data_4KP5
# 
_entry.id   4KP5 
# 
_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   4KP5         pdb_00004kp5 10.2210/pdb4kp5/pdb 
RCSB  RCSB079618   ?            ?                   
WWPDB D_1000079618 ?            ?                   
# 
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 2013-11-06 
2 'Structure model' 1 1 2018-05-16 
3 'Structure model' 1 2 2023-11-08 
4 'Structure model' 1 3 2024-11-06 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Data collection'        
2 2 'Structure model' '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_asym_id' 
9  3 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_atom_id' 
10 3 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_comp_id' 
11 3 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_seq_id'  
12 3 'Structure model' '_pdbx_struct_conn_angle.ptnr2_auth_asym_id'  
13 3 'Structure model' '_pdbx_struct_conn_angle.ptnr2_label_asym_id' 
14 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_auth_asym_id'  
15 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_auth_comp_id'  
16 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_auth_seq_id'   
17 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_asym_id' 
18 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_atom_id' 
19 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_comp_id' 
20 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_seq_id'  
21 3 'Structure model' '_pdbx_struct_conn_angle.value'               
22 3 'Structure model' '_struct_conn.pdbx_dist_value'                
23 3 'Structure model' '_struct_conn.ptnr1_auth_asym_id'             
24 3 'Structure model' '_struct_conn.ptnr1_auth_comp_id'             
25 3 'Structure model' '_struct_conn.ptnr1_auth_seq_id'              
26 3 'Structure model' '_struct_conn.ptnr1_label_asym_id'            
27 3 'Structure model' '_struct_conn.ptnr1_label_atom_id'            
28 3 'Structure model' '_struct_conn.ptnr1_label_comp_id'            
29 3 'Structure model' '_struct_conn.ptnr1_label_seq_id'             
30 3 'Structure model' '_struct_conn.ptnr2_auth_asym_id'             
31 3 'Structure model' '_struct_conn.ptnr2_auth_comp_id'             
32 3 'Structure model' '_struct_conn.ptnr2_auth_seq_id'              
33 3 'Structure model' '_struct_conn.ptnr2_label_asym_id'            
34 3 'Structure model' '_struct_conn.ptnr2_label_atom_id'            
35 3 'Structure model' '_struct_conn.ptnr2_label_comp_id'            
36 3 'Structure model' '_struct_ref_seq_dif.details'                 
37 3 'Structure model' '_struct_site.pdbx_auth_asym_id'              
38 3 'Structure model' '_struct_site.pdbx_auth_comp_id'              
39 3 'Structure model' '_struct_site.pdbx_auth_seq_id'               
# 
_pdbx_database_status.entry_id                        4KP5 
_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   2013-05-13 
_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 4KNI . unspecified 
PDB 4KNJ . unspecified 
PDB 4KNM . unspecified 
PDB 4KNN . unspecified 
PDB 4KP8 . unspecified 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Smirnov, A.'  1 
'Manakova, E.' 2 
'Grazulis, S.' 3 
# 
_citation.id                        primary 
_citation.title                     
'Benzenesulfonamides with pyrimidine moiety as inhibitors of human carbonic anhydrases I, II, VI, VII, XII, and XIII' 
_citation.journal_abbrev            Bioorg.Med.Chem. 
_citation.journal_volume            21 
_citation.page_first                6937 
_citation.page_last                 6947 
_citation.year                      2013 
_citation.journal_id_ASTM           BMECEP 
_citation.country                   UK 
_citation.journal_id_ISSN           0968-0896 
_citation.journal_id_CSD            1200 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   24103428 
_citation.pdbx_database_id_DOI      10.1016/j.bmc.2013.09.029 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Capkauskaite, E.'  1  ? 
primary 'Zubriene, A.'      2  ? 
primary 'Smirnov, A.'       3  ? 
primary 'Torresan, J.'      4  ? 
primary 'Kisonaite, M.'     5  ? 
primary 'Kazokaite, J.'     6  ? 
primary 'Gylyte, J.'        7  ? 
primary 'Michailoviene, V.' 8  ? 
primary 'Jogaite, V.'       9  ? 
primary 'Manakova, E.'      10 ? 
primary 'Grazulis, S.'      11 ? 
primary 'Tumkevicius, S.'   12 ? 
primary 'Matulis, D.'       13 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Carbonic anhydrase 12'                                         29917.318 4    4.2.1.1 ? 
'Catalytic domain, UNP residues 30-291' ? 
2 non-polymer syn 'ZINC ION'                                                      65.409    4    ?       ? ? ? 
3 non-polymer syn '2-chloro-4-[(pyrimidin-2-ylsulfanyl)acetyl]benzenesulfonamide' 343.809   4    ?       ? ? ? 
4 non-polymer syn 1,2-ETHANEDIOL                                                  62.068    6    ?       ? ? ? 
5 non-polymer syn 'SULFATE ION'                                                   96.063    1    ?       ? ? ? 
6 water       nat water                                                           18.015    1206 ?       ? ? ? 
# 
_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 '2-chloro-4-[(pyrimidin-2-ylsulfanyl)acetyl]benzenesulfonamide' E1F 
4 1,2-ETHANEDIOL                                                  EDO 
5 'SULFATE ION'                                                   SO4 
6 water                                                           HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   SER n 
1 3   LYS n 
1 4   TRP n 
1 5   THR n 
1 6   TYR n 
1 7   PHE n 
1 8   GLY n 
1 9   PRO n 
1 10  ASP n 
1 11  GLY n 
1 12  GLU n 
1 13  ASN n 
1 14  SER n 
1 15  TRP n 
1 16  SER n 
1 17  LYS n 
1 18  LYS n 
1 19  TYR n 
1 20  PRO n 
1 21  SER n 
1 22  CYS n 
1 23  GLY n 
1 24  GLY n 
1 25  LEU n 
1 26  LEU n 
1 27  GLN n 
1 28  SER n 
1 29  PRO n 
1 30  ILE n 
1 31  ASP n 
1 32  LEU n 
1 33  HIS n 
1 34  SER n 
1 35  ASP n 
1 36  ILE n 
1 37  LEU n 
1 38  GLN n 
1 39  TYR n 
1 40  ASP n 
1 41  ALA n 
1 42  SER n 
1 43  LEU n 
1 44  THR n 
1 45  PRO n 
1 46  LEU n 
1 47  GLU n 
1 48  PHE n 
1 49  GLN n 
1 50  GLY n 
1 51  TYR n 
1 52  ASN n 
1 53  LEU n 
1 54  SER n 
1 55  ALA n 
1 56  ASN n 
1 57  LYS n 
1 58  GLN n 
1 59  PHE n 
1 60  LEU n 
1 61  LEU n 
1 62  THR n 
1 63  ASN n 
1 64  ASN n 
1 65  GLY n 
1 66  HIS n 
1 67  SER n 
1 68  VAL n 
1 69  LYS n 
1 70  LEU n 
1 71  ASN n 
1 72  LEU n 
1 73  PRO n 
1 74  SER n 
1 75  ASP n 
1 76  MET n 
1 77  HIS n 
1 78  ILE n 
1 79  GLN n 
1 80  GLY n 
1 81  LEU n 
1 82  GLN n 
1 83  SER n 
1 84  ARG n 
1 85  TYR n 
1 86  SER n 
1 87  ALA n 
1 88  THR n 
1 89  GLN n 
1 90  LEU n 
1 91  HIS n 
1 92  LEU n 
1 93  HIS n 
1 94  TRP n 
1 95  GLY n 
1 96  ASN n 
1 97  PRO n 
1 98  ASN n 
1 99  ASP n 
1 100 PRO n 
1 101 HIS n 
1 102 GLY n 
1 103 SER n 
1 104 GLU n 
1 105 HIS n 
1 106 THR n 
1 107 VAL n 
1 108 SER n 
1 109 GLY n 
1 110 GLN n 
1 111 HIS n 
1 112 PHE n 
1 113 ALA n 
1 114 ALA n 
1 115 GLU n 
1 116 LEU n 
1 117 HIS n 
1 118 ILE n 
1 119 VAL n 
1 120 HIS n 
1 121 TYR n 
1 122 ASN n 
1 123 SER n 
1 124 ASP n 
1 125 LEU n 
1 126 TYR n 
1 127 PRO n 
1 128 ASP n 
1 129 ALA n 
1 130 SER n 
1 131 THR n 
1 132 ALA n 
1 133 SER n 
1 134 ASN n 
1 135 LYS n 
1 136 SER n 
1 137 GLU n 
1 138 GLY n 
1 139 LEU n 
1 140 ALA n 
1 141 VAL n 
1 142 LEU n 
1 143 ALA n 
1 144 VAL n 
1 145 LEU n 
1 146 ILE n 
1 147 GLU n 
1 148 MET n 
1 149 GLY n 
1 150 SER n 
1 151 PHE n 
1 152 ASN n 
1 153 PRO n 
1 154 SER n 
1 155 TYR n 
1 156 ASP n 
1 157 LYS n 
1 158 ILE n 
1 159 PHE n 
1 160 SER n 
1 161 HIS n 
1 162 LEU n 
1 163 GLN n 
1 164 HIS n 
1 165 VAL n 
1 166 LYS n 
1 167 TYR n 
1 168 LYS n 
1 169 GLY n 
1 170 GLN n 
1 171 GLU n 
1 172 ALA n 
1 173 PHE n 
1 174 VAL n 
1 175 PRO n 
1 176 GLY n 
1 177 PHE n 
1 178 ASN n 
1 179 ILE n 
1 180 GLU n 
1 181 GLU n 
1 182 LEU n 
1 183 LEU n 
1 184 PRO n 
1 185 GLU n 
1 186 ARG n 
1 187 THR n 
1 188 ALA n 
1 189 GLU n 
1 190 TYR n 
1 191 TYR n 
1 192 ARG n 
1 193 TYR n 
1 194 ARG n 
1 195 GLY n 
1 196 SER n 
1 197 LEU n 
1 198 THR n 
1 199 THR n 
1 200 PRO n 
1 201 PRO n 
1 202 CYS n 
1 203 ASN n 
1 204 PRO n 
1 205 THR n 
1 206 VAL n 
1 207 LEU n 
1 208 TRP n 
1 209 THR n 
1 210 VAL n 
1 211 PHE n 
1 212 ARG n 
1 213 ASN n 
1 214 PRO n 
1 215 VAL n 
1 216 GLN n 
1 217 ILE n 
1 218 SER n 
1 219 GLN n 
1 220 GLU n 
1 221 GLN n 
1 222 LEU n 
1 223 LEU n 
1 224 ALA n 
1 225 LEU n 
1 226 GLU n 
1 227 THR n 
1 228 ALA n 
1 229 LEU n 
1 230 TYR n 
1 231 CYS n 
1 232 THR n 
1 233 HIS n 
1 234 MET n 
1 235 ASP n 
1 236 ASP n 
1 237 PRO n 
1 238 SER n 
1 239 PRO n 
1 240 ARG n 
1 241 GLU n 
1 242 MET n 
1 243 ILE n 
1 244 ASN n 
1 245 ASN n 
1 246 PHE n 
1 247 ARG n 
1 248 GLN n 
1 249 VAL n 
1 250 GLN n 
1 251 LYS n 
1 252 PHE n 
1 253 ASP n 
1 254 GLU n 
1 255 ARG n 
1 256 LEU n 
1 257 VAL n 
1 258 TYR n 
1 259 THR n 
1 260 SER n 
1 261 PHE n 
1 262 SER n 
1 263 GLN n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      ? 
_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 
E1F non-polymer         . '2-chloro-4-[(pyrimidin-2-ylsulfanyl)acetyl]benzenesulfonamide' ?                 'C12 H10 Cl N3 O3 S2' 
343.809 
EDO non-polymer         . 1,2-ETHANEDIOL                                                  'ETHYLENE GLYCOL' 'C2 H6 O2'            
62.068  
GLN 'L-peptide linking' y GLUTAMINE                                                       ?                 'C5 H10 N2 O3'        
146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                                 ?                 'C5 H9 N O4'          
147.129 
GLY 'peptide linking'   y GLYCINE                                                         ?                 'C2 H5 N O2'          
75.067  
HIS 'L-peptide linking' y HISTIDINE                                                       ?                 'C6 H10 N3 O2 1'      
156.162 
HOH non-polymer         . WATER                                                           ?                 'H2 O'                
18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                                      ?                 'C6 H13 N O2'         
131.173 
LEU 'L-peptide linking' y LEUCINE                                                         ?                 'C6 H13 N O2'         
131.173 
LYS 'L-peptide linking' y LYSINE                                                          ?                 'C6 H15 N2 O2 1'      
147.195 
MET 'L-peptide linking' y METHIONINE                                                      ?                 'C5 H11 N O2 S'       
149.211 
PHE 'L-peptide linking' y PHENYLALANINE                                                   ?                 'C9 H11 N O2'         
165.189 
PRO 'L-peptide linking' y PROLINE                                                         ?                 'C5 H9 N O2'          
115.130 
SER 'L-peptide linking' y SERINE                                                          ?                 'C3 H7 N O3'          
105.093 
SO4 non-polymer         . 'SULFATE ION'                                                   ?                 'O4 S -2'             
96.063  
THR 'L-peptide linking' y THREONINE                                                       ?                 'C4 H9 N O3'          
119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                                      ?                 'C11 H12 N2 O2'       
204.225 
TYR 'L-peptide linking' y TYROSINE                                                        ?                 'C9 H11 N O3'         
181.189 
VAL 'L-peptide linking' y VALINE                                                          ?                 'C5 H11 N O2'         
117.146 
ZN  non-polymer         . 'ZINC ION'                                                      ?                 'Zn 2'                
65.409  
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   SER 2   2   ?   ?   ?   A . n 
A 1 3   LYS 3   3   3   LYS LYS A . n 
A 1 4   TRP 4   4   4   TRP TRP A . n 
A 1 5   THR 5   5   5   THR THR A . n 
A 1 6   TYR 6   6   6   TYR TYR A . n 
A 1 7   PHE 7   7   7   PHE PHE A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   PRO 9   9   9   PRO PRO A . n 
A 1 10  ASP 10  10  10  ASP ASP A . n 
A 1 11  GLY 11  11  11  GLY GLY A . n 
A 1 12  GLU 12  12  12  GLU GLU A . n 
A 1 13  ASN 13  13  13  ASN ASN A . n 
A 1 14  SER 14  14  14  SER SER A . n 
A 1 15  TRP 15  15  15  TRP TRP A . n 
A 1 16  SER 16  16  16  SER SER A . n 
A 1 17  LYS 17  17  17  LYS LYS A . n 
A 1 18  LYS 18  18  18  LYS LYS A . n 
A 1 19  TYR 19  19  19  TYR TYR A . n 
A 1 20  PRO 20  20  20  PRO PRO A . n 
A 1 21  SER 21  21  21  SER SER A . n 
A 1 22  CYS 22  22  22  CYS CYS A . n 
A 1 23  GLY 23  23  23  GLY GLY A . n 
A 1 24  GLY 24  24  24  GLY GLY A . n 
A 1 25  LEU 25  25  25  LEU LEU A . n 
A 1 26  LEU 26  26  26  LEU LEU A . n 
A 1 27  GLN 27  27  27  GLN GLN A . n 
A 1 28  SER 28  28  28  SER SER A . n 
A 1 29  PRO 29  29  29  PRO PRO A . n 
A 1 30  ILE 30  30  30  ILE ILE A . n 
A 1 31  ASP 31  31  31  ASP ASP A . n 
A 1 32  LEU 32  32  32  LEU LEU A . n 
A 1 33  HIS 33  33  33  HIS HIS A . n 
A 1 34  SER 34  34  34  SER SER A . n 
A 1 35  ASP 35  35  35  ASP ASP A . n 
A 1 36  ILE 36  36  36  ILE ILE A . n 
A 1 37  LEU 37  37  37  LEU LEU A . n 
A 1 38  GLN 38  38  38  GLN GLN A . n 
A 1 39  TYR 39  39  39  TYR TYR A . n 
A 1 40  ASP 40  40  40  ASP ASP A . n 
A 1 41  ALA 41  41  41  ALA ALA A . n 
A 1 42  SER 42  42  42  SER SER A . n 
A 1 43  LEU 43  43  43  LEU LEU A . n 
A 1 44  THR 44  44  44  THR THR A . n 
A 1 45  PRO 45  45  45  PRO PRO A . n 
A 1 46  LEU 46  46  46  LEU LEU A . n 
A 1 47  GLU 47  47  47  GLU GLU A . n 
A 1 48  PHE 48  48  48  PHE PHE A . n 
A 1 49  GLN 49  49  49  GLN GLN A . n 
A 1 50  GLY 50  50  50  GLY GLY A . n 
A 1 51  TYR 51  51  51  TYR TYR A . n 
A 1 52  ASN 52  52  52  ASN ASN A . n 
A 1 53  LEU 53  53  53  LEU LEU A . n 
A 1 54  SER 54  54  54  SER SER A . n 
A 1 55  ALA 55  55  55  ALA ALA A . n 
A 1 56  ASN 56  56  56  ASN ASN A . n 
A 1 57  LYS 57  57  57  LYS LYS A . n 
A 1 58  GLN 58  58  58  GLN GLN A . n 
A 1 59  PHE 59  59  59  PHE PHE A . n 
A 1 60  LEU 60  60  60  LEU LEU A . n 
A 1 61  LEU 61  61  61  LEU LEU A . n 
A 1 62  THR 62  62  62  THR THR A . n 
A 1 63  ASN 63  63  63  ASN ASN A . n 
A 1 64  ASN 64  64  64  ASN ASN A . n 
A 1 65  GLY 65  65  65  GLY GLY A . n 
A 1 66  HIS 66  66  66  HIS HIS A . n 
A 1 67  SER 67  67  67  SER SER A . n 
A 1 68  VAL 68  68  68  VAL VAL A . n 
A 1 69  LYS 69  69  69  LYS LYS A . n 
A 1 70  LEU 70  70  70  LEU LEU A . n 
A 1 71  ASN 71  71  71  ASN ASN A . n 
A 1 72  LEU 72  72  72  LEU LEU A . n 
A 1 73  PRO 73  73  73  PRO PRO A . n 
A 1 74  SER 74  74  74  SER SER A . n 
A 1 75  ASP 75  75  75  ASP ASP A . n 
A 1 76  MET 76  76  76  MET MET A . n 
A 1 77  HIS 77  77  77  HIS HIS A . n 
A 1 78  ILE 78  78  78  ILE ILE A . n 
A 1 79  GLN 79  79  79  GLN GLN A . n 
A 1 80  GLY 80  80  80  GLY GLY A . n 
A 1 81  LEU 81  81  81  LEU LEU A . n 
A 1 82  GLN 82  82  82  GLN GLN A . n 
A 1 83  SER 83  83  83  SER SER A . n 
A 1 84  ARG 84  84  84  ARG ARG A . n 
A 1 85  TYR 85  85  85  TYR TYR A . n 
A 1 86  SER 86  86  86  SER SER A . n 
A 1 87  ALA 87  87  87  ALA ALA A . n 
A 1 88  THR 88  88  88  THR THR A . n 
A 1 89  GLN 89  89  89  GLN GLN A . n 
A 1 90  LEU 90  90  90  LEU LEU A . n 
A 1 91  HIS 91  91  91  HIS HIS A . n 
A 1 92  LEU 92  92  92  LEU LEU A . n 
A 1 93  HIS 93  93  93  HIS HIS A . n 
A 1 94  TRP 94  94  94  TRP TRP A . n 
A 1 95  GLY 95  95  95  GLY GLY A . n 
A 1 96  ASN 96  96  96  ASN ASN A . n 
A 1 97  PRO 97  97  97  PRO PRO A . n 
A 1 98  ASN 98  98  98  ASN ASN A . n 
A 1 99  ASP 99  99  99  ASP ASP A . n 
A 1 100 PRO 100 100 100 PRO PRO A . n 
A 1 101 HIS 101 101 101 HIS HIS A . n 
A 1 102 GLY 102 102 102 GLY GLY A . n 
A 1 103 SER 103 103 103 SER SER A . n 
A 1 104 GLU 104 104 104 GLU GLU A . n 
A 1 105 HIS 105 105 105 HIS HIS A . n 
A 1 106 THR 106 106 106 THR THR A . n 
A 1 107 VAL 107 107 107 VAL VAL A . n 
A 1 108 SER 108 108 108 SER SER A . n 
A 1 109 GLY 109 109 109 GLY GLY A . n 
A 1 110 GLN 110 110 110 GLN GLN A . n 
A 1 111 HIS 111 111 111 HIS HIS A . n 
A 1 112 PHE 112 112 112 PHE PHE A . n 
A 1 113 ALA 113 113 113 ALA ALA A . n 
A 1 114 ALA 114 114 114 ALA ALA A . n 
A 1 115 GLU 115 115 115 GLU GLU A . n 
A 1 116 LEU 116 116 116 LEU LEU A . n 
A 1 117 HIS 117 117 117 HIS HIS A . n 
A 1 118 ILE 118 118 118 ILE ILE A . n 
A 1 119 VAL 119 119 119 VAL VAL A . n 
A 1 120 HIS 120 120 120 HIS HIS A . n 
A 1 121 TYR 121 121 121 TYR TYR A . n 
A 1 122 ASN 122 122 122 ASN ASN A . n 
A 1 123 SER 123 123 123 SER SER A . n 
A 1 124 ASP 124 124 124 ASP ASP A . n 
A 1 125 LEU 125 125 125 LEU LEU A . n 
A 1 126 TYR 126 126 126 TYR TYR A . n 
A 1 127 PRO 127 127 127 PRO PRO A . n 
A 1 128 ASP 128 128 128 ASP ASP A . n 
A 1 129 ALA 129 129 129 ALA ALA A . n 
A 1 130 SER 130 130 130 SER SER A . n 
A 1 131 THR 131 131 131 THR THR A . n 
A 1 132 ALA 132 132 132 ALA ALA A . n 
A 1 133 SER 133 133 133 SER SER A . n 
A 1 134 ASN 134 134 134 ASN ASN A . n 
A 1 135 LYS 135 135 135 LYS LYS A . n 
A 1 136 SER 136 136 136 SER SER A . n 
A 1 137 GLU 137 137 137 GLU GLU A . n 
A 1 138 GLY 138 138 138 GLY GLY A . n 
A 1 139 LEU 139 139 139 LEU LEU A . n 
A 1 140 ALA 140 140 140 ALA ALA A . n 
A 1 141 VAL 141 141 141 VAL VAL A . n 
A 1 142 LEU 142 142 142 LEU LEU A . n 
A 1 143 ALA 143 143 143 ALA ALA A . n 
A 1 144 VAL 144 144 144 VAL VAL A . n 
A 1 145 LEU 145 145 145 LEU LEU A . n 
A 1 146 ILE 146 146 146 ILE ILE A . n 
A 1 147 GLU 147 147 147 GLU GLU A . n 
A 1 148 MET 148 148 148 MET MET A . n 
A 1 149 GLY 149 149 149 GLY GLY A . n 
A 1 150 SER 150 150 150 SER SER A . n 
A 1 151 PHE 151 151 151 PHE PHE A . n 
A 1 152 ASN 152 152 152 ASN ASN A . n 
A 1 153 PRO 153 153 153 PRO PRO A . n 
A 1 154 SER 154 154 154 SER SER A . n 
A 1 155 TYR 155 155 155 TYR TYR A . n 
A 1 156 ASP 156 156 156 ASP ASP A . n 
A 1 157 LYS 157 157 157 LYS LYS A . n 
A 1 158 ILE 158 158 158 ILE ILE A . n 
A 1 159 PHE 159 159 159 PHE PHE A . n 
A 1 160 SER 160 160 160 SER SER A . n 
A 1 161 HIS 161 161 161 HIS HIS A . n 
A 1 162 LEU 162 162 162 LEU LEU A . n 
A 1 163 GLN 163 163 163 GLN GLN A . n 
A 1 164 HIS 164 164 164 HIS HIS A . n 
A 1 165 VAL 165 165 165 VAL VAL A . n 
A 1 166 LYS 166 166 166 LYS LYS A . n 
A 1 167 TYR 167 167 167 TYR TYR A . n 
A 1 168 LYS 168 168 168 LYS LYS A . n 
A 1 169 GLY 169 169 169 GLY GLY A . n 
A 1 170 GLN 170 170 170 GLN GLN A . n 
A 1 171 GLU 171 171 171 GLU GLU A . n 
A 1 172 ALA 172 172 172 ALA ALA A . n 
A 1 173 PHE 173 173 173 PHE PHE A . n 
A 1 174 VAL 174 174 174 VAL VAL A . n 
A 1 175 PRO 175 175 175 PRO PRO A . n 
A 1 176 GLY 176 176 176 GLY GLY A . n 
A 1 177 PHE 177 177 177 PHE PHE A . n 
A 1 178 ASN 178 178 178 ASN ASN A . n 
A 1 179 ILE 179 179 179 ILE ILE A . n 
A 1 180 GLU 180 180 180 GLU GLU A . n 
A 1 181 GLU 181 181 181 GLU GLU A . n 
A 1 182 LEU 182 182 182 LEU LEU A . n 
A 1 183 LEU 183 183 183 LEU LEU A . n 
A 1 184 PRO 184 184 184 PRO PRO A . n 
A 1 185 GLU 185 185 185 GLU GLU A . n 
A 1 186 ARG 186 186 186 ARG ARG A . n 
A 1 187 THR 187 187 187 THR THR A . n 
A 1 188 ALA 188 188 188 ALA ALA A . n 
A 1 189 GLU 189 189 189 GLU GLU A . n 
A 1 190 TYR 190 190 190 TYR TYR A . n 
A 1 191 TYR 191 191 191 TYR TYR A . n 
A 1 192 ARG 192 192 192 ARG ARG A . n 
A 1 193 TYR 193 193 193 TYR TYR A . n 
A 1 194 ARG 194 194 194 ARG ARG A . n 
A 1 195 GLY 195 195 195 GLY GLY A . n 
A 1 196 SER 196 196 196 SER SER A . n 
A 1 197 LEU 197 197 197 LEU LEU A . n 
A 1 198 THR 198 198 198 THR THR A . n 
A 1 199 THR 199 199 199 THR THR A . n 
A 1 200 PRO 200 200 200 PRO PRO A . n 
A 1 201 PRO 201 201 201 PRO PRO A . n 
A 1 202 CYS 202 202 202 CYS CYS A . n 
A 1 203 ASN 203 203 203 ASN ASN A . n 
A 1 204 PRO 204 204 204 PRO PRO A . n 
A 1 205 THR 205 205 205 THR THR A . n 
A 1 206 VAL 206 206 206 VAL VAL A . n 
A 1 207 LEU 207 207 207 LEU LEU A . n 
A 1 208 TRP 208 208 208 TRP TRP A . n 
A 1 209 THR 209 209 209 THR THR A . n 
A 1 210 VAL 210 210 210 VAL VAL A . n 
A 1 211 PHE 211 211 211 PHE PHE A . n 
A 1 212 ARG 212 212 212 ARG ARG A . n 
A 1 213 ASN 213 213 213 ASN ASN A . n 
A 1 214 PRO 214 214 214 PRO PRO A . n 
A 1 215 VAL 215 215 215 VAL VAL A . n 
A 1 216 GLN 216 216 216 GLN GLN A . n 
A 1 217 ILE 217 217 217 ILE ILE A . n 
A 1 218 SER 218 218 218 SER SER A . n 
A 1 219 GLN 219 219 219 GLN GLN A . n 
A 1 220 GLU 220 220 220 GLU GLU A . n 
A 1 221 GLN 221 221 221 GLN GLN A . n 
A 1 222 LEU 222 222 222 LEU LEU A . n 
A 1 223 LEU 223 223 223 LEU LEU A . n 
A 1 224 ALA 224 224 224 ALA ALA A . n 
A 1 225 LEU 225 225 225 LEU LEU A . n 
A 1 226 GLU 226 226 226 GLU GLU A . n 
A 1 227 THR 227 227 227 THR THR A . n 
A 1 228 ALA 228 228 228 ALA ALA A . n 
A 1 229 LEU 229 229 229 LEU LEU A . n 
A 1 230 TYR 230 230 230 TYR TYR A . n 
A 1 231 CYS 231 231 231 CYS CYS A . n 
A 1 232 THR 232 232 232 THR THR A . n 
A 1 233 HIS 233 233 233 HIS HIS A . n 
A 1 234 MET 234 234 234 MET MET A . n 
A 1 235 ASP 235 235 235 ASP ASP A . n 
A 1 236 ASP 236 236 236 ASP ASP A . n 
A 1 237 PRO 237 237 237 PRO PRO A . n 
A 1 238 SER 238 238 238 SER SER A . n 
A 1 239 PRO 239 239 239 PRO PRO A . n 
A 1 240 ARG 240 240 240 ARG ARG A . n 
A 1 241 GLU 241 241 241 GLU GLU A . n 
A 1 242 MET 242 242 242 MET MET A . n 
A 1 243 ILE 243 243 243 ILE ILE A . n 
A 1 244 ASN 244 244 244 ASN ASN A . n 
A 1 245 ASN 245 245 245 ASN ASN A . n 
A 1 246 PHE 246 246 246 PHE PHE A . n 
A 1 247 ARG 247 247 247 ARG ARG A . n 
A 1 248 GLN 248 248 248 GLN GLN A . n 
A 1 249 VAL 249 249 249 VAL VAL A . n 
A 1 250 GLN 250 250 250 GLN GLN A . n 
A 1 251 LYS 251 251 251 LYS LYS A . n 
A 1 252 PHE 252 252 252 PHE PHE A . n 
A 1 253 ASP 253 253 253 ASP ASP A . n 
A 1 254 GLU 254 254 254 GLU GLU A . n 
A 1 255 ARG 255 255 255 ARG ARG A . n 
A 1 256 LEU 256 256 256 LEU LEU A . n 
A 1 257 VAL 257 257 257 VAL VAL A . n 
A 1 258 TYR 258 258 258 TYR TYR A . n 
A 1 259 THR 259 259 259 THR THR A . n 
A 1 260 SER 260 260 260 SER SER A . n 
A 1 261 PHE 261 261 261 PHE PHE A . n 
A 1 262 SER 262 262 262 SER SER A . n 
A 1 263 GLN 263 263 263 GLN GLN A . n 
B 1 1   MET 1   1   ?   ?   ?   B . n 
B 1 2   SER 2   2   ?   ?   ?   B . n 
B 1 3   LYS 3   3   3   LYS LYS B . n 
B 1 4   TRP 4   4   4   TRP TRP B . n 
B 1 5   THR 5   5   5   THR THR B . n 
B 1 6   TYR 6   6   6   TYR TYR B . n 
B 1 7   PHE 7   7   7   PHE PHE B . n 
B 1 8   GLY 8   8   8   GLY GLY B . n 
B 1 9   PRO 9   9   9   PRO PRO B . n 
B 1 10  ASP 10  10  10  ASP ASP B . n 
B 1 11  GLY 11  11  11  GLY GLY B . n 
B 1 12  GLU 12  12  12  GLU GLU B . n 
B 1 13  ASN 13  13  13  ASN ASN B . n 
B 1 14  SER 14  14  14  SER SER B . n 
B 1 15  TRP 15  15  15  TRP TRP B . n 
B 1 16  SER 16  16  16  SER SER B . n 
B 1 17  LYS 17  17  17  LYS LYS B . n 
B 1 18  LYS 18  18  18  LYS LYS B . n 
B 1 19  TYR 19  19  19  TYR TYR B . n 
B 1 20  PRO 20  20  20  PRO PRO B . n 
B 1 21  SER 21  21  21  SER SER B . n 
B 1 22  CYS 22  22  22  CYS CYS B . n 
B 1 23  GLY 23  23  23  GLY GLY B . n 
B 1 24  GLY 24  24  24  GLY GLY B . n 
B 1 25  LEU 25  25  25  LEU LEU B . n 
B 1 26  LEU 26  26  26  LEU LEU B . n 
B 1 27  GLN 27  27  27  GLN GLN B . n 
B 1 28  SER 28  28  28  SER SER B . n 
B 1 29  PRO 29  29  29  PRO PRO B . n 
B 1 30  ILE 30  30  30  ILE ILE B . n 
B 1 31  ASP 31  31  31  ASP ASP B . n 
B 1 32  LEU 32  32  32  LEU LEU B . n 
B 1 33  HIS 33  33  33  HIS HIS B . n 
B 1 34  SER 34  34  34  SER SER B . n 
B 1 35  ASP 35  35  35  ASP ASP B . n 
B 1 36  ILE 36  36  36  ILE ILE B . n 
B 1 37  LEU 37  37  37  LEU LEU B . n 
B 1 38  GLN 38  38  38  GLN GLN B . n 
B 1 39  TYR 39  39  39  TYR TYR B . n 
B 1 40  ASP 40  40  40  ASP ASP B . n 
B 1 41  ALA 41  41  41  ALA ALA B . n 
B 1 42  SER 42  42  42  SER SER B . n 
B 1 43  LEU 43  43  43  LEU LEU B . n 
B 1 44  THR 44  44  44  THR THR B . n 
B 1 45  PRO 45  45  45  PRO PRO B . n 
B 1 46  LEU 46  46  46  LEU LEU B . n 
B 1 47  GLU 47  47  47  GLU GLU B . n 
B 1 48  PHE 48  48  48  PHE PHE B . n 
B 1 49  GLN 49  49  49  GLN GLN B . n 
B 1 50  GLY 50  50  50  GLY GLY B . n 
B 1 51  TYR 51  51  51  TYR TYR B . n 
B 1 52  ASN 52  52  52  ASN ASN B . n 
B 1 53  LEU 53  53  53  LEU LEU B . n 
B 1 54  SER 54  54  54  SER SER B . n 
B 1 55  ALA 55  55  55  ALA ALA B . n 
B 1 56  ASN 56  56  56  ASN ASN B . n 
B 1 57  LYS 57  57  57  LYS LYS B . n 
B 1 58  GLN 58  58  58  GLN GLN B . n 
B 1 59  PHE 59  59  59  PHE PHE B . n 
B 1 60  LEU 60  60  60  LEU LEU B . n 
B 1 61  LEU 61  61  61  LEU LEU B . n 
B 1 62  THR 62  62  62  THR THR B . n 
B 1 63  ASN 63  63  63  ASN ASN B . n 
B 1 64  ASN 64  64  64  ASN ASN B . n 
B 1 65  GLY 65  65  65  GLY GLY B . n 
B 1 66  HIS 66  66  66  HIS HIS B . n 
B 1 67  SER 67  67  67  SER SER B . n 
B 1 68  VAL 68  68  68  VAL VAL B . n 
B 1 69  LYS 69  69  69  LYS LYS B . n 
B 1 70  LEU 70  70  70  LEU LEU B . n 
B 1 71  ASN 71  71  71  ASN ASN B . n 
B 1 72  LEU 72  72  72  LEU LEU B . n 
B 1 73  PRO 73  73  73  PRO PRO B . n 
B 1 74  SER 74  74  74  SER SER B . n 
B 1 75  ASP 75  75  75  ASP ASP B . n 
B 1 76  MET 76  76  76  MET MET B . n 
B 1 77  HIS 77  77  77  HIS HIS B . n 
B 1 78  ILE 78  78  78  ILE ILE B . n 
B 1 79  GLN 79  79  79  GLN GLN B . n 
B 1 80  GLY 80  80  80  GLY GLY B . n 
B 1 81  LEU 81  81  81  LEU LEU B . n 
B 1 82  GLN 82  82  82  GLN GLN B . n 
B 1 83  SER 83  83  83  SER SER B . n 
B 1 84  ARG 84  84  84  ARG ARG B . n 
B 1 85  TYR 85  85  85  TYR TYR B . n 
B 1 86  SER 86  86  86  SER SER B . n 
B 1 87  ALA 87  87  87  ALA ALA B . n 
B 1 88  THR 88  88  88  THR THR B . n 
B 1 89  GLN 89  89  89  GLN GLN B . n 
B 1 90  LEU 90  90  90  LEU LEU B . n 
B 1 91  HIS 91  91  91  HIS HIS B . n 
B 1 92  LEU 92  92  92  LEU LEU B . n 
B 1 93  HIS 93  93  93  HIS HIS B . n 
B 1 94  TRP 94  94  94  TRP TRP B . n 
B 1 95  GLY 95  95  95  GLY GLY B . n 
B 1 96  ASN 96  96  96  ASN ASN B . n 
B 1 97  PRO 97  97  97  PRO PRO B . n 
B 1 98  ASN 98  98  98  ASN ASN B . n 
B 1 99  ASP 99  99  99  ASP ASP B . n 
B 1 100 PRO 100 100 100 PRO PRO B . n 
B 1 101 HIS 101 101 101 HIS HIS B . n 
B 1 102 GLY 102 102 102 GLY GLY B . n 
B 1 103 SER 103 103 103 SER SER B . n 
B 1 104 GLU 104 104 104 GLU GLU B . n 
B 1 105 HIS 105 105 105 HIS HIS B . n 
B 1 106 THR 106 106 106 THR THR B . n 
B 1 107 VAL 107 107 107 VAL VAL B . n 
B 1 108 SER 108 108 108 SER SER B . n 
B 1 109 GLY 109 109 109 GLY GLY B . n 
B 1 110 GLN 110 110 110 GLN GLN B . n 
B 1 111 HIS 111 111 111 HIS HIS B . n 
B 1 112 PHE 112 112 112 PHE PHE B . n 
B 1 113 ALA 113 113 113 ALA ALA B . n 
B 1 114 ALA 114 114 114 ALA ALA B . n 
B 1 115 GLU 115 115 115 GLU GLU B . n 
B 1 116 LEU 116 116 116 LEU LEU B . n 
B 1 117 HIS 117 117 117 HIS HIS B . n 
B 1 118 ILE 118 118 118 ILE ILE B . n 
B 1 119 VAL 119 119 119 VAL VAL B . n 
B 1 120 HIS 120 120 120 HIS HIS B . n 
B 1 121 TYR 121 121 121 TYR TYR B . n 
B 1 122 ASN 122 122 122 ASN ASN B . n 
B 1 123 SER 123 123 123 SER SER B . n 
B 1 124 ASP 124 124 124 ASP ASP B . n 
B 1 125 LEU 125 125 125 LEU LEU B . n 
B 1 126 TYR 126 126 126 TYR TYR B . n 
B 1 127 PRO 127 127 127 PRO PRO B . n 
B 1 128 ASP 128 128 128 ASP ASP B . n 
B 1 129 ALA 129 129 129 ALA ALA B . n 
B 1 130 SER 130 130 130 SER SER B . n 
B 1 131 THR 131 131 131 THR THR B . n 
B 1 132 ALA 132 132 132 ALA ALA B . n 
B 1 133 SER 133 133 133 SER SER B . n 
B 1 134 ASN 134 134 134 ASN ASN B . n 
B 1 135 LYS 135 135 135 LYS LYS B . n 
B 1 136 SER 136 136 136 SER SER B . n 
B 1 137 GLU 137 137 137 GLU GLU B . n 
B 1 138 GLY 138 138 138 GLY GLY B . n 
B 1 139 LEU 139 139 139 LEU LEU B . n 
B 1 140 ALA 140 140 140 ALA ALA B . n 
B 1 141 VAL 141 141 141 VAL VAL B . n 
B 1 142 LEU 142 142 142 LEU LEU B . n 
B 1 143 ALA 143 143 143 ALA ALA B . n 
B 1 144 VAL 144 144 144 VAL VAL B . n 
B 1 145 LEU 145 145 145 LEU LEU B . n 
B 1 146 ILE 146 146 146 ILE ILE B . n 
B 1 147 GLU 147 147 147 GLU GLU B . n 
B 1 148 MET 148 148 148 MET MET B . n 
B 1 149 GLY 149 149 149 GLY GLY B . n 
B 1 150 SER 150 150 150 SER SER B . n 
B 1 151 PHE 151 151 151 PHE PHE B . n 
B 1 152 ASN 152 152 152 ASN ASN B . n 
B 1 153 PRO 153 153 153 PRO PRO B . n 
B 1 154 SER 154 154 154 SER SER B . n 
B 1 155 TYR 155 155 155 TYR TYR B . n 
B 1 156 ASP 156 156 156 ASP ASP B . n 
B 1 157 LYS 157 157 157 LYS LYS B . n 
B 1 158 ILE 158 158 158 ILE ILE B . n 
B 1 159 PHE 159 159 159 PHE PHE B . n 
B 1 160 SER 160 160 160 SER SER B . n 
B 1 161 HIS 161 161 161 HIS HIS B . n 
B 1 162 LEU 162 162 162 LEU LEU B . n 
B 1 163 GLN 163 163 163 GLN GLN B . n 
B 1 164 HIS 164 164 164 HIS HIS B . n 
B 1 165 VAL 165 165 165 VAL VAL B . n 
B 1 166 LYS 166 166 166 LYS LYS B . n 
B 1 167 TYR 167 167 167 TYR TYR B . n 
B 1 168 LYS 168 168 168 LYS LYS B . n 
B 1 169 GLY 169 169 169 GLY GLY B . n 
B 1 170 GLN 170 170 170 GLN GLN B . n 
B 1 171 GLU 171 171 171 GLU GLU B . n 
B 1 172 ALA 172 172 172 ALA ALA B . n 
B 1 173 PHE 173 173 173 PHE PHE B . n 
B 1 174 VAL 174 174 174 VAL VAL B . n 
B 1 175 PRO 175 175 175 PRO PRO B . n 
B 1 176 GLY 176 176 176 GLY GLY B . n 
B 1 177 PHE 177 177 177 PHE PHE B . n 
B 1 178 ASN 178 178 178 ASN ASN B . n 
B 1 179 ILE 179 179 179 ILE ILE B . n 
B 1 180 GLU 180 180 180 GLU GLU B . n 
B 1 181 GLU 181 181 181 GLU GLU B . n 
B 1 182 LEU 182 182 182 LEU LEU B . n 
B 1 183 LEU 183 183 183 LEU LEU B . n 
B 1 184 PRO 184 184 184 PRO PRO B . n 
B 1 185 GLU 185 185 185 GLU GLU B . n 
B 1 186 ARG 186 186 186 ARG ARG B . n 
B 1 187 THR 187 187 187 THR THR B . n 
B 1 188 ALA 188 188 188 ALA ALA B . n 
B 1 189 GLU 189 189 189 GLU GLU B . n 
B 1 190 TYR 190 190 190 TYR TYR B . n 
B 1 191 TYR 191 191 191 TYR TYR B . n 
B 1 192 ARG 192 192 192 ARG ARG B . n 
B 1 193 TYR 193 193 193 TYR TYR B . n 
B 1 194 ARG 194 194 194 ARG ARG B . n 
B 1 195 GLY 195 195 195 GLY GLY B . n 
B 1 196 SER 196 196 196 SER SER B . n 
B 1 197 LEU 197 197 197 LEU LEU B . n 
B 1 198 THR 198 198 198 THR THR B . n 
B 1 199 THR 199 199 199 THR THR B . n 
B 1 200 PRO 200 200 200 PRO PRO B . n 
B 1 201 PRO 201 201 201 PRO PRO B . n 
B 1 202 CYS 202 202 202 CYS CYS B . n 
B 1 203 ASN 203 203 203 ASN ASN B . n 
B 1 204 PRO 204 204 204 PRO PRO B . n 
B 1 205 THR 205 205 205 THR THR B . n 
B 1 206 VAL 206 206 206 VAL VAL B . n 
B 1 207 LEU 207 207 207 LEU LEU B . n 
B 1 208 TRP 208 208 208 TRP TRP B . n 
B 1 209 THR 209 209 209 THR THR B . n 
B 1 210 VAL 210 210 210 VAL VAL B . n 
B 1 211 PHE 211 211 211 PHE PHE B . n 
B 1 212 ARG 212 212 212 ARG ARG B . n 
B 1 213 ASN 213 213 213 ASN ASN B . n 
B 1 214 PRO 214 214 214 PRO PRO B . n 
B 1 215 VAL 215 215 215 VAL VAL B . n 
B 1 216 GLN 216 216 216 GLN GLN B . n 
B 1 217 ILE 217 217 217 ILE ILE B . n 
B 1 218 SER 218 218 218 SER SER B . n 
B 1 219 GLN 219 219 219 GLN GLN B . n 
B 1 220 GLU 220 220 220 GLU GLU B . n 
B 1 221 GLN 221 221 221 GLN GLN B . n 
B 1 222 LEU 222 222 222 LEU LEU B . n 
B 1 223 LEU 223 223 223 LEU LEU B . n 
B 1 224 ALA 224 224 224 ALA ALA B . n 
B 1 225 LEU 225 225 225 LEU LEU B . n 
B 1 226 GLU 226 226 226 GLU GLU B . n 
B 1 227 THR 227 227 227 THR THR B . n 
B 1 228 ALA 228 228 228 ALA ALA B . n 
B 1 229 LEU 229 229 229 LEU LEU B . n 
B 1 230 TYR 230 230 230 TYR TYR B . n 
B 1 231 CYS 231 231 231 CYS CYS B . n 
B 1 232 THR 232 232 232 THR THR B . n 
B 1 233 HIS 233 233 233 HIS HIS B . n 
B 1 234 MET 234 234 234 MET MET B . n 
B 1 235 ASP 235 235 235 ASP ASP B . n 
B 1 236 ASP 236 236 236 ASP ASP B . n 
B 1 237 PRO 237 237 237 PRO PRO B . n 
B 1 238 SER 238 238 238 SER SER B . n 
B 1 239 PRO 239 239 239 PRO PRO B . n 
B 1 240 ARG 240 240 240 ARG ARG B . n 
B 1 241 GLU 241 241 241 GLU GLU B . n 
B 1 242 MET 242 242 242 MET MET B . n 
B 1 243 ILE 243 243 243 ILE ILE B . n 
B 1 244 ASN 244 244 244 ASN ASN B . n 
B 1 245 ASN 245 245 245 ASN ASN B . n 
B 1 246 PHE 246 246 246 PHE PHE B . n 
B 1 247 ARG 247 247 247 ARG ARG B . n 
B 1 248 GLN 248 248 248 GLN GLN B . n 
B 1 249 VAL 249 249 249 VAL VAL B . n 
B 1 250 GLN 250 250 250 GLN GLN B . n 
B 1 251 LYS 251 251 251 LYS LYS B . n 
B 1 252 PHE 252 252 252 PHE PHE B . n 
B 1 253 ASP 253 253 253 ASP ASP B . n 
B 1 254 GLU 254 254 254 GLU GLU B . n 
B 1 255 ARG 255 255 255 ARG ARG B . n 
B 1 256 LEU 256 256 256 LEU LEU B . n 
B 1 257 VAL 257 257 257 VAL VAL B . n 
B 1 258 TYR 258 258 258 TYR TYR B . n 
B 1 259 THR 259 259 259 THR THR B . n 
B 1 260 SER 260 260 260 SER SER B . n 
B 1 261 PHE 261 261 261 PHE PHE B . n 
B 1 262 SER 262 262 262 SER SER B . n 
B 1 263 GLN 263 263 263 GLN GLN B . n 
C 1 1   MET 1   1   ?   ?   ?   C . n 
C 1 2   SER 2   2   ?   ?   ?   C . n 
C 1 3   LYS 3   3   3   LYS LYS C . n 
C 1 4   TRP 4   4   4   TRP TRP C . n 
C 1 5   THR 5   5   5   THR THR C . n 
C 1 6   TYR 6   6   6   TYR TYR C . n 
C 1 7   PHE 7   7   7   PHE PHE C . n 
C 1 8   GLY 8   8   8   GLY GLY C . n 
C 1 9   PRO 9   9   9   PRO PRO C . n 
C 1 10  ASP 10  10  10  ASP ASP C . n 
C 1 11  GLY 11  11  11  GLY GLY C . n 
C 1 12  GLU 12  12  12  GLU GLU C . n 
C 1 13  ASN 13  13  13  ASN ASN C . n 
C 1 14  SER 14  14  14  SER SER C . n 
C 1 15  TRP 15  15  15  TRP TRP C . n 
C 1 16  SER 16  16  16  SER SER C . n 
C 1 17  LYS 17  17  17  LYS LYS C . n 
C 1 18  LYS 18  18  18  LYS LYS C . n 
C 1 19  TYR 19  19  19  TYR TYR C . n 
C 1 20  PRO 20  20  20  PRO PRO C . n 
C 1 21  SER 21  21  21  SER SER C . n 
C 1 22  CYS 22  22  22  CYS CYS C . n 
C 1 23  GLY 23  23  23  GLY GLY C . n 
C 1 24  GLY 24  24  24  GLY GLY C . n 
C 1 25  LEU 25  25  25  LEU LEU C . n 
C 1 26  LEU 26  26  26  LEU LEU C . n 
C 1 27  GLN 27  27  27  GLN GLN C . n 
C 1 28  SER 28  28  28  SER SER C . n 
C 1 29  PRO 29  29  29  PRO PRO C . n 
C 1 30  ILE 30  30  30  ILE ILE C . n 
C 1 31  ASP 31  31  31  ASP ASP C . n 
C 1 32  LEU 32  32  32  LEU LEU C . n 
C 1 33  HIS 33  33  33  HIS HIS C . n 
C 1 34  SER 34  34  34  SER SER C . n 
C 1 35  ASP 35  35  35  ASP ASP C . n 
C 1 36  ILE 36  36  36  ILE ILE C . n 
C 1 37  LEU 37  37  37  LEU LEU C . n 
C 1 38  GLN 38  38  38  GLN GLN C . n 
C 1 39  TYR 39  39  39  TYR TYR C . n 
C 1 40  ASP 40  40  40  ASP ASP C . n 
C 1 41  ALA 41  41  41  ALA ALA C . n 
C 1 42  SER 42  42  42  SER SER C . n 
C 1 43  LEU 43  43  43  LEU LEU C . n 
C 1 44  THR 44  44  44  THR THR C . n 
C 1 45  PRO 45  45  45  PRO PRO C . n 
C 1 46  LEU 46  46  46  LEU LEU C . n 
C 1 47  GLU 47  47  47  GLU GLU C . n 
C 1 48  PHE 48  48  48  PHE PHE C . n 
C 1 49  GLN 49  49  49  GLN GLN C . n 
C 1 50  GLY 50  50  50  GLY GLY C . n 
C 1 51  TYR 51  51  51  TYR TYR C . n 
C 1 52  ASN 52  52  52  ASN ASN C . n 
C 1 53  LEU 53  53  53  LEU LEU C . n 
C 1 54  SER 54  54  54  SER SER C . n 
C 1 55  ALA 55  55  55  ALA ALA C . n 
C 1 56  ASN 56  56  56  ASN ASN C . n 
C 1 57  LYS 57  57  57  LYS LYS C . n 
C 1 58  GLN 58  58  58  GLN GLN C . n 
C 1 59  PHE 59  59  59  PHE PHE C . n 
C 1 60  LEU 60  60  60  LEU LEU C . n 
C 1 61  LEU 61  61  61  LEU LEU C . n 
C 1 62  THR 62  62  62  THR THR C . n 
C 1 63  ASN 63  63  63  ASN ASN C . n 
C 1 64  ASN 64  64  64  ASN ASN C . n 
C 1 65  GLY 65  65  65  GLY GLY C . n 
C 1 66  HIS 66  66  66  HIS HIS C . n 
C 1 67  SER 67  67  67  SER SER C . n 
C 1 68  VAL 68  68  68  VAL VAL C . n 
C 1 69  LYS 69  69  69  LYS LYS C . n 
C 1 70  LEU 70  70  70  LEU LEU C . n 
C 1 71  ASN 71  71  71  ASN ASN C . n 
C 1 72  LEU 72  72  72  LEU LEU C . n 
C 1 73  PRO 73  73  73  PRO PRO C . n 
C 1 74  SER 74  74  74  SER SER C . n 
C 1 75  ASP 75  75  75  ASP ASP C . n 
C 1 76  MET 76  76  76  MET MET C . n 
C 1 77  HIS 77  77  77  HIS HIS C . n 
C 1 78  ILE 78  78  78  ILE ILE C . n 
C 1 79  GLN 79  79  79  GLN GLN C . n 
C 1 80  GLY 80  80  80  GLY GLY C . n 
C 1 81  LEU 81  81  81  LEU LEU C . n 
C 1 82  GLN 82  82  82  GLN GLN C . n 
C 1 83  SER 83  83  83  SER SER C . n 
C 1 84  ARG 84  84  84  ARG ARG C . n 
C 1 85  TYR 85  85  85  TYR TYR C . n 
C 1 86  SER 86  86  86  SER SER C . n 
C 1 87  ALA 87  87  87  ALA ALA C . n 
C 1 88  THR 88  88  88  THR THR C . n 
C 1 89  GLN 89  89  89  GLN GLN C . n 
C 1 90  LEU 90  90  90  LEU LEU C . n 
C 1 91  HIS 91  91  91  HIS HIS C . n 
C 1 92  LEU 92  92  92  LEU LEU C . n 
C 1 93  HIS 93  93  93  HIS HIS C . n 
C 1 94  TRP 94  94  94  TRP TRP C . n 
C 1 95  GLY 95  95  95  GLY GLY C . n 
C 1 96  ASN 96  96  96  ASN ASN C . n 
C 1 97  PRO 97  97  97  PRO PRO C . n 
C 1 98  ASN 98  98  98  ASN ASN C . n 
C 1 99  ASP 99  99  99  ASP ASP C . n 
C 1 100 PRO 100 100 100 PRO PRO C . n 
C 1 101 HIS 101 101 101 HIS HIS C . n 
C 1 102 GLY 102 102 102 GLY GLY C . n 
C 1 103 SER 103 103 103 SER SER C . n 
C 1 104 GLU 104 104 104 GLU GLU C . n 
C 1 105 HIS 105 105 105 HIS HIS C . n 
C 1 106 THR 106 106 106 THR THR C . n 
C 1 107 VAL 107 107 107 VAL VAL C . n 
C 1 108 SER 108 108 108 SER SER C . n 
C 1 109 GLY 109 109 109 GLY GLY C . n 
C 1 110 GLN 110 110 110 GLN GLN C . n 
C 1 111 HIS 111 111 111 HIS HIS C . n 
C 1 112 PHE 112 112 112 PHE PHE C . n 
C 1 113 ALA 113 113 113 ALA ALA C . n 
C 1 114 ALA 114 114 114 ALA ALA C . n 
C 1 115 GLU 115 115 115 GLU GLU C . n 
C 1 116 LEU 116 116 116 LEU LEU C . n 
C 1 117 HIS 117 117 117 HIS HIS C . n 
C 1 118 ILE 118 118 118 ILE ILE C . n 
C 1 119 VAL 119 119 119 VAL VAL C . n 
C 1 120 HIS 120 120 120 HIS HIS C . n 
C 1 121 TYR 121 121 121 TYR TYR C . n 
C 1 122 ASN 122 122 122 ASN ASN C . n 
C 1 123 SER 123 123 123 SER SER C . n 
C 1 124 ASP 124 124 124 ASP ASP C . n 
C 1 125 LEU 125 125 125 LEU LEU C . n 
C 1 126 TYR 126 126 126 TYR TYR C . n 
C 1 127 PRO 127 127 127 PRO PRO C . n 
C 1 128 ASP 128 128 128 ASP ASP C . n 
C 1 129 ALA 129 129 129 ALA ALA C . n 
C 1 130 SER 130 130 130 SER SER C . n 
C 1 131 THR 131 131 131 THR THR C . n 
C 1 132 ALA 132 132 132 ALA ALA C . n 
C 1 133 SER 133 133 133 SER SER C . n 
C 1 134 ASN 134 134 134 ASN ASN C . n 
C 1 135 LYS 135 135 135 LYS LYS C . n 
C 1 136 SER 136 136 136 SER SER C . n 
C 1 137 GLU 137 137 137 GLU GLU C . n 
C 1 138 GLY 138 138 138 GLY GLY C . n 
C 1 139 LEU 139 139 139 LEU LEU C . n 
C 1 140 ALA 140 140 140 ALA ALA C . n 
C 1 141 VAL 141 141 141 VAL VAL C . n 
C 1 142 LEU 142 142 142 LEU LEU C . n 
C 1 143 ALA 143 143 143 ALA ALA C . n 
C 1 144 VAL 144 144 144 VAL VAL C . n 
C 1 145 LEU 145 145 145 LEU LEU C . n 
C 1 146 ILE 146 146 146 ILE ILE C . n 
C 1 147 GLU 147 147 147 GLU GLU C . n 
C 1 148 MET 148 148 148 MET MET C . n 
C 1 149 GLY 149 149 149 GLY GLY C . n 
C 1 150 SER 150 150 150 SER SER C . n 
C 1 151 PHE 151 151 151 PHE PHE C . n 
C 1 152 ASN 152 152 152 ASN ASN C . n 
C 1 153 PRO 153 153 153 PRO PRO C . n 
C 1 154 SER 154 154 154 SER SER C . n 
C 1 155 TYR 155 155 155 TYR TYR C . n 
C 1 156 ASP 156 156 156 ASP ASP C . n 
C 1 157 LYS 157 157 157 LYS LYS C . n 
C 1 158 ILE 158 158 158 ILE ILE C . n 
C 1 159 PHE 159 159 159 PHE PHE C . n 
C 1 160 SER 160 160 160 SER SER C . n 
C 1 161 HIS 161 161 161 HIS HIS C . n 
C 1 162 LEU 162 162 162 LEU LEU C . n 
C 1 163 GLN 163 163 163 GLN GLN C . n 
C 1 164 HIS 164 164 164 HIS HIS C . n 
C 1 165 VAL 165 165 165 VAL VAL C . n 
C 1 166 LYS 166 166 166 LYS LYS C . n 
C 1 167 TYR 167 167 167 TYR TYR C . n 
C 1 168 LYS 168 168 168 LYS LYS C . n 
C 1 169 GLY 169 169 169 GLY GLY C . n 
C 1 170 GLN 170 170 170 GLN GLN C . n 
C 1 171 GLU 171 171 171 GLU GLU C . n 
C 1 172 ALA 172 172 172 ALA ALA C . n 
C 1 173 PHE 173 173 173 PHE PHE C . n 
C 1 174 VAL 174 174 174 VAL VAL C . n 
C 1 175 PRO 175 175 175 PRO PRO C . n 
C 1 176 GLY 176 176 176 GLY GLY C . n 
C 1 177 PHE 177 177 177 PHE PHE C . n 
C 1 178 ASN 178 178 178 ASN ASN C . n 
C 1 179 ILE 179 179 179 ILE ILE C . n 
C 1 180 GLU 180 180 180 GLU GLU C . n 
C 1 181 GLU 181 181 181 GLU GLU C . n 
C 1 182 LEU 182 182 182 LEU LEU C . n 
C 1 183 LEU 183 183 183 LEU LEU C . n 
C 1 184 PRO 184 184 184 PRO PRO C . n 
C 1 185 GLU 185 185 185 GLU GLU C . n 
C 1 186 ARG 186 186 186 ARG ARG C . n 
C 1 187 THR 187 187 187 THR THR C . n 
C 1 188 ALA 188 188 188 ALA ALA C . n 
C 1 189 GLU 189 189 189 GLU GLU C . n 
C 1 190 TYR 190 190 190 TYR TYR C . n 
C 1 191 TYR 191 191 191 TYR TYR C . n 
C 1 192 ARG 192 192 192 ARG ARG C . n 
C 1 193 TYR 193 193 193 TYR TYR C . n 
C 1 194 ARG 194 194 194 ARG ARG C . n 
C 1 195 GLY 195 195 195 GLY GLY C . n 
C 1 196 SER 196 196 196 SER SER C . n 
C 1 197 LEU 197 197 197 LEU LEU C . n 
C 1 198 THR 198 198 198 THR THR C . n 
C 1 199 THR 199 199 199 THR THR C . n 
C 1 200 PRO 200 200 200 PRO PRO C . n 
C 1 201 PRO 201 201 201 PRO PRO C . n 
C 1 202 CYS 202 202 202 CYS CYS C . n 
C 1 203 ASN 203 203 203 ASN ASN C . n 
C 1 204 PRO 204 204 204 PRO PRO C . n 
C 1 205 THR 205 205 205 THR THR C . n 
C 1 206 VAL 206 206 206 VAL VAL C . n 
C 1 207 LEU 207 207 207 LEU LEU C . n 
C 1 208 TRP 208 208 208 TRP TRP C . n 
C 1 209 THR 209 209 209 THR THR C . n 
C 1 210 VAL 210 210 210 VAL VAL C . n 
C 1 211 PHE 211 211 211 PHE PHE C . n 
C 1 212 ARG 212 212 212 ARG ARG C . n 
C 1 213 ASN 213 213 213 ASN ASN C . n 
C 1 214 PRO 214 214 214 PRO PRO C . n 
C 1 215 VAL 215 215 215 VAL VAL C . n 
C 1 216 GLN 216 216 216 GLN GLN C . n 
C 1 217 ILE 217 217 217 ILE ILE C . n 
C 1 218 SER 218 218 218 SER SER C . n 
C 1 219 GLN 219 219 219 GLN GLN C . n 
C 1 220 GLU 220 220 220 GLU GLU C . n 
C 1 221 GLN 221 221 221 GLN GLN C . n 
C 1 222 LEU 222 222 222 LEU LEU C . n 
C 1 223 LEU 223 223 223 LEU LEU C . n 
C 1 224 ALA 224 224 224 ALA ALA C . n 
C 1 225 LEU 225 225 225 LEU LEU C . n 
C 1 226 GLU 226 226 226 GLU GLU C . n 
C 1 227 THR 227 227 227 THR THR C . n 
C 1 228 ALA 228 228 228 ALA ALA C . n 
C 1 229 LEU 229 229 229 LEU LEU C . n 
C 1 230 TYR 230 230 230 TYR TYR C . n 
C 1 231 CYS 231 231 231 CYS CYS C . n 
C 1 232 THR 232 232 232 THR THR C . n 
C 1 233 HIS 233 233 233 HIS HIS C . n 
C 1 234 MET 234 234 234 MET MET C . n 
C 1 235 ASP 235 235 235 ASP ASP C . n 
C 1 236 ASP 236 236 236 ASP ASP C . n 
C 1 237 PRO 237 237 237 PRO PRO C . n 
C 1 238 SER 238 238 238 SER SER C . n 
C 1 239 PRO 239 239 239 PRO PRO C . n 
C 1 240 ARG 240 240 240 ARG ARG C . n 
C 1 241 GLU 241 241 241 GLU GLU C . n 
C 1 242 MET 242 242 242 MET MET C . n 
C 1 243 ILE 243 243 243 ILE ILE C . n 
C 1 244 ASN 244 244 244 ASN ASN C . n 
C 1 245 ASN 245 245 245 ASN ASN C . n 
C 1 246 PHE 246 246 246 PHE PHE C . n 
C 1 247 ARG 247 247 247 ARG ARG C . n 
C 1 248 GLN 248 248 248 GLN GLN C . n 
C 1 249 VAL 249 249 249 VAL VAL C . n 
C 1 250 GLN 250 250 250 GLN GLN C . n 
C 1 251 LYS 251 251 251 LYS LYS C . n 
C 1 252 PHE 252 252 252 PHE PHE C . n 
C 1 253 ASP 253 253 253 ASP ASP C . n 
C 1 254 GLU 254 254 254 GLU GLU C . n 
C 1 255 ARG 255 255 255 ARG ARG C . n 
C 1 256 LEU 256 256 256 LEU LEU C . n 
C 1 257 VAL 257 257 257 VAL VAL C . n 
C 1 258 TYR 258 258 258 TYR TYR C . n 
C 1 259 THR 259 259 259 THR THR C . n 
C 1 260 SER 260 260 260 SER SER C . n 
C 1 261 PHE 261 261 261 PHE PHE C . n 
C 1 262 SER 262 262 262 SER SER C . n 
C 1 263 GLN 263 263 ?   ?   ?   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 1    ZN  ZN  A . 
F 3 E1F 1   302 1    E1F E18 A . 
G 4 EDO 1   303 1    EDO EDO A . 
H 4 EDO 1   304 6    EDO EDO A . 
I 2 ZN  1   301 2    ZN  ZN  B . 
J 3 E1F 1   302 2    E1F E18 B . 
K 4 EDO 1   303 2    EDO EDO B . 
L 4 EDO 1   304 4    EDO EDO B . 
M 2 ZN  1   301 3    ZN  ZN  C . 
N 3 E1F 1   302 3    E1F E18 C . 
O 5 SO4 1   303 1    SO4 SO4 C . 
P 2 ZN  1   301 4    ZN  ZN  D . 
Q 3 E1F 1   302 4    E1F E18 D . 
R 4 EDO 1   303 3    EDO EDO D . 
S 4 EDO 1   304 5    EDO EDO D . 
T 6 HOH 1   401 6    HOH HOH A . 
T 6 HOH 2   402 7    HOH HOH A . 
T 6 HOH 3   403 13   HOH HOH A . 
T 6 HOH 4   404 16   HOH HOH A . 
T 6 HOH 5   405 19   HOH HOH A . 
T 6 HOH 6   406 22   HOH HOH A . 
T 6 HOH 7   407 24   HOH HOH A . 
T 6 HOH 8   408 29   HOH HOH A . 
T 6 HOH 9   409 34   HOH HOH A . 
T 6 HOH 10  410 37   HOH HOH A . 
T 6 HOH 11  411 38   HOH HOH A . 
T 6 HOH 12  412 41   HOH HOH A . 
T 6 HOH 13  413 42   HOH HOH A . 
T 6 HOH 14  414 44   HOH HOH A . 
T 6 HOH 15  415 46   HOH HOH A . 
T 6 HOH 16  416 48   HOH HOH A . 
T 6 HOH 17  417 54   HOH HOH A . 
T 6 HOH 18  418 55   HOH HOH A . 
T 6 HOH 19  419 56   HOH HOH A . 
T 6 HOH 20  420 61   HOH HOH A . 
T 6 HOH 21  421 69   HOH HOH A . 
T 6 HOH 22  422 71   HOH HOH A . 
T 6 HOH 23  423 73   HOH HOH A . 
T 6 HOH 24  424 74   HOH HOH A . 
T 6 HOH 25  425 75   HOH HOH A . 
T 6 HOH 26  426 86   HOH HOH A . 
T 6 HOH 27  427 87   HOH HOH A . 
T 6 HOH 28  428 89   HOH HOH A . 
T 6 HOH 29  429 95   HOH HOH A . 
T 6 HOH 30  430 100  HOH HOH A . 
T 6 HOH 31  431 101  HOH HOH A . 
T 6 HOH 32  432 113  HOH HOH A . 
T 6 HOH 33  433 121  HOH HOH A . 
T 6 HOH 34  434 127  HOH HOH A . 
T 6 HOH 35  435 128  HOH HOH A . 
T 6 HOH 36  436 130  HOH HOH A . 
T 6 HOH 37  437 134  HOH HOH A . 
T 6 HOH 38  438 135  HOH HOH A . 
T 6 HOH 39  439 139  HOH HOH A . 
T 6 HOH 40  440 141  HOH HOH A . 
T 6 HOH 41  441 142  HOH HOH A . 
T 6 HOH 42  442 144  HOH HOH A . 
T 6 HOH 43  443 151  HOH HOH A . 
T 6 HOH 44  444 152  HOH HOH A . 
T 6 HOH 45  445 154  HOH HOH A . 
T 6 HOH 46  446 155  HOH HOH A . 
T 6 HOH 47  447 172  HOH HOH A . 
T 6 HOH 48  448 173  HOH HOH A . 
T 6 HOH 49  449 176  HOH HOH A . 
T 6 HOH 50  450 180  HOH HOH A . 
T 6 HOH 51  451 186  HOH HOH A . 
T 6 HOH 52  452 189  HOH HOH A . 
T 6 HOH 53  453 190  HOH HOH A . 
T 6 HOH 54  454 198  HOH HOH A . 
T 6 HOH 55  455 201  HOH HOH A . 
T 6 HOH 56  456 203  HOH HOH A . 
T 6 HOH 57  457 207  HOH HOH A . 
T 6 HOH 58  458 208  HOH HOH A . 
T 6 HOH 59  459 212  HOH HOH A . 
T 6 HOH 60  460 215  HOH HOH A . 
T 6 HOH 61  461 217  HOH HOH A . 
T 6 HOH 62  462 219  HOH HOH A . 
T 6 HOH 63  463 223  HOH HOH A . 
T 6 HOH 64  464 225  HOH HOH A . 
T 6 HOH 65  465 226  HOH HOH A . 
T 6 HOH 66  466 228  HOH HOH A . 
T 6 HOH 67  467 229  HOH HOH A . 
T 6 HOH 68  468 233  HOH HOH A . 
T 6 HOH 69  469 245  HOH HOH A . 
T 6 HOH 70  470 248  HOH HOH A . 
T 6 HOH 71  471 251  HOH HOH A . 
T 6 HOH 72  472 258  HOH HOH A . 
T 6 HOH 73  473 263  HOH HOH A . 
T 6 HOH 74  474 271  HOH HOH A . 
T 6 HOH 75  475 276  HOH HOH A . 
T 6 HOH 76  476 277  HOH HOH A . 
T 6 HOH 77  477 280  HOH HOH A . 
T 6 HOH 78  478 281  HOH HOH A . 
T 6 HOH 79  479 287  HOH HOH A . 
T 6 HOH 80  480 289  HOH HOH A . 
T 6 HOH 81  481 292  HOH HOH A . 
T 6 HOH 82  482 294  HOH HOH A . 
T 6 HOH 83  483 296  HOH HOH A . 
T 6 HOH 84  484 302  HOH HOH A . 
T 6 HOH 85  485 308  HOH HOH A . 
T 6 HOH 86  486 312  HOH HOH A . 
T 6 HOH 87  487 319  HOH HOH A . 
T 6 HOH 88  488 329  HOH HOH A . 
T 6 HOH 89  489 330  HOH HOH A . 
T 6 HOH 90  490 337  HOH HOH A . 
T 6 HOH 91  491 340  HOH HOH A . 
T 6 HOH 92  492 348  HOH HOH A . 
T 6 HOH 93  493 350  HOH HOH A . 
T 6 HOH 94  494 353  HOH HOH A . 
T 6 HOH 95  495 355  HOH HOH A . 
T 6 HOH 96  496 358  HOH HOH A . 
T 6 HOH 97  497 362  HOH HOH A . 
T 6 HOH 98  498 367  HOH HOH A . 
T 6 HOH 99  499 379  HOH HOH A . 
T 6 HOH 100 500 382  HOH HOH A . 
T 6 HOH 101 501 383  HOH HOH A . 
T 6 HOH 102 502 384  HOH HOH A . 
T 6 HOH 103 503 385  HOH HOH A . 
T 6 HOH 104 504 404  HOH HOH A . 
T 6 HOH 105 505 405  HOH HOH A . 
T 6 HOH 106 506 419  HOH HOH A . 
T 6 HOH 107 507 422  HOH HOH A . 
T 6 HOH 108 508 423  HOH HOH A . 
T 6 HOH 109 509 429  HOH HOH A . 
T 6 HOH 110 510 431  HOH HOH A . 
T 6 HOH 111 511 436  HOH HOH A . 
T 6 HOH 112 512 442  HOH HOH A . 
T 6 HOH 113 513 448  HOH HOH A . 
T 6 HOH 114 514 449  HOH HOH A . 
T 6 HOH 115 515 453  HOH HOH A . 
T 6 HOH 116 516 455  HOH HOH A . 
T 6 HOH 117 517 458  HOH HOH A . 
T 6 HOH 118 518 460  HOH HOH A . 
T 6 HOH 119 519 468  HOH HOH A . 
T 6 HOH 120 520 479  HOH HOH A . 
T 6 HOH 121 521 482  HOH HOH A . 
T 6 HOH 122 522 485  HOH HOH A . 
T 6 HOH 123 523 488  HOH HOH A . 
T 6 HOH 124 524 490  HOH HOH A . 
T 6 HOH 125 525 496  HOH HOH A . 
T 6 HOH 126 526 501  HOH HOH A . 
T 6 HOH 127 527 503  HOH HOH A . 
T 6 HOH 128 528 505  HOH HOH A . 
T 6 HOH 129 529 507  HOH HOH A . 
T 6 HOH 130 530 508  HOH HOH A . 
T 6 HOH 131 531 510  HOH HOH A . 
T 6 HOH 132 532 515  HOH HOH A . 
T 6 HOH 133 533 516  HOH HOH A . 
T 6 HOH 134 534 518  HOH HOH A . 
T 6 HOH 135 535 530  HOH HOH A . 
T 6 HOH 136 536 533  HOH HOH A . 
T 6 HOH 137 537 536  HOH HOH A . 
T 6 HOH 138 538 538  HOH HOH A . 
T 6 HOH 139 539 539  HOH HOH A . 
T 6 HOH 140 540 541  HOH HOH A . 
T 6 HOH 141 541 542  HOH HOH A . 
T 6 HOH 142 542 543  HOH HOH A . 
T 6 HOH 143 543 546  HOH HOH A . 
T 6 HOH 144 544 550  HOH HOH A . 
T 6 HOH 145 545 552  HOH HOH A . 
T 6 HOH 146 546 553  HOH HOH A . 
T 6 HOH 147 547 556  HOH HOH A . 
T 6 HOH 148 548 560  HOH HOH A . 
T 6 HOH 149 549 562  HOH HOH A . 
T 6 HOH 150 550 567  HOH HOH A . 
T 6 HOH 151 551 571  HOH HOH A . 
T 6 HOH 152 552 573  HOH HOH A . 
T 6 HOH 153 553 580  HOH HOH A . 
T 6 HOH 154 554 582  HOH HOH A . 
T 6 HOH 155 555 584  HOH HOH A . 
T 6 HOH 156 556 604  HOH HOH A . 
T 6 HOH 157 557 605  HOH HOH A . 
T 6 HOH 158 558 606  HOH HOH A . 
T 6 HOH 159 559 608  HOH HOH A . 
T 6 HOH 160 560 610  HOH HOH A . 
T 6 HOH 161 561 612  HOH HOH A . 
T 6 HOH 162 562 622  HOH HOH A . 
T 6 HOH 163 563 637  HOH HOH A . 
T 6 HOH 164 564 642  HOH HOH A . 
T 6 HOH 165 565 643  HOH HOH A . 
T 6 HOH 166 566 647  HOH HOH A . 
T 6 HOH 167 567 648  HOH HOH A . 
T 6 HOH 168 568 655  HOH HOH A . 
T 6 HOH 169 569 659  HOH HOH A . 
T 6 HOH 170 570 675  HOH HOH A . 
T 6 HOH 171 571 677  HOH HOH A . 
T 6 HOH 172 572 679  HOH HOH A . 
T 6 HOH 173 573 681  HOH HOH A . 
T 6 HOH 174 574 685  HOH HOH A . 
T 6 HOH 175 575 686  HOH HOH A . 
T 6 HOH 176 576 687  HOH HOH A . 
T 6 HOH 177 577 690  HOH HOH A . 
T 6 HOH 178 578 692  HOH HOH A . 
T 6 HOH 179 579 693  HOH HOH A . 
T 6 HOH 180 580 705  HOH HOH A . 
T 6 HOH 181 581 706  HOH HOH A . 
T 6 HOH 182 582 714  HOH HOH A . 
T 6 HOH 183 583 717  HOH HOH A . 
T 6 HOH 184 584 720  HOH HOH A . 
T 6 HOH 185 585 722  HOH HOH A . 
T 6 HOH 186 586 723  HOH HOH A . 
T 6 HOH 187 587 726  HOH HOH A . 
T 6 HOH 188 588 729  HOH HOH A . 
T 6 HOH 189 589 732  HOH HOH A . 
T 6 HOH 190 590 734  HOH HOH A . 
T 6 HOH 191 591 735  HOH HOH A . 
T 6 HOH 192 592 744  HOH HOH A . 
T 6 HOH 193 593 747  HOH HOH A . 
T 6 HOH 194 594 748  HOH HOH A . 
T 6 HOH 195 595 754  HOH HOH A . 
T 6 HOH 196 596 757  HOH HOH A . 
T 6 HOH 197 597 778  HOH HOH A . 
T 6 HOH 198 598 786  HOH HOH A . 
T 6 HOH 199 599 794  HOH HOH A . 
T 6 HOH 200 600 795  HOH HOH A . 
T 6 HOH 201 601 796  HOH HOH A . 
T 6 HOH 202 602 798  HOH HOH A . 
T 6 HOH 203 603 800  HOH HOH A . 
T 6 HOH 204 604 804  HOH HOH A . 
T 6 HOH 205 605 805  HOH HOH A . 
T 6 HOH 206 606 806  HOH HOH A . 
T 6 HOH 207 607 807  HOH HOH A . 
T 6 HOH 208 608 815  HOH HOH A . 
T 6 HOH 209 609 817  HOH HOH A . 
T 6 HOH 210 610 818  HOH HOH A . 
T 6 HOH 211 611 825  HOH HOH A . 
T 6 HOH 212 612 827  HOH HOH A . 
T 6 HOH 213 613 830  HOH HOH A . 
T 6 HOH 214 614 831  HOH HOH A . 
T 6 HOH 215 615 835  HOH HOH A . 
T 6 HOH 216 616 840  HOH HOH A . 
T 6 HOH 217 617 847  HOH HOH A . 
T 6 HOH 218 618 849  HOH HOH A . 
T 6 HOH 219 619 852  HOH HOH A . 
T 6 HOH 220 620 855  HOH HOH A . 
T 6 HOH 221 621 856  HOH HOH A . 
T 6 HOH 222 622 857  HOH HOH A . 
T 6 HOH 223 623 864  HOH HOH A . 
T 6 HOH 224 624 865  HOH HOH A . 
T 6 HOH 225 625 869  HOH HOH A . 
T 6 HOH 226 626 872  HOH HOH A . 
T 6 HOH 227 627 875  HOH HOH A . 
T 6 HOH 228 628 876  HOH HOH A . 
T 6 HOH 229 629 877  HOH HOH A . 
T 6 HOH 230 630 883  HOH HOH A . 
T 6 HOH 231 631 884  HOH HOH A . 
T 6 HOH 232 632 885  HOH HOH A . 
T 6 HOH 233 633 890  HOH HOH A . 
T 6 HOH 234 634 891  HOH HOH A . 
T 6 HOH 235 635 893  HOH HOH A . 
T 6 HOH 236 636 894  HOH HOH A . 
T 6 HOH 237 637 897  HOH HOH A . 
T 6 HOH 238 638 899  HOH HOH A . 
T 6 HOH 239 639 901  HOH HOH A . 
T 6 HOH 240 640 904  HOH HOH A . 
T 6 HOH 241 641 908  HOH HOH A . 
T 6 HOH 242 642 909  HOH HOH A . 
T 6 HOH 243 643 910  HOH HOH A . 
T 6 HOH 244 644 911  HOH HOH A . 
T 6 HOH 245 645 912  HOH HOH A . 
T 6 HOH 246 646 913  HOH HOH A . 
T 6 HOH 247 647 914  HOH HOH A . 
T 6 HOH 248 648 915  HOH HOH A . 
T 6 HOH 249 649 916  HOH HOH A . 
T 6 HOH 250 650 917  HOH HOH A . 
T 6 HOH 251 651 918  HOH HOH A . 
T 6 HOH 252 652 919  HOH HOH A . 
T 6 HOH 253 653 921  HOH HOH A . 
T 6 HOH 254 654 922  HOH HOH A . 
T 6 HOH 255 655 923  HOH HOH A . 
T 6 HOH 256 656 924  HOH HOH A . 
T 6 HOH 257 657 925  HOH HOH A . 
T 6 HOH 258 658 926  HOH HOH A . 
T 6 HOH 259 659 928  HOH HOH A . 
T 6 HOH 260 660 1000 HOH HOH A . 
T 6 HOH 261 661 1001 HOH HOH A . 
T 6 HOH 262 662 1002 HOH HOH A . 
T 6 HOH 263 663 1003 HOH HOH A . 
T 6 HOH 264 664 1004 HOH HOH A . 
T 6 HOH 265 665 1005 HOH HOH A . 
T 6 HOH 266 666 1006 HOH HOH A . 
T 6 HOH 267 667 1016 HOH HOH A . 
T 6 HOH 268 668 1017 HOH HOH A . 
T 6 HOH 269 669 1018 HOH HOH A . 
T 6 HOH 270 670 1019 HOH HOH A . 
T 6 HOH 271 671 1020 HOH HOH A . 
T 6 HOH 272 672 1021 HOH HOH A . 
T 6 HOH 273 673 1034 HOH HOH A . 
T 6 HOH 274 674 1038 HOH HOH A . 
T 6 HOH 275 675 1041 HOH HOH A . 
T 6 HOH 276 676 1045 HOH HOH A . 
T 6 HOH 277 677 1046 HOH HOH A . 
T 6 HOH 278 678 1047 HOH HOH A . 
T 6 HOH 279 679 1049 HOH HOH A . 
T 6 HOH 280 680 1051 HOH HOH A . 
T 6 HOH 281 681 1056 HOH HOH A . 
T 6 HOH 282 682 1068 HOH HOH A . 
T 6 HOH 283 683 1069 HOH HOH A . 
T 6 HOH 284 684 1071 HOH HOH A . 
T 6 HOH 285 685 1074 HOH HOH A . 
T 6 HOH 286 686 1075 HOH HOH A . 
T 6 HOH 287 687 1077 HOH HOH A . 
T 6 HOH 288 688 1079 HOH HOH A . 
T 6 HOH 289 689 1082 HOH HOH A . 
T 6 HOH 290 690 1084 HOH HOH A . 
T 6 HOH 291 691 1088 HOH HOH A . 
T 6 HOH 292 692 1091 HOH HOH A . 
T 6 HOH 293 693 1092 HOH HOH A . 
T 6 HOH 294 694 1094 HOH HOH A . 
T 6 HOH 295 695 1096 HOH HOH A . 
T 6 HOH 296 696 1101 HOH HOH A . 
T 6 HOH 297 697 1103 HOH HOH A . 
T 6 HOH 298 698 1107 HOH HOH A . 
T 6 HOH 299 699 1110 HOH HOH A . 
T 6 HOH 300 700 1111 HOH HOH A . 
T 6 HOH 301 701 1115 HOH HOH A . 
T 6 HOH 302 702 1119 HOH HOH A . 
T 6 HOH 303 703 1124 HOH HOH A . 
T 6 HOH 304 704 1127 HOH HOH A . 
T 6 HOH 305 705 1128 HOH HOH A . 
T 6 HOH 306 706 1132 HOH HOH A . 
T 6 HOH 307 707 1139 HOH HOH A . 
T 6 HOH 308 708 1143 HOH HOH A . 
T 6 HOH 309 709 1144 HOH HOH A . 
T 6 HOH 310 710 1146 HOH HOH A . 
T 6 HOH 311 711 1147 HOH HOH A . 
T 6 HOH 312 712 1148 HOH HOH A . 
T 6 HOH 313 713 1149 HOH HOH A . 
T 6 HOH 314 714 1150 HOH HOH A . 
T 6 HOH 315 715 1151 HOH HOH A . 
T 6 HOH 316 716 1152 HOH HOH A . 
T 6 HOH 317 717 1153 HOH HOH A . 
T 6 HOH 318 718 1154 HOH HOH A . 
T 6 HOH 319 719 1155 HOH HOH A . 
T 6 HOH 320 720 1157 HOH HOH A . 
T 6 HOH 321 721 1187 HOH HOH A . 
T 6 HOH 322 722 1188 HOH HOH A . 
T 6 HOH 323 723 1190 HOH HOH A . 
T 6 HOH 324 724 1191 HOH HOH A . 
T 6 HOH 325 725 1192 HOH HOH A . 
T 6 HOH 326 726 93   HOH HOH A . 
T 6 HOH 327 727 346  HOH HOH A . 
T 6 HOH 328 728 1099 HOH HOH A . 
U 6 HOH 1   401 1145 HOH HOH B . 
U 6 HOH 2   402 1    HOH HOH B . 
U 6 HOH 3   403 3    HOH HOH B . 
U 6 HOH 4   404 4    HOH HOH B . 
U 6 HOH 5   405 14   HOH HOH B . 
U 6 HOH 6   406 17   HOH HOH B . 
U 6 HOH 7   407 20   HOH HOH B . 
U 6 HOH 8   408 28   HOH HOH B . 
U 6 HOH 9   409 33   HOH HOH B . 
U 6 HOH 10  410 39   HOH HOH B . 
U 6 HOH 11  411 47   HOH HOH B . 
U 6 HOH 12  412 50   HOH HOH B . 
U 6 HOH 13  413 57   HOH HOH B . 
U 6 HOH 14  414 59   HOH HOH B . 
U 6 HOH 15  415 64   HOH HOH B . 
U 6 HOH 16  416 65   HOH HOH B . 
U 6 HOH 17  417 66   HOH HOH B . 
U 6 HOH 18  418 70   HOH HOH B . 
U 6 HOH 19  419 78   HOH HOH B . 
U 6 HOH 20  420 79   HOH HOH B . 
U 6 HOH 21  421 80   HOH HOH B . 
U 6 HOH 22  422 83   HOH HOH B . 
U 6 HOH 23  423 84   HOH HOH B . 
U 6 HOH 24  424 85   HOH HOH B . 
U 6 HOH 25  425 94   HOH HOH B . 
U 6 HOH 26  426 97   HOH HOH B . 
U 6 HOH 27  427 98   HOH HOH B . 
U 6 HOH 28  428 99   HOH HOH B . 
U 6 HOH 29  429 102  HOH HOH B . 
U 6 HOH 30  430 104  HOH HOH B . 
U 6 HOH 31  431 106  HOH HOH B . 
U 6 HOH 32  432 107  HOH HOH B . 
U 6 HOH 33  433 114  HOH HOH B . 
U 6 HOH 34  434 118  HOH HOH B . 
U 6 HOH 35  435 119  HOH HOH B . 
U 6 HOH 36  436 126  HOH HOH B . 
U 6 HOH 37  437 129  HOH HOH B . 
U 6 HOH 38  438 131  HOH HOH B . 
U 6 HOH 39  439 133  HOH HOH B . 
U 6 HOH 40  440 137  HOH HOH B . 
U 6 HOH 41  441 140  HOH HOH B . 
U 6 HOH 42  442 145  HOH HOH B . 
U 6 HOH 43  443 146  HOH HOH B . 
U 6 HOH 44  444 147  HOH HOH B . 
U 6 HOH 45  445 153  HOH HOH B . 
U 6 HOH 46  446 162  HOH HOH B . 
U 6 HOH 47  447 163  HOH HOH B . 
U 6 HOH 48  448 164  HOH HOH B . 
U 6 HOH 49  449 170  HOH HOH B . 
U 6 HOH 50  450 174  HOH HOH B . 
U 6 HOH 51  451 175  HOH HOH B . 
U 6 HOH 52  452 177  HOH HOH B . 
U 6 HOH 53  453 178  HOH HOH B . 
U 6 HOH 54  454 179  HOH HOH B . 
U 6 HOH 55  455 182  HOH HOH B . 
U 6 HOH 56  456 184  HOH HOH B . 
U 6 HOH 57  457 191  HOH HOH B . 
U 6 HOH 58  458 192  HOH HOH B . 
U 6 HOH 59  459 196  HOH HOH B . 
U 6 HOH 60  460 197  HOH HOH B . 
U 6 HOH 61  461 200  HOH HOH B . 
U 6 HOH 62  462 202  HOH HOH B . 
U 6 HOH 63  463 205  HOH HOH B . 
U 6 HOH 64  464 209  HOH HOH B . 
U 6 HOH 65  465 218  HOH HOH B . 
U 6 HOH 66  466 224  HOH HOH B . 
U 6 HOH 67  467 230  HOH HOH B . 
U 6 HOH 68  468 234  HOH HOH B . 
U 6 HOH 69  469 236  HOH HOH B . 
U 6 HOH 70  470 237  HOH HOH B . 
U 6 HOH 71  471 239  HOH HOH B . 
U 6 HOH 72  472 240  HOH HOH B . 
U 6 HOH 73  473 244  HOH HOH B . 
U 6 HOH 74  474 247  HOH HOH B . 
U 6 HOH 75  475 255  HOH HOH B . 
U 6 HOH 76  476 257  HOH HOH B . 
U 6 HOH 77  477 259  HOH HOH B . 
U 6 HOH 78  478 264  HOH HOH B . 
U 6 HOH 79  479 266  HOH HOH B . 
U 6 HOH 80  480 267  HOH HOH B . 
U 6 HOH 81  481 269  HOH HOH B . 
U 6 HOH 82  482 270  HOH HOH B . 
U 6 HOH 83  483 275  HOH HOH B . 
U 6 HOH 84  484 278  HOH HOH B . 
U 6 HOH 85  485 279  HOH HOH B . 
U 6 HOH 86  486 282  HOH HOH B . 
U 6 HOH 87  487 291  HOH HOH B . 
U 6 HOH 88  488 293  HOH HOH B . 
U 6 HOH 89  489 299  HOH HOH B . 
U 6 HOH 90  490 300  HOH HOH B . 
U 6 HOH 91  491 303  HOH HOH B . 
U 6 HOH 92  492 305  HOH HOH B . 
U 6 HOH 93  493 306  HOH HOH B . 
U 6 HOH 94  494 310  HOH HOH B . 
U 6 HOH 95  495 313  HOH HOH B . 
U 6 HOH 96  496 315  HOH HOH B . 
U 6 HOH 97  497 316  HOH HOH B . 
U 6 HOH 98  498 322  HOH HOH B . 
U 6 HOH 99  499 324  HOH HOH B . 
U 6 HOH 100 500 328  HOH HOH B . 
U 6 HOH 101 501 331  HOH HOH B . 
U 6 HOH 102 502 332  HOH HOH B . 
U 6 HOH 103 503 336  HOH HOH B . 
U 6 HOH 104 504 342  HOH HOH B . 
U 6 HOH 105 505 345  HOH HOH B . 
U 6 HOH 106 506 347  HOH HOH B . 
U 6 HOH 107 507 351  HOH HOH B . 
U 6 HOH 108 508 352  HOH HOH B . 
U 6 HOH 109 509 357  HOH HOH B . 
U 6 HOH 110 510 361  HOH HOH B . 
U 6 HOH 111 511 363  HOH HOH B . 
U 6 HOH 112 512 368  HOH HOH B . 
U 6 HOH 113 513 369  HOH HOH B . 
U 6 HOH 114 514 370  HOH HOH B . 
U 6 HOH 115 515 371  HOH HOH B . 
U 6 HOH 116 516 373  HOH HOH B . 
U 6 HOH 117 517 374  HOH HOH B . 
U 6 HOH 118 518 377  HOH HOH B . 
U 6 HOH 119 519 394  HOH HOH B . 
U 6 HOH 120 520 395  HOH HOH B . 
U 6 HOH 121 521 397  HOH HOH B . 
U 6 HOH 122 522 403  HOH HOH B . 
U 6 HOH 123 523 406  HOH HOH B . 
U 6 HOH 124 524 410  HOH HOH B . 
U 6 HOH 125 525 413  HOH HOH B . 
U 6 HOH 126 526 415  HOH HOH B . 
U 6 HOH 127 527 418  HOH HOH B . 
U 6 HOH 128 528 427  HOH HOH B . 
U 6 HOH 129 529 430  HOH HOH B . 
U 6 HOH 130 530 432  HOH HOH B . 
U 6 HOH 131 531 433  HOH HOH B . 
U 6 HOH 132 532 437  HOH HOH B . 
U 6 HOH 133 533 438  HOH HOH B . 
U 6 HOH 134 534 439  HOH HOH B . 
U 6 HOH 135 535 441  HOH HOH B . 
U 6 HOH 136 536 444  HOH HOH B . 
U 6 HOH 137 537 445  HOH HOH B . 
U 6 HOH 138 538 457  HOH HOH B . 
U 6 HOH 139 539 470  HOH HOH B . 
U 6 HOH 140 540 475  HOH HOH B . 
U 6 HOH 141 541 477  HOH HOH B . 
U 6 HOH 142 542 483  HOH HOH B . 
U 6 HOH 143 543 491  HOH HOH B . 
U 6 HOH 144 544 495  HOH HOH B . 
U 6 HOH 145 545 506  HOH HOH B . 
U 6 HOH 146 546 512  HOH HOH B . 
U 6 HOH 147 547 514  HOH HOH B . 
U 6 HOH 148 548 522  HOH HOH B . 
U 6 HOH 149 549 524  HOH HOH B . 
U 6 HOH 150 550 527  HOH HOH B . 
U 6 HOH 151 551 528  HOH HOH B . 
U 6 HOH 152 552 531  HOH HOH B . 
U 6 HOH 153 553 532  HOH HOH B . 
U 6 HOH 154 554 537  HOH HOH B . 
U 6 HOH 155 555 544  HOH HOH B . 
U 6 HOH 156 556 557  HOH HOH B . 
U 6 HOH 157 557 563  HOH HOH B . 
U 6 HOH 158 558 566  HOH HOH B . 
U 6 HOH 159 559 569  HOH HOH B . 
U 6 HOH 160 560 577  HOH HOH B . 
U 6 HOH 161 561 586  HOH HOH B . 
U 6 HOH 162 562 587  HOH HOH B . 
U 6 HOH 163 563 594  HOH HOH B . 
U 6 HOH 164 564 595  HOH HOH B . 
U 6 HOH 165 565 596  HOH HOH B . 
U 6 HOH 166 566 597  HOH HOH B . 
U 6 HOH 167 567 598  HOH HOH B . 
U 6 HOH 168 568 602  HOH HOH B . 
U 6 HOH 169 569 607  HOH HOH B . 
U 6 HOH 170 570 609  HOH HOH B . 
U 6 HOH 171 571 611  HOH HOH B . 
U 6 HOH 172 572 614  HOH HOH B . 
U 6 HOH 173 573 615  HOH HOH B . 
U 6 HOH 174 574 618  HOH HOH B . 
U 6 HOH 175 575 620  HOH HOH B . 
U 6 HOH 176 576 624  HOH HOH B . 
U 6 HOH 177 577 625  HOH HOH B . 
U 6 HOH 178 578 626  HOH HOH B . 
U 6 HOH 179 579 629  HOH HOH B . 
U 6 HOH 180 580 632  HOH HOH B . 
U 6 HOH 181 581 633  HOH HOH B . 
U 6 HOH 182 582 634  HOH HOH B . 
U 6 HOH 183 583 635  HOH HOH B . 
U 6 HOH 184 584 640  HOH HOH B . 
U 6 HOH 185 585 644  HOH HOH B . 
U 6 HOH 186 586 645  HOH HOH B . 
U 6 HOH 187 587 652  HOH HOH B . 
U 6 HOH 188 588 653  HOH HOH B . 
U 6 HOH 189 589 656  HOH HOH B . 
U 6 HOH 190 590 660  HOH HOH B . 
U 6 HOH 191 591 664  HOH HOH B . 
U 6 HOH 192 592 665  HOH HOH B . 
U 6 HOH 193 593 670  HOH HOH B . 
U 6 HOH 194 594 671  HOH HOH B . 
U 6 HOH 195 595 672  HOH HOH B . 
U 6 HOH 196 596 673  HOH HOH B . 
U 6 HOH 197 597 676  HOH HOH B . 
U 6 HOH 198 598 680  HOH HOH B . 
U 6 HOH 199 599 682  HOH HOH B . 
U 6 HOH 200 600 683  HOH HOH B . 
U 6 HOH 201 601 684  HOH HOH B . 
U 6 HOH 202 602 691  HOH HOH B . 
U 6 HOH 203 603 696  HOH HOH B . 
U 6 HOH 204 604 700  HOH HOH B . 
U 6 HOH 205 605 704  HOH HOH B . 
U 6 HOH 206 606 709  HOH HOH B . 
U 6 HOH 207 607 711  HOH HOH B . 
U 6 HOH 208 608 712  HOH HOH B . 
U 6 HOH 209 609 716  HOH HOH B . 
U 6 HOH 210 610 719  HOH HOH B . 
U 6 HOH 211 611 728  HOH HOH B . 
U 6 HOH 212 612 731  HOH HOH B . 
U 6 HOH 213 613 733  HOH HOH B . 
U 6 HOH 214 614 742  HOH HOH B . 
U 6 HOH 215 615 743  HOH HOH B . 
U 6 HOH 216 616 745  HOH HOH B . 
U 6 HOH 217 617 752  HOH HOH B . 
U 6 HOH 218 618 763  HOH HOH B . 
U 6 HOH 219 619 764  HOH HOH B . 
U 6 HOH 220 620 772  HOH HOH B . 
U 6 HOH 221 621 773  HOH HOH B . 
U 6 HOH 222 622 774  HOH HOH B . 
U 6 HOH 223 623 779  HOH HOH B . 
U 6 HOH 224 624 781  HOH HOH B . 
U 6 HOH 225 625 789  HOH HOH B . 
U 6 HOH 226 626 791  HOH HOH B . 
U 6 HOH 227 627 793  HOH HOH B . 
U 6 HOH 228 628 797  HOH HOH B . 
U 6 HOH 229 629 802  HOH HOH B . 
U 6 HOH 230 630 803  HOH HOH B . 
U 6 HOH 231 631 810  HOH HOH B . 
U 6 HOH 232 632 812  HOH HOH B . 
U 6 HOH 233 633 813  HOH HOH B . 
U 6 HOH 234 634 814  HOH HOH B . 
U 6 HOH 235 635 821  HOH HOH B . 
U 6 HOH 236 636 832  HOH HOH B . 
U 6 HOH 237 637 833  HOH HOH B . 
U 6 HOH 238 638 834  HOH HOH B . 
U 6 HOH 239 639 837  HOH HOH B . 
U 6 HOH 240 640 839  HOH HOH B . 
U 6 HOH 241 641 841  HOH HOH B . 
U 6 HOH 242 642 843  HOH HOH B . 
U 6 HOH 243 643 844  HOH HOH B . 
U 6 HOH 244 644 848  HOH HOH B . 
U 6 HOH 245 645 858  HOH HOH B . 
U 6 HOH 246 646 859  HOH HOH B . 
U 6 HOH 247 647 860  HOH HOH B . 
U 6 HOH 248 648 861  HOH HOH B . 
U 6 HOH 249 649 862  HOH HOH B . 
U 6 HOH 250 650 866  HOH HOH B . 
U 6 HOH 251 651 868  HOH HOH B . 
U 6 HOH 252 652 870  HOH HOH B . 
U 6 HOH 253 653 873  HOH HOH B . 
U 6 HOH 254 654 878  HOH HOH B . 
U 6 HOH 255 655 880  HOH HOH B . 
U 6 HOH 256 656 888  HOH HOH B . 
U 6 HOH 257 657 892  HOH HOH B . 
U 6 HOH 258 658 896  HOH HOH B . 
U 6 HOH 259 659 898  HOH HOH B . 
U 6 HOH 260 660 903  HOH HOH B . 
U 6 HOH 261 661 907  HOH HOH B . 
U 6 HOH 262 662 920  HOH HOH B . 
U 6 HOH 263 663 927  HOH HOH B . 
U 6 HOH 264 664 929  HOH HOH B . 
U 6 HOH 265 665 930  HOH HOH B . 
U 6 HOH 266 666 931  HOH HOH B . 
U 6 HOH 267 667 932  HOH HOH B . 
U 6 HOH 268 668 933  HOH HOH B . 
U 6 HOH 269 669 934  HOH HOH B . 
U 6 HOH 270 670 935  HOH HOH B . 
U 6 HOH 271 671 936  HOH HOH B . 
U 6 HOH 272 672 937  HOH HOH B . 
U 6 HOH 273 673 938  HOH HOH B . 
U 6 HOH 274 674 939  HOH HOH B . 
U 6 HOH 275 675 940  HOH HOH B . 
U 6 HOH 276 676 941  HOH HOH B . 
U 6 HOH 277 677 942  HOH HOH B . 
U 6 HOH 278 678 943  HOH HOH B . 
U 6 HOH 279 679 1007 HOH HOH B . 
U 6 HOH 280 680 1008 HOH HOH B . 
U 6 HOH 281 681 1009 HOH HOH B . 
U 6 HOH 282 682 1010 HOH HOH B . 
U 6 HOH 283 683 1022 HOH HOH B . 
U 6 HOH 284 684 1023 HOH HOH B . 
U 6 HOH 285 685 1039 HOH HOH B . 
U 6 HOH 286 686 1044 HOH HOH B . 
U 6 HOH 287 687 1048 HOH HOH B . 
U 6 HOH 288 688 1050 HOH HOH B . 
U 6 HOH 289 689 1052 HOH HOH B . 
U 6 HOH 290 690 1053 HOH HOH B . 
U 6 HOH 291 691 1057 HOH HOH B . 
U 6 HOH 292 692 1058 HOH HOH B . 
U 6 HOH 293 693 1059 HOH HOH B . 
U 6 HOH 294 694 1065 HOH HOH B . 
U 6 HOH 295 695 1076 HOH HOH B . 
U 6 HOH 296 696 1080 HOH HOH B . 
U 6 HOH 297 697 1083 HOH HOH B . 
U 6 HOH 298 698 1100 HOH HOH B . 
U 6 HOH 299 699 1102 HOH HOH B . 
U 6 HOH 300 700 1106 HOH HOH B . 
U 6 HOH 301 701 1113 HOH HOH B . 
U 6 HOH 302 702 1116 HOH HOH B . 
U 6 HOH 303 703 1117 HOH HOH B . 
U 6 HOH 304 704 1118 HOH HOH B . 
U 6 HOH 305 705 1120 HOH HOH B . 
U 6 HOH 306 706 1125 HOH HOH B . 
U 6 HOH 307 707 1126 HOH HOH B . 
U 6 HOH 308 708 1130 HOH HOH B . 
U 6 HOH 309 709 1131 HOH HOH B . 
U 6 HOH 310 710 1134 HOH HOH B . 
U 6 HOH 311 711 1137 HOH HOH B . 
U 6 HOH 312 712 1140 HOH HOH B . 
U 6 HOH 313 713 1141 HOH HOH B . 
U 6 HOH 314 714 1156 HOH HOH B . 
U 6 HOH 315 715 1158 HOH HOH B . 
U 6 HOH 316 716 1159 HOH HOH B . 
U 6 HOH 317 717 1160 HOH HOH B . 
U 6 HOH 318 718 1161 HOH HOH B . 
U 6 HOH 319 719 1162 HOH HOH B . 
U 6 HOH 320 720 1163 HOH HOH B . 
U 6 HOH 321 721 1164 HOH HOH B . 
U 6 HOH 322 722 1165 HOH HOH B . 
U 6 HOH 323 723 1166 HOH HOH B . 
U 6 HOH 324 724 1168 HOH HOH B . 
U 6 HOH 325 725 1189 HOH HOH B . 
U 6 HOH 326 726 1193 HOH HOH B . 
U 6 HOH 327 727 1194 HOH HOH B . 
U 6 HOH 328 728 1195 HOH HOH B . 
U 6 HOH 329 729 1196 HOH HOH B . 
U 6 HOH 330 730 1205 HOH HOH B . 
U 6 HOH 331 731 1206 HOH HOH B . 
V 6 HOH 1   401 10   HOH HOH C . 
V 6 HOH 2   402 15   HOH HOH C . 
V 6 HOH 3   403 18   HOH HOH C . 
V 6 HOH 4   404 25   HOH HOH C . 
V 6 HOH 5   405 27   HOH HOH C . 
V 6 HOH 6   406 31   HOH HOH C . 
V 6 HOH 7   407 32   HOH HOH C . 
V 6 HOH 8   408 49   HOH HOH C . 
V 6 HOH 9   409 51   HOH HOH C . 
V 6 HOH 10  410 52   HOH HOH C . 
V 6 HOH 11  411 53   HOH HOH C . 
V 6 HOH 12  412 58   HOH HOH C . 
V 6 HOH 13  413 67   HOH HOH C . 
V 6 HOH 14  414 77   HOH HOH C . 
V 6 HOH 15  415 82   HOH HOH C . 
V 6 HOH 16  416 96   HOH HOH C . 
V 6 HOH 17  417 105  HOH HOH C . 
V 6 HOH 18  418 110  HOH HOH C . 
V 6 HOH 19  419 111  HOH HOH C . 
V 6 HOH 20  420 124  HOH HOH C . 
V 6 HOH 21  421 132  HOH HOH C . 
V 6 HOH 22  422 148  HOH HOH C . 
V 6 HOH 23  423 156  HOH HOH C . 
V 6 HOH 24  424 158  HOH HOH C . 
V 6 HOH 25  425 159  HOH HOH C . 
V 6 HOH 26  426 165  HOH HOH C . 
V 6 HOH 27  427 166  HOH HOH C . 
V 6 HOH 28  428 181  HOH HOH C . 
V 6 HOH 29  429 185  HOH HOH C . 
V 6 HOH 30  430 204  HOH HOH C . 
V 6 HOH 31  431 206  HOH HOH C . 
V 6 HOH 32  432 211  HOH HOH C . 
V 6 HOH 33  433 213  HOH HOH C . 
V 6 HOH 34  434 220  HOH HOH C . 
V 6 HOH 35  435 221  HOH HOH C . 
V 6 HOH 36  436 232  HOH HOH C . 
V 6 HOH 37  437 238  HOH HOH C . 
V 6 HOH 38  438 241  HOH HOH C . 
V 6 HOH 39  439 249  HOH HOH C . 
V 6 HOH 40  440 250  HOH HOH C . 
V 6 HOH 41  441 252  HOH HOH C . 
V 6 HOH 42  442 253  HOH HOH C . 
V 6 HOH 43  443 268  HOH HOH C . 
V 6 HOH 44  444 272  HOH HOH C . 
V 6 HOH 45  445 283  HOH HOH C . 
V 6 HOH 46  446 284  HOH HOH C . 
V 6 HOH 47  447 290  HOH HOH C . 
V 6 HOH 48  448 297  HOH HOH C . 
V 6 HOH 49  449 309  HOH HOH C . 
V 6 HOH 50  450 314  HOH HOH C . 
V 6 HOH 51  451 320  HOH HOH C . 
V 6 HOH 52  452 323  HOH HOH C . 
V 6 HOH 53  453 334  HOH HOH C . 
V 6 HOH 54  454 338  HOH HOH C . 
V 6 HOH 55  455 339  HOH HOH C . 
V 6 HOH 56  456 343  HOH HOH C . 
V 6 HOH 57  457 349  HOH HOH C . 
V 6 HOH 58  458 360  HOH HOH C . 
V 6 HOH 59  459 366  HOH HOH C . 
V 6 HOH 60  460 372  HOH HOH C . 
V 6 HOH 61  461 386  HOH HOH C . 
V 6 HOH 62  462 388  HOH HOH C . 
V 6 HOH 63  463 391  HOH HOH C . 
V 6 HOH 64  464 396  HOH HOH C . 
V 6 HOH 65  465 398  HOH HOH C . 
V 6 HOH 66  466 400  HOH HOH C . 
V 6 HOH 67  467 401  HOH HOH C . 
V 6 HOH 68  468 408  HOH HOH C . 
V 6 HOH 69  469 409  HOH HOH C . 
V 6 HOH 70  470 416  HOH HOH C . 
V 6 HOH 71  471 435  HOH HOH C . 
V 6 HOH 72  472 446  HOH HOH C . 
V 6 HOH 73  473 451  HOH HOH C . 
V 6 HOH 74  474 452  HOH HOH C . 
V 6 HOH 75  475 454  HOH HOH C . 
V 6 HOH 76  476 461  HOH HOH C . 
V 6 HOH 77  477 462  HOH HOH C . 
V 6 HOH 78  478 463  HOH HOH C . 
V 6 HOH 79  479 466  HOH HOH C . 
V 6 HOH 80  480 471  HOH HOH C . 
V 6 HOH 81  481 472  HOH HOH C . 
V 6 HOH 82  482 474  HOH HOH C . 
V 6 HOH 83  483 478  HOH HOH C . 
V 6 HOH 84  484 487  HOH HOH C . 
V 6 HOH 85  485 494  HOH HOH C . 
V 6 HOH 86  486 498  HOH HOH C . 
V 6 HOH 87  487 499  HOH HOH C . 
V 6 HOH 88  488 509  HOH HOH C . 
V 6 HOH 89  489 511  HOH HOH C . 
V 6 HOH 90  490 513  HOH HOH C . 
V 6 HOH 91  491 517  HOH HOH C . 
V 6 HOH 92  492 523  HOH HOH C . 
V 6 HOH 93  493 534  HOH HOH C . 
V 6 HOH 94  494 554  HOH HOH C . 
V 6 HOH 95  495 558  HOH HOH C . 
V 6 HOH 96  496 559  HOH HOH C . 
V 6 HOH 97  497 564  HOH HOH C . 
V 6 HOH 98  498 565  HOH HOH C . 
V 6 HOH 99  499 570  HOH HOH C . 
V 6 HOH 100 500 572  HOH HOH C . 
V 6 HOH 101 501 575  HOH HOH C . 
V 6 HOH 102 502 585  HOH HOH C . 
V 6 HOH 103 503 590  HOH HOH C . 
V 6 HOH 104 504 591  HOH HOH C . 
V 6 HOH 105 505 601  HOH HOH C . 
V 6 HOH 106 506 621  HOH HOH C . 
V 6 HOH 107 507 630  HOH HOH C . 
V 6 HOH 108 508 638  HOH HOH C . 
V 6 HOH 109 509 639  HOH HOH C . 
V 6 HOH 110 510 667  HOH HOH C . 
V 6 HOH 111 511 674  HOH HOH C . 
V 6 HOH 112 512 695  HOH HOH C . 
V 6 HOH 113 513 697  HOH HOH C . 
V 6 HOH 114 514 698  HOH HOH C . 
V 6 HOH 115 515 702  HOH HOH C . 
V 6 HOH 116 516 708  HOH HOH C . 
V 6 HOH 117 517 710  HOH HOH C . 
V 6 HOH 118 518 713  HOH HOH C . 
V 6 HOH 119 519 718  HOH HOH C . 
V 6 HOH 120 520 736  HOH HOH C . 
V 6 HOH 121 521 739  HOH HOH C . 
V 6 HOH 122 522 749  HOH HOH C . 
V 6 HOH 123 523 755  HOH HOH C . 
V 6 HOH 124 524 758  HOH HOH C . 
V 6 HOH 125 525 759  HOH HOH C . 
V 6 HOH 126 526 761  HOH HOH C . 
V 6 HOH 127 527 762  HOH HOH C . 
V 6 HOH 128 528 768  HOH HOH C . 
V 6 HOH 129 529 769  HOH HOH C . 
V 6 HOH 130 530 770  HOH HOH C . 
V 6 HOH 131 531 777  HOH HOH C . 
V 6 HOH 132 532 780  HOH HOH C . 
V 6 HOH 133 533 782  HOH HOH C . 
V 6 HOH 134 534 787  HOH HOH C . 
V 6 HOH 135 535 792  HOH HOH C . 
V 6 HOH 136 536 799  HOH HOH C . 
V 6 HOH 137 537 801  HOH HOH C . 
V 6 HOH 138 538 811  HOH HOH C . 
V 6 HOH 139 539 816  HOH HOH C . 
V 6 HOH 140 540 819  HOH HOH C . 
V 6 HOH 141 541 820  HOH HOH C . 
V 6 HOH 142 542 829  HOH HOH C . 
V 6 HOH 143 543 845  HOH HOH C . 
V 6 HOH 144 544 850  HOH HOH C . 
V 6 HOH 145 545 853  HOH HOH C . 
V 6 HOH 146 546 871  HOH HOH C . 
V 6 HOH 147 547 874  HOH HOH C . 
V 6 HOH 148 548 889  HOH HOH C . 
V 6 HOH 149 549 905  HOH HOH C . 
V 6 HOH 150 550 906  HOH HOH C . 
V 6 HOH 151 551 944  HOH HOH C . 
V 6 HOH 152 552 945  HOH HOH C . 
V 6 HOH 153 553 946  HOH HOH C . 
V 6 HOH 154 554 947  HOH HOH C . 
V 6 HOH 155 555 948  HOH HOH C . 
V 6 HOH 156 556 949  HOH HOH C . 
V 6 HOH 157 557 950  HOH HOH C . 
V 6 HOH 158 558 951  HOH HOH C . 
V 6 HOH 159 559 952  HOH HOH C . 
V 6 HOH 160 560 953  HOH HOH C . 
V 6 HOH 161 561 954  HOH HOH C . 
V 6 HOH 162 562 955  HOH HOH C . 
V 6 HOH 163 563 956  HOH HOH C . 
V 6 HOH 164 564 957  HOH HOH C . 
V 6 HOH 165 565 960  HOH HOH C . 
V 6 HOH 166 566 961  HOH HOH C . 
V 6 HOH 167 567 962  HOH HOH C . 
V 6 HOH 168 568 963  HOH HOH C . 
V 6 HOH 169 569 964  HOH HOH C . 
V 6 HOH 170 570 965  HOH HOH C . 
V 6 HOH 171 571 966  HOH HOH C . 
V 6 HOH 172 572 967  HOH HOH C . 
V 6 HOH 173 573 968  HOH HOH C . 
V 6 HOH 174 574 969  HOH HOH C . 
V 6 HOH 175 575 970  HOH HOH C . 
V 6 HOH 176 576 971  HOH HOH C . 
V 6 HOH 177 577 972  HOH HOH C . 
V 6 HOH 178 578 973  HOH HOH C . 
V 6 HOH 179 579 974  HOH HOH C . 
V 6 HOH 180 580 979  HOH HOH C . 
V 6 HOH 181 581 1011 HOH HOH C . 
V 6 HOH 182 582 1012 HOH HOH C . 
V 6 HOH 183 583 1013 HOH HOH C . 
V 6 HOH 184 584 1014 HOH HOH C . 
V 6 HOH 185 585 1015 HOH HOH C . 
V 6 HOH 186 586 1028 HOH HOH C . 
V 6 HOH 187 587 1029 HOH HOH C . 
V 6 HOH 188 588 1030 HOH HOH C . 
V 6 HOH 189 589 1031 HOH HOH C . 
V 6 HOH 190 590 1032 HOH HOH C . 
V 6 HOH 191 591 1033 HOH HOH C . 
V 6 HOH 192 592 1035 HOH HOH C . 
V 6 HOH 193 593 1037 HOH HOH C . 
V 6 HOH 194 594 1043 HOH HOH C . 
V 6 HOH 195 595 1055 HOH HOH C . 
V 6 HOH 196 596 1062 HOH HOH C . 
V 6 HOH 197 597 1063 HOH HOH C . 
V 6 HOH 198 598 1064 HOH HOH C . 
V 6 HOH 199 599 1066 HOH HOH C . 
V 6 HOH 200 600 1070 HOH HOH C . 
V 6 HOH 201 601 1072 HOH HOH C . 
V 6 HOH 202 602 1073 HOH HOH C . 
V 6 HOH 203 603 1085 HOH HOH C . 
V 6 HOH 204 604 1090 HOH HOH C . 
V 6 HOH 205 605 1093 HOH HOH C . 
V 6 HOH 206 606 1095 HOH HOH C . 
V 6 HOH 207 607 1098 HOH HOH C . 
V 6 HOH 208 608 1104 HOH HOH C . 
V 6 HOH 209 609 1129 HOH HOH C . 
V 6 HOH 210 610 1138 HOH HOH C . 
V 6 HOH 211 611 1169 HOH HOH C . 
V 6 HOH 212 612 1170 HOH HOH C . 
V 6 HOH 213 613 1171 HOH HOH C . 
V 6 HOH 214 614 1172 HOH HOH C . 
V 6 HOH 215 615 1173 HOH HOH C . 
V 6 HOH 216 616 1174 HOH HOH C . 
V 6 HOH 217 617 1175 HOH HOH C . 
V 6 HOH 218 618 1176 HOH HOH C . 
V 6 HOH 219 619 1177 HOH HOH C . 
V 6 HOH 220 620 1178 HOH HOH C . 
V 6 HOH 221 621 1179 HOH HOH C . 
V 6 HOH 222 622 1197 HOH HOH C . 
V 6 HOH 223 623 1198 HOH HOH C . 
V 6 HOH 224 624 1199 HOH HOH C . 
V 6 HOH 225 625 1200 HOH HOH C . 
V 6 HOH 226 626 1201 HOH HOH C . 
W 6 HOH 1   401 2    HOH HOH D . 
W 6 HOH 2   402 5    HOH HOH D . 
W 6 HOH 3   403 8    HOH HOH D . 
W 6 HOH 4   404 9    HOH HOH D . 
W 6 HOH 5   405 11   HOH HOH D . 
W 6 HOH 6   406 12   HOH HOH D . 
W 6 HOH 7   407 21   HOH HOH D . 
W 6 HOH 8   408 23   HOH HOH D . 
W 6 HOH 9   409 26   HOH HOH D . 
W 6 HOH 10  410 30   HOH HOH D . 
W 6 HOH 11  411 35   HOH HOH D . 
W 6 HOH 12  412 36   HOH HOH D . 
W 6 HOH 13  413 40   HOH HOH D . 
W 6 HOH 14  414 43   HOH HOH D . 
W 6 HOH 15  415 45   HOH HOH D . 
W 6 HOH 16  416 60   HOH HOH D . 
W 6 HOH 17  417 62   HOH HOH D . 
W 6 HOH 18  418 63   HOH HOH D . 
W 6 HOH 19  419 68   HOH HOH D . 
W 6 HOH 20  420 72   HOH HOH D . 
W 6 HOH 21  421 76   HOH HOH D . 
W 6 HOH 22  422 81   HOH HOH D . 
W 6 HOH 23  423 88   HOH HOH D . 
W 6 HOH 24  424 90   HOH HOH D . 
W 6 HOH 25  425 91   HOH HOH D . 
W 6 HOH 26  426 92   HOH HOH D . 
W 6 HOH 27  427 103  HOH HOH D . 
W 6 HOH 28  428 108  HOH HOH D . 
W 6 HOH 29  429 109  HOH HOH D . 
W 6 HOH 30  430 112  HOH HOH D . 
W 6 HOH 31  431 115  HOH HOH D . 
W 6 HOH 32  432 116  HOH HOH D . 
W 6 HOH 33  433 117  HOH HOH D . 
W 6 HOH 34  434 120  HOH HOH D . 
W 6 HOH 35  435 122  HOH HOH D . 
W 6 HOH 36  436 123  HOH HOH D . 
W 6 HOH 37  437 125  HOH HOH D . 
W 6 HOH 38  438 136  HOH HOH D . 
W 6 HOH 39  439 138  HOH HOH D . 
W 6 HOH 40  440 143  HOH HOH D . 
W 6 HOH 41  441 149  HOH HOH D . 
W 6 HOH 42  442 150  HOH HOH D . 
W 6 HOH 43  443 157  HOH HOH D . 
W 6 HOH 44  444 160  HOH HOH D . 
W 6 HOH 45  445 161  HOH HOH D . 
W 6 HOH 46  446 167  HOH HOH D . 
W 6 HOH 47  447 168  HOH HOH D . 
W 6 HOH 48  448 169  HOH HOH D . 
W 6 HOH 49  449 171  HOH HOH D . 
W 6 HOH 50  450 183  HOH HOH D . 
W 6 HOH 51  451 187  HOH HOH D . 
W 6 HOH 52  452 188  HOH HOH D . 
W 6 HOH 53  453 193  HOH HOH D . 
W 6 HOH 54  454 194  HOH HOH D . 
W 6 HOH 55  455 195  HOH HOH D . 
W 6 HOH 56  456 199  HOH HOH D . 
W 6 HOH 57  457 210  HOH HOH D . 
W 6 HOH 58  458 214  HOH HOH D . 
W 6 HOH 59  459 216  HOH HOH D . 
W 6 HOH 60  460 222  HOH HOH D . 
W 6 HOH 61  461 227  HOH HOH D . 
W 6 HOH 62  462 231  HOH HOH D . 
W 6 HOH 63  463 235  HOH HOH D . 
W 6 HOH 64  464 242  HOH HOH D . 
W 6 HOH 65  465 243  HOH HOH D . 
W 6 HOH 66  466 246  HOH HOH D . 
W 6 HOH 67  467 254  HOH HOH D . 
W 6 HOH 68  468 256  HOH HOH D . 
W 6 HOH 69  469 260  HOH HOH D . 
W 6 HOH 70  470 261  HOH HOH D . 
W 6 HOH 71  471 262  HOH HOH D . 
W 6 HOH 72  472 265  HOH HOH D . 
W 6 HOH 73  473 273  HOH HOH D . 
W 6 HOH 74  474 274  HOH HOH D . 
W 6 HOH 75  475 285  HOH HOH D . 
W 6 HOH 76  476 286  HOH HOH D . 
W 6 HOH 77  477 288  HOH HOH D . 
W 6 HOH 78  478 295  HOH HOH D . 
W 6 HOH 79  479 298  HOH HOH D . 
W 6 HOH 80  480 301  HOH HOH D . 
W 6 HOH 81  481 304  HOH HOH D . 
W 6 HOH 82  482 307  HOH HOH D . 
W 6 HOH 83  483 311  HOH HOH D . 
W 6 HOH 84  484 317  HOH HOH D . 
W 6 HOH 85  485 318  HOH HOH D . 
W 6 HOH 86  486 321  HOH HOH D . 
W 6 HOH 87  487 325  HOH HOH D . 
W 6 HOH 88  488 326  HOH HOH D . 
W 6 HOH 89  489 327  HOH HOH D . 
W 6 HOH 90  490 333  HOH HOH D . 
W 6 HOH 91  491 335  HOH HOH D . 
W 6 HOH 92  492 341  HOH HOH D . 
W 6 HOH 93  493 344  HOH HOH D . 
W 6 HOH 94  494 354  HOH HOH D . 
W 6 HOH 95  495 356  HOH HOH D . 
W 6 HOH 96  496 359  HOH HOH D . 
W 6 HOH 97  497 364  HOH HOH D . 
W 6 HOH 98  498 365  HOH HOH D . 
W 6 HOH 99  499 375  HOH HOH D . 
W 6 HOH 100 500 376  HOH HOH D . 
W 6 HOH 101 501 378  HOH HOH D . 
W 6 HOH 102 502 380  HOH HOH D . 
W 6 HOH 103 503 381  HOH HOH D . 
W 6 HOH 104 504 387  HOH HOH D . 
W 6 HOH 105 505 389  HOH HOH D . 
W 6 HOH 106 506 390  HOH HOH D . 
W 6 HOH 107 507 392  HOH HOH D . 
W 6 HOH 108 508 393  HOH HOH D . 
W 6 HOH 109 509 399  HOH HOH D . 
W 6 HOH 110 510 402  HOH HOH D . 
W 6 HOH 111 511 407  HOH HOH D . 
W 6 HOH 112 512 411  HOH HOH D . 
W 6 HOH 113 513 412  HOH HOH D . 
W 6 HOH 114 514 414  HOH HOH D . 
W 6 HOH 115 515 417  HOH HOH D . 
W 6 HOH 116 516 420  HOH HOH D . 
W 6 HOH 117 517 421  HOH HOH D . 
W 6 HOH 118 518 424  HOH HOH D . 
W 6 HOH 119 519 425  HOH HOH D . 
W 6 HOH 120 520 426  HOH HOH D . 
W 6 HOH 121 521 428  HOH HOH D . 
W 6 HOH 122 522 434  HOH HOH D . 
W 6 HOH 123 523 440  HOH HOH D . 
W 6 HOH 124 524 443  HOH HOH D . 
W 6 HOH 125 525 447  HOH HOH D . 
W 6 HOH 126 526 450  HOH HOH D . 
W 6 HOH 127 527 456  HOH HOH D . 
W 6 HOH 128 528 459  HOH HOH D . 
W 6 HOH 129 529 464  HOH HOH D . 
W 6 HOH 130 530 465  HOH HOH D . 
W 6 HOH 131 531 467  HOH HOH D . 
W 6 HOH 132 532 469  HOH HOH D . 
W 6 HOH 133 533 473  HOH HOH D . 
W 6 HOH 134 534 476  HOH HOH D . 
W 6 HOH 135 535 480  HOH HOH D . 
W 6 HOH 136 536 481  HOH HOH D . 
W 6 HOH 137 537 484  HOH HOH D . 
W 6 HOH 138 538 486  HOH HOH D . 
W 6 HOH 139 539 489  HOH HOH D . 
W 6 HOH 140 540 492  HOH HOH D . 
W 6 HOH 141 541 493  HOH HOH D . 
W 6 HOH 142 542 497  HOH HOH D . 
W 6 HOH 143 543 500  HOH HOH D . 
W 6 HOH 144 544 502  HOH HOH D . 
W 6 HOH 145 545 504  HOH HOH D . 
W 6 HOH 146 546 519  HOH HOH D . 
W 6 HOH 147 547 520  HOH HOH D . 
W 6 HOH 148 548 521  HOH HOH D . 
W 6 HOH 149 549 525  HOH HOH D . 
W 6 HOH 150 550 526  HOH HOH D . 
W 6 HOH 151 551 529  HOH HOH D . 
W 6 HOH 152 552 535  HOH HOH D . 
W 6 HOH 153 553 540  HOH HOH D . 
W 6 HOH 154 554 545  HOH HOH D . 
W 6 HOH 155 555 547  HOH HOH D . 
W 6 HOH 156 556 548  HOH HOH D . 
W 6 HOH 157 557 549  HOH HOH D . 
W 6 HOH 158 558 551  HOH HOH D . 
W 6 HOH 159 559 555  HOH HOH D . 
W 6 HOH 160 560 561  HOH HOH D . 
W 6 HOH 161 561 568  HOH HOH D . 
W 6 HOH 162 562 574  HOH HOH D . 
W 6 HOH 163 563 576  HOH HOH D . 
W 6 HOH 164 564 578  HOH HOH D . 
W 6 HOH 165 565 579  HOH HOH D . 
W 6 HOH 166 566 581  HOH HOH D . 
W 6 HOH 167 567 583  HOH HOH D . 
W 6 HOH 168 568 588  HOH HOH D . 
W 6 HOH 169 569 589  HOH HOH D . 
W 6 HOH 170 570 592  HOH HOH D . 
W 6 HOH 171 571 593  HOH HOH D . 
W 6 HOH 172 572 599  HOH HOH D . 
W 6 HOH 173 573 600  HOH HOH D . 
W 6 HOH 174 574 603  HOH HOH D . 
W 6 HOH 175 575 613  HOH HOH D . 
W 6 HOH 176 576 616  HOH HOH D . 
W 6 HOH 177 577 617  HOH HOH D . 
W 6 HOH 178 578 619  HOH HOH D . 
W 6 HOH 179 579 623  HOH HOH D . 
W 6 HOH 180 580 627  HOH HOH D . 
W 6 HOH 181 581 628  HOH HOH D . 
W 6 HOH 182 582 631  HOH HOH D . 
W 6 HOH 183 583 636  HOH HOH D . 
W 6 HOH 184 584 641  HOH HOH D . 
W 6 HOH 185 585 646  HOH HOH D . 
W 6 HOH 186 586 649  HOH HOH D . 
