A O   1 
HETATM 8982 O  O   . HOH X  5 .   ? 38.318  -15.599 12.354  1.00 30.27 ? 591 HOH A O   1 
HETATM 8983 O  O   . HOH X  5 .   ? 17.827  10.075  21.814  1.00 31.30 ? 592 HOH A O   1 
HETATM 8984 O  O   . HOH X  5 .   ? 15.056  -17.222 19.438  1.00 33.09 ? 593 HOH A O   1 
HETATM 8985 O  O   . HOH X  5 .   ? 47.948  -9.338  25.387  1.00 40.18 ? 594 HOH A O   1 
HETATM 8986 O  O   . HOH X  5 .   ? 10.140  2.873   -2.497  1.00 33.78 ? 595 HOH A O   1 
HETATM 8987 O  O   . HOH X  5 .   ? 38.667  6.314   19.186  1.00 36.53 ? 596 HOH A O   1 
HETATM 8988 O  O   . HOH X  5 .   ? 14.163  -1.977  28.927  1.00 23.28 ? 597 HOH A O   1 
HETATM 8989 O  O   . HOH X  5 .   ? 7.298   -1.795  25.913  1.00 35.23 ? 598 HOH A O   1 
HETATM 8990 O  O   . HOH X  5 .   ? 6.216   -3.005  13.311  1.00 22.29 ? 599 HOH A O   1 
HETATM 8991 O  O   . HOH X  5 .   ? 45.159  -6.262  13.255  1.00 38.37 ? 600 HOH A O   1 
HETATM 8992 O  O   . HOH X  5 .   ? 7.411   -15.801 7.544   1.00 32.46 ? 601 HOH A O   1 
HETATM 8993 O  O   . HOH X  5 .   ? 15.037  -13.708 16.561  1.00 15.48 ? 602 HOH A O   1 
HETATM 8994 O  O   . HOH X  5 .   ? 33.299  15.784  5.847   1.00 58.18 ? 603 HOH A O   1 
HETATM 8995 O  O   . HOH X  5 .   ? 41.338  10.398  0.362   1.00 37.55 ? 604 HOH A O   1 
HETATM 8996 O  O   . HOH X  5 .   ? 36.333  1.539   30.649  1.00 35.29 ? 605 HOH A O   1 
HETATM 8997 O  O   . HOH X  5 .   ? 30.092  -2.623  32.992  1.00 42.76 ? 606 HOH A O   1 
HETATM 8998 O  O   . HOH X  5 .   ? 24.732  -28.635 -0.992  1.00 30.24 ? 607 HOH A O   1 
HETATM 8999 O  O   . HOH X  5 .   ? 40.366  -3.879  -2.070  1.00 35.32 ? 608 HOH A O   1 
HETATM 9000 O  O   . HOH X  5 .   ? 36.287  15.447  7.598   1.00 44.36 ? 609 HOH A O   1 
HETATM 9001 O  O   . HOH X  5 .   ? 23.212  12.165  13.071  1.00 43.55 ? 610 HOH A O   1 
HETATM 9002 O  O   . HOH X  5 .   ? 24.230  9.395   14.666  1.00 40.17 ? 611 HOH A O   1 
HETATM 9003 O  O   . HOH X  5 .   ? 28.307  -24.087 8.332   1.00 39.85 ? 612 HOH A O   1 
HETATM 9004 O  O   . HOH X  5 .   ? 20.119  -7.250  32.373  1.00 25.77 ? 613 HOH A O   1 
HETATM 9005 O  O   . HOH X  5 .   ? 30.488  10.605  15.335  1.00 42.55 ? 614 HOH A O   1 
HETATM 9006 O  O   . HOH X  5 .   ? 26.663  -19.448 -1.365  1.00 35.44 ? 615 HOH A O   1 
HETATM 9007 O  O   . HOH X  5 .   ? 17.568  -6.370  33.646  1.00 34.13 ? 616 HOH A O   1 
HETATM 9008 O  O   . HOH X  5 .   ? 37.148  7.856   9.596   1.00 37.69 ? 617 HOH A O   1 
HETATM 9009 O  O   . HOH X  5 .   ? 23.737  -19.564 16.678  1.00 28.33 ? 618 HOH A O   1 
HETATM 9010 O  O   . HOH X  5 .   ? 25.420  -24.484 23.789  1.00 39.15 ? 619 HOH A O   1 
HETATM 9011 O  O   . HOH X  5 .   ? 6.220   3.014   -7.570  1.00 43.97 ? 620 HOH A O   1 
HETATM 9012 O  O   . HOH X  5 .   ? 4.330   13.554  19.474  1.00 34.94 ? 621 HOH A O   1 
HETATM 9013 O  O   . HOH X  5 .   ? 45.650  1.807   8.165   1.00 36.03 ? 622 HOH A O   1 
HETATM 9014 O  O   . HOH X  5 .   ? 16.045  13.877  -0.792  1.00 39.57 ? 623 HOH A O   1 
HETATM 9015 O  O   . HOH X  5 .   ? 28.707  -18.664 20.615  1.00 22.02 ? 624 HOH A O   1 
HETATM 9016 O  O   . HOH X  5 .   ? 30.207  -17.554 18.629  1.00 30.49 ? 625 HOH A O   1 
HETATM 9017 O  O   . HOH X  5 .   ? 16.223  2.196   -7.882  1.00 35.18 ? 626 HOH A O   1 
HETATM 9018 O  O   . HOH X  5 .   ? 27.797  11.252  22.691  1.00 40.19 ? 627 HOH A O   1 
HETATM 9019 O  O   . HOH X  5 .   ? 8.193   2.103   -3.671  1.00 39.00 ? 628 HOH A O   1 
HETATM 9020 O  O   . HOH X  5 .   ? 31.474  -8.728  -4.639  1.00 36.35 ? 629 HOH A O   1 
HETATM 9021 O  O   . HOH X  5 .   ? 13.027  -14.620 12.812  1.00 29.16 ? 630 HOH A O   1 
HETATM 9022 O  O   . HOH X  5 .   ? 7.183   -5.917  5.123   1.00 27.47 ? 631 HOH A O   1 
HETATM 9023 O  O   . HOH X  5 .   ? 13.502  25.160  13.117  1.00 27.10 ? 632 HOH A O   1 
HETATM 9024 O  O   . HOH X  5 .   ? 10.053  -4.253  30.031  1.00 34.92 ? 633 HOH A O   1 
HETATM 9025 O  O   . HOH X  5 .   ? 21.449  -1.295  -7.764  1.00 44.26 ? 634 HOH A O   1 
HETATM 9026 O  O   . HOH X  5 .   ? 13.180  13.501  -2.051  1.00 36.98 ? 635 HOH A O   1 
HETATM 9027 O  O   . HOH X  5 .   ? 33.697  -17.433 2.915   1.00 32.77 ? 636 HOH A O   1 
HETATM 9028 O  O   . HOH X  5 .   ? 40.755  10.014  -5.364  1.00 39.19 ? 637 HOH A O   1 
HETATM 9029 O  O   . HOH X  5 .   ? 23.399  -4.094  -5.604  1.00 41.29 ? 638 HOH A O   1 
HETATM 9030 O  O   . HOH X  5 .   ? 11.822  -5.844  -10.202 1.00 38.97 ? 639 HOH A O   1 
HETATM 9031 O  O   . HOH X  5 .   ? 7.808   6.653   15.533  1.00 17.80 ? 640 HOH A O   1 
HETATM 9032 O  O   . HOH X  5 .   ? 14.360  -18.410 17.056  1.00 36.83 ? 641 HOH A O   1 
HETATM 9033 O  O   . HOH X  5 .   ? 42.144  -13.853 12.262  1.00 38.36 ? 642 HOH A O   1 
HETATM 9034 O  O   . HOH X  5 .   ? 23.266  -10.257 32.496  1.00 30.24 ? 643 HOH A O   1 
HETATM 9035 O  O   . HOH X  5 .   ? 23.584  11.198  -1.782  1.00 38.38 ? 644 HOH A O   1 
HETATM 9036 O  O   . HOH X  5 .   ? 29.805  -4.047  -5.325  1.00 45.53 ? 645 HOH A O   1 
HETATM 9037 O  O   . HOH X  5 .   ? 50.989  -9.315  26.928  1.00 42.04 ? 646 HOH A O   1 
HETATM 9038 O  O   . HOH X  5 .   ? 35.930  -16.315 24.626  1.00 44.23 ? 647 HOH A O   1 
HETATM 9039 O  O   . HOH X  5 .   ? 39.356  -9.741  24.835  1.00 39.17 ? 648 HOH A O   1 
HETATM 9040 O  O   . HOH X  5 .   ? 30.101  -2.851  35.595  1.00 32.91 ? 649 HOH A O   1 
HETATM 9041 O  O   . HOH X  5 .   ? 5.876   -0.512  -2.713  1.00 28.45 ? 650 HOH A O   1 
HETATM 9042 O  O   . HOH X  5 .   ? 26.166  14.295  35.787  1.00 37.12 ? 651 HOH A O   1 
HETATM 9043 O  O   . HOH X  5 .   ? 36.152  -2.552  36.711  1.00 26.69 ? 652 HOH A O   1 
HETATM 9044 O  O   . HOH X  5 .   ? 24.152  -21.116 11.277  1.00 39.49 ? 653 HOH A O   1 
HETATM 9045 O  O   . HOH X  5 .   ? 31.586  -17.074 -5.582  1.00 37.91 ? 654 HOH A O   1 
HETATM 9046 O  O   . HOH X  5 .   ? 16.404  -16.516 7.924   1.00 29.84 ? 655 HOH A O   1 
HETATM 9047 O  O   . HOH X  5 .   ? 14.559  -12.362 29.464  1.00 18.72 ? 656 HOH A O   1 
HETATM 9048 O  O   . HOH X  5 .   ? 11.425  5.444   -2.507  1.00 34.67 ? 657 HOH A O   1 
HETATM 9049 O  O   . HOH X  5 .   ? 24.835  -14.330 30.877  1.00 37.93 ? 658 HOH A O   1 
HETATM 9050 O  O   . HOH X  5 .   ? 32.301  -15.049 28.258  1.00 33.93 ? 659 HOH A O   1 
HETATM 9051 O  O   . HOH X  5 .   ? 30.274  -18.044 -2.763  1.00 30.04 ? 660 HOH A O   1 
HETATM 9052 O  O   . HOH X  5 .   ? 36.461  13.709  -1.310  1.00 31.33 ? 661 HOH A O   1 
HETATM 9053 O  O   . HOH X  5 .   ? 14.939  -14.051 25.383  1.00 33.31 ? 662 HOH A O   1 
HETATM 9054 O  O   . HOH X  5 .   ? 21.276  16.129  5.188   1.00 23.86 ? 663 HOH A O   1 
HETATM 9055 O  O   . HOH X  5 .   ? 4.532   13.484  22.533  1.00 38.12 ? 664 HOH A O   1 
HETATM 9056 O  O   . HOH X  5 .   ? 11.385  -12.946 26.043  1.00 25.70 ? 665 HOH A O   1 
HETATM 9057 O  O   . HOH X  5 .   ? 36.171  -14.399 26.777  1.00 39.74 ? 666 HOH A O   1 
HETATM 9058 O  O   . HOH X  5 .   ? 15.507  4.614   -6.671  1.00 37.53 ? 667 HOH A O   1 
HETATM 9059 O  O   . HOH X  5 .   ? 21.040  11.946  -2.757  1.00 28.04 ? 668 HOH A O   1 
HETATM 9060 O  O   . HOH X  5 .   ? 20.802  17.934  3.431   1.00 38.81 ? 669 HOH A O   1 
HETATM 9061 O  O   . HOH X  5 .   ? 13.770  -17.072 7.458   1.00 32.09 ? 670 HOH A O   1 
HETATM 9062 O  O   . HOH X  5 .   ? 19.082  10.267  -4.396  1.00 30.32 ? 671 HOH A O   1 
HETATM 9063 O  O   . HOH X  5 .   ? 22.883  16.363  8.475   1.00 37.77 ? 672 HOH A O   1 
HETATM 9064 O  O   . HOH X  5 .   ? 18.446  6.573   -6.762  1.00 36.44 ? 673 HOH A O   1 
HETATM 9065 O  O   . HOH Y  5 .   ? -13.633 -3.681  26.757  1.00 36.35 ? 401 HOH B O   1 
HETATM 9066 O  O   . HOH Y  5 .   ? -26.995 -6.128  6.886   1.00 21.93 ? 402 HOH B O   1 
HETATM 9067 O  O   . HOH Y  5 .   ? -17.951 7.713   20.821  1.00 37.39 ? 403 HOH B O   1 
HETATM 9068 O  O   . HOH Y  5 .   ? -12.071 -17.668 13.227  1.00 31.63 ? 404 HOH B O   1 
HETATM 9069 O  O   . HOH Y  5 .   ? -0.763  18.114  0.599   1.00 32.14 ? 405 HOH B O   1 
HETATM 9070 O  O   . HOH Y  5 .   ? 2.742   6.665   16.778  1.00 24.97 ? 406 HOH B O   1 
HETATM 9071 O  O   . HOH Y  5 .   ? -24.253 0.868   21.076  1.00 30.58 ? 407 HOH B O   1 
HETATM 9072 O  O   . HOH Y  5 .   ? -18.397 8.313   -13.730 1.00 33.50 ? 408 HOH B O   1 
HETATM 9073 O  O   . HOH Y  5 .   ? 3.303   1.173   -12.844 1.00 30.20 ? 409 HOH B O   1 
HETATM 9074 O  O   . HOH Y  5 .   ? 3.473   18.194  -15.646 1.00 35.73 ? 410 HOH B O   1 
HETATM 9075 O  O   . HOH Y  5 .   ? -21.429 -9.841  10.033  1.00 38.76 ? 411 HOH B O   1 
HETATM 9076 O  O   . HOH Y  5 .   ? -21.887 1.500   18.697  1.00 30.38 ? 412 HOH B O   1 
HETATM 9077 O  O   . HOH Y  5 .   ? -3.707  13.816  -7.094  1.00 25.22 ? 413 HOH B O   1 
HETATM 9078 O  O   . HOH Y  5 .   ? -24.086 -9.290  12.230  1.00 34.53 ? 414 HOH B O   1 
HETATM 9079 O  O   . HOH Y  5 .   ? -17.520 11.043  4.299   1.00 33.54 ? 415 HOH B O   1 
HETATM 9080 O  O   . HOH Y  5 .   ? -20.895 -11.238 5.633   1.00 38.13 ? 416 HOH B O   1 
HETATM 9081 O  O   . HOH Y  5 .   ? -19.917 -7.830  -11.523 1.00 31.97 ? 417 HOH B O   1 
HETATM 9082 O  O   . HOH Y  5 .   ? -13.646 7.564   -15.588 1.00 20.20 ? 418 HOH B O   1 
HETATM 9083 O  O   . HOH Y  5 .   ? 1.130   0.501   -16.034 1.00 26.98 ? 419 HOH B O   1 
HETATM 9084 O  O   . HOH Y  5 .   ? -23.350 -8.860  14.771  1.00 33.27 ? 420 HOH B O   1 
HETATM 9085 O  O   . HOH Y  5 .   ? -5.813  -11.672 -14.837 1.00 23.66 ? 421 HOH B O   1 
HETATM 9086 O  O   . HOH Y  5 .   ? -0.083  16.719  -11.091 1.00 19.44 ? 422 HOH B O   1 
HETATM 9087 O  O   . HOH Y  5 .   ? -2.624  5.123   4.001   1.00 9.31  ? 423 HOH B O   1 
HETATM 9088 O  O   . HOH Y  5 .   ? -27.148 -10.043 1.924   1.00 22.98 ? 424 HOH B O   1 
HETATM 9089 O  O   . HOH Y  5 .   ? -17.687 13.385  -4.484  1.00 30.80 ? 425 HOH B O   1 
HETATM 9090 O  O   . HOH Y  5 .   ? -3.521  19.143  -19.910 1.00 28.37 ? 426 HOH B O   1 
HETATM 9091 O  O   . HOH Y  5 .   ? 5.825   -9.441  13.388  1.00 18.94 ? 427 HOH B O   1 
HETATM 9092 O  O   . HOH Y  5 .   ? -27.199 -3.652  -5.779  1.00 27.19 ? 428 HOH B O   1 
HETATM 9093 O  O   . HOH Y  5 .   ? -29.893 -4.583  -0.440  1.00 20.91 ? 429 HOH B O   1 
HETATM 9094 O  O   . HOH Y  5 .   ? -14.010 -14.972 28.375  1.00 20.61 ? 430 HOH B O   1 
HETATM 9095 O  O   . HOH Y  5 .   ? -20.176 -12.093 8.406   1.00 26.81 ? 431 HOH B O   1 
HETATM 9096 O  O   . HOH Y  5 .   ? 7.133   -11.390 24.148  1.00 30.18 ? 432 HOH B O   1 
HETATM 9097 O  O   . HOH Y  5 .   ? 8.876   16.635  0.902   1.00 19.82 ? 433 HOH B O   1 
HETATM 9098 O  O   . HOH Y  5 .   ? -5.040  14.293  -4.569  1.00 31.69 ? 434 HOH B O   1 
HETATM 9099 O  O   . HOH Y  5 .   ? -27.554 -4.052  8.997   1.00 21.17 ? 435 HOH B O   1 
HETATM 9100 O  O   . HOH Y  5 .   ? 5.168   6.356   0.983   1.00 10.71 ? 436 HOH B O   1 
HETATM 9101 O  O   . HOH Y  5 .   ? -0.519  4.047   -16.723 1.00 23.79 ? 437 HOH B O   1 
HETATM 9102 O  O   . HOH Y  5 .   ? 1.707   6.574   -8.207  1.00 16.42 ? 438 HOH B O   1 
HETATM 9103 O  O   . HOH Y  5 .   ? 3.232   6.165   24.138  1.00 53.99 ? 439 HOH B O   1 
HETATM 9104 O  O   . HOH Y  5 .   ? -4.588  15.972  14.138  1.00 34.80 ? 440 HOH B O   1 
HETATM 9105 O  O   . HOH Y  5 .   ? -21.123 -5.012  21.910  1.00 25.56 ? 441 HOH B O   1 
HETATM 9106 O  O   . HOH Y  5 .   ? -2.963  -12.836 15.244  1.00 27.11 ? 442 HOH B O   1 
HETATM 9107 O  O   . HOH Y  5 .   ? -32.104 -6.384  6.088   1.00 27.52 ? 443 HOH B O   1 
