data_4QJ0
# 
_entry.id   4QJ0 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.398 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   4QJ0         pdb_00004qj0 10.2210/pdb4qj0/pdb 
RCSB  RCSB086115   ?            ?                   
WWPDB D_1000086115 ?            ?                   
# 
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 2015-04-15 
2 'Structure model' 1 1 2018-05-16 
3 'Structure model' 1 2 2023-11-08 
4 'Structure model' 1 3 2024-10-30 
# 
_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' 'Refinement description' 
3 3 'Structure model' 'Data collection'        
4 3 'Structure model' 'Database references'    
5 3 'Structure model' 'Derived calculations'   
6 3 'Structure model' 'Refinement description' 
7 4 'Structure model' 'Structure summary'      
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1  2 'Structure model' diffrn_source                 
2  2 'Structure model' software                      
3  3 'Structure model' chem_comp_atom                
4  3 'Structure model' chem_comp_bond                
5  3 'Structure model' database_2                    
6  3 'Structure model' pdbx_initial_refinement_model 
7  3 'Structure model' pdbx_struct_conn_angle        
8  3 'Structure model' struct_conn                   
9  3 'Structure model' struct_ref_seq_dif            
10 3 'Structure model' struct_site                   
11 4 'Structure model' pdbx_entry_details            
12 4 'Structure model' pdbx_modification_feature     
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1  2 'Structure model' '_diffrn_source.pdbx_synchrotron_site'        
2  2 'Structure model' '_software.version'                           
3  3 'Structure model' '_database_2.pdbx_DOI'                        
4  3 'Structure model' '_database_2.pdbx_database_accession'         
5  3 'Structure model' '_pdbx_struct_conn_angle.ptnr1_auth_asym_id'  
6  3 'Structure model' '_pdbx_struct_conn_angle.ptnr1_auth_comp_id'  
7  3 'Structure model' '_pdbx_struct_conn_angle.ptnr1_auth_seq_id'   
8  3 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_alt_id'  
9  3 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_asym_id' 
10 3 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_atom_id' 
11 3 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_comp_id' 
12 3 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_seq_id'  
13 3 'Structure model' '_pdbx_struct_conn_angle.ptnr2_auth_asym_id'  
14 3 'Structure model' '_pdbx_struct_conn_angle.ptnr2_label_asym_id' 
15 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_auth_asym_id'  
16 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_auth_comp_id'  
17 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_auth_seq_id'   
18 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_alt_id'  
19 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_asym_id' 
20 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_atom_id' 
21 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_comp_id' 
22 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_seq_id'  
23 3 'Structure model' '_pdbx_struct_conn_angle.value'               
24 3 'Structure model' '_struct_conn.pdbx_dist_value'                
25 3 'Structure model' '_struct_conn.pdbx_ptnr2_label_alt_id'        
26 3 'Structure model' '_struct_conn.ptnr1_auth_asym_id'             
27 3 'Structure model' '_struct_conn.ptnr1_auth_comp_id'             
28 3 'Structure model' '_struct_conn.ptnr1_auth_seq_id'              
29 3 'Structure model' '_struct_conn.ptnr1_label_asym_id'            
30 3 'Structure model' '_struct_conn.ptnr1_label_atom_id'            
31 3 'Structure model' '_struct_conn.ptnr1_label_comp_id'            
32 3 'Structure model' '_struct_conn.ptnr1_label_seq_id'             
33 3 'Structure model' '_struct_conn.ptnr2_auth_asym_id'             
34 3 'Structure model' '_struct_conn.ptnr2_auth_comp_id'             
35 3 'Structure model' '_struct_conn.ptnr2_auth_seq_id'              
36 3 'Structure model' '_struct_conn.ptnr2_label_asym_id'            
37 3 'Structure model' '_struct_conn.ptnr2_label_atom_id'            
38 3 'Structure model' '_struct_conn.ptnr2_label_comp_id'            
39 3 'Structure model' '_struct_ref_seq_dif.details'                 
40 3 'Structure model' '_struct_site.pdbx_auth_asym_id'              
41 3 'Structure model' '_struct_site.pdbx_auth_comp_id'              
42 3 'Structure model' '_struct_site.pdbx_auth_seq_id'               
# 
_pdbx_database_status.entry_id                        4QJ0 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.recvd_initial_deposition_date   2014-06-03 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_nmr_data            ? 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.db_id 
_pdbx_database_related.details 
_pdbx_database_related.content_type 
PDB 4QIY . unspecified 
PDB 4QIZ . unspecified 
PDB 4QJM . unspecified 
PDB 4QJO . unspecified 
PDB 4QJP . unspecified 
PDB 4QJW . unspecified 
PDB 4QJX . unspecified 
PDB 4QTL . unspecified 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Manakova, E.' 1 
'Smirnov, A.'  2 
'Grazulis, S.' 3 
# 
_citation.id                        primary 
_citation.title                     
'Functionalization of Fluorinated Benzenesulfonamides and Their Inhibitory Properties toward Carbonic Anhydrases' 
_citation.journal_abbrev            Chemmedchem 
_citation.journal_volume            10 
_citation.page_first                662 
_citation.page_last                 687 
_citation.year                      2015 
_citation.journal_id_ASTM           ? 
_citation.country                   DE 
_citation.journal_id_ISSN           1860-7179 
_citation.journal_id_CSD            ? 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   25758852 
_citation.pdbx_database_id_DOI      10.1002/cmdc.201402490 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Dudutiene, V.'     1  ? 
primary 'Zubriene, A.'      2  ? 
primary 'Smirnov, A.'       3  ? 
primary 'Timm, D.D.'        4  ? 
primary 'Smirnoviene, J.'   5  ? 
primary 'Kazokaite, J.'     6  ? 
primary 'Michailoviene, V.' 7  ? 
primary 'Zaksauskas, A.'    8  ? 
primary 'Manakova, E.'      9  ? 
primary 'Grazulis, S.'      10 ? 
primary 'Matulis, D.'       11 ? 
# 
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 ? 'UNP residues 30-291' ? 
2 non-polymer syn 'ZINC ION'                                                                                                      
65.409    4    ?       ? ?                     ? 
3 non-polymer syn 1,2-ETHANEDIOL                                                                                                  
62.068    6    ?       ? ?                     ? 
4 non-polymer syn '2,3,6-trifluoro-5-{[(1R,2S)-2-hydroxy-1,2-diphenylethyl]amino}-4-[(2-hydroxyethyl)sulfonyl]benzenesulfonamide' 
530.537   4    ?       ? ?                     ? 
5 water       nat water                                                                                                           
18.015    1042 ?       ? ?                     ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Carbonate dehydratase XII, Carbonic anhydrase XII, CA-XII, Tumor antigen HOM-RCC-3.1.3' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MSKWTYFGPDGENSWSKKYPSCGGLLQSPIDLHSDILQYDASLTPLEFQGYNLSANKQFLLTNNGHSVKLNLPSDMHIQG
LQSRYSATQLHLHWGNPNDPHGSEHTVSGQHFAAELHIVHYNSDLYPDASTASNKSEGLAVLAVLIEMGSFNPSYDKIFS
HLQHVKYKGQEAFVPGFNIEELLPERTAEYYRYRGSLTTPPCNPTVLWTVFRNPVQISQEQLLALETALYCTHMDDPSPR
EMINNFRQVQKFDERLVYTSFSQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MSKWTYFGPDGENSWSKKYPSCGGLLQSPIDLHSDILQYDASLTPLEFQGYNLSANKQFLLTNNGHSVKLNLPSDMHIQG
LQSRYSATQLHLHWGNPNDPHGSEHTVSGQHFAAELHIVHYNSDLYPDASTASNKSEGLAVLAVLIEMGSFNPSYDKIFS
HLQHVKYKGQEAFVPGFNIEELLPERTAEYYRYRGSLTTPPCNPTVLWTVFRNPVQISQEQLLALETALYCTHMDDPSPR
EMINNFRQVQKFDERLVYTSFSQ
;
_entity_poly.pdbx_strand_id                 A,B,C,D 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'ZINC ION'                                                                                                      ZN  
3 1,2-ETHANEDIOL                                                                                                  EDO 
4 '2,3,6-trifluoro-5-{[(1R,2S)-2-hydroxy-1,2-diphenylethyl]amino}-4-[(2-hydroxyethyl)sulfonyl]benzenesulfonamide' WWX 
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                      ? 
_entity_src_gen.pdbx_beg_seq_num                   ? 
_entity_src_gen.pdbx_end_seq_num                   ? 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 CA12 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               'Rosetta(DE3)' 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pET21a 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE ?                 'C3 H7 N O2'          89.093  
ARG 'L-peptide linking' y ARGININE ?                 'C6 H15 N4 O2 1'      175.209 
ASN 'L-peptide linking' y ASPARAGINE ?                 'C4 H8 N2 O3'         132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ?                 'C4 H7 N O4'          133.103 
CYS 'L-peptide linking' y CYSTEINE ?                 'C3 H7 N O2 S'        121.158 
EDO non-polymer         . 1,2-ETHANEDIOL 'ETHYLENE GLYCOL' 'C2 H6 O2'            62.068  
GLN 'L-peptide linking' y GLUTAMINE ?                 'C5 H10 N2 O3'        146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ?                 'C5 H9 N O4'          147.129 
GLY 'peptide linking'   y GLYCINE ?                 'C2 H5 N O2'          75.067  
HIS 'L-peptide linking' y HISTIDINE ?                 'C6 H10 N3 O2 1'      156.162 
HOH non-polymer         . WATER ?                 'H2 O'                18.015  
ILE 'L-peptide linking' y ISOLEUCINE ?                 'C6 H13 N O2'         131.173 
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 
WWX non-polymer         . 
'2,3,6-trifluoro-5-{[(1R,2S)-2-hydroxy-1,2-diphenylethyl]amino}-4-[(2-hydroxyethyl)sulfonyl]benzenesulfonamide' ?                 
'C22 H21 F3 N2 O6 S2' 530.537 
ZN  non-polymer         . 'ZINC ION' ?                 'Zn 2'                65.409  
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   SER 2   2   ?   ?   ?   A . n 
A 1 3   LYS 3   3   3   LYS LYS A . n 
A 1 4   TRP 4   4   4   TRP TRP A . n 
A 1 5   THR 5   5   5   THR THR A . n 
A 1 6   TYR 6   6   6   TYR TYR A . n 
A 1 7   PHE 7   7   7   PHE PHE A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   PRO 9   9   9   PRO PRO A . n 
A 1 10  ASP 10  10  10  ASP ASP A . n 
A 1 11  GLY 11  11  11  GLY GLY A . n 
A 1 12  GLU 12  12  12  GLU GLU A . n 
A 1 13  ASN 13  13  13  ASN ASN A . n 
A 1 14  SER 14  14  14  SER SER A . n 
A 1 15  TRP 15  15  15  TRP TRP A . n 
A 1 16  SER 16  16  16  SER SER A . n 
A 1 17  LYS 17  17  17  LYS LYS A . n 
A 1 18  LYS 18  18  18  LYS LYS A . n 
A 1 19  TYR 19  19  19  TYR TYR A . n 
A 1 20  PRO 20  20  20  PRO PRO A . n 
A 1 21  SER 21  21  21  SER SER A . n 
A 1 22  CYS 22  22  22  CYS CYS A . n 
A 1 23  GLY 23  23  23  GLY GLY A . n 
A 1 24  GLY 24  24  24  GLY GLY A . n 
A 1 25  LEU 25  25  25  LEU LEU A . n 
A 1 26  LEU 26  26  26  LEU LEU A . n 
A 1 27  GLN 27  27  27  GLN GLN A . n 
A 1 28  SER 28  28  28  SER SER A . n 
A 1 29  PRO 29  29  29  PRO PRO A . n 
A 1 30  ILE 30  30  30  ILE ILE A . n 
A 1 31  ASP 31  31  31  ASP ASP A . n 
A 1 32  LEU 32  32  32  LEU LEU A . n 
A 1 33  HIS 33  33  33  HIS HIS A . n 
A 1 34  SER 34  34  34  SER SER A . n 
A 1 35  ASP 35  35  35  ASP ASP A . n 
A 1 36  ILE 36  36  36  ILE ILE A . n 
A 1 37  LEU 37  37  37  LEU LEU A . n 
A 1 38  GLN 38  38  38  GLN GLN A . n 
A 1 39  TYR 39  39  39  TYR TYR A . n 
A 1 40  ASP 40  40  40  ASP ASP A . n 
A 1 41  ALA 41  41  41  ALA ALA A . n 
A 1 42  SER 42  42  42  SER SER A . n 
A 1 43  LEU 43  43  43  LEU LEU A . n 
A 1 44  THR 44  44  44  THR THR A . n 
A 1 45  PRO 45  45  45  PRO PRO A . n 
A 1 46  LEU 46  46  46  LEU LEU A . n 
A 1 47  GLU 47  47  47  GLU GLU A . n 
A 1 48  PHE 48  48  48  PHE PHE A . n 
A 1 49  GLN 49  49  49  GLN GLN A . n 
A 1 50  GLY 50  50  50  GLY GLY A . n 
A 1 51  TYR 51  51  51  TYR TYR A . n 
A 1 52  ASN 52  52  52  ASN ASN A . n 
A 1 53  LEU 53  53  53  LEU LEU A . n 
A 1 54  SER 54  54  54  SER SER A . n 
A 1 55  ALA 55  55  55  ALA ALA A . n 
A 1 56  ASN 56  56  56  ASN ASN A . n 
A 1 57  LYS 57  57  57  LYS LYS A . n 
A 1 58  GLN 58  58  58  GLN GLN A . n 
A 1 59  PHE 59  59  59  PHE PHE A . n 
A 1 60  LEU 60  60  60  LEU LEU A . n 
A 1 61  LEU 61  61  61  LEU LEU A . n 
A 1 62  THR 62  62  62  THR THR A . n 
A 1 63  ASN 63  63  63  ASN ASN A . n 
A 1 64  ASN 64  64  64  ASN ASN A . n 
A 1 65  GLY 65  65  65  GLY GLY A . n 
A 1 66  HIS 66  66  66  HIS HIS A . n 
A 1 67  SER 67  67  67  SER SER A . n 
A 1 68  VAL 68  68  68  VAL VAL A . n 
A 1 69  LYS 69  69  69  LYS LYS A . n 
A 1 70  LEU 70  70  70  LEU LEU A . n 
A 1 71  ASN 71  71  71  ASN ASN A . n 
A 1 72  LEU 72  72  72  LEU LEU A . n 
A 1 73  PRO 73  73  73  PRO PRO A . n 
A 1 74  SER 74  74  74  SER SER A . n 
A 1 75  ASP 75  75  75  ASP ASP A . n 
A 1 76  MET 76  76  76  MET MET A . n 
A 1 77  HIS 77  77  77  HIS HIS A . n 
A 1 78  ILE 78  78  78  ILE ILE A . n 
A 1 79  GLN 79  79  79  GLN GLN A . n 
A 1 80  GLY 80  80  80  GLY GLY A . n 
A 1 81  LEU 81  81  81  LEU LEU A . n 
A 1 82  GLN 82  82  82  GLN GLN A . n 
A 1 83  SER 83  83  83  SER SER A . n 
A 1 84  ARG 84  84  84  ARG ARG A . n 
A 1 85  TYR 85  85  85  TYR TYR A . n 
A 1 86  SER 86  86  86  SER SER A . n 
A 1 87  ALA 87  87  87  ALA ALA A . n 
A 1 88  THR 88  88  88  THR THR A . n 
A 1 89  GLN 89  89  89  GLN GLN A . n 
A 1 90  LEU 90  90  90  LEU LEU A . n 
A 1 91  HIS 91  91  91  HIS HIS A . n 
A 1 92  LEU 92  92  92  LEU LEU A . n 
A 1 93  HIS 93  93  93  HIS HIS A . n 
A 1 94  TRP 94  94  94  TRP TRP A . n 
A 1 95  GLY 95  95  95  GLY GLY A . n 
A 1 96  ASN 96  96  96  ASN ASN A . n 
A 1 97  PRO 97  97  97  PRO PRO A . n 
A 1 98  ASN 98  98  98  ASN ASN A . n 
A 1 99  ASP 99  99  99  ASP ASP A . n 
A 1 100 PRO 100 100 100 PRO PRO A . n 
A 1 101 HIS 101 101 101 HIS HIS A . n 
A 1 102 GLY 102 102 102 GLY GLY A . n 
A 1 103 SER 103 103 103 SER SER A . n 
A 1 104 GLU 104 104 104 GLU GLU A . n 
A 1 105 HIS 105 105 105 HIS HIS A . n 
A 1 106 THR 106 106 106 THR THR A . n 
A 1 107 VAL 107 107 107 VAL VAL A . n 
A 1 108 SER 108 108 108 SER SER A . n 
A 1 109 GLY 109 109 109 GLY GLY A . n 
A 1 110 GLN 110 110 110 GLN GLN A . n 
A 1 111 HIS 111 111 111 HIS HIS A . n 
A 1 112 PHE 112 112 112 PHE PHE A . n 
A 1 113 ALA 113 113 113 ALA ALA A . n 
A 1 114 ALA 114 114 114 ALA ALA A . n 
A 1 115 GLU 115 115 115 GLU GLU A . n 
A 1 116 LEU 116 116 116 LEU LEU A . n 
A 1 117 HIS 117 117 117 HIS HIS A . n 
A 1 118 ILE 118 118 118 ILE ILE A . n 
A 1 119 VAL 119 119 119 VAL VAL A . n 
A 1 120 HIS 120 120 120 HIS HIS A . n 
A 1 121 TYR 121 121 121 TYR TYR A . n 
A 1 122 ASN 122 122 122 ASN ASN A . n 
A 1 123 SER 123 123 123 SER SER A . n 
A 1 124 ASP 124 124 124 ASP ASP A . n 
A 1 125 LEU 125 125 125 LEU LEU A . n 
A 1 126 TYR 126 126 126 TYR TYR A . n 
A 1 127 PRO 127 127 127 PRO PRO A . n 
A 1 128 ASP 128 128 128 ASP ASP A . n 
A 1 129 ALA 129 129 129 ALA ALA A . n 
A 1 130 SER 130 130 130 SER SER A . n 
A 1 131 THR 131 131 131 THR THR A . n 
A 1 132 ALA 132 132 132 ALA ALA A . n 
A 1 133 SER 133 133 133 SER SER A . n 
A 1 134 ASN 134 134 134 ASN ASN A . n 
A 1 135 LYS 135 135 135 LYS LYS A . n 
A 1 136 SER 136 136 136 SER SER A . n 
A 1 137 GLU 137 137 137 GLU GLU A . n 
A 1 138 GLY 138 138 138 GLY GLY A . n 
A 1 139 LEU 139 139 139 LEU LEU A . n 
A 1 140 ALA 140 140 140 ALA ALA A . n 
A 1 141 VAL 141 141 141 VAL VAL A . n 
A 1 142 LEU 142 142 142 LEU LEU A . n 
A 1 143 ALA 143 143 143 ALA ALA A . n 
A 1 144 VAL 144 144 144 VAL VAL A . n 
A 1 145 LEU 145 145 145 LEU LEU A . n 
A 1 146 ILE 146 146 146 ILE ILE A . n 
A 1 147 GLU 147 147 147 GLU GLU A . n 
A 1 148 MET 148 148 148 MET MET A . n 
A 1 149 GLY 149 149 149 GLY GLY A . n 
A 1 150 SER 150 150 150 SER SER A . n 
A 1 151 PHE 151 151 151 PHE PHE A . n 
A 1 152 ASN 152 152 152 ASN ASN A . n 
A 1 153 PRO 153 153 153 PRO PRO A . n 
A 1 154 SER 154 154 154 SER SER A . n 
A 1 155 TYR 155 155 155 TYR TYR A . n 
A 1 156 ASP 156 156 156 ASP ASP A . n 
A 1 157 LYS 157 157 157 LYS LYS A . n 
A 1 158 ILE 158 158 158 ILE ILE A . n 
A 1 159 PHE 159 159 159 PHE PHE A . n 
A 1 160 SER 160 160 160 SER SER A . n 
A 1 161 HIS 161 161 161 HIS HIS A . n 
A 1 162 LEU 162 162 162 LEU LEU A . n 
A 1 163 GLN 163 163 163 GLN GLN A . n 
A 1 164 HIS 164 164 164 HIS HIS A . n 
A 1 165 VAL 165 165 165 VAL VAL A . n 
A 1 166 LYS 166 166 166 LYS LYS A . n 
A 1 167 TYR 167 167 167 TYR TYR A . n 
A 1 168 LYS 168 168 168 LYS LYS A . n 
A 1 169 GLY 169 169 169 GLY GLY A . n 
A 1 170 GLN 170 170 170 GLN GLN A . n 
A 1 171 GLU 171 171 171 GLU GLU A . n 
A 1 172 ALA 172 172 172 ALA ALA A . n 
A 1 173 PHE 173 173 173 PHE PHE A . n 
A 1 174 VAL 174 174 174 VAL VAL A . n 
A 1 175 PRO 175 175 175 PRO PRO A . n 
A 1 176 GLY 176 176 176 GLY GLY A . n 
A 1 177 PHE 177 177 177 PHE PHE A . n 
A 1 178 ASN 178 178 178 ASN ASN A . n 
A 1 179 ILE 179 179 179 ILE ILE A . n 
A 1 180 GLU 180 180 180 GLU GLU A . n 
A 1 181 GLU 181 181 181 GLU GLU A . n 
A 1 182 LEU 182 182 182 LEU LEU A . n 
A 1 183 LEU 183 183 183 LEU LEU A . n 
A 1 184 PRO 184 184 184 PRO PRO A . n 
A 1 185 GLU 185 185 185 GLU GLU A . n 
A 1 186 ARG 186 186 186 ARG ARG A . n 
A 1 187 THR 187 187 187 THR THR A . n 
A 1 188 ALA 188 188 188 ALA ALA A . n 
A 1 189 GLU 189 189 189 GLU GLU A . n 
A 1 190 TYR 190 190 190 TYR TYR A . n 
A 1 191 TYR 191 191 191 TYR TYR A . n 
A 1 192 ARG 192 192 192 ARG ARG A . n 
A 1 193 TYR 193 193 193 TYR TYR A . n 
A 1 194 ARG 194 194 194 ARG ARG A . n 
A 1 195 GLY 195 195 195 GLY GLY A . n 
A 1 196 SER 196 196 196 SER SER A . n 
A 1 197 LEU 197 197 197 LEU LEU A . n 
A 1 198 THR 198 198 198 THR THR A . n 
A 1 199 THR 199 199 199 THR THR A . n 
A 1 200 PRO 200 200 200 PRO PRO A . n 
A 1 201 PRO 201 201 201 PRO PRO A . n 
A 1 202 CYS 202 202 202 CYS CYS A . n 
A 1 203 ASN 203 203 203 ASN ASN A . n 
A 1 204 PRO 204 204 204 PRO PRO A . n 
A 1 205 THR 205 205 205 THR THR A . n 
A 1 206 VAL 206 206 206 VAL VAL A . n 
A 1 207 LEU 207 207 207 LEU LEU A . n 
A 1 208 TRP 208 208 208 TRP TRP A . n 
A 1 209 THR 209 209 209 THR THR A . n 
A 1 210 VAL 210 210 210 VAL VAL A . n 
A 1 211 PHE 211 211 211 PHE PHE A . n 
A 1 212 ARG 212 212 212 ARG ARG A . n 
A 1 213 ASN 213 213 213 ASN ASN A . n 
A 1 214 PRO 214 214 214 PRO PRO A . n 
A 1 215 VAL 215 215 215 VAL VAL A . n 
A 1 216 GLN 216 216 216 GLN GLN A . n 
A 1 217 ILE 217 217 217 ILE ILE A . n 
A 1 218 SER 218 218 218 SER SER A . n 
A 1 219 GLN 219 219 219 GLN GLN A . n 
A 1 220 GLU 220 220 220 GLU GLU A . n 
A 1 221 GLN 221 221 221 GLN GLN A . n 
A 1 222 LEU 222 222 222 LEU LEU A . n 
A 1 223 LEU 223 223 223 LEU LEU A . n 
A 1 224 ALA 224 224 224 ALA ALA A . n 
A 1 225 LEU 225 225 225 LEU LEU A . n 
A 1 226 GLU 226 226 226 GLU GLU A . n 
A 1 227 THR 227 227 227 THR THR A . n 
A 1 228 ALA 228 228 228 ALA ALA A . n 
A 1 229 LEU 229 229 229 LEU LEU A . n 
A 1 230 TYR 230 230 230 TYR TYR A . n 
A 1 231 CYS 231 231 231 CYS CYS A . n 
A 1 232 THR 232 232 232 THR THR A . n 
A 1 233 HIS 233 233 233 HIS HIS A . n 
A 1 234 MET 234 234 234 MET MET A . n 
A 1 235 ASP 235 235 235 ASP ASP A . n 
A 1 236 ASP 236 236 236 ASP ASP A . n 
A 1 237 PRO 237 237 237 PRO PRO A . n 
A 1 238 SER 238 238 238 SER SER A . n 
A 1 239 PRO 239 239 239 PRO PRO A . n 
A 1 240 ARG 240 240 240 ARG ARG A . n 
A 1 241 GLU 241 241 241 GLU GLU A . n 
A 1 242 MET 242 242 242 MET MET A . n 
A 1 243 ILE 243 243 243 ILE ILE A . n 
A 1 244 ASN 244 244 244 ASN ASN A . n 
A 1 245 ASN 245 245 245 ASN ASN A . n 
A 1 246 PHE 246 246 246 PHE PHE A . n 
A 1 247 ARG 247 247 247 ARG ARG A . n 
A 1 248 GLN 248 248 248 GLN GLN A . n 
A 1 249 VAL 249 249 249 VAL VAL A . n 
A 1 250 GLN 250 250 250 GLN GLN A . n 
A 1 251 LYS 251 251 251 LYS LYS A . n 
A 1 252 PHE 252 252 252 PHE PHE A . n 
A 1 253 ASP 253 253 253 ASP ASP A . n 
A 1 254 GLU 254 254 254 GLU GLU A . n 
A 1 255 ARG 255 255 255 ARG ARG A . n 
A 1 256 LEU 256 256 256 LEU LEU A . n 
A 1 257 VAL 257 257 257 VAL VAL A . n 
A 1 258 TYR 258 258 258 TYR TYR A . n 
A 1 259 THR 259 259 259 THR THR A . n 
A 1 260 SER 260 260 260 SER SER A . n 
A 1 261 PHE 261 261 261 PHE PHE A . n 
A 1 262 SER 262 262 262 SER SER A . n 
A 1 263 GLN 263 263 ?   ?   ?   A . n 
B 1 1   MET 1   1   ?   ?   ?   B . n 
B 1 2   SER 2   2   ?   ?   ?   B . n 
B 1 3   LYS 3   3   3   LYS LYS B . n 
B 1 4   TRP 4   4   4   TRP TRP B . n 
B 1 5   THR 5   5   5   THR THR B . n 
B 1 6   TYR 6   6   6   TYR TYR B . n 
B 1 7   PHE 7   7   7   PHE PHE B . n 
B 1 8   GLY 8   8   8   GLY GLY B . n 
B 1 9   PRO 9   9   9   PRO PRO B . n 
B 1 10  ASP 10  10  10  ASP ASP B . n 
B 1 11  GLY 11  11  11  GLY GLY B . n 
B 1 12  GLU 12  12  12  GLU GLU B . n 
B 1 13  ASN 13  13  13  ASN ASN B . n 
B 1 14  SER 14  14  14  SER SER B . n 
B 1 15  TRP 15  15  15  TRP TRP B . n 
B 1 16  SER 16  16  16  SER SER B . n 
B 1 17  LYS 17  17  17  LYS LYS B . n 
B 1 18  LYS 18  18  18  LYS LYS B . n 
B 1 19  TYR 19  19  19  TYR TYR B . n 
B 1 20  PRO 20  20  20  PRO PRO B . n 
B 1 21  SER 21  21  21  SER SER B . n 
B 1 22  CYS 22  22  22  CYS CYS B . n 
B 1 23  GLY 23  23  23  GLY GLY B . n 
B 1 24  GLY 24  24  24  GLY GLY B . n 
B 1 25  LEU 25  25  25  LEU LEU B . n 
B 1 26  LEU 26  26  26  LEU LEU B . n 
B 1 27  GLN 27  27  27  GLN GLN B . n 
B 1 28  SER 28  28  28  SER SER B . n 
B 1 29  PRO 29  29  29  PRO PRO B . n 
B 1 30  ILE 30  30  30  ILE ILE B . n 
B 1 31  ASP 31  31  31  ASP ASP B . n 
B 1 32  LEU 32  32  32  LEU LEU B . n 
B 1 33  HIS 33  33  33  HIS HIS B . n 
B 1 34  SER 34  34  34  SER SER B . n 
B 1 35  ASP 35  35  35  ASP ASP B . n 
B 1 36  ILE 36  36  36  ILE ILE B . n 
B 1 37  LEU 37  37  37  LEU LEU B . n 
B 1 38  GLN 38  38  38  GLN GLN B . n 
B 1 39  TYR 39  39  39  TYR TYR B . n 
B 1 40  ASP 40  40  40  ASP ASP B . n 
B 1 41  ALA 41  41  41  ALA ALA B . n 
B 1 42  SER 42  42  42  SER SER B . n 
B 1 43  LEU 43  43  43  LEU LEU B . n 
B 1 44  THR 44  44  44  THR THR B . n 
B 1 45  PRO 45  45  45  PRO PRO B . n 
B 1 46  LEU 46  46  46  LEU LEU B . n 
B 1 47  GLU 47  47  47  GLU GLU B . n 
B 1 48  PHE 48  48  48  PHE PHE B . n 
B 1 49  GLN 49  49  49  GLN GLN B . n 
B 1 50  GLY 50  50  50  GLY GLY B . n 
B 1 51  TYR 51  51  51  TYR TYR B . n 
B 1 52  ASN 52  52  52  ASN ASN B . n 
B 1 53  LEU 53  53  53  LEU LEU B . n 
B 1 54  SER 54  54  54  SER SER B . n 
B 1 55  ALA 55  55  55  ALA ALA B . n 
B 1 56  ASN 56  56  56  ASN ASN B . n 
B 1 57  LYS 57  57  57  LYS LYS B . n 
B 1 58  GLN 58  58  58  GLN GLN B . n 
B 1 59  PHE 59  59  59  PHE PHE B . n 
B 1 60  LEU 60  60  60  LEU LEU B . n 
B 1 61  LEU 61  61  61  LEU LEU B . n 
B 1 62  THR 62  62  62  THR THR B . n 
B 1 63  ASN 63  63  63  ASN ASN B . n 
B 1 64  ASN 64  64  64  ASN ASN B . n 
B 1 65  GLY 65  65  65  GLY GLY B . n 
B 1 66  HIS 66  66  66  HIS HIS B . n 
B 1 67  SER 67  67  67  SER SER B . n 
B 1 68  VAL 68  68  68  VAL VAL B . n 
B 1 69  LYS 69  69  69  LYS LYS B . n 
B 1 70  LEU 70  70  70  LEU LEU B . n 
B 1 71  ASN 71  71  71  ASN ASN B . n 
B 1 72  LEU 72  72  72  LEU LEU B . n 
B 1 73  PRO 73  73  73  PRO PRO B . n 
B 1 74  SER 74  74  74  SER SER B . n 
B 1 75  ASP 75  75  75  ASP ASP B . n 
B 1 76  MET 76  76  76  MET MET B . n 
B 1 77  HIS 77  77  77  HIS HIS B . n 
B 1 78  ILE 78  78  78  ILE ILE B . n 
B 1 79  GLN 79  79  79  GLN GLN B . n 
B 1 80  GLY 80  80  80  GLY GLY B . n 
B 1 81  LEU 81  81  81  LEU LEU B . n 
B 1 82  GLN 82  82  82  GLN GLN B . n 
B 1 83  SER 83  83  83  SER SER B . n 
B 1 84  ARG 84  84  84  ARG ARG B . n 
B 1 85  TYR 85  85  85  TYR TYR B . n 
B 1 86  SER 86  86  86  SER SER B . n 
B 1 87  ALA 87  87  87  ALA ALA B . n 
B 1 88  THR 88  88  88  THR THR B . n 
B 1 89  GLN 89  89  89  GLN GLN B . n 
B 1 90  LEU 90  90  90  LEU LEU B . n 
B 1 91  HIS 91  91  91  HIS HIS B . n 
B 1 92  LEU 92  92  92  LEU LEU B . n 
B 1 93  HIS 93  93  93  HIS HIS B . n 
B 1 94  TRP 94  94  94  TRP TRP B . n 
B 1 95  GLY 95  95  95  GLY GLY B . n 
B 1 96  ASN 96  96  96  ASN ASN B . n 
B 1 97  PRO 97  97  97  PRO PRO B . n 
B 1 98  ASN 98  98  98  ASN ASN B . n 
B 1 99  ASP 99  99  99  ASP ASP B . n 
B 1 100 PRO 100 100 100 PRO PRO B . n 
B 1 101 HIS 101 101 101 HIS HIS B . n 
B 1 102 GLY 102 102 102 GLY GLY B . n 
B 1 103 SER 103 103 103 SER SER B . n 
B 1 104 GLU 104 104 104 GLU GLU B . n 
B 1 105 HIS 105 105 105 HIS HIS B . n 
B 1 106 THR 106 106 106 THR THR B . n 
B 1 107 VAL 107 107 107 VAL VAL B . n 
B 1 108 SER 108 108 108 SER SER B . n 
B 1 109 GLY 109 109 109 GLY GLY B . n 
B 1 110 GLN 110 110 110 GLN GLN B . n 
B 1 111 HIS 111 111 111 HIS HIS B . n 
B 1 112 PHE 112 112 112 PHE PHE B . n 
B 1 113 ALA 113 113 113 ALA ALA B . n 
B 1 114 ALA 114 114 114 ALA ALA B . n 
B 1 115 GLU 115 115 115 GLU GLU B . n 
B 1 116 LEU 116 116 116 LEU LEU B . n 
B 1 117 HIS 117 117 117 HIS HIS B . n 
B 1 118 ILE 118 118 118 ILE ILE B . n 
B 1 119 VAL 119 119 119 VAL VAL B . n 
B 1 120 HIS 120 120 120 HIS HIS B . n 
B 1 121 TYR 121 121 121 TYR TYR B . n 
B 1 122 ASN 122 122 122 ASN ASN B . n 
B 1 123 SER 123 123 123 SER SER B . n 
B 1 124 ASP 124 124 124 ASP ASP B . n 
B 1 125 LEU 125 125 125 LEU LEU B . n 
B 1 126 TYR 126 126 126 TYR TYR B . n 
B 1 127 PRO 127 127 127 PRO PRO B . n 
B 1 128 ASP 128 128 128 ASP ASP B . n 
B 1 129 ALA 129 129 129 ALA ALA B . n 
B 1 130 SER 130 130 130 SER SER B . n 
B 1 131 THR 131 131 131 THR THR B . n 
B 1 132 ALA 132 132 132 ALA ALA B . n 
B 1 133 SER 133 133 133 SER SER B . n 
B 1 134 ASN 134 134 134 ASN ASN B . n 
B 1 135 LYS 135 135 135 LYS LYS B . n 
B 1 136 SER 136 136 136 SER SER B . n 
B 1 137 GLU 137 137 137 GLU GLU B . n 
B 1 138 GLY 138 138 138 GLY GLY B . n 
B 1 139 LEU 139 139 139 LEU LEU B . n 
B 1 140 ALA 140 140 140 ALA ALA B . n 
B 1 141 VAL 141 141 141 VAL VAL B . n 
B 1 142 LEU 142 142 142 LEU LEU B . n 
B 1 143 ALA 143 143 143 ALA ALA B . n 
B 1 144 VAL 144 144 144 VAL VAL B . n 
B 1 145 LEU 145 145 145 LEU LEU B . n 
B 1 146 ILE 146 146 146 ILE ILE B . n 
B 1 147 GLU 147 147 147 GLU GLU B . n 
B 1 148 MET 148 148 148 MET MET B . n 
B 1 149 GLY 149 149 149 GLY GLY B . n 
B 1 150 SER 150 150 150 SER SER B . n 
B 1 151 PHE 151 151 151 PHE PHE B . n 
B 1 152 ASN 152 152 152 ASN ASN B . n 
B 1 153 PRO 153 153 153 PRO PRO B . n 
B 1 154 SER 154 154 154 SER SER B . n 
B 1 155 TYR 155 155 155 TYR TYR B . n 
B 1 156 ASP 156 156 156 ASP ASP B . n 
B 1 157 LYS 157 157 157 LYS LYS B . n 
B 1 158 ILE 158 158 158 ILE ILE B . n 
B 1 159 PHE 159 159 159 PHE PHE B . n 
B 1 160 SER 160 160 160 SER SER B . n 
B 1 161 HIS 161 161 161 HIS HIS B . n 
B 1 162 LEU 162 162 162 LEU LEU B . n 
B 1 163 GLN 163 163 163 GLN GLN B . n 
B 1 164 HIS 164 164 164 HIS HIS B . n 
B 1 165 VAL 165 165 165 VAL VAL B . n 
B 1 166 LYS 166 166 166 LYS LYS B . n 
B 1 167 TYR 167 167 167 TYR TYR B . n 
B 1 168 LYS 168 168 168 LYS LYS B . n 
B 1 169 GLY 169 169 169 GLY GLY B . n 
B 1 170 GLN 170 170 170 GLN GLN B . n 
B 1 171 GLU 171 171 171 GLU GLU B . n 
B 1 172 ALA 172 172 172 ALA ALA B . n 
B 1 173 PHE 173 173 173 PHE PHE B . n 
B 1 174 VAL 174 174 174 VAL VAL B . n 
B 1 175 PRO 175 175 175 PRO PRO B . n 
B 1 176 GLY 176 176 176 GLY GLY B . n 
B 1 177 PHE 177 177 177 PHE PHE B . n 
B 1 178 ASN 178 178 178 ASN ASN B . n 
B 1 179 ILE 179 179 179 ILE ILE B . n 
B 1 180 GLU 180 180 180 GLU GLU B . n 
B 1 181 GLU 181 181 181 GLU GLU B . n 
B 1 182 LEU 182 182 182 LEU LEU B . n 
B 1 183 LEU 183 183 183 LEU LEU B . n 
B 1 184 PRO 184 184 184 PRO PRO B . n 
B 1 185 GLU 185 185 185 GLU GLU B . n 
B 1 186 ARG 186 186 186 ARG ARG B . n 
B 1 187 THR 187 187 187 THR THR B . n 
B 1 188 ALA 188 188 188 ALA ALA B . n 
B 1 189 GLU 189 189 189 GLU GLU B . n 
B 1 190 TYR 190 190 190 TYR TYR B . n 
B 1 191 TYR 191 191 191 TYR TYR B . n 
B 1 192 ARG 192 192 192 ARG ARG B . n 
B 1 193 TYR 193 193 193 TYR TYR B . n 
B 1 194 ARG 194 194 194 ARG ARG B . n 
B 1 195 GLY 195 195 195 GLY GLY B . n 
B 1 196 SER 196 196 196 SER SER B . n 
B 1 197 LEU 197 197 197 LEU LEU B . n 
B 1 198 THR 198 198 198 THR THR B . n 
B 1 199 THR 199 199 199 THR THR B . n 
B 1 200 PRO 200 200 200 PRO PRO B . n 
B 1 201 PRO 201 201 201 PRO PRO B . n 
B 1 202 CYS 202 202 202 CYS CYS B . n 
B 1 203 ASN 203 203 203 ASN ASN B . n 
B 1 204 PRO 204 204 204 PRO PRO B . n 
B 1 205 THR 205 205 205 THR THR B . n 
B 1 206 VAL 206 206 206 VAL VAL B . n 
B 1 207 LEU 207 207 207 LEU LEU B . n 
B 1 208 TRP 208 208 208 TRP TRP B . n 
B 1 209 THR 209 209 209 THR THR B . n 
B 1 210 VAL 210 210 210 VAL VAL B . n 
B 1 211 PHE 211 211 211 PHE PHE B . n 
B 1 212 ARG 212 212 212 ARG ARG B . n 
B 1 213 ASN 213 213 213 ASN ASN B . n 
B 1 214 PRO 214 214 214 PRO PRO B . n 
B 1 215 VAL 215 215 215 VAL VAL B . n 
B 1 216 GLN 216 216 216 GLN GLN B . n 
B 1 217 ILE 217 217 217 ILE ILE B . n 
B 1 218 SER 218 218 218 SER SER B . n 
B 1 219 GLN 219 219 219 GLN GLN B . n 
B 1 220 GLU 220 220 220 GLU GLU B . n 
B 1 221 GLN 221 221 221 GLN GLN B . n 
B 1 222 LEU 222 222 222 LEU LEU B . n 
B 1 223 LEU 223 223 223 LEU LEU B . n 
B 1 224 ALA 224 224 224 ALA ALA B . n 
B 1 225 LEU 225 225 225 LEU LEU B . n 
B 1 226 GLU 226 226 226 GLU GLU B . n 
B 1 227 THR 227 227 227 THR THR B . n 
B 1 228 ALA 228 228 228 ALA ALA B . n 
B 1 229 LEU 229 229 229 LEU LEU B . n 
B 1 230 TYR 230 230 230 TYR TYR B . n 
B 1 231 CYS 231 231 231 CYS CYS B . n 
B 1 232 THR 232 232 232 THR THR B . n 
B 1 233 HIS 233 233 233 HIS HIS B . n 
B 1 234 MET 234 234 234 MET MET B . n 
B 1 235 ASP 235 235 235 ASP ASP B . n 
B 1 236 ASP 236 236 236 ASP ASP B . n 
B 1 237 PRO 237 237 237 PRO PRO B . n 
B 1 238 SER 238 238 238 SER SER B . n 
B 1 239 PRO 239 239 239 PRO PRO B . n 
B 1 240 ARG 240 240 240 ARG ARG B . n 
B 1 241 GLU 241 241 241 GLU GLU B . n 
B 1 242 MET 242 242 242 MET MET B . n 
B 1 243 ILE 243 243 243 ILE ILE B . n 
B 1 244 ASN 244 244 244 ASN ASN B . n 
B 1 245 ASN 245 245 245 ASN ASN B . n 
B 1 246 PHE 246 246 246 PHE PHE B . n 
B 1 247 ARG 247 247 247 ARG ARG B . n 
B 1 248 GLN 248 248 248 GLN GLN B . n 
B 1 249 VAL 249 249 249 VAL VAL B . n 
B 1 250 GLN 250 250 250 GLN GLN B . n 
B 1 251 LYS 251 251 251 LYS LYS B . n 
B 1 252 PHE 252 252 252 PHE PHE B . n 
B 1 253 ASP 253 253 253 ASP ASP B . n 
B 1 254 GLU 254 254 254 GLU GLU B . n 
B 1 255 ARG 255 255 255 ARG ARG B . n 
B 1 256 LEU 256 256 256 LEU LEU B . n 
B 1 257 VAL 257 257 257 VAL VAL B . n 
B 1 258 TYR 258 258 258 TYR TYR B . n 
B 1 259 THR 259 259 259 THR THR B . n 
B 1 260 SER 260 260 260 SER SER B . n 
B 1 261 PHE 261 261 261 PHE PHE B . n 
B 1 262 SER 262 262 262 SER SER B . n 
B 1 263 GLN 263 263 263 GLN GLN B . n 
C 1 1   MET 1   1   ?   ?   ?   C . n 
C 1 2   SER 2   2   ?   ?   ?   C . n 
C 1 3   LYS 3   3   3   LYS LYS C . n 
C 1 4   TRP 4   4   4   TRP TRP C . n 
C 1 5   THR 5   5   5   THR THR C . n 
C 1 6   TYR 6   6   6   TYR TYR C . n 
C 1 7   PHE 7   7   7   PHE PHE C . n 
C 1 8   GLY 8   8   8   GLY GLY C . n 
C 1 9   PRO 9   9   9   PRO PRO C . n 
C 1 10  ASP 10  10  10  ASP ASP C . n 
C 1 11  GLY 11  11  11  GLY GLY C . n 
C 1 12  GLU 12  12  12  GLU GLU C . n 
C 1 13  ASN 13  13  13  ASN ASN C . n 
C 1 14  SER 14  14  14  SER SER C . n 
C 1 15  TRP 15  15  15  TRP TRP C . n 
C 1 16  SER 16  16  16  SER SER C . n 
C 1 17  LYS 17  17  17  LYS LYS C . n 
C 1 18  LYS 18  18  18  LYS LYS C . n 
C 1 19  TYR 19  19  19  TYR TYR C . n 
C 1 20  PRO 20  20  20  PRO PRO C . n 
C 1 21  SER 21  21  21  SER SER C . n 
C 1 22  CYS 22  22  22  CYS CYS C . n 
C 1 23  GLY 23  23  23  GLY GLY C . n 
C 1 24  GLY 24  24  24  GLY GLY C . n 
C 1 25  LEU 25  25  25  LEU LEU C . n 
C 1 26  LEU 26  26  26  LEU LEU C . n 
C 1 27  GLN 27  27  27  GLN GLN C . n 
C 1 28  SER 28  28  28  SER SER C . n 
C 1 29  PRO 29  29  29  PRO PRO C . n 
C 1 30  ILE 30  30  30  ILE ILE C . n 
C 1 31  ASP 31  31  31  ASP ASP C . n 
C 1 32  LEU 32  32  32  LEU LEU C . n 
C 1 33  HIS 33  33  33  HIS HIS C . n 
C 1 34  SER 34  34  34  SER SER C . n 
C 1 35  ASP 35  35  35  ASP ASP C . n 
C 1 36  ILE 36  36  36  ILE ILE C . n 
C 1 37  LEU 37  37  37  LEU LEU C . n 
C 1 38  GLN 38  38  38  GLN GLN C . n 
C 1 39  TYR 39  39  39  TYR TYR C . n 
C 1 40  ASP 40  40  40  ASP ASP C . n 
C 1 41  ALA 41  41  41  ALA ALA C . n 
C 1 42  SER 42  42  42  SER SER C . n 
C 1 43  LEU 43  43  43  LEU LEU C . n 
C 1 44  THR 44  44  44  THR THR C . n 
C 1 45  PRO 45  45  45  PRO PRO C . n 
C 1 46  LEU 46  46  46  LEU LEU C . n 
C 1 47  GLU 47  47  47  GLU GLU C . n 
C 1 48  PHE 48  48  48  PHE PHE C . n 
C 1 49  GLN 49  49  49  GLN GLN C . n 
C 1 50  GLY 50  50  50  GLY GLY C . n 
C 1 51  TYR 51  51  51  TYR TYR C . n 
C 1 52  ASN 52  52  52  ASN ASN C . n 
C 1 53  LEU 53  53  53  LEU LEU C . n 
C 1 54  SER 54  54  54  SER SER C . n 
C 1 55  ALA 55  55  55  ALA ALA C . n 
C 1 56  ASN 56  56  56  ASN ASN C . n 
C 1 57  LYS 57  57  57  LYS LYS C . n 
C 1 58  GLN 58  58  58  GLN GLN C . n 
C 1 59  PHE 59  59  59  PHE PHE C . n 
C 1 60  LEU 60  60  60  LEU LEU C . n 
C 1 61  LEU 61  61  61  LEU LEU C . n 
C 1 62  THR 62  62  62  THR THR C . n 
C 1 63  ASN 63  63  63  ASN ASN C . n 
C 1 64  ASN 64  64  64  ASN ASN C . n 
C 1 65  GLY 65  65  65  GLY GLY C . n 
C 1 66  HIS 66  66  66  HIS HIS C . n 
C 1 67  SER 67  67  67  SER SER C . n 
C 1 68  VAL 68  68  68  VAL VAL C . n 
C 1 69  LYS 69  69  69  LYS LYS C . n 
C 1 70  LEU 70  70  70  LEU LEU C . n 
C 1 71  ASN 71  71  71  ASN ASN C . n 
C 1 72  LEU 72  72  72  LEU LEU C . n 
C 1 73  PRO 73  73  73  PRO PRO C . n 
C 1 74  SER 74  74  74  SER SER C . n 
C 1 75  ASP 75  75  75  ASP ASP C . n 
C 1 76  MET 76  76  76  MET MET C . n 
C 1 77  HIS 77  77  77  HIS HIS C . n 
C 1 78  ILE 78  78  78  ILE ILE C . n 
C 1 79  GLN 79  79  79  GLN GLN C . n 
C 1 80  GLY 80  80  80  GLY GLY C . n 
C 1 81  LEU 81  81  81  LEU LEU C . n 
C 1 82  GLN 82  82  82  GLN GLN C . n 
C 1 83  SER 83  83  83  SER SER C . n 
C 1 84  ARG 84  84  84  ARG ARG C . n 
C 1 85  TYR 85  85  85  TYR TYR C . n 
C 1 86  SER 86  86  86  SER SER C . n 
C 1 87  ALA 87  87  87  ALA ALA C . n 
C 1 88  THR 88  88  88  THR THR C . n 
C 1 89  GLN 89  89  89  GLN GLN C . n 
C 1 90  LEU 90  90  90  LEU LEU C . n 
C 1 91  HIS 91  91  91  HIS HIS C . n 
C 1 92  LEU 92  92  92  LEU LEU C . n 
C 1 93  HIS 93  93  93  HIS HIS C . n 
C 1 94  TRP 94  94  94  TRP TRP C . n 
C 1 95  GLY 95  95  95  GLY GLY C . n 
C 1 96  ASN 96  96  96  ASN ASN C . n 
C 1 97  PRO 97  97  97  PRO PRO C . n 
C 1 98  ASN 98  98  98  ASN ASN C . n 
C 1 99  ASP 99  99  99  ASP ASP C . n 
C 1 100 PRO 100 100 100 PRO PRO C . n 
C 1 101 HIS 101 101 101 HIS HIS C . n 
C 1 102 GLY 102 102 102 GLY GLY C . n 
C 1 103 SER 103 103 103 SER SER C . n 
C 1 104 GLU 104 104 104 GLU GLU C . n 
C 1 105 HIS 105 105 105 HIS HIS C . n 
C 1 106 THR 106 106 106 THR THR C . n 
C 1 107 VAL 107 107 107 VAL VAL C . n 
C 1 108 SER 108 108 108 SER SER C . n 
C 1 109 GLY 109 109 109 GLY GLY C . n 
C 1 110 GLN 110 110 110 GLN GLN C . n 
C 1 111 HIS 111 111 111 HIS HIS C . n 
C 1 112 PHE 112 112 112 PHE PHE C . n 
C 1 113 ALA 113 113 113 ALA ALA C . n 
C 1 114 ALA 114 114 114 ALA ALA C . n 
C 1 115 GLU 115 115 115 GLU GLU C . n 
C 1 116 LEU 116 116 116 LEU LEU C . n 
C 1 117 HIS 117 117 117 HIS HIS C . n 
C 1 118 ILE 118 118 118 ILE ILE C . n 
C 1 119 VAL 119 119 119 VAL VAL C . n 
C 1 120 HIS 120 120 120 HIS HIS C . n 
C 1 121 TYR 121 121 121 TYR TYR C . n 
C 1 122 ASN 122 122 122 ASN ASN C . n 
C 1 123 SER 123 123 123 SER SER C . n 
C 1 124 ASP 124 124 124 ASP ASP C . n 
C 1 125 LEU 125 125 125 LEU LEU C . n 
C 1 126 TYR 126 126 126 TYR TYR C . n 
C 1 127 PRO 127 127 127 PRO PRO C . n 
C 1 128 ASP 128 128 128 ASP ASP C . n 
C 1 129 ALA 129 129 129 ALA ALA C . n 
C 1 130 SER 130 130 130 SER SER C . n 
C 1 131 THR 131 131 131 THR THR C . n 
C 1 132 ALA 132 132 132 ALA ALA C . n 
C 1 133 SER 133 133 133 SER SER C . n 
C 1 134 ASN 134 134 134 ASN ASN C . n 
C 1 135 LYS 135 135 135 LYS LYS C . n 
C 1 136 SER 136 136 136 SER SER C . n 
C 1 137 GLU 137 137 137 GLU GLU C . n 
C 1 138 GLY 138 138 138 GLY GLY C . n 
C 1 139 LEU 139 139 139 LEU LEU C . n 
C 1 140 ALA 140 140 140 ALA ALA C . n 
C 1 141 VAL 141 141 141 VAL VAL C . n 
C 1 142 LEU 142 142 142 LEU LEU C . n 
C 1 143 ALA 143 143 143 ALA ALA C . n 
C 1 144 VAL 144 144 144 VAL VAL C . n 
C 1 145 LEU 145 145 145 LEU LEU C . n 
C 1 146 ILE 146 146 146 ILE ILE C . n 
C 1 147 GLU 147 147 147 GLU GLU C . n 
C 1 148 MET 148 148 148 MET MET C . n 
C 1 149 GLY 149 149 149 GLY GLY C . n 
C 1 150 SER 150 150 150 SER SER C . n 
C 1 151 PHE 151 151 151 PHE PHE C . n 
C 1 152 ASN 152 152 152 ASN ASN C . n 
C 1 153 PRO 153 153 153 PRO PRO C . n 
C 1 154 SER 154 154 154 SER SER C . n 
C 1 155 TYR 155 155 155 TYR TYR C . n 
C 1 156 ASP 156 156 156 ASP ASP C . n 
C 1 157 LYS 157 157 157 LYS LYS C . n 
C 1 158 ILE 158 158 158 ILE ILE C . n 
C 1 159 PHE 159 159 159 PHE PHE C . n 
C 1 160 SER 160 160 160 SER SER C . n 
C 1 161 HIS 161 161 161 HIS HIS C . n 
C 1 162 LEU 162 162 162 LEU LEU C . n 
C 1 163 GLN 163 163 163 GLN GLN C . n 
C 1 164 HIS 164 164 164 HIS HIS C . n 
C 1 165 VAL 165 165 165 VAL VAL C . n 
C 1 166 LYS 166 166 166 LYS LYS C . n 
C 1 167 TYR 167 167 167 TYR TYR C . n 
C 1 168 LYS 168 168 168 LYS LYS C . n 
C 1 169 GLY 169 169 169 GLY GLY C . n 
C 1 170 GLN 170 170 170 GLN GLN C . n 
C 1 171 GLU 171 171 171 GLU GLU C . n 
C 1 172 ALA 172 172 172 ALA ALA C . n 
C 1 173 PHE 173 173 173 PHE PHE C . n 
C 1 174 VAL 174 174 174 VAL VAL C . n 
C 1 175 PRO 175 175 175 PRO PRO C . n 
C 1 176 GLY 176 176 176 GLY GLY C . n 
C 1 177 PHE 177 177 177 PHE PHE C . n 
C 1 178 ASN 178 178 178 ASN ASN C . n 
C 1 179 ILE 179 179 179 ILE ILE C . n 
C 1 180 GLU 180 180 180 GLU GLU C . n 
C 1 181 GLU 181 181 181 GLU GLU C . n 
C 1 182 LEU 182 182 182 LEU LEU C . n 
C 1 183 LEU 183 183 183 LEU LEU C . n 
C 1 184 PRO 184 184 184 PRO PRO C . n 
C 1 185 GLU 185 185 185 GLU GLU C . n 
C 1 186 ARG 186 186 186 ARG ARG C . n 
C 1 187 THR 187 187 187 THR THR C . n 
C 1 188 ALA 188 188 188 ALA ALA C . n 
C 1 189 GLU 189 189 189 GLU GLU C . n 
C 1 190 TYR 190 190 190 TYR TYR C . n 
C 1 191 TYR 191 191 191 TYR TYR C . n 
C 1 192 ARG 192 192 192 ARG ARG C . n 
C 1 193 TYR 193 193 193 TYR TYR C . n 
C 1 194 ARG 194 194 194 ARG ARG C . n 
C 1 195 GLY 195 195 195 GLY GLY C . n 
C 1 196 SER 196 196 196 SER SER C . n 
C 1 197 LEU 197 197 197 LEU LEU C . n 
C 1 198 THR 198 198 198 THR THR C . n 
C 1 199 THR 199 199 199 THR THR C . n 
C 1 200 PRO 200 200 200 PRO PRO C . n 
C 1 201 PRO 201 201 201 PRO PRO C . n 
C 1 202 CYS 202 202 202 CYS CYS C . n 
C 1 203 ASN 203 203 203 ASN ASN C . n 
C 1 204 PRO 204 204 204 PRO PRO C . n 
C 1 205 THR 205 205 205 THR THR C . n 
C 1 206 VAL 206 206 206 VAL VAL C . n 
C 1 207 LEU 207 207 207 LEU LEU C . n 
C 1 208 TRP 208 208 208 TRP TRP C . n 
C 1 209 THR 209 209 209 THR THR C . n 
C 1 210 VAL 210 210 210 VAL VAL C . n 
C 1 211 PHE 211 211 211 PHE PHE C . n 
C 1 212 ARG 212 212 212 ARG ARG C . n 
C 1 213 ASN 213 213 213 ASN ASN C . n 
C 1 214 PRO 214 214 214 PRO PRO C . n 
C 1 215 VAL 215 215 215 VAL VAL C . n 
C 1 216 GLN 216 216 216 GLN GLN C . n 
C 1 217 ILE 217 217 217 ILE ILE C . n 
C 1 218 SER 218 218 218 SER SER C . n 
C 1 219 GLN 219 219 219 GLN GLN C . n 
C 1 220 GLU 220 220 220 GLU GLU C . n 
C 1 221 GLN 221 221 221 GLN GLN C . n 
C 1 222 LEU 222 222 222 LEU LEU C . n 
C 1 223 LEU 223 223 223 LEU LEU C . n 
C 1 224 ALA 224 224 224 ALA ALA C . n 
C 1 225 LEU 225 225 225 LEU LEU C . n 
C 1 226 GLU 226 226 226 GLU GLU C . n 
C 1 227 THR 227 227 227 THR THR C . n 
C 1 228 ALA 228 228 228 ALA ALA C . n 
C 1 229 LEU 229 229 229 LEU LEU C . n 
C 1 230 TYR 230 230 230 TYR TYR C . n 
C 1 231 CYS 231 231 231 CYS CYS C . n 
C 1 232 THR 232 232 232 THR THR C . n 
C 1 233 HIS 233 233 233 HIS HIS C . n 
C 1 234 MET 234 234 234 MET MET C . n 
C 1 235 ASP 235 235 235 ASP ASP C . n 
C 1 236 ASP 236 236 236 ASP ASP C . n 
C 1 237 PRO 237 237 237 PRO PRO C . n 
C 1 238 SER 238 238 238 SER SER C . n 
C 1 239 PRO 239 239 239 PRO PRO C . n 
C 1 240 ARG 240 240 240 ARG ARG C . n 
C 1 241 GLU 241 241 241 GLU GLU C . n 
C 1 242 MET 242 242 242 MET MET C . n 
C 1 243 ILE 243 243 243 ILE ILE C . n 
C 1 244 ASN 244 244 244 ASN ASN C . n 
C 1 245 ASN 245 245 245 ASN ASN C . n 
C 1 246 PHE 246 246 246 PHE PHE C . n 
C 1 247 ARG 247 247 247 ARG ARG C . n 
C 1 248 GLN 248 248 248 GLN GLN C . n 
C 1 249 VAL 249 249 249 VAL VAL C . n 
C 1 250 GLN 250 250 250 GLN GLN C . n 
C 1 251 LYS 251 251 251 LYS LYS C . n 
C 1 252 PHE 252 252 252 PHE PHE C . n 
C 1 253 ASP 253 253 253 ASP ASP C . n 
C 1 254 GLU 254 254 254 GLU GLU C . n 
C 1 255 ARG 255 255 255 ARG ARG C . n 
C 1 256 LEU 256 256 256 LEU LEU C . n 
C 1 257 VAL 257 257 257 VAL VAL C . n 
C 1 258 TYR 258 258 258 TYR TYR C . n 
C 1 259 THR 259 259 259 THR THR C . n 
C 1 260 SER 260 260 260 SER SER C . n 
C 1 261 PHE 261 261 261 PHE PHE C . n 
C 1 262 SER 262 262 262 SER SER C . n 
C 1 263 GLN 263 263 ?   ?   ?   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 ?   ?   ?   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   301 301 ZN  ZN  A . 
F 3 EDO 1   302 302 EDO EDO A . 
G 4 WWX 1   303 303 WWX WWX A . 
H 2 ZN  1   301 301 ZN  ZN  B . 
I 3 EDO 1   302 302 EDO EDO B . 
J 4 WWX 1   303 303 WWX WWX B . 
K 2 ZN  1   301 301 ZN  ZN  C . 
L 3 EDO 1   302 302 EDO EDO C . 
M 4 WWX 1   303 303 WWX WWX C . 
N 2 ZN  1   301 301 ZN  ZN  D . 
O 3 EDO 1   302 302 EDO EDO D . 
P 3 EDO 1   303 303 EDO EDO D . 
Q 3 EDO 1   304 304 EDO EDO D . 
R 4 WWX 1   305 305 WWX WWX D . 
S 5 HOH 1   401 401 HOH HOH A . 
S 5 HOH 2   402 402 HOH HOH A . 
S 5 HOH 3   403 403 HOH HOH A . 
S 5 HOH 4   404 404 HOH HOH A . 
S 5 HOH 5   405 405 HOH HOH A . 
S 5 HOH 6   406 406 HOH HOH A . 
S 5 HOH 7   407 407 HOH HOH A . 
S 5 HOH 8   408 408 HOH HOH A . 
S 5 HOH 9   409 409 HOH HOH A . 
S 5 HOH 10  410 410 HOH HOH A . 
S 5 HOH 11  411 411 HOH HOH A . 
S 5 HOH 12  412 412 HOH HOH A . 
S 5 HOH 13  413 413 HOH HOH A . 
S 5 HOH 14  414 414 HOH HOH A . 
S 5 HOH 15  415 415 HOH HOH A . 
S 5 HOH 16  416 416 HOH HOH A . 
S 5 HOH 17  417 417 HOH HOH A . 
S 5 HOH 18  418 418 HOH HOH A . 
S 5 HOH 19  419 419 HOH HOH A . 
S 5 HOH 20  420 420 HOH HOH A . 
S 5 HOH 21  421 421 HOH HOH A . 
S 5 HOH 22  422 422 HOH HOH A . 
S 5 HOH 23  423 423 HOH HOH A . 
S 5 HOH 24  424 424 HOH HOH A . 
S 5 HOH 25  425 425 HOH HOH A . 
S 5 HOH 26  426 426 HOH HOH A . 
S 5 HOH 27  427 427 HOH HOH A . 
S 5 HOH 28  428 428 HOH HOH A . 
S 5 HOH 29  429 429 HOH HOH A . 
S 5 HOH 30  430 430 HOH HOH A . 
S 5 HOH 31  431 431 HOH HOH A . 
S 5 HOH 32  432 432 HOH HOH A . 
S 5 HOH 33  433 433 HOH HOH A . 
S 5 HOH 34  434 434 HOH HOH A . 
S 5 HOH 35  435 435 HOH HOH A . 
S 5 HOH 36  436 436 HOH HOH A . 
S 5 HOH 37  437 437 HOH HOH A . 
S 5 HOH 38  438 438 HOH HOH A . 
S 5 HOH 39  439 439 HOH HOH A . 
S 5 HOH 40  440 440 HOH HOH A . 
S 5 HOH 41  441 441 HOH HOH A . 
S 5 HOH 42  442 442 HOH HOH A . 
S 5 HOH 43  443 443 HOH HOH A . 
S 5 HOH 44  444 444 HOH HOH A . 
S 5 HOH 45  445 445 HOH HOH A . 
S 5 HOH 46  446 446 HOH HOH A . 
S 5 HOH 47  447 447 HOH HOH A . 
S 5 HOH 48  448 448 HOH HOH A . 
S 5 HOH 49  449 449 HOH HOH A . 
S 5 HOH 50  450 450 HOH HOH A . 
S 5 HOH 51  451 451 HOH HOH A . 
S 5 HOH 52  452 452 HOH HOH A . 
S 5 HOH 53  453 453 HOH HOH A . 
S 5 HOH 54  454 454 HOH HOH A . 
S 5 HOH 55  455 455 HOH HOH A . 
S 5 HOH 56  456 456 HOH HOH A . 
S 5 HOH 57  457 457 HOH HOH A . 
S 5 HOH 58  458 458 HOH HOH A . 
S 5 HOH 59  459 459 HOH HOH A . 
S 5 HOH 60  460 460 HOH HOH A . 
S 5 HOH 61  461 461 HOH HOH A . 
S 5 HOH 62  462 462 HOH HOH A . 
S 5 HOH 63  463 463 HOH HOH A . 
S 5 HOH 64  464 464 HOH HOH A . 
S 5 HOH 65  465 465 HOH HOH A . 
S 5 HOH 66  466 466 HOH HOH A . 
S 5 HOH 67  467 467 HOH HOH A . 
S 5 HOH 68  468 468 HOH HOH A . 
S 5 HOH 69  469 469 HOH HOH A . 
S 5 HOH 70  470 470 HOH HOH A . 
S 5 HOH 71  471 471 HOH HOH A . 
S 5 HOH 72  472 472 HOH HOH A . 
S 5 HOH 73  473 473 HOH HOH A . 
S 5 HOH 74  474 474 HOH HOH A . 
S 5 HOH 75  475 475 HOH HOH A . 
S 5 HOH 76  476 476 HOH HOH A . 
S 5 HOH 77  477 477 HOH HOH A . 
S 5 HOH 78  478 478 HOH HOH A . 
S 5 HOH 79  479 479 HOH HOH A . 
S 5 HOH 80  480 480 HOH HOH A . 
S 5 HOH 81  481 481 HOH HOH A . 
S 5 HOH 82  482 482 HOH HOH A . 
S 5 HOH 83  483 483 HOH HOH A . 
S 5 HOH 84  484 484 HOH HOH A . 
S 5 HOH 85  485 485 HOH HOH A . 
S 5 HOH 86  486 486 HOH HOH A . 
S 5 HOH 87  487 487 HOH HOH A . 
S 5 HOH 88  488 488 HOH HOH A . 
S 5 HOH 89  489 489 HOH HOH A . 
S 5 HOH 90  490 490 HOH HOH A . 
S 5 HOH 91  491 491 HOH HOH A . 
S 5 HOH 92  492 492 HOH HOH A . 
S 5 HOH 93  493 493 HOH HOH A . 
S 5 HOH 94  494 494 HOH HOH A . 
S 5 HOH 95  495 495 HOH HOH A . 
S 5 HOH 96  496 496 HOH HOH A . 
S 5 HOH 97  497 497 HOH HOH A . 
S 5 HOH 98  498 498 HOH HOH A . 
S 5 HOH 99  499 499 HOH HOH A . 
S 5 HOH 100 500 500 HOH HOH A . 
S 5 HOH 101 501 501 HOH HOH A . 
S 5 HOH 102 502 502 HOH HOH A . 
S 5 HOH 103 503 503 HOH HOH A . 
S 5 HOH 104 504 504 HOH HOH A . 
S 5 HOH 105 505 505 HOH HOH A . 
S 5 HOH 106 506 506 HOH HOH A . 
S 5 HOH 107 507 507 HOH HOH A . 
S 5 HOH 108 508 508 HOH HOH A . 
S 5 HOH 109 509 509 HOH HOH A . 
S 5 HOH 110 510 510 HOH HOH A . 
S 5 HOH 111 511 511 HOH HOH A . 
S 5 HOH 112 512 512 HOH HOH A . 
S 5 HOH 113 513 513 HOH HOH A . 
S 5 HOH 114 514 514 HOH HOH A . 
S 5 HOH 115 515 515 HOH HOH A . 
S 5 HOH 116 516 516 HOH HOH A . 
S 5 HOH 117 517 517 HOH HOH A . 
S 5 HOH 118 518 518 HOH HOH A . 
S 5 HOH 119 519 519 HOH HOH A . 
S 5 HOH 120 520 520 HOH HOH A . 
S 5 HOH 121 521 521 HOH HOH A . 
S 5 HOH 122 522 522 HOH HOH A . 
S 5 HOH 123 523 523 HOH HOH A . 
S 5 HOH 124 524 524 HOH HOH A . 
S 5 HOH 125 525 525 HOH HOH A . 
S 5 HOH 126 526 526 HOH HOH A . 
S 5 HOH 127 527 527 HOH HOH A . 
S 5 HOH 128 528 528 HOH HOH A . 
S 5 HOH 129 529 529 HOH HOH A . 
S 5 HOH 130 530 530 HOH HOH A . 
S 5 HOH 131 531 531 HOH HOH A . 
S 5 HOH 132 532 532 HOH HOH A . 
S 5 HOH 133 533 533 HOH HOH A . 
S 5 HOH 134 534 534 HOH HOH A . 
S 5 HOH 135 535 535 HOH HOH A . 
S 5 HOH 136 536 536 HOH HOH A . 
S 5 HOH 137 537 537 HOH HOH A . 
S 5 HOH 138 538 538 HOH HOH A . 
S 5 HOH 139 539 539 HOH HOH A . 
S 5 HOH 140 540 540 HOH HOH A . 
S 5 HOH 141 541 541 HOH HOH A . 
S 5 HOH 142 542 542 HOH HOH A . 
S 5 HOH 143 543 543 HOH HOH A . 
S 5 HOH 144 544 544 HOH HOH A . 
S 5 HOH 145 545 545 HOH HOH A . 
S 5 HOH 146 546 546 HOH HOH A . 
S 5 HOH 147 547 547 HOH HOH A . 
S 5 HOH 148 548 548 HOH HOH A . 
S 5 HOH 149 549 549 HOH HOH A . 
S 5 HOH 150 550 550 HOH HOH A . 
S 5 HOH 151 551 551 HOH HOH A . 
S 5 HOH 152 552 552 HOH HOH A . 
S 5 HOH 153 553 553 HOH HOH A . 
S 5 HOH 154 554 554 HOH HOH A . 
S 5 HOH 155 555 555 HOH HOH A . 
S 5 HOH 156 556 556 HOH HOH A . 
S 5 HOH 157 557 557 HOH HOH A . 
S 5 HOH 158 558 558 HOH HOH A . 
S 5 HOH 159 559 559 HOH HOH A . 
S 5 HOH 160 560 560 HOH HOH A . 
S 5 HOH 161 561 561 HOH HOH A . 
S 5 HOH 162 562 562 HOH HOH A . 
S 5 HOH 163 563 563 HOH HOH A . 
S 5 HOH 164 564 564 HOH HOH A . 
S 5 HOH 165 565 565 HOH HOH A . 
S 5 HOH 166 566 566 HOH HOH A . 
S 5 HOH 167 567 567 HOH HOH A . 
S 5 HOH 168 568 568 HOH HOH A . 
S 5 HOH 169 569 569 HOH HOH A . 
S 5 HOH 170 570 570 HOH HOH A . 
S 5 HOH 171 571 571 HOH HOH A . 
S 5 HOH 172 572 572 HOH HOH A . 
S 5 HOH 173 573 573 HOH HOH A . 
S 5 HOH 174 574 574 HOH HOH A . 
S 5 HOH 175 575 575 HOH HOH A . 
S 5 HOH 176 576 576 HOH HOH A . 
S 5 HOH 177 577 577 HOH HOH A . 
S 5 HOH 178 578 578 HOH HOH A . 
S 5 HOH 179 579 579 HOH HOH A . 
S 5 HOH 180 580 580 HOH HOH A . 
S 5 HOH 181 581 581 HOH HOH A . 
S 5 HOH 182 582 582 HOH HOH A . 
S 5 HOH 183 583 583 HOH HOH A . 
S 5 HOH 184 584 584 HOH HOH A . 
S 5 HOH 185 585 585 HOH HOH A . 
S 5 HOH 186 586 586 HOH HOH A . 
S 5 HOH 187 587 587 HOH HOH A . 
S 5 HOH 188 588 588 HOH HOH A . 
S 5 HOH 189 589 589 HOH HOH A . 
S 5 HOH 190 590 590 HOH HOH A . 
S 5 HOH 191 591 591 HOH HOH A . 
S 5 HOH 192 592 592 HOH HOH A . 
S 5 HOH 193 593 593 HOH HOH A . 
S 5 HOH 194 594 594 HOH HOH A . 
S 5 HOH 195 595 595 HOH HOH A . 
S 5 HOH 196 596 596 HOH HOH A . 
S 5 HOH 197 597 597 HOH HOH A . 
S 5 HOH 198 598 598 HOH HOH A . 
S 5 HOH 199 599 599 HOH HOH A . 
S 5 HOH 200 600 600 HOH HOH A . 
S 5 HOH 201 601 601 HOH HOH A . 
S 5 HOH 202 602 602 HOH HOH A . 
S 5 HOH 203 603 603 HOH HOH A . 
S 5 HOH 204 604 604 HOH HOH A . 
S 5 HOH 205 605 605 HOH HOH A . 
S 5 HOH 206 606 606 HOH HOH A . 
S 5 HOH 207 607 607 HOH HOH A . 
S 5 HOH 208 608 608 HOH HOH A . 
S 5 HOH 209 609 609 HOH HOH A . 
S 5 HOH 210 610 610 HOH HOH A . 
S 5 HOH 211 611 611 HOH HOH A . 
S 5 HOH 212 612 612 HOH HOH A . 
S 5 HOH 213 613 613 HOH HOH A . 
S 5 HOH 214 614 614 HOH HOH A . 
S 5 HOH 215 615 615 HOH HOH A . 
S 5 HOH 216 616 616 HOH HOH A . 
S 5 HOH 217 617 617 HOH HOH A . 
S 5 HOH 218 618 618 HOH HOH A . 
S 5 HOH 219 619 619 HOH HOH A . 
S 5 HOH 220 620 620 HOH HOH A . 
S 5 HOH 221 621 621 HOH HOH A . 
S 5 HOH 222 622 622 HOH HOH A . 
S 5 HOH 223 623 623 HOH HOH A . 
S 5 HOH 224 624 624 HOH HOH A . 
S 5 HOH 225 625 625 HOH HOH A . 
S 5 HOH 226 626 626 HOH HOH A . 
S 5 HOH 227 627 627 HOH HOH A . 
S 5 HOH 228 628 628 HOH HOH A . 
S 5 HOH 229 629 629 HOH HOH A . 
S 5 HOH 230 630 630 HOH HOH A . 
S 5 HOH 231 631 631 HOH HOH A . 
S 5 HOH 232 632 632 HOH HOH A . 
S 5 HOH 233 633 633 HOH HOH A . 
S 5 HOH 234 634 634 HOH HOH A . 
S 5 HOH 235 635 635 HOH HOH A . 
S 5 HOH 236 636 636 HOH HOH A . 
S 5 HOH 237 637 637 HOH HOH A . 
S 5 HOH 238 638 638 HOH HOH A . 
S 5 HOH 239 639 639 HOH HOH A . 
S 5 HOH 240 640 640 HOH HOH A . 
S 5 HOH 241 641 641 HOH HOH A . 
S 5 HOH 242 642 642 HOH HOH A . 
S 5 HOH 243 643 643 HOH HOH A . 
T 5 HOH 1   401 401 HOH HOH B . 
T 5 HOH 2   402 402 HOH HOH B . 
T 5 HOH 3   403 403 HOH HOH B . 
T 5 HOH 4   404 404 HOH HOH B . 
T 5 HOH 5   405 405 HOH HOH B . 
T 5 HOH 6   406 406 HOH HOH B . 
T 5 HOH 7   407 407 HOH HOH B . 
T 5 HOH 8   408 408 HOH HOH B . 
T 5 HOH 9   409 409 HOH HOH B . 
T 5 HOH 10  410 410 HOH HOH B . 
T 5 HOH 11  411 411 HOH HOH B . 
T 5 HOH 12  412 412 HOH HOH B . 
T 5 HOH 13  413 413 HOH HOH B . 
T 5 HOH 14  414 414 HOH HOH B . 
T 5 HOH 15  415 415 HOH HOH B . 
T 5 HOH 16  416 416 HOH HOH B . 
T 5 HOH 17  417 417 HOH HOH B . 
T 5 HOH 18  418 418 HOH HOH B . 
T 5 HOH 19  419 419 HOH HOH B . 
T 5 HOH 20  420 420 HOH HOH B . 
T 5 HOH 21  421 421 HOH HOH B . 
T 5 HOH 22  422 422 HOH HOH B . 
T 5 HOH 23  423 423 HOH HOH B . 
T 5 HOH 24  424 424 HOH HOH B . 
T 5 HOH 25  425 425 HOH HOH B . 
T 5 HOH 26  426 426 HOH HOH B . 
T 5 HOH 27  427 427 HOH HOH B . 
T 5 HOH 28  428 428 HOH HOH B . 
T 5 HOH 29  429 429 HOH HOH B . 
T 5 HOH 30  430 430 HOH HOH B . 
T 5 HOH 31  431 431 HOH HOH B . 
T 5 HOH 32  432 432 HOH HOH B . 
T 5 HOH 33  433 433 HOH HOH B . 
T 5 HOH 34  434 434 HOH HOH B . 
T 5 HOH 35  435 435 HOH HOH B . 
T 5 HOH 36  436 436 HOH HOH B . 
T 5 HOH 37  437 437 HOH HOH B . 
T 5 HOH 38  438 438 HOH HOH B . 
T 5 HOH 39  439 439 HOH HOH B . 
T 5 HOH 40  440 440 HOH HOH B . 
T 5 HOH 41  441 441 HOH HOH B . 
T 5 HOH 42  442 442 HOH HOH B . 
T 5 HOH 43  443 443 HOH HOH B . 
T 5 HOH 44  444 444 HOH HOH B . 
T 5 HOH 45  445 445 HOH HOH B . 
T 5 HOH 46  446 446 HOH HOH B . 
T 5 HOH 47  447 447 HOH HOH B . 
T 5 HOH 48  448 448 HOH HOH B . 
T 5 HOH 49  449 449 HOH HOH B . 
T 5 HOH 50  450 450 HOH HOH B . 
T 5 HOH 51  451 451 HOH HOH B . 
T 5 HOH 52  452 452 HOH HOH B . 
T 5 HOH 53  453 453 HOH HOH B . 
T 5 HOH 54  454 454 HOH HOH B . 
T 5 HOH 55  455 455 HOH HOH B . 
T 5 HOH 56  456 456 HOH HOH B . 
T 5 HOH 57  457 457 HOH HOH B . 
T 5 HOH 58  458 458 HOH HOH B . 
T 5 HOH 59  459 459 HOH HOH B . 
T 5 HOH 60  460 460 HOH HOH B . 
T 5 HOH 61  461 461 HOH HOH B . 
T 5 HOH 62  462 462 HOH HOH B . 
T 5 HOH 63  463 463 HOH HOH B . 
T 5 HOH 64  464 464 HOH HOH B . 
T 5 HOH 65  465 465 HOH HOH B . 
T 5 HOH 66  466 466 HOH HOH B . 
T 5 HOH 67  467 467 HOH HOH B . 
T 5 HOH 68  468 468 HOH HOH B . 
T 5 HOH 69  469 469 HOH HOH B . 
T 5 HOH 70  470 470 HOH HOH B . 
T 5 HOH 71  471 471 HOH HOH B . 
T 5 HOH 72  472 472 HOH HOH B . 
T 5 HOH 73  473 473 HOH HOH B . 
T 5 HOH 74  474 474 HOH HOH B . 
T 5 HOH 75  475 475 HOH HOH B . 
T 5 HOH 76  476 476 HOH HOH B . 
T 5 HOH 77  477 477 HOH HOH B . 
T 5 HOH 78  478 478 HOH HOH B . 
T 5 HOH 79  479 479 HOH HOH B . 
T 5 HOH 80  480 480 HOH HOH B . 
T 5 HOH 81  481 481 HOH HOH B . 
T 5 HOH 82  482 482 HOH HOH B . 
T 5 HOH 83  483 483 HOH HOH B . 
T 5 HOH 84  484 484 HOH HOH B . 
T 5 HOH 85  485 485 HOH HOH B . 
T 5 HOH 86  486 486 HOH HOH B . 
T 5 HOH 87  487 487 HOH HOH B . 
T 5 HOH 88  488 488 HOH HOH B . 
T 5 HOH 89  489 489 HOH HOH B . 
T 5 HOH 90  490 490 HOH HOH B . 
T 5 HOH 91  491 491 HOH HOH B . 
T 5 HOH 92  492 492 HOH HOH B . 
T 5 HOH 93  493 493 HOH HOH B . 
T 5 HOH 94  494 494 HOH HOH B . 
T 5 HOH 95  495 495 HOH HOH B . 
T 5 HOH 96  496 496 HOH HOH B . 
T 5 HOH 97  497 497 HOH HOH B . 
T 5 HOH 98  498 498 HOH HOH B . 
T 5 HOH 99  499 499 HOH HOH B . 
T 5 HOH 100 500 500 HOH HOH B . 
T 5 HOH 101 501 501 HOH HOH B . 
T 5 HOH 102 502 502 HOH HOH B . 
T 5 HOH 103 503 503 HOH HOH B . 
T 5 HOH 104 504 504 HOH HOH B . 
T 5 HOH 105 505 505 HOH HOH B . 
T 5 HOH 106 506 506 HOH HOH B . 
T 5 HOH 107 507 507 HOH HOH B . 
T 5 HOH 108 508 508 HOH HOH B . 
T 5 HOH 109 509 509 HOH HOH B . 
T 5 HOH 110 510 510 HOH HOH B . 
T 5 HOH 111 511 511 HOH HOH B . 
T 5 HOH 112 512 512 HOH HOH B . 
T 5 HOH 113 513 513 HOH HOH B . 
T 5 HOH 114 514 514 HOH HOH B . 
T 5 HOH 115 515 515 HOH HOH B . 
T 5 HOH 116 516 516 HOH HOH B . 
T 5 HOH 117 517 517 HOH HOH B . 
T 5 HOH 118 518 518 HOH HOH B . 
T 5 HOH 119 519 519 HOH HOH B . 
T 5 HOH 120 520 520 HOH HOH B . 
T 5 HOH 121 521 521 HOH HOH B . 
T 5 HOH 122 522 522 HOH HOH B . 
T 5 HOH 123 523 523 HOH HOH B . 
T 5 HOH 124 524 524 HOH HOH B . 
T 5 HOH 125 525 525 HOH HOH B . 
T 5 HOH 126 526 526 HOH HOH B . 
T 5 HOH 127 527 527 HOH HOH B . 
T 5 HOH 128 528 528 HOH HOH B . 
T 5 HOH 129 529 529 HOH HOH B . 
T 5 HOH 130 530 530 HOH HOH B . 
T 5 HOH 131 531 531 HOH HOH B . 
T 5 HOH 132 532 532 HOH HOH B . 
T 5 HOH 133 533 533 HOH HOH B . 
T 5 HOH 134 534 534 HOH HOH B . 
T 5 HOH 135 535 535 HOH HOH B . 
T 5 HOH 136 536 536 HOH HOH B . 
T 5 HOH 137 537 537 HOH HOH B . 
T 5 HOH 138 538 538 HOH HOH B . 
T 5 HOH 139 539 539 HOH HOH B . 
T 5 HOH 140 540 540 HOH HOH B . 
T 5 HOH 141 541 541 HOH HOH B . 
T 5 HOH 142 542 542 HOH HOH B . 
T 5 HOH 143 543 543 HOH HOH B . 
T 5 HOH 144 544 544 HOH HOH B . 
T 5 HOH 145 545 545 HOH HOH B . 
T 5 HOH 146 546 546 HOH HOH B . 
T 5 HOH 147 547 547 HOH HOH B . 
T 5 HOH 148 548 548 HOH HOH B . 
T 5 HOH 149 549 549 HOH HOH B . 
T 5 HOH 150 550 550 HOH HOH B . 
T 5 HOH 151 551 551 HOH HOH B . 
T 5 HOH 152 552 552 HOH HOH B . 
T 5 HOH 153 553 553 HOH HOH B . 
T 5 HOH 154 554 554 HOH HOH B . 
T 5 HOH 155 555 555 HOH HOH B . 
T 5 HOH 156 556 556 HOH HOH B . 
T 5 HOH 157 557 557 HOH HOH B . 
T 5 HOH 158 558 558 HOH HOH B . 
T 5 HOH 159 559 559 HOH HOH B . 
T 5 HOH 160 560 560 HOH HOH B . 
T 5 HOH 161 561 561 HOH HOH B . 
T 5 HOH 162 562 562 HOH HOH B . 
T 5 HOH 163 563 563 HOH HOH B . 
T 5 HOH 164 564 564 HOH HOH B . 
T 5 HOH 165 565 565 HOH HOH B . 
T 5 HOH 166 566 566 HOH HOH B . 
T 5 HOH 167 567 567 HOH HOH B . 
T 5 HOH 168 568 568 HOH HOH B . 
T 5 HOH 169 569 569 HOH HOH B . 
T 5 HOH 170 570 570 HOH HOH B . 
T 5 HOH 171 571 571 HOH HOH B . 
T 5 HOH 172 572 572 HOH HOH B . 
T 5 HOH 173 573 573 HOH HOH B . 
T 5 HOH 174 574 574 HOH HOH B . 
T 5 HOH 175 575 575 HOH HOH B . 
T 5 HOH 176 576 576 HOH HOH B . 
T 5 HOH 177 577 577 HOH HOH B . 
T 5 HOH 178 578 578 HOH HOH B . 
T 5 HOH 179 579 579 HOH HOH B . 
T 5 HOH 180 580 580 HOH HOH B . 
T 5 HOH 181 581 581 HOH HOH B . 
T 5 HOH 182 582 582 HOH HOH B . 
T 5 HOH 183 583 583 HOH HOH B . 
T 5 HOH 184 584 584 HOH HOH B . 
T 5 HOH 185 585 585 HOH HOH B . 
T 5 HOH 186 586 586 HOH HOH B . 
T 5 HOH 187 587 587 HOH HOH B . 
T 5 HOH 188 588 588 HOH HOH B . 
T 5 HOH 189 589 589 HOH HOH B . 
T 5 HOH 190 590 590 HOH HOH B . 
T 5 HOH 191 591 591 HOH HOH B . 
T 5 HOH 192 592 592 HOH HOH B . 
T 5 HOH 193 593 593 HOH HOH B . 
T 5 HOH 194 594 594 HOH HOH B . 
T 5 HOH 195 595 595 HOH HOH B . 
T 5 HOH 196 596 596 HOH HOH B . 
T 5 HOH 197 597 597 HOH HOH B . 
T 5 HOH 198 598 598 HOH HOH B . 
T 5 HOH 199 599 599 HOH HOH B . 
T 5 HOH 200 600 600 HOH HOH B . 
T 5 HOH 201 601 601 HOH HOH B . 
T 5 HOH 202 602 602 HOH HOH B . 
T 5 HOH 203 603 603 HOH HOH B . 
T 5 HOH 204 604 604 HOH HOH B . 
T 5 HOH 205 605 605 HOH HOH B . 
T 5 HOH 206 606 606 HOH HOH B . 
T 5 HOH 207 607 607 HOH HOH B . 
T 5 HOH 208 608 608 HOH HOH B . 
T 5 HOH 209 609 609 HOH HOH B . 
T 5 HOH 210 610 610 HOH HOH B . 
T 5 HOH 211 611 611 HOH HOH B . 
T 5 HOH 212 612 612 HOH HOH B . 
T 5 HOH 213 613 613 HOH HOH B . 
T 5 HOH 214 614 614 HOH HOH B . 
T 5 HOH 215 615 615 HOH HOH B . 
T 5 HOH 216 616 616 HOH HOH B . 
T 5 HOH 217 617 617 HOH HOH B . 
T 5 HOH 218 618 618 HOH HOH B . 
T 5 HOH 219 619 619 HOH HOH B . 
T 5 HOH 220 620 620 HOH HOH B . 
T 5 HOH 221 621 621 HOH HOH B . 
T 5 HOH 222 622 622 HOH HOH B . 
T 5 HOH 223 623 623 HOH HOH B . 
T 5 HOH 224 624 624 HOH HOH B . 
T 5 HOH 225 625 625 HOH HOH B . 
T 5 HOH 226 626 626 HOH HOH B . 
T 5 HOH 227 627 627 HOH HOH B . 
T 5 HOH 228 628 628 HOH HOH B . 
T 5 HOH 229 629 629 HOH HOH B . 
T 5 HOH 230 630 630 HOH HOH B . 
T 5 HOH 231 631 631 HOH HOH B . 
T 5 HOH 232 632 632 HOH HOH B . 
T 5 HOH 233 633 633 HOH HOH B . 
T 5 HOH 234 634 634 HOH HOH B . 
T 5 HOH 235 635 635 HOH HOH B . 
T 5 HOH 236 636 636 HOH HOH B . 
T 5 HOH 237 637 637 HOH HOH B . 
T 5 HOH 238 638 638 HOH HOH B . 
T 5 HOH 239 639 639 HOH HOH B . 
T 5 HOH 240 640 640 HOH HOH B . 
T 5 HOH 241 641 641 HOH HOH B . 
T 5 HOH 242 642 642 HOH HOH B . 
T 5 HOH 243 643 643 HOH HOH B . 
T 5 HOH 244 644 644 HOH HOH B . 
T 5 HOH 245 645 645 HOH HOH B . 
T 5 HOH 246 646 646 HOH HOH B . 
T 5 HOH 247 647 647 HOH HOH B . 
T 5 HOH 248 648 648 HOH HOH B . 
T 5 HOH 249 649 649 HOH HOH B . 
T 5 HOH 250 650 650 HOH HOH B . 
T 5 HOH 251 651 651 HOH HOH B . 
T 5 HOH 252 652 652 HOH HOH B . 
T 5 HOH 253 653 653 HOH HOH B . 
T 5 HOH 254 654 654 HOH HOH B . 
T 5 HOH 255 655 655 HOH HOH B . 
T 5 HOH 256 656 656 HOH HOH B . 
T 5 HOH 257 657 657 HOH HOH B . 
T 5 HOH 258 658 658 HOH HOH B . 
T 5 HOH 259 659 659 HOH HOH B . 
T 5 HOH 260 660 660 HOH HOH B . 
T 5 HOH 261 661 661 HOH HOH B . 
T 5 HOH 262 662 662 HOH HOH B . 
T 5 HOH 263 663 663 HOH HOH B . 
T 5 HOH 264 664 664 HOH HOH B . 
T 5 HOH 265 665 665 HOH HOH B . 
T 5 HOH 266 666 666 HOH HOH B . 
T 5 HOH 267 667 667 HOH HOH B . 
T 5 HOH 268 668 668 HOH HOH B . 
T 5 HOH 269 669 669 HOH HOH B . 
T 5 HOH 270 670 670 HOH HOH B . 
T 5 HOH 271 671 671 HOH HOH B . 
T 5 HOH 272 672 672 HOH HOH B . 
T 5 HOH 273 673 673 HOH HOH B . 
T 5 HOH 274 674 674 HOH HOH B . 
T 5 HOH 275 675 675 HOH HOH B . 
T 5 HOH 276 676 676 HOH HOH B . 
T 5 HOH 277 677 677 HOH HOH B . 
T 5 HOH 278 678 678 HOH HOH B . 
T 5 HOH 279 679 679 HOH HOH B . 
T 5 HOH 280 680 680 HOH HOH B . 
T 5 HOH 281 681 681 HOH HOH B . 
T 5 HOH 282 682 682 HOH HOH B . 
T 5 HOH 283 683 683 HOH HOH B . 
T 5 HOH 284 684 684 HOH HOH B . 
T 5 HOH 285 685 685 HOH HOH B . 
T 5 HOH 286 686 686 HOH HOH B . 
T 5 HOH 287 687 687 HOH HOH B . 
T 5 HOH 288 688 688 HOH HOH B . 
T 5 HOH 289 689 689 HOH HOH B . 
T 5 HOH 290 690 690 HOH HOH B . 
U 5 HOH 1   401 401 HOH HOH C . 
U 5 HOH 2   402 402 HOH HOH C . 
U 5 HOH 3   403 403 HOH HOH C . 
U 5 HOH 4   404 404 HOH HOH C . 
U 5 HOH 5   405 405 HOH HOH C . 
U 5 HOH 6   406 406 HOH HOH C . 
U 5 HOH 7   407 407 HOH HOH C . 
U 5 HOH 8   408 408 HOH HOH C . 
U 5 HOH 9   409 409 HOH HOH C . 
U 5 HOH 10  410 410 HOH HOH C . 
U 5 HOH 11  411 411 HOH HOH C . 
U 5 HOH 12  412 412 HOH HOH C . 
U 5 HOH 13  413 413 HOH HOH C . 
U 5 HOH 14  414 414 HOH HOH C . 
U 5 HOH 15  415 415 HOH HOH C . 
U 5 HOH 16  416 416 HOH HOH C . 
U 5 HOH 17  417 417 HOH HOH C . 
U 5 HOH 18  418 418 HOH HOH C . 
U 5 HOH 19  419 419 HOH HOH C . 
U 5 HOH 20  420 420 HOH HOH C . 
U 5 HOH 21  421 421 HOH HOH C . 
U 5 HOH 22  422 422 HOH HOH C . 
U 5 HOH 23  423 423 HOH HOH C . 
U 5 HOH 24  424 424 HOH HOH C . 
U 5 HOH 25  425 425 HOH HOH C . 
U 5 HOH 26  426 426 HOH HOH C . 
U 5 HOH 27  427 427 HOH HOH C . 
U 5 HOH 28  428 428 HOH HOH C . 
U 5 HOH 29  429 429 HOH HOH C . 
U 5 HOH 30  430 430 HOH HOH C . 
U 5 HOH 31  431 431 HOH HOH C . 
U 5 HOH 32  432 432 HOH HOH C . 
U 5 HOH 33  433 433 HOH HOH C . 
U 5 HOH 34  434 434 HOH HOH C . 
U 5 HOH 35  435 435 HOH HOH C . 
U 5 HOH 36  436 436 HOH HOH C . 
U 5 HOH 37  437 437 HOH HOH C . 
U 5 HOH 38  438 438 HOH HOH C . 
U 5 HOH 39  439 439 HOH HOH C . 
U 5 HOH 40  440 440 HOH HOH C . 
U 5 HOH 41  441 441 HOH HOH C . 
U 5 HOH 42  442 442 HOH HOH C . 
U 5 HOH 43  443 443 HOH HOH C . 
U 5 HOH 44  444 444 HOH HOH C . 
U 5 HOH 45  445 445 HOH HOH C . 
U 5 HOH 46  446 446 HOH HOH C . 
U 5 HOH 47  447 447 HOH HOH C . 
U 5 HOH 48  448 448 HOH HOH C . 
U 5 HOH 49  449 449 HOH HOH C . 
U 5 HOH 50  450 450 HOH HOH C . 
U 5 HOH 51  451 451 HOH HOH C . 
U 5 HOH 52  452 452 HOH HOH C . 
U 5 HOH 53  453 453 HOH HOH C . 
U 5 HOH 54  454 454 HOH HOH C . 
U 5 HOH 55  455 455 HOH HOH C . 
U 5 HOH 56  456 456 HOH HOH C . 
U 5 HOH 57  457 457 HOH HOH C . 
U 5 HOH 58  458 458 HOH HOH C . 
U 5 HOH 59  459 459 HOH HOH C . 
U 5 HOH 60  460 460 HOH HOH C . 
U 5 HOH 61  461 461 HOH HOH C . 
U 5 HOH 62  462 462 HOH HOH C . 
U 5 HOH 63  463 463 HOH HOH C . 
U 5 HOH 64  464 464 HOH HOH C . 
U 5 HOH 65  465 465 HOH HOH C . 
U 5 HOH 66  466 466 HOH HOH C . 
U 5 HOH 67  467 467 HOH HOH C . 
U 5 HOH 68  468 468 HOH HOH C . 
U 5 HOH 69  469 469 HOH HOH C . 
U 5 HOH 70  470 470 HOH HOH C . 
U 5 HOH 71  471 471 HOH HOH C . 
U 5 HOH 72  472 472 HOH HOH C . 
U 5 HOH 73  473 473 HOH HOH C . 
U 5 HOH 74  474 474 HOH HOH C . 
U 5 HOH 75  475 475 HOH HOH C . 
U 5 HOH 76  476 476 HOH HOH C . 
U 5 HOH 77  477 477 HOH HOH C . 
U 5 HOH 78  478 478 HOH HOH C . 
U 5 HOH 79  479 479 HOH HOH C . 
U 5 HOH 80  480 480 HOH HOH C . 
U 5 HOH 81  481 481 HOH HOH C . 
U 5 HOH 82  482 482 HOH HOH C . 
U 5 HOH 83  483 483 HOH HOH C . 
U 5 HOH 84  484 484 HOH HOH C . 
U 5 HOH 85  485 485 HOH HOH C . 
U 5 HOH 86  486 486 HOH HOH C . 
U 5 HOH 87  487 487 HOH HOH C . 
U 5 HOH 88  488 488 HOH HOH C . 
U 5 HOH 89  489 489 HOH HOH C . 
U 5 HOH 90  490 490 HOH HOH C . 
U 5 HOH 91  491 491 HOH HOH C . 
U 5 HOH 92  492 492 HOH HOH C . 
U 5 HOH 93  493 493 HOH HOH C . 
U 5 HOH 94  494 494 HOH HOH C . 
U 5 HOH 95  495 495 HOH HOH C . 
U 5 HOH 96  496 496 HOH HOH C . 
U 5 HOH 97  497 497 HOH HOH C . 
U 5 HOH 98  498 498 HOH HOH C . 
U 5 HOH 99  499 499 HOH HOH C . 
U 5 HOH 100 500 500 HOH HOH C . 
U 5 HOH 101 501 501 HOH HOH C . 
U 5 HOH 102 502 502 HOH HOH C . 
U 5 HOH 103 503 503 HOH HOH C . 
U 5 HOH 104 504 504 HOH HOH C . 
U 5 HOH 105 505 505 HOH HOH C . 
U 5 HOH 106 506 506 HOH HOH C . 
U 5 HOH 107 507 507 HOH HOH C . 
U 5 HOH 108 508 508 HOH HOH C . 
U 5 HOH 109 509 509 HOH HOH C . 
U 5 HOH 110 510 510 HOH HOH C . 
U 5 HOH 111 511 511 HOH HOH C . 
U 5 HOH 112 512 512 HOH HOH C . 
U 5 HOH 113 513 513 HOH HOH C . 
U 5 HOH 114 514 514 HOH HOH C . 
U 5 HOH 115 515 515 HOH HOH C . 
U 5 HOH 116 516 516 HOH HOH C . 
U 5 HOH 117 517 517 HOH HOH C . 
U 5 HOH 118 518 518 HOH HOH C . 
U 5 HOH 119 519 519 HOH HOH C . 
U 5 HOH 120 520 520 HOH HOH C . 
U 5 HOH 121 521 521 HOH HOH C . 
U 5 HOH 122 522 522 HOH HOH C . 
U 5 HOH 123 523 523 HOH HOH C . 
U 5 HOH 124 524 524 HOH HOH C . 
U 5 HOH 125 525 525 HOH HOH C . 
U 5 HOH 126 526 526 HOH HOH C . 
U 5 HOH 127 527 527 HOH HOH C . 
U 5 HOH 128 528 528 HOH HOH C . 
U 5 HOH 129 529 529 HOH HOH C . 
U 5 HOH 130 530 530 HOH HOH C . 
U 5 HOH 131 531 531 HOH HOH C . 
U 5 HOH 132 532 532 HOH HOH C . 
U 5 HOH 133 533 533 HOH HOH C . 
U 5 HOH 134 534 534 HOH HOH C . 
U 5 HOH 135 535 535 HOH HOH C . 
U 5 HOH 136 536 536 HOH HOH C . 
U 5 HOH 137 537 537 HOH HOH C . 
U 5 HOH 138 538 538 HOH HOH C . 
U 5 HOH 139 539 539 HOH HOH C . 
U 5 HOH 140 540 540 HOH HOH C . 
U 5 HOH 141 541 541 HOH HOH C . 
U 5 HOH 142 542 542 HOH HOH C . 
U 5 HOH 143 543 543 HOH HOH C . 
U 5 HOH 144 544 544 HOH HOH C . 
U 5 HOH 145 545 545 HOH HOH C . 
U 5 HOH 146 546 546 HOH HOH C . 
U 5 HOH 147 547 547 HOH HOH C . 
U 5 HOH 148 548 548 HOH HOH C . 
U 5 HOH 149 549 549 HOH HOH C . 
U 5 HOH 150 550 550 HOH HOH C . 
U 5 HOH 151 551 551 HOH HOH C . 
U 5 HOH 152 552 552 HOH HOH C . 
U 5 HOH 153 553 553 HOH HOH C . 
U 5 HOH 154 554 554 HOH HOH C . 
U 5 HOH 155 555 555 HOH HOH C . 
U 5 HOH 156 556 556 HOH HOH C . 
U 5 HOH 157 557 557 HOH HOH C . 
U 5 HOH 158 558 558 HOH HOH C . 
U 5 HOH 159 559 559 HOH HOH C . 
U 5 HOH 160 560 560 HOH HOH C . 
U 5 HOH 161 561 561 HOH HOH C . 
U 5 HOH 162 562 562 HOH HOH C . 
U 5 HOH 163 563 563 HOH HOH C . 
U 5 HOH 164 564 564 HOH HOH C . 
U 5 HOH 165 565 565 HOH HOH C . 
U 5 HOH 166 566 566 HOH HOH C . 
U 5 HOH 167 567 567 HOH HOH C . 
U 5 HOH 168 568 568 HOH HOH C . 
U 5 HOH 169 569 569 HOH HOH C . 
U 5 HOH 170 570 570 HOH HOH C . 
U 5 HOH 171 571 571 HOH HOH C . 
U 5 HOH 172 572 572 HOH HOH C . 
U 5 HOH 173 573 573 HOH HOH C . 
U 5 HOH 174 574 574 HOH HOH C . 
U 5 HOH 175 575 575 HOH HOH C . 
U 5 HOH 176 576 576 HOH HOH C . 
U 5 HOH 177 577 577 HOH HOH C . 
U 5 HOH 178 578 578 HOH HOH C . 
U 5 HOH 179 579 579 HOH HOH C . 
U 5 HOH 180 580 580 HOH HOH C . 
U 5 HOH 181 581 581 HOH HOH C . 
U 5 HOH 182 582 582 HOH HOH C . 
U 5 HOH 183 583 583 HOH HOH C . 
U 5 HOH 184 584 584 HOH HOH C . 
U 5 HOH 185 585 585 HOH HOH C . 
U 5 HOH 186 586 586 HOH HOH C . 
U 5 HOH 187 587 587 HOH HOH C . 
U 5 HOH 188 588 588 HOH HOH C . 
U 5 HOH 189 589 589 HOH HOH C . 
U 5 HOH 190 590 590 HOH HOH C . 
U 5 HOH 191 591 591 HOH HOH C . 
U 5 HOH 192 592 592 HOH HOH C . 
U 5 HOH 193 593 593 HOH HOH C . 
U 5 HOH 194 594 594 HOH HOH C . 
U 5 HOH 195 595 595 HOH HOH C . 
U 5 HOH 196 596 596 HOH HOH C . 
U 5 HOH 197 597 597 HOH HOH C . 
U 5 HOH 198 598 598 HOH HOH C . 
U 5 HOH 199 599 599 HOH HOH C . 
U 5 HOH 200 600 600 HOH HOH C . 
U 5 HOH 201 601 601 HOH HOH C . 
U 5 HOH 202 602 602 HOH HOH C . 
U 5 HOH 203 603 603 HOH HOH C . 
U 5 HOH 204 604 604 HOH HOH C . 
U 5 HOH 205 605 605 HOH HOH C . 
U 5 HOH 206 606 606 HOH HOH C . 
U 5 HOH 207 607 607 HOH HOH C . 
U 5 HOH 208 608 608 HOH HOH C . 
U 5 HOH 209 609 609 HOH HOH C . 
U 5 HOH 210 610 610 HOH HOH C . 
U 5 HOH 211 611 611 HOH HOH C . 
U 5 HOH 212 612 612 HOH HOH C . 
V 5 HOH 1   401 401 HOH HOH D . 
V 5 HOH 2   402 402 HOH HOH D . 
V 5 HOH 3   403 403 HOH HOH D . 
V 5 HOH 4   404 404 HOH HOH D . 
V 5 HOH 5   405 405 HOH HOH D . 
V 5 HOH 6   406 406 HOH HOH D . 
V 5 HOH 7   407 407 HOH HOH D . 
V 5 HOH 8   408 408 HOH HOH D . 
V 5 HOH 9   409 409 HOH HOH D . 
V 5 HOH 10  410 410 HOH HOH D . 
V 5 HOH 11  411 411 HOH HOH D . 
V 5 HOH 12  412 412 HOH HOH D . 
V 5 HOH 13  413 413 HOH HOH D . 
V 5 HOH 14  414 414 HOH HOH D . 
V 5 HOH 15  415 415 HOH HOH D . 
V 5 HOH 16  416 416 HOH HOH D . 
V 5 HOH 17  417 417 HOH HOH D . 
V 5 HOH 18  418 418 HOH HOH D . 
V 5 HOH 19  419 419 HOH HOH D . 
V 5 HOH 20  420 420 HOH HOH D . 
V 5 HOH 21  421 421 HOH HOH D . 
V 5 HOH 22  422 422 HOH HOH D . 
V 5 HOH 23  423 423 HOH HOH D . 
V 5 HOH 24  424 424 HOH HOH D . 
V 5 HOH 25  425 425 HOH HOH D . 
V 5 HOH 26  426 426 HOH HOH D . 
V 5 HOH 27  427 427 HOH HOH D . 
V 5 HOH 28  428 428 HOH HOH D . 
V 5 HOH 29  429 429 HOH HOH D . 
V 5 HOH 30  430 430 HOH HOH D . 
V 5 HOH 31  431 431 HOH HOH D . 
V 5 HOH 32  432 432 HOH HOH D . 
V 5 HOH 33  433 433 HOH HOH D . 
V 5 HOH 34  434 434 HOH HOH D . 
V 5 HOH 35  435 435 HOH HOH D . 
V 5 HOH 36  436 436 HOH HOH D . 
V 5 HOH 37  437 437 HOH HOH D . 
V 5 HOH 38  438 438 HOH HOH D . 
V 5 HOH 39  439 439 HOH HOH D . 
V 5 HOH 40  440 440 HOH HOH D . 
V 5 HOH 41  441 441 HOH HOH D . 
V 5 HOH 42  442 442 HOH HOH D . 
V 5 HOH 43  443 443 HOH HOH D . 
V 5 HOH 44  444 444 HOH HOH D . 
V 5 HOH 45  445 445 HOH HOH D . 
V 5 HOH 46  446 446 HOH HOH D . 
V 5 HOH 47  447 447 HOH HOH D . 
V 5 HOH 48  448 448 HOH HOH D . 
V 5 HOH 49  449 449 HOH HOH D . 
V 5 HOH 50  450 450 HOH HOH D . 
V 5 HOH 51  451 451 HOH HOH D . 
V 5 HOH 52  452 452 HOH HOH D . 
V 5 HOH 53  453 453 HOH HOH D . 
V 5 HOH 54  454 454 HOH HOH D . 
V 5 HOH 55  455 455 HOH HOH D . 
V 5 HOH 56  456 456 HOH HOH D . 
V 5 HOH 57  457 457 HOH HOH D . 
V 5 HOH 58  458 458 HOH HOH D . 
V 5 HOH 59  459 459 HOH HOH D . 
V 5 HOH 60  460 460 HOH HOH D . 
V 5 HOH 61  461 461 HOH HOH D . 
V 5 HOH 62  462 462 HOH HOH D . 
V 5 HOH 63  463 463 HOH HOH D . 
V 5 HOH 64  464 464 HOH HOH D . 
V 5 HOH 65  465 465 HOH HOH D . 
V 5 HOH 66  466 466 HOH HOH D . 
V 5 HOH 67  467 467 HOH HOH D . 
V 5 HOH 68  468 468 HOH HOH D . 
V 5 HOH 69  469 469 HOH HOH D . 
V 5 HOH 70  470 470 HOH HOH D . 
V 5 HOH 71  471 471 HOH HOH D . 
V 5 HOH 72  472 472 HOH HOH D . 
V 5 HOH 73  473 473 HOH HOH D . 
V 5 HOH 74  474 474 HOH HOH D . 
V 5 HOH 75  475 475 HOH HOH D . 
V 5 HOH 76  476 476 HOH HOH D . 
V 5 HOH 77  477 477 HOH HOH D . 
V 5 HOH 78  478 478 HOH HOH D . 
V 5 HOH 79  479 479 HOH HOH D . 
V 5 HOH 80  480 480 HOH HOH D . 
V 5 HOH 81  481 481 HOH HOH D . 
V 5 HOH 82  482 482 HOH HOH D . 
V 5 HOH 83  483 483 HOH HOH D . 
V 5 HOH 84  484 484 HOH HOH D . 
V 5 HOH 85  485 485 HOH HOH D . 
V 5 HOH 86  486 486 HOH HOH D . 
V 5 HOH 87  487 487 HOH HOH D . 
V 5 HOH 88  488 488 HOH HOH D . 
V 5 HOH 89  489 489 HOH HOH D . 
V 5 HOH 90  490 490 HOH HOH D . 
V 5 HOH 91  491 491 HOH HOH D . 
V 5 HOH 92  492 492 HOH HOH D . 
V 5 HOH 93  493 493 HOH HOH D . 
V 5 HOH 94  494 494 HOH HOH D . 
V 5 HOH 95  495 495 HOH HOH D . 
V 5 HOH 96  496 496 HOH HOH D . 
V 5 HOH 97  497 497 HOH HOH D . 
V 5 HOH 98  498 498 HOH HOH D . 
V 5 HOH 99  499 499 HOH HOH D . 
V 5 HOH 100 500 500 HOH HOH D . 
V 5 HOH 101 501 501 HOH HOH D . 
V 5 HOH 102 502 502 HOH HOH D . 
V 5 HOH 103 503 503 HOH HOH D . 
V 5 HOH 104 504 504 HOH HOH D . 
V 5 HOH 105 505 505 HOH HOH D . 
V 5 HOH 106 506 506 HOH HOH D . 
V 5 HOH 107 507 507 HOH HOH D . 
V 5 HOH 108 508 508 HOH HOH D . 
V 5 HOH 109 509 509 HOH HOH D . 
V 5 HOH 110 510 510 HOH HOH D . 
V 5 HOH 111 511 511 HOH HOH D . 
V 5 HOH 112 512 512 HOH HOH D . 
V 5 HOH 113 513 513 HOH HOH D . 
V 5 HOH 114 514 514 HOH HOH D . 
V 5 HOH 115 515 515 HOH HOH D . 
V 5 HOH 116 516 516 HOH HOH D . 
V 5 HOH 117 517 517 HOH HOH D . 
V 5 HOH 118 518 518 HOH HOH D . 
V 5 HOH 119 519 519 HOH HOH D . 
V 5 HOH 120 520 520 HOH HOH D . 
V 5 HOH 121 521 521 HOH HOH D . 
V 5 HOH 122 522 522 HOH HOH D . 
V 5 HOH 123 523 523 HOH HOH D . 
V 5 HOH 124 524 524 HOH HOH D . 
V 5 HOH 125 525 525 HOH HOH D . 
V 5 HOH 126 526 526 HOH HOH D . 
V 5 HOH 127 527 527 HOH HOH D . 
V 5 HOH 128 528 528 HOH HOH D . 
V 5 HOH 129 529 529 HOH HOH D . 
V 5 HOH 130 530 530 HOH HOH D . 
V 5 HOH 131 531 531 HOH HOH D . 
V 5 HOH 132 532 532 HOH HOH D . 
V 5 HOH 133 533 533 HOH HOH D . 
V 5 HOH 134 534 534 HOH HOH D . 
V 5 HOH 135 535 535 HOH HOH D . 
V 5 HOH 136 536 536 HOH HOH D . 
V 5 HOH 137 537 537 HOH HOH D . 
V 5 HOH 138 538 538 HOH HOH D . 
V 5 HOH 139 539 539 HOH HOH D . 
V 5 HOH 140 540 540 HOH HOH D . 
V 5 HOH 141 541 541 HOH HOH D . 
V 5 HOH 142 542 542 HOH HOH D . 
V 5 HOH 143 543 543 HOH HOH D . 
V 5 HOH 144 544 544 HOH HOH D . 
V 5 HOH 145 545 545 HOH HOH D . 
V 5 HOH 146 546 546 HOH HOH D . 
V 5 HOH 147 547 547 HOH HOH D . 
V 5 HOH 148 548 548 HOH HOH D . 
V 5 HOH 149 549 549 HOH HOH D . 
V 5 HOH 150 550 550 HOH HOH D . 
V 5 HOH 151 551 551 HOH HOH D . 
V 5 HOH 152 552 552 HOH HOH D . 
V 5 HOH 153 553 553 HOH HOH D . 
V 5 HOH 154 554 554 HOH HOH D . 
V 5 HOH 155 555 555 HOH HOH D . 
V 5 HOH 156 556 556 HOH HOH D . 
V 5 HOH 157 557 557 HOH HOH D . 
V 5 HOH 158 558 558 HOH HOH D . 
V 5 HOH 159 559 559 HOH HOH D . 
V 5 HOH 160 560 560 HOH HOH D . 
V 5 HOH 161 561 561 HOH HOH D . 
V 5 HOH 162 562 562 HOH HOH D . 
V 5 HOH 163 563 563 HOH HOH D . 
V 5 HOH 164 564 564 HOH HOH D . 
V 5 HOH 165 565 565 HOH HOH D . 
V 5 HOH 166 566 566 HOH HOH D . 
V 5 HOH 167 567 567 HOH HOH D . 
V 5 HOH 168 568 568 HOH HOH D . 
V 5 HOH 169 569 569 HOH HOH D . 
V 5 HOH 170 570 570 HOH HOH D . 
V 5 HOH 171 571 571 HOH HOH D . 
V 5 HOH 172 572 572 HOH HOH D . 
V 5 HOH 173 573 573 HOH HOH D . 
V 5 HOH 174 574 574 HOH HOH D . 
V 5 HOH 175 575 575 HOH HOH D . 
V 5 HOH 176 576 576 HOH HOH D . 
V 5 HOH 177 577 577 HOH HOH D . 
V 5 HOH 178 578 578 HOH HOH D . 
V 5 HOH 179 579 579 HOH HOH D . 
V 5 HOH 180 580 580 HOH HOH D . 
V 5 HOH 181 581 581 HOH HOH D . 
V 5 HOH 182 582 582 HOH HOH D . 
V 5 HOH 183 583 583 HOH HOH D . 
V 5 HOH 184 584 584 HOH HOH D . 
V 5 HOH 185 585 585 HOH HOH D . 
V 5 HOH 186 586 586 HOH HOH D . 
V 5 HOH 187 587 587 HOH HOH D . 
V 5 HOH 188 588 588 HOH HOH D . 
V 5 HOH 189 589 589 HOH HOH D . 
V 5 HOH 190 590 590 HOH HOH D . 
V 5 HOH 191 591 591 HOH HOH D . 
V 5 HOH 192 592 592 HOH HOH D . 
V 5 HOH 193 593 593 HOH HOH D . 
V 5 HOH 194 594 594 HOH HOH D . 
V 5 HOH 195 595 595 HOH HOH D . 
V 5 HOH 196 596 596 HOH HOH D . 
V 5 HOH 197 597 597 HOH HOH D . 
V 5 HOH 198 598 598 HOH HOH D . 
V 5 HOH 199 599 599 HOH HOH D . 
V 5 HOH 200 600 600 HOH HOH D . 
V 5 HOH 201 601 601 HOH HOH D . 
V 5 HOH 202 602 602 HOH HOH D . 
V 5 HOH 203 603 603 HOH HOH D . 
V 5 HOH 204 604 604 HOH HOH D . 
V 5 HOH 205 605 605 HOH HOH D . 
V 5 HOH 206 606 606 HOH HOH D . 
V 5 HOH 207 607 607 HOH HOH D . 
V 5 HOH 208 608 608 HOH HOH D . 
V 5 HOH 209 609 609 HOH HOH D . 
V 5 HOH 210 610 610 HOH HOH D . 
V 5 HOH 211 611 611 HOH HOH D . 
V 5 HOH 212 612 612 HOH HOH D . 
V 5 HOH 213 613 613 HOH HOH D . 
V 5 HOH 214 614 614 HOH HOH D . 
V 5 HOH 215 615 615 HOH HOH D . 
V 5 HOH 216 616 616 HOH HOH D . 
V 5 HOH 217 617 617 HOH HOH D . 
V 5 HOH 218 618 618 HOH HOH D . 
V 5 HOH 219 619 619 HOH HOH D . 
V 5 HOH 220 620 620 HOH HOH D . 
V 5 HOH 221 621 621 HOH HOH D . 
V 5 HOH 222 622 622 HOH HOH D . 
V 5 HOH 223 623 623 HOH HOH D . 
V 5 HOH 224 624 624 HOH HOH D . 
V 5 HOH 225 625 625 HOH HOH D . 
V 5 HOH 226 626 626 HOH HOH D . 
V 5 HOH 227 627 627 HOH HOH D . 
V 5 HOH 228 628 628 HOH HOH D . 
V 5 HOH 229 629 629 HOH HOH D . 
V 5 HOH 230 630 630 HOH HOH D . 
V 5 HOH 231 631 631 HOH HOH D . 
V 5 HOH 232 632 632 HOH HOH D . 
V 5 HOH 233 633 633 HOH HOH D . 
V 5 HOH 234 634 634 HOH HOH D . 
V 5 HOH 235 635 635 HOH HOH D . 
V 5 HOH 236 636 636 HOH HOH D . 
V 5 HOH 237 637 637 HOH HOH D . 
V 5 HOH 238 638 638 HOH HOH D . 
V 5 HOH 239 639 639 HOH HOH D . 
V 5 HOH 240 640 640 HOH HOH D . 
V 5 HOH 241 641 641 HOH HOH D . 
V 5 HOH 242 642 642 HOH HOH D . 
V 5 HOH 243 643 643 HOH HOH D . 
V 5 HOH 244 644 644 HOH HOH D . 
V 5 HOH 245 645 645 HOH HOH D . 
V 5 HOH 246 646 646 HOH HOH D . 
V 5 HOH 247 647 647 HOH HOH D . 
V 5 HOH 248 648 648 HOH HOH D . 
V 5 HOH 249 649 649 HOH HOH D . 
V 5 HOH 250 650 650 HOH HOH D . 
V 5 HOH 251 651 651 HOH HOH D . 
V 5 HOH 252 652 652 HOH HOH D . 
V 5 HOH 253 653 653 HOH HOH D . 
V 5 HOH 254 654 654 HOH HOH D . 
V 5 HOH 255 655 655 HOH HOH D . 
V 5 HOH 256 656 656 HOH HOH D . 
V 5 HOH 257 657 657 HOH HOH D . 
V 5 HOH 258 658 658 HOH HOH D . 
V 5 HOH 259 659 659 HOH HOH D . 
V 5 HOH 260 660 660 HOH HOH D . 
V 5 HOH 261 661 661 HOH HOH D . 
V 5 HOH 262 662 662 HOH HOH D . 
V 5 HOH 263 663 663 HOH HOH D . 
V 5 HOH 264 664 664 HOH HOH D . 
V 5 HOH 265 665 665 HOH HOH D . 
V 5 HOH 266 666 666 HOH HOH D . 
V 5 HOH 267 667 667 HOH HOH D . 
V 5 HOH 268 668 668 HOH HOH D . 
V 5 HOH 269 669 669 HOH HOH D . 
V 5 HOH 270 670 670 HOH HOH D . 
V 5 HOH 271 671 671 HOH HOH D . 
V 5 HOH 272 672 672 HOH HOH D . 
V 5 HOH 273 673 673 HOH HOH D . 
V 5 HOH 274 674 674 HOH HOH D . 
V 5 HOH 275 675 675 HOH HOH D . 
V 5 HOH 276 676 676 HOH HOH D . 
V 5 HOH 277 677 677 HOH HOH D . 
V 5 HOH 278 678 678 HOH HOH D . 
V 5 HOH 279 679 679 HOH HOH D . 
V 5 HOH 280 680 680 HOH HOH D . 
V 5 HOH 281 681 681 HOH HOH D . 
V 5 HOH 282 682 682 HOH HOH D . 
V 5 HOH 283 683 683 HOH HOH D . 
V 5 HOH 284 684 684 HOH HOH D . 
V 5 HOH 285 685 685 HOH HOH D . 
V 5 HOH 286 686 686 HOH HOH D . 
V 5 HOH 287 687 687 HOH HOH D . 
V 5 HOH 288 688 688 HOH HOH D . 
V 5 HOH 289 689 689 HOH HOH D . 
V 5 HOH 290 690 690 HOH HOH D . 
V 5 HOH 291 691 691 HOH HOH D . 
V 5 HOH 292 692 692 HOH HOH D . 
V 5 HOH 293 693 693 HOH HOH D . 
V 5 HOH 294 694 694 HOH HOH D . 
V 5 HOH 295 695 695 HOH HOH D . 
V 5 HOH 296 696 696 HOH HOH D . 
V 5 HOH 297 697 697 HOH HOH D . 
# 
loop_
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
_software.pdbx_ordinal 
REFMAC      5.6.0117 ?               program 'Garib N. Murshudov' garib@ysbl.york.ac.uk refinement        
http://www.ccp4.ac.uk/dist/html/refmac5.html Fortran_77 ? 1 
SCALA       3.3.20   2011/05/18      other   'Phil R. Evans'      pre@mrc-lmb.cam.ac.uk 'data scaling'    
http://www.ccp4.ac.uk/dist/html/scala.html   Fortran_77 ? 2 
PDB_EXTRACT 3.006    'June 11, 2008' package PDB                  help@deposit.rcsb.org 'data extraction' 
http://sw-tools.pdb.org/apps/PDB_EXTRACT/    C++        ? 3 
HKL-2000    .        ?               ?       ?                    ?                     'data collection' ? ?          ? 4 
XDS         .        ?               ?       ?                    ?                     'data reduction'  ? ?          ? 5 
MOLREP      .        ?               ?       ?                    ?                     phasing           ? ?          ? 6 
# 
_cell.entry_id           4QJ0 
_cell.length_a           77.510 
_cell.length_b           74.242 
_cell.length_c           91.416 
_cell.angle_alpha        90.00 
_cell.angle_beta         108.87 
_cell.angle_gamma        90.00 
_cell.Z_PDB              8 
_cell.pdbx_unique_axis   ? 
_cell.length_a_esd       ? 
_cell.length_b_esd       ? 
_cell.length_c_esd       ? 
_cell.angle_alpha_esd    ? 
_cell.angle_beta_esd     ? 
_cell.angle_gamma_esd    ? 
# 
_symmetry.entry_id                         4QJ0 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
# 
_exptl.entry_id          4QJ0 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.08 
_exptl_crystal.density_percent_sol   40.86 
_exptl_crystal.description           ? 
_exptl_crystal.F_000                 ? 
_exptl_crystal.preparation           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.temp            291 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              7.0 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.pdbx_details    
'0.1M ammonium citrate pH 7.0, 0.2M ammonium sulfate, 26% PEG 4000, VAPOR DIFFUSION, SITTING DROP, temperature 291K' 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS PILATUS 6M' 
_diffrn_detector.pdbx_collection_date   2012-11-30 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    
;High Heat Load (HHL) Monochromator: Si 111; Large Offset Monochromator (LOM) 
: Si 311, Si 511
;
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_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.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'PETRA III, EMBL c/o DESY BEAMLINE P14 (MX2)' 
_diffrn_source.pdbx_synchrotron_site       'PETRA III, EMBL c/o DESY' 
_diffrn_source.pdbx_synchrotron_beamline   'P14 (MX2)' 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_wavelength_list        0.826606 
# 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.entry_id                     4QJ0 
_reflns.observed_criterion_sigma_I   0 
_reflns.observed_criterion_sigma_F   0 
_reflns.d_resolution_low             86.501 
_reflns.d_resolution_high            1.550 
_reflns.number_obs                   141122 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.400 
_reflns.pdbx_Rmerge_I_obs            ? 
_reflns.pdbx_Rsym_value              0.069 
_reflns.pdbx_netI_over_sigmaI        13.100 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_redundancy              5.200 
_reflns.R_free_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.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.pdbx_chi_squared             ? 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_CC_half                 ? 
_reflns.pdbx_Rpim_I_all              ? 
_reflns.pdbx_Rrim_I_all              ? 
# 
loop_
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_ordinal 
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.percent_possible_all 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.pdbx_redundancy 
_reflns_shell.percent_possible_obs 
_reflns_shell.number_unique_all 
_reflns_shell.number_measured_all 
_reflns_shell.number_measured_obs 
_reflns_shell.number_unique_obs 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_Rrim_I_all 
1 1  1.55 1.63  99.70 0.371 0.371 1.8  5.20 ? ? ? ? ? ? ? ? ? 
1 2  1.63 1.73  98.60 0.265 0.265 2.4  5.00 ? ? ? ? ? ? ? ? ? 
1 3  1.73 1.85  99.90 0.180 0.180 3.5  5.30 ? ? ? ? ? ? ? ? ? 
1 4  1.85 2.00  99.60 0.118 0.118 5.4  5.20 ? ? ? ? ? ? ? ? ? 
1 5  2.00 2.19  98.80 0.085 0.085 7.2  5.10 ? ? ? ? ? ? ? ? ? 
1 6  2.19 2.45  99.80 0.069 0.069 8.5  5.30 ? ? ? ? ? ? ? ? ? 
1 7  2.45 2.83  98.90 0.057 0.057 9.7  5.10 ? ? ? ? ? ? ? ? ? 
1 8  2.83 3.47  99.70 0.051 0.051 10.1 5.40 ? ? ? ? ? ? ? ? ? 
1 9  3.47 4.90  99.00 0.046 0.046 10.4 5.10 ? ? ? ? ? ? ? ? ? 
1 10 4.90 86.50 99.40 0.054 0.054 5.6  5.10 ? ? ? ? ? ? ? ? ? 
# 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.entry_id                                 4QJ0 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     127110 
_refine.ls_number_reflns_all                     141094 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          . 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             67.80 
_refine.ls_d_res_high                            1.55 
_refine.ls_percent_reflns_obs                    99.28 
_refine.ls_R_factor_obs                          0.18456 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.18018 
_refine.ls_R_factor_R_free                       0.22473 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 9.9 
_refine.ls_number_reflns_R_free                  13984 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            0.50 
_refine.occupancy_max                            1.00 
_refine.correlation_coeff_Fo_to_Fc               0.965 
_refine.correlation_coeff_Fo_to_Fc_free          0.948 
_refine.B_iso_mean                               18.990 
_refine.aniso_B[1][1]                            -0.39 
_refine.aniso_B[2][2]                            0.90 
_refine.aniso_B[3][3]                            -0.45 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            0.10 
_refine.aniso_B[2][3]                            0.00 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             1.40 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  'HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT' 
_refine.pdbx_starting_model                      1JD0 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R                       0.097 
_refine.pdbx_overall_ESU_R_Free                  0.101 
_refine.overall_SU_ML                            ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             ? 
_refine.overall_SU_R_Cruickshank_DPI             0.097 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.B_iso_min                                ? 
_refine.B_iso_max                                ? 
_refine.overall_SU_R_free                        ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        8362 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         168 
_refine_hist.number_atoms_solvent             1042 
_refine_hist.number_atoms_total               9572 
_refine_hist.d_res_high                       1.55 
_refine_hist.d_res_low                        67.80 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
r_bond_refined_d             0.023  0.020  ? 9077  'X-RAY DIFFRACTION' ? 
r_bond_other_d               ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          2.237  1.965  ? 12409 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       7.123  5.000  ? 1093  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       37.909 24.655 ? 449   'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       13.768 15.000 ? 1404  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       15.200 15.000 ? 33    'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.167  0.200  ? 1286  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.014  0.021  ? 7186  'X-RAY DIFFRACTION' ? 
r_gen_planes_other           ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_nbd_refined                ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_nbd_other                  ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_nbtor_refined              ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_nbtor_other                ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_refined        ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_other          ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_metal_ion_refined          ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_metal_ion_other            ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_refined       ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_other         ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_refined     ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_other       ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_refined ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_other   ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_mcbond_it                  ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_mcbond_other               ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_mcangle_it                 ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_mcangle_other              ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_scbond_it                  ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_scbond_other               ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_scangle_it                 ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_scangle_other              ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_long_range_B_refined       ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_long_range_B_other         ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_rigid_bond_restr           ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_sphericity_free            ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_sphericity_bonded          ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.d_res_high                       1.550 
_refine_ls_shell.d_res_low                        1.590 
_refine_ls_shell.number_reflns_R_work             9376 
_refine_ls_shell.R_factor_R_work                  0.224 
_refine_ls_shell.percent_reflns_obs               99.76 
_refine_ls_shell.R_factor_R_free                  0.268 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             1007 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.R_factor_obs                     ? 
# 
_struct.entry_id                  4QJ0 
_struct.title                     'Crystal structure of catalytic domain of human carbonic anhydrase isozyme XII with inhibitor' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        4QJ0 
_struct_keywords.text            
'drug design, carbonic anhydrase, benzenesulfonamide, metal-binding, LYASE-LYASE INHIBITOR complex' 
_struct_keywords.pdbx_keywords   'LYASE/LYASE INHIBITOR' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 1 ? 
D N N 1 ? 
E N N 2 ? 
F N N 3 ? 
G N N 4 ? 
H N N 2 ? 
I N N 3 ? 
J N N 4 ? 
K N N 2 ? 
L N N 3 ? 
M N N 4 ? 
N N N 2 ? 
O N N 3 ? 
P N N 3 ? 
Q N N 3 ? 
R N N 4 ? 
S N N 5 ? 
T N N 5 ? 
U N N 5 ? 
V 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.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;SKWTYFGPDGENSWSKKYPSCGGLLQSPIDLHSDILQYDASLTPLEFQGYNLSANKQFLLTNNGHSVKLNLPSDMHIQGL
QSRYSATQLHLHWGNPNDPHGSEHTVSGQHFAAELHIVHYNSDLYPDASTASNKSEGLAVLAVLIEMGSFNPSYDKIFSH
LQHVKYKGQEAFVPGFNIEELLPERTAEYYRYRGSLTTPPCNPTVLWTVFRNPVQISQEQLLALETALYCTHMDDPSPRE
MINNFRQVQKFDERLVYTSFSQ
;
_struct_ref.pdbx_align_begin           30 
_struct_ref.pdbx_db_isoform            ? 
# 
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 4QJ0 A 2 ? 263 ? O43570 30 ? 291 ? 2 263 
2 1 4QJ0 B 2 ? 263 ? O43570 30 ? 291 ? 2 263 
3 1 4QJ0 C 2 ? 263 ? O43570 30 ? 291 ? 2 263 
4 1 4QJ0 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 4QJ0 MET A 1 ? UNP O43570 ? ? 'expression tag' 1 1 
2 4QJ0 MET B 1 ? UNP O43570 ? ? 'expression tag' 1 2 
3 4QJ0 MET C 1 ? UNP O43570 ? ? 'expression tag' 1 3 
4 4QJ0 MET D 1 ? UNP O43570 ? ? 'expression tag' 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,S,T     
2 1 C,D,K,L,M,N,O,P,Q,R,U,V 
# 
_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  1  PHE A 7   ? TRP A 15  ? PHE A 7   TRP A 15  5 ? 9  
HELX_P HELX_P2  2  TYR A 19  ? GLY A 24  ? TYR A 19  GLY A 24  5 ? 6  
HELX_P HELX_P3  3  HIS A 33  ? ASP A 35  ? HIS A 33  ASP A 35  5 ? 3  
HELX_P HELX_P4  4  ASP A 128 ? SER A 133 ? ASP A 128 SER A 133 1 ? 6  
HELX_P HELX_P5  5  ASN A 152 ? SER A 160 ? ASN A 152 SER A 160 1 ? 9  
HELX_P HELX_P6  6  HIS A 161 ? LYS A 166 ? HIS A 161 LYS A 166 5 ? 6  
HELX_P HELX_P7  7  ASN A 178 ? LEU A 183 ? ASN A 178 LEU A 183 5 ? 6  
HELX_P HELX_P8  8  SER A 218 ? ALA A 228 ? SER A 218 ALA A 228 1 ? 11 
HELX_P HELX_P9  9  GLY B 11  ? LYS B 18  ? GLY B 11  LYS B 18  5 ? 8  
HELX_P HELX_P10 10 TYR B 19  ? GLY B 24  ? TYR B 19  GLY B 24  5 ? 6  
HELX_P HELX_P11 11 HIS B 33  ? ASP B 35  ? HIS B 33  ASP B 35  5 ? 3  
HELX_P HELX_P12 12 ASP B 128 ? SER B 133 ? ASP B 128 SER B 133 1 ? 6  
HELX_P HELX_P13 13 ASN B 152 ? SER B 160 ? ASN B 152 SER B 160 1 ? 9  
HELX_P HELX_P14 14 HIS B 161 ? VAL B 165 ? HIS B 161 VAL B 165 5 ? 5  
HELX_P HELX_P15 15 ASN B 178 ? LEU B 183 ? ASN B 178 LEU B 183 5 ? 6  
HELX_P HELX_P16 16 SER B 218 ? ALA B 228 ? SER B 218 ALA B 228 1 ? 11 
HELX_P HELX_P17 17 GLY C 11  ? LYS C 18  ? GLY C 11  LYS C 18  5 ? 8  
HELX_P HELX_P18 18 TYR C 19  ? GLY C 24  ? TYR C 19  GLY C 24  5 ? 6  
HELX_P HELX_P19 19 HIS C 33  ? ASP C 35  ? HIS C 33  ASP C 35  5 ? 3  
HELX_P HELX_P20 20 ASP C 128 ? SER C 133 ? ASP C 128 SER C 133 1 ? 6  
HELX_P HELX_P21 21 ASN C 152 ? SER C 160 ? ASN C 152 SER C 160 1 ? 9  
HELX_P HELX_P22 22 HIS C 161 ? VAL C 165 ? HIS C 161 VAL C 165 5 ? 5  
HELX_P HELX_P23 23 ASN C 178 ? LEU C 183 ? ASN C 178 LEU C 183 5 ? 6  
HELX_P HELX_P24 24 SER C 218 ? LEU C 229 ? SER C 218 LEU C 229 1 ? 12 
HELX_P HELX_P25 25 GLY D 11  ? LYS D 18  ? GLY D 11  LYS D 18  5 ? 8  
HELX_P HELX_P26 26 TYR D 19  ? GLY D 24  ? TYR D 19  GLY D 24  5 ? 6  
HELX_P HELX_P27 27 HIS D 33  ? ASP D 35  ? HIS D 33  ASP D 35  5 ? 3  
HELX_P HELX_P28 28 ASP D 128 ? SER D 133 ? ASP D 128 SER D 133 1 ? 6  
HELX_P HELX_P29 29 TYR D 155 ? SER D 160 ? TYR D 155 SER D 160 1 ? 6  
HELX_P HELX_P30 30 HIS D 161 ? VAL D 165 ? HIS D 161 VAL D 165 5 ? 5  
HELX_P HELX_P31 31 ASN D 178 ? LEU D 183 ? ASN D 178 LEU D 183 5 ? 6  
HELX_P HELX_P32 32 SER D 218 ? ALA D 228 ? SER D 218 ALA D 228 1 ? 11 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1  disulf ? ? A CYS 22  SG  ? ? ? 1_555 A CYS 202 SG ? ? A CYS 22  A CYS 202 1_555 ? ? ? ? ? ? ? 2.089 ? ? 
disulf2  disulf ? ? B CYS 22  SG  ? ? ? 1_555 B CYS 202 SG ? ? B CYS 22  B CYS 202 1_555 ? ? ? ? ? ? ? 2.012 ? ? 
disulf3  disulf ? ? C CYS 22  SG  ? ? ? 1_555 C CYS 202 SG ? ? C CYS 22  C CYS 202 1_555 ? ? ? ? ? ? ? 1.993 ? ? 
disulf4  disulf ? ? D CYS 22  SG  ? ? ? 1_555 D CYS 202 SG ? ? D CYS 22  D CYS 202 1_555 ? ? ? ? ? ? ? 2.049 ? ? 
metalc1  metalc ? ? A HIS 91  NE2 ? ? ? 1_555 E ZN  .   ZN ? ? A HIS 91  A ZN  301 1_555 ? ? ? ? ? ? ? 1.998 ? ? 
metalc2  metalc ? ? A HIS 93  NE2 ? ? ? 1_555 E ZN  .   ZN ? ? A HIS 93  A ZN  301 1_555 ? ? ? ? ? ? ? 2.038 ? ? 
metalc3  metalc ? ? A HIS 117 ND1 ? ? ? 1_555 E ZN  .   ZN ? ? A HIS 117 A ZN  301 1_555 ? ? ? ? ? ? ? 2.034 ? ? 
metalc4  metalc ? ? E ZN  .   ZN  ? ? ? 1_555 G WWX .   N4 ? ? A ZN  301 A WWX 303 1_555 ? ? ? ? ? ? ? 2.013 ? ? 
metalc5  metalc ? ? B HIS 91  NE2 ? ? ? 1_555 H ZN  .   ZN ? ? B HIS 91  B ZN  301 1_555 ? ? ? ? ? ? ? 2.015 ? ? 
metalc6  metalc ? ? B HIS 93  NE2 ? ? ? 1_555 H ZN  .   ZN ? ? B HIS 93  B ZN  301 1_555 ? ? ? ? ? ? ? 2.017 ? ? 
metalc7  metalc ? ? B HIS 117 ND1 ? ? ? 1_555 H ZN  .   ZN ? ? B HIS 117 B ZN  301 1_555 ? ? ? ? ? ? ? 2.029 ? ? 
metalc8  metalc ? ? H ZN  .   ZN  ? ? ? 1_555 J WWX .   N4 ? ? B ZN  301 B WWX 303 1_555 ? ? ? ? ? ? ? 1.734 ? ? 
metalc9  metalc ? ? C HIS 91  NE2 ? ? ? 1_555 K ZN  .   ZN ? ? C HIS 91  C ZN  301 1_555 ? ? ? ? ? ? ? 2.042 ? ? 
metalc10 metalc ? ? C HIS 93  NE2 ? ? ? 1_555 K ZN  .   ZN ? ? C HIS 93  C ZN  301 1_555 ? ? ? ? ? ? ? 1.987 ? ? 
metalc11 metalc ? ? C HIS 117 ND1 ? ? ? 1_555 K ZN  .   ZN ? ? C HIS 117 C ZN  301 1_555 ? ? ? ? ? ? ? 2.043 ? ? 
metalc12 metalc ? ? K ZN  .   ZN  ? ? ? 1_555 M WWX .   N4 ? ? C ZN  301 C WWX 303 1_555 ? ? ? ? ? ? ? 2.078 ? ? 
metalc13 metalc ? ? D HIS 91  NE2 ? ? ? 1_555 N ZN  .   ZN ? ? D HIS 91  D ZN  301 1_555 ? ? ? ? ? ? ? 1.996 ? ? 
metalc14 metalc ? ? D HIS 93  NE2 ? ? ? 1_555 N ZN  .   ZN ? ? D HIS 93  D ZN  301 1_555 ? ? ? ? ? ? ? 2.019 ? ? 
metalc15 metalc ? ? D HIS 117 ND1 ? ? ? 1_555 N ZN  .   ZN ? ? D HIS 117 D ZN  301 1_555 ? ? ? ? ? ? ? 2.053 ? ? 
metalc16 metalc ? ? N ZN  .   ZN  ? ? ? 1_555 R WWX .   N4 B ? D ZN  301 D WWX 305 1_555 ? ? ? ? ? ? ? 1.925 ? ? 
metalc17 metalc ? ? N ZN  .   ZN  ? ? ? 1_555 R WWX .   N4 A ? D ZN  301 D WWX 305 1_555 ? ? ? ? ? ? ? 1.925 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
metalc ? ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  NE2 ? A HIS 91  ? A HIS 91  ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 NE2 ? A HIS 93  ? A HIS 93  ? 1_555 101.8 ? 
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_555 112.0 ? 
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 98.8  ? 
4  NE2 ? A HIS 91  ? A HIS 91  ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 N4  ? G WWX .   ? A WWX 303 ? 1_555 107.1 ? 
5  NE2 ? A HIS 93  ? A HIS 93  ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 N4  ? G WWX .   ? A WWX 303 ? 1_555 114.3 ? 
6  ND1 ? A HIS 117 ? A HIS 117 ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 N4  ? G WWX .   ? A WWX 303 ? 1_555 121.2 ? 
7  NE2 ? B HIS 91  ? B HIS 91  ? 1_555 ZN ? H ZN . ? B ZN 301 ? 1_555 NE2 ? B HIS 93  ? B HIS 93  ? 1_555 104.3 ? 
8  NE2 ? B HIS 91  ? B HIS 91  ? 1_555 ZN ? H ZN . ? B ZN 301 ? 1_555 ND1 ? B HIS 117 ? B HIS 117 ? 1_555 114.0 ? 
9  NE2 ? B HIS 93  ? B HIS 93  ? 1_555 ZN ? H ZN . ? B ZN 301 ? 1_555 ND1 ? B HIS 117 ? B HIS 117 ? 1_555 99.1  ? 
10 NE2 ? B HIS 91  ? B HIS 91  ? 1_555 ZN ? H ZN . ? B ZN 301 ? 1_555 N4  ? J WWX .   ? B WWX 303 ? 1_555 113.2 ? 
11 NE2 ? B HIS 93  ? B HIS 93  ? 1_555 ZN ? H ZN . ? B ZN 301 ? 1_555 N4  ? J WWX .   ? B WWX 303 ? 1_555 113.5 ? 
12 ND1 ? B HIS 117 ? B HIS 117 ? 1_555 ZN ? H ZN . ? B ZN 301 ? 1_555 N4  ? J WWX .   ? B WWX 303 ? 1_555 111.9 ? 
13 NE2 ? C HIS 91  ? C HIS 91  ? 1_555 ZN ? K ZN . ? C ZN 301 ? 1_555 NE2 ? C HIS 93  ? C HIS 93  ? 1_555 102.6 ? 
14 NE2 ? C HIS 91  ? C HIS 91  ? 1_555 ZN ? K ZN . ? C ZN 301 ? 1_555 ND1 ? C HIS 117 ? C HIS 117 ? 1_555 115.0 ? 
15 NE2 ? C HIS 93  ? C HIS 93  ? 1_555 ZN ? K ZN . ? C ZN 301 ? 1_555 ND1 ? C HIS 117 ? C HIS 117 ? 1_555 100.7 ? 
16 NE2 ? C HIS 91  ? C HIS 91  ? 1_555 ZN ? K ZN . ? C ZN 301 ? 1_555 N4  ? M WWX .   ? C WWX 303 ? 1_555 114.4 ? 
17 NE2 ? C HIS 93  ? C HIS 93  ? 1_555 ZN ? K ZN . ? C ZN 301 ? 1_555 N4  ? M WWX .   ? C WWX 303 ? 1_555 108.4 ? 
18 ND1 ? C HIS 117 ? C HIS 117 ? 1_555 ZN ? K ZN . ? C ZN 301 ? 1_555 N4  ? M WWX .   ? C WWX 303 ? 1_555 113.8 ? 
19 NE2 ? D HIS 91  ? D HIS 91  ? 1_555 ZN ? N ZN . ? D ZN 301 ? 1_555 NE2 ? D HIS 93  ? D HIS 93  ? 1_555 103.5 ? 
20 NE2 ? D HIS 91  ? D HIS 91  ? 1_555 ZN ? N ZN . ? D ZN 301 ? 1_555 ND1 ? D HIS 117 ? D HIS 117 ? 1_555 108.6 ? 
21 NE2 ? D HIS 93  ? D HIS 93  ? 1_555 ZN ? N ZN . ? D ZN 301 ? 1_555 ND1 ? D HIS 117 ? D HIS 117 ? 1_555 100.4 ? 
22 NE2 ? D HIS 91  ? D HIS 91  ? 1_555 ZN ? N ZN . ? D ZN 301 ? 1_555 N4  B R WWX .   ? D WWX 305 ? 1_555 113.9 ? 
23 NE2 ? D HIS 93  ? D HIS 93  ? 1_555 ZN ? N ZN . ? D ZN 301 ? 1_555 N4  B R WWX .   ? D WWX 305 ? 1_555 111.2 ? 
24 ND1 ? D HIS 117 ? D HIS 117 ? 1_555 ZN ? N ZN . ? D ZN 301 ? 1_555 N4  B R WWX .   ? D WWX 305 ? 1_555 117.6 ? 
25 NE2 ? D HIS 91  ? D HIS 91  ? 1_555 ZN ? N ZN . ? D ZN 301 ? 1_555 N4  A R WWX .   ? D WWX 305 ? 1_555 113.8 ? 
26 NE2 ? D HIS 93  ? D HIS 93  ? 1_555 ZN ? N ZN . ? D ZN 301 ? 1_555 N4  A R WWX .   ? D WWX 305 ? 1_555 111.2 ? 
27 ND1 ? D HIS 117 ? D HIS 117 ? 1_555 ZN ? N ZN . ? D ZN 301 ? 1_555 N4  A R WWX .   ? D WWX 305 ? 1_555 117.6 ? 
28 N4  B R WWX .   ? D WWX 305 ? 1_555 ZN ? N ZN . ? D ZN 301 ? 1_555 N4  A R WWX .   ? D WWX 305 ? 1_555 0.0   ? 
# 
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 -2.17 
2 PRO 200 A . ? PRO 200 A PRO 201 A ? PRO 201 A 1 11.65 
3 SER 28  B . ? SER 28  B PRO 29  B ? PRO 29  B 1 0.36  
4 PRO 200 B . ? PRO 200 B PRO 201 B ? PRO 201 B 1 4.65  
5 SER 28  C . ? SER 28  C PRO 29  C ? PRO 29  C 1 -2.48 
6 PRO 200 C . ? PRO 200 C PRO 201 C ? PRO 201 C 1 5.25  
7 SER 28  D . ? SER 28  D PRO 29  D ? PRO 29  D 1 -2.17 
8 PRO 200 D . ? PRO 200 D PRO 201 D ? PRO 201 D 1 -0.03 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
A ? 2  ? 
B ? 10 ? 
C ? 6  ? 
D ? 2  ? 
E ? 10 ? 
F ? 6  ? 
G ? 2  ? 
H ? 10 ? 
I ? 6  ? 
J ? 2  ? 
K ? 10 ? 
L ? 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 
A 1 2  ? parallel      
B 1 2  ? parallel      
B 2 3  ? anti-parallel 
B 3 4  ? anti-parallel 
B 4 5  ? parallel      
B 5 6  ? anti-parallel 
B 6 7  ? anti-parallel 
B 7 8  ? anti-parallel 
B 8 9  ? anti-parallel 
B 9 10 ? anti-parallel 
C 1 2  ? anti-parallel 
C 2 3  ? anti-parallel 
C 3 4  ? anti-parallel 
C 4 5  ? anti-parallel 
C 5 6  ? parallel      
D 1 2  ? parallel      
E 1 2  ? parallel      
E 2 3  ? anti-parallel 
E 3 4  ? anti-parallel 
E 4 5  ? parallel      
E 5 6  ? anti-parallel 
E 6 7  ? anti-parallel 
E 7 8  ? anti-parallel 
E 8 9  ? anti-parallel 
E 9 10 ? anti-parallel 
F 1 2  ? anti-parallel 
F 2 3  ? anti-parallel 
F 3 4  ? anti-parallel 
F 4 5  ? anti-parallel 
F 5 6  ? parallel      
G 1 2  ? parallel      
H 1 2  ? parallel      
H 2 3  ? anti-parallel 
H 3 4  ? anti-parallel 
H 4 5  ? parallel      
H 5 6  ? anti-parallel 
H 6 7  ? anti-parallel 
H 7 8  ? anti-parallel 
H 8 9  ? anti-parallel 
H 9 10 ? anti-parallel 
I 1 2  ? anti-parallel 
I 2 3  ? anti-parallel 
I 3 4  ? anti-parallel 
I 4 5  ? anti-parallel 
I 5 6  ? parallel      
J 1 2  ? parallel      
K 1 2  ? parallel      
K 2 3  ? anti-parallel 
K 3 4  ? anti-parallel 
K 4 5  ? parallel      
K 5 6  ? anti-parallel 
K 6 7  ? anti-parallel 
K 7 8  ? anti-parallel 
K 8 9  ? anti-parallel 
K 9 10 ? anti-parallel 
L 1 2  ? anti-parallel 
L 2 3  ? anti-parallel 
L 3 4  ? anti-parallel 
L 4 5  ? anti-parallel 
L 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 
A 1  ASP A 31  ? LEU A 32  ? ASP A 31  LEU A 32  
A 2  THR A 106 ? VAL A 107 ? THR A 106 VAL A 107 
B 1  LEU A 37  ? TYR A 39  ? LEU A 37  TYR A 39  
B 2  VAL A 257 ? THR A 259 ? VAL A 257 THR A 259 
B 3  TYR A 190 ? GLY A 195 ? TYR A 190 GLY A 195 
B 4  VAL A 206 ? PHE A 211 ? VAL A 206 PHE A 211 
B 5  LEU A 139 ? MET A 148 ? LEU A 139 MET A 148 
B 6  ALA A 114 ? ASN A 122 ? ALA A 114 ASN A 122 
B 7  TYR A 85  ? TRP A 94  ? TYR A 85  TRP A 94  
B 8  VAL A 68  ? ASN A 71  ? VAL A 68  ASN A 71  
B 9  GLN A 58  ? ASN A 63  ? GLN A 58  ASN A 63  
B 10 GLU A 171 ? PRO A 175 ? GLU A 171 PRO A 175 
C 1  GLU A 47  ? GLN A 49  ? GLU A 47  GLN A 49  
C 2  HIS A 77  ? GLN A 79  ? HIS A 77  GLN A 79  
C 3  TYR A 85  ? TRP A 94  ? TYR A 85  TRP A 94  
C 4  ALA A 114 ? ASN A 122 ? ALA A 114 ASN A 122 
C 5  LEU A 139 ? MET A 148 ? LEU A 139 MET A 148 
C 6  VAL A 215 ? ILE A 217 ? VAL A 215 ILE A 217 
D 1  ASP B 31  ? LEU B 32  ? ASP B 31  LEU B 32  
D 2  THR B 106 ? VAL B 107 ? THR B 106 VAL B 107 
E 1  LEU B 37  ? TYR B 39  ? LEU B 37  TYR B 39  
E 2  VAL B 257 ? THR B 259 ? VAL B 257 THR B 259 
E 3  TYR B 190 ? GLY B 195 ? TYR B 190 GLY B 195 
E 4  VAL B 206 ? PHE B 211 ? VAL B 206 PHE B 211 
E 5  LEU B 139 ? MET B 148 ? LEU B 139 MET B 148 
E 6  ALA B 114 ? ASN B 122 ? ALA B 114 ASN B 122 
E 7  TYR B 85  ? TRP B 94  ? TYR B 85  TRP B 94  
E 8  VAL B 68  ? ASN B 71  ? VAL B 68  ASN B 71  
E 9  GLN B 58  ? ASN B 63  ? GLN B 58  ASN B 63  
E 10 GLU B 171 ? PRO B 175 ? GLU B 171 PRO B 175 
F 1  GLU B 47  ? GLN B 49  ? GLU B 47  GLN B 49  
F 2  HIS B 77  ? GLN B 79  ? HIS B 77  GLN B 79  
F 3  TYR B 85  ? TRP B 94  ? TYR B 85  TRP B 94  
F 4  ALA B 114 ? ASN B 122 ? ALA B 114 ASN B 122 
F 5  LEU B 139 ? MET B 148 ? LEU B 139 MET B 148 
F 6  VAL B 215 ? ILE B 217 ? VAL B 215 ILE B 217 
G 1  ASP C 31  ? LEU C 32  ? ASP C 31  LEU C 32  
G 2  THR C 106 ? VAL C 107 ? THR C 106 VAL C 107 
H 1  LEU C 37  ? TYR C 39  ? LEU C 37  TYR C 39  
H 2  VAL C 257 ? THR C 259 ? VAL C 257 THR C 259 
H 3  TYR C 190 ? GLY C 195 ? TYR C 190 GLY C 195 
H 4  VAL C 206 ? PHE C 211 ? VAL C 206 PHE C 211 
H 5  LEU C 139 ? MET C 148 ? LEU C 139 MET C 148 
H 6  ALA C 114 ? ASN C 122 ? ALA C 114 ASN C 122 
H 7  TYR C 85  ? TRP C 94  ? TYR C 85  TRP C 94  
H 8  VAL C 68  ? ASN C 71  ? VAL C 68  ASN C 71  
H 9  GLN C 58  ? ASN C 63  ? GLN C 58  ASN C 63  
H 10 GLU C 171 ? PRO C 175 ? GLU C 171 PRO C 175 
I 1  GLU C 47  ? GLN C 49  ? GLU C 47  GLN C 49  
I 2  HIS C 77  ? GLN C 79  ? HIS C 77  GLN C 79  
I 3  TYR C 85  ? TRP C 94  ? TYR C 85  TRP C 94  
I 4  ALA C 114 ? ASN C 122 ? ALA C 114 ASN C 122 
I 5  LEU C 139 ? MET C 148 ? LEU C 139 MET C 148 
I 6  VAL C 215 ? ILE C 217 ? VAL C 215 ILE C 217 
J 1  ASP D 31  ? LEU D 32  ? ASP D 31  LEU D 32  
J 2  THR D 106 ? VAL D 107 ? THR D 106 VAL D 107 
K 1  LEU D 37  ? TYR D 39  ? LEU D 37  TYR D 39  
K 2  VAL D 257 ? THR D 259 ? VAL D 257 THR D 259 
K 3  TYR D 190 ? GLY D 195 ? TYR D 190 GLY D 195 
K 4  VAL D 206 ? PHE D 211 ? VAL D 206 PHE D 211 
K 5  LEU D 139 ? MET D 148 ? LEU D 139 MET D 148 
K 6  ALA D 114 ? ASN D 122 ? ALA D 114 ASN D 122 
K 7  TYR D 85  ? TRP D 94  ? TYR D 85  TRP D 94  
K 8  VAL D 68  ? ASN D 71  ? VAL D 68  ASN D 71  
K 9  GLN D 58  ? ASN D 63  ? GLN D 58  ASN D 63  
K 10 GLU D 171 ? PRO D 175 ? GLU D 171 PRO D 175 
L 1  GLU D 47  ? GLN D 49  ? GLU D 47  GLN D 49  
L 2  HIS D 77  ? GLN D 79  ? HIS D 77  GLN D 79  
L 3  TYR D 85  ? TRP D 94  ? TYR D 85  TRP D 94  
L 4  ALA D 114 ? ASN D 122 ? ALA D 114 ASN D 122 
L 5  LEU D 139 ? MET D 148 ? LEU D 139 MET D 148 
L 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 
A 1 2  N LEU A 32  ? N LEU A 32  O THR A 106 ? O THR A 106 
B 1 2  N GLN A 38  ? N GLN A 38  O VAL A 257 ? O VAL A 257 
B 2 3  O TYR A 258 ? O TYR A 258 N ARG A 192 ? N ARG A 192 
B 3 4  N GLY A 195 ? N GLY A 195 O VAL A 206 ? O VAL A 206 
B 4 5  O THR A 209 ? O THR A 209 N ALA A 143 ? N ALA A 143 
B 5 6  O LEU A 142 ? O LEU A 142 N ILE A 118 ? N ILE A 118 
B 6 7  O VAL A 119 ? O VAL A 119 N GLN A 89  ? N GLN A 89  
B 7 8  O LEU A 90  ? O LEU A 90  N LEU A 70  ? N LEU A 70  
B 8 9  O LYS A 69  ? O LYS A 69  N THR A 62  ? N THR A 62  
B 9 10 N LEU A 61  ? N LEU A 61  O ALA A 172 ? O ALA A 172 
C 1 2  N GLN A 49  ? N GLN A 49  O HIS A 77  ? O HIS A 77  
C 2 3  N ILE A 78  ? N ILE A 78  O TYR A 85  ? O TYR A 85  
C 3 4  N GLN A 89  ? N GLN A 89  O VAL A 119 ? O VAL A 119 
C 4 5  N ILE A 118 ? N ILE A 118 O LEU A 142 ? O LEU A 142 
C 5 6  N GLU A 147 ? N GLU A 147 O VAL A 215 ? O VAL A 215 
D 1 2  N LEU B 32  ? N LEU B 32  O THR B 106 ? O THR B 106 
E 1 2  N GLN B 38  ? N GLN B 38  O VAL B 257 ? O VAL B 257 
E 2 3  O TYR B 258 ? O TYR B 258 N ARG B 192 ? N ARG B 192 
E 3 4  N TYR B 191 ? N TYR B 191 O VAL B 210 ? O VAL B 210 
E 4 5  O THR B 209 ? O THR B 209 N ALA B 143 ? N ALA B 143 
E 5 6  O VAL B 144 ? O VAL B 144 N LEU B 116 ? N LEU B 116 
E 6 7  O VAL B 119 ? O VAL B 119 N GLN B 89  ? N GLN B 89  
E 7 8  O LEU B 90  ? O LEU B 90  N LEU B 70  ? N LEU B 70  
E 8 9  O ASN B 71  ? O ASN B 71  N LEU B 60  ? N LEU B 60  
E 9 10 N LEU B 61  ? N LEU B 61  O ALA B 172 ? O ALA B 172 
F 1 2  N GLN B 49  ? N GLN B 49  O HIS B 77  ? O HIS B 77  
F 2 3  N ILE B 78  ? N ILE B 78  O TYR B 85  ? O TYR B 85  
F 3 4  N GLN B 89  ? N GLN B 89  O VAL B 119 ? O VAL B 119 
F 4 5  N LEU B 116 ? N LEU B 116 O VAL B 144 ? O VAL B 144 
F 5 6  N GLU B 147 ? N GLU B 147 O VAL B 215 ? O VAL B 215 
G 1 2  N LEU C 32  ? N LEU C 32  O THR C 106 ? O THR C 106 
H 1 2  N GLN C 38  ? N GLN C 38  O THR C 259 ? O THR C 259 
H 2 3  O TYR C 258 ? O TYR C 258 N ARG C 192 ? N ARG C 192 
H 3 4  N GLY C 195 ? N GLY C 195 O VAL C 206 ? O VAL C 206 
H 4 5  O THR C 209 ? O THR C 209 N ALA C 143 ? N ALA C 143 
H 5 6  O ILE C 146 ? O ILE C 146 N ALA C 114 ? N ALA C 114 
H 6 7  O VAL C 119 ? O VAL C 119 N GLN C 89  ? N GLN C 89  
H 7 8  O LEU C 90  ? O LEU C 90  N LEU C 70  ? N LEU C 70  
H 8 9  O ASN C 71  ? O ASN C 71  N LEU C 60  ? N LEU C 60  
H 9 10 N LEU C 61  ? N LEU C 61  O ALA C 172 ? O ALA C 172 
I 1 2  N GLN C 49  ? N GLN C 49  O HIS C 77  ? O HIS C 77  
I 2 3  N ILE C 78  ? N ILE C 78  O TYR C 85  ? O TYR C 85  
I 3 4  N GLN C 89  ? N GLN C 89  O VAL C 119 ? O VAL C 119 
I 4 5  N ALA C 114 ? N ALA C 114 O ILE C 146 ? O ILE C 146 
I 5 6  N GLU C 147 ? N GLU C 147 O VAL C 215 ? O VAL C 215 
J 1 2  N LEU D 32  ? N LEU D 32  O THR D 106 ? O THR D 106 
K 1 2  N GLN D 38  ? N GLN D 38  O THR D 259 ? O THR D 259 
K 2 3  O TYR D 258 ? O TYR D 258 N ARG D 192 ? N ARG D 192 
K 3 4  N GLY D 195 ? N GLY D 195 O VAL D 206 ? O VAL D 206 
K 4 5  O THR D 209 ? O THR D 209 N ALA D 143 ? N ALA D 143 
K 5 6  O VAL D 144 ? O VAL D 144 N LEU D 116 ? N LEU D 116 
K 6 7  O TYR D 121 ? O TYR D 121 N SER D 86  ? N SER D 86  
K 7 8  O LEU D 90  ? O LEU D 90  N LEU D 70  ? N LEU D 70  
K 8 9  O ASN D 71  ? O ASN D 71  N LEU D 60  ? N LEU D 60  
K 9 10 N LEU D 61  ? N LEU D 61  O ALA D 172 ? O ALA D 172 
L 1 2  N GLN D 49  ? N GLN D 49  O HIS D 77  ? O HIS D 77  
L 2 3  N ILE D 78  ? N ILE D 78  O TYR D 85  ? O TYR D 85  
L 3 4  N SER D 86  ? N SER D 86  O TYR D 121 ? O TYR D 121 
L 4 5  N LEU D 116 ? N LEU D 116 O VAL D 144 ? O VAL D 144 
L 5 6  N GLU D 147 ? N GLU D 147 O VAL D 215 ? O VAL D 215 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software A ZN  301 ? 4  'BINDING SITE FOR RESIDUE ZN A 301'  
AC2 Software A EDO 302 ? 3  'BINDING SITE FOR RESIDUE EDO A 302' 
AC3 Software A WWX 303 ? 19 'BINDING SITE FOR RESIDUE WWX A 303' 
AC4 Software B ZN  301 ? 4  'BINDING SITE FOR RESIDUE ZN B 301'  
AC5 Software B EDO 302 ? 7  'BINDING SITE FOR RESIDUE EDO B 302' 
AC6 Software B WWX 303 ? 19 'BINDING SITE FOR RESIDUE WWX B 303' 
AC7 Software C ZN  301 ? 4  'BINDING SITE FOR RESIDUE ZN C 301'  
AC8 Software C EDO 302 ? 4  'BINDING SITE FOR RESIDUE EDO C 302' 
AC9 Software C WWX 303 ? 22 'BINDING SITE FOR RESIDUE WWX C 303' 
BC1 Software D ZN  301 ? 4  'BINDING SITE FOR RESIDUE ZN D 301'  
BC2 Software D EDO 302 ? 7  'BINDING SITE FOR RESIDUE EDO D 302' 
BC3 Software D EDO 303 ? 4  'BINDING SITE FOR RESIDUE EDO D 303' 
BC4 Software D EDO 304 ? 3  'BINDING SITE FOR RESIDUE EDO D 304' 
BC5 Software D WWX 305 ? 24 'BINDING SITE FOR RESIDUE WWX 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  WWX G .   ? WWX A 303 . ? 1_555 ? 
5   AC2 3  ASP A 156 ? ASP A 156 . ? 1_555 ? 
6   AC2 3  SER A 160 ? SER A 160 . ? 1_555 ? 
7   AC2 3  HOH S .   ? HOH A 465 . ? 1_555 ? 
8   AC3 19 TRP A 4   ? TRP A 4   . ? 1_555 ? 
9   AC3 19 ASN A 64  ? ASN A 64  . ? 1_555 ? 
10  AC3 19 SER A 67  ? SER A 67  . ? 1_555 ? 
11  AC3 19 THR A 88  ? THR A 88  . ? 1_555 ? 
12  AC3 19 GLN A 89  ? GLN A 89  . ? 1_555 ? 
13  AC3 19 HIS A 91  ? HIS A 91  . ? 1_555 ? 
14  AC3 19 HIS A 93  ? HIS A 93  . ? 1_555 ? 
15  AC3 19 HIS A 117 ? HIS A 117 . ? 1_555 ? 
16  AC3 19 VAL A 119 ? VAL A 119 . ? 1_555 ? 
17  AC3 19 LEU A 139 ? LEU A 139 . ? 1_555 ? 
18  AC3 19 VAL A 141 ? VAL A 141 . ? 1_555 ? 
19  AC3 19 LEU A 197 ? LEU A 197 . ? 1_555 ? 
20  AC3 19 THR A 198 ? THR A 198 . ? 1_555 ? 
21  AC3 19 THR A 199 ? THR A 199 . ? 1_555 ? 
22  AC3 19 PRO A 200 ? PRO A 200 . ? 1_555 ? 
23  AC3 19 PRO A 201 ? PRO A 201 . ? 1_555 ? 
24  AC3 19 ZN  E .   ? ZN  A 301 . ? 1_555 ? 
25  AC3 19 HOH S .   ? HOH A 499 . ? 1_555 ? 
26  AC3 19 HOH S .   ? HOH A 609 . ? 1_555 ? 
27  AC4 4  HIS B 91  ? HIS B 91  . ? 1_555 ? 
28  AC4 4  HIS B 93  ? HIS B 93  . ? 1_555 ? 
29  AC4 4  HIS B 117 ? HIS B 117 . ? 1_555 ? 
30  AC4 4  WWX J .   ? WWX B 303 . ? 1_555 ? 
31  AC5 7  SER B 42  ? SER B 42  . ? 1_555 ? 
32  AC5 7  THR B 44  ? THR B 44  . ? 1_555 ? 
33  AC5 7  LEU B 46  ? LEU B 46  . ? 1_555 ? 
34  AC5 7  GLY B 80  ? GLY B 80  . ? 1_555 ? 
35  AC5 7  LEU B 81  ? LEU B 81  . ? 1_555 ? 
36  AC5 7  TYR B 190 ? TYR B 190 . ? 1_555 ? 
37  AC5 7  ARG B 192 ? ARG B 192 . ? 1_555 ? 
38  AC6 19 TRP B 4   ? TRP B 4   . ? 1_555 ? 
39  AC6 19 ASN B 64  ? ASN B 64  . ? 1_555 ? 
40  AC6 19 THR B 88  ? THR B 88  . ? 1_555 ? 
41  AC6 19 GLN B 89  ? GLN B 89  . ? 1_555 ? 
42  AC6 19 HIS B 91  ? HIS B 91  . ? 1_555 ? 
43  AC6 19 HIS B 93  ? HIS B 93  . ? 1_555 ? 
44  AC6 19 HIS B 117 ? HIS B 117 . ? 1_555 ? 
45  AC6 19 VAL B 119 ? VAL B 119 . ? 1_555 ? 
46  AC6 19 ALA B 129 ? ALA B 129 . ? 1_555 ? 
47  AC6 19 SER B 130 ? SER B 130 . ? 1_555 ? 
48  AC6 19 SER B 133 ? SER B 133 . ? 1_555 ? 
49  AC6 19 LEU B 139 ? LEU B 139 . ? 1_555 ? 
50  AC6 19 LEU B 197 ? LEU B 197 . ? 1_555 ? 
51  AC6 19 THR B 198 ? THR B 198 . ? 1_555 ? 
52  AC6 19 THR B 199 ? THR B 199 . ? 1_555 ? 
53  AC6 19 ZN  H .   ? ZN  B 301 . ? 1_555 ? 
54  AC6 19 HOH T .   ? HOH B 610 . ? 1_555 ? 
55  AC6 19 HOH T .   ? HOH B 661 . ? 1_555 ? 
56  AC6 19 HOH T .   ? HOH B 662 . ? 1_555 ? 
57  AC7 4  HIS C 91  ? HIS C 91  . ? 1_555 ? 
58  AC7 4  HIS C 93  ? HIS C 93  . ? 1_555 ? 
59  AC7 4  HIS C 117 ? HIS C 117 . ? 1_555 ? 
60  AC7 4  WWX M .   ? WWX C 303 . ? 1_555 ? 
61  AC8 4  ASN C 64  ? ASN C 64  . ? 1_555 ? 
62  AC8 4  HIS C 66  ? HIS C 66  . ? 1_555 ? 
63  AC8 4  LYS C 69  ? LYS C 69  . ? 1_555 ? 
64  AC8 4  WWX M .   ? WWX C 303 . ? 1_555 ? 
65  AC9 22 TRP C 4   ? TRP C 4   . ? 1_555 ? 
66  AC9 22 ASN C 64  ? ASN C 64  . ? 1_555 ? 
67  AC9 22 SER C 67  ? SER C 67  . ? 1_555 ? 
68  AC9 22 THR C 88  ? THR C 88  . ? 1_555 ? 
69  AC9 22 GLN C 89  ? GLN C 89  . ? 1_555 ? 
70  AC9 22 HIS C 91  ? HIS C 91  . ? 1_555 ? 
71  AC9 22 HIS C 93  ? HIS C 93  . ? 1_555 ? 
72  AC9 22 HIS C 117 ? HIS C 117 . ? 1_555 ? 
73  AC9 22 VAL C 119 ? VAL C 119 . ? 1_555 ? 
74  AC9 22 ALA C 129 ? ALA C 129 . ? 1_555 ? 
75  AC9 22 SER C 133 ? SER C 133 . ? 1_555 ? 
76  AC9 22 LEU C 139 ? LEU C 139 . ? 1_555 ? 
77  AC9 22 VAL C 141 ? VAL C 141 . ? 1_555 ? 
78  AC9 22 LEU C 197 ? LEU C 197 . ? 1_555 ? 
79  AC9 22 THR C 198 ? THR C 198 . ? 1_555 ? 
80  AC9 22 THR C 199 ? THR C 199 . ? 1_555 ? 
81  AC9 22 PRO C 200 ? PRO C 200 . ? 1_555 ? 
82  AC9 22 PRO C 201 ? PRO C 201 . ? 1_555 ? 
83  AC9 22 TRP C 208 ? TRP C 208 . ? 1_555 ? 
84  AC9 22 ZN  K .   ? ZN  C 301 . ? 1_555 ? 
85  AC9 22 EDO L .   ? EDO C 302 . ? 1_555 ? 
86  AC9 22 HOH U .   ? HOH C 549 . ? 1_555 ? 
87  BC1 4  HIS D 91  ? HIS D 91  . ? 1_555 ? 
88  BC1 4  HIS D 93  ? HIS D 93  . ? 1_555 ? 
89  BC1 4  HIS D 117 ? HIS D 117 . ? 1_555 ? 
90  BC1 4  WWX R .   ? WWX D 305 . ? 1_555 ? 
91  BC2 7  SER D 42  ? SER D 42  . ? 1_555 ? 
92  BC2 7  THR D 44  ? THR D 44  . ? 1_555 ? 
93  BC2 7  LEU D 46  ? LEU D 46  . ? 1_555 ? 
94  BC2 7  GLY D 80  ? GLY D 80  . ? 1_555 ? 
95  BC2 7  TYR D 190 ? TYR D 190 . ? 1_555 ? 
96  BC2 7  ARG D 192 ? ARG D 192 . ? 1_555 ? 
97  BC2 7  HOH V .   ? HOH D 675 . ? 1_555 ? 
98  BC3 4  ASN D 71  ? ASN D 71  . ? 1_555 ? 
99  BC3 4  LEU D 72  ? LEU D 72  . ? 1_555 ? 
100 BC3 4  THR D 88  ? THR D 88  . ? 1_555 ? 
101 BC3 4  HOH V .   ? HOH D 588 . ? 1_555 ? 
102 BC4 3  ASP D 156 ? ASP D 156 . ? 1_555 ? 
103 BC4 3  SER D 160 ? SER D 160 . ? 1_555 ? 
104 BC4 3  HOH V .   ? HOH D 626 . ? 1_555 ? 
105 BC5 24 ASN D 64  ? ASN D 64  . ? 1_555 ? 
106 BC5 24 SER D 67  ? SER D 67  . ? 1_555 ? 
107 BC5 24 GLN D 89  ? GLN D 89  . ? 1_555 ? 
108 BC5 24 HIS D 91  ? HIS D 91  . ? 1_555 ? 
109 BC5 24 HIS D 93  ? HIS D 93  . ? 1_555 ? 
110 BC5 24 HIS D 117 ? HIS D 117 . ? 1_555 ? 
111 BC5 24 VAL D 119 ? VAL D 119 . ? 1_555 ? 
112 BC5 24 ALA D 129 ? ALA D 129 . ? 1_555 ? 
113 BC5 24 SER D 130 ? SER D 130 . ? 1_555 ? 
114 BC5 24 SER D 133 ? SER D 133 . ? 1_555 ? 
115 BC5 24 LEU D 139 ? LEU D 139 . ? 1_555 ? 
116 BC5 24 VAL D 141 ? VAL D 141 . ? 1_555 ? 
117 BC5 24 LEU D 197 ? LEU D 197 . ? 1_555 ? 
118 BC5 24 THR D 198 ? THR D 198 . ? 1_555 ? 
119 BC5 24 THR D 199 ? THR D 199 . ? 1_555 ? 
120 BC5 24 PRO D 200 ? PRO D 200 . ? 1_555 ? 
121 BC5 24 PRO D 201 ? PRO D 201 . ? 1_555 ? 
122 BC5 24 TRP D 208 ? TRP D 208 . ? 1_555 ? 
123 BC5 24 ZN  N .   ? ZN  D 301 . ? 1_555 ? 
124 BC5 24 HOH V .   ? HOH D 500 . ? 1_555 ? 
125 BC5 24 HOH V .   ? HOH D 610 . ? 1_555 ? 
126 BC5 24 HOH V .   ? HOH D 629 . ? 1_555 ? 
127 BC5 24 HOH V .   ? HOH D 634 . ? 1_555 ? 
128 BC5 24 HOH V .   ? HOH D 670 . ? 1_555 ? 
# 
_pdbx_entry_details.entry_id                   4QJ0 
_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 
# 
_pdbx_validate_rmsd_bond.id                        1 
_pdbx_validate_rmsd_bond.PDB_model_num             1 
_pdbx_validate_rmsd_bond.auth_atom_id_1            C 
_pdbx_validate_rmsd_bond.auth_asym_id_1            B 
_pdbx_validate_rmsd_bond.auth_comp_id_1            PHE 
_pdbx_validate_rmsd_bond.auth_seq_id_1             252 
_pdbx_validate_rmsd_bond.PDB_ins_code_1            ? 
_pdbx_validate_rmsd_bond.label_alt_id_1            B 
_pdbx_validate_rmsd_bond.auth_atom_id_2            O 
_pdbx_validate_rmsd_bond.auth_asym_id_2            B 
_pdbx_validate_rmsd_bond.auth_comp_id_2            PHE 
_pdbx_validate_rmsd_bond.auth_seq_id_2             252 
_pdbx_validate_rmsd_bond.PDB_ins_code_2            ? 