W 6 HOH 187 587 650  HOH HOH D . 
W 6 HOH 188 588 651  HOH HOH D . 
W 6 HOH 189 589 654  HOH HOH D . 
W 6 HOH 190 590 657  HOH HOH D . 
W 6 HOH 191 591 658  HOH HOH D . 
W 6 HOH 192 592 661  HOH HOH D . 
W 6 HOH 193 593 662  HOH HOH D . 
W 6 HOH 194 594 663  HOH HOH D . 
W 6 HOH 195 595 666  HOH HOH D . 
W 6 HOH 196 596 668  HOH HOH D . 
W 6 HOH 197 597 669  HOH HOH D . 
W 6 HOH 198 598 678  HOH HOH D . 
W 6 HOH 199 599 688  HOH HOH D . 
W 6 HOH 200 600 689  HOH HOH D . 
W 6 HOH 201 601 694  HOH HOH D . 
W 6 HOH 202 602 699  HOH HOH D . 
W 6 HOH 203 603 701  HOH HOH D . 
W 6 HOH 204 604 703  HOH HOH D . 
W 6 HOH 205 605 707  HOH HOH D . 
W 6 HOH 206 606 715  HOH HOH D . 
W 6 HOH 207 607 721  HOH HOH D . 
W 6 HOH 208 608 724  HOH HOH D . 
W 6 HOH 209 609 725  HOH HOH D . 
W 6 HOH 210 610 727  HOH HOH D . 
W 6 HOH 211 611 730  HOH HOH D . 
W 6 HOH 212 612 737  HOH HOH D . 
W 6 HOH 213 613 738  HOH HOH D . 
W 6 HOH 214 614 740  HOH HOH D . 
W 6 HOH 215 615 741  HOH HOH D . 
W 6 HOH 216 616 746  HOH HOH D . 
W 6 HOH 217 617 750  HOH HOH D . 
W 6 HOH 218 618 751  HOH HOH D . 
W 6 HOH 219 619 753  HOH HOH D . 
W 6 HOH 220 620 756  HOH HOH D . 
W 6 HOH 221 621 760  HOH HOH D . 
W 6 HOH 222 622 765  HOH HOH D . 
W 6 HOH 223 623 766  HOH HOH D . 
W 6 HOH 224 624 767  HOH HOH D . 
W 6 HOH 225 625 771  HOH HOH D . 
W 6 HOH 226 626 775  HOH HOH D . 
W 6 HOH 227 627 776  HOH HOH D . 
W 6 HOH 228 628 783  HOH HOH D . 
W 6 HOH 229 629 784  HOH HOH D . 
W 6 HOH 230 630 785  HOH HOH D . 
W 6 HOH 231 631 788  HOH HOH D . 
W 6 HOH 232 632 790  HOH HOH D . 
W 6 HOH 233 633 808  HOH HOH D . 
W 6 HOH 234 634 809  HOH HOH D . 
W 6 HOH 235 635 822  HOH HOH D . 
W 6 HOH 236 636 823  HOH HOH D . 
W 6 HOH 237 637 824  HOH HOH D . 
W 6 HOH 238 638 826  HOH HOH D . 
W 6 HOH 239 639 828  HOH HOH D . 
W 6 HOH 240 640 836  HOH HOH D . 
W 6 HOH 241 641 838  HOH HOH D . 
W 6 HOH 242 642 842  HOH HOH D . 
W 6 HOH 243 643 846  HOH HOH D . 
W 6 HOH 244 644 851  HOH HOH D . 
W 6 HOH 245 645 854  HOH HOH D . 
W 6 HOH 246 646 863  HOH HOH D . 
W 6 HOH 247 647 867  HOH HOH D . 
W 6 HOH 248 648 879  HOH HOH D . 
W 6 HOH 249 649 881  HOH HOH D . 
W 6 HOH 250 650 882  HOH HOH D . 
W 6 HOH 251 651 886  HOH HOH D . 
W 6 HOH 252 652 887  HOH HOH D . 
W 6 HOH 253 653 895  HOH HOH D . 
W 6 HOH 254 654 900  HOH HOH D . 
W 6 HOH 255 655 902  HOH HOH D . 
W 6 HOH 256 656 958  HOH HOH D . 
W 6 HOH 257 657 959  HOH HOH D . 
W 6 HOH 258 658 975  HOH HOH D . 
W 6 HOH 259 659 976  HOH HOH D . 
W 6 HOH 260 660 977  HOH HOH D . 
W 6 HOH 261 661 978  HOH HOH D . 
W 6 HOH 262 662 980  HOH HOH D . 
W 6 HOH 263 663 981  HOH HOH D . 
W 6 HOH 264 664 982  HOH HOH D . 
W 6 HOH 265 665 983  HOH HOH D . 
W 6 HOH 266 666 984  HOH HOH D . 
W 6 HOH 267 667 985  HOH HOH D . 
W 6 HOH 268 668 986  HOH HOH D . 
W 6 HOH 269 669 987  HOH HOH D . 
W 6 HOH 270 670 988  HOH HOH D . 
W 6 HOH 271 671 989  HOH HOH D . 
W 6 HOH 272 672 990  HOH HOH D . 
W 6 HOH 273 673 991  HOH HOH D . 
W 6 HOH 274 674 992  HOH HOH D . 
W 6 HOH 275 675 993  HOH HOH D . 
W 6 HOH 276 676 994  HOH HOH D . 
W 6 HOH 277 677 995  HOH HOH D . 
W 6 HOH 278 678 996  HOH HOH D . 
W 6 HOH 279 679 997  HOH HOH D . 
W 6 HOH 280 680 998  HOH HOH D . 
W 6 HOH 281 681 999  HOH HOH D . 
W 6 HOH 282 682 1024 HOH HOH D . 
W 6 HOH 283 683 1025 HOH HOH D . 
W 6 HOH 284 684 1026 HOH HOH D . 
W 6 HOH 285 685 1027 HOH HOH D . 
W 6 HOH 286 686 1036 HOH HOH D . 
W 6 HOH 287 687 1040 HOH HOH D . 
W 6 HOH 288 688 1042 HOH HOH D . 
W 6 HOH 289 689 1054 HOH HOH D . 
W 6 HOH 290 690 1060 HOH HOH D . 
W 6 HOH 291 691 1061 HOH HOH D . 
W 6 HOH 292 692 1067 HOH HOH D . 
W 6 HOH 293 693 1078 HOH HOH D . 
W 6 HOH 294 694 1081 HOH HOH D . 
W 6 HOH 295 695 1086 HOH HOH D . 
W 6 HOH 296 696 1087 HOH HOH D . 
W 6 HOH 297 697 1089 HOH HOH D . 
W 6 HOH 298 698 1097 HOH HOH D . 
W 6 HOH 299 699 1105 HOH HOH D . 
W 6 HOH 300 700 1108 HOH HOH D . 
W 6 HOH 301 701 1109 HOH HOH D . 
W 6 HOH 302 702 1112 HOH HOH D . 
W 6 HOH 303 703 1114 HOH HOH D . 
W 6 HOH 304 704 1121 HOH HOH D . 
W 6 HOH 305 705 1122 HOH HOH D . 
W 6 HOH 306 706 1123 HOH HOH D . 
W 6 HOH 307 707 1133 HOH HOH D . 
W 6 HOH 308 708 1135 HOH HOH D . 
W 6 HOH 309 709 1136 HOH HOH D . 
W 6 HOH 310 710 1142 HOH HOH D . 
W 6 HOH 311 711 1167 HOH HOH D . 
W 6 HOH 312 712 1180 HOH HOH D . 
W 6 HOH 313 713 1181 HOH HOH D . 
W 6 HOH 314 714 1182 HOH HOH D . 
W 6 HOH 315 715 1183 HOH HOH D . 
W 6 HOH 316 716 1184 HOH HOH D . 
W 6 HOH 317 717 1185 HOH HOH D . 
W 6 HOH 318 718 1186 HOH HOH D . 
W 6 HOH 319 719 1202 HOH HOH D . 
W 6 HOH 320 720 1203 HOH HOH D . 
W 6 HOH 321 721 1204 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       3.2.19   22/12/2005      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 
DNA         .        ?               ?       ?                    ?                     'data collection' ? ?          ? 4 
XDS         .        ?               ?       ?                    ?                     'data reduction'  ? ?          ? 5 
MOLREP      .        ?               ?       ?                    ?                     phasing           ? ?          ? 6 
# 
_cell.entry_id           4KP5 
_cell.length_a           77.297 
_cell.length_b           74.157 
_cell.length_c           91.395 
_cell.angle_alpha        90.000 
_cell.angle_beta         108.810 
_cell.angle_gamma        90.000 
_cell.pdbx_unique_axis   ? 
_cell.Z_PDB              8 
_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                         4KP5 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.Int_Tables_number                4 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.space_group_name_Hall            ? 
# 
_exptl.crystals_number   1 
_exptl.entry_id          4KP5 
_exptl.method            'X-RAY DIFFRACTION' 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_percent_sol   40.7 
_exptl_crystal.density_Matthews      2.1 
_exptl_crystal.pdbx_mosaicity        0.23 
_exptl_crystal.density_meas          ? 
_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.pH              7.0 
_exptl_crystal_grow.temp            291 
_exptl_crystal_grow.pdbx_details    
'0.1M ammonium citrate pH 7.0, 0.2M ammonium sulfate, 30% PEG 4000, VAPOR DIFFUSION, SITTING DROP, temperature 291K' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_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.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.monochromator                    
'High Heat Load (HHL) Monochromator: Si 111; Large Offset Monochromator (LOM): Si 311, Si 511' 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_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_wavelength_list        0.826606 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_site       'PETRA III, EMBL c/o DESY' 
_diffrn_source.pdbx_synchrotron_beamline   'P14 (MX2)' 
# 
_reflns.entry_id                     4KP5 
_reflns.d_resolution_high            0.945 
_reflns.d_resolution_low             86.515 
_reflns.number_all                   ? 
_reflns.number_obs                   168177 
_reflns.pdbx_Rmerge_I_obs            0.045 
_reflns.pdbx_netI_over_sigmaI        24.300 
_reflns.pdbx_Rsym_value              0.045 
_reflns.pdbx_redundancy              7.000 
_reflns.percent_possible_obs         97.500 
_reflns.observed_criterion_sigma_F   0 
_reflns.observed_criterion_sigma_I   0 
_reflns.B_iso_Wilson_estimate        13.564 
_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_ordinal                 1 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_CC_half                 ? 
_reflns.pdbx_Rpim_I_all              ? 
_reflns.pdbx_Rrim_I_all              ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.number_measured_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_unique_obs 
_reflns_shell.pdbx_rejects 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_redundancy 
_reflns_shell.percent_possible_obs 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.percent_possible_all 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
1.45 1.53  ? 157582 ? ? 0.253 2.9  0.253 ? 6.60 ? 6.60  ? 23907 ? ? 0.300 ? 95.20 0.30 0.12 1  1 ? 
1.53 1.62  ? 166398 ? ? 0.179 4.1  0.179 ? 7.20 ? 9.70  ? 23108 ? ? 0.210 ? 97.30 0.21 0.08 2  1 ? 
1.62 1.73  ? 159721 ? ? 0.125 5.8  0.125 ? 7.30 ? 13.40 ? 21908 ? ? 0.148 ? 98.00 0.15 0.05 3  1 ? 
1.73 1.87  ? 146364 ? ? 0.086 8.1  0.086 ? 7.20 ? 18.50 ? 20418 ? ? 0.102 ? 98.10 0.10 0.04 4  1 ? 
1.87 2.05  ? 129833 ? ? 0.062 10.6 0.062 ? 6.90 ? 25.10 ? 18756 ? ? 0.074 ? 98.10 0.07 0.03 5  1 ? 
2.05 2.29  ? 112047 ? ? 0.048 13.0 0.048 ? 6.70 ? 31.90 ? 16710 ? ? 0.058 ? 96.20 0.06 0.02 6  1 ? 
2.29 2.65  ? 111623 ? ? 0.042 14.0 0.042 ? 7.30 ? 39.10 ? 15188 ? ? 0.050 ? 99.10 0.05 0.02 7  1 ? 
2.65 3.24  ? 92202  ? ? 0.036 15.3 0.036 ? 7.20 ? 46.30 ? 12856 ? ? 0.042 ? 99.00 0.04 0.02 8  1 ? 
3.24 4.59  ? 65268  ? ? 0.030 16.7 0.030 ? 6.70 ? 53.10 ? 9708  ? ? 0.035 ? 96.30 0.04 0.01 9  1 ? 
4.59 86.51 ? 41986  ? ? 0.027 12.5 0.027 ? 7.50 ? 57.40 ? 5618  ? ? 0.032 ? 99.90 0.03 0.01 10 1 ? 
# 
_refine.entry_id                                 4KP5 
_refine.ls_d_res_high                            1.450 
_refine.ls_d_res_low                             73.130 
_refine.pdbx_ls_sigma_F                          0.00 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    97.290 
_refine.ls_number_reflns_obs                     168150 
_refine.ls_number_reflns_all                     168150 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.details                                  
'HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT U VALUES      : REFINED INDIVIDUALLY' 
_refine.ls_R_factor_all                          0.181 
_refine.ls_R_factor_obs                          0.181 
_refine.ls_R_factor_R_work                       0.177 
_refine.ls_wR_factor_R_work                      0.182 
_refine.ls_R_factor_R_free                       0.216 
_refine.ls_wR_factor_R_free                      0.220 
_refine.ls_percent_reflns_R_free                 10.000 
_refine.ls_number_reflns_R_free                  16774 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               16.860 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            -0.320 
_refine.aniso_B[2][2]                            0.530 
_refine.aniso_B[3][3]                            -0.090 
_refine.aniso_B[1][2]                            0.000 
_refine.aniso_B[1][3]                            0.180 
_refine.aniso_B[2][3]                            0.000 
_refine.correlation_coeff_Fo_to_Fc               0.966 
_refine.correlation_coeff_Fo_to_Fc_free          0.952 
_refine.overall_SU_R_Cruickshank_DPI             0.081 
_refine.overall_SU_R_free                        0.084 
_refine.pdbx_overall_ESU_R                       0.081 
_refine.pdbx_overall_ESU_R_Free                  0.084 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_B                             ? 
_refine.solvent_model_details                    MASK 
_refine.pdbx_solvent_vdw_probe_radii             1.400 
_refine.pdbx_solvent_ion_probe_radii             0.800 
_refine.pdbx_solvent_shrinkage_radii             0.800 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.overall_FOM_work_R_set                   0.848 
_refine.B_iso_max                                67.94 
_refine.B_iso_min                                2.00 
_refine.pdbx_overall_phase_error                 ? 
_refine.occupancy_max                            1.00 
_refine.occupancy_min                            0.25 
_refine.pdbx_ls_sigma_I                          ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.pdbx_starting_model                      1JD0 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        8372 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         117 
_refine_hist.number_atoms_solvent             1206 
_refine_hist.number_atoms_total               9695 
_refine_hist.d_res_high                       1.450 
_refine_hist.d_res_low                        73.130 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.number 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
_refine_ls_restr.pdbx_refine_id 
r_bond_refined_d       9156  0.032  0.020  ? ? 'X-RAY DIFFRACTION' 
r_angle_refined_deg    12514 2.530  1.956  ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_1_deg 1125  7.393  5.000  ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_2_deg 454   38.346 24.714 ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_3_deg 1457  14.372 15.000 ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_4_deg 33    19.003 15.000 ? ? 'X-RAY DIFFRACTION' 
r_chiral_restr         1294  0.189  0.200  ? ? 'X-RAY DIFFRACTION' 
r_gen_planes_refined   7301  0.015  0.021  ? ? 'X-RAY DIFFRACTION' 
# 
_refine_ls_shell.d_res_high                       1.450 
_refine_ls_shell.d_res_low                        1.488 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.percent_reflns_obs               96.460 
_refine_ls_shell.number_reflns_R_work             11090 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_R_work                  0.207 
_refine_ls_shell.R_factor_R_free                  0.260 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             1232 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.number_reflns_all                12322 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.R_factor_obs                     ? 
# 
_struct.entry_id                  4KP5 
_struct.title                     
;Crystal structure of catalytic domain of human carbonic anhydrase isozyme XII with 2-Chloro-4-[(pyrimidin-2-ylsulfanyl)acetyl]benzenesulfonamide
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        4KP5 
_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 4 ? 
I N N 2 ? 
J N N 3 ? 
K N N 4 ? 
L N N 4 ? 
M N N 2 ? 
N N N 3 ? 
O N N 5 ? 
P N N 2 ? 
Q N N 3 ? 
R N N 4 ? 
S N N 4 ? 
T N N 6 ? 
U N N 6 ? 
V N N 6 ? 
W N N 6 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    CAH12_HUMAN 
_struct_ref.pdbx_db_accession          O43570 
_struct_ref.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 4KP5 A 2 ? 263 ? O43570 30 ? 291 ? 2 263 
2 1 4KP5 B 2 ? 263 ? O43570 30 ? 291 ? 2 263 
3 1 4KP5 C 2 ? 263 ? O43570 30 ? 291 ? 2 263 
4 1 4KP5 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 4KP5 MET A 1 ? UNP O43570 ? ? 'expression tag' 1 1 
2 4KP5 MET B 1 ? UNP O43570 ? ? 'expression tag' 1 2 
3 4KP5 MET C 1 ? UNP O43570 ? ? 'expression tag' 1 3 
4 4KP5 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,K,L,T,U 
2 1 C,D,M,N,O,P,Q,R,S,V,W   
# 
_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  GLY A 11  ? LYS A 18  ? GLY A 11  LYS A 18  5 ? 8  
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  SER B 14  ? TYR B 19  ? SER B 14  TYR B 19  1 ? 6  
HELX_P HELX_P10 10 PRO B 20  ? GLY B 24  ? PRO B 20  GLY B 24  5 ? 5  
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 PHE C 7   ? GLY C 11  ? PHE C 7   GLY C 11  5 ? 5  
HELX_P HELX_P18 18 SER C 14  ? LYS C 18  ? SER C 14  LYS C 18  5 ? 5  
HELX_P HELX_P19 19 TYR C 19  ? GLY C 24  ? TYR C 19  GLY C 24  5 ? 6  
HELX_P HELX_P20 20 HIS C 33  ? ASP C 35  ? HIS C 33  ASP C 35  5 ? 3  
HELX_P HELX_P21 21 ASP C 128 ? SER C 133 ? ASP C 128 SER C 133 1 ? 6  
HELX_P HELX_P22 22 ASN C 152 ? SER C 160 ? ASN C 152 SER C 160 1 ? 9  
HELX_P HELX_P23 23 HIS C 161 ? VAL C 165 ? HIS C 161 VAL C 165 5 ? 5  
HELX_P HELX_P24 24 ASN C 178 ? LEU C 183 ? ASN C 178 LEU C 183 5 ? 6  
HELX_P HELX_P25 25 SER C 218 ? ALA C 228 ? SER C 218 ALA C 228 1 ? 11 
HELX_P HELX_P26 26 GLY D 11  ? LYS D 18  ? GLY D 11  LYS D 18  5 ? 8  
HELX_P HELX_P27 27 TYR D 19  ? GLY D 24  ? TYR D 19  GLY D 24  5 ? 6  
HELX_P HELX_P28 28 HIS D 33  ? ASP D 35  ? HIS D 33  ASP D 35  5 ? 3  
HELX_P HELX_P29 29 ASP D 128 ? SER D 133 ? ASP D 128 SER D 133 1 ? 6  
HELX_P HELX_P30 30 ASN D 152 ? SER D 160 ? ASN D 152 SER D 160 1 ? 9  
HELX_P HELX_P31 31 HIS D 161 ? LYS D 166 ? HIS D 161 LYS D 166 5 ? 6  
HELX_P HELX_P32 32 ASN D 178 ? LEU D 183 ? ASN D 178 LEU D 183 5 ? 6  
HELX_P HELX_P33 33 SER D 218 ? LEU D 229 ? SER D 218 LEU D 229 1 ? 12 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1  disulf ? ? A CYS 22  SG  ? ? ? 1_555 A CYS 202 SG  ? ? A CYS 22  A CYS 202 1_555 ? ? ? ? ? ? ? 2.036 ? ? 
disulf2  disulf ? ? B CYS 22  SG  ? ? ? 1_555 B CYS 202 SG  ? ? B CYS 22  B CYS 202 1_555 ? ? ? ? ? ? ? 2.025 ? ? 
disulf3  disulf ? ? C CYS 22  SG  ? ? ? 1_555 C CYS 202 SG  ? ? C CYS 22  C CYS 202 1_555 ? ? ? ? ? ? ? 2.055 ? ? 
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 ? ? ? ? ? ? ? 2.056 ? ? 
metalc2  metalc ? ? A HIS 93  NE2 ? ? ? 1_555 E ZN  .   ZN  ? ? A HIS 93  A ZN  301 1_555 ? ? ? ? ? ? ? 2.036 ? ? 
metalc3  metalc ? ? A HIS 117 ND1 ? ? ? 1_555 E ZN  .   ZN  ? ? A HIS 117 A ZN  301 1_555 ? ? ? ? ? ? ? 2.000 ? ? 
metalc4  metalc ? ? E ZN  .   ZN  ? ? ? 1_555 F E1F .   N19 ? ? A ZN  301 A E1F 302 1_555 ? ? ? ? ? ? ? 1.984 ? ? 
metalc5  metalc ? ? B HIS 91  NE2 ? ? ? 1_555 I ZN  .   ZN  ? ? B HIS 91  B ZN  301 1_555 ? ? ? ? ? ? ? 2.115 ? ? 
metalc6  metalc ? ? B HIS 93  NE2 ? ? ? 1_555 I ZN  .   ZN  ? ? B HIS 93  B ZN  301 1_555 ? ? ? ? ? ? ? 2.049 ? ? 
metalc7  metalc ? ? B HIS 117 ND1 ? ? ? 1_555 I ZN  .   ZN  ? ? B HIS 117 B ZN  301 1_555 ? ? ? ? ? ? ? 2.051 ? ? 
metalc8  metalc ? ? I ZN  .   ZN  ? ? ? 1_555 J E1F .   N19 ? ? B ZN  301 B E1F 302 1_555 ? ? ? ? ? ? ? 1.941 ? ? 
metalc9  metalc ? ? C HIS 91  NE2 ? ? ? 1_555 M ZN  .   ZN  ? ? C HIS 91  C ZN  301 1_555 ? ? ? ? ? ? ? 2.039 ? ? 
metalc10 metalc ? ? C HIS 93  NE2 ? ? ? 1_555 M ZN  .   ZN  ? ? C HIS 93  C ZN  301 1_555 ? ? ? ? ? ? ? 2.038 ? ? 
metalc11 metalc ? ? C HIS 117 ND1 ? ? ? 1_555 M ZN  .   ZN  ? ? C HIS 117 C ZN  301 1_555 ? ? ? ? ? ? ? 2.035 ? ? 
metalc12 metalc ? ? M ZN  .   ZN  ? ? ? 1_555 N E1F .   N19 ? ? C ZN  301 C E1F 302 1_555 ? ? ? ? ? ? ? 1.968 ? ? 
metalc13 metalc ? ? M ZN  .   ZN  ? ? ? 1_555 N E1F .   S16 ? ? C ZN  301 C E1F 302 1_555 ? ? ? ? ? ? ? 2.980 ? ? 
metalc14 metalc ? ? D HIS 91  NE2 ? ? ? 1_555 P ZN  .   ZN  ? ? D HIS 91  D ZN  301 1_555 ? ? ? ? ? ? ? 2.014 ? ? 
metalc15 metalc ? ? D HIS 93  NE2 ? ? ? 1_555 P ZN  .   ZN  ? ? D HIS 93  D ZN  301 1_555 ? ? ? ? ? ? ? 2.036 ? ? 
metalc16 metalc ? ? D HIS 117 ND1 ? ? ? 1_555 P ZN  .   ZN  ? ? D HIS 117 D ZN  301 1_555 ? ? ? ? ? ? ? 2.034 ? ? 
metalc17 metalc ? ? P ZN  .   ZN  ? ? ? 1_555 Q E1F .   N19 ? ? D ZN  301 D E1F 302 1_555 ? ? ? ? ? ? ? 1.990 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
metalc ? ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  NE2 ? A HIS 91  ? A HIS 91  ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 NE2 ? A HIS 93  ? A HIS 93  ? 1_555 101.7 ? 
2  NE2 ? A HIS 91  ? A HIS 91  ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS 117 ? A HIS 117 ? 1_555 111.6 ? 
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 97.2  ? 
4  NE2 ? A HIS 91  ? A HIS 91  ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 N19 ? F E1F .   ? A E1F 302 ? 1_555 107.0 ? 
5  NE2 ? A HIS 93  ? A HIS 93  ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 N19 ? F E1F .   ? A E1F 302 ? 1_555 117.7 ? 
6  ND1 ? A HIS 117 ? A HIS 117 ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 N19 ? F E1F .   ? A E1F 302 ? 1_555 120.1 ? 
7  NE2 ? B HIS 91  ? B HIS 91  ? 1_555 ZN ? I ZN . ? B ZN 301 ? 1_555 NE2 ? B HIS 93  ? B HIS 93  ? 1_555 102.2 ? 
8  NE2 ? B HIS 91  ? B HIS 91  ? 1_555 ZN ? I ZN . ? B ZN 301 ? 1_555 ND1 ? B HIS 117 ? B HIS 117 ? 1_555 118.7 ? 
9  NE2 ? B HIS 93  ? B HIS 93  ? 1_555 ZN ? I ZN . ? B ZN 301 ? 1_555 ND1 ? B HIS 117 ? B HIS 117 ? 1_555 99.4  ? 
10 NE2 ? B HIS 91  ? B HIS 91  ? 1_555 ZN ? I ZN . ? B ZN 301 ? 1_555 N19 ? J E1F .   ? B E1F 302 ? 1_555 102.0 ? 
11 NE2 ? B HIS 93  ? B HIS 93  ? 1_555 ZN ? I ZN . ? B ZN 301 ? 1_555 N19 ? J E1F .   ? B E1F 302 ? 1_555 116.2 ? 
12 ND1 ? B HIS 117 ? B HIS 117 ? 1_555 ZN ? I ZN . ? B ZN 301 ? 1_555 N19 ? J E1F .   ? B E1F 302 ? 1_555 118.0 ? 
13 NE2 ? C HIS 91  ? C HIS 91  ? 1_555 ZN ? M ZN . ? C ZN 301 ? 1_555 NE2 ? C HIS 93  ? C HIS 93  ? 1_555 100.8 ? 
14 NE2 ? C HIS 91  ? C HIS 91  ? 1_555 ZN ? M ZN . ? C ZN 301 ? 1_555 ND1 ? C HIS 117 ? C HIS 117 ? 1_555 116.3 ? 
15 NE2 ? C HIS 93  ? C HIS 93  ? 1_555 ZN ? M ZN . ? C ZN 301 ? 1_555 ND1 ? C HIS 117 ? C HIS 117 ? 1_555 95.7  ? 
16 NE2 ? C HIS 91  ? C HIS 91  ? 1_555 ZN ? M ZN . ? C ZN 301 ? 1_555 N19 ? N E1F .   ? C E1F 302 ? 1_555 108.0 ? 
17 NE2 ? C HIS 93  ? C HIS 93  ? 1_555 ZN ? M ZN . ? C ZN 301 ? 1_555 N19 ? N E1F .   ? C E1F 302 ? 1_555 116.8 ? 
18 ND1 ? C HIS 117 ? C HIS 117 ? 1_555 ZN ? M ZN . ? C ZN 301 ? 1_555 N19 ? N E1F .   ? C E1F 302 ? 1_555 117.9 ? 
19 NE2 ? C HIS 91  ? C HIS 91  ? 1_555 ZN ? M ZN . ? C ZN 301 ? 1_555 S16 ? N E1F .   ? C E1F 302 ? 1_555 100.5 ? 
20 NE2 ? C HIS 93  ? C HIS 93  ? 1_555 ZN ? M ZN . ? C ZN 301 ? 1_555 S16 ? N E1F .   ? C E1F 302 ? 1_555 145.0 ? 
21 ND1 ? C HIS 117 ? C HIS 117 ? 1_555 ZN ? M ZN . ? C ZN 301 ? 1_555 S16 ? N E1F .   ? C E1F 302 ? 1_555 99.3  ? 
22 N19 ? N E1F .   ? C E1F 302 ? 1_555 ZN ? M ZN . ? C ZN 301 ? 1_555 S16 ? N E1F .   ? C E1F 302 ? 1_555 29.2  ? 
23 NE2 ? D HIS 91  ? D HIS 91  ? 1_555 ZN ? P ZN . ? D ZN 301 ? 1_555 NE2 ? D HIS 93  ? D HIS 93  ? 1_555 103.2 ? 
24 NE2 ? D HIS 91  ? D HIS 91  ? 1_555 ZN ? P ZN . ? D ZN 301 ? 1_555 ND1 ? D HIS 117 ? D HIS 117 ? 1_555 111.7 ? 
25 NE2 ? D HIS 93  ? D HIS 93  ? 1_555 ZN ? P ZN . ? D ZN 301 ? 1_555 ND1 ? D HIS 117 ? D HIS 117 ? 1_555 97.7  ? 
26 NE2 ? D HIS 91  ? D HIS 91  ? 1_555 ZN ? P ZN . ? D ZN 301 ? 1_555 N19 ? Q E1F .   ? D E1F 302 ? 1_555 107.8 ? 
27 NE2 ? D HIS 93  ? D HIS 93  ? 1_555 ZN ? P ZN . ? D ZN 301 ? 1_555 N19 ? Q E1F .   ? D E1F 302 ? 1_555 115.7 ? 
28 ND1 ? D HIS 117 ? D HIS 117 ? 1_555 ZN ? P ZN . ? D ZN 301 ? 1_555 N19 ? Q E1F .   ? D E1F 302 ? 1_555 119.5 ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 CYS A 22 ? CYS A 202 ? CYS A 22 ? 1_555 CYS A 202 ? 1_555 SG SG . . . None 'Disulfide bridge' 
2 CYS B 22 ? CYS B 202 ? CYS B 22 ? 1_555 CYS B 202 ? 1_555 SG SG . . . None 'Disulfide bridge' 
3 CYS C 22 ? CYS C 202 ? CYS C 22 ? 1_555 CYS C 202 ? 1_555 SG SG . . . None 'Disulfide bridge' 
4 CYS D 22 ? CYS D 202 ? CYS D 22 ? 1_555 CYS D 202 ? 1_555 SG SG . . . None 'Disulfide bridge' 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 SER 28  A . ? SER 28  A PRO 29  A ? PRO 29  A 1 1.78  
2 PRO 200 A . ? PRO 200 A PRO 201 A ? PRO 201 A 1 12.50 
3 SER 28  B . ? SER 28  B PRO 29  B ? PRO 29  B 1 -1.60 
4 PRO 200 B . ? PRO 200 B PRO 201 B ? PRO 201 B 1 5.38  
5 SER 28  C . ? SER 28  C PRO 29  C ? PRO 29  C 1 2.94  
6 PRO 200 C . ? PRO 200 C PRO 201 C ? PRO 201 C 1 -0.43 
7 SER 28  D . ? SER 28  D PRO 29  D ? PRO 29  D 1 -2.20 
8 PRO 200 D . ? PRO 200 D PRO 201 D ? PRO 201 D 1 -3.35 
# 
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 TYR A 191 ? N TYR A 191 O VAL A 210 ? O VAL A 210 
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 HIS A 117 ? O HIS A 117 N HIS A 91  ? N HIS A 91  
B 7 8  O LEU A 90  ? O LEU A 90  N LEU A 70  ? N LEU A 70  
B 8 9  O ASN A 71  ? O ASN A 71  N LEU A 60  ? N LEU A 60  
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 HIS A 91  ? N HIS A 91  O HIS A 117 ? O HIS A 117 
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 THR B 259 ? O THR B 259 
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 LEU B 142 ? O LEU B 142 N ILE B 118 ? N ILE B 118 
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 GLU B 47  ? N GLU B 47  O GLN B 79  ? O GLN B 79  
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 ILE B 118 ? N ILE B 118 O LEU B 142 ? O LEU B 142 
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 VAL C 257 ? O VAL C 257 
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 VAL C 144 ? O VAL C 144 N LEU C 116 ? N LEU C 116 
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 LEU C 116 ? N LEU C 116 O VAL C 144 ? O VAL C 144 
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 VAL D 257 ? O VAL D 257 
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 HIS D 117 ? O HIS D 117 N HIS D 91  ? N HIS D 91  
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 HIS D 91  ? N HIS D 91  O HIS D 117 ? O HIS D 117 
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 E1F 302 ? 13 'BINDING SITE FOR RESIDUE E1F A 302' 
AC3 Software A EDO 303 ? 7  'BINDING SITE FOR RESIDUE EDO A 303' 
AC4 Software A EDO 304 ? 4  'BINDING SITE FOR RESIDUE EDO A 304' 
AC5 Software B ZN  301 ? 4  'BINDING SITE FOR RESIDUE ZN B 301'  
AC6 Software B E1F 302 ? 12 'BINDING SITE FOR RESIDUE E1F B 302' 
AC7 Software B EDO 303 ? 5  'BINDING SITE FOR RESIDUE EDO B 303' 
AC8 Software B EDO 304 ? 5  'BINDING SITE FOR RESIDUE EDO B 304' 
AC9 Software C ZN  301 ? 4  'BINDING SITE FOR RESIDUE ZN C 301'  
BC1 Software C E1F 302 ? 14 'BINDING SITE FOR RESIDUE E1F C 302' 
BC2 Software C SO4 303 ? 5  'BINDING SITE FOR RESIDUE SO4 C 303' 
BC3 Software D ZN  301 ? 4  'BINDING SITE FOR RESIDUE ZN D 301'  
BC4 Software D E1F 302 ? 13 'BINDING SITE FOR RESIDUE E1F D 302' 
BC5 Software D EDO 303 ? 6  'BINDING SITE FOR RESIDUE EDO D 303' 
BC6 Software D EDO 304 ? 7  'BINDING SITE FOR RESIDUE EDO D 304' 
# 
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  E1F F .   ? E1F A 302 . ? 1_555 ? 
5   AC2 13 HIS A 91  ? HIS A 91  . ? 1_555 ? 
6   AC2 13 HIS A 93  ? HIS A 93  . ? 1_555 ? 
7   AC2 13 HIS A 117 ? HIS A 117 . ? 1_555 ? 
8   AC2 13 SER A 133 ? SER A 133 . ? 1_555 ? 
9   AC2 13 VAL A 141 ? VAL A 141 . ? 1_555 ? 
10  AC2 13 LEU A 197 ? LEU A 197 . ? 1_555 ? 
11  AC2 13 THR A 198 ? THR A 198 . ? 1_555 ? 
12  AC2 13 THR A 199 ? THR A 199 . ? 1_555 ? 
13  AC2 13 PRO A 201 ? PRO A 201 . ? 1_555 ? 
14  AC2 13 TRP A 208 ? TRP A 208 . ? 1_555 ? 
15  AC2 13 ZN  E .   ? ZN  A 301 . ? 1_555 ? 
16  AC2 13 EDO G .   ? EDO A 303 . ? 1_555 ? 
17  AC2 13 HOH T .   ? HOH A 670 . ? 1_555 ? 
18  AC3 7  ASN A 64  ? ASN A 64  . ? 1_555 ? 
19  AC3 7  HIS A 66  ? HIS A 66  . ? 1_555 ? 
20  AC3 7  GLN A 89  ? GLN A 89  . ? 1_555 ? 
21  AC3 7  HIS A 91  ? HIS A 91  . ? 1_555 ? 
22  AC3 7  E1F F .   ? E1F A 302 . ? 1_555 ? 
23  AC3 7  HOH T .   ? HOH A 666 . ? 1_555 ? 
24  AC3 7  HOH T .   ? HOH A 670 . ? 1_555 ? 
25  AC4 4  ASP A 156 ? ASP A 156 . ? 1_555 ? 
26  AC4 4  SER A 160 ? SER A 160 . ? 1_555 ? 
27  AC4 4  GLN A 221 ? GLN A 221 . ? 1_555 ? 
28  AC4 4  HOH T .   ? HOH A 564 . ? 1_555 ? 
29  AC5 4  HIS B 91  ? HIS B 91  . ? 1_555 ? 
30  AC5 4  HIS B 93  ? HIS B 93  . ? 1_555 ? 
31  AC5 4  HIS B 117 ? HIS B 117 . ? 1_555 ? 
32  AC5 4  E1F J .   ? E1F B 302 . ? 1_555 ? 
33  AC6 12 HIS B 91  ? HIS B 91  . ? 1_555 ? 
34  AC6 12 HIS B 93  ? HIS B 93  . ? 1_555 ? 
35  AC6 12 HIS B 117 ? HIS B 117 . ? 1_555 ? 
36  AC6 12 SER B 133 ? SER B 133 . ? 1_555 ? 
37  AC6 12 VAL B 141 ? VAL B 141 . ? 1_555 ? 
38  AC6 12 LEU B 197 ? LEU B 197 . ? 1_555 ? 
39  AC6 12 THR B 198 ? THR B 198 . ? 1_555 ? 
40  AC6 12 THR B 199 ? THR B 199 . ? 1_555 ? 
41  AC6 12 PRO B 201 ? PRO B 201 . ? 1_555 ? 
42  AC6 12 ASN B 203 ? ASN B 203 . ? 1_555 ? 
43  AC6 12 TRP B 208 ? TRP B 208 . ? 1_555 ? 
44  AC6 12 ZN  I .   ? ZN  B 301 . ? 1_555 ? 
45  AC7 5  ASN B 64  ? ASN B 64  . ? 1_555 ? 
46  AC7 5  GLN B 89  ? GLN B 89  . ? 1_555 ? 
47  AC7 5  HIS B 91  ? HIS B 91  . ? 1_555 ? 
48  AC7 5  HOH U .   ? HOH B 430 . ? 1_555 ? 
49  AC7 5  HOH U .   ? HOH B 489 . ? 1_555 ? 
50  AC8 5  THR B 44  ? THR B 44  . ? 1_555 ? 
51  AC8 5  LEU B 46  ? LEU B 46  . ? 1_555 ? 
52  AC8 5  GLY B 80  ? GLY B 80  . ? 1_555 ? 
53  AC8 5  TYR B 190 ? TYR B 190 . ? 1_555 ? 
54  AC8 5  ARG B 192 ? ARG B 192 . ? 1_555 ? 
55  AC9 4  HIS C 91  ? HIS C 91  . ? 1_555 ? 
56  AC9 4  HIS C 93  ? HIS C 93  . ? 1_555 ? 
57  AC9 4  HIS C 117 ? HIS C 117 . ? 1_555 ? 
58  AC9 4  E1F N .   ? E1F C 302 . ? 1_555 ? 
59  BC1 14 GLN C 89  ? GLN C 89  . ? 1_555 ? 
60  BC1 14 HIS C 91  ? HIS C 91  . ? 1_555 ? 
61  BC1 14 HIS C 93  ? HIS C 93  . ? 1_555 ? 
62  BC1 14 HIS C 117 ? HIS C 117 . ? 1_555 ? 
63  BC1 14 VAL C 119 ? VAL C 119 . ? 1_555 ? 
64  BC1 14 SER C 133 ? SER C 133 . ? 1_555 ? 
65  BC1 14 VAL C 141 ? VAL C 141 . ? 1_555 ? 
66  BC1 14 LEU C 197 ? LEU C 197 . ? 1_555 ? 
67  BC1 14 THR C 198 ? THR C 198 . ? 1_555 ? 
68  BC1 14 THR C 199 ? THR C 199 . ? 1_555 ? 
69  BC1 14 PRO C 201 ? PRO C 201 . ? 1_555 ? 
70  BC1 14 TRP C 208 ? TRP C 208 . ? 1_555 ? 
71  BC1 14 ZN  M .   ? ZN  C 301 . ? 1_555 ? 
72  BC1 14 HOH V .   ? HOH C 581 . ? 1_555 ? 
73  BC2 5  SER C 218 ? SER C 218 . ? 1_555 ? 
74  BC2 5  GLN C 219 ? GLN C 219 . ? 1_555 ? 
75  BC2 5  GLU C 220 ? GLU C 220 . ? 1_555 ? 
76  BC2 5  HOH V .   ? HOH C 576 . ? 1_555 ? 
77  BC2 5  HOH V .   ? HOH C 624 . ? 1_555 ? 
78  BC3 4  HIS D 91  ? HIS D 91  . ? 1_555 ? 
79  BC3 4  HIS D 93  ? HIS D 93  . ? 1_555 ? 
80  BC3 4  HIS D 117 ? HIS D 117 . ? 1_555 ? 
81  BC3 4  E1F Q .   ? E1F D 302 . ? 1_555 ? 
82  BC4 13 HIS D 91  ? HIS D 91  . ? 1_555 ? 
83  BC4 13 HIS D 93  ? HIS D 93  . ? 1_555 ? 
84  BC4 13 HIS D 117 ? HIS D 117 . ? 1_555 ? 
85  BC4 13 SER D 130 ? SER D 130 . ? 1_555 ? 
86  BC4 13 SER D 133 ? SER D 133 . ? 1_555 ? 
87  BC4 13 VAL D 141 ? VAL D 141 . ? 1_555 ? 
88  BC4 13 LEU D 197 ? LEU D 197 . ? 1_555 ? 
89  BC4 13 THR D 198 ? THR D 198 . ? 1_555 ? 
90  BC4 13 PRO D 201 ? PRO D 201 . ? 1_555 ? 
91  BC4 13 TRP D 208 ? TRP D 208 . ? 1_555 ? 
92  BC4 13 ZN  P .   ? ZN  D 301 . ? 1_555 ? 
93  BC4 13 EDO R .   ? EDO D 303 . ? 1_555 ? 
94  BC4 13 HOH W .   ? HOH D 678 . ? 1_555 ? 
95  BC5 6  ASN D 64  ? ASN D 64  . ? 1_555 ? 
96  BC5 6  HIS D 66  ? HIS D 66  . ? 1_555 ? 
97  BC5 6  GLN D 89  ? GLN D 89  . ? 1_555 ? 
98  BC5 6  HIS D 91  ? HIS D 91  . ? 1_555 ? 
99  BC5 6  E1F Q .   ? E1F D 302 . ? 1_555 ? 
100 BC5 6  HOH W .   ? HOH D 678 . ? 1_555 ? 
101 BC6 7  SER D 42  ? SER D 42  . ? 1_555 ? 
102 BC6 7  THR D 44  ? THR D 44  . ? 1_555 ? 
103 BC6 7  LEU D 46  ? LEU D 46  . ? 1_555 ? 
104 BC6 7  GLY D 80  ? GLY D 80  . ? 1_555 ? 
105 BC6 7  TYR D 190 ? TYR D 190 . ? 1_555 ? 
106 BC6 7  ARG D 192 ? ARG D 192 . ? 1_555 ? 
107 BC6 7  HOH W .   ? HOH D 713 . ? 1_555 ? 
# 
_pdbx_entry_details.entry_id                   4KP5 
_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_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   OD1 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   ASN 
_pdbx_validate_close_contact.auth_seq_id_1    71 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   B 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    711 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             1.63 
# 
_pdbx_validate_rmsd_bond.id                        1 
_pdbx_validate_rmsd_bond.PDB_model_num             1 
_pdbx_validate_rmsd_bond.auth_atom_id_1            CG 
_pdbx_validate_rmsd_bond.auth_asym_id_1            D 
_pdbx_validate_rmsd_bond.auth_comp_id_1            GLU 
_pdbx_validate_rmsd_bond.auth_seq_id_1             180 
_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            CD 
_pdbx_validate_rmsd_bond.auth_asym_id_2            D 
_pdbx_validate_rmsd_bond.auth_comp_id_2            GLU 
_pdbx_validate_rmsd_bond.auth_seq_id_2             180 
_pdbx_validate_rmsd_bond.PDB_ins_code_2            ? 
_pdbx_validate_rmsd_bond.label_alt_id_2            B 
_pdbx_validate_rmsd_bond.bond_value                1.606 
_pdbx_validate_rmsd_bond.bond_target_value         1.515 
_pdbx_validate_rmsd_bond.bond_deviation            0.091 
_pdbx_validate_rmsd_bond.bond_standard_deviation   0.015 
_pdbx_validate_rmsd_bond.linker_flag               N 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 CA B VAL 165 ? ? C  B VAL 165 ? ? N   B LYS 166 ? B 95.85  117.20 -21.35 2.20 Y 
2 1 O  B VAL 165 ? ? C  B VAL 165 ? ? N   B LYS 166 ? B 142.57 122.70 19.87  1.60 Y 
3 1 C  B VAL 165 ? ? N  B LYS 166 ? B CA  B LYS 166 ? B 101.71 121.70 -19.99 2.50 Y 
4 1 CA B LYS 166 ? B C  B LYS 166 ? B N   B TYR 167 ? ? 134.74 117.20 17.54  2.20 Y 
5 1 O  B LYS 166 ? B C  B LYS 166 ? B N   B TYR 167 ? ? 106.39 122.70 -16.31 1.60 Y 
6 1 C  B LYS 166 ? B N  B TYR 167 ? ? CA  B TYR 167 ? ? 139.24 121.70 17.54  2.50 Y 
7 1 NE C ARG 212 ? B CZ C ARG 212 ? B NH2 C ARG 212 ? B 115.75 120.30 -4.55  0.50 N 
8 1 CG C MET 242 ? B SD C MET 242 ? B CE  C MET 242 ? B 111.89 100.20 11.69  1.60 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ASP A 99  ? ? -151.62 72.13   
2  1 ASN A 245 ? ? -91.28  54.93   
3  1 LEU B 26  ? ? 71.05   31.06   
4  1 ASP B 99  ? ? -154.49 79.30   
5  1 ASN B 245 ? ? -97.68  58.12   
6  1 PHE B 252 ? ? -104.20 65.14   
7  1 GLU B 254 ? ? 92.55   -10.59  
8  1 PHE C 7   ? ? -149.65 -157.28 
9  1 ASP C 99  ? ? -164.03 73.72   
10 1 ASP C 235 ? ? -149.40 30.39   
11 1 ASN C 245 ? ? -96.71  53.91   
12 1 ASP D 99  ? ? -154.82 82.28   
13 1 ASN D 245 ? ? -94.22  52.99   
# 
_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 B MET 1   ? B MET 1   
4  1 Y 1 B SER 2   ? B SER 2   
5  1 Y 1 C MET 1   ? C MET 1   
6  1 Y 1 C SER 2   ? C SER 2   
7  1 Y 1 C GLN 263 ? C GLN 263 
8  1 Y 1 D MET 1   ? D MET 1   
9  1 Y 1 D SER 2   ? D SER 2   
10 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  
E1F O18  O  N N 88  
E1F C13  C  Y N 89  
E1F C1   C  Y N 90  
E1F C2   C  Y N 91  
E1F CL1  CL N N 92  
E1F C21  C  Y N 93  
E1F C5   C  Y N 94  
E1F C4   C  Y N 95  
E1F C3   C  Y N 96  
E1F S16  S  N N 97  
E1F N19  N  N N 98  
E1F O17  O  N N 99  
E1F C6   C  N N 100 
E1F O12  O  N N 101 
E1F C7   C  N N 102 
E1F S8   S  N N 103 
E1F C9   C  Y N 104 
E1F N11  N  Y N 105 
E1F C14  C  Y N 106 
E1F C15  C  Y N 107 
E1F N10  N  Y N 108 
E1F H1   H  N N 109 
E1F H2   H  N N 110 
E1F H3   H  N N 111 
E1F H4   H  N N 112 
E1F H5   H  N N 113 
E1F H6   H  N N 114 
E1F H7   H  N N 115 
E1F H8   H  N N 116 
E1F H9   H  N N 117 
E1F H10  H  N N 118 
EDO C1   C  N N 119 
EDO O1   O  N N 120 
EDO C2   C  N N 121 
EDO O2   O  N N 122 
EDO H11  H  N N 123 
EDO H12  H  N N 124 
EDO HO1  H  N N 125 
EDO H21  H  N N 126 
EDO H22  H  N N 127 
EDO HO2  H  N N 128 
GLN N    N  N N 129 
GLN CA   C  N S 130 
GLN C    C  N N 131 
GLN O    O  N N 132 
GLN CB   C  N N 133 
GLN CG   C  N N 134 
GLN CD   C  N N 135 
GLN OE1  O  N N 136 
GLN NE2  N  N N 137 
GLN OXT  O  N N 138 
GLN H    H  N N 139 
GLN H2   H  N N 140 
GLN HA   H  N N 141 
GLN HB2  H  N N 142 
GLN HB3  H  N N 143 
GLN HG2  H  N N 144 
GLN HG3  H  N N 145 
GLN HE21 H  N N 146 
GLN HE22 H  N N 147 
GLN HXT  H  N N 148 
GLU N    N  N N 149 
GLU CA   C  N S 150 
GLU C    C  N N 151 
GLU O    O  N N 152 
GLU CB   C  N N 153 
GLU CG   C  N N 154 
GLU CD   C  N N 155 
GLU OE1  O  N N 156 
GLU OE2  O  N N 157 
GLU OXT  O  N N 158 
GLU H    H  N N 159 
GLU H2   H  N N 160 
GLU HA   H  N N 161 
GLU HB2  H  N N 162 
GLU HB3  H  N N 163 
GLU HG2  H  N N 164 
GLU HG3  H  N N 165 
GLU HE2  H  N N 166 
GLU HXT  H  N N 167 
GLY N    N  N N 168 
GLY CA   C  N N 169 
GLY C    C  N N 170 
GLY O    O  N N 171 
GLY OXT  O  N N 172 
GLY H    H  N N 173 
GLY H2   H  N N 174 
GLY HA2  H  N N 175 
GLY HA3  H  N N 176 
GLY HXT  H  N N 177 
HIS N    N  N N 178 
HIS CA   C  N S 179 
HIS C    C  N N 180 
HIS O    O  N N 181 
HIS CB   C  N N 182 
HIS CG   C  Y N 183 
HIS ND1  N  Y N 184 
HIS CD2  C  Y N 185 
HIS CE1  C  Y N 186 
HIS NE2  N  Y N 187 
HIS OXT  O  N N 188 
HIS H    H  N N 189 
HIS H2   H  N N 190 
HIS HA   H  N N 191 
HIS HB2  H  N N 192 
HIS HB3  H  N N 193 
HIS HD1  H  N N 194 
HIS HD2  H  N N 195 
HIS HE1  H  N N 196 
HIS HE2  H  N N 197 
HIS HXT  H  N N 198 
HOH O    O  N N 199 
HOH H1   H  N N 200 
HOH H2   H  N N 201 
ILE N    N  N N 202 
ILE CA   C  N S 203 
ILE C    C  N N 204 
ILE O    O  N N 205 
ILE CB   C  N S 206 
ILE CG1  C  N N 207 
ILE CG2  C  N N 208 
ILE CD1  C  N N 209 
ILE OXT  O  N N 210 
ILE H    H  N N 211 
ILE H2   H  N N 212 
ILE HA   H  N N 213 
ILE HB   H  N N 214 
ILE HG12 H  N N 215 
ILE HG13 H  N N 216 
ILE HG21 H  N N 217 
ILE HG22 H  N N 218 
ILE HG23 H  N N 219 
ILE HD11 H  N N 220 
ILE HD12 H  N N 221 
ILE HD13 H  N N 222 
ILE HXT  H  N N 223 
LEU N    N  N N 224 
LEU CA   C  N S 225 
LEU C    C  N N 226 
LEU O    O  N N 227 
LEU CB   C  N N 228 
LEU CG   C  N N 229 
LEU CD1  C  N N 230 
LEU CD2  C  N N 231 
LEU OXT  O  N N 232 
LEU H    H  N N 233 
LEU H2   H  N N 234 
LEU HA   H  N N 235 
LEU HB2  H  N N 236 
LEU HB3  H  N N 237 
LEU HG   H  N N 238 
LEU HD11 H  N N 239 
LEU HD12 H  N N 240 
LEU HD13 H  N N 241 
LEU HD21 H  N N 242 
LEU HD22 H  N N 243 
LEU HD23 H  N N 244 
LEU HXT  H  N N 245 
LYS N    N  N N 246 
LYS CA   C  N S 247 
LYS C    C  N N 248 
LYS O    O  N N 249 
LYS CB   C  N N 250 
LYS CG   C  N N 251 
LYS CD   C  N N 252 
LYS CE   C  N N 253 
LYS NZ   N  N N 254 
LYS OXT  O  N N 255 
LYS H    H  N N 256 
LYS H2   H  N N 257 
LYS HA   H  N N 258 
LYS HB2  H  N N 259 
LYS HB3  H  N N 260 
LYS HG2  H  N N 261 
LYS HG3  H  N N 262 
LYS HD2  H  N N 263 
LYS HD3  H  N N 264 
LYS HE2  H  N N 265 
LYS HE3  H  N N 266 
LYS HZ1  H  N N 267 
LYS HZ2  H  N N 268 
LYS HZ3  H  N N 269 
LYS HXT  H  N N 270 
MET N    N  N N 271 
MET CA   C  N S 272 
MET C    C  N N 273 
MET O    O  N N 274 
MET CB   C  N N 275 
MET CG   C  N N 276 
MET SD   S  N N 277 
MET CE   C  N N 278 
MET OXT  O  N N 279 
MET H    H  N N 280 
MET H2   H  N N 281 
MET HA   H  N N 282 
MET HB2  H  N N 283 
MET HB3  H  N N 284 
MET HG2  H  N N 285 
MET HG3  H  N N 286 
MET HE1  H  N N 287 
MET HE2  H  N N 288 
MET HE3  H  N N 289 
MET HXT  H  N N 290 
PHE N    N  N N 291 
PHE CA   C  N S 292 
PHE C    C  N N 293 
PHE O    O  N N 294 
PHE CB   C  N N 295 
PHE CG   C  Y N 296 
PHE CD1  C  Y N 297 
PHE CD2  C  Y N 298 
PHE CE1  C  Y N 299 
PHE CE2  C  Y N 300 
PHE CZ   C  Y N 301 
PHE OXT  O  N N 302 
PHE H    H  N N 303 
PHE H2   H  N N 304 
PHE HA   H  N N 305 
PHE HB2  H  N N 306 
PHE HB3  H  N N 307 
PHE HD1  H  N N 308 
PHE HD2  H  N N 309 
PHE HE1  H  N N 310 
PHE HE2  H  N N 311 
PHE HZ   H  N N 312 
PHE HXT  H  N N 313 
PRO N    N  N N 314 
PRO CA   C  N S 315 
PRO C    C  N N 316 
PRO O    O  N N 317 
PRO CB   C  N N 318 
PRO CG   C  N N 319 
PRO CD   C  N N 320 
PRO OXT  O  N N 321 
PRO H    H  N N 322 
PRO HA   H  N N 323 
PRO HB2  H  N N 324 
PRO HB3  H  N N 325 
PRO HG2  H  N N 326 
PRO HG3  H  N N 327 
PRO HD2  H  N N 328 
PRO HD3  H  N N 329 
PRO HXT  H  N N 330 
SER N    N  N N 331 
SER CA   C  N S 332 
SER C    C  N N 333 
SER O    O  N N 334 
SER CB   C  N N 335 
SER OG   O  N N 336 
SER OXT  O  N N 337 
SER H    H  N N 338 
SER H2   H  N N 339 
SER HA   H  N N 340 
SER HB2  H  N N 341 
SER HB3  H  N N 342 
SER HG   H  N N 343 
SER HXT  H  N N 344 
SO4 S    S  N N 345 
SO4 O1   O  N N 346 
SO4 O2   O  N N 347 
SO4 O3   O  N N 348 
SO4 O4   O  N N 349 
THR N    N  N N 350 
THR CA   C  N S 351 
THR C    C  N N 352 
THR O    O  N N 353 
THR CB   C  N R 354 
THR OG1  O  N N 355 
THR CG2  C  N N 356 
THR OXT  O  N N 357 
THR H    H  N N 358 
THR H2   H  N N 359 
THR HA   H  N N 360 
THR HB   H  N N 361 
THR HG1  H  N N 362 
THR HG21 H  N N 363 
THR HG22 H  N N 364 
THR HG23 H  N N 365 
THR HXT  H  N N 366 
TRP N    N  N N 367 
TRP CA   C  N S 368 
TRP C    C  N N 369 
TRP O    O  N N 370 
TRP CB   C  N N 371 
TRP CG   C  Y N 372 
TRP CD1  C  Y N 373 
TRP CD2  C  Y N 374 
TRP NE1  N  Y N 375 
TRP CE2  C  Y N 376 
TRP CE3  C  Y N 377 
TRP CZ2  C  Y N 378 
TRP CZ3  C  Y N 379 
TRP CH2  C  Y N 380 
TRP OXT  O  N N 381 
TRP H    H  N N 382 
TRP H2   H  N N 383 
TRP HA   H  N N 384 
TRP HB2  H  N N 385 
TRP HB3  H  N N 386 
TRP HD1  H  N N 387 
TRP HE1  H  N N 388 
TRP HE3  H  N N 389 
TRP HZ2  H  N N 390 
TRP HZ3  H  N N 391 
TRP HH2  H  N N 392 
TRP HXT  H  N N 393 
TYR N    N  N N 394 
TYR CA   C  N S 395 
TYR C    C  N N 396 
TYR O    O  N N 397 
TYR CB   C  N N 398 
TYR CG   C  Y N 399 
TYR CD1  C  Y N 400 
TYR CD2  C  Y N 401 
TYR CE1  C  Y N 402 
TYR CE2  C  Y N 403 
TYR CZ   C  Y N 404 
TYR OH   O  N N 405 
TYR OXT  O  N N 406 
TYR H    H  N N 407 
TYR H2   H  N N 408 
TYR HA   H  N N 409 
TYR HB2  H  N N 410 
TYR HB3  H  N N 411 
TYR HD1  H  N N 412 
TYR HD2  H  N N 413 
TYR HE1  H  N N 414 
TYR HE2  H  N N 415 
TYR HH   H  N N 416 
TYR HXT  H  N N 417 
VAL N    N  N N 418 
VAL CA   C  N S 419 
VAL C    C  N N 420 
VAL O    O  N N 421 
VAL CB   C  N N 422 
VAL CG1  C  N N 423 
VAL CG2  C  N N 424 
VAL OXT  O  N N 425 
VAL H    H  N N 426 
VAL H2   H  N N 427 
VAL HA   H  N N 428 
VAL HB   H  N N 429 
VAL HG11 H  N N 430 
VAL HG12 H  N N 431 
VAL HG13 H  N N 432 
VAL HG21 H  N N 433 
VAL HG22 H  N N 434 
VAL HG23 H  N N 435 
VAL HXT  H  N N 436 
ZN  ZN   ZN N N 437 
# 
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  
E1F S8  C9   sing N N 83  
E1F S8  C7   sing N N 84  
E1F N11 C9   doub Y N 85  
E1F N11 C14  sing Y N 86  
E1F C9  N10  sing Y N 87  
E1F C7  C6   sing N N 88  
E1F O12 C6   doub N N 89  
E1F C14 C15  doub Y N 90  
E1F C6  C1   sing N N 91  
E1F C5  C1   doub Y N 92  
E1F C5  C4   sing Y N 93  
E1F C1  C21  sing Y N 94  
E1F N10 C13  doub Y N 95  
E1F C15 C13  sing Y N 96  
E1F C4  C3   doub Y N 97  
E1F C21 C2   doub Y N 98  
E1F C3  C2   sing Y N 99  
E1F C3  S16  sing N N 100 
E1F C2  CL1  sing N N 101 
E1F N19 S16  sing N N 102 
E1F O17 S16  doub N N 103 
E1F S16 O18  doub N N 104 
E1F C13 H1   sing N N 105 
E1F C21 H2   sing N N 106 
E1F C5  H3   sing N N 107 
E1F C4  H4   sing N N 108 
E1F N19 H5   sing N N 109 
E1F N19 H6   sing N N 110 
E1F C7  H7   sing N N 111 
E1F C7  H8   sing N N 112 
E1F C14 H9   sing N N 113 
E1F C15 H10  sing N N 114 
EDO C1  O1   sing N N 115 
EDO C1  C2   sing N N 116 
EDO C1  H11  sing N N 117 
EDO C1  H12  sing N N 118 
EDO O1  HO1  sing N N 119 
EDO C2  O2   sing N N 120 
EDO C2  H21  sing N N 121 
EDO C2  H22  sing N N 122 
EDO O2  HO2  sing N N 123 
GLN N   CA   sing N N 124 
GLN N   H    sing N N 125 
GLN N   H2   sing N N 126 
GLN CA  C    sing N N 127 
GLN CA  CB   sing N N 128 
GLN CA  HA   sing N N 129 
GLN C   O    doub N N 130 
GLN C   OXT  sing N N 131 
GLN CB  CG   sing N N 132 
GLN CB  HB2  sing N N 133 
GLN CB  HB3  sing N N 134 
GLN CG  CD   sing N N 135 
GLN CG  HG2  sing N N 136 
GLN CG  HG3  sing N N 137 
GLN CD  OE1  doub N N 138 
GLN CD  NE2  sing N N 139 
GLN NE2 HE21 sing N N 140 
GLN NE2 HE22 sing N N 141 
GLN OXT HXT  sing N N 142 
GLU N   CA   sing N N 143 
GLU N   H    sing N N 144 
GLU N   H2   sing N N 145 
GLU CA  C    sing N N 146 
GLU CA  CB   sing N N 147 
GLU CA  HA   sing N N 148 
GLU C   O    doub N N 149 
GLU C   OXT  sing N N 150 
GLU CB  CG   sing N N 151 
GLU CB  HB2  sing N N 152 
GLU CB  HB3  sing N N 153 
GLU CG  CD   sing N N 154 
GLU CG  HG2  sing N N 155 
GLU CG  HG3  sing N N 156 
GLU CD  OE1  doub N N 157 
GLU CD  OE2  sing N N 158 
GLU OE2 HE2  sing N N 159 
GLU OXT HXT  sing N N 160 
GLY N   CA   sing N N 161 
GLY N   H    sing N N 162 
GLY N   H2   sing N N 163 
GLY CA  C    sing N N 164 
GLY CA  HA2  sing N N 165 
GLY CA  HA3  sing N N 166 
GLY C   O    doub N N 167 
GLY C   OXT  sing N N 168 
GLY OXT HXT  sing N N 169 
HIS N   CA   sing N N 170 
HIS N   H    sing N N 171 
HIS N   H2   sing N N 172 
HIS CA  C    sing N N 173 
HIS CA  CB   sing N N 174 
HIS CA  HA   sing N N 175 
HIS C   O    doub N N 176 
HIS C   OXT  sing N N 177 
HIS CB  CG   sing N N 178 
HIS CB  HB2  sing N N 179 
HIS CB  HB3  sing N N 180 
HIS CG  ND1  sing Y N 181 
HIS CG  CD2  doub Y N 182 
HIS ND1 CE1  doub Y N 183 
HIS ND1 HD1  sing N N 184 
HIS CD2 NE2  sing Y N 185 
HIS CD2 HD2  sing N N 186 
HIS CE1 NE2  sing Y N 187 
HIS CE1 HE1  sing N N 188 
HIS NE2 HE2  sing N N 189 
HIS OXT HXT  sing N N 190 
HOH O   H1   sing N N 191 
HOH O   H2   sing N N 192 
ILE N   CA   sing N N 193 
ILE N   H    sing N N 194 
ILE N   H2   sing N N 195 
ILE CA  C    sing N N 196 
ILE CA  CB   sing N N 197 
ILE CA  HA   sing N N 198 
ILE C   O    doub N N 199 
ILE C   OXT  sing N N 200 
ILE CB  CG1  sing N N 201 
ILE CB  CG2  sing N N 202 
ILE CB  HB   sing N N 203 
ILE CG1 CD1  sing N N 204 
ILE CG1 HG12 sing N N 205 
ILE CG1 HG13 sing N N 206 
ILE CG2 HG21 sing N N 207 
ILE CG2 HG22 sing N N 208 
ILE CG2 HG23 sing N N 209 
ILE CD1 HD11 sing N N 210 
ILE CD1 HD12 sing N N 211 
ILE CD1 HD13 sing N N 212 
ILE OXT HXT  sing N N 213 
LEU N   CA   sing N N 214 
LEU N   H    sing N N 215 
LEU N   H2   sing N N 216 
LEU CA  C    sing N N 217 
LEU CA  CB   sing N N 218 
LEU CA  HA   sing N N 219 
LEU C   O    doub N N 220 
LEU C   OXT  sing N N 221 
LEU CB  CG   sing N N 222 
LEU CB  HB2  sing N N 223 
LEU CB  HB3  sing N N 224 
LEU CG  CD1  sing N N 225 
LEU CG  CD2  sing N N 226 
LEU CG  HG   sing N N 227 
LEU CD1 HD11 sing N N 228 
LEU CD1 HD12 sing N N 229 
LEU CD1 HD13 sing N N 230 
LEU CD2 HD21 sing N N 231 
LEU CD2 HD22 sing N N 232 
LEU CD2 HD23 sing N N 233 
LEU OXT HXT  sing N N 234 
LYS N   CA   sing N N 235 
LYS N   H    sing N N 236 
LYS N   H2   sing N N 237 
LYS CA  C    sing N N 238 
LYS CA  CB   sing N N 239 
LYS CA  HA   sing N N 240 
LYS C   O    doub N N 241 
LYS C   OXT  sing N N 242 
LYS CB  CG   sing N N 243 
LYS CB  HB2  sing N N 244 
LYS CB  HB3  sing N N 245 
LYS CG  CD   sing N N 246 
LYS CG  HG2  sing N N 247 
LYS CG  HG3  sing N N 248 
LYS CD  CE   sing N N 249 
LYS CD  HD2  sing N N 250 
LYS CD  HD3  sing N N 251 
LYS CE  NZ   sing N N 252 
LYS CE  HE2  sing N N 253 
LYS CE  HE3  sing N N 254 
LYS NZ  HZ1  sing N N 255 
LYS NZ  HZ2  sing N N 256 
LYS NZ  HZ3  sing N N 257 
LYS OXT HXT  sing N N 258 
MET N   CA   sing N N 259 
MET N   H    sing N N 260 
MET N   H2   sing N N 261 
MET CA  C    sing N N 262 
MET CA  CB   sing N N 263 
MET CA  HA   sing N N 264 
MET C   O    doub N N 265 
MET C   OXT  sing N N 266 
MET CB  CG   sing N N 267 
MET CB  HB2  sing N N 268 
MET CB  HB3  sing N N 269 
MET CG  SD   sing N N 270 
MET CG  HG2  sing N N 271 
MET CG  HG3  sing N N 272 
MET SD  CE   sing N N 273 
MET CE  HE1  sing N N 274 
MET CE  HE2  sing N N 275 
MET CE  HE3  sing N N 276 
MET OXT HXT  sing N N 277 
PHE N   CA   sing N N 278 
PHE N   H    sing N N 279 
PHE N   H2   sing N N 280 
PHE CA  C    sing N N 281 
PHE CA  CB   sing N N 282 
PHE CA  HA   sing N N 283 
PHE C   O    doub N N 284 
PHE C   OXT  sing N N 285 
PHE CB  CG   sing N N 286 
PHE CB  HB2  sing N N 287 
PHE CB  HB3  sing N N 288 
PHE CG  CD1  doub Y N 289 
PHE CG  CD2  sing Y N 290 
PHE CD1 CE1  sing Y N 291 
PHE CD1 HD1  sing N N 292 
PHE CD2 CE2  doub Y N 293 
PHE CD2 HD2  sing N N 294 
PHE CE1 CZ   doub Y N 295 
PHE CE1 HE1  sing N N 296 
PHE CE2 CZ   sing Y N 297 
PHE CE2 HE2  sing N N 298 
PHE CZ  HZ   sing N N 299 
PHE OXT HXT  sing N N 300 
PRO N   CA   sing N N 301 
PRO N   CD   sing N N 302 
PRO N   H    sing N N 303 
PRO CA  C    sing N N 304 
PRO CA  CB   sing N N 305 
PRO CA  HA   sing N N 306 
PRO C   O    doub N N 307 
PRO C   OXT  sing N N 308 
PRO CB  CG   sing N N 309 
PRO CB  HB2  sing N N 310 
PRO CB  HB3  sing N N 311 
PRO CG  CD   sing N N 312 
PRO CG  HG2  sing N N 313 
PRO CG  HG3  sing N N 314 
PRO CD  HD2  sing N N 315 
PRO CD  HD3  sing N N 316 
PRO OXT HXT  sing N N 317 
SER N   CA   sing N N 318 
SER N   H    sing N N 319 
SER N   H2   sing N N 320 
SER CA  C    sing N N 321 
SER CA  CB   sing N N 322 
SER CA  HA   sing N N 323 
SER C   O    doub N N 324 
SER C   OXT  sing N N 325 
SER CB  OG   sing N N 326 
SER CB  HB2  sing N N 327 
SER CB  HB3  sing N N 328 
SER OG  HG   sing N N 329 
SER OXT HXT  sing N N 330 
SO4 S   O1   doub N N 331 
SO4 S   O2   doub N N 332 
SO4 S   O3   sing N N 333 
SO4 S   O4   sing N N 334 
THR N   CA   sing N N 335 
THR N   H    sing N N 336 
THR N   H2   sing N N 337 
THR CA  C    sing N N 338 
THR CA  CB   sing N N 339 
THR CA  HA   sing N N 340 
THR C   O    doub N N 341 
THR C   OXT  sing N N 342 
THR CB  OG1  sing N N 343 
THR CB  CG2  sing N N 344 
THR CB  HB   sing N N 345 
THR OG1 HG1  sing N N 346 
THR CG2 HG21 sing N N 347 
THR CG2 HG22 sing N N 348 
THR CG2 HG23 sing N N 349 
THR OXT HXT  sing N N 350 
TRP N   CA   sing N N 351 
TRP N   H    sing N N 352 
TRP N   H2   sing N N 353 
TRP CA  C    sing N N 354 
TRP CA  CB   sing N N 355 
TRP CA  HA   sing N N 356 
TRP C   O    doub N N 357 
TRP C   OXT  sing N N 358 
TRP CB  CG   sing N N 359 
TRP CB  HB2  sing N N 360 
TRP CB  HB3  sing N N 361 
TRP CG  CD1  doub Y N 362 
TRP CG  CD2  sing Y N 363 
TRP CD1 NE1  sing Y N 364 
TRP CD1 HD1  sing N N 365 
TRP CD2 CE2  doub Y N 366 
TRP CD2 CE3  sing Y N 367 
TRP NE1 CE2  sing Y N 368 
TRP NE1 HE1  sing N N 369 
TRP CE2 CZ2  sing Y N 370 
TRP CE3 CZ3  doub Y N 371 
TRP CE3 HE3  sing N N 372 
TRP CZ2 CH2  doub Y N 373 
TRP CZ2 HZ2  sing N N 374 
TRP CZ3 CH2  sing Y N 375 
TRP CZ3 HZ3  sing N N 376 
TRP CH2 HH2  sing N N 377 
TRP OXT HXT  sing N N 378 
TYR N   CA   sing N N 379 
TYR N   H    sing N N 380 
TYR N   H2   sing N N 381 
TYR CA  C    sing N N 382 
TYR CA  CB   sing N N 383 
TYR CA  HA   sing N N 384 
TYR C   O    doub N N 385 
TYR C   OXT  sing N N 386 
TYR CB  CG   sing N N 387 
TYR CB  HB2  sing N N 388 
TYR CB  HB3  sing N N 389 
TYR CG  CD1  doub Y N 390 
TYR CG  CD2  sing Y N 391 
TYR CD1 CE1  sing Y N 392 
TYR CD1 HD1  sing N N 393 
TYR CD2 CE2  doub Y N 394 
TYR CD2 HD2  sing N N 395 
TYR CE1 CZ   doub Y N 396 
TYR CE1 HE1  sing N N 397 
TYR CE2 CZ   sing Y N 398 
TYR CE2 HE2  sing N N 399 
TYR CZ  OH   sing N N 400 
TYR OH  HH   sing N N 401 
TYR OXT HXT  sing N N 402 
VAL N   CA   sing N N 403 
VAL N   H    sing N N 404 
VAL N   H2   sing N N 405 
VAL CA  C    sing N N 406 
VAL CA  CB   sing N N 407 
VAL CA  HA   sing N N 408 
VAL C   O    doub N N 409 
VAL C   OXT  sing N N 410 
VAL CB  CG1  sing N N 411 
VAL CB  CG2  sing N N 412 
VAL CB  HB   sing N N 413 
VAL CG1 HG11 sing N N 414 
VAL CG1 HG12 sing N N 415 
VAL CG1 HG13 sing N N 416 
VAL CG2 HG21 sing N N 417 
VAL CG2 HG22 sing N N 418 
VAL CG2 HG23 sing N N 419 
VAL OXT HXT  sing N N 420 
# 
_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                    4KP5 
_atom_sites.fract_transf_matrix[1][1]   0.012937 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.004406 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.013485 
_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]   0.011559 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
# 
loop_
_atom_type.symbol 
C  
CL 
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1     N  N   A LYS A 1 3   ? 16.540  17.386  18.348  0.50 23.58 ? 3   LYS A N   1 
ATOM   2     N  N   B LYS A 1 3   ? 16.594  16.648  19.187  0.50 22.24 ? 3   LYS A N   1 
ATOM   3     C  CA  A LYS A 1 3   ? 17.463  16.175  18.324  0.50 23.91 ? 3   LYS A CA  1 
ATOM   4     C  CA  B LYS A 1 3   ? 17.322  16.526  17.835  0.50 22.55 ? 3   LYS A CA  1 
ATOM   5     C  C   A LYS A 1 3   ? 16.696  14.909  18.051  0.50 21.32 ? 3   LYS A C   1 
ATOM   6     C  C   B LYS A 1 3   ? 16.889  15.419  16.841  0.50 21.51 ? 3   LYS A C   1 
ATOM   7     O  O   A LYS A 1 3   ? 15.656  14.625  18.690  0.50 21.87 ? 3   LYS A O   1 
ATOM   8     O  O   B LYS A 1 3   ? 16.398  15.768  15.786  0.50 22.64 ? 3   LYS A O   1 
ATOM   9     C  CB  A LYS A 1 3   ? 18.249  15.982  19.623  0.50 23.25 ? 3   LYS A CB  1 
ATOM   10    C  CB  B LYS A 1 3   ? 18.849  16.507  18.009  0.50 21.63 ? 3   LYS A CB  1 
ATOM   11    C  CG  A LYS A 1 3   ? 19.668  15.483  19.388  0.50 25.74 ? 3   LYS A CG  1 
ATOM   12    C  CG  B LYS A 1 3   ? 19.626  16.322  16.696  0.50 21.95 ? 3   LYS A CG  1 
ATOM   13    C  CD  A LYS A 1 3   ? 19.844  13.971  19.228  0.50 24.66 ? 3   LYS A CD  1 
ATOM   14    C  CD  B LYS A 1 3   ? 18.917  16.878  15.470  0.50 20.64 ? 3   LYS A CD  1 
ATOM   15    C  CE  A LYS A 1 3   ? 21.311  13.665  19.350  0.50 27.07 ? 3   LYS A CE  1 
ATOM   16    C  CE  B LYS A 1 3   ? 18.755  18.403  15.579  0.50 25.48 ? 3   LYS A CE  1 
ATOM   17    N  NZ  A LYS A 1 3   ? 21.947  13.640  18.008  0.50 24.11 ? 3   LYS A NZ  1 
ATOM   18    N  NZ  B LYS A 1 3   ? 19.788  19.076  16.460  0.50 29.47 ? 3   LYS A NZ  1 
ATOM   19    N  N   . TRP A 1 4   ? 17.220  14.138  17.106  1.00 19.87 ? 4   TRP A N   1 
ATOM   20    C  CA  . TRP A 1 4   ? 16.413  13.037  16.545  1.00 15.83 ? 4   TRP A CA  1 
ATOM   21    C  C   . TRP A 1 4   ? 16.367  11.908  17.558  1.00 16.00 ? 4   TRP A C   1 
ATOM   22    O  O   . TRP A 1 4   ? 17.325  11.674  18.322  1.00 15.77 ? 4   TRP A O   1 
ATOM   23    C  CB  . TRP A 1 4   ? 16.966  12.570  15.202  1.00 14.42 ? 4   TRP A CB  1 
ATOM   24    C  CG  . TRP A 1 4   ? 18.294  11.941  15.192  1.00 12.71 ? 4   TRP A CG  1 
ATOM   25    C  CD1 . TRP A 1 4   ? 19.520  12.529  14.948  1.00 16.04 ? 4   TRP A CD1 1 
ATOM   26    C  CD2 . TRP A 1 4   ? 18.556  10.530  15.307  1.00 11.75 ? 4   TRP A CD2 1 
ATOM   27    N  NE1 . TRP A 1 4   ? 20.512  11.597  14.897  1.00 16.36 ? 4   TRP A NE1 1 
ATOM   28    C  CE2 . TRP A 1 4   ? 19.958  10.329  15.101  1.00 11.68 ? 4   TRP A CE2 1 
ATOM   29    C  CE3 . TRP A 1 4   ? 17.742  9.405   15.499  1.00 10.20 ? 4   TRP A CE3 1 
ATOM   30    C  CZ2 . TRP A 1 4   ? 20.528  9.047   15.167  1.00 10.92 ? 4   TRP A CZ2 1 
ATOM   31    C  CZ3 . TRP A 1 4   ? 18.293  8.177   15.494  1.00 11.13 ? 4   TRP A CZ3 1 
ATOM   32    C  CH2 . TRP A 1 4   ? 19.666  7.992   15.341  1.00 11.35 ? 4   TRP A CH2 1 
ATOM   33    N  N   . THR A 1 5   ? 15.240  11.228  17.564  1.00 14.28 ? 5   THR A N   1 
ATOM   34    C  CA  . THR A 1 5   ? 15.043  10.077  18.463  1.00 13.38 ? 5   THR A CA  1 
ATOM   35    C  C   . THR A 1 5   ? 14.260  9.000   17.707  1.00 14.09 ? 5   THR A C   1 
ATOM   36    O  O   . THR A 1 5   ? 13.934  9.131   16.535  1.00 14.11 ? 5   THR A O   1 
ATOM   37    C  CB  . THR A 1 5   ? 14.183  10.407  19.687  1.00 16.56 ? 5   THR A CB  1 
ATOM   38    O  OG1 . THR A 1 5   ? 12.859  10.672  19.165  1.00 19.22 ? 5   THR A OG1 1 
ATOM   39    C  CG2 . THR A 1 5   ? 14.730  11.750  20.282  1.00 17.13 ? 5   THR A CG2 1 
ATOM   40    N  N   . TYR A 1 6   ? 13.995  7.890   18.399  1.00 14.28 ? 6   TYR A N   1 
ATOM   41    C  CA  . TYR A 1 6   ? 13.132  6.862   17.853  1.00 11.83 ? 6   TYR A CA  1 
ATOM   42    C  C   . TYR A 1 6   ? 11.722  6.829   18.417  1.00 14.51 ? 6   TYR A C   1 
ATOM   43    O  O   . TYR A 1 6   ? 10.939  5.932   18.220  1.00 14.67 ? 6   TYR A O   1 
ATOM   44    C  CB  . TYR A 1 6   ? 13.729  5.429   18.088  1.00 12.84 ? 6   TYR A CB  1 
ATOM   45    C  CG  . TYR A 1 6   ? 14.982  5.185   17.309  1.00 9.69  ? 6   TYR A CG  1 
ATOM   46    C  CD1 . TYR A 1 6   ? 16.235  5.477   17.835  1.00 10.27 ? 6   TYR A CD1 1 
ATOM   47    C  CD2 . TYR A 1 6   ? 14.889  4.612   16.037  1.00 11.57 ? 6   TYR A CD2 1 
ATOM   48    C  CE1 . TYR A 1 6   ? 17.398  5.198   17.112  1.00 11.97 ? 6   TYR A CE1 1 
ATOM   49    C  CE2 . TYR A 1 6   ? 16.033  4.286   15.262  1.00 9.96  ? 6   TYR A CE2 1 
ATOM   50    C  CZ  . TYR A 1 6   ? 17.319  4.590   15.811  1.00 11.61 ? 6   TYR A CZ  1 
ATOM   51    O  OH  . TYR A 1 6   ? 18.394  4.281   15.114  1.00 11.33 ? 6   TYR A OH  1 
ATOM   52    N  N   . PHE A 1 7   ? 11.397  7.839   19.241  1.00 21.66 ? 7   PHE A N   1 
ATOM   53    C  CA  . PHE A 1 7   ? 10.093  7.814   19.957  1.00 24.29 ? 7   PHE A CA  1 
ATOM   54    C  C   . PHE A 1 7   ? 9.691   9.241   20.235  1.00 27.10 ? 7   PHE A C   1 
ATOM   55    O  O   . PHE A 1 7   ? 10.526  10.061  20.668  1.00 27.11 ? 7   PHE A O   1 
ATOM   56    C  CB  . PHE A 1 7   ? 10.161  6.972   21.262  1.00 27.27 ? 7   PHE A CB  1 
ATOM   57    C  CG  . PHE A 1 7   ? 8.838   6.925   22.091  1.00 27.87 ? 7   PHE A CG  1 
ATOM   58    C  CD1 . PHE A 1 7   ? 7.905   5.867   21.904  1.00 34.93 ? 7   PHE A CD1 1 
ATOM   59    C  CD2 . PHE A 1 7   ? 8.566   7.914   23.087  1.00 33.45 ? 7   PHE A CD2 1 
ATOM   60    C  CE1 . PHE A 1 7   ? 6.679   5.804   22.653  1.00 33.21 ? 7   PHE A CE1 1 
ATOM   61    C  CE2 . PHE A 1 7   ? 7.343   7.862   23.862  1.00 31.63 ? 7   PHE A CE2 1 
ATOM   62    C  CZ  . PHE A 1 7   ? 6.413   6.792   23.642  1.00 36.09 ? 7   PHE A CZ  1 
ATOM   63    N  N   . GLY A 1 8   ? 8.408   9.511   20.006  1.00 26.08 ? 8   GLY A N   1 
ATOM   64    C  CA  . GLY A 1 8   ? 7.778   10.817  20.346  1.00 27.53 ? 8   GLY A CA  1 
ATOM   65    C  C   . GLY A 1 8   ? 7.963   11.756  19.152  1.00 28.98 ? 8   GLY A C   1 
ATOM   66    O  O   . GLY A 1 8   ? 8.166   11.307  17.991  1.00 30.36 ? 8   GLY A O   1 
ATOM   67    N  N   . PRO A 1 9   ? 7.840   13.061  19.382  1.00 26.57 ? 9   PRO A N   1 
ATOM   68    C  CA  . PRO A 1 9   ? 7.783   14.111  18.370  1.00 25.93 ? 9   PRO A CA  1 
ATOM   69    C  C   . PRO A 1 9   ? 8.953   14.137  17.433  1.00 23.85 ? 9   PRO A C   1 
ATOM   70    O  O   . PRO A 1 9   ? 8.867   14.730  16.322  1.00 20.46 ? 9   PRO A O   1 
ATOM   71    C  CB  . PRO A 1 9   ? 7.855   15.408  19.239  1.00 25.71 ? 9   PRO A CB  1 
ATOM   72    C  CG  . PRO A 1 9   ? 7.269   15.001  20.453  1.00 27.89 ? 9   PRO A CG  1 
ATOM   73    C  CD  . PRO A 1 9   ? 7.705   13.634  20.734  1.00 27.09 ? 9   PRO A CD  1 
ATOM   74    N  N   . ASP A 1 10  ? 10.073  13.573  17.887  1.00 22.04 ? 10  ASP A N   1 
ATOM   75    C  CA  . ASP A 1 10  ? 11.270  13.686  17.124  1.00 20.47 ? 10  ASP A CA  1 
ATOM   76    C  C   . ASP A 1 10  ? 11.708  12.338  16.460  1.00 18.59 ? 10  ASP A C   1 
ATOM   77    O  O   . ASP A 1 10  ? 12.904  12.181  16.014  1.00 16.54 ? 10  ASP A O   1 
ATOM   78    C  CB  . ASP A 1 10  ? 12.432  14.241  18.000  1.00 21.05 ? 10  ASP A CB  1 
ATOM   79    C  CG  . ASP A 1 10  ? 12.206  15.697  18.432  1.00 27.78 ? 10  ASP A CG  1 
ATOM   80    O  OD1 . ASP A 1 10  ? 12.026  16.569  17.546  1.00 32.00 ? 10  ASP A OD1 1 
ATOM   81    O  OD2 . ASP A 1 10  ? 12.254  15.961  19.690  1.00 33.13 ? 10  ASP A OD2 1 
ATOM   82    N  N   . GLY A 1 11  ? 10.698  11.445  16.415  1.00 17.66 ? 11  GLY A N   1 
ATOM   83    C  CA  . GLY A 1 11  ? 10.844  10.022  15.960  1.00 10.36 ? 11  GLY A CA  1 
ATOM   84    C  C   . GLY A 1 11  ? 10.920  10.017  14.456  1.00 12.10 ? 11  GLY A C   1 
ATOM   85    O  O   . GLY A 1 11  ? 10.935  11.036  13.793  1.00 10.76 ? 11  GLY A O   1 
ATOM   86    N  N   . GLU A 1 12  ? 11.024  8.824   13.914  1.00 9.42  ? 12  GLU A N   1 
ATOM   87    C  CA  . GLU A 1 12  ? 11.370  8.609   12.538  1.00 8.46  ? 12  GLU A CA  1 
ATOM   88    C  C   . GLU A 1 12  ? 10.505  9.262   11.453  1.00 8.23  ? 12  GLU A C   1 
ATOM   89    O  O   . GLU A 1 12  ? 11.002  9.574   10.407  1.00 7.51  ? 12  GLU A O   1 
ATOM   90    C  CB  . GLU A 1 12  ? 11.553  7.070   12.242  1.00 10.04 ? 12  GLU A CB  1 
ATOM   91    C  CG  . GLU A 1 12  ? 10.219  6.267   12.202  1.00 8.25  ? 12  GLU A CG  1 
ATOM   92    C  CD  . GLU A 1 12  ? 10.529  4.818   12.355  1.00 8.32  ? 12  GLU A CD  1 
ATOM   93    O  OE1 . GLU A 1 12  ? 10.840  4.161   11.337  1.00 7.43  ? 12  GLU A OE1 1 
ATOM   94    O  OE2 . GLU A 1 12  ? 10.526  4.358   13.510  1.00 9.61  ? 12  GLU A OE2 1 
ATOM   95    N  N   . ASN A 1 13  ? 9.199   9.440   11.748  1.00 9.21  ? 13  ASN A N   1 
ATOM   96    C  CA  . ASN A 1 13  ? 8.380   10.080  10.752  1.00 9.07  ? 13  ASN A CA  1 
ATOM   97    C  C   . ASN A 1 13  ? 8.724   11.539  10.580  1.00 9.10  ? 13  ASN A C   1 
ATOM   98    O  O   . ASN A 1 13  ? 8.330   12.081  9.561   1.00 9.35  ? 13  ASN A O   1 
ATOM   99    C  CB  . ASN A 1 13  ? 6.884   9.948   11.035  1.00 9.88  ? 13  ASN A CB  1 
ATOM   100   C  CG  . ASN A 1 13  ? 6.374   8.517   10.898  1.00 9.44  ? 13  ASN A CG  1 
ATOM   101   O  OD1 . ASN A 1 13  ? 7.074   7.661   10.375  1.00 9.34  ? 13  ASN A OD1 1 
ATOM   102   N  ND2 . ASN A 1 13  ? 5.141   8.285   11.357  1.00 9.77  ? 13  ASN A ND2 1 
ATOM   103   N  N   A SER A 1 14  ? 9.390   12.087  11.621  0.50 8.50  ? 14  SER A N   1 
ATOM   104   N  N   B SER A 1 14  ? 9.497   12.135  11.467  0.50 9.64  ? 14  SER A N   1 
ATOM   105   C  CA  A SER A 1 14  ? 9.813   13.513  11.682  0.50 7.90  ? 14  SER A CA  1 
ATOM   106   C  CA  B SER A 1 14  ? 9.783   13.591  11.322  0.50 8.78  ? 14  SER A CA  1 
ATOM   107   C  C   A SER A 1 14  ? 11.270  13.767  11.267  0.50 8.36  ? 14  SER A C   1 
ATOM   108   C  C   B SER A 1 14  ? 11.245  13.777  10.956  0.50 10.05 ? 14  SER A C   1 
ATOM   109   O  O   A SER A 1 14  ? 11.665  14.915  11.125  0.50 8.56  ? 14  SER A O   1 
ATOM   110   O  O   B SER A 1 14  ? 11.691  14.865  10.671  0.50 8.54  ? 14  SER A O   1 
ATOM   111   C  CB  A SER A 1 14  ? 9.598   14.034  13.095  0.50 7.78  ? 14  SER A CB  1 
ATOM   112   C  CB  B SER A 1 14  ? 9.668   14.246  12.682  0.50 9.94  ? 14  SER A CB  1 
ATOM   113   O  OG  A SER A 1 14  ? 8.182   14.214  13.168  0.50 10.65 ? 14  SER A OG  1 
ATOM   114   O  OG  B SER A 1 14  ? 10.599  13.631  13.549  0.50 16.91 ? 14  SER A OG  1 
ATOM   115   N  N   . TRP A 1 15  ? 12.041  12.719  10.941  1.00 8.56  ? 15  TRP A N   1 
ATOM   116   C  CA  . TRP A 1 15  ? 13.493  12.929  10.580  1.00 8.70  ? 15  TRP A CA  1 
ATOM   117   C  C   . TRP A 1 15  ? 13.630  13.716  9.278   1.00 11.08 ? 15  TRP A C   1 
ATOM   118   O  O   . TRP A 1 15  ? 14.585  14.529  9.136   1.00 9.81  ? 15  TRP A O   1 
ATOM   119   C  CB  . TRP A 1 15  ? 14.166  11.574  10.339  1.00 10.17 ? 15  TRP A CB  1 
ATOM   120   C  CG  . TRP A 1 15  ? 14.373  10.742  11.601  1.00 10.06 ? 15  TRP A CG  1 
ATOM   121   C  CD1 . TRP A 1 15  ? 14.084  11.035  12.844  1.00 9.33  ? 15  TRP A CD1 1 
ATOM   122   C  CD2 . TRP A 1 15  ? 14.744  9.353   11.605  1.00 8.55  ? 15  TRP A CD2 1 
ATOM   123   N  NE1 . TRP A 1 15  ? 14.366  9.969   13.741  1.00 9.80  ? 15  TRP A NE1 1 
ATOM   124   C  CE2 . TRP A 1 15  ? 14.849  8.944   12.965  1.00 5.78  ? 15  TRP A CE2 1 
ATOM   125   C  CE3 . TRP A 1 15  ? 15.205  8.522   10.593  1.00 6.29  ? 15  TRP A CE3 1 
ATOM   126   C  CZ2 . TRP A 1 15  ? 15.275  7.594   13.312  1.00 6.53  ? 15  TRP A CZ2 1 
ATOM   127   C  CZ3 . TRP A 1 15  ? 15.637  7.175   10.930  1.00 6.92  ? 15  TRP A CZ3 1 
ATOM   128   C  CH2 . TRP A 1 15  ? 15.657  6.804   12.288  1.00 7.68  ? 15  TRP A CH2 1 
ATOM   129   N  N   . SER A 1 16  ? 12.702  13.597  8.335   1.00 9.19  ? 16  SER A N   1 
ATOM   130   C  CA  . SER A 1 16  ? 12.897  14.208  7.031   1.00 9.27  ? 16  SER A CA  1 
ATOM   131   C  C   . SER A 1 16  ? 12.830  15.768  7.118   1.00 8.57  ? 16  SER A C   1 
ATOM   132   O  O   . SER A 1 16  ? 13.200  16.425  6.140   1.00 9.73  ? 16  SER A O   1 
ATOM   133   C  CB  . SER A 1 16  ? 11.804  13.768  6.020   1.00 8.49  ? 16  SER A CB  1 
ATOM   134   O  OG  . SER A 1 16  ? 10.532  14.131  6.540   1.00 11.27 ? 16  SER A OG  1 
ATOM   135   N  N   A LYS A 1 17  ? 12.306  16.235  8.263   0.25 8.74  ? 17  LYS A N   1 
ATOM   136   N  N   B LYS A 1 17  ? 12.344  16.258  8.256   0.25 8.33  ? 17  LYS A N   1 
ATOM   137   N  N   C LYS A 1 17  ? 12.264  16.308  8.154   0.50 9.34  ? 17  LYS A N   1 
ATOM   138   C  CA  A LYS A 1 17  ? 12.190  17.691  8.531   0.25 8.00  ? 17  LYS A CA  1 
ATOM   139   C  CA  B LYS A 1 17  ? 12.288  17.726  8.454   0.25 7.00  ? 17  LYS A CA  1 
ATOM   140   C  CA  C LYS A 1 17  ? 12.263  17.808  8.145   0.50 7.46  ? 17  LYS A CA  1 
ATOM   141   C  C   A LYS A 1 17  ? 13.546  18.352  8.397   0.25 8.97  ? 17  LYS A C   1 
ATOM   142   C  C   B LYS A 1 17  ? 13.634  18.338  8.700   0.25 7.22  ? 17  LYS A C   1 
ATOM   143   C  C   C LYS A 1 17  ? 13.722  18.348  8.150   0.50 9.61  ? 17  LYS A C   1 
ATOM   144   O  O   A LYS A 1 17  ? 13.622  19.354  7.702   0.25 7.61  ? 17  LYS A O   1 
ATOM   145   O  O   B LYS A 1 17  ? 13.900  19.401  8.158   0.25 4.56  ? 17  LYS A O   1 
ATOM   146   O  O   C LYS A 1 17  ? 14.179  19.162  7.295   0.50 7.94  ? 17  LYS A O   1 
ATOM   147   C  CB  A LYS A 1 17  ? 11.514  18.027  9.885   0.25 8.43  ? 17  LYS A CB  1 
ATOM   148   C  CB  B LYS A 1 17  ? 11.338  18.137  9.560   0.25 7.42  ? 17  LYS A CB  1 
ATOM   149   C  CB  C LYS A 1 17  ? 11.488  18.276  9.372   0.50 7.44  ? 17  LYS A CB  1 
ATOM   150   C  CG  A LYS A 1 17  ? 10.068  17.485  10.011  0.25 4.02  ? 17  LYS A CG  1 
ATOM   151   C  CG  B LYS A 1 17  ? 9.918   18.056  9.152   0.25 7.06  ? 17  LYS A CG  1 
ATOM   152   C  CG  C LYS A 1 17  ? 11.437  19.805  9.513   0.50 8.41  ? 17  LYS A CG  1 
ATOM   153   C  CD  A LYS A 1 17  ? 9.347   18.021  11.178  0.25 6.37  ? 17  LYS A CD  1 
ATOM   154   C  CD  B LYS A 1 17  ? 9.086   18.878  10.123  0.25 10.52 ? 17  LYS A CD  1 
ATOM   155   C  CD  C LYS A 1 17  ? 10.580  20.241  10.678  0.50 11.13 ? 17  LYS A CD  1 
ATOM   156   C  CE  A LYS A 1 17  ? 7.974   17.343  11.256  0.25 4.12  ? 17  LYS A CE  1 
ATOM   157   C  CE  B LYS A 1 17  ? 7.882   18.130  10.625  0.25 15.94 ? 17  LYS A CE  1 
ATOM   158   C  CE  C LYS A 1 17  ? 9.098   20.173  10.393  0.50 12.75 ? 17  LYS A CE  1 
ATOM   159   N  NZ  A LYS A 1 17  ? 7.501   17.685  12.599  0.25 7.25  ? 17  LYS A NZ  1 
ATOM   160   N  NZ  B LYS A 1 17  ? 8.135   16.695  10.536  0.25 10.64 ? 17  LYS A NZ  1 
ATOM   161   N  NZ  C LYS A 1 17  ? 8.158   20.410  11.622  0.50 17.14 ? 17  LYS A NZ  1 
ATOM   162   N  N   A LYS A 1 18  ? 14.596  17.784  9.015   0.50 8.47  ? 18  LYS A N   1 
ATOM   163   N  N   B LYS A 1 18  ? 14.453  17.775  9.578   0.50 5.55  ? 18  LYS A N   1 
ATOM   164   C  CA  A LYS A 1 18  ? 15.892  18.425  9.148   0.50 10.69 ? 18  LYS A CA  1 
ATOM   165   C  CA  B LYS A 1 18  ? 15.859  18.194  9.587   0.50 8.85  ? 18  LYS A CA  1 
ATOM   166   C  C   A LYS A 1 18  ? 16.828  17.653  8.247   0.50 11.81 ? 18  LYS A C   1 
ATOM   167   C  C   B LYS A 1 18  ? 16.871  17.503  8.660   0.50 9.45  ? 18  LYS A C   1 
ATOM   168   O  O   A LYS A 1 18  ? 17.844  18.149  7.745   0.50 12.48 ? 18  LYS A O   1 
ATOM   169   O  O   B LYS A 1 18  ? 18.016  17.947  8.480   0.50 9.84  ? 18  LYS A O   1 
ATOM   170   C  CB  A LYS A 1 18  ? 16.392  18.426  10.607  0.50 11.07 ? 18  LYS A CB  1 
ATOM   171   C  CB  B LYS A 1 18  ? 16.319  18.022  11.027  0.50 11.26 ? 18  LYS A CB  1 
ATOM   172   C  CG  A LYS A 1 18  ? 15.641  19.335  11.586  0.50 14.38 ? 18  LYS A CG  1 
ATOM   173   C  CG  B LYS A 1 18  ? 17.512  18.836  11.454  0.50 16.59 ? 18  LYS A CG  1 
ATOM   174   C  CD  A LYS A 1 18  ? 16.429  19.464  12.956  0.50 16.58 ? 18  LYS A CD  1 
ATOM   175   C  CD  B LYS A 1 18  ? 18.829  18.281  11.152  0.50 20.92 ? 18  LYS A CD  1 
ATOM   176   C  CE  A LYS A 1 18  ? 17.898  18.837  12.926  0.50 14.82 ? 18  LYS A CE  1 
ATOM   177   C  CE  B LYS A 1 18  ? 19.867  18.800  12.174  0.50 16.83 ? 18  LYS A CE  1 
ATOM   178   N  NZ  A LYS A 1 18  ? 19.084  19.701  13.360  0.50 25.19 ? 18  LYS A NZ  1 
ATOM   179   N  NZ  B LYS A 1 18  ? 19.218  19.546  13.285  0.50 24.30 ? 18  LYS A NZ  1 
ATOM   180   N  N   . TYR A 1 19  ? 16.489  16.373  8.039   1.00 10.07 ? 19  TYR A N   1 
ATOM   181   C  CA  . TYR A 1 19  ? 17.391  15.492  7.313   1.00 9.89  ? 19  TYR A CA  1 
ATOM   182   C  C   . TYR A 1 19  ? 16.668  15.055  6.027   1.00 10.96 ? 19  TYR A C   1 
ATOM   183   O  O   . TYR A 1 19  ? 15.986  13.969  5.991   1.00 9.31  ? 19  TYR A O   1 
ATOM   184   C  CB  . TYR A 1 19  ? 17.717  14.241  8.152   1.00 10.77 ? 19  TYR A CB  1 
ATOM   185   C  CG  . TYR A 1 19  ? 18.375  14.600  9.416   1.00 7.75  ? 19  TYR A CG  1 
ATOM   186   C  CD1 . TYR A 1 19  ? 19.785  14.917  9.422   1.00 10.64 ? 19  TYR A CD1 1 
ATOM   187   C  CD2 . TYR A 1 19  ? 17.693  14.659  10.567  1.00 9.77  ? 19  TYR A CD2 1 
ATOM   188   C  CE1 . TYR A 1 19  ? 20.463  15.316  10.618  1.00 10.88 ? 19  TYR A CE1 1 
ATOM   189   C  CE2 . TYR A 1 19  ? 18.335  14.967  11.807  1.00 11.86 ? 19  TYR A CE2 1 
ATOM   190   C  CZ  . TYR A 1 19  ? 19.703  15.269  11.807  1.00 11.54 ? 19  TYR A CZ  1 
ATOM   191   O  OH  . TYR A 1 19  ? 20.330  15.560  13.052  1.00 17.76 ? 19  TYR A OH  1 
ATOM   192   N  N   . PRO A 1 20  ? 16.695  15.839  4.962   1.00 9.65  ? 20  PRO A N   1 
ATOM   193   C  CA  . PRO A 1 20  ? 15.786  15.624  3.883   1.00 9.47  ? 20  PRO A CA  1 
ATOM   194   C  C   . PRO A 1 20  ? 15.990  14.271  3.247   1.00 11.38 ? 20  PRO A C   1 
ATOM   195   O  O   . PRO A 1 20  ? 15.080  13.718  2.553   1.00 10.16 ? 20  PRO A O   1 
ATOM   196   C  CB  . PRO A 1 20  ? 16.082  16.740  2.857   1.00 12.14 ? 20  PRO A CB  1 
ATOM   197   C  CG  . PRO A 1 20  ? 16.754  17.763  3.771   1.00 12.71 ? 20  PRO A CG  1 
ATOM   198   C  CD  . PRO A 1 20  ? 17.469  17.098  4.796   1.00 10.12 ? 20  PRO A CD  1 
ATOM   199   N  N   . SER A 1 21  ? 17.209  13.688  3.302   1.00 9.77  ? 21  SER A N   1 
ATOM   200   C  CA  . SER A 1 21  ? 17.390  12.430  2.629   1.00 9.97  ? 21  SER A CA  1 
ATOM   201   C  C   . SER A 1 21  ? 16.579  11.316  3.287   1.00 9.10  ? 21  SER A C   1 
ATOM   202   O  O   . SER A 1 21  ? 16.382  10.310  2.590   1.00 8.10  ? 21  SER A O   1 
ATOM   203   C  CB  . SER A 1 21  ? 18.937  12.104  2.694   1.00 9.76  ? 21  SER A CB  1 
ATOM   204   O  OG  . SER A 1 21  ? 19.694  12.807  1.660   1.00 11.04 ? 21  SER A OG  1 
ATOM   205   N  N   . CYS A 1 22  ? 16.124  11.526  4.526   1.00 8.55  ? 22  CYS A N   1 
ATOM   206   C  CA  . CYS A 1 22  ? 15.234  10.523  5.174   1.00 7.99  ? 22  CYS A CA  1 
ATOM   207   C  C   . CYS A 1 22  ? 13.930  10.331  4.438   1.00 9.81  ? 22  CYS A C   1 
ATOM   208   O  O   . CYS A 1 22  ? 13.275  9.336   4.739   1.00 9.71  ? 22  CYS A O   1 
ATOM   209   C  CB  . CYS A 1 22  ? 15.093  10.795  6.610   1.00 8.51  ? 22  CYS A CB  1 
ATOM   210   S  SG  . CYS A 1 22  ? 16.688  10.844  7.515   1.00 9.97  ? 22  CYS A SG  1 
ATOM   211   N  N   . GLY A 1 23  ? 13.552  11.274  3.600   1.00 10.40 ? 23  GLY A N   1 
ATOM   212   C  CA  . GLY A 1 23  ? 12.423  11.116  2.734   1.00 8.32  ? 23  GLY A CA  1 
ATOM   213   C  C   . GLY A 1 23  ? 12.690  10.971  1.328   1.00 8.50  ? 23  GLY A C   1 
ATOM   214   O  O   . GLY A 1 23  ? 11.745  11.094  0.484   1.00 10.09 ? 23  GLY A O   1 
ATOM   215   N  N   . GLY A 1 24  ? 13.921  10.710  0.936   1.00 8.23  ? 24  GLY A N   1 
ATOM   216   C  CA  . GLY A 1 24  ? 14.368  10.478  -0.416  1.00 9.40  ? 24  GLY A CA  1 
ATOM   217   C  C   . GLY A 1 24  ? 14.456  9.047   -0.872  1.00 10.22 ? 24  GLY A C   1 
ATOM   218   O  O   . GLY A 1 24  ? 13.730  8.211   -0.263  1.00 12.63 ? 24  GLY A O   1 
ATOM   219   N  N   . LEU A 1 25  ? 15.223  8.839   -1.907  1.00 11.89 ? 25  LEU A N   1 
ATOM   220   C  CA  . LEU A 1 25  ? 15.358  7.530   -2.514  1.00 12.82 ? 25  LEU A CA  1 
ATOM   221   C  C   . LEU A 1 25  ? 16.308  6.599   -1.751  1.00 13.05 ? 25  LEU A C   1 
ATOM   222   O  O   . LEU A 1 25  ? 17.116  7.030   -0.904  1.00 11.67 ? 25  LEU A O   1 
ATOM   223   C  CB  . LEU A 1 25  ? 15.964  7.649   -3.904  1.00 15.01 ? 25  LEU A CB  1 
ATOM   224   C  CG  . LEU A 1 25  ? 15.147  8.648   -4.794  1.00 19.69 ? 25  LEU A CG  1 
ATOM   225   C  CD1 . LEU A 1 25  ? 15.904  8.786   -6.084  1.00 22.39 ? 25  LEU A CD1 1 
ATOM   226   C  CD2 . LEU A 1 25  ? 13.618  8.211   -4.951  1.00 24.41 ? 25  LEU A CD2 1 
ATOM   227   N  N   . LEU A 1 26  ? 16.166  5.304   -2.072  1.00 12.23 ? 26  LEU A N   1 
ATOM   228   C  CA  . LEU A 1 26  ? 17.119  4.190   -1.747  1.00 14.14 ? 26  LEU A CA  1 
ATOM   229   C  C   . LEU A 1 26  ? 17.122  4.038   -0.204  1.00 10.25 ? 26  LEU A C   1 
ATOM   230   O  O   . LEU A 1 26  ? 18.159  3.666   0.395   1.00 11.79 ? 26  LEU A O   1 
ATOM   231   C  CB  . LEU A 1 26  ? 18.551  4.430   -2.252  1.00 14.36 ? 26  LEU A CB  1 
ATOM   232   C  CG  . LEU A 1 26  ? 18.789  4.327   -3.780  1.00 19.36 ? 26  LEU A CG  1 
ATOM   233   C  CD1 . LEU A 1 26  ? 20.304  4.163   -4.021  1.00 23.28 ? 26  LEU A CD1 1 
ATOM   234   C  CD2 . LEU A 1 26  ? 18.120  3.189   -4.522  1.00 18.64 ? 26  LEU A CD2 1 
ATOM   235   N  N   . GLN A 1 27  ? 16.037  4.276   0.494   1.00 9.23  ? 27  GLN A N   1 
ATOM   236   C  CA  . GLN A 1 27  ? 16.047  4.162   2.023   1.00 7.37  ? 27  GLN A CA  1 
ATOM   237   C  C   . GLN A 1 27  ? 16.071  2.728   2.533   1.00 8.13  ? 27  GLN A C   1 
ATOM   238   O  O   . GLN A 1 27  ? 15.461  1.776   1.968   1.00 9.99  ? 27  GLN A O   1 
ATOM   239   C  CB  . GLN A 1 27  ? 14.888  4.864   2.649   1.00 9.18  ? 27  GLN A CB  1 
ATOM   240   C  CG  . GLN A 1 27  ? 14.946  6.409   2.328   1.00 7.34  ? 27  GLN A CG  1 
ATOM   241   C  CD  . GLN A 1 27  ? 16.078  7.045   3.056   1.00 7.61  ? 27  GLN A CD  1 
ATOM   242   O  OE1 . GLN A 1 27  ? 16.040  7.237   4.246   1.00 7.15  ? 27  GLN A OE1 1 
ATOM   243   N  NE2 . GLN A 1 27  ? 17.167  7.315   2.253   1.00 7.46  ? 27  GLN A NE2 1 
ATOM   244   N  N   . SER A 1 28  ? 16.830  2.594   3.632   1.00 6.11  ? 28  SER A N   1 
ATOM   245   C  CA  . SER A 1 28  ? 16.913  1.296   4.344   1.00 5.85  ? 28  SER A CA  1 
ATOM   246   C  C   . SER A 1 28  ? 16.384  1.531   5.754   1.00 6.94  ? 28  SER A C   1 
ATOM   247   O  O   . SER A 1 28  ? 16.292  2.650   6.233   1.00 6.84  ? 28  SER A O   1 
ATOM   248   C  CB  . SER A 1 28  ? 18.455  1.001   4.465   1.00 6.22  ? 28  SER A CB  1 
ATOM   249   O  OG  . SER A 1 28  ? 19.014  0.724   3.220   1.00 6.58  ? 28  SER A OG  1 
ATOM   250   N  N   . PRO A 1 29  ? 16.018  0.478   6.515   1.00 6.97  ? 29  PRO A N   1 
ATOM   251   C  CA  . PRO A 1 29  ? 16.121  -0.922  6.105   1.00 7.11  ? 29  PRO A CA  1 
ATOM   252   C  C   . PRO A 1 29  ? 14.917  -1.350  5.306   1.00 5.09  ? 29  PRO A C   1 
ATOM   253   O  O   . PRO A 1 29  ? 13.955  -0.591  5.096   1.00 7.82  ? 29  PRO A O   1 
ATOM   254   C  CB  . PRO A 1 29  ? 16.125  -1.660  7.493   1.00 6.77  ? 29  PRO A CB  1 
ATOM   255   C  CG  . PRO A 1 29  ? 15.147  -0.852  8.344   1.00 6.21  ? 29  PRO A CG  1 
ATOM   256   C  CD  . PRO A 1 29  ? 15.435  0.632   7.854   1.00 5.30  ? 29  PRO A CD  1 
ATOM   257   N  N   . ILE A 1 30  ? 14.902  -2.641  4.912   1.00 7.14  ? 30  ILE A N   1 
ATOM   258   C  CA  . ILE A 1 30  ? 13.889  -3.213  3.997   1.00 7.62  ? 30  ILE A CA  1 
ATOM   259   C  C   . ILE A 1 30  ? 13.614  -4.653  4.493   1.00 8.58  ? 30  ILE A C   1 
ATOM   260   O  O   . ILE A 1 30  ? 14.368  -5.285  5.252   1.00 8.65  ? 30  ILE A O   1 
ATOM   261   C  CB  . ILE A 1 30  ? 14.308  -3.285  2.567   1.00 8.78  ? 30  ILE A CB  1 
ATOM   262   C  CG1 . ILE A 1 30  ? 15.609  -4.103  2.373   1.00 8.00  ? 30  ILE A CG1 1 
ATOM   263   C  CG2 . ILE A 1 30  ? 14.480  -1.829  2.053   1.00 9.36  ? 30  ILE A CG2 1 
ATOM   264   C  CD1 . ILE A 1 30  ? 15.889  -4.304  0.825   1.00 10.37 ? 30  ILE A CD1 1 
ATOM   265   N  N   . ASP A 1 31  ? 12.453  -5.133  4.006   1.00 8.29  ? 31  ASP A N   1 
ATOM   266   C  CA  . ASP A 1 31  ? 12.090  -6.522  4.249   1.00 7.80  ? 31  ASP A CA  1 
ATOM   267   C  C   . ASP A 1 31  ? 12.711  -7.323  3.119   1.00 9.21  ? 31  ASP A C   1 
ATOM   268   O  O   . ASP A 1 31  ? 12.531  -7.063  1.919   1.00 10.99 ? 31  ASP A O   1 
ATOM   269   C  CB  . ASP A 1 31  ? 10.568  -6.718  4.223   1.00 9.22  ? 31  ASP A CB  1 
ATOM   270   C  CG  . ASP A 1 31  ? 10.120  -8.140  4.443   1.00 11.21 ? 31  ASP A CG  1 
ATOM   271   O  OD1 . ASP A 1 31  ? 10.737  -8.861  5.255   1.00 9.87  ? 31  ASP A OD1 1 
ATOM   272   O  OD2 . ASP A 1 31  ? 9.120   -8.522  3.806   1.00 13.71 ? 31  ASP A OD2 1 
ATOM   273   N  N   . LEU A 1 32  ? 13.421  -8.363  3.500   1.00 8.80  ? 32  LEU A N   1 
ATOM   274   C  CA  . LEU A 1 32  ? 14.043  -9.284  2.589   1.00 11.55 ? 32  LEU A CA  1 
ATOM   275   C  C   . LEU A 1 32  ? 13.129  -10.488 2.339   1.00 11.41 ? 32  LEU A C   1 
ATOM   276   O  O   . LEU A 1 32  ? 13.014  -11.370 3.173   1.00 12.42 ? 32  LEU A O   1 
ATOM   277   C  CB  . LEU A 1 32  ? 15.449  -9.788  3.173   1.00 9.67  ? 32  LEU A CB  1 
ATOM   278   C  CG  . LEU A 1 32  ? 16.327  -8.568  3.599   1.00 9.83  ? 32  LEU A CG  1 
ATOM   279   C  CD1 . LEU A 1 32  ? 17.591  -9.006  4.420   1.00 11.13 ? 32  LEU A CD1 1 
ATOM   280   C  CD2 . LEU A 1 32  ? 16.875  -7.841  2.371   1.00 15.07 ? 32  LEU A CD2 1 
ATOM   281   N  N   . HIS A 1 33  ? 12.351  -10.378 1.275   1.00 17.49 ? 33  HIS A N   1 
ATOM   282   C  CA  . HIS A 1 33  ? 11.438  -11.531 1.067   1.00 19.74 ? 33  HIS A CA  1 
ATOM   283   C  C   . HIS A 1 33  ? 11.600  -12.136 -0.259  1.00 19.66 ? 33  HIS A C   1 
ATOM   284   O  O   . HIS A 1 33  ? 12.153  -11.521 -1.140  1.00 16.97 ? 33  HIS A O   1 
ATOM   285   C  CB  . HIS A 1 33  ? 10.080  -11.044 1.380   1.00 21.77 ? 33  HIS A CB  1 
ATOM   286   C  CG  . HIS A 1 33  ? 9.621   -9.989  0.458   1.00 22.07 ? 33  HIS A CG  1 
ATOM   287   N  ND1 . HIS A 1 33  ? 9.863   -8.657  0.657   1.00 27.09 ? 33  HIS A ND1 1 
ATOM   288   C  CD2 . HIS A 1 33  ? 8.943   -10.092 -0.715  1.00 29.01 ? 33  HIS A CD2 1 
ATOM   289   C  CE1 . HIS A 1 33  ? 9.334   -7.970  -0.353  1.00 30.87 ? 33  HIS A CE1 1 
ATOM   290   N  NE2 . HIS A 1 33  ? 8.800   -8.821  -1.205  1.00 28.62 ? 33  HIS A NE2 1 
ATOM   291   N  N   . SER A 1 34  ? 11.087  -13.379 -0.385  1.00 19.55 ? 34  SER A N   1 
ATOM   292   C  CA  . SER A 1 34  ? 11.454  -14.204 -1.478  1.00 22.66 ? 34  SER A CA  1 
ATOM   293   C  C   . SER A 1 34  ? 11.158  -13.613 -2.863  1.00 22.84 ? 34  SER A C   1 
ATOM   294   O  O   . SER A 1 34  ? 11.938  -13.840 -3.784  1.00 25.39 ? 34  SER A O   1 
ATOM   295   C  CB  . SER A 1 34  ? 10.823  -15.592 -1.303  1.00 23.87 ? 34  SER A CB  1 
ATOM   296   O  OG  . SER A 1 34  ? 9.468   -15.421 -1.567  1.00 30.30 ? 34  SER A OG  1 
ATOM   297   N  N   . ASP A 1 35  ? 10.063  -12.856 -2.981  1.00 23.36 ? 35  ASP A N   1 
ATOM   298   C  CA  . ASP A 1 35  ? 9.646   -12.360 -4.282  1.00 25.91 ? 35  ASP A CA  1 
ATOM   299   C  C   . ASP A 1 35  ? 10.699  -11.424 -4.887  1.00 24.86 ? 35  ASP A C   1 
ATOM   300   O  O   . ASP A 1 35  ? 10.731  -11.300 -6.124  1.00 26.02 ? 35  ASP A O   1 
ATOM   301   C  CB  . ASP A 1 35  ? 8.263   -11.641 -4.221  1.00 26.20 ? 35  ASP A CB  1 
ATOM   302   C  CG  . ASP A 1 35  ? 7.103   -12.583 -3.842  1.00 35.58 ? 35  ASP A CG  1 
ATOM   303   O  OD1 . ASP A 1 35  ? 7.234   -13.845 -4.028  1.00 39.75 ? 35  ASP A OD1 1 
ATOM   304   O  OD2 . ASP A 1 35  ? 6.049   -12.039 -3.349  1.00 40.54 ? 35  ASP A OD2 1 
ATOM   305   N  N   . ILE A 1 36  ? 11.563  -10.777 -4.053  1.00 20.06 ? 36  ILE A N   1 
ATOM   306   C  CA  . ILE A 1 36  ? 12.449  -9.739  -4.593  1.00 19.18 ? 36  ILE A CA  1 
ATOM   307   C  C   . ILE A 1 36  ? 13.885  -10.234 -4.560  1.00 16.38 ? 36  ILE A C   1 
ATOM   308   O  O   . ILE A 1 36  ? 14.799  -9.471  -4.816  1.00 19.28 ? 36  ILE A O   1 
ATOM   309   C  CB  . ILE A 1 36  ? 12.353  -8.403  -3.817  1.00 16.89 ? 36  ILE A CB  1 
ATOM   310   C  CG1 . ILE A 1 36  ? 12.662  -8.700  -2.332  1.00 20.99 ? 36  ILE A CG1 1 
ATOM   311   C  CG2 . ILE A 1 36  ? 11.050  -7.618  -4.056  1.00 22.54 ? 36  ILE A CG2 1 
ATOM   312   C  CD1 . ILE A 1 36  ? 12.833  -7.485  -1.579  1.00 21.26 ? 36  ILE A CD1 1 
ATOM   313   N  N   . LEU A 1 37  ? 14.084  -11.514 -4.221  1.00 17.11 ? 37  LEU A N   1 
ATOM   314   C  CA  . LEU A 1 37  ? 15.517  -12.045 -4.125  1.00 16.83 ? 37  LEU A CA  1 
ATOM   315   C  C   . LEU A 1 37  ? 15.960  -12.576 -5.493  1.00 18.65 ? 37  LEU A C   1 