HETATM 9108 O  O   . HOH Y  5 .   ? -14.677 -13.304 24.054  1.00 26.96 ? 444 HOH B O   1 
HETATM 9109 O  O   . HOH Y  5 .   ? -0.712  -14.536 13.470  1.00 35.55 ? 445 HOH B O   1 
HETATM 9110 O  O   . HOH Y  5 .   ? -13.141 -17.327 6.922   1.00 37.04 ? 446 HOH B O   1 
HETATM 9111 O  O   . HOH Y  5 .   ? 7.937   11.914  14.739  1.00 21.27 ? 447 HOH B O   1 
HETATM 9112 O  O   . HOH Y  5 .   ? -8.898  14.729  -2.182  1.00 29.72 ? 448 HOH B O   1 
HETATM 9113 O  O   . HOH Y  5 .   ? 1.064   18.100  -13.938 1.00 26.44 ? 449 HOH B O   1 
HETATM 9114 O  O   . HOH Y  5 .   ? -20.342 -12.193 -2.223  1.00 30.83 ? 450 HOH B O   1 
HETATM 9115 O  O   . HOH Y  5 .   ? -16.522 -12.265 25.675  1.00 26.97 ? 451 HOH B O   1 
HETATM 9116 O  O   . HOH Y  5 .   ? -7.212  10.481  2.426   1.00 22.30 ? 452 HOH B O   1 
HETATM 9117 O  O   . HOH Y  5 .   ? -5.867  -12.685 11.856  1.00 17.77 ? 453 HOH B O   1 
HETATM 9118 O  O   . HOH Y  5 .   ? -4.509  11.282  -14.919 1.00 14.93 ? 454 HOH B O   1 
HETATM 9119 O  O   . HOH Y  5 .   ? -17.450 -12.632 3.556   1.00 20.25 ? 455 HOH B O   1 
HETATM 9120 O  O   . HOH Y  5 .   ? -2.819  17.126  -1.369  1.00 45.31 ? 456 HOH B O   1 
HETATM 9121 O  O   . HOH Y  5 .   ? -23.658 -7.747  20.519  1.00 35.70 ? 457 HOH B O   1 
HETATM 9122 O  O   . HOH Y  5 .   ? -4.216  16.108  -11.207 1.00 14.02 ? 458 HOH B O   1 
HETATM 9123 O  O   . HOH Y  5 .   ? -5.954  -16.436 5.513   1.00 26.92 ? 459 HOH B O   1 
HETATM 9124 O  O   . HOH Y  5 .   ? -32.971 -1.703  -8.289  1.00 26.52 ? 460 HOH B O   1 
HETATM 9125 O  O   . HOH Y  5 .   ? -4.015  -17.700 22.429  1.00 19.32 ? 461 HOH B O   1 
HETATM 9126 O  O   . HOH Y  5 .   ? -17.764 -16.440 -6.296  1.00 22.53 ? 462 HOH B O   1 
HETATM 9127 O  O   . HOH Y  5 .   ? -29.374 2.442   5.825   1.00 21.91 ? 463 HOH B O   1 
HETATM 9128 O  O   . HOH Y  5 .   ? 3.753   -2.179  22.853  1.00 23.49 ? 464 HOH B O   1 
HETATM 9129 O  O   . HOH Y  5 .   ? 6.901   -11.475 17.323  1.00 27.85 ? 465 HOH B O   1 
HETATM 9130 O  O   . HOH Y  5 .   ? -13.860 8.070   26.881  1.00 39.01 ? 466 HOH B O   1 
HETATM 9131 O  O   . HOH Y  5 .   ? 9.120   7.183   8.405   1.00 14.91 ? 467 HOH B O   1 
HETATM 9132 O  O   . HOH Y  5 .   ? -26.597 9.100   -2.706  1.00 30.65 ? 468 HOH B O   1 
HETATM 9133 O  O   . HOH Y  5 .   ? -28.163 6.917   19.933  1.00 50.85 ? 469 HOH B O   1 
HETATM 9134 O  O   . HOH Y  5 .   ? -1.728  20.513  8.284   1.00 31.16 ? 470 HOH B O   1 
HETATM 9135 O  O   . HOH Y  5 .   ? 7.785   21.443  7.830   1.00 10.88 ? 471 HOH B O   1 
HETATM 9136 O  O   . HOH Y  5 .   ? -26.888 -7.400  11.001  1.00 35.86 ? 472 HOH B O   1 
HETATM 9137 O  O   . HOH Y  5 .   ? 5.711   12.452  -4.349  1.00 18.00 ? 473 HOH B O   1 
HETATM 9138 O  O   . HOH Y  5 .   ? -3.651  -8.583  -9.166  1.00 18.17 ? 474 HOH B O   1 
HETATM 9139 O  O   . HOH Y  5 .   ? -14.028 -14.759 5.912   1.00 19.03 ? 475 HOH B O   1 
HETATM 9140 O  O   . HOH Y  5 .   ? -13.938 0.381   15.186  1.00 16.69 ? 476 HOH B O   1 
HETATM 9141 O  O   . HOH Y  5 .   ? -2.899  -5.302  -4.124  1.00 10.06 ? 477 HOH B O   1 
HETATM 9142 O  O   . HOH Y  5 .   ? -27.173 3.495   -10.308 1.00 34.42 ? 478 HOH B O   1 
HETATM 9143 O  O   . HOH Y  5 .   ? -1.344  -6.664  30.644  1.00 37.84 ? 479 HOH B O   1 
HETATM 9144 O  O   . HOH Y  5 .   ? 1.378   14.456  -11.153 1.00 15.35 ? 480 HOH B O   1 
HETATM 9145 O  O   . HOH Y  5 .   ? -5.488  11.138  20.739  1.00 40.82 ? 481 HOH B O   1 
HETATM 9146 O  O   . HOH Y  5 .   ? 2.718   -13.376 15.816  1.00 21.76 ? 482 HOH B O   1 
HETATM 9147 O  O   . HOH Y  5 .   ? -8.122  -1.354  -15.762 1.00 29.82 ? 483 HOH B O   1 
HETATM 9148 O  O   . HOH Y  5 .   ? -19.078 6.457   23.623  1.00 32.82 ? 484 HOH B O   1 
HETATM 9149 O  O   . HOH Y  5 .   ? -17.048 11.245  1.861   1.00 30.53 ? 485 HOH B O   1 
HETATM 9150 O  O   . HOH Y  5 .   ? -21.941 -2.156  -12.519 1.00 29.92 ? 486 HOH B O   1 
HETATM 9151 O  O   . HOH Y  5 .   ? -26.493 8.708   16.495  1.00 37.55 ? 487 HOH B O   1 
HETATM 9152 O  O   . HOH Y  5 .   ? -3.850  12.520  -18.161 1.00 19.53 ? 488 HOH B O   1 
HETATM 9153 O  O   . HOH Y  5 .   ? -23.227 9.488   6.525   1.00 19.44 ? 489 HOH B O   1 
HETATM 9154 O  O   . HOH Y  5 .   ? -6.482  -11.365 29.104  1.00 27.78 ? 490 HOH B O   1 
HETATM 9155 O  O   . HOH Y  5 .   ? 4.707   -5.900  8.778   1.00 26.06 ? 491 HOH B O   1 
HETATM 9156 O  O   . HOH Y  5 .   ? 3.755   3.483   -2.450  1.00 16.49 ? 492 HOH B O   1 
HETATM 9157 O  O   . HOH Y  5 .   ? -21.896 -8.766  -8.374  1.00 18.65 ? 493 HOH B O   1 
HETATM 9158 O  O   . HOH Y  5 .   ? -17.880 -10.147 28.566  1.00 23.16 ? 494 HOH B O   1 
HETATM 9159 O  O   . HOH Y  5 .   ? -35.383 7.027   2.886   1.00 29.95 ? 495 HOH B O   1 
HETATM 9160 O  O   . HOH Y  5 .   ? 4.900   -9.640  -12.165 1.00 24.03 ? 496 HOH B O   1 
HETATM 9161 O  O   . HOH Y  5 .   ? -17.027 -10.771 1.322   1.00 13.93 ? 497 HOH B O   1 
HETATM 9162 O  O   . HOH Y  5 .   ? -1.481  14.027  -4.418  1.00 25.72 ? 498 HOH B O   1 
HETATM 9163 O  O   . HOH Y  5 .   ? 3.695   -2.159  13.864  1.00 14.01 ? 499 HOH B O   1 
HETATM 9164 O  O   . HOH Y  5 .   ? 5.331   5.528   7.643   1.00 11.29 ? 500 HOH B O   1 
HETATM 9165 O  O   . HOH Y  5 .   ? -12.402 -13.542 -11.267 1.00 16.37 ? 501 HOH B O   1 
HETATM 9166 O  O   . HOH Y  5 .   ? -24.734 -2.465  -6.394  1.00 15.00 ? 502 HOH B O   1 
HETATM 9167 O  O   . HOH Y  5 .   ? -6.346  -18.188 -2.145  1.00 25.32 ? 503 HOH B O   1 
HETATM 9168 O  O   . HOH Y  5 .   ? -10.315 -8.934  8.212   1.00 8.97  ? 504 HOH B O   1 
HETATM 9169 O  O   . HOH Y  5 .   ? -26.773 -7.079  -1.436  1.00 23.27 ? 505 HOH B O   1 
HETATM 9170 O  O   . HOH Y  5 .   ? -18.427 -8.135  16.036  1.00 16.74 ? 506 HOH B O   1 
HETATM 9171 O  O   . HOH Y  5 .   ? 4.409   6.451   14.199  1.00 13.40 ? 507 HOH B O   1 
HETATM 9172 O  O   . HOH Y  5 .   ? 6.598   0.475   22.311  1.00 24.68 ? 508 HOH B O   1 
HETATM 9173 O  O   . HOH Y  5 .   ? -5.572  1.575   -9.905  1.00 10.08 ? 509 HOH B O   1 
HETATM 9174 O  O   . HOH Y  5 .   ? 8.089   4.619   5.155   1.00 9.82  ? 510 HOH B O   1 
HETATM 9175 O  O   . HOH Y  5 .   ? 3.227   5.281   16.244  1.00 18.79 ? 511 HOH B O   1 
HETATM 9176 O  O   . HOH Y  5 .   ? 4.640   17.052  3.386   1.00 23.05 ? 512 HOH B O   1 
HETATM 9177 O  O   . HOH Y  5 .   ? 4.210   10.036  -6.739  1.00 17.03 ? 513 HOH B O   1 
HETATM 9178 O  O   . HOH Y  5 .   ? 1.695   -1.577  5.806   1.00 8.74  ? 514 HOH B O   1 
HETATM 9179 O  O   . HOH Y  5 .   ? -17.888 9.219   -2.591  1.00 16.23 ? 515 HOH B O   1 
HETATM 9180 O  O   . HOH Y  5 .   ? -9.098  -7.867  -14.474 1.00 15.23 ? 516 HOH B O   1 
HETATM 9181 O  O   . HOH Y  5 .   ? 5.458   19.900  10.747  1.00 20.25 ? 517 HOH B O   1 
HETATM 9182 O  O   . HOH Y  5 .   ? -4.233  -19.215 18.087  1.00 27.01 ? 518 HOH B O   1 
HETATM 9183 O  O   . HOH Y  5 .   ? -23.052 -2.201  -8.653  1.00 15.50 ? 519 HOH B O   1 
HETATM 9184 O  O   . HOH Y  5 .   ? -1.076  5.819   -4.943  1.00 11.13 ? 520 HOH B O   1 
HETATM 9185 O  O   . HOH Y  5 .   ? -17.083 -10.418 20.255  1.00 15.51 ? 521 HOH B O   1 
HETATM 9186 O  O   . HOH Y  5 .   ? -0.843  15.961  -8.608  1.00 25.05 ? 522 HOH B O   1 
HETATM 9187 O  O   . HOH Y  5 .   ? -7.985  -19.778 25.137  1.00 38.72 ? 523 HOH B O   1 
HETATM 9188 O  O   . HOH Y  5 .   ? -10.544 14.328  -13.559 1.00 16.98 ? 524 HOH B O   1 
HETATM 9189 O  O   . HOH Y  5 .   ? -26.223 -9.859  6.221   1.00 30.25 ? 525 HOH B O   1 
HETATM 9190 O  O   . HOH Y  5 .   ? -7.352  -7.424  28.443  1.00 27.68 ? 526 HOH B O   1 
HETATM 9191 O  O   . HOH Y  5 .   ? 6.595   3.333   9.094   1.00 8.96  ? 527 HOH B O   1 
HETATM 9192 O  O   . HOH Y  5 .   ? 6.027   11.706  7.883   1.00 10.11 ? 528 HOH B O   1 
HETATM 9193 O  O   . HOH Y  5 .   ? -14.654 -14.211 19.900  1.00 30.98 ? 529 HOH B O   1 
HETATM 9194 O  O   . HOH Y  5 .   ? -4.489  0.274   21.873  1.00 18.35 ? 530 HOH B O   1 
HETATM 9195 O  O   . HOH Y  5 .   ? -1.958  -11.396 -3.084  1.00 15.21 ? 531 HOH B O   1 
HETATM 9196 O  O   . HOH Y  5 .   ? -20.518 -9.471  15.030  1.00 19.85 ? 532 HOH B O   1 
HETATM 9197 O  O   . HOH Y  5 .   ? -5.220  18.061  -7.409  1.00 33.08 ? 533 HOH B O   1 
HETATM 9198 O  O   . HOH Y  5 .   ? -15.971 -0.361  -14.893 1.00 24.65 ? 534 HOH B O   1 
HETATM 9199 O  O   . HOH Y  5 .   ? -16.911 -16.757 16.813  1.00 34.64 ? 535 HOH B O   1 
HETATM 9200 O  O   . HOH Y  5 .   ? -1.597  16.664  11.031  1.00 12.50 ? 536 HOH B O   1 
HETATM 9201 O  O   . HOH Y  5 .   ? 2.852   15.380  -5.311  1.00 37.55 ? 537 HOH B O   1 
HETATM 9202 O  O   . HOH Y  5 .   ? -14.482 13.977  -16.044 1.00 29.74 ? 538 HOH B O   1 
HETATM 9203 O  O   . HOH Y  5 .   ? -4.844  -12.708 22.170  1.00 30.14 ? 539 HOH B O   1 
HETATM 9204 O  O   . HOH Y  5 .   ? -26.678 10.465  5.051   1.00 28.72 ? 540 HOH B O   1 
HETATM 9205 O  O   . HOH Y  5 .   ? -6.080  2.414   -16.801 1.00 27.66 ? 541 HOH B O   1 
HETATM 9206 O  O   . HOH Y  5 .   ? -1.440  14.524  17.017  1.00 22.74 ? 542 HOH B O   1 
HETATM 9207 O  O   . HOH Y  5 .   ? -5.568  15.721  -0.941  1.00 37.00 ? 543 HOH B O   1 
HETATM 9208 O  O   . HOH Y  5 .   ? 9.221   7.070   -2.146  1.00 29.90 ? 544 HOH B O   1 
HETATM 9209 O  O   . HOH Y  5 .   ? 1.353   13.082  19.562  1.00 25.33 ? 545 HOH B O   1 
HETATM 9210 O  O   . HOH Y  5 .   ? -5.569  6.589   0.481   1.00 11.98 ? 546 HOH B O   1 
HETATM 9211 O  O   . HOH Y  5 .   ? -10.154 -3.074  24.720  1.00 44.08 ? 547 HOH B O   1 
HETATM 9212 O  O   . HOH Y  5 .   ? -31.921 5.337   -7.509  1.00 20.93 ? 548 HOH B O   1 
HETATM 9213 O  O   . HOH Y  5 .   ? -0.281  -13.276 22.645  1.00 31.48 ? 549 HOH B O   1 
HETATM 9214 O  O   . HOH Y  5 .   ? -26.583 9.692   12.207  1.00 43.33 ? 550 HOH B O   1 
HETATM 9215 O  O   . HOH Y  5 .   ? 4.976   9.187   14.294  1.00 13.77 ? 551 HOH B O   1 
HETATM 9216 O  O   . HOH Y  5 .   ? -27.405 6.974   -11.692 1.00 22.92 ? 552 HOH B O   1 
HETATM 9217 O  O   . HOH Y  5 .   ? 1.635   8.980   -6.830  1.00 12.92 ? 553 HOH B O   1 
HETATM 9218 O  O   . HOH Y  5 .   ? -19.779 -16.062 10.209  1.00 26.56 ? 554 HOH B O   1 
HETATM 9219 O  O   . HOH Y  5 .   ? -0.552  -0.092  26.884  1.00 32.13 ? 555 HOH B O   1 
HETATM 9220 O  O   . HOH Y  5 .   ? -14.314 -2.252  -13.706 1.00 25.90 ? 556 HOH B O   1 
HETATM 9221 O  O   . HOH Y  5 .   ? -9.710  7.570   19.727  1.00 39.03 ? 557 HOH B O   1 
HETATM 9222 O  O   . HOH Y  5 .   ? -10.692 17.270  -7.802  1.00 30.49 ? 558 HOH B O   1 
HETATM 9223 O  O   . HOH Y  5 .   ? -5.125  -14.998 -12.667 1.00 38.16 ? 559 HOH B O   1 
HETATM 9224 O  O   . HOH Y  5 .   ? -3.494  2.207   -11.920 1.00 11.78 ? 560 HOH B O   1 
HETATM 9225 O  O   . HOH Y  5 .   ? -3.145  7.182   -3.806  1.00 10.66 ? 561 HOH B O   1 
HETATM 9226 O  O   . HOH Y  5 .   ? -25.545 -7.133  13.462  1.00 23.58 ? 562 HOH B O   1 
HETATM 9227 O  O   . HOH Y  5 .   ? -0.527  11.987  16.246  1.00 14.33 ? 563 HOH B O   1 
HETATM 9228 O  O   . HOH Y  5 .   ? 3.986   -9.330  3.041   1.00 20.88 ? 564 HOH B O   1 
HETATM 9229 O  O   . HOH Y  5 .   ? -13.585 -6.888  -11.288 1.00 23.63 ? 565 HOH B O   1 
HETATM 9230 O  O   . HOH Y  5 .   ? 7.139   -0.793  17.953  1.00 19.93 ? 566 HOH B O   1 
HETATM 9231 O  O   . HOH Y  5 .   ? -1.425  18.266  14.437  1.00 37.45 ? 567 HOH B O   1 
HETATM 9232 O  O   . HOH Y  5 .   ? -16.807 9.830   -14.884 1.00 37.76 ? 568 HOH B O   1 
HETATM 9233 O  O   . HOH Y  5 .   ? -1.226  -0.592  -12.667 1.00 17.34 ? 569 HOH B O   1 