_pdbx_validate_rmsd_bond.label_alt_id_2            B 
_pdbx_validate_rmsd_bond.bond_value                1.386 
_pdbx_validate_rmsd_bond.bond_target_value         1.229 
_pdbx_validate_rmsd_bond.bond_deviation            0.157 
_pdbx_validate_rmsd_bond.bond_standard_deviation   0.019 
_pdbx_validate_rmsd_bond.linker_flag               N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ASN A 245 ? ? -93.62  57.85  
2  1 ASP B 99  ? ? -154.32 76.03  
3  1 ASN B 122 ? ? -66.94  97.16  
4  1 ASN B 245 ? ? -92.23  58.08  
5  1 ASP B 253 ? ? -65.68  75.18  
6  1 ASP B 253 ? ? -69.84  75.18  
7  1 PHE C 252 ? ? -150.85 87.51  
8  1 THR D 88  ? ? -130.02 -40.18 
9  1 THR D 88  ? ? -130.02 -40.31 
10 1 ASP D 99  ? ? -156.14 80.99  
11 1 SER D 136 ? B -37.25  131.80 
12 1 ASN D 245 ? ? -93.00  54.58  
# 
_phasing.method   MR 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET 1   ? A MET 1   
2  1 Y 1 A SER 2   ? A SER 2   
3  1 Y 1 A GLN 263 ? A GLN 263 
4  1 Y 1 B MET 1   ? B MET 1   
5  1 Y 1 B SER 2   ? B SER 2   
6  1 Y 1 C MET 1   ? C MET 1   
7  1 Y 1 C SER 2   ? C SER 2   
8  1 Y 1 C GLN 263 ? C GLN 263 
9  1 Y 1 D MET 1   ? D MET 1   
10 1 Y 1 D SER 2   ? D SER 2   
11 1 Y 1 D GLN 263 ? D GLN 263 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CYS N    N  N N 74  
CYS CA   C  N R 75  
CYS C    C  N N 76  
CYS O    O  N N 77  
CYS CB   C  N N 78  
CYS SG   S  N N 79  
CYS OXT  O  N N 80  
CYS H    H  N N 81  
CYS H2   H  N N 82  
CYS HA   H  N N 83  
CYS HB2  H  N N 84  
CYS HB3  H  N N 85  
CYS HG   H  N N 86  
CYS HXT  H  N N 87  
EDO C1   C  N N 88  
EDO O1   O  N N 89  
EDO C2   C  N N 90  
EDO O2   O  N N 91  
EDO H11  H  N N 92  
EDO H12  H  N N 93  
EDO HO1  H  N N 94  
EDO H21  H  N N 95  
EDO H22  H  N N 96  
EDO HO2  H  N N 97  
GLN N    N  N N 98  
GLN CA   C  N S 99  
GLN C    C  N N 100 
GLN O    O  N N 101 
GLN CB   C  N N 102 
GLN CG   C  N N 103 
GLN CD   C  N N 104 
GLN OE1  O  N N 105 
GLN NE2  N  N N 106 
GLN OXT  O  N N 107 
GLN H    H  N N 108 
GLN H2   H  N N 109 
GLN HA   H  N N 110 
GLN HB2  H  N N 111 
GLN HB3  H  N N 112 
GLN HG2  H  N N 113 
GLN HG3  H  N N 114 
GLN HE21 H  N N 115 
GLN HE22 H  N N 116 
GLN HXT  H  N N 117 
GLU N    N  N N 118 
GLU CA   C  N S 119 
GLU C    C  N N 120 
GLU O    O  N N 121 
GLU CB   C  N N 122 
GLU CG   C  N N 123 
GLU CD   C  N N 124 
GLU OE1  O  N N 125 
GLU OE2  O  N N 126 
GLU OXT  O  N N 127 
GLU H    H  N N 128 
GLU H2   H  N N 129 
GLU HA   H  N N 130 
GLU HB2  H  N N 131 
GLU HB3  H  N N 132 
GLU HG2  H  N N 133 
GLU HG3  H  N N 134 
GLU HE2  H  N N 135 
GLU HXT  H  N N 136 
GLY N    N  N N 137 
GLY CA   C  N N 138 
GLY C    C  N N 139 
GLY O    O  N N 140 
GLY OXT  O  N N 141 
GLY H    H  N N 142 
GLY H2   H  N N 143 
GLY HA2  H  N N 144 
GLY HA3  H  N N 145 
GLY HXT  H  N N 146 
HIS N    N  N N 147 
HIS CA   C  N S 148 
HIS C    C  N N 149 
HIS O    O  N N 150 
HIS CB   C  N N 151 
HIS CG   C  Y N 152 
HIS ND1  N  Y N 153 
HIS CD2  C  Y N 154 
HIS CE1  C  Y N 155 
HIS NE2  N  Y N 156 
HIS OXT  O  N N 157 
HIS H    H  N N 158 
HIS H2   H  N N 159 
HIS HA   H  N N 160 
HIS HB2  H  N N 161 
HIS HB3  H  N N 162 
HIS HD1  H  N N 163 
HIS HD2  H  N N 164 
HIS HE1  H  N N 165 
HIS HE2  H  N N 166 
HIS HXT  H  N N 167 
HOH O    O  N N 168 
HOH H1   H  N N 169 
HOH H2   H  N N 170 
ILE N    N  N N 171 
ILE CA   C  N S 172 
ILE C    C  N N 173 
ILE O    O  N N 174 
ILE CB   C  N S 175 
ILE CG1  C  N N 176 
ILE CG2  C  N N 177 
ILE CD1  C  N N 178 
ILE OXT  O  N N 179 
ILE H    H  N N 180 
ILE H2   H  N N 181 
ILE HA   H  N N 182 
ILE HB   H  N N 183 
ILE HG12 H  N N 184 
ILE HG13 H  N N 185 
ILE HG21 H  N N 186 
ILE HG22 H  N N 187 
ILE HG23 H  N N 188 
ILE HD11 H  N N 189 
ILE HD12 H  N N 190 
ILE HD13 H  N N 191 
ILE HXT  H  N N 192 
LEU N    N  N N 193 
LEU CA   C  N S 194 
LEU C    C  N N 195 
LEU O    O  N N 196 
LEU CB   C  N N 197 
LEU CG   C  N N 198 
LEU CD1  C  N N 199 
LEU CD2  C  N N 200 
LEU OXT  O  N N 201 
LEU H    H  N N 202 
LEU H2   H  N N 203 
LEU HA   H  N N 204 
LEU HB2  H  N N 205 
LEU HB3  H  N N 206 
LEU HG   H  N N 207 
LEU HD11 H  N N 208 
LEU HD12 H  N N 209 
LEU HD13 H  N N 210 
LEU HD21 H  N N 211 
LEU HD22 H  N N 212 
LEU HD23 H  N N 213 
LEU HXT  H  N N 214 
LYS N    N  N N 215 
LYS CA   C  N S 216 
LYS C    C  N N 217 
LYS O    O  N N 218 
LYS CB   C  N N 219 
LYS CG   C  N N 220 
LYS CD   C  N N 221 
LYS CE   C  N N 222 
LYS NZ   N  N N 223 
LYS OXT  O  N N 224 
LYS H    H  N N 225 
LYS H2   H  N N 226 
LYS HA   H  N N 227 
LYS HB2  H  N N 228 
LYS HB3  H  N N 229 
LYS HG2  H  N N 230 
LYS HG3  H  N N 231 
LYS HD2  H  N N 232 
LYS HD3  H  N N 233 
LYS HE2  H  N N 234 
LYS HE3  H  N N 235 
LYS HZ1  H  N N 236 
LYS HZ2  H  N N 237 
LYS HZ3  H  N N 238 
LYS HXT  H  N N 239 
MET N    N  N N 240 
MET CA   C  N S 241 
MET C    C  N N 242 
MET O    O  N N 243 
MET CB   C  N N 244 
MET CG   C  N N 245 
MET SD   S  N N 246 
MET CE   C  N N 247 
MET OXT  O  N N 248 
MET H    H  N N 249 
MET H2   H  N N 250 
MET HA   H  N N 251 
MET HB2  H  N N 252 
MET HB3  H  N N 253 
MET HG2  H  N N 254 
MET HG3  H  N N 255 
MET HE1  H  N N 256 
MET HE2  H  N N 257 
MET HE3  H  N N 258 
MET HXT  H  N N 259 
PHE N    N  N N 260 
PHE CA   C  N S 261 
PHE C    C  N N 262 
PHE O    O  N N 263 
PHE CB   C  N N 264 
PHE CG   C  Y N 265 
PHE CD1  C  Y N 266 
PHE CD2  C  Y N 267 
PHE CE1  C  Y N 268 
PHE CE2  C  Y N 269 
PHE CZ   C  Y N 270 
PHE OXT  O  N N 271 
PHE H    H  N N 272 
PHE H2   H  N N 273 
PHE HA   H  N N 274 
PHE HB2  H  N N 275 
PHE HB3  H  N N 276 
PHE HD1  H  N N 277 
PHE HD2  H  N N 278 
PHE HE1  H  N N 279 
PHE HE2  H  N N 280 
PHE HZ   H  N N 281 
PHE HXT  H  N N 282 
PRO N    N  N N 283 
PRO CA   C  N S 284 
PRO C    C  N N 285 
PRO O    O  N N 286 
PRO CB   C  N N 287 
PRO CG   C  N N 288 
PRO CD   C  N N 289 
PRO OXT  O  N N 290 
PRO H    H  N N 291 
PRO HA   H  N N 292 
PRO HB2  H  N N 293 
PRO HB3  H  N N 294 
PRO HG2  H  N N 295 
PRO HG3  H  N N 296 
PRO HD2  H  N N 297 
PRO HD3  H  N N 298 
PRO HXT  H  N N 299 
SER N    N  N N 300 
SER CA   C  N S 301 
SER C    C  N N 302 
SER O    O  N N 303 
SER CB   C  N N 304 
SER OG   O  N N 305 
SER OXT  O  N N 306 
SER H    H  N N 307 
SER H2   H  N N 308 
SER HA   H  N N 309 
SER HB2  H  N N 310 
SER HB3  H  N N 311 
SER HG   H  N N 312 
SER HXT  H  N N 313 
THR N    N  N N 314 
THR CA   C  N S 315 
THR C    C  N N 316 
THR O    O  N N 317 
THR CB   C  N R 318 
THR OG1  O  N N 319 
THR CG2  C  N N 320 
THR OXT  O  N N 321 
THR H    H  N N 322 
THR H2   H  N N 323 
THR HA   H  N N 324 
THR HB   H  N N 325 
THR HG1  H  N N 326 
THR HG21 H  N N 327 
THR HG22 H  N N 328 
THR HG23 H  N N 329 
THR HXT  H  N N 330 
TRP N    N  N N 331 
TRP CA   C  N S 332 
TRP C    C  N N 333 
TRP O    O  N N 334 
TRP CB   C  N N 335 
TRP CG   C  Y N 336 
TRP CD1  C  Y N 337 
TRP CD2  C  Y N 338 
TRP NE1  N  Y N 339 
TRP CE2  C  Y N 340 
TRP CE3  C  Y N 341 
TRP CZ2  C  Y N 342 
TRP CZ3  C  Y N 343 
TRP CH2  C  Y N 344 
TRP OXT  O  N N 345 
TRP H    H  N N 346 
TRP H2   H  N N 347 
TRP HA   H  N N 348 
TRP HB2  H  N N 349 
TRP HB3  H  N N 350 
TRP HD1  H  N N 351 
TRP HE1  H  N N 352 
TRP HE3  H  N N 353 
TRP HZ2  H  N N 354 
TRP HZ3  H  N N 355 
TRP HH2  H  N N 356 
TRP HXT  H  N N 357 
TYR N    N  N N 358 
TYR CA   C  N S 359 
TYR C    C  N N 360 
TYR O    O  N N 361 
TYR CB   C  N N 362 
TYR CG   C  Y N 363 
TYR CD1  C  Y N 364 
TYR CD2  C  Y N 365 
TYR CE1  C  Y N 366 
TYR CE2  C  Y N 367 
TYR CZ   C  Y N 368 
TYR OH   O  N N 369 
TYR OXT  O  N N 370 
TYR H    H  N N 371 
TYR H2   H  N N 372 
TYR HA   H  N N 373 
TYR HB2  H  N N 374 
TYR HB3  H  N N 375 
TYR HD1  H  N N 376 
TYR HD2  H  N N 377 
TYR HE1  H  N N 378 
TYR HE2  H  N N 379 
TYR HH   H  N N 380 
TYR HXT  H  N N 381 
VAL N    N  N N 382 
VAL CA   C  N S 383 
VAL C    C  N N 384 
VAL O    O  N N 385 
VAL CB   C  N N 386 
VAL CG1  C  N N 387 
VAL CG2  C  N N 388 
VAL OXT  O  N N 389 
VAL H    H  N N 390 
VAL H2   H  N N 391 
VAL HA   H  N N 392 
VAL HB   H  N N 393 
VAL HG11 H  N N 394 
VAL HG12 H  N N 395 
VAL HG13 H  N N 396 
VAL HG21 H  N N 397 
VAL HG22 H  N N 398 
VAL HG23 H  N N 399 
VAL HXT  H  N N 400 
WWX O16  O  N N 401 
WWX S14  S  N N 402 
WWX O15  O  N N 403 
WWX C18  C  N N 404 
WWX O20  O  N N 405 
WWX C17  C  N N 406 
WWX C8   C  Y N 407 
WWX C7   C  Y N 408 
WWX F12  F  N N 409 
WWX C6   C  Y N 410 
WWX F11  F  N N 411 
WWX C9   C  Y N 412 
WWX C10  C  Y N 413 
WWX F13  F  N N 414 
WWX C5   C  Y N 415 
WWX S1   S  N N 416 
WWX O3   O  N N 417 
WWX N4   N  N N 418 
WWX O2   O  N N 419 
WWX N19  N  N N 420 
WWX C21  C  N R 421 
WWX C30  C  Y N 422 
WWX C35  C  Y N 423 
WWX C34  C  Y N 424 
WWX C33  C  Y N 425 
WWX C32  C  Y N 426 
WWX C31  C  Y N 427 
WWX C22  C  N S 428 
WWX O29  O  N N 429 
WWX C23  C  Y N 430 
WWX C28  C  Y N 431 
WWX C27  C  Y N 432 
WWX C26  C  Y N 433 
WWX C25  C  Y N 434 
WWX C24  C  Y N 435 
WWX H1   H  N N 436 
WWX H2   H  N N 437 
WWX H3   H  N N 438 
WWX H4   H  N N 439 
WWX H5   H  N N 440 
WWX H6   H  N N 441 
WWX H7   H  N N 442 
WWX H8   H  N N 443 
WWX H9   H  N N 444 
WWX H10  H  N N 445 
WWX H11  H  N N 446 
WWX H12  H  N N 447 
WWX H13  H  N N 448 
WWX H14  H  N N 449 
WWX H15  H  N N 450 
WWX H16  H  N N 451 
WWX H17  H  N N 452 
WWX H18  H  N N 453 
WWX H19  H  N N 454 
WWX H20  H  N N 455 
WWX H21  H  N N 456 
ZN  ZN   ZN N N 457 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
EDO C1  O1   sing N N 83  
EDO C1  C2   sing N N 84  
EDO C1  H11  sing N N 85  
EDO C1  H12  sing N N 86  
EDO O1  HO1  sing N N 87  
EDO C2  O2   sing N N 88  
EDO C2  H21  sing N N 89  
EDO C2  H22  sing N N 90  
EDO O2  HO2  sing N N 91  
GLN N   CA   sing N N 92  
GLN N   H    sing N N 93  
GLN N   H2   sing N N 94  
GLN CA  C    sing N N 95  
GLN CA  CB   sing N N 96  
GLN CA  HA   sing N N 97  
GLN C   O    doub N N 98  
GLN C   OXT  sing N N 99  
GLN CB  CG   sing N N 100 
GLN CB  HB2  sing N N 101 
GLN CB  HB3  sing N N 102 
GLN CG  CD   sing N N 103 
GLN CG  HG2  sing N N 104 
GLN CG  HG3  sing N N 105 
GLN CD  OE1  doub N N 106 
GLN CD  NE2  sing N N 107 
GLN NE2 HE21 sing N N 108 
GLN NE2 HE22 sing N N 109 
GLN OXT HXT  sing N N 110 
GLU N   CA   sing N N 111 
GLU N   H    sing N N 112 
GLU N   H2   sing N N 113 
GLU CA  C    sing N N 114 
GLU CA  CB   sing N N 115 
GLU CA  HA   sing N N 116 
GLU C   O    doub N N 117 
GLU C   OXT  sing N N 118 
GLU CB  CG   sing N N 119 
GLU CB  HB2  sing N N 120 
GLU CB  HB3  sing N N 121 
GLU CG  CD   sing N N 122 
GLU CG  HG2  sing N N 123 
GLU CG  HG3  sing N N 124 
GLU CD  OE1  doub N N 125 
GLU CD  OE2  sing N N 126 
GLU OE2 HE2  sing N N 127 
GLU OXT HXT  sing N N 128 
GLY N   CA   sing N N 129 
GLY N   H    sing N N 130 
GLY N   H2   sing N N 131 
GLY CA  C    sing N N 132 
GLY CA  HA2  sing N N 133 
GLY CA  HA3  sing N N 134 
GLY C   O    doub N N 135 
GLY C   OXT  sing N N 136 
GLY OXT HXT  sing N N 137 
HIS N   CA   sing N N 138 
HIS N   H    sing N N 139 
HIS N   H2   sing N N 140 
HIS CA  C    sing N N 141 
HIS CA  CB   sing N N 142 
HIS CA  HA   sing N N 143 
HIS C   O    doub N N 144 
HIS C   OXT  sing N N 145 
HIS CB  CG   sing N N 146 
HIS CB  HB2  sing N N 147 
HIS CB  HB3  sing N N 148 
HIS CG  ND1  sing Y N 149 
HIS CG  CD2  doub Y N 150 
HIS ND1 CE1  doub Y N 151 
HIS ND1 HD1  sing N N 152 
HIS CD2 NE2  sing Y N 153 
HIS CD2 HD2  sing N N 154 
HIS CE1 NE2  sing Y N 155 
HIS CE1 HE1  sing N N 156 
HIS NE2 HE2  sing N N 157 
HIS OXT HXT  sing N N 158 
HOH O   H1   sing N N 159 
HOH O   H2   sing N N 160 
ILE N   CA   sing N N 161 
ILE N   H    sing N N 162 
ILE N   H2   sing N N 163 
ILE CA  C    sing N N 164 
ILE CA  CB   sing N N 165 
ILE CA  HA   sing N N 166 
ILE C   O    doub N N 167 
ILE C   OXT  sing N N 168 
ILE CB  CG1  sing N N 169 
ILE CB  CG2  sing N N 170 
ILE CB  HB   sing N N 171 
ILE CG1 CD1  sing N N 172 
ILE CG1 HG12 sing N N 173 
ILE CG1 HG13 sing N N 174 
ILE CG2 HG21 sing N N 175 
ILE CG2 HG22 sing N N 176 
ILE CG2 HG23 sing N N 177 
ILE CD1 HD11 sing N N 178 
ILE CD1 HD12 sing N N 179 
ILE CD1 HD13 sing N N 180 
ILE OXT HXT  sing N N 181 
LEU N   CA   sing N N 182 
LEU N   H    sing N N 183 
LEU N   H2   sing N N 184 
LEU CA  C    sing N N 185 
LEU CA  CB   sing N N 186 
LEU CA  HA   sing N N 187 
LEU C   O    doub N N 188 
LEU C   OXT  sing N N 189 
LEU CB  CG   sing N N 190 
LEU CB  HB2  sing N N 191 
LEU CB  HB3  sing N N 192 
LEU CG  CD1  sing N N 193 
LEU CG  CD2  sing N N 194 
LEU CG  HG   sing N N 195 
LEU CD1 HD11 sing N N 196 
LEU CD1 HD12 sing N N 197 
LEU CD1 HD13 sing N N 198 
LEU CD2 HD21 sing N N 199 
LEU CD2 HD22 sing N N 200 
LEU CD2 HD23 sing N N 201 
LEU OXT HXT  sing N N 202 
LYS N   CA   sing N N 203 
LYS N   H    sing N N 204 
LYS N   H2   sing N N 205 
LYS CA  C    sing N N 206 
LYS CA  CB   sing N N 207 
LYS CA  HA   sing N N 208 
LYS C   O    doub N N 209 
LYS C   OXT  sing N N 210 
LYS CB  CG   sing N N 211 
LYS CB  HB2  sing N N 212 
LYS CB  HB3  sing N N 213 
LYS CG  CD   sing N N 214 
LYS CG  HG2  sing N N 215 
LYS CG  HG3  sing N N 216 
LYS CD  CE   sing N N 217 
LYS CD  HD2  sing N N 218 
LYS CD  HD3  sing N N 219 
LYS CE  NZ   sing N N 220 
LYS CE  HE2  sing N N 221 
LYS CE  HE3  sing N N 222 
LYS NZ  HZ1  sing N N 223 
LYS NZ  HZ2  sing N N 224 
LYS NZ  HZ3  sing N N 225 
LYS OXT HXT  sing N N 226 
MET N   CA   sing N N 227 
MET N   H    sing N N 228 
MET N   H2   sing N N 229 
MET CA  C    sing N N 230 
MET CA  CB   sing N N 231 
MET CA  HA   sing N N 232 
MET C   O    doub N N 233 
MET C   OXT  sing N N 234 
MET CB  CG   sing N N 235 
MET CB  HB2  sing N N 236 
MET CB  HB3  sing N N 237 
MET CG  SD   sing N N 238 
MET CG  HG2  sing N N 239 
MET CG  HG3  sing N N 240 
MET SD  CE   sing N N 241 
MET CE  HE1  sing N N 242 
MET CE  HE2  sing N N 243 
MET CE  HE3  sing N N 244 
MET OXT HXT  sing N N 245 
PHE N   CA   sing N N 246 
PHE N   H    sing N N 247 
PHE N   H2   sing N N 248 
PHE CA  C    sing N N 249 
PHE CA  CB   sing N N 250 
PHE CA  HA   sing N N 251 
PHE C   O    doub N N 252 
PHE C   OXT  sing N N 253 
PHE CB  CG   sing N N 254 
PHE CB  HB2  sing N N 255 
PHE CB  HB3  sing N N 256 
PHE CG  CD1  doub Y N 257 
PHE CG  CD2  sing Y N 258 
PHE CD1 CE1  sing Y N 259 
PHE CD1 HD1  sing N N 260 
PHE CD2 CE2  doub Y N 261 
PHE CD2 HD2  sing N N 262 
PHE CE1 CZ   doub Y N 263 
PHE CE1 HE1  sing N N 264 
PHE CE2 CZ   sing Y N 265 
PHE CE2 HE2  sing N N 266 
PHE CZ  HZ   sing N N 267 
PHE OXT HXT  sing N N 268 
PRO N   CA   sing N N 269 
PRO N   CD   sing N N 270 
PRO N   H    sing N N 271 
PRO CA  C    sing N N 272 
PRO CA  CB   sing N N 273 
PRO CA  HA   sing N N 274 
PRO C   O    doub N N 275 
PRO C   OXT  sing N N 276 
PRO CB  CG   sing N N 277 
PRO CB  HB2  sing N N 278 
PRO CB  HB3  sing N N 279 
PRO CG  CD   sing N N 280 
PRO CG  HG2  sing N N 281 
PRO CG  HG3  sing N N 282 
PRO CD  HD2  sing N N 283 
PRO CD  HD3  sing N N 284 
PRO OXT HXT  sing N N 285 
SER N   CA   sing N N 286 
SER N   H    sing N N 287 
SER N   H2   sing N N 288 
SER CA  C    sing N N 289 
SER CA  CB   sing N N 290 
SER CA  HA   sing N N 291 
SER C   O    doub N N 292 
SER C   OXT  sing N N 293 
SER CB  OG   sing N N 294 
SER CB  HB2  sing N N 295 
SER CB  HB3  sing N N 296 
SER OG  HG   sing N N 297 
SER OXT HXT  sing N N 298 
THR N   CA   sing N N 299 
THR N   H    sing N N 300 
THR N   H2   sing N N 301 
THR CA  C    sing N N 302 
THR CA  CB   sing N N 303 
THR CA  HA   sing N N 304 
THR C   O    doub N N 305 
THR C   OXT  sing N N 306 
THR CB  OG1  sing N N 307 
THR CB  CG2  sing N N 308 
THR CB  HB   sing N N 309 
THR OG1 HG1  sing N N 310 
THR CG2 HG21 sing N N 311 
THR CG2 HG22 sing N N 312 
THR CG2 HG23 sing N N 313 
THR OXT HXT  sing N N 314 
TRP N   CA   sing N N 315 
TRP N   H    sing N N 316 
TRP N   H2   sing N N 317 
TRP CA  C    sing N N 318 
TRP CA  CB   sing N N 319 
TRP CA  HA   sing N N 320 
TRP C   O    doub N N 321 
TRP C   OXT  sing N N 322 
TRP CB  CG   sing N N 323 
TRP CB  HB2  sing N N 324 
TRP CB  HB3  sing N N 325 
TRP CG  CD1  doub Y N 326 
TRP CG  CD2  sing Y N 327 
TRP CD1 NE1  sing Y N 328 
TRP CD1 HD1  sing N N 329 
TRP CD2 CE2  doub Y N 330 
TRP CD2 CE3  sing Y N 331 
TRP NE1 CE2  sing Y N 332 
TRP NE1 HE1  sing N N 333 
TRP CE2 CZ2  sing Y N 334 
TRP CE3 CZ3  doub Y N 335 
TRP CE3 HE3  sing N N 336 
TRP CZ2 CH2  doub Y N 337 
TRP CZ2 HZ2  sing N N 338 
TRP CZ3 CH2  sing Y N 339 
TRP CZ3 HZ3  sing N N 340 
TRP CH2 HH2  sing N N 341 
TRP OXT HXT  sing N N 342 
TYR N   CA   sing N N 343 
TYR N   H    sing N N 344 
TYR N   H2   sing N N 345 
TYR CA  C    sing N N 346 
TYR CA  CB   sing N N 347 
TYR CA  HA   sing N N 348 
TYR C   O    doub N N 349 
TYR C   OXT  sing N N 350 
TYR CB  CG   sing N N 351 
TYR CB  HB2  sing N N 352 
TYR CB  HB3  sing N N 353 
TYR CG  CD1  doub Y N 354 
TYR CG  CD2  sing Y N 355 
TYR CD1 CE1  sing Y N 356 
TYR CD1 HD1  sing N N 357 
TYR CD2 CE2  doub Y N 358 
TYR CD2 HD2  sing N N 359 
TYR CE1 CZ   doub Y N 360 
TYR CE1 HE1  sing N N 361 
TYR CE2 CZ   sing Y N 362 
TYR CE2 HE2  sing N N 363 
TYR CZ  OH   sing N N 364 
TYR OH  HH   sing N N 365 
TYR OXT HXT  sing N N 366 
VAL N   CA   sing N N 367 
VAL N   H    sing N N 368 
VAL N   H2   sing N N 369 
VAL CA  C    sing N N 370 
VAL CA  CB   sing N N 371 
VAL CA  HA   sing N N 372 
VAL C   O    doub N N 373 
VAL C   OXT  sing N N 374 
VAL CB  CG1  sing N N 375 
VAL CB  CG2  sing N N 376 
VAL CB  HB   sing N N 377 
VAL CG1 HG11 sing N N 378 
VAL CG1 HG12 sing N N 379 
VAL CG1 HG13 sing N N 380 
VAL CG2 HG21 sing N N 381 
VAL CG2 HG22 sing N N 382 
VAL CG2 HG23 sing N N 383 
VAL OXT HXT  sing N N 384 
WWX O20 C18  sing N N 385 
WWX C18 C17  sing N N 386 
WWX C17 S14  sing N N 387 
WWX C25 C26  doub Y N 388 
WWX C25 C24  sing Y N 389 
WWX C26 C27  sing Y N 390 
WWX C24 C23  doub Y N 391 
WWX C27 C28  doub Y N 392 
WWX C23 C28  sing Y N 393 
WWX C23 C22  sing N N 394 
WWX O29 C22  sing N N 395 
WWX C22 C21  sing N N 396 
WWX O15 S14  doub N N 397 
WWX S14 O16  doub N N 398 
WWX S14 C8   sing N N 399 
WWX F12 C7   sing N N 400 
WWX C8  C7   doub Y N 401 
WWX C8  C9   sing Y N 402 
WWX C7  C6   sing Y N 403 
WWX C21 N19  sing N N 404 
WWX C21 C30  sing N N 405 
WWX N19 C9   sing N N 406 
WWX F11 C6   sing N N 407 
WWX C9  C10  doub Y N 408 
WWX C6  C5   doub Y N 409 
WWX C10 C5   sing Y N 410 
WWX C10 F13  sing N N 411 
WWX C5  S1   sing N N 412 
WWX C30 C31  doub Y N 413 
WWX C30 C35  sing Y N 414 
WWX C31 C32  sing Y N 415 
WWX C35 C34  doub Y N 416 
WWX O3  S1   doub N N 417 
WWX N4  S1   sing N N 418 
WWX S1  O2   doub N N 419 
WWX C32 C33  doub Y N 420 
WWX C34 C33  sing Y N 421 
WWX C18 H1   sing N N 422 
WWX C18 H2   sing N N 423 
WWX O20 H3   sing N N 424 
WWX C17 H4   sing N N 425 
WWX C17 H5   sing N N 426 
WWX N4  H6   sing N N 427 
WWX N4  H7   sing N N 428 
WWX N19 H8   sing N N 429 
WWX C21 H9   sing N N 430 
WWX C35 H10  sing N N 431 
WWX C34 H11  sing N N 432 
WWX C33 H12  sing N N 433 
WWX C32 H13  sing N N 434 
WWX C31 H14  sing N N 435 
WWX C22 H15  sing N N 436 
WWX O29 H16  sing N N 437 
WWX C28 H17  sing N N 438 
WWX C27 H18  sing N N 439 
WWX C26 H19  sing N N 440 
WWX C25 H20  sing N N 441 
WWX C24 H21  sing N N 442 
# 
_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                    4QJ0 
_atom_sites.fract_transf_matrix[1][1]   0.012902 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.004410 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.013469 
_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]   0.011560 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
F  
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . LYS A 1 3   ? 19.373  16.018  18.760  1.00 41.09 ? 3   LYS A N   1 
ATOM   2    C  CA  . LYS A 1 3   ? 18.239  16.435  17.883  1.00 39.27 ? 3   LYS A CA  1 
ATOM   3    C  C   . LYS A 1 3   ? 17.226  15.294  17.707  1.00 38.22 ? 3   LYS A C   1 
ATOM   4    O  O   . LYS A 1 3   ? 16.148  15.300  18.329  1.00 42.45 ? 3   LYS A O   1 
ATOM   5    C  CB  . LYS A 1 3   ? 18.726  16.954  16.513  1.00 48.71 ? 3   LYS A CB  1 
ATOM   6    C  CG  . LYS A 1 3   ? 20.199  16.693  16.212  1.00 50.94 ? 3   LYS A CG  1 
ATOM   7    C  CD  . LYS A 1 3   ? 21.152  17.733  16.819  1.00 50.88 ? 3   LYS A CD  1 
ATOM   8    C  CE  . LYS A 1 3   ? 22.593  17.499  16.359  1.00 53.39 ? 3   LYS A CE  1 
ATOM   9    N  NZ  . LYS A 1 3   ? 22.922  16.045  16.192  1.00 57.10 ? 3   LYS A NZ  1 
ATOM   10   N  N   . TRP A 1 4   ? 17.585  14.302  16.894  1.00 24.60 ? 4   TRP A N   1 
ATOM   11   C  CA  . TRP A 1 4   ? 16.615  13.283  16.476  1.00 18.73 ? 4   TRP A CA  1 
ATOM   12   C  C   . TRP A 1 4   ? 16.554  12.138  17.465  1.00 16.80 ? 4   TRP A C   1 
ATOM   13   O  O   . TRP A 1 4   ? 17.549  11.901  18.240  1.00 15.71 ? 4   TRP A O   1 
ATOM   14   C  CB  . TRP A 1 4   ? 17.069  12.843  15.100  1.00 16.91 ? 4   TRP A CB  1 
ATOM   15   C  CG  . TRP A 1 4   ? 18.383  12.100  15.034  1.00 13.55 ? 4   TRP A CG  1 
ATOM   16   C  CD1 . TRP A 1 4   ? 19.649  12.590  14.777  1.00 16.20 ? 4   TRP A CD1 1 
ATOM   17   C  CD2 . TRP A 1 4   ? 18.582  10.666  15.165  1.00 13.39 ? 4   TRP A CD2 1 
ATOM   18   N  NE1 . TRP A 1 4   ? 20.579  11.585  14.727  1.00 17.33 ? 4   TRP A NE1 1 
ATOM   19   C  CE2 . TRP A 1 4   ? 20.018  10.426  15.017  1.00 13.35 ? 4   TRP A CE2 1 
ATOM   20   C  CE3 . TRP A 1 4   ? 17.763  9.617   15.422  1.00 12.95 ? 4   TRP A CE3 1 
ATOM   21   C  CZ2 . TRP A 1 4   ? 20.550  9.127   15.048  1.00 13.27 ? 4   TRP A CZ2 1 
ATOM   22   C  CZ3 . TRP A 1 4   ? 18.294  8.314   15.485  1.00 11.44 ? 4   TRP A CZ3 1 
ATOM   23   C  CH2 . TRP A 1 4   ? 19.666  8.106   15.309  1.00 12.01 ? 4   TRP A CH2 1 
ATOM   24   N  N   . THR A 1 5   ? 15.424  11.447  17.506  1.00 16.44 ? 5   THR A N   1 
ATOM   25   C  CA  . THR A 1 5   ? 15.202  10.313  18.397  1.00 17.37 ? 5   THR A CA  1 
ATOM   26   C  C   . THR A 1 5   ? 14.515  9.181   17.643  1.00 16.51 ? 5   THR A C   1 
ATOM   27   O  O   . THR A 1 5   ? 14.075  9.330   16.505  1.00 16.29 ? 5   THR A O   1 
ATOM   28   C  CB  . THR A 1 5   ? 14.265  10.696  19.569  1.00 20.77 ? 5   THR A CB  1 
ATOM   29   O  OG1 . THR A 1 5   ? 12.994  11.125  19.027  1.00 21.77 ? 5   THR A OG1 1 
ATOM   30   C  CG2 . THR A 1 5   ? 14.912  11.863  20.383  1.00 21.91 ? 5   THR A CG2 1 
ATOM   31   N  N   . TYR A 1 6   ? 14.405  8.024   18.284  1.00 16.83 ? 6   TYR A N   1 
ATOM   32   C  CA  . TYR A 1 6   ? 13.653  6.912   17.773  1.00 17.36 ? 6   TYR A CA  1 
ATOM   33   C  C   . TYR A 1 6   ? 12.254  6.881   18.351  1.00 20.05 ? 6   TYR A C   1 
ATOM   34   O  O   . TYR A 1 6   ? 11.438  6.076   18.037  1.00 19.21 ? 6   TYR A O   1 
ATOM   35   C  CB  . TYR A 1 6   ? 14.415  5.645   18.185  1.00 18.53 ? 6   TYR A CB  1 
ATOM   36   C  CG  . TYR A 1 6   ? 15.559  5.295   17.294  1.00 14.06 ? 6   TYR A CG  1 
ATOM   37   C  CD1 . TYR A 1 6   ? 16.857  5.403   17.727  1.00 12.04 ? 6   TYR A CD1 1 
ATOM   38   C  CD2 . TYR A 1 6   ? 15.309  4.723   15.996  1.00 15.21 ? 6   TYR A CD2 1 
ATOM   39   C  CE1 . TYR A 1 6   ? 17.925  5.017   17.002  1.00 14.89 ? 6   TYR A CE1 1 
ATOM   40   C  CE2 . TYR A 1 6   ? 16.357  4.317   15.204  1.00 14.04 ? 6   TYR A CE2 1 
ATOM   41   C  CZ  . TYR A 1 6   ? 17.663  4.460   15.705  1.00 13.73 ? 6   TYR A CZ  1 
ATOM   42   O  OH  . TYR A 1 6   ? 18.756  4.129   15.034  1.00 15.44 ? 6   TYR A OH  1 
ATOM   43   N  N   . PHE A 1 7   ? 11.981  7.760   19.311  1.00 25.43 ? 7   PHE A N   1 
ATOM   44   C  CA  . PHE A 1 7   ? 10.683  7.747   19.974  1.00 29.67 ? 7   PHE A CA  1 
ATOM   45   C  C   . PHE A 1 7   ? 10.022  9.114   19.787  1.00 32.31 ? 7   PHE A C   1 
ATOM   46   O  O   . PHE A 1 7   ? 10.726  10.058  19.516  1.00 30.53 ? 7   PHE A O   1 
ATOM   47   C  CB  . PHE A 1 7   ? 10.925  7.461   21.469  1.00 36.56 ? 7   PHE A CB  1 
ATOM   48   C  CG  . PHE A 1 7   ? 11.844  8.465   22.143  1.00 37.93 ? 7   PHE A CG  1 
ATOM   49   C  CD1 . PHE A 1 7   ? 11.354  9.703   22.591  1.00 38.31 ? 7   PHE A CD1 1 
ATOM   50   C  CD2 . PHE A 1 7   ? 13.206  8.196   22.318  1.00 40.25 ? 7   PHE A CD2 1 
ATOM   51   C  CE1 . PHE A 1 7   ? 12.188  10.640  23.183  1.00 36.82 ? 7   PHE A CE1 1 
ATOM   52   C  CE2 . PHE A 1 7   ? 14.044  9.128   22.922  1.00 38.86 ? 7   PHE A CE2 1 
ATOM   53   C  CZ  . PHE A 1 7   ? 13.528  10.359  23.338  1.00 38.22 ? 7   PHE A CZ  1 
ATOM   54   N  N   . GLY A 1 8   ? 8.689   9.247   19.904  1.00 34.07 ? 8   GLY A N   1 
ATOM   55   C  CA  . GLY A 1 8   ? 8.032   10.577  20.202  1.00 36.38 ? 8   GLY A CA  1 
ATOM   56   C  C   . GLY A 1 8   ? 8.037   11.608  19.057  1.00 41.85 ? 8   GLY A C   1 
ATOM   57   O  O   . GLY A 1 8   ? 8.021   11.224  17.895  1.00 48.80 ? 8   GLY A O   1 
ATOM   58   N  N   . PRO A 1 9   ? 8.034   12.913  19.372  1.00 33.61 ? 9   PRO A N   1 
ATOM   59   C  CA  . PRO A 1 9   ? 7.897   14.034  18.411  1.00 34.97 ? 9   PRO A CA  1 
ATOM   60   C  C   . PRO A 1 9   ? 9.044   14.216  17.434  1.00 32.89 ? 9   PRO A C   1 
ATOM   61   O  O   . PRO A 1 9   ? 8.891   14.808  16.331  1.00 24.37 ? 9   PRO A O   1 
ATOM   62   C  CB  . PRO A 1 9   ? 7.806   15.270  19.327  1.00 35.95 ? 9   PRO A CB  1 
ATOM   63   C  CG  . PRO A 1 9   ? 7.139   14.728  20.547  1.00 35.71 ? 9   PRO A CG  1 
ATOM   64   C  CD  . PRO A 1 9   ? 7.752   13.358  20.753  1.00 39.20 ? 9   PRO A CD  1 
ATOM   65   N  N   . ASP A 1 10  ? 10.208  13.723  17.837  1.00 30.67 ? 10  ASP A N   1 
ATOM   66   C  CA  . ASP A 1 10  ? 11.402  13.889  17.052  1.00 29.86 ? 10  ASP A CA  1 
ATOM   67   C  C   . ASP A 1 10  ? 11.723  12.541  16.409  1.00 25.58 ? 10  ASP A C   1 
ATOM   68   O  O   . ASP A 1 10  ? 12.929  12.346  15.965  1.00 22.22 ? 10  ASP A O   1 
ATOM   69   C  CB  . ASP A 1 10  ? 12.557  14.344  17.968  1.00 30.61 ? 10  ASP A CB  1 
ATOM   70   C  CG  . ASP A 1 10  ? 12.414  15.818  18.393  1.00 41.59 ? 10  ASP A CG  1 
ATOM   71   O  OD1 . ASP A 1 10  ? 12.371  16.677  17.471  1.00 42.30 ? 10  ASP A OD1 1 
ATOM   72   O  OD2 . ASP A 1 10  ? 12.334  16.109  19.636  1.00 40.21 ? 10  ASP A OD2 1 
ATOM   73   N  N   . GLY A 1 11  ? 10.665  11.685  16.410  1.00 23.83 ? 11  GLY A N   1 
ATOM   74   C  CA  . GLY A 1 11  ? 10.697  10.242  15.929  1.00 16.68 ? 11  GLY A CA  1 
ATOM   75   C  C   . GLY A 1 11  ? 10.914  10.123  14.409  1.00 13.64 ? 11  GLY A C   1 
ATOM   76   O  O   . GLY A 1 11  ? 11.036  11.110  13.662  1.00 14.95 ? 11  GLY A O   1 
ATOM   77   N  N   . GLU A 1 12  ? 11.038  8.872   13.924  1.00 11.58 ? 12  GLU A N   1 
ATOM   78   C  CA  . GLU A 1 12  ? 11.411  8.697   12.548  1.00 11.41 ? 12  GLU A CA  1 
ATOM   79   C  C   . GLU A 1 12  ? 10.556  9.334   11.464  1.00 9.60  ? 12  GLU A C   1 
ATOM   80   O  O   . GLU A 1 12  ? 11.106  9.695   10.419  1.00 9.84  ? 12  GLU A O   1 
ATOM   81   C  CB  . GLU A 1 12  ? 11.620  7.192   12.254  1.00 10.40 ? 12  GLU A CB  1 
ATOM   82   C  CG  . GLU A 1 12  ? 10.337  6.334   12.223  1.00 9.96  ? 12  GLU A CG  1 
ATOM   83   C  CD  . GLU A 1 12  ? 10.668  4.861   12.375  1.00 11.23 ? 12  GLU A CD  1 
ATOM   84   O  OE1 . GLU A 1 12  ? 10.878  4.226   11.305  1.00 10.57 ? 12  GLU A OE1 1 
ATOM   85   O  OE2 . GLU A 1 12  ? 10.635  4.402   13.545  1.00 11.13 ? 12  GLU A OE2 1 
ATOM   86   N  N   . ASN A 1 13  ? 9.253   9.461   11.707  1.00 10.68 ? 13  ASN A N   1 
ATOM   87   C  CA  . ASN A 1 13  ? 8.436   10.154  10.729  1.00 10.73 ? 13  ASN A CA  1 
ATOM   88   C  C   . ASN A 1 13  ? 8.757   11.658  10.565  1.00 10.38 ? 13  ASN A C   1 
ATOM   89   O  O   . ASN A 1 13  ? 8.409   12.254  9.523   1.00 11.28 ? 13  ASN A O   1 
ATOM   90   C  CB  . ASN A 1 13  ? 6.938   10.015  11.012  1.00 9.51  ? 13  ASN A CB  1 
ATOM   91   C  CG  . ASN A 1 13  ? 6.438   8.567   10.837  1.00 11.24 ? 13  ASN A CG  1 
ATOM   92   O  OD1 . ASN A 1 13  ? 7.173   7.699   10.274  1.00 10.72 ? 13  ASN A OD1 1 
ATOM   93   N  ND2 . ASN A 1 13  ? 5.210   8.288   11.322  1.00 12.51 ? 13  ASN A ND2 1 
ATOM   94   N  N   A SER A 1 14  ? 9.490   12.230  11.530  0.50 10.53 ? 14  SER A N   1 
ATOM   95   N  N   B SER A 1 14  ? 9.468   12.244  11.537  0.50 11.13 ? 14  SER A N   1 
ATOM   96   C  CA  A SER A 1 14  ? 9.829   13.673  11.488  0.50 11.10 ? 14  SER A CA  1 
ATOM   97   C  CA  B SER A 1 14  ? 9.810   13.685  11.458  0.50 12.03 ? 14  SER A CA  1 
ATOM   98   C  C   A SER A 1 14  ? 11.310  13.888  11.126  0.50 11.10 ? 14  SER A C   1 
ATOM   99   C  C   B SER A 1 14  ? 11.269  13.878  10.982  0.50 11.92 ? 14  SER A C   1 
ATOM   100  O  O   A SER A 1 14  ? 11.767  15.013  11.046  0.50 11.32 ? 14  SER A O   1 
ATOM   101  O  O   B SER A 1 14  ? 11.672  14.987  10.689  0.50 12.40 ? 14  SER A O   1 
ATOM   102  C  CB  A SER A 1 14  ? 9.582   14.287  12.875  0.50 11.31 ? 14  SER A CB  1 
ATOM   103  C  CB  B SER A 1 14  ? 9.704   14.320  12.858  0.50 13.02 ? 14  SER A CB  1 
ATOM   104  O  OG  A SER A 1 14  ? 8.209   14.155  13.161  0.50 12.97 ? 14  SER A OG  1 
ATOM   105  O  OG  B SER A 1 14  ? 10.745  13.826  13.665  0.50 17.48 ? 14  SER A OG  1 
ATOM   106  N  N   . TRP A 1 15  ? 12.074  12.807  10.901  1.00 11.78 ? 15  TRP A N   1 
ATOM   107  C  CA  . TRP A 1 15  ? 13.516  12.988  10.479  1.00 11.10 ? 15  TRP A CA  1 
ATOM   108  C  C   . TRP A 1 15  ? 13.701  13.825  9.220   1.00 11.39 ? 15  TRP A C   1 
ATOM   109  O  O   . TRP A 1 15  ? 14.652  14.626  9.109   1.00 10.24 ? 15  TRP A O   1 
ATOM   110  C  CB  . TRP A 1 15  ? 14.236  11.643  10.255  1.00 10.28 ? 15  TRP A CB  1 
ATOM   111  C  CG  . TRP A 1 15  ? 14.423  10.819  11.523  1.00 10.58 ? 15  TRP A CG  1 
ATOM   112  C  CD1 . TRP A 1 15  ? 14.184  11.161  12.835  1.00 10.11 ? 15  TRP A CD1 1 
ATOM   113  C  CD2 . TRP A 1 15  ? 14.858  9.422   11.547  1.00 9.37  ? 15  TRP A CD2 1 
ATOM   114  N  NE1 . TRP A 1 15  ? 14.431  10.103  13.675  1.00 11.14 ? 15  TRP A NE1 1 
ATOM   115  C  CE2 . TRP A 1 15  ? 14.916  9.051   12.960  1.00 8.68  ? 15  TRP A CE2 1 
ATOM   116  C  CE3 . TRP A 1 15  ? 15.267  8.506   10.561  1.00 9.07  ? 15  TRP A CE3 1 
ATOM   117  C  CZ2 . TRP A 1 15  ? 15.245  7.718   13.369  1.00 9.30  ? 15  TRP A CZ2 1 
ATOM   118  C  CZ3 . TRP A 1 15  ? 15.668  7.242   10.974  1.00 9.65  ? 15  TRP A CZ3 1 
ATOM   119  C  CH2 . TRP A 1 15  ? 15.675  6.893   12.341  1.00 8.41  ? 15  TRP A CH2 1 
ATOM   120  N  N   . SER A 1 16  ? 12.788  13.704  8.239   1.00 10.41 ? 16  SER A N   1 
ATOM   121  C  CA  . SER A 1 16  ? 12.924  14.358  6.986   1.00 10.98 ? 16  SER A CA  1 
ATOM   122  C  C   . SER A 1 16  ? 12.813  15.881  7.062   1.00 10.63 ? 16  SER A C   1 
ATOM   123  O  O   . SER A 1 16  ? 13.236  16.487  6.112   1.00 10.29 ? 16  SER A O   1 
ATOM   124  C  CB  . SER A 1 16  ? 11.886  13.786  6.049   1.00 11.14 ? 16  SER A CB  1 
ATOM   125  O  OG  . SER A 1 16  ? 10.641  14.214  6.512   1.00 13.44 ? 16  SER A OG  1 
ATOM   126  N  N   A LYS A 1 17  ? 12.328  16.448  8.138   0.50 11.71 ? 17  LYS A N   1 
ATOM   127  N  N   B LYS A 1 17  ? 12.312  16.377  8.186   0.50 11.13 ? 17  LYS A N   1 
ATOM   128  C  CA  A LYS A 1 17  ? 12.319  17.931  8.204   0.50 10.81 ? 17  LYS A CA  1 
ATOM   129  C  CA  B LYS A 1 17  ? 12.208  17.838  8.351   0.50 10.29 ? 17  LYS A CA  1 
ATOM   130  C  C   A LYS A 1 17  ? 13.769  18.441  8.159   0.50 11.52 ? 17  LYS A C   1 
ATOM   131  C  C   B LYS A 1 17  ? 13.562  18.470  8.424   0.50 10.94 ? 17  LYS A C   1 
ATOM   132  O  O   A LYS A 1 17  ? 14.195  19.248  7.281   0.50 9.54  ? 17  LYS A O   1 
ATOM   133  O  O   B LYS A 1 17  ? 13.787  19.485  7.796   0.50 9.84  ? 17  LYS A O   1 
ATOM   134  C  CB  A LYS A 1 17  ? 11.624  18.346  9.493   0.50 12.29 ? 17  LYS A CB  1 
ATOM   135  C  CB  B LYS A 1 17  ? 11.469  18.255  9.594   0.50 11.21 ? 17  LYS A CB  1 
ATOM   136  C  CG  A LYS A 1 17  ? 10.133  18.072  9.449   0.50 14.20 ? 17  LYS A CG  1 
ATOM   137  C  CG  B LYS A 1 17  ? 11.535  19.762  9.621   0.50 12.01 ? 17  LYS A CG  1 
ATOM   138  C  CD  A LYS A 1 17  ? 9.634   17.693  10.836  0.50 14.28 ? 17  LYS A CD  1 
ATOM   139  C  CD  B LYS A 1 17  ? 10.744  20.315  10.783  0.50 13.43 ? 17  LYS A CD  1 
ATOM   140  C  CE  A LYS A 1 17  ? 8.182   17.185  10.793  0.50 14.20 ? 17  LYS A CE  1 
ATOM   141  C  CE  B LYS A 1 17  ? 9.252   20.003  10.675  0.50 14.38 ? 17  LYS A CE  1 
ATOM   142  N  NZ  A LYS A 1 17  ? 7.547   17.380  12.153  0.50 17.15 ? 17  LYS A NZ  1 
ATOM   143  N  NZ  B LYS A 1 17  ? 8.379   20.648  11.706  0.50 15.02 ? 17  LYS A NZ  1 
ATOM   144  N  N   A LYS A 1 18  ? 14.554  17.929  9.103   0.50 11.38 ? 18  LYS A N   1 
ATOM   145  N  N   B LYS A 1 18  ? 14.467  17.878  9.205   0.50 10.74 ? 18  LYS A N   1 
ATOM   146  C  CA  A LYS A 1 18  ? 15.920  18.438  9.237   0.50 12.14 ? 18  LYS A CA  1 
ATOM   147  C  CA  B LYS A 1 18  ? 15.844  18.415  9.256   0.50 11.67 ? 18  LYS A CA  1 
ATOM   148  C  C   A LYS A 1 18  ? 16.922  17.650  8.396   0.50 12.76 ? 18  LYS A C   1 
ATOM   149  C  C   B LYS A 1 18  ? 16.785  17.731  8.249   0.50 12.29 ? 18  LYS A C   1 
ATOM   150  O  O   A LYS A 1 18  ? 18.080  18.084  8.169   0.50 13.35 ? 18  LYS A O   1 
ATOM   151  O  O   B LYS A 1 18  ? 17.776  18.298  7.791   0.50 13.82 ? 18  LYS A O   1 
ATOM   152  C  CB  A LYS A 1 18  ? 16.326  18.515  10.703  0.50 13.64 ? 18  LYS A CB  1 
ATOM   153  C  CB  B LYS A 1 18  ? 16.414  18.335  10.671  0.50 12.94 ? 18  LYS A CB  1 
ATOM   154  C  CG  A LYS A 1 18  ? 15.552  19.624  11.438  0.50 14.19 ? 18  LYS A CG  1 
ATOM   155  C  CG  B LYS A 1 18  ? 17.890  18.669  10.815  0.50 13.52 ? 18  LYS A CG  1 
ATOM   156  C  CD  A LYS A 1 18  ? 16.233  20.945  11.243  0.50 17.23 ? 18  LYS A CD  1 
ATOM   157  C  CD  B LYS A 1 18  ? 18.305  18.656  12.310  0.50 16.56 ? 18  LYS A CD  1 
ATOM   158  C  CE  A LYS A 1 18  ? 15.396  21.960  11.995  0.50 17.76 ? 18  LYS A CE  1 
ATOM   159  C  CE  B LYS A 1 18  ? 19.799  18.950  12.480  0.50 16.68 ? 18  LYS A CE  1 
ATOM   160  N  NZ  A LYS A 1 18  ? 13.981  21.565  11.655  0.50 15.49 ? 18  LYS A NZ  1 
ATOM   161  N  NZ  B LYS A 1 18  ? 20.308  18.904  13.896  0.50 23.17 ? 18  LYS A NZ  1 
ATOM   162  N  N   . TYR A 1 19  ? 16.480  16.469  7.951   1.00 12.15 ? 19  TYR A N   1 
ATOM   163  C  CA  . TYR A 1 19  ? 17.382  15.554  7.177   1.00 11.32 ? 19  TYR A CA  1 
ATOM   164  C  C   . TYR A 1 19  ? 16.684  15.096  5.930   1.00 10.89 ? 19  TYR A C   1 
ATOM   165  O  O   . TYR A 1 19  ? 15.976  14.076  5.931   1.00 10.06 ? 19  TYR A O   1 
ATOM   166  C  CB  . TYR A 1 19  ? 17.801  14.386  8.069   1.00 11.82 ? 19  TYR A CB  1 
ATOM   167  C  CG  . TYR A 1 19  ? 18.446  14.755  9.345   1.00 12.53 ? 19  TYR A CG  1 
ATOM   168  C  CD1 . TYR A 1 19  ? 19.828  15.068  9.345   1.00 12.30 ? 19  TYR A CD1 1 
ATOM   169  C  CD2 . TYR A 1 19  ? 17.733  14.734  10.548  1.00 11.32 ? 19  TYR A CD2 1 
ATOM   170  C  CE1 . TYR A 1 19  ? 20.452  15.422  10.524  1.00 13.23 ? 19  TYR A CE1 1 
ATOM   171  C  CE2 . TYR A 1 19  ? 18.362  15.089  11.748  1.00 12.02 ? 19  TYR A CE2 1 
ATOM   172  C  CZ  . TYR A 1 19  ? 19.703  15.442  11.701  1.00 14.33 ? 19  TYR A CZ  1 
ATOM   173  O  OH  . TYR A 1 19  ? 20.350  15.727  12.927  1.00 19.50 ? 19  TYR A OH  1 
ATOM   174  N  N   . PRO A 1 20  ? 16.747  15.893  4.872   1.00 10.60 ? 20  PRO A N   1 
ATOM   175  C  CA  . PRO A 1 20  ? 15.865  15.666  3.741   1.00 11.78 ? 20  PRO A CA  1 
ATOM   176  C  C   . PRO A 1 20  ? 16.065  14.321  3.055   1.00 11.92 ? 20  PRO A C   1 
ATOM   177  O  O   . PRO A 1 20  ? 15.118  13.800  2.464   1.00 11.91 ? 20  PRO A O   1 
ATOM   178  C  CB  . PRO A 1 20  ? 16.178  16.785  2.773   1.00 12.38 ? 20  PRO A CB  1 
ATOM   179  C  CG  . PRO A 1 20  ? 16.757  17.806  3.614   1.00 13.37 ? 20  PRO A CG  1 
ATOM   180  C  CD  . PRO A 1 20  ? 17.503  17.155  4.707   1.00 10.51 ? 20  PRO A CD  1 
ATOM   181  N  N   . SER A 1 21  ? 17.275  13.737  3.121   1.00 10.85 ? 21  SER A N   1 
ATOM   182  C  CA  . SER A 1 21  ? 17.450  12.449  2.502   1.00 10.67 ? 21  SER A CA  1 
ATOM   183  C  C   . SER A 1 21  ? 16.651  11.354  3.206   1.00 10.49 ? 21  SER A C   1 
ATOM   184  O  O   . SER A 1 21  ? 16.416  10.380  2.586   1.00 9.55  ? 21  SER A O   1 
ATOM   185  C  CB  . SER A 1 21  ? 18.957  12.082  2.549   1.00 10.19 ? 21  SER A CB  1 
ATOM   186  O  OG  . SER A 1 21  ? 19.685  12.878  1.608   1.00 12.47 ? 21  SER A OG  1 
ATOM   187  N  N   . CYS A 1 22  ? 16.173  11.559  4.438   1.00 9.66  ? 22  CYS A N   1 
ATOM   188  C  CA  . CYS A 1 22  ? 15.301  10.565  5.130   1.00 9.94  ? 22  CYS A CA  1 
ATOM   189  C  C   . CYS A 1 22  ? 13.970  10.333  4.372   1.00 11.59 ? 22  CYS A C   1 
ATOM   190  O  O   . CYS A 1 22  ? 13.295  9.345   4.589   1.00 12.00 ? 22  CYS A O   1 
ATOM   191  C  CB  . CYS A 1 22  ? 15.080  10.999  6.616   1.00 9.16  ? 22  CYS A CB  1 
ATOM   192  S  SG  . CYS A 1 22  ? 16.719  10.960  7.459   1.00 10.42 ? 22  CYS A SG  1 
ATOM   193  N  N   . GLY A 1 23  ? 13.627  11.315  3.528   1.00 10.14 ? 23  GLY A N   1 
ATOM   194  C  CA  . GLY A 1 23  ? 12.405  11.238  2.658   1.00 10.36 ? 23  GLY A CA  1 
ATOM   195  C  C   . GLY A 1 23  ? 12.710  11.039  1.215   1.00 10.05 ? 23  GLY A C   1 
ATOM   196  O  O   . GLY A 1 23  ? 11.799  11.099  0.378   1.00 10.38 ? 23  GLY A O   1 
ATOM   197  N  N   . GLY A 1 24  ? 13.935  10.706  0.885   1.00 10.35 ? 24  GLY A N   1 
ATOM   198  C  CA  . GLY A 1 24  ? 14.359  10.518  -0.486  1.00 11.25 ? 24  GLY A CA  1 
ATOM   199  C  C   . GLY A 1 24  ? 14.474  9.090   -0.906  1.00 12.00 ? 24  GLY A C   1 
ATOM   200  O  O   . GLY A 1 24  ? 13.741  8.264   -0.426  1.00 12.57 ? 24  GLY A O   1 
ATOM   201  N  N   . LEU A 1 25  ? 15.320  8.894   -1.912  1.00 13.89 ? 25  LEU A N   1 
ATOM   202  C  CA  . LEU A 1 25  ? 15.442  7.634   -2.538  1.00 13.61 ? 25  LEU A CA  1 
ATOM   203  C  C   . LEU A 1 25  ? 16.352  6.685   -1.749  1.00 14.03 ? 25  LEU A C   1 
ATOM   204  O  O   . LEU A 1 25  ? 17.162  7.069   -0.865  1.00 13.90 ? 25  LEU A O   1 
ATOM   205  C  CB  . LEU A 1 25  ? 15.969  7.761   -3.988  1.00 17.28 ? 25  LEU A CB  1 
ATOM   206  C  CG  . LEU A 1 25  ? 15.062  8.595   -4.990  1.00 19.94 ? 25  LEU A CG  1 
ATOM   207  C  CD1 . LEU A 1 25  ? 15.852  8.761   -6.258  1.00 22.99 ? 25  LEU A CD1 1 
ATOM   208  C  CD2 . LEU A 1 25  ? 13.595  8.117   -5.210  1.00 23.81 ? 25  LEU A CD2 1 
ATOM   209  N  N   . LEU A 1 26  ? 16.157  5.409   -2.083  1.00 13.31 ? 26  LEU A N   1 
ATOM   210  C  CA  . LEU A 1 26  ? 17.096  4.323   -1.737  1.00 13.23 ? 26  LEU A CA  1 
ATOM   211  C  C   . LEU A 1 26  ? 17.155  4.099   -0.185  1.00 11.95 ? 26  LEU A C   1 
ATOM   212  O  O   . LEU A 1 26  ? 18.201  3.784   0.392   1.00 13.23 ? 26  LEU A O   1 
ATOM   213  C  CB  . LEU A 1 26  ? 18.520  4.532   -2.280  1.00 15.07 ? 26  LEU A CB  1 
ATOM   214  C  CG  . LEU A 1 26  ? 18.865  4.456   -3.780  1.00 20.88 ? 26  LEU A CG  1 
ATOM   215  C  CD1 . LEU A 1 26  ? 20.404  4.439   -3.903  1.00 20.91 ? 26  LEU A CD1 1 
ATOM   216  C  CD2 . LEU A 1 26  ? 18.339  3.216   -4.454  1.00 18.70 ? 26  LEU A CD2 1 
ATOM   217  N  N   . GLN A 1 27  ? 16.048  4.278   0.499   1.00 10.68 ? 27  GLN A N   1 
ATOM   218  C  CA  . GLN A 1 27  ? 16.090  4.225   1.943   1.00 8.23  ? 27  GLN A CA  1 
ATOM   219  C  C   . GLN A 1 27  ? 16.085  2.786   2.489   1.00 8.48  ? 27  GLN A C   1 
ATOM   220  O  O   . GLN A 1 27  ? 15.379  1.878   1.963   1.00 10.25 ? 27  GLN A O   1 
ATOM   221  C  CB  . GLN A 1 27  ? 14.914  4.948   2.591   1.00 8.71  ? 27  GLN A CB  1 
ATOM   222  C  CG  . GLN A 1 27  ? 15.024  6.405   2.241   1.00 8.15  ? 27  GLN A CG  1 
ATOM   223  C  CD  . GLN A 1 27  ? 16.183  7.084   3.007   1.00 6.88  ? 27  GLN A CD  1 
ATOM   224  O  OE1 . GLN A 1 27  ? 16.135  7.324   4.243   1.00 7.55  ? 27  GLN A OE1 1 
ATOM   225  N  NE2 . GLN A 1 27  ? 17.211  7.380   2.237   1.00 7.68  ? 27  GLN A NE2 1 
ATOM   226  N  N   . SER A 1 28  ? 16.850  2.611   3.601   1.00 8.04  ? 28  SER A N   1 
ATOM   227  C  CA  . SER A 1 28  ? 16.970  1.345   4.336   1.00 7.62  ? 28  SER A CA  1 
ATOM   228  C  C   . SER A 1 28  ? 16.393  1.559   5.731   1.00 7.65  ? 28  SER A C   1 
ATOM   229  O  O   . SER A 1 28  ? 16.317  2.670   6.189   1.00 7.77  ? 28  SER A O   1 
ATOM   230  C  CB  . SER A 1 28  ? 18.486  1.056   4.442   1.00 6.61  ? 28  SER A CB  1 
ATOM   231  O  OG  . SER A 1 28  ? 19.011  0.804   3.150   1.00 7.31  ? 28  SER A OG  1 
ATOM   232  N  N   . PRO A 1 29  ? 16.056  0.525   6.478   1.00 7.23  ? 29  PRO A N   1 
ATOM   233  C  CA  . PRO A 1 29  ? 16.148  -0.865  6.059   1.00 7.33  ? 29  PRO A CA  1 
ATOM   234  C  C   . PRO A 1 29  ? 14.894  -1.332  5.282   1.00 7.75  ? 29  PRO A C   1 
ATOM   235  O  O   . PRO A 1 29  ? 13.962  -0.568  5.047   1.00 9.67  ? 29  PRO A O   1 
ATOM   236  C  CB  . PRO A 1 29  ? 16.192  -1.585  7.403   1.00 7.02  ? 29  PRO A CB  1 
ATOM   237  C  CG  . PRO A 1 29  ? 15.139  -0.824  8.226   1.00 6.68  ? 29  PRO A CG  1 
ATOM   238  C  CD  . PRO A 1 29  ? 15.528  0.669   7.865   1.00 6.49  ? 29  PRO A CD  1 
ATOM   239  N  N   . ILE A 1 30  ? 14.935  -2.586  4.861   1.00 8.28  ? 30  ILE A N   1 
ATOM   240  C  CA  . ILE A 1 30  ? 13.894  -3.158  4.003   1.00 8.29  ? 30  ILE A CA  1 
ATOM   241  C  C   . ILE A 1 30  ? 13.610  -4.602  4.454   1.00 9.14  ? 30  ILE A C   1 
ATOM   242  O  O   . ILE A 1 30  ? 14.358  -5.198  5.229   1.00 9.37  ? 30  ILE A O   1 
ATOM   243  C  CB  . ILE A 1 30  ? 14.303  -3.196  2.534   1.00 9.12  ? 30  ILE A CB  1 
ATOM   244  C  CG1 . ILE A 1 30  ? 15.543  -4.133  2.337   1.00 8.75  ? 30  ILE A CG1 1 
ATOM   245  C  CG2 . ILE A 1 30  ? 14.519  -1.703  2.079   1.00 10.77 ? 30  ILE A CG2 1 
ATOM   246  C  CD1 . ILE A 1 30  ? 15.936  -4.209  0.835   1.00 10.10 ? 30  ILE A CD1 1 
ATOM   247  N  N   . ASP A 1 31  ? 12.461  -5.100  3.989   1.00 9.94  ? 31  ASP A N   1 
ATOM   248  C  CA  . ASP A 1 31  ? 12.114  -6.470  4.210   1.00 10.10 ? 31  ASP A CA  1 
ATOM   249  C  C   . ASP A 1 31  ? 12.739  -7.265  3.095   1.00 11.91 ? 31  ASP A C   1 
ATOM   250  O  O   . ASP A 1 31  ? 12.616  -6.961  1.868   1.00 13.74 ? 31  ASP A O   1 
ATOM   251  C  CB  . ASP A 1 31  ? 10.585  -6.631  4.114   1.00 10.78 ? 31  ASP A CB  1 
ATOM   252  C  CG  . ASP A 1 31  ? 10.151  -8.075  4.315   1.00 13.44 ? 31  ASP A CG  1 
ATOM   253  O  OD1 . ASP A 1 31  ? 10.686  -8.738  5.205   1.00 11.37 ? 31  ASP A OD1 1 
ATOM   254  O  OD2 . ASP A 1 31  ? 9.208   -8.502  3.651   1.00 18.54 ? 31  ASP A OD2 1 
ATOM   255  N  N   . LEU A 1 32  ? 13.442  -8.310  3.478   1.00 10.69 ? 32  LEU A N   1 
ATOM   256  C  CA  . LEU A 1 32  ? 14.104  -9.218  2.496   1.00 12.73 ? 32  LEU A CA  1 
ATOM   257  C  C   . LEU A 1 32  ? 13.189  -10.407 2.251   1.00 13.63 ? 32  LEU A C   1 
ATOM   258  O  O   . LEU A 1 32  ? 12.986  -11.243 3.122   1.00 14.64 ? 32  LEU A O   1 
ATOM   259  C  CB  . LEU A 1 32  ? 15.448  -9.738  3.080   1.00 12.43 ? 32  LEU A CB  1 
ATOM   260  C  CG  . LEU A 1 32  ? 16.343  -8.563  3.482   1.00 11.38 ? 32  LEU A CG  1 
ATOM   261  C  CD1 . LEU A 1 32  ? 17.570  -9.039  4.259   1.00 12.69 ? 32  LEU A CD1 1 
ATOM   262  C  CD2 . LEU A 1 32  ? 16.847  -7.803  2.262   1.00 14.64 ? 32  LEU A CD2 1 
ATOM   263  N  N   . HIS A 1 33  ? 12.510  -10.458 1.111   1.00 17.12 ? 33  HIS A N   1 
ATOM   264  C  CA  . HIS A 1 33  ? 11.511  -11.557 0.954   1.00 19.83 ? 33  HIS A CA  1 
ATOM   265  C  C   . HIS A 1 33  ? 11.627  -12.133 -0.385  1.00 22.19 ? 33  HIS A C   1 
ATOM   266  O  O   . HIS A 1 33  ? 12.140  -11.463 -1.294  1.00 21.31 ? 33  HIS A O   1 
ATOM   267  C  CB  . HIS A 1 33  ? 10.108  -11.036 1.274   1.00 22.14 ? 33  HIS A CB  1 
ATOM   268  C  CG  . HIS A 1 33  ? 9.632   -9.938  0.338   1.00 22.63 ? 33  HIS A CG  1 
ATOM   269  N  ND1 . HIS A 1 33  ? 9.920   -8.623  0.530   1.00 26.35 ? 33  HIS A ND1 1 
ATOM   270  C  CD2 . HIS A 1 33  ? 8.832   -10.009 -0.814  1.00 25.71 ? 33  HIS A CD2 1 
ATOM   271  C  CE1 . HIS A 1 33  ? 9.317   -7.883  -0.460  1.00 26.14 ? 33  HIS A CE1 1 
ATOM   272  N  NE2 . HIS A 1 33  ? 8.687   -8.733  -1.294  1.00 29.91 ? 33  HIS A NE2 1 
ATOM   273  N  N   . SER A 1 34  ? 11.161  -13.367 -0.552  1.00 21.76 ? 34  SER A N   1 
ATOM   274  C  CA  . SER A 1 34  ? 11.631  -14.135 -1.695  1.00 25.52 ? 34  SER A CA  1 
ATOM   275  C  C   . SER A 1 34  ? 11.239  -13.550 -3.056  1.00 27.96 ? 34  SER A C   1 
ATOM   276  O  O   . SER A 1 34  ? 12.000  -13.769 -4.014  1.00 31.49 ? 34  SER A O   1 
ATOM   277  C  CB  . SER A 1 34  ? 11.384  -15.658 -1.587  1.00 33.26 ? 34  SER A CB  1 
ATOM   278  O  OG  . SER A 1 34  ? 10.081  -15.907 -1.152  1.00 36.46 ? 34  SER A OG  1 
ATOM   279  N  N   . ASP A 1 35  ? 10.114  -12.809 -3.119  1.00 28.07 ? 35  ASP A N   1 
ATOM   280  C  CA  . ASP A 1 35  ? 9.650   -12.140 -4.354  1.00 32.91 ? 35  ASP A CA  1 
ATOM   281  C  C   . ASP A 1 35  ? 10.677  -11.258 -5.018  1.00 31.46 ? 35  ASP A C   1 
ATOM   282  O  O   . ASP A 1 35  ? 10.674  -11.122 -6.247  1.00 29.53 ? 35  ASP A O   1 
ATOM   283  C  CB  . ASP A 1 35  ? 8.417   -11.267 -4.112  1.00 36.83 ? 35  ASP A CB  1 
ATOM   284  C  CG  . ASP A 1 35  ? 7.147   -11.951 -4.538  1.00 46.08 ? 35  ASP A CG  1 
ATOM   285  O  OD1 . ASP A 1 35  ? 7.261   -13.039 -5.156  1.00 51.02 ? 35  ASP A OD1 1 
ATOM   286  O  OD2 . ASP A 1 35  ? 6.046   -11.426 -4.234  1.00 48.81 ? 35  ASP A OD2 1 
ATOM   287  N  N   . ILE A 1 36  ? 11.568  -10.693 -4.198  1.00 25.75 ? 36  ILE A N   1 
ATOM   288  C  CA  . ILE A 1 36  ? 12.524  -9.666  -4.652  1.00 22.42 ? 36  ILE A CA  1 
ATOM   289  C  C   . ILE A 1 36  ? 13.957  -10.202 -4.587  1.00 21.40 ? 36  ILE A C   1 
ATOM   290  O  O   . ILE A 1 36  ? 14.899  -9.461  -4.869  1.00 23.86 ? 36  ILE A O   1 
ATOM   291  C  CB  . ILE A 1 36  ? 12.406  -8.316  -3.849  1.00 21.19 ? 36  ILE A CB  1 
ATOM   292  C  CG1 . ILE A 1 36  ? 12.692  -8.586  -2.356  1.00 23.63 ? 36  ILE A CG1 1 
ATOM   293  C  CG2 . ILE A 1 36  ? 11.098  -7.565  -4.109  1.00 23.48 ? 36  ILE A CG2 1 
ATOM   294  C  CD1 . ILE A 1 36  ? 12.919  -7.382  -1.494  1.00 25.15 ? 36  ILE A CD1 1 
ATOM   295  N  N   . LEU A 1 37  ? 14.125  -11.459 -4.255  1.00 21.21 ? 37  LEU A N   1 
ATOM   296  C  CA  . LEU A 1 37  ? 15.479  -12.054 -4.229  1.00 21.63 ? 37  LEU A CA  1 
ATOM   297  C  C   . LEU A 1 37  ? 15.937  -12.492 -5.617  1.00 25.20 ? 37  LEU A C   1 
ATOM   298  O  O   . LEU A 1 37  ? 15.187  -13.127 -6.381  1.00 24.98 ? 37  LEU A O   1 
ATOM   299  C  CB  . LEU A 1 37  ? 15.562  -13.185 -3.204  1.00 20.99 ? 37  LEU A CB  1 
ATOM   300  C  CG  . LEU A 1 37  ? 15.162  -12.707 -1.828  1.00 21.18 ? 37  LEU A CG  1 
ATOM   301  C  CD1 . LEU A 1 37  ? 15.282  -13.898 -0.873  1.00 24.85 ? 37  LEU A CD1 1 
ATOM   302  C  CD2 . LEU A 1 37  ? 15.993  -11.556 -1.271  1.00 17.00 ? 37  LEU A CD2 1 
ATOM   303  N  N   . GLN A 1 38  ? 17.167  -12.155 -5.956  1.00 21.52 ? 38  GLN A N   1 
ATOM   304  C  CA  . GLN A 1 38  ? 17.743  -12.695 -7.176  1.00 21.31 ? 38  GLN A CA  1 
ATOM   305  C  C   . GLN A 1 38  ? 19.196  -13.144 -6.991  1.00 21.39 ? 38  GLN A C   1 
ATOM   306  O  O   . GLN A 1 38  ? 20.026  -12.360 -6.584  1.00 17.43 ? 38  GLN A O   1 
ATOM   307  C  CB  . GLN A 1 38  ? 17.572  -11.704 -8.352  1.00 22.06 ? 38  GLN A CB  1 
ATOM   308  C  CG  . GLN A 1 38  ? 18.346  -12.121 -9.581  1.00 25.49 ? 38  GLN A CG  1 
ATOM   309  C  CD  . GLN A 1 38  ? 18.051  -11.305 -10.817 1.00 28.30 ? 38  GLN A CD  1 
ATOM   310  O  OE1 . GLN A 1 38  ? 16.895  -11.254 -11.295 1.00 32.92 ? 38  GLN A OE1 1 
ATOM   311  N  NE2 . GLN A 1 38  ? 19.103  -10.685 -11.370 1.00 29.37 ? 38  GLN A NE2 1 
ATOM   312  N  N   . TYR A 1 39  ? 19.496  -14.409 -7.300  1.00 19.24 ? 39  TYR A N   1 
ATOM   313  C  CA  . TYR A 1 39  ? 20.819  -14.928 -7.191  1.00 18.87 ? 39  TYR A CA  1 
ATOM   314  C  C   . TYR A 1 39  ? 21.741  -14.198 -8.149  1.00 20.52 ? 39  TYR A C   1 
ATOM   315  O  O   . TYR A 1 39  ? 21.391  -13.970 -9.335  1.00 21.67 ? 39  TYR A O   1 
ATOM   316  C  CB  . TYR A 1 39  ? 20.764  -16.413 -7.579  1.00 20.03 ? 39  TYR A CB  1 
ATOM   317  C  CG  . TYR A 1 39  ? 22.138  -17.058 -7.677  1.00 23.19 ? 39  TYR A CG  1 
ATOM   318  C  CD1 . TYR A 1 39  ? 22.974  -17.094 -6.585  1.00 20.13 ? 39  TYR A CD1 1 
ATOM   319  C  CD2 . TYR A 1 39  ? 22.598  -17.619 -8.884  1.00 25.86 ? 39  TYR A CD2 1 
ATOM   320  C  CE1 . TYR A 1 39  ? 24.246  -17.635 -6.654  1.00 24.54 ? 39  TYR A CE1 1 
ATOM   321  C  CE2 . TYR A 1 39  ? 23.872  -18.199 -8.976  1.00 27.21 ? 39  TYR A CE2 1 
ATOM   322  C  CZ  . TYR A 1 39  ? 24.690  -18.227 -7.849  1.00 27.61 ? 39  TYR A CZ  1 
ATOM   323  O  OH  . TYR A 1 39  ? 25.936  -18.795 -7.953  1.00 30.53 ? 39  TYR A OH  1 
ATOM   324  N  N   . ASP A 1 40  ? 22.918  -13.844 -7.679  1.00 17.51 ? 40  ASP A N   1 
ATOM   325  C  CA  . ASP A 1 40  ? 23.879  -13.261 -8.530  1.00 20.24 ? 40  ASP A CA  1 
ATOM   326  C  C   . ASP A 1 40  ? 25.198  -13.929 -8.248  1.00 21.56 ? 40  ASP A C   1 
ATOM   327  O  O   . ASP A 1 40  ? 25.774  -13.793 -7.179  1.00 17.80 ? 40  ASP A O   1 
ATOM   328  C  CB  . ASP A 1 40  ? 23.898  -11.748 -8.240  1.00 25.37 ? 40  ASP A CB  1 
ATOM   329  C  CG  . ASP A 1 40  ? 24.916  -10.953 -9.125  1.00 29.84 ? 40  ASP A CG  1 
ATOM   330  O  OD1 . ASP A 1 40  ? 25.943  -11.498 -9.640  1.00 25.53 ? 40  ASP A OD1 1 
ATOM   331  O  OD2 . ASP A 1 40  ? 24.655  -9.728  -9.242  1.00 36.03 ? 40  ASP A OD2 1 
ATOM   332  N  N   . ALA A 1 41  ? 25.688  -14.683 -9.251  1.00 25.35 ? 41  ALA A N   1 
ATOM   333  C  CA  . ALA A 1 41  ? 27.022  -15.346 -9.222  1.00 28.23 ? 41  ALA A CA  1 
ATOM   334  C  C   . ALA A 1 41  ? 28.216  -14.457 -9.032  1.00 25.18 ? 41  ALA A C   1 
ATOM   335  O  O   . ALA A 1 41  ? 29.288  -14.941 -8.665  1.00 27.33 ? 41  ALA A O   1 
ATOM   336  C  CB  . ALA A 1 41  ? 27.238  -16.144 -10.513 1.00 25.41 ? 41  ALA A CB  1 
ATOM   337  N  N   . SER A 1 42  ? 28.073  -13.164 -9.248  1.00 26.56 ? 42  SER A N   1 
ATOM   338  C  CA  . SER A 1 42  ? 29.177  -12.253 -9.018  1.00 26.27 ? 42  SER A CA  1 
ATOM   339  C  C   . SER A 1 42  ? 29.468  -12.023 -7.544  1.00 26.41 ? 42  SER A C   1 
ATOM   340  O  O   . SER A 1 42  ? 30.497  -11.434 -7.173  1.00 26.27 ? 42  SER A O   1 
ATOM   341  C  CB  . SER A 1 42  ? 28.881  -10.910 -9.722  1.00 29.42 ? 42  SER A CB  1 
ATOM   342  O  OG  . SER A 1 42  ? 28.363  -9.895  -8.862  1.00 36.81 ? 42  SER A OG  1 
ATOM   343  N  N   . LEU A 1 43  ? 28.544  -12.467 -6.681  1.00 18.67 ? 43  LEU A N   1 
ATOM   344  C  CA  . LEU A 1 43  ? 28.692  -12.203 -5.255  1.00 18.02 ? 43  LEU A CA  1 
ATOM   345  C  C   . LEU A 1 43  ? 29.563  -13.195 -4.550  1.00 18.60 ? 43  LEU A C   1 
ATOM   346  O  O   . LEU A 1 43  ? 29.085  -14.154 -3.862  1.00 19.67 ? 43  LEU A O   1 
ATOM   347  C  CB  . LEU A 1 43  ? 27.313  -12.062 -4.609  1.00 13.93 ? 43  LEU A CB  1 
ATOM   348  C  CG  . LEU A 1 43  ? 26.492  -10.914 -5.200  1.00 15.44 ? 43  LEU A CG  1 
ATOM   349  C  CD1 . LEU A 1 43  ? 25.116  -10.869 -4.527  1.00 13.47 ? 43  LEU A CD1 1 
ATOM   350  C  CD2 . LEU A 1 43  ? 27.130  -9.541  -5.018  1.00 15.27 ? 43  LEU A CD2 1 
ATOM   351  N  N   . THR A 1 44  ? 30.863  -12.983 -4.680  1.00 17.91 ? 44  THR A N   1 
ATOM   352  C  CA  . THR A 1 44  ? 31.815  -13.883 -4.096  1.00 18.13 ? 44  THR A CA  1 
ATOM   353  C  C   . THR A 1 44  ? 32.063  -13.571 -2.601  1.00 18.04 ? 44  THR A C   1 
ATOM   354  O  O   . THR A 1 44  ? 31.580  -12.504 -2.073  1.00 16.01 ? 44  THR A O   1 
ATOM   355  C  CB  . THR A 1 44  ? 33.189  -13.736 -4.809  1.00 20.03 ? 44  THR A CB  1 
ATOM   356  O  OG1 . THR A 1 44  ? 33.431  -12.343 -4.994  1.00 20.41 ? 44  THR A OG1 1 
ATOM   357  C  CG2 . THR A 1 44  ? 33.170  -14.444 -6.124  1.00 25.41 ? 44  THR A CG2 1 
ATOM   358  N  N   . PRO A 1 45  ? 32.806  -14.415 -1.870  1.00 17.39 ? 45  PRO A N   1 
ATOM   359  C  CA  . PRO A 1 45  ? 32.978  -14.166 -0.445  1.00 17.49 ? 45  PRO A CA  1 
ATOM   360  C  C   . PRO A 1 45  ? 33.838  -12.984 -0.154  1.00 19.21 ? 45  PRO A C   1 
ATOM   361  O  O   . PRO A 1 45  ? 34.867  -12.789 -0.826  1.00 19.33 ? 45  PRO A O   1 
ATOM   362  C  CB  . PRO A 1 45  ? 33.672  -15.411 0.070   1.00 19.18 ? 45  PRO A CB  1 
ATOM   363  C  CG  . PRO A 1 45  ? 33.368  -16.474 -0.912  1.00 18.28 ? 45  PRO A CG  1 
ATOM   364  C  CD  . PRO A 1 45  ? 33.325  -15.753 -2.246  1.00 19.20 ? 45  PRO A CD  1 
ATOM   365  N  N   . LEU A 1 46  ? 33.432  -12.215 0.846   1.00 15.96 ? 46  LEU A N   1 
ATOM   366  C  CA  . LEU A 1 46  ? 34.277  -11.063 1.281   1.00 15.20 ? 46  LEU A CA  1 
ATOM   367  C  C   . LEU A 1 46  ? 35.380  -11.651 2.161   1.00 16.75 ? 46  LEU A C   1 
ATOM   368  O  O   . LEU A 1 46  ? 35.188  -12.740 2.756   1.00 17.86 ? 46  LEU A O   1 
ATOM   369  C  CB  . LEU A 1 46  ? 33.494  -10.067 2.151   1.00 15.11 ? 46  LEU A CB  1 
ATOM   370  C  CG  . LEU A 1 46  ? 32.330  -9.474  1.382   1.00 15.35 ? 46  LEU A CG  1 
ATOM   371  C  CD1 . LEU A 1 46  ? 31.649  -8.623  2.415   1.00 16.16 ? 46  LEU A CD1 1 
ATOM   372  C  CD2 . LEU A 1 46  ? 32.907  -8.602  0.234   1.00 20.37 ? 46  LEU A CD2 1 
ATOM   373  N  N   . GLU A 1 47  ? 36.503  -10.935 2.250   1.00 17.15 ? 47  GLU A N   1 
ATOM   374  C  CA  . GLU A 1 47  ? 37.599  -11.299 3.102   1.00 19.61 ? 47  GLU A CA  1 
ATOM   375  C  C   . GLU A 1 47  ? 37.710  -10.206 4.143   1.00 17.35 ? 47  GLU A C   1 
ATOM   376  O  O   . GLU A 1 47  ? 37.722  -9.004  3.839   1.00 18.83 ? 47  GLU A O   1 
ATOM   377  C  CB  . GLU A 1 47  ? 38.911  -11.350 2.309   1.00 26.21 ? 47  GLU A CB  1 
ATOM   378  C  CG  . GLU A 1 47  ? 39.051  -12.638 1.499   1.00 35.86 ? 47  GLU A CG  1 
ATOM   379  C  CD  . GLU A 1 47  ? 40.215  -12.593 0.509   1.00 47.77 ? 47  GLU A CD  1 
ATOM   380  O  OE1 . GLU A 1 47  ? 39.974  -12.839 -0.702  1.00 51.86 ? 47  GLU A OE1 1 
ATOM   381  O  OE2 . GLU A 1 47  ? 41.356  -12.275 0.932   1.00 50.77 ? 47  GLU A OE2 1 
ATOM   382  N  N   . PHE A 1 48  ? 37.807  -10.611 5.401   1.00 17.46 ? 48  PHE A N   1 
ATOM   383  C  CA  . PHE A 1 48  ? 37.828  -9.685  6.494   1.00 16.68 ? 48  PHE A CA  1 
ATOM   384  C  C   . PHE A 1 48  ? 39.258  -9.592  6.987   1.00 19.20 ? 48  PHE A C   1 
ATOM   385  O  O   . PHE A 1 48  ? 39.785  -10.554 7.577   1.00 21.01 ? 48  PHE A O   1 
ATOM   386  C  CB  . PHE A 1 48  ? 36.868  -10.101 7.578   1.00 17.41 ? 48  PHE A CB  1 
ATOM   387  C  CG  . PHE A 1 48  ? 35.532  -10.466 7.039   1.00 17.01 ? 48  PHE A CG  1 
ATOM   388  C  CD1 . PHE A 1 48  ? 34.650  -9.526  6.687   1.00 17.18 ? 48  PHE A CD1 1 
ATOM   389  C  CD2 . PHE A 1 48  ? 35.150  -11.801 6.881   1.00 17.24 ? 48  PHE A CD2 1 
ATOM   390  C  CE1 . PHE A 1 48  ? 33.405  -9.873  6.154   1.00 17.95 ? 48  PHE A CE1 1 
ATOM   391  C  CE2 . PHE A 1 48  ? 33.942  -12.160 6.310   1.00 18.64 ? 48  PHE A CE2 1 
ATOM   392  C  CZ  . PHE A 1 48  ? 33.042  -11.179 5.928   1.00 17.53 ? 48  PHE A CZ  1 
ATOM   393  N  N   . GLN A 1 49  ? 39.870  -8.447  6.717   1.00 15.64 ? 49  GLN A N   1 
ATOM   394  C  CA  . GLN A 1 49  ? 41.346  -8.275  6.897   1.00 15.82 ? 49  GLN A CA  1 
ATOM   395  C  C   . GLN A 1 49  ? 41.571  -7.344  8.091   1.00 15.31 ? 49  GLN A C   1 
ATOM   396  O  O   . GLN A 1 49  ? 40.903  -6.325  8.254   1.00 15.18 ? 49  GLN A O   1 
ATOM   397  C  CB  . GLN A 1 49  ? 41.981  -7.672  5.637   1.00 17.12 ? 49  GLN A CB  1 
ATOM   398  C  CG  . GLN A 1 49  ? 41.836  -8.620  4.450   1.00 23.43 ? 49  GLN A CG  1 
ATOM   399  C  CD  . GLN A 1 49  ? 42.873  -8.435  3.325   1.00 32.87 ? 49  GLN A CD  1 
ATOM   400  O  OE1 . GLN A 1 49  ? 43.336  -7.296  3.007   1.00 37.39 ? 49  GLN A OE1 1 
ATOM   401  N  NE2 . GLN A 1 49  ? 43.207  -9.567  2.665   1.00 35.85 ? 49  GLN A NE2 1 
ATOM   402  N  N   . GLY A 1 50  ? 42.506  -7.698  8.988   1.00 15.79 ? 50  GLY A N   1 
ATOM   403  C  CA  . GLY A 1 50  ? 42.775  -6.836  10.078  1.00 16.27 ? 50  GLY A CA  1 
ATOM   404  C  C   . GLY A 1 50  ? 41.698  -6.854  11.174  1.00 17.26 ? 50  GLY A C   1 
ATOM   405  O  O   . GLY A 1 50  ? 41.635  -5.941  12.006  1.00 16.22 ? 50  GLY A O   1 
ATOM   406  N  N   . TYR A 1 51  ? 40.825  -7.843  11.107  1.00 15.87 ? 51  TYR A N   1 
ATOM   407  C  CA  . TYR A 1 51  ? 39.718  -7.978  12.105  1.00 15.73 ? 51  TYR A CA  1 
ATOM   408  C  C   . TYR A 1 51  ? 40.194  -8.508  13.442  1.00 17.14 ? 51  TYR A C   1 
ATOM   409  O  O   . TYR A 1 51  ? 39.527  -8.402  14.486  1.00 15.21 ? 51  TYR A O   1 
ATOM   410  C  CB  . TYR A 1 51  ? 38.562  -8.887  11.566  1.00 14.15 ? 51  TYR A CB  1 
ATOM   411  C  CG  . TYR A 1 51  ? 37.518  -8.159  10.730  1.00 14.78 ? 51  TYR A CG  1 
ATOM   412  C  CD1 . TYR A 1 51  ? 36.151  -8.370  10.994  1.00 12.73 ? 51  TYR A CD1 1 
ATOM   413  C  CD2 . TYR A 1 51  ? 37.862  -7.257  9.728   1.00 13.09 ? 51  TYR A CD2 1 
ATOM   414  C  CE1 . TYR A 1 51  ? 35.205  -7.691  10.225  1.00 11.07 ? 51  TYR A CE1 1 
ATOM   415  C  CE2 . TYR A 1 51  ? 36.908  -6.640  8.933   1.00 14.20 ? 51  TYR A CE2 1 
ATOM   416  C  CZ  . TYR A 1 51  ? 35.602  -6.864  9.213   1.00 13.37 ? 51  TYR A CZ  1 
ATOM   417  O  OH  . TYR A 1 51  ? 34.574  -6.205  8.508   1.00 14.29 ? 51  TYR A OH  1 
ATOM   418  N  N   . ASN A 1 52  ? 41.353  -9.175  13.421  1.00 16.31 ? 52  ASN A N   1 
ATOM   419  C  CA  . ASN A 1 52  ? 41.859  -9.742  14.669  1.00 19.58 ? 52  ASN A CA  1 
ATOM   420  C  C   . ASN A 1 52  ? 42.605  -8.664  15.410  1.00 21.60 ? 52  ASN A C   1 
ATOM   421  O  O   . ASN A 1 52  ? 43.837  -8.549  15.283  1.00 23.36 ? 52  ASN A O   1 
ATOM   422  C  CB  . ASN A 1 52  ? 42.774  -10.958 14.403  1.00 19.12 ? 52  ASN A CB  1 
ATOM   423  C  CG  . ASN A 1 52  ? 43.007  -11.781 15.650  1.00 20.99 ? 52  ASN A CG  1 
ATOM   424  O  OD1 . ASN A 1 52  ? 42.460  -11.537 16.727  1.00 20.41 ? 52  ASN A OD1 1 
ATOM   425  N  ND2 . ASN A 1 52  ? 43.942  -12.759 15.530  1.00 25.18 ? 52  ASN A ND2 1 
ATOM   426  N  N   . LEU A 1 53  ? 41.886  -7.833  16.145  1.00 19.31 ? 53  LEU A N   1 
ATOM   427  C  CA  . LEU A 1 53  ? 42.472  -6.637  16.766  1.00 21.18 ? 53  LEU A CA  1 
ATOM   428  C  C   . LEU A 1 53  ? 43.457  -6.969  17.881  1.00 24.93 ? 53  LEU A C   1 
ATOM   429  O  O   . LEU A 1 53  ? 43.181  -7.792  18.754  1.00 22.70 ? 53  LEU A O   1 
ATOM   430  C  CB  . LEU A 1 53  ? 41.392  -5.709  17.347  1.00 19.24 ? 53  LEU A CB  1 
ATOM   431  C  CG  . LEU A 1 53  ? 40.407  -5.210  16.266  1.00 17.85 ? 53  LEU A CG  1 
ATOM   432  C  CD1 . LEU A 1 53  ? 39.339  -4.376  16.985  1.00 16.08 ? 53  LEU A CD1 1 
ATOM   433  C  CD2 . LEU A 1 53  ? 41.075  -4.531  15.054  1.00 18.09 ? 53  LEU A CD2 1 
ATOM   434  N  N   . SER A 1 54  ? 44.588  -6.272  17.828  1.00 25.28 ? 54  SER A N   1 
ATOM   435  C  CA  . SER A 1 54  ? 45.616  -6.458  18.827  1.00 27.33 ? 54  SER A CA  1 
ATOM   436  C  C   . SER A 1 54  ? 44.992  -6.365  20.224  1.00 26.42 ? 54  SER A C   1 
ATOM   437  O  O   . SER A 1 54  ? 44.407  -5.328  20.590  1.00 26.30 ? 54  SER A O   1 
ATOM   438  C  CB  . SER A 1 54  ? 46.661  -5.343  18.659  1.00 29.25 ? 54  SER A CB  1 
ATOM   439  O  OG  . SER A 1 54  ? 47.608  -5.527  19.684  1.00 32.56 ? 54  SER A OG  1 
ATOM   440  N  N   . ALA A 1 55  ? 45.113  -7.426  21.003  1.00 26.26 ? 55  ALA A N   1 
ATOM   441  C  CA  . ALA A 1 55  ? 44.696  -7.354  22.416  1.00 25.23 ? 55  ALA A CA  1 
ATOM   442  C  C   . ALA A 1 55  ? 45.572  -6.395  23.304  1.00 28.48 ? 55  ALA A C   1 
ATOM   443  O  O   . ALA A 1 55  ? 45.215  -6.073  24.444  1.00 33.49 ? 55  ALA A O   1 
ATOM   444  C  CB  . ALA A 1 55  ? 44.607  -8.744  23.012  1.00 27.90 ? 55  ALA A CB  1 
ATOM   445  N  N   . ASN A 1 56  ? 46.668  -5.900  22.719  1.00 33.51 ? 56  ASN A N   1 
ATOM   446  C  CA  . ASN A 1 56  ? 47.463  -4.779  23.288  1.00 33.76 ? 56  ASN A CA  1 
ATOM   447  C  C   . ASN A 1 56  ? 46.986  -3.357  22.957  1.00 36.74 ? 56  ASN A C   1 
ATOM   448  O  O   . ASN A 1 56  ? 47.656  -2.382  23.323  1.00 37.41 ? 56  ASN A O   1 
ATOM   449  C  CB  . ASN A 1 56  ? 48.930  -4.897  22.835  1.00 38.89 ? 56  ASN A CB  1 
ATOM   450  C  CG  . ASN A 1 56  ? 49.523  -6.257  23.127  1.00 39.34 ? 56  ASN A CG  1 
ATOM   451  O  OD1 . ASN A 1 56  ? 49.295  -6.839  24.200  1.00 44.65 ? 56  ASN A OD1 1 
ATOM   452  N  ND2 . ASN A 1 56  ? 50.290  -6.774  22.179  1.00 33.84 ? 56  ASN A ND2 1 
ATOM   453  N  N   . LYS A 1 57  ? 45.869  -3.236  22.231  1.00 31.26 ? 57  LYS A N   1 
ATOM   454  C  CA  . LYS A 1 57  ? 45.324  -1.948  21.855  1.00 27.96 ? 57  LYS A CA  1 
ATOM   455  C  C   . LYS A 1 57  ? 43.970  -1.939  22.525  1.00 26.57 ? 57  LYS A C   1 
ATOM   456  O  O   . LYS A 1 57  ? 43.414  -3.012  22.814  1.00 25.03 ? 57  LYS A O   1 
ATOM   457  C  CB  . LYS A 1 57  ? 45.187  -1.838  20.342  1.00 34.38 ? 57  LYS A CB  1 
ATOM   458  C  CG  . LYS A 1 57  ? 46.437  -1.406  19.608  1.00 39.96 ? 57  LYS A CG  1 
ATOM   459  C  CD  . LYS A 1 57  ? 46.223  -1.483  18.104  1.00 41.40 ? 57  LYS A CD  1 
ATOM   460  C  CE  . LYS A 1 57  ? 45.097  -0.563  17.604  1.00 44.98 ? 57  LYS A CE  1 
ATOM   461  N  NZ  . LYS A 1 57  ? 45.511  0.816   17.200  1.00 48.25 ? 57  LYS A NZ  1 
ATOM   462  N  N   . GLN A 1 58  ? 43.503  -0.742  22.849  1.00 25.00 ? 58  GLN A N   1 
ATOM   463  C  CA  . GLN A 1 58  ? 42.144  -0.551  23.349  1.00 25.39 ? 58  GLN A CA  1 
ATOM   464  C  C   . GLN A 1 58  ? 41.330  0.304   22.451  1.00 23.93 ? 58  GLN A C   1 
ATOM   465  O  O   . GLN A 1 58  ? 41.824  1.241   21.829  1.00 22.33 ? 58  GLN A O   1 
ATOM   466  C  CB  . GLN A 1 58  ? 42.220  0.066   24.704  1.00 24.35 ? 58  GLN A CB  1 
ATOM   467  C  CG  . GLN A 1 58  ? 42.946  -0.909  25.597  1.00 29.04 ? 58  GLN A CG  1 
ATOM   468  C  CD  . GLN A 1 58  ? 42.974  -0.395  27.005  1.00 32.09 ? 58  GLN A CD  1 
ATOM   469  O  OE1 . GLN A 1 58  ? 42.914  -1.158  27.960  1.00 41.39 ? 58  GLN A OE1 1 
ATOM   470  N  NE2 . GLN A 1 58  ? 43.018  0.933   27.137  1.00 31.19 ? 58  GLN A NE2 1 
ATOM   471  N  N   . PHE A 1 59  ? 40.031  -0.006  22.435  1.00 22.03 ? 59  PHE A N   1 
ATOM   472  C  CA  . PHE A 1 59  ? 39.090  0.568   21.510  1.00 19.39 ? 59  PHE A CA  1 
ATOM   473  C  C   . PHE A 1 59  ? 37.938  1.213   22.266  1.00 17.58 ? 59  PHE A C   1 
ATOM   474  O  O   . PHE A 1 59  ? 37.383  0.657   23.182  1.00 17.73 ? 59  PHE A O   1 
ATOM   475  C  CB  . PHE A 1 59  ? 38.632  -0.517  20.524  1.00 20.95 ? 59  PHE A CB  1 
ATOM   476  C  CG  . PHE A 1 59  ? 39.797  -1.129  19.796  1.00 20.45 ? 59  PHE A CG  1 
ATOM   477  C  CD1 . PHE A 1 59  ? 40.310  -0.499  18.662  1.00 20.89 ? 59  PHE A CD1 1 
ATOM   478  C  CD2 . PHE A 1 59  ? 40.463  -2.251  20.326  1.00 22.66 ? 59  PHE A CD2 1 
ATOM   479  C  CE1 . PHE A 1 59  ? 41.448  -1.016  18.034  1.00 21.40 ? 59  PHE A CE1 1 
ATOM   480  C  CE2 . PHE A 1 59  ? 41.606  -2.756  19.688  1.00 20.49 ? 59  PHE A CE2 1 
ATOM   481  C  CZ  . PHE A 1 59  ? 42.077  -2.128  18.550  1.00 22.97 ? 59  PHE A CZ  1 
ATOM   482  N  N   . LEU A 1 60  ? 37.636  2.427   21.879  1.00 18.41 ? 60  LEU A N   1 
ATOM   483  C  CA  . LEU A 1 60  ? 36.677  3.159   22.675  1.00 18.27 ? 60  LEU A CA  1 
ATOM   484  C  C   . LEU A 1 60  ? 35.206  2.765   22.419  1.00 18.54 ? 60  LEU A C   1 
ATOM   485  O  O   . LEU A 1 60  ? 34.737  2.852   21.267  1.00 17.19 ? 60  LEU A O   1 
ATOM   486  C  CB  . LEU A 1 60  ? 36.823  4.596   22.334  1.00 19.44 ? 60  LEU A CB  1 
ATOM   487  C  CG  . LEU A 1 60  ? 35.995  5.587   23.110  1.00 22.24 ? 60  LEU A CG  1 
ATOM   488  C  CD1 . LEU A 1 60  ? 36.507  5.566   24.561  1.00 23.64 ? 60  LEU A CD1 1 
ATOM   489  C  CD2 . LEU A 1 60  ? 36.087  6.977   22.478  1.00 25.58 ? 60  LEU A CD2 1 
ATOM   490  N  N   . LEU A 1 61  ? 34.501  2.438   23.486  1.00 16.85 ? 61  LEU A N   1 
ATOM   491  C  CA  . LEU A 1 61  ? 33.071  2.161   23.497  1.00 17.61 ? 61  LEU A CA  1 
ATOM   492  C  C   . LEU A 1 61  ? 32.322  3.401   23.981  1.00 18.17 ? 61  LEU A C   1 
ATOM   493  O  O   . LEU A 1 61  ? 32.655  3.924   25.056  1.00 18.80 ? 61  LEU A O   1 
ATOM   494  C  CB  . LEU A 1 61  ? 32.809  1.005   24.428  1.00 20.02 ? 61  LEU A CB  1 
ATOM   495  C  CG  . LEU A 1 61  ? 31.415  0.341   24.271  1.00 19.74 ? 61  LEU A CG  1 
ATOM   496  C  CD1 . LEU A 1 61  ? 31.340  -0.477  22.953  1.00 22.62 ? 61  LEU A CD1 1 
ATOM   497  C  CD2 . LEU A 1 61  ? 30.969  -0.559  25.412  1.00 20.78 ? 61  LEU A CD2 1 
ATOM   498  N  N   . THR A 1 62  ? 31.332  3.880   23.226  1.00 17.29 ? 62  THR A N   1 
ATOM   499  C  CA  . THR A 1 62  ? 30.600  5.093   23.603  1.00 17.47 ? 62  THR A CA  1 
ATOM   500  C  C   . THR A 1 62  ? 29.094  4.850   23.638  1.00 18.77 ? 62  THR A C   1 
ATOM   501  O  O   . THR A 1 62  ? 28.531  4.196   22.756  1.00 16.69 ? 62  THR A O   1 
ATOM   502  C  CB  . THR A 1 62  ? 30.908  6.262   22.661  1.00 20.98 ? 62  THR A CB  1 
ATOM   503  O  OG1 . THR A 1 62  ? 32.314  6.537   22.641  1.00 25.04 ? 62  THR A OG1 1 
ATOM   504  C  CG2 . THR A 1 62  ? 30.108  7.553   23.046  1.00 21.97 ? 62  THR A CG2 1 
ATOM   505  N  N   . ASN A 1 63  ? 28.410  5.423   24.610  1.00 17.23 ? 63  ASN A N   1 
ATOM   506  C  CA  . ASN A 1 63  ? 26.935  5.560   24.496  1.00 17.15 ? 63  ASN A CA  1 
ATOM   507  C  C   . ASN A 1 63  ? 26.684  6.950   23.920  1.00 19.47 ? 63  ASN A C   1 
ATOM   508  O  O   . ASN A 1 63  ? 27.054  7.992   24.516  1.00 19.18 ? 63  ASN A O   1 
ATOM   509  C  CB  . ASN A 1 63  ? 26.325  5.464   25.879  1.00 16.04 ? 63  ASN A CB  1 
ATOM   510  C  CG  . ASN A 1 63  ? 24.815  5.771   25.898  1.00 15.93 ? 63  ASN A CG  1 
ATOM   511  O  OD1 . ASN A 1 63  ? 24.250  6.533   25.047  1.00 16.23 ? 63  ASN A OD1 1 
ATOM   512  N  ND2 . ASN A 1 63  ? 24.150  5.233   26.939  1.00 13.78 ? 63  ASN A ND2 1 
ATOM   513  N  N   . ASN A 1 64  ? 26.077  7.024   22.725  1.00 17.43 ? 64  ASN A N   1 
ATOM   514  C  CA  . ASN A 1 64  ? 25.935  8.304   22.062  1.00 16.27 ? 64  ASN A CA  1 
ATOM   515  C  C   . ASN A 1 64  ? 24.484  8.792   22.095  1.00 16.04 ? 64  ASN A C   1 
ATOM   516  O  O   . ASN A 1 64  ? 24.094  9.775   21.434  1.00 18.71 ? 64  ASN A O   1 
ATOM   517  C  CB  . ASN A 1 64  ? 26.451  8.189   20.618  1.00 18.29 ? 64  ASN A CB  1 
ATOM   518  C  CG  . ASN A 1 64  ? 25.629  7.242   19.770  1.00 18.46 ? 64  ASN A CG  1 
ATOM   519  O  OD1 . ASN A 1 64  ? 24.544  6.801   20.129  1.00 17.86 ? 64  ASN A OD1 1 
ATOM   520  N  ND2 . ASN A 1 64  ? 26.180  6.934   18.571  1.00 20.57 ? 64  ASN A ND2 1 
ATOM   521  N  N   . GLY A 1 65  ? 23.683  8.116   22.901  1.00 17.79 ? 65  GLY A N   1 
ATOM   522  C  CA  . GLY A 1 65  ? 22.307  8.506   23.139  1.00 17.81 ? 65  GLY A CA  1 
ATOM   523  C  C   . GLY A 1 65  ? 21.369  7.852   22.132  1.00 19.61 ? 65  GLY A C   1 
ATOM   524  O  O   . GLY A 1 65  ? 20.166  7.826   22.326  1.00 21.69 ? 65  GLY A O   1 
ATOM   525  N  N   . HIS A 1 66  ? 21.950  7.285   21.067  1.00 15.40 ? 66  HIS A N   1 
ATOM   526  C  CA  . HIS A 1 66  ? 21.172  6.505   20.059  1.00 15.58 ? 66  HIS A CA  1 
ATOM   527  C  C   . HIS A 1 66  ? 21.430  5.040   20.070  1.00 16.30 ? 66  HIS A C   1 
ATOM   528  O  O   . HIS A 1 66  ? 20.515  4.273   19.823  1.00 18.12 ? 66  HIS A O   1 
ATOM   529  C  CB  . HIS A 1 66  ? 21.341  7.056   18.638  1.00 15.86 ? 66  HIS A CB  1 
ATOM   530  C  CG  . HIS A 1 66  ? 21.087  8.564   18.486  1.00 16.87 ? 66  HIS A CG  1 
ATOM   531  N  ND1 . HIS A 1 66  ? 19.821  9.156   18.547  1.00 18.37 ? 66  HIS A ND1 1 
ATOM   532  C  CD2 . HIS A 1 66  ? 21.976  9.581   18.241  1.00 18.01 ? 66  HIS A CD2 1 
ATOM   533  C  CE1 . HIS A 1 66  ? 19.938  10.483  18.386  1.00 18.54 ? 66  HIS A CE1 1 
ATOM   534  N  NE2 . HIS A 1 66  ? 21.252  10.761  18.161  1.00 21.62 ? 66  HIS A NE2 1 
ATOM   535  N  N   . SER A 1 67  ? 22.679  4.642   20.336  1.00 16.56 ? 67  SER A N   1 
ATOM   536  C  CA  . SER A 1 67  ? 23.048  3.229   20.404  1.00 16.44 ? 67  SER A CA  1 
ATOM   537  C  C   . SER A 1 67  ? 24.335  3.185   21.244  1.00 18.19 ? 67  SER A C   1 
ATOM   538  O  O   . SER A 1 67  ? 24.732  4.197   21.850  1.00 17.31 ? 67  SER A O   1 
ATOM   539  C  CB  . SER A 1 67  ? 23.265  2.694   18.958  1.00 16.49 ? 67  SER A CB  1 
ATOM   540  O  OG  . SER A 1 67  ? 23.744  1.321   19.002  1.00 19.28 ? 67  SER A OG  1 
ATOM   541  N  N   . VAL A 1 68  ? 24.929  1.997   21.281  1.00 16.97 ? 68  VAL A N   1 
ATOM   542  C  CA  . VAL A 1 68  ? 26.276  1.854   21.822  1.00 16.62 ? 68  VAL A CA  1 
ATOM   543  C  C   . VAL A 1 68  ? 27.176  1.518   20.644  1.00 16.22 ? 68  VAL A C   1 
ATOM   544  O  O   . VAL A 1 68  ? 26.858  0.611   19.850  1.00 15.86 ? 68  VAL A O   1 
ATOM   545  C  CB  . VAL A 1 68  ? 26.363  0.792   22.951  1.00 19.72 ? 68  VAL A CB  1 
ATOM   546  C  CG1 . VAL A 1 68  ? 25.880  -0.592  22.500  1.00 21.16 ? 68  VAL A CG1 1 
ATOM   547  C  CG2 . VAL A 1 68  ? 27.795  0.665   23.428  1.00 21.78 ? 68  VAL A CG2 1 
ATOM   548  N  N   . LYS A 1 69  ? 28.285  2.226   20.542  1.00 15.35 ? 69  LYS A N   1 
ATOM   549  C  CA  . LYS A 1 69  ? 29.179  2.083   19.426  1.00 16.26 ? 69  LYS A CA  1 
ATOM   550  C  C   . LYS A 1 69  ? 30.584  1.841   19.876  1.00 16.81 ? 69  LYS A C   1 
ATOM   551  O  O   . LYS A 1 69  ? 30.981  2.365   20.922  1.00 16.87 ? 69  LYS A O   1 
ATOM   552  C  CB  . LYS A 1 69  ? 29.116  3.292   18.503  1.00 17.53 ? 69  LYS A CB  1 
ATOM   553  C  CG  . LYS A 1 69  ? 29.651  4.543   19.072  1.00 21.88 ? 69  LYS A CG  1 
ATOM   554  C  CD  . LYS A 1 69  ? 29.928  5.569   17.981  1.00 23.64 ? 69  LYS A CD  1 
ATOM   555  C  CE  . LYS A 1 69  ? 30.761  6.660   18.661  1.00 25.96 ? 69  LYS A CE  1 
ATOM   556  N  NZ  . LYS A 1 69  ? 30.478  8.046   18.163  1.00 31.75 ? 69  LYS A NZ  1 
ATOM   557  N  N   . LEU A 1 70  ? 31.265  0.944   19.144  1.00 13.82 ? 70  LEU A N   1 
ATOM   558  C  CA  . LEU A 1 70  ? 32.711  0.665   19.376  1.00 13.55 ? 70  LEU A CA  1 
ATOM   559  C  C   . LEU A 1 70  ? 33.515  1.280   18.230  1.00 12.86 ? 70  LEU A C   1 
ATOM   560  O  O   . LEU A 1 70  ? 33.257  0.939   17.092  1.00 12.63 ? 70  LEU A O   1 
ATOM   561  C  CB  . LEU A 1 70  ? 32.893  -0.838  19.477  1.00 13.32 ? 70  LEU A CB  1 
ATOM   562  C  CG  . LEU A 1 70  ? 34.336  -1.264  19.718  1.00 13.09 ? 70  LEU A CG  1 
ATOM   563  C  CD1 . LEU A 1 70  ? 34.930  -0.660  21.030  1.00 14.50 ? 70  LEU A CD1 1 
ATOM   564  C  CD2 . LEU A 1 70  ? 34.429  -2.790  19.686  1.00 14.59 ? 70  LEU A CD2 1 
ATOM   565  N  N   . ASN A 1 71  ? 34.537  2.106   18.514  1.00 11.94 ? 71  ASN A N   1 
ATOM   566  C  CA  . ASN A 1 71  ? 35.391  2.630   17.443  1.00 14.65 ? 71  ASN A CA  1 
ATOM   567  C  C   . ASN A 1 71  ? 36.277  1.554   16.944  1.00 17.51 ? 71  ASN A C   1 
ATOM   568  O  O   . ASN A 1 71  ? 36.694  0.700   17.753  1.00 17.51 ? 71  ASN A O   1 
ATOM   569  C  CB  . ASN A 1 71  ? 36.228  3.846   17.913  1.00 17.40 ? 71  ASN A CB  1 
ATOM   570  C  CG  . ASN A 1 71  ? 35.368  5.044   18.155  1.00 22.31 ? 71  ASN A CG  1 
ATOM   571  O  OD1 . ASN A 1 71  ? 34.147  5.012   17.887  1.00 30.06 ? 71  ASN A OD1 1 
ATOM   572  N  ND2 . ASN A 1 71  ? 35.986  6.161   18.675  1.00 29.78 ? 71  ASN A ND2 1 
ATOM   573  N  N   . LEU A 1 72  ? 36.512  1.522   15.616  1.00 14.96 ? 72  LEU A N   1 
ATOM   574  C  CA  . LEU A 1 72  ? 37.357  0.473   15.025  1.00 14.41 ? 72  LEU A CA  1 
ATOM   575  C  C   . LEU A 1 72  ? 38.459  1.159   14.269  1.00 16.89 ? 72  LEU A C   1 
ATOM   576  O  O   . LEU A 1 72  ? 38.286  2.327   13.802  1.00 16.63 ? 72  LEU A O   1 
ATOM   577  C  CB  . LEU A 1 72  ? 36.482  -0.470  14.064  1.00 13.49 ? 72  LEU A CB  1 
ATOM   578  C  CG  . LEU A 1 72  ? 35.388  -1.207  14.810  1.00 11.72 ? 72  LEU A CG  1 
ATOM   579  C  CD1 . LEU A 1 72  ? 34.487  -1.708  13.639  1.00 11.39 ? 72  LEU A CD1 1 
ATOM   580  C  CD2 . LEU A 1 72  ? 35.912  -2.365  15.689  1.00 12.85 ? 72  LEU A CD2 1 
ATOM   581  N  N   . PRO A 1 73  ? 39.607  0.464   14.090  1.00 16.93 ? 73  PRO A N   1 
ATOM   582  C  CA  . PRO A 1 73  ? 40.763  1.077   13.413  1.00 17.69 ? 73  PRO A CA  1 
ATOM   583  C  C   . PRO A 1 73  ? 40.668  1.001   11.895  1.00 19.38 ? 73  PRO A C   1 
ATOM   584  O  O   . PRO A 1 73  ? 40.162  0.004   11.347  1.00 20.88 ? 73  PRO A O   1 
ATOM   585  C  CB  . PRO A 1 73  ? 41.934  0.250   13.951  1.00 18.32 ? 73  PRO A CB  1 
ATOM   586  C  CG  . PRO A 1 73  ? 41.350  -1.129  14.122  1.00 16.48 ? 73  PRO A CG  1 
ATOM   587  C  CD  . PRO A 1 73  ? 39.942  -0.859  14.654  1.00 15.89 ? 73  PRO A CD  1 
ATOM   588  N  N   . SER A 1 74  ? 41.150  2.023   11.217  1.00 21.41 ? 74  SER A N   1 
ATOM   589  C  CA  . SER A 1 74  ? 41.094  2.003   9.744   1.00 22.79 ? 74  SER A CA  1 
ATOM   590  C  C   . SER A 1 74  ? 41.978  0.903   9.096   1.00 22.55 ? 74  SER A C   1 
ATOM   591  O  O   . SER A 1 74  ? 41.807  0.561   7.902   1.00 25.97 ? 74  SER A O   1 
ATOM   592  C  CB  . SER A 1 74  ? 41.386  3.384   9.147   1.00 23.17 ? 74  SER A CB  1 
ATOM   593  O  OG  . SER A 1 74  ? 42.718  3.797   9.527   1.00 25.28 ? 74  SER A OG  1 
ATOM   594  N  N   . ASP A 1 75  ? 42.901  0.306   9.847   1.00 21.76 ? 75  ASP A N   1 
ATOM   595  C  CA  . ASP A 1 75  ? 43.615  -0.831  9.229   1.00 20.85 ? 75  ASP A CA  1 
ATOM   596  C  C   . ASP A 1 75  ? 42.744  -2.073  9.085   1.00 20.37 ? 75  ASP A C   1 
ATOM   597  O  O   . ASP A 1 75  ? 43.087  -3.075  8.447   1.00 19.55 ? 75  ASP A O   1 
ATOM   598  C  CB  . ASP A 1 75  ? 44.961  -1.107  9.922   1.00 24.95 ? 75  ASP A CB  1 
ATOM   599  C  CG  . ASP A 1 75  ? 44.776  -1.653  11.261  1.00 27.21 ? 75  ASP A CG  1 
ATOM   600  O  OD1 . ASP A 1 75  ? 44.507  -0.851  12.178  1.00 30.68 ? 75  ASP A OD1 1 
ATOM   601  O  OD2 . ASP A 1 75  ? 44.958  -2.879  11.417  1.00 35.07 ? 75  ASP A OD2 1 
ATOM   602  N  N   . MET A 1 76  ? 41.582  -2.020  9.717   1.00 18.41 ? 76  MET A N   1 
ATOM   603  C  CA  . MET A 1 76  ? 40.601  -3.064  9.569   1.00 14.71 ? 76  MET A CA  1 
ATOM   604  C  C   . MET A 1 76  ? 39.795  -2.831  8.303   1.00 14.26 ? 76  MET A C   1 
ATOM   605  O  O   . MET A 1 76  ? 39.334  -1.698  8.117   1.00 14.32 ? 76  MET A O   1 
ATOM   606  C  CB  . MET A 1 76  ? 39.716  -2.994  10.760  1.00 18.09 ? 76  MET A CB  1 
ATOM   607  C  CG  . MET A 1 76  ? 38.686  -4.038  10.856  1.00 17.56 ? 76  MET A CG  1 
ATOM   608  S  SD  . MET A 1 76  ? 37.847  -3.995  12.475  1.00 18.10 ? 76  MET A SD  1 
ATOM   609  C  CE  . MET A 1 76  ? 36.303  -4.684  11.976  1.00 17.22 ? 76  MET A CE  1 
ATOM   610  N  N   . HIS A 1 77  ? 39.728  -3.815  7.417   1.00 13.64 ? 77  HIS A N   1 
ATOM   611  C  CA  . HIS A 1 77  ? 38.969  -3.600  6.151   1.00 14.37 ? 77  HIS A CA  1 
ATOM   612  C  C   . HIS A 1 77  ? 38.389  -4.785  5.491   1.00 14.53 ? 77  HIS A C   1 
ATOM   613  O  O   . HIS A 1 77  ? 38.687  -5.956  5.797   1.00 15.97 ? 77  HIS A O   1 
ATOM   614  C  CB  . HIS A 1 77  ? 39.817  -2.876  5.124   1.00 17.08 ? 77  HIS A CB  1 
ATOM   615  C  CG  . HIS A 1 77  ? 41.045  -3.615  4.749   1.00 17.90 ? 77  HIS A CG  1 
ATOM   616  N  ND1 . HIS A 1 77  ? 42.211  -3.408  5.375   1.00 20.63 ? 77  HIS A ND1 1 
ATOM   617  C  CD2 . HIS A 1 77  ? 41.291  -4.536  3.749   1.00 19.78 ? 77  HIS A CD2 1 
ATOM   618  C  CE1 . HIS A 1 77  ? 43.158  -4.197  4.850   1.00 21.70 ? 77  HIS A CE1 1 
ATOM   619  N  NE2 . HIS A 1 77  ? 42.620  -4.877  3.843   1.00 22.12 ? 77  HIS A NE2 1 
ATOM   620  N  N   . ILE A 1 78  ? 37.456  -4.510  4.599   1.00 13.49 ? 78  ILE A N   1 
ATOM   621  C  CA  . ILE A 1 78  ? 36.918  -5.548  3.729   1.00 14.57 ? 78  ILE A CA  1 
ATOM   622  C  C   . ILE A 1 78  ? 37.635  -5.598  2.422   1.00 16.19 ? 78  ILE A C   1 
ATOM   623  O  O   . ILE A 1 78  ? 37.948  -4.554  1.803   1.00 14.96 ? 78  ILE A O   1 
ATOM   624  C  CB  . ILE A 1 78  ? 35.422  -5.250  3.424   1.00 14.62 ? 78  ILE A CB  1 
ATOM   625  C  CG1 . ILE A 1 78  ? 34.586  -5.204  4.670   1.00 17.25 ? 78  ILE A CG1 1 
ATOM   626  C  CG2 . ILE A 1 78  ? 34.909  -6.196  2.373   1.00 18.04 ? 78  ILE A CG2 1 
ATOM   627  C  CD1 . ILE A 1 78  ? 33.254  -4.477  4.366   1.00 16.61 ? 78  ILE A CD1 1 
ATOM   628  N  N   . GLN A 1 79  ? 38.003  -6.817  2.023   1.00 16.59 ? 79  GLN A N   1 
ATOM   629  C  CA  . GLN A 1 79  ? 38.584  -7.040  0.699   1.00 20.67 ? 79  GLN A CA  1 
ATOM   630  C  C   . GLN A 1 79  ? 37.521  -7.801  -0.106  1.00 19.58 ? 79  GLN A C   1 
ATOM   631  O  O   . GLN A 1 79  ? 36.815  -8.649  0.432   1.00 21.51 ? 79  GLN A O   1 
ATOM   632  C  CB  . GLN A 1 79  ? 39.863  -7.901  0.944   1.00 27.32 ? 79  GLN A CB  1 
ATOM   633  C  CG  . GLN A 1 79  ? 40.533  -8.497  -0.290  1.00 35.94 ? 79  GLN A CG  1 
ATOM   634  C  CD  . GLN A 1 79  ? 41.449  -7.502  -0.969  1.00 45.56 ? 79  GLN A CD  1 
ATOM   635  O  OE1 . GLN A 1 79  ? 41.674  -6.394  -0.451  1.00 46.42 ? 79  GLN A OE1 1 
ATOM   636  N  NE2 . GLN A 1 79  ? 42.010  -7.893  -2.126  1.00 45.53 ? 79  GLN A NE2 1 
ATOM   637  N  N   . GLY A 1 80  ? 37.366  -7.505  -1.378  1.00 22.02 ? 80  GLY A N   1 
ATOM   638  C  CA  . GLY A 1 80  ? 36.347  -8.202  -2.173  1.00 20.93 ? 80  GLY A CA  1 
ATOM   639  C  C   . GLY A 1 80  ? 35.442  -7.244  -2.926  1.00 23.24 ? 80  GLY A C   1 
ATOM   640  O  O   . GLY A 1 80  ? 34.821  -7.606  -3.959  1.00 24.29 ? 80  GLY A O   1 
ATOM   641  N  N   . LEU A 1 81  ? 35.310  -6.040  -2.391  1.00 20.01 ? 81  LEU A N   1 
ATOM   642  C  CA  . LEU A 1 81  ? 34.570  -5.042  -3.133  1.00 19.33 ? 81  LEU A CA  1 
ATOM   643  C  C   . LEU A 1 81  ? 35.473  -4.324  -4.169  1.00 21.09 ? 81  LEU A C   1 
ATOM   644  O  O   . LEU A 1 81  ? 36.653  -4.631  -4.276  1.00 20.91 ? 81  LEU A O   1 
ATOM   645  C  CB  . LEU A 1 81  ? 33.844  -4.048  -2.202  1.00 20.10 ? 81  LEU A CB  1 
ATOM   646  C  CG  . LEU A 1 81  ? 32.915  -4.731  -1.182  1.00 19.35 ? 81  LEU A CG  1 
ATOM   647  C  CD1 . LEU A 1 81  ? 32.421  -3.837  -0.063  1.00 20.10 ? 81  LEU A CD1 1 
ATOM   648  C  CD2 . LEU A 1 81  ? 31.749  -5.384  -1.944  1.00 19.34 ? 81  LEU A CD2 1 
ATOM   649  N  N   . GLN A 1 82  ? 34.855  -3.413  -4.918  1.00 24.06 ? 82  GLN A N   1 
ATOM   650  C  CA  . GLN A 1 82  ? 35.477  -2.631  -6.011  1.00 29.55 ? 82  GLN A CA  1 
ATOM   651  C  C   . GLN A 1 82  ? 36.724  -1.896  -5.438  1.00 27.30 ? 82  GLN A C   1 
ATOM   652  O  O   . GLN A 1 82  ? 37.911  -1.974  -5.960  1.00 25.60 ? 82  GLN A O   1 
ATOM   653  C  CB  . GLN A 1 82  ? 34.425  -1.547  -6.368  1.00 32.25 ? 82  GLN A CB  1 
ATOM   654  C  CG  . GLN A 1 82  ? 33.888  -0.844  -5.073  1.00 41.94 ? 82  GLN A CG  1 
ATOM   655  C  CD  . GLN A 1 82  ? 32.439  -1.159  -4.603  1.00 45.82 ? 82  GLN A CD  1 
ATOM   656  O  OE1 . GLN A 1 82  ? 31.718  -0.219  -4.202  1.00 49.43 ? 82  GLN A OE1 1 
ATOM   657  N  NE2 . GLN A 1 82  ? 32.007  -2.453  -4.637  1.00 37.95 ? 82  GLN A NE2 1 
ATOM   658  N  N   . SER A 1 83  ? 36.418  -1.216  -4.338  1.00 20.71 ? 83  SER A N   1 
ATOM   659  C  CA  . SER A 1 83  ? 37.384  -0.420  -3.596  1.00 16.57 ? 83  SER A CA  1 
ATOM   660  C  C   . SER A 1 83  ? 37.605  -1.095  -2.262  1.00 15.04 ? 83  SER A C   1 
ATOM   661  O  O   . SER A 1 83  ? 36.756  -1.840  -1.824  1.00 15.26 ? 83  SER A O   1 
ATOM   662  C  CB  . SER A 1 83  ? 36.821  0.930   -3.282  1.00 16.08 ? 83  SER A CB  1 
ATOM   663  O  OG  . SER A 1 83  ? 36.654  1.651   -4.470  1.00 17.82 ? 83  SER A OG  1 
ATOM   664  N  N   . ARG A 1 84  ? 38.703  -0.766  -1.559  1.00 14.52 ? 84  ARG A N   1 
ATOM   665  C  CA  . ARG A 1 84  ? 38.822  -1.111  -0.123  1.00 13.70 ? 84  ARG A CA  1 
ATOM   666  C  C   . ARG A 1 84  ? 37.914  -0.265  0.721   1.00 13.05 ? 84  ARG A C   1 
ATOM   667  O  O   . ARG A 1 84  ? 37.850  0.945   0.548   1.00 12.81 ? 84  ARG A O   1 
ATOM   668  C  CB  . ARG A 1 84  ? 40.235  -0.771  0.345   1.00 15.10 ? 84  ARG A CB  1 
ATOM   669  C  CG  . ARG A 1 84  ? 40.444  -1.011  1.839   1.00 14.94 ? 84  ARG A CG  1 
ATOM   670  C  CD  . ARG A 1 84  ? 41.914  -0.817  2.249   1.00 14.32 ? 84  ARG A CD  1 
ATOM   671  N  NE  . ARG A 1 84  ? 42.694  -1.935  1.772   1.00 15.26 ? 84  ARG A NE  1 
ATOM   672  C  CZ  . ARG A 1 84  ? 44.035  -2.089  2.072   1.00 16.86 ? 84  ARG A CZ  1 
ATOM   673  N  NH1 . ARG A 1 84  ? 44.604  -1.199  2.822   1.00 16.74 ? 84  ARG A NH1 1 
ATOM   674  N  NH2 . ARG A 1 84  ? 44.725  -3.124  1.634   1.00 17.15 ? 84  ARG A NH2 1 
ATOM   675  N  N   . TYR A 1 85  ? 37.167  -0.951  1.625   1.00 11.71 ? 85  TYR A N   1 
ATOM   676  C  CA  . TYR A 1 85  ? 36.369  -0.242  2.584   1.00 11.42 ? 85  TYR A CA  1 
ATOM   677  C  C   . TYR A 1 85  ? 36.921  -0.511  3.947   1.00 12.42 ? 85  TYR A C   1 
ATOM   678  O  O   . TYR A 1 85  ? 37.063  -1.680  4.389   1.00 12.31 ? 85  TYR A O   1 
ATOM   679  C  CB  . TYR A 1 85  ? 34.875  -0.717  2.509   1.00 13.12 ? 85  TYR A CB  1 
ATOM   680  C  CG  . TYR A 1 85  ? 34.154  -0.182  1.284   1.00 10.87 ? 85  TYR A CG  1 
ATOM   681  C  CD1 . TYR A 1 85  ? 33.315  0.945   1.418   1.00 12.01 ? 85  TYR A CD1 1 
ATOM   682  C  CD2 . TYR A 1 85  ? 34.280  -0.748  0.071   1.00 12.33 ? 85  TYR A CD2 1 
ATOM   683  C  CE1 . TYR A 1 85  ? 32.609  1.489   0.339   1.00 10.66 ? 85  TYR A CE1 1 
ATOM   684  C  CE2 . TYR A 1 85  ? 33.627  -0.191  -1.015  1.00 12.01 ? 85  TYR A CE2 1 
ATOM   685  C  CZ  . TYR A 1 85  ? 32.826  0.947   -0.879  1.00 12.29 ? 85  TYR A CZ  1 
ATOM   686  O  OH  . TYR A 1 85  ? 32.085  1.532   -1.918  1.00 17.69 ? 85  TYR A OH  1 
ATOM   687  N  N   . SER A 1 86  ? 37.271  0.548   4.654   1.00 11.42 ? 86  SER A N   1 
ATOM   688  C  CA  . SER A 1 86  ? 37.928  0.406   5.951   1.00 12.55 ? 86  SER A CA  1 
ATOM   689  C  C   . SER A 1 86  ? 36.951  0.623   7.106   1.00 11.77 ? 86  SER A C   1 
ATOM   690  O  O   . SER A 1 86  ? 36.033  1.439   7.004   1.00 11.58 ? 86  SER A O   1 
ATOM   691  C  CB  . SER A 1 86  ? 39.057  1.433   6.085   1.00 14.55 ? 86  SER A CB  1 
ATOM   692  O  OG  . SER A 1 86  ? 40.132  1.165   5.176   1.00 16.48 ? 86  SER A OG  1 
ATOM   693  N  N   . ALA A 1 87  ? 37.127  -0.122  8.201   1.00 12.03 ? 87  ALA A N   1 
ATOM   694  C  CA  . ALA A 1 87  ? 36.197  0.001   9.336   1.00 11.76 ? 87  ALA A CA  1 
ATOM   695  C  C   . ALA A 1 87  ? 36.308  1.353   10.040  1.00 13.45 ? 87  ALA A C   1 
ATOM   696  O  O   . ALA A 1 87  ? 37.386  1.972   10.109  1.00 14.36 ? 87  ALA A O   1 
ATOM   697  C  CB  . ALA A 1 87  ? 36.404  -1.106  10.348  1.00 12.01 ? 87  ALA A CB  1 
ATOM   698  N  N   . THR A 1 88  ? 35.169  1.842   10.524  1.00 12.42 ? 88  THR A N   1 
ATOM   699  C  CA  . THR A 1 88  ? 35.137  2.989   11.393  1.00 12.55 ? 88  THR A CA  1 
ATOM   700  C  C   . THR A 1 88  ? 34.491  2.731   12.750  1.00 12.16 ? 88  THR A C   1 
ATOM   701  O  O   . THR A 1 88  ? 34.916  3.213   13.752  1.00 13.12 ? 88  THR A O   1 
ATOM   702  C  CB  . THR A 1 88  ? 34.526  4.186   10.650  1.00 15.03 ? 88  THR A CB  1 
ATOM   703  O  OG1 . THR A 1 88  ? 34.444  5.319   11.519  1.00 16.41 ? 88  THR A OG1 1 
ATOM   704  C  CG2 . THR A 1 88  ? 33.046  3.886   10.188  1.00 15.51 ? 88  THR A CG2 1 
ATOM   705  N  N   A GLN A 1 89  ? 33.412  1.926   12.798  0.50 11.29 ? 89  GLN A N   1 
ATOM   706  N  N   B GLN A 1 89  ? 33.436  1.937   12.778  0.50 11.29 ? 89  GLN A N   1 
ATOM   707  C  CA  A GLN A 1 89  ? 32.753  1.616   14.061  0.50 11.30 ? 89  GLN A CA  1 
ATOM   708  C  CA  B GLN A 1 89  ? 32.750  1.594   14.016  0.50 11.30 ? 89  GLN A CA  1 
ATOM   709  C  C   A GLN A 1 89  ? 31.776  0.416   13.863  0.50 10.38 ? 89  GLN A C   1 
ATOM   710  C  C   B GLN A 1 89  ? 31.756  0.435   13.875  0.50 10.38 ? 89  GLN A C   1 
ATOM   711  O  O   A GLN A 1 89  ? 31.421  0.085   12.731  0.50 12.41 ? 89  GLN A O   1 
ATOM   712  O  O   B GLN A 1 89  ? 31.435  0.055   12.838  0.50 12.41 ? 89  GLN A O   1 
ATOM   713  C  CB  A GLN A 1 89  ? 31.908  2.805   14.649  0.50 13.27 ? 89  GLN A CB  1 
ATOM   714  C  CB  B GLN A 1 89  ? 31.982  2.787   14.599  0.50 13.27 ? 89  GLN A CB  1 
ATOM   715  C  CG  A GLN A 1 89  ? 30.863  3.218   13.659  0.50 17.45 ? 89  GLN A CG  1 
ATOM   716  C  CG  B GLN A 1 89  ? 30.916  3.358   13.709  0.50 17.45 ? 89  GLN A CG  1 
ATOM   717  C  CD  A GLN A 1 89  ? 29.746  4.002   14.247  0.50 21.19 ? 89  GLN A CD  1 
ATOM   718  C  CD  B GLN A 1 89  ? 29.549  3.169   14.261  0.50 21.19 ? 89  GLN A CD  1 
ATOM   719  O  OE1 A GLN A 1 89  ? 28.789  3.483   14.726  0.50 23.86 ? 89  GLN A OE1 1 
ATOM   720  O  OE1 B GLN A 1 89  ? 29.063  2.149   14.335  0.50 23.86 ? 89  GLN A OE1 1 
ATOM   721  N  NE2 A GLN A 1 89  ? 29.947  5.308   14.290  0.50 23.90 ? 89  GLN A NE2 1 
ATOM   722  N  NE2 B GLN A 1 89  ? 28.956  4.207   14.591  0.50 23.90 ? 89  GLN A NE2 1 
ATOM   723  N  N   . LEU A 1 90  ? 31.401  -0.174  14.980  1.00 10.49 ? 90  LEU A N   1 
ATOM   724  C  CA  . LEU A 1 90  ? 30.257  -1.067  15.005  1.00 10.71 ? 90  LEU A CA  1 
ATOM   725  C  C   . LEU A 1 90  ? 29.278  -0.603  16.054  1.00 10.97 ? 90  LEU A C   1 
ATOM   726  O  O   . LEU A 1 90  ? 29.599  0.126   16.983  1.00 10.75 ? 90  LEU A O   1 
ATOM   727  C  CB  . LEU A 1 90  ? 30.676  -2.559  15.096  1.00 10.73 ? 90  LEU A CB  1 
ATOM   728  C  CG  . LEU A 1 90  ? 31.393  -3.021  16.394  1.00 12.11 ? 90  LEU A CG  1 
ATOM   729  C  CD1 . LEU A 1 90  ? 30.518  -3.124  17.649  1.00 11.59 ? 90  LEU A CD1 1 
ATOM   730  C  CD2 . LEU A 1 90  ? 32.087  -4.370  16.066  1.00 13.25 ? 90  LEU A CD2 1 
ATOM   731  N  N   . HIS A 1 91  ? 28.027  -1.017  15.888  1.00 9.59  ? 91  HIS A N   1 
ATOM   732  C  CA  . HIS A 1 91  ? 26.956  -0.657  16.840  1.00 9.51  ? 91  HIS A CA  1 
ATOM   733  C  C   . HIS A 1 91  ? 25.803  -1.617  16.709  1.00 9.79  ? 91  HIS A C   1 
ATOM   734  O  O   . HIS A 1 91  ? 25.826  -2.434  15.806  1.00 8.87  ? 91  HIS A O   1 
ATOM   735  C  CB  . HIS A 1 91  ? 26.465  0.830   16.650  1.00 10.00 ? 91  HIS A CB  1 
ATOM   736  C  CG  . HIS A 1 91  ? 25.856  1.057   15.284  1.00 10.39 ? 91  HIS A CG  1 
ATOM   737  N  ND1 . HIS A 1 91  ? 26.573  1.489   14.269  1.00 10.01 ? 91  HIS A ND1 1 
ATOM   738  C  CD2 . HIS A 1 91  ? 24.600  0.722   14.796  1.00 9.25  ? 91  HIS A CD2 1 
ATOM   739  C  CE1 . HIS A 1 91  ? 25.807  1.503   13.142  1.00 8.93  ? 91  HIS A CE1 1 
ATOM   740  N  NE2 . HIS A 1 91  ? 24.586  1.045   13.482  1.00 9.43  ? 91  HIS A NE2 1 
ATOM   741  N  N   . LEU A 1 92  ? 24.787  -1.514  17.585  1.00 9.79  ? 92  LEU A N   1 
ATOM   742  C  CA  . LEU A 1 92  ? 23.664  -2.445  17.513  1.00 9.20  ? 92  LEU A CA  1 
ATOM   743  C  C   . LEU A 1 92  ? 22.309  -1.696  17.548  1.00 8.59  ? 92  LEU A C   1 
ATOM   744  O  O   . LEU A 1 92  ? 22.192  -0.516  17.867  1.00 9.69  ? 92  LEU A O   1 
ATOM   745  C  CB  . LEU A 1 92  ? 23.698  -3.325  18.769  1.00 11.37 ? 92  LEU A CB  1 
ATOM   746  C  CG  . LEU A 1 92  ? 24.933  -4.309  18.736  1.00 11.62 ? 92  LEU A CG  1 
ATOM   747  C  CD1 . LEU A 1 92  ? 25.878  -3.803  19.790  1.00 15.42 ? 92  LEU A CD1 1 
ATOM   748  C  CD2 . LEU A 1 92  ? 24.441  -5.695  19.042  1.00 12.69 ? 92  LEU A CD2 1 
ATOM   749  N  N   . HIS A 1 93  ? 21.266  -2.451  17.209  1.00 8.49  ? 93  HIS A N   1 
ATOM   750  C  CA  . HIS A 1 93  ? 19.851  -1.962  17.198  1.00 9.12  ? 93  HIS A CA  1 
ATOM   751  C  C   . HIS A 1 93  ? 19.057  -3.064  17.828  1.00 9.17  ? 93  HIS A C   1 
ATOM   752  O  O   . HIS A 1 93  ? 19.283  -4.270  17.569  1.00 10.48 ? 93  HIS A O   1 
ATOM   753  C  CB  . HIS A 1 93  ? 19.353  -1.799  15.768  1.00 8.86  ? 93  HIS A CB  1 
ATOM   754  C  CG  . HIS A 1 93  ? 20.126  -0.762  14.977  1.00 8.49  ? 93  HIS A CG  1 
ATOM   755  N  ND1 . HIS A 1 93  ? 19.845  0.555   15.038  1.00 8.33  ? 93  HIS A ND1 1 
ATOM   756  C  CD2 . HIS A 1 93  ? 21.220  -0.888  14.118  1.00 7.78  ? 93  HIS A CD2 1 
ATOM   757  C  CE1 . HIS A 1 93  ? 20.699  1.236   14.246  1.00 8.18  ? 93  HIS A CE1 1 
ATOM   758  N  NE2 . HIS A 1 93  ? 21.538  0.349   13.683  1.00 8.81  ? 93  HIS A NE2 1 
ATOM   759  N  N   . TRP A 1 94  ? 18.077  -2.686  18.691  1.00 10.29 ? 94  TRP A N   1 
ATOM   760  C  CA  . TRP A 1 94  ? 17.330  -3.753  19.415  1.00 9.34  ? 94  TRP A CA  1 
ATOM   761  C  C   . TRP A 1 94  ? 15.942  -3.273  19.753  1.00 11.00 ? 94  TRP A C   1 
ATOM   762  O  O   . TRP A 1 94  ? 15.659  -2.074  19.562  1.00 10.56 ? 94  TRP A O   1 
ATOM   763  C  CB  . TRP A 1 94  ? 18.069  -4.218  20.755  1.00 10.31 ? 94  TRP A CB  1 
ATOM   764  C  CG  . TRP A 1 94  ? 18.390  -3.104  21.680  1.00 10.28 ? 94  TRP A CG  1 
ATOM   765  C  CD1 . TRP A 1 94  ? 17.574  -2.613  22.693  1.00 10.83 ? 94  TRP A CD1 1 
ATOM   766  C  CD2 . TRP A 1 94  ? 19.585  -2.284  21.698  1.00 10.16 ? 94  TRP A CD2 1 
ATOM   767  N  NE1 . TRP A 1 94  ? 18.190  -1.556  23.327  1.00 11.25 ? 94  TRP A NE1 1 
ATOM   768  C  CE2 . TRP A 1 94  ? 19.449  -1.373  22.823  1.00 10.56 ? 94  TRP A CE2 1 
ATOM   769  C  CE3 . TRP A 1 94  ? 20.813  -2.269  20.968  1.00 9.73  ? 94  TRP A CE3 1 
ATOM   770  C  CZ2 . TRP A 1 94  ? 20.364  -0.386  23.073  1.00 10.26 ? 94  TRP A CZ2 1 
ATOM   771  C  CZ3 . TRP A 1 94  ? 21.750  -1.293  21.226  1.00 10.71 ? 94  TRP A CZ3 1 
ATOM   772  C  CH2 . TRP A 1 94  ? 21.580  -0.384  22.330  1.00 10.26 ? 94  TRP A CH2 1 
ATOM   773  N  N   . GLY A 1 95  ? 15.152  -4.143  20.320  1.00 10.25 ? 95  GLY A N   1 
ATOM   774  C  CA  . GLY A 1 95  ? 13.708  -3.833  20.660  1.00 11.32 ? 95  GLY A CA  1 
ATOM   775  C  C   . GLY A 1 95  ? 13.614  -3.519  22.184  1.00 10.59 ? 95  GLY A C   1 
ATOM   776  O  O   . GLY A 1 95  ? 14.254  -2.609  22.758  1.00 12.64 ? 95  GLY A O   1 
ATOM   777  N  N   . ASN A 1 96  ? 12.729  -4.277  22.840  1.00 14.23 ? 96  ASN A N   1 
ATOM   778  C  CA  . ASN A 1 96  ? 12.547  -4.056  24.289  1.00 14.83 ? 96  ASN A CA  1 
ATOM   779  C  C   . ASN A 1 96  ? 12.062  -5.387  24.899  1.00 14.93 ? 96  ASN A C   1 
ATOM   780  O  O   . ASN A 1 96  ? 11.624  -6.279  24.226  1.00 12.55 ? 96  ASN A O   1 
ATOM   781  C  CB  . ASN A 1 96  ? 11.562  -2.924  24.534  1.00 15.13 ? 96  ASN A CB  1 
ATOM   782  C  CG  . ASN A 1 96  ? 10.130  -3.310  24.193  1.00 16.02 ? 96  ASN A CG  1 
ATOM   783  O  OD1 . ASN A 1 96  ? 9.439   -3.940  25.017  1.00 19.66 ? 96  ASN A OD1 1 
ATOM   784  N  ND2 . ASN A 1 96  ? 9.710   -2.998  23.006  1.00 18.16 ? 96  ASN A ND2 1 
ATOM   785  N  N   . PRO A 1 97  ? 12.132  -5.515  26.247  1.00 16.26 ? 97  PRO A N   1 
ATOM   786  C  CA  . PRO A 1 97  ? 11.799  -6.789  26.779  1.00 15.76 ? 97  PRO A CA  1 
ATOM   787  C  C   . PRO A 1 97  ? 10.378  -7.255  26.575  1.00 15.58 ? 97  PRO A C   1 
ATOM   788  O  O   . PRO A 1 97  ? 10.133  -8.414  26.506  1.00 15.10 ? 97  PRO A O   1 
ATOM   789  C  CB  . PRO A 1 97  ? 12.076  -6.585  28.297  1.00 15.38 ? 97  PRO A CB  1 
ATOM   790  C  CG  . PRO A 1 97  ? 13.155  -5.568  28.336  1.00 19.69 ? 97  PRO A CG  1 
ATOM   791  C  CD  . PRO A 1 97  ? 12.836  -4.648  27.218  1.00 18.38 ? 97  PRO A CD  1 
ATOM   792  N  N   . ASN A 1 98  ? 9.450   -6.353  26.442  1.00 14.47 ? 98  ASN A N   1 
ATOM   793  C  CA  . ASN A 1 98  ? 8.057   -6.792  26.089  1.00 18.57 ? 98  ASN A CA  1 
ATOM   794  C  C   . ASN A 1 98  ? 7.837   -7.201  24.634  1.00 16.67 ? 98  ASN A C   1 
ATOM   795  O  O   . ASN A 1 98  ? 6.895   -7.914  24.299  1.00 19.58 ? 98  ASN A O   1 
ATOM   796  C  CB  . ASN A 1 98  ? 7.083   -5.652  26.459  1.00 19.87 ? 98  ASN A CB  1 
ATOM   797  C  CG  . ASN A 1 98  ? 6.989   -5.459  27.969  1.00 27.74 ? 98  ASN A CG  1 
ATOM   798  O  OD1 . ASN A 1 98  ? 6.984   -6.423  28.750  1.00 31.53 ? 98  ASN A OD1 1 
ATOM   799  N  ND2 . ASN A 1 98  ? 6.889   -4.223  28.373  1.00 33.22 ? 98  ASN A ND2 1 
ATOM   800  N  N   . ASP A 1 99  ? 8.747   -6.762  23.757  1.00 14.43 ? 99  ASP A N   1 
ATOM   801  C  CA  . ASP A 1 99  ? 8.644   -7.059  22.320  1.00 16.14 ? 99  ASP A CA  1 
ATOM   802  C  C   . ASP A 1 99  ? 10.081  -7.160  21.778  1.00 13.05 ? 99  ASP A C   1 
ATOM   803  O  O   . ASP A 1 99  ? 10.614  -6.190  21.233  1.00 13.73 ? 99  ASP A O   1 
ATOM   804  C  CB  . ASP A 1 99  ? 7.844   -5.960  21.637  1.00 17.07 ? 99  ASP A CB  1 
ATOM   805  C  CG  . ASP A 1 99  ? 7.284   -6.395  20.275  1.00 20.72 ? 99  ASP A CG  1 
ATOM   806  O  OD1 . ASP A 1 99  ? 7.553   -7.482  19.767  1.00 22.91 ? 99  ASP A OD1 1 
ATOM   807  O  OD2 . ASP A 1 99  ? 6.582   -5.596  19.675  1.00 22.45 ? 99  ASP A OD2 1 
ATOM   808  N  N   . PRO A 1 100 ? 10.752  -8.312  22.068  1.00 13.21 ? 100 PRO A N   1 
ATOM   809  C  CA  . PRO A 1 100 ? 12.246  -8.368  21.904  1.00 12.75 ? 100 PRO A CA  1 
ATOM   810  C  C   . PRO A 1 100 ? 12.564  -8.714  20.437  1.00 13.42 ? 100 PRO A C   1 
ATOM   811  O  O   . PRO A 1 100 ? 13.138  -9.731  20.089  1.00 13.62 ? 100 PRO A O   1 
ATOM   812  C  CB  . PRO A 1 100 ? 12.679  -9.504  22.852  1.00 14.18 ? 100 PRO A CB  1 
ATOM   813  C  CG  . PRO A 1 100 ? 11.515  -10.409 22.843  1.00 13.69 ? 100 PRO A CG  1 
ATOM   814  C  CD  . PRO A 1 100 ? 10.274  -9.486  22.827  1.00 13.56 ? 100 PRO A CD  1 
ATOM   815  N  N   . HIS A 1 101 ? 12.124  -7.832  19.566  1.00 13.50 ? 101 HIS A N   1 
ATOM   816  C  CA  . HIS A 1 101 ? 12.264  -8.087  18.096  1.00 15.30 ? 101 HIS A CA  1 
ATOM   817  C  C   . HIS A 1 101 ? 12.622  -6.835  17.374  1.00 14.49 ? 101 HIS A C   1 
ATOM   818  O  O   . HIS A 1 101 ? 11.807  -6.316  16.576  1.00 18.10 ? 101 HIS A O   1 
ATOM   819  C  CB  . HIS A 1 101 ? 10.916  -8.581  17.526  1.00 14.27 ? 101 HIS A CB  1 
ATOM   820  C  CG  . HIS A 1 101 ? 10.377  -9.738  18.306  1.00 16.37 ? 101 HIS A CG  1 
ATOM   821  N  ND1 . HIS A 1 101 ? 10.900  -10.973 18.206  1.00 18.22 ? 101 HIS A ND1 1 
ATOM   822  C  CD2 . HIS A 1 101 ? 9.379   -9.809  19.276  1.00 17.76 ? 101 HIS A CD2 1 
ATOM   823  C  CE1 . HIS A 1 101 ? 10.249  -11.808 19.035  1.00 19.68 ? 101 HIS A CE1 1 
ATOM   824  N  NE2 . HIS A 1 101 ? 9.342   -11.094 19.715  1.00 19.00 ? 101 HIS A NE2 1 
ATOM   825  N  N   . GLY A 1 102 ? 13.842  -6.353  17.566  1.00 11.46 ? 102 GLY A N   1 
ATOM   826  C  CA  . GLY A 1 102 ? 14.248  -5.004  17.152  1.00 9.98  ? 102 GLY A CA  1 
ATOM   827  C  C   . GLY A 1 102 ? 15.339  -4.964  16.088  1.00 10.44 ? 102 GLY A C   1 
ATOM   828  O  O   . GLY A 1 102 ? 16.050  -4.004  15.996  1.00 9.64  ? 102 GLY A O   1 
ATOM   829  N  N   . SER A 1 103 ? 15.488  -6.019  15.305  1.00 10.08 ? 103 SER A N   1 
ATOM   830  C  CA  . SER A 1 103 ? 16.374  -5.892  14.115  1.00 9.25  ? 103 SER A CA  1 
ATOM   831  C  C   . SER A 1 103 ? 15.795  -4.803  13.183  1.00 10.07 ? 103 SER A C   1 
ATOM   832  O  O   . SER A 1 103 ? 14.596  -4.486  13.221  1.00 11.56 ? 103 SER A O   1 
ATOM   833  C  CB  . SER A 1 103 ? 16.473  -7.261  13.370  1.00 9.81  ? 103 SER A CB  1 
ATOM   834  O  OG  . SER A 1 103 ? 15.259  -7.609  12.676  1.00 9.22  ? 103 SER A OG  1 
ATOM   835  N  N   . GLU A 1 104 ? 16.665  -4.284  12.337  1.00 8.04  ? 104 GLU A N   1 
ATOM   836  C  CA  . GLU A 1 104 ? 16.229  -3.258  11.335  1.00 8.21  ? 104 GLU A CA  1 
ATOM   837  C  C   . GLU A 1 104 ? 15.700  -3.939  10.074  1.00 9.00  ? 104 GLU A C   1 
ATOM   838  O  O   . GLU A 1 104 ? 14.572  -3.743  9.625   1.00 8.20  ? 104 GLU A O   1 
ATOM   839  C  CB  . GLU A 1 104 ? 17.462  -2.380  10.928  1.00 8.38  ? 104 GLU A CB  1 
ATOM   840  C  CG  . GLU A 1 104 ? 17.983  -1.659  12.218  1.00 9.05  ? 104 GLU A CG  1 
ATOM   841  C  CD  . GLU A 1 104 ? 18.353  -0.210  11.923  1.00 10.18 ? 104 GLU A CD  1 
ATOM   842  O  OE1 . GLU A 1 104 ? 19.369  0.041   11.356  1.00 10.89 ? 104 GLU A OE1 1 
ATOM   843  O  OE2 . GLU A 1 104 ? 17.498  0.724   12.166  1.00 10.38 ? 104 GLU A OE2 1 
ATOM   844  N  N   . HIS A 1 105 ? 16.571  -4.765  9.488   1.00 8.28  ? 105 HIS A N   1 
ATOM   845  C  CA  . HIS A 1 105 ? 16.071  -5.608  8.397   1.00 8.12  ? 105 HIS A CA  1 
ATOM   846  C  C   . HIS A 1 105 ? 15.188  -6.657  8.937   1.00 8.29  ? 105 HIS A C   1 
ATOM   847  O  O   . HIS A 1 105 ? 15.389  -7.207  10.030  1.00 10.33 ? 105 HIS A O   1 
ATOM   848  C  CB  . HIS A 1 105 ? 17.245  -6.235  7.596   1.00 7.48  ? 105 HIS A CB  1 
ATOM   849  C  CG  . HIS A 1 105 ? 18.033  -5.176  6.887   1.00 8.56  ? 105 HIS A CG  1 
ATOM   850  N  ND1 . HIS A 1 105 ? 19.091  -4.527  7.474   1.00 8.30  ? 105 HIS A ND1 1 
ATOM   851  C  CD2 . HIS A 1 105 ? 17.853  -4.618  5.650   1.00 8.23  ? 105 HIS A CD2 1 
ATOM   852  C  CE1 . HIS A 1 105 ? 19.556  -3.624  6.620   1.00 8.55  ? 105 HIS A CE1 1 
ATOM   853  N  NE2 . HIS A 1 105 ? 18.819  -3.691  5.502   1.00 8.31  ? 105 HIS A NE2 1 
ATOM   854  N  N   . THR A 1 106 ? 14.273  -7.079  8.089   1.00 8.79  ? 106 THR A N   1 
ATOM   855  C  CA  . THR A 1 106 ? 13.362  -8.227  8.334   1.00 9.57  ? 106 THR A CA  1 
ATOM   856  C  C   . THR A 1 106 ? 13.518  -9.236  7.237   1.00 8.61  ? 106 THR A C   1 
ATOM   857  O  O   . THR A 1 106 ? 13.960  -8.897  6.160   1.00 9.81  ? 106 THR A O   1 
ATOM   858  C  CB  . THR A 1 106 ? 11.878  -7.792  8.469   1.00 9.82  ? 106 THR A CB  1 
ATOM   859  O  OG1 . THR A 1 106 ? 11.420  -7.203  7.248   1.00 10.93 ? 106 THR A OG1 1 
ATOM   860  C  CG2 . THR A 1 106 ? 11.691  -6.883  9.639   1.00 10.17 ? 106 THR A CG2 1 
ATOM   861  N  N   . VAL A 1 107 ? 13.187  -10.509 7.530   1.00 9.00  ? 107 VAL A N   1 
ATOM   862  C  CA  . VAL A 1 107 ? 13.280  -11.565 6.530   1.00 9.91  ? 107 VAL A CA  1 
ATOM   863  C  C   . VAL A 1 107 ? 11.851  -12.209 6.435   1.00 9.82  ? 107 VAL A C   1 
ATOM   864  O  O   . VAL A 1 107 ? 11.331  -12.625 7.483   1.00 11.60 ? 107 VAL A O   1 
ATOM   865  C  CB  . VAL A 1 107 ? 14.355  -12.607 6.916   1.00 9.84  ? 107 VAL A CB  1 
ATOM   866  C  CG1 . VAL A 1 107 ? 14.276  -13.786 5.952   1.00 10.51 ? 107 VAL A CG1 1 
ATOM   867  C  CG2 . VAL A 1 107 ? 15.783  -11.978 6.960   1.00 11.96 ? 107 VAL A CG2 1 
ATOM   868  N  N   . SER A 1 108 ? 11.254  -12.183 5.263   1.00 10.89 ? 108 SER A N   1 
ATOM   869  C  CA  . SER A 1 108 ? 9.888   -12.678 5.031   1.00 12.31 ? 108 SER A CA  1 
ATOM   870  C  C   . SER A 1 108 ? 8.961   -12.079 6.065   1.00 12.29 ? 108 SER A C   1 
ATOM   871  O  O   . SER A 1 108 ? 8.089   -12.776 6.685   1.00 13.86 ? 108 SER A O   1 
ATOM   872  C  CB  . SER A 1 108 ? 9.870   -14.217 5.106   1.00 13.84 ? 108 SER A CB  1 
ATOM   873  O  OG  . SER A 1 108 ? 10.721  -14.796 4.138   1.00 18.07 ? 108 SER A OG  1 
ATOM   874  N  N   . GLY A 1 109 ? 9.173   -10.783 6.329   1.00 11.49 ? 109 GLY A N   1 
ATOM   875  C  CA  . GLY A 1 109 ? 8.300   -9.995  7.209   1.00 11.61 ? 109 GLY A CA  1 
ATOM   876  C  C   . GLY A 1 109 ? 8.608   -10.098 8.730   1.00 13.62 ? 109 GLY A C   1 
ATOM   877  O  O   . GLY A 1 109 ? 8.013   -9.364  9.512   1.00 16.50 ? 109 GLY A O   1 
ATOM   878  N  N   . GLN A 1 110 ? 9.581   -10.930 9.130   1.00 12.12 ? 110 GLN A N   1 
ATOM   879  C  CA  . GLN A 1 110 ? 9.941   -11.190 10.530  1.00 14.35 ? 110 GLN A CA  1 
ATOM   880  C  C   . GLN A 1 110 ? 11.176  -10.411 10.991  1.00 11.61 ? 110 GLN A C   1 
ATOM   881  O  O   . GLN A 1 110 ? 12.201  -10.442 10.338  1.00 10.99 ? 110 GLN A O   1 
ATOM   882  C  CB  . GLN A 1 110 ? 10.234  -12.669 10.662  1.00 14.16 ? 110 GLN A CB  1 
ATOM   883  C  CG  . GLN A 1 110 ? 9.132   -13.599 10.099  1.00 14.82 ? 110 GLN A CG  1 
ATOM   884  C  CD  . GLN A 1 110 ? 7.714   -13.180 10.463  1.00 14.26 ? 110 GLN A CD  1 
ATOM   885  O  OE1 . GLN A 1 110 ? 6.869   -12.905 9.552   1.00 18.50 ? 110 GLN A OE1 1 
ATOM   886  N  NE2 . GLN A 1 110 ? 7.443   -13.140 11.741  1.00 13.63 ? 110 GLN A NE2 1 
ATOM   887  N  N   . HIS A 1 111 ? 11.038  -9.799  12.156  1.00 11.96 ? 111 HIS A N   1 
ATOM   888  C  CA  . HIS A 1 111 ? 12.177  -9.227  12.835  1.00 12.27 ? 111 HIS A CA  1 
ATOM   889  C  C   . HIS A 1 111 ? 12.945  -10.253 13.539  1.00 13.20 ? 111 HIS A C   1 
ATOM   890  O  O   . HIS A 1 111 ? 12.388  -11.211 14.094  1.00 18.09 ? 111 HIS A O   1 
ATOM   891  C  CB  . HIS A 1 111 ? 11.736  -8.194  13.881  1.00 14.27 ? 111 HIS A CB  1 
ATOM   892  C  CG  . HIS A 1 111 ? 11.389  -6.857  13.305  1.00 13.84 ? 111 HIS A CG  1 
ATOM   893  N  ND1 . HIS A 1 111 ? 10.125  -6.515  12.822  1.00 15.61 ? 111 HIS A ND1 1 
ATOM   894  C  CD2 . HIS A 1 111 ? 12.192  -5.744  13.129  1.00 13.02 ? 111 HIS A CD2 1 
ATOM   895  C  CE1 . HIS A 1 111 ? 10.151  -5.223  12.402  1.00 14.84 ? 111 HIS A CE1 1 
ATOM   896  N  NE2 . HIS A 1 111 ? 11.443  -4.760  12.596  1.00 16.15 ? 111 HIS A NE2 1 
ATOM   897  N  N   . PHE A 1 112 ? 14.239  -10.098 13.528  1.00 10.98 ? 112 PHE A N   1 
ATOM   898  C  CA  . PHE A 1 112 ? 15.083  -10.809 14.477  1.00 10.08 ? 112 PHE A CA  1 
ATOM   899  C  C   . PHE A 1 112 ? 15.134  -10.045 15.800  1.00 11.09 ? 112 PHE A C   1 
ATOM   900  O  O   . PHE A 1 112 ? 14.711  -8.816  15.889  1.00 10.73 ? 112 PHE A O   1 
ATOM   901  C  CB  . PHE A 1 112 ? 16.481  -11.015 13.841  1.00 11.43 ? 112 PHE A CB  1 
ATOM   902  C  CG  . PHE A 1 112 ? 16.463  -12.109 12.795  1.00 12.31 ? 112 PHE A CG  1 
ATOM   903  C  CD1 . PHE A 1 112 ? 16.945  -13.424 13.104  1.00 14.29 ? 112 PHE A CD1 1 
ATOM   904  C  CD2 . PHE A 1 112 ? 15.855  -11.856 11.526  1.00 13.64 ? 112 PHE A CD2 1 
ATOM   905  C  CE1 . PHE A 1 112 ? 16.867  -14.477 12.155  1.00 15.52 ? 112 PHE A CE1 1 
ATOM   906  C  CE2 . PHE A 1 112 ? 15.728  -12.956 10.630  1.00 15.64 ? 112 PHE A CE2 1 
ATOM   907  C  CZ  . PHE A 1 112 ? 16.244  -14.229 10.957  1.00 15.87 ? 112 PHE A CZ  1 
ATOM   908  N  N   . ALA A 1 113 ? 15.788  -10.633 16.823  1.00 10.35 ? 113 ALA A N   1 
ATOM   909  C  CA  . ALA A 1 113 ? 15.847  -9.947  18.119  1.00 10.76 ? 113 ALA A CA  1 
ATOM   910  C  C   . ALA A 1 113 ? 16.606  -8.637  18.093  1.00 9.63  ? 113 ALA A C   1 
ATOM   911  O  O   . ALA A 1 113 ? 16.233  -7.599  18.726  1.00 11.18 ? 113 ALA A O   1 
ATOM   912  C  CB  . ALA A 1 113 ? 16.469  -10.821 19.215  1.00 11.26 ? 113 ALA A CB  1 
ATOM   913  N  N   . ALA A 1 114 ? 17.732  -8.637  17.325  1.00 8.81  ? 114 ALA A N   1 
ATOM   914  C  CA  . ALA A 1 114 ? 18.581  -7.453  17.274  1.00 8.75  ? 114 ALA A CA  1 
ATOM   915  C  C   . ALA A 1 114 ? 19.413  -7.497  16.015  1.00 8.37  ? 114 ALA A C   1 
ATOM   916  O  O   . ALA A 1 114 ? 19.332  -8.499  15.273  1.00 10.32 ? 114 ALA A O   1 
ATOM   917  C  CB  . ALA A 1 114 ? 19.467  -7.383  18.531  1.00 10.20 ? 114 ALA A CB  1 
ATOM   918  N  N   . GLU A 1 115 ? 20.208  -6.445  15.807  1.00 8.27  ? 115 GLU A N   1 
ATOM   919  C  CA  . GLU A 1 115 ? 21.048  -6.422  14.595  1.00 9.50  ? 115 GLU A CA  1 
ATOM   920  C  C   . GLU A 1 115 ? 22.330  -5.659  14.899  1.00 9.80  ? 115 GLU A C   1 
ATOM   921  O  O   . GLU A 1 115 ? 22.317  -4.576  15.489  1.00 10.59 ? 115 GLU A O   1 
ATOM   922  C  CB  . GLU A 1 115 ? 20.250  -5.791  13.421  1.00 8.05  ? 115 GLU A CB  1 
ATOM   923  C  CG  . GLU A 1 115 ? 20.957  -5.748  12.044  1.00 7.82  ? 115 GLU A CG  1 
ATOM   924  C  CD  . GLU A 1 115 ? 19.998  -5.430  10.906  1.00 8.32  ? 115 GLU A CD  1 
ATOM   925  O  OE1 . GLU A 1 115 ? 18.785  -5.739  11.029  1.00 8.62  ? 115 GLU A OE1 1 
ATOM   926  O  OE2 . GLU A 1 115 ? 20.435  -4.927  9.881   1.00 8.30  ? 115 GLU A OE2 1 
ATOM   927  N  N   . LEU A 1 116 ? 23.508  -6.202  14.454  1.00 9.45  ? 116 LEU A N   1 
ATOM   928  C  CA  . LEU A 1 116 ? 24.821  -5.573  14.632  1.00 10.19 ? 116 LEU A CA  1 
ATOM   929  C  C   . LEU A 1 116 ? 25.180  -5.055  13.273  1.00 8.68  ? 116 LEU A C   1 
ATOM   930  O  O   . LEU A 1 116 ? 24.992  -5.737  12.219  1.00 8.47  ? 116 LEU A O   1 
ATOM   931  C  CB  . LEU A 1 116 ? 25.822  -6.688  14.979  1.00 10.51 ? 116 LEU A CB  1 
ATOM   932  C  CG  . LEU A 1 116 ? 27.302  -6.233  14.877  1.00 12.72 ? 116 LEU A CG  1 
ATOM   933  C  CD1 . LEU A 1 116 ? 27.666  -5.441  16.106  1.00 14.71 ? 116 LEU A CD1 1 
ATOM   934  C  CD2 . LEU A 1 116 ? 28.188  -7.461  14.762  1.00 14.63 ? 116 LEU A CD2 1 
ATOM   935  N  N   . HIS A 1 117 ? 25.684  -3.806  13.237  1.00 7.88  ? 117 HIS A N   1 
ATOM   936  C  CA  . HIS A 1 117 ? 26.212  -3.168  11.988  1.00 8.67  ? 117 HIS A CA  1 
ATOM   937  C  C   . HIS A 1 117 ? 27.656  -2.835  12.184  1.00 9.24  ? 117 HIS A C   1 
ATOM   938  O  O   . HIS A 1 117 ? 28.043  -2.225  13.157  1.00 8.98  ? 117 HIS A O   1 
ATOM   939  C  CB  . HIS A 1 117 ? 25.481  -1.861  11.758  1.00 8.95  ? 117 HIS A CB  1 
ATOM   940  C  CG  . HIS A 1 117 ? 24.058  -2.081  11.351  1.00 8.31  ? 117 HIS A CG  1 
ATOM   941  N  ND1 . HIS A 1 117 ? 23.070  -1.122  11.437  1.00 8.79  ? 117 HIS A ND1 1 
ATOM   942  C  CD2 . HIS A 1 117 ? 23.512  -3.144  10.779  1.00 8.96  ? 117 HIS A CD2 1 
ATOM   943  C  CE1 . HIS A 1 117 ? 21.926  -1.674  10.958  1.00 8.28  ? 117 HIS A CE1 1 
ATOM   944  N  NE2 . HIS A 1 117 ? 22.164  -2.852  10.530  1.00 8.47  ? 117 HIS A NE2 1 
ATOM   945  N  N   . ILE A 1 118 ? 28.478  -3.266  11.230  1.00 10.05 ? 118 ILE A N   1 
ATOM   946  C  CA  . ILE A 1 118 ? 29.919  -2.927  11.216  1.00 9.08  ? 118 ILE A CA  1 
ATOM   947  C  C   . ILE A 1 118 ? 30.063  -1.978  10.049  1.00 8.86  ? 118 ILE A C   1 
ATOM   948  O  O   . ILE A 1 118 ? 29.941  -2.399  8.821   1.00 8.74  ? 118 ILE A O   1 
ATOM   949  C  CB  . ILE A 1 118 ? 30.799  -4.143  11.035  1.00 10.02 ? 118 ILE A CB  1 
ATOM   950  C  CG1 . ILE A 1 118 ? 30.467  -5.231  12.058  1.00 10.87 ? 118 ILE A CG1 1 
ATOM   951  C  CG2 . ILE A 1 118 ? 32.245  -3.596  11.215  1.00 10.57 ? 118 ILE A CG2 1 
ATOM   952  C  CD1 . ILE A 1 118 ? 31.327  -6.522  11.959  1.00 12.44 ? 118 ILE A CD1 1 
ATOM   953  N  N   . VAL A 1 119 ? 30.276  -0.687  10.365  1.00 8.75  ? 119 VAL A N   1 
ATOM   954  C  CA  . VAL A 1 119 ? 30.269  0.344   9.362   1.00 9.99  ? 119 VAL A CA  1 
ATOM   955  C  C   . VAL A 1 119 ? 31.673  0.507   8.794   1.00 9.92  ? 119 VAL A C   1 
ATOM   956  O  O   . VAL A 1 119 ? 32.607  0.617   9.560   1.00 10.79 ? 119 VAL A O   1 
ATOM   957  C  CB  . VAL A 1 119 ? 29.808  1.664   9.971   1.00 10.22 ? 119 VAL A CB  1 
ATOM   958  C  CG1 . VAL A 1 119 ? 29.773  2.743   8.891   1.00 10.18 ? 119 VAL A CG1 1 
ATOM   959  C  CG2 . VAL A 1 119 ? 28.422  1.520   10.703  1.00 10.22 ? 119 VAL A CG2 1 
ATOM   960  N  N   . HIS A 1 120 ? 31.761  0.549   7.466   1.00 10.31 ? 120 HIS A N   1 
ATOM   961  C  CA  . HIS A 1 120 ? 33.062  0.826   6.719   1.00 11.15 ? 120 HIS A CA  1 
ATOM   962  C  C   . HIS A 1 120 ? 32.882  1.958   5.789   1.00 11.70 ? 120 HIS A C   1 
ATOM   963  O  O   . HIS A 1 120 ? 31.756  2.229   5.341   1.00 11.95 ? 120 HIS A O   1 
ATOM   964  C  CB  . HIS A 1 120 ? 33.499  -0.419  5.908   1.00 11.04 ? 120 HIS A CB  1 
ATOM   965  C  CG  . HIS A 1 120 ? 33.662  -1.691  6.729   1.00 11.15 ? 120 HIS A CG  1 
ATOM   966  N  ND1 . HIS A 1 120 ? 32.572  -2.360  7.299   1.00 10.89 ? 120 HIS A ND1 1 
ATOM   967  C  CD2 . HIS A 1 120 ? 34.801  -2.453  7.019   1.00 10.84 ? 120 HIS A CD2 1 
ATOM   968  C  CE1 . HIS A 1 120 ? 33.023  -3.485  7.943   1.00 9.88  ? 120 HIS A CE1 1 
ATOM   969  N  NE2 . HIS A 1 120 ? 34.391  -3.578  7.728   1.00 10.81 ? 120 HIS A NE2 1 
ATOM   970  N  N   . TYR A 1 121 ? 33.992  2.620   5.374   1.00 11.41 ? 121 TYR A N   1 
ATOM   971  C  CA  . TYR A 1 121 ? 33.936  3.712   4.376   1.00 11.44 ? 121 TYR A CA  1 
ATOM   972  C  C   . TYR A 1 121 ? 34.977  3.503   3.296   1.00 13.18 ? 121 TYR A C   1 
ATOM   973  O  O   . TYR A 1 121 ? 35.975  2.804   3.548   1.00 12.65 ? 121 TYR A O   1 
ATOM   974  C  CB  . TYR A 1 121 ? 34.221  5.077   5.090   1.00 12.57 ? 121 TYR A CB  1 
ATOM   975  C  CG  . TYR A 1 121 ? 35.636  5.253   5.613   1.00 13.90 ? 121 TYR A CG  1 
ATOM   976  C  CD1 . TYR A 1 121 ? 36.598  5.944   4.854   1.00 15.78 ? 121 TYR A CD1 1 
ATOM   977  C  CD2 . TYR A 1 121 ? 35.999  4.744   6.865   1.00 14.97 ? 121 TYR A CD2 1 
ATOM   978  C  CE1 . TYR A 1 121 ? 37.916  6.099   5.345   1.00 15.36 ? 121 TYR A CE1 1 
ATOM   979  C  CE2 . TYR A 1 121 ? 37.322  4.880   7.368   1.00 17.49 ? 121 TYR A CE2 1 
ATOM   980  C  CZ  . TYR A 1 121 ? 38.244  5.534   6.593   1.00 18.50 ? 121 TYR A CZ  1 
ATOM   981  O  OH  . TYR A 1 121 ? 39.573  5.691   7.026   1.00 20.31 ? 121 TYR A OH  1 
ATOM   982  N  N   . ASN A 1 122 ? 34.751  4.117   2.138   1.00 13.49 ? 122 ASN A N   1 
ATOM   983  C  CA  . ASN A 1 122 ? 35.640  3.901   0.956   1.00 12.46 ? 122 ASN A CA  1 
ATOM   984  C  C   . ASN A 1 122 ? 36.913  4.708   1.175   1.00 14.44 ? 122 ASN A C   1 
ATOM   985  O  O   . ASN A 1 122 ? 36.927  5.912   0.963   1.00 13.46 ? 122 ASN A O   1 
ATOM   986  C  CB  . ASN A 1 122 ? 34.903  4.290   -0.319  1.00 12.61 ? 122 ASN A CB  1 
ATOM   987  C  CG  . ASN A 1 122 ? 35.659  3.956   -1.550  1.00 15.79 ? 122 ASN A CG  1 
ATOM   988  O  OD1 . ASN A 1 122 ? 36.937  3.913   -1.531  1.00 15.11 ? 122 ASN A OD1 1 
ATOM   989  N  ND2 . ASN A 1 122 ? 34.938  3.586   -2.604  1.00 14.94 ? 122 ASN A ND2 1 
ATOM   990  N  N   . SER A 1 123 ? 37.957  3.997   1.625   1.00 13.07 ? 123 SER A N   1 
ATOM   991  C  CA  . SER A 1 123 ? 39.162  4.686   2.035   1.00 13.90 ? 123 SER A CA  1 
ATOM   992  C  C   . SER A 1 123 ? 40.096  4.864   0.786   1.00 14.75 ? 123 SER A C   1 
ATOM   993  O  O   . SER A 1 123 ? 41.093  5.643   0.896   1.00 16.49 ? 123 SER A O   1 
ATOM   994  C  CB  . SER A 1 123 ? 39.853  3.868   3.186   1.00 13.54 ? 123 SER A CB  1 
ATOM   995  O  OG  . SER A 1 123 ? 40.045  2.554   2.806   1.00 12.26 ? 123 SER A OG  1 
ATOM   996  N  N   . ASP A 1 124 ? 39.791  4.155   -0.320  1.00 14.39 ? 124 ASP A N   1 
ATOM   997  C  CA  . ASP A 1 124 ? 40.514  4.395   -1.592  1.00 15.12 ? 124 ASP A CA  1 
ATOM   998  C  C   . ASP A 1 124 ? 40.123  5.761   -2.110  1.00 18.43 ? 124 ASP A C   1 
ATOM   999  O  O   . ASP A 1 124 ? 40.959  6.468   -2.721  1.00 20.66 ? 124 ASP A O   1 
ATOM   1000 C  CB  . ASP A 1 124 ? 40.190  3.341   -2.614  1.00 14.57 ? 124 ASP A CB  1 
ATOM   1001 C  CG  . ASP A 1 124 ? 40.798  2.034   -2.303  1.00 15.51 ? 124 ASP A CG  1 
ATOM   1002 O  OD1 . ASP A 1 124 ? 41.849  1.988   -1.581  1.00 16.65 ? 124 ASP A OD1 1 
ATOM   1003 O  OD2 . ASP A 1 124 ? 40.338  1.050   -2.863  1.00 17.15 ? 124 ASP A OD2 1 
ATOM   1004 N  N   . LEU A 1 125 ? 38.872  6.162   -1.912  1.00 16.00 ? 125 LEU A N   1 
ATOM   1005 C  CA  . LEU A 1 125 ? 38.335  7.423   -2.481  1.00 21.06 ? 125 LEU A CA  1 
ATOM   1006 C  C   . LEU A 1 125 ? 38.304  8.578   -1.545  1.00 20.45 ? 125 LEU A C   1 
ATOM   1007 O  O   . LEU A 1 125 ? 38.404  9.740   -2.032  1.00 26.23 ? 125 LEU A O   1 
ATOM   1008 C  CB  . LEU A 1 125 ? 36.940  7.149   -3.073  1.00 23.21 ? 125 LEU A CB  1 
ATOM   1009 C  CG  . LEU A 1 125 ? 36.765  6.482   -4.455  1.00 28.39 ? 125 LEU A CG  1 
ATOM   1010 C  CD1 . LEU A 1 125 ? 37.599  5.238   -4.753  1.00 35.25 ? 125 LEU A CD1 1 
ATOM   1011 C  CD2 . LEU A 1 125 ? 35.300  6.268   -4.805  1.00 29.13 ? 125 LEU A CD2 1 
ATOM   1012 N  N   . TYR A 1 126 ? 38.131  8.322   -0.228  1.00 19.28 ? 126 TYR A N   1 
ATOM   1013 C  CA  . TYR A 1 126 ? 37.911  9.321   0.853   1.00 20.68 ? 126 TYR A CA  1 
ATOM   1014 C  C   . TYR A 1 126 ? 38.817  9.182   2.086   1.00 23.39 ? 126 TYR A C   1 
ATOM   1015 O  O   . TYR A 1 126 ? 39.324  8.057   2.409   1.00 20.54 ? 126 TYR A O   1 
ATOM   1016 C  CB  . TYR A 1 126 ? 36.407  9.329   1.332   1.00 21.86 ? 126 TYR A CB  1 
ATOM   1017 C  CG  . TYR A 1 126 ? 35.489  9.349   0.121   1.00 21.78 ? 126 TYR A CG  1 
ATOM   1018 C  CD1 . TYR A 1 126 ? 35.456  10.466  -0.752  1.00 24.78 ? 126 TYR A CD1 1 
ATOM   1019 C  CD2 . TYR A 1 126 ? 34.676  8.211   -0.217  1.00 24.93 ? 126 TYR A CD2 1 
ATOM   1020 C  CE1 . TYR A 1 126 ? 34.653  10.457  -1.890  1.00 26.02 ? 126 TYR A CE1 1 
ATOM   1021 C  CE2 . TYR A 1 126 ? 33.909  8.169   -1.387  1.00 25.14 ? 126 TYR A CE2 1 
ATOM   1022 C  CZ  . TYR A 1 126 ? 33.885  9.300   -2.215  1.00 28.14 ? 126 TYR A CZ  1 
ATOM   1023 O  OH  . TYR A 1 126 ? 33.117  9.288   -3.338  1.00 26.22 ? 126 TYR A OH  1 
ATOM   1024 N  N   . PRO A 1 127 ? 39.070  10.320  2.788   1.00 23.49 ? 127 PRO A N   1 
ATOM   1025 C  CA  . PRO A 1 127 ? 39.989  10.327  3.918   1.00 24.32 ? 127 PRO A CA  1 
ATOM   1026 C  C   . PRO A 1 127 ? 39.504  9.781   5.214   1.00 24.41 ? 127 PRO A C   1 
ATOM   1027 O  O   . PRO A 1 127 ? 40.310  9.313   6.042   1.00 25.30 ? 127 PRO A O   1 
ATOM   1028 C  CB  . PRO A 1 127 ? 40.338  11.827  4.096   1.00 26.65 ? 127 PRO A CB  1 
ATOM   1029 C  CG  . PRO A 1 127 ? 39.181  12.528  3.504   1.00 23.65 ? 127 PRO A CG  1 
ATOM   1030 C  CD  . PRO A 1 127 ? 38.729  11.694  2.361   1.00 24.73 ? 127 PRO A CD  1 
ATOM   1031 N  N   . ASP A 1 128 ? 38.182  9.826   5.422   1.00 23.19 ? 128 ASP A N   1 
ATOM   1032 C  CA  . ASP A 1 128 ? 37.571  9.309   6.635   1.00 21.22 ? 128 ASP A CA  1 
ATOM   1033 C  C   . ASP A 1 128 ? 36.058  9.112   6.369   1.00 19.55 ? 128 ASP A C   1 
ATOM   1034 O  O   . ASP A 1 128 ? 35.566  9.433   5.277   1.00 18.86 ? 128 ASP A O   1 
ATOM   1035 C  CB  . ASP A 1 128 ? 37.826  10.185  7.864   1.00 27.07 ? 128 ASP A CB  1 
ATOM   1036 C  CG  . ASP A 1 128 ? 37.408  11.613  7.665   1.00 29.23 ? 128 ASP A CG  1 
ATOM   1037 O  OD1 . ASP A 1 128 ? 37.925  12.446  8.469   1.00 32.76 ? 128 ASP A OD1 1 
ATOM   1038 O  OD2 . ASP A 1 128 ? 36.559  11.947  6.784   1.00 28.56 ? 128 ASP A OD2 1 
ATOM   1039 N  N   . ALA A 1 129 ? 35.399  8.521   7.346   1.00 22.35 ? 129 ALA A N   1 
ATOM   1040 C  CA  . ALA A 1 129 ? 34.054  8.085   7.211   1.00 21.80 ? 129 ALA A CA  1 
ATOM   1041 C  C   . ALA A 1 129 ? 33.133  9.266   7.183   1.00 24.01 ? 129 ALA A C   1 
ATOM   1042 O  O   . ALA A 1 129 ? 32.142  9.224   6.451   1.00 20.24 ? 129 ALA A O   1 
ATOM   1043 C  CB  . ALA A 1 129 ? 33.660  7.152   8.353   1.00 24.01 ? 129 ALA A CB  1 
ATOM   1044 N  N   . SER A 1 130 ? 33.438  10.289  7.977   1.00 22.98 ? 130 SER A N   1 
ATOM   1045 C  CA  . SER A 1 130 ? 32.634  11.517  7.958   1.00 26.25 ? 130 SER A CA  1 
ATOM   1046 C  C   . SER A 1 130 ? 32.567  12.073  6.555   1.00 23.91 ? 130 SER A C   1 
ATOM   1047 O  O   . SER A 1 130 ? 31.489  12.397  6.041   1.00 23.84 ? 130 SER A O   1 
ATOM   1048 C  CB  . SER A 1 130 ? 33.248  12.539  8.921   1.00 29.01 ? 130 SER A CB  1 
ATOM   1049 O  OG  . SER A 1 130 ? 32.651  13.810  8.722   1.00 39.84 ? 130 SER A OG  1 
ATOM   1050 N  N   . THR A 1 131 ? 33.708  12.187  5.887   1.00 22.11 ? 131 THR A N   1 
ATOM   1051 C  CA  . THR A 1 131 ? 33.754  12.738  4.571   1.00 20.66 ? 131 THR A CA  1 
ATOM   1052 C  C   . THR A 1 131 ? 33.070  11.798  3.555   1.00 20.62 ? 131 THR A C   1 
ATOM   1053 O  O   . THR A 1 131 ? 32.395  12.256  2.591   1.00 22.50 ? 131 THR A O   1 
ATOM   1054 C  CB  . THR A 1 131 ? 35.224  12.997  4.172   1.00 22.00 ? 131 THR A CB  1 
ATOM   1055 O  OG1 . THR A 1 131 ? 35.793  13.914  5.143   1.00 26.62 ? 131 THR A OG1 1 
ATOM   1056 C  CG2 . THR A 1 131 ? 35.347  13.531  2.795   1.00 22.33 ? 131 THR A CG2 1 
ATOM   1057 N  N   . ALA A 1 132 ? 33.280  10.474  3.698   1.00 18.32 ? 132 ALA A N   1 
ATOM   1058 C  CA  . ALA A 1 132 ? 32.600  9.536   2.761   1.00 16.91 ? 132 ALA A CA  1 
ATOM   1059 C  C   . ALA A 1 132 ? 31.066  9.460   2.861   1.00 15.19 ? 132 ALA A C   1 
ATOM   1060 O  O   . ALA A 1 132 ? 30.456  9.066   1.898   1.00 15.64 ? 132 ALA A O   1 
ATOM   1061 C  CB  . ALA A 1 132 ? 33.132  8.086   2.953   1.00 13.94 ? 132 ALA A CB  1 
ATOM   1062 N  N   . SER A 1 133 ? 30.517  9.829   3.999   1.00 17.52 ? 133 SER A N   1 
ATOM   1063 C  CA  . SER A 1 133 ? 29.170  9.457   4.365   1.00 21.47 ? 133 SER A CA  1 
ATOM   1064 C  C   . SER A 1 133 ? 28.099  9.994   3.388   1.00 21.66 ? 133 SER A C   1 
ATOM   1065 O  O   . SER A 1 133 ? 27.040  9.350   3.256   1.00 18.52 ? 133 SER A O   1 
ATOM   1066 C  CB  . SER A 1 133 ? 28.915  9.882   5.804   1.00 22.48 ? 133 SER A CB  1 
ATOM   1067 O  OG  . SER A 1 133 ? 28.930  11.305  5.865   1.00 25.72 ? 133 SER A OG  1 
ATOM   1068 N  N   . ASN A 1 134 ? 28.394  11.097  2.667   1.00 20.17 ? 134 ASN A N   1 
ATOM   1069 C  CA  . ASN A 1 134 ? 27.494  11.701  1.657   1.00 19.70 ? 134 ASN A CA  1 
ATOM   1070 C  C   . ASN A 1 134 ? 27.983  11.676  0.197   1.00 19.54 ? 134 ASN A C   1 
ATOM   1071 O  O   . ASN A 1 134 ? 27.452  12.349  -0.680  1.00 22.49 ? 134 ASN A O   1 
ATOM   1072 C  CB  . ASN A 1 134 ? 27.083  13.132  2.088   1.00 22.64 ? 134 ASN A CB  1 
ATOM   1073 C  CG  . ASN A 1 134 ? 28.246  14.103  2.037   1.00 29.29 ? 134 ASN A CG  1 
ATOM   1074 O  OD1 . ASN A 1 134 ? 29.410  13.682  2.100   1.00 27.04 ? 134 ASN A OD1 1 
ATOM   1075 N  ND2 . ASN A 1 134 ? 27.939  15.418  1.842   1.00 26.18 ? 134 ASN A ND2 1 
ATOM   1076 N  N   . LYS A 1 135 ? 28.934  10.818  -0.091  1.00 17.06 ? 135 LYS A N   1 
ATOM   1077 C  CA  . LYS A 1 135 ? 29.466  10.615  -1.404  1.00 19.85 ? 135 LYS A CA  1 
ATOM   1078 C  C   . LYS A 1 135 ? 29.159  9.321   -2.047  1.00 20.25 ? 135 LYS A C   1 
ATOM   1079 O  O   . LYS A 1 135 ? 28.929  8.312   -1.359  1.00 18.32 ? 135 LYS A O   1 
ATOM   1080 C  CB  . LYS A 1 135 ? 31.003  10.845  -1.303  1.00 23.83 ? 135 LYS A CB  1 
ATOM   1081 C  CG  . LYS A 1 135 ? 31.250  12.153  -0.544  1.00 25.50 ? 135 LYS A CG  1 
ATOM   1082 C  CD  . LYS A 1 135 ? 32.447  12.947  -1.045  1.00 30.57 ? 135 LYS A CD  1 
ATOM   1083 C  CE  . LYS A 1 135 ? 32.514  14.336  -0.474  1.00 27.86 ? 135 LYS A CE  1 
ATOM   1084 N  NZ  . LYS A 1 135 ? 31.896  14.541  0.863   1.00 26.98 ? 135 LYS A NZ  1 
ATOM   1085 N  N   . SER A 1 136 ? 29.242  9.328   -3.359  1.00 21.69 ? 136 SER A N   1 
ATOM   1086 C  CA  . SER A 1 136 ? 29.003  8.179   -4.218  1.00 27.17 ? 136 SER A CA  1 
ATOM   1087 C  C   . SER A 1 136 ? 29.900  7.050   -3.767  1.00 24.10 ? 136 SER A C   1 
ATOM   1088 O  O   . SER A 1 136 ? 31.100  7.233   -3.668  1.00 25.10 ? 136 SER A O   1 
ATOM   1089 C  CB  . SER A 1 136 ? 29.362  8.550   -5.668  1.00 32.37 ? 136 SER A CB  1 
ATOM   1090 O  OG  . SER A 1 136 ? 29.919  7.470   -6.423  1.00 44.60 ? 136 SER A OG  1 
ATOM   1091 N  N   . GLU A 1 137 ? 29.310  5.873   -3.553  1.00 27.08 ? 137 GLU A N   1 
ATOM   1092 C  CA  . GLU A 1 137 ? 30.123  4.698   -3.200  1.00 23.92 ? 137 GLU A CA  1 
ATOM   1093 C  C   . GLU A 1 137 ? 30.759  4.870   -1.809  1.00 21.64 ? 137 GLU A C   1 
ATOM   1094 O  O   . GLU A 1 137 ? 31.812  4.255   -1.530  1.00 18.78 ? 137 GLU A O   1 
ATOM   1095 C  CB  . GLU A 1 137 ? 31.194  4.375   -4.276  1.00 30.73 ? 137 GLU A CB  1 
ATOM   1096 C  CG  . GLU A 1 137 ? 30.655  4.256   -5.726  1.00 37.51 ? 137 GLU A CG  1 
ATOM   1097 C  CD  . GLU A 1 137 ? 30.145  2.855   -6.117  1.00 51.33 ? 137 GLU A CD  1 
ATOM   1098 O  OE1 . GLU A 1 137 ? 30.950  1.883   -6.070  1.00 55.73 ? 137 GLU A OE1 1 
ATOM   1099 O  OE2 . GLU A 1 137 ? 28.944  2.726   -6.497  1.00 56.22 ? 137 GLU A OE2 1 
ATOM   1100 N  N   . GLY A 1 138 ? 30.205  5.716   -0.948  1.00 15.98 ? 138 GLY A N   1 
ATOM   1101 C  CA  . GLY A 1 138 ? 30.942  6.099   0.220   1.00 14.36 ? 138 GLY A CA  1 
ATOM   1102 C  C   . GLY A 1 138 ? 31.114  5.039   1.307   1.00 12.73 ? 138 GLY A C   1 
ATOM   1103 O  O   . GLY A 1 138 ? 32.139  5.006   1.999   1.00 13.14 ? 138 GLY A O   1 
ATOM   1104 N  N   . LEU A 1 139 ? 30.015  4.285   1.574   1.00 11.99 ? 139 LEU A N   1 
ATOM   1105 C  CA  . LEU A 1 139 ? 29.950  3.419   2.742   1.00 10.32 ? 139 LEU A CA  1 
ATOM   1106 C  C   . LEU A 1 139 ? 29.593  2.006   2.402   1.00 9.35  ? 139 LEU A C   1 
ATOM   1107 O  O   . LEU A 1 139 ? 28.924  1.740   1.412   1.00 10.31 ? 139 LEU A O   1 
ATOM   1108 C  CB  . LEU A 1 139 ? 28.877  3.910   3.782   1.00 10.78 ? 139 LEU A CB  1 
ATOM   1109 C  CG  . LEU A 1 139 ? 29.041  5.413   4.206   1.00 11.92 ? 139 LEU A CG  1 
ATOM   1110 C  CD1 . LEU A 1 139 ? 27.769  5.857   4.969   1.00 12.48 ? 139 LEU A CD1 1 
ATOM   1111 C  CD2 . LEU A 1 139 ? 30.323  5.536   5.051   1.00 14.55 ? 139 LEU A CD2 1 
ATOM   1112 N  N   . ALA A 1 140 ? 30.070  1.079   3.248   1.00 8.79  ? 140 ALA A N   1 
ATOM   1113 C  CA  . ALA A 1 140 ? 29.633  -0.298  3.182   1.00 8.91  ? 140 ALA A CA  1 
ATOM   1114 C  C   . ALA A 1 140 ? 29.394  -0.754  4.580   1.00 8.38  ? 140 ALA A C   1 
ATOM   1115 O  O   . ALA A 1 140 ? 30.247  -0.665  5.415   1.00 10.10 ? 140 ALA A O   1 
ATOM   1116 C  CB  . ALA A 1 140 ? 30.659  -1.170  2.408   1.00 8.96  ? 140 ALA A CB  1 
ATOM   1117 N  N   . VAL A 1 141 ? 28.213  -1.341  4.824   1.00 8.46  ? 141 VAL A N   1 
ATOM   1118 C  CA  . VAL A 1 141 ? 27.868  -1.796  6.143   1.00 7.96  ? 141 VAL A CA  1 
ATOM   1119 C  C   . VAL A 1 141 ? 27.658  -3.298  6.116   1.00 7.94  ? 141 VAL A C   1 
ATOM   1120 O  O   . VAL A 1 141 ? 26.943  -3.784  5.197   1.00 9.47  ? 141 VAL A O   1 
ATOM   1121 C  CB  . VAL A 1 141 ? 26.597  -1.136  6.686   1.00 8.00  ? 141 VAL A CB  1 
ATOM   1122 C  CG1 . VAL A 1 141 ? 26.341  -1.615  8.142   1.00 8.46  ? 141 VAL A CG1 1 
ATOM   1123 C  CG2 . VAL A 1 141 ? 26.802  0.362   6.734   1.00 9.37  ? 141 VAL A CG2 1 
ATOM   1124 N  N   . LEU A 1 142 ? 28.205  -4.042  7.104   1.00 7.91  ? 142 LEU A N   1 
ATOM   1125 C  CA  . LEU A 1 142 ? 27.890  -5.450  7.210   1.00 7.94  ? 142 LEU A CA  1 
ATOM   1126 C  C   . LEU A 1 142 ? 26.836  -5.545  8.326   1.00 8.96  ? 142 LEU A C   1 
ATOM   1127 O  O   . LEU A 1 142 ? 27.002  -4.872  9.415   1.00 10.00 ? 142 LEU A O   1 
ATOM   1128 C  CB  . LEU A 1 142 ? 29.120  -6.205  7.743   1.00 9.30  ? 142 LEU A CB  1 
ATOM   1129 C  CG  . LEU A 1 142 ? 30.352  -6.094  6.832   1.00 8.99  ? 142 LEU A CG  1 
ATOM   1130 C  CD1 . LEU A 1 142 ? 31.494  -6.927  7.471   1.00 10.74 ? 142 LEU A CD1 1 
ATOM   1131 C  CD2 . LEU A 1 142 ? 30.073  -6.620  5.448   1.00 10.13 ? 142 LEU A CD2 1 
ATOM   1132 N  N   . ALA A 1 143 ? 25.802  -6.347  8.096   1.00 7.23  ? 143 ALA A N   1 
ATOM   1133 C  CA  . ALA A 1 143 ? 24.732  -6.473  9.095   1.00 7.50  ? 143 ALA A CA  1 
ATOM   1134 C  C   . ALA A 1 143 ? 24.641  -7.952  9.488   1.00 8.04  ? 143 ALA A C   1 
ATOM   1135 O  O   . ALA A 1 143 ? 24.525  -8.808  8.622   1.00 8.28  ? 143 ALA A O   1 
ATOM   1136 C  CB  . ALA A 1 143 ? 23.394  -6.009  8.504   1.00 8.96  ? 143 ALA A CB  1 
ATOM   1137 N  N   . VAL A 1 144 ? 24.623  -8.178  10.800  1.00 7.90  ? 144 VAL A N   1 
ATOM   1138 C  CA  . VAL A 1 144 ? 24.450  -9.528  11.325  1.00 8.63  ? 144 VAL A CA  1 
ATOM   1139 C  C   . VAL A 1 144 ? 23.121  -9.537  12.114  1.00 9.45  ? 144 VAL A C   1 
ATOM   1140 O  O   . VAL A 1 144 ? 22.888  -8.712  13.014  1.00 9.38  ? 144 VAL A O   1 
ATOM   1141 C  CB  . VAL A 1 144 ? 25.611  -9.830  12.320  1.00 10.05 ? 144 VAL A CB  1 
ATOM   1142 C  CG1 . VAL A 1 144 ? 25.378  -11.266 12.941  1.00 12.55 ? 144 VAL A CG1 1 
ATOM   1143 C  CG2 . VAL A 1 144 ? 27.000  -9.732  11.618  1.00 9.06  ? 144 VAL A CG2 1 
ATOM   1144 N  N   . LEU A 1 145 ? 22.245  -10.459 11.725  1.00 9.62  ? 145 LEU A N   1 
ATOM   1145 C  CA  . LEU A 1 145 ? 20.952  -10.659 12.399  1.00 9.51  ? 145 LEU A CA  1 
ATOM   1146 C  C   . LEU A 1 145 ? 21.235  -11.450 13.683  1.00 9.72  ? 145 LEU A C   1 
ATOM   1147 O  O   . LEU A 1 145 ? 22.025  -12.419 13.652  1.00 10.07 ? 145 LEU A O   1 
ATOM   1148 C  CB  . LEU A 1 145 ? 19.970  -11.399 11.477  1.00 9.48  ? 145 LEU A CB  1 
ATOM   1149 C  CG  . LEU A 1 145 ? 19.695  -10.591 10.189  1.00 11.01 ? 145 LEU A CG  1 
ATOM   1150 C  CD1 . LEU A 1 145 ? 19.077  -11.522 9.145   1.00 11.55 ? 145 LEU A CD1 1 
ATOM   1151 C  CD2 . LEU A 1 145 ? 18.805  -9.382  10.506  1.00 11.95 ? 145 LEU A CD2 1 
ATOM   1152 N  N   . ILE A 1 146 ? 20.570  -11.087 14.782  1.00 8.61  ? 146 ILE A N   1 
ATOM   1153 C  CA  . ILE A 1 146 ? 20.809  -11.745 16.062  1.00 10.71 ? 146 ILE A CA  1 
ATOM   1154 C  C   . ILE A 1 146 ? 19.528  -12.324 16.598  1.00 11.10 ? 146 ILE A C   1 
ATOM   1155 O  O   . ILE A 1 146 ? 18.512  -11.657 16.583  1.00 10.34 ? 146 ILE A O   1 
ATOM   1156 C  CB  . ILE A 1 146 ? 21.330  -10.712 17.104  1.00 10.21 ? 146 ILE A CB  1 
ATOM   1157 C  CG1 . ILE A 1 146 ? 22.690  -10.086 16.662  1.00 11.67 ? 146 ILE A CG1 1 
ATOM   1158 C  CG2 . ILE A 1 146 ? 21.498  -11.382 18.527  1.00 11.92 ? 146 ILE A CG2 1 
ATOM   1159 C  CD1 . ILE A 1 146 ? 23.152  -8.833  17.417  1.00 10.42 ? 146 ILE A CD1 1 
ATOM   1160 N  N   . GLU A 1 147 ? 19.591  -13.579 17.014  1.00 12.14 ? 147 GLU A N   1 
ATOM   1161 C  CA  . GLU A 1 147 ? 18.428  -14.273 17.644  1.00 14.39 ? 147 GLU A CA  1 
ATOM   1162 C  C   . GLU A 1 147 ? 18.810  -14.808 19.015  1.00 13.69 ? 147 GLU A C   1 
ATOM   1163 O  O   . GLU A 1 147 ? 19.990  -14.909 19.356  1.00 12.19 ? 147 GLU A O   1 
ATOM   1164 C  CB  . GLU A 1 147 ? 17.869  -15.380 16.748  1.00 17.57 ? 147 GLU A CB  1 
ATOM   1165 C  CG  . GLU A 1 147 ? 18.760  -16.637 16.675  1.00 17.95 ? 147 GLU A CG  1 
ATOM   1166 C  CD  . GLU A 1 147 ? 18.334  -17.598 15.583  1.00 19.59 ? 147 GLU A CD  1 
ATOM   1167 O  OE1 . GLU A 1 147 ? 17.388  -17.297 14.813  1.00 20.57 ? 147 GLU A OE1 1 
ATOM   1168 O  OE2 . GLU A 1 147 ? 19.001  -18.659 15.393  1.00 23.17 ? 147 GLU A OE2 1 
ATOM   1169 N  N   . MET A 1 148 ? 17.816  -14.969 19.886  1.00 15.12 ? 148 MET A N   1 
ATOM   1170 C  CA  . MET A 1 148 ? 18.102  -15.555 21.191  1.00 17.63 ? 148 MET A CA  1 
ATOM   1171 C  C   . MET A 1 148 ? 18.431  -17.092 21.074  1.00 18.59 ? 148 MET A C   1 
ATOM   1172 O  O   . MET A 1 148 ? 17.814  -17.823 20.339  1.00 20.75 ? 148 MET A O   1 
ATOM   1173 C  CB  . MET A 1 148 ? 16.936  -15.212 22.176  1.00 20.77 ? 148 MET A CB  1 
ATOM   1174 C  CG  . MET A 1 148 ? 17.264  -15.544 23.623  1.00 23.49 ? 148 MET A CG  1 
ATOM   1175 S  SD  . MET A 1 148 ? 16.946  -17.249 24.057  1.00 29.38 ? 148 MET A SD  1 
ATOM   1176 C  CE  . MET A 1 148 ? 15.159  -17.362 23.817  1.00 27.50 ? 148 MET A CE  1 
ATOM   1177 N  N   . GLY A 1 149 ? 19.430  -17.593 21.797  1.00 18.73 ? 149 GLY A N   1 
ATOM   1178 C  CA  . GLY A 1 149 ? 19.745  -19.034 21.767  1.00 19.74 ? 149 GLY A CA  1 
ATOM   1179 C  C   . GLY A 1 149 ? 20.864  -19.262 22.781  1.00 18.51 ? 149 GLY A C   1 
ATOM   1180 O  O   . GLY A 1 149 ? 20.749  -18.796 23.927  1.00 19.74 ? 149 GLY A O   1 
ATOM   1181 N  N   A SER A 1 150 ? 21.970  -19.852 22.337  0.50 19.71 ? 150 SER A N   1 
ATOM   1182 N  N   B SER A 1 150 ? 21.930  -19.965 22.392  0.50 19.28 ? 150 SER A N   1 
ATOM   1183 C  CA  A SER A 1 150 ? 23.121  -20.083 23.216  0.50 18.37 ? 150 SER A CA  1 
ATOM   1184 C  CA  B SER A 1 150 ? 23.049  -20.242 23.325  0.50 17.80 ? 150 SER A CA  1 
ATOM   1185 C  C   A SER A 1 150 ? 23.855  -18.832 23.634  0.50 19.15 ? 150 SER A C   1 
ATOM   1186 C  C   B SER A 1 150 ? 23.892  -19.002 23.592  0.50 18.53 ? 150 SER A C   1 
ATOM   1187 O  O   A SER A 1 150 ? 23.889  -17.832 22.931  0.50 17.69 ? 150 SER A O   1 
ATOM   1188 O  O   B SER A 1 150 ? 24.015  -18.164 22.698  0.50 17.46 ? 150 SER A O   1 
ATOM   1189 C  CB  A SER A 1 150 ? 24.106  -21.041 22.538  0.50 21.39 ? 150 SER A CB  1 
ATOM   1190 C  CB  B SER A 1 150 ? 23.941  -21.350 22.745  0.50 20.01 ? 150 SER A CB  1 
ATOM   1191 O  OG  A SER A 1 150 ? 23.382  -22.174 22.116  0.50 21.98 ? 150 SER A OG  1 
ATOM   1192 O  OG  B SER A 1 150 ? 24.369  -20.986 21.438  0.50 18.70 ? 150 SER A OG  1 
ATOM   1193 N  N   . PHE A 1 151 ? 24.443  -18.880 24.809  1.00 15.81 ? 151 PHE A N   1 
ATOM   1194 C  CA  . PHE A 1 151 ? 25.344  -17.838 25.225  1.00 17.17 ? 151 PHE A CA  1 
ATOM   1195 C  C   . PHE A 1 151 ? 26.485  -17.692 24.220  1.00 15.97 ? 151 PHE A C   1 
ATOM   1196 O  O   . PHE A 1 151 ? 27.078  -18.710 23.762  1.00 18.99 ? 151 PHE A O   1 
ATOM   1197 C  CB  . PHE A 1 151 ? 25.928  -18.215 26.626  1.00 16.01 ? 151 PHE A CB  1 
ATOM   1198 C  CG  . PHE A 1 151 ? 26.910  -17.234 27.137  1.00 16.33 ? 151 PHE A CG  1 
ATOM   1199 C  CD1 . PHE A 1 151 ? 26.535  -16.035 27.703  1.00 17.29 ? 151 PHE A CD1 1 
ATOM   1200 C  CD2 . PHE A 1 151 ? 28.278  -17.491 27.009  1.00 18.56 ? 151 PHE A CD2 1 
ATOM   1201 C  CE1 . PHE A 1 151 ? 27.478  -15.082 28.102  1.00 17.30 ? 151 PHE A CE1 1 
ATOM   1202 C  CE2 . PHE A 1 151 ? 29.199  -16.571 27.425  1.00 16.57 ? 151 PHE A CE2 1 
ATOM   1203 C  CZ  . PHE A 1 151 ? 28.841  -15.368 27.943  1.00 16.19 ? 151 PHE A CZ  1 
ATOM   1204 N  N   . ASN A 1 152 ? 26.782  -16.438 23.883  1.00 16.47 ? 152 ASN A N   1 
ATOM   1205 C  CA  . ASN A 1 152 ? 27.884  -16.115 22.992  1.00 15.75 ? 152 ASN A CA  1 
ATOM   1206 C  C   . ASN A 1 152 ? 29.034  -15.384 23.673  1.00 16.56 ? 152 ASN A C   1 
ATOM   1207 O  O   . ASN A 1 152 ? 29.005  -14.171 23.989  1.00 15.71 ? 152 ASN A O   1 
ATOM   1208 C  CB  . ASN A 1 152 ? 27.213  -15.312 21.834  1.00 14.41 ? 152 ASN A CB  1 
ATOM   1209 C  CG  . ASN A 1 152 ? 28.119  -15.137 20.643  1.00 14.30 ? 152 ASN A CG  1 
ATOM   1210 O  OD1 . ASN A 1 152 ? 29.294  -14.740 20.777  1.00 14.73 ? 152 ASN A OD1 1 
ATOM   1211 N  ND2 . ASN A 1 152 ? 27.560  -15.408 19.479  1.00 15.93 ? 152 ASN A ND2 1 
ATOM   1212 N  N   . PRO A 1 153 ? 30.152  -16.110 23.926  1.00 18.79 ? 153 PRO A N   1 
ATOM   1213 C  CA  . PRO A 1 153 ? 31.273  -15.431 24.554  1.00 18.19 ? 153 PRO A CA  1 
ATOM   1214 C  C   . PRO A 1 153 ? 31.813  -14.250 23.741  1.00 17.57 ? 153 PRO A C   1 
ATOM   1215 O  O   . PRO A 1 153 ? 32.287  -13.232 24.278  1.00 18.95 ? 153 PRO A O   1 
ATOM   1216 C  CB  . PRO A 1 153 ? 32.354  -16.564 24.739  1.00 19.50 ? 153 PRO A CB  1 
ATOM   1217 C  CG  . PRO A 1 153 ? 31.661  -17.840 24.382  1.00 20.79 ? 153 PRO A CG  1 