ATOM   316   O  O   . LEU A 1 37  ? 15.145  -13.296 -6.201  1.00 20.80 ? 37  LEU A O   1 
ATOM   317   C  CB  . LEU A 1 37  ? 15.530  -13.167 -3.054  1.00 16.72 ? 37  LEU A CB  1 
ATOM   318   C  CG  . LEU A 1 37  ? 15.105  -12.694 -1.664  1.00 16.06 ? 37  LEU A CG  1 
ATOM   319   C  CD1 . LEU A 1 37  ? 15.186  -13.846 -0.631  1.00 21.31 ? 37  LEU A CD1 1 
ATOM   320   C  CD2 . LEU A 1 37  ? 15.930  -11.596 -1.141  1.00 16.97 ? 37  LEU A CD2 1 
ATOM   321   N  N   . GLN A 1 38  ? 17.202  -12.299 -5.901  1.00 16.99 ? 38  GLN A N   1 
ATOM   322   C  CA  . GLN A 1 38  ? 17.692  -12.947 -7.140  1.00 19.54 ? 38  GLN A CA  1 
ATOM   323   C  C   . GLN A 1 38  ? 19.139  -13.331 -6.936  1.00 18.34 ? 38  GLN A C   1 
ATOM   324   O  O   . GLN A 1 38  ? 19.966  -12.497 -6.559  1.00 15.78 ? 38  GLN A O   1 
ATOM   325   C  CB  . GLN A 1 38  ? 17.531  -11.981 -8.272  1.00 21.18 ? 38  GLN A CB  1 
ATOM   326   C  CG  . GLN A 1 38  ? 17.896  -12.553 -9.649  1.00 26.13 ? 38  GLN A CG  1 
ATOM   327   C  CD  . GLN A 1 38  ? 17.694  -11.528 -10.726 1.00 31.18 ? 38  GLN A CD  1 
ATOM   328   O  OE1 . GLN A 1 38  ? 16.538  -11.311 -11.182 1.00 37.80 ? 38  GLN A OE1 1 
ATOM   329   N  NE2 . GLN A 1 38  ? 18.775  -10.867 -11.122 1.00 32.05 ? 38  GLN A NE2 1 
ATOM   330   N  N   . TYR A 1 39  ? 19.451  -14.612 -7.177  1.00 17.95 ? 39  TYR A N   1 
ATOM   331   C  CA  . TYR A 1 39  ? 20.765  -15.128 -7.067  1.00 17.11 ? 39  TYR A CA  1 
ATOM   332   C  C   . TYR A 1 39  ? 21.604  -14.395 -8.109  1.00 16.79 ? 39  TYR A C   1 
ATOM   333   O  O   . TYR A 1 39  ? 21.180  -14.164 -9.290  1.00 18.40 ? 39  TYR A O   1 
ATOM   334   C  CB  . TYR A 1 39  ? 20.696  -16.609 -7.437  1.00 17.59 ? 39  TYR A CB  1 
ATOM   335   C  CG  . TYR A 1 39  ? 22.056  -17.269 -7.518  1.00 20.82 ? 39  TYR A CG  1 
ATOM   336   C  CD1 . TYR A 1 39  ? 22.906  -17.210 -6.431  1.00 16.47 ? 39  TYR A CD1 1 
ATOM   337   C  CD2 . TYR A 1 39  ? 22.528  -17.939 -8.698  1.00 17.14 ? 39  TYR A CD2 1 
ATOM   338   C  CE1 . TYR A 1 39  ? 24.180  -17.761 -6.408  1.00 18.65 ? 39  TYR A CE1 1 
ATOM   339   C  CE2 . TYR A 1 39  ? 23.877  -18.473 -8.706  1.00 20.26 ? 39  TYR A CE2 1 
ATOM   340   C  CZ  . TYR A 1 39  ? 24.671  -18.408 -7.578  1.00 22.18 ? 39  TYR A CZ  1 
ATOM   341   O  OH  . TYR A 1 39  ? 25.967  -18.967 -7.532  1.00 26.57 ? 39  TYR A OH  1 
ATOM   342   N  N   . ASP A 1 40  ? 22.770  -14.007 -7.695  1.00 15.76 ? 40  ASP A N   1 
ATOM   343   C  CA  . ASP A 1 40  ? 23.759  -13.415 -8.534  1.00 16.02 ? 40  ASP A CA  1 
ATOM   344   C  C   . ASP A 1 40  ? 25.078  -14.172 -8.216  1.00 18.90 ? 40  ASP A C   1 
ATOM   345   O  O   . ASP A 1 40  ? 25.687  -13.963 -7.199  1.00 15.95 ? 40  ASP A O   1 
ATOM   346   C  CB  . ASP A 1 40  ? 23.807  -11.890 -8.257  1.00 18.17 ? 40  ASP A CB  1 
ATOM   347   C  CG  . ASP A 1 40  ? 24.800  -11.133 -9.178  1.00 24.34 ? 40  ASP A CG  1 
ATOM   348   O  OD1 . ASP A 1 40  ? 25.729  -11.770 -9.754  1.00 26.26 ? 40  ASP A OD1 1 
ATOM   349   O  OD2 . ASP A 1 40  ? 24.585  -9.904  -9.332  1.00 30.28 ? 40  ASP A OD2 1 
ATOM   350   N  N   . ALA A 1 41  ? 25.491  -15.103 -9.132  1.00 20.93 ? 41  ALA A N   1 
ATOM   351   C  CA  . ALA A 1 41  ? 26.813  -15.753 -9.058  1.00 24.54 ? 41  ALA A CA  1 
ATOM   352   C  C   . ALA A 1 41  ? 27.998  -14.788 -8.994  1.00 23.89 ? 41  ALA A C   1 
ATOM   353   O  O   . ALA A 1 41  ? 29.110  -15.179 -8.589  1.00 27.19 ? 41  ALA A O   1 
ATOM   354   C  CB  . ALA A 1 41  ? 27.025  -16.735 -10.254 1.00 24.93 ? 41  ALA A CB  1 
ATOM   355   N  N   . SER A 1 42  ? 27.839  -13.522 -9.388  1.00 23.92 ? 42  SER A N   1 
ATOM   356   C  CA  . SER A 1 42  ? 28.895  -12.507 -9.199  1.00 24.38 ? 42  SER A CA  1 
ATOM   357   C  C   . SER A 1 42  ? 29.288  -12.258 -7.739  1.00 24.66 ? 42  SER A C   1 
ATOM   358   O  O   . SER A 1 42  ? 30.315  -11.634 -7.413  1.00 27.19 ? 42  SER A O   1 
ATOM   359   C  CB  . SER A 1 42  ? 28.398  -11.153 -9.793  1.00 24.11 ? 42  SER A CB  1 
ATOM   360   O  OG  . SER A 1 42  ? 28.604  -10.051 -8.896  1.00 33.15 ? 42  SER A OG  1 
ATOM   361   N  N   . LEU A 1 43  ? 28.402  -12.643 -6.829  1.00 18.08 ? 43  LEU A N   1 
ATOM   362   C  CA  . LEU A 1 43  ? 28.620  -12.346 -5.412  1.00 18.86 ? 43  LEU A CA  1 
ATOM   363   C  C   . LEU A 1 43  ? 29.523  -13.263 -4.654  1.00 18.13 ? 43  LEU A C   1 
ATOM   364   O  O   . LEU A 1 43  ? 29.079  -14.233 -3.983  1.00 20.39 ? 43  LEU A O   1 
ATOM   365   C  CB  . LEU A 1 43  ? 27.285  -12.165 -4.710  1.00 15.95 ? 43  LEU A CB  1 
ATOM   366   C  CG  . LEU A 1 43  ? 26.439  -10.994 -5.247  1.00 16.54 ? 43  LEU A CG  1 
ATOM   367   C  CD1 . LEU A 1 43  ? 25.054  -10.888 -4.562  1.00 12.37 ? 43  LEU A CD1 1 
ATOM   368   C  CD2 . LEU A 1 43  ? 27.062  -9.606  -5.162  1.00 13.91 ? 43  LEU A CD2 1 
ATOM   369   N  N   . THR A 1 44  ? 30.809  -12.989 -4.760  1.00 17.67 ? 44  THR A N   1 
ATOM   370   C  CA  . THR A 1 44  ? 31.813  -13.798 -4.193  1.00 18.97 ? 44  THR A CA  1 
ATOM   371   C  C   . THR A 1 44  ? 32.080  -13.482 -2.701  1.00 18.18 ? 44  THR A C   1 
ATOM   372   O  O   . THR A 1 44  ? 31.599  -12.463 -2.178  1.00 16.66 ? 44  THR A O   1 
ATOM   373   C  CB  . THR A 1 44  ? 33.129  -13.554 -5.018  1.00 18.89 ? 44  THR A CB  1 
ATOM   374   O  OG1 . THR A 1 44  ? 33.504  -12.201 -4.852  1.00 21.91 ? 44  THR A OG1 1 
ATOM   375   C  CG2 . THR A 1 44  ? 32.839  -13.813 -6.462  1.00 25.14 ? 44  THR A CG2 1 
ATOM   376   N  N   . PRO A 1 45  ? 32.774  -14.366 -1.967  1.00 17.15 ? 45  PRO A N   1 
ATOM   377   C  CA  . PRO A 1 45  ? 33.047  -14.108 -0.542  1.00 16.90 ? 45  PRO A CA  1 
ATOM   378   C  C   . PRO A 1 45  ? 33.873  -12.864 -0.254  1.00 17.20 ? 45  PRO A C   1 
ATOM   379   O  O   . PRO A 1 45  ? 34.905  -12.644 -0.888  1.00 19.14 ? 45  PRO A O   1 
ATOM   380   C  CB  . PRO A 1 45  ? 33.808  -15.363 -0.069  1.00 18.68 ? 45  PRO A CB  1 
ATOM   381   C  CG  . PRO A 1 45  ? 33.344  -16.442 -1.116  1.00 19.11 ? 45  PRO A CG  1 
ATOM   382   C  CD  . PRO A 1 45  ? 33.272  -15.723 -2.389  1.00 19.84 ? 45  PRO A CD  1 
ATOM   383   N  N   . LEU A 1 46  ? 33.500  -12.086 0.740   1.00 14.69 ? 46  LEU A N   1 
ATOM   384   C  CA  . LEU A 1 46  ? 34.339  -10.937 1.150   1.00 13.43 ? 46  LEU A CA  1 
ATOM   385   C  C   . LEU A 1 46  ? 35.468  -11.520 1.991   1.00 14.31 ? 46  LEU A C   1 
ATOM   386   O  O   . LEU A 1 46  ? 35.315  -12.600 2.587   1.00 16.90 ? 46  LEU A O   1 
ATOM   387   C  CB  . LEU A 1 46  ? 33.524  -10.019 2.037   1.00 13.13 ? 46  LEU A CB  1 
ATOM   388   C  CG  . LEU A 1 46  ? 32.352  -9.407  1.249   1.00 15.42 ? 46  LEU A CG  1 
ATOM   389   C  CD1 . LEU A 1 46  ? 31.576  -8.513  2.154   1.00 14.96 ? 46  LEU A CD1 1 
ATOM   390   C  CD2 . LEU A 1 46  ? 32.899  -8.534  0.043   1.00 17.43 ? 46  LEU A CD2 1 
ATOM   391   N  N   . GLU A 1 47  ? 36.541  -10.772 2.061   1.00 13.66 ? 47  GLU A N   1 
ATOM   392   C  CA  . GLU A 1 47  ? 37.629  -11.068 2.913   1.00 14.50 ? 47  GLU A CA  1 
ATOM   393   C  C   . GLU A 1 47  ? 37.743  -10.011 3.948   1.00 14.13 ? 47  GLU A C   1 
ATOM   394   O  O   . GLU A 1 47  ? 37.674  -8.792  3.689   1.00 14.57 ? 47  GLU A O   1 
ATOM   395   C  CB  . GLU A 1 47  ? 38.967  -11.212 2.148   1.00 18.11 ? 47  GLU A CB  1 
ATOM   396   C  CG  . GLU A 1 47  ? 38.809  -12.111 0.924   1.00 23.64 ? 47  GLU A CG  1 
ATOM   397   C  CD  . GLU A 1 47  ? 39.916  -11.923 -0.092  1.00 38.06 ? 47  GLU A CD  1 
ATOM   398   O  OE1 . GLU A 1 47  ? 39.720  -11.126 -1.088  1.00 44.37 ? 47  GLU A OE1 1 
ATOM   399   O  OE2 . GLU A 1 47  ? 40.984  -12.557 0.147   1.00 44.56 ? 47  GLU A OE2 1 
ATOM   400   N  N   . PHE A 1 48  ? 37.868  -10.419 5.221   1.00 13.20 ? 48  PHE A N   1 
ATOM   401   C  CA  . PHE A 1 48  ? 37.914  -9.525  6.377   1.00 11.89 ? 48  PHE A CA  1 
ATOM   402   C  C   . PHE A 1 48  ? 39.350  -9.390  6.808   1.00 13.76 ? 48  PHE A C   1 
ATOM   403   O  O   . PHE A 1 48  ? 39.934  -10.324 7.356   1.00 17.39 ? 48  PHE A O   1 
ATOM   404   C  CB  . PHE A 1 48  ? 36.978  -10.047 7.469   1.00 14.43 ? 48  PHE A CB  1 
ATOM   405   C  CG  . PHE A 1 48  ? 35.617  -10.429 6.932   1.00 12.32 ? 48  PHE A CG  1 
ATOM   406   C  CD1 . PHE A 1 48  ? 34.776  -9.501  6.418   1.00 14.02 ? 48  PHE A CD1 1 
ATOM   407   C  CD2 . PHE A 1 48  ? 35.293  -11.835 6.756   1.00 14.52 ? 48  PHE A CD2 1 
ATOM   408   C  CE1 . PHE A 1 48  ? 33.486  -9.843  5.799   1.00 13.27 ? 48  PHE A CE1 1 
ATOM   409   C  CE2 . PHE A 1 48  ? 34.052  -12.186 6.207   1.00 14.51 ? 48  PHE A CE2 1 
ATOM   410   C  CZ  . PHE A 1 48  ? 33.156  -11.166 5.676   1.00 13.99 ? 48  PHE A CZ  1 
ATOM   411   N  N   . GLN A 1 49  ? 39.860  -8.204  6.598   1.00 12.35 ? 49  GLN A N   1 
ATOM   412   C  CA  . GLN A 1 49  ? 41.340  -8.012  6.685   1.00 12.67 ? 49  GLN A CA  1 
ATOM   413   C  C   . GLN A 1 49  ? 41.566  -7.077  7.870   1.00 10.24 ? 49  GLN A C   1 
ATOM   414   O  O   . GLN A 1 49  ? 40.863  -6.088  8.035   1.00 10.49 ? 49  GLN A O   1 
ATOM   415   C  CB  . GLN A 1 49  ? 41.912  -7.306  5.433   1.00 13.45 ? 49  GLN A CB  1 
ATOM   416   C  CG  . GLN A 1 49  ? 41.739  -8.215  4.236   1.00 19.81 ? 49  GLN A CG  1 
ATOM   417   C  CD  . GLN A 1 49  ? 42.872  -8.303  3.266   1.00 33.03 ? 49  GLN A CD  1 
ATOM   418   O  OE1 . GLN A 1 49  ? 43.421  -7.263  2.814   1.00 39.50 ? 49  GLN A OE1 1 
ATOM   419   N  NE2 . GLN A 1 49  ? 43.193  -9.536  2.859   1.00 29.81 ? 49  GLN A NE2 1 
ATOM   420   N  N   . GLY A 1 50  ? 42.539  -7.338  8.745   1.00 12.18 ? 50  GLY A N   1 
ATOM   421   C  CA  . GLY A 1 50  ? 42.742  -6.601  9.882   1.00 12.17 ? 50  GLY A CA  1 
ATOM   422   C  C   . GLY A 1 50  ? 41.613  -6.529  10.979  1.00 11.80 ? 50  GLY A C   1 
ATOM   423   O  O   . GLY A 1 50  ? 41.619  -5.692  11.811  1.00 13.78 ? 50  GLY A O   1 
ATOM   424   N  N   . TYR A 1 51  ? 40.818  -7.598  10.977  1.00 12.27 ? 51  TYR A N   1 
ATOM   425   C  CA  . TYR A 1 51  ? 39.742  -7.752  11.966  1.00 11.87 ? 51  TYR A CA  1 
ATOM   426   C  C   . TYR A 1 51  ? 40.286  -8.243  13.284  1.00 13.24 ? 51  TYR A C   1 
ATOM   427   O  O   . TYR A 1 51  ? 39.614  -8.089  14.308  1.00 12.61 ? 51  TYR A O   1 
ATOM   428   C  CB  . TYR A 1 51  ? 38.595  -8.697  11.439  1.00 11.45 ? 51  TYR A CB  1 
ATOM   429   C  CG  . TYR A 1 51  ? 37.530  -7.965  10.553  1.00 10.48 ? 51  TYR A CG  1 
ATOM   430   C  CD1 . TYR A 1 51  ? 36.161  -8.223  10.802  1.00 10.17 ? 51  TYR A CD1 1 
ATOM   431   C  CD2 . TYR A 1 51  ? 37.874  -7.076  9.539   1.00 9.84  ? 51  TYR A CD2 1 
ATOM   432   C  CE1 . TYR A 1 51  ? 35.180  -7.631  9.996   1.00 11.58 ? 51  TYR A CE1 1 
ATOM   433   C  CE2 . TYR A 1 51  ? 36.913  -6.500  8.735   1.00 11.01 ? 51  TYR A CE2 1 
ATOM   434   C  CZ  . TYR A 1 51  ? 35.585  -6.713  9.057   1.00 11.49 ? 51  TYR A CZ  1 
ATOM   435   O  OH  . TYR A 1 51  ? 34.600  -6.030  8.323   1.00 12.20 ? 51  TYR A OH  1 
ATOM   436   N  N   . ASN A 1 52  ? 41.479  -8.888  13.258  1.00 13.76 ? 52  ASN A N   1 
ATOM   437   C  CA  . ASN A 1 52  ? 42.012  -9.407  14.529  1.00 14.94 ? 52  ASN A CA  1 
ATOM   438   C  C   . ASN A 1 52  ? 42.760  -8.302  15.262  1.00 17.14 ? 52  ASN A C   1 
ATOM   439   O  O   . ASN A 1 52  ? 43.976  -8.033  14.981  1.00 18.30 ? 52  ASN A O   1 
ATOM   440   C  CB  . ASN A 1 52  ? 42.770  -10.713 14.223  1.00 15.47 ? 52  ASN A CB  1 
ATOM   441   C  CG  . ASN A 1 52  ? 43.245  -11.391 15.487  1.00 21.46 ? 52  ASN A CG  1 
ATOM   442   O  OD1 . ASN A 1 52  ? 42.556  -11.401 16.503  1.00 18.76 ? 52  ASN A OD1 1 
ATOM   443   N  ND2 . ASN A 1 52  ? 44.527  -11.900 15.433  1.00 26.95 ? 52  ASN A ND2 1 
ATOM   444   N  N   . LEU A 1 53  ? 42.026  -7.496  15.980  1.00 16.45 ? 53  LEU A N   1 
ATOM   445   C  CA  . LEU A 1 53  ? 42.514  -6.257  16.535  1.00 16.66 ? 53  LEU A CA  1 
ATOM   446   C  C   . LEU A 1 53  ? 43.577  -6.613  17.576  1.00 19.51 ? 53  LEU A C   1 
ATOM   447   O  O   . LEU A 1 53  ? 43.353  -7.500  18.375  1.00 21.11 ? 53  LEU A O   1 
ATOM   448   C  CB  . LEU A 1 53  ? 41.415  -5.373  17.176  1.00 14.91 ? 53  LEU A CB  1 
ATOM   449   C  CG  . LEU A 1 53  ? 40.263  -5.012  16.207  1.00 12.15 ? 53  LEU A CG  1 
ATOM   450   C  CD1 . LEU A 1 53  ? 39.312  -4.179  16.994  1.00 13.26 ? 53  LEU A CD1 1 
ATOM   451   C  CD2 . LEU A 1 53  ? 40.879  -4.323  14.922  1.00 15.04 ? 53  LEU A CD2 1 
ATOM   452   N  N   . SER A 1 54  ? 44.670  -5.880  17.496  1.00 20.55 ? 54  SER A N   1 
ATOM   453   C  CA  . SER A 1 54  ? 45.780  -6.066  18.466  1.00 22.43 ? 54  SER A CA  1 
ATOM   454   C  C   . SER A 1 54  ? 45.179  -6.145  19.876  1.00 22.71 ? 54  SER A C   1 
ATOM   455   O  O   . SER A 1 54  ? 44.493  -5.200  20.298  1.00 22.30 ? 54  SER A O   1 
ATOM   456   C  CB  . SER A 1 54  ? 46.657  -4.824  18.387  1.00 20.95 ? 54  SER A CB  1 
ATOM   457   O  OG  . SER A 1 54  ? 47.756  -4.929  19.337  1.00 22.16 ? 54  SER A OG  1 
ATOM   458   N  N   . ALA A 1 55  ? 45.451  -7.206  20.633  1.00 25.73 ? 55  ALA A N   1 
ATOM   459   C  CA  . ALA A 1 55  ? 44.983  -7.242  22.044  1.00 24.80 ? 55  ALA A CA  1 
ATOM   460   C  C   . ALA A 1 55  ? 45.778  -6.215  22.875  1.00 24.64 ? 55  ALA A C   1 
ATOM   461   O  O   . ALA A 1 55  ? 45.448  -5.956  24.001  1.00 23.39 ? 55  ALA A O   1 
ATOM   462   C  CB  . ALA A 1 55  ? 45.156  -8.700  22.667  1.00 27.96 ? 55  ALA A CB  1 
ATOM   463   N  N   . ASN A 1 56  ? 46.839  -5.638  22.287  1.00 24.65 ? 56  ASN A N   1 
ATOM   464   C  CA  . ASN A 1 56  ? 47.580  -4.561  22.984  1.00 24.05 ? 56  ASN A CA  1 
ATOM   465   C  C   . ASN A 1 56  ? 47.148  -3.133  22.658  1.00 23.30 ? 56  ASN A C   1 
ATOM   466   O  O   . ASN A 1 56  ? 47.755  -2.170  23.096  1.00 26.05 ? 56  ASN A O   1 
ATOM   467   C  CB  . ASN A 1 56  ? 49.064  -4.691  22.598  1.00 22.77 ? 56  ASN A CB  1 
ATOM   468   C  CG  . ASN A 1 56  ? 49.634  -5.958  23.086  1.00 26.19 ? 56  ASN A CG  1 
ATOM   469   O  OD1 . ASN A 1 56  ? 49.465  -6.279  24.259  1.00 30.42 ? 56  ASN A OD1 1 
ATOM   470   N  ND2 . ASN A 1 56  ? 50.239  -6.728  22.215  1.00 28.72 ? 56  ASN A ND2 1 
ATOM   471   N  N   . LYS A 1 57  ? 46.083  -2.972  21.832  1.00 20.36 ? 57  LYS A N   1 
ATOM   472   C  CA  . LYS A 1 57  ? 45.443  -1.684  21.601  1.00 17.48 ? 57  LYS A CA  1 
ATOM   473   C  C   . LYS A 1 57  ? 44.052  -1.608  22.336  1.00 15.00 ? 57  LYS A C   1 
ATOM   474   O  O   . LYS A 1 57  ? 43.529  -2.633  22.671  1.00 17.74 ? 57  LYS A O   1 
ATOM   475   C  CB  . LYS A 1 57  ? 45.231  -1.426  20.087  1.00 18.76 ? 57  LYS A CB  1 
ATOM   476   C  CG  . LYS A 1 57  ? 46.554  -1.238  19.302  1.00 21.27 ? 57  LYS A CG  1 
ATOM   477   C  CD  . LYS A 1 57  ? 46.228  -1.080  17.799  1.00 20.77 ? 57  LYS A CD  1 
ATOM   478   C  CE  . LYS A 1 57  ? 47.464  -0.538  16.913  1.00 18.27 ? 57  LYS A CE  1 
ATOM   479   N  NZ  . LYS A 1 57  ? 48.032  0.896   17.059  1.00 21.05 ? 57  LYS A NZ  1 
ATOM   480   N  N   . GLN A 1 58  ? 43.586  -0.422  22.618  1.00 16.73 ? 58  GLN A N   1 
ATOM   481   C  CA  . GLN A 1 58  ? 42.229  -0.210  23.243  1.00 17.99 ? 58  GLN A CA  1 
ATOM   482   C  C   . GLN A 1 58  ? 41.388  0.580   22.321  1.00 18.49 ? 58  GLN A C   1 
ATOM   483   O  O   . GLN A 1 58  ? 41.905  1.404   21.571  1.00 19.51 ? 58  GLN A O   1 
ATOM   484   C  CB  . GLN A 1 58  ? 42.336  0.496   24.561  1.00 19.87 ? 58  GLN A CB  1 
ATOM   485   C  CG  . GLN A 1 58  ? 42.785  -0.516  25.507  1.00 21.31 ? 58  GLN A CG  1 
ATOM   486   C  CD  . GLN A 1 58  ? 43.088  0.052   26.823  1.00 23.67 ? 58  GLN A CD  1 
ATOM   487   O  OE1 . GLN A 1 58  ? 43.605  -0.644  27.681  1.00 27.37 ? 58  GLN A OE1 1 
ATOM   488   N  NE2 . GLN A 1 58  ? 42.760  1.307   27.001  1.00 23.49 ? 58  GLN A NE2 1 
ATOM   489   N  N   . PHE A 1 59  ? 40.085  0.217   22.240  1.00 16.14 ? 59  PHE A N   1 
ATOM   490   C  CA  . PHE A 1 59  ? 39.163  0.881   21.324  1.00 15.53 ? 59  PHE A CA  1 
ATOM   491   C  C   . PHE A 1 59  ? 38.004  1.505   22.041  1.00 13.71 ? 59  PHE A C   1 
ATOM   492   O  O   . PHE A 1 59  ? 37.513  0.932   23.005  1.00 14.67 ? 59  PHE A O   1 
ATOM   493   C  CB  . PHE A 1 59  ? 38.725  -0.181  20.353  1.00 13.99 ? 59  PHE A CB  1 
ATOM   494   C  CG  . PHE A 1 59  ? 39.883  -0.699  19.542  1.00 15.46 ? 59  PHE A CG  1 
ATOM   495   C  CD1 . PHE A 1 59  ? 40.274  -0.119  18.369  1.00 18.90 ? 59  PHE A CD1 1 
ATOM   496   C  CD2 . PHE A 1 59  ? 40.604  -1.803  20.032  1.00 17.82 ? 59  PHE A CD2 1 
ATOM   497   C  CE1 . PHE A 1 59  ? 41.416  -0.597  17.665  1.00 13.93 ? 59  PHE A CE1 1 
ATOM   498   C  CE2 . PHE A 1 59  ? 41.745  -2.330  19.336  1.00 15.70 ? 59  PHE A CE2 1 
ATOM   499   C  CZ  . PHE A 1 59  ? 42.123  -1.723  18.117  1.00 15.91 ? 59  PHE A CZ  1 
ATOM   500   N  N   . LEU A 1 60  ? 37.692  2.735   21.668  1.00 14.00 ? 60  LEU A N   1 
ATOM   501   C  CA  . LEU A 1 60  ? 36.775  3.569   22.395  1.00 13.85 ? 60  LEU A CA  1 
ATOM   502   C  C   . LEU A 1 60  ? 35.273  3.123   22.188  1.00 14.16 ? 60  LEU A C   1 
ATOM   503   O  O   . LEU A 1 60  ? 34.773  3.042   21.072  1.00 14.98 ? 60  LEU A O   1 
ATOM   504   C  CB  . LEU A 1 60  ? 36.936  4.996   21.992  1.00 14.94 ? 60  LEU A CB  1 
ATOM   505   C  CG  . LEU A 1 60  ? 36.168  5.948   22.812  1.00 19.90 ? 60  LEU A CG  1 
ATOM   506   C  CD1 . LEU A 1 60  ? 36.716  6.002   24.293  1.00 21.94 ? 60  LEU A CD1 1 
ATOM   507   C  CD2 . LEU A 1 60  ? 36.130  7.318   22.217  1.00 20.75 ? 60  LEU A CD2 1 
ATOM   508   N  N   . LEU A 1 61  ? 34.615  2.766   23.248  1.00 14.93 ? 61  LEU A N   1 
ATOM   509   C  CA  . LEU A 1 61  ? 33.194  2.446   23.297  1.00 14.53 ? 61  LEU A CA  1 
ATOM   510   C  C   . LEU A 1 61  ? 32.468  3.624   23.850  1.00 15.46 ? 61  LEU A C   1 
ATOM   511   O  O   . LEU A 1 61  ? 32.842  4.158   24.895  1.00 15.37 ? 61  LEU A O   1 
ATOM   512   C  CB  . LEU A 1 61  ? 33.008  1.244   24.189  1.00 14.61 ? 61  LEU A CB  1 
ATOM   513   C  CG  . LEU A 1 61  ? 31.593  0.662   24.253  1.00 15.60 ? 61  LEU A CG  1 
ATOM   514   C  CD1 . LEU A 1 61  ? 31.360  -0.291  22.977  1.00 16.30 ? 61  LEU A CD1 1 
ATOM   515   C  CD2 . LEU A 1 61  ? 31.371  -0.209  25.509  1.00 19.71 ? 61  LEU A CD2 1 
ATOM   516   N  N   A THR A 1 62  ? 31.400  4.036   23.178  0.50 14.90 ? 62  THR A N   1 
ATOM   517   N  N   B THR A 1 62  ? 31.432  4.108   23.149  0.50 14.37 ? 62  THR A N   1 
ATOM   518   C  CA  A THR A 1 62  ? 30.677  5.204   23.565  0.50 15.50 ? 62  THR A CA  1 
ATOM   519   C  CA  B THR A 1 62  ? 30.702  5.305   23.538  0.50 14.48 ? 62  THR A CA  1 
ATOM   520   C  C   A THR A 1 62  ? 29.202  4.848   23.649  0.50 15.72 ? 62  THR A C   1 
ATOM   521   C  C   B THR A 1 62  ? 29.189  5.110   23.450  0.50 15.00 ? 62  THR A C   1 
ATOM   522   O  O   A THR A 1 62  ? 28.760  3.902   22.963  0.50 14.95 ? 62  THR A O   1 
ATOM   523   O  O   B THR A 1 62  ? 28.687  4.538   22.459  0.50 10.86 ? 62  THR A O   1 
ATOM   524   C  CB  A THR A 1 62  ? 30.879  6.386   22.550  0.50 16.85 ? 62  THR A CB  1 
ATOM   525   C  CB  B THR A 1 62  ? 31.012  6.555   22.638  0.50 15.80 ? 62  THR A CB  1 
ATOM   526   O  OG1 A THR A 1 62  ? 32.284  6.637   22.319  0.50 17.22 ? 62  THR A OG1 1 
ATOM   527   O  OG1 B THR A 1 62  ? 30.659  6.258   21.272  0.50 11.17 ? 62  THR A OG1 1 
ATOM   528   C  CG2 A THR A 1 62  ? 30.109  7.667   23.002  0.50 15.55 ? 62  THR A CG2 1 
ATOM   529   C  CG2 B THR A 1 62  ? 32.466  7.058   22.741  0.50 18.22 ? 62  THR A CG2 1 
ATOM   530   N  N   . ASN A 1 63  ? 28.451  5.639   24.418  1.00 13.80 ? 63  ASN A N   1 
ATOM   531   C  CA  . ASN A 1 63  ? 26.987  5.714   24.259  1.00 14.80 ? 63  ASN A CA  1 
ATOM   532   C  C   . ASN A 1 63  ? 26.739  7.140   23.671  1.00 14.71 ? 63  ASN A C   1 
ATOM   533   O  O   . ASN A 1 63  ? 27.032  8.211   24.283  1.00 16.46 ? 63  ASN A O   1 
ATOM   534   C  CB  . ASN A 1 63  ? 26.342  5.586   25.635  1.00 15.61 ? 63  ASN A CB  1 
ATOM   535   C  CG  . ASN A 1 63  ? 24.854  5.880   25.657  1.00 13.51 ? 63  ASN A CG  1 
ATOM   536   O  OD1 . ASN A 1 63  ? 24.322  6.596   24.830  1.00 15.02 ? 63  ASN A OD1 1 
ATOM   537   N  ND2 . ASN A 1 63  ? 24.233  5.420   26.744  1.00 13.35 ? 63  ASN A ND2 1 
ATOM   538   N  N   . ASN A 1 64  ? 26.263  7.200   22.431  1.00 13.83 ? 64  ASN A N   1 
ATOM   539   C  CA  . ASN A 1 64  ? 26.027  8.495   21.801  1.00 15.30 ? 64  ASN A CA  1 
ATOM   540   C  C   . ASN A 1 64  ? 24.556  8.962   21.857  1.00 15.76 ? 64  ASN A C   1 
ATOM   541   O  O   . ASN A 1 64  ? 24.144  9.946   21.146  1.00 17.17 ? 64  ASN A O   1 
ATOM   542   C  CB  . ASN A 1 64  ? 26.521  8.446   20.336  1.00 15.05 ? 64  ASN A CB  1 
ATOM   543   C  CG  . ASN A 1 64  ? 25.601  7.538   19.447  1.00 18.71 ? 64  ASN A CG  1 
ATOM   544   O  OD1 . ASN A 1 64  ? 24.628  6.952   19.890  1.00 14.57 ? 64  ASN A OD1 1 
ATOM   545   N  ND2 . ASN A 1 64  ? 25.894  7.516   18.146  1.00 21.62 ? 64  ASN A ND2 1 
ATOM   546   N  N   . GLY A 1 65  ? 23.778  8.327   22.718  1.00 14.92 ? 65  GLY A N   1 
ATOM   547   C  CA  . GLY A 1 65  ? 22.393  8.696   22.914  1.00 17.03 ? 65  GLY A CA  1 
ATOM   548   C  C   . GLY A 1 65  ? 21.462  7.993   21.916  1.00 17.51 ? 65  GLY A C   1 
ATOM   549   O  O   . GLY A 1 65  ? 20.245  8.036   22.125  1.00 17.82 ? 65  GLY A O   1 
ATOM   550   N  N   . HIS A 1 66  ? 22.029  7.317   20.890  1.00 14.73 ? 66  HIS A N   1 
ATOM   551   C  CA  . HIS A 1 66  ? 21.218  6.532   19.892  1.00 14.40 ? 66  HIS A CA  1 
ATOM   552   C  C   . HIS A 1 66  ? 21.540  5.064   19.866  1.00 13.94 ? 66  HIS A C   1 
ATOM   553   O  O   . HIS A 1 66  ? 20.634  4.300   19.509  1.00 13.01 ? 66  HIS A O   1 
ATOM   554   C  CB  . HIS A 1 66  ? 21.338  7.095   18.472  1.00 14.22 ? 66  HIS A CB  1 
ATOM   555   C  CG  . HIS A 1 66  ? 21.193  8.587   18.385  1.00 14.10 ? 66  HIS A CG  1 
ATOM   556   N  ND1 . HIS A 1 66  ? 19.986  9.231   18.489  1.00 13.82 ? 66  HIS A ND1 1 
ATOM   557   C  CD2 . HIS A 1 66  ? 22.134  9.528   18.168  1.00 13.69 ? 66  HIS A CD2 1 
ATOM   558   C  CE1 . HIS A 1 66  ? 20.204  10.561  18.392  1.00 13.43 ? 66  HIS A CE1 1 
ATOM   559   N  NE2 . HIS A 1 66  ? 21.497  10.741  18.160  1.00 14.23 ? 66  HIS A NE2 1 
ATOM   560   N  N   . SER A 1 67  ? 22.784  4.688   20.158  1.00 10.66 ? 67  SER A N   1 
ATOM   561   C  CA  . SER A 1 67  ? 23.193  3.274   20.199  1.00 10.79 ? 67  SER A CA  1 
ATOM   562   C  C   . SER A 1 67  ? 24.445  3.225   21.100  1.00 11.10 ? 67  SER A C   1 
ATOM   563   O  O   . SER A 1 67  ? 24.874  4.215   21.602  1.00 12.55 ? 67  SER A O   1 
ATOM   564   C  CB  . SER A 1 67  ? 23.530  2.753   18.806  1.00 9.65  ? 67  SER A CB  1 
ATOM   565   O  OG  . SER A 1 67  ? 23.854  1.373   18.838  1.00 11.38 ? 67  SER A OG  1 
ATOM   566   N  N   . VAL A 1 68  ? 24.993  2.043   21.219  1.00 11.01 ? 68  VAL A N   1 
ATOM   567   C  CA  . VAL A 1 68  ? 26.343  1.891   21.786  1.00 12.13 ? 68  VAL A CA  1 
ATOM   568   C  C   . VAL A 1 68  ? 27.253  1.641   20.564  1.00 13.47 ? 68  VAL A C   1 
ATOM   569   O  O   . VAL A 1 68  ? 26.952  0.780   19.734  1.00 12.77 ? 68  VAL A O   1 
ATOM   570   C  CB  . VAL A 1 68  ? 26.337  0.769   22.828  1.00 13.24 ? 68  VAL A CB  1 
ATOM   571   C  CG1 . VAL A 1 68  ? 25.884  -0.623  22.286  1.00 14.14 ? 68  VAL A CG1 1 
ATOM   572   C  CG2 . VAL A 1 68  ? 27.789  0.642   23.286  1.00 16.93 ? 68  VAL A CG2 1 
ATOM   573   N  N   . LYS A 1 69  ? 28.365  2.401   20.456  1.00 13.50 ? 69  LYS A N   1 
ATOM   574   C  CA  . LYS A 1 69  ? 29.257  2.298   19.304  1.00 11.91 ? 69  LYS A CA  1 
ATOM   575   C  C   . LYS A 1 69  ? 30.681  2.001   19.758  1.00 12.60 ? 69  LYS A C   1 
ATOM   576   O  O   . LYS A 1 69  ? 31.150  2.599   20.752  1.00 15.48 ? 69  LYS A O   1 
ATOM   577   C  CB  . LYS A 1 69  ? 29.121  3.510   18.426  1.00 16.11 ? 69  LYS A CB  1 
ATOM   578   C  CG  . LYS A 1 69  ? 29.890  4.677   18.702  1.00 21.22 ? 69  LYS A CG  1 
ATOM   579   C  CD  . LYS A 1 69  ? 29.872  5.670   17.548  1.00 24.92 ? 69  LYS A CD  1 
ATOM   580   C  CE  . LYS A 1 69  ? 30.351  6.930   18.207  1.00 34.18 ? 69  LYS A CE  1 
ATOM   581   N  NZ  . LYS A 1 69  ? 30.565  8.078   17.263  1.00 35.03 ? 69  LYS A NZ  1 
ATOM   582   N  N   . LEU A 1 70  ? 31.360  1.155   19.000  1.00 10.84 ? 70  LEU A N   1 
ATOM   583   C  CA  . LEU A 1 70  ? 32.795  0.827   19.247  1.00 11.27 ? 70  LEU A CA  1 
ATOM   584   C  C   . LEU A 1 70  ? 33.556  1.411   18.075  1.00 11.86 ? 70  LEU A C   1 
ATOM   585   O  O   . LEU A 1 70  ? 33.300  1.046   16.931  1.00 11.44 ? 70  LEU A O   1 
ATOM   586   C  CB  . LEU A 1 70  ? 32.940  -0.668  19.318  1.00 10.89 ? 70  LEU A CB  1 
ATOM   587   C  CG  . LEU A 1 70  ? 34.450  -1.113  19.544  1.00 9.76  ? 70  LEU A CG  1 
ATOM   588   C  CD1 . LEU A 1 70  ? 35.069  -0.696  20.856  1.00 13.87 ? 70  LEU A CD1 1 
ATOM   589   C  CD2 . LEU A 1 70  ? 34.513  -2.619  19.399  1.00 11.25 ? 70  LEU A CD2 1 
ATOM   590   N  N   A ASN A 1 71  ? 34.550  2.261   18.361  0.50 10.84 ? 71  ASN A N   1 
ATOM   591   N  N   B ASN A 1 71  ? 34.504  2.324   18.351  0.50 11.42 ? 71  ASN A N   1 
ATOM   592   C  CA  A ASN A 1 71  ? 35.398  2.760   17.306  0.50 11.36 ? 71  ASN A CA  1 
ATOM   593   C  CA  B ASN A 1 71  ? 35.318  2.863   17.284  0.50 12.38 ? 71  ASN A CA  1 
ATOM   594   C  C   A ASN A 1 71  ? 36.331  1.675   16.770  0.50 11.78 ? 71  ASN A C   1 
ATOM   595   C  C   B ASN A 1 71  ? 36.331  1.816   16.804  0.50 12.48 ? 71  ASN A C   1 
ATOM   596   O  O   A ASN A 1 71  ? 36.764  0.723   17.455  0.50 12.76 ? 71  ASN A O   1 
ATOM   597   O  O   B ASN A 1 71  ? 36.897  1.080   17.632  0.50 13.53 ? 71  ASN A O   1 
ATOM   598   C  CB  A ASN A 1 71  ? 36.154  4.005   17.824  0.50 11.85 ? 71  ASN A CB  1 
ATOM   599   C  CB  B ASN A 1 71  ? 36.094  4.076   17.814  0.50 13.17 ? 71  ASN A CB  1 
ATOM   600   C  CG  A ASN A 1 71  ? 35.256  5.233   17.876  0.50 12.64 ? 71  ASN A CG  1 
ATOM   601   C  CG  B ASN A 1 71  ? 37.075  4.558   16.813  0.50 16.88 ? 71  ASN A CG  1 
ATOM   602   O  OD1 A ASN A 1 71  ? 34.063  5.193   17.528  0.50 14.26 ? 71  ASN A OD1 1 
ATOM   603   O  OD1 B ASN A 1 71  ? 36.692  4.927   15.697  0.50 19.38 ? 71  ASN A OD1 1 
ATOM   604   N  ND2 A ASN A 1 71  ? 35.837  6.381   18.268  0.50 17.69 ? 71  ASN A ND2 1 
ATOM   605   N  ND2 B ASN A 1 71  ? 38.351  4.551   17.169  0.50 23.92 ? 71  ASN A ND2 1 
ATOM   606   N  N   . LEU A 1 72  ? 36.559  1.760   15.482  1.00 10.13 ? 72  LEU A N   1 
ATOM   607   C  CA  . LEU A 1 72  ? 37.398  0.718   14.858  1.00 12.08 ? 72  LEU A CA  1 
ATOM   608   C  C   . LEU A 1 72  ? 38.512  1.398   14.057  1.00 12.81 ? 72  LEU A C   1 
ATOM   609   O  O   . LEU A 1 72  ? 38.351  2.551   13.604  1.00 12.89 ? 72  LEU A O   1 
ATOM   610   C  CB  . LEU A 1 72  ? 36.563  -0.169  13.862  1.00 9.71  ? 72  LEU A CB  1 
ATOM   611   C  CG  . LEU A 1 72  ? 35.525  -0.998  14.599  1.00 10.13 ? 72  LEU A CG  1 
ATOM   612   C  CD1 . LEU A 1 72  ? 34.505  -1.574  13.586  1.00 9.44  ? 72  LEU A CD1 1 
ATOM   613   C  CD2 . LEU A 1 72  ? 36.085  -2.131  15.587  1.00 12.14 ? 72  LEU A CD2 1 
ATOM   614   N  N   . PRO A 1 73  ? 39.651  0.680   13.846  1.00 13.08 ? 73  PRO A N   1 
ATOM   615   C  CA  . PRO A 1 73  ? 40.797  1.357   13.179  1.00 13.27 ? 73  PRO A CA  1 
ATOM   616   C  C   . PRO A 1 73  ? 40.707  1.214   11.700  1.00 13.16 ? 73  PRO A C   1 
ATOM   617   O  O   . PRO A 1 73  ? 40.262  0.198   11.177  1.00 14.04 ? 73  PRO A O   1 
ATOM   618   C  CB  . PRO A 1 73  ? 42.010  0.571   13.779  1.00 12.21 ? 73  PRO A CB  1 
ATOM   619   C  CG  . PRO A 1 73  ? 41.531  -0.812  13.926  1.00 12.18 ? 73  PRO A CG  1 
ATOM   620   C  CD  . PRO A 1 73  ? 39.975  -0.694  14.321  1.00 12.79 ? 73  PRO A CD  1 
ATOM   621   N  N   . SER A 1 74  ? 41.310  2.198   10.995  1.00 14.34 ? 74  SER A N   1 
ATOM   622   C  CA  . SER A 1 74  ? 41.157  2.211   9.552   1.00 15.89 ? 74  SER A CA  1 
ATOM   623   C  C   . SER A 1 74  ? 42.029  1.119   8.851   1.00 14.58 ? 74  SER A C   1 
ATOM   624   O  O   . SER A 1 74  ? 41.895  0.948   7.638   1.00 17.14 ? 74  SER A O   1 
ATOM   625   C  CB  . SER A 1 74  ? 41.424  3.623   8.982   1.00 18.46 ? 74  SER A CB  1 
ATOM   626   O  OG  . SER A 1 74  ? 42.722  4.063   9.355   1.00 21.71 ? 74  SER A OG  1 
ATOM   627   N  N   . ASP A 1 75  ? 42.950  0.416   9.545   1.00 13.68 ? 75  ASP A N   1 
ATOM   628   C  CA  . ASP A 1 75  ? 43.598  -0.651  8.826   1.00 14.66 ? 75  ASP A CA  1 
ATOM   629   C  C   . ASP A 1 75  ? 42.718  -1.912  8.725   1.00 12.25 ? 75  ASP A C   1 
ATOM   630   O  O   . ASP A 1 75  ? 43.045  -2.846  8.047   1.00 16.65 ? 75  ASP A O   1 
ATOM   631   C  CB  . ASP A 1 75  ? 44.960  -0.952  9.550   1.00 16.26 ? 75  ASP A CB  1 
ATOM   632   C  CG  . ASP A 1 75  ? 44.725  -1.330  10.964  1.00 17.99 ? 75  ASP A CG  1 
ATOM   633   O  OD1 . ASP A 1 75  ? 44.356  -0.452  11.737  1.00 23.78 ? 75  ASP A OD1 1 
ATOM   634   O  OD2 . ASP A 1 75  ? 44.937  -2.518  11.251  1.00 22.80 ? 75  ASP A OD2 1 
ATOM   635   N  N   . MET A 1 76  ? 41.586  -1.912  9.482   1.00 12.35 ? 76  MET A N   1 
ATOM   636   C  CA  . MET A 1 76  ? 40.584  -3.013  9.339   1.00 12.03 ? 76  MET A CA  1 
ATOM   637   C  C   . MET A 1 76  ? 39.729  -2.716  8.141   1.00 9.09  ? 76  MET A C   1 
ATOM   638   O  O   . MET A 1 76  ? 39.370  -1.531  7.954   1.00 11.15 ? 76  MET A O   1 
ATOM   639   C  CB  . MET A 1 76  ? 39.779  -2.943  10.583  1.00 12.96 ? 76  MET A CB  1 
ATOM   640   C  CG  . MET A 1 76  ? 38.634  -3.833  10.603  1.00 13.38 ? 76  MET A CG  1 
ATOM   641   S  SD  . MET A 1 76  ? 37.834  -3.847  12.225  1.00 12.64 ? 76  MET A SD  1 
ATOM   642   C  CE  . MET A 1 76  ? 36.201  -4.543  11.826  1.00 12.18 ? 76  MET A CE  1 
ATOM   643   N  N   . HIS A 1 77  ? 39.636  -3.638  7.264   1.00 9.63  ? 77  HIS A N   1 
ATOM   644   C  CA  . HIS A 1 77  ? 38.897  -3.399  6.032   1.00 8.56  ? 77  HIS A CA  1 
ATOM   645   C  C   . HIS A 1 77  ? 38.345  -4.610  5.435   1.00 9.42  ? 77  HIS A C   1 
ATOM   646   O  O   . HIS A 1 77  ? 38.708  -5.782  5.663   1.00 12.57 ? 77  HIS A O   1 
ATOM   647   C  CB  . HIS A 1 77  ? 39.829  -2.665  5.023   1.00 14.09 ? 77  HIS A CB  1 
ATOM   648   C  CG  . HIS A 1 77  ? 41.013  -3.478  4.527   1.00 12.15 ? 77  HIS A CG  1 
ATOM   649   N  ND1 . HIS A 1 77  ? 42.242  -3.400  5.141   1.00 15.52 ? 77  HIS A ND1 1 
ATOM   650   C  CD2 . HIS A 1 77  ? 41.187  -4.204  3.410   1.00 14.42 ? 77  HIS A CD2 1 
ATOM   651   C  CE1 . HIS A 1 77  ? 43.102  -4.123  4.442   1.00 14.19 ? 77  HIS A CE1 1 
ATOM   652   N  NE2 . HIS A 1 77  ? 42.496  -4.634  3.403   1.00 15.73 ? 77  HIS A NE2 1 
ATOM   653   N  N   . ILE A 1 78  ? 37.441  -4.351  4.478   1.00 11.21 ? 78  ILE A N   1 
ATOM   654   C  CA  . ILE A 1 78  ? 36.897  -5.359  3.583   1.00 12.46 ? 78  ILE A CA  1 
ATOM   655   C  C   . ILE A 1 78  ? 37.660  -5.385  2.273   1.00 11.49 ? 78  ILE A C   1 
ATOM   656   O  O   . ILE A 1 78  ? 37.831  -4.332  1.698   1.00 12.42 ? 78  ILE A O   1 
ATOM   657   C  CB  . ILE A 1 78  ? 35.349  -5.035  3.271   1.00 12.42 ? 78  ILE A CB  1 
ATOM   658   C  CG1 . ILE A 1 78  ? 34.467  -5.230  4.534   1.00 14.60 ? 78  ILE A CG1 1 
ATOM   659   C  CG2 . ILE A 1 78  ? 34.836  -5.929  2.180   1.00 17.35 ? 78  ILE A CG2 1 
ATOM   660   C  CD1 . ILE A 1 78  ? 33.047  -4.444  4.305   1.00 14.45 ? 78  ILE A CD1 1 
ATOM   661   N  N   . GLN A 1 79  ? 38.019  -6.595  1.832   1.00 12.97 ? 79  GLN A N   1 
ATOM   662   C  CA  . GLN A 1 79  ? 38.551  -6.813  0.524   1.00 15.23 ? 79  GLN A CA  1 
ATOM   663   C  C   . GLN A 1 79  ? 37.504  -7.599  -0.278  1.00 15.60 ? 79  GLN A C   1 
ATOM   664   O  O   . GLN A 1 79  ? 36.856  -8.517  0.201   1.00 16.49 ? 79  GLN A O   1 
ATOM   665   C  CB  . GLN A 1 79  ? 39.843  -7.606  0.710   1.00 18.80 ? 79  GLN A CB  1 
ATOM   666   C  CG  . GLN A 1 79  ? 40.424  -7.969  -0.626  1.00 24.74 ? 79  GLN A CG  1 
ATOM   667   C  CD  . GLN A 1 79  ? 41.770  -8.497  -0.409  1.00 37.35 ? 79  GLN A CD  1 
ATOM   668   O  OE1 . GLN A 1 79  ? 42.735  -7.738  -0.330  1.00 43.94 ? 79  GLN A OE1 1 
ATOM   669   N  NE2 . GLN A 1 79  ? 41.866  -9.810  -0.274  1.00 45.48 ? 79  GLN A NE2 1 
ATOM   670   N  N   . GLY A 1 80  ? 37.360  -7.279  -1.556  1.00 16.54 ? 80  GLY A N   1 
ATOM   671   C  CA  . GLY A 1 80  ? 36.350  -7.963  -2.411  1.00 18.04 ? 80  GLY A CA  1 
ATOM   672   C  C   . GLY A 1 80  ? 35.392  -7.050  -3.156  1.00 17.82 ? 80  GLY A C   1 
ATOM   673   O  O   . GLY A 1 80  ? 34.726  -7.514  -4.128  1.00 18.45 ? 80  GLY A O   1 
ATOM   674   N  N   . LEU A 1 81  ? 35.225  -5.828  -2.640  1.00 16.51 ? 81  LEU A N   1 
ATOM   675   C  CA  . LEU A 1 81  ? 34.356  -4.772  -3.261  1.00 18.55 ? 81  LEU A CA  1 
ATOM   676   C  C   . LEU A 1 81  ? 35.156  -3.991  -4.364  1.00 20.16 ? 81  LEU A C   1 
ATOM   677   O  O   . LEU A 1 81  ? 36.341  -4.269  -4.549  1.00 22.61 ? 81  LEU A O   1 
ATOM   678   C  CB  . LEU A 1 81  ? 33.699  -3.857  -2.237  1.00 16.54 ? 81  LEU A CB  1 
ATOM   679   C  CG  . LEU A 1 81  ? 32.844  -4.649  -1.205  1.00 13.26 ? 81  LEU A CG  1 
ATOM   680   C  CD1 . LEU A 1 81  ? 32.362  -3.679  -0.188  1.00 15.72 ? 81  LEU A CD1 1 
ATOM   681   C  CD2 . LEU A 1 81  ? 31.595  -5.262  -1.995  1.00 16.53 ? 81  LEU A CD2 1 
ATOM   682   N  N   . GLN A 1 82  ? 34.481  -3.006  -4.997  1.00 22.64 ? 82  GLN A N   1 
ATOM   683   C  CA  . GLN A 1 82  ? 35.100  -2.166  -6.085  1.00 24.02 ? 82  GLN A CA  1 
ATOM   684   C  C   . GLN A 1 82  ? 36.120  -1.177  -5.597  1.00 23.21 ? 82  GLN A C   1 
ATOM   685   O  O   . GLN A 1 82  ? 36.851  -0.504  -6.371  1.00 25.31 ? 82  GLN A O   1 
ATOM   686   C  CB  . GLN A 1 82  ? 34.043  -1.368  -6.809  1.00 24.33 ? 82  GLN A CB  1 
ATOM   687   C  CG  . GLN A 1 82  ? 32.983  -2.302  -7.562  1.00 27.48 ? 82  GLN A CG  1 
ATOM   688   C  CD  . GLN A 1 82  ? 33.481  -2.927  -8.894  1.00 38.12 ? 82  GLN A CD  1 
ATOM   689   O  OE1 . GLN A 1 82  ? 34.469  -2.457  -9.530  1.00 37.76 ? 82  GLN A OE1 1 
ATOM   690   N  NE2 . GLN A 1 82  ? 32.752  -3.996  -9.346  1.00 35.74 ? 82  GLN A NE2 1 
ATOM   691   N  N   . SER A 1 83  ? 36.109  -0.966  -4.333  1.00 19.53 ? 83  SER A N   1 
ATOM   692   C  CA  . SER A 1 83  ? 37.133  -0.140  -3.726  1.00 15.29 ? 83  SER A CA  1 
ATOM   693   C  C   . SER A 1 83  ? 37.401  -0.832  -2.406  1.00 15.05 ? 83  SER A C   1 
ATOM   694   O  O   . SER A 1 83  ? 36.560  -1.663  -1.937  1.00 12.50 ? 83  SER A O   1 
ATOM   695   C  CB  . SER A 1 83  ? 36.558  1.194   -3.403  1.00 14.78 ? 83  SER A CB  1 
ATOM   696   O  OG  . SER A 1 83  ? 36.261  1.901   -4.628  1.00 19.31 ? 83  SER A OG  1 
ATOM   697   N  N   . ARG A 1 84  ? 38.483  -0.408  -1.746  1.00 12.88 ? 84  ARG A N   1 
ATOM   698   C  CA  . ARG A 1 84  ? 38.660  -0.897  -0.373  1.00 11.29 ? 84  ARG A CA  1 
ATOM   699   C  C   . ARG A 1 84  ? 37.698  -0.076  0.525   1.00 10.74 ? 84  ARG A C   1 
ATOM   700   O  O   . ARG A 1 84  ? 37.583  1.127   0.411   1.00 13.23 ? 84  ARG A O   1 
ATOM   701   C  CB  . ARG A 1 84  ? 40.107  -0.576  0.045   1.00 12.41 ? 84  ARG A CB  1 
ATOM   702   C  CG  . ARG A 1 84  ? 40.323  -0.998  1.533   1.00 10.63 ? 84  ARG A CG  1 
ATOM   703   C  CD  . ARG A 1 84  ? 41.764  -0.836  2.003   1.00 12.18 ? 84  ARG A CD  1 
ATOM   704   N  NE  . ARG A 1 84  ? 42.632  -1.854  1.451   1.00 14.06 ? 84  ARG A NE  1 
ATOM   705   C  CZ  . ARG A 1 84  ? 43.896  -1.972  1.816   1.00 12.54 ? 84  ARG A CZ  1 
ATOM   706   N  NH1 . ARG A 1 84  ? 44.393  -1.119  2.698   1.00 14.88 ? 84  ARG A NH1 1 
ATOM   707   N  NH2 . ARG A 1 84  ? 44.660  -2.917  1.299   1.00 17.05 ? 84  ARG A NH2 1 
ATOM   708   N  N   . TYR A 1 85  ? 37.015  -0.795  1.486   1.00 11.04 ? 85  TYR A N   1 
ATOM   709   C  CA  . TYR A 1 85  ? 36.196  -0.103  2.438   1.00 10.16 ? 85  TYR A CA  1 
ATOM   710   C  C   . TYR A 1 85  ? 36.772  -0.372  3.848   1.00 9.21  ? 85  TYR A C   1 
ATOM   711   O  O   . TYR A 1 85  ? 36.844  -1.590  4.278   1.00 11.80 ? 85  TYR A O   1 
ATOM   712   C  CB  . TYR A 1 85  ? 34.734  -0.574  2.389   1.00 11.63 ? 85  TYR A CB  1 
ATOM   713   C  CG  . TYR A 1 85  ? 33.972  0.000   1.204   1.00 9.11  ? 85  TYR A CG  1 
ATOM   714   C  CD1 . TYR A 1 85  ? 33.153  1.117   1.349   1.00 8.60  ? 85  TYR A CD1 1 
ATOM   715   C  CD2 . TYR A 1 85  ? 34.086  -0.567  -0.062  1.00 12.00 ? 85  TYR A CD2 1 
ATOM   716   C  CE1 . TYR A 1 85  ? 32.464  1.646   0.265   1.00 8.28  ? 85  TYR A CE1 1 
ATOM   717   C  CE2 . TYR A 1 85  ? 33.400  -0.043  -1.150  1.00 11.26 ? 85  TYR A CE2 1 
ATOM   718   C  CZ  . TYR A 1 85  ? 32.592  1.063   -0.979  1.00 10.28 ? 85  TYR A CZ  1 
ATOM   719   O  OH  . TYR A 1 85  ? 31.908  1.589   -2.052  1.00 17.15 ? 85  TYR A OH  1 
ATOM   720   N  N   . SER A 1 86  ? 37.222  0.715   4.480   1.00 9.00  ? 86  SER A N   1 
ATOM   721   C  CA  . SER A 1 86  ? 37.926  0.620   5.796   1.00 9.96  ? 86  SER A CA  1 
ATOM   722   C  C   . SER A 1 86  ? 36.915  0.805   6.928   1.00 11.13 ? 86  SER A C   1 
ATOM   723   O  O   . SER A 1 86  ? 35.981  1.614   6.828   1.00 11.74 ? 86  SER A O   1 
ATOM   724   C  CB  . SER A 1 86  ? 39.012  1.725   5.915   1.00 11.50 ? 86  SER A CB  1 
ATOM   725   O  OG  . SER A 1 86  ? 40.015  1.423   4.953   1.00 14.08 ? 86  SER A OG  1 
ATOM   726   N  N   . ALA A 1 87  ? 37.132  0.061   8.024   1.00 9.27  ? 87  ALA A N   1 
ATOM   727   C  CA  . ALA A 1 87  ? 36.208  0.167   9.157   1.00 9.82  ? 87  ALA A CA  1 
ATOM   728   C  C   . ALA A 1 87  ? 36.278  1.511   9.838   1.00 10.61 ? 87  ALA A C   1 
ATOM   729   O  O   . ALA A 1 87  ? 37.353  2.169   9.886   1.00 12.03 ? 87  ALA A O   1 
ATOM   730   C  CB  . ALA A 1 87  ? 36.507  -0.831  10.224  1.00 10.99 ? 87  ALA A CB  1 
ATOM   731   N  N   . THR A 1 88  ? 35.125  1.960   10.339  1.00 10.29 ? 88  THR A N   1 
ATOM   732   C  CA  . THR A 1 88  ? 35.085  3.115   11.198  1.00 10.13 ? 88  THR A CA  1 
ATOM   733   C  C   . THR A 1 88  ? 34.453  2.849   12.563  1.00 10.08 ? 88  THR A C   1 
ATOM   734   O  O   . THR A 1 88  ? 34.914  3.413   13.578  1.00 9.73  ? 88  THR A O   1 
ATOM   735   C  CB  . THR A 1 88  ? 34.471  4.315   10.452  1.00 11.63 ? 88  THR A CB  1 
ATOM   736   O  OG1 . THR A 1 88  ? 34.340  5.372   11.347  1.00 14.70 ? 88  THR A OG1 1 
ATOM   737   C  CG2 . THR A 1 88  ? 33.016  4.015   9.965   1.00 11.85 ? 88  THR A CG2 1 
ATOM   738   N  N   . GLN A 1 89  ? 33.393  2.022   12.626  1.00 9.22  ? 89  GLN A N   1 
ATOM   739   C  CA  . GLN A 1 89  ? 32.745  1.831   13.914  1.00 10.63 ? 89  GLN A CA  1 
ATOM   740   C  C   . GLN A 1 89  ? 31.763  0.619   13.763  1.00 10.20 ? 89  GLN A C   1 
ATOM   741   O  O   . GLN A 1 89  ? 31.361  0.310   12.649  1.00 10.87 ? 89  GLN A O   1 
ATOM   742   C  CB  . GLN A 1 89  ? 31.965  3.070   14.444  1.00 11.34 ? 89  GLN A CB  1 
ATOM   743   C  CG  . GLN A 1 89  ? 30.990  3.621   13.472  1.00 12.55 ? 89  GLN A CG  1 
ATOM   744   C  CD  . GLN A 1 89  ? 29.522  3.419   13.914  1.00 13.64 ? 89  GLN A CD  1 
ATOM   745   O  OE1 . GLN A 1 89  ? 29.177  2.322   14.290  1.00 13.28 ? 89  GLN A OE1 1 
ATOM   746   N  NE2 . GLN A 1 89  ? 28.760  4.409   13.953  1.00 20.14 ? 89  GLN A NE2 1 
ATOM   747   N  N   . LEU A 1 90  ? 31.418  0.016   14.894  1.00 9.34  ? 90  LEU A N   1 
ATOM   748   C  CA  . LEU A 1 90  ? 30.252  -0.879  14.912  1.00 7.22  ? 90  LEU A CA  1 
ATOM   749   C  C   . LEU A 1 90  ? 29.304  -0.469  15.961  1.00 7.98  ? 90  LEU A C   1 
ATOM   750   O  O   . LEU A 1 90  ? 29.657  0.229   16.948  1.00 8.01  ? 90  LEU A O   1 
ATOM   751   C  CB  . LEU A 1 90  ? 30.675  -2.389  15.036  1.00 7.45  ? 90  LEU A CB  1 
ATOM   752   C  CG  . LEU A 1 90  ? 31.491  -2.798  16.281  1.00 8.55  ? 90  LEU A CG  1 
ATOM   753   C  CD1 . LEU A 1 90  ? 30.585  -2.939  17.551  1.00 10.04 ? 90  LEU A CD1 1 
ATOM   754   C  CD2 . LEU A 1 90  ? 32.162  -4.152  15.956  1.00 10.68 ? 90  LEU A CD2 1 
ATOM   755   N  N   . HIS A 1 91  ? 28.032  -0.866  15.782  1.00 7.64  ? 91  HIS A N   1 
ATOM   756   C  CA  . HIS A 1 91  ? 26.997  -0.532  16.784  1.00 6.60  ? 91  HIS A CA  1 
ATOM   757   C  C   . HIS A 1 91  ? 25.833  -1.488  16.603  1.00 7.82  ? 91  HIS A C   1 
ATOM   758   O  O   . HIS A 1 91  ? 25.890  -2.351  15.691  1.00 7.11  ? 91  HIS A O   1 
ATOM   759   C  CB  . HIS A 1 91  ? 26.559  0.967   16.608  1.00 6.81  ? 91  HIS A CB  1 
ATOM   760   C  CG  . HIS A 1 91  ? 25.894  1.156   15.263  1.00 8.50  ? 91  HIS A CG  1 
ATOM   761   N  ND1 . HIS A 1 91  ? 26.614  1.592   14.173  1.00 7.98  ? 91  HIS A ND1 1 
ATOM   762   C  CD2 . HIS A 1 91  ? 24.630  0.852   14.808  1.00 6.84  ? 91  HIS A CD2 1 
ATOM   763   C  CE1 . HIS A 1 91  ? 25.833  1.563   13.104  1.00 8.03  ? 91  HIS A CE1 1 
ATOM   764   N  NE2 . HIS A 1 91  ? 24.624  1.119   13.442  1.00 7.01  ? 91  HIS A NE2 1 
ATOM   765   N  N   . LEU A 1 92  ? 24.827  -1.383  17.447  1.00 7.83  ? 92  LEU A N   1 
ATOM   766   C  CA  . LEU A 1 92  ? 23.730  -2.321  17.389  1.00 6.49  ? 92  LEU A CA  1 
ATOM   767   C  C   . LEU A 1 92  ? 22.379  -1.612  17.463  1.00 6.17  ? 92  LEU A C   1 
ATOM   768   O  O   . LEU A 1 92  ? 22.247  -0.444  17.802  1.00 7.96  ? 92  LEU A O   1 
ATOM   769   C  CB  . LEU A 1 92  ? 23.763  -3.297  18.612  1.00 10.57 ? 92  LEU A CB  1 
ATOM   770   C  CG  . LEU A 1 92  ? 25.001  -4.202  18.595  1.00 7.24  ? 92  LEU A CG  1 
ATOM   771   C  CD1 . LEU A 1 92  ? 26.090  -3.609  19.533  1.00 14.37 ? 92  LEU A CD1 1 
ATOM   772   C  CD2 . LEU A 1 92  ? 24.612  -5.664  18.946  1.00 12.38 ? 92  LEU A CD2 1 
ATOM   773   N  N   . HIS A 1 93  ? 21.337  -2.360  17.082  1.00 6.75  ? 93  HIS A N   1 
ATOM   774   C  CA  . HIS A 1 93  ? 19.901  -1.911  17.170  1.00 7.10  ? 93  HIS A CA  1 
ATOM   775   C  C   . HIS A 1 93  ? 19.136  -3.033  17.788  1.00 6.95  ? 93  HIS A C   1 
ATOM   776   O  O   . HIS A 1 93  ? 19.432  -4.243  17.564  1.00 6.63  ? 93  HIS A O   1 
ATOM   777   C  CB  . HIS A 1 93  ? 19.333  -1.661  15.714  1.00 8.20  ? 93  HIS A CB  1 
ATOM   778   C  CG  . HIS A 1 93  ? 20.091  -0.659  14.932  1.00 5.70  ? 93  HIS A CG  1 
ATOM   779   N  ND1 . HIS A 1 93  ? 19.826  0.699   14.939  1.00 7.62  ? 93  HIS A ND1 1 
ATOM   780   C  CD2 . HIS A 1 93  ? 21.155  -0.846  14.127  1.00 5.86  ? 93  HIS A CD2 1 
ATOM   781   C  CE1 . HIS A 1 93  ? 20.721  1.313   14.136  1.00 7.99  ? 93  HIS A CE1 1 
ATOM   782   N  NE2 . HIS A 1 93  ? 21.537  0.409   13.637  1.00 7.66  ? 93  HIS A NE2 1 
ATOM   783   N  N   . TRP A 1 94  ? 18.218  -2.694  18.670  1.00 7.51  ? 94  TRP A N   1 
ATOM   784   C  CA  . TRP A 1 94  ? 17.445  -3.735  19.366  1.00 7.18  ? 94  TRP A CA  1 
ATOM   785   C  C   . TRP A 1 94  ? 16.037  -3.217  19.761  1.00 9.15  ? 94  TRP A C   1 
ATOM   786   O  O   . TRP A 1 94  ? 15.714  -2.039  19.585  1.00 7.45  ? 94  TRP A O   1 
ATOM   787   C  CB  . TRP A 1 94  ? 18.176  -4.209  20.642  1.00 8.31  ? 94  TRP A CB  1 
ATOM   788   C  CG  . TRP A 1 94  ? 18.502  -3.002  21.613  1.00 7.84  ? 94  TRP A CG  1 
ATOM   789   C  CD1 . TRP A 1 94  ? 17.699  -2.547  22.611  1.00 9.17  ? 94  TRP A CD1 1 
ATOM   790   C  CD2 . TRP A 1 94  ? 19.691  -2.175  21.600  1.00 8.62  ? 94  TRP A CD2 1 
ATOM   791   N  NE1 . TRP A 1 94  ? 18.326  -1.429  23.263  1.00 8.95  ? 94  TRP A NE1 1 
ATOM   792   C  CE2 . TRP A 1 94  ? 19.570  -1.243  22.679  1.00 9.21  ? 94  TRP A CE2 1 
ATOM   793   C  CE3 . TRP A 1 94  ? 20.899  -2.172  20.847  1.00 9.03  ? 94  TRP A CE3 1 
ATOM   794   C  CZ2 . TRP A 1 94  ? 20.558  -0.305  23.005  1.00 8.51  ? 94  TRP A CZ2 1 
ATOM   795   C  CZ3 . TRP A 1 94  ? 21.868  -1.192  21.142  1.00 8.15  ? 94  TRP A CZ3 1 
ATOM   796   C  CH2 . TRP A 1 94  ? 21.689  -0.305  22.212  1.00 8.18  ? 94  TRP A CH2 1 
ATOM   797   N  N   . GLY A 1 95  ? 15.263  -4.091  20.365  1.00 7.84  ? 95  GLY A N   1 
ATOM   798   C  CA  . GLY A 1 95  ? 13.862  -3.788  20.730  1.00 9.39  ? 95  GLY A CA  1 
ATOM   799   C  C   . GLY A 1 95  ? 13.752  -3.471  22.234  1.00 8.07  ? 95  GLY A C   1 
ATOM   800   O  O   . GLY A 1 95  ? 14.391  -2.571  22.807  1.00 8.29  ? 95  GLY A O   1 
ATOM   801   N  N   . ASN A 1 96  ? 12.932  -4.331  22.907  1.00 8.80  ? 96  ASN A N   1 
ATOM   802   C  CA  . ASN A 1 96  ? 12.727  -4.094  24.372  1.00 9.20  ? 96  ASN A CA  1 
ATOM   803   C  C   . ASN A 1 96  ? 12.208  -5.432  24.948  1.00 10.98 ? 96  ASN A C   1 
ATOM   804   O  O   . ASN A 1 96  ? 11.743  -6.288  24.209  1.00 10.33 ? 96  ASN A O   1 
ATOM   805   C  CB  . ASN A 1 96  ? 11.772  -2.962  24.637  1.00 10.13 ? 96  ASN A CB  1 
ATOM   806   C  CG  . ASN A 1 96  ? 10.347  -3.342  24.324  1.00 12.87 ? 96  ASN A CG  1 
ATOM   807   O  OD1 . ASN A 1 96  ? 9.684   -3.942  25.214  1.00 14.46 ? 96  ASN A OD1 1 
ATOM   808   N  ND2 . ASN A 1 96  ? 9.826   -3.035  23.154  1.00 14.32 ? 96  ASN A ND2 1 
ATOM   809   N  N   . PRO A 1 97  ? 12.308  -5.596  26.304  1.00 10.31 ? 97  PRO A N   1 
ATOM   810   C  CA  . PRO A 1 97  ? 12.007  -6.925  26.800  1.00 9.85  ? 97  PRO A CA  1 
ATOM   811   C  C   . PRO A 1 97  ? 10.546  -7.379  26.578  1.00 10.15 ? 97  PRO A C   1 
ATOM   812   O  O   . PRO A 1 97  ? 10.294  -8.574  26.547  1.00 12.59 ? 97  PRO A O   1 
ATOM   813   C  CB  . PRO A 1 97  ? 12.310  -6.826  28.303  1.00 11.54 ? 97  PRO A CB  1 
ATOM   814   C  CG  . PRO A 1 97  ? 13.426  -5.738  28.385  1.00 12.51 ? 97  PRO A CG  1 
ATOM   815   C  CD  . PRO A 1 97  ? 12.920  -4.751  27.366  1.00 13.15 ? 97  PRO A CD  1 
ATOM   816   N  N   . ASN A 1 98  ? 9.639   -6.441  26.477  1.00 10.37 ? 98  ASN A N   1 
ATOM   817   C  CA  . ASN A 1 98  ? 8.213   -6.829  26.140  1.00 12.95 ? 98  ASN A CA  1 
ATOM   818   C  C   . ASN A 1 98  ? 7.966   -7.189  24.678  1.00 11.55 ? 98  ASN A C   1 
ATOM   819   O  O   . ASN A 1 98  ? 6.965   -7.783  24.332  1.00 14.91 ? 98  ASN A O   1 
ATOM   820   C  CB  . ASN A 1 98  ? 7.243   -5.682  26.516  1.00 11.16 ? 98  ASN A CB  1 
ATOM   821   C  CG  . ASN A 1 98  ? 7.128   -5.519  28.043  1.00 20.84 ? 98  ASN A CG  1 
ATOM   822   O  OD1 . ASN A 1 98  ? 7.235   -6.470  28.780  1.00 27.66 ? 98  ASN A OD1 1 
ATOM   823   N  ND2 . ASN A 1 98  ? 6.818   -4.341  28.466  1.00 24.87 ? 98  ASN A ND2 1 
ATOM   824   N  N   . ASP A 1 99  ? 8.884   -6.807  23.789  1.00 10.04 ? 99  ASP A N   1 
ATOM   825   C  CA  . ASP A 1 99  ? 8.738   -7.097  22.380  1.00 9.99  ? 99  ASP A CA  1 
ATOM   826   C  C   . ASP A 1 99  ? 10.159  -7.203  21.770  1.00 11.02 ? 99  ASP A C   1 
ATOM   827   O  O   . ASP A 1 99  ? 10.688  -6.242  21.183  1.00 10.43 ? 99  ASP A O   1 
ATOM   828   C  CB  . ASP A 1 99  ? 7.895   -6.019  21.685  1.00 11.17 ? 99  ASP A CB  1 
ATOM   829   C  CG  . ASP A 1 99  ? 7.359   -6.471  20.319  1.00 13.27 ? 99  ASP A CG  1 
ATOM   830   O  OD1 . ASP A 1 99  ? 7.814   -7.473  19.767  1.00 15.96 ? 99  ASP A OD1 1 
ATOM   831   O  OD2 . ASP A 1 99  ? 6.451   -5.821  19.831  1.00 17.56 ? 99  ASP A OD2 1 
ATOM   832   N  N   . PRO A 1 100 ? 10.870  -8.273  22.081  1.00 8.94  ? 100 PRO A N   1 
ATOM   833   C  CA  . PRO A 1 100 ? 12.345  -8.340  21.909  1.00 9.23  ? 100 PRO A CA  1 
ATOM   834   C  C   . PRO A 1 100 ? 12.676  -8.716  20.489  1.00 12.26 ? 100 PRO A C   1 
ATOM   835   O  O   . PRO A 1 100 ? 13.238  -9.750  20.170  1.00 11.01 ? 100 PRO A O   1 
ATOM   836   C  CB  . PRO A 1 100 ? 12.773  -9.430  22.911  1.00 11.68 ? 100 PRO A CB  1 
ATOM   837   C  CG  . PRO A 1 100 ? 11.544  -10.379 22.913  1.00 11.59 ? 100 PRO A CG  1 
ATOM   838   C  CD  . PRO A 1 100 ? 10.341  -9.458  22.853  1.00 11.16 ? 100 PRO A CD  1 
ATOM   839   N  N   . HIS A 1 101 ? 12.233  -7.863  19.581  1.00 10.43 ? 101 HIS A N   1 
ATOM   840   C  CA  . HIS A 1 101 ? 12.316  -8.133  18.109  1.00 10.86 ? 101 HIS A CA  1 
ATOM   841   C  C   . HIS A 1 101 ? 12.664  -6.881  17.357  1.00 11.88 ? 101 HIS A C   1 
ATOM   842   O  O   . HIS A 1 101 ? 11.869  -6.381  16.533  1.00 14.99 ? 101 HIS A O   1 
ATOM   843   C  CB  . HIS A 1 101 ? 10.963  -8.678  17.561  1.00 12.05 ? 101 HIS A CB  1 
ATOM   844   C  CG  . HIS A 1 101 ? 10.462  -9.805  18.373  1.00 12.92 ? 101 HIS A CG  1 
ATOM   845   N  ND1 . HIS A 1 101 ? 10.984  -11.072 18.341  1.00 14.62 ? 101 HIS A ND1 1 
ATOM   846   C  CD2 . HIS A 1 101 ? 9.438   -9.835  19.258  1.00 13.02 ? 101 HIS A CD2 1 
ATOM   847   C  CE1 . HIS A 1 101 ? 10.294  -11.846 19.177  1.00 15.20 ? 101 HIS A CE1 1 
ATOM   848   N  NE2 . HIS A 1 101 ? 9.390   -11.096 19.777  1.00 14.38 ? 101 HIS A NE2 1 
ATOM   849   N  N   . GLY A 1 102 ? 13.891  -6.450  17.595  1.00 8.15  ? 102 GLY A N   1 
ATOM   850   C  CA  . GLY A 1 102 ? 14.326  -5.098  17.208  1.00 8.07  ? 102 GLY A CA  1 
ATOM   851   C  C   . GLY A 1 102 ? 15.420  -5.040  16.138  1.00 7.32  ? 102 GLY A C   1 
ATOM   852   O  O   . GLY A 1 102 ? 16.102  -4.031  16.031  1.00 7.81  ? 102 GLY A O   1 
ATOM   853   N  N   . SER A 1 103 ? 15.592  -6.076  15.316  1.00 7.14  ? 103 SER A N   1 
ATOM   854   C  CA  . SER A 1 103 ? 16.450  -5.886  14.119  1.00 5.76  ? 103 SER A CA  1 
ATOM   855   C  C   . SER A 1 103 ? 15.852  -4.808  13.212  1.00 8.08  ? 103 SER A C   1 
ATOM   856   O  O   . SER A 1 103 ? 14.639  -4.513  13.271  1.00 8.73  ? 103 SER A O   1 
ATOM   857   C  CB  . SER A 1 103 ? 16.598  -7.163  13.308  1.00 6.97  ? 103 SER A CB  1 
ATOM   858   O  OG  . SER A 1 103 ? 15.334  -7.599  12.704  1.00 7.20  ? 103 SER A OG  1 
ATOM   859   N  N   . GLU A 1 104 ? 16.695  -4.306  12.345  1.00 6.40  ? 104 GLU A N   1 
ATOM   860   C  CA  . GLU A 1 104 ? 16.223  -3.331  11.355  1.00 6.64  ? 104 GLU A CA  1 
ATOM   861   C  C   . GLU A 1 104 ? 15.760  -4.003  10.062  1.00 6.92  ? 104 GLU A C   1 
ATOM   862   O  O   . GLU A 1 104 ? 14.612  -3.833  9.646   1.00 6.70  ? 104 GLU A O   1 
ATOM   863   C  CB  . GLU A 1 104 ? 17.374  -2.336  11.023  1.00 7.32  ? 104 GLU A CB  1 
ATOM   864   C  CG  . GLU A 1 104 ? 17.905  -1.626  12.278  1.00 7.48  ? 104 GLU A CG  1 
ATOM   865   C  CD  . GLU A 1 104 ? 18.278  -0.176  11.935  1.00 6.84  ? 104 GLU A CD  1 
ATOM   866   O  OE1 . GLU A 1 104 ? 19.328  0.004   11.373  1.00 7.93  ? 104 GLU A OE1 1 
ATOM   867   O  OE2 . GLU A 1 104 ? 17.429  0.674   12.192  1.00 8.93  ? 104 GLU A OE2 1 
ATOM   868   N  N   . HIS A 1 105 ? 16.601  -4.812  9.462   1.00 6.09  ? 105 HIS A N   1 
ATOM   869   C  CA  . HIS A 1 105 ? 16.123  -5.659  8.351   1.00 6.42  ? 105 HIS A CA  1 
ATOM   870   C  C   . HIS A 1 105 ? 15.183  -6.755  8.894   1.00 6.63  ? 105 HIS A C   1 
ATOM   871   O  O   . HIS A 1 105 ? 15.382  -7.249  10.022  1.00 7.39  ? 105 HIS A O   1 
ATOM   872   C  CB  . HIS A 1 105 ? 17.310  -6.238  7.592   1.00 6.42  ? 105 HIS A CB  1 
ATOM   873   C  CG  . HIS A 1 105 ? 18.072  -5.175  6.867   1.00 6.56  ? 105 HIS A CG  1 
ATOM   874   N  ND1 . HIS A 1 105 ? 19.120  -4.476  7.436   1.00 6.76  ? 105 HIS A ND1 1 
ATOM   875   C  CD2 . HIS A 1 105 ? 17.868  -4.684  5.623   1.00 7.22  ? 105 HIS A CD2 1 
ATOM   876   C  CE1 . HIS A 1 105 ? 19.522  -3.534  6.575   1.00 7.24  ? 105 HIS A CE1 1 
ATOM   877   N  NE2 . HIS A 1 105 ? 18.817  -3.657  5.471   1.00 8.08  ? 105 HIS A NE2 1 
ATOM   878   N  N   . THR A 1 106 ? 14.226  -7.123  8.071   1.00 6.76  ? 106 THR A N   1 
ATOM   879   C  CA  . THR A 1 106 ? 13.389  -8.359  8.354   1.00 6.58  ? 106 THR A CA  1 
ATOM   880   C  C   . THR A 1 106 ? 13.570  -9.291  7.244   1.00 6.47  ? 106 THR A C   1 
ATOM   881   O  O   . THR A 1 106 ? 14.010  -9.001  6.135   1.00 7.99  ? 106 THR A O   1 
ATOM   882   C  CB  . THR A 1 106 ? 11.914  -7.906  8.519   1.00 8.65  ? 106 THR A CB  1 
ATOM   883   O  OG1 . THR A 1 106 ? 11.475  -7.278  7.292   1.00 7.80  ? 106 THR A OG1 1 
ATOM   884   C  CG2 . THR A 1 106 ? 11.749  -6.947  9.694   1.00 9.11  ? 106 THR A CG2 1 
ATOM   885   N  N   . VAL A 1 107 ? 13.262  -10.572 7.556   1.00 8.13  ? 107 VAL A N   1 
ATOM   886   C  CA  . VAL A 1 107 ? 13.338  -11.637 6.590   1.00 8.55  ? 107 VAL A CA  1 
ATOM   887   C  C   . VAL A 1 107 ? 11.921  -12.307 6.475   1.00 7.84  ? 107 VAL A C   1 
ATOM   888   O  O   . VAL A 1 107 ? 11.370  -12.746 7.499   1.00 9.14  ? 107 VAL A O   1 
ATOM   889   C  CB  . VAL A 1 107 ? 14.409  -12.712 6.903   1.00 9.06  ? 107 VAL A CB  1 
ATOM   890   C  CG1 . VAL A 1 107 ? 14.314  -13.878 5.951   1.00 11.22 ? 107 VAL A CG1 1 
ATOM   891   C  CG2 . VAL A 1 107 ? 15.880  -12.123 7.009   1.00 9.73  ? 107 VAL A CG2 1 
ATOM   892   N  N   . SER A 1 108 ? 11.302  -12.208 5.304   1.00 9.35  ? 108 SER A N   1 
ATOM   893   C  CA  . SER A 1 108 ? 9.937   -12.730 5.090   1.00 10.12 ? 108 SER A CA  1 
ATOM   894   C  C   . SER A 1 108 ? 9.033   -12.182 6.167   1.00 9.98  ? 108 SER A C   1 
ATOM   895   O  O   . SER A 1 108 ? 8.159   -12.828 6.741   1.00 10.82 ? 108 SER A O   1 
ATOM   896   C  CB  . SER A 1 108 ? 9.984   -14.240 5.092   1.00 10.68 ? 108 SER A CB  1 
ATOM   897   O  OG  . SER A 1 108 ? 10.770  -14.749 4.036   1.00 15.60 ? 108 SER A OG  1 
ATOM   898   N  N   . GLY A 1 109 ? 9.208   -10.865 6.434   1.00 7.73  ? 109 GLY A N   1 
ATOM   899   C  CA  . GLY A 1 109 ? 8.343   -10.086 7.334   1.00 9.42  ? 109 GLY A CA  1 
ATOM   900   C  C   . GLY A 1 109 ? 8.691   -10.211 8.833   1.00 11.79 ? 109 GLY A C   1 
ATOM   901   O  O   . GLY A 1 109 ? 8.014   -9.627  9.631   1.00 14.77 ? 109 GLY A O   1 
ATOM   902   N  N   . GLN A 1 110 ? 9.675   -11.081 9.183   1.00 10.20 ? 110 GLN A N   1 
ATOM   903   C  CA  . GLN A 1 110 ? 10.034  -11.276 10.559  1.00 9.64  ? 110 GLN A CA  1 
ATOM   904   C  C   . GLN A 1 110 ? 11.289  -10.553 11.046  1.00 7.88  ? 110 GLN A C   1 
ATOM   905   O  O   . GLN A 1 110 ? 12.306  -10.549 10.365  1.00 8.06  ? 110 GLN A O   1 
ATOM   906   C  CB  . GLN A 1 110 ? 10.317  -12.721 10.718  1.00 11.98 ? 110 GLN A CB  1 
ATOM   907   C  CG  . GLN A 1 110 ? 9.220   -13.710 10.206  1.00 12.65 ? 110 GLN A CG  1 
ATOM   908   C  CD  . GLN A 1 110 ? 7.817   -13.264 10.626  1.00 12.00 ? 110 GLN A CD  1 
ATOM   909   O  OE1 . GLN A 1 110 ? 7.479   -13.185 11.792  1.00 15.09 ? 110 GLN A OE1 1 
ATOM   910   N  NE2 . GLN A 1 110 ? 7.007   -12.979 9.631   1.00 14.78 ? 110 GLN A NE2 1 
ATOM   911   N  N   . HIS A 1 111 ? 11.132  -9.886  12.194  1.00 10.15 ? 111 HIS A N   1 
ATOM   912   C  CA  . HIS A 1 111 ? 12.278  -9.298  12.818  1.00 10.40 ? 111 HIS A CA  1 
ATOM   913   C  C   . HIS A 1 111 ? 13.067  -10.334 13.546  1.00 12.38 ? 111 HIS A C   1 
ATOM   914   O  O   . HIS A 1 111 ? 12.537  -11.401 13.969  1.00 14.24 ? 111 HIS A O   1 
ATOM   915   C  CB  . HIS A 1 111 ? 11.896  -8.358  13.941  1.00 11.20 ? 111 HIS A CB  1 
ATOM   916   C  CG  . HIS A 1 111 ? 11.483  -7.025  13.498  1.00 9.75  ? 111 HIS A CG  1 
ATOM   917   N  ND1 . HIS A 1 111 ? 10.232  -6.712  12.968  1.00 16.55 ? 111 HIS A ND1 1 
ATOM   918   C  CD2 . HIS A 1 111 ? 12.264  -5.946  13.289  1.00 9.75  ? 111 HIS A CD2 1 
ATOM   919   C  CE1 . HIS A 1 111 ? 10.209  -5.417  12.643  1.00 12.68 ? 111 HIS A CE1 1 
ATOM   920   N  NE2 . HIS A 1 111 ? 11.473  -4.945  12.789  1.00 14.37 ? 111 HIS A NE2 1 
ATOM   921   N  N   . PHE A 1 112 ? 14.357  -10.121 13.603  1.00 9.86  ? 112 PHE A N   1 
ATOM   922   C  CA  . PHE A 1 112 ? 15.244  -10.819 14.530  1.00 8.83  ? 112 PHE A CA  1 
ATOM   923   C  C   . PHE A 1 112 ? 15.303  -10.044 15.858  1.00 7.92  ? 112 PHE A C   1 
ATOM   924   O  O   . PHE A 1 112 ? 14.787  -8.861  15.914  1.00 8.32  ? 112 PHE A O   1 
ATOM   925   C  CB  . PHE A 1 112 ? 16.618  -11.064 13.908  1.00 8.37  ? 112 PHE A CB  1 
ATOM   926   C  CG  . PHE A 1 112 ? 16.574  -12.126 12.853  1.00 11.34 ? 112 PHE A CG  1 
ATOM   927   C  CD1 . PHE A 1 112 ? 17.071  -13.418 13.134  1.00 12.26 ? 112 PHE A CD1 1 
ATOM   928   C  CD2 . PHE A 1 112 ? 16.015  -11.872 11.554  1.00 11.40 ? 112 PHE A CD2 1 
ATOM   929   C  CE1 . PHE A 1 112 ? 16.991  -14.480 12.246  1.00 11.23 ? 112 PHE A CE1 1 
ATOM   930   C  CE2 . PHE A 1 112 ? 15.961  -12.976 10.627  1.00 16.74 ? 112 PHE A CE2 1 
ATOM   931   C  CZ  . PHE A 1 112 ? 16.476  -14.245 11.028  1.00 13.91 ? 112 PHE A CZ  1 
ATOM   932   N  N   . ALA A 1 113 ? 15.955  -10.591 16.889  1.00 7.17  ? 113 ALA A N   1 
ATOM   933   C  CA  . ALA A 1 113 ? 15.972  -9.918  18.149  1.00 8.05  ? 113 ALA A CA  1 
ATOM   934   C  C   . ALA A 1 113 ? 16.716  -8.611  18.098  1.00 6.74  ? 113 ALA A C   1 
ATOM   935   O  O   . ALA A 1 113 ? 16.377  -7.619  18.756  1.00 8.21  ? 113 ALA A O   1 
ATOM   936   C  CB  . ALA A 1 113 ? 16.608  -10.861 19.229  1.00 10.01 ? 113 ALA A CB  1 
ATOM   937   N  N   . ALA A 1 114 ? 17.796  -8.602  17.331  1.00 6.71  ? 114 ALA A N   1 
ATOM   938   C  CA  . ALA A 1 114 ? 18.696  -7.403  17.284  1.00 5.96  ? 114 ALA A CA  1 
ATOM   939   C  C   . ALA A 1 114 ? 19.502  -7.495  16.014  1.00 5.81  ? 114 ALA A C   1 
ATOM   940   O  O   . ALA A 1 114 ? 19.445  -8.476  15.271  1.00 6.97  ? 114 ALA A O   1 
ATOM   941   C  CB  . ALA A 1 114 ? 19.597  -7.361  18.533  1.00 8.77  ? 114 ALA A CB  1 
ATOM   942   N  N   . GLU A 1 115 ? 20.284  -6.419  15.793  1.00 7.04  ? 115 GLU A N   1 
ATOM   943   C  CA  . GLU A 1 115 ? 21.141  -6.436  14.583  1.00 7.00  ? 115 GLU A CA  1 
ATOM   944   C  C   . GLU A 1 115 ? 22.423  -5.643  14.875  1.00 7.79  ? 115 GLU A C   1 
ATOM   945   O  O   . GLU A 1 115 ? 22.348  -4.519  15.515  1.00 8.70  ? 115 GLU A O   1 
ATOM   946   C  CB  . GLU A 1 115 ? 20.267  -5.823  13.430  1.00 7.70  ? 115 GLU A CB  1 
ATOM   947   C  CG  . GLU A 1 115 ? 20.954  -5.774  12.044  1.00 7.30  ? 115 GLU A CG  1 
ATOM   948   C  CD  . GLU A 1 115 ? 20.006  -5.403  10.901  1.00 8.21  ? 115 GLU A CD  1 
ATOM   949   O  OE1 . GLU A 1 115 ? 18.801  -5.672  11.066  1.00 8.05  ? 115 GLU A OE1 1 
ATOM   950   O  OE2 . GLU A 1 115 ? 20.496  -4.918  9.859   1.00 7.24  ? 115 GLU A OE2 1 
ATOM   951   N  N   . LEU A 1 116 ? 23.561  -6.179  14.414  1.00 6.17  ? 116 LEU A N   1 
ATOM   952   C  CA  . LEU A 1 116 ? 24.882  -5.520  14.524  1.00 6.11  ? 116 LEU A CA  1 
ATOM   953   C  C   . LEU A 1 116 ? 25.227  -4.964  13.140  1.00 5.51  ? 116 LEU A C   1 
ATOM   954   O  O   . LEU A 1 116 ? 25.028  -5.604  12.104  1.00 5.78  ? 116 LEU A O   1 
ATOM   955   C  CB  . LEU A 1 116 ? 25.945  -6.579  14.931  1.00 7.85  ? 116 LEU A CB  1 
ATOM   956   C  CG  . LEU A 1 116 ? 27.435  -6.113  14.777  1.00 8.22  ? 116 LEU A CG  1 
ATOM   957   C  CD1 . LEU A 1 116 ? 27.741  -5.302  15.923  1.00 11.86 ? 116 LEU A CD1 1 
ATOM   958   C  CD2 . LEU A 1 116 ? 28.345  -7.310  14.691  1.00 8.76  ? 116 LEU A CD2 1 
ATOM   959   N  N   . HIS A 1 117 ? 25.713  -3.692  13.148  1.00 5.57  ? 117 HIS A N   1 
ATOM   960   C  CA  . HIS A 1 117 ? 26.272  -3.092  11.940  1.00 5.81  ? 117 HIS A CA  1 
ATOM   961   C  C   . HIS A 1 117 ? 27.733  -2.735  12.092  1.00 5.82  ? 117 HIS A C   1 
ATOM   962   O  O   . HIS A 1 117 ? 28.083  -2.067  13.078  1.00 7.20  ? 117 HIS A O   1 
ATOM   963   C  CB  . HIS A 1 117 ? 25.503  -1.818  11.685  1.00 6.68  ? 117 HIS A CB  1 
ATOM   964   C  CG  . HIS A 1 117 ? 24.067  -2.029  11.299  1.00 6.47  ? 117 HIS A CG  1 
ATOM   965   N  ND1 . HIS A 1 117 ? 23.035  -1.083  11.472  1.00 7.27  ? 117 HIS A ND1 1 
ATOM   966   C  CD2 . HIS A 1 117 ? 23.513  -3.096  10.745  1.00 6.53  ? 117 HIS A CD2 1 
ATOM   967   C  CE1 . HIS A 1 117 ? 21.905  -1.594  10.983  1.00 7.17  ? 117 HIS A CE1 1 
ATOM   968   N  NE2 . HIS A 1 117 ? 22.137  -2.851  10.579  1.00 6.40  ? 117 HIS A NE2 1 
ATOM   969   N  N   . ILE A 1 118 ? 28.501  -3.198  11.121  1.00 6.78  ? 118 ILE A N   1 
ATOM   970   C  CA  . ILE A 1 118 ? 29.942  -2.856  11.104  1.00 6.22  ? 118 ILE A CA  1 
ATOM   971   C  C   . ILE A 1 118 ? 30.109  -1.924  9.918   1.00 8.49  ? 118 ILE A C   1 
ATOM   972   O  O   . ILE A 1 118 ? 29.929  -2.330  8.744   1.00 7.33  ? 118 ILE A O   1 
ATOM   973   C  CB  . ILE A 1 118 ? 30.856  -4.058  10.951  1.00 8.63  ? 118 ILE A CB  1 
ATOM   974   C  CG1 . ILE A 1 118 ? 30.560  -5.095  12.011  1.00 7.80  ? 118 ILE A CG1 1 
ATOM   975   C  CG2 . ILE A 1 118 ? 32.315  -3.571  11.171  1.00 10.43 ? 118 ILE A CG2 1 
ATOM   976   C  CD1 . ILE A 1 118 ? 31.325  -6.367  11.781  1.00 10.43 ? 118 ILE A CD1 1 
ATOM   977   N  N   . VAL A 1 119 ? 30.261  -0.641  10.249  1.00 7.68  ? 119 VAL A N   1 
ATOM   978   C  CA  . VAL A 1 119 ? 30.247  0.457   9.234   1.00 8.38  ? 119 VAL A CA  1 
ATOM   979   C  C   . VAL A 1 119 ? 31.642  0.624   8.669   1.00 7.63  ? 119 VAL A C   1 
ATOM   980   O  O   . VAL A 1 119 ? 32.592  0.783   9.476   1.00 9.74  ? 119 VAL A O   1 
ATOM   981   C  CB  . VAL A 1 119 ? 29.788  1.769   9.864   1.00 8.25  ? 119 VAL A CB  1 
ATOM   982   C  CG1 . VAL A 1 119 ? 29.705  2.892   8.797   1.00 10.88 ? 119 VAL A CG1 1 
ATOM   983   C  CG2 . VAL A 1 119 ? 28.371  1.633   10.551  1.00 7.95  ? 119 VAL A CG2 1 
ATOM   984   N  N   . HIS A 1 120 ? 31.738  0.652   7.373   1.00 8.84  ? 120 HIS A N   1 
ATOM   985   C  CA  . HIS A 1 120 ? 33.049  0.892   6.648   1.00 8.02  ? 120 HIS A CA  1 
ATOM   986   C  C   . HIS A 1 120 ? 32.844  2.054   5.647   1.00 9.59  ? 120 HIS A C   1 
ATOM   987   O  O   . HIS A 1 120 ? 31.713  2.380   5.228   1.00 9.15  ? 120 HIS A O   1 
ATOM   988   C  CB  . HIS A 1 120 ? 33.461  -0.319  5.816   1.00 8.76  ? 120 HIS A CB  1 
ATOM   989   C  CG  . HIS A 1 120 ? 33.647  -1.591  6.614   1.00 10.61 ? 120 HIS A CG  1 
ATOM   990   N  ND1 . HIS A 1 120 ? 32.601  -2.273  7.273   1.00 8.57  ? 120 HIS A ND1 1 
ATOM   991   C  CD2 . HIS A 1 120 ? 34.767  -2.343  6.865   1.00 9.67  ? 120 HIS A CD2 1 
ATOM   992   C  CE1 . HIS A 1 120 ? 33.067  -3.416  7.810   1.00 7.87  ? 120 HIS A CE1 1 
ATOM   993   N  NE2 . HIS A 1 120 ? 34.398  -3.503  7.585   1.00 9.36  ? 120 HIS A NE2 1 
ATOM   994   N  N   . TYR A 1 121 ? 33.946  2.709   5.275   1.00 10.43 ? 121 TYR A N   1 
ATOM   995   C  CA  . TYR A 1 121 ? 33.882  3.830   4.299   1.00 10.71 ? 121 TYR A CA  1 
ATOM   996   C  C   . TYR A 1 121 ? 34.859  3.623   3.169   1.00 12.26 ? 121 TYR A C   1 
ATOM   997   O  O   . TYR A 1 121 ? 35.892  2.920   3.401   1.00 11.37 ? 121 TYR A O   1 
ATOM   998   C  CB  . TYR A 1 121 ? 34.109  5.190   4.953   1.00 12.96 ? 121 TYR A CB  1 
ATOM   999   C  CG  . TYR A 1 121 ? 35.548  5.383   5.488   1.00 13.67 ? 121 TYR A CG  1 
ATOM   1000  C  CD1 . TYR A 1 121 ? 36.507  6.090   4.728   1.00 14.03 ? 121 TYR A CD1 1 
ATOM   1001  C  CD2 . TYR A 1 121 ? 35.933  4.901   6.740   1.00 13.65 ? 121 TYR A CD2 1 
ATOM   1002  C  CE1 . TYR A 1 121 ? 37.847  6.219   5.206   1.00 16.09 ? 121 TYR A CE1 1 
ATOM   1003  C  CE2 . TYR A 1 121 ? 37.253  5.009   7.201   1.00 15.77 ? 121 TYR A CE2 1 
ATOM   1004  C  CZ  . TYR A 1 121 ? 38.172  5.679   6.413   1.00 16.35 ? 121 TYR A CZ  1 
ATOM   1005  O  OH  . TYR A 1 121 ? 39.482  5.832   6.882   1.00 16.82 ? 121 TYR A OH  1 
ATOM   1006  N  N   . ASN A 1 122 ? 34.617  4.218   1.993   1.00 11.76 ? 122 ASN A N   1 
ATOM   1007  C  CA  . ASN A 1 122 ? 35.516  4.034   0.833   1.00 13.15 ? 122 ASN A CA  1 
ATOM   1008  C  C   . ASN A 1 122 ? 36.785  4.877   1.042   1.00 13.48 ? 122 ASN A C   1 
ATOM   1009  O  O   . ASN A 1 122 ? 36.797  6.079   0.908   1.00 13.55 ? 122 ASN A O   1 
ATOM   1010  C  CB  . ASN A 1 122 ? 34.773  4.506   -0.428  1.00 12.26 ? 122 ASN A CB  1 
ATOM   1011  C  CG  . ASN A 1 122 ? 35.526  4.260   -1.616  1.00 14.09 ? 122 ASN A CG  1 
ATOM   1012  O  OD1 . ASN A 1 122 ? 36.780  4.192   -1.610  1.00 15.64 ? 122 ASN A OD1 1 
ATOM   1013  N  ND2 . ASN A 1 122 ? 34.822  3.960   -2.717  1.00 19.89 ? 122 ASN A ND2 1 
ATOM   1014  N  N   . SER A 1 123 ? 37.825  4.168   1.522   1.00 11.10 ? 123 SER A N   1 
ATOM   1015  C  CA  . SER A 1 123 ? 39.046  4.852   1.851   1.00 12.77 ? 123 SER A CA  1 
ATOM   1016  C  C   . SER A 1 123 ? 39.878  5.058   0.605   1.00 13.94 ? 123 SER A C   1 
ATOM   1017  O  O   . SER A 1 123 ? 40.894  5.804   0.714   1.00 15.73 ? 123 SER A O   1 
ATOM   1018  C  CB  . SER A 1 123 ? 39.835  3.982   2.928   1.00 10.27 ? 123 SER A CB  1 
ATOM   1019  O  OG  . SER A 1 123 ? 39.871  2.670   2.595   1.00 13.08 ? 123 SER A OG  1 
ATOM   1020  N  N   . ASP A 1 124 ? 39.559  4.447   -0.513  1.00 13.46 ? 124 ASP A N   1 
ATOM   1021  C  CA  . ASP A 1 124 ? 40.341  4.679   -1.759  1.00 14.40 ? 124 ASP A CA  1 
ATOM   1022  C  C   . ASP A 1 124 ? 39.937  6.083   -2.190  1.00 19.76 ? 124 ASP A C   1 
ATOM   1023  O  O   . ASP A 1 124 ? 40.751  6.820   -2.769  1.00 20.19 ? 124 ASP A O   1 
ATOM   1024  C  CB  . ASP A 1 124 ? 39.942  3.685   -2.775  1.00 16.52 ? 124 ASP A CB  1 
ATOM   1025  C  CG  . ASP A 1 124 ? 40.583  2.317   -2.550  1.00 13.20 ? 124 ASP A CG  1 
ATOM   1026  O  OD1 . ASP A 1 124 ? 41.576  2.234   -1.795  1.00 15.06 ? 124 ASP A OD1 1 
ATOM   1027  O  OD2 . ASP A 1 124 ? 40.095  1.322   -3.132  1.00 15.83 ? 124 ASP A OD2 1 
ATOM   1028  N  N   . LEU A 1 125 ? 38.690  6.440   -1.988  1.00 17.51 ? 125 LEU A N   1 
ATOM   1029  C  CA  . LEU A 1 125 ? 38.160  7.777   -2.470  1.00 18.61 ? 125 LEU A CA  1 
ATOM   1030  C  C   . LEU A 1 125 ? 38.205  8.878   -1.473  1.00 18.24 ? 125 LEU A C   1 
ATOM   1031  O  O   . LEU A 1 125 ? 38.337  10.109  -1.837  1.00 22.17 ? 125 LEU A O   1 
ATOM   1032  C  CB  . LEU A 1 125 ? 36.735  7.594   -3.193  1.00 20.55 ? 125 LEU A CB  1 
ATOM   1033  C  CG  . LEU A 1 125 ? 36.586  6.580   -4.304  1.00 21.75 ? 125 LEU A CG  1 
ATOM   1034  C  CD1 . LEU A 1 125 ? 35.171  6.620   -5.034  1.00 22.83 ? 125 LEU A CD1 1 
ATOM   1035  C  CD2 . LEU A 1 125 ? 37.737  6.744   -5.353  1.00 25.66 ? 125 LEU A CD2 1 
ATOM   1036  N  N   . TYR A 1 126 ? 37.974  8.585   -0.168  1.00 17.00 ? 126 TYR A N   1 
ATOM   1037  C  CA  . TYR A 1 126 ? 37.712  9.574   0.873   1.00 17.10 ? 126 TYR A CA  1 
ATOM   1038  C  C   . TYR A 1 126 ? 38.600  9.417   2.175   1.00 17.80 ? 126 TYR A C   1 
ATOM   1039  O  O   . TYR A 1 126 ? 39.008  8.303   2.508   1.00 18.03 ? 126 TYR A O   1 
ATOM   1040  C  CB  . TYR A 1 126 ? 36.191  9.528   1.339   1.00 18.61 ? 126 TYR A CB  1 
ATOM   1041  C  CG  . TYR A 1 126 ? 35.264  9.592   0.132   1.00 19.13 ? 126 TYR A CG  1 
ATOM   1042  C  CD1 . TYR A 1 126 ? 35.162  10.777  -0.633  1.00 22.67 ? 126 TYR A CD1 1 
ATOM   1043  C  CD2 . TYR A 1 126 ? 34.446  8.486   -0.219  1.00 20.18 ? 126 TYR A CD2 1 
ATOM   1044  C  CE1 . TYR A 1 126 ? 34.380  10.799  -1.746  1.00 21.91 ? 126 TYR A CE1 1 
ATOM   1045  C  CE2 . TYR A 1 126 ? 33.630  8.497   -1.371  1.00 21.77 ? 126 TYR A CE2 1 
ATOM   1046  C  CZ  . TYR A 1 126 ? 33.586  9.665   -2.099  1.00 23.37 ? 126 TYR A CZ  1 
ATOM   1047  O  OH  . TYR A 1 126 ? 32.732  9.699   -3.184  1.00 24.66 ? 126 TYR A OH  1 
ATOM   1048  N  N   . PRO A 1 127 ? 38.882  10.497  2.851   1.00 18.59 ? 127 PRO A N   1 
ATOM   1049  C  CA  . PRO A 1 127 ? 39.836  10.371  3.966   1.00 20.11 ? 127 PRO A CA  1 
ATOM   1050  C  C   . PRO A 1 127 ? 39.248  9.852   5.268   1.00 21.31 ? 127 PRO A C   1 
ATOM   1051  O  O   . PRO A 1 127 ? 40.014  9.383   6.182   1.00 22.76 ? 127 PRO A O   1 
ATOM   1052  C  CB  . PRO A 1 127 ? 40.349  11.824  4.133   1.00 20.49 ? 127 PRO A CB  1 
ATOM   1053  C  CG  . PRO A 1 127 ? 39.202  12.709  3.562   1.00 21.94 ? 127 PRO A CG  1 
ATOM   1054  C  CD  . PRO A 1 127 ? 38.471  11.917  2.620   1.00 18.09 ? 127 PRO A CD  1 
ATOM   1055  N  N   . ASP A 1 128 ? 37.905  9.889   5.400   1.00 18.71 ? 128 ASP A N   1 
ATOM   1056  C  CA  . ASP A 1 128 ? 37.311  9.451   6.669   1.00 18.86 ? 128 ASP A CA  1 
ATOM   1057  C  C   . ASP A 1 128 ? 35.829  9.197   6.421   1.00 16.75 ? 128 ASP A C   1 
ATOM   1058  O  O   . ASP A 1 128 ? 35.334  9.528   5.332   1.00 15.97 ? 128 ASP A O   1 
ATOM   1059  C  CB  . ASP A 1 128 ? 37.490  10.457  7.818   1.00 19.07 ? 128 ASP A CB  1 
ATOM   1060  C  CG  . ASP A 1 128 ? 37.163  11.873  7.434   1.00 25.15 ? 128 ASP A CG  1 
ATOM   1061  O  OD1 . ASP A 1 128 ? 37.992  12.772  7.803   1.00 31.71 ? 128 ASP A OD1 1 
ATOM   1062  O  OD2 . ASP A 1 128 ? 36.115  12.087  6.791   1.00 21.77 ? 128 ASP A OD2 1 
ATOM   1063  N  N   . ALA A 1 129 ? 35.147  8.604   7.416   1.00 18.18 ? 129 ALA A N   1 
ATOM   1064  C  CA  . ALA A 1 129 ? 33.813  8.149   7.132   1.00 16.66 ? 129 ALA A CA  1 
ATOM   1065  C  C   . ALA A 1 129 ? 32.852  9.349   7.088   1.00 17.34 ? 129 ALA A C   1 
ATOM   1066  O  O   . ALA A 1 129 ? 31.862  9.266   6.340   1.00 17.08 ? 129 ALA A O   1 
ATOM   1067  C  CB  . ALA A 1 129 ? 33.360  7.187   8.246   1.00 19.42 ? 129 ALA A CB  1 
ATOM   1068  N  N   . SER A 1 130 ? 33.153  10.418  7.838   1.00 19.16 ? 130 SER A N   1 
ATOM   1069  C  CA  . SER A 1 130 ? 32.291  11.595  7.877   1.00 20.67 ? 130 SER A CA  1 
ATOM   1070  C  C   . SER A 1 130 ? 32.238  12.168  6.486   1.00 19.21 ? 130 SER A C   1 
ATOM   1071  O  O   . SER A 1 130 ? 31.156  12.454  5.998   1.00 20.45 ? 130 SER A O   1 
ATOM   1072  C  CB  . SER A 1 130 ? 32.908  12.615  8.894   1.00 21.61 ? 130 SER A CB  1 
ATOM   1073  O  OG  . SER A 1 130 ? 32.126  13.808  8.901   1.00 28.82 ? 130 SER A OG  1 
ATOM   1074  N  N   . THR A 1 131 ? 33.381  12.307  5.805   1.00 17.71 ? 131 THR A N   1 
ATOM   1075  C  CA  . THR A 1 131 ? 33.458  12.940  4.531   1.00 17.46 ? 131 THR A CA  1 
ATOM   1076  C  C   . THR A 1 131 ? 32.832  12.000  3.531   1.00 15.44 ? 131 THR A C   1 
ATOM   1077  O  O   . THR A 1 131 ? 32.138  12.402  2.592   1.00 16.63 ? 131 THR A O   1 
ATOM   1078  C  CB  . THR A 1 131 ? 34.929  13.144  4.159   1.00 20.60 ? 131 THR A CB  1 
ATOM   1079  O  OG1 . THR A 1 131 ? 35.496  14.055  5.157   1.00 22.16 ? 131 THR A OG1 1 
ATOM   1080  C  CG2 . THR A 1 131 ? 35.086  13.607  2.628   1.00 20.57 ? 131 THR A CG2 1 
ATOM   1081  N  N   . ALA A 1 132 ? 33.068  10.687  3.671   1.00 16.64 ? 132 ALA A N   1 
ATOM   1082  C  CA  . ALA A 1 132 ? 32.456  9.748   2.708   1.00 14.45 ? 132 ALA A CA  1 
ATOM   1083  C  C   . ALA A 1 132 ? 30.885  9.618   2.786   1.00 11.92 ? 132 ALA A C   1 
ATOM   1084  O  O   . ALA A 1 132 ? 30.289  9.219   1.771   1.00 12.97 ? 132 ALA A O   1 
ATOM   1085  C  CB  . ALA A 1 132 ? 32.983  8.329   2.876   1.00 13.55 ? 132 ALA A CB  1 
ATOM   1086  N  N   . SER A 1 133 ? 30.360  9.924   3.957   1.00 13.55 ? 133 SER A N   1 
ATOM   1087  C  CA  . SER A 1 133 ? 28.931  9.548   4.267   1.00 16.26 ? 133 SER A CA  1 
ATOM   1088  C  C   . SER A 1 133 ? 27.886  10.108  3.283   1.00 18.19 ? 133 SER A C   1 
ATOM   1089  O  O   . SER A 1 133 ? 26.774  9.521   3.056   1.00 17.01 ? 133 SER A O   1 
ATOM   1090  C  CB  . SER A 1 133 ? 28.587  9.790   5.698   1.00 17.75 ? 133 SER A CB  1 
ATOM   1091  O  OG  . SER A 1 133 ? 28.532  11.213  5.960   1.00 17.89 ? 133 SER A OG  1 
ATOM   1092  N  N   . ASN A 1 134 ? 28.189  11.283  2.737   1.00 17.19 ? 134 ASN A N   1 
ATOM   1093  C  CA  . ASN A 1 134 ? 27.268  11.917  1.780   1.00 19.04 ? 134 ASN A CA  1 
ATOM   1094  C  C   . ASN A 1 134 ? 27.746  11.889  0.363   1.00 18.00 ? 134 ASN A C   1 
ATOM   1095  O  O   . ASN A 1 134 ? 27.280  12.621  -0.512  1.00 21.45 ? 134 ASN A O   1 
ATOM   1096  C  CB  . ASN A 1 134 ? 26.816  13.321  2.269   1.00 17.61 ? 134 ASN A CB  1 
ATOM   1097  C  CG  . ASN A 1 134 ? 27.975  14.310  2.331   1.00 24.36 ? 134 ASN A CG  1 
ATOM   1098  O  OD1 . ASN A 1 134 ? 29.181  13.886  2.286   1.00 22.22 ? 134 ASN A OD1 1 
ATOM   1099  N  ND2 . ASN A 1 134 ? 27.649  15.632  2.364   1.00 24.21 ? 134 ASN A ND2 1 
ATOM   1100  N  N   . LYS A 1 135 ? 28.601  10.966  -0.001  1.00 16.92 ? 135 LYS A N   1 
ATOM   1101  C  CA  . LYS A 1 135 ? 29.196  10.862  -1.301  1.00 19.88 ? 135 LYS A CA  1 
ATOM   1102  C  C   . LYS A 1 135 ? 28.967  9.564   -1.970  1.00 19.26 ? 135 LYS A C   1 
ATOM   1103  O  O   . LYS A 1 135 ? 28.738  8.524   -1.334  1.00 16.28 ? 135 LYS A O   1 
ATOM   1104  C  CB  . LYS A 1 135 ? 30.745  11.254  -1.212  1.00 19.31 ? 135 LYS A CB  1 
ATOM   1105  C  CG  . LYS A 1 135 ? 30.845  12.804  -1.027  1.00 23.83 ? 135 LYS A CG  1 
ATOM   1106  C  CD  . LYS A 1 135 ? 32.263  13.398  -0.832  1.00 22.32 ? 135 LYS A CD  1 
ATOM   1107  C  CE  . LYS A 1 135 ? 32.156  14.702  -0.122  1.00 26.60 ? 135 LYS A CE  1 
ATOM   1108  N  NZ  . LYS A 1 135 ? 31.706  14.756  1.257   1.00 24.82 ? 135 LYS A NZ  1 
ATOM   1109  N  N   . SER A 1 136 ? 29.093  9.554   -3.276  1.00 19.14 ? 136 SER A N   1 
ATOM   1110  C  CA  . SER A 1 136 ? 28.803  8.434   -4.130  1.00 21.54 ? 136 SER A CA  1 
ATOM   1111  C  C   . SER A 1 136 ? 29.698  7.268   -3.642  1.00 19.42 ? 136 SER A C   1 
ATOM   1112  O  O   . SER A 1 136 ? 30.911  7.403   -3.462  1.00 21.54 ? 136 SER A O   1 
ATOM   1113  C  CB  . SER A 1 136 ? 29.195  8.784   -5.598  1.00 21.66 ? 136 SER A CB  1 
ATOM   1114  O  OG  . SER A 1 136 ? 28.861  7.701   -6.396  1.00 28.63 ? 136 SER A OG  1 
ATOM   1115  N  N   . GLU A 1 137 ? 29.094  6.100   -3.516  1.00 21.14 ? 137 GLU A N   1 
ATOM   1116  C  CA  . GLU A 1 137 ? 29.926  4.904   -3.161  1.00 19.73 ? 137 GLU A CA  1 
ATOM   1117  C  C   . GLU A 1 137 ? 30.582  5.086   -1.817  1.00 18.09 ? 137 GLU A C   1 
ATOM   1118  O  O   . GLU A 1 137 ? 31.619  4.409   -1.559  1.00 17.11 ? 137 GLU A O   1 
ATOM   1119  C  CB  . GLU A 1 137 ? 31.041  4.549   -4.177  1.00 23.18 ? 137 GLU A CB  1 
ATOM   1120  C  CG  . GLU A 1 137 ? 30.576  4.488   -5.633  1.00 30.13 ? 137 GLU A CG  1 
ATOM   1121  C  CD  . GLU A 1 137 ? 29.677  3.293   -5.950  1.00 41.34 ? 137 GLU A CD  1 
ATOM   1122  O  OE1 . GLU A 1 137 ? 29.067  2.699   -5.008  1.00 46.66 ? 137 GLU A OE1 1 
ATOM   1123  O  OE2 . GLU A 1 137 ? 29.579  2.937   -7.169  1.00 44.55 ? 137 GLU A OE2 1 
ATOM   1124  N  N   . GLY A 1 138 ? 29.997  5.864   -0.925  1.00 12.77 ? 138 GLY A N   1 
ATOM   1125  C  CA  . GLY A 1 138 ? 30.734  6.296   0.233   1.00 13.89 ? 138 GLY A CA  1 
ATOM   1126  C  C   . GLY A 1 138 ? 30.903  5.204   1.274   1.00 14.02 ? 138 GLY A C   1 
ATOM   1127  O  O   . GLY A 1 138 ? 31.943  5.134   1.948   1.00 13.14 ? 138 GLY A O   1 
ATOM   1128  N  N   . LEU A 1 139 ? 29.857  4.384   1.517   1.00 11.38 ? 139 LEU A N   1 
ATOM   1129  C  CA  . LEU A 1 139 ? 29.846  3.542   2.739   1.00 9.85  ? 139 LEU A CA  1 
ATOM   1130  C  C   . LEU A 1 139 ? 29.527  2.083   2.370   1.00 10.11 ? 139 LEU A C   1 
ATOM   1131  O  O   . LEU A 1 139 ? 28.822  1.849   1.341   1.00 10.39 ? 139 LEU A O   1 
ATOM   1132  C  CB  . LEU A 1 139 ? 28.872  4.018   3.837   1.00 10.12 ? 139 LEU A CB  1 
ATOM   1133  C  CG  . LEU A 1 139 ? 29.047  5.459   4.261   1.00 10.20 ? 139 LEU A CG  1 
ATOM   1134  C  CD1 . LEU A 1 139 ? 27.793  5.967   5.115   1.00 13.06 ? 139 LEU A CD1 1 
ATOM   1135  C  CD2 . LEU A 1 139 ? 30.367  5.614   5.090   1.00 14.44 ? 139 LEU A CD2 1 
ATOM   1136  N  N   . ALA A 1 140 ? 29.927  1.141   3.242   1.00 9.14  ? 140 ALA A N   1 
ATOM   1137  C  CA  . ALA A 1 140 ? 29.556  -0.261  3.090   1.00 8.29  ? 140 ALA A CA  1 
ATOM   1138  C  C   . ALA A 1 140 ? 29.337  -0.750  4.512   1.00 8.14  ? 140 ALA A C   1 
ATOM   1139  O  O   . ALA A 1 140 ? 30.206  -0.566  5.377   1.00 9.31  ? 140 ALA A O   1 
ATOM   1140  C  CB  . ALA A 1 140 ? 30.586  -1.036  2.423   1.00 8.74  ? 140 ALA A CB  1 
ATOM   1141  N  N   . VAL A 1 141 ? 28.194  -1.363  4.794   1.00 8.33  ? 141 VAL A N   1 
ATOM   1142  C  CA  . VAL A 1 141 ? 27.935  -1.900  6.115   1.00 8.06  ? 141 VAL A CA  1 
ATOM   1143  C  C   . VAL A 1 141 ? 27.748  -3.400  6.051   1.00 6.93  ? 141 VAL A C   1 
ATOM   1144  O  O   . VAL A 1 141 ? 27.171  -3.981  5.077   1.00 7.71  ? 141 VAL A O   1 
ATOM   1145  C  CB  . VAL A 1 141 ? 26.643  -1.316  6.681   1.00 7.22  ? 141 VAL A CB  1 
ATOM   1146  C  CG1 . VAL A 1 141 ? 26.253  -1.900  8.035   1.00 9.24  ? 141 VAL A CG1 1 
ATOM   1147  C  CG2 . VAL A 1 141 ? 26.768  0.175   6.812   1.00 9.31  ? 141 VAL A CG2 1 
ATOM   1148  N  N   . LEU A 1 142 ? 28.340  -4.087  7.049   1.00 6.76  ? 142 LEU A N   1 
ATOM   1149  C  CA  . LEU A 1 142 ? 28.046  -5.563  7.183   1.00 7.48  ? 142 LEU A CA  1 
ATOM   1150  C  C   . LEU A 1 142 ? 26.982  -5.559  8.300   1.00 7.79  ? 142 LEU A C   1 
ATOM   1151  O  O   . LEU A 1 142 ? 27.208  -5.007  9.408   1.00 8.84  ? 142 LEU A O   1 
ATOM   1152  C  CB  . LEU A 1 142 ? 29.296  -6.307  7.674   1.00 6.63  ? 142 LEU A CB  1 
ATOM   1153  C  CG  . LEU A 1 142 ? 30.508  -6.167  6.700   1.00 8.14  ? 142 LEU A CG  1 
ATOM   1154  C  CD1 . LEU A 1 142 ? 31.684  -7.034  7.341   1.00 11.31 ? 142 LEU A CD1 1 
ATOM   1155  C  CD2 . LEU A 1 142 ? 30.188  -6.659  5.360   1.00 7.76  ? 142 LEU A CD2 1 
ATOM   1156  N  N   . ALA A 1 143 ? 25.898  -6.318  8.021   1.00 6.67  ? 143 ALA A N   1 
ATOM   1157  C  CA  . ALA A 1 143 ? 24.839  -6.478  9.049   1.00 6.91  ? 143 ALA A CA  1 
ATOM   1158  C  C   . ALA A 1 143 ? 24.719  -7.988  9.403   1.00 5.57  ? 143 ALA A C   1 
ATOM   1159  O  O   . ALA A 1 143 ? 24.683  -8.839  8.524   1.00 7.62  ? 143 ALA A O   1 
ATOM   1160  C  CB  . ALA A 1 143 ? 23.509  -5.948  8.438   1.00 8.12  ? 143 ALA A CB  1 
ATOM   1161  N  N   . VAL A 1 144 ? 24.741  -8.148  10.765  1.00 5.69  ? 144 VAL A N   1 
ATOM   1162  C  CA  . VAL A 1 144 ? 24.540  -9.524  11.315  1.00 7.43  ? 144 VAL A CA  1 
ATOM   1163  C  C   . VAL A 1 144 ? 23.211  -9.494  12.083  1.00 7.67  ? 144 VAL A C   1 
ATOM   1164  O  O   . VAL A 1 144 ? 22.994  -8.661  12.986  1.00 7.19  ? 144 VAL A O   1 
ATOM   1165  C  CB  . VAL A 1 144 ? 25.675  -9.792  12.292  1.00 7.69  ? 144 VAL A CB  1 
ATOM   1166  C  CG1 . VAL A 1 144 ? 25.449  -11.252 12.843  1.00 10.92 ? 144 VAL A CG1 1 
ATOM   1167  C  CG2 . VAL A 1 144 ? 27.035  -9.727  11.607  1.00 8.11  ? 144 VAL A CG2 1 
ATOM   1168  N  N   . LEU A 1 145 ? 22.348  -10.448 11.727  1.00 7.62  ? 145 LEU A N   1 
ATOM   1169  C  CA  . LEU A 1 145 ? 21.088  -10.621 12.455  1.00 6.59  ? 145 LEU A CA  1 
ATOM   1170  C  C   . LEU A 1 145 ? 21.389  -11.412 13.718  1.00 6.96  ? 145 LEU A C   1 
ATOM   1171  O  O   . LEU A 1 145 ? 22.121  -12.412 13.648  1.00 8.72  ? 145 LEU A O   1 
ATOM   1172  C  CB  . LEU A 1 145 ? 20.098  -11.359 11.531  1.00 8.44  ? 145 LEU A CB  1 
ATOM   1173  C  CG  . LEU A 1 145 ? 19.832  -10.606 10.187  1.00 9.28  ? 145 LEU A CG  1 
ATOM   1174  C  CD1 . LEU A 1 145 ? 19.115  -11.535 9.208   1.00 11.92 ? 145 LEU A CD1 1 
ATOM   1175  C  CD2 . LEU A 1 145 ? 18.955  -9.345  10.485  1.00 10.68 ? 145 LEU A CD2 1 
ATOM   1176  N  N   . ILE A 1 146 ? 20.743  -11.078 14.798  1.00 6.15  ? 146 ILE A N   1 
ATOM   1177  C  CA  . ILE A 1 146 ? 20.973  -11.698 16.072  1.00 8.31  ? 146 ILE A CA  1 
ATOM   1178  C  C   . ILE A 1 146 ? 19.655  -12.244 16.621  1.00 10.04 ? 146 ILE A C   1 
ATOM   1179  O  O   . ILE A 1 146 ? 18.667  -11.606 16.642  1.00 8.63  ? 146 ILE A O   1 
ATOM   1180  C  CB  . ILE A 1 146 ? 21.462  -10.630 17.046  1.00 8.73  ? 146 ILE A CB  1 
ATOM   1181  C  CG1 . ILE A 1 146 ? 22.829  -10.063 16.598  1.00 8.16  ? 146 ILE A CG1 1 
ATOM   1182  C  CG2 . ILE A 1 146 ? 21.672  -11.183 18.514  1.00 11.55 ? 146 ILE A CG2 1 
ATOM   1183  C  CD1 . ILE A 1 146 ? 23.194  -8.740  17.358  1.00 8.86  ? 146 ILE A CD1 1 
ATOM   1184  N  N   . GLU A 1 147 ? 19.737  -13.520 17.054  1.00 9.33  ? 147 GLU A N   1 