HETATM 9234 O  O   . HOH Y  5 .   ? 5.582   -8.291  -1.340  1.00 25.03 ? 570 HOH B O   1 
HETATM 9235 O  O   . HOH Y  5 .   ? 6.554   4.828   13.754  1.00 12.68 ? 571 HOH B O   1 
HETATM 9236 O  O   . HOH Y  5 .   ? -17.569 -16.647 3.434   1.00 42.27 ? 572 HOH B O   1 
HETATM 9237 O  O   . HOH Y  5 .   ? 5.942   -6.119  14.601  1.00 23.37 ? 573 HOH B O   1 
HETATM 9238 O  O   . HOH Y  5 .   ? -12.958 -19.461 16.062  1.00 39.79 ? 574 HOH B O   1 
HETATM 9239 O  O   . HOH Y  5 .   ? 0.234   -14.043 8.758   1.00 38.46 ? 575 HOH B O   1 
HETATM 9240 O  O   . HOH Y  5 .   ? 0.543   8.130   -4.455  1.00 14.84 ? 576 HOH B O   1 
HETATM 9241 O  O   . HOH Y  5 .   ? 4.376   3.326   -5.839  1.00 19.46 ? 577 HOH B O   1 
HETATM 9242 O  O   . HOH Y  5 .   ? 4.215   8.194   7.688   1.00 9.85  ? 578 HOH B O   1 
HETATM 9243 O  O   . HOH Y  5 .   ? -32.490 -3.984  -1.708  1.00 26.49 ? 579 HOH B O   1 
HETATM 9244 O  O   . HOH Y  5 .   ? 2.233   5.148   -5.666  1.00 17.41 ? 580 HOH B O   1 
HETATM 9245 O  O   . HOH Y  5 .   ? -1.858  9.544   -3.283  1.00 15.15 ? 581 HOH B O   1 
HETATM 9246 O  O   . HOH Y  5 .   ? -33.628 3.018   2.629   1.00 29.94 ? 582 HOH B O   1 
HETATM 9247 O  O   . HOH Y  5 .   ? -2.703  -0.287  25.252  1.00 23.43 ? 583 HOH B O   1 
HETATM 9248 O  O   . HOH Y  5 .   ? 4.378   -2.093  6.479   1.00 14.69 ? 584 HOH B O   1 
HETATM 9249 O  O   . HOH Y  5 .   ? -24.265 8.933   -1.647  1.00 19.43 ? 585 HOH B O   1 
HETATM 9250 O  O   . HOH Y  5 .   ? -3.486  -2.933  29.143  1.00 31.14 ? 586 HOH B O   1 
HETATM 9251 O  O   . HOH Y  5 .   ? -1.490  -9.774  -10.107 1.00 20.10 ? 587 HOH B O   1 
HETATM 9252 O  O   . HOH Y  5 .   ? -10.555 -10.511 29.650  1.00 21.91 ? 588 HOH B O   1 
HETATM 9253 O  O   . HOH Y  5 .   ? -6.059  -15.433 13.084  1.00 24.28 ? 589 HOH B O   1 
HETATM 9254 O  O   . HOH Y  5 .   ? -13.391 -11.999 11.688  1.00 11.44 ? 590 HOH B O   1 
HETATM 9255 O  O   . HOH Y  5 .   ? 4.058   11.217  -13.269 1.00 30.04 ? 591 HOH B O   1 
HETATM 9256 O  O   . HOH Y  5 .   ? 3.806   -16.169 18.091  1.00 37.47 ? 592 HOH B O   1 
HETATM 9257 O  O   . HOH Y  5 .   ? -11.197 -15.902 3.242   1.00 31.13 ? 593 HOH B O   1 
HETATM 9258 O  O   . HOH Y  5 .   ? 4.194   -2.472  -3.357  1.00 31.61 ? 594 HOH B O   1 
HETATM 9259 O  O   . HOH Y  5 .   ? -12.616 -0.624  22.852  1.00 23.57 ? 595 HOH B O   1 
HETATM 9260 O  O   . HOH Y  5 .   ? 8.752   8.826   1.879   1.00 16.70 ? 596 HOH B O   1 
HETATM 9261 O  O   . HOH Y  5 .   ? -23.269 11.465  -1.037  1.00 22.11 ? 597 HOH B O   1 
HETATM 9262 O  O   . HOH Y  5 .   ? 3.993   -15.080 9.901   1.00 35.86 ? 598 HOH B O   1 
HETATM 9263 O  O   . HOH Y  5 .   ? -22.756 5.969   -12.370 1.00 20.61 ? 599 HOH B O   1 
HETATM 9264 O  O   . HOH Y  5 .   ? 2.311   6.150   -12.367 1.00 20.61 ? 600 HOH B O   1 
HETATM 9265 O  O   . HOH Y  5 .   ? -16.110 -5.794  -12.705 1.00 28.23 ? 601 HOH B O   1 
HETATM 9266 O  O   . HOH Y  5 .   ? -2.753  1.603   -14.654 1.00 21.68 ? 602 HOH B O   1 
HETATM 9267 O  O   . HOH Y  5 .   ? -3.353  -12.372 -0.796  1.00 19.46 ? 603 HOH B O   1 
HETATM 9268 O  O   . HOH Y  5 .   ? -17.591 12.618  -12.636 1.00 27.78 ? 604 HOH B O   1 
HETATM 9269 O  O   . HOH Y  5 .   ? -30.823 7.214   -4.134  1.00 23.23 ? 605 HOH B O   1 
HETATM 9270 O  O   . HOH Y  5 .   ? -29.406 7.310   -1.646  1.00 30.54 ? 606 HOH B O   1 
HETATM 9271 O  O   . HOH Y  5 .   ? -14.672 -14.046 0.794   1.00 17.84 ? 607 HOH B O   1 
HETATM 9272 O  O   . HOH Y  5 .   ? -14.318 -10.892 23.821  1.00 30.73 ? 608 HOH B O   1 
HETATM 9273 O  O   . HOH Y  5 .   ? -4.547  -16.421 15.356  1.00 37.94 ? 609 HOH B O   1 
HETATM 9274 O  O   . HOH Y  5 .   ? -29.816 -3.041  7.425   1.00 23.21 ? 610 HOH B O   1 
HETATM 9275 O  O   . HOH Y  5 .   ? 4.123   -5.081  -0.464  1.00 28.42 ? 611 HOH B O   1 
HETATM 9276 O  O   . HOH Y  5 .   ? -4.306  -13.093 25.836  1.00 25.32 ? 612 HOH B O   1 
HETATM 9277 O  O   . HOH Y  5 .   ? -30.957 2.106   2.179   1.00 23.69 ? 613 HOH B O   1 
HETATM 9278 O  O   . HOH Y  5 .   ? -13.909 11.158  4.559   1.00 29.39 ? 614 HOH B O   1 
HETATM 9279 O  O   . HOH Y  5 .   ? 3.506   15.226  1.619   1.00 28.56 ? 615 HOH B O   1 
HETATM 9280 O  O   . HOH Y  5 .   ? -0.242  21.239  0.222   1.00 39.91 ? 616 HOH B O   1 
HETATM 9281 O  O   . HOH Y  5 .   ? 0.426   3.861   24.527  1.00 38.48 ? 617 HOH B O   1 
HETATM 9282 O  O   . HOH Y  5 .   ? 8.428   4.195   19.688  1.00 31.73 ? 618 HOH B O   1 
HETATM 9283 O  O   . HOH Y  5 .   ? -19.621 -13.670 14.469  1.00 20.92 ? 619 HOH B O   1 
HETATM 9284 O  O   . HOH Y  5 .   ? -7.174  6.995   19.206  1.00 23.60 ? 620 HOH B O   1 
HETATM 9285 O  O   . HOH Y  5 .   ? -9.621  16.830  -15.859 1.00 23.24 ? 621 HOH B O   1 
HETATM 9286 O  O   . HOH Y  5 .   ? -11.266 -17.765 20.965  1.00 42.06 ? 622 HOH B O   1 
HETATM 9287 O  O   . HOH Y  5 .   ? -5.799  15.624  2.249   1.00 36.85 ? 623 HOH B O   1 
HETATM 9288 O  O   . HOH Y  5 .   ? -2.149  11.716  -5.054  1.00 18.04 ? 624 HOH B O   1 
HETATM 9289 O  O   . HOH Y  5 .   ? 2.321   7.229   -14.954 1.00 36.14 ? 625 HOH B O   1 
HETATM 9290 O  O   . HOH Y  5 .   ? 7.872   -6.955  16.766  1.00 27.16 ? 626 HOH B O   1 
HETATM 9291 O  O   . HOH Y  5 .   ? -34.841 -2.704  -2.063  1.00 31.14 ? 627 HOH B O   1 
HETATM 9292 O  O   . HOH Y  5 .   ? 6.177   7.587   17.508  1.00 33.22 ? 628 HOH B O   1 
HETATM 9293 O  O   . HOH Y  5 .   ? 3.423   21.383  9.575   1.00 21.21 ? 629 HOH B O   1 
HETATM 9294 O  O   . HOH Y  5 .   ? -14.986 -14.697 -2.562  1.00 16.94 ? 630 HOH B O   1 
HETATM 9295 O  O   . HOH Y  5 .   ? -8.012  -16.324 -10.533 1.00 29.92 ? 631 HOH B O   1 
HETATM 9296 O  O   . HOH Y  5 .   ? -20.317 -13.224 11.579  1.00 33.40 ? 632 HOH B O   1 
HETATM 9297 O  O   . HOH Y  5 .   ? -2.685  -10.644 -14.790 1.00 28.80 ? 633 HOH B O   1 
HETATM 9298 O  O   . HOH Y  5 .   ? 1.462   -0.413  -12.203 1.00 28.82 ? 634 HOH B O   1 
HETATM 9299 O  O   . HOH Y  5 .   ? -20.080 12.882  7.616   1.00 30.42 ? 635 HOH B O   1 
HETATM 9300 O  O   . HOH Y  5 .   ? 4.061   14.712  -10.962 1.00 33.33 ? 636 HOH B O   1 
HETATM 9301 O  O   . HOH Y  5 .   ? 5.928   -2.534  1.663   1.00 30.99 ? 637 HOH B O   1 
HETATM 9302 O  O   . HOH Y  5 .   ? 7.721   -3.406  3.473   1.00 20.84 ? 638 HOH B O   1 
HETATM 9303 O  O   . HOH Y  5 .   ? -0.744  -12.725 15.398  1.00 33.87 ? 639 HOH B O   1 
HETATM 9304 O  O   . HOH Y  5 .   ? -24.728 -1.106  -11.461 1.00 22.30 ? 640 HOH B O   1 
HETATM 9305 O  O   . HOH Y  5 .   ? 7.554   1.332   19.838  1.00 22.32 ? 641 HOH B O   1 
HETATM 9306 O  O   . HOH Y  5 .   ? 11.554  14.672  -0.219  1.00 32.66 ? 642 HOH B O   1 
HETATM 9307 O  O   . HOH Y  5 .   ? -8.477  17.775  -3.612  1.00 40.71 ? 643 HOH B O   1 
HETATM 9308 O  O   . HOH Y  5 .   ? -29.000 9.803   -6.406  1.00 46.14 ? 644 HOH B O   1 
HETATM 9309 O  O   . HOH Y  5 .   ? -27.555 -5.963  -4.652  1.00 34.97 ? 645 HOH B O   1 
HETATM 9310 O  O   . HOH Y  5 .   ? -12.091 -19.880 24.504  1.00 33.47 ? 646 HOH B O   1 
HETATM 9311 O  O   . HOH Y  5 .   ? -30.225 4.796   2.672   1.00 32.33 ? 647 HOH B O   1 
HETATM 9312 O  O   . HOH Y  5 .   ? -21.456 -6.487  -9.821  1.00 28.93 ? 648 HOH B O   1 
HETATM 9313 O  O   . HOH Y  5 .   ? -29.822 8.639   6.188   1.00 38.37 ? 649 HOH B O   1 
HETATM 9314 O  O   . HOH Y  5 .   ? -3.737  -15.084 23.065  1.00 43.76 ? 650 HOH B O   1 
HETATM 9315 O  O   . HOH Y  5 .   ? 1.764   16.008  16.709  1.00 42.14 ? 651 HOH B O   1 
HETATM 9316 O  O   . HOH Y  5 .   ? -9.195  1.763   -19.470 1.00 32.53 ? 652 HOH B O   1 
HETATM 9317 O  O   . HOH Y  5 .   ? -13.697 13.505  -2.467  1.00 40.96 ? 653 HOH B O   1 
HETATM 9318 O  O   . HOH Y  5 .   ? -9.670  -18.320 12.841  1.00 39.98 ? 654 HOH B O   1 
HETATM 9319 O  O   . HOH Y  5 .   ? -9.921  20.159  -8.515  1.00 45.30 ? 655 HOH B O   1 
HETATM 9320 O  O   . HOH Y  5 .   ? -23.817 -10.894 5.111   1.00 45.07 ? 656 HOH B O   1 
HETATM 9321 O  O   . HOH Y  5 .   ? -0.162  -13.156 -4.416  1.00 25.47 ? 657 HOH B O   1 
HETATM 9322 O  O   . HOH Y  5 .   ? 12.335  11.452  -3.713  1.00 30.51 ? 658 HOH B O   1 
HETATM 9323 O  O   . HOH Y  5 .   ? 5.348   13.886  -6.339  1.00 37.56 ? 659 HOH B O   1 
HETATM 9324 O  O   . HOH Y  5 .   ? -20.307 -3.919  26.236  1.00 35.26 ? 660 HOH B O   1 
HETATM 9325 O  O   . HOH Y  5 .   ? 7.573   7.592   -0.074  1.00 23.58 ? 661 HOH B O   1 
HETATM 9326 O  O   . HOH Y  5 .   ? -17.555 -14.295 -2.259  1.00 29.39 ? 662 HOH B O   1 
HETATM 9327 O  O   . HOH Y  5 .   ? -10.780 15.123  -5.070  1.00 39.12 ? 663 HOH B O   1 
HETATM 9328 O  O   . HOH Y  5 .   ? -12.980 14.235  -4.863  1.00 38.82 ? 664 HOH B O   1 
HETATM 9329 O  O   . HOH Y  5 .   ? -23.365 -4.535  -10.116 1.00 29.70 ? 665 HOH B O   1 
HETATM 9330 O  O   . HOH Y  5 .   ? -18.318 -13.774 -0.072  1.00 38.41 ? 666 HOH B O   1 
HETATM 9331 O  O   . HOH Y  5 .   ? -8.139  -5.482  -15.505 1.00 25.96 ? 667 HOH B O   1 
HETATM 9332 O  O   . HOH Y  5 .   ? -12.791 -9.131  -12.574 1.00 27.70 ? 668 HOH B O   1 
HETATM 9333 O  O   . HOH Y  5 .   ? 6.355   -5.665  11.228  1.00 30.95 ? 669 HOH B O   1 
HETATM 9334 O  O   . HOH Y  5 .   ? 5.882   2.283   -3.633  1.00 31.39 ? 670 HOH B O   1 
HETATM 9335 O  O   . HOH Y  5 .   ? 5.063   12.116  -11.255 1.00 38.53 ? 671 HOH B O   1 
HETATM 9336 O  O   . HOH Y  5 .   ? -23.660 16.928  21.808  1.00 40.27 ? 672 HOH B O   1 
HETATM 9337 O  O   . HOH Y  5 .   ? 7.969   10.780  -7.572  1.00 33.52 ? 673 HOH B O   1 
HETATM 9338 O  O   . HOH Y  5 .   ? 7.822   5.906   0.705   1.00 21.56 ? 674 HOH B O   1 
HETATM 9339 O  O   . HOH Y  5 .   ? 1.943   -15.767 16.614  1.00 31.57 ? 675 HOH B O   1 
HETATM 9340 O  O   . HOH Y  5 .   ? -29.182 -7.447  6.848   1.00 30.59 ? 676 HOH B O   1 
HETATM 9341 O  O   . HOH Y  5 .   ? 2.735   -11.121 -11.457 1.00 38.83 ? 677 HOH B O   1 
HETATM 9342 O  O   . HOH Y  5 .   ? -28.425 -9.953  -4.121  1.00 42.46 ? 678 HOH B O   1 
HETATM 9343 O  O   . HOH Y  5 .   ? 4.413   -11.977 24.629  1.00 39.55 ? 679 HOH B O   1 
HETATM 9344 O  O   . HOH Y  5 .   ? -11.623 -8.284  -14.917 1.00 26.81 ? 680 HOH B O   1 
HETATM 9345 O  O   . HOH Y  5 .   ? -17.258 9.295   23.758  1.00 37.57 ? 681 HOH B O   1 
HETATM 9346 O  O   . HOH Y  5 .   ? 7.576   -9.440  15.644  1.00 20.13 ? 682 HOH B O   1 
HETATM 9347 O  O   . HOH Y  5 .   ? -21.456 -12.080 15.874  1.00 27.78 ? 683 HOH B O   1 
HETATM 9348 O  O   . HOH Y  5 .   ? -19.172 -16.381 -3.838  1.00 31.05 ? 684 HOH B O   1 
HETATM 9349 O  O   . HOH Y  5 .   ? -3.737  16.301  -8.637  1.00 26.54 ? 685 HOH B O   1 
HETATM 9350 O  O   . HOH Y  5 .   ? -16.873 -14.191 27.727  1.00 25.44 ? 686 HOH B O   1 
HETATM 9351 O  O   . HOH Y  5 .   ? 2.573   -11.546 -8.293  1.00 37.93 ? 687 HOH B O   1 
HETATM 9352 O  O   . HOH Y  5 .   ? 1.229   22.812  10.449  1.00 26.06 ? 688 HOH B O   1 
HETATM 9353 O  O   . HOH Y  5 .   ? -29.457 7.191   1.141   1.00 33.13 ? 689 HOH B O   1 
HETATM 9354 O  O   . HOH Y  5 .   ? 5.405   -13.025 15.837  1.00 26.63 ? 690 HOH B O   1 
HETATM 9355 O  O   . HOH Y  5 .   ? -15.709 -14.562 3.522   1.00 24.87 ? 691 HOH B O   1 
HETATM 9356 O  O   . HOH Y  5 .   ? -22.714 -12.413 1.340   1.00 35.48 ? 692 HOH B O   1 
HETATM 9357 O  O   . HOH Y  5 .   ? -1.290  21.870  10.650  1.00 32.27 ? 693 HOH B O   1 
HETATM 9358 O  O   . HOH Y  5 .   ? -4.554  -13.740 9.566   1.00 31.73 ? 694 HOH B O   1 
HETATM 9359 O  O   . HOH Y  5 .   ? -3.395  15.321  18.436  1.00 31.27 ? 695 HOH B O   1 
HETATM 9360 O  O   . HOH Y  5 .   ? -3.338  -17.426 19.911  1.00 25.91 ? 696 HOH B O   1 