ATOM   1218 C  CD  . PRO A 1 153 ? 30.356  -17.550 23.667  1.00 18.18 ? 153 PRO A CD  1 
ATOM   1219 N  N   . SER A 1 154 ? 31.715  -14.361 22.418  1.00 15.89 ? 154 SER A N   1 
ATOM   1220 C  CA  . SER A 1 154 ? 32.359  -13.286 21.640  1.00 15.80 ? 154 SER A CA  1 
ATOM   1221 C  C   . SER A 1 154 ? 31.549  -12.029 21.787  1.00 14.33 ? 154 SER A C   1 
ATOM   1222 O  O   . SER A 1 154 ? 32.118  -10.959 21.944  1.00 14.91 ? 154 SER A O   1 
ATOM   1223 C  CB  . SER A 1 154 ? 32.498  -13.687 20.203  1.00 16.81 ? 154 SER A CB  1 
ATOM   1224 O  OG  . SER A 1 154 ? 33.314  -14.846 20.131  1.00 19.58 ? 154 SER A OG  1 
ATOM   1225 N  N   . TYR A 1 155 ? 30.209  -12.156 21.740  1.00 13.47 ? 155 TYR A N   1 
ATOM   1226 C  CA  . TYR A 1 155 ? 29.413  -10.888 21.993  1.00 13.82 ? 155 TYR A CA  1 
ATOM   1227 C  C   . TYR A 1 155 ? 29.587  -10.381 23.401  1.00 16.59 ? 155 TYR A C   1 
ATOM   1228 O  O   . TYR A 1 155 ? 29.485  -9.170  23.649  1.00 16.63 ? 155 TYR A O   1 
ATOM   1229 C  CB  . TYR A 1 155 ? 27.917  -11.059 21.659  1.00 12.49 ? 155 TYR A CB  1 
ATOM   1230 C  CG  . TYR A 1 155 ? 27.689  -10.901 20.149  1.00 12.55 ? 155 TYR A CG  1 
ATOM   1231 C  CD1 . TYR A 1 155 ? 27.102  -9.734  19.663  1.00 13.18 ? 155 TYR A CD1 1 
ATOM   1232 C  CD2 . TYR A 1 155 ? 28.076  -11.868 19.253  1.00 12.47 ? 155 TYR A CD2 1 
ATOM   1233 C  CE1 . TYR A 1 155 ? 26.919  -9.560  18.295  1.00 11.40 ? 155 TYR A CE1 1 
ATOM   1234 C  CE2 . TYR A 1 155 ? 27.866  -11.713 17.850  1.00 13.23 ? 155 TYR A CE2 1 
ATOM   1235 C  CZ  . TYR A 1 155 ? 27.354  -10.491 17.411  1.00 12.41 ? 155 TYR A CZ  1 
ATOM   1236 O  OH  . TYR A 1 155 ? 27.075  -10.364 16.044  1.00 11.72 ? 155 TYR A OH  1 
ATOM   1237 N  N   . ASP A 1 156 ? 29.939  -11.313 24.305  1.00 16.33 ? 156 ASP A N   1 
ATOM   1238 C  CA  . ASP A 1 156 ? 30.153  -10.832 25.649  1.00 17.12 ? 156 ASP A CA  1 
ATOM   1239 C  C   . ASP A 1 156 ? 31.417  -9.984  25.853  1.00 17.19 ? 156 ASP A C   1 
ATOM   1240 O  O   . ASP A 1 156 ? 31.489  -9.181  26.823  1.00 17.19 ? 156 ASP A O   1 
ATOM   1241 C  CB  . ASP A 1 156 ? 29.997  -11.960 26.673  1.00 20.39 ? 156 ASP A CB  1 
ATOM   1242 C  CG  . ASP A 1 156 ? 29.007  -11.563 27.801  1.00 23.44 ? 156 ASP A CG  1 
ATOM   1243 O  OD1 . ASP A 1 156 ? 27.871  -11.065 27.510  1.00 20.47 ? 156 ASP A OD1 1 
ATOM   1244 O  OD2 . ASP A 1 156 ? 29.338  -11.754 28.996  1.00 23.93 ? 156 ASP A OD2 1 
ATOM   1245 N  N   . LYS A 1 157 ? 32.328  -10.014 24.881  1.00 15.75 ? 157 LYS A N   1 
ATOM   1246 C  CA  . LYS A 1 157 ? 33.505  -9.163  24.926  1.00 17.27 ? 157 LYS A CA  1 
ATOM   1247 C  C   . LYS A 1 157 ? 33.093  -7.685  24.789  1.00 17.95 ? 157 LYS A C   1 
ATOM   1248 O  O   . LYS A 1 157 ? 33.792  -6.779  25.276  1.00 21.12 ? 157 LYS A O   1 
ATOM   1249 C  CB  . LYS A 1 157 ? 34.595  -9.554  23.913  1.00 17.21 ? 157 LYS A CB  1 
ATOM   1250 C  CG  . LYS A 1 157 ? 35.108  -10.991 24.182  1.00 18.30 ? 157 LYS A CG  1 
ATOM   1251 C  CD  . LYS A 1 157 ? 35.910  -11.544 22.989  1.00 17.66 ? 157 LYS A CD  1 
ATOM   1252 C  CE  . LYS A 1 157 ? 36.360  -12.987 23.214  1.00 20.02 ? 157 LYS A CE  1 
ATOM   1253 N  NZ  . LYS A 1 157 ? 37.372  -13.388 22.220  1.00 21.79 ? 157 LYS A NZ  1 
ATOM   1254 N  N   . ILE A 1 158 ? 31.959  -7.457  24.106  1.00 16.81 ? 158 ILE A N   1 
ATOM   1255 C  CA  . ILE A 1 158 ? 31.326  -6.107  24.115  1.00 16.98 ? 158 ILE A CA  1 
ATOM   1256 C  C   . ILE A 1 158 ? 30.386  -5.934  25.296  1.00 17.12 ? 158 ILE A C   1 
ATOM   1257 O  O   . ILE A 1 158 ? 30.519  -4.960  26.036  1.00 17.93 ? 158 ILE A O   1 
ATOM   1258 C  CB  . ILE A 1 158 ? 30.525  -5.776  22.829  1.00 17.00 ? 158 ILE A CB  1 
ATOM   1259 C  CG1 . ILE A 1 158 ? 31.460  -5.880  21.643  1.00 19.97 ? 158 ILE A CG1 1 
ATOM   1260 C  CG2 . ILE A 1 158 ? 29.928  -4.343  22.868  1.00 17.20 ? 158 ILE A CG2 1 
ATOM   1261 C  CD1 . ILE A 1 158 ? 30.756  -5.878  20.291  1.00 19.01 ? 158 ILE A CD1 1 
ATOM   1262 N  N   . PHE A 1 159 ? 29.423  -6.840  25.461  1.00 16.70 ? 159 PHE A N   1 
ATOM   1263 C  CA  . PHE A 1 159 ? 28.364  -6.642  26.429  1.00 16.82 ? 159 PHE A CA  1 
ATOM   1264 C  C   . PHE A 1 159 ? 28.842  -6.502  27.880  1.00 18.52 ? 159 PHE A C   1 
ATOM   1265 O  O   . PHE A 1 159 ? 28.241  -5.759  28.630  1.00 19.54 ? 159 PHE A O   1 
ATOM   1266 C  CB  . PHE A 1 159 ? 27.289  -7.694  26.390  1.00 15.73 ? 159 PHE A CB  1 
ATOM   1267 C  CG  . PHE A 1 159 ? 26.563  -7.844  25.048  1.00 19.82 ? 159 PHE A CG  1 
ATOM   1268 C  CD1 . PHE A 1 159 ? 26.477  -6.809  24.139  1.00 16.38 ? 159 PHE A CD1 1 
ATOM   1269 C  CD2 . PHE A 1 159 ? 25.962  -9.052  24.734  1.00 18.81 ? 159 PHE A CD2 1 
ATOM   1270 C  CE1 . PHE A 1 159 ? 25.778  -6.974  22.931  1.00 15.54 ? 159 PHE A CE1 1 
ATOM   1271 C  CE2 . PHE A 1 159 ? 25.257  -9.240  23.559  1.00 19.45 ? 159 PHE A CE2 1 
ATOM   1272 C  CZ  . PHE A 1 159 ? 25.157  -8.190  22.651  1.00 17.37 ? 159 PHE A CZ  1 
ATOM   1273 N  N   . SER A 1 160 ? 29.925  -7.181  28.238  1.00 20.08 ? 160 SER A N   1 
ATOM   1274 C  CA  . SER A 1 160 ? 30.433  -7.034  29.641  1.00 21.78 ? 160 SER A CA  1 
ATOM   1275 C  C   . SER A 1 160 ? 30.817  -5.597  30.006  1.00 24.20 ? 160 SER A C   1 
ATOM   1276 O  O   . SER A 1 160 ? 31.040  -5.304  31.178  1.00 24.43 ? 160 SER A O   1 
ATOM   1277 C  CB  . SER A 1 160 ? 31.608  -7.979  29.890  1.00 21.58 ? 160 SER A CB  1 
ATOM   1278 O  OG  . SER A 1 160 ? 32.732  -7.648  29.108  1.00 22.58 ? 160 SER A OG  1 
ATOM   1279 N  N   . HIS A 1 161 ? 30.990  -4.705  29.017  1.00 19.88 ? 161 HIS A N   1 
ATOM   1280 C  CA  . HIS A 1 161 ? 31.290  -3.335  29.320  1.00 19.84 ? 161 HIS A CA  1 
ATOM   1281 C  C   . HIS A 1 161 ? 30.094  -2.435  29.368  1.00 20.47 ? 161 HIS A C   1 
ATOM   1282 O  O   . HIS A 1 161 ? 30.288  -1.237  29.609  1.00 18.54 ? 161 HIS A O   1 
ATOM   1283 C  CB  . HIS A 1 161 ? 32.335  -2.758  28.335  1.00 22.38 ? 161 HIS A CB  1 
ATOM   1284 C  CG  . HIS A 1 161 ? 33.633  -3.503  28.312  1.00 22.97 ? 161 HIS A CG  1 
ATOM   1285 N  ND1 . HIS A 1 161 ? 34.671  -3.163  29.103  1.00 26.33 ? 161 HIS A ND1 1 
ATOM   1286 C  CD2 . HIS A 1 161 ? 34.042  -4.622  27.569  1.00 24.74 ? 161 HIS A CD2 1 
ATOM   1287 C  CE1 . HIS A 1 161 ? 35.716  -3.991  28.874  1.00 27.91 ? 161 HIS A CE1 1 
ATOM   1288 N  NE2 . HIS A 1 161 ? 35.332  -4.901  27.928  1.00 24.36 ? 161 HIS A NE2 1 
ATOM   1289 N  N   . LEU A 1 162 ? 28.891  -2.938  29.054  1.00 17.81 ? 162 LEU A N   1 
ATOM   1290 C  CA  . LEU A 1 162 ? 27.730  -2.042  28.953  1.00 18.62 ? 162 LEU A CA  1 
ATOM   1291 C  C   . LEU A 1 162 ? 27.474  -1.200  30.244  1.00 19.98 ? 162 LEU A C   1 
ATOM   1292 O  O   . LEU A 1 162 ? 27.083  -0.021  30.144  1.00 19.04 ? 162 LEU A O   1 
ATOM   1293 C  CB  . LEU A 1 162 ? 26.427  -2.783  28.574  1.00 17.98 ? 162 LEU A CB  1 
ATOM   1294 C  CG  . LEU A 1 162 ? 26.488  -3.423  27.165  1.00 20.76 ? 162 LEU A CG  1 
ATOM   1295 C  CD1 . LEU A 1 162 ? 25.309  -4.383  26.963  1.00 20.39 ? 162 LEU A CD1 1 
ATOM   1296 C  CD2 . LEU A 1 162 ? 26.569  -2.357  26.086  1.00 23.21 ? 162 LEU A CD2 1 
ATOM   1297 N  N   . GLN A 1 163 ? 27.729  -1.782  31.432  1.00 22.51 ? 163 GLN A N   1 
ATOM   1298 C  CA  . GLN A 1 163 ? 27.423  -0.997  32.634  1.00 23.23 ? 163 GLN A CA  1 
ATOM   1299 C  C   . GLN A 1 163 ? 28.229  0.288   32.729  1.00 25.82 ? 163 GLN A C   1 
ATOM   1300 O  O   . GLN A 1 163 ? 27.722  1.272   33.240  1.00 30.82 ? 163 GLN A O   1 
ATOM   1301 C  CB  . GLN A 1 163 ? 27.500  -1.795  33.957  1.00 31.18 ? 163 GLN A CB  1 
ATOM   1302 C  CG  . GLN A 1 163 ? 28.374  -3.056  33.904  1.00 36.54 ? 163 GLN A CG  1 
ATOM   1303 C  CD  . GLN A 1 163 ? 29.828  -2.852  34.317  1.00 45.59 ? 163 GLN A CD  1 
ATOM   1304 O  OE1 . GLN A 1 163 ? 30.710  -2.720  33.452  1.00 48.18 ? 163 GLN A OE1 1 
ATOM   1305 N  NE2 . GLN A 1 163 ? 30.099  -2.859  35.656  1.00 39.46 ? 163 GLN A NE2 1 
ATOM   1306 N  N   . HIS A 1 164 ? 29.420  0.322   32.128  1.00 22.21 ? 164 HIS A N   1 
ATOM   1307 C  CA  . HIS A 1 164 ? 30.255  1.525   32.148  1.00 21.71 ? 164 HIS A CA  1 
ATOM   1308 C  C   . HIS A 1 164 ? 29.856  2.515   31.154  1.00 20.47 ? 164 HIS A C   1 
ATOM   1309 O  O   . HIS A 1 164 ? 30.400  3.617   31.189  1.00 21.60 ? 164 HIS A O   1 
ATOM   1310 C  CB  . HIS A 1 164 ? 31.764  1.224   31.938  1.00 19.47 ? 164 HIS A CB  1 
ATOM   1311 C  CG  . HIS A 1 164 ? 32.399  0.303   32.989  1.00 21.05 ? 164 HIS A CG  1 
ATOM   1312 N  ND1 . HIS A 1 164 ? 32.158  0.408   34.323  1.00 20.09 ? 164 HIS A ND1 1 
ATOM   1313 C  CD2 . HIS A 1 164 ? 33.284  -0.770  32.828  1.00 23.70 ? 164 HIS A CD2 1 
ATOM   1314 C  CE1 . HIS A 1 164 ? 32.820  -0.587  34.972  1.00 20.72 ? 164 HIS A CE1 1 
ATOM   1315 N  NE2 . HIS A 1 164 ? 33.526  -1.283  34.057  1.00 29.19 ? 164 HIS A NE2 1 
ATOM   1316 N  N   . VAL A 1 165 ? 28.945  2.168   30.210  1.00 19.01 ? 165 VAL A N   1 
ATOM   1317 C  CA  . VAL A 1 165 ? 28.366  3.201   29.269  1.00 18.77 ? 165 VAL A CA  1 
ATOM   1318 C  C   . VAL A 1 165 ? 26.870  3.376   29.382  1.00 19.57 ? 165 VAL A C   1 
ATOM   1319 O  O   . VAL A 1 165 ? 26.203  3.749   28.401  1.00 19.18 ? 165 VAL A O   1 
ATOM   1320 C  CB  . VAL A 1 165 ? 28.791  2.951   27.803  1.00 18.05 ? 165 VAL A CB  1 
ATOM   1321 C  CG1 . VAL A 1 165 ? 30.320  3.114   27.725  1.00 19.21 ? 165 VAL A CG1 1 
ATOM   1322 C  CG2 . VAL A 1 165 ? 28.445  1.524   27.346  1.00 17.42 ? 165 VAL A CG2 1 
ATOM   1323 N  N   . LYS A 1 166 ? 26.349  3.204   30.598  1.00 20.35 ? 166 LYS A N   1 
ATOM   1324 C  CA  . LYS A 1 166 ? 24.915  3.371   30.881  1.00 18.65 ? 166 LYS A CA  1 
ATOM   1325 C  C   . LYS A 1 166 ? 24.241  4.633   30.328  1.00 17.60 ? 166 LYS A C   1 
ATOM   1326 O  O   . LYS A 1 166 ? 23.131  4.561   29.762  1.00 18.00 ? 166 LYS A O   1 
ATOM   1327 C  CB  . LYS A 1 166 ? 24.625  3.256   32.393  1.00 24.30 ? 166 LYS A CB  1 
ATOM   1328 C  CG  . LYS A 1 166 ? 24.672  1.811   32.855  1.00 30.57 ? 166 LYS A CG  1 
ATOM   1329 C  CD  . LYS A 1 166 ? 24.027  1.639   34.236  1.00 31.31 ? 166 LYS A CD  1 
ATOM   1330 C  CE  . LYS A 1 166 ? 22.995  2.729   34.530  1.00 32.67 ? 166 LYS A CE  1 
ATOM   1331 N  NZ  . LYS A 1 166 ? 21.569  2.259   34.443  1.00 39.94 ? 166 LYS A NZ  1 
ATOM   1332 N  N   . TYR A 1 167 ? 24.927  5.813   30.464  1.00 17.33 ? 167 TYR A N   1 
ATOM   1333 C  CA  . TYR A 1 167 ? 24.286  7.090   30.094  1.00 17.53 ? 167 TYR A CA  1 
ATOM   1334 C  C   . TYR A 1 167 ? 24.939  7.747   28.925  1.00 15.92 ? 167 TYR A C   1 
ATOM   1335 O  O   . TYR A 1 167 ? 26.152  7.563   28.653  1.00 18.42 ? 167 TYR A O   1 
ATOM   1336 C  CB  . TYR A 1 167 ? 24.338  8.083   31.271  1.00 16.39 ? 167 TYR A CB  1 
ATOM   1337 C  CG  . TYR A 1 167 ? 23.639  7.490   32.489  1.00 15.97 ? 167 TYR A CG  1 
ATOM   1338 C  CD1 . TYR A 1 167 ? 22.258  7.518   32.594  1.00 18.52 ? 167 TYR A CD1 1 
ATOM   1339 C  CD2 . TYR A 1 167 ? 24.383  6.834   33.501  1.00 14.87 ? 167 TYR A CD2 1 
ATOM   1340 C  CE1 . TYR A 1 167 ? 21.629  6.992   33.708  1.00 19.26 ? 167 TYR A CE1 1 
ATOM   1341 C  CE2 . TYR A 1 167 ? 23.761  6.255   34.609  1.00 19.01 ? 167 TYR A CE2 1 
ATOM   1342 C  CZ  . TYR A 1 167 ? 22.387  6.368   34.707  1.00 20.18 ? 167 TYR A CZ  1 
ATOM   1343 O  OH  . TYR A 1 167 ? 21.768  5.845   35.808  1.00 23.23 ? 167 TYR A OH  1 
ATOM   1344 N  N   . LYS A 1 168 ? 24.183  8.645   28.307  1.00 18.31 ? 168 LYS A N   1 
ATOM   1345 C  CA  . LYS A 1 168 ? 24.704  9.333   27.160  1.00 18.48 ? 168 LYS A CA  1 
ATOM   1346 C  C   . LYS A 1 168 ? 26.031  10.035  27.448  1.00 20.77 ? 168 LYS A C   1 
ATOM   1347 O  O   . LYS A 1 168 ? 26.159  10.705  28.472  1.00 20.75 ? 168 LYS A O   1 
ATOM   1348 C  CB  . LYS A 1 168 ? 23.630  10.304  26.620  1.00 18.43 ? 168 LYS A CB  1 
ATOM   1349 C  CG  . LYS A 1 168 ? 24.146  11.141  25.453  1.00 23.28 ? 168 LYS A CG  1 
ATOM   1350 C  CD  . LYS A 1 168 ? 23.035  12.029  24.866  1.00 24.60 ? 168 LYS A CD  1 
ATOM   1351 C  CE  . LYS A 1 168 ? 23.570  12.813  23.679  1.00 28.37 ? 168 LYS A CE  1 
ATOM   1352 N  NZ  . LYS A 1 168 ? 22.511  13.722  23.135  1.00 33.95 ? 168 LYS A NZ  1 
ATOM   1353 N  N   . GLY A 1 169 ? 27.026  9.845   26.591  1.00 20.17 ? 169 GLY A N   1 
ATOM   1354 C  CA  . GLY A 1 169 ? 28.265  10.570  26.700  1.00 20.60 ? 169 GLY A CA  1 
ATOM   1355 C  C   . GLY A 1 169 ? 29.262  9.779   27.478  1.00 21.64 ? 169 GLY A C   1 
ATOM   1356 O  O   . GLY A 1 169 ? 30.427  10.146  27.470  1.00 28.02 ? 169 GLY A O   1 
ATOM   1357 N  N   . GLN A 1 170 ? 28.822  8.696   28.123  1.00 18.98 ? 170 GLN A N   1 
ATOM   1358 C  CA  . GLN A 1 170 ? 29.797  7.807   28.812  1.00 18.07 ? 170 GLN A CA  1 
ATOM   1359 C  C   . GLN A 1 170 ? 30.597  6.961   27.844  1.00 20.71 ? 170 GLN A C   1 
ATOM   1360 O  O   . GLN A 1 170 ? 30.084  6.622   26.757  1.00 19.02 ? 170 GLN A O   1 
ATOM   1361 C  CB  . GLN A 1 170 ? 29.095  6.928   29.858  1.00 18.35 ? 170 GLN A CB  1 
ATOM   1362 C  CG  . GLN A 1 170 ? 28.642  7.756   31.049  1.00 20.90 ? 170 GLN A CG  1 
ATOM   1363 C  CD  . GLN A 1 170 ? 28.036  6.960   32.177  1.00 21.52 ? 170 GLN A CD  1 
ATOM   1364 O  OE1 . GLN A 1 170 ? 27.512  5.833   32.002  1.00 21.26 ? 170 GLN A OE1 1 
ATOM   1365 N  NE2 . GLN A 1 170 ? 28.189  7.495   33.399  1.00 20.26 ? 170 GLN A NE2 1 
ATOM   1366 N  N   . GLU A 1 171 ? 31.867  6.686   28.197  1.00 20.00 ? 171 GLU A N   1 
ATOM   1367 C  CA  . GLU A 1 171 ? 32.826  5.893   27.423  1.00 18.63 ? 171 GLU A CA  1 
ATOM   1368 C  C   . GLU A 1 171 ? 33.569  4.817   28.219  1.00 20.41 ? 171 GLU A C   1 
ATOM   1369 O  O   . GLU A 1 171 ? 33.746  4.924   29.460  1.00 20.98 ? 171 GLU A O   1 
ATOM   1370 C  CB  . GLU A 1 171 ? 33.836  6.844   26.745  1.00 23.79 ? 171 GLU A CB  1 
ATOM   1371 C  CG  . GLU A 1 171 ? 33.164  8.058   26.100  1.00 27.65 ? 171 GLU A CG  1 
ATOM   1372 C  CD  . GLU A 1 171 ? 34.095  9.127   25.489  1.00 34.65 ? 171 GLU A CD  1 
ATOM   1373 O  OE1 . GLU A 1 171 ? 35.360  9.148   25.719  1.00 32.31 ? 171 GLU A OE1 1 
ATOM   1374 O  OE2 . GLU A 1 171 ? 33.511  9.961   24.734  1.00 33.77 ? 171 GLU A OE2 1 
ATOM   1375 N  N   . ALA A 1 172 ? 34.033  3.780   27.543  1.00 20.20 ? 172 ALA A N   1 
ATOM   1376 C  CA  . ALA A 1 172 ? 34.826  2.736   28.190  1.00 20.10 ? 172 ALA A CA  1 
ATOM   1377 C  C   . ALA A 1 172 ? 35.820  2.268   27.163  1.00 26.32 ? 172 ALA A C   1 
ATOM   1378 O  O   . ALA A 1 172 ? 35.618  2.453   25.958  1.00 26.60 ? 172 ALA A O   1 
ATOM   1379 C  CB  . ALA A 1 172 ? 33.921  1.587   28.674  1.00 20.01 ? 172 ALA A CB  1 
ATOM   1380 N  N   . PHE A 1 173 ? 36.871  1.632   27.641  1.00 22.20 ? 173 PHE A N   1 
ATOM   1381 C  CA  . PHE A 1 173 ? 37.874  1.056   26.779  1.00 25.68 ? 173 PHE A CA  1 
ATOM   1382 C  C   . PHE A 1 173 ? 37.738  -0.440  26.635  1.00 24.33 ? 173 PHE A C   1 
ATOM   1383 O  O   . PHE A 1 173 ? 37.579  -1.167  27.627  1.00 27.04 ? 173 PHE A O   1 
ATOM   1384 C  CB  . PHE A 1 173 ? 39.275  1.527   27.214  1.00 22.56 ? 173 PHE A CB  1 
ATOM   1385 C  CG  . PHE A 1 173 ? 39.614  2.889   26.656  1.00 27.69 ? 173 PHE A CG  1 
ATOM   1386 C  CD1 . PHE A 1 173 ? 39.812  3.053   25.286  1.00 27.43 ? 173 PHE A CD1 1 
ATOM   1387 C  CD2 . PHE A 1 173 ? 39.660  3.999   27.479  1.00 32.54 ? 173 PHE A CD2 1 
ATOM   1388 C  CE1 . PHE A 1 173 ? 40.087  4.302   24.732  1.00 29.29 ? 173 PHE A CE1 1 
ATOM   1389 C  CE2 . PHE A 1 173 ? 39.951  5.262   26.946  1.00 31.71 ? 173 PHE A CE2 1 
ATOM   1390 C  CZ  . PHE A 1 173 ? 40.165  5.411   25.571  1.00 32.52 ? 173 PHE A CZ  1 
ATOM   1391 N  N   . VAL A 1 174 ? 37.771  -0.906  25.387  1.00 21.00 ? 174 VAL A N   1 
ATOM   1392 C  CA  . VAL A 1 174 ? 37.625  -2.338  25.154  1.00 20.54 ? 174 VAL A CA  1 
ATOM   1393 C  C   . VAL A 1 174 ? 38.872  -2.915  24.530  1.00 22.62 ? 174 VAL A C   1 
ATOM   1394 O  O   . VAL A 1 174 ? 39.299  -2.391  23.514  1.00 23.98 ? 174 VAL A O   1 
ATOM   1395 C  CB  . VAL A 1 174 ? 36.395  -2.572  24.218  1.00 19.69 ? 174 VAL A CB  1 
ATOM   1396 C  CG1 . VAL A 1 174 ? 36.286  -4.045  23.859  1.00 18.27 ? 174 VAL A CG1 1 
ATOM   1397 C  CG2 . VAL A 1 174 ? 35.112  -2.004  24.858  1.00 18.90 ? 174 VAL A CG2 1 
ATOM   1398 N  N   . PRO A 1 175 ? 39.463  -3.985  25.144  1.00 21.59 ? 175 PRO A N   1 
ATOM   1399 C  CA  . PRO A 1 175 ? 40.721  -4.511  24.629  1.00 23.98 ? 175 PRO A CA  1 
ATOM   1400 C  C   . PRO A 1 175 ? 40.428  -5.207  23.309  1.00 20.12 ? 175 PRO A C   1 
ATOM   1401 O  O   . PRO A 1 175 ? 39.348  -5.763  23.170  1.00 20.23 ? 175 PRO A O   1 
ATOM   1402 C  CB  . PRO A 1 175 ? 41.154  -5.566  25.701  1.00 25.00 ? 175 PRO A CB  1 
ATOM   1403 C  CG  . PRO A 1 175 ? 40.257  -5.313  26.879  1.00 25.56 ? 175 PRO A CG  1 
ATOM   1404 C  CD  . PRO A 1 175 ? 38.972  -4.780  26.275  1.00 23.75 ? 175 PRO A CD  1 
ATOM   1405 N  N   . GLY A 1 176 ? 41.385  -5.165  22.384  1.00 21.17 ? 176 GLY A N   1 
ATOM   1406 C  CA  . GLY A 1 176 ? 41.250  -5.791  21.090  1.00 18.49 ? 176 GLY A CA  1 
ATOM   1407 C  C   . GLY A 1 176 ? 40.880  -7.227  21.181  1.00 20.48 ? 176 GLY A C   1 
ATOM   1408 O  O   . GLY A 1 176 ? 41.447  -7.978  21.990  1.00 24.70 ? 176 GLY A O   1 
ATOM   1409 N  N   . PHE A 1 177 ? 39.868  -7.605  20.382  1.00 18.37 ? 177 PHE A N   1 
ATOM   1410 C  CA  . PHE A 1 177 ? 39.536  -8.971  20.127  1.00 16.22 ? 177 PHE A CA  1 
ATOM   1411 C  C   . PHE A 1 177 ? 39.197  -9.211  18.647  1.00 15.64 ? 177 PHE A C   1 
ATOM   1412 O  O   . PHE A 1 177 ? 39.218  -8.280  17.863  1.00 16.08 ? 177 PHE A O   1 
ATOM   1413 C  CB  . PHE A 1 177 ? 38.428  -9.483  21.024  1.00 17.88 ? 177 PHE A CB  1 
ATOM   1414 C  CG  . PHE A 1 177 ? 37.042  -8.906  20.709  1.00 18.50 ? 177 PHE A CG  1 
ATOM   1415 C  CD1 . PHE A 1 177 ? 36.101  -9.656  19.911  1.00 20.05 ? 177 PHE A CD1 1 
ATOM   1416 C  CD2 . PHE A 1 177 ? 36.688  -7.622  21.173  1.00 18.19 ? 177 PHE A CD2 1 
ATOM   1417 C  CE1 . PHE A 1 177 ? 34.823  -9.114  19.633  1.00 18.03 ? 177 PHE A CE1 1 
ATOM   1418 C  CE2 . PHE A 1 177 ? 35.409  -7.103  20.901  1.00 22.49 ? 177 PHE A CE2 1 
ATOM   1419 C  CZ  . PHE A 1 177 ? 34.485  -7.847  20.105  1.00 18.82 ? 177 PHE A CZ  1 
ATOM   1420 N  N   . ASN A 1 178 ? 39.002  -10.446 18.257  1.00 16.20 ? 178 ASN A N   1 
ATOM   1421 C  CA  . ASN A 1 178 ? 38.804  -10.749 16.816  1.00 15.15 ? 178 ASN A CA  1 
ATOM   1422 C  C   . ASN A 1 178 ? 37.330  -10.506 16.458  1.00 14.81 ? 178 ASN A C   1 
ATOM   1423 O  O   . ASN A 1 178 ? 36.426  -11.328 16.778  1.00 13.58 ? 178 ASN A O   1 
ATOM   1424 C  CB  . ASN A 1 178 ? 39.172  -12.211 16.526  1.00 16.47 ? 178 ASN A CB  1 
ATOM   1425 C  CG  . ASN A 1 178 ? 38.990  -12.585 15.071  1.00 19.61 ? 178 ASN A CG  1 
ATOM   1426 O  OD1 . ASN A 1 178 ? 38.790  -11.772 14.150  1.00 18.11 ? 178 ASN A OD1 1 
ATOM   1427 N  ND2 . ASN A 1 178 ? 39.023  -13.872 14.840  1.00 22.18 ? 178 ASN A ND2 1 
ATOM   1428 N  N   . ILE A 1 179 ? 37.137  -9.394  15.817  1.00 14.72 ? 179 ILE A N   1 
ATOM   1429 C  CA  . ILE A 1 179 ? 35.777  -8.963  15.397  1.00 13.87 ? 179 ILE A CA  1 
ATOM   1430 C  C   . ILE A 1 179 ? 35.104  -9.998  14.486  1.00 14.27 ? 179 ILE A C   1 
ATOM   1431 O  O   . ILE A 1 179 ? 33.876  -10.069 14.465  1.00 13.78 ? 179 ILE A O   1 
ATOM   1432 C  CB  . ILE A 1 179 ? 35.825  -7.596  14.691  1.00 15.50 ? 179 ILE A CB  1 
ATOM   1433 C  CG1 . ILE A 1 179 ? 36.471  -6.526  15.576  1.00 16.29 ? 179 ILE A CG1 1 
ATOM   1434 C  CG2 . ILE A 1 179 ? 34.410  -7.172  14.264  1.00 15.51 ? 179 ILE A CG2 1 
ATOM   1435 C  CD1 . ILE A 1 179 ? 35.869  -6.411  16.977  1.00 15.98 ? 179 ILE A CD1 1 
ATOM   1436 N  N   . GLU A 1 180 ? 35.848  -10.783 13.691  1.00 13.55 ? 180 GLU A N   1 
ATOM   1437 C  CA  . GLU A 1 180 ? 35.250  -11.834 12.911  1.00 14.57 ? 180 GLU A CA  1 
ATOM   1438 C  C   . GLU A 1 180 ? 34.435  -12.834 13.770  1.00 13.58 ? 180 GLU A C   1 
ATOM   1439 O  O   . GLU A 1 180 ? 33.557  -13.487 13.223  1.00 14.45 ? 180 GLU A O   1 
ATOM   1440 C  CB  . GLU A 1 180 ? 36.306  -12.541 12.043  1.00 15.81 ? 180 GLU A CB  1 
ATOM   1441 C  CG  . GLU A 1 180 ? 35.731  -13.310 10.872  1.00 20.49 ? 180 GLU A CG  1 
ATOM   1442 C  CD  . GLU A 1 180 ? 36.783  -13.722 9.859   1.00 22.54 ? 180 GLU A CD  1 
ATOM   1443 O  OE1 . GLU A 1 180 ? 37.973  -13.388 9.993   1.00 22.58 ? 180 GLU A OE1 1 
ATOM   1444 O  OE2 . GLU A 1 180 ? 36.391  -14.373 8.911   1.00 25.83 ? 180 GLU A OE2 1 
ATOM   1445 N  N   . GLU A 1 181 ? 34.734  -12.913 15.098  1.00 14.70 ? 181 GLU A N   1 
ATOM   1446 C  CA  . GLU A 1 181 ? 33.979  -13.808 15.994  1.00 14.36 ? 181 GLU A CA  1 
ATOM   1447 C  C   . GLU A 1 181 ? 32.467  -13.369 16.097  1.00 12.71 ? 181 GLU A C   1 
ATOM   1448 O  O   . GLU A 1 181 ? 31.662  -14.181 16.508  1.00 14.23 ? 181 GLU A O   1 
ATOM   1449 C  CB  . GLU A 1 181 ? 34.554  -13.911 17.396  1.00 16.34 ? 181 GLU A CB  1 
ATOM   1450 C  CG  . GLU A 1 181 ? 35.983  -14.495 17.488  1.00 19.42 ? 181 GLU A CG  1 
ATOM   1451 C  CD  . GLU A 1 181 ? 36.635  -14.313 18.851  1.00 23.86 ? 181 GLU A CD  1 
ATOM   1452 O  OE1 . GLU A 1 181 ? 35.965  -13.884 19.869  1.00 23.81 ? 181 GLU A OE1 1 
ATOM   1453 O  OE2 . GLU A 1 181 ? 37.891  -14.557 18.905  1.00 25.16 ? 181 GLU A OE2 1 
ATOM   1454 N  N   . LEU A 1 182 ? 32.190  -12.103 15.744  1.00 12.85 ? 182 LEU A N   1 
ATOM   1455 C  CA  . LEU A 1 182 ? 30.832  -11.597 15.790  1.00 10.89 ? 182 LEU A CA  1 
ATOM   1456 C  C   . LEU A 1 182 ? 30.033  -11.950 14.509  1.00 10.99 ? 182 LEU A C   1 
ATOM   1457 O  O   . LEU A 1 182 ? 28.788  -11.793 14.492  1.00 11.76 ? 182 LEU A O   1 
ATOM   1458 C  CB  . LEU A 1 182 ? 30.868  -10.049 15.977  1.00 10.81 ? 182 LEU A CB  1 
ATOM   1459 C  CG  . LEU A 1 182 ? 31.631  -9.493  17.153  1.00 10.71 ? 182 LEU A CG  1 
ATOM   1460 C  CD1 . LEU A 1 182 ? 31.581  -7.930  17.151  1.00 11.24 ? 182 LEU A CD1 1 
ATOM   1461 C  CD2 . LEU A 1 182 ? 31.061  -10.061 18.456  1.00 11.20 ? 182 LEU A CD2 1 
ATOM   1462 N  N   . LEU A 1 183 ? 30.696  -12.492 13.492  1.00 11.80 ? 183 LEU A N   1 
ATOM   1463 C  CA  . LEU A 1 183 ? 30.028  -12.844 12.272  1.00 12.26 ? 183 LEU A CA  1 
ATOM   1464 C  C   . LEU A 1 183 ? 29.434  -14.254 12.368  1.00 11.66 ? 183 LEU A C   1 
ATOM   1465 O  O   . LEU A 1 183 ? 29.939  -15.085 13.176  1.00 14.20 ? 183 LEU A O   1 
ATOM   1466 C  CB  . LEU A 1 183 ? 30.985  -12.778 11.093  1.00 11.74 ? 183 LEU A CB  1 
ATOM   1467 C  CG  . LEU A 1 183 ? 31.694  -11.391 10.993  1.00 12.65 ? 183 LEU A CG  1 
ATOM   1468 C  CD1 . LEU A 1 183 ? 32.659  -11.347 9.786   1.00 17.95 ? 183 LEU A CD1 1 
ATOM   1469 C  CD2 . LEU A 1 183 ? 30.711  -10.193 10.877  1.00 14.29 ? 183 LEU A CD2 1 
ATOM   1470 N  N   . PRO A 1 184 ? 28.395  -14.515 11.600  1.00 12.05 ? 184 PRO A N   1 
ATOM   1471 C  CA  . PRO A 1 184 ? 27.755  -15.778 11.634  1.00 12.92 ? 184 PRO A CA  1 
ATOM   1472 C  C   . PRO A 1 184 ? 28.474  -16.873 10.846  1.00 15.60 ? 184 PRO A C   1 
ATOM   1473 O  O   . PRO A 1 184 ? 29.514  -16.637 10.255  1.00 15.73 ? 184 PRO A O   1 
ATOM   1474 C  CB  . PRO A 1 184 ? 26.380  -15.491 11.034  1.00 14.18 ? 184 PRO A CB  1 
ATOM   1475 C  CG  . PRO A 1 184 ? 26.734  -14.491 9.919   1.00 11.74 ? 184 PRO A CG  1 
ATOM   1476 C  CD  . PRO A 1 184 ? 27.637  -13.566 10.735  1.00 11.73 ? 184 PRO A CD  1 
ATOM   1477 N  N   . GLU A 1 185 ? 27.879  -18.073 10.913  1.00 18.35 ? 185 GLU A N   1 
ATOM   1478 C  CA  . GLU A 1 185 ? 28.261  -19.184 10.036  1.00 18.10 ? 185 GLU A CA  1 
ATOM   1479 C  C   . GLU A 1 185 ? 28.020  -18.848 8.583   1.00 18.90 ? 185 GLU A C   1 
ATOM   1480 O  O   . GLU A 1 185 ? 27.064  -18.078 8.225   1.00 17.47 ? 185 GLU A O   1 
ATOM   1481 C  CB  . GLU A 1 185 ? 27.345  -20.387 10.421  1.00 22.48 ? 185 GLU A CB  1 
ATOM   1482 C  CG  . GLU A 1 185 ? 27.712  -21.010 11.780  1.00 28.16 ? 185 GLU A CG  1 
ATOM   1483 C  CD  . GLU A 1 185 ? 29.206  -21.237 12.000  1.00 37.40 ? 185 GLU A CD  1 
ATOM   1484 O  OE1 . GLU A 1 185 ? 29.863  -21.979 11.215  1.00 33.50 ? 185 GLU A OE1 1 
ATOM   1485 O  OE2 . GLU A 1 185 ? 29.730  -20.672 12.984  1.00 42.90 ? 185 GLU A OE2 1 
ATOM   1486 N  N   . ARG A 1 186 ? 28.922  -19.349 7.731   1.00 16.14 ? 186 ARG A N   1 
ATOM   1487 C  CA  . ARG A 1 186 ? 28.833  -19.279 6.293   1.00 17.55 ? 186 ARG A CA  1 
ATOM   1488 C  C   . ARG A 1 186 ? 28.588  -17.818 5.855   1.00 14.65 ? 186 ARG A C   1 
ATOM   1489 O  O   . ARG A 1 186 ? 27.595  -17.554 5.140   1.00 15.63 ? 186 ARG A O   1 
ATOM   1490 C  CB  . ARG A 1 186 ? 27.749  -20.200 5.772   1.00 19.78 ? 186 ARG A CB  1 
ATOM   1491 C  CG  . ARG A 1 186 ? 28.047  -21.633 6.237   1.00 25.70 ? 186 ARG A CG  1 
ATOM   1492 C  CD  . ARG A 1 186 ? 27.156  -22.738 5.677   1.00 24.98 ? 186 ARG A CD  1 
ATOM   1493 N  NE  . ARG A 1 186 ? 25.708  -22.476 5.624   1.00 27.53 ? 186 ARG A NE  1 
ATOM   1494 C  CZ  . ARG A 1 186 ? 24.861  -22.566 6.648   1.00 27.78 ? 186 ARG A CZ  1 
ATOM   1495 N  NH1 . ARG A 1 186 ? 25.297  -22.871 7.856   1.00 31.42 ? 186 ARG A NH1 1 
ATOM   1496 N  NH2 . ARG A 1 186 ? 23.558  -22.320 6.471   1.00 32.25 ? 186 ARG A NH2 1 
ATOM   1497 N  N   . THR A 1 187 ? 29.578  -16.972 6.152   1.00 13.25 ? 187 THR A N   1 
ATOM   1498 C  CA  . THR A 1 187 ? 29.519  -15.602 5.740   1.00 13.25 ? 187 THR A CA  1 
ATOM   1499 C  C   . THR A 1 187 ? 29.550  -15.509 4.208   1.00 12.91 ? 187 THR A C   1 
ATOM   1500 O  O   . THR A 1 187 ? 29.285  -14.437 3.670   1.00 13.58 ? 187 THR A O   1 
ATOM   1501 C  CB  . THR A 1 187 ? 30.704  -14.767 6.253   1.00 12.52 ? 187 THR A CB  1 
ATOM   1502 O  OG1 . THR A 1 187 ? 31.948  -15.453 5.973   1.00 15.42 ? 187 THR A OG1 1 
ATOM   1503 C  CG2 . THR A 1 187 ? 30.592  -14.476 7.772   1.00 13.23 ? 187 THR A CG2 1 
ATOM   1504 N  N   . ALA A 1 188 ? 29.917  -16.568 3.476   1.00 12.84 ? 188 ALA A N   1 
ATOM   1505 C  CA  . ALA A 1 188 ? 29.691  -16.529 1.994   1.00 13.27 ? 188 ALA A CA  1 
ATOM   1506 C  C   . ALA A 1 188 ? 28.241  -16.331 1.521   1.00 11.46 ? 188 ALA A C   1 
ATOM   1507 O  O   . ALA A 1 188 ? 27.996  -15.947 0.401   1.00 13.26 ? 188 ALA A O   1 
ATOM   1508 C  CB  . ALA A 1 188 ? 30.293  -17.837 1.385   1.00 16.08 ? 188 ALA A CB  1 
ATOM   1509 N  N   . GLU A 1 189 ? 27.294  -16.627 2.411   1.00 12.16 ? 189 GLU A N   1 
ATOM   1510 C  CA  . GLU A 1 189 ? 25.861  -16.534 2.123   1.00 12.73 ? 189 GLU A CA  1 
ATOM   1511 C  C   . GLU A 1 189 ? 25.368  -15.166 2.651   1.00 11.62 ? 189 GLU A C   1 
ATOM   1512 O  O   . GLU A 1 189 ? 25.376  -14.895 3.842   1.00 10.87 ? 189 GLU A O   1 
ATOM   1513 C  CB  . GLU A 1 189 ? 25.086  -17.695 2.798   1.00 14.18 ? 189 GLU A CB  1 
ATOM   1514 C  CG  . GLU A 1 189 ? 25.426  -19.097 2.225   1.00 15.40 ? 189 GLU A CG  1 
ATOM   1515 C  CD  . GLU A 1 189 ? 24.956  -20.250 3.100   1.00 23.39 ? 189 GLU A CD  1 
ATOM   1516 O  OE1 . GLU A 1 189 ? 24.243  -20.078 4.116   1.00 23.25 ? 189 GLU A OE1 1 
ATOM   1517 O  OE2 . GLU A 1 189 ? 25.356  -21.402 2.747   1.00 24.81 ? 189 GLU A OE2 1 
ATOM   1518 N  N   . TYR A 1 190 ? 24.945  -14.322 1.719   1.00 10.50 ? 190 TYR A N   1 
ATOM   1519 C  CA  . TYR A 1 190 ? 24.449  -12.964 2.099   1.00 10.27 ? 190 TYR A CA  1 
ATOM   1520 C  C   . TYR A 1 190 ? 23.544  -12.359 1.051   1.00 10.54 ? 190 TYR A C   1 
ATOM   1521 O  O   . TYR A 1 190 ? 23.494  -12.740 -0.130  1.00 9.63  ? 190 TYR A O   1 
ATOM   1522 C  CB  . TYR A 1 190 ? 25.639  -12.005 2.353   1.00 11.61 ? 190 TYR A CB  1 
ATOM   1523 C  CG  . TYR A 1 190 ? 26.596  -11.864 1.167   1.00 11.40 ? 190 TYR A CG  1 
ATOM   1524 C  CD1 . TYR A 1 190 ? 26.344  -10.935 0.174   1.00 10.28 ? 190 TYR A CD1 1 
ATOM   1525 C  CD2 . TYR A 1 190 ? 27.805  -12.597 1.110   1.00 11.32 ? 190 TYR A CD2 1 
ATOM   1526 C  CE1 . TYR A 1 190 ? 27.224  -10.735 -0.896  1.00 11.89 ? 190 TYR A CE1 1 
ATOM   1527 C  CE2 . TYR A 1 190 ? 28.684  -12.399 0.058   1.00 11.43 ? 190 TYR A CE2 1 
ATOM   1528 C  CZ  . TYR A 1 190 ? 28.387  -11.477 -0.901  1.00 10.81 ? 190 TYR A CZ  1 
ATOM   1529 O  OH  . TYR A 1 190 ? 29.297  -11.302 -1.981  1.00 13.48 ? 190 TYR A OH  1 
ATOM   1530 N  N   . TYR A 1 191 ? 22.802  -11.343 1.518   1.00 10.45 ? 191 TYR A N   1 
ATOM   1531 C  CA  . TYR A 1 191 ? 22.001  -10.442 0.713   1.00 9.83  ? 191 TYR A CA  1 
ATOM   1532 C  C   . TYR A 1 191 ? 22.759  -9.184  0.452   1.00 9.72  ? 191 TYR A C   1 
ATOM   1533 O  O   . TYR A 1 191 ? 23.481  -8.691  1.330   1.00 9.45  ? 191 TYR A O   1 
ATOM   1534 C  CB  . TYR A 1 191 ? 20.729  -10.073 1.538   1.00 10.51 ? 191 TYR A CB  1 
ATOM   1535 C  CG  . TYR A 1 191 ? 19.873  -11.229 2.085   1.00 10.87 ? 191 TYR A CG  1 
ATOM   1536 C  CD1 . TYR A 1 191 ? 18.810  -11.711 1.328   1.00 10.44 ? 191 TYR A CD1 1 
ATOM   1537 C  CD2 . TYR A 1 191 ? 20.056  -11.651 3.423   1.00 9.73  ? 191 TYR A CD2 1 
ATOM   1538 C  CE1 . TYR A 1 191 ? 17.971  -12.711 1.861   1.00 10.31 ? 191 TYR A CE1 1 
ATOM   1539 C  CE2 . TYR A 1 191 ? 19.233  -12.641 3.964   1.00 10.51 ? 191 TYR A CE2 1 
ATOM   1540 C  CZ  . TYR A 1 191 ? 18.236  -13.132 3.136   1.00 10.34 ? 191 TYR A CZ  1 
ATOM   1541 O  OH  . TYR A 1 191 ? 17.420  -14.130 3.712   1.00 13.65 ? 191 TYR A OH  1 
ATOM   1542 N  N   . ARG A 1 192 ? 22.602  -8.644  -0.735  1.00 8.88  ? 192 ARG A N   1 
ATOM   1543 C  CA  . ARG A 1 192 ? 23.401  -7.389  -1.032  1.00 9.23  ? 192 ARG A CA  1 
ATOM   1544 C  C   . ARG A 1 192 ? 22.427  -6.441  -1.744  1.00 10.34 ? 192 ARG A C   1 
ATOM   1545 O  O   . ARG A 1 192 ? 21.658  -6.858  -2.659  1.00 11.11 ? 192 ARG A O   1 
ATOM   1546 C  CB  . ARG A 1 192 ? 24.529  -7.846  -2.005  1.00 11.86 ? 192 ARG A CB  1 
ATOM   1547 C  CG  . ARG A 1 192 ? 25.116  -6.669  -2.858  1.00 12.74 ? 192 ARG A CG  1 
ATOM   1548 C  CD  . ARG A 1 192 ? 25.946  -5.765  -1.958  1.00 11.53 ? 192 ARG A CD  1 
ATOM   1549 N  NE  . ARG A 1 192 ? 26.947  -6.403  -1.125  1.00 12.00 ? 192 ARG A NE  1 
ATOM   1550 C  CZ  . ARG A 1 192 ? 28.074  -6.981  -1.531  1.00 11.29 ? 192 ARG A CZ  1 
ATOM   1551 N  NH1 . ARG A 1 192 ? 28.454  -6.958  -2.838  1.00 16.51 ? 192 ARG A NH1 1 
ATOM   1552 N  NH2 . ARG A 1 192 ? 28.870  -7.523  -0.636  1.00 12.70 ? 192 ARG A NH2 1 
ATOM   1553 N  N   . TYR A 1 193 ? 22.429  -5.159  -1.387  1.00 8.90  ? 193 TYR A N   1 
ATOM   1554 C  CA  . TYR A 1 193 ? 21.589  -4.171  -2.118  1.00 9.26  ? 193 TYR A CA  1 
ATOM   1555 C  C   . TYR A 1 193 ? 22.166  -2.785  -1.834  1.00 8.81  ? 193 TYR A C   1 
ATOM   1556 O  O   . TYR A 1 193 ? 22.856  -2.559  -0.836  1.00 8.82  ? 193 TYR A O   1 
ATOM   1557 C  CB  . TYR A 1 193 ? 20.112  -4.274  -1.752  1.00 9.32  ? 193 TYR A CB  1 
ATOM   1558 C  CG  . TYR A 1 193 ? 19.747  -3.727  -0.396  1.00 8.59  ? 193 TYR A CG  1 
ATOM   1559 C  CD1 . TYR A 1 193 ? 19.198  -2.417  -0.290  1.00 9.06  ? 193 TYR A CD1 1 
ATOM   1560 C  CD2 . TYR A 1 193 ? 19.935  -4.475  0.768   1.00 8.43  ? 193 TYR A CD2 1 
ATOM   1561 C  CE1 . TYR A 1 193 ? 18.847  -1.838  0.926   1.00 8.00  ? 193 TYR A CE1 1 
ATOM   1562 C  CE2 . TYR A 1 193 ? 19.573  -3.909  2.021   1.00 8.37  ? 193 TYR A CE2 1 
ATOM   1563 C  CZ  . TYR A 1 193 ? 19.077  -2.588  2.113   1.00 8.12  ? 193 TYR A CZ  1 
ATOM   1564 O  OH  . TYR A 1 193 ? 18.728  -2.036  3.285   1.00 8.11  ? 193 TYR A OH  1 
ATOM   1565 N  N   . ARG A 1 194 ? 21.860  -1.868  -2.737  1.00 10.35 ? 194 ARG A N   1 
ATOM   1566 C  CA  . ARG A 1 194 ? 22.224  -0.468  -2.468  1.00 9.77  ? 194 ARG A CA  1 
ATOM   1567 C  C   . ARG A 1 194 ? 21.133  0.219   -1.672  1.00 9.78  ? 194 ARG A C   1 
ATOM   1568 O  O   . ARG A 1 194 ? 19.912  0.203   -2.007  1.00 10.81 ? 194 ARG A O   1 
ATOM   1569 C  CB  . ARG A 1 194 ? 22.380  0.276   -3.823  1.00 14.05 ? 194 ARG A CB  1 
ATOM   1570 C  CG  . ARG A 1 194 ? 23.587  -0.237  -4.590  1.00 17.26 ? 194 ARG A CG  1 
ATOM   1571 C  CD  . ARG A 1 194 ? 24.017  0.584   -5.839  1.00 27.01 ? 194 ARG A CD  1 
ATOM   1572 N  NE  . ARG A 1 194 ? 25.342  0.008   -6.196  1.00 36.80 ? 194 ARG A NE  1 
ATOM   1573 C  CZ  . ARG A 1 194 ? 26.526  0.421   -5.698  1.00 44.21 ? 194 ARG A CZ  1 
ATOM   1574 N  NH1 . ARG A 1 194 ? 26.603  1.483   -4.884  1.00 44.35 ? 194 ARG A NH1 1 
ATOM   1575 N  NH2 . ARG A 1 194 ? 27.653  -0.216  -6.035  1.00 48.12 ? 194 ARG A NH2 1 
ATOM   1576 N  N   . GLY A 1 195 ? 21.556  0.852   -0.536  1.00 9.47  ? 195 GLY A N   1 
ATOM   1577 C  CA  . GLY A 1 195 ? 20.576  1.562   0.259   1.00 8.88  ? 195 GLY A CA  1 
ATOM   1578 C  C   . GLY A 1 195 ? 21.154  2.752   0.954   1.00 9.88  ? 195 GLY A C   1 
ATOM   1579 O  O   . GLY A 1 195 ? 21.996  3.477   0.380   1.00 9.34  ? 195 GLY A O   1 
ATOM   1580 N  N   . SER A 1 196 ? 20.722  2.944   2.170   1.00 8.61  ? 196 SER A N   1 
ATOM   1581 C  CA  . SER A 1 196 ? 21.047  4.232   2.830   1.00 8.74  ? 196 SER A CA  1 
ATOM   1582 C  C   . SER A 1 196 ? 21.512  3.939   4.294   1.00 9.85  ? 196 SER A C   1 
ATOM   1583 O  O   . SER A 1 196 ? 21.307  2.839   4.847   1.00 7.91  ? 196 SER A O   1 
ATOM   1584 C  CB  . SER A 1 196 ? 19.822  5.138   2.925   1.00 9.66  ? 196 SER A CB  1 
ATOM   1585 O  OG  . SER A 1 196 ? 18.863  4.644   3.895   1.00 9.25  ? 196 SER A OG  1 
ATOM   1586 N  N   . LEU A 1 197 ? 21.997  4.985   4.927   1.00 9.09  ? 197 LEU A N   1 
ATOM   1587 C  CA  . LEU A 1 197 ? 22.104  4.965   6.387   1.00 9.70  ? 197 LEU A CA  1 
ATOM   1588 C  C   . LEU A 1 197 ? 20.667  4.755   6.951   1.00 8.97  ? 197 LEU A C   1 
ATOM   1589 O  O   . LEU A 1 197 ? 19.712  5.301   6.395   1.00 8.72  ? 197 LEU A O   1 
ATOM   1590 C  CB  . LEU A 1 197 ? 22.741  6.257   6.994   1.00 10.61 ? 197 LEU A CB  1 
ATOM   1591 C  CG  . LEU A 1 197 ? 24.232  6.503   6.652   1.00 12.78 ? 197 LEU A CG  1 
ATOM   1592 C  CD1 . LEU A 1 197 ? 24.495  7.002   5.252   1.00 19.04 ? 197 LEU A CD1 1 
ATOM   1593 C  CD2 . LEU A 1 197 ? 24.687  7.640   7.553   1.00 15.50 ? 197 LEU A CD2 1 
ATOM   1594 N  N   . THR A 1 198 ? 20.492  4.018   8.030   1.00 8.56  ? 198 THR A N   1 
ATOM   1595 C  CA  . THR A 1 198 ? 19.165  3.886   8.595   1.00 8.44  ? 198 THR A CA  1 
ATOM   1596 C  C   . THR A 1 198 ? 18.860  4.931   9.673   1.00 9.40  ? 198 THR A C   1 
ATOM   1597 O  O   . THR A 1 198 ? 17.838  4.830   10.442  1.00 10.09 ? 198 THR A O   1 
ATOM   1598 C  CB  . THR A 1 198 ? 19.027  2.466   9.241   1.00 7.84  ? 198 THR A CB  1 
ATOM   1599 O  OG1 . THR A 1 198 ? 19.972  2.343   10.312  1.00 7.90  ? 198 THR A OG1 1 
ATOM   1600 C  CG2 . THR A 1 198 ? 19.204  1.316   8.225   1.00 8.51  ? 198 THR A CG2 1 
ATOM   1601 N  N   . THR A 1 199 ? 19.772  5.907   9.818   1.00 10.60 ? 199 THR A N   1 
ATOM   1602 C  CA  . THR A 1 199 ? 19.694  6.949   10.837  1.00 10.28 ? 199 THR A CA  1 
ATOM   1603 C  C   . THR A 1 199 ? 20.013  8.221   10.117  1.00 9.88  ? 199 THR A C   1 
ATOM   1604 O  O   . THR A 1 199 ? 20.713  8.218   9.087   1.00 11.28 ? 199 THR A O   1 
ATOM   1605 C  CB  . THR A 1 199 ? 20.810  6.840   11.940  1.00 11.75 ? 199 THR A CB  1 
ATOM   1606 O  OG1 . THR A 1 199 ? 22.070  6.792   11.327  1.00 15.09 ? 199 THR A OG1 1 
ATOM   1607 C  CG2 . THR A 1 199 ? 20.617  5.496   12.747  1.00 13.43 ? 199 THR A CG2 1 
ATOM   1608 N  N   . PRO A 1 200 ? 19.487  9.343   10.656  1.00 10.44 ? 200 PRO A N   1 
ATOM   1609 C  CA  . PRO A 1 200 ? 19.838  10.585  9.986   1.00 10.73 ? 200 PRO A CA  1 
ATOM   1610 C  C   . PRO A 1 200 ? 21.357  10.740  9.849   1.00 11.03 ? 200 PRO A C   1 
ATOM   1611 O  O   . PRO A 1 200 ? 22.065  10.320  10.756  1.00 13.14 ? 200 PRO A O   1 
ATOM   1612 C  CB  . PRO A 1 200 ? 19.284  11.616  10.984  1.00 10.49 ? 200 PRO A CB  1 
ATOM   1613 C  CG  . PRO A 1 200 ? 18.065  10.977  11.577  1.00 9.17  ? 200 PRO A CG  1 
ATOM   1614 C  CD  . PRO A 1 200 ? 18.485  9.511   11.729  1.00 9.83  ? 200 PRO A CD  1 
ATOM   1615 N  N   . PRO A 1 201 ? 21.805  11.295  8.755   1.00 10.56 ? 201 PRO A N   1 
ATOM   1616 C  CA  . PRO A 1 201 ? 21.009  12.032  7.692   1.00 10.83 ? 201 PRO A CA  1 
ATOM   1617 C  C   . PRO A 1 201 ? 20.435  11.167  6.594   1.00 10.69 ? 201 PRO A C   1 
ATOM   1618 O  O   . PRO A 1 201 ? 20.000  11.643  5.596   1.00 11.83 ? 201 PRO A O   1 
ATOM   1619 C  CB  . PRO A 1 201 ? 22.037  13.015  7.052   1.00 11.97 ? 201 PRO A CB  1 
ATOM   1620 C  CG  . PRO A 1 201 ? 23.240  12.943  7.908   1.00 11.98 ? 201 PRO A CG  1 
ATOM   1621 C  CD  . PRO A 1 201 ? 23.261  11.589  8.639   1.00 11.62 ? 201 PRO A CD  1 
ATOM   1622 N  N   . CYS A 1 202 ? 20.522  9.851   6.766   1.00 9.48  ? 202 CYS A N   1 
ATOM   1623 C  CA  . CYS A 1 202 ? 19.872  8.863   5.840   1.00 9.45  ? 202 CYS A CA  1 
ATOM   1624 C  C   . CYS A 1 202 ? 20.457  8.905   4.429   1.00 9.04  ? 202 CYS A C   1 
ATOM   1625 O  O   . CYS A 1 202 ? 19.787  8.577   3.442   1.00 10.73 ? 202 CYS A O   1 
ATOM   1626 C  CB  . CYS A 1 202 ? 18.329  9.103   5.795   1.00 9.87  ? 202 CYS A CB  1 
ATOM   1627 S  SG  . CYS A 1 202 ? 17.451  9.005   7.371   1.00 10.35 ? 202 CYS A SG  1 
ATOM   1628 N  N   . ASN A 1 203 ? 21.737  9.262   4.311   1.00 9.68  ? 203 ASN A N   1 
ATOM   1629 C  CA  . ASN A 1 203 ? 22.309  9.419   2.934   1.00 11.57 ? 203 ASN A CA  1 
ATOM   1630 C  C   . ASN A 1 203 ? 22.246  8.086   2.197   1.00 9.54  ? 203 ASN A C   1 
ATOM   1631 O  O   . ASN A 1 203 ? 22.495  7.002   2.779   1.00 9.55  ? 203 ASN A O   1 
ATOM   1632 C  CB  . ASN A 1 203 ? 23.748  9.868   3.002   1.00 13.85 ? 203 ASN A CB  1 
ATOM   1633 C  CG  . ASN A 1 203 ? 23.861  11.089  3.851   1.00 14.35 ? 203 ASN A CG  1 
ATOM   1634 O  OD1 . ASN A 1 203 ? 23.902  10.999  5.036   1.00 18.88 ? 203 ASN A OD1 1 
ATOM   1635 N  ND2 . ASN A 1 203 ? 23.781  12.245  3.218   1.00 19.12 ? 203 ASN A ND2 1 
ATOM   1636 N  N   . PRO A 1 204 ? 21.838  8.095   0.926   1.00 9.93  ? 204 PRO A N   1 
ATOM   1637 C  CA  . PRO A 1 204 ? 21.648  6.875   0.096   1.00 11.48 ? 204 PRO A CA  1 
ATOM   1638 C  C   . PRO A 1 204 ? 22.994  6.482   -0.467  1.00 11.86 ? 204 PRO A C   1 
ATOM   1639 O  O   . PRO A 1 204 ? 23.209  6.399   -1.716  1.00 12.84 ? 204 PRO A O   1 
ATOM   1640 C  CB  . PRO A 1 204 ? 20.747  7.371   -1.020  1.00 11.01 ? 204 PRO A CB  1 
ATOM   1641 C  CG  . PRO A 1 204 ? 21.154  8.866   -1.186  1.00 11.18 ? 204 PRO A CG  1 
ATOM   1642 C  CD  . PRO A 1 204 ? 21.281  9.325   0.245   1.00 11.54 ? 204 PRO A CD  1 
ATOM   1643 N  N   . THR A 1 205 ? 23.918  6.209   0.451   1.00 10.05 ? 205 THR A N   1 
ATOM   1644 C  CA  . THR A 1 205 ? 25.321  5.965   0.022   1.00 10.78 ? 205 THR A CA  1 
ATOM   1645 C  C   . THR A 1 205 ? 25.906  4.669   0.583   1.00 10.33 ? 205 THR A C   1 
ATOM   1646 O  O   . THR A 1 205 ? 27.136  4.525   0.571   1.00 10.46 ? 205 THR A O   1 
ATOM   1647 C  CB  . THR A 1 205 ? 26.230  7.040   0.602   1.00 11.93 ? 205 THR A CB  1 
ATOM   1648 O  OG1 . THR A 1 205 ? 25.972  7.204   1.993   1.00 12.69 ? 205 THR A OG1 1 
ATOM   1649 C  CG2 . THR A 1 205 ? 25.871  8.372   -0.126  1.00 11.78 ? 205 THR A CG2 1 
ATOM   1650 N  N   . VAL A 1 206 ? 25.049  3.776   1.081   1.00 8.74  ? 206 VAL A N   1 
ATOM   1651 C  CA  . VAL A 1 206 ? 25.513  2.514   1.649   1.00 9.21  ? 206 VAL A CA  1 
ATOM   1652 C  C   . VAL A 1 206 ? 25.278  1.305   0.776   1.00 9.08  ? 206 VAL A C   1 
ATOM   1653 O  O   . VAL A 1 206 ? 24.149  1.006   0.318   1.00 11.03 ? 206 VAL A O   1 
ATOM   1654 C  CB  . VAL A 1 206 ? 24.751  2.282   3.004   1.00 8.52  ? 206 VAL A CB  1 
ATOM   1655 C  CG1 . VAL A 1 206 ? 25.119  0.927   3.562   1.00 8.35  ? 206 VAL A CG1 1 
ATOM   1656 C  CG2 . VAL A 1 206 ? 24.993  3.444   4.049   1.00 8.35  ? 206 VAL A CG2 1 
ATOM   1657 N  N   . LEU A 1 207 ? 26.334  0.533   0.606   1.00 9.24  ? 207 LEU A N   1 
ATOM   1658 C  CA  . LEU A 1 207 ? 26.281  -0.786  0.010   1.00 10.57 ? 207 LEU A CA  1 
ATOM   1659 C  C   . LEU A 1 207 ? 26.064  -1.768  1.177   1.00 9.48  ? 207 LEU A C   1 
ATOM   1660 O  O   . LEU A 1 207 ? 26.937  -1.968  2.021   1.00 11.10 ? 207 LEU A O   1 
ATOM   1661 C  CB  . LEU A 1 207 ? 27.571  -1.109  -0.758  1.00 12.28 ? 207 LEU A CB  1 
ATOM   1662 C  CG  . LEU A 1 207 ? 27.433  -2.443  -1.486  1.00 14.17 ? 207 LEU A CG  1 
ATOM   1663 C  CD1 . LEU A 1 207 ? 26.437  -2.328  -2.682  1.00 16.84 ? 207 LEU A CD1 1 
ATOM   1664 C  CD2 . LEU A 1 207 ? 28.822  -2.791  -1.892  1.00 18.18 ? 207 LEU A CD2 1 
ATOM   1665 N  N   . TRP A 1 208 ? 24.849  -2.326  1.251   1.00 8.53  ? 208 TRP A N   1 
ATOM   1666 C  CA  . TRP A 1 208 ? 24.477  -3.274  2.312   1.00 7.73  ? 208 TRP A CA  1 
ATOM   1667 C  C   . TRP A 1 208 ? 24.871  -4.660  2.062   1.00 8.50  ? 208 TRP A C   1 
ATOM   1668 O  O   . TRP A 1 208 ? 24.617  -5.169  0.923   1.00 9.30  ? 208 TRP A O   1 
ATOM   1669 C  CB  . TRP A 1 208 ? 22.973  -3.224  2.573   1.00 8.14  ? 208 TRP A CB  1 
ATOM   1670 C  CG  . TRP A 1 208 ? 22.607  -2.013  3.392   1.00 7.95  ? 208 TRP A CG  1 
ATOM   1671 C  CD1 . TRP A 1 208 ? 22.124  -0.778  2.937   1.00 7.55  ? 208 TRP A CD1 1 
ATOM   1672 C  CD2 . TRP A 1 208 ? 22.726  -1.850  4.865   1.00 7.42  ? 208 TRP A CD2 1 
ATOM   1673 N  NE1 . TRP A 1 208 ? 21.934  0.077   3.957   1.00 8.02  ? 208 TRP A NE1 1 
ATOM   1674 C  CE2 . TRP A 1 208 ? 22.279  -0.496  5.176   1.00 7.56  ? 208 TRP A CE2 1 
ATOM   1675 C  CE3 . TRP A 1 208 ? 23.165  -2.682  5.918   1.00 7.81  ? 208 TRP A CE3 1 
ATOM   1676 C  CZ2 . TRP A 1 208 ? 22.289  0.029   6.479   1.00 8.26  ? 208 TRP A CZ2 1 
ATOM   1677 C  CZ3 . TRP A 1 208 ? 23.149  -2.181  7.238   1.00 7.87  ? 208 TRP A CZ3 1 
ATOM   1678 C  CH2 . TRP A 1 208 ? 22.761  -0.817  7.493   1.00 9.71  ? 208 TRP A CH2 1 
ATOM   1679 N  N   . THR A 1 209 ? 25.448  -5.319  3.052   1.00 8.40  ? 209 THR A N   1 
ATOM   1680 C  CA  . THR A 1 209 ? 25.630  -6.789  2.959   1.00 8.36  ? 209 THR A CA  1 
ATOM   1681 C  C   . THR A 1 209 ? 24.992  -7.361  4.255   1.00 8.33  ? 209 THR A C   1 
ATOM   1682 O  O   . THR A 1 209 ? 25.498  -7.035  5.357   1.00 8.85  ? 209 THR A O   1 
ATOM   1683 C  CB  . THR A 1 209 ? 27.126  -7.178  2.993   1.00 9.80  ? 209 THR A CB  1 
ATOM   1684 O  OG1 . THR A 1 209 ? 27.707  -6.606  1.795   1.00 10.31 ? 209 THR A OG1 1 
ATOM   1685 C  CG2 . THR A 1 209 ? 27.316  -8.693  2.978   1.00 10.50 ? 209 THR A CG2 1 
ATOM   1686 N  N   . VAL A 1 210 ? 23.909  -8.131  4.132   1.00 7.79  ? 210 VAL A N   1 
ATOM   1687 C  CA  . VAL A 1 210 ? 23.221  -8.665  5.326   1.00 7.42  ? 210 VAL A CA  1 
ATOM   1688 C  C   . VAL A 1 210 ? 23.437  -10.191 5.255   1.00 7.35  ? 210 VAL A C   1 
ATOM   1689 O  O   . VAL A 1 210 ? 23.078  -10.808 4.234   1.00 9.36  ? 210 VAL A O   1 
ATOM   1690 C  CB  . VAL A 1 210 ? 21.667  -8.369  5.317   1.00 8.09  ? 210 VAL A CB  1 
ATOM   1691 C  CG1 . VAL A 1 210 ? 21.008  -8.988  6.595   1.00 9.33  ? 210 VAL A CG1 1 
ATOM   1692 C  CG2 . VAL A 1 210 ? 21.413  -6.875  5.118   1.00 9.31  ? 210 VAL A CG2 1 
ATOM   1693 N  N   . PHE A 1 211 ? 24.132  -10.702 6.255   1.00 7.85  ? 211 PHE A N   1 
ATOM   1694 C  CA  . PHE A 1 211 ? 24.415  -12.139 6.207   1.00 7.94  ? 211 PHE A CA  1 
ATOM   1695 C  C   . PHE A 1 211 ? 23.180  -12.970 6.328   1.00 8.71  ? 211 PHE A C   1 
ATOM   1696 O  O   . PHE A 1 211 ? 22.224  -12.639 7.059   1.00 8.98  ? 211 PHE A O   1 
ATOM   1697 C  CB  . PHE A 1 211 ? 25.480  -12.531 7.227   1.00 8.55  ? 211 PHE A CB  1 
ATOM   1698 C  CG  . PHE A 1 211 ? 26.806  -11.888 7.000   1.00 9.09  ? 211 PHE A CG  1 
ATOM   1699 C  CD1 . PHE A 1 211 ? 27.617  -12.304 5.929   1.00 10.96 ? 211 PHE A CD1 1 
ATOM   1700 C  CD2 . PHE A 1 211 ? 27.239  -10.813 7.842   1.00 9.64  ? 211 PHE A CD2 1 
ATOM   1701 C  CE1 . PHE A 1 211 ? 28.824  -11.617 5.649   1.00 10.58 ? 211 PHE A CE1 1 
ATOM   1702 C  CE2 . PHE A 1 211 ? 28.487  -10.184 7.603   1.00 10.33 ? 211 PHE A CE2 1 
ATOM   1703 C  CZ  . PHE A 1 211 ? 29.276  -10.586 6.502   1.00 10.62 ? 211 PHE A CZ  1 
ATOM   1704 N  N   . ARG A 1 212 ? 23.178  -14.055 5.547   1.00 9.09  ? 212 ARG A N   1 
ATOM   1705 C  CA  . ARG A 1 212 ? 21.975  -14.914 5.528   1.00 10.72 ? 212 ARG A CA  1 
ATOM   1706 C  C   . ARG A 1 212 ? 21.671  -15.526 6.889   1.00 10.44 ? 212 ARG A C   1 
ATOM   1707 O  O   . ARG A 1 212 ? 20.471  -15.599 7.294   1.00 10.87 ? 212 ARG A O   1 
ATOM   1708 C  CB  . ARG A 1 212 ? 22.177  -16.059 4.542   1.00 10.80 ? 212 ARG A CB  1 
ATOM   1709 C  CG  . ARG A 1 212 ? 20.883  -16.836 4.372   1.00 13.26 ? 212 ARG A CG  1 
ATOM   1710 C  CD  . ARG A 1 212 ? 21.216  -18.119 3.575   1.00 15.59 ? 212 ARG A CD  1 
ATOM   1711 N  NE  . ARG A 1 212 ? 20.052  -19.004 3.434   1.00 23.10 ? 212 ARG A NE  1 
ATOM   1712 C  CZ  . ARG A 1 212 ? 19.770  -20.044 4.219   1.00 28.19 ? 212 ARG A CZ  1 
ATOM   1713 N  NH1 . ARG A 1 212 ? 20.579  -20.394 5.207   1.00 30.10 ? 212 ARG A NH1 1 
ATOM   1714 N  NH2 . ARG A 1 212 ? 18.666  -20.760 3.978   1.00 26.75 ? 212 ARG A NH2 1 
ATOM   1715 N  N   . ASN A 1 213 ? 22.695  -15.953 7.609   1.00 9.81  ? 213 ASN A N   1 
ATOM   1716 C  CA  . ASN A 1 213 ? 22.482  -16.704 8.876   1.00 11.47 ? 213 ASN A CA  1 
ATOM   1717 C  C   . ASN A 1 213 ? 22.649  -15.843 10.075  1.00 10.44 ? 213 ASN A C   1 
ATOM   1718 O  O   . ASN A 1 213 ? 23.582  -15.027 10.125  1.00 11.38 ? 213 ASN A O   1 
ATOM   1719 C  CB  . ASN A 1 213 ? 23.494  -17.843 8.893   1.00 10.99 ? 213 ASN A CB  1 
ATOM   1720 C  CG  . ASN A 1 213 ? 23.340  -18.720 7.661   1.00 13.10 ? 213 ASN A CG  1 
ATOM   1721 O  OD1 . ASN A 1 213 ? 22.201  -19.111 7.260   1.00 16.27 ? 213 ASN A OD1 1 
ATOM   1722 N  ND2 . ASN A 1 213 ? 24.463  -18.937 6.984   1.00 13.85 ? 213 ASN A ND2 1 
ATOM   1723 N  N   . PRO A 1 214 ? 21.759  -15.975 11.050  1.00 11.38 ? 214 PRO A N   1 
ATOM   1724 C  CA  . PRO A 1 214 ? 21.862  -15.216 12.277  1.00 11.87 ? 214 PRO A CA  1 
ATOM   1725 C  C   . PRO A 1 214 ? 22.917  -15.858 13.234  1.00 11.91 ? 214 PRO A C   1 
ATOM   1726 O  O   . PRO A 1 214 ? 23.319  -17.048 13.056  1.00 11.99 ? 214 PRO A O   1 
ATOM   1727 C  CB  . PRO A 1 214 ? 20.467  -15.395 12.956  1.00 12.31 ? 214 PRO A CB  1 
ATOM   1728 C  CG  . PRO A 1 214 ? 19.986  -16.662 12.409  1.00 13.15 ? 214 PRO A CG  1 
ATOM   1729 C  CD  . PRO A 1 214 ? 20.597  -16.892 11.028  1.00 12.77 ? 214 PRO A CD  1 
ATOM   1730 N  N   . VAL A 1 215 ? 23.310  -15.024 14.166  1.00 12.04 ? 215 VAL A N   1 
ATOM   1731 C  CA  . VAL A 1 215 ? 24.095  -15.463 15.338  1.00 12.80 ? 215 VAL A CA  1 
ATOM   1732 C  C   . VAL A 1 215 ? 23.113  -15.647 16.470  1.00 14.10 ? 215 VAL A C   1 
ATOM   1733 O  O   . VAL A 1 215 ? 22.002  -15.157 16.389  1.00 12.87 ? 215 VAL A O   1 
ATOM   1734 C  CB  . VAL A 1 215 ? 25.202  -14.524 15.735  1.00 13.59 ? 215 VAL A CB  1 
ATOM   1735 C  CG1 . VAL A 1 215 ? 26.279  -14.422 14.638  1.00 12.49 ? 215 VAL A CG1 1 
ATOM   1736 C  CG2 . VAL A 1 215 ? 24.740  -13.143 16.175  1.00 12.08 ? 215 VAL A CG2 1 
ATOM   1737 N  N   . GLN A 1 216 ? 23.559  -16.322 17.556  1.00 15.15 ? 216 GLN A N   1 
ATOM   1738 C  CA  . GLN A 1 216 ? 22.740  -16.470 18.775  1.00 14.46 ? 216 GLN A CA  1 
ATOM   1739 C  C   . GLN A 1 216 ? 23.404  -15.844 19.944  1.00 15.05 ? 216 GLN A C   1 
ATOM   1740 O  O   . GLN A 1 216 ? 24.631  -15.867 20.064  1.00 15.33 ? 216 GLN A O   1 
ATOM   1741 C  CB  . GLN A 1 216 ? 22.489  -17.976 19.088  1.00 14.54 ? 216 GLN A CB  1 
ATOM   1742 C  CG  . GLN A 1 216 ? 21.708  -18.650 18.032  1.00 16.69 ? 216 GLN A CG  1 
ATOM   1743 C  CD  . GLN A 1 216 ? 21.273  -20.029 18.444  1.00 25.49 ? 216 GLN A CD  1 
ATOM   1744 O  OE1 . GLN A 1 216 ? 21.805  -20.663 19.433  1.00 30.67 ? 216 GLN A OE1 1 
ATOM   1745 N  NE2 . GLN A 1 216 ? 20.270  -20.524 17.715  1.00 24.07 ? 216 GLN A NE2 1 
ATOM   1746 N  N   . ILE A 1 217 ? 22.615  -15.187 20.800  1.00 13.71 ? 217 ILE A N   1 
ATOM   1747 C  CA  . ILE A 1 217 ? 23.073  -14.706 22.107  1.00 13.93 ? 217 ILE A CA  1 
ATOM   1748 C  C   . ILE A 1 217 ? 22.086  -15.219 23.133  1.00 14.30 ? 217 ILE A C   1 
ATOM   1749 O  O   . ILE A 1 217 ? 20.985  -15.539 22.768  1.00 13.99 ? 217 ILE A O   1 
ATOM   1750 C  CB  . ILE A 1 217 ? 23.206  -13.174 22.160  1.00 13.49 ? 217 ILE A CB  1 
ATOM   1751 C  CG1 . ILE A 1 217 ? 21.853  -12.414 22.005  1.00 13.63 ? 217 ILE A CG1 1 
ATOM   1752 C  CG2 . ILE A 1 217 ? 24.242  -12.721 21.137  1.00 15.63 ? 217 ILE A CG2 1 
ATOM   1753 C  CD1 . ILE A 1 217 ? 21.988  -10.939 22.184  1.00 12.81 ? 217 ILE A CD1 1 
ATOM   1754 N  N   . SER A 1 218 ? 22.497  -15.320 24.409  1.00 14.34 ? 218 SER A N   1 
ATOM   1755 C  CA  . SER A 1 218 ? 21.515  -15.902 25.331  1.00 15.61 ? 218 SER A CA  1 
ATOM   1756 C  C   . SER A 1 218 ? 20.429  -14.914 25.692  1.00 16.65 ? 218 SER A C   1 
ATOM   1757 O  O   . SER A 1 218 ? 20.544  -13.712 25.465  1.00 15.04 ? 218 SER A O   1 
ATOM   1758 C  CB  . SER A 1 218 ? 22.215  -16.312 26.627  1.00 14.57 ? 218 SER A CB  1 
ATOM   1759 O  OG  . SER A 1 218 ? 22.738  -15.189 27.346  1.00 15.83 ? 218 SER A OG  1 
ATOM   1760 N  N   . GLN A 1 219 ? 19.402  -15.461 26.338  1.00 18.17 ? 219 GLN A N   1 
ATOM   1761 C  CA  . GLN A 1 219 ? 18.296  -14.568 26.785  1.00 19.70 ? 219 GLN A CA  1 
ATOM   1762 C  C   . GLN A 1 219 ? 18.789  -13.562 27.800  1.00 17.78 ? 219 GLN A C   1 
ATOM   1763 O  O   . GLN A 1 219 ? 18.375  -12.407 27.762  1.00 16.24 ? 219 GLN A O   1 
ATOM   1764 C  CB  . GLN A 1 219 ? 17.148  -15.370 27.307  1.00 25.72 ? 219 GLN A CB  1 
ATOM   1765 C  CG  . GLN A 1 219 ? 17.487  -16.196 28.503  1.00 30.78 ? 219 GLN A CG  1 
ATOM   1766 C  CD  . GLN A 1 219 ? 16.235  -16.813 29.020  1.00 38.49 ? 219 GLN A CD  1 
ATOM   1767 O  OE1 . GLN A 1 219 ? 15.626  -17.636 28.319  1.00 41.90 ? 219 GLN A OE1 1 
ATOM   1768 N  NE2 . GLN A 1 219 ? 15.792  -16.386 30.222  1.00 39.50 ? 219 GLN A NE2 1 
ATOM   1769 N  N   . GLU A 1 220 ? 19.762  -13.902 28.637  1.00 18.10 ? 220 GLU A N   1 
ATOM   1770 C  CA  . GLU A 1 220 ? 20.310  -12.987 29.548  1.00 16.78 ? 220 GLU A CA  1 
ATOM   1771 C  C   . GLU A 1 220 ? 21.131  -11.910 28.850  1.00 17.33 ? 220 GLU A C   1 
ATOM   1772 O  O   . GLU A 1 220 ? 21.100  -10.751 29.263  1.00 16.17 ? 220 GLU A O   1 
ATOM   1773 C  CB  . GLU A 1 220 ? 21.225  -13.689 30.625  1.00 20.90 ? 220 GLU A CB  1 
ATOM   1774 C  CG  . GLU A 1 220 ? 20.450  -14.681 31.499  1.00 22.87 ? 220 GLU A CG  1 
ATOM   1775 C  CD  . GLU A 1 220 ? 20.135  -16.067 30.874  1.00 28.69 ? 220 GLU A CD  1 
ATOM   1776 O  OE1 . GLU A 1 220 ? 20.663  -16.515 29.792  1.00 26.10 ? 220 GLU A OE1 1 
ATOM   1777 O  OE2 . GLU A 1 220 ? 19.263  -16.765 31.471  1.00 30.67 ? 220 GLU A OE2 1 
ATOM   1778 N  N   . GLN A 1 221 ? 21.843  -12.321 27.788  1.00 16.53 ? 221 GLN A N   1 
ATOM   1779 C  CA  . GLN A 1 221 ? 22.632  -11.320 27.003  1.00 15.79 ? 221 GLN A CA  1 
ATOM   1780 C  C   . GLN A 1 221 ? 21.701  -10.294 26.309  1.00 14.56 ? 221 GLN A C   1 
ATOM   1781 O  O   . GLN A 1 221 ? 21.969  -9.072  26.364  1.00 14.69 ? 221 GLN A O   1 
ATOM   1782 C  CB  . GLN A 1 221 ? 23.484  -11.996 25.931  1.00 17.50 ? 221 GLN A CB  1 
ATOM   1783 C  CG  . GLN A 1 221 ? 24.732  -12.619 26.568  1.00 16.86 ? 221 GLN A CG  1 
ATOM   1784 C  CD  . GLN A 1 221 ? 25.639  -13.336 25.565  1.00 12.04 ? 221 GLN A CD  1 
ATOM   1785 O  OE1 . GLN A 1 221 ? 25.220  -14.236 24.875  1.00 15.00 ? 221 GLN A OE1 1 
ATOM   1786 N  NE2 . GLN A 1 221 ? 26.915  -12.877 25.469  1.00 15.05 ? 221 GLN A NE2 1 
ATOM   1787 N  N   . LEU A 1 222 ? 20.636  -10.816 25.759  1.00 14.73 ? 222 LEU A N   1 
ATOM   1788 C  CA  . LEU A 1 222 ? 19.700  -9.957  25.027  1.00 14.08 ? 222 LEU A CA  1 
ATOM   1789 C  C   . LEU A 1 222 ? 19.012  -9.024  26.003  1.00 15.32 ? 222 LEU A C   1 
ATOM   1790 O  O   . LEU A 1 222 ? 18.870  -7.841  25.748  1.00 12.79 ? 222 LEU A O   1 
ATOM   1791 C  CB  . LEU A 1 222 ? 18.684  -10.807 24.257  1.00 14.76 ? 222 LEU A CB  1 
ATOM   1792 C  CG  . LEU A 1 222 ? 17.517  -10.047 23.581  1.00 13.80 ? 222 LEU A CG  1 
ATOM   1793 C  CD1 . LEU A 1 222 ? 18.182  -9.164  22.474  1.00 14.52 ? 222 LEU A CD1 1 
ATOM   1794 C  CD2 . LEU A 1 222 ? 16.630  -11.155 22.982  1.00 13.04 ? 222 LEU A CD2 1 
ATOM   1795 N  N   . LEU A 1 223 ? 18.664  -9.543  27.210  1.00 15.05 ? 223 LEU A N   1 
ATOM   1796 C  CA  . LEU A 1 223 ? 18.032  -8.652  28.206  1.00 14.46 ? 223 LEU A CA  1 
ATOM   1797 C  C   . LEU A 1 223 ? 18.991  -7.600  28.713  1.00 15.05 ? 223 LEU A C   1 
ATOM   1798 O  O   . LEU A 1 223 ? 18.608  -6.470  28.862  1.00 16.59 ? 223 LEU A O   1 
ATOM   1799 C  CB  . LEU A 1 223 ? 17.676  -9.544  29.387  1.00 14.54 ? 223 LEU A CB  1 
ATOM   1800 C  CG  . LEU A 1 223 ? 16.841  -8.897  30.498  1.00 16.14 ? 223 LEU A CG  1 
ATOM   1801 C  CD1 . LEU A 1 223 ? 15.524  -8.442  29.941  1.00 14.92 ? 223 LEU A CD1 1 
ATOM   1802 C  CD2 . LEU A 1 223 ? 16.603  -9.983  31.572  1.00 18.69 ? 223 LEU A CD2 1 
ATOM   1803 N  N   . ALA A 1 224 ? 20.277  -7.970  28.873  1.00 14.69 ? 224 ALA A N   1 
ATOM   1804 C  CA  . ALA A 1 224 ? 21.261  -6.996  29.227  1.00 17.43 ? 224 ALA A CA  1 
ATOM   1805 C  C   . ALA A 1 224 ? 21.330  -5.827  28.208  1.00 16.67 ? 224 ALA A C   1 
ATOM   1806 O  O   . ALA A 1 224 ? 21.325  -4.630  28.564  1.00 17.53 ? 224 ALA A O   1 
ATOM   1807 C  CB  . ALA A 1 224 ? 22.618  -7.718  29.407  1.00 16.58 ? 224 ALA A CB  1 
ATOM   1808 N  N   . LEU A 1 225 ? 21.389  -6.177  26.932  1.00 15.85 ? 225 LEU A N   1 
ATOM   1809 C  CA  . LEU A 1 225 ? 21.481  -5.130  25.921  1.00 15.98 ? 225 LEU A CA  1 
ATOM   1810 C  C   . LEU A 1 225 ? 20.228  -4.256  25.949  1.00 15.85 ? 225 LEU A C   1 
ATOM   1811 O  O   . LEU A 1 225 ? 20.290  -3.029  25.735  1.00 19.17 ? 225 LEU A O   1 
ATOM   1812 C  CB  . LEU A 1 225 ? 21.596  -5.881  24.604  1.00 14.85 ? 225 LEU A CB  1 
ATOM   1813 C  CG  . LEU A 1 225 ? 21.684  -4.987  23.342  1.00 14.49 ? 225 LEU A CG  1 
ATOM   1814 C  CD1 . LEU A 1 225 ? 22.937  -4.122  23.344  1.00 15.63 ? 225 LEU A CD1 1 
ATOM   1815 C  CD2 . LEU A 1 225 ? 21.635  -5.849  22.107  1.00 13.36 ? 225 LEU A CD2 1 
ATOM   1816 N  N   . GLU A 1 226 ? 19.071  -4.883  26.163  1.00 13.96 ? 226 GLU A N   1 
ATOM   1817 C  CA  . GLU A 1 226 ? 17.787  -4.079  26.150  1.00 13.51 ? 226 GLU A CA  1 
ATOM   1818 C  C   . GLU A 1 226 ? 17.604  -3.186  27.371  1.00 15.96 ? 226 GLU A C   1 
ATOM   1819 O  O   . GLU A 1 226 ? 16.757  -2.310  27.365  1.00 16.03 ? 226 GLU A O   1 
ATOM   1820 C  CB  . GLU A 1 226 ? 16.604  -5.043  26.086  1.00 13.66 ? 226 GLU A CB  1 
ATOM   1821 C  CG  . GLU A 1 226 ? 16.510  -5.838  24.770  1.00 14.51 ? 226 GLU A CG  1 
ATOM   1822 C  CD  . GLU A 1 226 ? 15.612  -7.050  24.808  1.00 16.13 ? 226 GLU A CD  1 
ATOM   1823 O  OE1 . GLU A 1 226 ? 15.277  -7.579  25.912  1.00 15.13 ? 226 GLU A OE1 1 
ATOM   1824 O  OE2 . GLU A 1 226 ? 15.178  -7.527  23.752  1.00 15.83 ? 226 GLU A OE2 1 
ATOM   1825 N  N   . THR A 1 227 ? 18.323  -3.496  28.459  1.00 17.13 ? 227 THR A N   1 
ATOM   1826 C  CA  . THR A 1 227 ? 18.059  -2.857  29.794  1.00 16.87 ? 227 THR A CA  1 
ATOM   1827 C  C   . THR A 1 227 ? 19.239  -2.076  30.368  1.00 17.41 ? 227 THR A C   1 
ATOM   1828 O  O   . THR A 1 227 ? 19.050  -1.315  31.315  1.00 20.98 ? 227 THR A O   1 
ATOM   1829 C  CB  . THR A 1 227 ? 17.551  -3.878  30.851  1.00 18.37 ? 227 THR A CB  1 
ATOM   1830 O  OG1 . THR A 1 227 ? 18.526  -4.880  31.032  1.00 19.03 ? 227 THR A OG1 1 
ATOM   1831 C  CG2 . THR A 1 227 ? 16.200  -4.530  30.429  1.00 20.17 ? 227 THR A CG2 1 
ATOM   1832 N  N   . ALA A 1 228 ? 20.413  -2.232  29.789  1.00 18.39 ? 228 ALA A N   1 
ATOM   1833 C  CA  . ALA A 1 228 ? 21.606  -1.665  30.377  1.00 18.60 ? 228 ALA A CA  1 
ATOM   1834 C  C   . ALA A 1 228 ? 21.662  -0.173  30.131  1.00 19.46 ? 228 ALA A C   1 
ATOM   1835 O  O   . ALA A 1 228 ? 22.347  0.538   30.918  1.00 20.46 ? 228 ALA A O   1 
ATOM   1836 C  CB  . ALA A 1 228 ? 22.883  -2.402  29.847  1.00 19.93 ? 228 ALA A CB  1 
ATOM   1837 N  N   . LEU A 1 229 ? 21.054  0.345   29.029  1.00 15.96 ? 229 LEU A N   1 
ATOM   1838 C  CA  . LEU A 1 229 ? 21.421  1.697   28.594  1.00 16.23 ? 229 LEU A CA  1 
ATOM   1839 C  C   . LEU A 1 229 ? 20.311  2.663   28.602  1.00 16.21 ? 229 LEU A C   1 
ATOM   1840 O  O   . LEU A 1 229 ? 19.125  2.243   28.445  1.00 16.41 ? 229 LEU A O   1 
ATOM   1841 C  CB  . LEU A 1 229 ? 22.042  1.688   27.185  1.00 16.18 ? 229 LEU A CB  1 
ATOM   1842 C  CG  . LEU A 1 229 ? 22.994  0.522   26.944  1.00 20.64 ? 229 LEU A CG  1 
ATOM   1843 C  CD1 . LEU A 1 229 ? 23.366  0.491   25.469  1.00 23.62 ? 229 LEU A CD1 1 
ATOM   1844 C  CD2 . LEU A 1 229 ? 24.230  0.704   27.823  1.00 19.65 ? 229 LEU A CD2 1 
ATOM   1845 N  N   . TYR A 1 230 ? 20.711  3.928   28.777  1.00 17.19 ? 230 TYR A N   1 
ATOM   1846 C  CA  . TYR A 1 230 ? 19.781  5.074   28.625  1.00 18.26 ? 230 TYR A CA  1 
ATOM   1847 C  C   . TYR A 1 230 ? 20.181  6.019   27.518  1.00 17.96 ? 230 TYR A C   1 
ATOM   1848 O  O   . TYR A 1 230 ? 21.352  6.149   27.152  1.00 17.06 ? 230 TYR A O   1 
ATOM   1849 C  CB  . TYR A 1 230 ? 19.737  5.944   29.922  1.00 20.85 ? 230 TYR A CB  1 
ATOM   1850 C  CG  . TYR A 1 230 ? 19.107  5.304   31.102  1.00 26.20 ? 230 TYR A CG  1 
ATOM   1851 C  CD1 . TYR A 1 230 ? 17.825  5.649   31.472  1.00 29.96 ? 230 TYR A CD1 1 
ATOM   1852 C  CD2 . TYR A 1 230 ? 19.818  4.400   31.891  1.00 30.66 ? 230 TYR A CD2 1 
ATOM   1853 C  CE1 . TYR A 1 230 ? 17.219  5.080   32.570  1.00 31.00 ? 230 TYR A CE1 1 
ATOM   1854 C  CE2 . TYR A 1 230 ? 19.215  3.830   33.011  1.00 37.03 ? 230 TYR A CE2 1 
ATOM   1855 C  CZ  . TYR A 1 230 ? 17.904  4.190   33.327  1.00 33.75 ? 230 TYR A CZ  1 
ATOM   1856 O  OH  . TYR A 1 230 ? 17.243  3.667   34.427  1.00 39.14 ? 230 TYR A OH  1 
ATOM   1857 N  N   A CYS A 1 231 ? 19.183  6.730   26.961  0.50 17.19 ? 231 CYS A N   1 
ATOM   1858 N  N   B CYS A 1 231 ? 19.183  6.723   26.986  0.50 18.93 ? 231 CYS A N   1 
ATOM   1859 C  CA  A CYS A 1 231 ? 19.394  7.729   25.917  0.50 17.55 ? 231 CYS A CA  1 
ATOM   1860 C  CA  B CYS A 1 231 ? 19.422  7.641   25.916  0.50 20.35 ? 231 CYS A CA  1 
ATOM   1861 C  C   A CYS A 1 231 ? 19.873  9.033   26.482  0.50 18.54 ? 231 CYS A C   1 
ATOM   1862 C  C   B CYS A 1 231 ? 19.566  9.081   26.428  0.50 20.17 ? 231 CYS A C   1 
ATOM   1863 O  O   A CYS A 1 231 ? 20.503  9.848   25.797  0.50 17.52 ? 231 CYS A O   1 
ATOM   1864 O  O   B CYS A 1 231 ? 19.758  10.037  25.650  0.50 21.06 ? 231 CYS A O   1 
ATOM   1865 C  CB  A CYS A 1 231 ? 18.084  8.029   25.197  0.50 16.07 ? 231 CYS A CB  1 
ATOM   1866 C  CB  B CYS A 1 231 ? 18.344  7.459   24.843  0.50 20.71 ? 231 CYS A CB  1 
ATOM   1867 S  SG  A CYS A 1 231 ? 17.545  6.717   24.103  0.50 13.17 ? 231 CYS A SG  1 
ATOM   1868 S  SG  B CYS A 1 231 ? 16.621  7.545   25.390  0.50 23.17 ? 231 CYS A SG  1 
ATOM   1869 N  N   . THR A 1 232 ? 19.564  9.200   27.768  1.00 21.17 ? 232 THR A N   1 
ATOM   1870 C  CA  . THR A 1 232 ? 19.759  10.438  28.463  1.00 21.50 ? 232 THR A CA  1 
ATOM   1871 C  C   . THR A 1 232 ? 21.071  10.521  29.276  1.00 20.77 ? 232 THR A C   1 
ATOM   1872 O  O   . THR A 1 232 ? 21.697  9.485   29.628  1.00 19.09 ? 232 THR A O   1 
ATOM   1873 C  CB  . THR A 1 232 ? 18.529  10.651  29.360  1.00 20.23 ? 232 THR A CB  1 
ATOM   1874 O  OG1 . THR A 1 232 ? 18.218  9.447   30.067  1.00 20.19 ? 232 THR A OG1 1 
ATOM   1875 C  CG2 . THR A 1 232 ? 17.313  11.080  28.464  1.00 23.21 ? 232 THR A CG2 1 
ATOM   1876 N  N   . HIS A 1 233 ? 21.534  11.774  29.491  1.00 21.37 ? 233 HIS A N   1 
ATOM   1877 C  CA  . HIS A 1 233 ? 22.684  12.034  30.429  1.00 24.99 ? 233 HIS A CA  1 
ATOM   1878 C  C   . HIS A 1 233 ? 22.362  11.630  31.862  1.00 23.56 ? 233 HIS A C   1 
ATOM   1879 O  O   . HIS A 1 233 ? 21.197  11.533  32.285  1.00 25.29 ? 233 HIS A O   1 
ATOM   1880 C  CB  . HIS A 1 233 ? 23.091  13.510  30.417  1.00 25.61 ? 233 HIS A CB  1 
ATOM   1881 C  CG  . HIS A 1 233 ? 23.741  13.959  29.123  1.00 30.04 ? 233 HIS A CG  1 
ATOM   1882 N  ND1 . HIS A 1 233 ? 23.093  14.700  28.215  1.00 36.49 ? 233 HIS A ND1 1 
ATOM   1883 C  CD2 . HIS A 1 233 ? 25.024  13.724  28.603  1.00 31.78 ? 233 HIS A CD2 1 
ATOM   1884 C  CE1 . HIS A 1 233 ? 23.909  14.953  27.167  1.00 33.54 ? 233 HIS A CE1 1 
ATOM   1885 N  NE2 . HIS A 1 233 ? 25.089  14.347  27.397  1.00 30.90 ? 233 HIS A NE2 1 
ATOM   1886 N  N   . MET A 1 234 ? 23.417  11.396  32.630  1.00 24.02 ? 234 MET A N   1 
ATOM   1887 C  CA  . MET A 1 234 ? 23.248  10.841  33.963  1.00 24.45 ? 234 MET A CA  1 
ATOM   1888 C  C   . MET A 1 234 ? 22.422  11.782  34.853  1.00 25.08 ? 234 MET A C   1 
ATOM   1889 O  O   . MET A 1 234 ? 21.586  11.353  35.655  1.00 22.79 ? 234 MET A O   1 
ATOM   1890 C  CB  . MET A 1 234 ? 24.591  10.493  34.559  1.00 27.56 ? 234 MET A CB  1 
ATOM   1891 C  CG  . MET A 1 234 ? 24.541  10.147  36.040  1.00 28.37 ? 234 MET A CG  1 
ATOM   1892 S  SD  . MET A 1 234 ? 26.157  9.506   36.596  1.00 32.15 ? 234 MET A SD  1 
ATOM   1893 C  CE  . MET A 1 234 ? 27.319  10.689  35.909  1.00 34.40 ? 234 MET A CE  1 
ATOM   1894 N  N   . ASP A 1 235 ? 22.622  13.087  34.664  1.00 27.31 ? 235 ASP A N   1 
ATOM   1895 C  CA  . ASP A 1 235 ? 21.916  14.053  35.514  1.00 28.88 ? 235 ASP A CA  1 
ATOM   1896 C  C   . ASP A 1 235 ? 20.536  14.504  35.014  1.00 32.28 ? 235 ASP A C   1 
ATOM   1897 O  O   . ASP A 1 235 ? 19.844  15.318  35.661  1.00 28.86 ? 235 ASP A O   1 
ATOM   1898 C  CB  . ASP A 1 235 ? 22.813  15.274  35.795  1.00 34.83 ? 235 ASP A CB  1 
ATOM   1899 C  CG  . ASP A 1 235 ? 22.834  16.293  34.623  1.00 42.93 ? 235 ASP A CG  1 
ATOM   1900 O  OD1 . ASP A 1 235 ? 22.571  15.929  33.431  1.00 42.98 ? 235 ASP A OD1 1 
ATOM   1901 O  OD2 . ASP A 1 235 ? 23.114  17.481  34.910  1.00 46.00 ? 235 ASP A OD2 1 
ATOM   1902 N  N   . ASP A 1 236 ? 20.102  13.966  33.881  1.00 28.82 ? 236 ASP A N   1 
ATOM   1903 C  CA  . ASP A 1 236 ? 18.766  14.224  33.378  1.00 30.70 ? 236 ASP A CA  1 
ATOM   1904 C  C   . ASP A 1 236 ? 17.675  13.828  34.380  1.00 32.08 ? 236 ASP A C   1 
ATOM   1905 O  O   . ASP A 1 236 ? 17.581  12.669  34.796  1.00 31.13 ? 236 ASP A O   1 
ATOM   1906 C  CB  . ASP A 1 236 ? 18.568  13.515  32.020  1.00 28.17 ? 236 ASP A CB  1 
ATOM   1907 C  CG  . ASP A 1 236 ? 17.451  14.141  31.195  1.00 32.72 ? 236 ASP A CG  1 
ATOM   1908 O  OD1 . ASP A 1 236 ? 16.433  14.542  31.785  1.00 35.39 ? 236 ASP A OD1 1 
ATOM   1909 O  OD2 . ASP A 1 236 ? 17.557  14.224  29.942  1.00 31.79 ? 236 ASP A OD2 1 
ATOM   1910 N  N   . PRO A 1 237 ? 16.853  14.808  34.806  1.00 33.77 ? 237 PRO A N   1 
ATOM   1911 C  CA  . PRO A 1 237 ? 15.795  14.494  35.769  1.00 34.13 ? 237 PRO A CA  1 
ATOM   1912 C  C   . PRO A 1 237 ? 14.687  13.646  35.156  1.00 34.04 ? 237 PRO A C   1 
ATOM   1913 O  O   . PRO A 1 237 ? 13.850  13.118  35.874  1.00 31.64 ? 237 PRO A O   1 
ATOM   1914 C  CB  . PRO A 1 237 ? 15.246  15.889  36.150  1.00 33.95 ? 237 PRO A CB  1 
ATOM   1915 C  CG  . PRO A 1 237 ? 15.455  16.694  34.905  1.00 38.27 ? 237 PRO A CG  1 
ATOM   1916 C  CD  . PRO A 1 237 ? 16.798  16.220  34.370  1.00 35.97 ? 237 PRO A CD  1 
ATOM   1917 N  N   . SER A 1 238 ? 14.682  13.506  33.827  1.00 33.79 ? 238 SER A N   1 
ATOM   1918 C  CA  . SER A 1 238 ? 13.693  12.657  33.170  1.00 35.60 ? 238 SER A CA  1 
ATOM   1919 C  C   . SER A 1 238 ? 14.403  11.575  32.311  1.00 31.46 ? 238 SER A C   1 
ATOM   1920 O  O   . SER A 1 238 ? 14.536  11.746  31.085  1.00 30.16 ? 238 SER A O   1 
ATOM   1921 C  CB  . SER A 1 238 ? 12.721  13.519  32.337  1.00 37.07 ? 238 SER A CB  1 
ATOM   1922 O  OG  . SER A 1 238 ? 13.395  14.631  31.749  1.00 49.27 ? 238 SER A OG  1 
ATOM   1923 N  N   . PRO A 1 239 ? 14.869  10.480  32.964  1.00 28.61 ? 239 PRO A N   1 
ATOM   1924 C  CA  . PRO A 1 239 ? 15.698  9.482   32.207  1.00 27.50 ? 239 PRO A CA  1 
ATOM   1925 C  C   . PRO A 1 239 ? 14.827  8.709   31.190  1.00 28.82 ? 239 PRO A C   1 
ATOM   1926 O  O   . PRO A 1 239 ? 13.648  8.406   31.469  1.00 29.91 ? 239 PRO A O   1 
ATOM   1927 C  CB  . PRO A 1 239 ? 16.208  8.548   33.294  1.00 28.94 ? 239 PRO A CB  1 
ATOM   1928 C  CG  . PRO A 1 239 ? 15.233  8.722   34.442  1.00 32.52 ? 239 PRO A CG  1 
ATOM   1929 C  CD  . PRO A 1 239 ? 14.861  10.185  34.405  1.00 27.67 ? 239 PRO A CD  1 
ATOM   1930 N  N   . ARG A 1 240 ? 15.403  8.448   30.012  1.00 25.09 ? 240 ARG A N   1 
ATOM   1931 C  CA  . ARG A 1 240 ? 14.756  7.625   28.994  1.00 27.06 ? 240 ARG A CA  1 
ATOM   1932 C  C   . ARG A 1 240 ? 15.597  6.357   28.713  1.00 22.52 ? 240 ARG A C   1 
ATOM   1933 O  O   . ARG A 1 240 ? 16.764  6.402   28.375  1.00 22.23 ? 240 ARG A O   1 
ATOM   1934 C  CB  . ARG A 1 240 ? 14.544  8.393   27.676  1.00 30.51 ? 240 ARG A CB  1 
ATOM   1935 C  CG  . ARG A 1 240 ? 13.777  9.732   27.709  1.00 39.10 ? 240 ARG A CG  1 
ATOM   1936 C  CD  . ARG A 1 240 ? 13.833  10.511  26.368  1.00 35.22 ? 240 ARG A CD  1 
ATOM   1937 N  NE  . ARG A 1 240 ? 14.930  11.510  26.171  1.00 37.22 ? 240 ARG A NE  1 
ATOM   1938 C  CZ  . ARG A 1 240 ? 15.904  11.476  25.216  1.00 41.80 ? 240 ARG A CZ  1 
ATOM   1939 N  NH1 . ARG A 1 240 ? 16.013  10.480  24.329  1.00 37.62 ? 240 ARG A NH1 1 
ATOM   1940 N  NH2 . ARG A 1 240 ? 16.817  12.449  25.127  1.00 39.76 ? 240 ARG A NH2 1 
ATOM   1941 N  N   . GLU A 1 241 ? 14.964  5.227   28.830  1.00 20.36 ? 241 GLU A N   1 
ATOM   1942 C  CA  . GLU A 1 241 ? 15.620  3.967   28.471  1.00 22.95 ? 241 GLU A CA  1 
ATOM   1943 C  C   . GLU A 1 241 ? 15.994  3.949   26.989  1.00 18.75 ? 241 GLU A C   1 
ATOM   1944 O  O   . GLU A 1 241 ? 15.218  4.377   26.145  1.00 18.98 ? 241 GLU A O   1 
ATOM   1945 C  CB  . GLU A 1 241 ? 14.666  2.834   28.703  1.00 25.72 ? 241 GLU A CB  1 
ATOM   1946 C  CG  . GLU A 1 241 ? 14.499  2.376   30.134  1.00 30.86 ? 241 GLU A CG  1 
ATOM   1947 C  CD  . GLU A 1 241 ? 13.320  1.460   30.283  1.00 35.63 ? 241 GLU A CD  1 
ATOM   1948 O  OE1 . GLU A 1 241 ? 12.454  1.425   29.374  1.00 47.12 ? 241 GLU A OE1 1 
ATOM   1949 O  OE2 . GLU A 1 241 ? 13.231  0.781   31.321  1.00 42.04 ? 241 GLU A OE2 1 
ATOM   1950 N  N   . MET A 1 242 ? 17.135  3.338   26.659  1.00 16.86 ? 242 MET A N   1 
ATOM   1951 C  CA  . MET A 1 242 ? 17.469  3.152   25.249  1.00 13.86 ? 242 MET A CA  1 
ATOM   1952 C  C   . MET A 1 242 ? 16.929  1.793   24.798  1.00 12.78 ? 242 MET A C   1 
ATOM   1953 O  O   . MET A 1 242 ? 17.581  0.720   25.036  1.00 13.98 ? 242 MET A O   1 
ATOM   1954 C  CB  . MET A 1 242 ? 18.989  3.227   25.032  1.00 13.77 ? 242 MET A CB  1 
ATOM   1955 C  CG  . MET A 1 242 ? 19.405  3.158   23.543  1.00 14.45 ? 242 MET A CG  1 
ATOM   1956 S  SD  . MET A 1 242 ? 21.215  3.109   23.401  1.00 15.21 ? 242 MET A SD  1 
ATOM   1957 C  CE  . MET A 1 242 ? 21.464  4.831   23.866  1.00 17.83 ? 242 MET A CE  1 
ATOM   1958 N  N   . ILE A 1 243 ? 15.754  1.828   24.100  1.00 12.54 ? 243 ILE A N   1 
ATOM   1959 C  CA  . ILE A 1 243 ? 15.067  0.660   23.607  1.00 11.78 ? 243 ILE A CA  1 
ATOM   1960 C  C   . ILE A 1 243 ? 14.468  1.016   22.221  1.00 11.75 ? 243 ILE A C   1 
ATOM   1961 O  O   . ILE A 1 243 ? 14.282  2.226   21.891  1.00 12.04 ? 243 ILE A O   1 
ATOM   1962 C  CB  . ILE A 1 243 ? 13.923  0.240   24.574  1.00 14.95 ? 243 ILE A CB  1 
ATOM   1963 C  CG1 . ILE A 1 243 ? 13.032  1.439   24.929  1.00 14.23 ? 243 ILE A CG1 1 
ATOM   1964 C  CG2 . ILE A 1 243 ? 14.502  -0.631  25.753  1.00 15.33 ? 243 ILE A CG2 1 
ATOM   1965 C  CD1 . ILE A 1 243 ? 11.814  1.021   25.814  1.00 15.39 ? 243 ILE A CD1 1 
ATOM   1966 N  N   . ASN A 1 244 ? 14.110  -0.018  21.461  1.00 10.57 ? 244 ASN A N   1 
ATOM   1967 C  CA  . ASN A 1 244 ? 13.424  0.198   20.149  1.00 10.99 ? 244 ASN A CA  1 
ATOM   1968 C  C   . ASN A 1 244 ? 14.171  1.177   19.266  1.00 12.46 ? 244 ASN A C   1 
ATOM   1969 O  O   . ASN A 1 244 ? 13.576  2.046   18.641  1.00 12.29 ? 244 ASN A O   1 
ATOM   1970 C  CB  . ASN A 1 244 ? 11.958  0.646   20.394  1.00 11.14 ? 244 ASN A CB  1 
ATOM   1971 C  CG  . ASN A 1 244 ? 11.246  -0.265  21.359  1.00 12.02 ? 244 ASN A CG  1 
ATOM   1972 O  OD1 . ASN A 1 244 ? 11.381  -1.480  21.281  1.00 13.71 ? 244 ASN A OD1 1 
ATOM   1973 N  ND2 . ASN A 1 244 ? 10.427  0.307   22.314  1.00 14.34 ? 244 ASN A ND2 1 
ATOM   1974 N  N   . ASN A 1 245 ? 15.514  1.045   19.243  1.00 9.86  ? 245 ASN A N   1 
ATOM   1975 C  CA  . ASN A 1 245 ? 16.357  1.949   18.517  1.00 9.52  ? 245 ASN A CA  1 
ATOM   1976 C  C   . ASN A 1 245 ? 16.631  1.397   17.131  1.00 8.50  ? 245 ASN A C   1 
ATOM   1977 O  O   . ASN A 1 245 ? 17.801  1.149   16.745  1.00 9.62  ? 245 ASN A O   1 
ATOM   1978 C  CB  . ASN A 1 245 ? 17.633  2.307   19.289  1.00 10.78 ? 245 ASN A CB  1 
ATOM   1979 C  CG  . ASN A 1 245 ? 18.488  1.080   19.629  1.00 10.56 ? 245 ASN A CG  1 
ATOM   1980 O  OD1 . ASN A 1 245 ? 18.016  -0.087  19.681  1.00 11.35 ? 245 ASN A OD1 1 
ATOM   1981 N  ND2 . ASN A 1 245 ? 19.788  1.365   19.922  1.00 10.81 ? 245 ASN A ND2 1 
ATOM   1982 N  N   . PHE A 1 246 ? 15.575  1.155   16.381  1.00 8.12  ? 246 PHE A N   1 
ATOM   1983 C  CA  . PHE A 1 246 ? 15.633  0.692   15.014  1.00 8.94  ? 246 PHE A CA  1 
ATOM   1984 C  C   . PHE A 1 246 ? 14.620  1.495   14.193  1.00 9.39  ? 246 PHE A C   1 
ATOM   1985 O  O   . PHE A 1 246 ? 13.591  1.908   14.726  1.00 10.01 ? 246 PHE A O   1 
ATOM   1986 C  CB  . PHE A 1 246 ? 15.306  -0.849  14.960  1.00 9.36  ? 246 PHE A CB  1 
ATOM   1987 C  CG  . PHE A 1 246 ? 13.912  -1.221  15.396  1.00 9.32  ? 246 PHE A CG  1 
ATOM   1988 C  CD1 . PHE A 1 246 ? 12.845  -1.319  14.447  1.00 9.98  ? 246 PHE A CD1 1 
ATOM   1989 C  CD2 . PHE A 1 246 ? 13.636  -1.429  16.738  1.00 9.24  ? 246 PHE A CD2 1 
ATOM   1990 C  CE1 . PHE A 1 246 ? 11.533  -1.640  14.885  1.00 10.23 ? 246 PHE A CE1 1 
ATOM   1991 C  CE2 . PHE A 1 246 ? 12.343  -1.793  17.164  1.00 11.28 ? 246 PHE A CE2 1 
ATOM   1992 C  CZ  . PHE A 1 246 ? 11.274  -1.842  16.250  1.00 10.16 ? 246 PHE A CZ  1 
ATOM   1993 N  N   . ARG A 1 247 ? 14.902  1.616   12.894  1.00 8.45  ? 247 ARG A N   1 
ATOM   1994 C  CA  . ARG A 1 247 ? 13.982  2.202   11.927  1.00 8.80  ? 247 ARG A CA  1 
ATOM   1995 C  C   . ARG A 1 247 ? 13.011  1.199   11.397  1.00 8.16  ? 247 ARG A C   1 
ATOM   1996 O  O   . ARG A 1 247 ? 13.362  0.055   11.122  1.00 8.26  ? 247 ARG A O   1 
ATOM   1997 C  CB  . ARG A 1 247 ? 14.765  2.902   10.833  1.00 7.79  ? 247 ARG A CB  1 
ATOM   1998 C  CG  . ARG A 1 247 ? 13.927  3.924   9.993   1.00 7.27  ? 247 ARG A CG  1 
ATOM   1999 C  CD  . ARG A 1 247 ? 14.788  4.364   8.807   1.00 8.15  ? 247 ARG A CD  1 
ATOM   2000 N  NE  . ARG A 1 247 ? 14.159  5.533   8.169   1.00 7.91  ? 247 ARG A NE  1 
ATOM   2001 C  CZ  . ARG A 1 247 ? 14.637  6.109   7.077   1.00 8.52  ? 247 ARG A CZ  1 
ATOM   2002 N  NH1 . ARG A 1 247 ? 15.665  5.527   6.369   1.00 8.95  ? 247 ARG A NH1 1 
ATOM   2003 N  NH2 . ARG A 1 247 ? 14.028  7.240   6.633   1.00 9.10  ? 247 ARG A NH2 1 
ATOM   2004 N  N   . GLN A 1 248 ? 11.720  1.575   11.248  1.00 8.72  ? 248 GLN A N   1 
ATOM   2005 C  CA  . GLN A 1 248 ? 10.783  0.788   10.475  1.00 8.53  ? 248 GLN A CA  1 
ATOM   2006 C  C   . GLN A 1 248 ? 11.252  0.469   9.040   1.00 9.13  ? 248 GLN A C   1 
ATOM   2007 O  O   . GLN A 1 248 ? 11.963  1.276   8.430   1.00 8.94  ? 248 GLN A O   1 
ATOM   2008 C  CB  . GLN A 1 248 ? 9.408   1.440   10.370  1.00 9.14  ? 248 GLN A CB  1 
ATOM   2009 C  CG  . GLN A 1 248 ? 8.733   1.702   11.718  1.00 9.57  ? 248 GLN A CG  1 
ATOM   2010 C  CD  . GLN A 1 248 ? 8.392   0.452   12.477  1.00 10.49 ? 248 GLN A CD  1 
ATOM   2011 O  OE1 . GLN A 1 248 ? 9.146   0.026   13.358  1.00 10.18 ? 248 GLN A OE1 1 
ATOM   2012 N  NE2 . GLN A 1 248 ? 7.282   -0.135  12.147  1.00 10.96 ? 248 GLN A NE2 1 
ATOM   2013 N  N   . VAL A 1 249 ? 10.821  -0.630  8.477   1.00 9.09  ? 249 VAL A N   1 
ATOM   2014 C  CA  . VAL A 1 249 ? 11.186  -0.970  7.113   1.00 9.85  ? 249 VAL A CA  1 
ATOM   2015 C  C   . VAL A 1 249 ? 10.582  0.002   6.138   1.00 10.16 ? 249 VAL A C   1 
ATOM   2016 O  O   . VAL A 1 249 ? 9.423   0.534   6.365   1.00 10.52 ? 249 VAL A O   1 
ATOM   2017 C  CB  . VAL A 1 249 ? 10.808  -2.434  6.715   1.00 11.02 ? 249 VAL A CB  1 
ATOM   2018 C  CG1 . VAL A 1 249 ? 11.696  -3.456  7.477   1.00 11.51 ? 249 VAL A CG1 1 
ATOM   2019 C  CG2 . VAL A 1 249 ? 9.341   -2.772  6.850   1.00 13.54 ? 249 VAL A CG2 1 
ATOM   2020 N  N   . GLN A 1 250 ? 11.332  0.239   5.030   1.00 9.54  ? 250 GLN A N   1 
ATOM   2021 C  CA  . GLN A 1 250 ? 10.928  1.222   4.019   1.00 9.97  ? 250 GLN A CA  1 
ATOM   2022 C  C   . GLN A 1 250 ? 10.288  0.536   2.826   1.00 10.66 ? 250 GLN A C   1 
ATOM   2023 O  O   . GLN A 1 250 ? 10.611  -0.600  2.507   1.00 10.44 ? 250 GLN A O   1 
ATOM   2024 C  CB  . GLN A 1 250 ? 12.163  1.999   3.508   1.00 8.22  ? 250 GLN A CB  1 
ATOM   2025 C  CG  . GLN A 1 250 ? 12.987  2.601   4.662   1.00 8.63  ? 250 GLN A CG  1 
ATOM   2026 C  CD  . GLN A 1 250 ? 12.235  3.694   5.377   1.00 8.95  ? 250 GLN A CD  1 
ATOM   2027 O  OE1 . GLN A 1 250 ? 11.964  4.724   4.762   1.00 10.40 ? 250 GLN A OE1 1 
ATOM   2028 N  NE2 . GLN A 1 250 ? 11.955  3.563   6.653   1.00 7.97  ? 250 GLN A NE2 1 
ATOM   2029 N  N   . LYS A 1 251 ? 9.458   1.255   2.056   1.00 8.94  ? 251 LYS A N   1 
ATOM   2030 C  CA  . LYS A 1 251 ? 8.999   0.694   0.792   1.00 10.11 ? 251 LYS A CA  1 
ATOM   2031 C  C   . LYS A 1 251 ? 10.205  0.442   -0.144  1.00 11.02 ? 251 LYS A C   1 
ATOM   2032 O  O   . LYS A 1 251 ? 11.177  1.236   -0.121  1.00 11.74 ? 251 LYS A O   1 
ATOM   2033 C  CB  . LYS A 1 251 ? 8.058   1.728   0.138   1.00 9.40  ? 251 LYS A CB  1 
ATOM   2034 C  CG  . LYS A 1 251 ? 6.718   1.770   0.911   1.00 11.91 ? 251 LYS A CG  1 
ATOM   2035 C  CD  . LYS A 1 251 ? 5.702   2.533   0.210   1.00 11.63 ? 251 LYS A CD  1 
ATOM   2036 C  CE  . LYS A 1 251 ? 4.232   2.238   0.649   1.00 11.60 ? 251 LYS A CE  1 
ATOM   2037 N  NZ  . LYS A 1 251 ? 4.021   2.328   2.134   1.00 10.69 ? 251 LYS A NZ  1 
ATOM   2038 N  N   . PHE A 1 252 ? 10.172  -0.624  -0.913  1.00 12.93 ? 252 PHE A N   1 
ATOM   2039 C  CA  . PHE A 1 252 ? 11.290  -1.034  -1.766  1.00 14.84 ? 252 PHE A CA  1 
ATOM   2040 C  C   . PHE A 1 252 ? 10.592  -1.668  -2.972  1.00 19.15 ? 252 PHE A C   1 
ATOM   2041 O  O   . PHE A 1 252 ? 10.194  -2.848  -2.917  1.00 23.40 ? 252 PHE A O   1 
ATOM   2042 C  CB  . PHE A 1 252 ? 12.057  -2.149  -1.053  1.00 17.26 ? 252 PHE A CB  1 
ATOM   2043 C  CG  . PHE A 1 252 ? 13.303  -2.579  -1.736  1.00 18.20 ? 252 PHE A CG  1 
ATOM   2044 C  CD1 . PHE A 1 252 ? 14.442  -1.819  -1.675  1.00 17.49 ? 252 PHE A CD1 1 
ATOM   2045 C  CD2 . PHE A 1 252 ? 13.330  -3.794  -2.437  1.00 20.80 ? 252 PHE A CD2 1 
ATOM   2046 C  CE1 . PHE A 1 252 ? 15.610  -2.271  -2.313  1.00 19.38 ? 252 PHE A CE1 1 
ATOM   2047 C  CE2 . PHE A 1 252 ? 14.519  -4.267  -3.042  1.00 20.56 ? 252 PHE A CE2 1 
ATOM   2048 C  CZ  . PHE A 1 252 ? 15.639  -3.480  -2.963  1.00 19.79 ? 252 PHE A CZ  1 
ATOM   2049 N  N   . ASP A 1 253 ? 10.358  -0.872  -3.997  1.00 24.61 ? 253 ASP A N   1 
ATOM   2050 C  CA  . ASP A 1 253 ? 9.438   -1.299  -5.115  1.00 24.98 ? 253 ASP A CA  1 
ATOM   2051 C  C   . ASP A 1 253 ? 10.180  -1.295  -6.450  1.00 24.28 ? 253 ASP A C   1 
ATOM   2052 O  O   . ASP A 1 253 ? 10.978  -0.424  -6.675  1.00 23.72 ? 253 ASP A O   1 
ATOM   2053 C  CB  . ASP A 1 253 ? 8.238   -0.356  -5.218  1.00 31.32 ? 253 ASP A CB  1 
ATOM   2054 C  CG  . ASP A 1 253 ? 7.175   -0.909  -6.114  1.00 39.60 ? 253 ASP A CG  1 
ATOM   2055 O  OD1 . ASP A 1 253 ? 6.907   -2.139  -6.009  1.00 44.56 ? 253 ASP A OD1 1 
ATOM   2056 O  OD2 . ASP A 1 253 ? 6.614   -0.148  -6.937  1.00 43.54 ? 253 ASP A OD2 1 
ATOM   2057 N  N   . GLU A 1 254 ? 9.913   -2.291  -7.320  1.00 25.73 ? 254 GLU A N   1 
ATOM   2058 C  CA  . GLU A 1 254 ? 10.602  -2.364  -8.621  1.00 26.14 ? 254 GLU A CA  1 
ATOM   2059 C  C   . GLU A 1 254 ? 12.139  -2.446  -8.447  1.00 23.68 ? 254 GLU A C   1 
ATOM   2060 O  O   . GLU A 1 254 ? 12.935  -1.989  -9.269  1.00 25.22 ? 254 GLU A O   1 
ATOM   2061 C  CB  . GLU A 1 254 ? 10.123  -1.233  -9.549  1.00 28.48 ? 254 GLU A CB  1 
ATOM   2062 C  CG  . GLU A 1 254 ? 8.619   -1.338  -9.785  1.00 30.20 ? 254 GLU A CG  1 
ATOM   2063 C  CD  . GLU A 1 254 ? 8.052   -0.237  -10.652 1.00 38.67 ? 254 GLU A CD  1 
ATOM   2064 O  OE1 . GLU A 1 254 ? 8.681   0.847   -10.748 1.00 35.58 ? 254 GLU A OE1 1 
ATOM   2065 O  OE2 . GLU A 1 254 ? 6.950   -0.447  -11.214 1.00 41.13 ? 254 GLU A OE2 1 
ATOM   2066 N  N   . ARG A 1 255 ? 12.537  -3.079  -7.360  1.00 22.79 ? 255 ARG A N   1 
ATOM   2067 C  CA  . ARG A 1 255 ? 13.992  -3.280  -7.088  1.00 22.49 ? 255 ARG A CA  1 
ATOM   2068 C  C   . ARG A 1 255 ? 14.255  -4.692  -6.552  1.00 22.90 ? 255 ARG A C   1 
ATOM   2069 O  O   . ARG A 1 255 ? 13.356  -5.369  -6.021  1.00 22.23 ? 255 ARG A O   1 
ATOM   2070 C  CB  . ARG A 1 255 ? 14.464  -2.277  -6.065  1.00 22.41 ? 255 ARG A CB  1 
ATOM   2071 C  CG  . ARG A 1 255 ? 14.469  -0.837  -6.548  1.00 23.74 ? 255 ARG A CG  1 
ATOM   2072 C  CD  . ARG A 1 255 ? 14.994  0.092   -5.467  1.00 21.90 ? 255 ARG A CD  1 
ATOM   2073 N  NE  . ARG A 1 255 ? 16.388  -0.307  -5.251  1.00 22.88 ? 255 ARG A NE  1 
ATOM   2074 C  CZ  . ARG A 1 255 ? 17.086  -0.016  -4.157  1.00 22.46 ? 255 ARG A CZ  1 
ATOM   2075 N  NH1 . ARG A 1 255 ? 16.507  0.675   -3.146  1.00 22.71 ? 255 ARG A NH1 1 
ATOM   2076 N  NH2 . ARG A 1 255 ? 18.328  -0.481  -4.084  1.00 17.86 ? 255 ARG A NH2 1 
ATOM   2077 N  N   . LEU A 1 256 ? 15.504  -5.142  -6.716  1.00 21.38 ? 256 LEU A N   1 
ATOM   2078 C  CA  . LEU A 1 256 ? 15.897  -6.489  -6.332  1.00 18.69 ? 256 LEU A CA  1 
ATOM   2079 C  C   . LEU A 1 256 ? 16.917  -6.380  -5.162  1.00 17.99 ? 256 LEU A C   1 
ATOM   2080 O  O   . LEU A 1 256 ? 17.653  -5.381  -5.030  1.00 20.57 ? 256 LEU A O   1 
ATOM   2081 C  CB  . LEU A 1 256 ? 16.530  -7.210  -7.523  1.00 22.87 ? 256 LEU A CB  1 
ATOM   2082 C  CG  . LEU A 1 256 ? 15.507  -7.456  -8.660  1.00 23.57 ? 256 LEU A CG  1 
ATOM   2083 C  CD1 . LEU A 1 256 ? 16.262  -8.092  -9.787  1.00 28.37 ? 256 LEU A CD1 1 
ATOM   2084 C  CD2 . LEU A 1 256 ? 14.363  -8.387  -8.251  1.00 28.37 ? 256 LEU A CD2 1 
ATOM   2085 N  N   . VAL A 1 257 ? 16.888  -7.431  -4.358  1.00 17.39 ? 257 VAL A N   1 
ATOM   2086 C  CA  . VAL A 1 257 ? 17.978  -7.678  -3.485  1.00 15.17 ? 257 VAL A CA  1 
ATOM   2087 C  C   . VAL A 1 257 ? 18.747  -8.881  -4.071  1.00 15.34 ? 257 VAL A C   1 
ATOM   2088 O  O   . VAL A 1 257 ? 18.127  -9.935  -4.360  1.00 16.55 ? 257 VAL A O   1 
ATOM   2089 C  CB  . VAL A 1 257 ? 17.468  -7.965  -2.082  1.00 18.35 ? 257 VAL A CB  1 
ATOM   2090 C  CG1 . VAL A 1 257 ? 18.578  -8.482  -1.215  1.00 17.79 ? 257 VAL A CG1 1 
ATOM   2091 C  CG2 . VAL A 1 257 ? 16.863  -6.706  -1.508  1.00 18.95 ? 257 VAL A CG2 1 
ATOM   2092 N  N   . TYR A 1 258 ? 20.051  -8.779  -4.222  1.00 13.39 ? 258 TYR A N   1 
ATOM   2093 C  CA  . TYR A 1 258 ? 20.797  -9.841  -4.837  1.00 14.55 ? 258 TYR A CA  1 
ATOM   2094 C  C   . TYR A 1 258 ? 21.306  -10.756 -3.758  1.00 15.05 ? 258 TYR A C   1 
ATOM   2095 O  O   . TYR A 1 258 ? 21.620  -10.301 -2.654  1.00 15.16 ? 258 TYR A O   1 
ATOM   2096 C  CB  . TYR A 1 258 ? 21.922  -9.263  -5.638  1.00 14.07 ? 258 TYR A CB  1 
ATOM   2097 C  CG  . TYR A 1 258 ? 21.327  -8.335  -6.689  1.00 19.86 ? 258 TYR A CG  1 
ATOM   2098 C  CD1 . TYR A 1 258 ? 20.768  -8.870  -7.868  1.00 18.29 ? 258 TYR A CD1 1 
ATOM   2099 C  CD2 . TYR A 1 258 ? 21.243  -6.972  -6.469  1.00 19.14 ? 258 TYR A CD2 1 
ATOM   2100 C  CE1 . TYR A 1 258 ? 20.224  -8.036  -8.841  1.00 23.01 ? 258 TYR A CE1 1 
ATOM   2101 C  CE2 . TYR A 1 258 ? 20.639  -6.158  -7.412  1.00 20.57 ? 258 TYR A CE2 1 
ATOM   2102 C  CZ  . TYR A 1 258 ? 20.140  -6.702  -8.577  1.00 21.57 ? 258 TYR A CZ  1 
ATOM   2103 O  OH  . TYR A 1 258 ? 19.587  -5.833  -9.499  1.00 28.45 ? 258 TYR A OH  1 
ATOM   2104 N  N   . THR A 1 259 ? 21.385  -12.045 -4.054  1.00 14.07 ? 259 THR A N   1 
ATOM   2105 C  CA  . THR A 1 259 ? 21.816  -13.021 -3.059  1.00 13.71 ? 259 THR A CA  1 
ATOM   2106 C  C   . THR A 1 259 ? 23.012  -13.787 -3.547  1.00 12.81 ? 259 THR A C   1 
ATOM   2107 O  O   . THR A 1 259 ? 23.129  -14.085 -4.770  1.00 14.53 ? 259 THR A O   1 
ATOM   2108 C  CB  . THR A 1 259 ? 20.681  -14.024 -2.663  1.00 13.68 ? 259 THR A CB  1 
ATOM   2109 O  OG1 . THR A 1 259 ? 20.262  -14.691 -3.844  1.00 16.28 ? 259 THR A OG1 1 
ATOM   2110 C  CG2 . THR A 1 259 ? 19.502  -13.307 -2.076  1.00 14.70 ? 259 THR A CG2 1 
ATOM   2111 N  N   . SER A 1 260 ? 23.922  -14.109 -2.668  1.00 11.95 ? 260 SER A N   1 
ATOM   2112 C  CA  . SER A 1 260 ? 25.086  -14.937 -3.061  1.00 13.04 ? 260 SER A CA  1 
ATOM   2113 C  C   . SER A 1 260 ? 24.767  -16.440 -3.072  1.00 17.16 ? 260 SER A C   1 
ATOM   2114 O  O   . SER A 1 260 ? 25.624  -17.245 -3.429  1.00 17.41 ? 260 SER A O   1 
ATOM   2115 C  CB  . SER A 1 260 ? 26.271  -14.650 -2.173  1.00 13.79 ? 260 SER A CB  1 
ATOM   2116 O  OG  . SER A 1 260 ? 25.933  -15.148 -0.858  1.00 13.38 ? 260 SER A OG  1 
ATOM   2117 N  N   . PHE A 1 261 ? 23.544  -16.776 -2.684  1.00 16.49 ? 261 PHE A N   1 
ATOM   2118 C  CA  . PHE A 1 261 ? 23.114  -18.193 -2.593  1.00 17.60 ? 261 PHE A CA  1 
ATOM   2119 C  C   . PHE A 1 261 ? 21.881  -18.374 -3.464  1.00 20.92 ? 261 PHE A C   1 
ATOM   2120 O  O   . PHE A 1 261 ? 21.122  -17.450 -3.675  1.00 20.72 ? 261 PHE A O   1 
ATOM   2121 C  CB  . PHE A 1 261 ? 22.836  -18.538 -1.117  1.00 15.26 ? 261 PHE A CB  1 
ATOM   2122 C  CG  . PHE A 1 261 ? 21.894  -17.599 -0.449  1.00 15.29 ? 261 PHE A CG  1 
ATOM   2123 C  CD1 . PHE A 1 261 ? 20.507  -17.842 -0.391  1.00 16.24 ? 261 PHE A CD1 1 
ATOM   2124 C  CD2 . PHE A 1 261 ? 22.377  -16.413 0.081   1.00 15.16 ? 261 PHE A CD2 1 
ATOM   2125 C  CE1 . PHE A 1 261 ? 19.645  -16.947 0.172   1.00 16.27 ? 261 PHE A CE1 1 
ATOM   2126 C  CE2 . PHE A 1 261 ? 21.522  -15.516 0.652   1.00 16.86 ? 261 PHE A CE2 1 
ATOM   2127 C  CZ  . PHE A 1 261 ? 20.138  -15.782 0.719   1.00 15.36 ? 261 PHE A CZ  1 
ATOM   2128 N  N   . SER A 1 262 ? 21.668  -19.577 -4.006  1.00 28.10 ? 262 SER A N   1 
ATOM   2129 C  CA  . SER A 1 262 ? 20.376  -19.844 -4.716  1.00 32.53 ? 262 SER A CA  1 
ATOM   2130 C  C   . SER A 1 262 ? 19.321  -20.709 -3.979  1.00 42.34 ? 262 SER A C   1 
ATOM   2131 O  O   . SER A 1 262 ? 19.559  -21.478 -3.043  1.00 40.23 ? 262 SER A O   1 
ATOM   2132 C  CB  . SER A 1 262 ? 20.632  -20.398 -6.120  1.00 37.49 ? 262 SER A CB  1 
ATOM   2133 O  OG  . SER A 1 262 ? 21.353  -21.608 -6.061  1.00 37.41 ? 262 SER A OG  1 
ATOM   2134 N  N   . LYS B 1 3   ? -1.386  17.479  -2.052  1.00 32.72 ? 3   LYS B N   1 
ATOM   2135 C  CA  . LYS B 1 3   ? -0.339  16.957  -2.998  1.00 32.94 ? 3   LYS B CA  1 
ATOM   2136 C  C   . LYS B 1 3   ? 0.579   15.955  -2.283  1.00 26.42 ? 3   LYS B C   1 
ATOM   2137 O  O   . LYS B 1 3   ? 1.575   15.483  -2.870  1.00 24.98 ? 3   LYS B O   1 
ATOM   2138 C  CB  . LYS B 1 3   ? 0.500   18.062  -3.633  1.00 39.42 ? 3   LYS B CB  1 
ATOM   2139 C  CG  . LYS B 1 3   ? 1.487   18.689  -2.685  1.00 41.94 ? 3   LYS B CG  1 
ATOM   2140 C  CD  . LYS B 1 3   ? 1.948   20.050  -3.223  1.00 51.35 ? 3   LYS B CD  1 
ATOM   2141 C  CE  . LYS B 1 3   ? 3.057   19.898  -4.260  1.00 48.65 ? 3   LYS B CE  1 
ATOM   2142 N  NZ  . LYS B 1 3   ? 4.238   19.156  -3.705  1.00 48.87 ? 3   LYS B NZ  1 
ATOM   2143 N  N   . TRP B 1 4   ? 0.239   15.599  -1.033  1.00 18.51 ? 4   TRP B N   1 
ATOM   2144 C  CA  . TRP B 1 4   ? 0.882   14.432  -0.454  1.00 15.43 ? 4   TRP B CA  1 
ATOM   2145 C  C   . TRP B 1 4   ? 0.555   13.238  -1.330  1.00 13.60 ? 4   TRP B C   1 
ATOM   2146 O  O   . TRP B 1 4   ? -0.497  13.212  -2.022  1.00 15.71 ? 4   TRP B O   1 
ATOM   2147 C  CB  . TRP B 1 4   ? 0.442   14.246  1.006   1.00 13.06 ? 4   TRP B CB  1 
ATOM   2148 C  CG  . TRP B 1 4   ? -1.045  13.925  1.229   1.00 13.55 ? 4   TRP B CG  1 
ATOM   2149 C  CD1 . TRP B 1 4   ? -2.073  14.780  1.595   1.00 13.87 ? 4   TRP B CD1 1 
ATOM   2150 C  CD2 . TRP B 1 4   ? -1.664  12.596  1.244   1.00 12.14 ? 4   TRP B CD2 1 
ATOM   2151 N  NE1 . TRP B 1 4   ? -3.274  14.117  1.708   1.00 13.81 ? 4   TRP B NE1 1 
ATOM   2152 C  CE2 . TRP B 1 4   ? -3.074  12.791  1.528   1.00 11.94 ? 4   TRP B CE2 1 
ATOM   2153 C  CE3 . TRP B 1 4   ? -1.169  11.285  1.039   1.00 11.64 ? 4   TRP B CE3 1 
ATOM   2154 C  CZ2 . TRP B 1 4   ? -3.945  11.732  1.630   1.00 11.10 ? 4   TRP B CZ2 1 
ATOM   2155 C  CZ3 . TRP B 1 4   ? -2.078  10.198  1.107   1.00 10.05 ? 4   TRP B CZ3 1 
ATOM   2156 C  CH2 . TRP B 1 4   ? -3.446  10.438  1.395   1.00 10.81 ? 4   TRP B CH2 1 
ATOM   2157 N  N   . THR B 1 5   ? 1.444   12.256  -1.273  1.00 12.09 ? 5   THR B N   1 
ATOM   2158 C  CA  . THR B 1 5   ? 1.324   11.007  -2.056  1.00 11.80 ? 5   THR B CA  1 
ATOM   2159 C  C   . THR B 1 5   ? 1.851   9.817   -1.257  1.00 11.73 ? 5   THR B C   1 
ATOM   2160 O  O   . THR B 1 5   ? 2.225   9.975   -0.064  1.00 11.25 ? 5   THR B O   1 
ATOM   2161 C  CB  . THR B 1 5   ? 2.205   11.105  -3.318  1.00 13.20 ? 5   THR B CB  1 
ATOM   2162 O  OG1 . THR B 1 5   ? 3.575   11.061  -2.908  1.00 13.67 ? 5   THR B OG1 1 
ATOM   2163 C  CG2 . THR B 1 5   ? 1.879   12.413  -4.150  1.00 13.21 ? 5   THR B CG2 1 
ATOM   2164 N  N   . TYR B 1 6   ? 1.893   8.665   -1.911  1.00 12.84 ? 6   TYR B N   1 
ATOM   2165 C  CA  . TYR B 1 6   ? 2.548   7.530   -1.343  1.00 11.30 ? 6   TYR B CA  1 
ATOM   2166 C  C   . TYR B 1 6   ? 3.860   7.184   -1.967  1.00 11.53 ? 6   TYR B C   1 
ATOM   2167 O  O   . TYR B 1 6   ? 4.463   6.117   -1.648  1.00 11.54 ? 6   TYR B O   1 
ATOM   2168 C  CB  . TYR B 1 6   ? 1.624   6.289   -1.478  1.00 11.98 ? 6   TYR B CB  1 
ATOM   2169 C  CG  . TYR B 1 6   ? 0.359   6.340   -0.633  1.00 11.15 ? 6   TYR B CG  1 
ATOM   2170 C  CD1 . TYR B 1 6   ? 0.384   5.836   0.711   1.00 11.61 ? 6   TYR B CD1 1 
ATOM   2171 C  CD2 . TYR B 1 6   ? -0.844  6.843   -1.125  1.00 9.81  ? 6   TYR B CD2 1 
ATOM   2172 C  CE1 . TYR B 1 6   ? -0.811  5.830   1.497   1.00 10.15 ? 6   TYR B CE1 1 
ATOM   2173 C  CE2 . TYR B 1 6   ? -1.991  6.847   -0.367  1.00 10.04 ? 6   TYR B CE2 1 
ATOM   2174 C  CZ  . TYR B 1 6   ? -1.960  6.380   0.997   1.00 9.37  ? 6   TYR B CZ  1 
ATOM   2175 O  OH  . TYR B 1 6   ? -3.138  6.421   1.633   1.00 11.65 ? 6   TYR B OH  1 
ATOM   2176 N  N   . PHE B 1 7   ? 4.386   8.011   -2.848  1.00 14.19 ? 7   PHE B N   1 
ATOM   2177 C  CA  . PHE B 1 7   ? 5.610   7.639   -3.506  1.00 17.29 ? 7   PHE B CA  1 
ATOM   2178 C  C   . PHE B 1 7   ? 6.349   8.886   -3.879  1.00 17.93 ? 7   PHE B C   1 
ATOM   2179 O  O   . PHE B 1 7   ? 5.777   9.771   -4.495  1.00 18.76 ? 7   PHE B O   1 
ATOM   2180 C  CB  . PHE B 1 7   ? 5.301   6.851   -4.828  1.00 19.06 ? 7   PHE B CB  1 
ATOM   2181 C  CG  . PHE B 1 7   ? 6.529   6.572   -5.628  1.00 23.71 ? 7   PHE B CG  1 
ATOM   2182 C  CD1 . PHE B 1 7   ? 7.475   5.622   -5.206  1.00 26.35 ? 7   PHE B CD1 1 
ATOM   2183 C  CD2 . PHE B 1 7   ? 6.772   7.294   -6.810  1.00 29.10 ? 7   PHE B CD2 1 
ATOM   2184 C  CE1 . PHE B 1 7   ? 8.627   5.394   -5.946  1.00 30.72 ? 7   PHE B CE1 1 
ATOM   2185 C  CE2 . PHE B 1 7   ? 7.920   7.065   -7.558  1.00 34.45 ? 7   PHE B CE2 1 
ATOM   2186 C  CZ  . PHE B 1 7   ? 8.850   6.125   -7.129  1.00 32.93 ? 7   PHE B CZ  1 
ATOM   2187 N  N   . GLY B 1 8   ? 7.641   8.928   -3.552  1.00 18.63 ? 8   GLY B N   1 
ATOM   2188 C  CA  . GLY B 1 8   ? 8.437   10.100  -4.020  1.00 19.55 ? 8   GLY B CA  1 
ATOM   2189 C  C   . GLY B 1 8   ? 8.653   11.143  -2.942  1.00 20.18 ? 8   GLY B C   1 
ATOM   2190 O  O   . GLY B 1 8   ? 8.438   10.897  -1.735  1.00 18.74 ? 8   GLY B O   1 
ATOM   2191 N  N   . PRO B 1 9   ? 9.004   12.373  -3.370  1.00 20.94 ? 9   PRO B N   1 
ATOM   2192 C  CA  . PRO B 1 9   ? 9.350   13.434  -2.463  1.00 20.69 ? 9   PRO B CA  1 
ATOM   2193 C  C   . PRO B 1 9   ? 8.297   13.787  -1.521  1.00 18.72 ? 9   PRO B C   1 
ATOM   2194 O  O   . PRO B 1 9   ? 8.632   14.216  -0.429  1.00 19.15 ? 9   PRO B O   1 
ATOM   2195 C  CB  . PRO B 1 9   ? 9.641   14.622  -3.386  1.00 25.65 ? 9   PRO B CB  1 
ATOM   2196 C  CG  . PRO B 1 9   ? 10.074  14.003  -4.629  1.00 23.33 ? 9   PRO B CG  1 
ATOM   2197 C  CD  . PRO B 1 9   ? 9.269   12.732  -4.775  1.00 24.22 ? 9   PRO B CD  1 
ATOM   2198 N  N   . ASP B 1 10  ? 7.015   13.614  -1.904  1.00 16.87 ? 10  ASP B N   1 
ATOM   2199 C  CA  . ASP B 1 10  ? 5.898   13.980  -1.086  1.00 15.26 ? 10  ASP B CA  1 
ATOM   2200 C  C   . ASP B 1 10  ? 5.263   12.730  -0.421  1.00 12.43 ? 10  ASP B C   1 
ATOM   2201 O  O   . ASP B 1 10  ? 4.161   12.843  0.095   1.00 14.03 ? 10  ASP B O   1 
ATOM   2202 C  CB  . ASP B 1 10  ? 4.799   14.741  -1.903  1.00 16.79 ? 10  ASP B CB  1 
ATOM   2203 C  CG  . ASP B 1 10  ? 5.365   16.065  -2.492  1.00 23.86 ? 10  ASP B CG  1 
ATOM   2204 O  OD1 . ASP B 1 10  ? 6.048   16.739  -1.689  1.00 24.94 ? 10  ASP B OD1 1 
ATOM   2205 O  OD2 . ASP B 1 10  ? 5.263   16.328  -3.730  1.00 27.20 ? 10  ASP B OD2 1 
ATOM   2206 N  N   . GLY B 1 11  ? 5.989   11.610  -0.438  1.00 12.34 ? 11  GLY B N   1 
ATOM   2207 C  CA  . GLY B 1 11  ? 5.476   10.367  0.223   1.00 10.72 ? 11  GLY B CA  1 
ATOM   2208 C  C   . GLY B 1 11  ? 5.571   10.355  1.760   1.00 10.50 ? 11  GLY B C   1 
ATOM   2209 O  O   . GLY B 1 11  ? 5.747   11.391  2.412   1.00 9.93  ? 11  GLY B O   1 
ATOM   2210 N  N   . GLU B 1 12  ? 5.349   9.206   2.348   1.00 10.43 ? 12  GLU B N   1 
ATOM   2211 C  CA  . GLU B 1 12  ? 4.953   9.134   3.735   1.00 10.52 ? 12  GLU B CA  1 
ATOM   2212 C  C   . GLU B 1 12  ? 5.990   9.588   4.738   1.00 9.03  ? 12  GLU B C   1 
ATOM   2213 O  O   . GLU B 1 12  ? 5.627   10.037  5.774   1.00 9.83  ? 12  GLU B O   1 
ATOM   2214 C  CB  . GLU B 1 12  ? 4.473   7.721   4.068   1.00 10.05 ? 12  GLU B CB  1 
ATOM   2215 C  CG  . GLU B 1 12  ? 5.589   6.718   4.139   1.00 10.49 ? 12  GLU B CG  1 
ATOM   2216 C  CD  . GLU B 1 12  ? 5.022   5.276   4.114   1.00 10.70 ? 12  GLU B CD  1 
ATOM   2217 O  OE1 . GLU B 1 12  ? 4.626   4.798   5.163   1.00 10.68 ? 12  GLU B OE1 1 
ATOM   2218 O  OE2 . GLU B 1 12  ? 4.903   4.728   3.010   1.00 9.83  ? 12  GLU B OE2 1 
ATOM   2219 N  N   . ASN B 1 13  ? 7.279   9.473   4.392   1.00 10.62 ? 13  ASN B N   1 
ATOM   2220 C  CA  . ASN B 1 13  ? 8.282   9.945   5.353   1.00 9.73  ? 13  ASN B CA  1 
ATOM   2221 C  C   . ASN B 1 13  ? 8.371   11.500  5.374   1.00 9.85  ? 13  ASN B C   1 
ATOM   2222 O  O   . ASN B 1 13  ? 8.963   12.066  6.294   1.00 10.04 ? 13  ASN B O   1 
ATOM   2223 C  CB  . ASN B 1 13  ? 9.665   9.451   4.936   1.00 9.35  ? 13  ASN B CB  1 
ATOM   2224 C  CG  . ASN B 1 13  ? 9.846   7.966   5.203   1.00 10.22 ? 13  ASN B CG  1 
ATOM   2225 O  OD1 . ASN B 1 13  ? 8.937   7.302   5.723   1.00 10.67 ? 13  ASN B OD1 1 
ATOM   2226 N  ND2 . ASN B 1 13  ? 11.017  7.440   4.826   1.00 10.51 ? 13  ASN B ND2 1 
ATOM   2227 N  N   . SER B 1 14  ? 7.678   12.139  4.425   1.00 9.39  ? 14  SER B N   1 
ATOM   2228 C  CA  . SER B 1 14  ? 7.539   13.616  4.372   1.00 9.78  ? 14  SER B CA  1 
ATOM   2229 C  C   . SER B 1 14  ? 6.231   14.181  4.848   1.00 10.02 ? 14  SER B C   1 
ATOM   2230 O  O   . SER B 1 14  ? 6.101   15.441  4.946   1.00 10.94 ? 14  SER B O   1 
ATOM   2231 C  CB  . SER B 1 14  ? 7.829   14.091  2.967   1.00 9.97  ? 14  SER B CB  1 
ATOM   2232 O  OG  . SER B 1 14  ? 9.183   13.837  2.616   1.00 11.84 ? 14  SER B OG  1 
ATOM   2233 N  N   . TRP B 1 15  ? 5.230   13.352  5.145   1.00 10.17 ? 15  TRP B N   1 
ATOM   2234 C  CA  . TRP B 1 15  ? 3.901   13.904  5.520   1.00 9.90  ? 15  TRP B CA  1 
ATOM   2235 C  C   . TRP B 1 15  ? 4.012   14.788  6.700   1.00 12.20 ? 15  TRP B C   1 
ATOM   2236 O  O   . TRP B 1 15  ? 3.299   15.795  6.791   1.00 11.34 ? 15  TRP B O   1 
ATOM   2237 C  CB  . TRP B 1 15  ? 2.963   12.771  5.883   1.00 10.39 ? 15  TRP B CB  1 
ATOM   2238 C  CG  . TRP B 1 15  ? 2.536   11.938  4.711   1.00 9.13  ? 15  TRP B CG  1 
ATOM   2239 C  CD1 . TRP B 1 15  ? 2.782   12.115  3.342   1.00 10.56 ? 15  TRP B CD1 1 
ATOM   2240 C  CD2 . TRP B 1 15  ? 1.743   10.673  4.807   1.00 10.03 ? 15  TRP B CD2 1 
ATOM   2241 N  NE1 . TRP B 1 15  ? 2.226   11.096  2.628   1.00 10.80 ? 15  TRP B NE1 1 
ATOM   2242 C  CE2 . TRP B 1 15  ? 1.597   10.197  3.442   1.00 9.82  ? 15  TRP B CE2 1 
ATOM   2243 C  CE3 . TRP B 1 15  ? 1.158   9.922   5.880   1.00 9.57  ? 15  TRP B CE3 1 
ATOM   2244 C  CZ2 . TRP B 1 15  ? 0.889   9.029   3.146   1.00 10.85 ? 15  TRP B CZ2 1 
ATOM   2245 C  CZ3 . TRP B 1 15  ? 0.474   8.729   5.532   1.00 8.70  ? 15  TRP B CZ3 1 
ATOM   2246 C  CH2 . TRP B 1 15  ? 0.318   8.351   4.224   1.00 9.63  ? 15  TRP B CH2 1 
ATOM   2247 N  N   . SER B 1 16  ? 4.864   14.445  7.648   1.00 11.58 ? 16  SER B N   1 
ATOM   2248 C  CA  . SER B 1 16  ? 4.950   15.280  8.867   1.00 11.87 ? 16  SER B CA  1 
ATOM   2249 C  C   . SER B 1 16  ? 5.439   16.709  8.677   1.00 10.39 ? 16  SER B C   1 
ATOM   2250 O  O   . SER B 1 16  ? 5.216   17.490  9.591   1.00 13.77 ? 16  SER B O   1 
ATOM   2251 C  CB  . SER B 1 16  ? 5.887   14.626  9.905   1.00 12.36 ? 16  SER B CB  1 
ATOM   2252 O  OG  . SER B 1 16  ? 7.205   14.723  9.354   1.00 15.89 ? 16  SER B OG  1 
ATOM   2253 N  N   . LYS B 1 17  ? 6.010   16.980  7.533   1.00 10.79 ? 17  LYS B N   1 
ATOM   2254 C  CA  . LYS B 1 17  ? 6.453   18.346  7.242   1.00 10.88 ? 17  LYS B CA  1 
ATOM   2255 C  C   . LYS B 1 17  ? 5.257   19.256  7.183   1.00 13.53 ? 17  LYS B C   1 
ATOM   2256 O  O   . LYS B 1 17  ? 5.413   20.479  7.551   1.00 12.80 ? 17  LYS B O   1 
ATOM   2257 C  CB  . LYS B 1 17  ? 7.234   18.421  5.909   1.00 11.49 ? 17  LYS B CB  1 
ATOM   2258 C  CG  . LYS B 1 17  ? 8.522   17.565  5.878   1.00 10.74 ? 17  LYS B CG  1 
ATOM   2259 C  CD  . LYS B 1 17  ? 9.082   17.539  4.473   1.00 9.85  ? 17  LYS B CD  1 
ATOM   2260 C  CE  . LYS B 1 17  ? 10.324  16.651  4.251   1.00 10.89 ? 17  LYS B CE  1 
ATOM   2261 N  NZ  . LYS B 1 17  ? 10.907  16.763  2.917   1.00 11.84 ? 17  LYS B NZ  1 
ATOM   2262 N  N   . LYS B 1 18  ? 4.139   18.794  6.631   1.00 11.67 ? 18  LYS B N   1 
ATOM   2263 C  CA  . LYS B 1 18  ? 2.958   19.687  6.517   1.00 13.15 ? 18  LYS B CA  1 
ATOM   2264 C  C   . LYS B 1 18  ? 1.853   19.307  7.496   1.00 14.00 ? 18  LYS B C   1 
ATOM   2265 O  O   . LYS B 1 18  ? 0.919   20.087  7.735   1.00 13.70 ? 18  LYS B O   1 
ATOM   2266 C  CB  . LYS B 1 18  ? 2.378   19.627  5.114   1.00 15.04 ? 18  LYS B CB  1 
ATOM   2267 C  CG  . LYS B 1 18  ? 3.274   20.237  4.011   1.00 21.44 ? 18  LYS B CG  1 
ATOM   2268 C  CD  . LYS B 1 18  ? 2.707   20.068  2.590   1.00 23.95 ? 18  LYS B CD  1 
ATOM   2269 C  CE  . LYS B 1 18  ? 3.298   21.099  1.579   1.00 26.85 ? 18  LYS B CE  1 
ATOM   2270 N  NZ  . LYS B 1 18  ? 2.504   21.159  0.273   1.00 28.32 ? 18  LYS B NZ  1 
ATOM   2271 N  N   . TYR B 1 19  ? 1.907   18.077  8.034   1.00 13.45 ? 19  TYR B N   1 
ATOM   2272 C  CA  . TYR B 1 19  ? 0.877   17.504  8.851   1.00 13.88 ? 19  TYR B CA  1 
ATOM   2273 C  C   . TYR B 1 19  ? 1.525   16.950  10.130  1.00 14.05 ? 19  TYR B C   1 
ATOM   2274 O  O   . TYR B 1 19  ? 1.890   15.762  10.213  1.00 12.22 ? 19  TYR B O   1 
ATOM   2275 C  CB  . TYR B 1 19  ? 0.200   16.363  8.077   1.00 13.41 ? 19  TYR B CB  1 
ATOM   2276 C  CG  . TYR B 1 19  ? -0.446  16.785  6.755   1.00 13.19 ? 19  TYR B CG  1 
ATOM   2277 C  CD1 . TYR B 1 19  ? -1.723  17.399  6.725   1.00 13.48 ? 19  TYR B CD1 1 
ATOM   2278 C  CD2 . TYR B 1 19  ? 0.203   16.601  5.583   1.00 12.80 ? 19  TYR B CD2 1 
ATOM   2279 C  CE1 . TYR B 1 19  ? -2.263  17.767  5.491   1.00 16.37 ? 19  TYR B CE1 1 
ATOM   2280 C  CE2 . TYR B 1 19  ? -0.298  16.999  4.391   1.00 14.05 ? 19  TYR B CE2 1 
ATOM   2281 C  CZ  . TYR B 1 19  ? -1.569  17.575  4.359   1.00 16.77 ? 19  TYR B CZ  1 
ATOM   2282 O  OH  . TYR B 1 19  ? -2.122  17.961  3.115   1.00 23.69 ? 19  TYR B OH  1 
ATOM   2283 N  N   . PRO B 1 20  ? 1.629   17.774  11.155  1.00 13.40 ? 20  PRO B N   1 
ATOM   2284 C  CA  . PRO B 1 20  ? 2.403   17.380  12.319  1.00 14.70 ? 20  PRO B CA  1 
ATOM   2285 C  C   . PRO B 1 20  ? 1.963   16.111  13.008  1.00 13.42 ? 20  PRO B C   1 
ATOM   2286 O  O   . PRO B 1 20  ? 2.853   15.415  13.536  1.00 14.48 ? 20  PRO B O   1 
ATOM   2287 C  CB  . PRO B 1 20  ? 2.379   18.628  13.239  1.00 18.48 ? 20  PRO B CB  1 
ATOM   2288 C  CG  . PRO B 1 20  ? 1.932   19.738  12.351  1.00 16.34 ? 20  PRO B CG  1 
ATOM   2289 C  CD  . PRO B 1 20  ? 1.204   19.212  11.164  1.00 13.40 ? 20  PRO B CD  1 
ATOM   2290 N  N   . SER B 1 21  ? 0.674   15.813  12.990  1.00 12.31 ? 21  SER B N   1 
ATOM   2291 C  CA  . SER B 1 21  ? 0.179   14.649  13.706  1.00 12.83 ? 21  SER B CA  1 
ATOM   2292 C  C   . SER B 1 21  ? 0.789   13.423  13.055  1.00 12.35 ? 21  SER B C   1 
ATOM   2293 O  O   . SER B 1 21  ? 0.759   12.376  13.709  1.00 12.61 ? 21  SER B O   1 
ATOM   2294 C  CB  . SER B 1 21  ? -1.335  14.567  13.752  1.00 13.33 ? 21  SER B CB  1 
ATOM   2295 O  OG  . SER B 1 21  ? -1.803  15.692  14.584  1.00 17.01 ? 21  SER B OG  1 
ATOM   2296 N  N   . CYS B 1 22  ? 1.190   13.495  11.796  1.00 12.93 ? 22  CYS B N   1 
ATOM   2297 C  CA  . CYS B 1 22  ? 1.741   12.248  11.188  1.00 11.90 ? 22  CYS B CA  1 
ATOM   2298 C  C   . CYS B 1 22  ? 3.058   11.856  11.781  1.00 13.24 ? 22  CYS B C   1 
ATOM   2299 O  O   . CYS B 1 22  ? 3.485   10.717  11.570  1.00 13.23 ? 22  CYS B O   1 
ATOM   2300 C  CB  . CYS B 1 22  ? 1.892   12.382  9.642   1.00 11.37 ? 22  CYS B CB  1 
ATOM   2301 S  SG  . CYS B 1 22  ? 0.327   12.761  8.739   1.00 12.31 ? 22  CYS B SG  1 
ATOM   2302 N  N   . GLY B 1 23  ? 3.682   12.762  12.555  1.00 12.42 ? 23  GLY B N   1 
ATOM   2303 C  CA  . GLY B 1 23  ? 4.929   12.532  13.251  1.00 16.83 ? 23  GLY B CA  1 
ATOM   2304 C  C   . GLY B 1 23  ? 4.630   12.342  14.742  1.00 17.18 ? 23  GLY B C   1 
ATOM   2305 O  O   . GLY B 1 23  ? 5.585   12.255  15.569  1.00 19.22 ? 23  GLY B O   1 
ATOM   2306 N  N   . GLY B 1 24  ? 3.348   12.291  15.137  1.00 17.27 ? 24  GLY B N   1 
ATOM   2307 C  CA  . GLY B 1 24  ? 3.001   12.282  16.568  1.00 16.88 ? 24  GLY B CA  1 
ATOM   2308 C  C   . GLY B 1 24  ? 2.799   10.872  17.067  1.00 17.33 ? 24  GLY B C   1 
ATOM   2309 O  O   . GLY B 1 24  ? 3.273   9.914   16.441  1.00 19.33 ? 24  GLY B O   1 
ATOM   2310 N  N   . LEU B 1 25  ? 2.155   10.733  18.218  1.00 20.84 ? 25  LEU B N   1 
ATOM   2311 C  CA  . LEU B 1 25  ? 1.974   9.352   18.731  1.00 21.39 ? 25  LEU B CA  1 
ATOM   2312 C  C   . LEU B 1 25  ? 0.698   8.750   18.194  1.00 18.19 ? 25  LEU B C   1 
ATOM   2313 O  O   . LEU B 1 25  ? -0.112  9.408   17.459  1.00 18.05 ? 25  LEU B O   1 
ATOM   2314 C  CB  . LEU B 1 25  ? 2.091   9.278   20.274  1.00 25.05 ? 25  LEU B CB  1 
ATOM   2315 C  CG  . LEU B 1 25  ? 3.392   9.886   20.815  1.00 27.42 ? 25  LEU B CG  1 
ATOM   2316 C  CD1 . LEU B 1 25  ? 3.118   10.506  22.171  1.00 31.36 ? 25  LEU B CD1 1 
ATOM   2317 C  CD2 . LEU B 1 25  ? 4.537   8.878   20.809  1.00 28.11 ? 25  LEU B CD2 1 
ATOM   2318 N  N   . LEU B 1 26  ? 0.510   7.477   18.573  1.00 17.16 ? 26  LEU B N   1 
ATOM   2319 C  CA  . LEU B 1 26  ? -0.699  6.711   18.335  1.00 17.64 ? 26  LEU B CA  1 
ATOM   2320 C  C   . LEU B 1 26  ? -0.971  6.483   16.840  1.00 14.43 ? 26  LEU B C   1 
ATOM   2321 O  O   . LEU B 1 26  ? -2.114  6.487   16.421  1.00 15.18 ? 26  LEU B O   1 
ATOM   2322 C  CB  . LEU B 1 26  ? -1.979  7.294   18.956  1.00 20.78 ? 26  LEU B CB  1 
ATOM   2323 C  CG  . LEU B 1 26  ? -1.910  7.641   20.477  1.00 24.44 ? 26  LEU B CG  1 
ATOM   2324 C  CD1 . LEU B 1 26  ? -3.154  8.398   20.958  1.00 30.50 ? 26  LEU B CD1 1 
ATOM   2325 C  CD2 . LEU B 1 26  ? -1.589  6.372   21.283  1.00 26.42 ? 26  LEU B CD2 1 
ATOM   2326 N  N   . GLN B 1 27  ? 0.090   6.313   16.055  1.00 13.54 ? 27  GLN B N   1 
ATOM   2327 C  CA  . GLN B 1 27  ? -0.136  6.256   14.607  1.00 10.80 ? 27  GLN B CA  1 
ATOM   2328 C  C   . GLN B 1 27  ? -0.487  4.887   14.118  1.00 11.15 ? 27  GLN B C   1 
ATOM   2329 O  O   . GLN B 1 27  ? -0.047  3.879   14.699  1.00 13.06 ? 27  GLN B O   1 
ATOM   2330 C  CB  . GLN B 1 27  ? 1.103   6.740   13.865  1.00 11.71 ? 27  GLN B CB  1 
ATOM   2331 C  CG  . GLN B 1 27  ? 1.349   8.208   14.161  1.00 12.13 ? 27  GLN B CG  1 
ATOM   2332 C  CD  . GLN B 1 27  ? 0.282   9.081   13.446  1.00 10.98 ? 27  GLN B CD  1 
ATOM   2333 O  OE1 . GLN B 1 27  ? 0.256   9.209   12.207  1.00 11.08 ? 27  GLN B OE1 1 
ATOM   2334 N  NE2 . GLN B 1 27  ? -0.644  9.595   14.204  1.00 12.79 ? 27  GLN B NE2 1 
ATOM   2335 N  N   . SER B 1 28  ? -1.334  4.829   13.088  1.00 9.81  ? 28  SER B N   1 
ATOM   2336 C  CA  . SER B 1 28  ? -1.695  3.575   12.389  1.00 9.27  ? 28  SER B CA  1 
ATOM   2337 C  C   . SER B 1 28  ? -1.158  3.621   10.972  1.00 9.46  ? 28  SER B C   1 
ATOM   2338 O  O   . SER B 1 28  ? -0.863  4.669   10.467  1.00 9.77  ? 28  SER B O   1 
ATOM   2339 C  CB  . SER B 1 28  ? -3.213  3.526   12.340  1.00 8.70  ? 28  SER B CB  1 
ATOM   2340 O  OG  . SER B 1 28  ? -3.701  3.457   13.699  1.00 9.13  ? 28  SER B OG  1 
ATOM   2341 N  N   . PRO B 1 29  ? -1.054  2.504   10.277  1.00 8.66  ? 29  PRO B N   1 
ATOM   2342 C  CA  . PRO B 1 29  ? -1.428  1.160   10.752  1.00 9.38  ? 29  PRO B CA  1 
ATOM   2343 C  C   . PRO B 1 29  ? -0.268  0.516   11.520  1.00 8.24  ? 29  PRO B C   1 
ATOM   2344 O  O   . PRO B 1 29  ? 0.760   1.128   11.768  1.00 9.38  ? 29  PRO B O   1 
ATOM   2345 C  CB  . PRO B 1 29  ? -1.630  0.372   9.408   1.00 9.74  ? 29  PRO B CB  1 
ATOM   2346 C  CG  . PRO B 1 29  ? -0.541  0.996   8.549   1.00 8.70  ? 29  PRO B CG  1 
ATOM   2347 C  CD  . PRO B 1 29  ? -0.596  2.468   8.864   1.00 10.03 ? 29  PRO B CD  1 
ATOM   2348 N  N   . ILE B 1 30  ? -0.566  -0.683  12.000  1.00 9.41  ? 30  ILE B N   1 
ATOM   2349 C  CA  . ILE B 1 30  ? 0.430   -1.424  12.839  1.00 9.68  ? 30  ILE B CA  1 
ATOM   2350 C  C   . ILE B 1 30  ? 0.450   -2.913  12.413  1.00 9.13  ? 30  ILE B C   1 
ATOM   2351 O  O   . ILE B 1 30  ? -0.426  -3.445  11.734  1.00 8.48  ? 30  ILE B O   1 
ATOM   2352 C  CB  . ILE B 1 30  ? 0.096   -1.367  14.369  1.00 10.21 ? 30  ILE B CB  1 
ATOM   2353 C  CG1 . ILE B 1 30  ? -1.324  -1.940  14.641  1.00 10.45 ? 30  ILE B CG1 1 
ATOM   2354 C  CG2 . ILE B 1 30  ? 0.311   0.115   14.841  1.00 10.71 ? 30  ILE B CG2 1 
ATOM   2355 C  CD1 . ILE B 1 30  ? -1.571  -2.048  16.149  1.00 11.35 ? 30  ILE B CD1 1 
ATOM   2356 N  N   . ASP B 1 31  ? 1.571   -3.577  12.819  1.00 9.33  ? 31  ASP B N   1 
ATOM   2357 C  CA  . ASP B 1 31  ? 1.675   -5.020  12.672  1.00 9.94  ? 31  ASP B CA  1 
ATOM   2358 C  C   . ASP B 1 31  ? 1.083   -5.720  13.874  1.00 11.21 ? 31  ASP B C   1 
ATOM   2359 O  O   . ASP B 1 31  ? 1.474   -5.472  15.007  1.00 12.64 ? 31  ASP B O   1 
ATOM   2360 C  CB  . ASP B 1 31  ? 3.147   -5.423  12.626  1.00 10.00 ? 31  ASP B CB  1 
ATOM   2361 C  CG  . ASP B 1 31  ? 3.269   -6.926  12.475  1.00 12.68 ? 31  ASP B CG  1 
ATOM   2362 O  OD1 . ASP B 1 31  ? 2.762   -7.498  11.497  1.00 11.89 ? 31  ASP B OD1 1 
ATOM   2363 O  OD2 . ASP B 1 31  ? 3.906   -7.541  13.375  1.00 16.49 ? 31  ASP B OD2 1 
ATOM   2364 N  N   . LEU B 1 32  ? 0.127   -6.581  13.613  1.00 10.54 ? 32  LEU B N   1 
ATOM   2365 C  CA  . LEU B 1 32  ? -0.597  -7.347  14.667  1.00 11.71 ? 32  LEU B CA  1 
ATOM   2366 C  C   . LEU B 1 32  ? 0.175   -8.621  14.941  1.00 11.20 ? 32  LEU B C   1 
ATOM   2367 O  O   . LEU B 1 32  ? 0.220   -9.476  14.079  1.00 14.13 ? 32  LEU B O   1 
ATOM   2368 C  CB  . LEU B 1 32  ? -2.024  -7.607  14.173  1.00 12.50 ? 32  LEU B CB  1 
ATOM   2369 C  CG  . LEU B 1 32  ? -2.755  -6.262  13.812  1.00 13.61 ? 32  LEU B CG  1 
ATOM   2370 C  CD1 . LEU B 1 32  ? -4.088  -6.544  13.035  1.00 14.66 ? 32  LEU B CD1 1 
ATOM   2371 C  CD2 . LEU B 1 32  ? -3.042  -5.419  15.034  1.00 17.19 ? 32  LEU B CD2 1 
ATOM   2372 N  N   . HIS B 1 33  ? 0.877   -8.712  16.062  1.00 12.41 ? 33  HIS B N   1 
ATOM   2373 C  CA  . HIS B 1 33  ? 1.667   -9.895  16.322  1.00 13.45 ? 33  HIS B CA  1 
ATOM   2374 C  C   . HIS B 1 33  ? 1.583   -10.226 17.814  1.00 13.38 ? 33  HIS B C   1 
ATOM   2375 O  O   . HIS B 1 33  ? 1.295   -9.369  18.632  1.00 12.41 ? 33  HIS B O   1 
ATOM   2376 C  CB  . HIS B 1 33  ? 3.180   -9.666  15.921  1.00 14.70 ? 33  HIS B CB  1 
ATOM   2377 C  CG  . HIS B 1 33  ? 3.869   -8.460  16.649  1.00 14.43 ? 33  HIS B CG  1 
ATOM   2378 N  ND1 . HIS B 1 33  ? 3.608   -7.180  16.347  1.00 16.24 ? 33  HIS B ND1 1 
ATOM   2379 C  CD2 . HIS B 1 33  ? 4.829   -8.413  17.671  1.00 13.54 ? 33  HIS B CD2 1 
ATOM   2380 C  CE1 . HIS B 1 33  ? 4.342   -6.345  17.141  1.00 18.96 ? 33  HIS B CE1 1 
ATOM   2381 N  NE2 . HIS B 1 33  ? 5.098   -7.097  17.930  1.00 16.06 ? 33  HIS B NE2 1 
ATOM   2382 N  N   . SER B 1 34  ? 1.877   -11.487 18.138  1.00 15.03 ? 34  SER B N   1 
ATOM   2383 C  CA  . SER B 1 34  ? 1.552   -12.019 19.483  1.00 15.01 ? 34  SER B CA  1 
ATOM   2384 C  C   . SER B 1 34  ? 2.058   -11.180 20.622  1.00 14.39 ? 34  SER B C   1 
ATOM   2385 O  O   . SER B 1 34  ? 1.325   -11.091 21.616  1.00 14.89 ? 34  SER B O   1 
ATOM   2386 C  CB  . SER B 1 34  ? 2.059   -13.476 19.611  1.00 20.42 ? 34  SER B CB  1 
ATOM   2387 O  OG  . SER B 1 34  ? 3.465   -13.470 19.456  1.00 21.45 ? 34  SER B OG  1 
ATOM   2388 N  N   . ASP B 1 35  ? 3.273   -10.575 20.577  1.00 13.38 ? 35  ASP B N   1 
ATOM   2389 C  CA  . ASP B 1 35  ? 3.807   -9.909  21.764  1.00 15.42 ? 35  ASP B CA  1 
ATOM   2390 C  C   . ASP B 1 35  ? 3.037   -8.740  22.267  1.00 15.54 ? 35  ASP B C   1 
ATOM   2391 O  O   . ASP B 1 35  ? 3.181   -8.317  23.416  1.00 19.47 ? 35  ASP B O   1 
ATOM   2392 C  CB  . ASP B 1 35  ? 5.271   -9.396  21.545  1.00 16.58 ? 35  ASP B CB  1 
ATOM   2393 C  CG  . ASP B 1 35  ? 6.163   -10.442 20.940  1.00 19.67 ? 35  ASP B CG  1 
ATOM   2394 O  OD1 . ASP B 1 35  ? 5.879   -10.832 19.762  1.00 20.24 ? 35  ASP B OD1 1 
ATOM   2395 O  OD2 . ASP B 1 35  ? 7.161   -10.845 21.650  1.00 18.22 ? 35  ASP B OD2 1 
ATOM   2396 N  N   . ILE B 1 36  ? 2.186   -8.167  21.423  1.00 14.25 ? 36  ILE B N   1 
ATOM   2397 C  CA  . ILE B 1 36  ? 1.471   -6.977  21.812  1.00 15.42 ? 36  ILE B CA  1 
ATOM   2398 C  C   . ILE B 1 36  ? -0.050  -7.200  21.866  1.00 14.50 ? 36  ILE B C   1 
ATOM   2399 O  O   . ILE B 1 36  ? -0.790  -6.264  22.007  1.00 16.39 ? 36  ILE B O   1 
ATOM   2400 C  CB  . ILE B 1 36  ? 1.814   -5.727  20.931  1.00 18.06 ? 36  ILE B CB  1 
ATOM   2401 C  CG1 . ILE B 1 36  ? 1.715   -6.032  19.432  1.00 21.59 ? 36  ILE B CG1 1 
ATOM   2402 C  CG2 . ILE B 1 36  ? 3.214   -5.256  21.288  1.00 19.69 ? 36  ILE B CG2 1 
ATOM   2403 C  CD1 . ILE B 1 36  ? 0.354   -6.153  18.837  1.00 19.77 ? 36  ILE B CD1 1 
ATOM   2404 N  N   . LEU B 1 37  ? -0.467  -8.465  21.711  1.00 12.29 ? 37  LEU B N   1 
ATOM   2405 C  CA  . LEU B 1 37  ? -1.948  -8.905  21.748  1.00 14.09 ? 37  LEU B CA  1 
ATOM   2406 C  C   . LEU B 1 37  ? -2.330  -9.266  23.186  1.00 15.70 ? 37  LEU B C   1 
ATOM   2407 O  O   . LEU B 1 37  ? -1.510  -9.872  23.934  1.00 18.20 ? 37  LEU B O   1 
ATOM   2408 C  CB  . LEU B 1 37  ? -2.227  -10.114 20.852  1.00 13.33 ? 37  LEU B CB  1 
ATOM   2409 C  CG  . LEU B 1 37  ? -1.879  -9.915  19.363  1.00 15.10 ? 37  LEU B CG  1 
ATOM   2410 C  CD1 . LEU B 1 37  ? -2.226  -11.048 18.443  1.00 17.01 ? 37  LEU B CD1 1 
ATOM   2411 C  CD2 . LEU B 1 37  ? -2.566  -8.654  18.890  1.00 14.22 ? 37  LEU B CD2 1 
ATOM   2412 N  N   . GLN B 1 38  ? -3.547  -8.925  23.579  1.00 13.94 ? 38  GLN B N   1 
ATOM   2413 C  CA  . GLN B 1 38  ? -4.036  -9.329  24.929  1.00 14.91 ? 38  GLN B CA  1 
ATOM   2414 C  C   . GLN B 1 38  ? -5.527  -9.558  24.818  1.00 15.63 ? 38  GLN B C   1 
ATOM   2415 O  O   . GLN B 1 38  ? -6.265  -8.659  24.403  1.00 15.93 ? 38  GLN B O   1 
ATOM   2416 C  CB  . GLN B 1 38  ? -3.814  -8.276  25.931  1.00 17.24 ? 38  GLN B CB  1 
ATOM   2417 C  CG  . GLN B 1 38  ? -4.118  -8.813  27.351  1.00 22.68 ? 38  GLN B CG  1 
ATOM   2418 C  CD  . GLN B 1 38  ? -3.639  -7.824  28.359  1.00 25.53 ? 38  GLN B CD  1 
ATOM   2419 O  OE1 . GLN B 1 38  ? -2.438  -7.808  28.666  1.00 36.06 ? 38  GLN B OE1 1 
ATOM   2420 N  NE2 . GLN B 1 38  ? -4.535  -6.953  28.853  1.00 26.97 ? 38  GLN B NE2 1 
ATOM   2421 N  N   . TYR B 1 39  ? -5.970  -10.737 25.239  1.00 13.12 ? 39  TYR B N   1 
ATOM   2422 C  CA  . TYR B 1 39  ? -7.398  -11.028 25.179  1.00 13.16 ? 39  TYR B CA  1 
ATOM   2423 C  C   . TYR B 1 39  ? -8.164  -10.135 26.139  1.00 14.04 ? 39  TYR B C   1 
ATOM   2424 O  O   . TYR B 1 39  ? -7.731  -9.879  27.295  1.00 15.81 ? 39  TYR B O   1 
ATOM   2425 C  CB  . TYR B 1 39  ? -7.601  -12.509 25.561  1.00 12.38 ? 39  TYR B CB  1 
ATOM   2426 C  CG  . TYR B 1 39  ? -9.036  -12.863 25.703  1.00 12.31 ? 39  TYR B CG  1 
ATOM   2427 C  CD1 . TYR B 1 39  ? -9.931  -12.809 24.663  1.00 13.10 ? 39  TYR B CD1 1 
ATOM   2428 C  CD2 . TYR B 1 39  ? -9.539  -13.220 26.974  1.00 13.75 ? 39  TYR B CD2 1 
ATOM   2429 C  CE1 . TYR B 1 39  ? -11.248 -13.141 24.776  1.00 14.28 ? 39  TYR B CE1 1 
ATOM   2430 C  CE2 . TYR B 1 39  ? -10.882 -13.523 27.125  1.00 14.69 ? 39  TYR B CE2 1 
ATOM   2431 C  CZ  . TYR B 1 39  ? -11.722 -13.517 26.044  1.00 14.71 ? 39  TYR B CZ  1 
ATOM   2432 O  OH  . TYR B 1 39  ? -13.053 -13.856 26.141  1.00 16.75 ? 39  TYR B OH  1 
ATOM   2433 N  N   . ASP B 1 40  ? -9.285  -9.565  25.638  1.00 12.78 ? 40  ASP B N   1 
ATOM   2434 C  CA  . ASP B 1 40  ? -10.168 -8.814  26.491  1.00 13.67 ? 40  ASP B CA  1 
ATOM   2435 C  C   . ASP B 1 40  ? -11.589 -9.304  26.301  1.00 14.27 ? 40  ASP B C   1 
ATOM   2436 O  O   . ASP B 1 40  ? -12.249 -9.034  25.273  1.00 14.72 ? 40  ASP B O   1 
ATOM   2437 C  CB  . ASP B 1 40  ? -10.004 -7.349  26.079  1.00 14.14 ? 40  ASP B CB  1 
ATOM   2438 C  CG  . ASP B 1 40  ? -10.868 -6.422  26.867  1.00 16.56 ? 40  ASP B CG  1 
ATOM   2439 O  OD1 . ASP B 1 40  ? -11.695 -6.885  27.675  1.00 18.02 ? 40  ASP B OD1 1 
ATOM   2440 O  OD2 . ASP B 1 40  ? -10.753 -5.165  26.604  1.00 19.73 ? 40  ASP B OD2 1 
ATOM   2441 N  N   . ALA B 1 41  ? -12.146 -9.968  27.332  1.00 14.93 ? 41  ALA B N   1 
ATOM   2442 C  CA  . ALA B 1 41  ? -13.464 -10.577 27.308  1.00 17.50 ? 41  ALA B CA  1 
ATOM   2443 C  C   . ALA B 1 41  ? -14.635 -9.610  27.225  1.00 17.39 ? 41  ALA B C   1 
ATOM   2444 O  O   . ALA B 1 41  ? -15.771 -10.002 26.890  1.00 18.43 ? 41  ALA B O   1 
ATOM   2445 C  CB  . ALA B 1 41  ? -13.567 -11.442 28.565  1.00 15.86 ? 41  ALA B CB  1 
ATOM   2446 N  N   . SER B 1 42  ? -14.344 -8.342  27.490  1.00 16.75 ? 42  SER B N   1 
ATOM   2447 C  CA  . SER B 1 42  ? -15.375 -7.328  27.337  1.00 16.54 ? 42  SER B CA  1 
ATOM   2448 C  C   . SER B 1 42  ? -15.599 -6.818  25.888  1.00 17.00 ? 42  SER B C   1 
ATOM   2449 O  O   . SER B 1 42  ? -16.518 -5.966  25.610  1.00 18.21 ? 42  SER B O   1 
ATOM   2450 C  CB  . SER B 1 42  ? -14.998 -6.152  28.267  1.00 22.69 ? 42  SER B CB  1 
ATOM   2451 O  OG  . SER B 1 42  ? -14.081 -5.231  27.716  1.00 22.15 ? 42  SER B OG  1 
ATOM   2452 N  N   . LEU B 1 43  ? -14.788 -7.320  24.968  1.00 14.37 ? 43  LEU B N   1 
ATOM   2453 C  CA  . LEU B 1 43  ? -14.970 -6.988  23.512  1.00 13.45 ? 43  LEU B CA  1 
ATOM   2454 C  C   . LEU B 1 43  ? -16.057 -7.856  22.948  1.00 13.28 ? 43  LEU B C   1 
ATOM   2455 O  O   . LEU B 1 43  ? -15.794 -8.897  22.296  1.00 13.96 ? 43  LEU B O   1 
ATOM   2456 C  CB  . LEU B 1 43  ? -13.645 -7.152  22.745  1.00 13.04 ? 43  LEU B CB  1 
ATOM   2457 C  CG  . LEU B 1 43  ? -12.553 -6.181  23.173  1.00 13.35 ? 43  LEU B CG  1 
ATOM   2458 C  CD1 . LEU B 1 43  ? -11.257 -6.436  22.361  1.00 12.52 ? 43  LEU B CD1 1 
ATOM   2459 C  CD2 . LEU B 1 43  ? -12.935 -4.712  23.106  1.00 13.99 ? 43  LEU B CD2 1 
ATOM   2460 N  N   . THR B 1 44  ? -17.305 -7.433  23.218  1.00 15.90 ? 44  THR B N   1 
ATOM   2461 C  CA  . THR B 1 44  ? -18.494 -8.152  22.788  1.00 13.90 ? 44  THR B CA  1 
ATOM   2462 C  C   . THR B 1 44  ? -18.787 -7.901  21.304  1.00 13.72 ? 44  THR B C   1 
ATOM   2463 O  O   . THR B 1 44  ? -18.160 -6.999  20.720  1.00 12.88 ? 44  THR B O   1 
ATOM   2464 C  CB  . THR B 1 44  ? -19.672 -7.732  23.719  1.00 13.73 ? 44  THR B CB  1 
ATOM   2465 O  OG1 . THR B 1 44  ? -19.676 -6.321  23.823  1.00 18.54 ? 44  THR B OG1 1 
ATOM   2466 C  CG2 . THR B 1 44  ? -19.351 -8.254  25.148  1.00 14.90 ? 44  THR B CG2 1 
ATOM   2467 N  N   . PRO B 1 45  ? -19.693 -8.690  20.667  1.00 12.89 ? 45  PRO B N   1 
ATOM   2468 C  CA  . PRO B 1 45  ? -19.905 -8.526  19.222  1.00 14.05 ? 45  PRO B CA  1 
ATOM   2469 C  C   . PRO B 1 45  ? -20.495 -7.205  18.835  1.00 14.17 ? 45  PRO B C   1 
ATOM   2470 O  O   . PRO B 1 45  ? -21.428 -6.707  19.539  1.00 16.41 ? 45  PRO B O   1 
ATOM   2471 C  CB  . PRO B 1 45  ? -20.800 -9.709  18.794  1.00 15.95 ? 45  PRO B CB  1 
ATOM   2472 C  CG  . PRO B 1 45  ? -20.563 -10.762 19.843  1.00 14.75 ? 45  PRO B CG  1 
ATOM   2473 C  CD  . PRO B 1 45  ? -20.298 -9.980  21.116  1.00 13.48 ? 45  PRO B CD  1 
ATOM   2474 N  N   . LEU B 1 46  ? -19.993 -6.606  17.733  1.00 14.16 ? 46  LEU B N   1 
ATOM   2475 C  CA  . LEU B 1 46  ? -20.643 -5.403  17.245  1.00 15.61 ? 46  LEU B CA  1 
ATOM   2476 C  C   . LEU B 1 46  ? -21.931 -5.778  16.555  1.00 15.56 ? 46  LEU B C   1 
ATOM   2477 O  O   . LEU B 1 46  ? -22.097 -6.869  16.046  1.00 16.30 ? 46  LEU B O   1 
ATOM   2478 C  CB  . LEU B 1 46  ? -19.709 -4.730  16.263  1.00 15.42 ? 46  LEU B CB  1 
ATOM   2479 C  CG  . LEU B 1 46  ? -18.432 -4.047  16.841  1.00 20.03 ? 46  LEU B CG  1 
ATOM   2480 C  CD1 . LEU B 1 46  ? -17.574 -3.528  15.681  1.00 19.41 ? 46  LEU B CD1 1 
ATOM   2481 C  CD2 . LEU B 1 46  ? -18.750 -2.843  17.711  1.00 22.05 ? 46  LEU B CD2 1 
ATOM   2482 N  N   . GLU B 1 47  ? -22.859 -4.839  16.537  1.00 18.53 ? 47  GLU B N   1 
ATOM   2483 C  CA  . GLU B 1 47  ? -24.069 -4.976  15.745  1.00 19.26 ? 47  GLU B CA  1 
ATOM   2484 C  C   . GLU B 1 47  ? -24.038 -3.919  14.606  1.00 17.67 ? 47  GLU B C   1 
ATOM   2485 O  O   . GLU B 1 47  ? -23.634 -2.759  14.824  1.00 19.51 ? 47  GLU B O   1 
ATOM   2486 C  CB  . GLU B 1 47  ? -25.326 -4.774  16.618  1.00 24.31 ? 47  GLU B CB  1 
ATOM   2487 C  CG  . GLU B 1 47  ? -25.471 -5.826  17.718  1.00 32.53 ? 47  GLU B CG  1 
ATOM   2488 C  CD  . GLU B 1 47  ? -26.885 -5.843  18.362  1.00 37.29 ? 47  GLU B CD  1 
ATOM   2489 O  OE1 . GLU B 1 47  ? -27.268 -4.879  19.106  1.00 37.87 ? 47  GLU B OE1 1 
ATOM   2490 O  OE2 . GLU B 1 47  ? -27.603 -6.843  18.137  1.00 39.36 ? 47  GLU B OE2 1 
ATOM   2491 N  N   . PHE B 1 48  ? -24.394 -4.410  13.429  1.00 19.15 ? 48  PHE B N   1 
ATOM   2492 C  CA  . PHE B 1 48  ? -24.257 -3.603  12.188  1.00 18.74 ? 48  PHE B CA  1 
ATOM   2493 C  C   . PHE B 1 48  ? -25.660 -3.191  11.759  1.00 20.10 ? 48  PHE B C   1 
ATOM   2494 O  O   . PHE B 1 48  ? -26.388 -4.050  11.232  1.00 25.88 ? 48  PHE B O   1 
ATOM   2495 C  CB  . PHE B 1 48  ? -23.544 -4.381  11.064  1.00 18.63 ? 48  PHE B CB  1 
ATOM   2496 C  CG  . PHE B 1 48  ? -22.213 -4.911  11.493  1.00 17.92 ? 48  PHE B CG  1 
ATOM   2497 C  CD1 . PHE B 1 48  ? -21.141 -4.065  11.622  1.00 16.44 ? 48  PHE B CD1 1 
ATOM   2498 C  CD2 . PHE B 1 48  ? -22.061 -6.254  11.861  1.00 18.26 ? 48  PHE B CD2 1 
ATOM   2499 C  CE1 . PHE B 1 48  ? -19.925 -4.509  12.129  1.00 17.76 ? 48  PHE B CE1 1 
ATOM   2500 C  CE2 . PHE B 1 48  ? -20.838 -6.726  12.361  1.00 19.54 ? 48  PHE B CE2 1 
ATOM   2501 C  CZ  . PHE B 1 48  ? -19.755 -5.855  12.457  1.00 17.39 ? 48  PHE B CZ  1 
ATOM   2502 N  N   . GLN B 1 49  ? -26.011 -1.933  11.997  1.00 17.09 ? 49  GLN B N   1 
ATOM   2503 C  CA  . GLN B 1 49  ? -27.432 -1.568  11.754  1.00 19.64 ? 49  GLN B CA  1 
ATOM   2504 C  C   . GLN B 1 49  ? -27.546 -0.658  10.524  1.00 16.81 ? 49  GLN B C   1 
ATOM   2505 O  O   . GLN B 1 49  ? -26.721 0.289   10.381  1.00 17.07 ? 49  GLN B O   1 
ATOM   2506 C  CB  . GLN B 1 49  ? -27.993 -0.806  12.906  1.00 23.07 ? 49  GLN B CB  1 
ATOM   2507 C  CG  . GLN B 1 49  ? -27.679 -1.386  14.275  1.00 32.53 ? 49  GLN B CG  1 
ATOM   2508 C  CD  . GLN B 1 49  ? -28.719 -2.336  14.827  1.00 40.31 ? 49  GLN B CD  1 
ATOM   2509 O  OE1 . GLN B 1 49  ? -28.748 -2.544  16.060  1.00 46.18 ? 49  GLN B OE1 1 
ATOM   2510 N  NE2 . GLN B 1 49  ? -29.582 -2.925  13.947  1.00 37.21 ? 49  GLN B NE2 1 
ATOM   2511 N  N   . GLY B 1 50  ? -28.549 -0.936  9.701   1.00 18.20 ? 50  GLY B N   1 
ATOM   2512 C  CA  . GLY B 1 50  ? -28.799 -0.036  8.566   1.00 16.89 ? 50  GLY B CA  1 
ATOM   2513 C  C   . GLY B 1 50  ? -27.742 -0.340  7.507   1.00 17.60 ? 50  GLY B C   1 
ATOM   2514 O  O   . GLY B 1 50  ? -27.580 0.456   6.603   1.00 16.95 ? 50  GLY B O   1 
ATOM   2515 N  N   . TYR B 1 51  ? -27.022 -1.479  7.615   1.00 15.21 ? 51  TYR B N   1 
ATOM   2516 C  CA  . TYR B 1 51  ? -25.997 -1.804  6.562   1.00 14.46 ? 51  TYR B CA  1 
ATOM   2517 C  C   . TYR B 1 51  ? -26.601 -2.332  5.278   1.00 15.05 ? 51  TYR B C   1 
ATOM   2518 O  O   . TYR B 1 51  ? -25.998 -2.347  4.201   1.00 14.31 ? 51  TYR B O   1 
ATOM   2519 C  CB  . TYR B 1 51  ? -25.007 -2.897  7.120   1.00 14.93 ? 51  TYR B CB  1 
ATOM   2520 C  CG  . TYR B 1 51  ? -23.780 -2.328  7.775   1.00 13.93 ? 51  TYR B CG  1 
ATOM   2521 C  CD1 . TYR B 1 51  ? -22.531 -2.838  7.408   1.00 13.99 ? 51  TYR B CD1 1 
ATOM   2522 C  CD2 . TYR B 1 51  ? -23.843 -1.354  8.799   1.00 12.25 ? 51  TYR B CD2 1 
ATOM   2523 C  CE1 . TYR B 1 51  ? -21.394 -2.299  8.042   1.00 12.99 ? 51  TYR B CE1 1 
ATOM   2524 C  CE2 . TYR B 1 51  ? -22.749 -0.821  9.436   1.00 13.11 ? 51  TYR B CE2 1 
ATOM   2525 C  CZ  . TYR B 1 51  ? -21.499 -1.290  9.028   1.00 12.78 ? 51  TYR B CZ  1 
ATOM   2526 O  OH  . TYR B 1 51  ? -20.408 -0.735  9.633   1.00 15.38 ? 51  TYR B OH  1 
ATOM   2527 N  N   . ASN B 1 52  ? -27.863 -2.820  5.345   1.00 15.65 ? 52  ASN B N   1 
ATOM   2528 C  CA  . ASN B 1 52  ? -28.546 -3.328  4.163   1.00 16.52 ? 52  ASN B CA  1 
ATOM   2529 C  C   . ASN B 1 52  ? -29.142 -2.216  3.318   1.00 16.03 ? 52  ASN B C   1 
ATOM   2530 O  O   . ASN B 1 52  ? -30.311 -1.951  3.408   1.00 15.70 ? 52  ASN B O   1 
ATOM   2531 C  CB  . ASN B 1 52  ? -29.708 -4.290  4.526   1.00 19.01 ? 52  ASN B CB  1 
ATOM   2532 C  CG  . ASN B 1 52  ? -30.183 -5.102  3.317   1.00 21.73 ? 52  ASN B CG  1 
ATOM   2533 O  OD1 . ASN B 1 52  ? -29.659 -5.027  2.207   1.00 27.45 ? 52  ASN B OD1 1 
ATOM   2534 N  ND2 . ASN B 1 52  ? -31.227 -5.937  3.538   1.00 25.48 ? 52  ASN B ND2 1 
ATOM   2535 N  N   . LEU B 1 53  ? -28.295 -1.548  2.543   1.00 13.89 ? 53  LEU B N   1 
ATOM   2536 C  CA  . LEU B 1 53  ? -28.749 -0.384  1.767   1.00 12.72 ? 53  LEU B CA  1 
ATOM   2537 C  C   . LEU B 1 53  ? -29.709 -0.857  0.553   1.00 11.56 ? 53  LEU B C   1 
ATOM   2538 O  O   . LEU B 1 53  ? -29.464 -1.844  -0.143  1.00 14.06 ? 53  LEU B O   1 
ATOM   2539 C  CB  . LEU B 1 53  ? -27.548 0.294   1.156   1.00 13.42 ? 53  LEU B CB  1 
ATOM   2540 C  CG  . LEU B 1 53  ? -26.522 0.702   2.208   1.00 13.64 ? 53  LEU B CG  1 
ATOM   2541 C  CD1 . LEU B 1 53  ? -25.472 1.358   1.348   1.00 15.12 ? 53  LEU B CD1 1 
ATOM   2542 C  CD2 . LEU B 1 53  ? -26.952 1.637   3.266   1.00 14.94 ? 53  LEU B CD2 1 
ATOM   2543 N  N   . SER B 1 54  ? -30.784 -0.095  0.349   1.00 12.48 ? 54  SER B N   1 
ATOM   2544 C  CA  . SER B 1 54  ? -31.722 -0.449  -0.692  1.00 13.20 ? 54  SER B CA  1 
ATOM   2545 C  C   . SER B 1 54  ? -31.095 -0.438  -2.076  1.00 13.97 ? 54  SER B C   1 
ATOM   2546 O  O   . SER B 1 54  ? -30.507 0.569   -2.422  1.00 14.51 ? 54  SER B O   1 
ATOM   2547 C  CB  . SER B 1 54  ? -32.902 0.510   -0.690  1.00 14.69 ? 54  SER B CB  1 
ATOM   2548 O  OG  . SER B 1 54  ? -33.792 0.123   -1.740  1.00 14.28 ? 54  SER B OG  1 
ATOM   2549 N  N   . ALA B 1 55  ? -31.246 -1.527  -2.860  1.00 14.11 ? 55  ALA B N   1 
ATOM   2550 C  CA  . ALA B 1 55  ? -30.836 -1.536  -4.258  1.00 14.91 ? 55  ALA B CA  1 
ATOM   2551 C  C   . ALA B 1 55  ? -31.524 -0.566  -5.181  1.00 14.96 ? 55  ALA B C   1 
ATOM   2552 O  O   . ALA B 1 55  ? -31.095 -0.362  -6.319  1.00 15.76 ? 55  ALA B O   1 
ATOM   2553 C  CB  . ALA B 1 55  ? -30.987 -2.954  -4.841  1.00 19.79 ? 55  ALA B CB  1 
ATOM   2554 N  N   . ASN B 1 56  ? -32.607 0.040   -4.693  1.00 14.63 ? 56  ASN B N   1 
ATOM   2555 C  CA  . ASN B 1 56  ? -33.312 1.027   -5.530  1.00 14.94 ? 56  ASN B CA  1 
ATOM   2556 C  C   . ASN B 1 56  ? -32.819 2.393   -5.222  1.00 13.79 ? 56  ASN B C   1 
ATOM   2557 O  O   . ASN B 1 56  ? -33.175 3.349   -5.925  1.00 17.36 ? 56  ASN B O   1 
ATOM   2558 C  CB  . ASN B 1 56  ? -34.832 1.006   -5.343  1.00 15.60 ? 56  ASN B CB  1 
ATOM   2559 C  CG  . ASN B 1 56  ? -35.459 -0.304  -5.783  1.00 16.79 ? 56  ASN B CG  1 
ATOM   2560 O  OD1 . ASN B 1 56  ? -34.895 -1.101  -6.514  1.00 20.33 ? 56  ASN B OD1 1 
ATOM   2561 N  ND2 . ASN B 1 56  ? -36.715 -0.480  -5.386  1.00 20.87 ? 56  ASN B ND2 1 
ATOM   2562 N  N   . LYS B 1 57  ? -31.929 2.488   -4.230  1.00 14.63 ? 57  LYS B N   1 
ATOM   2563 C  CA  . LYS B 1 57  ? -31.280 3.754   -3.912  1.00 13.81 ? 57  LYS B CA  1 
ATOM   2564 C  C   . LYS B 1 57  ? -29.834 3.676   -4.489  1.00 12.42 ? 57  LYS B C   1 
ATOM   2565 O  O   . LYS B 1 57  ? -29.395 2.668   -4.959  1.00 13.25 ? 57  LYS B O   1 
ATOM   2566 C  CB  . LYS B 1 57  ? -31.240 3.958   -2.412  1.00 16.03 ? 57  LYS B CB  1 
ATOM   2567 C  CG  . LYS B 1 57  ? -32.590 4.422   -1.820  1.00 17.36 ? 57  LYS B CG  1 
ATOM   2568 C  CD  . LYS B 1 57  ? -32.480 4.478   -0.318  1.00 23.26 ? 57  LYS B CD  1 
ATOM   2569 C  CE  . LYS B 1 57  ? -33.362 5.545   0.309   1.00 29.94 ? 57  LYS B CE  1 
ATOM   2570 N  NZ  . LYS B 1 57  ? -33.433 5.405   1.808   1.00 35.62 ? 57  LYS B NZ  1 
ATOM   2571 N  N   . GLN B 1 58  ? -29.206 4.832   -4.536  1.00 12.15 ? 58  GLN B N   1 
ATOM   2572 C  CA  . GLN B 1 58  ? -27.821 4.921   -5.067  1.00 12.67 ? 58  GLN B CA  1 
ATOM   2573 C  C   . GLN B 1 58  ? -26.929 5.845   -4.214  1.00 11.05 ? 58  GLN B C   1 
ATOM   2574 O  O   . GLN B 1 58  ? -27.346 6.806   -3.530  1.00 12.75 ? 58  GLN B O   1 
ATOM   2575 C  CB  . GLN B 1 58  ? -27.748 5.182   -6.568  1.00 18.00 ? 58  GLN B CB  1 
ATOM   2576 C  CG  . GLN B 1 58  ? -28.206 6.564   -6.841  1.00 18.12 ? 58  GLN B CG  1 
ATOM   2577 C  CD  . GLN B 1 58  ? -28.508 6.796   -8.311  1.00 21.45 ? 58  GLN B CD  1 
ATOM   2578 O  OE1 . GLN B 1 58  ? -28.465 5.851   -9.180  1.00 22.44 ? 58  GLN B OE1 1 
ATOM   2579 N  NE2 . GLN B 1 58  ? -28.792 8.100   -8.628  1.00 25.33 ? 58  GLN B NE2 1 
ATOM   2580 N  N   . PHE B 1 59  ? -25.631 5.477   -4.192  1.00 10.59 ? 59  PHE B N   1 
ATOM   2581 C  CA  . PHE B 1 59  ? -24.621 6.030   -3.296  1.00 10.28 ? 59  PHE B CA  1 
ATOM   2582 C  C   . PHE B 1 59  ? -23.431 6.464   -4.127  1.00 9.69  ? 59  PHE B C   1 
ATOM   2583 O  O   . PHE B 1 59  ? -23.041 5.791   -5.083  1.00 11.02 ? 59  PHE B O   1 
ATOM   2584 C  CB  . PHE B 1 59  ? -24.263 4.952   -2.250  1.00 11.49 ? 59  PHE B CB  1 
ATOM   2585 C  CG  . PHE B 1 59  ? -25.514 4.556   -1.460  1.00 11.16 ? 59  PHE B CG  1 
ATOM   2586 C  CD1 . PHE B 1 59  ? -26.384 3.550   -1.976  1.00 11.68 ? 59  PHE B CD1 1 
ATOM   2587 C  CD2 . PHE B 1 59  ? -25.834 5.275   -0.308  1.00 12.29 ? 59  PHE B CD2 1 
ATOM   2588 C  CE1 . PHE B 1 59  ? -27.601 3.316   -1.267  1.00 10.89 ? 59  PHE B CE1 1 
ATOM   2589 C  CE2 . PHE B 1 59  ? -27.082 5.060   0.379   1.00 11.85 ? 59  PHE B CE2 1 
ATOM   2590 C  CZ  . PHE B 1 59  ? -27.915 4.064   -0.120  1.00 11.77 ? 59  PHE B CZ  1 
ATOM   2591 N  N   . LEU B 1 60  ? -22.941 7.625   -3.780  1.00 10.45 ? 60  LEU B N   1 
ATOM   2592 C  CA  . LEU B 1 60  ? -21.893 8.269   -4.566  1.00 9.74  ? 60  LEU B CA  1 
ATOM   2593 C  C   . LEU B 1 60  ? -20.510 7.676   -4.368  1.00 9.66  ? 60  LEU B C   1 
ATOM   2594 O  O   . LEU B 1 60  ? -19.978 7.642   -3.242  1.00 10.71 ? 60  LEU B O   1 
ATOM   2595 C  CB  . LEU B 1 60  ? -21.832 9.767   -4.241  1.00 12.84 ? 60  LEU B CB  1 
ATOM   2596 C  CG  . LEU B 1 60  ? -21.039 10.781  -5.094  1.00 14.06 ? 60  LEU B CG  1 
ATOM   2597 C  CD1 . LEU B 1 60  ? -21.843 10.871  -6.404  1.00 13.53 ? 60  LEU B CD1 1 
ATOM   2598 C  CD2 . LEU B 1 60  ? -20.875 12.144  -4.405  1.00 16.10 ? 60  LEU B CD2 1 
ATOM   2599 N  N   . LEU B 1 61  ? -19.935 7.237   -5.461  1.00 9.46  ? 61  LEU B N   1 
ATOM   2600 C  CA  . LEU B 1 61  ? -18.543 6.777   -5.519  1.00 9.30  ? 61  LEU B CA  1 
ATOM   2601 C  C   . LEU B 1 61  ? -17.635 7.873   -6.083  1.00 10.18 ? 61  LEU B C   1 
ATOM   2602 O  O   . LEU B 1 61  ? -18.000 8.529   -7.017  1.00 12.08 ? 61  LEU B O   1 
ATOM   2603 C  CB  . LEU B 1 61  ? -18.528 5.514   -6.375  1.00 10.88 ? 61  LEU B CB  1 
ATOM   2604 C  CG  . LEU B 1 61  ? -17.190 4.817   -6.520  1.00 10.72 ? 61  LEU B CG  1 
ATOM   2605 C  CD1 . LEU B 1 61  ? -16.963 3.907   -5.263  1.00 12.42 ? 61  LEU B CD1 1 
ATOM   2606 C  CD2 . LEU B 1 61  ? -17.209 3.816   -7.665  1.00 12.13 ? 61  LEU B CD2 1 
ATOM   2607 N  N   . THR B 1 62  ? -16.518 8.183   -5.423  1.00 9.49  ? 62  THR B N   1 
ATOM   2608 C  CA  . THR B 1 62  ? -15.714 9.335   -5.866  1.00 9.88  ? 62  THR B CA  1 
ATOM   2609 C  C   . THR B 1 62  ? -14.234 8.889   -5.858  1.00 10.37 ? 62  THR B C   1 
ATOM   2610 O  O   . THR B 1 62  ? -13.758 8.290   -4.877  1.00 11.62 ? 62  THR B O   1 
ATOM   2611 C  CB  . THR B 1 62  ? -15.801 10.444  -4.837  1.00 12.30 ? 62  THR B CB  1 
ATOM   2612 O  OG1 . THR B 1 62  ? -17.138 10.896  -4.697  1.00 15.49 ? 62  THR B OG1 1 
ATOM   2613 C  CG2 . THR B 1 62  ? -14.928 11.719  -5.246  1.00 15.50 ? 62  THR B CG2 1 
ATOM   2614 N  N   . ASN B 1 63  ? -13.482 9.279   -6.889  1.00 10.35 ? 63  ASN B N   1 
ATOM   2615 C  CA  . ASN B 1 63  ? -11.996 9.227   -6.826  1.00 10.33 ? 63  ASN B CA  1 
ATOM   2616 C  C   . ASN B 1 63  ? -11.508 10.540  -6.307  1.00 11.95 ? 63  ASN B C   1 
ATOM   2617 O  O   . ASN B 1 63  ? -11.702 11.621  -6.903  1.00 10.39 ? 63  ASN B O   1 
ATOM   2618 C  CB  . ASN B 1 63  ? -11.516 8.898   -8.289  1.00 10.81 ? 63  ASN B CB  1 
ATOM   2619 C  CG  . ASN B 1 63  ? -10.012 8.963   -8.436  1.00 9.25  ? 63  ASN B CG  1 
ATOM   2620 O  OD1 . ASN B 1 63  ? -9.293  9.576   -7.611  1.00 9.34  ? 63  ASN B OD1 1 
ATOM   2621 N  ND2 . ASN B 1 63  ? -9.515  8.250   -9.462  1.00 9.05  ? 63  ASN B ND2 1 
ATOM   2622 N  N   . ASN B 1 64  ? -10.878 10.480  -5.126  1.00 11.49 ? 64  ASN B N   1 
ATOM   2623 C  CA  . ASN B 1 64  ? -10.474 11.697  -4.513  1.00 12.34 ? 64  ASN B CA  1 
ATOM   2624 C  C   . ASN B 1 64  ? -8.972  12.013  -4.730  1.00 12.79 ? 64  ASN B C   1 
ATOM   2625 O  O   . ASN B 1 64  ? -8.449  12.927  -4.103  1.00 13.83 ? 64  ASN B O   1 
ATOM   2626 C  CB  . ASN B 1 64  ? -10.831 11.702  -3.014  1.00 13.71 ? 64  ASN B CB  1 
ATOM   2627 C  CG  . ASN B 1 64  ? -10.114 10.671  -2.232  1.00 19.54 ? 64  ASN B CG  1 
ATOM   2628 O  OD1 . ASN B 1 64  ? -9.162  9.978   -2.689  1.00 15.71 ? 64  ASN B OD1 1 
ATOM   2629 N  ND2 . ASN B 1 64  ? -10.556 10.545  -0.965  1.00 20.15 ? 64  ASN B ND2 1 
ATOM   2630 N  N   . GLY B 1 65  ? -8.334  11.267  -5.645  1.00 11.75 ? 65  GLY B N   1 
ATOM   2631 C  CA  . GLY B 1 65  ? -6.910  11.482  -5.884  1.00 11.62 ? 65  GLY B CA  1 
ATOM   2632 C  C   . GLY B 1 65  ? -6.025  10.658  -5.001  1.00 11.01 ? 65  GLY B C   1 
ATOM   2633 O  O   . GLY B 1 65  ? -4.839  10.548  -5.290  1.00 11.76 ? 65  GLY B O   1 
ATOM   2634 N  N   . HIS B 1 66  ? -6.572  10.086  -3.903  1.00 11.48 ? 66  HIS B N   1 
ATOM   2635 C  CA  . HIS B 1 66  ? -5.794  9.147   -3.014  1.00 11.76 ? 66  HIS B CA  1 
ATOM   2636 C  C   . HIS B 1 66  ? -6.353  7.735   -2.903  1.00 13.37 ? 66  HIS B C   1 
ATOM   2637 O  O   . HIS B 1 66  ? -5.587  6.749   -2.659  1.00 13.48 ? 66  HIS B O   1 
ATOM   2638 C  CB  . HIS B 1 66  ? -5.656  9.781   -1.621  1.00 13.33 ? 66  HIS B CB  1 
ATOM   2639 C  CG  . HIS B 1 66  ? -5.078  11.165  -1.621  1.00 13.10 ? 66  HIS B CG  1 
ATOM   2640 N  ND1 . HIS B 1 66  ? -3.732  11.410  -1.847  1.00 13.52 ? 66  HIS B ND1 1 
ATOM   2641 C  CD2 . HIS B 1 66  ? -5.648  12.379  -1.367  1.00 14.91 ? 66  HIS B CD2 1 
ATOM   2642 C  CE1 . HIS B 1 66  ? -3.536  12.724  -1.760  1.00 14.64 ? 66  HIS B CE1 1 
ATOM   2643 N  NE2 . HIS B 1 66  ? -4.729  13.301  -1.485  1.00 17.44 ? 66  HIS B NE2 1 
ATOM   2644 N  N   . SER B 1 67  ? -7.710  7.590   -3.057  1.00 12.11 ? 67  SER B N   1 
ATOM   2645 C  CA  . SER B 1 67  ? -8.379  6.241   -2.977  1.00 12.47 ? 67  SER B CA  1 
ATOM   2646 C  C   . SER B 1 67  ? -9.645  6.419   -3.794  1.00 12.10 ? 67  SER B C   1 
ATOM   2647 O  O   . SER B 1 67  ? -9.891  7.474   -4.366  1.00 12.40 ? 67  SER B O   1 
ATOM   2648 C  CB  . SER B 1 67  ? -8.782  5.875   -1.500  1.00 14.38 ? 67  SER B CB  1 
ATOM   2649 O  OG  . SER B 1 67  ? -9.212  4.467   -1.422  1.00 13.73 ? 67  SER B OG  1 
ATOM   2650 N  N   . VAL B 1 68  ? -10.416 5.332   -3.821  1.00 12.81 ? 68  VAL B N   1 
ATOM   2651 C  CA  . VAL B 1 68  ? -11.799 5.562   -4.266  1.00 11.90 ? 68  VAL B CA  1 
ATOM   2652 C  C   . VAL B 1 68  ? -12.676 5.372   -3.028  1.00 11.22 ? 68  VAL B C   1 
ATOM   2653 O  O   . VAL B 1 68  ? -12.423 4.416   -2.243  1.00 11.22 ? 68  VAL B O   1 
ATOM   2654 C  CB  . VAL B 1 68  ? -12.061 4.535   -5.324  1.00 13.57 ? 68  VAL B CB  1 