ATOM   1185  C  CA  . GLU A 1 147 ? 18.573  -14.165 17.706  1.00 11.17 ? 147 GLU A CA  1 
ATOM   1186  C  C   . GLU A 1 147 ? 18.999  -14.746 19.051  1.00 8.96  ? 147 GLU A C   1 
ATOM   1187  O  O   . GLU A 1 147 ? 20.175  -14.847 19.405  1.00 10.08 ? 147 GLU A O   1 
ATOM   1188  C  CB  . GLU A 1 147 ? 18.011  -15.267 16.867  1.00 13.13 ? 147 GLU A CB  1 
ATOM   1189  C  CG  . GLU A 1 147 ? 18.990  -16.398 16.667  1.00 12.48 ? 147 GLU A CG  1 
ATOM   1190  C  CD  . GLU A 1 147 ? 18.495  -17.411 15.676  1.00 12.57 ? 147 GLU A CD  1 
ATOM   1191  O  OE1 . GLU A 1 147 ? 17.581  -17.246 14.840  1.00 14.76 ? 147 GLU A OE1 1 
ATOM   1192  O  OE2 . GLU A 1 147 ? 19.126  -18.534 15.638  1.00 19.92 ? 147 GLU A OE2 1 
ATOM   1193  N  N   . MET A 1 148 ? 17.998  -15.100 19.864  1.00 11.52 ? 148 MET A N   1 
ATOM   1194  C  CA  . MET A 1 148 ? 18.308  -15.601 21.200  1.00 13.05 ? 148 MET A CA  1 
ATOM   1195  C  C   . MET A 1 148 ? 18.627  -17.038 21.124  1.00 12.70 ? 148 MET A C   1 
ATOM   1196  O  O   . MET A 1 148 ? 17.929  -17.777 20.453  1.00 15.82 ? 148 MET A O   1 
ATOM   1197  C  CB  . MET A 1 148 ? 17.027  -15.450 22.023  1.00 15.73 ? 148 MET A CB  1 
ATOM   1198  C  CG  . MET A 1 148 ? 17.142  -14.535 23.211  1.00 25.62 ? 148 MET A CG  1 
ATOM   1199  S  SD  . MET A 1 148 ? 17.816  -15.598 24.506  1.00 37.13 ? 148 MET A SD  1 
ATOM   1200  C  CE  . MET A 1 148 ? 17.127  -17.167 23.973  1.00 3.58  ? 148 MET A CE  1 
ATOM   1201  N  N   . GLY A 1 149 ? 19.687  -17.475 21.819  1.00 12.71 ? 149 GLY A N   1 
ATOM   1202  C  CA  . GLY A 1 149 ? 19.990  -18.933 21.887  1.00 12.43 ? 149 GLY A CA  1 
ATOM   1203  C  C   . GLY A 1 149 ? 21.116  -19.100 22.896  1.00 12.62 ? 149 GLY A C   1 
ATOM   1204  O  O   . GLY A 1 149 ? 21.031  -18.663 24.027  1.00 12.72 ? 149 GLY A O   1 
ATOM   1205  N  N   A SER A 1 150 ? 22.202  -19.660 22.378  0.50 13.47 ? 150 SER A N   1 
ATOM   1206  N  N   B SER A 1 150 ? 22.166  -19.758 22.459  0.50 13.67 ? 150 SER A N   1 
ATOM   1207  C  CA  A SER A 1 150 ? 23.383  -19.863 23.184  0.50 13.39 ? 150 SER A CA  1 
ATOM   1208  C  CA  B SER A 1 150 ? 23.203  -20.073 23.413  0.50 12.91 ? 150 SER A CA  1 
ATOM   1209  C  C   A SER A 1 150 ? 24.078  -18.583 23.688  0.50 14.11 ? 150 SER A C   1 
ATOM   1210  C  C   B SER A 1 150 ? 24.087  -18.838 23.649  0.50 13.27 ? 150 SER A C   1 
ATOM   1211  O  O   A SER A 1 150 ? 24.234  -17.543 22.978  0.50 12.28 ? 150 SER A O   1 
ATOM   1212  O  O   B SER A 1 150 ? 24.303  -18.082 22.668  0.50 10.73 ? 150 SER A O   1 
ATOM   1213  C  CB  A SER A 1 150 ? 24.411  -20.754 22.418  0.50 14.20 ? 150 SER A CB  1 
ATOM   1214  C  CB  B SER A 1 150 ? 24.057  -21.202 22.842  0.50 15.47 ? 150 SER A CB  1 
ATOM   1215  O  OG  A SER A 1 150 ? 23.826  -22.022 22.112  0.50 17.93 ? 150 SER A OG  1 
ATOM   1216  O  OG  B SER A 1 150 ? 24.491  -20.849 21.509  0.50 16.99 ? 150 SER A OG  1 
ATOM   1217  N  N   . PHE A 1 151 ? 24.648  -18.663 24.887  1.00 13.16 ? 151 PHE A N   1 
ATOM   1218  C  CA  . PHE A 1 151 ? 25.575  -17.618 25.300  1.00 13.79 ? 151 PHE A CA  1 
ATOM   1219  C  C   . PHE A 1 151 ? 26.717  -17.475 24.242  1.00 13.50 ? 151 PHE A C   1 
ATOM   1220  O  O   . PHE A 1 151 ? 27.240  -18.541 23.688  1.00 17.12 ? 151 PHE A O   1 
ATOM   1221  C  CB  . PHE A 1 151 ? 26.179  -17.968 26.679  1.00 13.09 ? 151 PHE A CB  1 
ATOM   1222  C  CG  . PHE A 1 151 ? 27.159  -17.009 27.155  1.00 14.11 ? 151 PHE A CG  1 
ATOM   1223  C  CD1 . PHE A 1 151 ? 26.753  -15.755 27.679  1.00 12.35 ? 151 PHE A CD1 1 
ATOM   1224  C  CD2 . PHE A 1 151 ? 28.571  -17.265 27.088  1.00 12.85 ? 151 PHE A CD2 1 
ATOM   1225  C  CE1 . PHE A 1 151 ? 27.656  -14.798 28.064  1.00 13.73 ? 151 PHE A CE1 1 
ATOM   1226  C  CE2 . PHE A 1 151 ? 29.470  -16.346 27.521  1.00 14.98 ? 151 PHE A CE2 1 
ATOM   1227  C  CZ  . PHE A 1 151 ? 29.037  -15.097 27.983  1.00 14.71 ? 151 PHE A CZ  1 
ATOM   1228  N  N   . ASN A 1 152 ? 27.116  -16.237 23.993  1.00 12.18 ? 152 ASN A N   1 
ATOM   1229  C  CA  . ASN A 1 152 ? 28.122  -15.953 23.008  1.00 11.62 ? 152 ASN A CA  1 
ATOM   1230  C  C   . ASN A 1 152 ? 29.257  -15.181 23.618  1.00 12.03 ? 152 ASN A C   1 
ATOM   1231  O  O   . ASN A 1 152 ? 29.189  -13.982 23.901  1.00 14.07 ? 152 ASN A O   1 
ATOM   1232  C  CB  . ASN A 1 152 ? 27.438  -15.112 21.836  1.00 11.66 ? 152 ASN A CB  1 
ATOM   1233  C  CG  . ASN A 1 152 ? 28.338  -15.057 20.623  1.00 10.89 ? 152 ASN A CG  1 
ATOM   1234  O  OD1 . ASN A 1 152 ? 29.499  -14.630 20.744  1.00 13.44 ? 152 ASN A OD1 1 
ATOM   1235  N  ND2 . ASN A 1 152 ? 27.740  -15.203 19.505  1.00 12.29 ? 152 ASN A ND2 1 
ATOM   1236  N  N   . PRO A 1 153 ? 30.398  -15.882 23.918  1.00 13.49 ? 153 PRO A N   1 
ATOM   1237  C  CA  . PRO A 1 153 ? 31.534  -15.231 24.555  1.00 15.09 ? 153 PRO A CA  1 
ATOM   1238  C  C   . PRO A 1 153 ? 32.048  -14.028 23.761  1.00 15.09 ? 153 PRO A C   1 
ATOM   1239  O  O   . PRO A 1 153 ? 32.525  -13.047 24.340  1.00 15.11 ? 153 PRO A O   1 
ATOM   1240  C  CB  . PRO A 1 153 ? 32.560  -16.395 24.613  1.00 16.61 ? 153 PRO A CB  1 
ATOM   1241  C  CG  . PRO A 1 153 ? 31.769  -17.709 24.662  1.00 17.90 ? 153 PRO A CG  1 
ATOM   1242  C  CD  . PRO A 1 153 ? 30.521  -17.355 23.747  1.00 13.31 ? 153 PRO A CD  1 
ATOM   1243  N  N   . SER A 1 154 ? 31.946  -14.121 22.431  1.00 14.48 ? 154 SER A N   1 
ATOM   1244  C  CA  . SER A 1 154 ? 32.568  -12.994 21.649  1.00 12.70 ? 154 SER A CA  1 
ATOM   1245  C  C   . SER A 1 154 ? 31.766  -11.708 21.802  1.00 10.90 ? 154 SER A C   1 
ATOM   1246  O  O   . SER A 1 154 ? 32.338  -10.647 21.966  1.00 13.56 ? 154 SER A O   1 
ATOM   1247  C  CB  . SER A 1 154 ? 32.726  -13.409 20.196  1.00 14.79 ? 154 SER A CB  1 
ATOM   1248  O  OG  . SER A 1 154 ? 33.587  -14.606 20.090  1.00 18.91 ? 154 SER A OG  1 
ATOM   1249  N  N   . TYR A 1 155 ? 30.399  -11.847 21.709  1.00 12.76 ? 155 TYR A N   1 
ATOM   1250  C  CA  . TYR A 1 155 ? 29.579  -10.610 21.991  1.00 11.06 ? 155 TYR A CA  1 
ATOM   1251  C  C   . TYR A 1 155 ? 29.769  -10.096 23.386  1.00 12.87 ? 155 TYR A C   1 
ATOM   1252  O  O   . TYR A 1 155 ? 29.685  -8.881  23.599  1.00 13.70 ? 155 TYR A O   1 
ATOM   1253  C  CB  . TYR A 1 155 ? 28.105  -10.818 21.668  1.00 9.99  ? 155 TYR A CB  1 
ATOM   1254  C  CG  . TYR A 1 155 ? 27.831  -10.677 20.117  1.00 10.31 ? 155 TYR A CG  1 
ATOM   1255  C  CD1 . TYR A 1 155 ? 27.251  -9.510  19.596  1.00 12.11 ? 155 TYR A CD1 1 
ATOM   1256  C  CD2 . TYR A 1 155 ? 28.156  -11.707 19.221  1.00 9.89  ? 155 TYR A CD2 1 
ATOM   1257  C  CE1 . TYR A 1 155 ? 27.005  -9.452  18.241  1.00 9.58  ? 155 TYR A CE1 1 
ATOM   1258  C  CE2 . TYR A 1 155 ? 27.972  -11.586 17.784  1.00 9.23  ? 155 TYR A CE2 1 
ATOM   1259  C  CZ  . TYR A 1 155 ? 27.394  -10.394 17.355  1.00 9.19  ? 155 TYR A CZ  1 
ATOM   1260  O  OH  . TYR A 1 155 ? 27.174  -10.194 15.984  1.00 10.01 ? 155 TYR A OH  1 
ATOM   1261  N  N   . ASP A 1 156 ? 30.062  -11.041 24.333  1.00 12.45 ? 156 ASP A N   1 
ATOM   1262  C  CA  . ASP A 1 156 ? 30.329  -10.565 25.696  1.00 14.18 ? 156 ASP A CA  1 
ATOM   1263  C  C   . ASP A 1 156 ? 31.616  -9.689  25.808  1.00 12.97 ? 156 ASP A C   1 
ATOM   1264  O  O   . ASP A 1 156 ? 31.732  -8.927  26.773  1.00 15.76 ? 156 ASP A O   1 
ATOM   1265  C  CB  . ASP A 1 156 ? 30.294  -11.654 26.730  1.00 16.28 ? 156 ASP A CB  1 
ATOM   1266  C  CG  . ASP A 1 156 ? 29.258  -11.358 27.803  1.00 18.65 ? 156 ASP A CG  1 
ATOM   1267  O  OD1 . ASP A 1 156 ? 28.146  -10.931 27.423  1.00 15.02 ? 156 ASP A OD1 1 
ATOM   1268  O  OD2 . ASP A 1 156 ? 29.554  -11.498 29.007  1.00 23.43 ? 156 ASP A OD2 1 
ATOM   1269  N  N   . LYS A 1 157 ? 32.509  -9.783  24.821  1.00 12.04 ? 157 LYS A N   1 
ATOM   1270  C  CA  . LYS A 1 157 ? 33.670  -8.942  24.836  1.00 14.26 ? 157 LYS A CA  1 
ATOM   1271  C  C   . LYS A 1 157 ? 33.207  -7.468  24.684  1.00 15.48 ? 157 LYS A C   1 
ATOM   1272  O  O   . LYS A 1 157 ? 33.942  -6.570  25.186  1.00 16.57 ? 157 LYS A O   1 
ATOM   1273  C  CB  . LYS A 1 157 ? 34.733  -9.379  23.804  1.00 14.31 ? 157 LYS A CB  1 
ATOM   1274  C  CG  . LYS A 1 157 ? 35.259  -10.758 24.076  1.00 14.45 ? 157 LYS A CG  1 
ATOM   1275  C  CD  . LYS A 1 157 ? 36.199  -11.259 22.987  1.00 19.00 ? 157 LYS A CD  1 
ATOM   1276  C  CE  . LYS A 1 157 ? 36.613  -12.719 23.169  1.00 17.95 ? 157 LYS A CE  1 
ATOM   1277  N  NZ  . LYS A 1 157 ? 37.623  -13.204 22.131  1.00 19.56 ? 157 LYS A NZ  1 
ATOM   1278  N  N   . ILE A 1 158 ? 32.017  -7.203  24.063  1.00 14.26 ? 158 ILE A N   1 
ATOM   1279  C  CA  . ILE A 1 158 ? 31.515  -5.833  24.056  1.00 14.56 ? 158 ILE A CA  1 
ATOM   1280  C  C   . ILE A 1 158 ? 30.514  -5.685  25.217  1.00 13.52 ? 158 ILE A C   1 
ATOM   1281  O  O   . ILE A 1 158 ? 30.567  -4.663  25.961  1.00 14.60 ? 158 ILE A O   1 
ATOM   1282  C  CB  . ILE A 1 158 ? 30.771  -5.570  22.788  1.00 16.02 ? 158 ILE A CB  1 
ATOM   1283  C  CG1 . ILE A 1 158 ? 31.720  -5.767  21.593  1.00 19.39 ? 158 ILE A CG1 1 
ATOM   1284  C  CG2 . ILE A 1 158 ? 30.087  -4.155  22.777  1.00 14.79 ? 158 ILE A CG2 1 
ATOM   1285  C  CD1 . ILE A 1 158 ? 31.029  -5.775  20.228  1.00 19.77 ? 158 ILE A CD1 1 
ATOM   1286  N  N   . PHE A 1 159 ? 29.628  -6.695  25.415  1.00 12.83 ? 159 PHE A N   1 
ATOM   1287  C  CA  . PHE A 1 159 ? 28.563  -6.491  26.382  1.00 13.34 ? 159 PHE A CA  1 
ATOM   1288  C  C   . PHE A 1 159 ? 29.037  -6.316  27.839  1.00 12.19 ? 159 PHE A C   1 
ATOM   1289  O  O   . PHE A 1 159 ? 28.359  -5.667  28.598  1.00 15.63 ? 159 PHE A O   1 
ATOM   1290  C  CB  . PHE A 1 159 ? 27.509  -7.602  26.336  1.00 11.04 ? 159 PHE A CB  1 
ATOM   1291  C  CG  . PHE A 1 159 ? 26.754  -7.695  24.984  1.00 13.25 ? 159 PHE A CG  1 
ATOM   1292  C  CD1 . PHE A 1 159 ? 26.715  -6.590  24.049  1.00 14.09 ? 159 PHE A CD1 1 
ATOM   1293  C  CD2 . PHE A 1 159 ? 26.113  -8.891  24.655  1.00 14.20 ? 159 PHE A CD2 1 
ATOM   1294  C  CE1 . PHE A 1 159 ? 25.957  -6.766  22.831  1.00 13.43 ? 159 PHE A CE1 1 
ATOM   1295  C  CE2 . PHE A 1 159 ? 25.422  -8.990  23.515  1.00 13.73 ? 159 PHE A CE2 1 
ATOM   1296  C  CZ  . PHE A 1 159 ? 25.384  -7.934  22.588  1.00 12.51 ? 159 PHE A CZ  1 
ATOM   1297  N  N   . SER A 1 160 ? 30.210  -6.875  28.148  1.00 14.44 ? 160 SER A N   1 
ATOM   1298  C  CA  . SER A 1 160 ? 30.693  -6.747  29.526  1.00 15.41 ? 160 SER A CA  1 
ATOM   1299  C  C   . SER A 1 160 ? 31.085  -5.347  29.855  1.00 17.02 ? 160 SER A C   1 
ATOM   1300  O  O   . SER A 1 160 ? 31.284  -5.061  31.066  1.00 18.81 ? 160 SER A O   1 
ATOM   1301  C  CB  . SER A 1 160 ? 31.869  -7.750  29.728  1.00 14.32 ? 160 SER A CB  1 
ATOM   1302  O  OG  . SER A 1 160 ? 32.949  -7.332  28.947  1.00 16.98 ? 160 SER A OG  1 
ATOM   1303  N  N   . HIS A 1 161 ? 31.219  -4.463  28.839  1.00 14.90 ? 161 HIS A N   1 
ATOM   1304  C  CA  . HIS A 1 161 ? 31.511  -3.059  29.134  1.00 15.73 ? 161 HIS A CA  1 
ATOM   1305  C  C   . HIS A 1 161 ? 30.298  -2.123  29.127  1.00 16.50 ? 161 HIS A C   1 
ATOM   1306  O  O   . HIS A 1 161 ? 30.429  -0.921  29.382  1.00 16.28 ? 161 HIS A O   1 
ATOM   1307  C  CB  . HIS A 1 161 ? 32.515  -2.535  28.123  1.00 18.19 ? 161 HIS A CB  1 
ATOM   1308  C  CG  . HIS A 1 161 ? 33.792  -3.298  28.140  1.00 17.72 ? 161 HIS A CG  1 
ATOM   1309  N  ND1 . HIS A 1 161 ? 34.885  -2.902  28.892  1.00 22.87 ? 161 HIS A ND1 1 
ATOM   1310  C  CD2 . HIS A 1 161 ? 34.185  -4.410  27.459  1.00 20.44 ? 161 HIS A CD2 1 
ATOM   1311  C  CE1 . HIS A 1 161 ? 35.891  -3.750  28.698  1.00 23.08 ? 161 HIS A CE1 1 
ATOM   1312  N  NE2 . HIS A 1 161 ? 35.507  -4.649  27.795  1.00 18.92 ? 161 HIS A NE2 1 
ATOM   1313  N  N   . LEU A 1 162 ? 29.079  -2.675  28.888  1.00 17.16 ? 162 LEU A N   1 
ATOM   1314  C  CA  . LEU A 1 162 ? 27.891  -1.813  28.810  1.00 17.69 ? 162 LEU A CA  1 
ATOM   1315  C  C   . LEU A 1 162 ? 27.646  -1.005  30.075  1.00 18.51 ? 162 LEU A C   1 
ATOM   1316  O  O   . LEU A 1 162 ? 27.112  0.126   30.008  1.00 16.40 ? 162 LEU A O   1 
ATOM   1317  C  CB  . LEU A 1 162 ? 26.599  -2.664  28.551  1.00 18.32 ? 162 LEU A CB  1 
ATOM   1318  C  CG  . LEU A 1 162 ? 26.612  -3.289  27.138  1.00 16.53 ? 162 LEU A CG  1 
ATOM   1319  C  CD1 . LEU A 1 162 ? 25.335  -4.255  26.938  1.00 18.43 ? 162 LEU A CD1 1 
ATOM   1320  C  CD2 . LEU A 1 162 ? 26.846  -2.259  25.956  1.00 22.30 ? 162 LEU A CD2 1 
ATOM   1321  N  N   . GLN A 1 163 ? 27.984  -1.607  31.238  1.00 20.42 ? 163 GLN A N   1 
ATOM   1322  C  CA  . GLN A 1 163 ? 27.636  -0.867  32.487  1.00 22.14 ? 163 GLN A CA  1 
ATOM   1323  C  C   . GLN A 1 163 ? 28.430  0.444   32.577  1.00 22.36 ? 163 GLN A C   1 
ATOM   1324  O  O   . GLN A 1 163 ? 27.856  1.496   33.003  1.00 25.42 ? 163 GLN A O   1 
ATOM   1325  C  CB  . GLN A 1 163 ? 27.727  -1.735  33.726  1.00 27.35 ? 163 GLN A CB  1 
ATOM   1326  C  CG  . GLN A 1 163 ? 29.126  -2.073  34.149  1.00 30.18 ? 163 GLN A CG  1 
ATOM   1327  C  CD  . GLN A 1 163 ? 29.947  -2.804  33.099  1.00 35.34 ? 163 GLN A CD  1 
ATOM   1328  O  OE1 . GLN A 1 163 ? 29.539  -3.842  32.584  1.00 43.25 ? 163 GLN A OE1 1 
ATOM   1329  N  NE2 . GLN A 1 163 ? 31.096  -2.274  32.790  1.00 35.00 ? 163 GLN A NE2 1 
ATOM   1330  N  N   . HIS A 1 164 ? 29.612  0.450   31.946  1.00 17.25 ? 164 HIS A N   1 
ATOM   1331  C  CA  . HIS A 1 164 ? 30.430  1.690   31.859  1.00 17.32 ? 164 HIS A CA  1 
ATOM   1332  C  C   . HIS A 1 164 ? 30.011  2.718   30.909  1.00 16.79 ? 164 HIS A C   1 
ATOM   1333  O  O   . HIS A 1 164 ? 30.590  3.817   30.876  1.00 17.73 ? 164 HIS A O   1 
ATOM   1334  C  CB  . HIS A 1 164 ? 31.912  1.379   31.705  1.00 14.22 ? 164 HIS A CB  1 
ATOM   1335  C  CG  . HIS A 1 164 ? 32.478  0.538   32.829  1.00 16.37 ? 164 HIS A CG  1 
ATOM   1336  N  ND1 . HIS A 1 164 ? 33.465  -0.401  32.641  1.00 22.43 ? 164 HIS A ND1 1 
ATOM   1337  C  CD2 . HIS A 1 164 ? 32.208  0.527   34.152  1.00 14.65 ? 164 HIS A CD2 1 
ATOM   1338  C  CE1 . HIS A 1 164 ? 33.744  -0.987  33.811  1.00 24.83 ? 164 HIS A CE1 1 
ATOM   1339  N  NE2 . HIS A 1 164 ? 32.994  -0.429  34.745  1.00 20.34 ? 164 HIS A NE2 1 
ATOM   1340  N  N   . VAL A 1 165 ? 28.988  2.353   30.075  1.00 14.61 ? 165 VAL A N   1 
ATOM   1341  C  CA  . VAL A 1 165 ? 28.552  3.348   29.127  1.00 14.73 ? 165 VAL A CA  1 
ATOM   1342  C  C   . VAL A 1 165 ? 27.032  3.547   29.207  1.00 15.42 ? 165 VAL A C   1 
ATOM   1343  O  O   . VAL A 1 165 ? 26.336  3.824   28.206  1.00 14.22 ? 165 VAL A O   1 
ATOM   1344  C  CB  . VAL A 1 165 ? 29.022  3.064   27.656  1.00 15.93 ? 165 VAL A CB  1 
ATOM   1345  C  CG1 . VAL A 1 165 ? 30.581  3.180   27.532  1.00 15.70 ? 165 VAL A CG1 1 
ATOM   1346  C  CG2 . VAL A 1 165 ? 28.618  1.705   27.138  1.00 14.77 ? 165 VAL A CG2 1 
ATOM   1347  N  N   A LYS A 1 166 ? 26.495  3.406   30.420  0.50 13.63 ? 166 LYS A N   1 
ATOM   1348  N  N   B LYS A 1 166 ? 26.549  3.423   30.435  0.50 12.90 ? 166 LYS A N   1 
ATOM   1349  C  CA  A LYS A 1 166 ? 25.028  3.539   30.656  0.50 14.15 ? 166 LYS A CA  1 
ATOM   1350  C  CA  B LYS A 1 166 ? 25.125  3.532   30.760  0.50 12.61 ? 166 LYS A CA  1 
ATOM   1351  C  C   A LYS A 1 166 ? 24.427  4.816   30.067  0.50 14.16 ? 166 LYS A C   1 
ATOM   1352  C  C   B LYS A 1 166 ? 24.428  4.768   30.212  0.50 13.43 ? 166 LYS A C   1 
ATOM   1353  O  O   A LYS A 1 166 ? 23.367  4.800   29.441  0.50 14.57 ? 166 LYS A O   1 
ATOM   1354  O  O   B LYS A 1 166 ? 23.279  4.634   29.763  0.50 13.80 ? 166 LYS A O   1 
ATOM   1355  C  CB  A LYS A 1 166 ? 24.615  3.401   32.144  0.50 15.32 ? 166 LYS A CB  1 
ATOM   1356  C  CB  B LYS A 1 166 ? 24.872  3.409   32.277  0.50 14.09 ? 166 LYS A CB  1 
ATOM   1357  C  CG  A LYS A 1 166 ? 24.933  2.018   32.774  0.50 18.15 ? 166 LYS A CG  1 
ATOM   1358  C  CG  B LYS A 1 166 ? 23.418  3.497   32.723  0.50 10.95 ? 166 LYS A CG  1 
ATOM   1359  C  CD  A LYS A 1 166 ? 24.307  1.852   34.218  0.50 15.99 ? 166 LYS A CD  1 
ATOM   1360  C  CD  B LYS A 1 166 ? 23.274  2.927   34.185  0.50 15.06 ? 166 LYS A CD  1 
ATOM   1361  C  CE  A LYS A 1 166 ? 23.225  2.924   34.557  0.50 22.04 ? 166 LYS A CE  1 
ATOM   1362  C  CE  B LYS A 1 166 ? 23.594  1.410   34.243  0.50 16.80 ? 166 LYS A CE  1 
ATOM   1363  N  NZ  A LYS A 1 166 ? 21.856  2.598   34.036  0.50 26.19 ? 166 LYS A NZ  1 
ATOM   1364  N  NZ  B LYS A 1 166 ? 24.253  0.836   35.475  0.50 22.18 ? 166 LYS A NZ  1 
ATOM   1365  N  N   . TYR A 1 167 ? 25.089  5.960   30.274  1.00 14.04 ? 167 TYR A N   1 
ATOM   1366  C  CA  . TYR A 1 167 ? 24.447  7.186   29.898  1.00 14.10 ? 167 TYR A CA  1 
ATOM   1367  C  C   . TYR A 1 167 ? 25.110  7.917   28.740  1.00 14.16 ? 167 TYR A C   1 
ATOM   1368  O  O   . TYR A 1 167 ? 26.277  7.711   28.444  1.00 14.72 ? 167 TYR A O   1 
ATOM   1369  C  CB  . TYR A 1 167 ? 24.469  8.171   31.067  1.00 14.18 ? 167 TYR A CB  1 
ATOM   1370  C  CG  . TYR A 1 167 ? 23.673  7.651   32.249  1.00 12.58 ? 167 TYR A CG  1 
ATOM   1371  C  CD1 . TYR A 1 167 ? 22.260  7.736   32.251  1.00 17.53 ? 167 TYR A CD1 1 
ATOM   1372  C  CD2 . TYR A 1 167 ? 24.339  7.132   33.356  1.00 13.28 ? 167 TYR A CD2 1 
ATOM   1373  C  CE1 . TYR A 1 167 ? 21.506  7.218   33.332  1.00 18.93 ? 167 TYR A CE1 1 
ATOM   1374  C  CE2 . TYR A 1 167 ? 23.588  6.631   34.438  1.00 18.71 ? 167 TYR A CE2 1 
ATOM   1375  C  CZ  . TYR A 1 167 ? 22.146  6.707   34.408  1.00 21.62 ? 167 TYR A CZ  1 
ATOM   1376  O  OH  . TYR A 1 167 ? 21.369  6.248   35.503  1.00 22.43 ? 167 TYR A OH  1 
ATOM   1377  N  N   . LYS A 1 168 ? 24.319  8.762   28.071  1.00 17.00 ? 168 LYS A N   1 
ATOM   1378  C  CA  . LYS A 1 168 ? 24.827  9.447   26.901  1.00 18.16 ? 168 LYS A CA  1 
ATOM   1379  C  C   . LYS A 1 168 ? 26.145  10.219  27.181  1.00 19.40 ? 168 LYS A C   1 
ATOM   1380  O  O   . LYS A 1 168 ? 26.235  10.927  28.215  1.00 19.82 ? 168 LYS A O   1 
ATOM   1381  C  CB  . LYS A 1 168 ? 23.724  10.415  26.420  1.00 18.06 ? 168 LYS A CB  1 
ATOM   1382  C  CG  . LYS A 1 168 ? 24.130  11.049  25.118  1.00 19.44 ? 168 LYS A CG  1 
ATOM   1383  C  CD  . LYS A 1 168 ? 23.187  12.144  24.573  1.00 22.86 ? 168 LYS A CD  1 
ATOM   1384  C  CE  . LYS A 1 168 ? 23.890  12.701  23.327  1.00 22.41 ? 168 LYS A CE  1 
ATOM   1385  N  NZ  . LYS A 1 168 ? 23.206  13.915  22.894  1.00 30.59 ? 168 LYS A NZ  1 
ATOM   1386  N  N   . GLY A 1 169 ? 27.142  10.155  26.299  1.00 17.18 ? 169 GLY A N   1 
ATOM   1387  C  CA  . GLY A 1 169 ? 28.393  10.881  26.645  1.00 17.99 ? 169 GLY A CA  1 
ATOM   1388  C  C   . GLY A 1 169 ? 29.376  10.056  27.434  1.00 20.62 ? 169 GLY A C   1 
ATOM   1389  O  O   . GLY A 1 169 ? 30.522  10.371  27.504  1.00 23.94 ? 169 GLY A O   1 
ATOM   1390  N  N   . GLN A 1 170 ? 28.942  8.954   28.041  1.00 17.57 ? 170 GLN A N   1 
ATOM   1391  C  CA  . GLN A 1 170 ? 29.937  8.121   28.692  1.00 15.99 ? 170 GLN A CA  1 
ATOM   1392  C  C   . GLN A 1 170 ? 30.742  7.268   27.735  1.00 17.27 ? 170 GLN A C   1 
ATOM   1393  O  O   . GLN A 1 170 ? 30.247  6.913   26.622  1.00 16.56 ? 170 GLN A O   1 
ATOM   1394  C  CB  . GLN A 1 170 ? 29.249  7.249   29.742  1.00 15.76 ? 170 GLN A CB  1 
ATOM   1395  C  CG  . GLN A 1 170 ? 28.693  8.093   30.814  1.00 13.97 ? 170 GLN A CG  1 
ATOM   1396  C  CD  . GLN A 1 170 ? 28.107  7.246   31.947  1.00 16.55 ? 170 GLN A CD  1 
ATOM   1397  O  OE1 . GLN A 1 170 ? 27.610  6.173   31.752  1.00 17.87 ? 170 GLN A OE1 1 
ATOM   1398  N  NE2 . GLN A 1 170 ? 28.182  7.785   33.169  1.00 19.84 ? 170 GLN A NE2 1 
ATOM   1399  N  N   A GLU A 1 171 ? 31.926  6.853   28.177  0.50 16.52 ? 171 GLU A N   1 
ATOM   1400  N  N   B GLU A 1 171 ? 31.928  6.810   28.142  0.50 15.38 ? 171 GLU A N   1 
ATOM   1401  C  CA  A GLU A 1 171 ? 32.889  6.141   27.385  0.50 17.45 ? 171 GLU A CA  1 
ATOM   1402  C  CA  B GLU A 1 171 ? 32.870  6.124   27.286  0.50 16.09 ? 171 GLU A CA  1 
ATOM   1403  C  C   A GLU A 1 171 ? 33.590  5.033   28.187  0.50 17.20 ? 171 GLU A C   1 
ATOM   1404  C  C   B GLU A 1 171 ? 33.761  5.201   28.066  0.50 16.27 ? 171 GLU A C   1 
ATOM   1405  O  O   A GLU A 1 171 ? 33.527  4.955   29.478  0.50 14.11 ? 171 GLU A O   1 
ATOM   1406  O  O   B GLU A 1 171 ? 34.075  5.490   29.240  0.50 17.09 ? 171 GLU A O   1 
ATOM   1407  C  CB  A GLU A 1 171 ? 33.862  7.133   26.629  0.50 18.56 ? 171 GLU A CB  1 
ATOM   1408  C  CB  B GLU A 1 171 ? 33.786  7.132   26.574  0.50 16.67 ? 171 GLU A CB  1 
ATOM   1409  C  CG  A GLU A 1 171 ? 33.103  8.386   26.050  0.50 21.15 ? 171 GLU A CG  1 
ATOM   1410  C  CG  B GLU A 1 171 ? 34.866  7.621   27.533  0.50 14.54 ? 171 GLU A CG  1 
ATOM   1411  C  CD  A GLU A 1 171 ? 33.915  9.478   25.288  0.50 20.60 ? 171 GLU A CD  1 
ATOM   1412  C  CD  B GLU A 1 171 ? 35.906  8.486   26.873  0.50 17.92 ? 171 GLU A CD  1 
ATOM   1413  O  OE1 A GLU A 1 171 ? 35.162  9.624   25.487  0.50 18.59 ? 171 GLU A OE1 1 
ATOM   1414  O  OE1 B GLU A 1 171 ? 35.671  9.032   25.777  0.50 18.64 ? 171 GLU A OE1 1 
ATOM   1415  O  OE2 A GLU A 1 171 ? 33.284  10.232  24.492  0.50 22.56 ? 171 GLU A OE2 1 
ATOM   1416  O  OE2 B GLU A 1 171 ? 36.990  8.587   27.472  0.50 16.88 ? 171 GLU A OE2 1 
ATOM   1417  N  N   . ALA A 1 172 ? 34.137  4.090   27.456  1.00 16.78 ? 172 ALA A N   1 
ATOM   1418  C  CA  . ALA A 1 172 ? 34.992  3.060   28.051  1.00 17.12 ? 172 ALA A CA  1 
ATOM   1419  C  C   . ALA A 1 172 ? 35.919  2.543   26.966  1.00 18.36 ? 172 ALA A C   1 
ATOM   1420  O  O   . ALA A 1 172 ? 35.785  2.924   25.787  1.00 18.31 ? 172 ALA A O   1 
ATOM   1421  C  CB  . ALA A 1 172 ? 34.139  1.925   28.575  1.00 16.88 ? 172 ALA A CB  1 
ATOM   1422  N  N   . PHE A 1 173 ? 36.923  1.773   27.343  1.00 17.47 ? 173 PHE A N   1 
ATOM   1423  C  CA  . PHE A 1 173 ? 37.913  1.218   26.426  1.00 18.62 ? 173 PHE A CA  1 
ATOM   1424  C  C   . PHE A 1 173 ? 37.823  -0.287  26.440  1.00 19.01 ? 173 PHE A C   1 
ATOM   1425  O  O   . PHE A 1 173 ? 37.696  -0.910  27.519  1.00 21.58 ? 173 PHE A O   1 
ATOM   1426  C  CB  . PHE A 1 173 ? 39.317  1.665   26.867  1.00 18.73 ? 173 PHE A CB  1 
ATOM   1427  C  CG  . PHE A 1 173 ? 39.579  3.082   26.469  1.00 19.63 ? 173 PHE A CG  1 
ATOM   1428  C  CD1 . PHE A 1 173 ? 39.926  3.425   25.124  1.00 21.72 ? 173 PHE A CD1 1 
ATOM   1429  C  CD2 . PHE A 1 173 ? 39.465  4.100   27.413  1.00 26.70 ? 173 PHE A CD2 1 
ATOM   1430  C  CE1 . PHE A 1 173 ? 40.198  4.753   24.767  1.00 22.96 ? 173 PHE A CE1 1 
ATOM   1431  C  CE2 . PHE A 1 173 ? 39.714  5.446   27.072  1.00 29.30 ? 173 PHE A CE2 1 
ATOM   1432  C  CZ  . PHE A 1 173 ? 40.096  5.777   25.740  1.00 23.51 ? 173 PHE A CZ  1 
ATOM   1433  N  N   . VAL A 1 174 ? 37.781  -0.884  25.235  1.00 16.01 ? 174 VAL A N   1 
ATOM   1434  C  CA  . VAL A 1 174 ? 37.678  -2.291  25.029  1.00 16.02 ? 174 VAL A CA  1 
ATOM   1435  C  C   . VAL A 1 174 ? 38.976  -2.758  24.428  1.00 16.24 ? 174 VAL A C   1 
ATOM   1436  O  O   . VAL A 1 174 ? 39.385  -2.295  23.381  1.00 17.34 ? 174 VAL A O   1 
ATOM   1437  C  CB  . VAL A 1 174 ? 36.487  -2.539  24.050  1.00 13.81 ? 174 VAL A CB  1 
ATOM   1438  C  CG1 . VAL A 1 174 ? 36.420  -3.961  23.809  1.00 15.61 ? 174 VAL A CG1 1 
ATOM   1439  C  CG2 . VAL A 1 174 ? 35.181  -2.019  24.642  1.00 17.66 ? 174 VAL A CG2 1 
ATOM   1440  N  N   . PRO A 1 175 ? 39.632  -3.760  25.036  1.00 16.93 ? 175 PRO A N   1 
ATOM   1441  C  CA  . PRO A 1 175 ? 40.873  -4.246  24.439  1.00 17.74 ? 175 PRO A CA  1 
ATOM   1442  C  C   . PRO A 1 175 ? 40.572  -4.947  23.123  1.00 17.59 ? 175 PRO A C   1 
ATOM   1443  O  O   . PRO A 1 175 ? 39.520  -5.582  22.951  1.00 15.80 ? 175 PRO A O   1 
ATOM   1444  C  CB  . PRO A 1 175 ? 41.440  -5.185  25.536  1.00 18.66 ? 175 PRO A CB  1 
ATOM   1445  C  CG  . PRO A 1 175 ? 40.642  -4.899  26.729  1.00 18.70 ? 175 PRO A CG  1 
ATOM   1446  C  CD  . PRO A 1 175 ? 39.285  -4.433  26.290  1.00 17.43 ? 175 PRO A CD  1 
ATOM   1447  N  N   . GLY A 1 176 ? 41.491  -4.861  22.201  1.00 16.15 ? 176 GLY A N   1 
ATOM   1448  C  CA  . GLY A 1 176 ? 41.274  -5.469  20.958  1.00 15.84 ? 176 GLY A CA  1 
ATOM   1449  C  C   . GLY A 1 176 ? 40.964  -6.912  21.056  1.00 15.22 ? 176 GLY A C   1 
ATOM   1450  O  O   . GLY A 1 176 ? 41.560  -7.697  21.805  1.00 18.26 ? 176 GLY A O   1 
ATOM   1451  N  N   . PHE A 1 177 ? 40.023  -7.340  20.205  1.00 14.17 ? 177 PHE A N   1 
ATOM   1452  C  CA  . PHE A 1 177 ? 39.730  -8.750  19.954  1.00 13.20 ? 177 PHE A CA  1 
ATOM   1453  C  C   . PHE A 1 177 ? 39.366  -9.025  18.469  1.00 11.86 ? 177 PHE A C   1 
ATOM   1454  O  O   . PHE A 1 177 ? 39.350  -8.039  17.708  1.00 12.82 ? 177 PHE A O   1 
ATOM   1455  C  CB  . PHE A 1 177 ? 38.651  -9.296  20.864  1.00 14.73 ? 177 PHE A CB  1 
ATOM   1456  C  CG  . PHE A 1 177 ? 37.250  -8.751  20.523  1.00 13.87 ? 177 PHE A CG  1 
ATOM   1457  C  CD1 . PHE A 1 177 ? 36.339  -9.556  19.805  1.00 16.92 ? 177 PHE A CD1 1 
ATOM   1458  C  CD2 . PHE A 1 177 ? 36.899  -7.510  20.979  1.00 12.62 ? 177 PHE A CD2 1 
ATOM   1459  C  CE1 . PHE A 1 177 ? 35.038  -9.007  19.518  1.00 15.42 ? 177 PHE A CE1 1 
ATOM   1460  C  CE2 . PHE A 1 177 ? 35.562  -6.948  20.678  1.00 15.20 ? 177 PHE A CE2 1 
ATOM   1461  C  CZ  . PHE A 1 177 ? 34.683  -7.716  19.961  1.00 12.58 ? 177 PHE A CZ  1 
ATOM   1462  N  N   . ASN A 1 178 ? 39.223  -10.259 18.071  1.00 12.00 ? 178 ASN A N   1 
ATOM   1463  C  CA  . ASN A 1 178 ? 38.960  -10.560 16.669  1.00 12.07 ? 178 ASN A CA  1 
ATOM   1464  C  C   . ASN A 1 178 ? 37.484  -10.314 16.295  1.00 13.07 ? 178 ASN A C   1 
ATOM   1465  O  O   . ASN A 1 178 ? 36.538  -11.095 16.639  1.00 12.54 ? 178 ASN A O   1 
ATOM   1466  C  CB  . ASN A 1 178 ? 39.312  -12.004 16.357  1.00 13.95 ? 178 ASN A CB  1 
ATOM   1467  C  CG  . ASN A 1 178 ? 39.089  -12.389 14.910  1.00 16.52 ? 178 ASN A CG  1 
ATOM   1468  O  OD1 . ASN A 1 178 ? 38.798  -11.564 14.013  1.00 15.11 ? 178 ASN A OD1 1 
ATOM   1469  N  ND2 . ASN A 1 178 ? 39.140  -13.678 14.642  1.00 19.85 ? 178 ASN A ND2 1 
ATOM   1470  N  N   . ILE A 1 179 ? 37.296  -9.165  15.619  1.00 11.09 ? 179 ILE A N   1 
ATOM   1471  C  CA  . ILE A 1 179 ? 35.893  -8.809  15.266  1.00 12.00 ? 179 ILE A CA  1 
ATOM   1472  C  C   . ILE A 1 179 ? 35.248  -9.886  14.357  1.00 12.74 ? 179 ILE A C   1 
ATOM   1473  O  O   . ILE A 1 179 ? 34.009  -9.952  14.301  1.00 10.43 ? 179 ILE A O   1 
ATOM   1474  C  CB  . ILE A 1 179 ? 35.963  -7.434  14.593  1.00 11.16 ? 179 ILE A CB  1 
ATOM   1475  C  CG1 . ILE A 1 179 ? 36.568  -6.338  15.461  1.00 11.39 ? 179 ILE A CG1 1 
ATOM   1476  C  CG2 . ILE A 1 179 ? 34.528  -7.003  14.143  1.00 11.21 ? 179 ILE A CG2 1 
ATOM   1477  C  CD1 . ILE A 1 179 ? 35.936  -6.181  16.861  1.00 12.94 ? 179 ILE A CD1 1 
ATOM   1478  N  N   . GLU A 1 180 ? 35.982  -10.685 13.602  1.00 11.21 ? 180 GLU A N   1 
ATOM   1479  C  CA  . GLU A 1 180 ? 35.347  -11.655 12.786  1.00 11.20 ? 180 GLU A CA  1 
ATOM   1480  C  C   . GLU A 1 180 ? 34.556  -12.662 13.702  1.00 11.21 ? 180 GLU A C   1 
ATOM   1481  O  O   . GLU A 1 180 ? 33.683  -13.325 13.156  1.00 13.01 ? 180 GLU A O   1 
ATOM   1482  C  CB  . GLU A 1 180 ? 36.424  -12.320 11.949  1.00 13.94 ? 180 GLU A CB  1 
ATOM   1483  C  CG  . GLU A 1 180 ? 35.859  -13.153 10.813  1.00 16.85 ? 180 GLU A CG  1 
ATOM   1484  C  CD  . GLU A 1 180 ? 36.846  -13.627 9.723   1.00 14.44 ? 180 GLU A CD  1 
ATOM   1485  O  OE1 . GLU A 1 180 ? 38.006  -13.284 9.879   1.00 20.36 ? 180 GLU A OE1 1 
ATOM   1486  O  OE2 . GLU A 1 180 ? 36.377  -14.367 8.861   1.00 20.98 ? 180 GLU A OE2 1 
ATOM   1487  N  N   . GLU A 1 181 ? 34.879  -12.689 15.038  1.00 10.76 ? 181 GLU A N   1 
ATOM   1488  C  CA  . GLU A 1 181 ? 34.130  -13.648 15.855  1.00 12.12 ? 181 GLU A CA  1 
ATOM   1489  C  C   . GLU A 1 181 ? 32.652  -13.191 15.970  1.00 10.41 ? 181 GLU A C   1 
ATOM   1490  O  O   . GLU A 1 181 ? 31.827  -13.961 16.480  1.00 12.47 ? 181 GLU A O   1 
ATOM   1491  C  CB  . GLU A 1 181 ? 34.676  -13.744 17.268  1.00 12.72 ? 181 GLU A CB  1 
ATOM   1492  C  CG  . GLU A 1 181 ? 36.151  -14.249 17.374  1.00 14.52 ? 181 GLU A CG  1 
ATOM   1493  C  CD  . GLU A 1 181 ? 36.773  -14.098 18.760  1.00 17.67 ? 181 GLU A CD  1 
ATOM   1494  O  OE1 . GLU A 1 181 ? 36.170  -13.583 19.756  1.00 18.97 ? 181 GLU A OE1 1 
ATOM   1495  O  OE2 . GLU A 1 181 ? 38.029  -14.389 18.779  1.00 19.86 ? 181 GLU A OE2 1 
ATOM   1496  N  N   . LEU A 1 182 ? 32.360  -11.912 15.624  1.00 9.53  ? 182 LEU A N   1 
ATOM   1497  C  CA  . LEU A 1 182 ? 30.981  -11.484 15.756  1.00 9.10  ? 182 LEU A CA  1 
ATOM   1498  C  C   . LEU A 1 182 ? 30.175  -11.867 14.524  1.00 9.38  ? 182 LEU A C   1 
ATOM   1499  O  O   . LEU A 1 182 ? 28.928  -11.662 14.480  1.00 9.52  ? 182 LEU A O   1 
ATOM   1500  C  CB  . LEU A 1 182 ? 30.970  -9.946  15.852  1.00 8.93  ? 182 LEU A CB  1 
ATOM   1501  C  CG  . LEU A 1 182 ? 31.763  -9.403  17.037  1.00 7.62  ? 182 LEU A CG  1 
ATOM   1502  C  CD1 . LEU A 1 182 ? 31.647  -7.860  17.099  1.00 9.09  ? 182 LEU A CD1 1 
ATOM   1503  C  CD2 . LEU A 1 182 ? 31.249  -9.941  18.352  1.00 12.80 ? 182 LEU A CD2 1 
ATOM   1504  N  N   . LEU A 1 183 ? 30.817  -12.360 13.465  1.00 9.27  ? 183 LEU A N   1 
ATOM   1505  C  CA  . LEU A 1 183 ? 30.141  -12.744 12.225  1.00 9.66  ? 183 LEU A CA  1 
ATOM   1506  C  C   . LEU A 1 183 ? 29.547  -14.137 12.352  1.00 11.40 ? 183 LEU A C   1 
ATOM   1507  O  O   . LEU A 1 183 ? 30.131  -14.976 13.071  1.00 11.56 ? 183 LEU A O   1 
ATOM   1508  C  CB  . LEU A 1 183 ? 31.113  -12.705 11.010  1.00 10.89 ? 183 LEU A CB  1 
ATOM   1509  C  CG  . LEU A 1 183 ? 31.692  -11.277 10.854  1.00 10.51 ? 183 LEU A CG  1 
ATOM   1510  C  CD1 . LEU A 1 183 ? 32.583  -11.243 9.655   1.00 15.90 ? 183 LEU A CD1 1 
ATOM   1511  C  CD2 . LEU A 1 183 ? 30.685  -10.113 10.794  1.00 13.73 ? 183 LEU A CD2 1 
ATOM   1512  N  N   . PRO A 1 184 ? 28.504  -14.441 11.615  1.00 10.00 ? 184 PRO A N   1 
ATOM   1513  C  CA  . PRO A 1 184 ? 27.915  -15.769 11.613  1.00 11.75 ? 184 PRO A CA  1 
ATOM   1514  C  C   . PRO A 1 184 ? 28.664  -16.748 10.791  1.00 14.52 ? 184 PRO A C   1 
ATOM   1515  O  O   . PRO A 1 184 ? 29.739  -16.475 10.228  1.00 15.13 ? 184 PRO A O   1 
ATOM   1516  C  CB  . PRO A 1 184 ? 26.497  -15.523 11.047  1.00 12.22 ? 184 PRO A CB  1 
ATOM   1517  C  CG  . PRO A 1 184 ? 26.835  -14.343 10.019  1.00 9.63  ? 184 PRO A CG  1 
ATOM   1518  C  CD  . PRO A 1 184 ? 27.807  -13.507 10.675  1.00 10.03 ? 184 PRO A CD  1 
ATOM   1519  N  N   . GLU A 1 185 ? 28.073  -17.963 10.832  1.00 17.88 ? 185 GLU A N   1 
ATOM   1520  C  CA  . GLU A 1 185 ? 28.520  -19.060 9.959   1.00 17.04 ? 185 GLU A CA  1 
ATOM   1521  C  C   . GLU A 1 185 ? 28.213  -18.763 8.498   1.00 19.72 ? 185 GLU A C   1 
ATOM   1522  O  O   . GLU A 1 185 ? 27.198  -18.023 8.200   1.00 16.74 ? 185 GLU A O   1 
ATOM   1523  C  CB  . GLU A 1 185 ? 27.677  -20.264 10.383  1.00 21.36 ? 185 GLU A CB  1 
ATOM   1524  C  CG  . GLU A 1 185 ? 28.053  -20.690 11.825  1.00 27.89 ? 185 GLU A CG  1 
ATOM   1525  C  CD  . GLU A 1 185 ? 29.529  -20.997 11.907  1.00 35.51 ? 185 GLU A CD  1 
ATOM   1526  O  OE1 . GLU A 1 185 ? 29.959  -21.855 11.117  1.00 34.86 ? 185 GLU A OE1 1 
ATOM   1527  O  OE2 . GLU A 1 185 ? 30.267  -20.350 12.690  1.00 37.37 ? 185 GLU A OE2 1 
ATOM   1528  N  N   . ARG A 1 186 ? 29.100  -19.283 7.625   1.00 15.73 ? 186 ARG A N   1 
ATOM   1529  C  CA  . ARG A 1 186 ? 28.910  -19.235 6.212   1.00 18.68 ? 186 ARG A CA  1 
ATOM   1530  C  C   . ARG A 1 186 ? 28.661  -17.753 5.817   1.00 16.12 ? 186 ARG A C   1 
ATOM   1531  O  O   . ARG A 1 186 ? 27.659  -17.411 5.101   1.00 15.41 ? 186 ARG A O   1 
ATOM   1532  C  CB  . ARG A 1 186 ? 27.802  -20.110 5.689   1.00 19.44 ? 186 ARG A CB  1 
ATOM   1533  C  CG  . ARG A 1 186 ? 27.901  -21.523 6.278   1.00 25.92 ? 186 ARG A CG  1 
ATOM   1534  C  CD  . ARG A 1 186 ? 26.966  -22.569 5.688   1.00 27.72 ? 186 ARG A CD  1 
ATOM   1535  N  NE  . ARG A 1 186 ? 25.584  -22.509 6.186   1.00 33.43 ? 186 ARG A NE  1 
ATOM   1536  C  CZ  . ARG A 1 186 ? 25.227  -22.647 7.470   1.00 34.65 ? 186 ARG A CZ  1 
ATOM   1537  N  NH1 . ARG A 1 186 ? 26.141  -22.777 8.423   1.00 37.76 ? 186 ARG A NH1 1 
ATOM   1538  N  NH2 . ARG A 1 186 ? 23.944  -22.579 7.819   1.00 36.01 ? 186 ARG A NH2 1 
ATOM   1539  N  N   . THR A 1 187 ? 29.670  -16.970 6.121   1.00 11.86 ? 187 THR A N   1 
ATOM   1540  C  CA  . THR A 1 187 ? 29.647  -15.580 5.642   1.00 12.98 ? 187 THR A CA  1 
ATOM   1541  C  C   . THR A 1 187 ? 29.661  -15.442 4.145   1.00 12.98 ? 187 THR A C   1 
ATOM   1542  O  O   . THR A 1 187 ? 29.347  -14.367 3.647   1.00 13.30 ? 187 THR A O   1 
ATOM   1543  C  CB  . THR A 1 187 ? 30.767  -14.738 6.188   1.00 13.28 ? 187 THR A CB  1 
ATOM   1544  O  OG1 . THR A 1 187 ? 32.007  -15.430 5.992   1.00 13.76 ? 187 THR A OG1 1 
ATOM   1545  C  CG2 . THR A 1 187 ? 30.630  -14.448 7.729   1.00 12.68 ? 187 THR A CG2 1 
ATOM   1546  N  N   . ALA A 1 188 ? 30.017  -16.495 3.400   1.00 13.02 ? 188 ALA A N   1 
ATOM   1547  C  CA  . ALA A 1 188 ? 29.772  -16.450 1.920   1.00 13.32 ? 188 ALA A CA  1 
ATOM   1548  C  C   . ALA A 1 188 ? 28.311  -16.256 1.518   1.00 11.69 ? 188 ALA A C   1 
ATOM   1549  O  O   . ALA A 1 188 ? 28.085  -15.881 0.366   1.00 12.09 ? 188 ALA A O   1 
ATOM   1550  C  CB  . ALA A 1 188 ? 30.288  -17.753 1.243   1.00 15.70 ? 188 ALA A CB  1 
ATOM   1551  N  N   . GLU A 1 189 ? 27.386  -16.545 2.436   1.00 12.45 ? 189 GLU A N   1 
ATOM   1552  C  CA  . GLU A 1 189 ? 25.962  -16.489 2.112   1.00 12.07 ? 189 GLU A CA  1 
ATOM   1553  C  C   . GLU A 1 189 ? 25.429  -15.167 2.625   1.00 10.51 ? 189 GLU A C   1 
ATOM   1554  O  O   . GLU A 1 189 ? 25.386  -14.933 3.812   1.00 8.52  ? 189 GLU A O   1 
ATOM   1555  C  CB  . GLU A 1 189 ? 25.183  -17.626 2.764   1.00 13.59 ? 189 GLU A CB  1 
ATOM   1556  C  CG  . GLU A 1 189 ? 25.663  -19.009 2.199   1.00 18.12 ? 189 GLU A CG  1 
ATOM   1557  C  CD  . GLU A 1 189 ? 25.098  -20.186 2.980   1.00 26.08 ? 189 GLU A CD  1 
ATOM   1558  O  OE1 . GLU A 1 189 ? 24.351  -20.062 3.987   1.00 23.78 ? 189 GLU A OE1 1 
ATOM   1559  O  OE2 . GLU A 1 189 ? 25.554  -21.314 2.629   1.00 33.63 ? 189 GLU A OE2 1 
ATOM   1560  N  N   . TYR A 1 190 ? 24.998  -14.295 1.711   1.00 9.67  ? 190 TYR A N   1 
ATOM   1561  C  CA  . TYR A 1 190 ? 24.541  -12.943 2.080   1.00 8.92  ? 190 TYR A CA  1 
ATOM   1562  C  C   . TYR A 1 190 ? 23.566  -12.398 1.081   1.00 8.91  ? 190 TYR A C   1 
ATOM   1563  O  O   . TYR A 1 190 ? 23.477  -12.785 -0.091  1.00 8.64  ? 190 TYR A O   1 
ATOM   1564  C  CB  . TYR A 1 190 ? 25.739  -11.979 2.324   1.00 9.96  ? 190 TYR A CB  1 
ATOM   1565  C  CG  . TYR A 1 190 ? 26.634  -11.836 1.110   1.00 10.68 ? 190 TYR A CG  1 
ATOM   1566  C  CD1 . TYR A 1 190 ? 26.320  -10.949 0.109   1.00 11.03 ? 190 TYR A CD1 1 
ATOM   1567  C  CD2 . TYR A 1 190 ? 27.884  -12.484 1.059   1.00 11.77 ? 190 TYR A CD2 1 
ATOM   1568  C  CE1 . TYR A 1 190 ? 27.162  -10.776 -1.030  1.00 11.38 ? 190 TYR A CE1 1 
ATOM   1569  C  CE2 . TYR A 1 190 ? 28.702  -12.283 -0.047  1.00 10.27 ? 190 TYR A CE2 1 
ATOM   1570  C  CZ  . TYR A 1 190 ? 28.366  -11.414 -1.026  1.00 11.46 ? 190 TYR A CZ  1 
ATOM   1571  O  OH  . TYR A 1 190 ? 29.281  -11.317 -2.136  1.00 12.10 ? 190 TYR A OH  1 
ATOM   1572  N  N   . TYR A 1 191 ? 22.798  -11.414 1.565   1.00 8.73  ? 191 TYR A N   1 
ATOM   1573  C  CA  . TYR A 1 191 ? 21.983  -10.443 0.739   1.00 7.86  ? 191 TYR A CA  1 
ATOM   1574  C  C   . TYR A 1 191 ? 22.747  -9.164  0.473   1.00 9.49  ? 191 TYR A C   1 
ATOM   1575  O  O   . TYR A 1 191 ? 23.472  -8.684  1.331   1.00 9.41  ? 191 TYR A O   1 
ATOM   1576  C  CB  . TYR A 1 191 ? 20.671  -10.048 1.503   1.00 8.46  ? 191 TYR A CB  1 
ATOM   1577  C  CG  . TYR A 1 191 ? 19.860  -11.191 2.114   1.00 8.23  ? 191 TYR A CG  1 
ATOM   1578  C  CD1 . TYR A 1 191 ? 18.765  -11.717 1.413   1.00 10.06 ? 191 TYR A CD1 1 
ATOM   1579  C  CD2 . TYR A 1 191 ? 20.140  -11.586 3.437   1.00 7.05  ? 191 TYR A CD2 1 
ATOM   1580  C  CE1 . TYR A 1 191 ? 18.027  -12.754 1.974   1.00 9.79  ? 191 TYR A CE1 1 
ATOM   1581  C  CE2 . TYR A 1 191 ? 19.328  -12.561 4.072   1.00 7.76  ? 191 TYR A CE2 1 
ATOM   1582  C  CZ  . TYR A 1 191 ? 18.262  -13.104 3.312   1.00 10.06 ? 191 TYR A CZ  1 
ATOM   1583  O  OH  . TYR A 1 191 ? 17.497  -14.131 3.873   1.00 11.67 ? 191 TYR A OH  1 
ATOM   1584  N  N   . ARG A 1 192 ? 22.565  -8.656  -0.734  1.00 8.45  ? 192 ARG A N   1 
ATOM   1585  C  CA  . ARG A 1 192 ? 23.292  -7.424  -1.130  1.00 8.82  ? 192 ARG A CA  1 
ATOM   1586  C  C   . ARG A 1 192 ? 22.333  -6.479  -1.851  1.00 8.05  ? 192 ARG A C   1 
ATOM   1587  O  O   . ARG A 1 192 ? 21.600  -6.890  -2.775  1.00 9.06  ? 192 ARG A O   1 
ATOM   1588  C  CB  . ARG A 1 192 ? 24.422  -7.851  -2.111  1.00 9.34  ? 192 ARG A CB  1 
ATOM   1589  C  CG  . ARG A 1 192 ? 25.076  -6.666  -2.914  1.00 12.23 ? 192 ARG A CG  1 
ATOM   1590  C  CD  . ARG A 1 192 ? 25.877  -5.744  -2.036  1.00 12.09 ? 192 ARG A CD  1 
ATOM   1591  N  NE  . ARG A 1 192 ? 26.864  -6.390  -1.139  1.00 11.58 ? 192 ARG A NE  1 
ATOM   1592  C  CZ  . ARG A 1 192 ? 27.996  -7.000  -1.580  1.00 11.63 ? 192 ARG A CZ  1 
ATOM   1593  N  NH1 . ARG A 1 192 ? 28.368  -6.945  -2.918  1.00 15.04 ? 192 ARG A NH1 1 
ATOM   1594  N  NH2 . ARG A 1 192 ? 28.849  -7.547  -0.715  1.00 12.69 ? 192 ARG A NH2 1 
ATOM   1595  N  N   . TYR A 1 193 ? 22.367  -5.182  -1.435  1.00 7.79  ? 193 TYR A N   1 
ATOM   1596  C  CA  . TYR A 1 193 ? 21.572  -4.190  -2.155  1.00 7.91  ? 193 TYR A CA  1 
ATOM   1597  C  C   . TYR A 1 193 ? 22.121  -2.820  -1.863  1.00 8.44  ? 193 TYR A C   1 
ATOM   1598  O  O   . TYR A 1 193 ? 22.828  -2.608  -0.859  1.00 9.26  ? 193 TYR A O   1 
ATOM   1599  C  CB  . TYR A 1 193 ? 20.038  -4.314  -1.797  1.00 8.82  ? 193 TYR A CB  1 
ATOM   1600  C  CG  . TYR A 1 193 ? 19.656  -3.762  -0.429  1.00 7.72  ? 193 TYR A CG  1 
ATOM   1601  C  CD1 . TYR A 1 193 ? 19.120  -2.466  -0.327  1.00 8.76  ? 193 TYR A CD1 1 
ATOM   1602  C  CD2 . TYR A 1 193 ? 19.896  -4.466  0.773   1.00 8.71  ? 193 TYR A CD2 1 
ATOM   1603  C  CE1 . TYR A 1 193 ? 18.810  -1.905  0.929   1.00 10.21 ? 193 TYR A CE1 1 
ATOM   1604  C  CE2 . TYR A 1 193 ? 19.567  -3.961  2.010   1.00 7.55  ? 193 TYR A CE2 1 
ATOM   1605  C  CZ  . TYR A 1 193 ? 19.053  -2.644  2.119   1.00 8.54  ? 193 TYR A CZ  1 
ATOM   1606  O  OH  . TYR A 1 193 ? 18.728  -2.084  3.300   1.00 8.36  ? 193 TYR A OH  1 
ATOM   1607  N  N   . ARG A 1 194 ? 21.780  -1.823  -2.687  1.00 9.05  ? 194 ARG A N   1 
ATOM   1608  C  CA  . ARG A 1 194 ? 22.201  -0.455  -2.449  1.00 8.07  ? 194 ARG A CA  1 
ATOM   1609  C  C   . ARG A 1 194 ? 21.086  0.250   -1.680  1.00 9.64  ? 194 ARG A C   1 
ATOM   1610  O  O   . ARG A 1 194 ? 19.838  0.257   -2.003  1.00 11.05 ? 194 ARG A O   1 
ATOM   1611  C  CB  . ARG A 1 194 ? 22.291  0.254   -3.805  1.00 13.80 ? 194 ARG A CB  1 
ATOM   1612  C  CG  . ARG A 1 194 ? 23.481  -0.192  -4.560  1.00 13.69 ? 194 ARG A CG  1 
ATOM   1613  C  CD  . ARG A 1 194 ? 23.995  0.633   -5.713  1.00 20.34 ? 194 ARG A CD  1 
ATOM   1614  N  NE  . ARG A 1 194 ? 25.289  0.087   -6.149  1.00 36.99 ? 194 ARG A NE  1 
ATOM   1615  C  CZ  . ARG A 1 194 ? 26.464  0.453   -5.650  1.00 40.32 ? 194 ARG A CZ  1 
ATOM   1616  N  NH1 . ARG A 1 194 ? 26.516  1.387   -4.709  1.00 43.76 ? 194 ARG A NH1 1 
ATOM   1617  N  NH2 . ARG A 1 194 ? 27.593  -0.096  -6.088  1.00 42.19 ? 194 ARG A NH2 1 
ATOM   1618  N  N   . GLY A 1 195 ? 21.482  0.884   -0.590  1.00 9.00  ? 195 GLY A N   1 
ATOM   1619  C  CA  . GLY A 1 195 ? 20.544  1.595   0.270   1.00 8.60  ? 195 GLY A CA  1 
ATOM   1620  C  C   . GLY A 1 195 ? 21.111  2.768   0.985   1.00 8.92  ? 195 GLY A C   1 
ATOM   1621  O  O   . GLY A 1 195 ? 21.979  3.485   0.399   1.00 8.72  ? 195 GLY A O   1 
ATOM   1622  N  N   . SER A 1 196 ? 20.716  2.952   2.211   1.00 7.01  ? 196 SER A N   1 
ATOM   1623  C  CA  . SER A 1 196 ? 21.010  4.236   2.842   1.00 7.62  ? 196 SER A CA  1 
ATOM   1624  C  C   . SER A 1 196 ? 21.436  3.975   4.347   1.00 7.44  ? 196 SER A C   1 
ATOM   1625  O  O   . SER A 1 196 ? 21.276  2.828   4.898   1.00 7.11  ? 196 SER A O   1 
ATOM   1626  C  CB  . SER A 1 196 ? 19.765  5.158   2.984   1.00 7.72  ? 196 SER A CB  1 
ATOM   1627  O  OG  . SER A 1 196 ? 18.813  4.631   3.961   1.00 7.58  ? 196 SER A OG  1 
ATOM   1628  N  N   . LEU A 1 197 ? 21.952  5.009   4.974   1.00 7.64  ? 197 LEU A N   1 
ATOM   1629  C  CA  . LEU A 1 197 ? 22.083  4.938   6.430   1.00 8.19  ? 197 LEU A CA  1 
ATOM   1630  C  C   . LEU A 1 197 ? 20.647  4.721   6.997   1.00 6.82  ? 197 LEU A C   1 
ATOM   1631  O  O   . LEU A 1 197 ? 19.660  5.340   6.454   1.00 7.77  ? 197 LEU A O   1 
ATOM   1632  C  CB  . LEU A 1 197 ? 22.600  6.282   7.004   1.00 9.76  ? 197 LEU A CB  1 
ATOM   1633  C  CG  . LEU A 1 197 ? 24.078  6.556   6.988   1.00 11.56 ? 197 LEU A CG  1 
ATOM   1634  C  CD1 . LEU A 1 197 ? 24.473  7.132   5.609   1.00 15.05 ? 197 LEU A CD1 1 
ATOM   1635  C  CD2 . LEU A 1 197 ? 24.337  7.655   8.018   1.00 15.17 ? 197 LEU A CD2 1 
ATOM   1636  N  N   . THR A 1 198 ? 20.489  3.922   8.056   1.00 6.55  ? 198 THR A N   1 
ATOM   1637  C  CA  . THR A 1 198 ? 19.161  3.782   8.632   1.00 7.10  ? 198 THR A CA  1 
ATOM   1638  C  C   . THR A 1 198 ? 18.885  4.823   9.728   1.00 7.67  ? 198 THR A C   1 
ATOM   1639  O  O   . THR A 1 198 ? 17.819  4.780   10.400  1.00 7.78  ? 198 THR A O   1 
ATOM   1640  C  CB  . THR A 1 198 ? 18.976  2.362   9.279   1.00 7.16  ? 198 THR A CB  1 
ATOM   1641  O  OG1 . THR A 1 198 ? 19.963  2.277   10.337  1.00 7.60  ? 198 THR A OG1 1 
ATOM   1642  C  CG2 . THR A 1 198 ? 19.199  1.253   8.259   1.00 8.75  ? 198 THR A CG2 1 
ATOM   1643  N  N   . THR A 1 199 ? 19.878  5.729   10.005  1.00 6.72  ? 199 THR A N   1 
ATOM   1644  C  CA  . THR A 1 199 ? 19.746  6.822   10.914  1.00 7.14  ? 199 THR A CA  1 
ATOM   1645  C  C   . THR A 1 199 ? 19.953  8.085   10.135  1.00 8.29  ? 199 THR A C   1 
ATOM   1646  O  O   . THR A 1 199 ? 20.616  8.069   9.080   1.00 9.09  ? 199 THR A O   1 
ATOM   1647  C  CB  . THR A 1 199 ? 20.772  6.827   12.029  1.00 8.28  ? 199 THR A CB  1 
ATOM   1648  O  OG1 . THR A 1 199 ? 22.033  6.847   11.408  1.00 11.87 ? 199 THR A OG1 1 
ATOM   1649  C  CG2 . THR A 1 199 ? 20.661  5.448   12.823  1.00 11.79 ? 199 THR A CG2 1 
ATOM   1650  N  N   . PRO A 1 200 ? 19.433  9.176   10.739  1.00 7.17  ? 200 PRO A N   1 
ATOM   1651  C  CA  . PRO A 1 200 ? 19.789  10.486  10.115  1.00 8.80  ? 200 PRO A CA  1 
ATOM   1652  C  C   . PRO A 1 200 ? 21.330  10.596  9.932   1.00 10.09 ? 200 PRO A C   1 
ATOM   1653  O  O   . PRO A 1 200 ? 22.024  10.119  10.842  1.00 10.88 ? 200 PRO A O   1 
ATOM   1654  C  CB  . PRO A 1 200 ? 19.250  11.476  11.134  1.00 8.94  ? 200 PRO A CB  1 
ATOM   1655  C  CG  . PRO A 1 200 ? 18.056  10.865  11.686  1.00 8.05  ? 200 PRO A CG  1 
ATOM   1656  C  CD  . PRO A 1 200 ? 18.477  9.347   11.825  1.00 8.20  ? 200 PRO A CD  1 
ATOM   1657  N  N   . PRO A 1 201 ? 21.783  11.133  8.848   1.00 8.26  ? 201 PRO A N   1 
ATOM   1658  C  CA  . PRO A 1 201 ? 20.999  11.913  7.826   1.00 8.89  ? 201 PRO A CA  1 
ATOM   1659  C  C   . PRO A 1 201 ? 20.416  11.087  6.704   1.00 9.40  ? 201 PRO A C   1 
ATOM   1660  O  O   . PRO A 1 201 ? 19.909  11.619  5.730   1.00 9.98  ? 201 PRO A O   1 
ATOM   1661  C  CB  . PRO A 1 201 ? 22.012  12.907  7.240   1.00 7.66  ? 201 PRO A CB  1 
ATOM   1662  C  CG  . PRO A 1 201 ? 23.214  12.914  8.171   1.00 10.11 ? 201 PRO A CG  1 
ATOM   1663  C  CD  . PRO A 1 201 ? 23.253  11.391  8.716   1.00 10.01 ? 201 PRO A CD  1 
ATOM   1664  N  N   . CYS A 1 202 ? 20.513  9.732   6.807   1.00 8.64  ? 202 CYS A N   1 
ATOM   1665  C  CA  . CYS A 1 202 ? 19.816  8.764   5.859   1.00 7.84  ? 202 CYS A CA  1 
ATOM   1666  C  C   . CYS A 1 202 ? 20.343  8.846   4.438   1.00 6.55  ? 202 CYS A C   1 
ATOM   1667  O  O   . CYS A 1 202 ? 19.691  8.590   3.470   1.00 9.43  ? 202 CYS A O   1 
ATOM   1668  C  CB  . CYS A 1 202 ? 18.242  9.011   5.863   1.00 9.31  ? 202 CYS A CB  1 
ATOM   1669  S  SG  . CYS A 1 202 ? 17.414  8.944   7.418   1.00 8.47  ? 202 CYS A SG  1 
ATOM   1670  N  N   . ASN A 1 203 ? 21.623  9.256   4.313   1.00 8.71  ? 203 ASN A N   1 
ATOM   1671  C  CA  . ASN A 1 203 ? 22.131  9.390   2.934   1.00 9.89  ? 203 ASN A CA  1 
ATOM   1672  C  C   . ASN A 1 203 ? 22.113  8.127   2.178   1.00 9.23  ? 203 ASN A C   1 
ATOM   1673  O  O   . ASN A 1 203 ? 22.406  7.052   2.756   1.00 8.49  ? 203 ASN A O   1 
ATOM   1674  C  CB  . ASN A 1 203 ? 23.610  9.835   3.002   1.00 13.08 ? 203 ASN A CB  1 
ATOM   1675  C  CG  . ASN A 1 203 ? 23.775  11.006  3.935   1.00 11.52 ? 203 ASN A CG  1 
ATOM   1676  O  OD1 . ASN A 1 203 ? 23.853  10.814  5.158   1.00 14.56 ? 203 ASN A OD1 1 
ATOM   1677  N  ND2 . ASN A 1 203 ? 23.701  12.258  3.400   1.00 19.28 ? 203 ASN A ND2 1 
ATOM   1678  N  N   . PRO A 1 204 ? 21.718  8.107   0.904   1.00 9.77  ? 204 PRO A N   1 
ATOM   1679  C  CA  . PRO A 1 204 ? 21.571  6.870   0.112   1.00 10.68 ? 204 PRO A CA  1 
ATOM   1680  C  C   . PRO A 1 204 ? 22.923  6.431   -0.492  1.00 9.79  ? 204 PRO A C   1 
ATOM   1681  O  O   . PRO A 1 204 ? 23.104  6.271   -1.718  1.00 11.63 ? 204 PRO A O   1 
ATOM   1682  C  CB  . PRO A 1 204 ? 20.565  7.251   -1.006  1.00 11.01 ? 204 PRO A CB  1 
ATOM   1683  C  CG  . PRO A 1 204 ? 20.999  8.831   -1.213  1.00 11.22 ? 204 PRO A CG  1 
ATOM   1684  C  CD  . PRO A 1 204 ? 21.268  9.354   0.191   1.00 9.38  ? 204 PRO A CD  1 
ATOM   1685  N  N   . THR A 1 205 ? 23.870  6.219   0.441   1.00 8.47  ? 205 THR A N   1 
ATOM   1686  C  CA  . THR A 1 205 ? 25.247  6.022   -0.012  1.00 10.02 ? 205 THR A CA  1 
ATOM   1687  C  C   . THR A 1 205 ? 25.857  4.738   0.589   1.00 10.15 ? 205 THR A C   1 
ATOM   1688  O  O   . THR A 1 205 ? 27.058  4.541   0.544   1.00 10.05 ? 205 THR A O   1 
ATOM   1689  C  CB  . THR A 1 205 ? 26.055  7.135   0.597   1.00 9.64  ? 205 THR A CB  1 
ATOM   1690  O  OG1 . THR A 1 205 ? 25.890  7.171   1.983   1.00 10.13 ? 205 THR A OG1 1 
ATOM   1691  C  CG2 . THR A 1 205 ? 25.700  8.543   -0.105  1.00 10.59 ? 205 THR A CG2 1 
ATOM   1692  N  N   . VAL A 1 206 ? 24.979  3.799   1.030   1.00 8.85  ? 206 VAL A N   1 
ATOM   1693  C  CA  . VAL A 1 206 ? 25.468  2.537   1.587   1.00 8.78  ? 206 VAL A CA  1 
ATOM   1694  C  C   . VAL A 1 206 ? 25.263  1.328   0.757   1.00 8.34  ? 206 VAL A C   1 
ATOM   1695  O  O   . VAL A 1 206 ? 24.157  1.037   0.319   1.00 9.64  ? 206 VAL A O   1 
ATOM   1696  C  CB  . VAL A 1 206 ? 24.713  2.310   2.961   1.00 9.59  ? 206 VAL A CB  1 
ATOM   1697  C  CG1 . VAL A 1 206 ? 25.134  0.896   3.557   1.00 8.34  ? 206 VAL A CG1 1 
ATOM   1698  C  CG2 . VAL A 1 206 ? 24.967  3.435   3.913   1.00 8.14  ? 206 VAL A CG2 1 
ATOM   1699  N  N   . LEU A 1 207 ? 26.313  0.560   0.566   1.00 9.02  ? 207 LEU A N   1 
ATOM   1700  C  CA  . LEU A 1 207 ? 26.249  -0.754  -0.047  1.00 9.17  ? 207 LEU A CA  1 
ATOM   1701  C  C   . LEU A 1 207 ? 26.061  -1.756  1.129   1.00 8.60  ? 207 LEU A C   1 
ATOM   1702  O  O   . LEU A 1 207 ? 26.931  -1.887  2.040   1.00 8.58  ? 207 LEU A O   1 
ATOM   1703  C  CB  . LEU A 1 207 ? 27.553  -1.052  -0.812  1.00 9.79  ? 207 LEU A CB  1 
ATOM   1704  C  CG  . LEU A 1 207 ? 27.415  -2.395  -1.566  1.00 13.71 ? 207 LEU A CG  1 
ATOM   1705  C  CD1 . LEU A 1 207 ? 26.330  -2.219  -2.745  1.00 15.47 ? 207 LEU A CD1 1 
ATOM   1706  C  CD2 . LEU A 1 207 ? 28.750  -2.856  -2.132  1.00 19.49 ? 207 LEU A CD2 1 
ATOM   1707  N  N   . TRP A 1 208 ? 24.833  -2.288  1.219   1.00 7.79  ? 208 TRP A N   1 
ATOM   1708  C  CA  . TRP A 1 208 ? 24.484  -3.270  2.274   1.00 7.99  ? 208 TRP A CA  1 
ATOM   1709  C  C   . TRP A 1 208 ? 24.869  -4.726  1.941   1.00 7.29  ? 208 TRP A C   1 
ATOM   1710  O  O   . TRP A 1 208 ? 24.589  -5.228  0.877   1.00 8.72  ? 208 TRP A O   1 
ATOM   1711  C  CB  . TRP A 1 208 ? 22.920  -3.209  2.562   1.00 8.68  ? 208 TRP A CB  1 
ATOM   1712  C  CG  . TRP A 1 208 ? 22.567  -2.022  3.351   1.00 7.18  ? 208 TRP A CG  1 
ATOM   1713  C  CD1 . TRP A 1 208 ? 22.116  -0.823  2.875   1.00 6.65  ? 208 TRP A CD1 1 
ATOM   1714  C  CD2 . TRP A 1 208 ? 22.656  -1.844  4.777   1.00 6.19  ? 208 TRP A CD2 1 
ATOM   1715  N  NE1 . TRP A 1 208 ? 21.965  0.099   3.872   1.00 6.83  ? 208 TRP A NE1 1 
ATOM   1716  C  CE2 . TRP A 1 208 ? 22.299  -0.495  5.090   1.00 7.13  ? 208 TRP A CE2 1 
ATOM   1717  C  CE3 . TRP A 1 208 ? 23.099  -2.683  5.826   1.00 7.43  ? 208 TRP A CE3 1 
ATOM   1718  C  CZ2 . TRP A 1 208 ? 22.293  -0.011  6.396   1.00 6.71  ? 208 TRP A CZ2 1 
ATOM   1719  C  CZ3 . TRP A 1 208 ? 23.049  -2.230  7.127   1.00 6.67  ? 208 TRP A CZ3 1 
ATOM   1720  C  CH2 . TRP A 1 208 ? 22.749  -0.843  7.405   1.00 6.72  ? 208 TRP A CH2 1 
ATOM   1721  N  N   . THR A 1 209 ? 25.422  -5.364  3.000   1.00 5.36  ? 209 THR A N   1 
ATOM   1722  C  CA  . THR A 1 209 ? 25.650  -6.772  2.987   1.00 7.19  ? 209 THR A CA  1 
ATOM   1723  C  C   . THR A 1 209 ? 25.014  -7.303  4.275   1.00 7.33  ? 209 THR A C   1 
ATOM   1724  O  O   . THR A 1 209 ? 25.526  -7.019  5.354   1.00 7.36  ? 209 THR A O   1 
ATOM   1725  C  CB  . THR A 1 209 ? 27.183  -7.184  2.924   1.00 8.40  ? 209 THR A CB  1 
ATOM   1726  O  OG1 . THR A 1 209 ? 27.695  -6.573  1.709   1.00 8.80  ? 209 THR A OG1 1 
ATOM   1727  C  CG2 . THR A 1 209 ? 27.341  -8.685  2.935   1.00 9.61  ? 209 THR A CG2 1 
ATOM   1728  N  N   . VAL A 1 210 ? 23.920  -8.071  4.100   1.00 7.07  ? 210 VAL A N   1 
ATOM   1729  C  CA  . VAL A 1 210 ? 23.252  -8.648  5.297   1.00 6.75  ? 210 VAL A CA  1 
ATOM   1730  C  C   . VAL A 1 210 ? 23.529  -10.180 5.216   1.00 6.60  ? 210 VAL A C   1 
ATOM   1731  O  O   . VAL A 1 210 ? 23.161  -10.830 4.247   1.00 7.91  ? 210 VAL A O   1 
ATOM   1732  C  CB  . VAL A 1 210 ? 21.728  -8.349  5.260   1.00 6.45  ? 210 VAL A CB  1 
ATOM   1733  C  CG1 . VAL A 1 210 ? 21.123  -8.940  6.584   1.00 8.10  ? 210 VAL A CG1 1 
ATOM   1734  C  CG2 . VAL A 1 210 ? 21.451  -6.850  5.108   1.00 7.28  ? 210 VAL A CG2 1 
ATOM   1735  N  N   . PHE A 1 211 ? 24.252  -10.670 6.225   1.00 6.48  ? 211 PHE A N   1 
ATOM   1736  C  CA  . PHE A 1 211 ? 24.517  -12.121 6.192   1.00 7.96  ? 211 PHE A CA  1 
ATOM   1737  C  C   . PHE A 1 211 ? 23.251  -12.887 6.325   1.00 6.96  ? 211 PHE A C   1 
ATOM   1738  O  O   . PHE A 1 211 ? 22.338  -12.609 7.077   1.00 7.16  ? 211 PHE A O   1 
ATOM   1739  C  CB  . PHE A 1 211 ? 25.560  -12.477 7.255   1.00 7.23  ? 211 PHE A CB  1 
ATOM   1740  C  CG  . PHE A 1 211 ? 26.898  -11.865 6.960   1.00 6.84  ? 211 PHE A CG  1 
ATOM   1741  C  CD1 . PHE A 1 211 ? 27.654  -12.271 5.894   1.00 8.80  ? 211 PHE A CD1 1 
ATOM   1742  C  CD2 . PHE A 1 211 ? 27.414  -10.793 7.776   1.00 7.91  ? 211 PHE A CD2 1 
ATOM   1743  C  CE1 . PHE A 1 211 ? 28.919  -11.646 5.548   1.00 9.98  ? 211 PHE A CE1 1 
ATOM   1744  C  CE2 . PHE A 1 211 ? 28.713  -10.240 7.436   1.00 8.21  ? 211 PHE A CE2 1 
ATOM   1745  C  CZ  . PHE A 1 211 ? 29.410  -10.649 6.350   1.00 8.91  ? 211 PHE A CZ  1 
ATOM   1746  N  N   . ARG A 1 212 ? 23.231  -14.055 5.625   1.00 8.09  ? 212 ARG A N   1 
ATOM   1747  C  CA  . ARG A 1 212 ? 21.981  -14.899 5.558   1.00 7.58  ? 212 ARG A CA  1 
ATOM   1748  C  C   . ARG A 1 212 ? 21.719  -15.502 6.943   1.00 9.92  ? 212 ARG A C   1 
ATOM   1749  O  O   . ARG A 1 212 ? 20.577  -15.563 7.380   1.00 11.20 ? 212 ARG A O   1 
ATOM   1750  C  CB  . ARG A 1 212 ? 22.166  -15.994 4.558   1.00 10.71 ? 212 ARG A CB  1 
ATOM   1751  C  CG  . ARG A 1 212 ? 20.928  -16.891 4.429   1.00 11.06 ? 212 ARG A CG  1 
ATOM   1752  C  CD  . ARG A 1 212 ? 21.295  -18.146 3.671   1.00 16.54 ? 212 ARG A CD  1 
ATOM   1753  N  NE  . ARG A 1 212 ? 20.028  -18.806 3.370   1.00 21.77 ? 212 ARG A NE  1 
ATOM   1754  C  CZ  . ARG A 1 212 ? 19.869  -19.753 2.453   1.00 27.34 ? 212 ARG A CZ  1 
ATOM   1755  N  NH1 . ARG A 1 212 ? 20.919  -20.251 1.838   1.00 31.21 ? 212 ARG A NH1 1 
ATOM   1756  N  NH2 . ARG A 1 212 ? 18.618  -20.206 2.196   1.00 34.43 ? 212 ARG A NH2 1 
ATOM   1757  N  N   . ASN A 1 213 ? 22.808  -15.907 7.637   1.00 8.37  ? 213 ASN A N   1 
ATOM   1758  C  CA  . ASN A 1 213 ? 22.631  -16.684 8.895   1.00 10.30 ? 213 ASN A CA  1 
ATOM   1759  C  C   . ASN A 1 213 ? 22.757  -15.762 10.065  1.00 8.89  ? 213 ASN A C   1 
ATOM   1760  O  O   . ASN A 1 213 ? 23.707  -14.980 10.132  1.00 10.47 ? 213 ASN A O   1 
ATOM   1761  C  CB  . ASN A 1 213 ? 23.653  -17.850 8.937   1.00 11.12 ? 213 ASN A CB  1 
ATOM   1762  C  CG  . ASN A 1 213 ? 23.530  -18.765 7.715   1.00 13.75 ? 213 ASN A CG  1 
ATOM   1763  O  OD1 . ASN A 1 213 ? 24.511  -18.951 6.958   1.00 18.19 ? 213 ASN A OD1 1 
ATOM   1764  N  ND2 . ASN A 1 213 ? 22.352  -19.194 7.441   1.00 14.66 ? 213 ASN A ND2 1 
ATOM   1765  N  N   . PRO A 1 214 ? 21.874  -15.937 11.086  1.00 9.63  ? 214 PRO A N   1 
ATOM   1766  C  CA  . PRO A 1 214 ? 21.988  -15.159 12.288  1.00 10.50 ? 214 PRO A CA  1 
ATOM   1767  C  C   . PRO A 1 214 ? 23.068  -15.739 13.252  1.00 10.25 ? 214 PRO A C   1 
ATOM   1768  O  O   . PRO A 1 214 ? 23.490  -16.934 13.100  1.00 11.20 ? 214 PRO A O   1 
ATOM   1769  C  CB  . PRO A 1 214 ? 20.637  -15.289 12.924  1.00 10.89 ? 214 PRO A CB  1 
ATOM   1770  C  CG  . PRO A 1 214 ? 20.266  -16.751 12.682  1.00 13.88 ? 214 PRO A CG  1 
ATOM   1771  C  CD  . PRO A 1 214 ? 20.686  -16.876 11.147  1.00 11.93 ? 214 PRO A CD  1 
ATOM   1772  N  N   . VAL A 1 215 ? 23.488  -14.928 14.190  1.00 8.59  ? 215 VAL A N   1 
ATOM   1773  C  CA  . VAL A 1 215 ? 24.258  -15.408 15.349  1.00 8.32  ? 215 VAL A CA  1 
ATOM   1774  C  C   . VAL A 1 215 ? 23.302  -15.543 16.528  1.00 8.53  ? 215 VAL A C   1 
ATOM   1775  O  O   . VAL A 1 215 ? 22.177  -15.012 16.491  1.00 9.83  ? 215 VAL A O   1 
ATOM   1776  C  CB  . VAL A 1 215 ? 25.409  -14.557 15.718  1.00 10.93 ? 215 VAL A CB  1 
ATOM   1777  C  CG1 . VAL A 1 215 ? 26.460  -14.399 14.601  1.00 10.58 ? 215 VAL A CG1 1 
ATOM   1778  C  CG2 . VAL A 1 215 ? 24.882  -13.173 16.200  1.00 9.70  ? 215 VAL A CG2 1 
ATOM   1779  N  N   . GLN A 1 216 ? 23.771  -16.230 17.604  1.00 9.63  ? 216 GLN A N   1 
ATOM   1780  C  CA  . GLN A 1 216 ? 22.966  -16.313 18.864  1.00 8.76  ? 216 GLN A CA  1 
ATOM   1781  C  C   . GLN A 1 216 ? 23.654  -15.653 19.983  1.00 12.70 ? 216 GLN A C   1 
ATOM   1782  O  O   . GLN A 1 216 ? 24.878  -15.734 20.093  1.00 11.94 ? 216 GLN A O   1 
ATOM   1783  C  CB  . GLN A 1 216 ? 22.685  -17.818 19.207  1.00 10.43 ? 216 GLN A CB  1 
ATOM   1784  C  CG  . GLN A 1 216 ? 21.864  -18.502 18.133  1.00 12.37 ? 216 GLN A CG  1 
ATOM   1785  C  CD  . GLN A 1 216 ? 21.371  -19.848 18.487  1.00 22.12 ? 216 GLN A CD  1 
ATOM   1786  O  OE1 . GLN A 1 216 ? 21.825  -20.475 19.499  1.00 22.09 ? 216 GLN A OE1 1 
ATOM   1787  N  NE2 . GLN A 1 216 ? 20.350  -20.301 17.735  1.00 23.55 ? 216 GLN A NE2 1 
ATOM   1788  N  N   . ILE A 1 217 ? 22.851  -15.019 20.852  1.00 10.48 ? 217 ILE A N   1 
ATOM   1789  C  CA  . ILE A 1 217 ? 23.300  -14.584 22.196  1.00 10.79 ? 217 ILE A CA  1 
ATOM   1790  C  C   . ILE A 1 217 ? 22.290  -15.148 23.187  1.00 11.69 ? 217 ILE A C   1 
ATOM   1791  O  O   . ILE A 1 217 ? 21.172  -15.455 22.780  1.00 10.24 ? 217 ILE A O   1 
ATOM   1792  C  CB  . ILE A 1 217 ? 23.438  -13.010 22.215  1.00 9.31  ? 217 ILE A CB  1 
ATOM   1793  C  CG1 . ILE A 1 217 ? 22.039  -12.257 21.996  1.00 11.08 ? 217 ILE A CG1 1 
ATOM   1794  C  CG2 . ILE A 1 217 ? 24.488  -12.580 21.105  1.00 12.47 ? 217 ILE A CG2 1 
ATOM   1795  C  CD1 . ILE A 1 217 ? 22.192  -10.743 22.224  1.00 10.64 ? 217 ILE A CD1 1 
ATOM   1796  N  N   . SER A 1 218 ? 22.726  -15.199 24.435  1.00 11.84 ? 218 SER A N   1 
ATOM   1797  C  CA  . SER A 1 218 ? 21.762  -15.789 25.350  1.00 10.93 ? 218 SER A CA  1 
ATOM   1798  C  C   . SER A 1 218 ? 20.598  -14.856 25.725  1.00 13.61 ? 218 SER A C   1 
ATOM   1799  O  O   . SER A 1 218 ? 20.657  -13.646 25.508  1.00 12.11 ? 218 SER A O   1 
ATOM   1800  C  CB  . SER A 1 218 ? 22.460  -16.166 26.651  1.00 13.53 ? 218 SER A CB  1 
ATOM   1801  O  OG  . SER A 1 218 ? 22.963  -15.030 27.328  1.00 11.79 ? 218 SER A OG  1 
ATOM   1802  N  N   . GLN A 1 219 ? 19.601  -15.414 26.401  1.00 13.75 ? 219 GLN A N   1 
ATOM   1803  C  CA  . GLN A 1 219 ? 18.543  -14.528 26.892  1.00 12.78 ? 219 GLN A CA  1 
ATOM   1804  C  C   . GLN A 1 219 ? 19.026  -13.508 27.849  1.00 12.53 ? 219 GLN A C   1 
ATOM   1805  O  O   . GLN A 1 219 ? 18.606  -12.403 27.804  1.00 13.04 ? 219 GLN A O   1 
ATOM   1806  C  CB  . GLN A 1 219 ? 17.414  -15.389 27.458  1.00 18.71 ? 219 GLN A CB  1 
ATOM   1807  C  CG  . GLN A 1 219 ? 17.734  -16.034 28.713  1.00 23.40 ? 219 GLN A CG  1 
ATOM   1808  C  CD  . GLN A 1 219 ? 16.469  -16.676 29.190  1.00 34.85 ? 219 GLN A CD  1 
ATOM   1809  O  OE1 . GLN A 1 219 ? 16.020  -17.669 28.588  1.00 34.75 ? 219 GLN A OE1 1 
ATOM   1810  N  NE2 . GLN A 1 219 ? 15.809  -16.047 30.194  1.00 33.10 ? 219 GLN A NE2 1 
ATOM   1811  N  N   . GLU A 1 220 ? 20.005  -13.798 28.679  1.00 13.68 ? 220 GLU A N   1 
ATOM   1812  C  CA  . GLU A 1 220 ? 20.498  -12.873 29.586  1.00 13.50 ? 220 GLU A CA  1 
ATOM   1813  C  C   . GLU A 1 220 ? 21.325  -11.743 28.866  1.00 13.16 ? 220 GLU A C   1 
ATOM   1814  O  O   . GLU A 1 220 ? 21.305  -10.573 29.254  1.00 12.37 ? 220 GLU A O   1 
ATOM   1815  C  CB  . GLU A 1 220 ? 21.427  -13.559 30.610  1.00 14.01 ? 220 GLU A CB  1 
ATOM   1816  C  CG  . GLU A 1 220 ? 20.735  -14.652 31.554  1.00 16.62 ? 220 GLU A CG  1 
ATOM   1817  C  CD  . GLU A 1 220 ? 20.451  -16.026 30.850  1.00 25.87 ? 220 GLU A CD  1 
ATOM   1818  O  OE1 . GLU A 1 220 ? 21.006  -16.408 29.766  1.00 22.51 ? 220 GLU A OE1 1 
ATOM   1819  O  OE2 . GLU A 1 220 ? 19.596  -16.760 31.401  1.00 25.90 ? 220 GLU A OE2 1 
ATOM   1820  N  N   . GLN A 1 221 ? 22.101  -12.161 27.818  1.00 11.36 ? 221 GLN A N   1 
ATOM   1821  C  CA  . GLN A 1 221 ? 22.847  -11.120 27.060  1.00 9.90  ? 221 GLN A CA  1 
ATOM   1822  C  C   . GLN A 1 221 ? 21.870  -10.206 26.312  1.00 11.31 ? 221 GLN A C   1 
ATOM   1823  O  O   . GLN A 1 221 ? 22.081  -9.002  26.360  1.00 10.20 ? 221 GLN A O   1 
ATOM   1824  C  CB  . GLN A 1 221 ? 23.681  -11.798 26.003  1.00 9.99  ? 221 GLN A CB  1 
ATOM   1825  C  CG  . GLN A 1 221 ? 24.992  -12.426 26.595  1.00 14.10 ? 221 GLN A CG  1 
ATOM   1826  C  CD  . GLN A 1 221 ? 25.768  -13.152 25.535  1.00 10.74 ? 221 GLN A CD  1 
ATOM   1827  O  OE1 . GLN A 1 221 ? 25.340  -14.061 24.899  1.00 11.65 ? 221 GLN A OE1 1 
ATOM   1828  N  NE2 . GLN A 1 221 ? 27.006  -12.725 25.417  1.00 12.43 ? 221 GLN A NE2 1 
ATOM   1829  N  N   . LEU A 1 222 ? 20.812  -10.787 25.765  1.00 10.69 ? 222 LEU A N   1 
ATOM   1830  C  CA  . LEU A 1 222 ? 19.864  -9.950  25.051  1.00 11.42 ? 222 LEU A CA  1 
ATOM   1831  C  C   . LEU A 1 222 ? 19.169  -8.994  26.053  1.00 12.51 ? 222 LEU A C   1 
ATOM   1832  O  O   . LEU A 1 222 ? 18.968  -7.823  25.790  1.00 10.02 ? 222 LEU A O   1 
ATOM   1833  C  CB  . LEU A 1 222 ? 18.850  -10.758 24.285  1.00 11.13 ? 222 LEU A CB  1 
ATOM   1834  C  CG  . LEU A 1 222 ? 17.650  -10.033 23.701  1.00 11.40 ? 222 LEU A CG  1 
ATOM   1835  C  CD1 . LEU A 1 222 ? 18.206  -9.071  22.548  1.00 11.70 ? 222 LEU A CD1 1 
ATOM   1836  C  CD2 . LEU A 1 222 ? 16.617  -10.999 23.130  1.00 12.91 ? 222 LEU A CD2 1 
ATOM   1837  N  N   . LEU A 1 223 ? 18.768  -9.506  27.249  1.00 11.06 ? 223 LEU A N   1 
ATOM   1838  C  CA  . LEU A 1 223 ? 18.104  -8.591  28.216  1.00 12.09 ? 223 LEU A CA  1 
ATOM   1839  C  C   . LEU A 1 223 ? 19.076  -7.544  28.687  1.00 10.79 ? 223 LEU A C   1 
ATOM   1840  O  O   . LEU A 1 223 ? 18.667  -6.402  28.855  1.00 11.60 ? 223 LEU A O   1 
ATOM   1841  C  CB  . LEU A 1 223 ? 17.786  -9.489  29.433  1.00 12.78 ? 223 LEU A CB  1 
ATOM   1842  C  CG  . LEU A 1 223 ? 17.083  -8.754  30.481  1.00 13.85 ? 223 LEU A CG  1 
ATOM   1843  C  CD1 . LEU A 1 223 ? 15.691  -8.153  30.030  1.00 16.92 ? 223 LEU A CD1 1 
ATOM   1844  C  CD2 . LEU A 1 223 ? 16.944  -9.799  31.609  1.00 15.77 ? 223 LEU A CD2 1 
ATOM   1845  N  N   . ALA A 1 224 ? 20.395  -7.862  28.802  1.00 10.78 ? 224 ALA A N   1 
ATOM   1846  C  CA  . ALA A 1 224 ? 21.363  -6.853  29.203  1.00 12.91 ? 224 ALA A CA  1 
ATOM   1847  C  C   . ALA A 1 224 ? 21.443  -5.731  28.211  1.00 12.21 ? 224 ALA A C   1 
ATOM   1848  O  O   . ALA A 1 224 ? 21.447  -4.543  28.513  1.00 13.21 ? 224 ALA A O   1 
ATOM   1849  C  CB  . ALA A 1 224 ? 22.774  -7.452  29.477  1.00 13.53 ? 224 ALA A CB  1 
ATOM   1850  N  N   . LEU A 1 225 ? 21.518  -6.118  26.943  1.00 11.08 ? 225 LEU A N   1 
ATOM   1851  C  CA  . LEU A 1 225 ? 21.652  -5.070  25.903  1.00 12.50 ? 225 LEU A CA  1 
ATOM   1852  C  C   . LEU A 1 225 ? 20.402  -4.205  25.920  1.00 12.42 ? 225 LEU A C   1 
ATOM   1853  O  O   . LEU A 1 225 ? 20.513  -2.982  25.719  1.00 14.85 ? 225 LEU A O   1 
ATOM   1854  C  CB  . LEU A 1 225 ? 21.770  -5.820  24.572  1.00 11.22 ? 225 LEU A CB  1 
ATOM   1855  C  CG  . LEU A 1 225 ? 21.843  -4.906  23.329  1.00 11.15 ? 225 LEU A CG  1 
ATOM   1856  C  CD1 . LEU A 1 225 ? 23.095  -4.042  23.334  1.00 11.83 ? 225 LEU A CD1 1 
ATOM   1857  C  CD2 . LEU A 1 225 ? 21.784  -5.714  22.052  1.00 12.10 ? 225 LEU A CD2 1 
ATOM   1858  N  N   . GLU A 1 226 ? 19.208  -4.822  26.104  1.00 9.78  ? 226 GLU A N   1 
ATOM   1859  C  CA  . GLU A 1 226 ? 17.986  -4.042  26.108  1.00 11.42 ? 226 GLU A CA  1 
ATOM   1860  C  C   . GLU A 1 226 ? 17.764  -3.117  27.304  1.00 13.63 ? 226 GLU A C   1 
ATOM   1861  O  O   . GLU A 1 226 ? 16.870  -2.251  27.279  1.00 14.18 ? 226 GLU A O   1 
ATOM   1862  C  CB  . GLU A 1 226 ? 16.814  -5.030  26.070  1.00 11.34 ? 226 GLU A CB  1 
ATOM   1863  C  CG  . GLU A 1 226 ? 16.635  -5.858  24.730  1.00 8.90  ? 226 GLU A CG  1 
ATOM   1864  C  CD  . GLU A 1 226 ? 15.714  -6.981  24.826  1.00 11.42 ? 226 GLU A CD  1 
ATOM   1865  O  OE1 . GLU A 1 226 ? 15.478  -7.520  25.973  1.00 11.99 ? 226 GLU A OE1 1 
ATOM   1866  O  OE2 . GLU A 1 226 ? 15.288  -7.454  23.754  1.00 11.99 ? 226 GLU A OE2 1 
ATOM   1867  N  N   . THR A 1 227 ? 18.437  -3.434  28.420  1.00 12.76 ? 227 THR A N   1 
ATOM   1868  C  CA  . THR A 1 227 ? 18.153  -2.741  29.706  1.00 14.32 ? 227 THR A CA  1 
ATOM   1869  C  C   . THR A 1 227 ? 19.344  -1.916  30.213  1.00 14.33 ? 227 THR A C   1 
ATOM   1870  O  O   . THR A 1 227 ? 19.129  -1.201  31.173  1.00 18.05 ? 227 THR A O   1 
ATOM   1871  C  CB  . THR A 1 227 ? 17.754  -3.748  30.843  1.00 14.98 ? 227 THR A CB  1 
ATOM   1872  O  OG1 . THR A 1 227 ? 18.739  -4.725  31.036  1.00 16.00 ? 227 THR A OG1 1 
ATOM   1873  C  CG2 . THR A 1 227 ? 16.439  -4.427  30.502  1.00 16.71 ? 227 THR A CG2 1 
ATOM   1874  N  N   . ALA A 1 228 ? 20.555  -1.997  29.637  1.00 14.07 ? 228 ALA A N   1 
ATOM   1875  C  CA  . ALA A 1 228 ? 21.764  -1.432  30.189  1.00 12.65 ? 228 ALA A CA  1 
ATOM   1876  C  C   . ALA A 1 228 ? 21.866  0.019   29.959  1.00 13.76 ? 228 ALA A C   1 
ATOM   1877  O  O   . ALA A 1 228 ? 22.585  0.683   30.724  1.00 16.74 ? 228 ALA A O   1 
ATOM   1878  C  CB  . ALA A 1 228 ? 22.970  -2.167  29.626  1.00 17.19 ? 228 ALA A CB  1 
ATOM   1879  N  N   . LEU A 1 229 ? 21.231  0.543   28.877  1.00 12.43 ? 229 LEU A N   1 
ATOM   1880  C  CA  . LEU A 1 229 ? 21.626  1.884   28.428  1.00 14.46 ? 229 LEU A CA  1 
ATOM   1881  C  C   . LEU A 1 229 ? 20.488  2.837   28.403  1.00 12.78 ? 229 LEU A C   1 
ATOM   1882  O  O   . LEU A 1 229 ? 19.277  2.455   28.234  1.00 13.12 ? 229 LEU A O   1 
ATOM   1883  C  CB  . LEU A 1 229 ? 22.138  1.788   27.024  1.00 12.22 ? 229 LEU A CB  1 
ATOM   1884  C  CG  . LEU A 1 229 ? 23.244  0.747   26.720  1.00 15.34 ? 229 LEU A CG  1 
ATOM   1885  C  CD1 . LEU A 1 229 ? 23.683  0.848   25.224  1.00 17.06 ? 229 LEU A CD1 1 
ATOM   1886  C  CD2 . LEU A 1 229 ? 24.440  0.944   27.666  1.00 16.49 ? 229 LEU A CD2 1 
ATOM   1887  N  N   . TYR A 1 230 ? 20.837  4.104   28.539  1.00 12.12 ? 230 TYR A N   1 
ATOM   1888  C  CA  . TYR A 1 230 ? 19.946  5.256   28.420  1.00 14.38 ? 230 TYR A CA  1 
ATOM   1889  C  C   . TYR A 1 230 ? 20.337  6.195   27.286  1.00 13.91 ? 230 TYR A C   1 
ATOM   1890  O  O   . TYR A 1 230 ? 21.527  6.334   26.971  1.00 13.94 ? 230 TYR A O   1 
ATOM   1891  C  CB  . TYR A 1 230 ? 19.808  6.082   29.726  1.00 17.50 ? 230 TYR A CB  1 
ATOM   1892  C  CG  . TYR A 1 230 ? 19.169  5.330   30.888  1.00 20.34 ? 230 TYR A CG  1 
ATOM   1893  C  CD1 . TYR A 1 230 ? 17.940  5.750   31.358  1.00 23.50 ? 230 TYR A CD1 1 
ATOM   1894  C  CD2 . TYR A 1 230 ? 19.809  4.252   31.565  1.00 23.78 ? 230 TYR A CD2 1 
ATOM   1895  C  CE1 . TYR A 1 230 ? 17.296  5.164   32.438  1.00 25.49 ? 230 TYR A CE1 1 
ATOM   1896  C  CE2 . TYR A 1 230 ? 19.132  3.603   32.704  1.00 28.94 ? 230 TYR A CE2 1 
ATOM   1897  C  CZ  . TYR A 1 230 ? 17.882  4.135   33.122  1.00 27.10 ? 230 TYR A CZ  1 
ATOM   1898  O  OH  . TYR A 1 230 ? 17.151  3.582   34.161  1.00 32.11 ? 230 TYR A OH  1 
ATOM   1899  N  N   . CYS A 1 231 ? 19.345  6.913   26.747  1.00 15.61 ? 231 CYS A N   1 
ATOM   1900  C  CA  . CYS A 1 231 ? 19.547  7.896   25.693  1.00 17.30 ? 231 CYS A CA  1 
ATOM   1901  C  C   . CYS A 1 231 ? 19.992  9.226   26.222  1.00 17.31 ? 231 CYS A C   1 
ATOM   1902  O  O   . CYS A 1 231 ? 20.548  10.008  25.525  1.00 18.80 ? 231 CYS A O   1 
ATOM   1903  C  CB  . CYS A 1 231 ? 18.210  8.191   24.921  1.00 17.24 ? 231 CYS A CB  1 
ATOM   1904  S  SG  . CYS A 1 231 ? 17.679  6.763   23.911  1.00 18.21 ? 231 CYS A SG  1 
ATOM   1905  N  N   . THR A 1 232 ? 19.782  9.392   27.517  1.00 15.83 ? 232 THR A N   1 
ATOM   1906  C  CA  . THR A 1 232 ? 19.937  10.686  28.162  1.00 15.95 ? 232 THR A CA  1 
ATOM   1907  C  C   . THR A 1 232 ? 21.257  10.689  28.977  1.00 15.54 ? 232 THR A C   1 
ATOM   1908  O  O   . THR A 1 232 ? 21.834  9.637   29.355  1.00 17.40 ? 232 THR A O   1 
ATOM   1909  C  CB  . THR A 1 232 ? 18.695  10.943  29.086  1.00 15.12 ? 232 THR A CB  1 
ATOM   1910  O  OG1 . THR A 1 232 ? 18.332  9.744   29.793  1.00 16.18 ? 232 THR A OG1 1 
ATOM   1911  C  CG2 . THR A 1 232 ? 17.444  11.342  28.263  1.00 18.59 ? 232 THR A CG2 1 
ATOM   1912  N  N   . HIS A 1 233 ? 21.683  11.944  29.300  1.00 17.69 ? 233 HIS A N   1 
ATOM   1913  C  CA  . HIS A 1 233 ? 22.827  12.158  30.176  1.00 17.91 ? 233 HIS A CA  1 
ATOM   1914  C  C   . HIS A 1 233 ? 22.470  11.795  31.588  1.00 18.68 ? 233 HIS A C   1 
ATOM   1915  O  O   . HIS A 1 233 ? 21.284  11.829  31.991  1.00 18.62 ? 233 HIS A O   1 
ATOM   1916  C  CB  . HIS A 1 233 ? 23.166  13.651  30.119  1.00 18.15 ? 233 HIS A CB  1 
ATOM   1917  C  CG  . HIS A 1 233 ? 23.920  14.006  28.878  1.00 23.11 ? 233 HIS A CG  1 
ATOM   1918  N  ND1 . HIS A 1 233 ? 23.362  14.677  27.813  1.00 29.50 ? 233 HIS A ND1 1 
ATOM   1919  C  CD2 . HIS A 1 233 ? 25.201  13.737  28.522  1.00 27.86 ? 233 HIS A CD2 1 
ATOM   1920  C  CE1 . HIS A 1 233 ? 24.271  14.835  26.870  1.00 26.70 ? 233 HIS A CE1 1 
ATOM   1921  N  NE2 . HIS A 1 233 ? 25.392  14.268  27.269  1.00 28.68 ? 233 HIS A NE2 1 
ATOM   1922  N  N   . MET A 1 234 ? 23.503  11.443  32.325  1.00 20.05 ? 234 MET A N   1 
ATOM   1923  C  CA  . MET A 1 234 ? 23.362  10.974  33.681  1.00 22.37 ? 234 MET A CA  1 
ATOM   1924  C  C   . MET A 1 234 ? 22.509  11.863  34.566  1.00 22.73 ? 234 MET A C   1 
ATOM   1925  O  O   . MET A 1 234 ? 21.721  11.355  35.343  1.00 21.58 ? 234 MET A O   1 
ATOM   1926  C  CB  . MET A 1 234 ? 24.713  10.780  34.349  1.00 23.54 ? 234 MET A CB  1 
ATOM   1927  C  CG  . MET A 1 234 ? 24.607  9.929   35.638  1.00 25.18 ? 234 MET A CG  1 
ATOM   1928  S  SD  . MET A 1 234 ? 26.304  9.705   36.325  1.00 29.17 ? 234 MET A SD  1 
ATOM   1929  C  CE  . MET A 1 234 ? 26.728  11.434  36.136  1.00 30.53 ? 234 MET A CE  1 
ATOM   1930  N  N   A ASP A 1 235 ? 22.654  13.188  34.438  0.50 22.79 ? 235 ASP A N   1 
ATOM   1931  N  N   B ASP A 1 235 ? 22.671  13.180  34.419  0.50 22.71 ? 235 ASP A N   1 
ATOM   1932  C  CA  A ASP A 1 235 ? 21.941  14.104  35.367  0.50 23.94 ? 235 ASP A CA  1 
ATOM   1933  C  CA  B ASP A 1 235 ? 21.984  14.116  35.320  0.50 24.00 ? 235 ASP A CA  1 
ATOM   1934  C  C   A ASP A 1 235 ? 20.555  14.507  34.933  0.50 23.27 ? 235 ASP A C   1 
ATOM   1935  C  C   B ASP A 1 235 ? 20.751  14.752  34.690  0.50 23.53 ? 235 ASP A C   1 
ATOM   1936  O  O   A ASP A 1 235 ? 19.869  15.258  35.634  0.50 21.05 ? 235 ASP A O   1 
ATOM   1937  O  O   B ASP A 1 235 ? 20.334  15.858  35.064  0.50 24.91 ? 235 ASP A O   1 
ATOM   1938  C  CB  A ASP A 1 235 ? 22.753  15.379  35.644  0.50 24.69 ? 235 ASP A CB  1 
ATOM   1939  C  CB  B ASP A 1 235 ? 22.971  15.172  35.850  0.50 24.10 ? 235 ASP A CB  1 
ATOM   1940  C  CG  A ASP A 1 235 ? 23.000  16.213  34.395  0.50 27.78 ? 235 ASP A CG  1 
ATOM   1941  C  CG  B ASP A 1 235 ? 24.185  14.548  36.561  0.50 24.57 ? 235 ASP A CG  1 
ATOM   1942  O  OD1 A ASP A 1 235 ? 24.101  16.794  34.306  0.50 31.80 ? 235 ASP A OD1 1 
ATOM   1943  O  OD1 B ASP A 1 235 ? 24.002  13.664  37.418  0.50 22.21 ? 235 ASP A OD1 1 
ATOM   1944  O  OD2 A ASP A 1 235 ? 22.118  16.285  33.512  0.50 30.94 ? 235 ASP A OD2 1 
ATOM   1945  O  OD2 B ASP A 1 235 ? 25.340  14.901  36.242  0.50 27.14 ? 235 ASP A OD2 1 
ATOM   1946  N  N   . ASP A 1 236 ? 20.125  14.010  33.780  1.00 22.76 ? 236 ASP A N   1 
ATOM   1947  C  CA  . ASP A 1 236 ? 18.847  14.413  33.186  1.00 22.37 ? 236 ASP A CA  1 
ATOM   1948  C  C   . ASP A 1 236 ? 17.726  14.020  34.124  1.00 22.36 ? 236 ASP A C   1 
ATOM   1949  O  O   . ASP A 1 236 ? 17.621  12.846  34.538  1.00 22.76 ? 236 ASP A O   1 
ATOM   1950  C  CB  . ASP A 1 236 ? 18.692  13.772  31.777  1.00 21.74 ? 236 ASP A CB  1 
ATOM   1951  C  CG  . ASP A 1 236 ? 17.534  14.357  31.008  1.00 25.67 ? 236 ASP A CG  1 
ATOM   1952  O  OD1 . ASP A 1 236 ? 16.495  14.736  31.620  1.00 26.58 ? 236 ASP A OD1 1 
ATOM   1953  O  OD2 . ASP A 1 236 ? 17.618  14.385  29.750  1.00 24.83 ? 236 ASP A OD2 1 
ATOM   1954  N  N   . PRO A 1 237 ? 16.956  15.017  34.628  1.00 23.81 ? 237 PRO A N   1 
ATOM   1955  C  CA  . PRO A 1 237 ? 15.845  14.632  35.511  1.00 24.18 ? 237 PRO A CA  1 
ATOM   1956  C  C   . PRO A 1 237 ? 14.705  13.797  34.843  1.00 26.23 ? 237 PRO A C   1 
ATOM   1957  O  O   . PRO A 1 237 ? 13.776  13.329  35.522  1.00 27.04 ? 237 PRO A O   1 
ATOM   1958  C  CB  . PRO A 1 237 ? 15.272  16.012  36.000  1.00 26.10 ? 237 PRO A CB  1 
ATOM   1959  C  CG  . PRO A 1 237 ? 15.736  17.010  35.030  1.00 25.53 ? 237 PRO A CG  1 
ATOM   1960  C  CD  . PRO A 1 237 ? 17.061  16.485  34.460  1.00 24.52 ? 237 PRO A CD  1 
ATOM   1961  N  N   . SER A 1 238 ? 14.718  13.668  33.510  1.00 26.18 ? 238 SER A N   1 
ATOM   1962  C  CA  . SER A 1 238 ? 13.718  12.829  32.852  1.00 27.14 ? 238 SER A CA  1 
ATOM   1963  C  C   . SER A 1 238 ? 14.437  11.761  31.986  1.00 24.69 ? 238 SER A C   1 
ATOM   1964  O  O   . SER A 1 238 ? 14.504  11.922  30.785  1.00 24.59 ? 238 SER A O   1 
ATOM   1965  C  CB  . SER A 1 238 ? 12.680  13.649  32.054  1.00 27.68 ? 238 SER A CB  1 
ATOM   1966  O  OG  . SER A 1 238 ? 13.205  14.900  31.681  1.00 36.93 ? 238 SER A OG  1 
ATOM   1967  N  N   . PRO A 1 239 ? 14.931  10.682  32.648  1.00 24.22 ? 239 PRO A N   1 
ATOM   1968  C  CA  . PRO A 1 239 ? 15.703  9.697   31.887  1.00 22.74 ? 239 PRO A CA  1 
ATOM   1969  C  C   . PRO A 1 239 ? 14.843  8.957   30.827  1.00 24.13 ? 239 PRO A C   1 
ATOM   1970  O  O   . PRO A 1 239 ? 13.637  8.717   31.028  1.00 24.56 ? 239 PRO A O   1 
ATOM   1971  C  CB  . PRO A 1 239 ? 16.184  8.743   32.954  1.00 22.41 ? 239 PRO A CB  1 
ATOM   1972  C  CG  . PRO A 1 239 ? 15.251  8.972   34.169  1.00 27.56 ? 239 PRO A CG  1 
ATOM   1973  C  CD  . PRO A 1 239 ? 14.927  10.388  34.090  1.00 22.59 ? 239 PRO A CD  1 
ATOM   1974  N  N   . ARG A 1 240 ? 15.479  8.579   29.723  1.00 21.60 ? 240 ARG A N   1 
ATOM   1975  C  CA  . ARG A 1 240 ? 14.819  7.796   28.683  1.00 21.50 ? 240 ARG A CA  1 
ATOM   1976  C  C   . ARG A 1 240 ? 15.693  6.573   28.392  1.00 18.40 ? 240 ARG A C   1 
ATOM   1977  O  O   . ARG A 1 240 ? 16.886  6.657   28.053  1.00 18.03 ? 240 ARG A O   1 
ATOM   1978  C  CB  . ARG A 1 240 ? 14.605  8.571   27.389  1.00 23.05 ? 240 ARG A CB  1 
ATOM   1979  C  CG  . ARG A 1 240 ? 13.881  9.918   27.454  1.00 29.82 ? 240 ARG A CG  1 
ATOM   1980  C  CD  . ARG A 1 240 ? 13.821  10.554  26.078  1.00 26.01 ? 240 ARG A CD  1 
ATOM   1981  N  NE  . ARG A 1 240 ? 14.909  11.539  25.785  1.00 33.79 ? 240 ARG A NE  1 
ATOM   1982  C  CZ  . ARG A 1 240 ? 15.863  11.433  24.832  1.00 29.65 ? 240 ARG A CZ  1 
ATOM   1983  N  NH1 . ARG A 1 240 ? 15.968  10.370  24.034  1.00 29.57 ? 240 ARG A NH1 1 
ATOM   1984  N  NH2 . ARG A 1 240 ? 16.758  12.424  24.692  1.00 33.48 ? 240 ARG A NH2 1 
ATOM   1985  N  N   . GLU A 1 241 ? 15.079  5.417   28.535  1.00 16.85 ? 241 GLU A N   1 
ATOM   1986  C  CA  . GLU A 1 241 ? 15.817  4.198   28.261  1.00 17.51 ? 241 GLU A CA  1 
ATOM   1987  C  C   . GLU A 1 241 ? 16.110  4.083   26.775  1.00 13.79 ? 241 GLU A C   1 
ATOM   1988  O  O   . GLU A 1 241 ? 15.283  4.498   25.944  1.00 15.80 ? 241 GLU A O   1 
ATOM   1989  C  CB  . GLU A 1 241 ? 14.992  2.986   28.664  1.00 17.53 ? 241 GLU A CB  1 
ATOM   1990  C  CG  . GLU A 1 241 ? 14.642  2.816   30.140  1.00 22.16 ? 241 GLU A CG  1 
ATOM   1991  C  CD  . GLU A 1 241 ? 13.575  1.710   30.379  1.00 22.85 ? 241 GLU A CD  1 
ATOM   1992  O  OE1 . GLU A 1 241 ? 12.717  1.360   29.488  1.00 35.71 ? 241 GLU A OE1 1 
ATOM   1993  O  OE2 . GLU A 1 241 ? 13.601  1.132   31.491  1.00 36.59 ? 241 GLU A OE2 1 
ATOM   1994  N  N   . MET A 1 242 ? 17.256  3.460   26.473  1.00 11.98 ? 242 MET A N   1 
ATOM   1995  C  CA  . MET A 1 242 ? 17.608  3.172   25.086  1.00 10.71 ? 242 MET A CA  1 
ATOM   1996  C  C   . MET A 1 242 ? 17.069  1.829   24.667  1.00 10.94 ? 242 MET A C   1 
ATOM   1997  O  O   . MET A 1 242 ? 17.676  0.817   24.884  1.00 11.45 ? 242 MET A O   1 
ATOM   1998  C  CB  . MET A 1 242 ? 19.155  3.319   24.867  1.00 10.05 ? 242 MET A CB  1 
ATOM   1999  C  CG  . MET A 1 242 ? 19.557  3.127   23.391  1.00 13.26 ? 242 MET A CG  1 
ATOM   2000  S  SD  . MET A 1 242 ? 21.295  3.200   23.170  1.00 12.35 ? 242 MET A SD  1 
ATOM   2001  C  CE  . MET A 1 242 ? 21.578  4.861   23.722  1.00 13.60 ? 242 MET A CE  1 
ATOM   2002  N  N   . ILE A 1 243 ? 15.824  1.905   24.103  1.00 9.94  ? 243 ILE A N   1 
ATOM   2003  C  CA  . ILE A 1 243 ? 15.139  0.704   23.622  1.00 9.96  ? 243 ILE A CA  1 
ATOM   2004  C  C   . ILE A 1 243 ? 14.521  1.019   22.233  1.00 10.07 ? 243 ILE A C   1 
ATOM   2005  O  O   . ILE A 1 243 ? 14.314  2.211   21.871  1.00 10.15 ? 243 ILE A O   1 
ATOM   2006  C  CB  . ILE A 1 243 ? 14.001  0.317   24.557  1.00 10.11 ? 243 ILE A CB  1 
ATOM   2007  C  CG1 . ILE A 1 243 ? 13.134  1.505   24.952  1.00 12.29 ? 243 ILE A CG1 1 
ATOM   2008  C  CG2 . ILE A 1 243 ? 14.561  -0.305  25.841  1.00 16.39 ? 243 ILE A CG2 1 
ATOM   2009  C  CD1 . ILE A 1 243 ? 11.840  1.020   25.767  1.00 13.05 ? 243 ILE A CD1 1 
ATOM   2010  N  N   . ASN A 1 244 ? 14.179  0.010   21.446  1.00 7.82  ? 244 ASN A N   1 
ATOM   2011  C  CA  . ASN A 1 244 ? 13.437  0.199   20.197  1.00 9.32  ? 244 ASN A CA  1 
ATOM   2012  C  C   . ASN A 1 244 ? 14.163  1.175   19.287  1.00 9.44  ? 244 ASN A C   1 
ATOM   2013  O  O   . ASN A 1 244 ? 13.545  1.982   18.613  1.00 10.86 ? 244 ASN A O   1 
ATOM   2014  C  CB  . ASN A 1 244 ? 11.975  0.602   20.511  1.00 9.71  ? 244 ASN A CB  1 
ATOM   2015  C  CG  . ASN A 1 244 ? 11.324  -0.363  21.431  1.00 10.81 ? 244 ASN A CG  1 
ATOM   2016  O  OD1 . ASN A 1 244 ? 11.549  -1.566  21.337  1.00 11.29 ? 244 ASN A OD1 1 
ATOM   2017  N  ND2 . ASN A 1 244 ? 10.532  0.203   22.406  1.00 14.80 ? 244 ASN A ND2 1 
ATOM   2018  N  N   . ASN A 1 245 ? 15.537  1.047   19.282  1.00 8.41  ? 245 ASN A N   1 
ATOM   2019  C  CA  . ASN A 1 245 ? 16.368  1.971   18.480  1.00 8.90  ? 245 ASN A CA  1 
ATOM   2020  C  C   . ASN A 1 245 ? 16.586  1.363   17.088  1.00 7.17  ? 245 ASN A C   1 
ATOM   2021  O  O   . ASN A 1 245 ? 17.740  1.224   16.634  1.00 7.74  ? 245 ASN A O   1 
ATOM   2022  C  CB  . ASN A 1 245 ? 17.673  2.311   19.211  1.00 8.52  ? 245 ASN A CB  1 
ATOM   2023  C  CG  . ASN A 1 245 ? 18.532  1.116   19.479  1.00 9.24  ? 245 ASN A CG  1 
ATOM   2024  O  OD1 . ASN A 1 245 ? 18.061  0.006   19.472  1.00 9.05  ? 245 ASN A OD1 1 
ATOM   2025  N  ND2 . ASN A 1 245 ? 19.851  1.334   19.820  1.00 10.18 ? 245 ASN A ND2 1 
ATOM   2026  N  N   . PHE A 1 246 ? 15.498  1.016   16.379  1.00 7.23  ? 246 PHE A N   1 
ATOM   2027  C  CA  . PHE A 1 246 ? 15.567  0.539   14.964  1.00 6.28  ? 246 PHE A CA  1 
ATOM   2028  C  C   . PHE A 1 246 ? 14.542  1.332   14.161  1.00 7.43  ? 246 PHE A C   1 
ATOM   2029  O  O   . PHE A 1 246 ? 13.537  1.734   14.755  1.00 7.36  ? 246 PHE A O   1 
ATOM   2030  C  CB  . PHE A 1 246 ? 15.218  -0.955  14.918  1.00 7.34  ? 246 PHE A CB  1 
ATOM   2031  C  CG  . PHE A 1 246 ? 13.817  -1.290  15.472  1.00 6.63  ? 246 PHE A CG  1 
ATOM   2032  C  CD1 . PHE A 1 246 ? 12.718  -1.469  14.571  1.00 9.21  ? 246 PHE A CD1 1 
ATOM   2033  C  CD2 . PHE A 1 246 ? 13.603  -1.514  16.849  1.00 8.35  ? 246 PHE A CD2 1 
ATOM   2034  C  CE1 . PHE A 1 246 ? 11.466  -1.754  15.043  1.00 8.39  ? 246 PHE A CE1 1 
ATOM   2035  C  CE2 . PHE A 1 246 ? 12.310  -1.835  17.348  1.00 8.03  ? 246 PHE A CE2 1 
ATOM   2036  C  CZ  . PHE A 1 246 ? 11.260  -1.927  16.424  1.00 7.05  ? 246 PHE A CZ  1 
ATOM   2037  N  N   . ARG A 1 247 ? 14.871  1.495   12.895  1.00 7.35  ? 247 ARG A N   1 
ATOM   2038  C  CA  . ARG A 1 247 ? 13.930  2.154   11.989  1.00 6.03  ? 247 ARG A CA  1 
ATOM   2039  C  C   . ARG A 1 247 ? 12.931  1.159   11.433  1.00 6.10  ? 247 ARG A C   1 
ATOM   2040  O  O   . ARG A 1 247 ? 13.305  0.024   11.162  1.00 7.06  ? 247 ARG A O   1 
ATOM   2041  C  CB  . ARG A 1 247 ? 14.686  2.822   10.872  1.00 7.98  ? 247 ARG A CB  1 
ATOM   2042  C  CG  . ARG A 1 247 ? 13.871  3.849   9.971   1.00 5.45  ? 247 ARG A CG  1 
ATOM   2043  C  CD  . ARG A 1 247 ? 14.734  4.231   8.831   1.00 7.48  ? 247 ARG A CD  1 
ATOM   2044  N  NE  . ARG A 1 247 ? 14.091  5.442   8.206   1.00 6.99  ? 247 ARG A NE  1 
ATOM   2045  C  CZ  . ARG A 1 247 ? 14.579  6.007   7.119   1.00 6.76  ? 247 ARG A CZ  1 
ATOM   2046  N  NH1 . ARG A 1 247 ? 15.598  5.483   6.457   1.00 6.40  ? 247 ARG A NH1 1 
ATOM   2047  N  NH2 . ARG A 1 247 ? 14.037  7.154   6.697   1.00 6.29  ? 247 ARG A NH2 1 
ATOM   2048  N  N   . GLN A 1 248 ? 11.642  1.501   11.258  1.00 6.05  ? 248 GLN A N   1 
ATOM   2049  C  CA  . GLN A 1 248 ? 10.753  0.677   10.470  1.00 5.52  ? 248 GLN A CA  1 
ATOM   2050  C  C   . GLN A 1 248 ? 11.169  0.422   9.056   1.00 7.55  ? 248 GLN A C   1 
ATOM   2051  O  O   . GLN A 1 248 ? 11.933  1.193   8.451   1.00 7.24  ? 248 GLN A O   1 
ATOM   2052  C  CB  . GLN A 1 248 ? 9.374   1.364   10.393  1.00 8.49  ? 248 GLN A CB  1 
ATOM   2053  C  CG  . GLN A 1 248 ? 8.681   1.597   11.736  1.00 6.24  ? 248 GLN A CG  1 