HETATM 9361 O  O   . HOH Y  5 .   ? 5.051   -7.330  1.202   1.00 18.95 ? 697 HOH B O   1 
HETATM 9362 O  O   . HOH Y  5 .   ? -17.881 -12.672 21.366  1.00 25.66 ? 698 HOH B O   1 
HETATM 9363 O  O   . HOH Y  5 .   ? -0.548  -12.027 -8.958  1.00 20.82 ? 699 HOH B O   1 
HETATM 9364 O  O   . HOH Y  5 .   ? -11.040 17.038  -18.550 1.00 38.01 ? 700 HOH B O   1 
HETATM 9365 O  O   . HOH Y  5 .   ? -29.304 -6.268  -2.537  1.00 34.17 ? 701 HOH B O   1 
HETATM 9366 O  O   . HOH Y  5 .   ? 10.723  9.449   -6.774  1.00 46.74 ? 702 HOH B O   1 
HETATM 9367 O  O   . HOH Y  5 .   ? -18.683 -11.951 23.805  1.00 34.43 ? 703 HOH B O   1 
HETATM 9368 O  O   . HOH Y  5 .   ? -16.034 14.643  -13.751 1.00 40.90 ? 704 HOH B O   1 
HETATM 9369 O  O   . HOH Y  5 .   ? -0.832  24.086  7.015   1.00 38.22 ? 705 HOH B O   1 
HETATM 9370 O  O   . HOH Y  5 .   ? -20.975 -10.830 -9.943  1.00 24.31 ? 706 HOH B O   1 
HETATM 9371 O  O   . HOH Y  5 .   ? -3.966  1.782   24.132  1.00 29.90 ? 707 HOH B O   1 
HETATM 9372 O  O   . HOH Y  5 .   ? -27.465 8.904   1.384   1.00 41.92 ? 708 HOH B O   1 
HETATM 9373 O  O   . HOH Y  5 .   ? 5.560   9.687   -9.081  1.00 33.79 ? 709 HOH B O   1 
HETATM 9374 O  O   . HOH Y  5 .   ? -2.986  18.969  10.827  1.00 26.31 ? 710 HOH B O   1 
HETATM 9375 O  O   . HOH Y  5 .   ? -1.668  20.291  13.289  1.00 35.16 ? 711 HOH B O   1 
HETATM 9376 O  O   . HOH Y  5 .   ? 3.847   6.271   -9.810  1.00 28.38 ? 712 HOH B O   1 
HETATM 9377 O  O   . HOH Y  5 .   ? -12.935 -14.285 30.870  1.00 20.91 ? 713 HOH B O   1 
HETATM 9378 O  O   . HOH Y  5 .   ? -19.004 -16.168 15.405  1.00 33.40 ? 714 HOH B O   1 
HETATM 9379 O  O   . HOH Y  5 .   ? -7.795  -9.936  -15.906 1.00 17.89 ? 715 HOH B O   1 
HETATM 9380 O  O   . HOH Y  5 .   ? -2.062  -15.361 10.972  1.00 34.85 ? 716 HOH B O   1 
HETATM 9381 O  O   . HOH Y  5 .   ? -10.384 -13.151 30.553  1.00 24.45 ? 717 HOH B O   1 
HETATM 9382 O  O   . HOH Y  5 .   ? -1.015  -14.275 6.337   1.00 35.75 ? 718 HOH B O   1 
HETATM 9383 O  O   . HOH Y  5 .   ? 12.826  11.569  -6.272  1.00 35.00 ? 719 HOH B O   1 
HETATM 9384 O  O   . HOH Y  5 .   ? -9.810  -11.383 -17.156 1.00 34.81 ? 720 HOH B O   1 
HETATM 9385 O  O   . HOH Y  5 .   ? -2.988  4.284   24.032  1.00 42.28 ? 721 HOH B O   1 
HETATM 9386 O  O   . HOH Y  5 .   ? -21.956 -13.457 -9.441  1.00 36.51 ? 722 HOH B O   1 
HETATM 9387 O  O   . HOH Y  5 .   ? -21.745 -13.659 18.139  1.00 38.31 ? 723 HOH B O   1 
HETATM 9388 O  O   . HOH Y  5 .   ? -19.918 -14.289 20.354  1.00 30.32 ? 724 HOH B O   1 
HETATM 9389 O  O   . HOH Z  5 .   ? 56.398  3.798   -12.841 1.00 17.04 ? 401 HOH C O   1 
HETATM 9390 O  O   . HOH Z  5 .   ? 62.073  4.395   -31.978 1.00 39.27 ? 402 HOH C O   1 
HETATM 9391 O  O   . HOH Z  5 .   ? 19.699  1.115   -51.556 1.00 26.89 ? 403 HOH C O   1 
HETATM 9392 O  O   . HOH Z  5 .   ? 36.190  -9.740  -53.490 1.00 29.32 ? 404 HOH C O   1 
HETATM 9393 O  O   . HOH Z  5 .   ? 27.364  25.060  -32.245 1.00 17.07 ? 405 HOH C O   1 
HETATM 9394 O  O   . HOH Z  5 .   ? 22.359  -8.844  -39.614 1.00 26.70 ? 406 HOH C O   1 
HETATM 9395 O  O   . HOH Z  5 .   ? 33.099  12.831  -8.548  1.00 39.38 ? 407 HOH C O   1 
HETATM 9396 O  O   . HOH Z  5 .   ? 20.742  -2.079  -50.833 1.00 28.91 ? 408 HOH C O   1 
HETATM 9397 O  O   . HOH Z  5 .   ? 32.665  -19.545 -49.799 1.00 33.23 ? 409 HOH C O   1 
HETATM 9398 O  O   . HOH Z  5 .   ? 47.350  -1.631  -9.510  1.00 29.36 ? 410 HOH C O   1 
HETATM 9399 O  O   . HOH Z  5 .   ? 37.570  16.753  -30.171 1.00 37.38 ? 411 HOH C O   1 
HETATM 9400 O  O   . HOH Z  5 .   ? 56.349  8.033   -37.485 1.00 31.35 ? 412 HOH C O   1 
HETATM 9401 O  O   . HOH Z  5 .   ? 33.766  -18.280 -41.418 1.00 39.66 ? 413 HOH C O   1 
HETATM 9402 O  O   . HOH Z  5 .   ? 47.617  -13.719 -29.256 1.00 39.55 ? 414 HOH C O   1 
HETATM 9403 O  O   . HOH Z  5 .   ? 22.412  -6.388  -31.397 1.00 24.09 ? 415 HOH C O   1 
HETATM 9404 O  O   . HOH Z  5 .   ? 33.300  -1.756  -48.977 1.00 21.72 ? 416 HOH C O   1 
HETATM 9405 O  O   . HOH Z  5 .   ? 47.149  8.939   -27.172 1.00 25.47 ? 417 HOH C O   1 
HETATM 9406 O  O   . HOH Z  5 .   ? 58.537  -1.896  -29.687 1.00 28.70 ? 418 HOH C O   1 
HETATM 9407 O  O   . HOH Z  5 .   ? 26.318  -8.314  -15.875 1.00 28.23 ? 419 HOH C O   1 
HETATM 9408 O  O   . HOH Z  5 .   ? 41.957  6.941   -9.863  1.00 37.31 ? 420 HOH C O   1 
HETATM 9409 O  O   . HOH Z  5 .   ? 44.002  -5.763  -50.061 1.00 25.09 ? 421 HOH C O   1 
HETATM 9410 O  O   . HOH Z  5 .   ? 39.099  -19.849 -45.909 1.00 33.19 ? 422 HOH C O   1 
HETATM 9411 O  O   . HOH Z  5 .   ? 38.589  10.244  -31.428 1.00 29.49 ? 423 HOH C O   1 
HETATM 9412 O  O   . HOH Z  5 .   ? 38.819  -2.813  -11.303 1.00 31.18 ? 424 HOH C O   1 
HETATM 9413 O  O   . HOH Z  5 .   ? 38.567  -14.426 -13.326 1.00 44.59 ? 425 HOH C O   1 
HETATM 9414 O  O   . HOH Z  5 .   ? 28.538  18.263  -31.590 1.00 16.99 ? 426 HOH C O   1 
HETATM 9415 O  O   . HOH Z  5 .   ? 35.762  -13.739 -54.328 1.00 22.35 ? 427 HOH C O   1 
HETATM 9416 O  O   . HOH Z  5 .   ? 44.015  -14.871 -27.782 1.00 34.35 ? 428 HOH C O   1 
HETATM 9417 O  O   . HOH Z  5 .   ? 59.094  -7.831  -21.243 1.00 46.59 ? 429 HOH C O   1 
HETATM 9418 O  O   . HOH Z  5 .   ? 50.814  -4.542  -54.155 1.00 33.92 ? 430 HOH C O   1 
HETATM 9419 O  O   . HOH Z  5 .   ? 32.538  5.063   -30.433 1.00 12.46 ? 431 HOH C O   1 
HETATM 9420 O  O   . HOH Z  5 .   ? 54.131  -6.912  -17.994 1.00 38.13 ? 432 HOH C O   1 
HETATM 9421 O  O   . HOH Z  5 .   ? 52.906  4.731   -48.775 1.00 28.26 ? 433 HOH C O   1 
HETATM 9422 O  O   . HOH Z  5 .   ? 52.484  1.351   -12.831 1.00 35.25 ? 434 HOH C O   1 
HETATM 9423 O  O   . HOH Z  5 .   ? 33.444  12.126  -11.073 1.00 26.27 ? 435 HOH C O   1 
HETATM 9424 O  O   . HOH Z  5 .   ? 28.038  15.845  -29.401 1.00 24.04 ? 436 HOH C O   1 
HETATM 9425 O  O   . HOH Z  5 .   ? 27.376  -10.374 -26.593 1.00 22.49 ? 437 HOH C O   1 
HETATM 9426 O  O   . HOH Z  5 .   ? 59.224  3.255   -20.315 1.00 36.34 ? 438 HOH C O   1 
HETATM 9427 O  O   . HOH Z  5 .   ? 27.505  7.626   -18.684 1.00 32.45 ? 439 HOH C O   1 
HETATM 9428 O  O   . HOH Z  5 .   ? 25.867  5.414   -24.027 1.00 27.51 ? 440 HOH C O   1 
HETATM 9429 O  O   . HOH Z  5 .   ? 49.061  1.833   -12.362 1.00 38.29 ? 441 HOH C O   1 
HETATM 9430 O  O   . HOH Z  5 .   ? 42.113  -18.141 -53.335 1.00 30.20 ? 442 HOH C O   1 
HETATM 9431 O  O   . HOH Z  5 .   ? 37.728  14.139  -28.797 1.00 38.58 ? 443 HOH C O   1 
HETATM 9432 O  O   . HOH Z  5 .   ? 46.492  8.073   -11.329 1.00 22.97 ? 444 HOH C O   1 
HETATM 9433 O  O   . HOH Z  5 .   ? 28.632  -7.726  -16.829 1.00 21.28 ? 445 HOH C O   1 
HETATM 9434 O  O   . HOH Z  5 .   ? 25.339  8.209   -27.953 1.00 15.28 ? 446 HOH C O   1 
HETATM 9435 O  O   . HOH Z  5 .   ? 51.737  -2.468  -43.470 1.00 24.45 ? 447 HOH C O   1 
HETATM 9436 O  O   . HOH Z  5 .   ? 24.737  -13.118 -41.386 1.00 24.43 ? 448 HOH C O   1 
HETATM 9437 O  O   . HOH Z  5 .   ? 43.465  -1.357  -10.588 1.00 32.95 ? 449 HOH C O   1 
HETATM 9438 O  O   . HOH Z  5 .   ? 44.720  -14.832 -50.062 1.00 32.45 ? 450 HOH C O   1 
HETATM 9439 O  O   . HOH Z  5 .   ? 23.955  8.919   -34.942 1.00 13.32 ? 451 HOH C O   1 
HETATM 9440 O  O   . HOH Z  5 .   ? 35.601  -21.346 -50.995 1.00 27.38 ? 452 HOH C O   1 
HETATM 9441 O  O   . HOH Z  5 .   ? 53.984  -13.309 -25.425 1.00 31.65 ? 453 HOH C O   1 
HETATM 9442 O  O   . HOH Z  5 .   ? 22.110  -1.015  -23.621 1.00 26.58 ? 454 HOH C O   1 
HETATM 9443 O  O   . HOH Z  5 .   ? 48.771  -12.996 -33.823 1.00 34.94 ? 455 HOH C O   1 
HETATM 9444 O  O   . HOH Z  5 .   ? 29.656  -4.831  -21.973 1.00 15.14 ? 456 HOH C O   1 
HETATM 9445 O  O   . HOH Z  5 .   ? 56.633  8.982   -40.079 1.00 30.82 ? 457 HOH C O   1 
HETATM 9446 O  O   . HOH Z  5 .   ? 48.246  -10.806 -15.856 1.00 31.86 ? 458 HOH C O   1 
HETATM 9447 O  O   . HOH Z  5 .   ? 46.997  11.483  -21.502 1.00 41.47 ? 459 HOH C O   1 
HETATM 9448 O  O   . HOH Z  5 .   ? 25.359  -1.788  -40.567 1.00 12.63 ? 460 HOH C O   1 
HETATM 9449 O  O   . HOH Z  5 .   ? 26.122  5.417   -43.459 1.00 27.71 ? 461 HOH C O   1 
HETATM 9450 O  O   . HOH Z  5 .   ? 45.220  16.728  -38.720 1.00 36.63 ? 462 HOH C O   1 
HETATM 9451 O  O   . HOH Z  5 .   ? 53.785  -10.100 -22.204 1.00 27.21 ? 463 HOH C O   1 
HETATM 9452 O  O   . HOH Z  5 .   ? 28.652  3.317   -43.447 1.00 15.96 ? 464 HOH C O   1 
HETATM 9453 O  O   . HOH Z  5 .   ? 48.050  -12.884 -39.100 1.00 27.64 ? 465 HOH C O   1 
HETATM 9454 O  O   . HOH Z  5 .   ? 51.398  8.383   -31.051 1.00 30.66 ? 466 HOH C O   1 
HETATM 9455 O  O   . HOH Z  5 .   ? 43.870  4.071   -44.296 1.00 19.70 ? 467 HOH C O   1 
HETATM 9456 O  O   . HOH Z  5 .   ? 56.849  4.425   -41.859 1.00 19.98 ? 468 HOH C O   1 
HETATM 9457 O  O   . HOH Z  5 .   ? 24.124  13.069  -42.417 1.00 15.22 ? 469 HOH C O   1 
HETATM 9458 O  O   . HOH Z  5 .   ? 33.839  -16.210 -16.775 1.00 40.32 ? 470 HOH C O   1 
HETATM 9459 O  O   . HOH Z  5 .   ? 35.270  -18.186 -33.976 1.00 33.56 ? 471 HOH C O   1 
HETATM 9460 O  O   . HOH Z  5 .   ? 27.550  16.217  -41.301 1.00 14.77 ? 472 HOH C O   1 
HETATM 9461 O  O   . HOH Z  5 .   ? 32.896  -13.445 -36.819 1.00 19.91 ? 473 HOH C O   1 
HETATM 9462 O  O   . HOH Z  5 .   ? 47.956  -8.962  -51.095 1.00 34.97 ? 474 HOH C O   1 
HETATM 9463 O  O   . HOH Z  5 .   ? 54.724  -10.021 -30.599 1.00 26.31 ? 475 HOH C O   1 
HETATM 9464 O  O   . HOH Z  5 .   ? 41.675  -8.409  -54.758 1.00 19.53 ? 476 HOH C O   1 
HETATM 9465 O  O   . HOH Z  5 .   ? 43.330  -2.398  -40.258 1.00 13.04 ? 477 HOH C O   1 
HETATM 9466 O  O   . HOH Z  5 .   ? 53.740  -3.723  -45.884 1.00 36.08 ? 478 HOH C O   1 
HETATM 9467 O  O   . HOH Z  5 .   ? 26.368  7.169   -14.109 1.00 38.09 ? 479 HOH C O   1 
HETATM 9468 O  O   . HOH Z  5 .   ? 26.200  6.898   -41.178 1.00 12.32 ? 480 HOH C O   1 
HETATM 9469 O  O   . HOH Z  5 .   ? 25.127  6.464   -34.566 1.00 10.84 ? 481 HOH C O   1 
HETATM 9470 O  O   . HOH Z  5 .   ? 33.349  -21.676 -41.803 1.00 42.21 ? 482 HOH C O   1 
HETATM 9471 O  O   . HOH Z  5 .   ? 34.295  15.886  -38.329 1.00 12.09 ? 483 HOH C O   1 
HETATM 9472 O  O   . HOH Z  5 .   ? 22.580  -2.030  -31.242 1.00 32.37 ? 484 HOH C O   1 
HETATM 9473 O  O   . HOH Z  5 .   ? 26.057  -3.514  -42.569 1.00 18.84 ? 485 HOH C O   1 
HETATM 9474 O  O   . HOH Z  5 .   ? 37.554  8.886   -47.392 1.00 28.64 ? 486 HOH C O   1 
HETATM 9475 O  O   . HOH Z  5 .   ? 23.605  -4.661  -35.841 1.00 18.57 ? 487 HOH C O   1 
HETATM 9476 O  O   . HOH Z  5 .   ? 50.068  -9.356  -45.922 1.00 32.09 ? 488 HOH C O   1 
HETATM 9477 O  O   . HOH Z  5 .   ? 24.529  19.014  -28.753 1.00 37.16 ? 489 HOH C O   1 
HETATM 9478 O  O   . HOH Z  5 .   ? 45.446  -7.114  -45.351 1.00 18.12 ? 490 HOH C O   1 
HETATM 9479 O  O   . HOH Z  5 .   ? 37.813  -10.420 -33.129 1.00 14.26 ? 491 HOH C O   1 
HETATM 9480 O  O   . HOH Z  5 .   ? 44.954  -14.026 -44.412 1.00 20.29 ? 492 HOH C O   1 
HETATM 9481 O  O   . HOH Z  5 .   ? 34.818  -7.966  -11.028 1.00 30.38 ? 493 HOH C O   1 
HETATM 9482 O  O   . HOH Z  5 .   ? 32.479  0.149   -50.746 1.00 34.72 ? 494 HOH C O   1 
HETATM 9483 O  O   . HOH Z  5 .   ? 51.397  7.147   -28.348 1.00 25.81 ? 495 HOH C O   1 
HETATM 9484 O  O   . HOH Z  5 .   ? 47.149  -14.661 -31.977 1.00 33.50 ? 496 HOH C O   1 
HETATM 9485 O  O   . HOH Z  5 .   ? 60.087  -2.089  -35.311 1.00 33.35 ? 497 HOH C O   1 
HETATM 9486 O  O   . HOH Z  5 .   ? 20.211  -10.147 -29.682 1.00 19.54 ? 498 HOH C O   1 