ATOM   2655 C  CG1 . VAL B 1 68  ? -11.781 3.047   -4.961  1.00 13.07 ? 68  VAL B CG1 1 
ATOM   2656 C  CG2 . VAL B 1 68  ? -13.471 4.731   -5.929  1.00 15.91 ? 68  VAL B CG2 1 
ATOM   2657 N  N   . LYS B 1 69  ? -13.657 6.256   -2.855  1.00 11.69 ? 69  LYS B N   1 
ATOM   2658 C  CA  . LYS B 1 69  ? -14.548 6.177   -1.630  1.00 10.23 ? 69  LYS B CA  1 
ATOM   2659 C  C   . LYS B 1 69  ? -15.981 6.024   -2.098  1.00 11.11 ? 69  LYS B C   1 
ATOM   2660 O  O   . LYS B 1 69  ? -16.398 6.573   -3.117  1.00 11.05 ? 69  LYS B O   1 
ATOM   2661 C  CB  . LYS B 1 69  ? -14.335 7.407   -0.714  1.00 13.85 ? 69  LYS B CB  1 
ATOM   2662 C  CG  . LYS B 1 69  ? -14.539 8.739   -1.363  1.00 16.44 ? 69  LYS B CG  1 
ATOM   2663 C  CD  . LYS B 1 69  ? -14.508 9.798   -0.244  1.00 18.58 ? 69  LYS B CD  1 
ATOM   2664 C  CE  . LYS B 1 69  ? -14.926 11.118  -0.811  1.00 21.94 ? 69  LYS B CE  1 
ATOM   2665 N  NZ  . LYS B 1 69  ? -15.206 12.122  0.265   1.00 29.08 ? 69  LYS B NZ  1 
ATOM   2666 N  N   . LEU B 1 70  ? -16.779 5.340   -1.275  1.00 8.93  ? 70  LEU B N   1 
ATOM   2667 C  CA  . LEU B 1 70  ? -18.260 5.294   -1.466  1.00 9.16  ? 70  LEU B CA  1 
ATOM   2668 C  C   . LEU B 1 70  ? -18.825 6.002   -0.243  1.00 9.25  ? 70  LEU B C   1 
ATOM   2669 O  O   . LEU B 1 70  ? -18.576 5.628   0.919   1.00 8.74  ? 70  LEU B O   1 
ATOM   2670 C  CB  . LEU B 1 70  ? -18.660 3.849   -1.490  1.00 8.69  ? 70  LEU B CB  1 
ATOM   2671 C  CG  . LEU B 1 70  ? -20.175 3.662   -1.623  1.00 9.46  ? 70  LEU B CG  1 
ATOM   2672 C  CD1 . LEU B 1 70  ? -20.588 4.004   -3.059  1.00 10.47 ? 70  LEU B CD1 1 
ATOM   2673 C  CD2 . LEU B 1 70  ? -20.424 2.204   -1.315  1.00 10.29 ? 70  LEU B CD2 1 
ATOM   2674 N  N   . ASN B 1 71  ? -19.672 7.019   -0.482  1.00 10.41 ? 71  ASN B N   1 
ATOM   2675 C  CA  . ASN B 1 71  ? -20.353 7.721   0.635   1.00 9.82  ? 71  ASN B CA  1 
ATOM   2676 C  C   . ASN B 1 71  ? -21.480 6.837   1.195   1.00 10.91 ? 71  ASN B C   1 
ATOM   2677 O  O   . ASN B 1 71  ? -22.147 6.067   0.448   1.00 11.80 ? 71  ASN B O   1 
ATOM   2678 C  CB  . ASN B 1 71  ? -20.946 9.058   0.102   1.00 12.66 ? 71  ASN B CB  1 
ATOM   2679 C  CG  . ASN B 1 71  ? -19.927 10.095  -0.209  1.00 14.83 ? 71  ASN B CG  1 
ATOM   2680 O  OD1 . ASN B 1 71  ? -18.733 9.930   0.003   1.00 18.58 ? 71  ASN B OD1 1 
ATOM   2681 N  ND2 . ASN B 1 71  ? -20.454 11.274  -0.625  1.00 17.42 ? 71  ASN B ND2 1 
ATOM   2682 N  N   . LEU B 1 72  ? -21.624 6.912   2.525   1.00 10.94 ? 72  LEU B N   1 
ATOM   2683 C  CA  . LEU B 1 72  ? -22.587 6.045   3.185   1.00 13.27 ? 72  LEU B CA  1 
ATOM   2684 C  C   . LEU B 1 72  ? -23.556 6.894   3.953   1.00 13.29 ? 72  LEU B C   1 
ATOM   2685 O  O   . LEU B 1 72  ? -23.241 8.011   4.328   1.00 13.39 ? 72  LEU B O   1 
ATOM   2686 C  CB  . LEU B 1 72  ? -21.877 5.049   4.107   1.00 11.58 ? 72  LEU B CB  1 
ATOM   2687 C  CG  . LEU B 1 72  ? -20.922 4.066   3.422   1.00 11.75 ? 72  LEU B CG  1 
ATOM   2688 C  CD1 . LEU B 1 72  ? -19.993 3.396   4.425   1.00 11.64 ? 72  LEU B CD1 1 
ATOM   2689 C  CD2 . LEU B 1 72  ? -21.666 3.026   2.594   1.00 11.12 ? 72  LEU B CD2 1 
ATOM   2690 N  N   . PRO B 1 73  ? -24.772 6.341   4.146   1.00 13.53 ? 73  PRO B N   1 
ATOM   2691 C  CA  . PRO B 1 73  ? -25.823 7.160   4.775   1.00 16.20 ? 73  PRO B CA  1 
ATOM   2692 C  C   . PRO B 1 73  ? -25.730 7.163   6.302   1.00 18.56 ? 73  PRO B C   1 
ATOM   2693 O  O   . PRO B 1 73  ? -25.210 6.226   6.899   1.00 17.15 ? 73  PRO B O   1 
ATOM   2694 C  CB  . PRO B 1 73  ? -27.066 6.460   4.335   1.00 14.86 ? 73  PRO B CB  1 
ATOM   2695 C  CG  . PRO B 1 73  ? -26.712 4.996   4.212   1.00 14.75 ? 73  PRO B CG  1 
ATOM   2696 C  CD  . PRO B 1 73  ? -25.319 5.082   3.639   1.00 14.28 ? 73  PRO B CD  1 
ATOM   2697 N  N   . SER B 1 74  ? -26.214 8.226   6.931   1.00 24.15 ? 74  SER B N   1 
ATOM   2698 C  CA  . SER B 1 74  ? -25.982 8.284   8.391   1.00 23.67 ? 74  SER B CA  1 
ATOM   2699 C  C   . SER B 1 74  ? -26.967 7.419   9.164   1.00 25.25 ? 74  SER B C   1 
ATOM   2700 O  O   . SER B 1 74  ? -26.712 7.189   10.358  1.00 26.60 ? 74  SER B O   1 
ATOM   2701 C  CB  . SER B 1 74  ? -26.040 9.698   8.900   1.00 26.47 ? 74  SER B CB  1 
ATOM   2702 O  OG  . SER B 1 74  ? -27.321 10.206  8.607   1.00 26.28 ? 74  SER B OG  1 
ATOM   2703 N  N   . ASP B 1 75  ? -27.971 6.863   8.482   1.00 22.75 ? 75  ASP B N   1 
ATOM   2704 C  CA  . ASP B 1 75  ? -28.834 5.789   9.092   1.00 25.65 ? 75  ASP B CA  1 
ATOM   2705 C  C   . ASP B 1 75  ? -28.146 4.400   9.232   1.00 22.99 ? 75  ASP B C   1 
ATOM   2706 O  O   . ASP B 1 75  ? -28.694 3.440   9.737   1.00 23.31 ? 75  ASP B O   1 
ATOM   2707 C  CB  . ASP B 1 75  ? -30.279 5.706   8.483   1.00 29.82 ? 75  ASP B CB  1 
ATOM   2708 C  CG  . ASP B 1 75  ? -30.337 5.295   6.969   1.00 37.66 ? 75  ASP B CG  1 
ATOM   2709 O  OD1 . ASP B 1 75  ? -29.347 4.881   6.350   1.00 40.60 ? 75  ASP B OD1 1 
ATOM   2710 O  OD2 . ASP B 1 75  ? -31.448 5.380   6.356   1.00 44.19 ? 75  ASP B OD2 1 
ATOM   2711 N  N   . MET B 1 76  ? -26.895 4.336   8.792   1.00 19.35 ? 76  MET B N   1 
ATOM   2712 C  CA  . MET B 1 76  ? -26.068 3.159   8.928   1.00 17.28 ? 76  MET B CA  1 
ATOM   2713 C  C   . MET B 1 76  ? -25.159 3.355   10.135  1.00 16.25 ? 76  MET B C   1 
ATOM   2714 O  O   . MET B 1 76  ? -24.505 4.435   10.330  1.00 13.32 ? 76  MET B O   1 
ATOM   2715 C  CB  . MET B 1 76  ? -25.225 3.081   7.632   1.00 16.81 ? 76  MET B CB  1 
ATOM   2716 C  CG  . MET B 1 76  ? -24.261 1.941   7.631   1.00 15.97 ? 76  MET B CG  1 
ATOM   2717 S  SD  . MET B 1 76  ? -23.674 1.794   5.867   1.00 16.91 ? 76  MET B SD  1 
ATOM   2718 C  CE  . MET B 1 76  ? -22.317 0.676   6.163   1.00 13.60 ? 76  MET B CE  1 
ATOM   2719 N  N   . HIS B 1 77  ? -25.203 2.358   11.052  1.00 17.65 ? 77  HIS B N   1 
ATOM   2720 C  CA  . HIS B 1 77  ? -24.537 2.542   12.350  1.00 17.53 ? 77  HIS B CA  1 
ATOM   2721 C  C   . HIS B 1 77  ? -23.894 1.278   12.855  1.00 14.74 ? 77  HIS B C   1 
ATOM   2722 O  O   . HIS B 1 77  ? -24.205 0.152   12.407  1.00 17.94 ? 77  HIS B O   1 
ATOM   2723 C  CB  . HIS B 1 77  ? -25.578 2.906   13.475  1.00 19.86 ? 77  HIS B CB  1 
ATOM   2724 C  CG  . HIS B 1 77  ? -26.264 4.222   13.326  1.00 26.03 ? 77  HIS B CG  1 
ATOM   2725 N  ND1 . HIS B 1 77  ? -25.770 5.371   13.862  1.00 34.44 ? 77  HIS B ND1 1 
ATOM   2726 C  CD2 . HIS B 1 77  ? -27.484 4.547   12.744  1.00 29.83 ? 77  HIS B CD2 1 
ATOM   2727 C  CE1 . HIS B 1 77  ? -26.645 6.407   13.585  1.00 32.58 ? 77  HIS B CE1 1 
ATOM   2728 N  NE2 . HIS B 1 77  ? -27.671 5.901   12.887  1.00 31.18 ? 77  HIS B NE2 1 
ATOM   2729 N  N   . ILE B 1 78  ? -22.957 1.509   13.733  1.00 15.15 ? 78  ILE B N   1 
ATOM   2730 C  CA  . ILE B 1 78  ? -22.444 0.322   14.506  1.00 18.37 ? 78  ILE B CA  1 
ATOM   2731 C  C   . ILE B 1 78  ? -22.868 0.521   15.955  1.00 22.35 ? 78  ILE B C   1 
ATOM   2732 O  O   . ILE B 1 78  ? -22.759 1.630   16.513  1.00 22.70 ? 78  ILE B O   1 
ATOM   2733 C  CB  . ILE B 1 78  ? -20.933 0.035   14.347  1.00 20.11 ? 78  ILE B CB  1 
ATOM   2734 C  CG1 . ILE B 1 78  ? -20.036 1.272   14.459  1.00 23.15 ? 78  ILE B CG1 1 
ATOM   2735 C  CG2 . ILE B 1 78  ? -20.617 -0.651  13.009  1.00 22.17 ? 78  ILE B CG2 1 
ATOM   2736 C  CD1 . ILE B 1 78  ? -18.562 0.938   14.162  1.00 21.81 ? 78  ILE B CD1 1 
ATOM   2737 N  N   . GLN B 1 79  ? -23.391 -0.567  16.501  1.00 27.32 ? 79  GLN B N   1 
ATOM   2738 C  CA  . GLN B 1 79  ? -23.856 -0.618  17.872  1.00 33.38 ? 79  GLN B CA  1 
ATOM   2739 C  C   . GLN B 1 79  ? -23.027 -1.663  18.620  1.00 30.50 ? 79  GLN B C   1 
ATOM   2740 O  O   . GLN B 1 79  ? -22.712 -2.751  18.125  1.00 25.58 ? 79  GLN B O   1 
ATOM   2741 C  CB  . GLN B 1 79  ? -25.335 -0.996  17.860  1.00 39.11 ? 79  GLN B CB  1 
ATOM   2742 C  CG  . GLN B 1 79  ? -26.058 -0.943  19.206  1.00 51.34 ? 79  GLN B CG  1 
ATOM   2743 C  CD  . GLN B 1 79  ? -27.518 -1.313  19.045  1.00 57.34 ? 79  GLN B CD  1 
ATOM   2744 O  OE1 . GLN B 1 79  ? -28.167 -0.850  18.105  1.00 68.12 ? 79  GLN B OE1 1 
ATOM   2745 N  NE2 . GLN B 1 79  ? -28.037 -2.162  19.939  1.00 57.54 ? 79  GLN B NE2 1 
ATOM   2746 N  N   . GLY B 1 80  ? -22.759 -1.360  19.856  1.00 33.99 ? 80  GLY B N   1 
ATOM   2747 C  CA  . GLY B 1 80  ? -21.962 -2.267  20.659  1.00 32.19 ? 80  GLY B CA  1 
ATOM   2748 C  C   . GLY B 1 80  ? -20.931 -1.393  21.307  1.00 29.72 ? 80  GLY B C   1 
ATOM   2749 O  O   . GLY B 1 80  ? -20.500 -1.668  22.440  1.00 27.93 ? 80  GLY B O   1 
ATOM   2750 N  N   . LEU B 1 81  ? -20.559 -0.296  20.626  1.00 29.21 ? 81  LEU B N   1 
ATOM   2751 C  CA  . LEU B 1 81  ? -19.647 0.660   21.244  1.00 30.37 ? 81  LEU B CA  1 
ATOM   2752 C  C   . LEU B 1 81  ? -20.354 1.463   22.332  1.00 33.75 ? 81  LEU B C   1 
ATOM   2753 O  O   . LEU B 1 81  ? -21.591 1.332   22.526  1.00 36.81 ? 81  LEU B O   1 
ATOM   2754 C  CB  . LEU B 1 81  ? -18.919 1.551   20.208  1.00 28.86 ? 81  LEU B CB  1 
ATOM   2755 C  CG  . LEU B 1 81  ? -18.190 0.732   19.119  1.00 30.50 ? 81  LEU B CG  1 
ATOM   2756 C  CD1 . LEU B 1 81  ? -17.553 1.582   18.031  1.00 30.13 ? 81  LEU B CD1 1 
ATOM   2757 C  CD2 . LEU B 1 81  ? -17.097 -0.084  19.753  1.00 28.48 ? 81  LEU B CD2 1 
ATOM   2758 N  N   . GLN B 1 82  ? -19.589 2.270   23.047  1.00 31.72 ? 82  GLN B N   1 
ATOM   2759 C  CA  . GLN B 1 82  ? -20.158 3.013   24.198  1.00 37.03 ? 82  GLN B CA  1 
ATOM   2760 C  C   . GLN B 1 82  ? -20.840 4.319   23.780  1.00 40.20 ? 82  GLN B C   1 
ATOM   2761 O  O   . GLN B 1 82  ? -21.296 5.107   24.632  1.00 37.12 ? 82  GLN B O   1 
ATOM   2762 C  CB  . GLN B 1 82  ? -19.106 3.273   25.244  1.00 34.37 ? 82  GLN B CB  1 
ATOM   2763 C  CG  . GLN B 1 82  ? -18.550 2.023   25.910  1.00 34.96 ? 82  GLN B CG  1 
ATOM   2764 C  CD  . GLN B 1 82  ? -17.445 2.407   26.891  1.00 40.09 ? 82  GLN B CD  1 
ATOM   2765 O  OE1 . GLN B 1 82  ? -17.497 2.098   28.085  1.00 38.51 ? 82  GLN B OE1 1 
ATOM   2766 N  NE2 . GLN B 1 82  ? -16.471 3.168   26.394  1.00 38.97 ? 82  GLN B NE2 1 
ATOM   2767 N  N   . SER B 1 83  ? -20.859 4.553   22.463  1.00 40.06 ? 83  SER B N   1 
ATOM   2768 C  CA  . SER B 1 83  ? -21.723 5.549   21.810  1.00 39.10 ? 83  SER B CA  1 
ATOM   2769 C  C   . SER B 1 83  ? -22.128 4.926   20.499  1.00 35.38 ? 83  SER B C   1 
ATOM   2770 O  O   . SER B 1 83  ? -21.485 3.968   20.034  1.00 30.63 ? 83  SER B O   1 
ATOM   2771 C  CB  . SER B 1 83  ? -20.955 6.842   21.501  1.00 42.46 ? 83  SER B CB  1 
ATOM   2772 O  OG  . SER B 1 83  ? -20.839 7.658   22.640  1.00 48.19 ? 83  SER B OG  1 
ATOM   2773 N  N   . ARG B 1 84  ? -23.177 5.432   19.861  1.00 33.57 ? 84  ARG B N   1 
ATOM   2774 C  CA  . ARG B 1 84  ? -23.387 4.874   18.561  1.00 31.81 ? 84  ARG B CA  1 
ATOM   2775 C  C   . ARG B 1 84  ? -22.472 5.641   17.556  1.00 28.17 ? 84  ARG B C   1 
ATOM   2776 O  O   . ARG B 1 84  ? -22.140 6.837   17.730  1.00 26.10 ? 84  ARG B O   1 
ATOM   2777 C  CB  . ARG B 1 84  ? -24.861 4.705   18.219  1.00 35.54 ? 84  ARG B CB  1 
ATOM   2778 C  CG  . ARG B 1 84  ? -25.481 5.682   17.267  1.00 38.73 ? 84  ARG B CG  1 
ATOM   2779 C  CD  . ARG B 1 84  ? -26.786 5.029   16.850  1.00 42.56 ? 84  ARG B CD  1 
ATOM   2780 N  NE  . ARG B 1 84  ? -27.750 5.994   16.359  1.00 49.14 ? 84  ARG B NE  1 
ATOM   2781 C  CZ  . ARG B 1 84  ? -29.002 5.691   16.034  1.00 46.17 ? 84  ARG B CZ  1 
ATOM   2782 N  NH1 . ARG B 1 84  ? -29.446 4.447   16.161  1.00 48.80 ? 84  ARG B NH1 1 
ATOM   2783 N  NH2 . ARG B 1 84  ? -29.820 6.645   15.608  1.00 54.97 ? 84  ARG B NH2 1 
ATOM   2784 N  N   . TYR B 1 85  ? -22.000 4.898   16.563  1.00 23.85 ? 85  TYR B N   1 
ATOM   2785 C  CA  . TYR B 1 85  ? -21.097 5.494   15.566  1.00 19.23 ? 85  TYR B CA  1 
ATOM   2786 C  C   . TYR B 1 85  ? -21.797 5.321   14.304  1.00 16.25 ? 85  TYR B C   1 
ATOM   2787 O  O   . TYR B 1 85  ? -22.229 4.193   13.954  1.00 19.95 ? 85  TYR B O   1 
ATOM   2788 C  CB  . TYR B 1 85  ? -19.764 4.750   15.482  1.00 17.65 ? 85  TYR B CB  1 
ATOM   2789 C  CG  . TYR B 1 85  ? -18.872 5.151   16.549  1.00 19.78 ? 85  TYR B CG  1 
ATOM   2790 C  CD1 . TYR B 1 85  ? -17.872 6.086   16.341  1.00 17.05 ? 85  TYR B CD1 1 
ATOM   2791 C  CD2 . TYR B 1 85  ? -19.018 4.607   17.832  1.00 21.83 ? 85  TYR B CD2 1 
ATOM   2792 C  CE1 . TYR B 1 85  ? -17.014 6.475   17.329  1.00 20.53 ? 85  TYR B CE1 1 
ATOM   2793 C  CE2 . TYR B 1 85  ? -18.132 4.990   18.841  1.00 22.47 ? 85  TYR B CE2 1 
ATOM   2794 C  CZ  . TYR B 1 85  ? -17.161 5.949   18.596  1.00 23.91 ? 85  TYR B CZ  1 
ATOM   2795 O  OH  . TYR B 1 85  ? -16.270 6.376   19.591  1.00 27.97 ? 85  TYR B OH  1 
ATOM   2796 N  N   . SER B 1 86  ? -21.911 6.413   13.536  1.00 16.05 ? 86  SER B N   1 
ATOM   2797 C  CA  . SER B 1 86  ? -22.636 6.322   12.245  1.00 16.11 ? 86  SER B CA  1 
ATOM   2798 C  C   . SER B 1 86  ? -21.680 6.339   11.032  1.00 11.65 ? 86  SER B C   1 
ATOM   2799 O  O   . SER B 1 86  ? -20.682 7.019   11.121  1.00 14.76 ? 86  SER B O   1 
ATOM   2800 C  CB  . SER B 1 86  ? -23.506 7.586   12.045  1.00 23.60 ? 86  SER B CB  1 
ATOM   2801 O  OG  . SER B 1 86  ? -24.722 7.445   12.789  1.00 24.39 ? 86  SER B OG  1 
ATOM   2802 N  N   . ALA B 1 87  ? -22.040 5.577   10.020  1.00 13.51 ? 87  ALA B N   1 
ATOM   2803 C  CA  . ALA B 1 87  ? -21.174 5.400   8.793   1.00 13.77 ? 87  ALA B CA  1 
ATOM   2804 C  C   . ALA B 1 87  ? -21.010 6.780   8.115   1.00 13.82 ? 87  ALA B C   1 
ATOM   2805 O  O   . ALA B 1 87  ? -21.918 7.650   8.133   1.00 14.06 ? 87  ALA B O   1 
ATOM   2806 C  CB  . ALA B 1 87  ? -21.677 4.315   7.863   1.00 16.03 ? 87  ALA B CB  1 
ATOM   2807 N  N   . THR B 1 88  ? -19.846 7.012   7.524   1.00 10.93 ? 88  THR B N   1 
ATOM   2808 C  CA  . THR B 1 88  ? -19.679 8.157   6.603   1.00 13.13 ? 88  THR B CA  1 
ATOM   2809 C  C   . THR B 1 88  ? -19.165 7.762   5.231   1.00 11.68 ? 88  THR B C   1 
ATOM   2810 O  O   . THR B 1 88  ? -19.674 8.241   4.175   1.00 12.50 ? 88  THR B O   1 
ATOM   2811 C  CB  . THR B 1 88  ? -18.866 9.229   7.193   1.00 15.45 ? 88  THR B CB  1 
ATOM   2812 O  OG1 . THR B 1 88  ? -18.857 10.366  6.255   1.00 19.92 ? 88  THR B OG1 1 
ATOM   2813 C  CG2 . THR B 1 88  ? -17.416 8.794   7.541   1.00 15.52 ? 88  THR B CG2 1 
ATOM   2814 N  N   . GLN B 1 89  ? -18.196 6.821   5.169   1.00 9.70  ? 89  GLN B N   1 
ATOM   2815 C  CA  . GLN B 1 89  ? -17.703 6.395   3.872   1.00 9.65  ? 89  GLN B CA  1 
ATOM   2816 C  C   . GLN B 1 89  ? -16.971 5.059   4.010   1.00 8.02  ? 89  GLN B C   1 
ATOM   2817 O  O   . GLN B 1 89  ? -16.582 4.732   5.135   1.00 9.08  ? 89  GLN B O   1 
ATOM   2818 C  CB  . GLN B 1 89  ? -16.783 7.455   3.215   1.00 10.61 ? 89  GLN B CB  1 
ATOM   2819 C  CG  . GLN B 1 89  ? -15.622 7.877   4.100   1.00 12.75 ? 89  GLN B CG  1 
ATOM   2820 C  CD  . GLN B 1 89  ? -14.310 7.374   3.526   1.00 15.22 ? 89  GLN B CD  1 
ATOM   2821 O  OE1 . GLN B 1 89  ? -13.930 6.202   3.572   1.00 18.98 ? 89  GLN B OE1 1 
ATOM   2822 N  NE2 . GLN B 1 89  ? -13.531 8.268   3.195   1.00 14.05 ? 89  GLN B NE2 1 
ATOM   2823 N  N   . LEU B 1 90  ? -16.772 4.384   2.905   1.00 7.42  ? 90  LEU B N   1 
ATOM   2824 C  CA  . LEU B 1 90  ? -15.799 3.248   2.875   1.00 7.05  ? 90  LEU B CA  1 
ATOM   2825 C  C   . LEU B 1 90  ? -14.802 3.478   1.745   1.00 7.93  ? 90  LEU B C   1 
ATOM   2826 O  O   . LEU B 1 90  ? -15.073 4.199   0.793   1.00 8.65  ? 90  LEU B O   1 
ATOM   2827 C  CB  . LEU B 1 90  ? -16.435 1.810   2.829   1.00 7.74  ? 90  LEU B CB  1 
ATOM   2828 C  CG  . LEU B 1 90  ? -17.431 1.559   1.734   1.00 7.92  ? 90  LEU B CG  1 
ATOM   2829 C  CD1 . LEU B 1 90  ? -16.676 1.245   0.436   1.00 8.94  ? 90  LEU B CD1 1 
ATOM   2830 C  CD2 . LEU B 1 90  ? -18.296 0.310   2.068   1.00 8.45  ? 90  LEU B CD2 1 
ATOM   2831 N  N   . HIS B 1 91  ? -13.612 2.843   1.856   1.00 6.97  ? 91  HIS B N   1 
ATOM   2832 C  CA  . HIS B 1 91  ? -12.616 3.036   0.788   1.00 7.29  ? 91  HIS B CA  1 
ATOM   2833 C  C   . HIS B 1 91  ? -11.648 1.902   0.931   1.00 7.81  ? 91  HIS B C   1 
ATOM   2834 O  O   . HIS B 1 91  ? -11.784 1.091   1.850   1.00 7.23  ? 91  HIS B O   1 
ATOM   2835 C  CB  . HIS B 1 91  ? -11.926 4.401   0.951   1.00 7.48  ? 91  HIS B CB  1 
ATOM   2836 C  CG  . HIS B 1 91  ? -11.178 4.548   2.254   1.00 6.91  ? 91  HIS B CG  1 
ATOM   2837 N  ND1 . HIS B 1 91  ? -11.682 5.217   3.306   1.00 7.58  ? 91  HIS B ND1 1 
ATOM   2838 C  CD2 . HIS B 1 91  ? -9.931  4.071   2.652   1.00 7.38  ? 91  HIS B CD2 1 
ATOM   2839 C  CE1 . HIS B 1 91  ? -10.803 5.178   4.325   1.00 7.75  ? 91  HIS B CE1 1 
ATOM   2840 N  NE2 . HIS B 1 91  ? -9.732  4.476   3.923   1.00 7.43  ? 91  HIS B NE2 1 
ATOM   2841 N  N   . LEU B 1 92  ? -10.674 1.838   0.022   1.00 6.85  ? 92  LEU B N   1 
ATOM   2842 C  CA  . LEU B 1 92  ? -9.726  0.685   -0.012  1.00 7.54  ? 92  LEU B CA  1 
ATOM   2843 C  C   . LEU B 1 92  ? -8.292  1.178   -0.123  1.00 7.02  ? 92  LEU B C   1 
ATOM   2844 O  O   . LEU B 1 92  ? -8.015  2.349   -0.489  1.00 7.88  ? 92  LEU B O   1 
ATOM   2845 C  CB  . LEU B 1 92  ? -10.027 -0.257  -1.165  1.00 8.77  ? 92  LEU B CB  1 
ATOM   2846 C  CG  . LEU B 1 92  ? -11.358 -1.003  -0.990  1.00 9.34  ? 92  LEU B CG  1 
ATOM   2847 C  CD1 . LEU B 1 92  ? -12.288 -0.331  -1.951  1.00 12.76 ? 92  LEU B CD1 1 
ATOM   2848 C  CD2 . LEU B 1 92  ? -11.230 -2.458  -1.330  1.00 12.40 ? 92  LEU B CD2 1 
ATOM   2849 N  N   . HIS B 1 93  ? -7.411  0.243   0.222   1.00 7.40  ? 93  HIS B N   1 
ATOM   2850 C  CA  . HIS B 1 93  ? -5.958  0.435   0.024   1.00 6.70  ? 93  HIS B CA  1 
ATOM   2851 C  C   . HIS B 1 93  ? -5.411  -0.796  -0.607  1.00 7.13  ? 93  HIS B C   1 
ATOM   2852 O  O   . HIS B 1 93  ? -5.874  -1.879  -0.302  1.00 7.77  ? 93  HIS B O   1 
ATOM   2853 C  CB  . HIS B 1 93  ? -5.289  0.599   1.418   1.00 6.91  ? 93  HIS B CB  1 
ATOM   2854 C  CG  . HIS B 1 93  ? -5.776  1.748   2.209   1.00 7.61  ? 93  HIS B CG  1 
ATOM   2855 N  ND1 . HIS B 1 93  ? -5.182  3.018   2.141   1.00 7.74  ? 93  HIS B ND1 1 
ATOM   2856 C  CD2 . HIS B 1 93  ? -6.842  1.843   3.086   1.00 7.33  ? 93  HIS B CD2 1 
ATOM   2857 C  CE1 . HIS B 1 93  ? -5.854  3.861   2.957   1.00 8.94  ? 93  HIS B CE1 1 
ATOM   2858 N  NE2 . HIS B 1 93  ? -6.860  3.161   3.536   1.00 7.51  ? 93  HIS B NE2 1 
ATOM   2859 N  N   . TRP B 1 94  ? -4.433  -0.663  -1.529  1.00 7.30  ? 94  TRP B N   1 
ATOM   2860 C  CA  . TRP B 1 94  ? -3.961  -1.807  -2.345  1.00 6.53  ? 94  TRP B CA  1 
ATOM   2861 C  C   . TRP B 1 94  ? -2.536  -1.570  -2.817  1.00 6.93  ? 94  TRP B C   1 
ATOM   2862 O  O   . TRP B 1 94  ? -1.947  -0.491  -2.584  1.00 8.19  ? 94  TRP B O   1 
ATOM   2863 C  CB  . TRP B 1 94  ? -4.929  -2.077  -3.501  1.00 7.73  ? 94  TRP B CB  1 
ATOM   2864 C  CG  . TRP B 1 94  ? -5.098  -0.912  -4.460  1.00 7.24  ? 94  TRP B CG  1 
ATOM   2865 C  CD1 . TRP B 1 94  ? -4.328  -0.623  -5.601  1.00 7.52  ? 94  TRP B CD1 1 
ATOM   2866 C  CD2 . TRP B 1 94  ? -6.098  0.138   -4.365  1.00 7.31  ? 94  TRP B CD2 1 
ATOM   2867 N  NE1 . TRP B 1 94  ? -4.732  0.559   -6.160  1.00 7.97  ? 94  TRP B NE1 1 
ATOM   2868 C  CE2 . TRP B 1 94  ? -5.867  1.021   -5.510  1.00 7.26  ? 94  TRP B CE2 1 
ATOM   2869 C  CE3 . TRP B 1 94  ? -7.214  0.401   -3.538  1.00 7.95  ? 94  TRP B CE3 1 
ATOM   2870 C  CZ2 . TRP B 1 94  ? -6.658  2.159   -5.758  1.00 7.22  ? 94  TRP B CZ2 1 
ATOM   2871 C  CZ3 . TRP B 1 94  ? -7.977  1.553   -3.797  1.00 7.55  ? 94  TRP B CZ3 1 
ATOM   2872 C  CH2 . TRP B 1 94  ? -7.741  2.396   -4.905  1.00 6.67  ? 94  TRP B CH2 1 
ATOM   2873 N  N   . GLY B 1 95  ? -2.028  -2.648  -3.436  1.00 6.71  ? 95  GLY B N   1 
ATOM   2874 C  CA  . GLY B 1 95  ? -0.604  -2.646  -3.940  1.00 7.56  ? 95  GLY B CA  1 
ATOM   2875 C  C   . GLY B 1 95  ? -0.592  -2.345  -5.416  1.00 7.29  ? 95  GLY B C   1 
ATOM   2876 O  O   . GLY B 1 95  ? -1.099  -1.296  -5.919  1.00 8.17  ? 95  GLY B O   1 
ATOM   2877 N  N   . ASN B 1 96  ? 0.027   -3.233  -6.225  1.00 9.36  ? 96  ASN B N   1 
ATOM   2878 C  CA  . ASN B 1 96  ? 0.082   -2.955  -7.654  1.00 10.64 ? 96  ASN B CA  1 
ATOM   2879 C  C   . ASN B 1 96  ? 0.102   -4.305  -8.415  1.00 11.29 ? 96  ASN B C   1 
ATOM   2880 O  O   . ASN B 1 96  ? 0.208   -5.321  -7.762  1.00 10.64 ? 96  ASN B O   1 
ATOM   2881 C  CB  . ASN B 1 96  ? 1.358   -2.127  -7.939  1.00 12.22 ? 96  ASN B CB  1 
ATOM   2882 C  CG  . ASN B 1 96  ? 2.654   -2.893  -7.730  1.00 13.88 ? 96  ASN B CG  1 
ATOM   2883 O  OD1 . ASN B 1 96  ? 3.045   -3.642  -8.666  1.00 21.10 ? 96  ASN B OD1 1 
ATOM   2884 N  ND2 . ASN B 1 96  ? 3.313   -2.765  -6.592  1.00 14.04 ? 96  ASN B ND2 1 
ATOM   2885 N  N   . PRO B 1 97  ? -0.028  -4.301  -9.780  1.00 11.39 ? 97  PRO B N   1 
ATOM   2886 C  CA  . PRO B 1 97  ? -0.219  -5.581  -10.446 1.00 12.80 ? 97  PRO B CA  1 
ATOM   2887 C  C   . PRO B 1 97  ? 0.934   -6.539  -10.284 1.00 12.32 ? 97  PRO B C   1 
ATOM   2888 O  O   . PRO B 1 97  ? 0.717   -7.756  -10.333 1.00 14.27 ? 97  PRO B O   1 
ATOM   2889 C  CB  . PRO B 1 97  ? -0.388  -5.210  -11.919 1.00 13.21 ? 97  PRO B CB  1 
ATOM   2890 C  CG  . PRO B 1 97  ? -1.025  -3.847  -11.830 1.00 12.69 ? 97  PRO B CG  1 
ATOM   2891 C  CD  . PRO B 1 97  ? -0.256  -3.193  -10.708 1.00 13.09 ? 97  PRO B CD  1 
ATOM   2892 N  N   . ASN B 1 98  ? 2.157   -6.019  -10.055 1.00 10.58 ? 98  ASN B N   1 
ATOM   2893 C  CA  . ASN B 1 98  ? 3.323   -6.859  -9.927  1.00 13.13 ? 98  ASN B CA  1 
ATOM   2894 C  C   . ASN B 1 98  ? 3.640   -7.231  -8.489  1.00 15.04 ? 98  ASN B C   1 
ATOM   2895 O  O   . ASN B 1 98  ? 4.560   -8.007  -8.231  1.00 19.41 ? 98  ASN B O   1 
ATOM   2896 C  CB  . ASN B 1 98  ? 4.540   -6.161  -10.609 1.00 13.18 ? 98  ASN B CB  1 
ATOM   2897 C  CG  . ASN B 1 98  ? 4.309   -5.983  -12.104 1.00 12.59 ? 98  ASN B CG  1 
ATOM   2898 O  OD1 . ASN B 1 98  ? 4.237   -7.001  -12.856 1.00 13.77 ? 98  ASN B OD1 1 
ATOM   2899 N  ND2 . ASN B 1 98  ? 4.047   -4.711  -12.553 1.00 15.24 ? 98  ASN B ND2 1 
ATOM   2900 N  N   . ASP B 1 99  ? 2.873   -6.674  -7.558  1.00 13.11 ? 99  ASP B N   1 
ATOM   2901 C  CA  . ASP B 1 99  ? 3.108   -6.916  -6.113  1.00 14.58 ? 99  ASP B CA  1 
ATOM   2902 C  C   . ASP B 1 99  ? 1.751   -6.707  -5.387  1.00 11.41 ? 99  ASP B C   1 
ATOM   2903 O  O   . ASP B 1 99  ? 1.511   -5.606  -4.878  1.00 11.76 ? 99  ASP B O   1 
ATOM   2904 C  CB  . ASP B 1 99  ? 4.190   -5.945  -5.534  1.00 17.59 ? 99  ASP B CB  1 
ATOM   2905 C  CG  . ASP B 1 99  ? 4.502   -6.187  -4.005  1.00 23.01 ? 99  ASP B CG  1 
ATOM   2906 O  OD1 . ASP B 1 99  ? 4.212   -7.298  -3.512  1.00 25.85 ? 99  ASP B OD1 1 
ATOM   2907 O  OD2 . ASP B 1 99  ? 4.940   -5.198  -3.353  1.00 30.97 ? 99  ASP B OD2 1 
ATOM   2908 N  N   . PRO B 1 100 ? 0.834   -7.671  -5.490  1.00 10.47 ? 100 PRO B N   1 
ATOM   2909 C  CA  . PRO B 1 100 ? -0.548  -7.463  -4.978  1.00 10.72 ? 100 PRO B CA  1 
ATOM   2910 C  C   . PRO B 1 100 ? -0.522  -7.650  -3.444  1.00 10.85 ? 100 PRO B C   1 
ATOM   2911 O  O   . PRO B 1 100 ? -1.075  -8.602  -2.939  1.00 11.72 ? 100 PRO B O   1 
ATOM   2912 C  CB  . PRO B 1 100 ? -1.417  -8.507  -5.759  1.00 12.14 ? 100 PRO B CB  1 
ATOM   2913 C  CG  . PRO B 1 100 ? -0.363  -9.517  -6.165  1.00 13.97 ? 100 PRO B CG  1 
ATOM   2914 C  CD  . PRO B 1 100 ? 0.989   -8.948  -6.266  1.00 12.19 ? 100 PRO B CD  1 
ATOM   2915 N  N   . HIS B 1 101 ? 0.190   -6.760  -2.721  1.00 11.46 ? 101 HIS B N   1 
ATOM   2916 C  CA  . HIS B 1 101 ? 0.388   -6.865  -1.244  1.00 11.55 ? 101 HIS B CA  1 
ATOM   2917 C  C   . HIS B 1 101 ? 0.333   -5.563  -0.570  1.00 12.47 ? 101 HIS B C   1 
ATOM   2918 O  O   . HIS B 1 101 ? 1.278   -5.167  0.130   1.00 16.83 ? 101 HIS B O   1 
ATOM   2919 C  CB  . HIS B 1 101 ? 1.630   -7.621  -0.794  1.00 12.57 ? 101 HIS B CB  1 
ATOM   2920 C  CG  . HIS B 1 101 ? 1.723   -8.955  -1.395  1.00 15.94 ? 101 HIS B CG  1 
ATOM   2921 N  ND1 . HIS B 1 101 ? 1.116   -10.050 -0.852  1.00 21.71 ? 101 HIS B ND1 1 
ATOM   2922 C  CD2 . HIS B 1 101 ? 2.273   -9.349  -2.613  1.00 14.62 ? 101 HIS B CD2 1 
ATOM   2923 C  CE1 . HIS B 1 101 ? 1.289   -11.102 -1.684  1.00 19.19 ? 101 HIS B CE1 1 
ATOM   2924 N  NE2 . HIS B 1 101 ? 2.044   -10.705 -2.722  1.00 20.64 ? 101 HIS B NE2 1 
ATOM   2925 N  N   . GLY B 1 102 ? -0.849  -4.948  -0.627  1.00 9.92  ? 102 GLY B N   1 
ATOM   2926 C  CA  . GLY B 1 102 ? -1.023  -3.530  -0.226  1.00 8.60  ? 102 GLY B CA  1 
ATOM   2927 C  C   . GLY B 1 102 ? -2.021  -3.349  0.932   1.00 7.54  ? 102 GLY B C   1 
ATOM   2928 O  O   . GLY B 1 102 ? -2.477  -2.245  1.076   1.00 8.83  ? 102 GLY B O   1 
ATOM   2929 N  N   . SER B 1 103 ? -2.233  -4.356  1.827   1.00 8.24  ? 103 SER B N   1 
ATOM   2930 C  CA  . SER B 1 103 ? -2.921  -4.006  3.055   1.00 7.74  ? 103 SER B CA  1 
ATOM   2931 C  C   . SER B 1 103 ? -2.149  -2.990  3.915   1.00 8.43  ? 103 SER B C   1 
ATOM   2932 O  O   . SER B 1 103 ? -0.903  -2.812  3.743   1.00 8.66  ? 103 SER B O   1 
ATOM   2933 C  CB  . SER B 1 103 ? -3.277  -5.275  3.832   1.00 8.44  ? 103 SER B CB  1 
ATOM   2934 O  OG  . SER B 1 103 ? -2.064  -5.805  4.429   1.00 8.33  ? 103 SER B OG  1 
ATOM   2935 N  N   . GLU B 1 104 ? -2.856  -2.278  4.774   1.00 7.36  ? 104 GLU B N   1 
ATOM   2936 C  CA  . GLU B 1 104 ? -2.195  -1.363  5.712   1.00 7.41  ? 104 GLU B CA  1 
ATOM   2937 C  C   . GLU B 1 104 ? -1.772  -2.053  6.953   1.00 7.44  ? 104 GLU B C   1 
ATOM   2938 O  O   . GLU B 1 104 ? -0.578  -2.085  7.279   1.00 8.20  ? 104 GLU B O   1 
ATOM   2939 C  CB  . GLU B 1 104 ? -3.070  -0.136  6.039   1.00 8.52  ? 104 GLU B CB  1 
ATOM   2940 C  CG  . GLU B 1 104 ? -3.502  0.596   4.753   1.00 8.85  ? 104 GLU B CG  1 
ATOM   2941 C  CD  . GLU B 1 104 ? -3.544  2.047   5.052   1.00 8.53  ? 104 GLU B CD  1 
ATOM   2942 O  OE1 . GLU B 1 104 ? -4.560  2.511   5.634   1.00 8.44  ? 104 GLU B OE1 1 
ATOM   2943 O  OE2 . GLU B 1 104 ? -2.661  2.801   4.686   1.00 10.20 ? 104 GLU B OE2 1 
ATOM   2944 N  N   . HIS B 1 105 ? -2.718  -2.662  7.669   1.00 8.81  ? 105 HIS B N   1 
ATOM   2945 C  CA  . HIS B 1 105 ? -2.274  -3.588  8.719   1.00 8.27  ? 105 HIS B CA  1 
ATOM   2946 C  C   . HIS B 1 105 ? -1.636  -4.844  8.232   1.00 9.02  ? 105 HIS B C   1 
ATOM   2947 O  O   . HIS B 1 105 ? -1.992  -5.388  7.163   1.00 9.47  ? 105 HIS B O   1 
ATOM   2948 C  CB  . HIS B 1 105 ? -3.517  -3.949  9.570   1.00 8.43  ? 105 HIS B CB  1 
ATOM   2949 C  CG  . HIS B 1 105 ? -4.065  -2.753  10.303  1.00 8.49  ? 105 HIS B CG  1 
ATOM   2950 N  ND1 . HIS B 1 105 ? -5.001  -1.921  9.736   1.00 8.87  ? 105 HIS B ND1 1 
ATOM   2951 C  CD2 . HIS B 1 105 ? -3.750  -2.232  11.533  1.00 9.04  ? 105 HIS B CD2 1 
ATOM   2952 C  CE1 . HIS B 1 105 ? -5.219  -0.917  10.588  1.00 8.74  ? 105 HIS B CE1 1 
ATOM   2953 N  NE2 . HIS B 1 105 ? -4.460  -1.111  11.692  1.00 9.85  ? 105 HIS B NE2 1 
ATOM   2954 N  N   . THR B 1 106 ? -0.641  -5.316  8.992   1.00 9.42  ? 106 THR B N   1 
ATOM   2955 C  CA  . THR B 1 106 ? -0.051  -6.629  8.665   1.00 9.79  ? 106 THR B CA  1 
ATOM   2956 C  C   . THR B 1 106 ? -0.350  -7.533  9.899   1.00 9.43  ? 106 THR B C   1 
ATOM   2957 O  O   . THR B 1 106 ? -0.669  -7.066  10.954  1.00 9.20  ? 106 THR B O   1 
ATOM   2958 C  CB  . THR B 1 106 ? 1.447   -6.469  8.419   1.00 9.96  ? 106 THR B CB  1 
ATOM   2959 O  OG1 . THR B 1 106 ? 2.110   -5.836  9.537   1.00 11.43 ? 106 THR B OG1 1 
ATOM   2960 C  CG2 . THR B 1 106 ? 1.655   -5.604  7.146   1.00 11.45 ? 106 THR B CG2 1 
ATOM   2961 N  N   . VAL B 1 107 ? -0.229  -8.839  9.676   1.00 12.06 ? 107 VAL B N   1 
ATOM   2962 C  CA  . VAL B 1 107 ? -0.457  -9.815  10.732  1.00 13.14 ? 107 VAL B CA  1 
ATOM   2963 C  C   . VAL B 1 107 ? 0.737   -10.710 10.709  1.00 12.11 ? 107 VAL B C   1 
ATOM   2964 O  O   . VAL B 1 107 ? 1.042   -11.338 9.694   1.00 14.43 ? 107 VAL B O   1 
ATOM   2965 C  CB  . VAL B 1 107 ? -1.746  -10.677 10.485  1.00 12.38 ? 107 VAL B CB  1 
ATOM   2966 C  CG1 . VAL B 1 107 ? -1.845  -11.758 11.587  1.00 13.27 ? 107 VAL B CG1 1 
ATOM   2967 C  CG2 . VAL B 1 107 ? -3.023  -9.798  10.544  1.00 14.14 ? 107 VAL B CG2 1 
ATOM   2968 N  N   . SER B 1 108 ? 1.371   -10.757 11.884  1.00 14.08 ? 108 SER B N   1 
ATOM   2969 C  CA  . SER B 1 108 ? 2.667   -11.440 12.119  1.00 14.75 ? 108 SER B CA  1 
ATOM   2970 C  C   . SER B 1 108 ? 3.596   -11.175 10.924  1.00 14.78 ? 108 SER B C   1 
ATOM   2971 O  O   . SER B 1 108 ? 4.197   -12.102 10.347  1.00 15.83 ? 108 SER B O   1 
ATOM   2972 C  CB  . SER B 1 108 ? 2.451   -12.956 12.310  1.00 16.71 ? 108 SER B CB  1 
ATOM   2973 O  OG  . SER B 1 108 ? 1.533   -13.136 13.370  1.00 18.29 ? 108 SER B OG  1 
ATOM   2974 N  N   . GLY B 1 109 ? 3.689   -9.906  10.547  1.00 14.54 ? 109 GLY B N   1 
ATOM   2975 C  CA  . GLY B 1 109 ? 4.582   -9.463  9.566   1.00 14.89 ? 109 GLY B CA  1 
ATOM   2976 C  C   . GLY B 1 109 ? 4.188   -9.698  8.087   1.00 17.55 ? 109 GLY B C   1 
ATOM   2977 O  O   . GLY B 1 109 ? 4.954   -9.325  7.159   1.00 20.79 ? 109 GLY B O   1 
ATOM   2978 N  N   . GLN B 1 110 ? 3.009   -10.231 7.850   1.00 17.78 ? 110 GLN B N   1 
ATOM   2979 C  CA  . GLN B 1 110 ? 2.635   -10.444 6.434   1.00 18.54 ? 110 GLN B CA  1 
ATOM   2980 C  C   . GLN B 1 110 ? 1.553   -9.433  6.010   1.00 13.31 ? 110 GLN B C   1 
ATOM   2981 O  O   . GLN B 1 110 ? 0.603   -9.159  6.780   1.00 12.10 ? 110 GLN B O   1 
ATOM   2982 C  CB  . GLN B 1 110 ? 2.126   -11.851 6.236   1.00 22.52 ? 110 GLN B CB  1 
ATOM   2983 C  CG  . GLN B 1 110 ? 3.020   -12.937 6.873   1.00 27.66 ? 110 GLN B CG  1 
ATOM   2984 C  CD  . GLN B 1 110 ? 4.321   -13.209 6.086   1.00 34.35 ? 110 GLN B CD  1 
ATOM   2985 O  OE1 . GLN B 1 110 ? 4.638   -12.532 5.109   1.00 41.36 ? 110 GLN B OE1 1 
ATOM   2986 N  NE2 . GLN B 1 110 ? 5.078   -14.203 6.532   1.00 42.70 ? 110 GLN B NE2 1 
ATOM   2987 N  N   . HIS B 1 111 ? 1.749   -8.850  4.809   1.00 13.05 ? 111 HIS B N   1 
ATOM   2988 C  CA  . HIS B 1 111 ? 0.709   -8.056  4.131   1.00 13.67 ? 111 HIS B CA  1 
ATOM   2989 C  C   . HIS B 1 111 ? -0.303  -8.955  3.525   1.00 13.30 ? 111 HIS B C   1 
ATOM   2990 O  O   . HIS B 1 111 ? 0.026   -9.963  2.906   1.00 15.75 ? 111 HIS B O   1 
ATOM   2991 C  CB  . HIS B 1 111 ? 1.242   -7.211  2.952   1.00 16.59 ? 111 HIS B CB  1 
ATOM   2992 C  CG  . HIS B 1 111 ? 1.891   -5.966  3.354   1.00 13.60 ? 111 HIS B CG  1 
ATOM   2993 N  ND1 . HIS B 1 111 ? 1.201   -4.814  3.580   1.00 16.60 ? 111 HIS B ND1 1 
ATOM   2994 C  CD2 . HIS B 1 111 ? 3.226   -5.698  3.605   1.00 17.42 ? 111 HIS B CD2 1 
ATOM   2995 C  CE1 . HIS B 1 111 ? 2.079   -3.837  3.962   1.00 17.38 ? 111 HIS B CE1 1 
ATOM   2996 N  NE2 . HIS B 1 111 ? 3.320   -4.384  3.987   1.00 19.36 ? 111 HIS B NE2 1 
ATOM   2997 N  N   . PHE B 1 112 ? -1.554  -8.538  3.564   1.00 11.25 ? 112 PHE B N   1 
ATOM   2998 C  CA  . PHE B 1 112 ? -2.564  -9.112  2.755   1.00 10.01 ? 112 PHE B CA  1 
ATOM   2999 C  C   . PHE B 1 112 ? -2.648  -8.336  1.430   1.00 9.40  ? 112 PHE B C   1 
ATOM   3000 O  O   . PHE B 1 112 ? -1.974  -7.304  1.293   1.00 10.28 ? 112 PHE B O   1 
ATOM   3001 C  CB  . PHE B 1 112 ? -3.885  -8.986  3.593   1.00 11.33 ? 112 PHE B CB  1 
ATOM   3002 C  CG  . PHE B 1 112 ? -3.991  -10.070 4.648   1.00 13.55 ? 112 PHE B CG  1 
ATOM   3003 C  CD1 . PHE B 1 112 ? -4.613  -11.248 4.338   1.00 17.77 ? 112 PHE B CD1 1 
ATOM   3004 C  CD2 . PHE B 1 112 ? -3.374  -9.888  5.895   1.00 16.45 ? 112 PHE B CD2 1 
ATOM   3005 C  CE1 . PHE B 1 112 ? -4.694  -12.288 5.271   1.00 21.76 ? 112 PHE B CE1 1 
ATOM   3006 C  CE2 . PHE B 1 112 ? -3.450  -10.942 6.857   1.00 16.56 ? 112 PHE B CE2 1 
ATOM   3007 C  CZ  . PHE B 1 112 ? -4.092  -12.103 6.504   1.00 18.77 ? 112 PHE B CZ  1 
ATOM   3008 N  N   . ALA B 1 113 ? -3.466  -8.793  0.500   1.00 8.63  ? 113 ALA B N   1 
ATOM   3009 C  CA  . ALA B 1 113 ? -3.496  -8.156  -0.826  1.00 9.90  ? 113 ALA B CA  1 
ATOM   3010 C  C   . ALA B 1 113 ? -3.998  -6.707  -0.775  1.00 8.74  ? 113 ALA B C   1 
ATOM   3011 O  O   . ALA B 1 113 ? -3.531  -5.860  -1.528  1.00 9.42  ? 113 ALA B O   1 
ATOM   3012 C  CB  . ALA B 1 113 ? -4.404  -8.973  -1.717  1.00 10.85 ? 113 ALA B CB  1 
ATOM   3013 N  N   . ALA B 1 114 ? -5.015  -6.466  0.038   1.00 8.69  ? 114 ALA B N   1 
ATOM   3014 C  CA  . ALA B 1 114 ? -5.684  -5.131  0.076   1.00 7.45  ? 114 ALA B CA  1 
ATOM   3015 C  C   . ALA B 1 114 ? -6.402  -5.018  1.434   1.00 7.76  ? 114 ALA B C   1 
ATOM   3016 O  O   . ALA B 1 114 ? -6.340  -5.960  2.256   1.00 8.38  ? 114 ALA B O   1 
ATOM   3017 C  CB  . ALA B 1 114 ? -6.659  -4.953  -1.105  1.00 8.29  ? 114 ALA B CB  1 
ATOM   3018 N  N   . GLU B 1 115 ? -6.980  -3.843  1.670   1.00 7.82  ? 115 GLU B N   1 
ATOM   3019 C  CA  . GLU B 1 115 ? -7.732  -3.634  2.894   1.00 7.91  ? 115 GLU B CA  1 
ATOM   3020 C  C   . GLU B 1 115 ? -8.876  -2.701  2.653   1.00 8.47  ? 115 GLU B C   1 
ATOM   3021 O  O   . GLU B 1 115 ? -8.742  -1.701  1.938   1.00 8.61  ? 115 GLU B O   1 
ATOM   3022 C  CB  . GLU B 1 115 ? -6.741  -3.074  3.912   1.00 8.20  ? 115 GLU B CB  1 
ATOM   3023 C  CG  . GLU B 1 115 ? -7.286  -3.056  5.364   1.00 8.69  ? 115 GLU B CG  1 
ATOM   3024 C  CD  . GLU B 1 115 ? -6.221  -2.722  6.397   1.00 10.30 ? 115 GLU B CD  1 
ATOM   3025 O  OE1 . GLU B 1 115 ? -6.496  -2.035  7.421   1.00 10.78 ? 115 GLU B OE1 1 
ATOM   3026 O  OE2 . GLU B 1 115 ? -5.063  -3.199  6.238   1.00 8.90  ? 115 GLU B OE2 1 
ATOM   3027 N  N   . LEU B 1 116 ? -10.045 -3.014  3.221   1.00 7.72  ? 116 LEU B N   1 
ATOM   3028 C  CA  . LEU B 1 116 ? -11.255 -2.177  3.131   1.00 7.85  ? 116 LEU B CA  1 
ATOM   3029 C  C   . LEU B 1 116 ? -11.380 -1.477  4.491   1.00 8.08  ? 116 LEU B C   1 
ATOM   3030 O  O   . LEU B 1 116 ? -11.253 -2.130  5.583   1.00 8.28  ? 116 LEU B O   1 
ATOM   3031 C  CB  . LEU B 1 116 ? -12.499 -3.028  2.918   1.00 9.57  ? 116 LEU B CB  1 
ATOM   3032 C  CG  . LEU B 1 116 ? -13.830 -2.235  3.103   1.00 9.51  ? 116 LEU B CG  1 
ATOM   3033 C  CD1 . LEU B 1 116 ? -14.187 -1.511  1.816   1.00 11.55 ? 116 LEU B CD1 1 
ATOM   3034 C  CD2 . LEU B 1 116 ? -14.900 -3.273  3.300   1.00 10.74 ? 116 LEU B CD2 1 
ATOM   3035 N  N   . HIS B 1 117 ? -11.587 -0.183  4.484   1.00 7.12  ? 117 HIS B N   1 
ATOM   3036 C  CA  . HIS B 1 117 ? -11.940 0.632   5.686   1.00 8.25  ? 117 HIS B CA  1 
ATOM   3037 C  C   . HIS B 1 117 ? -13.354 1.159   5.587   1.00 8.31  ? 117 HIS B C   1 
ATOM   3038 O  O   . HIS B 1 117 ? -13.719 1.759   4.625   1.00 7.30  ? 117 HIS B O   1 
ATOM   3039 C  CB  . HIS B 1 117 ? -10.973 1.784   5.774   1.00 7.64  ? 117 HIS B CB  1 
ATOM   3040 C  CG  . HIS B 1 117 ? -9.595  1.324   6.146   1.00 8.38  ? 117 HIS B CG  1 
ATOM   3041 N  ND1 . HIS B 1 117 ? -8.468  2.033   5.906   1.00 7.87  ? 117 HIS B ND1 1 
ATOM   3042 C  CD2 . HIS B 1 117 ? -9.194  0.101   6.663   1.00 7.26  ? 117 HIS B CD2 1 
ATOM   3043 C  CE1 . HIS B 1 117 ? -7.404  1.383   6.364   1.00 7.48  ? 117 HIS B CE1 1 
ATOM   3044 N  NE2 . HIS B 1 117 ? -7.824  0.144   6.801   1.00 7.19  ? 117 HIS B NE2 1 
ATOM   3045 N  N   . ILE B 1 118 ? -14.169 0.883   6.627   1.00 9.10  ? 118 ILE B N   1 
ATOM   3046 C  CA  . ILE B 1 118 ? -15.495 1.538   6.728   1.00 9.47  ? 118 ILE B CA  1 
ATOM   3047 C  C   . ILE B 1 118 ? -15.432 2.535   7.894   1.00 9.94  ? 118 ILE B C   1 
ATOM   3048 O  O   . ILE B 1 118 ? -15.217 2.155   9.085   1.00 9.79  ? 118 ILE B O   1 
ATOM   3049 C  CB  . ILE B 1 118 ? -16.574 0.524   6.986   1.00 9.42  ? 118 ILE B CB  1 
ATOM   3050 C  CG1 . ILE B 1 118 ? -16.505 -0.684  5.990   1.00 10.33 ? 118 ILE B CG1 1 
ATOM   3051 C  CG2 . ILE B 1 118 ? -17.949 1.302   6.975   1.00 9.40  ? 118 ILE B CG2 1 
ATOM   3052 C  CD1 . ILE B 1 118 ? -17.603 -1.777  6.195   1.00 13.89 ? 118 ILE B CD1 1 
ATOM   3053 N  N   . VAL B 1 119 ? -15.450 3.831   7.562   1.00 10.43 ? 119 VAL B N   1 
ATOM   3054 C  CA  . VAL B 1 119 ? -15.237 4.916   8.496   1.00 10.45 ? 119 VAL B CA  1 
ATOM   3055 C  C   . VAL B 1 119 ? -16.575 5.369   9.089   1.00 11.87 ? 119 VAL B C   1 
ATOM   3056 O  O   . VAL B 1 119 ? -17.525 5.594   8.358   1.00 11.46 ? 119 VAL B O   1 
ATOM   3057 C  CB  . VAL B 1 119 ? -14.596 6.122   7.762   1.00 11.24 ? 119 VAL B CB  1 
ATOM   3058 C  CG1 . VAL B 1 119 ? -14.247 7.204   8.750   1.00 12.69 ? 119 VAL B CG1 1 
ATOM   3059 C  CG2 . VAL B 1 119 ? -13.309 5.663   6.962   1.00 10.59 ? 119 VAL B CG2 1 
ATOM   3060 N  N   . HIS B 1 120 ? -16.553 5.427   10.413  1.00 10.84 ? 120 HIS B N   1 
ATOM   3061 C  CA  . HIS B 1 120 ? -17.693 5.903   11.196  1.00 13.43 ? 120 HIS B CA  1 
ATOM   3062 C  C   . HIS B 1 120 ? -17.273 7.043   12.083  1.00 12.91 ? 120 HIS B C   1 
ATOM   3063 O  O   . HIS B 1 120 ? -16.101 7.264   12.467  1.00 12.01 ? 120 HIS B O   1 
ATOM   3064 C  CB  . HIS B 1 120 ? -18.320 4.721   12.053  1.00 12.85 ? 120 HIS B CB  1 
ATOM   3065 C  CG  . HIS B 1 120 ? -18.701 3.486   11.321  1.00 12.71 ? 120 HIS B CG  1 
ATOM   3066 N  ND1 . HIS B 1 120 ? -17.747 2.652   10.725  1.00 12.55 ? 120 HIS B ND1 1 
ATOM   3067 C  CD2 . HIS B 1 120 ? -19.924 2.854   11.136  1.00 12.35 ? 120 HIS B CD2 1 
ATOM   3068 C  CE1 . HIS B 1 120 ? -18.369 1.605   10.184  1.00 11.57 ? 120 HIS B CE1 1 
ATOM   3069 N  NE2 . HIS B 1 120 ? -19.723 1.704   10.438  1.00 14.91 ? 120 HIS B NE2 1 
ATOM   3070 N  N   . TYR B 1 121 ? -18.239 7.886   12.528  1.00 15.84 ? 121 TYR B N   1 
ATOM   3071 C  CA  . TYR B 1 121 ? -17.922 8.962   13.466  1.00 18.98 ? 121 TYR B CA  1 
ATOM   3072 C  C   . TYR B 1 121 ? -18.956 8.900   14.633  1.00 19.35 ? 121 TYR B C   1 
ATOM   3073 O  O   . TYR B 1 121 ? -20.047 8.438   14.431  1.00 20.78 ? 121 TYR B O   1 
ATOM   3074 C  CB  . TYR B 1 121 ? -17.995 10.365  12.755  1.00 19.69 ? 121 TYR B CB  1 
ATOM   3075 C  CG  . TYR B 1 121 ? -19.435 10.763  12.267  1.00 19.41 ? 121 TYR B CG  1 
ATOM   3076 C  CD1 . TYR B 1 121 ? -20.199 11.671  13.011  1.00 26.28 ? 121 TYR B CD1 1 
ATOM   3077 C  CD2 . TYR B 1 121 ? -19.987 10.255  11.086  1.00 20.53 ? 121 TYR B CD2 1 
ATOM   3078 C  CE1 . TYR B 1 121 ? -21.472 12.026  12.580  1.00 23.67 ? 121 TYR B CE1 1 
ATOM   3079 C  CE2 . TYR B 1 121 ? -21.268 10.600  10.635  1.00 23.00 ? 121 TYR B CE2 1 
ATOM   3080 C  CZ  . TYR B 1 121 ? -22.001 11.489  11.399  1.00 24.08 ? 121 TYR B CZ  1 
ATOM   3081 O  OH  . TYR B 1 121 ? -23.283 11.829  10.950  1.00 29.43 ? 121 TYR B OH  1 
ATOM   3082 N  N   . ASN B 1 122 ? -18.581 9.368   15.804  1.00 20.57 ? 122 ASN B N   1 
ATOM   3083 C  CA  . ASN B 1 122 ? -19.508 9.345   16.964  1.00 24.18 ? 122 ASN B CA  1 
ATOM   3084 C  C   . ASN B 1 122 ? -20.736 10.334  16.719  1.00 25.02 ? 122 ASN B C   1 
ATOM   3085 O  O   . ASN B 1 122 ? -20.606 11.552  16.849  1.00 24.34 ? 122 ASN B O   1 
ATOM   3086 C  CB  . ASN B 1 122 ? -18.698 9.650   18.233  1.00 27.51 ? 122 ASN B CB  1 
ATOM   3087 C  CG  . ASN B 1 122 ? -19.504 9.434   19.522  1.00 32.57 ? 122 ASN B CG  1 
ATOM   3088 O  OD1 . ASN B 1 122 ? -20.715 9.586   19.529  1.00 34.36 ? 122 ASN B OD1 1 
ATOM   3089 N  ND2 . ASN B 1 122 ? -18.813 9.084   20.612  1.00 35.34 ? 122 ASN B ND2 1 
ATOM   3090 N  N   . SER B 1 123 ? -21.843 9.794   16.263  1.00 31.95 ? 123 SER B N   1 
ATOM   3091 C  CA  . SER B 1 123 ? -22.997 10.669  15.933  1.00 32.62 ? 123 SER B CA  1 
ATOM   3092 C  C   . SER B 1 123 ? -23.741 11.159  17.217  1.00 41.95 ? 123 SER B C   1 
ATOM   3093 O  O   . SER B 1 123 ? -24.410 12.206  17.184  1.00 43.66 ? 123 SER B O   1 
ATOM   3094 C  CB  . SER B 1 123 ? -23.905 10.020  14.910  1.00 33.69 ? 123 SER B CB  1 
ATOM   3095 O  OG  . SER B 1 123 ? -24.198 8.687   15.275  1.00 36.86 ? 123 SER B OG  1 
ATOM   3096 N  N   . ASP B 1 124 ? -23.586 10.424  18.331  1.00 43.19 ? 124 ASP B N   1 
ATOM   3097 C  CA  . ASP B 1 124 ? -24.039 10.888  19.671  1.00 47.50 ? 124 ASP B CA  1 
ATOM   3098 C  C   . ASP B 1 124 ? -23.549 12.304  19.960  1.00 46.09 ? 124 ASP B C   1 
ATOM   3099 O  O   . ASP B 1 124 ? -24.321 13.162  20.402  1.00 44.36 ? 124 ASP B O   1 
ATOM   3100 C  CB  . ASP B 1 124 ? -23.532 9.984   20.827  1.00 45.24 ? 124 ASP B CB  1 
ATOM   3101 C  CG  . ASP B 1 124 ? -24.307 8.666   20.969  1.00 52.94 ? 124 ASP B CG  1 
ATOM   3102 O  OD1 . ASP B 1 124 ? -25.152 8.325   20.100  1.00 48.27 ? 124 ASP B OD1 1 
ATOM   3103 O  OD2 . ASP B 1 124 ? -24.057 7.960   21.980  1.00 53.18 ? 124 ASP B OD2 1 
ATOM   3104 N  N   . LEU B 1 125 ? -22.265 12.529  19.690  1.00 45.40 ? 125 LEU B N   1 
ATOM   3105 C  CA  . LEU B 1 125 ? -21.543 13.708  20.122  1.00 40.28 ? 125 LEU B CA  1 
ATOM   3106 C  C   . LEU B 1 125 ? -21.223 14.676  19.015  1.00 43.64 ? 125 LEU B C   1 
ATOM   3107 O  O   . LEU B 1 125 ? -20.874 15.832  19.306  1.00 47.46 ? 125 LEU B O   1 
ATOM   3108 C  CB  . LEU B 1 125 ? -20.215 13.331  20.802  1.00 39.53 ? 125 LEU B CB  1 
ATOM   3109 C  CG  . LEU B 1 125 ? -20.122 12.354  21.971  1.00 41.32 ? 125 LEU B CG  1 
ATOM   3110 C  CD1 . LEU B 1 125 ? -18.711 12.222  22.528  1.00 40.11 ? 125 LEU B CD1 1 
ATOM   3111 C  CD2 . LEU B 1 125 ? -21.113 12.694  23.077  1.00 39.88 ? 125 LEU B CD2 1 
ATOM   3112 N  N   . TYR B 1 126 ? -21.302 14.239  17.756  1.00 38.87 ? 126 TYR B N   1 
ATOM   3113 C  CA  . TYR B 1 126 ? -20.836 15.110  16.644  1.00 39.41 ? 126 TYR B CA  1 
ATOM   3114 C  C   . TYR B 1 126 ? -21.779 15.185  15.455  1.00 38.16 ? 126 TYR B C   1 
ATOM   3115 O  O   . TYR B 1 126 ? -22.564 14.256  15.219  1.00 40.59 ? 126 TYR B O   1 
ATOM   3116 C  CB  . TYR B 1 126 ? -19.375 14.788  16.244  1.00 36.56 ? 126 TYR B CB  1 
ATOM   3117 C  CG  . TYR B 1 126 ? -18.481 14.718  17.449  1.00 37.99 ? 126 TYR B CG  1 
ATOM   3118 C  CD1 . TYR B 1 126 ? -18.221 15.859  18.214  1.00 41.37 ? 126 TYR B CD1 1 
ATOM   3119 C  CD2 . TYR B 1 126 ? -17.912 13.506  17.863  1.00 36.22 ? 126 TYR B CD2 1 
ATOM   3120 C  CE1 . TYR B 1 126 ? -17.427 15.803  19.342  1.00 40.13 ? 126 TYR B CE1 1 
ATOM   3121 C  CE2 . TYR B 1 126 ? -17.112 13.450  18.984  1.00 38.65 ? 126 TYR B CE2 1 
ATOM   3122 C  CZ  . TYR B 1 126 ? -16.862 14.600  19.716  1.00 42.13 ? 126 TYR B CZ  1 
ATOM   3123 O  OH  . TYR B 1 126 ? -16.052 14.535  20.824  1.00 41.57 ? 126 TYR B OH  1 
ATOM   3124 N  N   . PRO B 1 127 ? -21.765 16.331  14.742  1.00 42.94 ? 127 PRO B N   1 
ATOM   3125 C  CA  . PRO B 1 127 ? -22.651 16.653  13.615  1.00 41.63 ? 127 PRO B CA  1 
ATOM   3126 C  C   . PRO B 1 127 ? -22.293 16.009  12.260  1.00 43.50 ? 127 PRO B C   1 
ATOM   3127 O  O   . PRO B 1 127 ? -23.124 15.953  11.346  1.00 43.41 ? 127 PRO B O   1 
ATOM   3128 C  CB  . PRO B 1 127 ? -22.529 18.190  13.508  1.00 43.09 ? 127 PRO B CB  1 
ATOM   3129 C  CG  . PRO B 1 127 ? -21.205 18.511  14.113  1.00 45.34 ? 127 PRO B CG  1 
ATOM   3130 C  CD  . PRO B 1 127 ? -21.067 17.530  15.247  1.00 41.20 ? 127 PRO B CD  1 
ATOM   3131 N  N   . ASP B 1 128 ? -21.062 15.530  12.146  1.00 41.32 ? 128 ASP B N   1 
ATOM   3132 C  CA  . ASP B 1 128 ? -20.514 15.008  10.908  1.00 38.23 ? 128 ASP B CA  1 
ATOM   3133 C  C   . ASP B 1 128 ? -19.109 14.486  11.244  1.00 35.24 ? 128 ASP B C   1 
ATOM   3134 O  O   . ASP B 1 128 ? -18.593 14.721  12.353  1.00 33.09 ? 128 ASP B O   1 
ATOM   3135 C  CB  . ASP B 1 128 ? -20.422 16.133  9.868   1.00 39.89 ? 128 ASP B CB  1 
ATOM   3136 C  CG  . ASP B 1 128 ? -19.658 17.327  10.389  1.00 38.33 ? 128 ASP B CG  1 
ATOM   3137 O  OD1 . ASP B 1 128 ? -20.126 17.954  11.358  1.00 45.39 ? 128 ASP B OD1 1 
ATOM   3138 O  OD2 . ASP B 1 128 ? -18.589 17.646  9.853   1.00 37.66 ? 128 ASP B OD2 1 
ATOM   3139 N  N   . ALA B 1 129 ? -18.519 13.783  10.283  1.00 33.96 ? 129 ALA B N   1 
ATOM   3140 C  CA  . ALA B 1 129 ? -17.199 13.209  10.411  1.00 32.90 ? 129 ALA B CA  1 
ATOM   3141 C  C   . ALA B 1 129 ? -16.057 14.229  10.442  1.00 36.49 ? 129 ALA B C   1 
ATOM   3142 O  O   . ALA B 1 129 ? -15.112 14.063  11.220  1.00 32.84 ? 129 ALA B O   1 
ATOM   3143 C  CB  . ALA B 1 129 ? -16.970 12.204  9.292   1.00 33.85 ? 129 ALA B CB  1 
ATOM   3144 N  N   A SER B 1 130 ? -16.128 15.268  9.607   0.50 35.47 ? 130 SER B N   1 
ATOM   3145 N  N   B SER B 1 130 ? -16.153 15.282  9.623   0.50 34.30 ? 130 SER B N   1 
ATOM   3146 C  CA  A SER B 1 130 ? -15.076 16.300  9.603   0.50 37.22 ? 130 SER B CA  1 
ATOM   3147 C  CA  B SER B 1 130 ? -15.094 16.315  9.569   0.50 35.61 ? 130 SER B CA  1 
ATOM   3148 C  C   A SER B 1 130 ? -14.890 16.837  11.020  0.50 36.62 ? 130 SER B C   1 
ATOM   3149 C  C   B SER B 1 130 ? -15.095 17.268  10.765  0.50 38.03 ? 130 SER B C   1 
ATOM   3150 O  O   A SER B 1 130 ? -13.761 17.044  11.489  0.50 37.37 ? 130 SER B O   1 
ATOM   3151 O  O   B SER B 1 130 ? -14.305 18.214  10.797  0.50 42.00 ? 130 SER B O   1 
ATOM   3152 C  CB  A SER B 1 130 ? -15.426 17.446  8.650   0.50 37.95 ? 130 SER B CB  1 
ATOM   3153 C  CB  B SER B 1 130 ? -15.140 17.118  8.266   0.50 32.71 ? 130 SER B CB  1 
ATOM   3154 O  OG  A SER B 1 130 ? -16.259 17.004  7.595   0.50 37.84 ? 130 SER B OG  1 
ATOM   3155 O  OG  B SER B 1 130 ? -14.066 18.048  8.234   0.50 28.49 ? 130 SER B OG  1 
ATOM   3156 N  N   . THR B 1 131 ? -16.017 17.033  11.697  1.00 37.84 ? 131 THR B N   1 
ATOM   3157 C  CA  . THR B 1 131 ? -16.046 17.625  13.021  1.00 39.63 ? 131 THR B CA  1 
ATOM   3158 C  C   . THR B 1 131 ? -15.532 16.623  14.039  1.00 36.80 ? 131 THR B C   1 
ATOM   3159 O  O   . THR B 1 131 ? -14.830 17.027  14.959  1.00 38.55 ? 131 THR B O   1 
ATOM   3160 C  CB  . THR B 1 131 ? -17.500 17.971  13.416  1.00 42.60 ? 131 THR B CB  1 
ATOM   3161 O  OG1 . THR B 1 131 ? -17.953 19.023  12.577  1.00 45.23 ? 131 THR B OG1 1 
ATOM   3162 C  CG2 . THR B 1 131 ? -17.652 18.399  14.910  1.00 44.31 ? 131 THR B CG2 1 
ATOM   3163 N  N   . ALA B 1 132 ? -15.899 15.333  13.877  1.00 35.13 ? 132 ALA B N   1 
ATOM   3164 C  CA  . ALA B 1 132 ? -15.551 14.312  14.865  1.00 30.45 ? 132 ALA B CA  1 
ATOM   3165 C  C   . ALA B 1 132 ? -14.068 13.978  14.769  1.00 28.31 ? 132 ALA B C   1 
ATOM   3166 O  O   . ALA B 1 132 ? -13.473 13.437  15.724  1.00 24.65 ? 132 ALA B O   1 
ATOM   3167 C  CB  . ALA B 1 132 ? -16.418 13.085  14.739  1.00 27.93 ? 132 ALA B CB  1 
ATOM   3168 N  N   . SER B 1 133 ? -13.474 14.348  13.639  1.00 26.54 ? 133 SER B N   1 
ATOM   3169 C  CA  . SER B 1 133 ? -12.150 13.811  13.270  1.00 28.83 ? 133 SER B CA  1 
ATOM   3170 C  C   . SER B 1 133 ? -10.944 14.296  14.082  1.00 30.87 ? 133 SER B C   1 
ATOM   3171 O  O   . SER B 1 133 ? -9.860  13.628  14.095  1.00 25.77 ? 133 SER B O   1 
ATOM   3172 C  CB  . SER B 1 133 ? -11.917 14.020  11.782  1.00 29.17 ? 133 SER B CB  1 
ATOM   3173 O  OG  . SER B 1 133 ? -11.690 15.377  11.520  1.00 34.43 ? 133 SER B OG  1 
ATOM   3174 N  N   . ASN B 1 134 ? -11.089 15.462  14.705  1.00 36.01 ? 134 ASN B N   1 
ATOM   3175 C  CA  . ASN B 1 134 ? -10.064 15.920  15.626  1.00 35.28 ? 134 ASN B CA  1 
ATOM   3176 C  C   . ASN B 1 134 ? -10.485 15.835  17.082  1.00 36.28 ? 134 ASN B C   1 
ATOM   3177 O  O   . ASN B 1 134 ? -9.908  16.467  17.949  1.00 43.31 ? 134 ASN B O   1 
ATOM   3178 C  CB  . ASN B 1 134 ? -9.358  17.254  15.210  1.00 43.01 ? 134 ASN B CB  1 
ATOM   3179 C  CG  . ASN B 1 134 ? -10.306 18.318  14.629  1.00 43.77 ? 134 ASN B CG  1 
ATOM   3180 O  OD1 . ASN B 1 134 ? -11.531 18.156  14.543  1.00 48.65 ? 134 ASN B OD1 1 
ATOM   3181 N  ND2 . ASN B 1 134 ? -9.715  19.442  14.247  1.00 44.81 ? 134 ASN B ND2 1 
ATOM   3182 N  N   . LYS B 1 135 ? -11.431 14.961  17.369  1.00 34.06 ? 135 LYS B N   1 
ATOM   3183 C  CA  . LYS B 1 135 ? -11.930 14.876  18.742  1.00 38.86 ? 135 LYS B CA  1 
ATOM   3184 C  C   . LYS B 1 135 ? -11.737 13.539  19.365  1.00 41.23 ? 135 LYS B C   1 
ATOM   3185 O  O   . LYS B 1 135 ? -11.794 12.479  18.693  1.00 34.63 ? 135 LYS B O   1 
ATOM   3186 C  CB  . LYS B 1 135 ? -13.386 15.366  18.877  1.00 45.62 ? 135 LYS B CB  1 
ATOM   3187 C  CG  . LYS B 1 135 ? -13.523 16.827  18.430  1.00 52.56 ? 135 LYS B CG  1 
ATOM   3188 C  CD  . LYS B 1 135 ? -14.645 17.607  19.126  1.00 53.96 ? 135 LYS B CD  1 
ATOM   3189 C  CE  . LYS B 1 135 ? -14.475 19.122  18.967  1.00 58.09 ? 135 LYS B CE  1 
ATOM   3190 N  NZ  . LYS B 1 135 ? -13.849 19.548  17.666  1.00 52.11 ? 135 LYS B NZ  1 
ATOM   3191 N  N   . SER B 1 136 ? -11.469 13.587  20.660  1.00 39.45 ? 136 SER B N   1 
ATOM   3192 C  CA  . SER B 1 136 ? -11.264 12.389  21.406  1.00 42.13 ? 136 SER B CA  1 
ATOM   3193 C  C   . SER B 1 136 ? -12.488 11.546  21.161  1.00 41.00 ? 136 SER B C   1 
ATOM   3194 O  O   . SER B 1 136 ? -13.637 12.044  21.206  1.00 43.17 ? 136 SER B O   1 
ATOM   3195 C  CB  . SER B 1 136 ? -11.097 12.704  22.917  1.00 50.96 ? 136 SER B CB  1 
ATOM   3196 O  OG  . SER B 1 136 ? -11.061 11.518  23.725  1.00 53.74 ? 136 SER B OG  1 
ATOM   3197 N  N   . GLU B 1 137 ? -12.235 10.288  20.856  1.00 35.57 ? 137 GLU B N   1 
ATOM   3198 C  CA  . GLU B 1 137 ? -13.298 9.287   20.675  1.00 41.47 ? 137 GLU B CA  1 
ATOM   3199 C  C   . GLU B 1 137 ? -14.045 9.474   19.353  1.00 35.41 ? 137 GLU B C   1 
ATOM   3200 O  O   . GLU B 1 137 ? -15.048 8.808   19.121  1.00 34.83 ? 137 GLU B O   1 
ATOM   3201 C  CB  . GLU B 1 137 ? -14.330 9.327   21.831  1.00 45.93 ? 137 GLU B CB  1 
ATOM   3202 C  CG  . GLU B 1 137 ? -13.750 9.618   23.220  1.00 58.50 ? 137 GLU B CG  1 
ATOM   3203 C  CD  . GLU B 1 137 ? -13.416 8.378   24.029  1.00 68.26 ? 137 GLU B CD  1 
ATOM   3204 O  OE1 . GLU B 1 137 ? -14.137 8.124   25.021  1.00 75.50 ? 137 GLU B OE1 1 
ATOM   3205 O  OE2 . GLU B 1 137 ? -12.442 7.665   23.683  1.00 73.66 ? 137 GLU B OE2 1 
ATOM   3206 N  N   . GLY B 1 138 ? -13.536 10.322  18.473  1.00 25.81 ? 138 GLY B N   1 
ATOM   3207 C  CA  . GLY B 1 138 ? -14.362 10.780  17.366  1.00 23.19 ? 138 GLY B CA  1 
ATOM   3208 C  C   . GLY B 1 138 ? -14.708 9.786   16.264  1.00 19.11 ? 138 GLY B C   1 
ATOM   3209 O  O   . GLY B 1 138 ? -15.755 9.863   15.661  1.00 18.22 ? 138 GLY B O   1 
ATOM   3210 N  N   . LEU B 1 139 ? -13.742 8.927   15.900  1.00 16.42 ? 139 LEU B N   1 
ATOM   3211 C  CA  . LEU B 1 139 ? -13.910 8.069   14.729  1.00 14.66 ? 139 LEU B CA  1 
ATOM   3212 C  C   . LEU B 1 139 ? -13.775 6.574   15.132  1.00 12.13 ? 139 LEU B C   1 
ATOM   3213 O  O   . LEU B 1 139 ? -13.011 6.279   16.084  1.00 14.25 ? 139 LEU B O   1 
ATOM   3214 C  CB  . LEU B 1 139 ? -12.856 8.423   13.653  1.00 15.99 ? 139 LEU B CB  1 
ATOM   3215 C  CG  . LEU B 1 139 ? -12.877 9.873   13.133  1.00 16.46 ? 139 LEU B CG  1 
ATOM   3216 C  CD1 . LEU B 1 139 ? -11.655 10.090  12.248  1.00 16.04 ? 139 LEU B CD1 1 
ATOM   3217 C  CD2 . LEU B 1 139 ? -14.175 10.069  12.354  1.00 16.66 ? 139 LEU B CD2 1 
ATOM   3218 N  N   . ALA B 1 140 ? -14.432 5.712   14.420  1.00 11.12 ? 140 ALA B N   1 
ATOM   3219 C  CA  . ALA B 1 140 ? -14.277 4.242   14.582  1.00 11.02 ? 140 ALA B CA  1 
ATOM   3220 C  C   . ALA B 1 140 ? -14.184 3.797   13.168  1.00 11.85 ? 140 ALA B C   1 
ATOM   3221 O  O   . ALA B 1 140 ? -15.112 4.014   12.335  1.00 12.18 ? 140 ALA B O   1 
ATOM   3222 C  CB  . ALA B 1 140 ? -15.489 3.639   15.232  1.00 11.97 ? 140 ALA B CB  1 
ATOM   3223 N  N   . VAL B 1 141 ? -13.081 3.070   12.874  1.00 9.88  ? 141 VAL B N   1 
ATOM   3224 C  CA  . VAL B 1 141 ? -12.969 2.487   11.543  1.00 9.23  ? 141 VAL B CA  1 
ATOM   3225 C  C   . VAL B 1 141 ? -12.956 0.993   11.625  1.00 10.31 ? 141 VAL B C   1 
ATOM   3226 O  O   . VAL B 1 141 ? -12.275 0.438   12.512  1.00 11.55 ? 141 VAL B O   1 
ATOM   3227 C  CB  . VAL B 1 141 ? -11.671 3.052   10.844  1.00 8.63  ? 141 VAL B CB  1 
ATOM   3228 C  CG1 . VAL B 1 141 ? -11.517 2.428   9.431   1.00 9.21  ? 141 VAL B CG1 1 
ATOM   3229 C  CG2 . VAL B 1 141 ? -11.682 4.583   10.716  1.00 10.48 ? 141 VAL B CG2 1 
ATOM   3230 N  N   . LEU B 1 142 ? -13.690 0.331   10.772  1.00 9.17  ? 142 LEU B N   1 
ATOM   3231 C  CA  . LEU B 1 142 ? -13.718 -1.145  10.676  1.00 9.92  ? 142 LEU B CA  1 
ATOM   3232 C  C   . LEU B 1 142 ? -12.755 -1.503  9.530   1.00 11.30 ? 142 LEU B C   1 
ATOM   3233 O  O   . LEU B 1 142 ? -12.904 -0.925  8.500   1.00 11.25 ? 142 LEU B O   1 
ATOM   3234 C  CB  . LEU B 1 142 ? -15.081 -1.734  10.376  1.00 11.02 ? 142 LEU B CB  1 
ATOM   3235 C  CG  . LEU B 1 142 ? -16.276 -1.425  11.301  1.00 12.04 ? 142 LEU B CG  1 
ATOM   3236 C  CD1 . LEU B 1 142 ? -17.488 -2.093  10.716  1.00 12.63 ? 142 LEU B CD1 1 
ATOM   3237 C  CD2 . LEU B 1 142 ? -16.044 -1.890  12.773  1.00 13.95 ? 142 LEU B CD2 1 
ATOM   3238 N  N   . ALA B 1 143 ? -11.810 -2.432  9.733   1.00 9.85  ? 143 ALA B N   1 
ATOM   3239 C  CA  . ALA B 1 143 ? -10.903 -2.835  8.674   1.00 8.54  ? 143 ALA B CA  1 
ATOM   3240 C  C   . ALA B 1 143 ? -11.105 -4.300  8.371   1.00 8.72  ? 143 ALA B C   1 
ATOM   3241 O  O   . ALA B 1 143 ? -11.212 -5.138  9.254   1.00 9.96  ? 143 ALA B O   1 
ATOM   3242 C  CB  . ALA B 1 143 ? -9.492  -2.585  9.179   1.00 9.24  ? 143 ALA B CB  1 
ATOM   3243 N  N   . VAL B 1 144 ? -11.220 -4.587  7.078   1.00 7.42  ? 144 VAL B N   1 
ATOM   3244 C  CA  . VAL B 1 144 ? -11.299 -5.941  6.553   1.00 7.92  ? 144 VAL B CA  1 
ATOM   3245 C  C   . VAL B 1 144 ? -10.072 -6.173  5.725   1.00 9.21  ? 144 VAL B C   1 
ATOM   3246 O  O   . VAL B 1 144 ? -9.766  -5.432  4.755   1.00 9.77  ? 144 VAL B O   1 
ATOM   3247 C  CB  . VAL B 1 144 ? -12.550 -6.172  5.663   1.00 7.45  ? 144 VAL B CB  1 
ATOM   3248 C  CG1 . VAL B 1 144 ? -12.676 -7.637  5.142   1.00 8.34  ? 144 VAL B CG1 1 
ATOM   3249 C  CG2 . VAL B 1 144 ? -13.805 -5.769  6.457   1.00 8.90  ? 144 VAL B CG2 1 
ATOM   3250 N  N   . LEU B 1 145 ? -9.360  -7.231  6.103   1.00 9.97  ? 145 LEU B N   1 
ATOM   3251 C  CA  . LEU B 1 145 ? -8.186  -7.702  5.376   1.00 10.36 ? 145 LEU B CA  1 
ATOM   3252 C  C   . LEU B 1 145 ? -8.642  -8.513  4.221   1.00 10.04 ? 145 LEU B C   1 
ATOM   3253 O  O   . LEU B 1 145 ? -9.608  -9.296  4.295   1.00 9.62  ? 145 LEU B O   1 
ATOM   3254 C  CB  . LEU B 1 145 ? -7.287  -8.547  6.316   1.00 11.23 ? 145 LEU B CB  1 
ATOM   3255 C  CG  . LEU B 1 145 ? -6.789  -7.798  7.541   1.00 11.92 ? 145 LEU B CG  1 
ATOM   3256 C  CD1 . LEU B 1 145 ? -6.178  -8.769  8.582   1.00 14.07 ? 145 LEU B CD1 1 
ATOM   3257 C  CD2 . LEU B 1 145 ? -5.703  -6.788  7.164   1.00 13.74 ? 145 LEU B CD2 1 
ATOM   3258 N  N   . ILE B 1 146 ? -8.016  -8.274  3.063   1.00 9.45  ? 146 ILE B N   1 
ATOM   3259 C  CA  . ILE B 1 146 ? -8.466  -8.853  1.786   1.00 9.20  ? 146 ILE B CA  1 
ATOM   3260 C  C   . ILE B 1 146 ? -7.348  -9.746  1.210   1.00 9.47  ? 146 ILE B C   1 
ATOM   3261 O  O   . ILE B 1 146 ? -6.205  -9.250  1.044   1.00 10.42 ? 146 ILE B O   1 
ATOM   3262 C  CB  . ILE B 1 146 ? -8.824  -7.760  0.768   1.00 8.80  ? 146 ILE B CB  1 
ATOM   3263 C  CG1 . ILE B 1 146 ? -10.097 -6.988  1.243   1.00 9.17  ? 146 ILE B CG1 1 
ATOM   3264 C  CG2 . ILE B 1 146 ? -9.196  -8.416  -0.569  1.00 9.91  ? 146 ILE B CG2 1 
ATOM   3265 C  CD1 . ILE B 1 146 ? -10.320 -5.709  0.439   1.00 8.90  ? 146 ILE B CD1 1 
ATOM   3266 N  N   . GLU B 1 147 ? -7.622  -11.025 0.937   1.00 10.25 ? 147 GLU B N   1 
ATOM   3267 C  CA  . GLU B 1 147 ? -6.599  -11.877 0.339   1.00 11.18 ? 147 GLU B CA  1 
ATOM   3268 C  C   . GLU B 1 147 ? -7.046  -12.256 -1.087  1.00 11.71 ? 147 GLU B C   1 
ATOM   3269 O  O   . GLU B 1 147 ? -8.230  -12.215 -1.439  1.00 10.94 ? 147 GLU B O   1 
ATOM   3270 C  CB  . GLU B 1 147 ? -6.360  -13.149 1.186   1.00 15.63 ? 147 GLU B CB  1 
ATOM   3271 C  CG  . GLU B 1 147 ? -7.460  -14.139 1.279   1.00 21.02 ? 147 GLU B CG  1 
ATOM   3272 C  CD  . GLU B 1 147 ? -7.148  -15.290 2.330   1.00 24.68 ? 147 GLU B CD  1 
ATOM   3273 O  OE1 . GLU B 1 147 ? -6.045  -15.224 2.997   1.00 23.03 ? 147 GLU B OE1 1 
ATOM   3274 O  OE2 . GLU B 1 147 ? -8.024  -16.245 2.481   1.00 28.48 ? 147 GLU B OE2 1 
ATOM   3275 N  N   . MET B 1 148 ? -6.080  -12.622 -1.921  1.00 9.59  ? 148 MET B N   1 
ATOM   3276 C  CA  . MET B 1 148 ? -6.354  -13.138 -3.245  1.00 9.32  ? 148 MET B CA  1 
ATOM   3277 C  C   . MET B 1 148 ? -6.915  -14.558 -3.120  1.00 9.69  ? 148 MET B C   1 
ATOM   3278 O  O   . MET B 1 148 ? -6.329  -15.423 -2.467  1.00 11.66 ? 148 MET B O   1 
ATOM   3279 C  CB  . MET B 1 148 ? -5.052  -13.182 -4.078  1.00 8.84  ? 148 MET B CB  1 
ATOM   3280 C  CG  . MET B 1 148 ? -5.334  -13.500 -5.541  1.00 9.91  ? 148 MET B CG  1 
ATOM   3281 S  SD  . MET B 1 148 ? -3.782  -13.622 -6.466  1.00 13.46 ? 148 MET B SD  1 
ATOM   3282 C  CE  . MET B 1 148 ? -3.306  -11.875 -6.456  1.00 11.74 ? 148 MET B CE  1 
ATOM   3283 N  N   . GLY B 1 149 ? -8.086  -14.708 -3.721  1.00 8.95  ? 149 GLY B N   1 
ATOM   3284 C  CA  . GLY B 1 149 ? -8.760  -16.030 -3.611  1.00 9.33  ? 149 GLY B CA  1 
ATOM   3285 C  C   . GLY B 1 149 ? -9.904  -16.063 -4.610  1.00 9.08  ? 149 GLY B C   1 
ATOM   3286 O  O   . GLY B 1 149 ? -9.737  -15.788 -5.848  1.00 9.56  ? 149 GLY B O   1 
ATOM   3287 N  N   . SER B 1 150 ? -11.063 -16.491 -4.105  1.00 9.59  ? 150 SER B N   1 
ATOM   3288 C  CA  . SER B 1 150 ? -12.267 -16.574 -5.022  1.00 10.43 ? 150 SER B CA  1 
ATOM   3289 C  C   . SER B 1 150 ? -12.843 -15.228 -5.411  1.00 10.76 ? 150 SER B C   1 
ATOM   3290 O  O   . SER B 1 150 ? -12.765 -14.263 -4.617  1.00 10.65 ? 150 SER B O   1 
ATOM   3291 C  CB  . SER B 1 150 ? -13.388 -17.340 -4.289  1.00 10.08 ? 150 SER B CB  1 
ATOM   3292 O  OG  . SER B 1 150 ? -13.018 -18.714 -4.195  1.00 11.43 ? 150 SER B OG  1 
ATOM   3293 N  N   . PHE B 1 151 ? -13.406 -15.216 -6.620  1.00 11.87 ? 151 PHE B N   1 
ATOM   3294 C  CA  . PHE B 1 151 ? -14.188 -14.045 -7.019  1.00 10.98 ? 151 PHE B CA  1 
ATOM   3295 C  C   . PHE B 1 151 ? -15.256 -13.719 -5.994  1.00 11.10 ? 151 PHE B C   1 
ATOM   3296 O  O   . PHE B 1 151 ? -15.939 -14.623 -5.452  1.00 12.30 ? 151 PHE B O   1 
ATOM   3297 C  CB  . PHE B 1 151 ? -14.886 -14.348 -8.356  1.00 10.87 ? 151 PHE B CB  1 
ATOM   3298 C  CG  . PHE B 1 151 ? -15.733 -13.203 -8.855  1.00 10.59 ? 151 PHE B CG  1 
ATOM   3299 C  CD1 . PHE B 1 151 ? -15.139 -12.172 -9.540  1.00 11.72 ? 151 PHE B CD1 1 
ATOM   3300 C  CD2 . PHE B 1 151 ? -17.102 -13.222 -8.681  1.00 11.89 ? 151 PHE B CD2 1 
ATOM   3301 C  CE1 . PHE B 1 151 ? -15.916 -11.092 -9.968  1.00 10.73 ? 151 PHE B CE1 1 
ATOM   3302 C  CE2 . PHE B 1 151 ? -17.939 -12.132 -9.147  1.00 12.69 ? 151 PHE B CE2 1 
ATOM   3303 C  CZ  . PHE B 1 151 ? -17.319 -11.083 -9.796  1.00 11.57 ? 151 PHE B CZ  1 
ATOM   3304 N  N   . ASN B 1 152 ? -15.452 -12.428 -5.703  1.00 9.67  ? 152 ASN B N   1 
ATOM   3305 C  CA  . ASN B 1 152 ? -16.356 -11.995 -4.683  1.00 9.82  ? 152 ASN B CA  1 
ATOM   3306 C  C   . ASN B 1 152 ? -17.409 -11.121 -5.312  1.00 10.91 ? 152 ASN B C   1 
ATOM   3307 O  O   . ASN B 1 152 ? -17.173 -9.891  -5.627  1.00 9.53  ? 152 ASN B O   1 
ATOM   3308 C  CB  . ASN B 1 152 ? -15.568 -11.152 -3.631  1.00 10.55 ? 152 ASN B CB  1 
ATOM   3309 C  CG  . ASN B 1 152 ? -16.375 -10.902 -2.397  1.00 10.70 ? 152 ASN B CG  1 
ATOM   3310 O  OD1 . ASN B 1 152 ? -17.519 -10.461 -2.468  1.00 10.87 ? 152 ASN B OD1 1 
ATOM   3311 N  ND2 . ASN B 1 152 ? -15.786 -11.179 -1.203  1.00 9.61  ? 152 ASN B ND2 1 
ATOM   3312 N  N   . PRO B 1 153 ? -18.613 -11.656 -5.510  1.00 11.02 ? 153 PRO B N   1 
ATOM   3313 C  CA  . PRO B 1 153 ? -19.689 -10.837 -6.118  1.00 11.29 ? 153 PRO B CA  1 
ATOM   3314 C  C   . PRO B 1 153 ? -20.034 -9.587  -5.330  1.00 13.25 ? 153 PRO B C   1 
ATOM   3315 O  O   . PRO B 1 153 ? -20.405 -8.554  -5.988  1.00 14.20 ? 153 PRO B O   1 
ATOM   3316 C  CB  . PRO B 1 153 ? -20.874 -11.810 -6.207  1.00 13.53 ? 153 PRO B CB  1 
ATOM   3317 C  CG  . PRO B 1 153 ? -20.264 -13.182 -6.080  1.00 15.76 ? 153 PRO B CG  1 
ATOM   3318 C  CD  . PRO B 1 153 ? -19.015 -13.073 -5.248  1.00 12.49 ? 153 PRO B CD  1 
ATOM   3319 N  N   . SER B 1 154 ? -19.940 -9.566  -3.996  1.00 11.30 ? 154 SER B N   1 
ATOM   3320 C  CA  . SER B 1 154 ? -20.305 -8.368  -3.249  1.00 12.05 ? 154 SER B CA  1 
ATOM   3321 C  C   . SER B 1 154 ? -19.305 -7.250  -3.488  1.00 11.72 ? 154 SER B C   1 
ATOM   3322 O  O   . SER B 1 154 ? -19.688 -6.094  -3.675  1.00 11.06 ? 154 SER B O   1 
ATOM   3323 C  CB  . SER B 1 154 ? -20.498 -8.622  -1.737  1.00 15.17 ? 154 SER B CB  1 
ATOM   3324 O  OG  . SER B 1 154 ? -21.385 -9.732  -1.554  1.00 20.63 ? 154 SER B OG  1 
ATOM   3325 N  N   . TYR B 1 155 ? -18.009 -7.575  -3.434  1.00 10.27 ? 155 TYR B N   1 
ATOM   3326 C  CA  . TYR B 1 155 ? -17.022 -6.536  -3.702  1.00 9.61  ? 155 TYR B CA  1 
ATOM   3327 C  C   . TYR B 1 155 ? -17.144 -6.063  -5.157  1.00 9.21  ? 155 TYR B C   1 
ATOM   3328 O  O   . TYR B 1 155 ? -16.798 -4.885  -5.424  1.00 9.65  ? 155 TYR B O   1 
ATOM   3329 C  CB  . TYR B 1 155 ? -15.570 -7.047  -3.415  1.00 9.26  ? 155 TYR B CB  1 
ATOM   3330 C  CG  . TYR B 1 155 ? -15.199 -6.945  -1.988  1.00 9.76  ? 155 TYR B CG  1 
ATOM   3331 C  CD1 . TYR B 1 155 ? -14.468 -5.832  -1.511  1.00 9.13  ? 155 TYR B CD1 1 
ATOM   3332 C  CD2 . TYR B 1 155 ? -15.671 -7.858  -1.069  1.00 8.78  ? 155 TYR B CD2 1 
ATOM   3333 C  CE1 . TYR B 1 155 ? -14.125 -5.736  -0.142  1.00 9.59  ? 155 TYR B CE1 1 
ATOM   3334 C  CE2 . TYR B 1 155 ? -15.393 -7.721  0.289   1.00 9.54  ? 155 TYR B CE2 1 
ATOM   3335 C  CZ  . TYR B 1 155 ? -14.625 -6.660  0.749   1.00 9.46  ? 155 TYR B CZ  1 
ATOM   3336 O  OH  . TYR B 1 155 ? -14.305 -6.461  2.087   1.00 9.42  ? 155 TYR B OH  1 
ATOM   3337 N  N   . ASP B 1 156 ? -17.607 -6.898  -6.064  1.00 9.33  ? 156 ASP B N   1 
ATOM   3338 C  CA  . ASP B 1 156 ? -17.732 -6.505  -7.462  1.00 9.75  ? 156 ASP B CA  1 
ATOM   3339 C  C   . ASP B 1 156 ? -18.806 -5.436  -7.650  1.00 10.78 ? 156 ASP B C   1 
ATOM   3340 O  O   . ASP B 1 156 ? -18.808 -4.759  -8.691  1.00 11.71 ? 156 ASP B O   1 
ATOM   3341 C  CB  . ASP B 1 156 ? -17.907 -7.697  -8.434  1.00 10.83 ? 156 ASP B CB  1 
ATOM   3342 C  CG  . ASP B 1 156 ? -16.984 -7.538  -9.627  1.00 11.51 ? 156 ASP B CG  1 
ATOM   3343 O  OD1 . ASP B 1 156 ? -15.734 -7.281  -9.417  1.00 10.98 ? 156 ASP B OD1 1 
ATOM   3344 O  OD2 . ASP B 1 156 ? -17.568 -7.611  -10.757 1.00 16.03 ? 156 ASP B OD2 1 
ATOM   3345 N  N   . LYS B 1 157 ? -19.740 -5.355  -6.686  1.00 10.40 ? 157 LYS B N   1 
ATOM   3346 C  CA  . LYS B 1 157 ? -20.795 -4.289  -6.748  1.00 11.46 ? 157 LYS B CA  1 
ATOM   3347 C  C   . LYS B 1 157 ? -20.067 -2.950  -6.685  1.00 11.64 ? 157 LYS B C   1 
ATOM   3348 O  O   . LYS B 1 157 ? -20.597 -1.980  -7.229  1.00 13.04 ? 157 LYS B O   1 
ATOM   3349 C  CB  . LYS B 1 157 ? -21.830 -4.418  -5.636  1.00 11.41 ? 157 LYS B CB  1 
ATOM   3350 C  CG  . LYS B 1 157 ? -22.668 -5.716  -5.840  1.00 13.09 ? 157 LYS B CG  1 
ATOM   3351 C  CD  . LYS B 1 157 ? -23.482 -6.094  -4.587  1.00 17.48 ? 157 LYS B CD  1 
ATOM   3352 C  CE  . LYS B 1 157 ? -24.360 -7.320  -4.919  1.00 18.15 ? 157 LYS B CE  1 
ATOM   3353 N  NZ  . LYS B 1 157 ? -25.023 -7.955  -3.723  1.00 21.68 ? 157 LYS B NZ  1 
ATOM   3354 N  N   . ILE B 1 158 ? -18.867 -2.870  -6.076  1.00 10.07 ? 158 ILE B N   1 
ATOM   3355 C  CA  . ILE B 1 158 ? -18.095 -1.582  -6.109  1.00 10.67 ? 158 ILE B CA  1 
ATOM   3356 C  C   . ILE B 1 158 ? -17.190 -1.661  -7.328  1.00 11.46 ? 158 ILE B C   1 
ATOM   3357 O  O   . ILE B 1 158 ? -17.107 -0.653  -8.104  1.00 12.21 ? 158 ILE B O   1 
ATOM   3358 C  CB  . ILE B 1 158 ? -17.240 -1.422  -4.794  1.00 11.15 ? 158 ILE B CB  1 
ATOM   3359 C  CG1 . ILE B 1 158 ? -18.234 -1.297  -3.650  1.00 11.72 ? 158 ILE B CG1 1 
ATOM   3360 C  CG2 . ILE B 1 158 ? -16.260 -0.203  -4.893  1.00 12.29 ? 158 ILE B CG2 1 
ATOM   3361 C  CD1 . ILE B 1 158 ? -17.610 -1.311  -2.239  1.00 15.24 ? 158 ILE B CD1 1 
ATOM   3362 N  N   . PHE B 1 159 ? -16.490 -2.788  -7.570  1.00 11.14 ? 159 PHE B N   1 
ATOM   3363 C  CA  . PHE B 1 159 ? -15.387 -2.735  -8.549  1.00 12.75 ? 159 PHE B CA  1 
ATOM   3364 C  C   . PHE B 1 159 ? -15.867 -2.564  -9.961  1.00 13.08 ? 159 PHE B C   1 
ATOM   3365 O  O   . PHE B 1 159 ? -15.162 -2.050  -10.892 1.00 16.04 ? 159 PHE B O   1 
ATOM   3366 C  CB  . PHE B 1 159 ? -14.516 -4.002  -8.503  1.00 10.75 ? 159 PHE B CB  1 
ATOM   3367 C  CG  . PHE B 1 159 ? -13.850 -4.242  -7.185  1.00 12.46 ? 159 PHE B CG  1 
ATOM   3368 C  CD1 . PHE B 1 159 ? -13.441 -3.157  -6.383  1.00 12.71 ? 159 PHE B CD1 1 
ATOM   3369 C  CD2 . PHE B 1 159 ? -13.511 -5.524  -6.817  1.00 12.90 ? 159 PHE B CD2 1 
ATOM   3370 C  CE1 . PHE B 1 159 ? -12.769 -3.404  -5.191  1.00 13.90 ? 159 PHE B CE1 1 
ATOM   3371 C  CE2 . PHE B 1 159 ? -12.810 -5.766  -5.626  1.00 14.10 ? 159 PHE B CE2 1 
ATOM   3372 C  CZ  . PHE B 1 159 ? -12.438 -4.706  -4.825  1.00 14.98 ? 159 PHE B CZ  1 
ATOM   3373 N  N   . SER B 1 160 ? -17.089 -2.958  -10.161 1.00 12.71 ? 160 SER B N   1 
ATOM   3374 C  CA  . SER B 1 160 ? -17.729 -2.805  -11.513 1.00 13.46 ? 160 SER B CA  1 
ATOM   3375 C  C   . SER B 1 160 ? -17.925 -1.372  -11.907 1.00 15.20 ? 160 SER B C   1 
ATOM   3376 O  O   . SER B 1 160 ? -18.202 -1.116  -13.078 1.00 18.18 ? 160 SER B O   1 
ATOM   3377 C  CB  . SER B 1 160 ? -19.065 -3.666  -11.597 1.00 13.22 ? 160 SER B CB  1 
ATOM   3378 O  OG  . SER B 1 160 ? -20.035 -3.198  -10.778 1.00 15.21 ? 160 SER B OG  1 
ATOM   3379 N  N   . HIS B 1 161 ? -17.785 -0.429  -11.022 1.00 13.00 ? 161 HIS B N   1 
ATOM   3380 C  CA  . HIS B 1 161 ? -17.951 0.989   -11.350 1.00 13.42 ? 161 HIS B CA  1 
ATOM   3381 C  C   . HIS B 1 161 ? -16.648 1.766   -11.420 1.00 17.05 ? 161 HIS B C   1 
ATOM   3382 O  O   . HIS B 1 161 ? -16.691 2.962   -11.739 1.00 16.89 ? 161 HIS B O   1 
ATOM   3383 C  CB  . HIS B 1 161 ? -18.885 1.680   -10.359 1.00 14.13 ? 161 HIS B CB  1 
ATOM   3384 C  CG  . HIS B 1 161 ? -20.285 1.121   -10.377 1.00 14.04 ? 161 HIS B CG  1 
ATOM   3385 N  ND1 . HIS B 1 161 ? -21.256 1.628   -11.155 1.00 15.89 ? 161 HIS B ND1 1 
ATOM   3386 C  CD2 . HIS B 1 161 ? -20.845 0.039   -9.702  1.00 16.75 ? 161 HIS B CD2 1 
ATOM   3387 C  CE1 . HIS B 1 161 ? -22.387 0.921   -10.977 1.00 15.50 ? 161 HIS B CE1 1 
ATOM   3388 N  NE2 . HIS B 1 161 ? -22.134 -0.052  -10.087 1.00 15.57 ? 161 HIS B NE2 1 
ATOM   3389 N  N   . LEU B 1 162 ? -15.533 1.115   -11.143 1.00 19.70 ? 162 LEU B N   1 
ATOM   3390 C  CA  . LEU B 1 162 ? -14.216 1.824   -11.193 1.00 19.83 ? 162 LEU B CA  1 
ATOM   3391 C  C   . LEU B 1 162 ? -13.925 2.530   -12.513 1.00 22.01 ? 162 LEU B C   1 
ATOM   3392 O  O   . LEU B 1 162 ? -13.329 3.612   -12.473 1.00 18.60 ? 162 LEU B O   1 
ATOM   3393 C  CB  . LEU B 1 162 ? -13.101 0.807   -11.018 1.00 22.56 ? 162 LEU B CB  1 
ATOM   3394 C  CG  . LEU B 1 162 ? -13.159 0.159   -9.629  1.00 22.90 ? 162 LEU B CG  1 
ATOM   3395 C  CD1 . LEU B 1 162 ? -12.119 -0.947  -9.613  1.00 22.20 ? 162 LEU B CD1 1 
ATOM   3396 C  CD2 . LEU B 1 162 ? -12.918 1.254   -8.596  1.00 24.60 ? 162 LEU B CD2 1 
ATOM   3397 N  N   . GLN B 1 163 ? -14.255 1.925   -13.660 1.00 20.98 ? 163 GLN B N   1 
ATOM   3398 C  CA  . GLN B 1 163 ? -13.988 2.603   -14.975 1.00 20.68 ? 163 GLN B CA  1 
ATOM   3399 C  C   . GLN B 1 163 ? -14.755 3.934   -15.145 1.00 21.63 ? 163 GLN B C   1 
ATOM   3400 O  O   . GLN B 1 163 ? -14.582 4.609   -16.165 1.00 22.95 ? 163 GLN B O   1 
ATOM   3401 C  CB  . GLN B 1 163 ? -14.432 1.678   -16.086 1.00 25.62 ? 163 GLN B CB  1 
ATOM   3402 C  CG  . GLN B 1 163 ? -15.845 1.175   -15.831 1.00 27.71 ? 163 GLN B CG  1 
ATOM   3403 C  CD  . GLN B 1 163 ? -15.966 -0.173  -15.037 1.00 32.83 ? 163 GLN B CD  1 
ATOM   3404 O  OE1 . GLN B 1 163 ? -15.223 -0.509  -14.022 1.00 32.80 ? 163 GLN B OE1 1 
ATOM   3405 N  NE2 . GLN B 1 163 ? -16.956 -0.938  -15.478 1.00 37.02 ? 163 GLN B NE2 1 
ATOM   3406 N  N   . HIS B 1 164 ? -15.579 4.325   -14.200 1.00 17.59 ? 164 HIS B N   1 
ATOM   3407 C  CA  . HIS B 1 164 ? -16.310 5.511   -14.291 1.00 16.88 ? 164 HIS B CA  1 
ATOM   3408 C  C   . HIS B 1 164 ? -15.805 6.545   -13.322 1.00 14.24 ? 164 HIS B C   1 
ATOM   3409 O  O   . HIS B 1 164 ? -16.296 7.672   -13.235 1.00 13.28 ? 164 HIS B O   1 
ATOM   3410 C  CB  . HIS B 1 164 ? -17.808 5.145   -14.300 1.00 23.80 ? 164 HIS B CB  1 
ATOM   3411 C  CG  . HIS B 1 164 ? -18.108 3.923   -15.111 1.00 28.33 ? 164 HIS B CG  1 
ATOM   3412 N  ND1 . HIS B 1 164 ? -17.775 3.822   -16.407 1.00 31.88 ? 164 HIS B ND1 1 
ATOM   3413 C  CD2 . HIS B 1 164 ? -18.707 2.715   -14.760 1.00 31.51 ? 164 HIS B CD2 1 
ATOM   3414 C  CE1 . HIS B 1 164 ? -18.151 2.617   -16.870 1.00 34.66 ? 164 HIS B CE1 1 
ATOM   3415 N  NE2 . HIS B 1 164 ? -18.721 1.943   -15.861 1.00 34.69 ? 164 HIS B NE2 1 
ATOM   3416 N  N   . VAL B 1 165 ? -14.770 6.149   -12.558 1.00 12.78 ? 165 VAL B N   1 
ATOM   3417 C  CA  . VAL B 1 165 ? -14.140 7.103   -11.601 1.00 12.12 ? 165 VAL B CA  1 
ATOM   3418 C  C   . VAL B 1 165 ? -12.636 6.982   -11.792 1.00 9.94  ? 165 VAL B C   1 
ATOM   3419 O  O   . VAL B 1 165 ? -11.847 7.065   -10.861 1.00 11.22 ? 165 VAL B O   1 
ATOM   3420 C  CB  . VAL B 1 165 ? -14.569 6.966   -10.108 1.00 12.57 ? 165 VAL B CB  1 
ATOM   3421 C  CG1 . VAL B 1 165 ? -16.051 7.429   -10.022 1.00 13.59 ? 165 VAL B CG1 1 
ATOM   3422 C  CG2 . VAL B 1 165 ? -14.441 5.537   -9.653  1.00 12.59 ? 165 VAL B CG2 1 
ATOM   3423 N  N   A LYS B 1 166 ? -12.183 6.815   -13.035 0.50 9.16  ? 166 LYS B N   1 
ATOM   3424 N  N   B LYS B 1 166 ? -12.258 6.855   -13.049 0.50 9.19  ? 166 LYS B N   1 
ATOM   3425 C  CA  A LYS B 1 166 ? -10.748 6.576   -13.246 0.50 9.33  ? 166 LYS B CA  1 
ATOM   3426 C  CA  B LYS B 1 166 ? -10.892 6.651   -13.388 0.50 9.42  ? 166 LYS B CA  1 
ATOM   3427 C  C   A LYS B 1 166 ? -9.870  7.746   -12.764 0.50 8.98  ? 166 LYS B C   1 
ATOM   3428 C  C   B LYS B 1 166 ? -9.911  7.736   -12.897 0.50 9.23  ? 166 LYS B C   1 
ATOM   3429 O  O   A LYS B 1 166 ? -8.731  7.517   -12.285 0.50 8.29  ? 166 LYS B O   1 
ATOM   3430 O  O   B LYS B 1 166 ? -8.759  7.449   -12.563 0.50 8.84  ? 166 LYS B O   1 
ATOM   3431 C  CB  A LYS B 1 166 ? -10.467 6.321   -14.726 0.50 8.93  ? 166 LYS B CB  1 
ATOM   3432 C  CB  B LYS B 1 166 ? -10.813 6.609   -14.887 0.50 8.72  ? 166 LYS B CB  1 
ATOM   3433 C  CG  A LYS B 1 166 ? -10.989 4.986   -15.226 0.50 9.64  ? 166 LYS B CG  1 
ATOM   3434 C  CG  B LYS B 1 166 ? -9.395  6.285   -15.269 0.50 9.49  ? 166 LYS B CG  1 
ATOM   3435 C  CD  A LYS B 1 166 ? -10.650 4.835   -16.696 0.50 10.64 ? 166 LYS B CD  1 
ATOM   3436 C  CD  B LYS B 1 166 ? -9.317  5.910   -16.754 0.50 10.49 ? 166 LYS B CD  1 
ATOM   3437 C  CE  A LYS B 1 166 ? -9.250  4.340   -16.930 0.50 12.05 ? 166 LYS B CE  1 
ATOM   3438 C  CE  B LYS B 1 166 ? -8.067  5.063   -16.907 0.50 12.50 ? 166 LYS B CE  1 
ATOM   3439 N  NZ  A LYS B 1 166 ? -9.008  2.973   -16.351 0.50 13.59 ? 166 LYS B NZ  1 
ATOM   3440 N  NZ  B LYS B 1 166 ? -7.672  4.968   -18.396 0.50 12.68 ? 166 LYS B NZ  1 
ATOM   3441 N  N   . TYR B 1 167 ? -10.383 8.977   -12.925 1.00 9.33  ? 167 TYR B N   1 
ATOM   3442 C  CA  . TYR B 1 167 ? -9.588  10.125  -12.596 1.00 9.58  ? 167 TYR B CA  1 
ATOM   3443 C  C   . TYR B 1 167 ? -10.022 10.920  -11.385 1.00 7.98  ? 167 TYR B C   1 
ATOM   3444 O  O   . TYR B 1 167 ? -11.224 10.925  -11.014 1.00 8.51  ? 167 TYR B O   1 
ATOM   3445 C  CB  . TYR B 1 167 ? -9.567  11.075  -13.865 1.00 9.63  ? 167 TYR B CB  1 
ATOM   3446 C  CG  . TYR B 1 167 ? -9.113  10.334  -15.096 1.00 10.82 ? 167 TYR B CG  1 
ATOM   3447 C  CD1 . TYR B 1 167 ? -7.758  10.020  -15.279 1.00 11.59 ? 167 TYR B CD1 1 
ATOM   3448 C  CD2 . TYR B 1 167 ? -10.033 9.960   -16.085 1.00 11.90 ? 167 TYR B CD2 1 
ATOM   3449 C  CE1 . TYR B 1 167 ? -7.322  9.254   -16.358 1.00 13.28 ? 167 TYR B CE1 1 
ATOM   3450 C  CE2 . TYR B 1 167 ? -9.586  9.242   -17.218 1.00 13.14 ? 167 TYR B CE2 1 
ATOM   3451 C  CZ  . TYR B 1 167 ? -8.247  8.932   -17.363 1.00 15.93 ? 167 TYR B CZ  1 
ATOM   3452 O  OH  . TYR B 1 167 ? -7.874  8.138   -18.481 1.00 16.85 ? 167 TYR B OH  1 
ATOM   3453 N  N   . LYS B 1 168 ? -9.056  11.666  -10.832 1.00 8.27  ? 168 LYS B N   1 
ATOM   3454 C  CA  . LYS B 1 168 ? -9.399  12.519  -9.673  1.00 9.42  ? 168 LYS B CA  1 
ATOM   3455 C  C   . LYS B 1 168 ? -10.573 13.436  -9.982  1.00 10.18 ? 168 LYS B C   1 
ATOM   3456 O  O   . LYS B 1 168 ? -10.662 14.085  -11.033 1.00 11.06 ? 168 LYS B O   1 
ATOM   3457 C  CB  . LYS B 1 168 ? -8.174  13.386  -9.307  1.00 10.99 ? 168 LYS B CB  1 
ATOM   3458 C  CG  . LYS B 1 168 ? -8.417  14.198  -8.065  1.00 12.06 ? 168 LYS B CG  1 
ATOM   3459 C  CD  . LYS B 1 168 ? -7.156  14.969  -7.724  1.00 15.11 ? 168 LYS B CD  1 
ATOM   3460 C  CE  . LYS B 1 168 ? -7.480  15.884  -6.537  1.00 19.17 ? 168 LYS B CE  1 
ATOM   3461 N  NZ  . LYS B 1 168 ? -6.341  16.788  -6.253  1.00 23.93 ? 168 LYS B NZ  1 
ATOM   3462 N  N   . GLY B 1 169 ? -11.480 13.490  -8.997  1.00 10.48 ? 169 GLY B N   1 
ATOM   3463 C  CA  . GLY B 1 169 ? -12.665 14.323  -9.043  1.00 12.12 ? 169 GLY B CA  1 
ATOM   3464 C  C   . GLY B 1 169 ? -13.872 13.698  -9.677  1.00 13.21 ? 169 GLY B C   1 
ATOM   3465 O  O   . GLY B 1 169 ? -15.011 14.293  -9.595  1.00 14.95 ? 169 GLY B O   1 
ATOM   3466 N  N   . GLN B 1 170 ? -13.709 12.564  -10.365 1.00 10.71 ? 170 GLN B N   1 
ATOM   3467 C  CA  . GLN B 1 170 ? -14.827 11.906  -11.032 1.00 11.53 ? 170 GLN B CA  1 
ATOM   3468 C  C   . GLN B 1 170 ? -15.701 11.216  -9.963  1.00 12.63 ? 170 GLN B C   1 
ATOM   3469 O  O   . GLN B 1 170 ? -15.222 10.771  -8.914  1.00 12.27 ? 170 GLN B O   1 
ATOM   3470 C  CB  . GLN B 1 170 ? -14.313 10.933  -12.076 1.00 10.87 ? 170 GLN B CB  1 
ATOM   3471 C  CG  . GLN B 1 170 ? -13.639 11.701  -13.269 1.00 11.60 ? 170 GLN B CG  1 
ATOM   3472 C  CD  . GLN B 1 170 ? -13.394 10.804  -14.442 1.00 12.73 ? 170 GLN B CD  1 
ATOM   3473 O  OE1 . GLN B 1 170 ? -13.053 9.640   -14.320 1.00 12.36 ? 170 GLN B OE1 1 
ATOM   3474 N  NE2 . GLN B 1 170 ? -13.483 11.373  -15.633 1.00 15.66 ? 170 GLN B NE2 1 
ATOM   3475 N  N   . GLU B 1 171 ? -16.981 11.238  -10.245 1.00 13.29 ? 171 GLU B N   1 
ATOM   3476 C  CA  . GLU B 1 171 ? -18.039 10.699  -9.368  1.00 13.63 ? 171 GLU B CA  1 
ATOM   3477 C  C   . GLU B 1 171 ? -18.966 9.776   -10.186 1.00 15.42 ? 171 GLU B C   1 
ATOM   3478 O  O   . GLU B 1 171 ? -19.159 9.949   -11.428 1.00 17.61 ? 171 GLU B O   1 
ATOM   3479 C  CB  . GLU B 1 171 ? -18.826 11.863  -8.767  1.00 15.44 ? 171 GLU B CB  1 
ATOM   3480 C  CG  . GLU B 1 171 ? -17.957 12.754  -7.845  1.00 19.51 ? 171 GLU B CG  1 
ATOM   3481 C  CD  . GLU B 1 171 ? -18.670 13.910  -7.121  1.00 25.61 ? 171 GLU B CD  1 
ATOM   3482 O  OE1 . GLU B 1 171 ? -19.790 14.256  -7.482  1.00 27.36 ? 171 GLU B OE1 1 
ATOM   3483 O  OE2 . GLU B 1 171 ? -18.065 14.472  -6.180  1.00 31.64 ? 171 GLU B OE2 1 
ATOM   3484 N  N   . ALA B 1 172 ? -19.482 8.716   -9.557  1.00 13.21 ? 172 ALA B N   1 
ATOM   3485 C  CA  . ALA B 1 172 ? -20.381 7.749   -10.167 1.00 13.53 ? 172 ALA B CA  1 
ATOM   3486 C  C   . ALA B 1 172 ? -21.318 7.255   -9.042  1.00 14.06 ? 172 ALA B C   1 
ATOM   3487 O  O   . ALA B 1 172 ? -21.111 7.587   -7.895  1.00 14.40 ? 172 ALA B O   1 
ATOM   3488 C  CB  . ALA B 1 172 ? -19.671 6.609   -10.815 1.00 14.25 ? 172 ALA B CB  1 
ATOM   3489 N  N   . PHE B 1 173 ? -22.449 6.715   -9.425  1.00 13.02 ? 173 PHE B N   1 
ATOM   3490 C  CA  . PHE B 1 173 ? -23.411 6.164   -8.466  1.00 11.08 ? 173 PHE B CA  1 
ATOM   3491 C  C   . PHE B 1 173 ? -23.460 4.669   -8.514  1.00 12.76 ? 173 PHE B C   1 
ATOM   3492 O  O   . PHE B 1 173 ? -23.428 4.036   -9.560  1.00 15.65 ? 173 PHE B O   1 
ATOM   3493 C  CB  . PHE B 1 173 ? -24.806 6.737   -8.835  1.00 13.48 ? 173 PHE B CB  1 
ATOM   3494 C  CG  . PHE B 1 173 ? -25.105 8.116   -8.269  1.00 15.42 ? 173 PHE B CG  1 
ATOM   3495 C  CD1 . PHE B 1 173 ? -25.220 8.345   -6.876  1.00 17.42 ? 173 PHE B CD1 1 
ATOM   3496 C  CD2 . PHE B 1 173 ? -25.301 9.217   -9.109  1.00 19.71 ? 173 PHE B CD2 1 
ATOM   3497 C  CE1 . PHE B 1 173 ? -25.478 9.603   -6.356  1.00 20.46 ? 173 PHE B CE1 1 
ATOM   3498 C  CE2 . PHE B 1 173 ? -25.574 10.486  -8.596  1.00 21.57 ? 173 PHE B CE2 1 
ATOM   3499 C  CZ  . PHE B 1 173 ? -25.619 10.703  -7.216  1.00 22.06 ? 173 PHE B CZ  1 
ATOM   3500 N  N   . VAL B 1 174 ? -23.486 4.095   -7.319  1.00 11.92 ? 174 VAL B N   1 
ATOM   3501 C  CA  . VAL B 1 174 ? -23.464 2.652   -7.135  1.00 12.11 ? 174 VAL B CA  1 
ATOM   3502 C  C   . VAL B 1 174 ? -24.864 2.362   -6.472  1.00 12.34 ? 174 VAL B C   1 
ATOM   3503 O  O   . VAL B 1 174 ? -25.166 2.914   -5.421  1.00 12.28 ? 174 VAL B O   1 
ATOM   3504 C  CB  . VAL B 1 174 ? -22.340 2.230   -6.189  1.00 12.96 ? 174 VAL B CB  1 
ATOM   3505 C  CG1 . VAL B 1 174 ? -22.356 0.724   -5.889  1.00 14.97 ? 174 VAL B CG1 1 
ATOM   3506 C  CG2 . VAL B 1 174 ? -20.980 2.561   -6.846  1.00 13.76 ? 174 VAL B CG2 1 
ATOM   3507 N  N   . PRO B 1 175 ? -25.609 1.422   -7.077  1.00 11.64 ? 175 PRO B N   1 
ATOM   3508 C  CA  . PRO B 1 175 ? -26.872 1.012   -6.364  1.00 12.48 ? 175 PRO B CA  1 
ATOM   3509 C  C   . PRO B 1 175 ? -26.517 0.430   -4.955  1.00 11.87 ? 175 PRO B C   1 
ATOM   3510 O  O   . PRO B 1 175 ? -25.494 -0.229  -4.734  1.00 13.89 ? 175 PRO B O   1 
ATOM   3511 C  CB  . PRO B 1 175 ? -27.464 -0.021  -7.293  1.00 12.91 ? 175 PRO B CB  1 
ATOM   3512 C  CG  . PRO B 1 175 ? -26.907 0.248   -8.688  1.00 12.45 ? 175 PRO B CG  1 
ATOM   3513 C  CD  . PRO B 1 175 ? -25.461 0.771   -8.393  1.00 11.89 ? 175 PRO B CD  1 
ATOM   3514 N  N   . GLY B 1 176 ? -27.466 0.593   -4.039  1.00 12.71 ? 176 GLY B N   1 
ATOM   3515 C  CA  . GLY B 1 176 ? -27.347 0.061   -2.684  1.00 12.71 ? 176 GLY B CA  1 
ATOM   3516 C  C   . GLY B 1 176 ? -27.271 -1.442  -2.729  1.00 13.06 ? 176 GLY B C   1 
ATOM   3517 O  O   . GLY B 1 176 ? -27.812 -2.148  -3.586  1.00 13.60 ? 176 GLY B O   1 
ATOM   3518 N  N   . PHE B 1 177 ? -26.475 -1.901  -1.741  1.00 12.45 ? 177 PHE B N   1 
ATOM   3519 C  CA  . PHE B 1 177 ? -26.405 -3.363  -1.496  1.00 12.09 ? 177 PHE B CA  1 
ATOM   3520 C  C   . PHE B 1 177 ? -26.114 -3.525  -0.018  1.00 12.91 ? 177 PHE B C   1 
ATOM   3521 O  O   . PHE B 1 177 ? -25.938 -2.575  0.721   1.00 13.19 ? 177 PHE B O   1 
ATOM   3522 C  CB  . PHE B 1 177 ? -25.350 -4.105  -2.361  1.00 13.14 ? 177 PHE B CB  1 
ATOM   3523 C  CG  . PHE B 1 177 ? -23.935 -3.663  -2.123  1.00 13.97 ? 177 PHE B CG  1 
ATOM   3524 C  CD1 . PHE B 1 177 ? -23.036 -4.477  -1.372  1.00 14.59 ? 177 PHE B CD1 1 
ATOM   3525 C  CD2 . PHE B 1 177 ? -23.472 -2.448  -2.690  1.00 12.89 ? 177 PHE B CD2 1 
ATOM   3526 C  CE1 . PHE B 1 177 ? -21.697 -4.101  -1.206  1.00 12.77 ? 177 PHE B CE1 1 
ATOM   3527 C  CE2 . PHE B 1 177 ? -22.136 -2.065  -2.498  1.00 14.47 ? 177 PHE B CE2 1 
ATOM   3528 C  CZ  . PHE B 1 177 ? -21.265 -2.861  -1.737  1.00 13.05 ? 177 PHE B CZ  1 
ATOM   3529 N  N   . ASN B 1 178 ? -26.133 -4.793  0.439   1.00 14.47 ? 178 ASN B N   1 
ATOM   3530 C  CA  . ASN B 1 178 ? -25.877 -5.032  1.813   1.00 14.33 ? 178 ASN B CA  1 
ATOM   3531 C  C   . ASN B 1 178 ? -24.360 -5.006  2.126   1.00 12.68 ? 178 ASN B C   1 
ATOM   3532 O  O   . ASN B 1 178 ? -23.585 -5.918  1.785   1.00 13.55 ? 178 ASN B O   1 
ATOM   3533 C  CB  . ASN B 1 178 ? -26.514 -6.368  2.241   1.00 14.79 ? 178 ASN B CB  1 
ATOM   3534 C  CG  . ASN B 1 178 ? -26.285 -6.670  3.676   1.00 14.33 ? 178 ASN B CG  1 
ATOM   3535 O  OD1 . ASN B 1 178 ? -25.948 -5.856  4.531   1.00 15.58 ? 178 ASN B OD1 1 
ATOM   3536 N  ND2 . ASN B 1 178 ? -26.557 -8.009  3.984   1.00 20.28 ? 178 ASN B ND2 1 
ATOM   3537 N  N   . ILE B 1 179 ? -23.998 -3.900  2.740   1.00 11.95 ? 179 ILE B N   1 
ATOM   3538 C  CA  . ILE B 1 179 ? -22.537 -3.655  3.110   1.00 12.38 ? 179 ILE B CA  1 
ATOM   3539 C  C   . ILE B 1 179 ? -22.036 -4.746  4.007   1.00 15.20 ? 179 ILE B C   1 
ATOM   3540 O  O   . ILE B 1 179 ? -20.814 -5.016  4.031   1.00 13.61 ? 179 ILE B O   1 
ATOM   3541 C  CB  . ILE B 1 179 ? -22.331 -2.256  3.748   1.00 13.70 ? 179 ILE B CB  1 
ATOM   3542 C  CG1 . ILE B 1 179 ? -22.879 -1.237  2.711   1.00 12.35 ? 179 ILE B CG1 1 
ATOM   3543 C  CG2 . ILE B 1 179 ? -20.863 -1.895  4.104   1.00 12.63 ? 179 ILE B CG2 1 
ATOM   3544 C  CD1 . ILE B 1 179 ? -22.250 -1.320  1.313   1.00 13.76 ? 179 ILE B CD1 1 
ATOM   3545 N  N   . GLU B 1 180 ? -22.893 -5.399  4.781   1.00 13.25 ? 180 GLU B N   1 
ATOM   3546 C  CA  . GLU B 1 180 ? -22.375 -6.497  5.605   1.00 15.22 ? 180 GLU B CA  1 
ATOM   3547 C  C   . GLU B 1 180 ? -21.791 -7.645  4.791   1.00 14.01 ? 180 GLU B C   1 
ATOM   3548 O  O   . GLU B 1 180 ? -20.959 -8.466  5.343   1.00 14.68 ? 180 GLU B O   1 
ATOM   3549 C  CB  . GLU B 1 180 ? -23.490 -6.936  6.598   1.00 19.60 ? 180 GLU B CB  1 
ATOM   3550 C  CG  . GLU B 1 180 ? -22.958 -7.747  7.777   1.00 21.46 ? 180 GLU B CG  1 
ATOM   3551 C  CD  . GLU B 1 180 ? -24.031 -8.089  8.820   1.00 26.40 ? 180 GLU B CD  1 
ATOM   3552 O  OE1 . GLU B 1 180 ? -25.221 -7.603  8.724   1.00 23.98 ? 180 GLU B OE1 1 
ATOM   3553 O  OE2 . GLU B 1 180 ? -23.623 -8.839  9.749   1.00 25.47 ? 180 GLU B OE2 1 
ATOM   3554 N  N   . GLU B 1 181 ? -22.178 -7.760  3.504   1.00 12.97 ? 181 GLU B N   1 
ATOM   3555 C  CA  . GLU B 1 181 ? -21.624 -8.777  2.617   1.00 12.94 ? 181 GLU B CA  1 
ATOM   3556 C  C   . GLU B 1 181 ? -20.104 -8.554  2.388   1.00 12.06 ? 181 GLU B C   1 
ATOM   3557 O  O   . GLU B 1 181 ? -19.454 -9.455  1.878   1.00 14.37 ? 181 GLU B O   1 
ATOM   3558 C  CB  . GLU B 1 181 ? -22.288 -8.736  1.211   1.00 13.96 ? 181 GLU B CB  1 
ATOM   3559 C  CG  . GLU B 1 181 ? -23.770 -9.076  1.244   1.00 18.38 ? 181 GLU B CG  1 
ATOM   3560 C  CD  . GLU B 1 181 ? -24.442 -8.969  -0.120  1.00 23.00 ? 181 GLU B CD  1 
ATOM   3561 O  OE1 . GLU B 1 181 ? -23.799 -8.632  -1.188  1.00 24.83 ? 181 GLU B OE1 1 
ATOM   3562 O  OE2 . GLU B 1 181 ? -25.716 -9.143  -0.144  1.00 23.50 ? 181 GLU B OE2 1 
ATOM   3563 N  N   . LEU B 1 182 ? -19.606 -7.372  2.699   1.00 11.28 ? 182 LEU B N   1 
ATOM   3564 C  CA  . LEU B 1 182 ? -18.165 -7.087  2.541   1.00 11.37 ? 182 LEU B CA  1 
ATOM   3565 C  C   . LEU B 1 182 ? -17.390 -7.545  3.772   1.00 11.39 ? 182 LEU B C   1 
ATOM   3566 O  O   . LEU B 1 182 ? -16.117 -7.496  3.764   1.00 12.45 ? 182 LEU B O   1 
ATOM   3567 C  CB  . LEU B 1 182 ? -17.954 -5.599  2.390   1.00 10.23 ? 182 LEU B CB  1 
ATOM   3568 C  CG  . LEU B 1 182 ? -18.648 -4.981  1.122   1.00 8.92  ? 182 LEU B CG  1 
ATOM   3569 C  CD1 . LEU B 1 182 ? -18.270 -3.478  1.109   1.00 9.52  ? 182 LEU B CD1 1 
ATOM   3570 C  CD2 . LEU B 1 182 ? -18.291 -5.543  -0.161  1.00 10.36 ? 182 LEU B CD2 1 
ATOM   3571 N  N   . LEU B 1 183 ? -18.089 -7.869  4.882   1.00 10.27 ? 183 LEU B N   1 
ATOM   3572 C  CA  . LEU B 1 183 ? -17.378 -8.257  6.142   1.00 11.07 ? 183 LEU B CA  1 
ATOM   3573 C  C   . LEU B 1 183 ? -17.131 -9.736  6.054   1.00 12.50 ? 183 LEU B C   1 
ATOM   3574 O  O   . LEU B 1 183 ? -17.798 -10.468 5.355   1.00 13.99 ? 183 LEU B O   1 
ATOM   3575 C  CB  . LEU B 1 183 ? -18.277 -8.001  7.348   1.00 13.16 ? 183 LEU B CB  1 
ATOM   3576 C  CG  . LEU B 1 183 ? -18.719 -6.545  7.406   1.00 12.43 ? 183 LEU B CG  1 
ATOM   3577 C  CD1 . LEU B 1 183 ? -19.470 -6.206  8.717   1.00 15.88 ? 183 LEU B CD1 1 
ATOM   3578 C  CD2 . LEU B 1 183 ? -17.519 -5.621  7.365   1.00 14.45 ? 183 LEU B CD2 1 
ATOM   3579 N  N   . PRO B 1 184 ? -16.090 -10.199 6.785   1.00 12.03 ? 184 PRO B N   1 
ATOM   3580 C  CA  . PRO B 1 184 ? -15.730 -11.644 6.776   1.00 14.50 ? 184 PRO B CA  1 
ATOM   3581 C  C   . PRO B 1 184 ? -16.596 -12.464 7.661   1.00 15.02 ? 184 PRO B C   1 
ATOM   3582 O  O   . PRO B 1 184 ? -17.563 -11.989 8.275   1.00 15.24 ? 184 PRO B O   1 
ATOM   3583 C  CB  . PRO B 1 184 ? -14.304 -11.630 7.377   1.00 14.96 ? 184 PRO B CB  1 
ATOM   3584 C  CG  . PRO B 1 184 ? -14.350 -10.436 8.304   1.00 14.95 ? 184 PRO B CG  1 
ATOM   3585 C  CD  . PRO B 1 184 ? -15.178 -9.406  7.593   1.00 14.18 ? 184 PRO B CD  1 
ATOM   3586 N  N   . GLU B 1 185 ? -16.235 -13.749 7.625   1.00 17.44 ? 185 GLU B N   1 
ATOM   3587 C  CA  . GLU B 1 185 ? -16.780 -14.720 8.608   1.00 18.73 ? 185 GLU B CA  1 
ATOM   3588 C  C   . GLU B 1 185 ? -16.387 -14.391 10.051  1.00 17.34 ? 185 GLU B C   1 
ATOM   3589 O  O   . GLU B 1 185 ? -15.249 -13.898 10.340  1.00 17.07 ? 185 GLU B O   1 
ATOM   3590 C  CB  . GLU B 1 185 ? -16.264 -16.097 8.262   1.00 22.99 ? 185 GLU B CB  1 
ATOM   3591 C  CG  . GLU B 1 185 ? -16.867 -16.608 6.975   1.00 29.87 ? 185 GLU B CG  1 
ATOM   3592 C  CD  . GLU B 1 185 ? -16.557 -18.082 6.744   1.00 43.70 ? 185 GLU B CD  1 
ATOM   3593 O  OE1 . GLU B 1 185 ? -17.510 -18.829 6.416   1.00 54.99 ? 185 GLU B OE1 1 
ATOM   3594 O  OE2 . GLU B 1 185 ? -15.373 -18.497 6.901   1.00 48.76 ? 185 GLU B OE2 1 
ATOM   3595 N  N   . ARG B 1 186 ? -17.338 -14.624 10.963  1.00 18.17 ? 186 ARG B N   1 
ATOM   3596 C  CA  . ARG B 1 186 ? -17.071 -14.566 12.421  1.00 17.27 ? 186 ARG B CA  1 
ATOM   3597 C  C   . ARG B 1 186 ? -16.599 -13.146 12.767  1.00 15.25 ? 186 ARG B C   1 
ATOM   3598 O  O   . ARG B 1 186 ? -15.482 -12.853 13.318  1.00 17.00 ? 186 ARG B O   1 
ATOM   3599 C  CB  . ARG B 1 186 ? -16.117 -15.673 12.915  1.00 20.40 ? 186 ARG B CB  1 
ATOM   3600 C  CG  . ARG B 1 186 ? -16.725 -17.088 12.888  1.00 25.01 ? 186 ARG B CG  1 
ATOM   3601 C  CD  . ARG B 1 186 ? -15.687 -18.140 13.304  1.00 27.01 ? 186 ARG B CD  1 
ATOM   3602 N  NE  . ARG B 1 186 ? -14.506 -18.307 12.445  1.00 30.05 ? 186 ARG B NE  1 
ATOM   3603 C  CZ  . ARG B 1 186 ? -14.539 -18.831 11.216  1.00 34.37 ? 186 ARG B CZ  1 
ATOM   3604 N  NH1 . ARG B 1 186 ? -15.707 -19.172 10.674  1.00 40.89 ? 186 ARG B NH1 1 
ATOM   3605 N  NH2 . ARG B 1 186 ? -13.421 -18.989 10.513  1.00 34.90 ? 186 ARG B NH2 1 
ATOM   3606 N  N   . THR B 1 187 ? -17.466 -12.241 12.405  1.00 13.53 ? 187 THR B N   1 
ATOM   3607 C  CA  . THR B 1 187 ? -17.181 -10.839 12.804  1.00 12.09 ? 187 THR B CA  1 
ATOM   3608 C  C   . THR B 1 187 ? -17.023 -10.639 14.310  1.00 11.93 ? 187 THR B C   1 
ATOM   3609 O  O   . THR B 1 187 ? -16.481 -9.621  14.787  1.00 12.27 ? 187 THR B O   1 
ATOM   3610 C  CB  . THR B 1 187 ? -18.194 -9.873  12.225  1.00 14.23 ? 187 THR B CB  1 
ATOM   3611 O  OG1 . THR B 1 187 ? -19.521 -10.295 12.587  1.00 15.26 ? 187 THR B OG1 1 
ATOM   3612 C  CG2 . THR B 1 187 ? -18.068 -9.815  10.646  1.00 15.21 ? 187 THR B CG2 1 
ATOM   3613 N  N   . ALA B 1 188 ? -17.498 -11.619 15.125  1.00 13.27 ? 188 ALA B N   1 
ATOM   3614 C  CA  . ALA B 1 188 ? -17.271 -11.487 16.522  1.00 12.08 ? 188 ALA B CA  1 
ATOM   3615 C  C   . ALA B 1 188 ? -15.798 -11.496 16.919  1.00 11.46 ? 188 ALA B C   1 
ATOM   3616 O  O   . ALA B 1 188 ? -15.469 -11.087 18.010  1.00 12.14 ? 188 ALA B O   1 
ATOM   3617 C  CB  . ALA B 1 188 ? -18.022 -12.576 17.335  1.00 14.45 ? 188 ALA B CB  1 
ATOM   3618 N  N   . GLU B 1 189 ? -14.940 -12.034 16.083  1.00 11.95 ? 189 GLU B N   1 
ATOM   3619 C  CA  . GLU B 1 189 ? -13.461 -12.111 16.339  1.00 11.30 ? 189 GLU B CA  1 
ATOM   3620 C  C   . GLU B 1 189 ? -12.729 -10.958 15.694  1.00 11.45 ? 189 GLU B C   1 
ATOM   3621 O  O   . GLU B 1 189 ? -12.722 -10.837 14.414  1.00 11.77 ? 189 GLU B O   1 
ATOM   3622 C  CB  . GLU B 1 189 ? -12.940 -13.432 15.793  1.00 14.61 ? 189 GLU B CB  1 
ATOM   3623 C  CG  . GLU B 1 189 ? -13.706 -14.578 16.465  1.00 18.16 ? 189 GLU B CG  1 
ATOM   3624 C  CD  . GLU B 1 189 ? -13.200 -15.964 16.090  1.00 24.94 ? 189 GLU B CD  1 
ATOM   3625 O  OE1 . GLU B 1 189 ? -11.971 -16.212 15.896  1.00 26.21 ? 189 GLU B OE1 1 
ATOM   3626 O  OE2 . GLU B 1 189 ? -14.081 -16.902 16.030  1.00 31.22 ? 189 GLU B OE2 1 
ATOM   3627 N  N   . TYR B 1 190 ? -12.219 -10.077 16.490  1.00 10.24 ? 190 TYR B N   1 
ATOM   3628 C  CA  . TYR B 1 190 ? -11.526 -8.881  15.963  1.00 9.68  ? 190 TYR B CA  1 
ATOM   3629 C  C   . TYR B 1 190 ? -10.432 -8.416  16.890  1.00 10.37 ? 190 TYR B C   1 
ATOM   3630 O  O   . TYR B 1 190 ? -10.376 -8.776  18.071  1.00 10.30 ? 190 TYR B O   1 
ATOM   3631 C  CB  . TYR B 1 190 ? -12.586 -7.769  15.700  1.00 8.80  ? 190 TYR B CB  1 
ATOM   3632 C  CG  . TYR B 1 190 ? -13.409 -7.369  16.970  1.00 8.99  ? 190 TYR B CG  1 
ATOM   3633 C  CD1 . TYR B 1 190 ? -12.888 -6.414  17.892  1.00 9.27  ? 190 TYR B CD1 1 
ATOM   3634 C  CD2 . TYR B 1 190 ? -14.682 -7.884  17.160  1.00 9.49  ? 190 TYR B CD2 1 
ATOM   3635 C  CE1 . TYR B 1 190 ? -13.671 -6.002  18.990  1.00 10.00 ? 190 TYR B CE1 1 
ATOM   3636 C  CE2 . TYR B 1 190 ? -15.431 -7.499  18.279  1.00 9.76  ? 190 TYR B CE2 1 
ATOM   3637 C  CZ  . TYR B 1 190 ? -14.924 -6.544  19.143  1.00 10.45 ? 190 TYR B CZ  1 
ATOM   3638 O  OH  . TYR B 1 190 ? -15.724 -6.173  20.204  1.00 12.55 ? 190 TYR B OH  1 
ATOM   3639 N  N   . TYR B 1 191 ? -9.564  -7.532  16.382  1.00 9.50  ? 191 TYR B N   1 
ATOM   3640 C  CA  . TYR B 1 191 ? -8.551  -6.871  17.129  1.00 9.28  ? 191 TYR B CA  1 
ATOM   3641 C  C   . TYR B 1 191 ? -8.987  -5.431  17.307  1.00 10.61 ? 191 TYR B C   1 
ATOM   3642 O  O   . TYR B 1 191 ? -9.681  -4.881  16.445  1.00 10.42 ? 191 TYR B O   1 
ATOM   3643 C  CB  . TYR B 1 191 ? -7.224  -6.735  16.279  1.00 9.55  ? 191 TYR B CB  1 
ATOM   3644 C  CG  . TYR B 1 191 ? -6.633  -7.994  15.699  1.00 10.91 ? 191 TYR B CG  1 
ATOM   3645 C  CD1 . TYR B 1 191 ? -5.631  -8.627  16.397  1.00 11.27 ? 191 TYR B CD1 1 
ATOM   3646 C  CD2 . TYR B 1 191 ? -7.042  -8.494  14.439  1.00 10.27 ? 191 TYR B CD2 1 
ATOM   3647 C  CE1 . TYR B 1 191 ? -5.058  -9.773  15.868  1.00 12.57 ? 191 TYR B CE1 1 
ATOM   3648 C  CE2 . TYR B 1 191 ? -6.444  -9.636  13.855  1.00 12.50 ? 191 TYR B CE2 1 
ATOM   3649 C  CZ  . TYR B 1 191 ? -5.458  -10.277 14.628  1.00 13.19 ? 191 TYR B CZ  1 
ATOM   3650 O  OH  . TYR B 1 191 ? -4.869  -11.377 14.049  1.00 17.51 ? 191 TYR B OH  1 
ATOM   3651 N  N   . ARG B 1 192 ? -8.676  -4.838  18.448  1.00 10.61 ? 192 ARG B N   1 
ATOM   3652 C  CA  . ARG B 1 192 ? -9.141  -3.501  18.766  1.00 9.91  ? 192 ARG B CA  1 
ATOM   3653 C  C   . ARG B 1 192 ? -8.016  -2.705  19.379  1.00 12.07 ? 192 ARG B C   1 
ATOM   3654 O  O   . ARG B 1 192 ? -7.375  -3.134  20.315  1.00 11.28 ? 192 ARG B O   1 
ATOM   3655 C  CB  . ARG B 1 192 ? -10.345 -3.601  19.787  1.00 12.12 ? 192 ARG B CB  1 
ATOM   3656 C  CG  . ARG B 1 192 ? -10.633 -2.280  20.560  1.00 13.81 ? 192 ARG B CG  1 
ATOM   3657 C  CD  . ARG B 1 192 ? -11.407 -1.263  19.748  1.00 13.07 ? 192 ARG B CD  1 
ATOM   3658 N  NE  . ARG B 1 192 ? -12.565 -1.772  19.023  1.00 14.89 ? 192 ARG B NE  1 
ATOM   3659 C  CZ  . ARG B 1 192 ? -13.745 -2.137  19.552  1.00 15.95 ? 192 ARG B CZ  1 
ATOM   3660 N  NH1 . ARG B 1 192 ? -14.020 -2.004  20.897  1.00 17.37 ? 192 ARG B NH1 1 
ATOM   3661 N  NH2 . ARG B 1 192 ? -14.665 -2.619  18.742  1.00 16.52 ? 192 ARG B NH2 1 
ATOM   3662 N  N   . TYR B 1 193 ? -7.836  -1.452  18.950  1.00 11.70 ? 193 TYR B N   1 
ATOM   3663 C  CA  . TYR B 1 193 ? -6.747  -0.645  19.452  1.00 11.88 ? 193 TYR B CA  1 
ATOM   3664 C  C   . TYR B 1 193 ? -7.019  0.834   19.171  1.00 11.64 ? 193 TYR B C   1 
ATOM   3665 O  O   . TYR B 1 193 ? -7.833  1.155   18.278  1.00 13.05 ? 193 TYR B O   1 
ATOM   3666 C  CB  . TYR B 1 193 ? -5.323  -1.088  18.963  1.00 11.90 ? 193 TYR B CB  1 
ATOM   3667 C  CG  . TYR B 1 193 ? -4.946  -0.643  17.561  1.00 10.06 ? 193 TYR B CG  1 
ATOM   3668 C  CD1 . TYR B 1 193 ? -4.205  0.553   17.356  1.00 9.60  ? 193 TYR B CD1 1 
ATOM   3669 C  CD2 . TYR B 1 193 ? -5.387  -1.377  16.454  1.00 9.86  ? 193 TYR B CD2 1 
ATOM   3670 C  CE1 . TYR B 1 193 ? -3.846  0.934   16.099  1.00 10.03 ? 193 TYR B CE1 1 
ATOM   3671 C  CE2 . TYR B 1 193 ? -5.036  -0.989  15.156  1.00 8.42  ? 193 TYR B CE2 1 
ATOM   3672 C  CZ  . TYR B 1 193 ? -4.315  0.196   15.009  1.00 8.65  ? 193 TYR B CZ  1 
ATOM   3673 O  OH  . TYR B 1 193 ? -4.001  0.604   13.724  1.00 10.58 ? 193 TYR B OH  1 
ATOM   3674 N  N   . ARG B 1 194 ? -6.309  1.684   19.898  1.00 12.93 ? 194 ARG B N   1 
ATOM   3675 C  CA  . ARG B 1 194 ? -6.424  3.132   19.696  1.00 13.71 ? 194 ARG B CA  1 
ATOM   3676 C  C   . ARG B 1 194 ? -5.354  3.547   18.739  1.00 15.04 ? 194 ARG B C   1 
ATOM   3677 O  O   . ARG B 1 194 ? -4.159  3.379   18.976  1.00 15.98 ? 194 ARG B O   1 
ATOM   3678 C  CB  . ARG B 1 194 ? -6.203  3.871   21.041  1.00 19.28 ? 194 ARG B CB  1 
ATOM   3679 C  CG  . ARG B 1 194 ? -7.254  3.455   22.053  1.00 24.99 ? 194 ARG B CG  1 
ATOM   3680 C  CD  . ARG B 1 194 ? -7.543  4.508   23.104  1.00 38.92 ? 194 ARG B CD  1 
ATOM   3681 N  NE  . ARG B 1 194 ? -8.909  4.319   23.629  1.00 42.85 ? 194 ARG B NE  1 
ATOM   3682 C  CZ  . ARG B 1 194 ? -9.923  5.169   23.450  1.00 48.51 ? 194 ARG B CZ  1 
ATOM   3683 N  NH1 . ARG B 1 194 ? -9.744  6.303   22.781  1.00 52.47 ? 194 ARG B NH1 1 
ATOM   3684 N  NH2 . ARG B 1 194 ? -11.124 4.888   23.959  1.00 49.77 ? 194 ARG B NH2 1 
ATOM   3685 N  N   . GLY B 1 195 ? -5.766  4.159   17.623  1.00 13.01 ? 195 GLY B N   1 
ATOM   3686 C  CA  . GLY B 1 195 ? -4.765  4.670   16.667  1.00 12.91 ? 195 GLY B CA  1 
ATOM   3687 C  C   . GLY B 1 195 ? -5.190  5.956   15.999  1.00 14.51 ? 195 GLY B C   1 
ATOM   3688 O  O   . GLY B 1 195 ? -5.800  6.837   16.588  1.00 14.62 ? 195 GLY B O   1 
ATOM   3689 N  N   . SER B 1 196 ? -4.828  6.048   14.738  1.00 11.98 ? 196 SER B N   1 
ATOM   3690 C  CA  . SER B 1 196 ? -4.937  7.314   13.989  1.00 10.43 ? 196 SER B CA  1 
ATOM   3691 C  C   . SER B 1 196 ? -5.529  7.056   12.571  1.00 10.62 ? 196 SER B C   1 
ATOM   3692 O  O   . SER B 1 196 ? -5.634  5.909   12.083  1.00 11.34 ? 196 SER B O   1 
ATOM   3693 C  CB  . SER B 1 196 ? -3.523  7.972   13.837  1.00 10.28 ? 196 SER B CB  1 
ATOM   3694 O  OG  . SER B 1 196 ? -2.812  7.262   12.823  1.00 11.43 ? 196 SER B OG  1 
ATOM   3695 N  N   . LEU B 1 197 ? -5.845  8.159   11.902  1.00 11.00 ? 197 LEU B N   1 
ATOM   3696 C  CA  . LEU B 1 197 ? -6.055  8.100   10.419  1.00 10.21 ? 197 LEU B CA  1 
ATOM   3697 C  C   . LEU B 1 197 ? -4.727  7.637   9.845   1.00 9.70  ? 197 LEU B C   1 
ATOM   3698 O  O   . LEU B 1 197 ? -3.634  8.013   10.310  1.00 9.87  ? 197 LEU B O   1 
ATOM   3699 C  CB  . LEU B 1 197 ? -6.374  9.527   9.884   1.00 10.93 ? 197 LEU B CB  1 
ATOM   3700 C  CG  . LEU B 1 197 ? -7.693  10.070  10.340  1.00 14.05 ? 197 LEU B CG  1 
ATOM   3701 C  CD1 . LEU B 1 197 ? -7.738  11.435  9.608   1.00 16.73 ? 197 LEU B CD1 1 
ATOM   3702 C  CD2 . LEU B 1 197 ? -8.919  9.271   10.077  1.00 16.26 ? 197 LEU B CD2 1 
ATOM   3703 N  N   . THR B 1 198 ? -4.805  6.778   8.794   1.00 9.94  ? 198 THR B N   1 
ATOM   3704 C  CA  . THR B 1 198 ? -3.552  6.308   8.140   1.00 8.93  ? 198 THR B CA  1 
ATOM   3705 C  C   . THR B 1 198 ? -3.090  7.229   6.997   1.00 9.81  ? 198 THR B C   1 
ATOM   3706 O  O   . THR B 1 198 ? -2.113  6.929   6.272   1.00 11.48 ? 198 THR B O   1 
ATOM   3707 C  CB  . THR B 1 198 ? -3.672  4.897   7.606   1.00 9.04  ? 198 THR B CB  1 
ATOM   3708 O  OG1 . THR B 1 198 ? -4.642  4.903   6.543   1.00 9.33  ? 198 THR B OG1 1 
ATOM   3709 C  CG2 . THR B 1 198 ? -4.130  3.915   8.702   1.00 9.87  ? 198 THR B CG2 1 
ATOM   3710 N  N   . THR B 1 199 ? -3.786  8.374   6.868   1.00 11.70 ? 199 THR B N   1 
ATOM   3711 C  CA  . THR B 1 199 ? -3.511  9.352   5.783   1.00 10.66 ? 199 THR B CA  1 
ATOM   3712 C  C   . THR B 1 199 ? -3.423  10.720  6.505   1.00 11.34 ? 199 THR B C   1 
ATOM   3713 O  O   . THR B 1 199 ? -4.087  10.883  7.529   1.00 12.86 ? 199 THR B O   1 
ATOM   3714 C  CB  . THR B 1 199 ? -4.649  9.414   4.704   1.00 12.46 ? 199 THR B CB  1 
ATOM   3715 O  OG1 . THR B 1 199 ? -5.879  9.698   5.392   1.00 16.03 ? 199 THR B OG1 1 
ATOM   3716 C  CG2 . THR B 1 199 ? -4.698  8.107   3.958   1.00 13.86 ? 199 THR B CG2 1 
ATOM   3717 N  N   . PRO B 1 200 ? -2.705  11.674  5.918   1.00 11.06 ? 200 PRO B N   1 
ATOM   3718 C  CA  . PRO B 1 200 ? -2.777  13.064  6.420   1.00 11.98 ? 200 PRO B CA  1 
ATOM   3719 C  C   . PRO B 1 200 ? -4.247  13.461  6.560   1.00 13.17 ? 200 PRO B C   1 
ATOM   3720 O  O   . PRO B 1 200 ? -5.053  13.125  5.662   1.00 13.88 ? 200 PRO B O   1 
ATOM   3721 C  CB  . PRO B 1 200 ? -2.120  13.860  5.296   1.00 11.17 ? 200 PRO B CB  1 
ATOM   3722 C  CG  . PRO B 1 200 ? -1.058  12.935  4.767   1.00 10.37 ? 200 PRO B CG  1 
ATOM   3723 C  CD  . PRO B 1 200 ? -1.786  11.577  4.757   1.00 11.44 ? 200 PRO B CD  1 
ATOM   3724 N  N   . PRO B 1 201 ? -4.574  14.210  7.646   1.00 12.65 ? 201 PRO B N   1 
ATOM   3725 C  CA  . PRO B 1 201 ? -3.682  14.767  8.657   1.00 12.16 ? 201 PRO B CA  1 
ATOM   3726 C  C   . PRO B 1 201 ? -3.238  13.844  9.788   1.00 12.40 ? 201 PRO B C   1 
ATOM   3727 O  O   . PRO B 1 201 ? -2.659  14.244  10.796  1.00 12.72 ? 201 PRO B O   1 
ATOM   3728 C  CB  . PRO B 1 201 ? -4.483  16.006  9.242   1.00 12.97 ? 201 PRO B CB  1 
ATOM   3729 C  CG  . PRO B 1 201 ? -5.766  15.948  8.512   1.00 15.80 ? 201 PRO B CG  1 
ATOM   3730 C  CD  . PRO B 1 201 ? -5.972  14.610  7.873   1.00 13.84 ? 201 PRO B CD  1 
ATOM   3731 N  N   . CYS B 1 202 ? -3.564  12.544  9.679   1.00 11.47 ? 202 CYS B N   1 
ATOM   3732 C  CA  . CYS B 1 202 ? -3.074  11.490  10.652  1.00 11.37 ? 202 CYS B CA  1 
ATOM   3733 C  C   . CYS B 1 202 ? -3.595  11.689  12.140  1.00 11.91 ? 202 CYS B C   1 
ATOM   3734 O  O   . CYS B 1 202 ? -2.909  11.328  13.088  1.00 12.74 ? 202 CYS B O   1 
ATOM   3735 C  CB  . CYS B 1 202 ? -1.526  11.473  10.718  1.00 11.19 ? 202 CYS B CB  1 
ATOM   3736 S  SG  . CYS B 1 202 ? -0.749  11.095  9.078   1.00 11.85 ? 202 CYS B SG  1 
ATOM   3737 N  N   . ASN B 1 203 ? -4.771  12.291  12.260  1.00 15.45 ? 203 ASN B N   1 
ATOM   3738 C  CA  . ASN B 1 203 ? -5.357  12.591  13.567  1.00 16.61 ? 203 ASN B CA  1 
ATOM   3739 C  C   . ASN B 1 203 ? -5.351  11.347  14.427  1.00 16.11 ? 203 ASN B C   1 
ATOM   3740 O  O   . ASN B 1 203 ? -5.800  10.295  13.969  1.00 14.54 ? 203 ASN B O   1 
ATOM   3741 C  CB  . ASN B 1 203 ? -6.809  13.048  13.421  1.00 18.08 ? 203 ASN B CB  1 
ATOM   3742 C  CG  . ASN B 1 203 ? -6.969  14.298  12.522  1.00 24.25 ? 203 ASN B CG  1 
ATOM   3743 O  OD1 . ASN B 1 203 ? -6.029  14.770  11.902  1.00 27.03 ? 203 ASN B OD1 1 
ATOM   3744 N  ND2 . ASN B 1 203 ? -8.176  14.830  12.479  1.00 25.16 ? 203 ASN B ND2 1 
ATOM   3745 N  N   . PRO B 1 204 ? -4.893  11.468  15.680  1.00 15.40 ? 204 PRO B N   1 
ATOM   3746 C  CA  . PRO B 1 204 ? -4.879  10.232  16.567  1.00 14.65 ? 204 PRO B CA  1 
ATOM   3747 C  C   . PRO B 1 204 ? -6.195  10.015  17.290  1.00 17.90 ? 204 PRO B C   1 
ATOM   3748 O  O   . PRO B 1 204 ? -6.240  9.973   18.535  1.00 16.78 ? 204 PRO B O   1 
ATOM   3749 C  CB  . PRO B 1 204 ? -3.697  10.489  17.526  1.00 16.80 ? 204 PRO B CB  1 
ATOM   3750 C  CG  . PRO B 1 204 ? -3.753  12.066  17.632  1.00 16.41 ? 204 PRO B CG  1 
ATOM   3751 C  CD  . PRO B 1 204 ? -4.129  12.603  16.245  1.00 17.87 ? 204 PRO B CD  1 
ATOM   3752 N  N   . THR B 1 205 ? -7.270  9.871   16.520  1.00 13.78 ? 205 THR B N   1 
ATOM   3753 C  CA  . THR B 1 205 ? -8.605  9.941   17.045  1.00 14.34 ? 205 THR B CA  1 
ATOM   3754 C  C   . THR B 1 205 ? -9.465  8.767   16.577  1.00 12.53 ? 205 THR B C   1 
ATOM   3755 O  O   . THR B 1 205 ? -10.688 8.812   16.657  1.00 15.62 ? 205 THR B O   1 
ATOM   3756 C  CB  . THR B 1 205 ? -9.283  11.265  16.517  1.00 16.26 ? 205 THR B CB  1 
ATOM   3757 O  OG1 . THR B 1 205 ? -9.228  11.265  15.069  1.00 16.95 ? 205 THR B OG1 1 
ATOM   3758 C  CG2 . THR B 1 205 ? -8.569  12.423  17.078  1.00 18.07 ? 205 THR B CG2 1 
ATOM   3759 N  N   . VAL B 1 206 ? -8.838  7.661   16.129  1.00 11.81 ? 206 VAL B N   1 
ATOM   3760 C  CA  . VAL B 1 206 ? -9.586  6.511   15.665  1.00 11.66 ? 206 VAL B CA  1 
ATOM   3761 C  C   . VAL B 1 206 ? -9.542  5.257   16.584  1.00 11.94 ? 206 VAL B C   1 
ATOM   3762 O  O   . VAL B 1 206 ? -8.482  4.833   17.009  1.00 13.02 ? 206 VAL B O   1 
ATOM   3763 C  CB  . VAL B 1 206 ? -9.002  6.034   14.265  1.00 11.16 ? 206 VAL B CB  1 
ATOM   3764 C  CG1 . VAL B 1 206 ? -9.671  4.788   13.809  1.00 11.11 ? 206 VAL B CG1 1 
ATOM   3765 C  CG2 . VAL B 1 206 ? -9.016  7.148   13.228  1.00 12.61 ? 206 VAL B CG2 1 
ATOM   3766 N  N   . LEU B 1 207 ? -10.691 4.752   16.913  1.00 12.38 ? 207 LEU B N   1 
ATOM   3767 C  CA  . LEU B 1 207 ? -10.832 3.418   17.519  1.00 12.04 ? 207 LEU B CA  1 
ATOM   3768 C  C   . LEU B 1 207 ? -10.894 2.418   16.358  1.00 11.75 ? 207 LEU B C   1 
ATOM   3769 O  O   . LEU B 1 207 ? -11.854 2.289   15.643  1.00 10.06 ? 207 LEU B O   1 
ATOM   3770 C  CB  . LEU B 1 207 ? -12.164 3.361   18.321  1.00 13.84 ? 207 LEU B CB  1 
ATOM   3771 C  CG  . LEU B 1 207 ? -12.229 2.209   19.306  1.00 19.04 ? 207 LEU B CG  1 
ATOM   3772 C  CD1 . LEU B 1 207 ? -10.995 2.195   20.235  1.00 21.08 ? 207 LEU B CD1 1 
ATOM   3773 C  CD2 . LEU B 1 207 ? -13.501 2.327   20.110  1.00 23.16 ? 207 LEU B CD2 1 
ATOM   3774 N  N   . TRP B 1 208 ? -9.804  1.674   16.224  1.00 11.18 ? 208 TRP B N   1 
ATOM   3775 C  CA  . TRP B 1 208 ? -9.691  0.608   15.180  1.00 10.60 ? 208 TRP B CA  1 
ATOM   3776 C  C   . TRP B 1 208 ? -10.316 -0.708  15.580  1.00 10.84 ? 208 TRP B C   1 
ATOM   3777 O  O   . TRP B 1 208 ? -10.055 -1.170  16.706  1.00 11.38 ? 208 TRP B O   1 
ATOM   3778 C  CB  . TRP B 1 208 ? -8.200  0.367   14.832  1.00 10.33 ? 208 TRP B CB  1 
ATOM   3779 C  CG  . TRP B 1 208 ? -7.704  1.459   13.918  1.00 10.16 ? 208 TRP B CG  1 
ATOM   3780 C  CD1 . TRP B 1 208 ? -7.004  2.611   14.267  1.00 9.68  ? 208 TRP B CD1 1 
ATOM   3781 C  CD2 . TRP B 1 208 ? -7.909  1.562   12.468  1.00 9.99  ? 208 TRP B CD2 1 
ATOM   3782 N  NE1 . TRP B 1 208 ? -6.749  3.381   13.160  1.00 11.21 ? 208 TRP B NE1 1 
ATOM   3783 C  CE2 . TRP B 1 208 ? -7.266  2.809   12.051  1.00 10.06 ? 208 TRP B CE2 1 
ATOM   3784 C  CE3 . TRP B 1 208 ? -8.526  0.770   11.512  1.00 9.21  ? 208 TRP B CE3 1 
ATOM   3785 C  CZ2 . TRP B 1 208 ? -7.254  3.220   10.730  1.00 9.37  ? 208 TRP B CZ2 1 
ATOM   3786 C  CZ3 . TRP B 1 208 ? -8.507  1.196   10.183  1.00 10.11 ? 208 TRP B CZ3 1 
ATOM   3787 C  CH2 . TRP B 1 208 ? -7.886  2.392   9.804   1.00 9.37  ? 208 TRP B CH2 1 
ATOM   3788 N  N   . THR B 1 209 ? -11.099 -1.316  14.693  1.00 8.35  ? 209 THR B N   1 
ATOM   3789 C  CA  . THR B 1 209 ? -11.491 -2.739  14.827  1.00 9.00  ? 209 THR B CA  1 
ATOM   3790 C  C   . THR B 1 209 ? -10.990 -3.373  13.555  1.00 9.72  ? 209 THR B C   1 
ATOM   3791 O  O   . THR B 1 209 ? -11.521 -3.081  12.469  1.00 9.88  ? 209 THR B O   1 
ATOM   3792 C  CB  . THR B 1 209 ? -13.016 -2.826  14.956  1.00 9.09  ? 209 THR B CB  1 
ATOM   3793 O  OG1 . THR B 1 209 ? -13.428 -2.084  16.100  1.00 10.71 ? 209 THR B OG1 1 
ATOM   3794 C  CG2 . THR B 1 209 ? -13.509 -4.312  14.990  1.00 8.55  ? 209 THR B CG2 1 
ATOM   3795 N  N   . VAL B 1 210 ? -10.043 -4.309  13.665  1.00 9.42  ? 210 VAL B N   1 
ATOM   3796 C  CA  . VAL B 1 210 ? -9.630  -5.088  12.491  1.00 8.45  ? 210 VAL B CA  1 
ATOM   3797 C  C   . VAL B 1 210 ? -10.176 -6.466  12.631  1.00 8.44  ? 210 VAL B C   1 
ATOM   3798 O  O   . VAL B 1 210 ? -9.880  -7.146  13.666  1.00 9.79  ? 210 VAL B O   1 
ATOM   3799 C  CB  . VAL B 1 210 ? -8.110  -5.192  12.441  1.00 8.61  ? 210 VAL B CB  1 
ATOM   3800 C  CG1 . VAL B 1 210 ? -7.703  -5.933  11.184  1.00 8.02  ? 210 VAL B CG1 1 
ATOM   3801 C  CG2 . VAL B 1 210 ? -7.505  -3.773  12.436  1.00 8.66  ? 210 VAL B CG2 1 
ATOM   3802 N  N   . PHE B 1 211 ? -11.023 -6.885  11.729  1.00 7.90  ? 211 PHE B N   1 
ATOM   3803 C  CA  . PHE B 1 211 ? -11.531 -8.299  11.807  1.00 8.19  ? 211 PHE B CA  1 
ATOM   3804 C  C   . PHE B 1 211 ? -10.455 -9.345  11.732  1.00 9.31  ? 211 PHE B C   1 
ATOM   3805 O  O   . PHE B 1 211 ? -9.490  -9.185  10.949  1.00 9.83  ? 211 PHE B O   1 
ATOM   3806 C  CB  . PHE B 1 211 ? -12.716 -8.525  10.824  1.00 8.41  ? 211 PHE B CB  1 
ATOM   3807 C  CG  . PHE B 1 211 ? -13.882 -7.640  11.149  1.00 10.12 ? 211 PHE B CG  1 
ATOM   3808 C  CD1 . PHE B 1 211 ? -14.199 -6.525  10.369  1.00 10.77 ? 211 PHE B CD1 1 
ATOM   3809 C  CD2 . PHE B 1 211 ? -14.664 -7.897  12.290  1.00 10.10 ? 211 PHE B CD2 1 
ATOM   3810 C  CE1 . PHE B 1 211 ? -15.299 -5.720  10.712  1.00 12.05 ? 211 PHE B CE1 1 
ATOM   3811 C  CE2 . PHE B 1 211 ? -15.732 -7.120  12.610  1.00 11.35 ? 211 PHE B CE2 1 
ATOM   3812 C  CZ  . PHE B 1 211 ? -16.061 -5.980  11.836  1.00 11.47 ? 211 PHE B CZ  1 
ATOM   3813 N  N   . ARG B 1 212 ? -10.562 -10.396 12.535  1.00 8.83  ? 212 ARG B N   1 
ATOM   3814 C  CA  . ARG B 1 212 ? -9.512  -11.417 12.533  1.00 10.08 ? 212 ARG B CA  1 
ATOM   3815 C  C   . ARG B 1 212 ? -9.421  -12.108 11.162  1.00 11.78 ? 212 ARG B C   1 
ATOM   3816 O  O   . ARG B 1 212 ? -8.294  -12.466 10.712  1.00 12.65 ? 212 ARG B O   1 
ATOM   3817 C  CB  . ARG B 1 212 ? -9.832  -12.488 13.578  1.00 9.37  ? 212 ARG B CB  1 
ATOM   3818 C  CG  . ARG B 1 212 ? -8.742  -13.610 13.677  1.00 10.77 ? 212 ARG B CG  1 
ATOM   3819 C  CD  . ARG B 1 212 ? -9.280  -14.648 14.670  1.00 13.51 ? 212 ARG B CD  1 
ATOM   3820 N  NE  . ARG B 1 212 ? -8.140  -15.548 14.905  1.00 15.73 ? 212 ARG B NE  1 
ATOM   3821 C  CZ  . ARG B 1 212 ? -8.188  -16.533 15.803  1.00 17.37 ? 212 ARG B CZ  1 
ATOM   3822 N  NH1 . ARG B 1 212 ? -9.320  -16.846 16.447  1.00 16.45 ? 212 ARG B NH1 1 
ATOM   3823 N  NH2 . ARG B 1 212 ? -7.082  -17.211 16.029  1.00 21.84 ? 212 ARG B NH2 1 
ATOM   3824 N  N   . ASN B 1 213 ? -10.572 -12.400 10.534  1.00 11.52 ? 213 ASN B N   1 
ATOM   3825 C  CA  . ASN B 1 213 ? -10.570 -13.250 9.329   1.00 12.74 ? 213 ASN B CA  1 
ATOM   3826 C  C   . ASN B 1 213 ? -10.607 -12.398 8.062   1.00 11.85 ? 213 ASN B C   1 
ATOM   3827 O  O   . ASN B 1 213 ? -11.355 -11.421 8.013   1.00 12.02 ? 213 ASN B O   1 
ATOM   3828 C  CB  . ASN B 1 213 ? -11.762 -14.224 9.341   1.00 15.34 ? 213 ASN B CB  1 
ATOM   3829 C  CG  . ASN B 1 213 ? -11.743 -15.143 10.595  1.00 17.29 ? 213 ASN B CG  1 
ATOM   3830 O  OD1 . ASN B 1 213 ? -12.705 -15.194 11.372  1.00 21.60 ? 213 ASN B OD1 1 
ATOM   3831 N  ND2 . ASN B 1 213 ? -10.641 -15.792 10.788  1.00 20.37 ? 213 ASN B ND2 1 
ATOM   3832 N  N   . PRO B 1 214 ? -9.796  -12.747 7.047   1.00 12.44 ? 214 PRO B N   1 
ATOM   3833 C  CA  . PRO B 1 214 ? -9.865  -12.000 5.804   1.00 11.76 ? 214 PRO B CA  1 
ATOM   3834 C  C   . PRO B 1 214 ? -11.057 -12.433 4.970   1.00 10.25 ? 214 PRO B C   1 
ATOM   3835 O  O   . PRO B 1 214 ? -11.622 -13.557 5.158   1.00 12.46 ? 214 PRO B O   1 
ATOM   3836 C  CB  . PRO B 1 214 ? -8.549  -12.377 5.093   1.00 11.66 ? 214 PRO B CB  1 
ATOM   3837 C  CG  . PRO B 1 214 ? -8.316  -13.809 5.560   1.00 14.18 ? 214 PRO B CG  1 
ATOM   3838 C  CD  . PRO B 1 214 ? -8.693  -13.744 7.057   1.00 13.94 ? 214 PRO B CD  1 
ATOM   3839 N  N   . VAL B 1 215 ? -11.405 -11.570 4.041   1.00 8.92  ? 215 VAL B N   1 
ATOM   3840 C  CA  . VAL B 1 215 ? -12.239 -11.970 2.905   1.00 9.30  ? 215 VAL B CA  1 
ATOM   3841 C  C   . VAL B 1 215 ? -11.359 -12.251 1.664   1.00 9.90  ? 215 VAL B C   1 
ATOM   3842 O  O   . VAL B 1 215 ? -10.145 -11.961 1.673   1.00 9.85  ? 215 VAL B O   1 
ATOM   3843 C  CB  . VAL B 1 215 ? -13.289 -10.878 2.557   1.00 10.27 ? 215 VAL B CB  1 
ATOM   3844 C  CG1 . VAL B 1 215 ? -14.243 -10.606 3.751   1.00 11.36 ? 215 VAL B CG1 1 
ATOM   3845 C  CG2 . VAL B 1 215 ? -12.654 -9.591  1.977   1.00 9.69  ? 215 VAL B CG2 1 
ATOM   3846 N  N   . GLN B 1 216 ? -11.931 -12.846 0.635   1.00 9.19  ? 216 GLN B N   1 
ATOM   3847 C  CA  . GLN B 1 216 ? -11.188 -13.154 -0.620  1.00 9.43  ? 216 GLN B CA  1 
ATOM   3848 C  C   . GLN B 1 216 ? -11.835 -12.391 -1.763  1.00 8.21  ? 216 GLN B C   1 
ATOM   3849 O  O   . GLN B 1 216 ? -13.064 -12.204 -1.849  1.00 9.05  ? 216 GLN B O   1 
ATOM   3850 C  CB  . GLN B 1 216 ? -11.246 -14.635 -1.044  1.00 11.00 ? 216 GLN B CB  1 
ATOM   3851 C  CG  . GLN B 1 216 ? -10.564 -15.554 -0.052  1.00 11.95 ? 216 GLN B CG  1 
ATOM   3852 C  CD  . GLN B 1 216 ? -10.539 -17.021 -0.479  1.00 14.71 ? 216 GLN B CD  1 
ATOM   3853 O  OE1 . GLN B 1 216 ? -11.107 -17.483 -1.507  1.00 13.31 ? 216 GLN B OE1 1 
ATOM   3854 N  NE2 . GLN B 1 216 ? -9.825  -17.779 0.349   1.00 20.34 ? 216 GLN B NE2 1 
ATOM   3855 N  N   . ILE B 1 217 ? -10.982 -11.831 -2.620  1.00 8.12  ? 217 ILE B N   1 
ATOM   3856 C  CA  . ILE B 1 217 ? -11.426 -11.348 -3.943  1.00 8.24  ? 217 ILE B CA  1 
ATOM   3857 C  C   . ILE B 1 217 ? -10.431 -11.998 -4.965  1.00 8.35  ? 217 ILE B C   1 
ATOM   3858 O  O   . ILE B 1 217 ? -9.326  -12.401 -4.575  1.00 8.34  ? 217 ILE B O   1 
ATOM   3859 C  CB  . ILE B 1 217 ? -11.453 -9.773  -4.068  1.00 8.49  ? 217 ILE B CB  1 
ATOM   3860 C  CG1 . ILE B 1 217 ? -10.060 -9.202  -4.132  1.00 9.01  ? 217 ILE B CG1 1 
ATOM   3861 C  CG2 . ILE B 1 217 ? -12.339 -9.194  -2.932  1.00 10.11 ? 217 ILE B CG2 1 
ATOM   3862 C  CD1 . ILE B 1 217 ? -9.974  -7.663  -4.182  1.00 9.37  ? 217 ILE B CD1 1 
ATOM   3863 N  N   . SER B 1 218 ? -10.820 -12.087 -6.243  1.00 8.94  ? 218 SER B N   1 
ATOM   3864 C  CA  . SER B 1 218 ? -9.952  -12.792 -7.182  1.00 9.58  ? 218 SER B CA  1 
ATOM   3865 C  C   . SER B 1 218 ? -8.816  -11.992 -7.709  1.00 10.55 ? 218 SER B C   1 
ATOM   3866 O  O   . SER B 1 218 ? -8.813  -10.724 -7.565  1.00 9.55  ? 218 SER B O   1 
ATOM   3867 C  CB  . SER B 1 218 ? -10.774 -13.331 -8.352  1.00 9.45  ? 218 SER B CB  1 
ATOM   3868 O  OG  . SER B 1 218 ? -11.221 -12.206 -9.176  1.00 10.97 ? 218 SER B OG  1 
ATOM   3869 N  N   A GLN B 1 219 ? -7.848  -12.670 -8.328  0.50 10.53 ? 219 GLN B N   1 
ATOM   3870 N  N   B GLN B 1 219 ? -7.844  -12.700 -8.298  0.50 10.74 ? 219 GLN B N   1 
ATOM   3871 C  CA  A GLN B 1 219 ? -6.705  -11.992 -8.952  0.50 10.89 ? 219 GLN B CA  1 
ATOM   3872 C  CA  B GLN B 1 219 ? -6.684  -12.163 -9.046  0.50 11.19 ? 219 GLN B CA  1 
ATOM   3873 C  C   A GLN B 1 219 ? -7.251  -11.009 -9.999  0.50 10.90 ? 219 GLN B C   1 
ATOM   3874 C  C   B GLN B 1 219 ? -7.179  -11.107 -10.030 0.50 11.12 ? 219 GLN B C   1 
ATOM   3875 O  O   A GLN B 1 219 ? -6.733  -9.899  -10.132 0.50 11.23 ? 219 GLN B O   1 
ATOM   3876 O  O   B GLN B 1 219 ? -6.522  -10.053 -10.155 0.50 11.16 ? 219 GLN B O   1 
ATOM   3877 C  CB  A GLN B 1 219 ? -5.703  -12.985 -9.558  0.50 11.13 ? 219 GLN B CB  1 
ATOM   3878 C  CB  B GLN B 1 219 ? -6.025  -13.339 -9.796  0.50 11.57 ? 219 GLN B CB  1 
ATOM   3879 C  CG  A GLN B 1 219 ? -4.422  -12.299 -10.120 0.50 13.87 ? 219 GLN B CG  1 
ATOM   3880 C  CG  B GLN B 1 219 ? -4.646  -13.217 -10.473 0.50 15.94 ? 219 GLN B CG  1 
ATOM   3881 C  CD  A GLN B 1 219 ? -4.565  -11.759 -11.541 0.50 14.97 ? 219 GLN B CD  1 
ATOM   3882 C  CD  B GLN B 1 219 ? -4.124  -14.620 -10.840 0.50 15.85 ? 219 GLN B CD  1 
ATOM   3883 O  OE1 A GLN B 1 219 ? -3.737  -10.960 -11.976 0.50 16.04 ? 219 GLN B OE1 1 
ATOM   3884 O  OE1 B GLN B 1 219 ? -3.545  -15.411 -9.983  0.50 17.33 ? 219 GLN B OE1 1 
ATOM   3885 N  NE2 A GLN B 1 219 ? -5.595  -12.162 -12.256 0.50 16.11 ? 219 GLN B NE2 1 
ATOM   3886 N  NE2 B GLN B 1 219 ? -4.464  -15.011 -12.057 0.50 18.01 ? 219 GLN B NE2 1 
ATOM   3887 N  N   . GLU B 1 220 ? -8.282  -11.397 -10.738 1.00 11.84 ? 220 GLU B N   1 
ATOM   3888 C  CA  . GLU B 1 220 ? -8.801  -10.473 -11.802 1.00 12.25 ? 220 GLU B CA  1 
ATOM   3889 C  C   . GLU B 1 220 ? -9.422  -9.205  -11.151 1.00 11.57 ? 220 GLU B C   1 
ATOM   3890 O  O   . GLU B 1 220 ? -9.278  -8.045  -11.676 1.00 11.32 ? 220 GLU B O   1 
ATOM   3891 C  CB  . GLU B 1 220 ? -9.848  -11.173 -12.647 1.00 14.59 ? 220 GLU B CB  1 
ATOM   3892 C  CG  . GLU B 1 220 ? -9.154  -12.295 -13.474 1.00 15.12 ? 220 GLU B CG  1 
ATOM   3893 C  CD  . GLU B 1 220 ? -8.931  -13.651 -12.831 1.00 19.87 ? 220 GLU B CD  1 
ATOM   3894 O  OE1 . GLU B 1 220 ? -9.303  -13.886 -11.671 1.00 18.24 ? 220 GLU B OE1 1 
ATOM   3895 O  OE2 . GLU B 1 220 ? -8.349  -14.515 -13.570 1.00 22.00 ? 220 GLU B OE2 1 
ATOM   3896 N  N   . GLN B 1 221 ? -10.073 -9.386  -10.002 1.00 9.91  ? 221 GLN B N   1 
ATOM   3897 C  CA  . GLN B 1 221 ? -10.638 -8.231  -9.291  1.00 9.67  ? 221 GLN B CA  1 
ATOM   3898 C  C   . GLN B 1 221 ? -9.529  -7.347  -8.740  1.00 8.51  ? 221 GLN B C   1 
ATOM   3899 O  O   . GLN B 1 221 ? -9.541  -6.074  -8.861  1.00 8.23  ? 221 GLN B O   1 
ATOM   3900 C  CB  . GLN B 1 221 ? -11.522 -8.671  -8.131  1.00 8.60  ? 221 GLN B CB  1 
ATOM   3901 C  CG  . GLN B 1 221 ? -12.831 -9.249  -8.630  1.00 8.60  ? 221 GLN B CG  1 
ATOM   3902 C  CD  . GLN B 1 221 ? -13.745 -9.658  -7.473  1.00 8.62  ? 221 GLN B CD  1 
ATOM   3903 O  OE1 . GLN B 1 221 ? -13.404 -10.639 -6.749  1.00 10.65 ? 221 GLN B OE1 1 
ATOM   3904 N  NE2 . GLN B 1 221 ? -14.917 -8.981  -7.272  1.00 8.88  ? 221 GLN B NE2 1 
ATOM   3905 N  N   . LEU B 1 222 ? -8.485  -7.949  -8.208  1.00 9.42  ? 222 LEU B N   1 
ATOM   3906 C  CA  . LEU B 1 222 ? -7.339  -7.129  -7.712  1.00 8.99  ? 222 LEU B CA  1 
ATOM   3907 C  C   . LEU B 1 222 ? -6.686  -6.397  -8.888  1.00 8.92  ? 222 LEU B C   1 
ATOM   3908 O  O   . LEU B 1 222 ? -6.282  -5.249  -8.751  1.00 9.94  ? 222 LEU B O   1 
ATOM   3909 C  CB  . LEU B 1 222 ? -6.308  -8.079  -7.018  1.00 10.02 ? 222 LEU B CB  1 
ATOM   3910 C  CG  . LEU B 1 222 ? -6.730  -8.443  -5.600  1.00 9.93  ? 222 LEU B CG  1 
ATOM   3911 C  CD1 . LEU B 1 222 ? -6.079  -9.771  -5.189  1.00 12.95 ? 222 LEU B CD1 1 
ATOM   3912 C  CD2 . LEU B 1 222 ? -6.349  -7.195  -4.716  1.00 10.86 ? 222 LEU B CD2 1 
ATOM   3913 N  N   . LEU B 1 223 ? -6.522  -7.079  -10.044 1.00 9.42  ? 223 LEU B N   1 
ATOM   3914 C  CA  . LEU B 1 223 ? -5.886  -6.468  -11.223 1.00 11.02 ? 223 LEU B CA  1 
ATOM   3915 C  C   . LEU B 1 223 ? -6.703  -5.273  -11.660 1.00 9.90  ? 223 LEU B C   1 
ATOM   3916 O  O   . LEU B 1 223 ? -6.096  -4.261  -11.991 1.00 10.10 ? 223 LEU B O   1 
ATOM   3917 C  CB  . LEU B 1 223 ? -5.725  -7.525  -12.347 1.00 11.69 ? 223 LEU B CB  1 
ATOM   3918 C  CG  . LEU B 1 223 ? -4.868  -6.905  -13.495 1.00 14.35 ? 223 LEU B CG  1 
ATOM   3919 C  CD1 . LEU B 1 223 ? -3.417  -6.637  -13.073 1.00 15.52 ? 223 LEU B CD1 1 
ATOM   3920 C  CD2 . LEU B 1 223 ? -4.965  -7.850  -14.689 1.00 17.48 ? 223 LEU B CD2 1 
ATOM   3921 N  N   . ALA B 1 224 ? -8.052  -5.392  -11.713 1.00 10.76 ? 224 ALA B N   1 
ATOM   3922 C  CA  . ALA B 1 224 ? -8.892  -4.256  -12.090 1.00 10.90 ? 224 ALA B CA  1 
ATOM   3923 C  C   . ALA B 1 224 ? -8.690  -3.126  -11.117 1.00 11.54 ? 224 ALA B C   1 
ATOM   3924 O  O   . ALA B 1 224 ? -8.430  -2.021  -11.532 1.00 12.48 ? 224 ALA B O   1 
ATOM   3925 C  CB  . ALA B 1 224 ? -10.332 -4.680  -12.152 1.00 12.90 ? 224 ALA B CB  1 
ATOM   3926 N  N   . LEU B 1 225 ? -8.679  -3.416  -9.810  1.00 10.92 ? 225 LEU B N   1 
ATOM   3927 C  CA  . LEU B 1 225 ? -8.540  -2.350  -8.824  1.00 10.66 ? 225 LEU B CA  1 
ATOM   3928 C  C   . LEU B 1 225 ? -7.178  -1.622  -8.986  1.00 11.02 ? 225 LEU B C   1 
ATOM   3929 O  O   . LEU B 1 225 ? -7.063  -0.398  -8.746  1.00 13.16 ? 225 LEU B O   1 
ATOM   3930 C  CB  . LEU B 1 225 ? -8.714  -2.993  -7.396  1.00 10.51 ? 225 LEU B CB  1 
ATOM   3931 C  CG  . LEU B 1 225 ? -8.498  -2.054  -6.200  1.00 10.97 ? 225 LEU B CG  1 
ATOM   3932 C  CD1 . LEU B 1 225 ? -9.516  -0.883  -6.176  1.00 11.93 ? 225 LEU B CD1 1 
ATOM   3933 C  CD2 . LEU B 1 225 ? -8.532  -2.887  -4.892  1.00 11.95 ? 225 LEU B CD2 1 
ATOM   3934 N  N   . GLU B 1 226 ? -6.155  -2.407  -9.270  1.00 9.84  ? 226 GLU B N   1 
ATOM   3935 C  CA  . GLU B 1 226 ? -4.776  -1.944  -9.315  1.00 9.12  ? 226 GLU B CA  1 
ATOM   3936 C  C   . GLU B 1 226 ? -4.469  -1.232  -10.640 1.00 9.86  ? 226 GLU B C   1 
ATOM   3937 O  O   . GLU B 1 226 ? -3.407  -0.661  -10.736 1.00 13.09 ? 226 GLU B O   1 
ATOM   3938 C  CB  . GLU B 1 226 ? -3.797  -3.135  -9.201  1.00 9.13  ? 226 GLU B CB  1 
ATOM   3939 C  CG  . GLU B 1 226 ? -3.812  -3.722  -7.770  1.00 8.51  ? 226 GLU B CG  1 
ATOM   3940 C  CD  . GLU B 1 226 ? -3.435  -5.192  -7.772  1.00 9.97  ? 226 GLU B CD  1 
ATOM   3941 O  OE1 . GLU B 1 226 ? -3.174  -5.779  -8.841  1.00 11.71 ? 226 GLU B OE1 1 
ATOM   3942 O  OE2 . GLU B 1 226 ? -3.467  -5.786  -6.714  1.00 11.43 ? 226 GLU B OE2 1 
ATOM   3943 N  N   . THR B 1 227 ? -5.290  -1.410  -11.657 1.00 9.35  ? 227 THR B N   1 
ATOM   3944 C  CA  . THR B 1 227 ? -5.035  -0.810  -12.965 1.00 10.84 ? 227 THR B CA  1 
ATOM   3945 C  C   . THR B 1 227 ? -6.081  0.197   -13.363 1.00 11.52 ? 227 THR B C   1 
ATOM   3946 O  O   . THR B 1 227 ? -5.770  0.972   -14.315 1.00 14.65 ? 227 THR B O   1 
ATOM   3947 C  CB  . THR B 1 227 ? -4.932  -1.867  -14.109 1.00 11.44 ? 227 THR B CB  1 
ATOM   3948 O  OG1 . THR B 1 227 ? -6.168  -2.576  -14.233 1.00 10.35 ? 227 THR B OG1 1 
ATOM   3949 C  CG2 . THR B 1 227 ? -3.750  -2.867  -13.932 1.00 10.60 ? 227 THR B CG2 1 
ATOM   3950 N  N   . ALA B 1 228 ? -7.221  0.309   -12.691 1.00 11.41 ? 228 ALA B N   1 
ATOM   3951 C  CA  . ALA B 1 228 ? -8.277  1.213   -13.187 1.00 11.90 ? 228 ALA B CA  1 
ATOM   3952 C  C   . ALA B 1 228 ? -8.074  2.726   -12.897 1.00 11.31 ? 228 ALA B C   1 
ATOM   3953 O  O   . ALA B 1 228 ? -8.634  3.568   -13.619 1.00 12.55 ? 228 ALA B O   1 
ATOM   3954 C  CB  . ALA B 1 228 ? -9.580  0.760   -12.614 1.00 12.50 ? 228 ALA B CB  1 
ATOM   3955 N  N   . LEU B 1 229 ? -7.318  3.069   -11.879 1.00 10.21 ? 229 LEU B N   1 
ATOM   3956 C  CA  . LEU B 1 229 ? -7.486  4.389   -11.257 1.00 9.99  ? 229 LEU B CA  1 
ATOM   3957 C  C   . LEU B 1 229 ? -6.185  5.152   -11.290 1.00 8.98  ? 229 LEU B C   1 
ATOM   3958 O  O   . LEU B 1 229 ? -5.093  4.586   -11.230 1.00 9.64  ? 229 LEU B O   1 
ATOM   3959 C  CB  . LEU B 1 229 ? -7.899  4.262   -9.765  1.00 11.27 ? 229 LEU B CB  1 
ATOM   3960 C  CG  . LEU B 1 229 ? -9.190  3.406   -9.575  1.00 11.71 ? 229 LEU B CG  1 
ATOM   3961 C  CD1 . LEU B 1 229 ? -9.442  3.181   -8.060  1.00 11.93 ? 229 LEU B CD1 1 
ATOM   3962 C  CD2 . LEU B 1 229 ? -10.371 4.076   -10.258 1.00 13.45 ? 229 LEU B CD2 1 
ATOM   3963 N  N   . TYR B 1 230 ? -6.352  6.454   -11.394 1.00 9.08  ? 230 TYR B N   1 
ATOM   3964 C  CA  . TYR B 1 230 ? -5.271  7.496   -11.400 1.00 9.77  ? 230 TYR B CA  1 
ATOM   3965 C  C   . TYR B 1 230 ? -5.472  8.458   -10.255 1.00 10.22 ? 230 TYR B C   1 
ATOM   3966 O  O   . TYR B 1 230 ? -6.606  8.837   -9.926  1.00 9.87  ? 230 TYR B O   1 
ATOM   3967 C  CB  . TYR B 1 230 ? -5.257  8.200   -12.794 1.00 9.69  ? 230 TYR B CB  1 
ATOM   3968 C  CG  . TYR B 1 230 ? -4.676  7.275   -13.814 1.00 9.96  ? 230 TYR B CG  1 
ATOM   3969 C  CD1 . TYR B 1 230 ? -3.330  7.285   -14.089 1.00 12.36 ? 230 TYR B CD1 1 
ATOM   3970 C  CD2 . TYR B 1 230 ? -5.505  6.342   -14.419 1.00 11.87 ? 230 TYR B CD2 1 
ATOM   3971 C  CE1 . TYR B 1 230 ? -2.786  6.318   -14.948 1.00 13.24 ? 230 TYR B CE1 1 
ATOM   3972 C  CE2 . TYR B 1 230 ? -4.972  5.348   -15.289 1.00 13.63 ? 230 TYR B CE2 1 
ATOM   3973 C  CZ  . TYR B 1 230 ? -3.639  5.379   -15.527 1.00 13.69 ? 230 TYR B CZ  1 
ATOM   3974 O  OH  . TYR B 1 230 ? -3.087  4.381   -16.365 1.00 18.12 ? 230 TYR B OH  1 
ATOM   3975 N  N   . CYS B 1 231 ? -4.368  8.909   -9.710  1.00 8.75  ? 231 CYS B N   1 
ATOM   3976 C  CA  . CYS B 1 231 ? -4.403  9.932   -8.660  1.00 9.07  ? 231 CYS B CA  1 
ATOM   3977 C  C   . CYS B 1 231 ? -4.694  11.323  -9.254  1.00 8.75  ? 231 CYS B C   1 
ATOM   3978 O  O   . CYS B 1 231 ? -5.040  12.260  -8.507  1.00 10.32 ? 231 CYS B O   1 
ATOM   3979 C  CB  . CYS B 1 231 ? -3.045  10.045  -8.011  1.00 8.85  ? 231 CYS B CB  1 
ATOM   3980 S  SG  . CYS B 1 231 ? -2.534  8.559   -7.097  1.00 10.51 ? 231 CYS B SG  1 
ATOM   3981 N  N   . THR B 1 232 ? -4.489  11.436  -10.548 1.00 9.40  ? 232 THR B N   1 
ATOM   3982 C  CA  . THR B 1 232 ? -4.456  12.776  -11.205 1.00 9.02  ? 232 THR B CA  1 
ATOM   3983 C  C   . THR B 1 232 ? -5.754  12.995  -11.994 1.00 9.33  ? 232 THR B C   1 
ATOM   3984 O  O   . THR B 1 232 ? -6.495  12.001  -12.352 1.00 9.86  ? 232 THR B O   1 
ATOM   3985 C  CB  . THR B 1 232 ? -3.210  12.828  -12.128 1.00 9.32  ? 232 THR B CB  1 
ATOM   3986 O  OG1 . THR B 1 232 ? -3.059  11.528  -12.689 1.00 10.01 ? 232 THR B OG1 1 
ATOM   3987 C  CG2 . THR B 1 232 ? -1.944  13.031  -11.312 1.00 9.56  ? 232 THR B CG2 1 
ATOM   3988 N  N   . HIS B 1 233 ? -6.014  14.296  -12.291 1.00 10.16 ? 233 HIS B N   1 
ATOM   3989 C  CA  . HIS B 1 233 ? -7.093  14.618  -13.192 1.00 11.26 ? 233 HIS B CA  1 
ATOM   3990 C  C   . HIS B 1 233 ? -6.960  14.047  -14.601 1.00 10.88 ? 233 HIS B C   1 
ATOM   3991 O  O   . HIS B 1 233 ? -5.865  13.724  -15.059 1.00 11.25 ? 233 HIS B O   1 
ATOM   3992 C  CB  . HIS B 1 233 ? -7.258  16.134  -13.282 1.00 12.89 ? 233 HIS B CB  1 
ATOM   3993 C  CG  . HIS B 1 233 ? -7.702  16.727  -11.997 1.00 16.02 ? 233 HIS B CG  1 
ATOM   3994 N  ND1 . HIS B 1 233 ? -6.881  17.419  -11.224 1.00 23.52 ? 233 HIS B ND1 1 
ATOM   3995 C  CD2 . HIS B 1 233 ? -8.899  16.672  -11.346 1.00 17.63 ? 233 HIS B CD2 1 
ATOM   3996 C  CE1 . HIS B 1 233 ? -7.531  17.798  -10.098 1.00 23.06 ? 233 HIS B CE1 1 
ATOM   3997 N  NE2 . HIS B 1 233 ? -8.747  17.345  -10.172 1.00 19.13 ? 233 HIS B NE2 1 
ATOM   3998 N  N   . MET B 1 234 ? -8.114  13.881  -15.268 1.00 10.49 ? 234 MET B N   1 
ATOM   3999 C  CA  . MET B 1 234 ? -8.178  13.415  -16.659 1.00 11.60 ? 234 MET B CA  1 
ATOM   4000 C  C   . MET B 1 234 ? -7.264  14.180  -17.581 1.00 12.05 ? 234 MET B C   1 
ATOM   4001 O  O   . MET B 1 234 ? -6.659  13.590  -18.492 1.00 13.29 ? 234 MET B O   1 
ATOM   4002 C  CB  . MET B 1 234 ? -9.617  13.412  -17.134 1.00 13.82 ? 234 MET B CB  1 
ATOM   4003 C  CG  . MET B 1 234 ? -9.747  12.699  -18.489 1.00 16.31 ? 234 MET B CG  1 
ATOM   4004 S  SD  . MET B 1 234 ? -11.560 12.436  -18.716 1.00 23.61 ? 234 MET B SD  1 
ATOM   4005 C  CE  . MET B 1 234 ? -11.579 11.705  -20.372 1.00 23.78 ? 234 MET B CE  1 
ATOM   4006 N  N   . ASP B 1 235 ? -7.104  15.460  -17.298 1.00 12.65 ? 235 ASP B N   1 
ATOM   4007 C  CA  . ASP B 1 235 ? -6.279  16.284  -18.214 1.00 14.19 ? 235 ASP B CA  1 
ATOM   4008 C  C   . ASP B 1 235 ? -4.877  16.564  -17.735 1.00 15.21 ? 235 ASP B C   1 
ATOM   4009 O  O   . ASP B 1 235 ? -4.196  17.437  -18.288 1.00 15.41 ? 235 ASP B O   1 
ATOM   4010 C  CB  . ASP B 1 235 ? -7.003  17.617  -18.504 1.00 17.74 ? 235 ASP B CB  1 
ATOM   4011 C  CG  . ASP B 1 235 ? -7.052  18.537  -17.292 1.00 20.74 ? 235 ASP B CG  1 
ATOM   4012 O  OD1 . ASP B 1 235 ? -6.668  18.148  -16.172 1.00 24.14 ? 235 ASP B OD1 1 
ATOM   4013 O  OD2 . ASP B 1 235 ? -7.548  19.684  -17.439 1.00 29.01 ? 235 ASP B OD2 1 
ATOM   4014 N  N   . ASP B 1 236 ? -4.374  15.806  -16.762 1.00 11.81 ? 236 ASP B N   1 
ATOM   4015 C  CA  . ASP B 1 236 ? -3.070  16.113  -16.195 1.00 11.67 ? 236 ASP B CA  1 
ATOM   4016 C  C   . ASP B 1 236 ? -1.999  15.620  -17.125 1.00 11.57 ? 236 ASP B C   1 
ATOM   4017 O  O   . ASP B 1 236 ? -1.986  14.466  -17.477 1.00 10.56 ? 236 ASP B O   1 
ATOM   4018 C  CB  . ASP B 1 236 ? -2.914  15.411  -14.811 1.00 11.84 ? 236 ASP B CB  1 
ATOM   4019 C  CG  . ASP B 1 236 ? -1.831  16.089  -13.976 1.00 13.22 ? 236 ASP B CG  1 
ATOM   4020 O  OD1 . ASP B 1 236 ? -0.698  16.326  -14.496 1.00 12.90 ? 236 ASP B OD1 1 
ATOM   4021 O  OD2 . ASP B 1 236 ? -2.081  16.394  -12.781 1.00 15.32 ? 236 ASP B OD2 1 
ATOM   4022 N  N   . PRO B 1 237 ? -1.024  16.444  -17.519 1.00 11.30 ? 237 PRO B N   1 
ATOM   4023 C  CA  . PRO B 1 237 ? 0.051   16.020  -18.385 1.00 12.24 ? 237 PRO B CA  1 
ATOM   4024 C  C   . PRO B 1 237 ? 1.129   15.207  -17.653 1.00 11.92 ? 237 PRO B C   1 
ATOM   4025 O  O   . PRO B 1 237 ? 2.008   14.686  -18.306 1.00 12.43 ? 237 PRO B O   1 
ATOM   4026 C  CB  . PRO B 1 237 ? 0.653   17.384  -18.838 1.00 12.86 ? 237 PRO B CB  1 
ATOM   4027 C  CG  . PRO B 1 237 ? 0.372   18.278  -17.633 1.00 13.27 ? 237 PRO B CG  1 
ATOM   4028 C  CD  . PRO B 1 237 ? -1.046  17.893  -17.327 1.00 11.56 ? 237 PRO B CD  1 
ATOM   4029 N  N   A SER B 1 238 ? 0.980   15.022  -16.330 0.50 10.34 ? 238 SER B N   1 
ATOM   4030 N  N   B SER B 1 238 ? 1.098   15.006  -16.319 0.50 10.33 ? 238 SER B N   1 
ATOM   4031 C  CA  A SER B 1 238 ? 1.882   14.218  -15.518 0.50 10.70 ? 238 SER B CA  1 
ATOM   4032 C  CA  B SER B 1 238 ? 2.038   14.024  -15.696 0.50 10.49 ? 238 SER B CA  1 
ATOM   4033 C  C   A SER B 1 238 ? 0.998   13.182  -14.778 0.50 10.15 ? 238 SER B C   1 
ATOM   4034 C  C   B SER B 1 238 ? 1.209   13.081  -14.844 0.50 10.24 ? 238 SER B C   1 
ATOM   4035 O  O   A SER B 1 238 ? 0.740   13.307  -13.574 0.50 9.66  ? 238 SER B O   1 
ATOM   4036 O  O   B SER B 1 238 ? 1.195   13.193  -13.615 0.50 10.16 ? 238 SER B O   1 
ATOM   4037 C  CB  A SER B 1 238 ? 2.577   15.116  -14.483 0.50 12.15 ? 238 SER B CB  1 
ATOM   4038 C  CB  B SER B 1 238 ? 3.073   14.652  -14.767 0.50 13.00 ? 238 SER B CB  1 
ATOM   4039 O  OG  A SER B 1 238 ? 3.728   14.408  -14.031 0.50 15.64 ? 238 SER B OG  1 
ATOM   4040 O  OG  B SER B 1 238 ? 3.615   15.835  -15.290 0.50 14.01 ? 238 SER B OG  1 
ATOM   4041 N  N   . PRO B 1 239 ? 0.474   12.202  -15.506 1.00 10.45 ? 239 PRO B N   1 
ATOM   4042 C  CA  . PRO B 1 239 ? -0.428  11.232  -14.826 1.00 10.73 ? 239 PRO B CA  1 
ATOM   4043 C  C   . PRO B 1 239 ? 0.311   10.330  -13.856 1.00 9.89  ? 239 PRO B C   1 
ATOM   4044 O  O   . PRO B 1 239 ? 1.572   10.030  -13.975 1.00 10.06 ? 239 PRO B O   1 
ATOM   4045 C  CB  . PRO B 1 239 ? -0.925  10.312  -15.950 1.00 12.40 ? 239 PRO B CB  1 
ATOM   4046 C  CG  . PRO B 1 239 ? -0.321  10.821  -17.203 1.00 15.22 ? 239 PRO B CG  1 
ATOM   4047 C  CD  . PRO B 1 239 ? 0.578   11.990  -16.946 1.00 11.57 ? 239 PRO B CD  1 
ATOM   4048 N  N   . ARG B 1 240 ? -0.432  9.956   -12.775 1.00 9.07  ? 240 ARG B N   1 
ATOM   4049 C  CA  . ARG B 1 240 ? 0.195   9.093   -11.753 1.00 9.79  ? 240 ARG B CA  1 
ATOM   4050 C  C   . ARG B 1 240 ? -0.834  8.002   -11.468 1.00 9.32  ? 240 ARG B C   1 
ATOM   4051 O  O   . ARG B 1 240 ? -1.953  8.312   -11.086 1.00 10.24 ? 240 ARG B O   1 
ATOM   4052 C  CB  . ARG B 1 240 ? 0.438   9.803   -10.417 1.00 9.95  ? 240 ARG B CB  1 
ATOM   4053 C  CG  . ARG B 1 240 ? 1.613   10.799  -10.614 1.00 11.78 ? 240 ARG B CG  1 
ATOM   4054 C  CD  . ARG B 1 240 ? 1.882   11.603  -9.331  1.00 12.54 ? 240 ARG B CD  1 
ATOM   4055 N  NE  . ARG B 1 240 ? 0.841   12.548  -9.048  1.00 14.23 ? 240 ARG B NE  1 
ATOM   4056 C  CZ  . ARG B 1 240 ? -0.025  12.439  -8.021  1.00 13.20 ? 240 ARG B CZ  1 
ATOM   4057 N  NH1 . ARG B 1 240 ? -0.013  11.357  -7.230  1.00 12.51 ? 240 ARG B NH1 1 
ATOM   4058 N  NH2 . ARG B 1 240 ? -0.960  13.350  -7.886  1.00 14.85 ? 240 ARG B NH2 1 
ATOM   4059 N  N   . GLU B 1 241 ? -0.428  6.739   -11.670 1.00 9.00  ? 241 GLU B N   1 
ATOM   4060 C  CA  . GLU B 1 241 ? -1.334  5.629   -11.319 1.00 10.10 ? 241 GLU B CA  1 
ATOM   4061 C  C   . GLU B 1 241 ? -1.635  5.601   -9.797  1.00 8.79  ? 241 GLU B C   1 
ATOM   4062 O  O   . GLU B 1 241 ? -0.757  5.742   -8.957  1.00 9.26  ? 241 GLU B O   1 
ATOM   4063 C  CB  . GLU B 1 241 ? -0.594  4.369   -11.649 1.00 11.70 ? 241 GLU B CB  1 
ATOM   4064 C  CG  . GLU B 1 241 ? -0.521  4.264   -13.164 1.00 12.65 ? 241 GLU B CG  1 
ATOM   4065 C  CD  . GLU B 1 241 ? 0.401   3.169   -13.567 1.00 18.77 ? 241 GLU B CD  1 
ATOM   4066 O  OE1 . GLU B 1 241 ? 1.584   3.229   -13.172 1.00 23.90 ? 241 GLU B OE1 1 
ATOM   4067 O  OE2 . GLU B 1 241 ? -0.020  2.269   -14.281 1.00 25.91 ? 241 GLU B OE2 1 
ATOM   4068 N  N   . MET B 1 242 ? -2.883  5.247   -9.463  1.00 7.96  ? 242 MET B N   1 
ATOM   4069 C  CA  . MET B 1 242 ? -3.196  5.069   -8.042  1.00 8.40  ? 242 MET B CA  1 
ATOM   4070 C  C   . MET B 1 242 ? -2.965  3.572   -7.669  1.00 7.74  ? 242 MET B C   1 
ATOM   4071 O  O   . MET B 1 242 ? -3.810  2.632   -7.866  1.00 8.30  ? 242 MET B O   1 
ATOM   4072 C  CB  . MET B 1 242 ? -4.645  5.501   -7.825  1.00 9.13  ? 242 MET B CB  1 
ATOM   4073 C  CG  . MET B 1 242 ? -5.057  5.523   -6.320  1.00 8.34  ? 242 MET B CG  1 
ATOM   4074 S  SD  . MET B 1 242 ? -6.824  5.787   -6.059  1.00 9.02  ? 242 MET B SD  1 
ATOM   4075 C  CE  . MET B 1 242 ? -6.932  7.539   -6.537  1.00 9.87  ? 242 MET B CE  1 
ATOM   4076 N  N   . ILE B 1 243 ? -1.739  3.415   -7.151  1.00 7.66  ? 243 ILE B N   1 
ATOM   4077 C  CA  . ILE B 1 243 ? -1.173  2.117   -6.790  1.00 8.00  ? 243 ILE B CA  1 
ATOM   4078 C  C   . ILE B 1 243 ? -0.401  2.308   -5.478  1.00 8.07  ? 243 ILE B C   1 
ATOM   4079 O  O   . ILE B 1 243 ? 0.100   3.432   -5.136  1.00 8.55  ? 243 ILE B O   1 
ATOM   4080 C  CB  . ILE B 1 243 ? -0.263  1.491   -7.854  1.00 9.31  ? 243 ILE B CB  1 
ATOM   4081 C  CG1 . ILE B 1 243 ? 0.844   2.490   -8.190  1.00 8.85  ? 243 ILE B CG1 1 
ATOM   4082 C  CG2 . ILE B 1 243 ? -1.067  1.032   -9.075  1.00 9.37  ? 243 ILE B CG2 1 
ATOM   4083 C  CD1 . ILE B 1 243 ? 1.851   1.920   -9.171  1.00 10.76 ? 243 ILE B CD1 1 
ATOM   4084 N  N   . ASN B 1 244 ? -0.257  1.201   -4.746  1.00 7.20  ? 244 ASN B N   1 
ATOM   4085 C  CA  . ASN B 1 244 ? 0.557   1.167   -3.550  1.00 8.31  ? 244 ASN B CA  1 
ATOM   4086 C  C   . ASN B 1 244 ? 0.186   2.307   -2.579  1.00 8.18  ? 244 ASN B C   1 
ATOM   4087 O  O   . ASN B 1 244 ? 1.005   2.935   -1.936  1.00 7.96  ? 244 ASN B O   1 
ATOM   4088 C  CB  . ASN B 1 244 ? 2.076   1.305   -3.868  1.00 9.09  ? 244 ASN B CB  1 
ATOM   4089 C  CG  . ASN B 1 244 ? 2.510   0.277   -4.855  1.00 10.87 ? 244 ASN B CG  1 
ATOM   4090 O  OD1 . ASN B 1 244 ? 2.121   -0.905  -4.791  1.00 12.11 ? 244 ASN B OD1 1 
ATOM   4091 N  ND2 . ASN B 1 244 ? 3.243   0.754   -5.889  1.00 12.10 ? 244 ASN B ND2 1 