ATOM   2054  C  CD  . GLN A 1 248 ? 8.337   0.342   12.458  1.00 9.47  ? 248 GLN A CD  1 
ATOM   2055  O  OE1 . GLN A 1 248 ? 9.084   -0.063  13.330  1.00 9.31  ? 248 GLN A OE1 1 
ATOM   2056  N  NE2 . GLN A 1 248 ? 7.184   -0.246  12.152  1.00 8.73  ? 248 GLN A NE2 1 
ATOM   2057  N  N   . VAL A 1 249 ? 10.827  -0.735  8.496   1.00 5.81  ? 249 VAL A N   1 
ATOM   2058  C  CA  . VAL A 1 249 ? 11.186  -1.033  7.122   1.00 7.76  ? 249 VAL A CA  1 
ATOM   2059  C  C   . VAL A 1 249 ? 10.570  -0.004  6.147   1.00 7.68  ? 249 VAL A C   1 
ATOM   2060  O  O   . VAL A 1 249 ? 9.450   0.475   6.391   1.00 8.13  ? 249 VAL A O   1 
ATOM   2061  C  CB  . VAL A 1 249 ? 10.862  -2.508  6.739   1.00 8.47  ? 249 VAL A CB  1 
ATOM   2062  C  CG1 . VAL A 1 249 ? 11.704  -3.545  7.503   1.00 8.15  ? 249 VAL A CG1 1 
ATOM   2063  C  CG2 . VAL A 1 249 ? 9.404   -2.764  6.787   1.00 11.81 ? 249 VAL A CG2 1 
ATOM   2064  N  N   . GLN A 1 250 ? 11.260  0.176   5.043   1.00 7.13  ? 250 GLN A N   1 
ATOM   2065  C  CA  . GLN A 1 250 ? 10.841  1.195   4.038   1.00 7.93  ? 250 GLN A CA  1 
ATOM   2066  C  C   . GLN A 1 250 ? 10.267  0.474   2.834   1.00 8.67  ? 250 GLN A C   1 
ATOM   2067  O  O   . GLN A 1 250 ? 10.602  -0.673  2.546   1.00 9.59  ? 250 GLN A O   1 
ATOM   2068  C  CB  . GLN A 1 250 ? 12.120  1.929   3.558   1.00 8.08  ? 250 GLN A CB  1 
ATOM   2069  C  CG  . GLN A 1 250 ? 12.973  2.530   4.767   1.00 6.96  ? 250 GLN A CG  1 
ATOM   2070  C  CD  . GLN A 1 250 ? 12.246  3.632   5.466   1.00 6.87  ? 250 GLN A CD  1 
ATOM   2071  O  OE1 . GLN A 1 250 ? 11.977  4.695   4.827   1.00 8.60  ? 250 GLN A OE1 1 
ATOM   2072  N  NE2 . GLN A 1 250 ? 11.907  3.509   6.696   1.00 6.73  ? 250 GLN A NE2 1 
ATOM   2073  N  N   . LYS A 1 251 ? 9.417   1.203   2.065   1.00 7.62  ? 251 LYS A N   1 
ATOM   2074  C  CA  . LYS A 1 251 ? 8.958   0.628   0.802   1.00 8.84  ? 251 LYS A CA  1 
ATOM   2075  C  C   . LYS A 1 251 ? 10.168  0.324   -0.084  1.00 10.20 ? 251 LYS A C   1 
ATOM   2076  O  O   . LYS A 1 251 ? 11.176  1.164   -0.075  1.00 10.40 ? 251 LYS A O   1 
ATOM   2077  C  CB  . LYS A 1 251 ? 8.028   1.608   0.096   1.00 8.95  ? 251 LYS A CB  1 
ATOM   2078  C  CG  . LYS A 1 251 ? 6.656   1.665   0.829   1.00 12.18 ? 251 LYS A CG  1 
ATOM   2079  C  CD  . LYS A 1 251 ? 5.669   2.432   0.118   1.00 13.66 ? 251 LYS A CD  1 
ATOM   2080  C  CE  . LYS A 1 251 ? 4.216   2.144   0.615   1.00 7.98  ? 251 LYS A CE  1 
ATOM   2081  N  NZ  . LYS A 1 251 ? 4.004   2.201   2.126   1.00 6.74  ? 251 LYS A NZ  1 
ATOM   2082  N  N   . PHE A 1 252 ? 10.063  -0.694  -0.929  1.00 10.73 ? 252 PHE A N   1 
ATOM   2083  C  CA  . PHE A 1 252 ? 11.156  -1.129  -1.808  1.00 12.45 ? 252 PHE A CA  1 
ATOM   2084  C  C   . PHE A 1 252 ? 10.403  -1.782  -3.008  1.00 15.86 ? 252 PHE A C   1 
ATOM   2085  O  O   . PHE A 1 252 ? 10.059  -2.939  -2.940  1.00 20.59 ? 252 PHE A O   1 
ATOM   2086  C  CB  . PHE A 1 252 ? 11.995  -2.219  -1.078  1.00 14.59 ? 252 PHE A CB  1 
ATOM   2087  C  CG  . PHE A 1 252 ? 13.240  -2.653  -1.792  1.00 15.00 ? 252 PHE A CG  1 
ATOM   2088  C  CD1 . PHE A 1 252 ? 14.410  -1.914  -1.704  1.00 14.10 ? 252 PHE A CD1 1 
ATOM   2089  C  CD2 . PHE A 1 252 ? 13.231  -3.944  -2.400  1.00 16.55 ? 252 PHE A CD2 1 
ATOM   2090  C  CE1 . PHE A 1 252 ? 15.586  -2.382  -2.316  1.00 14.66 ? 252 PHE A CE1 1 
ATOM   2091  C  CE2 . PHE A 1 252 ? 14.440  -4.429  -2.967  1.00 15.18 ? 252 PHE A CE2 1 
ATOM   2092  C  CZ  . PHE A 1 252 ? 15.603  -3.610  -2.893  1.00 14.49 ? 252 PHE A CZ  1 
ATOM   2093  N  N   . ASP A 1 253 ? 10.196  -1.068  -4.073  1.00 20.86 ? 253 ASP A N   1 
ATOM   2094  C  CA  . ASP A 1 253 ? 9.319   -1.546  -5.179  1.00 19.34 ? 253 ASP A CA  1 
ATOM   2095  C  C   . ASP A 1 253 ? 10.127  -1.424  -6.467  1.00 18.06 ? 253 ASP A C   1 
ATOM   2096  O  O   . ASP A 1 253 ? 10.917  -0.491  -6.659  1.00 20.47 ? 253 ASP A O   1 
ATOM   2097  C  CB  . ASP A 1 253 ? 8.044   -0.682  -5.270  1.00 21.93 ? 253 ASP A CB  1 
ATOM   2098  C  CG  . ASP A 1 253 ? 7.001   -1.270  -6.237  1.00 25.36 ? 253 ASP A CG  1 
ATOM   2099  O  OD1 . ASP A 1 253 ? 6.832   -2.535  -6.248  1.00 26.38 ? 253 ASP A OD1 1 
ATOM   2100  O  OD2 . ASP A 1 253 ? 6.404   -0.468  -6.991  1.00 30.94 ? 253 ASP A OD2 1 
ATOM   2101  N  N   . GLU A 1 254 ? 9.937   -2.434  -7.321  1.00 19.56 ? 254 GLU A N   1 
ATOM   2102  C  CA  . GLU A 1 254 ? 10.572  -2.524  -8.636  1.00 21.07 ? 254 GLU A CA  1 
ATOM   2103  C  C   . GLU A 1 254 ? 12.076  -2.585  -8.490  1.00 20.38 ? 254 GLU A C   1 
ATOM   2104  O  O   . GLU A 1 254 ? 12.814  -2.009  -9.288  1.00 22.40 ? 254 GLU A O   1 
ATOM   2105  C  CB  . GLU A 1 254 ? 10.199  -1.309  -9.512  1.00 20.37 ? 254 GLU A CB  1 
ATOM   2106  C  CG  . GLU A 1 254 ? 8.644   -1.094  -9.564  1.00 22.85 ? 254 GLU A CG  1 
ATOM   2107  C  CD  . GLU A 1 254 ? 8.131   -0.030  -10.512 1.00 25.35 ? 254 GLU A CD  1 
ATOM   2108  O  OE1 . GLU A 1 254 ? 8.775   1.015   -10.704 1.00 32.31 ? 254 GLU A OE1 1 
ATOM   2109  O  OE2 . GLU A 1 254 ? 6.997   -0.240  -11.036 1.00 34.30 ? 254 GLU A OE2 1 
ATOM   2110  N  N   . ARG A 1 255 ? 12.528  -3.281  -7.444  1.00 18.47 ? 255 ARG A N   1 
ATOM   2111  C  CA  . ARG A 1 255 ? 13.952  -3.410  -7.159  1.00 18.98 ? 255 ARG A CA  1 
ATOM   2112  C  C   . ARG A 1 255 ? 14.191  -4.814  -6.619  1.00 19.42 ? 255 ARG A C   1 
ATOM   2113  O  O   . ARG A 1 255 ? 13.258  -5.538  -6.129  1.00 19.97 ? 255 ARG A O   1 
ATOM   2114  C  CB  . ARG A 1 255 ? 14.436  -2.405  -6.134  1.00 17.76 ? 255 ARG A CB  1 
ATOM   2115  C  CG  . ARG A 1 255 ? 14.394  -0.917  -6.579  1.00 20.03 ? 255 ARG A CG  1 
ATOM   2116  C  CD  . ARG A 1 255 ? 15.020  0.071   -5.562  1.00 20.33 ? 255 ARG A CD  1 
ATOM   2117  N  NE  . ARG A 1 255 ? 16.400  -0.325  -5.286  1.00 22.31 ? 255 ARG A NE  1 
ATOM   2118  C  CZ  . ARG A 1 255 ? 17.062  -0.046  -4.174  1.00 22.53 ? 255 ARG A CZ  1 
ATOM   2119  N  NH1 . ARG A 1 255 ? 16.482  0.652   -3.205  1.00 20.12 ? 255 ARG A NH1 1 
ATOM   2120  N  NH2 . ARG A 1 255 ? 18.314  -0.461  -4.027  1.00 15.70 ? 255 ARG A NH2 1 
ATOM   2121  N  N   . LEU A 1 256 ? 15.478  -5.207  -6.725  1.00 18.35 ? 256 LEU A N   1 
ATOM   2122  C  CA  . LEU A 1 256 ? 15.831  -6.533  -6.326  1.00 18.06 ? 256 LEU A CA  1 
ATOM   2123  C  C   . LEU A 1 256 ? 16.846  -6.462  -5.183  1.00 15.51 ? 256 LEU A C   1 
ATOM   2124  O  O   . LEU A 1 256 ? 17.634  -5.501  -5.078  1.00 18.40 ? 256 LEU A O   1 
ATOM   2125  C  CB  . LEU A 1 256 ? 16.476  -7.274  -7.498  1.00 19.64 ? 256 LEU A CB  1 
ATOM   2126  C  CG  . LEU A 1 256 ? 15.481  -7.640  -8.631  1.00 22.25 ? 256 LEU A CG  1 
ATOM   2127  C  CD1 . LEU A 1 256 ? 16.259  -8.031  -9.796  1.00 18.35 ? 256 LEU A CD1 1 
ATOM   2128  C  CD2 . LEU A 1 256 ? 14.690  -8.834  -8.167  1.00 20.52 ? 256 LEU A CD2 1 
ATOM   2129  N  N   . VAL A 1 257 ? 16.834  -7.548  -4.401  1.00 16.81 ? 257 VAL A N   1 
ATOM   2130  C  CA  . VAL A 1 257 ? 17.957  -7.822  -3.525  1.00 15.10 ? 257 VAL A CA  1 
ATOM   2131  C  C   . VAL A 1 257 ? 18.648  -9.052  -4.077  1.00 14.23 ? 257 VAL A C   1 
ATOM   2132  O  O   . VAL A 1 257 ? 17.997  -10.113 -4.267  1.00 15.23 ? 257 VAL A O   1 
ATOM   2133  C  CB  . VAL A 1 257 ? 17.427  -8.099  -2.066  1.00 14.43 ? 257 VAL A CB  1 
ATOM   2134  C  CG1 . VAL A 1 257 ? 18.534  -8.564  -1.107  1.00 14.14 ? 257 VAL A CG1 1 
ATOM   2135  C  CG2 . VAL A 1 257 ? 16.746  -6.877  -1.404  1.00 17.04 ? 257 VAL A CG2 1 
ATOM   2136  N  N   . TYR A 1 258 ? 19.972  -8.955  -4.234  1.00 13.58 ? 258 TYR A N   1 
ATOM   2137  C  CA  . TYR A 1 258 ? 20.764  -9.983  -4.891  1.00 12.57 ? 258 TYR A CA  1 
ATOM   2138  C  C   . TYR A 1 258 ? 21.237  -10.820 -3.767  1.00 12.65 ? 258 TYR A C   1 
ATOM   2139  O  O   . TYR A 1 258 ? 21.572  -10.360 -2.659  1.00 13.29 ? 258 TYR A O   1 
ATOM   2140  C  CB  . TYR A 1 258 ? 21.940  -9.352  -5.674  1.00 14.14 ? 258 TYR A CB  1 
ATOM   2141  C  CG  . TYR A 1 258 ? 21.374  -8.461  -6.723  1.00 20.00 ? 258 TYR A CG  1 
ATOM   2142  C  CD1 . TYR A 1 258 ? 20.778  -9.028  -7.846  1.00 20.10 ? 258 TYR A CD1 1 
ATOM   2143  C  CD2 . TYR A 1 258 ? 21.262  -7.097  -6.505  1.00 18.01 ? 258 TYR A CD2 1 
ATOM   2144  C  CE1 . TYR A 1 258 ? 20.181  -8.209  -8.827  1.00 24.93 ? 258 TYR A CE1 1 
ATOM   2145  C  CE2 . TYR A 1 258 ? 20.630  -6.275  -7.471  1.00 22.29 ? 258 TYR A CE2 1 
ATOM   2146  C  CZ  . TYR A 1 258 ? 20.133  -6.862  -8.612  1.00 20.67 ? 258 TYR A CZ  1 
ATOM   2147  O  OH  . TYR A 1 258 ? 19.510  -6.009  -9.520  1.00 25.42 ? 258 TYR A OH  1 
ATOM   2148  N  N   . THR A 1 259 ? 21.346  -12.129 -4.019  1.00 12.42 ? 259 THR A N   1 
ATOM   2149  C  CA  . THR A 1 259 ? 21.826  -13.085 -2.998  1.00 13.01 ? 259 THR A CA  1 
ATOM   2150  C  C   . THR A 1 259 ? 23.000  -13.884 -3.510  1.00 11.35 ? 259 THR A C   1 
ATOM   2151  O  O   . THR A 1 259 ? 23.087  -14.210 -4.752  1.00 12.84 ? 259 THR A O   1 
ATOM   2152  C  CB  . THR A 1 259 ? 20.650  -14.074 -2.584  1.00 11.75 ? 259 THR A CB  1 
ATOM   2153  O  OG1 . THR A 1 259 ? 20.137  -14.706 -3.760  1.00 16.43 ? 259 THR A OG1 1 
ATOM   2154  C  CG2 . THR A 1 259 ? 19.561  -13.338 -1.924  1.00 12.13 ? 259 THR A CG2 1 
ATOM   2155  N  N   . SER A 1 260 ? 23.923  -14.177 -2.611  1.00 11.42 ? 260 SER A N   1 
ATOM   2156  C  CA  . SER A 1 260 ? 25.043  -14.992 -2.995  1.00 13.43 ? 260 SER A CA  1 
ATOM   2157  C  C   . SER A 1 260 ? 24.698  -16.455 -2.957  1.00 14.84 ? 260 SER A C   1 
ATOM   2158  O  O   . SER A 1 260 ? 25.636  -17.287 -3.253  1.00 17.74 ? 260 SER A O   1 
ATOM   2159  C  CB  . SER A 1 260 ? 26.242  -14.698 -2.176  1.00 13.93 ? 260 SER A CB  1 
ATOM   2160  O  OG  . SER A 1 260 ? 25.965  -15.089 -0.842  1.00 13.37 ? 260 SER A OG  1 
ATOM   2161  N  N   . PHE A 1 261 ? 23.481  -16.790 -2.619  1.00 14.78 ? 261 PHE A N   1 
ATOM   2162  C  CA  . PHE A 1 261 ? 23.114  -18.177 -2.452  1.00 18.33 ? 261 PHE A CA  1 
ATOM   2163  C  C   . PHE A 1 261 ? 21.876  -18.355 -3.294  1.00 19.51 ? 261 PHE A C   1 
ATOM   2164  O  O   . PHE A 1 261 ? 21.089  -17.435 -3.481  1.00 20.68 ? 261 PHE A O   1 
ATOM   2165  C  CB  . PHE A 1 261 ? 22.870  -18.479 -0.972  1.00 16.18 ? 261 PHE A CB  1 
ATOM   2166  C  CG  . PHE A 1 261 ? 21.892  -17.527 -0.328  1.00 16.07 ? 261 PHE A CG  1 
ATOM   2167  C  CD1 . PHE A 1 261 ? 20.512  -17.759 -0.290  1.00 14.91 ? 261 PHE A CD1 1 
ATOM   2168  C  CD2 . PHE A 1 261 ? 22.363  -16.327 0.214   1.00 12.57 ? 261 PHE A CD2 1 
ATOM   2169  C  CE1 . PHE A 1 261 ? 19.630  -16.885 0.317   1.00 15.18 ? 261 PHE A CE1 1 
ATOM   2170  C  CE2 . PHE A 1 261 ? 21.500  -15.396 0.811   1.00 14.38 ? 261 PHE A CE2 1 
ATOM   2171  C  CZ  . PHE A 1 261 ? 20.107  -15.651 0.852   1.00 14.31 ? 261 PHE A CZ  1 
ATOM   2172  N  N   . SER A 1 262 ? 21.727  -19.512 -3.897  1.00 26.21 ? 262 SER A N   1 
ATOM   2173  C  CA  . SER A 1 262 ? 20.391  -19.745 -4.458  1.00 30.94 ? 262 SER A CA  1 
ATOM   2174  C  C   . SER A 1 262 ? 19.726  -20.706 -3.502  1.00 34.29 ? 262 SER A C   1 
ATOM   2175  O  O   . SER A 1 262 ? 18.689  -20.400 -2.894  1.00 35.86 ? 262 SER A O   1 
ATOM   2176  C  CB  . SER A 1 262 ? 20.470  -20.323 -5.861  1.00 31.54 ? 262 SER A CB  1 
ATOM   2177  O  OG  . SER A 1 262 ? 21.434  -21.340 -5.879  1.00 35.46 ? 262 SER A OG  1 
ATOM   2178  N  N   . GLN A 1 263 ? 20.396  -21.837 -3.317  1.00 38.11 ? 263 GLN A N   1 
ATOM   2179  C  CA  . GLN A 1 263 ? 19.885  -22.898 -2.459  1.00 40.84 ? 263 GLN A CA  1 
ATOM   2180  C  C   . GLN A 1 263 ? 20.037  -22.439 -0.967  1.00 42.45 ? 263 GLN A C   1 
ATOM   2181  O  O   . GLN A 1 263 ? 19.009  -22.301 -0.261  1.00 43.78 ? 263 GLN A O   1 
ATOM   2182  C  CB  . GLN A 1 263 ? 20.522  -24.276 -2.830  1.00 40.21 ? 263 GLN A CB  1 
ATOM   2183  C  CG  . GLN A 1 263 ? 21.883  -24.647 -2.191  1.00 38.82 ? 263 GLN A CG  1 
ATOM   2184  C  CD  . GLN A 1 263 ? 22.421  -26.021 -2.665  1.00 40.61 ? 263 GLN A CD  1 
ATOM   2185  O  OE1 . GLN A 1 263 ? 23.597  -26.357 -2.415  1.00 37.48 ? 263 GLN A OE1 1 
ATOM   2186  N  NE2 . GLN A 1 263 ? 21.564  -26.818 -3.350  1.00 28.04 ? 263 GLN A NE2 1 
ATOM   2187  O  OXT . GLN A 1 263 ? 21.157  -22.133 -0.467  1.00 42.24 ? 263 GLN A OXT 1 
ATOM   2188  N  N   . LYS B 1 3   ? -1.752  17.375  -1.650  1.00 26.70 ? 3   LYS B N   1 
ATOM   2189  C  CA  . LYS B 1 3   ? -0.704  16.887  -2.697  1.00 26.05 ? 3   LYS B CA  1 
ATOM   2190  C  C   . LYS B 1 3   ? 0.293   15.834  -2.207  1.00 22.19 ? 3   LYS B C   1 
ATOM   2191  O  O   . LYS B 1 3   ? 1.264   15.466  -2.921  1.00 22.70 ? 3   LYS B O   1 
ATOM   2192  C  CB  . LYS B 1 3   ? 0.123   17.986  -3.333  1.00 28.76 ? 3   LYS B CB  1 
ATOM   2193  C  CG  . LYS B 1 3   ? 1.366   18.463  -2.572  1.00 34.05 ? 3   LYS B CG  1 
ATOM   2194  C  CD  . LYS B 1 3   ? 1.642   19.973  -2.956  1.00 40.55 ? 3   LYS B CD  1 
ATOM   2195  C  CE  . LYS B 1 3   ? 2.698   20.081  -4.050  1.00 41.29 ? 3   LYS B CE  1 
ATOM   2196  N  NZ  . LYS B 1 3   ? 2.992   21.476  -4.534  1.00 42.41 ? 3   LYS B NZ  1 
ATOM   2197  N  N   . TRP B 1 4   ? 0.102   15.392  -0.969  1.00 15.98 ? 4   TRP B N   1 
ATOM   2198  C  CA  . TRP B 1 4   ? 0.800   14.260  -0.446  1.00 12.91 ? 4   TRP B CA  1 
ATOM   2199  C  C   . TRP B 1 4   ? 0.527   13.068  -1.332  1.00 11.72 ? 4   TRP B C   1 
ATOM   2200  O  O   . TRP B 1 4   ? -0.481  12.959  -2.086  1.00 12.81 ? 4   TRP B O   1 
ATOM   2201  C  CB  . TRP B 1 4   ? 0.296   14.032  0.984   1.00 12.03 ? 4   TRP B CB  1 
ATOM   2202  C  CG  . TRP B 1 4   ? -1.216  13.696  1.167   1.00 10.25 ? 4   TRP B CG  1 
ATOM   2203  C  CD1 . TRP B 1 4   ? -2.277  14.549  1.472   1.00 12.41 ? 4   TRP B CD1 1 
ATOM   2204  C  CD2 . TRP B 1 4   ? -1.836  12.380  1.169   1.00 8.36  ? 4   TRP B CD2 1 
ATOM   2205  N  NE1 . TRP B 1 4   ? -3.465  13.861  1.610   1.00 10.82 ? 4   TRP B NE1 1 
ATOM   2206  C  CE2 . TRP B 1 4   ? -3.216  12.534  1.440   1.00 10.34 ? 4   TRP B CE2 1 
ATOM   2207  C  CE3 . TRP B 1 4   ? -1.343  11.052  0.967   1.00 9.37  ? 4   TRP B CE3 1 
ATOM   2208  C  CZ2 . TRP B 1 4   ? -4.096  11.458  1.567   1.00 9.83  ? 4   TRP B CZ2 1 
ATOM   2209  C  CZ3 . TRP B 1 4   ? -2.208  10.017  1.058   1.00 9.58  ? 4   TRP B CZ3 1 
ATOM   2210  C  CH2 . TRP B 1 4   ? -3.551  10.187  1.366   1.00 10.30 ? 4   TRP B CH2 1 
ATOM   2211  N  N   . THR B 1 5   ? 1.479   12.130  -1.279  1.00 10.27 ? 5   THR B N   1 
ATOM   2212  C  CA  . THR B 1 5   ? 1.377   10.938  -2.137  1.00 9.41  ? 5   THR B CA  1 
ATOM   2213  C  C   . THR B 1 5   ? 1.851   9.687   -1.308  1.00 10.32 ? 5   THR B C   1 
ATOM   2214  O  O   . THR B 1 5   ? 2.228   9.827   -0.131  1.00 9.34  ? 5   THR B O   1 
ATOM   2215  C  CB  . THR B 1 5   ? 2.242   11.054  -3.356  1.00 9.46  ? 5   THR B CB  1 
ATOM   2216  O  OG1 . THR B 1 5   ? 3.602   10.985  -2.895  1.00 12.19 ? 5   THR B OG1 1 
ATOM   2217  C  CG2 . THR B 1 5   ? 1.969   12.403  -4.140  1.00 11.51 ? 5   THR B CG2 1 
ATOM   2218  N  N   . TYR B 1 6   ? 1.948   8.564   -1.974  1.00 9.71  ? 6   TYR B N   1 
ATOM   2219  C  CA  . TYR B 1 6   ? 2.579   7.405   -1.366  1.00 9.60  ? 6   TYR B CA  1 
ATOM   2220  C  C   . TYR B 1 6   ? 3.978   7.043   -1.935  1.00 10.14 ? 6   TYR B C   1 
ATOM   2221  O  O   . TYR B 1 6   ? 4.521   5.991   -1.628  1.00 10.46 ? 6   TYR B O   1 
ATOM   2222  C  CB  . TYR B 1 6   ? 1.672   6.204   -1.525  1.00 8.71  ? 6   TYR B CB  1 
ATOM   2223  C  CG  . TYR B 1 6   ? 0.433   6.238   -0.663  1.00 8.79  ? 6   TYR B CG  1 
ATOM   2224  C  CD1 . TYR B 1 6   ? 0.447   5.716   0.619   1.00 7.23  ? 6   TYR B CD1 1 
ATOM   2225  C  CD2 . TYR B 1 6   ? -0.755  6.778   -1.138  1.00 6.97  ? 6   TYR B CD2 1 
ATOM   2226  C  CE1 . TYR B 1 6   ? -0.686  5.733   1.410   1.00 6.53  ? 6   TYR B CE1 1 
ATOM   2227  C  CE2 . TYR B 1 6   ? -1.892  6.805   -0.353  1.00 7.39  ? 6   TYR B CE2 1 
ATOM   2228  C  CZ  . TYR B 1 6   ? -1.857  6.278   0.917   1.00 6.32  ? 6   TYR B CZ  1 
ATOM   2229  O  OH  . TYR B 1 6   ? -2.998  6.306   1.684   1.00 7.07  ? 6   TYR B OH  1 
ATOM   2230  N  N   . PHE B 1 7   ? 4.497   7.921   -2.804  1.00 11.90 ? 7   PHE B N   1 
ATOM   2231  C  CA  . PHE B 1 7   ? 5.658   7.557   -3.584  1.00 12.34 ? 7   PHE B CA  1 
ATOM   2232  C  C   . PHE B 1 7   ? 6.393   8.841   -3.926  1.00 13.99 ? 7   PHE B C   1 
ATOM   2233  O  O   . PHE B 1 7   ? 5.818   9.709   -4.516  1.00 13.73 ? 7   PHE B O   1 
ATOM   2234  C  CB  . PHE B 1 7   ? 5.304   6.834   -4.929  1.00 16.09 ? 7   PHE B CB  1 
ATOM   2235  C  CG  . PHE B 1 7   ? 6.513   6.471   -5.656  1.00 17.99 ? 7   PHE B CG  1 
ATOM   2236  C  CD1 . PHE B 1 7   ? 7.451   5.567   -5.149  1.00 20.51 ? 7   PHE B CD1 1 
ATOM   2237  C  CD2 . PHE B 1 7   ? 6.811   7.145   -6.874  1.00 24.40 ? 7   PHE B CD2 1 
ATOM   2238  C  CE1 . PHE B 1 7   ? 8.655   5.268   -5.839  1.00 27.83 ? 7   PHE B CE1 1 
ATOM   2239  C  CE2 . PHE B 1 7   ? 7.990   6.871   -7.579  1.00 27.21 ? 7   PHE B CE2 1 
ATOM   2240  C  CZ  . PHE B 1 7   ? 8.896   5.955   -7.084  1.00 26.17 ? 7   PHE B CZ  1 
ATOM   2241  N  N   . GLY B 1 8   ? 7.677   8.884   -3.605  1.00 14.07 ? 8   GLY B N   1 
ATOM   2242  C  CA  . GLY B 1 8   ? 8.483   10.068  -4.055  1.00 15.77 ? 8   GLY B CA  1 
ATOM   2243  C  C   . GLY B 1 8   ? 8.600   11.136  -2.981  1.00 16.98 ? 8   GLY B C   1 
ATOM   2244  O  O   . GLY B 1 8   ? 8.467   10.891  -1.758  1.00 15.67 ? 8   GLY B O   1 
ATOM   2245  N  N   . PRO B 1 9   ? 8.932   12.384  -3.383  1.00 18.33 ? 9   PRO B N   1 
ATOM   2246  C  CA  . PRO B 1 9   ? 9.212   13.391  -2.400  1.00 17.90 ? 9   PRO B CA  1 
ATOM   2247  C  C   . PRO B 1 9   ? 8.176   13.728  -1.445  1.00 16.86 ? 9   PRO B C   1 
ATOM   2248  O  O   . PRO B 1 9   ? 8.489   14.250  -0.423  1.00 18.63 ? 9   PRO B O   1 
ATOM   2249  C  CB  . PRO B 1 9   ? 9.542   14.645  -3.227  1.00 19.54 ? 9   PRO B CB  1 
ATOM   2250  C  CG  . PRO B 1 9   ? 10.047  14.037  -4.462  1.00 19.67 ? 9   PRO B CG  1 
ATOM   2251  C  CD  . PRO B 1 9   ? 9.228   12.850  -4.731  1.00 20.83 ? 9   PRO B CD  1 
ATOM   2252  N  N   . ASP B 1 10  ? 6.896   13.527  -1.839  1.00 14.39 ? 10  ASP B N   1 
ATOM   2253  C  CA  . ASP B 1 10  ? 5.767   13.857  -1.082  1.00 14.37 ? 10  ASP B CA  1 
ATOM   2254  C  C   . ASP B 1 10  ? 5.147   12.603  -0.385  1.00 10.08 ? 10  ASP B C   1 
ATOM   2255  O  O   . ASP B 1 10  ? 4.060   12.716  0.155   1.00 11.30 ? 10  ASP B O   1 
ATOM   2256  C  CB  . ASP B 1 10  ? 4.752   14.586  -1.930  1.00 15.50 ? 10  ASP B CB  1 
ATOM   2257  C  CG  . ASP B 1 10  ? 5.309   15.931  -2.450  1.00 18.20 ? 10  ASP B CG  1 
ATOM   2258  O  OD1 . ASP B 1 10  ? 6.017   16.623  -1.711  1.00 24.35 ? 10  ASP B OD1 1 
ATOM   2259  O  OD2 . ASP B 1 10  ? 5.149   16.198  -3.622  1.00 21.46 ? 10  ASP B OD2 1 
ATOM   2260  N  N   . GLY B 1 11  ? 5.962   11.540  -0.390  1.00 10.76 ? 11  GLY B N   1 
ATOM   2261  C  CA  . GLY B 1 11  ? 5.527   10.229  0.220   1.00 8.62  ? 11  GLY B CA  1 
ATOM   2262  C  C   . GLY B 1 11  ? 5.638   10.298  1.734   1.00 8.68  ? 11  GLY B C   1 
ATOM   2263  O  O   . GLY B 1 11  ? 5.777   11.288  2.404   1.00 8.72  ? 11  GLY B O   1 
ATOM   2264  N  N   . GLU B 1 12  ? 5.359   9.126   2.310   1.00 7.58  ? 12  GLU B N   1 
ATOM   2265  C  CA  . GLU B 1 12  ? 4.911   9.071   3.709   1.00 7.25  ? 12  GLU B CA  1 
ATOM   2266  C  C   . GLU B 1 12  ? 5.942   9.540   4.746   1.00 6.02  ? 12  GLU B C   1 
ATOM   2267  O  O   . GLU B 1 12  ? 5.610   9.949   5.824   1.00 7.81  ? 12  GLU B O   1 
ATOM   2268  C  CB  . GLU B 1 12  ? 4.478   7.611   4.109   1.00 8.06  ? 12  GLU B CB  1 
ATOM   2269  C  CG  . GLU B 1 12  ? 5.591   6.572   4.130   1.00 7.47  ? 12  GLU B CG  1 
ATOM   2270  C  CD  . GLU B 1 12  ? 4.964   5.158   4.131   1.00 6.29  ? 12  GLU B CD  1 
ATOM   2271  O  OE1 . GLU B 1 12  ? 4.600   4.702   5.210   1.00 7.38  ? 12  GLU B OE1 1 
ATOM   2272  O  OE2 . GLU B 1 12  ? 4.863   4.642   3.006   1.00 7.78  ? 12  GLU B OE2 1 
ATOM   2273  N  N   . ASN B 1 13  ? 7.241   9.430   4.403   1.00 8.01  ? 13  ASN B N   1 
ATOM   2274  C  CA  . ASN B 1 13  ? 8.253   9.891   5.363   1.00 6.68  ? 13  ASN B CA  1 
ATOM   2275  C  C   . ASN B 1 13  ? 8.302   11.455  5.439   1.00 7.77  ? 13  ASN B C   1 
ATOM   2276  O  O   . ASN B 1 13  ? 8.873   12.013  6.396   1.00 8.56  ? 13  ASN B O   1 
ATOM   2277  C  CB  . ASN B 1 13  ? 9.678   9.378   5.009   1.00 6.04  ? 13  ASN B CB  1 
ATOM   2278  C  CG  . ASN B 1 13  ? 9.823   7.891   5.236   1.00 7.88  ? 13  ASN B CG  1 
ATOM   2279  O  OD1 . ASN B 1 13  ? 8.901   7.231   5.823   1.00 7.86  ? 13  ASN B OD1 1 
ATOM   2280  N  ND2 . ASN B 1 13  ? 10.991  7.390   4.900   1.00 9.57  ? 13  ASN B ND2 1 
ATOM   2281  N  N   . SER B 1 14  ? 7.593   12.036  4.487   1.00 7.09  ? 14  SER B N   1 
ATOM   2282  C  CA  . SER B 1 14  ? 7.512   13.567  4.437   1.00 7.70  ? 14  SER B CA  1 
ATOM   2283  C  C   . SER B 1 14  ? 6.194   14.111  4.870   1.00 8.92  ? 14  SER B C   1 
ATOM   2284  O  O   . SER B 1 14  ? 6.014   15.329  5.006   1.00 9.72  ? 14  SER B O   1 
ATOM   2285  C  CB  . SER B 1 14  ? 7.782   14.026  3.009   1.00 8.59  ? 14  SER B CB  1 
ATOM   2286  O  OG  . SER B 1 14  ? 9.118   13.740  2.669   1.00 9.60  ? 14  SER B OG  1 
ATOM   2287  N  N   . TRP B 1 15  ? 5.195   13.274  5.120   1.00 7.91  ? 15  TRP B N   1 
ATOM   2288  C  CA  . TRP B 1 15  ? 3.839   13.823  5.456   1.00 7.60  ? 15  TRP B CA  1 
ATOM   2289  C  C   . TRP B 1 15  ? 3.901   14.618  6.692   1.00 8.36  ? 15  TRP B C   1 
ATOM   2290  O  O   . TRP B 1 15  ? 3.202   15.688  6.725   1.00 9.23  ? 15  TRP B O   1 
ATOM   2291  C  CB  . TRP B 1 15  ? 2.878   12.668  5.804   1.00 9.24  ? 15  TRP B CB  1 
ATOM   2292  C  CG  . TRP B 1 15  ? 2.473   11.828  4.643   1.00 7.23  ? 15  TRP B CG  1 
ATOM   2293  C  CD1 . TRP B 1 15  ? 2.756   11.981  3.315   1.00 8.01  ? 15  TRP B CD1 1 
ATOM   2294  C  CD2 . TRP B 1 15  ? 1.710   10.544  4.764   1.00 7.19  ? 15  TRP B CD2 1 
ATOM   2295  N  NE1 . TRP B 1 15  ? 2.153   10.913  2.564   1.00 8.29  ? 15  TRP B NE1 1 
ATOM   2296  C  CE2 . TRP B 1 15  ? 1.572   10.027  3.452   1.00 7.51  ? 15  TRP B CE2 1 
ATOM   2297  C  CE3 . TRP B 1 15  ? 1.152   9.831   5.821   1.00 6.91  ? 15  TRP B CE3 1 
ATOM   2298  C  CZ2 . TRP B 1 15  ? 0.829   8.842   3.164   1.00 7.54  ? 15  TRP B CZ2 1 
ATOM   2299  C  CZ3 . TRP B 1 15  ? 0.408   8.670   5.562   1.00 7.32  ? 15  TRP B CZ3 1 
ATOM   2300  C  CH2 . TRP B 1 15  ? 0.300   8.195   4.244   1.00 7.74  ? 15  TRP B CH2 1 
ATOM   2301  N  N   . SER B 1 16  ? 4.758   14.342  7.657   1.00 8.20  ? 16  SER B N   1 
ATOM   2302  C  CA  . SER B 1 16  ? 4.828   15.151  8.913   1.00 9.82  ? 16  SER B CA  1 
ATOM   2303  C  C   . SER B 1 16  ? 5.307   16.631  8.678   1.00 10.30 ? 16  SER B C   1 
ATOM   2304  O  O   . SER B 1 16  ? 5.087   17.425  9.583   1.00 11.70 ? 16  SER B O   1 
ATOM   2305  C  CB  . SER B 1 16  ? 5.822   14.492  9.909   1.00 10.60 ? 16  SER B CB  1 
ATOM   2306  O  OG  . SER B 1 16  ? 7.107   14.623  9.342   1.00 13.15 ? 16  SER B OG  1 
ATOM   2307  N  N   . LYS B 1 17  ? 5.915   16.878  7.538   1.00 8.99  ? 17  LYS B N   1 
ATOM   2308  C  CA  . LYS B 1 17  ? 6.405   18.254  7.240   1.00 9.87  ? 17  LYS B CA  1 
ATOM   2309  C  C   . LYS B 1 17  ? 5.183   19.130  7.135   1.00 10.57 ? 17  LYS B C   1 
ATOM   2310  O  O   . LYS B 1 17  ? 5.325   20.385  7.472   1.00 11.56 ? 17  LYS B O   1 
ATOM   2311  C  CB  . LYS B 1 17  ? 7.134   18.307  5.934   1.00 8.75  ? 17  LYS B CB  1 
ATOM   2312  C  CG  . LYS B 1 17  ? 8.463   17.477  5.866   1.00 12.48 ? 17  LYS B CG  1 
ATOM   2313  C  CD  . LYS B 1 17  ? 9.035   17.517  4.492   1.00 8.39  ? 17  LYS B CD  1 
ATOM   2314  C  CE  . LYS B 1 17  ? 10.257  16.562  4.310   1.00 9.59  ? 17  LYS B CE  1 
ATOM   2315  N  NZ  . LYS B 1 17  ? 10.814  16.648  3.019   1.00 9.61  ? 17  LYS B NZ  1 
ATOM   2316  N  N   . LYS B 1 18  ? 4.050   18.706  6.590   1.00 10.41 ? 18  LYS B N   1 
ATOM   2317  C  CA  . LYS B 1 18  ? 2.826   19.589  6.449   1.00 9.98  ? 18  LYS B CA  1 
ATOM   2318  C  C   . LYS B 1 18  ? 1.721   19.170  7.425   1.00 10.18 ? 18  LYS B C   1 
ATOM   2319  O  O   . LYS B 1 18  ? 0.799   19.953  7.642   1.00 13.17 ? 18  LYS B O   1 
ATOM   2320  C  CB  . LYS B 1 18  ? 2.242   19.382  5.107   1.00 12.61 ? 18  LYS B CB  1 
ATOM   2321  C  CG  . LYS B 1 18  ? 3.089   20.054  3.984   1.00 17.05 ? 18  LYS B CG  1 
ATOM   2322  C  CD  . LYS B 1 18  ? 2.738   19.722  2.473   1.00 18.70 ? 18  LYS B CD  1 
ATOM   2323  C  CE  . LYS B 1 18  ? 3.437   20.747  1.540   1.00 23.87 ? 18  LYS B CE  1 
ATOM   2324  N  NZ  . LYS B 1 18  ? 2.248   21.210  0.640   1.00 29.13 ? 18  LYS B NZ  1 
ATOM   2325  N  N   . TYR B 1 19  ? 1.795   17.908  7.987   1.00 8.83  ? 19  TYR B N   1 
ATOM   2326  C  CA  . TYR B 1 19  ? 0.679   17.366  8.776   1.00 10.80 ? 19  TYR B CA  1 
ATOM   2327  C  C   . TYR B 1 19  ? 1.303   16.893  10.045  1.00 10.48 ? 19  TYR B C   1 
ATOM   2328  O  O   . TYR B 1 19  ? 1.742   15.712  10.152  1.00 10.60 ? 19  TYR B O   1 
ATOM   2329  C  CB  . TYR B 1 19  ? 0.041   16.159  8.022   1.00 11.13 ? 19  TYR B CB  1 
ATOM   2330  C  CG  . TYR B 1 19  ? -0.556  16.610  6.676   1.00 8.95  ? 19  TYR B CG  1 
ATOM   2331  C  CD1 . TYR B 1 19  ? -1.810  17.268  6.699   1.00 10.71 ? 19  TYR B CD1 1 
ATOM   2332  C  CD2 . TYR B 1 19  ? 0.137   16.435  5.456   1.00 8.18  ? 19  TYR B CD2 1 
ATOM   2333  C  CE1 . TYR B 1 19  ? -2.404  17.640  5.497   1.00 11.40 ? 19  TYR B CE1 1 
ATOM   2334  C  CE2 . TYR B 1 19  ? -0.466  16.836  4.269   1.00 9.74  ? 19  TYR B CE2 1 
ATOM   2335  C  CZ  . TYR B 1 19  ? -1.740  17.483  4.325   1.00 12.72 ? 19  TYR B CZ  1 
ATOM   2336  O  OH  . TYR B 1 19  ? -2.301  17.871  3.095   1.00 15.92 ? 19  TYR B OH  1 
ATOM   2337  N  N   . PRO B 1 20  ? 1.440   17.720  11.089  1.00 10.80 ? 20  PRO B N   1 
ATOM   2338  C  CA  . PRO B 1 20  ? 2.214   17.353  12.235  1.00 12.13 ? 20  PRO B CA  1 
ATOM   2339  C  C   . PRO B 1 20  ? 1.779   16.035  12.902  1.00 10.75 ? 20  PRO B C   1 
ATOM   2340  O  O   . PRO B 1 20  ? 2.647   15.366  13.541  1.00 10.79 ? 20  PRO B O   1 
ATOM   2341  C  CB  . PRO B 1 20  ? 2.108   18.578  13.170  1.00 12.11 ? 20  PRO B CB  1 
ATOM   2342  C  CG  . PRO B 1 20  ? 1.641   19.681  12.237  1.00 14.59 ? 20  PRO B CG  1 
ATOM   2343  C  CD  . PRO B 1 20  ? 0.918   19.138  11.073  1.00 11.82 ? 20  PRO B CD  1 
ATOM   2344  N  N   . SER B 1 21  ? 0.452   15.753  12.904  1.00 9.72  ? 21  SER B N   1 
ATOM   2345  C  CA  . SER B 1 21  ? -0.009  14.552  13.652  1.00 8.32  ? 21  SER B CA  1 
ATOM   2346  C  C   . SER B 1 21  ? 0.584   13.311  13.011  1.00 9.02  ? 21  SER B C   1 
ATOM   2347  O  O   . SER B 1 21  ? 0.570   12.278  13.721  1.00 9.29  ? 21  SER B O   1 
ATOM   2348  C  CB  . SER B 1 21  ? -1.510  14.502  13.621  1.00 10.40 ? 21  SER B CB  1 
ATOM   2349  O  OG  . SER B 1 21  ? -2.024  15.509  14.513  1.00 13.44 ? 21  SER B OG  1 
ATOM   2350  N  N   . CYS B 1 22  ? 0.974   13.309  11.748  1.00 8.35  ? 22  CYS B N   1 
ATOM   2351  C  CA  . CYS B 1 22  ? 1.599   12.128  11.104  1.00 7.20  ? 22  CYS B CA  1 
ATOM   2352  C  C   . CYS B 1 22  ? 2.902   11.772  11.760  1.00 9.93  ? 22  CYS B C   1 
ATOM   2353  O  O   . CYS B 1 22  ? 3.359   10.661  11.542  1.00 9.80  ? 22  CYS B O   1 
ATOM   2354  C  CB  . CYS B 1 22  ? 1.775   12.380  9.614   1.00 9.66  ? 22  CYS B CB  1 
ATOM   2355  S  SG  . CYS B 1 22  ? 0.225   12.653  8.705   1.00 8.90  ? 22  CYS B SG  1 
ATOM   2356  N  N   . GLY B 1 23  ? 3.559   12.696  12.484  1.00 9.60  ? 23  GLY B N   1 
ATOM   2357  C  CA  . GLY B 1 23  ? 4.750   12.484  13.280  1.00 10.81 ? 23  GLY B CA  1 
ATOM   2358  C  C   . GLY B 1 23  ? 4.439   12.346  14.745  1.00 10.37 ? 23  GLY B C   1 
ATOM   2359  O  O   . GLY B 1 23  ? 5.367   12.323  15.604  1.00 14.33 ? 23  GLY B O   1 
ATOM   2360  N  N   . GLY B 1 24  ? 3.179   12.221  15.143  1.00 11.32 ? 24  GLY B N   1 
ATOM   2361  C  CA  . GLY B 1 24  ? 2.834   12.229  16.551  1.00 13.85 ? 24  GLY B CA  1 
ATOM   2362  C  C   . GLY B 1 24  ? 2.540   10.854  17.071  1.00 15.56 ? 24  GLY B C   1 
ATOM   2363  O  O   . GLY B 1 24  ? 3.013   9.870   16.490  1.00 16.98 ? 24  GLY B O   1 
ATOM   2364  N  N   . LEU B 1 25  ? 1.800   10.861  18.142  1.00 16.37 ? 25  LEU B N   1 
ATOM   2365  C  CA  . LEU B 1 25  ? 1.532   9.539   18.783  1.00 18.72 ? 25  LEU B CA  1 
ATOM   2366  C  C   . LEU B 1 25  ? 0.339   8.829   18.158  1.00 18.08 ? 25  LEU B C   1 
ATOM   2367  O  O   . LEU B 1 25  ? -0.440  9.438   17.399  1.00 14.44 ? 25  LEU B O   1 
ATOM   2368  C  CB  . LEU B 1 25  ? 1.313   9.740   20.329  1.00 21.43 ? 25  LEU B CB  1 
ATOM   2369  C  CG  . LEU B 1 25  ? 2.565   10.341  21.056  1.00 27.15 ? 25  LEU B CG  1 
ATOM   2370  C  CD1 . LEU B 1 25  ? 2.237   10.602  22.506  1.00 30.07 ? 25  LEU B CD1 1 
ATOM   2371  C  CD2 . LEU B 1 25  ? 3.712   9.476   20.946  1.00 26.92 ? 25  LEU B CD2 1 
ATOM   2372  N  N   . LEU B 1 26  ? 0.211   7.544   18.510  1.00 17.25 ? 26  LEU B N   1 
ATOM   2373  C  CA  . LEU B 1 26  ? -1.022  6.768   18.321  1.00 15.11 ? 26  LEU B CA  1 
ATOM   2374  C  C   . LEU B 1 26  ? -1.234  6.487   16.816  1.00 10.60 ? 26  LEU B C   1 
ATOM   2375  O  O   . LEU B 1 26  ? -2.388  6.401   16.361  1.00 11.37 ? 26  LEU B O   1 
ATOM   2376  C  CB  . LEU B 1 26  ? -2.271  7.474   18.889  1.00 15.60 ? 26  LEU B CB  1 
ATOM   2377  C  CG  . LEU B 1 26  ? -2.327  7.594   20.445  1.00 21.78 ? 26  LEU B CG  1 
ATOM   2378  C  CD1 . LEU B 1 26  ? -3.670  8.272   20.812  1.00 23.78 ? 26  LEU B CD1 1 
ATOM   2379  C  CD2 . LEU B 1 26  ? -2.143  6.206   21.119  1.00 25.58 ? 26  LEU B CD2 1 
ATOM   2380  N  N   . GLN B 1 27  ? -0.139  6.365   16.084  1.00 10.57 ? 27  GLN B N   1 
ATOM   2381  C  CA  . GLN B 1 27  ? -0.264  6.172   14.604  1.00 8.87  ? 27  GLN B CA  1 
ATOM   2382  C  C   . GLN B 1 27  ? -0.659  4.794   14.150  1.00 9.52  ? 27  GLN B C   1 
ATOM   2383  O  O   . GLN B 1 27  ? -0.214  3.781   14.727  1.00 10.20 ? 27  GLN B O   1 
ATOM   2384  C  CB  . GLN B 1 27  ? 0.961   6.671   13.812  1.00 6.86  ? 27  GLN B CB  1 
ATOM   2385  C  CG  . GLN B 1 27  ? 1.223   8.199   14.086  1.00 9.91  ? 27  GLN B CG  1 
ATOM   2386  C  CD  . GLN B 1 27  ? 0.159   9.025   13.434  1.00 8.32  ? 27  GLN B CD  1 
ATOM   2387  O  OE1 . GLN B 1 27  ? 0.210   9.143   12.192  1.00 9.72  ? 27  GLN B OE1 1 
ATOM   2388  N  NE2 . GLN B 1 27  ? -0.818  9.541   14.211  1.00 9.08  ? 27  GLN B NE2 1 
ATOM   2389  N  N   . SER B 1 28  ? -1.437  4.783   13.080  1.00 6.45  ? 28  SER B N   1 
ATOM   2390  C  CA  . SER B 1 28  ? -1.817  3.559   12.387  1.00 6.75  ? 28  SER B CA  1 
ATOM   2391  C  C   . SER B 1 28  ? -1.254  3.570   10.977  1.00 7.16  ? 28  SER B C   1 
ATOM   2392  O  O   . SER B 1 28  ? -0.993  4.608   10.398  1.00 7.12  ? 28  SER B O   1 
ATOM   2393  C  CB  . SER B 1 28  ? -3.333  3.521   12.307  1.00 7.79  ? 28  SER B CB  1 
ATOM   2394  O  OG  . SER B 1 28  ? -3.861  3.418   13.643  1.00 7.66  ? 28  SER B OG  1 
ATOM   2395  N  N   . PRO B 1 29  ? -1.130  2.431   10.297  1.00 5.82  ? 29  PRO B N   1 
ATOM   2396  C  CA  . PRO B 1 29  ? -1.461  1.015   10.761  1.00 6.35  ? 29  PRO B CA  1 
ATOM   2397  C  C   . PRO B 1 29  ? -0.328  0.450   11.576  1.00 5.93  ? 29  PRO B C   1 
ATOM   2398  O  O   . PRO B 1 29  ? 0.724   1.052   11.768  1.00 7.22  ? 29  PRO B O   1 
ATOM   2399  C  CB  . PRO B 1 29  ? -1.692  0.324   9.406   1.00 8.08  ? 29  PRO B CB  1 
ATOM   2400  C  CG  . PRO B 1 29  ? -0.545  0.854   8.623   1.00 6.36  ? 29  PRO B CG  1 
ATOM   2401  C  CD  . PRO B 1 29  ? -0.658  2.373   8.884   1.00 6.40  ? 29  PRO B CD  1 
ATOM   2402  N  N   . ILE B 1 30  ? -0.600  -0.781  12.048  1.00 6.66  ? 30  ILE B N   1 
ATOM   2403  C  CA  . ILE B 1 30  ? 0.427   -1.509  12.867  1.00 6.79  ? 30  ILE B CA  1 
ATOM   2404  C  C   . ILE B 1 30  ? 0.427   -2.988  12.454  1.00 6.76  ? 30  ILE B C   1 
ATOM   2405  O  O   . ILE B 1 30  ? -0.431  -3.440  11.740  1.00 7.02  ? 30  ILE B O   1 
ATOM   2406  C  CB  . ILE B 1 30  ? 0.112   -1.434  14.419  1.00 7.02  ? 30  ILE B CB  1 
ATOM   2407  C  CG1 . ILE B 1 30  ? -1.313  -1.912  14.699  1.00 8.61  ? 30  ILE B CG1 1 
ATOM   2408  C  CG2 . ILE B 1 30  ? 0.270   0.061   14.813  1.00 8.47  ? 30  ILE B CG2 1 
ATOM   2409  C  CD1 . ILE B 1 30  ? -1.556  -2.061  16.180  1.00 9.40  ? 30  ILE B CD1 1 
ATOM   2410  N  N   . ASP B 1 31  ? 1.518   -3.615  12.916  1.00 6.29  ? 31  ASP B N   1 
ATOM   2411  C  CA  . ASP B 1 31  ? 1.670   -5.048  12.734  1.00 6.44  ? 31  ASP B CA  1 
ATOM   2412  C  C   . ASP B 1 31  ? 1.010   -5.728  13.961  1.00 8.88  ? 31  ASP B C   1 
ATOM   2413  O  O   . ASP B 1 31  ? 1.419   -5.527  15.056  1.00 9.61  ? 31  ASP B O   1 
ATOM   2414  C  CB  . ASP B 1 31  ? 3.148   -5.501  12.641  1.00 7.14  ? 31  ASP B CB  1 
ATOM   2415  C  CG  . ASP B 1 31  ? 3.306   -6.988  12.509  1.00 10.51 ? 31  ASP B CG  1 
ATOM   2416  O  OD1 . ASP B 1 31  ? 2.726   -7.576  11.572  1.00 9.89  ? 31  ASP B OD1 1 
ATOM   2417  O  OD2 . ASP B 1 31  ? 4.023   -7.563  13.348  1.00 13.45 ? 31  ASP B OD2 1 
ATOM   2418  N  N   . LEU B 1 32  ? 0.065   -6.595  13.619  1.00 8.27  ? 32  LEU B N   1 
ATOM   2419  C  CA  . LEU B 1 32  ? -0.638  -7.383  14.697  1.00 8.04  ? 32  LEU B CA  1 
ATOM   2420  C  C   . LEU B 1 32  ? 0.160   -8.673  14.960  1.00 9.87  ? 32  LEU B C   1 
ATOM   2421  O  O   . LEU B 1 32  ? 0.184   -9.490  14.084  1.00 10.71 ? 32  LEU B O   1 
ATOM   2422  C  CB  . LEU B 1 32  ? -2.055  -7.652  14.192  1.00 8.47  ? 32  LEU B CB  1 
ATOM   2423  C  CG  . LEU B 1 32  ? -2.823  -6.359  13.808  1.00 8.56  ? 32  LEU B CG  1 
ATOM   2424  C  CD1 . LEU B 1 32  ? -4.161  -6.693  13.067  1.00 12.63 ? 32  LEU B CD1 1 
ATOM   2425  C  CD2 . LEU B 1 32  ? -3.063  -5.529  15.010  1.00 12.54 ? 32  LEU B CD2 1 
ATOM   2426  N  N   . HIS B 1 33  ? 0.846   -8.706  16.106  1.00 9.33  ? 33  HIS B N   1 
ATOM   2427  C  CA  . HIS B 1 33  ? 1.707   -9.848  16.423  1.00 9.85  ? 33  HIS B CA  1 
ATOM   2428  C  C   . HIS B 1 33  ? 1.591   -10.148 17.909  1.00 8.53  ? 33  HIS B C   1 
ATOM   2429  O  O   . HIS B 1 33  ? 1.258   -9.351  18.706  1.00 10.30 ? 33  HIS B O   1 
ATOM   2430  C  CB  . HIS B 1 33  ? 3.193   -9.594  16.002  1.00 10.24 ? 33  HIS B CB  1 
ATOM   2431  C  CG  . HIS B 1 33  ? 3.829   -8.393  16.704  1.00 10.69 ? 33  HIS B CG  1 
ATOM   2432  N  ND1 . HIS B 1 33  ? 3.498   -7.083  16.431  1.00 14.36 ? 33  HIS B ND1 1 
ATOM   2433  C  CD2 . HIS B 1 33  ? 4.748   -8.334  17.723  1.00 9.26  ? 33  HIS B CD2 1 
ATOM   2434  C  CE1 . HIS B 1 33  ? 4.188   -6.277  17.257  1.00 17.26 ? 33  HIS B CE1 1 
ATOM   2435  N  NE2 . HIS B 1 33  ? 4.994   -7.016  17.998  1.00 12.53 ? 33  HIS B NE2 1 
ATOM   2436  N  N   . SER B 1 34  ? 1.962   -11.429 18.197  1.00 11.57 ? 34  SER B N   1 
ATOM   2437  C  CA  . SER B 1 34  ? 1.619   -11.983 19.524  1.00 12.04 ? 34  SER B CA  1 
ATOM   2438  C  C   . SER B 1 34  ? 2.101   -11.141 20.667  1.00 11.42 ? 34  SER B C   1 
ATOM   2439  O  O   . SER B 1 34  ? 1.377   -11.039 21.680  1.00 12.86 ? 34  SER B O   1 
ATOM   2440  C  CB  . SER B 1 34  ? 2.184   -13.413 19.686  1.00 14.34 ? 34  SER B CB  1 
ATOM   2441  O  OG  . SER B 1 34  ? 3.615   -13.464 19.563  1.00 17.20 ? 34  SER B OG  1 
ATOM   2442  N  N   . ASP B 1 35  ? 3.292   -10.517 20.598  1.00 9.96  ? 35  ASP B N   1 
ATOM   2443  C  CA  . ASP B 1 35  ? 3.805   -9.870  21.804  1.00 12.70 ? 35  ASP B CA  1 
ATOM   2444  C  C   . ASP B 1 35  ? 2.968   -8.730  22.302  1.00 13.10 ? 35  ASP B C   1 
ATOM   2445  O  O   . ASP B 1 35  ? 3.128   -8.198  23.438  1.00 16.04 ? 35  ASP B O   1 
ATOM   2446  C  CB  . ASP B 1 35  ? 5.266   -9.313  21.529  1.00 13.63 ? 35  ASP B CB  1 
ATOM   2447  C  CG  . ASP B 1 35  ? 6.157   -10.336 20.929  1.00 15.05 ? 35  ASP B CG  1 
ATOM   2448  O  OD1 . ASP B 1 35  ? 5.927   -10.754 19.791  1.00 14.87 ? 35  ASP B OD1 1 
ATOM   2449  O  OD2 . ASP B 1 35  ? 7.169   -10.679 21.625  1.00 14.87 ? 35  ASP B OD2 1 
ATOM   2450  N  N   . ILE B 1 36  ? 2.124   -8.203  21.418  1.00 11.69 ? 36  ILE B N   1 
ATOM   2451  C  CA  . ILE B 1 36  ? 1.393   -7.008  21.779  1.00 12.77 ? 36  ILE B CA  1 
ATOM   2452  C  C   . ILE B 1 36  ? -0.142  -7.230  21.865  1.00 11.32 ? 36  ILE B C   1 
ATOM   2453  O  O   . ILE B 1 36  ? -0.893  -6.262  22.050  1.00 12.54 ? 36  ILE B O   1 
ATOM   2454  C  CB  . ILE B 1 36  ? 1.692   -5.716  20.941  1.00 13.61 ? 36  ILE B CB  1 
ATOM   2455  C  CG1 . ILE B 1 36  ? 1.586   -5.964  19.460  1.00 18.67 ? 36  ILE B CG1 1 
ATOM   2456  C  CG2 . ILE B 1 36  ? 3.101   -5.199  21.227  1.00 16.83 ? 36  ILE B CG2 1 
ATOM   2457  C  CD1 . ILE B 1 36  ? 0.294   -6.121  18.918  1.00 20.75 ? 36  ILE B CD1 1 
ATOM   2458  N  N   . LEU B 1 37  ? -0.507  -8.494  21.732  1.00 11.12 ? 37  LEU B N   1 
ATOM   2459  C  CA  . LEU B 1 37  ? -2.020  -8.899  21.713  1.00 12.22 ? 37  LEU B CA  1 
ATOM   2460  C  C   . LEU B 1 37  ? -2.381  -9.301  23.123  1.00 14.72 ? 37  LEU B C   1 
ATOM   2461  O  O   . LEU B 1 37  ? -1.561  -9.922  23.819  1.00 17.02 ? 37  LEU B O   1 
ATOM   2462  C  CB  . LEU B 1 37  ? -2.240  -10.096 20.825  1.00 11.56 ? 37  LEU B CB  1 
ATOM   2463  C  CG  . LEU B 1 37  ? -1.966  -9.932  19.326  1.00 13.61 ? 37  LEU B CG  1 
ATOM   2464  C  CD1 . LEU B 1 37  ? -2.194  -11.093 18.451  1.00 16.49 ? 37  LEU B CD1 1 
ATOM   2465  C  CD2 . LEU B 1 37  ? -2.725  -8.709  18.809  1.00 13.07 ? 37  LEU B CD2 1 
ATOM   2466  N  N   . GLN B 1 38  ? -3.588  -8.971  23.534  1.00 11.48 ? 38  GLN B N   1 
ATOM   2467  C  CA  . GLN B 1 38  ? -4.075  -9.443  24.881  1.00 14.03 ? 38  GLN B CA  1 
ATOM   2468  C  C   . GLN B 1 38  ? -5.577  -9.607  24.745  1.00 13.23 ? 38  GLN B C   1 
ATOM   2469  O  O   . GLN B 1 38  ? -6.331  -8.725  24.324  1.00 12.69 ? 38  GLN B O   1 
ATOM   2470  C  CB  . GLN B 1 38  ? -3.867  -8.436  25.876  1.00 15.12 ? 38  GLN B CB  1 
ATOM   2471  C  CG  . GLN B 1 38  ? -4.226  -8.936  27.349  1.00 18.11 ? 38  GLN B CG  1 
ATOM   2472  C  CD  . GLN B 1 38  ? -3.790  -7.894  28.318  1.00 22.65 ? 38  GLN B CD  1 
ATOM   2473  O  OE1 . GLN B 1 38  ? -2.584  -7.809  28.592  1.00 34.29 ? 38  GLN B OE1 1 
ATOM   2474  N  NE2 . GLN B 1 38  ? -4.675  -7.077  28.783  1.00 26.01 ? 38  GLN B NE2 1 
ATOM   2475  N  N   . TYR B 1 39  ? -6.017  -10.783 25.129  1.00 12.68 ? 39  TYR B N   1 
ATOM   2476  C  CA  . TYR B 1 39  ? -7.461  -11.052 25.056  1.00 11.72 ? 39  TYR B CA  1 
ATOM   2477  C  C   . TYR B 1 39  ? -8.199  -10.164 26.050  1.00 11.33 ? 39  TYR B C   1 
ATOM   2478  O  O   . TYR B 1 39  ? -7.731  -9.888  27.184  1.00 12.98 ? 39  TYR B O   1 
ATOM   2479  C  CB  . TYR B 1 39  ? -7.621  -12.546 25.457  1.00 13.10 ? 39  TYR B CB  1 
ATOM   2480  C  CG  . TYR B 1 39  ? -9.076  -12.936 25.632  1.00 12.03 ? 39  TYR B CG  1 
ATOM   2481  C  CD1 . TYR B 1 39  ? -9.956  -12.919 24.554  1.00 13.18 ? 39  TYR B CD1 1 
ATOM   2482  C  CD2 . TYR B 1 39  ? -9.577  -13.295 26.876  1.00 13.61 ? 39  TYR B CD2 1 
ATOM   2483  C  CE1 . TYR B 1 39  ? -11.290 -13.263 24.710  1.00 12.49 ? 39  TYR B CE1 1 
ATOM   2484  C  CE2 . TYR B 1 39  ? -10.909 -13.640 27.041  1.00 11.77 ? 39  TYR B CE2 1 
ATOM   2485  C  CZ  . TYR B 1 39  ? -11.761 -13.623 25.955  1.00 11.17 ? 39  TYR B CZ  1 
ATOM   2486  O  OH  . TYR B 1 39  ? -13.084 -13.967 26.119  1.00 15.90 ? 39  TYR B OH  1 
ATOM   2487  N  N   . ASP B 1 40  ? -9.380  -9.703  25.619  1.00 9.59  ? 40  ASP B N   1 
ATOM   2488  C  CA  . ASP B 1 40  ? -10.265 -8.879  26.449  1.00 11.03 ? 40  ASP B CA  1 
ATOM   2489  C  C   . ASP B 1 40  ? -11.654 -9.396  26.323  1.00 11.94 ? 40  ASP B C   1 
ATOM   2490  O  O   . ASP B 1 40  ? -12.333 -9.195  25.286  1.00 11.99 ? 40  ASP B O   1 
ATOM   2491  C  CB  . ASP B 1 40  ? -10.120 -7.392  26.060  1.00 10.42 ? 40  ASP B CB  1 
ATOM   2492  C  CG  . ASP B 1 40  ? -10.940 -6.488  26.860  1.00 18.35 ? 40  ASP B CG  1 
ATOM   2493  O  OD1 . ASP B 1 40  ? -11.756 -6.958  27.632  1.00 17.97 ? 40  ASP B OD1 1 
ATOM   2494  O  OD2 . ASP B 1 40  ? -10.712 -5.248  26.682  1.00 21.84 ? 40  ASP B OD2 1 
ATOM   2495  N  N   . ALA B 1 41  ? -12.190 -10.093 27.348  1.00 12.23 ? 41  ALA B N   1 
ATOM   2496  C  CA  . ALA B 1 41  ? -13.514 -10.700 27.261  1.00 13.71 ? 41  ALA B CA  1 
ATOM   2497  C  C   . ALA B 1 41  ? -14.653 -9.649  27.177  1.00 14.16 ? 41  ALA B C   1 
ATOM   2498  O  O   . ALA B 1 41  ? -15.805 -9.981  26.772  1.00 15.18 ? 41  ALA B O   1 
ATOM   2499  C  CB  . ALA B 1 41  ? -13.665 -11.594 28.496  1.00 14.74 ? 41  ALA B CB  1 
ATOM   2500  N  N   . SER B 1 42  ? -14.367 -8.386  27.474  1.00 14.27 ? 42  SER B N   1 
ATOM   2501  C  CA  . SER B 1 42  ? -15.413 -7.386  27.345  1.00 13.23 ? 42  SER B CA  1 
ATOM   2502  C  C   . SER B 1 42  ? -15.644 -6.894  25.863  1.00 13.61 ? 42  SER B C   1 
ATOM   2503  O  O   . SER B 1 42  ? -16.509 -6.017  25.573  1.00 14.90 ? 42  SER B O   1 
ATOM   2504  C  CB  . SER B 1 42  ? -15.063 -6.046  28.086  1.00 17.06 ? 42  SER B CB  1 
ATOM   2505  O  OG  . SER B 1 42  ? -14.008 -5.267  27.454  1.00 21.79 ? 42  SER B OG  1 
ATOM   2506  N  N   . LEU B 1 43  ? -14.833 -7.379  24.929  1.00 11.41 ? 43  LEU B N   1 
ATOM   2507  C  CA  . LEU B 1 43  ? -15.044 -7.027  23.470  1.00 10.35 ? 43  LEU B CA  1 
ATOM   2508  C  C   . LEU B 1 43  ? -16.089 -7.924  22.899  1.00 9.54  ? 43  LEU B C   1 
ATOM   2509  O  O   . LEU B 1 43  ? -15.859 -9.029  22.332  1.00 11.93 ? 43  LEU B O   1 
ATOM   2510  C  CB  . LEU B 1 43  ? -13.711 -7.176  22.779  1.00 10.64 ? 43  LEU B CB  1 
ATOM   2511  C  CG  . LEU B 1 43  ? -12.599 -6.208  23.135  1.00 8.99  ? 43  LEU B CG  1 
ATOM   2512  C  CD1 . LEU B 1 43  ? -11.265 -6.493  22.420  1.00 11.56 ? 43  LEU B CD1 1 
ATOM   2513  C  CD2 . LEU B 1 43  ? -12.973 -4.736  22.965  1.00 10.69 ? 43  LEU B CD2 1 
ATOM   2514  N  N   . THR B 1 44  ? -17.318 -7.458  23.186  1.00 12.64 ? 44  THR B N   1 
ATOM   2515  C  CA  . THR B 1 44  ? -18.500 -8.212  22.756  1.00 12.49 ? 44  THR B CA  1 
ATOM   2516  C  C   . THR B 1 44  ? -18.836 -7.966  21.282  1.00 12.20 ? 44  THR B C   1 
ATOM   2517  O  O   . THR B 1 44  ? -18.222 -7.042  20.671  1.00 12.33 ? 44  THR B O   1 
ATOM   2518  C  CB  . THR B 1 44  ? -19.709 -7.786  23.631  1.00 13.10 ? 44  THR B CB  1 
ATOM   2519  O  OG1 . THR B 1 44  ? -19.695 -6.378  23.773  1.00 16.38 ? 44  THR B OG1 1 
ATOM   2520  C  CG2 . THR B 1 44  ? -19.482 -8.377  25.075  1.00 16.55 ? 44  THR B CG2 1 
ATOM   2521  N  N   . PRO B 1 45  ? -19.717 -8.742  20.647  1.00 12.73 ? 45  PRO B N   1 
ATOM   2522  C  CA  . PRO B 1 45  ? -19.953 -8.587  19.207  1.00 12.74 ? 45  PRO B CA  1 
ATOM   2523  C  C   . PRO B 1 45  ? -20.581 -7.267  18.792  1.00 12.62 ? 45  PRO B C   1 
ATOM   2524  O  O   . PRO B 1 45  ? -21.383 -6.664  19.551  1.00 15.32 ? 45  PRO B O   1 
ATOM   2525  C  CB  . PRO B 1 45  ? -20.834 -9.752  18.839  1.00 14.43 ? 45  PRO B CB  1 
ATOM   2526  C  CG  . PRO B 1 45  ? -20.498 -10.761 20.004  1.00 14.66 ? 45  PRO B CG  1 
ATOM   2527  C  CD  . PRO B 1 45  ? -20.420 -9.948  21.163  1.00 15.16 ? 45  PRO B CD  1 
ATOM   2528  N  N   . LEU B 1 46  ? -20.072 -6.741  17.672  1.00 9.76  ? 46  LEU B N   1 
ATOM   2529  C  CA  . LEU B 1 46  ? -20.730 -5.528  17.107  1.00 10.73 ? 46  LEU B CA  1 
ATOM   2530  C  C   . LEU B 1 46  ? -21.949 -6.002  16.296  1.00 10.43 ? 46  LEU B C   1 
ATOM   2531  O  O   . LEU B 1 46  ? -21.991 -7.119  15.772  1.00 11.82 ? 46  LEU B O   1 
ATOM   2532  C  CB  . LEU B 1 46  ? -19.737 -4.829  16.116  1.00 10.97 ? 46  LEU B CB  1 
ATOM   2533  C  CG  . LEU B 1 46  ? -18.574 -4.252  16.894  1.00 12.60 ? 46  LEU B CG  1 
ATOM   2534  C  CD1 . LEU B 1 46  ? -17.674 -3.658  15.746  1.00 16.65 ? 46  LEU B CD1 1 
ATOM   2535  C  CD2 . LEU B 1 46  ? -18.968 -3.298  18.025  1.00 15.64 ? 46  LEU B CD2 1 
ATOM   2536  N  N   . GLU B 1 47  ? -22.904 -5.086  16.253  1.00 11.81 ? 47  GLU B N   1 
ATOM   2537  C  CA  . GLU B 1 47  ? -24.059 -5.296  15.360  1.00 13.70 ? 47  GLU B CA  1 
ATOM   2538  C  C   . GLU B 1 47  ? -24.046 -4.184  14.223  1.00 11.24 ? 47  GLU B C   1 
ATOM   2539  O  O   . GLU B 1 47  ? -23.807 -3.013  14.503  1.00 13.79 ? 47  GLU B O   1 
ATOM   2540  C  CB  . GLU B 1 47  ? -25.398 -5.159  16.149  1.00 14.31 ? 47  GLU B CB  1 
ATOM   2541  C  CG  . GLU B 1 47  ? -25.544 -6.309  17.239  1.00 17.54 ? 47  GLU B CG  1 
ATOM   2542  C  CD  . GLU B 1 47  ? -26.925 -6.240  17.970  1.00 21.72 ? 47  GLU B CD  1 
ATOM   2543  O  OE1 . GLU B 1 47  ? -27.273 -5.155  18.508  1.00 31.61 ? 47  GLU B OE1 1 
ATOM   2544  O  OE2 . GLU B 1 47  ? -27.627 -7.234  17.972  1.00 34.49 ? 47  GLU B OE2 1 
ATOM   2545  N  N   . PHE B 1 48  ? -24.379 -4.631  13.049  1.00 12.00 ? 48  PHE B N   1 
ATOM   2546  C  CA  . PHE B 1 48  ? -24.314 -3.755  11.813  1.00 11.61 ? 48  PHE B CA  1 
ATOM   2547  C  C   . PHE B 1 48  ? -25.755 -3.444  11.380  1.00 11.22 ? 48  PHE B C   1 
ATOM   2548  O  O   . PHE B 1 48  ? -26.424 -4.352  10.841  1.00 15.98 ? 48  PHE B O   1 
ATOM   2549  C  CB  . PHE B 1 48  ? -23.532 -4.463  10.772  1.00 12.23 ? 48  PHE B CB  1 
ATOM   2550  C  CG  . PHE B 1 48  ? -22.228 -4.986  11.319  1.00 11.27 ? 48  PHE B CG  1 
ATOM   2551  C  CD1 . PHE B 1 48  ? -21.170 -4.163  11.714  1.00 13.37 ? 48  PHE B CD1 1 
ATOM   2552  C  CD2 . PHE B 1 48  ? -22.078 -6.397  11.462  1.00 12.07 ? 48  PHE B CD2 1 
ATOM   2553  C  CE1 . PHE B 1 48  ? -19.939 -4.714  12.344  1.00 10.27 ? 48  PHE B CE1 1 
ATOM   2554  C  CE2 . PHE B 1 48  ? -20.897 -6.916  12.050  1.00 14.93 ? 48  PHE B CE2 1 
ATOM   2555  C  CZ  . PHE B 1 48  ? -19.868 -6.120  12.445  1.00 13.11 ? 48  PHE B CZ  1 
ATOM   2556  N  N   . GLN B 1 49  ? -26.089 -2.197  11.638  1.00 11.40 ? 49  GLN B N   1 
ATOM   2557  C  CA  . GLN B 1 49  ? -27.481 -1.787  11.454  1.00 12.17 ? 49  GLN B CA  1 
ATOM   2558  C  C   . GLN B 1 49  ? -27.598 -0.882  10.196  1.00 10.70 ? 49  GLN B C   1 
ATOM   2559  O  O   . GLN B 1 49  ? -26.815 0.042   9.977   1.00 11.77 ? 49  GLN B O   1 
ATOM   2560  C  CB  . GLN B 1 49  ? -27.992 -1.053  12.658  1.00 12.28 ? 49  GLN B CB  1 
ATOM   2561  C  CG  . GLN B 1 49  ? -27.853 -1.857  13.958  1.00 15.70 ? 49  GLN B CG  1 
ATOM   2562  C  CD  . GLN B 1 49  ? -28.639 -3.101  13.963  1.00 22.10 ? 49  GLN B CD  1 
ATOM   2563  O  OE1 . GLN B 1 49  ? -28.108 -4.272  14.069  1.00 25.60 ? 49  GLN B OE1 1 
ATOM   2564  N  NE2 . GLN B 1 49  ? -29.943 -2.943  13.760  1.00 20.59 ? 49  GLN B NE2 1 
ATOM   2565  N  N   . GLY B 1 50  ? -28.617 -1.109  9.396   1.00 13.29 ? 50  GLY B N   1 
ATOM   2566  C  CA  . GLY B 1 50  ? -28.794 -0.258  8.183   1.00 10.84 ? 50  GLY B CA  1 
ATOM   2567  C  C   . GLY B 1 50  ? -27.707 -0.450  7.143   1.00 12.01 ? 50  GLY B C   1 
ATOM   2568  O  O   . GLY B 1 50  ? -27.604 0.320   6.190   1.00 12.24 ? 50  GLY B O   1 
ATOM   2569  N  N   . TYR B 1 51  ? -26.943 -1.556  7.250   1.00 10.49 ? 51  TYR B N   1 
ATOM   2570  C  CA  . TYR B 1 51  ? -25.963 -1.909  6.191   1.00 10.59 ? 51  TYR B CA  1 
ATOM   2571  C  C   . TYR B 1 51  ? -26.565 -2.412  4.851   1.00 11.74 ? 51  TYR B C   1 
ATOM   2572  O  O   . TYR B 1 51  ? -25.958 -2.372  3.813   1.00 10.49 ? 51  TYR B O   1 
ATOM   2573  C  CB  . TYR B 1 51  ? -24.982 -3.034  6.727   1.00 9.91  ? 51  TYR B CB  1 
ATOM   2574  C  CG  . TYR B 1 51  ? -23.810 -2.473  7.509   1.00 8.50  ? 51  TYR B CG  1 
ATOM   2575  C  CD1 . TYR B 1 51  ? -22.508 -2.882  7.244   1.00 8.37  ? 51  TYR B CD1 1 
ATOM   2576  C  CD2 . TYR B 1 51  ? -24.008 -1.524  8.507   1.00 9.87  ? 51  TYR B CD2 1 
ATOM   2577  C  CE1 . TYR B 1 51  ? -21.439 -2.367  7.954   1.00 9.45  ? 51  TYR B CE1 1 
ATOM   2578  C  CE2 . TYR B 1 51  ? -22.943 -1.002  9.224   1.00 7.86  ? 51  TYR B CE2 1 
ATOM   2579  C  CZ  . TYR B 1 51  ? -21.660 -1.428  8.942   1.00 10.05 ? 51  TYR B CZ  1 
ATOM   2580  O  OH  . TYR B 1 51  ? -20.592 -0.919  9.646   1.00 11.21 ? 51  TYR B OH  1 
ATOM   2581  N  N   . ASN B 1 52  ? -27.820 -2.923  4.900   1.00 11.00 ? 52  ASN B N   1 
ATOM   2582  C  CA  . ASN B 1 52  ? -28.471 -3.478  3.664   1.00 10.14 ? 52  ASN B CA  1 
ATOM   2583  C  C   . ASN B 1 52  ? -29.104 -2.347  2.864   1.00 12.74 ? 52  ASN B C   1 
ATOM   2584  O  O   . ASN B 1 52  ? -30.255 -1.952  3.099   1.00 13.94 ? 52  ASN B O   1 
ATOM   2585  C  CB  . ASN B 1 52  ? -29.567 -4.538  4.033   1.00 13.55 ? 52  ASN B CB  1 
ATOM   2586  C  CG  . ASN B 1 52  ? -30.135 -5.192  2.866   1.00 17.66 ? 52  ASN B CG  1 
ATOM   2587  O  OD1 . ASN B 1 52  ? -29.738 -4.985  1.724   1.00 22.02 ? 52  ASN B OD1 1 
ATOM   2588  N  ND2 . ASN B 1 52  ? -31.114 -6.072  3.134   1.00 22.72 ? 52  ASN B ND2 1 
ATOM   2589  N  N   . LEU B 1 53  ? -28.273 -1.681  2.098   1.00 12.00 ? 53  LEU B N   1 
ATOM   2590  C  CA  . LEU B 1 53  ? -28.721 -0.434  1.460   1.00 11.56 ? 53  LEU B CA  1 
ATOM   2591  C  C   . LEU B 1 53  ? -29.700 -0.873  0.238   1.00 9.52  ? 53  LEU B C   1 
ATOM   2592  O  O   . LEU B 1 53  ? -29.485 -1.833  -0.468  1.00 12.58 ? 53  LEU B O   1 
ATOM   2593  C  CB  . LEU B 1 53  ? -27.527 0.340   0.838   1.00 11.85 ? 53  LEU B CB  1 
ATOM   2594  C  CG  . LEU B 1 53  ? -26.378 0.660   1.807   1.00 11.80 ? 53  LEU B CG  1 
ATOM   2595  C  CD1 . LEU B 1 53  ? -25.232 1.315   0.946   1.00 13.86 ? 53  LEU B CD1 1 
ATOM   2596  C  CD2 . LEU B 1 53  ? -26.882 1.449   2.946   1.00 12.30 ? 53  LEU B CD2 1 
ATOM   2597  N  N   . SER B 1 54  ? -30.768 -0.050  0.132   1.00 10.35 ? 54  SER B N   1 
ATOM   2598  C  CA  . SER B 1 54  ? -31.740 -0.268  -0.954  1.00 12.21 ? 54  SER B CA  1 
ATOM   2599  C  C   . SER B 1 54  ? -31.098 -0.307  -2.353  1.00 11.14 ? 54  SER B C   1 
ATOM   2600  O  O   . SER B 1 54  ? -30.443 0.679   -2.686  1.00 11.02 ? 54  SER B O   1 
ATOM   2601  C  CB  . SER B 1 54  ? -32.871 0.721   -0.874  1.00 13.24 ? 54  SER B CB  1 
ATOM   2602  O  OG  . SER B 1 54  ? -33.705 0.358   -1.942  1.00 13.43 ? 54  SER B OG  1 
ATOM   2603  N  N   . ALA B 1 55  ? -31.324 -1.375  -3.139  1.00 13.26 ? 55  ALA B N   1 
ATOM   2604  C  CA  . ALA B 1 55  ? -30.834 -1.444  -4.508  1.00 13.09 ? 55  ALA B CA  1 
ATOM   2605  C  C   . ALA B 1 55  ? -31.544 -0.461  -5.386  1.00 11.95 ? 55  ALA B C   1 
ATOM   2606  O  O   . ALA B 1 55  ? -31.121 -0.244  -6.551  1.00 16.11 ? 55  ALA B O   1 
ATOM   2607  C  CB  . ALA B 1 55  ? -31.008 -2.845  -5.099  1.00 14.66 ? 55  ALA B CB  1 
ATOM   2608  N  N   . ASN B 1 56  ? -32.629 0.169   -4.877  1.00 13.19 ? 56  ASN B N   1 
ATOM   2609  C  CA  . ASN B 1 56  ? -33.330 1.161   -5.696  1.00 12.99 ? 56  ASN B CA  1 
ATOM   2610  C  C   . ASN B 1 56  ? -32.779 2.522   -5.448  1.00 11.82 ? 56  ASN B C   1 
ATOM   2611  O  O   . ASN B 1 56  ? -33.152 3.473   -6.172  1.00 15.21 ? 56  ASN B O   1 
ATOM   2612  C  CB  . ASN B 1 56  ? -34.854 1.114   -5.521  1.00 12.36 ? 56  ASN B CB  1 
ATOM   2613  C  CG  . ASN B 1 56  ? -35.403 -0.244  -5.816  1.00 18.82 ? 56  ASN B CG  1 
ATOM   2614  O  OD1 . ASN B 1 56  ? -34.885 -0.955  -6.667  1.00 19.39 ? 56  ASN B OD1 1 
ATOM   2615  N  ND2 . ASN B 1 56  ? -36.423 -0.642  -5.042  1.00 23.30 ? 56  ASN B ND2 1 
ATOM   2616  N  N   . LYS B 1 57  ? -31.906 2.716   -4.449  1.00 11.45 ? 57  LYS B N   1 
ATOM   2617  C  CA  . LYS B 1 57  ? -31.244 3.954   -4.170  1.00 11.20 ? 57  LYS B CA  1 
ATOM   2618  C  C   . LYS B 1 57  ? -29.796 3.836   -4.712  1.00 12.60 ? 57  LYS B C   1 
ATOM   2619  O  O   . LYS B 1 57  ? -29.341 2.754   -5.144  1.00 12.29 ? 57  LYS B O   1 
ATOM   2620  C  CB  . LYS B 1 57  ? -31.162 4.137   -2.673  1.00 13.24 ? 57  LYS B CB  1 
ATOM   2621  C  CG  . LYS B 1 57  ? -32.542 4.527   -2.069  1.00 14.65 ? 57  LYS B CG  1 
ATOM   2622  C  CD  . LYS B 1 57  ? -32.530 4.727   -0.578  1.00 22.23 ? 57  LYS B CD  1 
ATOM   2623  C  CE  . LYS B 1 57  ? -32.453 6.154   -0.084  1.00 29.55 ? 57  LYS B CE  1 
ATOM   2624  N  NZ  . LYS B 1 57  ? -32.991 6.040   1.377   1.00 26.94 ? 57  LYS B NZ  1 
ATOM   2625  N  N   . GLN B 1 58  ? -29.130 4.950   -4.804  1.00 11.43 ? 58  GLN B N   1 
ATOM   2626  C  CA  . GLN B 1 58  ? -27.763 4.955   -5.369  1.00 11.55 ? 58  GLN B CA  1 
ATOM   2627  C  C   . GLN B 1 58  ? -26.880 5.850   -4.504  1.00 11.80 ? 58  GLN B C   1 
ATOM   2628  O  O   . GLN B 1 58  ? -27.304 6.818   -3.877  1.00 11.55 ? 58  GLN B O   1 
ATOM   2629  C  CB  . GLN B 1 58  ? -27.588 5.357   -6.812  1.00 17.11 ? 58  GLN B CB  1 
ATOM   2630  C  CG  . GLN B 1 58  ? -28.231 6.618   -7.255  1.00 19.59 ? 58  GLN B CG  1 
ATOM   2631  C  CD  . GLN B 1 58  ? -28.673 6.538   -8.699  1.00 24.70 ? 58  GLN B CD  1 
ATOM   2632  O  OE1 . GLN B 1 58  ? -28.213 5.715   -9.492  1.00 25.63 ? 58  GLN B OE1 1 
ATOM   2633  N  NE2 . GLN B 1 58  ? -29.587 7.426   -9.057  1.00 32.00 ? 58  GLN B NE2 1 
ATOM   2634  N  N   . PHE B 1 59  ? -25.597 5.457   -4.465  1.00 11.90 ? 59  PHE B N   1 
ATOM   2635  C  CA  . PHE B 1 59  ? -24.615 6.043   -3.563  1.00 10.18 ? 59  PHE B CA  1 
ATOM   2636  C  C   . PHE B 1 59  ? -23.376 6.448   -4.335  1.00 8.88  ? 59  PHE B C   1 
ATOM   2637  O  O   . PHE B 1 59  ? -22.986 5.773   -5.293  1.00 9.72  ? 59  PHE B O   1 
ATOM   2638  C  CB  . PHE B 1 59  ? -24.269 4.959   -2.514  1.00 10.52 ? 59  PHE B CB  1 
ATOM   2639  C  CG  . PHE B 1 59  ? -25.522 4.577   -1.716  1.00 10.62 ? 59  PHE B CG  1 
ATOM   2640  C  CD1 . PHE B 1 59  ? -26.416 3.603   -2.182  1.00 11.10 ? 59  PHE B CD1 1 
ATOM   2641  C  CD2 . PHE B 1 59  ? -25.777 5.291   -0.569  1.00 11.68 ? 59  PHE B CD2 1 
ATOM   2642  C  CE1 . PHE B 1 59  ? -27.644 3.423   -1.488  1.00 9.83  ? 59  PHE B CE1 1 
ATOM   2643  C  CE2 . PHE B 1 59  ? -27.042 5.055   0.121   1.00 13.18 ? 59  PHE B CE2 1 
ATOM   2644  C  CZ  . PHE B 1 59  ? -27.904 4.094   -0.372  1.00 10.61 ? 59  PHE B CZ  1 
ATOM   2645  N  N   . LEU B 1 60  ? -22.905 7.625   -3.943  1.00 8.96  ? 60  LEU B N   1 
ATOM   2646  C  CA  . LEU B 1 60  ? -21.876 8.244   -4.764  1.00 10.06 ? 60  LEU B CA  1 
ATOM   2647  C  C   . LEU B 1 60  ? -20.474 7.620   -4.555  1.00 9.07  ? 60  LEU B C   1 
ATOM   2648  O  O   . LEU B 1 60  ? -19.986 7.614   -3.401  1.00 9.79  ? 60  LEU B O   1 
ATOM   2649  C  CB  . LEU B 1 60  ? -21.813 9.727   -4.289  1.00 10.49 ? 60  LEU B CB  1 
ATOM   2650  C  CG  . LEU B 1 60  ? -20.997 10.655  -5.219  1.00 15.28 ? 60  LEU B CG  1 
ATOM   2651  C  CD1 . LEU B 1 60  ? -21.731 10.919  -6.509  1.00 17.74 ? 60  LEU B CD1 1 
ATOM   2652  C  CD2 . LEU B 1 60  ? -20.708 12.001  -4.509  1.00 14.46 ? 60  LEU B CD2 1 
ATOM   2653  N  N   . LEU B 1 61  ? -19.842 7.194   -5.621  1.00 10.16 ? 61  LEU B N   1 
ATOM   2654  C  CA  . LEU B 1 61  ? -18.471 6.739   -5.666  1.00 8.67  ? 61  LEU B CA  1 
ATOM   2655  C  C   . LEU B 1 61  ? -17.596 7.833   -6.237  1.00 10.11 ? 61  LEU B C   1 
ATOM   2656  O  O   . LEU B 1 61  ? -17.991 8.461   -7.209  1.00 12.69 ? 61  LEU B O   1 
ATOM   2657  C  CB  . LEU B 1 61  ? -18.427 5.514   -6.529  1.00 10.94 ? 61  LEU B CB  1 
ATOM   2658  C  CG  . LEU B 1 61  ? -17.189 4.667   -6.593  1.00 12.78 ? 61  LEU B CG  1 
ATOM   2659  C  CD1 . LEU B 1 61  ? -16.931 3.882   -5.241  1.00 13.25 ? 61  LEU B CD1 1 
ATOM   2660  C  CD2 . LEU B 1 61  ? -17.129 3.589   -7.747  1.00 12.95 ? 61  LEU B CD2 1 
ATOM   2661  N  N   . THR B 1 62  ? -16.434 8.061   -5.637  1.00 8.82  ? 62  THR B N   1 
ATOM   2662  C  CA  . THR B 1 62  ? -15.625 9.227   -6.031  1.00 10.32 ? 62  THR B CA  1 
ATOM   2663  C  C   . THR B 1 62  ? -14.152 8.769   -5.929  1.00 12.38 ? 62  THR B C   1 
ATOM   2664  O  O   . THR B 1 62  ? -13.725 8.052   -5.035  1.00 11.91 ? 62  THR B O   1 
ATOM   2665  C  CB  . THR B 1 62  ? -15.739 10.346  -5.132  1.00 13.03 ? 62  THR B CB  1 
ATOM   2666  O  OG1 . THR B 1 62  ? -17.095 10.770  -4.894  1.00 16.61 ? 62  THR B OG1 1 
ATOM   2667  C  CG2 . THR B 1 62  ? -14.926 11.662  -5.560  1.00 16.68 ? 62  THR B CG2 1 
ATOM   2668  N  N   . ASN B 1 63  ? -13.384 9.184   -6.903  1.00 10.41 ? 63  ASN B N   1 
ATOM   2669  C  CA  . ASN B 1 63  ? -11.907 9.113   -6.812  1.00 10.06 ? 63  ASN B CA  1 
ATOM   2670  C  C   . ASN B 1 63  ? -11.438 10.376  -6.254  1.00 10.23 ? 63  ASN B C   1 
ATOM   2671  O  O   . ASN B 1 63  ? -11.589 11.489  -6.843  1.00 8.97  ? 63  ASN B O   1 
ATOM   2672  C  CB  . ASN B 1 63  ? -11.402 8.898   -8.265  1.00 10.60 ? 63  ASN B CB  1 
ATOM   2673  C  CG  . ASN B 1 63  ? -9.921  8.947   -8.374  1.00 9.39  ? 63  ASN B CG  1 
ATOM   2674  O  OD1 . ASN B 1 63  ? -9.200  9.548   -7.539  1.00 8.55  ? 63  ASN B OD1 1 
ATOM   2675  N  ND2 . ASN B 1 63  ? -9.419  8.248   -9.400  1.00 8.65  ? 63  ASN B ND2 1 
ATOM   2676  N  N   . ASN B 1 64  ? -10.806 10.295  -5.096  1.00 9.80  ? 64  ASN B N   1 
ATOM   2677  C  CA  . ASN B 1 64  ? -10.434 11.574  -4.401  1.00 9.38  ? 64  ASN B CA  1 
ATOM   2678  C  C   . ASN B 1 64  ? -8.902  11.858  -4.563  1.00 11.42 ? 64  ASN B C   1 
ATOM   2679  O  O   . ASN B 1 64  ? -8.358  12.741  -3.880  1.00 12.75 ? 64  ASN B O   1 
ATOM   2680  C  CB  . ASN B 1 64  ? -10.785 11.548  -2.862  1.00 10.61 ? 64  ASN B CB  1 
ATOM   2681  C  CG  . ASN B 1 64  ? -9.946  10.553  -2.109  1.00 14.28 ? 64  ASN B CG  1 
ATOM   2682  O  OD1 . ASN B 1 64  ? -9.101  9.827   -2.658  1.00 10.04 ? 64  ASN B OD1 1 
ATOM   2683  N  ND2 . ASN B 1 64  ? -10.219 10.439  -0.799  1.00 17.96 ? 64  ASN B ND2 1 
ATOM   2684  N  N   . GLY B 1 65  ? -8.283  11.193  -5.535  1.00 9.91  ? 65  GLY B N   1 
ATOM   2685  C  CA  . GLY B 1 65  ? -6.820  11.398  -5.743  1.00 10.88 ? 65  GLY B CA  1 
ATOM   2686  C  C   . GLY B 1 65  ? -5.948  10.526  -4.899  1.00 9.48  ? 65  GLY B C   1 
ATOM   2687  O  O   . GLY B 1 65  ? -4.783  10.391  -5.196  1.00 10.65 ? 65  GLY B O   1 
ATOM   2688  N  N   . HIS B 1 66  ? -6.519  9.801   -3.915  1.00 9.82  ? 66  HIS B N   1 
ATOM   2689  C  CA  . HIS B 1 66  ? -5.743  8.905   -2.949  1.00 9.99  ? 66  HIS B CA  1 
ATOM   2690  C  C   . HIS B 1 66  ? -6.310  7.531   -2.828  1.00 9.80  ? 66  HIS B C   1 
ATOM   2691  O  O   . HIS B 1 66  ? -5.516  6.575   -2.497  1.00 8.80  ? 66  HIS B O   1 
ATOM   2692  C  CB  . HIS B 1 66  ? -5.663  9.526   -1.581  1.00 10.20 ? 66  HIS B CB  1 
ATOM   2693  C  CG  . HIS B 1 66  ? -5.162  10.940  -1.627  1.00 9.94  ? 66  HIS B CG  1 
ATOM   2694  N  ND1 . HIS B 1 66  ? -3.841  11.240  -1.916  1.00 12.06 ? 66  HIS B ND1 1 
ATOM   2695  C  CD2 . HIS B 1 66  ? -5.787  12.112  -1.411  1.00 10.02 ? 66  HIS B CD2 1 
ATOM   2696  C  CE1 . HIS B 1 66  ? -3.694  12.565  -1.882  1.00 9.96  ? 66  HIS B CE1 1 
ATOM   2697  N  NE2 . HIS B 1 66  ? -4.848  13.076  -1.519  1.00 12.78 ? 66  HIS B NE2 1 
ATOM   2698  N  N   . SER B 1 67  ? -7.629  7.391   -3.028  1.00 7.61  ? 67  SER B N   1 
ATOM   2699  C  CA  . SER B 1 67  ? -8.309  6.058   -3.026  1.00 7.87  ? 67  SER B CA  1 
ATOM   2700  C  C   . SER B 1 67  ? -9.596  6.198   -3.793  1.00 10.28 ? 67  SER B C   1 
ATOM   2701  O  O   . SER B 1 67  ? -9.822  7.264   -4.379  1.00 9.88  ? 67  SER B O   1 
ATOM   2702  C  CB  . SER B 1 67  ? -8.733  5.662   -1.554  1.00 9.46  ? 67  SER B CB  1 
ATOM   2703  O  OG  . SER B 1 67  ? -9.200  4.308   -1.444  1.00 9.95  ? 67  SER B OG  1 
ATOM   2704  N  N   . VAL B 1 68  ? -10.366 5.117   -3.818  1.00 8.79  ? 68  VAL B N   1 
ATOM   2705  C  CA  . VAL B 1 68  ? -11.706 5.245   -4.373  1.00 9.17  ? 68  VAL B CA  1 
ATOM   2706  C  C   . VAL B 1 68  ? -12.609 5.141   -3.116  1.00 8.71  ? 68  VAL B C   1 
ATOM   2707  O  O   . VAL B 1 68  ? -12.442 4.192   -2.309  1.00 8.97  ? 68  VAL B O   1 
ATOM   2708  C  CB  . VAL B 1 68  ? -11.997 4.168   -5.407  1.00 9.06  ? 68  VAL B CB  1 
ATOM   2709  C  CG1 . VAL B 1 68  ? -11.709 2.729   -4.903  1.00 12.94 ? 68  VAL B CG1 1 
ATOM   2710  C  CG2 . VAL B 1 68  ? -13.398 4.301   -6.012  1.00 15.91 ? 68  VAL B CG2 1 
ATOM   2711  N  N   . LYS B 1 69  ? -13.583 6.055   -2.992  1.00 8.98  ? 69  LYS B N   1 
ATOM   2712  C  CA  . LYS B 1 69  ? -14.498 6.035   -1.781  1.00 8.65  ? 69  LYS B CA  1 
ATOM   2713  C  C   . LYS B 1 69  ? -15.940 5.977   -2.223  1.00 8.72  ? 69  LYS B C   1 
ATOM   2714  O  O   . LYS B 1 69  ? -16.373 6.545   -3.238  1.00 10.30 ? 69  LYS B O   1 
ATOM   2715  C  CB  . LYS B 1 69  ? -14.260 7.210   -0.867  1.00 14.65 ? 69  LYS B CB  1 
ATOM   2716  C  CG  . LYS B 1 69  ? -14.555 8.505   -1.381  1.00 18.84 ? 69  LYS B CG  1 
ATOM   2717  C  CD  . LYS B 1 69  ? -14.553 9.514   -0.132  1.00 18.01 ? 69  LYS B CD  1 
ATOM   2718  C  CE  . LYS B 1 69  ? -14.719 10.829  -0.763  1.00 22.43 ? 69  LYS B CE  1 
ATOM   2719  N  NZ  . LYS B 1 69  ? -14.761 11.757  0.405   1.00 26.48 ? 69  LYS B NZ  1 
ATOM   2720  N  N   . LEU B 1 70  ? -16.731 5.283   -1.435  1.00 7.52  ? 70  LEU B N   1 
ATOM   2721  C  CA  . LEU B 1 70  ? -18.182 5.176   -1.616  1.00 6.31  ? 70  LEU B CA  1 
ATOM   2722  C  C   . LEU B 1 70  ? -18.756 5.890   -0.433  1.00 8.19  ? 70  LEU B C   1 
ATOM   2723  O  O   . LEU B 1 70  ? -18.519 5.502   0.750   1.00 6.82  ? 70  LEU B O   1 
ATOM   2724  C  CB  . LEU B 1 70  ? -18.544 3.690   -1.606  1.00 6.94  ? 70  LEU B CB  1 
ATOM   2725  C  CG  . LEU B 1 70  ? -20.064 3.452   -1.783  1.00 8.54  ? 70  LEU B CG  1 
ATOM   2726  C  CD1 . LEU B 1 70  ? -20.563 3.927   -3.178  1.00 10.97 ? 70  LEU B CD1 1 
ATOM   2727  C  CD2 . LEU B 1 70  ? -20.407 1.949   -1.635  1.00 9.58  ? 70  LEU B CD2 1 
ATOM   2728  N  N   . ASN B 1 71  ? -19.607 6.926   -0.671  1.00 8.76  ? 71  ASN B N   1 
ATOM   2729  C  CA  . ASN B 1 71  ? -20.335 7.626   0.438   1.00 9.50  ? 71  ASN B CA  1 
ATOM   2730  C  C   . ASN B 1 71  ? -21.455 6.710   0.941   1.00 10.49 ? 71  ASN B C   1 
ATOM   2731  O  O   . ASN B 1 71  ? -22.069 5.925   0.153   1.00 10.97 ? 71  ASN B O   1 
ATOM   2732  C  CB  . ASN B 1 71  ? -20.923 8.955   -0.087  1.00 10.35 ? 71  ASN B CB  1 
ATOM   2733  C  CG  . ASN B 1 71  ? -19.884 10.040  -0.276  1.00 14.34 ? 71  ASN B CG  1 
ATOM   2734  O  OD1 . ASN B 1 71  ? -18.713 9.898   -0.024  1.00 15.78 ? 71  ASN B OD1 1 
ATOM   2735  N  ND2 . ASN B 1 71  ? -20.419 11.256  -0.635  1.00 20.09 ? 71  ASN B ND2 1 
ATOM   2736  N  N   . LEU B 1 72  ? -21.658 6.796   2.263   1.00 8.53  ? 72  LEU B N   1 
ATOM   2737  C  CA  . LEU B 1 72  ? -22.610 5.913   2.910   1.00 8.22  ? 72  LEU B CA  1 
ATOM   2738  C  C   . LEU B 1 72  ? -23.574 6.789   3.719   1.00 10.95 ? 72  LEU B C   1 
ATOM   2739  O  O   . LEU B 1 72  ? -23.208 7.927   4.141   1.00 10.59 ? 72  LEU B O   1 
ATOM   2740  C  CB  . LEU B 1 72  ? -21.868 4.929   3.901   1.00 9.06  ? 72  LEU B CB  1 
ATOM   2741  C  CG  . LEU B 1 72  ? -20.939 3.918   3.160   1.00 8.39  ? 72  LEU B CG  1 
ATOM   2742  C  CD1 . LEU B 1 72  ? -19.955 3.263   4.243   1.00 9.35  ? 72  LEU B CD1 1 
ATOM   2743  C  CD2 . LEU B 1 72  ? -21.607 2.926   2.305   1.00 11.06 ? 72  LEU B CD2 1 
ATOM   2744  N  N   . PRO B 1 73  ? -24.789 6.300   3.914   1.00 9.76  ? 73  PRO B N   1 
ATOM   2745  C  CA  . PRO B 1 73  ? -25.824 7.125   4.588   1.00 11.02 ? 73  PRO B CA  1 
ATOM   2746  C  C   . PRO B 1 73  ? -25.706 7.049   6.092   1.00 12.77 ? 73  PRO B C   1 
ATOM   2747  O  O   . PRO B 1 73  ? -25.281 6.005   6.654   1.00 13.81 ? 73  PRO B O   1 
ATOM   2748  C  CB  . PRO B 1 73  ? -27.086 6.472   4.119   1.00 10.46 ? 73  PRO B CB  1 
ATOM   2749  C  CG  . PRO B 1 73  ? -26.737 4.907   3.956   1.00 11.05 ? 73  PRO B CG  1 
ATOM   2750  C  CD  . PRO B 1 73  ? -25.305 5.026   3.382   1.00 10.34 ? 73  PRO B CD  1 
ATOM   2751  N  N   . SER B 1 74  ? -26.056 8.152   6.759   1.00 15.67 ? 74  SER B N   1 
ATOM   2752  C  CA  . SER B 1 74  ? -25.880 8.187   8.225   1.00 14.34 ? 74  SER B CA  1 
ATOM   2753  C  C   . SER B 1 74  ? -26.841 7.285   8.977   1.00 14.26 ? 74  SER B C   1 
ATOM   2754  O  O   . SER B 1 74  ? -26.604 7.012   10.194  1.00 14.93 ? 74  SER B O   1 
ATOM   2755  C  CB  . SER B 1 74  ? -25.974 9.637   8.716   1.00 18.31 ? 74  SER B CB  1 
ATOM   2756  O  OG  . SER B 1 74  ? -27.256 10.139  8.430   1.00 21.47 ? 74  SER B OG  1 
ATOM   2757  N  N   . ASP B 1 75  ? -27.856 6.732   8.321   1.00 14.77 ? 75  ASP B N   1 
ATOM   2758  C  CA  . ASP B 1 75  ? -28.747 5.757   9.021   1.00 15.45 ? 75  ASP B CA  1 
ATOM   2759  C  C   . ASP B 1 75  ? -28.060 4.420   9.194   1.00 15.75 ? 75  ASP B C   1 
ATOM   2760  O  O   . ASP B 1 75  ? -28.434 3.650   10.030  1.00 15.01 ? 75  ASP B O   1 
ATOM   2761  C  CB  . ASP B 1 75  ? -30.034 5.512   8.192   1.00 15.97 ? 75  ASP B CB  1 
ATOM   2762  C  CG  . ASP B 1 75  ? -29.791 5.665   6.606   1.00 25.39 ? 75  ASP B CG  1 
ATOM   2763  O  OD1 . ASP B 1 75  ? -29.683 6.826   6.115   1.00 33.75 ? 75  ASP B OD1 1 
ATOM   2764  O  OD2 . ASP B 1 75  ? -29.695 4.679   5.838   1.00 32.79 ? 75  ASP B OD2 1 
ATOM   2765  N  N   . MET B 1 76  ? -26.987 4.182   8.439   1.00 12.22 ? 76  MET B N   1 
ATOM   2766  C  CA  . MET B 1 76  ? -26.134 2.976   8.617   1.00 11.12 ? 76  MET B CA  1 
ATOM   2767  C  C   . MET B 1 76  ? -25.208 3.173   9.837   1.00 11.63 ? 76  MET B C   1 
ATOM   2768  O  O   . MET B 1 76  ? -24.540 4.229   9.992   1.00 11.41 ? 76  MET B O   1 
ATOM   2769  C  CB  . MET B 1 76  ? -25.363 2.909   7.337   1.00 12.40 ? 76  MET B CB  1 
ATOM   2770  C  CG  . MET B 1 76  ? -24.354 1.719   7.402   1.00 14.21 ? 76  MET B CG  1 
ATOM   2771  S  SD  . MET B 1 76  ? -23.614 1.588   5.685   1.00 12.05 ? 76  MET B SD  1 
ATOM   2772  C  CE  . MET B 1 76  ? -22.113 0.718   6.206   1.00 9.65  ? 76  MET B CE  1 
ATOM   2773  N  N   . HIS B 1 77  ? -25.198 2.216   10.761  1.00 11.86 ? 77  HIS B N   1 
ATOM   2774  C  CA  . HIS B 1 77  ? -24.414 2.448   11.980  1.00 12.15 ? 77  HIS B CA  1 
ATOM   2775  C  C   . HIS B 1 77  ? -23.990 1.165   12.640  1.00 9.54  ? 77  HIS B C   1 
ATOM   2776  O  O   . HIS B 1 77  ? -24.511 0.092   12.329  1.00 11.41 ? 77  HIS B O   1 
ATOM   2777  C  CB  . HIS B 1 77  ? -25.214 3.371   13.002  1.00 14.27 ? 77  HIS B CB  1 
ATOM   2778  C  CG  . HIS B 1 77  ? -26.473 2.744   13.518  1.00 16.48 ? 77  HIS B CG  1 
ATOM   2779  N  ND1 . HIS B 1 77  ? -27.702 2.786   12.849  1.00 18.05 ? 77  HIS B ND1 1 
ATOM   2780  C  CD2 . HIS B 1 77  ? -26.690 2.048   14.672  1.00 20.89 ? 77  HIS B CD2 1 
ATOM   2781  C  CE1 . HIS B 1 77  ? -28.592 2.091   13.561  1.00 17.51 ? 77  HIS B CE1 1 
ATOM   2782  N  NE2 . HIS B 1 77  ? -28.028 1.683   14.681  1.00 19.19 ? 77  HIS B NE2 1 
ATOM   2783  N  N   . ILE B 1 78  ? -23.036 1.364   13.562  1.00 11.83 ? 78  ILE B N   1 
ATOM   2784  C  CA  . ILE B 1 78  ? -22.645 0.199   14.387  1.00 13.37 ? 78  ILE B CA  1 
ATOM   2785  C  C   . ILE B 1 78  ? -23.333 0.321   15.739  1.00 12.61 ? 78  ILE B C   1 
ATOM   2786  O  O   . ILE B 1 78  ? -23.312 1.457   16.292  1.00 14.49 ? 78  ILE B O   1 
ATOM   2787  C  CB  . ILE B 1 78  ? -21.109 0.289   14.621  1.00 12.91 ? 78  ILE B CB  1 
ATOM   2788  C  CG1 . ILE B 1 78  ? -20.281 0.132   13.356  1.00 16.55 ? 78  ILE B CG1 1 
ATOM   2789  C  CG2 . ILE B 1 78  ? -20.674 -0.740  15.721  1.00 14.72 ? 78  ILE B CG2 1 
ATOM   2790  C  CD1 . ILE B 1 78  ? -18.804 0.621   13.555  1.00 16.50 ? 78  ILE B CD1 1 
ATOM   2791  N  N   . GLN B 1 79  ? -23.847 -0.812  16.241  1.00 12.61 ? 79  GLN B N   1 
ATOM   2792  C  CA  . GLN B 1 79  ? -24.437 -0.896  17.586  1.00 14.48 ? 79  GLN B CA  1 
ATOM   2793  C  C   . GLN B 1 79  ? -23.422 -1.790  18.355  1.00 15.09 ? 79  GLN B C   1 
ATOM   2794  O  O   . GLN B 1 79  ? -22.924 -2.828  17.793  1.00 15.12 ? 79  GLN B O   1 
ATOM   2795  C  CB  . GLN B 1 79  ? -25.780 -1.611  17.426  1.00 13.81 ? 79  GLN B CB  1 
ATOM   2796  C  CG  . GLN B 1 79  ? -26.548 -2.054  18.677  1.00 20.73 ? 79  GLN B CG  1 
ATOM   2797  C  CD  . GLN B 1 79  ? -26.860 -0.883  19.606  1.00 21.96 ? 79  GLN B CD  1 
ATOM   2798  O  OE1 . GLN B 1 79  ? -27.317 0.175   19.148  1.00 24.33 ? 79  GLN B OE1 1 
ATOM   2799  N  NE2 . GLN B 1 79  ? -26.695 -1.076  20.910  1.00 31.40 ? 79  GLN B NE2 1 
ATOM   2800  N  N   . GLY B 1 80  ? -23.126 -1.380  19.576  1.00 15.45 ? 80  GLY B N   1 
ATOM   2801  C  CA  . GLY B 1 80  ? -22.262 -2.187  20.461  1.00 15.71 ? 80  GLY B CA  1 
ATOM   2802  C  C   . GLY B 1 80  ? -21.068 -1.438  20.990  1.00 15.56 ? 80  GLY B C   1 
ATOM   2803  O  O   . GLY B 1 80  ? -20.441 -1.832  22.013  1.00 17.67 ? 80  GLY B O   1 
ATOM   2804  N  N   . LEU B 1 81  ? -20.673 -0.287  20.412  1.00 14.82 ? 81  LEU B N   1 
ATOM   2805  C  CA  . LEU B 1 81  ? -19.662 0.581   21.019  1.00 13.72 ? 81  LEU B CA  1 
ATOM   2806  C  C   . LEU B 1 81  ? -20.254 1.454   22.096  1.00 16.70 ? 81  LEU B C   1 
ATOM   2807  O  O   . LEU B 1 81  ? -21.498 1.380   22.343  1.00 18.17 ? 81  LEU B O   1 
ATOM   2808  C  CB  . LEU B 1 81  ? -18.934 1.437   19.923  1.00 16.69 ? 81  LEU B CB  1 
ATOM   2809  C  CG  . LEU B 1 81  ? -18.180 0.541   18.896  1.00 15.28 ? 81  LEU B CG  1 
ATOM   2810  C  CD1 . LEU B 1 81  ? -17.715 1.483   17.805  1.00 18.74 ? 81  LEU B CD1 1 
ATOM   2811  C  CD2 . LEU B 1 81  ? -16.953 -0.029  19.624  1.00 17.32 ? 81  LEU B CD2 1 
ATOM   2812  N  N   . GLN B 1 82  ? -19.485 2.373   22.661  1.00 17.94 ? 82  GLN B N   1 
ATOM   2813  C  CA  . GLN B 1 82  ? -20.077 3.098   23.788  1.00 22.03 ? 82  GLN B CA  1 
ATOM   2814  C  C   . GLN B 1 82  ? -20.862 4.352   23.388  1.00 23.11 ? 82  GLN B C   1 
ATOM   2815  O  O   . GLN B 1 82  ? -21.413 5.003   24.262  1.00 22.53 ? 82  GLN B O   1 
ATOM   2816  C  CB  . GLN B 1 82  ? -19.030 3.422   24.805  1.00 22.95 ? 82  GLN B CB  1 
ATOM   2817  C  CG  . GLN B 1 82  ? -18.584 2.215   25.676  1.00 26.08 ? 82  GLN B CG  1 
ATOM   2818  C  CD  . GLN B 1 82  ? -17.503 2.693   26.689  1.00 32.46 ? 82  GLN B CD  1 
ATOM   2819  O  OE1 . GLN B 1 82  ? -17.691 2.688   27.906  1.00 32.02 ? 82  GLN B OE1 1 
ATOM   2820  N  NE2 . GLN B 1 82  ? -16.415 3.222   26.148  1.00 34.80 ? 82  GLN B NE2 1 
ATOM   2821  N  N   . SER B 1 83  ? -20.821 4.706   22.072  1.00 20.87 ? 83  SER B N   1 
ATOM   2822  C  CA  . SER B 1 83  ? -21.708 5.698   21.412  1.00 18.72 ? 83  SER B CA  1 
ATOM   2823  C  C   . SER B 1 83  ? -22.128 5.036   20.126  1.00 19.42 ? 83  SER B C   1 
ATOM   2824  O  O   . SER B 1 83  ? -21.460 4.100   19.692  1.00 15.28 ? 83  SER B O   1 
ATOM   2825  C  CB  . SER B 1 83  ? -20.964 7.020   21.109  1.00 22.09 ? 83  SER B CB  1 
ATOM   2826  O  OG  . SER B 1 83  ? -20.693 7.642   22.343  1.00 25.09 ? 83  SER B OG  1 
ATOM   2827  N  N   . ARG B 1 84  ? -23.207 5.498   19.506  1.00 17.55 ? 84  ARG B N   1 
ATOM   2828  C  CA  . ARG B 1 84  ? -23.540 5.103   18.173  1.00 18.56 ? 84  ARG B CA  1 
ATOM   2829  C  C   . ARG B 1 84  ? -22.490 5.730   17.209  1.00 16.57 ? 84  ARG B C   1 
ATOM   2830  O  O   . ARG B 1 84  ? -22.157 6.868   17.308  1.00 15.22 ? 84  ARG B O   1 
ATOM   2831  C  CB  . ARG B 1 84  ? -24.977 5.530   17.800  1.00 20.35 ? 84  ARG B CB  1 
ATOM   2832  C  CG  . ARG B 1 84  ? -25.249 5.527   16.320  1.00 21.95 ? 84  ARG B CG  1 
ATOM   2833  C  CD  . ARG B 1 84  ? -26.694 5.833   15.974  1.00 36.32 ? 84  ARG B CD  1 
ATOM   2834  N  NE  . ARG B 1 84  ? -26.856 5.976   14.554  1.00 41.76 ? 84  ARG B NE  1 
ATOM   2835  C  CZ  . ARG B 1 84  ? -27.989 5.854   13.903  1.00 40.48 ? 84  ARG B CZ  1 
ATOM   2836  N  NH1 . ARG B 1 84  ? -29.103 5.599   14.559  1.00 39.31 ? 84  ARG B NH1 1 
ATOM   2837  N  NH2 . ARG B 1 84  ? -27.994 5.996   12.601  1.00 36.10 ? 84  ARG B NH2 1 
ATOM   2838  N  N   . TYR B 1 85  ? -21.961 4.887   16.325  1.00 12.70 ? 85  TYR B N   1 
ATOM   2839  C  CA  . TYR B 1 85  ? -21.089 5.417   15.222  1.00 10.13 ? 85  TYR B CA  1 
ATOM   2840  C  C   . TYR B 1 85  ? -21.791 5.188   13.946  1.00 9.82  ? 85  TYR B C   1 
ATOM   2841  O  O   . TYR B 1 85  ? -22.104 4.042   13.598  1.00 12.39 ? 85  TYR B O   1 
ATOM   2842  C  CB  . TYR B 1 85  ? -19.711 4.682   15.285  1.00 11.58 ? 85  TYR B CB  1 
ATOM   2843  C  CG  . TYR B 1 85  ? -18.852 5.218   16.414  1.00 12.00 ? 85  TYR B CG  1 
ATOM   2844  C  CD1 . TYR B 1 85  ? -17.838 6.109   16.183  1.00 10.61 ? 85  TYR B CD1 1 
ATOM   2845  C  CD2 . TYR B 1 85  ? -19.027 4.727   17.692  1.00 13.95 ? 85  TYR B CD2 1 
ATOM   2846  C  CE1 . TYR B 1 85  ? -17.008 6.571   17.192  1.00 13.42 ? 85  TYR B CE1 1 
ATOM   2847  C  CE2 . TYR B 1 85  ? -18.155 5.160   18.720  1.00 13.35 ? 85  TYR B CE2 1 
ATOM   2848  C  CZ  . TYR B 1 85  ? -17.180 6.080   18.474  1.00 16.55 ? 85  TYR B CZ  1 
ATOM   2849  O  OH  . TYR B 1 85  ? -16.356 6.499   19.538  1.00 18.27 ? 85  TYR B OH  1 
ATOM   2850  N  N   . SER B 1 86  ? -22.011 6.294   13.248  1.00 9.95  ? 86  SER B N   1 
ATOM   2851  C  CA  . SER B 1 86  ? -22.757 6.203   12.000  1.00 10.48 ? 86  SER B CA  1 
ATOM   2852  C  C   . SER B 1 86  ? -21.751 6.243   10.805  1.00 8.99  ? 86  SER B C   1 
ATOM   2853  O  O   . SER B 1 86  ? -20.702 6.900   10.845  1.00 10.92 ? 86  SER B O   1 
ATOM   2854  C  CB  . SER B 1 86  ? -23.773 7.363   11.786  1.00 12.96 ? 86  SER B CB  1 
ATOM   2855  O  OG  . SER B 1 86  ? -24.801 7.330   12.834  1.00 16.05 ? 86  SER B OG  1 
ATOM   2856  N  N   . ALA B 1 87  ? -22.123 5.522   9.767   1.00 8.98  ? 87  ALA B N   1 
ATOM   2857  C  CA  . ALA B 1 87  ? -21.210 5.410   8.591   1.00 9.02  ? 87  ALA B CA  1 
ATOM   2858  C  C   . ALA B 1 87  ? -21.068 6.757   7.907   1.00 10.47 ? 87  ALA B C   1 
ATOM   2859  O  O   . ALA B 1 87  ? -22.050 7.578   7.836   1.00 11.52 ? 87  ALA B O   1 
ATOM   2860  C  CB  . ALA B 1 87  ? -21.716 4.359   7.682   1.00 13.54 ? 87  ALA B CB  1 
ATOM   2861  N  N   . THR B 1 88  ? -19.903 6.965   7.274   1.00 9.02  ? 88  THR B N   1 
ATOM   2862  C  CA  . THR B 1 88  ? -19.744 8.051   6.337   1.00 9.40  ? 88  THR B CA  1 
ATOM   2863  C  C   . THR B 1 88  ? -19.201 7.676   4.996   1.00 10.32 ? 88  THR B C   1 
ATOM   2864  O  O   . THR B 1 88  ? -19.645 8.153   3.965   1.00 8.77  ? 88  THR B O   1 
ATOM   2865  C  CB  . THR B 1 88  ? -18.881 9.107   6.991   1.00 10.74 ? 88  THR B CB  1 
ATOM   2866  O  OG1 . THR B 1 88  ? -18.840 10.276  6.088   1.00 16.32 ? 88  THR B OG1 1 
ATOM   2867  C  CG2 . THR B 1 88  ? -17.484 8.674   7.482   1.00 9.95  ? 88  THR B CG2 1 
ATOM   2868  N  N   . GLN B 1 89  ? -18.235 6.729   4.942   1.00 8.39  ? 89  GLN B N   1 
ATOM   2869  C  CA  . GLN B 1 89  ? -17.734 6.352   3.640   1.00 7.23  ? 89  GLN B CA  1 
ATOM   2870  C  C   . GLN B 1 89  ? -16.955 5.023   3.808   1.00 6.74  ? 89  GLN B C   1 
ATOM   2871  O  O   . GLN B 1 89  ? -16.544 4.719   4.966   1.00 7.33  ? 89  GLN B O   1 
ATOM   2872  C  CB  . GLN B 1 89  ? -16.796 7.457   3.068   1.00 8.05  ? 89  GLN B CB  1 
ATOM   2873  C  CG  . GLN B 1 89  ? -15.652 7.838   3.995   1.00 10.46 ? 89  GLN B CG  1 
ATOM   2874  C  CD  . GLN B 1 89  ? -14.312 7.364   3.518   1.00 10.74 ? 89  GLN B CD  1 
ATOM   2875  O  OE1 . GLN B 1 89  ? -14.202 6.207   3.158   1.00 10.40 ? 89  GLN B OE1 1 
ATOM   2876  N  NE2 . GLN B 1 89  ? -13.355 8.182   3.441   1.00 15.61 ? 89  GLN B NE2 1 
ATOM   2877  N  N   . LEU B 1 90  ? -16.776 4.299   2.743   1.00 5.79  ? 90  LEU B N   1 
ATOM   2878  C  CA  . LEU B 1 90  ? -15.781 3.214   2.720   1.00 5.77  ? 90  LEU B CA  1 
ATOM   2879  C  C   . LEU B 1 90  ? -14.805 3.438   1.574   1.00 7.51  ? 90  LEU B C   1 
ATOM   2880  O  O   . LEU B 1 90  ? -15.066 4.116   0.602   1.00 6.94  ? 90  LEU B O   1 
ATOM   2881  C  CB  . LEU B 1 90  ? -16.415 1.761   2.706   1.00 5.88  ? 90  LEU B CB  1 
ATOM   2882  C  CG  . LEU B 1 90  ? -17.362 1.473   1.527   1.00 6.78  ? 90  LEU B CG  1 
ATOM   2883  C  CD1 . LEU B 1 90  ? -16.636 1.182   0.221   1.00 6.66  ? 90  LEU B CD1 1 
ATOM   2884  C  CD2 . LEU B 1 90  ? -18.288 0.255   1.897   1.00 7.88  ? 90  LEU B CD2 1 
ATOM   2885  N  N   . HIS B 1 91  ? -13.607 2.841   1.677   1.00 5.88  ? 91  HIS B N   1 
ATOM   2886  C  CA  . HIS B 1 91  ? -12.555 2.976   0.628   1.00 5.28  ? 91  HIS B CA  1 
ATOM   2887  C  C   . HIS B 1 91  ? -11.589 1.776   0.820   1.00 5.99  ? 91  HIS B C   1 
ATOM   2888  O  O   . HIS B 1 91  ? -11.773 0.950   1.722   1.00 5.12  ? 91  HIS B O   1 
ATOM   2889  C  CB  . HIS B 1 91  ? -11.868 4.344   0.758   1.00 4.64  ? 91  HIS B CB  1 
ATOM   2890  C  CG  . HIS B 1 91  ? -11.129 4.528   2.047   1.00 4.44  ? 91  HIS B CG  1 
ATOM   2891  N  ND1 . HIS B 1 91  ? -11.692 5.135   3.148   1.00 5.45  ? 91  HIS B ND1 1 
ATOM   2892  C  CD2 . HIS B 1 91  ? -9.871  4.183   2.411   1.00 5.88  ? 91  HIS B CD2 1 
ATOM   2893  C  CE1 . HIS B 1 91  ? -10.813 5.157   4.135   1.00 6.06  ? 91  HIS B CE1 1 
ATOM   2894  N  NE2 . HIS B 1 91  ? -9.700  4.585   3.713   1.00 5.89  ? 91  HIS B NE2 1 
ATOM   2895  N  N   . LEU B 1 92  ? -10.595 1.754   -0.069  1.00 5.28  ? 92  LEU B N   1 
ATOM   2896  C  CA  . LEU B 1 92  ? -9.671  0.640   -0.023  1.00 6.05  ? 92  LEU B CA  1 
ATOM   2897  C  C   . LEU B 1 92  ? -8.239  1.119   -0.140  1.00 5.62  ? 92  LEU B C   1 
ATOM   2898  O  O   . LEU B 1 92  ? -7.932  2.277   -0.516  1.00 6.03  ? 92  LEU B O   1 
ATOM   2899  C  CB  . LEU B 1 92  ? -9.924  -0.366  -1.143  1.00 7.34  ? 92  LEU B CB  1 
ATOM   2900  C  CG  . LEU B 1 92  ? -11.345 -0.990  -1.109  1.00 6.84  ? 92  LEU B CG  1 
ATOM   2901  C  CD1 . LEU B 1 92  ? -12.306 -0.368  -1.985  1.00 13.18 ? 92  LEU B CD1 1 
ATOM   2902  C  CD2 . LEU B 1 92  ? -11.210 -2.462  -1.348  1.00 9.79  ? 92  LEU B CD2 1 
ATOM   2903  N  N   . HIS B 1 93  ? -7.356  0.194   0.202   1.00 6.16  ? 93  HIS B N   1 
ATOM   2904  C  CA  . HIS B 1 93  ? -5.850  0.318   -0.012  1.00 5.08  ? 93  HIS B CA  1 
ATOM   2905  C  C   . HIS B 1 93  ? -5.334  -0.863  -0.683  1.00 5.75  ? 93  HIS B C   1 
ATOM   2906  O  O   . HIS B 1 93  ? -5.816  -1.982  -0.323  1.00 6.08  ? 93  HIS B O   1 
ATOM   2907  C  CB  . HIS B 1 93  ? -5.188  0.483   1.379   1.00 6.55  ? 93  HIS B CB  1 
ATOM   2908  C  CG  . HIS B 1 93  ? -5.716  1.674   2.161   1.00 7.14  ? 93  HIS B CG  1 
ATOM   2909  N  ND1 . HIS B 1 93  ? -5.137  2.962   2.097   1.00 7.01  ? 93  HIS B ND1 1 
ATOM   2910  C  CD2 . HIS B 1 93  ? -6.755  1.769   3.055   1.00 5.53  ? 93  HIS B CD2 1 
ATOM   2911  C  CE1 . HIS B 1 93  ? -5.848  3.806   2.874   1.00 6.30  ? 93  HIS B CE1 1 
ATOM   2912  N  NE2 . HIS B 1 93  ? -6.814  3.131   3.464   1.00 4.85  ? 93  HIS B NE2 1 
ATOM   2913  N  N   . TRP B 1 94  ? -4.387  -0.724  -1.600  1.00 6.47  ? 94  TRP B N   1 
ATOM   2914  C  CA  . TRP B 1 94  ? -3.932  -1.919  -2.356  1.00 4.70  ? 94  TRP B CA  1 
ATOM   2915  C  C   . TRP B 1 94  ? -2.534  -1.643  -2.883  1.00 6.06  ? 94  TRP B C   1 
ATOM   2916  O  O   . TRP B 1 94  ? -1.909  -0.606  -2.600  1.00 5.92  ? 94  TRP B O   1 
ATOM   2917  C  CB  . TRP B 1 94  ? -4.889  -2.215  -3.516  1.00 6.10  ? 94  TRP B CB  1 
ATOM   2918  C  CG  . TRP B 1 94  ? -5.023  -0.966  -4.459  1.00 6.94  ? 94  TRP B CG  1 
ATOM   2919  C  CD1 . TRP B 1 94  ? -4.204  -0.691  -5.581  1.00 8.01  ? 94  TRP B CD1 1 
ATOM   2920  C  CD2 . TRP B 1 94  ? -6.028  0.087   -4.381  1.00 6.66  ? 94  TRP B CD2 1 
ATOM   2921  N  NE1 . TRP B 1 94  ? -4.682  0.488   -6.180  1.00 7.35  ? 94  TRP B NE1 1 
ATOM   2922  C  CE2 . TRP B 1 94  ? -5.820  0.930   -5.512  1.00 6.12  ? 94  TRP B CE2 1 