HETATM 9487 O  O   . HOH Z  5 .   ? 27.184  -0.877  -32.144 1.00 10.59 ? 499 HOH C O   1 
HETATM 9488 O  O   . HOH Z  5 .   ? 20.992  13.506  -35.573 1.00 8.67  ? 500 HOH C O   1 
HETATM 9489 O  O   . HOH Z  5 .   ? 41.534  -3.419  -11.442 1.00 38.85 ? 501 HOH C O   1 
HETATM 9490 O  O   . HOH Z  5 .   ? 56.184  -2.108  -42.410 1.00 32.14 ? 502 HOH C O   1 
HETATM 9491 O  O   . HOH Z  5 .   ? 55.858  -8.194  -32.579 1.00 22.52 ? 503 HOH C O   1 
HETATM 9492 O  O   . HOH Z  5 .   ? 26.771  9.343   -34.671 1.00 11.75 ? 504 HOH C O   1 
HETATM 9493 O  O   . HOH Z  5 .   ? 26.349  3.172   -47.283 1.00 30.05 ? 505 HOH C O   1 
HETATM 9494 O  O   . HOH Z  5 .   ? 41.395  7.291   -46.720 1.00 23.92 ? 506 HOH C O   1 
HETATM 9495 O  O   . HOH Z  5 .   ? 35.324  6.012   -26.708 1.00 21.07 ? 507 HOH C O   1 
HETATM 9496 O  O   . HOH Z  5 .   ? 46.367  -11.430 -40.359 1.00 24.60 ? 508 HOH C O   1 
HETATM 9497 O  O   . HOH Z  5 .   ? 47.026  -13.158 -52.937 1.00 21.96 ? 509 HOH C O   1 
HETATM 9498 O  O   . HOH Z  5 .   ? 47.148  7.253   -22.804 1.00 25.50 ? 510 HOH C O   1 
HETATM 9499 O  O   . HOH Z  5 .   ? 40.167  -8.173  -13.495 1.00 32.20 ? 511 HOH C O   1 
HETATM 9500 O  O   . HOH Z  5 .   ? 43.861  -12.884 -25.663 1.00 25.30 ? 512 HOH C O   1 
HETATM 9501 O  O   . HOH Z  5 .   ? 22.491  0.370   -27.741 1.00 23.06 ? 513 HOH C O   1 
HETATM 9502 O  O   . HOH Z  5 .   ? 28.184  -10.547 -22.258 1.00 21.07 ? 514 HOH C O   1 
HETATM 9503 O  O   . HOH Z  5 .   ? 33.965  1.631   -16.457 1.00 17.92 ? 515 HOH C O   1 
HETATM 9504 O  O   . HOH Z  5 .   ? 35.524  17.070  -41.426 1.00 29.46 ? 516 HOH C O   1 
HETATM 9505 O  O   . HOH Z  5 .   ? 22.240  6.805   -32.152 1.00 10.70 ? 517 HOH C O   1 
HETATM 9506 O  O   . HOH Z  5 .   ? 58.174  -7.234  -30.837 1.00 25.34 ? 518 HOH C O   1 
HETATM 9507 O  O   . HOH Z  5 .   ? 25.637  -3.317  -48.178 1.00 28.56 ? 519 HOH C O   1 
HETATM 9508 O  O   . HOH Z  5 .   ? 33.629  22.446  -34.864 1.00 37.85 ? 520 HOH C O   1 
HETATM 9509 O  O   . HOH Z  5 .   ? 33.777  13.489  -44.147 1.00 18.72 ? 521 HOH C O   1 
HETATM 9510 O  O   . HOH Z  5 .   ? 40.560  -16.558 -30.026 1.00 24.51 ? 522 HOH C O   1 
HETATM 9511 O  O   . HOH Z  5 .   ? 58.942  -7.601  -34.291 1.00 30.86 ? 523 HOH C O   1 
HETATM 9512 O  O   . HOH Z  5 .   ? 22.215  -13.791 -35.631 1.00 36.78 ? 524 HOH C O   1 
HETATM 9513 O  O   . HOH Z  5 .   ? 27.841  2.371   -52.115 1.00 32.59 ? 525 HOH C O   1 
HETATM 9514 O  O   . HOH Z  5 .   ? 53.110  6.316   -31.323 1.00 22.76 ? 526 HOH C O   1 
HETATM 9515 O  O   . HOH Z  5 .   ? 24.348  -0.748  -32.827 1.00 19.27 ? 527 HOH C O   1 
HETATM 9516 O  O   . HOH Z  5 .   ? 50.306  -4.742  -15.962 1.00 38.81 ? 528 HOH C O   1 
HETATM 9517 O  O   . HOH Z  5 .   ? 52.800  8.616   -23.854 1.00 27.54 ? 529 HOH C O   1 
HETATM 9518 O  O   . HOH Z  5 .   ? 41.864  -18.984 -17.896 1.00 44.22 ? 530 HOH C O   1 
HETATM 9519 O  O   . HOH Z  5 .   ? 41.002  14.177  -37.158 1.00 33.21 ? 531 HOH C O   1 
HETATM 9520 O  O   . HOH Z  5 .   ? 23.042  -11.617 -44.486 1.00 27.12 ? 532 HOH C O   1 
HETATM 9521 O  O   . HOH Z  5 .   ? 29.312  5.928   -47.361 1.00 17.52 ? 533 HOH C O   1 
HETATM 9522 O  O   . HOH Z  5 .   ? 62.112  -1.050  -32.317 1.00 25.51 ? 534 HOH C O   1 
HETATM 9523 O  O   . HOH Z  5 .   ? 24.898  -1.882  -23.492 1.00 24.39 ? 535 HOH C O   1 
HETATM 9524 O  O   . HOH Z  5 .   ? 23.494  4.701   -35.930 1.00 8.15  ? 536 HOH C O   1 
HETATM 9525 O  O   . HOH Z  5 .   ? 32.004  2.377   -43.596 1.00 15.77 ? 537 HOH C O   1 
HETATM 9526 O  O   . HOH Z  5 .   ? 25.965  12.942  -35.397 1.00 10.85 ? 538 HOH C O   1 
HETATM 9527 O  O   . HOH Z  5 .   ? 35.940  -1.232  -48.343 1.00 18.26 ? 539 HOH C O   1 
HETATM 9528 O  O   . HOH Z  5 .   ? 32.677  7.528   -22.625 1.00 27.35 ? 540 HOH C O   1 
HETATM 9529 O  O   . HOH Z  5 .   ? 26.469  3.837   -49.875 1.00 39.60 ? 541 HOH C O   1 
HETATM 9530 O  O   . HOH Z  5 .   ? 56.910  -8.318  -22.849 1.00 40.49 ? 542 HOH C O   1 
HETATM 9531 O  O   . HOH Z  5 .   ? 23.814  5.514   -40.561 1.00 12.95 ? 543 HOH C O   1 
HETATM 9532 O  O   . HOH Z  5 .   ? 41.036  3.930   -6.674  1.00 21.83 ? 544 HOH C O   1 
HETATM 9533 O  O   . HOH Z  5 .   ? 19.635  -7.657  -17.503 1.00 31.57 ? 545 HOH C O   1 
HETATM 9534 O  O   . HOH Z  5 .   ? 32.611  11.247  -43.171 1.00 12.55 ? 546 HOH C O   1 
HETATM 9535 O  O   . HOH Z  5 .   ? 22.566  11.028  -29.291 1.00 17.09 ? 547 HOH C O   1 
HETATM 9536 O  O   . HOH Z  5 .   ? 38.364  4.930   -45.154 1.00 18.11 ? 548 HOH C O   1 
HETATM 9537 O  O   . HOH Z  5 .   ? 58.069  -0.919  -16.049 1.00 29.21 ? 549 HOH C O   1 
HETATM 9538 O  O   . HOH Z  5 .   ? 36.763  -17.141 -27.249 1.00 41.96 ? 550 HOH C O   1 
HETATM 9539 O  O   . HOH Z  5 .   ? 39.321  -26.567 -44.358 1.00 25.27 ? 551 HOH C O   1 
HETATM 9540 O  O   . HOH Z  5 .   ? 28.775  -14.301 -48.664 1.00 41.39 ? 552 HOH C O   1 
HETATM 9541 O  O   . HOH Z  5 .   ? 48.864  2.945   -49.153 1.00 41.68 ? 553 HOH C O   1 
HETATM 9542 O  O   . HOH Z  5 .   ? 29.647  -14.047 -28.066 1.00 29.38 ? 554 HOH C O   1 
HETATM 9543 O  O   . HOH Z  5 .   ? 22.787  -8.691  -17.149 1.00 35.42 ? 555 HOH C O   1 
HETATM 9544 O  O   . HOH Z  5 .   ? 31.489  2.462   -14.605 1.00 20.33 ? 556 HOH C O   1 
HETATM 9545 O  O   . HOH Z  5 .   ? 26.257  11.285  -45.367 1.00 24.18 ? 557 HOH C O   1 
HETATM 9546 O  O   . HOH Z  5 .   ? 27.187  6.605   -21.095 1.00 29.35 ? 558 HOH C O   1 
HETATM 9547 O  O   . HOH Z  5 .   ? 42.410  -13.973 -48.584 1.00 37.47 ? 559 HOH C O   1 
HETATM 9548 O  O   . HOH Z  5 .   ? 26.513  -13.666 -34.445 1.00 22.00 ? 560 HOH C O   1 
HETATM 9549 O  O   . HOH Z  5 .   ? 31.550  12.566  -46.515 1.00 21.95 ? 561 HOH C O   1 
HETATM 9550 O  O   . HOH Z  5 .   ? 25.502  14.600  -23.146 1.00 31.52 ? 562 HOH C O   1 
HETATM 9551 O  O   . HOH Z  5 .   ? 44.203  13.799  -47.763 1.00 36.24 ? 563 HOH C O   1 
HETATM 9552 O  O   . HOH Z  5 .   ? 48.079  18.857  -40.724 1.00 38.74 ? 564 HOH C O   1 
HETATM 9553 O  O   . HOH Z  5 .   ? 24.461  -3.805  -44.747 1.00 27.28 ? 565 HOH C O   1 
HETATM 9554 O  O   . HOH Z  5 .   ? 42.639  16.899  -44.410 1.00 35.10 ? 566 HOH C O   1 
HETATM 9555 O  O   . HOH Z  5 .   ? 46.846  11.073  -12.913 1.00 34.76 ? 567 HOH C O   1 
HETATM 9556 O  O   . HOH Z  5 .   ? 28.317  -10.582 -51.254 1.00 37.83 ? 568 HOH C O   1 
HETATM 9557 O  O   . HOH Z  5 .   ? 40.044  14.027  -12.514 1.00 34.98 ? 569 HOH C O   1 
HETATM 9558 O  O   . HOH Z  5 .   ? 39.947  -12.044 -54.984 1.00 25.08 ? 570 HOH C O   1 
HETATM 9559 O  O   . HOH Z  5 .   ? 32.085  -2.177  -51.568 1.00 34.39 ? 571 HOH C O   1 
HETATM 9560 O  O   . HOH Z  5 .   ? 38.705  16.515  -38.803 1.00 23.21 ? 572 HOH C O   1 
HETATM 9561 O  O   . HOH Z  5 .   ? 53.444  5.904   -23.322 1.00 27.69 ? 573 HOH C O   1 
HETATM 9562 O  O   . HOH Z  5 .   ? 30.326  6.600   -21.473 1.00 25.79 ? 574 HOH C O   1 
HETATM 9563 O  O   . HOH Z  5 .   ? 29.335  9.083   -22.238 1.00 27.86 ? 575 HOH C O   1 
HETATM 9564 O  O   . HOH Z  5 .   ? 26.452  9.662   -41.703 1.00 13.25 ? 576 HOH C O   1 
HETATM 9565 O  O   . HOH Z  5 .   ? 41.600  9.039   -7.701  1.00 30.17 ? 577 HOH C O   1 
HETATM 9566 O  O   . HOH Z  5 .   ? 46.742  -0.835  -47.428 1.00 31.51 ? 578 HOH C O   1 
HETATM 9567 O  O   . HOH Z  5 .   ? 50.817  -13.722 -19.071 1.00 43.69 ? 579 HOH C O   1 
HETATM 9568 O  O   . HOH Z  5 .   ? 40.804  -15.711 -25.209 1.00 25.12 ? 580 HOH C O   1 
HETATM 9569 O  O   . HOH Z  5 .   ? 29.759  -12.473 -23.706 1.00 23.47 ? 581 HOH C O   1 
HETATM 9570 O  O   . HOH Z  5 .   ? 53.063  -11.401 -36.768 1.00 33.81 ? 582 HOH C O   1 
HETATM 9571 O  O   . HOH Z  5 .   ? 42.318  -4.006  -48.279 1.00 22.76 ? 583 HOH C O   1 
HETATM 9572 O  O   . HOH Z  5 .   ? 40.789  -16.255 -22.067 1.00 30.04 ? 584 HOH C O   1 
HETATM 9573 O  O   . HOH Z  5 .   ? 22.340  -0.470  -44.118 1.00 20.77 ? 585 HOH C O   1 
HETATM 9574 O  O   . HOH Z  5 .   ? 22.460  -5.277  -41.051 1.00 24.64 ? 586 HOH C O   1 
HETATM 9575 O  O   . HOH Z  5 .   ? 38.888  13.770  -42.867 1.00 26.98 ? 587 HOH C O   1 
HETATM 9576 O  O   . HOH Z  5 .   ? 28.841  3.470   -46.183 1.00 20.24 ? 588 HOH C O   1 
HETATM 9577 O  O   . HOH Z  5 .   ? 33.887  3.741   -7.978  1.00 30.39 ? 589 HOH C O   1 
HETATM 9578 O  O   . HOH Z  5 .   ? 48.104  17.521  -36.641 1.00 41.30 ? 590 HOH C O   1 
HETATM 9579 O  O   . HOH Z  5 .   ? 52.014  5.466   -12.717 1.00 29.65 ? 591 HOH C O   1 
HETATM 9580 O  O   . HOH Z  5 .   ? 43.873  13.102  -9.983  1.00 30.43 ? 592 HOH C O   1 
HETATM 9581 O  O   . HOH Z  5 .   ? 48.721  11.133  -23.843 1.00 36.96 ? 593 HOH C O   1 
HETATM 9582 O  O   . HOH Z  5 .   ? 35.698  19.356  -35.786 1.00 35.64 ? 594 HOH C O   1 
HETATM 9583 O  O   . HOH Z  5 .   ? 47.066  -16.498 -35.500 1.00 32.74 ? 595 HOH C O   1 
HETATM 9584 O  O   . HOH Z  5 .   ? 28.209  6.718   -43.743 1.00 21.33 ? 596 HOH C O   1 
HETATM 9585 O  O   . HOH Z  5 .   ? 23.869  -9.276  -28.916 1.00 36.03 ? 597 HOH C O   1 
HETATM 9586 O  O   . HOH Z  5 .   ? 30.171  -9.916  -16.375 1.00 34.70 ? 598 HOH C O   1 
HETATM 9587 O  O   . HOH Z  5 .   ? 52.498  17.878  -38.901 1.00 42.33 ? 599 HOH C O   1 
HETATM 9588 O  O   . HOH Z  5 .   ? 40.589  -14.129 -36.127 1.00 16.77 ? 600 HOH C O   1 
HETATM 9589 O  O   . HOH Z  5 .   ? 44.473  7.431   -8.918  1.00 35.14 ? 601 HOH C O   1 
HETATM 9590 O  O   . HOH Z  5 .   ? 51.752  9.929   -33.225 1.00 28.27 ? 602 HOH C O   1 
HETATM 9591 O  O   . HOH Z  5 .   ? 29.623  -12.374 -40.621 1.00 35.15 ? 603 HOH C O   1 
HETATM 9592 O  O   . HOH Z  5 .   ? 24.661  5.449   -21.172 1.00 27.32 ? 604 HOH C O   1 
HETATM 9593 O  O   . HOH Z  5 .   ? 49.818  12.385  -32.717 1.00 28.25 ? 605 HOH C O   1 
HETATM 9594 O  O   . HOH Z  5 .   ? 32.030  10.147  -23.095 1.00 32.38 ? 606 HOH C O   1 
HETATM 9595 O  O   . HOH Z  5 .   ? 23.738  3.459   -50.849 1.00 43.07 ? 607 HOH C O   1 
HETATM 9596 O  O   . HOH Z  5 .   ? 46.780  -16.929 -38.168 1.00 25.18 ? 608 HOH C O   1 
HETATM 9597 O  O   . HOH Z  5 .   ? 39.641  18.011  -40.880 1.00 28.98 ? 609 HOH C O   1 
HETATM 9598 O  O   . HOH Z  5 .   ? 22.973  2.146   -18.716 1.00 26.04 ? 610 HOH C O   1 
HETATM 9599 O  O   . HOH Z  5 .   ? 29.755  -11.740 -26.369 1.00 19.23 ? 611 HOH C O   1 
HETATM 9600 O  O   . HOH Z  5 .   ? 41.144  4.343   -45.533 1.00 37.17 ? 612 HOH C O   1 
HETATM 9601 O  O   . HOH Z  5 .   ? 22.466  19.138  -30.493 1.00 30.88 ? 613 HOH C O   1 
HETATM 9602 O  O   . HOH Z  5 .   ? 37.693  -20.981 -40.806 1.00 44.68 ? 614 HOH C O   1 
HETATM 9603 O  O   . HOH Z  5 .   ? 22.941  -4.543  -26.453 1.00 31.14 ? 615 HOH C O   1 
HETATM 9604 O  O   . HOH Z  5 .   ? 53.934  6.922   -27.529 1.00 26.54 ? 616 HOH C O   1 
HETATM 9605 O  O   . HOH Z  5 .   ? 32.836  -14.983 -47.138 1.00 37.88 ? 617 HOH C O   1 
HETATM 9606 O  O   . HOH Z  5 .   ? 32.564  12.403  -21.775 1.00 31.85 ? 618 HOH C O   1 
HETATM 9607 O  O   . HOH Z  5 .   ? 21.159  -0.210  -21.138 1.00 24.86 ? 619 HOH C O   1 
HETATM 9608 O  O   . HOH Z  5 .   ? 21.076  -1.158  -29.688 1.00 21.59 ? 620 HOH C O   1 
HETATM 9609 O  O   . HOH Z  5 .   ? 53.967  -9.266  -19.036 1.00 40.44 ? 621 HOH C O   1 
HETATM 9610 O  O   . HOH Z  5 .   ? 34.186  20.468  -30.342 1.00 44.21 ? 622 HOH C O   1 
HETATM 9611 O  O   . HOH Z  5 .   ? 25.025  4.572   -45.778 1.00 33.46 ? 623 HOH C O   1 
HETATM 9612 O  O   . HOH Z  5 .   ? 24.317  -14.436 -47.854 1.00 43.92 ? 624 HOH C O   1 