ATOM   4092 N  N   . ASN B 1 245 ? -1.141  2.488   -2.428  1.00 8.03  ? 245 ASN B N   1 
ATOM   4093 C  CA  . ASN B 1 245 ? -1.676  3.522   -1.539  1.00 7.23  ? 245 ASN B CA  1 
ATOM   4094 C  C   . ASN B 1 245 ? -1.951  3.022   -0.128  1.00 7.92  ? 245 ASN B C   1 
ATOM   4095 O  O   . ASN B 1 245 ? -3.071  3.076   0.387   1.00 8.61  ? 245 ASN B O   1 
ATOM   4096 C  CB  . ASN B 1 245 ? -2.983  4.122   -2.170  1.00 8.47  ? 245 ASN B CB  1 
ATOM   4097 C  CG  . ASN B 1 245 ? -4.076  3.104   -2.376  1.00 7.75  ? 245 ASN B CG  1 
ATOM   4098 O  OD1 . ASN B 1 245 ? -3.879  1.912   -2.471  1.00 8.49  ? 245 ASN B OD1 1 
ATOM   4099 N  ND2 . ASN B 1 245 ? -5.318  3.631   -2.527  1.00 9.01  ? 245 ASN B ND2 1 
ATOM   4100 N  N   . PHE B 1 246 ? -0.899  2.520   0.484   1.00 7.29  ? 246 PHE B N   1 
ATOM   4101 C  CA  . PHE B 1 246 ? -0.943  2.118   1.894   1.00 7.16  ? 246 PHE B CA  1 
ATOM   4102 C  C   . PHE B 1 246 ? 0.273   2.668   2.607   1.00 7.43  ? 246 PHE B C   1 
ATOM   4103 O  O   . PHE B 1 246 ? 1.341   2.874   1.973   1.00 7.08  ? 246 PHE B O   1 
ATOM   4104 C  CB  . PHE B 1 246 ? -0.923  0.563   1.935   1.00 7.57  ? 246 PHE B CB  1 
ATOM   4105 C  CG  . PHE B 1 246 ? 0.360   -0.095  1.331   1.00 8.02  ? 246 PHE B CG  1 
ATOM   4106 C  CD1 . PHE B 1 246 ? 1.475   -0.457  2.153   1.00 9.75  ? 246 PHE B CD1 1 
ATOM   4107 C  CD2 . PHE B 1 246 ? 0.430   -0.299  -0.021  1.00 8.36  ? 246 PHE B CD2 1 
ATOM   4108 C  CE1 . PHE B 1 246 ? 2.601   -1.003  1.559   1.00 10.53 ? 246 PHE B CE1 1 
ATOM   4109 C  CE2 . PHE B 1 246 ? 1.579   -0.858  -0.626  1.00 9.59  ? 246 PHE B CE2 1 
ATOM   4110 C  CZ  . PHE B 1 246 ? 2.647   -1.190  0.212   1.00 10.48 ? 246 PHE B CZ  1 
ATOM   4111 N  N   . ARG B 1 247 ? 0.083   2.976   3.864   1.00 8.28  ? 247 ARG B N   1 
ATOM   4112 C  CA  . ARG B 1 247 ? 1.214   3.480   4.732   1.00 8.30  ? 247 ARG B CA  1 
ATOM   4113 C  C   . ARG B 1 247 ? 1.931   2.283   5.325   1.00 8.25  ? 247 ARG B C   1 
ATOM   4114 O  O   . ARG B 1 247 ? 1.319   1.274   5.650   1.00 8.77  ? 247 ARG B O   1 
ATOM   4115 C  CB  . ARG B 1 247 ? 0.625   4.347   5.848   1.00 8.57  ? 247 ARG B CB  1 
ATOM   4116 C  CG  . ARG B 1 247 ? 1.624   5.167   6.602   1.00 7.82  ? 247 ARG B CG  1 
ATOM   4117 C  CD  . ARG B 1 247 ? 0.934   5.846   7.771   1.00 8.87  ? 247 ARG B CD  1 
ATOM   4118 N  NE  . ARG B 1 247 ? 1.781   6.944   8.283   1.00 8.97  ? 247 ARG B NE  1 
ATOM   4119 C  CZ  . ARG B 1 247 ? 1.472   7.648   9.377   1.00 9.15  ? 247 ARG B CZ  1 
ATOM   4120 N  NH1 . ARG B 1 247 ? 0.319   7.388   10.043  1.00 9.02  ? 247 ARG B NH1 1 
ATOM   4121 N  NH2 . ARG B 1 247 ? 2.223   8.687   9.748   1.00 10.11 ? 247 ARG B NH2 1 
ATOM   4122 N  N   . GLN B 1 248 ? 3.249   2.430   5.530   1.00 8.14  ? 248 GLN B N   1 
ATOM   4123 C  CA  . GLN B 1 248 ? 4.032   1.427   6.280   1.00 8.25  ? 248 GLN B CA  1 
ATOM   4124 C  C   . GLN B 1 248 ? 3.534   1.347   7.713   1.00 8.02  ? 248 GLN B C   1 
ATOM   4125 O  O   . GLN B 1 248 ? 3.021   2.313   8.261   1.00 8.93  ? 248 GLN B O   1 
ATOM   4126 C  CB  . GLN B 1 248 ? 5.508   1.784   6.278   1.00 7.88  ? 248 GLN B CB  1 
ATOM   4127 C  CG  . GLN B 1 248 ? 6.214   1.790   4.916   1.00 8.09  ? 248 GLN B CG  1 
ATOM   4128 C  CD  . GLN B 1 248 ? 6.225   0.433   4.288   1.00 9.22  ? 248 GLN B CD  1 
ATOM   4129 O  OE1 . GLN B 1 248 ? 5.317   0.056   3.532   1.00 9.70  ? 248 GLN B OE1 1 
ATOM   4130 N  NE2 . GLN B 1 248 ? 7.238   -0.341  4.613   1.00 10.28 ? 248 GLN B NE2 1 
ATOM   4131 N  N   . VAL B 1 249 ? 3.719   0.187   8.322   1.00 8.26  ? 249 VAL B N   1 
ATOM   4132 C  CA  . VAL B 1 249 ? 3.291   0.054   9.735   1.00 8.33  ? 249 VAL B CA  1 
ATOM   4133 C  C   . VAL B 1 249 ? 4.184   0.933   10.641  1.00 8.93  ? 249 VAL B C   1 
ATOM   4134 O  O   . VAL B 1 249 ? 5.336   1.259   10.288  1.00 8.30  ? 249 VAL B O   1 
ATOM   4135 C  CB  . VAL B 1 249 ? 3.392   -1.409  10.226  1.00 7.90  ? 249 VAL B CB  1 
ATOM   4136 C  CG1 . VAL B 1 249 ? 2.319   -2.261  9.498   1.00 8.28  ? 249 VAL B CG1 1 
ATOM   4137 C  CG2 . VAL B 1 249 ? 4.768   -1.987  9.921   1.00 8.77  ? 249 VAL B CG2 1 
ATOM   4138 N  N   . GLN B 1 250 ? 3.606   1.306   11.768  1.00 8.69  ? 250 GLN B N   1 
ATOM   4139 C  CA  . GLN B 1 250 ? 4.169   2.289   12.671  1.00 9.06  ? 250 GLN B CA  1 
ATOM   4140 C  C   . GLN B 1 250 ? 4.671   1.661   13.961  1.00 9.90  ? 250 GLN B C   1 
ATOM   4141 O  O   . GLN B 1 250 ? 4.217   0.610   14.373  1.00 10.31 ? 250 GLN B O   1 
ATOM   4142 C  CB  . GLN B 1 250 ? 3.065   3.330   13.065  1.00 9.40  ? 250 GLN B CB  1 
ATOM   4143 C  CG  . GLN B 1 250 ? 2.418   3.886   11.793  1.00 9.27  ? 250 GLN B CG  1 
ATOM   4144 C  CD  . GLN B 1 250 ? 3.314   4.836   11.062  1.00 9.41  ? 250 GLN B CD  1 
ATOM   4145 O  OE1 . GLN B 1 250 ? 3.711   5.867   11.647  1.00 11.11 ? 250 GLN B OE1 1 
ATOM   4146 N  NE2 . GLN B 1 250 ? 3.577   4.579   9.790   1.00 9.26  ? 250 GLN B NE2 1 
ATOM   4147 N  N   . LYS B 1 251 ? 5.597   2.359   14.611  1.00 9.81  ? 251 LYS B N   1 
ATOM   4148 C  CA  . LYS B 1 251 ? 6.010   1.904   15.970  1.00 11.54 ? 251 LYS B CA  1 
ATOM   4149 C  C   . LYS B 1 251 ? 4.811   1.826   16.933  1.00 12.40 ? 251 LYS B C   1 
ATOM   4150 O  O   . LYS B 1 251 ? 3.914   2.689   16.915  1.00 12.62 ? 251 LYS B O   1 
ATOM   4151 C  CB  . LYS B 1 251 ? 7.019   2.897   16.583  1.00 12.33 ? 251 LYS B CB  1 
ATOM   4152 C  CG  . LYS B 1 251 ? 8.424   2.875   15.964  1.00 13.31 ? 251 LYS B CG  1 
ATOM   4153 C  CD  . LYS B 1 251 ? 9.268   1.760   16.507  1.00 14.04 ? 251 LYS B CD  1 
ATOM   4154 C  CE  . LYS B 1 251 ? 10.773  1.840   16.078  1.00 12.81 ? 251 LYS B CE  1 
ATOM   4155 N  NZ  . LYS B 1 251 ? 10.930  1.900   14.578  1.00 11.41 ? 251 LYS B NZ  1 
ATOM   4156 N  N   A PHE B 1 252 ? 4.817   0.806   17.786  0.50 13.65 ? 252 PHE B N   1 
ATOM   4157 N  N   B PHE B 1 252 ? 4.829   0.744   17.726  0.50 13.65 ? 252 PHE B N   1 
ATOM   4158 C  CA  A PHE B 1 252 ? 3.750   0.685   18.753  0.50 14.19 ? 252 PHE B CA  1 
ATOM   4159 C  CA  B PHE B 1 252 ? 3.900   0.467   18.822  0.50 14.19 ? 252 PHE B CA  1 
ATOM   4160 C  C   A PHE B 1 252 ? 4.295   1.217   20.049  0.50 18.95 ? 252 PHE B C   1 
ATOM   4161 C  C   B PHE B 1 252 ? 4.395   1.217   20.049  0.50 18.95 ? 252 PHE B C   1 
ATOM   4162 O  O   A PHE B 1 252 ? 4.865   0.516   20.885  0.50 16.28 ? 252 PHE B O   1 
ATOM   4163 O  O   B PHE B 1 252 ? 5.170   0.618   21.030  0.50 16.28 ? 252 PHE B O   1 
ATOM   4164 C  CB  A PHE B 1 252 ? 3.189   -0.731  18.884  0.50 13.81 ? 252 PHE B CB  1 
ATOM   4165 C  CB  B PHE B 1 252 ? 3.914   -1.027  19.190  0.50 13.81 ? 252 PHE B CB  1 
ATOM   4166 C  CG  A PHE B 1 252 ? 1.712   -0.754  19.183  0.50 14.96 ? 252 PHE B CG  1 
ATOM   4167 C  CG  B PHE B 1 252 ? 3.203   -1.932  18.212  0.50 14.96 ? 252 PHE B CG  1 
ATOM   4168 C  CD1 A PHE B 1 252 ? 0.876   0.227   18.672  0.50 14.28 ? 252 PHE B CD1 1 
ATOM   4169 C  CD1 B PHE B 1 252 ? 1.830   -2.128  18.288  0.50 14.28 ? 252 PHE B CD1 1 
ATOM   4170 C  CD2 A PHE B 1 252 ? 1.166   -1.739  19.987  0.50 16.92 ? 252 PHE B CD2 1 
ATOM   4171 C  CD2 B PHE B 1 252 ? 3.921   -2.640  17.264  0.50 16.92 ? 252 PHE B CD2 1 
ATOM   4172 C  CE1 A PHE B 1 252 ? -0.479  0.220   18.947  0.50 14.62 ? 252 PHE B CE1 1 
ATOM   4173 C  CE1 B PHE B 1 252 ? 1.187   -2.980  17.404  0.50 14.62 ? 252 PHE B CE1 1 
ATOM   4174 C  CE2 A PHE B 1 252 ? -0.189  -1.751  20.267  0.50 16.07 ? 252 PHE B CE2 1 
ATOM   4175 C  CE2 B PHE B 1 252 ? 3.284   -3.493  16.384  0.50 16.07 ? 252 PHE B CE2 1 
ATOM   4176 C  CZ  A PHE B 1 252 ? -1.012  -0.772  19.746  0.50 16.83 ? 252 PHE B CZ  1 
ATOM   4177 C  CZ  B PHE B 1 252 ? 1.917   -3.665  16.453  0.50 16.83 ? 252 PHE B CZ  1 
ATOM   4178 N  N   . ASP B 1 253 ? 4.104   2.523   20.203  1.00 23.72 ? 253 ASP B N   1 
ATOM   4179 C  CA  . ASP B 1 253 ? 4.623   3.250   21.353  1.00 30.38 ? 253 ASP B CA  1 
ATOM   4180 C  C   . ASP B 1 253 ? 3.930   2.768   22.626  1.00 30.73 ? 253 ASP B C   1 
ATOM   4181 O  O   . ASP B 1 253 ? 3.075   3.460   23.177  1.00 36.18 ? 253 ASP B O   1 
ATOM   4182 C  CB  . ASP B 1 253 ? 4.411   4.756   21.182  1.00 33.85 ? 253 ASP B CB  1 
ATOM   4183 C  CG  . ASP B 1 253 ? 4.644   5.220   19.761  1.00 43.52 ? 253 ASP B CG  1 
ATOM   4184 O  OD1 . ASP B 1 253 ? 5.754   4.993   19.234  1.00 43.18 ? 253 ASP B OD1 1 
ATOM   4185 O  OD2 . ASP B 1 253 ? 3.717   5.811   19.168  1.00 41.37 ? 253 ASP B OD2 1 
ATOM   4186 N  N   . GLU B 1 254 ? 4.311   1.583   23.094  1.00 30.34 ? 254 GLU B N   1 
ATOM   4187 C  CA  . GLU B 1 254 ? 3.786   1.056   24.374  1.00 31.78 ? 254 GLU B CA  1 
ATOM   4188 C  C   . GLU B 1 254 ? 2.298   0.653   24.348  1.00 30.43 ? 254 GLU B C   1 
ATOM   4189 O  O   . GLU B 1 254 ? 1.764   0.301   25.360  1.00 32.11 ? 254 GLU B O   1 
ATOM   4190 C  CB  . GLU B 1 254 ? 4.009   2.024   25.580  1.00 34.82 ? 254 GLU B CB  1 
ATOM   4191 C  CG  . GLU B 1 254 ? 5.418   2.615   25.761  1.00 41.46 ? 254 GLU B CG  1 
ATOM   4192 C  CD  . GLU B 1 254 ? 6.295   1.917   26.797  1.00 53.54 ? 254 GLU B CD  1 
ATOM   4193 O  OE1 . GLU B 1 254 ? 5.838   1.600   27.907  1.00 54.11 ? 254 GLU B OE1 1 
ATOM   4194 O  OE2 . GLU B 1 254 ? 7.505   1.695   26.515  1.00 55.57 ? 254 GLU B OE2 1 
ATOM   4195 N  N   A ARG B 1 255 ? 1.667   0.716   23.195  0.50 27.05 ? 255 ARG B N   1 
ATOM   4196 N  N   B ARG B 1 255 ? 1.653   0.789   23.189  0.50 24.17 ? 255 ARG B N   1 
ATOM   4197 C  CA  A ARG B 1 255 ? 0.261   0.375   23.096  0.50 25.54 ? 255 ARG B CA  1 
ATOM   4198 C  CA  B ARG B 1 255 ? 0.269   0.332   22.991  0.50 21.81 ? 255 ARG B CA  1 
ATOM   4199 C  C   A ARG B 1 255 ? 0.095   -1.168  22.966  0.50 25.27 ? 255 ARG B C   1 
ATOM   4200 C  C   B ARG B 1 255 ? 0.178   -1.222  23.117  0.50 22.86 ? 255 ARG B C   1 
ATOM   4201 O  O   A ARG B 1 255 ? 0.976   -1.838  22.373  0.50 25.64 ? 255 ARG B O   1 
ATOM   4202 O  O   B ARG B 1 255 ? 1.156   -1.940  22.834  0.50 23.75 ? 255 ARG B O   1 
ATOM   4203 C  CB  A ARG B 1 255 ? -0.294  1.187   21.927  0.50 25.28 ? 255 ARG B CB  1 
ATOM   4204 C  CB  B ARG B 1 255 ? -0.269  0.819   21.610  0.50 17.97 ? 255 ARG B CB  1 
ATOM   4205 C  CG  A ARG B 1 255 ? 0.072   2.656   22.137  0.50 23.58 ? 255 ARG B CG  1 
ATOM   4206 C  CG  B ARG B 1 255 ? -0.719  2.277   21.549  0.50 16.93 ? 255 ARG B CG  1 
ATOM   4207 C  CD  A ARG B 1 255 ? 0.464   3.286   20.824  0.50 24.55 ? 255 ARG B CD  1 
ATOM   4208 C  CD  B ARG B 1 255 ? -1.178  2.656   20.136  0.50 12.61 ? 255 ARG B CD  1 
ATOM   4209 N  NE  A ARG B 1 255 ? -0.707  3.303   19.956  0.50 23.42 ? 255 ARG B NE  1 
ATOM   4210 N  NE  B ARG B 1 255 ? -0.043  2.696   19.179  0.50 13.45 ? 255 ARG B NE  1 
ATOM   4211 C  CZ  A ARG B 1 255 ? -0.622  3.491   18.646  0.50 23.48 ? 255 ARG B CZ  1 
ATOM   4212 C  CZ  B ARG B 1 255 ? -0.092  2.984   17.862  0.50 12.91 ? 255 ARG B CZ  1 
ATOM   4213 N  NH1 A ARG B 1 255 ? 0.579   3.664   18.072  0.50 27.83 ? 255 ARG B NH1 1 
ATOM   4214 N  NH1 B ARG B 1 255 ? -1.279  3.255   17.296  0.50 12.85 ? 255 ARG B NH1 1 
ATOM   4215 N  NH2 A ARG B 1 255 ? -1.725  3.477   17.904  0.50 20.76 ? 255 ARG B NH2 1 
ATOM   4216 N  NH2 B ARG B 1 255 ? 1.067   3.080   17.127  0.50 10.79 ? 255 ARG B NH2 1 
ATOM   4217 N  N   . LEU B 1 256 ? -0.974  -1.729  23.564  1.00 21.58 ? 256 LEU B N   1 
ATOM   4218 C  CA  . LEU B 1 256 ? -1.338  -3.133  23.329  1.00 19.88 ? 256 LEU B CA  1 
ATOM   4219 C  C   . LEU B 1 256 ? -2.540  -3.105  22.356  1.00 18.81 ? 256 LEU B C   1 
ATOM   4220 O  O   . LEU B 1 256 ? -3.296  -2.118  22.330  1.00 19.06 ? 256 LEU B O   1 
ATOM   4221 C  CB  . LEU B 1 256 ? -1.775  -3.891  24.598  1.00 24.96 ? 256 LEU B CB  1 
ATOM   4222 C  CG  . LEU B 1 256 ? -0.744  -4.015  25.713  1.00 25.50 ? 256 LEU B CG  1 
ATOM   4223 C  CD1 . LEU B 1 256 ? -1.362  -4.957  26.750  1.00 28.24 ? 256 LEU B CD1 1 
ATOM   4224 C  CD2 . LEU B 1 256 ? 0.605   -4.464  25.175  1.00 28.24 ? 256 LEU B CD2 1 
ATOM   4225 N  N   . VAL B 1 257 ? -2.743  -4.248  21.713  1.00 14.94 ? 257 VAL B N   1 
ATOM   4226 C  CA  . VAL B 1 257 ? -3.905  -4.483  20.900  1.00 14.17 ? 257 VAL B CA  1 
ATOM   4227 C  C   . VAL B 1 257 ? -4.708  -5.522  21.618  1.00 13.14 ? 257 VAL B C   1 
ATOM   4228 O  O   . VAL B 1 257 ? -4.209  -6.646  21.955  1.00 13.35 ? 257 VAL B O   1 
ATOM   4229 C  CB  . VAL B 1 257 ? -3.472  -5.027  19.501  1.00 14.56 ? 257 VAL B CB  1 
ATOM   4230 C  CG1 . VAL B 1 257 ? -4.634  -5.489  18.659  1.00 13.23 ? 257 VAL B CG1 1 
ATOM   4231 C  CG2 . VAL B 1 257 ? -2.701  -3.934  18.755  1.00 13.67 ? 257 VAL B CG2 1 
ATOM   4232 N  N   . TYR B 1 258 ? -5.996  -5.246  21.759  1.00 12.55 ? 258 TYR B N   1 
ATOM   4233 C  CA  . TYR B 1 258 ? -6.903  -6.115  22.543  1.00 13.91 ? 258 TYR B CA  1 
ATOM   4234 C  C   . TYR B 1 258 ? -7.670  -7.030  21.625  1.00 14.09 ? 258 TYR B C   1 
ATOM   4235 O  O   . TYR B 1 258 ? -7.992  -6.602  20.522  1.00 14.96 ? 258 TYR B O   1 
ATOM   4236 C  CB  . TYR B 1 258 ? -7.825  -5.186  23.351  1.00 14.87 ? 258 TYR B CB  1 
ATOM   4237 C  CG  . TYR B 1 258 ? -7.010  -4.337  24.279  1.00 17.99 ? 258 TYR B CG  1 
ATOM   4238 C  CD1 . TYR B 1 258 ? -6.513  -4.869  25.498  1.00 20.33 ? 258 TYR B CD1 1 
ATOM   4239 C  CD2 . TYR B 1 258 ? -6.596  -3.059  23.899  1.00 18.71 ? 258 TYR B CD2 1 
ATOM   4240 C  CE1 . TYR B 1 258 ? -5.708  -4.107  26.314  1.00 21.46 ? 258 TYR B CE1 1 
ATOM   4241 C  CE2 . TYR B 1 258 ? -5.791  -2.269  24.721  1.00 23.15 ? 258 TYR B CE2 1 
ATOM   4242 C  CZ  . TYR B 1 258 ? -5.334  -2.805  25.935  1.00 22.22 ? 258 TYR B CZ  1 
ATOM   4243 O  OH  . TYR B 1 258 ? -4.535  -1.956  26.711  1.00 24.77 ? 258 TYR B OH  1 
ATOM   4244 N  N   . THR B 1 259 ? -7.892  -8.305  21.943  1.00 10.89 ? 259 THR B N   1 
ATOM   4245 C  CA  . THR B 1 259 ? -8.493  -9.218  21.040  1.00 11.94 ? 259 THR B CA  1 
ATOM   4246 C  C   . THR B 1 259 ? -9.787  -9.789  21.655  1.00 12.67 ? 259 THR B C   1 
ATOM   4247 O  O   . THR B 1 259 ? -9.867  -10.005 22.859  1.00 13.73 ? 259 THR B O   1 
ATOM   4248 C  CB  . THR B 1 259 ? -7.599  -10.388 20.621  1.00 12.61 ? 259 THR B CB  1 
ATOM   4249 O  OG1 . THR B 1 259 ? -7.126  -11.097 21.789  1.00 14.12 ? 259 THR B OG1 1 
ATOM   4250 C  CG2 . THR B 1 259 ? -6.305  -9.915  19.915  1.00 11.87 ? 259 THR B CG2 1 
ATOM   4251 N  N   . SER B 1 260 ? -10.778 -10.020 20.835  1.00 11.51 ? 260 SER B N   1 
ATOM   4252 C  CA  . SER B 1 260 ? -12.068 -10.529 21.333  1.00 11.76 ? 260 SER B CA  1 
ATOM   4253 C  C   . SER B 1 260 ? -12.017 -12.021 21.327  1.00 13.93 ? 260 SER B C   1 
ATOM   4254 O  O   . SER B 1 260 ? -13.040 -12.695 21.663  1.00 14.43 ? 260 SER B O   1 
ATOM   4255 C  CB  . SER B 1 260 ? -13.230 -10.031 20.406  1.00 12.41 ? 260 SER B CB  1 
ATOM   4256 O  OG  . SER B 1 260 ? -13.077 -10.631 19.163  1.00 12.08 ? 260 SER B OG  1 
ATOM   4257 N  N   . PHE B 1 261 ? -10.881 -12.578 20.887  1.00 13.99 ? 261 PHE B N   1 
ATOM   4258 C  CA  . PHE B 1 261 ? -10.744 -14.024 20.738  1.00 14.59 ? 261 PHE B CA  1 
ATOM   4259 C  C   . PHE B 1 261 ? -9.545  -14.387 21.605  1.00 16.52 ? 261 PHE B C   1 
ATOM   4260 O  O   . PHE B 1 261 ? -8.581  -13.698 21.640  1.00 15.99 ? 261 PHE B O   1 
ATOM   4261 C  CB  . PHE B 1 261 ? -10.584 -14.501 19.277  1.00 13.87 ? 261 PHE B CB  1 
ATOM   4262 C  CG  . PHE B 1 261 ? -9.493  -13.785 18.514  1.00 15.40 ? 261 PHE B CG  1 
ATOM   4263 C  CD1 . PHE B 1 261 ? -8.187  -14.281 18.389  1.00 17.04 ? 261 PHE B CD1 1 
ATOM   4264 C  CD2 . PHE B 1 261 ? -9.783  -12.545 17.925  1.00 15.35 ? 261 PHE B CD2 1 
ATOM   4265 C  CE1 . PHE B 1 261 ? -7.185  -13.589 17.705  1.00 17.16 ? 261 PHE B CE1 1 
ATOM   4266 C  CE2 . PHE B 1 261 ? -8.802  -11.879 17.221  1.00 16.03 ? 261 PHE B CE2 1 
ATOM   4267 C  CZ  . PHE B 1 261 ? -7.495  -12.349 17.130  1.00 15.24 ? 261 PHE B CZ  1 
ATOM   4268 N  N   . SER B 1 262 ? -9.615  -15.532 22.304  1.00 19.27 ? 262 SER B N   1 
ATOM   4269 C  CA  . SER B 1 262 ? -8.511  -15.837 23.201  1.00 24.85 ? 262 SER B CA  1 
ATOM   4270 C  C   . SER B 1 262 ? -7.453  -16.669 22.509  1.00 28.01 ? 262 SER B C   1 
ATOM   4271 O  O   . SER B 1 262 ? -6.285  -16.668 22.939  1.00 35.23 ? 262 SER B O   1 
ATOM   4272 C  CB  . SER B 1 262 ? -8.996  -16.543 24.485  1.00 26.25 ? 262 SER B CB  1 
ATOM   4273 O  OG  . SER B 1 262 ? -9.917  -17.603 24.158  1.00 30.68 ? 262 SER B OG  1 
ATOM   4274 N  N   . GLN B 1 263 ? -7.874  -17.393 21.471  1.00 31.26 ? 263 GLN B N   1 
ATOM   4275 C  CA  . GLN B 1 263 ? -7.029  -18.337 20.722  1.00 30.36 ? 263 GLN B CA  1 
ATOM   4276 C  C   . GLN B 1 263 ? -7.644  -18.488 19.343  1.00 29.65 ? 263 GLN B C   1 
ATOM   4277 O  O   . GLN B 1 263 ? -7.033  -19.119 18.454  1.00 28.06 ? 263 GLN B O   1 
ATOM   4278 C  CB  . GLN B 1 263 ? -6.907  -19.715 21.423  1.00 34.35 ? 263 GLN B CB  1 
ATOM   4279 C  CG  . GLN B 1 263 ? -8.213  -20.458 21.718  1.00 40.24 ? 263 GLN B CG  1 
ATOM   4280 C  CD  . GLN B 1 263 ? -8.087  -21.465 22.867  1.00 43.05 ? 263 GLN B CD  1 
ATOM   4281 O  OE1 . GLN B 1 263 ? -7.201  -22.317 22.861  1.00 43.38 ? 263 GLN B OE1 1 
ATOM   4282 N  NE2 . GLN B 1 263 ? -8.997  -21.382 23.840  1.00 47.84 ? 263 GLN B NE2 1 
ATOM   4283 O  OXT . GLN B 1 263 ? -8.780  -17.970 19.145  1.00 22.92 ? 263 GLN B OXT 1 
ATOM   4284 N  N   . LYS C 1 3   ? 34.566  18.303  -26.209 1.00 52.83 ? 3   LYS C N   1 
ATOM   4285 C  CA  . LYS C 1 3   ? 33.718  17.754  -25.097 1.00 53.91 ? 3   LYS C CA  1 
ATOM   4286 C  C   . LYS C 1 3   ? 32.452  17.033  -25.641 1.00 53.41 ? 3   LYS C C   1 
ATOM   4287 O  O   . LYS C 1 3   ? 31.300  17.345  -25.254 1.00 59.55 ? 3   LYS C O   1 
ATOM   4288 C  CB  . LYS C 1 3   ? 33.361  18.849  -24.070 1.00 59.15 ? 3   LYS C CB  1 
ATOM   4289 C  CG  . LYS C 1 3   ? 32.884  18.343  -22.702 1.00 70.55 ? 3   LYS C CG  1 
ATOM   4290 C  CD  . LYS C 1 3   ? 34.029  18.144  -21.700 1.00 77.19 ? 3   LYS C CD  1 
ATOM   4291 C  CE  . LYS C 1 3   ? 33.542  18.219  -20.251 1.00 77.10 ? 3   LYS C CE  1 
ATOM   4292 N  NZ  . LYS C 1 3   ? 34.638  18.217  -19.230 1.00 75.43 ? 3   LYS C NZ  1 
ATOM   4293 N  N   . TRP C 1 4   ? 32.680  16.092  -26.565 1.00 37.20 ? 4   TRP C N   1 
ATOM   4294 C  CA  . TRP C 1 4   ? 31.659  15.078  -26.942 1.00 27.69 ? 4   TRP C CA  1 
ATOM   4295 C  C   . TRP C 1 4   ? 31.558  13.977  -25.921 1.00 24.34 ? 4   TRP C C   1 
ATOM   4296 O  O   . TRP C 1 4   ? 32.494  13.688  -25.128 1.00 21.32 ? 4   TRP C O   1 
ATOM   4297 C  CB  . TRP C 1 4   ? 31.956  14.536  -28.358 1.00 21.97 ? 4   TRP C CB  1 
ATOM   4298 C  CG  . TRP C 1 4   ? 33.236  13.770  -28.447 1.00 18.06 ? 4   TRP C CG  1 
ATOM   4299 C  CD1 . TRP C 1 4   ? 34.518  14.251  -28.760 1.00 17.59 ? 4   TRP C CD1 1 
ATOM   4300 C  CD2 . TRP C 1 4   ? 33.403  12.379  -28.198 1.00 15.76 ? 4   TRP C CD2 1 
ATOM   4301 N  NE1 . TRP C 1 4   ? 35.431  13.259  -28.714 1.00 17.45 ? 4   TRP C NE1 1 
ATOM   4302 C  CE2 . TRP C 1 4   ? 34.825  12.077  -28.390 1.00 17.87 ? 4   TRP C CE2 1 
ATOM   4303 C  CE3 . TRP C 1 4   ? 32.533  11.332  -27.920 1.00 15.08 ? 4   TRP C CE3 1 
ATOM   4304 C  CZ2 . TRP C 1 4   ? 35.325  10.796  -28.285 1.00 16.00 ? 4   TRP C CZ2 1 
ATOM   4305 C  CZ3 . TRP C 1 4   ? 33.073  10.039  -27.804 1.00 14.07 ? 4   TRP C CZ3 1 
ATOM   4306 C  CH2 . TRP C 1 4   ? 34.434  9.784   -27.945 1.00 15.10 ? 4   TRP C CH2 1 
ATOM   4307 N  N   . THR C 1 5   ? 30.415  13.298  -25.935 1.00 21.33 ? 5   THR C N   1 
ATOM   4308 C  CA  . THR C 1 5   ? 30.150  12.230  -25.025 1.00 20.60 ? 5   THR C CA  1 
ATOM   4309 C  C   . THR C 1 5   ? 29.408  11.074  -25.727 1.00 19.51 ? 5   THR C C   1 
ATOM   4310 O  O   . THR C 1 5   ? 28.826  11.284  -26.840 1.00 18.80 ? 5   THR C O   1 
ATOM   4311 C  CB  . THR C 1 5   ? 29.255  12.692  -23.852 1.00 25.58 ? 5   THR C CB  1 
ATOM   4312 O  OG1 . THR C 1 5   ? 28.014  13.149  -24.363 1.00 23.27 ? 5   THR C OG1 1 
ATOM   4313 C  CG2 . THR C 1 5   ? 29.887  13.892  -23.146 1.00 24.60 ? 5   THR C CG2 1 
ATOM   4314 N  N   . TYR C 1 6   ? 29.461  9.902   -25.100 1.00 19.95 ? 6   TYR C N   1 
ATOM   4315 C  CA  . TYR C 1 6   ? 28.677  8.745   -25.529 1.00 19.40 ? 6   TYR C CA  1 
ATOM   4316 C  C   . TYR C 1 6   ? 27.287  8.772   -24.978 1.00 23.61 ? 6   TYR C C   1 
ATOM   4317 O  O   . TYR C 1 6   ? 26.460  8.064   -25.465 1.00 23.61 ? 6   TYR C O   1 
ATOM   4318 C  CB  . TYR C 1 6   ? 29.318  7.427   -25.163 1.00 20.66 ? 6   TYR C CB  1 
ATOM   4319 C  CG  . TYR C 1 6   ? 30.494  6.994   -26.002 1.00 20.19 ? 6   TYR C CG  1 
ATOM   4320 C  CD1 . TYR C 1 6   ? 31.780  6.960   -25.472 1.00 18.90 ? 6   TYR C CD1 1 
ATOM   4321 C  CD2 . TYR C 1 6   ? 30.278  6.526   -27.332 1.00 18.92 ? 6   TYR C CD2 1 
ATOM   4322 C  CE1 . TYR C 1 6   ? 32.841  6.478   -26.204 1.00 19.55 ? 6   TYR C CE1 1 
ATOM   4323 C  CE2 . TYR C 1 6   ? 31.342  6.077   -28.079 1.00 17.64 ? 6   TYR C CE2 1 
ATOM   4324 C  CZ  . TYR C 1 6   ? 32.609  6.103   -27.551 1.00 17.29 ? 6   TYR C CZ  1 
ATOM   4325 O  OH  . TYR C 1 6   ? 33.704  5.622   -28.249 1.00 16.93 ? 6   TYR C OH  1 
ATOM   4326 N  N   . PHE C 1 7   ? 27.061  9.548   -23.912 1.00 26.48 ? 7   PHE C N   1 
ATOM   4327 C  CA  . PHE C 1 7   ? 25.786  9.471   -23.182 1.00 25.93 ? 7   PHE C CA  1 
ATOM   4328 C  C   . PHE C 1 7   ? 25.065  10.733  -23.516 1.00 25.83 ? 7   PHE C C   1 
ATOM   4329 O  O   . PHE C 1 7   ? 25.698  11.787  -23.723 1.00 25.42 ? 7   PHE C O   1 
ATOM   4330 C  CB  . PHE C 1 7   ? 25.998  9.350   -21.643 1.00 26.61 ? 7   PHE C CB  1 
ATOM   4331 C  CG  . PHE C 1 7   ? 26.986  10.318  -21.075 1.00 26.53 ? 7   PHE C CG  1 
ATOM   4332 C  CD1 . PHE C 1 7   ? 26.580  11.586  -20.650 1.00 26.51 ? 7   PHE C CD1 1 
ATOM   4333 C  CD2 . PHE C 1 7   ? 28.350  9.957   -20.928 1.00 28.07 ? 7   PHE C CD2 1 
ATOM   4334 C  CE1 . PHE C 1 7   ? 27.525  12.526  -20.160 1.00 27.73 ? 7   PHE C CE1 1 
ATOM   4335 C  CE2 . PHE C 1 7   ? 29.266  10.871  -20.422 1.00 29.31 ? 7   PHE C CE2 1 
ATOM   4336 C  CZ  . PHE C 1 7   ? 28.849  12.169  -20.043 1.00 27.80 ? 7   PHE C CZ  1 
ATOM   4337 N  N   . GLY C 1 8   ? 23.739  10.719  -23.584 1.00 23.60 ? 8   GLY C N   1 
ATOM   4338 C  CA  . GLY C 1 8   ? 22.960  11.956  -23.702 1.00 30.93 ? 8   GLY C CA  1 
ATOM   4339 C  C   . GLY C 1 8   ? 23.246  13.082  -24.708 1.00 44.15 ? 8   GLY C C   1 
ATOM   4340 O  O   . GLY C 1 8   ? 23.708  12.844  -25.826 1.00 58.08 ? 8   GLY C O   1 
ATOM   4341 N  N   . PRO C 1 9   ? 22.865  14.289  -24.299 1.00 41.52 ? 9   PRO C N   1 
ATOM   4342 C  CA  . PRO C 1 9   ? 22.826  15.462  -25.175 1.00 41.94 ? 9   PRO C CA  1 
ATOM   4343 C  C   . PRO C 1 9   ? 24.021  15.538  -26.104 1.00 42.02 ? 9   PRO C C   1 
ATOM   4344 O  O   . PRO C 1 9   ? 23.860  15.515  -27.324 1.00 29.94 ? 9   PRO C O   1 
ATOM   4345 C  CB  . PRO C 1 9   ? 22.857  16.630  -24.187 1.00 48.88 ? 9   PRO C CB  1 
ATOM   4346 C  CG  . PRO C 1 9   ? 22.228  16.085  -22.951 1.00 49.47 ? 9   PRO C CG  1 
ATOM   4347 C  CD  . PRO C 1 9   ? 22.639  14.640  -22.887 1.00 42.49 ? 9   PRO C CD  1 
ATOM   4348 N  N   . ASP C 1 10  ? 25.210  15.633  -25.526 1.00 42.76 ? 10  ASP C N   1 
ATOM   4349 C  CA  . ASP C 1 10  ? 26.442  15.780  -26.348 1.00 39.78 ? 10  ASP C CA  1 
ATOM   4350 C  C   . ASP C 1 10  ? 26.843  14.505  -27.085 1.00 31.62 ? 10  ASP C C   1 
ATOM   4351 O  O   . ASP C 1 10  ? 28.049  14.428  -27.632 1.00 24.84 ? 10  ASP C O   1 
ATOM   4352 C  CB  . ASP C 1 10  ? 27.600  16.196  -25.449 1.00 42.31 ? 10  ASP C CB  1 
ATOM   4353 C  CG  . ASP C 1 10  ? 27.414  17.569  -24.900 1.00 53.12 ? 10  ASP C CG  1 
ATOM   4354 O  OD1 . ASP C 1 10  ? 27.449  18.526  -25.722 1.00 50.74 ? 10  ASP C OD1 1 
ATOM   4355 O  OD2 . ASP C 1 10  ? 27.199  17.673  -23.657 1.00 53.68 ? 10  ASP C OD2 1 
ATOM   4356 N  N   . GLY C 1 11  ? 25.854  13.580  -27.068 1.00 31.26 ? 11  GLY C N   1 
ATOM   4357 C  CA  . GLY C 1 11  ? 25.803  12.108  -27.533 1.00 19.90 ? 11  GLY C CA  1 
ATOM   4358 C  C   . GLY C 1 11  ? 25.838  11.896  -29.056 1.00 15.05 ? 11  GLY C C   1 
ATOM   4359 O  O   . GLY C 1 11  ? 25.796  12.887  -29.777 1.00 15.03 ? 11  GLY C O   1 
ATOM   4360 N  N   . GLU C 1 12  ? 25.937  10.630  -29.472 1.00 12.25 ? 12  GLU C N   1 
ATOM   4361 C  CA  . GLU C 1 12  ? 26.335  10.395  -30.879 1.00 11.55 ? 12  GLU C CA  1 
ATOM   4362 C  C   . GLU C 1 12  ? 25.490  11.084  -31.918 1.00 12.28 ? 12  GLU C C   1 
ATOM   4363 O  O   . GLU C 1 12  ? 26.025  11.431  -32.981 1.00 11.91 ? 12  GLU C O   1 
ATOM   4364 C  CB  . GLU C 1 12  ? 26.526  8.909   -31.160 1.00 10.25 ? 12  GLU C CB  1 
ATOM   4365 C  CG  . GLU C 1 12  ? 25.164  8.201   -31.261 1.00 9.84  ? 12  GLU C CG  1 
ATOM   4366 C  CD  . GLU C 1 12  ? 25.407  6.723   -31.072 1.00 9.86  ? 12  GLU C CD  1 
ATOM   4367 O  OE1 . GLU C 1 12  ? 25.748  5.941   -32.015 1.00 11.74 ? 12  GLU C OE1 1 
ATOM   4368 O  OE2 . GLU C 1 12  ? 25.463  6.305   -29.859 1.00 13.18 ? 12  GLU C OE2 1 
ATOM   4369 N  N   . ASN C 1 13  ? 24.168  11.218  -31.771 1.00 10.73 ? 13  ASN C N   1 
ATOM   4370 C  CA  . ASN C 1 13  ? 23.420  11.848  -32.833 1.00 10.72 ? 13  ASN C CA  1 
ATOM   4371 C  C   . ASN C 1 13  ? 23.706  13.345  -33.012 1.00 10.89 ? 13  ASN C C   1 
ATOM   4372 O  O   . ASN C 1 13  ? 23.345  13.931  -34.027 1.00 12.03 ? 13  ASN C O   1 
ATOM   4373 C  CB  . ASN C 1 13  ? 21.904  11.704  -32.560 1.00 10.52 ? 13  ASN C CB  1 
ATOM   4374 C  CG  . ASN C 1 13  ? 21.469  10.261  -32.630 1.00 10.79 ? 13  ASN C CG  1 
ATOM   4375 O  OD1 . ASN C 1 13  ? 22.137  9.382   -33.191 1.00 10.52 ? 13  ASN C OD1 1 
ATOM   4376 N  ND2 . ASN C 1 13  ? 20.288  10.014  -32.074 1.00 11.36 ? 13  ASN C ND2 1 
ATOM   4377 N  N   A SER C 1 14  ? 24.339  13.938  -31.997 0.50 12.89 ? 14  SER C N   1 
ATOM   4378 N  N   B SER C 1 14  ? 24.326  13.967  -32.001 0.50 13.05 ? 14  SER C N   1 
ATOM   4379 C  CA  A SER C 1 14  ? 24.718  15.328  -32.042 0.50 12.92 ? 14  SER C CA  1 
ATOM   4380 C  CA  B SER C 1 14  ? 24.723  15.364  -32.088 0.50 13.19 ? 14  SER C CA  1 
ATOM   4381 C  C   A SER C 1 14  ? 26.156  15.566  -32.502 0.50 12.71 ? 14  SER C C   1 
ATOM   4382 C  C   B SER C 1 14  ? 26.196  15.568  -32.421 0.50 12.79 ? 14  SER C C   1 
ATOM   4383 O  O   A SER C 1 14  ? 26.489  16.712  -32.806 0.50 12.78 ? 14  SER C O   1 
ATOM   4384 O  O   B SER C 1 14  ? 26.620  16.696  -32.500 0.50 13.01 ? 14  SER C O   1 
ATOM   4385 C  CB  A SER C 1 14  ? 24.526  15.982  -30.652 0.50 11.74 ? 14  SER C CB  1 
ATOM   4386 C  CB  B SER C 1 14  ? 24.495  16.084  -30.743 0.50 12.44 ? 14  SER C CB  1 
ATOM   4387 O  OG  A SER C 1 14  ? 23.139  16.089  -30.351 0.50 13.91 ? 14  SER C OG  1 
ATOM   4388 O  OG  B SER C 1 14  ? 25.309  15.525  -29.735 0.50 15.22 ? 14  SER C OG  1 
ATOM   4389 N  N   . TRP C 1 15  ? 26.957  14.502  -32.606 1.00 11.91 ? 15  TRP C N   1 
ATOM   4390 C  CA  . TRP C 1 15  ? 28.367  14.677  -33.009 1.00 12.06 ? 15  TRP C CA  1 
ATOM   4391 C  C   . TRP C 1 15  ? 28.553  15.497  -34.241 1.00 13.22 ? 15  TRP C C   1 
ATOM   4392 O  O   . TRP C 1 15  ? 29.520  16.265  -34.311 1.00 12.88 ? 15  TRP C O   1 
ATOM   4393 C  CB  . TRP C 1 15  ? 29.043  13.379  -33.189 1.00 10.89 ? 15  TRP C CB  1 
ATOM   4394 C  CG  . TRP C 1 15  ? 29.181  12.547  -31.968 1.00 10.27 ? 15  TRP C CG  1 
ATOM   4395 C  CD1 . TRP C 1 15  ? 29.008  12.948  -30.610 1.00 10.97 ? 15  TRP C CD1 1 
ATOM   4396 C  CD2 . TRP C 1 15  ? 29.691  11.180  -31.899 1.00 10.58 ? 15  TRP C CD2 1 
ATOM   4397 N  NE1 . TRP C 1 15  ? 29.328  11.917  -29.738 1.00 12.00 ? 15  TRP C NE1 1 
ATOM   4398 C  CE2 . TRP C 1 15  ? 29.722  10.798  -30.486 1.00 11.20 ? 15  TRP C CE2 1 
ATOM   4399 C  CE3 . TRP C 1 15  ? 30.096  10.214  -32.875 1.00 9.71  ? 15  TRP C CE3 1 
ATOM   4400 C  CZ2 . TRP C 1 15  ? 30.133  9.543   -30.073 1.00 10.60 ? 15  TRP C CZ2 1 
ATOM   4401 C  CZ3 . TRP C 1 15  ? 30.485  8.954   -32.443 1.00 9.63  ? 15  TRP C CZ3 1 
ATOM   4402 C  CH2 . TRP C 1 15  ? 30.554  8.611   -31.062 1.00 10.42 ? 15  TRP C CH2 1 
ATOM   4403 N  N   . SER C 1 16  ? 27.660  15.338  -35.239 1.00 10.77 ? 16  SER C N   1 
ATOM   4404 C  CA  . SER C 1 16  ? 27.862  15.978  -36.541 1.00 10.96 ? 16  SER C CA  1 
ATOM   4405 C  C   . SER C 1 16  ? 27.795  17.503  -36.482 1.00 13.17 ? 16  SER C C   1 
ATOM   4406 O  O   . SER C 1 16  ? 28.199  18.179  -37.421 1.00 13.03 ? 16  SER C O   1 
ATOM   4407 C  CB  . SER C 1 16  ? 26.841  15.495  -37.537 1.00 10.69 ? 16  SER C CB  1 
ATOM   4408 O  OG  . SER C 1 16  ? 25.512  15.851  -37.088 1.00 13.84 ? 16  SER C OG  1 
ATOM   4409 N  N   A LYS C 1 17  ? 27.312  18.007  -35.339 0.50 12.21 ? 17  LYS C N   1 
ATOM   4410 N  N   B LYS C 1 17  ? 27.212  18.091  -35.436 0.50 11.54 ? 17  LYS C N   1 
ATOM   4411 C  CA  A LYS C 1 17  ? 27.175  19.460  -35.101 0.50 14.19 ? 17  LYS C CA  1 
ATOM   4412 C  CA  B LYS C 1 17  ? 27.207  19.596  -35.377 0.50 12.40 ? 17  LYS C CA  1 
ATOM   4413 C  C   A LYS C 1 17  ? 28.550  20.143  -35.122 0.50 12.75 ? 17  LYS C C   1 
ATOM   4414 C  C   B LYS C 1 17  ? 28.702  20.086  -35.304 0.50 11.56 ? 17  LYS C C   1 
ATOM   4415 O  O   A LYS C 1 17  ? 28.707  21.145  -35.804 0.50 13.93 ? 17  LYS C O   1 
ATOM   4416 O  O   B LYS C 1 17  ? 29.146  20.878  -36.145 0.50 12.07 ? 17  LYS C O   1 
ATOM   4417 C  CB  A LYS C 1 17  ? 26.492  19.698  -33.769 0.50 13.18 ? 17  LYS C CB  1 
ATOM   4418 C  CB  B LYS C 1 17  ? 26.365  20.100  -34.196 0.50 11.35 ? 17  LYS C CB  1 
ATOM   4419 C  CG  A LYS C 1 17  ? 25.058  19.212  -33.684 0.50 15.03 ? 17  LYS C CG  1 
ATOM   4420 C  CG  B LYS C 1 17  ? 24.844  19.891  -34.276 0.50 11.73 ? 17  LYS C CG  1 
ATOM   4421 C  CD  A LYS C 1 17  ? 24.426  19.449  -32.296 0.50 15.19 ? 17  LYS C CD  1 
ATOM   4422 C  CD  B LYS C 1 17  ? 24.208  20.224  -32.918 0.50 13.13 ? 17  LYS C CD  1 
ATOM   4423 C  CE  A LYS C 1 17  ? 22.961  19.055  -32.200 0.50 17.09 ? 17  LYS C CE  1 
ATOM   4424 C  CE  B LYS C 1 17  ? 23.932  21.711  -32.819 0.50 13.56 ? 17  LYS C CE  1 
ATOM   4425 N  NZ  A LYS C 1 17  ? 22.466  19.310  -30.809 0.50 18.57 ? 17  LYS C NZ  1 
ATOM   4426 N  NZ  B LYS C 1 17  ? 23.364  22.139  -31.513 0.50 15.73 ? 17  LYS C NZ  1 
ATOM   4427 N  N   . LYS C 1 18  ? 29.485  19.587  -34.363 1.00 13.39 ? 18  LYS C N   1 
ATOM   4428 C  CA  . LYS C 1 18  ? 30.866  20.052  -34.251 1.00 15.07 ? 18  LYS C CA  1 
ATOM   4429 C  C   . LYS C 1 18  ? 31.822  19.279  -35.146 1.00 16.61 ? 18  LYS C C   1 
ATOM   4430 O  O   . LYS C 1 18  ? 32.955  19.748  -35.401 1.00 19.40 ? 18  LYS C O   1 
ATOM   4431 C  CB  . LYS C 1 18  ? 31.388  20.010  -32.771 1.00 17.98 ? 18  LYS C CB  1 
ATOM   4432 C  CG  . LYS C 1 18  ? 30.649  20.942  -31.816 1.00 26.25 ? 18  LYS C CG  1 
ATOM   4433 C  CD  . LYS C 1 18  ? 31.147  22.402  -31.828 1.00 33.11 ? 18  LYS C CD  1 
ATOM   4434 C  CE  . LYS C 1 18  ? 30.036  23.373  -31.452 1.00 38.46 ? 18  LYS C CE  1 
ATOM   4435 N  NZ  . LYS C 1 18  ? 28.766  22.970  -32.162 1.00 31.61 ? 18  LYS C NZ  1 
ATOM   4436 N  N   . TYR C 1 19  ? 31.437  18.061  -35.531 1.00 13.77 ? 19  TYR C N   1 
ATOM   4437 C  CA  . TYR C 1 19  ? 32.348  17.172  -36.293 1.00 12.88 ? 19  TYR C CA  1 
ATOM   4438 C  C   . TYR C 1 19  ? 31.641  16.704  -37.580 1.00 12.86 ? 19  TYR C C   1 
ATOM   4439 O  O   . TYR C 1 19  ? 30.993  15.636  -37.548 1.00 14.11 ? 19  TYR C O   1 
ATOM   4440 C  CB  . TYR C 1 19  ? 32.726  15.989  -35.423 1.00 13.28 ? 19  TYR C CB  1 
ATOM   4441 C  CG  . TYR C 1 19  ? 33.347  16.433  -34.120 1.00 13.76 ? 19  TYR C CG  1 
ATOM   4442 C  CD1 . TYR C 1 19  ? 34.713  16.702  -34.037 1.00 16.06 ? 19  TYR C CD1 1 
ATOM   4443 C  CD2 . TYR C 1 19  ? 32.600  16.470  -32.951 1.00 14.64 ? 19  TYR C CD2 1 
ATOM   4444 C  CE1 . TYR C 1 19  ? 35.273  17.055  -32.810 1.00 15.50 ? 19  TYR C CE1 1 
ATOM   4445 C  CE2 . TYR C 1 19  ? 33.172  16.748  -31.701 1.00 15.32 ? 19  TYR C CE2 1 
ATOM   4446 C  CZ  . TYR C 1 19  ? 34.489  17.130  -31.648 1.00 17.36 ? 19  TYR C CZ  1 
ATOM   4447 O  OH  . TYR C 1 19  ? 35.100  17.402  -30.381 1.00 23.03 ? 19  TYR C OH  1 
ATOM   4448 N  N   . PRO C 1 20  ? 31.677  17.506  -38.644 1.00 12.81 ? 20  PRO C N   1 
ATOM   4449 C  CA  . PRO C 1 20  ? 30.772  17.285  -39.735 1.00 13.44 ? 20  PRO C CA  1 
ATOM   4450 C  C   . PRO C 1 20  ? 31.005  15.886  -40.328 1.00 12.83 ? 20  PRO C C   1 
ATOM   4451 O  O   . PRO C 1 20  ? 30.080  15.361  -40.979 1.00 14.39 ? 20  PRO C O   1 
ATOM   4452 C  CB  . PRO C 1 20  ? 31.096  18.386  -40.745 1.00 14.11 ? 20  PRO C CB  1 
ATOM   4453 C  CG  . PRO C 1 20  ? 31.830  19.468  -39.973 1.00 17.42 ? 20  PRO C CG  1 
ATOM   4454 C  CD  . PRO C 1 20  ? 32.418  18.808  -38.760 1.00 13.20 ? 20  PRO C CD  1 
ATOM   4455 N  N   . SER C 1 21  ? 32.204  15.341  -40.233 1.00 12.05 ? 21  SER C N   1 
ATOM   4456 C  CA  . SER C 1 21  ? 32.468  14.003  -40.890 1.00 11.09 ? 21  SER C CA  1 
ATOM   4457 C  C   . SER C 1 21  ? 31.594  12.936  -40.260 1.00 11.69 ? 21  SER C C   1 
ATOM   4458 O  O   . SER C 1 21  ? 31.372  11.883  -40.896 1.00 11.41 ? 21  SER C O   1 
ATOM   4459 C  CB  . SER C 1 21  ? 33.930  13.623  -40.815 1.00 11.66 ? 21  SER C CB  1 
ATOM   4460 O  OG  . SER C 1 21  ? 34.642  14.434  -41.743 1.00 14.01 ? 21  SER C OG  1 
ATOM   4461 N  N   . CYS C 1 22  ? 31.069  13.201  -39.059 1.00 11.01 ? 22  CYS C N   1 
ATOM   4462 C  CA  . CYS C 1 22  ? 30.233  12.174  -38.363 1.00 10.76 ? 22  CYS C CA  1 
ATOM   4463 C  C   . CYS C 1 22  ? 28.898  12.043  -39.100 1.00 11.36 ? 22  CYS C C   1 
ATOM   4464 O  O   . CYS C 1 22  ? 28.245  10.990  -38.873 1.00 11.45 ? 22  CYS C O   1 
ATOM   4465 C  CB  . CYS C 1 22  ? 30.051  12.484  -36.868 1.00 10.94 ? 22  CYS C CB  1 
ATOM   4466 S  SG  . CYS C 1 22  ? 31.591  12.480  -35.923 1.00 12.86 ? 22  CYS C SG  1 
ATOM   4467 N  N   . GLY C 1 23  ? 28.498  12.979  -39.965 1.00 11.19 ? 23  GLY C N   1 
ATOM   4468 C  CA  . GLY C 1 23  ? 27.295  12.825  -40.823 1.00 11.16 ? 23  GLY C CA  1 
ATOM   4469 C  C   . GLY C 1 23  ? 27.644  12.508  -42.262 1.00 12.75 ? 23  GLY C C   1 
ATOM   4470 O  O   . GLY C 1 23  ? 26.761  12.618  -43.139 1.00 12.37 ? 23  GLY C O   1 
ATOM   4471 N  N   . GLY C 1 24  ? 28.907  12.142  -42.486 1.00 12.08 ? 24  GLY C N   1 
ATOM   4472 C  CA  . GLY C 1 24  ? 29.447  11.984  -43.850 1.00 13.06 ? 24  GLY C CA  1 
ATOM   4473 C  C   . GLY C 1 24  ? 29.439  10.600  -44.377 1.00 13.43 ? 24  GLY C C   1 
ATOM   4474 O  O   . GLY C 1 24  ? 28.738  9.716   -43.830 1.00 14.24 ? 24  GLY C O   1 
ATOM   4475 N  N   . LEU C 1 25  ? 30.288  10.384  -45.366 1.00 13.85 ? 25  LEU C N   1 
ATOM   4476 C  CA  . LEU C 1 25  ? 30.475  9.029   -45.972 1.00 14.25 ? 25  LEU C CA  1 
ATOM   4477 C  C   . LEU C 1 25  ? 31.333  8.169   -45.100 1.00 15.41 ? 25  LEU C C   1 
ATOM   4478 O  O   . LEU C 1 25  ? 32.145  8.613   -44.199 1.00 13.70 ? 25  LEU C O   1 
ATOM   4479 C  CB  . LEU C 1 25  ? 31.072  9.130   -47.416 1.00 16.88 ? 25  LEU C CB  1 
ATOM   4480 C  CG  . LEU C 1 25  ? 30.337  10.108  -48.351 1.00 21.05 ? 25  LEU C CG  1 
ATOM   4481 C  CD1 . LEU C 1 25  ? 31.094  10.191  -49.670 1.00 24.92 ? 25  LEU C CD1 1 
ATOM   4482 C  CD2 . LEU C 1 25  ? 28.903  9.606   -48.506 1.00 26.36 ? 25  LEU C CD2 1 
ATOM   4483 N  N   . LEU C 1 26  ? 31.222  6.876   -45.423 1.00 13.89 ? 26  LEU C N   1 
ATOM   4484 C  CA  . LEU C 1 26  ? 32.142  5.816   -44.961 1.00 13.43 ? 26  LEU C CA  1 
ATOM   4485 C  C   . LEU C 1 26  ? 32.155  5.664   -43.433 1.00 11.80 ? 26  LEU C C   1 
ATOM   4486 O  O   . LEU C 1 26  ? 33.187  5.264   -42.837 1.00 13.00 ? 26  LEU C O   1 
ATOM   4487 C  CB  . LEU C 1 26  ? 33.632  5.935   -45.416 1.00 13.79 ? 26  LEU C CB  1 
ATOM   4488 C  CG  . LEU C 1 26  ? 34.081  5.824   -46.863 1.00 19.14 ? 26  LEU C CG  1 
ATOM   4489 C  CD1 . LEU C 1 26  ? 35.616  5.628   -47.032 1.00 19.08 ? 26  LEU C CD1 1 
ATOM   4490 C  CD2 . LEU C 1 26  ? 33.294  4.930   -47.805 1.00 19.48 ? 26  LEU C CD2 1 
ATOM   4491 N  N   . GLN C 1 27  ? 30.990  5.835   -42.817 1.00 10.03 ? 27  GLN C N   1 
ATOM   4492 C  CA  . GLN C 1 27  ? 30.992  5.717   -41.346 1.00 9.72  ? 27  GLN C CA  1 
ATOM   4493 C  C   . GLN C 1 27  ? 30.998  4.332   -40.735 1.00 9.83  ? 27  GLN C C   1 
ATOM   4494 O  O   . GLN C 1 27  ? 30.312  3.401   -41.260 1.00 12.00 ? 27  GLN C O   1 
ATOM   4495 C  CB  . GLN C 1 27  ? 29.782  6.458   -40.771 1.00 9.07  ? 27  GLN C CB  1 
ATOM   4496 C  CG  . GLN C 1 27  ? 29.829  7.985   -41.063 1.00 9.27  ? 27  GLN C CG  1 
ATOM   4497 C  CD  . GLN C 1 27  ? 31.036  8.632   -40.322 1.00 9.76  ? 27  GLN C CD  1 
ATOM   4498 O  OE1 . GLN C 1 27  ? 30.984  8.880   -39.127 1.00 9.38  ? 27  GLN C OE1 1 
ATOM   4499 N  NE2 . GLN C 1 27  ? 32.149  8.920   -41.084 1.00 8.71  ? 27  GLN C NE2 1 
ATOM   4500 N  N   . SER C 1 28  ? 31.754  4.172   -39.632 1.00 9.16  ? 28  SER C N   1 
ATOM   4501 C  CA  . SER C 1 28  ? 31.870  2.866   -38.880 1.00 9.24  ? 28  SER C CA  1 
ATOM   4502 C  C   . SER C 1 28  ? 31.258  3.123   -37.492 1.00 8.99  ? 28  SER C C   1 
ATOM   4503 O  O   . SER C 1 28  ? 31.173  4.261   -37.056 1.00 10.84 ? 28  SER C O   1 
ATOM   4504 C  CB  . SER C 1 28  ? 33.387  2.479   -38.683 1.00 9.28  ? 28  SER C CB  1 
ATOM   4505 O  OG  . SER C 1 28  ? 33.910  2.315   -40.013 1.00 9.31  ? 28  SER C OG  1 
ATOM   4506 N  N   . PRO C 1 29  ? 30.932  2.073   -36.780 1.00 8.59  ? 29  PRO C N   1 
ATOM   4507 C  CA  . PRO C 1 29  ? 31.018  0.676   -37.126 1.00 7.96  ? 29  PRO C CA  1 
ATOM   4508 C  C   . PRO C 1 29  ? 29.775  0.260   -37.945 1.00 8.63  ? 29  PRO C C   1 
ATOM   4509 O  O   . PRO C 1 29  ? 28.865  1.048   -38.216 1.00 8.89  ? 29  PRO C O   1 
ATOM   4510 C  CB  . PRO C 1 29  ? 30.924  -0.006  -35.762 1.00 8.36  ? 29  PRO C CB  1 
ATOM   4511 C  CG  . PRO C 1 29  ? 29.982  0.892   -34.987 1.00 9.62  ? 29  PRO C CG  1 
ATOM   4512 C  CD  . PRO C 1 29  ? 30.347  2.300   -35.436 1.00 9.21  ? 29  PRO C CD  1 
ATOM   4513 N  N   . ILE C 1 30  ? 29.822  -1.015  -38.336 1.00 8.65  ? 30  ILE C N   1 
ATOM   4514 C  CA  . ILE C 1 30  ? 28.757  -1.584  -39.198 1.00 8.67  ? 30  ILE C CA  1 
ATOM   4515 C  C   . ILE C 1 30  ? 28.464  -2.998  -38.697 1.00 9.14  ? 30  ILE C C   1 
ATOM   4516 O  O   . ILE C 1 30  ? 29.222  -3.609  -37.943 1.00 9.38  ? 30  ILE C O   1 
ATOM   4517 C  CB  . ILE C 1 30  ? 29.217  -1.645  -40.670 1.00 9.02  ? 30  ILE C CB  1 
ATOM   4518 C  CG1 . ILE C 1 30  ? 30.475  -2.535  -40.787 1.00 7.88  ? 30  ILE C CG1 1 
ATOM   4519 C  CG2 . ILE C 1 30  ? 29.479  -0.217  -41.162 1.00 9.28  ? 30  ILE C CG2 1 
ATOM   4520 C  CD1 . ILE C 1 30  ? 30.788  -2.703  -42.275 1.00 9.19  ? 30  ILE C CD1 1 
ATOM   4521 N  N   . ASP C 1 31  ? 27.317  -3.515  -39.199 1.00 9.51  ? 31  ASP C N   1 
ATOM   4522 C  CA  . ASP C 1 31  ? 26.987  -4.934  -39.066 1.00 9.67  ? 31  ASP C CA  1 
ATOM   4523 C  C   . ASP C 1 31  ? 27.590  -5.766  -40.140 1.00 10.58 ? 31  ASP C C   1 
ATOM   4524 O  O   . ASP C 1 31  ? 27.480  -5.475  -41.358 1.00 10.71 ? 31  ASP C O   1 
ATOM   4525 C  CB  . ASP C 1 31  ? 25.481  -5.108  -39.199 1.00 11.03 ? 31  ASP C CB  1 
ATOM   4526 C  CG  . ASP C 1 31  ? 25.067  -6.556  -38.958 1.00 13.44 ? 31  ASP C CG  1 
ATOM   4527 O  OD1 . ASP C 1 31  ? 25.527  -7.158  -37.980 1.00 12.94 ? 31  ASP C OD1 1 
ATOM   4528 O  OD2 . ASP C 1 31  ? 24.192  -7.022  -39.704 1.00 16.65 ? 31  ASP C OD2 1 
ATOM   4529 N  N   . LEU C 1 32  ? 28.255  -6.858  -39.710 1.00 10.41 ? 32  LEU C N   1 
ATOM   4530 C  CA  . LEU C 1 32  ? 28.896  -7.772  -40.632 1.00 12.11 ? 32  LEU C CA  1 
ATOM   4531 C  C   . LEU C 1 32  ? 28.032  -9.002  -40.851 1.00 12.43 ? 32  LEU C C   1 
ATOM   4532 O  O   . LEU C 1 32  ? 27.778  -9.759  -39.932 1.00 15.17 ? 32  LEU C O   1 
ATOM   4533 C  CB  . LEU C 1 32  ? 30.262  -8.249  -40.047 1.00 12.37 ? 32  LEU C CB  1 
ATOM   4534 C  CG  . LEU C 1 32  ? 31.173  -7.052  -39.626 1.00 11.93 ? 32  LEU C CG  1 
ATOM   4535 C  CD1 . LEU C 1 32  ? 32.424  -7.487  -38.793 1.00 13.87 ? 32  LEU C CD1 1 
ATOM   4536 C  CD2 . LEU C 1 32  ? 31.629  -6.144  -40.801 1.00 12.36 ? 32  LEU C CD2 1 
ATOM   4537 N  N   . HIS C 1 33  ? 27.514  -9.148  -42.056 1.00 15.24 ? 33  HIS C N   1 
ATOM   4538 C  CA  . HIS C 1 33  ? 26.469  -10.167 -42.260 1.00 16.65 ? 33  HIS C CA  1 
ATOM   4539 C  C   . HIS C 1 33  ? 26.639  -10.777 -43.639 1.00 17.01 ? 33  HIS C C   1 
ATOM   4540 O  O   . HIS C 1 33  ? 27.216  -10.125 -44.503 1.00 16.95 ? 33  HIS C O   1 
ATOM   4541 C  CB  . HIS C 1 33  ? 25.052  -9.605  -42.000 1.00 20.53 ? 33  HIS C CB  1 
ATOM   4542 C  CG  . HIS C 1 33  ? 24.624  -8.535  -42.954 1.00 19.54 ? 33  HIS C CG  1 
ATOM   4543 N  ND1 . HIS C 1 33  ? 23.896  -8.792  -44.071 1.00 23.48 ? 33  HIS C ND1 1 
ATOM   4544 C  CD2 . HIS C 1 33  ? 24.808  -7.151  -42.918 1.00 20.89 ? 33  HIS C CD2 1 
ATOM   4545 C  CE1 . HIS C 1 33  ? 23.630  -7.624  -44.710 1.00 23.24 ? 33  HIS C CE1 1 
ATOM   4546 N  NE2 . HIS C 1 33  ? 24.174  -6.623  -43.999 1.00 24.37 ? 33  HIS C NE2 1 
ATOM   4547 N  N   A SER C 1 34  ? 26.133  -12.005 -43.851 0.50 19.02 ? 34  SER C N   1 
ATOM   4548 N  N   B SER C 1 34  ? 26.144  -12.012 -43.870 0.50 18.27 ? 34  SER C N   1 
ATOM   4549 C  CA  A SER C 1 34  ? 26.588  -12.848 -44.963 0.50 20.09 ? 34  SER C CA  1 
ATOM   4550 C  CA  B SER C 1 34  ? 26.621  -12.829 -45.009 0.50 18.88 ? 34  SER C CA  1 
ATOM   4551 C  C   A SER C 1 34  ? 26.359  -12.288 -46.333 0.50 19.04 ? 34  SER C C   1 
ATOM   4552 C  C   B SER C 1 34  ? 26.372  -12.262 -46.358 0.50 18.55 ? 34  SER C C   1 
ATOM   4553 O  O   A SER C 1 34  ? 27.235  -12.449 -47.198 0.50 19.24 ? 34  SER C O   1 
ATOM   4554 O  O   B SER C 1 34  ? 27.232  -12.407 -47.242 0.50 19.10 ? 34  SER C O   1 
ATOM   4555 C  CB  A SER C 1 34  ? 26.007  -14.262 -44.878 0.50 22.79 ? 34  SER C CB  1 
ATOM   4556 C  CB  B SER C 1 34  ? 26.073  -14.256 -44.993 0.50 20.27 ? 34  SER C CB  1 
ATOM   4557 O  OG  A SER C 1 34  ? 24.600  -14.207 -44.720 0.50 25.95 ? 34  SER C OG  1 
ATOM   4558 O  OG  B SER C 1 34  ? 26.341  -14.876 -43.761 0.50 20.89 ? 34  SER C OG  1 
ATOM   4559 N  N   . ASP C 1 35  ? 25.223  -11.604 -46.513 1.00 19.73 ? 35  ASP C N   1 
ATOM   4560 C  CA  . ASP C 1 35  ? 24.802  -11.077 -47.800 1.00 23.07 ? 35  ASP C CA  1 
ATOM   4561 C  C   . ASP C 1 35  ? 25.686  -9.944  -48.311 1.00 21.05 ? 35  ASP C C   1 
ATOM   4562 O  O   . ASP C 1 35  ? 25.648  -9.623  -49.509 1.00 25.07 ? 35  ASP C O   1 
ATOM   4563 C  CB  . ASP C 1 35  ? 23.307  -10.632 -47.782 1.00 29.91 ? 35  ASP C CB  1 
ATOM   4564 C  CG  . ASP C 1 35  ? 22.347  -11.780 -47.456 1.00 44.14 ? 35  ASP C CG  1 
ATOM   4565 O  OD1 . ASP C 1 35  ? 22.642  -12.942 -47.825 1.00 50.54 ? 35  ASP C OD1 1 
ATOM   4566 O  OD2 . ASP C 1 35  ? 21.284  -11.528 -46.823 1.00 52.34 ? 35  ASP C OD2 1 
ATOM   4567 N  N   . ILE C 1 36  ? 26.554  -9.364  -47.463 1.00 16.89 ? 36  ILE C N   1 
ATOM   4568 C  CA  . ILE C 1 36  ? 27.479  -8.324  -47.944 1.00 15.41 ? 36  ILE C CA  1 
ATOM   4569 C  C   . ILE C 1 36  ? 28.949  -8.785  -47.900 1.00 16.35 ? 36  ILE C C   1 
ATOM   4570 O  O   . ILE C 1 36  ? 29.837  -7.998  -48.094 1.00 16.26 ? 36  ILE C O   1 
ATOM   4571 C  CB  . ILE C 1 36  ? 27.278  -7.017  -47.164 1.00 16.42 ? 36  ILE C CB  1 
ATOM   4572 C  CG1 . ILE C 1 36  ? 27.494  -7.240  -45.683 1.00 15.36 ? 36  ILE C CG1 1 
ATOM   4573 C  CG2 . ILE C 1 36  ? 25.874  -6.401  -47.520 1.00 17.08 ? 36  ILE C CG2 1 
ATOM   4574 C  CD1 . ILE C 1 36  ? 27.762  -5.962  -44.923 1.00 17.39 ? 36  ILE C CD1 1 
ATOM   4575 N  N   . LEU C 1 37  ? 29.206  -10.041 -47.604 1.00 16.62 ? 37  LEU C N   1 
ATOM   4576 C  CA  . LEU C 1 37  ? 30.603  -10.529 -47.504 1.00 16.19 ? 37  LEU C CA  1 
ATOM   4577 C  C   . LEU C 1 37  ? 31.090  -11.037 -48.831 1.00 17.78 ? 37  LEU C C   1 
ATOM   4578 O  O   . LEU C 1 37  ? 30.315  -11.617 -49.603 1.00 21.23 ? 37  LEU C O   1 
ATOM   4579 C  CB  . LEU C 1 37  ? 30.667  -11.674 -46.504 1.00 17.03 ? 37  LEU C CB  1 
ATOM   4580 C  CG  . LEU C 1 37  ? 30.284  -11.398 -45.058 1.00 17.72 ? 37  LEU C CG  1 
ATOM   4581 C  CD1 . LEU C 1 37  ? 30.631  -12.654 -44.322 1.00 16.86 ? 37  LEU C CD1 1 
ATOM   4582 C  CD2 . LEU C 1 37  ? 30.974  -10.177 -44.462 1.00 16.71 ? 37  LEU C CD2 1 
ATOM   4583 N  N   . GLN C 1 38  ? 32.330  -10.723 -49.195 1.00 15.27 ? 38  GLN C N   1 
ATOM   4584 C  CA  . GLN C 1 38  ? 32.908  -11.250 -50.432 1.00 17.72 ? 38  GLN C CA  1 
ATOM   4585 C  C   . GLN C 1 38  ? 34.369  -11.669 -50.178 1.00 15.56 ? 38  GLN C C   1 
ATOM   4586 O  O   . GLN C 1 38  ? 35.199  -10.891 -49.738 1.00 14.91 ? 38  GLN C O   1 
ATOM   4587 C  CB  . GLN C 1 38  ? 32.840  -10.203 -51.525 1.00 18.00 ? 38  GLN C CB  1 
ATOM   4588 C  CG  . GLN C 1 38  ? 33.183  -10.797 -52.903 1.00 23.19 ? 38  GLN C CG  1 
ATOM   4589 C  CD  . GLN C 1 38  ? 32.914  -9.831  -54.045 1.00 25.91 ? 38  GLN C CD  1 
ATOM   4590 O  OE1 . GLN C 1 38  ? 31.758  -9.719  -54.570 1.00 32.31 ? 38  GLN C OE1 1 
ATOM   4591 N  NE2 . GLN C 1 38  ? 33.929  -9.091  -54.401 1.00 24.72 ? 38  GLN C NE2 1 
ATOM   4592 N  N   . TYR C 1 39  ? 34.698  -12.948 -50.458 1.00 16.68 ? 39  TYR C N   1 
ATOM   4593 C  CA  . TYR C 1 39  ? 36.077  -13.365 -50.397 1.00 16.68 ? 39  TYR C CA  1 
ATOM   4594 C  C   . TYR C 1 39  ? 36.983  -12.537 -51.306 1.00 18.29 ? 39  TYR C C   1 
ATOM   4595 O  O   . TYR C 1 39  ? 36.612  -12.283 -52.482 1.00 19.63 ? 39  TYR C O   1 
ATOM   4596 C  CB  . TYR C 1 39  ? 36.105  -14.890 -50.778 1.00 20.08 ? 39  TYR C CB  1 
ATOM   4597 C  CG  . TYR C 1 39  ? 37.527  -15.331 -50.955 1.00 22.57 ? 39  TYR C CG  1 
ATOM   4598 C  CD1 . TYR C 1 39  ? 38.329  -15.495 -49.850 1.00 22.16 ? 39  TYR C CD1 1 
ATOM   4599 C  CD2 . TYR C 1 39  ? 38.061  -15.554 -52.236 1.00 26.05 ? 39  TYR C CD2 1 
ATOM   4600 C  CE1 . TYR C 1 39  ? 39.649  -15.894 -49.998 1.00 27.19 ? 39  TYR C CE1 1 
ATOM   4601 C  CE2 . TYR C 1 39  ? 39.378  -15.977 -52.398 1.00 28.20 ? 39  TYR C CE2 1 
ATOM   4602 C  CZ  . TYR C 1 39  ? 40.178  -16.132 -51.282 1.00 29.19 ? 39  TYR C CZ  1 
ATOM   4603 O  OH  . TYR C 1 39  ? 41.525  -16.481 -51.441 1.00 29.19 ? 39  TYR C OH  1 
ATOM   4604 N  N   . ASP C 1 40  ? 38.143  -12.116 -50.789 1.00 17.80 ? 40  ASP C N   1 
ATOM   4605 C  CA  . ASP C 1 40  ? 39.095  -11.227 -51.537 1.00 21.76 ? 40  ASP C CA  1 
ATOM   4606 C  C   . ASP C 1 40  ? 40.504  -11.894 -51.404 1.00 22.40 ? 40  ASP C C   1 
ATOM   4607 O  O   . ASP C 1 40  ? 41.070  -11.959 -50.306 1.00 22.58 ? 40  ASP C O   1 
ATOM   4608 C  CB  . ASP C 1 40  ? 39.071  -9.829  -50.914 1.00 20.72 ? 40  ASP C CB  1 
ATOM   4609 C  CG  . ASP C 1 40  ? 40.022  -8.865  -51.546 1.00 23.78 ? 40  ASP C CG  1 
ATOM   4610 O  OD1 . ASP C 1 40  ? 40.826  -9.311  -52.333 1.00 22.34 ? 40  ASP C OD1 1 
ATOM   4611 O  OD2 . ASP C 1 40  ? 39.997  -7.620  -51.256 1.00 27.25 ? 40  ASP C OD2 1 
ATOM   4612 N  N   . ALA C 1 41  ? 41.053  -12.404 -52.518 1.00 21.91 ? 41  ALA C N   1 
ATOM   4613 C  CA  . ALA C 1 41  ? 42.372  -13.112 -52.448 1.00 22.79 ? 41  ALA C CA  1 
ATOM   4614 C  C   . ALA C 1 41  ? 43.527  -12.200 -52.057 1.00 20.69 ? 41  ALA C C   1 
ATOM   4615 O  O   . ALA C 1 41  ? 44.614  -12.648 -51.684 1.00 19.82 ? 41  ALA C O   1 
ATOM   4616 C  CB  . ALA C 1 41  ? 42.660  -13.735 -53.804 1.00 23.78 ? 41  ALA C CB  1 
ATOM   4617 N  N   . SER C 1 42  ? 43.350  -10.888 -52.146 1.00 20.45 ? 42  SER C N   1 
ATOM   4618 C  CA  . SER C 1 42  ? 44.409  -10.000 -51.755 1.00 18.79 ? 42  SER C CA  1 
ATOM   4619 C  C   . SER C 1 42  ? 44.632  -10.012 -50.234 1.00 20.32 ? 42  SER C C   1 
ATOM   4620 O  O   . SER C 1 42  ? 45.604  -9.399  -49.754 1.00 23.06 ? 42  SER C O   1 
ATOM   4621 C  CB  . SER C 1 42  ? 44.123  -8.583  -52.214 1.00 20.95 ? 42  SER C CB  1 
ATOM   4622 O  OG  . SER C 1 42  ? 43.159  -7.943  -51.363 1.00 22.30 ? 42  SER C OG  1 
ATOM   4623 N  N   . LEU C 1 43  ? 43.715  -10.667 -49.487 1.00 19.17 ? 43  LEU C N   1 
ATOM   4624 C  CA  . LEU C 1 43  ? 43.699  -10.482 -48.022 1.00 19.20 ? 43  LEU C CA  1 
ATOM   4625 C  C   . LEU C 1 43  ? 44.522  -11.520 -47.329 1.00 19.14 ? 43  LEU C C   1 
ATOM   4626 O  O   . LEU C 1 43  ? 44.007  -12.465 -46.742 1.00 19.64 ? 43  LEU C O   1 
ATOM   4627 C  CB  . LEU C 1 43  ? 42.260  -10.504 -47.512 1.00 16.16 ? 43  LEU C CB  1 
ATOM   4628 C  CG  . LEU C 1 43  ? 41.443  -9.310  -47.967 1.00 15.79 ? 43  LEU C CG  1 
ATOM   4629 C  CD1 . LEU C 1 43  ? 40.046  -9.289  -47.301 1.00 13.97 ? 43  LEU C CD1 1 
ATOM   4630 C  CD2 . LEU C 1 43  ? 42.112  -7.965  -47.753 1.00 15.35 ? 43  LEU C CD2 1 
ATOM   4631 N  N   . THR C 1 44  ? 45.845  -11.377 -47.495 1.00 20.62 ? 44  THR C N   1 
ATOM   4632 C  CA  . THR C 1 44  ? 46.803  -12.381 -46.975 1.00 21.40 ? 44  THR C CA  1 
ATOM   4633 C  C   . THR C 1 44  ? 46.982  -12.148 -45.476 1.00 25.27 ? 44  THR C C   1 
ATOM   4634 O  O   . THR C 1 44  ? 46.529  -11.097 -44.975 1.00 19.57 ? 44  THR C O   1 
ATOM   4635 C  CB  . THR C 1 44  ? 48.158  -12.237 -47.736 1.00 21.28 ? 44  THR C CB  1 
ATOM   4636 O  OG1 . THR C 1 44  ? 48.519  -10.842 -47.806 1.00 23.51 ? 44  THR C OG1 1 
ATOM   4637 C  CG2 . THR C 1 44  ? 48.026  -12.798 -49.162 1.00 22.60 ? 44  THR C CG2 1 
ATOM   4638 N  N   . PRO C 1 45  ? 47.680  -13.041 -44.751 1.00 24.18 ? 45  PRO C N   1 
ATOM   4639 C  CA  . PRO C 1 45  ? 47.898  -12.791 -43.291 1.00 25.10 ? 45  PRO C CA  1 
ATOM   4640 C  C   . PRO C 1 45  ? 48.730  -11.545 -42.970 1.00 25.98 ? 45  PRO C C   1 
ATOM   4641 O  O   . PRO C 1 45  ? 49.756  -11.288 -43.639 1.00 28.47 ? 45  PRO C O   1 
ATOM   4642 C  CB  . PRO C 1 45  ? 48.604  -14.052 -42.809 1.00 28.00 ? 45  PRO C CB  1 
ATOM   4643 C  CG  . PRO C 1 45  ? 48.206  -15.118 -43.815 1.00 26.64 ? 45  PRO C CG  1 
ATOM   4644 C  CD  . PRO C 1 45  ? 48.155  -14.378 -45.135 1.00 25.25 ? 45  PRO C CD  1 
ATOM   4645 N  N   . LEU C 1 46  ? 48.301  -10.765 -41.976 1.00 24.00 ? 46  LEU C N   1 
ATOM   4646 C  CA  . LEU C 1 46  ? 49.089  -9.668  -41.482 1.00 26.46 ? 46  LEU C CA  1 
ATOM   4647 C  C   . LEU C 1 46  ? 50.216  -10.203 -40.606 1.00 26.21 ? 46  LEU C C   1 
ATOM   4648 O  O   . LEU C 1 46  ? 50.079  -11.272 -40.040 1.00 25.67 ? 46  LEU C O   1 
ATOM   4649 C  CB  . LEU C 1 46  ? 48.254  -8.693  -40.655 1.00 25.19 ? 46  LEU C CB  1 
ATOM   4650 C  CG  . LEU C 1 46  ? 47.144  -7.976  -41.448 1.00 26.77 ? 46  LEU C CG  1 
ATOM   4651 C  CD1 . LEU C 1 46  ? 46.283  -7.155  -40.470 1.00 24.00 ? 46  LEU C CD1 1 
ATOM   4652 C  CD2 . LEU C 1 46  ? 47.664  -7.119  -42.608 1.00 26.95 ? 46  LEU C CD2 1 
ATOM   4653 N  N   . GLU C 1 47  ? 51.281  -9.426  -40.513 1.00 26.44 ? 47  GLU C N   1 
ATOM   4654 C  CA  . GLU C 1 47  ? 52.388  -9.720  -39.649 1.00 28.39 ? 47  GLU C CA  1 
ATOM   4655 C  C   . GLU C 1 47  ? 52.482  -8.649  -38.610 1.00 24.35 ? 47  GLU C C   1 
ATOM   4656 O  O   . GLU C 1 47  ? 52.460  -7.452  -38.911 1.00 23.07 ? 47  GLU C O   1 
ATOM   4657 C  CB  . GLU C 1 47  ? 53.661  -9.736  -40.494 1.00 32.88 ? 47  GLU C CB  1 
ATOM   4658 C  CG  . GLU C 1 47  ? 53.814  -10.930 -41.424 1.00 42.35 ? 47  GLU C CG  1 
ATOM   4659 C  CD  . GLU C 1 47  ? 55.200  -10.960 -42.089 1.00 52.42 ? 47  GLU C CD  1 
ATOM   4660 O  OE1 . GLU C 1 47  ? 56.190  -11.311 -41.386 1.00 55.90 ? 47  GLU C OE1 1 
ATOM   4661 O  OE2 . GLU C 1 47  ? 55.304  -10.612 -43.309 1.00 57.18 ? 47  GLU C OE2 1 
ATOM   4662 N  N   . PHE C 1 48  ? 52.560  -9.018  -37.335 1.00 24.92 ? 48  PHE C N   1 
ATOM   4663 C  CA  . PHE C 1 48  ? 52.547  -8.010  -36.274 1.00 28.06 ? 48  PHE C CA  1 
ATOM   4664 C  C   . PHE C 1 48  ? 53.962  -7.887  -35.736 1.00 28.41 ? 48  PHE C C   1 
ATOM   4665 O  O   . PHE C 1 48  ? 54.495  -8.860  -35.240 1.00 33.34 ? 48  PHE C O   1 
ATOM   4666 C  CB  . PHE C 1 48  ? 51.510  -8.363  -35.157 1.00 28.49 ? 48  PHE C CB  1 
ATOM   4667 C  CG  . PHE C 1 48  ? 50.184  -8.806  -35.724 1.00 25.87 ? 48  PHE C CG  1 
ATOM   4668 C  CD1 . PHE C 1 48  ? 49.259  -7.857  -36.107 1.00 25.52 ? 48  PHE C CD1 1 
ATOM   4669 C  CD2 . PHE C 1 48  ? 49.933  -10.141 -35.985 1.00 26.69 ? 48  PHE C CD2 1 
ATOM   4670 C  CE1 . PHE C 1 48  ? 48.101  -8.250  -36.708 1.00 21.28 ? 48  PHE C CE1 1 
ATOM   4671 C  CE2 . PHE C 1 48  ? 48.745  -10.551 -36.552 1.00 26.17 ? 48  PHE C CE2 1 
ATOM   4672 C  CZ  . PHE C 1 48  ? 47.827  -9.576  -36.901 1.00 21.41 ? 48  PHE C CZ  1 
ATOM   4673 N  N   . GLN C 1 49  ? 54.556  -6.717  -35.900 1.00 23.93 ? 49  GLN C N   1 
ATOM   4674 C  CA  . GLN C 1 49  ? 55.961  -6.502  -35.555 1.00 28.07 ? 49  GLN C CA  1 
ATOM   4675 C  C   . GLN C 1 49  ? 56.196  -5.547  -34.393 1.00 24.60 ? 49  GLN C C   1 
ATOM   4676 O  O   . GLN C 1 49  ? 55.626  -4.438  -34.330 1.00 25.61 ? 49  GLN C O   1 
ATOM   4677 C  CB  . GLN C 1 49  ? 56.706  -6.030  -36.838 1.00 28.78 ? 49  GLN C CB  1 
ATOM   4678 C  CG  . GLN C 1 49  ? 56.446  -6.928  -38.044 1.00 33.20 ? 49  GLN C CG  1 
ATOM   4679 C  CD  . GLN C 1 49  ? 57.538  -6.884  -39.114 1.00 42.59 ? 49  GLN C CD  1 
ATOM   4680 O  OE1 . GLN C 1 49  ? 58.041  -5.801  -39.498 1.00 47.16 ? 49  GLN C OE1 1 
ATOM   4681 N  NE2 . GLN C 1 49  ? 57.897  -8.069  -39.630 1.00 40.25 ? 49  GLN C NE2 1 
ATOM   4682 N  N   . GLY C 1 50  ? 57.179  -5.893  -33.503 1.00 25.08 ? 50  GLY C N   1 
ATOM   4683 C  CA  . GLY C 1 50  ? 57.509  -5.041  -32.360 1.00 25.27 ? 50  GLY C CA  1 
ATOM   4684 C  C   . GLY C 1 50  ? 56.424  -4.944  -31.286 1.00 24.79 ? 50  GLY C C   1 
ATOM   4685 O  O   . GLY C 1 50  ? 56.374  -3.949  -30.524 1.00 24.69 ? 50  GLY C O   1 
ATOM   4686 N  N   . TYR C 1 51  ? 55.585  -5.951  -31.263 1.00 26.30 ? 51  TYR C N   1 
ATOM   4687 C  CA  . TYR C 1 51  ? 54.405  -6.020  -30.370 1.00 30.78 ? 51  TYR C CA  1 
ATOM   4688 C  C   . TYR C 1 51  ? 54.871  -6.431  -28.968 1.00 26.92 ? 51  TYR C C   1 
ATOM   4689 O  O   . TYR C 1 51  ? 54.198  -6.157  -27.978 1.00 23.26 ? 51  TYR C O   1 
ATOM   4690 C  CB  . TYR C 1 51  ? 53.292  -6.968  -30.927 1.00 28.65 ? 51  TYR C CB  1 
ATOM   4691 C  CG  . TYR C 1 51  ? 52.261  -6.278  -31.851 1.00 30.88 ? 51  TYR C CG  1 
ATOM   4692 C  CD1 . TYR C 1 51  ? 50.886  -6.518  -31.677 1.00 27.48 ? 51  TYR C CD1 1 
ATOM   4693 C  CD2 . TYR C 1 51  ? 52.671  -5.378  -32.891 1.00 26.64 ? 51  TYR C CD2 1 
ATOM   4694 C  CE1 . TYR C 1 51  ? 49.951  -5.919  -32.495 1.00 24.56 ? 51  TYR C CE1 1 
ATOM   4695 C  CE2 . TYR C 1 51  ? 51.726  -4.739  -33.719 1.00 24.49 ? 51  TYR C CE2 1 
ATOM   4696 C  CZ  . TYR C 1 51  ? 50.373  -5.033  -33.519 1.00 26.62 ? 51  TYR C CZ  1 
ATOM   4697 O  OH  . TYR C 1 51  ? 49.409  -4.447  -34.319 1.00 21.90 ? 51  TYR C OH  1 
ATOM   4698 N  N   . ASN C 1 52  ? 56.030  -7.087  -28.888 1.00 24.44 ? 52  ASN C N   1 
ATOM   4699 C  CA  . ASN C 1 52  ? 56.434  -7.635  -27.577 1.00 25.22 ? 52  ASN C CA  1 
ATOM   4700 C  C   . ASN C 1 52  ? 57.091  -6.504  -26.781 1.00 28.89 ? 52  ASN C C   1 
ATOM   4701 O  O   . ASN C 1 52  ? 58.266  -6.176  -27.009 1.00 28.22 ? 52  ASN C O   1 
ATOM   4702 C  CB  . ASN C 1 52  ? 57.329  -8.883  -27.764 1.00 28.79 ? 52  ASN C CB  1 
ATOM   4703 C  CG  . ASN C 1 52  ? 57.161  -9.868  -26.630 1.00 33.76 ? 52  ASN C CG  1 
ATOM   4704 O  OD1 . ASN C 1 52  ? 56.973  -9.438  -25.508 1.00 33.39 ? 52  ASN C OD1 1 
ATOM   4705 N  ND2 . ASN C 1 52  ? 57.163  -11.190 -26.909 1.00 34.05 ? 52  ASN C ND2 1 
ATOM   4706 N  N   . LEU C 1 53  ? 56.341  -5.869  -25.895 1.00 24.81 ? 53  LEU C N   1 
ATOM   4707 C  CA  . LEU C 1 53  ? 56.885  -4.659  -25.314 1.00 27.09 ? 53  LEU C CA  1 
ATOM   4708 C  C   . LEU C 1 53  ? 57.515  -5.104  -24.008 1.00 26.79 ? 53  LEU C C   1 
ATOM   4709 O  O   . LEU C 1 53  ? 56.882  -5.794  -23.217 1.00 26.44 ? 53  LEU C O   1 
ATOM   4710 C  CB  . LEU C 1 53  ? 55.795  -3.633  -25.107 1.00 26.81 ? 53  LEU C CB  1 
ATOM   4711 C  CG  . LEU C 1 53  ? 54.871  -3.429  -26.308 1.00 25.54 ? 53  LEU C CG  1 
ATOM   4712 C  CD1 . LEU C 1 53  ? 53.755  -2.500  -25.871 1.00 30.04 ? 53  LEU C CD1 1 
ATOM   4713 C  CD2 . LEU C 1 53  ? 55.665  -2.711  -27.419 1.00 29.11 ? 53  LEU C CD2 1 
ATOM   4714 N  N   . SER C 1 54  ? 58.773  -4.766  -23.814 1.00 30.55 ? 54  SER C N   1 
ATOM   4715 C  CA  . SER C 1 54  ? 59.479  -5.156  -22.588 1.00 34.22 ? 54  SER C CA  1 
ATOM   4716 C  C   . SER C 1 54  ? 58.707  -4.871  -21.270 1.00 32.43 ? 54  SER C C   1 
ATOM   4717 O  O   . SER C 1 54  ? 58.225  -3.724  -21.024 1.00 31.91 ? 54  SER C O   1 
ATOM   4718 C  CB  . SER C 1 54  ? 60.822  -4.413  -22.538 1.00 34.58 ? 54  SER C CB  1 
ATOM   4719 O  OG  . SER C 1 54  ? 61.624  -4.716  -23.670 1.00 40.45 ? 54  SER C OG  1 
ATOM   4720 N  N   . ALA C 1 55  ? 58.683  -5.860  -20.386 1.00 33.21 ? 55  ALA C N   1 
ATOM   4721 C  CA  . ALA C 1 55  ? 58.255  -5.617  -18.970 1.00 33.76 ? 55  ALA C CA  1 
ATOM   4722 C  C   . ALA C 1 55  ? 58.911  -4.406  -18.263 1.00 34.92 ? 55  ALA C C   1 
ATOM   4723 O  O   . ALA C 1 55  ? 58.278  -3.818  -17.335 1.00 26.80 ? 55  ALA C O   1 
ATOM   4724 C  CB  . ALA C 1 55  ? 58.414  -6.866  -18.120 1.00 34.37 ? 55  ALA C CB  1 
ATOM   4725 N  N   . ASN C 1 56  ? 60.133  -4.016  -18.696 1.00 29.89 ? 56  ASN C N   1 
ATOM   4726 C  CA  . ASN C 1 56  ? 60.911  -3.024  -17.919 1.00 32.94 ? 56  ASN C CA  1 
ATOM   4727 C  C   . ASN C 1 56  ? 60.497  -1.637  -18.403 1.00 35.83 ? 56  ASN C C   1 
ATOM   4728 O  O   . ASN C 1 56  ? 60.791  -0.577  -17.773 1.00 34.29 ? 56  ASN C O   1 
ATOM   4729 C  CB  . ASN C 1 56  ? 62.406  -3.218  -18.069 1.00 42.64 ? 56  ASN C CB  1 
ATOM   4730 C  CG  . ASN C 1 56  ? 62.877  -2.944  -19.478 1.00 48.26 ? 56  ASN C CG  1 
ATOM   4731 O  OD1 . ASN C 1 56  ? 62.634  -3.750  -20.395 1.00 55.07 ? 56  ASN C OD1 1 
ATOM   4732 N  ND2 . ASN C 1 56  ? 63.559  -1.797  -19.673 1.00 55.01 ? 56  ASN C ND2 1 
ATOM   4733 N  N   . LYS C 1 57  ? 59.812  -1.639  -19.551 1.00 29.15 ? 57  LYS C N   1 
ATOM   4734 C  CA  . LYS C 1 57  ? 59.342  -0.370  -20.096 1.00 29.89 ? 57  LYS C CA  1 
ATOM   4735 C  C   . LYS C 1 57  ? 57.934  -0.108  -19.549 1.00 25.90 ? 57  LYS C C   1 
ATOM   4736 O  O   . LYS C 1 57  ? 57.312  -0.972  -18.903 1.00 20.46 ? 57  LYS C O   1 
ATOM   4737 C  CB  . LYS C 1 57  ? 59.348  -0.364  -21.627 1.00 30.96 ? 57  LYS C CB  1 
ATOM   4738 C  CG  . LYS C 1 57  ? 60.716  -0.460  -22.265 1.00 35.38 ? 57  LYS C CG  1 
ATOM   4739 C  CD  . LYS C 1 57  ? 60.495  -0.331  -23.752 1.00 39.72 ? 57  LYS C CD  1 
ATOM   4740 C  CE  . LYS C 1 57  ? 61.815  -0.122  -24.467 1.00 40.11 ? 57  LYS C CE  1 
ATOM   4741 N  NZ  . LYS C 1 57  ? 61.559  0.326   -25.866 1.00 42.83 ? 57  LYS C NZ  1 
ATOM   4742 N  N   . GLN C 1 58  ? 57.454  1.127   -19.707 1.00 28.54 ? 58  GLN C N   1 
ATOM   4743 C  CA  . GLN C 1 58  ? 56.105  1.420   -19.263 1.00 26.49 ? 58  GLN C CA  1 
ATOM   4744 C  C   . GLN C 1 58  ? 55.372  2.326   -20.260 1.00 29.26 ? 58  GLN C C   1 
ATOM   4745 O  O   . GLN C 1 58  ? 56.009  3.097   -21.003 1.00 26.28 ? 58  GLN C O   1 
ATOM   4746 C  CB  . GLN C 1 58  ? 56.121  2.058   -17.838 1.00 29.37 ? 58  GLN C CB  1 
ATOM   4747 C  CG  . GLN C 1 58  ? 56.831  3.435   -17.747 1.00 29.79 ? 58  GLN C CG  1 
ATOM   4748 C  CD  . GLN C 1 58  ? 56.732  4.118   -16.340 1.00 33.03 ? 58  GLN C CD  1 
ATOM   4749 O  OE1 . GLN C 1 58  ? 56.467  3.444   -15.327 1.00 31.20 ? 58  GLN C OE1 1 
ATOM   4750 N  NE2 . GLN C 1 58  ? 56.917  5.464   -16.289 1.00 29.63 ? 58  GLN C NE2 1 
ATOM   4751 N  N   . PHE C 1 59  ? 54.026  2.224   -20.221 1.00 25.74 ? 59  PHE C N   1 
ATOM   4752 C  CA  . PHE C 1 59  ? 53.077  2.866   -21.187 1.00 22.28 ? 59  PHE C CA  1 
ATOM   4753 C  C   . PHE C 1 59  ? 51.933  3.575   -20.541 1.00 20.49 ? 59  PHE C C   1 
ATOM   4754 O  O   . PHE C 1 59  ? 51.358  3.058   -19.665 1.00 22.47 ? 59  PHE C O   1 
ATOM   4755 C  CB  . PHE C 1 59  ? 52.722  1.816   -22.282 1.00 22.24 ? 59  PHE C CB  1 
ATOM   4756 C  CG  . PHE C 1 59  ? 53.976  1.222   -22.889 1.00 25.80 ? 59  PHE C CG  1 
ATOM   4757 C  CD1 . PHE C 1 59  ? 54.636  1.905   -23.912 1.00 23.45 ? 59  PHE C CD1 1 
ATOM   4758 C  CD2 . PHE C 1 59  ? 54.562  0.079   -22.377 1.00 23.12 ? 59  PHE C CD2 1 
ATOM   4759 C  CE1 . PHE C 1 59  ? 55.834  1.435   -24.434 1.00 25.94 ? 59  PHE C CE1 1 
ATOM   4760 C  CE2 . PHE C 1 59  ? 55.795  -0.374  -22.881 1.00 24.69 ? 59  PHE C CE2 1 
ATOM   4761 C  CZ  . PHE C 1 59  ? 56.410  0.277   -23.939 1.00 24.12 ? 59  PHE C CZ  1 
ATOM   4762 N  N   . LEU C 1 60  ? 51.654  4.843   -20.915 1.00 17.94 ? 60  LEU C N   1 
ATOM   4763 C  CA  . LEU C 1 60  ? 50.761  5.705   -20.174 1.00 18.91 ? 60  LEU C CA  1 
ATOM   4764 C  C   . LEU C 1 60  ? 49.323  5.291   -20.479 1.00 19.28 ? 60  LEU C C   1 
ATOM   4765 O  O   . LEU C 1 60  ? 48.862  5.275   -21.670 1.00 21.73 ? 60  LEU C O   1 
ATOM   4766 C  CB  . LEU C 1 60  ? 50.984  7.160   -20.625 1.00 19.68 ? 60  LEU C CB  1 
ATOM   4767 C  CG  . LEU C 1 60  ? 50.248  8.293   -19.921 1.00 23.48 ? 60  LEU C CG  1 
ATOM   4768 C  CD1 . LEU C 1 60  ? 50.683  8.265   -18.451 1.00 22.34 ? 60  LEU C CD1 1 
ATOM   4769 C  CD2 . LEU C 1 60  ? 50.438  9.657   -20.634 1.00 26.82 ? 60  LEU C CD2 1 
ATOM   4770 N  N   . LEU C 1 61  ? 48.624  5.049   -19.442 1.00 18.34 ? 61  LEU C N   1 
ATOM   4771 C  CA  . LEU C 1 61  ? 47.187  4.773   -19.510 1.00 19.82 ? 61  LEU C CA  1 
ATOM   4772 C  C   . LEU C 1 61  ? 46.404  5.997   -19.043 1.00 23.09 ? 61  LEU C C   1 
ATOM   4773 O  O   . LEU C 1 61  ? 46.769  6.581   -18.014 1.00 24.37 ? 61  LEU C O   1 
ATOM   4774 C  CB  . LEU C 1 61  ? 46.833  3.569   -18.641 1.00 19.91 ? 61  LEU C CB  1 
ATOM   4775 C  CG  . LEU C 1 61  ? 47.598  2.290   -18.977 1.00 19.65 ? 61  LEU C CG  1 
ATOM   4776 C  CD1 . LEU C 1 61  ? 49.096  2.554   -19.007 1.00 16.78 ? 61  LEU C CD1 1 
ATOM   4777 C  CD2 . LEU C 1 61  ? 47.255  1.174   -18.002 1.00 23.15 ? 61  LEU C CD2 1 
ATOM   4778 N  N   . THR C 1 62  ? 45.385  6.350   -19.810 1.00 19.27 ? 62  THR C N   1 
ATOM   4779 C  CA  . THR C 1 62  ? 44.700  7.634   -19.578 1.00 20.16 ? 62  THR C CA  1 
ATOM   4780 C  C   . THR C 1 62  ? 43.199  7.361   -19.599 1.00 22.22 ? 62  THR C C   1 
ATOM   4781 O  O   . THR C 1 62  ? 42.715  6.646   -20.502 1.00 22.56 ? 62  THR C O   1 
ATOM   4782 C  CB  . THR C 1 62  ? 44.994  8.610   -20.686 1.00 21.85 ? 62  THR C CB  1 
ATOM   4783 O  OG1 . THR C 1 62  ? 46.394  8.872   -20.701 1.00 23.03 ? 62  THR C OG1 1 
ATOM   4784 C  CG2 . THR C 1 62  ? 44.211  9.904   -20.501 1.00 23.81 ? 62  THR C CG2 1 
ATOM   4785 N  N   A ASN C 1 63  ? 42.480  7.918   -18.618 0.50 21.42 ? 63  ASN C N   1 
ATOM   4786 N  N   B ASN C 1 63  ? 42.464  7.845   -18.585 0.50 24.07 ? 63  ASN C N   1 
ATOM   4787 C  CA  A ASN C 1 63  ? 41.078  8.043   -18.708 0.50 18.08 ? 63  ASN C CA  1 
ATOM   4788 C  CA  B ASN C 1 63  ? 41.066  8.059   -18.785 0.50 21.89 ? 63  ASN C CA  1 
ATOM   4789 C  C   A ASN C 1 63  ? 40.760  9.357   -19.373 0.50 21.59 ? 63  ASN C C   1 
ATOM   4790 C  C   B ASN C 1 63  ? 40.918  9.364   -19.438 0.50 25.35 ? 63  ASN C C   1 
ATOM   4791 O  O   A ASN C 1 63  ? 40.886  10.405  -18.719 0.50 18.95 ? 63  ASN C O   1 
ATOM   4792 O  O   B ASN C 1 63  ? 41.275  10.402  -18.840 0.50 23.90 ? 63  ASN C O   1 
ATOM   4793 C  CB  A ASN C 1 63  ? 40.489  8.049   -17.298 0.50 17.45 ? 63  ASN C CB  1 
ATOM   4794 C  CB  B ASN C 1 63  ? 40.269  8.120   -17.491 0.50 24.80 ? 63  ASN C CB  1 
ATOM   4795 C  CG  A ASN C 1 63  ? 38.954  8.235   -17.283 0.50 15.00 ? 63  ASN C CG  1 
ATOM   4796 C  CG  B ASN C 1 63  ? 40.129  6.776   -16.875 0.50 22.93 ? 63  ASN C CG  1 
ATOM   4797 O  OD1 A ASN C 1 63  ? 38.383  8.903   -18.121 0.50 12.46 ? 63  ASN C OD1 1 
ATOM   4798 O  OD1 B ASN C 1 63  ? 41.126  6.089   -16.784 0.50 21.22 ? 63  ASN C OD1 1 
ATOM   4799 N  ND2 A ASN C 1 63  ? 38.335  7.795   -16.192 0.50 12.12 ? 63  ASN C ND2 1 
ATOM   4800 N  ND2 B ASN C 1 63  ? 38.929  6.401   -16.396 0.50 19.24 ? 63  ASN C ND2 1 
ATOM   4801 N  N   . ASN C 1 64  ? 40.404  9.324   -20.659 1.00 20.87 ? 64  ASN C N   1 
ATOM   4802 C  CA  . ASN C 1 64  ? 40.143  10.554  -21.350 1.00 24.40 ? 64  ASN C CA  1 
ATOM   4803 C  C   . ASN C 1 64  ? 38.721  10.885  -21.325 1.00 20.44 ? 64  ASN C C   1 
ATOM   4804 O  O   . ASN C 1 64  ? 38.284  11.865  -21.991 1.00 25.01 ? 64  ASN C O   1 
ATOM   4805 C  CB  . ASN C 1 64  ? 40.683  10.458  -22.737 1.00 22.79 ? 64  ASN C CB  1 
ATOM   4806 C  CG  . ASN C 1 64  ? 39.980  9.426   -23.538 1.00 26.04 ? 64  ASN C CG  1 
ATOM   4807 O  OD1 . ASN C 1 64  ? 39.023  8.740   -23.081 1.00 24.81 ? 64  ASN C OD1 1 
ATOM   4808 N  ND2 . ASN C 1 64  ? 40.493  9.236   -24.745 1.00 26.99 ? 64  ASN C ND2 1 
ATOM   4809 N  N   . GLY C 1 65  ? 37.998  10.172  -20.436 1.00 25.25 ? 65  GLY C N   1 
ATOM   4810 C  CA  . GLY C 1 65  ? 36.591  10.427  -20.155 1.00 26.07 ? 65  GLY C CA  1 
ATOM   4811 C  C   . GLY C 1 65  ? 35.722  9.521   -21.013 1.00 25.92 ? 65  GLY C C   1 
ATOM   4812 O  O   . GLY C 1 65  ? 34.562  9.299   -20.715 1.00 30.42 ? 65  GLY C O   1 
ATOM   4813 N  N   . HIS C 1 66  ? 36.308  9.042   -22.099 1.00 24.67 ? 66  HIS C N   1 
ATOM   4814 C  CA  . HIS C 1 66  ? 35.609  8.192   -23.072 1.00 23.91 ? 66  HIS C CA  1 
ATOM   4815 C  C   . HIS C 1 66  ? 35.894  6.760   -23.027 1.00 22.77 ? 66  HIS C C   1 
ATOM   4816 O  O   . HIS C 1 66  ? 35.035  5.920   -23.341 1.00 29.03 ? 66  HIS C O   1 
ATOM   4817 C  CB  . HIS C 1 66  ? 35.997  8.689   -24.474 1.00 20.59 ? 66  HIS C CB  1 
ATOM   4818 C  CG  . HIS C 1 66  ? 35.666  10.124  -24.716 1.00 19.45 ? 66  HIS C CG  1 
ATOM   4819 N  ND1 . HIS C 1 66  ? 36.602  11.031  -25.028 1.00 23.34 ? 66  HIS C ND1 1 
ATOM   4820 C  CD2 . HIS C 1 66  ? 34.453  10.800  -24.676 1.00 18.05 ? 66  HIS C CD2 1 
ATOM   4821 C  CE1 . HIS C 1 66  ? 36.023  12.233  -25.176 1.00 20.73 ? 66  HIS C CE1 1 
ATOM   4822 N  NE2 . HIS C 1 66  ? 34.706  12.090  -24.961 1.00 21.80 ? 66  HIS C NE2 1 
ATOM   4823 N  N   . SER C 1 67  ? 37.112  6.393   -22.655 1.00 22.13 ? 67  SER C N   1 
ATOM   4824 C  CA  . SER C 1 67  ? 37.530  5.053   -22.565 1.00 17.66 ? 67  SER C CA  1 
ATOM   4825 C  C   . SER C 1 67  ? 38.770  5.002   -21.702 1.00 22.36 ? 67  SER C C   1 
ATOM   4826 O  O   . SER C 1 67  ? 39.101  5.996   -21.059 1.00 27.91 ? 67  SER C O   1 
ATOM   4827 C  CB  . SER C 1 67  ? 37.784  4.374   -23.994 1.00 19.39 ? 67  SER C CB  1 
ATOM   4828 O  OG  . SER C 1 67  ? 38.162  3.021   -23.902 1.00 20.93 ? 67  SER C OG  1 
ATOM   4829 N  N   . VAL C 1 68  ? 39.341  3.852   -21.617 1.00 19.02 ? 68  VAL C N   1 
ATOM   4830 C  CA  . VAL C 1 68  ? 40.734  3.778   -21.150 1.00 23.96 ? 68  VAL C CA  1 
ATOM   4831 C  C   . VAL C 1 68  ? 41.656  3.383   -22.314 1.00 25.92 ? 68  VAL C C   1 
ATOM   4832 O  O   . VAL C 1 68  ? 41.466  2.309   -22.982 1.00 23.60 ? 68  VAL C O   1 
ATOM   4833 C  CB  . VAL C 1 68  ? 40.857  2.848   -19.959 1.00 27.18 ? 68  VAL C CB  1 
ATOM   4834 C  CG1 . VAL C 1 68  ? 40.599  1.419   -20.358 1.00 21.76 ? 68  VAL C CG1 1 
ATOM   4835 C  CG2 . VAL C 1 68  ? 42.236  3.000   -19.323 1.00 26.75 ? 68  VAL C CG2 1 
ATOM   4836 N  N   . LYS C 1 69  ? 42.596  4.322   -22.567 1.00 24.69 ? 69  LYS C N   1 
ATOM   4837 C  CA  . LYS C 1 69  ? 43.572  4.194   -23.678 1.00 21.19 ? 69  LYS C CA  1 
ATOM   4838 C  C   . LYS C 1 69  ? 44.912  3.949   -23.061 1.00 27.54 ? 69  LYS C C   1 
ATOM   4839 O  O   . LYS C 1 69  ? 45.229  4.499   -21.988 1.00 26.31 ? 69  LYS C O   1 
ATOM   4840 C  CB  . LYS C 1 69  ? 43.553  5.448   -24.577 1.00 26.84 ? 69  LYS C CB  1 
ATOM   4841 C  CG  . LYS C 1 69  ? 44.722  6.425   -24.523 1.00 27.22 ? 69  LYS C CG  1 
ATOM   4842 C  CD  . LYS C 1 69  ? 44.413  7.748   -25.216 1.00 28.40 ? 69  LYS C CD  1 
ATOM   4843 C  CE  . LYS C 1 69  ? 45.415  8.840   -24.776 1.00 27.92 ? 69  LYS C CE  1 
ATOM   4844 N  NZ  . LYS C 1 69  ? 45.177  10.166  -25.442 1.00 30.99 ? 69  LYS C NZ  1 
ATOM   4845 N  N   . LEU C 1 70  ? 45.642  3.052   -23.704 1.00 24.54 ? 70  LEU C N   1 
ATOM   4846 C  CA  . LEU C 1 70  ? 47.050  2.877   -23.495 1.00 23.83 ? 70  LEU C CA  1 
ATOM   4847 C  C   . LEU C 1 70  ? 47.843  3.443   -24.660 1.00 24.23 ? 70  LEU C C   1 
ATOM   4848 O  O   . LEU C 1 70  ? 47.663  3.016   -25.823 1.00 22.04 ? 70  LEU C O   1 
ATOM   4849 C  CB  . LEU C 1 70  ? 47.331  1.391   -23.342 1.00 18.63 ? 70  LEU C CB  1 
ATOM   4850 C  CG  . LEU C 1 70  ? 48.714  0.902   -23.016 1.00 25.42 ? 70  LEU C CG  1 
ATOM   4851 C  CD1 . LEU C 1 70  ? 49.023  1.374   -21.601 1.00 22.07 ? 70  LEU C CD1 1 
ATOM   4852 C  CD2 . LEU C 1 70  ? 48.793  -0.630  -23.120 1.00 17.61 ? 70  LEU C CD2 1 
ATOM   4853 N  N   . ASN C 1 71  ? 48.742  4.374   -24.337 1.00 22.87 ? 71  ASN C N   1 
ATOM   4854 C  CA  . ASN C 1 71  ? 49.684  4.889   -25.328 1.00 24.19 ? 71  ASN C CA  1 
ATOM   4855 C  C   . ASN C 1 71  ? 50.581  3.728   -25.858 1.00 21.99 ? 71  ASN C C   1 
ATOM   4856 O  O   . ASN C 1 71  ? 51.011  2.877   -25.097 1.00 25.44 ? 71  ASN C O   1 
ATOM   4857 C  CB  . ASN C 1 71  ? 50.469  6.028   -24.727 1.00 21.83 ? 71  ASN C CB  1 
ATOM   4858 C  CG  . ASN C 1 71  ? 49.713  7.312   -24.814 1.00 26.57 ? 71  ASN C CG  1 
ATOM   4859 O  OD1 . ASN C 1 71  ? 48.469  7.336   -25.124 1.00 24.86 ? 71  ASN C OD1 1 
ATOM   4860 N  ND2 . ASN C 1 71  ? 50.421  8.419   -24.589 1.00 23.18 ? 71  ASN C ND2 1 
ATOM   4861 N  N   . LEU C 1 72  ? 50.864  3.640   -27.190 1.00 18.08 ? 72  LEU C N   1 
ATOM   4862 C  CA  . LEU C 1 72  ? 51.705  2.517   -27.688 1.00 19.03 ? 72  LEU C CA  1 
ATOM   4863 C  C   . LEU C 1 72  ? 52.886  3.146   -28.541 1.00 15.84 ? 72  LEU C C   1 
ATOM   4864 O  O   . LEU C 1 72  ? 52.697  4.260   -29.107 1.00 21.92 ? 72  LEU C O   1 
ATOM   4865 C  CB  . LEU C 1 72  ? 50.908  1.593   -28.636 1.00 18.87 ? 72  LEU C CB  1 
ATOM   4866 C  CG  . LEU C 1 72  ? 49.812  0.636   -28.047 1.00 22.35 ? 72  LEU C CG  1 
ATOM   4867 C  CD1 . LEU C 1 72  ? 48.989  0.071   -29.205 1.00 22.36 ? 72  LEU C CD1 1 
ATOM   4868 C  CD2 . LEU C 1 72  ? 50.407  -0.519  -27.288 1.00 22.84 ? 72  LEU C CD2 1 
ATOM   4869 N  N   . PRO C 1 73  ? 54.022  2.467   -28.650 1.00 22.66 ? 73  PRO C N   1 
ATOM   4870 C  CA  . PRO C 1 73  ? 55.171  3.191   -29.289 1.00 20.00 ? 73  PRO C CA  1 
ATOM   4871 C  C   . PRO C 1 73  ? 55.267  2.898   -30.796 1.00 24.07 ? 73  PRO C C   1 
ATOM   4872 O  O   . PRO C 1 73  ? 54.937  1.770   -31.247 1.00 27.39 ? 73  PRO C O   1 
ATOM   4873 C  CB  . PRO C 1 73  ? 56.372  2.571   -28.575 1.00 22.93 ? 73  PRO C CB  1 
ATOM   4874 C  CG  . PRO C 1 73  ? 55.999  1.112   -28.568 1.00 18.81 ? 73  PRO C CG  1 
ATOM   4875 C  CD  . PRO C 1 73  ? 54.447  1.101   -28.293 1.00 16.69 ? 73  PRO C CD  1 
ATOM   4876 N  N   . SER C 1 74  ? 55.732  3.908   -31.528 1.00 27.62 ? 74  SER C N   1 
ATOM   4877 C  CA  . SER C 1 74  ? 55.786  3.818   -33.001 1.00 28.08 ? 74  SER C CA  1 
ATOM   4878 C  C   . SER C 1 74  ? 56.603  2.653   -33.659 1.00 29.05 ? 74  SER C C   1 
ATOM   4879 O  O   . SER C 1 74  ? 56.449  2.444   -34.870 1.00 29.48 ? 74  SER C O   1 
ATOM   4880 C  CB  . SER C 1 74  ? 56.046  5.176   -33.615 1.00 35.99 ? 74  SER C CB  1 
ATOM   4881 O  OG  . SER C 1 74  ? 57.199  5.786   -33.054 1.00 41.85 ? 74  SER C OG  1 
ATOM   4882 N  N   . ASP C 1 75  ? 57.427  1.883   -32.905 1.00 29.98 ? 75  ASP C N   1 
ATOM   4883 C  CA  . ASP C 1 75  ? 58.122  0.663   -33.405 1.00 27.04 ? 75  ASP C CA  1 
ATOM   4884 C  C   . ASP C 1 75  ? 57.295  -0.576  -33.624 1.00 28.13 ? 75  ASP C C   1 
ATOM   4885 O  O   . ASP C 1 75  ? 57.718  -1.619  -34.238 1.00 24.07 ? 75  ASP C O   1 
ATOM   4886 C  CB  . ASP C 1 75  ? 59.281  0.225   -32.494 1.00 34.89 ? 75  ASP C CB  1 
ATOM   4887 C  CG  . ASP C 1 75  ? 60.591  0.769   -32.948 1.00 36.04 ? 75  ASP C CG  1 
ATOM   4888 O  OD1 . ASP C 1 75  ? 61.520  -0.032  -33.092 1.00 47.21 ? 75  ASP C OD1 1 
ATOM   4889 O  OD2 . ASP C 1 75  ? 60.689  2.004   -33.108 1.00 38.28 ? 75  ASP C OD2 1 
ATOM   4890 N  N   . MET C 1 76  ? 56.111  -0.504  -33.008 1.00 26.38 ? 76  MET C N   1 
ATOM   4891 C  CA  . MET C 1 76  ? 55.150  -1.510  -33.151 1.00 28.12 ? 76  MET C CA  1 
ATOM   4892 C  C   . MET C 1 76  ? 54.491  -1.204  -34.491 1.00 21.59 ? 76  MET C C   1 
ATOM   4893 O  O   . MET C 1 76  ? 54.083  -0.090  -34.723 1.00 20.89 ? 76  MET C O   1 
ATOM   4894 C  CB  . MET C 1 76  ? 54.136  -1.351  -32.036 1.00 30.50 ? 76  MET C CB  1 
ATOM   4895 C  CG  . MET C 1 76  ? 53.620  -2.650  -31.558 1.00 38.48 ? 76  MET C CG  1 
ATOM   4896 S  SD  . MET C 1 76  ? 52.622  -2.197  -30.131 1.00 31.95 ? 76  MET C SD  1 
ATOM   4897 C  CE  . MET C 1 76  ? 50.981  -2.708  -30.660 1.00 33.01 ? 76  MET C CE  1 
ATOM   4898 N  N   . HIS C 1 77  ? 54.486  -2.189  -35.346 1.00 20.38 ? 77  HIS C N   1 
ATOM   4899 C  CA  . HIS C 1 77  ? 53.780  -2.019  -36.637 1.00 23.99 ? 77  HIS C CA  1 
ATOM   4900 C  C   . HIS C 1 77  ? 53.177  -3.201  -37.320 1.00 19.61 ? 77  HIS C C   1 
ATOM   4901 O  O   . HIS C 1 77  ? 53.452  -4.370  -37.054 1.00 17.99 ? 77  HIS C O   1 
ATOM   4902 C  CB  . HIS C 1 77  ? 54.608  -1.232  -37.622 1.00 25.85 ? 77  HIS C CB  1 
ATOM   4903 C  CG  . HIS C 1 77  ? 55.854  -1.904  -38.010 1.00 25.88 ? 77  HIS C CG  1 
ATOM   4904 N  ND1 . HIS C 1 77  ? 57.028  -1.603  -37.423 1.00 29.47 ? 77  HIS C ND1 1 
ATOM   4905 C  CD2 . HIS C 1 77  ? 56.116  -2.869  -38.982 1.00 29.34 ? 77  HIS C CD2 1 
ATOM   4906 C  CE1 . HIS C 1 77  ? 57.997  -2.347  -37.977 1.00 30.23 ? 77  HIS C CE1 1 
ATOM   4907 N  NE2 . HIS C 1 77  ? 57.435  -3.134  -38.936 1.00 33.69 ? 77  HIS C NE2 1 
ATOM   4908 N  N   . ILE C 1 78  ? 52.245  -2.887  -38.240 1.00 18.94 ? 78  ILE C N   1 
ATOM   4909 C  CA  . ILE C 1 78  ? 51.696  -3.911  -39.060 1.00 19.38 ? 78  ILE C CA  1 
ATOM   4910 C  C   . ILE C 1 78  ? 52.460  -3.995  -40.370 1.00 20.33 ? 78  ILE C C   1 
ATOM   4911 O  O   . ILE C 1 78  ? 52.683  -3.007  -41.021 1.00 23.59 ? 78  ILE C O   1 
ATOM   4912 C  CB  . ILE C 1 78  ? 50.202  -3.580  -39.463 1.00 22.86 ? 78  ILE C CB  1 
ATOM   4913 C  CG1 . ILE C 1 78  ? 49.334  -3.493  -38.251 1.00 25.41 ? 78  ILE C CG1 1 
ATOM   4914 C  CG2 . ILE C 1 78  ? 49.660  -4.623  -40.424 1.00 25.79 ? 78  ILE C CG2 1 
ATOM   4915 C  CD1 . ILE C 1 78  ? 47.975  -2.885  -38.526 1.00 23.91 ? 78  ILE C CD1 1 
ATOM   4916 N  N   . GLN C 1 79  ? 52.803  -5.201  -40.728 1.00 21.69 ? 79  GLN C N   1 
ATOM   4917 C  CA  . GLN C 1 79  ? 53.479  -5.514  -41.962 1.00 26.60 ? 79  GLN C CA  1 
ATOM   4918 C  C   . GLN C 1 79  ? 52.442  -6.251  -42.829 1.00 26.16 ? 79  GLN C C   1 
ATOM   4919 O  O   . GLN C 1 79  ? 51.713  -7.142  -42.378 1.00 26.88 ? 79  GLN C O   1 
ATOM   4920 C  CB  . GLN C 1 79  ? 54.706  -6.404  -41.642 1.00 31.55 ? 79  GLN C CB  1 
ATOM   4921 C  CG  . GLN C 1 79  ? 55.555  -6.813  -42.834 1.00 37.38 ? 79  GLN C CG  1 
ATOM   4922 C  CD  . GLN C 1 79  ? 56.146  -5.636  -43.611 1.00 47.31 ? 79  GLN C CD  1 
ATOM   4923 O  OE1 . GLN C 1 79  ? 56.058  -4.461  -43.203 1.00 44.56 ? 79  GLN C OE1 1 
ATOM   4924 N  NE2 . GLN C 1 79  ? 56.763  -5.954  -44.747 1.00 56.27 ? 79  GLN C NE2 1 
ATOM   4925 N  N   . GLY C 1 80  ? 52.347  -5.881  -44.079 1.00 23.67 ? 80  GLY C N   1 
ATOM   4926 C  CA  . GLY C 1 80  ? 51.480  -6.653  -44.976 1.00 25.07 ? 80  GLY C CA  1 
ATOM   4927 C  C   . GLY C 1 80  ? 50.430  -5.802  -45.660 1.00 26.24 ? 80  GLY C C   1 
ATOM   4928 O  O   . GLY C 1 80  ? 49.722  -6.275  -46.570 1.00 28.35 ? 80  GLY C O   1 
ATOM   4929 N  N   . LEU C 1 81  ? 50.316  -4.538  -45.263 1.00 25.34 ? 81  LEU C N   1 
ATOM   4930 C  CA  . LEU C 1 81  ? 49.391  -3.645  -45.957 1.00 24.76 ? 81  LEU C CA  1 
ATOM   4931 C  C   . LEU C 1 81  ? 50.183  -2.848  -46.996 1.00 27.42 ? 81  LEU C C   1 
ATOM   4932 O  O   . LEU C 1 81  ? 51.405  -3.023  -47.131 1.00 32.05 ? 81  LEU C O   1 
ATOM   4933 C  CB  . LEU C 1 81  ? 48.688  -2.731  -44.970 1.00 22.72 ? 81  LEU C CB  1 
ATOM   4934 C  CG  . LEU C 1 81  ? 47.798  -3.387  -43.908 1.00 22.93 ? 81  LEU C CG  1 
ATOM   4935 C  CD1 . LEU C 1 81  ? 47.214  -2.392  -42.868 1.00 20.40 ? 81  LEU C CD1 1 
ATOM   4936 C  CD2 . LEU C 1 81  ? 46.655  -4.069  -44.685 1.00 24.86 ? 81  LEU C CD2 1 
ATOM   4937 N  N   . GLN C 1 82  ? 49.514  -1.955  -47.698 1.00 27.70 ? 82  GLN C N   1 
ATOM   4938 C  CA  . GLN C 1 82  ? 50.194  -1.183  -48.751 1.00 32.76 ? 82  GLN C CA  1 
ATOM   4939 C  C   . GLN C 1 82  ? 51.221  -0.149  -48.262 1.00 32.54 ? 82  GLN C C   1 
ATOM   4940 O  O   . GLN C 1 82  ? 52.066  0.299   -49.026 1.00 29.69 ? 82  GLN C O   1 
ATOM   4941 C  CB  . GLN C 1 82  ? 49.153  -0.562  -49.681 1.00 37.56 ? 82  GLN C CB  1 
ATOM   4942 C  CG  . GLN C 1 82  ? 48.309  -1.639  -50.370 1.00 43.33 ? 82  GLN C CG  1 
ATOM   4943 C  CD  . GLN C 1 82  ? 48.647  -1.787  -51.837 1.00 48.67 ? 82  GLN C CD  1 
ATOM   4944 O  OE1 . GLN C 1 82  ? 47.894  -1.302  -52.684 1.00 53.15 ? 82  GLN C OE1 1 
ATOM   4945 N  NE2 . GLN C 1 82  ? 49.793  -2.429  -52.151 1.00 41.62 ? 82  GLN C NE2 1 
ATOM   4946 N  N   . SER C 1 83  ? 51.115  0.243   -47.000 1.00 24.03 ? 83  SER C N   1 
ATOM   4947 C  CA  . SER C 1 83  ? 52.010  1.179   -46.366 1.00 20.61 ? 83  SER C CA  1 
ATOM   4948 C  C   . SER C 1 83  ? 52.324  0.541   -45.033 1.00 19.32 ? 83  SER C C   1 
ATOM   4949 O  O   . SER C 1 83  ? 51.552  -0.253  -44.555 1.00 16.76 ? 83  SER C O   1 
ATOM   4950 C  CB  . SER C 1 83  ? 51.367  2.534   -46.104 1.00 22.45 ? 83  SER C CB  1 
ATOM   4951 O  OG  . SER C 1 83  ? 51.172  3.246   -47.305 1.00 23.38 ? 83  SER C OG  1 
ATOM   4952 N  N   . ARG C 1 84  ? 53.422  0.945   -44.401 1.00 17.22 ? 84  ARG C N   1 
ATOM   4953 C  CA  . ARG C 1 84  ? 53.630  0.642   -42.972 1.00 19.18 ? 84  ARG C CA  1 
ATOM   4954 C  C   . ARG C 1 84  ? 52.660  1.399   -42.119 1.00 15.07 ? 84  ARG C C   1 
ATOM   4955 O  O   . ARG C 1 84  ? 52.557  2.619   -42.207 1.00 17.57 ? 84  ARG C O   1 
ATOM   4956 C  CB  . ARG C 1 84  ? 55.053  1.069   -42.535 1.00 17.52 ? 84  ARG C CB  1 
ATOM   4957 C  CG  . ARG C 1 84  ? 55.250  0.680   -41.054 1.00 18.54 ? 84  ARG C CG  1 
ATOM   4958 C  CD  . ARG C 1 84  ? 56.662  0.971   -40.627 1.00 19.98 ? 84  ARG C CD  1 
ATOM   4959 N  NE  . ARG C 1 84  ? 57.488  -0.118  -41.110 1.00 18.62 ? 84  ARG C NE  1 
ATOM   4960 C  CZ  . ARG C 1 84  ? 58.810  -0.206  -40.805 1.00 19.66 ? 84  ARG C CZ  1 
ATOM   4961 N  NH1 . ARG C 1 84  ? 59.359  0.784   -40.112 1.00 21.47 ? 84  ARG C NH1 1 
ATOM   4962 N  NH2 . ARG C 1 84  ? 59.523  -1.233  -41.226 1.00 20.66 ? 84  ARG C NH2 1 
ATOM   4963 N  N   . TYR C 1 85  ? 51.980  0.677   -41.192 1.00 17.20 ? 85  TYR C N   1 
ATOM   4964 C  CA  . TYR C 1 85  ? 51.191  1.381   -40.184 1.00 15.85 ? 85  TYR C CA  1 
ATOM   4965 C  C   . TYR C 1 85  ? 51.771  1.090   -38.806 1.00 15.98 ? 85  TYR C C   1 
ATOM   4966 O  O   . TYR C 1 85  ? 51.902  -0.025  -38.448 1.00 15.75 ? 85  TYR C O   1 
ATOM   4967 C  CB  . TYR C 1 85  ? 49.713  0.816   -40.236 1.00 14.91 ? 85  TYR C CB  1 
ATOM   4968 C  CG  . TYR C 1 85  ? 48.956  1.363   -41.434 1.00 14.07 ? 85  TYR C CG  1 
ATOM   4969 C  CD1 . TYR C 1 85  ? 48.166  2.514   -41.308 1.00 13.11 ? 85  TYR C CD1 1 
ATOM   4970 C  CD2 . TYR C 1 85  ? 49.058  0.754   -42.690 1.00 14.65 ? 85  TYR C CD2 1 
ATOM   4971 C  CE1 . TYR C 1 85  ? 47.475  3.023   -42.409 1.00 14.13 ? 85  TYR C CE1 1 
ATOM   4972 C  CE2 . TYR C 1 85  ? 48.379  1.310   -43.792 1.00 15.35 ? 85  TYR C CE2 1 
ATOM   4973 C  CZ  . TYR C 1 85  ? 47.599  2.396   -43.653 1.00 14.74 ? 85  TYR C CZ  1 
ATOM   4974 O  OH  . TYR C 1 85  ? 46.900  2.923   -44.754 1.00 16.77 ? 85  TYR C OH  1 
ATOM   4975 N  N   . SER C 1 86  ? 52.090  2.162   -38.098 1.00 18.60 ? 86  SER C N   1 
ATOM   4976 C  CA  . SER C 1 86  ? 52.722  2.034   -36.810 1.00 19.58 ? 86  SER C CA  1 
ATOM   4977 C  C   . SER C 1 86  ? 51.642  2.242   -35.739 1.00 18.42 ? 86  SER C C   1 
ATOM   4978 O  O   . SER C 1 86  ? 50.809  3.140   -35.829 1.00 22.27 ? 86  SER C O   1 
ATOM   4979 C  CB  . SER C 1 86  ? 53.767  3.121   -36.652 1.00 18.83 ? 86  SER C CB  1 
ATOM   4980 O  OG  . SER C 1 86  ? 54.799  2.958   -37.669 1.00 18.91 ? 86  SER C OG  1 
ATOM   4981 N  N   . ALA C 1 87  ? 51.836  1.519   -34.664 1.00 21.73 ? 87  ALA C N   1 
ATOM   4982 C  CA  . ALA C 1 87  ? 50.958  1.685   -33.483 1.00 20.71 ? 87  ALA C CA  1 
ATOM   4983 C  C   . ALA C 1 87  ? 50.964  3.058   -32.795 1.00 22.96 ? 87  ALA C C   1 
ATOM   4984 O  O   . ALA C 1 87  ? 51.984  3.793   -32.782 1.00 21.57 ? 87  ALA C O   1 
ATOM   4985 C  CB  . ALA C 1 87  ? 51.280  0.547   -32.541 1.00 18.39 ? 87  ALA C CB  1 
ATOM   4986 N  N   . THR C 1 88  ? 49.815  3.486   -32.248 1.00 19.98 ? 88  THR C N   1 
ATOM   4987 C  CA  . THR C 1 88  ? 49.712  4.722   -31.486 1.00 20.92 ? 88  THR C CA  1 
ATOM   4988 C  C   . THR C 1 88  ? 49.074  4.485   -30.134 1.00 23.66 ? 88  THR C C   1 
ATOM   4989 O  O   . THR C 1 88  ? 49.500  5.086   -29.128 1.00 21.59 ? 88  THR C O   1 
ATOM   4990 C  CB  . THR C 1 88  ? 49.101  5.889   -32.225 1.00 20.11 ? 88  THR C CB  1 
ATOM   4991 O  OG1 . THR C 1 88  ? 49.080  7.136   -31.503 1.00 21.53 ? 88  THR C OG1 1 
ATOM   4992 C  CG2 . THR C 1 88  ? 47.687  5.542   -32.720 1.00 17.82 ? 88  THR C CG2 1 
ATOM   4993 N  N   . GLN C 1 89  ? 48.074  3.593   -30.092 1.00 20.92 ? 89  GLN C N   1 
ATOM   4994 C  CA  . GLN C 1 89  ? 47.380  3.271   -28.828 1.00 23.44 ? 89  GLN C CA  1 
ATOM   4995 C  C   . GLN C 1 89  ? 46.396  2.190   -29.047 1.00 22.63 ? 89  GLN C C   1 
ATOM   4996 O  O   . GLN C 1 89  ? 45.996  1.937   -30.177 1.00 21.08 ? 89  GLN C O   1 
ATOM   4997 C  CB  . GLN C 1 89  ? 46.609  4.458   -28.334 1.00 23.07 ? 89  GLN C CB  1 
ATOM   4998 C  CG  . GLN C 1 89  ? 45.707  5.066   -29.382 1.00 28.09 ? 89  GLN C CG  1 
ATOM   4999 C  CD  . GLN C 1 89  ? 44.451  5.599   -28.815 1.00 23.00 ? 89  GLN C CD  1 
ATOM   5000 O  OE1 . GLN C 1 89  ? 43.553  4.822   -28.423 1.00 29.57 ? 89  GLN C OE1 1 
ATOM   5001 N  NE2 . GLN C 1 89  ? 44.310  6.916   -28.886 1.00 23.60 ? 89  GLN C NE2 1 
ATOM   5002 N  N   . LEU C 1 90  ? 45.931  1.633   -27.943 1.00 20.76 ? 90  LEU C N   1 
ATOM   5003 C  CA  . LEU C 1 90  ? 44.730  0.830   -27.962 1.00 20.00 ? 90  LEU C CA  1 
ATOM   5004 C  C   . LEU C 1 90  ? 43.793  1.238   -26.899 1.00 23.46 ? 90  LEU C C   1 
ATOM   5005 O  O   . LEU C 1 90  ? 44.140  2.067   -26.005 1.00 21.29 ? 90  LEU C O   1 
ATOM   5006 C  CB  . LEU C 1 90  ? 45.097  -0.594  -27.702 1.00 16.16 ? 90  LEU C CB  1 
ATOM   5007 C  CG  . LEU C 1 90  ? 45.908  -0.910  -26.393 1.00 20.14 ? 90  LEU C CG  1 
ATOM   5008 C  CD1 . LEU C 1 90  ? 45.019  -0.984  -25.147 1.00 18.89 ? 90  LEU C CD1 1 
ATOM   5009 C  CD2 . LEU C 1 90  ? 46.435  -2.269  -26.619 1.00 14.85 ? 90  LEU C CD2 1 
ATOM   5010 N  N   . HIS C 1 91  ? 42.575  0.655   -26.997 1.00 17.25 ? 91  HIS C N   1 
ATOM   5011 C  CA  . HIS C 1 91  ? 41.517  1.054   -26.101 1.00 18.25 ? 91  HIS C CA  1 
ATOM   5012 C  C   . HIS C 1 91  ? 40.362  0.098   -26.308 1.00 18.73 ? 91  HIS C C   1 
ATOM   5013 O  O   . HIS C 1 91  ? 40.424  -0.834  -27.114 1.00 17.64 ? 91  HIS C O   1 
ATOM   5014 C  CB  . HIS C 1 91  ? 41.136  2.443   -26.370 1.00 17.46 ? 91  HIS C CB  1 
ATOM   5015 C  CG  . HIS C 1 91  ? 40.589  2.633   -27.748 1.00 17.08 ? 91  HIS C CG  1 
ATOM   5016 N  ND1 . HIS C 1 91  ? 41.235  3.370   -28.669 1.00 18.30 ? 91  HIS C ND1 1 
ATOM   5017 C  CD2 . HIS C 1 91  ? 39.400  2.191   -28.322 1.00 18.41 ? 91  HIS C CD2 1 
ATOM   5018 C  CE1 . HIS C 1 91  ? 40.499  3.417   -29.788 1.00 16.69 ? 91  HIS C CE1 1 
ATOM   5019 N  NE2 . HIS C 1 91  ? 39.380  2.671   -29.564 1.00 13.65 ? 91  HIS C NE2 1 
ATOM   5020 N  N   . LEU C 1 92  ? 39.322  0.278   -25.458 1.00 17.54 ? 92  LEU C N   1 
ATOM   5021 C  CA  . LEU C 1 92  ? 38.243  -0.753  -25.425 1.00 19.89 ? 92  LEU C CA  1 
ATOM   5022 C  C   . LEU C 1 92  ? 36.915  -0.053  -25.507 1.00 13.74 ? 92  LEU C C   1 
ATOM   5023 O  O   . LEU C 1 92  ? 36.786  1.097   -25.257 1.00 14.17 ? 92  LEU C O   1 
ATOM   5024 C  CB  . LEU C 1 92  ? 38.323  -1.594  -24.141 1.00 18.99 ? 92  LEU C CB  1 
ATOM   5025 C  CG  . LEU C 1 92  ? 39.426  -2.665  -24.194 1.00 20.74 ? 92  LEU C CG  1 
ATOM   5026 C  CD1 . LEU C 1 92  ? 40.358  -2.499  -22.997 1.00 26.32 ? 92  LEU C CD1 1 
ATOM   5027 C  CD2 . LEU C 1 92  ? 39.012  -4.080  -24.213 1.00 22.12 ? 92  LEU C CD2 1 
ATOM   5028 N  N   . HIS C 1 93  ? 35.891  -0.807  -25.926 1.00 15.49 ? 93  HIS C N   1 
ATOM   5029 C  CA  . HIS C 1 93  ? 34.501  -0.321  -25.980 1.00 14.92 ? 93  HIS C CA  1 
ATOM   5030 C  C   . HIS C 1 93  ? 33.644  -1.425  -25.360 1.00 10.90 ? 93  HIS C C   1 
ATOM   5031 O  O   . HIS C 1 93  ? 33.850  -2.631  -25.590 1.00 11.90 ? 93  HIS C O   1 
ATOM   5032 C  CB  . HIS C 1 93  ? 34.001  -0.021  -27.417 1.00 11.50 ? 93  HIS C CB  1 
ATOM   5033 C  CG  . HIS C 1 93  ? 34.836  0.987   -28.162 1.00 10.46 ? 93  HIS C CG  1 
ATOM   5034 N  ND1 . HIS C 1 93  ? 34.595  2.310   -28.108 1.00 11.81 ? 93  HIS C ND1 1 
ATOM   5035 C  CD2 . HIS C 1 93  ? 35.923  0.820   -29.018 1.00 10.90 ? 93  HIS C CD2 1 
ATOM   5036 C  CE1 . HIS C 1 93  ? 35.493  2.960   -28.873 1.00 10.79 ? 93  HIS C CE1 1 
ATOM   5037 N  NE2 . HIS C 1 93  ? 36.301  2.046   -29.434 1.00 9.76  ? 93  HIS C NE2 1 
ATOM   5038 N  N   . TRP C 1 94  ? 32.747  -0.977  -24.498 1.00 13.34 ? 94  TRP C N   1 
ATOM   5039 C  CA  . TRP C 1 94  ? 31.944  -1.862  -23.680 1.00 14.30 ? 94  TRP C CA  1 
ATOM   5040 C  C   . TRP C 1 94  ? 30.507  -1.371  -23.486 1.00 13.31 ? 94  TRP C C   1 
ATOM   5041 O  O   . TRP C 1 94  ? 30.158  -0.213  -23.698 1.00 13.83 ? 94  TRP C O   1 
ATOM   5042 C  CB  . TRP C 1 94  ? 32.651  -2.379  -22.335 1.00 16.28 ? 94  TRP C CB  1 
ATOM   5043 C  CG  . TRP C 1 94  ? 32.921  -1.269  -21.403 1.00 19.36 ? 94  TRP C CG  1 
ATOM   5044 C  CD1 . TRP C 1 94  ? 32.115  -0.806  -20.393 1.00 16.53 ? 94  TRP C CD1 1 
ATOM   5045 C  CD2 . TRP C 1 94  ? 34.132  -0.441  -21.346 1.00 16.35 ? 94  TRP C CD2 1 
ATOM   5046 N  NE1 . TRP C 1 94  ? 32.664  0.277   -19.778 1.00 17.42 ? 94  TRP C NE1 1 
ATOM   5047 C  CE2 . TRP C 1 94  ? 33.928  0.516   -20.273 1.00 19.50 ? 94  TRP C CE2 1 
ATOM   5048 C  CE3 . TRP C 1 94  ? 35.328  -0.383  -22.095 1.00 18.91 ? 94  TRP C CE3 1 
ATOM   5049 C  CZ2 . TRP C 1 94  ? 34.854  1.493   -19.961 1.00 20.26 ? 94  TRP C CZ2 1 
ATOM   5050 C  CZ3 . TRP C 1 94  ? 36.284  0.536   -21.713 1.00 17.67 ? 94  TRP C CZ3 1 
ATOM   5051 C  CH2 . TRP C 1 94  ? 36.055  1.486   -20.696 1.00 19.84 ? 94  TRP C CH2 1 
ATOM   5052 N  N   . GLY C 1 95  ? 29.746  -2.341  -22.952 1.00 15.96 ? 95  GLY C N   1 
ATOM   5053 C  CA  . GLY C 1 95  ? 28.321  -2.123  -22.548 1.00 16.12 ? 95  GLY C CA  1 
ATOM   5054 C  C   . GLY C 1 95  ? 28.134  -1.720  -21.051 1.00 17.27 ? 95  GLY C C   1 
ATOM   5055 O  O   . GLY C 1 95  ? 28.672  -0.703  -20.549 1.00 15.41 ? 95  GLY C O   1 
ATOM   5056 N  N   . ASN C 1 96  ? 27.210  -2.435  -20.406 1.00 18.91 ? 96  ASN C N   1 
ATOM   5057 C  CA  . ASN C 1 96  ? 26.922  -2.161  -18.959 1.00 20.13 ? 96  ASN C CA  1 
ATOM   5058 C  C   . ASN C 1 96  ? 26.457  -3.475  -18.327 1.00 19.37 ? 96  ASN C C   1 
ATOM   5059 O  O   . ASN C 1 96  ? 26.238  -4.492  -18.999 1.00 19.02 ? 96  ASN C O   1 
ATOM   5060 C  CB  . ASN C 1 96  ? 25.959  -0.984  -18.767 1.00 20.09 ? 96  ASN C CB  1 
ATOM   5061 C  CG  . ASN C 1 96  ? 24.519  -1.313  -19.154 1.00 24.54 ? 96  ASN C CG  1 
ATOM   5062 O  OD1 . ASN C 1 96  ? 23.769  -1.868  -18.370 1.00 24.94 ? 96  ASN C OD1 1 
ATOM   5063 N  ND2 . ASN C 1 96  ? 24.118  -0.891  -20.363 1.00 24.98 ? 96  ASN C ND2 1 
ATOM   5064 N  N   . PRO C 1 97  ? 26.425  -3.529  -16.969 1.00 21.33 ? 97  PRO C N   1 
ATOM   5065 C  CA  . PRO C 1 97  ? 26.134  -4.808  -16.400 1.00 19.71 ? 97  PRO C CA  1 
ATOM   5066 C  C   . PRO C 1 97  ? 24.721  -5.331  -16.646 1.00 19.04 ? 97  PRO C C   1 
ATOM   5067 O  O   . PRO C 1 97  ? 24.534  -6.517  -16.699 1.00 21.28 ? 97  PRO C O   1 
ATOM   5068 C  CB  . PRO C 1 97  ? 26.376  -4.584  -14.890 1.00 20.69 ? 97  PRO C CB  1 
ATOM   5069 C  CG  . PRO C 1 97  ? 27.350  -3.447  -14.853 1.00 21.14 ? 97  PRO C CG  1 
ATOM   5070 C  CD  . PRO C 1 97  ? 26.951  -2.564  -15.973 1.00 21.70 ? 97  PRO C CD  1 
ATOM   5071 N  N   . ASN C 1 98  ? 23.813  -4.427  -16.860 1.00 19.99 ? 98  ASN C N   1 
ATOM   5072 C  CA  . ASN C 1 98  ? 22.397  -4.804  -17.189 1.00 22.97 ? 98  ASN C CA  1 
ATOM   5073 C  C   . ASN C 1 98  ? 22.231  -5.235  -18.660 1.00 24.21 ? 98  ASN C C   1 
ATOM   5074 O  O   . ASN C 1 98  ? 21.304  -5.976  -19.025 1.00 24.88 ? 98  ASN C O   1 
ATOM   5075 C  CB  . ASN C 1 98  ? 21.504  -3.634  -16.872 1.00 23.89 ? 98  ASN C CB  1 
ATOM   5076 C  CG  . ASN C 1 98  ? 21.492  -3.322  -15.399 1.00 32.01 ? 98  ASN C CG  1 
ATOM   5077 O  OD1 . ASN C 1 98  ? 21.533  -4.233  -14.561 1.00 34.19 ? 98  ASN C OD1 1 
ATOM   5078 N  ND2 . ASN C 1 98  ? 21.500  -2.044  -15.075 1.00 31.20 ? 98  ASN C ND2 1 
ATOM   5079 N  N   . ASP C 1 99  ? 23.169  -4.819  -19.505 1.00 20.47 ? 99  ASP C N   1 
ATOM   5080 C  CA  . ASP C 1 99  ? 23.099  -5.225  -20.921 1.00 19.85 ? 99  ASP C CA  1 
ATOM   5081 C  C   . ASP C 1 99  ? 24.560  -5.325  -21.431 1.00 18.06 ? 99  ASP C C   1 
ATOM   5082 O  O   . ASP C 1 99  ? 25.061  -4.327  -22.012 1.00 16.99 ? 99  ASP C O   1 
ATOM   5083 C  CB  . ASP C 1 99  ? 22.316  -4.133  -21.642 1.00 20.76 ? 99  ASP C CB  1 
ATOM   5084 C  CG  . ASP C 1 99  ? 21.882  -4.524  -23.054 1.00 20.78 ? 99  ASP C CG  1 
ATOM   5085 O  OD1 . ASP C 1 99  ? 21.948  -5.700  -23.402 1.00 22.20 ? 99  ASP C OD1 1 
ATOM   5086 O  OD2 . ASP C 1 99  ? 21.501  -3.615  -23.783 1.00 22.50 ? 99  ASP C OD2 1 
ATOM   5087 N  N   . PRO C 1 100 ? 25.196  -6.455  -21.189 1.00 18.60 ? 100 PRO C N   1 
ATOM   5088 C  CA  . PRO C 1 100 ? 26.660  -6.545  -21.354 1.00 18.18 ? 100 PRO C CA  1 
ATOM   5089 C  C   . PRO C 1 100 ? 27.009  -6.945  -22.804 1.00 17.54 ? 100 PRO C C   1 
ATOM   5090 O  O   . PRO C 1 100 ? 27.592  -7.992  -23.089 1.00 19.17 ? 100 PRO C O   1 
ATOM   5091 C  CB  . PRO C 1 100 ? 27.054  -7.599  -20.313 1.00 18.82 ? 100 PRO C CB  1 
ATOM   5092 C  CG  . PRO C 1 100 ? 25.891  -8.550  -20.246 1.00 22.13 ? 100 PRO C CG  1 
ATOM   5093 C  CD  . PRO C 1 100 ? 24.666  -7.663  -20.523 1.00 18.57 ? 100 PRO C CD  1 
ATOM   5094 N  N   . HIS C 1 101 ? 26.631  -6.047  -23.707 1.00 16.65 ? 101 HIS C N   1 
ATOM   5095 C  CA  . HIS C 1 101 ? 26.802  -6.298  -25.164 1.00 16.15 ? 101 HIS C CA  1 
ATOM   5096 C  C   . HIS C 1 101 ? 27.189  -4.995  -25.817 1.00 18.84 ? 101 HIS C C   1 
ATOM   5097 O  O   . HIS C 1 101 ? 26.353  -4.345  -26.492 1.00 19.93 ? 101 HIS C O   1 
ATOM   5098 C  CB  . HIS C 1 101 ? 25.441  -6.837  -25.745 1.00 17.98 ? 101 HIS C CB  1 
ATOM   5099 C  CG  . HIS C 1 101 ? 24.907  -8.047  -24.973 1.00 18.69 ? 101 HIS C CG  1 
ATOM   5100 N  ND1 . HIS C 1 101 ? 25.444  -9.281  -25.091 1.00 21.17 ? 101 HIS C ND1 1 
ATOM   5101 C  CD2 . HIS C 1 101 ? 23.884  -8.158  -24.025 1.00 20.83 ? 101 HIS C CD2 1 
ATOM   5102 C  CE1 . HIS C 1 101 ? 24.790  -10.139 -24.279 1.00 22.12 ? 101 HIS C CE1 1 
ATOM   5103 N  NE2 . HIS C 1 101 ? 23.835  -9.453  -23.630 1.00 22.67 ? 101 HIS C NE2 1 
ATOM   5104 N  N   . GLY C 1 102 ? 28.464  -4.578  -25.657 1.00 16.12 ? 102 GLY C N   1 
ATOM   5105 C  CA  . GLY C 1 102 ? 28.883  -3.264  -26.066 1.00 14.73 ? 102 GLY C CA  1 
ATOM   5106 C  C   . GLY C 1 102 ? 30.029  -3.176  -27.074 1.00 12.43 ? 102 GLY C C   1 
ATOM   5107 O  O   . GLY C 1 102 ? 30.660  -2.083  -27.176 1.00 13.50 ? 102 GLY C O   1 
ATOM   5108 N  N   . SER C 1 103 ? 30.136  -4.250  -27.869 1.00 11.94 ? 103 SER C N   1 
ATOM   5109 C  CA  . SER C 1 103 ? 31.016  -4.132  -29.089 1.00 12.11 ? 103 SER C CA  1 
ATOM   5110 C  C   . SER C 1 103 ? 30.497  -3.033  -30.008 1.00 13.10 ? 103 SER C C   1 
ATOM   5111 O  O   . SER C 1 103 ? 29.255  -2.640  -30.004 1.00 11.95 ? 103 SER C O   1 
ATOM   5112 C  CB  . SER C 1 103 ? 31.196  -5.455  -29.789 1.00 12.46 ? 103 SER C CB  1 
ATOM   5113 O  OG  . SER C 1 103 ? 29.956  -5.813  -30.473 1.00 10.96 ? 103 SER C OG  1 
ATOM   5114 N  N   . GLU C 1 104 ? 31.405  -2.557  -30.863 1.00 10.87 ? 104 GLU C N   1 
ATOM   5115 C  CA  . GLU C 1 104 ? 31.013  -1.573  -31.840 1.00 10.65 ? 104 GLU C CA  1 
ATOM   5116 C  C   . GLU C 1 104 ? 30.510  -2.292  -33.114 1.00 10.58 ? 104 GLU C C   1 
ATOM   5117 O  O   . GLU C 1 104 ? 29.355  -2.115  -33.563 1.00 10.91 ? 104 GLU C O   1 
ATOM   5118 C  CB  . GLU C 1 104 ? 32.165  -0.632  -32.207 1.00 10.99 ? 104 GLU C CB  1 
ATOM   5119 C  CG  . GLU C 1 104 ? 32.778  0.029   -30.960 1.00 11.28 ? 104 GLU C CG  1 
ATOM   5120 C  CD  . GLU C 1 104 ? 33.047  1.467   -31.230 1.00 11.90 ? 104 GLU C CD  1 
ATOM   5121 O  OE1 . GLU C 1 104 ? 34.120  1.702   -31.842 1.00 12.88 ? 104 GLU C OE1 1 
ATOM   5122 O  OE2 . GLU C 1 104 ? 32.226  2.396   -31.035 1.00 11.74 ? 104 GLU C OE2 1 
ATOM   5123 N  N   . HIS C 1 105 ? 31.345  -3.041  -33.749 1.00 11.30 ? 105 HIS C N   1 
ATOM   5124 C  CA  . HIS C 1 105 ? 30.837  -3.962  -34.811 1.00 10.84 ? 105 HIS C CA  1 
ATOM   5125 C  C   . HIS C 1 105 ? 29.942  -5.067  -34.291 1.00 11.21 ? 105 HIS C C   1 
ATOM   5126 O  O   . HIS C 1 105 ? 30.138  -5.585  -33.180 1.00 13.90 ? 105 HIS C O   1 
ATOM   5127 C  CB  . HIS C 1 105 ? 32.025  -4.585  -35.577 1.00 11.01 ? 105 HIS C CB  1 
ATOM   5128 C  CG  . HIS C 1 105 ? 32.840  -3.554  -36.291 1.00 10.33 ? 105 HIS C CG  1 
ATOM   5129 N  ND1 . HIS C 1 105 ? 33.864  -2.876  -35.672 1.00 11.54 ? 105 HIS C ND1 1 
ATOM   5130 C  CD2 . HIS C 1 105 ? 32.705  -3.019  -37.558 1.00 9.44  ? 105 HIS C CD2 1 
ATOM   5131 C  CE1 . HIS C 1 105 ? 34.394  -1.983  -36.513 1.00 11.75 ? 105 HIS C CE1 1 
ATOM   5132 N  NE2 . HIS C 1 105 ? 33.696  -2.061  -37.706 1.00 10.30 ? 105 HIS C NE2 1 
ATOM   5133 N  N   . THR C 1 106 ? 28.987  -5.433  -35.114 1.00 9.87  ? 106 THR C N   1 
ATOM   5134 C  CA  . THR C 1 106 ? 28.151  -6.584  -34.826 1.00 10.10 ? 106 THR C CA  1 
ATOM   5135 C  C   . THR C 1 106 ? 28.321  -7.602  -35.958 1.00 10.18 ? 106 THR C C   1 
ATOM   5136 O  O   . THR C 1 106 ? 28.789  -7.275  -37.078 1.00 10.36 ? 106 THR C O   1 
ATOM   5137 C  CB  . THR C 1 106 ? 26.639  -6.147  -34.745 1.00 10.05 ? 106 THR C CB  1 
ATOM   5138 O  OG1 . THR C 1 106 ? 26.211  -5.532  -36.001 1.00 11.07 ? 106 THR C OG1 1 
ATOM   5139 C  CG2 . THR C 1 106 ? 26.455  -5.133  -33.621 1.00 12.03 ? 106 THR C CG2 1 
ATOM   5140 N  N   . VAL C 1 107 ? 27.972  -8.876  -35.630 1.00 10.95 ? 107 VAL C N   1 
ATOM   5141 C  CA  . VAL C 1 107 ? 28.001  -9.958  -36.571 1.00 11.87 ? 107 VAL C CA  1 
ATOM   5142 C  C   . VAL C 1 107 ? 26.623  -10.585 -36.658 1.00 11.80 ? 107 VAL C C   1 
ATOM   5143 O  O   . VAL C 1 107 ? 26.109  -11.067 -35.602 1.00 13.47 ? 107 VAL C O   1 
ATOM   5144 C  CB  . VAL C 1 107 ? 29.058  -11.005 -36.184 1.00 13.39 ? 107 VAL C CB  1 
ATOM   5145 C  CG1 . VAL C 1 107 ? 29.071  -12.073 -37.241 1.00 13.06 ? 107 VAL C CG1 1 
ATOM   5146 C  CG2 . VAL C 1 107 ? 30.459  -10.347 -36.069 1.00 14.74 ? 107 VAL C CG2 1 
ATOM   5147 N  N   . SER C 1 108 ? 26.033  -10.565 -37.861 1.00 12.47 ? 108 SER C N   1 
ATOM   5148 C  CA  . SER C 1 108 ? 24.638  -11.028 -38.041 1.00 13.54 ? 108 SER C CA  1 
ATOM   5149 C  C   . SER C 1 108 ? 23.703  -10.391 -37.006 1.00 13.19 ? 108 SER C C   1 
ATOM   5150 O  O   . SER C 1 108 ? 22.792  -11.108 -36.455 1.00 12.76 ? 108 SER C O   1 
ATOM   5151 C  CB  . SER C 1 108 ? 24.526  -12.549 -37.949 1.00 14.48 ? 108 SER C CB  1 
ATOM   5152 O  OG  . SER C 1 108 ? 25.431  -13.128 -38.850 1.00 19.35 ? 108 SER C OG  1 
ATOM   5153 N  N   . GLY C 1 109 ? 23.878  -9.101  -36.775 1.00 10.89 ? 109 GLY C N   1 
ATOM   5154 C  CA  . GLY C 1 109 ? 23.007  -8.336  -35.914 1.00 12.77 ? 109 GLY C CA  1 
ATOM   5155 C  C   . GLY C 1 109 ? 23.348  -8.423  -34.439 1.00 12.94 ? 109 GLY C C   1 
ATOM   5156 O  O   . GLY C 1 109 ? 22.755  -7.694  -33.645 1.00 16.95 ? 109 GLY C O   1 
ATOM   5157 N  N   . GLN C 1 110 ? 24.307  -9.261  -34.081 1.00 13.42 ? 110 GLN C N   1 
ATOM   5158 C  CA  . GLN C 1 110 ? 24.608  -9.515  -32.684 1.00 14.89 ? 110 GLN C CA  1 
ATOM   5159 C  C   . GLN C 1 110 ? 25.833  -8.747  -32.162 1.00 13.45 ? 110 GLN C C   1 
ATOM   5160 O  O   . GLN C 1 110 ? 26.893  -8.789  -32.813 1.00 12.85 ? 110 GLN C O   1 
ATOM   5161 C  CB  . GLN C 1 110 ? 24.880  -11.036 -32.506 1.00 15.57 ? 110 GLN C CB  1 
ATOM   5162 C  CG  . GLN C 1 110 ? 23.823  -11.965 -33.098 1.00 17.66 ? 110 GLN C CG  1 
ATOM   5163 C  CD  . GLN C 1 110 ? 22.436  -11.555 -32.651 1.00 20.11 ? 110 GLN C CD  1 
ATOM   5164 O  OE1 . GLN C 1 110 ? 22.189  -11.448 -31.457 1.00 18.82 ? 110 GLN C OE1 1 
ATOM   5165 N  NE2 . GLN C 1 110 ? 21.590  -11.145 -33.634 1.00 19.70 ? 110 GLN C NE2 1 
ATOM   5166 N  N   . HIS C 1 111 ? 25.669  -8.052  -31.046 1.00 13.21 ? 111 HIS C N   1 
ATOM   5167 C  CA  . HIS C 1 111 ? 26.819  -7.422  -30.384 1.00 13.49 ? 111 HIS C CA  1 
ATOM   5168 C  C   . HIS C 1 111 ? 27.584  -8.487  -29.668 1.00 16.34 ? 111 HIS C C   1 
ATOM   5169 O  O   . HIS C 1 111 ? 27.013  -9.473  -29.151 1.00 17.78 ? 111 HIS C O   1 
ATOM   5170 C  CB  . HIS C 1 111 ? 26.491  -6.375  -29.330 1.00 14.85 ? 111 HIS C CB  1 
ATOM   5171 C  CG  . HIS C 1 111 ? 26.006  -5.093  -29.907 1.00 14.20 ? 111 HIS C CG  1 
ATOM   5172 N  ND1 . HIS C 1 111 ? 26.791  -4.008  -30.037 1.00 13.73 ? 111 HIS C ND1 1 
ATOM   5173 C  CD2 . HIS C 1 111 ? 24.764  -4.749  -30.412 1.00 14.63 ? 111 HIS C CD2 1 
ATOM   5174 C  CE1 . HIS C 1 111 ? 26.079  -3.016  -30.593 1.00 13.24 ? 111 HIS C CE1 1 
ATOM   5175 N  NE2 . HIS C 1 111 ? 24.837  -3.470  -30.813 1.00 16.89 ? 111 HIS C NE2 1 
ATOM   5176 N  N   . PHE C 1 112 ? 28.884  -8.290  -29.600 1.00 14.07 ? 112 PHE C N   1 
ATOM   5177 C  CA  . PHE C 1 112 ? 29.695  -9.037  -28.637 1.00 13.85 ? 112 PHE C CA  1 
ATOM   5178 C  C   . PHE C 1 112 ? 29.756  -8.260  -27.331 1.00 13.63 ? 112 PHE C C   1 
ATOM   5179 O  O   . PHE C 1 112 ? 29.322  -7.111  -27.252 1.00 14.27 ? 112 PHE C O   1 
ATOM   5180 C  CB  . PHE C 1 112 ? 31.097  -9.306  -29.255 1.00 14.92 ? 112 PHE C CB  1 
ATOM   5181 C  CG  . PHE C 1 112 ? 31.072  -10.437 -30.215 1.00 16.33 ? 112 PHE C CG  1 
ATOM   5182 C  CD1 . PHE C 1 112 ? 31.470  -11.754 -29.825 1.00 17.78 ? 112 PHE C CD1 1 
ATOM   5183 C  CD2 . PHE C 1 112 ? 30.560  -10.288 -31.543 1.00 16.60 ? 112 PHE C CD2 1 
ATOM   5184 C  CE1 . PHE C 1 112 ? 31.429  -12.827 -30.724 1.00 21.28 ? 112 PHE C CE1 1 
ATOM   5185 C  CE2 . PHE C 1 112 ? 30.558  -11.385 -32.440 1.00 20.79 ? 112 PHE C CE2 1 
ATOM   5186 C  CZ  . PHE C 1 112 ? 30.969  -12.648 -32.031 1.00 22.33 ? 112 PHE C CZ  1 
ATOM   5187 N  N   . ALA C 1 113 ? 30.355  -8.845  -26.263 1.00 14.91 ? 113 ALA C N   1 
ATOM   5188 C  CA  . ALA C 1 113 ? 30.481  -8.118  -25.031 1.00 13.19 ? 113 ALA C CA  1 
ATOM   5189 C  C   . ALA C 1 113 ? 31.180  -6.797  -24.999 1.00 13.61 ? 113 ALA C C   1 
ATOM   5190 O  O   . ALA C 1 113 ? 30.753  -5.928  -24.353 1.00 14.90 ? 113 ALA C O   1 
ATOM   5191 C  CB  . ALA C 1 113 ? 31.067  -9.023  -23.924 1.00 17.01 ? 113 ALA C CB  1 
ATOM   5192 N  N   . ALA C 1 114 ? 32.295  -6.715  -25.747 1.00 13.92 ? 114 ALA C N   1 
ATOM   5193 C  CA  . ALA C 1 114 ? 33.194  -5.653  -25.768 1.00 13.35 ? 114 ALA C CA  1 
ATOM   5194 C  C   . ALA C 1 114 ? 34.008  -5.758  -27.071 1.00 12.09 ? 114 ALA C C   1 
ATOM   5195 O  O   . ALA C 1 114 ? 33.960  -6.759  -27.758 1.00 15.90 ? 114 ALA C O   1 
ATOM   5196 C  CB  . ALA C 1 114 ? 34.140  -5.883  -24.598 1.00 15.37 ? 114 ALA C CB  1 
ATOM   5197 N  N   . GLU C 1 115 ? 34.804  -4.737  -27.330 1.00 12.22 ? 115 GLU C N   1 
ATOM   5198 C  CA  . GLU C 1 115 ? 35.665  -4.760  -28.549 1.00 13.47 ? 115 GLU C CA  1 
ATOM   5199 C  C   . GLU C 1 115 ? 36.973  -3.966  -28.148 1.00 12.90 ? 115 GLU C C   1 
ATOM   5200 O  O   . GLU C 1 115 ? 36.931  -2.924  -27.513 1.00 13.56 ? 115 GLU C O   1 
ATOM   5201 C  CB  . GLU C 1 115 ? 34.956  -3.994  -29.652 1.00 12.85 ? 115 GLU C CB  1 
ATOM   5202 C  CG  . GLU C 1 115 ? 35.618  -4.167  -31.034 1.00 13.58 ? 115 GLU C CG  1 
ATOM   5203 C  CD  . GLU C 1 115 ? 34.695  -3.795  -32.173 1.00 13.45 ? 115 GLU C CD  1 
ATOM   5204 O  OE1 . GLU C 1 115 ? 35.171  -3.215  -33.152 1.00 12.34 ? 115 GLU C OE1 1 
ATOM   5205 O  OE2 . GLU C 1 115 ? 33.473  -4.097  -32.084 1.00 12.95 ? 115 GLU C OE2 1 
ATOM   5206 N  N   . LEU C 1 116 ? 38.112  -4.537  -28.569 1.00 14.37 ? 116 LEU C N   1 
ATOM   5207 C  CA  . LEU C 1 116 ? 39.397  -3.871  -28.379 1.00 15.60 ? 116 LEU C CA  1 
ATOM   5208 C  C   . LEU C 1 116 ? 39.829  -3.292  -29.746 1.00 13.30 ? 116 LEU C C   1 
ATOM   5209 O  O   . LEU C 1 116 ? 39.651  -4.022  -30.778 1.00 15.93 ? 116 LEU C O   1 
ATOM   5210 C  CB  . LEU C 1 116 ? 40.351  -4.965  -28.034 1.00 15.39 ? 116 LEU C CB  1 
ATOM   5211 C  CG  . LEU C 1 116 ? 41.834  -4.495  -28.013 1.00 17.31 ? 116 LEU C CG  1 
ATOM   5212 C  CD1 . LEU C 1 116 ? 42.143  -3.563  -26.803 1.00 16.72 ? 116 LEU C CD1 1 
ATOM   5213 C  CD2 . LEU C 1 116 ? 42.741  -5.690  -28.190 1.00 20.14 ? 116 LEU C CD2 1 
ATOM   5214 N  N   . HIS C 1 117 ? 40.319  -2.058  -29.748 1.00 14.85 ? 117 HIS C N   1 
ATOM   5215 C  CA  . HIS C 1 117 ? 40.836  -1.376  -30.961 1.00 12.87 ? 117 HIS C CA  1 
ATOM   5216 C  C   . HIS C 1 117 ? 42.342  -1.227  -30.765 1.00 15.61 ? 117 HIS C C   1 
ATOM   5217 O  O   . HIS C 1 117 ? 42.713  -0.771  -29.765 1.00 15.28 ? 117 HIS C O   1 
ATOM   5218 C  CB  . HIS C 1 117 ? 40.135  -0.139  -31.197 1.00 13.75 ? 117 HIS C CB  1 
ATOM   5219 C  CG  . HIS C 1 117 ? 38.750  -0.405  -31.727 1.00 12.05 ? 117 HIS C CG  1 
ATOM   5220 N  ND1 . HIS C 1 117 ? 37.761  0.492   -31.686 1.00 14.41 ? 117 HIS C ND1 1 
ATOM   5221 C  CD2 . HIS C 1 117 ? 38.207  -1.568  -32.286 1.00 12.50 ? 117 HIS C CD2 1 
ATOM   5222 C  CE1 . HIS C 1 117 ? 36.644  -0.053  -32.209 1.00 11.55 ? 117 HIS C CE1 1 
ATOM   5223 N  NE2 . HIS C 1 117 ? 36.923  -1.311  -32.579 1.00 11.33 ? 117 HIS C NE2 1 
ATOM   5224 N  N   . ILE C 1 118 ? 43.117  -1.733  -31.712 1.00 13.65 ? 118 ILE C N   1 
ATOM   5225 C  CA  . ILE C 1 118 ? 44.603  -1.446  -31.763 1.00 15.00 ? 118 ILE C CA  1 
ATOM   5226 C  C   . ILE C 1 118 ? 44.890  -0.448  -32.868 1.00 14.17 ? 118 ILE C C   1 
ATOM   5227 O  O   . ILE C 1 118 ? 44.739  -0.845  -34.061 1.00 16.39 ? 118 ILE C O   1 
ATOM   5228 C  CB  . ILE C 1 118 ? 45.453  -2.706  -31.873 1.00 15.59 ? 118 ILE C CB  1 
ATOM   5229 C  CG1 . ILE C 1 118 ? 45.067  -3.792  -30.826 1.00 17.49 ? 118 ILE C CG1 1 
ATOM   5230 C  CG2 . ILE C 1 118 ? 46.923  -2.258  -31.618 1.00 14.41 ? 118 ILE C CG2 1 
ATOM   5231 C  CD1 . ILE C 1 118 ? 45.742  -5.161  -30.889 1.00 18.85 ? 118 ILE C CD1 1 
ATOM   5232 N  N   . VAL C 1 119 ? 45.057  0.833   -32.536 1.00 14.84 ? 119 VAL C N   1 
ATOM   5233 C  CA  . VAL C 1 119 ? 45.038  1.988   -33.495 1.00 14.44 ? 119 VAL C CA  1 
ATOM   5234 C  C   . VAL C 1 119 ? 46.468  2.110   -34.079 1.00 17.39 ? 119 VAL C C   1 
ATOM   5235 O  O   . VAL C 1 119 ? 47.469  2.153   -33.310 1.00 18.28 ? 119 VAL C O   1 
ATOM   5236 C  CB  . VAL C 1 119 ? 44.576  3.339   -32.938 1.00 14.13 ? 119 VAL C CB  1 
ATOM   5237 C  CG1 . VAL C 1 119 ? 44.479  4.391   -33.985 1.00 15.85 ? 119 VAL C CG1 1 
ATOM   5238 C  CG2 . VAL C 1 119 ? 43.182  3.133   -32.293 1.00 14.42 ? 119 VAL C CG2 1 
ATOM   5239 N  N   . HIS C 1 120 ? 46.581  2.103   -35.392 1.00 16.37 ? 120 HIS C N   1 
ATOM   5240 C  CA  . HIS C 1 120 ? 47.939  2.351   -36.034 1.00 16.52 ? 120 HIS C CA  1 
ATOM   5241 C  C   . HIS C 1 120 ? 47.771  3.539   -37.001 1.00 19.42 ? 120 HIS C C   1 
ATOM   5242 O  O   . HIS C 1 120 ? 46.690  3.808   -37.507 1.00 17.09 ? 120 HIS C O   1 
ATOM   5243 C  CB  . HIS C 1 120 ? 48.378  1.140   -36.844 1.00 15.23 ? 120 HIS C CB  1 
ATOM   5244 C  CG  . HIS C 1 120 ? 48.488  -0.169  -36.086 1.00 16.72 ? 120 HIS C CG  1 
ATOM   5245 N  ND1 . HIS C 1 120 ? 47.423  -0.791  -35.573 1.00 16.43 ? 120 HIS C ND1 1 
ATOM   5246 C  CD2 . HIS C 1 120 ? 49.581  -1.002  -35.840 1.00 18.89 ? 120 HIS C CD2 1 
ATOM   5247 C  CE1 . HIS C 1 120 ? 47.798  -1.986  -35.064 1.00 17.34 ? 120 HIS C CE1 1 
ATOM   5248 N  NE2 . HIS C 1 120 ? 49.147  -2.081  -35.183 1.00 19.97 ? 120 HIS C NE2 1 
ATOM   5249 N  N   . TYR C 1 121 ? 48.850  4.275   -37.370 1.00 16.04 ? 121 TYR C N   1 
ATOM   5250 C  CA  . TYR C 1 121 ? 48.762  5.395   -38.316 1.00 18.13 ? 121 TYR C CA  1 
ATOM   5251 C  C   . TYR C 1 121 ? 49.771  5.118   -39.468 1.00 16.02 ? 121 TYR C C   1 
ATOM   5252 O  O   . TYR C 1 121 ? 50.745  4.362   -39.282 1.00 15.09 ? 121 TYR C O   1 
ATOM   5253 C  CB  . TYR C 1 121 ? 49.076  6.812   -37.713 1.00 17.41 ? 121 TYR C CB  1 
ATOM   5254 C  CG  . TYR C 1 121 ? 50.512  6.974   -37.212 1.00 19.66 ? 121 TYR C CG  1 
ATOM   5255 C  CD1 . TYR C 1 121 ? 51.466  7.673   -37.958 1.00 20.99 ? 121 TYR C CD1 1 
ATOM   5256 C  CD2 . TYR C 1 121 ? 50.865  6.412   -36.041 1.00 17.42 ? 121 TYR C CD2 1 
ATOM   5257 C  CE1 . TYR C 1 121 ? 52.802  7.785   -37.466 1.00 20.24 ? 121 TYR C CE1 1 
ATOM   5258 C  CE2 . TYR C 1 121 ? 52.151  6.509   -35.524 1.00 21.71 ? 121 TYR C CE2 1 
ATOM   5259 C  CZ  . TYR C 1 121 ? 53.104  7.184   -36.260 1.00 21.12 ? 121 TYR C CZ  1 
ATOM   5260 O  OH  . TYR C 1 121 ? 54.368  7.199   -35.683 1.00 23.05 ? 121 TYR C OH  1 
ATOM   5261 N  N   . ASN C 1 122 ? 49.516  5.733   -40.591 1.00 16.32 ? 122 ASN C N   1 
ATOM   5262 C  CA  . ASN C 1 122 ? 50.411  5.495   -41.805 1.00 14.50 ? 122 ASN C CA  1 
ATOM   5263 C  C   . ASN C 1 122 ? 51.703  6.359   -41.626 1.00 15.03 ? 122 ASN C C   1 
ATOM   5264 O  O   . ASN C 1 122 ? 51.692  7.577   -41.846 1.00 17.23 ? 122 ASN C O   1 
ATOM   5265 C  CB  . ASN C 1 122 ? 49.671  5.935   -43.001 1.00 14.71 ? 122 ASN C CB  1 
ATOM   5266 C  CG  . ASN C 1 122 ? 50.343  5.536   -44.270 1.00 16.62 ? 122 ASN C CG  1 
ATOM   5267 O  OD1 . ASN C 1 122 ? 51.582  5.583   -44.320 1.00 18.09 ? 122 ASN C OD1 1 
ATOM   5268 N  ND2 . ASN C 1 122 ? 49.589  5.103   -45.284 1.00 17.07 ? 122 ASN C ND2 1 
ATOM   5269 N  N   . SER C 1 123 ? 52.715  5.652   -41.158 1.00 17.09 ? 123 SER C N   1 
ATOM   5270 C  CA  . SER C 1 123 ? 53.948  6.350   -40.783 1.00 17.65 ? 123 SER C CA  1 
ATOM   5271 C  C   . SER C 1 123 ? 54.803  6.544   -42.043 1.00 22.01 ? 123 SER C C   1 
ATOM   5272 O  O   . SER C 1 123 ? 55.668  7.464   -42.048 1.00 22.47 ? 123 SER C O   1 
ATOM   5273 C  CB  . SER C 1 123 ? 54.695  5.595   -39.696 1.00 15.90 ? 123 SER C CB  1 
ATOM   5274 O  OG  . SER C 1 123 ? 54.871  4.260   -39.932 1.00 15.79 ? 123 SER C OG  1 
ATOM   5275 N  N   . ASP C 1 124 ? 54.528  5.763   -43.088 1.00 20.40 ? 124 ASP C N   1 
ATOM   5276 C  CA  . ASP C 1 124 ? 55.093  6.130   -44.449 1.00 18.83 ? 124 ASP C CA  1 
ATOM   5277 C  C   . ASP C 1 124 ? 54.685  7.488   -45.014 1.00 22.50 ? 124 ASP C C   1 
ATOM   5278 O  O   . ASP C 1 124 ? 55.478  8.127   -45.713 1.00 26.38 ? 124 ASP C O   1 
ATOM   5279 C  CB  . ASP C 1 124 ? 54.805  5.091   -45.476 1.00 18.10 ? 124 ASP C CB  1 
ATOM   5280 C  CG  . ASP C 1 124 ? 55.515  3.809   -45.196 1.00 18.84 ? 124 ASP C CG  1 
ATOM   5281 O  OD1 . ASP C 1 124 ? 56.574  3.846   -44.423 1.00 19.00 ? 124 ASP C OD1 1 
ATOM   5282 O  OD2 . ASP C 1 124 ? 55.062  2.759   -45.733 1.00 20.24 ? 124 ASP C OD2 1 
ATOM   5283 N  N   . LEU C 1 125 ? 53.448  7.952   -44.767 1.00 16.70 ? 125 LEU C N   1 
ATOM   5284 C  CA  . LEU C 1 125 ? 53.030  9.241   -45.254 1.00 18.45 ? 125 LEU C CA  1 
ATOM   5285 C  C   . LEU C 1 125 ? 53.060  10.395  -44.267 1.00 16.98 ? 125 LEU C C   1 
ATOM   5286 O  O   . LEU C 1 125 ? 53.010  11.607  -44.660 1.00 21.71 ? 125 LEU C O   1 
ATOM   5287 C  CB  . LEU C 1 125 ? 51.600  9.133   -45.788 1.00 17.75 ? 125 LEU C CB  1 
ATOM   5288 C  CG  . LEU C 1 125 ? 51.338  8.040   -46.845 1.00 21.15 ? 125 LEU C CG  1 
ATOM   5289 C  CD1 . LEU C 1 125 ? 49.856  8.060   -47.160 1.00 18.87 ? 125 LEU C CD1 1 
ATOM   5290 C  CD2 . LEU C 1 125 ? 52.146  8.267   -48.109 1.00 23.37 ? 125 LEU C CD2 1 
ATOM   5291 N  N   . TYR C 1 126 ? 52.946  10.066  -42.995 1.00 18.62 ? 126 TYR C N   1 
ATOM   5292 C  CA  . TYR C 1 126 ? 52.610  11.124  -42.006 1.00 17.02 ? 126 TYR C CA  1 
ATOM   5293 C  C   . TYR C 1 126 ? 53.489  10.963  -40.783 1.00 18.51 ? 126 TYR C C   1 
ATOM   5294 O  O   . TYR C 1 126 ? 53.869  9.884   -40.443 1.00 17.62 ? 126 TYR C O   1 
ATOM   5295 C  CB  . TYR C 1 126 ? 51.115  10.970  -41.494 1.00 17.27 ? 126 TYR C CB  1 
ATOM   5296 C  CG  . TYR C 1 126 ? 50.158  11.028  -42.622 1.00 18.38 ? 126 TYR C CG  1 
ATOM   5297 C  CD1 . TYR C 1 126 ? 50.136  12.149  -43.483 1.00 21.94 ? 126 TYR C CD1 1 
ATOM   5298 C  CD2 . TYR C 1 126 ? 49.370  9.911   -42.926 1.00 20.51 ? 126 TYR C CD2 1 
ATOM   5299 C  CE1 . TYR C 1 126 ? 49.326  12.204  -44.586 1.00 18.82 ? 126 TYR C CE1 1 
ATOM   5300 C  CE2 . TYR C 1 126 ? 48.567  9.922   -44.038 1.00 20.36 ? 126 TYR C CE2 1 
ATOM   5301 C  CZ  . TYR C 1 126 ? 48.496  11.059  -44.846 1.00 19.35 ? 126 TYR C CZ  1 
ATOM   5302 O  OH  . TYR C 1 126 ? 47.712  11.101  -45.983 1.00 19.46 ? 126 TYR C OH  1 
ATOM   5303 N  N   . PRO C 1 127 ? 53.812  12.083  -40.078 1.00 20.94 ? 127 PRO C N   1 
ATOM   5304 C  CA  . PRO C 1 127 ? 54.791  11.962  -38.963 1.00 24.40 ? 127 PRO C CA  1 
ATOM   5305 C  C   . PRO C 1 127 ? 54.245  11.425  -37.631 1.00 25.93 ? 127 PRO C C   1 
ATOM   5306 O  O   . PRO C 1 127 ? 54.998  10.893  -36.811 1.00 26.73 ? 127 PRO C O   1 
ATOM   5307 C  CB  . PRO C 1 127 ? 55.285  13.392  -38.798 1.00 25.07 ? 127 PRO C CB  1 
ATOM   5308 C  CG  . PRO C 1 127 ? 54.181  14.245  -39.311 1.00 24.22 ? 127 PRO C CG  1 
ATOM   5309 C  CD  . PRO C 1 127 ? 53.505  13.472  -40.417 1.00 23.81 ? 127 PRO C CD  1 
ATOM   5310 N  N   . ASP C 1 128 ? 52.923  11.499  -37.463 1.00 22.49 ? 128 ASP C N   1 
ATOM   5311 C  CA  . ASP C 1 128 ? 52.318  11.007  -36.221 1.00 24.30 ? 128 ASP C CA  1 
ATOM   5312 C  C   . ASP C 1 128 ? 50.829  10.764  -36.442 1.00 21.37 ? 128 ASP C C   1 
ATOM   5313 O  O   . ASP C 1 128 ? 50.278  11.168  -37.469 1.00 20.97 ? 128 ASP C O   1 
ATOM   5314 C  CB  . ASP C 1 128 ? 52.509  12.011  -35.050 1.00 26.00 ? 128 ASP C CB  1 
ATOM   5315 C  CG  . ASP C 1 128 ? 52.281  13.453  -35.449 1.00 34.84 ? 128 ASP C CG  1 
ATOM   5316 O  OD1 . ASP C 1 128 ? 53.257  14.244  -35.412 1.00 40.31 ? 128 ASP C OD1 1 
ATOM   5317 O  OD2 . ASP C 1 128 ? 51.154  13.848  -35.832 1.00 28.79 ? 128 ASP C OD2 1 
ATOM   5318 N  N   . ALA C 1 129 ? 50.205  10.143  -35.441 1.00 27.72 ? 129 ALA C N   1 
ATOM   5319 C  CA  . ALA C 1 129 ? 48.766  9.768   -35.526 1.00 26.51 ? 129 ALA C CA  1 
ATOM   5320 C  C   . ALA C 1 129 ? 47.809  10.962  -35.583 1.00 26.75 ? 129 ALA C C   1 
ATOM   5321 O  O   . ALA C 1 129 ? 46.845  10.966  -36.357 1.00 24.68 ? 129 ALA C O   1 
ATOM   5322 C  CB  . ALA C 1 129 ? 48.383  8.793   -34.418 1.00 31.06 ? 129 ALA C CB  1 
ATOM   5323 N  N   . SER C 1 130 ? 48.094  11.979  -34.794 1.00 26.18 ? 130 SER C N   1 
ATOM   5324 C  CA  . SER C 1 130 ? 47.457  13.274  -34.948 1.00 27.47 ? 130 SER C CA  1 
ATOM   5325 C  C   . SER C 1 130 ? 47.408  13.832  -36.342 1.00 26.65 ? 130 SER C C   1 
ATOM   5326 O  O   . SER C 1 130 ? 46.373  14.282  -36.731 1.00 24.36 ? 130 SER C O   1 
ATOM   5327 C  CB  . SER C 1 130 ? 48.142  14.352  -34.099 1.00 28.28 ? 130 SER C CB  1 
ATOM   5328 O  OG  . SER C 1 130 ? 47.372  14.538  -32.953 1.00 34.38 ? 130 SER C OG  1 
ATOM   5329 N  N   . THR C 1 131 ? 48.558  13.895  -37.065 1.00 20.71 ? 131 THR C N   1 
ATOM   5330 C  CA  . THR C 1 131 ? 48.561  14.489  -38.382 1.00 22.69 ? 131 THR C CA  1 
ATOM   5331 C  C   . THR C 1 131 ? 47.840  13.487  -39.328 1.00 19.60 ? 131 THR C C   1 
ATOM   5332 O  O   . THR C 1 131 ? 47.145  13.927  -40.269 1.00 21.30 ? 131 THR C O   1 
ATOM   5333 C  CB  . THR C 1 131 ? 50.021  14.759  -38.850 1.00 23.20 ? 131 THR C CB  1 
ATOM   5334 O  OG1 . THR C 1 131 ? 50.613  15.738  -37.967 1.00 20.61 ? 131 THR C OG1 1 
ATOM   5335 C  CG2 . THR C 1 131 ? 50.059  15.330  -40.280 1.00 23.66 ? 131 THR C CG2 1 
ATOM   5336 N  N   . ALA C 1 132 ? 48.042  12.204  -39.044 1.00 17.15 ? 132 ALA C N   1 
ATOM   5337 C  CA  . ALA C 1 132 ? 47.498  11.130  -39.951 1.00 16.88 ? 132 ALA C CA  1 
ATOM   5338 C  C   . ALA C 1 132 ? 45.971  11.045  -39.904 1.00 18.09 ? 132 ALA C C   1 
ATOM   5339 O  O   . ALA C 1 132 ? 45.351  10.779  -40.910 1.00 16.76 ? 132 ALA C O   1 
ATOM   5340 C  CB  . ALA C 1 132 ? 48.111  9.798   -39.681 1.00 16.42 ? 132 ALA C CB  1 
ATOM   5341 N  N   . SER C 1 133 ? 45.395  11.395  -38.754 1.00 18.83 ? 133 SER C N   1 
ATOM   5342 C  CA  . SER C 1 133 ? 44.033  10.887  -38.482 1.00 18.44 ? 133 SER C CA  1 
ATOM   5343 C  C   . SER C 1 133 ? 42.970  11.537  -39.366 1.00 18.34 ? 133 SER C C   1 
ATOM   5344 O  O   . SER C 1 133 ? 41.866  10.945  -39.597 1.00 17.61 ? 133 SER C O   1 
ATOM   5345 C  CB  . SER C 1 133 ? 43.660  10.928  -36.961 1.00 17.77 ? 133 SER C CB  1 
ATOM   5346 O  OG  . SER C 1 133 ? 43.631  12.270  -36.594 1.00 20.89 ? 133 SER C OG  1 
ATOM   5347 N  N   . ASN C 1 134 ? 43.201  12.747  -39.880 1.00 16.79 ? 134 ASN C N   1 
ATOM   5348 C  CA  . ASN C 1 134 ? 42.224  13.373  -40.770 1.00 20.48 ? 134 ASN C CA  1 
ATOM   5349 C  C   . ASN C 1 134 ? 42.707  13.388  -42.221 1.00 17.43 ? 134 ASN C C   1 
ATOM   5350 O  O   . ASN C 1 134 ? 42.218  14.131  -43.066 1.00 20.78 ? 134 ASN C O   1 
ATOM   5351 C  CB  . ASN C 1 134 ? 41.842  14.760  -40.276 1.00 21.01 ? 134 ASN C CB  1 
ATOM   5352 C  CG  . ASN C 1 134 ? 43.007  15.749  -40.419 1.00 25.03 ? 134 ASN C CG  1 
ATOM   5353 O  OD1 . ASN C 1 134 ? 44.172  15.328  -40.527 1.00 25.65 ? 134 ASN C OD1 1 
ATOM   5354 N  ND2 . ASN C 1 134 ? 42.695  17.059  -40.441 1.00 25.56 ? 134 ASN C ND2 1 
ATOM   5355 N  N   . LYS C 1 135 ? 43.616  12.465  -42.548 1.00 18.41 ? 135 LYS C N   1 
ATOM   5356 C  CA  . LYS C 1 135 ? 44.234  12.508  -43.877 1.00 18.93 ? 135 LYS C CA  1 
ATOM   5357 C  C   . LYS C 1 135 ? 44.096  11.179  -44.572 1.00 18.80 ? 135 LYS C C   1 
ATOM   5358 O  O   . LYS C 1 135 ? 43.895  10.113  -43.939 1.00 19.54 ? 135 LYS C O   1 
ATOM   5359 C  CB  . LYS C 1 135 ? 45.744  12.894  -43.732 1.00 20.34 ? 135 LYS C CB  1 
ATOM   5360 C  CG  . LYS C 1 135 ? 45.883  14.367  -43.301 1.00 22.86 ? 135 LYS C CG  1 
ATOM   5361 C  CD  . LYS C 1 135 ? 47.338  14.870  -43.304 1.00 24.18 ? 135 LYS C CD  1 
ATOM   5362 C  CE  . LYS C 1 135 ? 47.384  16.300  -42.750 1.00 24.90 ? 135 LYS C CE  1 
ATOM   5363 N  NZ  . LYS C 1 135 ? 46.875  16.442  -41.336 1.00 23.22 ? 135 LYS C NZ  1 
ATOM   5364 N  N   . SER C 1 136 ? 44.239  11.264  -45.892 1.00 18.75 ? 136 SER C N   1 
ATOM   5365 C  CA  . SER C 1 136 ? 44.066  10.136  -46.763 1.00 20.27 ? 136 SER C CA  1 
ATOM   5366 C  C   . SER C 1 136 ? 44.873  8.954   -46.324 1.00 17.36 ? 136 SER C C   1 
ATOM   5367 O  O   . SER C 1 136 ? 46.089  9.088   -46.051 1.00 19.68 ? 136 SER C O   1 
ATOM   5368 C  CB  . SER C 1 136 ? 44.529  10.537  -48.163 1.00 21.79 ? 136 SER C CB  1 
ATOM   5369 O  OG  . SER C 1 136 ? 44.298  9.437   -49.005 1.00 25.11 ? 136 SER C OG  1 
ATOM   5370 N  N   . GLU C 1 137 ? 44.243  7.782   -46.196 1.00 15.40 ? 137 GLU C N   1 
ATOM   5371 C  CA  . GLU C 1 137 ? 44.957  6.532   -45.837 1.00 17.25 ? 137 GLU C CA  1 
ATOM   5372 C  C   . GLU C 1 137 ? 45.729  6.646   -44.528 1.00 16.71 ? 137 GLU C C   1 
ATOM   5373 O  O   . GLU C 1 137 ? 46.724  5.961   -44.307 1.00 15.43 ? 137 GLU C O   1 
ATOM   5374 C  CB  . GLU C 1 137 ? 45.898  6.075   -46.951 1.00 18.66 ? 137 GLU C CB  1 
ATOM   5375 C  CG  . GLU C 1 137 ? 45.124  5.818   -48.219 1.00 22.53 ? 137 GLU C CG  1 
ATOM   5376 C  CD  . GLU C 1 137 ? 45.981  5.329   -49.392 1.00 30.46 ? 137 GLU C CD  1 
ATOM   5377 O  OE1 . GLU C 1 137 ? 45.339  4.701   -50.259 1.00 32.77 ? 137 GLU C OE1 1 
ATOM   5378 O  OE2 . GLU C 1 137 ? 47.228  5.564   -49.474 1.00 36.81 ? 137 GLU C OE2 1 
ATOM   5379 N  N   . GLY C 1 138 ? 45.176  7.438   -43.597 1.00 15.06 ? 138 GLY C N   1 
ATOM   5380 C  CA  . GLY C 1 138 ? 45.867  7.820   -42.378 1.00 15.01 ? 138 GLY C CA  1 
ATOM   5381 C  C   . GLY C 1 138 ? 45.983  6.718   -41.370 1.00 16.54 ? 138 GLY C C   1 
ATOM   5382 O  O   . GLY C 1 138 ? 46.955  6.659   -40.589 1.00 14.87 ? 138 GLY C O   1 
ATOM   5383 N  N   . LEU C 1 139 ? 44.922  5.862   -41.259 1.00 12.38 ? 139 LEU C N   1 
ATOM   5384 C  CA  . LEU C 1 139 ? 44.798  4.989   -40.123 1.00 13.30 ? 139 LEU C CA  1 
ATOM   5385 C  C   . LEU C 1 139 ? 44.475  3.562   -40.493 1.00 11.76 ? 139 LEU C C   1 
ATOM   5386 O  O   . LEU C 1 139 ? 43.890  3.279   -41.533 1.00 14.43 ? 139 LEU C O   1 
ATOM   5387 C  CB  . LEU C 1 139 ? 43.690  5.500   -39.169 1.00 12.73 ? 139 LEU C CB  1 
ATOM   5388 C  CG  . LEU C 1 139 ? 43.886  6.860   -38.524 1.00 13.24 ? 139 LEU C CG  1 
ATOM   5389 C  CD1 . LEU C 1 139 ? 42.582  7.452   -37.878 1.00 14.58 ? 139 LEU C CD1 1 
ATOM   5390 C  CD2 . LEU C 1 139 ? 45.063  6.790   -37.539 1.00 14.96 ? 139 LEU C CD2 1 
ATOM   5391 N  N   . ALA C 1 140 ? 44.924  2.634   -39.687 1.00 11.48 ? 140 ALA C N   1 
ATOM   5392 C  CA  . ALA C 1 140 ? 44.487  1.263   -39.775 1.00 11.54 ? 140 ALA C CA  1 
ATOM   5393 C  C   . ALA C 1 140 ? 44.254  0.747   -38.384 1.00 12.75 ? 140 ALA C C   1 
ATOM   5394 O  O   . ALA C 1 140 ? 45.073  0.878   -37.506 1.00 13.82 ? 140 ALA C O   1 
ATOM   5395 C  CB  . ALA C 1 140 ? 45.485  0.448   -40.536 1.00 11.79 ? 140 ALA C CB  1 
ATOM   5396 N  N   . VAL C 1 141 ? 43.046  0.185   -38.150 1.00 12.13 ? 141 VAL C N   1 
ATOM   5397 C  CA  . VAL C 1 141 ? 42.711  -0.284  -36.817 1.00 12.61 ? 141 VAL C CA  1 
ATOM   5398 C  C   . VAL C 1 141 ? 42.425  -1.789  -36.841 1.00 12.50 ? 141 VAL C C   1 
ATOM   5399 O  O   . VAL C 1 141 ? 41.763  -2.294  -37.754 1.00 12.53 ? 141 VAL C O   1 
ATOM   5400 C  CB  . VAL C 1 141 ? 41.509  0.529   -36.267 1.00 11.64 ? 141 VAL C CB  1 
ATOM   5401 C  CG1 . VAL C 1 141 ? 41.155  -0.025  -34.859 1.00 13.34 ? 141 VAL C CG1 1 
ATOM   5402 C  CG2 . VAL C 1 141 ? 41.763  2.032   -36.246 1.00 14.61 ? 141 VAL C CG2 1 
ATOM   5403 N  N   . LEU C 1 142 ? 42.908  -2.522  -35.826 1.00 12.14 ? 142 LEU C N   1 
ATOM   5404 C  CA  . LEU C 1 142 ? 42.646  -3.957  -35.681 1.00 12.60 ? 142 LEU C CA  1 
ATOM   5405 C  C   . LEU C 1 142 ? 41.550  -4.022  -34.647 1.00 13.65 ? 142 LEU C C   1 
ATOM   5406 O  O   . LEU C 1 142 ? 41.721  -3.446  -33.553 1.00 15.53 ? 142 LEU C O   1 
ATOM   5407 C  CB  . LEU C 1 142 ? 43.871  -4.746  -35.141 1.00 14.72 ? 142 LEU C CB  1 
ATOM   5408 C  CG  . LEU C 1 142 ? 45.134  -4.469  -35.992 1.00 15.84 ? 142 LEU C CG  1 
ATOM   5409 C  CD1 . LEU C 1 142 ? 46.211  -5.318  -35.341 1.00 18.79 ? 142 LEU C CD1 1 
ATOM   5410 C  CD2 . LEU C 1 142 ? 44.889  -4.983  -37.376 1.00 14.11 ? 142 LEU C CD2 1 
ATOM   5411 N  N   . ALA C 1 143 ? 40.488  -4.738  -34.962 1.00 11.65 ? 143 ALA C N   1 
ATOM   5412 C  CA  . ALA C 1 143 ? 39.398  -4.927  -33.999 1.00 12.67 ? 143 ALA C CA  1 
ATOM   5413 C  C   . ALA C 1 143 ? 39.289  -6.359  -33.587 1.00 11.96 ? 143 ALA C C   1 
ATOM   5414 O  O   . ALA C 1 143 ? 39.325  -7.277  -34.399 1.00 14.31 ? 143 ALA C O   1 
ATOM   5415 C  CB  . ALA C 1 143 ? 38.071  -4.420  -34.570 1.00 12.91 ? 143 ALA C CB  1 
ATOM   5416 N  N   . VAL C 1 144 ? 39.256  -6.562  -32.251 1.00 14.23 ? 144 VAL C N   1 
ATOM   5417 C  CA  . VAL C 1 144 ? 39.045  -7.914  -31.677 1.00 13.01 ? 144 VAL C CA  1 
ATOM   5418 C  C   . VAL C 1 144 ? 37.705  -7.899  -30.903 1.00 12.66 ? 144 VAL C C   1 
ATOM   5419 O  O   . VAL C 1 144 ? 37.494  -6.999  -30.074 1.00 14.17 ? 144 VAL C O   1 
ATOM   5420 C  CB  . VAL C 1 144 ? 40.187  -8.254  -30.670 1.00 13.15 ? 144 VAL C CB  1 
ATOM   5421 C  CG1 . VAL C 1 144 ? 39.965  -9.702  -30.156 1.00 13.14 ? 144 VAL C CG1 1 
ATOM   5422 C  CG2 . VAL C 1 144 ? 41.500  -8.187  -31.459 1.00 14.14 ? 144 VAL C CG2 1 
ATOM   5423 N  N   . LEU C 1 145 ? 36.839  -8.857  -31.280 1.00 14.98 ? 145 LEU C N   1 
ATOM   5424 C  CA  . LEU C 1 145 ? 35.550  -9.016  -30.594 1.00 16.83 ? 145 LEU C CA  1 
ATOM   5425 C  C   . LEU C 1 145 ? 35.800  -9.873  -29.360 1.00 19.72 ? 145 LEU C C   1 
ATOM   5426 O  O   . LEU C 1 145 ? 36.412  -10.992 -29.433 1.00 18.38 ? 145 LEU C O   1 
ATOM   5427 C  CB  . LEU C 1 145 ? 34.576  -9.742  -31.504 1.00 15.77 ? 145 LEU C CB  1 
ATOM   5428 C  CG  . LEU C 1 145 ? 34.460  -9.023  -32.868 1.00 17.96 ? 145 LEU C CG  1 
ATOM   5429 C  CD1 . LEU C 1 145 ? 33.787  -9.923  -33.890 1.00 17.47 ? 145 LEU C CD1 1 
ATOM   5430 C  CD2 . LEU C 1 145 ? 33.724  -7.723  -32.661 1.00 17.62 ? 145 LEU C CD2 1 
ATOM   5431 N  N   . ILE C 1 146 ? 35.169  -9.405  -28.272 1.00 17.48 ? 146 ILE C N   1 
ATOM   5432 C  CA  . ILE C 1 146 ? 35.362  -10.007 -26.941 1.00 19.09 ? 146 ILE C CA  1 
ATOM   5433 C  C   . ILE C 1 146 ? 34.065  -10.608 -26.467 1.00 20.94 ? 146 ILE C C   1 
ATOM   5434 O  O   . ILE C 1 146 ? 33.062  -9.853  -26.419 1.00 19.02 ? 146 ILE C O   1 
ATOM   5435 C  CB  . ILE C 1 146 ? 35.781  -8.921  -25.933 1.00 18.37 ? 146 ILE C CB  1 
ATOM   5436 C  CG1 . ILE C 1 146 ? 37.209  -8.260  -26.237 1.00 18.62 ? 146 ILE C CG1 1 
ATOM   5437 C  CG2 . ILE C 1 146 ? 35.938  -9.630  -24.575 1.00 19.94 ? 146 ILE C CG2 1 
ATOM   5438 C  CD1 . ILE C 1 146 ? 37.558  -6.918  -25.602 1.00 18.03 ? 146 ILE C CD1 1 
ATOM   5439 N  N   . GLU C 1 147 ? 34.070  -11.877 -26.047 1.00 22.67 ? 147 GLU C N   1 
ATOM   5440 C  CA  . GLU C 1 147 ? 32.866  -12.547 -25.449 1.00 22.66 ? 147 GLU C CA  1 
ATOM   5441 C  C   . GLU C 1 147 ? 33.189  -13.240 -24.099 1.00 28.06 ? 147 GLU C C   1 
ATOM   5442 O  O   . GLU C 1 147 ? 34.295  -13.687 -23.927 1.00 26.23 ? 147 GLU C O   1 
ATOM   5443 C  CB  . GLU C 1 147 ? 32.312  -13.584 -26.394 1.00 25.51 ? 147 GLU C CB  1 
ATOM   5444 C  CG  . GLU C 1 147 ? 33.223  -14.830 -26.537 1.00 26.02 ? 147 GLU C CG  1 
ATOM   5445 C  CD  . GLU C 1 147 ? 32.774  -15.827 -27.623 1.00 33.70 ? 147 GLU C CD  1 
ATOM   5446 O  OE1 . GLU C 1 147 ? 31.779  -15.539 -28.347 1.00 29.97 ? 147 GLU C OE1 1 
ATOM   5447 O  OE2 . GLU C 1 147 ? 33.398  -16.917 -27.789 1.00 35.06 ? 147 GLU C OE2 1 
ATOM   5448 N  N   . MET C 1 148 ? 32.234  -13.316 -23.168 1.00 27.38 ? 148 MET C N   1 
ATOM   5449 C  CA  . MET C 1 148 ? 32.423  -14.155 -21.939 1.00 28.91 ? 148 MET C CA  1 
ATOM   5450 C  C   . MET C 1 148 ? 32.820  -15.619 -22.183 1.00 29.95 ? 148 MET C C   1 
ATOM   5451 O  O   . MET C 1 148 ? 32.360  -16.288 -23.109 1.00 34.20 ? 148 MET C O   1 
ATOM   5452 C  CB  . MET C 1 148 ? 31.185  -14.112 -21.021 1.00 33.61 ? 148 MET C CB  1 
ATOM   5453 C  CG  . MET C 1 148 ? 30.988  -12.847 -20.181 1.00 37.75 ? 148 MET C CG  1 
ATOM   5454 S  SD  . MET C 1 148 ? 29.742  -12.993 -18.802 1.00 55.73 ? 148 MET C SD  1 
ATOM   5455 C  CE  . MET C 1 148 ? 28.837  -14.510 -19.191 1.00 45.33 ? 148 MET C CE  1 
ATOM   5456 N  N   . GLY C 1 149 ? 33.744  -16.095 -21.337 1.00 32.16 ? 149 GLY C N   1 
ATOM   5457 C  CA  . GLY C 1 149 ? 34.164  -17.484 -21.262 1.00 31.23 ? 149 GLY C CA  1 
ATOM   5458 C  C   . GLY C 1 149 ? 35.251  -17.480 -20.190 1.00 33.33 ? 149 GLY C C   1 
ATOM   5459 O  O   . GLY C 1 149 ? 35.101  -16.810 -19.111 1.00 29.66 ? 149 GLY C O   1 
ATOM   5460 N  N   . SER C 1 150 ? 36.381  -18.118 -20.534 1.00 38.80 ? 150 SER C N   1 
ATOM   5461 C  CA  . SER C 1 150 ? 37.588  -18.281 -19.641 1.00 35.99 ? 150 SER C CA  1 
ATOM   5462 C  C   . SER C 1 150 ? 38.282  -16.997 -19.228 1.00 39.42 ? 150 SER C C   1 
ATOM   5463 O  O   . SER C 1 150 ? 38.318  -16.025 -20.026 1.00 32.95 ? 150 SER C O   1 
ATOM   5464 C  CB  . SER C 1 150 ? 38.663  -19.102 -20.348 1.00 43.81 ? 150 SER C CB  1 
ATOM   5465 O  OG  . SER C 1 150 ? 38.265  -20.445 -20.524 1.00 41.87 ? 150 SER C OG  1 
ATOM   5466 N  N   . PHE C 1 151 ? 38.910  -17.020 -18.036 1.00 33.34 ? 151 PHE C N   1 
ATOM   5467 C  CA  . PHE C 1 151 ? 39.740  -15.901 -17.550 1.00 33.03 ? 151 PHE C CA  1 
ATOM   5468 C  C   . PHE C 1 151 ? 40.806  -15.634 -18.612 1.00 30.09 ? 151 PHE C C   1 
ATOM   5469 O  O   . PHE C 1 151 ? 41.265  -16.555 -19.231 1.00 30.70 ? 151 PHE C O   1 
ATOM   5470 C  CB  . PHE C 1 151 ? 40.422  -16.218 -16.164 1.00 29.63 ? 151 PHE C CB  1 
ATOM   5471 C  CG  . PHE C 1 151 ? 41.328  -15.116 -15.642 1.00 26.19 ? 151 PHE C CG  1 
ATOM   5472 C  CD1 . PHE C 1 151 ? 40.809  -13.952 -15.129 1.00 28.95 ? 151 PHE C CD1 1 
ATOM   5473 C  CD2 . PHE C 1 151 ? 42.713  -15.276 -15.643 1.00 26.10 ? 151 PHE C CD2 1 
ATOM   5474 C  CE1 . PHE C 1 151 ? 41.650  -12.917 -14.676 1.00 30.95 ? 151 PHE C CE1 1 
ATOM   5475 C  CE2 . PHE C 1 151 ? 43.552  -14.265 -15.207 1.00 26.33 ? 151 PHE C CE2 1 
ATOM   5476 C  CZ  . PHE C 1 151 ? 43.040  -13.082 -14.708 1.00 27.98 ? 151 PHE C CZ  1 
ATOM   5477 N  N   . ASN C 1 152 ? 41.152  -14.361 -18.803 1.00 34.68 ? 152 ASN C N   1 
ATOM   5478 C  CA  . ASN C 1 152 ? 42.240  -13.968 -19.717 1.00 31.17 ? 152 ASN C CA  1 
ATOM   5479 C  C   . ASN C 1 152 ? 43.381  -13.209 -19.051 1.00 24.79 ? 152 ASN C C   1 
ATOM   5480 O  O   . ASN C 1 152 ? 43.237  -12.014 -18.644 1.00 29.80 ? 152 ASN C O   1 
ATOM   5481 C  CB  . ASN C 1 152 ? 41.630  -13.164 -20.880 1.00 31.90 ? 152 ASN C CB  1 
ATOM   5482 C  CG  . ASN C 1 152 ? 42.597  -12.974 -22.027 1.00 32.43 ? 152 ASN C CG  1 
ATOM   5483 O  OD1 . ASN C 1 152 ? 43.757  -12.619 -21.827 1.00 31.47 ? 152 ASN C OD1 1 
ATOM   5484 N  ND2 . ASN C 1 152 ? 42.105  -13.170 -23.243 1.00 34.83 ? 152 ASN C ND2 1 
ATOM   5485 N  N   . PRO C 1 153 ? 44.535  -13.893 -18.860 1.00 32.93 ? 153 PRO C N   1 
ATOM   5486 C  CA  . PRO C 1 153 ? 45.793  -13.361 -18.330 1.00 30.98 ? 153 PRO C CA  1 
ATOM   5487 C  C   . PRO C 1 153 ? 46.284  -12.080 -18.984 1.00 29.38 ? 153 PRO C C   1 
ATOM   5488 O  O   . PRO C 1 153 ? 46.675  -11.085 -18.295 1.00 31.34 ? 153 PRO C O   1 
ATOM   5489 C  CB  . PRO C 1 153 ? 46.774  -14.488 -18.652 1.00 35.75 ? 153 PRO C CB  1 
ATOM   5490 C  CG  . PRO C 1 153 ? 45.970  -15.716 -18.503 1.00 32.63 ? 153 PRO C CG  1 
ATOM   5491 C  CD  . PRO C 1 153 ? 44.632  -15.347 -19.135 1.00 22.23 ? 153 PRO C CD  1 
ATOM   5492 N  N   . SER C 1 154 ? 46.196  -12.052 -20.324 1.00 30.76 ? 154 SER C N   1 
ATOM   5493 C  CA  . SER C 1 154 ? 46.729  -10.908 -21.046 1.00 25.94 ? 154 SER C CA  1 
ATOM   5494 C  C   . SER C 1 154 ? 45.904  -9.702  -20.914 1.00 24.26 ? 154 SER C C   1 
ATOM   5495 O  O   . SER C 1 154 ? 46.448  -8.581  -20.679 1.00 23.73 ? 154 SER C O   1 
ATOM   5496 C  CB  . SER C 1 154 ? 47.050  -11.294 -22.465 1.00 30.95 ? 154 SER C CB  1 
ATOM   5497 O  OG  . SER C 1 154 ? 47.437  -12.652 -22.484 1.00 32.42 ? 154 SER C OG  1 
ATOM   5498 N  N   . TYR C 1 155 ? 44.551  -9.884  -20.993 1.00 27.73 ? 155 TYR C N   1 
ATOM   5499 C  CA  . TYR C 1 155 ? 43.655  -8.750  -20.775 1.00 26.61 ? 155 TYR C CA  1 
ATOM   5500 C  C   . TYR C 1 155 ? 43.790  -8.189  -19.360 1.00 21.91 ? 155 TYR C C   1 
ATOM   5501 O  O   . TYR C 1 155 ? 43.667  -6.913  -19.113 1.00 24.42 ? 155 TYR C O   1 
ATOM   5502 C  CB  . TYR C 1 155 ? 42.168  -9.101  -21.174 1.00 24.29 ? 155 TYR C CB  1 
ATOM   5503 C  CG  . TYR C 1 155 ? 41.964  -8.936  -22.674 1.00 23.67 ? 155 TYR C CG  1 
ATOM   5504 C  CD1 . TYR C 1 155 ? 41.466  -7.715  -23.204 1.00 24.84 ? 155 TYR C CD1 1 
ATOM   5505 C  CD2 . TYR C 1 155 ? 42.330  -9.973  -23.539 1.00 22.92 ? 155 TYR C CD2 1 
ATOM   5506 C  CE1 . TYR C 1 155 ? 41.312  -7.564  -24.596 1.00 26.41 ? 155 TYR C CE1 1 
ATOM   5507 C  CE2 . TYR C 1 155 ? 42.208  -9.817  -24.949 1.00 23.95 ? 155 TYR C CE2 1 
ATOM   5508 C  CZ  . TYR C 1 155 ? 41.686  -8.616  -25.419 1.00 22.48 ? 155 TYR C CZ  1 
ATOM   5509 O  OH  . TYR C 1 155 ? 41.584  -8.458  -26.816 1.00 22.00 ? 155 TYR C OH  1 
ATOM   5510 N  N   . ASP C 1 156 ? 44.094  -9.075  -18.429 1.00 30.48 ? 156 ASP C N   1 
ATOM   5511 C  CA  . ASP C 1 156 ? 44.333  -8.612  -17.049 1.00 34.89 ? 156 ASP C CA  1 
ATOM   5512 C  C   . ASP C 1 156 ? 45.540  -7.650  -16.779 1.00 30.15 ? 156 ASP C C   1 
ATOM   5513 O  O   . ASP C 1 156 ? 45.540  -6.926  -15.783 1.00 28.33 ? 156 ASP C O   1 
ATOM   5514 C  CB  . ASP C 1 156 ? 44.196  -9.750  -16.009 1.00 38.47 ? 156 ASP C CB  1 
ATOM   5515 C  CG  . ASP C 1 156 ? 43.144  -9.420  -14.922 1.00 42.94 ? 156 ASP C CG  1 
ATOM   5516 O  OD1 . ASP C 1 156 ? 41.931  -9.327  -15.270 1.00 38.57 ? 156 ASP C OD1 1 
ATOM   5517 O  OD2 . ASP C 1 156 ? 43.525  -9.230  -13.737 1.00 39.32 ? 156 ASP C OD2 1 
ATOM   5518 N  N   . LYS C 1 157 ? 46.469  -7.516  -17.738 1.00 28.42 ? 157 LYS C N   1 
ATOM   5519 C  CA  . LYS C 1 157 ? 47.615  -6.647  -17.568 1.00 25.02 ? 157 LYS C CA  1 
ATOM   5520 C  C   . LYS C 1 157 ? 47.119  -5.249  -17.802 1.00 30.71 ? 157 LYS C C   1 
ATOM   5521 O  O   . LYS C 1 157 ? 47.728  -4.296  -17.308 1.00 34.66 ? 157 LYS C O   1 
ATOM   5522 C  CB  . LYS C 1 157 ? 48.660  -7.072  -18.565 1.00 27.88 ? 157 LYS C CB  1 
ATOM   5523 C  CG  . LYS C 1 157 ? 48.677  -8.600  -18.678 1.00 28.71 ? 157 LYS C CG  1 
ATOM   5524 C  CD  . LYS C 1 157 ? 49.961  -9.050  -19.344 1.00 31.17 ? 157 LYS C CD  1 
ATOM   5525 C  CE  . LYS C 1 157 ? 50.110  -10.558 -19.228 1.00 29.81 ? 157 LYS C CE  1 
ATOM   5526 N  NZ  . LYS C 1 157 ? 51.162  -11.066 -20.179 1.00 30.93 ? 157 LYS C NZ  1 
ATOM   5527 N  N   . ILE C 1 158 ? 45.984  -5.107  -18.505 1.00 23.10 ? 158 ILE C N   1 
ATOM   5528 C  CA  . ILE C 1 158 ? 45.462  -3.770  -18.594 1.00 24.65 ? 158 ILE C CA  1 