ATOM   2923  C  CE3 . TRP B 1 94  ? -7.149  0.337   -3.530  1.00 7.73  ? 94  TRP B CE3 1 
ATOM   2924  C  CZ2 . TRP B 1 94  ? -6.591  2.070   -5.717  1.00 5.93  ? 94  TRP B CZ2 1 
ATOM   2925  C  CZ3 . TRP B 1 94  ? -7.949  1.495   -3.773  1.00 7.84  ? 94  TRP B CZ3 1 
ATOM   2926  C  CH2 . TRP B 1 94  ? -7.629  2.371   -4.852  1.00 5.38  ? 94  TRP B CH2 1 
ATOM   2927  N  N   . GLY B 1 95  ? -1.997  -2.685  -3.521  1.00 6.60  ? 95  GLY B N   1 
ATOM   2928  C  CA  . GLY B 1 95  ? -0.549  -2.654  -3.985  1.00 6.97  ? 95  GLY B CA  1 
ATOM   2929  C  C   . GLY B 1 95  ? -0.518  -2.426  -5.472  1.00 6.17  ? 95  GLY B C   1 
ATOM   2930  O  O   . GLY B 1 95  ? -1.031  -1.396  -5.937  1.00 8.02  ? 95  GLY B O   1 
ATOM   2931  N  N   . ASN B 1 96  ? 0.026   -3.325  -6.279  1.00 9.30  ? 96  ASN B N   1 
ATOM   2932  C  CA  . ASN B 1 96  ? 0.094   -3.067  -7.726  1.00 9.51  ? 96  ASN B CA  1 
ATOM   2933  C  C   . ASN B 1 96  ? 0.143   -4.405  -8.447  1.00 10.89 ? 96  ASN B C   1 
ATOM   2934  O  O   . ASN B 1 96  ? 0.259   -5.412  -7.770  1.00 10.25 ? 96  ASN B O   1 
ATOM   2935  C  CB  . ASN B 1 96  ? 1.290   -2.211  -8.112  1.00 12.08 ? 96  ASN B CB  1 
ATOM   2936  C  CG  . ASN B 1 96  ? 2.636   -2.946  -7.868  1.00 13.02 ? 96  ASN B CG  1 
ATOM   2937  O  OD1 . ASN B 1 96  ? 2.984   -3.707  -8.793  1.00 18.84 ? 96  ASN B OD1 1 
ATOM   2938  N  ND2 . ASN B 1 96  ? 3.331   -2.815  -6.779  1.00 10.90 ? 96  ASN B ND2 1 
ATOM   2939  N  N   . PRO B 1 97  ? -0.019  -4.424  -9.772  1.00 10.14 ? 97  PRO B N   1 
ATOM   2940  C  CA  . PRO B 1 97  ? -0.168  -5.677  -10.445 1.00 12.30 ? 97  PRO B CA  1 
ATOM   2941  C  C   . PRO B 1 97  ? 0.954   -6.635  -10.274 1.00 11.34 ? 97  PRO B C   1 
ATOM   2942  O  O   . PRO B 1 97  ? 0.693   -7.893  -10.398 1.00 13.79 ? 97  PRO B O   1 
ATOM   2943  C  CB  . PRO B 1 97  ? -0.188  -5.248  -11.899 1.00 14.02 ? 97  PRO B CB  1 
ATOM   2944  C  CG  . PRO B 1 97  ? -1.017  -3.911  -11.888 1.00 12.34 ? 97  PRO B CG  1 
ATOM   2945  C  CD  . PRO B 1 97  ? -0.210  -3.309  -10.717 1.00 12.76 ? 97  PRO B CD  1 
ATOM   2946  N  N   . ASN B 1 98  ? 2.164   -6.148  -10.079 1.00 8.27  ? 98  ASN B N   1 
ATOM   2947  C  CA  . ASN B 1 98  ? 3.359   -7.033  -9.982  1.00 11.99 ? 98  ASN B CA  1 
ATOM   2948  C  C   . ASN B 1 98  ? 3.662   -7.342  -8.547  1.00 13.68 ? 98  ASN B C   1 
ATOM   2949  O  O   . ASN B 1 98  ? 4.440   -8.251  -8.263  1.00 17.97 ? 98  ASN B O   1 
ATOM   2950  C  CB  . ASN B 1 98  ? 4.565   -6.371  -10.707 1.00 10.44 ? 98  ASN B CB  1 
ATOM   2951  C  CG  . ASN B 1 98  ? 4.275   -6.187  -12.168 1.00 13.15 ? 98  ASN B CG  1 
ATOM   2952  O  OD1 . ASN B 1 98  ? 4.000   -7.186  -12.910 1.00 12.68 ? 98  ASN B OD1 1 
ATOM   2953  N  ND2 . ASN B 1 98  ? 4.110   -4.910  -12.579 1.00 14.80 ? 98  ASN B ND2 1 
ATOM   2954  N  N   . ASP B 1 99  ? 2.911   -6.772  -7.595  1.00 11.28 ? 99  ASP B N   1 
ATOM   2955  C  CA  . ASP B 1 99  ? 3.191   -7.025  -6.157  1.00 10.67 ? 99  ASP B CA  1 
ATOM   2956  C  C   . ASP B 1 99  ? 1.806   -6.781  -5.495  1.00 9.20  ? 99  ASP B C   1 
ATOM   2957  O  O   . ASP B 1 99  ? 1.549   -5.693  -4.934  1.00 9.15  ? 99  ASP B O   1 
ATOM   2958  C  CB  . ASP B 1 99  ? 4.172   -6.039  -5.487  1.00 13.61 ? 99  ASP B CB  1 
ATOM   2959  C  CG  . ASP B 1 99  ? 4.473   -6.409  -4.003  1.00 16.26 ? 99  ASP B CG  1 
ATOM   2960  O  OD1 . ASP B 1 99  ? 3.950   -7.471  -3.563  1.00 23.20 ? 99  ASP B OD1 1 
ATOM   2961  O  OD2 . ASP B 1 99  ? 5.035   -5.591  -3.274  1.00 30.14 ? 99  ASP B OD2 1 
ATOM   2962  N  N   . PRO B 1 100 ? 0.881   -7.723  -5.549  1.00 8.57  ? 100 PRO B N   1 
ATOM   2963  C  CA  . PRO B 1 100 ? -0.473  -7.552  -4.960  1.00 9.44  ? 100 PRO B CA  1 
ATOM   2964  C  C   . PRO B 1 100 ? -0.479  -7.772  -3.433  1.00 9.15  ? 100 PRO B C   1 
ATOM   2965  O  O   . PRO B 1 100 ? -1.054  -8.715  -2.916  1.00 10.50 ? 100 PRO B O   1 
ATOM   2966  C  CB  . PRO B 1 100 ? -1.355  -8.468  -5.787  1.00 10.86 ? 100 PRO B CB  1 
ATOM   2967  C  CG  . PRO B 1 100 ? -0.299  -9.642  -6.043  1.00 11.54 ? 100 PRO B CG  1 
ATOM   2968  C  CD  . PRO B 1 100 ? 1.009   -8.994  -6.308  1.00 10.52 ? 100 PRO B CD  1 
ATOM   2969  N  N   . HIS B 1 101 ? 0.201   -6.923  -2.713  1.00 9.01  ? 101 HIS B N   1 
ATOM   2970  C  CA  . HIS B 1 101 ? 0.423   -7.031  -1.246  1.00 9.82  ? 101 HIS B CA  1 
ATOM   2971  C  C   . HIS B 1 101 ? 0.355   -5.704  -0.561  1.00 10.05 ? 101 HIS B C   1 
ATOM   2972  O  O   . HIS B 1 101 ? 1.321   -5.283  0.173   1.00 14.37 ? 101 HIS B O   1 
ATOM   2973  C  CB  . HIS B 1 101 ? 1.714   -7.740  -0.887  1.00 12.33 ? 101 HIS B CB  1 
ATOM   2974  C  CG  . HIS B 1 101 ? 1.713   -9.138  -1.395  1.00 14.29 ? 101 HIS B CG  1 
ATOM   2975  N  ND1 . HIS B 1 101 ? 2.330   -9.481  -2.582  1.00 16.19 ? 101 HIS B ND1 1 
ATOM   2976  C  CD2 . HIS B 1 101 ? 1.076   -10.250 -0.945  1.00 19.04 ? 101 HIS B CD2 1 
ATOM   2977  C  CE1 . HIS B 1 101 ? 2.162   -10.780 -2.805  1.00 16.06 ? 101 HIS B CE1 1 
ATOM   2978  N  NE2 . HIS B 1 101 ? 1.356   -11.250 -1.859  1.00 20.03 ? 101 HIS B NE2 1 
ATOM   2979  N  N   . GLY B 1 102 ? -0.822  -5.112  -0.559  1.00 7.16  ? 102 GLY B N   1 
ATOM   2980  C  CA  . GLY B 1 102 ? -0.970  -3.728  -0.235  1.00 6.78  ? 102 GLY B CA  1 
ATOM   2981  C  C   . GLY B 1 102 ? -1.966  -3.489  0.897   1.00 5.65  ? 102 GLY B C   1 
ATOM   2982  O  O   . GLY B 1 102 ? -2.460  -2.332  1.065   1.00 7.79  ? 102 GLY B O   1 
ATOM   2983  N  N   . SER B 1 103 ? -2.176  -4.461  1.831   1.00 5.81  ? 103 SER B N   1 
ATOM   2984  C  CA  . SER B 1 103 ? -2.938  -4.104  3.028   1.00 6.45  ? 103 SER B CA  1 
ATOM   2985  C  C   . SER B 1 103 ? -2.110  -3.073  3.873   1.00 7.73  ? 103 SER B C   1 
ATOM   2986  O  O   . SER B 1 103 ? -0.869  -2.978  3.706   1.00 8.39  ? 103 SER B O   1 
ATOM   2987  C  CB  . SER B 1 103 ? -3.238  -5.438  3.817   1.00 6.94  ? 103 SER B CB  1 
ATOM   2988  O  OG  . SER B 1 103 ? -2.000  -5.880  4.428   1.00 6.94  ? 103 SER B OG  1 
ATOM   2989  N  N   . GLU B 1 104 ? -2.804  -2.357  4.733   1.00 6.30  ? 104 GLU B N   1 
ATOM   2990  C  CA  . GLU B 1 104 ? -2.151  -1.482  5.657   1.00 6.95  ? 104 GLU B CA  1 
ATOM   2991  C  C   . GLU B 1 104 ? -1.722  -2.173  6.949   1.00 4.72  ? 104 GLU B C   1 
ATOM   2992  O  O   . GLU B 1 104 ? -0.561  -2.201  7.293   1.00 6.60  ? 104 GLU B O   1 
ATOM   2993  C  CB  . GLU B 1 104 ? -3.069  -0.268  5.971   1.00 6.60  ? 104 GLU B CB  1 
ATOM   2994  C  CG  . GLU B 1 104 ? -3.498  0.509   4.716   1.00 6.98  ? 104 GLU B CG  1 
ATOM   2995  C  CD  . GLU B 1 104 ? -3.560  1.955   4.986   1.00 5.60  ? 104 GLU B CD  1 
ATOM   2996  O  OE1 . GLU B 1 104 ? -4.581  2.369   5.558   1.00 7.06  ? 104 GLU B OE1 1 
ATOM   2997  O  OE2 . GLU B 1 104 ? -2.606  2.670   4.649   1.00 7.96  ? 104 GLU B OE2 1 
ATOM   2998  N  N   . HIS B 1 105 ? -2.685  -2.750  7.656   1.00 6.73  ? 105 HIS B N   1 
ATOM   2999  C  CA  . HIS B 1 105 ? -2.324  -3.663  8.773   1.00 6.10  ? 105 HIS B CA  1 
ATOM   3000  C  C   . HIS B 1 105 ? -1.634  -4.936  8.202   1.00 6.92  ? 105 HIS B C   1 
ATOM   3001  O  O   . HIS B 1 105 ? -1.956  -5.398  7.129   1.00 6.42  ? 105 HIS B O   1 
ATOM   3002  C  CB  . HIS B 1 105 ? -3.562  -3.995  9.592   1.00 5.28  ? 105 HIS B CB  1 
ATOM   3003  C  CG  . HIS B 1 105 ? -4.041  -2.771  10.300  1.00 7.51  ? 105 HIS B CG  1 
ATOM   3004  N  ND1 . HIS B 1 105 ? -5.023  -1.984  9.735   1.00 7.01  ? 105 HIS B ND1 1 
ATOM   3005  C  CD2 . HIS B 1 105 ? -3.768  -2.308  11.530  1.00 6.24  ? 105 HIS B CD2 1 
ATOM   3006  C  CE1 . HIS B 1 105 ? -5.230  -0.965  10.572  1.00 9.08  ? 105 HIS B CE1 1 
ATOM   3007  N  NE2 . HIS B 1 105 ? -4.490  -1.132  11.688  1.00 7.60  ? 105 HIS B NE2 1 
ATOM   3008  N  N   . THR B 1 106 ? -0.721  -5.454  9.051   1.00 7.29  ? 106 THR B N   1 
ATOM   3009  C  CA  . THR B 1 106 ? -0.069  -6.772  8.744   1.00 7.02  ? 106 THR B CA  1 
ATOM   3010  C  C   . THR B 1 106 ? -0.355  -7.607  9.930   1.00 6.64  ? 106 THR B C   1 
ATOM   3011  O  O   . THR B 1 106 ? -0.721  -7.158  10.987  1.00 7.39  ? 106 THR B O   1 
ATOM   3012  C  CB  . THR B 1 106 ? 1.395   -6.529  8.445   1.00 7.70  ? 106 THR B CB  1 
ATOM   3013  O  OG1 . THR B 1 106 ? 2.052   -5.981  9.590   1.00 7.98  ? 106 THR B OG1 1 
ATOM   3014  C  CG2 . THR B 1 106 ? 1.568   -5.648  7.217   1.00 8.97  ? 106 THR B CG2 1 
ATOM   3015  N  N   . VAL B 1 107 ? -0.249  -8.946  9.639   1.00 8.13  ? 107 VAL B N   1 
ATOM   3016  C  CA  . VAL B 1 107 ? -0.442  -9.906  10.744  1.00 9.01  ? 107 VAL B CA  1 
ATOM   3017  C  C   . VAL B 1 107 ? 0.782   -10.821 10.770  1.00 7.03  ? 107 VAL B C   1 
ATOM   3018  O  O   . VAL B 1 107 ? 1.202   -11.371 9.774   1.00 10.30 ? 107 VAL B O   1 
ATOM   3019  C  CB  . VAL B 1 107 ? -1.674  -10.807 10.470  1.00 9.62  ? 107 VAL B CB  1 
ATOM   3020  C  CG1 . VAL B 1 107 ? -1.783  -11.824 11.612  1.00 13.01 ? 107 VAL B CG1 1 
ATOM   3021  C  CG2 . VAL B 1 107 ? -2.993  -9.970  10.484  1.00 10.43 ? 107 VAL B CG2 1 
ATOM   3022  N  N   . SER B 1 108 ? 1.418   -10.762 11.928  1.00 10.22 ? 108 SER B N   1 
ATOM   3023  C  CA  . SER B 1 108 ? 2.744   -11.494 12.108  1.00 10.11 ? 108 SER B CA  1 
ATOM   3024  C  C   . SER B 1 108 ? 3.673   -11.212 10.916  1.00 10.98 ? 108 SER B C   1 
ATOM   3025  O  O   . SER B 1 108 ? 4.289   -12.121 10.297  1.00 13.65 ? 108 SER B O   1 
ATOM   3026  C  CB  . SER B 1 108 ? 2.498   -13.015 12.340  1.00 11.46 ? 108 SER B CB  1 
ATOM   3027  O  OG  . SER B 1 108 ? 1.571   -13.216 13.352  1.00 14.35 ? 108 SER B OG  1 
ATOM   3028  N  N   . GLY B 1 109 ? 3.766   -9.930  10.598  1.00 10.64 ? 109 GLY B N   1 
ATOM   3029  C  CA  . GLY B 1 109 ? 4.697   -9.514  9.589   1.00 11.91 ? 109 GLY B CA  1 
ATOM   3030  C  C   . GLY B 1 109 ? 4.284   -9.659  8.115   1.00 13.57 ? 109 GLY B C   1 
ATOM   3031  O  O   . GLY B 1 109 ? 5.067   -9.221  7.190   1.00 16.59 ? 109 GLY B O   1 
ATOM   3032  N  N   . GLN B 1 110 ? 3.101   -10.203 7.890   1.00 13.73 ? 110 GLN B N   1 
ATOM   3033  C  CA  . GLN B 1 110 ? 2.675   -10.456 6.497   1.00 14.77 ? 110 GLN B CA  1 
ATOM   3034  C  C   . GLN B 1 110 ? 1.548   -9.507  6.049   1.00 10.10 ? 110 GLN B C   1 
ATOM   3035  O  O   . GLN B 1 110 ? 0.600   -9.226  6.804   1.00 9.73  ? 110 GLN B O   1 
ATOM   3036  C  CB  . GLN B 1 110 ? 2.084   -11.814 6.457   1.00 14.92 ? 110 GLN B CB  1 
ATOM   3037  C  CG  . GLN B 1 110 ? 2.977   -13.045 7.005   1.00 17.47 ? 110 GLN B CG  1 
ATOM   3038  C  CD  . GLN B 1 110 ? 4.415   -12.984 6.511   1.00 23.70 ? 110 GLN B CD  1 
ATOM   3039  O  OE1 . GLN B 1 110 ? 4.668   -13.224 5.318   1.00 28.84 ? 110 GLN B OE1 1 
ATOM   3040  N  NE2 . GLN B 1 110 ? 5.382   -12.683 7.440   1.00 21.90 ? 110 GLN B NE2 1 
ATOM   3041  N  N   . HIS B 1 111 ? 1.794   -8.909  4.862   1.00 10.19 ? 111 HIS B N   1 
ATOM   3042  C  CA  . HIS B 1 111 ? 0.727   -8.184  4.183   1.00 10.43 ? 111 HIS B CA  1 
ATOM   3043  C  C   . HIS B 1 111 ? -0.298  -9.058  3.559   1.00 11.06 ? 111 HIS B C   1 
ATOM   3044  O  O   . HIS B 1 111 ? 0.063   -10.161 3.017   1.00 15.29 ? 111 HIS B O   1 
ATOM   3045  C  CB  . HIS B 1 111 ? 1.178   -7.352  2.984   1.00 12.67 ? 111 HIS B CB  1 
ATOM   3046  C  CG  . HIS B 1 111 ? 1.896   -6.103  3.376   1.00 9.96  ? 111 HIS B CG  1 
ATOM   3047  N  ND1 . HIS B 1 111 ? 1.243   -4.886  3.554   1.00 12.35 ? 111 HIS B ND1 1 
ATOM   3048  C  CD2 . HIS B 1 111 ? 3.207   -5.904  3.702   1.00 13.33 ? 111 HIS B CD2 1 
ATOM   3049  C  CE1 . HIS B 1 111 ? 2.159   -3.979  3.933   1.00 15.97 ? 111 HIS B CE1 1 
ATOM   3050  N  NE2 . HIS B 1 111 ? 3.355   -4.553  4.000   1.00 18.72 ? 111 HIS B NE2 1 
ATOM   3051  N  N   . PHE B 1 112 ? -1.553  -8.650  3.582   1.00 7.76  ? 112 PHE B N   1 
ATOM   3052  C  CA  . PHE B 1 112 ? -2.576  -9.165  2.796   1.00 7.88  ? 112 PHE B CA  1 
ATOM   3053  C  C   . PHE B 1 112 ? -2.657  -8.425  1.426   1.00 6.13  ? 112 PHE B C   1 
ATOM   3054  O  O   . PHE B 1 112 ? -1.868  -7.441  1.227   1.00 7.66  ? 112 PHE B O   1 
ATOM   3055  C  CB  . PHE B 1 112 ? -3.911  -9.082  3.546   1.00 9.19  ? 112 PHE B CB  1 
ATOM   3056  C  CG  . PHE B 1 112 ? -4.006  -10.139 4.617   1.00 8.94  ? 112 PHE B CG  1 
ATOM   3057  C  CD1 . PHE B 1 112 ? -4.626  -11.330 4.363   1.00 12.84 ? 112 PHE B CD1 1 
ATOM   3058  C  CD2 . PHE B 1 112 ? -3.317  -9.918  5.802   1.00 12.00 ? 112 PHE B CD2 1 
ATOM   3059  C  CE1 . PHE B 1 112 ? -4.641  -12.370 5.387   1.00 17.48 ? 112 PHE B CE1 1 
ATOM   3060  C  CE2 . PHE B 1 112 ? -3.356  -10.942 6.809   1.00 17.35 ? 112 PHE B CE2 1 
ATOM   3061  C  CZ  . PHE B 1 112 ? -4.016  -12.069 6.536   1.00 16.62 ? 112 PHE B CZ  1 
ATOM   3062  N  N   . ALA B 1 113 ? -3.456  -8.855  0.475   1.00 6.53  ? 113 ALA B N   1 
ATOM   3063  C  CA  . ALA B 1 113 ? -3.479  -8.242  -0.835  1.00 7.32  ? 113 ALA B CA  1 
ATOM   3064  C  C   . ALA B 1 113 ? -3.948  -6.834  -0.757  1.00 6.93  ? 113 ALA B C   1 
ATOM   3065  O  O   . ALA B 1 113 ? -3.501  -5.964  -1.507  1.00 7.57  ? 113 ALA B O   1 
ATOM   3066  C  CB  . ALA B 1 113 ? -4.354  -9.069  -1.787  1.00 9.82  ? 113 ALA B CB  1 
ATOM   3067  N  N   . ALA B 1 114 ? -4.983  -6.593  0.056   1.00 5.78  ? 114 ALA B N   1 
ATOM   3068  C  CA  . ALA B 1 114 ? -5.597  -5.226  0.051   1.00 5.09  ? 114 ALA B CA  1 
ATOM   3069  C  C   . ALA B 1 114 ? -6.349  -5.106  1.374   1.00 6.01  ? 114 ALA B C   1 
ATOM   3070  O  O   . ALA B 1 114 ? -6.350  -6.032  2.241   1.00 6.73  ? 114 ALA B O   1 
ATOM   3071  C  CB  . ALA B 1 114 ? -6.599  -5.040  -1.146  1.00 6.39  ? 114 ALA B CB  1 
ATOM   3072  N  N   . GLU B 1 115 ? -6.967  -3.938  1.613   1.00 5.31  ? 115 GLU B N   1 
ATOM   3073  C  CA  . GLU B 1 115 ? -7.711  -3.697  2.831   1.00 5.07  ? 115 GLU B CA  1 
ATOM   3074  C  C   . GLU B 1 115 ? -8.850  -2.768  2.606   1.00 6.34  ? 115 GLU B C   1 
ATOM   3075  O  O   . GLU B 1 115 ? -8.679  -1.749  1.866   1.00 6.74  ? 115 GLU B O   1 
ATOM   3076  C  CB  . GLU B 1 115 ? -6.764  -3.138  3.889   1.00 6.82  ? 115 GLU B CB  1 
ATOM   3077  C  CG  . GLU B 1 115 ? -7.314  -3.003  5.315   1.00 6.29  ? 115 GLU B CG  1 
ATOM   3078  C  CD  . GLU B 1 115 ? -6.232  -2.783  6.384   1.00 6.63  ? 115 GLU B CD  1 
ATOM   3079  O  OE1 . GLU B 1 115 ? -6.495  -2.116  7.437   1.00 6.77  ? 115 GLU B OE1 1 
ATOM   3080  O  OE2 . GLU B 1 115 ? -5.065  -3.220  6.173   1.00 5.46  ? 115 GLU B OE2 1 
ATOM   3081  N  N   . LEU B 1 116 ? -9.992  -3.054  3.186   1.00 5.17  ? 116 LEU B N   1 
ATOM   3082  C  CA  . LEU B 1 116 ? -11.186 -2.210  3.113   1.00 5.39  ? 116 LEU B CA  1 
ATOM   3083  C  C   . LEU B 1 116 ? -11.376 -1.517  4.435   1.00 4.16  ? 116 LEU B C   1 
ATOM   3084  O  O   . LEU B 1 116 ? -11.237 -2.151  5.540   1.00 5.78  ? 116 LEU B O   1 
ATOM   3085  C  CB  . LEU B 1 116 ? -12.435 -3.114  2.898   1.00 6.93  ? 116 LEU B CB  1 
ATOM   3086  C  CG  . LEU B 1 116 ? -13.796 -2.322  3.080   1.00 6.52  ? 116 LEU B CG  1 
ATOM   3087  C  CD1 . LEU B 1 116 ? -14.139 -1.513  1.825   1.00 7.92  ? 116 LEU B CD1 1 
ATOM   3088  C  CD2 . LEU B 1 116 ? -14.913 -3.358  3.166   1.00 7.54  ? 116 LEU B CD2 1 
ATOM   3089  N  N   . HIS B 1 117 ? -11.593 -0.199  4.425   1.00 4.03  ? 117 HIS B N   1 
ATOM   3090  C  CA  . HIS B 1 117 ? -11.954 0.577   5.645   1.00 5.09  ? 117 HIS B CA  1 
ATOM   3091  C  C   . HIS B 1 117 ? -13.341 1.117   5.475   1.00 5.66  ? 117 HIS B C   1 
ATOM   3092  O  O   . HIS B 1 117 ? -13.658 1.808   4.479   1.00 6.04  ? 117 HIS B O   1 
ATOM   3093  C  CB  . HIS B 1 117 ? -10.990 1.736   5.785   1.00 4.99  ? 117 HIS B CB  1 
ATOM   3094  C  CG  . HIS B 1 117 ? -9.616  1.262   6.121   1.00 5.34  ? 117 HIS B CG  1 
ATOM   3095  N  ND1 . HIS B 1 117 ? -8.462  2.003   5.870   1.00 5.62  ? 117 HIS B ND1 1 
ATOM   3096  C  CD2 . HIS B 1 117 ? -9.220  0.089   6.681   1.00 5.80  ? 117 HIS B CD2 1 
ATOM   3097  C  CE1 . HIS B 1 117 ? -7.402  1.343   6.287   1.00 7.27  ? 117 HIS B CE1 1 
ATOM   3098  N  NE2 . HIS B 1 117 ? -7.829  0.144   6.763   1.00 5.56  ? 117 HIS B NE2 1 
ATOM   3099  N  N   . ILE B 1 118 ? -14.176 0.807   6.506   1.00 6.12  ? 118 ILE B N   1 
ATOM   3100  C  CA  . ILE B 1 118 ? -15.522 1.414   6.549   1.00 6.50  ? 118 ILE B CA  1 
ATOM   3101  C  C   . ILE B 1 118 ? -15.525 2.408   7.693   1.00 7.71  ? 118 ILE B C   1 
ATOM   3102  O  O   . ILE B 1 118 ? -15.348 2.039   8.874   1.00 6.71  ? 118 ILE B O   1 
ATOM   3103  C  CB  . ILE B 1 118 ? -16.582 0.354   6.820   1.00 5.74  ? 118 ILE B CB  1 
ATOM   3104  C  CG1 . ILE B 1 118 ? -16.475 -0.835  5.795   1.00 6.26  ? 118 ILE B CG1 1 
ATOM   3105  C  CG2 . ILE B 1 118 ? -18.039 1.063   6.650   1.00 7.92  ? 118 ILE B CG2 1 
ATOM   3106  C  CD1 . ILE B 1 118 ? -17.603 -1.955  5.974   1.00 11.12 ? 118 ILE B CD1 1 
ATOM   3107  N  N   . VAL B 1 119 ? -15.498 3.722   7.356   1.00 7.26  ? 119 VAL B N   1 
ATOM   3108  C  CA  . VAL B 1 119 ? -15.267 4.811   8.301   1.00 6.93  ? 119 VAL B CA  1 
ATOM   3109  C  C   . VAL B 1 119 ? -16.624 5.249   8.878   1.00 7.33  ? 119 VAL B C   1 
ATOM   3110  O  O   . VAL B 1 119 ? -17.549 5.462   8.094   1.00 8.54  ? 119 VAL B O   1 
ATOM   3111  C  CB  . VAL B 1 119 ? -14.643 6.019   7.584   1.00 7.88  ? 119 VAL B CB  1 
ATOM   3112  C  CG1 . VAL B 1 119 ? -14.311 7.212   8.584   1.00 11.59 ? 119 VAL B CG1 1 
ATOM   3113  C  CG2 . VAL B 1 119 ? -13.303 5.570   6.819   1.00 8.60  ? 119 VAL B CG2 1 
ATOM   3114  N  N   . HIS B 1 120 ? -16.655 5.331   10.196  1.00 7.53  ? 120 HIS B N   1 
ATOM   3115  C  CA  . HIS B 1 120 ? -17.885 5.772   10.956  1.00 9.69  ? 120 HIS B CA  1 
ATOM   3116  C  C   . HIS B 1 120 ? -17.409 6.924   11.868  1.00 9.81  ? 120 HIS B C   1 
ATOM   3117  O  O   . HIS B 1 120 ? -16.258 7.077   12.261  1.00 9.06  ? 120 HIS B O   1 
ATOM   3118  C  CB  . HIS B 1 120 ? -18.433 4.610   11.799  1.00 8.57  ? 120 HIS B CB  1 
ATOM   3119  C  CG  . HIS B 1 120 ? -18.850 3.402   11.085  1.00 8.40  ? 120 HIS B CG  1 
ATOM   3120  N  ND1 . HIS B 1 120 ? -17.919 2.529   10.483  1.00 7.52  ? 120 HIS B ND1 1 
ATOM   3121  C  CD2 . HIS B 1 120 ? -20.053 2.829   10.918  1.00 9.11  ? 120 HIS B CD2 1 
ATOM   3122  C  CE1 . HIS B 1 120 ? -18.587 1.491   9.979   1.00 11.65 ? 120 HIS B CE1 1 
ATOM   3123  N  NE2 . HIS B 1 120 ? -19.900 1.637   10.224  1.00 10.44 ? 120 HIS B NE2 1 
ATOM   3124  N  N   . TYR B 1 121 ? -18.360 7.801   12.208  1.00 11.18 ? 121 TYR B N   1 
ATOM   3125  C  CA  . TYR B 1 121 ? -18.071 8.860   13.162  1.00 12.73 ? 121 TYR B CA  1 
ATOM   3126  C  C   . TYR B 1 121 ? -19.123 8.842   14.307  1.00 13.89 ? 121 TYR B C   1 
ATOM   3127  O  O   . TYR B 1 121 ? -20.183 8.298   14.157  1.00 12.29 ? 121 TYR B O   1 
ATOM   3128  C  CB  . TYR B 1 121 ? -18.102 10.228  12.474  1.00 14.80 ? 121 TYR B CB  1 
ATOM   3129  C  CG  . TYR B 1 121 ? -19.522 10.627  11.979  1.00 12.56 ? 121 TYR B CG  1 
ATOM   3130  C  CD1 . TYR B 1 121 ? -20.328 11.500  12.719  1.00 16.26 ? 121 TYR B CD1 1 
ATOM   3131  C  CD2 . TYR B 1 121 ? -19.999 10.082  10.793  1.00 12.75 ? 121 TYR B CD2 1 
ATOM   3132  C  CE1 . TYR B 1 121 ? -21.599 11.829  12.251  1.00 16.08 ? 121 TYR B CE1 1 
ATOM   3133  C  CE2 . TYR B 1 121 ? -21.253 10.394  10.299  1.00 13.90 ? 121 TYR B CE2 1 
ATOM   3134  C  CZ  . TYR B 1 121 ? -22.031 11.242  11.036  1.00 18.82 ? 121 TYR B CZ  1 
ATOM   3135  O  OH  . TYR B 1 121 ? -23.285 11.543  10.521  1.00 22.19 ? 121 TYR B OH  1 
ATOM   3136  N  N   . ASN B 1 122 ? -18.752 9.411   15.466  1.00 12.43 ? 122 ASN B N   1 
ATOM   3137  C  CA  . ASN B 1 122 ? -19.662 9.389   16.618  1.00 14.17 ? 122 ASN B CA  1 
ATOM   3138  C  C   . ASN B 1 122 ? -20.814 10.449  16.386  1.00 15.32 ? 122 ASN B C   1 
ATOM   3139  O  O   . ASN B 1 122 ? -20.581 11.646  16.608  1.00 16.70 ? 122 ASN B O   1 
ATOM   3140  C  CB  . ASN B 1 122 ? -18.881 9.736   17.912  1.00 15.72 ? 122 ASN B CB  1 
ATOM   3141  C  CG  . ASN B 1 122 ? -19.768 9.651   19.147  1.00 19.57 ? 122 ASN B CG  1 
ATOM   3142  O  OD1 . ASN B 1 122 ? -20.979 9.807   19.045  1.00 18.04 ? 122 ASN B OD1 1 
ATOM   3143  N  ND2 . ASN B 1 122 ? -19.169 9.343   20.286  1.00 24.32 ? 122 ASN B ND2 1 
ATOM   3144  N  N   . SER B 1 123 ? -21.924 9.984   15.812  1.00 17.55 ? 123 SER B N   1 
ATOM   3145  C  CA  . SER B 1 123 ? -23.077 10.860  15.500  1.00 16.67 ? 123 SER B CA  1 
ATOM   3146  C  C   . SER B 1 123 ? -23.849 11.277  16.776  1.00 20.56 ? 123 SER B C   1 
ATOM   3147  O  O   . SER B 1 123 ? -24.769 12.125  16.663  1.00 18.72 ? 123 SER B O   1 
ATOM   3148  C  CB  . SER B 1 123 ? -23.939 10.165  14.475  1.00 16.37 ? 123 SER B CB  1 
ATOM   3149  O  OG  . SER B 1 123 ? -24.267 8.883   14.882  1.00 18.50 ? 123 SER B OG  1 
ATOM   3150  N  N   . ASP B 1 124 ? -23.602 10.625  17.897  1.00 19.23 ? 124 ASP B N   1 
ATOM   3151  C  CA  . ASP B 1 124 ? -24.250 11.001  19.190  1.00 21.20 ? 124 ASP B CA  1 
ATOM   3152  C  C   . ASP B 1 124 ? -23.726 12.332  19.632  1.00 23.06 ? 124 ASP B C   1 
ATOM   3153  O  O   . ASP B 1 124 ? -24.503 13.149  20.188  1.00 22.92 ? 124 ASP B O   1 
ATOM   3154  C  CB  . ASP B 1 124 ? -24.047 9.935   20.263  1.00 22.58 ? 124 ASP B CB  1 
ATOM   3155  C  CG  . ASP B 1 124 ? -24.944 8.789   20.080  1.00 22.15 ? 124 ASP B CG  1 
ATOM   3156  O  OD1 . ASP B 1 124 ? -25.961 8.868   19.317  1.00 24.96 ? 124 ASP B OD1 1 
ATOM   3157  O  OD2 . ASP B 1 124 ? -24.686 7.737   20.725  1.00 25.33 ? 124 ASP B OD2 1 
ATOM   3158  N  N   . LEU B 1 125 ? -22.486 12.625  19.273  1.00 21.89 ? 125 LEU B N   1 
ATOM   3159  C  CA  . LEU B 1 125 ? -21.702 13.818  19.706  1.00 21.47 ? 125 LEU B CA  1 
ATOM   3160  C  C   . LEU B 1 125 ? -21.414 14.792  18.576  1.00 22.40 ? 125 LEU B C   1 
ATOM   3161  O  O   . LEU B 1 125 ? -21.196 16.024  18.834  1.00 26.23 ? 125 LEU B O   1 
ATOM   3162  C  CB  . LEU B 1 125 ? -20.371 13.442  20.289  1.00 23.54 ? 125 LEU B CB  1 
ATOM   3163  C  CG  . LEU B 1 125 ? -20.158 13.157  21.808  1.00 29.88 ? 125 LEU B CG  1 
ATOM   3164  C  CD1 . LEU B 1 125 ? -21.437 12.964  22.738  1.00 23.43 ? 125 LEU B CD1 1 
ATOM   3165  C  CD2 . LEU B 1 125 ? -19.048 12.155  22.143  1.00 22.69 ? 125 LEU B CD2 1 
ATOM   3166  N  N   . TYR B 1 126 ? -21.350 14.315  17.329  1.00 22.58 ? 126 TYR B N   1 
ATOM   3167  C  CA  . TYR B 1 126 ? -20.900 15.235  16.225  1.00 21.53 ? 126 TYR B CA  1 
ATOM   3168  C  C   . TYR B 1 126 ? -21.823 15.224  15.029  1.00 20.99 ? 126 TYR B C   1 
ATOM   3169  O  O   . TYR B 1 126 ? -22.482 14.201  14.772  1.00 20.93 ? 126 TYR B O   1 
ATOM   3170  C  CB  . TYR B 1 126 ? -19.428 14.912  15.800  1.00 23.60 ? 126 TYR B CB  1 
ATOM   3171  C  CG  . TYR B 1 126 ? -18.495 14.871  16.970  1.00 21.72 ? 126 TYR B CG  1 
ATOM   3172  C  CD1 . TYR B 1 126 ? -18.159 16.055  17.672  1.00 29.25 ? 126 TYR B CD1 1 
ATOM   3173  C  CD2 . TYR B 1 126 ? -17.967 13.651  17.427  1.00 23.47 ? 126 TYR B CD2 1 
ATOM   3174  C  CE1 . TYR B 1 126 ? -17.300 16.013  18.810  1.00 28.39 ? 126 TYR B CE1 1 
ATOM   3175  C  CE2 . TYR B 1 126 ? -17.140 13.578  18.534  1.00 24.07 ? 126 TYR B CE2 1 
ATOM   3176  C  CZ  . TYR B 1 126 ? -16.776 14.786  19.213  1.00 27.55 ? 126 TYR B CZ  1 
ATOM   3177  O  OH  . TYR B 1 126 ? -15.928 14.748  20.293  1.00 27.35 ? 126 TYR B OH  1 
ATOM   3178  N  N   . PRO B 1 127 ? -21.922 16.382  14.349  1.00 24.42 ? 127 PRO B N   1 
ATOM   3179  C  CA  . PRO B 1 127 ? -22.783 16.604  13.215  1.00 25.46 ? 127 PRO B CA  1 
ATOM   3180  C  C   . PRO B 1 127 ? -22.317 15.907  11.902  1.00 24.83 ? 127 PRO B C   1 
ATOM   3181  O  O   . PRO B 1 127 ? -23.112 15.682  11.003  1.00 26.01 ? 127 PRO B O   1 
ATOM   3182  C  CB  . PRO B 1 127 ? -22.749 18.151  13.090  1.00 25.47 ? 127 PRO B CB  1 
ATOM   3183  C  CG  . PRO B 1 127 ? -21.381 18.558  13.647  1.00 27.77 ? 127 PRO B CG  1 
ATOM   3184  C  CD  . PRO B 1 127 ? -21.151 17.580  14.766  1.00 25.87 ? 127 PRO B CD  1 
ATOM   3185  N  N   . ASP B 1 128 ? -21.034 15.518  11.813  1.00 23.36 ? 128 ASP B N   1 
ATOM   3186  C  CA  . ASP B 1 128 ? -20.514 14.996  10.570  1.00 21.79 ? 128 ASP B CA  1 
ATOM   3187  C  C   . ASP B 1 128 ? -19.134 14.443  10.871  1.00 21.55 ? 128 ASP B C   1 
ATOM   3188  O  O   . ASP B 1 128 ? -18.553 14.734  11.909  1.00 20.43 ? 128 ASP B O   1 
ATOM   3189  C  CB  . ASP B 1 128 ? -20.439 16.208  9.546   1.00 23.98 ? 128 ASP B CB  1 
ATOM   3190  C  CG  . ASP B 1 128 ? -19.527 17.325  10.006  1.00 28.15 ? 128 ASP B CG  1 
ATOM   3191  O  OD1 . ASP B 1 128 ? -19.951 18.186  10.811  1.00 34.78 ? 128 ASP B OD1 1 
ATOM   3192  O  OD2 . ASP B 1 128 ? -18.392 17.422  9.507   1.00 28.53 ? 128 ASP B OD2 1 
ATOM   3193  N  N   . ALA B 1 129 ? -18.573 13.661  9.948   1.00 19.45 ? 129 ALA B N   1 
ATOM   3194  C  CA  . ALA B 1 129 ? -17.256 13.069  10.124  1.00 19.39 ? 129 ALA B CA  1 
ATOM   3195  C  C   . ALA B 1 129 ? -16.097 14.012  10.161  1.00 18.00 ? 129 ALA B C   1 
ATOM   3196  O  O   . ALA B 1 129 ? -15.128 13.787  10.902  1.00 18.64 ? 129 ALA B O   1 
ATOM   3197  C  CB  . ALA B 1 129 ? -17.025 11.957  9.008   1.00 18.76 ? 129 ALA B CB  1 
ATOM   3198  N  N   A SER B 1 130 ? -16.268 15.111  9.408   0.50 20.00 ? 130 SER B N   1 
ATOM   3199  N  N   B SER B 1 130 ? -16.129 15.107  9.406   0.50 18.71 ? 130 SER B N   1 
ATOM   3200  C  CA  A SER B 1 130 ? -15.249 16.161  9.237   0.50 22.53 ? 130 SER B CA  1 
ATOM   3201  C  CA  B SER B 1 130 ? -14.972 16.032  9.437   0.50 19.43 ? 130 SER B CA  1 
ATOM   3202  C  C   A SER B 1 130 ? -14.925 16.826  10.556  0.50 23.04 ? 130 SER B C   1 
ATOM   3203  C  C   B SER B 1 130 ? -14.871 16.643  10.840  0.50 20.99 ? 130 SER B C   1 
ATOM   3204  O  O   A SER B 1 130 ? -13.722 17.037  10.834  0.50 22.97 ? 130 SER B O   1 
ATOM   3205  O  O   B SER B 1 130 ? -13.821 16.647  11.502  0.50 18.08 ? 130 SER B O   1 
ATOM   3206  C  CB  A SER B 1 130 ? -15.720 17.234  8.231   0.50 23.10 ? 130 SER B CB  1 
ATOM   3207  C  CB  B SER B 1 130 ? -15.071 17.084  8.303   0.50 19.17 ? 130 SER B CB  1 
ATOM   3208  O  OG  A SER B 1 130 ? -15.853 16.761  6.906   0.50 26.77 ? 130 SER B OG  1 
ATOM   3209  O  OG  B SER B 1 130 ? -14.156 18.144  8.457   0.50 19.38 ? 130 SER B OG  1 
ATOM   3210  N  N   . THR B 1 131 ? -15.980 17.130  11.343  1.00 23.46 ? 131 THR B N   1 
ATOM   3211  C  CA  . THR B 1 131 ? -15.940 17.669  12.696  1.00 24.55 ? 131 THR B CA  1 
ATOM   3212  C  C   . THR B 1 131 ? -15.458 16.678  13.701  1.00 23.06 ? 131 THR B C   1 
ATOM   3213  O  O   . THR B 1 131 ? -14.714 17.047  14.574  1.00 25.70 ? 131 THR B O   1 
ATOM   3214  C  CB  . THR B 1 131 ? -17.367 18.033  13.135  1.00 25.91 ? 131 THR B CB  1 
ATOM   3215  O  OG1 . THR B 1 131 ? -17.870 19.044  12.269  1.00 27.75 ? 131 THR B OG1 1 
ATOM   3216  C  CG2 . THR B 1 131 ? -17.495 18.392  14.682  1.00 26.75 ? 131 THR B CG2 1 
ATOM   3217  N  N   . ALA B 1 132 ? -15.900 15.394  13.617  1.00 21.73 ? 132 ALA B N   1 
ATOM   3218  C  CA  . ALA B 1 132 ? -15.488 14.319  14.526  1.00 21.25 ? 132 ALA B CA  1 
ATOM   3219  C  C   . ALA B 1 132 ? -13.980 14.039  14.448  1.00 18.31 ? 132 ALA B C   1 
ATOM   3220  O  O   . ALA B 1 132 ? -13.441 13.485  15.439  1.00 18.94 ? 132 ALA B O   1 
ATOM   3221  C  CB  . ALA B 1 132 ? -16.314 12.987  14.251  1.00 20.53 ? 132 ALA B CB  1 
ATOM   3222  N  N   . SER B 1 133 ? -13.384 14.319  13.278  1.00 19.65 ? 133 SER B N   1 
ATOM   3223  C  CA  . SER B 1 133 ? -12.072 13.719  12.879  1.00 21.13 ? 133 SER B CA  1 
ATOM   3224  C  C   . SER B 1 133 ? -10.973 14.251  13.767  1.00 25.26 ? 133 SER B C   1 
ATOM   3225  O  O   . SER B 1 133 ? -9.959  13.571  14.027  1.00 22.43 ? 133 SER B O   1 
ATOM   3226  C  CB  . SER B 1 133 ? -11.776 13.883  11.397  1.00 22.31 ? 133 SER B CB  1 
ATOM   3227  O  OG  . SER B 1 133 ? -11.551 15.242  10.987  1.00 23.36 ? 133 SER B OG  1 
ATOM   3228  N  N   . ASN B 1 134 ? -11.123 15.483  14.248  1.00 29.05 ? 134 ASN B N   1 
ATOM   3229  C  CA  . ASN B 1 134 ? -10.082 15.938  15.184  1.00 29.50 ? 134 ASN B CA  1 
ATOM   3230  C  C   . ASN B 1 134 ? -10.527 15.951  16.630  1.00 30.54 ? 134 ASN B C   1 
ATOM   3231  O  O   . ASN B 1 134 ? -10.003 16.723  17.403  1.00 33.73 ? 134 ASN B O   1 
ATOM   3232  C  CB  . ASN B 1 134 ? -9.345  17.224  14.691  1.00 30.83 ? 134 ASN B CB  1 
ATOM   3233  C  CG  . ASN B 1 134 ? -10.301 18.327  14.383  1.00 30.69 ? 134 ASN B CG  1 
ATOM   3234  O  OD1 . ASN B 1 134 ? -11.534 18.130  14.440  1.00 31.07 ? 134 ASN B OD1 1 
ATOM   3235  N  ND2 . ASN B 1 134 ? -9.759  19.524  14.053  1.00 32.53 ? 134 ASN B ND2 1 
ATOM   3236  N  N   . LYS B 1 135 ? -11.392 15.018  17.047  1.00 30.73 ? 135 LYS B N   1 
ATOM   3237  C  CA  . LYS B 1 135 ? -11.925 14.921  18.436  1.00 31.84 ? 135 LYS B CA  1 
ATOM   3238  C  C   . LYS B 1 135 ? -11.856 13.536  19.061  1.00 31.60 ? 135 LYS B C   1 
ATOM   3239  O  O   . LYS B 1 135 ? -11.768 12.527  18.336  1.00 26.89 ? 135 LYS B O   1 
ATOM   3240  C  CB  . LYS B 1 135 ? -13.359 15.526  18.494  1.00 34.43 ? 135 LYS B CB  1 
ATOM   3241  C  CG  . LYS B 1 135 ? -13.490 16.824  17.642  1.00 32.80 ? 135 LYS B CG  1 
ATOM   3242  C  CD  . LYS B 1 135 ? -14.469 17.877  18.176  1.00 34.97 ? 135 LYS B CD  1 
ATOM   3243  C  CE  . LYS B 1 135 ? -14.160 19.239  17.549  1.00 33.61 ? 135 LYS B CE  1 
ATOM   3244  N  NZ  . LYS B 1 135 ? -14.368 19.262  16.064  1.00 36.15 ? 135 LYS B NZ  1 
ATOM   3245  N  N   . SER B 1 136 ? -11.865 13.476  20.397  1.00 30.34 ? 136 SER B N   1 
ATOM   3246  C  CA  . SER B 1 136 ? -11.455 12.264  21.167  1.00 31.10 ? 136 SER B CA  1 
ATOM   3247  C  C   . SER B 1 136 ? -12.339 11.043  20.809  1.00 29.57 ? 136 SER B C   1 
ATOM   3248  O  O   . SER B 1 136 ? -13.508 11.201  20.958  1.00 31.13 ? 136 SER B O   1 
ATOM   3249  C  CB  . SER B 1 136 ? -11.588 12.553  22.714  1.00 32.04 ? 136 SER B CB  1 
ATOM   3250  O  OG  . SER B 1 136 ? -11.782 11.310  23.464  1.00 33.72 ? 136 SER B OG  1 
ATOM   3251  N  N   . GLU B 1 137 ? -11.819 9.904   20.312  1.00 29.64 ? 137 GLU B N   1 
ATOM   3252  C  CA  . GLU B 1 137 ? -12.682 8.747   19.879  1.00 29.35 ? 137 GLU B CA  1 
ATOM   3253  C  C   . GLU B 1 137 ? -13.820 9.163   18.916  1.00 25.50 ? 137 GLU B C   1 
ATOM   3254  O  O   . GLU B 1 137 ? -14.933 8.512   18.964  1.00 24.19 ? 137 GLU B O   1 
ATOM   3255  C  CB  . GLU B 1 137 ? -13.322 8.052   21.102  1.00 31.20 ? 137 GLU B CB  1 
ATOM   3256  C  CG  . GLU B 1 137 ? -14.245 9.002   21.962  1.00 37.54 ? 137 GLU B CG  1 
ATOM   3257  C  CD  . GLU B 1 137 ? -14.188 8.747   23.472  1.00 45.43 ? 137 GLU B CD  1 
ATOM   3258  O  OE1 . GLU B 1 137 ? -13.093 8.875   24.085  1.00 47.13 ? 137 GLU B OE1 1 
ATOM   3259  O  OE2 . GLU B 1 137 ? -15.262 8.409   24.040  1.00 47.52 ? 137 GLU B OE2 1 
ATOM   3260  N  N   . GLY B 1 138 ? -13.589 10.230  18.127  1.00 19.03 ? 138 GLY B N   1 
ATOM   3261  C  CA  . GLY B 1 138 ? -14.514 10.733  17.134  1.00 16.62 ? 138 GLY B CA  1 
ATOM   3262  C  C   . GLY B 1 138 ? -14.830 9.767   15.995  1.00 13.30 ? 138 GLY B C   1 
ATOM   3263  O  O   . GLY B 1 138 ? -15.897 9.859   15.371  1.00 14.53 ? 138 GLY B O   1 
ATOM   3264  N  N   . LEU B 1 139 ? -13.899 8.895   15.636  1.00 10.18 ? 139 LEU B N   1 
ATOM   3265  C  CA  . LEU B 1 139 ? -14.054 7.982   14.474  1.00 9.91  ? 139 LEU B CA  1 
ATOM   3266  C  C   . LEU B 1 139 ? -13.936 6.539   14.915  1.00 7.83  ? 139 LEU B C   1 
ATOM   3267  O  O   . LEU B 1 139 ? -13.242 6.238   15.910  1.00 10.34 ? 139 LEU B O   1 
ATOM   3268  C  CB  . LEU B 1 139 ? -12.980 8.303   13.473  1.00 12.29 ? 139 LEU B CB  1 
ATOM   3269  C  CG  . LEU B 1 139 ? -12.978 9.710   12.881  1.00 9.45  ? 139 LEU B CG  1 
ATOM   3270  C  CD1 . LEU B 1 139 ? -11.815 9.900   11.919  1.00 12.98 ? 139 LEU B CD1 1 
ATOM   3271  C  CD2 . LEU B 1 139 ? -14.343 9.992   12.193  1.00 11.32 ? 139 LEU B CD2 1 
ATOM   3272  N  N   . ALA B 1 140 ? -14.566 5.654   14.188  1.00 9.71  ? 140 ALA B N   1 
ATOM   3273  C  CA  . ALA B 1 140 ? -14.366 4.228   14.406  1.00 9.22  ? 140 ALA B CA  1 
ATOM   3274  C  C   . ALA B 1 140 ? -14.353 3.662   13.001  1.00 9.34  ? 140 ALA B C   1 
ATOM   3275  O  O   . ALA B 1 140 ? -15.239 3.932   12.137  1.00 9.90  ? 140 ALA B O   1 
ATOM   3276  C  CB  . ALA B 1 140 ? -15.520 3.689   15.157  1.00 9.39  ? 140 ALA B CB  1 
ATOM   3277  N  N   . VAL B 1 141 ? -13.294 2.880   12.728  1.00 7.35  ? 141 VAL B N   1 
ATOM   3278  C  CA  . VAL B 1 141 ? -13.140 2.237   11.430  1.00 6.67  ? 141 VAL B CA  1 
ATOM   3279  C  C   . VAL B 1 141 ? -13.280 0.738   11.578  1.00 7.58  ? 141 VAL B C   1 
ATOM   3280  O  O   . VAL B 1 141 ? -12.672 0.152   12.542  1.00 8.60  ? 141 VAL B O   1 
ATOM   3281  C  CB  . VAL B 1 141 ? -11.778 2.561   10.831  1.00 5.87  ? 141 VAL B CB  1 
ATOM   3282  C  CG1 . VAL B 1 141 ? -11.633 1.883   9.486   1.00 10.07 ? 141 VAL B CG1 1 
ATOM   3283  C  CG2 . VAL B 1 141 ? -11.715 4.071   10.628  1.00 7.84  ? 141 VAL B CG2 1 
ATOM   3284  N  N   . LEU B 1 142 ? -13.998 0.113   10.664  1.00 5.90  ? 142 LEU B N   1 
ATOM   3285  C  CA  . LEU B 1 142 ? -13.987 -1.332  10.556  1.00 7.18  ? 142 LEU B CA  1 
ATOM   3286  C  C   . LEU B 1 142 ? -13.038 -1.663  9.432   1.00 8.35  ? 142 LEU B C   1 
ATOM   3287  O  O   . LEU B 1 142 ? -13.184 -1.145  8.309   1.00 8.58  ? 142 LEU B O   1 
ATOM   3288  C  CB  . LEU B 1 142 ? -15.328 -1.890  10.193  1.00 8.14  ? 142 LEU B CB  1 
ATOM   3289  C  CG  . LEU B 1 142 ? -16.482 -1.640  11.135  1.00 7.87  ? 142 LEU B CG  1 
ATOM   3290  C  CD1 . LEU B 1 142 ? -17.770 -2.295  10.680  1.00 10.65 ? 142 LEU B CD1 1 
ATOM   3291  C  CD2 . LEU B 1 142 ? -16.187 -2.055  12.622  1.00 8.48  ? 142 LEU B CD2 1 
ATOM   3292  N  N   . ALA B 1 143 ? -12.019 -2.515  9.688   1.00 7.28  ? 143 ALA B N   1 
ATOM   3293  C  CA  . ALA B 1 143 ? -11.061 -2.907  8.656   1.00 5.13  ? 143 ALA B CA  1 
ATOM   3294  C  C   . ALA B 1 143 ? -11.206 -4.342  8.303   1.00 5.98  ? 143 ALA B C   1 
ATOM   3295  O  O   . ALA B 1 143 ? -11.226 -5.229  9.211   1.00 6.46  ? 143 ALA B O   1 
ATOM   3296  C  CB  . ALA B 1 143 ? -9.594  -2.641  9.162   1.00 6.57  ? 143 ALA B CB  1 
ATOM   3297  N  N   . VAL B 1 144 ? -11.261 -4.617  6.975   1.00 3.96  ? 144 VAL B N   1 
ATOM   3298  C  CA  . VAL B 1 144 ? -11.329 -6.020  6.474   1.00 5.46  ? 144 VAL B CA  1 
ATOM   3299  C  C   . VAL B 1 144 ? -10.067 -6.253  5.680   1.00 8.39  ? 144 VAL B C   1 
ATOM   3300  O  O   . VAL B 1 144 ? -9.791  -5.558  4.685   1.00 6.53  ? 144 VAL B O   1 
ATOM   3301  C  CB  . VAL B 1 144 ? -12.569 -6.195  5.580   1.00 4.93  ? 144 VAL B CB  1 
ATOM   3302  C  CG1 . VAL B 1 144 ? -12.616 -7.662  5.120   1.00 7.29  ? 144 VAL B CG1 1 
ATOM   3303  C  CG2 . VAL B 1 144 ? -13.868 -5.883  6.370   1.00 7.01  ? 144 VAL B CG2 1 
ATOM   3304  N  N   . LEU B 1 145 ? -9.349  -7.337  6.058   1.00 6.56  ? 145 LEU B N   1 
ATOM   3305  C  CA  . LEU B 1 145 ? -8.152  -7.748  5.342   1.00 7.45  ? 145 LEU B CA  1 
ATOM   3306  C  C   . LEU B 1 145 ? -8.630  -8.531  4.104   1.00 6.53  ? 145 LEU B C   1 
ATOM   3307  O  O   . LEU B 1 145 ? -9.564  -9.368  4.226   1.00 6.87  ? 145 LEU B O   1 
ATOM   3308  C  CB  . LEU B 1 145 ? -7.293  -8.651  6.257   1.00 8.52  ? 145 LEU B CB  1 
ATOM   3309  C  CG  . LEU B 1 145 ? -6.832  -7.895  7.529   1.00 9.77  ? 145 LEU B CG  1 
ATOM   3310  C  CD1 . LEU B 1 145 ? -6.209  -8.899  8.560   1.00 11.62 ? 145 LEU B CD1 1 
ATOM   3311  C  CD2 . LEU B 1 145 ? -5.722  -6.874  7.154   1.00 11.29 ? 145 LEU B CD2 1 
ATOM   3312  N  N   . ILE B 1 146 ? -8.022  -8.340  2.941   1.00 6.35  ? 146 ILE B N   1 
ATOM   3313  C  CA  . ILE B 1 146 ? -8.478  -8.923  1.702   1.00 6.44  ? 146 ILE B CA  1 
ATOM   3314  C  C   . ILE B 1 146 ? -7.308  -9.734  1.155   1.00 6.80  ? 146 ILE B C   1 
ATOM   3315  O  O   . ILE B 1 146 ? -6.159  -9.257  1.015   1.00 6.75  ? 146 ILE B O   1 
ATOM   3316  C  CB  . ILE B 1 146 ? -8.899  -7.861  0.678   1.00 7.16  ? 146 ILE B CB  1 
ATOM   3317  C  CG1 . ILE B 1 146 ? -10.054 -7.052  1.223   1.00 8.18  ? 146 ILE B CG1 1 
ATOM   3318  C  CG2 . ILE B 1 146 ? -9.154  -8.546  -0.657  1.00 7.61  ? 146 ILE B CG2 1 
ATOM   3319  C  CD1 . ILE B 1 146 ? -10.335 -5.763  0.370   1.00 7.18  ? 146 ILE B CD1 1 
ATOM   3320  N  N   . GLU B 1 147 ? -7.602  -11.011 0.864   1.00 7.06  ? 147 GLU B N   1 
ATOM   3321  C  CA  . GLU B 1 147 ? -6.601  -11.898 0.306   1.00 9.69  ? 147 GLU B CA  1 
ATOM   3322  C  C   . GLU B 1 147 ? -6.992  -12.333 -1.136  1.00 8.55  ? 147 GLU B C   1 
ATOM   3323  O  O   . GLU B 1 147 ? -8.192  -12.359 -1.441  1.00 8.27  ? 147 GLU B O   1 
ATOM   3324  C  CB  . GLU B 1 147 ? -6.350  -13.129 1.175   1.00 13.70 ? 147 GLU B CB  1 
ATOM   3325  C  CG  . GLU B 1 147 ? -7.535  -13.959 1.551   1.00 18.77 ? 147 GLU B CG  1 
ATOM   3326  C  CD  . GLU B 1 147 ? -7.130  -15.195 2.323   1.00 20.60 ? 147 GLU B CD  1 
ATOM   3327  O  OE1 . GLU B 1 147 ? -6.014  -15.223 2.888   1.00 19.20 ? 147 GLU B OE1 1 
ATOM   3328  O  OE2 . GLU B 1 147 ? -7.930  -16.154 2.338   1.00 28.05 ? 147 GLU B OE2 1 
ATOM   3329  N  N   . MET B 1 148 ? -6.038  -12.664 -1.941  1.00 7.34  ? 148 MET B N   1 
ATOM   3330  C  CA  . MET B 1 148 ? -6.285  -13.212 -3.216  1.00 7.68  ? 148 MET B CA  1 
ATOM   3331  C  C   . MET B 1 148 ? -6.853  -14.640 -3.101  1.00 8.27  ? 148 MET B C   1 
ATOM   3332  O  O   . MET B 1 148 ? -6.225  -15.527 -2.433  1.00 9.13  ? 148 MET B O   1 
ATOM   3333  C  CB  . MET B 1 148 ? -4.976  -13.233 -4.044  1.00 7.81  ? 148 MET B CB  1 
ATOM   3334  C  CG  . MET B 1 148 ? -5.246  -13.589 -5.496  1.00 9.93  ? 148 MET B CG  1 
ATOM   3335  S  SD  . MET B 1 148 ? -3.683  -13.744 -6.459  1.00 10.65 ? 148 MET B SD  1 
ATOM   3336  C  CE  . MET B 1 148 ? -3.268  -12.058 -6.502  1.00 10.81 ? 148 MET B CE  1 
ATOM   3337  N  N   . GLY B 1 149 ? -8.033  -14.775 -3.747  1.00 6.75  ? 149 GLY B N   1 
ATOM   3338  C  CA  . GLY B 1 149 ? -8.763  -16.063 -3.625  1.00 7.27  ? 149 GLY B CA  1 
ATOM   3339  C  C   . GLY B 1 149 ? -9.809  -16.097 -4.691  1.00 5.79  ? 149 GLY B C   1 
ATOM   3340  O  O   . GLY B 1 149 ? -9.622  -15.809 -5.847  1.00 7.82  ? 149 GLY B O   1 
ATOM   3341  N  N   . SER B 1 150 ? -10.992 -16.553 -4.236  1.00 7.63  ? 150 SER B N   1 
ATOM   3342  C  CA  . SER B 1 150 ? -12.154 -16.644 -5.102  1.00 8.86  ? 150 SER B CA  1 
ATOM   3343  C  C   . SER B 1 150 ? -12.700 -15.265 -5.478  1.00 8.79  ? 150 SER B C   1 
ATOM   3344  O  O   . SER B 1 150 ? -12.669 -14.309 -4.682  1.00 10.05 ? 150 SER B O   1 
ATOM   3345  C  CB  . SER B 1 150 ? -13.287 -17.390 -4.337  1.00 7.11  ? 150 SER B CB  1 
ATOM   3346  O  OG  . SER B 1 150 ? -12.960 -18.814 -4.205  1.00 9.03  ? 150 SER B OG  1 
ATOM   3347  N  N   . PHE B 1 151 ? -13.319 -15.296 -6.658  1.00 7.79  ? 151 PHE B N   1 
ATOM   3348  C  CA  . PHE B 1 151 ? -14.094 -14.111 -7.120  1.00 8.15  ? 151 PHE B CA  1 
ATOM   3349  C  C   . PHE B 1 151 ? -15.131 -13.803 -6.064  1.00 8.97  ? 151 PHE B C   1 
ATOM   3350  O  O   . PHE B 1 151 ? -15.783 -14.688 -5.448  1.00 10.85 ? 151 PHE B O   1 
ATOM   3351  C  CB  . PHE B 1 151 ? -14.815 -14.427 -8.445  1.00 9.58  ? 151 PHE B CB  1 
ATOM   3352  C  CG  . PHE B 1 151 ? -15.632 -13.274 -8.970  1.00 9.40  ? 151 PHE B CG  1 
ATOM   3353  C  CD1 . PHE B 1 151 ? -15.010 -12.200 -9.589  1.00 12.83 ? 151 PHE B CD1 1 
ATOM   3354  C  CD2 . PHE B 1 151 ? -17.015 -13.253 -8.830  1.00 11.61 ? 151 PHE B CD2 1 
ATOM   3355  C  CE1 . PHE B 1 151 ? -15.745 -11.143 -10.071 1.00 11.00 ? 151 PHE B CE1 1 
ATOM   3356  C  CE2 . PHE B 1 151 ? -17.753 -12.193 -9.314  1.00 10.56 ? 151 PHE B CE2 1 
ATOM   3357  C  CZ  . PHE B 1 151 ? -17.113 -11.134 -9.930  1.00 8.30  ? 151 PHE B CZ  1 
ATOM   3358  N  N   . ASN B 1 152 ? -15.386 -12.453 -5.829  1.00 7.65  ? 152 ASN B N   1 
ATOM   3359  C  CA  . ASN B 1 152 ? -16.270 -12.028 -4.804  1.00 7.47  ? 152 ASN B CA  1 
ATOM   3360  C  C   . ASN B 1 152 ? -17.371 -11.134 -5.442  1.00 9.55  ? 152 ASN B C   1 
ATOM   3361  O  O   . ASN B 1 152 ? -17.076 -9.947  -5.740  1.00 8.79  ? 152 ASN B O   1 
ATOM   3362  C  CB  . ASN B 1 152 ? -15.457 -11.227 -3.690  1.00 6.29  ? 152 ASN B CB  1 
ATOM   3363  C  CG  . ASN B 1 152 ? -16.291 -10.989 -2.471  1.00 8.01  ? 152 ASN B CG  1 
ATOM   3364  O  OD1 . ASN B 1 152 ? -17.431 -10.490 -2.559  1.00 8.37  ? 152 ASN B OD1 1 
ATOM   3365  N  ND2 . ASN B 1 152 ? -15.725 -11.274 -1.266  1.00 8.22  ? 152 ASN B ND2 1 
ATOM   3366  N  N   . PRO B 1 153 ? -18.592 -11.601 -5.626  1.00 8.29  ? 153 PRO B N   1 
ATOM   3367  C  CA  . PRO B 1 153 ? -19.639 -10.836 -6.302  1.00 8.20  ? 153 PRO B CA  1 
ATOM   3368  C  C   . PRO B 1 153 ? -19.910 -9.594  -5.513  1.00 10.67 ? 153 PRO B C   1 
ATOM   3369  O  O   . PRO B 1 153 ? -20.271 -8.541  -6.166  1.00 11.45 ? 153 PRO B O   1 
ATOM   3370  C  CB  . PRO B 1 153 ? -20.834 -11.814 -6.359  1.00 10.23 ? 153 PRO B CB  1 
ATOM   3371  C  CG  . PRO B 1 153 ? -20.272 -13.155 -6.285  1.00 14.43 ? 153 PRO B CG  1 
ATOM   3372  C  CD  . PRO B 1 153 ? -18.973 -13.027 -5.382  1.00 10.40 ? 153 PRO B CD  1 
ATOM   3373  N  N   . SER B 1 154 ? -19.873 -9.629  -4.189  1.00 9.40  ? 154 SER B N   1 
ATOM   3374  C  CA  . SER B 1 154 ? -20.244 -8.404  -3.454  1.00 8.87  ? 154 SER B CA  1 
ATOM   3375  C  C   . SER B 1 154 ? -19.230 -7.300  -3.643  1.00 9.24  ? 154 SER B C   1 
ATOM   3376  O  O   . SER B 1 154 ? -19.565 -6.072  -3.840  1.00 8.85  ? 154 SER B O   1 
ATOM   3377  C  CB  . SER B 1 154 ? -20.307 -8.707  -1.964  1.00 12.46 ? 154 SER B CB  1 
ATOM   3378  O  OG  . SER B 1 154 ? -21.322 -9.687  -1.749  1.00 16.35 ? 154 SER B OG  1 
ATOM   3379  N  N   . TYR B 1 155 ? -17.898 -7.599  -3.580  1.00 7.49  ? 155 TYR B N   1 
ATOM   3380  C  CA  . TYR B 1 155 ? -16.923 -6.525  -3.860  1.00 7.57  ? 155 TYR B CA  1 
ATOM   3381  C  C   . TYR B 1 155 ? -17.072 -6.069  -5.286  1.00 7.78  ? 155 TYR B C   1 
ATOM   3382  O  O   . TYR B 1 155 ? -16.716 -4.914  -5.620  1.00 7.94  ? 155 TYR B O   1 
ATOM   3383  C  CB  . TYR B 1 155 ? -15.473 -6.977  -3.555  1.00 7.23  ? 155 TYR B CB  1 
ATOM   3384  C  CG  . TYR B 1 155 ? -15.114 -6.885  -2.084  1.00 7.28  ? 155 TYR B CG  1 
ATOM   3385  C  CD1 . TYR B 1 155 ? -14.375 -5.795  -1.525  1.00 8.03  ? 155 TYR B CD1 1 
ATOM   3386  C  CD2 . TYR B 1 155 ? -15.536 -7.847  -1.174  1.00 6.86  ? 155 TYR B CD2 1 
ATOM   3387  C  CE1 . TYR B 1 155 ? -14.096 -5.674  -0.208  1.00 7.86  ? 155 TYR B CE1 1 
ATOM   3388  C  CE2 . TYR B 1 155 ? -15.282 -7.750  0.174   1.00 9.09  ? 155 TYR B CE2 1 
ATOM   3389  C  CZ  . TYR B 1 155 ? -14.554 -6.642  0.671   1.00 8.63  ? 155 TYR B CZ  1 
ATOM   3390  O  OH  . TYR B 1 155 ? -14.225 -6.450  1.975   1.00 8.42  ? 155 TYR B OH  1 
ATOM   3391  N  N   . ASP B 1 156 ? -17.511 -6.875  -6.175  1.00 7.06  ? 156 ASP B N   1 
ATOM   3392  C  CA  . ASP B 1 156 ? -17.654 -6.522  -7.582  1.00 7.17  ? 156 ASP B CA  1 
ATOM   3393  C  C   . ASP B 1 156 ? -18.753 -5.463  -7.717  1.00 7.58  ? 156 ASP B C   1 
ATOM   3394  O  O   . ASP B 1 156 ? -18.753 -4.739  -8.786  1.00 10.03 ? 156 ASP B O   1 
ATOM   3395  C  CB  . ASP B 1 156 ? -17.792 -7.706  -8.620  1.00 9.26  ? 156 ASP B CB  1 
ATOM   3396  C  CG  . ASP B 1 156 ? -16.830 -7.561  -9.782  1.00 8.30  ? 156 ASP B CG  1 
ATOM   3397  O  OD1 . ASP B 1 156 ? -15.621 -7.362  -9.528  1.00 9.12  ? 156 ASP B OD1 1 
ATOM   3398  O  OD2 . ASP B 1 156 ? -17.279 -7.621  -10.941 1.00 15.88 ? 156 ASP B OD2 1 
ATOM   3399  N  N   . LYS B 1 157 ? -19.682 -5.331  -6.749  1.00 7.77  ? 157 LYS B N   1 
ATOM   3400  C  CA  . LYS B 1 157 ? -20.720 -4.262  -6.907  1.00 9.31  ? 157 LYS B CA  1 
ATOM   3401  C  C   . LYS B 1 157 ? -19.981 -2.958  -6.799  1.00 10.34 ? 157 LYS B C   1 
ATOM   3402  O  O   . LYS B 1 157 ? -20.478 -2.009  -7.431  1.00 11.25 ? 157 LYS B O   1 
ATOM   3403  C  CB  . LYS B 1 157 ? -21.743 -4.405  -5.823  1.00 11.13 ? 157 LYS B CB  1 
ATOM   3404  C  CG  . LYS B 1 157 ? -22.583 -5.710  -5.979  1.00 13.24 ? 157 LYS B CG  1 
ATOM   3405  C  CD  . LYS B 1 157 ? -23.564 -6.011  -4.822  1.00 16.70 ? 157 LYS B CD  1 
ATOM   3406  C  CE  . LYS B 1 157 ? -24.315 -7.380  -5.120  1.00 18.10 ? 157 LYS B CE  1 
ATOM   3407  N  NZ  . LYS B 1 157 ? -25.111 -7.706  -3.827  1.00 21.86 ? 157 LYS B NZ  1 
ATOM   3408  N  N   . ILE B 1 158 ? -18.777 -2.907  -6.218  1.00 9.60  ? 158 ILE B N   1 
ATOM   3409  C  CA  . ILE B 1 158 ? -17.967 -1.613  -6.242  1.00 9.76  ? 158 ILE B CA  1 
ATOM   3410  C  C   . ILE B 1 158 ? -17.052 -1.654  -7.430  1.00 9.26  ? 158 ILE B C   1 
ATOM   3411  O  O   . ILE B 1 158 ? -17.032 -0.716  -8.253  1.00 10.36 ? 158 ILE B O   1 
ATOM   3412  C  CB  . ILE B 1 158 ? -17.127 -1.526  -4.983  1.00 9.18  ? 158 ILE B CB  1 
ATOM   3413  C  CG1 . ILE B 1 158 ? -18.077 -1.270  -3.828  1.00 11.95 ? 158 ILE B CG1 1 
ATOM   3414  C  CG2 . ILE B 1 158 ? -16.126 -0.289  -5.095  1.00 10.39 ? 158 ILE B CG2 1 
ATOM   3415  C  CD1 . ILE B 1 158 ? -17.329 -1.421  -2.432  1.00 17.48 ? 158 ILE B CD1 1 
ATOM   3416  N  N   . PHE B 1 159 ? -16.306 -2.762  -7.718  1.00 8.15  ? 159 PHE B N   1 
ATOM   3417  C  CA  . PHE B 1 159 ? -15.288 -2.723  -8.692  1.00 8.48  ? 159 PHE B CA  1 
ATOM   3418  C  C   . PHE B 1 159 ? -15.851 -2.603  -10.081 1.00 10.58 ? 159 PHE B C   1 
ATOM   3419  O  O   . PHE B 1 159 ? -15.141 -2.135  -10.993 1.00 12.69 ? 159 PHE B O   1 
ATOM   3420  C  CB  . PHE B 1 159 ? -14.417 -3.990  -8.638  1.00 8.00  ? 159 PHE B CB  1 
ATOM   3421  C  CG  . PHE B 1 159 ? -13.730 -4.204  -7.317  1.00 9.22  ? 159 PHE B CG  1 
ATOM   3422  C  CD1 . PHE B 1 159 ? -13.350 -3.146  -6.447  1.00 9.28  ? 159 PHE B CD1 1 
ATOM   3423  C  CD2 . PHE B 1 159 ? -13.416 -5.567  -6.900  1.00 9.71  ? 159 PHE B CD2 1 
ATOM   3424  C  CE1 . PHE B 1 159 ? -12.626 -3.467  -5.187  1.00 10.98 ? 159 PHE B CE1 1 
ATOM   3425  C  CE2 . PHE B 1 159 ? -12.776 -5.789  -5.751  1.00 10.47 ? 159 PHE B CE2 1 
ATOM   3426  C  CZ  . PHE B 1 159 ? -12.359 -4.787  -4.926  1.00 11.59 ? 159 PHE B CZ  1 
ATOM   3427  N  N   . SER B 1 160 ? -17.076 -2.985  -10.280 1.00 10.23 ? 160 SER B N   1 
ATOM   3428  C  CA  . SER B 1 160 ? -17.579 -2.947  -11.713 1.00 11.85 ? 160 SER B CA  1 
ATOM   3429  C  C   . SER B 1 160 ? -17.763 -1.503  -12.095 1.00 12.98 ? 160 SER B C   1 
ATOM   3430  O  O   . SER B 1 160 ? -17.970 -1.244  -13.309 1.00 15.03 ? 160 SER B O   1 
ATOM   3431  C  CB  . SER B 1 160 ? -18.929 -3.721  -11.819 1.00 14.11 ? 160 SER B CB  1 
ATOM   3432  O  OG  . SER B 1 160 ? -19.860 -3.204  -10.965 1.00 15.19 ? 160 SER B OG  1 
ATOM   3433  N  N   . HIS B 1 161 ? -17.643 -0.524  -11.168 1.00 12.17 ? 161 HIS B N   1 
ATOM   3434  C  CA  . HIS B 1 161 ? -17.794 0.930   -11.512 1.00 12.89 ? 161 HIS B CA  1 
ATOM   3435  C  C   . HIS B 1 161 ? -16.476 1.658   -11.657 1.00 15.50 ? 161 HIS B C   1 
ATOM   3436  O  O   . HIS B 1 161 ? -16.535 2.903   -11.914 1.00 14.23 ? 161 HIS B O   1 
ATOM   3437  C  CB  . HIS B 1 161 ? -18.655 1.607   -10.478 1.00 14.37 ? 161 HIS B CB  1 
ATOM   3438  C  CG  . HIS B 1 161 ? -20.057 1.119   -10.484 1.00 17.86 ? 161 HIS B CG  1 
ATOM   3439  N  ND1 . HIS B 1 161 ? -20.997 1.591   -11.391 1.00 17.23 ? 161 HIS B ND1 1 
ATOM   3440  C  CD2 . HIS B 1 161 ? -20.641 0.086   -9.842  1.00 16.74 ? 161 HIS B CD2 1 
ATOM   3441  C  CE1 . HIS B 1 161 ? -22.148 0.962   -11.171 1.00 19.83 ? 161 HIS B CE1 1 
ATOM   3442  N  NE2 . HIS B 1 161 ? -21.947 0.024   -10.246 1.00 16.23 ? 161 HIS B NE2 1 
ATOM   3443  N  N   . LEU B 1 162 ? -15.344 0.985   -11.518 1.00 15.77 ? 162 LEU B N   1 
ATOM   3444  C  CA  . LEU B 1 162 ? -14.058 1.674   -11.411 1.00 18.29 ? 162 LEU B CA  1 
ATOM   3445  C  C   . LEU B 1 162 ? -13.742 2.419   -12.673 1.00 19.68 ? 162 LEU B C   1 
ATOM   3446  O  O   . LEU B 1 162 ? -13.181 3.528   -12.548 1.00 19.84 ? 162 LEU B O   1 
ATOM   3447  C  CB  . LEU B 1 162 ? -12.941 0.716   -11.123 1.00 17.11 ? 162 LEU B CB  1 
ATOM   3448  C  CG  . LEU B 1 162 ? -13.111 0.074   -9.705  1.00 20.68 ? 162 LEU B CG  1 
ATOM   3449  C  CD1 . LEU B 1 162 ? -11.996 -0.780  -9.540  1.00 18.23 ? 162 LEU B CD1 1 
ATOM   3450  C  CD2 . LEU B 1 162 ? -13.260 1.138   -8.494  1.00 22.05 ? 162 LEU B CD2 1 
ATOM   3451  N  N   . GLN B 1 163 ? -14.099 1.883   -13.847 1.00 18.89 ? 163 GLN B N   1 
ATOM   3452  C  CA  . GLN B 1 163 ? -13.695 2.589   -15.104 1.00 18.96 ? 163 GLN B CA  1 
ATOM   3453  C  C   . GLN B 1 163 ? -14.477 3.913   -15.289 1.00 20.08 ? 163 GLN B C   1 
ATOM   3454  O  O   . GLN B 1 163 ? -14.189 4.635   -16.291 1.00 22.88 ? 163 GLN B O   1 
ATOM   3455  C  CB  . GLN B 1 163 ? -13.805 1.713   -16.420 1.00 22.72 ? 163 GLN B CB  1 
ATOM   3456  C  CG  . GLN B 1 163 ? -12.896 0.387   -16.497 1.00 23.18 ? 163 GLN B CG  1 
ATOM   3457  C  CD  . GLN B 1 163 ? -11.344 0.577   -16.312 1.00 26.80 ? 163 GLN B CD  1 
ATOM   3458  O  OE1 . GLN B 1 163 ? -10.782 1.591   -16.695 1.00 29.62 ? 163 GLN B OE1 1 
ATOM   3459  N  NE2 . GLN B 1 163 ? -10.668 -0.431  -15.708 1.00 30.65 ? 163 GLN B NE2 1 
ATOM   3460  N  N   A HIS B 1 164 ? -15.358 4.241   -14.389 0.50 17.19 ? 164 HIS B N   1 
ATOM   3461  N  N   B HIS B 1 164 ? -15.508 4.184   -14.470 0.50 17.52 ? 164 HIS B N   1 
ATOM   3462  C  CA  A HIS B 1 164 ? -16.102 5.451   -14.448 0.50 15.55 ? 164 HIS B CA  1 
ATOM   3463  C  CA  B HIS B 1 164 ? -16.261 5.460   -14.409 0.50 17.39 ? 164 HIS B CA  1 
ATOM   3464  C  C   A HIS B 1 164 ? -15.684 6.493   -13.379 0.50 13.42 ? 164 HIS B C   1 
ATOM   3465  C  C   B HIS B 1 164 ? -15.627 6.507   -13.468 0.50 14.23 ? 164 HIS B C   1 
ATOM   3466  O  O   A HIS B 1 164 ? -16.235 7.614   -13.226 0.50 13.31 ? 164 HIS B O   1 
ATOM   3467  O  O   B HIS B 1 164 ? -16.073 7.660   -13.441 0.50 14.80 ? 164 HIS B O   1 
ATOM   3468  C  CB  A HIS B 1 164 ? -17.550 5.004   -14.452 0.50 16.35 ? 164 HIS B CB  1 
ATOM   3469  C  CB  B HIS B 1 164 ? -17.749 5.311   -13.922 0.50 16.69 ? 164 HIS B CB  1 
ATOM   3470  C  CG  A HIS B 1 164 ? -17.750 3.822   -15.359 0.50 13.57 ? 164 HIS B CG  1 
ATOM   3471  C  CG  B HIS B 1 164 ? -18.796 5.263   -15.002 0.50 22.14 ? 164 HIS B CG  1 
ATOM   3472  N  ND1 A HIS B 1 164 ? -17.346 3.853   -16.676 0.50 16.67 ? 164 HIS B ND1 1 
ATOM   3473  N  ND1 B HIS B 1 164 ? -19.602 4.169   -15.194 0.50 25.34 ? 164 HIS B ND1 1 
ATOM   3474  C  CD2 A HIS B 1 164 ? -18.223 2.573   -15.133 0.50 16.06 ? 164 HIS B CD2 1 
ATOM   3475  C  CD2 B HIS B 1 164 ? -19.257 6.214   -15.852 0.50 23.86 ? 164 HIS B CD2 1 
ATOM   3476  C  CE1 A HIS B 1 164 ? -17.585 2.671   -17.229 0.50 14.75 ? 164 HIS B CE1 1 
ATOM   3477  C  CE1 B HIS B 1 164 ? -20.500 4.427   -16.136 0.50 20.72 ? 164 HIS B CE1 1 
ATOM   3478  N  NE2 A HIS B 1 164 ? -18.147 1.892   -16.324 0.50 17.12 ? 164 HIS B NE2 1 
ATOM   3479  N  NE2 B HIS B 1 164 ? -20.340 5.675   -16.528 0.50 19.58 ? 164 HIS B NE2 1 
ATOM   3480  N  N   . VAL B 1 165 ? -14.648 6.084   -12.627 1.00 11.87 ? 165 VAL B N   1 
ATOM   3481  C  CA  . VAL B 1 165 ? -14.034 6.971   -11.641 1.00 10.81 ? 165 VAL B CA  1 
ATOM   3482  C  C   . VAL B 1 165 ? -12.512 6.874   -11.803 1.00 9.10  ? 165 VAL B C   1 
ATOM   3483  O  O   . VAL B 1 165 ? -11.749 6.959   -10.822 1.00 11.13 ? 165 VAL B O   1 
ATOM   3484  C  CB  . VAL B 1 165 ? -14.475 6.749   -10.122 1.00 11.36 ? 165 VAL B CB  1 
ATOM   3485  C  CG1 . VAL B 1 165 ? -15.890 7.175   -9.966  1.00 13.91 ? 165 VAL B CG1 1 
ATOM   3486  C  CG2 . VAL B 1 165 ? -14.334 5.327   -9.725  1.00 13.48 ? 165 VAL B CG2 1 
ATOM   3487  N  N   A LYS B 1 166 ? -11.947 6.695   -13.004 0.50 8.21  ? 166 LYS B N   1 
ATOM   3488  N  N   B LYS B 1 166 ? -12.522 6.801   -13.263 0.50 9.50  ? 166 LYS B N   1 
ATOM   3489  C  CA  A LYS B 1 166 ? -10.494 6.502   -13.193 0.50 9.21  ? 166 LYS B CA  1 
ATOM   3490  C  CA  B LYS B 1 166 ? -11.198 6.541   -13.539 0.50 8.16  ? 166 LYS B CA  1 
ATOM   3491  C  C   A LYS B 1 166 ? -9.695  7.704   -12.682 0.50 8.96  ? 166 LYS B C   1 
ATOM   3492  C  C   B LYS B 1 166 ? -10.212 7.640   -13.034 0.50 8.90  ? 166 LYS B C   1 
ATOM   3493  O  O   A LYS B 1 166 ? -8.575  7.563   -12.169 0.50 7.67  ? 166 LYS B O   1 
ATOM   3494  O  O   B LYS B 1 166 ? -9.117  7.313   -12.684 0.50 7.61  ? 166 LYS B O   1 
ATOM   3495  C  CB  A LYS B 1 166 ? -10.129 6.257   -14.663 0.50 8.57  ? 166 LYS B CB  1 
ATOM   3496  C  CB  B LYS B 1 166 ? -11.059 6.435   -15.005 0.50 7.82  ? 166 LYS B CB  1 
ATOM   3497  C  CG  A LYS B 1 166 ? -10.822 5.075   -15.321 0.50 9.13  ? 166 LYS B CG  1 
ATOM   3498  C  CG  B LYS B 1 166 ? -9.679  5.980   -15.255 0.50 8.86  ? 166 LYS B CG  1 
ATOM   3499  C  CD  A LYS B 1 166 ? -10.392 4.855   -16.758 0.50 8.58  ? 166 LYS B CD  1 
ATOM   3500  C  CD  B LYS B 1 166 ? -9.469  5.660   -16.763 0.50 11.02 ? 166 LYS B CD  1 
ATOM   3501  C  CE  A LYS B 1 166 ? -8.969  4.445   -16.961 0.50 12.52 ? 166 LYS B CE  1 
ATOM   3502  C  CE  B LYS B 1 166 ? -8.135  5.145   -16.860 0.50 13.47 ? 166 LYS B CE  1 
ATOM   3503  N  NZ  A LYS B 1 166 ? -8.641  3.079   -16.367 0.50 11.21 ? 166 LYS B NZ  1 
ATOM   3504  N  NZ  B LYS B 1 166 ? -8.349  3.759   -16.192 0.50 22.06 ? 166 LYS B NZ  1 
ATOM   3505  N  N   . TYR B 1 167 ? -10.301 8.917   -12.814 1.00 8.93  ? 167 TYR B N   1 
ATOM   3506  C  CA  . TYR B 1 167 ? -9.440  10.042  -12.558 1.00 8.54  ? 167 TYR B CA  1 
ATOM   3507  C  C   . TYR B 1 167 ? -9.919  10.836  -11.325 1.00 7.60  ? 167 TYR B C   1 
ATOM   3508  O  O   . TYR B 1 167 ? -11.157 10.869  -11.028 1.00 8.12  ? 167 TYR B O   1 
ATOM   3509  C  CB  . TYR B 1 167 ? -9.426  11.016  -13.827 1.00 10.62 ? 167 TYR B CB  1 
ATOM   3510  C  CG  . TYR B 1 167 ? -9.010  10.236  -15.105 1.00 10.36 ? 167 TYR B CG  1 
ATOM   3511  C  CD1 . TYR B 1 167 ? -7.746  9.933   -15.287 1.00 11.55 ? 167 TYR B CD1 1 
ATOM   3512  C  CD2 . TYR B 1 167 ? -9.978  9.883   -16.085 1.00 11.40 ? 167 TYR B CD2 1 
ATOM   3513  C  CE1 . TYR B 1 167 ? -7.351  9.169   -16.400 1.00 12.23 ? 167 TYR B CE1 1 
ATOM   3514  C  CE2 . TYR B 1 167 ? -9.609  9.137   -17.220 1.00 12.82 ? 167 TYR B CE2 1 
ATOM   3515  C  CZ  . TYR B 1 167 ? -8.290  8.828   -17.332 1.00 12.93 ? 167 TYR B CZ  1 
ATOM   3516  O  OH  . TYR B 1 167 ? -7.937  8.068   -18.478 1.00 14.93 ? 167 TYR B OH  1 
ATOM   3517  N  N   . LYS B 1 168 ? -8.997  11.598  -10.711 1.00 9.16  ? 168 LYS B N   1 
ATOM   3518  C  CA  . LYS B 1 168 ? -9.300  12.435  -9.584  1.00 10.72 ? 168 LYS B CA  1 
ATOM   3519  C  C   . LYS B 1 168 ? -10.457 13.358  -9.909  1.00 11.32 ? 168 LYS B C   1 
ATOM   3520  O  O   . LYS B 1 168 ? -10.502 14.041  -10.935 1.00 10.77 ? 168 LYS B O   1 
ATOM   3521  C  CB  . LYS B 1 168 ? -8.123  13.360  -9.250  1.00 10.00 ? 168 LYS B CB  1 
ATOM   3522  C  CG  . LYS B 1 168 ? -8.391  14.131  -8.035  1.00 10.45 ? 168 LYS B CG  1 
ATOM   3523  C  CD  . LYS B 1 168 ? -7.143  14.783  -7.521  1.00 14.12 ? 168 LYS B CD  1 
ATOM   3524  C  CE  . LYS B 1 168 ? -7.502  15.627  -6.247  1.00 19.17 ? 168 LYS B CE  1 
ATOM   3525  N  NZ  . LYS B 1 168 ? -6.470  16.667  -6.016  1.00 29.00 ? 168 LYS B NZ  1 
ATOM   3526  N  N   . GLY B 1 169 ? -11.401 13.360  -8.965  1.00 9.48  ? 169 GLY B N   1 
ATOM   3527  C  CA  . GLY B 1 169 ? -12.583 14.201  -9.060  1.00 13.72 ? 169 GLY B CA  1 
ATOM   3528  C  C   . GLY B 1 169 ? -13.767 13.635  -9.730  1.00 14.18 ? 169 GLY B C   1 
ATOM   3529  O  O   . GLY B 1 169 ? -14.884 14.234  -9.690  1.00 16.59 ? 169 GLY B O   1 
ATOM   3530  N  N   . GLN B 1 170 ? -13.594 12.488  -10.415 1.00 11.36 ? 170 GLN B N   1 
ATOM   3531  C  CA  . GLN B 1 170 ? -14.715 11.874  -11.068 1.00 12.14 ? 170 GLN B CA  1 
ATOM   3532  C  C   . GLN B 1 170 ? -15.614 11.208  -10.029 1.00 12.56 ? 170 GLN B C   1 
ATOM   3533  O  O   . GLN B 1 170 ? -15.131 10.684  -9.039  1.00 11.96 ? 170 GLN B O   1 
ATOM   3534  C  CB  . GLN B 1 170 ? -14.186 10.882  -12.110 1.00 11.35 ? 170 GLN B CB  1 
ATOM   3535  C  CG  . GLN B 1 170 ? -13.451 11.687  -13.299 1.00 12.49 ? 170 GLN B CG  1 
ATOM   3536  C  CD  . GLN B 1 170 ? -13.184 10.808  -14.473 1.00 12.13 ? 170 GLN B CD  1 
ATOM   3537  O  OE1 . GLN B 1 170 ? -12.908 9.607   -14.371 1.00 13.39 ? 170 GLN B OE1 1 
ATOM   3538  N  NE2 . GLN B 1 170 ? -13.266 11.398  -15.697 1.00 18.26 ? 170 GLN B NE2 1 
ATOM   3539  N  N   . GLU B 1 171 ? -16.873 11.145  -10.406 1.00 13.52 ? 171 GLU B N   1 
ATOM   3540  C  CA  . GLU B 1 171 ? -17.953 10.610  -9.524  1.00 14.44 ? 171 GLU B CA  1 
ATOM   3541  C  C   . GLU B 1 171 ? -18.853 9.670   -10.358 1.00 14.89 ? 171 GLU B C   1 
ATOM   3542  O  O   . GLU B 1 171 ? -19.038 9.862   -11.590 1.00 15.78 ? 171 GLU B O   1 
ATOM   3543  C  CB  . GLU B 1 171 ? -18.804 11.697  -8.976  1.00 16.17 ? 171 GLU B CB  1 
ATOM   3544  C  CG  . GLU B 1 171 ? -18.190 12.670  -8.038  1.00 18.25 ? 171 GLU B CG  1 
ATOM   3545  C  CD  . GLU B 1 171 ? -19.203 13.754  -7.793  1.00 24.48 ? 171 GLU B CD  1 
ATOM   3546  O  OE1 . GLU B 1 171 ? -20.186 13.823  -8.612  1.00 29.22 ? 171 GLU B OE1 1 
ATOM   3547  O  OE2 . GLU B 1 171 ? -19.046 14.401  -6.760  1.00 29.95 ? 171 GLU B OE2 1 
ATOM   3548  N  N   . ALA B 1 172 ? -19.387 8.622   -9.726  1.00 13.59 ? 172 ALA B N   1 
ATOM   3549  C  CA  . ALA B 1 172 ? -20.247 7.652   -10.348 1.00 13.47 ? 172 ALA B CA  1 
ATOM   3550  C  C   . ALA B 1 172 ? -21.252 7.235   -9.236  1.00 13.03 ? 172 ALA B C   1 
ATOM   3551  O  O   . ALA B 1 172 ? -21.051 7.533   -8.044  1.00 13.96 ? 172 ALA B O   1 
ATOM   3552  C  CB  . ALA B 1 172 ? -19.450 6.404   -10.898 1.00 15.53 ? 172 ALA B CB  1 
ATOM   3553  N  N   . PHE B 1 173 ? -22.391 6.702   -9.609  1.00 13.16 ? 173 PHE B N   1 
ATOM   3554  C  CA  . PHE B 1 173 ? -23.409 6.162   -8.679  1.00 11.46 ? 173 PHE B CA  1 
ATOM   3555  C  C   . PHE B 1 173 ? -23.475 4.653   -8.714  1.00 13.35 ? 173 PHE B C   1 
ATOM   3556  O  O   . PHE B 1 173 ? -23.422 4.025   -9.759  1.00 16.74 ? 173 PHE B O   1 
ATOM   3557  C  CB  . PHE B 1 173 ? -24.782 6.767   -9.094  1.00 16.12 ? 173 PHE B CB  1 
ATOM   3558  C  CG  . PHE B 1 173 ? -24.990 8.161   -8.591  1.00 16.26 ? 173 PHE B CG  1 
ATOM   3559  C  CD1 . PHE B 1 173 ? -25.058 8.363   -7.225  1.00 20.51 ? 173 PHE B CD1 1 
ATOM   3560  C  CD2 . PHE B 1 173 ? -25.233 9.215   -9.416  1.00 22.76 ? 173 PHE B CD2 1 
ATOM   3561  C  CE1 . PHE B 1 173 ? -25.242 9.598   -6.607  1.00 20.57 ? 173 PHE B CE1 1 
ATOM   3562  C  CE2 . PHE B 1 173 ? -25.427 10.476  -8.849  1.00 21.64 ? 173 PHE B CE2 1 
ATOM   3563  C  CZ  . PHE B 1 173 ? -25.454 10.693  -7.436  1.00 22.80 ? 173 PHE B CZ  1 
ATOM   3564  N  N   . VAL B 1 174 ? -23.477 4.111   -7.508  1.00 11.27 ? 174 VAL B N   1 
ATOM   3565  C  CA  . VAL B 1 174 ? -23.472 2.661   -7.290  1.00 12.29 ? 174 VAL B CA  1 
ATOM   3566  C  C   . VAL B 1 174 ? -24.824 2.350   -6.657  1.00 11.07 ? 174 VAL B C   1 
ATOM   3567  O  O   . VAL B 1 174 ? -25.190 2.886   -5.664  1.00 11.83 ? 174 VAL B O   1 
ATOM   3568  C  CB  . VAL B 1 174 ? -22.363 2.252   -6.298  1.00 10.97 ? 174 VAL B CB  1 
ATOM   3569  C  CG1 . VAL B 1 174 ? -22.436 0.761   -6.024  1.00 12.42 ? 174 VAL B CG1 1 
ATOM   3570  C  CG2 . VAL B 1 174 ? -20.900 2.481   -6.946  1.00 13.44 ? 174 VAL B CG2 1 
ATOM   3571  N  N   . PRO B 1 175 ? -25.579 1.391   -7.302  1.00 9.26  ? 175 PRO B N   1 
ATOM   3572  C  CA  . PRO B 1 175 ? -26.844 0.994   -6.631  1.00 9.14  ? 175 PRO B CA  1 
ATOM   3573  C  C   . PRO B 1 175 ? -26.550 0.407   -5.215  1.00 10.36 ? 175 PRO B C   1 
ATOM   3574  O  O   . PRO B 1 175 ? -25.514 -0.263  -5.032  1.00 10.60 ? 175 PRO B O   1 
ATOM   3575  C  CB  . PRO B 1 175 ? -27.379 -0.076  -7.499  1.00 9.71  ? 175 PRO B CB  1 
ATOM   3576  C  CG  . PRO B 1 175 ? -26.792 0.136   -8.905  1.00 11.36 ? 175 PRO B CG  1 
ATOM   3577  C  CD  . PRO B 1 175 ? -25.408 0.822   -8.656  1.00 11.49 ? 175 PRO B CD  1 
ATOM   3578  N  N   . GLY B 1 176 ? -27.461 0.593   -4.299  1.00 10.67 ? 176 GLY B N   1 
ATOM   3579  C  CA  . GLY B 1 176 ? -27.275 0.075   -2.930  1.00 9.88  ? 176 GLY B CA  1 
ATOM   3580  C  C   . GLY B 1 176 ? -27.230 -1.417  -2.991  1.00 10.77 ? 176 GLY B C   1 
ATOM   3581  O  O   . GLY B 1 176 ? -27.805 -2.102  -3.844  1.00 11.36 ? 176 GLY B O   1 
ATOM   3582  N  N   . PHE B 1 177 ? -26.416 -1.905  -2.025  1.00 9.87  ? 177 PHE B N   1 
ATOM   3583  C  CA  . PHE B 1 177 ? -26.316 -3.379  -1.841  1.00 9.29  ? 177 PHE B CA  1 
ATOM   3584  C  C   . PHE B 1 177 ? -26.028 -3.543  -0.345  1.00 9.02  ? 177 PHE B C   1 
ATOM   3585  O  O   . PHE B 1 177 ? -25.869 -2.625  0.424   1.00 9.19  ? 177 PHE B O   1 
ATOM   3586  C  CB  . PHE B 1 177 ? -25.239 -4.056  -2.735  1.00 10.94 ? 177 PHE B CB  1 
ATOM   3587  C  CG  . PHE B 1 177 ? -23.827 -3.606  -2.469  1.00 10.26 ? 177 PHE B CG  1 
ATOM   3588  C  CD1 . PHE B 1 177 ? -23.003 -4.416  -1.676  1.00 13.52 ? 177 PHE B CD1 1 
ATOM   3589  C  CD2 . PHE B 1 177 ? -23.316 -2.385  -3.014  1.00 11.05 ? 177 PHE B CD2 1 
ATOM   3590  C  CE1 . PHE B 1 177 ? -21.720 -4.042  -1.395  1.00 9.83  ? 177 PHE B CE1 1 
ATOM   3591  C  CE2 . PHE B 1 177 ? -22.000 -2.042  -2.784  1.00 14.44 ? 177 PHE B CE2 1 
ATOM   3592  C  CZ  . PHE B 1 177 ? -21.206 -2.872  -1.929  1.00 11.85 ? 177 PHE B CZ  1 
ATOM   3593  N  N   . ASN B 1 178 ? -26.009 -4.821  0.039   1.00 10.77 ? 178 ASN B N   1 
ATOM   3594  C  CA  . ASN B 1 178 ? -25.805 -5.100  1.443   1.00 10.97 ? 178 ASN B CA  1 
ATOM   3595  C  C   . ASN B 1 178 ? -24.268 -5.085  1.800   1.00 9.60  ? 178 ASN B C   1 
ATOM   3596  O  O   . ASN B 1 178 ? -23.529 -5.967  1.495   1.00 11.47 ? 178 ASN B O   1 
ATOM   3597  C  CB  . ASN B 1 178 ? -26.458 -6.465  1.793   1.00 11.50 ? 178 ASN B CB  1 
ATOM   3598  C  CG  . ASN B 1 178 ? -26.349 -6.751  3.216   1.00 12.45 ? 178 ASN B CG  1 
ATOM   3599  O  OD1 . ASN B 1 178 ? -25.925 -5.997  4.071   1.00 12.88 ? 178 ASN B OD1 1 
ATOM   3600  N  ND2 . ASN B 1 178 ? -26.618 -8.073  3.533   1.00 15.59 ? 178 ASN B ND2 1 
ATOM   3601  N  N   . ILE B 1 179 ? -23.922 -3.958  2.443   1.00 8.35  ? 179 ILE B N   1 
ATOM   3602  C  CA  . ILE B 1 179 ? -22.452 -3.689  2.801   1.00 9.27  ? 179 ILE B CA  1 
ATOM   3603  C  C   . ILE B 1 179 ? -21.985 -4.801  3.744   1.00 9.68  ? 179 ILE B C   1 
ATOM   3604  O  O   . ILE B 1 179 ? -20.765 -5.053  3.796   1.00 9.35  ? 179 ILE B O   1 
ATOM   3605  C  CB  . ILE B 1 179 ? -22.369 -2.288  3.414   1.00 7.84  ? 179 ILE B CB  1 
ATOM   3606  C  CG1 . ILE B 1 179 ? -22.893 -1.202  2.470   1.00 9.41  ? 179 ILE B CG1 1 
ATOM   3607  C  CG2 . ILE B 1 179 ? -20.880 -2.003  3.843   1.00 9.44  ? 179 ILE B CG2 1 
ATOM   3608  C  CD1 . ILE B 1 179 ? -22.225 -1.202  1.049   1.00 9.80  ? 179 ILE B CD1 1 
ATOM   3609  N  N   . GLU B 1 180 ? -22.888 -5.416  4.539   1.00 9.24  ? 180 GLU B N   1 
ATOM   3610  C  CA  . GLU B 1 180 ? -22.399 -6.487  5.412   1.00 10.59 ? 180 GLU B CA  1 
ATOM   3611  C  C   . GLU B 1 180 ? -21.848 -7.604  4.575   1.00 9.71  ? 180 GLU B C   1 
ATOM   3612  O  O   . GLU B 1 180 ? -21.041 -8.374  5.151   1.00 11.27 ? 180 GLU B O   1 
ATOM   3613  C  CB  . GLU B 1 180 ? -23.545 -6.995  6.303   1.00 11.87 ? 180 GLU B CB  1 
ATOM   3614  C  CG  . GLU B 1 180 ? -22.987 -7.663  7.617   1.00 14.61 ? 180 GLU B CG  1 
ATOM   3615  C  CD  . GLU B 1 180 ? -24.120 -8.075  8.626   1.00 15.66 ? 180 GLU B CD  1 
ATOM   3616  O  OE1 . GLU B 1 180 ? -25.285 -7.680  8.333   1.00 15.79 ? 180 GLU B OE1 1 
ATOM   3617  O  OE2 . GLU B 1 180 ? -23.769 -8.702  9.626   1.00 22.40 ? 180 GLU B OE2 1 
ATOM   3618  N  N   . GLU B 1 181 ? -22.196 -7.776  3.282   1.00 9.21  ? 181 GLU B N   1 
ATOM   3619  C  CA  . GLU B 1 181 ? -21.586 -8.806  2.504   1.00 9.71  ? 181 GLU B CA  1 
ATOM   3620  C  C   . GLU B 1 181 ? -20.086 -8.603  2.250   1.00 10.34 ? 181 GLU B C   1 
ATOM   3621  O  O   . GLU B 1 181 ? -19.409 -9.482  1.707   1.00 11.34 ? 181 GLU B O   1 
ATOM   3622  C  CB  . GLU B 1 181 ? -22.282 -8.940  1.108   1.00 12.52 ? 181 GLU B CB  1 
ATOM   3623  C  CG  . GLU B 1 181 ? -23.731 -9.215  1.091   1.00 14.99 ? 181 GLU B CG  1 
ATOM   3624  C  CD  . GLU B 1 181 ? -24.371 -8.980  -0.282  1.00 17.86 ? 181 GLU B CD  1 
ATOM   3625  O  OE1 . GLU B 1 181 ? -23.744 -8.590  -1.341  1.00 19.62 ? 181 GLU B OE1 1 
ATOM   3626  O  OE2 . GLU B 1 181 ? -25.641 -9.130  -0.342  1.00 21.28 ? 181 GLU B OE2 1 
ATOM   3627  N  N   . LEU B 1 182 ? -19.581 -7.406  2.534   1.00 7.99  ? 182 LEU B N   1 
ATOM   3628  C  CA  . LEU B 1 182 ? -18.137 -7.178  2.359   1.00 7.11  ? 182 LEU B CA  1 
ATOM   3629  C  C   . LEU B 1 182 ? -17.382 -7.605  3.597   1.00 6.56  ? 182 LEU B C   1 
ATOM   3630  O  O   . LEU B 1 182 ? -16.155 -7.538  3.598   1.00 7.23  ? 182 LEU B O   1 
ATOM   3631  C  CB  . LEU B 1 182 ? -17.920 -5.610  2.178   1.00 8.41  ? 182 LEU B CB  1 
ATOM   3632  C  CG  . LEU B 1 182 ? -18.585 -4.968  0.986   1.00 6.49  ? 182 LEU B CG  1 
ATOM   3633  C  CD1 . LEU B 1 182 ? -18.339 -3.417  0.947   1.00 6.47  ? 182 LEU B CD1 1 
ATOM   3634  C  CD2 . LEU B 1 182 ? -18.176 -5.647  -0.296  1.00 9.24  ? 182 LEU B CD2 1 
ATOM   3635  N  N   . LEU B 1 183 ? -18.035 -7.871  4.727   1.00 9.29  ? 183 LEU B N   1 
ATOM   3636  C  CA  . LEU B 1 183 ? -17.354 -8.351  5.983   1.00 7.97  ? 183 LEU B CA  1 
ATOM   3637  C  C   . LEU B 1 183 ? -17.140 -9.884  5.915   1.00 8.99  ? 183 LEU B C   1 
ATOM   3638  O  O   . LEU B 1 183 ? -17.825 -10.622 5.216   1.00 10.61 ? 183 LEU B O   1 
ATOM   3639  C  CB  . LEU B 1 183 ? -18.241 -8.039  7.165   1.00 9.99  ? 183 LEU B CB  1 
ATOM   3640  C  CG  . LEU B 1 183 ? -18.587 -6.542  7.286   1.00 10.21 ? 183 LEU B CG  1 
ATOM   3641  C  CD1 . LEU B 1 183 ? -19.414 -6.236  8.628   1.00 17.01 ? 183 LEU B CD1 1 
ATOM   3642  C  CD2 . LEU B 1 183 ? -17.468 -5.581  7.255   1.00 13.74 ? 183 LEU B CD2 1 
ATOM   3643  N  N   . PRO B 1 184 ? -16.089 -10.280 6.695   1.00 8.77  ? 184 PRO B N   1 
ATOM   3644  C  CA  . PRO B 1 184 ? -15.748 -11.712 6.661   1.00 10.56 ? 184 PRO B CA  1 
ATOM   3645  C  C   . PRO B 1 184 ? -16.603 -12.489 7.598   1.00 14.32 ? 184 PRO B C   1 
ATOM   3646  O  O   . PRO B 1 184 ? -17.583 -12.019 8.170   1.00 13.86 ? 184 PRO B O   1 
ATOM   3647  C  CB  . PRO B 1 184 ? -14.307 -11.667 7.300   1.00 13.31 ? 184 PRO B CB  1 
ATOM   3648  C  CG  . PRO B 1 184 ? -14.407 -10.499 8.277   1.00 12.47 ? 184 PRO B CG  1 
ATOM   3649  C  CD  . PRO B 1 184 ? -15.175 -9.501  7.507   1.00 10.17 ? 184 PRO B CD  1 
ATOM   3650  N  N   . GLU B 1 185 ? -16.214 -13.782 7.607   1.00 15.06 ? 185 GLU B N   1 
ATOM   3651  C  CA  . GLU B 1 185 ? -16.803 -14.758 8.568   1.00 15.15 ? 185 GLU B CA  1 
ATOM   3652  C  C   . GLU B 1 185 ? -16.421 -14.431 9.976   1.00 14.75 ? 185 GLU B C   1 
ATOM   3653  O  O   . GLU B 1 185 ? -15.287 -13.911 10.221  1.00 15.62 ? 185 GLU B O   1 
ATOM   3654  C  CB  . GLU B 1 185 ? -16.236 -16.133 8.237   1.00 18.22 ? 185 GLU B CB  1 
ATOM   3655  C  CG  . GLU B 1 185 ? -16.797 -16.670 6.956   1.00 24.71 ? 185 GLU B CG  1 
ATOM   3656  C  CD  . GLU B 1 185 ? -16.757 -18.204 6.957   1.00 38.29 ? 185 GLU B CD  1 
ATOM   3657  O  OE1 . GLU B 1 185 ? -17.845 -18.836 6.777   1.00 45.94 ? 185 GLU B OE1 1 
ATOM   3658  O  OE2 . GLU B 1 185 ? -15.641 -18.742 7.201   1.00 40.58 ? 185 GLU B OE2 1 
ATOM   3659  N  N   . ARG B 1 186 ? -17.380 -14.648 10.916  1.00 13.46 ? 186 ARG B N   1 
ATOM   3660  C  CA  . ARG B 1 186 ? -17.120 -14.594 12.332  1.00 17.08 ? 186 ARG B CA  1 
ATOM   3661  C  C   . ARG B 1 186 ? -16.647 -13.188 12.709  1.00 13.81 ? 186 ARG B C   1 
ATOM   3662  O  O   . ARG B 1 186 ? -15.576 -12.942 13.293  1.00 15.08 ? 186 ARG B O   1 
ATOM   3663  C  CB  . ARG B 1 186 ? -16.157 -15.713 12.797  1.00 16.61 ? 186 ARG B CB  1 
ATOM   3664  C  CG  . ARG B 1 186 ? -16.605 -17.208 12.497  1.00 21.37 ? 186 ARG B CG  1 
ATOM   3665  C  CD  . ARG B 1 186 ? -15.580 -18.228 13.136  1.00 20.60 ? 186 ARG B CD  1 
ATOM   3666  N  NE  . ARG B 1 186 ? -14.333 -18.344 12.362  1.00 23.58 ? 186 ARG B NE  1 
ATOM   3667  C  CZ  . ARG B 1 186 ? -14.241 -18.863 11.130  1.00 32.57 ? 186 ARG B CZ  1 
ATOM   3668  N  NH1 . ARG B 1 186 ? -15.329 -19.246 10.494  1.00 36.79 ? 186 ARG B NH1 1 
ATOM   3669  N  NH2 . ARG B 1 186 ? -13.046 -18.954 10.501  1.00 37.13 ? 186 ARG B NH2 1 
ATOM   3670  N  N   . THR B 1 187 ? -17.481 -12.248 12.377  1.00 10.35 ? 187 THR B N   1 
ATOM   3671  C  CA  . THR B 1 187 ? -17.156 -10.902 12.764  1.00 9.07  ? 187 THR B CA  1 
ATOM   3672  C  C   . THR B 1 187 ? -17.000 -10.714 14.259  1.00 9.97  ? 187 THR B C   1 
ATOM   3673  O  O   . THR B 1 187 ? -16.478 -9.721  14.685  1.00 10.74 ? 187 THR B O   1 
ATOM   3674  C  CB  . THR B 1 187 ? -18.135 -9.899  12.184  1.00 9.27  ? 187 THR B CB  1 
ATOM   3675  O  OG1 . THR B 1 187 ? -19.460 -10.312 12.581  1.00 11.65 ? 187 THR B OG1 1 
ATOM   3676  C  CG2 . THR B 1 187 ? -18.011 -9.846  10.678  1.00 11.72 ? 187 THR B CG2 1 
ATOM   3677  N  N   . ALA B 1 188 ? -17.491 -11.615 15.131  1.00 9.99  ? 188 ALA B N   1 
ATOM   3678  C  CA  . ALA B 1 188 ? -17.230 -11.494 16.514  1.00 9.02  ? 188 ALA B CA  1 
ATOM   3679  C  C   . ALA B 1 188 ? -15.790 -11.545 16.896  1.00 8.02  ? 188 ALA B C   1 
ATOM   3680  O  O   . ALA B 1 188 ? -15.479 -11.127 17.962  1.00 8.88  ? 188 ALA B O   1 
ATOM   3681  C  CB  . ALA B 1 188 ? -17.963 -12.730 17.238  1.00 10.13 ? 188 ALA B CB  1 
ATOM   3682  N  N   A GLU B 1 189 ? -14.927 -12.108 16.013  0.50 9.70  ? 189 GLU B N   1 
ATOM   3683  N  N   B GLU B 1 189 ? -14.950 -12.056 15.967  0.50 8.94  ? 189 GLU B N   1 
ATOM   3684  C  CA  A GLU B 1 189 ? -13.473 -12.159 16.366  0.50 9.01  ? 189 GLU B CA  1 
ATOM   3685  C  CA  B GLU B 1 189 ? -13.507 -12.234 16.256  0.50 7.86  ? 189 GLU B CA  1 
ATOM   3686  C  C   A GLU B 1 189 ? -12.820 -10.966 15.657  0.50 10.24 ? 189 GLU B C   1 
ATOM   3687  C  C   B GLU B 1 189 ? -12.728 -11.036 15.627  0.50 9.24  ? 189 GLU B C   1 
ATOM   3688  O  O   A GLU B 1 189 ? -12.897 -10.787 14.389  0.50 9.40  ? 189 GLU B O   1 
ATOM   3689  O  O   B GLU B 1 189 ? -12.639 -10.933 14.337  0.50 7.05  ? 189 GLU B O   1 
ATOM   3690  C  CB  A GLU B 1 189 ? -12.854 -13.462 15.927  0.50 9.31  ? 189 GLU B CB  1 
ATOM   3691  C  CB  B GLU B 1 189 ? -13.106 -13.481 15.531  0.50 8.48  ? 189 GLU B CB  1 
ATOM   3692  C  CG  A GLU B 1 189 ? -13.584 -14.675 16.581  0.50 11.11 ? 189 GLU B CG  1 
ATOM   3693  C  CG  B GLU B 1 189 ? -13.776 -14.819 15.977  0.50 11.74 ? 189 GLU B CG  1 
ATOM   3694  C  CD  A GLU B 1 189 ? -13.254 -16.045 15.921  0.50 13.03 ? 189 GLU B CD  1 
ATOM   3695  C  CD  B GLU B 1 189 ? -12.877 -15.874 15.531  0.50 18.60 ? 189 GLU B CD  1 
ATOM   3696  O  OE1 A GLU B 1 189 ? -12.073 -16.289 15.488  0.50 13.09 ? 189 GLU B OE1 1 
ATOM   3697  O  OE1 B GLU B 1 189 ? -12.844 -16.137 14.289  0.50 18.38 ? 189 GLU B OE1 1 
ATOM   3698  O  OE2 A GLU B 1 189 ? -14.141 -16.958 15.840  0.50 17.22 ? 189 GLU B OE2 1 
ATOM   3699  O  OE2 B GLU B 1 189 ? -12.119 -16.325 16.437  0.50 18.44 ? 189 GLU B OE2 1 
ATOM   3700  N  N   . TYR B 1 190 ? -12.239 -10.145 16.478  1.00 7.57  ? 190 TYR B N   1 
ATOM   3701  C  CA  . TYR B 1 190 ? -11.563 -8.914  15.949  1.00 7.23  ? 190 TYR B CA  1 
ATOM   3702  C  C   . TYR B 1 190 ? -10.481 -8.489  16.898  1.00 8.04  ? 190 TYR B C   1 
ATOM   3703  O  O   . TYR B 1 190 ? -10.416 -8.860  18.070  1.00 7.14  ? 190 TYR B O   1 
ATOM   3704  C  CB  . TYR B 1 190 ? -12.569 -7.787  15.656  1.00 7.95  ? 190 TYR B CB  1 
ATOM   3705  C  CG  . TYR B 1 190 ? -13.396 -7.451  16.934  1.00 7.35  ? 190 TYR B CG  1 
ATOM   3706  C  CD1 . TYR B 1 190 ? -12.934 -6.550  17.899  1.00 8.24  ? 190 TYR B CD1 1 
ATOM   3707  C  CD2 . TYR B 1 190 ? -14.700 -7.959  17.109  1.00 7.50  ? 190 TYR B CD2 1 
ATOM   3708  C  CE1 . TYR B 1 190 ? -13.749 -6.129  18.985  1.00 6.59  ? 190 TYR B CE1 1 
ATOM   3709  C  CE2 . TYR B 1 190 ? -15.474 -7.619  18.272  1.00 7.79  ? 190 TYR B CE2 1 
ATOM   3710  C  CZ  . TYR B 1 190 ? -14.976 -6.706  19.156  1.00 8.55  ? 190 TYR B CZ  1 
ATOM   3711  O  OH  . TYR B 1 190 ? -15.742 -6.322  20.237  1.00 10.47 ? 190 TYR B OH  1 
ATOM   3712  N  N   . TYR B 1 191 ? -9.629  -7.587  16.348  1.00 7.34  ? 191 TYR B N   1 
ATOM   3713  C  CA  . TYR B 1 191 ? -8.594  -6.881  17.081  1.00 6.58  ? 191 TYR B CA  1 
ATOM   3714  C  C   . TYR B 1 191 ? -9.075  -5.455  17.277  1.00 7.40  ? 191 TYR B C   1 
ATOM   3715  O  O   . TYR B 1 191 ? -9.742  -4.845  16.378  1.00 8.03  ? 191 TYR B O   1 
ATOM   3716  C  CB  . TYR B 1 191 ? -7.273  -6.763  16.232  1.00 7.94  ? 191 TYR B CB  1 
ATOM   3717  C  CG  . TYR B 1 191 ? -6.692  -8.024  15.625  1.00 7.48  ? 191 TYR B CG  1 
ATOM   3718  C  CD1 . TYR B 1 191 ? -5.683  -8.724  16.359  1.00 9.08  ? 191 TYR B CD1 1 
ATOM   3719  C  CD2 . TYR B 1 191 ? -7.072  -8.478  14.405  1.00 6.60  ? 191 TYR B CD2 1 
ATOM   3720  C  CE1 . TYR B 1 191 ? -5.137  -9.872  15.816  1.00 8.58  ? 191 TYR B CE1 1 
ATOM   3721  C  CE2 . TYR B 1 191 ? -6.463  -9.642  13.789  1.00 8.88  ? 191 TYR B CE2 1 
ATOM   3722  C  CZ  . TYR B 1 191 ? -5.476  -10.290 14.561  1.00 8.87  ? 191 TYR B CZ  1 
ATOM   3723  O  OH  . TYR B 1 191 ? -4.883  -11.459 13.985  1.00 12.31 ? 191 TYR B OH  1 
ATOM   3724  N  N   . ARG B 1 192 ? -8.807  -4.864  18.427  1.00 7.65  ? 192 ARG B N   1 
ATOM   3725  C  CA  . ARG B 1 192 ? -9.221  -3.518  18.762  1.00 7.47  ? 192 ARG B CA  1 
ATOM   3726  C  C   . ARG B 1 192 ? -8.102  -2.734  19.315  1.00 8.80  ? 192 ARG B C   1 
ATOM   3727  O  O   . ARG B 1 192 ? -7.406  -3.215  20.254  1.00 8.70  ? 192 ARG B O   1 
ATOM   3728  C  CB  . ARG B 1 192 ? -10.351 -3.609  19.870  1.00 8.20  ? 192 ARG B CB  1 
ATOM   3729  C  CG  . ARG B 1 192 ? -10.734 -2.308  20.565  1.00 10.00 ? 192 ARG B CG  1 
ATOM   3730  C  CD  . ARG B 1 192 ? -11.404 -1.233  19.687  1.00 9.98  ? 192 ARG B CD  1 
ATOM   3731  N  NE  . ARG B 1 192 ? -12.527 -1.794  18.892  1.00 11.12 ? 192 ARG B NE  1 
ATOM   3732  C  CZ  . ARG B 1 192 ? -13.703 -2.211  19.381  1.00 10.31 ? 192 ARG B CZ  1 
ATOM   3733  N  NH1 . ARG B 1 192 ? -13.948 -2.039  20.724  1.00 12.99 ? 192 ARG B NH1 1 
ATOM   3734  N  NH2 . ARG B 1 192 ? -14.628 -2.760  18.631  1.00 9.93  ? 192 ARG B NH2 1 
ATOM   3735  N  N   . TYR B 1 193 ? -7.936  -1.515  18.857  1.00 8.05  ? 193 TYR B N   1 
ATOM   3736  C  CA  . TYR B 1 193 ? -6.925  -0.646  19.392  1.00 9.55  ? 193 TYR B CA  1 
ATOM   3737  C  C   . TYR B 1 193 ? -7.164  0.803   19.119  1.00 7.76  ? 193 TYR B C   1 
ATOM   3738  O  O   . TYR B 1 193 ? -7.979  1.074   18.180  1.00 8.89  ? 193 TYR B O   1 
ATOM   3739  C  CB  . TYR B 1 193 ? -5.470  -1.048  18.943  1.00 8.86  ? 193 TYR B CB  1 
ATOM   3740  C  CG  . TYR B 1 193 ? -5.088  -0.673  17.507  1.00 8.00  ? 193 TYR B CG  1 
ATOM   3741  C  CD1 . TYR B 1 193 ? -4.323  0.491   17.315  1.00 8.44  ? 193 TYR B CD1 1 
ATOM   3742  C  CD2 . TYR B 1 193 ? -5.493  -1.420  16.388  1.00 8.26  ? 193 TYR B CD2 1 
ATOM   3743  C  CE1 . TYR B 1 193 ? -3.984  0.897   16.042  1.00 7.33  ? 193 TYR B CE1 1 
ATOM   3744  C  CE2 . TYR B 1 193 ? -5.201  -1.041  15.107  1.00 6.80  ? 193 TYR B CE2 1 
ATOM   3745  C  CZ  . TYR B 1 193 ? -4.440  0.144   14.950  1.00 7.87  ? 193 TYR B CZ  1 
ATOM   3746  O  OH  . TYR B 1 193 ? -4.062  0.576   13.715  1.00 8.71  ? 193 TYR B OH  1 
ATOM   3747  N  N   . ARG B 1 194 ? -6.462  1.678   19.858  1.00 10.93 ? 194 ARG B N   1 
ATOM   3748  C  CA  . ARG B 1 194 ? -6.652  3.098   19.646  1.00 9.95  ? 194 ARG B CA  1 
ATOM   3749  C  C   . ARG B 1 194 ? -5.539  3.568   18.754  1.00 9.62  ? 194 ARG B C   1 
ATOM   3750  O  O   . ARG B 1 194 ? -4.351  3.338   18.953  1.00 12.19 ? 194 ARG B O   1 
ATOM   3751  C  CB  . ARG B 1 194 ? -6.507  3.881   20.964  1.00 15.89 ? 194 ARG B CB  1 
ATOM   3752  C  CG  . ARG B 1 194 ? -7.748  3.744   21.899  1.00 20.74 ? 194 ARG B CG  1 
ATOM   3753  C  CD  . ARG B 1 194 ? -8.778  4.983   21.762  1.00 32.53 ? 194 ARG B CD  1 
ATOM   3754  N  NE  . ARG B 1 194 ? -9.730  5.233   22.911  1.00 34.23 ? 194 ARG B NE  1 
ATOM   3755  C  CZ  . ARG B 1 194 ? -10.875 5.946   22.839  1.00 34.58 ? 194 ARG B CZ  1 
ATOM   3756  N  NH1 . ARG B 1 194 ? -11.229 6.580   21.724  1.00 39.27 ? 194 ARG B NH1 1 
ATOM   3757  N  NH2 . ARG B 1 194 ? -11.666 6.089   23.907  1.00 35.50 ? 194 ARG B NH2 1 
ATOM   3758  N  N   . GLY B 1 195 ? -5.891  4.196   17.608  1.00 9.55  ? 195 GLY B N   1 
ATOM   3759  C  CA  . GLY B 1 195 ? -4.881  4.667   16.646  1.00 8.66  ? 195 GLY B CA  1 
ATOM   3760  C  C   . GLY B 1 195 ? -5.358  5.930   15.916  1.00 9.61  ? 195 GLY B C   1 
ATOM   3761  O  O   . GLY B 1 195 ? -6.077  6.785   16.499  1.00 9.95  ? 195 GLY B O   1 
ATOM   3762  N  N   . SER B 1 196 ? -5.002  5.982   14.641  1.00 8.76  ? 196 SER B N   1 
ATOM   3763  C  CA  . SER B 1 196 ? -5.107  7.224   13.926  1.00 8.37  ? 196 SER B CA  1 
ATOM   3764  C  C   . SER B 1 196 ? -5.672  6.975   12.509  1.00 7.15  ? 196 SER B C   1 
ATOM   3765  O  O   . SER B 1 196 ? -5.778  5.849   11.965  1.00 8.57  ? 196 SER B O   1 
ATOM   3766  C  CB  . SER B 1 196 ? -3.755  7.916   13.754  1.00 9.37  ? 196 SER B CB  1 
ATOM   3767  O  OG  . SER B 1 196 ? -2.942  7.213   12.753  1.00 7.29  ? 196 SER B OG  1 
ATOM   3768  N  N   . LEU B 1 197 ? -5.965  8.088   11.852  1.00 6.92  ? 197 LEU B N   1 
ATOM   3769  C  CA  . LEU B 1 197 ? -6.119  7.975   10.340  1.00 5.88  ? 197 LEU B CA  1 
ATOM   3770  C  C   . LEU B 1 197 ? -4.777  7.546   9.793   1.00 5.14  ? 197 LEU B C   1 
ATOM   3771  O  O   . LEU B 1 197 ? -3.732  7.908   10.272  1.00 6.86  ? 197 LEU B O   1 
ATOM   3772  C  CB  . LEU B 1 197 ? -6.328  9.421   9.731   1.00 7.23  ? 197 LEU B CB  1 
ATOM   3773  C  CG  . LEU B 1 197 ? -7.728  9.877   9.623   1.00 9.50  ? 197 LEU B CG  1 
ATOM   3774  C  CD1 . LEU B 1 197 ? -8.406  10.099  10.903  1.00 16.58 ? 197 LEU B CD1 1 
ATOM   3775  C  CD2 . LEU B 1 197 ? -7.716  11.274  8.840   1.00 9.69  ? 197 LEU B CD2 1 
ATOM   3776  N  N   . THR B 1 198 ? -4.895  6.657   8.752   1.00 7.24  ? 198 THR B N   1 
ATOM   3777  C  CA  . THR B 1 198 ? -3.637  6.191   8.095   1.00 7.18  ? 198 THR B CA  1 
ATOM   3778  C  C   . THR B 1 198 ? -3.178  7.043   7.008   1.00 7.07  ? 198 THR B C   1 
ATOM   3779  O  O   . THR B 1 198 ? -2.178  6.819   6.335   1.00 6.70  ? 198 THR B O   1 
ATOM   3780  C  CB  . THR B 1 198 ? -3.756  4.766   7.620   1.00 7.16  ? 198 THR B CB  1 
ATOM   3781  O  OG1 . THR B 1 198 ? -4.720  4.786   6.539   1.00 6.98  ? 198 THR B OG1 1 
ATOM   3782  C  CG2 . THR B 1 198 ? -4.172  3.737   8.684   1.00 8.33  ? 198 THR B CG2 1 
ATOM   3783  N  N   . THR B 1 199 ? -3.982  8.156   6.739   1.00 7.95  ? 199 THR B N   1 
ATOM   3784  C  CA  . THR B 1 199 ? -3.647  9.179   5.675   1.00 7.02  ? 199 THR B CA  1 
ATOM   3785  C  C   . THR B 1 199 ? -3.541  10.507  6.432   1.00 8.39  ? 199 THR B C   1 
ATOM   3786  O  O   . THR B 1 199 ? -4.176  10.719  7.448   1.00 8.90  ? 199 THR B O   1 
ATOM   3787  C  CB  . THR B 1 199 ? -4.743  9.246   4.632   1.00 5.92  ? 199 THR B CB  1 
ATOM   3788  O  OG1 . THR B 1 199 ? -5.971  9.591   5.281   1.00 12.97 ? 199 THR B OG1 1 
ATOM   3789  C  CG2 . THR B 1 199 ? -4.944  7.852   4.004   1.00 8.97  ? 199 THR B CG2 1 
ATOM   3790  N  N   . PRO B 1 200 ? -2.829  11.457  5.820   1.00 7.68  ? 200 PRO B N   1 
ATOM   3791  C  CA  . PRO B 1 200 ? -2.931  12.849  6.287   1.00 8.06  ? 200 PRO B CA  1 