HETATM 9613 O  O   . HOH Z  5 .   ? 56.511  7.688   -14.231 1.00 34.10 ? 625 HOH C O   1 
HETATM 9614 O  O   . HOH Z  5 .   ? 46.423  14.958  -31.170 1.00 47.80 ? 626 HOH C O   1 
HETATM 9615 O  O   . HOH Z  5 .   ? 27.436  20.769  -30.371 1.00 33.48 ? 627 HOH C O   1 
HETATM 9616 O  O   . HOH Z  5 .   ? 33.345  4.069   -10.917 1.00 38.45 ? 628 HOH C O   1 
HETATM 9617 O  O   . HOH Z  5 .   ? 45.642  -6.099  -47.937 1.00 25.98 ? 629 HOH C O   1 
HETATM 9618 O  O   . HOH Z  5 .   ? 56.227  11.992  -42.427 1.00 35.83 ? 630 HOH C O   1 
HETATM 9619 O  O   . HOH Z  5 .   ? 46.768  -3.658  -48.412 1.00 32.51 ? 631 HOH C O   1 
HETATM 9620 O  O   . HOH Z  5 .   ? 36.918  15.505  -25.765 1.00 37.29 ? 632 HOH C O   1 
HETATM 9621 O  O   . HOH Z  5 .   ? 62.992  0.413   -19.785 1.00 33.34 ? 633 HOH C O   1 
HETATM 9622 O  O   . HOH Z  5 .   ? 27.758  -12.735 -30.021 1.00 31.16 ? 634 HOH C O   1 
HETATM 9623 O  O   . HOH Z  5 .   ? 43.304  -16.471 -21.919 1.00 42.65 ? 635 HOH C O   1 
HETATM 9624 O  O   . HOH Z  5 .   ? 42.809  -5.728  -54.171 1.00 24.94 ? 636 HOH C O   1 
HETATM 9625 O  O   . HOH Z  5 .   ? 54.062  5.077   -25.785 1.00 31.27 ? 637 HOH C O   1 
HETATM 9626 O  O   . HOH Z  5 .   ? 26.381  7.723   -45.515 1.00 39.28 ? 638 HOH C O   1 
HETATM 9627 O  O   . HOH Z  5 .   ? 20.608  1.129   -45.788 1.00 28.25 ? 639 HOH C O   1 
HETATM 9628 O  O   . HOH Z  5 .   ? 28.103  15.256  -45.377 1.00 36.12 ? 640 HOH C O   1 
HETATM 9629 O  O   . HOH Z  5 .   ? 21.220  -3.984  -31.934 1.00 30.94 ? 641 HOH C O   1 
HETATM 9630 O  O   . HOH Z  5 .   ? 34.413  -18.338 -30.859 1.00 39.16 ? 642 HOH C O   1 
HETATM 9631 O  O   . HOH Z  5 .   ? 48.623  -15.698 -39.740 1.00 32.31 ? 643 HOH C O   1 
HETATM 9632 O  O   . HOH Z  5 .   ? 35.757  1.248   -50.235 1.00 36.97 ? 644 HOH C O   1 
HETATM 9633 O  O   . HOH Z  5 .   ? 22.714  3.697   -46.762 1.00 36.06 ? 645 HOH C O   1 
HETATM 9634 O  O   . HOH Z  5 .   ? 45.081  -17.915 -20.155 1.00 49.09 ? 646 HOH C O   1 
HETATM 9635 O  O   . HOH Z  5 .   ? 22.641  8.625   -27.819 1.00 17.08 ? 647 HOH C O   1 
HETATM 9636 O  O   . HOH Z  5 .   ? 20.939  5.158   -51.545 1.00 40.27 ? 648 HOH C O   1 
HETATM 9637 O  O   . HOH Z  5 .   ? 44.999  -1.882  -48.641 1.00 41.89 ? 649 HOH C O   1 
HETATM 9638 O  O   . HOH Z  5 .   ? 22.047  -4.102  -37.947 1.00 24.08 ? 650 HOH C O   1 
HETATM 9639 O  O   . HOH Z  5 .   ? 28.491  27.052  -30.455 1.00 25.76 ? 651 HOH C O   1 
HETATM 9640 O  O   . HOH Z  5 .   ? 45.701  -16.075 -45.445 1.00 29.12 ? 652 HOH C O   1 
HETATM 9641 O  O   . HOH Z  5 .   ? 47.009  -12.895 -14.598 1.00 34.61 ? 653 HOH C O   1 
HETATM 9642 O  O   . HOH Z  5 .   ? 38.575  -2.700  -48.713 1.00 39.18 ? 654 HOH C O   1 
HETATM 9643 O  O   . HOH Z  5 .   ? 41.936  -25.962 -44.866 1.00 39.28 ? 655 HOH C O   1 
HETATM 9644 O  O   . HOH Z  5 .   ? 50.469  -13.197 -16.414 1.00 40.80 ? 656 HOH C O   1 
HETATM 9645 O  O   . HOH Z  5 .   ? 42.022  -10.666 -56.349 1.00 18.24 ? 657 HOH C O   1 
HETATM 9646 O  O   . HOH Z  5 .   ? 36.151  17.884  -38.095 1.00 25.96 ? 658 HOH C O   1 
HETATM 9647 O  O   . HOH Z  5 .   ? 40.478  16.769  -36.623 1.00 28.63 ? 659 HOH C O   1 
HETATM 9648 O  O   . HOH Z  5 .   ? 34.527  9.252   -47.839 1.00 36.93 ? 660 HOH C O   1 
HETATM 9649 O  O   . HOH Z  5 .   ? 45.647  -19.306 -39.300 1.00 42.49 ? 661 HOH C O   1 
HETATM 9650 O  O   . HOH Z  5 .   ? 19.266  15.967  -20.967 1.00 36.02 ? 662 HOH C O   1 
HETATM 9651 O  O   . HOH Z  5 .   ? 35.889  13.490  -46.004 1.00 34.32 ? 663 HOH C O   1 
HETATM 9652 O  O   . HOH Z  5 .   ? 30.212  5.794   -49.766 1.00 36.09 ? 664 HOH C O   1 
HETATM 9653 O  O   . HOH Z  5 .   ? 49.045  -11.270 -52.493 1.00 22.89 ? 665 HOH C O   1 
HETATM 9654 O  O   . HOH Z  5 .   ? 40.524  -15.134 -56.228 1.00 27.52 ? 666 HOH C O   1 
HETATM 9655 O  O   . HOH Z  5 .   ? 52.706  17.131  -42.141 1.00 38.78 ? 667 HOH C O   1 
HETATM 9656 O  O   . HOH Z  5 .   ? 35.743  19.374  -40.380 1.00 36.99 ? 668 HOH C O   1 
HETATM 9657 O  O   . HOH Z  5 .   ? 50.700  15.939  -44.309 1.00 40.29 ? 669 HOH C O   1 
HETATM 9658 O  O   . HOH Z  5 .   ? 26.816  6.808   -47.668 1.00 35.72 ? 670 HOH C O   1 
HETATM 9659 O  O   . HOH Z  5 .   ? 34.179  11.739  -47.609 1.00 29.38 ? 671 HOH C O   1 
HETATM 9660 O  O   . HOH Z  5 .   ? 49.466  -15.925 -48.116 1.00 35.82 ? 672 HOH C O   1 
HETATM 9661 O  O   . HOH Z  5 .   ? 26.228  -11.270 -17.209 1.00 37.90 ? 673 HOH C O   1 
HETATM 9662 O  O   . HOH Z  5 .   ? 51.252  -12.888 -51.523 1.00 37.51 ? 674 HOH C O   1 
HETATM 9663 O  O   . HOH Z  5 .   ? 33.578  8.163   -50.019 1.00 36.13 ? 675 HOH C O   1 
HETATM 9664 O  O   . HOH Z  5 .   ? 30.818  14.109  -49.996 1.00 44.84 ? 676 HOH C O   1 
HETATM 9665 O  O   . HOH AA 5 .   ? 5.693   -14.811 -39.974 1.00 28.62 ? 401 HOH D O   1 
HETATM 9666 O  O   . HOH AA 5 .   ? -9.425  5.477   -21.783 1.00 32.68 ? 402 HOH D O   1 
HETATM 9667 O  O   . HOH AA 5 .   ? 17.638  -6.647  -56.002 1.00 28.39 ? 403 HOH D O   1 
HETATM 9668 O  O   . HOH AA 5 .   ? 4.177   -14.711 -17.104 1.00 41.79 ? 404 HOH D O   1 
HETATM 9669 O  O   . HOH AA 5 .   ? 14.224  19.773  -42.814 1.00 29.21 ? 405 HOH D O   1 
HETATM 9670 O  O   . HOH AA 5 .   ? 12.675  19.753  -29.354 1.00 25.66 ? 406 HOH D O   1 
HETATM 9671 O  O   . HOH AA 5 .   ? -14.534 4.787   -37.072 1.00 22.81 ? 407 HOH D O   1 
HETATM 9672 O  O   . HOH AA 5 .   ? -5.896  13.659  -37.204 1.00 26.92 ? 408 HOH D O   1 
HETATM 9673 O  O   . HOH AA 5 .   ? 8.735   -14.619 -37.387 1.00 28.15 ? 409 HOH D O   1 
HETATM 9674 O  O   . HOH AA 5 .   ? 11.251  15.486  -50.499 1.00 34.38 ? 410 HOH D O   1 
HETATM 9675 O  O   . HOH AA 5 .   ? 5.689   -14.591 -33.834 1.00 48.55 ? 411 HOH D O   1 
HETATM 9676 O  O   . HOH AA 5 .   ? 14.675  -12.114 -34.290 1.00 32.77 ? 412 HOH D O   1 
HETATM 9677 O  O   . HOH AA 5 .   ? -0.129  -10.360 -17.950 1.00 22.71 ? 413 HOH D O   1 
HETATM 9678 O  O   . HOH AA 5 .   ? 1.475   8.074   -22.818 1.00 39.63 ? 414 HOH D O   1 
HETATM 9679 O  O   . HOH AA 5 .   ? -9.963  15.140  -30.663 1.00 28.52 ? 415 HOH D O   1 
HETATM 9680 O  O   . HOH AA 5 .   ? 14.306  -8.327  -52.602 1.00 28.13 ? 416 HOH D O   1 
HETATM 9681 O  O   . HOH AA 5 .   ? 9.665   -13.255 -55.388 1.00 35.30 ? 417 HOH D O   1 
HETATM 9682 O  O   . HOH AA 5 .   ? 10.088  15.966  -47.976 1.00 33.58 ? 418 HOH D O   1 
HETATM 9683 O  O   . HOH AA 5 .   ? 23.989  18.383  -42.706 1.00 18.11 ? 419 HOH D O   1 
HETATM 9684 O  O   . HOH AA 5 .   ? 6.003   16.319  -45.532 1.00 37.83 ? 420 HOH D O   1 
HETATM 9685 O  O   . HOH AA 5 .   ? -5.649  19.525  -21.768 1.00 30.42 ? 421 HOH D O   1 
HETATM 9686 O  O   . HOH AA 5 .   ? 12.276  6.949   -39.325 1.00 9.33  ? 422 HOH D O   1 
HETATM 9687 O  O   . HOH AA 5 .   ? -1.876  -8.934  -16.572 1.00 21.79 ? 423 HOH D O   1 
HETATM 9688 O  O   . HOH AA 5 .   ? -4.454  10.030  -57.190 1.00 31.69 ? 424 HOH D O   1 
HETATM 9689 O  O   . HOH AA 5 .   ? 4.248   -0.823  -14.658 1.00 28.47 ? 425 HOH D O   1 
HETATM 9690 O  O   . HOH AA 5 .   ? 20.066  7.984   -42.366 1.00 10.76 ? 426 HOH D O   1 
HETATM 9691 O  O   . HOH AA 5 .   ? 23.014  13.680  -28.665 1.00 21.42 ? 427 HOH D O   1 
HETATM 9692 O  O   . HOH AA 5 .   ? -5.771  -10.257 -45.059 1.00 32.33 ? 428 HOH D O   1 
HETATM 9693 O  O   . HOH AA 5 .   ? -7.029  -3.082  -53.239 1.00 30.64 ? 429 HOH D O   1 
HETATM 9694 O  O   . HOH AA 5 .   ? 21.853  -9.511  -18.924 1.00 29.09 ? 430 HOH D O   1 
HETATM 9695 O  O   . HOH AA 5 .   ? -2.852  -10.458 -39.345 1.00 20.36 ? 431 HOH D O   1 
HETATM 9696 O  O   . HOH AA 5 .   ? -2.636  15.204  -47.774 1.00 32.84 ? 432 HOH D O   1 
HETATM 9697 O  O   . HOH AA 5 .   ? -5.493  -10.014 -34.298 1.00 25.12 ? 433 HOH D O   1 
HETATM 9698 O  O   . HOH AA 5 .   ? -2.749  -14.621 -39.349 1.00 31.13 ? 434 HOH D O   1 
HETATM 9699 O  O   . HOH AA 5 .   ? 20.586  -7.581  -29.691 1.00 18.93 ? 435 HOH D O   1 
HETATM 9700 O  O   . HOH AA 5 .   ? 1.209   9.105   -59.144 1.00 24.80 ? 436 HOH D O   1 
HETATM 9701 O  O   . HOH AA 5 .   ? 2.141   -15.344 -29.491 1.00 23.30 ? 437 HOH D O   1 
HETATM 9702 O  O   . HOH AA 5 .   ? -10.545 11.705  -25.959 1.00 20.40 ? 438 HOH D O   1 
HETATM 9703 O  O   . HOH AA 5 .   ? 18.051  7.388   -27.064 1.00 14.96 ? 439 HOH D O   1 
HETATM 9704 O  O   . HOH AA 5 .   ? 16.596  8.110   -51.502 1.00 20.19 ? 440 HOH D O   1 
HETATM 9705 O  O   . HOH AA 5 .   ? -8.488  -6.453  -28.164 1.00 36.55 ? 441 HOH D O   1 
HETATM 9706 O  O   . HOH AA 5 .   ? -6.174  4.268   -24.330 1.00 19.73 ? 442 HOH D O   1 
HETATM 9707 O  O   . HOH AA 5 .   ? -1.941  11.088  -58.440 1.00 36.52 ? 443 HOH D O   1 
HETATM 9708 O  O   . HOH AA 5 .   ? 14.706  -13.427 -30.596 1.00 32.97 ? 444 HOH D O   1 
HETATM 9709 O  O   . HOH AA 5 .   ? -2.826  11.183  -45.956 1.00 19.62 ? 445 HOH D O   1 
HETATM 9710 O  O   . HOH AA 5 .   ? -1.656  13.307  -38.497 1.00 32.21 ? 446 HOH D O   1 
HETATM 9711 O  O   . HOH AA 5 .   ? 19.434  -4.024  -34.158 1.00 25.52 ? 447 HOH D O   1 
HETATM 9712 O  O   . HOH AA 5 .   ? -10.035 5.358   -55.109 1.00 35.90 ? 448 HOH D O   1 
HETATM 9713 O  O   . HOH AA 5 .   ? 21.110  18.564  -42.624 1.00 33.32 ? 449 HOH D O   1 
HETATM 9714 O  O   . HOH AA 5 .   ? 13.449  22.421  -35.029 1.00 32.60 ? 450 HOH D O   1 
HETATM 9715 O  O   . HOH AA 5 .   ? -5.955  5.255   -56.199 1.00 27.01 ? 451 HOH D O   1 
HETATM 9716 O  O   . HOH AA 5 .   ? -6.835  11.058  -19.549 1.00 12.39 ? 452 HOH D O   1 
HETATM 9717 O  O   . HOH AA 5 .   ? 14.410  5.945   -60.242 1.00 26.79 ? 453 HOH D O   1 
HETATM 9718 O  O   . HOH AA 5 .   ? -6.392  -9.111  -37.351 1.00 32.29 ? 454 HOH D O   1 
HETATM 9719 O  O   . HOH AA 5 .   ? -18.696 5.215   -40.345 1.00 29.51 ? 455 HOH D O   1 
HETATM 9720 O  O   . HOH AA 5 .   ? -12.549 -7.907  -41.047 1.00 24.39 ? 456 HOH D O   1 
HETATM 9721 O  O   . HOH AA 5 .   ? 16.498  0.241   -37.369 1.00 9.83  ? 457 HOH D O   1 
HETATM 9722 O  O   . HOH AA 5 .   ? 19.323  8.428   -29.196 1.00 12.34 ? 458 HOH D O   1 
HETATM 9723 O  O   . HOH AA 5 .   ? -6.301  -2.561  -21.120 1.00 27.77 ? 459 HOH D O   1 
HETATM 9724 O  O   . HOH AA 5 .   ? 18.642  5.149   -45.682 1.00 17.85 ? 460 HOH D O   1 
HETATM 9725 O  O   . HOH AA 5 .   ? 10.706  13.266  -58.516 1.00 24.81 ? 461 HOH D O   1 
HETATM 9726 O  O   . HOH AA 5 .   ? 9.093   3.282   -52.918 1.00 12.73 ? 462 HOH D O   1 
HETATM 9727 O  O   . HOH AA 5 .   ? 1.110   2.549   -28.066 1.00 9.99  ? 463 HOH D O   1 
HETATM 9728 O  O   . HOH AA 5 .   ? -3.136  -14.670 -49.137 1.00 26.54 ? 464 HOH D O   1 
HETATM 9729 O  O   . HOH AA 5 .   ? -12.093 -4.912  -44.280 1.00 22.88 ? 465 HOH D O   1 
HETATM 9730 O  O   . HOH AA 5 .   ? 11.810  -7.064  -52.026 1.00 23.01 ? 466 HOH D O   1 
HETATM 9731 O  O   . HOH AA 5 .   ? 11.953  -3.623  -47.149 1.00 11.45 ? 467 HOH D O   1 
HETATM 9732 O  O   . HOH AA 5 .   ? -15.255 -2.451  -43.373 1.00 21.66 ? 468 HOH D O   1 
HETATM 9733 O  O   . HOH AA 5 .   ? -10.098 15.234  -20.761 1.00 22.56 ? 469 HOH D O   1 
HETATM 9734 O  O   . HOH AA 5 .   ? 8.792   -10.714 -31.082 1.00 16.80 ? 470 HOH D O   1 
HETATM 9735 O  O   . HOH AA 5 .   ? 0.820   -12.134 -13.824 1.00 31.22 ? 471 HOH D O   1 
HETATM 9736 O  O   . HOH AA 5 .   ? -5.680  -5.622  -53.529 1.00 30.20 ? 472 HOH D O   1 
HETATM 9737 O  O   . HOH AA 5 .   ? -8.007  11.873  -36.780 1.00 17.94 ? 473 HOH D O   1 
HETATM 9738 O  O   . HOH AA 5 .   ? -12.120 -9.127  -44.686 1.00 34.49 ? 474 HOH D O   1 