ATOM   5529 C  C   . ILE C 1 158 ? 44.568  -3.581  -17.376 1.00 25.20 ? 158 ILE C C   1 
ATOM   5530 O  O   . ILE C 1 158 ? 44.536  -2.472  -16.735 1.00 27.78 ? 158 ILE C O   1 
ATOM   5531 C  CB  . ILE C 1 158 ? 44.642  -3.590  -19.908 1.00 23.48 ? 158 ILE C CB  1 
ATOM   5532 C  CG1 . ILE C 1 158 ? 45.588  -3.790  -21.084 1.00 30.25 ? 158 ILE C CG1 1 
ATOM   5533 C  CG2 . ILE C 1 158 ? 43.997  -2.203  -19.954 1.00 30.03 ? 158 ILE C CG2 1 
ATOM   5534 C  CD1 . ILE C 1 158 ? 44.904  -3.855  -22.434 1.00 30.70 ? 158 ILE C CD1 1 
ATOM   5535 N  N   . PHE C 1 159 ? 43.785  -4.624  -17.127 1.00 25.85 ? 159 PHE C N   1 
ATOM   5536 C  CA  . PHE C 1 159 ? 42.557  -4.410  -16.363 1.00 25.33 ? 159 PHE C CA  1 
ATOM   5537 C  C   . PHE C 1 159 ? 42.967  -4.101  -14.922 1.00 26.56 ? 159 PHE C C   1 
ATOM   5538 O  O   . PHE C 1 159 ? 42.214  -3.491  -14.162 1.00 24.96 ? 159 PHE C O   1 
ATOM   5539 C  CB  . PHE C 1 159 ? 41.616  -5.634  -16.441 1.00 26.21 ? 159 PHE C CB  1 
ATOM   5540 C  CG  . PHE C 1 159 ? 40.866  -5.764  -17.763 1.00 30.13 ? 159 PHE C CG  1 
ATOM   5541 C  CD1 . PHE C 1 159 ? 40.679  -4.661  -18.654 1.00 29.23 ? 159 PHE C CD1 1 
ATOM   5542 C  CD2 . PHE C 1 159 ? 40.359  -7.011  -18.137 1.00 22.83 ? 159 PHE C CD2 1 
ATOM   5543 C  CE1 . PHE C 1 159 ? 40.011  -4.852  -19.893 1.00 26.58 ? 159 PHE C CE1 1 
ATOM   5544 C  CE2 . PHE C 1 159 ? 39.675  -7.183  -19.359 1.00 31.72 ? 159 PHE C CE2 1 
ATOM   5545 C  CZ  . PHE C 1 159 ? 39.531  -6.127  -20.238 1.00 25.65 ? 159 PHE C CZ  1 
ATOM   5546 N  N   A SER C 1 160 ? 44.171  -4.530  -14.553 0.50 24.52 ? 160 SER C N   1 
ATOM   5547 N  N   B SER C 1 160 ? 44.187  -4.463  -14.561 0.50 25.10 ? 160 SER C N   1 
ATOM   5548 C  CA  A SER C 1 160 ? 44.586  -4.431  -13.164 0.50 22.34 ? 160 SER C CA  1 
ATOM   5549 C  CA  B SER C 1 160 ? 44.585  -4.380  -13.175 0.50 23.43 ? 160 SER C CA  1 
ATOM   5550 C  C   A SER C 1 160 ? 44.876  -3.027  -12.693 0.50 23.52 ? 160 SER C C   1 
ATOM   5551 C  C   B SER C 1 160 ? 45.169  -3.066  -12.784 0.50 24.60 ? 160 SER C C   1 
ATOM   5552 O  O   A SER C 1 160 ? 44.982  -2.801  -11.493 0.50 22.24 ? 160 SER C O   1 
ATOM   5553 O  O   B SER C 1 160 ? 45.783  -2.928  -11.715 0.50 24.55 ? 160 SER C O   1 
ATOM   5554 C  CB  A SER C 1 160 ? 45.709  -5.407  -12.791 0.50 23.55 ? 160 SER C CB  1 
ATOM   5555 C  CB  B SER C 1 160 ? 45.511  -5.503  -12.848 0.50 25.32 ? 160 SER C CB  1 
ATOM   5556 O  OG  A SER C 1 160 ? 46.753  -5.515  -13.746 0.50 19.59 ? 160 SER C OG  1 
ATOM   5557 O  OG  B SER C 1 160 ? 44.815  -6.671  -13.162 0.50 22.62 ? 160 SER C OG  1 
ATOM   5558 N  N   . HIS C 1 161 ? 44.920  -2.090  -13.623 1.00 23.40 ? 161 HIS C N   1 
ATOM   5559 C  CA  . HIS C 1 161 ? 45.273  -0.743  -13.342 1.00 24.08 ? 161 HIS C CA  1 
ATOM   5560 C  C   . HIS C 1 161 ? 44.171  0.192   -13.456 1.00 22.91 ? 161 HIS C C   1 
ATOM   5561 O  O   . HIS C 1 161 ? 44.382  1.441   -13.334 1.00 23.43 ? 161 HIS C O   1 
ATOM   5562 C  CB  . HIS C 1 161 ? 46.481  -0.359  -14.251 1.00 30.40 ? 161 HIS C CB  1 
ATOM   5563 C  CG  . HIS C 1 161 ? 47.633  -1.369  -14.166 1.00 35.60 ? 161 HIS C CG  1 
ATOM   5564 N  ND1 . HIS C 1 161 ? 48.762  -1.138  -13.461 1.00 36.81 ? 161 HIS C ND1 1 
ATOM   5565 C  CD2 . HIS C 1 161 ? 47.753  -2.669  -14.676 1.00 33.68 ? 161 HIS C CD2 1 
ATOM   5566 C  CE1 . HIS C 1 161 ? 49.578  -2.216  -13.545 1.00 36.78 ? 161 HIS C CE1 1 
ATOM   5567 N  NE2 . HIS C 1 161 ? 48.948  -3.153  -14.285 1.00 38.60 ? 161 HIS C NE2 1 
ATOM   5568 N  N   . LEU C 1 162 ? 42.953  -0.341  -13.671 1.00 25.22 ? 162 LEU C N   1 
ATOM   5569 C  CA  . LEU C 1 162 ? 41.833  0.544   -13.920 1.00 25.76 ? 162 LEU C CA  1 
ATOM   5570 C  C   . LEU C 1 162 ? 41.546  1.405   -12.717 1.00 24.08 ? 162 LEU C C   1 
ATOM   5571 O  O   . LEU C 1 162 ? 41.190  2.587   -12.908 1.00 23.54 ? 162 LEU C O   1 
ATOM   5572 C  CB  . LEU C 1 162 ? 40.570  -0.197  -14.401 1.00 25.09 ? 162 LEU C CB  1 
ATOM   5573 C  CG  . LEU C 1 162 ? 40.711  -1.620  -14.939 1.00 31.22 ? 162 LEU C CG  1 
ATOM   5574 C  CD1 . LEU C 1 162 ? 39.866  -2.586  -14.131 1.00 34.95 ? 162 LEU C CD1 1 
ATOM   5575 C  CD2 . LEU C 1 162 ? 40.283  -1.624  -16.391 1.00 30.26 ? 162 LEU C CD2 1 
ATOM   5576 N  N   . GLN C 1 163 ? 41.808  0.908   -11.498 1.00 25.70 ? 163 GLN C N   1 
ATOM   5577 C  CA  . GLN C 1 163 ? 41.509  1.700   -10.278 1.00 25.67 ? 163 GLN C CA  1 
ATOM   5578 C  C   . GLN C 1 163 ? 42.478  2.877   -10.119 1.00 22.34 ? 163 GLN C C   1 
ATOM   5579 O  O   . GLN C 1 163 ? 42.266  3.742   -9.239  1.00 25.83 ? 163 GLN C O   1 
ATOM   5580 C  CB  . GLN C 1 163 ? 41.472  0.838   -9.003  1.00 26.94 ? 163 GLN C CB  1 
ATOM   5581 C  CG  . GLN C 1 163 ? 40.418  -0.323  -9.001  1.00 27.22 ? 163 GLN C CG  1 
ATOM   5582 C  CD  . GLN C 1 163 ? 38.934  0.117   -9.066  1.00 33.97 ? 163 GLN C CD  1 
ATOM   5583 O  OE1 . GLN C 1 163 ? 38.527  1.207   -8.610  1.00 31.25 ? 163 GLN C OE1 1 
ATOM   5584 N  NE2 . GLN C 1 163 ? 38.109  -0.746  -9.645  1.00 34.17 ? 163 GLN C NE2 1 
ATOM   5585 N  N   . HIS C 1 164 ? 43.544  2.919   -10.935 1.00 25.11 ? 164 HIS C N   1 
ATOM   5586 C  CA  . HIS C 1 164 ? 44.430  4.089   -10.912 1.00 21.17 ? 164 HIS C CA  1 
ATOM   5587 C  C   . HIS C 1 164 ? 44.009  5.267   -11.770 1.00 27.56 ? 164 HIS C C   1 
ATOM   5588 O  O   . HIS C 1 164 ? 44.499  6.416   -11.615 1.00 24.35 ? 164 HIS C O   1 
ATOM   5589 C  CB  . HIS C 1 164 ? 45.891  3.707   -11.136 1.00 24.73 ? 164 HIS C CB  1 
ATOM   5590 C  CG  . HIS C 1 164 ? 46.397  2.647   -10.164 1.00 21.73 ? 164 HIS C CG  1 
ATOM   5591 N  ND1 . HIS C 1 164 ? 46.565  2.874   -8.832  1.00 28.35 ? 164 HIS C ND1 1 
ATOM   5592 C  CD2 . HIS C 1 164 ? 46.680  1.309   -10.365 1.00 24.38 ? 164 HIS C CD2 1 
ATOM   5593 C  CE1 . HIS C 1 164 ? 46.935  1.740   -8.236  1.00 23.30 ? 164 HIS C CE1 1 
ATOM   5594 N  NE2 . HIS C 1 164 ? 47.042  0.791   -9.168  1.00 26.39 ? 164 HIS C NE2 1 
ATOM   5595 N  N   . VAL C 1 165 ? 43.084  4.999   -12.695 1.00 25.95 ? 165 VAL C N   1 
ATOM   5596 C  CA  . VAL C 1 165 ? 42.610  6.041   -13.597 1.00 23.59 ? 165 VAL C CA  1 
ATOM   5597 C  C   . VAL C 1 165 ? 41.073  6.204   -13.523 1.00 23.93 ? 165 VAL C C   1 
ATOM   5598 O  O   . VAL C 1 165 ? 40.358  6.357   -14.530 1.00 21.31 ? 165 VAL C O   1 
ATOM   5599 C  CB  . VAL C 1 165 ? 43.145  5.730   -15.018 1.00 23.93 ? 165 VAL C CB  1 
ATOM   5600 C  CG1 . VAL C 1 165 ? 44.640  6.029   -15.041 1.00 24.46 ? 165 VAL C CG1 1 
ATOM   5601 C  CG2 . VAL C 1 165 ? 42.887  4.272   -15.398 1.00 19.79 ? 165 VAL C CG2 1 
ATOM   5602 N  N   . LYS C 1 166 ? 40.525  6.232   -12.326 1.00 22.17 ? 166 LYS C N   1 
ATOM   5603 C  CA  . LYS C 1 166 ? 39.074  6.161   -12.221 1.00 19.44 ? 166 LYS C CA  1 
ATOM   5604 C  C   . LYS C 1 166 ? 38.381  7.361   -12.711 1.00 22.82 ? 166 LYS C C   1 
ATOM   5605 O  O   . LYS C 1 166 ? 37.178  7.306   -13.065 1.00 23.78 ? 166 LYS C O   1 
ATOM   5606 C  CB  . LYS C 1 166 ? 38.628  5.808   -10.754 1.00 25.15 ? 166 LYS C CB  1 
ATOM   5607 C  CG  . LYS C 1 166 ? 38.964  4.366   -10.380 1.00 25.03 ? 166 LYS C CG  1 
ATOM   5608 C  CD  . LYS C 1 166 ? 38.488  4.000   -8.958  1.00 30.95 ? 166 LYS C CD  1 
ATOM   5609 C  CE  . LYS C 1 166 ? 36.960  3.995   -8.811  1.00 30.07 ? 166 LYS C CE  1 
ATOM   5610 N  NZ  . LYS C 1 166 ? 36.319  2.699   -9.208  1.00 31.88 ? 166 LYS C NZ  1 
ATOM   5611 N  N   . TYR C 1 167 ? 39.076  8.476   -12.805 1.00 21.11 ? 167 TYR C N   1 
ATOM   5612 C  CA  . TYR C 1 167 ? 38.363  9.687   -13.131 1.00 24.39 ? 167 TYR C CA  1 
ATOM   5613 C  C   . TYR C 1 167 ? 38.868  10.266  -14.430 1.00 22.58 ? 167 TYR C C   1 
ATOM   5614 O  O   . TYR C 1 167 ? 40.033  10.046  -14.790 1.00 28.20 ? 167 TYR C O   1 
ATOM   5615 C  CB  . TYR C 1 167 ? 38.499  10.730  -11.991 1.00 23.59 ? 167 TYR C CB  1 
ATOM   5616 C  CG  . TYR C 1 167 ? 37.888  10.297  -10.667 1.00 27.49 ? 167 TYR C CG  1 
ATOM   5617 C  CD1 . TYR C 1 167 ? 36.493  10.312  -10.476 1.00 28.88 ? 167 TYR C CD1 1 
ATOM   5618 C  CD2 . TYR C 1 167 ? 38.702  9.806   -9.622  1.00 26.05 ? 167 TYR C CD2 1 
ATOM   5619 C  CE1 . TYR C 1 167 ? 35.945  9.906   -9.257  1.00 31.47 ? 167 TYR C CE1 1 
ATOM   5620 C  CE2 . TYR C 1 167 ? 38.163  9.393   -8.402  1.00 29.90 ? 167 TYR C CE2 1 
ATOM   5621 C  CZ  . TYR C 1 167 ? 36.783  9.425   -8.231  1.00 32.21 ? 167 TYR C CZ  1 
ATOM   5622 O  OH  . TYR C 1 167 ? 36.220  9.037   -7.021  1.00 34.92 ? 167 TYR C OH  1 
ATOM   5623 N  N   . LYS C 1 168 ? 38.060  11.149  -15.041 1.00 23.60 ? 168 LYS C N   1 
ATOM   5624 C  CA  . LYS C 1 168 ? 38.467  11.732  -16.307 1.00 22.76 ? 168 LYS C CA  1 
ATOM   5625 C  C   . LYS C 1 168 ? 39.743  12.590  -16.111 1.00 26.09 ? 168 LYS C C   1 
ATOM   5626 O  O   . LYS C 1 168 ? 39.823  13.434  -15.160 1.00 29.12 ? 168 LYS C O   1 
ATOM   5627 C  CB  . LYS C 1 168 ? 37.417  12.701  -16.837 1.00 26.09 ? 168 LYS C CB  1 
ATOM   5628 C  CG  . LYS C 1 168 ? 37.833  13.370  -18.143 1.00 24.64 ? 168 LYS C CG  1 
ATOM   5629 C  CD  . LYS C 1 168 ? 36.670  14.162  -18.652 1.00 29.97 ? 168 LYS C CD  1 
ATOM   5630 C  CE  . LYS C 1 168 ? 37.014  14.824  -19.973 1.00 29.93 ? 168 LYS C CE  1 
ATOM   5631 N  NZ  . LYS C 1 168 ? 35.855  15.701  -20.334 1.00 38.92 ? 168 LYS C NZ  1 
ATOM   5632 N  N   . GLY C 1 169 ? 40.685  12.401  -17.035 1.00 24.16 ? 169 GLY C N   1 
ATOM   5633 C  CA  . GLY C 1 169 ? 41.936  13.132  -17.064 1.00 25.94 ? 169 GLY C CA  1 
ATOM   5634 C  C   . GLY C 1 169 ? 43.035  12.443  -16.291 1.00 24.39 ? 169 GLY C C   1 
ATOM   5635 O  O   . GLY C 1 169 ? 44.194  12.888  -16.357 1.00 25.69 ? 169 GLY C O   1 
ATOM   5636 N  N   . GLN C 1 170 ? 42.723  11.378  -15.534 1.00 22.40 ? 170 GLN C N   1 
ATOM   5637 C  CA  . GLN C 1 170 ? 43.737  10.744  -14.748 1.00 23.56 ? 170 GLN C CA  1 
ATOM   5638 C  C   . GLN C 1 170 ? 44.633  9.874   -15.554 1.00 25.50 ? 170 GLN C C   1 
ATOM   5639 O  O   . GLN C 1 170 ? 44.204  9.180   -16.499 1.00 22.48 ? 170 GLN C O   1 
ATOM   5640 C  CB  . GLN C 1 170 ? 43.171  9.957   -13.536 1.00 28.13 ? 170 GLN C CB  1 
ATOM   5641 C  CG  . GLN C 1 170 ? 42.681  10.885  -12.417 1.00 26.71 ? 170 GLN C CG  1 
ATOM   5642 C  CD  . GLN C 1 170 ? 42.227  10.082  -11.204 1.00 29.06 ? 170 GLN C CD  1 
ATOM   5643 O  OE1 . GLN C 1 170 ? 41.598  9.024   -11.363 1.00 27.92 ? 170 GLN C OE1 1 
ATOM   5644 N  NE2 . GLN C 1 170 ? 42.551  10.572  -9.973  1.00 28.08 ? 170 GLN C NE2 1 
ATOM   5645 N  N   . GLU C 1 171 ? 45.904  9.869   -15.198 1.00 24.66 ? 171 GLU C N   1 
ATOM   5646 C  CA  . GLU C 1 171 ? 46.857  8.937   -15.870 1.00 26.77 ? 171 GLU C CA  1 
ATOM   5647 C  C   . GLU C 1 171 ? 47.594  8.018   -14.917 1.00 28.61 ? 171 GLU C C   1 
ATOM   5648 O  O   . GLU C 1 171 ? 47.801  8.372   -13.722 1.00 31.39 ? 171 GLU C O   1 
ATOM   5649 C  CB  . GLU C 1 171 ? 47.873  9.727   -16.716 1.00 29.59 ? 171 GLU C CB  1 
ATOM   5650 C  CG  . GLU C 1 171 ? 47.168  10.725  -17.612 1.00 30.43 ? 171 GLU C CG  1 
ATOM   5651 C  CD  . GLU C 1 171 ? 48.131  11.669  -18.309 1.00 36.05 ? 171 GLU C CD  1 
ATOM   5652 O  OE1 . GLU C 1 171 ? 49.252  11.893  -17.761 1.00 37.95 ? 171 GLU C OE1 1 
ATOM   5653 O  OE2 . GLU C 1 171 ? 47.718  12.170  -19.404 1.00 39.12 ? 171 GLU C OE2 1 
ATOM   5654 N  N   . ALA C 1 172 ? 48.005  6.871   -15.425 1.00 23.21 ? 172 ALA C N   1 
ATOM   5655 C  CA  . ALA C 1 172 ? 48.839  5.921   -14.668 1.00 28.51 ? 172 ALA C CA  1 
ATOM   5656 C  C   . ALA C 1 172 ? 49.697  5.132   -15.614 1.00 31.69 ? 172 ALA C C   1 
ATOM   5657 O  O   . ALA C 1 172 ? 49.457  5.159   -16.818 1.00 35.14 ? 172 ALA C O   1 
ATOM   5658 C  CB  . ALA C 1 172 ? 48.003  4.985   -13.781 1.00 26.85 ? 172 ALA C CB  1 
ATOM   5659 N  N   . PHE C 1 173 ? 50.738  4.476   -15.118 1.00 33.43 ? 173 PHE C N   1 
ATOM   5660 C  CA  . PHE C 1 173 ? 51.632  3.666   -16.004 1.00 34.72 ? 173 PHE C CA  1 
ATOM   5661 C  C   . PHE C 1 173 ? 51.323  2.156   -15.855 1.00 34.49 ? 173 PHE C C   1 
ATOM   5662 O  O   . PHE C 1 173 ? 50.831  1.711   -14.816 1.00 27.65 ? 173 PHE C O   1 
ATOM   5663 C  CB  . PHE C 1 173 ? 53.153  4.014   -15.886 1.00 34.99 ? 173 PHE C CB  1 
ATOM   5664 C  CG  . PHE C 1 173 ? 53.576  5.335   -16.558 1.00 33.55 ? 173 PHE C CG  1 
ATOM   5665 C  CD1 . PHE C 1 173 ? 53.874  5.395   -17.945 1.00 34.11 ? 173 PHE C CD1 1 
ATOM   5666 C  CD2 . PHE C 1 173 ? 53.725  6.527   -15.823 1.00 34.17 ? 173 PHE C CD2 1 
ATOM   5667 C  CE1 . PHE C 1 173 ? 54.277  6.596   -18.568 1.00 35.07 ? 173 PHE C CE1 1 
ATOM   5668 C  CE2 . PHE C 1 173 ? 54.129  7.727   -16.448 1.00 36.55 ? 173 PHE C CE2 1 
ATOM   5669 C  CZ  . PHE C 1 173 ? 54.414  7.765   -17.824 1.00 33.51 ? 173 PHE C CZ  1 
ATOM   5670 N  N   . VAL C 1 174 ? 51.484  1.423   -16.956 1.00 30.52 ? 174 VAL C N   1 
ATOM   5671 C  CA  . VAL C 1 174 ? 51.298  -0.068  -17.033 1.00 33.16 ? 174 VAL C CA  1 
ATOM   5672 C  C   . VAL C 1 174 ? 52.594  -0.548  -17.606 1.00 33.73 ? 174 VAL C C   1 
ATOM   5673 O  O   . VAL C 1 174 ? 53.048  -0.035  -18.662 1.00 34.34 ? 174 VAL C O   1 
ATOM   5674 C  CB  . VAL C 1 174 ? 50.179  -0.517  -18.038 1.00 34.38 ? 174 VAL C CB  1 
ATOM   5675 C  CG1 . VAL C 1 174 ? 50.294  -2.007  -18.445 1.00 28.47 ? 174 VAL C CG1 1 
ATOM   5676 C  CG2 . VAL C 1 174 ? 48.827  -0.318  -17.392 1.00 37.68 ? 174 VAL C CG2 1 
ATOM   5677 N  N   . PRO C 1 175 ? 53.211  -1.536  -16.942 1.00 34.03 ? 175 PRO C N   1 
ATOM   5678 C  CA  . PRO C 1 175 ? 54.448  -2.046  -17.506 1.00 31.33 ? 175 PRO C CA  1 
ATOM   5679 C  C   . PRO C 1 175 ? 54.185  -2.646  -18.893 1.00 28.24 ? 175 PRO C C   1 
ATOM   5680 O  O   . PRO C 1 175 ? 53.093  -3.025  -19.136 1.00 26.08 ? 175 PRO C O   1 
ATOM   5681 C  CB  . PRO C 1 175 ? 54.876  -3.129  -16.487 1.00 31.92 ? 175 PRO C CB  1 
ATOM   5682 C  CG  . PRO C 1 175 ? 53.654  -3.422  -15.656 1.00 33.39 ? 175 PRO C CG  1 
ATOM   5683 C  CD  . PRO C 1 175 ? 52.877  -2.135  -15.631 1.00 32.40 ? 175 PRO C CD  1 
ATOM   5684 N  N   . GLY C 1 176 ? 55.204  -2.771  -19.741 1.00 25.07 ? 176 GLY C N   1 
ATOM   5685 C  CA  . GLY C 1 176 ? 55.085  -3.330  -21.063 1.00 25.62 ? 176 GLY C CA  1 
ATOM   5686 C  C   . GLY C 1 176 ? 54.797  -4.827  -20.997 1.00 25.37 ? 176 GLY C C   1 
ATOM   5687 O  O   . GLY C 1 176 ? 55.077  -5.445  -19.984 1.00 23.89 ? 176 GLY C O   1 
ATOM   5688 N  N   . PHE C 1 177 ? 54.160  -5.332  -22.051 1.00 27.11 ? 177 PHE C N   1 
ATOM   5689 C  CA  . PHE C 1 177 ? 53.866  -6.813  -22.252 1.00 24.87 ? 177 PHE C CA  1 
ATOM   5690 C  C   . PHE C 1 177 ? 53.631  -7.054  -23.761 1.00 29.72 ? 177 PHE C C   1 
ATOM   5691 O  O   . PHE C 1 177 ? 53.602  -6.093  -24.541 1.00 26.60 ? 177 PHE C O   1 
ATOM   5692 C  CB  . PHE C 1 177 ? 52.668  -7.263  -21.335 1.00 27.76 ? 177 PHE C CB  1 
ATOM   5693 C  CG  . PHE C 1 177 ? 51.312  -6.768  -21.762 1.00 27.30 ? 177 PHE C CG  1 
ATOM   5694 C  CD1 . PHE C 1 177 ? 50.474  -7.566  -22.501 1.00 27.45 ? 177 PHE C CD1 1 
ATOM   5695 C  CD2 . PHE C 1 177 ? 50.898  -5.465  -21.438 1.00 26.46 ? 177 PHE C CD2 1 
ATOM   5696 C  CE1 . PHE C 1 177 ? 49.230  -7.125  -22.923 1.00 28.35 ? 177 PHE C CE1 1 
ATOM   5697 C  CE2 . PHE C 1 177 ? 49.652  -4.985  -21.843 1.00 30.42 ? 177 PHE C CE2 1 
ATOM   5698 C  CZ  . PHE C 1 177 ? 48.827  -5.816  -22.625 1.00 27.56 ? 177 PHE C CZ  1 
ATOM   5699 N  N   . ASN C 1 178 ? 53.498  -8.300  -24.205 1.00 23.67 ? 178 ASN C N   1 
ATOM   5700 C  CA  . ASN C 1 178 ? 53.357  -8.572  -25.592 1.00 23.38 ? 178 ASN C CA  1 
ATOM   5701 C  C   . ASN C 1 178 ? 51.924  -8.282  -26.095 1.00 26.79 ? 178 ASN C C   1 
ATOM   5702 O  O   . ASN C 1 178 ? 50.985  -8.980  -25.704 1.00 26.83 ? 178 ASN C O   1 
ATOM   5703 C  CB  . ASN C 1 178 ? 53.574  -10.077 -25.730 1.00 24.06 ? 178 ASN C CB  1 
ATOM   5704 C  CG  . ASN C 1 178 ? 53.567  -10.517 -27.163 1.00 29.74 ? 178 ASN C CG  1 
ATOM   5705 O  OD1 . ASN C 1 178 ? 53.472  -9.691  -28.119 1.00 24.86 ? 178 ASN C OD1 1 
ATOM   5706 N  ND2 . ASN C 1 178 ? 53.616  -11.835 -27.347 1.00 25.12 ? 178 ASN C ND2 1 
ATOM   5707 N  N   . ILE C 1 179 ? 51.762  -7.173  -26.834 1.00 25.17 ? 179 ILE C N   1 
ATOM   5708 C  CA  . ILE C 1 179 ? 50.443  -6.768  -27.269 1.00 25.54 ? 179 ILE C CA  1 
ATOM   5709 C  C   . ILE C 1 179 ? 49.775  -7.873  -28.087 1.00 25.60 ? 179 ILE C C   1 
ATOM   5710 O  O   . ILE C 1 179 ? 48.514  -7.970  -28.192 1.00 28.11 ? 179 ILE C O   1 
ATOM   5711 C  CB  . ILE C 1 179 ? 50.498  -5.414  -27.988 1.00 27.35 ? 179 ILE C CB  1 
ATOM   5712 C  CG1 . ILE C 1 179 ? 51.075  -4.366  -27.048 1.00 27.17 ? 179 ILE C CG1 1 
ATOM   5713 C  CG2 . ILE C 1 179 ? 49.100  -4.984  -28.456 1.00 28.56 ? 179 ILE C CG2 1 
ATOM   5714 C  CD1 . ILE C 1 179 ? 50.378  -4.268  -25.668 1.00 26.20 ? 179 ILE C CD1 1 
ATOM   5715 N  N   . GLU C 1 180 ? 50.575  -8.716  -28.676 1.00 27.56 ? 180 GLU C N   1 
ATOM   5716 C  CA  . GLU C 1 180 ? 50.033  -9.745  -29.557 1.00 25.23 ? 180 GLU C CA  1 
ATOM   5717 C  C   . GLU C 1 180 ? 49.184  -10.781 -28.799 1.00 33.21 ? 180 GLU C C   1 
ATOM   5718 O  O   . GLU C 1 180 ? 48.361  -11.462 -29.376 1.00 23.74 ? 180 GLU C O   1 
ATOM   5719 C  CB  . GLU C 1 180 ? 51.120  -10.373 -30.418 1.00 27.96 ? 180 GLU C CB  1 
ATOM   5720 C  CG  . GLU C 1 180 ? 50.636  -11.422 -31.405 1.00 31.08 ? 180 GLU C CG  1 
ATOM   5721 C  CD  . GLU C 1 180 ? 51.729  -11.848 -32.396 1.00 35.16 ? 180 GLU C CD  1 
ATOM   5722 O  OE1 . GLU C 1 180 ? 52.896  -11.366 -32.274 1.00 32.29 ? 180 GLU C OE1 1 
ATOM   5723 O  OE2 . GLU C 1 180 ? 51.409  -12.710 -33.259 1.00 30.78 ? 180 GLU C OE2 1 
ATOM   5724 N  N   . GLU C 1 181 ? 49.365  -10.911 -27.492 1.00 30.96 ? 181 GLU C N   1 
ATOM   5725 C  CA  . GLU C 1 181 ? 48.530  -11.903 -26.803 1.00 33.16 ? 181 GLU C CA  1 
ATOM   5726 C  C   . GLU C 1 181 ? 47.028  -11.480 -26.735 1.00 30.81 ? 181 GLU C C   1 
ATOM   5727 O  O   . GLU C 1 181 ? 46.191  -12.337 -26.406 1.00 30.50 ? 181 GLU C O   1 
ATOM   5728 C  CB  . GLU C 1 181 ? 49.069  -12.228 -25.398 1.00 36.71 ? 181 GLU C CB  1 
ATOM   5729 C  CG  . GLU C 1 181 ? 50.585  -12.389 -25.276 1.00 44.42 ? 181 GLU C CG  1 
ATOM   5730 C  CD  . GLU C 1 181 ? 51.036  -12.597 -23.825 1.00 47.66 ? 181 GLU C CD  1 
ATOM   5731 O  OE1 . GLU C 1 181 ? 50.203  -13.054 -23.017 1.00 45.30 ? 181 GLU C OE1 1 
ATOM   5732 O  OE2 . GLU C 1 181 ? 52.228  -12.318 -23.482 1.00 48.40 ? 181 GLU C OE2 1 
ATOM   5733 N  N   . LEU C 1 182 ? 46.745  -10.180 -26.972 1.00 27.31 ? 182 LEU C N   1 
ATOM   5734 C  CA  . LEU C 1 182 ? 45.340  -9.625  -27.045 1.00 21.77 ? 182 LEU C CA  1 
ATOM   5735 C  C   . LEU C 1 182 ? 44.555  -10.171 -28.321 1.00 27.79 ? 182 LEU C C   1 
ATOM   5736 O  O   . LEU C 1 182 ? 43.300  -10.265 -28.401 1.00 21.17 ? 182 LEU C O   1 
ATOM   5737 C  CB  . LEU C 1 182 ? 45.392  -8.084  -26.889 1.00 25.41 ? 182 LEU C CB  1 
ATOM   5738 C  CG  . LEU C 1 182 ? 46.080  -7.398  -25.686 1.00 18.66 ? 182 LEU C CG  1 
ATOM   5739 C  CD1 . LEU C 1 182 ? 45.956  -5.870  -25.634 1.00 20.71 ? 182 LEU C CD1 1 
ATOM   5740 C  CD2 . LEU C 1 182 ? 45.685  -7.887  -24.259 1.00 22.44 ? 182 LEU C CD2 1 
ATOM   5741 N  N   . LEU C 1 183 ? 45.299  -10.556 -29.333 1.00 23.81 ? 183 LEU C N   1 
ATOM   5742 C  CA  . LEU C 1 183 ? 44.750  -11.089 -30.535 1.00 24.60 ? 183 LEU C CA  1 
ATOM   5743 C  C   . LEU C 1 183 ? 44.151  -12.470 -30.417 1.00 25.46 ? 183 LEU C C   1 
ATOM   5744 O  O   . LEU C 1 183 ? 44.578  -13.294 -29.576 1.00 24.84 ? 183 LEU C O   1 
ATOM   5745 C  CB  . LEU C 1 183 ? 45.779  -11.007 -31.666 1.00 24.92 ? 183 LEU C CB  1 
ATOM   5746 C  CG  . LEU C 1 183 ? 46.396  -9.637  -31.965 1.00 24.89 ? 183 LEU C CG  1 
ATOM   5747 C  CD1 . LEU C 1 183 ? 47.250  -9.716  -33.225 1.00 26.92 ? 183 LEU C CD1 1 
ATOM   5748 C  CD2 . LEU C 1 183 ? 45.303  -8.586  -32.119 1.00 23.15 ? 183 LEU C CD2 1 
ATOM   5749 N  N   . PRO C 1 184 ? 43.152  -12.765 -31.242 1.00 27.32 ? 184 PRO C N   1 
ATOM   5750 C  CA  . PRO C 1 184 ? 42.474  -14.041 -31.198 1.00 27.43 ? 184 PRO C CA  1 
ATOM   5751 C  C   . PRO C 1 184 ? 43.189  -15.188 -31.950 1.00 32.11 ? 184 PRO C C   1 
ATOM   5752 O  O   . PRO C 1 184 ? 44.296  -14.993 -32.494 1.00 29.55 ? 184 PRO C O   1 
ATOM   5753 C  CB  . PRO C 1 184 ? 41.099  -13.713 -31.803 1.00 28.39 ? 184 PRO C CB  1 
ATOM   5754 C  CG  . PRO C 1 184 ? 41.448  -12.655 -32.811 1.00 22.92 ? 184 PRO C CG  1 
ATOM   5755 C  CD  . PRO C 1 184 ? 42.529  -11.828 -32.213 1.00 25.05 ? 184 PRO C CD  1 
ATOM   5756 N  N   . GLU C 1 185 ? 42.578  -16.377 -31.941 1.00 34.58 ? 185 GLU C N   1 
ATOM   5757 C  CA  . GLU C 1 185 ? 42.980  -17.505 -32.773 1.00 40.67 ? 185 GLU C CA  1 
ATOM   5758 C  C   . GLU C 1 185 ? 42.793  -17.253 -34.275 1.00 37.51 ? 185 GLU C C   1 
ATOM   5759 O  O   . GLU C 1 185 ? 41.827  -16.564 -34.711 1.00 31.25 ? 185 GLU C O   1 
ATOM   5760 C  CB  . GLU C 1 185 ? 42.143  -18.748 -32.417 1.00 44.59 ? 185 GLU C CB  1 
ATOM   5761 C  CG  . GLU C 1 185 ? 42.414  -19.339 -31.048 1.00 54.72 ? 185 GLU C CG  1 
ATOM   5762 C  CD  . GLU C 1 185 ? 43.883  -19.579 -30.804 1.00 60.36 ? 185 GLU C CD  1 
ATOM   5763 O  OE1 . GLU C 1 185 ? 44.523  -18.662 -30.239 1.00 62.26 ? 185 GLU C OE1 1 
ATOM   5764 O  OE2 . GLU C 1 185 ? 44.387  -20.662 -31.188 1.00 61.36 ? 185 GLU C OE2 1 
ATOM   5765 N  N   . ARG C 1 186 ? 43.694  -17.834 -35.067 1.00 32.90 ? 186 ARG C N   1 
ATOM   5766 C  CA  . ARG C 1 186 ? 43.608  -17.762 -36.535 1.00 33.79 ? 186 ARG C CA  1 
ATOM   5767 C  C   . ARG C 1 186 ? 43.424  -16.317 -37.044 1.00 31.88 ? 186 ARG C C   1 
ATOM   5768 O  O   . ARG C 1 186 ? 42.451  -15.981 -37.797 1.00 29.63 ? 186 ARG C O   1 
ATOM   5769 C  CB  . ARG C 1 186 ? 42.563  -18.742 -37.036 1.00 39.39 ? 186 ARG C CB  1 
ATOM   5770 C  CG  . ARG C 1 186 ? 42.727  -20.094 -36.341 1.00 45.04 ? 186 ARG C CG  1 
ATOM   5771 C  CD  . ARG C 1 186 ? 41.694  -21.108 -36.774 1.00 55.33 ? 186 ARG C CD  1 
ATOM   5772 N  NE  . ARG C 1 186 ? 40.413  -20.954 -36.076 1.00 56.90 ? 186 ARG C NE  1 
ATOM   5773 C  CZ  . ARG C 1 186 ? 39.241  -21.292 -36.613 1.00 58.72 ? 186 ARG C CZ  1 
ATOM   5774 N  NH1 . ARG C 1 186 ? 39.208  -21.793 -37.849 1.00 61.40 ? 186 ARG C NH1 1 
ATOM   5775 N  NH2 . ARG C 1 186 ? 38.106  -21.135 -35.931 1.00 54.39 ? 186 ARG C NH2 1 
ATOM   5776 N  N   . THR C 1 187 ? 44.374  -15.459 -36.656 1.00 26.83 ? 187 THR C N   1 
ATOM   5777 C  CA  . THR C 1 187 ? 44.387  -14.096 -37.148 1.00 24.97 ? 187 THR C CA  1 
ATOM   5778 C  C   . THR C 1 187 ? 44.336  -13.999 -38.688 1.00 22.24 ? 187 THR C C   1 
ATOM   5779 O  O   . THR C 1 187 ? 44.085  -12.897 -39.145 1.00 17.98 ? 187 THR C O   1 
ATOM   5780 C  CB  . THR C 1 187 ? 45.581  -13.249 -36.668 1.00 27.27 ? 187 THR C CB  1 
ATOM   5781 O  OG1 . THR C 1 187 ? 46.763  -14.017 -36.890 1.00 30.64 ? 187 THR C OG1 1 
ATOM   5782 C  CG2 . THR C 1 187 ? 45.421  -12.870 -35.171 1.00 29.06 ? 187 THR C CG2 1 
ATOM   5783 N  N   . ALA C 1 188 ? 44.641  -15.084 -39.442 1.00 18.41 ? 188 ALA C N   1 
ATOM   5784 C  CA  . ALA C 1 188 ? 44.552  -15.117 -40.936 1.00 21.34 ? 188 ALA C CA  1 
ATOM   5785 C  C   . ALA C 1 188 ? 43.095  -14.898 -41.393 1.00 19.18 ? 188 ALA C C   1 
ATOM   5786 O  O   . ALA C 1 188 ? 42.854  -14.435 -42.550 1.00 21.75 ? 188 ALA C O   1 
ATOM   5787 C  CB  . ALA C 1 188 ? 45.069  -16.448 -41.526 1.00 25.05 ? 188 ALA C CB  1 
ATOM   5788 N  N   . GLU C 1 189 ? 42.144  -15.211 -40.502 1.00 19.76 ? 189 GLU C N   1 
ATOM   5789 C  CA  . GLU C 1 189 ? 40.697  -15.013 -40.804 1.00 20.17 ? 189 GLU C CA  1 
ATOM   5790 C  C   . GLU C 1 189 ? 40.200  -13.625 -40.282 1.00 17.98 ? 189 GLU C C   1 
ATOM   5791 O  O   . GLU C 1 189 ? 40.175  -13.329 -39.040 1.00 18.34 ? 189 GLU C O   1 
ATOM   5792 C  CB  . GLU C 1 189 ? 39.856  -16.169 -40.239 1.00 24.75 ? 189 GLU C CB  1 
ATOM   5793 C  CG  . GLU C 1 189 ? 40.265  -17.479 -40.891 1.00 29.44 ? 189 GLU C CG  1 
ATOM   5794 C  CD  . GLU C 1 189 ? 39.861  -18.736 -40.127 1.00 36.96 ? 189 GLU C CD  1 
ATOM   5795 O  OE1 . GLU C 1 189 ? 39.018  -18.667 -39.190 1.00 37.53 ? 189 GLU C OE1 1 
ATOM   5796 O  OE2 . GLU C 1 189 ? 40.421  -19.820 -40.457 1.00 38.18 ? 189 GLU C OE2 1 
ATOM   5797 N  N   . TYR C 1 190 ? 39.795  -12.792 -41.231 1.00 14.18 ? 190 TYR C N   1 
ATOM   5798 C  CA  . TYR C 1 190 ? 39.363  -11.441 -40.874 1.00 14.12 ? 190 TYR C CA  1 
ATOM   5799 C  C   . TYR C 1 190 ? 38.466  -10.814 -41.918 1.00 13.36 ? 190 TYR C C   1 
ATOM   5800 O  O   . TYR C 1 190 ? 38.398  -11.243 -43.067 1.00 13.82 ? 190 TYR C O   1 
ATOM   5801 C  CB  . TYR C 1 190 ? 40.568  -10.507 -40.580 1.00 15.94 ? 190 TYR C CB  1 
ATOM   5802 C  CG  . TYR C 1 190 ? 41.548  -10.341 -41.749 1.00 13.92 ? 190 TYR C CG  1 
ATOM   5803 C  CD1 . TYR C 1 190 ? 41.376  -9.324  -42.722 1.00 14.39 ? 190 TYR C CD1 1 
ATOM   5804 C  CD2 . TYR C 1 190 ? 42.716  -11.146 -41.778 1.00 16.05 ? 190 TYR C CD2 1 
ATOM   5805 C  CE1 . TYR C 1 190 ? 42.275  -9.144  -43.768 1.00 14.24 ? 190 TYR C CE1 1 
ATOM   5806 C  CE2 . TYR C 1 190 ? 43.613  -10.972 -42.804 1.00 15.98 ? 190 TYR C CE2 1 
ATOM   5807 C  CZ  . TYR C 1 190 ? 43.376  -10.015 -43.775 1.00 16.40 ? 190 TYR C CZ  1 
ATOM   5808 O  OH  . TYR C 1 190 ? 44.315  -9.828  -44.775 1.00 16.60 ? 190 TYR C OH  1 
ATOM   5809 N  N   . TYR C 1 191 ? 37.747  -9.769  -41.472 1.00 13.35 ? 191 TYR C N   1 
ATOM   5810 C  CA  . TYR C 1 191 ? 36.941  -8.972  -42.308 1.00 11.81 ? 191 TYR C CA  1 
ATOM   5811 C  C   . TYR C 1 191 ? 37.684  -7.712  -42.598 1.00 10.63 ? 191 TYR C C   1 
ATOM   5812 O  O   . TYR C 1 191 ? 38.378  -7.228  -41.697 1.00 11.08 ? 191 TYR C O   1 
ATOM   5813 C  CB  . TYR C 1 191 ? 35.662  -8.564  -41.588 1.00 12.20 ? 191 TYR C CB  1 
ATOM   5814 C  CG  . TYR C 1 191 ? 34.753  -9.683  -41.026 1.00 12.76 ? 191 TYR C CG  1 
ATOM   5815 C  CD1 . TYR C 1 191 ? 33.737  -10.245 -41.820 1.00 13.36 ? 191 TYR C CD1 1 
ATOM   5816 C  CD2 . TYR C 1 191 ? 34.872  -10.094 -39.692 1.00 12.98 ? 191 TYR C CD2 1 
ATOM   5817 C  CE1 . TYR C 1 191 ? 32.899  -11.217 -41.310 1.00 14.75 ? 191 TYR C CE1 1 
ATOM   5818 C  CE2 . TYR C 1 191 ? 34.049  -11.053 -39.138 1.00 14.77 ? 191 TYR C CE2 1 
ATOM   5819 C  CZ  . TYR C 1 191 ? 33.061  -11.618 -39.978 1.00 15.05 ? 191 TYR C CZ  1 
ATOM   5820 O  OH  . TYR C 1 191 ? 32.246  -12.596 -39.484 1.00 18.81 ? 191 TYR C OH  1 
ATOM   5821 N  N   . ARG C 1 192 ? 37.473  -7.105  -43.781 1.00 10.19 ? 192 ARG C N   1 
ATOM   5822 C  CA  . ARG C 1 192 ? 38.217  -5.900  -44.160 1.00 10.95 ? 192 ARG C CA  1 
ATOM   5823 C  C   . ARG C 1 192 ? 37.308  -4.897  -44.835 1.00 10.77 ? 192 ARG C C   1 
ATOM   5824 O  O   . ARG C 1 192 ? 36.595  -5.272  -45.831 1.00 10.82 ? 192 ARG C O   1 
ATOM   5825 C  CB  . ARG C 1 192 ? 39.427  -6.242  -45.069 1.00 11.04 ? 192 ARG C CB  1 
ATOM   5826 C  CG  . ARG C 1 192 ? 40.028  -5.023  -45.850 1.00 13.99 ? 192 ARG C CG  1 
ATOM   5827 C  CD  . ARG C 1 192 ? 40.855  -4.079  -44.985 1.00 14.10 ? 192 ARG C CD  1 
ATOM   5828 N  NE  . ARG C 1 192 ? 41.802  -4.755  -44.132 1.00 14.98 ? 192 ARG C NE  1 
ATOM   5829 C  CZ  . ARG C 1 192 ? 42.957  -5.352  -44.488 1.00 15.74 ? 192 ARG C CZ  1 
ATOM   5830 N  NH1 . ARG C 1 192 ? 43.316  -5.389  -45.763 1.00 13.49 ? 192 ARG C NH1 1 
ATOM   5831 N  NH2 . ARG C 1 192 ? 43.759  -5.934  -43.548 1.00 15.11 ? 192 ARG C NH2 1 
ATOM   5832 N  N   . TYR C 1 193 ? 37.320  -3.609  -44.442 1.00 10.83 ? 193 TYR C N   1 
ATOM   5833 C  CA  . TYR C 1 193 ? 36.572  -2.661  -45.237 1.00 10.59 ? 193 TYR C CA  1 
ATOM   5834 C  C   . TYR C 1 193 ? 37.144  -1.271  -44.952 1.00 9.71  ? 193 TYR C C   1 
ATOM   5835 O  O   . TYR C 1 193 ? 37.809  -1.078  -43.884 1.00 10.93 ? 193 TYR C O   1 
ATOM   5836 C  CB  . TYR C 1 193 ? 35.054  -2.709  -44.913 1.00 10.08 ? 193 TYR C CB  1 
ATOM   5837 C  CG  . TYR C 1 193 ? 34.655  -2.135  -43.532 1.00 9.80  ? 193 TYR C CG  1 
ATOM   5838 C  CD1 . TYR C 1 193 ? 34.119  -0.854  -43.476 1.00 8.51  ? 193 TYR C CD1 1 
ATOM   5839 C  CD2 . TYR C 1 193 ? 34.796  -2.862  -42.356 1.00 9.33  ? 193 TYR C CD2 1 
ATOM   5840 C  CE1 . TYR C 1 193 ? 33.719  -0.318  -42.259 1.00 9.89  ? 193 TYR C CE1 1 
ATOM   5841 C  CE2 . TYR C 1 193 ? 34.458  -2.308  -41.096 1.00 9.27  ? 193 TYR C CE2 1 
ATOM   5842 C  CZ  . TYR C 1 193 ? 33.954  -1.016  -41.087 1.00 8.16  ? 193 TYR C CZ  1 
ATOM   5843 O  OH  . TYR C 1 193 ? 33.568  -0.416  -39.916 1.00 9.73  ? 193 TYR C OH  1 
ATOM   5844 N  N   . ARG C 1 194 ? 36.878  -0.336  -45.860 1.00 11.36 ? 194 ARG C N   1 
ATOM   5845 C  CA  . ARG C 1 194 ? 37.253  1.081   -45.684 1.00 12.41 ? 194 ARG C CA  1 
ATOM   5846 C  C   . ARG C 1 194 ? 36.183  1.800   -44.890 1.00 12.33 ? 194 ARG C C   1 
ATOM   5847 O  O   . ARG C 1 194 ? 35.006  1.762   -45.254 1.00 11.44 ? 194 ARG C O   1 
ATOM   5848 C  CB  . ARG C 1 194 ? 37.381  1.771   -47.065 1.00 15.55 ? 194 ARG C CB  1 
ATOM   5849 C  CG  . ARG C 1 194 ? 38.563  1.156   -47.787 1.00 21.90 ? 194 ARG C CG  1 
ATOM   5850 C  CD  . ARG C 1 194 ? 39.064  2.025   -48.931 1.00 32.62 ? 194 ARG C CD  1 
ATOM   5851 N  NE  . ARG C 1 194 ? 40.272  1.403   -49.504 1.00 43.19 ? 194 ARG C NE  1 
ATOM   5852 C  CZ  . ARG C 1 194 ? 41.535  1.703   -49.163 1.00 55.74 ? 194 ARG C CZ  1 
ATOM   5853 N  NH1 . ARG C 1 194 ? 41.819  2.652   -48.254 1.00 56.19 ? 194 ARG C NH1 1 
ATOM   5854 N  NH2 . ARG C 1 194 ? 42.540  1.045   -49.743 1.00 54.13 ? 194 ARG C NH2 1 
ATOM   5855 N  N   . GLY C 1 195 ? 36.567  2.353   -43.731 1.00 10.16 ? 195 GLY C N   1 
ATOM   5856 C  CA  . GLY C 1 195 ? 35.558  3.105   -42.927 1.00 10.35 ? 195 GLY C CA  1 
ATOM   5857 C  C   . GLY C 1 195 ? 36.089  4.323   -42.239 1.00 10.40 ? 195 GLY C C   1 
ATOM   5858 O  O   . GLY C 1 195 ? 36.961  5.003   -42.783 1.00 11.47 ? 195 GLY C O   1 
ATOM   5859 N  N   . SER C 1 196 ? 35.585  4.560   -41.023 1.00 9.80  ? 196 SER C N   1 
ATOM   5860 C  CA  . SER C 1 196 ? 35.931  5.811   -40.341 1.00 10.12 ? 196 SER C CA  1 
ATOM   5861 C  C   . SER C 1 196 ? 36.390  5.507   -38.926 1.00 9.14  ? 196 SER C C   1 
ATOM   5862 O  O   . SER C 1 196 ? 36.254  4.369   -38.373 1.00 9.02  ? 196 SER C O   1 
ATOM   5863 C  CB  . SER C 1 196 ? 34.703  6.727   -40.334 1.00 10.65 ? 196 SER C CB  1 
ATOM   5864 O  OG  . SER C 1 196 ? 33.711  6.261   -39.411 1.00 10.53 ? 196 SER C OG  1 
ATOM   5865 N  N   . LEU C 1 197 ? 36.873  6.557   -38.286 1.00 10.13 ? 197 LEU C N   1 
ATOM   5866 C  CA  . LEU C 1 197 ? 36.952  6.529   -36.842 1.00 10.74 ? 197 LEU C CA  1 
ATOM   5867 C  C   . LEU C 1 197 ? 35.493  6.373   -36.330 1.00 10.62 ? 197 LEU C C   1 
ATOM   5868 O  O   . LEU C 1 197 ? 34.563  6.891   -36.888 1.00 11.54 ? 197 LEU C O   1 
ATOM   5869 C  CB  . LEU C 1 197 ? 37.550  7.806   -36.237 1.00 12.36 ? 197 LEU C CB  1 
ATOM   5870 C  CG  . LEU C 1 197 ? 39.056  8.037   -36.362 1.00 13.46 ? 197 LEU C CG  1 
ATOM   5871 C  CD1 . LEU C 1 197 ? 39.284  8.596   -37.700 1.00 14.64 ? 197 LEU C CD1 1 
ATOM   5872 C  CD2 . LEU C 1 197 ? 39.344  9.239   -35.484 1.00 14.38 ? 197 LEU C CD2 1 
ATOM   5873 N  N   . THR C 1 198 ? 35.381  5.601   -35.240 1.00 10.59 ? 198 THR C N   1 
ATOM   5874 C  CA  . THR C 1 198 ? 34.039  5.429   -34.604 1.00 11.53 ? 198 THR C CA  1 
ATOM   5875 C  C   . THR C 1 198 ? 33.736  6.532   -33.589 1.00 13.21 ? 198 THR C C   1 
ATOM   5876 O  O   . THR C 1 198 ? 32.658  6.551   -32.924 1.00 12.23 ? 198 THR C O   1 
ATOM   5877 C  CB  . THR C 1 198 ? 33.857  4.070   -33.971 1.00 11.71 ? 198 THR C CB  1 
ATOM   5878 O  OG1 . THR C 1 198 ? 34.811  3.969   -32.910 1.00 11.90 ? 198 THR C OG1 1 
ATOM   5879 C  CG2 . THR C 1 198 ? 34.029  2.878   -34.922 1.00 10.64 ? 198 THR C CG2 1 
ATOM   5880 N  N   . THR C 1 199 ? 34.664  7.477   -33.429 1.00 12.35 ? 199 THR C N   1 
ATOM   5881 C  CA  . THR C 1 199 ? 34.540  8.592   -32.496 1.00 12.50 ? 199 THR C CA  1 
ATOM   5882 C  C   . THR C 1 199 ? 34.765  9.853   -33.248 1.00 12.29 ? 199 THR C C   1 
ATOM   5883 O  O   . THR C 1 199 ? 35.430  9.836   -34.259 1.00 12.60 ? 199 THR C O   1 
ATOM   5884 C  CB  . THR C 1 199 ? 35.677  8.412   -31.402 1.00 13.83 ? 199 THR C CB  1 
ATOM   5885 O  OG1 . THR C 1 199 ? 36.958  8.458   -32.043 1.00 14.68 ? 199 THR C OG1 1 
ATOM   5886 C  CG2 . THR C 1 199 ? 35.628  7.058   -30.672 1.00 15.19 ? 199 THR C CG2 1 
ATOM   5887 N  N   . PRO C 1 200 ? 34.295  10.994  -32.767 1.00 11.30 ? 200 PRO C N   1 
ATOM   5888 C  CA  . PRO C 1 200 ? 34.602  12.300  -33.380 1.00 12.39 ? 200 PRO C CA  1 
ATOM   5889 C  C   . PRO C 1 200 ? 36.164  12.386  -33.506 1.00 12.91 ? 200 PRO C C   1 
ATOM   5890 O  O   . PRO C 1 200 ? 36.875  11.850  -32.650 1.00 13.62 ? 200 PRO C O   1 
ATOM   5891 C  CB  . PRO C 1 200 ? 34.116  13.324  -32.316 1.00 12.34 ? 200 PRO C CB  1 
ATOM   5892 C  CG  . PRO C 1 200 ? 32.934  12.521  -31.714 1.00 10.16 ? 200 PRO C CG  1 
ATOM   5893 C  CD  . PRO C 1 200 ? 33.370  11.080  -31.588 1.00 10.41 ? 200 PRO C CD  1 
ATOM   5894 N  N   . PRO C 1 201 ? 36.633  12.982  -34.603 1.00 13.40 ? 201 PRO C N   1 
ATOM   5895 C  CA  . PRO C 1 201 ? 35.870  13.659  -35.654 1.00 12.45 ? 201 PRO C CA  1 
ATOM   5896 C  C   . PRO C 1 201 ? 35.297  12.766  -36.794 1.00 10.34 ? 201 PRO C C   1 
ATOM   5897 O  O   . PRO C 1 201 ? 34.746  13.315  -37.741 1.00 12.60 ? 201 PRO C O   1 
ATOM   5898 C  CB  . PRO C 1 201 ? 36.867  14.708  -36.234 1.00 14.49 ? 201 PRO C CB  1 
ATOM   5899 C  CG  . PRO C 1 201 ? 38.028  14.650  -35.297 1.00 13.70 ? 201 PRO C CG  1 
ATOM   5900 C  CD  . PRO C 1 201 ? 38.090  13.254  -34.746 1.00 13.83 ? 201 PRO C CD  1 
ATOM   5901 N  N   . CYS C 1 202 ? 35.367  11.448  -36.579 1.00 11.45 ? 202 CYS C N   1 
ATOM   5902 C  CA  . CYS C 1 202 ? 34.757  10.444  -37.492 1.00 11.26 ? 202 CYS C CA  1 
ATOM   5903 C  C   . CYS C 1 202 ? 35.345  10.467  -38.846 1.00 11.32 ? 202 CYS C C   1 
ATOM   5904 O  O   . CYS C 1 202 ? 34.604  10.175  -39.792 1.00 11.91 ? 202 CYS C O   1 
ATOM   5905 C  CB  . CYS C 1 202 ? 33.186  10.674  -37.626 1.00 12.97 ? 202 CYS C CB  1 
ATOM   5906 S  SG  . CYS C 1 202 ? 32.249  10.601  -36.011 1.00 12.09 ? 202 CYS C SG  1 
ATOM   5907 N  N   . ASN C 1 203 ? 36.633  10.851  -39.004 1.00 10.68 ? 203 ASN C N   1 
ATOM   5908 C  CA  . ASN C 1 203 ? 37.142  10.963  -40.342 1.00 11.70 ? 203 ASN C CA  1 
ATOM   5909 C  C   . ASN C 1 203 ? 37.094  9.616   -41.067 1.00 10.90 ? 203 ASN C C   1 
ATOM   5910 O  O   . ASN C 1 203 ? 37.346  8.586   -40.476 1.00 10.57 ? 203 ASN C O   1 
ATOM   5911 C  CB  . ASN C 1 203 ? 38.579  11.484  -40.308 1.00 13.16 ? 203 ASN C CB  1 
ATOM   5912 C  CG  . ASN C 1 203 ? 38.697  12.727  -39.432 1.00 13.47 ? 203 ASN C CG  1 
ATOM   5913 O  OD1 . ASN C 1 203 ? 38.750  12.581  -38.222 1.00 15.34 ? 203 ASN C OD1 1 
ATOM   5914 N  ND2 . ASN C 1 203 ? 38.590  13.908  -40.015 1.00 16.24 ? 203 ASN C ND2 1 
ATOM   5915 N  N   . PRO C 1 204 ? 36.804  9.671   -42.369 1.00 12.15 ? 204 PRO C N   1 
ATOM   5916 C  CA  . PRO C 1 204 ? 36.696  8.364   -43.159 1.00 13.41 ? 204 PRO C CA  1 
ATOM   5917 C  C   . PRO C 1 204 ? 38.055  7.968   -43.676 1.00 13.15 ? 204 PRO C C   1 
ATOM   5918 O  O   . PRO C 1 204 ? 38.234  7.795   -44.908 1.00 15.56 ? 204 PRO C O   1 
ATOM   5919 C  CB  . PRO C 1 204 ? 35.835  8.753   -44.319 1.00 13.38 ? 204 PRO C CB  1 
ATOM   5920 C  CG  . PRO C 1 204 ? 36.062  10.261  -44.552 1.00 13.09 ? 204 PRO C CG  1 
ATOM   5921 C  CD  . PRO C 1 204 ? 36.314  10.848  -43.130 1.00 13.71 ? 204 PRO C CD  1 
ATOM   5922 N  N   . THR C 1 205 ? 38.939  7.762   -42.758 1.00 12.01 ? 205 THR C N   1 
ATOM   5923 C  CA  . THR C 1 205 ? 40.360  7.570   -43.058 1.00 13.20 ? 205 THR C CA  1 
ATOM   5924 C  C   . THR C 1 205 ? 40.885  6.284   -42.450 1.00 12.66 ? 205 THR C C   1 
ATOM   5925 O  O   . THR C 1 205 ? 42.154  6.031   -42.387 1.00 13.47 ? 205 THR C O   1 
ATOM   5926 C  CB  . THR C 1 205 ? 41.139  8.717   -42.398 1.00 13.36 ? 205 THR C CB  1 
ATOM   5927 O  OG1 . THR C 1 205 ? 40.836  8.651   -40.974 1.00 14.97 ? 205 THR C OG1 1 
ATOM   5928 C  CG2 . THR C 1 205 ? 40.718  10.055  -43.039 1.00 15.89 ? 205 THR C CG2 1 
ATOM   5929 N  N   . VAL C 1 206 ? 39.987  5.343   -42.048 1.00 13.12 ? 206 VAL C N   1 
ATOM   5930 C  CA  . VAL C 1 206 ? 40.371  4.137   -41.410 1.00 11.89 ? 206 VAL C CA  1 
ATOM   5931 C  C   . VAL C 1 206 ? 40.209  2.835   -42.280 1.00 11.59 ? 206 VAL C C   1 
ATOM   5932 O  O   . VAL C 1 206 ? 39.110  2.533   -42.787 1.00 12.58 ? 206 VAL C O   1 
ATOM   5933 C  CB  . VAL C 1 206 ? 39.570  3.887   -40.090 1.00 10.21 ? 206 VAL C CB  1 
ATOM   5934 C  CG1 . VAL C 1 206 ? 39.968  2.560   -39.512 1.00 9.36  ? 206 VAL C CG1 1 
ATOM   5935 C  CG2 . VAL C 1 206 ? 39.747  5.012   -39.064 1.00 10.67 ? 206 VAL C CG2 1 
ATOM   5936 N  N   . LEU C 1 207 ? 41.303  2.126   -42.470 1.00 9.77  ? 207 LEU C N   1 
ATOM   5937 C  CA  . LEU C 1 207 ? 41.266  0.735   -43.011 1.00 10.23 ? 207 LEU C CA  1 
ATOM   5938 C  C   . LEU C 1 207 ? 41.015  -0.194  -41.849 1.00 9.55  ? 207 LEU C C   1 
ATOM   5939 O  O   . LEU C 1 207 ? 41.841  -0.365  -40.927 1.00 9.08  ? 207 LEU C O   1 
ATOM   5940 C  CB  . LEU C 1 207 ? 42.618  0.439   -43.723 1.00 12.17 ? 207 LEU C CB  1 
ATOM   5941 C  CG  . LEU C 1 207 ? 42.579  -0.900  -44.451 1.00 13.85 ? 207 LEU C CG  1 
ATOM   5942 C  CD1 . LEU C 1 207 ? 41.742  -0.807  -45.729 1.00 16.86 ? 207 LEU C CD1 1 
ATOM   5943 C  CD2 . LEU C 1 207 ? 44.009  -1.235  -44.925 1.00 18.60 ? 207 LEU C CD2 1 
ATOM   5944 N  N   . TRP C 1 208 ? 39.798  -0.788  -41.828 1.00 9.60  ? 208 TRP C N   1 
ATOM   5945 C  CA  . TRP C 1 208 ? 39.403  -1.737  -40.739 1.00 10.01 ? 208 TRP C CA  1 
ATOM   5946 C  C   . TRP C 1 208 ? 39.731  -3.136  -40.970 1.00 10.68 ? 208 TRP C C   1 
ATOM   5947 O  O   . TRP C 1 208 ? 39.537  -3.663  -42.090 1.00 10.83 ? 208 TRP C O   1 
ATOM   5948 C  CB  . TRP C 1 208 ? 37.865  -1.625  -40.544 1.00 10.10 ? 208 TRP C CB  1 
ATOM   5949 C  CG  . TRP C 1 208 ? 37.492  -0.410  -39.761 1.00 9.50  ? 208 TRP C CG  1 
ATOM   5950 C  CD1 . TRP C 1 208 ? 36.974  0.794   -40.199 1.00 10.43 ? 208 TRP C CD1 1 
ATOM   5951 C  CD2 . TRP C 1 208 ? 37.596  -0.277  -38.304 1.00 9.65  ? 208 TRP C CD2 1 
ATOM   5952 N  NE1 . TRP C 1 208 ? 36.825  1.687   -39.161 1.00 10.50 ? 208 TRP C NE1 1 
ATOM   5953 C  CE2 . TRP C 1 208 ? 37.166  1.089   -37.995 1.00 9.55  ? 208 TRP C CE2 1 
ATOM   5954 C  CE3 . TRP C 1 208 ? 38.006  -1.137  -37.231 1.00 11.01 ? 208 TRP C CE3 1 
ATOM   5955 C  CZ2 . TRP C 1 208 ? 37.159  1.580   -36.674 1.00 10.68 ? 208 TRP C CZ2 1 
ATOM   5956 C  CZ3 . TRP C 1 208 ? 37.967  -0.598  -35.901 1.00 10.15 ? 208 TRP C CZ3 1 
ATOM   5957 C  CH2 . TRP C 1 208 ? 37.567  0.697   -35.682 1.00 10.12 ? 208 TRP C CH2 1 
ATOM   5958 N  N   . THR C 1 209 ? 40.265  -3.795  -39.964 1.00 10.71 ? 209 THR C N   1 
ATOM   5959 C  CA  . THR C 1 209 ? 40.457  -5.252  -39.924 1.00 11.65 ? 209 THR C CA  1 
ATOM   5960 C  C   . THR C 1 209 ? 39.808  -5.743  -38.688 1.00 12.95 ? 209 THR C C   1 
ATOM   5961 O  O   . THR C 1 209 ? 40.280  -5.413  -37.594 1.00 14.36 ? 209 THR C O   1 
ATOM   5962 C  CB  . THR C 1 209 ? 41.952  -5.613  -39.918 1.00 13.19 ? 209 THR C CB  1 
ATOM   5963 O  OG1 . THR C 1 209 ? 42.557  -5.017  -41.117 1.00 12.04 ? 209 THR C OG1 1 
ATOM   5964 C  CG2 . THR C 1 209 ? 42.180  -7.088  -39.854 1.00 13.31 ? 209 THR C CG2 1 
ATOM   5965 N  N   . VAL C 1 210 ? 38.706  -6.464  -38.843 1.00 11.71 ? 210 VAL C N   1 
ATOM   5966 C  CA  . VAL C 1 210 ? 38.024  -7.048  -37.703 1.00 11.95 ? 210 VAL C CA  1 
ATOM   5967 C  C   . VAL C 1 210 ? 38.262  -8.548  -37.722 1.00 12.19 ? 210 VAL C C   1 
ATOM   5968 O  O   . VAL C 1 210 ? 37.959  -9.229  -38.670 1.00 12.65 ? 210 VAL C O   1 
ATOM   5969 C  CB  . VAL C 1 210 ? 36.486  -6.762  -37.759 1.00 10.99 ? 210 VAL C CB  1 
ATOM   5970 C  CG1 . VAL C 1 210 ? 35.828  -7.372  -36.508 1.00 11.98 ? 210 VAL C CG1 1 
ATOM   5971 C  CG2 . VAL C 1 210 ? 36.212  -5.279  -37.947 1.00 12.56 ? 210 VAL C CG2 1 
ATOM   5972 N  N   . PHE C 1 211 ? 38.895  -9.109  -36.692 1.00 13.03 ? 211 PHE C N   1 
ATOM   5973 C  CA  . PHE C 1 211 ? 39.188  -10.535 -36.793 1.00 13.38 ? 211 PHE C CA  1 
ATOM   5974 C  C   . PHE C 1 211 ? 37.897  -11.343 -36.686 1.00 14.77 ? 211 PHE C C   1 
ATOM   5975 O  O   . PHE C 1 211 ? 36.973  -10.928 -35.936 1.00 17.72 ? 211 PHE C O   1 
ATOM   5976 C  CB  . PHE C 1 211 ? 40.185  -10.930 -35.699 1.00 15.00 ? 211 PHE C CB  1 
ATOM   5977 C  CG  . PHE C 1 211 ? 41.517  -10.323 -35.941 1.00 15.36 ? 211 PHE C CG  1 
ATOM   5978 C  CD1 . PHE C 1 211 ? 42.335  -10.874 -36.933 1.00 17.05 ? 211 PHE C CD1 1 
ATOM   5979 C  CD2 . PHE C 1 211 ? 41.947  -9.235  -35.195 1.00 16.60 ? 211 PHE C CD2 1 
ATOM   5980 C  CE1 . PHE C 1 211 ? 43.589  -10.257 -37.213 1.00 15.99 ? 211 PHE C CE1 1 
ATOM   5981 C  CE2 . PHE C 1 211 ? 43.182  -8.633  -35.442 1.00 18.26 ? 211 PHE C CE2 1 
ATOM   5982 C  CZ  . PHE C 1 211 ? 43.960  -9.120  -36.487 1.00 16.42 ? 211 PHE C CZ  1 
ATOM   5983 N  N   . ARG C 1 212 ? 37.856  -12.485 -37.380 1.00 15.20 ? 212 ARG C N   1 
ATOM   5984 C  CA  . ARG C 1 212 ? 36.655  -13.293 -37.488 1.00 17.85 ? 212 ARG C CA  1 
ATOM   5985 C  C   . ARG C 1 212 ? 36.344  -13.887 -36.104 1.00 17.36 ? 212 ARG C C   1 
ATOM   5986 O  O   . ARG C 1 212 ? 35.203  -13.950 -35.696 1.00 19.70 ? 212 ARG C O   1 
ATOM   5987 C  CB  . ARG C 1 212 ? 36.848  -14.420 -38.496 1.00 18.88 ? 212 ARG C CB  1 
ATOM   5988 C  CG  . ARG C 1 212 ? 35.567  -15.257 -38.743 1.00 21.20 ? 212 ARG C CG  1 
ATOM   5989 C  CD  . ARG C 1 212 ? 35.825  -16.667 -39.235 1.00 29.24 ? 212 ARG C CD  1 
ATOM   5990 N  NE  . ARG C 1 212 ? 34.608  -17.177 -39.880 1.00 32.37 ? 212 ARG C NE  1 
ATOM   5991 C  CZ  . ARG C 1 212 ? 34.567  -18.073 -40.872 1.00 35.54 ? 212 ARG C CZ  1 
ATOM   5992 N  NH1 . ARG C 1 212 ? 35.684  -18.622 -41.348 1.00 37.70 ? 212 ARG C NH1 1 
ATOM   5993 N  NH2 . ARG C 1 212 ? 33.387  -18.413 -41.397 1.00 36.13 ? 212 ARG C NH2 1 
ATOM   5994 N  N   . ASN C 1 213 ? 37.369  -14.358 -35.399 1.00 16.97 ? 213 ASN C N   1 
ATOM   5995 C  CA  . ASN C 1 213 ? 37.201  -15.105 -34.149 1.00 17.69 ? 213 ASN C CA  1 
ATOM   5996 C  C   . ASN C 1 213 ? 37.354  -14.209 -32.911 1.00 19.09 ? 213 ASN C C   1 
ATOM   5997 O  O   . ASN C 1 213 ? 38.274  -13.374 -32.789 1.00 17.81 ? 213 ASN C O   1 
ATOM   5998 C  CB  . ASN C 1 213 ? 38.192  -16.306 -34.139 1.00 21.37 ? 213 ASN C CB  1 
ATOM   5999 C  CG  . ASN C 1 213 ? 38.128  -17.127 -35.429 1.00 23.88 ? 213 ASN C CG  1 
ATOM   6000 O  OD1 . ASN C 1 213 ? 39.172  -17.373 -36.076 1.00 28.63 ? 213 ASN C OD1 1 
ATOM   6001 N  ND2 . ASN C 1 213 ? 36.917  -17.535 -35.845 1.00 23.61 ? 213 ASN C ND2 1 
ATOM   6002 N  N   . PRO C 1 214 ? 36.418  -14.363 -31.942 1.00 17.27 ? 214 PRO C N   1 
ATOM   6003 C  CA  . PRO C 1 214 ? 36.378  -13.591 -30.752 1.00 17.71 ? 214 PRO C CA  1 
ATOM   6004 C  C   . PRO C 1 214 ? 37.438  -14.096 -29.721 1.00 18.85 ? 214 PRO C C   1 
ATOM   6005 O  O   . PRO C 1 214 ? 37.883  -15.242 -29.851 1.00 21.47 ? 214 PRO C O   1 
ATOM   6006 C  CB  . PRO C 1 214 ? 34.956  -13.877 -30.197 1.00 18.23 ? 214 PRO C CB  1 
ATOM   6007 C  CG  . PRO C 1 214 ? 34.635  -15.230 -30.718 1.00 19.92 ? 214 PRO C CG  1 
ATOM   6008 C  CD  . PRO C 1 214 ? 35.266  -15.267 -32.084 1.00 19.32 ? 214 PRO C CD  1 
ATOM   6009 N  N   . VAL C 1 215 ? 37.861  -13.225 -28.828 1.00 18.73 ? 215 VAL C N   1 
ATOM   6010 C  CA  . VAL C 1 215 ? 38.568  -13.713 -27.626 1.00 22.97 ? 215 VAL C CA  1 
ATOM   6011 C  C   . VAL C 1 215 ? 37.585  -13.853 -26.473 1.00 26.78 ? 215 VAL C C   1 
ATOM   6012 O  O   . VAL C 1 215 ? 36.462  -13.320 -26.505 1.00 22.71 ? 215 VAL C O   1 
ATOM   6013 C  CB  . VAL C 1 215 ? 39.709  -12.802 -27.180 1.00 21.97 ? 215 VAL C CB  1 
ATOM   6014 C  CG1 . VAL C 1 215 ? 40.779  -12.718 -28.283 1.00 23.63 ? 215 VAL C CG1 1 
ATOM   6015 C  CG2 . VAL C 1 215 ? 39.258  -11.416 -26.737 1.00 22.29 ? 215 VAL C CG2 1 
ATOM   6016 N  N   . GLN C 1 216 ? 38.049  -14.527 -25.427 1.00 28.05 ? 216 GLN C N   1 
ATOM   6017 C  CA  . GLN C 1 216 ? 37.334  -14.574 -24.147 1.00 31.30 ? 216 GLN C CA  1 
ATOM   6018 C  C   . GLN C 1 216 ? 37.955  -13.851 -22.918 1.00 31.45 ? 216 GLN C C   1 
ATOM   6019 O  O   . GLN C 1 216 ? 39.178  -13.769 -22.744 1.00 28.73 ? 216 GLN C O   1 
ATOM   6020 C  CB  . GLN C 1 216 ? 37.058  -16.006 -23.816 1.00 32.55 ? 216 GLN C CB  1 
ATOM   6021 C  CG  . GLN C 1 216 ? 36.389  -16.762 -24.921 1.00 38.81 ? 216 GLN C CG  1 
ATOM   6022 C  CD  . GLN C 1 216 ? 35.792  -18.040 -24.419 1.00 48.86 ? 216 GLN C CD  1 
ATOM   6023 O  OE1 . GLN C 1 216 ? 36.302  -18.671 -23.461 1.00 51.75 ? 216 GLN C OE1 1 
ATOM   6024 N  NE2 . GLN C 1 216 ? 34.695  -18.449 -25.051 1.00 51.67 ? 216 GLN C NE2 1 
ATOM   6025 N  N   . ILE C 1 217 ? 37.086  -13.316 -22.080 1.00 28.16 ? 217 ILE C N   1 
ATOM   6026 C  CA  . ILE C 1 217 ? 37.422  -12.711 -20.783 1.00 23.20 ? 217 ILE C CA  1 
ATOM   6027 C  C   . ILE C 1 217 ? 36.319  -13.261 -19.846 1.00 30.24 ? 217 ILE C C   1 
ATOM   6028 O  O   . ILE C 1 217 ? 35.145  -13.256 -20.203 1.00 27.50 ? 217 ILE C O   1 
ATOM   6029 C  CB  . ILE C 1 217 ? 37.593  -11.170 -20.752 1.00 26.75 ? 217 ILE C CB  1 
ATOM   6030 C  CG1 . ILE C 1 217 ? 36.280  -10.388 -20.912 1.00 19.12 ? 217 ILE C CG1 1 
ATOM   6031 C  CG2 . ILE C 1 217 ? 38.735  -10.713 -21.701 1.00 24.36 ? 217 ILE C CG2 1 
ATOM   6032 C  CD1 . ILE C 1 217 ? 36.389  -8.860  -20.766 1.00 22.59 ? 217 ILE C CD1 1 
ATOM   6033 N  N   . SER C 1 218 ? 36.681  -13.871 -18.717 1.00 30.44 ? 218 SER C N   1 
ATOM   6034 C  CA  . SER C 1 218 ? 35.629  -14.423 -17.852 1.00 30.63 ? 218 SER C CA  1 
ATOM   6035 C  C   . SER C 1 218 ? 34.567  -13.355 -17.467 1.00 30.16 ? 218 SER C C   1 
ATOM   6036 O  O   . SER C 1 218 ? 34.770  -12.128 -17.642 1.00 29.37 ? 218 SER C O   1 
ATOM   6037 C  CB  . SER C 1 218 ? 36.290  -15.088 -16.643 1.00 31.79 ? 218 SER C CB  1 
ATOM   6038 O  OG  . SER C 1 218 ? 36.893  -14.093 -15.854 1.00 26.67 ? 218 SER C OG  1 
ATOM   6039 N  N   . GLN C 1 219 ? 33.410  -13.787 -16.942 1.00 34.27 ? 219 GLN C N   1 
ATOM   6040 C  CA  . GLN C 1 219 ? 32.393  -12.801 -16.463 1.00 34.32 ? 219 GLN C CA  1 
ATOM   6041 C  C   . GLN C 1 219 ? 32.966  -11.867 -15.424 1.00 26.63 ? 219 GLN C C   1 
ATOM   6042 O  O   . GLN C 1 219 ? 32.659  -10.695 -15.318 1.00 24.51 ? 219 GLN C O   1 
ATOM   6043 C  CB  . GLN C 1 219 ? 31.098  -13.485 -15.946 1.00 37.72 ? 219 GLN C CB  1 
ATOM   6044 C  CG  . GLN C 1 219 ? 31.263  -14.645 -14.989 1.00 49.69 ? 219 GLN C CG  1 
ATOM   6045 C  CD  . GLN C 1 219 ? 30.879  -14.339 -13.531 1.00 57.65 ? 219 GLN C CD  1 
ATOM   6046 O  OE1 . GLN C 1 219 ? 30.664  -15.270 -12.740 1.00 59.11 ? 219 GLN C OE1 1 
ATOM   6047 N  NE2 . GLN C 1 219 ? 30.788  -13.048 -13.169 1.00 57.19 ? 219 GLN C NE2 1 
ATOM   6048 N  N   . GLU C 1 220 ? 33.864  -12.401 -14.629 1.00 32.90 ? 220 GLU C N   1 
ATOM   6049 C  CA  . GLU C 1 220 ? 34.531  -11.608 -13.627 1.00 31.45 ? 220 GLU C CA  1 
ATOM   6050 C  C   . GLU C 1 220 ? 35.338  -10.427 -14.245 1.00 27.99 ? 220 GLU C C   1 
ATOM   6051 O  O   . GLU C 1 220 ? 35.235  -9.288  -13.815 1.00 24.81 ? 220 GLU C O   1 
ATOM   6052 C  CB  . GLU C 1 220 ? 35.430  -12.556 -12.771 1.00 37.64 ? 220 GLU C CB  1 
ATOM   6053 C  CG  . GLU C 1 220 ? 34.755  -13.844 -12.250 1.00 43.54 ? 220 GLU C CG  1 
ATOM   6054 C  CD  . GLU C 1 220 ? 34.759  -15.061 -13.202 1.00 49.18 ? 220 GLU C CD  1 
ATOM   6055 O  OE1 . GLU C 1 220 ? 33.887  -15.155 -14.089 1.00 49.67 ? 220 GLU C OE1 1 
ATOM   6056 O  OE2 . GLU C 1 220 ? 35.605  -15.980 -13.033 1.00 53.73 ? 220 GLU C OE2 1 
ATOM   6057 N  N   . GLN C 1 221 ? 36.107  -10.698 -15.291 1.00 30.58 ? 221 GLN C N   1 
ATOM   6058 C  CA  . GLN C 1 221 ? 36.867  -9.618  -15.976 1.00 28.43 ? 221 GLN C CA  1 
ATOM   6059 C  C   . GLN C 1 221 ? 36.027  -8.527  -16.659 1.00 21.13 ? 221 GLN C C   1 
ATOM   6060 O  O   . GLN C 1 221 ? 36.257  -7.295  -16.509 1.00 23.56 ? 221 GLN C O   1 
ATOM   6061 C  CB  . GLN C 1 221 ? 37.762  -10.247 -17.002 1.00 28.58 ? 221 GLN C CB  1 
ATOM   6062 C  CG  . GLN C 1 221 ? 38.940  -10.957 -16.346 1.00 27.62 ? 221 GLN C CG  1 
ATOM   6063 C  CD  . GLN C 1 221 ? 39.862  -11.515 -17.371 1.00 26.90 ? 221 GLN C CD  1 
ATOM   6064 O  OE1 . GLN C 1 221 ? 39.570  -12.559 -17.988 1.00 24.77 ? 221 GLN C OE1 1 
ATOM   6065 N  NE2 . GLN C 1 221 ? 41.071  -10.898 -17.463 1.00 27.05 ? 221 GLN C NE2 1 
ATOM   6066 N  N   . LEU C 1 222 ? 34.980  -9.022  -17.324 1.00 25.20 ? 222 LEU C N   1 
ATOM   6067 C  CA  . LEU C 1 222 ? 34.027  -8.121  -17.965 1.00 23.23 ? 222 LEU C CA  1 
ATOM   6068 C  C   . LEU C 1 222 ? 33.291  -7.194  -17.034 1.00 19.94 ? 222 LEU C C   1 
ATOM   6069 O  O   . LEU C 1 222 ? 33.166  -5.957  -17.217 1.00 23.38 ? 222 LEU C O   1 
ATOM   6070 C  CB  . LEU C 1 222 ? 33.032  -8.949  -18.714 1.00 21.34 ? 222 LEU C CB  1 
ATOM   6071 C  CG  . LEU C 1 222 ? 32.007  -8.094  -19.453 1.00 22.07 ? 222 LEU C CG  1 
ATOM   6072 C  CD1 . LEU C 1 222 ? 32.619  -7.176  -20.496 1.00 21.68 ? 222 LEU C CD1 1 
ATOM   6073 C  CD2 . LEU C 1 222 ? 31.137  -9.115  -20.150 1.00 20.36 ? 222 LEU C CD2 1 
ATOM   6074 N  N   . LEU C 1 223 ? 32.797  -7.811  -15.924 1.00 24.69 ? 223 LEU C N   1 
ATOM   6075 C  CA  . LEU C 1 223 ? 32.257  -6.981  -14.871 1.00 23.55 ? 223 LEU C CA  1 
ATOM   6076 C  C   . LEU C 1 223 ? 33.172  -5.907  -14.338 1.00 21.94 ? 223 LEU C C   1 
ATOM   6077 O  O   . LEU C 1 223 ? 32.793  -4.792  -14.150 1.00 23.44 ? 223 LEU C O   1 
ATOM   6078 C  CB  . LEU C 1 223 ? 31.758  -7.858  -13.722 1.00 26.12 ? 223 LEU C CB  1 
ATOM   6079 C  CG  . LEU C 1 223 ? 30.663  -7.202  -12.876 1.00 28.73 ? 223 LEU C CG  1 
ATOM   6080 C  CD1 . LEU C 1 223 ? 29.361  -6.961  -13.594 1.00 27.16 ? 223 LEU C CD1 1 
ATOM   6081 C  CD2 . LEU C 1 223 ? 30.380  -8.152  -11.720 1.00 31.32 ? 223 LEU C CD2 1 
ATOM   6082 N  N   . ALA C 1 224 ? 34.428  -6.263  -14.127 1.00 24.97 ? 224 ALA C N   1 
ATOM   6083 C  CA  . ALA C 1 224 ? 35.470  -5.322  -13.690 1.00 27.30 ? 224 ALA C CA  1 
ATOM   6084 C  C   . ALA C 1 224 ? 35.595  -4.128  -14.671 1.00 20.60 ? 224 ALA C C   1 
ATOM   6085 O  O   . ALA C 1 224 ? 35.513  -2.959  -14.291 1.00 26.81 ? 224 ALA C O   1 
ATOM   6086 C  CB  . ALA C 1 224 ? 36.802  -6.109  -13.580 1.00 24.64 ? 224 ALA C CB  1 
ATOM   6087 N  N   . LEU C 1 225 ? 35.728  -4.454  -15.959 1.00 24.34 ? 225 LEU C N   1 
ATOM   6088 C  CA  . LEU C 1 225 ? 35.806  -3.471  -17.034 1.00 25.54 ? 225 LEU C CA  1 
ATOM   6089 C  C   . LEU C 1 225 ? 34.608  -2.556  -17.029 1.00 22.14 ? 225 LEU C C   1 
ATOM   6090 O  O   . LEU C 1 225 ? 34.690  -1.339  -17.061 1.00 20.34 ? 225 LEU C O   1 
ATOM   6091 C  CB  . LEU C 1 225 ? 35.891  -4.257  -18.371 1.00 22.55 ? 225 LEU C CB  1 
ATOM   6092 C  CG  . LEU C 1 225 ? 36.084  -3.366  -19.609 1.00 22.88 ? 225 LEU C CG  1 
ATOM   6093 C  CD1 . LEU C 1 225 ? 37.295  -2.464  -19.486 1.00 24.78 ? 225 LEU C CD1 1 
ATOM   6094 C  CD2 . LEU C 1 225 ? 36.156  -4.274  -20.850 1.00 23.02 ? 225 LEU C CD2 1 
ATOM   6095 N  N   . GLU C 1 226 ? 33.431  -3.152  -16.894 1.00 22.47 ? 226 GLU C N   1 
ATOM   6096 C  CA  . GLU C 1 226 ? 32.216  -2.317  -16.933 1.00 22.88 ? 226 GLU C CA  1 
ATOM   6097 C  C   . GLU C 1 226 ? 31.975  -1.456  -15.696 1.00 27.50 ? 226 GLU C C   1 
ATOM   6098 O  O   . GLU C 1 226 ? 31.198  -0.499  -15.743 1.00 24.34 ? 226 GLU C O   1 
ATOM   6099 C  CB  . GLU C 1 226 ? 30.986  -3.209  -17.106 1.00 24.53 ? 226 GLU C CB  1 
ATOM   6100 C  CG  . GLU C 1 226 ? 30.905  -3.999  -18.433 1.00 25.65 ? 226 GLU C CG  1 
ATOM   6101 C  CD  . GLU C 1 226 ? 29.915  -5.099  -18.340 1.00 26.28 ? 226 GLU C CD  1 
ATOM   6102 O  OE1 . GLU C 1 226 ? 29.514  -5.457  -17.190 1.00 27.86 ? 226 GLU C OE1 1 
ATOM   6103 O  OE2 . GLU C 1 226 ? 29.566  -5.691  -19.375 1.00 22.31 ? 226 GLU C OE2 1 
ATOM   6104 N  N   . THR C 1 227 ? 32.624  -1.797  -14.562 1.00 27.86 ? 227 THR C N   1 
ATOM   6105 C  CA  . THR C 1 227 ? 32.347  -1.101  -13.285 1.00 31.74 ? 227 THR C CA  1 
ATOM   6106 C  C   . THR C 1 227 ? 33.471  -0.203  -12.670 1.00 31.84 ? 227 THR C C   1 
ATOM   6107 O  O   . THR C 1 227 ? 33.229  0.503   -11.702 1.00 26.41 ? 227 THR C O   1 
ATOM   6108 C  CB  . THR C 1 227 ? 31.822  -2.075  -12.188 1.00 26.66 ? 227 THR C CB  1 
ATOM   6109 O  OG1 . THR C 1 227 ? 32.775  -3.115  -11.961 1.00 27.46 ? 227 THR C OG1 1 
ATOM   6110 C  CG2 . THR C 1 227 ? 30.445  -2.689  -12.560 1.00 30.17 ? 227 THR C CG2 1 
ATOM   6111 N  N   . ALA C 1 228 ? 34.670  -0.228  -13.253 1.00 30.13 ? 228 ALA C N   1 
ATOM   6112 C  CA  . ALA C 1 228 ? 35.842  0.469   -12.685 1.00 27.95 ? 228 ALA C CA  1 
ATOM   6113 C  C   . ALA C 1 228 ? 35.857  1.941   -12.920 1.00 31.79 ? 228 ALA C C   1 
ATOM   6114 O  O   . ALA C 1 228 ? 36.350  2.719   -12.087 1.00 29.01 ? 228 ALA C O   1 
ATOM   6115 C  CB  . ALA C 1 228 ? 37.097  -0.165  -13.227 1.00 31.75 ? 228 ALA C CB  1 
ATOM   6116 N  N   . LEU C 1 229 ? 35.364  2.386   -14.067 1.00 22.96 ? 229 LEU C N   1 
ATOM   6117 C  CA  . LEU C 1 229 ? 35.591  3.789   -14.404 1.00 23.73 ? 229 LEU C CA  1 
ATOM   6118 C  C   . LEU C 1 229 ? 34.503  4.762   -14.382 1.00 22.62 ? 229 LEU C C   1 
ATOM   6119 O  O   . LEU C 1 229 ? 33.337  4.443   -14.630 1.00 26.98 ? 229 LEU C O   1 
ATOM   6120 C  CB  . LEU C 1 229 ? 36.178  3.856   -15.817 1.00 22.69 ? 229 LEU C CB  1 
ATOM   6121 C  CG  . LEU C 1 229 ? 37.445  3.055   -16.019 1.00 20.58 ? 229 LEU C CG  1 
ATOM   6122 C  CD1 . LEU C 1 229 ? 38.019  3.417   -17.372 1.00 22.10 ? 229 LEU C CD1 1 
ATOM   6123 C  CD2 . LEU C 1 229 ? 38.542  3.346   -15.025 1.00 21.18 ? 229 LEU C CD2 1 
ATOM   6124 N  N   A TYR C 1 230 ? 34.802  5.942   -13.889 0.50 24.35 ? 230 TYR C N   1 
ATOM   6125 N  N   B TYR C 1 230 ? 34.903  6.017   -14.338 0.50 25.02 ? 230 TYR C N   1 
ATOM   6126 C  CA  A TYR C 1 230 ? 33.939  7.010   -14.118 0.50 22.80 ? 230 TYR C CA  1 
ATOM   6127 C  CA  B TYR C 1 230 ? 33.992  7.097   -14.431 0.50 25.74 ? 230 TYR C CA  1 
ATOM   6128 C  C   A TYR C 1 230 ? 34.507  7.515   -15.375 0.50 21.20 ? 230 TYR C C   1 
ATOM   6129 C  C   B TYR C 1 230 ? 34.411  8.106   -15.519 0.50 24.65 ? 230 TYR C C   1 
ATOM   6130 O  O   A TYR C 1 230 ? 35.639  7.102   -15.787 0.50 16.84 ? 230 TYR C O   1 
ATOM   6131 O  O   B TYR C 1 230 ? 35.608  8.310   -15.810 0.50 23.66 ? 230 TYR C O   1 
ATOM   6132 C  CB  A TYR C 1 230 ? 34.003  8.103   -13.043 0.50 24.17 ? 230 TYR C CB  1 
ATOM   6133 C  CB  B TYR C 1 230 ? 33.768  7.650   -13.009 0.50 29.10 ? 230 TYR C CB  1 
ATOM   6134 C  CG  A TYR C 1 230 ? 33.522  7.645   -11.694 0.50 24.42 ? 230 TYR C CG  1 
ATOM   6135 C  CG  B TYR C 1 230 ? 33.409  6.498   -12.069 0.50 30.12 ? 230 TYR C CG  1 
ATOM   6136 C  CD1 A TYR C 1 230 ? 32.168  7.510   -11.428 0.50 23.97 ? 230 TYR C CD1 1 
ATOM   6137 C  CD1 B TYR C 1 230 ? 32.093  6.275   -11.652 0.50 31.73 ? 230 TYR C CD1 1 
ATOM   6138 C  CD2 A TYR C 1 230 ? 34.431  7.311   -10.685 0.50 24.60 ? 230 TYR C CD2 1 
ATOM   6139 C  CD2 B TYR C 1 230 ? 34.374  5.602   -11.645 0.50 31.08 ? 230 TYR C CD2 1 
ATOM   6140 C  CE1 A TYR C 1 230 ? 31.733  7.055   -10.194 0.50 24.93 ? 230 TYR C CE1 1 
ATOM   6141 C  CE1 B TYR C 1 230 ? 31.777  5.209   -10.819 0.50 30.73 ? 230 TYR C CE1 1 
ATOM   6142 C  CE2 A TYR C 1 230 ? 33.998  6.887   -9.437  0.50 25.76 ? 230 TYR C CE2 1 
ATOM   6143 C  CE2 B TYR C 1 230 ? 34.060  4.532   -10.829 0.50 30.52 ? 230 TYR C CE2 1 
ATOM   6144 C  CZ  A TYR C 1 230 ? 32.643  6.784   -9.198  0.50 25.12 ? 230 TYR C CZ  1 
ATOM   6145 C  CZ  B TYR C 1 230 ? 32.766  4.346   -10.418 0.50 32.35 ? 230 TYR C CZ  1 
ATOM   6146 O  OH  A TYR C 1 230 ? 32.211  6.345   -7.957  0.50 27.53 ? 230 TYR C OH  1 
ATOM   6147 O  OH  B TYR C 1 230 ? 32.502  3.280   -9.596  0.50 35.31 ? 230 TYR C OH  1 
ATOM   6148 N  N   A CYS C 1 231 ? 33.683  8.369   -15.965 0.50 20.94 ? 231 CYS C N   1 
ATOM   6149 N  N   B CYS C 1 231 ? 33.428  8.676   -16.193 0.50 25.33 ? 231 CYS C N   1 
ATOM   6150 C  CA  A CYS C 1 231 ? 33.981  9.247   -17.053 0.50 23.44 ? 231 CYS C CA  1 
ATOM   6151 C  CA  B CYS C 1 231 ? 33.742  9.581   -17.273 0.50 25.88 ? 231 CYS C CA  1 
ATOM   6152 C  C   A CYS C 1 231 ? 34.329  10.675  -16.623 0.50 25.62 ? 231 CYS C C   1 
ATOM   6153 C  C   B CYS C 1 231 ? 33.814  11.004  -16.772 0.50 27.16 ? 231 CYS C C   1 
ATOM   6154 O  O   A CYS C 1 231 ? 35.032  11.331  -17.357 0.50 25.87 ? 231 CYS C O   1 
ATOM   6155 O  O   B CYS C 1 231 ? 33.880  11.985  -17.539 0.50 23.45 ? 231 CYS C O   1 
ATOM   6156 C  CB  A CYS C 1 231 ? 32.750  9.369   -17.944 0.50 22.71 ? 231 CYS C CB  1 
ATOM   6157 C  CB  B CYS C 1 231 ? 32.734  9.450   -18.409 0.50 26.28 ? 231 CYS C CB  1 
ATOM   6158 S  SG  A CYS C 1 231 ? 32.256  7.908   -18.884 0.50 22.87 ? 231 CYS C SG  1 
ATOM   6159 S  SG  B CYS C 1 231 ? 31.015  9.513   -17.894 0.50 24.26 ? 231 CYS C SG  1 
ATOM   6160 N  N   . THR C 1 232 ? 33.822  11.141  -15.456 1.00 27.89 ? 232 THR C N   1 
ATOM   6161 C  CA  . THR C 1 232 ? 33.803  12.531  -14.964 1.00 27.44 ? 232 THR C CA  1 
ATOM   6162 C  C   . THR C 1 232 ? 35.042  12.917  -14.130 1.00 28.94 ? 232 THR C C   1 
ATOM   6163 O  O   . THR C 1 232 ? 35.721  12.051  -13.661 1.00 21.34 ? 232 THR C O   1 
ATOM   6164 C  CB  . THR C 1 232 ? 32.567  12.745  -14.073 1.00 29.24 ? 232 THR C CB  1 
ATOM   6165 O  OG1 . THR C 1 232 ? 32.422  11.587  -13.223 1.00 27.02 ? 232 THR C OG1 1 
ATOM   6166 C  CG2 . THR C 1 232 ? 31.304  13.023  -14.939 1.00 28.38 ? 232 THR C CG2 1 
ATOM   6167 N  N   . HIS C 1 233 ? 35.261  14.214  -13.870 1.00 29.58 ? 233 HIS C N   1 
ATOM   6168 C  CA  . HIS C 1 233 ? 36.489  14.636  -13.140 1.00 36.41 ? 233 HIS C CA  1 
ATOM   6169 C  C   . HIS C 1 233 ? 36.417  14.280  -11.678 1.00 36.01 ? 233 HIS C C   1 
ATOM   6170 O  O   . HIS C 1 233 ? 35.316  14.123  -11.118 1.00 35.81 ? 233 HIS C O   1 
ATOM   6171 C  CB  . HIS C 1 233 ? 36.795  16.113  -13.386 1.00 39.51 ? 233 HIS C CB  1 
ATOM   6172 C  CG  . HIS C 1 233 ? 37.531  16.365  -14.691 1.00 44.42 ? 233 HIS C CG  1 
ATOM   6173 N  ND1 . HIS C 1 233 ? 36.911  16.848  -15.812 1.00 49.19 ? 233 HIS C ND1 1 
ATOM   6174 C  CD2 . HIS C 1 233 ? 38.882  16.185  -15.036 1.00 43.75 ? 233 HIS C CD2 1 
ATOM   6175 C  CE1 . HIS C 1 233 ? 37.825  16.973  -16.808 1.00 42.84 ? 233 HIS C CE1 1 
ATOM   6176 N  NE2 . HIS C 1 233 ? 39.025  16.570  -16.331 1.00 47.55 ? 233 HIS C NE2 1 
ATOM   6177 N  N   . MET C 1 234 ? 37.587  14.136  -11.067 1.00 43.53 ? 234 MET C N   1 
ATOM   6178 C  CA  . MET C 1 234 ? 37.805  13.477  -9.753  1.00 47.82 ? 234 MET C CA  1 
ATOM   6179 C  C   . MET C 1 234 ? 36.919  13.797  -8.555  1.00 52.33 ? 234 MET C C   1 
ATOM   6180 O  O   . MET C 1 234 ? 36.645  12.912  -7.716  1.00 52.91 ? 234 MET C O   1 
ATOM   6181 C  CB  . MET C 1 234 ? 39.261  13.624  -9.291  1.00 49.11 ? 234 MET C CB  1 
ATOM   6182 C  CG  . MET C 1 234 ? 39.689  12.421  -8.461  1.00 52.94 ? 234 MET C CG  1 
ATOM   6183 S  SD  . MET C 1 234 ? 40.766  12.725  -7.058  1.00 59.34 ? 234 MET C SD  1 
ATOM   6184 C  CE  . MET C 1 234 ? 41.252  11.016  -6.686  1.00 53.06 ? 234 MET C CE  1 
ATOM   6185 N  N   . ASP C 1 235 ? 36.522  15.054  -8.445  1.00 52.58 ? 235 ASP C N   1 
ATOM   6186 C  CA  . ASP C 1 235 ? 35.650  15.451  -7.373  1.00 56.57 ? 235 ASP C CA  1 
ATOM   6187 C  C   . ASP C 1 235 ? 34.364  16.101  -7.883  1.00 62.48 ? 235 ASP C C   1 
ATOM   6188 O  O   . ASP C 1 235 ? 33.669  16.772  -7.109  1.00 63.08 ? 235 ASP C O   1 
ATOM   6189 C  CB  . ASP C 1 235 ? 36.404  16.341  -6.362  1.00 68.70 ? 235 ASP C CB  1 
ATOM   6190 C  CG  . ASP C 1 235 ? 37.599  17.078  -6.989  1.00 73.82 ? 235 ASP C CG  1 
ATOM   6191 O  OD1 . ASP C 1 235 ? 37.391  18.040  -7.764  1.00 74.46 ? 235 ASP C OD1 1 
ATOM   6192 O  OD2 . ASP C 1 235 ? 38.753  16.697  -6.700  1.00 70.04 ? 235 ASP C OD2 1 
ATOM   6193 N  N   . ASP C 1 236 ? 34.038  15.894  -9.173  1.00 60.01 ? 236 ASP C N   1 
ATOM   6194 C  CA  . ASP C 1 236 ? 32.693  16.220  -9.722  1.00 53.37 ? 236 ASP C CA  1 
ATOM   6195 C  C   . ASP C 1 236 ? 31.653  15.780  -8.664  1.00 48.35 ? 236 ASP C C   1 
ATOM   6196 O  O   . ASP C 1 236 ? 31.616  14.606  -8.310  1.00 48.38 ? 236 ASP C O   1 
ATOM   6197 C  CB  . ASP C 1 236 ? 32.451  15.483  -11.074 1.00 48.28 ? 236 ASP C CB  1 
ATOM   6198 C  CG  . ASP C 1 236 ? 31.371  16.140  -11.947 1.00 48.53 ? 236 ASP C CG  1 
ATOM   6199 O  OD1 . ASP C 1 236 ? 30.498  16.888  -11.432 1.00 52.34 ? 236 ASP C OD1 1 
ATOM   6200 O  OD2 . ASP C 1 236 ? 31.385  15.919  -13.180 1.00 47.82 ? 236 ASP C OD2 1 
ATOM   6201 N  N   . PRO C 1 237 ? 30.839  16.716  -8.126  1.00 47.45 ? 237 PRO C N   1 
ATOM   6202 C  CA  . PRO C 1 237 ? 29.870  16.234  -7.112  1.00 47.15 ? 237 PRO C CA  1 
ATOM   6203 C  C   . PRO C 1 237 ? 28.770  15.303  -7.720  1.00 47.62 ? 237 PRO C C   1 
ATOM   6204 O  O   . PRO C 1 237 ? 27.966  14.731  -6.975  1.00 41.64 ? 237 PRO C O   1 
ATOM   6205 C  CB  . PRO C 1 237 ? 29.258  17.540  -6.569  1.00 45.65 ? 237 PRO C CB  1 
ATOM   6206 C  CG  . PRO C 1 237 ? 29.354  18.500  -7.709  1.00 45.21 ? 237 PRO C CG  1 
ATOM   6207 C  CD  . PRO C 1 237 ? 30.622  18.145  -8.456  1.00 44.18 ? 237 PRO C CD  1 
ATOM   6208 N  N   . SER C 1 238 ? 28.747  15.182  -9.056  1.00 45.60 ? 238 SER C N   1 
ATOM   6209 C  CA  . SER C 1 238 ? 27.776  14.353  -9.811  1.00 42.55 ? 238 SER C CA  1 
ATOM   6210 C  C   . SER C 1 238 ? 28.473  13.369  -10.778 1.00 40.46 ? 238 SER C C   1 
ATOM   6211 O  O   . SER C 1 238 ? 28.469  13.556  -12.002 1.00 38.82 ? 238 SER C O   1 
ATOM   6212 C  CB  . SER C 1 238 ? 26.799  15.241  -10.582 1.00 42.47 ? 238 SER C CB  1 
ATOM   6213 O  OG  . SER C 1 238 ? 25.803  15.792  -9.725  1.00 43.05 ? 238 SER C OG  1 
ATOM   6214 N  N   . PRO C 1 239 ? 29.078  12.315  -10.222 1.00 35.67 ? 239 PRO C N   1 
ATOM   6215 C  CA  . PRO C 1 239 ? 29.882  11.360  -10.963 1.00 34.04 ? 239 PRO C CA  1 
ATOM   6216 C  C   . PRO C 1 239 ? 29.072  10.471  -11.902 1.00 35.83 ? 239 PRO C C   1 
ATOM   6217 O  O   . PRO C 1 239 ? 27.859  10.236  -11.670 1.00 35.64 ? 239 PRO C O   1 
ATOM   6218 C  CB  . PRO C 1 239 ? 30.512  10.508  -9.863  1.00 33.06 ? 239 PRO C CB  1 
ATOM   6219 C  CG  . PRO C 1 239 ? 29.628  10.708  -8.667  1.00 32.39 ? 239 PRO C CG  1 
ATOM   6220 C  CD  . PRO C 1 239 ? 29.211  12.122  -8.763  1.00 35.46 ? 239 PRO C CD  1 
ATOM   6221 N  N   . ARG C 1 240 ? 29.725  9.971   -12.950 1.00 30.87 ? 240 ARG C N   1 
ATOM   6222 C  CA  . ARG C 1 240 ? 29.036  9.118   -13.938 1.00 29.49 ? 240 ARG C CA  1 
ATOM   6223 C  C   . ARG C 1 240 ? 29.875  7.921   -14.290 1.00 27.15 ? 240 ARG C C   1 
ATOM   6224 O  O   . ARG C 1 240 ? 31.074  8.075   -14.544 1.00 24.31 ? 240 ARG C O   1 
ATOM   6225 C  CB  . ARG C 1 240 ? 28.714  9.886   -15.207 1.00 33.03 ? 240 ARG C CB  1 
ATOM   6226 C  CG  . ARG C 1 240 ? 27.580  10.857  -15.153 1.00 38.62 ? 240 ARG C CG  1 
ATOM   6227 C  CD  . ARG C 1 240 ? 27.168  11.170  -16.608 1.00 48.93 ? 240 ARG C CD  1 
ATOM   6228 N  NE  . ARG C 1 240 ? 26.797  12.581  -16.781 1.00 52.11 ? 240 ARG C NE  1 
ATOM   6229 C  CZ  . ARG C 1 240 ? 27.668  13.598  -16.902 1.00 57.67 ? 240 ARG C CZ  1 
ATOM   6230 N  NH1 . ARG C 1 240 ? 28.983  13.382  -16.895 1.00 55.73 ? 240 ARG C NH1 1 
ATOM   6231 N  NH2 . ARG C 1 240 ? 27.221  14.843  -17.040 1.00 58.37 ? 240 ARG C NH2 1 
ATOM   6232 N  N   . GLU C 1 241 ? 29.257  6.736   -14.347 1.00 23.56 ? 241 GLU C N   1 
ATOM   6233 C  CA  . GLU C 1 241 ? 29.902  5.535   -14.724 1.00 23.78 ? 241 GLU C CA  1 
ATOM   6234 C  C   . GLU C 1 241 ? 30.270  5.691   -16.212 1.00 21.86 ? 241 GLU C C   1 
ATOM   6235 O  O   . GLU C 1 241 ? 29.551  6.338   -17.017 1.00 24.66 ? 241 GLU C O   1 
ATOM   6236 C  CB  . GLU C 1 241 ? 29.006  4.312   -14.523 1.00 30.20 ? 241 GLU C CB  1 
ATOM   6237 C  CG  . GLU C 1 241 ? 28.547  4.156   -13.097 1.00 36.11 ? 241 GLU C CG  1 
ATOM   6238 C  CD  . GLU C 1 241 ? 27.526  3.047   -12.936 1.00 42.94 ? 241 GLU C CD  1 
ATOM   6239 O  OE1 . GLU C 1 241 ? 26.634  2.913   -13.789 1.00 42.43 ? 241 GLU C OE1 1 
ATOM   6240 O  OE2 . GLU C 1 241 ? 27.601  2.304   -11.939 1.00 51.23 ? 241 GLU C OE2 1 
ATOM   6241 N  N   . MET C 1 242 ? 31.475  5.223   -16.495 1.00 21.07 ? 242 MET C N   1 
ATOM   6242 C  CA  . MET C 1 242 ? 31.925  5.083   -17.890 1.00 20.55 ? 242 MET C CA  1 
ATOM   6243 C  C   . MET C 1 242 ? 31.356  3.737   -18.361 1.00 16.87 ? 242 MET C C   1 
ATOM   6244 O  O   . MET C 1 242 ? 31.880  2.623   -18.105 1.00 16.33 ? 242 MET C O   1 
ATOM   6245 C  CB  . MET C 1 242 ? 33.451  5.127   -18.013 1.00 21.36 ? 242 MET C CB  1 
ATOM   6246 C  CG  . MET C 1 242 ? 33.842  5.066   -19.510 1.00 20.60 ? 242 MET C CG  1 
ATOM   6247 S  SD  . MET C 1 242 ? 35.639  4.911   -19.594 1.00 23.34 ? 242 MET C SD  1 
ATOM   6248 C  CE  . MET C 1 242 ? 36.151  6.538   -19.134 1.00 24.81 ? 242 MET C CE  1 
ATOM   6249 N  N   . ILE C 1 243 ? 30.218  3.820   -19.088 1.00 16.09 ? 243 ILE C N   1 
ATOM   6250 C  CA  . ILE C 1 243 ? 29.556  2.585   -19.605 1.00 16.83 ? 243 ILE C CA  1 
ATOM   6251 C  C   . ILE C 1 243 ? 28.979  2.932   -21.003 1.00 13.28 ? 243 ILE C C   1 
ATOM   6252 O  O   . ILE C 1 243 ? 28.915  4.074   -21.364 1.00 15.60 ? 243 ILE C O   1 
ATOM   6253 C  CB  . ILE C 1 243 ? 28.358  2.088   -18.691 1.00 15.48 ? 243 ILE C CB  1 
ATOM   6254 C  CG1 . ILE C 1 243 ? 27.461  3.244   -18.346 1.00 16.60 ? 243 ILE C CG1 1 
ATOM   6255 C  CG2 . ILE C 1 243 ? 28.895  1.308   -17.469 1.00 18.73 ? 243 ILE C CG2 1 
ATOM   6256 C  CD1 . ILE C 1 243 ? 26.288  2.755   -17.449 1.00 16.59 ? 243 ILE C CD1 1 
ATOM   6257 N  N   . ASN C 1 244 ? 28.718  1.893   -21.768 1.00 16.15 ? 244 ASN C N   1 
ATOM   6258 C  CA  . ASN C 1 244 ? 28.019  2.060   -23.091 1.00 16.33 ? 244 ASN C CA  1 
ATOM   6259 C  C   . ASN C 1 244 ? 28.807  2.973   -23.962 1.00 14.66 ? 244 ASN C C   1 
ATOM   6260 O  O   . ASN C 1 244 ? 28.319  3.880   -24.598 1.00 14.86 ? 244 ASN C O   1 
ATOM   6261 C  CB  . ASN C 1 244 ? 26.607  2.617   -22.871 1.00 15.75 ? 244 ASN C CB  1 
ATOM   6262 C  CG  . ASN C 1 244 ? 25.787  1.750   -21.952 1.00 16.30 ? 244 ASN C CG  1 
ATOM   6263 O  OD1 . ASN C 1 244 ? 25.841  0.506   -22.039 1.00 17.43 ? 244 ASN C OD1 1 
ATOM   6264 N  ND2 . ASN C 1 244 ? 25.048  2.429   -21.041 1.00 16.54 ? 244 ASN C ND2 1 
ATOM   6265 N  N   . ASN C 1 245 ? 30.118  2.760   -23.920 1.00 15.42 ? 245 ASN C N   1 
ATOM   6266 C  CA  . ASN C 1 245 ? 30.981  3.688   -24.668 1.00 14.32 ? 245 ASN C CA  1 
ATOM   6267 C  C   . ASN C 1 245 ? 31.316  3.144   -26.048 1.00 15.05 ? 245 ASN C C   1 
ATOM   6268 O  O   . ASN C 1 245 ? 32.485  2.795   -26.371 1.00 15.81 ? 245 ASN C O   1 
ATOM   6269 C  CB  . ASN C 1 245 ? 32.261  3.990   -23.822 1.00 16.31 ? 245 ASN C CB  1 
ATOM   6270 C  CG  . ASN C 1 245 ? 33.042  2.776   -23.472 1.00 16.39 ? 245 ASN C CG  1 
ATOM   6271 O  OD1 . ASN C 1 245 ? 32.609  1.619   -23.484 1.00 15.41 ? 245 ASN C OD1 1 
ATOM   6272 N  ND2 . ASN C 1 245 ? 34.339  3.029   -23.042 1.00 16.46 ? 245 ASN C ND2 1 
ATOM   6273 N  N   . PHE C 1 246 ? 30.251  3.015   -26.841 1.00 13.57 ? 246 PHE C N   1 
ATOM   6274 C  CA  . PHE C 1 246 ? 30.392  2.458   -28.193 1.00 13.01 ? 246 PHE C CA  1 
ATOM   6275 C  C   . PHE C 1 246 ? 29.407  3.209   -29.036 1.00 12.36 ? 246 PHE C C   1 
ATOM   6276 O  O   . PHE C 1 246 ? 28.399  3.780   -28.541 1.00 12.67 ? 246 PHE C O   1 
ATOM   6277 C  CB  . PHE C 1 246 ? 30.120  0.951   -28.284 1.00 13.65 ? 246 PHE C CB  1 
ATOM   6278 C  CG  . PHE C 1 246 ? 28.726  0.574   -27.901 1.00 14.85 ? 246 PHE C CG  1 
ATOM   6279 C  CD1 . PHE C 1 246 ? 27.728  0.483   -28.855 1.00 12.61 ? 246 PHE C CD1 1 
ATOM   6280 C  CD2 . PHE C 1 246 ? 28.407  0.295   -26.560 1.00 15.24 ? 246 PHE C CD2 1 
ATOM   6281 C  CE1 . PHE C 1 246 ? 26.396  0.189   -28.475 1.00 14.65 ? 246 PHE C CE1 1 
ATOM   6282 C  CE2 . PHE C 1 246 ? 27.088  -0.057  -26.160 1.00 15.59 ? 246 PHE C CE2 1 
ATOM   6283 C  CZ  . PHE C 1 246 ? 26.061  -0.093  -27.144 1.00 13.38 ? 246 PHE C CZ  1 
ATOM   6284 N  N   . ARG C 1 247 ? 29.708  3.307   -30.329 1.00 10.35 ? 247 ARG C N   1 
ATOM   6285 C  CA  . ARG C 1 247 ? 28.782  3.916   -31.303 1.00 10.73 ? 247 ARG C CA  1 
ATOM   6286 C  C   . ARG C 1 247 ? 27.812  2.897   -31.868 1.00 9.92  ? 247 ARG C C   1 
ATOM   6287 O  O   . ARG C 1 247 ? 28.198  1.747   -32.060 1.00 9.37  ? 247 ARG C O   1 
ATOM   6288 C  CB  . ARG C 1 247 ? 29.603  4.488   -32.476 1.00 11.37 ? 247 ARG C CB  1 
ATOM   6289 C  CG  . ARG C 1 247 ? 28.836  5.523   -33.271 1.00 8.47  ? 247 ARG C CG  1 
ATOM   6290 C  CD  . ARG C 1 247 ? 29.630  5.995   -34.497 1.00 8.50  ? 247 ARG C CD  1 
ATOM   6291 N  NE  . ARG C 1 247 ? 29.035  7.134   -35.149 1.00 9.36  ? 247 ARG C NE  1 
ATOM   6292 C  CZ  . ARG C 1 247 ? 29.498  7.688   -36.280 1.00 8.89  ? 247 ARG C CZ  1 
ATOM   6293 N  NH1 . ARG C 1 247 ? 30.524  7.103   -36.957 1.00 8.90  ? 247 ARG C NH1 1 
ATOM   6294 N  NH2 . ARG C 1 247 ? 28.887  8.800   -36.728 1.00 8.94  ? 247 ARG C NH2 1 
ATOM   6295 N  N   . GLN C 1 248 ? 26.563  3.342   -32.101 1.00 10.40 ? 248 GLN C N   1 
ATOM   6296 C  CA  . GLN C 1 248 ? 25.586  2.432   -32.762 1.00 9.77  ? 248 GLN C CA  1 
ATOM   6297 C  C   . GLN C 1 248 ? 26.067  2.131   -34.225 1.00 10.58 ? 248 GLN C C   1 
ATOM   6298 O  O   . GLN C 1 248 ? 26.833  2.933   -34.820 1.00 11.13 ? 248 GLN C O   1 
ATOM   6299 C  CB  . GLN C 1 248 ? 24.239  3.184   -32.894 1.00 10.66 ? 248 GLN C CB  1 
ATOM   6300 C  CG  . GLN C 1 248 ? 23.526  3.521   -31.561 1.00 10.30 ? 248 GLN C CG  1 
ATOM   6301 C  CD  . GLN C 1 248 ? 23.163  2.277   -30.784 1.00 11.41 ? 248 GLN C CD  1 
ATOM   6302 O  OE1 . GLN C 1 248 ? 23.898  1.805   -29.895 1.00 13.51 ? 248 GLN C OE1 1 
ATOM   6303 N  NE2 . GLN C 1 248 ? 22.015  1.673   -31.175 1.00 12.75 ? 248 GLN C NE2 1 
ATOM   6304 N  N   . VAL C 1 249 ? 25.637  0.992   -34.769 1.00 10.08 ? 249 VAL C N   1 
ATOM   6305 C  CA  . VAL C 1 249 ? 26.023  0.644   -36.164 1.00 10.25 ? 249 VAL C CA  1 
ATOM   6306 C  C   . VAL C 1 249 ? 25.420  1.625   -37.168 1.00 10.59 ? 249 VAL C C   1 
ATOM   6307 O  O   . VAL C 1 249 ? 24.291  2.207   -37.001 1.00 10.50 ? 249 VAL C O   1 
ATOM   6308 C  CB  . VAL C 1 249 ? 25.636  -0.786  -36.580 1.00 11.81 ? 249 VAL C CB  1 
ATOM   6309 C  CG1 . VAL C 1 249 ? 26.447  -1.816  -35.781 1.00 11.83 ? 249 VAL C CG1 1 
ATOM   6310 C  CG2 . VAL C 1 249 ? 24.113  -0.954  -36.510 1.00 12.89 ? 249 VAL C CG2 1 
ATOM   6311 N  N   . GLN C 1 250 ? 26.202  1.843   -38.233 1.00 10.04 ? 250 GLN C N   1 
ATOM   6312 C  CA  . GLN C 1 250 ? 25.805  2.847   -39.237 1.00 9.81  ? 250 GLN C CA  1 
ATOM   6313 C  C   . GLN C 1 250 ? 25.206  2.157   -40.444 1.00 11.19 ? 250 GLN C C   1 
ATOM   6314 O  O   . GLN C 1 250 ? 25.568  0.990   -40.711 1.00 11.59 ? 250 GLN C O   1 
ATOM   6315 C  CB  . GLN C 1 250 ? 27.072  3.550   -39.727 1.00 9.07  ? 250 GLN C CB  1 
ATOM   6316 C  CG  . GLN C 1 250 ? 27.895  4.146   -38.563 1.00 9.53  ? 250 GLN C CG  1 
ATOM   6317 C  CD  . GLN C 1 250 ? 27.187  5.305   -37.917 1.00 9.38  ? 250 GLN C CD  1 
ATOM   6318 O  OE1 . GLN C 1 250 ? 26.925  6.317   -38.567 1.00 10.42 ? 250 GLN C OE1 1 
ATOM   6319 N  NE2 . GLN C 1 250 ? 26.858  5.154   -36.633 1.00 10.11 ? 250 GLN C NE2 1 
ATOM   6320 N  N   . LYS C 1 251 ? 24.362  2.858   -41.201 1.00 9.43  ? 251 LYS C N   1 
ATOM   6321 C  CA  . LYS C 1 251 ? 23.927  2.212   -42.497 1.00 9.82  ? 251 LYS C CA  1 
ATOM   6322 C  C   . LYS C 1 251 ? 25.131  1.965   -43.417 1.00 10.70 ? 251 LYS C C   1 
ATOM   6323 O  O   . LYS C 1 251 ? 26.116  2.750   -43.409 1.00 11.51 ? 251 LYS C O   1 
ATOM   6324 C  CB  . LYS C 1 251 ? 22.955  3.120   -43.207 1.00 9.19  ? 251 LYS C CB  1 
ATOM   6325 C  CG  . LYS C 1 251 ? 21.607  3.186   -42.455 1.00 10.48 ? 251 LYS C CG  1 
ATOM   6326 C  CD  . LYS C 1 251 ? 20.587  4.048   -43.164 1.00 10.91 ? 251 LYS C CD  1 
ATOM   6327 C  CE  . LYS C 1 251 ? 19.136  3.748   -42.754 1.00 9.83  ? 251 LYS C CE  1 
ATOM   6328 N  NZ  . LYS C 1 251 ? 18.928  3.905   -41.274 1.00 9.21  ? 251 LYS C NZ  1 
ATOM   6329 N  N   . PHE C 1 252 ? 25.014  0.902   -44.240 1.00 12.53 ? 252 PHE C N   1 
ATOM   6330 C  CA  . PHE C 1 252 ? 26.130  0.474   -45.096 1.00 13.64 ? 252 PHE C CA  1 
ATOM   6331 C  C   . PHE C 1 252 ? 25.438  -0.143  -46.263 1.00 16.64 ? 252 PHE C C   1 
ATOM   6332 O  O   . PHE C 1 252 ? 25.110  -1.335  -46.225 1.00 19.37 ? 252 PHE C O   1 
ATOM   6333 C  CB  . PHE C 1 252 ? 26.903  -0.607  -44.383 1.00 14.31 ? 252 PHE C CB  1 
ATOM   6334 C  CG  . PHE C 1 252 ? 28.183  -1.021  -45.049 1.00 13.88 ? 252 PHE C CG  1 
ATOM   6335 C  CD1 . PHE C 1 252 ? 29.320  -0.252  -44.890 1.00 14.39 ? 252 PHE C CD1 1 
ATOM   6336 C  CD2 . PHE C 1 252 ? 28.259  -2.290  -45.686 1.00 17.35 ? 252 PHE C CD2 1 
ATOM   6337 C  CE1 . PHE C 1 252 ? 30.534  -0.676  -45.415 1.00 14.28 ? 252 PHE C CE1 1 
ATOM   6338 C  CE2 . PHE C 1 252 ? 29.488  -2.727  -46.231 1.00 15.72 ? 252 PHE C CE2 1 
ATOM   6339 C  CZ  . PHE C 1 252 ? 30.598  -1.921  -46.067 1.00 14.31 ? 252 PHE C CZ  1 
ATOM   6340 N  N   . ASP C 1 253 ? 25.098  0.645   -47.248 1.00 18.87 ? 253 ASP C N   1 
ATOM   6341 C  CA  . ASP C 1 253 ? 24.226  0.160   -48.321 1.00 19.50 ? 253 ASP C CA  1 
ATOM   6342 C  C   . ASP C 1 253 ? 25.002  0.084   -49.644 1.00 18.94 ? 253 ASP C C   1 
ATOM   6343 O  O   . ASP C 1 253 ? 25.847  0.932   -49.930 1.00 20.73 ? 253 ASP C O   1 
ATOM   6344 C  CB  . ASP C 1 253 ? 23.019  1.096   -48.343 1.00 21.62 ? 253 ASP C CB  1 
ATOM   6345 C  CG  . ASP C 1 253 ? 22.008  0.730   -49.351 1.00 23.17 ? 253 ASP C CG  1 
ATOM   6346 O  OD1 . ASP C 1 253 ? 21.494  -0.424  -49.311 1.00 25.30 ? 253 ASP C OD1 1 
ATOM   6347 O  OD2 . ASP C 1 253 ? 21.733  1.635   -50.166 1.00 22.73 ? 253 ASP C OD2 1 
ATOM   6348 N  N   A GLU C 1 254 ? 24.745  -0.950  -50.438 0.50 21.61 ? 254 GLU C N   1 
ATOM   6349 N  N   B GLU C 1 254 ? 24.737  -0.951  -50.443 0.50 18.94 ? 254 GLU C N   1 
ATOM   6350 C  CA  A GLU C 1 254 ? 25.400  -1.101  -51.741 0.50 23.11 ? 254 GLU C CA  1 
ATOM   6351 C  CA  B GLU C 1 254 ? 25.412  -1.076  -51.739 0.50 20.31 ? 254 GLU C CA  1 
ATOM   6352 C  C   A GLU C 1 254 ? 26.926  -1.260  -51.669 0.50 20.68 ? 254 GLU C C   1 
ATOM   6353 C  C   B GLU C 1 254 ? 26.945  -0.980  -51.569 0.50 18.45 ? 254 GLU C C   1 
ATOM   6354 O  O   A GLU C 1 254 ? 27.624  -1.070  -52.665 0.50 21.14 ? 254 GLU C O   1 
ATOM   6355 O  O   B GLU C 1 254 ? 27.652  -0.322  -52.372 0.50 16.50 ? 254 GLU C O   1 
ATOM   6356 C  CB  A GLU C 1 254 ? 25.043  0.074   -52.654 0.50 24.49 ? 254 GLU C CB  1 
ATOM   6357 C  CB  B GLU C 1 254 ? 24.930  0.015   -52.710 0.50 21.62 ? 254 GLU C CB  1 
ATOM   6358 C  CG  A GLU C 1 254 ? 23.604  0.064   -53.145 0.50 27.18 ? 254 GLU C CG  1 
ATOM   6359 C  CG  B GLU C 1 254 ? 23.416  0.066   -52.901 0.50 22.70 ? 254 GLU C CG  1 
ATOM   6360 C  CD  A GLU C 1 254 ? 23.394  0.956   -54.353 0.50 28.97 ? 254 GLU C CD  1 
ATOM   6361 C  CD  B GLU C 1 254 ? 22.898  -1.069  -53.746 0.50 23.44 ? 254 GLU C CD  1 
ATOM   6362 O  OE1 A GLU C 1 254 ? 24.023  0.698   -55.401 0.50 30.31 ? 254 GLU C OE1 1 
ATOM   6363 O  OE1 B GLU C 1 254 ? 23.622  -1.499  -54.663 0.50 29.61 ? 254 GLU C OE1 1 
ATOM   6364 O  OE2 A GLU C 1 254 ? 22.600  1.915   -54.255 0.50 32.01 ? 254 GLU C OE2 1 
ATOM   6365 O  OE2 B GLU C 1 254 ? 21.761  -1.506  -53.511 0.50 25.19 ? 254 GLU C OE2 1 
ATOM   6366 N  N   . ARG C 1 255 ? 27.430  -1.612  -50.491 1.00 17.17 ? 255 ARG C N   1 
ATOM   6367 C  CA  . ARG C 1 255 ? 28.870  -1.856  -50.269 1.00 17.84 ? 255 ARG C CA  1 
ATOM   6368 C  C   . ARG C 1 255 ? 29.145  -3.279  -49.799 1.00 16.81 ? 255 ARG C C   1 
ATOM   6369 O  O   . ARG C 1 255 ? 28.253  -4.017  -49.309 1.00 19.04 ? 255 ARG C O   1 
ATOM   6370 C  CB  . ARG C 1 255 ? 29.447  -0.913  -49.189 1.00 15.46 ? 255 ARG C CB  1 
ATOM   6371 C  CG  . ARG C 1 255 ? 29.257  0.542   -49.624 1.00 17.10 ? 255 ARG C CG  1 
ATOM   6372 C  CD  . ARG C 1 255 ? 29.992  1.516   -48.704 1.00 16.86 ? 255 ARG C CD  1 
ATOM   6373 N  NE  . ARG C 1 255 ? 31.368  1.071   -48.484 1.00 17.31 ? 255 ARG C NE  1 
ATOM   6374 C  CZ  . ARG C 1 255 ? 32.097  1.370   -47.411 1.00 17.86 ? 255 ARG C CZ  1 
ATOM   6375 N  NH1 . ARG C 1 255 ? 31.587  2.129   -46.453 1.00 17.64 ? 255 ARG C NH1 1 
ATOM   6376 N  NH2 . ARG C 1 255 ? 33.338  0.913   -47.299 1.00 13.44 ? 255 ARG C NH2 1 
ATOM   6377 N  N   . LEU C 1 256 ? 30.408  -3.665  -49.957 1.00 15.20 ? 256 LEU C N   1 
ATOM   6378 C  CA  . LEU C 1 256 ? 30.884  -5.026  -49.548 1.00 15.62 ? 256 LEU C CA  1 
ATOM   6379 C  C   . LEU C 1 256 ? 31.887  -4.936  -48.334 1.00 15.18 ? 256 LEU C C   1 
ATOM   6380 O  O   . LEU C 1 256 ? 32.566  -3.911  -48.161 1.00 15.87 ? 256 LEU C O   1 
ATOM   6381 C  CB  . LEU C 1 256 ? 31.572  -5.798  -50.720 1.00 17.24 ? 256 LEU C CB  1 
ATOM   6382 C  CG  . LEU C 1 256 ? 30.677  -6.027  -51.944 1.00 20.92 ? 256 LEU C CG  1 
ATOM   6383 C  CD1 . LEU C 1 256 ? 31.536  -6.419  -53.144 1.00 21.20 ? 256 LEU C CD1 1 
ATOM   6384 C  CD2 . LEU C 1 256 ? 29.728  -7.173  -51.604 1.00 23.47 ? 256 LEU C CD2 1 
ATOM   6385 N  N   . VAL C 1 257 ? 31.898  -6.026  -47.578 1.00 15.74 ? 257 VAL C N   1 
ATOM   6386 C  CA  . VAL C 1 257 ? 32.945  -6.280  -46.599 1.00 13.92 ? 257 VAL C CA  1 
ATOM   6387 C  C   . VAL C 1 257 ? 33.704  -7.450  -47.183 1.00 14.15 ? 257 VAL C C   1 
ATOM   6388 O  O   . VAL C 1 257 ? 33.122  -8.540  -47.471 1.00 14.61 ? 257 VAL C O   1 
ATOM   6389 C  CB  . VAL C 1 257 ? 32.392  -6.663  -45.240 1.00 14.14 ? 257 VAL C CB  1 
ATOM   6390 C  CG1 . VAL C 1 257 ? 33.504  -7.166  -44.348 1.00 15.55 ? 257 VAL C CG1 1 
ATOM   6391 C  CG2 . VAL C 1 257 ? 31.691  -5.446  -44.629 1.00 16.34 ? 257 VAL C CG2 1 
ATOM   6392 N  N   . TYR C 1 258 ? 34.997  -7.279  -47.361 1.00 13.37 ? 258 TYR C N   1 
ATOM   6393 C  CA  . TYR C 1 258 ? 35.846  -8.326  -47.962 1.00 14.17 ? 258 TYR C CA  1 
ATOM   6394 C  C   . TYR C 1 258 ? 36.382  -9.258  -46.847 1.00 14.12 ? 258 TYR C C   1 
ATOM   6395 O  O   . TYR C 1 258 ? 36.617  -8.856  -45.722 1.00 14.80 ? 258 TYR C O   1 
ATOM   6396 C  CB  . TYR C 1 258 ? 36.945  -7.678  -48.792 1.00 13.88 ? 258 TYR C CB  1 
ATOM   6397 C  CG  . TYR C 1 258 ? 36.362  -6.793  -49.816 1.00 17.14 ? 258 TYR C CG  1 
ATOM   6398 C  CD1 . TYR C 1 258 ? 35.904  -7.313  -51.030 1.00 18.32 ? 258 TYR C CD1 1 
ATOM   6399 C  CD2 . TYR C 1 258 ? 36.266  -5.421  -49.607 1.00 18.89 ? 258 TYR C CD2 1 
ATOM   6400 C  CE1 . TYR C 1 258 ? 35.306  -6.510  -51.996 1.00 21.30 ? 258 TYR C CE1 1 
ATOM   6401 C  CE2 . TYR C 1 258 ? 35.667  -4.601  -50.562 1.00 21.70 ? 258 TYR C CE2 1 
ATOM   6402 C  CZ  . TYR C 1 258 ? 35.244  -5.143  -51.782 1.00 24.27 ? 258 TYR C CZ  1 
ATOM   6403 O  OH  . TYR C 1 258 ? 34.662  -4.311  -52.736 1.00 24.67 ? 258 TYR C OH  1 
ATOM   6404 N  N   . THR C 1 259 ? 36.524  -10.544 -47.161 1.00 14.14 ? 259 THR C N   1 
ATOM   6405 C  CA  . THR C 1 259 ? 36.851  -11.457 -46.158 1.00 14.84 ? 259 THR C CA  1 
ATOM   6406 C  C   . THR C 1 259 ? 38.062  -12.238 -46.623 1.00 16.05 ? 259 THR C C   1 
ATOM   6407 O  O   . THR C 1 259 ? 38.182  -12.522 -47.814 1.00 17.78 ? 259 THR C O   1 
ATOM   6408 C  CB  . THR C 1 259 ? 35.727  -12.470 -45.817 1.00 17.04 ? 259 THR C CB  1 
ATOM   6409 O  OG1 . THR C 1 259 ? 35.294  -13.177 -46.991 1.00 17.20 ? 259 THR C OG1 1 
ATOM   6410 C  CG2 . THR C 1 259 ? 34.501  -11.690 -45.288 1.00 15.47 ? 259 THR C CG2 1 
ATOM   6411 N  N   . SER C 1 260 ? 38.936  -12.581 -45.680 1.00 15.78 ? 260 SER C N   1 
ATOM   6412 C  CA  . SER C 1 260 ? 40.128  -13.345 -46.075 1.00 16.41 ? 260 SER C CA  1 
ATOM   6413 C  C   . SER C 1 260 ? 39.750  -14.802 -46.096 1.00 19.41 ? 260 SER C C   1 
ATOM   6414 O  O   . SER C 1 260 ? 40.639  -15.640 -46.341 1.00 23.35 ? 260 SER C O   1 
ATOM   6415 C  CB  . SER C 1 260 ? 41.231  -13.095 -45.079 1.00 16.82 ? 260 SER C CB  1 
ATOM   6416 O  OG  . SER C 1 260 ? 40.831  -13.692 -43.870 1.00 15.55 ? 260 SER C OG  1 
ATOM   6417 N  N   . PHE C 1 261 ? 38.528  -15.149 -45.666 1.00 18.33 ? 261 PHE C N   1 
ATOM   6418 C  CA  . PHE C 1 261 ? 38.093  -16.567 -45.618 1.00 19.07 ? 261 PHE C CA  1 
ATOM   6419 C  C   . PHE C 1 261 ? 36.907  -16.753 -46.567 1.00 22.92 ? 261 PHE C C   1 
ATOM   6420 O  O   . PHE C 1 261 ? 36.184  -15.785 -46.893 1.00 23.23 ? 261 PHE C O   1 
ATOM   6421 C  CB  . PHE C 1 261 ? 37.674  -16.944 -44.169 1.00 17.68 ? 261 PHE C CB  1 
ATOM   6422 C  CG  . PHE C 1 261 ? 36.704  -15.972 -43.520 1.00 19.48 ? 261 PHE C CG  1 
ATOM   6423 C  CD1 . PHE C 1 261 ? 35.359  -16.202 -43.583 1.00 20.57 ? 261 PHE C CD1 1 
ATOM   6424 C  CD2 . PHE C 1 261 ? 37.150  -14.828 -42.881 1.00 18.97 ? 261 PHE C CD2 1 
ATOM   6425 C  CE1 . PHE C 1 261 ? 34.472  -15.326 -42.989 1.00 22.53 ? 261 PHE C CE1 1 
ATOM   6426 C  CE2 . PHE C 1 261 ? 36.286  -13.936 -42.291 1.00 19.00 ? 261 PHE C CE2 1 
ATOM   6427 C  CZ  . PHE C 1 261 ? 34.931  -14.186 -42.324 1.00 19.72 ? 261 PHE C CZ  1 
ATOM   6428 N  N   . SER C 1 262 ? 36.686  -17.991 -46.990 1.00 27.56 ? 262 SER C N   1 
ATOM   6429 C  CA  . SER C 1 262 ? 35.496  -18.356 -47.756 1.00 36.76 ? 262 SER C CA  1 
ATOM   6430 C  C   . SER C 1 262 ? 34.390  -19.056 -46.950 1.00 41.59 ? 262 SER C C   1 
ATOM   6431 O  O   . SER C 1 262 ? 34.640  -19.990 -46.190 1.00 41.67 ? 262 SER C O   1 
ATOM   6432 C  CB  . SER C 1 262 ? 35.905  -19.246 -48.909 1.00 38.13 ? 262 SER C CB  1 
ATOM   6433 O  OG  . SER C 1 262 ? 36.665  -18.493 -49.842 1.00 48.29 ? 262 SER C OG  1 
ATOM   6434 N  N   . LYS D 1 3   ? 16.115  20.016  -45.585 1.00 37.07 ? 3   LYS D N   1 
ATOM   6435 C  CA  . LYS D 1 3   ? 15.020  19.128  -46.076 1.00 33.56 ? 3   LYS D CA  1 
ATOM   6436 C  C   . LYS D 1 3   ? 15.424  17.702  -45.670 1.00 27.87 ? 3   LYS D C   1 
ATOM   6437 O  O   . LYS D 1 3   ? 16.144  17.050  -46.433 1.00 22.28 ? 3   LYS D O   1 
ATOM   6438 C  CB  . LYS D 1 3   ? 14.988  19.197  -47.597 1.00 39.81 ? 3   LYS D CB  1 
ATOM   6439 C  CG  . LYS D 1 3   ? 15.858  20.292  -48.243 1.00 46.57 ? 3   LYS D CG  1 
ATOM   6440 C  CD  . LYS D 1 3   ? 17.336  19.941  -48.415 1.00 43.84 ? 3   LYS D CD  1 
ATOM   6441 C  CE  . LYS D 1 3   ? 18.176  21.164  -48.075 1.00 43.69 ? 3   LYS D CE  1 
ATOM   6442 N  NZ  . LYS D 1 3   ? 19.403  20.765  -47.322 1.00 39.24 ? 3   LYS D NZ  1 
ATOM   6443 N  N   . TRP D 1 4   ? 14.977  17.214  -44.485 1.00 19.78 ? 4   TRP D N   1 
ATOM   6444 C  CA  . TRP D 1 4   ? 15.581  16.040  -43.957 1.00 17.06 ? 4   TRP D CA  1 
ATOM   6445 C  C   . TRP D 1 4   ? 15.298  14.842  -44.814 1.00 13.44 ? 4   TRP D C   1 
ATOM   6446 O  O   . TRP D 1 4   ? 14.273  14.768  -45.512 1.00 13.23 ? 4   TRP D O   1 
ATOM   6447 C  CB  . TRP D 1 4   ? 15.199  15.841  -42.497 1.00 15.74 ? 4   TRP D CB  1 
ATOM   6448 C  CG  . TRP D 1 4   ? 13.760  15.468  -42.278 1.00 13.44 ? 4   TRP D CG  1 
ATOM   6449 C  CD1 . TRP D 1 4   ? 12.688  16.282  -41.970 1.00 13.78 ? 4   TRP D CD1 1 
ATOM   6450 C  CD2 . TRP D 1 4   ? 13.212  14.094  -42.239 1.00 12.68 ? 4   TRP D CD2 1 
ATOM   6451 N  NE1 . TRP D 1 4   ? 11.546  15.544  -41.793 1.00 14.14 ? 4   TRP D NE1 1 
ATOM   6452 C  CE2 . TRP D 1 4   ? 11.785  14.224  -41.976 1.00 12.01 ? 4   TRP D CE2 1 
ATOM   6453 C  CE3 . TRP D 1 4   ? 13.764  12.831  -42.389 1.00 12.57 ? 4   TRP D CE3 1 
ATOM   6454 C  CZ2 . TRP D 1 4   ? 10.967  13.123  -41.788 1.00 10.84 ? 4   TRP D CZ2 1 
ATOM   6455 C  CZ3 . TRP D 1 4   ? 12.908  11.704  -42.276 1.00 11.57 ? 4   TRP D CZ3 1 
ATOM   6456 C  CH2 . TRP D 1 4   ? 11.554  11.842  -41.952 1.00 10.65 ? 4   TRP D CH2 1 
ATOM   6457 N  N   . THR D 1 5   ? 16.254  13.926  -44.801 1.00 12.93 ? 5   THR D N   1 
ATOM   6458 C  CA  . THR D 1 5   ? 16.204  12.649  -45.541 1.00 13.37 ? 5   THR D CA  1 
ATOM   6459 C  C   . THR D 1 5   ? 16.717  11.498  -44.718 1.00 12.78 ? 5   THR D C   1 
ATOM   6460 O  O   . THR D 1 5   ? 17.117  11.637  -43.529 1.00 11.18 ? 5   THR D O   1 
ATOM   6461 C  CB  . THR D 1 5   ? 17.051  12.652  -46.854 1.00 15.81 ? 5   THR D CB  1 
ATOM   6462 O  OG1 . THR D 1 5   ? 18.407  12.665  -46.408 1.00 14.50 ? 5   THR D OG1 1 
ATOM   6463 C  CG2 . THR D 1 5   ? 16.741  13.921  -47.634 1.00 15.77 ? 5   THR D CG2 1 
ATOM   6464 N  N   . TYR D 1 6   ? 16.727  10.287  -45.324 1.00 12.23 ? 6   TYR D N   1 
ATOM   6465 C  CA  . TYR D 1 6   ? 17.373  9.140   -44.761 1.00 12.31 ? 6   TYR D CA  1 
ATOM   6466 C  C   . TYR D 1 6   ? 18.711  8.748   -45.329 1.00 12.61 ? 6   TYR D C   1 
ATOM   6467 O  O   . TYR D 1 6   ? 19.248  7.680   -45.070 1.00 14.30 ? 6   TYR D O   1 
ATOM   6468 C  CB  . TYR D 1 6   ? 16.388  7.932   -44.873 1.00 11.45 ? 6   TYR D CB  1 
ATOM   6469 C  CG  . TYR D 1 6   ? 15.165  8.035   -44.014 1.00 9.71  ? 6   TYR D CG  1 
ATOM   6470 C  CD1 . TYR D 1 6   ? 15.179  7.513   -42.678 1.00 10.16 ? 6   TYR D CD1 1 
ATOM   6471 C  CD2 . TYR D 1 6   ? 13.972  8.491   -44.540 1.00 8.77  ? 6   TYR D CD2 1 
ATOM   6472 C  CE1 . TYR D 1 6   ? 14.014  7.494   -41.910 1.00 10.01 ? 6   TYR D CE1 1 
ATOM   6473 C  CE2 . TYR D 1 6   ? 12.796  8.524   -43.758 1.00 9.66  ? 6   TYR D CE2 1 
ATOM   6474 C  CZ  . TYR D 1 6   ? 12.853  8.022   -42.422 1.00 9.42  ? 6   TYR D CZ  1 
ATOM   6475 O  OH  . TYR D 1 6   ? 11.647  8.012   -41.744 1.00 9.58  ? 6   TYR D OH  1 
ATOM   6476 N  N   . PHE D 1 7   ? 19.236  9.551   -46.225 1.00 15.62 ? 7   PHE D N   1 
ATOM   6477 C  CA  . PHE D 1 7   ? 20.445  9.177   -46.954 1.00 16.80 ? 7   PHE D CA  1 
ATOM   6478 C  C   . PHE D 1 7   ? 21.212  10.437  -47.350 1.00 15.90 ? 7   PHE D C   1 
ATOM   6479 O  O   . PHE D 1 7   ? 20.661  11.301  -47.993 1.00 20.17 ? 7   PHE D O   1 
ATOM   6480 C  CB  . PHE D 1 7   ? 20.058  8.513   -48.274 1.00 20.26 ? 7   PHE D CB  1 
ATOM   6481 C  CG  . PHE D 1 7   ? 21.249  8.100   -49.086 1.00 27.95 ? 7   PHE D CG  1 
ATOM   6482 C  CD1 . PHE D 1 7   ? 22.138  7.149   -48.585 1.00 26.56 ? 7   PHE D CD1 1 
ATOM   6483 C  CD2 . PHE D 1 7   ? 21.505  8.680   -50.342 1.00 30.20 ? 7   PHE D CD2 1 
ATOM   6484 C  CE1 . PHE D 1 7   ? 23.264  6.752   -49.326 1.00 32.16 ? 7   PHE D CE1 1 
ATOM   6485 C  CE2 . PHE D 1 7   ? 22.622  8.298   -51.077 1.00 33.42 ? 7   PHE D CE2 1 
ATOM   6486 C  CZ  . PHE D 1 7   ? 23.502  7.331   -50.576 1.00 31.53 ? 7   PHE D CZ  1 
ATOM   6487 N  N   . GLY D 1 8   ? 22.499  10.530  -47.021 1.00 15.98 ? 8   GLY D N   1 
ATOM   6488 C  CA  . GLY D 1 8   ? 23.276  11.665  -47.591 1.00 18.25 ? 8   GLY D CA  1 
ATOM   6489 C  C   . GLY D 1 8   ? 23.516  12.675  -46.492 1.00 18.62 ? 8   GLY D C   1 
ATOM   6490 O  O   . GLY D 1 8   ? 23.338  12.399  -45.316 1.00 16.85 ? 8   GLY D O   1 
ATOM   6491 N  N   . PRO D 1 9   ? 23.870  13.907  -46.874 1.00 20.92 ? 9   PRO D N   1 
ATOM   6492 C  CA  . PRO D 1 9   ? 24.206  14.986  -45.930 1.00 21.60 ? 9   PRO D CA  1 
ATOM   6493 C  C   . PRO D 1 9   ? 23.120  15.406  -44.986 1.00 20.29 ? 9   PRO D C   1 
ATOM   6494 O  O   . PRO D 1 9   ? 23.410  15.968  -43.953 1.00 21.66 ? 9   PRO D O   1 
ATOM   6495 C  CB  . PRO D 1 9   ? 24.545  16.159  -46.874 1.00 21.74 ? 9   PRO D CB  1 
ATOM   6496 C  CG  . PRO D 1 9   ? 25.075  15.481  -48.085 1.00 23.86 ? 9   PRO D CG  1 
ATOM   6497 C  CD  . PRO D 1 9   ? 24.261  14.216  -48.265 1.00 23.26 ? 9   PRO D CD  1 
ATOM   6498 N  N   . ASP D 1 10  ? 21.843  15.112  -45.317 1.00 17.18 ? 10  ASP D N   1 
ATOM   6499 C  CA  . ASP D 1 10  ? 20.695  15.544  -44.504 1.00 17.97 ? 10  ASP D CA  1 
ATOM   6500 C  C   . ASP D 1 10  ? 20.085  14.319  -43.871 1.00 12.88 ? 10  ASP D C   1 
ATOM   6501 O  O   . ASP D 1 10  ? 18.978  14.399  -43.381 1.00 14.82 ? 10  ASP D O   1 
ATOM   6502 C  CB  . ASP D 1 10  ? 19.674  16.301  -45.368 1.00 18.20 ? 10  ASP D CB  1 
ATOM   6503 C  CG  . ASP D 1 10  ? 20.298  17.562  -46.019 1.00 23.74 ? 10  ASP D CG  1 
ATOM   6504 O  OD1 . ASP D 1 10  ? 20.977  18.303  -45.312 1.00 27.42 ? 10  ASP D OD1 1 
ATOM   6505 O  OD2 . ASP D 1 10  ? 20.125  17.747  -47.223 1.00 26.59 ? 10  ASP D OD2 1 
ATOM   6506 N  N   . GLY D 1 11  ? 20.854  13.248  -43.877 1.00 11.37 ? 11  GLY D N   1 
ATOM   6507 C  CA  . GLY D 1 11  ? 20.445  11.924  -43.265 1.00 10.03 ? 11  GLY D CA  1 
ATOM   6508 C  C   . GLY D 1 11  ? 20.499  11.945  -41.726 1.00 9.96  ? 11  GLY D C   1 
ATOM   6509 O  O   . GLY D 1 11  ? 20.658  13.018  -41.094 1.00 9.74  ? 11  GLY D O   1 
ATOM   6510 N  N   . GLU D 1 12  ? 20.224  10.829  -41.095 1.00 8.86  ? 12  GLU D N   1 
ATOM   6511 C  CA  . GLU D 1 12  ? 19.864  10.781  -39.714 1.00 8.85  ? 12  GLU D CA  1 
ATOM   6512 C  C   . GLU D 1 12  ? 20.924  11.229  -38.728 1.00 9.88  ? 12  GLU D C   1 
ATOM   6513 O  O   . GLU D 1 12  ? 20.576  11.658  -37.643 1.00 9.72  ? 12  GLU D O   1 
ATOM   6514 C  CB  . GLU D 1 12  ? 19.378  9.309   -39.354 1.00 9.28  ? 12  GLU D CB  1 
ATOM   6515 C  CG  . GLU D 1 12  ? 20.460  8.284   -39.227 1.00 9.72  ? 12  GLU D CG  1 
ATOM   6516 C  CD  . GLU D 1 12  ? 19.876  6.880   -39.257 1.00 10.10 ? 12  GLU D CD  1 
ATOM   6517 O  OE1 . GLU D 1 12  ? 19.541  6.411   -38.157 1.00 9.54  ? 12  GLU D OE1 1 
ATOM   6518 O  OE2 . GLU D 1 12  ? 19.787  6.352   -40.375 1.00 11.28 ? 12  GLU D OE2 1 
ATOM   6519 N  N   . ASN D 1 13  ? 22.216  11.083  -39.075 1.00 9.27  ? 13  ASN D N   1 
ATOM   6520 C  CA  . ASN D 1 13  ? 23.261  11.584  -38.203 1.00 9.37  ? 13  ASN D CA  1 
ATOM   6521 C  C   . ASN D 1 13  ? 23.331  13.117  -38.158 1.00 9.97  ? 13  ASN D C   1 
ATOM   6522 O  O   . ASN D 1 13  ? 23.939  13.637  -37.188 1.00 9.94  ? 13  ASN D O   1 
ATOM   6523 C  CB  . ASN D 1 13  ? 24.616  11.036  -38.615 1.00 10.18 ? 13  ASN D CB  1 
ATOM   6524 C  CG  . ASN D 1 13  ? 24.797  9.582   -38.242 1.00 11.47 ? 13  ASN D CG  1 
ATOM   6525 O  OD1 . ASN D 1 13  ? 23.900  8.916   -37.728 1.00 10.10 ? 13  ASN D OD1 1 
ATOM   6526 N  ND2 . ASN D 1 13  ? 25.978  9.053   -38.576 1.00 10.33 ? 13  ASN D ND2 1 
ATOM   6527 N  N   . SER D 1 14  ? 22.630  13.731  -39.094 1.00 8.92  ? 14  SER D N   1 
ATOM   6528 C  CA  . SER D 1 14  ? 22.596  15.215  -39.204 1.00 8.99  ? 14  SER D CA  1 
ATOM   6529 C  C   . SER D 1 14  ? 21.272  15.806  -38.714 1.00 9.88  ? 14  SER D C   1 
ATOM   6530 O  O   . SER D 1 14  ? 21.153  17.011  -38.690 1.00 10.28 ? 14  SER D O   1 
ATOM   6531 C  CB  . SER D 1 14  ? 22.877  15.705  -40.673 1.00 9.77  ? 14  SER D CB  1 
ATOM   6532 O  OG  . SER D 1 14  ? 24.204  15.368  -40.904 1.00 12.84 ? 14  SER D OG  1 
ATOM   6533 N  N   . TRP D 1 15  ? 20.238  15.019  -38.408 1.00 8.62  ? 15  TRP D N   1 
ATOM   6534 C  CA  . TRP D 1 15  ? 18.970  15.596  -38.042 1.00 9.81  ? 15  TRP D CA  1 
ATOM   6535 C  C   . TRP D 1 15  ? 19.045  16.517  -36.824 1.00 10.08 ? 15  TRP D C   1 
ATOM   6536 O  O   . TRP D 1 15  ? 18.324  17.543  -36.807 1.00 11.42 ? 15  TRP D O   1 
ATOM   6537 C  CB  . TRP D 1 15  ? 17.965  14.482  -37.655 1.00 10.50 ? 15  TRP D CB  1 
ATOM   6538 C  CG  . TRP D 1 15  ? 17.507  13.591  -38.820 1.00 10.24 ? 15  TRP D CG  1 
ATOM   6539 C  CD1 . TRP D 1 15  ? 17.730  13.743  -40.158 1.00 8.85  ? 15  TRP D CD1 1 
ATOM   6540 C  CD2 . TRP D 1 15  ? 16.737  12.349  -38.687 1.00 9.28  ? 15  TRP D CD2 1 
ATOM   6541 N  NE1 . TRP D 1 15  ? 17.142  12.714  -40.884 1.00 9.58  ? 15  TRP D NE1 1 
ATOM   6542 C  CE2 . TRP D 1 15  ? 16.519  11.859  -40.034 1.00 9.07  ? 15  TRP D CE2 1 
ATOM   6543 C  CE3 . TRP D 1 15  ? 16.184  11.666  -37.602 1.00 9.39  ? 15  TRP D CE3 1 
ATOM   6544 C  CZ2 . TRP D 1 15  ? 15.854  10.647  -40.284 1.00 10.04 ? 15  TRP D CZ2 1 
ATOM   6545 C  CZ3 . TRP D 1 15  ? 15.506  10.444  -37.833 1.00 9.09  ? 15  TRP D CZ3 1 
ATOM   6546 C  CH2 . TRP D 1 15  ? 15.289  9.987   -39.173 1.00 9.40  ? 15  TRP D CH2 1 
ATOM   6547 N  N   A SER D 1 16  ? 19.933  16.210  -35.885 0.50 9.97  ? 16  SER D N   1 
ATOM   6548 N  N   B SER D 1 16  ? 19.947  16.210  -35.891 0.50 10.94 ? 16  SER D N   1 
ATOM   6549 C  CA  A SER D 1 16  ? 19.999  16.987  -34.629 0.50 10.05 ? 16  SER D CA  1 
ATOM   6550 C  CA  B SER D 1 16  ? 20.047  16.972  -34.617 0.50 11.73 ? 16  SER D CA  1 
ATOM   6551 C  C   A SER D 1 16  ? 20.430  18.403  -34.926 0.50 10.02 ? 16  SER D C   1 
ATOM   6552 C  C   B SER D 1 16  ? 20.616  18.349  -34.835 0.50 10.99 ? 16  SER D C   1 
ATOM   6553 O  O   A SER D 1 16  ? 20.094  19.330  -34.148 0.50 9.83  ? 16  SER D O   1 
ATOM   6554 O  O   B SER D 1 16  ? 20.574  19.191  -33.909 0.50 11.00 ? 16  SER D O   1 
ATOM   6555 C  CB  A SER D 1 16  ? 21.006  16.353  -33.729 0.50 9.24  ? 16  SER D CB  1 
ATOM   6556 C  CB  B SER D 1 16  ? 20.922  16.227  -33.656 0.50 12.11 ? 16  SER D CB  1 
ATOM   6557 O  OG  A SER D 1 16  ? 22.293  16.456  -34.306 0.50 9.21  ? 16  SER D OG  1 
ATOM   6558 O  OG  B SER D 1 16  ? 20.475  14.894  -33.547 0.50 17.34 ? 16  SER D OG  1 
ATOM   6559 N  N   . LYS D 1 17  ? 21.147  18.565  -36.056 1.00 11.38 ? 17  LYS D N   1 
ATOM   6560 C  CA  . LYS D 1 17  ? 21.561  19.953  -36.466 1.00 12.30 ? 17  LYS D CA  1 
ATOM   6561 C  C   . LYS D 1 17  ? 20.385  20.947  -36.523 1.00 13.07 ? 17  LYS D C   1 
ATOM   6562 O  O   . LYS D 1 17  ? 20.532  22.149  -36.138 1.00 15.59 ? 17  LYS D O   1 
ATOM   6563 C  CB  . LYS D 1 17  ? 22.293  19.996  -37.797 1.00 11.42 ? 17  LYS D CB  1 
ATOM   6564 C  CG  . LYS D 1 17  ? 23.589  19.197  -37.753 1.00 11.76 ? 17  LYS D CG  1 
ATOM   6565 C  CD  . LYS D 1 17  ? 24.066  19.057  -39.210 1.00 11.47 ? 17  LYS D CD  1 
ATOM   6566 C  CE  . LYS D 1 17  ? 25.321  18.261  -39.316 1.00 12.32 ? 17  LYS D CE  1 
ATOM   6567 N  NZ  . LYS D 1 17  ? 25.917  18.451  -40.716 1.00 13.78 ? 17  LYS D NZ  1 
ATOM   6568 N  N   . LYS D 1 18  ? 19.232  20.514  -36.972 1.00 11.14 ? 18  LYS D N   1 
ATOM   6569 C  CA  . LYS D 1 18  ? 18.032  21.331  -37.029 1.00 12.78 ? 18  LYS D CA  1 
ATOM   6570 C  C   . LYS D 1 18  ? 16.944  20.963  -36.050 1.00 12.71 ? 18  LYS D C   1 
ATOM   6571 O  O   . LYS D 1 18  ? 15.984  21.776  -35.883 1.00 14.99 ? 18  LYS D O   1 
ATOM   6572 C  CB  . LYS D 1 18  ? 17.399  21.283  -38.412 1.00 13.49 ? 18  LYS D CB  1 
ATOM   6573 C  CG  . LYS D 1 18  ? 18.289  21.914  -39.553 1.00 18.17 ? 18  LYS D CG  1 
ATOM   6574 C  CD  . LYS D 1 18  ? 17.510  21.904  -40.879 1.00 19.44 ? 18  LYS D CD  1 
ATOM   6575 C  CE  . LYS D 1 18  ? 18.254  22.606  -42.023 1.00 23.21 ? 18  LYS D CE  1 
ATOM   6576 N  NZ  . LYS D 1 18  ? 17.924  22.017  -43.380 1.00 23.69 ? 18  LYS D NZ  1 
ATOM   6577 N  N   . TYR D 1 19  ? 17.054  19.766  -35.480 1.00 11.27 ? 19  TYR D N   1 
ATOM   6578 C  CA  . TYR D 1 19  ? 15.927  19.215  -34.662 1.00 11.00 ? 19  TYR D CA  1 
ATOM   6579 C  C   . TYR D 1 19  ? 16.577  18.684  -33.409 1.00 10.97 ? 19  TYR D C   1 
ATOM   6580 O  O   . TYR D 1 19  ? 16.987  17.530  -33.320 1.00 11.67 ? 19  TYR D O   1 
ATOM   6581 C  CB  . TYR D 1 19  ? 15.241  18.040  -35.440 1.00 11.73 ? 19  TYR D CB  1 
ATOM   6582 C  CG  . TYR D 1 19  ? 14.597  18.464  -36.713 1.00 10.26 ? 19  TYR D CG  1 
ATOM   6583 C  CD1 . TYR D 1 19  ? 13.395  19.195  -36.774 1.00 12.06 ? 19  TYR D CD1 1 
ATOM   6584 C  CD2 . TYR D 1 19  ? 15.264  18.210  -37.925 1.00 10.65 ? 19  TYR D CD2 1 
ATOM   6585 C  CE1 . TYR D 1 19  ? 12.831  19.571  -37.967 1.00 13.13 ? 19  TYR D CE1 1 
ATOM   6586 C  CE2 . TYR D 1 19  ? 14.715  18.587  -39.104 1.00 12.72 ? 19  TYR D CE2 1 
ATOM   6587 C  CZ  . TYR D 1 19  ? 13.517  19.297  -39.151 1.00 13.52 ? 19  TYR D CZ  1 
ATOM   6588 O  OH  . TYR D 1 19  ? 12.922  19.634  -40.381 1.00 17.12 ? 19  TYR D OH  1 
ATOM   6589 N  N   . PRO D 1 20  ? 16.781  19.542  -32.390 1.00 10.66 ? 20  PRO D N   1 
ATOM   6590 C  CA  . PRO D 1 20  ? 17.564  19.188  -31.199 1.00 12.10 ? 20  PRO D CA  1 
ATOM   6591 C  C   . PRO D 1 20  ? 17.071  17.907  -30.498 1.00 10.18 ? 20  PRO D C   1 
ATOM   6592 O  O   . PRO D 1 20  ? 17.869  17.222  -29.954 1.00 11.04 ? 20  PRO D O   1 
ATOM   6593 C  CB  . PRO D 1 20  ? 17.436  20.375  -30.253 1.00 13.16 ? 20  PRO D CB  1 
ATOM   6594 C  CG  . PRO D 1 20  ? 16.538  21.243  -30.936 1.00 12.86 ? 20  PRO D CG  1 
ATOM   6595 C  CD  . PRO D 1 20  ? 16.186  20.879  -32.336 1.00 11.81 ? 20  PRO D CD  1 
ATOM   6596 N  N   . SER D 1 21  ? 15.747  17.657  -30.489 1.00 11.32 ? 21  SER D N   1 
ATOM   6597 C  CA  . SER D 1 21  ? 15.275  16.440  -29.818 1.00 11.08 ? 21  SER D CA  1 
ATOM   6598 C  C   . SER D 1 21  ? 15.792  15.155  -30.466 1.00 10.19 ? 21  SER D C   1 
ATOM   6599 O  O   . SER D 1 21  ? 15.884  14.160  -29.770 1.00 11.71 ? 21  SER D O   1 
ATOM   6600 C  CB  . SER D 1 21  ? 13.742  16.322  -29.737 1.00 10.40 ? 21  SER D CB  1 
ATOM   6601 O  OG  . SER D 1 21  ? 13.310  17.338  -28.813 1.00 13.76 ? 21  SER D OG  1 
ATOM   6602 N  N   . CYS D 1 22  ? 16.236  15.214  -31.738 1.00 11.33 ? 22  CYS D N   1 
ATOM   6603 C  CA  . CYS D 1 22  ? 16.842  14.040  -32.367 1.00 11.76 ? 22  CYS D CA  1 
ATOM   6604 C  C   . CYS D 1 22  ? 18.180  13.647  -31.780 1.00 12.59 ? 22  CYS D C   1 
ATOM   6605 O  O   . CYS D 1 22  ? 18.677  12.529  -31.979 1.00 12.68 ? 22  CYS D O   1 
ATOM   6606 C  CB  . CYS D 1 22  ? 17.002  14.275  -33.856 1.00 12.57 ? 22  CYS D CB  1 
ATOM   6607 S  SG  . CYS D 1 22  ? 15.456  14.510  -34.708 1.00 11.51 ? 22  CYS D SG  1 
ATOM   6608 N  N   . GLY D 1 23  ? 18.754  14.561  -30.954 1.00 13.66 ? 23  GLY D N   1 
ATOM   6609 C  CA  . GLY D 1 23  ? 19.983  14.324  -30.220 1.00 13.88 ? 23  GLY D CA  1 
ATOM   6610 C  C   . GLY D 1 23  ? 19.779  14.222  -28.731 1.00 16.24 ? 23  GLY D C   1 
ATOM   6611 O  O   . GLY D 1 23  ? 20.743  14.209  -27.933 1.00 16.37 ? 23  GLY D O   1 
ATOM   6612 N  N   . GLY D 1 24  ? 18.511  14.155  -28.355 1.00 14.50 ? 24  GLY D N   1 
ATOM   6613 C  CA  . GLY D 1 24  ? 18.095  14.067  -26.951 1.00 17.23 ? 24  GLY D CA  1 
ATOM   6614 C  C   . GLY D 1 24  ? 17.880  12.685  -26.411 1.00 16.23 ? 24  GLY D C   1 
ATOM   6615 O  O   . GLY D 1 24  ? 18.266  11.685  -27.030 1.00 16.88 ? 24  GLY D O   1 
ATOM   6616 N  N   . LEU D 1 25  ? 17.285  12.591  -25.234 1.00 17.72 ? 25  LEU D N   1 
ATOM   6617 C  CA  . LEU D 1 25  ? 17.164  11.286  -24.687 1.00 17.27 ? 25  LEU D CA  1 
ATOM   6618 C  C   . LEU D 1 25  ? 15.820  10.657  -25.206 1.00 14.72 ? 25  LEU D C   1 
ATOM   6619 O  O   . LEU D 1 25  ? 15.022  11.277  -25.887 1.00 14.13 ? 25  LEU D O   1 
ATOM   6620 C  CB  . LEU D 1 25  ? 17.185  11.293  -23.131 1.00 22.67 ? 25  LEU D CB  1 
ATOM   6621 C  CG  . LEU D 1 25  ? 18.396  11.914  -22.411 1.00 22.41 ? 25  LEU D CG  1 
ATOM   6622 C  CD1 . LEU D 1 25  ? 17.948  12.231  -20.990 1.00 26.34 ? 25  LEU D CD1 1 
ATOM   6623 C  CD2 . LEU D 1 25  ? 19.479  10.841  -22.437 1.00 22.24 ? 25  LEU D CD2 1 
ATOM   6624 N  N   . LEU D 1 26  ? 15.680  9.387   -24.830 1.00 15.00 ? 26  LEU D N   1 
ATOM   6625 C  CA  . LEU D 1 26  ? 14.442  8.576   -25.011 1.00 13.73 ? 26  LEU D CA  1 
ATOM   6626 C  C   . LEU D 1 26  ? 14.102  8.411   -26.505 1.00 12.67 ? 26  LEU D C   1 
ATOM   6627 O  O   . LEU D 1 26  ? 12.912  8.491   -26.927 1.00 12.72 ? 26  LEU D O   1 
ATOM   6628 C  CB  . LEU D 1 26  ? 13.250  9.127   -24.258 1.00 18.45 ? 26  LEU D CB  1 
ATOM   6629 C  CG  . LEU D 1 26  ? 13.483  9.363   -22.755 1.00 23.37 ? 26  LEU D CG  1 
ATOM   6630 C  CD1 . LEU D 1 26  ? 12.166  9.875   -22.240 1.00 26.17 ? 26  LEU D CD1 1 
ATOM   6631 C  CD2 . LEU D 1 26  ? 13.936  8.117   -22.008 1.00 24.86 ? 26  LEU D CD2 1 
ATOM   6632 N  N   . GLN D 1 27  ? 15.147  8.226   -27.330 1.00 9.90  ? 27  GLN D N   1 
ATOM   6633 C  CA  . GLN D 1 27  ? 14.848  8.061   -28.773 1.00 9.58  ? 27  GLN D CA  1 
ATOM   6634 C  C   . GLN D 1 27  ? 14.435  6.668   -29.214 1.00 9.18  ? 27  GLN D C   1 
ATOM   6635 O  O   . GLN D 1 27  ? 14.806  5.603   -28.582 1.00 10.42 ? 27  GLN D O   1 
ATOM   6636 C  CB  . GLN D 1 27  ? 16.098  8.478   -29.590 1.00 10.15 ? 27  GLN D CB  1 
ATOM   6637 C  CG  . GLN D 1 27  ? 16.437  9.930   -29.270 1.00 10.30 ? 27  GLN D CG  1 
ATOM   6638 C  CD  . GLN D 1 27  ? 15.432  10.811  -29.968 1.00 9.14  ? 27  GLN D CD  1 
ATOM   6639 O  OE1 . GLN D 1 27  ? 15.438  10.995  -31.200 1.00 10.55 ? 27  GLN D OE1 1 
ATOM   6640 N  NE2 . GLN D 1 27  ? 14.511  11.403  -29.167 1.00 10.84 ? 27  GLN D NE2 1 
ATOM   6641 N  N   . SER D 1 28  ? 13.690  6.689   -30.312 1.00 9.22  ? 28  SER D N   1 
ATOM   6642 C  CA  . SER D 1 28  ? 13.240  5.451   -31.030 1.00 8.24  ? 28  SER D CA  1 
ATOM   6643 C  C   . SER D 1 28  ? 13.785  5.389   -32.437 1.00 8.54  ? 28  SER D C   1 
ATOM   6644 O  O   . SER D 1 28  ? 14.063  6.434   -33.015 1.00 9.07  ? 28  SER D O   1 
ATOM   6645 C  CB  . SER D 1 28  ? 11.704  5.446   -31.061 1.00 8.71  ? 28  SER D CB  1 
ATOM   6646 O  OG  . SER D 1 28  ? 11.235  5.281   -29.691 1.00 9.14  ? 28  SER D OG  1 
ATOM   6647 N  N   . PRO D 1 29  ? 13.845  4.207   -33.046 1.00 7.70  ? 29  PRO D N   1 
ATOM   6648 C  CA  . PRO D 1 29  ? 13.480  2.848   -32.524 1.00 8.31  ? 29  PRO D CA  1 
ATOM   6649 C  C   . PRO D 1 29  ? 14.585  2.247   -31.687 1.00 9.14  ? 29  PRO D C   1 
ATOM   6650 O  O   . PRO D 1 29  ? 15.643  2.863   -31.544 1.00 9.82  ? 29  PRO D O   1 
ATOM   6651 C  CB  . PRO D 1 29  ? 13.222  2.062   -33.851 1.00 8.95  ? 29  PRO D CB  1 
ATOM   6652 C  CG  . PRO D 1 29  ? 14.349  2.603   -34.748 1.00 7.84  ? 29  PRO D CG  1 
ATOM   6653 C  CD  . PRO D 1 29  ? 14.444  4.104   -34.410 1.00 8.21  ? 29  PRO D CD  1 
ATOM   6654 N  N   . ILE D 1 30  ? 14.325  1.026   -31.179 1.00 9.12  ? 30  ILE D N   1 
ATOM   6655 C  CA  . ILE D 1 30  ? 15.311  0.321   -30.397 1.00 9.17  ? 30  ILE D CA  1 
ATOM   6656 C  C   . ILE D 1 30  ? 15.292  -1.170  -30.768 1.00 8.68  ? 30  ILE D C   1 
ATOM   6657 O  O   . ILE D 1 30  ? 14.356  -1.618  -31.525 1.00 9.56  ? 30  ILE D O   1 
ATOM   6658 C  CB  . ILE D 1 30  ? 15.051  0.448   -28.895 1.00 10.07 ? 30  ILE D CB  1 
ATOM   6659 C  CG1 . ILE D 1 30  ? 13.589  0.052   -28.582 1.00 11.43 ? 30  ILE D CG1 1 
ATOM   6660 C  CG2 . ILE D 1 30  ? 15.278  1.910   -28.442 1.00 10.38 ? 30  ILE D CG2 1 
ATOM   6661 C  CD1 . ILE D 1 30  ? 13.373  -0.042  -27.061 1.00 14.33 ? 30  ILE D CD1 1 
ATOM   6662 N  N   . ASP D 1 31  ? 16.345  -1.878  -30.321 1.00 9.08  ? 31  ASP D N   1 
ATOM   6663 C  CA  . ASP D 1 31  ? 16.456  -3.332  -30.530 1.00 10.11 ? 31  ASP D CA  1 
ATOM   6664 C  C   . ASP D 1 31  ? 15.826  -4.012  -29.337 1.00 12.81 ? 31  ASP D C   1 
ATOM   6665 O  O   . ASP D 1 31  ? 16.249  -3.785  -28.215 1.00 12.96 ? 31  ASP D O   1 
ATOM   6666 C  CB  . ASP D 1 31  ? 17.908  -3.720  -30.708 1.00 13.37 ? 31  ASP D CB  1 
ATOM   6667 C  CG  . ASP D 1 31  ? 18.051  -5.207  -30.754 1.00 14.65 ? 31  ASP D CG  1 
ATOM   6668 O  OD1 . ASP D 1 31  ? 17.446  -5.778  -31.676 1.00 12.62 ? 31  ASP D OD1 1 
ATOM   6669 O  OD2 . ASP D 1 31  ? 18.674  -5.873  -29.880 1.00 18.09 ? 31  ASP D OD2 1 
ATOM   6670 N  N   . LEU D 1 32  ? 14.847  -4.855  -29.579 1.00 11.62 ? 32  LEU D N   1 
ATOM   6671 C  CA  . LEU D 1 32  ? 14.120  -5.574  -28.519 1.00 11.59 ? 32  LEU D CA  1 
ATOM   6672 C  C   . LEU D 1 32  ? 14.876  -6.871  -28.263 1.00 13.55 ? 32  LEU D C   1 
ATOM   6673 O  O   . LEU D 1 32  ? 14.879  -7.760  -29.119 1.00 14.37 ? 32  LEU D O   1 
ATOM   6674 C  CB  . LEU D 1 32  ? 12.651  -5.842  -28.973 1.00 11.09 ? 32  LEU D CB  1 
ATOM   6675 C  CG  . LEU D 1 32  ? 11.911  -4.511  -29.323 1.00 11.63 ? 32  LEU D CG  1 
ATOM   6676 C  CD1 . LEU D 1 32  ? 10.618  -4.911  -30.070 1.00 12.02 ? 32  LEU D CD1 1 
ATOM   6677 C  CD2 . LEU D 1 32  ? 11.630  -3.606  -28.102 1.00 13.01 ? 32  LEU D CD2 1 
ATOM   6678 N  N   . HIS D 1 33  ? 15.582  -6.991  -27.117 1.00 13.77 ? 33  HIS D N   1 
ATOM   6679 C  CA  . HIS D 1 33  ? 16.331  -8.200  -26.879 1.00 14.31 ? 33  HIS D CA  1 
ATOM   6680 C  C   . HIS D 1 33  ? 16.303  -8.531  -25.393 1.00 14.20 ? 33  HIS D C   1 
ATOM   6681 O  O   . HIS D 1 33  ? 15.992  -7.652  -24.575 1.00 16.27 ? 33  HIS D O   1 
ATOM   6682 C  CB  . HIS D 1 33  ? 17.762  -8.062  -27.452 1.00 14.48 ? 33  HIS D CB  1 
ATOM   6683 C  CG  . HIS D 1 33  ? 18.582  -7.042  -26.722 1.00 13.96 ? 33  HIS D CG  1 
ATOM   6684 N  ND1 . HIS D 1 33  ? 18.514  -5.703  -26.990 1.00 15.54 ? 33  HIS D ND1 1 
ATOM   6685 C  CD2 . HIS D 1 33  ? 19.442  -7.187  -25.650 1.00 14.81 ? 33  HIS D CD2 1 
ATOM   6686 C  CE1 . HIS D 1 33  ? 19.322  -5.034  -26.118 1.00 18.49 ? 33  HIS D CE1 1 
ATOM   6687 N  NE2 . HIS D 1 33  ? 19.879  -5.934  -25.310 1.00 15.85 ? 33  HIS D NE2 1 
ATOM   6688 N  N   . SER D 1 34  ? 16.556  -9.810  -25.073 1.00 14.62 ? 34  SER D N   1 
ATOM   6689 C  CA  . SER D 1 34  ? 16.186  -10.357 -23.706 1.00 16.20 ? 34  SER D CA  1 
ATOM   6690 C  C   . SER D 1 34  ? 16.704  -9.536  -22.543 1.00 16.86 ? 34  SER D C   1 
ATOM   6691 O  O   . SER D 1 34  ? 15.959  -9.324  -21.563 1.00 15.51 ? 34  SER D O   1 
ATOM   6692 C  CB  . SER D 1 34  ? 16.684  -11.806 -23.570 1.00 19.56 ? 34  SER D CB  1 
ATOM   6693 O  OG  . SER D 1 34  ? 18.093  -11.823 -23.785 1.00 23.36 ? 34  SER D OG  1 
ATOM   6694 N  N   . ASP D 1 35  ? 17.946  -9.038  -22.589 1.00 14.84 ? 35  ASP D N   1 
ATOM   6695 C  CA  . ASP D 1 35  ? 18.511  -8.492  -21.389 1.00 15.63 ? 35  ASP D CA  1 
ATOM   6696 C  C   . ASP D 1 35  ? 17.744  -7.276  -20.941 1.00 14.40 ? 35  ASP D C   1 
ATOM   6697 O  O   . ASP D 1 35  ? 17.814  -6.894  -19.744 1.00 17.11 ? 35  ASP D O   1 
ATOM   6698 C  CB  . ASP D 1 35  ? 19.993  -7.990  -21.632 1.00 18.12 ? 35  ASP D CB  1 
ATOM   6699 C  CG  . ASP D 1 35  ? 20.850  -9.001  -22.313 1.00 21.19 ? 35  ASP D CG  1 
ATOM   6700 O  OD1 . ASP D 1 35  ? 21.836  -9.451  -21.628 1.00 19.60 ? 35  ASP D OD1 1 
ATOM   6701 O  OD2 . ASP D 1 35  ? 20.565  -9.305  -23.516 1.00 21.31 ? 35  ASP D OD2 1 
ATOM   6702 N  N   . ILE D 1 36  ? 16.992  -6.635  -21.851 1.00 13.99 ? 36  ILE D N   1 
ATOM   6703 C  CA  . ILE D 1 36  ? 16.307  -5.371  -21.485 1.00 13.49 ? 36  ILE D CA  1 
ATOM   6704 C  C   . ILE D 1 36  ? 14.789  -5.481  -21.349 1.00 13.02 ? 36  ILE D C   1 
ATOM   6705 O  O   . ILE D 1 36  ? 14.106  -4.461  -21.152 1.00 14.78 ? 36  ILE D O   1 
ATOM   6706 C  CB  . ILE D 1 36  ? 16.754  -4.124  -22.302 1.00 17.01 ? 36  ILE D CB  1 
ATOM   6707 C  CG1 . ILE D 1 36  ? 16.600  -4.368  -23.796 1.00 18.18 ? 36  ILE D CG1 1 
ATOM   6708 C  CG2 . ILE D 1 36  ? 18.231  -3.852  -21.978 1.00 17.55 ? 36  ILE D CG2 1 
ATOM   6709 C  CD1 . ILE D 1 36  ? 15.190  -4.531  -24.307 1.00 18.87 ? 36  ILE D CD1 1 
ATOM   6710 N  N   . LEU D 1 37  ? 14.305  -6.721  -21.465 1.00 12.43 ? 37  LEU D N   1 
ATOM   6711 C  CA  . LEU D 1 37  ? 12.803  -6.980  -21.388 1.00 14.00 ? 37  LEU D CA  1 
ATOM   6712 C  C   . LEU D 1 37  ? 12.422  -7.282  -19.937 1.00 16.33 ? 37  LEU D C   1 
ATOM   6713 O  O   . LEU D 1 37  ? 13.183  -8.003  -19.243 1.00 16.27 ? 37  LEU D O   1 
ATOM   6714 C  CB  . LEU D 1 37  ? 12.478  -8.172  -22.221 1.00 14.55 ? 37  LEU D CB  1 
ATOM   6715 C  CG  . LEU D 1 37  ? 12.699  -8.054  -23.735 1.00 15.86 ? 37  LEU D CG  1 
ATOM   6716 C  CD1 . LEU D 1 37  ? 12.356  -9.384  -24.363 1.00 16.26 ? 37  LEU D CD1 1 
ATOM   6717 C  CD2 . LEU D 1 37  ? 12.019  -6.872  -24.422 1.00 16.06 ? 37  LEU D CD2 1 
ATOM   6718 N  N   . GLN D 1 38  ? 11.263  -6.749  -19.503 1.00 13.36 ? 38  GLN D N   1 
ATOM   6719 C  CA  . GLN D 1 38  ? 10.776  -7.176  -18.181 1.00 13.68 ? 38  GLN D CA  1 
ATOM   6720 C  C   . GLN D 1 38  ? 9.260   -7.327  -18.207 1.00 12.93 ? 38  GLN D C   1 
ATOM   6721 O  O   . GLN D 1 38  ? 8.564   -6.422  -18.674 1.00 13.87 ? 38  GLN D O   1 
ATOM   6722 C  CB  . GLN D 1 38  ? 11.109  -6.135  -17.224 1.00 16.91 ? 38  GLN D CB  1 
ATOM   6723 C  CG  . GLN D 1 38  ? 10.748  -6.616  -15.846 1.00 20.83 ? 38  GLN D CG  1 
ATOM   6724 C  CD  . GLN D 1 38  ? 11.384  -5.760  -14.844 1.00 22.04 ? 38  GLN D CD  1 
ATOM   6725 O  OE1 . GLN D 1 38  ? 12.563  -5.926  -14.581 1.00 27.27 ? 38  GLN D OE1 1 
ATOM   6726 N  NE2 . GLN D 1 38  ? 10.663  -4.765  -14.367 1.00 26.16 ? 38  GLN D NE2 1 
ATOM   6727 N  N   . TYR D 1 39  ? 8.752   -8.475  -17.755 1.00 12.49 ? 39  TYR D N   1 
ATOM   6728 C  CA  . TYR D 1 39  ? 7.333   -8.696  -17.754 1.00 11.54 ? 39  TYR D CA  1 
ATOM   6729 C  C   . TYR D 1 39  ? 6.653   -7.723  -16.786 1.00 11.89 ? 39  TYR D C   1 
ATOM   6730 O  O   . TYR D 1 39  ? 7.196   -7.416  -15.691 1.00 12.75 ? 39  TYR D O   1 
ATOM   6731 C  CB  . TYR D 1 39  ? 7.105   -10.125 -17.264 1.00 13.06 ? 39  TYR D CB  1 
ATOM   6732 C  CG  . TYR D 1 39  ? 5.638   -10.407 -17.010 1.00 12.59 ? 39  TYR D CG  1 
ATOM   6733 C  CD1 . TYR D 1 39  ? 4.683   -10.374 -18.067 1.00 13.94 ? 39  TYR D CD1 1 
ATOM   6734 C  CD2 . TYR D 1 39  ? 5.193   -10.633 -15.708 1.00 13.39 ? 39  TYR D CD2 1 
ATOM   6735 C  CE1 . TYR D 1 39  ? 3.327   -10.552 -17.843 1.00 14.58 ? 39  TYR D CE1 1 
ATOM   6736 C  CE2 . TYR D 1 39  ? 3.822   -10.865 -15.491 1.00 13.06 ? 39  TYR D CE2 1 
ATOM   6737 C  CZ  . TYR D 1 39  ? 2.932   -10.840 -16.506 1.00 14.08 ? 39  TYR D CZ  1 
ATOM   6738 O  OH  . TYR D 1 39  ? 1.558   -11.056 -16.264 1.00 17.62 ? 39  TYR D OH  1 
ATOM   6739 N  N   . ASP D 1 40  ? 5.488   -7.208  -17.210 1.00 11.81 ? 40  ASP D N   1 
ATOM   6740 C  CA  . ASP D 1 40  ? 4.745   -6.243  -16.392 1.00 12.11 ? 40  ASP D CA  1 
ATOM   6741 C  C   . ASP D 1 40  ? 3.305   -6.693  -16.461 1.00 11.69 ? 40  ASP D C   1 
ATOM   6742 O  O   . ASP D 1 40  ? 2.643   -6.525  -17.497 1.00 12.28 ? 40  ASP D O   1 
ATOM   6743 C  CB  . ASP D 1 40  ? 4.944   -4.849  -17.019 1.00 14.18 ? 40  ASP D CB  1 
ATOM   6744 C  CG  . ASP D 1 40  ? 4.303   -3.717  -16.201 1.00 18.60 ? 40  ASP D CG  1 
ATOM   6745 O  OD1 . ASP D 1 40  ? 3.510   -3.965  -15.252 1.00 15.14 ? 40  ASP D OD1 1 
ATOM   6746 O  OD2 . ASP D 1 40  ? 4.494   -2.523  -16.596 1.00 19.56 ? 40  ASP D OD2 1 
ATOM   6747 N  N   . ALA D 1 41  ? 2.759   -7.160  -15.299 1.00 10.88 ? 41  ALA D N   1 
ATOM   6748 C  CA  . ALA D 1 41  ? 1.360   -7.569  -15.238 1.00 12.27 ? 41  ALA D CA  1 
ATOM   6749 C  C   . ALA D 1 41  ? 0.341   -6.414  -15.383 1.00 12.69 ? 41  ALA D C   1 
ATOM   6750 O  O   . ALA D 1 41  ? -0.840  -6.630  -15.633 1.00 13.47 ? 41  ALA D O   1 
ATOM   6751 C  CB  . ALA D 1 41  ? 1.158   -8.251  -13.899 1.00 11.63 ? 41  ALA D CB  1 
ATOM   6752 N  N   . SER D 1 42  ? 0.804   -5.170  -15.383 1.00 12.69 ? 42  SER D N   1 
ATOM   6753 C  CA  . SER D 1 42  ? -0.057  -4.011  -15.546 1.00 14.40 ? 42  SER D CA  1 
ATOM   6754 C  C   . SER D 1 42  ? -0.399  -3.749  -17.007 1.00 15.82 ? 42  SER D C   1 
ATOM   6755 O  O   . SER D 1 42  ? -1.339  -2.957  -17.261 1.00 17.02 ? 42  SER D O   1 
ATOM   6756 C  CB  . SER D 1 42  ? 0.506   -2.759  -14.808 1.00 16.15 ? 42  SER D CB  1 
ATOM   6757 O  OG  . SER D 1 42  ? 1.506   -2.113  -15.609 1.00 18.89 ? 42  SER D OG  1 
ATOM   6758 N  N   . LEU D 1 43  ? 0.311   -4.454  -17.941 1.00 14.90 ? 43  LEU D N   1 
ATOM   6759 C  CA  . LEU D 1 43  ? 0.085   -4.290  -19.379 1.00 15.89 ? 43  LEU D CA  1 
ATOM   6760 C  C   . LEU D 1 43  ? -1.059  -5.206  -19.819 1.00 15.63 ? 43  LEU D C   1 
ATOM   6761 O  O   . LEU D 1 43  ? -0.905  -6.331  -20.332 1.00 15.06 ? 43  LEU D O   1 
ATOM   6762 C  CB  . LEU D 1 43  ? 1.376   -4.619  -20.135 1.00 14.74 ? 43  LEU D CB  1 
ATOM   6763 C  CG  . LEU D 1 43  ? 2.533   -3.712  -19.806 1.00 17.18 ? 43  LEU D CG  1 
ATOM   6764 C  CD1 . LEU D 1 43  ? 3.712   -4.229  -20.657 1.00 15.14 ? 43  LEU D CD1 1 
ATOM   6765 C  CD2 . LEU D 1 43  ? 2.285   -2.240  -20.017 1.00 21.45 ? 43  LEU D CD2 1 
ATOM   6766 N  N   . THR D 1 44  ? -2.275  -4.645  -19.719 1.00 16.82 ? 44  THR D N   1 
ATOM   6767 C  CA  . THR D 1 44  ? -3.464  -5.432  -20.041 1.00 15.72 ? 44  THR D CA  1 
ATOM   6768 C  C   . THR D 1 44  ? -3.830  -5.236  -21.545 1.00 14.68 ? 44  THR D C   1 
ATOM   6769 O  O   . THR D 1 44  ? -3.277  -4.373  -22.215 1.00 13.96 ? 44  THR D O   1 
ATOM   6770 C  CB  . THR D 1 44  ? -4.659  -4.945  -19.158 1.00 15.33 ? 44  THR D CB  1 
ATOM   6771 O  OG1 . THR D 1 44  ? -4.738  -3.553  -19.328 1.00 18.91 ? 44  THR D OG1 1 
ATOM   6772 C  CG2 . THR D 1 44  ? -4.326  -5.146  -17.666 1.00 20.79 ? 44  THR D CG2 1 
ATOM   6773 N  N   . PRO D 1 45  ? -4.861  -5.922  -22.045 1.00 15.97 ? 45  PRO D N   1 
ATOM   6774 C  CA  . PRO D 1 45  ? -4.961  -5.833  -23.503 1.00 14.39 ? 45  PRO D CA  1 
ATOM   6775 C  C   . PRO D 1 45  ? -5.550  -4.533  -24.036 1.00 14.92 ? 45  PRO D C   1 
ATOM   6776 O  O   . PRO D 1 45  ? -6.459  -3.982  -23.406 1.00 17.57 ? 45  PRO D O   1 
ATOM   6777 C  CB  . PRO D 1 45  ? -5.829  -7.065  -23.883 1.00 17.11 ? 45  PRO D CB  1 
ATOM   6778 C  CG  . PRO D 1 45  ? -5.689  -7.987  -22.704 1.00 17.39 ? 45  PRO D CG  1 
ATOM   6779 C  CD  . PRO D 1 45  ? -5.472  -7.163  -21.485 1.00 16.93 ? 45  PRO D CD  1 
ATOM   6780 N  N   . LEU D 1 46  ? -5.012  -3.999  -25.119 1.00 14.43 ? 46  LEU D N   1 
ATOM   6781 C  CA  . LEU D 1 46  ? -5.624  -2.803  -25.788 1.00 14.58 ? 46  LEU D CA  1 
ATOM   6782 C  C   . LEU D 1 46  ? -6.978  -3.193  -26.365 1.00 13.64 ? 46  LEU D C   1 
ATOM   6783 O  O   . LEU D 1 46  ? -7.160  -4.327  -26.839 1.00 14.22 ? 46  LEU D O   1 
ATOM   6784 C  CB  . LEU D 1 46  ? -4.738  -2.256  -26.911 1.00 15.95 ? 46  LEU D CB  1 
ATOM   6785 C  CG  . LEU D 1 46  ? -3.368  -1.691  -26.427 1.00 17.92 ? 46  LEU D CG  1 
ATOM   6786 C  CD1 . LEU D 1 46  ? -2.452  -1.516  -27.640 1.00 20.31 ? 46  LEU D CD1 1 
ATOM   6787 C  CD2 . LEU D 1 46  ? -3.589  -0.379  -25.721 1.00 22.07 ? 46  LEU D CD2 1 
ATOM   6788 N  N   . GLU D 1 47  ? -7.871  -2.228  -26.387 1.00 14.98 ? 47  GLU D N   1 
ATOM   6789 C  CA  . GLU D 1 47  ? -9.077  -2.377  -27.169 1.00 17.56 ? 47  GLU D CA  1 
ATOM   6790 C  C   . GLU D 1 47  ? -9.003  -1.397  -28.355 1.00 16.35 ? 47  GLU D C   1 
ATOM   6791 O  O   . GLU D 1 47  ? -8.693  -0.188  -28.223 1.00 14.99 ? 47  GLU D O   1 
ATOM   6792 C  CB  . GLU D 1 47  ? -10.354 -2.130  -26.360 1.00 25.42 ? 47  GLU D CB  1 
ATOM   6793 C  CG  . GLU D 1 47  ? -10.724 -3.205  -25.336 1.00 37.99 ? 47  GLU D CG  1 
ATOM   6794 C  CD  . GLU D 1 47  ? -12.251 -3.289  -25.106 1.00 51.27 ? 47  GLU D CD  1 
ATOM   6795 O  OE1 . GLU D 1 47  ? -12.997 -2.303  -25.435 1.00 60.04 ? 47  GLU D OE1 1 
ATOM   6796 O  OE2 . GLU D 1 47  ? -12.700 -4.350  -24.599 1.00 54.38 ? 47  GLU D OE2 1 
ATOM   6797 N  N   . PHE D 1 48  ? -9.375  -1.915  -29.492 1.00 15.72 ? 48  PHE D N   1 
ATOM   6798 C  CA  . PHE D 1 48  ? -9.371  -1.156  -30.752 1.00 15.50 ? 48  PHE D CA  1 
ATOM   6799 C  C   . PHE D 1 48  ? -10.791 -0.764  -31.111 1.00 18.12 ? 48  PHE D C   1 
ATOM   6800 O  O   . PHE D 1 48  ? -11.605 -1.619  -31.427 1.00 21.28 ? 48  PHE D O   1 
ATOM   6801 C  CB  . PHE D 1 48  ? -8.691  -2.019  -31.860 1.00 14.20 ? 48  PHE D CB  1 
ATOM   6802 C  CG  . PHE D 1 48  ? -7.371  -2.578  -31.452 1.00 12.89 ? 48  PHE D CG  1 
ATOM   6803 C  CD1 . PHE D 1 48  ? -6.229  -1.829  -31.348 1.00 13.74 ? 48  PHE D CD1 1 
ATOM   6804 C  CD2 . PHE D 1 48  ? -7.297  -3.928  -31.121 1.00 14.85 ? 48  PHE D CD2 1 
ATOM   6805 C  CE1 . PHE D 1 48  ? -5.026  -2.412  -30.888 1.00 15.00 ? 48  PHE D CE1 1 
ATOM   6806 C  CE2 . PHE D 1 48  ? -6.120  -4.510  -30.658 1.00 14.58 ? 48  PHE D CE2 1 
ATOM   6807 C  CZ  . PHE D 1 48  ? -4.958  -3.757  -30.547 1.00 15.83 ? 48  PHE D CZ  1 
ATOM   6808 N  N   . GLN D 1 49  ? -11.135 0.510   -30.971 1.00 14.68 ? 49  GLN D N   1 
ATOM   6809 C  CA  . GLN D 1 49  ? -12.509 0.980   -31.180 1.00 16.08 ? 49  GLN D CA  1 
ATOM   6810 C  C   . GLN D 1 49  ? -12.596 1.741   -32.482 1.00 15.41 ? 49  GLN D C   1 
ATOM   6811 O  O   . GLN D 1 49  ? -11.769 2.624   -32.732 1.00 14.53 ? 49  GLN D O   1 
ATOM   6812 C  CB  . GLN D 1 49  ? -12.917 1.921   -30.059 1.00 20.35 ? 49  GLN D CB  1 
ATOM   6813 C  CG  . GLN D 1 49  ? -12.666 1.382   -28.651 1.00 26.43 ? 49  GLN D CG  1 
ATOM   6814 C  CD  . GLN D 1 49  ? -13.515 0.162   -28.181 1.00 38.86 ? 49  GLN D CD  1 
ATOM   6815 O  OE1 . GLN D 1 49  ? -13.636 -0.072  -26.955 1.00 48.41 ? 49  GLN D OE1 1 
ATOM   6816 N  NE2 . GLN D 1 49  ? -14.050 -0.643  -29.119 1.00 39.12 ? 49  GLN D NE2 1 
ATOM   6817 N  N   . GLY D 1 50  ? -13.656 1.491   -33.291 1.00 12.68 ? 50  GLY D N   1 
ATOM   6818 C  CA  . GLY D 1 50  ? -13.843 2.250   -34.467 1.00 12.85 ? 50  GLY D CA  1 
ATOM   6819 C  C   . GLY D 1 50  ? -12.833 1.986   -35.574 1.00 11.50 ? 50  GLY D C   1 
ATOM   6820 O  O   . GLY D 1 50  ? -12.747 2.845   -36.505 1.00 11.82 ? 50  GLY D O   1 
ATOM   6821 N  N   . TYR D 1 51  ? -12.147 0.832   -35.431 1.00 12.45 ? 51  TYR D N   1 
ATOM   6822 C  CA  . TYR D 1 51  ? -11.167 0.402   -36.467 1.00 11.67 ? 51  TYR D CA  1 
ATOM   6823 C  C   . TYR D 1 51  ? -11.840 -0.136  -37.726 1.00 13.14 ? 51  TYR D C   1 
ATOM   6824 O  O   . TYR D 1 51  ? -11.240 -0.155  -38.813 1.00 12.18 ? 51  TYR D O   1 
ATOM   6825 C  CB  . TYR D 1 51  ? -10.190 -0.680  -35.920 1.00 10.96 ? 51  TYR D CB  1 
ATOM   6826 C  CG  . TYR D 1 51  ? -8.993  -0.115  -35.198 1.00 11.00 ? 51  TYR D CG  1 
ATOM   6827 C  CD1 . TYR D 1 51  ? -7.747  -0.566  -35.542 1.00 10.61 ? 51  TYR D CD1 1 
ATOM   6828 C  CD2 . TYR D 1 51  ? -9.092  0.950   -34.268 1.00 11.03 ? 51  TYR D CD2 1 
ATOM   6829 C  CE1 . TYR D 1 51  ? -6.603  -0.046  -34.928 1.00 11.17 ? 51  TYR D CE1 1 
ATOM   6830 C  CE2 . TYR D 1 51  ? -7.971  1.476   -33.652 1.00 11.96 ? 51  TYR D CE2 1 
ATOM   6831 C  CZ  . TYR D 1 51  ? -6.727  1.002   -34.047 1.00 11.05 ? 51  TYR D CZ  1 
ATOM   6832 O  OH  . TYR D 1 51  ? -5.510  1.416   -33.494 1.00 11.14 ? 51  TYR D OH  1 
ATOM   6833 N  N   . ASN D 1 52  ? -13.135 -0.530  -37.625 1.00 13.24 ? 52  ASN D N   1 
ATOM   6834 C  CA  . ASN D 1 52  ? -13.760 -1.081  -38.785 1.00 12.78 ? 52  ASN D CA  1 
ATOM   6835 C  C   . ASN D 1 52  ? -14.357 0.025   -39.651 1.00 14.57 ? 52  ASN D C   1 
ATOM   6836 O  O   . ASN D 1 52  ? -15.549 0.470   -39.479 1.00 16.64 ? 52  ASN D O   1 
ATOM   6837 C  CB  . ASN D 1 52  ? -14.834 -2.093  -38.336 1.00 13.66 ? 52  ASN D CB  1 
ATOM   6838 C  CG  . ASN D 1 52  ? -15.402 -2.874  -39.491 1.00 14.58 ? 52  ASN D CG  1 
ATOM   6839 O  OD1 . ASN D 1 52  ? -15.183 -2.567  -40.606 1.00 16.51 ? 52  ASN D OD1 1 
ATOM   6840 N  ND2 . ASN D 1 52  ? -16.234 -3.836  -39.181 1.00 21.26 ? 52  ASN D ND2 1 
ATOM   6841 N  N   . LEU D 1 53  ? -13.536 0.552   -40.537 1.00 13.97 ? 53  LEU D N   1 
ATOM   6842 C  CA  . LEU D 1 53  ? -13.974 1.724   -41.345 1.00 13.59 ? 53  LEU D CA  1 
ATOM   6843 C  C   . LEU D 1 53  ? -14.927 1.254   -42.473 1.00 16.19 ? 53  LEU D C   1 
ATOM   6844 O  O   . LEU D 1 53  ? -14.713 0.231   -43.110 1.00 15.96 ? 53  LEU D O   1 
ATOM   6845 C  CB  . LEU D 1 53  ? -12.764 2.488   -41.949 1.00 14.87 ? 53  LEU D CB  1 
ATOM   6846 C  CG  . LEU D 1 53  ? -11.666 2.772   -40.924 1.00 14.19 ? 53  LEU D CG  1 
ATOM   6847 C  CD1 . LEU D 1 53  ? -10.534 3.432   -41.710 1.00 14.19 ? 53  LEU D CD1 1 
ATOM   6848 C  CD2 . LEU D 1 53  ? -12.214 3.703   -39.804 1.00 13.18 ? 53  LEU D CD2 1 
ATOM   6849 N  N   . SER D 1 54  ? -15.968 2.010   -42.682 1.00 14.12 ? 54  SER D N   1 
ATOM   6850 C  CA  . SER D 1 54  ? -16.950 1.638   -43.703 1.00 16.48 ? 54  SER D CA  1 
ATOM   6851 C  C   . SER D 1 54  ? -16.383 1.683   -45.152 1.00 16.79 ? 54  SER D C   1 
ATOM   6852 O  O   . SER D 1 54  ? -15.723 2.638   -45.564 1.00 16.20 ? 54  SER D O   1 
ATOM   6853 C  CB  . SER D 1 54  ? -18.105 2.594   -43.659 1.00 19.02 ? 54  SER D CB  1 
ATOM   6854 O  OG  . SER D 1 54  ? -19.058 2.278   -44.685 1.00 17.55 ? 54  SER D OG  1 
ATOM   6855 N  N   . ALA D 1 55  ? -16.748 0.657   -45.892 1.00 19.31 ? 55  ALA D N   1 
ATOM   6856 C  CA  . ALA D 1 55  ? -16.239 0.510   -47.237 1.00 19.52 ? 55  ALA D CA  1 
ATOM   6857 C  C   . ALA D 1 55  ? -16.928 1.528   -48.131 1.00 16.98 ? 55  ALA D C   1 
ATOM   6858 O  O   . ALA D 1 55  ? -16.549 1.768   -49.311 1.00 17.14 ? 55  ALA D O   1 
ATOM   6859 C  CB  . ALA D 1 55  ? -16.505 -0.935  -47.716 1.00 23.86 ? 55  ALA D CB  1 
ATOM   6860 N  N   . ASN D 1 56  ? -17.987 2.171   -47.636 1.00 19.86 ? 56  ASN D N   1 
ATOM   6861 C  CA  . ASN D 1 56  ? -18.593 3.277   -48.339 1.00 18.56 ? 56  ASN D CA  1 
ATOM   6862 C  C   . ASN D 1 56  ? -18.023 4.638   -48.038 1.00 18.11 ? 56  ASN D C   1 
ATOM   6863 O  O   . ASN D 1 56  ? -18.433 5.633   -48.629 1.00 21.84 ? 56  ASN D O   1 
ATOM   6864 C  CB  . ASN D 1 56  ? -20.139 3.354   -48.074 1.00 20.27 ? 56  ASN D CB  1 
ATOM   6865 C  CG  . ASN D 1 56  ? -20.929 2.285   -48.824 1.00 27.85 ? 56  ASN D CG  1 
ATOM   6866 O  OD1 . ASN D 1 56  ? -20.393 1.566   -49.680 1.00 28.63 ? 56  ASN D OD1 1 
ATOM   6867 N  ND2 . ASN D 1 56  ? -22.244 2.203   -48.528 1.00 31.14 ? 56  ASN D ND2 1 
ATOM   6868 N  N   . LYS D 1 57  ? -17.051 4.720   -47.132 1.00 16.87 ? 57  LYS D N   1 
ATOM   6869 C  CA  . LYS D 1 57  ? -16.361 5.954   -46.899 1.00 15.79 ? 57  LYS D CA  1 
ATOM   6870 C  C   . LYS D 1 57  ? -14.929 5.782   -47.483 1.00 15.44 ? 57  LYS D C   1 
ATOM   6871 O  O   . LYS D 1 57  ? -14.557 4.673   -47.920 1.00 16.18 ? 57  LYS D O   1 
ATOM   6872 C  CB  . LYS D 1 57  ? -16.257 6.194   -45.394 1.00 16.88 ? 57  LYS D CB  1 
ATOM   6873 C  CG  . LYS D 1 57  ? -17.643 6.472   -44.804 1.00 21.22 ? 57  LYS D CG  1 
ATOM   6874 C  CD  . LYS D 1 57  ? -17.513 6.960   -43.369 1.00 23.12 ? 57  LYS D CD  1 
ATOM   6875 C  CE  . LYS D 1 57  ? -18.699 7.845   -43.026 1.00 28.05 ? 57  LYS D CE  1 
ATOM   6876 N  NZ  . LYS D 1 57  ? -18.707 8.041   -41.543 1.00 28.29 ? 57  LYS D NZ  1 
ATOM   6877 N  N   . GLN D 1 58  ? -14.261 6.890   -47.625 1.00 16.01 ? 58  GLN D N   1 
ATOM   6878 C  CA  . GLN D 1 58  ? -12.916 6.839   -48.245 1.00 17.22 ? 58  GLN D CA  1 
ATOM   6879 C  C   . GLN D 1 58  ? -11.933 7.734   -47.463 1.00 15.22 ? 58  GLN D C   1 
ATOM   6880 O  O   . GLN D 1 58  ? -12.305 8.724   -46.755 1.00 16.19 ? 58  GLN D O   1 
ATOM   6881 C  CB  . GLN D 1 58  ? -12.954 7.138   -49.746 1.00 23.06 ? 58  GLN D CB  1 
ATOM   6882 C  CG  . GLN D 1 58  ? -13.321 8.553   -50.038 1.00 22.45 ? 58  GLN D CG  1 
ATOM   6883 C  CD  . GLN D 1 58  ? -13.522 8.844   -51.553 1.00 23.84 ? 58  GLN D CD  1 
ATOM   6884 O  OE1 . GLN D 1 58  ? -13.307 7.958   -52.452 1.00 24.86 ? 58  GLN D OE1 1 
ATOM   6885 N  NE2 . GLN D 1 58  ? -13.832 10.137  -51.843 1.00 25.00 ? 58  GLN D NE2 1 
ATOM   6886 N  N   . PHE D 1 59  ? -10.665 7.322   -47.508 1.00 13.83 ? 59  PHE D N   1 
ATOM   6887 C  CA  . PHE D 1 59  ? -9.599  7.888   -46.655 1.00 13.02 ? 59  PHE D CA  1 
ATOM   6888 C  C   . PHE D 1 59  ? -8.461  8.268   -47.532 1.00 11.56 ? 59  PHE D C   1 
ATOM   6889 O  O   . PHE D 1 59  ? -8.136  7.558   -48.453 1.00 12.90 ? 59  PHE D O   1 
ATOM   6890 C  CB  . PHE D 1 59  ? -9.255  6.882   -45.551 1.00 12.76 ? 59  PHE D CB  1 
ATOM   6891 C  CG  . PHE D 1 59  ? -10.490 6.558   -44.705 1.00 13.38 ? 59  PHE D CG  1 
ATOM   6892 C  CD1 . PHE D 1 59  ? -11.435 5.589   -45.156 1.00 13.67 ? 59  PHE D CD1 1 
ATOM   6893 C  CD2 . PHE D 1 59  ? -10.856 7.382   -43.615 1.00 15.84 ? 59  PHE D CD2 1 
ATOM   6894 C  CE1 . PHE D 1 59  ? -12.630 5.328   -44.440 1.00 13.06 ? 59  PHE D CE1 1 
ATOM   6895 C  CE2 . PHE D 1 59  ? -12.034 7.125   -42.915 1.00 14.07 ? 59  PHE D CE2 1 
ATOM   6896 C  CZ  . PHE D 1 59  ? -12.912 6.118   -43.324 1.00 14.41 ? 59  PHE D CZ  1 
ATOM   6897 N  N   . LEU D 1 60  ? -7.885  9.429   -47.200 1.00 10.80 ? 60  LEU D N   1 
ATOM   6898 C  CA  . LEU D 1 60  ? -6.849  10.005  -47.998 1.00 11.66 ? 60  LEU D CA  1 
ATOM   6899 C  C   . LEU D 1 60  ? -5.491  9.325   -47.803 1.00 11.58 ? 60  LEU D C   1 
ATOM   6900 O  O   . LEU D 1 60  ? -4.901  9.349   -46.694 1.00 11.91 ? 60  LEU D O   1 
ATOM   6901 C  CB  . LEU D 1 60  ? -6.741  11.514  -47.636 1.00 13.01 ? 60  LEU D CB  1 
ATOM   6902 C  CG  . LEU D 1 60  ? -6.020  12.287  -48.694 1.00 16.12 ? 60  LEU D CG  1 
ATOM   6903 C  CD1 . LEU D 1 60  ? -6.768  12.259  -50.021 1.00 17.28 ? 60  LEU D CD1 1 
ATOM   6904 C  CD2 . LEU D 1 60  ? -5.759  13.699  -48.190 1.00 19.05 ? 60  LEU D CD2 1 
ATOM   6905 N  N   . LEU D 1 61  ? -4.958  8.847   -48.913 1.00 11.70 ? 61  LEU D N   1 
ATOM   6906 C  CA  . LEU D 1 61  ? -3.563  8.336   -48.981 1.00 11.82 ? 61  LEU D CA  1 
ATOM   6907 C  C   . LEU D 1 61  ? -2.661  9.386   -49.627 1.00 11.82 ? 61  LEU D C   1 
ATOM   6908 O  O   . LEU D 1 61  ? -2.993  9.957   -50.716 1.00 14.24 ? 61  LEU D O   1 
ATOM   6909 C  CB  . LEU D 1 61  ? -3.540  7.062   -49.812 1.00 11.96 ? 61  LEU D CB  1 
ATOM   6910 C  CG  . LEU D 1 61  ? -2.230  6.241   -49.796 1.00 12.09 ? 61  LEU D CG  1 
ATOM   6911 C  CD1 . LEU D 1 61  ? -2.027  5.508   -48.514 1.00 11.75 ? 61  LEU D CD1 1 
ATOM   6912 C  CD2 . LEU D 1 61  ? -2.287  5.240   -50.980 1.00 12.88 ? 61  LEU D CD2 1 
ATOM   6913 N  N   . THR D 1 62  ? -1.514  9.685   -48.970 1.00 10.89 ? 62  THR D N   1 
ATOM   6914 C  CA  . THR D 1 62  ? -0.666  10.777  -49.503 1.00 12.10 ? 62  THR D CA  1 
ATOM   6915 C  C   . THR D 1 62  ? 0.807   10.308  -49.495 1.00 11.28 ? 62  THR D C   1 
ATOM   6916 O  O   . THR D 1 62  ? 1.266   9.636   -48.553 1.00 12.22 ? 62  THR D O   1 
ATOM   6917 C  CB  . THR D 1 62  ? -0.764  11.998  -48.591 1.00 12.97 ? 62  THR D CB  1 
ATOM   6918 O  OG1 . THR D 1 62  ? -2.089  12.498  -48.505 1.00 17.35 ? 62  THR D OG1 1 
ATOM   6919 C  CG2 . THR D 1 62  ? 0.119   13.206  -49.114 1.00 16.09 ? 62  THR D CG2 1 
ATOM   6920 N  N   . ASN D 1 63  ? 1.557   10.688  -50.522 1.00 11.40 ? 63  ASN D N   1 
ATOM   6921 C  CA  . ASN D 1 63  ? 3.043   10.566  -50.469 1.00 11.17 ? 63  ASN D CA  1 
ATOM   6922 C  C   . ASN D 1 63  ? 3.521   11.899  -49.946 1.00 12.36 ? 63  ASN D C   1 
ATOM   6923 O  O   . ASN D 1 63  ? 3.351   12.938  -50.565 1.00 14.63 ? 63  ASN D O   1 
ATOM   6924 C  CB  . ASN D 1 63  ? 3.540   10.329  -51.967 1.00 10.89 ? 63  ASN D CB  1 
ATOM   6925 C  CG  . ASN D 1 63  ? 5.037   10.353  -52.093 1.00 11.59 ? 63  ASN D CG  1 
ATOM   6926 O  OD1 . ASN D 1 63  ? 5.720   10.976  -51.240 1.00 13.51 ? 63  ASN D OD1 1 
ATOM   6927 N  ND2 . ASN D 1 63  ? 5.554   9.649   -53.127 1.00 11.22 ? 63  ASN D ND2 1 
ATOM   6928 N  N   . ASN D 1 64  ? 4.114   11.897  -48.759 1.00 11.65 ? 64  ASN D N   1 
ATOM   6929 C  CA  . ASN D 1 64  ? 4.558   13.150  -48.107 1.00 13.66 ? 64  ASN D CA  1 
ATOM   6930 C  C   . ASN D 1 64  ? 6.068   13.419  -48.295 1.00 13.43 ? 64  ASN D C   1 
ATOM   6931 O  O   . ASN D 1 64  ? 6.616   14.310  -47.608 1.00 16.48 ? 64  ASN D O   1 
ATOM   6932 C  CB  . ASN D 1 64  ? 4.142   13.141  -46.619 1.00 15.07 ? 64  ASN D CB  1 
ATOM   6933 C  CG  . ASN D 1 64  ? 4.878   12.102  -45.779 1.00 17.38 ? 64  ASN D CG  1 
ATOM   6934 O  OD1 . ASN D 1 64  ? 5.796   11.433  -46.253 1.00 14.76 ? 64  ASN D OD1 1 
ATOM   6935 N  ND2 . ASN D 1 64  ? 4.483   11.969  -44.453 1.00 18.28 ? 64  ASN D ND2 1 
ATOM   6936 N  N   . GLY D 1 65  ? 6.687   12.603  -49.187 1.00 13.49 ? 65  GLY D N   1 
ATOM   6937 C  CA  . GLY D 1 65  ? 8.115   12.748  -49.496 1.00 12.79 ? 65  GLY D CA  1 
ATOM   6938 C  C   . GLY D 1 65  ? 8.985   11.945  -48.516 1.00 12.72 ? 65  GLY D C   1 
ATOM   6939 O  O   . GLY D 1 65  ? 10.182  11.832  -48.747 1.00 12.18 ? 65  GLY D O   1 
ATOM   6940 N  N   . HIS D 1 66  ? 8.407   11.348  -47.473 1.00 11.99 ? 66  HIS D N   1 
ATOM   6941 C  CA  . HIS D 1 66  ? 9.159   10.493  -46.536 1.00 12.33 ? 66  HIS D CA  1 
ATOM   6942 C  C   . HIS D 1 66  ? 8.617   9.098   -46.462 1.00 12.36 ? 66  HIS D C   1 
ATOM   6943 O  O   . HIS D 1 66  ? 9.350   8.159   -46.154 1.00 12.67 ? 66  HIS D O   1 
ATOM   6944 C  CB  . HIS D 1 66  ? 9.213   11.114  -45.126 1.00 12.53 ? 66  HIS D CB  1 
ATOM   6945 C  CG  . HIS D 1 66  ? 9.807   12.491  -45.093 1.00 13.91 ? 66  HIS D CG  1 
ATOM   6946 N  ND1 . HIS D 1 66  ? 11.116  12.721  -45.322 1.00 13.44 ? 66  HIS D ND1 1 
ATOM   6947 C  CD2 . HIS D 1 66  ? 9.219   13.712  -44.841 1.00 15.35 ? 66  HIS D CD2 1 
ATOM   6948 C  CE1 . HIS D 1 66  ? 11.337  14.072  -45.220 1.00 15.18 ? 66  HIS D CE1 1 
ATOM   6949 N  NE2 . HIS D 1 66  ? 10.172  14.660  -44.931 1.00 17.50 ? 66  HIS D NE2 1 
ATOM   6950 N  N   . SER D 1 67  ? 7.295   8.944   -46.637 1.00 11.96 ? 67  SER D N   1 
ATOM   6951 C  CA  . SER D 1 67  ? 6.629   7.641   -46.622 1.00 11.59 ? 67  SER D CA  1 
ATOM   6952 C  C   . SER D 1 67  ? 5.350   7.834   -47.402 1.00 11.49 ? 67  SER D C   1 
ATOM   6953 O  O   . SER D 1 67  ? 5.102   8.890   -47.977 1.00 13.16 ? 67  SER D O   1 
ATOM   6954 C  CB  . SER D 1 67  ? 6.255   7.303   -45.167 1.00 12.99 ? 67  SER D CB  1 
ATOM   6955 O  OG  . SER D 1 67  ? 5.716   5.995   -44.979 1.00 13.45 ? 67  SER D OG  1 
ATOM   6956 N  N   . VAL D 1 68  ? 4.532   6.807   -47.340 1.00 11.13 ? 68  VAL D N   1 
ATOM   6957 C  CA  . VAL D 1 68  ? 3.127   6.844   -47.740 1.00 11.22 ? 68  VAL D CA  1 
ATOM   6958 C  C   . VAL D 1 68  ? 2.244   6.769   -46.506 1.00 9.78  ? 68  VAL D C   1 
ATOM   6959 O  O   . VAL D 1 68  ? 2.474   5.973   -45.637 1.00 10.74 ? 68  VAL D O   1 
ATOM   6960 C  CB  . VAL D 1 68  ? 2.829   5.764   -48.789 1.00 12.28 ? 68  VAL D CB  1 
ATOM   6961 C  CG1 . VAL D 1 68  ? 3.033   4.358   -48.286 1.00 12.18 ? 68  VAL D CG1 1 
ATOM   6962 C  CG2 . VAL D 1 68  ? 1.424   5.932   -49.324 1.00 15.95 ? 68  VAL D CG2 1 
ATOM   6963 N  N   . LYS D 1 69  ? 1.303   7.704   -46.395 1.00 9.95  ? 69  LYS D N   1 
ATOM   6964 C  CA  . LYS D 1 69  ? 0.425   7.758   -45.183 1.00 10.50 ? 69  LYS D CA  1 