ATOM   3792  C  C   . PRO B 1 200 ? -4.395  13.268  6.450   1.00 10.42 ? 200 PRO B C   1 
ATOM   3793  O  O   . PRO B 1 200 ? -5.158  12.931  5.591   1.00 11.02 ? 200 PRO B O   1 
ATOM   3794  C  CB  . PRO B 1 200 ? -2.181  13.618  5.186   1.00 8.55  ? 200 PRO B CB  1 
ATOM   3795  C  CG  . PRO B 1 200 ? -1.096  12.708  4.710   1.00 8.70  ? 200 PRO B CG  1 
ATOM   3796  C  CD  . PRO B 1 200 ? -1.915  11.361  4.693   1.00 8.54  ? 200 PRO B CD  1 
ATOM   3797  N  N   . PRO B 1 201 ? -4.715  14.011  7.517   1.00 10.54 ? 201 PRO B N   1 
ATOM   3798  C  CA  . PRO B 1 201 ? -3.782  14.576  8.519   1.00 9.95  ? 201 PRO B CA  1 
ATOM   3799  C  C   . PRO B 1 201 ? -3.409  13.708  9.696   1.00 8.97  ? 201 PRO B C   1 
ATOM   3800  O  O   . PRO B 1 201 ? -2.788  14.140  10.636  1.00 8.63  ? 201 PRO B O   1 
ATOM   3801  C  CB  . PRO B 1 201 ? -4.539  15.839  9.045   1.00 10.45 ? 201 PRO B CB  1 
ATOM   3802  C  CG  . PRO B 1 201 ? -5.803  15.927  8.181   1.00 14.50 ? 201 PRO B CG  1 
ATOM   3803  C  CD  . PRO B 1 201 ? -6.098  14.528  7.615   1.00 10.94 ? 201 PRO B CD  1 
ATOM   3804  N  N   . CYS B 1 202 ? -3.708  12.397  9.584   1.00 8.49  ? 202 CYS B N   1 
ATOM   3805  C  CA  . CYS B 1 202 ? -3.210  11.308  10.545  1.00 9.78  ? 202 CYS B CA  1 
ATOM   3806  C  C   . CYS B 1 202 ? -3.687  11.593  12.023  1.00 7.13  ? 202 CYS B C   1 
ATOM   3807  O  O   . CYS B 1 202 ? -3.004  11.231  13.016  1.00 9.53  ? 202 CYS B O   1 
ATOM   3808  C  CB  . CYS B 1 202 ? -1.665  11.325  10.567  1.00 10.54 ? 202 CYS B CB  1 
ATOM   3809  S  SG  . CYS B 1 202 ? -0.861  10.973  9.020   1.00 9.07  ? 202 CYS B SG  1 
ATOM   3810  N  N   A ASN B 1 203 ? -4.900  12.127  12.133  0.50 10.52 ? 203 ASN B N   1 
ATOM   3811  N  N   B ASN B 1 203 ? -4.860  12.251  12.168  0.50 11.04 ? 203 ASN B N   1 
ATOM   3812  C  CA  A ASN B 1 203 ? -5.517  12.402  13.406  0.50 9.72  ? 203 ASN B CA  1 
ATOM   3813  C  CA  B ASN B 1 203 ? -5.350  12.545  13.516  0.50 11.70 ? 203 ASN B CA  1 
ATOM   3814  C  C   A ASN B 1 203 ? -5.618  11.235  14.341  0.50 11.45 ? 203 ASN B C   1 
ATOM   3815  C  C   B ASN B 1 203 ? -5.397  11.286  14.327  0.50 10.70 ? 203 ASN B C   1 
ATOM   3816  O  O   A ASN B 1 203 ? -6.319  10.263  13.968  0.50 8.65  ? 203 ASN B O   1 
ATOM   3817  O  O   B ASN B 1 203 ? -5.771  10.255  13.851  0.50 8.29  ? 203 ASN B O   1 
ATOM   3818  C  CB  A ASN B 1 203 ? -6.918  12.912  13.152  0.50 11.71 ? 203 ASN B CB  1 
ATOM   3819  C  CB  B ASN B 1 203 ? -6.714  13.255  13.597  0.50 13.20 ? 203 ASN B CB  1 
ATOM   3820  C  CG  A ASN B 1 203 ? -6.869  14.122  12.246  0.50 12.31 ? 203 ASN B CG  1 
ATOM   3821  C  CG  B ASN B 1 203 ? -6.808  14.438  12.620  0.50 20.01 ? 203 ASN B CG  1 
ATOM   3822  O  OD1 A ASN B 1 203 ? -6.833  13.983  11.075  0.50 11.05 ? 203 ASN B OD1 1 
ATOM   3823  O  OD1 B ASN B 1 203 ? -5.793  14.916  12.138  0.50 24.86 ? 203 ASN B OD1 1 
ATOM   3824  N  ND2 A ASN B 1 203 ? -6.720  15.339  12.862  0.50 20.64 ? 203 ASN B ND2 1 
ATOM   3825  N  ND2 B ASN B 1 203 ? -8.043  14.896  12.311  0.50 16.39 ? 203 ASN B ND2 1 
ATOM   3826  N  N   . PRO B 1 204 ? -5.053  11.324  15.576  1.00 10.39 ? 204 PRO B N   1 
ATOM   3827  C  CA  . PRO B 1 204 ? -5.096  10.113  16.492  1.00 10.59 ? 204 PRO B CA  1 
ATOM   3828  C  C   . PRO B 1 204 ? -6.424  9.905   17.172  1.00 11.97 ? 204 PRO B C   1 
ATOM   3829  O  O   . PRO B 1 204 ? -6.503  9.904   18.460  1.00 13.83 ? 204 PRO B O   1 
ATOM   3830  C  CB  . PRO B 1 204 ? -3.941  10.418  17.524  1.00 11.45 ? 204 PRO B CB  1 
ATOM   3831  C  CG  . PRO B 1 204 ? -3.929  11.986  17.600  1.00 12.97 ? 204 PRO B CG  1 
ATOM   3832  C  CD  . PRO B 1 204 ? -4.299  12.493  16.134  1.00 12.81 ? 204 PRO B CD  1 
ATOM   3833  N  N   . THR B 1 205 ? -7.483  9.838   16.376  1.00 9.16  ? 205 THR B N   1 
ATOM   3834  C  CA  . THR B 1 205 ? -8.823  9.882   16.883  1.00 12.44 ? 205 THR B CA  1 
ATOM   3835  C  C   . THR B 1 205 ? -9.671  8.716   16.460  1.00 10.93 ? 205 THR B C   1 
ATOM   3836  O  O   . THR B 1 205 ? -10.890 8.796   16.505  1.00 12.40 ? 205 THR B O   1 
ATOM   3837  C  CB  . THR B 1 205 ? -9.459  11.137  16.314  1.00 12.66 ? 205 THR B CB  1 
ATOM   3838  O  OG1 . THR B 1 205 ? -9.317  11.131  14.880  1.00 11.72 ? 205 THR B OG1 1 
ATOM   3839  C  CG2 . THR B 1 205 ? -8.813  12.414  16.922  1.00 14.95 ? 205 THR B CG2 1 
ATOM   3840  N  N   . VAL B 1 206 ? -8.994  7.632   16.050  1.00 8.77  ? 206 VAL B N   1 
ATOM   3841  C  CA  . VAL B 1 206 ? -9.693  6.434   15.629  1.00 8.96  ? 206 VAL B CA  1 
ATOM   3842  C  C   . VAL B 1 206 ? -9.714  5.178   16.561  1.00 6.94  ? 206 VAL B C   1 
ATOM   3843  O  O   . VAL B 1 206 ? -8.647  4.772   16.942  1.00 9.25  ? 206 VAL B O   1 
ATOM   3844  C  CB  . VAL B 1 206 ? -9.123  6.008   14.191  1.00 8.06  ? 206 VAL B CB  1 
ATOM   3845  C  CG1 . VAL B 1 206 ? -9.900  4.779   13.673  1.00 9.91  ? 206 VAL B CG1 1 
ATOM   3846  C  CG2 . VAL B 1 206 ? -9.182  7.148   13.174  1.00 9.68  ? 206 VAL B CG2 1 
ATOM   3847  N  N   . LEU B 1 207 ? -10.872 4.686   16.825  1.00 7.96  ? 207 LEU B N   1 
ATOM   3848  C  CA  . LEU B 1 207 ? -11.039 3.364   17.431  1.00 8.61  ? 207 LEU B CA  1 
ATOM   3849  C  C   . LEU B 1 207 ? -11.038 2.340   16.268  1.00 8.90  ? 207 LEU B C   1 
ATOM   3850  O  O   . LEU B 1 207 ? -11.956 2.275   15.464  1.00 9.31  ? 207 LEU B O   1 
ATOM   3851  C  CB  . LEU B 1 207 ? -12.402 3.374   18.140  1.00 10.98 ? 207 LEU B CB  1 
ATOM   3852  C  CG  . LEU B 1 207 ? -12.474 2.204   19.130  1.00 17.28 ? 207 LEU B CG  1 
ATOM   3853  C  CD1 . LEU B 1 207 ? -11.328 2.289   20.218  1.00 23.29 ? 207 LEU B CD1 1 
ATOM   3854  C  CD2 . LEU B 1 207 ? -13.855 2.064   19.749  1.00 21.32 ? 207 LEU B CD2 1 
ATOM   3855  N  N   . TRP B 1 208 ? -9.955  1.588   16.152  1.00 7.32  ? 208 TRP B N   1 
ATOM   3856  C  CA  . TRP B 1 208 ? -9.799  0.521   15.177  1.00 7.72  ? 208 TRP B CA  1 
ATOM   3857  C  C   . TRP B 1 208 ? -10.419 -0.814  15.510  1.00 7.51  ? 208 TRP B C   1 
ATOM   3858  O  O   . TRP B 1 208 ? -10.191 -1.224  16.693  1.00 8.94  ? 208 TRP B O   1 
ATOM   3859  C  CB  . TRP B 1 208 ? -8.319  0.307   14.803  1.00 8.33  ? 208 TRP B CB  1 
ATOM   3860  C  CG  . TRP B 1 208 ? -7.809  1.433   13.883  1.00 7.49  ? 208 TRP B CG  1 
ATOM   3861  C  CD1 . TRP B 1 208 ? -7.201  2.604   14.240  1.00 8.37  ? 208 TRP B CD1 1 
ATOM   3862  C  CD2 . TRP B 1 208 ? -7.941  1.468   12.488  1.00 6.98  ? 208 TRP B CD2 1 
ATOM   3863  N  NE1 . TRP B 1 208 ? -6.928  3.387   13.154  1.00 8.32  ? 208 TRP B NE1 1 
ATOM   3864  C  CE2 . TRP B 1 208 ? -7.449  2.742   12.046  1.00 7.04  ? 208 TRP B CE2 1 
ATOM   3865  C  CE3 . TRP B 1 208 ? -8.501  0.621   11.549  1.00 7.06  ? 208 TRP B CE3 1 
ATOM   3866  C  CZ2 . TRP B 1 208 ? -7.436  3.125   10.715  1.00 6.89  ? 208 TRP B CZ2 1 
ATOM   3867  C  CZ3 . TRP B 1 208 ? -8.487  0.997   10.213  1.00 8.38  ? 208 TRP B CZ3 1 
ATOM   3868  C  CH2 . TRP B 1 208 ? -7.936  2.251   9.813   1.00 6.36  ? 208 TRP B CH2 1 
ATOM   3869  N  N   . THR B 1 209 ? -11.202 -1.355  14.613  1.00 6.88  ? 209 THR B N   1 
ATOM   3870  C  CA  . THR B 1 209 ? -11.580 -2.784  14.717  1.00 6.50  ? 209 THR B CA  1 
ATOM   3871  C  C   . THR B 1 209 ? -11.100 -3.455  13.490  1.00 6.90  ? 209 THR B C   1 
ATOM   3872  O  O   . THR B 1 209 ? -11.600 -3.124  12.394  1.00 7.29  ? 209 THR B O   1 
ATOM   3873  C  CB  . THR B 1 209 ? -13.143 -2.861  14.869  1.00 7.39  ? 209 THR B CB  1 
ATOM   3874  O  OG1 . THR B 1 209 ? -13.520 -2.166  16.031  1.00 8.23  ? 209 THR B OG1 1 
ATOM   3875  C  CG2 . THR B 1 209 ? -13.552 -4.326  14.987  1.00 6.85  ? 209 THR B CG2 1 
ATOM   3876  N  N   . VAL B 1 210 ? -10.184 -4.397  13.600  1.00 6.83  ? 210 VAL B N   1 
ATOM   3877  C  CA  . VAL B 1 210 ? -9.701  -5.160  12.456  1.00 5.89  ? 210 VAL B CA  1 
ATOM   3878  C  C   . VAL B 1 210 ? -10.251 -6.553  12.554  1.00 6.40  ? 210 VAL B C   1 
ATOM   3879  O  O   . VAL B 1 210 ? -9.987  -7.247  13.574  1.00 7.47  ? 210 VAL B O   1 
ATOM   3880  C  CB  . VAL B 1 210 ? -8.115  -5.183  12.397  1.00 5.72  ? 210 VAL B CB  1 
ATOM   3881  C  CG1 . VAL B 1 210 ? -7.666  -5.905  11.168  1.00 7.59  ? 210 VAL B CG1 1 
ATOM   3882  C  CG2 . VAL B 1 210 ? -7.605  -3.756  12.378  1.00 6.40  ? 210 VAL B CG2 1 
ATOM   3883  N  N   . PHE B 1 211 ? -11.112 -6.958  11.669  1.00 6.01  ? 211 PHE B N   1 
ATOM   3884  C  CA  . PHE B 1 211 ? -11.547 -8.352  11.798  1.00 6.92  ? 211 PHE B CA  1 
ATOM   3885  C  C   . PHE B 1 211 ? -10.457 -9.393  11.677  1.00 6.58  ? 211 PHE B C   1 
ATOM   3886  O  O   . PHE B 1 211 ? -9.479  -9.242  10.905  1.00 7.04  ? 211 PHE B O   1 
ATOM   3887  C  CB  . PHE B 1 211 ? -12.687 -8.602  10.781  1.00 7.51  ? 211 PHE B CB  1 
ATOM   3888  C  CG  . PHE B 1 211 ? -13.886 -7.743  11.068  1.00 6.87  ? 211 PHE B CG  1 
ATOM   3889  C  CD1 . PHE B 1 211 ? -14.239 -6.656  10.272  1.00 10.44 ? 211 PHE B CD1 1 
ATOM   3890  C  CD2 . PHE B 1 211 ? -14.641 -7.972  12.195  1.00 7.89  ? 211 PHE B CD2 1 
ATOM   3891  C  CE1 . PHE B 1 211 ? -15.394 -5.862  10.568  1.00 9.62  ? 211 PHE B CE1 1 
ATOM   3892  C  CE2 . PHE B 1 211 ? -15.726 -7.209  12.519  1.00 9.58  ? 211 PHE B CE2 1 
ATOM   3893  C  CZ  . PHE B 1 211 ? -16.131 -6.072  11.698  1.00 9.93  ? 211 PHE B CZ  1 
ATOM   3894  N  N   . ARG B 1 212 ? -10.584 -10.494 12.448  1.00 7.30  ? 212 ARG B N   1 
ATOM   3895  C  CA  . ARG B 1 212 ? -9.562  -11.529 12.433  1.00 8.08  ? 212 ARG B CA  1 
ATOM   3896  C  C   . ARG B 1 212 ? -9.448  -12.288 11.093  1.00 8.16  ? 212 ARG B C   1 
ATOM   3897  O  O   . ARG B 1 212 ? -8.357  -12.559 10.695  1.00 9.12  ? 212 ARG B O   1 
ATOM   3898  C  CB  . ARG B 1 212 ? -9.886  -12.514 13.560  1.00 7.50  ? 212 ARG B CB  1 
ATOM   3899  C  CG  . ARG B 1 212 ? -8.820  -13.614 13.640  1.00 10.16 ? 212 ARG B CG  1 
ATOM   3900  C  CD  . ARG B 1 212 ? -9.332  -14.773 14.587  1.00 12.68 ? 212 ARG B CD  1 
ATOM   3901  N  NE  . ARG B 1 212 ? -8.195  -15.625 14.889  1.00 15.19 ? 212 ARG B NE  1 
ATOM   3902  C  CZ  . ARG B 1 212 ? -8.221  -16.555 15.840  1.00 16.67 ? 212 ARG B CZ  1 
ATOM   3903  N  NH1 . ARG B 1 212 ? -9.366  -16.836 16.392  1.00 17.33 ? 212 ARG B NH1 1 
ATOM   3904  N  NH2 . ARG B 1 212 ? -7.042  -17.158 16.171  1.00 20.87 ? 212 ARG B NH2 1 
ATOM   3905  N  N   . ASN B 1 213 ? -10.595 -12.514 10.456  1.00 7.81  ? 213 ASN B N   1 
ATOM   3906  C  CA  . ASN B 1 213 ? -10.620 -13.320 9.270   1.00 9.67  ? 213 ASN B CA  1 
ATOM   3907  C  C   . ASN B 1 213 ? -10.641 -12.444 8.022   1.00 9.06  ? 213 ASN B C   1 
ATOM   3908  O  O   . ASN B 1 213 ? -11.458 -11.495 7.954   1.00 8.57  ? 213 ASN B O   1 
ATOM   3909  C  CB  . ASN B 1 213 ? -11.862 -14.253 9.294   1.00 11.60 ? 213 ASN B CB  1 
ATOM   3910  C  CG  . ASN B 1 213 ? -11.836 -15.160 10.527  1.00 16.79 ? 213 ASN B CG  1 
ATOM   3911  O  OD1 . ASN B 1 213 ? -10.821 -15.747 10.751  1.00 20.80 ? 213 ASN B OD1 1 
ATOM   3912  N  ND2 . ASN B 1 213 ? -12.878 -15.207 11.286  1.00 17.48 ? 213 ASN B ND2 1 
ATOM   3913  N  N   . PRO B 1 214 ? -9.818  -12.739 7.036   1.00 9.04  ? 214 PRO B N   1 
ATOM   3914  C  CA  . PRO B 1 214 ? -9.899  -12.058 5.744   1.00 8.77  ? 214 PRO B CA  1 
ATOM   3915  C  C   . PRO B 1 214 ? -11.091 -12.467 4.934   1.00 8.47  ? 214 PRO B C   1 
ATOM   3916  O  O   . PRO B 1 214 ? -11.644 -13.580 5.086   1.00 10.99 ? 214 PRO B O   1 
ATOM   3917  C  CB  . PRO B 1 214 ? -8.577  -12.392 5.049   1.00 8.59  ? 214 PRO B CB  1 
ATOM   3918  C  CG  . PRO B 1 214 ? -8.352  -13.868 5.490   1.00 12.87 ? 214 PRO B CG  1 
ATOM   3919  C  CD  . PRO B 1 214 ? -8.769  -13.814 7.037   1.00 12.19 ? 214 PRO B CD  1 
ATOM   3920  N  N   . VAL B 1 215 ? -11.361 -11.685 3.911   1.00 7.78  ? 215 VAL B N   1 
ATOM   3921  C  CA  . VAL B 1 215 ? -12.220 -12.062 2.802   1.00 8.21  ? 215 VAL B CA  1 
ATOM   3922  C  C   . VAL B 1 215 ? -11.377 -12.329 1.580   1.00 8.20  ? 215 VAL B C   1 
ATOM   3923  O  O   . VAL B 1 215 ? -10.184 -11.997 1.582   1.00 7.84  ? 215 VAL B O   1 
ATOM   3924  C  CB  . VAL B 1 215 ? -13.240 -11.011 2.498   1.00 6.59  ? 215 VAL B CB  1 
ATOM   3925  C  CG1 . VAL B 1 215 ? -14.181 -10.750 3.611   1.00 10.43 ? 215 VAL B CG1 1 
ATOM   3926  C  CG2 . VAL B 1 215 ? -12.616 -9.724  1.885   1.00 8.67  ? 215 VAL B CG2 1 
ATOM   3927  N  N   . GLN B 1 216 ? -11.895 -12.973 0.557   1.00 7.45  ? 216 GLN B N   1 
ATOM   3928  C  CA  . GLN B 1 216 ? -11.167 -13.165 -0.710  1.00 6.70  ? 216 GLN B CA  1 
ATOM   3929  C  C   . GLN B 1 216 ? -11.785 -12.424 -1.848  1.00 6.26  ? 216 GLN B C   1 
ATOM   3930  O  O   . GLN B 1 216 ? -13.030 -12.291 -1.937  1.00 8.08  ? 216 GLN B O   1 
ATOM   3931  C  CB  . GLN B 1 216 ? -11.247 -14.661 -1.109  1.00 9.31  ? 216 GLN B CB  1 
ATOM   3932  C  CG  . GLN B 1 216 ? -10.471 -15.614 -0.076  1.00 8.70  ? 216 GLN B CG  1 
ATOM   3933  C  CD  . GLN B 1 216 ? -10.428 -17.035 -0.546  1.00 12.52 ? 216 GLN B CD  1 
ATOM   3934  O  OE1 . GLN B 1 216 ? -11.055 -17.513 -1.542  1.00 10.78 ? 216 GLN B OE1 1 
ATOM   3935  N  NE2 . GLN B 1 216 ? -9.610  -17.779 0.203   1.00 18.82 ? 216 GLN B NE2 1 
ATOM   3936  N  N   . ILE B 1 217 ? -10.924 -11.869 -2.714  1.00 6.43  ? 217 ILE B N   1 
ATOM   3937  C  CA  . ILE B 1 217 ? -11.365 -11.427 -4.041  1.00 5.58  ? 217 ILE B CA  1 
ATOM   3938  C  C   . ILE B 1 217 ? -10.419 -12.107 -5.062  1.00 6.41  ? 217 ILE B C   1 
ATOM   3939  O  O   . ILE B 1 217 ? -9.278  -12.479 -4.627  1.00 6.45  ? 217 ILE B O   1 
ATOM   3940  C  CB  . ILE B 1 217 ? -11.341 -9.841  -4.132  1.00 6.25  ? 217 ILE B CB  1 
ATOM   3941  C  CG1 . ILE B 1 217 ? -9.932  -9.333  -4.141  1.00 5.85  ? 217 ILE B CG1 1 
ATOM   3942  C  CG2 . ILE B 1 217 ? -12.256 -9.231  -3.038  1.00 7.86  ? 217 ILE B CG2 1 
ATOM   3943  C  CD1 . ILE B 1 217 ? -9.915  -7.708  -4.241  1.00 9.77  ? 217 ILE B CD1 1 
ATOM   3944  N  N   . SER B 1 218 ? -10.749 -12.117 -6.339  1.00 5.97  ? 218 SER B N   1 
ATOM   3945  C  CA  . SER B 1 218 ? -9.864  -12.870 -7.220  1.00 5.95  ? 218 SER B CA  1 
ATOM   3946  C  C   . SER B 1 218 ? -8.698  -12.116 -7.674  1.00 6.78  ? 218 SER B C   1 
ATOM   3947  O  O   . SER B 1 218 ? -8.667  -10.828 -7.584  1.00 7.21  ? 218 SER B O   1 
ATOM   3948  C  CB  . SER B 1 218 ? -10.646 -13.395 -8.401  1.00 7.02  ? 218 SER B CB  1 
ATOM   3949  O  OG  . SER B 1 218 ? -11.093 -12.255 -9.201  1.00 9.49  ? 218 SER B OG  1 
ATOM   3950  N  N   . GLN B 1 219 ? -7.735  -12.744 -8.310  1.00 9.11  ? 219 GLN B N   1 
ATOM   3951  C  CA  . GLN B 1 219 ? -6.609  -12.094 -8.973  1.00 9.36  ? 219 GLN B CA  1 
ATOM   3952  C  C   . GLN B 1 219 ? -7.128  -11.070 -10.029 1.00 10.38 ? 219 GLN B C   1 
ATOM   3953  O  O   . GLN B 1 219 ? -6.550  -9.976  -10.166 1.00 8.99  ? 219 GLN B O   1 
ATOM   3954  C  CB  . GLN B 1 219 ? -5.733  -13.160 -9.740  1.00 12.17 ? 219 GLN B CB  1 
ATOM   3955  C  CG  . GLN B 1 219 ? -4.374  -12.515 -10.164 1.00 18.92 ? 219 GLN B CG  1 
ATOM   3956  C  CD  . GLN B 1 219 ? -4.403  -11.870 -11.505 1.00 23.36 ? 219 GLN B CD  1 
ATOM   3957  O  OE1 . GLN B 1 219 ? -3.581  -11.005 -11.805 1.00 25.10 ? 219 GLN B OE1 1 
ATOM   3958  N  NE2 . GLN B 1 219 ? -5.357  -12.263 -12.316 1.00 21.79 ? 219 GLN B NE2 1 
ATOM   3959  N  N   . GLU B 1 220 ? -8.159  -11.414 -10.745 1.00 9.98  ? 220 GLU B N   1 
ATOM   3960  C  CA  . GLU B 1 220 ? -8.701  -10.490 -11.800 1.00 9.94  ? 220 GLU B CA  1 
ATOM   3961  C  C   . GLU B 1 220 ? -9.295  -9.264  -11.190 1.00 10.08 ? 220 GLU B C   1 
ATOM   3962  O  O   . GLU B 1 220 ? -9.208  -8.180  -11.744 1.00 10.65 ? 220 GLU B O   1 
ATOM   3963  C  CB  . GLU B 1 220 ? -9.699  -11.207 -12.671 1.00 12.52 ? 220 GLU B CB  1 
ATOM   3964  C  CG  . GLU B 1 220 ? -9.108  -12.292 -13.563 1.00 13.00 ? 220 GLU B CG  1 
ATOM   3965  C  CD  . GLU B 1 220 ? -8.836  -13.599 -12.820 1.00 18.95 ? 220 GLU B CD  1 
ATOM   3966  O  OE1 . GLU B 1 220 ? -9.269  -13.742 -11.660 1.00 13.60 ? 220 GLU B OE1 1 
ATOM   3967  O  OE2 . GLU B 1 220 ? -8.187  -14.488 -13.408 1.00 20.45 ? 220 GLU B OE2 1 
ATOM   3968  N  N   . GLN B 1 221 ? -9.922  -9.442  -10.021 1.00 7.94  ? 221 GLN B N   1 
ATOM   3969  C  CA  . GLN B 1 221 ? -10.537 -8.279  -9.340  1.00 7.85  ? 221 GLN B CA  1 
ATOM   3970  C  C   . GLN B 1 221 ? -9.447  -7.427  -8.751  1.00 8.96  ? 221 GLN B C   1 
ATOM   3971  O  O   . GLN B 1 221 ? -9.481  -6.174  -8.964  1.00 7.53  ? 221 GLN B O   1 
ATOM   3972  C  CB  . GLN B 1 221 ? -11.436 -8.723  -8.202  1.00 7.99  ? 221 GLN B CB  1 
ATOM   3973  C  CG  . GLN B 1 221 ? -12.689 -9.309  -8.686  1.00 6.94  ? 221 GLN B CG  1 
ATOM   3974  C  CD  . GLN B 1 221 ? -13.590 -9.732  -7.554  1.00 8.08  ? 221 GLN B CD  1 
ATOM   3975  O  OE1 . GLN B 1 221 ? -13.288 -10.726 -6.797  1.00 9.15  ? 221 GLN B OE1 1 
ATOM   3976  N  NE2 . GLN B 1 221 ? -14.784 -9.084  -7.403  1.00 7.70  ? 221 GLN B NE2 1 
ATOM   3977  N  N   . LEU B 1 222 ? -8.406  -7.991  -8.180  1.00 7.20  ? 222 LEU B N   1 
ATOM   3978  C  CA  . LEU B 1 222 ? -7.268  -7.215  -7.720  1.00 6.67  ? 222 LEU B CA  1 
ATOM   3979  C  C   . LEU B 1 222 ? -6.659  -6.498  -8.949  1.00 7.75  ? 222 LEU B C   1 
ATOM   3980  O  O   . LEU B 1 222 ? -6.255  -5.318  -8.780  1.00 9.15  ? 222 LEU B O   1 
ATOM   3981  C  CB  . LEU B 1 222 ? -6.216  -8.120  -7.037  1.00 8.53  ? 222 LEU B CB  1 
ATOM   3982  C  CG  . LEU B 1 222 ? -6.596  -8.452  -5.615  1.00 8.29  ? 222 LEU B CG  1 
ATOM   3983  C  CD1 . LEU B 1 222 ? -5.920  -9.766  -5.083  1.00 9.58  ? 222 LEU B CD1 1 
ATOM   3984  C  CD2 . LEU B 1 222 ? -6.266  -7.230  -4.672  1.00 11.03 ? 222 LEU B CD2 1 
ATOM   3985  N  N   . LEU B 1 223 ? -6.448  -7.137  -10.094 1.00 8.15  ? 223 LEU B N   1 
ATOM   3986  C  CA  . LEU B 1 223 ? -5.784  -6.491  -11.242 1.00 7.99  ? 223 LEU B CA  1 
ATOM   3987  C  C   . LEU B 1 223 ? -6.652  -5.343  -11.659 1.00 9.64  ? 223 LEU B C   1 
ATOM   3988  O  O   . LEU B 1 223 ? -6.030  -4.317  -12.046 1.00 10.83 ? 223 LEU B O   1 
ATOM   3989  C  CB  . LEU B 1 223 ? -5.563  -7.580  -12.376 1.00 10.64 ? 223 LEU B CB  1 
ATOM   3990  C  CG  . LEU B 1 223 ? -4.752  -6.999  -13.528 1.00 10.20 ? 223 LEU B CG  1 
ATOM   3991  C  CD1 . LEU B 1 223 ? -3.433  -6.660  -13.239 1.00 13.08 ? 223 LEU B CD1 1 
ATOM   3992  C  CD2 . LEU B 1 223 ? -4.794  -8.060  -14.652 1.00 15.74 ? 223 LEU B CD2 1 
ATOM   3993  N  N   . ALA B 1 224 ? -7.969  -5.529  -11.699 1.00 9.85  ? 224 ALA B N   1 
ATOM   3994  C  CA  . ALA B 1 224 ? -8.831  -4.389  -12.129 1.00 10.10 ? 224 ALA B CA  1 
ATOM   3995  C  C   . ALA B 1 224 ? -8.607  -3.243  -11.146 1.00 11.50 ? 224 ALA B C   1 
ATOM   3996  O  O   . ALA B 1 224 ? -8.353  -2.067  -11.568 1.00 12.06 ? 224 ALA B O   1 
ATOM   3997  C  CB  . ALA B 1 224 ? -10.273 -4.720  -12.113 1.00 12.49 ? 224 ALA B CB  1 
ATOM   3998  N  N   . LEU B 1 225 ? -8.642  -3.457  -9.833  1.00 8.90  ? 225 LEU B N   1 
ATOM   3999  C  CA  . LEU B 1 225 ? -8.467  -2.387  -8.856  1.00 9.55  ? 225 LEU B CA  1 
ATOM   4000  C  C   . LEU B 1 225 ? -7.139  -1.737  -8.969  1.00 9.57  ? 225 LEU B C   1 
ATOM   4001  O  O   . LEU B 1 225 ? -7.041  -0.493  -8.880  1.00 11.14 ? 225 LEU B O   1 
ATOM   4002  C  CB  . LEU B 1 225 ? -8.694  -3.000  -7.443  1.00 7.64  ? 225 LEU B CB  1 
ATOM   4003  C  CG  . LEU B 1 225 ? -8.457  -2.061  -6.287  1.00 10.78 ? 225 LEU B CG  1 
ATOM   4004  C  CD1 . LEU B 1 225 ? -9.519  -0.955  -6.364  1.00 10.33 ? 225 LEU B CD1 1 
ATOM   4005  C  CD2 . LEU B 1 225 ? -8.492  -2.854  -4.949  1.00 10.81 ? 225 LEU B CD2 1 
ATOM   4006  N  N   . GLU B 1 226 ? -6.081  -2.466  -9.282  1.00 8.30  ? 226 GLU B N   1 
ATOM   4007  C  CA  . GLU B 1 226 ? -4.727  -1.998  -9.353  1.00 8.40  ? 226 GLU B CA  1 
ATOM   4008  C  C   . GLU B 1 226 ? -4.397  -1.279  -10.706 1.00 8.00  ? 226 GLU B C   1 
ATOM   4009  O  O   . GLU B 1 226 ? -3.288  -0.684  -10.744 1.00 12.81 ? 226 GLU B O   1 
ATOM   4010  C  CB  . GLU B 1 226 ? -3.748  -3.188  -9.191  1.00 9.01  ? 226 GLU B CB  1 
ATOM   4011  C  CG  . GLU B 1 226 ? -3.811  -3.826  -7.828  1.00 9.65  ? 226 GLU B CG  1 
ATOM   4012  C  CD  . GLU B 1 226 ? -3.400  -5.254  -7.855  1.00 10.43 ? 226 GLU B CD  1 
ATOM   4013  O  OE1 . GLU B 1 226 ? -3.126  -5.888  -8.903  1.00 11.41 ? 226 GLU B OE1 1 
ATOM   4014  O  OE2 . GLU B 1 226 ? -3.457  -5.893  -6.795  1.00 9.72  ? 226 GLU B OE2 1 
ATOM   4015  N  N   . THR B 1 227 ? -5.276  -1.433  -11.674 1.00 8.98  ? 227 THR B N   1 
ATOM   4016  C  CA  . THR B 1 227 ? -4.981  -0.815  -12.982 1.00 10.36 ? 227 THR B CA  1 
ATOM   4017  C  C   . THR B 1 227 ? -6.015  0.187   -13.384 1.00 12.47 ? 227 THR B C   1 
ATOM   4018  O  O   . THR B 1 227 ? -5.709  0.881   -14.374 1.00 15.27 ? 227 THR B O   1 
ATOM   4019  C  CB  . THR B 1 227 ? -4.914  -1.898  -14.134 1.00 11.64 ? 227 THR B CB  1 
ATOM   4020  O  OG1 . THR B 1 227 ? -6.133  -2.648  -14.231 1.00 11.37 ? 227 THR B OG1 1 
ATOM   4021  C  CG2 . THR B 1 227 ? -3.701  -2.897  -13.935 1.00 11.53 ? 227 THR B CG2 1 
ATOM   4022  N  N   . ALA B 1 228 ? -7.110  0.348   -12.690 1.00 8.97  ? 228 ALA B N   1 
ATOM   4023  C  CA  . ALA B 1 228 ? -8.237  1.158   -13.234 1.00 10.26 ? 228 ALA B CA  1 
ATOM   4024  C  C   . ALA B 1 228 ? -7.947  2.654   -12.954 1.00 10.71 ? 228 ALA B C   1 
ATOM   4025  O  O   . ALA B 1 228 ? -8.569  3.485   -13.623 1.00 14.40 ? 228 ALA B O   1 
ATOM   4026  C  CB  . ALA B 1 228 ? -9.459  0.801   -12.627 1.00 12.53 ? 228 ALA B CB  1 
ATOM   4027  N  N   . LEU B 1 229 ? -7.230  2.979   -11.912 1.00 8.62  ? 229 LEU B N   1 
ATOM   4028  C  CA  . LEU B 1 229 ? -7.360  4.312   -11.284 1.00 9.43  ? 229 LEU B CA  1 
ATOM   4029  C  C   . LEU B 1 229 ? -6.067  5.049   -11.276 1.00 9.44  ? 229 LEU B C   1 
ATOM   4030  O  O   . LEU B 1 229 ? -4.968  4.560   -11.214 1.00 8.52  ? 229 LEU B O   1 
ATOM   4031  C  CB  . LEU B 1 229 ? -7.836  4.177   -9.818  1.00 11.30 ? 229 LEU B CB  1 
ATOM   4032  C  CG  . LEU B 1 229 ? -9.159  3.383   -9.610  1.00 11.20 ? 229 LEU B CG  1 
ATOM   4033  C  CD1 . LEU B 1 229 ? -9.414  3.174   -8.113  1.00 12.13 ? 229 LEU B CD1 1 
ATOM   4034  C  CD2 . LEU B 1 229 ? -10.269 4.023   -10.243 1.00 14.99 ? 229 LEU B CD2 1 
ATOM   4035  N  N   . TYR B 1 230 ? -6.283  6.372   -11.360 1.00 9.30  ? 230 TYR B N   1 
ATOM   4036  C  CA  . TYR B 1 230 ? -5.213  7.423   -11.362 1.00 10.00 ? 230 TYR B CA  1 
ATOM   4037  C  C   . TYR B 1 230 ? -5.368  8.373   -10.213 1.00 8.04  ? 230 TYR B C   1 
ATOM   4038  O  O   . TYR B 1 230 ? -6.530  8.718   -9.901  1.00 9.06  ? 230 TYR B O   1 
ATOM   4039  C  CB  . TYR B 1 230 ? -5.163  8.138   -12.745 1.00 10.65 ? 230 TYR B CB  1 
ATOM   4040  C  CG  . TYR B 1 230 ? -4.589  7.184   -13.754 1.00 8.42  ? 230 TYR B CG  1 
ATOM   4041  C  CD1 . TYR B 1 230 ? -3.234  7.186   -14.053 1.00 11.24 ? 230 TYR B CD1 1 
ATOM   4042  C  CD2 . TYR B 1 230 ? -5.397  6.231   -14.367 1.00 8.87  ? 230 TYR B CD2 1 
ATOM   4043  C  CE1 . TYR B 1 230 ? -2.706  6.292   -14.965 1.00 14.99 ? 230 TYR B CE1 1 
ATOM   4044  C  CE2 . TYR B 1 230 ? -4.874  5.335   -15.279 1.00 10.67 ? 230 TYR B CE2 1 
ATOM   4045  C  CZ  . TYR B 1 230 ? -3.527  5.372   -15.571 1.00 10.91 ? 230 TYR B CZ  1 
ATOM   4046  O  OH  . TYR B 1 230 ? -3.006  4.484   -16.475 1.00 19.07 ? 230 TYR B OH  1 
ATOM   4047  N  N   . CYS B 1 231 ? -4.273  8.836   -9.629  1.00 9.24  ? 231 CYS B N   1 
ATOM   4048  C  CA  . CYS B 1 231 ? -4.324  9.864   -8.571  1.00 8.63  ? 231 CYS B CA  1 
ATOM   4049  C  C   . CYS B 1 231 ? -4.640  11.257  -9.167  1.00 9.57  ? 231 CYS B C   1 
ATOM   4050  O  O   . CYS B 1 231 ? -4.973  12.173  -8.468  1.00 10.98 ? 231 CYS B O   1 
ATOM   4051  C  CB  . CYS B 1 231 ? -2.966  10.043  -7.901  1.00 8.39  ? 231 CYS B CB  1 
ATOM   4052  S  SG  . CYS B 1 231 ? -2.487  8.438   -7.055  1.00 10.57 ? 231 CYS B SG  1 
ATOM   4053  N  N   . THR B 1 232 ? -4.387  11.374  -10.450 1.00 9.15  ? 232 THR B N   1 
ATOM   4054  C  CA  . THR B 1 232 ? -4.357  12.719  -11.087 1.00 8.47  ? 232 THR B CA  1 
ATOM   4055  C  C   . THR B 1 232 ? -5.682  12.902  -11.885 1.00 9.46  ? 232 THR B C   1 
ATOM   4056  O  O   . THR B 1 232 ? -6.419  12.035  -12.226 1.00 9.77  ? 232 THR B O   1 
ATOM   4057  C  CB  . THR B 1 232 ? -3.183  12.748  -12.110 1.00 9.20  ? 232 THR B CB  1 
ATOM   4058  O  OG1 . THR B 1 232 ? -2.983  11.440  -12.742 1.00 9.19  ? 232 THR B OG1 1 
ATOM   4059  C  CG2 . THR B 1 232 ? -1.904  13.098  -11.358 1.00 11.50 ? 232 THR B CG2 1 
ATOM   4060  N  N   . HIS B 1 233 ? -5.942  14.209  -12.224 1.00 8.75  ? 233 HIS B N   1 
ATOM   4061  C  CA  . HIS B 1 233 ? -7.058  14.508  -13.100 1.00 9.61  ? 233 HIS B CA  1 
ATOM   4062  C  C   . HIS B 1 233 ? -6.952  13.986  -14.535 1.00 8.47  ? 233 HIS B C   1 
ATOM   4063  O  O   . HIS B 1 233 ? -5.816  13.758  -15.006 1.00 9.78  ? 233 HIS B O   1 
ATOM   4064  C  CB  . HIS B 1 233 ? -7.246  16.041  -13.153 1.00 11.57 ? 233 HIS B CB  1 
ATOM   4065  C  CG  . HIS B 1 233 ? -7.702  16.626  -11.850 1.00 12.73 ? 233 HIS B CG  1 
ATOM   4066  N  ND1 . HIS B 1 233 ? -6.858  17.389  -11.059 1.00 20.45 ? 233 HIS B ND1 1 
ATOM   4067  C  CD2 . HIS B 1 233 ? -8.865  16.537  -11.190 1.00 16.77 ? 233 HIS B CD2 1 
ATOM   4068  C  CE1 . HIS B 1 233 ? -7.498  17.743  -9.960  1.00 22.80 ? 233 HIS B CE1 1 
ATOM   4069  N  NE2 . HIS B 1 233 ? -8.695  17.203  -9.990  1.00 17.92 ? 233 HIS B NE2 1 
ATOM   4070  N  N   A MET B 1 234 ? -8.088  13.815  -15.210 0.50 9.51  ? 234 MET B N   1 
ATOM   4071  N  N   B MET B 1 234 ? -8.070  13.862  -15.265 0.50 10.31 ? 234 MET B N   1 
ATOM   4072  C  CA  A MET B 1 234 ? -8.154  13.351  -16.579 0.50 8.96  ? 234 MET B CA  1 
ATOM   4073  C  CA  B MET B 1 234 ? -8.083  13.304  -16.623 0.50 12.32 ? 234 MET B CA  1 
ATOM   4074  C  C   A MET B 1 234 ? -7.105  14.081  -17.457 0.50 9.55  ? 234 MET B C   1 
ATOM   4075  C  C   B MET B 1 234 ? -7.245  14.110  -17.623 0.50 10.51 ? 234 MET B C   1 
ATOM   4076  O  O   A MET B 1 234 ? -6.366  13.479  -18.186 0.50 9.69  ? 234 MET B O   1 
ATOM   4077  O  O   B MET B 1 234 ? -6.791  13.569  -18.662 0.50 9.55  ? 234 MET B O   1 
ATOM   4078  C  CB  A MET B 1 234 ? -9.580  13.543  -17.114 0.50 10.86 ? 234 MET B CB  1 
ATOM   4079  C  CB  B MET B 1 234 ? -9.511  13.111  -17.163 0.50 11.55 ? 234 MET B CB  1 
ATOM   4080  C  CG  A MET B 1 234 ? -9.858  12.888  -18.482 0.50 9.50  ? 234 MET B CG  1 
ATOM   4081  C  CG  B MET B 1 234 ? -9.585  12.140  -18.383 0.50 15.89 ? 234 MET B CG  1 
ATOM   4082  S  SD  A MET B 1 234 ? -11.639 12.615  -18.711 0.50 13.40 ? 234 MET B SD  1 
ATOM   4083  S  SD  B MET B 1 234 ? -11.318 11.756  -18.784 0.50 23.81 ? 234 MET B SD  1 
ATOM   4084  C  CE  A MET B 1 234 ? -11.566 11.534  -20.139 0.50 15.69 ? 234 MET B CE  1 
ATOM   4085  C  CE  B MET B 1 234 ? -11.532 13.317  -19.643 0.50 16.01 ? 234 MET B CE  1 
ATOM   4086  N  N   . ASP B 1 235 ? -7.051  15.402  -17.316 1.00 12.26 ? 235 ASP B N   1 
ATOM   4087  C  CA  . ASP B 1 235 ? -6.222  16.215  -18.240 1.00 13.80 ? 235 ASP B CA  1 
ATOM   4088  C  C   . ASP B 1 235 ? -4.858  16.525  -17.722 1.00 14.14 ? 235 ASP B C   1 
ATOM   4089  O  O   . ASP B 1 235 ? -4.171  17.432  -18.219 1.00 17.66 ? 235 ASP B O   1 
ATOM   4090  C  CB  . ASP B 1 235 ? -6.976  17.524  -18.552 1.00 16.81 ? 235 ASP B CB  1 
ATOM   4091  C  CG  . ASP B 1 235 ? -6.998  18.446  -17.370 1.00 20.10 ? 235 ASP B CG  1 
ATOM   4092  O  OD1 . ASP B 1 235 ? -6.768  18.053  -16.168 1.00 20.93 ? 235 ASP B OD1 1 
ATOM   4093  O  OD2 . ASP B 1 235 ? -7.413  19.657  -17.568 1.00 27.62 ? 235 ASP B OD2 1 
ATOM   4094  N  N   . ASP B 1 236 ? -4.320  15.766  -16.751 1.00 11.04 ? 236 ASP B N   1 
ATOM   4095  C  CA  . ASP B 1 236 ? -3.050  16.085  -16.178 1.00 10.00 ? 236 ASP B CA  1 
ATOM   4096  C  C   . ASP B 1 236 ? -1.918  15.591  -17.090 1.00 10.88 ? 236 ASP B C   1 
ATOM   4097  O  O   . ASP B 1 236 ? -1.909  14.436  -17.499 1.00 10.28 ? 236 ASP B O   1 
ATOM   4098  C  CB  . ASP B 1 236 ? -2.908  15.386  -14.814 1.00 11.32 ? 236 ASP B CB  1 
ATOM   4099  C  CG  . ASP B 1 236 ? -1.737  15.993  -13.992 1.00 12.19 ? 236 ASP B CG  1 
ATOM   4100  O  OD1 . ASP B 1 236 ? -0.591  16.141  -14.484 1.00 12.63 ? 236 ASP B OD1 1 
ATOM   4101  O  OD2 . ASP B 1 236 ? -1.894  16.262  -12.782 1.00 14.54 ? 236 ASP B OD2 1 
ATOM   4102  N  N   . PRO B 1 237 ? -0.973  16.453  -17.523 1.00 10.35 ? 237 PRO B N   1 
ATOM   4103  C  CA  . PRO B 1 237 ? 0.118   15.985  -18.364 1.00 11.48 ? 237 PRO B CA  1 
ATOM   4104  C  C   . PRO B 1 237 ? 1.172   15.099  -17.684 1.00 10.46 ? 237 PRO B C   1 
ATOM   4105  O  O   . PRO B 1 237 ? 2.067   14.583  -18.371 1.00 9.95  ? 237 PRO B O   1 
ATOM   4106  C  CB  . PRO B 1 237 ? 0.731   17.323  -18.878 1.00 11.57 ? 237 PRO B CB  1 
ATOM   4107  C  CG  . PRO B 1 237 ? 0.439   18.232  -17.748 1.00 12.90 ? 237 PRO B CG  1 
ATOM   4108  C  CD  . PRO B 1 237 ? -0.951  17.942  -17.331 1.00 11.75 ? 237 PRO B CD  1 
ATOM   4109  N  N   A SER B 1 238 ? 1.043   14.927  -16.346 0.50 8.91  ? 238 SER B N   1 
ATOM   4110  N  N   B SER B 1 238 ? 1.117   14.932  -16.335 0.50 8.56  ? 238 SER B N   1 
ATOM   4111  C  CA  A SER B 1 238 ? 1.964   14.097  -15.576 0.50 10.09 ? 238 SER B CA  1 
ATOM   4112  C  CA  B SER B 1 238 ? 1.990   13.964  -15.626 0.50 9.61  ? 238 SER B CA  1 
ATOM   4113  C  C   A SER B 1 238 ? 1.211   13.015  -14.810 0.50 8.69  ? 238 SER B C   1 
ATOM   4114  C  C   B SER B 1 238 ? 1.069   13.051  -14.814 0.50 7.97  ? 238 SER B C   1 
ATOM   4115  O  O   A SER B 1 238 ? 1.313   13.006  -13.602 0.50 9.62  ? 238 SER B O   1 
ATOM   4116  O  O   B SER B 1 238 ? 0.802   13.221  -13.614 0.50 8.42  ? 238 SER B O   1 
ATOM   4117  C  CB  A SER B 1 238 ? 2.744   14.896  -14.532 0.50 8.87  ? 238 SER B CB  1 
ATOM   4118  C  CB  B SER B 1 238 ? 3.038   14.592  -14.747 0.50 9.18  ? 238 SER B CB  1 
ATOM   4119  O  OG  A SER B 1 238 ? 3.860   14.071  -14.250 0.50 14.27 ? 238 SER B OG  1 
ATOM   4120  O  OG  B SER B 1 238 ? 3.642   15.708  -15.403 0.50 11.69 ? 238 SER B OG  1 
ATOM   4121  N  N   . PRO B 1 239 ? 0.541   12.094  -15.531 1.00 9.26  ? 239 PRO B N   1 
ATOM   4122  C  CA  . PRO B 1 239 ? -0.362  11.135  -14.825 1.00 9.94  ? 239 PRO B CA  1 
ATOM   4123  C  C   . PRO B 1 239 ? 0.407   10.313  -13.801 1.00 10.28 ? 239 PRO B C   1 
ATOM   4124  O  O   . PRO B 1 239 ? 1.580   9.964   -13.988 1.00 9.58  ? 239 PRO B O   1 
ATOM   4125  C  CB  . PRO B 1 239 ? -0.853  10.201  -15.945 1.00 11.46 ? 239 PRO B CB  1 
ATOM   4126  C  CG  . PRO B 1 239 ? -0.471  10.830  -17.247 1.00 15.43 ? 239 PRO B CG  1 
ATOM   4127  C  CD  . PRO B 1 239 ? 0.585   11.877  -17.002 1.00 10.91 ? 239 PRO B CD  1 
ATOM   4128  N  N   . ARG B 1 240 ? -0.319  9.999   -12.711 1.00 9.50  ? 240 ARG B N   1 
ATOM   4129  C  CA  . ARG B 1 240 ? 0.251   9.067   -11.692 1.00 9.56  ? 240 ARG B CA  1 
ATOM   4130  C  C   . ARG B 1 240 ? -0.780  7.948   -11.400 1.00 7.23  ? 240 ARG B C   1 
ATOM   4131  O  O   . ARG B 1 240 ? -1.922  8.237   -11.077 1.00 9.90  ? 240 ARG B O   1 
ATOM   4132  C  CB  . ARG B 1 240 ? 0.536   9.782   -10.382 1.00 7.87  ? 240 ARG B CB  1 
ATOM   4133  C  CG  . ARG B 1 240 ? 1.737   10.747  -10.631 1.00 10.39 ? 240 ARG B CG  1 
ATOM   4134  C  CD  . ARG B 1 240 ? 1.993   11.512  -9.336  1.00 13.02 ? 240 ARG B CD  1 
ATOM   4135  N  NE  . ARG B 1 240 ? 0.925   12.491  -9.016  1.00 16.44 ? 240 ARG B NE  1 
ATOM   4136  C  CZ  . ARG B 1 240 ? 0.026   12.355  -8.012  1.00 20.41 ? 240 ARG B CZ  1 
ATOM   4137  N  NH1 . ARG B 1 240 ? -0.004  11.277  -7.212  1.00 13.37 ? 240 ARG B NH1 1 
ATOM   4138  N  NH2 . ARG B 1 240 ? -0.891  13.262  -7.852  1.00 16.64 ? 240 ARG B NH2 1 
ATOM   4139  N  N   . GLU B 1 241 ? -0.402  6.703   -11.629 1.00 9.78  ? 241 GLU B N   1 
ATOM   4140  C  CA  . GLU B 1 241 ? -1.272  5.566   -11.292 1.00 9.72  ? 241 GLU B CA  1 
ATOM   4141  C  C   . GLU B 1 241 ? -1.535  5.517   -9.759  1.00 6.67  ? 241 GLU B C   1 
ATOM   4142  O  O   . GLU B 1 241 ? -0.635  5.672   -8.964  1.00 8.51  ? 241 GLU B O   1 
ATOM   4143  C  CB  . GLU B 1 241 ? -0.584  4.282   -11.674 1.00 10.02 ? 241 GLU B CB  1 
ATOM   4144  C  CG  . GLU B 1 241 ? -0.415  4.184   -13.207 1.00 13.27 ? 241 GLU B CG  1 
ATOM   4145  C  CD  . GLU B 1 241 ? 0.480   3.063   -13.634 1.00 18.13 ? 241 GLU B CD  1 
ATOM   4146  O  OE1 . GLU B 1 241 ? 1.629   3.121   -13.214 1.00 22.08 ? 241 GLU B OE1 1 
ATOM   4147  O  OE2 . GLU B 1 241 ? -0.013  2.096   -14.241 1.00 25.05 ? 241 GLU B OE2 1 
ATOM   4148  N  N   . MET B 1 242 ? -2.800  5.169   -9.457  1.00 7.20  ? 242 MET B N   1 
ATOM   4149  C  CA  . MET B 1 242 ? -3.153  4.969   -7.999  1.00 8.77  ? 242 MET B CA  1 
ATOM   4150  C  C   . MET B 1 242 ? -2.885  3.481   -7.645  1.00 6.72  ? 242 MET B C   1 
ATOM   4151  O  O   . MET B 1 242 ? -3.682  2.587   -7.901  1.00 7.45  ? 242 MET B O   1 
ATOM   4152  C  CB  . MET B 1 242 ? -4.618  5.331   -7.830  1.00 8.46  ? 242 MET B CB  1 
ATOM   4153  C  CG  . MET B 1 242 ? -5.012  5.360   -6.344  1.00 7.71  ? 242 MET B CG  1 
ATOM   4154  S  SD  . MET B 1 242 ? -6.726  5.649   -6.071  1.00 8.61  ? 242 MET B SD  1 
ATOM   4155  C  CE  . MET B 1 242 ? -6.814  7.371   -6.520  1.00 9.40  ? 242 MET B CE  1 
ATOM   4156  N  N   . ILE B 1 243 ? -1.657  3.329   -7.168  1.00 6.70  ? 243 ILE B N   1 
ATOM   4157  C  CA  . ILE B 1 243 ? -1.076  2.031   -6.799  1.00 7.00  ? 243 ILE B CA  1 
ATOM   4158  C  C   . ILE B 1 243 ? -0.324  2.210   -5.498  1.00 6.64  ? 243 ILE B C   1 
ATOM   4159  O  O   . ILE B 1 243 ? 0.132   3.348   -5.150  1.00 7.80  ? 243 ILE B O   1 
ATOM   4160  C  CB  . ILE B 1 243 ? -0.104  1.370   -7.895  1.00 8.74  ? 243 ILE B CB  1 
ATOM   4161  C  CG1 . ILE B 1 243 ? 0.934   2.447   -8.305  1.00 9.62  ? 243 ILE B CG1 1 
ATOM   4162  C  CG2 . ILE B 1 243 ? -0.967  0.919   -9.043  1.00 8.76  ? 243 ILE B CG2 1 
ATOM   4163  C  CD1 . ILE B 1 243 ? 1.963   1.932   -9.266  1.00 12.36 ? 243 ILE B CD1 1 
ATOM   4164  N  N   . ASN B 1 244 ? -0.179  1.094   -4.749  1.00 7.13  ? 244 ASN B N   1 
ATOM   4165  C  CA  . ASN B 1 244 ? 0.635   1.170   -3.532  1.00 6.77  ? 244 ASN B CA  1 
ATOM   4166  C  C   . ASN B 1 244 ? 0.268   2.266   -2.572  1.00 7.05  ? 244 ASN B C   1 
ATOM   4167  O  O   . ASN B 1 244 ? 1.053   2.851   -1.941  1.00 7.62  ? 244 ASN B O   1 
ATOM   4168  C  CB  . ASN B 1 244 ? 2.146   1.286   -3.906  1.00 7.80  ? 244 ASN B CB  1 
ATOM   4169  C  CG  . ASN B 1 244 ? 2.530   0.196   -4.873  1.00 8.69  ? 244 ASN B CG  1 
ATOM   4170  O  OD1 . ASN B 1 244 ? 2.200   -1.021  -4.771  1.00 11.32 ? 244 ASN B OD1 1 
ATOM   4171  N  ND2 . ASN B 1 244 ? 3.314   0.612   -5.862  1.00 15.72 ? 244 ASN B ND2 1 
ATOM   4172  N  N   . ASN B 1 245 ? -1.067  2.373   -2.411  1.00 6.53  ? 245 ASN B N   1 
ATOM   4173  C  CA  . ASN B 1 245 ? -1.636  3.450   -1.599  1.00 5.41  ? 245 ASN B CA  1 
ATOM   4174  C  C   . ASN B 1 245 ? -1.942  2.908   -0.170  1.00 6.24  ? 245 ASN B C   1 
ATOM   4175  O  O   . ASN B 1 245 ? -3.046  3.036   0.345   1.00 6.54  ? 245 ASN B O   1 
ATOM   4176  C  CB  . ASN B 1 245 ? -2.927  4.035   -2.273  1.00 6.68  ? 245 ASN B CB  1 
ATOM   4177  C  CG  . ASN B 1 245 ? -4.054  3.083   -2.436  1.00 6.29  ? 245 ASN B CG  1 
ATOM   4178  O  OD1 . ASN B 1 245 ? -3.818  1.847   -2.460  1.00 7.65  ? 245 ASN B OD1 1 
ATOM   4179  N  ND2 . ASN B 1 245 ? -5.279  3.578   -2.642  1.00 6.52  ? 245 ASN B ND2 1 
ATOM   4180  N  N   . PHE B 1 246 ? -0.874  2.414   0.453   1.00 4.66  ? 246 PHE B N   1 
ATOM   4181  C  CA  . PHE B 1 246 ? -0.886  1.968   1.822   1.00 4.33  ? 246 PHE B CA  1 
ATOM   4182  C  C   . PHE B 1 246 ? 0.268   2.544   2.549   1.00 5.81  ? 246 PHE B C   1 
ATOM   4183  O  O   . PHE B 1 246 ? 1.369   2.733   1.979   1.00 6.74  ? 246 PHE B O   1 
ATOM   4184  C  CB  . PHE B 1 246 ? -0.865  0.415   1.891   1.00 6.92  ? 246 PHE B CB  1 
ATOM   4185  C  CG  . PHE B 1 246 ? 0.395   -0.223  1.281   1.00 6.56  ? 246 PHE B CG  1 
ATOM   4186  C  CD1 . PHE B 1 246 ? 1.481   -0.624  2.157   1.00 6.80  ? 246 PHE B CD1 1 
ATOM   4187  C  CD2 . PHE B 1 246 ? 0.472   -0.458  -0.102  1.00 6.73  ? 246 PHE B CD2 1 
ATOM   4188  C  CE1 . PHE B 1 246 ? 2.640   -1.139  1.612   1.00 7.39  ? 246 PHE B CE1 1 
ATOM   4189  C  CE2 . PHE B 1 246 ? 1.664   -1.028  -0.640  1.00 7.28  ? 246 PHE B CE2 1 
ATOM   4190  C  CZ  . PHE B 1 246 ? 2.752   -1.313  0.219   1.00 7.41  ? 246 PHE B CZ  1 
ATOM   4191  N  N   . ARG B 1 247 ? 0.073   2.854   3.833   1.00 5.61  ? 247 ARG B N   1 
ATOM   4192  C  CA  . ARG B 1 247 ? 1.181   3.344   4.684   1.00 5.65  ? 247 ARG B CA  1 
ATOM   4193  C  C   . ARG B 1 247 ? 1.931   2.176   5.305   1.00 5.99  ? 247 ARG B C   1 
ATOM   4194  O  O   . ARG B 1 247 ? 1.321   1.142   5.658   1.00 6.50  ? 247 ARG B O   1 
ATOM   4195  C  CB  . ARG B 1 247 ? 0.551   4.214   5.825   1.00 6.53  ? 247 ARG B CB  1 
ATOM   4196  C  CG  . ARG B 1 247 ? 1.527   5.106   6.575   1.00 5.79  ? 247 ARG B CG  1 
ATOM   4197  C  CD  . ARG B 1 247 ? 0.846   5.697   7.773   1.00 6.87  ? 247 ARG B CD  1 
ATOM   4198  N  NE  . ARG B 1 247 ? 1.718   6.812   8.311   1.00 6.89  ? 247 ARG B NE  1 
ATOM   4199  C  CZ  . ARG B 1 247 ? 1.392   7.567   9.377   1.00 7.80  ? 247 ARG B CZ  1 
ATOM   4200  N  NH1 . ARG B 1 247 ? 0.280   7.322   10.070  1.00 6.82  ? 247 ARG B NH1 1 
ATOM   4201  N  NH2 . ARG B 1 247 ? 2.183   8.578   9.759   1.00 7.61  ? 247 ARG B NH2 1 
ATOM   4202  N  N   . GLN B 1 248 ? 3.243   2.331   5.537   1.00 6.06  ? 248 GLN B N   1 
ATOM   4203  C  CA  . GLN B 1 248 ? 4.012   1.323   6.303   1.00 6.56  ? 248 GLN B CA  1 
ATOM   4204  C  C   . GLN B 1 248 ? 3.535   1.228   7.714   1.00 7.01  ? 248 GLN B C   1 
ATOM   4205  O  O   . GLN B 1 248 ? 2.939   2.171   8.258   1.00 7.51  ? 248 GLN B O   1 
ATOM   4206  C  CB  . GLN B 1 248 ? 5.494   1.728   6.332   1.00 6.24  ? 248 GLN B CB  1 
ATOM   4207  C  CG  . GLN B 1 248 ? 6.149   1.711   4.952   1.00 6.21  ? 248 GLN B CG  1 
ATOM   4208  C  CD  . GLN B 1 248 ? 6.168   0.348   4.330   1.00 6.95  ? 248 GLN B CD  1 
ATOM   4209  O  OE1 . GLN B 1 248 ? 5.313   0.008   3.499   1.00 7.26  ? 248 GLN B OE1 1 
ATOM   4210  N  NE2 . GLN B 1 248 ? 7.213   -0.425  4.669   1.00 8.17  ? 248 GLN B NE2 1 
ATOM   4211  N  N   . VAL B 1 249 ? 3.717   0.091   8.381   1.00 5.49  ? 249 VAL B N   1 
ATOM   4212  C  CA  . VAL B 1 249 ? 3.317   -0.018  9.780   1.00 7.65  ? 249 VAL B CA  1 
ATOM   4213  C  C   . VAL B 1 249 ? 4.133   0.887   10.680  1.00 8.27  ? 249 VAL B C   1 
ATOM   4214  O  O   . VAL B 1 249 ? 5.301   1.203   10.345  1.00 7.24  ? 249 VAL B O   1 
ATOM   4215  C  CB  . VAL B 1 249 ? 3.355   -1.505  10.258  1.00 8.19  ? 249 VAL B CB  1 
ATOM   4216  C  CG1 . VAL B 1 249 ? 2.279   -2.364  9.470   1.00 7.08  ? 249 VAL B CG1 1 
ATOM   4217  C  CG2 . VAL B 1 249 ? 4.711   -2.125  10.091  1.00 9.06  ? 249 VAL B CG2 1 
ATOM   4218  N  N   . GLN B 1 250 ? 3.528   1.252   11.793  1.00 7.05  ? 250 GLN B N   1 
ATOM   4219  C  CA  . GLN B 1 250 ? 4.104   2.223   12.697  1.00 7.10  ? 250 GLN B CA  1 
ATOM   4220  C  C   . GLN B 1 250 ? 4.609   1.622   13.993  1.00 7.32  ? 250 GLN B C   1 
ATOM   4221  O  O   . GLN B 1 250 ? 4.148   0.552   14.349  1.00 9.33  ? 250 GLN B O   1 
ATOM   4222  C  CB  . GLN B 1 250 ? 2.990   3.265   13.111  1.00 6.76  ? 250 GLN B CB  1 
ATOM   4223  C  CG  . GLN B 1 250 ? 2.318   3.900   11.882  1.00 9.03  ? 250 GLN B CG  1 
ATOM   4224  C  CD  . GLN B 1 250 ? 3.251   4.793   11.088  1.00 9.08  ? 250 GLN B CD  1 
ATOM   4225  O  OE1 . GLN B 1 250 ? 3.634   5.842   11.674  1.00 9.19  ? 250 GLN B OE1 1 
ATOM   4226  N  NE2 . GLN B 1 250 ? 3.529   4.531   9.820   1.00 8.52  ? 250 GLN B NE2 1 
ATOM   4227  N  N   . LYS B 1 251 ? 5.520   2.304   14.665  1.00 7.75  ? 251 LYS B N   1 
ATOM   4228  C  CA  . LYS B 1 251 ? 5.945   1.840   15.972  1.00 7.79  ? 251 LYS B CA  1 
ATOM   4229  C  C   . LYS B 1 251 ? 4.716   1.783   16.918  1.00 10.90 ? 251 LYS B C   1 
ATOM   4230  O  O   . LYS B 1 251 ? 3.833   2.557   16.799  1.00 10.19 ? 251 LYS B O   1 
ATOM   4231  C  CB  . LYS B 1 251 ? 6.993   2.779   16.592  1.00 11.04 ? 251 LYS B CB  1 
ATOM   4232  C  CG  . LYS B 1 251 ? 8.361   2.846   15.895  1.00 11.43 ? 251 LYS B CG  1 
ATOM   4233  C  CD  . LYS B 1 251 ? 9.214   1.725   16.408  1.00 10.86 ? 251 LYS B CD  1 
ATOM   4234  C  CE  . LYS B 1 251 ? 10.698  1.830   16.034  1.00 10.57 ? 251 LYS B CE  1 
ATOM   4235  N  NZ  . LYS B 1 251 ? 10.866  1.860   14.538  1.00 9.42  ? 251 LYS B NZ  1 
ATOM   4236  N  N   . PHE B 1 252 ? 4.687   0.778   17.759  1.00 11.67 ? 252 PHE B N   1 
ATOM   4237  C  CA  . PHE B 1 252 ? 3.571   0.617   18.649  1.00 14.39 ? 252 PHE B CA  1 
ATOM   4238  C  C   . PHE B 1 252 ? 3.991   1.049   20.021  1.00 24.85 ? 252 PHE B C   1 
ATOM   4239  O  O   . PHE B 1 252 ? 4.231   0.322   20.911  1.00 23.59 ? 252 PHE B O   1 
ATOM   4240  C  CB  . PHE B 1 252 ? 2.900   -0.742  18.492  1.00 20.71 ? 252 PHE B CB  1 
ATOM   4241  C  CG  . PHE B 1 252 ? 1.493   -0.749  18.968  1.00 18.96 ? 252 PHE B CG  1 
ATOM   4242  C  CD1 . PHE B 1 252 ? 0.618   0.256   18.597  1.00 16.42 ? 252 PHE B CD1 1 
ATOM   4243  C  CD2 . PHE B 1 252 ? 1.074   -1.712  19.832  1.00 20.76 ? 252 PHE B CD2 1 
ATOM   4244  C  CE1 . PHE B 1 252 ? -0.652  0.304   19.089  1.00 19.48 ? 252 PHE B CE1 1 
ATOM   4245  C  CE2 . PHE B 1 252 ? -0.219  -1.691  20.308  1.00 21.97 ? 252 PHE B CE2 1 
ATOM   4246  C  CZ  . PHE B 1 252 ? -1.085  -0.683  19.932  1.00 22.81 ? 252 PHE B CZ  1 
ATOM   4247  N  N   . ASP B 1 253 ? 4.264   2.289   20.087  1.00 30.00 ? 253 ASP B N   1 
ATOM   4248  C  CA  . ASP B 1 253 ? 4.997   2.666   21.299  1.00 30.00 ? 253 ASP B CA  1 
ATOM   4249  C  C   . ASP B 1 253 ? 4.289   2.687   22.664  1.00 30.00 ? 253 ASP B C   1 
ATOM   4250  O  O   . ASP B 1 253 ? 3.822   3.693   23.233  1.00 30.00 ? 253 ASP B O   1 
ATOM   4251  C  CB  . ASP B 1 253 ? 6.190   3.599   21.070  1.00 20.00 ? 253 ASP B CB  1 
ATOM   4252  C  CG  . ASP B 1 253 ? 7.371   2.845   20.452  1.00 20.00 ? 253 ASP B CG  1 
ATOM   4253  O  OD1 . ASP B 1 253 ? 7.159   1.676   20.055  1.00 20.00 ? 253 ASP B OD1 1 
ATOM   4254  O  OD2 . ASP B 1 253 ? 8.490   3.390   20.364  1.00 20.00 ? 253 ASP B OD2 1 
ATOM   4255  N  N   . GLU B 1 254 ? 4.238   1.462   23.151  1.00 30.00 ? 254 GLU B N   1 
ATOM   4256  C  CA  . GLU B 1 254 ? 3.631   1.093   24.415  1.00 30.00 ? 254 GLU B CA  1 
ATOM   4257  C  C   . GLU B 1 254 ? 2.171   0.660   24.375  1.00 30.00 ? 254 GLU B C   1 
ATOM   4258  O  O   . GLU B 1 254 ? 1.676   0.104   25.327  1.00 30.00 ? 254 GLU B O   1 
ATOM   4259  C  CB  . GLU B 1 254 ? 3.810   2.169   25.461  1.00 20.00 ? 254 GLU B CB  1 
ATOM   4260  C  CG  . GLU B 1 254 ? 4.320   1.530   26.709  1.00 20.00 ? 254 GLU B CG  1 
ATOM   4261  C  CD  . GLU B 1 254 ? 5.492   2.243   27.263  1.00 20.00 ? 254 GLU B CD  1 
ATOM   4262  O  OE1 . GLU B 1 254 ? 5.920   3.178   26.591  1.00 20.00 ? 254 GLU B OE1 1 
ATOM   4263  O  OE2 . GLU B 1 254 ? 5.948   1.890   28.361  1.00 20.00 ? 254 GLU B OE2 1 
ATOM   4264  N  N   . ARG B 1 255 ? 1.535   0.864   23.244  1.00 26.23 ? 255 ARG B N   1 
ATOM   4265  C  CA  . ARG B 1 255 ? 0.210   0.386   23.054  1.00 22.17 ? 255 ARG B CA  1 
ATOM   4266  C  C   . ARG B 1 255 ? 0.119   -1.268  23.104  1.00 22.90 ? 255 ARG B C   1 
ATOM   4267  O  O   . ARG B 1 255 ? 0.979   -1.980  22.668  1.00 22.50 ? 255 ARG B O   1 
ATOM   4268  C  CB  . ARG B 1 255 ? -0.301  1.003   21.735  1.00 22.56 ? 255 ARG B CB  1 
ATOM   4269  C  CG  . ARG B 1 255 ? 0.032   2.517   21.716  1.00 24.94 ? 255 ARG B CG  1 
ATOM   4270  C  CD  . ARG B 1 255 ? 0.587   2.952   20.356  1.00 28.06 ? 255 ARG B CD  1 
ATOM   4271  N  NE  . ARG B 1 255 ? -0.513  3.058   19.406  1.00 23.08 ? 255 ARG B NE  1 
ATOM   4272  C  CZ  . ARG B 1 255 ? -0.432  3.183   18.076  1.00 25.83 ? 255 ARG B CZ  1 
ATOM   4273  N  NH1 . ARG B 1 255 ? 0.741   3.254   17.452  1.00 15.25 ? 255 ARG B NH1 1 
ATOM   4274  N  NH2 . ARG B 1 255 ? -1.556  3.251   17.359  1.00 15.11 ? 255 ARG B NH2 1 
ATOM   4275  N  N   . LEU B 1 256 ? -0.976  -1.805  23.660  1.00 18.62 ? 256 LEU B N   1 
ATOM   4276  C  CA  . LEU B 1 256 ? -1.456  -3.139  23.401  1.00 17.64 ? 256 LEU B CA  1 
ATOM   4277  C  C   . LEU B 1 256 ? -2.684  -3.149  22.389  1.00 16.55 ? 256 LEU B C   1 
ATOM   4278  O  O   . LEU B 1 256 ? -3.369  -2.194  22.281  1.00 16.60 ? 256 LEU B O   1 
ATOM   4279  C  CB  . LEU B 1 256 ? -1.874  -3.825  24.679  1.00 22.07 ? 256 LEU B CB  1 
ATOM   4280  C  CG  . LEU B 1 256 ? -0.894  -3.995  25.798  1.00 24.86 ? 256 LEU B CG  1 
ATOM   4281  C  CD1 . LEU B 1 256 ? -1.550  -4.992  26.734  1.00 30.32 ? 256 LEU B CD1 1 
ATOM   4282  C  CD2 . LEU B 1 256 ? 0.430   -4.457  25.208  1.00 26.36 ? 256 LEU B CD2 1 
ATOM   4283  N  N   . VAL B 1 257 ? -2.832  -4.254  21.672  1.00 13.79 ? 257 VAL B N   1 
ATOM   4284  C  CA  . VAL B 1 257 ? -3.959  -4.529  20.856  1.00 12.55 ? 257 VAL B CA  1 
ATOM   4285  C  C   . VAL B 1 257 ? -4.764  -5.579  21.599  1.00 12.25 ? 257 VAL B C   1 
ATOM   4286  O  O   . VAL B 1 257 ? -4.271  -6.690  21.988  1.00 12.98 ? 257 VAL B O   1 
ATOM   4287  C  CB  . VAL B 1 257 ? -3.575  -5.090  19.533  1.00 10.50 ? 257 VAL B CB  1 
ATOM   4288  C  CG1 . VAL B 1 257 ? -4.749  -5.503  18.696  1.00 10.16 ? 257 VAL B CG1 1 
ATOM   4289  C  CG2 . VAL B 1 257 ? -2.800  -3.977  18.723  1.00 11.22 ? 257 VAL B CG2 1 
ATOM   4290  N  N   . TYR B 1 258 ? -6.068  -5.322  21.744  1.00 9.45  ? 258 TYR B N   1 
ATOM   4291  C  CA  . TYR B 1 258 ? -6.962  -6.238  22.474  1.00 11.38 ? 258 TYR B CA  1 
ATOM   4292  C  C   . TYR B 1 258 ? -7.755  -7.081  21.551  1.00 10.34 ? 258 TYR B C   1 
ATOM   4293  O  O   . TYR B 1 258 ? -8.141  -6.689  20.442  1.00 11.07 ? 258 TYR B O   1 
ATOM   4294  C  CB  . TYR B 1 258 ? -7.925  -5.363  23.328  1.00 13.58 ? 258 TYR B CB  1 
ATOM   4295  C  CG  . TYR B 1 258 ? -7.112  -4.458  24.285  1.00 14.93 ? 258 TYR B CG  1 
ATOM   4296  C  CD1 . TYR B 1 258 ? -6.536  -5.002  25.492  1.00 18.67 ? 258 TYR B CD1 1 
ATOM   4297  C  CD2 . TYR B 1 258 ? -6.728  -3.130  23.917  1.00 16.13 ? 258 TYR B CD2 1 
ATOM   4298  C  CE1 . TYR B 1 258 ? -5.752  -4.234  26.313  1.00 19.12 ? 258 TYR B CE1 1 
ATOM   4299  C  CE2 . TYR B 1 258 ? -5.902  -2.375  24.738  1.00 20.48 ? 258 TYR B CE2 1 
ATOM   4300  C  CZ  . TYR B 1 258 ? -5.416  -2.924  25.906  1.00 18.91 ? 258 TYR B CZ  1 
ATOM   4301  O  OH  . TYR B 1 258 ? -4.615  -2.056  26.671  1.00 21.24 ? 258 TYR B OH  1 
ATOM   4302  N  N   . THR B 1 259 ? -7.853  -8.387  21.818  1.00 9.85  ? 259 THR B N   1 
ATOM   4303  C  CA  . THR B 1 259 ? -8.508  -9.293  20.936  1.00 10.76 ? 259 THR B CA  1 
ATOM   4304  C  C   . THR B 1 259 ? -9.813  -9.834  21.556  1.00 11.29 ? 259 THR B C   1 
ATOM   4305  O  O   . THR B 1 259 ? -9.877  -10.052 22.808  1.00 11.20 ? 259 THR B O   1 
ATOM   4306  C  CB  . THR B 1 259 ? -7.649  -10.433 20.550  1.00 11.38 ? 259 THR B CB  1 
ATOM   4307  O  OG1 . THR B 1 259 ? -7.170  -11.175 21.744  1.00 12.57 ? 259 THR B OG1 1 
ATOM   4308  C  CG2 . THR B 1 259 ? -6.366  -9.926  19.806  1.00 11.91 ? 259 THR B CG2 1 
ATOM   4309  N  N   . SER B 1 260 ? -10.830 -10.009 20.762  1.00 8.33  ? 260 SER B N   1 
ATOM   4310  C  CA  . SER B 1 260 ? -12.110 -10.570 21.278  1.00 9.27  ? 260 SER B CA  1 
ATOM   4311  C  C   . SER B 1 260 ? -12.060 -12.104 21.232  1.00 10.78 ? 260 SER B C   1 
ATOM   4312  O  O   . SER B 1 260 ? -13.063 -12.726 21.666  1.00 13.86 ? 260 SER B O   1 
ATOM   4313  C  CB  . SER B 1 260 ? -13.254 -10.096 20.359  1.00 10.80 ? 260 SER B CB  1 
ATOM   4314  O  OG  . SER B 1 260 ? -13.136 -10.672 19.090  1.00 9.43  ? 260 SER B OG  1 
ATOM   4315  N  N   . PHE B 1 261 ? -10.940 -12.713 20.779  1.00 11.56 ? 261 PHE B N   1 
ATOM   4316  C  CA  . PHE B 1 261 ? -10.755 -14.151 20.691  1.00 11.89 ? 261 PHE B CA  1 
ATOM   4317  C  C   . PHE B 1 261 ? -9.522  -14.471 21.545  1.00 14.53 ? 261 PHE B C   1 
ATOM   4318  O  O   . PHE B 1 261 ? -8.576  -13.707 21.669  1.00 12.37 ? 261 PHE B O   1 
ATOM   4319  C  CB  . PHE B 1 261 ? -10.575 -14.593 19.198  1.00 11.13 ? 261 PHE B CB  1 
ATOM   4320  C  CG  . PHE B 1 261 ? -9.527  -13.859 18.445  1.00 11.71 ? 261 PHE B CG  1 
ATOM   4321  C  CD1 . PHE B 1 261 ? -8.207  -14.312 18.416  1.00 14.77 ? 261 PHE B CD1 1 
ATOM   4322  C  CD2 . PHE B 1 261 ? -9.822  -12.600 17.858  1.00 12.11 ? 261 PHE B CD2 1 
ATOM   4323  C  CE1 . PHE B 1 261 ? -7.255  -13.662 17.730  1.00 14.56 ? 261 PHE B CE1 1 
ATOM   4324  C  CE2 . PHE B 1 261 ? -8.864  -11.970 17.206  1.00 13.91 ? 261 PHE B CE2 1 
ATOM   4325  C  CZ  . PHE B 1 261 ? -7.566  -12.413 17.137  1.00 13.88 ? 261 PHE B CZ  1 
ATOM   4326  N  N   . SER B 1 262 ? -9.569  -15.630 22.204  1.00 17.76 ? 262 SER B N   1 
ATOM   4327  C  CA  . SER B 1 262 ? -8.475  -15.844 23.135  1.00 23.62 ? 262 SER B CA  1 
ATOM   4328  C  C   . SER B 1 262 ? -7.314  -16.421 22.363  1.00 26.50 ? 262 SER B C   1 
ATOM   4329  O  O   . SER B 1 262 ? -6.137  -15.924 22.530  1.00 28.77 ? 262 SER B O   1 
ATOM   4330  C  CB  . SER B 1 262 ? -8.835  -16.646 24.414  1.00 25.48 ? 262 SER B CB  1 
ATOM   4331  O  OG  . SER B 1 262 ? -9.796  -17.668 24.142  1.00 30.78 ? 262 SER B OG  1 
ATOM   4332  N  N   . GLN B 1 263 ? -7.704  -17.427 21.551  1.00 28.49 ? 263 GLN B N   1 
ATOM   4333  C  CA  . GLN B 1 263 ? -6.875  -18.324 20.731  1.00 28.39 ? 263 GLN B CA  1 
ATOM   4334  C  C   . GLN B 1 263 ? -7.547  -18.453 19.372  1.00 26.62 ? 263 GLN B C   1 
ATOM   4335  O  O   . GLN B 1 263 ? -6.952  -19.025 18.424  1.00 27.55 ? 263 GLN B O   1 
ATOM   4336  C  CB  . GLN B 1 263 ? -6.746  -19.777 21.350  1.00 28.80 ? 263 GLN B CB  1 
ATOM   4337  C  CG  . GLN B 1 263 ? -8.012  -20.365 21.893  1.00 35.33 ? 263 GLN B CG  1 
ATOM   4338  C  CD  . GLN B 1 263 ? -7.798  -21.038 23.257  1.00 41.02 ? 263 GLN B CD  1 
ATOM   4339  O  OE1 . GLN B 1 263 ? -7.804  -22.267 23.354  1.00 40.31 ? 263 GLN B OE1 1 
ATOM   4340  N  NE2 . GLN B 1 263 ? -7.635  -20.219 24.324  1.00 48.13 ? 263 GLN B NE2 1 
ATOM   4341  O  OXT . GLN B 1 263 ? -8.708  -18.079 19.216  1.00 23.49 ? 263 GLN B OXT 1 
ATOM   4342  N  N   A LYS C 1 3   ? 33.603  17.253  -24.325 0.50 30.25 ? 3   LYS C N   1 
ATOM   4343  N  N   B LYS C 1 3   ? 33.931  17.650  -25.410 0.50 25.97 ? 3   LYS C N   1 
ATOM   4344  C  CA  A LYS C 1 3   ? 32.685  17.979  -25.297 0.50 28.98 ? 3   LYS C CA  1 
ATOM   4345  C  CA  B LYS C 1 3   ? 32.876  17.280  -24.412 0.50 26.91 ? 3   LYS C CA  1 
ATOM   4346  C  C   A LYS C 1 3   ? 31.873  17.069  -26.236 0.50 28.50 ? 3   LYS C C   1 
ATOM   4347  C  C   B LYS C 1 3   ? 31.829  16.399  -25.084 0.50 25.74 ? 3   LYS C C   1 
ATOM   4348  O  O   A LYS C 1 3   ? 30.965  17.507  -26.959 0.50 28.15 ? 3   LYS C O   1 
ATOM   4349  O  O   B LYS C 1 3   ? 30.692  16.274  -24.609 0.50 26.72 ? 3   LYS C O   1 
ATOM   4350  C  CB  A LYS C 1 3   ? 33.453  19.027  -26.103 0.50 30.55 ? 3   LYS C CB  1 
ATOM   4351  C  CB  B LYS C 1 3   ? 32.222  18.514  -23.852 0.50 26.65 ? 3   LYS C CB  1 
ATOM   4352  C  CG  A LYS C 1 3   ? 34.782  18.563  -26.651 0.50 31.13 ? 3   LYS C CG  1 
ATOM   4353  C  CG  B LYS C 1 3   ? 30.880  18.871  -24.482 0.50 26.06 ? 3   LYS C CG  1 
ATOM   4354  C  CD  A LYS C 1 3   ? 35.666  19.764  -26.895 0.50 30.67 ? 3   LYS C CD  1 
ATOM   4355  C  CD  B LYS C 1 3   ? 30.552  20.334  -24.201 0.50 29.74 ? 3   LYS C CD  1 
ATOM   4356  C  CE  A LYS C 1 3   ? 36.542  20.086  -25.671 0.50 32.75 ? 3   LYS C CE  1 
ATOM   4357  C  CE  B LYS C 1 3   ? 31.200  20.810  -22.889 0.50 31.24 ? 3   LYS C CE  1 
ATOM   4358  N  NZ  A LYS C 1 3   ? 35.789  20.723  -24.557 0.50 32.75 ? 3   LYS C NZ  1 
ATOM   4359  N  NZ  B LYS C 1 3   ? 30.505  20.296  -21.672 0.50 32.98 ? 3   LYS C NZ  1 
ATOM   4360  N  N   . TRP C 1 4   ? 32.205  15.794  -26.214 1.00 25.53 ? 4   TRP C N   1 
ATOM   4361  C  CA  . TRP C 1 4   ? 31.310  14.797  -26.777 1.00 22.34 ? 4   TRP C CA  1 
ATOM   4362  C  C   . TRP C 1 4   ? 31.156  13.613  -25.797 1.00 21.65 ? 4   TRP C C   1 
ATOM   4363  O  O   . TRP C 1 4   ? 32.080  13.242  -25.011 1.00 20.99 ? 4   TRP C O   1 
ATOM   4364  C  CB  . TRP C 1 4   ? 31.714  14.416  -28.240 1.00 19.31 ? 4   TRP C CB  1 
ATOM   4365  C  CG  . TRP C 1 4   ? 33.014  13.728  -28.335 1.00 17.75 ? 4   TRP C CG  1 
ATOM   4366  C  CD1 . TRP C 1 4   ? 34.246  14.303  -28.544 1.00 15.11 ? 4   TRP C CD1 1 
ATOM   4367  C  CD2 . TRP C 1 4   ? 33.260  12.346  -28.104 1.00 12.54 ? 4   TRP C CD2 1 
ATOM   4368  N  NE1 . TRP C 1 4   ? 35.228  13.358  -28.491 1.00 16.70 ? 4   TRP C NE1 1 
ATOM   4369  C  CE2 . TRP C 1 4   ? 34.677  12.106  -28.285 1.00 17.07 ? 4   TRP C CE2 1 
ATOM   4370  C  CE3 . TRP C 1 4   ? 32.420  11.231  -27.902 1.00 13.95 ? 4   TRP C CE3 1 
ATOM   4371  C  CZ2 . TRP C 1 4   ? 35.266  10.804  -28.190 1.00 17.14 ? 4   TRP C CZ2 1 
ATOM   4372  C  CZ3 . TRP C 1 4   ? 32.984  9.967   -27.813 1.00 13.96 ? 4   TRP C CZ3 1 
ATOM   4373  C  CH2 . TRP C 1 4   ? 34.409  9.737   -27.967 1.00 14.40 ? 4   TRP C CH2 1 
ATOM   4374  N  N   . THR C 1 5   ? 30.001  12.968  -25.869 1.00 22.06 ? 5   THR C N   1 
ATOM   4375  C  CA  . THR C 1 5   ? 29.758  11.839  -25.026 1.00 22.01 ? 5   THR C CA  1 
ATOM   4376  C  C   . THR C 1 5   ? 28.990  10.720  -25.760 1.00 21.76 ? 5   THR C C   1 
ATOM   4377  O  O   . THR C 1 5   ? 28.632  10.841  -26.962 1.00 18.78 ? 5   THR C O   1 
ATOM   4378  C  CB  . THR C 1 5   ? 28.851  12.213  -23.784 1.00 24.62 ? 5   THR C CB  1 
ATOM   4379  O  OG1 . THR C 1 5   ? 27.531  12.540  -24.269 1.00 25.62 ? 5   THR C OG1 1 
ATOM   4380  C  CG2 . THR C 1 5   ? 29.430  13.463  -23.041 1.00 24.46 ? 5   THR C CG2 1 
ATOM   4381  N  N   . TYR C 1 6   ? 28.666  9.653   -25.046 1.00 23.50 ? 6   TYR C N   1 
ATOM   4382  C  CA  . TYR C 1 6   ? 27.723  8.621   -25.576 1.00 25.26 ? 6   TYR C CA  1 
ATOM   4383  C  C   . TYR C 1 6   ? 26.269  8.732   -25.039 1.00 27.46 ? 6   TYR C C   1 
ATOM   4384  O  O   . TYR C 1 6   ? 25.503  7.755   -25.127 1.00 27.87 ? 6   TYR C O   1 
ATOM   4385  C  CB  . TYR C 1 6   ? 28.231  7.216   -25.351 1.00 20.66 ? 6   TYR C CB  1 
ATOM   4386  C  CG  . TYR C 1 6   ? 29.526  6.925   -26.098 1.00 21.54 ? 6   TYR C CG  1 
ATOM   4387  C  CD1 . TYR C 1 6   ? 30.767  7.161   -25.513 1.00 19.88 ? 6   TYR C CD1 1 
ATOM   4388  C  CD2 . TYR C 1 6   ? 29.498  6.409   -27.394 1.00 17.58 ? 6   TYR C CD2 1 
ATOM   4389  C  CE1 . TYR C 1 6   ? 31.943  6.887   -26.201 1.00 19.32 ? 6   TYR C CE1 1 
ATOM   4390  C  CE2 . TYR C 1 6   ? 30.664  6.135   -28.081 1.00 19.91 ? 6   TYR C CE2 1 
ATOM   4391  C  CZ  . TYR C 1 6   ? 31.882  6.373   -27.486 1.00 17.07 ? 6   TYR C CZ  1 
ATOM   4392  O  OH  . TYR C 1 6   ? 33.018  6.088   -28.206 1.00 18.26 ? 6   TYR C OH  1 
ATOM   4393  N  N   . PHE C 1 7   ? 25.869  9.887   -24.481 1.00 31.43 ? 7   PHE C N   1 
ATOM   4394  C  CA  . PHE C 1 7   ? 24.455  10.042  -23.963 1.00 35.01 ? 7   PHE C CA  1 
ATOM   4395  C  C   . PHE C 1 7   ? 23.852  11.487  -24.024 1.00 35.97 ? 7   PHE C C   1 
ATOM   4396  O  O   . PHE C 1 7   ? 24.334  12.352  -24.795 1.00 35.58 ? 7   PHE C O   1 
ATOM   4397  C  CB  . PHE C 1 7   ? 24.403  9.598   -22.524 1.00 37.83 ? 7   PHE C CB  1 
ATOM   4398  C  CG  . PHE C 1 7   ? 25.124  10.539  -21.639 1.00 38.92 ? 7   PHE C CG  1 
ATOM   4399  C  CD1 . PHE C 1 7   ? 24.544  11.781  -21.315 1.00 42.16 ? 7   PHE C CD1 1 
ATOM   4400  C  CD2 . PHE C 1 7   ? 26.413  10.236  -21.173 1.00 41.59 ? 7   PHE C CD2 1 
ATOM   4401  C  CE1 . PHE C 1 7   ? 25.227  12.708  -20.514 1.00 41.02 ? 7   PHE C CE1 1 
ATOM   4402  C  CE2 . PHE C 1 7   ? 27.106  11.143  -20.375 1.00 39.42 ? 7   PHE C CE2 1 
ATOM   4403  C  CZ  . PHE C 1 7   ? 26.522  12.385  -20.061 1.00 40.14 ? 7   PHE C CZ  1 
ATOM   4404  N  N   . GLY C 1 8   ? 22.841  11.767  -23.184 1.00 35.40 ? 8   GLY C N   1 
ATOM   4405  C  CA  . GLY C 1 8   ? 22.237  13.134  -23.025 1.00 34.65 ? 8   GLY C CA  1 
ATOM   4406  C  C   . GLY C 1 8   ? 22.161  13.924  -24.335 1.00 34.85 ? 8   GLY C C   1 
ATOM   4407  O  O   . GLY C 1 8   ? 21.917  13.318  -25.430 1.00 36.50 ? 8   GLY C O   1 
ATOM   4408  N  N   . PRO C 1 9   ? 22.387  15.242  -24.299 1.00 34.09 ? 9   PRO C N   1 
ATOM   4409  C  CA  . PRO C 1 9   ? 22.337  15.930  -25.592 1.00 32.67 ? 9   PRO C CA  1 
ATOM   4410  C  C   . PRO C 1 9   ? 23.663  16.007  -26.322 1.00 29.13 ? 9   PRO C C   1 
ATOM   4411  O  O   . PRO C 1 9   ? 23.686  16.652  -27.361 1.00 27.27 ? 9   PRO C O   1 
ATOM   4412  C  CB  . PRO C 1 9   ? 21.872  17.373  -25.233 1.00 33.95 ? 9   PRO C CB  1 
ATOM   4413  C  CG  . PRO C 1 9   ? 22.410  17.555  -23.756 1.00 34.33 ? 9   PRO C CG  1 
ATOM   4414  C  CD  . PRO C 1 9   ? 22.571  16.171  -23.148 1.00 33.39 ? 9   PRO C CD  1 
ATOM   4415  N  N   . ASP C 1 10  ? 24.759  15.483  -25.756 1.00 28.66 ? 10  ASP C N   1 
ATOM   4416  C  CA  . ASP C 1 10  ? 26.072  15.581  -26.451 1.00 26.95 ? 10  ASP C CA  1 
ATOM   4417  C  C   . ASP C 1 10  ? 26.499  14.255  -27.053 1.00 25.03 ? 10  ASP C C   1 
ATOM   4418  O  O   . ASP C 1 10  ? 27.690  14.114  -27.467 1.00 25.04 ? 10  ASP C O   1 
ATOM   4419  C  CB  . ASP C 1 10  ? 27.208  16.118  -25.559 1.00 27.88 ? 10  ASP C CB  1 
ATOM   4420  C  CG  . ASP C 1 10  ? 26.965  17.552  -25.141 1.00 33.20 ? 10  ASP C CG  1 
ATOM   4421  O  OD1 . ASP C 1 10  ? 26.636  18.406  -26.016 1.00 35.13 ? 10  ASP C OD1 1 
ATOM   4422  O  OD2 . ASP C 1 10  ? 27.071  17.793  -23.913 1.00 39.99 ? 10  ASP C OD2 1 
ATOM   4423  N  N   . GLY C 1 11  ? 25.540  13.305  -27.028 1.00 24.83 ? 11  GLY C N   1 
ATOM   4424  C  CA  . GLY C 1 11  ? 25.674  11.944  -27.601 1.00 17.17 ? 11  GLY C CA  1 
ATOM   4425  C  C   . GLY C 1 11  ? 25.734  11.885  -29.144 1.00 13.08 ? 11  GLY C C   1 
ATOM   4426  O  O   . GLY C 1 11  ? 25.738  12.883  -29.877 1.00 14.75 ? 11  GLY C O   1 
ATOM   4427  N  N   . GLU C 1 12  ? 25.762  10.575  -29.553 1.00 12.95 ? 12  GLU C N   1 
ATOM   4428  C  CA  . GLU C 1 12  ? 26.196  10.323  -30.945 1.00 12.73 ? 12  GLU C CA  1 
ATOM   4429  C  C   . GLU C 1 12  ? 25.311  10.989  -31.999 1.00 12.09 ? 12  GLU C C   1 
ATOM   4430  O  O   . GLU C 1 12  ? 25.820  11.334  -33.067 1.00 10.45 ? 12  GLU C O   1 
ATOM   4431  C  CB  . GLU C 1 12  ? 26.378  8.800   -31.194 1.00 11.83 ? 12  GLU C CB  1 
ATOM   4432  C  CG  . GLU C 1 12  ? 24.982  8.136   -31.335 1.00 11.18 ? 12  GLU C CG  1 
ATOM   4433  C  CD  . GLU C 1 12  ? 25.250  6.691   -31.100 1.00 10.03 ? 12  GLU C CD  1 
ATOM   4434  O  OE1 . GLU C 1 12  ? 25.547  5.886   -32.037 1.00 10.46 ? 12  GLU C OE1 1 
ATOM   4435  O  OE2 . GLU C 1 12  ? 25.286  6.210   -29.882 1.00 13.06 ? 12  GLU C OE2 1 
ATOM   4436  N  N   . ASN C 1 13  ? 24.015  11.178  -31.759 1.00 10.47 ? 13  ASN C N   1 
ATOM   4437  C  CA  . ASN C 1 13  ? 23.213  11.776  -32.745 1.00 10.50 ? 13  ASN C CA  1 
ATOM   4438  C  C   . ASN C 1 13  ? 23.531  13.288  -32.975 1.00 10.22 ? 13  ASN C C   1 
ATOM   4439  O  O   . ASN C 1 13  ? 23.171  13.859  -33.980 1.00 11.84 ? 13  ASN C O   1 
ATOM   4440  C  CB  . ASN C 1 13  ? 21.703  11.610  -32.460 1.00 10.13 ? 13  ASN C CB  1 
ATOM   4441  C  CG  . ASN C 1 13  ? 21.251  10.182  -32.559 1.00 11.66 ? 13  ASN C CG  1 
ATOM   4442  O  OD1 . ASN C 1 13  ? 21.924  9.293   -33.159 1.00 10.68 ? 13  ASN C OD1 1 
ATOM   4443  N  ND2 . ASN C 1 13  ? 20.032  9.987   -32.129 1.00 9.91  ? 13  ASN C ND2 1 
ATOM   4444  N  N   A SER C 1 14  ? 24.232  13.829  -31.950 0.50 11.11 ? 14  SER C N   1 
ATOM   4445  N  N   B SER C 1 14  ? 24.214  13.924  -32.004 0.50 11.90 ? 14  SER C N   1 
ATOM   4446  C  CA  A SER C 1 14  ? 24.591  15.263  -31.967 0.50 11.74 ? 14  SER C CA  1 
ATOM   4447  C  CA  B SER C 1 14  ? 24.583  15.367  -32.217 0.50 11.28 ? 14  SER C CA  1 
ATOM   4448  C  C   A SER C 1 14  ? 25.996  15.548  -32.489 0.50 11.94 ? 14  SER C C   1 
ATOM   4449  C  C   B SER C 1 14  ? 26.104  15.536  -32.406 0.50 12.12 ? 14  SER C C   1 
ATOM   4450  O  O   A SER C 1 14  ? 26.251  16.733  -32.894 0.50 8.19  ? 14  SER C O   1 
ATOM   4451  O  O   B SER C 1 14  ? 26.643  16.590  -32.384 0.50 11.54 ? 14  SER C O   1 
ATOM   4452  C  CB  A SER C 1 14  ? 24.385  15.868  -30.560 0.50 12.15 ? 14  SER C CB  1 
ATOM   4453  C  CB  B SER C 1 14  ? 24.228  16.175  -30.973 0.50 11.79 ? 14  SER C CB  1 
ATOM   4454  O  OG  A SER C 1 14  ? 23.001  15.989  -30.306 0.50 12.62 ? 14  SER C OG  1 
ATOM   4455  O  OG  B SER C 1 14  ? 25.023  15.688  -29.914 0.50 14.61 ? 14  SER C OG  1 
ATOM   4456  N  N   . TRP C 1 15  ? 26.807  14.460  -32.582 1.00 11.04 ? 15  TRP C N   1 
ATOM   4457  C  CA  . TRP C 1 15  ? 28.253  14.637  -32.932 1.00 11.39 ? 15  TRP C CA  1 
ATOM   4458  C  C   . TRP C 1 15  ? 28.404  15.471  -34.183 1.00 11.21 ? 15  TRP C C   1 
ATOM   4459  O  O   . TRP C 1 15  ? 29.422  16.237  -34.288 1.00 12.37 ? 15  TRP C O   1 
ATOM   4460  C  CB  . TRP C 1 15  ? 28.937  13.372  -33.189 1.00 10.74 ? 15  TRP C CB  1 
ATOM   4461  C  CG  . TRP C 1 15  ? 29.078  12.512  -31.959 1.00 8.69  ? 15  TRP C CG  1 
ATOM   4462  C  CD1 . TRP C 1 15  ? 28.845  12.861  -30.619 1.00 12.21 ? 15  TRP C CD1 1 
ATOM   4463  C  CD2 . TRP C 1 15  ? 29.552  11.155  -31.881 1.00 9.81  ? 15  TRP C CD2 1 
ATOM   4464  N  NE1 . TRP C 1 15  ? 29.115  11.830  -29.747 1.00 11.61 ? 15  TRP C NE1 1 
ATOM   4465  C  CE2 . TRP C 1 15  ? 29.545  10.727  -30.478 1.00 12.34 ? 15  TRP C CE2 1 
ATOM   4466  C  CE3 . TRP C 1 15  ? 29.951  10.236  -32.877 1.00 9.40  ? 15  TRP C CE3 1 
ATOM   4467  C  CZ2 . TRP C 1 15  ? 29.941  9.464   -30.080 1.00 11.28 ? 15  TRP C CZ2 1 
ATOM   4468  C  CZ3 . TRP C 1 15  ? 30.310  8.980   -32.504 1.00 8.35  ? 15  TRP C CZ3 1 
ATOM   4469  C  CH2 . TRP C 1 15  ? 30.377  8.577   -31.114 1.00 9.20  ? 15  TRP C CH2 1 
ATOM   4470  N  N   . SER C 1 16  ? 27.515  15.275  -35.184 1.00 10.97 ? 16  SER C N   1 
ATOM   4471  C  CA  . SER C 1 16  ? 27.708  15.943  -36.478 1.00 10.08 ? 16  SER C CA  1 
ATOM   4472  C  C   . SER C 1 16  ? 27.664  17.464  -36.385 1.00 11.30 ? 16  SER C C   1 
ATOM   4473  O  O   . SER C 1 16  ? 28.070  18.173  -37.338 1.00 12.41 ? 16  SER C O   1 
ATOM   4474  C  CB  . SER C 1 16  ? 26.699  15.521  -37.510 1.00 11.94 ? 16  SER C CB  1 
ATOM   4475  O  OG  . SER C 1 16  ? 25.384  15.831  -37.010 1.00 12.84 ? 16  SER C OG  1 
ATOM   4476  N  N   A LYS C 1 17  ? 27.188  17.929  -35.211 0.50 11.63 ? 17  LYS C N   1 
ATOM   4477  N  N   B LYS C 1 17  ? 27.090  18.006  -35.316 0.50 11.11 ? 17  LYS C N   1 
ATOM   4478  C  CA  A LYS C 1 17  ? 27.052  19.415  -34.998 0.50 13.46 ? 17  LYS C CA  1 
ATOM   4479  C  CA  B LYS C 1 17  ? 27.060  19.537  -35.279 0.50 10.66 ? 17  LYS C CA  1 
ATOM   4480  C  C   A LYS C 1 17  ? 28.429  20.079  -35.065 0.50 12.96 ? 17  LYS C C   1 
ATOM   4481  C  C   B LYS C 1 17  ? 28.558  20.072  -35.218 0.50 11.17 ? 17  LYS C C   1 
ATOM   4482  O  O   A LYS C 1 17  ? 28.598  21.074  -35.758 0.50 14.80 ? 17  LYS C O   1 
ATOM   4483  O  O   B LYS C 1 17  ? 28.975  20.922  -36.062 0.50 13.09 ? 17  LYS C O   1 
ATOM   4484  C  CB  A LYS C 1 17  ? 26.389  19.701  -33.659 0.50 12.54 ? 17  LYS C CB  1 
ATOM   4485  C  CB  B LYS C 1 17  ? 26.118  20.019  -34.133 0.50 7.74  ? 17  LYS C CB  1 
ATOM   4486  C  CG  A LYS C 1 17  ? 24.890  19.389  -33.585 0.50 16.17 ? 17  LYS C CG  1 
ATOM   4487  C  CG  B LYS C 1 17  ? 24.626  19.736  -34.366 0.50 12.02 ? 17  LYS C CG  1 
ATOM   4488  C  CD  A LYS C 1 17  ? 24.333  19.604  -32.178 0.50 13.96 ? 17  LYS C CD  1 
ATOM   4489  C  CD  B LYS C 1 17  ? 23.809  20.088  -33.118 0.50 11.54 ? 17  LYS C CD  1 
ATOM   4490  C  CE  A LYS C 1 17  ? 22.849  19.243  -32.047 0.50 14.18 ? 17  LYS C CE  1 
ATOM   4491  C  CE  B LYS C 1 17  ? 23.788  21.636  -32.955 0.50 14.03 ? 17  LYS C CE  1 
ATOM   4492  N  NZ  A LYS C 1 17  ? 22.374  19.237  -30.663 0.50 16.95 ? 17  LYS C NZ  1 
ATOM   4493  N  NZ  B LYS C 1 17  ? 23.159  21.807  -31.578 0.50 15.90 ? 17  LYS C NZ  1 
ATOM   4494  N  N   . LYS C 1 18  ? 29.349  19.532  -34.312 1.00 12.20 ? 18  LYS C N   1 
ATOM   4495  C  CA  . LYS C 1 18  ? 30.749  19.974  -34.206 1.00 14.35 ? 18  LYS C CA  1 
ATOM   4496  C  C   . LYS C 1 18  ? 31.694  19.212  -35.033 1.00 17.33 ? 18  LYS C C   1 
ATOM   4497  O  O   . LYS C 1 18  ? 32.833  19.698  -35.235 1.00 18.74 ? 18  LYS C O   1 
ATOM   4498  C  CB  . LYS C 1 18  ? 31.164  19.886  -32.746 1.00 17.20 ? 18  LYS C CB  1 
ATOM   4499  C  CG  . LYS C 1 18  ? 30.463  20.931  -31.822 1.00 24.11 ? 18  LYS C CG  1 
ATOM   4500  C  CD  . LYS C 1 18  ? 31.119  22.339  -31.714 1.00 30.92 ? 18  LYS C CD  1 
ATOM   4501  C  CE  . LYS C 1 18  ? 30.092  23.374  -31.223 1.00 30.64 ? 18  LYS C CE  1 
ATOM   4502  N  NZ  . LYS C 1 18  ? 28.792  23.123  -32.058 1.00 30.92 ? 18  LYS C NZ  1 
ATOM   4503  N  N   . TYR C 1 19  ? 31.334  17.989  -35.479 1.00 13.67 ? 19  TYR C N   1 
ATOM   4504  C  CA  . TYR C 1 19  ? 32.254  17.158  -36.212 1.00 12.49 ? 19  TYR C CA  1 
ATOM   4505  C  C   . TYR C 1 19  ? 31.525  16.737  -37.511 1.00 11.82 ? 19  TYR C C   1 
ATOM   4506  O  O   . TYR C 1 19  ? 30.895  15.634  -37.527 1.00 13.02 ? 19  TYR C O   1 
ATOM   4507  C  CB  . TYR C 1 19  ? 32.565  15.931  -35.372 1.00 12.27 ? 19  TYR C CB  1 
ATOM   4508  C  CG  . TYR C 1 19  ? 33.199  16.327  -34.030 1.00 15.20 ? 19  TYR C CG  1 
ATOM   4509  C  CD1 . TYR C 1 19  ? 34.578  16.680  -33.969 1.00 14.39 ? 19  TYR C CD1 1 
ATOM   4510  C  CD2 . TYR C 1 19  ? 32.426  16.339  -32.881 1.00 12.27 ? 19  TYR C CD2 1 
ATOM   4511  C  CE1 . TYR C 1 19  ? 35.202  17.027  -32.706 1.00 15.46 ? 19  TYR C CE1 1 
ATOM   4512  C  CE2 . TYR C 1 19  ? 33.052  16.682  -31.621 1.00 14.65 ? 19  TYR C CE2 1 
ATOM   4513  C  CZ  . TYR C 1 19  ? 34.403  17.057  -31.587 1.00 15.68 ? 19  TYR C CZ  1 
ATOM   4514  O  OH  . TYR C 1 19  ? 35.007  17.340  -30.354 1.00 22.64 ? 19  TYR C OH  1 
ATOM   4515  N  N   . PRO C 1 20  ? 31.556  17.548  -38.547 1.00 12.29 ? 20  PRO C N   1 
ATOM   4516  C  CA  . PRO C 1 20  ? 30.677  17.305  -39.656 1.00 13.26 ? 20  PRO C CA  1 
ATOM   4517  C  C   . PRO C 1 20  ? 30.880  15.874  -40.277 1.00 11.94 ? 20  PRO C C   1 
ATOM   4518  O  O   . PRO C 1 20  ? 29.957  15.357  -40.935 1.00 11.74 ? 20  PRO C O   1 
ATOM   4519  C  CB  . PRO C 1 20  ? 30.969  18.427  -40.702 1.00 12.91 ? 20  PRO C CB  1 
ATOM   4520  C  CG  . PRO C 1 20  ? 31.754  19.444  -39.854 1.00 17.09 ? 20  PRO C CG  1 
ATOM   4521  C  CD  . PRO C 1 20  ? 32.370  18.779  -38.718 1.00 12.31 ? 20  PRO C CD  1 
ATOM   4522  N  N   . SER C 1 21  ? 32.080  15.311  -40.213 1.00 10.67 ? 21  SER C N   1 
ATOM   4523  C  CA  . SER C 1 21  ? 32.307  13.975  -40.809 1.00 10.42 ? 21  SER C CA  1 
ATOM   4524  C  C   . SER C 1 21  ? 31.467  12.938  -40.150 1.00 10.69 ? 21  SER C C   1 
ATOM   4525  O  O   . SER C 1 21  ? 31.168  11.908  -40.839 1.00 11.26 ? 21  SER C O   1 
ATOM   4526  C  CB  . SER C 1 21  ? 33.810  13.659  -40.715 1.00 11.06 ? 21  SER C CB  1 
ATOM   4527  O  OG  . SER C 1 21  ? 34.507  14.450  -41.695 1.00 13.10 ? 21  SER C OG  1 
ATOM   4528  N  N   . CYS C 1 22  ? 30.947  13.190  -38.969 1.00 10.29 ? 22  CYS C N   1 
ATOM   4529  C  CA  . CYS C 1 22  ? 30.081  12.168  -38.339 1.00 11.56 ? 22  CYS C CA  1 
ATOM   4530  C  C   . CYS C 1 22  ? 28.746  11.970  -39.069 1.00 10.80 ? 22  CYS C C   1 
ATOM   4531  O  O   . CYS C 1 22  ? 28.062  10.960  -38.762 1.00 11.53 ? 22  CYS C O   1 
ATOM   4532  C  CB  . CYS C 1 22  ? 29.908  12.466  -36.862 1.00 10.37 ? 22  CYS C CB  1 
ATOM   4533  S  SG  . CYS C 1 22  ? 31.414  12.556  -35.888 1.00 11.53 ? 22  CYS C SG  1 
ATOM   4534  N  N   . GLY C 1 23  ? 28.365  12.939  -39.890 1.00 11.66 ? 23  GLY C N   1 
ATOM   4535  C  CA  . GLY C 1 23  ? 27.194  12.821  -40.738 1.00 11.34 ? 23  GLY C CA  1 
ATOM   4536  C  C   . GLY C 1 23  ? 27.504  12.587  -42.203 1.00 9.81  ? 23  GLY C C   1 
ATOM   4537  O  O   . GLY C 1 23  ? 26.605  12.718  -43.024 1.00 10.91 ? 23  GLY C O   1 
ATOM   4538  N  N   . GLY C 1 24  ? 28.777  12.235  -42.514 1.00 10.38 ? 24  GLY C N   1 
ATOM   4539  C  CA  . GLY C 1 24  ? 29.201  12.059  -43.884 1.00 11.92 ? 24  GLY C CA  1 
ATOM   4540  C  C   . GLY C 1 24  ? 29.315  10.618  -44.345 1.00 12.39 ? 24  GLY C C   1 
ATOM   4541  O  O   . GLY C 1 24  ? 28.617  9.748   -43.790 1.00 13.02 ? 24  GLY C O   1 
ATOM   4542  N  N   . LEU C 1 25  ? 30.140  10.398  -45.364 1.00 12.12 ? 25  LEU C N   1 
ATOM   4543  C  CA  . LEU C 1 25  ? 30.253  9.051   -45.996 1.00 12.65 ? 25  LEU C CA  1 
ATOM   4544  C  C   . LEU C 1 25  ? 31.109  8.153   -45.119 1.00 13.67 ? 25  LEU C C   1 
ATOM   4545  O  O   . LEU C 1 25  ? 31.922  8.583   -44.251 1.00 11.36 ? 25  LEU C O   1 
ATOM   4546  C  CB  . LEU C 1 25  ? 30.909  9.202   -47.394 1.00 14.45 ? 25  LEU C CB  1 
ATOM   4547  C  CG  . LEU C 1 25  ? 30.161  10.182  -48.320 1.00 17.82 ? 25  LEU C CG  1 
ATOM   4548  C  CD1 . LEU C 1 25  ? 30.896  10.349  -49.645 1.00 20.37 ? 25  LEU C CD1 1 
ATOM   4549  C  CD2 . LEU C 1 25  ? 28.804  9.559   -48.624 1.00 24.60 ? 25  LEU C CD2 1 
ATOM   4550  N  N   . LEU C 1 26  ? 31.012  6.847   -45.410 1.00 11.45 ? 26  LEU C N   1 
ATOM   4551  C  CA  . LEU C 1 26  ? 31.982  5.801   -44.979 1.00 13.09 ? 26  LEU C CA  1 
ATOM   4552  C  C   . LEU C 1 26  ? 32.018  5.640   -43.463 1.00 10.83 ? 26  LEU C C   1 
ATOM   4553  O  O   . LEU C 1 26  ? 33.047  5.213   -42.902 1.00 12.22 ? 26  LEU C O   1 
ATOM   4554  C  CB  . LEU C 1 26  ? 33.460  5.995   -45.470 1.00 12.06 ? 26  LEU C CB  1 
ATOM   4555  C  CG  . LEU C 1 26  ? 33.806  5.960   -46.974 1.00 21.80 ? 26  LEU C CG  1 
ATOM   4556  C  CD1 . LEU C 1 26  ? 35.339  5.844   -47.260 1.00 21.01 ? 26  LEU C CD1 1 
ATOM   4557  C  CD2 . LEU C 1 26  ? 33.026  4.936   -47.756 1.00 19.69 ? 26  LEU C CD2 1 
ATOM   4558  N  N   . GLN C 1 27  ? 30.838  5.819   -42.819 1.00 8.57  ? 27  GLN C N   1 
ATOM   4559  C  CA  . GLN C 1 27  ? 30.818  5.720   -41.343 1.00 8.97  ? 27  GLN C CA  1 
ATOM   4560  C  C   . GLN C 1 27  ? 30.874  4.321   -40.777 1.00 11.09 ? 27  GLN C C   1 
ATOM   4561  O  O   . GLN C 1 27  ? 30.300  3.366   -41.343 1.00 11.94 ? 27  GLN C O   1 
ATOM   4562  C  CB  . GLN C 1 27  ? 29.655  6.479   -40.764 1.00 8.43  ? 27  GLN C CB  1 
ATOM   4563  C  CG  . GLN C 1 27  ? 29.718  8.018   -41.075 1.00 8.43  ? 27  GLN C CG  1 
ATOM   4564  C  CD  . GLN C 1 27  ? 30.867  8.696   -40.407 1.00 8.34  ? 27  GLN C CD  1 
ATOM   4565  O  OE1 . GLN C 1 27  ? 30.821  8.855   -39.165 1.00 9.01  ? 27  GLN C OE1 1 
ATOM   4566  N  NE2 . GLN C 1 27  ? 31.975  8.959   -41.161 1.00 9.06  ? 27  GLN C NE2 1 
ATOM   4567  N  N   . SER C 1 28  ? 31.638  4.139   -39.707 1.00 7.78  ? 28  SER C N   1 
ATOM   4568  C  CA  . SER C 1 28  ? 31.696  2.921   -38.943 1.00 7.51  ? 28  SER C CA  1 
ATOM   4569  C  C   . SER C 1 28  ? 31.127  3.140   -37.544 1.00 7.55  ? 28  SER C C   1 
ATOM   4570  O  O   . SER C 1 28  ? 31.010  4.283   -37.106 1.00 8.78  ? 28  SER C O   1 
ATOM   4571  C  CB  . SER C 1 28  ? 33.226  2.630   -38.728 1.00 7.41  ? 28  SER C CB  1 
ATOM   4572  O  OG  . SER C 1 28  ? 33.803  2.332   -40.027 1.00 8.39  ? 28  SER C OG  1 
ATOM   4573  N  N   . PRO C 1 29  ? 30.762  2.110   -36.824 1.00 7.16  ? 29  PRO C N   1 
ATOM   4574  C  CA  . PRO C 1 29  ? 30.879  0.711   -37.164 1.00 5.29  ? 29  PRO C CA  1 
ATOM   4575  C  C   . PRO C 1 29  ? 29.646  0.246   -37.980 1.00 7.96  ? 29  PRO C C   1 
ATOM   4576  O  O   . PRO C 1 29  ? 28.696  0.994   -38.224 1.00 8.30  ? 29  PRO C O   1 
ATOM   4577  C  CB  . PRO C 1 29  ? 30.827  -0.018  -35.833 1.00 8.08  ? 29  PRO C CB  1 
ATOM   4578  C  CG  . PRO C 1 29  ? 29.893  0.835   -35.053 1.00 8.74  ? 29  PRO C CG  1 
ATOM   4579  C  CD  . PRO C 1 29  ? 30.151  2.279   -35.492 1.00 9.02  ? 29  PRO C CD  1 
ATOM   4580  N  N   . ILE C 1 30  ? 29.680  -1.057  -38.387 1.00 8.35  ? 30  ILE C N   1 
ATOM   4581  C  CA  . ILE C 1 30  ? 28.641  -1.633  -39.273 1.00 8.31  ? 30  ILE C CA  1 
ATOM   4582  C  C   . ILE C 1 30  ? 28.349  -3.065  -38.826 1.00 7.75  ? 30  ILE C C   1 
ATOM   4583  O  O   . ILE C 1 30  ? 29.105  -3.644  -38.023 1.00 9.20  ? 30  ILE C O   1 
ATOM   4584  C  CB  . ILE C 1 30  ? 29.096  -1.666  -40.765 1.00 8.37  ? 30  ILE C CB  1 
ATOM   4585  C  CG1 . ILE C 1 30  ? 30.346  -2.556  -40.893 1.00 9.40  ? 30  ILE C CG1 1 
ATOM   4586  C  CG2 . ILE C 1 30  ? 29.304  -0.180  -41.266 1.00 10.15 ? 30  ILE C CG2 1 
ATOM   4587  C  CD1 . ILE C 1 30  ? 30.715  -2.751  -42.436 1.00 10.46 ? 30  ILE C CD1 1 
ATOM   4588  N  N   . ASP C 1 31  ? 27.184  -3.528  -39.242 1.00 7.44  ? 31  ASP C N   1 
ATOM   4589  C  CA  . ASP C 1 31  ? 26.871  -4.986  -39.103 1.00 7.38  ? 31  ASP C CA  1 
ATOM   4590  C  C   . ASP C 1 31  ? 27.504  -5.772  -40.199 1.00 9.39  ? 31  ASP C C   1 
ATOM   4591  O  O   . ASP C 1 31  ? 27.343  -5.495  -41.411 1.00 10.27 ? 31  ASP C O   1 
ATOM   4592  C  CB  . ASP C 1 31  ? 25.353  -5.174  -39.204 1.00 8.90  ? 31  ASP C CB  1 
ATOM   4593  C  CG  . ASP C 1 31  ? 24.930  -6.645  -39.012 1.00 10.85 ? 31  ASP C CG  1 
ATOM   4594  O  OD1 . ASP C 1 31  ? 25.380  -7.216  -38.021 1.00 10.35 ? 31  ASP C OD1 1 
ATOM   4595  O  OD2 . ASP C 1 31  ? 23.986  -7.078  -39.743 1.00 15.04 ? 31  ASP C OD2 1 
ATOM   4596  N  N   . LEU C 1 32  ? 28.178  -6.859  -39.803 1.00 9.63  ? 32  LEU C N   1 
ATOM   4597  C  CA  . LEU C 1 32  ? 28.879  -7.728  -40.722 1.00 9.32  ? 32  LEU C CA  1 
ATOM   4598  C  C   . LEU C 1 32  ? 27.977  -8.971  -40.923 1.00 11.08 ? 32  LEU C C   1 
ATOM   4599  O  O   . LEU C 1 32  ? 27.780  -9.743  -40.005 1.00 12.83 ? 32  LEU C O   1 
ATOM   4600  C  CB  . LEU C 1 32  ? 30.237  -8.168  -40.003 1.00 10.12 ? 32  LEU C CB  1 
ATOM   4601  C  CG  . LEU C 1 32  ? 31.133  -7.005  -39.553 1.00 10.44 ? 32  LEU C CG  1 
ATOM   4602  C  CD1 . LEU C 1 32  ? 32.357  -7.425  -38.741 1.00 13.17 ? 32  LEU C CD1 1 
ATOM   4603  C  CD2 . LEU C 1 32  ? 31.592  -6.281  -40.799 1.00 12.38 ? 32  LEU C CD2 1 
ATOM   4604  N  N   . HIS C 1 33  ? 27.413  -9.114  -42.078 1.00 16.63 ? 33  HIS C N   1 
ATOM   4605  C  CA  . HIS C 1 33  ? 26.432  -10.195 -42.264 1.00 18.61 ? 33  HIS C CA  1 
ATOM   4606  C  C   . HIS C 1 33  ? 26.588  -10.823 -43.627 1.00 18.40 ? 33  HIS C C   1 
ATOM   4607  O  O   . HIS C 1 33  ? 27.092  -10.115 -44.491 1.00 17.09 ? 33  HIS C O   1 
ATOM   4608  C  CB  . HIS C 1 33  ? 25.023  -9.713  -41.984 1.00 19.49 ? 33  HIS C CB  1 
ATOM   4609  C  CG  . HIS C 1 33  ? 24.543  -8.672  -42.906 1.00 21.85 ? 33  HIS C CG  1 
ATOM   4610  N  ND1 . HIS C 1 33  ? 23.799  -8.972  -44.035 1.00 26.39 ? 33  HIS C ND1 1 
ATOM   4611  C  CD2 . HIS C 1 33  ? 24.702  -7.339  -42.883 1.00 22.46 ? 33  HIS C CD2 1 
ATOM   4612  C  CE1 . HIS C 1 33  ? 23.561  -7.859  -44.696 1.00 25.59 ? 33  HIS C CE1 1 
ATOM   4613  N  NE2 . HIS C 1 33  ? 24.100  -6.850  -44.022 1.00 27.57 ? 33  HIS C NE2 1 
ATOM   4614  N  N   . SER C 1 34  ? 26.078  -12.078 -43.852 1.00 18.97 ? 34  SER C N   1 
ATOM   4615  C  CA  . SER C 1 34  ? 26.553  -12.890 -44.959 1.00 21.65 ? 34  SER C CA  1 
ATOM   4616  C  C   . SER C 1 34  ? 26.234  -12.318 -46.255 1.00 17.68 ? 34  SER C C   1 
ATOM   4617  O  O   . SER C 1 34  ? 27.093  -12.452 -47.159 1.00 20.05 ? 34  SER C O   1 
ATOM   4618  C  CB  . SER C 1 34  ? 26.042  -14.348 -44.921 1.00 21.71 ? 34  SER C CB  1 
ATOM   4619  O  OG  . SER C 1 34  ? 24.640  -14.280 -44.797 1.00 32.10 ? 34  SER C OG  1 
ATOM   4620  N  N   . ASP C 1 35  ? 25.115  -11.565 -46.343 1.00 20.51 ? 35  ASP C N   1 
ATOM   4621  C  CA  . ASP C 1 35  ? 24.635  -11.069 -47.649 1.00 23.06 ? 35  ASP C CA  1 
ATOM   4622  C  C   . ASP C 1 35  ? 25.586  -10.085 -48.282 1.00 19.69 ? 35  ASP C C   1 
ATOM   4623  O  O   . ASP C 1 35  ? 25.609  -9.880  -49.537 1.00 21.64 ? 35  ASP C O   1 
ATOM   4624  C  CB  . ASP C 1 35  ? 23.211  -10.438 -47.570 1.00 24.69 ? 35  ASP C CB  1 
ATOM   4625  C  CG  . ASP C 1 35  ? 22.088  -11.486 -47.279 1.00 34.03 ? 35  ASP C CG  1 
ATOM   4626  O  OD1 . ASP C 1 35  ? 22.366  -12.713 -47.419 1.00 35.18 ? 35  ASP C OD1 1 
ATOM   4627  O  OD2 . ASP C 1 35  ? 20.934  -11.062 -46.869 1.00 39.73 ? 35  ASP C OD2 1 
ATOM   4628  N  N   . ILE C 1 36  ? 26.468  -9.451  -47.464 1.00 15.81 ? 36  ILE C N   1 
ATOM   4629  C  CA  . ILE C 1 36  ? 27.308  -8.415  -47.953 1.00 14.30 ? 36  ILE C CA  1 
ATOM   4630  C  C   . ILE C 1 36  ? 28.808  -8.835  -47.915 1.00 12.16 ? 36  ILE C C   1 
ATOM   4631  O  O   . ILE C 1 36  ? 29.655  -8.016  -48.153 1.00 13.87 ? 36  ILE C O   1 
ATOM   4632  C  CB  . ILE C 1 36  ? 27.115  -7.106  -47.190 1.00 13.25 ? 36  ILE C CB  1 
ATOM   4633  C  CG1 . ILE C 1 36  ? 27.446  -7.230  -45.701 1.00 15.05 ? 36  ILE C CG1 1 
ATOM   4634  C  CG2 . ILE C 1 36  ? 25.647  -6.456  -47.469 1.00 17.30 ? 36  ILE C CG2 1 
ATOM   4635  C  CD1 . ILE C 1 36  ? 27.634  -5.858  -44.928 1.00 15.85 ? 36  ILE C CD1 1 
ATOM   4636  N  N   . LEU C 1 37  ? 29.094  -10.108 -47.612 1.00 15.98 ? 37  LEU C N   1 
ATOM   4637  C  CA  . LEU C 1 37  ? 30.494  -10.539 -47.547 1.00 14.46 ? 37  LEU C CA  1 
ATOM   4638  C  C   . LEU C 1 37  ? 30.960  -11.008 -48.892 1.00 16.23 ? 37  LEU C C   1 
ATOM   4639  O  O   . LEU C 1 37  ? 30.141  -11.656 -49.700 1.00 17.32 ? 37  LEU C O   1 
ATOM   4640  C  CB  . LEU C 1 37  ? 30.667  -11.681 -46.582 1.00 16.34 ? 37  LEU C CB  1 
ATOM   4641  C  CG  . LEU C 1 37  ? 30.156  -11.476 -45.169 1.00 15.18 ? 37  LEU C CG  1 
ATOM   4642  C  CD1 . LEU C 1 37  ? 30.334  -12.660 -44.236 1.00 16.75 ? 37  LEU C CD1 1 
ATOM   4643  C  CD2 . LEU C 1 37  ? 30.863  -10.225 -44.542 1.00 16.75 ? 37  LEU C CD2 1 
ATOM   4644  N  N   . GLN C 1 38  ? 32.209  -10.760 -49.224 1.00 14.31 ? 38  GLN C N   1 
ATOM   4645  C  CA  . GLN C 1 38  ? 32.755  -11.297 -50.506 1.00 14.77 ? 38  GLN C CA  1 
ATOM   4646  C  C   . GLN C 1 38  ? 34.198  -11.673 -50.219 1.00 13.81 ? 38  GLN C C   1 
ATOM   4647  O  O   . GLN C 1 38  ? 35.014  -10.868 -49.799 1.00 13.63 ? 38  GLN C O   1 
ATOM   4648  C  CB  . GLN C 1 38  ? 32.688  -10.241 -51.585 1.00 16.79 ? 38  GLN C CB  1 
ATOM   4649  C  CG  . GLN C 1 38  ? 33.268  -10.723 -52.996 1.00 16.29 ? 38  GLN C CG  1 
ATOM   4650  C  CD  . GLN C 1 38  ? 32.882  -9.756  -54.069 1.00 23.04 ? 38  GLN C CD  1 
ATOM   4651  O  OE1 . GLN C 1 38  ? 31.673  -9.647  -54.465 1.00 29.74 ? 38  GLN C OE1 1 
ATOM   4652  N  NE2 . GLN C 1 38  ? 33.808  -8.995  -54.464 1.00 21.71 ? 38  GLN C NE2 1 
ATOM   4653  N  N   . TYR C 1 39  ? 34.540  -12.960 -50.510 1.00 15.96 ? 39  TYR C N   1 
ATOM   4654  C  CA  . TYR C 1 39  ? 35.942  -13.333 -50.450 1.00 16.72 ? 39  TYR C CA  1 
ATOM   4655  C  C   . TYR C 1 39  ? 36.848  -12.553 -51.360 1.00 17.02 ? 39  TYR C C   1 
ATOM   4656  O  O   . TYR C 1 39  ? 36.477  -12.263 -52.547 1.00 19.88 ? 39  TYR C O   1 
ATOM   4657  C  CB  . TYR C 1 39  ? 35.980  -14.880 -50.769 1.00 19.11 ? 39  TYR C CB  1 
ATOM   4658  C  CG  . TYR C 1 39  ? 37.422  -15.363 -50.876 1.00 19.94 ? 39  TYR C CG  1 
ATOM   4659  C  CD1 . TYR C 1 39  ? 38.267  -15.394 -49.756 1.00 20.04 ? 39  TYR C CD1 1 
ATOM   4660  C  CD2 . TYR C 1 39  ? 37.944  -15.750 -52.143 1.00 20.16 ? 39  TYR C CD2 1 