HETATM 9739 O  O   . HOH AA 5 .   ? 19.838  11.113  -29.104 1.00 12.54 ? 475 HOH D O   1 
HETATM 9740 O  O   . HOH AA 5 .   ? -7.994  3.531   -21.242 1.00 26.17 ? 476 HOH D O   1 
HETATM 9741 O  O   . HOH AA 5 .   ? 14.440  2.275   -16.306 1.00 26.59 ? 477 HOH D O   1 
HETATM 9742 O  O   . HOH AA 5 .   ? 4.628   16.030  -56.951 1.00 23.80 ? 478 HOH D O   1 
HETATM 9743 O  O   . HOH AA 5 .   ? -12.737 -1.786  -34.010 1.00 18.33 ? 479 HOH D O   1 
HETATM 9744 O  O   . HOH AA 5 .   ? 17.377  -11.565 -27.252 1.00 23.55 ? 480 HOH D O   1 
HETATM 9745 O  O   . HOH AA 5 .   ? -3.474  -5.645  -26.677 1.00 16.31 ? 481 HOH D O   1 
HETATM 9746 O  O   . HOH AA 5 .   ? 13.434  15.718  -47.893 1.00 29.30 ? 482 HOH D O   1 
HETATM 9747 O  O   . HOH AA 5 .   ? -0.613  19.251  -21.458 1.00 29.80 ? 483 HOH D O   1 
HETATM 9748 O  O   . HOH AA 5 .   ? -2.249  13.131  -41.513 1.00 24.79 ? 484 HOH D O   1 
HETATM 9749 O  O   . HOH AA 5 .   ? 19.145  11.558  -50.160 1.00 19.21 ? 485 HOH D O   1 
HETATM 9750 O  O   . HOH AA 5 .   ? 18.646  -0.151  -20.252 1.00 24.37 ? 486 HOH D O   1 
HETATM 9751 O  O   . HOH AA 5 .   ? 21.456  5.143   -34.170 1.00 9.14  ? 487 HOH D O   1 
HETATM 9752 O  O   . HOH AA 5 .   ? 20.351  -6.944  -44.446 1.00 32.63 ? 488 HOH D O   1 
HETATM 9753 O  O   . HOH AA 5 .   ? -2.250  11.487  -20.196 1.00 22.42 ? 489 HOH D O   1 
HETATM 9754 O  O   . HOH AA 5 .   ? 23.935  8.536   -45.563 1.00 32.49 ? 490 HOH D O   1 
HETATM 9755 O  O   . HOH AA 5 .   ? 11.503  -11.192 -27.392 1.00 29.24 ? 491 HOH D O   1 
HETATM 9756 O  O   . HOH AA 5 .   ? -7.167  -7.003  -51.395 1.00 20.79 ? 492 HOH D O   1 
HETATM 9757 O  O   . HOH AA 5 .   ? 6.293   18.004  -32.999 1.00 29.13 ? 493 HOH D O   1 
HETATM 9758 O  O   . HOH AA 5 .   ? 19.543  18.780  -40.098 1.00 26.75 ? 494 HOH D O   1 
HETATM 9759 O  O   . HOH AA 5 .   ? -12.298 -3.880  -35.920 1.00 23.70 ? 495 HOH D O   1 
HETATM 9760 O  O   . HOH AA 5 .   ? 9.388   8.329   -42.846 1.00 11.76 ? 496 HOH D O   1 
HETATM 9761 O  O   . HOH AA 5 .   ? 6.762   -13.917 -50.763 1.00 10.72 ? 497 HOH D O   1 
HETATM 9762 O  O   . HOH AA 5 .   ? 0.467   -12.691 -36.833 1.00 15.12 ? 498 HOH D O   1 
HETATM 9763 O  O   . HOH AA 5 .   ? -2.445  -8.868  -41.586 1.00 16.28 ? 499 HOH D O   1 
HETATM 9764 O  O   . HOH AA 5 .   ? 3.286   -13.727 -39.303 1.00 27.02 ? 500 HOH D O   1 
HETATM 9765 O  O   . HOH AA 5 .   ? 12.760  -9.713  -45.942 1.00 16.98 ? 501 HOH D O   1 
HETATM 9766 O  O   . HOH AA 5 .   ? 20.658  14.112  -47.714 1.00 17.61 ? 502 HOH D O   1 
HETATM 9767 O  O   . HOH AA 5 .   ? 18.536  -0.232  -29.347 1.00 14.04 ? 503 HOH D O   1 
HETATM 9768 O  O   . HOH AA 5 .   ? 0.770   -8.156  -18.812 1.00 16.81 ? 504 HOH D O   1 
HETATM 9769 O  O   . HOH AA 5 .   ? -12.812 8.517   -55.095 1.00 26.29 ? 505 HOH D O   1 
HETATM 9770 O  O   . HOH AA 5 .   ? -9.980  -0.498  -49.268 1.00 15.72 ? 506 HOH D O   1 
HETATM 9771 O  O   . HOH AA 5 .   ? 22.996  6.310   -38.157 1.00 9.42  ? 507 HOH D O   1 
HETATM 9772 O  O   . HOH AA 5 .   ? -8.401  -0.243  -51.531 1.00 16.83 ? 508 HOH D O   1 
HETATM 9773 O  O   . HOH AA 5 .   ? 5.858   -6.365  -57.396 1.00 17.24 ? 509 HOH D O   1 
HETATM 9774 O  O   . HOH AA 5 .   ? 13.503  18.507  -32.457 1.00 11.85 ? 510 HOH D O   1 
HETATM 9775 O  O   . HOH AA 5 .   ? -2.345  -14.206 -25.993 1.00 34.67 ? 511 HOH D O   1 
HETATM 9776 O  O   . HOH AA 5 .   ? -10.371 -4.685  -29.480 1.00 25.94 ? 512 HOH D O   1 
HETATM 9777 O  O   . HOH AA 5 .   ? 20.252  7.366   -35.698 1.00 10.69 ? 513 HOH D O   1 
HETATM 9778 O  O   . HOH AA 5 .   ? -12.281 10.085  -23.172 1.00 24.87 ? 514 HOH D O   1 
HETATM 9779 O  O   . HOH AA 5 .   ? -8.183  13.550  -44.256 1.00 24.98 ? 515 HOH D O   1 
HETATM 9780 O  O   . HOH AA 5 .   ? 11.026  17.721  -54.546 1.00 24.01 ? 516 HOH D O   1 
HETATM 9781 O  O   . HOH AA 5 .   ? 5.995   3.583   -19.335 1.00 34.15 ? 517 HOH D O   1 
HETATM 9782 O  O   . HOH AA 5 .   ? 9.515   17.538  -44.825 1.00 37.92 ? 518 HOH D O   1 
HETATM 9783 O  O   . HOH AA 5 .   ? -6.858  0.203   -55.801 1.00 25.35 ? 519 HOH D O   1 
HETATM 9784 O  O   . HOH AA 5 .   ? 10.427  2.369   -21.353 1.00 15.90 ? 520 HOH D O   1 
HETATM 9785 O  O   . HOH AA 5 .   ? 19.231  4.838   -49.087 1.00 17.99 ? 521 HOH D O   1 
HETATM 9786 O  O   . HOH AA 5 .   ? -9.855  8.332   -20.601 1.00 21.10 ? 522 HOH D O   1 
HETATM 9787 O  O   . HOH AA 5 .   ? 2.911   21.216  -31.823 1.00 33.97 ? 523 HOH D O   1 
HETATM 9788 O  O   . HOH AA 5 .   ? -5.644  -7.000  -27.663 1.00 16.70 ? 524 HOH D O   1 
HETATM 9789 O  O   . HOH AA 5 .   ? 4.410   -6.898  -34.694 1.00 9.52  ? 525 HOH D O   1 
HETATM 9790 O  O   . HOH AA 5 .   ? 13.826  7.497   -48.292 1.00 11.63 ? 526 HOH D O   1 
HETATM 9791 O  O   . HOH AA 5 .   ? -9.072  -5.222  -22.795 1.00 37.44 ? 527 HOH D O   1 
HETATM 9792 O  O   . HOH AA 5 .   ? 16.508  19.612  -56.804 1.00 35.80 ? 528 HOH D O   1 
HETATM 9793 O  O   . HOH AA 5 .   ? -2.171  -7.812  -22.476 1.00 15.81 ? 529 HOH D O   1 
HETATM 9794 O  O   . HOH AA 5 .   ? 12.301  1.907   -17.891 1.00 16.95 ? 530 HOH D O   1 
HETATM 9795 O  O   . HOH AA 5 .   ? 0.741   24.042  -29.969 1.00 36.15 ? 531 HOH D O   1 
HETATM 9796 O  O   . HOH AA 5 .   ? -11.450 11.304  -45.991 1.00 35.84 ? 532 HOH D O   1 
HETATM 9797 O  O   . HOH AA 5 .   ? 11.084  -0.716  -13.870 1.00 32.41 ? 533 HOH D O   1 
HETATM 9798 O  O   . HOH AA 5 .   ? 8.289   -16.485 -44.913 1.00 24.99 ? 534 HOH D O   1 
HETATM 9799 O  O   . HOH AA 5 .   ? 20.335  21.699  -32.736 1.00 23.58 ? 535 HOH D O   1 
HETATM 9800 O  O   . HOH AA 5 .   ? 5.535   12.349  -22.899 1.00 20.50 ? 536 HOH D O   1 
HETATM 9801 O  O   . HOH AA 5 .   ? -13.834 -1.330  -49.055 1.00 24.68 ? 537 HOH D O   1 
HETATM 9802 O  O   . HOH AA 5 .   ? 16.280  16.076  -54.583 1.00 22.74 ? 538 HOH D O   1 
HETATM 9803 O  O   . HOH AA 5 .   ? 8.370   -9.233  -13.799 1.00 28.57 ? 539 HOH D O   1 
HETATM 9804 O  O   . HOH AA 5 .   ? 21.696  -9.702  -25.940 1.00 29.11 ? 540 HOH D O   1 
HETATM 9805 O  O   . HOH AA 5 .   ? 7.435   12.680  -41.226 1.00 27.09 ? 541 HOH D O   1 
HETATM 9806 O  O   . HOH AA 5 .   ? 11.784  8.859   -47.121 1.00 12.30 ? 542 HOH D O   1 
HETATM 9807 O  O   . HOH AA 5 .   ? 19.055  -11.733 -20.900 1.00 37.91 ? 543 HOH D O   1 
HETATM 9808 O  O   . HOH AA 5 .   ? 15.307  5.900   -18.693 1.00 36.03 ? 544 HOH D O   1 
HETATM 9809 O  O   . HOH AA 5 .   ? 5.938   21.370  -25.552 1.00 18.15 ? 545 HOH D O   1 
HETATM 9810 O  O   . HOH AA 5 .   ? 16.609  10.650  -50.257 1.00 15.31 ? 546 HOH D O   1 
HETATM 9811 O  O   . HOH AA 5 .   ? 23.010  6.407   -23.636 1.00 25.92 ? 547 HOH D O   1 
HETATM 9812 O  O   . HOH AA 5 .   ? -2.702  -0.615  -16.769 1.00 26.35 ? 548 HOH D O   1 
HETATM 9813 O  O   . HOH AA 5 .   ? 0.138   -12.363 -22.659 1.00 39.88 ? 549 HOH D O   1 
HETATM 9814 O  O   . HOH AA 5 .   ? 19.203  9.994   -35.708 1.00 9.62  ? 550 HOH D O   1 
HETATM 9815 O  O   . HOH AA 5 .   ? 18.844  -0.789  -46.276 1.00 26.04 ? 551 HOH D O   1 
HETATM 9816 O  O   . HOH AA 5 .   ? -17.923 -1.743  -44.739 1.00 36.04 ? 552 HOH D O   1 
HETATM 9817 O  O   . HOH AA 5 .   ? -12.043 -4.732  -31.803 1.00 34.30 ? 553 HOH D O   1 
HETATM 9818 O  O   . HOH AA 5 .   ? 1.366   -17.380 -26.458 1.00 41.24 ? 554 HOH D O   1 
HETATM 9819 O  O   . HOH AA 5 .   ? 18.864  -3.440  -42.996 1.00 23.47 ? 555 HOH D O   1 
HETATM 9820 O  O   . HOH AA 5 .   ? -5.246  -13.792 -32.323 1.00 23.21 ? 556 HOH D O   1 
HETATM 9821 O  O   . HOH AA 5 .   ? 14.575  13.893  -27.203 1.00 14.48 ? 557 HOH D O   1 
HETATM 9822 O  O   . HOH AA 5 .   ? 21.443  6.732   -29.601 1.00 12.37 ? 558 HOH D O   1 
HETATM 9823 O  O   . HOH AA 5 .   ? -15.798 9.451   -47.176 1.00 26.05 ? 559 HOH D O   1 
HETATM 9824 O  O   . HOH AA 5 .   ? 6.308   -0.262  -58.237 1.00 32.34 ? 560 HOH D O   1 
HETATM 9825 O  O   . HOH AA 5 .   ? 11.555  22.050  -61.642 1.00 36.55 ? 561 HOH D O   1 
HETATM 9826 O  O   . HOH AA 5 .   ? 17.166  6.713   -48.970 1.00 17.96 ? 562 HOH D O   1 
HETATM 9827 O  O   . HOH AA 5 .   ? -16.247 4.288   -41.001 1.00 22.23 ? 563 HOH D O   1 
HETATM 9828 O  O   . HOH AA 5 .   ? 21.340  2.415   -20.947 1.00 21.81 ? 564 HOH D O   1 
HETATM 9829 O  O   . HOH AA 5 .   ? 16.981  18.815  -43.281 1.00 37.42 ? 565 HOH D O   1 
HETATM 9830 O  O   . HOH AA 5 .   ? 19.155  -0.362  -36.648 1.00 14.64 ? 566 HOH D O   1 
HETATM 9831 O  O   . HOH AA 5 .   ? 20.970  9.499   -25.791 1.00 29.36 ? 567 HOH D O   1 
HETATM 9832 O  O   . HOH AA 5 .   ? 9.044   -10.096 -57.974 1.00 21.34 ? 568 HOH D O   1 
HETATM 9833 O  O   . HOH AA 5 .   ? 17.202  7.554   -55.648 1.00 22.58 ? 569 HOH D O   1 
HETATM 9834 O  O   . HOH AA 5 .   ? -6.513  -7.723  -32.832 1.00 33.87 ? 570 HOH D O   1 
HETATM 9835 O  O   . HOH AA 5 .   ? 8.011   9.041   -24.199 1.00 19.91 ? 571 HOH D O   1 
HETATM 9836 O  O   . HOH AA 5 .   ? 18.600  -7.675  -40.116 1.00 20.03 ? 572 HOH D O   1 
HETATM 9837 O  O   . HOH AA 5 .   ? 1.257   -9.920  -31.090 1.00 12.19 ? 573 HOH D O   1 
HETATM 9838 O  O   . HOH AA 5 .   ? -5.692  -9.983  -39.853 1.00 45.85 ? 574 HOH D O   1 
HETATM 9839 O  O   . HOH AA 5 .   ? 15.553  9.743   -47.873 1.00 14.83 ? 575 HOH D O   1 
HETATM 9840 O  O   . HOH AA 5 .   ? 13.063  11.237  -46.706 1.00 16.29 ? 576 HOH D O   1 
HETATM 9841 O  O   . HOH AA 5 .   ? 14.068  -11.179 -20.426 1.00 36.63 ? 577 HOH D O   1 
HETATM 9842 O  O   . HOH AA 5 .   ? 0.618   15.623  -59.393 1.00 28.40 ? 578 HOH D O   1 
HETATM 9843 O  O   . HOH AA 5 .   ? 0.965   -5.136  -54.374 1.00 22.54 ? 579 HOH D O   1 
HETATM 9844 O  O   . HOH AA 5 .   ? -0.014  -12.199 -42.064 1.00 17.63 ? 580 HOH D O   1 
HETATM 9845 O  O   . HOH AA 5 .   ? 4.162   18.714  -51.096 1.00 29.43 ? 581 HOH D O   1 
HETATM 9846 O  O   . HOH AA 5 .   ? 11.320  3.734   -55.074 1.00 14.90 ? 582 HOH D O   1 
HETATM 9847 O  O   . HOH AA 5 .   ? 2.750   9.453   -24.697 1.00 16.22 ? 583 HOH D O   1 
HETATM 9848 O  O   . HOH AA 5 .   ? -2.927  22.198  -35.098 1.00 22.17 ? 584 HOH D O   1 
HETATM 9849 O  O   . HOH AA 5 .   ? 18.901  -13.274 -33.063 1.00 34.59 ? 585 HOH D O   1 
HETATM 9850 O  O   . HOH AA 5 .   ? 13.560  1.221   -55.683 1.00 20.79 ? 586 HOH D O   1 
HETATM 9851 O  O   . HOH AA 5 .   ? 14.170  17.653  -52.445 1.00 33.41 ? 587 HOH D O   1 
HETATM 9852 O  O   . HOH AA 5 .   ? 8.754   21.645  -29.695 1.00 19.11 ? 588 HOH D O   1 
HETATM 9853 O  O   . HOH AA 5 .   ? 10.679  -10.603 -16.995 1.00 23.10 ? 589 HOH D O   1 
HETATM 9854 O  O   . HOH AA 5 .   ? 22.034  1.241   -25.060 1.00 20.81 ? 590 HOH D O   1 
HETATM 9855 O  O   . HOH AA 5 .   ? -9.635  16.049  -28.496 1.00 29.98 ? 591 HOH D O   1 
HETATM 9856 O  O   . HOH AA 5 .   ? -13.427 12.460  -32.179 1.00 41.98 ? 592 HOH D O   1 
HETATM 9857 O  O   . HOH AA 5 .   ? 18.504  16.938  -41.920 1.00 27.94 ? 593 HOH D O   1 
HETATM 9858 O  O   . HOH AA 5 .   ? -14.132 12.404  -53.732 1.00 41.06 ? 594 HOH D O   1 
HETATM 9859 O  O   . HOH AA 5 .   ? 8.648   -13.656 -29.644 1.00 32.00 ? 595 HOH D O   1 
HETATM 9860 O  O   . HOH AA 5 .   ? -14.486 10.442  -36.695 1.00 35.71 ? 596 HOH D O   1 
HETATM 9861 O  O   . HOH AA 5 .   ? 20.537  17.930  -29.880 1.00 30.23 ? 597 HOH D O   1 
HETATM 9862 O  O   . HOH AA 5 .   ? 22.195  3.672   -23.301 1.00 17.57 ? 598 HOH D O   1 
HETATM 9863 O  O   . HOH AA 5 .   ? 11.158  13.803  -61.127 1.00 23.17 ? 599 HOH D O   1 
HETATM 9864 O  O   . HOH AA 5 .   ? 16.490  15.208  -23.944 1.00 26.48 ? 600 HOH D O   1 
HETATM 9865 O  O   . HOH AA 5 .   ? 23.692  10.497  -41.541 1.00 16.16 ? 601 HOH D O   1 