ATOM   6965 C  C   . LYS D 1 69  ? -1.045  7.769   -45.535 1.00 10.51 ? 69  LYS D C   1 
ATOM   6966 O  O   . LYS D 1 69  ? -1.417  8.277   -46.583 1.00 12.10 ? 69  LYS D O   1 
ATOM   6967 C  CB  . LYS D 1 69  ? 0.781   8.975   -44.333 1.00 12.67 ? 69  LYS D CB  1 
ATOM   6968 C  CG  . LYS D 1 69  ? 0.323   10.290  -44.892 1.00 15.76 ? 69  LYS D CG  1 
ATOM   6969 C  CD  . LYS D 1 69  ? 0.269   11.349  -43.748 1.00 19.17 ? 69  LYS D CD  1 
ATOM   6970 C  CE  . LYS D 1 69  ? -0.013  12.612  -44.488 1.00 21.38 ? 69  LYS D CE  1 
ATOM   6971 N  NZ  . LYS D 1 69  ? -0.175  13.687  -43.467 1.00 26.79 ? 69  LYS D NZ  1 
ATOM   6972 N  N   . LEU D 1 70  ? -1.817  7.095   -44.708 1.00 9.70  ? 70  LEU D N   1 
ATOM   6973 C  CA  . LEU D 1 70  ? -3.238  7.062   -44.816 1.00 8.87  ? 70  LEU D CA  1 
ATOM   6974 C  C   . LEU D 1 70  ? -3.777  7.833   -43.611 1.00 9.41  ? 70  LEU D C   1 
ATOM   6975 O  O   . LEU D 1 70  ? -3.515  7.484   -42.432 1.00 10.21 ? 70  LEU D O   1 
ATOM   6976 C  CB  . LEU D 1 70  ? -3.747  5.614   -44.794 1.00 9.10  ? 70  LEU D CB  1 
ATOM   6977 C  CG  . LEU D 1 70  ? -5.270  5.405   -44.928 1.00 9.20  ? 70  LEU D CG  1 
ATOM   6978 C  CD1 . LEU D 1 70  ? -5.673  5.879   -46.362 1.00 12.28 ? 70  LEU D CD1 1 
ATOM   6979 C  CD2 . LEU D 1 70  ? -5.580  3.926   -44.641 1.00 11.19 ? 70  LEU D CD2 1 
ATOM   6980 N  N   . ASN D 1 71  ? -4.644  8.811   -43.951 1.00 11.08 ? 71  ASN D N   1 
ATOM   6981 C  CA  . ASN D 1 71  ? -5.314  9.609   -42.895 1.00 10.51 ? 71  ASN D CA  1 
ATOM   6982 C  C   . ASN D 1 71  ? -6.395  8.803   -42.242 1.00 11.34 ? 71  ASN D C   1 
ATOM   6983 O  O   . ASN D 1 71  ? -7.147  8.022   -42.938 1.00 12.27 ? 71  ASN D O   1 
ATOM   6984 C  CB  . ASN D 1 71  ? -5.940  10.830  -43.467 1.00 13.06 ? 71  ASN D CB  1 
ATOM   6985 C  CG  . ASN D 1 71  ? -5.001  11.908  -43.723 1.00 14.60 ? 71  ASN D CG  1 
ATOM   6986 O  OD1 . ASN D 1 71  ? -3.775  11.820  -43.558 1.00 19.41 ? 71  ASN D OD1 1 
ATOM   6987 N  ND2 . ASN D 1 71  ? -5.592  13.027  -44.162 1.00 18.95 ? 71  ASN D ND2 1 
ATOM   6988 N  N   . LEU D 1 72  ? -6.480  8.862   -40.919 1.00 9.94  ? 72  LEU D N   1 
ATOM   6989 C  CA  . LEU D 1 72  ? -7.486  8.065   -40.188 1.00 10.47 ? 72  LEU D CA  1 
ATOM   6990 C  C   . LEU D 1 72  ? -8.409  9.020   -39.411 1.00 11.40 ? 72  LEU D C   1 
ATOM   6991 O  O   . LEU D 1 72  ? -8.018  10.138  -39.083 1.00 14.45 ? 72  LEU D O   1 
ATOM   6992 C  CB  . LEU D 1 72  ? -6.790  7.102   -39.211 1.00 10.74 ? 72  LEU D CB  1 
ATOM   6993 C  CG  . LEU D 1 72  ? -5.910  6.032   -39.910 1.00 12.19 ? 72  LEU D CG  1 
ATOM   6994 C  CD1 . LEU D 1 72  ? -5.092  5.336   -38.853 1.00 9.79  ? 72  LEU D CD1 1 
ATOM   6995 C  CD2 . LEU D 1 72  ? -6.813  5.082   -40.700 1.00 12.63 ? 72  LEU D CD2 1 
ATOM   6996 N  N   . PRO D 1 73  ? -9.646  8.563   -39.146 1.00 11.42 ? 73  PRO D N   1 
ATOM   6997 C  CA  . PRO D 1 73  ? -10.666 9.420   -38.495 1.00 14.05 ? 73  PRO D CA  1 
ATOM   6998 C  C   . PRO D 1 73  ? -10.500 9.453   -36.961 1.00 16.89 ? 73  PRO D C   1 
ATOM   6999 O  O   . PRO D 1 73  ? -10.091 8.459   -36.371 1.00 14.24 ? 73  PRO D O   1 
ATOM   7000 C  CB  . PRO D 1 73  ? -11.955 8.739   -38.938 1.00 13.56 ? 73  PRO D CB  1 
ATOM   7001 C  CG  . PRO D 1 73  ? -11.625 7.251   -38.974 1.00 13.26 ? 73  PRO D CG  1 
ATOM   7002 C  CD  . PRO D 1 73  ? -10.258 7.289   -39.657 1.00 12.89 ? 73  PRO D CD  1 
ATOM   7003 N  N   . SER D 1 74  ? -10.768 10.593  -36.315 1.00 17.08 ? 74  SER D N   1 
ATOM   7004 C  CA  . SER D 1 74  ? -10.492 10.637  -34.884 1.00 17.76 ? 74  SER D CA  1 
ATOM   7005 C  C   . SER D 1 74  ? -11.469 9.826   -34.052 1.00 17.20 ? 74  SER D C   1 
ATOM   7006 O  O   . SER D 1 74  ? -11.202 9.588   -32.834 1.00 18.00 ? 74  SER D O   1 
ATOM   7007 C  CB  . SER D 1 74  ? -10.342 12.072  -34.376 1.00 19.08 ? 74  SER D CB  1 
ATOM   7008 O  OG  . SER D 1 74  ? -11.536 12.818  -34.761 1.00 21.92 ? 74  SER D OG  1 
ATOM   7009 N  N   . ASP D 1 75  ? -12.550 9.378   -34.666 1.00 17.51 ? 75  ASP D N   1 
ATOM   7010 C  CA  . ASP D 1 75  ? -13.421 8.450   -33.927 1.00 19.80 ? 75  ASP D CA  1 
ATOM   7011 C  C   . ASP D 1 75  ? -12.809 7.049   -33.730 1.00 19.79 ? 75  ASP D C   1 
ATOM   7012 O  O   . ASP D 1 75  ? -13.294 6.267   -32.894 1.00 19.72 ? 75  ASP D O   1 
ATOM   7013 C  CB  . ASP D 1 75  ? -14.862 8.431   -34.468 1.00 25.99 ? 75  ASP D CB  1 
ATOM   7014 C  CG  . ASP D 1 75  ? -14.992 7.804   -35.820 1.00 37.35 ? 75  ASP D CG  1 
ATOM   7015 O  OD1 . ASP D 1 75  ? -13.973 7.650   -36.535 1.00 46.77 ? 75  ASP D OD1 1 
ATOM   7016 O  OD2 . ASP D 1 75  ? -16.149 7.477   -36.212 1.00 44.69 ? 75  ASP D OD2 1 
ATOM   7017 N  N   . MET D 1 76  ? -11.750 6.740   -34.490 1.00 15.39 ? 76  MET D N   1 
ATOM   7018 C  CA  . MET D 1 76  ? -11.003 5.497   -34.285 1.00 15.52 ? 76  MET D CA  1 
ATOM   7019 C  C   . MET D 1 76  ? -10.131 5.733   -33.033 1.00 13.21 ? 76  MET D C   1 
ATOM   7020 O  O   . MET D 1 76  ? -9.424  6.717   -32.966 1.00 12.23 ? 76  MET D O   1 
ATOM   7021 C  CB  . MET D 1 76  ? -10.153 5.237   -35.561 1.00 15.49 ? 76  MET D CB  1 
ATOM   7022 C  CG  . MET D 1 76  ? -9.370  3.975   -35.558 1.00 16.03 ? 76  MET D CG  1 
ATOM   7023 S  SD  . MET D 1 76  ? -8.709  3.948   -37.274 1.00 16.22 ? 76  MET D SD  1 
ATOM   7024 C  CE  . MET D 1 76  ? -7.382  2.836   -37.002 1.00 16.27 ? 76  MET D CE  1 
ATOM   7025 N  N   . HIS D 1 77  ? -10.176 4.837   -32.053 1.00 13.64 ? 77  HIS D N   1 
ATOM   7026 C  CA  . HIS D 1 77  ? -9.304  5.013   -30.893 1.00 13.15 ? 77  HIS D CA  1 
ATOM   7027 C  C   . HIS D 1 77  ? -8.831  3.839   -30.222 1.00 15.09 ? 77  HIS D C   1 
ATOM   7028 O  O   . HIS D 1 77  ? -9.304  2.732   -30.519 1.00 14.29 ? 77  HIS D O   1 
ATOM   7029 C  CB  . HIS D 1 77  ? -9.979  5.997   -29.928 1.00 19.85 ? 77  HIS D CB  1 
ATOM   7030 C  CG  . HIS D 1 77  ? -11.230 5.529   -29.361 1.00 22.10 ? 77  HIS D CG  1 
ATOM   7031 N  ND1 . HIS D 1 77  ? -12.417 5.624   -30.028 1.00 24.99 ? 77  HIS D ND1 1 
ATOM   7032 C  CD2 . HIS D 1 77  ? -11.535 5.058   -28.087 1.00 27.56 ? 77  HIS D CD2 1 
ATOM   7033 C  CE1 . HIS D 1 77  ? -13.410 5.144   -29.255 1.00 27.99 ? 77  HIS D CE1 1 
ATOM   7034 N  NE2 . HIS D 1 77  ? -12.882 4.787   -28.069 1.00 28.84 ? 77  HIS D NE2 1 
ATOM   7035 N  N   . ILE D 1 78  ? -7.840  3.996   -29.351 1.00 12.27 ? 78  ILE D N   1 
ATOM   7036 C  CA  . ILE D 1 78  ? -7.476  2.924   -28.469 1.00 14.41 ? 78  ILE D CA  1 
ATOM   7037 C  C   . ILE D 1 78  ? -7.837  3.188   -26.994 1.00 14.09 ? 78  ILE D C   1 
ATOM   7038 O  O   . ILE D 1 78  ? -7.722  4.325   -26.524 1.00 15.44 ? 78  ILE D O   1 
ATOM   7039 C  CB  . ILE D 1 78  ? -6.024  2.493   -28.592 1.00 15.66 ? 78  ILE D CB  1 
ATOM   7040 C  CG1 . ILE D 1 78  ? -5.061  3.640   -28.536 1.00 16.60 ? 78  ILE D CG1 1 
ATOM   7041 C  CG2 . ILE D 1 78  ? -5.836  1.752   -29.891 1.00 16.44 ? 78  ILE D CG2 1 
ATOM   7042 C  CD1 . ILE D 1 78  ? -3.632  3.116   -28.884 1.00 18.19 ? 78  ILE D CD1 1 
ATOM   7043 N  N   . GLN D 1 79  ? -8.310  2.139   -26.353 1.00 16.77 ? 79  GLN D N   1 
ATOM   7044 C  CA  . GLN D 1 79  ? -8.547  2.094   -24.896 1.00 19.30 ? 79  GLN D CA  1 
ATOM   7045 C  C   . GLN D 1 79  ? -7.600  1.147   -24.245 1.00 18.27 ? 79  GLN D C   1 
ATOM   7046 O  O   . GLN D 1 79  ? -7.157  0.133   -24.854 1.00 18.15 ? 79  GLN D O   1 
ATOM   7047 C  CB  . GLN D 1 79  ? -10.010 1.733   -24.566 1.00 24.22 ? 79  GLN D CB  1 
ATOM   7048 C  CG  . GLN D 1 79  ? -11.018 2.786   -25.022 1.00 30.13 ? 79  GLN D CG  1 
ATOM   7049 C  CD  . GLN D 1 79  ? -11.054 4.028   -24.143 1.00 33.22 ? 79  GLN D CD  1 
ATOM   7050 O  OE1 . GLN D 1 79  ? -10.027 4.696   -23.857 1.00 36.08 ? 79  GLN D OE1 1 
ATOM   7051 N  NE2 . GLN D 1 79  ? -12.246 4.355   -23.705 1.00 40.06 ? 79  GLN D NE2 1 
ATOM   7052 N  N   . GLY D 1 80  ? -7.216  1.477   -22.996 1.00 15.92 ? 80  GLY D N   1 
ATOM   7053 C  CA  . GLY D 1 80  ? -6.367  0.630   -22.226 1.00 17.38 ? 80  GLY D CA  1 
ATOM   7054 C  C   . GLY D 1 80  ? -5.175  1.372   -21.706 1.00 23.26 ? 80  GLY D C   1 
ATOM   7055 O  O   . GLY D 1 80  ? -4.428  0.824   -20.881 1.00 30.98 ? 80  GLY D O   1 
ATOM   7056 N  N   . LEU D 1 81  ? -4.912  2.564   -22.238 1.00 16.76 ? 81  LEU D N   1 
ATOM   7057 C  CA  . LEU D 1 81  ? -3.748  3.270   -21.778 1.00 15.55 ? 81  LEU D CA  1 
ATOM   7058 C  C   . LEU D 1 81  ? -4.188  4.257   -20.678 1.00 14.01 ? 81  LEU D C   1 
ATOM   7059 O  O   . LEU D 1 81  ? -5.351  4.146   -20.184 1.00 17.28 ? 81  LEU D O   1 
ATOM   7060 C  CB  . LEU D 1 81  ? -3.082  3.983   -22.942 1.00 14.26 ? 81  LEU D CB  1 
ATOM   7061 C  CG  . LEU D 1 81  ? -2.591  3.127   -24.110 1.00 15.52 ? 81  LEU D CG  1 
ATOM   7062 C  CD1 . LEU D 1 81  ? -2.040  4.027   -25.269 1.00 14.59 ? 81  LEU D CD1 1 
ATOM   7063 C  CD2 . LEU D 1 81  ? -1.490  2.199   -23.594 1.00 14.33 ? 81  LEU D CD2 1 
ATOM   7064 N  N   . GLN D 1 82  ? -3.308  5.167   -20.269 1.00 14.47 ? 82  GLN D N   1 
ATOM   7065 C  CA  . GLN D 1 82  ? -3.722  6.147   -19.209 1.00 14.03 ? 82  GLN D CA  1 
ATOM   7066 C  C   . GLN D 1 82  ? -4.720  7.177   -19.633 1.00 12.98 ? 82  GLN D C   1 
ATOM   7067 O  O   . GLN D 1 82  ? -5.333  7.827   -18.785 1.00 13.74 ? 82  GLN D O   1 
ATOM   7068 C  CB  . GLN D 1 82  ? -2.489  6.804   -18.591 1.00 13.91 ? 82  GLN D CB  1 
ATOM   7069 C  CG  . GLN D 1 82  ? -2.062  8.120   -19.235 1.00 15.80 ? 82  GLN D CG  1 
ATOM   7070 C  CD  . GLN D 1 82  ? -1.584  7.979   -20.696 1.00 16.97 ? 82  GLN D CD  1 
ATOM   7071 O  OE1 . GLN D 1 82  ? -1.276  6.885   -21.212 1.00 19.12 ? 82  GLN D OE1 1 
ATOM   7072 N  NE2 . GLN D 1 82  ? -1.409  9.112   -21.321 1.00 18.86 ? 82  GLN D NE2 1 
ATOM   7073 N  N   . SER D 1 83  ? -4.907  7.359   -20.935 1.00 11.41 ? 83  SER D N   1 
ATOM   7074 C  CA  . SER D 1 83  ? -5.834  8.346   -21.498 1.00 12.74 ? 83  SER D CA  1 
ATOM   7075 C  C   . SER D 1 83  ? -6.377  7.714   -22.772 1.00 12.93 ? 83  SER D C   1 
ATOM   7076 O  O   . SER D 1 83  ? -5.776  6.709   -23.331 1.00 11.85 ? 83  SER D O   1 
ATOM   7077 C  CB  . SER D 1 83  ? -5.108  9.591   -21.974 1.00 13.65 ? 83  SER D CB  1 
ATOM   7078 O  OG  . SER D 1 83  ? -4.521  10.302  -20.881 1.00 13.69 ? 83  SER D OG  1 
ATOM   7079 N  N   . ARG D 1 84  ? -7.441  8.299   -23.316 1.00 12.79 ? 84  ARG D N   1 
ATOM   7080 C  CA  . ARG D 1 84  ? -7.948  7.826   -24.636 1.00 13.78 ? 84  ARG D CA  1 
ATOM   7081 C  C   . ARG D 1 84  ? -6.994  8.386   -25.700 1.00 13.40 ? 84  ARG D C   1 
ATOM   7082 O  O   . ARG D 1 84  ? -6.666  9.582   -25.667 1.00 12.16 ? 84  ARG D O   1 
ATOM   7083 C  CB  . ARG D 1 84  ? -9.414  8.243   -24.896 1.00 16.64 ? 84  ARG D CB  1 
ATOM   7084 C  CG  . ARG D 1 84  ? -9.715  8.045   -26.397 1.00 19.99 ? 84  ARG D CG  1 
ATOM   7085 C  CD  . ARG D 1 84  ? -11.045 8.556   -26.978 1.00 28.21 ? 84  ARG D CD  1 
ATOM   7086 N  NE  . ARG D 1 84  ? -12.145 8.106   -26.193 1.00 35.94 ? 84  ARG D NE  1 
ATOM   7087 C  CZ  . ARG D 1 84  ? -13.430 8.141   -26.585 1.00 39.46 ? 84  ARG D CZ  1 
ATOM   7088 N  NH1 . ARG D 1 84  ? -13.765 8.571   -27.806 1.00 37.99 ? 84  ARG D NH1 1 
ATOM   7089 N  NH2 . ARG D 1 84  ? -14.373 7.725   -25.735 1.00 37.85 ? 84  ARG D NH2 1 
ATOM   7090 N  N   . TYR D 1 85  ? -6.531  7.537   -26.617 1.00 11.99 ? 85  TYR D N   1 
ATOM   7091 C  CA  . TYR D 1 85  ? -5.782  8.035   -27.767 1.00 9.86  ? 85  TYR D CA  1 
ATOM   7092 C  C   . TYR D 1 85  ? -6.580  7.819   -29.025 1.00 10.92 ? 85  TYR D C   1 
ATOM   7093 O  O   . TYR D 1 85  ? -6.986  6.673   -29.289 1.00 14.64 ? 85  TYR D O   1 
ATOM   7094 C  CB  . TYR D 1 85  ? -4.473  7.314   -27.843 1.00 10.30 ? 85  TYR D CB  1 
ATOM   7095 C  CG  . TYR D 1 85  ? -3.429  7.826   -26.819 1.00 9.64  ? 85  TYR D CG  1 
ATOM   7096 C  CD1 . TYR D 1 85  ? -2.411  8.735   -27.165 1.00 9.80  ? 85  TYR D CD1 1 
ATOM   7097 C  CD2 . TYR D 1 85  ? -3.418  7.336   -25.483 1.00 9.52  ? 85  TYR D CD2 1 
ATOM   7098 C  CE1 . TYR D 1 85  ? -1.471  9.147   -26.254 1.00 9.95  ? 85  TYR D CE1 1 
ATOM   7099 C  CE2 . TYR D 1 85  ? -2.506  7.737   -24.582 1.00 9.74  ? 85  TYR D CE2 1 
ATOM   7100 C  CZ  . TYR D 1 85  ? -1.546  8.704   -24.962 1.00 10.81 ? 85  TYR D CZ  1 
ATOM   7101 O  OH  . TYR D 1 85  ? -0.604  9.143   -24.023 1.00 12.37 ? 85  TYR D OH  1 
ATOM   7102 N  N   . SER D 1 86  ? -6.608  8.846   -29.843 1.00 8.97  ? 86  SER D N   1 
ATOM   7103 C  CA  . SER D 1 86  ? -7.420  8.833   -31.076 1.00 10.72 ? 86  SER D CA  1 
ATOM   7104 C  C   . SER D 1 86  ? -6.487  8.717   -32.296 1.00 10.20 ? 86  SER D C   1 
ATOM   7105 O  O   . SER D 1 86  ? -5.393  9.321   -32.294 1.00 10.72 ? 86  SER D O   1 
ATOM   7106 C  CB  . SER D 1 86  ? -8.275  10.095  -31.250 1.00 11.66 ? 86  SER D CB  1 
ATOM   7107 O  OG  . SER D 1 86  ? -9.244  10.043  -30.162 1.00 13.85 ? 86  SER D OG  1 
ATOM   7108 N  N   . ALA D 1 87  ? -6.917  7.927   -33.284 1.00 9.99  ? 87  ALA D N   1 
ATOM   7109 C  CA  . ALA D 1 87  ? -6.030  7.735   -34.451 1.00 10.45 ? 87  ALA D CA  1 
ATOM   7110 C  C   . ALA D 1 87  ? -5.930  8.997   -35.259 1.00 9.97  ? 87  ALA D C   1 
ATOM   7111 O  O   . ALA D 1 87  ? -6.844  9.863   -35.292 1.00 11.43 ? 87  ALA D O   1 
ATOM   7112 C  CB  . ALA D 1 87  ? -6.606  6.585   -35.281 1.00 9.75  ? 87  ALA D CB  1 
ATOM   7113 N  N   . THR D 1 88  ? -4.785  9.118   -35.961 1.00 10.93 ? 88  THR D N   1 
ATOM   7114 C  CA  . THR D 1 88  ? -4.548  10.230  -36.873 1.00 10.40 ? 88  THR D CA  1 
ATOM   7115 C  C   . THR D 1 88  ? -4.071  9.778   -38.250 1.00 9.70  ? 88  THR D C   1 
ATOM   7116 O  O   . THR D 1 88  ? -4.482  10.296  -39.262 1.00 10.51 ? 88  THR D O   1 
ATOM   7117 C  CB  . THR D 1 88  ? -3.638  11.324  -36.216 1.00 12.09 ? 88  THR D CB  1 
ATOM   7118 O  OG1 . THR D 1 88  ? -3.457  12.389  -37.167 1.00 14.16 ? 88  THR D OG1 1 
ATOM   7119 C  CG2 . THR D 1 88  ? -2.279  10.831  -35.844 1.00 10.77 ? 88  THR D CG2 1 
ATOM   7120 N  N   A GLN D 1 89  ? -3.201  8.780   -38.275 0.50 10.13 ? 89  GLN D N   1 
ATOM   7121 N  N   B GLN D 1 89  ? -3.201  8.787   -38.314 0.50 10.13 ? 89  GLN D N   1 
ATOM   7122 C  CA  A GLN D 1 89  ? -2.672  8.299   -39.588 0.50 10.62 ? 89  GLN D CA  1 
ATOM   7123 C  CA  B GLN D 1 89  ? -2.694  8.304   -39.613 0.50 10.62 ? 89  GLN D CA  1 
ATOM   7124 C  C   A GLN D 1 89  ? -1.993  6.958   -39.384 0.50 8.67  ? 89  GLN D C   1 
ATOM   7125 C  C   B GLN D 1 89  ? -1.997  6.970   -39.424 0.50 8.67  ? 89  GLN D C   1 
ATOM   7126 O  O   A GLN D 1 89  ? -1.620  6.634   -38.261 0.50 9.64  ? 89  GLN D O   1 
ATOM   7127 O  O   B GLN D 1 89  ? -1.663  6.650   -38.366 0.50 9.64  ? 89  GLN D O   1 
ATOM   7128 C  CB  A GLN D 1 89  ? -1.677  9.323   -40.213 0.50 10.43 ? 89  GLN D CB  1 
ATOM   7129 C  CB  B GLN D 1 89  ? -1.696  9.325   -40.213 0.50 10.43 ? 89  GLN D CB  1 
ATOM   7130 C  CG  A GLN D 1 89  ? -0.463  9.567   -39.339 0.50 15.26 ? 89  GLN D CG  1 
ATOM   7131 C  CG  B GLN D 1 89  ? -0.405  9.460   -39.400 0.50 15.26 ? 89  GLN D CG  1 
ATOM   7132 C  CD  A GLN D 1 89  ? 0.755   9.005   -40.002 0.50 18.02 ? 89  GLN D CD  1 
ATOM   7133 C  CD  B GLN D 1 89  ? 0.777   10.032  -40.158 0.50 18.02 ? 89  GLN D CD  1 
ATOM   7134 O  OE1 A GLN D 1 89  ? 1.055   7.818   -40.011 0.50 18.52 ? 89  GLN D OE1 1 
ATOM   7135 O  OE1 B GLN D 1 89  ? 0.920   11.227  -40.223 0.50 18.52 ? 89  GLN D OE1 1 
ATOM   7136 N  NE2 A GLN D 1 89  ? 1.546   9.883   -40.467 0.50 22.70 ? 89  GLN D NE2 1 
ATOM   7137 N  NE2 B GLN D 1 89  ? 1.552   9.251   -40.664 0.50 22.70 ? 89  GLN D NE2 1 
ATOM   7138 N  N   . LEU D 1 90  ? -1.842  6.198   -40.490 1.00 8.26  ? 90  LEU D N   1 
ATOM   7139 C  CA  . LEU D 1 90  ? -0.895  5.115   -40.481 1.00 8.58  ? 90  LEU D CA  1 
ATOM   7140 C  C   . LEU D 1 90  ? 0.097   5.327   -41.639 1.00 8.56  ? 90  LEU D C   1 
ATOM   7141 O  O   . LEU D 1 90  ? -0.196  6.006   -42.608 1.00 8.91  ? 90  LEU D O   1 
ATOM   7142 C  CB  . LEU D 1 90  ? -1.550  3.726   -40.511 1.00 9.19  ? 90  LEU D CB  1 
ATOM   7143 C  CG  . LEU D 1 90  ? -2.549  3.358   -41.614 1.00 8.35  ? 90  LEU D CG  1 
ATOM   7144 C  CD1 . LEU D 1 90  ? -1.820  3.064   -42.920 1.00 8.92  ? 90  LEU D CD1 1 
ATOM   7145 C  CD2 . LEU D 1 90  ? -3.427  2.190   -41.164 1.00 10.03 ? 90  LEU D CD2 1 
ATOM   7146 N  N   . HIS D 1 91  ? 1.278   4.693   -41.508 1.00 8.29  ? 91  HIS D N   1 
ATOM   7147 C  CA  . HIS D 1 91  ? 2.287   4.812   -42.576 1.00 8.52  ? 91  HIS D CA  1 
ATOM   7148 C  C   . HIS D 1 91  ? 3.257   3.685   -42.408 1.00 8.37  ? 91  HIS D C   1 
ATOM   7149 O  O   . HIS D 1 91  ? 3.108   2.878   -41.480 1.00 7.72  ? 91  HIS D O   1 
ATOM   7150 C  CB  . HIS D 1 91  ? 3.045   6.110   -42.506 1.00 9.12  ? 91  HIS D CB  1 
ATOM   7151 C  CG  . HIS D 1 91  ? 3.794   6.268   -41.224 1.00 8.56  ? 91  HIS D CG  1 
ATOM   7152 N  ND1 . HIS D 1 91  ? 3.315   7.085   -40.237 1.00 10.00 ? 91  HIS D ND1 1 
ATOM   7153 C  CD2 . HIS D 1 91  ? 4.957   5.653   -40.739 1.00 8.88  ? 91  HIS D CD2 1 
ATOM   7154 C  CE1 . HIS D 1 91  ? 4.161   7.023   -39.189 1.00 8.30  ? 91  HIS D CE1 1 
ATOM   7155 N  NE2 . HIS D 1 91  ? 5.159   6.140   -39.488 1.00 8.21  ? 91  HIS D NE2 1 
ATOM   7156 N  N   . LEU D 1 92  ? 4.215   3.537   -43.335 1.00 8.73  ? 92  LEU D N   1 
ATOM   7157 C  CA  . LEU D 1 92  ? 5.139   2.391   -43.305 1.00 8.45  ? 92  LEU D CA  1 
ATOM   7158 C  C   . LEU D 1 92  ? 6.579   2.839   -43.431 1.00 8.30  ? 92  LEU D C   1 
ATOM   7159 O  O   . LEU D 1 92  ? 6.905   3.958   -43.812 1.00 9.48  ? 92  LEU D O   1 
ATOM   7160 C  CB  . LEU D 1 92  ? 4.846   1.439   -44.453 1.00 10.00 ? 92  LEU D CB  1 
ATOM   7161 C  CG  . LEU D 1 92  ? 3.428   0.756   -44.264 1.00 11.45 ? 92  LEU D CG  1 
ATOM   7162 C  CD1 . LEU D 1 92  ? 2.477   1.306   -45.276 1.00 14.64 ? 92  LEU D CD1 1 
ATOM   7163 C  CD2 . LEU D 1 92  ? 3.577   -0.742  -44.327 1.00 13.07 ? 92  LEU D CD2 1 
ATOM   7164 N  N   . HIS D 1 93  ? 7.451   1.916   -43.109 1.00 8.18  ? 93  HIS D N   1 
ATOM   7165 C  CA  . HIS D 1 93  ? 8.950   2.087   -43.242 1.00 7.55  ? 93  HIS D CA  1 
ATOM   7166 C  C   . HIS D 1 93  ? 9.443   0.816   -43.865 1.00 7.50  ? 93  HIS D C   1 
ATOM   7167 O  O   . HIS D 1 93  ? 8.954   -0.292  -43.514 1.00 8.02  ? 93  HIS D O   1 
ATOM   7168 C  CB  . HIS D 1 93  ? 9.597   2.303   -41.841 1.00 7.81  ? 93  HIS D CB  1 
ATOM   7169 C  CG  . HIS D 1 93  ? 9.111   3.481   -41.105 1.00 8.15  ? 93  HIS D CG  1 
ATOM   7170 N  ND1 . HIS D 1 93  ? 9.739   4.687   -41.216 1.00 7.29  ? 93  HIS D ND1 1 
ATOM   7171 C  CD2 . HIS D 1 93  ? 8.025   3.677   -40.243 1.00 7.46  ? 93  HIS D CD2 1 
ATOM   7172 C  CE1 . HIS D 1 93  ? 9.095   5.611   -40.461 1.00 7.76  ? 93  HIS D CE1 1 
ATOM   7173 N  NE2 . HIS D 1 93  ? 8.081   5.005   -39.828 1.00 7.38  ? 93  HIS D NE2 1 
ATOM   7174 N  N   . TRP D 1 94  ? 10.395  0.938   -44.833 1.00 7.13  ? 94  TRP D N   1 
ATOM   7175 C  CA  . TRP D 1 94  ? 10.876  -0.270  -45.611 1.00 6.86  ? 94  TRP D CA  1 
ATOM   7176 C  C   . TRP D 1 94  ? 12.325  -0.065  -46.051 1.00 7.92  ? 94  TRP D C   1 
ATOM   7177 O  O   . TRP D 1 94  ? 12.938  1.003   -45.805 1.00 9.11  ? 94  TRP D O   1 
ATOM   7178 C  CB  . TRP D 1 94  ? 9.909   -0.568  -46.734 1.00 7.52  ? 94  TRP D CB  1 
ATOM   7179 C  CG  . TRP D 1 94  ? 9.814   0.626   -47.714 1.00 8.13  ? 94  TRP D CG  1 
ATOM   7180 C  CD1 . TRP D 1 94  ? 10.624  0.871   -48.821 1.00 8.95  ? 94  TRP D CD1 1 
ATOM   7181 C  CD2 . TRP D 1 94  ? 8.788   1.674   -47.698 1.00 8.05  ? 94  TRP D CD2 1 
ATOM   7182 N  NE1 . TRP D 1 94  ? 10.214  2.008   -49.465 1.00 8.16  ? 94  TRP D NE1 1 
ATOM   7183 C  CE2 . TRP D 1 94  ? 9.064   2.521   -48.832 1.00 8.08  ? 94  TRP D CE2 1 
ATOM   7184 C  CE3 . TRP D 1 94  ? 7.655   1.984   -46.873 1.00 8.93  ? 94  TRP D CE3 1 
ATOM   7185 C  CZ2 . TRP D 1 94  ? 8.258   3.626   -49.147 1.00 9.27  ? 94  TRP D CZ2 1 
ATOM   7186 C  CZ3 . TRP D 1 94  ? 6.877   3.097   -47.188 1.00 8.88  ? 94  TRP D CZ3 1 
ATOM   7187 C  CH2 . TRP D 1 94  ? 7.175   3.932   -48.300 1.00 8.66  ? 94  TRP D CH2 1 
ATOM   7188 N  N   . GLY D 1 95  ? 12.831  -1.147  -46.647 1.00 9.35  ? 95  GLY D N   1 
ATOM   7189 C  CA  . GLY D 1 95  ? 14.278  -1.121  -47.116 1.00 8.92  ? 95  GLY D CA  1 
ATOM   7190 C  C   . GLY D 1 95  ? 14.307  -0.913  -48.639 1.00 9.23  ? 95  GLY D C   1 
ATOM   7191 O  O   . GLY D 1 95  ? 13.803  0.085   -49.203 1.00 8.70  ? 95  GLY D O   1 
ATOM   7192 N  N   . ASN D 1 96  ? 14.873  -1.927  -49.353 1.00 9.60  ? 96  ASN D N   1 
ATOM   7193 C  CA  . ASN D 1 96  ? 14.963  -1.714  -50.821 1.00 13.20 ? 96  ASN D CA  1 
ATOM   7194 C  C   . ASN D 1 96  ? 15.066  -3.093  -51.431 1.00 13.86 ? 96  ASN D C   1 
ATOM   7195 O  O   . ASN D 1 96  ? 15.178  -4.085  -50.707 1.00 14.40 ? 96  ASN D O   1 
ATOM   7196 C  CB  . ASN D 1 96  ? 16.186  -0.806  -51.158 1.00 13.01 ? 96  ASN D CB  1 
ATOM   7197 C  CG  . ASN D 1 96  ? 17.483  -1.521  -50.924 1.00 16.39 ? 96  ASN D CG  1 
ATOM   7198 O  OD1 . ASN D 1 96  ? 17.914  -2.241  -51.828 1.00 23.05 ? 96  ASN D OD1 1 
ATOM   7199 N  ND2 . ASN D 1 96  ? 18.133  -1.304  -49.783 1.00 16.66 ? 96  ASN D ND2 1 
ATOM   7200 N  N   . PRO D 1 97  ? 14.963  -3.207  -52.784 1.00 16.21 ? 97  PRO D N   1 
ATOM   7201 C  CA  . PRO D 1 97  ? 14.975  -4.584  -53.374 1.00 19.44 ? 97  PRO D CA  1 
ATOM   7202 C  C   . PRO D 1 97  ? 16.262  -5.329  -53.087 1.00 20.97 ? 97  PRO D C   1 
ATOM   7203 O  O   . PRO D 1 97  ? 16.195  -6.541  -52.880 1.00 22.95 ? 97  PRO D O   1 
ATOM   7204 C  CB  . PRO D 1 97  ? 14.697  -4.351  -54.850 1.00 20.27 ? 97  PRO D CB  1 
ATOM   7205 C  CG  . PRO D 1 97  ? 14.167  -2.962  -54.944 1.00 20.77 ? 97  PRO D CG  1 
ATOM   7206 C  CD  . PRO D 1 97  ? 14.625  -2.180  -53.748 1.00 17.93 ? 97  PRO D CD  1 
ATOM   7207 N  N   . ASN D 1 98  ? 17.389  -4.639  -52.902 1.00 20.34 ? 98  ASN D N   1 
ATOM   7208 C  CA  . ASN D 1 98  ? 18.643  -5.317  -52.571 1.00 24.80 ? 98  ASN D CA  1 
ATOM   7209 C  C   . ASN D 1 98  ? 18.851  -5.628  -51.093 1.00 24.25 ? 98  ASN D C   1 
ATOM   7210 O  O   . ASN D 1 98  ? 19.837  -6.265  -50.709 1.00 26.59 ? 98  ASN D O   1 
ATOM   7211 C  CB  . ASN D 1 98  ? 19.812  -4.518  -53.116 1.00 25.06 ? 98  ASN D CB  1 
ATOM   7212 C  CG  . ASN D 1 98  ? 19.731  -4.363  -54.620 1.00 33.57 ? 98  ASN D CG  1 
ATOM   7213 O  OD1 . ASN D 1 98  ? 19.178  -5.232  -55.329 1.00 40.26 ? 98  ASN D OD1 1 
ATOM   7214 N  ND2 . ASN D 1 98  ? 20.238  -3.238  -55.123 1.00 39.32 ? 98  ASN D ND2 1 
ATOM   7215 N  N   . ASP D 1 99  ? 17.978  -5.092  -50.235 1.00 19.51 ? 99  ASP D N   1 
ATOM   7216 C  CA  . ASP D 1 99  ? 18.107  -5.320  -48.813 1.00 18.58 ? 99  ASP D CA  1 
ATOM   7217 C  C   . ASP D 1 99  ? 16.707  -5.118  -48.218 1.00 15.21 ? 99  ASP D C   1 
ATOM   7218 O  O   . ASP D 1 99  ? 16.364  -3.999  -47.746 1.00 13.84 ? 99  ASP D O   1 
ATOM   7219 C  CB  . ASP D 1 99  ? 19.149  -4.348  -48.210 1.00 22.36 ? 99  ASP D CB  1 
ATOM   7220 C  CG  . ASP D 1 99  ? 19.271  -4.487  -46.680 1.00 25.78 ? 99  ASP D CG  1 
ATOM   7221 O  OD1 . ASP D 1 99  ? 18.913  -5.609  -46.209 1.00 24.14 ? 99  ASP D OD1 1 
ATOM   7222 O  OD2 . ASP D 1 99  ? 19.658  -3.492  -45.985 1.00 28.40 ? 99  ASP D OD2 1 
ATOM   7223 N  N   . PRO D 1 100 ? 15.848  -6.110  -48.300 1.00 14.17 ? 100 PRO D N   1 
ATOM   7224 C  CA  . PRO D 1 100 ? 14.384  -5.963  -47.931 1.00 14.39 ? 100 PRO D CA  1 
ATOM   7225 C  C   . PRO D 1 100 ? 14.289  -6.192  -46.419 1.00 13.58 ? 100 PRO D C   1 
ATOM   7226 O  O   . PRO D 1 100 ? 13.674  -7.150  -45.932 1.00 14.04 ? 100 PRO D O   1 
ATOM   7227 C  CB  . PRO D 1 100 ? 13.705  -7.055  -48.739 1.00 14.81 ? 100 PRO D CB  1 
ATOM   7228 C  CG  . PRO D 1 100 ? 14.815  -8.063  -48.904 1.00 16.67 ? 100 PRO D CG  1 
ATOM   7229 C  CD  . PRO D 1 100 ? 16.136  -7.405  -48.959 1.00 16.48 ? 100 PRO D CD  1 
ATOM   7230 N  N   . HIS D 1 101 ? 15.002  -5.346  -45.696 1.00 13.18 ? 101 HIS D N   1 
ATOM   7231 C  CA  . HIS D 1 101 ? 15.130  -5.446  -44.193 1.00 12.15 ? 101 HIS D CA  1 
ATOM   7232 C  C   . HIS D 1 101 ? 15.063  -4.100  -43.551 1.00 11.79 ? 101 HIS D C   1 
ATOM   7233 O  O   . HIS D 1 101 ? 16.033  -3.604  -42.924 1.00 15.62 ? 101 HIS D O   1 
ATOM   7234 C  CB  . HIS D 1 101 ? 16.420  -6.160  -43.795 1.00 14.19 ? 101 HIS D CB  1 
ATOM   7235 C  CG  . HIS D 1 101 ? 16.486  -7.560  -44.374 1.00 19.74 ? 101 HIS D CG  1 
ATOM   7236 N  ND1 . HIS D 1 101 ? 15.843  -8.634  -43.827 1.00 21.00 ? 101 HIS D ND1 1 
ATOM   7237 C  CD2 . HIS D 1 101 ? 17.048  -8.008  -45.576 1.00 19.08 ? 101 HIS D CD2 1 
ATOM   7238 C  CE1 . HIS D 1 101 ? 16.002  -9.713  -44.628 1.00 22.77 ? 101 HIS D CE1 1 
ATOM   7239 N  NE2 . HIS D 1 101 ? 16.741  -9.339  -45.694 1.00 24.72 ? 101 HIS D NE2 1 
ATOM   7240 N  N   . GLY D 1 102 ? 13.904  -3.475  -43.708 1.00 9.73  ? 102 GLY D N   1 
ATOM   7241 C  CA  . GLY D 1 102 ? 13.758  -2.062  -43.392 1.00 8.75  ? 102 GLY D CA  1 
ATOM   7242 C  C   . GLY D 1 102 ? 12.840  -1.765  -42.242 1.00 8.80  ? 102 GLY D C   1 
ATOM   7243 O  O   . GLY D 1 102 ? 12.359  -0.670  -42.153 1.00 9.68  ? 102 GLY D O   1 
ATOM   7244 N  N   . SER D 1 103 ? 12.534  -2.734  -41.367 1.00 8.95  ? 103 SER D N   1 
ATOM   7245 C  CA  . SER D 1 103 ? 11.794  -2.342  -40.141 1.00 8.95  ? 103 SER D CA  1 
ATOM   7246 C  C   . SER D 1 103 ? 12.618  -1.323  -39.294 1.00 8.81  ? 103 SER D C   1 
ATOM   7247 O  O   . SER D 1 103 ? 13.871  -1.334  -39.392 1.00 8.60  ? 103 SER D O   1 
ATOM   7248 C  CB  . SER D 1 103 ? 11.457  -3.588  -39.297 1.00 9.90  ? 103 SER D CB  1 
ATOM   7249 O  OG  . SER D 1 103 ? 12.663  -4.176  -38.663 1.00 9.10  ? 103 SER D OG  1 
ATOM   7250 N  N   . GLU D 1 104 ? 11.936  -0.572  -38.440 1.00 8.44  ? 104 GLU D N   1 
ATOM   7251 C  CA  . GLU D 1 104 ? 12.634  0.384   -37.582 1.00 9.53  ? 104 GLU D CA  1 
ATOM   7252 C  C   . GLU D 1 104 ? 13.069  -0.388  -36.350 1.00 8.22  ? 104 GLU D C   1 
ATOM   7253 O  O   . GLU D 1 104 ? 14.260  -0.419  -35.983 1.00 9.43  ? 104 GLU D O   1 
ATOM   7254 C  CB  . GLU D 1 104 ? 11.678  1.524   -37.239 1.00 8.81  ? 104 GLU D CB  1 
ATOM   7255 C  CG  . GLU D 1 104 ? 11.298  2.261   -38.513 1.00 8.96  ? 104 GLU D CG  1 
ATOM   7256 C  CD  . GLU D 1 104 ? 11.276  3.741   -38.232 1.00 8.90  ? 104 GLU D CD  1 
ATOM   7257 O  OE1 . GLU D 1 104 ? 10.299  4.201   -37.655 1.00 10.18 ? 104 GLU D OE1 1 
ATOM   7258 O  OE2 . GLU D 1 104 ? 12.229  4.420   -38.647 1.00 9.03  ? 104 GLU D OE2 1 
ATOM   7259 N  N   . HIS D 1 105 ? 12.102  -0.987  -35.622 1.00 8.55  ? 105 HIS D N   1 
ATOM   7260 C  CA  . HIS D 1 105 ? 12.484  -1.821  -34.478 1.00 8.33  ? 105 HIS D CA  1 
ATOM   7261 C  C   . HIS D 1 105 ? 13.105  -3.096  -34.962 1.00 8.71  ? 105 HIS D C   1 
ATOM   7262 O  O   . HIS D 1 105 ? 12.727  -3.650  -36.017 1.00 9.64  ? 105 HIS D O   1 
ATOM   7263 C  CB  . HIS D 1 105 ? 11.215  -2.117  -33.605 1.00 7.63  ? 105 HIS D CB  1 
ATOM   7264 C  CG  . HIS D 1 105 ? 10.715  -0.873  -32.923 1.00 8.45  ? 105 HIS D CG  1 
ATOM   7265 N  ND1 . HIS D 1 105 ? 9.796   -0.052  -33.481 1.00 8.38  ? 105 HIS D ND1 1 
ATOM   7266 C  CD2 . HIS D 1 105 ? 11.069  -0.315  -31.686 1.00 7.92  ? 105 HIS D CD2 1 
ATOM   7267 C  CE1 . HIS D 1 105 ? 9.632   1.033   -32.670 1.00 8.38  ? 105 HIS D CE1 1 
ATOM   7268 N  NE2 . HIS D 1 105 ? 10.367  0.867   -31.555 1.00 8.34  ? 105 HIS D NE2 1 
ATOM   7269 N  N   . THR D 1 106 ? 14.000  -3.637  -34.183 1.00 9.13  ? 106 THR D N   1 
ATOM   7270 C  CA  . THR D 1 106 ? 14.594  -4.937  -34.495 1.00 9.89  ? 106 THR D CA  1 
ATOM   7271 C  C   . THR D 1 106 ? 14.336  -5.869  -33.305 1.00 9.61  ? 106 THR D C   1 
ATOM   7272 O  O   . THR D 1 106 ? 14.048  -5.429  -32.213 1.00 9.37  ? 106 THR D O   1 
ATOM   7273 C  CB  . THR D 1 106 ? 16.119  -4.802  -34.822 1.00 10.31 ? 106 THR D CB  1 
ATOM   7274 O  OG1 . THR D 1 106 ? 16.823  -4.165  -33.721 1.00 12.67 ? 106 THR D OG1 1 
ATOM   7275 C  CG2 . THR D 1 106 ? 16.344  -3.939  -36.046 1.00 11.86 ? 106 THR D CG2 1 
ATOM   7276 N  N   . VAL D 1 107 ? 14.440  -7.194  -33.553 1.00 10.47 ? 107 VAL D N   1 
ATOM   7277 C  CA  . VAL D 1 107 ? 14.242  -8.142  -32.473 1.00 11.38 ? 107 VAL D CA  1 
ATOM   7278 C  C   . VAL D 1 107 ? 15.449  -9.046  -32.465 1.00 12.37 ? 107 VAL D C   1 
ATOM   7279 O  O   . VAL D 1 107 ? 15.760  -9.662  -33.459 1.00 13.18 ? 107 VAL D O   1 
ATOM   7280 C  CB  . VAL D 1 107 ? 12.946  -9.002  -32.640 1.00 10.54 ? 107 VAL D CB  1 
ATOM   7281 C  CG1 . VAL D 1 107 ? 12.878  -10.023 -31.506 1.00 11.01 ? 107 VAL D CG1 1 
ATOM   7282 C  CG2 . VAL D 1 107 ? 11.668  -8.091  -32.642 1.00 12.91 ? 107 VAL D CG2 1 
ATOM   7283 N  N   . SER D 1 108 ? 16.082  -9.109  -31.305 1.00 12.74 ? 108 SER D N   1 
ATOM   7284 C  CA  . SER D 1 108 ? 17.353  -9.885  -31.123 1.00 13.52 ? 108 SER D CA  1 
ATOM   7285 C  C   . SER D 1 108 ? 18.322  -9.552  -32.277 1.00 14.05 ? 108 SER D C   1 
ATOM   7286 O  O   . SER D 1 108 ? 18.927  -10.430 -32.850 1.00 15.02 ? 108 SER D O   1 
ATOM   7287 C  CB  . SER D 1 108 ? 17.043  -11.389 -30.986 1.00 14.08 ? 108 SER D CB  1 
ATOM   7288 O  OG  . SER D 1 108 ? 16.249  -11.490 -29.797 1.00 18.19 ? 108 SER D OG  1 
ATOM   7289 N  N   . GLY D 1 109 ? 18.385  -8.259  -32.614 1.00 12.64 ? 109 GLY D N   1 
ATOM   7290 C  CA  . GLY D 1 109 ? 19.300  -7.679  -33.607 1.00 13.63 ? 109 GLY D CA  1 
ATOM   7291 C  C   . GLY D 1 109 ? 18.913  -7.887  -35.083 1.00 15.27 ? 109 GLY D C   1 
ATOM   7292 O  O   . GLY D 1 109 ? 19.688  -7.569  -35.989 1.00 19.03 ? 109 GLY D O   1 
ATOM   7293 N  N   A GLN D 1 110 ? 17.719  -8.400  -35.333 0.50 13.44 ? 110 GLN D N   1 
ATOM   7294 N  N   B GLN D 1 110 ? 17.708  -8.357  -35.327 0.50 14.20 ? 110 GLN D N   1 
ATOM   7295 C  CA  A GLN D 1 110 ? 17.332  -8.718  -36.701 0.50 14.48 ? 110 GLN D CA  1 
ATOM   7296 C  CA  B GLN D 1 110 ? 17.342  -8.654  -36.689 0.50 15.91 ? 110 GLN D CA  1 
ATOM   7297 C  C   A GLN D 1 110 ? 16.238  -7.761  -37.124 0.50 12.05 ? 110 GLN D C   1 
ATOM   7298 C  C   B GLN D 1 110 ? 16.236  -7.737  -37.117 0.50 12.77 ? 110 GLN D C   1 
ATOM   7299 O  O   A GLN D 1 110 ? 15.267  -7.569  -36.377 0.50 10.93 ? 110 GLN D O   1 
ATOM   7300 O  O   B GLN D 1 110 ? 15.256  -7.556  -36.378 0.50 11.47 ? 110 GLN D O   1 
ATOM   7301 C  CB  A GLN D 1 110 ? 16.780  -10.143 -36.808 0.50 14.16 ? 110 GLN D CB  1 
ATOM   7302 C  CB  B GLN D 1 110 ? 16.843  -10.079 -36.784 0.50 17.08 ? 110 GLN D CB  1 
ATOM   7303 C  CG  A GLN D 1 110 ? 17.646  -11.256 -36.181 0.50 15.79 ? 110 GLN D CG  1 
ATOM   7304 C  CG  B GLN D 1 110 ? 17.651  -11.056 -35.933 0.50 21.42 ? 110 GLN D CG  1 
ATOM   7305 C  CD  A GLN D 1 110 ? 19.070  -11.234 -36.687 0.50 16.81 ? 110 GLN D CD  1 
ATOM   7306 C  CD  B GLN D 1 110 ? 17.378  -12.482 -36.311 0.50 24.44 ? 110 GLN D CD  1 
ATOM   7307 O  OE1 A GLN D 1 110 ? 20.023  -11.031 -35.903 0.50 18.71 ? 110 GLN D OE1 1 
ATOM   7308 O  OE1 B GLN D 1 110 ? 16.884  -13.279 -35.498 0.50 31.82 ? 110 GLN D OE1 1 
ATOM   7309 N  NE2 A GLN D 1 110 ? 19.234  -11.408 -37.982 0.50 16.80 ? 110 GLN D NE2 1 
ATOM   7310 N  NE2 B GLN D 1 110 ? 17.686  -12.818 -37.547 0.50 23.28 ? 110 GLN D NE2 1 
ATOM   7311 N  N   . HIS D 1 111 ? 16.397  -7.156  -38.307 1.00 12.55 ? 111 HIS D N   1 
ATOM   7312 C  CA  . HIS D 1 111 ? 15.317  -6.398  -38.946 1.00 12.70 ? 111 HIS D CA  1 
ATOM   7313 C  C   . HIS D 1 111 ? 14.303  -7.352  -39.515 1.00 12.92 ? 111 HIS D C   1 
ATOM   7314 O  O   . HIS D 1 111 ? 14.594  -8.485  -39.935 1.00 16.27 ? 111 HIS D O   1 
ATOM   7315 C  CB  . HIS D 1 111 ? 15.752  -5.586  -40.139 1.00 13.66 ? 111 HIS D CB  1 
ATOM   7316 C  CG  . HIS D 1 111 ? 16.500  -4.354  -39.777 1.00 11.12 ? 111 HIS D CG  1 
ATOM   7317 N  ND1 . HIS D 1 111 ? 15.899  -3.126  -39.574 1.00 14.12 ? 111 HIS D ND1 1 
ATOM   7318 C  CD2 . HIS D 1 111 ? 17.857  -4.161  -39.587 1.00 13.02 ? 111 HIS D CD2 1 
ATOM   7319 C  CE1 . HIS D 1 111 ? 16.827  -2.223  -39.269 1.00 13.86 ? 111 HIS D CE1 1 
ATOM   7320 N  NE2 . HIS D 1 111 ? 18.028  -2.824  -39.287 1.00 14.93 ? 111 HIS D NE2 1 
ATOM   7321 N  N   . PHE D 1 112 ? 13.059  -6.909  -39.485 1.00 10.43 ? 112 PHE D N   1 
ATOM   7322 C  CA  . PHE D 1 112 ? 12.033  -7.488  -40.313 1.00 10.51 ? 112 PHE D CA  1 
ATOM   7323 C  C   . PHE D 1 112 ? 12.012  -6.709  -41.636 1.00 8.88  ? 112 PHE D C   1 
ATOM   7324 O  O   . PHE D 1 112 ? 12.738  -5.696  -41.800 1.00 10.91 ? 112 PHE D O   1 
ATOM   7325 C  CB  . PHE D 1 112 ? 10.663  -7.415  -39.551 1.00 11.56 ? 112 PHE D CB  1 
ATOM   7326 C  CG  . PHE D 1 112 ? 10.540  -8.435  -38.463 1.00 13.58 ? 112 PHE D CG  1 
ATOM   7327 C  CD1 . PHE D 1 112 ? 9.854   -9.596  -38.769 1.00 16.70 ? 112 PHE D CD1 1 
ATOM   7328 C  CD2 . PHE D 1 112 ? 11.195  -8.292  -37.231 1.00 16.82 ? 112 PHE D CD2 1 
ATOM   7329 C  CE1 . PHE D 1 112 ? 9.699   -10.593 -37.820 1.00 17.72 ? 112 PHE D CE1 1 
ATOM   7330 C  CE2 . PHE D 1 112 ? 11.057  -9.329  -36.285 1.00 18.24 ? 112 PHE D CE2 1 
ATOM   7331 C  CZ  . PHE D 1 112 ? 10.324  -10.423 -36.594 1.00 18.32 ? 112 PHE D CZ  1 
ATOM   7332 N  N   . ALA D 1 113 ? 11.165  -7.194  -42.591 1.00 8.73  ? 113 ALA D N   1 
ATOM   7333 C  CA  . ALA D 1 113 ? 11.162  -6.574  -43.905 1.00 9.73  ? 113 ALA D CA  1 
ATOM   7334 C  C   . ALA D 1 113 ? 10.720  -5.148  -43.874 1.00 8.95  ? 113 ALA D C   1 
ATOM   7335 O  O   . ALA D 1 113 ? 11.205  -4.322  -44.671 1.00 10.16 ? 113 ALA D O   1 
ATOM   7336 C  CB  . ALA D 1 113 ? 10.270  -7.388  -44.882 1.00 10.73 ? 113 ALA D CB  1 
ATOM   7337 N  N   . ALA D 1 114 ? 9.661   -4.887  -43.090 1.00 8.41  ? 114 ALA D N   1 
ATOM   7338 C  CA  . ALA D 1 114 ? 9.075   -3.515  -43.123 1.00 8.03  ? 114 ALA D CA  1 
ATOM   7339 C  C   . ALA D 1 114 ? 8.304   -3.364  -41.787 1.00 8.72  ? 114 ALA D C   1 
ATOM   7340 O  O   . ALA D 1 114 ? 8.322   -4.271  -40.938 1.00 9.43  ? 114 ALA D O   1 
ATOM   7341 C  CB  . ALA D 1 114 ? 8.087   -3.394  -44.325 1.00 8.17  ? 114 ALA D CB  1 
ATOM   7342 N  N   . GLU D 1 115 ? 7.719   -2.194  -41.577 1.00 8.19  ? 115 GLU D N   1 
ATOM   7343 C  CA  . GLU D 1 115 ? 7.031   -1.911  -40.300 1.00 8.36  ? 115 GLU D CA  1 
ATOM   7344 C  C   . GLU D 1 115 ? 5.910   -0.946  -40.570 1.00 8.80  ? 115 GLU D C   1 
ATOM   7345 O  O   . GLU D 1 115 ? 6.070   0.034   -41.279 1.00 9.56  ? 115 GLU D O   1 
ATOM   7346 C  CB  . GLU D 1 115 ? 8.024   -1.295  -39.280 1.00 8.23  ? 115 GLU D CB  1 
ATOM   7347 C  CG  . GLU D 1 115 ? 7.475   -1.108  -37.866 1.00 9.29  ? 115 GLU D CG  1 
ATOM   7348 C  CD  . GLU D 1 115 ? 8.603   -0.934  -36.840 1.00 9.58  ? 115 GLU D CD  1 
ATOM   7349 O  OE1 . GLU D 1 115 ? 9.722   -1.440  -37.027 1.00 9.41  ? 115 GLU D OE1 1 
ATOM   7350 O  OE2 . GLU D 1 115 ? 8.302   -0.244  -35.796 1.00 10.96 ? 115 GLU D OE2 1 
ATOM   7351 N  N   . LEU D 1 116 ? 4.738   -1.265  -40.030 1.00 7.45  ? 116 LEU D N   1 
ATOM   7352 C  CA  . LEU D 1 116 ? 3.562   -0.381  -40.057 1.00 8.16  ? 116 LEU D CA  1 
ATOM   7353 C  C   . LEU D 1 116 ? 3.424   0.328   -38.723 1.00 8.29  ? 116 LEU D C   1 
ATOM   7354 O  O   . LEU D 1 116 ? 3.549   -0.310  -37.649 1.00 8.81  ? 116 LEU D O   1 
ATOM   7355 C  CB  . LEU D 1 116 ? 2.318   -1.299  -40.168 1.00 8.83  ? 116 LEU D CB  1 
ATOM   7356 C  CG  . LEU D 1 116 ? 1.016   -0.483  -40.085 1.00 8.89  ? 116 LEU D CG  1 
ATOM   7357 C  CD1 . LEU D 1 116 ? 0.742   0.334   -41.365 1.00 10.55 ? 116 LEU D CD1 1 
ATOM   7358 C  CD2 . LEU D 1 116 ? -0.151  -1.461  -39.815 1.00 10.78 ? 116 LEU D CD2 1 
ATOM   7359 N  N   . HIS D 1 117 ? 3.245   1.640   -38.798 1.00 8.19  ? 117 HIS D N   1 
ATOM   7360 C  CA  . HIS D 1 117 ? 2.897   2.477   -37.604 1.00 8.01  ? 117 HIS D CA  1 
ATOM   7361 C  C   . HIS D 1 117 ? 1.538   3.052   -37.716 1.00 8.03  ? 117 HIS D C   1 
ATOM   7362 O  O   . HIS D 1 117 ? 1.175   3.699   -38.718 1.00 9.02  ? 117 HIS D O   1 
ATOM   7363 C  CB  . HIS D 1 117 ? 3.895   3.601   -37.490 1.00 9.09  ? 117 HIS D CB  1 
ATOM   7364 C  CG  . HIS D 1 117 ? 5.275   3.130   -37.155 1.00 8.19  ? 117 HIS D CG  1 
ATOM   7365 N  ND1 . HIS D 1 117 ? 6.400   3.892   -37.435 1.00 8.85  ? 117 HIS D ND1 1 
ATOM   7366 C  CD2 . HIS D 1 117 ? 5.709   1.958   -36.531 1.00 9.22  ? 117 HIS D CD2 1 
ATOM   7367 C  CE1 . HIS D 1 117 ? 7.513   3.191   -36.986 1.00 8.85  ? 117 HIS D CE1 1 
ATOM   7368 N  NE2 . HIS D 1 117 ? 7.082   2.018   -36.454 1.00 7.74  ? 117 HIS D NE2 1 
ATOM   7369 N  N   . ILE D 1 118 ? 0.730   2.800   -36.684 1.00 9.16  ? 118 ILE D N   1 
ATOM   7370 C  CA  . ILE D 1 118 ? -0.606  3.445   -36.568 1.00 8.61  ? 118 ILE D CA  1 
ATOM   7371 C  C   . ILE D 1 118 ? -0.468  4.490   -35.470 1.00 8.43  ? 118 ILE D C   1 
ATOM   7372 O  O   . ILE D 1 118 ? -0.335  4.140   -34.277 1.00 9.74  ? 118 ILE D O   1 
ATOM   7373 C  CB  . ILE D 1 118 ? -1.693  2.395   -36.253 1.00 8.82  ? 118 ILE D CB  1 
ATOM   7374 C  CG1 . ILE D 1 118 ? -1.609  1.232   -37.272 1.00 10.07 ? 118 ILE D CG1 1 
ATOM   7375 C  CG2 . ILE D 1 118 ? -3.078  3.078   -36.355 1.00 8.68  ? 118 ILE D CG2 1 
ATOM   7376 C  CD1 . ILE D 1 118 ? -2.683  0.153   -36.971 1.00 11.26 ? 118 ILE D CD1 1 
ATOM   7377 N  N   . VAL D 1 119 ? -0.511  5.778   -35.856 1.00 8.13  ? 119 VAL D N   1 
ATOM   7378 C  CA  . VAL D 1 119 ? -0.246  6.836   -34.937 1.00 8.63  ? 119 VAL D CA  1 
ATOM   7379 C  C   . VAL D 1 119 ? -1.577  7.347   -34.349 1.00 8.91  ? 119 VAL D C   1 
ATOM   7380 O  O   . VAL D 1 119 ? -2.537  7.586   -35.079 1.00 8.82  ? 119 VAL D O   1 
ATOM   7381 C  CB  . VAL D 1 119 ? 0.397   7.995   -35.731 1.00 7.93  ? 119 VAL D CB  1 
ATOM   7382 C  CG1 . VAL D 1 119 ? 0.746   9.195   -34.825 1.00 9.68  ? 119 VAL D CG1 1 
ATOM   7383 C  CG2 . VAL D 1 119 ? 1.690   7.577   -36.483 1.00 7.88  ? 119 VAL D CG2 1 
ATOM   7384 N  N   . HIS D 1 120 ? -1.559  7.572   -33.021 1.00 9.39  ? 120 HIS D N   1 
ATOM   7385 C  CA  . HIS D 1 120 ? -2.702  8.104   -32.243 1.00 10.14 ? 120 HIS D CA  1 
ATOM   7386 C  C   . HIS D 1 120 ? -2.189  9.233   -31.395 1.00 10.98 ? 120 HIS D C   1 
ATOM   7387 O  O   . HIS D 1 120 ? -1.007  9.265   -31.002 1.00 10.56 ? 120 HIS D O   1 
ATOM   7388 C  CB  . HIS D 1 120 ? -3.260  6.998   -31.304 1.00 9.60  ? 120 HIS D CB  1 
ATOM   7389 C  CG  . HIS D 1 120 ? -3.708  5.707   -32.008 1.00 9.50  ? 120 HIS D CG  1 
ATOM   7390 N  ND1 . HIS D 1 120 ? -2.809  4.807   -32.564 1.00 9.91  ? 120 HIS D ND1 1 
ATOM   7391 C  CD2 . HIS D 1 120 ? -4.957  5.159   -32.095 1.00 10.73 ? 120 HIS D CD2 1 
ATOM   7392 C  CE1 . HIS D 1 120 ? -3.546  3.744   -33.068 1.00 9.79  ? 120 HIS D CE1 1 
ATOM   7393 N  NE2 . HIS D 1 120 ? -4.840  3.947   -32.758 1.00 10.55 ? 120 HIS D NE2 1 
ATOM   7394 N  N   . TYR D 1 121 ? -3.090  10.168  -31.061 1.00 9.50  ? 121 TYR D N   1 
ATOM   7395 C  CA  . TYR D 1 121 ? -2.725  11.321  -30.210 1.00 9.47  ? 121 TYR D CA  1 
ATOM   7396 C  C   . TYR D 1 121 ? -3.645  11.336  -28.988 1.00 10.19 ? 121 TYR D C   1 
ATOM   7397 O  O   . TYR D 1 121 ? -4.759  10.770  -29.035 1.00 10.23 ? 121 TYR D O   1 
ATOM   7398 C  CB  . TYR D 1 121 ? -2.814  12.611  -31.009 1.00 10.48 ? 121 TYR D CB  1 
ATOM   7399 C  CG  . TYR D 1 121 ? -4.204  13.034  -31.342 1.00 10.36 ? 121 TYR D CG  1 
ATOM   7400 C  CD1 . TYR D 1 121 ? -4.904  13.947  -30.542 1.00 11.59 ? 121 TYR D CD1 1 
ATOM   7401 C  CD2 . TYR D 1 121 ? -4.809  12.505  -32.476 1.00 11.99 ? 121 TYR D CD2 1 
ATOM   7402 C  CE1 . TYR D 1 121 ? -6.200  14.298  -30.894 1.00 12.08 ? 121 TYR D CE1 1 
ATOM   7403 C  CE2 . TYR D 1 121 ? -6.112  12.823  -32.813 1.00 13.24 ? 121 TYR D CE2 1 
ATOM   7404 C  CZ  . TYR D 1 121 ? -6.789  13.703  -32.008 1.00 14.54 ? 121 TYR D CZ  1 
ATOM   7405 O  OH  . TYR D 1 121 ? -8.111  13.984  -32.396 1.00 17.61 ? 121 TYR D OH  1 
ATOM   7406 N  N   . ASN D 1 122 ? -3.139  11.945  -27.907 1.00 10.02 ? 122 ASN D N   1 
ATOM   7407 C  CA  . ASN D 1 122 ? -3.897  12.042  -26.632 1.00 10.05 ? 122 ASN D CA  1 
ATOM   7408 C  C   . ASN D 1 122 ? -4.998  13.026  -26.770 1.00 11.47 ? 122 ASN D C   1 
ATOM   7409 O  O   . ASN D 1 122 ? -4.761  14.222  -26.633 1.00 11.21 ? 122 ASN D O   1 
ATOM   7410 C  CB  . ASN D 1 122 ? -2.888  12.397  -25.535 1.00 10.02 ? 122 ASN D CB  1 
ATOM   7411 C  CG  . ASN D 1 122 ? -3.490  12.242  -24.164 1.00 9.88  ? 122 ASN D CG  1 
ATOM   7412 O  OD1 . ASN D 1 122 ? -4.773  12.346  -24.026 1.00 10.76 ? 122 ASN D OD1 1 
ATOM   7413 N  ND2 . ASN D 1 122 ? -2.678  11.920  -23.186 1.00 10.73 ? 122 ASN D ND2 1 
ATOM   7414 N  N   . SER D 1 123 ? -6.183  12.544  -27.077 1.00 10.42 ? 123 SER D N   1 
ATOM   7415 C  CA  . SER D 1 123 ? -7.344  13.434  -27.284 1.00 11.56 ? 123 SER D CA  1 
ATOM   7416 C  C   . SER D 1 123 ? -8.065  13.862  -25.979 1.00 11.80 ? 123 SER D C   1 
ATOM   7417 O  O   . SER D 1 123 ? -8.913  14.705  -25.981 1.00 13.33 ? 123 SER D O   1 
ATOM   7418 C  CB  . SER D 1 123 ? -8.328  12.817  -28.283 1.00 10.69 ? 123 SER D CB  1 
ATOM   7419 O  OG  . SER D 1 123 ? -8.590  11.448  -27.885 1.00 13.49 ? 123 SER D OG  1 
ATOM   7420 N  N   . ASP D 1 124 ? -7.631  13.322  -24.877 1.00 13.16 ? 124 ASP D N   1 
ATOM   7421 C  CA  . ASP D 1 124 ? -8.114  13.790  -23.560 1.00 13.17 ? 124 ASP D CA  1 
ATOM   7422 C  C   . ASP D 1 124 ? -7.401  15.111  -23.264 1.00 14.37 ? 124 ASP D C   1 
ATOM   7423 O  O   . ASP D 1 124 ? -7.921  15.960  -22.502 1.00 15.96 ? 124 ASP D O   1 
ATOM   7424 C  CB  . ASP D 1 124 ? -7.786  12.707  -22.499 1.00 12.52 ? 124 ASP D CB  1 
ATOM   7425 C  CG  . ASP D 1 124 ? -8.732  11.516  -22.547 1.00 12.24 ? 124 ASP D CG  1 
ATOM   7426 O  OD1 . ASP D 1 124 ? -9.708  11.480  -23.298 1.00 15.40 ? 124 ASP D OD1 1 
ATOM   7427 O  OD2 . ASP D 1 124 ? -8.442  10.585  -21.820 1.00 14.92 ? 124 ASP D OD2 1 
ATOM   7428 N  N   . LEU D 1 125 ? -6.194  15.295  -23.798 1.00 14.56 ? 125 LEU D N   1 
ATOM   7429 C  CA  . LEU D 1 125 ? -5.321  16.466  -23.448 1.00 14.84 ? 125 LEU D CA  1 
ATOM   7430 C  C   . LEU D 1 125 ? -5.253  17.453  -24.603 1.00 16.01 ? 125 LEU D C   1 
ATOM   7431 O  O   . LEU D 1 125 ? -5.089  18.670  -24.362 1.00 15.46 ? 125 LEU D O   1 
ATOM   7432 C  CB  . LEU D 1 125 ? -3.899  15.997  -23.058 1.00 14.64 ? 125 LEU D CB  1 
ATOM   7433 C  CG  . LEU D 1 125 ? -3.675  15.619  -21.549 1.00 15.15 ? 125 LEU D CG  1 
ATOM   7434 C  CD1 . LEU D 1 125 ? -4.572  14.439  -21.177 1.00 19.49 ? 125 LEU D CD1 1 
ATOM   7435 C  CD2 . LEU D 1 125 ? -2.210  15.250  -21.477 1.00 18.45 ? 125 LEU D CD2 1 
ATOM   7436 N  N   . TYR D 1 126 ? -5.347  16.980  -25.853 1.00 13.90 ? 126 TYR D N   1 
ATOM   7437 C  CA  . TYR D 1 126 ? -4.967  17.811  -27.010 1.00 14.69 ? 126 TYR D CA  1 
ATOM   7438 C  C   . TYR D 1 126 ? -6.001  17.725  -28.107 1.00 15.59 ? 126 TYR D C   1 
ATOM   7439 O  O   . TYR D 1 126 ? -6.602  16.701  -28.271 1.00 14.82 ? 126 TYR D O   1 
ATOM   7440 C  CB  . TYR D 1 126 ? -3.622  17.342  -27.597 1.00 13.77 ? 126 TYR D CB  1 
ATOM   7441 C  CG  . TYR D 1 126 ? -2.553  17.356  -26.527 1.00 13.35 ? 126 TYR D CG  1 
ATOM   7442 C  CD1 . TYR D 1 126 ? -2.205  18.537  -25.886 1.00 13.18 ? 126 TYR D CD1 1 
ATOM   7443 C  CD2 . TYR D 1 126 ? -1.902  16.144  -26.102 1.00 13.06 ? 126 TYR D CD2 1 
ATOM   7444 C  CE1 . TYR D 1 126 ? -1.290  18.530  -24.788 1.00 12.41 ? 126 TYR D CE1 1 
ATOM   7445 C  CE2 . TYR D 1 126 ? -0.946  16.137  -25.074 1.00 13.28 ? 126 TYR D CE2 1 
ATOM   7446 C  CZ  . TYR D 1 126 ? -0.649  17.334  -24.409 1.00 12.67 ? 126 TYR D CZ  1 
ATOM   7447 O  OH  . TYR D 1 126 ? 0.289   17.310  -23.395 1.00 14.61 ? 126 TYR D OH  1 
ATOM   7448 N  N   . PRO D 1 127 ? -6.193  18.825  -28.881 1.00 16.18 ? 127 PRO D N   1 
ATOM   7449 C  CA  . PRO D 1 127 ? -7.210  18.848  -29.991 1.00 17.97 ? 127 PRO D CA  1 
ATOM   7450 C  C   . PRO D 1 127 ? -6.853  18.104  -31.275 1.00 20.38 ? 127 PRO D C   1 
ATOM   7451 O  O   . PRO D 1 127 ? -7.749  17.756  -32.061 1.00 23.84 ? 127 PRO D O   1 
ATOM   7452 C  CB  . PRO D 1 127 ? -7.310  20.362  -30.284 1.00 19.54 ? 127 PRO D CB  1 
ATOM   7453 C  CG  . PRO D 1 127 ? -6.004  20.964  -29.797 1.00 20.46 ? 127 PRO D CG  1 
ATOM   7454 C  CD  . PRO D 1 127 ? -5.684  20.179  -28.548 1.00 19.09 ? 127 PRO D CD  1 
ATOM   7455 N  N   . ASP D 1 128 ? -5.569  17.851  -31.541 1.00 16.58 ? 128 ASP D N   1 
ATOM   7456 C  CA  . ASP D 1 128 ? -5.131  17.193  -32.723 1.00 17.91 ? 128 ASP D CA  1 
ATOM   7457 C  C   . ASP D 1 128 ? -3.695  16.738  -32.565 1.00 16.93 ? 128 ASP D C   1 
ATOM   7458 O  O   . ASP D 1 128 ? -3.032  17.130  -31.561 1.00 15.60 ? 128 ASP D O   1 
ATOM   7459 C  CB  . ASP D 1 128 ? -5.277  18.242  -33.887 1.00 22.21 ? 128 ASP D CB  1 
ATOM   7460 C  CG  . ASP D 1 128 ? -4.486  19.512  -33.594 1.00 23.58 ? 128 ASP D CG  1 
ATOM   7461 O  OD1 . ASP D 1 128 ? -5.088  20.503  -33.129 1.00 34.53 ? 128 ASP D OD1 1 
ATOM   7462 O  OD2 . ASP D 1 128 ? -3.249  19.502  -33.777 1.00 25.17 ? 128 ASP D OD2 1 
ATOM   7463 N  N   . ALA D 1 129 ? -3.209  15.896  -33.485 1.00 15.69 ? 129 ALA D N   1 
ATOM   7464 C  CA  . ALA D 1 129 ? -1.926  15.295  -33.398 1.00 15.40 ? 129 ALA D CA  1 
ATOM   7465 C  C   . ALA D 1 129 ? -0.803  16.290  -33.506 1.00 14.05 ? 129 ALA D C   1 
ATOM   7466 O  O   . ALA D 1 129 ? 0.218   16.109  -32.844 1.00 15.34 ? 129 ALA D O   1 
ATOM   7467 C  CB  . ALA D 1 129 ? -1.739  14.183  -34.429 1.00 16.14 ? 129 ALA D CB  1 
ATOM   7468 N  N   A SER D 1 130 ? -0.951  17.316  -34.353 0.50 15.90 ? 130 SER D N   1 
ATOM   7469 N  N   B SER D 1 130 ? -0.978  17.310  -34.343 0.50 15.73 ? 130 SER D N   1 
ATOM   7470 C  CA  A SER D 1 130 ? 0.111   18.351  -34.450 0.50 14.52 ? 130 SER D CA  1 
ATOM   7471 C  CA  B SER D 1 130 ? 0.075   18.320  -34.475 0.50 14.36 ? 130 SER D CA  1 
ATOM   7472 C  C   A SER D 1 130 ? 0.320   19.068  -33.106 0.50 15.00 ? 130 SER D C   1 
ATOM   7473 C  C   B SER D 1 130 ? 0.305   19.093  -33.147 0.50 14.91 ? 130 SER D C   1 
ATOM   7474 O  O   A SER D 1 130 ? 1.455   19.262  -32.663 0.50 15.82 ? 130 SER D O   1 
ATOM   7475 O  O   B SER D 1 130 ? 1.448   19.340  -32.751 0.50 16.02 ? 130 SER D O   1 
ATOM   7476 C  CB  A SER D 1 130 ? -0.229  19.383  -35.549 0.50 16.14 ? 130 SER D CB  1 
ATOM   7477 C  CB  B SER D 1 130 ? -0.272  19.287  -35.621 0.50 15.69 ? 130 SER D CB  1 
ATOM   7478 O  OG  A SER D 1 130 ? -0.273  18.735  -36.791 0.50 17.05 ? 130 SER D OG  1 
ATOM   7479 O  OG  B SER D 1 130 ? 0.798   20.168  -35.763 0.50 16.47 ? 130 SER D OG  1 
ATOM   7480 N  N   . THR D 1 131 ? -0.766  19.431  -32.442 1.00 14.93 ? 131 THR D N   1 
ATOM   7481 C  CA  . THR D 1 131 ? -0.622  20.089  -31.157 1.00 13.88 ? 131 THR D CA  1 
ATOM   7482 C  C   . THR D 1 131 ? -0.024  19.078  -30.144 1.00 13.97 ? 131 THR D C   1 
ATOM   7483 O  O   . THR D 1 131 ? 0.823   19.377  -29.270 1.00 14.22 ? 131 THR D O   1 
ATOM   7484 C  CB  . THR D 1 131 ? -1.973  20.570  -30.656 1.00 15.14 ? 131 THR D CB  1 
ATOM   7485 O  OG1 . THR D 1 131 ? -2.501  21.585  -31.561 1.00 18.03 ? 131 THR D OG1 1 
ATOM   7486 C  CG2 . THR D 1 131 ? -1.791  21.248  -29.260 1.00 14.45 ? 131 THR D CG2 1 
ATOM   7487 N  N   . ALA D 1 132 ? -0.490  17.850  -30.191 1.00 11.28 ? 132 ALA D N   1 
ATOM   7488 C  CA  . ALA D 1 132 ? 0.006   16.857  -29.292 1.00 11.94 ? 132 ALA D CA  1 
ATOM   7489 C  C   . ALA D 1 132 ? 1.515   16.447  -29.401 1.00 12.87 ? 132 ALA D C   1 
ATOM   7490 O  O   . ALA D 1 132 ? 2.131   15.946  -28.438 1.00 10.95 ? 132 ALA D O   1 
ATOM   7491 C  CB  . ALA D 1 132 ? -0.840  15.588  -29.482 1.00 12.00 ? 132 ALA D CB  1 
ATOM   7492 N  N   . SER D 1 133 ? 2.052   16.512  -30.637 1.00 13.14 ? 133 SER D N   1 
ATOM   7493 C  CA  . SER D 1 133 ? 3.243   15.770  -30.981 1.00 14.97 ? 133 SER D CA  1 
ATOM   7494 C  C   . SER D 1 133 ? 4.463   16.253  -30.186 1.00 12.44 ? 133 SER D C   1 
ATOM   7495 O  O   . SER D 1 133 ? 5.396   15.518  -30.044 1.00 12.75 ? 133 SER D O   1 
ATOM   7496 C  CB  . SER D 1 133 ? 3.516   15.781  -32.521 1.00 15.29 ? 133 SER D CB  1 
ATOM   7497 O  OG  . SER D 1 133 ? 3.788   17.122  -32.898 1.00 19.41 ? 133 SER D OG  1 
ATOM   7498 N  N   . ASN D 1 134 ? 4.472   17.518  -29.686 1.00 12.80 ? 134 ASN D N   1 
ATOM   7499 C  CA  . ASN D 1 134 ? 5.617   17.963  -28.936 1.00 13.71 ? 134 ASN D CA  1 
ATOM   7500 C  C   . ASN D 1 134 ? 5.309   18.202  -27.481 1.00 14.06 ? 134 ASN D C   1 
ATOM   7501 O  O   . ASN D 1 134 ? 6.070   18.857  -26.740 1.00 13.96 ? 134 ASN D O   1 
ATOM   7502 C  CB  . ASN D 1 134 ? 6.250   19.258  -29.584 1.00 14.67 ? 134 ASN D CB  1 
ATOM   7503 C  CG  . ASN D 1 134 ? 5.335   20.486  -29.430 1.00 19.43 ? 134 ASN D CG  1 
ATOM   7504 O  OD1 . ASN D 1 134 ? 4.094   20.369  -29.323 1.00 19.62 ? 134 ASN D OD1 1 
ATOM   7505 N  ND2 . ASN D 1 134 ? 5.956   21.708  -29.414 1.00 20.00 ? 134 ASN D ND2 1 
ATOM   7506 N  N   . LYS D 1 135 ? 4.238   17.542  -27.030 1.00 11.40 ? 135 LYS D N   1 
ATOM   7507 C  CA  . LYS D 1 135 ? 3.769   17.719  -25.657 1.00 13.09 ? 135 LYS D CA  1 
ATOM   7508 C  C   . LYS D 1 135 ? 3.708   16.465  -24.877 1.00 11.58 ? 135 LYS D C   1 
ATOM   7509 O  O   . LYS D 1 135 ? 3.691   15.322  -25.417 1.00 11.53 ? 135 LYS D O   1 
ATOM   7510 C  CB  . LYS D 1 135 ? 2.412   18.452  -25.690 1.00 11.54 ? 135 LYS D CB  1 
ATOM   7511 C  CG  . LYS D 1 135 ? 2.575   19.897  -26.250 1.00 12.69 ? 135 LYS D CG  1 
ATOM   7512 C  CD  . LYS D 1 135 ? 1.290   20.687  -26.299 1.00 14.50 ? 135 LYS D CD  1 
ATOM   7513 C  CE  . LYS D 1 135 ? 1.494   22.031  -26.995 1.00 15.95 ? 135 LYS D CE  1 
ATOM   7514 N  NZ  . LYS D 1 135 ? 1.898   21.891  -28.479 1.00 15.86 ? 135 LYS D NZ  1 
ATOM   7515 N  N   A SER D 1 136 ? 3.660   16.664  -23.554 0.50 12.37 ? 136 SER D N   1 
ATOM   7516 N  N   B SER D 1 136 ? 3.842   16.625  -23.548 0.50 13.79 ? 136 SER D N   1 
ATOM   7517 C  CA  A SER D 1 136 ? 3.668   15.575  -22.598 0.50 11.08 ? 136 SER D CA  1 
ATOM   7518 C  CA  B SER D 1 136 ? 3.706   15.542  -22.589 0.50 13.18 ? 136 SER D CA  1 
ATOM   7519 C  C   A SER D 1 136 ? 2.579   14.546  -22.853 0.50 11.25 ? 136 SER D C   1 
ATOM   7520 C  C   B SER D 1 136 ? 2.631   14.557  -22.958 0.50 12.51 ? 136 SER D C   1 
ATOM   7521 O  O   A SER D 1 136 ? 1.367   14.861  -22.905 0.50 10.83 ? 136 SER D O   1 
ATOM   7522 O  O   B SER D 1 136 ? 1.483   14.929  -23.228 0.50 12.63 ? 136 SER D O   1 
ATOM   7523 C  CB  A SER D 1 136 ? 3.456   16.116  -21.176 0.50 11.83 ? 136 SER D CB  1 
ATOM   7524 C  CB  B SER D 1 136 ? 3.313   16.109  -21.221 0.50 16.14 ? 136 SER D CB  1 
ATOM   7525 O  OG  A SER D 1 136 ? 3.697   15.068  -20.275 0.50 10.32 ? 136 SER D OG  1 
ATOM   7526 O  OG  B SER D 1 136 ? 4.476   16.563  -20.589 0.50 19.45 ? 136 SER D OG  1 
ATOM   7527 N  N   . GLU D 1 137 ? 2.993   13.279  -22.896 1.00 11.49 ? 137 GLU D N   1 
ATOM   7528 C  CA  . GLU D 1 137 ? 2.014   12.197  -23.161 1.00 12.27 ? 137 GLU D CA  1 
ATOM   7529 C  C   . GLU D 1 137 ? 1.270   12.310  -24.487 1.00 11.98 ? 137 GLU D C   1 
ATOM   7530 O  O   . GLU D 1 137 ? 0.174   11.826  -24.632 1.00 11.35 ? 137 GLU D O   1 
ATOM   7531 C  CB  . GLU D 1 137 ? 1.004   11.971  -22.020 1.00 13.55 ? 137 GLU D CB  1 
ATOM   7532 C  CG  . GLU D 1 137 ? 1.646   12.001  -20.616 1.00 17.27 ? 137 GLU D CG  1 
ATOM   7533 C  CD  . GLU D 1 137 ? 2.587   10.828  -20.376 1.00 21.51 ? 137 GLU D CD  1 
ATOM   7534 O  OE1 . GLU D 1 137 ? 2.369   9.713   -20.876 1.00 22.17 ? 137 GLU D OE1 1 
ATOM   7535 O  OE2 . GLU D 1 137 ? 3.624   11.037  -19.706 1.00 30.48 ? 137 GLU D OE2 1 
ATOM   7536 N  N   . GLY D 1 138 ? 1.827   13.026  -25.475 1.00 11.15 ? 138 GLY D N   1 
ATOM   7537 C  CA  . GLY D 1 138 ? 1.061   13.348  -26.615 1.00 9.41  ? 138 GLY D CA  1 
ATOM   7538 C  C   . GLY D 1 138 ? 0.622   12.226  -27.554 1.00 8.78  ? 138 GLY D C   1 
ATOM   7539 O  O   . GLY D 1 138 ? -0.442  12.398  -28.185 1.00 8.95  ? 138 GLY D O   1 
ATOM   7540 N  N   . LEU D 1 139 ? 1.490   11.225  -27.740 1.00 9.49  ? 139 LEU D N   1 
ATOM   7541 C  CA  . LEU D 1 139 ? 1.273   10.274  -28.847 1.00 9.71  ? 139 LEU D CA  1 
ATOM   7542 C  C   . LEU D 1 139 ? 1.403   8.848   -28.338 1.00 9.29  ? 139 LEU D C   1 
ATOM   7543 O  O   . LEU D 1 139 ? 2.111   8.564   -27.376 1.00 9.97  ? 139 LEU D O   1 
ATOM   7544 C  CB  . LEU D 1 139 ? 2.380   10.470  -29.942 1.00 9.40  ? 139 LEU D CB  1 
ATOM   7545 C  CG  . LEU D 1 139 ? 2.382   11.850  -30.607 1.00 10.23 ? 139 LEU D CG  1 
ATOM   7546 C  CD1 . LEU D 1 139 ? 3.675   11.927  -31.466 1.00 10.94 ? 139 LEU D CD1 1 
ATOM   7547 C  CD2 . LEU D 1 139 ? 1.129   12.150  -31.480 1.00 11.14 ? 139 LEU D CD2 1 
ATOM   7548 N  N   . ALA D 1 140 ? 0.691   7.911   -29.003 1.00 9.48  ? 140 ALA D N   1 
ATOM   7549 C  CA  . ALA D 1 140 ? 0.849   6.470   -28.810 1.00 9.13  ? 140 ALA D CA  1 
ATOM   7550 C  C   . ALA D 1 140 ? 0.857   5.910   -30.222 1.00 9.12  ? 140 ALA D C   1 
ATOM   7551 O  O   . ALA D 1 140 ? -0.100  6.174   -31.015 1.00 9.87  ? 140 ALA D O   1 
ATOM   7552 C  CB  . ALA D 1 140 ? -0.309  5.906   -27.950 1.00 10.30 ? 140 ALA D CB  1 
ATOM   7553 N  N   . VAL D 1 141 ? 1.900   5.099   -30.484 1.00 9.18  ? 141 VAL D N   1 
ATOM   7554 C  CA  . VAL D 1 141 ? 1.961   4.444   -31.768 1.00 9.66  ? 141 VAL D CA  1 
ATOM   7555 C  C   . VAL D 1 141 ? 1.898   2.991   -31.601 1.00 10.00 ? 141 VAL D C   1 
ATOM   7556 O  O   . VAL D 1 141 ? 2.555   2.431   -30.733 1.00 9.66  ? 141 VAL D O   1 
ATOM   7557 C  CB  . VAL D 1 141 ? 3.266   4.911   -32.511 1.00 8.17  ? 141 VAL D CB  1 
ATOM   7558 C  CG1 . VAL D 1 141 ? 3.331   4.258   -33.877 1.00 8.72  ? 141 VAL D CG1 1 
ATOM   7559 C  CG2 . VAL D 1 141 ? 3.315   6.438   -32.654 1.00 8.82  ? 141 VAL D CG2 1 
ATOM   7560 N  N   . LEU D 1 142 ? 1.127   2.348   -32.493 1.00 8.59  ? 142 LEU D N   1 
ATOM   7561 C  CA  . LEU D 1 142 ? 1.155   0.898   -32.578 1.00 8.52  ? 142 LEU D CA  1 
ATOM   7562 C  C   . LEU D 1 142 ? 2.113   0.486   -33.709 1.00 8.50  ? 142 LEU D C   1 
ATOM   7563 O  O   . LEU D 1 142 ? 2.025   1.037   -34.839 1.00 10.54 ? 142 LEU D O   1 
ATOM   7564 C  CB  . LEU D 1 142 ? -0.225  0.373   -32.939 1.00 10.55 ? 142 LEU D CB  1 
ATOM   7565 C  CG  . LEU D 1 142 ? -1.352  0.767   -31.942 1.00 10.68 ? 142 LEU D CG  1 
ATOM   7566 C  CD1 . LEU D 1 142 ? -2.616  -0.016  -32.389 1.00 11.61 ? 142 LEU D CD1 1 
ATOM   7567 C  CD2 . LEU D 1 142 ? -0.955  0.533   -30.435 1.00 10.68 ? 142 LEU D CD2 1 
ATOM   7568 N  N   . ALA D 1 143 ? 3.003   -0.441  -33.428 1.00 9.75  ? 143 ALA D N   1 
ATOM   7569 C  CA  . ALA D 1 143 ? 3.939   -0.914  -34.480 1.00 8.90  ? 143 ALA D CA  1 
ATOM   7570 C  C   . ALA D 1 143 ? 3.690   -2.349  -34.805 1.00 8.68  ? 143 ALA D C   1 
ATOM   7571 O  O   . ALA D 1 143 ? 3.627   -3.208  -33.876 1.00 8.56  ? 143 ALA D O   1 
ATOM   7572 C  CB  . ALA D 1 143 ? 5.345   -0.717  -33.995 1.00 8.89  ? 143 ALA D CB  1 
ATOM   7573 N  N   . VAL D 1 144 ? 3.511   -2.608  -36.094 1.00 8.54  ? 144 VAL D N   1 
ATOM   7574 C  CA  . VAL D 1 144 ? 3.372   -4.043  -36.542 1.00 8.30  ? 144 VAL D CA  1 
ATOM   7575 C  C   . VAL D 1 144 ? 4.628   -4.362  -37.381 1.00 9.06  ? 144 VAL D C   1 
ATOM   7576 O  O   . VAL D 1 144 ? 4.939   -3.697  -38.346 1.00 9.88  ? 144 VAL D O   1 
ATOM   7577 C  CB  . VAL D 1 144 ? 2.131   -4.219  -37.378 1.00 8.85  ? 144 VAL D CB  1 
ATOM   7578 C  CG1 . VAL D 1 144 ? 1.994   -5.676  -37.893 1.00 9.22  ? 144 VAL D CG1 1 
ATOM   7579 C  CG2 . VAL D 1 144 ? 0.904   -3.716  -36.580 1.00 9.62  ? 144 VAL D CG2 1 
ATOM   7580 N  N   . LEU D 1 145 ? 5.363   -5.364  -36.931 1.00 8.89  ? 145 LEU D N   1 
ATOM   7581 C  CA  . LEU D 1 145 ? 6.517   -5.861  -37.713 1.00 9.37  ? 145 LEU D CA  1 
ATOM   7582 C  C   . LEU D 1 145 ? 6.016   -6.702  -38.889 1.00 9.45  ? 145 LEU D C   1 
ATOM   7583 O  O   . LEU D 1 145 ? 5.035   -7.467  -38.748 1.00 9.98  ? 145 LEU D O   1 
ATOM   7584 C  CB  . LEU D 1 145 ? 7.423   -6.714  -36.823 1.00 10.25 ? 145 LEU D CB  1 
ATOM   7585 C  CG  . LEU D 1 145 ? 7.945   -5.990  -35.584 1.00 11.33 ? 145 LEU D CG  1 
ATOM   7586 C  CD1 . LEU D 1 145 ? 8.499   -7.013  -34.573 1.00 13.22 ? 145 LEU D CD1 1 
ATOM   7587 C  CD2 . LEU D 1 145 ? 9.048   -5.021  -35.988 1.00 13.67 ? 145 LEU D CD2 1 
ATOM   7588 N  N   . ILE D 1 146 ? 6.630   -6.490  -40.039 1.00 9.43  ? 146 ILE D N   1 
ATOM   7589 C  CA  . ILE D 1 146 ? 6.181   -7.100  -41.284 1.00 9.12  ? 146 ILE D CA  1 
ATOM   7590 C  C   . ILE D 1 146 ? 7.259   -7.989  -41.879 1.00 9.88  ? 146 ILE D C   1 
ATOM   7591 O  O   . ILE D 1 146 ? 8.407   -7.498  -42.115 1.00 10.49 ? 146 ILE D O   1 
ATOM   7592 C  CB  . ILE D 1 146 ? 5.799   -6.031  -42.308 1.00 9.64  ? 146 ILE D CB  1 
ATOM   7593 C  CG1 . ILE D 1 146 ? 4.607   -5.183  -41.814 1.00 10.72 ? 146 ILE D CG1 1 
ATOM   7594 C  CG2 . ILE D 1 146 ? 5.481   -6.706  -43.671 1.00 8.64  ? 146 ILE D CG2 1 
ATOM   7595 C  CD1 . ILE D 1 146 ? 4.385   -3.941  -42.691 1.00 10.46 ? 146 ILE D CD1 1 
ATOM   7596 N  N   A GLU D 1 147 ? 6.924   -9.268  -42.044 0.50 9.46  ? 147 GLU D N   1 
ATOM   7597 N  N   B GLU D 1 147 ? 6.971   -9.295  -41.976 0.50 9.52  ? 147 GLU D N   1 
ATOM   7598 C  CA  A GLU D 1 147 ? 7.839   -10.282 -42.591 0.50 10.20 ? 147 GLU D CA  1 
ATOM   7599 C  CA  B GLU D 1 147 ? 7.924   -10.293 -42.549 0.50 10.28 ? 147 GLU D CA  1 
ATOM   7600 C  C   A GLU D 1 147 ? 7.512   -10.589 -44.042 0.50 10.02 ? 147 GLU D C   1 
ATOM   7601 C  C   B GLU D 1 147 ? 7.538   -10.658 -43.972 0.50 10.09 ? 147 GLU D C   1 
ATOM   7602 O  O   A GLU D 1 147 ? 6.357   -10.579 -44.477 0.50 8.77  ? 147 GLU D O   1 
ATOM   7603 O  O   B GLU D 1 147 ? 6.363   -10.738 -44.311 0.50 8.80  ? 147 GLU D O   1 
ATOM   7604 C  CB  A GLU D 1 147 ? 7.651   -11.579 -41.778 0.50 11.12 ? 147 GLU D CB  1 
ATOM   7605 C  CB  B GLU D 1 147 ? 7.979   -11.583 -41.667 0.50 11.62 ? 147 GLU D CB  1 
ATOM   7606 C  CG  A GLU D 1 147 ? 8.657   -12.666 -42.100 0.50 14.07 ? 147 GLU D CG  1 
ATOM   7607 C  CG  B GLU D 1 147 ? 6.908   -12.682 -41.847 0.50 14.99 ? 147 GLU D CG  1 
ATOM   7608 C  CD  A GLU D 1 147 ? 8.877   -13.669 -40.954 0.50 15.31 ? 147 GLU D CD  1 
ATOM   7609 C  CD  B GLU D 1 147 ? 6.989   -13.787 -40.727 0.50 14.80 ? 147 GLU D CD  1 
ATOM   7610 O  OE1 A GLU D 1 147 ? 9.356   -14.795 -41.244 0.50 21.10 ? 147 GLU D OE1 1 
ATOM   7611 O  OE1 B GLU D 1 147 ? 6.010   -14.488 -40.320 0.50 18.40 ? 147 GLU D OE1 1 
ATOM   7612 O  OE2 A GLU D 1 147 ? 8.617   -13.343 -39.749 0.50 16.11 ? 147 GLU D OE2 1 
ATOM   7613 O  OE2 B GLU D 1 147 ? 8.043   -13.875 -40.142 0.50 16.32 ? 147 GLU D OE2 1 
ATOM   7614 N  N   . MET D 1 148 ? 8.540   -10.926 -44.824 1.00 10.52 ? 148 MET D N   1 
ATOM   7615 C  CA  . MET D 1 148 ? 8.282   -11.451 -46.188 1.00 12.17 ? 148 MET D CA  1 
ATOM   7616 C  C   . MET D 1 148 ? 7.669   -12.837 -46.054 1.00 11.24 ? 148 MET D C   1 
ATOM   7617 O  O   . MET D 1 148 ? 8.237   -13.761 -45.422 1.00 13.28 ? 148 MET D O   1 
ATOM   7618 C  CB  . MET D 1 148 ? 9.563   -11.539 -47.053 1.00 12.71 ? 148 MET D CB  1 
ATOM   7619 C  CG  . MET D 1 148 ? 9.241   -11.936 -48.474 1.00 13.92 ? 148 MET D CG  1 
ATOM   7620 S  SD  . MET D 1 148 ? 10.832  -12.015 -49.394 1.00 14.97 ? 148 MET D SD  1 
ATOM   7621 C  CE  . MET D 1 148 ? 11.274  -10.280 -49.406 1.00 16.00 ? 148 MET D CE  1 
ATOM   7622 N  N   . GLY D 1 149 ? 6.488   -13.022 -46.663 1.00 11.21 ? 149 GLY D N   1 
ATOM   7623 C  CA  . GLY D 1 149 ? 5.746   -14.317 -46.531 1.00 11.12 ? 149 GLY D CA  1 
ATOM   7624 C  C   . GLY D 1 149 ? 4.644   -14.455 -47.553 1.00 11.23 ? 149 GLY D C   1 
ATOM   7625 O  O   . GLY D 1 149 ? 4.783   -14.195 -48.768 1.00 10.40 ? 149 GLY D O   1 
ATOM   7626 N  N   . SER D 1 150 ? 3.462   -14.791 -47.039 1.00 10.92 ? 150 SER D N   1 
ATOM   7627 C  CA  . SER D 1 150 ? 2.295   -14.941 -47.933 1.00 10.93 ? 150 SER D CA  1 
ATOM   7628 C  C   . SER D 1 150 ? 1.677   -13.561 -48.323 1.00 10.87 ? 150 SER D C   1 
ATOM   7629 O  O   . SER D 1 150 ? 1.774   -12.600 -47.564 1.00 11.94 ? 150 SER D O   1 
ATOM   7630 C  CB  . SER D 1 150 ? 1.207   -15.702 -47.234 1.00 10.85 ? 150 SER D CB  1 
ATOM   7631 O  OG  . SER D 1 150 ? 1.607   -17.086 -47.132 1.00 11.93 ? 150 SER D OG  1 
ATOM   7632 N  N   . PHE D 1 151 ? 1.074   -13.539 -49.520 1.00 10.86 ? 151 PHE D N   1 
ATOM   7633 C  CA  . PHE D 1 151 ? 0.292   -12.362 -49.946 1.00 11.05 ? 151 PHE D CA  1 
ATOM   7634 C  C   . PHE D 1 151 ? -0.755  -12.022 -48.908 1.00 10.93 ? 151 PHE D C   1 
ATOM   7635 O  O   . PHE D 1 151 ? -1.446  -12.926 -48.339 1.00 11.70 ? 151 PHE D O   1 
ATOM   7636 C  CB  . PHE D 1 151 ? -0.383  -12.718 -51.253 1.00 10.74 ? 151 PHE D CB  1 
ATOM   7637 C  CG  . PHE D 1 151 ? -1.241  -11.599 -51.801 1.00 10.71 ? 151 PHE D CG  1 
ATOM   7638 C  CD1 . PHE D 1 151 ? -0.626  -10.552 -52.432 1.00 11.66 ? 151 PHE D CD1 1 
ATOM   7639 C  CD2 . PHE D 1 151 ? -2.621  -11.627 -51.603 1.00 12.91 ? 151 PHE D CD2 1 
ATOM   7640 C  CE1 . PHE D 1 151 ? -1.372  -9.479  -52.885 1.00 10.96 ? 151 PHE D CE1 1 
ATOM   7641 C  CE2 . PHE D 1 151 ? -3.371  -10.546 -52.060 1.00 11.55 ? 151 PHE D CE2 1 
ATOM   7642 C  CZ  . PHE D 1 151 ? -2.758  -9.537  -52.721 1.00 11.67 ? 151 PHE D CZ  1 
ATOM   7643 N  N   . ASN D 1 152 ? -0.918  -10.705 -48.688 1.00 10.23 ? 152 ASN D N   1 
ATOM   7644 C  CA  . ASN D 1 152 ? -1.778  -10.220 -47.623 1.00 10.40 ? 152 ASN D CA  1 
ATOM   7645 C  C   . ASN D 1 152 ? -2.828  -9.321  -48.279 1.00 10.96 ? 152 ASN D C   1 
ATOM   7646 O  O   . ASN D 1 152 ? -2.545  -8.166  -48.672 1.00 11.10 ? 152 ASN D O   1 
ATOM   7647 C  CB  . ASN D 1 152 ? -0.961  -9.406  -46.603 1.00 10.27 ? 152 ASN D CB  1 
ATOM   7648 C  CG  . ASN D 1 152 ? -1.751  -9.093  -45.337 1.00 10.43 ? 152 ASN D CG  1 
ATOM   7649 O  OD1 . ASN D 1 152 ? -2.886  -8.604  -45.413 1.00 11.35 ? 152 ASN D OD1 1 
ATOM   7650 N  ND2 . ASN D 1 152 ? -1.168  -9.396  -44.187 1.00 10.13 ? 152 ASN D ND2 1 
ATOM   7651 N  N   . PRO D 1 153 ? -4.081  -9.876  -48.414 1.00 11.55 ? 153 PRO D N   1 
ATOM   7652 C  CA  . PRO D 1 153 ? -5.124  -9.116  -49.100 1.00 13.17 ? 153 PRO D CA  1 
ATOM   7653 C  C   . PRO D 1 153 ? -5.494  -7.825  -48.364 1.00 11.28 ? 153 PRO D C   1 
ATOM   7654 O  O   . PRO D 1 153 ? -5.864  -6.847  -48.990 1.00 13.28 ? 153 PRO D O   1 
ATOM   7655 C  CB  . PRO D 1 153 ? -6.341  -10.061 -49.034 1.00 14.24 ? 153 PRO D CB  1 
ATOM   7656 C  CG  . PRO D 1 153 ? -5.738  -11.413 -48.986 1.00 17.09 ? 153 PRO D CG  1 
ATOM   7657 C  CD  . PRO D 1 153 ? -4.540  -11.241 -48.053 1.00 13.15 ? 153 PRO D CD  1 
ATOM   7658 N  N   . SER D 1 154 ? -5.302  -7.798  -47.061 1.00 11.48 ? 154 SER D N   1 
ATOM   7659 C  CA  . SER D 1 154 ? -5.687  -6.580  -46.329 1.00 11.66 ? 154 SER D CA  1 
ATOM   7660 C  C   . SER D 1 154 ? -4.662  -5.473  -46.503 1.00 11.02 ? 154 SER D C   1 
ATOM   7661 O  O   . SER D 1 154 ? -5.006  -4.290  -46.764 1.00 11.09 ? 154 SER D O   1 
ATOM   7662 C  CB  . SER D 1 154 ? -5.906  -6.883  -44.860 1.00 11.48 ? 154 SER D CB  1 
ATOM   7663 O  OG  . SER D 1 154 ? -6.852  -7.930  -44.632 1.00 15.12 ? 154 SER D OG  1 
ATOM   7664 N  N   . TYR D 1 155 ? -3.359  -5.795  -46.435 1.00 9.75  ? 155 TYR D N   1 
ATOM   7665 C  CA  . TYR D 1 155 ? -2.350  -4.781  -46.792 1.00 10.14 ? 155 TYR D CA  1 
ATOM   7666 C  C   . TYR D 1 155 ? -2.458  -4.362  -48.228 1.00 9.95  ? 155 TYR D C   1 
ATOM   7667 O  O   . TYR D 1 155 ? -2.140  -3.210  -48.587 1.00 12.20 ? 155 TYR D O   1 
ATOM   7668 C  CB  . TYR D 1 155 ? -0.900  -5.249  -46.480 1.00 9.29  ? 155 TYR D CB  1 
ATOM   7669 C  CG  . TYR D 1 155 ? -0.571  -5.104  -45.017 1.00 8.89  ? 155 TYR D CG  1 
ATOM   7670 C  CD1 . TYR D 1 155 ? 0.193   -3.970  -44.594 1.00 9.83  ? 155 TYR D CD1 1 
ATOM   7671 C  CD2 . TYR D 1 155 ? -0.971  -6.061  -44.072 1.00 9.14  ? 155 TYR D CD2 1 
ATOM   7672 C  CE1 . TYR D 1 155 ? 0.515   -3.838  -43.228 1.00 10.01 ? 155 TYR D CE1 1 
ATOM   7673 C  CE2 . TYR D 1 155 ? -0.678  -5.925  -42.695 1.00 9.31  ? 155 TYR D CE2 1 
ATOM   7674 C  CZ  . TYR D 1 155 ? 0.055   -4.782  -42.267 1.00 10.29 ? 155 TYR D CZ  1 
ATOM   7675 O  OH  . TYR D 1 155 ? 0.356   -4.581  -40.939 1.00 10.20 ? 155 TYR D OH  1 
ATOM   7676 N  N   . ASP D 1 156 ? -2.949  -5.260  -49.077 1.00 10.68 ? 156 ASP D N   1 
ATOM   7677 C  CA  . ASP D 1 156 ? -3.060  -4.841  -50.456 1.00 11.14 ? 156 ASP D CA  1 
ATOM   7678 C  C   . ASP D 1 156 ? -4.140  -3.767  -50.706 1.00 10.78 ? 156 ASP D C   1 
ATOM   7679 O  O   . ASP D 1 156 ? -4.158  -3.150  -51.792 1.00 12.08 ? 156 ASP D O   1 
ATOM   7680 C  CB  . ASP D 1 156 ? -3.346  -6.049  -51.361 1.00 12.26 ? 156 ASP D CB  1 
ATOM   7681 C  CG  . ASP D 1 156 ? -2.511  -5.963  -52.622 1.00 14.03 ? 156 ASP D CG  1 
ATOM   7682 O  OD1 . ASP D 1 156 ? -1.243  -5.763  -52.552 1.00 12.54 ? 156 ASP D OD1 1 
ATOM   7683 O  OD2 . ASP D 1 156 ? -3.164  -6.016  -53.710 1.00 15.58 ? 156 ASP D OD2 1 
ATOM   7684 N  N   . LYS D 1 157 ? -5.048  -3.596  -49.744 1.00 12.16 ? 157 LYS D N   1 
ATOM   7685 C  CA  . LYS D 1 157 ? -6.059  -2.542  -49.869 1.00 12.96 ? 157 LYS D CA  1 
ATOM   7686 C  C   . LYS D 1 157 ? -5.339  -1.193  -49.833 1.00 14.14 ? 157 LYS D C   1 
ATOM   7687 O  O   . LYS D 1 157 ? -5.856  -0.228  -50.428 1.00 16.24 ? 157 LYS D O   1 
ATOM   7688 C  CB  . LYS D 1 157 ? -7.109  -2.669  -48.759 1.00 13.08 ? 157 LYS D CB  1 
ATOM   7689 C  CG  . LYS D 1 157 ? -7.926  -3.994  -48.899 1.00 14.14 ? 157 LYS D CG  1 
ATOM   7690 C  CD  . LYS D 1 157 ? -8.849  -4.253  -47.658 1.00 19.32 ? 157 LYS D CD  1 
ATOM   7691 C  CE  . LYS D 1 157 ? -9.672  -5.563  -47.739 1.00 22.03 ? 157 LYS D CE  1 
ATOM   7692 N  NZ  . LYS D 1 157 ? -10.308 -6.231  -46.545 1.00 25.05 ? 157 LYS D NZ  1 
ATOM   7693 N  N   . ILE D 1 158 ? -4.128  -1.110  -49.243 1.00 13.11 ? 158 ILE D N   1 
ATOM   7694 C  CA  . ILE D 1 158 ? -3.348  0.100   -49.322 1.00 12.48 ? 158 ILE D CA  1 
ATOM   7695 C  C   . ILE D 1 158 ? -2.466  0.017   -50.561 1.00 12.07 ? 158 ILE D C   1 
ATOM   7696 O  O   . ILE D 1 158 ? -2.395  0.955   -51.342 1.00 12.34 ? 158 ILE D O   1 
ATOM   7697 C  CB  . ILE D 1 158 ? -2.473  0.235   -48.052 1.00 12.40 ? 158 ILE D CB  1 
ATOM   7698 C  CG1 . ILE D 1 158 ? -3.400  0.482   -46.848 1.00 13.48 ? 158 ILE D CG1 1 
ATOM   7699 C  CG2 . ILE D 1 158 ? -1.456  1.376   -48.167 1.00 11.34 ? 158 ILE D CG2 1 
ATOM   7700 C  CD1 . ILE D 1 158 ? -2.731  0.401   -45.493 1.00 15.66 ? 158 ILE D CD1 1 
ATOM   7701 N  N   . PHE D 1 159 ? -1.793  -1.131  -50.744 1.00 11.58 ? 159 PHE D N   1 
ATOM   7702 C  CA  . PHE D 1 159 ? -0.710  -1.159  -51.724 1.00 11.09 ? 159 PHE D CA  1 
ATOM   7703 C  C   . PHE D 1 159 ? -1.215  -1.047  -53.160 1.00 12.17 ? 159 PHE D C   1 
ATOM   7704 O  O   . PHE D 1 159 ? -0.491  -0.630  -54.053 1.00 12.49 ? 159 PHE D O   1 
ATOM   7705 C  CB  . PHE D 1 159 ? 0.122   -2.464  -51.642 1.00 10.85 ? 159 PHE D CB  1 
ATOM   7706 C  CG  . PHE D 1 159 ? 0.851   -2.666  -50.324 1.00 12.36 ? 159 PHE D CG  1 
ATOM   7707 C  CD1 . PHE D 1 159 ? 1.289   -1.596  -49.532 1.00 12.95 ? 159 PHE D CD1 1 
ATOM   7708 C  CD2 . PHE D 1 159 ? 1.078   -4.003  -49.878 1.00 11.32 ? 159 PHE D CD2 1 
ATOM   7709 C  CE1 . PHE D 1 159 ? 1.957   -1.871  -48.298 1.00 12.55 ? 159 PHE D CE1 1 
ATOM   7710 C  CE2 . PHE D 1 159 ? 1.804   -4.203  -48.674 1.00 12.23 ? 159 PHE D CE2 1 
ATOM   7711 C  CZ  . PHE D 1 159 ? 2.226   -3.139  -47.899 1.00 13.25 ? 159 PHE D CZ  1 
ATOM   7712 N  N   . SER D 1 160 ? -2.459  -1.407  -53.392 1.00 12.27 ? 160 SER D N   1 
ATOM   7713 C  CA  . SER D 1 160 ? -3.008  -1.304  -54.747 1.00 12.72 ? 160 SER D CA  1 
ATOM   7714 C  C   . SER D 1 160 ? -3.128  0.127   -55.239 1.00 13.58 ? 160 SER D C   1 
ATOM   7715 O  O   . SER D 1 160 ? -3.247  0.346   -56.441 1.00 15.95 ? 160 SER D O   1 
ATOM   7716 C  CB  . SER D 1 160 ? -4.379  -2.030  -54.848 1.00 15.41 ? 160 SER D CB  1 
ATOM   7717 O  OG  . SER D 1 160 ? -5.350  -1.317  -54.094 1.00 15.66 ? 160 SER D OG  1 
ATOM   7718 N  N   . HIS D 1 161 ? -2.993  1.097   -54.333 1.00 12.17 ? 161 HIS D N   1 
ATOM   7719 C  CA  . HIS D 1 161 ? -3.049  2.472   -54.672 1.00 11.79 ? 161 HIS D CA  1 
ATOM   7720 C  C   . HIS D 1 161 ? -1.733  3.138   -54.835 1.00 13.75 ? 161 HIS D C   1 
ATOM   7721 O  O   . HIS D 1 161 ? -1.672  4.371   -55.164 1.00 13.07 ? 161 HIS D O   1 
ATOM   7722 C  CB  . HIS D 1 161 ? -3.842  3.264   -53.589 1.00 13.18 ? 161 HIS D CB  1 
ATOM   7723 C  CG  . HIS D 1 161 ? -5.280  2.873   -53.501 1.00 14.76 ? 161 HIS D CG  1 
ATOM   7724 N  ND1 . HIS D 1 161 ? -6.235  3.508   -54.196 1.00 18.03 ? 161 HIS D ND1 1 
ATOM   7725 C  CD2 . HIS D 1 161 ? -5.911  1.870   -52.783 1.00 15.68 ? 161 HIS D CD2 1 
ATOM   7726 C  CE1 . HIS D 1 161 ? -7.421  2.941   -53.930 1.00 18.18 ? 161 HIS D CE1 1 
ATOM   7727 N  NE2 . HIS D 1 161 ? -7.224  1.940   -53.064 1.00 17.15 ? 161 HIS D NE2 1 
ATOM   7728 N  N   . LEU D 1 162 ? -0.655  2.379   -54.638 1.00 13.98 ? 162 LEU D N   1 
ATOM   7729 C  CA  . LEU D 1 162 ? 0.716   3.021   -54.679 1.00 14.21 ? 162 LEU D CA  1 
ATOM   7730 C  C   . LEU D 1 162 ? 1.007   3.685   -56.006 1.00 14.13 ? 162 LEU D C   1 
ATOM   7731 O  O   . LEU D 1 162 ? 1.678   4.766   -56.061 1.00 17.06 ? 162 LEU D O   1 
ATOM   7732 C  CB  . LEU D 1 162 ? 1.815   1.932   -54.395 1.00 14.72 ? 162 LEU D CB  1 
ATOM   7733 C  CG  . LEU D 1 162 ? 1.872   1.422   -52.962 1.00 14.79 ? 162 LEU D CG  1 
ATOM   7734 C  CD1 . LEU D 1 162 ? 2.797   0.182   -52.856 1.00 16.51 ? 162 LEU D CD1 1 
ATOM   7735 C  CD2 . LEU D 1 162 ? 2.292   2.483   -51.939 1.00 15.36 ? 162 LEU D CD2 1 
ATOM   7736 N  N   . GLN D 1 163 ? 0.510   3.092   -57.101 1.00 17.92 ? 163 GLN D N   1 
ATOM   7737 C  CA  . GLN D 1 163 ? 0.787   3.714   -58.422 1.00 19.94 ? 163 GLN D CA  1 
ATOM   7738 C  C   . GLN D 1 163 ? 0.147   5.076   -58.695 1.00 20.31 ? 163 GLN D C   1 
ATOM   7739 O  O   . GLN D 1 163 ? 0.487   5.712   -59.688 1.00 24.44 ? 163 GLN D O   1 
ATOM   7740 C  CB  . GLN D 1 163 ? 0.636   2.712   -59.583 1.00 23.38 ? 163 GLN D CB  1 
ATOM   7741 C  CG  . GLN D 1 163 ? 1.598   1.504   -59.510 1.00 27.87 ? 163 GLN D CG  1 
ATOM   7742 C  CD  . GLN D 1 163 ? 3.144   1.772   -59.568 1.00 28.09 ? 163 GLN D CD  1 
ATOM   7743 O  OE1 . GLN D 1 163 ? 3.614   2.673   -60.234 1.00 30.29 ? 163 GLN D OE1 1 
ATOM   7744 N  NE2 . GLN D 1 163 ? 3.922   0.906   -58.904 1.00 28.31 ? 163 GLN D NE2 1 
ATOM   7745 N  N   . HIS D 1 164 ? -0.772  5.495   -57.824 1.00 16.09 ? 164 HIS D N   1 
ATOM   7746 C  CA  . HIS D 1 164 ? -1.371  6.799   -57.857 1.00 17.11 ? 164 HIS D CA  1 
ATOM   7747 C  C   . HIS D 1 164 ? -0.779  7.848   -56.964 1.00 16.29 ? 164 HIS D C   1 
ATOM   7748 O  O   . HIS D 1 164 ? -1.218  9.035   -56.949 1.00 18.93 ? 164 HIS D O   1 
ATOM   7749 C  CB  . HIS D 1 164 ? -2.856  6.642   -57.568 1.00 20.01 ? 164 HIS D CB  1 
ATOM   7750 C  CG  . HIS D 1 164 ? -3.521  5.766   -58.563 1.00 26.27 ? 164 HIS D CG  1 
ATOM   7751 N  ND1 . HIS D 1 164 ? -3.716  6.150   -59.829 1.00 30.83 ? 164 HIS D ND1 1 
ATOM   7752 C  CD2 . HIS D 1 164 ? -4.031  4.496   -58.450 1.00 31.29 ? 164 HIS D CD2 1 
ATOM   7753 C  CE1 . HIS D 1 164 ? -4.339  5.178   -60.509 1.00 31.48 ? 164 HIS D CE1 1 
ATOM   7754 N  NE2 . HIS D 1 164 ? -4.527  4.153   -59.674 1.00 40.16 ? 164 HIS D NE2 1 
ATOM   7755 N  N   . VAL D 1 165 ? 0.233   7.435   -56.173 1.00 14.75 ? 165 VAL D N   1 
ATOM   7756 C  CA  . VAL D 1 165 ? 0.890   8.373   -55.246 1.00 12.61 ? 165 VAL D CA  1 
ATOM   7757 C  C   . VAL D 1 165 ? 2.383   8.301   -55.413 1.00 12.61 ? 165 VAL D C   1 
ATOM   7758 O  O   . VAL D 1 165 ? 3.145   8.381   -54.436 1.00 13.19 ? 165 VAL D O   1 
ATOM   7759 C  CB  . VAL D 1 165 ? 0.507   8.139   -53.747 1.00 12.34 ? 165 VAL D CB  1 
ATOM   7760 C  CG1 . VAL D 1 165 ? -0.973  8.599   -53.636 1.00 13.28 ? 165 VAL D CG1 1 
ATOM   7761 C  CG2 . VAL D 1 165 ? 0.682   6.672   -53.286 1.00 13.19 ? 165 VAL D CG2 1 
ATOM   7762 N  N   A LYS D 1 166 ? 2.857   8.173   -56.636 0.50 12.80 ? 166 LYS D N   1 
ATOM   7763 N  N   B LYS D 1 166 ? 2.796   8.196   -56.668 0.50 13.72 ? 166 LYS D N   1 
ATOM   7764 C  CA  A LYS D 1 166 ? 4.279   7.918   -56.798 0.50 12.53 ? 166 LYS D CA  1 
ATOM   7765 C  CA  B LYS D 1 166 ? 4.181   7.934   -57.012 0.50 14.11 ? 166 LYS D CA  1 
ATOM   7766 C  C   A LYS D 1 166 ? 5.144   9.100   -56.357 0.50 12.60 ? 166 LYS D C   1 
ATOM   7767 C  C   B LYS D 1 166 ? 5.138   9.043   -56.583 0.50 14.04 ? 166 LYS D C   1 
ATOM   7768 O  O   A LYS D 1 166 ? 6.246   8.921   -55.817 0.50 12.17 ? 166 LYS D O   1 
ATOM   7769 O  O   B LYS D 1 166 ? 6.290   8.730   -56.258 0.50 13.75 ? 166 LYS D O   1 
ATOM   7770 C  CB  A LYS D 1 166 ? 4.558   7.544   -58.243 0.50 11.62 ? 166 LYS D CB  1 
ATOM   7771 C  CB  B LYS D 1 166 ? 4.296   7.713   -58.519 0.50 14.03 ? 166 LYS D CB  1 
ATOM   7772 C  CG  A LYS D 1 166 ? 3.919   6.210   -58.610 0.50 11.05 ? 166 LYS D CG  1 
ATOM   7773 C  CG  B LYS D 1 166 ? 5.709   7.529   -59.050 0.50 14.28 ? 166 LYS D CG  1 
ATOM   7774 C  CD  A LYS D 1 166 ? 4.196   5.865   -60.039 0.50 11.39 ? 166 LYS D CD  1 
ATOM   7775 C  CD  B LYS D 1 166 ? 5.727   7.195   -60.532 0.50 15.43 ? 166 LYS D CD  1 
ATOM   7776 C  CE  A LYS D 1 166 ? 5.707   5.746   -60.291 0.50 11.11 ? 166 LYS D CE  1 
ATOM   7777 C  CE  B LYS D 1 166 ? 4.971   5.912   -60.897 0.50 15.70 ? 166 LYS D CE  1 
ATOM   7778 N  NZ  A LYS D 1 166 ? 6.321   4.438   -59.906 0.50 11.82 ? 166 LYS D NZ  1 
ATOM   7779 N  NZ  B LYS D 1 166 ? 5.270   4.684   -60.076 0.50 15.02 ? 166 LYS D NZ  1 
ATOM   7780 N  N   . TYR D 1 167 ? 4.677   10.312  -56.649 1.00 14.14 ? 167 TYR D N   1 
ATOM   7781 C  CA  . TYR D 1 167 ? 5.481   11.493  -56.335 1.00 15.67 ? 167 TYR D CA  1 
ATOM   7782 C  C   . TYR D 1 167 ? 5.010   12.348  -55.138 1.00 15.20 ? 167 TYR D C   1 
ATOM   7783 O  O   . TYR D 1 167 ? 3.804   12.333  -54.758 1.00 15.05 ? 167 TYR D O   1 
ATOM   7784 C  CB  . TYR D 1 167 ? 5.549   12.373  -57.586 1.00 17.63 ? 167 TYR D CB  1 
ATOM   7785 C  CG  . TYR D 1 167 ? 6.153   11.671  -58.761 1.00 20.74 ? 167 TYR D CG  1 
ATOM   7786 C  CD1 . TYR D 1 167 ? 7.532   11.461  -58.821 1.00 22.16 ? 167 TYR D CD1 1 
ATOM   7787 C  CD2 . TYR D 1 167 ? 5.345   11.197  -59.794 1.00 21.19 ? 167 TYR D CD2 1 
ATOM   7788 C  CE1 . TYR D 1 167 ? 8.099   10.796  -59.905 1.00 23.95 ? 167 TYR D CE1 1 
ATOM   7789 C  CE2 . TYR D 1 167 ? 5.898   10.542  -60.891 1.00 26.88 ? 167 TYR D CE2 1 
ATOM   7790 C  CZ  . TYR D 1 167 ? 7.290   10.336  -60.934 1.00 26.51 ? 167 TYR D CZ  1 
ATOM   7791 O  OH  . TYR D 1 167 ? 7.874   9.684   -62.027 1.00 31.32 ? 167 TYR D OH  1 
ATOM   7792 N  N   . LYS D 1 168 ? 5.957   13.041  -54.501 1.00 14.52 ? 168 LYS D N   1 
ATOM   7793 C  CA  . LYS D 1 168 ? 5.653   13.863  -53.320 1.00 16.11 ? 168 LYS D CA  1 
ATOM   7794 C  C   . LYS D 1 168 ? 4.467   14.717  -53.574 1.00 15.65 ? 168 LYS D C   1 
ATOM   7795 O  O   . LYS D 1 168 ? 4.394   15.368  -54.629 1.00 17.56 ? 168 LYS D O   1 
ATOM   7796 C  CB  . LYS D 1 168 ? 6.875   14.748  -52.916 1.00 15.91 ? 168 LYS D CB  1 
ATOM   7797 C  CG  . LYS D 1 168 ? 6.557   15.531  -51.655 1.00 16.05 ? 168 LYS D CG  1 
ATOM   7798 C  CD  . LYS D 1 168 ? 7.800   16.256  -51.118 1.00 18.88 ? 168 LYS D CD  1 
ATOM   7799 C  CE  . LYS D 1 168 ? 7.382   17.220  -50.047 1.00 20.69 ? 168 LYS D CE  1 
ATOM   7800 N  NZ  . LYS D 1 168 ? 8.622   17.591  -49.301 1.00 24.83 ? 168 LYS D NZ  1 
ATOM   7801 N  N   . GLY D 1 169 ? 3.507   14.722  -52.644 1.00 16.60 ? 169 GLY D N   1 
ATOM   7802 C  CA  . GLY D 1 169 ? 2.346   15.622  -52.769 1.00 16.43 ? 169 GLY D CA  1 
ATOM   7803 C  C   . GLY D 1 169 ? 1.167   14.934  -53.445 1.00 17.42 ? 169 GLY D C   1 
ATOM   7804 O  O   . GLY D 1 169 ? 0.051   15.442  -53.384 1.00 19.66 ? 169 GLY D O   1 
ATOM   7805 N  N   . GLN D 1 170 ? 1.359   13.804  -54.119 1.00 14.96 ? 170 GLN D N   1 
ATOM   7806 C  CA  . GLN D 1 170 ? 0.220   13.222  -54.792 1.00 15.62 ? 170 GLN D CA  1 
ATOM   7807 C  C   . GLN D 1 170 ? -0.636  12.448  -53.740 1.00 16.62 ? 170 GLN D C   1 
ATOM   7808 O  O   . GLN D 1 170 ? -0.108  12.051  -52.663 1.00 15.98 ? 170 GLN D O   1 
ATOM   7809 C  CB  . GLN D 1 170 ? 0.685   12.286  -55.889 1.00 15.79 ? 170 GLN D CB  1 
ATOM   7810 C  CG  . GLN D 1 170 ? 1.428   13.008  -57.025 1.00 15.52 ? 170 GLN D CG  1 
ATOM   7811 C  CD  . GLN D 1 170 ? 1.732   12.101  -58.179 1.00 18.26 ? 170 GLN D CD  1 
ATOM   7812 O  OE1 . GLN D 1 170 ? 2.106   10.945  -58.035 1.00 17.85 ? 170 GLN D OE1 1 
ATOM   7813 N  NE2 . GLN D 1 170 ? 1.473   12.625  -59.410 1.00 19.93 ? 170 GLN D NE2 1 
ATOM   7814 N  N   . GLU D 1 171 ? -1.938  12.297  -54.032 1.00 17.51 ? 171 GLU D N   1 
ATOM   7815 C  CA  . GLU D 1 171 ? -2.974  11.868  -53.061 1.00 17.46 ? 171 GLU D CA  1 
ATOM   7816 C  C   . GLU D 1 171 ? -3.919  10.930  -53.853 1.00 16.94 ? 171 GLU D C   1 
ATOM   7817 O  O   . GLU D 1 171 ? -4.032  11.014  -55.104 1.00 18.12 ? 171 GLU D O   1 
ATOM   7818 C  CB  . GLU D 1 171 ? -3.756  13.059  -52.513 1.00 21.70 ? 171 GLU D CB  1 
ATOM   7819 C  CG  . GLU D 1 171 ? -2.908  14.030  -51.719 1.00 27.00 ? 171 GLU D CG  1 
ATOM   7820 C  CD  . GLU D 1 171 ? -3.733  15.206  -51.267 1.00 33.41 ? 171 GLU D CD  1 
ATOM   7821 O  OE1 . GLU D 1 171 ? -4.673  15.533  -52.010 1.00 32.20 ? 171 GLU D OE1 1 
ATOM   7822 O  OE2 . GLU D 1 171 ? -3.477  15.741  -50.161 1.00 41.08 ? 171 GLU D OE2 1 
ATOM   7823 N  N   . ALA D 1 172 ? -4.465  9.951   -53.149 1.00 15.41 ? 172 ALA D N   1 
ATOM   7824 C  CA  . ALA D 1 172 ? -5.418  9.019   -53.716 1.00 14.52 ? 172 ALA D CA  1 
ATOM   7825 C  C   . ALA D 1 172 ? -6.421  8.714   -52.611 1.00 15.86 ? 172 ALA D C   1 
ATOM   7826 O  O   . ALA D 1 172 ? -6.118  8.822   -51.459 1.00 17.34 ? 172 ALA D O   1 
ATOM   7827 C  CB  . ALA D 1 172 ? -4.729  7.726   -54.175 1.00 14.78 ? 172 ALA D CB  1 
ATOM   7828 N  N   . PHE D 1 173 ? -7.619  8.302   -52.949 1.00 14.94 ? 173 PHE D N   1 
ATOM   7829 C  CA  . PHE D 1 173 ? -8.560  7.856   -51.904 1.00 16.78 ? 173 PHE D CA  1 
ATOM   7830 C  C   . PHE D 1 173 ? -8.615  6.339   -51.820 1.00 15.97 ? 173 PHE D C   1 
ATOM   7831 O  O   . PHE D 1 173 ? -8.584  5.659   -52.833 1.00 17.31 ? 173 PHE D O   1 
ATOM   7832 C  CB  . PHE D 1 173 ? -9.951  8.391   -52.222 1.00 17.13 ? 173 PHE D CB  1 
ATOM   7833 C  CG  . PHE D 1 173 ? -10.189 9.791   -51.718 1.00 20.91 ? 173 PHE D CG  1 
ATOM   7834 C  CD1 . PHE D 1 173 ? -10.184 10.055  -50.334 1.00 24.83 ? 173 PHE D CD1 1 
ATOM   7835 C  CD2 . PHE D 1 173 ? -10.416 10.810  -52.589 1.00 29.33 ? 173 PHE D CD2 1 
ATOM   7836 C  CE1 . PHE D 1 173 ? -10.398 11.332  -49.851 1.00 30.34 ? 173 PHE D CE1 1 
ATOM   7837 C  CE2 . PHE D 1 173 ? -10.648 12.111  -52.117 1.00 26.72 ? 173 PHE D CE2 1 
ATOM   7838 C  CZ  . PHE D 1 173 ? -10.617 12.365  -50.750 1.00 28.58 ? 173 PHE D CZ  1 
ATOM   7839 N  N   . VAL D 1 174 ? -8.628  5.826   -50.611 1.00 13.52 ? 174 VAL D N   1 
ATOM   7840 C  CA  . VAL D 1 174 ? -8.702  4.414   -50.335 1.00 13.68 ? 174 VAL D CA  1 
ATOM   7841 C  C   . VAL D 1 174 ? -10.090 4.193   -49.646 1.00 14.54 ? 174 VAL D C   1 
ATOM   7842 O  O   . VAL D 1 174 ? -10.408 4.829   -48.596 1.00 15.85 ? 174 VAL D O   1 
ATOM   7843 C  CB  . VAL D 1 174 ? -7.596  4.098   -49.341 1.00 13.49 ? 174 VAL D CB  1 
ATOM   7844 C  CG1 . VAL D 1 174 ? -7.632  2.666   -48.923 1.00 12.72 ? 174 VAL D CG1 1 
ATOM   7845 C  CG2 . VAL D 1 174 ? -6.197  4.440   -49.992 1.00 13.37 ? 174 VAL D CG2 1 
ATOM   7846 N  N   . PRO D 1 175 ? -10.900 3.265   -50.189 1.00 14.27 ? 175 PRO D N   1 
ATOM   7847 C  CA  . PRO D 1 175 ? -12.158 3.003   -49.470 1.00 13.57 ? 175 PRO D CA  1 
ATOM   7848 C  C   . PRO D 1 175 ? -11.897 2.451   -48.088 1.00 13.41 ? 175 PRO D C   1 
ATOM   7849 O  O   . PRO D 1 175 ? -10.962 1.721   -47.886 1.00 13.95 ? 175 PRO D O   1 
ATOM   7850 C  CB  . PRO D 1 175 ? -12.789 1.878   -50.280 1.00 15.01 ? 175 PRO D CB  1 
ATOM   7851 C  CG  . PRO D 1 175 ? -12.252 2.077   -51.676 1.00 15.56 ? 175 PRO D CG  1 
ATOM   7852 C  CD  . PRO D 1 175 ? -10.816 2.532   -51.467 1.00 14.15 ? 175 PRO D CD  1 
ATOM   7853 N  N   . GLY D 1 176 ? -12.774 2.716   -47.125 1.00 14.89 ? 176 GLY D N   1 
ATOM   7854 C  CA  . GLY D 1 176 ? -12.518 2.142   -45.802 1.00 12.41 ? 176 GLY D CA  1 
ATOM   7855 C  C   . GLY D 1 176 ? -12.522 0.589   -45.749 1.00 12.82 ? 176 GLY D C   1 
ATOM   7856 O  O   . GLY D 1 176 ? -13.196 -0.113  -46.564 1.00 15.05 ? 176 GLY D O   1 
ATOM   7857 N  N   . PHE D 1 177 ? -11.749 0.101   -44.817 1.00 13.03 ? 177 PHE D N   1 
ATOM   7858 C  CA  . PHE D 1 177 ? -11.706 -1.325  -44.500 1.00 13.34 ? 177 PHE D CA  1 
ATOM   7859 C  C   . PHE D 1 177 ? -11.421 -1.528  -43.013 1.00 14.14 ? 177 PHE D C   1 
ATOM   7860 O  O   . PHE D 1 177 ? -11.221 -0.535  -42.311 1.00 13.51 ? 177 PHE D O   1 
ATOM   7861 C  CB  . PHE D 1 177 ? -10.732 -2.032  -45.438 1.00 14.03 ? 177 PHE D CB  1 
ATOM   7862 C  CG  . PHE D 1 177 ? -9.258  -1.705  -45.195 1.00 12.42 ? 177 PHE D CG  1 
ATOM   7863 C  CD1 . PHE D 1 177 ? -8.465  -2.565  -44.369 1.00 16.02 ? 177 PHE D CD1 1 
ATOM   7864 C  CD2 . PHE D 1 177 ? -8.674  -0.585  -45.770 1.00 14.95 ? 177 PHE D CD2 1 
ATOM   7865 C  CE1 . PHE D 1 177 ? -7.110  -2.283  -44.216 1.00 14.84 ? 177 PHE D CE1 1 
ATOM   7866 C  CE2 . PHE D 1 177 ? -7.307  -0.303  -45.581 1.00 13.56 ? 177 PHE D CE2 1 
ATOM   7867 C  CZ  . PHE D 1 177 ? -6.585  -1.117  -44.757 1.00 16.05 ? 177 PHE D CZ  1 
ATOM   7868 N  N   . ASN D 1 178 ? -11.418 -2.765  -42.528 1.00 15.85 ? 178 ASN D N   1 
ATOM   7869 C  CA  . ASN D 1 178 ? -11.252 -2.938  -41.106 1.00 14.97 ? 178 ASN D CA  1 
ATOM   7870 C  C   . ASN D 1 178 ? -9.745  -2.913  -40.861 1.00 14.11 ? 178 ASN D C   1 
ATOM   7871 O  O   . ASN D 1 178 ? -9.050  -3.926  -41.122 1.00 13.38 ? 178 ASN D O   1 
ATOM   7872 C  CB  . ASN D 1 178 ? -11.810 -4.266  -40.687 1.00 14.19 ? 178 ASN D CB  1 
ATOM   7873 C  CG  . ASN D 1 178 ? -11.685 -4.498  -39.202 1.00 15.93 ? 178 ASN D CG  1 
ATOM   7874 O  OD1 . ASN D 1 178 ? -11.276 -3.627  -38.411 1.00 14.84 ? 178 ASN D OD1 1 
ATOM   7875 N  ND2 . ASN D 1 178 ? -12.190 -5.687  -38.766 1.00 22.04 ? 178 ASN D ND2 1 
ATOM   7876 N  N   . ILE D 1 179 ? -9.272  -1.809  -40.284 1.00 12.08 ? 179 ILE D N   1 
ATOM   7877 C  CA  . ILE D 1 179 ? -7.844  -1.659  -39.920 1.00 12.78 ? 179 ILE D CA  1 
ATOM   7878 C  C   . ILE D 1 179 ? -7.302  -2.723  -38.991 1.00 11.82 ? 179 ILE D C   1 
ATOM   7879 O  O   . ILE D 1 179 ? -6.073  -2.957  -38.968 1.00 11.13 ? 179 ILE D O   1 
ATOM   7880 C  CB  . ILE D 1 179 ? -7.602  -0.223  -39.360 1.00 12.60 ? 179 ILE D CB  1 
ATOM   7881 C  CG1 . ILE D 1 179 ? -8.171  0.815   -40.342 1.00 12.40 ? 179 ILE D CG1 1 
ATOM   7882 C  CG2 . ILE D 1 179 ? -6.097  0.080   -39.012 1.00 10.79 ? 179 ILE D CG2 1 
ATOM   7883 C  CD1 . ILE D 1 179 ? -7.457  0.782   -41.719 1.00 13.22 ? 179 ILE D CD1 1 
ATOM   7884 N  N   A GLU D 1 180 ? -8.180  -3.419  -38.232 0.50 11.44 ? 180 GLU D N   1 
ATOM   7885 N  N   B GLU D 1 180 ? -8.162  -3.376  -38.179 0.50 12.76 ? 180 GLU D N   1 
ATOM   7886 C  CA  A GLU D 1 180 ? -7.740  -4.492  -37.369 0.50 11.77 ? 180 GLU D CA  1 
ATOM   7887 C  CA  B GLU D 1 180 ? -7.688  -4.445  -37.314 0.50 13.96 ? 180 GLU D CA  1 
ATOM   7888 C  C   A GLU D 1 180 ? -7.173  -5.626  -38.188 0.50 10.91 ? 180 GLU D C   1 
ATOM   7889 C  C   B GLU D 1 180 ? -7.206  -5.649  -38.164 0.50 12.19 ? 180 GLU D C   1 
ATOM   7890 O  O   A GLU D 1 180 ? -6.364  -6.370  -37.654 0.50 11.67 ? 180 GLU D O   1 
ATOM   7891 O  O   B GLU D 1 180 ? -6.441  -6.445  -37.636 0.50 13.02 ? 180 GLU D O   1 
ATOM   7892 C  CB  A GLU D 1 180 ? -8.873  -5.034  -36.479 0.50 11.97 ? 180 GLU D CB  1 
ATOM   7893 C  CB  B GLU D 1 180 ? -8.689  -4.790  -36.147 0.50 17.29 ? 180 GLU D CB  1 
ATOM   7894 C  CG  A GLU D 1 180 ? -8.286  -5.538  -35.154 0.50 12.77 ? 180 GLU D CG  1 
ATOM   7895 C  CG  B GLU D 1 180 ? -10.162 -4.829  -36.489 0.50 21.09 ? 180 GLU D CG  1 
ATOM   7896 C  CD  A GLU D 1 180 ? -9.317  -5.732  -34.055 0.50 14.15 ? 180 GLU D CD  1 
ATOM   7897 C  CD  B GLU D 1 180 ? -11.115 -4.340  -35.370 0.50 21.89 ? 180 GLU D CD  1 
ATOM   7898 O  OE1 A GLU D 1 180 ? -10.427 -5.282  -34.222 0.50 13.44 ? 180 GLU D OE1 1 
ATOM   7899 O  OE1 B GLU D 1 180 ? -10.793 -4.496  -34.151 0.50 23.81 ? 180 GLU D OE1 1 
ATOM   7900 O  OE2 A GLU D 1 180 ? -8.959  -6.332  -33.056 0.50 15.73 ? 180 GLU D OE2 1 
ATOM   7901 O  OE2 B GLU D 1 180 ? -12.208 -3.823  -35.750 0.50 17.04 ? 180 GLU D OE2 1 
ATOM   7902 N  N   . GLU D 1 181 ? -7.584  -5.714  -39.450 1.00 12.34 ? 181 GLU D N   1 
ATOM   7903 C  CA  . GLU D 1 181 ? -7.020  -6.709  -40.377 1.00 11.69 ? 181 GLU D CA  1 
ATOM   7904 C  C   . GLU D 1 181 ? -5.503  -6.583  -40.609 1.00 12.91 ? 181 GLU D C   1 
ATOM   7905 O  O   . GLU D 1 181 ? -4.859  -7.538  -41.057 1.00 13.21 ? 181 GLU D O   1 
ATOM   7906 C  CB  . GLU D 1 181 ? -7.746  -6.628  -41.684 1.00 13.99 ? 181 GLU D CB  1 
ATOM   7907 C  CG  . GLU D 1 181 ? -9.182  -7.142  -41.624 1.00 15.94 ? 181 GLU D CG  1 
ATOM   7908 C  CD  . GLU D 1 181 ? -9.887  -6.973  -42.962 1.00 19.24 ? 181 GLU D CD  1 
ATOM   7909 O  OE1 . GLU D 1 181 ? -9.241  -6.615  -44.016 1.00 21.21 ? 181 GLU D OE1 1 
ATOM   7910 O  OE2 . GLU D 1 181 ? -11.130 -7.189  -43.009 1.00 19.54 ? 181 GLU D OE2 1 
ATOM   7911 N  N   . LEU D 1 182 ? -5.003  -5.379  -40.329 1.00 12.03 ? 182 LEU D N   1 
ATOM   7912 C  CA  . LEU D 1 182 ? -3.560  -5.103  -40.400 1.00 10.46 ? 182 LEU D CA  1 
ATOM   7913 C  C   . LEU D 1 182 ? -2.777  -5.582  -39.182 1.00 11.27 ? 182 LEU D C   1 
ATOM   7914 O  O   . LEU D 1 182 ? -1.518  -5.619  -39.245 1.00 11.22 ? 182 LEU D O   1 
ATOM   7915 C  CB  . LEU D 1 182 ? -3.316  -3.578  -40.626 1.00 9.52  ? 182 LEU D CB  1 
ATOM   7916 C  CG  . LEU D 1 182 ? -4.006  -2.981  -41.865 1.00 9.05  ? 182 LEU D CG  1 
ATOM   7917 C  CD1 . LEU D 1 182 ? -3.651  -1.516  -41.971 1.00 9.74  ? 182 LEU D CD1 1 
ATOM   7918 C  CD2 . LEU D 1 182 ? -3.646  -3.631  -43.199 1.00 9.47  ? 182 LEU D CD2 1 
ATOM   7919 N  N   . LEU D 1 183 ? -3.447  -5.918  -38.083 1.00 10.99 ? 183 LEU D N   1 
ATOM   7920 C  CA  . LEU D 1 183 ? -2.770  -6.321  -36.876 1.00 11.59 ? 183 LEU D CA  1 
ATOM   7921 C  C   . LEU D 1 183 ? -2.513  -7.779  -36.882 1.00 10.52 ? 183 LEU D C   1 
ATOM   7922 O  O   . LEU D 1 183 ? -3.198  -8.597  -37.587 1.00 11.82 ? 183 LEU D O   1 
ATOM   7923 C  CB  . LEU D 1 183 ? -3.680  -5.989  -35.654 1.00 13.28 ? 183 LEU D CB  1 
ATOM   7924 C  CG  . LEU D 1 183 ? -4.051  -4.502  -35.596 1.00 12.94 ? 183 LEU D CG  1 
ATOM   7925 C  CD1 . LEU D 1 183 ? -4.947  -4.216  -34.393 1.00 15.67 ? 183 LEU D CD1 1 
ATOM   7926 C  CD2 . LEU D 1 183 ? -2.845  -3.545  -35.482 1.00 14.87 ? 183 LEU D CD2 1 
ATOM   7927 N  N   . PRO D 1 184 ? -1.484  -8.194  -36.120 1.00 11.49 ? 184 PRO D N   1 
ATOM   7928 C  CA  . PRO D 1 184 ? -1.104  -9.629  -36.049 1.00 12.34 ? 184 PRO D CA  1 
ATOM   7929 C  C   . PRO D 1 184 ? -1.965  -10.393 -35.079 1.00 12.44 ? 184 PRO D C   1 
ATOM   7930 O  O   . PRO D 1 184 ? -2.918  -9.862  -34.448 1.00 15.17 ? 184 PRO D O   1 
ATOM   7931 C  CB  . PRO D 1 184 ? 0.355   -9.562  -35.531 1.00 12.96 ? 184 PRO D CB  1 
ATOM   7932 C  CG  . PRO D 1 184 ? 0.245   -8.363  -34.522 1.00 13.81 ? 184 PRO D CG  1 
ATOM   7933 C  CD  . PRO D 1 184 ? -0.594  -7.387  -35.285 1.00 12.35 ? 184 PRO D CD  1 
ATOM   7934 N  N   . GLU D 1 185 ? -1.650  -11.694 -35.052 1.00 15.93 ? 185 GLU D N   1 
ATOM   7935 C  CA  . GLU D 1 185 ? -2.249  -12.612 -34.090 1.00 17.54 ? 185 GLU D CA  1 
ATOM   7936 C  C   . GLU D 1 185 ? -1.862  -12.234 -32.680 1.00 17.22 ? 185 GLU D C   1 
ATOM   7937 O  O   . GLU D 1 185 ? -0.779  -11.629 -32.437 1.00 15.73 ? 185 GLU D O   1 
ATOM   7938 C  CB  . GLU D 1 185 ? -1.793  -14.047 -34.384 1.00 21.52 ? 185 GLU D CB  1 
ATOM   7939 C  CG  . GLU D 1 185 ? -2.328  -14.556 -35.708 1.00 24.97 ? 185 GLU D CG  1 
ATOM   7940 C  CD  . GLU D 1 185 ? -1.918  -16.020 -35.879 1.00 36.93 ? 185 GLU D CD  1 
ATOM   7941 O  OE1 . GLU D 1 185 ? -1.957  -16.760 -34.854 1.00 42.99 ? 185 GLU D OE1 1 
ATOM   7942 O  OE2 . GLU D 1 185 ? -1.552  -16.436 -37.017 1.00 44.01 ? 185 GLU D OE2 1 
ATOM   7943 N  N   . ARG D 1 186 ? -2.774  -12.496 -31.752 1.00 14.22 ? 186 ARG D N   1 
ATOM   7944 C  CA  . ARG D 1 186 ? -2.493  -12.381 -30.341 1.00 15.21 ? 186 ARG D CA  1 
ATOM   7945 C  C   . ARG D 1 186 ? -1.998  -11.004 -29.954 1.00 14.49 ? 186 ARG D C   1 
ATOM   7946 O  O   . ARG D 1 186 ? -0.879  -10.819 -29.388 1.00 14.61 ? 186 ARG D O   1 
ATOM   7947 C  CB  . ARG D 1 186 ? -1.518  -13.481 -29.877 1.00 19.27 ? 186 ARG D CB  1 
ATOM   7948 C  CG  . ARG D 1 186 ? -2.184  -14.859 -29.918 1.00 23.49 ? 186 ARG D CG  1 
ATOM   7949 C  CD  . ARG D 1 186 ? -1.304  -16.065 -29.566 1.00 27.96 ? 186 ARG D CD  1 
ATOM   7950 N  NE  . ARG D 1 186 ? -0.217  -16.295 -30.532 1.00 33.60 ? 186 ARG D NE  1 
ATOM   7951 C  CZ  . ARG D 1 186 ? -0.378  -16.766 -31.779 1.00 35.56 ? 186 ARG D CZ  1 
ATOM   7952 N  NH1 . ARG D 1 186 ? -1.588  -17.073 -32.247 1.00 39.76 ? 186 ARG D NH1 1 
ATOM   7953 N  NH2 . ARG D 1 186 ? 0.671   -16.901 -32.569 1.00 33.69 ? 186 ARG D NH2 1 
ATOM   7954 N  N   . THR D 1 187 ? -2.787  -10.023 -30.306 1.00 14.06 ? 187 THR D N   1 
ATOM   7955 C  CA  . THR D 1 187 ? -2.412  -8.631  -29.980 1.00 14.37 ? 187 THR D CA  1 
ATOM   7956 C  C   . THR D 1 187 ? -2.259  -8.330  -28.479 1.00 14.06 ? 187 THR D C   1 
ATOM   7957 O  O   . THR D 1 187 ? -1.714  -7.285  -28.072 1.00 13.25 ? 187 THR D O   1 
ATOM   7958 C  CB  . THR D 1 187 ? -3.399  -7.618  -30.579 1.00 13.18 ? 187 THR D CB  1 
ATOM   7959 O  OG1 . THR D 1 187 ? -4.756  -7.906  -30.185 1.00 16.51 ? 187 THR D OG1 1 
ATOM   7960 C  CG2 . THR D 1 187 ? -3.358  -7.611  -32.155 1.00 14.75 ? 187 THR D CG2 1 
ATOM   7961 N  N   . ALA D 1 188 ? -2.751  -9.207  -27.605 1.00 14.90 ? 188 ALA D N   1 
ATOM   7962 C  CA  . ALA D 1 188 ? -2.549  -8.982  -26.177 1.00 13.82 ? 188 ALA D CA  1 
ATOM   7963 C  C   . ALA D 1 188 ? -1.054  -9.151  -25.762 1.00 12.34 ? 188 ALA D C   1 
ATOM   7964 O  O   . ALA D 1 188 ? -0.670  -8.689  -24.674 1.00 12.26 ? 188 ALA D O   1 
ATOM   7965 C  CB  . ALA D 1 188 ? -3.386  -9.993  -25.367 1.00 14.99 ? 188 ALA D CB  1 
ATOM   7966 N  N   . GLU D 1 189 ? -0.263  -9.808  -26.641 1.00 12.72 ? 189 GLU D N   1 
ATOM   7967 C  CA  . GLU D 1 189 ? 1.211   -10.011 -26.433 1.00 11.98 ? 189 GLU D CA  1 
ATOM   7968 C  C   . GLU D 1 189 ? 1.972   -8.866  -27.189 1.00 10.94 ? 189 GLU D C   1 
ATOM   7969 O  O   . GLU D 1 189 ? 1.969   -8.809  -28.401 1.00 11.78 ? 189 GLU D O   1 
ATOM   7970 C  CB  . GLU D 1 189 ? 1.637   -11.324 -27.011 1.00 16.85 ? 189 GLU D CB  1 
ATOM   7971 C  CG  . GLU D 1 189 ? 0.804   -12.428 -26.361 1.00 18.06 ? 189 GLU D CG  1 
ATOM   7972 C  CD  . GLU D 1 189 ? 1.271   -13.849 -26.715 1.00 25.02 ? 189 GLU D CD  1 
ATOM   7973 O  OE1 . GLU D 1 189 ? 2.364   -14.017 -27.231 1.00 22.36 ? 189 GLU D OE1 1 
ATOM   7974 O  OE2 . GLU D 1 189 ? 0.522   -14.830 -26.424 1.00 28.20 ? 189 GLU D OE2 1 
ATOM   7975 N  N   . TYR D 1 190 ? 2.635   -8.060  -26.389 1.00 11.36 ? 190 TYR D N   1 
ATOM   7976 C  CA  . TYR D 1 190 ? 3.307   -6.874  -26.942 1.00 10.30 ? 190 TYR D CA  1 
ATOM   7977 C  C   . TYR D 1 190 ? 4.378   -6.366  -26.046 1.00 11.14 ? 190 TYR D C   1 
ATOM   7978 O  O   . TYR D 1 190 ? 4.478   -6.708  -24.840 1.00 10.61 ? 190 TYR D O   1 
ATOM   7979 C  CB  . TYR D 1 190 ? 2.305   -5.698  -27.192 1.00 10.88 ? 190 TYR D CB  1 
ATOM   7980 C  CG  . TYR D 1 190 ? 1.533   -5.247  -25.991 1.00 10.84 ? 190 TYR D CG  1 
ATOM   7981 C  CD1 . TYR D 1 190 ? 2.093   -4.375  -25.083 1.00 10.59 ? 190 TYR D CD1 1 
ATOM   7982 C  CD2 . TYR D 1 190 ? 0.205   -5.691  -25.812 1.00 12.07 ? 190 TYR D CD2 1 
ATOM   7983 C  CE1 . TYR D 1 190 ? 1.348   -3.893  -23.955 1.00 10.95 ? 190 TYR D CE1 1 
ATOM   7984 C  CE2 . TYR D 1 190 ? -0.536  -5.262  -24.711 1.00 12.65 ? 190 TYR D CE2 1 
ATOM   7985 C  CZ  . TYR D 1 190 ? 0.072   -4.396  -23.797 1.00 12.49 ? 190 TYR D CZ  1 
ATOM   7986 O  OH  . TYR D 1 190 ? -0.682  -3.900  -22.742 1.00 12.36 ? 190 TYR D OH  1 
ATOM   7987 N  N   . TYR D 1 191 ? 5.259   -5.576  -26.666 1.00 9.77  ? 191 TYR D N   1 
ATOM   7988 C  CA  . TYR D 1 191 ? 6.353   -4.869  -26.001 1.00 10.45 ? 191 TYR D CA  1 
ATOM   7989 C  C   . TYR D 1 191 ? 5.878   -3.423  -25.827 1.00 9.66  ? 191 TYR D C   1 
ATOM   7990 O  O   . TYR D 1 191 ? 5.255   -2.850  -26.707 1.00 10.23 ? 191 TYR D O   1 
ATOM   7991 C  CB  . TYR D 1 191 ? 7.575   -4.771  -26.929 1.00 10.49 ? 191 TYR D CB  1 
ATOM   7992 C  CG  . TYR D 1 191 ? 8.122   -6.098  -27.422 1.00 10.19 ? 191 TYR D CG  1 
ATOM   7993 C  CD1 . TYR D 1 191 ? 9.108   -6.794  -26.711 1.00 10.90 ? 191 TYR D CD1 1 
ATOM   7994 C  CD2 . TYR D 1 191 ? 7.697   -6.606  -28.672 1.00 11.63 ? 191 TYR D CD2 1 
ATOM   7995 C  CE1 . TYR D 1 191 ? 9.621   -7.966  -27.193 1.00 11.00 ? 191 TYR D CE1 1 
ATOM   7996 C  CE2 . TYR D 1 191 ? 8.237   -7.825  -29.171 1.00 12.08 ? 191 TYR D CE2 1 
ATOM   7997 C  CZ  . TYR D 1 191 ? 9.228   -8.462  -28.408 1.00 12.37 ? 191 TYR D CZ  1 
ATOM   7998 O  OH  . TYR D 1 191 ? 9.801   -9.650  -28.870 1.00 16.43 ? 191 TYR D OH  1 
ATOM   7999 N  N   . ARG D 1 192 ? 6.170   -2.799  -24.705 1.00 9.94  ? 192 ARG D N   1 
ATOM   8000 C  CA  . ARG D 1 192 ? 5.765   -1.413  -24.491 1.00 11.16 ? 192 ARG D CA  1 
ATOM   8001 C  C   . ARG D 1 192 ? 6.979   -0.656  -23.896 1.00 10.38 ? 192 ARG D C   1 
ATOM   8002 O  O   . ARG D 1 192 ? 7.631   -1.124  -22.988 1.00 11.63 ? 192 ARG D O   1 
ATOM   8003 C  CB  . ARG D 1 192 ? 4.546   -1.420  -23.605 1.00 13.18 ? 192 ARG D CB  1 
ATOM   8004 C  CG  . ARG D 1 192 ? 4.338   -0.194  -22.813 1.00 18.02 ? 192 ARG D CG  1 
ATOM   8005 C  CD  . ARG D 1 192 ? 3.302   0.758   -23.404 1.00 17.84 ? 192 ARG D CD  1 
ATOM   8006 N  NE  . ARG D 1 192 ? 2.243   0.113   -24.180 1.00 20.40 ? 192 ARG D NE  1 
ATOM   8007 C  CZ  . ARG D 1 192 ? 1.064   -0.254  -23.685 1.00 17.75 ? 192 ARG D CZ  1 
ATOM   8008 N  NH1 . ARG D 1 192 ? 0.792   -0.068  -22.401 1.00 22.56 ? 192 ARG D NH1 1 
ATOM   8009 N  NH2 . ARG D 1 192 ? 0.158   -0.819  -24.475 1.00 18.28 ? 192 ARG D NH2 1 
ATOM   8010 N  N   . TYR D 1 193 ? 7.239   0.528   -24.427 1.00 10.30 ? 193 TYR D N   1 
ATOM   8011 C  CA  . TYR D 1 193 ? 8.272   1.375   -23.810 1.00 9.66  ? 193 TYR D CA  1 
ATOM   8012 C  C   . TYR D 1 193 ? 8.041   2.868   -24.158 1.00 9.47  ? 193 TYR D C   1 
ATOM   8013 O  O   . TYR D 1 193 ? 7.283   3.203   -25.071 1.00 11.89 ? 193 TYR D O   1 
ATOM   8014 C  CB  . TYR D 1 193 ? 9.668   0.935   -24.320 1.00 10.28 ? 193 TYR D CB  1 
ATOM   8015 C  CG  . TYR D 1 193 ? 9.968   1.346   -25.757 1.00 9.83  ? 193 TYR D CG  1 
ATOM   8016 C  CD1 . TYR D 1 193 ? 10.799  2.452   -25.958 1.00 9.60  ? 193 TYR D CD1 1 
ATOM   8017 C  CD2 . TYR D 1 193 ? 9.539   0.584   -26.857 1.00 10.31 ? 193 TYR D CD2 1 
ATOM   8018 C  CE1 . TYR D 1 193 ? 11.096  2.874   -27.263 1.00 10.26 ? 193 TYR D CE1 1 
ATOM   8019 C  CE2 . TYR D 1 193 ? 9.816   1.018   -28.155 1.00 9.73  ? 193 TYR D CE2 1 
ATOM   8020 C  CZ  . TYR D 1 193 ? 10.612  2.149   -28.329 1.00 10.51 ? 193 TYR D CZ  1 
ATOM   8021 O  OH  . TYR D 1 193 ? 10.944  2.620   -29.589 1.00 10.17 ? 193 TYR D OH  1 
ATOM   8022 N  N   . ARG D 1 194 ? 8.758   3.739   -23.450 1.00 10.69 ? 194 ARG D N   1 
ATOM   8023 C  CA  . ARG D 1 194 ? 8.613   5.199   -23.662 1.00 10.86 ? 194 ARG D CA  1 
ATOM   8024 C  C   . ARG D 1 194 ? 9.722   5.637   -24.627 1.00 11.02 ? 194 ARG D C   1 
ATOM   8025 O  O   . ARG D 1 194 ? 10.928  5.326   -24.399 1.00 12.03 ? 194 ARG D O   1 
ATOM   8026 C  CB  . ARG D 1 194 ? 8.908   5.923   -22.346 1.00 14.95 ? 194 ARG D CB  1 
ATOM   8027 C  CG  . ARG D 1 194 ? 7.913   5.507   -21.295 1.00 18.07 ? 194 ARG D CG  1 
ATOM   8028 C  CD  . ARG D 1 194 ? 6.812   6.486   -21.305 1.00 24.52 ? 194 ARG D CD  1 
ATOM   8029 N  NE  . ARG D 1 194 ? 5.796   6.085   -20.340 1.00 34.62 ? 194 ARG D NE  1 
ATOM   8030 C  CZ  . ARG D 1 194 ? 4.659   6.744   -20.180 1.00 38.53 ? 194 ARG D CZ  1 
ATOM   8031 N  NH1 . ARG D 1 194 ? 4.450   7.838   -20.926 1.00 32.97 ? 194 ARG D NH1 1 
ATOM   8032 N  NH2 . ARG D 1 194 ? 3.739   6.298   -19.297 1.00 35.72 ? 194 ARG D NH2 1 
ATOM   8033 N  N   . GLY D 1 195 ? 9.277   6.253   -25.710 1.00 8.25  ? 195 GLY D N   1 
ATOM   8034 C  CA  . GLY D 1 195 ? 10.228  6.701   -26.760 1.00 10.40 ? 195 GLY D CA  1 
ATOM   8035 C  C   . GLY D 1 195 ? 9.851   7.965   -27.384 1.00 10.45 ? 195 GLY D C   1 
ATOM   8036 O  O   . GLY D 1 195 ? 9.282   8.874   -26.782 1.00 9.52  ? 195 GLY D O   1 
ATOM   8037 N  N   . SER D 1 196 ? 10.205  8.034   -28.659 1.00 9.35  ? 196 SER D N   1 
ATOM   8038 C  CA  . SER D 1 196 ? 10.133  9.245   -29.421 1.00 8.91  ? 196 SER D CA  1 
ATOM   8039 C  C   . SER D 1 196 ? 9.536   8.976   -30.792 1.00 8.59  ? 196 SER D C   1 
ATOM   8040 O  O   . SER D 1 196 ? 9.391   7.802   -31.268 1.00 8.27  ? 196 SER D O   1 
ATOM   8041 C  CB  . SER D 1 196 ? 11.515  9.876   -29.595 1.00 9.74  ? 196 SER D CB  1 
ATOM   8042 O  OG  . SER D 1 196 ? 12.273  9.106   -30.579 1.00 8.23  ? 196 SER D OG  1 
ATOM   8043 N  N   . LEU D 1 197 ? 9.259   10.045  -31.486 1.00 8.11  ? 197 LEU D N   1 
ATOM   8044 C  CA  . LEU D 1 197 ? 9.022   9.954   -32.939 1.00 9.22  ? 197 LEU D CA  1 
ATOM   8045 C  C   . LEU D 1 197 ? 10.313  9.473   -33.628 1.00 9.43  ? 197 LEU D C   1 
ATOM   8046 O  O   . LEU D 1 197 ? 11.406  9.826   -33.178 1.00 10.01 ? 197 LEU D O   1 
ATOM   8047 C  CB  . LEU D 1 197 ? 8.717   11.342  -33.514 1.00 11.16 ? 197 LEU D CB  1 
ATOM   8048 C  CG  . LEU D 1 197 ? 7.353   11.924  -33.329 1.00 11.92 ? 197 LEU D CG  1 
ATOM   8049 C  CD1 . LEU D 1 197 ? 7.201   12.390  -31.914 1.00 14.91 ? 197 LEU D CD1 1 
ATOM   8050 C  CD2 . LEU D 1 197 ? 7.338   13.183  -34.242 1.00 16.06 ? 197 LEU D CD2 1 
ATOM   8051 N  N   . THR D 1 198 ? 10.174  8.543   -34.593 1.00 8.56  ? 198 THR D N   1 
ATOM   8052 C  CA  . THR D 1 198 ? 11.409  8.082   -35.242 1.00 9.16  ? 198 THR D CA  1 
ATOM   8053 C  C   . THR D 1 198 ? 11.852  8.976   -36.390 1.00 9.35  ? 198 THR D C   1 
ATOM   8054 O  O   . THR D 1 198 ? 12.801  8.622   -37.121 1.00 10.45 ? 198 THR D O   1 
ATOM   8055 C  CB  . THR D 1 198 ? 11.268  6.679   -35.763 1.00 8.44  ? 198 THR D CB  1 
ATOM   8056 O  OG1 . THR D 1 198 ? 10.255  6.690   -36.782 1.00 8.09  ? 198 THR D OG1 1 
ATOM   8057 C  CG2 . THR D 1 198 ? 10.781  5.736   -34.665 1.00 9.60  ? 198 THR D CG2 1 
ATOM   8058 N  N   . THR D 1 199 ? 11.188  10.119  -36.562 1.00 9.35  ? 199 THR D N   1 
ATOM   8059 C  CA  . THR D 1 199 ? 11.521  11.092  -37.622 1.00 10.32 ? 199 THR D CA  1 
ATOM   8060 C  C   . THR D 1 199 ? 11.662  12.413  -36.897 1.00 10.72 ? 199 THR D C   1 
ATOM   8061 O  O   . THR D 1 199 ? 10.964  12.635  -35.914 1.00 12.00 ? 199 THR D O   1 
ATOM   8062 C  CB  . THR D 1 199 ? 10.315  11.210  -38.603 1.00 11.86 ? 199 THR D CB  1 
ATOM   8063 O  OG1 . THR D 1 199 ? 9.124   11.541  -37.861 1.00 13.72 ? 199 THR D OG1 1 
ATOM   8064 C  CG2 . THR D 1 199 ? 10.065  9.810   -39.251 1.00 13.34 ? 199 THR D CG2 1 
ATOM   8065 N  N   . PRO D 1 200 ? 12.313  13.345  -37.554 1.00 9.24  ? 200 PRO D N   1 
ATOM   8066 C  CA  . PRO D 1 200 ? 12.282  14.717  -37.070 1.00 10.28 ? 200 PRO D CA  1 
ATOM   8067 C  C   . PRO D 1 200 ? 10.842  15.143  -36.823 1.00 10.57 ? 200 PRO D C   1 
ATOM   8068 O  O   . PRO D 1 200 ? 9.981   14.912  -37.691 1.00 10.67 ? 200 PRO D O   1 
ATOM   8069 C  CB  . PRO D 1 200 ? 12.862  15.463  -38.256 1.00 8.97  ? 200 PRO D CB  1 
ATOM   8070 C  CG  . PRO D 1 200 ? 13.903  14.522  -38.775 1.00 9.53  ? 200 PRO D CG  1 
ATOM   8071 C  CD  . PRO D 1 200 ? 13.205  13.175  -38.741 1.00 9.04  ? 200 PRO D CD  1 
ATOM   8072 N  N   . PRO D 1 201 ? 10.606  15.951  -35.764 1.00 10.78 ? 201 PRO D N   1 
ATOM   8073 C  CA  . PRO D 1 201 ? 11.560  16.465  -34.828 1.00 10.91 ? 201 PRO D CA  1 
ATOM   8074 C  C   . PRO D 1 201 ? 11.949  15.595  -33.694 1.00 11.34 ? 201 PRO D C   1 
ATOM   8075 O  O   . PRO D 1 201 ? 12.558  16.048  -32.732 1.00 11.38 ? 201 PRO D O   1 
ATOM   8076 C  CB  . PRO D 1 201 ? 10.821  17.730  -34.233 1.00 12.25 ? 201 PRO D CB  1 
ATOM   8077 C  CG  . PRO D 1 201 ? 9.697   17.921  -35.101 1.00 14.28 ? 201 PRO D CG  1 
ATOM   8078 C  CD  . PRO D 1 201 ? 9.296   16.584  -35.606 1.00 12.75 ? 201 PRO D CD  1 
ATOM   8079 N  N   . CYS D 1 202 ? 11.571  14.289  -33.757 1.00 9.81  ? 202 CYS D N   1 
ATOM   8080 C  CA  . CYS D 1 202 ? 12.072  13.283  -32.800 1.00 10.10 ? 202 CYS D CA  1 
ATOM   8081 C  C   . CYS D 1 202 ? 11.629  13.530  -31.336 1.00 10.72 ? 202 CYS D C   1 
ATOM   8082 O  O   . CYS D 1 202 ? 12.319  13.186  -30.429 1.00 12.15 ? 202 CYS D O   1 
ATOM   8083 C  CB  . CYS D 1 202 ? 13.598  13.158  -32.770 1.00 9.63  ? 202 CYS D CB  1 
ATOM   8084 S  SG  . CYS D 1 202 ? 14.345  12.812  -34.422 1.00 11.72 ? 202 CYS D SG  1 
ATOM   8085 N  N   . ASN D 1 203 ? 10.452  14.130  -31.205 1.00 11.69 ? 203 ASN D N   1 
ATOM   8086 C  CA  . ASN D 1 203 ? 10.041  14.490  -29.833 1.00 12.09 ? 203 ASN D CA  1 
ATOM   8087 C  C   . ASN D 1 203 ? 9.876   13.268  -28.976 1.00 12.22 ? 203 ASN D C   1 
ATOM   8088 O  O   . ASN D 1 203 ? 9.305   12.267  -29.475 1.00 10.21 ? 203 ASN D O   1 
ATOM   8089 C  CB  . ASN D 1 203 ? 8.731   15.234  -29.867 1.00 12.31 ? 203 ASN D CB  1 
ATOM   8090 C  CG  . ASN D 1 203 ? 8.820   16.450  -30.773 1.00 14.16 ? 203 ASN D CG  1 
ATOM   8091 O  OD1 . ASN D 1 203 ? 8.737   16.340  -31.984 1.00 15.31 ? 203 ASN D OD1 1 
ATOM   8092 N  ND2 . ASN D 1 203 ? 9.123   17.551  -30.171 1.00 17.41 ? 203 ASN D ND2 1 
ATOM   8093 N  N   . PRO D 1 204 ? 10.314  13.320  -27.721 1.00 11.37 ? 204 PRO D N   1 
ATOM   8094 C  CA  . PRO D 1 204 ? 10.245  12.181  -26.808 1.00 10.79 ? 204 PRO D CA  1 
ATOM   8095 C  C   . PRO D 1 204 ? 8.866   12.060  -26.105 1.00 11.60 ? 204 PRO D C   1 
ATOM   8096 O  O   . PRO D 1 204 ? 8.751   12.143  -24.847 1.00 12.91 ? 204 PRO D O   1 
ATOM   8097 C  CB  . PRO D 1 204 ? 11.390  12.457  -25.797 1.00 13.17 ? 204 PRO D CB  1 
ATOM   8098 C  CG  . PRO D 1 204 ? 11.360  13.996  -25.745 1.00 11.63 ? 204 PRO D CG  1 
ATOM   8099 C  CD  . PRO D 1 204 ? 11.149  14.421  -27.149 1.00 11.85 ? 204 PRO D CD  1 
ATOM   8100 N  N   . THR D 1 205 ? 7.860   11.883  -26.947 1.00 9.89  ? 205 THR D N   1 
ATOM   8101 C  CA  . THR D 1 205 ? 6.439   12.019  -26.548 1.00 9.52  ? 205 THR D CA  1 
ATOM   8102 C  C   . THR D 1 205 ? 5.583   10.822  -26.979 1.00 9.57  ? 205 THR D C   1 
ATOM   8103 O  O   . THR D 1 205 ? 4.353   10.903  -26.934 1.00 10.74 ? 205 THR D O   1 
ATOM   8104 C  CB  . THR D 1 205 ? 5.842   13.247  -27.203 1.00 10.39 ? 205 THR D CB  1 
ATOM   8105 O  OG1 . THR D 1 205 ? 5.992   13.134  -28.638 1.00 10.71 ? 205 THR D OG1 1 
ATOM   8106 C  CG2 . THR D 1 205 ? 6.477   14.623  -26.733 1.00 10.95 ? 205 THR D CG2 1 
ATOM   8107 N  N   . VAL D 1 206 ? 6.239   9.738   -27.359 1.00 9.45  ? 206 VAL D N   1 
ATOM   8108 C  CA  . VAL D 1 206 ? 5.539   8.579   -27.849 1.00 8.78  ? 206 VAL D CA  1 
ATOM   8109 C  C   . VAL D 1 206 ? 5.583   7.383   -26.854 1.00 8.82  ? 206 VAL D C   1 
ATOM   8110 O  O   . VAL D 1 206 ? 6.592   6.909   -26.451 1.00 9.97  ? 206 VAL D O   1 
ATOM   8111 C  CB  . VAL D 1 206 ? 6.127   8.094   -29.203 1.00 8.30  ? 206 VAL D CB  1 
ATOM   8112 C  CG1 . VAL D 1 206 ? 5.404   6.844   -29.689 1.00 8.44  ? 206 VAL D CG1 1 
ATOM   8113 C  CG2 . VAL D 1 206 ? 6.129   9.143   -30.270 1.00 7.85  ? 206 VAL D CG2 1 
ATOM   8114 N  N   . LEU D 1 207 ? 4.409   6.896   -26.513 1.00 10.34 ? 207 LEU D N   1 
ATOM   8115 C  CA  . LEU D 1 207 ? 4.310   5.629   -25.874 1.00 11.27 ? 207 LEU D CA  1 
ATOM   8116 C  C   . LEU D 1 207 ? 4.223   4.557   -26.970 1.00 10.00 ? 207 LEU D C   1 
ATOM   8117 O  O   . LEU D 1 207 ? 3.238   4.567   -27.722 1.00 10.39 ? 207 LEU D O   1 
ATOM   8118 C  CB  . LEU D 1 207 ? 3.010   5.567   -25.027 1.00 12.06 ? 207 LEU D CB  1 
ATOM   8119 C  CG  . LEU D 1 207 ? 2.916   4.308   -24.178 1.00 14.24 ? 207 LEU D CG  1 
ATOM   8120 C  CD1 . LEU D 1 207 ? 4.030   4.155   -23.186 1.00 14.75 ? 207 LEU D CD1 1 
ATOM   8121 C  CD2 . LEU D 1 207 ? 1.592   4.411   -23.427 1.00 17.88 ? 207 LEU D CD2 1 
ATOM   8122 N  N   . TRP D 1 208 ? 5.235   3.738   -27.078 1.00 8.82  ? 208 TRP D N   1 
ATOM   8123 C  CA  . TRP D 1 208 ? 5.263   2.657   -28.102 1.00 8.06  ? 208 TRP D CA  1 
ATOM   8124 C  C   . TRP D 1 208 ? 4.676   1.331   -27.682 1.00 8.01  ? 208 TRP D C   1 
ATOM   8125 O  O   . TRP D 1 208 ? 5.013   0.882   -26.588 1.00 9.02  ? 208 TRP D O   1 
ATOM   8126 C  CB  . TRP D 1 208 ? 6.770   2.442   -28.493 1.00 8.68  ? 208 TRP D CB  1 
ATOM   8127 C  CG  . TRP D 1 208 ? 7.260   3.501   -29.427 1.00 8.52  ? 208 TRP D CG  1 
ATOM   8128 C  CD1 . TRP D 1 208 ? 8.048   4.606   -29.132 1.00 9.20  ? 208 TRP D CD1 1 
ATOM   8129 C  CD2 . TRP D 1 208 ? 7.086   3.508   -30.879 1.00 8.10  ? 208 TRP D CD2 1 
ATOM   8130 N  NE1 . TRP D 1 208 ? 8.214   5.392   -30.253 1.00 8.38  ? 208 TRP D NE1 1 
ATOM   8131 C  CE2 . TRP D 1 208 ? 7.636   4.800   -31.349 1.00 8.04  ? 208 TRP D CE2 1 
ATOM   8132 C  CE3 . TRP D 1 208 ? 6.382   2.711   -31.781 1.00 9.22  ? 208 TRP D CE3 1 
ATOM   8133 C  CZ2 . TRP D 1 208 ? 7.605   5.180   -32.701 1.00 8.45  ? 208 TRP D CZ2 1 
ATOM   8134 C  CZ3 . TRP D 1 208 ? 6.371   3.107   -33.136 1.00 8.33  ? 208 TRP D CZ3 1 
ATOM   8135 C  CH2 . TRP D 1 208 ? 6.929   4.340   -33.589 1.00 9.01  ? 208 TRP D CH2 1 
ATOM   8136 N  N   . THR D 1 209 ? 3.868   0.751   -28.572 1.00 7.89  ? 209 THR D N   1 
ATOM   8137 C  CA  . THR D 1 209 ? 3.432   -0.599  -28.402 1.00 7.69  ? 209 THR D CA  1 
ATOM   8138 C  C   . THR D 1 209 ? 3.894   -1.305  -29.670 1.00 8.07  ? 209 THR D C   1 
ATOM   8139 O  O   . THR D 1 209 ? 3.376   -0.994  -30.738 1.00 8.94  ? 209 THR D O   1 
ATOM   8140 C  CB  . THR D 1 209 ? 1.878   -0.667  -28.278 1.00 9.51  ? 209 THR D CB  1 
ATOM   8141 O  OG1 . THR D 1 209 ? 1.532   0.045   -27.091 1.00 9.41  ? 209 THR D OG1 1 
ATOM   8142 C  CG2 . THR D 1 209 ? 1.443   -2.131  -27.999 1.00 10.20 ? 209 THR D CG2 1 
ATOM   8143 N  N   . VAL D 1 210 ? 4.722   -2.342  -29.520 1.00 8.47  ? 210 VAL D N   1 
ATOM   8144 C  CA  . VAL D 1 210 ? 5.210   -3.155  -30.659 1.00 8.30  ? 210 VAL D CA  1 
ATOM   8145 C  C   . VAL D 1 210 ? 4.614   -4.537  -30.438 1.00 8.93  ? 210 VAL D C   1 
ATOM   8146 O  O   . VAL D 1 210 ? 4.919   -5.170  -29.454 1.00 9.38  ? 210 VAL D O   1 
ATOM   8147 C  CB  . VAL D 1 210 ? 6.737   -3.203  -30.751 1.00 8.77  ? 210 VAL D CB  1 
ATOM   8148 C  CG1 . VAL D 1 210 ? 7.147   -4.072  -31.966 1.00 9.06  ? 210 VAL D CG1 1 
ATOM   8149 C  CG2 . VAL D 1 210 ? 7.349   -1.760  -30.821 1.00 8.78  ? 210 VAL D CG2 1 
ATOM   8150 N  N   . PHE D 1 211 ? 3.756   -5.005  -31.362 1.00 8.56  ? 211 PHE D N   1 
ATOM   8151 C  CA  . PHE D 1 211 ? 3.175   -6.320  -31.149 1.00 8.70  ? 211 PHE D CA  1 
ATOM   8152 C  C   . PHE D 1 211 ? 4.255   -7.432  -31.238 1.00 10.06 ? 211 PHE D C   1 
ATOM   8153 O  O   . PHE D 1 211 ? 5.217   -7.340  -32.010 1.00 10.89 ? 211 PHE D O   1 
ATOM   8154 C  CB  . PHE D 1 211 ? 2.058   -6.547  -32.124 1.00 9.31  ? 211 PHE D CB  1 
ATOM   8155 C  CG  . PHE D 1 211 ? 0.928   -5.617  -31.877 1.00 9.21  ? 211 PHE D CG  1 
ATOM   8156 C  CD1 . PHE D 1 211 ? 0.124   -5.833  -30.703 1.00 9.70  ? 211 PHE D CD1 1 
ATOM   8157 C  CD2 . PHE D 1 211 ? 0.627   -4.568  -32.701 1.00 9.80  ? 211 PHE D CD2 1 
ATOM   8158 C  CE1 . PHE D 1 211 ? -0.886  -4.930  -30.416 1.00 10.84 ? 211 PHE D CE1 1 
ATOM   8159 C  CE2 . PHE D 1 211 ? -0.444  -3.719  -32.455 1.00 10.60 ? 211 PHE D CE2 1 
ATOM   8160 C  CZ  . PHE D 1 211 ? -1.194  -3.870  -31.269 1.00 10.80 ? 211 PHE D CZ  1 
ATOM   8161 N  N   . ARG D 1 212 ? 4.094   -8.445  -30.414 1.00 11.15 ? 212 ARG D N   1 
ATOM   8162 C  CA  . ARG D 1 212 ? 5.106   -9.518  -30.386 1.00 10.69 ? 212 ARG D CA  1 
ATOM   8163 C  C   . ARG D 1 212 ? 5.170   -10.288 -31.701 1.00 11.34 ? 212 ARG D C   1 
ATOM   8164 O  O   . ARG D 1 212 ? 6.254   -10.614 -32.182 1.00 12.98 ? 212 ARG D O   1 
ATOM   8165 C  CB  . ARG D 1 212 ? 4.799   -10.499 -29.232 1.00 11.56 ? 212 ARG D CB  1 
ATOM   8166 C  CG  . ARG D 1 212 ? 5.792   -11.625 -29.166 1.00 13.52 ? 212 ARG D CG  1 
ATOM   8167 C  CD  . ARG D 1 212 ? 5.317   -12.587 -28.095 1.00 14.35 ? 212 ARG D CD  1 
ATOM   8168 N  NE  . ARG D 1 212 ? 6.358   -13.605 -27.827 1.00 15.08 ? 212 ARG D NE  1 
ATOM   8169 C  CZ  . ARG D 1 212 ? 6.217   -14.603 -26.987 1.00 19.37 ? 212 ARG D CZ  1 
ATOM   8170 N  NH1 . ARG D 1 212 ? 5.092   -14.799 -26.351 1.00 20.33 ? 212 ARG D NH1 1 
ATOM   8171 N  NH2 . ARG D 1 212 ? 7.224   -15.440 -26.820 1.00 21.20 ? 212 ARG D NH2 1 
ATOM   8172 N  N   . ASN D 1 213 ? 4.046   -10.552 -32.320 1.00 11.40 ? 213 ASN D N   1 
ATOM   8173 C  CA  . ASN D 1 213 ? 4.018   -11.382 -33.551 1.00 11.75 ? 213 ASN D CA  1 
ATOM   8174 C  C   . ASN D 1 213 ? 4.016   -10.463 -34.812 1.00 12.50 ? 213 ASN D C   1 
ATOM   8175 O  O   . ASN D 1 213 ? 3.280   -9.479  -34.858 1.00 12.10 ? 213 ASN D O   1 
ATOM   8176 C  CB  . ASN D 1 213 ? 2.722   -12.224 -33.535 1.00 13.69 ? 213 ASN D CB  1 
ATOM   8177 C  CG  . ASN D 1 213 ? 2.719   -13.175 -32.360 1.00 18.02 ? 213 ASN D CG  1 
ATOM   8178 O  OD1 . ASN D 1 213 ? 1.790   -13.158 -31.555 1.00 19.63 ? 213 ASN D OD1 1 
ATOM   8179 N  ND2 . ASN D 1 213 ? 3.763   -13.952 -32.233 1.00 19.65 ? 213 ASN D ND2 1 
ATOM   8180 N  N   . PRO D 1 214 ? 4.773   -10.816 -35.854 1.00 11.80 ? 214 PRO D N   1 
ATOM   8181 C  CA  . PRO D 1 214 ? 4.667   -10.092 -37.139 1.00 11.39 ? 214 PRO D CA  1 
ATOM   8182 C  C   . PRO D 1 214 ? 3.495   -10.523 -37.960 1.00 10.61 ? 214 PRO D C   1 
ATOM   8183 O  O   . PRO D 1 214 ? 2.869   -11.533 -37.641 1.00 12.88 ? 214 PRO D O   1 
ATOM   8184 C  CB  . PRO D 1 214 ? 5.969   -10.474 -37.887 1.00 12.10 ? 214 PRO D CB  1 
ATOM   8185 C  CG  . PRO D 1 214 ? 6.132   -11.924 -37.393 1.00 13.33 ? 214 PRO D CG  1 
ATOM   8186 C  CD  . PRO D 1 214 ? 5.754   -11.925 -35.895 1.00 13.26 ? 214 PRO D CD  1 
ATOM   8187 N  N   . VAL D 1 215 ? 3.180   -9.737  -38.973 1.00 10.18 ? 215 VAL D N   1 
ATOM   8188 C  CA  . VAL D 1 215 ? 2.342   -10.190 -40.075 1.00 10.14 ? 215 VAL D CA  1 
ATOM   8189 C  C   . VAL D 1 215 ? 3.212   -10.492 -41.270 1.00 10.58 ? 215 VAL D C   1 
ATOM   8190 O  O   . VAL D 1 215 ? 4.426   -10.175 -41.251 1.00 11.02 ? 215 VAL D O   1 
ATOM   8191 C  CB  . VAL D 1 215 ? 1.296   -9.125  -40.442 1.00 9.82  ? 215 VAL D CB  1 
ATOM   8192 C  CG1 . VAL D 1 215 ? 0.353   -8.822  -39.303 1.00 11.68 ? 215 VAL D CG1 1 
ATOM   8193 C  CG2 . VAL D 1 215 ? 1.923   -7.794  -40.972 1.00 10.21 ? 215 VAL D CG2 1 
ATOM   8194 N  N   . GLN D 1 216 ? 2.616   -11.055 -42.307 1.00 10.17 ? 216 GLN D N   1 
ATOM   8195 C  CA  . GLN D 1 216 ? 3.355   -11.337 -43.536 1.00 10.25 ? 216 GLN D CA  1 
ATOM   8196 C  C   . GLN D 1 216 ? 2.723   -10.582 -44.712 1.00 11.79 ? 216 GLN D C   1 
ATOM   8197 O  O   . GLN D 1 216 ? 1.496   -10.437 -44.838 1.00 12.05 ? 216 GLN D O   1 
ATOM   8198 C  CB  . GLN D 1 216 ? 3.269   -12.838 -43.915 1.00 12.98 ? 216 GLN D CB  1 
ATOM   8199 C  CG  . GLN D 1 216 ? 4.035   -13.671 -43.004 1.00 14.23 ? 216 GLN D CG  1 
ATOM   8200 C  CD  . GLN D 1 216 ? 3.944   -15.170 -43.326 1.00 15.65 ? 216 GLN D CD  1 
ATOM   8201 O  OE1 . GLN D 1 216 ? 3.434   -15.623 -44.363 1.00 16.05 ? 216 GLN D OE1 1 
ATOM   8202 N  NE2 . GLN D 1 216 ? 4.459   -15.978 -42.352 1.00 23.08 ? 216 GLN D NE2 1 
ATOM   8203 N  N   . ILE D 1 217 ? 3.564   -10.162 -45.628 1.00 9.91  ? 217 ILE D N   1 
ATOM   8204 C  CA  . ILE D 1 217 ? 3.116   -9.739  -46.945 1.00 9.92  ? 217 ILE D CA  1 
ATOM   8205 C  C   . ILE D 1 217 ? 4.095   -10.389 -47.950 1.00 9.37  ? 217 ILE D C   1 
ATOM   8206 O  O   . ILE D 1 217 ? 5.220   -10.786 -47.541 1.00 9.65  ? 217 ILE D O   1 
ATOM   8207 C  CB  . ILE D 1 217 ? 3.118   -8.181  -47.116 1.00 9.70  ? 217 ILE D CB  1 
ATOM   8208 C  CG1 . ILE D 1 217 ? 4.573   -7.621  -47.182 1.00 9.52  ? 217 ILE D CG1 1 
ATOM   8209 C  CG2 . ILE D 1 217 ? 2.284   -7.493  -46.077 1.00 12.12 ? 217 ILE D CG2 1 
ATOM   8210 C  CD1 . ILE D 1 217 ? 4.667   -6.051  -47.364 1.00 9.72  ? 217 ILE D CD1 1 
ATOM   8211 N  N   . SER D 1 218 ? 3.699   -10.484 -49.219 1.00 8.83  ? 218 SER D N   1 
ATOM   8212 C  CA  . SER D 1 218 ? 4.570   -11.202 -50.168 1.00 10.11 ? 218 SER D CA  1 
ATOM   8213 C  C   . SER D 1 218 ? 5.744   -10.452 -50.640 1.00 9.89  ? 218 SER D C   1 
ATOM   8214 O  O   . SER D 1 218 ? 5.794   -9.225  -50.533 1.00 10.78 ? 218 SER D O   1 
ATOM   8215 C  CB  . SER D 1 218 ? 3.739   -11.649 -51.344 1.00 10.83 ? 218 SER D CB  1 
ATOM   8216 O  OG  . SER D 1 218 ? 3.326   -10.607 -52.193 1.00 10.95 ? 218 SER D OG  1 
ATOM   8217 N  N   A GLN D 1 219 ? 6.671   -11.178 -51.247 0.50 10.65 ? 219 GLN D N   1 
ATOM   8218 N  N   B GLN D 1 219 ? 6.660   -11.186 -51.267 0.50 10.82 ? 219 GLN D N   1 
ATOM   8219 C  CA  A GLN D 1 219 ? 7.800   -10.503 -51.821 0.50 11.88 ? 219 GLN D CA  1 
ATOM   8220 C  CA  B GLN D 1 219 ? 7.774   -10.566 -51.957 0.50 12.25 ? 219 GLN D CA  1 
ATOM   8221 C  C   A GLN D 1 219 ? 7.371   -9.558  -52.989 0.50 10.82 ? 219 GLN D C   1 
ATOM   8222 C  C   B GLN D 1 219 ? 7.295   -9.481  -52.937 0.50 10.90 ? 219 GLN D C   1 
ATOM   8223 O  O   A GLN D 1 219 ? 8.018   -8.522  -53.194 0.50 11.91 ? 219 GLN D O   1 
ATOM   8224 O  O   B GLN D 1 219 ? 7.821   -8.312  -52.997 0.50 11.27 ? 219 GLN D O   1 
ATOM   8225 C  CB  A GLN D 1 219 ? 8.847   -11.506 -52.281 0.50 12.97 ? 219 GLN D CB  1 
ATOM   8226 C  CB  B GLN D 1 219 ? 8.468   -11.609 -52.815 0.50 13.65 ? 219 GLN D CB  1 
ATOM   8227 C  CG  A GLN D 1 219 ? 9.962   -10.926 -53.172 0.50 16.27 ? 219 GLN D CG  1 
ATOM   8228 C  CG  B GLN D 1 219 ? 9.865   -11.186 -53.251 0.50 17.56 ? 219 GLN D CG  1 
ATOM   8229 C  CD  A GLN D 1 219 ? 10.426  -9.521  -52.822 0.50 15.93 ? 219 GLN D CD  1 
ATOM   8230 C  CD  B GLN D 1 219 ? 9.873   -10.369 -54.523 0.50 16.39 ? 219 GLN D CD  1 
ATOM   8231 O  OE1 A GLN D 1 219 ? 10.329  -9.085  -51.671 0.50 18.24 ? 219 GLN D OE1 1 
ATOM   8232 O  OE1 B GLN D 1 219 ? 10.695  -9.458  -54.690 0.50 18.01 ? 219 GLN D OE1 1 
ATOM   8233 N  NE2 A GLN D 1 219 ? 10.888  -8.782  -53.831 0.50 15.31 ? 219 GLN D NE2 1 
ATOM   8234 N  NE2 B GLN D 1 219 ? 8.945   -10.647 -55.378 0.50 18.32 ? 219 GLN D NE2 1 
ATOM   8235 N  N   . GLU D 1 220 ? 6.265   -9.862  -53.672 1.00 10.53 ? 220 GLU D N   1 
ATOM   8236 C  CA  . GLU D 1 220 ? 5.794   -8.997  -54.759 1.00 11.26 ? 220 GLU D CA  1 
ATOM   8237 C  C   . GLU D 1 220 ? 5.171   -7.754  -54.154 1.00 10.11 ? 220 GLU D C   1 
ATOM   8238 O  O   . GLU D 1 220 ? 5.393   -6.626  -54.677 1.00 10.86 ? 220 GLU D O   1 
ATOM   8239 C  CB  . GLU D 1 220 ? 4.793   -9.669  -55.668 1.00 12.57 ? 220 GLU D CB  1 
ATOM   8240 C  CG  . GLU D 1 220 ? 5.394   -10.841 -56.483 1.00 14.89 ? 220 GLU D CG  1 
ATOM   8241 C  CD  . GLU D 1 220 ? 5.609   -12.124 -55.733 1.00 18.97 ? 220 GLU D CD  1 
ATOM   8242 O  OE1 . GLU D 1 220 ? 5.143   -12.321 -54.608 1.00 19.58 ? 220 GLU D OE1 1 
ATOM   8243 O  OE2 . GLU D 1 220 ? 6.280   -13.013 -56.330 1.00 25.76 ? 220 GLU D OE2 1 
ATOM   8244 N  N   . GLN D 1 221 ? 4.484   -7.889  -53.001 1.00 9.26  ? 221 GLN D N   1 
ATOM   8245 C  CA  . GLN D 1 221 ? 4.022   -6.663  -52.319 1.00 10.13 ? 221 GLN D CA  1 
ATOM   8246 C  C   . GLN D 1 221 ? 5.143   -5.795  -51.803 1.00 8.92  ? 221 GLN D C   1 
ATOM   8247 O  O   . GLN D 1 221 ? 5.105   -4.546  -51.986 1.00 10.32 ? 221 GLN D O   1 
ATOM   8248 C  CB  . GLN D 1 221 ? 3.098   -7.019  -51.204 1.00 8.58  ? 221 GLN D CB  1 
ATOM   8249 C  CG  . GLN D 1 221 ? 1.771   -7.646  -51.643 1.00 9.50  ? 221 GLN D CG  1 
ATOM   8250 C  CD  . GLN D 1 221 ? 0.903   -8.089  -50.503 1.00 8.93  ? 221 GLN D CD  1 
ATOM   8251 O  OE1 . GLN D 1 221 ? 1.208   -9.016  -49.704 1.00 9.63  ? 221 GLN D OE1 1 
ATOM   8252 N  NE2 . GLN D 1 221 ? -0.257  -7.404  -50.375 1.00 9.26  ? 221 GLN D NE2 1 
ATOM   8253 N  N   . LEU D 1 222 ? 6.170   -6.420  -51.218 1.00 9.86  ? 222 LEU D N   1 
ATOM   8254 C  CA  . LEU D 1 222 ? 7.279   -5.679  -50.693 1.00 10.05 ? 222 LEU D CA  1 
ATOM   8255 C  C   . LEU D 1 222 ? 8.019   -5.008  -51.845 1.00 10.06 ? 222 LEU D C   1 
ATOM   8256 O  O   . LEU D 1 222 ? 8.405   -3.809  -51.772 1.00 11.26 ? 222 LEU D O   1 
ATOM   8257 C  CB  . LEU D 1 222 ? 8.225   -6.641  -49.991 1.00 11.91 ? 222 LEU D CB  1 
ATOM   8258 C  CG  . LEU D 1 222 ? 7.833   -6.853  -48.562 1.00 15.00 ? 222 LEU D CG  1 
ATOM   8259 C  CD1 . LEU D 1 222 ? 8.665   -7.978  -48.020 1.00 14.63 ? 222 LEU D CD1 1 
ATOM   8260 C  CD2 . LEU D 1 222 ? 8.273   -5.636  -47.754 1.00 14.48 ? 222 LEU D CD2 1 
ATOM   8261 N  N   . LEU D 1 223 ? 8.168   -5.708  -52.977 1.00 8.98  ? 223 LEU D N   1 
ATOM   8262 C  CA  . LEU D 1 223 ? 8.868   -5.087  -54.126 1.00 10.61 ? 223 LEU D CA  1 
ATOM   8263 C  C   . LEU D 1 223 ? 8.097   -3.879  -54.661 1.00 11.15 ? 223 LEU D C   1 
ATOM   8264 O  O   . LEU D 1 223 ? 8.693   -2.878  -55.039 1.00 11.84 ? 223 LEU D O   1 
ATOM   8265 C  CB  . LEU D 1 223 ? 9.059   -6.113  -55.232 1.00 10.70 ? 223 LEU D CB  1 
ATOM   8266 C  CG  . LEU D 1 223 ? 9.850   -5.560  -56.422 1.00 14.08 ? 223 LEU D CG  1 
ATOM   8267 C  CD1 . LEU D 1 223 ? 11.257  -5.262  -55.906 1.00 15.17 ? 223 LEU D CD1 1 
ATOM   8268 C  CD2 . LEU D 1 223 ? 9.928   -6.669  -57.489 1.00 15.02 ? 223 LEU D CD2 1 
ATOM   8269 N  N   . ALA D 1 224 ? 6.763   -3.963  -54.688 1.00 11.01 ? 224 ALA D N   1 
ATOM   8270 C  CA  . ALA D 1 224 ? 5.955   -2.821  -55.169 1.00 13.11 ? 224 ALA D CA  1 
ATOM   8271 C  C   . ALA D 1 224 ? 6.138   -1.638  -54.212 1.00 13.97 ? 224 ALA D C   1 
ATOM   8272 O  O   . ALA D 1 224 ? 6.426   -0.515  -54.628 1.00 14.28 ? 224 ALA D O   1 
ATOM   8273 C  CB  . ALA D 1 224 ? 4.476   -3.241  -55.281 1.00 14.72 ? 224 ALA D CB  1 
ATOM   8274 N  N   . LEU D 1 225 ? 6.110   -1.934  -52.918 1.00 11.63 ? 225 LEU D N   1 
ATOM   8275 C  CA  . LEU D 1 225 ? 6.274   -0.887  -51.911 1.00 12.57 ? 225 LEU D CA  1 
ATOM   8276 C  C   . LEU D 1 225 ? 7.646   -0.200  -52.068 1.00 12.79 ? 225 LEU D C   1 
ATOM   8277 O  O   . LEU D 1 225 ? 7.771   1.036   -51.973 1.00 16.42 ? 225 LEU D O   1 
ATOM   8278 C  CB  . LEU D 1 225 ? 6.011   -1.466  -50.542 1.00 12.11 ? 225 LEU D CB  1 
ATOM   8279 C  CG  . LEU D 1 225 ? 6.216   -0.491  -49.361 1.00 14.37 ? 225 LEU D CG  1 
ATOM   8280 C  CD1 . LEU D 1 225 ? 5.251   0.703   -49.404 1.00 14.84 ? 225 LEU D CD1 1 
ATOM   8281 C  CD2 . LEU D 1 225 ? 6.090   -1.193  -48.006 1.00 12.64 ? 225 LEU D CD2 1 
ATOM   8282 N  N   . GLU D 1 226 ? 8.670   -0.997  -52.341 1.00 12.11 ? 226 GLU D N   1 
ATOM   8283 C  CA  . GLU D 1 226 ? 10.062  -0.554  -52.392 1.00 11.69 ? 226 GLU D CA  1 
ATOM   8284 C  C   . GLU D 1 226 ? 10.371  0.179   -53.678 1.00 13.66 ? 226 GLU D C   1 
ATOM   8285 O  O   . GLU D 1 226 ? 11.393  0.814   -53.739 1.00 14.07 ? 226 GLU D O   1 
ATOM   8286 C  CB  . GLU D 1 226 ? 10.992  -1.804  -52.257 1.00 10.88 ? 226 GLU D CB  1 
ATOM   8287 C  CG  . GLU D 1 226 ? 11.054  -2.406  -50.851 1.00 11.26 ? 226 GLU D CG  1 
ATOM   8288 C  CD  . GLU D 1 226 ? 11.465  -3.849  -50.891 1.00 12.68 ? 226 GLU D CD  1 
ATOM   8289 O  OE1 . GLU D 1 226 ? 11.648  -4.445  -51.982 1.00 13.67 ? 226 GLU D OE1 1 
ATOM   8290 O  OE2 . GLU D 1 226 ? 11.611  -4.471  -49.844 1.00 14.37 ? 226 GLU D OE2 1 
ATOM   8291 N  N   . THR D 1 227 ? 9.559   0.038   -54.714 1.00 12.95 ? 227 THR D N   1 
ATOM   8292 C  CA  . THR D 1 227 ? 9.935   0.563   -56.022 1.00 14.32 ? 227 THR D CA  1 
ATOM   8293 C  C   . THR D 1 227 ? 8.876   1.560   -56.568 1.00 14.33 ? 227 THR D C   1 
ATOM   8294 O  O   . THR D 1 227 ? 9.207   2.264   -57.543 1.00 16.61 ? 227 THR D O   1 
ATOM   8295 C  CB  . THR D 1 227 ? 10.170  -0.585  -57.080 1.00 15.52 ? 227 THR D CB  1 
ATOM   8296 O  OG1 . THR D 1 227 ? 8.930   -1.265  -57.227 1.00 14.84 ? 227 THR D OG1 1 
ATOM   8297 C  CG2 . THR D 1 227 ? 11.337  -1.528  -56.707 1.00 17.17 ? 227 THR D CG2 1 
ATOM   8298 N  N   . ALA D 1 228 ? 7.712   1.728   -55.930 1.00 13.48 ? 228 ALA D N   1 
ATOM   8299 C  CA  . ALA D 1 228 ? 6.606   2.564   -56.468 1.00 14.43 ? 228 ALA D CA  1 
ATOM   8300 C  C   . ALA D 1 228 ? 6.873   4.033   -56.310 1.00 14.69 ? 228 ALA D C   1 
ATOM   8301 O  O   . ALA D 1 228 ? 6.391   4.815   -57.109 1.00 16.95 ? 228 ALA D O   1 
ATOM   8302 C  CB  . ALA D 1 228 ? 5.307   2.195   -55.816 1.00 15.41 ? 228 ALA D CB  1 
ATOM   8303 N  N   . LEU D 1 229 ? 7.592   4.415   -55.255 1.00 12.78 ? 229 LEU D N   1 
ATOM   8304 C  CA  . LEU D 1 229 ? 7.509   5.784   -54.776 1.00 12.89 ? 229 LEU D CA  1 
ATOM   8305 C  C   . LEU D 1 229 ? 8.806   6.549   -54.867 1.00 11.78 ? 229 LEU D C   1 
ATOM   8306 O  O   . LEU D 1 229 ? 9.906   5.999   -54.724 1.00 12.57 ? 229 LEU D O   1 
ATOM   8307 C  CB  . LEU D 1 229 ? 7.013   5.848   -53.293 1.00 13.02 ? 229 LEU D CB  1 
ATOM   8308 C  CG  . LEU D 1 229 ? 5.788   4.954   -53.009 1.00 14.44 ? 229 LEU D CG  1 
ATOM   8309 C  CD1 . LEU D 1 229 ? 5.481   4.944   -51.496 1.00 15.67 ? 229 LEU D CD1 1 
ATOM   8310 C  CD2 . LEU D 1 229 ? 4.559   5.321   -53.856 1.00 15.57 ? 229 LEU D CD2 1 
ATOM   8311 N  N   . TYR D 1 230 ? 8.622   7.846   -55.089 1.00 11.96 ? 230 TYR D N   1 
ATOM   8312 C  CA  . TYR D 1 230 ? 9.722   8.839   -54.998 1.00 13.83 ? 230 TYR D CA  1 
ATOM   8313 C  C   . TYR D 1 230 ? 9.514   9.814   -53.878 1.00 13.26 ? 230 TYR D C   1 
ATOM   8314 O  O   . TYR D 1 230 ? 8.397   10.172  -53.531 1.00 12.97 ? 230 TYR D O   1 
ATOM   8315 C  CB  . TYR D 1 230 ? 9.793   9.656   -56.307 1.00 13.73 ? 230 TYR D CB  1 
ATOM   8316 C  CG  . TYR D 1 230 ? 10.332  8.826   -57.432 1.00 17.66 ? 230 TYR D CG  1 
ATOM   8317 C  CD1 . TYR D 1 230 ? 11.690  8.824   -57.712 1.00 20.97 ? 230 TYR D CD1 1 
ATOM   8318 C  CD2 . TYR D 1 230 ? 9.506   7.916   -58.150 1.00 21.94 ? 230 TYR D CD2 1 
ATOM   8319 C  CE1 . TYR D 1 230 ? 12.213  7.981   -58.698 1.00 25.24 ? 230 TYR D CE1 1 
ATOM   8320 C  CE2 . TYR D 1 230 ? 10.048  7.084   -59.133 1.00 24.20 ? 230 TYR D CE2 1 
ATOM   8321 C  CZ  . TYR D 1 230 ? 11.379  7.143   -59.404 1.00 25.94 ? 230 TYR D CZ  1 
ATOM   8322 O  OH  . TYR D 1 230 ? 11.897  6.310   -60.394 1.00 31.81 ? 230 TYR D OH  1 
ATOM   8323 N  N   . CYS D 1 231 ? 10.621  10.286  -53.317 1.00 14.38 ? 231 CYS D N   1 
ATOM   8324 C  CA  . CYS D 1 231 ? 10.567  11.267  -52.253 1.00 12.30 ? 231 CYS D CA  1 
ATOM   8325 C  C   . CYS D 1 231 ? 10.330  12.678  -52.834 1.00 12.02 ? 231 CYS D C   1 
ATOM   8326 O  O   . CYS D 1 231 ? 10.006  13.585  -52.102 1.00 14.05 ? 231 CYS D O   1 
ATOM   8327 C  CB  . CYS D 1 231 ? 11.941  11.334  -51.602 1.00 12.63 ? 231 CYS D CB  1 
ATOM   8328 S  SG  . CYS D 1 231 ? 12.478  9.910   -50.647 1.00 15.28 ? 231 CYS D SG  1 
ATOM   8329 N  N   . THR D 1 232 ? 10.628  12.799  -54.132 1.00 14.01 ? 232 THR D N   1 
ATOM   8330 C  CA  . THR D 1 232 ? 10.615  14.114  -54.777 1.00 13.43 ? 232 THR D CA  1 
ATOM   8331 C  C   . THR D 1 232 ? 9.313   14.373  -55.542 1.00 15.59 ? 232 THR D C   1 
ATOM   8332 O  O   . THR D 1 232 ? 8.567   13.494  -55.922 1.00 16.17 ? 232 THR D O   1 
ATOM   8333 C  CB  . THR D 1 232 ? 11.828  14.166  -55.766 1.00 13.13 ? 232 THR D CB  1 
ATOM   8334 O  OG1 . THR D 1 232 ? 12.003  12.860  -56.337 1.00 15.54 ? 232 THR D OG1 1 
ATOM   8335 C  CG2 . THR D 1 232 ? 13.080  14.458  -55.005 1.00 14.59 ? 232 THR D CG2 1 
ATOM   8336 N  N   . HIS D 1 233 ? 9.059   15.664  -55.781 1.00 15.16 ? 233 HIS D N   1 
ATOM   8337 C  CA  . HIS D 1 233 ? 7.959   16.122  -56.633 1.00 17.25 ? 233 HIS D CA  1 
ATOM   8338 C  C   . HIS D 1 233 ? 8.252   15.704  -58.039 1.00 17.68 ? 233 HIS D C   1 
ATOM   8339 O  O   . HIS D 1 233 ? 9.418   15.525  -58.464 1.00 19.07 ? 233 HIS D O   1 
ATOM   8340 C  CB  . HIS D 1 233 ? 7.863   17.666  -56.605 1.00 19.97 ? 233 HIS D CB  1 
ATOM   8341 C  CG  . HIS D 1 233 ? 7.398   18.219  -55.315 1.00 21.72 ? 233 HIS D CG  1 
ATOM   8342 N  ND1 . HIS D 1 233 ? 8.186   18.981  -54.528 1.00 28.13 ? 233 HIS D ND1 1 
ATOM   8343 C  CD2 . HIS D 1 233 ? 6.179   18.096  -54.655 1.00 25.06 ? 233 HIS D CD2 1 
ATOM   8344 C  CE1 . HIS D 1 233 ? 7.492   19.335  -53.416 1.00 30.96 ? 233 HIS D CE1 1 
ATOM   8345 N  NE2 . HIS D 1 233 ? 6.277   18.787  -53.493 1.00 27.64 ? 233 HIS D NE2 1 
ATOM   8346 N  N   . MET D 1 234 ? 7.193   15.500  -58.786 1.00 21.02 ? 234 MET D N   1 
ATOM   8347 C  CA  . MET D 1 234 ? 7.284   14.990  -60.121 1.00 23.18 ? 234 MET D CA  1 
ATOM   8348 C  C   . MET D 1 234 ? 8.178   15.899  -60.982 1.00 27.40 ? 234 MET D C   1 
ATOM   8349 O  O   . MET D 1 234 ? 8.787   15.427  -61.942 1.00 31.51 ? 234 MET D O   1 
ATOM   8350 C  CB  . MET D 1 234 ? 5.866   14.973  -60.632 1.00 30.17 ? 234 MET D CB  1 
ATOM   8351 C  CG  . MET D 1 234 ? 5.652   14.221  -61.916 1.00 33.21 ? 234 MET D CG  1 
ATOM   8352 S  SD  . MET D 1 234 ? 3.892   14.436  -62.246 1.00 42.04 ? 234 MET D SD  1 
ATOM   8353 C  CE  . MET D 1 234 ? 4.015   14.859  -63.969 1.00 38.83 ? 234 MET D CE  1 
ATOM   8354 N  N   . ASP D 1 235 ? 8.342   17.183  -60.594 1.00 26.52 ? 235 ASP D N   1 
ATOM   8355 C  CA  . ASP D 1 235 ? 9.149   18.073  -61.423 1.00 28.90 ? 235 ASP D CA  1 
ATOM   8356 C  C   . ASP D 1 235 ? 10.565  18.310  -60.882 1.00 29.89 ? 235 ASP D C   1 
ATOM   8357 O  O   . ASP D 1 235 ? 11.281  19.172  -61.377 1.00 26.24 ? 235 ASP D O   1 
ATOM   8358 C  CB  . ASP D 1 235 ? 8.396   19.402  -61.689 1.00 36.13 ? 235 ASP D CB  1 
ATOM   8359 C  CG  . ASP D 1 235 ? 8.146   20.199  -60.433 1.00 38.66 ? 235 ASP D CG  1 
ATOM   8360 O  OD1 . ASP D 1 235 ? 8.489   19.695  -59.341 1.00 40.26 ? 235 ASP D OD1 1 
ATOM   8361 O  OD2 . ASP D 1 235 ? 7.612   21.339  -60.531 1.00 34.57 ? 235 ASP D OD2 1 
ATOM   8362 N  N   . ASP D 1 236 ? 11.005  17.527  -59.902 1.00 22.67 ? 236 ASP D N   1 
ATOM   8363 C  CA  . ASP D 1 236 ? 12.305  17.731  -59.396 1.00 25.14 ? 236 ASP D CA  1 
ATOM   8364 C  C   . ASP D 1 236 ? 13.251  17.235  -60.454 1.00 25.08 ? 236 ASP D C   1 
ATOM   8365 O  O   . ASP D 1 236 ? 13.084  16.119  -60.949 1.00 24.92 ? 236 ASP D O   1 
ATOM   8366 C  CB  . ASP D 1 236 ? 12.501  16.955  -58.083 1.00 24.00 ? 236 ASP D CB  1 
ATOM   8367 C  CG  . ASP D 1 236 ? 13.617  17.517  -57.235 1.00 25.63 ? 236 ASP D CG  1 
ATOM   8368 O  OD1 . ASP D 1 236 ? 14.762  17.670  -57.750 1.00 25.27 ? 236 ASP D OD1 1 
ATOM   8369 O  OD2 . ASP D 1 236 ? 13.373  17.798  -56.029 1.00 25.22 ? 236 ASP D OD2 1 
ATOM   8370 N  N   . PRO D 1 237 ? 14.202  18.101  -60.843 1.00 27.16 ? 237 PRO D N   1 
ATOM   8371 C  CA  . PRO D 1 237 ? 15.231  17.649  -61.768 1.00 29.31 ? 237 PRO D CA  1 
ATOM   8372 C  C   . PRO D 1 237 ? 16.167  16.651  -61.120 1.00 28.52 ? 237 PRO D C   1 
ATOM   8373 O  O   . PRO D 1 237 ? 16.945  16.026  -61.818 1.00 27.32 ? 237 PRO D O   1 
ATOM   8374 C  CB  . PRO D 1 237 ? 15.993  18.942  -62.080 1.00 28.47 ? 237 PRO D CB  1 
ATOM   8375 C  CG  . PRO D 1 237 ? 15.895  19.759  -60.813 1.00 28.80 ? 237 PRO D CG  1 
ATOM   8376 C  CD  . PRO D 1 237 ? 14.460  19.483  -60.355 1.00 27.53 ? 237 PRO D CD  1 
ATOM   8377 N  N   . SER D 1 238 ? 16.089  16.464  -59.784 1.00 26.20 ? 238 SER D N   1 
ATOM   8378 C  CA  . SER D 1 238 ? 16.983  15.536  -59.135 1.00 25.05 ? 238 SER D CA  1 
ATOM   8379 C  C   . SER D 1 238 ? 16.145  14.459  -58.378 1.00 21.35 ? 238 SER D C   1 
ATOM   8380 O  O   . SER D 1 238 ? 15.996  14.537  -57.177 1.00 19.44 ? 238 SER D O   1 
ATOM   8381 C  CB  . SER D 1 238 ? 17.927  16.330  -58.213 1.00 31.40 ? 238 SER D CB  1 
ATOM   8382 O  OG  . SER D 1 238 ? 18.799  15.458  -57.518 1.00 38.34 ? 238 SER D OG  1 
ATOM   8383 N  N   . PRO D 1 239 ? 15.532  13.525  -59.114 1.00 19.72 ? 239 PRO D N   1 
ATOM   8384 C  CA  . PRO D 1 239 ? 14.663  12.557  -58.378 1.00 18.98 ? 239 PRO D CA  1 
ATOM   8385 C  C   . PRO D 1 239 ? 15.348  11.653  -57.426 1.00 17.71 ? 239 PRO D C   1 
ATOM   8386 O  O   . PRO D 1 239 ? 16.484  11.184  -57.670 1.00 19.36 ? 239 PRO D O   1 
ATOM   8387 C  CB  . PRO D 1 239 ? 14.004  11.733  -59.503 1.00 21.09 ? 239 PRO D CB  1 
ATOM   8388 C  CG  . PRO D 1 239 ? 14.840  11.931  -60.699 1.00 22.60 ? 239 PRO D CG  1 
ATOM   8389 C  CD  . PRO D 1 239 ? 15.447  13.314  -60.574 1.00 24.04 ? 239 PRO D CD  1 
ATOM   8390 N  N   . ARG D 1 240 ? 14.648  11.306  -56.350 1.00 17.35 ? 240 ARG D N   1 
ATOM   8391 C  CA  . ARG D 1 240 ? 15.217  10.406  -55.357 1.00 15.22 ? 240 ARG D CA  1 
ATOM   8392 C  C   . ARG D 1 240 ? 14.172  9.344   -54.988 1.00 16.20 ? 240 ARG D C   1 
ATOM   8393 O  O   . ARG D 1 240 ? 13.026  9.717   -54.610 1.00 16.36 ? 240 ARG D O   1 
ATOM   8394 C  CB  . ARG D 1 240 ? 15.589  11.121  -54.038 1.00 18.23 ? 240 ARG D CB  1 
ATOM   8395 C  CG  . ARG D 1 240 ? 16.661  12.230  -54.188 1.00 18.48 ? 240 ARG D CG  1 
ATOM   8396 C  CD  . ARG D 1 240 ? 16.944  12.881  -52.819 1.00 20.87 ? 240 ARG D CD  1 
ATOM   8397 N  NE  . ARG D 1 240 ? 15.922  13.906  -52.551 1.00 21.69 ? 240 ARG D NE  1 
ATOM   8398 C  CZ  . ARG D 1 240 ? 14.938  13.821  -51.637 1.00 20.73 ? 240 ARG D CZ  1 
ATOM   8399 N  NH1 . ARG D 1 240 ? 14.857  12.752  -50.828 1.00 17.64 ? 240 ARG D NH1 1 
ATOM   8400 N  NH2 . ARG D 1 240 ? 14.074  14.822  -51.501 1.00 19.75 ? 240 ARG D NH2 1 
ATOM   8401 N  N   . GLU D 1 241 ? 14.577  8.094   -55.119 1.00 14.76 ? 241 GLU D N   1 
ATOM   8402 C  CA  . GLU D 1 241 ? 13.679  6.969   -54.761 1.00 14.48 ? 241 GLU D CA  1 
ATOM   8403 C  C   . GLU D 1 241 ? 13.388  6.950   -53.297 1.00 14.92 ? 241 GLU D C   1 
ATOM   8404 O  O   . GLU D 1 241 ? 14.260  7.235   -52.461 1.00 14.75 ? 241 GLU D O   1 
ATOM   8405 C  CB  . GLU D 1 241 ? 14.363  5.664   -55.084 1.00 18.18 ? 241 GLU D CB  1 
ATOM   8406 C  CG  . GLU D 1 241 ? 14.571  5.559   -56.590 1.00 21.83 ? 241 GLU D CG  1 
ATOM   8407 C  CD  . GLU D 1 241 ? 15.343  4.341   -57.000 1.00 28.62 ? 241 GLU D CD  1 
ATOM   8408 O  OE1 . GLU D 1 241 ? 16.238  3.815   -56.263 1.00 34.63 ? 241 GLU D OE1 1 
ATOM   8409 O  OE2 . GLU D 1 241 ? 15.073  3.909   -58.134 1.00 35.90 ? 241 GLU D OE2 1 
ATOM   8410 N  N   . MET D 1 242 ? 12.134  6.552   -52.956 1.00 11.21 ? 242 MET D N   1 
ATOM   8411 C  CA  . MET D 1 242 ? 11.790  6.422   -51.533 1.00 10.62 ? 242 MET D CA  1 
ATOM   8412 C  C   . MET D 1 242 ? 12.095  4.988   -51.100 1.00 10.09 ? 242 MET D C   1 
ATOM   8413 O  O   . MET D 1 242 ? 11.255  4.156   -51.213 1.00 11.14 ? 242 MET D O   1 
ATOM   8414 C  CB  . MET D 1 242 ? 10.302  6.752   -51.370 1.00 9.07  ? 242 MET D CB  1 
ATOM   8415 C  CG  . MET D 1 242 ? 9.949   6.835   -49.852 1.00 10.46 ? 242 MET D CG  1 
ATOM   8416 S  SD  . MET D 1 242 ? 8.181   7.169   -49.637 1.00 10.94 ? 242 MET D SD  1 
ATOM   8417 C  CE  . MET D 1 242 ? 8.097   8.850   -50.239 1.00 9.47  ? 242 MET D CE  1 
ATOM   8418 N  N   . ILE D 1 243 ? 13.306  4.786   -50.569 1.00 10.04 ? 243 ILE D N   1 
ATOM   8419 C  CA  . ILE D 1 243 ? 13.840  3.467   -50.157 1.00 9.80  ? 243 ILE D CA  1 
ATOM   8420 C  C   . ILE D 1 243 ? 14.579  3.723   -48.807 1.00 9.42  ? 243 ILE D C   1 
ATOM   8421 O  O   . ILE D 1 243 ? 15.017  4.856   -48.542 1.00 9.32  ? 243 ILE D O   1 
ATOM   8422 C  CB  . ILE D 1 243 ? 14.785  2.854   -51.192 1.00 10.75 ? 243 ILE D CB  1 
ATOM   8423 C  CG1 . ILE D 1 243 ? 15.936  3.885   -51.509 1.00 10.46 ? 243 ILE D CG1 1 
ATOM   8424 C  CG2 . ILE D 1 243 ? 13.993  2.475   -52.429 1.00 13.10 ? 243 ILE D CG2 1 
ATOM   8425 C  CD1 . ILE D 1 243 ? 17.040  3.282   -52.391 1.00 13.17 ? 243 ILE D CD1 1 
ATOM   8426 N  N   . ASN D 1 244 ? 14.708  2.651   -48.046 1.00 9.14  ? 244 ASN D N   1 
ATOM   8427 C  CA  . ASN D 1 244 ? 15.476  2.682   -46.816 1.00 10.00 ? 244 ASN D CA  1 
ATOM   8428 C  C   . ASN D 1 244 ? 15.065  3.846   -45.898 1.00 9.90  ? 244 ASN D C   1 
ATOM   8429 O  O   . ASN D 1 244 ? 15.896  4.531   -45.304 1.00 10.97 ? 244 ASN D O   1 
ATOM   8430 C  CB  . ASN D 1 244 ? 16.984  2.816   -47.139 1.00 9.65  ? 244 ASN D CB  1 
ATOM   8431 C  CG  . ASN D 1 244 ? 17.427  1.733   -48.022 1.00 13.47 ? 244 ASN D CG  1 
ATOM   8432 O  OD1 . ASN D 1 244 ? 16.968  0.602   -47.947 1.00 11.66 ? 244 ASN D OD1 1 
ATOM   8433 N  ND2 . ASN D 1 244 ? 18.323  2.129   -48.970 1.00 14.65 ? 244 ASN D ND2 1 
ATOM   8434 N  N   . ASN D 1 245 ? 13.748  4.038   -45.755 1.00 9.36  ? 245 ASN D N   1 
ATOM   8435 C  CA  . ASN D 1 245 ? 13.187  5.133   -44.961 1.00 8.18  ? 245 ASN D CA  1 
ATOM   8436 C  C   . ASN D 1 245 ? 12.920  4.637   -43.505 1.00 9.02  ? 245 ASN D C   1 
ATOM   8437 O  O   . ASN D 1 245 ? 11.784  4.657   -43.000 1.00 9.76  ? 245 ASN D O   1 
ATOM   8438 C  CB  . ASN D 1 245 ? 11.907  5.686   -45.636 1.00 8.57  ? 245 ASN D CB  1 
ATOM   8439 C  CG  . ASN D 1 245 ? 10.799  4.667   -45.817 1.00 8.26  ? 245 ASN D CG  1 
ATOM   8440 O  OD1 . ASN D 1 245 ? 11.008  3.484   -45.743 1.00 8.41  ? 245 ASN D OD1 1 
ATOM   8441 N  ND2 . ASN D 1 245 ? 9.595   5.160   -46.054 1.00 9.10  ? 245 ASN D ND2 1 
ATOM   8442 N  N   . PHE D 1 246 ? 13.986  4.090   -42.873 1.00 7.83  ? 246 PHE D N   1 
ATOM   8443 C  CA  . PHE D 1 246 ? 13.941  3.691   -41.456 1.00 7.63  ? 246 PHE D CA  1 
ATOM   8444 C  C   . PHE D 1 246 ? 15.114  4.378   -40.757 1.00 7.95  ? 246 PHE D C   1 
ATOM   8445 O  O   . PHE D 1 246 ? 16.199  4.513   -41.328 1.00 8.75  ? 246 PHE D O   1 
ATOM   8446 C  CB  . PHE D 1 246 ? 13.963  2.111   -41.372 1.00 8.06  ? 246 PHE D CB  1 
ATOM   8447 C  CG  . PHE D 1 246 ? 15.237  1.465   -41.911 1.00 8.24  ? 246 PHE D CG  1 
ATOM   8448 C  CD1 . PHE D 1 246 ? 16.331  1.168   -41.086 1.00 9.89  ? 246 PHE D CD1 1 
ATOM   8449 C  CD2 . PHE D 1 246 ? 15.287  1.191   -43.259 1.00 8.89  ? 246 PHE D CD2 1 
ATOM   8450 C  CE1 . PHE D 1 246 ? 17.488  0.568   -41.620 1.00 9.87  ? 246 PHE D CE1 1 
ATOM   8451 C  CE2 . PHE D 1 246 ? 16.422  0.595   -43.856 1.00 9.59  ? 246 PHE D CE2 1 
ATOM   8452 C  CZ  . PHE D 1 246 ? 17.529  0.293   -43.028 1.00 10.05 ? 246 PHE D CZ  1 
ATOM   8453 N  N   . ARG D 1 247 ? 14.945  4.660   -39.485 1.00 7.72  ? 247 ARG D N   1 
ATOM   8454 C  CA  . ARG D 1 247 ? 16.085  5.128   -38.656 1.00 7.75  ? 247 ARG D CA  1 
ATOM   8455 C  C   . ARG D 1 247 ? 16.795  3.946   -38.040 1.00 8.37  ? 247 ARG D C   1 
ATOM   8456 O  O   . ARG D 1 247 ? 16.151  2.949   -37.712 1.00 8.54  ? 247 ARG D O   1 
ATOM   8457 C  CB  . ARG D 1 247 ? 15.480  6.089   -37.616 1.00 7.82  ? 247 ARG D CB  1 
ATOM   8458 C  CG  . ARG D 1 247 ? 16.524  6.871   -36.832 1.00 8.52  ? 247 ARG D CG  1 
ATOM   8459 C  CD  . ARG D 1 247 ? 15.841  7.545   -35.637 1.00 8.72  ? 247 ARG D CD  1 
ATOM   8460 N  NE  . ARG D 1 247 ? 16.687  8.670   -35.133 1.00 9.32  ? 247 ARG D NE  1 
ATOM   8461 C  CZ  . ARG D 1 247 ? 16.405  9.353   -34.029 1.00 10.51 ? 247 ARG D CZ  1 
ATOM   8462 N  NH1 . ARG D 1 247 ? 15.288  9.060   -33.287 1.00 10.19 ? 247 ARG D NH1 1 
ATOM   8463 N  NH2 . ARG D 1 247 ? 17.213  10.347  -33.671 1.00 10.13 ? 247 ARG D NH2 1 
ATOM   8464 N  N   . GLN D 1 248 ? 18.153  4.066   -37.803 1.00 7.78  ? 248 GLN D N   1 
ATOM   8465 C  CA  . GLN D 1 248 ? 18.885  3.048   -37.055 1.00 8.48  ? 248 GLN D CA  1 
ATOM   8466 C  C   . GLN D 1 248 ? 18.367  2.995   -35.598 1.00 7.58  ? 248 GLN D C   1 
ATOM   8467 O  O   . GLN D 1 248 ? 17.821  3.975   -35.067 1.00 8.54  ? 248 GLN D O   1 
ATOM   8468 C  CB  . GLN D 1 248 ? 20.362  3.457   -37.004 1.00 8.82  ? 248 GLN D CB  1 
ATOM   8469 C  CG  . GLN D 1 248 ? 21.015  3.432   -38.388 1.00 8.76  ? 248 GLN D CG  1 
ATOM   8470 C  CD  . GLN D 1 248 ? 21.039  2.035   -39.024 1.00 9.61  ? 248 GLN D CD  1 
ATOM   8471 O  OE1 . GLN D 1 248 ? 20.120  1.690   -39.779 1.00 11.08 ? 248 GLN D OE1 1 
ATOM   8472 N  NE2 . GLN D 1 248 ? 22.062  1.190   -38.720 1.00 10.52 ? 248 GLN D NE2 1 
ATOM   8473 N  N   . VAL D 1 249 ? 18.535  1.819   -34.986 1.00 8.67  ? 249 VAL D N   1 
ATOM   8474 C  CA  . VAL D 1 249 ? 18.198  1.694   -33.562 1.00 9.32  ? 249 VAL D CA  1 
ATOM   8475 C  C   . VAL D 1 249 ? 19.091  2.605   -32.668 1.00 9.58  ? 249 VAL D C   1 
ATOM   8476 O  O   . VAL D 1 249 ? 20.215  2.952   -33.045 1.00 10.01 ? 249 VAL D O   1 
ATOM   8477 C  CB  . VAL D 1 249 ? 18.239  0.236   -33.054 1.00 10.29 ? 249 VAL D CB  1 
ATOM   8478 C  CG1 . VAL D 1 249 ? 17.179  -0.574  -33.770 1.00 9.97  ? 249 VAL D CG1 1 
ATOM   8479 C  CG2 . VAL D 1 249 ? 19.623  -0.367  -33.208 1.00 10.95 ? 249 VAL D CG2 1 
ATOM   8480 N  N   . GLN D 1 250 ? 18.533  3.008   -31.540 1.00 8.99  ? 250 GLN D N   1 
ATOM   8481 C  CA  . GLN D 1 250 ? 19.108  4.031   -30.627 1.00 8.96  ? 250 GLN D CA  1 
ATOM   8482 C  C   . GLN D 1 250 ? 19.553  3.443   -29.300 1.00 9.86  ? 250 GLN D C   1 
ATOM   8483 O  O   . GLN D 1 250 ? 19.134  2.364   -28.882 1.00 10.20 ? 250 GLN D O   1 
ATOM   8484 C  CB  . GLN D 1 250 ? 17.962  5.045   -30.273 1.00 8.37  ? 250 GLN D CB  1 
ATOM   8485 C  CG  . GLN D 1 250 ? 17.301  5.622   -31.535 1.00 7.96  ? 250 GLN D CG  1 
ATOM   8486 C  CD  . GLN D 1 250 ? 18.233  6.577   -32.263 1.00 9.27  ? 250 GLN D CD  1 
ATOM   8487 O  OE1 . GLN D 1 250 ? 18.694  7.574   -31.653 1.00 10.58 ? 250 GLN D OE1 1 
ATOM   8488 N  NE2 . GLN D 1 250 ? 18.494  6.323   -33.546 1.00 8.82  ? 250 GLN D NE2 1 
ATOM   8489 N  N   . LYS D 1 251 ? 20.444  4.166   -28.649 1.00 11.02 ? 251 LYS D N   1 
ATOM   8490 C  CA  . LYS D 1 251 ? 20.842  3.774   -27.295 1.00 11.10 ? 251 LYS D CA  1 
ATOM   8491 C  C   . LYS D 1 251 ? 19.623  3.712   -26.357 1.00 11.09 ? 251 LYS D C   1 
ATOM   8492 O  O   . LYS D 1 251 ? 18.691  4.515   -26.408 1.00 12.47 ? 251 LYS D O   1 
ATOM   8493 C  CB  . LYS D 1 251 ? 21.764  4.878   -26.753 1.00 11.85 ? 251 LYS D CB  1 
ATOM   8494 C  CG  . LYS D 1 251 ? 23.140  4.922   -27.440 1.00 11.97 ? 251 LYS D CG  1 
ATOM   8495 C  CD  . LYS D 1 251 ? 24.011  3.884   -26.855 1.00 11.85 ? 251 LYS D CD  1 
ATOM   8496 C  CE  . LYS D 1 251 ? 25.491  3.989   -27.231 1.00 12.16 ? 251 LYS D CE  1 
ATOM   8497 N  NZ  . LYS D 1 251 ? 25.645  3.715   -28.722 1.00 10.24 ? 251 LYS D NZ  1 
ATOM   8498 N  N   . PHE D 1 252 ? 19.713  2.754   -25.468 1.00 13.24 ? 252 PHE D N   1 
ATOM   8499 C  CA  . PHE D 1 252 ? 18.621  2.596   -24.455 1.00 15.15 ? 252 PHE D CA  1 
ATOM   8500 C  C   . PHE D 1 252 ? 18.520  3.632   -23.365 1.00 20.82 ? 252 PHE D C   1 
ATOM   8501 O  O   . PHE D 1 252 ? 17.409  3.804   -22.839 1.00 20.55 ? 252 PHE D O   1 
ATOM   8502 C  CB  . PHE D 1 252 ? 18.760  1.234   -23.786 1.00 18.05 ? 252 PHE D CB  1 
ATOM   8503 C  CG  . PHE D 1 252 ? 18.124  0.176   -24.594 1.00 23.43 ? 252 PHE D CG  1 
ATOM   8504 C  CD1 . PHE D 1 252 ? 16.755  -0.067  -24.431 1.00 23.58 ? 252 PHE D CD1 1 
ATOM   8505 C  CD2 . PHE D 1 252 ? 18.831  -0.470  -25.600 1.00 26.21 ? 252 PHE D CD2 1 
ATOM   8506 C  CE1 . PHE D 1 252 ? 16.133  -1.012  -25.235 1.00 28.50 ? 252 PHE D CE1 1 
ATOM   8507 C  CE2 . PHE D 1 252 ? 18.186  -1.430  -26.434 1.00 27.24 ? 252 PHE D CE2 1 
ATOM   8508 C  CZ  . PHE D 1 252 ? 16.845  -1.691  -26.221 1.00 26.82 ? 252 PHE D CZ  1 
ATOM   8509 N  N   . ASP D 1 253 ? 19.623  4.341   -23.007 1.00 19.00 ? 253 ASP D N   1 
ATOM   8510 C  CA  . ASP D 1 253 ? 19.517  5.441   -22.024 1.00 22.84 ? 253 ASP D CA  1 
ATOM   8511 C  C   . ASP D 1 253 ? 18.819  4.904   -20.744 1.00 23.12 ? 253 ASP D C   1 
ATOM   8512 O  O   . ASP D 1 253 ? 17.935  5.610   -20.192 1.00 23.43 ? 253 ASP D O   1 
ATOM   8513 C  CB  . ASP D 1 253 ? 18.655  6.605   -22.561 1.00 24.39 ? 253 ASP D CB  1 
ATOM   8514 C  CG  . ASP D 1 253 ? 19.289  7.327   -23.757 1.00 29.13 ? 253 ASP D CG  1 
ATOM   8515 O  OD1 . ASP D 1 253 ? 20.545  7.285   -23.901 1.00 28.91 ? 253 ASP D OD1 1 
ATOM   8516 O  OD2 . ASP D 1 253 ? 18.500  7.952   -24.518 1.00 30.31 ? 253 ASP D OD2 1 
ATOM   8517 N  N   . GLU D 1 254 ? 19.150  3.667   -20.378 1.00 21.23 ? 254 GLU D N   1 
ATOM   8518 C  CA  . GLU D 1 254 ? 18.724  3.042   -19.096 1.00 24.91 ? 254 GLU D CA  1 
ATOM   8519 C  C   . GLU D 1 254 ? 17.233  2.637   -19.073 1.00 25.32 ? 254 GLU D C   1 
ATOM   8520 O  O   . GLU D 1 254 ? 16.702  2.274   -18.009 1.00 23.19 ? 254 GLU D O   1 
ATOM   8521 C  CB  . GLU D 1 254 ? 18.991  3.983   -17.905 1.00 29.74 ? 254 GLU D CB  1 
ATOM   8522 C  CG  . GLU D 1 254 ? 20.369  4.637   -17.951 1.00 39.68 ? 254 GLU D CG  1 
ATOM   8523 C  CD  . GLU D 1 254 ? 21.082  4.593   -16.624 1.00 51.47 ? 254 GLU D CD  1 
ATOM   8524 O  OE1 . GLU D 1 254 ? 22.237  4.084   -16.600 1.00 55.55 ? 254 GLU D OE1 1 
ATOM   8525 O  OE2 . GLU D 1 254 ? 20.494  5.079   -15.614 1.00 53.41 ? 254 GLU D OE2 1 
ATOM   8526 N  N   . ARG D 1 255 ? 16.559  2.760   -20.211 1.00 20.22 ? 255 ARG D N   1 
ATOM   8527 C  CA  . ARG D 1 255 ? 15.173  2.262   -20.349 1.00 17.62 ? 255 ARG D CA  1 
ATOM   8528 C  C   . ARG D 1 255 ? 15.132  0.743   -20.280 1.00 20.33 ? 255 ARG D C   1 
ATOM   8529 O  O   . ARG D 1 255 ? 16.075  0.072   -20.683 1.00 22.23 ? 255 ARG D O   1 
ATOM   8530 C  CB  . ARG D 1 255 ? 14.531  2.747   -21.683 1.00 17.95 ? 255 ARG D CB  1 
ATOM   8531 C  CG  . ARG D 1 255 ? 14.216  4.215   -21.772 1.00 18.60 ? 255 ARG D CG  1 
ATOM   8532 C  CD  . ARG D 1 255 ? 13.734  4.554   -23.178 1.00 17.49 ? 255 ARG D CD  1 
ATOM   8533 N  NE  . ARG D 1 255 ? 14.843  4.559   -24.118 1.00 18.37 ? 255 ARG D NE  1 
ATOM   8534 C  CZ  . ARG D 1 255 ? 14.723  4.865   -25.398 1.00 16.96 ? 255 ARG D CZ  1 
ATOM   8535 N  NH1 . ARG D 1 255 ? 13.497  5.169   -25.873 1.00 13.77 ? 255 ARG D NH1 1 
ATOM   8536 N  NH2 . ARG D 1 255 ? 15.859  4.935   -26.166 1.00 13.90 ? 255 ARG D NH2 1 
ATOM   8537 N  N   . LEU D 1 256 ? 14.039  0.197   -19.740 1.00 18.06 ? 256 LEU D N   1 
ATOM   8538 C  CA  . LEU D 1 256 ? 13.686  -1.175  -19.989 1.00 14.92 ? 256 LEU D CA  1 
ATOM   8539 C  C   . LEU D 1 256 ? 12.456  -1.165  -20.976 1.00 13.92 ? 256 LEU D C   1 
ATOM   8540 O  O   . LEU D 1 256 ? 11.817  -0.130  -21.160 1.00 15.43 ? 256 LEU D O   1 
ATOM   8541 C  CB  . LEU D 1 256 ? 13.260  -1.864  -18.710 1.00 17.38 ? 256 LEU D CB  1 
ATOM   8542 C  CG  . LEU D 1 256 ? 14.291  -1.961  -17.590 1.00 18.24 ? 256 LEU D CG  1 
ATOM   8543 C  CD1 . LEU D 1 256 ? 13.629  -2.610  -16.374 1.00 20.48 ? 256 LEU D CD1 1 
ATOM   8544 C  CD2 . LEU D 1 256 ? 15.507  -2.748  -18.102 1.00 22.13 ? 256 LEU D CD2 1 
ATOM   8545 N  N   . VAL D 1 257 ? 12.224  -2.291  -21.618 1.00 14.12 ? 257 VAL D N   1 
ATOM   8546 C  CA  . VAL D 1 257 ? 11.034  -2.494  -22.427 1.00 13.49 ? 257 VAL D CA  1 
ATOM   8547 C  C   . VAL D 1 257 ? 10.201  -3.482  -21.673 1.00 13.22 ? 257 VAL D C   1 
ATOM   8548 O  O   . VAL D 1 257 ? 10.646  -4.549  -21.265 1.00 12.62 ? 257 VAL D O   1 
ATOM   8549 C  CB  . VAL D 1 257 ? 11.404  -3.039  -23.832 1.00 13.95 ? 257 VAL D CB  1 
ATOM   8550 C  CG1 . VAL D 1 257 ? 10.138  -3.406  -24.566 1.00 13.71 ? 257 VAL D CG1 1 
ATOM   8551 C  CG2 . VAL D 1 257 ? 12.178  -1.979  -24.629 1.00 13.84 ? 257 VAL D CG2 1 
ATOM   8552 N  N   . TYR D 1 258 ? 8.956   -3.100  -21.443 1.00 11.86 ? 258 TYR D N   1 
ATOM   8553 C  CA  . TYR D 1 258 ? 8.071   -3.968  -20.596 1.00 12.98 ? 258 TYR D CA  1 
ATOM   8554 C  C   . TYR D 1 258 ? 7.253   -4.834  -21.483 1.00 13.33 ? 258 TYR D C   1 
ATOM   8555 O  O   . TYR D 1 258 ? 6.865   -4.454  -22.609 1.00 14.49 ? 258 TYR D O   1 
ATOM   8556 C  CB  . TYR D 1 258 ? 7.193   -3.106  -19.700 1.00 14.41 ? 258 TYR D CB  1 
ATOM   8557 C  CG  . TYR D 1 258 ? 8.063   -2.263  -18.806 1.00 16.31 ? 258 TYR D CG  1 
ATOM   8558 C  CD1 . TYR D 1 258 ? 8.551   -2.804  -17.611 1.00 16.67 ? 258 TYR D CD1 1 
ATOM   8559 C  CD2 . TYR D 1 258 ? 8.529   -0.989  -19.236 1.00 16.56 ? 258 TYR D CD2 1 
ATOM   8560 C  CE1 . TYR D 1 258 ? 9.412   -2.041  -16.827 1.00 20.13 ? 258 TYR D CE1 1 
ATOM   8561 C  CE2 . TYR D 1 258 ? 9.340   -0.237  -18.442 1.00 18.31 ? 258 TYR D CE2 1 
ATOM   8562 C  CZ  . TYR D 1 258 ? 9.768   -0.770  -17.238 1.00 17.43 ? 258 TYR D CZ  1 
ATOM   8563 O  OH  . TYR D 1 258 ? 10.620  0.000   -16.440 1.00 21.44 ? 258 TYR D OH  1 
ATOM   8564 N  N   . THR D 1 259 ? 6.959   -6.021  -21.039 1.00 10.93 ? 259 THR D N   1 
ATOM   8565 C  CA  . THR D 1 259 ? 6.285   -6.972  -21.950 1.00 10.74 ? 259 THR D CA  1 
ATOM   8566 C  C   . THR D 1 259 ? 5.012   -7.507  -21.267 1.00 11.65 ? 259 THR D C   1 
ATOM   8567 O  O   . THR D 1 259 ? 4.961   -7.624  -20.037 1.00 12.51 ? 259 THR D O   1 
ATOM   8568 C  CB  . THR D 1 259 ? 7.099   -8.216  -22.368 1.00 12.10 ? 259 THR D CB  1 
ATOM   8569 O  OG1 . THR D 1 259 ? 7.590   -8.906  -21.183 1.00 15.12 ? 259 THR D OG1 1 
ATOM   8570 C  CG2 . THR D 1 259 ? 8.385   -7.716  -23.153 1.00 11.75 ? 259 THR D CG2 1 
ATOM   8571 N  N   . SER D 1 260 ? 4.051   -7.851  -22.076 1.00 12.35 ? 260 SER D N   1 
ATOM   8572 C  CA  . SER D 1 260 ? 2.794   -8.423  -21.542 1.00 12.85 ? 260 SER D CA  1 
ATOM   8573 C  C   . SER D 1 260 ? 2.801   -9.953  -21.541 1.00 16.05 ? 260 SER D C   1 
ATOM   8574 O  O   . SER D 1 260 ? 1.730   -10.599 -21.302 1.00 17.38 ? 260 SER D O   1 
ATOM   8575 C  CB  . SER D 1 260 ? 1.633   -7.951  -22.389 1.00 12.64 ? 260 SER D CB  1 
ATOM   8576 O  OG  . SER D 1 260 ? 1.705   -8.516  -23.720 1.00 13.42 ? 260 SER D OG  1 
ATOM   8577 N  N   . PHE D 1 261 ? 3.944   -10.545 -21.830 1.00 16.47 ? 261 PHE D N   1 
ATOM   8578 C  CA  . PHE D 1 261 ? 4.077   -12.001 -21.972 1.00 17.94 ? 261 PHE D CA  1 
ATOM   8579 C  C   . PHE D 1 261 ? 5.397   -12.362 -21.265 1.00 18.99 ? 261 PHE D C   1 
ATOM   8580 O  O   . PHE D 1 261 ? 6.285   -11.536 -21.131 1.00 18.68 ? 261 PHE D O   1 
ATOM   8581 C  CB  . PHE D 1 261 ? 4.115   -12.431 -23.451 1.00 18.50 ? 261 PHE D CB  1 
ATOM   8582 C  CG  . PHE D 1 261 ? 5.149   -11.689 -24.263 1.00 16.57 ? 261 PHE D CG  1 
ATOM   8583 C  CD1 . PHE D 1 261 ? 6.435   -12.249 -24.454 1.00 19.30 ? 261 PHE D CD1 1 
ATOM   8584 C  CD2 . PHE D 1 261 ? 4.864   -10.458 -24.863 1.00 17.57 ? 261 PHE D CD2 1 
ATOM   8585 C  CE1 . PHE D 1 261 ? 7.421   -11.597 -25.231 1.00 17.63 ? 261 PHE D CE1 1 
ATOM   8586 C  CE2 . PHE D 1 261 ? 5.865   -9.828  -25.654 1.00 17.10 ? 261 PHE D CE2 1 
ATOM   8587 C  CZ  . PHE D 1 261 ? 7.121   -10.358 -25.803 1.00 16.44 ? 261 PHE D CZ  1 
ATOM   8588 N  N   . SER D 1 262 ? 5.516   -13.595 -20.765 1.00 27.17 ? 262 SER D N   1 
ATOM   8589 C  CA  . SER D 1 262 ? 6.852   -14.157 -20.433 1.00 32.19 ? 262 SER D CA  1 
ATOM   8590 C  C   . SER D 1 262 ? 7.470   -15.133 -21.474 1.00 35.44 ? 262 SER D C   1 
ATOM   8591 O  O   . SER D 1 262 ? 6.835   -15.770 -22.327 1.00 37.04 ? 262 SER D O   1 
ATOM   8592 C  CB  . SER D 1 262 ? 6.875   -14.760 -19.025 1.00 38.21 ? 262 SER D CB  1 
ATOM   8593 O  OG  . SER D 1 262 ? 6.652   -13.737 -18.054 1.00 36.01 ? 262 SER D OG  1 
HETATM 8594 ZN ZN  . ZN  E 2 .   ? 23.001  0.713   12.311  1.00 9.38  ? 301 ZN  A ZN  1 
HETATM 8595 C  C1  . EDO F 3 .   ? 26.267  -8.921  29.817  1.00 32.84 ? 302 EDO A C1  1 
HETATM 8596 O  O1  . EDO F 3 .   ? 25.883  -10.051 29.052  1.00 34.38 ? 302 EDO A O1  1 
HETATM 8597 C  C2  . EDO F 3 .   ? 27.179  -9.289  31.022  1.00 33.01 ? 302 EDO A C2  1 
HETATM 8598 O  O2  . EDO F 3 .   ? 28.529  -9.634  30.639  1.00 30.98 ? 302 EDO A O2  1 
HETATM 8599 O  O16 . WWX G 4 .   ? 29.072  7.181   12.203  1.00 25.07 ? 303 WWX A O16 1 
HETATM 8600 S  S14 . WWX G 4 .   ? 28.721  6.699   10.770  1.00 24.50 ? 303 WWX A S14 1 
HETATM 8601 O  O15 . WWX G 4 .   ? 29.992  5.878   10.377  1.00 23.64 ? 303 WWX A O15 1 
HETATM 8602 C  C18 . WWX G 4 .   ? 30.110  8.719   9.544   1.00 31.95 ? 303 WWX A C18 1 
HETATM 8603 O  O20 . WWX G 4 .   ? 29.985  9.790   10.456  1.00 38.16 ? 303 WWX A O20 1 
HETATM 8604 C  C17 . WWX G 4 .   ? 28.735  8.041   9.556   1.00 27.35 ? 303 WWX A C17 1 
HETATM 8605 C  C8  . WWX G 4 .   ? 27.250  5.652   10.685  1.00 22.29 ? 303 WWX A C8  1 
HETATM 8606 C  C7  . WWX G 4 .   ? 27.156  4.930   9.502   1.00 25.87 ? 303 WWX A C7  1 
HETATM 8607 F  F12 . WWX G 4 .   ? 28.085  5.078   8.500   1.00 24.32 ? 303 WWX A F12 1 
HETATM 8608 C  C6  . WWX G 4 .   ? 26.088  4.033   9.336   1.00 23.14 ? 303 WWX A C6  1 
HETATM 8609 F  F11 . WWX G 4 .   ? 26.004  3.346   8.179   1.00 22.73 ? 303 WWX A F11 1 
HETATM 8610 C  C9  . WWX G 4 .   ? 26.255  5.548   11.685  1.00 22.68 ? 303 WWX A C9  1 
HETATM 8611 C  C10 . WWX G 4 .   ? 25.182  4.671   11.467  1.00 17.99 ? 303 WWX A C10 1 
HETATM 8612 F  F13 . WWX G 4 .   ? 24.197  4.443   12.300  1.00 18.48 ? 303 WWX A F13 1 
HETATM 8613 C  C5  . WWX G 4 .   ? 25.121  3.926   10.295  1.00 19.73 ? 303 WWX A C5  1 
HETATM 8614 S  S1  . WWX G 4 .   ? 23.851  2.696   10.109  1.00 16.06 ? 303 WWX A S1  1 
HETATM 8615 O  O3  . WWX G 4 .   ? 23.121  2.931   8.789   1.00 15.63 ? 303 WWX A O3  1 
HETATM 8616 N  N4  . WWX G 4 .   ? 22.713  2.378   11.217  1.00 12.88 ? 303 WWX A N4  1 
HETATM 8617 O  O2  . WWX G 4 .   ? 24.706  1.438   9.924   1.00 16.06 ? 303 WWX A O2  1 
HETATM 8618 N  N19 . WWX G 4 .   ? 26.366  6.325   12.859  1.00 18.70 ? 303 WWX A N19 1 
HETATM 8619 C  C21 . WWX G 4 .   ? 25.333  7.377   13.078  1.00 20.86 ? 303 WWX A C21 1 
HETATM 8620 C  C30 . WWX G 4 .   ? 25.745  8.582   12.256  1.00 22.21 ? 303 WWX A C30 1 
HETATM 8621 C  C35 . WWX G 4 .   ? 25.274  8.672   10.935  1.00 22.93 ? 303 WWX A C35 1 
HETATM 8622 C  C34 . WWX G 4 .   ? 25.700  9.775   10.113  1.00 26.10 ? 303 WWX A C34 1 
HETATM 8623 C  C33 . WWX G 4 .   ? 26.555  10.777  10.615  1.00 27.68 ? 303 WWX A C33 1 
HETATM 8624 C  C32 . WWX G 4 .   ? 26.973  10.674  11.954  1.00 29.57 ? 303 WWX A C32 1 
HETATM 8625 C  C31 . WWX G 4 .   ? 26.582  9.586   12.763  1.00 24.54 ? 303 WWX A C31 1 
HETATM 8626 C  C22 . WWX G 4 .   ? 25.134  7.731   14.577  1.00 21.51 ? 303 WWX A C22 1 
HETATM 8627 O  O29 . WWX G 4 .   ? 24.130  8.664   14.652  1.00 19.69 ? 303 WWX A O29 1 
HETATM 8628 C  C23 . WWX G 4 .   ? 24.741  6.434   15.185  1.00 21.42 ? 303 WWX A C23 1 
HETATM 8629 C  C28 . WWX G 4 .   ? 23.385  6.019   15.103  1.00 23.96 ? 303 WWX A C28 1 
HETATM 8630 C  C27 . WWX G 4 .   ? 22.996  4.744   15.541  1.00 18.80 ? 303 WWX A C27 1 
HETATM 8631 C  C26 . WWX G 4 .   ? 23.998  3.948   16.064  1.00 20.40 ? 303 WWX A C26 1 
HETATM 8632 C  C25 . WWX G 4 .   ? 25.354  4.431   16.188  1.00 23.43 ? 303 WWX A C25 1 
HETATM 8633 C  C24 . WWX G 4 .   ? 25.784  5.674   15.695  1.00 18.60 ? 303 WWX A C24 1 
HETATM 8634 ZN ZN  . ZN  H 2 .   ? -8.142  3.797   4.957   1.00 8.49  ? 301 ZN  B ZN  1 
HETATM 8635 C  C1  . EDO I 3 .   ? -17.665 -3.697  21.510  1.00 26.36 ? 302 EDO B C1  1 
HETATM 8636 O  O1  . EDO I 3 .   ? -16.628 -3.579  20.503  1.00 25.57 ? 302 EDO B O1  1 
HETATM 8637 C  C2  . EDO I 3 .   ? -17.507 -2.678  22.694  1.00 33.88 ? 302 EDO B C2  1 
HETATM 8638 O  O2  . EDO I 3 .   ? -16.630 -3.222  23.693  1.00 35.99 ? 302 EDO B O2  1 
HETATM 8639 O  O16 . WWX J 4 .   ? -10.414 8.630   1.292   1.00 43.03 ? 303 WWX B O16 1 
HETATM 8640 S  S14 . WWX J 4 .   ? -9.689  9.817   2.001   1.00 44.95 ? 303 WWX B S14 1 
HETATM 8641 O  O15 . WWX J 4 .   ? -10.904 10.774  2.182   1.00 47.37 ? 303 WWX B O15 1 
HETATM 8642 C  C18 . WWX J 4 .   ? -7.290  10.930  1.830   1.00 35.67 ? 303 WWX B C18 1 
HETATM 8643 O  O20 . WWX J 4 .   ? -7.941  11.883  2.567   1.00 26.80 ? 303 WWX B O20 1 
HETATM 8644 C  C17 . WWX J 4 .   ? -8.342  10.352  0.919   1.00 38.92 ? 303 WWX B C17 1 
HETATM 8645 C  C8  . WWX J 4 .   ? -9.376  8.937   3.504   1.00 35.58 ? 303 WWX B C8  1 
HETATM 8646 C  C7  . WWX J 4 .   ? -8.438  7.949   3.266   1.00 31.75 ? 303 WWX B C7  1 
HETATM 8647 F  F12 . WWX J 4 .   ? -7.817  7.749   2.004   1.00 34.44 ? 303 WWX B F12 1 
HETATM 8648 C  C6  . WWX J 4 .   ? -8.110  7.207   4.403   1.00 25.10 ? 303 WWX B C6  1 
HETATM 8649 F  F11 . WWX J 4 .   ? -7.189  6.237   4.040   1.00 28.81 ? 303 WWX B F11 1 
HETATM 8650 C  C9  . WWX J 4 .   ? -9.999  9.128   4.764   1.00 31.34 ? 303 WWX B C9  1 
HETATM 8651 C  C10 . WWX J 4 .   ? -9.651  8.291   5.882   1.00 26.44 ? 303 WWX B C10 1 
HETATM 8652 F  F13 . WWX J 4 .   ? -10.138 8.286   7.159   1.00 31.39 ? 303 WWX B F13 1 
HETATM 8653 C  C5  . WWX J 4 .   ? -8.701  7.302   5.699   1.00 22.27 ? 303 WWX B C5  1 
HETATM 8654 S  S1  . WWX J 4 .   ? -8.323  6.040   7.075   1.00 16.95 ? 303 WWX B S1  1 
HETATM 8655 O  O3  . WWX J 4 .   ? -7.577  6.311   8.335   1.00 17.49 ? 303 WWX B O3  1 
HETATM 8656 N  N4  . WWX J 4 .   ? -7.461  4.986   6.019   1.00 17.30 ? 303 WWX B N4  1 
HETATM 8657 O  O2  . WWX J 4 .   ? -9.450  5.197   7.393   1.00 14.56 ? 303 WWX B O2  1 
HETATM 8658 N  N19 . WWX J 4 .   ? -10.902 10.163  4.790   1.00 30.19 ? 303 WWX B N19 1 
HETATM 8659 C  C21 . WWX J 4 .   ? -10.901 11.006  5.993   1.00 33.27 ? 303 WWX B C21 1 
HETATM 8660 C  C30 . WWX J 4 .   ? -12.176 10.904  6.806   1.00 22.38 ? 303 WWX B C30 1 
HETATM 8661 C  C35 . WWX J 4 .   ? -13.349 10.539  6.248   1.00 29.24 ? 303 WWX B C35 1 
HETATM 8662 C  C34 . WWX J 4 .   ? -14.487 10.394  7.023   1.00 27.77 ? 303 WWX B C34 1 
HETATM 8663 C  C33 . WWX J 4 .   ? -14.409 10.679  8.404   1.00 30.54 ? 303 WWX B C33 1 
HETATM 8664 C  C32 . WWX J 4 .   ? -13.191 11.035  9.031   1.00 27.19 ? 303 WWX B C32 1 
HETATM 8665 C  C31 . WWX J 4 .   ? -12.032 11.145  8.218   1.00 28.89 ? 303 WWX B C31 1 
HETATM 8666 C  C22 . WWX J 4 .   ? -10.334 12.409  5.644   1.00 40.18 ? 303 WWX B C22 1 
HETATM 8667 O  O29 . WWX J 4 .   ? -10.454 12.803  4.299   1.00 47.43 ? 303 WWX B O29 1 
HETATM 8668 C  C23 . WWX J 4 .   ? -10.679 13.512  6.611   1.00 41.96 ? 303 WWX B C23 1 
HETATM 8669 C  C28 . WWX J 4 .   ? -9.644  13.828  7.526   1.00 38.14 ? 303 WWX B C28 1 
HETATM 8670 C  C27 . WWX J 4 .   ? -9.845  14.823  8.516   1.00 40.01 ? 303 WWX B C27 1 
HETATM 8671 C  C26 . WWX J 4 .   ? -11.080 15.509  8.567   1.00 41.48 ? 303 WWX B C26 1 
HETATM 8672 C  C25 . WWX J 4 .   ? -12.106 15.191  7.644   1.00 42.26 ? 303 WWX B C25 1 
HETATM 8673 C  C24 . WWX J 4 .   ? -11.945 14.188  6.668   1.00 38.81 ? 303 WWX B C24 1 
HETATM 8674 ZN ZN  . ZN  K 2 .   ? 37.761  2.310   -30.755 1.00 14.19 ? 301 ZN  C ZN  1 
HETATM 8675 C  C1  . EDO L 3 .   ? 40.920  12.882  -25.768 1.00 38.35 ? 302 EDO C C1  1 
HETATM 8676 O  O1  . EDO L 3 .   ? 39.727  12.364  -26.292 1.00 41.44 ? 302 EDO C O1  1 
HETATM 8677 C  C2  . EDO L 3 .   ? 42.089  12.249  -26.485 1.00 38.04 ? 302 EDO C C2  1 
HETATM 8678 O  O2  . EDO L 3 .   ? 42.381  11.087  -25.737 1.00 33.95 ? 302 EDO C O2  1 
HETATM 8679 O  O16 . WWX M 4 .   ? 43.661  8.955   -30.805 1.00 26.95 ? 303 WWX C O16 1 
HETATM 8680 S  S14 . WWX M 4 .   ? 43.497  8.426   -32.278 1.00 22.40 ? 303 WWX C S14 1 
HETATM 8681 O  O15 . WWX M 4 .   ? 44.545  7.357   -32.394 1.00 21.85 ? 303 WWX C O15 1 
HETATM 8682 C  C18 . WWX M 4 .   ? 44.844  10.541  -33.596 1.00 27.27 ? 303 WWX C C18 1 
HETATM 8683 O  O20 . WWX M 4 .   ? 45.014  11.450  -32.521 1.00 33.44 ? 303 WWX C O20 1 
HETATM 8684 C  C17 . WWX M 4 .   ? 43.488  9.812   -33.453 1.00 25.14 ? 303 WWX C C17 1 
HETATM 8685 C  C8  . WWX M 4 .   ? 42.057  7.317   -32.412 1.00 21.55 ? 303 WWX C C8  1 
HETATM 8686 C  C7  . WWX M 4 .   ? 41.958  6.509   -33.540 1.00 22.62 ? 303 WWX C C7  1 
HETATM 8687 F  F12 . WWX M 4 .   ? 42.899  6.598   -34.517 1.00 22.67 ? 303 WWX C F12 1 
HETATM 8688 C  C6  . WWX M 4 .   ? 40.930  5.588   -33.752 1.00 21.34 ? 303 WWX C C6  1 
HETATM 8689 F  F11 . WWX M 4 .   ? 40.908  4.777   -34.883 1.00 20.31 ? 303 WWX C F11 1 
HETATM 8690 C  C9  . WWX M 4 .   ? 40.995  7.188   -31.449 1.00 22.80 ? 303 WWX C C9  1 
HETATM 8691 C  C10 . WWX M 4 .   ? 39.956  6.228   -31.644 1.00 21.78 ? 303 WWX C C10 1 
HETATM 8692 F  F13 . WWX M 4 .   ? 38.950  6.129   -30.740 1.00 18.27 ? 303 WWX C F13 1 
HETATM 8693 C  C5  . WWX M 4 .   ? 39.905  5.426   -32.800 1.00 19.81 ? 303 WWX C C5  1 
HETATM 8694 S  S1  . WWX M 4 .   ? 38.641  4.125   -33.066 1.00 17.55 ? 303 WWX C S1  1 
HETATM 8695 O  O3  . WWX M 4 .   ? 38.121  4.298   -34.471 1.00 16.57 ? 303 WWX C O3  1 
HETATM 8696 N  N4  . WWX M 4 .   ? 37.243  3.891   -32.000 1.00 10.25 ? 303 WWX C N4  1 
HETATM 8697 O  O2  . WWX M 4 .   ? 39.470  2.870   -32.973 1.00 15.95 ? 303 WWX C O2  1 
HETATM 8698 N  N19 . WWX M 4 .   ? 40.972  7.967   -30.240 1.00 21.69 ? 303 WWX C N19 1 
HETATM 8699 C  C21 . WWX M 4 .   ? 40.032  9.066   -30.124 1.00 22.01 ? 303 WWX C C21 1 
HETATM 8700 C  C30 . WWX M 4 .   ? 40.466  10.280  -30.907 1.00 23.87 ? 303 WWX C C30 1 
HETATM 8701 C  C35 . WWX M 4 .   ? 40.033  10.511  -32.238 1.00 21.27 ? 303 WWX C C35 1 
HETATM 8702 C  C34 . WWX M 4 .   ? 40.463  11.645  -32.992 1.00 22.89 ? 303 WWX C C34 1 
HETATM 8703 C  C33 . WWX M 4 .   ? 41.345  12.598  -32.428 1.00 19.76 ? 303 WWX C C33 1 
HETATM 8704 C  C32 . WWX M 4 .   ? 41.748  12.333  -31.117 1.00 22.55 ? 303 WWX C C32 1 
HETATM 8705 C  C31 . WWX M 4 .   ? 41.397  11.219  -30.362 1.00 22.51 ? 303 WWX C C31 1 
HETATM 8706 C  C22 . WWX M 4 .   ? 39.716  9.385   -28.586 1.00 22.08 ? 303 WWX C C22 1 
HETATM 8707 O  O29 . WWX M 4 .   ? 38.884  10.493  -28.528 1.00 20.97 ? 303 WWX C O29 1 
HETATM 8708 C  C23 . WWX M 4 .   ? 39.255  8.117   -27.990 1.00 24.09 ? 303 WWX C C23 1 
HETATM 8709 C  C28 . WWX M 4 .   ? 37.834  7.887   -27.997 1.00 22.11 ? 303 WWX C C28 1 
HETATM 8710 C  C27 . WWX M 4 .   ? 37.377  6.649   -27.541 1.00 19.31 ? 303 WWX C C27 1 
HETATM 8711 C  C26 . WWX M 4 .   ? 38.229  5.686   -27.075 1.00 19.69 ? 303 WWX C C26 1 
HETATM 8712 C  C25 . WWX M 4 .   ? 39.665  5.935   -27.036 1.00 20.43 ? 303 WWX C C25 1 
HETATM 8713 C  C24 . WWX M 4 .   ? 40.161  7.154   -27.491 1.00 21.61 ? 303 WWX C C24 1 
HETATM 8714 ZN ZN  . ZN  N 2 .   ? 6.777   5.649   -38.428 1.00 8.56  ? 301 ZN  D ZN  1 
HETATM 8715 C  C1  . EDO O 3 .   ? -3.067  -1.511  -21.718 1.00 32.25 ? 302 EDO D C1  1 
HETATM 8716 O  O1  . EDO O 3 .   ? -2.186  -1.525  -22.823 1.00 33.33 ? 302 EDO D O1  1 
HETATM 8717 C  C2  . EDO O 3 .   ? -2.404  -1.355  -20.344 1.00 28.12 ? 302 EDO D C2  1 
HETATM 8718 O  O2  . EDO O 3 .   ? -1.258  -0.524  -20.361 1.00 36.55 ? 302 EDO D O2  1 
HETATM 8719 C  C1  . EDO P 3 .   ? -6.694  13.620  -40.783 1.00 43.52 ? 303 EDO D C1  1 
HETATM 8720 O  O1  . EDO P 3 .   ? -6.311  12.484  -40.038 1.00 39.08 ? 303 EDO D O1  1 
HETATM 8721 C  C2  . EDO P 3 .   ? -7.982  13.371  -41.593 1.00 40.17 ? 303 EDO D C2  1 
HETATM 8722 O  O2  . EDO P 3 .   ? -8.866  12.583  -40.799 1.00 35.95 ? 303 EDO D O2  1 
HETATM 8723 C  C1  . EDO Q 3 .   ? 0.508   -4.091  -55.125 1.00 28.43 ? 304 EDO D C1  1 
HETATM 8724 O  O1  . EDO Q 3 .   ? 0.903   -5.300  -54.455 1.00 26.43 ? 304 EDO D O1  1 
HETATM 8725 C  C2  . EDO Q 3 .   ? -0.706  -4.163  -56.130 1.00 33.28 ? 304 EDO D C2  1 
HETATM 8726 O  O2  . EDO Q 3 .   ? -1.985  -4.624  -55.589 1.00 28.44 ? 304 EDO D O2  1 
HETATM 8727 O  O16 A WWX R 4 .   ? 2.385   13.105  -38.482 0.50 19.50 ? 305 WWX D O16 1 
HETATM 8728 O  O16 B WWX R 4 .   ? 2.403   13.153  -38.470 0.50 19.49 ? 305 WWX D O16 1 
HETATM 8729 S  S14 A WWX R 4 .   ? 2.671   12.753  -37.008 0.50 18.68 ? 305 WWX D S14 1 
HETATM 8730 S  S14 B WWX R 4 .   ? 2.668   12.737  -37.006 0.50 18.66 ? 305 WWX D S14 1 
HETATM 8731 O  O15 A WWX R 4 .   ? 1.327   12.251  -36.477 0.50 20.37 ? 305 WWX D O15 1 
HETATM 8732 O  O15 B WWX R 4 .   ? 1.314   12.258  -36.470 0.50 20.54 ? 305 WWX D O15 1 
HETATM 8733 C  C18 A WWX R 4 .   ? 1.892   15.210  -35.948 0.50 19.53 ? 305 WWX D C18 1 
HETATM 8734 C  C18 B WWX R 4 .   ? 2.291   15.292  -35.748 0.50 19.22 ? 305 WWX D C18 1 
HETATM 8735 O  O20 A WWX R 4 .   ? 1.789   15.885  -37.169 0.50 20.97 ? 305 WWX D O20 1 
HETATM 8736 O  O20 B WWX R 4 .   ? 3.039   16.459  -35.906 0.50 23.37 ? 305 WWX D O20 1 
HETATM 8737 C  C17 A WWX R 4 .   ? 3.085   14.287  -36.102 0.50 18.88 ? 305 WWX D C17 1 
HETATM 8738 C  C17 B WWX R 4 .   ? 3.251   14.144  -36.000 0.50 18.85 ? 305 WWX D C17 1 
HETATM 8739 C  C8  A WWX R 4 .   ? 3.855   11.398  -36.864 0.50 17.02 ? 305 WWX D C8  1 
HETATM 8740 C  C8  B WWX R 4 .   ? 3.847   11.378  -36.880 0.50 17.12 ? 305 WWX D C8  1 
HETATM 8741 C  C7  A WWX R 4 .   ? 3.852   10.695  -35.671 0.50 17.22 ? 305 WWX D C7  1 
HETATM 8742 C  C7  B WWX R 4 .   ? 3.848   10.685  -35.682 0.50 17.29 ? 305 WWX D C7  1 
HETATM 8743 F  F12 A WWX R 4 .   ? 3.093   11.102  -34.605 0.50 17.61 ? 305 WWX D F12 1 
HETATM 8744 F  F12 B WWX R 4 .   ? 3.081   11.096  -34.623 0.50 17.86 ? 305 WWX D F12 1 
HETATM 8745 C  C6  A WWX R 4 .   ? 4.690   9.623   -35.495 0.50 15.71 ? 305 WWX D C6  1 
HETATM 8746 C  C6  B WWX R 4 .   ? 4.686   9.615   -35.500 0.50 15.78 ? 305 WWX D C6  1 
HETATM 8747 F  F11 A WWX R 4 .   ? 4.714   8.958   -34.301 0.50 17.40 ? 305 WWX D F11 1 
HETATM 8748 F  F11 B WWX R 4 .   ? 4.709   8.952   -34.305 0.50 17.47 ? 305 WWX D F11 1 
HETATM 8749 C  C9  A WWX R 4 .   ? 4.705   11.017  -37.922 0.50 17.79 ? 305 WWX D C9  1 
HETATM 8750 C  C9  B WWX R 4 .   ? 4.705   11.007  -37.933 0.50 17.86 ? 305 WWX D C9  1 
HETATM 8751 C  C10 A WWX R 4 .   ? 5.533   9.930   -37.725 0.50 16.38 ? 305 WWX D C10 1 
HETATM 8752 C  C10 B WWX R 4 .   ? 5.535   9.922   -37.731 0.50 16.46 ? 305 WWX D C10 1 
HETATM 8753 F  F13 A WWX R 4 .   ? 6.385   9.592   -38.710 0.50 16.21 ? 305 WWX D F13 1 
HETATM 8754 F  F13 B WWX R 4 .   ? 6.390   9.585   -38.713 0.50 16.30 ? 305 WWX D F13 1 
HETATM 8755 C  C5  A WWX R 4 .   ? 5.580   9.247   -36.499 0.50 15.19 ? 305 WWX D C5  1 
HETATM 8756 C  C5  B WWX R 4 .   ? 5.579   9.242   -36.503 0.50 15.25 ? 305 WWX D C5  1 
HETATM 8757 S  S1  A WWX R 4 .   ? 6.508   7.735   -36.193 0.50 13.35 ? 305 WWX D S1  1 
HETATM 8758 S  S1  B WWX R 4 .   ? 6.508   7.734   -36.194 0.50 13.36 ? 305 WWX D S1  1 
HETATM 8759 O  O3  A WWX R 4 .   ? 7.392   7.942   -34.993 0.50 13.97 ? 305 WWX D O3  1 
HETATM 8760 O  O3  B WWX R 4 .   ? 7.393   7.945   -34.994 0.50 13.98 ? 305 WWX D O3  1 
HETATM 8761 N  N4  A WWX R 4 .   ? 7.513   7.108   -37.410 0.50 11.66 ? 305 WWX D N4  1 
HETATM 8762 N  N4  B WWX R 4 .   ? 7.514   7.107   -37.410 0.50 11.69 ? 305 WWX D N4  1 
HETATM 8763 O  O2  A WWX R 4 .   ? 5.381   6.746   -35.943 0.50 13.67 ? 305 WWX D O2  1 
HETATM 8764 O  O2  B WWX R 4 .   ? 5.383   6.744   -35.942 0.50 13.70 ? 305 WWX D O2  1 
HETATM 8765 N  N19 A WWX R 4 .   ? 4.734   11.727  -39.175 0.50 17.91 ? 305 WWX D N19 1 
HETATM 8766 N  N19 B WWX R 4 .   ? 4.735   11.718  -39.184 0.50 17.94 ? 305 WWX D N19 1 
HETATM 8767 C  C21 A WWX R 4 .   ? 5.925   12.539  -39.522 0.50 17.64 ? 305 WWX D C21 1 
HETATM 8768 C  C21 B WWX R 4 .   ? 5.923   12.535  -39.526 0.50 17.68 ? 305 WWX D C21 1 
HETATM 8769 C  C30 A WWX R 4 .   ? 5.831   13.881  -38.842 0.50 18.48 ? 305 WWX D C30 1 
HETATM 8770 C  C30 B WWX R 4 .   ? 5.828   13.877  -38.844 0.50 18.51 ? 305 WWX D C30 1 
HETATM 8771 C  C35 A WWX R 4 .   ? 6.515   14.122  -37.643 0.50 19.05 ? 305 WWX D C35 1 
HETATM 8772 C  C35 B WWX R 4 .   ? 6.514   14.118  -37.646 0.50 19.08 ? 305 WWX D C35 1 
HETATM 8773 C  C34 A WWX R 4 .   ? 6.453   15.357  -36.981 0.50 19.61 ? 305 WWX D C34 1 
HETATM 8774 C  C34 B WWX R 4 .   ? 6.452   15.353  -36.983 0.50 19.64 ? 305 WWX D C34 1 
HETATM 8775 C  C33 A WWX R 4 .   ? 5.677   16.368  -37.532 0.50 19.17 ? 305 WWX D C33 1 
HETATM 8776 C  C33 B WWX R 4 .   ? 5.675   16.364  -37.532 0.50 19.19 ? 305 WWX D C33 1 
HETATM 8777 C  C32 A WWX R 4 .   ? 4.995   16.129  -38.733 0.50 19.87 ? 305 WWX D C32 1 
HETATM 8778 C  C32 B WWX R 4 .   ? 4.992   16.125  -38.733 0.50 19.90 ? 305 WWX D C32 1 
HETATM 8779 C  C31 A WWX R 4 .   ? 5.060   14.899  -39.398 0.50 19.28 ? 305 WWX D C31 1 
HETATM 8780 C  C31 B WWX R 4 .   ? 5.057   14.895  -39.399 0.50 19.31 ? 305 WWX D C31 1 
HETATM 8781 C  C22 A WWX R 4 .   ? 6.085   12.647  -41.056 0.50 18.09 ? 305 WWX D C22 1 
HETATM 8782 C  C22 B WWX R 4 .   ? 6.084   12.646  -41.059 0.50 18.10 ? 305 WWX D C22 1 
HETATM 8783 O  O29 A WWX R 4 .   ? 7.237   13.422  -41.305 0.50 16.84 ? 305 WWX D O29 1 
HETATM 8784 O  O29 B WWX R 4 .   ? 7.236   13.423  -41.305 0.50 16.85 ? 305 WWX D O29 1 
HETATM 8785 C  C23 A WWX R 4 .   ? 6.255   11.234  -41.489 0.50 19.03 ? 305 WWX D C23 1 
HETATM 8786 C  C23 B WWX R 4 .   ? 6.255   11.233  -41.492 0.50 19.04 ? 305 WWX D C23 1 
HETATM 8787 C  C28 A WWX R 4 .   ? 7.563   10.729  -41.556 0.50 18.78 ? 305 WWX D C28 1 
HETATM 8788 C  C28 B WWX R 4 .   ? 7.564   10.729  -41.558 0.50 18.78 ? 305 WWX D C28 1 
HETATM 8789 C  C27 A WWX R 4 .   ? 7.805   9.393   -41.874 0.50 18.40 ? 305 WWX D C27 1 
HETATM 8790 C  C27 B WWX R 4 .   ? 7.806   9.393   -41.875 0.50 18.40 ? 305 WWX D C27 1 
HETATM 8791 C  C26 A WWX R 4 .   ? 6.730   8.552   -42.130 0.50 17.39 ? 305 WWX D C26 1 
HETATM 8792 C  C26 B WWX R 4 .   ? 6.731   8.551   -42.130 0.50 17.39 ? 305 WWX D C26 1 
HETATM 8793 C  C25 A WWX R 4 .   ? 5.426   9.052   -42.075 0.50 18.02 ? 305 WWX D C25 1 
HETATM 8794 C  C25 B WWX R 4 .   ? 5.427   9.050   -42.076 0.50 18.02 ? 305 WWX D C25 1 
HETATM 8795 C  C24 A WWX R 4 .   ? 5.144   10.407  -41.736 0.50 18.10 ? 305 WWX D C24 1 
HETATM 8796 C  C24 B WWX R 4 .   ? 5.145   10.406  -41.737 0.50 18.11 ? 305 WWX D C24 1 
HETATM 8797 O  O   . HOH S 5 .   ? 8.891   4.136   2.638   1.00 14.16 ? 401 HOH A O   1 
HETATM 8798 O  O   . HOH S 5 .   ? 8.708   3.074   7.317   1.00 10.80 ? 402 HOH A O   1 
HETATM 8799 O  O   . HOH S 5 .   ? 19.356  14.309  4.968   1.00 12.45 ? 403 HOH A O   1 
HETATM 8800 O  O   . HOH S 5 .   ? 15.154  -6.788  21.120  1.00 12.52 ? 404 HOH A O   1 
HETATM 8801 O  O   . HOH S 5 .   ? 6.089   11.812  7.953   1.00 11.76 ? 405 HOH A O   1 
HETATM 8802 O  O   . HOH S 5 .   ? 17.969  3.209   12.677  1.00 11.14 ? 406 HOH A O   1 
HETATM 8803 O  O   . HOH S 5 .   ? 12.041  7.662   8.641   1.00 9.54  ? 407 HOH A O   1 
HETATM 8804 O  O   . HOH S 5 .   ? 17.756  9.669   0.070   1.00 12.51 ? 408 HOH A O   1 
HETATM 8805 O  O   . HOH S 5 .   ? 12.467  -2.505  11.006  1.00 8.74  ? 409 HOH A O   1 
HETATM 8806 O  O   . HOH S 5 .   ? 22.993  -12.382 9.752   1.00 10.56 ? 410 HOH A O   1 
HETATM 8807 O  O   . HOH S 5 .   ? 25.622  -15.946 6.640   1.00 12.09 ? 411 HOH A O   1 
HETATM 8808 O  O   . HOH S 5 .   ? 7.449   5.081   11.144  1.00 11.71 ? 412 HOH A O   1 
HETATM 8809 O  O   . HOH S 5 .   ? 28.508  -4.148  2.648   1.00 11.15 ? 413 HOH A O   1 
HETATM 8810 O  O   . HOH S 5 .   ? 11.391  5.401   2.098   1.00 12.11 ? 414 HOH A O   1 
HETATM 8811 O  O   . HOH S 5 .   ? 31.423  -13.217 2.502   1.00 19.08 ? 415 HOH A O   1 
HETATM 8812 O  O   . HOH S 5 .   ? 8.798   -6.280  7.325   1.00 17.65 ? 416 HOH A O   1 
HETATM 8813 O  O   . HOH S 5 .   ? 29.861  -15.696 -1.642  1.00 18.27 ? 417 HOH A O   1 
HETATM 8814 O  O   . HOH S 5 .   ? 20.990  -2.665  -5.270  1.00 23.38 ? 418 HOH A O   1 
HETATM 8815 O  O   . HOH S 5 .   ? 19.610  -0.681  26.782  1.00 15.03 ? 419 HOH A O   1 
HETATM 8816 O  O   . HOH S 5 .   ? 11.561  8.116   1.643   1.00 13.17 ? 420 HOH A O   1 
HETATM 8817 O  O   . HOH S 5 .   ? 10.335  4.922   8.756   1.00 13.15 ? 421 HOH A O   1 
HETATM 8818 O  O   . HOH S 5 .   ? 10.497  -3.354  2.697   1.00 14.49 ? 422 HOH A O   1 
HETATM 8819 O  O   . HOH S 5 .   ? 13.975  1.987   -2.927  1.00 19.86 ? 423 HOH A O   1 
HETATM 8820 O  O   . HOH S 5 .   ? 14.165  -1.962  28.927  1.00 20.32 ? 424 HOH A O   1 
HETATM 8821 O  O   . HOH S 5 .   ? 9.305   11.631  1.015   1.00 16.22 ? 425 HOH A O   1 
HETATM 8822 O  O   . HOH S 5 .   ? 13.965  1.718   -0.350  1.00 18.27 ? 426 HOH A O   1 
HETATM 8823 O  O   . HOH S 5 .   ? 13.703  16.556  11.724  1.00 16.13 ? 427 HOH A O   1 
HETATM 8824 O  O   . HOH S 5 .   ? 14.318  -9.902  26.059  1.00 18.22 ? 428 HOH A O   1 
HETATM 8825 O  O   . HOH S 5 .   ? 23.399  3.314   -2.088  1.00 17.20 ? 429 HOH A O   1 
HETATM 8826 O  O   . HOH S 5 .   ? 9.661   -2.471  10.432  1.00 17.73 ? 430 HOH A O   1 
HETATM 8827 O  O   . HOH S 5 .   ? 7.814   9.262   14.191  1.00 18.61 ? 431 HOH A O   1 
HETATM 8828 O  O   . HOH S 5 .   ? 18.049  -15.102 6.190   1.00 16.13 ? 432 HOH A O   1 
HETATM 8829 O  O   . HOH S 5 .   ? 5.533   -11.986 13.368  1.00 20.71 ? 433 HOH A O   1 
HETATM 8830 O  O   . HOH S 5 .   ? 14.393  4.461   -4.101  1.00 19.84 ? 434 HOH A O   1 
HETATM 8831 O  O   . HOH S 5 .   ? 17.159  0.777   -0.454  1.00 17.60 ? 435 HOH A O   1 
HETATM 8832 O  O   . HOH S 5 .   ? 5.924   -3.861  -7.976  1.00 29.43 ? 436 HOH A O   1 
HETATM 8833 O  O   . HOH S 5 .   ? 45.887  1.620   25.878  1.00 43.97 ? 437 HOH A O   1 
HETATM 8834 O  O   . HOH S 5 .   ? 12.557  14.660  2.245   1.00 15.14 ? 438 HOH A O   1 
HETATM 8835 O  O   . HOH S 5 .   ? 26.628  5.456   -3.590  1.00 31.69 ? 439 HOH A O   1 
HETATM 8836 O  O   . HOH S 5 .   ? 12.905  -14.389 12.843  1.00 31.24 ? 440 HOH A O   1 
HETATM 8837 O  O   . HOH S 5 .   ? 6.205   -2.922  13.242  1.00 20.53 ? 441 HOH A O   1 
HETATM 8838 O  O   . HOH S 5 .   ? 23.810  -21.298 26.561  1.00 27.04 ? 442 HOH A O   1 
HETATM 8839 O  O   . HOH S 5 .   ? 8.091   6.697   15.485  1.00 16.78 ? 443 HOH A O   1 
HETATM 8840 O  O   . HOH S 5 .   ? 10.681  6.354   15.399  1.00 13.25 ? 444 HOH A O   1 
HETATM 8841 O  O   . HOH S 5 .   ? 18.908  11.891  -0.937  1.00 17.25 ? 445 HOH A O   1 
HETATM 8842 O  O   . HOH S 5 .   ? 30.607  -8.821  -2.447  1.00 18.91 ? 446 HOH A O   1 
HETATM 8843 O  O   . HOH S 5 .   ? 14.905  -13.581 16.479  1.00 17.09 ? 447 HOH A O   1 
HETATM 8844 O  O   . HOH S 5 .   ? 39.932  -12.262 11.803  1.00 18.80 ? 448 HOH A O   1 
HETATM 8845 O  O   . HOH S 5 .   ? 13.353  5.175   -0.522  1.00 20.03 ? 449 HOH A O   1 
HETATM 8846 O  O   . HOH S 5 .   ? 17.295  0.236   28.669  1.00 21.17 ? 450 HOH A O   1 
HETATM 8847 O  O   . HOH S 5 .   ? 7.800   -8.128  11.748  1.00 24.48 ? 451 HOH A O   1 
HETATM 8848 O  O   . HOH S 5 .   ? 11.956  -10.457 27.341  1.00 18.96 ? 452 HOH A O   1 
HETATM 8849 O  O   . HOH S 5 .   ? 15.878  -11.933 27.058  1.00 21.72 ? 453 HOH A O   1 
HETATM 8850 O  O   . HOH S 5 .   ? 33.136  -15.114 3.679   1.00 21.92 ? 454 HOH A O   1 
HETATM 8851 O  O   . HOH S 5 .   ? 19.396  9.532   32.444  1.00 20.18 ? 455 HOH A O   1 
HETATM 8852 O  O   . HOH S 5 .   ? 41.073  -10.570 9.917   1.00 19.41 ? 456 HOH A O   1 
HETATM 8853 O  O   . HOH S 5 .   ? 7.392   -1.883  -0.798  1.00 25.73 ? 457 HOH A O   1 
HETATM 8854 O  O   . HOH S 5 .   ? 23.888  14.980  4.485   1.00 26.25 ? 458 HOH A O   1 
HETATM 8855 O  O   . HOH S 5 .   ? 39.182  3.807   19.814  1.00 27.65 ? 459 HOH A O   1 
HETATM 8856 O  O   . HOH S 5 .   ? 11.828  -15.297 8.563   1.00 20.16 ? 460 HOH A O   1 
HETATM 8857 O  O   . HOH S 5 .   ? 36.868  -4.404  -0.787  1.00 21.34 ? 461 HOH A O   1 
HETATM 8858 O  O   . HOH S 5 .   ? 26.009  -18.532 20.655  1.00 22.61 ? 462 HOH A O   1 
HETATM 8859 O  O   . HOH S 5 .   ? 16.663  11.056  -3.265  1.00 21.25 ? 463 HOH A O   1 
HETATM 8860 O  O   . HOH S 5 .   ? 14.887  -15.900 14.957  1.00 20.47 ? 464 HOH A O   1 
HETATM 8861 O  O   . HOH S 5 .   ? 24.260  -11.913 30.238  1.00 30.79 ? 465 HOH A O   1 
HETATM 8862 O  O   . HOH S 5 .   ? 20.642  -9.942  31.892  1.00 22.23 ? 466 HOH A O   1 
HETATM 8863 O  O   . HOH S 5 .   ? 31.469  -18.914 4.264   1.00 23.01 ? 467 HOH A O   1 
HETATM 8864 O  O   . HOH S 5 .   ? 17.990  5.567   20.972  1.00 18.33 ? 468 HOH A O   1 
HETATM 8865 O  O   . HOH S 5 .   ? 38.361  -15.542 12.281  1.00 25.37 ? 469 HOH A O   1 
HETATM 8866 O  O   . HOH S 5 .   ? 36.918  4.760   14.852  1.00 30.46 ? 470 HOH A O   1 
HETATM 8867 O  O   . HOH S 5 .   ? 36.194  -7.150  26.454  1.00 23.24 ? 471 HOH A O   1 
HETATM 8868 O  O   . HOH S 5 .   ? 26.036  -17.909 17.418  1.00 18.88 ? 472 HOH A O   1 
HETATM 8869 O  O   . HOH S 5 .   ? 12.611  -12.344 16.431  1.00 22.67 ? 473 HOH A O   1 
HETATM 8870 O  O   . HOH S 5 .   ? 11.309  3.502   19.058  1.00 22.86 ? 474 HOH A O   1 
HETATM 8871 O  O   . HOH S 5 .   ? 39.421  -12.757 20.051  1.00 23.70 ? 475 HOH A O   1 
HETATM 8872 O  O   . HOH S 5 .   ? 13.584  -12.505 20.821  1.00 22.41 ? 476 HOH A O   1 
HETATM 8873 O  O   . HOH S 5 .   ? 20.045  13.973  28.725  1.00 22.98 ? 477 HOH A O   1 
HETATM 8874 O  O   . HOH S 5 .   ? 4.925   -9.079  25.701  1.00 28.36 ? 478 HOH A O   1 
HETATM 8875 O  O   . HOH S 5 .   ? 37.163  8.241   27.549  1.00 31.30 ? 479 HOH A O   1 
HETATM 8876 O  O   . HOH S 5 .   ? 25.511  -18.572 12.509  1.00 22.28 ? 480 HOH A O   1 
HETATM 8877 O  O   . HOH S 5 .   ? 32.981  4.942   20.501  1.00 20.53 ? 481 HOH A O   1 
HETATM 8878 O  O   . HOH S 5 .   ? 12.147  -2.598  -12.388 1.00 43.28 ? 482 HOH A O   1 
HETATM 8879 O  O   . HOH S 5 .   ? 8.533   0.042   24.414  1.00 26.37 ? 483 HOH A O   1 
HETATM 8880 O  O   . HOH S 5 .   ? 32.141  -16.934 10.485  1.00 27.07 ? 484 HOH A O   1 
HETATM 8881 O  O   . HOH S 5 .   ? 33.629  6.351   15.681  1.00 31.98 ? 485 HOH A O   1 
HETATM 8882 O  O   . HOH S 5 .   ? 15.070  -14.373 19.050  1.00 18.74 ? 486 HOH A O   1 
HETATM 8883 O  O   . HOH S 5 .   ? 4.819   -0.208  -8.217  1.00 29.31 ? 487 HOH A O   1 
HETATM 8884 O  O   . HOH S 5 .   ? 28.788  2.434   -1.178  1.00 23.31 ? 488 HOH A O   1 
HETATM 8885 O  O   . HOH S 5 .   ? 10.993  -4.492  -5.135  1.00 30.02 ? 489 HOH A O   1 
HETATM 8886 O  O   . HOH S 5 .   ? 9.538   -5.284  -1.504  1.00 27.39 ? 490 HOH A O   1 
HETATM 8887 O  O   . HOH S 5 .   ? 29.066  -15.098 16.983  1.00 19.66 ? 491 HOH A O   1 
HETATM 8888 O  O   . HOH S 5 .   ? 18.653  20.753  8.174   1.00 32.35 ? 492 HOH A O   1 
HETATM 8889 O  O   . HOH S 5 .   ? 10.868  12.337  20.793  1.00 34.56 ? 493 HOH A O   1 
HETATM 8890 O  O   . HOH S 5 .   ? 32.040  -17.078 20.763  1.00 36.75 ? 494 HOH A O   1 
HETATM 8891 O  O   . HOH S 5 .   ? 16.675  -13.601 30.855  1.00 23.55 ? 495 HOH A O   1 
HETATM 8892 O  O   . HOH S 5 .   ? 17.329  -3.487  -8.438  1.00 34.47 ? 496 HOH A O   1 
HETATM 8893 O  O   . HOH S 5 .   ? 27.730  -21.149 24.573  1.00 33.65 ? 497 HOH A O   1 
HETATM 8894 O  O   . HOH S 5 .   ? 33.644  -13.473 26.757  1.00 26.36 ? 498 HOH A O   1 
HETATM 8895 O  O   . HOH S 5 .   ? 23.175  10.847  13.186  1.00 23.56 ? 499 HOH A O   1 
HETATM 8896 O  O   . HOH S 5 .   ? 44.083  -10.095 8.375   1.00 25.34 ? 500 HOH A O   1 
HETATM 8897 O  O   . HOH S 5 .   ? 48.098  -9.233  25.085  1.00 37.46 ? 501 HOH A O   1 
HETATM 8898 O  O   . HOH S 5 .   ? 29.613  12.097  -4.508  1.00 34.22 ? 502 HOH A O   1 
HETATM 8899 O  O   . HOH S 5 .   ? 38.279  -13.515 5.672   1.00 22.65 ? 503 HOH A O   1 
HETATM 8900 O  O   . HOH S 5 .   ? 18.142  -19.789 1.541   1.00 30.88 ? 504 HOH A O   1 
HETATM 8901 O  O   . HOH S 5 .   ? 20.844  17.970  7.627   1.00 32.78 ? 505 HOH A O   1 
HETATM 8902 O  O   . HOH S 5 .   ? 27.486  -5.567  -5.192  1.00 23.93 ? 506 HOH A O   1 
HETATM 8903 O  O   . HOH S 5 .   ? 38.617  4.064   11.497  1.00 23.64 ? 507 HOH A O   1 
HETATM 8904 O  O   . HOH S 5 .   ? 8.116   -10.522 26.228  1.00 26.78 ? 508 HOH A O   1 
HETATM 8905 O  O   . HOH S 5 .   ? 36.813  7.516   9.988   1.00 28.91 ? 509 HOH A O   1 
HETATM 8906 O  O   . HOH S 5 .   ? 17.146  8.141   20.256  1.00 24.84 ? 510 HOH A O   1 
HETATM 8907 O  O   . HOH S 5 .   ? 29.980  -3.932  -5.517  1.00 34.12 ? 511 HOH A O   1 
HETATM 8908 O  O   . HOH S 5 .   ? 32.196  -18.437 7.031   1.00 29.09 ? 512 HOH A O   1 
HETATM 8909 O  O   . HOH S 5 .   ? 7.342   -6.658  2.310   1.00 21.50 ? 513 HOH A O   1 
HETATM 8910 O  O   . HOH S 5 .   ? 38.047  -7.631  24.506  1.00 28.99 ? 514 HOH A O   1 
HETATM 8911 O  O   . HOH S 5 .   ? 9.539   -14.308 1.755   1.00 30.48 ? 515 HOH A O   1 
HETATM 8912 O  O   . HOH S 5 .   ? 6.712   -9.903  4.353   1.00 30.79 ? 516 HOH A O   1 
HETATM 8913 O  O   . HOH S 5 .   ? 24.975  13.969  33.466  1.00 33.50 ? 517 HOH A O   1 
HETATM 8914 O  O   . HOH S 5 .   ? 43.567  -9.667  11.505  1.00 26.68 ? 518 HOH A O   1 
HETATM 8915 O  O   . HOH S 5 .   ? 15.677  4.695   21.921  1.00 22.29 ? 519 HOH A O   1 
HETATM 8916 O  O   . HOH S 5 .   ? 11.344  3.993   -0.056  1.00 26.13 ? 520 HOH A O   1 
HETATM 8917 O  O   . HOH S 5 .   ? 24.983  16.119  2.231   1.00 26.17 ? 521 HOH A O   1 
HETATM 8918 O  O   . HOH S 5 .   ? 26.428  10.920  31.276  1.00 25.61 ? 522 HOH A O   1 
HETATM 8919 O  O   . HOH S 5 .   ? 10.201  -3.925  19.243  1.00 29.99 ? 523 HOH A O   1 
HETATM 8920 O  O   . HOH S 5 .   ? 31.141  -21.011 8.658   1.00 27.61 ? 524 HOH A O   1 
HETATM 8921 O  O   . HOH S 5 .   ? 4.960   -7.008  1.234   1.00 23.08 ? 525 HOH A O   1 
HETATM 8922 O  O   . HOH S 5 .   ? 9.699   -3.223  27.750  1.00 35.09 ? 526 HOH A O   1 
HETATM 8923 O  O   . HOH S 5 .   ? 27.891  3.617   33.921  1.00 26.94 ? 527 HOH A O   1 
HETATM 8924 O  O   . HOH S 5 .   ? 9.180   2.198   -8.128  1.00 35.70 ? 528 HOH A O   1 
HETATM 8925 O  O   . HOH S 5 .   ? 35.282  10.133  10.599  1.00 32.50 ? 529 HOH A O   1 
HETATM 8926 O  O   . HOH S 5 .   ? 23.378  4.481   37.995  1.00 33.01 ? 530 HOH A O   1 
HETATM 8927 O  O   . HOH S 5 .   ? 13.199  14.399  14.135  1.00 24.88 ? 531 HOH A O   1 
HETATM 8928 O  O   . HOH S 5 .   ? 26.780  13.373  24.813  1.00 34.48 ? 532 HOH A O   1 
HETATM 8929 O  O   . HOH S 5 .   ? 23.612  -16.301 29.650  1.00 29.48 ? 533 HOH A O   1 
HETATM 8930 O  O   . HOH S 5 .   ? 41.683  -9.159  24.367  1.00 41.31 ? 534 HOH A O   1 
HETATM 8931 O  O   . HOH S 5 .   ? 11.068  -5.127  0.721   1.00 20.59 ? 535 HOH A O   1 
HETATM 8932 O  O   . HOH S 5 .   ? 32.572  6.304   13.104  1.00 28.45 ? 536 HOH A O   1 
HETATM 8933 O  O   . HOH S 5 .   ? 18.448  -3.129  -5.787  1.00 28.01 ? 537 HOH A O   1 
HETATM 8934 O  O   . HOH S 5 .   ? 19.382  -18.480 26.335  1.00 23.61 ? 538 HOH A O   1 
HETATM 8935 O  O   . HOH S 5 .   ? 37.313  7.344   30.135  1.00 26.78 ? 539 HOH A O   1 
HETATM 8936 O  O   . HOH S 5 .   ? 30.126  -17.809 18.682  1.00 27.64 ? 540 HOH A O   1 
HETATM 8937 O  O   . HOH S 5 .   ? 32.635  -16.257 12.956  1.00 37.03 ? 541 HOH A O   1 
HETATM 8938 O  O   . HOH S 5 .   ? 45.181  -4.356  7.572   1.00 26.14 ? 542 HOH A O   1 
HETATM 8939 O  O   . HOH S 5 .   ? 9.368   -10.893 14.330  1.00 32.88 ? 543 HOH A O   1 
HETATM 8940 O  O   . HOH S 5 .   ? 8.054   -13.091 -1.464  1.00 31.18 ? 544 HOH A O   1 
HETATM 8941 O  O   . HOH S 5 .   ? 11.648  1.542   -4.031  1.00 30.71 ? 545 HOH A O   1 
HETATM 8942 O  O   . HOH S 5 .   ? 41.047  -4.256  0.771   1.00 29.31 ? 546 HOH A O   1 
HETATM 8943 O  O   . HOH S 5 .   ? 18.897  12.799  20.754  1.00 39.61 ? 547 HOH A O   1 
HETATM 8944 O  O   . HOH S 5 .   ? 11.299  9.843   -2.172  1.00 28.22 ? 548 HOH A O   1 
HETATM 8945 O  O   . HOH S 5 .   ? 27.451  -16.133 -5.521  1.00 29.31 ? 549 HOH A O   1 
HETATM 8946 O  O   . HOH S 5 .   ? 36.714  6.232   12.135  1.00 34.33 ? 550 HOH A O   1 
HETATM 8947 O  O   . HOH S 5 .   ? 19.988  -7.319  32.390  1.00 25.13 ? 551 HOH A O   1 
HETATM 8948 O  O   . HOH S 5 .   ? 27.634  -4.912  31.276  1.00 27.98 ? 552 HOH A O   1 
HETATM 8949 O  O   . HOH S 5 .   ? 32.505  -15.109 28.130  1.00 32.43 ? 553 HOH A O   1 
HETATM 8950 O  O   . HOH S 5 .   ? 16.361  -18.593 12.647  1.00 33.76 ? 554 HOH A O   1 
HETATM 8951 O  O   . HOH S 5 .   ? 26.774  -19.357 -1.256  1.00 36.84 ? 555 HOH A O   1 
HETATM 8952 O  O   . HOH S 5 .   ? 23.979  -21.386 -3.502  1.00 31.26 ? 556 HOH A O   1 
HETATM 8953 O  O   . HOH S 5 .   ? 14.593  -12.423 29.467  1.00 24.82 ? 557 HOH A O   1 
HETATM 8954 O  O   . HOH S 5 .   ? 5.338   -12.964 15.743  1.00 25.84 ? 558 HOH A O   1 
HETATM 8955 O  O   . HOH S 5 .   ? 24.949  -18.297 30.411  1.00 36.55 ? 559 HOH A O   1 
HETATM 8956 O  O   . HOH S 5 .   ? 28.689  -18.710 20.622  1.00 24.84 ? 560 HOH A O   1 
HETATM 8957 O  O   . HOH S 5 .   ? 26.605  13.509  8.002   1.00 30.93 ? 561 HOH A O   1 
HETATM 8958 O  O   . HOH S 5 .   ? 12.614  11.505  -3.715  1.00 27.65 ? 562 HOH A O   1 
HETATM 8959 O  O   . HOH S 5 .   ? 28.147  8.876   17.405  1.00 27.70 ? 563 HOH A O   1 
HETATM 8960 O  O   . HOH S 5 .   ? 24.987  10.515  17.191  1.00 35.51 ? 564 HOH A O   1 
HETATM 8961 O  O   . HOH S 5 .   ? 20.323  21.942  9.283   1.00 35.74 ? 565 HOH A O   1 
HETATM 8962 O  O   . HOH S 5 .   ? 22.773  16.627  7.999   1.00 41.36 ? 566 HOH A O   1 
HETATM 8963 O  O   . HOH S 5 .   ? 25.989  11.784  6.438   1.00 30.43 ? 567 HOH A O   1 
HETATM 8964 O  O   . HOH S 5 .   ? 24.321  12.079  0.410   1.00 29.76 ? 568 HOH A O   1 
HETATM 8965 O  O   . HOH S 5 .   ? 21.169  11.813  -2.805  1.00 27.18 ? 569 HOH A O   1 
HETATM 8966 O  O   . HOH S 5 .   ? 19.270  10.516  -4.445  1.00 29.77 ? 570 HOH A O   1 
HETATM 8967 O  O   . HOH S 5 .   ? 18.696  6.573   -6.833  1.00 39.11 ? 571 HOH A O   1 
HETATM 8968 O  O   . HOH S 5 .   ? 15.191  4.569   -6.628  1.00 30.48 ? 572 HOH A O   1 
HETATM 8969 O  O   . HOH S 5 .   ? 11.930  5.414   -4.276  1.00 36.68 ? 573 HOH A O   1 
HETATM 8970 O  O   . HOH S 5 .   ? 10.121  4.168   -2.708  1.00 37.78 ? 574 HOH A O   1 
HETATM 8971 O  O   . HOH S 5 .   ? 21.294  16.228  4.857   1.00 26.92 ? 575 HOH A O   1 
HETATM 8972 O  O   . HOH S 5 .   ? 33.679  -17.432 2.924   1.00 27.26 ? 576 HOH A O   1 
HETATM 8973 O  O   . HOH S 5 .   ? 30.185  -18.068 -2.765  1.00 29.16 ? 577 HOH A O   1 
HETATM 8974 O  O   . HOH S 5 .   ? 29.855  9.925   33.859  1.00 28.91 ? 578 HOH A O   1 
HETATM 8975 O  O   . HOH S 5 .   ? 7.174   -2.056  25.912  1.00 31.19 ? 579 HOH A O   1 
HETATM 8976 O  O   . HOH S 5 .   ? 21.598  2.669   -6.870  1.00 28.09 ? 580 HOH A O   1 
HETATM 8977 O  O   . HOH S 5 .   ? 35.054  -1.251  30.771  1.00 33.43 ? 581 HOH A O   1 
HETATM 8978 O  O   . HOH S 5 .   ? 17.511  20.531  5.885   1.00 30.54 ? 582 HOH A O   1 
HETATM 8979 O  O   . HOH S 5 .   ? 14.749  -14.007 25.490  1.00 26.94 ? 583 HOH A O   1 
HETATM 8980 O  O   . HOH S 5 .   ? 36.622  13.897  -1.009  1.00 33.08 ? 584 HOH A O   1 
HETATM 8981 O  O   . HOH S 5 .   ? 13.815  -17.062 7.401   1.00 28.15 ? 585 HOH A O   1 
HETATM 8982 O  O   . HOH S 5 .   ? 34.302  16.946  1.340   1.00 40.37 ? 586 HOH A O   1 
HETATM 8983 O  O   . HOH S 5 .   ? 25.583  6.246   37.668  1.00 28.60 ? 587 HOH A O   1 
HETATM 8984 O  O   . HOH S 5 .   ? 42.124  -14.208 11.946  1.00 30.25 ? 588 HOH A O   1 
HETATM 8985 O  O   . HOH S 5 .   ? 11.342  2.605   -6.693  1.00 40.33 ? 589 HOH A O   1 
HETATM 8986 O  O   . HOH S 5 .   ? 34.423  3.504   31.772  1.00 34.41 ? 590 HOH A O   1 
HETATM 8987 O  O   . HOH S 5 .   ? 20.098  7.829   -4.711  1.00 38.62 ? 591 HOH A O   1 
HETATM 8988 O  O   . HOH S 5 .   ? 23.660  -4.323  -5.495  1.00 33.36 ? 592 HOH A O   1 
HETATM 8989 O  O   . HOH S 5 .   ? 16.856  2.239   -7.834  1.00 31.50 ? 593 HOH A O   1 
HETATM 8990 O  O   . HOH S 5 .   ? 46.240  -9.353  16.864  1.00 39.88 ? 594 HOH A O   1 
HETATM 8991 O  O   . HOH S 5 .   ? 22.210  -19.235 14.974  1.00 30.85 ? 595 HOH A O   1 
HETATM 8992 O  O   . HOH S 5 .   ? 7.327   -0.781  -14.071 1.00 43.90 ? 596 HOH A O   1 
HETATM 8993 O  O   . HOH S 5 .   ? 19.385  -6.349  -11.889 1.00 33.40 ? 597 HOH A O   1 
HETATM 8994 O  O   . HOH S 5 .   ? 17.803  19.713  0.000   1.00 40.60 ? 598 HOH A O   1 
HETATM 8995 O  O   . HOH S 5 .   ? 6.619   15.835  15.637  1.00 30.00 ? 599 HOH A O   1 
HETATM 8996 O  O   . HOH S 5 .   ? 10.513  -9.188  -8.178  1.00 29.34 ? 600 HOH A O   1 
HETATM 8997 O  O   . HOH S 5 .   ? 17.418  -16.488 -8.015  1.00 28.99 ? 601 HOH A O   1 
HETATM 8998 O  O   . HOH S 5 .   ? 33.799  -4.158  32.492  1.00 33.83 ? 602 HOH A O   1 
HETATM 8999 O  O   . HOH S 5 .   ? 51.795  -9.480  26.921  1.00 42.21 ? 603 HOH A O   1 
HETATM 9000 O  O   . HOH S 5 .   ? 32.712  -18.459 27.894  1.00 38.59 ? 604 HOH A O   1 
HETATM 9001 O  O   . HOH S 5 .   ? 9.620   -4.833  16.407  1.00 33.24 ? 605 HOH A O   1 
HETATM 9002 O  O   . HOH S 5 .   ? 42.755  -1.216  5.885   1.00 32.65 ? 606 HOH A O   1 
HETATM 9003 O  O   . HOH S 5 .   ? 28.625  -24.214 8.344   1.00 37.14 ? 607 HOH A O   1 
HETATM 9004 O  O   . HOH S 5 .   ? 32.281  8.517   12.144  1.00 36.55 ? 608 HOH A O   1 
HETATM 9005 O  O   . HOH S 5 .   ? 28.472  7.739   15.148  1.00 31.44 ? 609 HOH A O   1 
HETATM 9006 O  O   . HOH S 5 .   ? 9.917   3.046   22.748  1.00 27.75 ? 610 HOH A O   1 
HETATM 9007 O  O   . HOH S 5 .   ? 15.628  13.933  -0.510  1.00 33.83 ? 611 HOH A O   1 
HETATM 9008 O  O   . HOH S 5 .   ? 22.360  7.242   -4.331  1.00 30.50 ? 612 HOH A O   1 
HETATM 9009 O  O   . HOH S 5 .   ? 23.913  11.239  -2.238  1.00 32.61 ? 613 HOH A O   1 
HETATM 9010 O  O   . HOH S 5 .   ? 19.978  -15.372 -11.146 1.00 39.85 ? 614 HOH A O   1 
HETATM 9011 O  O   . HOH S 5 .   ? 36.665  -14.373 -1.996  1.00 36.63 ? 615 HOH A O   1 
HETATM 9012 O  O   . HOH S 5 .   ? 45.290  -4.305  15.512  1.00 33.28 ? 616 HOH A O   1 
HETATM 9013 O  O   . HOH S 5 .   ? 38.813  -5.519  -2.965  1.00 28.83 ? 617 HOH A O   1 
HETATM 9014 O  O   . HOH S 5 .   ? 11.226  -12.867 26.194  1.00 34.97 ? 618 HOH A O   1 
HETATM 9015 O  O   . HOH S 5 .   ? 15.145  -17.241 19.386  1.00 32.85 ? 619 HOH A O   1 
HETATM 9016 O  O   . HOH S 5 .   ? 30.644  14.762  4.506   1.00 36.23 ? 620 HOH A O   1 
HETATM 9017 O  O   . HOH S 5 .   ? 34.134  1.717   -5.744  1.00 33.24 ? 621 HOH A O   1 
HETATM 9018 O  O   . HOH S 5 .   ? 23.634  -22.613 18.526  1.00 44.37 ? 622 HOH A O   1 
HETATM 9019 O  O   . HOH S 5 .   ? 23.806  -19.446 16.783  1.00 30.45 ? 623 HOH A O   1 
HETATM 9020 O  O   . HOH S 5 .   ? 36.370  -14.071 26.694  1.00 45.51 ? 624 HOH A O   1 
HETATM 9021 O  O   . HOH S 5 .   ? 25.687  16.572  25.176  1.00 39.06 ? 625 HOH A O   1 
HETATM 9022 O  O   . HOH S 5 .   ? 29.291  -16.906 14.912  1.00 28.20 ? 626 HOH A O   1 
HETATM 9023 O  O   . HOH S 5 .   ? 24.808  -23.120 10.589  1.00 38.08 ? 627 HOH A O   1 
HETATM 9024 O  O   . HOH S 5 .   ? 19.921  -19.745 8.873   1.00 32.93 ? 628 HOH A O   1 
HETATM 9025 O  O   . HOH S 5 .   ? 26.212  2.536   -2.576  1.00 36.34 ? 629 HOH A O   1 
HETATM 9026 O  O   . HOH S 5 .   ? 11.595  9.962   32.589  1.00 36.59 ? 630 HOH A O   1 
HETATM 9027 O  O   . HOH S 5 .   ? 12.088  4.917   29.444  1.00 34.39 ? 631 HOH A O   1 
HETATM 9028 O  O   . HOH S 5 .   ? 10.909  1.456   -12.278 1.00 32.68 ? 632 HOH A O   1 
HETATM 9029 O  O   . HOH S 5 .   ? 5.444   -2.926  -10.422 1.00 36.67 ? 633 HOH A O   1 
HETATM 9030 O  O   . HOH S 5 .   ? 12.904  11.497  -6.549  1.00 32.04 ? 634 HOH A O   1 
HETATM 9031 O  O   . HOH S 5 .   ? 9.699   -16.762 8.382   1.00 32.95 ? 635 HOH A O   1 
HETATM 9032 O  O   . HOH S 5 .   ? 7.949   -1.597  15.265  1.00 29.58 ? 636 HOH A O   1 
HETATM 9033 O  O   . HOH S 5 .   ? 26.284  8.961   -7.385  1.00 38.82 ? 637 HOH A O   1 
HETATM 9034 O  O   . HOH S 5 .   ? 14.866  7.203   21.128  1.00 29.67 ? 638 HOH A O   1 
HETATM 9035 O  O   . HOH S 5 .   ? 36.543  1.561   30.862  1.00 34.42 ? 639 HOH A O   1 
HETATM 9036 O  O   . HOH S 5 .   ? 23.086  15.479  12.963  1.00 30.00 ? 640 HOH A O   1 
HETATM 9037 O  O   . HOH S 5 .   ? 25.781  14.374  10.537  1.00 30.00 ? 641 HOH A O   1 
HETATM 9038 O  O   . HOH S 5 .   ? 29.242  13.079  8.076   1.00 30.00 ? 642 HOH A O   1 
HETATM 9039 O  O   . HOH S 5 .   ? 8.609   -13.731 28.041  1.00 39.87 ? 643 HOH A O   1 
HETATM 9040 O  O   . HOH T 5 .   ? -16.994 -10.443 20.241  1.00 14.36 ? 401 HOH B O   1 
HETATM 9041 O  O   . HOH T 5 .   ? 4.268   8.349   7.705   1.00 11.89 ? 402 HOH B O   1 
HETATM 9042 O  O   . HOH T 5 .   ? -10.316 -8.881  8.235   1.00 10.66 ? 403 HOH B O   1 
HETATM 9043 O  O   . HOH T 5 .   ? 5.387   5.675   7.713   1.00 10.41 ? 404 HOH B O   1 
HETATM 9044 O  O   . HOH T 5 .   ? 1.706   -1.437  5.816   1.00 9.40  ? 405 HOH B O   1 
HETATM 9045 O  O   . HOH T 5 .   ? 11.036  11.327  8.081   1.00 10.85 ? 406 HOH B O   1 
HETATM 9046 O  O   . HOH T 5 .   ? -0.413  12.101  16.302  1.00 15.97 ? 407 HOH B O   1 
HETATM 9047 O  O   . HOH T 5 .   ? 6.643   4.965   13.786  1.00 13.55 ? 408 HOH B O   1 
HETATM 9048 O  O   . HOH T 5 .   ? -18.032 9.470   -2.592  1.00 15.53 ? 409 HOH B O   1 
HETATM 9049 O  O   . HOH T 5 .   ? -4.247  16.187  -11.263 1.00 13.15 ? 410 HOH B O   1 
HETATM 9050 O  O   . HOH T 5 .   ? 1.454   14.479  -11.147 1.00 13.25 ? 411 HOH B O   1 
HETATM 9051 O  O   . HOH T 5 .   ? -35.355 2.390   1.172   1.00 16.73 ? 412 HOH B O   1 
HETATM 9052 O  O   . HOH T 5 .   ? -2.653  5.295   4.027   1.00 10.49 ? 413 HOH B O   1 
HETATM 9053 O  O   . HOH T 5 .   ? -18.335 -8.050  16.104  1.00 14.86 ? 414 HOH B O   1 
HETATM 9054 O  O   . HOH T 5 .   ? -3.044  7.396   -3.893  1.00 14.05 ? 415 HOH B O   1 
HETATM 9055 O  O   . HOH T 5 .   ? -4.505  11.452  -15.049 1.00 15.27 ? 416 HOH B O   1 
HETATM 9056 O  O   . HOH T 5 .   ? -13.315 -11.901 11.664  1.00 12.94 ? 417 HOH B O   1 
HETATM 9057 O  O   . HOH T 5 .   ? -12.355 -13.435 -11.292 1.00 15.95 ? 418 HOH B O   1 
HETATM 9058 O  O   . HOH T 5 .   ? -3.584  2.337   -11.978 1.00 12.33 ? 419 HOH B O   1 
HETATM 9059 O  O   . HOH T 5 .   ? -7.922  -15.543 -7.787  1.00 14.31 ? 420 HOH B O   1 
HETATM 9060 O  O   . HOH T 5 .   ? 2.190   6.184   -12.540 1.00 17.36 ? 421 HOH B O   1 
HETATM 9061 O  O   . HOH T 5 .   ? -2.899  -5.255  -4.092  1.00 10.61 ? 422 HOH B O   1 
HETATM 9062 O  O   . HOH T 5 .   ? 6.674   3.418   9.138   1.00 10.80 ? 423 HOH B O   1 
HETATM 9063 O  O   . HOH T 5 .   ? -17.064 -10.734 1.336   1.00 16.46 ? 424 HOH B O   1 
HETATM 9064 O  O   . HOH T 5 .   ? -3.749  13.991  -6.988  1.00 21.24 ? 425 HOH B O   1 
HETATM 9065 O  O   . HOH T 5 .   ? 5.185   6.549   0.987   1.00 11.72 ? 426 HOH B O   1 
HETATM 9066 O  O   . HOH T 5 .   ? -6.658  -8.753  -18.301 1.00 20.76 ? 427 HOH B O   1 
HETATM 9067 O  O   . HOH T 5 .   ? -24.271 9.113   -1.634  1.00 18.41 ? 428 HOH B O   1 
HETATM 9068 O  O   . HOH T 5 .   ? 5.045   9.282   14.364  1.00 14.84 ? 429 HOH B O   1 
HETATM 9069 O  O   . HOH T 5 .   ? -1.119  5.996   -4.949  1.00 12.61 ? 430 HOH B O   1 
HETATM 9070 O  O   . HOH T 5 .   ? -1.461  16.770  11.219  1.00 15.49 ? 431 HOH B O   1 
HETATM 9071 O  O   . HOH T 5 .   ? -24.714 -2.439  -6.318  1.00 15.95 ? 432 HOH B O   1 
HETATM 9072 O  O   . HOH T 5 .   ? 3.794   -2.070  13.968  1.00 14.76 ? 433 HOH B O   1 
HETATM 9073 O  O   . HOH T 5 .   ? 1.667   6.681   -8.190  1.00 15.14 ? 434 HOH B O   1 
HETATM 9074 O  O   . HOH T 5 .   ? -13.975 -14.743 5.890   1.00 17.50 ? 435 HOH B O   1 
HETATM 9075 O  O   . HOH T 5 .   ? -4.523  0.447   22.003  1.00 21.63 ? 436 HOH B O   1 
HETATM 9076 O  O   . HOH T 5 .   ? 8.157   4.729   5.160   1.00 9.83  ? 437 HOH B O   1 
HETATM 9077 O  O   . HOH T 5 .   ? 4.369   -1.990  6.539   1.00 14.98 ? 438 HOH B O   1 
HETATM 9078 O  O   . HOH T 5 .   ? 0.564   8.266   -4.449  1.00 16.62 ? 439 HOH B O   1 
HETATM 9079 O  O   . HOH T 5 .   ? -6.026  -15.645 25.486  1.00 21.95 ? 440 HOH B O   1 
HETATM 9080 O  O   . HOH T 5 .   ? -9.069  -7.772  -14.407 1.00 16.99 ? 441 HOH B O   1 
HETATM 9081 O  O   . HOH T 5 .   ? -0.130  16.776  -11.130 1.00 19.64 ? 442 HOH B O   1 
HETATM 9082 O  O   . HOH T 5 .   ? -5.610  1.654   -9.887  1.00 10.30 ? 443 HOH B O   1 
HETATM 9083 O  O   . HOH T 5 .   ? -21.857 -8.692  -8.310  1.00 20.29 ? 444 HOH B O   1 
HETATM 9084 O  O   . HOH T 5 .   ? -7.744  -9.884  -15.823 1.00 19.22 ? 445 HOH B O   1 
HETATM 9085 O  O   . HOH T 5 .   ? -5.741  -12.558 11.780  1.00 16.75 ? 446 HOH B O   1 
HETATM 9086 O  O   . HOH T 5 .   ? 3.710   3.616   -2.412  1.00 15.94 ? 447 HOH B O   1 
HETATM 9087 O  O   . HOH T 5 .   ? 4.221   10.187  -6.734  1.00 18.57 ? 448 HOH B O   1 
HETATM 9088 O  O   . HOH T 5 .   ? -30.827 7.311   -3.870  1.00 24.59 ? 449 HOH B O   1 
HETATM 9089 O  O   . HOH T 5 .   ? 5.942   2.344   -3.556  1.00 25.91 ? 450 HOH B O   1 
HETATM 9090 O  O   . HOH T 5 .   ? 7.791   6.109   0.724   1.00 21.42 ? 451 HOH B O   1 
HETATM 9091 O  O   . HOH T 5 .   ? 5.902   -9.275  13.459  1.00 18.33 ? 452 HOH B O   1 
HETATM 9092 O  O   . HOH T 5 .   ? 9.198   7.302   8.418   1.00 17.33 ? 453 HOH B O   1 
HETATM 9093 O  O   . HOH T 5 .   ? 1.614   9.039   -6.835  1.00 13.13 ? 454 HOH B O   1 
HETATM 9094 O  O   . HOH T 5 .   ? -23.200 9.582   6.643   1.00 20.17 ? 455 HOH B O   1 
HETATM 9095 O  O   . HOH T 5 .   ? 4.513   6.569   14.128  1.00 12.86 ? 456 HOH B O   1 
HETATM 9096 O  O   . HOH T 5 .   ? -23.097 -2.205  -8.553  1.00 17.02 ? 457 HOH B O   1 
HETATM 9097 O  O   . HOH T 5 .   ? 5.724   12.478  -4.388  1.00 21.84 ? 458 HOH B O   1 
HETATM 9098 O  O   . HOH T 5 .   ? -3.557  -8.708  -9.149  1.00 27.19 ? 459 HOH B O   1 
HETATM 9099 O  O   . HOH T 5 .   ? 7.827   -3.160  3.540   1.00 18.16 ? 460 HOH B O   1 
HETATM 9100 O  O   . HOH T 5 .   ? -1.220  -0.500  -12.624 1.00 17.77 ? 461 HOH B O   1 
HETATM 9101 O  O   . HOH T 5 .   ? -21.500 -12.050 15.903  1.00 26.45 ? 462 HOH B O   1 
HETATM 9102 O  O   . HOH T 5 .   ? -10.565 14.507  -13.721 1.00 15.53 ? 463 HOH B O   1 
HETATM 9103 O  O   . HOH T 5 .   ? -17.873 12.789  -12.531 1.00 22.88 ? 464 HOH B O   1 
HETATM 9104 O  O   . HOH T 5 .   ? -14.579 -14.019 0.863   1.00 19.29 ? 465 HOH B O   1 
HETATM 9105 O  O   . HOH T 5 .   ? -3.224  -12.559 -0.929  1.00 19.80 ? 466 HOH B O   1 
HETATM 9106 O  O   . HOH T 5 .   ? -20.429 -9.681  15.018  1.00 20.95 ? 467 HOH B O   1 
HETATM 9107 O  O   . HOH T 5 .   ? -7.031  7.055   19.178  1.00 20.76 ? 468 HOH B O   1 
HETATM 9108 O  O   . HOH T 5 .   ? -13.776 7.543   -15.619 1.00 16.35 ? 469 HOH B O   1 
HETATM 9109 O  O   . HOH T 5 .   ? -27.627 -4.067  9.030   1.00 20.27 ? 470 HOH B O   1 
HETATM 9110 O  O   . HOH T 5 .   ? -13.880 0.454   15.348  1.00 15.52 ? 471 HOH B O   1 
HETATM 9111 O  O   . HOH T 5 .   ? 8.678   8.738   1.864   1.00 19.41 ? 472 HOH B O   1 
HETATM 9112 O  O   . HOH T 5 .   ? -1.769  9.733   -3.336  1.00 17.65 ? 473 HOH B O   1 
HETATM 9113 O  O   . HOH T 5 .   ? -1.977  -11.331 -3.102  1.00 17.46 ? 474 HOH B O   1 
HETATM 9114 O  O   . HOH T 5 .   ? 5.915   -0.420  -2.599  1.00 29.06 ? 475 HOH B O   1 
HETATM 9115 O  O   . HOH T 5 .   ? 4.326   3.408   -5.933  1.00 22.16 ? 476 HOH B O   1 
HETATM 9116 O  O   . HOH T 5 .   ? -13.555 -11.735 -13.042 1.00 26.57 ? 477 HOH B O   1 
HETATM 9117 O  O   . HOH T 5 .   ? 8.923   16.760  0.832   1.00 18.11 ? 478 HOH B O   1 
HETATM 9118 O  O   . HOH T 5 .   ? -8.189  -5.513  -15.545 1.00 26.64 ? 479 HOH B O   1 
HETATM 9119 O  O   . HOH T 5 .   ? -2.115  11.824  -5.184  1.00 15.83 ? 480 HOH B O   1 
HETATM 9120 O  O   . HOH T 5 .   ? -20.955 -10.687 -9.757  1.00 26.15 ? 481 HOH B O   1 
HETATM 9121 O  O   . HOH T 5 .   ? -3.806  12.664  -18.307 1.00 18.90 ? 482 HOH B O   1 
HETATM 9122 O  O   . HOH T 5 .   ? -33.670 -4.670  12.969  1.00 26.52 ? 483 HOH B O   1 
HETATM 9123 O  O   . HOH T 5 .   ? -17.391 -12.596 3.563   1.00 23.23 ? 484 HOH B O   1 
HETATM 9124 O  O   . HOH T 5 .   ? -2.814  -0.065  25.307  1.00 28.84 ? 485 HOH B O   1 
HETATM 9125 O  O   . HOH T 5 .   ? -17.646 -14.166 -2.140  1.00 28.08 ? 486 HOH B O   1 
HETATM 9126 O  O   . HOH T 5 .   ? -16.633 -14.101 27.812  1.00 23.86 ? 487 HOH B O   1 
HETATM 9127 O  O   . HOH T 5 .   ? -30.099 -1.557  -9.274  1.00 29.66 ? 488 HOH B O   1 
HETATM 9128 O  O   . HOH T 5 .   ? 2.297   5.247   -5.775  1.00 17.75 ? 489 HOH B O   1 
HETATM 9129 O  O   . HOH T 5 .   ? -21.568 10.355  3.437   1.00 28.51 ? 490 HOH B O   1 
HETATM 9130 O  O   . HOH T 5 .   ? 11.415  14.625  -0.064  1.00 24.99 ? 491 HOH B O   1 
HETATM 9131 O  O   . HOH T 5 .   ? -25.472 -7.104  13.215  1.00 28.18 ? 492 HOH B O   1 
HETATM 9132 O  O   . HOH T 5 .   ? -13.647 -6.703  -11.253 1.00 20.67 ? 493 HOH B O   1 
HETATM 9133 O  O   . HOH T 5 .   ? -1.020  16.051  -8.602  1.00 25.31 ? 494 HOH B O   1 
HETATM 9134 O  O   . HOH T 5 .   ? 7.196   -11.200 24.203  1.00 29.97 ? 495 HOH B O   1 
HETATM 9135 O  O   . HOH T 5 .   ? 5.951   -2.417  1.627   1.00 30.10 ? 496 HOH B O   1 
HETATM 9136 O  O   . HOH T 5 .   ? -14.077 -15.051 28.241  1.00 22.31 ? 497 HOH B O   1 
HETATM 9137 O  O   . HOH T 5 .   ? -19.555 -13.488 14.588  1.00 20.89 ? 498 HOH B O   1 
HETATM 9138 O  O   . HOH T 5 .   ? -5.475  -16.976 -10.720 1.00 25.41 ? 499 HOH B O   1 
HETATM 9139 O  O   . HOH T 5 .   ? -26.191 -9.505  6.468   1.00 33.28 ? 500 HOH B O   1 
HETATM 9140 O  O   . HOH T 5 .   ? 1.781   -16.104 4.984   1.00 41.91 ? 501 HOH B O   1 
HETATM 9141 O  O   . HOH T 5 .   ? -21.699 1.436   18.724  1.00 35.98 ? 502 HOH B O   1 
HETATM 9142 O  O   . HOH T 5 .   ? -9.566  16.851  -16.127 1.00 22.32 ? 503 HOH B O   1 
HETATM 9143 O  O   . HOH T 5 .   ? -14.879 -14.523 -2.411  1.00 18.66 ? 504 HOH B O   1 
HETATM 9144 O  O   . HOH T 5 .   ? -1.217  14.633  17.201  1.00 27.70 ? 505 HOH B O   1 
HETATM 9145 O  O   . HOH T 5 .   ? -21.732 -6.353  -9.586  1.00 28.91 ? 506 HOH B O   1 
HETATM 9146 O  O   . HOH T 5 .   ? -4.232  -12.884 25.920  1.00 29.43 ? 507 HOH B O   1 
HETATM 9147 O  O   . HOH T 5 .   ? 0.973   18.282  -13.929 1.00 24.51 ? 508 HOH B O   1 
HETATM 9148 O  O   . HOH T 5 .   ? -12.372 -0.332  22.894  1.00 27.11 ? 509 HOH B O   1 
HETATM 9149 O  O   . HOH T 5 .   ? -29.445 2.441   5.850   1.00 25.11 ? 510 HOH B O   1 
HETATM 9150 O  O   . HOH T 5 .   ? -19.545 -0.772  -16.121 1.00 27.78 ? 511 HOH B O   1 
HETATM 9151 O  O   . HOH T 5 .   ? -26.812 -7.010  -1.280  1.00 25.74 ? 512 HOH B O   1 
HETATM 9152 O  O   . HOH T 5 .   ? -31.055 2.242   2.114   1.00 26.25 ? 513 HOH B O   1 
HETATM 9153 O  O   . HOH T 5 .   ? -29.842 -2.951  7.367   1.00 24.66 ? 514 HOH B O   1 
HETATM 9154 O  O   . HOH T 5 .   ? -15.016 5.892   26.090  1.00 32.09 ? 515 HOH B O   1 
HETATM 9155 O  O   . HOH T 5 .   ? -13.227 -14.289 30.785  1.00 23.97 ? 516 HOH B O   1 
HETATM 9156 O  O   . HOH T 5 .   ? -0.091  -13.868 8.783   1.00 29.33 ? 517 HOH B O   1 
HETATM 9157 O  O   . HOH T 5 .   ? 5.316   16.242  13.489  1.00 30.09 ? 518 HOH B O   1 
HETATM 9158 O  O   . HOH T 5 .   ? -27.247 -3.693  -5.682  1.00 26.57 ? 519 HOH B O   1 
HETATM 9159 O  O   . HOH T 5 .   ? -26.797 9.184   -2.651  1.00 35.93 ? 520 HOH B O   1 
HETATM 9160 O  O   . HOH T 5 .   ? -31.648 5.373   -7.513  1.00 26.42 ? 521 HOH B O   1 
HETATM 9161 O  O   . HOH T 5 .   ? -4.971  14.430  -4.528  1.00 33.62 ? 522 HOH B O   1 
HETATM 9162 O  O   . HOH T 5 .   ? -24.737 -1.086  -11.244 1.00 22.52 ? 523 HOH B O   1 
HETATM 9163 O  O   . HOH T 5 .   ? 2.742   -13.282 15.899  1.00 21.39 ? 524 HOH B O   1 
HETATM 9164 O  O   . HOH T 5 .   ? -12.818 -9.037  -12.514 1.00 25.73 ? 525 HOH B O   1 
HETATM 9165 O  O   . HOH T 5 .   ? -14.327 -10.918 23.838  1.00 30.82 ? 526 HOH B O   1 
HETATM 9166 O  O   . HOH T 5 .   ? -10.738 17.560  -8.163  1.00 24.81 ? 527 HOH B O   1 
HETATM 9167 O  O   . HOH T 5 .   ? 4.083   -2.149  -3.191  1.00 29.20 ? 528 HOH B O   1 
HETATM 9168 O  O   . HOH T 5 .   ? -26.605 10.437  5.350   1.00 32.27 ? 529 HOH B O   1 
HETATM 9169 O  O   . HOH T 5 .   ? 7.761   1.424   19.833  1.00 27.44 ? 530 HOH B O   1 
HETATM 9170 O  O   . HOH T 5 .   ? -35.001 5.503   -4.962  1.00 28.93 ? 531 HOH B O   1 
HETATM 9171 O  O   . HOH T 5 .   ? -19.289 -16.046 15.540  1.00 29.24 ? 532 HOH B O   1 
HETATM 9172 O  O   . HOH T 5 .   ? -25.602 3.363   -10.999 1.00 27.60 ? 533 HOH B O   1 
HETATM 9173 O  O   . HOH T 5 .   ? -29.963 -4.472  -0.458  1.00 26.43 ? 534 HOH B O   1 
HETATM 9174 O  O   . HOH T 5 .   ? -16.844 -16.804 3.670   1.00 41.87 ? 535 HOH B O   1 
HETATM 9175 O  O   . HOH T 5 .   ? 4.708   -5.577  8.772   1.00 27.49 ? 536 HOH B O   1 
HETATM 9176 O  O   . HOH T 5 .   ? -32.458 -3.882  -1.747  1.00 29.01 ? 537 HOH B O   1 
HETATM 9177 O  O   . HOH T 5 .   ? -18.057 -4.071  26.529  1.00 34.34 ? 538 HOH B O   1 
HETATM 9178 O  O   . HOH T 5 .   ? -15.510 -14.648 3.500   1.00 28.50 ? 539 HOH B O   1 
HETATM 9179 O  O   . HOH T 5 .   ? -38.607 2.152   -5.842  1.00 23.86 ? 540 HOH B O   1 
HETATM 9180 O  O   . HOH T 5 .   ? -27.169 -9.899  2.007   1.00 26.61 ? 541 HOH B O   1 
HETATM 9181 O  O   . HOH T 5 .   ? -6.219  2.231   -16.874 1.00 27.20 ? 542 HOH B O   1 
HETATM 9182 O  O   . HOH T 5 .   ? 7.004   0.499   22.415  1.00 34.40 ? 543 HOH B O   1 
HETATM 9183 O  O   . HOH T 5 .   ? -14.570 -13.446 24.011  1.00 30.04 ? 544 HOH B O   1 
HETATM 9184 O  O   . HOH T 5 .   ? -16.504 -12.230 25.640  1.00 23.63 ? 545 HOH B O   1 
HETATM 9185 O  O   . HOH T 5 .   ? -23.542 -4.610  -9.890  1.00 29.61 ? 546 HOH B O   1 
HETATM 9186 O  O   . HOH T 5 .   ? -10.648 -10.450 29.794  1.00 21.43 ? 547 HOH B O   1 
HETATM 9187 O  O   . HOH T 5 .   ? 4.388   17.304  3.826   1.00 24.85 ? 548 HOH B O   1 
HETATM 9188 O  O   . HOH T 5 .   ? 5.504   -8.230  -1.368  1.00 28.39 ? 549 HOH B O   1 
HETATM 9189 O  O   . HOH T 5 .   ? -2.413  -10.658 -14.648 1.00 29.74 ? 550 HOH B O   1 
HETATM 9190 O  O   . HOH T 5 .   ? -20.160 -12.065 8.218   1.00 29.78 ? 551 HOH B O   1 
HETATM 9191 O  O   . HOH T 5 .   ? -1.578  20.618  8.569   1.00 32.03 ? 552 HOH B O   1 
HETATM 9192 O  O   . HOH T 5 .   ? 4.751   -9.701  -12.196 1.00 24.47 ? 553 HOH B O   1 
HETATM 9193 O  O   . HOH T 5 .   ? -29.153 10.011  -6.487  1.00 34.39 ? 554 HOH B O   1 
HETATM 9194 O  O   . HOH T 5 .   ? 7.080   -0.963  17.862  1.00 23.06 ? 555 HOH B O   1 
HETATM 9195 O  O   . HOH T 5 .   ? -24.184 -10.850 4.933   1.00 43.99 ? 556 HOH B O   1 
HETATM 9196 O  O   . HOH T 5 .   ? -1.578  -9.816  -10.271 1.00 30.64 ? 557 HOH B O   1 
HETATM 9197 O  O   . HOH T 5 .   ? 1.212   -0.374  -12.206 1.00 26.70 ? 558 HOH B O   1 
HETATM 9198 O  O   . HOH T 5 .   ? 7.001   -11.298 17.224  1.00 27.80 ? 559 HOH B O   1 
HETATM 9199 O  O   . HOH T 5 .   ? -1.404  14.272  -4.303  1.00 25.23 ? 560 HOH B O   1 
HETATM 9200 O  O   . HOH T 5 .   ? -18.617 -11.951 23.838  1.00 32.21 ? 561 HOH B O   1 
HETATM 9201 O  O   . HOH T 5 .   ? -29.636 8.887   6.176   1.00 43.10 ? 562 HOH B O   1 
HETATM 9202 O  O   . HOH T 5 .   ? -7.843  -20.688 16.724  1.00 39.31 ? 563 HOH B O   1 
HETATM 9203 O  O   . HOH T 5 .   ? -29.122 7.389   -1.404  1.00 29.06 ? 564 HOH B O   1 
HETATM 9204 O  O   . HOH T 5 .   ? 4.241   11.717  -13.108 1.00 38.61 ? 565 HOH B O   1 
HETATM 9205 O  O   . HOH T 5 .   ? -20.799 -0.508  -13.946 1.00 30.51 ? 566 HOH B O   1 
HETATM 9206 O  O   . HOH T 5 .   ? -14.631 -14.227 19.865  1.00 32.85 ? 567 HOH B O   1 
HETATM 9207 O  O   . HOH T 5 .   ? -32.770 -1.848  14.750  1.00 32.25 ? 568 HOH B O   1 
HETATM 9208 O  O   . HOH T 5 .   ? -15.274 -12.494 31.686  1.00 28.60 ? 569 HOH B O   1 
HETATM 9209 O  O   . HOH T 5 .   ? -26.984 -6.235  6.819   1.00 21.62 ? 570 HOH B O   1 
HETATM 9210 O  O   . HOH T 5 .   ? -16.888 11.091  4.502   1.00 31.90 ? 571 HOH B O   1 
HETATM 9211 O  O   . HOH T 5 .   ? -0.496  4.195   -16.683 1.00 31.74 ? 572 HOH B O   1 
HETATM 9212 O  O   . HOH T 5 .   ? 6.111   -6.049  14.641  1.00 20.51 ? 573 HOH B O   1 
HETATM 9213 O  O   . HOH T 5 .   ? 3.995   -9.190  2.948   1.00 24.11 ? 574 HOH B O   1 
HETATM 9214 O  O   . HOH T 5 .   ? 1.424   13.141  19.597  1.00 29.47 ? 575 HOH B O   1 
HETATM 9215 O  O   . HOH T 5 .   ? 4.009   15.012  1.727   1.00 30.66 ? 576 HOH B O   1 
HETATM 9216 O  O   . HOH T 5 .   ? 8.969   3.246   20.339  1.00 29.73 ? 577 HOH B O   1 
HETATM 9217 O  O   . HOH T 5 .   ? -31.906 -6.422  6.360   1.00 30.91 ? 578 HOH B O   1 
HETATM 9218 O  O   . HOH T 5 .   ? -33.513 2.632   2.920   1.00 33.80 ? 579 HOH B O   1 
HETATM 9219 O  O   . HOH T 5 .   ? -14.405 14.003  -16.151 1.00 29.54 ? 580 HOH B O   1 
HETATM 9220 O  O   . HOH T 5 .   ? -20.233 -12.155 -2.284  1.00 28.32 ? 581 HOH B O   1 
HETATM 9221 O  O   . HOH T 5 .   ? 3.450   5.575   16.469  1.00 37.49 ? 582 HOH B O   1 
HETATM 9222 O  O   . HOH T 5 .   ? -26.313 -3.065  -10.247 1.00 28.91 ? 583 HOH B O   1 
HETATM 9223 O  O   . HOH T 5 .   ? -0.850  -12.906 4.203   1.00 35.46 ? 584 HOH B O   1 
HETATM 9224 O  O   . HOH T 5 .   ? -0.509  -13.361 22.469  1.00 32.37 ? 585 HOH B O   1 
HETATM 9225 O  O   . HOH T 5 .   ? -27.660 3.579   -10.175 1.00 33.78 ? 586 HOH B O   1 
HETATM 9226 O  O   . HOH T 5 .   ? -5.924  -15.494 13.160  1.00 26.21 ? 587 HOH B O   1 
HETATM 9227 O  O   . HOH T 5 .   ? -2.973  -12.714 15.316  1.00 30.89 ? 588 HOH B O   1 
HETATM 9228 O  O   . HOH T 5 .   ? -20.965 -5.058  21.916  1.00 34.12 ? 589 HOH B O   1 
HETATM 9229 O  O   . HOH T 5 .   ? -10.983 -15.797 3.245   1.00 26.12 ? 590 HOH B O   1 
HETATM 9230 O  O   . HOH T 5 .   ? 5.236   12.438  -10.802 1.00 42.33 ? 591 HOH B O   1 
HETATM 9231 O  O   . HOH T 5 .   ? 6.311   14.734  -14.779 1.00 35.62 ? 592 HOH B O   1 
HETATM 9232 O  O   . HOH T 5 .   ? 0.569   6.494   -16.587 1.00 32.05 ? 593 HOH B O   1 
HETATM 9233 O  O   . HOH T 5 .   ? -27.403 -6.014  -4.514  1.00 30.77 ? 594 HOH B O   1 
HETATM 9234 O  O   . HOH T 5 .   ? -11.643 -8.065  -14.907 1.00 25.47 ? 595 HOH B O   1 
HETATM 9235 O  O   . HOH T 5 .   ? 1.923   -15.785 16.584  1.00 27.99 ? 596 HOH B O   1 
HETATM 9236 O  O   . HOH T 5 .   ? -10.577 -13.032 30.599  1.00 21.30 ? 597 HOH B O   1 
HETATM 9237 O  O   . HOH T 5 .   ? -17.649 -12.618 29.709  1.00 24.01 ? 598 HOH B O   1 
HETATM 9238 O  O   . HOH T 5 .   ? -17.687 -12.659 21.332  1.00 26.25 ? 599 HOH B O   1 
HETATM 9239 O  O   . HOH T 5 .   ? -36.501 3.941   -6.528  1.00 23.19 ? 600 HOH B O   1 
HETATM 9240 O  O   . HOH T 5 .   ? 7.237   -5.491  5.013   1.00 27.87 ? 601 HOH B O   1 
HETATM 9241 O  O   . HOH T 5 .   ? 7.605   -9.445  15.712  1.00 22.70 ? 602 HOH B O   1 
HETATM 9242 O  O   . HOH T 5 .   ? 3.868   15.001  -10.463 1.00 27.43 ? 603 HOH B O   1 
HETATM 9243 O  O   . HOH T 5 .   ? 5.543   9.899   -8.867  1.00 29.74 ? 604 HOH B O   1 
HETATM 9244 O  O   . HOH T 5 .   ? -29.640 7.125   1.336   1.00 30.32 ? 605 HOH B O   1 
HETATM 9245 O  O   . HOH T 5 .   ? -2.770  19.122  10.850  1.00 31.12 ? 606 HOH B O   1 
HETATM 9246 O  O   . HOH T 5 .   ? -3.852  -14.410 17.634  1.00 33.03 ? 607 HOH B O   1 
HETATM 9247 O  O   . HOH T 5 .   ? -4.079  1.830   24.314  1.00 37.27 ? 608 HOH B O   1 
HETATM 9248 O  O   . HOH T 5 .   ? 8.070   11.038  -7.536  1.00 32.72 ? 609 HOH B O   1 
HETATM 9249 O  O   . HOH T 5 .   ? -8.737  13.710  0.470   1.00 38.76 ? 610 HOH B O   1 
HETATM 9250 O  O   . HOH T 5 .   ? 8.891   6.729   -2.041  1.00 29.22 ? 611 HOH B O   1 
HETATM 9251 O  O   . HOH T 5 .   ? -24.752 8.378   1.104   1.00 23.47 ? 612 HOH B O   1 
HETATM 9252 O  O   . HOH T 5 .   ? -4.614  -13.684 9.606   1.00 28.79 ? 613 HOH B O   1 
HETATM 9253 O  O   . HOH T 5 .   ? -16.346 -5.917  -12.486 1.00 27.62 ? 614 HOH B O   1 
HETATM 9254 O  O   . HOH T 5 .   ? -9.530  7.705   19.861  1.00 35.10 ? 615 HOH B O   1 
HETATM 9255 O  O   . HOH T 5 .   ? -2.813  1.538   -14.448 1.00 28.95 ? 616 HOH B O   1 
HETATM 9256 O  O   . HOH T 5 .   ? -7.361  -7.459  28.367  1.00 31.37 ? 617 HOH B O   1 
HETATM 9257 O  O   . HOH T 5 .   ? 3.829   6.302   -9.937  1.00 24.47 ? 618 HOH B O   1 
HETATM 9258 O  O   . HOH T 5 .   ? -17.693 13.281  -4.099  1.00 32.71 ? 619 HOH B O   1 
HETATM 9259 O  O   . HOH T 5 .   ? -19.642 -15.976 10.336  1.00 29.04 ? 620 HOH B O   1 
HETATM 9260 O  O   . HOH T 5 .   ? -23.470 11.531  -1.186  1.00 23.99 ? 621 HOH B O   1 
HETATM 9261 O  O   . HOH T 5 .   ? 1.132   0.635   -16.078 1.00 27.89 ? 622 HOH B O   1 
HETATM 9262 O  O   . HOH T 5 .   ? -20.211 -7.574  -11.241 1.00 30.21 ? 623 HOH B O   1 
HETATM 9263 O  O   . HOH T 5 .   ? 3.230   1.134   -12.880 1.00 28.42 ? 624 HOH B O   1 
HETATM 9264 O  O   . HOH T 5 .   ? -11.016 16.893  -18.652 1.00 30.37 ? 625 HOH B O   1 
HETATM 9265 O  O   . HOH T 5 .   ? 7.884   -6.768  16.569  1.00 30.61 ? 626 HOH B O   1 
HETATM 9266 O  O   . HOH T 5 .   ? -0.751  18.223  0.996   1.00 35.34 ? 627 HOH B O   1 
HETATM 9267 O  O   . HOH T 5 .   ? 3.598   -16.174 18.270  1.00 29.41 ? 628 HOH B O   1 
HETATM 9268 O  O   . HOH T 5 .   ? -0.169  -13.049 -4.387  1.00 28.94 ? 629 HOH B O   1 
HETATM 9269 O  O   . HOH T 5 .   ? -5.837  11.359  20.708  1.00 28.54 ? 630 HOH B O   1 
HETATM 9270 O  O   . HOH T 5 .   ? 5.710   20.691  -5.578  1.00 32.67 ? 631 HOH B O   1 
HETATM 9271 O  O   . HOH T 5 .   ? -22.055 -2.560  -12.353 1.00 29.40 ? 632 HOH B O   1 
HETATM 9272 O  O   . HOH T 5 .   ? -3.267  15.386  18.482  1.00 33.10 ? 633 HOH B O   1 
HETATM 9273 O  O   . HOH T 5 .   ? -13.592 -3.106  27.022  1.00 37.71 ? 634 HOH B O   1 
HETATM 9274 O  O   . HOH T 5 .   ? -29.281 -6.610  -2.443  1.00 36.67 ? 635 HOH B O   1 
HETATM 9275 O  O   . HOH T 5 .   ? -8.618  14.843  -2.128  1.00 40.83 ? 636 HOH B O   1 
HETATM 9276 O  O   . HOH T 5 .   ? 2.019   6.709   23.179  1.00 37.78 ? 637 HOH B O   1 
HETATM 9277 O  O   . HOH T 5 .   ? -19.192 -16.324 -3.692  1.00 28.85 ? 638 HOH B O   1 
HETATM 9278 O  O   . HOH T 5 .   ? -28.437 -3.235  -7.986  1.00 31.55 ? 639 HOH B O   1 
HETATM 9279 O  O   . HOH T 5 .   ? -29.250 -7.528  6.662   1.00 30.76 ? 640 HOH B O   1 
HETATM 9280 O  O   . HOH T 5 .   ? 4.527   -11.897 24.773  1.00 37.89 ? 641 HOH B O   1 
HETATM 9281 O  O   . HOH T 5 .   ? 1.423   -15.291 23.062  1.00 33.25 ? 642 HOH B O   1 
HETATM 9282 O  O   . HOH T 5 .   ? -17.069 9.606   23.609  1.00 38.21 ? 643 HOH B O   1 
HETATM 9283 O  O   . HOH T 5 .   ? -6.569  -11.505 29.119  1.00 29.74 ? 644 HOH B O   1 
HETATM 9284 O  O   . HOH T 5 .   ? -3.666  16.214  -8.631  1.00 30.49 ? 645 HOH B O   1 
HETATM 9285 O  O   . HOH T 5 .   ? 4.337   -13.320 22.427  1.00 32.53 ? 646 HOH B O   1 
HETATM 9286 O  O   . HOH T 5 .   ? -10.782 15.948  -6.165  1.00 37.82 ? 647 HOH B O   1 
HETATM 9287 O  O   . HOH T 5 .   ? 2.545   -11.374 -11.801 1.00 37.51 ? 648 HOH B O   1 
HETATM 9288 O  O   . HOH T 5 .   ? -0.764  4.915   25.228  1.00 33.58 ? 649 HOH B O   1 
HETATM 9289 O  O   . HOH T 5 .   ? -22.485 12.220  -10.587 1.00 34.73 ? 650 HOH B O   1 
HETATM 9290 O  O   . HOH T 5 .   ? -19.479 15.816  0.687   1.00 31.01 ? 651 HOH B O   1 
HETATM 9291 O  O   . HOH T 5 .   ? -26.519 9.503   12.250  1.00 37.76 ? 652 HOH B O   1 
HETATM 9292 O  O   . HOH T 5 .   ? -22.966 6.382   -12.339 1.00 24.24 ? 653 HOH B O   1 
HETATM 9293 O  O   . HOH T 5 .   ? -21.233 3.746   -12.834 1.00 21.20 ? 654 HOH B O   1 
HETATM 9294 O  O   . HOH T 5 .   ? 6.280   16.827  0.966   1.00 30.73 ? 655 HOH B O   1 
HETATM 9295 O  O   . HOH T 5 .   ? 6.027   19.011  2.023   1.00 33.43 ? 656 HOH B O   1 
HETATM 9296 O  O   . HOH T 5 .   ? 1.356   22.768  10.028  1.00 28.38 ? 657 HOH B O   1 
HETATM 9297 O  O   . HOH T 5 .   ? -5.606  18.066  11.914  1.00 40.92 ? 658 HOH B O   1 
HETATM 9298 O  O   . HOH T 5 .   ? -8.857  17.122  10.893  1.00 33.20 ? 659 HOH B O   1 
HETATM 9299 O  O   . HOH T 5 .   ? -19.621 13.112  7.675   1.00 32.70 ? 660 HOH B O   1 
HETATM 9300 O  O   . HOH T 5 .   ? -12.189 12.581  0.209   1.00 27.92 ? 661 HOH B O   1 
HETATM 9301 O  O   . HOH T 5 .   ? -13.718 11.255  2.847   1.00 37.27 ? 662 HOH B O   1 
HETATM 9302 O  O   . HOH T 5 .   ? -17.292 11.434  1.898   1.00 37.57 ? 663 HOH B O   1 
HETATM 9303 O  O   . HOH T 5 .   ? -3.314  4.495   24.046  1.00 43.46 ? 664 HOH B O   1 
HETATM 9304 O  O   . HOH T 5 .   ? -4.818  -12.776 22.186  1.00 36.80 ? 665 HOH B O   1 
HETATM 9305 O  O   . HOH T 5 .   ? -1.856  -12.245 25.220  1.00 32.62 ? 666 HOH B O   1 
HETATM 9306 O  O   . HOH T 5 .   ? -2.138  -15.416 10.776  1.00 35.25 ? 667 HOH B O   1 
HETATM 9307 O  O   . HOH T 5 .   ? 4.075   -14.880 9.886   1.00 33.91 ? 668 HOH B O   1 
HETATM 9308 O  O   . HOH T 5 .   ? -20.414 -3.816  26.228  1.00 36.90 ? 669 HOH B O   1 
HETATM 9309 O  O   . HOH T 5 .   ? -24.289 -9.797  16.283  1.00 37.19 ? 670 HOH B O   1 
HETATM 9310 O  O   . HOH T 5 .   ? -23.122 -8.809  14.680  1.00 33.32 ? 671 HOH B O   1 
HETATM 9311 O  O   . HOH T 5 .   ? -20.264 -13.236 11.679  1.00 28.71 ? 672 HOH B O   1 
HETATM 9312 O  O   . HOH T 5 .   ? -16.615 -16.764 16.753  1.00 33.13 ? 673 HOH B O   1 
HETATM 9313 O  O   . HOH T 5 .   ? -12.182 -17.405 13.265  1.00 31.36 ? 674 HOH B O   1 
HETATM 9314 O  O   . HOH T 5 .   ? -13.129 -17.183 6.667   1.00 34.60 ? 675 HOH B O   1 
HETATM 9315 O  O   . HOH T 5 .   ? -24.193 0.876   20.983  1.00 38.26 ? 676 HOH B O   1 
HETATM 9316 O  O   . HOH T 5 .   ? -18.950 6.416   23.644  1.00 31.83 ? 677 HOH B O   1 
HETATM 9317 O  O   . HOH T 5 .   ? -22.177 -13.066 -9.535  1.00 37.41 ? 678 HOH B O   1 
HETATM 9318 O  O   . HOH T 5 .   ? -11.170 1.186   -16.320 1.00 33.41 ? 679 HOH B O   1 
HETATM 9319 O  O   . HOH T 5 .   ? -12.474 17.549  -11.176 1.00 38.01 ? 680 HOH B O   1 
HETATM 9320 O  O   . HOH T 5 .   ? -21.307 -9.799  10.118  1.00 33.38 ? 681 HOH B O   1 
HETATM 9321 O  O   . HOH T 5 .   ? -7.862  -1.366  29.177  1.00 40.52 ? 682 HOH B O   1 
HETATM 9322 O  O   . HOH T 5 .   ? -8.035  -6.342  -18.094 1.00 35.04 ? 683 HOH B O   1 
HETATM 9323 O  O   . HOH T 5 .   ? -12.292 -11.029 -15.522 1.00 39.94 ? 684 HOH B O   1 
HETATM 9324 O  O   . HOH T 5 .   ? -30.068 4.890   3.000   1.00 39.35 ? 685 HOH B O   1 
HETATM 9325 O  O   . HOH T 5 .   ? -31.812 8.680   -1.109  1.00 45.14 ? 686 HOH B O   1 
HETATM 9326 O  O   . HOH T 5 .   ? -20.969 -11.157 5.767   1.00 37.50 ? 687 HOH B O   1 
HETATM 9327 O  O   . HOH T 5 .   ? -27.415 8.970   1.366   1.00 36.95 ? 688 HOH B O   1 
HETATM 9328 O  O   . HOH T 5 .   ? -0.543  -12.877 15.644  1.00 37.48 ? 689 HOH B O   1 
HETATM 9329 O  O   . HOH T 5 .   ? -22.088 -13.217 18.115  1.00 38.02 ? 690 HOH B O   1 
HETATM 9330 O  O   . HOH U 5 .   ? 47.920  -8.775  -51.122 1.00 31.35 ? 401 HOH C O   1 
HETATM 9331 O  O   . HOH U 5 .   ? 32.728  11.164  -43.258 1.00 12.35 ? 402 HOH C O   1 
HETATM 9332 O  O   . HOH U 5 .   ? 26.040  12.863  -35.403 1.00 11.75 ? 403 HOH C O   1 
HETATM 9333 O  O   . HOH U 5 .   ? 32.166  2.388   -43.698 1.00 17.01 ? 404 HOH C O   1 
HETATM 9334 O  O   . HOH U 5 .   ? 25.409  -1.730  -40.636 1.00 12.43 ? 405 HOH C O   1 
HETATM 9335 O  O   . HOH U 5 .   ? 26.274  6.930   -41.161 1.00 11.79 ? 406 HOH C O   1 
HETATM 9336 O  O   . HOH U 5 .   ? 43.374  -2.571  -40.238 1.00 13.96 ? 407 HOH C O   1 
HETATM 9337 O  O   . HOH U 5 .   ? 23.811  5.609   -40.644 1.00 11.59 ? 408 HOH C O   1 
HETATM 9338 O  O   . HOH U 5 .   ? 23.574  4.673   -35.986 1.00 8.94  ? 409 HOH C O   1 
HETATM 9339 O  O   . HOH U 5 .   ? 26.967  9.364   -34.687 1.00 12.19 ? 410 HOH C O   1 
HETATM 9340 O  O   . HOH U 5 .   ? 34.362  15.849  -38.429 1.00 12.12 ? 411 HOH C O   1 
HETATM 9341 O  O   . HOH U 5 .   ? 23.598  -4.580  -35.995 1.00 18.65 ? 412 HOH C O   1 
HETATM 9342 O  O   . HOH U 5 .   ? 41.453  7.122   -46.576 1.00 22.12 ? 413 HOH C O   1 
HETATM 9343 O  O   . HOH U 5 .   ? 24.281  -0.718  -32.903 1.00 17.07 ? 414 HOH C O   1 
HETATM 9344 O  O   . HOH U 5 .   ? 27.266  -0.884  -32.187 1.00 10.71 ? 415 HOH C O   1 
HETATM 9345 O  O   . HOH U 5 .   ? 22.708  10.924  -29.297 1.00 17.36 ? 416 HOH C O   1 
HETATM 9346 O  O   . HOH U 5 .   ? 26.590  9.528   -41.919 1.00 14.97 ? 417 HOH C O   1 
HETATM 9347 O  O   . HOH U 5 .   ? 38.553  4.885   -45.242 1.00 16.95 ? 418 HOH C O   1 
HETATM 9348 O  O   . HOH U 5 .   ? 36.102  -1.272  -48.409 1.00 18.50 ? 419 HOH C O   1 
HETATM 9349 O  O   . HOH U 5 .   ? 32.811  4.938   -30.584 1.00 15.58 ? 420 HOH C O   1 
HETATM 9350 O  O   . HOH U 5 .   ? 25.226  6.493   -34.638 1.00 12.94 ? 421 HOH C O   1 
HETATM 9351 O  O   . HOH U 5 .   ? 33.850  1.621   -16.389 1.00 19.83 ? 422 HOH C O   1 
HETATM 9352 O  O   . HOH U 5 .   ? 21.145  -1.277  -29.927 1.00 22.50 ? 423 HOH C O   1 
HETATM 9353 O  O   . HOH U 5 .   ? 22.342  6.785   -32.221 1.00 11.21 ? 424 HOH C O   1 
HETATM 9354 O  O   . HOH U 5 .   ? 28.804  3.117   -43.477 1.00 13.90 ? 425 HOH C O   1 
HETATM 9355 O  O   . HOH U 5 .   ? 28.654  18.233  -31.703 1.00 15.31 ? 426 HOH C O   1 
HETATM 9356 O  O   . HOH U 5 .   ? 28.997  3.543   -46.246 1.00 20.19 ? 427 HOH C O   1 
HETATM 9357 O  O   . HOH U 5 .   ? 44.805  -14.228 -44.510 1.00 23.03 ? 428 HOH C O   1 
HETATM 9358 O  O   . HOH U 5 .   ? 37.632  -10.678 -33.219 1.00 18.82 ? 429 HOH C O   1 
HETATM 9359 O  O   . HOH U 5 .   ? 20.231  -10.101 -29.756 1.00 19.92 ? 430 HOH C O   1 
HETATM 9360 O  O   . HOH U 5 .   ? 41.646  14.719  -35.154 1.00 26.93 ? 431 HOH C O   1 
HETATM 9361 O  O   . HOH U 5 .   ? 29.419  5.903   -47.442 1.00 17.81 ? 432 HOH C O   1 
HETATM 9362 O  O   . HOH U 5 .   ? 29.695  -5.000  -22.062 1.00 17.78 ? 433 HOH C O   1 
HETATM 9363 O  O   . HOH U 5 .   ? 25.789  -3.217  -48.387 1.00 26.11 ? 434 HOH C O   1 
HETATM 9364 O  O   . HOH U 5 .   ? 25.527  8.129   -28.041 1.00 15.87 ? 435 HOH C O   1 
HETATM 9365 O  O   . HOH U 5 .   ? 24.250  13.057  -42.527 1.00 18.37 ? 436 HOH C O   1 
HETATM 9366 O  O   . HOH U 5 .   ? 47.309  8.978   -26.939 1.00 23.76 ? 437 HOH C O   1 
HETATM 9367 O  O   . HOH U 5 .   ? 46.162  -12.039 -40.444 1.00 24.32 ? 438 HOH C O   1 
HETATM 9368 O  O   . HOH U 5 .   ? 36.339  17.668  -38.379 1.00 21.55 ? 439 HOH C O   1 
HETATM 9369 O  O   . HOH U 5 .   ? 38.768  16.593  -38.853 1.00 21.78 ? 440 HOH C O   1 
HETATM 9370 O  O   . HOH U 5 .   ? 33.969  13.402  -44.246 1.00 19.58 ? 441 HOH C O   1 
HETATM 9371 O  O   . HOH U 5 .   ? 22.923  8.482   -27.929 1.00 19.89 ? 442 HOH C O   1 
HETATM 9372 O  O   . HOH U 5 .   ? 28.477  6.689   -44.035 1.00 21.04 ? 443 HOH C O   1 
HETATM 9373 O  O   . HOH U 5 .   ? 27.503  16.195  -41.227 1.00 16.52 ? 444 HOH C O   1 
HETATM 9374 O  O   . HOH U 5 .   ? 26.215  5.471   -24.354 1.00 20.86 ? 445 HOH C O   1 
HETATM 9375 O  O   . HOH U 5 .   ? 22.365  -6.262  -31.442 1.00 21.29 ? 446 HOH C O   1 
HETATM 9376 O  O   . HOH U 5 .   ? 45.384  -7.413  -45.295 1.00 21.55 ? 447 HOH C O   1 
HETATM 9377 O  O   . HOH U 5 .   ? 26.919  7.082   -47.728 1.00 31.33 ? 448 HOH C O   1 
HETATM 9378 O  O   . HOH U 5 .   ? 44.031  3.883   -44.219 1.00 21.24 ? 449 HOH C O   1 
HETATM 9379 O  O   . HOH U 5 .   ? 22.308  -7.565  -27.449 1.00 23.40 ? 450 HOH C O   1 
HETATM 9380 O  O   . HOH U 5 .   ? 22.356  -0.434  -44.205 1.00 23.51 ? 451 HOH C O   1 
HETATM 9381 O  O   . HOH U 5 .   ? 22.384  -8.901  -39.808 1.00 22.69 ? 452 HOH C O   1 
HETATM 9382 O  O   . HOH U 5 .   ? 42.089  -10.498 -56.445 1.00 21.52 ? 453 HOH C O   1 
HETATM 9383 O  O   . HOH U 5 .   ? 40.366  -14.274 -36.240 1.00 21.49 ? 454 HOH C O   1 
HETATM 9384 O  O   . HOH U 5 .   ? 38.259  21.184  -17.087 1.00 24.51 ? 455 HOH C O   1 
HETATM 9385 O  O   . HOH U 5 .   ? 27.915  -10.672 -22.463 1.00 23.72 ? 456 HOH C O   1 
HETATM 9386 O  O   . HOH U 5 .   ? 51.611  -2.748  -43.472 1.00 26.35 ? 457 HOH C O   1 
HETATM 9387 O  O   . HOH U 5 .   ? 26.440  -13.633 -34.555 1.00 24.45 ? 458 HOH C O   1 
HETATM 9388 O  O   . HOH U 5 .   ? 33.412  -1.680  -48.933 1.00 20.28 ? 459 HOH C O   1 
HETATM 9389 O  O   . HOH U 5 .   ? 53.557  5.864   -23.224 1.00 23.92 ? 460 HOH C O   1 
HETATM 9390 O  O   . HOH U 5 .   ? 56.975  -8.281  -23.213 1.00 35.27 ? 461 HOH C O   1 
HETATM 9391 O  O   . HOH U 5 .   ? 27.127  -10.372 -26.705 1.00 24.82 ? 462 HOH C O   1 
HETATM 9392 O  O   . HOH U 5 .   ? 33.471  11.986  -10.982 1.00 27.20 ? 463 HOH C O   1 
HETATM 9393 O  O   . HOH U 5 .   ? 32.682  -13.634 -36.936 1.00 22.34 ? 464 HOH C O   1 
HETATM 9394 O  O   . HOH U 5 .   ? 32.333  -2.076  -51.891 1.00 30.34 ? 465 HOH C O   1 
HETATM 9395 O  O   . HOH U 5 .   ? 44.260  14.498  -34.895 1.00 32.38 ? 466 HOH C O   1 
HETATM 9396 O  O   . HOH U 5 .   ? 31.475  2.370   -14.448 1.00 24.98 ? 467 HOH C O   1 
HETATM 9397 O  O   . HOH U 5 .   ? 22.963  1.757   -18.900 1.00 29.00 ? 468 HOH C O   1 
HETATM 9398 O  O   . HOH U 5 .   ? 53.330  -13.380 -29.621 1.00 34.31 ? 469 HOH C O   1 
HETATM 9399 O  O   . HOH U 5 .   ? 46.954  -13.207 -53.100 1.00 24.66 ? 470 HOH C O   1 
HETATM 9400 O  O   . HOH U 5 .   ? 24.425  -3.666  -44.556 1.00 23.06 ? 471 HOH C O   1 
HETATM 9401 O  O   . HOH U 5 .   ? 59.377  -7.926  -20.888 1.00 37.25 ? 472 HOH C O   1 
HETATM 9402 O  O   . HOH U 5 .   ? 39.231  13.738  -42.852 1.00 24.39 ? 473 HOH C O   1 
HETATM 9403 O  O   . HOH U 5 .   ? 39.962  17.870  -40.848 1.00 23.96 ? 474 HOH C O   1 
HETATM 9404 O  O   . HOH U 5 .   ? 51.405  6.948   -28.207 1.00 24.83 ? 475 HOH C O   1 
HETATM 9405 O  O   . HOH U 5 .   ? 26.295  5.489   -43.377 1.00 18.91 ? 476 HOH C O   1 
HETATM 9406 O  O   . HOH U 5 .   ? 38.916  -19.895 -46.339 1.00 33.38 ? 477 HOH C O   1 
HETATM 9407 O  O   . HOH U 5 .   ? 56.209  12.046  -42.448 1.00 41.05 ? 478 HOH C O   1 
HETATM 9408 O  O   . HOH U 5 .   ? 31.704  18.127  -28.190 1.00 27.35 ? 479 HOH C O   1 
HETATM 9409 O  O   . HOH U 5 .   ? 26.062  -3.498  -42.508 1.00 18.21 ? 480 HOH C O   1 
HETATM 9410 O  O   . HOH U 5 .   ? 40.273  -16.673 -30.111 1.00 27.50 ? 481 HOH C O   1 
HETATM 9411 O  O   . HOH U 5 .   ? 29.329  -13.932 -28.134 1.00 27.79 ? 482 HOH C O   1 
HETATM 9412 O  O   . HOH U 5 .   ? 19.695  -7.842  -17.629 1.00 26.78 ? 483 HOH C O   1 
HETATM 9413 O  O   . HOH U 5 .   ? 29.492  -12.541 -23.819 1.00 22.09 ? 484 HOH C O   1 
HETATM 9414 O  O   . HOH U 5 .   ? 22.741  0.005   -28.022 1.00 25.32 ? 485 HOH C O   1 
HETATM 9415 O  O   . HOH U 5 .   ? 46.471  -17.376 -38.289 1.00 30.43 ? 486 HOH C O   1 
HETATM 9416 O  O   . HOH U 5 .   ? 29.431  -11.857 -26.589 1.00 22.03 ? 487 HOH C O   1 
HETATM 9417 O  O   . HOH U 5 .   ? 20.604  17.835  -29.943 1.00 26.58 ? 488 HOH C O   1 
HETATM 9418 O  O   . HOH U 5 .   ? 43.519  -13.241 -25.870 1.00 31.98 ? 489 HOH C O   1 
HETATM 9419 O  O   . HOH U 5 .   ? 58.603  -1.865  -29.459 1.00 36.49 ? 490 HOH C O   1 
HETATM 9420 O  O   . HOH U 5 .   ? 40.879  13.062  -36.775 1.00 26.34 ? 491 HOH C O   1 
HETATM 9421 O  O   . HOH U 5 .   ? 42.459  -4.112  -48.286 1.00 24.57 ? 492 HOH C O   1 
HETATM 9422 O  O   . HOH U 5 .   ? 24.513  -12.927 -41.511 1.00 26.25 ? 493 HOH C O   1 
HETATM 9423 O  O   . HOH U 5 .   ? 47.929  -13.311 -39.186 1.00 31.89 ? 494 HOH C O   1 
HETATM 9424 O  O   . HOH U 5 .   ? 46.610  -2.158  -47.630 1.00 42.76 ? 495 HOH C O   1 
HETATM 9425 O  O   . HOH U 5 .   ? 20.649  -1.978  -50.725 1.00 29.31 ? 496 HOH C O   1 
HETATM 9426 O  O   . HOH U 5 .   ? 50.009  -4.794  -15.907 1.00 39.45 ? 497 HOH C O   1 
HETATM 9427 O  O   . HOH U 5 .   ? 22.528  -5.269  -41.204 1.00 26.88 ? 498 HOH C O   1 
HETATM 9428 O  O   . HOH U 5 .   ? 47.130  -14.813 -31.985 1.00 32.02 ? 499 HOH C O   1 
HETATM 9429 O  O   . HOH U 5 .   ? 26.522  3.219   -47.338 1.00 29.36 ? 500 HOH C O   1 
HETATM 9430 O  O   . HOH U 5 .   ? 23.015  -11.535 -44.483 1.00 30.32 ? 501 HOH C O   1 
HETATM 9431 O  O   . HOH U 5 .   ? 39.987  -11.885 -55.059 1.00 26.92 ? 502 HOH C O   1 
HETATM 9432 O  O   . HOH U 5 .   ? 48.039  -11.024 -15.524 1.00 30.05 ? 503 HOH C O   1 
HETATM 9433 O  O   . HOH U 5 .   ? 47.308  7.088   -22.624 1.00 25.20 ? 504 HOH C O   1 
HETATM 9434 O  O   . HOH U 5 .   ? 25.033  -2.014  -23.764 1.00 24.36 ? 505 HOH C O   1 
HETATM 9435 O  O   . HOH U 5 .   ? 63.677  -1.832  -22.357 1.00 43.56 ? 506 HOH C O   1 
HETATM 9436 O  O   . HOH U 5 .   ? 41.657  -8.201  -54.780 1.00 23.47 ? 507 HOH C O   1 
HETATM 9437 O  O   . HOH U 5 .   ? 28.609  -7.882  -17.147 1.00 27.03 ? 508 HOH C O   1 
HETATM 9438 O  O   . HOH U 5 .   ? 54.940  -5.565  -17.096 1.00 32.32 ? 509 HOH C O   1 
HETATM 9439 O  O   . HOH U 5 .   ? 22.118  -4.073  -38.213 1.00 27.69 ? 510 HOH C O   1 
HETATM 9440 O  O   . HOH U 5 .   ? 19.888  1.036   -51.416 1.00 30.42 ? 511 HOH C O   1 
HETATM 9441 O  O   . HOH U 5 .   ? 50.775  -4.559  -54.135 1.00 29.45 ? 512 HOH C O   1 
HETATM 9442 O  O   . HOH U 5 .   ? 51.771  9.385   -33.014 1.00 32.59 ? 513 HOH C O   1 
HETATM 9443 O  O   . HOH U 5 .   ? 26.356  11.353  -45.698 1.00 26.20 ? 514 HOH C O   1 
HETATM 9444 O  O   . HOH U 5 .   ? 26.303  -8.343  -15.934 1.00 29.78 ? 515 HOH C O   1 
HETATM 9445 O  O   . HOH U 5 .   ? 41.865  6.741   -10.389 1.00 30.23 ? 516 HOH C O   1 
HETATM 9446 O  O   . HOH U 5 .   ? 56.584  8.714   -39.788 1.00 33.35 ? 517 HOH C O   1 
HETATM 9447 O  O   . HOH U 5 .   ? 23.789  -9.049  -29.025 1.00 33.07 ? 518 HOH C O   1 
HETATM 9448 O  O   . HOH U 5 .   ? 47.141  8.079   -29.781 1.00 30.32 ? 519 HOH C O   1 
HETATM 9449 O  O   . HOH U 5 .   ? 56.659  7.093   -37.129 1.00 28.74 ? 520 HOH C O   1 
HETATM 9450 O  O   . HOH U 5 .   ? 37.874  16.686  -43.173 1.00 39.41 ? 521 HOH C O   1 
HETATM 9451 O  O   . HOH U 5 .   ? 23.712  3.744   -51.262 1.00 38.48 ? 522 HOH C O   1 
HETATM 9452 O  O   . HOH U 5 .   ? 48.270  18.783  -40.622 1.00 36.35 ? 523 HOH C O   1 
HETATM 9453 O  O   . HOH U 5 .   ? 47.746  -13.234 -15.825 1.00 37.22 ? 524 HOH C O   1 
HETATM 9454 O  O   . HOH U 5 .   ? 37.596  16.999  -30.390 1.00 31.43 ? 525 HOH C O   1 
HETATM 9455 O  O   . HOH U 5 .   ? 27.806  7.182   -19.157 1.00 31.81 ? 526 HOH C O   1 
HETATM 9456 O  O   . HOH U 5 .   ? 39.835  14.125  -12.397 1.00 34.87 ? 527 HOH C O   1 
HETATM 9457 O  O   . HOH U 5 .   ? 21.206  -0.829  -21.406 1.00 32.16 ? 528 HOH C O   1 
HETATM 9458 O  O   . HOH U 5 .   ? 40.385  -15.174 -56.347 1.00 30.87 ? 529 HOH C O   1 
HETATM 9459 O  O   . HOH U 5 .   ? 31.828  10.010  -23.095 1.00 28.63 ? 530 HOH C O   1 
HETATM 9460 O  O   . HOH U 5 .   ? 50.543  -13.241 -16.211 1.00 35.18 ? 531 HOH C O   1 
HETATM 9461 O  O   . HOH U 5 .   ? 23.200  -4.092  -47.969 1.00 33.21 ? 532 HOH C O   1 
HETATM 9462 O  O   . HOH U 5 .   ? 52.254  12.694  -47.209 1.00 32.59 ? 533 HOH C O   1 
HETATM 9463 O  O   . HOH U 5 .   ? 64.867  -5.722  -20.017 1.00 38.41 ? 534 HOH C O   1 
HETATM 9464 O  O   . HOH U 5 .   ? 32.440  7.438   -21.947 1.00 28.94 ? 535 HOH C O   1 
HETATM 9465 O  O   . HOH U 5 .   ? 33.029  12.659  -8.134  1.00 34.76 ? 536 HOH C O   1 
HETATM 9466 O  O   . HOH U 5 .   ? 58.116  -7.598  -30.827 1.00 32.17 ? 537 HOH C O   1 
HETATM 9467 O  O   . HOH U 5 .   ? 41.365  4.389   -45.521 1.00 28.78 ? 538 HOH C O   1 
HETATM 9468 O  O   . HOH U 5 .   ? 53.599  -4.228  -45.912 1.00 36.43 ? 539 HOH C O   1 
HETATM 9469 O  O   . HOH U 5 .   ? 61.890  -7.265  -16.727 1.00 32.61 ? 540 HOH C O   1 
HETATM 9470 O  O   . HOH U 5 .   ? 31.803  12.632  -46.555 1.00 26.16 ? 541 HOH C O   1 
HETATM 9471 O  O   . HOH U 5 .   ? 59.438  3.616   -34.414 1.00 37.88 ? 542 HOH C O   1 
HETATM 9472 O  O   . HOH U 5 .   ? 27.391  -12.629 -30.028 1.00 32.82 ? 543 HOH C O   1 
HETATM 9473 O  O   . HOH U 5 .   ? 24.061  5.402   -22.938 1.00 30.61 ? 544 HOH C O   1 
HETATM 9474 O  O   . HOH U 5 .   ? 34.328  11.852  -47.728 1.00 23.88 ? 545 HOH C O   1 
HETATM 9475 O  O   . HOH U 5 .   ? 40.028  -17.574 -22.744 1.00 31.85 ? 546 HOH C O   1 
HETATM 9476 O  O   . HOH U 5 .   ? 36.120  13.376  -46.052 1.00 28.06 ? 547 HOH C O   1 
HETATM 9477 O  O   . HOH U 5 .   ? 34.761  9.153   -47.946 1.00 32.41 ? 548 HOH C O   1 
HETATM 9478 O  O   . HOH U 5 .   ? 37.966  12.384  -30.092 1.00 23.03 ? 549 HOH C O   1 
HETATM 9479 O  O   . HOH U 5 .   ? 40.322  16.048  -32.580 1.00 29.62 ? 550 HOH C O   1 
HETATM 9480 O  O   . HOH U 5 .   ? 40.592  16.915  -36.755 1.00 30.56 ? 551 HOH C O   1 
HETATM 9481 O  O   . HOH U 5 .   ? 46.682  8.072   -11.376 1.00 24.79 ? 552 HOH C O   1 
HETATM 9482 O  O   . HOH U 5 .   ? 49.972  6.707   -11.572 1.00 25.88 ? 553 HOH C O   1 
HETATM 9483 O  O   . HOH U 5 .   ? 53.575  -10.236 -22.223 1.00 31.16 ? 554 HOH C O   1 
HETATM 9484 O  O   . HOH U 5 .   ? 22.249  -13.923 -35.235 1.00 38.89 ? 555 HOH C O   1 
HETATM 9485 O  O   . HOH U 5 .   ? 45.632  16.529  -38.410 1.00 29.85 ? 556 HOH C O   1 
HETATM 9486 O  O   . HOH U 5 .   ? 46.319  -15.721 -47.916 1.00 41.39 ? 557 HOH C O   1 
HETATM 9487 O  O   . HOH U 5 .   ? 34.676  -8.058  -11.011 1.00 33.41 ? 558 HOH C O   1 
HETATM 9488 O  O   . HOH U 5 .   ? 34.662  -19.930 -43.842 1.00 29.49 ? 559 HOH C O   1 
HETATM 9489 O  O   . HOH U 5 .   ? 46.611  11.288  -12.799 1.00 30.07 ? 560 HOH C O   1 
HETATM 9490 O  O   . HOH U 5 .   ? 28.156  -15.234 -35.647 1.00 33.13 ? 561 HOH C O   1 
HETATM 9491 O  O   . HOH U 5 .   ? 27.838  2.507   -52.249 1.00 34.79 ? 562 HOH C O   1 
HETATM 9492 O  O   . HOH U 5 .   ? 33.787  8.148   -50.154 1.00 31.73 ? 563 HOH C O   1 
HETATM 9493 O  O   . HOH U 5 .   ? 54.350  4.953   -25.836 1.00 31.12 ? 564 HOH C O   1 
HETATM 9494 O  O   . HOH U 5 .   ? 53.968  6.869   -27.550 1.00 26.41 ? 565 HOH C O   1 
HETATM 9495 O  O   . HOH U 5 .   ? 58.858  -9.268  -34.560 1.00 48.74 ? 566 HOH C O   1 
HETATM 9496 O  O   . HOH U 5 .   ? 48.320  -16.388 -39.814 1.00 33.32 ? 567 HOH C O   1 
HETATM 9497 O  O   . HOH U 5 .   ? 42.723  -5.902  -54.301 1.00 26.79 ? 568 HOH C O   1 
HETATM 9498 O  O   . HOH U 5 .   ? 35.398  16.946  -41.731 1.00 29.67 ? 569 HOH C O   1 
HETATM 9499 O  O   . HOH U 5 .   ? 49.184  -11.270 -52.524 1.00 26.22 ? 570 HOH C O   1 
HETATM 9500 O  O   . HOH U 5 .   ? 22.478  -8.278  -17.454 1.00 33.73 ? 571 HOH C O   1 
HETATM 9501 O  O   . HOH U 5 .   ? 52.696  17.289  -41.894 1.00 39.52 ? 572 HOH C O   1 
HETATM 9502 O  O   . HOH U 5 .   ? 37.611  8.667   -47.552 1.00 27.11 ? 573 HOH C O   1 
HETATM 9503 O  O   . HOH U 5 .   ? 41.797  -3.961  -11.132 1.00 36.38 ? 574 HOH C O   1 
HETATM 9504 O  O   . HOH U 5 .   ? 40.055  -8.203  -13.547 1.00 33.73 ? 575 HOH C O   1 
HETATM 9505 O  O   . HOH U 5 .   ? 36.450  -1.858  -53.015 1.00 41.78 ? 576 HOH C O   1 
HETATM 9506 O  O   . HOH U 5 .   ? 31.217  -16.726 -30.927 1.00 36.37 ? 577 HOH C O   1 
HETATM 9507 O  O   . HOH U 5 .   ? 30.012  5.699   -49.932 1.00 29.42 ? 578 HOH C O   1 
HETATM 9508 O  O   . HOH U 5 .   ? 44.605  -15.037 -50.404 1.00 27.32 ? 579 HOH C O   1 
HETATM 9509 O  O   . HOH U 5 .   ? 35.969  1.270   -50.176 1.00 37.38 ? 580 HOH C O   1 
HETATM 9510 O  O   . HOH U 5 .   ? 27.274  -13.771 -31.913 1.00 32.03 ? 581 HOH C O   1 
HETATM 9511 O  O   . HOH U 5 .   ? 47.346  -6.639  -52.755 1.00 41.38 ? 582 HOH C O   1 
HETATM 9512 O  O   . HOH U 5 .   ? 52.192  -5.288  -18.067 1.00 41.94 ? 583 HOH C O   1 
HETATM 9513 O  O   . HOH U 5 .   ? 19.952  -11.169 -27.429 1.00 30.02 ? 584 HOH C O   1 
HETATM 9514 O  O   . HOH U 5 .   ? 26.423  7.212   -13.927 1.00 33.84 ? 585 HOH C O   1 
HETATM 9515 O  O   . HOH U 5 .   ? 35.601  19.667  -40.473 1.00 42.85 ? 586 HOH C O   1 
HETATM 9516 O  O   . HOH U 5 .   ? 28.389  -12.875 -41.101 1.00 38.07 ? 587 HOH C O   1 
HETATM 9517 O  O   . HOH U 5 .   ? 30.898  -15.100 -35.644 1.00 31.14 ? 588 HOH C O   1 
HETATM 9518 O  O   . HOH U 5 .   ? 28.072  -10.502 -51.260 1.00 37.44 ? 589 HOH C O   1 
HETATM 9519 O  O   . HOH U 5 .   ? 45.074  -16.545 -45.860 1.00 34.13 ? 590 HOH C O   1 
HETATM 9520 O  O   . HOH U 5 .   ? 41.267  -18.208 -43.753 1.00 38.95 ? 591 HOH C O   1 
HETATM 9521 O  O   . HOH U 5 .   ? 55.643  -8.439  -32.341 1.00 25.33 ? 592 HOH C O   1 
HETATM 9522 O  O   . HOH U 5 .   ? 47.981  -14.741 -34.312 1.00 43.35 ? 593 HOH C O   1 
HETATM 9523 O  O   . HOH U 5 .   ? 61.520  -6.195  -19.633 1.00 41.88 ? 594 HOH C O   1 
HETATM 9524 O  O   . HOH U 5 .   ? 59.341  2.565   -30.501 1.00 28.30 ? 595 HOH C O   1 
HETATM 9525 O  O   . HOH U 5 .   ? 47.278  0.275   -47.120 1.00 40.59 ? 596 HOH C O   1 
HETATM 9526 O  O   . HOH U 5 .   ? 22.191  -1.059  -23.669 1.00 31.89 ? 597 HOH C O   1 
HETATM 9527 O  O   . HOH U 5 .   ? 58.825  5.495   -40.323 1.00 37.89 ? 598 HOH C O   1 
HETATM 9528 O  O   . HOH U 5 .   ? 51.073  15.577  -43.953 1.00 39.07 ? 599 HOH C O   1 
HETATM 9529 O  O   . HOH U 5 .   ? 40.267  -16.206 -25.426 1.00 33.69 ? 600 HOH C O   1 
HETATM 9530 O  O   . HOH U 5 .   ? 42.456  -1.386  -11.063 1.00 40.65 ? 601 HOH C O   1 
HETATM 9531 O  O   . HOH U 5 .   ? 51.413  8.844   -14.902 1.00 31.91 ? 602 HOH C O   1 
HETATM 9532 O  O   . HOH U 5 .   ? 33.819  -18.524 -30.596 1.00 39.94 ? 603 HOH C O   1 
HETATM 9533 O  O   . HOH U 5 .   ? 29.915  6.793   -21.047 1.00 33.70 ? 604 HOH C O   1 
HETATM 9534 O  O   . HOH U 5 .   ? 26.084  4.202   -49.942 1.00 40.49 ? 605 HOH C O   1 
HETATM 9535 O  O   . HOH U 5 .   ? 32.899  0.670   -50.939 1.00 39.18 ? 606 HOH C O   1 
HETATM 9536 O  O   . HOH U 5 .   ? 55.822  5.269   -22.318 1.00 30.94 ? 607 HOH C O   1 
HETATM 9537 O  O   . HOH U 5 .   ? 53.391  -15.688 -26.295 1.00 32.32 ? 608 HOH C O   1 
HETATM 9538 O  O   . HOH U 5 .   ? 54.822  1.002   -14.697 1.00 34.80 ? 609 HOH C O   1 
HETATM 9539 O  O   . HOH U 5 .   ? 59.877  -2.884  -25.633 1.00 35.44 ? 610 HOH C O   1 
HETATM 9540 O  O   . HOH U 5 .   ? 24.252  -2.854  -27.652 1.00 36.53 ? 611 HOH C O   1 
HETATM 9541 O  O   . HOH U 5 .   ? 50.707  -13.401 -19.192 1.00 46.52 ? 612 HOH C O   1 
HETATM 9542 O  O   . HOH V 5 .   ? -15.265 -4.920  -35.985 1.00 36.11 ? 401 HOH D O   1 
HETATM 9543 O  O   . HOH V 5 .   ? 21.006  13.535  -35.671 1.00 12.21 ? 402 HOH D O   1 
HETATM 9544 O  O   . HOH V 5 .   ? 1.236   -9.907  -31.122 1.00 14.29 ? 403 HOH D O   1 
HETATM 9545 O  O   . HOH V 5 .   ? 21.575  6.642   -29.711 1.00 12.33 ? 404 HOH D O   1 
HETATM 9546 O  O   . HOH V 5 .   ? 16.542  0.261   -37.448 1.00 10.07 ? 405 HOH D O   1 
HETATM 9547 O  O   . HOH V 5 .   ? 8.827   -10.778 -31.176 1.00 16.16 ? 406 HOH D O   1 
HETATM 9548 O  O   . HOH V 5 .   ? 20.371  7.336   -35.741 1.00 12.42 ? 407 HOH D O   1 
HETATM 9549 O  O   . HOH V 5 .   ? 13.723  18.507  -32.350 1.00 13.38 ? 408 HOH D O   1 
HETATM 9550 O  O   . HOH V 5 .   ? 6.583   -14.059 -50.841 1.00 12.65 ? 409 HOH D O   1 
HETATM 9551 O  O   . HOH V 5 .   ? 19.247  10.034  -35.747 1.00 11.68 ? 410 HOH D O   1 
HETATM 9552 O  O   . HOH V 5 .   ? 4.376   -6.914  -34.766 1.00 10.79 ? 411 HOH D O   1 
HETATM 9553 O  O   . HOH V 5 .   ? 18.626  -0.321  -29.419 1.00 14.11 ? 412 HOH D O   1 
HETATM 9554 O  O   . HOH V 5 .   ? 12.154  6.998   -39.286 1.00 12.41 ? 413 HOH D O   1 
HETATM 9555 O  O   . HOH V 5 .   ? 2.694   9.367   -24.756 1.00 17.37 ? 414 HOH D O   1 
HETATM 9556 O  O   . HOH V 5 .   ? 1.180   2.580   -28.132 1.00 12.08 ? 415 HOH D O   1 
HETATM 9557 O  O   . HOH V 5 .   ? 23.054  6.300   -38.195 1.00 10.52 ? 416 HOH D O   1 
HETATM 9558 O  O   . HOH V 5 .   ? -7.250  -7.081  -51.322 1.00 20.95 ? 417 HOH D O   1 
HETATM 9559 O  O   . HOH V 5 .   ? 0.465   -12.699 -36.861 1.00 18.48 ? 418 HOH D O   1 
HETATM 9560 O  O   . HOH V 5 .   ? 20.666  4.081   -46.801 1.00 23.24 ? 419 HOH D O   1 
HETATM 9561 O  O   . HOH V 5 .   ? -8.339  -0.251  -51.475 1.00 15.90 ? 420 HOH D O   1 
HETATM 9562 O  O   . HOH V 5 .   ? 5.808   -6.472  -57.411 1.00 15.02 ? 421 HOH D O   1 
HETATM 9563 O  O   . HOH V 5 .   ? 11.908  8.741   -47.358 1.00 13.55 ? 422 HOH D O   1 
HETATM 9564 O  O   . HOH V 5 .   ? -2.537  -8.764  -41.600 1.00 17.42 ? 423 HOH D O   1 
HETATM 9565 O  O   . HOH V 5 .   ? -12.764 -1.692  -33.937 1.00 15.88 ? 424 HOH D O   1 
HETATM 9566 O  O   . HOH V 5 .   ? 11.929  -3.661  -47.195 1.00 13.01 ? 425 HOH D O   1 
HETATM 9567 O  O   . HOH V 5 .   ? 15.677  9.677   -47.935 1.00 16.95 ? 426 HOH D O   1 
HETATM 9568 O  O   . HOH V 5 .   ? 13.911  7.449   -48.444 1.00 14.56 ? 427 HOH D O   1 
HETATM 9569 O  O   . HOH V 5 .   ? 19.163  -0.364  -36.781 1.00 15.06 ? 428 HOH D O   1 
HETATM 9570 O  O   . HOH V 5 .   ? 17.495  -6.642  -56.153 1.00 26.33 ? 429 HOH D O   1 
HETATM 9571 O  O   . HOH V 5 .   ? 12.090  -7.091  -52.058 1.00 22.73 ? 430 HOH D O   1 
HETATM 9572 O  O   . HOH V 5 .   ? -10.372 11.665  -25.937 1.00 16.90 ? 431 HOH D O   1 
HETATM 9573 O  O   . HOH V 5 .   ? 24.089  8.921   -35.024 1.00 14.04 ? 432 HOH D O   1 
HETATM 9574 O  O   . HOH V 5 .   ? 14.746  13.863  -27.158 1.00 18.26 ? 433 HOH D O   1 
HETATM 9575 O  O   . HOH V 5 .   ? -9.977  -0.547  -49.282 1.00 17.68 ? 434 HOH D O   1 
HETATM 9576 O  O   . HOH V 5 .   ? 21.546  5.132   -34.232 1.00 9.26  ? 435 HOH D O   1 
HETATM 9577 O  O   . HOH V 5 .   ? 19.076  11.607  -50.130 1.00 18.96 ? 436 HOH D O   1 
HETATM 9578 O  O   . HOH V 5 .   ? 7.033   -8.488  -58.884 1.00 23.13 ? 437 HOH D O   1 
HETATM 9579 O  O   . HOH V 5 .   ? -15.171 -2.398  -43.383 1.00 23.59 ? 438 HOH D O   1 
HETATM 9580 O  O   . HOH V 5 .   ? 20.052  8.030   -42.411 1.00 12.03 ? 439 HOH D O   1 
HETATM 9581 O  O   . HOH V 5 .   ? 20.009  11.048  -29.037 1.00 16.56 ? 440 HOH D O   1 
HETATM 9582 O  O   . HOH V 5 .   ? 19.511  8.400   -29.240 1.00 14.18 ? 441 HOH D O   1 
HETATM 9583 O  O   . HOH V 5 .   ? -0.292  -12.851 -45.209 1.00 14.54 ? 442 HOH D O   1 
HETATM 9584 O  O   . HOH V 5 .   ? 10.756  13.084  -58.781 1.00 19.78 ? 443 HOH D O   1 
HETATM 9585 O  O   . HOH V 5 .   ? -2.853  11.161  -46.164 1.00 18.58 ? 444 HOH D O   1 
HETATM 9586 O  O   . HOH V 5 .   ? -7.795  12.085  -36.796 1.00 19.26 ? 445 HOH D O   1 
HETATM 9587 O  O   . HOH V 5 .   ? 18.576  5.161   -45.639 1.00 15.45 ? 446 HOH D O   1 
HETATM 9588 O  O   . HOH V 5 .   ? -15.157 -0.489  -35.473 1.00 16.85 ? 447 HOH D O   1 
HETATM 9589 O  O   . HOH V 5 .   ? -20.623 4.263   -41.702 1.00 21.15 ? 448 HOH D O   1 
HETATM 9590 O  O   . HOH V 5 .   ? 23.998  18.439  -42.775 1.00 20.89 ? 449 HOH D O   1 
HETATM 9591 O  O   . HOH V 5 .   ? 9.163   3.195   -52.953 1.00 13.17 ? 450 HOH D O   1 
HETATM 9592 O  O   . HOH V 5 .   ? -6.734  11.105  -19.563 1.00 13.88 ? 451 HOH D O   1 
HETATM 9593 O  O   . HOH V 5 .   ? -2.197  -7.868  -22.558 1.00 16.66 ? 452 HOH D O   1 
HETATM 9594 O  O   . HOH V 5 .   ? 17.272  7.480   -55.747 1.00 25.49 ? 453 HOH D O   1 
HETATM 9595 O  O   . HOH V 5 .   ? -9.723  8.480   -20.640 1.00 21.05 ? 454 HOH D O   1 
HETATM 9596 O  O   . HOH V 5 .   ? 10.895  -14.105 -52.586 1.00 23.11 ? 455 HOH D O   1 
HETATM 9597 O  O   . HOH V 5 .   ? 10.435  2.322   -21.330 1.00 18.53 ? 456 HOH D O   1 
HETATM 9598 O  O   . HOH V 5 .   ? -2.942  -12.428 -45.196 1.00 21.62 ? 457 HOH D O   1 
HETATM 9599 O  O   . HOH V 5 .   ? 11.388  3.561   -55.117 1.00 13.80 ? 458 HOH D O   1 
HETATM 9600 O  O   . HOH V 5 .   ? 23.549  10.552  -41.645 1.00 19.56 ? 459 HOH D O   1 
HETATM 9601 O  O   . HOH V 5 .   ? 8.076   8.945   -24.306 1.00 16.52 ? 460 HOH D O   1 
HETATM 9602 O  O   . HOH V 5 .   ? 12.185  20.878  -32.321 1.00 19.38 ? 461 HOH D O   1 
HETATM 9603 O  O   . HOH V 5 .   ? 3.180   -6.694  -57.977 1.00 23.01 ? 462 HOH D O   1 
HETATM 9604 O  O   . HOH V 5 .   ? -0.002  -0.051  -56.826 1.00 20.26 ? 463 HOH D O   1 
HETATM 9605 O  O   . HOH V 5 .   ? 12.704  -9.725  -46.042 1.00 17.06 ? 464 HOH D O   1 
HETATM 9606 O  O   . HOH V 5 .   ? -15.505 7.633   -55.536 1.00 22.54 ? 465 HOH D O   1 
HETATM 9607 O  O   . HOH V 5 .   ? 2.206   -11.856 -54.245 1.00 17.81 ? 466 HOH D O   1 
HETATM 9608 O  O   . HOH V 5 .   ? 20.603  14.072  -47.862 1.00 21.50 ? 467 HOH D O   1 
HETATM 9609 O  O   . HOH V 5 .   ? 12.277  1.824   -17.915 1.00 21.38 ? 468 HOH D O   1 
HETATM 9610 O  O   . HOH V 5 .   ? 19.212  4.631   -49.304 1.00 19.10 ? 469 HOH D O   1 
HETATM 9611 O  O   . HOH V 5 .   ? -3.313  -5.522  -26.757 1.00 20.40 ? 470 HOH D O   1 
HETATM 9612 O  O   . HOH V 5 .   ? 16.622  10.509  -50.385 1.00 17.34 ? 471 HOH D O   1 
HETATM 9613 O  O   . HOH V 5 .   ? -6.944  0.115   -55.749 1.00 23.01 ? 472 HOH D O   1 
HETATM 9614 O  O   . HOH V 5 .   ? -5.640  -6.902  -27.663 1.00 20.34 ? 473 HOH D O   1 
HETATM 9615 O  O   . HOH V 5 .   ? -12.240 -4.883  -44.220 1.00 23.04 ? 474 HOH D O   1 
HETATM 9616 O  O   . HOH V 5 .   ? 9.430   20.139  -31.664 1.00 18.46 ? 475 HOH D O   1 
HETATM 9617 O  O   . HOH V 5 .   ? -5.747  -5.961  -53.747 1.00 26.24 ? 476 HOH D O   1 
HETATM 9618 O  O   . HOH V 5 .   ? -3.126  -9.742  -21.021 1.00 23.85 ? 477 HOH D O   1 
HETATM 9619 O  O   . HOH V 5 .   ? -3.891  -8.527  -18.492 1.00 22.00 ? 478 HOH D O   1 
HETATM 9620 O  O   . HOH V 5 .   ? -1.801  -8.865  -16.580 1.00 20.97 ? 479 HOH D O   1 
HETATM 9621 O  O   . HOH V 5 .   ? 10.736  -10.416 -16.911 1.00 23.00 ? 480 HOH D O   1 
HETATM 9622 O  O   . HOH V 5 .   ? 18.137  7.442   -27.086 1.00 19.01 ? 481 HOH D O   1 
HETATM 9623 O  O   . HOH V 5 .   ? -2.877  -10.515 -39.319 1.00 20.89 ? 482 HOH D O   1 
HETATM 9624 O  O   . HOH V 5 .   ? -2.141  11.572  -20.206 1.00 21.22 ? 483 HOH D O   1 
HETATM 9625 O  O   . HOH V 5 .   ? 13.095  11.260  -46.769 1.00 16.84 ? 484 HOH D O   1 
HETATM 9626 O  O   . HOH V 5 .   ? -6.103  23.426  -32.049 1.00 20.52 ? 485 HOH D O   1 
HETATM 9627 O  O   . HOH V 5 .   ? 11.800  -10.088 -57.953 1.00 22.92 ? 486 HOH D O   1 
HETATM 9628 O  O   . HOH V 5 .   ? 0.767   -7.974  -18.811 1.00 20.96 ? 487 HOH D O   1 
HETATM 9629 O  O   . HOH V 5 .   ? -13.784 -1.317  -49.071 1.00 24.55 ? 488 HOH D O   1 
HETATM 9630 O  O   . HOH V 5 .   ? 11.049  17.437  -54.673 1.00 24.38 ? 489 HOH D O   1 
HETATM 9631 O  O   . HOH V 5 .   ? 11.250  -10.516 -43.677 1.00 23.35 ? 490 HOH D O   1 
HETATM 9632 O  O   . HOH V 5 .   ? 16.518  15.840  -54.663 1.00 21.57 ? 491 HOH D O   1 
HETATM 9633 O  O   . HOH V 5 .   ? 20.816  -1.022  -41.895 1.00 29.68 ? 492 HOH D O   1 
HETATM 9634 O  O   . HOH V 5 .   ? -0.143  -10.184 -18.145 1.00 29.36 ? 493 HOH D O   1 
HETATM 9635 O  O   . HOH V 5 .   ? -2.564  13.507  -56.724 1.00 24.04 ? 494 HOH D O   1 
HETATM 9636 O  O   . HOH V 5 .   ? -15.809 9.511   -47.205 1.00 25.73 ? 495 HOH D O   1 
HETATM 9637 O  O   . HOH V 5 .   ? 16.724  8.021   -51.460 1.00 22.75 ? 496 HOH D O   1 
HETATM 9638 O  O   . HOH V 5 .   ? 14.282  19.820  -42.734 1.00 32.76 ? 497 HOH D O   1 
HETATM 9639 O  O   . HOH V 5 .   ? 14.577  -12.080 -34.357 1.00 27.96 ? 498 HOH D O   1 
HETATM 9640 O  O   . HOH V 5 .   ? 20.407  21.587  -32.636 1.00 28.25 ? 499 HOH D O   1 
HETATM 9641 O  O   . HOH V 5 .   ? 8.804   15.396  -40.060 1.00 20.74 ? 500 HOH D O   1 
HETATM 9642 O  O   . HOH V 5 .   ? -5.864  -10.306 -39.654 1.00 37.16 ? 501 HOH D O   1 
HETATM 9643 O  O   . HOH V 5 .   ? -4.988  -11.163 -28.172 1.00 21.58 ? 502 HOH D O   1 
HETATM 9644 O  O   . HOH V 5 .   ? -2.607  -0.476  -16.628 1.00 25.52 ? 503 HOH D O   1 
HETATM 9645 O  O   . HOH V 5 .   ? 14.277  16.300  -26.280 1.00 22.11 ? 504 HOH D O   1 
HETATM 9646 O  O   . HOH V 5 .   ? -12.480 -7.884  -40.834 1.00 25.74 ? 505 HOH D O   1 
HETATM 9647 O  O   . HOH V 5 .   ? -2.607  -14.661 -39.372 1.00 35.74 ? 506 HOH D O   1 
HETATM 9648 O  O   . HOH V 5 .   ? -12.191 8.661   -30.131 1.00 26.44 ? 507 HOH D O   1 
HETATM 9649 O  O   . HOH V 5 .   ? -6.111  5.160   -56.299 1.00 24.71 ? 508 HOH D O   1 
HETATM 9650 O  O   . HOH V 5 .   ? -12.119 10.188  -23.206 1.00 22.40 ? 509 HOH D O   1 
HETATM 9651 O  O   . HOH V 5 .   ? 22.400  3.283   -23.438 1.00 20.96 ? 510 HOH D O   1 
HETATM 9652 O  O   . HOH V 5 .   ? -10.631 -4.566  -29.239 1.00 25.21 ? 511 HOH D O   1 
HETATM 9653 O  O   . HOH V 5 .   ? 13.656  1.100   -55.776 1.00 25.76 ? 512 HOH D O   1 
HETATM 9654 O  O   . HOH V 5 .   ? -8.213  8.338   -55.821 1.00 27.48 ? 513 HOH D O   1 
HETATM 9655 O  O   . HOH V 5 .   ? 17.265  6.489   -49.077 1.00 20.48 ? 514 HOH D O   1 
HETATM 9656 O  O   . HOH V 5 .   ? -16.233 4.309   -40.873 1.00 22.06 ? 515 HOH D O   1 
HETATM 9657 O  O   . HOH V 5 .   ? 2.242   -15.257 -29.592 1.00 27.91 ? 516 HOH D O   1 
HETATM 9658 O  O   . HOH V 5 .   ? -20.475 5.754   -50.748 1.00 23.18 ? 517 HOH D O   1 
HETATM 9659 O  O   . HOH V 5 .   ? 22.693  -1.790  -39.820 1.00 21.42 ? 518 HOH D O   1 
HETATM 9660 O  O   . HOH V 5 .   ? 3.999   19.409  -22.325 1.00 24.92 ? 519 HOH D O   1 
HETATM 9661 O  O   . HOH V 5 .   ? -9.063  11.094  -45.145 1.00 19.70 ? 520 HOH D O   1 
HETATM 9662 O  O   . HOH V 5 .   ? -14.539 4.794   -37.058 1.00 25.58 ? 521 HOH D O   1 
HETATM 9663 O  O   . HOH V 5 .   ? 18.595  -7.691  -40.148 1.00 21.41 ? 522 HOH D O   1 
HETATM 9664 O  O   . HOH V 5 .   ? 19.589  18.828  -40.239 1.00 24.05 ? 523 HOH D O   1 
HETATM 9665 O  O   . HOH V 5 .   ? 20.607  -7.730  -29.618 1.00 22.71 ? 524 HOH D O   1 
HETATM 9666 O  O   . HOH V 5 .   ? 12.771  13.205  -48.652 1.00 19.78 ? 525 HOH D O   1 
HETATM 9667 O  O   . HOH V 5 .   ? -6.781  -9.207  -26.767 1.00 25.95 ? 526 HOH D O   1 
HETATM 9668 O  O   . HOH V 5 .   ? -0.144  -12.223 -42.101 1.00 19.32 ? 527 HOH D O   1 
HETATM 9669 O  O   . HOH V 5 .   ? 18.872  -3.375  -42.981 1.00 22.90 ? 528 HOH D O   1 
HETATM 9670 O  O   . HOH V 5 .   ? 1.385   8.828   -59.348 1.00 22.21 ? 529 HOH D O   1 
HETATM 9671 O  O   . HOH V 5 .   ? -12.651 -4.431  -47.454 1.00 31.08 ? 530 HOH D O   1 
HETATM 9672 O  O   . HOH V 5 .   ? 17.182  -11.665 -27.386 1.00 23.65 ? 531 HOH D O   1 
HETATM 9673 O  O   . HOH V 5 .   ? 4.635   15.786  -57.445 1.00 21.79 ? 532 HOH D O   1 
HETATM 9674 O  O   . HOH V 5 .   ? 14.306  2.561   -16.477 1.00 29.18 ? 533 HOH D O   1 
HETATM 9675 O  O   . HOH V 5 .   ? 8.995   -10.138 -58.048 1.00 20.39 ? 534 HOH D O   1 
HETATM 9676 O  O   . HOH V 5 .   ? 8.937   21.703  -29.667 1.00 19.82 ? 535 HOH D O   1 
HETATM 9677 O  O   . HOH V 5 .   ? -3.998  10.072  -17.387 1.00 20.87 ? 536 HOH D O   1 
HETATM 9678 O  O   . HOH V 5 .   ? -9.962  15.338  -20.929 1.00 23.10 ? 537 HOH D O   1 
HETATM 9679 O  O   . HOH V 5 .   ? 4.377   -0.739  -14.500 1.00 31.59 ? 538 HOH D O   1 
HETATM 9680 O  O   . HOH V 5 .   ? -12.869 8.437   -55.187 1.00 27.92 ? 539 HOH D O   1 
HETATM 9681 O  O   . HOH V 5 .   ? 21.386  2.274   -21.127 1.00 24.37 ? 540 HOH D O   1 
HETATM 9682 O  O   . HOH V 5 .   ? 5.555   12.300  -22.932 1.00 19.91 ? 541 HOH D O   1 
HETATM 9683 O  O   . HOH V 5 .   ? 2.410   10.995  -61.836 1.00 39.65 ? 542 HOH D O   1 
HETATM 9684 O  O   . HOH V 5 .   ? 4.700   -16.549 -29.980 1.00 42.37 ? 543 HOH D O   1 
HETATM 9685 O  O   . HOH V 5 .   ? -7.813  3.488   -21.168 1.00 27.34 ? 544 HOH D O   1 
HETATM 9686 O  O   . HOH V 5 .   ? 12.641  19.830  -29.342 1.00 29.21 ? 545 HOH D O   1 
HETATM 9687 O  O   . HOH V 5 .   ? 26.225  15.998  -43.587 1.00 27.70 ? 546 HOH D O   1 
HETATM 9688 O  O   . HOH V 5 .   ? 8.915   17.716  -27.267 1.00 25.22 ? 547 HOH D O   1 
HETATM 9689 O  O   . HOH V 5 .   ? 1.571   7.813   -22.454 1.00 27.28 ? 548 HOH D O   1 
HETATM 9690 O  O   . HOH V 5 .   ? -7.137  -3.193  -53.122 1.00 27.64 ? 549 HOH D O   1 
HETATM 9691 O  O   . HOH V 5 .   ? -6.417  7.651   -57.410 1.00 26.94 ? 550 HOH D O   1 
HETATM 9692 O  O   . HOH V 5 .   ? -0.786  23.049  -34.039 1.00 32.70 ? 551 HOH D O   1 
HETATM 9693 O  O   . HOH V 5 .   ? -9.442  16.111  -28.457 1.00 25.31 ? 552 HOH D O   1 
HETATM 9694 O  O   . HOH V 5 .   ? 16.767  15.101  -23.813 1.00 25.25 ? 553 HOH D O   1 
HETATM 9695 O  O   . HOH V 5 .   ? 18.310  17.169  -41.728 1.00 27.08 ? 554 HOH D O   1 
HETATM 9696 O  O   . HOH V 5 .   ? -11.712 -2.626  -49.734 1.00 25.53 ? 555 HOH D O   1 
HETATM 9697 O  O   . HOH V 5 .   ? 18.853  -13.187 -33.337 1.00 32.78 ? 556 HOH D O   1 
HETATM 9698 O  O   . HOH V 5 .   ? -9.329  5.674   -21.600 1.00 37.16 ? 557 HOH D O   1 
HETATM 9699 O  O   . HOH V 5 .   ? -15.749 4.258   -51.007 1.00 38.34 ? 558 HOH D O   1 
HETATM 9700 O  O   . HOH V 5 .   ? 10.259  19.491  -40.327 1.00 38.40 ? 559 HOH D O   1 
HETATM 9701 O  O   . HOH V 5 .   ? 13.953  -11.339 -20.812 1.00 35.17 ? 560 HOH D O   1 
HETATM 9702 O  O   . HOH V 5 .   ? -6.085  4.427   -24.347 1.00 18.25 ? 561 HOH D O   1 
HETATM 9703 O  O   . HOH V 5 .   ? 21.126  20.624  -41.457 1.00 23.41 ? 562 HOH D O   1 
HETATM 9704 O  O   . HOH V 5 .   ? 13.560  22.393  -34.819 1.00 30.26 ? 563 HOH D O   1 
HETATM 9705 O  O   . HOH V 5 .   ? 2.675   -0.881  -57.437 1.00 28.11 ? 564 HOH D O   1 
HETATM 9706 O  O   . HOH V 5 .   ? 21.330  9.182   -25.832 1.00 27.30 ? 565 HOH D O   1 
HETATM 9707 O  O   . HOH V 5 .   ? -5.683  -10.931 -30.936 1.00 29.35 ? 566 HOH D O   1 
HETATM 9708 O  O   . HOH V 5 .   ? 23.711  8.307   -45.548 1.00 25.91 ? 567 HOH D O   1 
HETATM 9709 O  O   . HOH V 5 .   ? -2.688  16.757  -36.815 1.00 24.00 ? 568 HOH D O   1 
HETATM 9710 O  O   . HOH V 5 .   ? -5.268  -13.848 -32.392 1.00 27.69 ? 569 HOH D O   1 
HETATM 9711 O  O   . HOH V 5 .   ? 14.327  -8.375  -52.437 1.00 24.85 ? 570 HOH D O   1 
HETATM 9712 O  O   . HOH V 5 .   ? 5.353   9.364   -23.629 1.00 24.94 ? 571 HOH D O   1 
HETATM 9713 O  O   . HOH V 5 .   ? -4.607  14.771  -35.909 1.00 21.21 ? 572 HOH D O   1 
HETATM 9714 O  O   . HOH V 5 .   ? 18.990  -0.826  -46.290 1.00 26.43 ? 573 HOH D O   1 
HETATM 9715 O  O   . HOH V 5 .   ? -5.455  -10.250 -44.783 1.00 34.66 ? 574 HOH D O   1 
HETATM 9716 O  O   . HOH V 5 .   ? -2.996  22.475  -35.070 1.00 24.35 ? 575 HOH D O   1 
HETATM 9717 O  O   . HOH V 5 .   ? 4.198   17.771  -18.109 1.00 30.43 ? 576 HOH D O   1 
HETATM 9718 O  O   . HOH V 5 .   ? 11.339  15.483  -50.589 1.00 29.79 ? 577 HOH D O   1 
HETATM 9719 O  O   . HOH V 5 .   ? 22.588  7.978   -22.778 1.00 32.22 ? 578 HOH D O   1 
HETATM 9720 O  O   . HOH V 5 .   ? 4.336   13.190  -18.330 1.00 27.24 ? 579 HOH D O   1 
HETATM 9721 O  O   . HOH V 5 .   ? 12.256  17.073  -24.273 1.00 34.12 ? 580 HOH D O   1 
HETATM 9722 O  O   . HOH V 5 .   ? 0.580   -11.744 -13.927 1.00 30.43 ? 581 HOH D O   1 
HETATM 9723 O  O   . HOH V 5 .   ? 8.047   -12.383 -59.135 1.00 36.90 ? 582 HOH D O   1 
HETATM 9724 O  O   . HOH V 5 .   ? 5.830   2.428   -19.937 1.00 55.04 ? 583 HOH D O   1 
HETATM 9725 O  O   . HOH V 5 .   ? -14.263 9.650   -44.605 1.00 30.68 ? 584 HOH D O   1 
HETATM 9726 O  O   . HOH V 5 .   ? 6.512   17.090  -33.276 1.00 26.98 ? 585 HOH D O   1 
HETATM 9727 O  O   . HOH V 5 .   ? 19.486  -4.144  -34.203 1.00 21.71 ? 586 HOH D O   1 
HETATM 9728 O  O   . HOH V 5 .   ? 20.472  1.164   -45.567 1.00 27.27 ? 587 HOH D O   1 
HETATM 9729 O  O   . HOH V 5 .   ? -9.559  10.394  -42.265 1.00 24.77 ? 588 HOH D O   1 
HETATM 9730 O  O   . HOH V 5 .   ? 2.913   14.261  -43.493 1.00 28.08 ? 589 HOH D O   1 
HETATM 9731 O  O   . HOH V 5 .   ? 11.235  14.097  -61.250 1.00 31.47 ? 590 HOH D O   1 
HETATM 9732 O  O   . HOH V 5 .   ? 8.454   -9.053  -13.902 1.00 26.68 ? 591 HOH D O   1 
HETATM 9733 O  O   . HOH V 5 .   ? 7.687   -4.697  -14.434 1.00 29.53 ? 592 HOH D O   1 
HETATM 9734 O  O   . HOH V 5 .   ? 3.398   -13.930 -39.128 1.00 27.38 ? 593 HOH D O   1 
HETATM 9735 O  O   . HOH V 5 .   ? 21.770  0.636   -25.670 1.00 27.68 ? 594 HOH D O   1 
HETATM 9736 O  O   . HOH V 5 .   ? 9.727   -13.270 -55.490 1.00 32.41 ? 595 HOH D O   1 
HETATM 9737 O  O   . HOH V 5 .   ? -13.268 12.611  -32.260 1.00 33.83 ? 596 HOH D O   1 
HETATM 9738 O  O   . HOH V 5 .   ? -2.776  13.090  -41.054 1.00 33.51 ? 597 HOH D O   1 
HETATM 9739 O  O   . HOH V 5 .   ? -9.767  5.388   -55.352 1.00 32.77 ? 598 HOH D O   1 
HETATM 9740 O  O   . HOH V 5 .   ? -11.518 -7.368  -36.330 1.00 31.68 ? 599 HOH D O   1 
HETATM 9741 O  O   . HOH V 5 .   ? -10.036 14.854  -30.784 1.00 25.75 ? 600 HOH D O   1 
HETATM 9742 O  O   . HOH V 5 .   ? -5.405  -9.875  -34.539 1.00 30.54 ? 601 HOH D O   1 
HETATM 9743 O  O   . HOH V 5 .   ? 13.279  15.685  -47.804 1.00 24.71 ? 602 HOH D O   1 
HETATM 9744 O  O   . HOH V 5 .   ? 4.296   18.588  -51.363 1.00 31.51 ? 603 HOH D O   1 
HETATM 9745 O  O   . HOH V 5 .   ? 6.405   -0.527  -58.483 1.00 37.14 ? 604 HOH D O   1 
HETATM 9746 O  O   . HOH V 5 .   ? 6.534   -14.982 -30.946 1.00 41.08 ? 605 HOH D O   1 
HETATM 9747 O  O   . HOH V 5 .   ? 2.688   21.850  -31.692 1.00 31.33 ? 606 HOH D O   1 
HETATM 9748 O  O   . HOH V 5 .   ? 19.733  -5.672  -41.919 1.00 23.67 ? 607 HOH D O   1 
HETATM 9749 O  O   . HOH V 5 .   ? 3.521   -15.435 -21.757 1.00 40.06 ? 608 HOH D O   1 
HETATM 9750 O  O   . HOH V 5 .   ? 21.578  -9.694  -26.051 1.00 26.85 ? 609 HOH D O   1 
HETATM 9751 O  O   . HOH V 5 .   ? 2.815   18.528  -37.113 1.00 37.43 ? 610 HOH D O   1 
HETATM 9752 O  O   . HOH V 5 .   ? 20.355  -6.908  -44.398 1.00 32.92 ? 611 HOH D O   1 
HETATM 9753 O  O   . HOH V 5 .   ? -4.422  -14.103 -41.506 1.00 35.76 ? 612 HOH D O   1 
HETATM 9754 O  O   . HOH V 5 .   ? 11.527  -11.125 -27.531 1.00 29.41 ? 613 HOH D O   1 
HETATM 9755 O  O   . HOH V 5 .   ? -16.169 3.215   -38.321 1.00 28.93 ? 614 HOH D O   1 
HETATM 9756 O  O   . HOH V 5 .   ? 1.654   -14.559 -17.687 1.00 37.87 ? 615 HOH D O   1 
HETATM 9757 O  O   . HOH V 5 .   ? -1.191  -12.332 -39.104 1.00 27.24 ? 616 HOH D O   1 
HETATM 9758 O  O   . HOH V 5 .   ? -16.427 5.502   -53.894 1.00 23.76 ? 617 HOH D O   1 
HETATM 9759 O  O   . HOH V 5 .   ? 10.800  -12.795 -25.509 1.00 39.67 ? 618 HOH D O   1 
HETATM 9760 O  O   . HOH V 5 .   ? 7.150   -4.069  -58.239 1.00 30.07 ? 619 HOH D O   1 
HETATM 9761 O  O   . HOH V 5 .   ? 16.435  24.362  -34.058 1.00 26.35 ? 620 HOH D O   1 
HETATM 9762 O  O   . HOH V 5 .   ? 1.094   -10.134 -56.020 1.00 26.12 ? 621 HOH D O   1 
HETATM 9763 O  O   . HOH V 5 .   ? 9.918   -12.023 -33.424 1.00 33.12 ? 622 HOH D O   1 
HETATM 9764 O  O   . HOH V 5 .   ? -6.686  -9.332  -52.663 1.00 26.84 ? 623 HOH D O   1 
HETATM 9765 O  O   . HOH V 5 .   ? 12.057  5.945   -19.565 1.00 23.93 ? 624 HOH D O   1 
HETATM 9766 O  O   . HOH V 5 .   ? 22.687  7.551   -42.616 1.00 23.19 ? 625 HOH D O   1 
HETATM 9767 O  O   . HOH V 5 .   ? 1.901   -7.489  -55.596 1.00 29.47 ? 626 HOH D O   1 
HETATM 9768 O  O   . HOH V 5 .   ? 10.191  -10.808 -20.600 1.00 34.79 ? 627 HOH D O   1 
HETATM 9769 O  O   . HOH V 5 .   ? -8.222  19.391  -26.124 1.00 30.97 ? 628 HOH D O   1 
HETATM 9770 O  O   . HOH V 5 .   ? 2.202   13.478  -41.410 1.00 28.22 ? 629 HOH D O   1 
HETATM 9771 O  O   . HOH V 5 .   ? 7.647   20.872  -33.598 1.00 30.98 ? 630 HOH D O   1 
HETATM 9772 O  O   . HOH V 5 .   ? 21.182  18.591  -42.570 1.00 30.73 ? 631 HOH D O   1 
HETATM 9773 O  O   . HOH V 5 .   ? 2.848   1.652   -20.063 1.00 30.26 ? 632 HOH D O   1 
HETATM 9774 O  O   . HOH V 5 .   ? -2.275  -14.401 -25.915 1.00 30.25 ? 633 HOH D O   1 
HETATM 9775 O  O   . HOH V 5 .   ? 5.913   15.394  -43.262 1.00 35.65 ? 634 HOH D O   1 
HETATM 9776 O  O   . HOH V 5 .   ? -4.739  9.775   -57.359 1.00 31.40 ? 635 HOH D O   1 
HETATM 9777 O  O   . HOH V 5 .   ? 10.240  8.398   -19.392 1.00 25.90 ? 636 HOH D O   1 
HETATM 9778 O  O   . HOH V 5 .   ? 14.320  -11.717 -47.551 1.00 32.63 ? 637 HOH D O   1 
HETATM 9779 O  O   . HOH V 5 .   ? -11.312 13.070  -38.031 1.00 28.78 ? 638 HOH D O   1 
HETATM 9780 O  O   . HOH V 5 .   ? 15.455  -7.203  -17.802 1.00 36.59 ? 639 HOH D O   1 
HETATM 9781 O  O   . HOH V 5 .   ? -9.594  -11.830 -49.895 1.00 32.80 ? 640 HOH D O   1 
HETATM 9782 O  O   . HOH V 5 .   ? -1.483  12.849  -38.701 1.00 29.01 ? 641 HOH D O   1 
HETATM 9783 O  O   . HOH V 5 .   ? 3.332   19.710  -20.040 1.00 29.78 ? 642 HOH D O   1 
HETATM 9784 O  O   . HOH V 5 .   ? 17.930  15.991  -50.443 1.00 36.39 ? 643 HOH D O   1 
HETATM 9785 O  O   . HOH V 5 .   ? 18.464  -4.470  -18.131 1.00 33.71 ? 644 HOH D O   1 
HETATM 9786 O  O   . HOH V 5 .   ? 18.651  -0.515  -20.239 1.00 31.37 ? 645 HOH D O   1 
HETATM 9787 O  O   . HOH V 5 .   ? 16.710  2.362   -59.601 1.00 37.81 ? 646 HOH D O   1 
HETATM 9788 O  O   . HOH V 5 .   ? -9.628  0.471   -54.361 1.00 27.72 ? 647 HOH D O   1 
HETATM 9789 O  O   . HOH V 5 .   ? 1.025   24.159  -29.889 1.00 31.16 ? 648 HOH D O   1 
HETATM 9790 O  O   . HOH V 5 .   ? 20.748  11.600  -52.456 1.00 33.60 ? 649 HOH D O   1 
HETATM 9791 O  O   . HOH V 5 .   ? 14.025  -10.909 -27.335 1.00 37.42 ? 650 HOH D O   1 
HETATM 9792 O  O   . HOH V 5 .   ? 1.206   -15.293 -36.283 1.00 32.78 ? 651 HOH D O   1 
HETATM 9793 O  O   . HOH V 5 .   ? 16.403  19.539  -56.977 1.00 32.77 ? 652 HOH D O   1 
HETATM 9794 O  O   . HOH V 5 .   ? -5.526  19.577  -21.799 1.00 30.46 ? 653 HOH D O   1 
HETATM 9795 O  O   . HOH V 5 .   ? -1.387  15.530  -58.162 1.00 35.94 ? 654 HOH D O   1 
HETATM 9796 O  O   . HOH V 5 .   ? 15.301  9.946   -18.975 1.00 36.71 ? 655 HOH D O   1 
HETATM 9797 O  O   . HOH V 5 .   ? 12.360  13.202  -22.141 1.00 34.65 ? 656 HOH D O   1 
HETATM 9798 O  O   . HOH V 5 .   ? -11.216 12.350  -30.685 1.00 30.64 ? 657 HOH D O   1 
HETATM 9799 O  O   . HOH V 5 .   ? 18.792  7.644   -53.200 1.00 34.75 ? 658 HOH D O   1 
HETATM 9800 O  O   . HOH V 5 .   ? 11.088  -16.434 -21.000 1.00 37.86 ? 659 HOH D O   1 
HETATM 9801 O  O   . HOH V 5 .   ? 8.621   -13.706 -29.746 1.00 30.64 ? 660 HOH D O   1 
HETATM 9802 O  O   . HOH V 5 .   ? 0.144   -12.016 -22.778 1.00 35.75 ? 661 HOH D O   1 
HETATM 9803 O  O   . HOH V 5 .   ? 14.890  -12.747 -43.439 1.00 44.22 ? 662 HOH D O   1 
HETATM 9804 O  O   . HOH V 5 .   ? 1.636   -15.774 -39.513 1.00 32.75 ? 663 HOH D O   1 
HETATM 9805 O  O   . HOH V 5 .   ? 14.559  -13.385 -30.673 1.00 34.62 ? 664 HOH D O   1 
HETATM 9806 O  O   . HOH V 5 .   ? 4.056   17.182  -49.190 1.00 43.39 ? 665 HOH D O   1 
HETATM 9807 O  O   . HOH V 5 .   ? 9.462   17.251  -43.677 1.00 39.28 ? 666 HOH D O   1 
HETATM 9808 O  O   . HOH V 5 .   ? 9.023   21.033  -36.599 1.00 36.35 ? 667 HOH D O   1 
HETATM 9809 O  O   . HOH V 5 .   ? 6.699   -18.117 -25.085 1.00 46.36 ? 668 HOH D O   1 
HETATM 9810 O  O   . HOH V 5 .   ? 4.163   -14.474 -17.257 1.00 40.06 ? 669 HOH D O   1 
HETATM 9811 O  O   . HOH V 5 .   ? -0.514  15.448  -38.172 1.00 31.69 ? 670 HOH D O   1 
HETATM 9812 O  O   . HOH V 5 .   ? 10.055  2.475   -14.336 1.00 36.32 ? 671 HOH D O   1 
HETATM 9813 O  O   . HOH V 5 .   ? 10.742  3.820   -19.120 1.00 29.22 ? 672 HOH D O   1 
HETATM 9814 O  O   . HOH V 5 .   ? 22.699  -4.955  -26.774 1.00 33.18 ? 673 HOH D O   1 
HETATM 9815 O  O   . HOH V 5 .   ? 25.098  5.838   -46.131 1.00 39.16 ? 674 HOH D O   1 
HETATM 9816 O  O   . HOH V 5 .   ? -0.556  0.226   -18.147 1.00 34.48 ? 675 HOH D O   1 
HETATM 9817 O  O   . HOH V 5 .   ? -4.854  -11.254 -22.030 1.00 34.54 ? 676 HOH D O   1 
HETATM 9818 O  O   . HOH V 5 .   ? -4.518  -13.610 -26.756 1.00 38.42 ? 677 HOH D O   1 
HETATM 9819 O  O   . HOH V 5 .   ? 1.245   -17.361 -26.964 1.00 32.83 ? 678 HOH D O   1 
HETATM 9820 O  O   . HOH V 5 .   ? -18.521 -1.604  -44.981 1.00 36.15 ? 679 HOH D O   1 
HETATM 9821 O  O   . HOH V 5 .   ? -17.330 8.200   -50.070 1.00 29.74 ? 680 HOH D O   1 
HETATM 9822 O  O   . HOH V 5 .   ? -11.611 11.184  -46.036 1.00 34.09 ? 681 HOH D O   1 
HETATM 9823 O  O   . HOH V 5 .   ? -7.385  13.320  -54.038 1.00 42.98 ? 682 HOH D O   1 
HETATM 9824 O  O   . HOH V 5 .   ? 20.003  -1.120  -39.744 1.00 28.59 ? 683 HOH D O   1 
HETATM 9825 O  O   . HOH V 5 .   ? -8.428  -10.539 -41.791 1.00 35.06 ? 684 HOH D O   1 
HETATM 9826 O  O   . HOH V 5 .   ? -5.890  -9.917  -41.859 1.00 37.51 ? 685 HOH D O   1 
HETATM 9827 O  O   . HOH V 5 .   ? -6.260  -9.167  -37.465 1.00 32.00 ? 686 HOH D O   1 
HETATM 9828 O  O   . HOH V 5 .   ? -8.725  -4.256  -56.039 1.00 38.66 ? 687 HOH D O   1 
HETATM 9829 O  O   . HOH V 5 .   ? 11.294  17.866  -52.103 1.00 32.85 ? 688 HOH D O   1 
HETATM 9830 O  O   . HOH V 5 .   ? -1.597  -19.144 -36.965 1.00 49.37 ? 689 HOH D O   1 
HETATM 9831 O  O   . HOH V 5 .   ? 9.882   15.699  -48.142 1.00 38.26 ? 690 HOH D O   1 
HETATM 9832 O  O   . HOH V 5 .   ? -0.116  19.375  -21.645 1.00 35.43 ? 691 HOH D O   1 
HETATM 9833 O  O   . HOH V 5 .   ? 11.091  -0.623  -13.866 1.00 30.10 ? 692 HOH D O   1 
HETATM 9834 O  O   . HOH V 5 .   ? 8.199   4.043   -18.004 1.00 35.20 ? 693 HOH D O   1 
HETATM 9835 O  O   . HOH V 5 .   ? -0.979  23.977  -31.786 1.00 38.40 ? 694 HOH D O   1 
HETATM 9836 O  O   . HOH V 5 .   ? 3.111   -18.197 -39.787 1.00 32.76 ? 695 HOH D O   1 
HETATM 9837 O  O   . HOH V 5 .   ? 17.297  8.434   -19.814 1.00 38.43 ? 696 HOH D O   1 
HETATM 9838 O  O   . HOH V 5 .   ? 6.343   19.001  -34.959 1.00 30.00 ? 697 HOH D O   1 
# 