HETATM 9866 O  O   . HOH AA 5 .   ? 18.452  23.052  -34.172 1.00 21.93 ? 602 HOH D O   1 
HETATM 9867 O  O   . HOH AA 5 .   ? 26.591  16.083  -43.620 1.00 29.24 ? 603 HOH D O   1 
HETATM 9868 O  O   . HOH AA 5 .   ? -4.897  -11.276 -28.127 1.00 22.88 ? 604 HOH D O   1 
HETATM 9869 O  O   . HOH AA 5 .   ? 18.582  -4.374  -18.033 1.00 32.19 ? 605 HOH D O   1 
HETATM 9870 O  O   . HOH AA 5 .   ? 9.268   20.051  -31.935 1.00 19.36 ? 606 HOH D O   1 
HETATM 9871 O  O   . HOH AA 5 .   ? 11.471  -16.590 -21.207 1.00 49.98 ? 607 HOH D O   1 
HETATM 9872 O  O   . HOH AA 5 .   ? 0.036   0.210   -56.806 1.00 23.70 ? 608 HOH D O   1 
HETATM 9873 O  O   . HOH AA 5 .   ? 7.624   -4.824  -14.424 1.00 28.02 ? 609 HOH D O   1 
HETATM 9874 O  O   . HOH AA 5 .   ? -9.243  10.966  -44.842 1.00 17.12 ? 610 HOH D O   1 
HETATM 9875 O  O   . HOH AA 5 .   ? -20.479 5.813   -50.893 1.00 22.70 ? 611 HOH D O   1 
HETATM 9876 O  O   . HOH AA 5 .   ? -8.236  8.464   -55.746 1.00 28.20 ? 612 HOH D O   1 
HETATM 9877 O  O   . HOH AA 5 .   ? 14.020  16.387  -26.328 1.00 19.57 ? 613 HOH D O   1 
HETATM 9878 O  O   . HOH AA 5 .   ? 11.267  -10.509 -43.484 1.00 18.78 ? 614 HOH D O   1 
HETATM 9879 O  O   . HOH AA 5 .   ? 16.368  24.104  -34.163 1.00 28.31 ? 615 HOH D O   1 
HETATM 9880 O  O   . HOH AA 5 .   ? -14.324 9.524   -44.548 1.00 30.53 ? 616 HOH D O   1 
HETATM 9881 O  O   . HOH AA 5 .   ? -2.650  13.974  -56.387 1.00 27.39 ? 617 HOH D O   1 
HETATM 9882 O  O   . HOH AA 5 .   ? -12.176 5.440   -53.120 1.00 35.12 ? 618 HOH D O   1 
HETATM 9883 O  O   . HOH AA 5 .   ? -17.272 -4.246  -36.410 1.00 31.08 ? 619 HOH D O   1 
HETATM 9884 O  O   . HOH AA 5 .   ? -10.653 19.350  -30.861 1.00 28.45 ? 620 HOH D O   1 
HETATM 9885 O  O   . HOH AA 5 .   ? 9.385   17.025  -40.286 1.00 38.32 ? 621 HOH D O   1 
HETATM 9886 O  O   . HOH AA 5 .   ? -3.990  9.969   -17.281 1.00 19.45 ? 622 HOH D O   1 
HETATM 9887 O  O   . HOH AA 5 .   ? -15.075 -0.626  -35.415 1.00 21.85 ? 623 HOH D O   1 
HETATM 9888 O  O   . HOH AA 5 .   ? 4.331   24.048  -28.383 1.00 28.21 ? 624 HOH D O   1 
HETATM 9889 O  O   . HOH AA 5 .   ? 8.635   17.665  -27.451 1.00 21.98 ? 625 HOH D O   1 
HETATM 9890 O  O   . HOH AA 5 .   ? 12.843  13.373  -48.466 1.00 21.62 ? 626 HOH D O   1 
HETATM 9891 O  O   . HOH AA 5 .   ? -11.620 12.753  -38.073 1.00 29.16 ? 627 HOH D O   1 
HETATM 9892 O  O   . HOH AA 5 .   ? -0.234  -12.802 -45.282 1.00 15.93 ? 628 HOH D O   1 
HETATM 9893 O  O   . HOH AA 5 .   ? -11.353 -7.536  -36.445 1.00 30.78 ? 629 HOH D O   1 
HETATM 9894 O  O   . HOH AA 5 .   ? 2.419   1.767   -20.213 1.00 28.10 ? 630 HOH D O   1 
HETATM 9895 O  O   . HOH AA 5 .   ? 1.297   -15.172 -35.617 1.00 34.16 ? 631 HOH D O   1 
HETATM 9896 O  O   . HOH AA 5 .   ? -12.747 -4.432  -47.410 1.00 30.63 ? 632 HOH D O   1 
HETATM 9897 O  O   . HOH AA 5 .   ? 20.785  -4.066  -28.427 1.00 24.90 ? 633 HOH D O   1 
HETATM 9898 O  O   . HOH AA 5 .   ? -16.047 3.148   -38.371 1.00 32.40 ? 634 HOH D O   1 
HETATM 9899 O  O   . HOH AA 5 .   ? 5.231   9.480   -23.638 1.00 22.83 ? 635 HOH D O   1 
HETATM 9900 O  O   . HOH AA 5 .   ? -1.805  -4.076  -55.841 1.00 38.61 ? 636 HOH D O   1 
HETATM 9901 O  O   . HOH AA 5 .   ? -9.618  0.507   -54.369 1.00 27.69 ? 637 HOH D O   1 
HETATM 9902 O  O   . HOH AA 5 .   ? -11.437 12.224  -30.483 1.00 31.28 ? 638 HOH D O   1 
HETATM 9903 O  O   . HOH AA 5 .   ? 2.213   11.224  -61.648 1.00 37.58 ? 639 HOH D O   1 
HETATM 9904 O  O   . HOH AA 5 .   ? -5.667  -11.054 -30.841 1.00 26.11 ? 640 HOH D O   1 
HETATM 9905 O  O   . HOH AA 5 .   ? 14.570  -3.881  -12.954 1.00 37.28 ? 641 HOH D O   1 
HETATM 9906 O  O   . HOH AA 5 .   ? 22.647  -1.621  -39.819 1.00 22.08 ? 642 HOH D O   1 
HETATM 9907 O  O   . HOH AA 5 .   ? 7.222   20.171  -47.499 1.00 40.09 ? 643 HOH D O   1 
HETATM 9908 O  O   . HOH AA 5 .   ? -17.381 8.253   -50.206 1.00 32.20 ? 644 HOH D O   1 
HETATM 9909 O  O   . HOH AA 5 .   ? -17.083 -5.751  -41.615 1.00 38.28 ? 645 HOH D O   1 
HETATM 9910 O  O   . HOH AA 5 .   ? -8.939  16.632  -34.343 1.00 39.93 ? 646 HOH D O   1 
HETATM 9911 O  O   . HOH AA 5 .   ? 21.369  -4.876  -57.653 1.00 38.65 ? 647 HOH D O   1 
HETATM 9912 O  O   . HOH AA 5 .   ? 8.659   -13.194 -16.407 1.00 38.64 ? 648 HOH D O   1 
HETATM 9913 O  O   . HOH AA 5 .   ? -16.206 4.009   -51.574 1.00 45.38 ? 649 HOH D O   1 
HETATM 9914 O  O   . HOH AA 5 .   ? 6.601   -15.257 -30.619 1.00 41.49 ? 650 HOH D O   1 
HETATM 9915 O  O   . HOH AA 5 .   ? 5.474   18.665  -59.051 1.00 32.89 ? 651 HOH D O   1 
HETATM 9916 O  O   . HOH AA 5 .   ? 1.217   15.374  -45.849 1.00 41.60 ? 652 HOH D O   1 
HETATM 9917 O  O   . HOH AA 5 .   ? 19.950  -8.124  -55.754 1.00 34.64 ? 653 HOH D O   1 
HETATM 9918 O  O   . HOH AA 5 .   ? 10.284  -10.880 -20.368 1.00 32.25 ? 654 HOH D O   1 
HETATM 9919 O  O   . HOH AA 5 .   ? 13.785  -10.708 -27.687 1.00 34.60 ? 655 HOH D O   1 
HETATM 9920 O  O   . HOH AA 5 .   ? -2.758  -12.454 -45.226 1.00 24.55 ? 656 HOH D O   1 
HETATM 9921 O  O   . HOH AA 5 .   ? 4.598   -16.568 -30.122 1.00 43.99 ? 657 HOH D O   1 
HETATM 9922 O  O   . HOH AA 5 .   ? -15.197 6.908   -40.467 1.00 27.55 ? 658 HOH D O   1 
HETATM 9923 O  O   . HOH AA 5 .   ? 7.193   -4.058  -58.172 1.00 32.62 ? 659 HOH D O   1 
HETATM 9924 O  O   . HOH AA 5 .   ? -14.715 -5.299  -36.447 1.00 32.88 ? 660 HOH D O   1 
HETATM 9925 O  O   . HOH AA 5 .   ? 27.348  13.033  -47.178 1.00 28.85 ? 661 HOH D O   1 
HETATM 9926 O  O   . HOH AA 5 .   ? -12.500 14.386  -26.438 1.00 37.07 ? 662 HOH D O   1 
HETATM 9927 O  O   . HOH AA 5 .   ? -9.097  -8.763  -37.803 1.00 42.07 ? 663 HOH D O   1 
HETATM 9928 O  O   . HOH AA 5 .   ? -8.678  19.323  -26.058 1.00 34.03 ? 664 HOH D O   1 
HETATM 9929 O  O   . HOH AA 5 .   ? -0.533  23.458  -33.819 1.00 41.54 ? 665 HOH D O   1 
HETATM 9930 O  O   . HOH AA 5 .   ? 22.376  -7.315  -27.379 1.00 23.91 ? 666 HOH D O   1 
HETATM 9931 O  O   . HOH AA 5 .   ? 20.653  3.844   -46.915 1.00 25.78 ? 667 HOH D O   1 
HETATM 9932 O  O   . HOH AA 5 .   ? 21.328  8.664   -20.628 1.00 42.89 ? 668 HOH D O   1 
HETATM 9933 O  O   . HOH AA 5 .   ? 1.992   -7.430  -55.470 1.00 24.80 ? 669 HOH D O   1 
HETATM 9934 O  O   . HOH AA 5 .   ? 22.533  9.111   -43.467 1.00 20.49 ? 670 HOH D O   1 
HETATM 9935 O  O   . HOH AA 5 .   ? 10.049  19.952  -27.998 1.00 29.55 ? 671 HOH D O   1 
HETATM 9936 O  O   . HOH AA 5 .   ? 14.395  -11.569 -47.334 1.00 31.13 ? 672 HOH D O   1 
HETATM 9937 O  O   . HOH AA 5 .   ? -16.258 10.056  -54.524 1.00 28.42 ? 673 HOH D O   1 
HETATM 9938 O  O   . HOH AA 5 .   ? 16.313  1.131   -55.343 1.00 31.31 ? 674 HOH D O   1 
HETATM 9939 O  O   . HOH AA 5 .   ? 23.180  5.273   -18.279 1.00 35.31 ? 675 HOH D O   1 
HETATM 9940 O  O   . HOH AA 5 .   ? 12.200  -12.478 -56.731 1.00 31.59 ? 676 HOH D O   1 
HETATM 9941 O  O   . HOH AA 5 .   ? 18.157  16.282  -50.452 1.00 36.80 ? 677 HOH D O   1 
HETATM 9942 O  O   . HOH AA 5 .   ? 20.781  -1.290  -42.051 1.00 29.40 ? 678 HOH D O   1 
HETATM 9943 O  O   . HOH AA 5 .   ? -22.149 6.302   -49.280 1.00 29.97 ? 679 HOH D O   1 
HETATM 9944 O  O   . HOH AA 5 .   ? 22.702  7.536   -42.514 1.00 25.96 ? 680 HOH D O   1 
HETATM 9945 O  O   . HOH AA 5 .   ? 19.713  13.257  -54.602 1.00 43.70 ? 681 HOH D O   1 
HETATM 9946 O  O   . HOH AA 5 .   ? 3.949   16.989  -48.705 1.00 37.03 ? 682 HOH D O   1 
HETATM 9947 O  O   . HOH AA 5 .   ? 8.282   -17.720 -29.665 1.00 44.24 ? 683 HOH D O   1 
HETATM 9948 O  O   . HOH AA 5 .   ? 3.263   -6.839  -57.950 1.00 25.17 ? 684 HOH D O   1 
HETATM 9949 O  O   . HOH AA 5 .   ? -6.717  -9.228  -26.727 1.00 26.25 ? 685 HOH D O   1 
HETATM 9950 O  O   . HOH AA 5 .   ? -6.456  7.768   -57.242 1.00 27.64 ? 686 HOH D O   1 
HETATM 9951 O  O   . HOH AA 5 .   ? -1.149  -12.409 -39.075 1.00 25.71 ? 687 HOH D O   1 
HETATM 9952 O  O   . HOH AA 5 .   ? 4.521   -15.676 -35.887 1.00 39.99 ? 688 HOH D O   1 
HETATM 9953 O  O   . HOH AA 5 .   ? -3.087  -9.886  -20.935 1.00 23.58 ? 689 HOH D O   1 
HETATM 9954 O  O   . HOH AA 5 .   ? 10.004  -12.003 -33.195 1.00 28.46 ? 690 HOH D O   1 
HETATM 9955 O  O   . HOH AA 5 .   ? 19.875  -11.241 -27.297 1.00 33.66 ? 691 HOH D O   1 
HETATM 9956 O  O   . HOH AA 5 .   ? 0.559   6.641   -16.719 1.00 32.81 ? 692 HOH D O   1 
HETATM 9957 O  O   . HOH AA 5 .   ? -4.467  -14.656 -46.330 1.00 34.57 ? 693 HOH D O   1 
HETATM 9958 O  O   . HOH AA 5 .   ? 1.492   -15.512 -39.623 1.00 35.66 ? 694 HOH D O   1 
HETATM 9959 O  O   . HOH AA 5 .   ? -3.902  -8.733  -18.487 1.00 21.99 ? 695 HOH D O   1 
HETATM 9960 O  O   . HOH AA 5 .   ? 14.620  -0.478  -58.265 1.00 39.59 ? 696 HOH D O   1 
HETATM 9961 O  O   . HOH AA 5 .   ? -14.616 9.312   -41.940 1.00 32.13 ? 697 HOH D O   1 
HETATM 9962 O  O   . HOH AA 5 .   ? -8.277  -10.717 -41.734 1.00 39.25 ? 698 HOH D O   1 
HETATM 9963 O  O   . HOH AA 5 .   ? 19.891  -5.734  -41.886 1.00 19.55 ? 699 HOH D O   1 
HETATM 9964 O  O   . HOH AA 5 .   ? -7.798  -6.319  -18.032 1.00 37.14 ? 700 HOH D O   1 
HETATM 9965 O  O   . HOH AA 5 .   ? 25.553  10.980  -50.341 1.00 42.69 ? 701 HOH D O   1 
HETATM 9966 O  O   . HOH AA 5 .   ? -1.268  16.034  -57.686 1.00 40.58 ? 702 HOH D O   1 
HETATM 9967 O  O   . HOH AA 5 .   ? 14.835  26.090  -35.297 1.00 31.91 ? 703 HOH D O   1 
HETATM 9968 O  O   . HOH AA 5 .   ? 10.721  3.867   -19.087 1.00 21.19 ? 704 HOH D O   1 
HETATM 9969 O  O   . HOH AA 5 .   ? 18.658  7.908   -52.993 1.00 35.04 ? 705 HOH D O   1 
HETATM 9970 O  O   . HOH AA 5 .   ? -6.504  -9.196  -52.856 1.00 29.09 ? 706 HOH D O   1 
HETATM 9971 O  O   . HOH AA 5 .   ? 12.002  20.731  -32.408 1.00 19.23 ? 707 HOH D O   1 
HETATM 9972 O  O   . HOH AA 5 .   ? -14.679 -4.413  -45.404 1.00 36.29 ? 708 HOH D O   1 
HETATM 9973 O  O   . HOH AA 5 .   ? 12.221  -12.822 -33.858 1.00 42.68 ? 709 HOH D O   1 
HETATM 9974 O  O   . HOH AA 5 .   ? -2.465  22.013  -25.761 1.00 30.78 ? 710 HOH D O   1 
HETATM 9975 O  O   . HOH AA 5 .   ? 7.263   20.504  -33.839 1.00 24.44 ? 711 HOH D O   1 
HETATM 9976 O  O   . HOH AA 5 .   ? -4.631  -13.561 -26.704 1.00 53.32 ? 712 HOH D O   1 
HETATM 9977 O  O   . HOH AA 5 .   ? 27.611  13.032  -49.743 1.00 36.50 ? 713 HOH D O   1 
HETATM 9978 O  O   . HOH AA 5 .   ? 7.070   -8.479  -58.917 1.00 22.65 ? 714 HOH D O   1 
HETATM 9979 O  O   . HOH AA 5 .   ? 14.947  9.601   -18.556 1.00 34.63 ? 715 HOH D O   1 
HETATM 9980 O  O   . HOH AA 5 .   ? 14.762  24.506  -31.976 1.00 27.90 ? 716 HOH D O   1 
HETATM 9981 O  O   . HOH AA 5 .   ? -6.630  -8.773  -18.214 1.00 22.60 ? 717 HOH D O   1 
HETATM 9982 O  O   . HOH AA 5 .   ? 1.508   -19.583 -38.824 1.00 30.89 ? 718 HOH D O   1 
HETATM 9983 O  O   . HOH AA 5 .   ? 11.755  6.251   -19.472 1.00 30.29 ? 719 HOH D O   1 
HETATM 9984 O  O   . HOH AA 5 .   ? -4.480  -14.140 -41.593 1.00 35.94 ? 720 HOH D O   1 
HETATM 9985 O  O   . HOH AA 5 .   ? -4.929  -11.311 -22.027 1.00 39.82 ? 721 HOH D O   1 
HETATM 9986 O  O   . HOH AA 5 .   ? 10.255  8.460   -19.354 1.00 30.95 ? 722 HOH D O   1 
HETATM 9987 O  O   . HOH AA 5 .   ? 8.436   20.835  -36.459 1.00 39.36 ? 723 HOH D O   1 
HETATM 9988 O  O   . HOH AA 5 .   ? -7.719  -10.278 -20.212 1.00 34.83 ? 724 HOH D O   1 
HETATM 9989 O  O   . HOH AA 5 .   ? -7.196  -10.810 -24.404 1.00 32.81 ? 725 HOH D O   1 
HETATM 9990 O  O   . HOH AA 5 .   ? -9.155  -12.162 -50.085 1.00 36.60 ? 726 HOH D O   1 
HETATM 9991 O  O   . HOH AA 5 .   ? -3.531  -15.809 -43.439 1.00 36.57 ? 727 HOH D O   1 
# 