ATOM   4661  C  CE1 . TYR C 1 39  ? 39.604  -15.775 -49.886 1.00 24.30 ? 39  TYR C CE1 1 
ATOM   4662  C  CE2 . TYR C 1 39  ? 39.254  -16.150 -52.296 1.00 23.92 ? 39  TYR C CE2 1 
ATOM   4663  C  CZ  . TYR C 1 39  ? 40.085  -16.202 -51.157 1.00 26.02 ? 39  TYR C CZ  1 
ATOM   4664  O  OH  . TYR C 1 39  ? 41.426  -16.606 -51.367 1.00 25.88 ? 39  TYR C OH  1 
ATOM   4665  N  N   . ASP C 1 40  ? 38.021  -12.157 -50.885 1.00 16.13 ? 40  ASP C N   1 
ATOM   4666  C  CA  . ASP C 1 40  ? 38.968  -11.298 -51.658 1.00 17.76 ? 40  ASP C CA  1 
ATOM   4667  C  C   . ASP C 1 40  ? 40.384  -11.967 -51.418 1.00 18.52 ? 40  ASP C C   1 
ATOM   4668  O  O   . ASP C 1 40  ? 40.939  -11.964 -50.301 1.00 18.87 ? 40  ASP C O   1 
ATOM   4669  C  CB  . ASP C 1 40  ? 38.903  -9.886  -51.099 1.00 18.46 ? 40  ASP C CB  1 
ATOM   4670  C  CG  . ASP C 1 40  ? 39.878  -8.889  -51.733 1.00 21.91 ? 40  ASP C CG  1 
ATOM   4671  O  OD1 . ASP C 1 40  ? 40.787  -9.289  -52.463 1.00 20.00 ? 40  ASP C OD1 1 
ATOM   4672  O  OD2 . ASP C 1 40  ? 39.778  -7.638  -51.418 1.00 21.00 ? 40  ASP C OD2 1 
ATOM   4673  N  N   . ALA C 1 41  ? 40.966  -12.469 -52.523 1.00 17.84 ? 41  ALA C N   1 
ATOM   4674  C  CA  . ALA C 1 41  ? 42.305  -13.146 -52.445 1.00 17.44 ? 41  ALA C CA  1 
ATOM   4675  C  C   . ALA C 1 41  ? 43.445  -12.221 -52.053 1.00 19.93 ? 41  ALA C C   1 
ATOM   4676  O  O   . ALA C 1 41  ? 44.540  -12.667 -51.692 1.00 18.31 ? 41  ALA C O   1 
ATOM   4677  C  CB  . ALA C 1 41  ? 42.618  -13.766 -53.807 1.00 19.89 ? 41  ALA C CB  1 
ATOM   4678  N  N   . SER C 1 42  ? 43.272  -10.901 -52.091 1.00 17.58 ? 42  SER C N   1 
ATOM   4679  C  CA  . SER C 1 42  ? 44.354  -10.016 -51.784 1.00 19.00 ? 42  SER C CA  1 
ATOM   4680  C  C   . SER C 1 42  ? 44.586  -9.978  -50.262 1.00 17.53 ? 42  SER C C   1 
ATOM   4681  O  O   . SER C 1 42  ? 45.621  -9.398  -49.796 1.00 20.97 ? 42  SER C O   1 
ATOM   4682  C  CB  . SER C 1 42  ? 44.053  -8.619  -52.284 1.00 18.85 ? 42  SER C CB  1 
ATOM   4683  O  OG  . SER C 1 42  ? 43.032  -8.004  -51.433 1.00 21.20 ? 42  SER C OG  1 
ATOM   4684  N  N   . LEU C 1 43  ? 43.585  -10.533 -49.541 1.00 18.30 ? 43  LEU C N   1 
ATOM   4685  C  CA  . LEU C 1 43  ? 43.619  -10.425 -48.100 1.00 17.19 ? 43  LEU C CA  1 
ATOM   4686  C  C   . LEU C 1 43  ? 44.444  -11.527 -47.434 1.00 18.74 ? 43  LEU C C   1 
ATOM   4687  O  O   . LEU C 1 43  ? 43.921  -12.459 -46.818 1.00 20.08 ? 43  LEU C O   1 
ATOM   4688  C  CB  . LEU C 1 43  ? 42.196  -10.373 -47.544 1.00 16.59 ? 43  LEU C CB  1 
ATOM   4689  C  CG  . LEU C 1 43  ? 41.354  -9.173  -48.040 1.00 16.23 ? 43  LEU C CG  1 
ATOM   4690  C  CD1 . LEU C 1 43  ? 39.923  -9.360  -47.403 1.00 16.86 ? 43  LEU C CD1 1 
ATOM   4691  C  CD2 . LEU C 1 43  ? 41.953  -7.796  -47.930 1.00 16.49 ? 43  LEU C CD2 1 
ATOM   4692  N  N   . THR C 1 44  ? 45.749  -11.373 -47.620 1.00 19.84 ? 44  THR C N   1 
ATOM   4693  C  CA  . THR C 1 44  ? 46.776  -12.226 -46.999 1.00 19.93 ? 44  THR C CA  1 
ATOM   4694  C  C   . THR C 1 44  ? 46.955  -11.965 -45.495 1.00 22.80 ? 44  THR C C   1 
ATOM   4695  O  O   . THR C 1 44  ? 46.561  -10.903 -44.932 1.00 18.87 ? 44  THR C O   1 
ATOM   4696  C  CB  . THR C 1 44  ? 48.120  -11.984 -47.827 1.00 20.22 ? 44  THR C CB  1 
ATOM   4697  O  OG1 . THR C 1 44  ? 48.386  -10.574 -47.945 1.00 23.12 ? 44  THR C OG1 1 
ATOM   4698  C  CG2 . THR C 1 44  ? 47.873  -12.574 -49.217 1.00 22.92 ? 44  THR C CG2 1 
ATOM   4699  N  N   . PRO C 1 45  ? 47.663  -12.865 -44.792 1.00 21.22 ? 45  PRO C N   1 
ATOM   4700  C  CA  . PRO C 1 45  ? 47.934  -12.675 -43.379 1.00 23.09 ? 45  PRO C CA  1 
ATOM   4701  C  C   . PRO C 1 45  ? 48.816  -11.474 -43.071 1.00 24.03 ? 45  PRO C C   1 
ATOM   4702  O  O   . PRO C 1 45  ? 49.850  -11.320 -43.715 1.00 24.33 ? 45  PRO C O   1 
ATOM   4703  C  CB  . PRO C 1 45  ? 48.655  -13.983 -43.042 1.00 22.56 ? 45  PRO C CB  1 
ATOM   4704  C  CG  . PRO C 1 45  ? 48.127  -14.931 -44.029 1.00 22.02 ? 45  PRO C CG  1 
ATOM   4705  C  CD  . PRO C 1 45  ? 48.203  -14.174 -45.243 1.00 20.47 ? 45  PRO C CD  1 
ATOM   4706  N  N   . LEU C 1 46  ? 48.397  -10.578 -42.163 1.00 19.98 ? 46  LEU C N   1 
ATOM   4707  C  CA  . LEU C 1 46  ? 49.144  -9.409  -41.749 1.00 21.27 ? 46  LEU C CA  1 
ATOM   4708  C  C   . LEU C 1 46  ? 50.290  -9.900  -40.822 1.00 21.71 ? 46  LEU C C   1 
ATOM   4709  O  O   . LEU C 1 46  ? 50.163  -10.929 -40.186 1.00 22.88 ? 46  LEU C O   1 
ATOM   4710  C  CB  . LEU C 1 46  ? 48.238  -8.478  -40.937 1.00 18.96 ? 46  LEU C CB  1 
ATOM   4711  C  CG  . LEU C 1 46  ? 47.033  -7.982  -41.722 1.00 22.42 ? 46  LEU C CG  1 
ATOM   4712  C  CD1 . LEU C 1 46  ? 46.281  -7.042  -40.863 1.00 23.95 ? 46  LEU C CD1 1 
ATOM   4713  C  CD2 . LEU C 1 46  ? 47.608  -7.301  -43.005 1.00 21.79 ? 46  LEU C CD2 1 
ATOM   4714  N  N   . GLU C 1 47  ? 51.337  -9.082  -40.720 1.00 21.66 ? 47  GLU C N   1 
ATOM   4715  C  CA  . GLU C 1 47  ? 52.404  -9.314  -39.723 1.00 23.28 ? 47  GLU C CA  1 
ATOM   4716  C  C   . GLU C 1 47  ? 52.476  -8.197  -38.747 1.00 22.11 ? 47  GLU C C   1 
ATOM   4717  O  O   . GLU C 1 47  ? 52.321  -6.998  -39.121 1.00 22.36 ? 47  GLU C O   1 
ATOM   4718  C  CB  . GLU C 1 47  ? 53.730  -9.450  -40.457 1.00 25.42 ? 47  GLU C CB  1 
ATOM   4719  C  CG  . GLU C 1 47  ? 53.692  -10.584 -41.526 1.00 28.98 ? 47  GLU C CG  1 
ATOM   4720  C  CD  . GLU C 1 47  ? 54.947  -10.631 -42.432 1.00 33.74 ? 47  GLU C CD  1 
ATOM   4721  O  OE1 . GLU C 1 47  ? 56.101  -10.625 -41.865 1.00 40.80 ? 47  GLU C OE1 1 
ATOM   4722  O  OE2 . GLU C 1 47  ? 54.765  -10.710 -43.706 1.00 41.23 ? 47  GLU C OE2 1 
ATOM   4723  N  N   . PHE C 1 48  ? 52.615  -8.538  -37.460 1.00 20.19 ? 48  PHE C N   1 
ATOM   4724  C  CA  . PHE C 1 48  ? 52.581  -7.582  -36.374 1.00 22.40 ? 48  PHE C CA  1 
ATOM   4725  C  C   . PHE C 1 48  ? 54.015  -7.384  -35.909 1.00 23.71 ? 48  PHE C C   1 
ATOM   4726  O  O   . PHE C 1 48  ? 54.605  -8.308  -35.351 1.00 25.39 ? 48  PHE C O   1 
ATOM   4727  C  CB  . PHE C 1 48  ? 51.552  -8.037  -35.265 1.00 21.89 ? 48  PHE C CB  1 
ATOM   4728  C  CG  . PHE C 1 48  ? 50.232  -8.562  -35.875 1.00 22.54 ? 48  PHE C CG  1 
ATOM   4729  C  CD1 . PHE C 1 48  ? 49.328  -7.706  -36.434 1.00 20.72 ? 48  PHE C CD1 1 
ATOM   4730  C  CD2 . PHE C 1 48  ? 49.967  -9.956  -35.987 1.00 20.38 ? 48  PHE C CD2 1 
ATOM   4731  C  CE1 . PHE C 1 48  ? 48.196  -8.256  -37.019 1.00 17.72 ? 48  PHE C CE1 1 
ATOM   4732  C  CE2 . PHE C 1 48  ? 48.849  -10.445 -36.550 1.00 23.16 ? 48  PHE C CE2 1 
ATOM   4733  C  CZ  . PHE C 1 48  ? 47.966  -9.612  -37.052 1.00 21.02 ? 48  PHE C CZ  1 
ATOM   4734  N  N   . GLN C 1 49  ? 54.553  -6.189  -36.090 1.00 22.98 ? 49  GLN C N   1 
ATOM   4735  C  CA  . GLN C 1 49  ? 55.998  -5.976  -35.788 1.00 23.99 ? 49  GLN C CA  1 
ATOM   4736  C  C   . GLN C 1 49  ? 56.256  -5.042  -34.657 1.00 23.51 ? 49  GLN C C   1 
ATOM   4737  O  O   . GLN C 1 49  ? 55.606  -4.021  -34.578 1.00 21.49 ? 49  GLN C O   1 
ATOM   4738  C  CB  . GLN C 1 49  ? 56.620  -5.492  -37.069 1.00 25.73 ? 49  GLN C CB  1 
ATOM   4739  C  CG  . GLN C 1 49  ? 56.528  -6.616  -38.023 1.00 28.37 ? 49  GLN C CG  1 
ATOM   4740  C  CD  . GLN C 1 49  ? 57.295  -6.389  -39.256 1.00 38.09 ? 49  GLN C CD  1 
ATOM   4741  O  OE1 . GLN C 1 49  ? 57.525  -5.226  -39.655 1.00 41.79 ? 49  GLN C OE1 1 
ATOM   4742  N  NE2 . GLN C 1 49  ? 57.714  -7.495  -39.914 1.00 35.88 ? 49  GLN C NE2 1 
ATOM   4743  N  N   . GLY C 1 50  ? 57.241  -5.386  -33.762 1.00 20.79 ? 50  GLY C N   1 
ATOM   4744  C  CA  . GLY C 1 50  ? 57.518  -4.579  -32.578 1.00 23.40 ? 50  GLY C CA  1 
ATOM   4745  C  C   . GLY C 1 50  ? 56.404  -4.506  -31.571 1.00 20.40 ? 50  GLY C C   1 
ATOM   4746  O  O   . GLY C 1 50  ? 56.258  -3.532  -30.837 1.00 19.93 ? 50  GLY C O   1 
ATOM   4747  N  N   . TYR C 1 51  ? 55.576  -5.515  -31.554 1.00 20.63 ? 51  TYR C N   1 
ATOM   4748  C  CA  . TYR C 1 51  ? 54.399  -5.596  -30.656 1.00 21.67 ? 51  TYR C CA  1 
ATOM   4749  C  C   . TYR C 1 51  ? 54.828  -6.097  -29.291 1.00 22.55 ? 51  TYR C C   1 
ATOM   4750  O  O   . TYR C 1 51  ? 54.134  -5.908  -28.324 1.00 21.11 ? 51  TYR C O   1 
ATOM   4751  C  CB  . TYR C 1 51  ? 53.247  -6.534  -31.188 1.00 20.98 ? 51  TYR C CB  1 
ATOM   4752  C  CG  . TYR C 1 51  ? 52.200  -5.852  -32.102 1.00 19.94 ? 51  TYR C CG  1 
ATOM   4753  C  CD1 . TYR C 1 51  ? 50.837  -6.129  -31.935 1.00 16.43 ? 51  TYR C CD1 1 
ATOM   4754  C  CD2 . TYR C 1 51  ? 52.592  -4.971  -33.130 1.00 16.71 ? 51  TYR C CD2 1 
ATOM   4755  C  CE1 . TYR C 1 51  ? 49.886  -5.538  -32.728 1.00 20.29 ? 51  TYR C CE1 1 
ATOM   4756  C  CE2 . TYR C 1 51  ? 51.626  -4.379  -33.969 1.00 18.31 ? 51  TYR C CE2 1 
ATOM   4757  C  CZ  . TYR C 1 51  ? 50.307  -4.697  -33.770 1.00 19.95 ? 51  TYR C CZ  1 
ATOM   4758  O  OH  . TYR C 1 51  ? 49.358  -4.125  -34.597 1.00 19.17 ? 51  TYR C OH  1 
ATOM   4759  N  N   . ASN C 1 52  ? 56.007  -6.733  -29.236 1.00 24.34 ? 52  ASN C N   1 
ATOM   4760  C  CA  . ASN C 1 52  ? 56.539  -7.208  -27.961 1.00 27.23 ? 52  ASN C CA  1 
ATOM   4761  C  C   . ASN C 1 52  ? 57.228  -6.080  -27.206 1.00 27.39 ? 52  ASN C C   1 
ATOM   4762  O  O   . ASN C 1 52  ? 58.424  -5.840  -27.442 1.00 30.13 ? 52  ASN C O   1 
ATOM   4763  C  CB  . ASN C 1 52  ? 57.552  -8.355  -28.205 1.00 26.56 ? 52  ASN C CB  1 
ATOM   4764  C  CG  . ASN C 1 52  ? 57.340  -9.438  -27.284 1.00 33.29 ? 52  ASN C CG  1 
ATOM   4765  O  OD1 . ASN C 1 52  ? 57.120  -9.206  -26.089 1.00 30.86 ? 52  ASN C OD1 1 
ATOM   4766  N  ND2 . ASN C 1 52  ? 57.234  -10.646 -27.827 1.00 35.24 ? 52  ASN C ND2 1 
ATOM   4767  N  N   . LEU C 1 53  ? 56.483  -5.408  -26.324 1.00 28.28 ? 53  LEU C N   1 
ATOM   4768  C  CA  . LEU C 1 53  ? 56.992  -4.188  -25.712 1.00 28.78 ? 53  LEU C CA  1 
ATOM   4769  C  C   . LEU C 1 53  ? 57.635  -4.715  -24.414 1.00 30.39 ? 53  LEU C C   1 
ATOM   4770  O  O   . LEU C 1 53  ? 57.020  -5.474  -23.642 1.00 30.43 ? 53  LEU C O   1 
ATOM   4771  C  CB  . LEU C 1 53  ? 55.900  -3.133  -25.432 1.00 26.46 ? 53  LEU C CB  1 
ATOM   4772  C  CG  . LEU C 1 53  ? 54.855  -2.743  -26.522 1.00 24.40 ? 53  LEU C CG  1 
ATOM   4773  C  CD1 . LEU C 1 53  ? 53.813  -1.795  -25.868 1.00 21.32 ? 53  LEU C CD1 1 
ATOM   4774  C  CD2 . LEU C 1 53  ? 55.480  -2.067  -27.752 1.00 23.73 ? 53  LEU C CD2 1 
ATOM   4775  N  N   . SER C 1 54  ? 58.836  -4.265  -24.161 1.00 34.26 ? 54  SER C N   1 
ATOM   4776  C  CA  . SER C 1 54  ? 59.525  -4.727  -22.982 1.00 36.19 ? 54  SER C CA  1 
ATOM   4777  C  C   . SER C 1 54  ? 58.823  -4.407  -21.681 1.00 38.81 ? 54  SER C C   1 
ATOM   4778  O  O   . SER C 1 54  ? 58.380  -3.274  -21.471 1.00 37.41 ? 54  SER C O   1 
ATOM   4779  C  CB  . SER C 1 54  ? 60.889  -4.111  -22.952 1.00 36.86 ? 54  SER C CB  1 
ATOM   4780  O  OG  . SER C 1 54  ? 61.204  -3.560  -24.206 1.00 38.86 ? 54  SER C OG  1 
ATOM   4781  N  N   . ALA C 1 55  ? 58.793  -5.413  -20.803 1.00 40.94 ? 55  ALA C N   1 
ATOM   4782  C  CA  . ALA C 1 55  ? 58.371  -5.265  -19.415 1.00 43.05 ? 55  ALA C CA  1 
ATOM   4783  C  C   . ALA C 1 55  ? 59.155  -4.136  -18.757 1.00 43.33 ? 55  ALA C C   1 
ATOM   4784  O  O   . ALA C 1 55  ? 58.756  -3.644  -17.707 1.00 44.67 ? 55  ALA C O   1 
ATOM   4785  C  CB  . ALA C 1 55  ? 58.585  -6.552  -18.635 1.00 43.28 ? 55  ALA C CB  1 
ATOM   4786  N  N   . ASN C 1 56  ? 60.239  -3.751  -19.416 1.00 30.00 ? 56  ASN C N   1 
ATOM   4787  C  CA  . ASN C 1 56  ? 61.172  -2.735  -18.973 1.00 30.00 ? 56  ASN C CA  1 
ATOM   4788  C  C   . ASN C 1 56  ? 60.535  -1.371  -19.079 1.00 30.00 ? 56  ASN C C   1 
ATOM   4789  O  O   . ASN C 1 56  ? 60.617  -0.548  -18.137 1.00 30.00 ? 56  ASN C O   1 
ATOM   4790  C  CB  . ASN C 1 56  ? 62.338  -2.692  -19.960 1.00 20.00 ? 56  ASN C CB  1 
ATOM   4791  C  CG  . ASN C 1 56  ? 63.604  -3.412  -19.477 1.00 20.00 ? 56  ASN C CG  1 
ATOM   4792  O  OD1 . ASN C 1 56  ? 64.074  -3.221  -18.362 1.00 20.00 ? 56  ASN C OD1 1 
ATOM   4793  N  ND2 . ASN C 1 56  ? 64.204  -4.189  -20.379 1.00 20.00 ? 56  ASN C ND2 1 
ATOM   4794  N  N   . LYS C 1 57  ? 59.940  -1.165  -20.269 1.00 40.48 ? 57  LYS C N   1 
ATOM   4795  C  CA  . LYS C 1 57  ? 59.430  0.117   -20.751 1.00 39.40 ? 57  LYS C CA  1 
ATOM   4796  C  C   . LYS C 1 57  ? 58.081  0.271   -20.145 1.00 35.69 ? 57  LYS C C   1 
ATOM   4797  O  O   . LYS C 1 57  ? 57.528  -0.662  -19.644 1.00 35.32 ? 57  LYS C O   1 
ATOM   4798  C  CB  . LYS C 1 57  ? 59.211  0.076   -22.279 1.00 38.88 ? 57  LYS C CB  1 
ATOM   4799  C  CG  . LYS C 1 57  ? 60.400  0.169   -23.204 1.00 40.76 ? 57  LYS C CG  1 
ATOM   4800  C  CD  . LYS C 1 57  ? 60.383  1.493   -23.961 1.00 42.93 ? 57  LYS C CD  1 
ATOM   4801  C  CE  . LYS C 1 57  ? 59.753  1.383   -25.360 1.00 47.56 ? 57  LYS C CE  1 
ATOM   4802  N  NZ  . LYS C 1 57  ? 58.994  2.600   -25.774 1.00 46.47 ? 57  LYS C NZ  1 
ATOM   4803  N  N   . GLN C 1 58  ? 57.533  1.475   -20.222 1.00 34.00 ? 58  GLN C N   1 
ATOM   4804  C  CA  . GLN C 1 58  ? 56.172  1.708   -19.796 1.00 31.27 ? 58  GLN C CA  1 
ATOM   4805  C  C   . GLN C 1 58  ? 55.446  2.736   -20.686 1.00 27.38 ? 58  GLN C C   1 
ATOM   4806  O  O   . GLN C 1 58  ? 56.095  3.530   -21.413 1.00 26.93 ? 58  GLN C O   1 
ATOM   4807  C  CB  . GLN C 1 58  ? 56.225  2.225   -18.362 1.00 33.24 ? 58  GLN C CB  1 
ATOM   4808  C  CG  . GLN C 1 58  ? 56.742  3.677   -18.298 1.00 33.55 ? 58  GLN C CG  1 
ATOM   4809  C  CD  . GLN C 1 58  ? 58.008  4.064   -19.189 1.00 43.28 ? 58  GLN C CD  1 
ATOM   4810  O  OE1 . GLN C 1 58  ? 58.546  3.264   -19.987 1.00 46.32 ? 58  GLN C OE1 1 
ATOM   4811  N  NE2 . GLN C 1 58  ? 58.460  5.322   -19.036 1.00 47.93 ? 58  GLN C NE2 1 
ATOM   4812  N  N   . PHE C 1 59  ? 54.104  2.668   -20.602 1.00 24.52 ? 59  PHE C N   1 
ATOM   4813  C  CA  . PHE C 1 59  ? 53.113  3.254   -21.533 1.00 22.85 ? 59  PHE C CA  1 
ATOM   4814  C  C   . PHE C 1 59  ? 51.977  3.934   -20.834 1.00 21.26 ? 59  PHE C C   1 
ATOM   4815  O  O   . PHE C 1 59  ? 51.420  3.391   -19.909 1.00 21.96 ? 59  PHE C O   1 
ATOM   4816  C  CB  . PHE C 1 59  ? 52.733  2.091   -22.508 1.00 23.61 ? 59  PHE C CB  1 
ATOM   4817  C  CG  . PHE C 1 59  ? 53.939  1.492   -23.164 1.00 23.35 ? 59  PHE C CG  1 
ATOM   4818  C  CD1 . PHE C 1 59  ? 54.503  2.120   -24.267 1.00 20.42 ? 59  PHE C CD1 1 
ATOM   4819  C  CD2 . PHE C 1 59  ? 54.658  0.364   -22.555 1.00 21.10 ? 59  PHE C CD2 1 
ATOM   4820  C  CE1 . PHE C 1 59  ? 55.683  1.604   -24.896 1.00 25.61 ? 59  PHE C CE1 1 
ATOM   4821  C  CE2 . PHE C 1 59  ? 55.830  -0.109  -23.130 1.00 22.64 ? 59  PHE C CE2 1 
ATOM   4822  C  CZ  . PHE C 1 59  ? 56.356  0.451   -24.281 1.00 25.02 ? 59  PHE C CZ  1 
ATOM   4823  N  N   . LEU C 1 60  ? 51.663  5.185   -21.192 1.00 18.07 ? 60  LEU C N   1 
ATOM   4824  C  CA  . LEU C 1 60  ? 50.764  6.040   -20.469 1.00 19.65 ? 60  LEU C CA  1 
ATOM   4825  C  C   . LEU C 1 60  ? 49.333  5.540   -20.797 1.00 20.18 ? 60  LEU C C   1 
ATOM   4826  O  O   . LEU C 1 60  ? 48.955  5.468   -21.999 1.00 21.79 ? 60  LEU C O   1 
ATOM   4827  C  CB  . LEU C 1 60  ? 50.961  7.448   -21.020 1.00 18.54 ? 60  LEU C CB  1 
ATOM   4828  C  CG  . LEU C 1 60  ? 50.136  8.577   -20.455 1.00 21.09 ? 60  LEU C CG  1 
ATOM   4829  C  CD1 . LEU C 1 60  ? 50.483  8.626   -18.919 1.00 22.23 ? 60  LEU C CD1 1 
ATOM   4830  C  CD2 . LEU C 1 60  ? 50.308  9.938   -21.200 1.00 21.16 ? 60  LEU C CD2 1 
ATOM   4831  N  N   A LEU C 1 61  ? 48.578  5.251   -19.745 0.50 19.06 ? 61  LEU C N   1 
ATOM   4832  N  N   B LEU C 1 61  ? 48.598  5.103   -19.789 0.50 19.99 ? 61  LEU C N   1 
ATOM   4833  C  CA  A LEU C 1 61  ? 47.153  4.922   -19.714 0.50 17.99 ? 61  LEU C CA  1 
ATOM   4834  C  CA  B LEU C 1 61  ? 47.147  4.936   -19.828 0.50 20.62 ? 61  LEU C CA  1 
ATOM   4835  C  C   A LEU C 1 61  ? 46.254  6.093   -19.197 0.50 19.00 ? 61  LEU C C   1 
ATOM   4836  C  C   B LEU C 1 61  ? 46.496  6.241   -19.429 0.50 20.60 ? 61  LEU C C   1 
ATOM   4837  O  O   A LEU C 1 61  ? 46.412  6.605   -18.080 0.50 17.95 ? 61  LEU C O   1 
ATOM   4838  O  O   B LEU C 1 61  ? 46.995  6.911   -18.493 0.50 20.76 ? 61  LEU C O   1 
ATOM   4839  C  CB  A LEU C 1 61  ? 47.034  3.698   -18.834 0.50 17.87 ? 61  LEU C CB  1 
ATOM   4840  C  CB  B LEU C 1 61  ? 46.739  3.909   -18.798 0.50 21.46 ? 61  LEU C CB  1 
ATOM   4841  C  CG  A LEU C 1 61  ? 45.636  3.160   -18.667 0.50 13.06 ? 61  LEU C CG  1 
ATOM   4842  C  CG  B LEU C 1 61  ? 46.908  2.413   -19.013 0.50 22.67 ? 61  LEU C CG  1 
ATOM   4843  C  CD1 A LEU C 1 61  ? 45.278  2.147   -19.802 0.50 15.33 ? 61  LEU C CD1 1 
ATOM   4844  C  CD1 B LEU C 1 61  ? 46.190  1.707   -17.918 0.50 25.20 ? 61  LEU C CD1 1 
ATOM   4845  C  CD2 A LEU C 1 61  ? 45.506  2.500   -17.260 0.50 17.01 ? 61  LEU C CD2 1 
ATOM   4846  C  CD2 B LEU C 1 61  ? 46.289  1.884   -20.348 0.50 20.95 ? 61  LEU C CD2 1 
ATOM   4847  N  N   . THR C 1 62  ? 45.339  6.526   -20.020 1.00 18.81 ? 62  THR C N   1 
ATOM   4848  C  CA  . THR C 1 62  ? 44.646  7.815   -19.822 1.00 18.56 ? 62  THR C CA  1 
ATOM   4849  C  C   . THR C 1 62  ? 43.194  7.530   -19.845 1.00 22.17 ? 62  THR C C   1 
ATOM   4850  O  O   . THR C 1 62  ? 42.673  6.788   -20.757 1.00 21.54 ? 62  THR C O   1 
ATOM   4851  C  CB  . THR C 1 62  ? 44.864  8.864   -20.930 1.00 20.42 ? 62  THR C CB  1 
ATOM   4852  O  OG1 . THR C 1 62  ? 46.244  9.205   -20.973 1.00 21.72 ? 62  THR C OG1 1 
ATOM   4853  C  CG2 . THR C 1 62  ? 44.061  10.200  -20.604 1.00 21.72 ? 62  THR C CG2 1 
ATOM   4854  N  N   . ASN C 1 63  ? 42.483  8.087   -18.861 1.00 20.61 ? 63  ASN C N   1 
ATOM   4855  C  CA  . ASN C 1 63  ? 41.118  8.118   -18.990 1.00 18.65 ? 63  ASN C CA  1 
ATOM   4856  C  C   . ASN C 1 63  ? 40.808  9.472   -19.660 1.00 22.54 ? 63  ASN C C   1 
ATOM   4857  O  O   . ASN C 1 63  ? 40.913  10.528  -19.012 1.00 23.67 ? 63  ASN C O   1 
ATOM   4858  C  CB  . ASN C 1 63  ? 40.474  8.015   -17.578 1.00 20.52 ? 63  ASN C CB  1 
ATOM   4859  C  CG  . ASN C 1 63  ? 38.921  8.252   -17.575 1.00 18.85 ? 63  ASN C CG  1 
ATOM   4860  O  OD1 . ASN C 1 63  ? 38.322  8.882   -18.458 1.00 19.64 ? 63  ASN C OD1 1 
ATOM   4861  N  ND2 . ASN C 1 63  ? 38.269  7.874   -16.443 1.00 17.11 ? 63  ASN C ND2 1 
ATOM   4862  N  N   . ASN C 1 64  ? 40.417  9.441   -20.950 1.00 19.28 ? 64  ASN C N   1 
ATOM   4863  C  CA  . ASN C 1 64  ? 40.129  10.705  -21.611 1.00 23.06 ? 64  ASN C CA  1 
ATOM   4864  C  C   . ASN C 1 64  ? 38.680  11.058  -21.524 1.00 20.23 ? 64  ASN C C   1 
ATOM   4865  O  O   . ASN C 1 64  ? 38.220  12.043  -22.198 1.00 23.83 ? 64  ASN C O   1 
ATOM   4866  C  CB  . ASN C 1 64  ? 40.636  10.660  -23.060 1.00 19.32 ? 64  ASN C CB  1 
ATOM   4867  C  CG  . ASN C 1 64  ? 39.806  9.684   -23.885 1.00 22.18 ? 64  ASN C CG  1 
ATOM   4868  O  OD1 . ASN C 1 64  ? 38.709  9.272   -23.477 1.00 23.10 ? 64  ASN C OD1 1 
ATOM   4869  N  ND2 . ASN C 1 64  ? 40.307  9.307   -25.046 1.00 27.12 ? 64  ASN C ND2 1 
ATOM   4870  N  N   . GLY C 1 65  ? 37.933  10.410  -20.587 1.00 24.39 ? 65  GLY C N   1 
ATOM   4871  C  CA  . GLY C 1 65  ? 36.493  10.693  -20.400 1.00 23.90 ? 65  GLY C CA  1 
ATOM   4872  C  C   . GLY C 1 65  ? 35.621  9.971   -21.405 1.00 25.54 ? 65  GLY C C   1 
ATOM   4873  O  O   . GLY C 1 65  ? 34.422  9.988   -21.294 1.00 27.16 ? 65  GLY C O   1 
ATOM   4874  N  N   . HIS C 1 66  ? 36.240  9.359   -22.403 1.00 23.61 ? 66  HIS C N   1 
ATOM   4875  C  CA  . HIS C 1 66  ? 35.450  8.693   -23.443 1.00 22.60 ? 66  HIS C CA  1 
ATOM   4876  C  C   . HIS C 1 66  ? 35.750  7.234   -23.380 1.00 18.36 ? 66  HIS C C   1 
ATOM   4877  O  O   . HIS C 1 66  ? 34.875  6.390   -23.642 1.00 22.93 ? 66  HIS C O   1 
ATOM   4878  C  CB  . HIS C 1 66  ? 35.812  9.221   -24.816 1.00 17.97 ? 66  HIS C CB  1 
ATOM   4879  C  CG  . HIS C 1 66  ? 35.606  10.671  -24.937 1.00 22.27 ? 66  HIS C CG  1 
ATOM   4880  N  ND1 . HIS C 1 66  ? 36.657  11.541  -25.139 1.00 20.09 ? 66  HIS C ND1 1 
ATOM   4881  C  CD2 . HIS C 1 66  ? 34.492  11.417  -24.838 1.00 16.45 ? 66  HIS C CD2 1 
ATOM   4882  C  CE1 . HIS C 1 66  ? 36.173  12.768  -25.246 1.00 22.12 ? 66  HIS C CE1 1 
ATOM   4883  N  NE2 . HIS C 1 66  ? 34.873  12.726  -25.013 1.00 27.84 ? 66  HIS C NE2 1 
ATOM   4884  N  N   . SER C 1 67  ? 36.997  6.922   -23.183 1.00 20.23 ? 67  SER C N   1 
ATOM   4885  C  CA  . SER C 1 67  ? 37.461  5.570   -23.025 1.00 15.16 ? 67  SER C CA  1 
ATOM   4886  C  C   . SER C 1 67  ? 38.711  5.589   -22.134 1.00 21.47 ? 67  SER C C   1 
ATOM   4887  O  O   . SER C 1 67  ? 39.040  6.683   -21.608 1.00 22.80 ? 67  SER C O   1 
ATOM   4888  C  CB  . SER C 1 67  ? 37.728  4.978   -24.471 1.00 17.04 ? 67  SER C CB  1 
ATOM   4889  O  OG  . SER C 1 67  ? 38.116  3.594   -24.376 1.00 17.36 ? 67  SER C OG  1 
ATOM   4890  N  N   . VAL C 1 68  ? 39.330  4.410   -21.976 1.00 16.18 ? 68  VAL C N   1 
ATOM   4891  C  CA  . VAL C 1 68  ? 40.689  4.282   -21.478 1.00 18.97 ? 68  VAL C CA  1 
ATOM   4892  C  C   . VAL C 1 68  ? 41.560  3.953   -22.638 1.00 19.73 ? 68  VAL C C   1 
ATOM   4893  O  O   . VAL C 1 68  ? 41.280  2.969   -23.362 1.00 19.55 ? 68  VAL C O   1 
ATOM   4894  C  CB  . VAL C 1 68  ? 40.822  3.165   -20.342 1.00 18.59 ? 68  VAL C CB  1 
ATOM   4895  C  CG1 . VAL C 1 68  ? 40.597  1.757   -20.768 1.00 17.70 ? 68  VAL C CG1 1 
ATOM   4896  C  CG2 . VAL C 1 68  ? 42.238  3.145   -19.687 1.00 20.61 ? 68  VAL C CG2 1 
ATOM   4897  N  N   A LYS C 1 69  ? 42.599  4.762   -22.815 0.50 18.98 ? 69  LYS C N   1 
ATOM   4898  N  N   B LYS C 1 69  ? 42.644  4.694   -22.790 0.50 19.40 ? 69  LYS C N   1 
ATOM   4899  C  CA  A LYS C 1 69  ? 43.551  4.680   -23.951 0.50 18.17 ? 69  LYS C CA  1 
ATOM   4900  C  CA  B LYS C 1 69  ? 43.494  4.573   -23.988 0.50 18.80 ? 69  LYS C CA  1 
ATOM   4901  C  C   A LYS C 1 69  ? 44.842  4.275   -23.317 0.50 18.96 ? 69  LYS C C   1 
ATOM   4902  C  C   B LYS C 1 69  ? 44.941  4.477   -23.543 0.50 19.54 ? 69  LYS C C   1 
ATOM   4903  O  O   A LYS C 1 69  ? 45.118  4.649   -22.156 0.50 14.99 ? 69  LYS C O   1 
ATOM   4904  O  O   B LYS C 1 69  ? 45.437  5.224   -22.667 0.50 18.72 ? 69  LYS C O   1 
ATOM   4905  C  CB  A LYS C 1 69  ? 43.693  6.099   -24.577 0.50 19.85 ? 69  LYS C CB  1 
ATOM   4906  C  CB  B LYS C 1 69  ? 43.142  5.724   -24.972 0.50 20.91 ? 69  LYS C CB  1 
ATOM   4907  C  CG  A LYS C 1 69  ? 44.928  6.375   -25.456 0.50 20.69 ? 69  LYS C CG  1 
ATOM   4908  C  CG  B LYS C 1 69  ? 44.248  6.630   -25.527 0.50 23.29 ? 69  LYS C CG  1 
ATOM   4909  C  CD  A LYS C 1 69  ? 44.844  7.762   -26.108 0.50 19.86 ? 69  LYS C CD  1 
ATOM   4910  C  CD  B LYS C 1 69  ? 43.639  8.022   -25.617 0.50 21.08 ? 69  LYS C CD  1 
ATOM   4911  C  CE  A LYS C 1 69  ? 44.660  8.934   -25.091 0.50 21.45 ? 69  LYS C CE  1 
ATOM   4912  C  CE  B LYS C 1 69  ? 44.345  9.005   -26.542 0.50 26.83 ? 69  LYS C CE  1 
ATOM   4913  N  NZ  A LYS C 1 69  ? 44.925  10.304  -25.744 0.50 18.01 ? 69  LYS C NZ  1 
ATOM   4914  N  NZ  B LYS C 1 69  ? 43.682  10.311  -26.276 0.50 24.15 ? 69  LYS C NZ  1 
ATOM   4915  N  N   . LEU C 1 70  ? 45.567  3.415   -24.037 1.00 17.82 ? 70  LEU C N   1 
ATOM   4916  C  CA  . LEU C 1 70  ? 47.007  3.137   -23.847 1.00 18.57 ? 70  LEU C CA  1 
ATOM   4917  C  C   . LEU C 1 70  ? 47.808  3.676   -25.001 1.00 19.53 ? 70  LEU C C   1 
ATOM   4918  O  O   . LEU C 1 70  ? 47.669  3.199   -26.153 1.00 17.73 ? 70  LEU C O   1 
ATOM   4919  C  CB  . LEU C 1 70  ? 47.237  1.611   -23.644 1.00 14.67 ? 70  LEU C CB  1 
ATOM   4920  C  CG  . LEU C 1 70  ? 48.668  1.150   -23.309 1.00 22.06 ? 70  LEU C CG  1 
ATOM   4921  C  CD1 . LEU C 1 70  ? 49.001  1.651   -21.863 1.00 20.57 ? 70  LEU C CD1 1 
ATOM   4922  C  CD2 . LEU C 1 70  ? 48.939  -0.381  -23.436 1.00 14.51 ? 70  LEU C CD2 1 
ATOM   4923  N  N   . ASN C 1 71  ? 48.713  4.616   -24.721 1.00 18.84 ? 71  ASN C N   1 
ATOM   4924  C  CA  . ASN C 1 71  ? 49.625  5.098   -25.724 1.00 21.58 ? 71  ASN C CA  1 
ATOM   4925  C  C   . ASN C 1 71  ? 50.603  3.971   -26.195 1.00 21.01 ? 71  ASN C C   1 
ATOM   4926  O  O   . ASN C 1 71  ? 51.074  3.141   -25.384 1.00 20.77 ? 71  ASN C O   1 
ATOM   4927  C  CB  . ASN C 1 71  ? 50.343  6.327   -25.167 1.00 20.87 ? 71  ASN C CB  1 
ATOM   4928  C  CG  . ASN C 1 71  ? 49.495  7.596   -25.291 1.00 26.71 ? 71  ASN C CG  1 
ATOM   4929  O  OD1 . ASN C 1 71  ? 48.303  7.540   -25.679 1.00 27.47 ? 71  ASN C OD1 1 
ATOM   4930  N  ND2 . ASN C 1 71  ? 50.109  8.776   -24.982 1.00 26.11 ? 71  ASN C ND2 1 
ATOM   4931  N  N   . LEU C 1 72  ? 50.889  3.890   -27.521 1.00 17.09 ? 72  LEU C N   1 
ATOM   4932  C  CA  . LEU C 1 72  ? 51.717  2.805   -28.055 1.00 17.49 ? 72  LEU C CA  1 
ATOM   4933  C  C   . LEU C 1 72  ? 52.874  3.337   -28.942 1.00 17.13 ? 72  LEU C C   1 
ATOM   4934  O  O   . LEU C 1 72  ? 52.762  4.519   -29.405 1.00 18.37 ? 72  LEU C O   1 
ATOM   4935  C  CB  . LEU C 1 72  ? 50.864  1.988   -29.029 1.00 17.10 ? 72  LEU C CB  1 
ATOM   4936  C  CG  . LEU C 1 72  ? 49.829  1.059   -28.310 1.00 20.87 ? 72  LEU C CG  1 
ATOM   4937  C  CD1 . LEU C 1 72  ? 48.891  0.442   -29.412 1.00 20.13 ? 72  LEU C CD1 1 
ATOM   4938  C  CD2 . LEU C 1 72  ? 50.446  -0.079  -27.539 1.00 24.91 ? 72  LEU C CD2 1 
ATOM   4939  N  N   . PRO C 1 73  ? 54.049  2.670   -29.047 1.00 20.58 ? 73  PRO C N   1 
ATOM   4940  C  CA  . PRO C 1 73  ? 55.197  3.452   -29.603 1.00 20.27 ? 73  PRO C CA  1 
ATOM   4941  C  C   . PRO C 1 73  ? 55.349  3.326   -31.145 1.00 22.59 ? 73  PRO C C   1 
ATOM   4942  O  O   . PRO C 1 73  ? 55.056  2.265   -31.667 1.00 24.31 ? 73  PRO C O   1 
ATOM   4943  C  CB  . PRO C 1 73  ? 56.411  2.778   -28.926 1.00 21.42 ? 73  PRO C CB  1 
ATOM   4944  C  CG  . PRO C 1 73  ? 56.048  1.289   -28.961 1.00 19.49 ? 73  PRO C CG  1 
ATOM   4945  C  CD  . PRO C 1 73  ? 54.477  1.296   -28.667 1.00 18.17 ? 73  PRO C CD  1 
ATOM   4946  N  N   . SER C 1 74  ? 55.814  4.353   -31.838 1.00 24.14 ? 74  SER C N   1 
ATOM   4947  C  CA  . SER C 1 74  ? 55.728  4.379   -33.295 1.00 25.42 ? 74  SER C CA  1 
ATOM   4948  C  C   . SER C 1 74  ? 56.488  3.323   -34.035 1.00 26.96 ? 74  SER C C   1 
ATOM   4949  O  O   . SER C 1 74  ? 56.201  3.095   -35.243 1.00 25.61 ? 74  SER C O   1 
ATOM   4950  C  CB  . SER C 1 74  ? 56.026  5.810   -33.848 1.00 28.17 ? 74  SER C CB  1 
ATOM   4951  O  OG  . SER C 1 74  ? 57.239  6.392   -33.368 1.00 30.33 ? 74  SER C OG  1 
ATOM   4952  N  N   . ASP C 1 75  ? 57.457  2.663   -33.371 1.00 24.99 ? 75  ASP C N   1 
ATOM   4953  C  CA  . ASP C 1 75  ? 58.256  1.617   -34.031 1.00 23.53 ? 75  ASP C CA  1 
ATOM   4954  C  C   . ASP C 1 75  ? 57.409  0.295   -33.999 1.00 22.82 ? 75  ASP C C   1 
ATOM   4955  O  O   . ASP C 1 75  ? 57.758  -0.718  -34.595 1.00 24.35 ? 75  ASP C O   1 
ATOM   4956  C  CB  . ASP C 1 75  ? 59.608  1.452   -33.310 1.00 24.65 ? 75  ASP C CB  1 
ATOM   4957  C  CG  . ASP C 1 75  ? 59.448  0.909   -31.901 1.00 27.69 ? 75  ASP C CG  1 
ATOM   4958  O  OD1 . ASP C 1 75  ? 59.233  1.720   -30.973 1.00 28.57 ? 75  ASP C OD1 1 
ATOM   4959  O  OD2 . ASP C 1 75  ? 59.533  -0.323  -31.721 1.00 33.50 ? 75  ASP C OD2 1 
ATOM   4960  N  N   A MET C 1 76  ? 56.260  0.330   -33.310 0.50 21.41 ? 76  MET C N   1 
ATOM   4961  N  N   B MET C 1 76  ? 56.283  0.300   -33.305 0.50 20.83 ? 76  MET C N   1 
ATOM   4962  C  CA  A MET C 1 76  ? 55.295  -0.790  -33.367 0.50 19.27 ? 76  MET C CA  1 
ATOM   4963  C  CA  B MET C 1 76  ? 55.443  -0.872  -33.445 0.50 17.46 ? 76  MET C CA  1 
ATOM   4964  C  C   A MET C 1 76  ? 54.426  -0.674  -34.671 0.50 17.81 ? 76  MET C C   1 
ATOM   4965  C  C   B MET C 1 76  ? 54.502  -0.676  -34.683 0.50 17.08 ? 76  MET C C   1 
ATOM   4966  O  O   A MET C 1 76  ? 53.896  0.407   -34.893 0.50 19.12 ? 76  MET C O   1 
ATOM   4967  O  O   B MET C 1 76  ? 53.987  0.438   -34.851 0.50 17.73 ? 76  MET C O   1 
ATOM   4968  C  CB  A MET C 1 76  ? 54.381  -0.672  -32.156 0.50 20.07 ? 76  MET C CB  1 
ATOM   4969  C  CB  B MET C 1 76  ? 54.628  -1.000  -32.199 0.50 19.05 ? 76  MET C CB  1 
ATOM   4970  C  CG  A MET C 1 76  ? 53.599  -1.916  -31.762 0.50 19.75 ? 76  MET C CG  1 
ATOM   4971  C  CG  B MET C 1 76  ? 53.294  -1.549  -32.419 0.50 14.16 ? 76  MET C CG  1 
ATOM   4972  S  SD  A MET C 1 76  ? 52.577  -1.792  -30.219 0.50 20.40 ? 76  MET C SD  1 
ATOM   4973  S  SD  B MET C 1 76  ? 52.457  -1.625  -30.838 0.50 14.58 ? 76  MET C SD  1 
ATOM   4974  C  CE  A MET C 1 76  ? 50.981  -2.334  -30.960 0.50 11.07 ? 76  MET C CE  1 
ATOM   4975  C  CE  B MET C 1 76  ? 52.519  -3.241  -30.577 0.50 4.63  ? 76  MET C CE  1 
ATOM   4976  N  N   . HIS C 1 77  ? 54.324  -1.723  -35.485 1.00 15.56 ? 77  HIS C N   1 
ATOM   4977  C  CA  . HIS C 1 77  ? 53.669  -1.579  -36.864 1.00 18.27 ? 77  HIS C CA  1 
ATOM   4978  C  C   . HIS C 1 77  ? 53.109  -2.824  -37.509 1.00 18.01 ? 77  HIS C C   1 
ATOM   4979  O  O   . HIS C 1 77  ? 53.401  -3.970  -37.229 1.00 15.79 ? 77  HIS C O   1 
ATOM   4980  C  CB  . HIS C 1 77  ? 54.538  -0.792  -37.885 1.00 19.14 ? 77  HIS C CB  1 
ATOM   4981  C  CG  . HIS C 1 77  ? 55.754  -1.539  -38.342 1.00 22.43 ? 77  HIS C CG  1 
ATOM   4982  N  ND1 . HIS C 1 77  ? 56.971  -1.448  -37.695 1.00 20.88 ? 77  HIS C ND1 1 
ATOM   4983  C  CD2 . HIS C 1 77  ? 55.975  -2.303  -39.445 1.00 23.71 ? 77  HIS C CD2 1 
ATOM   4984  C  CE1 . HIS C 1 77  ? 57.878  -2.130  -38.362 1.00 23.60 ? 77  HIS C CE1 1 
ATOM   4985  N  NE2 . HIS C 1 77  ? 57.304  -2.687  -39.416 1.00 21.86 ? 77  HIS C NE2 1 
ATOM   4986  N  N   . ILE C 1 78  ? 52.187  -2.599  -38.478 1.00 18.68 ? 78  ILE C N   1 
ATOM   4987  C  CA  . ILE C 1 78  ? 51.665  -3.665  -39.281 1.00 19.11 ? 78  ILE C CA  1 
ATOM   4988  C  C   . ILE C 1 78  ? 52.407  -3.675  -40.642 1.00 17.87 ? 78  ILE C C   1 
ATOM   4989  O  O   . ILE C 1 78  ? 52.613  -2.623  -41.252 1.00 21.60 ? 78  ILE C O   1 
ATOM   4990  C  CB  . ILE C 1 78  ? 50.082  -3.362  -39.662 1.00 20.33 ? 78  ILE C CB  1 
ATOM   4991  C  CG1 . ILE C 1 78  ? 49.158  -3.292  -38.435 1.00 21.21 ? 78  ILE C CG1 1 
ATOM   4992  C  CG2 . ILE C 1 78  ? 49.610  -4.391  -40.628 1.00 19.91 ? 78  ILE C CG2 1 
ATOM   4993  C  CD1 . ILE C 1 78  ? 47.830  -2.450  -38.615 1.00 21.33 ? 78  ILE C CD1 1 
ATOM   4994  N  N   . GLN C 1 79  ? 52.776  -4.882  -41.002 1.00 20.12 ? 79  GLN C N   1 
ATOM   4995  C  CA  . GLN C 1 79  ? 53.344  -5.271  -42.259 1.00 25.05 ? 79  GLN C CA  1 
ATOM   4996  C  C   . GLN C 1 79  ? 52.325  -6.109  -43.087 1.00 23.15 ? 79  GLN C C   1 
ATOM   4997  O  O   . GLN C 1 79  ? 51.658  -7.062  -42.619 1.00 23.50 ? 79  GLN C O   1 
ATOM   4998  C  CB  . GLN C 1 79  ? 54.556  -6.154  -41.883 1.00 26.59 ? 79  GLN C CB  1 
ATOM   4999  C  CG  . GLN C 1 79  ? 55.117  -6.992  -42.989 1.00 34.70 ? 79  GLN C CG  1 
ATOM   5000  C  CD  . GLN C 1 79  ? 55.921  -6.125  -43.914 1.00 43.91 ? 79  GLN C CD  1 
ATOM   5001  O  OE1 . GLN C 1 79  ? 55.432  -5.089  -44.416 1.00 45.43 ? 79  GLN C OE1 1 
ATOM   5002  N  NE2 . GLN C 1 79  ? 57.193  -6.504  -44.113 1.00 49.50 ? 79  GLN C NE2 1 
ATOM   5003  N  N   . GLY C 1 80  ? 52.180  -5.750  -44.342 1.00 23.87 ? 80  GLY C N   1 
ATOM   5004  C  CA  . GLY C 1 80  ? 51.326  -6.483  -45.219 1.00 23.55 ? 80  GLY C CA  1 
ATOM   5005  C  C   . GLY C 1 80  ? 50.306  -5.622  -45.923 1.00 24.23 ? 80  GLY C C   1 
ATOM   5006  O  O   . GLY C 1 80  ? 49.604  -6.138  -46.811 1.00 24.89 ? 80  GLY C O   1 
ATOM   5007  N  N   . LEU C 1 81  ? 50.177  -4.332  -45.539 1.00 23.34 ? 81  LEU C N   1 
ATOM   5008  C  CA  . LEU C 1 81  ? 49.192  -3.497  -46.199 1.00 22.39 ? 81  LEU C CA  1 
ATOM   5009  C  C   . LEU C 1 81  ? 49.942  -2.713  -47.250 1.00 24.51 ? 81  LEU C C   1 
ATOM   5010  O  O   . LEU C 1 81  ? 51.161  -2.857  -47.379 1.00 26.71 ? 81  LEU C O   1 
ATOM   5011  C  CB  . LEU C 1 81  ? 48.460  -2.542  -45.224 1.00 19.87 ? 81  LEU C CB  1 
ATOM   5012  C  CG  . LEU C 1 81  ? 47.593  -3.199  -44.154 1.00 19.34 ? 81  LEU C CG  1 
ATOM   5013  C  CD1 . LEU C 1 81  ? 47.201  -2.323  -42.915 1.00 17.77 ? 81  LEU C CD1 1 
ATOM   5014  C  CD2 . LEU C 1 81  ? 46.305  -3.719  -44.890 1.00 20.36 ? 81  LEU C CD2 1 
ATOM   5015  N  N   . GLN C 1 82  ? 49.243  -1.865  -47.971 1.00 25.23 ? 82  GLN C N   1 
ATOM   5016  C  CA  . GLN C 1 82  ? 49.879  -1.095  -49.042 1.00 26.39 ? 82  GLN C CA  1 
ATOM   5017  C  C   . GLN C 1 82  ? 50.804  0.058   -48.591 1.00 24.37 ? 82  GLN C C   1 
ATOM   5018  O  O   . GLN C 1 82  ? 51.558  0.597   -49.395 1.00 25.90 ? 82  GLN C O   1 
ATOM   5019  C  CB  . GLN C 1 82  ? 48.791  -0.616  -50.066 1.00 29.06 ? 82  GLN C CB  1 
ATOM   5020  C  CG  . GLN C 1 82  ? 48.303  -1.837  -50.955 1.00 31.10 ? 82  GLN C CG  1 
ATOM   5021  C  CD  . GLN C 1 82  ? 47.227  -1.526  -52.060 1.00 34.48 ? 82  GLN C CD  1 
ATOM   5022  O  OE1 . GLN C 1 82  ? 46.504  -2.454  -52.514 1.00 42.75 ? 82  GLN C OE1 1 
ATOM   5023  N  NE2 . GLN C 1 82  ? 47.122  -0.234  -52.497 1.00 40.76 ? 82  GLN C NE2 1 
ATOM   5024  N  N   . SER C 1 83  ? 50.761  0.458   -47.313 1.00 22.05 ? 83  SER C N   1 
ATOM   5025  C  CA  . SER C 1 83  ? 51.700  1.409   -46.711 1.00 18.94 ? 83  SER C CA  1 
ATOM   5026  C  C   . SER C 1 83  ? 52.007  0.825   -45.361 1.00 18.08 ? 83  SER C C   1 
ATOM   5027  O  O   . SER C 1 83  ? 51.301  -0.029  -44.856 1.00 14.80 ? 83  SER C O   1 
ATOM   5028  C  CB  . SER C 1 83  ? 51.059  2.715   -46.427 1.00 20.87 ? 83  SER C CB  1 
ATOM   5029  O  OG  . SER C 1 83  ? 50.715  3.347   -47.620 1.00 23.66 ? 83  SER C OG  1 
ATOM   5030  N  N   . ARG C 1 84  ? 53.093  1.293   -44.738 1.00 16.24 ? 84  ARG C N   1 
ATOM   5031  C  CA  . ARG C 1 84  ? 53.265  0.991   -43.313 1.00 14.55 ? 84  ARG C CA  1 
ATOM   5032  C  C   . ARG C 1 84  ? 52.369  1.739   -42.409 1.00 11.58 ? 84  ARG C C   1 
ATOM   5033  O  O   . ARG C 1 84  ? 52.244  2.960   -42.527 1.00 14.65 ? 84  ARG C O   1 
ATOM   5034  C  CB  . ARG C 1 84  ? 54.746  1.229   -42.897 1.00 15.12 ? 84  ARG C CB  1 
ATOM   5035  C  CG  . ARG C 1 84  ? 54.987  0.784   -41.449 1.00 19.18 ? 84  ARG C CG  1 
ATOM   5036  C  CD  . ARG C 1 84  ? 56.385  1.059   -40.946 1.00 17.65 ? 84  ARG C CD  1 
ATOM   5037  N  NE  . ARG C 1 84  ? 57.232  0.022   -41.541 1.00 15.44 ? 84  ARG C NE  1 
ATOM   5038  C  CZ  . ARG C 1 84  ? 58.558  -0.108  -41.196 1.00 21.45 ? 84  ARG C CZ  1 
ATOM   5039  N  NH1 . ARG C 1 84  ? 59.060  0.780   -40.366 1.00 21.39 ? 84  ARG C NH1 1 
ATOM   5040  N  NH2 . ARG C 1 84  ? 59.335  -1.056  -41.719 1.00 18.47 ? 84  ARG C NH2 1 
ATOM   5041  N  N   . TYR C 1 85  ? 51.719  1.015   -41.475 1.00 15.18 ? 85  TYR C N   1 
ATOM   5042  C  CA  . TYR C 1 85  ? 50.935  1.660   -40.436 1.00 14.18 ? 85  TYR C CA  1 
ATOM   5043  C  C   . TYR C 1 85  ? 51.576  1.397   -39.099 1.00 14.15 ? 85  TYR C C   1 
ATOM   5044  O  O   . TYR C 1 85  ? 51.684  0.243   -38.756 1.00 14.40 ? 85  TYR C O   1 
ATOM   5045  C  CB  . TYR C 1 85  ? 49.503  1.010   -40.548 1.00 16.26 ? 85  TYR C CB  1 
ATOM   5046  C  CG  . TYR C 1 85  ? 48.719  1.560   -41.761 1.00 11.31 ? 85  TYR C CG  1 
ATOM   5047  C  CD1 . TYR C 1 85  ? 47.936  2.681   -41.609 1.00 15.65 ? 85  TYR C CD1 1 
ATOM   5048  C  CD2 . TYR C 1 85  ? 48.795  0.922   -43.003 1.00 14.50 ? 85  TYR C CD2 1 
ATOM   5049  C  CE1 . TYR C 1 85  ? 47.234  3.189   -42.655 1.00 13.77 ? 85  TYR C CE1 1 
ATOM   5050  C  CE2 . TYR C 1 85  ? 48.036  1.440   -44.095 1.00 15.94 ? 85  TYR C CE2 1 
ATOM   5051  C  CZ  . TYR C 1 85  ? 47.291  2.564   -43.892 1.00 14.10 ? 85  TYR C CZ  1 
ATOM   5052  O  OH  . TYR C 1 85  ? 46.535  3.127   -44.968 1.00 16.60 ? 85  TYR C OH  1 
ATOM   5053  N  N   . SER C 1 86  ? 51.937  2.470   -38.429 1.00 15.47 ? 86  SER C N   1 
ATOM   5054  C  CA  . SER C 1 86  ? 52.562  2.414   -37.159 1.00 16.09 ? 86  SER C CA  1 
ATOM   5055  C  C   . SER C 1 86  ? 51.498  2.636   -36.068 1.00 17.63 ? 86  SER C C   1 
ATOM   5056  O  O   . SER C 1 86  ? 50.667  3.541   -36.132 1.00 18.61 ? 86  SER C O   1 
ATOM   5057  C  CB  . SER C 1 86  ? 53.694  3.470   -37.106 1.00 17.84 ? 86  SER C CB  1 
ATOM   5058  O  OG  . SER C 1 86  ? 54.695  3.201   -38.119 1.00 17.24 ? 86  SER C OG  1 
ATOM   5059  N  N   . ALA C 1 87  ? 51.757  1.971   -34.967 1.00 18.32 ? 87  ALA C N   1 
ATOM   5060  C  CA  . ALA C 1 87  ? 50.913  2.162   -33.768 1.00 16.41 ? 87  ALA C CA  1 
ATOM   5061  C  C   . ALA C 1 87  ? 50.876  3.530   -33.106 1.00 16.80 ? 87  ALA C C   1 
ATOM   5062  O  O   . ALA C 1 87  ? 51.917  4.279   -33.166 1.00 17.57 ? 87  ALA C O   1 
ATOM   5063  C  CB  . ALA C 1 87  ? 51.133  1.022   -32.827 1.00 16.50 ? 87  ALA C CB  1 
ATOM   5064  N  N   . THR C 1 88  ? 49.690  3.906   -32.548 1.00 16.46 ? 88  THR C N   1 
ATOM   5065  C  CA  . THR C 1 88  ? 49.525  5.187   -31.817 1.00 16.01 ? 88  THR C CA  1 
ATOM   5066  C  C   . THR C 1 88  ? 48.911  4.937   -30.447 1.00 18.57 ? 88  THR C C   1 
ATOM   5067  O  O   . THR C 1 88  ? 49.436  5.507   -29.408 1.00 15.39 ? 88  THR C O   1 
ATOM   5068  C  CB  . THR C 1 88  ? 48.936  6.303   -32.564 1.00 18.23 ? 88  THR C CB  1 
ATOM   5069  O  OG1 . THR C 1 88  ? 48.839  7.464   -31.685 1.00 18.90 ? 88  THR C OG1 1 
ATOM   5070  C  CG2 . THR C 1 88  ? 47.500  5.976   -33.096 1.00 18.18 ? 88  THR C CG2 1 
ATOM   5071  N  N   . GLN C 1 89  ? 47.894  4.054   -30.347 1.00 17.67 ? 89  GLN C N   1 
ATOM   5072  C  CA  . GLN C 1 89  ? 47.153  3.953   -29.041 1.00 17.04 ? 89  GLN C CA  1 
ATOM   5073  C  C   . GLN C 1 89  ? 46.190  2.777   -29.239 1.00 17.75 ? 89  GLN C C   1 
ATOM   5074  O  O   . GLN C 1 89  ? 45.858  2.433   -30.427 1.00 15.12 ? 89  GLN C O   1 
ATOM   5075  C  CB  . GLN C 1 89  ? 46.452  5.262   -28.665 1.00 18.64 ? 89  GLN C CB  1 
ATOM   5076  C  CG  . GLN C 1 89  ? 45.412  5.722   -29.679 1.00 18.31 ? 89  GLN C CG  1 
ATOM   5077  C  CD  . GLN C 1 89  ? 43.979  5.481   -29.161 1.00 15.61 ? 89  GLN C CD  1 
ATOM   5078  O  OE1 . GLN C 1 89  ? 43.665  4.364   -28.826 1.00 17.83 ? 89  GLN C OE1 1 
ATOM   5079  N  NE2 . GLN C 1 89  ? 43.143  6.491   -29.149 1.00 26.50 ? 89  GLN C NE2 1 
ATOM   5080  N  N   . LEU C 1 90  ? 45.860  2.083   -28.158 1.00 17.05 ? 90  LEU C N   1 
ATOM   5081  C  CA  . LEU C 1 90  ? 44.736  1.184   -28.118 1.00 14.89 ? 90  LEU C CA  1 
ATOM   5082  C  C   . LEU C 1 90  ? 43.756  1.625   -27.097 1.00 16.94 ? 90  LEU C C   1 
ATOM   5083  O  O   . LEU C 1 90  ? 44.050  2.406   -26.175 1.00 16.26 ? 90  LEU C O   1 
ATOM   5084  C  CB  . LEU C 1 90  ? 45.165  -0.227  -27.997 1.00 14.08 ? 90  LEU C CB  1 
ATOM   5085  C  CG  . LEU C 1 90  ? 45.866  -0.614  -26.637 1.00 14.88 ? 90  LEU C CG  1 
ATOM   5086  C  CD1 . LEU C 1 90  ? 44.926  -0.751  -25.386 1.00 15.46 ? 90  LEU C CD1 1 
ATOM   5087  C  CD2 . LEU C 1 90  ? 46.382  -1.990  -26.876 1.00 15.51 ? 90  LEU C CD2 1 
ATOM   5088  N  N   . HIS C 1 91  ? 42.505  1.210   -27.258 1.00 14.38 ? 91  HIS C N   1 
ATOM   5089  C  CA  . HIS C 1 91  ? 41.456  1.574   -26.317 1.00 12.97 ? 91  HIS C CA  1 
ATOM   5090  C  C   . HIS C 1 91  ? 40.313  0.487   -26.473 1.00 15.31 ? 91  HIS C C   1 
ATOM   5091  O  O   . HIS C 1 91  ? 40.377  -0.488  -27.259 1.00 17.52 ? 91  HIS C O   1 
ATOM   5092  C  CB  . HIS C 1 91  ? 40.966  3.009   -26.543 1.00 15.13 ? 91  HIS C CB  1 
ATOM   5093  C  CG  . HIS C 1 91  ? 40.371  3.154   -27.910 1.00 16.97 ? 91  HIS C CG  1 
ATOM   5094  N  ND1 . HIS C 1 91  ? 41.127  3.468   -29.027 1.00 18.47 ? 91  HIS C ND1 1 
ATOM   5095  C  CD2 . HIS C 1 91  ? 39.123  2.873   -28.322 1.00 16.25 ? 91  HIS C CD2 1 
ATOM   5096  C  CE1 . HIS C 1 91  ? 40.316  3.440   -30.081 1.00 13.61 ? 91  HIS C CE1 1 
ATOM   5097  N  NE2 . HIS C 1 91  ? 39.123  2.973   -29.697 1.00 10.78 ? 91  HIS C NE2 1 
ATOM   5098  N  N   . LEU C 1 92  ? 39.285  0.626   -25.624 1.00 16.62 ? 92  LEU C N   1 
ATOM   5099  C  CA  . LEU C 1 92  ? 38.240  -0.382  -25.631 1.00 17.07 ? 92  LEU C CA  1 
ATOM   5100  C  C   . LEU C 1 92  ? 36.881  0.314   -25.625 1.00 9.68  ? 92  LEU C C   1 
ATOM   5101  O  O   . LEU C 1 92  ? 36.702  1.536   -25.457 1.00 15.02 ? 92  LEU C O   1 
ATOM   5102  C  CB  . LEU C 1 92  ? 38.321  -1.339  -24.377 1.00 15.83 ? 92  LEU C CB  1 
ATOM   5103  C  CG  . LEU C 1 92  ? 39.550  -2.278  -24.544 1.00 18.79 ? 92  LEU C CG  1 
ATOM   5104  C  CD1 . LEU C 1 92  ? 40.663  -1.829  -23.580 1.00 23.10 ? 92  LEU C CD1 1 
ATOM   5105  C  CD2 . LEU C 1 92  ? 39.167  -3.643  -24.278 1.00 18.35 ? 92  LEU C CD2 1 
ATOM   5106  N  N   . HIS C 1 93  ? 35.909  -0.515  -26.062 1.00 15.09 ? 93  HIS C N   1 
ATOM   5107  C  CA  . HIS C 1 93  ? 34.474  -0.152  -26.041 1.00 12.08 ? 93  HIS C CA  1 
ATOM   5108  C  C   . HIS C 1 93  ? 33.660  -1.277  -25.373 1.00 11.15 ? 93  HIS C C   1 
ATOM   5109  O  O   . HIS C 1 93  ? 33.851  -2.453  -25.637 1.00 13.80 ? 93  HIS C O   1 
ATOM   5110  C  CB  . HIS C 1 93  ? 34.000  -0.008  -27.547 1.00 14.35 ? 93  HIS C CB  1 
ATOM   5111  C  CG  . HIS C 1 93  ? 34.706  1.080   -28.312 1.00 9.82  ? 93  HIS C CG  1 
ATOM   5112  N  ND1 . HIS C 1 93  ? 34.411  2.393   -28.260 1.00 12.59 ? 93  HIS C ND1 1 
ATOM   5113  C  CD2 . HIS C 1 93  ? 35.826  0.978   -29.140 1.00 11.89 ? 93  HIS C CD2 1 
ATOM   5114  C  CE1 . HIS C 1 93  ? 35.240  3.092   -29.040 1.00 12.56 ? 93  HIS C CE1 1 
ATOM   5115  N  NE2 . HIS C 1 93  ? 36.073  2.230   -29.608 1.00 10.62 ? 93  HIS C NE2 1 
ATOM   5116  N  N   . TRP C 1 94  ? 32.699  -0.822  -24.536 1.00 12.19 ? 94  TRP C N   1 
ATOM   5117  C  CA  . TRP C 1 94  ? 31.936  -1.813  -23.823 1.00 15.46 ? 94  TRP C CA  1 
ATOM   5118  C  C   . TRP C 1 94  ? 30.463  -1.306  -23.558 1.00 9.22  ? 94  TRP C C   1 
ATOM   5119  O  O   . TRP C 1 94  ? 30.132  -0.109  -23.703 1.00 13.23 ? 94  TRP C O   1 
ATOM   5120  C  CB  . TRP C 1 94  ? 32.701  -2.281  -22.470 1.00 15.90 ? 94  TRP C CB  1 
ATOM   5121  C  CG  . TRP C 1 94  ? 32.996  -1.166  -21.543 1.00 21.93 ? 94  TRP C CG  1 
ATOM   5122  C  CD1 . TRP C 1 94  ? 32.175  -0.656  -20.549 1.00 20.61 ? 94  TRP C CD1 1 
ATOM   5123  C  CD2 . TRP C 1 94  ? 34.162  -0.338  -21.542 1.00 17.31 ? 94  TRP C CD2 1 
ATOM   5124  N  NE1 . TRP C 1 94  ? 32.718  0.454   -19.964 1.00 17.39 ? 94  TRP C NE1 1 
ATOM   5125  C  CE2 . TRP C 1 94  ? 33.980  0.657   -20.489 1.00 19.67 ? 94  TRP C CE2 1 
ATOM   5126  C  CE3 . TRP C 1 94  ? 35.364  -0.321  -22.307 1.00 21.04 ? 94  TRP C CE3 1 
ATOM   5127  C  CZ2 . TRP C 1 94  ? 34.968  1.595   -20.145 1.00 19.75 ? 94  TRP C CZ2 1 
ATOM   5128  C  CZ3 . TRP C 1 94  ? 36.319  0.651   -21.956 1.00 17.47 ? 94  TRP C CZ3 1 
ATOM   5129  C  CH2 . TRP C 1 94  ? 36.103  1.604   -20.933 1.00 22.32 ? 94  TRP C CH2 1 
ATOM   5130  N  N   . GLY C 1 95  ? 29.799  -2.326  -22.931 1.00 15.55 ? 95  GLY C N   1 
ATOM   5131  C  CA  . GLY C 1 95  ? 28.416  -2.188  -22.486 1.00 16.21 ? 95  GLY C CA  1 
ATOM   5132  C  C   . GLY C 1 95  ? 28.286  -1.762  -21.009 1.00 18.31 ? 95  GLY C C   1 
ATOM   5133  O  O   . GLY C 1 95  ? 28.790  -0.723  -20.542 1.00 18.97 ? 95  GLY C O   1 
ATOM   5134  N  N   . ASN C 1 96  ? 27.413  -2.511  -20.369 1.00 20.51 ? 96  ASN C N   1 
ATOM   5135  C  CA  . ASN C 1 96  ? 27.095  -2.197  -18.916 1.00 20.49 ? 96  ASN C CA  1 
ATOM   5136  C  C   . ASN C 1 96  ? 26.621  -3.486  -18.318 1.00 20.36 ? 96  ASN C C   1 
ATOM   5137  O  O   . ASN C 1 96  ? 26.312  -4.443  -19.003 1.00 21.87 ? 96  ASN C O   1 
ATOM   5138  C  CB  . ASN C 1 96  ? 26.031  -1.168  -18.783 1.00 21.45 ? 96  ASN C CB  1 
ATOM   5139  C  CG  . ASN C 1 96  ? 24.665  -1.739  -19.099 1.00 24.13 ? 96  ASN C CG  1 
ATOM   5140  O  OD1 . ASN C 1 96  ? 24.075  -2.451  -18.272 1.00 29.30 ? 96  ASN C OD1 1 
ATOM   5141  N  ND2 . ASN C 1 96  ? 24.182  -1.501  -20.318 1.00 26.80 ? 96  ASN C ND2 1 
ATOM   5142  N  N   . PRO C 1 97  ? 26.662  -3.623  -16.951 1.00 23.56 ? 97  PRO C N   1 
ATOM   5143  C  CA  . PRO C 1 97  ? 26.315  -4.957  -16.477 1.00 22.09 ? 97  PRO C CA  1 
ATOM   5144  C  C   . PRO C 1 97  ? 24.873  -5.508  -16.691 1.00 22.46 ? 97  PRO C C   1 
ATOM   5145  O  O   . PRO C 1 97  ? 24.688  -6.753  -16.691 1.00 22.44 ? 97  PRO C O   1 
ATOM   5146  C  CB  . PRO C 1 97  ? 26.609  -4.872  -14.929 1.00 24.38 ? 97  PRO C CB  1 
ATOM   5147  C  CG  . PRO C 1 97  ? 27.600  -3.850  -14.863 1.00 22.98 ? 97  PRO C CG  1 
ATOM   5148  C  CD  . PRO C 1 97  ? 27.177  -2.753  -15.859 1.00 25.37 ? 97  PRO C CD  1 
ATOM   5149  N  N   . ASN C 1 98  ? 23.920  -4.583  -16.827 1.00 22.21 ? 98  ASN C N   1 
ATOM   5150  C  CA  . ASN C 1 98  ? 22.503  -4.931  -17.176 1.00 23.33 ? 98  ASN C CA  1 
ATOM   5151  C  C   . ASN C 1 98  ? 22.363  -5.409  -18.645 1.00 22.53 ? 98  ASN C C   1 
ATOM   5152  O  O   . ASN C 1 98  ? 21.329  -5.911  -19.027 1.00 24.07 ? 98  ASN C O   1 
ATOM   5153  C  CB  . ASN C 1 98  ? 21.597  -3.706  -16.993 1.00 21.61 ? 98  ASN C CB  1 
ATOM   5154  C  CG  . ASN C 1 98  ? 21.515  -3.260  -15.538 1.00 28.86 ? 98  ASN C CG  1 
ATOM   5155  O  OD1 . ASN C 1 98  ? 21.319  -4.089  -14.653 1.00 33.17 ? 98  ASN C OD1 1 
ATOM   5156  N  ND2 . ASN C 1 98  ? 21.678  -1.958  -15.289 1.00 33.62 ? 98  ASN C ND2 1 
ATOM   5157  N  N   . ASP C 1 99  ? 23.389  -5.207  -19.460 1.00 21.17 ? 99  ASP C N   1 
ATOM   5158  C  CA  . ASP C 1 99  ? 23.216  -5.448  -20.937 1.00 19.24 ? 99  ASP C CA  1 
ATOM   5159  C  C   . ASP C 1 99  ? 24.642  -5.517  -21.463 1.00 17.76 ? 99  ASP C C   1 
ATOM   5160  O  O   . ASP C 1 99  ? 25.092  -4.506  -22.067 1.00 20.11 ? 99  ASP C O   1 
ATOM   5161  C  CB  . ASP C 1 99  ? 22.414  -4.323  -21.581 1.00 17.79 ? 99  ASP C CB  1 
ATOM   5162  C  CG  . ASP C 1 99  ? 21.851  -4.677  -22.971 1.00 21.32 ? 99  ASP C CG  1 
ATOM   5163  O  OD1 . ASP C 1 99  ? 21.961  -5.798  -23.428 1.00 23.11 ? 99  ASP C OD1 1 
ATOM   5164  O  OD2 . ASP C 1 99  ? 21.266  -3.794  -23.594 1.00 22.05 ? 99  ASP C OD2 1 
ATOM   5165  N  N   . PRO C 1 100 ? 25.292  -6.599  -21.174 1.00 18.89 ? 100 PRO C N   1 
ATOM   5166  C  CA  . PRO C 1 100 ? 26.759  -6.673  -21.323 1.00 19.03 ? 100 PRO C CA  1 
ATOM   5167  C  C   . PRO C 1 100 ? 27.098  -7.016  -22.797 1.00 18.57 ? 100 PRO C C   1 
ATOM   5168  O  O   . PRO C 1 100 ? 27.671  -8.059  -23.096 1.00 18.81 ? 100 PRO C O   1 
ATOM   5169  C  CB  . PRO C 1 100 ? 27.146  -7.809  -20.375 1.00 19.83 ? 100 PRO C CB  1 
ATOM   5170  C  CG  . PRO C 1 100 ? 26.030  -8.735  -20.404 1.00 21.14 ? 100 PRO C CG  1 
ATOM   5171  C  CD  . PRO C 1 100 ? 24.814  -7.810  -20.454 1.00 18.78 ? 100 PRO C CD  1 
ATOM   5172  N  N   . HIS C 1 101 ? 26.664  -6.090  -23.710 1.00 16.52 ? 101 HIS C N   1 
ATOM   5173  C  CA  . HIS C 1 101 ? 26.805  -6.345  -25.172 1.00 16.64 ? 101 HIS C CA  1 
ATOM   5174  C  C   . HIS C 1 101 ? 27.185  -5.047  -25.884 1.00 18.66 ? 101 HIS C C   1 
ATOM   5175  O  O   . HIS C 1 101 ? 26.390  -4.565  -26.687 1.00 18.91 ? 101 HIS C O   1 
ATOM   5176  C  CB  . HIS C 1 101 ? 25.479  -6.855  -25.759 1.00 18.32 ? 101 HIS C CB  1 
ATOM   5177  C  CG  . HIS C 1 101 ? 24.931  -8.025  -25.023 1.00 20.04 ? 101 HIS C CG  1 
ATOM   5178  N  ND1 . HIS C 1 101 ? 25.450  -9.300  -25.137 1.00 19.56 ? 101 HIS C ND1 1 
ATOM   5179  C  CD2 . HIS C 1 101 ? 23.988  -8.071  -24.045 1.00 20.06 ? 101 HIS C CD2 1 
ATOM   5180  C  CE1 . HIS C 1 101 ? 24.822  -10.103 -24.287 1.00 20.99 ? 101 HIS C CE1 1 
ATOM   5181  N  NE2 . HIS C 1 101 ? 23.929  -9.382  -23.631 1.00 19.95 ? 101 HIS C NE2 1 
ATOM   5182  N  N   . GLY C 1 102 ? 28.414  -4.579  -25.694 1.00 12.92 ? 102 GLY C N   1 
ATOM   5183  C  CA  . GLY C 1 102 ? 28.865  -3.272  -26.158 1.00 13.09 ? 102 GLY C CA  1 
ATOM   5184  C  C   . GLY C 1 102 ? 30.096  -3.219  -27.087 1.00 11.05 ? 102 GLY C C   1 
ATOM   5185  O  O   . GLY C 1 102 ? 30.707  -2.146  -27.171 1.00 12.58 ? 102 GLY C O   1 
ATOM   5186  N  N   . SER C 1 103 ? 30.158  -4.252  -27.916 1.00 13.24 ? 103 SER C N   1 
ATOM   5187  C  CA  . SER C 1 103 ? 31.038  -4.119  -29.119 1.00 12.28 ? 103 SER C CA  1 
ATOM   5188  C  C   . SER C 1 103 ? 30.454  -3.103  -30.078 1.00 13.23 ? 103 SER C C   1 
ATOM   5189  O  O   . SER C 1 103 ? 29.245  -2.740  -29.979 1.00 12.11 ? 103 SER C O   1 
ATOM   5190  C  CB  . SER C 1 103 ? 31.155  -5.424  -29.890 1.00 12.65 ? 103 SER C CB  1 
ATOM   5191  O  OG  . SER C 1 103 ? 29.914  -5.862  -30.518 1.00 11.74 ? 103 SER C OG  1 
ATOM   5192  N  N   . GLU C 1 104 ? 31.333  -2.529  -30.896 1.00 10.09 ? 104 GLU C N   1 
ATOM   5193  C  CA  . GLU C 1 104 ? 30.896  -1.634  -31.909 1.00 10.33 ? 104 GLU C CA  1 
ATOM   5194  C  C   . GLU C 1 104 ? 30.405  -2.322  -33.200 1.00 10.24 ? 104 GLU C C   1 
ATOM   5195  O  O   . GLU C 1 104 ? 29.262  -2.099  -33.633 1.00 8.69  ? 104 GLU C O   1 
ATOM   5196  C  CB  . GLU C 1 104 ? 32.005  -0.665  -32.232 1.00 9.34  ? 104 GLU C CB  1 
ATOM   5197  C  CG  . GLU C 1 104 ? 32.614  0.093   -30.990 1.00 10.87 ? 104 GLU C CG  1 
ATOM   5198  C  CD  . GLU C 1 104 ? 32.888  1.502   -31.299 1.00 11.64 ? 104 GLU C CD  1 
ATOM   5199  O  OE1 . GLU C 1 104 ? 33.963  1.685   -31.910 1.00 11.92 ? 104 GLU C OE1 1 
ATOM   5200  O  OE2 . GLU C 1 104 ? 32.156  2.438   -31.087 1.00 12.32 ? 104 GLU C OE2 1 
ATOM   5201  N  N   . HIS C 1 105 ? 31.251  -3.124  -33.791 1.00 9.50  ? 105 HIS C N   1 
ATOM   5202  C  CA  . HIS C 1 105 ? 30.772  -3.983  -34.943 1.00 8.66  ? 105 HIS C CA  1 
ATOM   5203  C  C   . HIS C 1 105 ? 29.848  -5.084  -34.392 1.00 9.17  ? 105 HIS C C   1 
ATOM   5204  O  O   . HIS C 1 105 ? 30.009  -5.557  -33.219 1.00 10.39 ? 105 HIS C O   1 
ATOM   5205  C  CB  . HIS C 1 105 ? 31.948  -4.595  -35.702 1.00 10.12 ? 105 HIS C CB  1 
ATOM   5206  C  CG  . HIS C 1 105 ? 32.731  -3.536  -36.405 1.00 10.01 ? 105 HIS C CG  1 
ATOM   5207  N  ND1 . HIS C 1 105 ? 33.801  -2.902  -35.793 1.00 10.90 ? 105 HIS C ND1 1 
ATOM   5208  C  CD2 . HIS C 1 105 ? 32.572  -2.987  -37.647 1.00 8.23  ? 105 HIS C CD2 1 
ATOM   5209  C  CE1 . HIS C 1 105 ? 34.263  -1.993  -36.643 1.00 8.46  ? 105 HIS C CE1 1 
ATOM   5210  N  NE2 . HIS C 1 105 ? 33.541  -2.058  -37.779 1.00 9.48  ? 105 HIS C NE2 1 
ATOM   5211  N  N   . THR C 1 106 ? 28.894  -5.497  -35.206 1.00 7.53  ? 106 THR C N   1 
ATOM   5212  C  CA  . THR C 1 106 ? 28.046  -6.650  -34.894 1.00 9.49  ? 106 THR C CA  1 
ATOM   5213  C  C   . THR C 1 106 ? 28.210  -7.694  -35.992 1.00 8.72  ? 106 THR C C   1 
ATOM   5214  O  O   . THR C 1 106 ? 28.680  -7.399  -37.115 1.00 8.87  ? 106 THR C O   1 
ATOM   5215  C  CB  . THR C 1 106 ? 26.551  -6.211  -34.789 1.00 10.43 ? 106 THR C CB  1 
ATOM   5216  O  OG1 . THR C 1 106 ? 26.124  -5.588  -36.012 1.00 9.90  ? 106 THR C OG1 1 
ATOM   5217  C  CG2 . THR C 1 106 ? 26.379  -5.248  -33.621 1.00 10.72 ? 106 THR C CG2 1 
ATOM   5218  N  N   . VAL C 1 107 ? 27.928  -8.979  -35.667 1.00 9.80  ? 107 VAL C N   1 
ATOM   5219  C  CA  . VAL C 1 107 ? 27.991  -9.986  -36.656 1.00 12.22 ? 107 VAL C CA  1 
ATOM   5220  C  C   . VAL C 1 107 ? 26.579  -10.632 -36.788 1.00 12.32 ? 107 VAL C C   1 
ATOM   5221  O  O   . VAL C 1 107 ? 26.029  -11.128 -35.777 1.00 12.74 ? 107 VAL C O   1 
ATOM   5222  C  CB  . VAL C 1 107 ? 29.012  -11.074 -36.286 1.00 13.00 ? 107 VAL C CB  1 
ATOM   5223  C  CG1 . VAL C 1 107 ? 28.980  -12.148 -37.275 1.00 13.74 ? 107 VAL C CG1 1 
ATOM   5224  C  CG2 . VAL C 1 107 ? 30.478  -10.400 -36.134 1.00 13.88 ? 107 VAL C CG2 1 
ATOM   5225  N  N   . SER C 1 108 ? 25.979  -10.584 -37.975 1.00 10.84 ? 108 SER C N   1 
ATOM   5226  C  CA  . SER C 1 108 ? 24.607  -11.065 -38.175 1.00 12.72 ? 108 SER C CA  1 
ATOM   5227  C  C   . SER C 1 108 ? 23.689  -10.457 -37.091 1.00 12.02 ? 108 SER C C   1 
ATOM   5228  O  O   . SER C 1 108 ? 22.790  -11.138 -36.480 1.00 14.03 ? 108 SER C O   1 
ATOM   5229  C  CB  . SER C 1 108 ? 24.558  -12.608 -38.108 1.00 12.84 ? 108 SER C CB  1 
ATOM   5230  O  OG  . SER C 1 108 ? 25.435  -13.172 -39.078 1.00 19.39 ? 108 SER C OG  1 
ATOM   5231  N  N   . GLY C 1 109 ? 23.873  -9.173  -36.884 1.00 10.34 ? 109 GLY C N   1 
ATOM   5232  C  CA  . GLY C 1 109 ? 23.000  -8.508  -35.949 1.00 11.06 ? 109 GLY C CA  1 
ATOM   5233  C  C   . GLY C 1 109 ? 23.369  -8.525  -34.497 1.00 13.65 ? 109 GLY C C   1 
ATOM   5234  O  O   . GLY C 1 109 ? 22.738  -7.795  -33.690 1.00 14.87 ? 109 GLY C O   1 
ATOM   5235  N  N   . GLN C 1 110 ? 24.349  -9.347  -34.123 1.00 12.26 ? 110 GLN C N   1 
ATOM   5236  C  CA  . GLN C 1 110 ? 24.619  -9.599  -32.710 1.00 12.73 ? 110 GLN C CA  1 
ATOM   5237  C  C   . GLN C 1 110 ? 25.860  -8.855  -32.211 1.00 11.87 ? 110 GLN C C   1 
ATOM   5238  O  O   . GLN C 1 110 ? 26.907  -8.830  -32.878 1.00 11.71 ? 110 GLN C O   1 
ATOM   5239  C  CB  . GLN C 1 110 ? 24.850  -11.112 -32.537 1.00 14.71 ? 110 GLN C CB  1 
ATOM   5240  C  CG  . GLN C 1 110 ? 23.736  -12.028 -33.079 1.00 15.82 ? 110 GLN C CG  1 
ATOM   5241  C  CD  . GLN C 1 110 ? 22.332  -11.546 -32.603 1.00 14.24 ? 110 GLN C CD  1 
ATOM   5242  O  OE1 . GLN C 1 110 ? 22.081  -11.462 -31.450 1.00 17.20 ? 110 GLN C OE1 1 
ATOM   5243  N  NE2 . GLN C 1 110 ? 21.462  -11.177 -33.573 1.00 21.30 ? 110 GLN C NE2 1 
ATOM   5244  N  N   . HIS C 1 111 ? 25.698  -8.087  -31.125 1.00 13.58 ? 111 HIS C N   1 
ATOM   5245  C  CA  . HIS C 1 111 ? 26.868  -7.521  -30.443 1.00 12.89 ? 111 HIS C CA  1 
ATOM   5246  C  C   . HIS C 1 111 ? 27.664  -8.576  -29.702 1.00 15.58 ? 111 HIS C C   1 
ATOM   5247  O  O   . HIS C 1 111 ? 27.132  -9.604  -29.332 1.00 17.80 ? 111 HIS C O   1 
ATOM   5248  C  CB  . HIS C 1 111 ? 26.513  -6.471  -29.370 1.00 14.48 ? 111 HIS C CB  1 
ATOM   5249  C  CG  . HIS C 1 111 ? 25.985  -5.214  -29.918 1.00 12.56 ? 111 HIS C CG  1 
ATOM   5250  N  ND1 . HIS C 1 111 ? 26.761  -4.066  -30.064 1.00 14.04 ? 111 HIS C ND1 1 
ATOM   5251  C  CD2 . HIS C 1 111 ? 24.751  -4.910  -30.404 1.00 12.88 ? 111 HIS C CD2 1 
ATOM   5252  C  CE1 . HIS C 1 111 ? 26.003  -3.113  -30.590 1.00 14.03 ? 111 HIS C CE1 1 
ATOM   5253  N  NE2 . HIS C 1 111 ? 24.751  -3.577  -30.724 1.00 16.87 ? 111 HIS C NE2 1 
ATOM   5254  N  N   . PHE C 1 112 ? 28.944  -8.326  -29.592 1.00 13.75 ? 112 PHE C N   1 
ATOM   5255  C  CA  . PHE C 1 112 ? 29.799  -9.054  -28.666 1.00 15.13 ? 112 PHE C CA  1 
ATOM   5256  C  C   . PHE C 1 112 ? 29.837  -8.273  -27.386 1.00 14.58 ? 112 PHE C C   1 
ATOM   5257  O  O   . PHE C 1 112 ? 29.353  -7.087  -27.281 1.00 13.71 ? 112 PHE C O   1 
ATOM   5258  C  CB  . PHE C 1 112 ? 31.180  -9.287  -29.266 1.00 16.10 ? 112 PHE C CB  1 
ATOM   5259  C  CG  . PHE C 1 112 ? 31.182  -10.373 -30.220 1.00 14.19 ? 112 PHE C CG  1 
ATOM   5260  C  CD1 . PHE C 1 112 ? 31.571  -11.677 -29.872 1.00 18.04 ? 112 PHE C CD1 1 
ATOM   5261  C  CD2 . PHE C 1 112 ? 30.564  -10.248 -31.532 1.00 15.54 ? 112 PHE C CD2 1 
ATOM   5262  C  CE1 . PHE C 1 112 ? 31.546  -12.756 -30.779 1.00 18.70 ? 112 PHE C CE1 1 
ATOM   5263  C  CE2 . PHE C 1 112 ? 30.520  -11.335 -32.472 1.00 22.12 ? 112 PHE C CE2 1 
ATOM   5264  C  CZ  . PHE C 1 112 ? 30.969  -12.629 -32.083 1.00 22.24 ? 112 PHE C CZ  1 
ATOM   5265  N  N   . ALA C 1 113 ? 30.402  -8.863  -26.275 1.00 16.22 ? 113 ALA C N   1 
ATOM   5266  C  CA  . ALA C 1 113 ? 30.540  -8.050  -25.103 1.00 14.02 ? 113 ALA C CA  1 
ATOM   5267  C  C   . ALA C 1 113 ? 31.238  -6.722  -25.061 1.00 13.00 ? 113 ALA C C   1 
ATOM   5268  O  O   . ALA C 1 113 ? 30.845  -5.809  -24.418 1.00 16.24 ? 113 ALA C O   1 
ATOM   5269  C  CB  . ALA C 1 113 ? 31.082  -8.911  -23.921 1.00 16.58 ? 113 ALA C CB  1 
ATOM   5270  N  N   . ALA C 1 114 ? 32.368  -6.663  -25.813 1.00 13.06 ? 114 ALA C N   1 
ATOM   5271  C  CA  . ALA C 1 114 ? 33.199  -5.503  -25.893 1.00 12.46 ? 114 ALA C CA  1 
ATOM   5272  C  C   . ALA C 1 114 ? 34.066  -5.701  -27.183 1.00 10.64 ? 114 ALA C C   1 
ATOM   5273  O  O   . ALA C 1 114 ? 33.979  -6.665  -27.820 1.00 12.77 ? 114 ALA C O   1 
ATOM   5274  C  CB  . ALA C 1 114 ? 34.177  -5.578  -24.652 1.00 14.98 ? 114 ALA C CB  1 
ATOM   5275  N  N   . GLU C 1 115 ? 34.821  -4.659  -27.431 1.00 13.03 ? 115 GLU C N   1 
ATOM   5276  C  CA  . GLU C 1 115 ? 35.672  -4.697  -28.576 1.00 13.83 ? 115 GLU C CA  1 
ATOM   5277  C  C   . GLU C 1 115 ? 36.967  -3.804  -28.196 1.00 10.21 ? 115 GLU C C   1 
ATOM   5278  O  O   . GLU C 1 115 ? 36.934  -2.614  -27.657 1.00 13.10 ? 115 GLU C O   1 
ATOM   5279  C  CB  . GLU C 1 115 ? 34.909  -3.968  -29.721 1.00 12.80 ? 115 GLU C CB  1 
ATOM   5280  C  CG  . GLU C 1 115 ? 35.618  -4.025  -31.128 1.00 12.83 ? 115 GLU C CG  1 
ATOM   5281  C  CD  . GLU C 1 115 ? 34.633  -3.727  -32.268 1.00 10.99 ? 115 GLU C CD  1 
ATOM   5282  O  OE1 . GLU C 1 115 ? 35.121  -3.226  -33.278 1.00 10.75 ? 115 GLU C OE1 1 
ATOM   5283  O  OE2 . GLU C 1 115 ? 33.426  -4.015  -32.121 1.00 11.76 ? 115 GLU C OE2 1 
ATOM   5284  N  N   . LEU C 1 116 ? 38.089  -4.375  -28.660 1.00 13.18 ? 116 LEU C N   1 
ATOM   5285  C  CA  . LEU C 1 116 ? 39.352  -3.656  -28.546 1.00 14.12 ? 116 LEU C CA  1 
ATOM   5286  C  C   . LEU C 1 116 ? 39.807  -3.072  -29.930 1.00 10.22 ? 116 LEU C C   1 
ATOM   5287  O  O   . LEU C 1 116 ? 39.653  -3.892  -30.934 1.00 15.36 ? 116 LEU C O   1 
ATOM   5288  C  CB  . LEU C 1 116 ? 40.381  -4.703  -28.174 1.00 16.90 ? 116 LEU C CB  1 
ATOM   5289  C  CG  . LEU C 1 116 ? 41.861  -4.247  -28.197 1.00 14.74 ? 116 LEU C CG  1 
ATOM   5290  C  CD1 . LEU C 1 116 ? 42.207  -3.249  -27.034 1.00 16.26 ? 116 LEU C CD1 1 
ATOM   5291  C  CD2 . LEU C 1 116 ? 42.791  -5.488  -28.402 1.00 19.37 ? 116 LEU C CD2 1 
ATOM   5292  N  N   . HIS C 1 117 ? 40.299  -1.798  -29.915 1.00 14.11 ? 117 HIS C N   1 
ATOM   5293  C  CA  . HIS C 1 117 ? 40.713  -1.073  -31.195 1.00 10.92 ? 117 HIS C CA  1 
ATOM   5294  C  C   . HIS C 1 117 ? 42.240  -0.873  -30.964 1.00 14.09 ? 117 HIS C C   1 
ATOM   5295  O  O   . HIS C 1 117 ? 42.603  -0.160  -30.013 1.00 14.40 ? 117 HIS C O   1 
ATOM   5296  C  CB  . HIS C 1 117 ? 39.922  0.164   -31.383 1.00 13.09 ? 117 HIS C CB  1 
ATOM   5297  C  CG  . HIS C 1 117 ? 38.572  -0.186  -31.857 1.00 8.88  ? 117 HIS C CG  1 
ATOM   5298  N  ND1 . HIS C 1 117 ? 37.541  0.665   -31.733 1.00 16.25 ? 117 HIS C ND1 1 
ATOM   5299  C  CD2 . HIS C 1 117 ? 38.154  -1.395  -32.380 1.00 10.32 ? 117 HIS C CD2 1 
ATOM   5300  C  CE1 . HIS C 1 117 ? 36.467  0.028   -32.259 1.00 9.97  ? 117 HIS C CE1 1 
ATOM   5301  N  NE2 . HIS C 1 117 ? 36.804  -1.178  -32.709 1.00 10.79 ? 117 HIS C NE2 1 
ATOM   5302  N  N   . ILE C 1 118 ? 43.053  -1.338  -31.897 1.00 13.60 ? 118 ILE C N   1 
ATOM   5303  C  CA  . ILE C 1 118 ? 44.503  -0.945  -31.961 1.00 15.99 ? 118 ILE C CA  1 
ATOM   5304  C  C   . ILE C 1 118 ? 44.748  -0.016  -33.102 1.00 11.73 ? 118 ILE C C   1 
ATOM   5305  O  O   . ILE C 1 118 ? 44.632  -0.475  -34.325 1.00 12.40 ? 118 ILE C O   1 
ATOM   5306  C  CB  . ILE C 1 118 ? 45.348  -2.128  -32.065 1.00 16.41 ? 118 ILE C CB  1 
ATOM   5307  C  CG1 . ILE C 1 118 ? 45.001  -3.184  -31.048 1.00 19.29 ? 118 ILE C CG1 1 
ATOM   5308  C  CG2 . ILE C 1 118 ? 46.876  -1.696  -31.856 1.00 16.38 ? 118 ILE C CG2 1 
ATOM   5309  C  CD1 . ILE C 1 118 ? 45.786  -4.406  -31.043 1.00 20.49 ? 118 ILE C CD1 1 
ATOM   5310  N  N   . VAL C 1 119 ? 44.929  1.238   -32.842 1.00 13.75 ? 119 VAL C N   1 
ATOM   5311  C  CA  . VAL C 1 119 ? 44.890  2.357   -33.792 1.00 12.98 ? 119 VAL C CA  1 
ATOM   5312  C  C   . VAL C 1 119 ? 46.303  2.569   -34.293 1.00 17.39 ? 119 VAL C C   1 
ATOM   5313  O  O   . VAL C 1 119 ? 47.289  2.747   -33.563 1.00 15.11 ? 119 VAL C O   1 
ATOM   5314  C  CB  . VAL C 1 119 ? 44.390  3.627   -33.237 1.00 13.54 ? 119 VAL C CB  1 
ATOM   5315  C  CG1 . VAL C 1 119 ? 44.240  4.720   -34.307 1.00 14.00 ? 119 VAL C CG1 1 
ATOM   5316  C  CG2 . VAL C 1 119 ? 43.014  3.332   -32.454 1.00 16.97 ? 119 VAL C CG2 1 
ATOM   5317  N  N   . HIS C 1 120 ? 46.398  2.463   -35.608 1.00 14.93 ? 120 HIS C N   1 
ATOM   5318  C  CA  . HIS C 1 120 ? 47.693  2.759   -36.355 1.00 16.09 ? 120 HIS C CA  1 
ATOM   5319  C  C   . HIS C 1 120 ? 47.539  3.900   -37.358 1.00 16.87 ? 120 HIS C C   1 
ATOM   5320  O  O   . HIS C 1 120 ? 46.434  4.207   -37.810 1.00 13.13 ? 120 HIS C O   1 
ATOM   5321  C  CB  . HIS C 1 120 ? 48.197  1.555   -37.142 1.00 16.72 ? 120 HIS C CB  1 
ATOM   5322  C  CG  . HIS C 1 120 ? 48.360  0.281   -36.385 1.00 13.29 ? 120 HIS C CG  1 
ATOM   5323  N  ND1 . HIS C 1 120 ? 47.289  -0.362  -35.775 1.00 12.85 ? 120 HIS C ND1 1 
ATOM   5324  C  CD2 . HIS C 1 120 ? 49.466  -0.477  -36.114 1.00 18.11 ? 120 HIS C CD2 1 
ATOM   5325  C  CE1 . HIS C 1 120 ? 47.703  -1.518  -35.270 1.00 12.40 ? 120 HIS C CE1 1 
ATOM   5326  N  NE2 . HIS C 1 120 ? 49.040  -1.609  -35.432 1.00 15.35 ? 120 HIS C NE2 1 
ATOM   5327  N  N   . TYR C 1 121 ? 48.648  4.541   -37.750 1.00 14.21 ? 121 TYR C N   1 
ATOM   5328  C  CA  . TYR C 1 121 ? 48.560  5.640   -38.669 1.00 15.54 ? 121 TYR C CA  1 
ATOM   5329  C  C   . TYR C 1 121 ? 49.548  5.318   -39.793 1.00 15.89 ? 121 TYR C C   1 
ATOM   5330  O  O   . TYR C 1 121 ? 50.536  4.592   -39.561 1.00 14.59 ? 121 TYR C O   1 
ATOM   5331  C  CB  . TYR C 1 121 ? 48.831  7.047   -38.005 1.00 16.95 ? 121 TYR C CB  1 
ATOM   5332  C  CG  . TYR C 1 121 ? 50.273  7.268   -37.502 1.00 16.89 ? 121 TYR C CG  1 
ATOM   5333  C  CD1 . TYR C 1 121 ? 51.142  8.062   -38.244 1.00 16.82 ? 121 TYR C CD1 1 
ATOM   5334  C  CD2 . TYR C 1 121 ? 50.700  6.724   -36.239 1.00 15.34 ? 121 TYR C CD2 1 
ATOM   5335  C  CE1 . TYR C 1 121 ? 52.532  8.213   -37.791 1.00 16.41 ? 121 TYR C CE1 1 
ATOM   5336  C  CE2 . TYR C 1 121 ? 52.024  6.880   -35.765 1.00 18.19 ? 121 TYR C CE2 1 
ATOM   5337  C  CZ  . TYR C 1 121 ? 52.904  7.611   -36.584 1.00 20.47 ? 121 TYR C CZ  1 
ATOM   5338  O  OH  . TYR C 1 121 ? 54.240  7.839   -36.160 1.00 19.18 ? 121 TYR C OH  1 
ATOM   5339  N  N   . ASN C 1 122 ? 49.318  5.981   -40.920 1.00 15.23 ? 122 ASN C N   1 
ATOM   5340  C  CA  . ASN C 1 122 ? 50.158  5.760   -42.108 1.00 15.14 ? 122 ASN C CA  1 
ATOM   5341  C  C   . ASN C 1 122 ? 51.428  6.591   -41.967 1.00 12.39 ? 122 ASN C C   1 
ATOM   5342  O  O   . ASN C 1 122 ? 51.406  7.795   -42.224 1.00 16.68 ? 122 ASN C O   1 
ATOM   5343  C  CB  . ASN C 1 122 ? 49.421  6.221   -43.335 1.00 15.32 ? 122 ASN C CB  1 
ATOM   5344  C  CG  . ASN C 1 122 ? 50.054  5.784   -44.591 1.00 17.10 ? 122 ASN C CG  1 
ATOM   5345  O  OD1 . ASN C 1 122 ? 51.300  5.659   -44.662 1.00 16.43 ? 122 ASN C OD1 1 
ATOM   5346  N  ND2 . ASN C 1 122 ? 49.213  5.462   -45.614 1.00 17.73 ? 122 ASN C ND2 1 
ATOM   5347  N  N   . SER C 1 123 ? 52.462  5.935   -41.509 1.00 15.37 ? 123 SER C N   1 
ATOM   5348  C  CA  . SER C 1 123 ? 53.705  6.666   -41.185 1.00 15.37 ? 123 SER C CA  1 
ATOM   5349  C  C   . SER C 1 123 ? 54.532  6.874   -42.434 1.00 17.97 ? 123 SER C C   1 
ATOM   5350  O  O   . SER C 1 123 ? 55.467  7.702   -42.423 1.00 18.31 ? 123 SER C O   1 
ATOM   5351  C  CB  . SER C 1 123 ? 54.447  5.933   -40.102 1.00 17.21 ? 123 SER C CB  1 
ATOM   5352  O  OG  . SER C 1 123 ? 54.590  4.552   -40.294 1.00 16.23 ? 123 SER C OG  1 
ATOM   5353  N  N   . ASP C 1 124 ? 54.242  6.152   -43.496 1.00 16.66 ? 124 ASP C N   1 
ATOM   5354  C  CA  . ASP C 1 124 ? 54.828  6.440   -44.813 1.00 15.47 ? 124 ASP C CA  1 
ATOM   5355  C  C   . ASP C 1 124 ? 54.417  7.781   -45.382 1.00 18.76 ? 124 ASP C C   1 
ATOM   5356  O  O   . ASP C 1 124 ? 55.158  8.351   -46.148 1.00 21.41 ? 124 ASP C O   1 
ATOM   5357  C  CB  . ASP C 1 124 ? 54.513  5.325   -45.795 1.00 14.69 ? 124 ASP C CB  1 
ATOM   5358  C  CG  . ASP C 1 124 ? 55.257  4.066   -45.516 1.00 20.53 ? 124 ASP C CG  1 
ATOM   5359  O  OD1 . ASP C 1 124 ? 56.317  4.095   -44.786 1.00 19.74 ? 124 ASP C OD1 1 
ATOM   5360  O  OD2 . ASP C 1 124 ? 54.864  2.995   -46.001 1.00 16.41 ? 124 ASP C OD2 1 
ATOM   5361  N  N   A LEU C 1 125 ? 53.217  8.277   -45.077 0.50 14.91 ? 125 LEU C N   1 
ATOM   5362  N  N   B LEU C 1 125 ? 53.226  8.244   -45.056 0.50 13.58 ? 125 LEU C N   1 
ATOM   5363  C  CA  A LEU C 1 125 ? 52.726  9.563   -45.652 0.50 18.06 ? 125 LEU C CA  1 
ATOM   5364  C  CA  B LEU C 1 125 ? 52.720  9.475   -45.627 0.50 16.07 ? 125 LEU C CA  1 
ATOM   5365  C  C   A LEU C 1 125 ? 52.606  10.653  -44.595 0.50 17.76 ? 125 LEU C C   1 
ATOM   5366  C  C   B LEU C 1 125 ? 52.798  10.592  -44.601 0.50 16.53 ? 125 LEU C C   1 
ATOM   5367  O  O   A LEU C 1 125 ? 52.478  11.886  -44.944 0.50 18.80 ? 125 LEU C O   1 
ATOM   5368  O  O   B LEU C 1 125 ? 53.004  11.776  -44.992 0.50 18.40 ? 125 LEU C O   1 
ATOM   5369  C  CB  A LEU C 1 125 ? 51.339  9.382   -46.322 0.50 17.92 ? 125 LEU C CB  1 
ATOM   5370  C  CB  B LEU C 1 125 ? 51.261  9.259   -46.078 0.50 15.88 ? 125 LEU C CB  1 
ATOM   5371  C  CG  A LEU C 1 125 ? 51.242  8.822   -47.747 0.50 20.46 ? 125 LEU C CG  1 
ATOM   5372  C  CG  B LEU C 1 125 ? 50.981  8.281   -47.222 0.50 10.05 ? 125 LEU C CG  1 
ATOM   5373  C  CD1 A LEU C 1 125 ? 52.113  7.642   -47.933 0.50 19.03 ? 125 LEU C CD1 1 
ATOM   5374  C  CD1 B LEU C 1 125 ? 49.430  8.277   -47.449 0.50 13.54 ? 125 LEU C CD1 1 
ATOM   5375  C  CD2 A LEU C 1 125 ? 49.797  8.461   -48.186 0.50 19.38 ? 125 LEU C CD2 1 
ATOM   5376  C  CD2 B LEU C 1 125 ? 51.816  8.817   -48.483 0.50 13.23 ? 125 LEU C CD2 1 
ATOM   5377  N  N   . TYR C 1 126 ? 52.589  10.257  -43.318 1.00 16.73 ? 126 TYR C N   1 
ATOM   5378  C  CA  . TYR C 1 126 ? 52.300  11.272  -42.281 1.00 17.03 ? 126 TYR C CA  1 
ATOM   5379  C  C   . TYR C 1 126 ? 53.209  11.151  -41.038 1.00 18.93 ? 126 TYR C C   1 
ATOM   5380  O  O   . TYR C 1 126 ? 53.605  10.038  -40.699 1.00 16.98 ? 126 TYR C O   1 
ATOM   5381  C  CB  . TYR C 1 126 ? 50.794  11.222  -41.866 1.00 16.28 ? 126 TYR C CB  1 
ATOM   5382  C  CG  . TYR C 1 126 ? 49.860  11.242  -43.067 1.00 17.68 ? 126 TYR C CG  1 
ATOM   5383  C  CD1 . TYR C 1 126 ? 49.804  12.360  -43.956 1.00 18.58 ? 126 TYR C CD1 1 
ATOM   5384  C  CD2 . TYR C 1 126 ? 48.972  10.153  -43.328 1.00 19.17 ? 126 TYR C CD2 1 
ATOM   5385  C  CE1 . TYR C 1 126 ? 48.966  12.381  -45.050 1.00 17.50 ? 126 TYR C CE1 1 
ATOM   5386  C  CE2 . TYR C 1 126 ? 48.168  10.156  -44.446 1.00 20.39 ? 126 TYR C CE2 1 
ATOM   5387  C  CZ  . TYR C 1 126 ? 48.151  11.247  -45.282 1.00 19.71 ? 126 TYR C CZ  1 
ATOM   5388  O  OH  . TYR C 1 126 ? 47.342  11.345  -46.371 1.00 19.57 ? 126 TYR C OH  1 
ATOM   5389  N  N   . PRO C 1 127 ? 53.516  12.322  -40.347 1.00 18.34 ? 127 PRO C N   1 
ATOM   5390  C  CA  . PRO C 1 127 ? 54.444  12.315  -39.215 1.00 21.97 ? 127 PRO C CA  1 
ATOM   5391  C  C   . PRO C 1 127 ? 53.899  11.778  -37.954 1.00 21.80 ? 127 PRO C C   1 
ATOM   5392  O  O   . PRO C 1 127 ? 54.671  11.301  -37.084 1.00 22.30 ? 127 PRO C O   1 
ATOM   5393  C  CB  . PRO C 1 127 ? 54.733  13.819  -38.967 1.00 21.15 ? 127 PRO C CB  1 
ATOM   5394  C  CG  . PRO C 1 127 ? 53.745  14.608  -39.733 1.00 21.88 ? 127 PRO C CG  1 
ATOM   5395  C  CD  . PRO C 1 127 ? 53.199  13.687  -40.817 1.00 21.17 ? 127 PRO C CD  1 
ATOM   5396  N  N   . ASP C 1 128 ? 52.560  11.816  -37.808 1.00 20.35 ? 128 ASP C N   1 
ATOM   5397  C  CA  . ASP C 1 128 ? 52.008  11.373  -36.520 1.00 20.87 ? 128 ASP C CA  1 
ATOM   5398  C  C   . ASP C 1 128 ? 50.536  11.002  -36.738 1.00 20.54 ? 128 ASP C C   1 
ATOM   5399  O  O   . ASP C 1 128 ? 49.934  11.415  -37.762 1.00 19.00 ? 128 ASP C O   1 
ATOM   5400  C  CB  . ASP C 1 128 ? 52.128  12.479  -35.363 1.00 19.59 ? 128 ASP C CB  1 
ATOM   5401  C  CG  . ASP C 1 128 ? 51.832  13.919  -35.852 1.00 28.32 ? 128 ASP C CG  1 
ATOM   5402  O  OD1 . ASP C 1 128 ? 52.720  14.851  -35.757 1.00 31.05 ? 128 ASP C OD1 1 
ATOM   5403  O  OD2 . ASP C 1 128 ? 50.683  14.166  -36.309 1.00 30.51 ? 128 ASP C OD2 1 
ATOM   5404  N  N   . ALA C 1 129 ? 49.911  10.457  -35.701 1.00 19.60 ? 129 ALA C N   1 
ATOM   5405  C  CA  . ALA C 1 129 ? 48.482  10.063  -35.883 1.00 19.16 ? 129 ALA C CA  1 
ATOM   5406  C  C   . ALA C 1 129 ? 47.478  11.224  -35.972 1.00 21.76 ? 129 ALA C C   1 
ATOM   5407  O  O   . ALA C 1 129 ? 46.525  11.131  -36.715 1.00 20.10 ? 129 ALA C O   1 
ATOM   5408  C  CB  . ALA C 1 129 ? 48.068  9.099   -34.874 1.00 21.80 ? 129 ALA C CB  1 
ATOM   5409  N  N   . SER C 1 130 ? 47.663  12.250  -35.166 1.00 23.14 ? 130 SER C N   1 
ATOM   5410  C  CA  . SER C 1 130 ? 46.921  13.484  -35.227 1.00 26.51 ? 130 SER C CA  1 
ATOM   5411  C  C   . SER C 1 130 ? 46.885  14.016  -36.660 1.00 24.13 ? 130 SER C C   1 
ATOM   5412  O  O   . SER C 1 130 ? 45.826  14.263  -37.225 1.00 25.80 ? 130 SER C O   1 
ATOM   5413  C  CB  . SER C 1 130 ? 47.605  14.484  -34.242 1.00 27.40 ? 130 SER C CB  1 
ATOM   5414  O  OG  . SER C 1 130 ? 46.989  15.764  -34.296 1.00 35.21 ? 130 SER C OG  1 
ATOM   5415  N  N   . THR C 1 131 ? 48.071  14.212  -37.270 1.00 21.46 ? 131 THR C N   1 
ATOM   5416  C  CA  . THR C 1 131 ? 48.137  14.770  -38.638 1.00 20.31 ? 131 THR C CA  1 
ATOM   5417  C  C   . THR C 1 131 ? 47.420  13.798  -39.604 1.00 18.36 ? 131 THR C C   1 
ATOM   5418  O  O   . THR C 1 131 ? 46.749  14.246  -40.544 1.00 18.20 ? 131 THR C O   1 
ATOM   5419  C  CB  . THR C 1 131 ? 49.646  14.964  -39.079 1.00 20.87 ? 131 THR C CB  1 
ATOM   5420  O  OG1 . THR C 1 131 ? 50.262  15.853  -38.115 1.00 23.81 ? 131 THR C OG1 1 
ATOM   5421  C  CG2 . THR C 1 131 ? 49.775  15.547  -40.485 1.00 23.94 ? 131 THR C CG2 1 
ATOM   5422  N  N   . ALA C 1 132 ? 47.653  12.513  -39.405 1.00 18.17 ? 132 ALA C N   1 
ATOM   5423  C  CA  . ALA C 1 132 ? 47.113  11.464  -40.329 1.00 17.02 ? 132 ALA C CA  1 
ATOM   5424  C  C   . ALA C 1 132 ? 45.601  11.349  -40.290 1.00 18.01 ? 132 ALA C C   1 
ATOM   5425  O  O   . ALA C 1 132 ? 44.996  10.983  -41.281 1.00 17.29 ? 132 ALA C O   1 
ATOM   5426  C  CB  . ALA C 1 132 ? 47.669  10.141  -39.965 1.00 14.89 ? 132 ALA C CB  1 
ATOM   5427  N  N   . SER C 1 133 ? 45.032  11.687  -39.130 1.00 16.93 ? 133 SER C N   1 
ATOM   5428  C  CA  . SER C 1 133 ? 43.649  11.177  -38.845 1.00 17.73 ? 133 SER C CA  1 
ATOM   5429  C  C   . SER C 1 133 ? 42.657  11.794  -39.740 1.00 18.68 ? 133 SER C C   1 
ATOM   5430  O  O   . SER C 1 133 ? 41.554  11.156  -39.896 1.00 17.20 ? 133 SER C O   1 
ATOM   5431  C  CB  . SER C 1 133 ? 43.307  11.393  -37.345 1.00 18.23 ? 133 SER C CB  1 
ATOM   5432  O  OG  . SER C 1 133 ? 43.340  12.846  -37.102 1.00 19.60 ? 133 SER C OG  1 
ATOM   5433  N  N   . ASN C 1 134 ? 42.898  12.972  -40.326 1.00 18.04 ? 134 ASN C N   1 
ATOM   5434  C  CA  . ASN C 1 134 ? 41.891  13.578  -41.186 1.00 19.76 ? 134 ASN C CA  1 
ATOM   5435  C  C   . ASN C 1 134 ? 42.337  13.593  -42.668 1.00 16.13 ? 134 ASN C C   1 
ATOM   5436  O  O   . ASN C 1 134 ? 41.878  14.382  -43.505 1.00 21.59 ? 134 ASN C O   1 
ATOM   5437  C  CB  . ASN C 1 134 ? 41.499  14.985  -40.678 1.00 20.89 ? 134 ASN C CB  1 
ATOM   5438  C  CG  . ASN C 1 134 ? 42.656  15.945  -40.754 1.00 25.14 ? 134 ASN C CG  1 
ATOM   5439  O  OD1 . ASN C 1 134 ? 43.823  15.538  -40.831 1.00 24.53 ? 134 ASN C OD1 1 
ATOM   5440  N  ND2 . ASN C 1 134 ? 42.319  17.221  -40.822 1.00 26.97 ? 134 ASN C ND2 1 
ATOM   5441  N  N   . LYS C 1 135 ? 43.228  12.679  -43.024 1.00 18.46 ? 135 LYS C N   1 
ATOM   5442  C  CA  . LYS C 1 135 ? 43.867  12.669  -44.290 1.00 18.55 ? 135 LYS C CA  1 
ATOM   5443  C  C   . LYS C 1 135 ? 43.779  11.345  -44.969 1.00 18.20 ? 135 LYS C C   1 
ATOM   5444  O  O   . LYS C 1 135 ? 43.579  10.300  -44.302 1.00 16.39 ? 135 LYS C O   1 
ATOM   5445  C  CB  . LYS C 1 135 ? 45.371  13.018  -44.146 1.00 19.06 ? 135 LYS C CB  1 
ATOM   5446  C  CG  . LYS C 1 135 ? 45.537  14.425  -43.569 1.00 20.03 ? 135 LYS C CG  1 
ATOM   5447  C  CD  . LYS C 1 135 ? 47.003  14.878  -43.621 1.00 22.60 ? 135 LYS C CD  1 
ATOM   5448  C  CE  . LYS C 1 135 ? 47.044  16.361  -43.321 1.00 23.36 ? 135 LYS C CE  1 
ATOM   5449  N  NZ  . LYS C 1 135 ? 46.321  16.806  -42.046 1.00 24.85 ? 135 LYS C NZ  1 
ATOM   5450  N  N   . SER C 1 136 ? 43.810  11.406  -46.288 1.00 18.97 ? 136 SER C N   1 
ATOM   5451  C  CA  . SER C 1 136 ? 43.660  10.232  -47.122 1.00 18.87 ? 136 SER C CA  1 
ATOM   5452  C  C   . SER C 1 136 ? 44.532  9.025   -46.619 1.00 16.32 ? 136 SER C C   1 
ATOM   5453  O  O   . SER C 1 136 ? 45.757  9.193   -46.355 1.00 17.51 ? 136 SER C O   1 
ATOM   5454  C  CB  . SER C 1 136 ? 44.078  10.652  -48.510 1.00 19.42 ? 136 SER C CB  1 
ATOM   5455  O  OG  . SER C 1 136 ? 44.077  9.508   -49.268 1.00 25.20 ? 136 SER C OG  1 
ATOM   5456  N  N   . GLU C 1 137 ? 43.934  7.839   -46.462 1.00 17.45 ? 137 GLU C N   1 
ATOM   5457  C  CA  . GLU C 1 137 ? 44.638  6.591   -46.120 1.00 17.54 ? 137 GLU C CA  1 
ATOM   5458  C  C   . GLU C 1 137 ? 45.345  6.773   -44.782 1.00 15.72 ? 137 GLU C C   1 
ATOM   5459  O  O   . GLU C 1 137 ? 46.398  6.150   -44.535 1.00 17.23 ? 137 GLU C O   1 
ATOM   5460  C  CB  . GLU C 1 137 ? 45.655  6.143   -47.128 1.00 15.29 ? 137 GLU C CB  1 
ATOM   5461  C  CG  . GLU C 1 137 ? 45.015  5.725   -48.407 1.00 21.76 ? 137 GLU C CG  1 
ATOM   5462  C  CD  . GLU C 1 137 ? 45.948  5.414   -49.621 1.00 26.04 ? 137 GLU C CD  1 
ATOM   5463  O  OE1 . GLU C 1 137 ? 45.361  4.822   -50.565 1.00 29.49 ? 137 GLU C OE1 1 
ATOM   5464  O  OE2 . GLU C 1 137 ? 47.189  5.725   -49.658 1.00 32.30 ? 137 GLU C OE2 1 
ATOM   5465  N  N   . GLY C 1 138 ? 44.787  7.594   -43.921 1.00 14.13 ? 138 GLY C N   1 
ATOM   5466  C  CA  . GLY C 1 138 ? 45.531  7.979   -42.739 1.00 14.60 ? 138 GLY C CA  1 
ATOM   5467  C  C   . GLY C 1 138 ? 45.699  6.938   -41.676 1.00 16.27 ? 138 GLY C C   1 
ATOM   5468  O  O   . GLY C 1 138 ? 46.672  6.943   -40.898 1.00 15.59 ? 138 GLY C O   1 
ATOM   5469  N  N   . LEU C 1 139 ? 44.696  6.047   -41.521 1.00 13.16 ? 139 LEU C N   1 
ATOM   5470  C  CA  . LEU C 1 139 ? 44.594  5.209   -40.378 1.00 11.98 ? 139 LEU C CA  1 
ATOM   5471  C  C   . LEU C 1 139 ? 44.279  3.782   -40.713 1.00 12.51 ? 139 LEU C C   1 
ATOM   5472  O  O   . LEU C 1 139 ? 43.609  3.555   -41.751 1.00 11.96 ? 139 LEU C O   1 
ATOM   5473  C  CB  . LEU C 1 139 ? 43.657  5.731   -39.253 1.00 13.18 ? 139 LEU C CB  1 
ATOM   5474  C  CG  . LEU C 1 139 ? 43.807  7.160   -38.729 1.00 12.87 ? 139 LEU C CG  1 
ATOM   5475  C  CD1 . LEU C 1 139 ? 42.557  7.612   -38.011 1.00 17.08 ? 139 LEU C CD1 1 
ATOM   5476  C  CD2 . LEU C 1 139 ? 45.045  7.188   -37.761 1.00 15.49 ? 139 LEU C CD2 1 
ATOM   5477  N  N   . ALA C 1 140 ? 44.621  2.846   -39.833 1.00 10.42 ? 140 ALA C N   1 
ATOM   5478  C  CA  . ALA C 1 140 ? 44.266  1.444   -39.933 1.00 10.76 ? 140 ALA C CA  1 
ATOM   5479  C  C   . ALA C 1 140 ? 44.010  0.955   -38.566 1.00 13.44 ? 140 ALA C C   1 
ATOM   5480  O  O   . ALA C 1 140 ? 44.818  1.226   -37.668 1.00 12.92 ? 140 ALA C O   1 
ATOM   5481  C  CB  . ALA C 1 140 ? 45.336  0.603   -40.623 1.00 12.35 ? 140 ALA C CB  1 
ATOM   5482  N  N   . VAL C 1 141 ? 42.897  0.229   -38.315 1.00 11.18 ? 141 VAL C N   1 
ATOM   5483  C  CA  . VAL C 1 141 ? 42.623  -0.242  -36.977 1.00 12.35 ? 141 VAL C CA  1 
ATOM   5484  C  C   . VAL C 1 141 ? 42.460  -1.732  -37.024 1.00 10.76 ? 141 VAL C C   1 
ATOM   5485  O  O   . VAL C 1 141 ? 41.896  -2.322  -37.970 1.00 11.61 ? 141 VAL C O   1 
ATOM   5486  C  CB  . VAL C 1 141 ? 41.321  0.391   -36.410 1.00 8.75  ? 141 VAL C CB  1 
ATOM   5487  C  CG1 . VAL C 1 141 ? 40.965  -0.308  -35.060 1.00 14.90 ? 141 VAL C CG1 1 
ATOM   5488  C  CG2 . VAL C 1 141 ? 41.405  1.875   -36.289 1.00 11.85 ? 141 VAL C CG2 1 
ATOM   5489  N  N   . LEU C 1 142 ? 43.048  -2.392  -36.027 1.00 10.45 ? 142 LEU C N   1 
ATOM   5490  C  CA  . LEU C 1 142 ? 42.751  -3.797  -35.803 1.00 11.11 ? 142 LEU C CA  1 
ATOM   5491  C  C   . LEU C 1 142 ? 41.698  -3.938  -34.738 1.00 11.35 ? 142 LEU C C   1 
ATOM   5492  O  O   . LEU C 1 142 ? 41.886  -3.293  -33.634 1.00 13.13 ? 142 LEU C O   1 
ATOM   5493  C  CB  . LEU C 1 142 ? 44.016  -4.573  -35.272 1.00 13.35 ? 142 LEU C CB  1 
ATOM   5494  C  CG  . LEU C 1 142 ? 45.255  -4.437  -36.206 1.00 12.67 ? 142 LEU C CG  1 
ATOM   5495  C  CD1 . LEU C 1 142 ? 46.381  -5.307  -35.602 1.00 17.16 ? 142 LEU C CD1 1 
ATOM   5496  C  CD2 . LEU C 1 142 ? 45.025  -4.914  -37.618 1.00 14.83 ? 142 LEU C CD2 1 
ATOM   5497  N  N   . ALA C 1 143 ? 40.591  -4.608  -35.034 1.00 11.09 ? 143 ALA C N   1 
ATOM   5498  C  CA  . ALA C 1 143 ? 39.498  -4.744  -34.074 1.00 12.10 ? 143 ALA C CA  1 
ATOM   5499  C  C   . ALA C 1 143 ? 39.354  -6.184  -33.707 1.00 10.48 ? 143 ALA C C   1 
ATOM   5500  O  O   . ALA C 1 143 ? 39.320  -7.149  -34.477 1.00 12.06 ? 143 ALA C O   1 
ATOM   5501  C  CB  . ALA C 1 143 ? 38.159  -4.293  -34.740 1.00 11.07 ? 143 ALA C CB  1 
ATOM   5502  N  N   . VAL C 1 144 ? 39.296  -6.295  -32.355 1.00 13.16 ? 144 VAL C N   1 
ATOM   5503  C  CA  . VAL C 1 144 ? 39.116  -7.619  -31.743 1.00 12.55 ? 144 VAL C CA  1 
ATOM   5504  C  C   . VAL C 1 144 ? 37.788  -7.695  -30.927 1.00 11.20 ? 144 VAL C C   1 
ATOM   5505  O  O   . VAL C 1 144 ? 37.509  -6.852  -30.134 1.00 13.91 ? 144 VAL C O   1 
ATOM   5506  C  CB  . VAL C 1 144 ? 40.306  -7.939  -30.763 1.00 13.30 ? 144 VAL C CB  1 
ATOM   5507  C  CG1 . VAL C 1 144 ? 40.035  -9.355  -30.210 1.00 14.95 ? 144 VAL C CG1 1 
ATOM   5508  C  CG2 . VAL C 1 144 ? 41.630  -7.961  -31.494 1.00 15.84 ? 144 VAL C CG2 1 
ATOM   5509  N  N   . LEU C 1 145 ? 37.000  -8.663  -31.381 1.00 13.53 ? 145 LEU C N   1 
ATOM   5510  C  CA  . LEU C 1 145 ? 35.666  -8.859  -30.707 1.00 14.32 ? 145 LEU C CA  1 
ATOM   5511  C  C   . LEU C 1 145 ? 35.964  -9.651  -29.371 1.00 15.49 ? 145 LEU C C   1 
ATOM   5512  O  O   . LEU C 1 145 ? 36.683  -10.695 -29.449 1.00 18.27 ? 145 LEU C O   1 
ATOM   5513  C  CB  . LEU C 1 145 ? 34.712  -9.573  -31.616 1.00 14.57 ? 145 LEU C CB  1 
ATOM   5514  C  CG  . LEU C 1 145 ? 34.475  -8.825  -32.934 1.00 15.09 ? 145 LEU C CG  1 
ATOM   5515  C  CD1 . LEU C 1 145 ? 33.745  -9.718  -33.867 1.00 15.19 ? 145 LEU C CD1 1 
ATOM   5516  C  CD2 . LEU C 1 145 ? 33.587  -7.659  -32.570 1.00 14.58 ? 145 LEU C CD2 1 
ATOM   5517  N  N   . ILE C 1 146 ? 35.289  -9.154  -28.303 1.00 13.94 ? 146 ILE C N   1 
ATOM   5518  C  CA  . ILE C 1 146 ? 35.522  -9.626  -26.820 1.00 15.36 ? 146 ILE C CA  1 
ATOM   5519  C  C   . ILE C 1 146 ? 34.165  -10.291 -26.425 1.00 18.93 ? 146 ILE C C   1 
ATOM   5520  O  O   . ILE C 1 146 ? 33.108  -9.629  -26.387 1.00 16.01 ? 146 ILE C O   1 
ATOM   5521  C  CB  . ILE C 1 146 ? 35.960  -8.505  -25.886 1.00 16.48 ? 146 ILE C CB  1 
ATOM   5522  C  CG1 . ILE C 1 146 ? 37.355  -7.928  -26.274 1.00 15.03 ? 146 ILE C CG1 1 
ATOM   5523  C  CG2 . ILE C 1 146 ? 36.163  -9.187  -24.453 1.00 16.74 ? 146 ILE C CG2 1 
ATOM   5524  C  CD1 . ILE C 1 146 ? 37.801  -6.635  -25.593 1.00 20.75 ? 146 ILE C CD1 1 
ATOM   5525  N  N   . GLU C 1 147 ? 34.229  -11.596 -26.090 1.00 21.04 ? 147 GLU C N   1 
ATOM   5526  C  CA  . GLU C 1 147 ? 33.132  -12.290 -25.419 1.00 23.41 ? 147 GLU C CA  1 
ATOM   5527  C  C   . GLU C 1 147 ? 33.547  -12.840 -24.031 1.00 25.60 ? 147 GLU C C   1 
ATOM   5528  O  O   . GLU C 1 147 ? 34.740  -12.853 -23.648 1.00 24.08 ? 147 GLU C O   1 
ATOM   5529  C  CB  . GLU C 1 147 ? 32.564  -13.393 -26.255 1.00 20.98 ? 147 GLU C CB  1 
ATOM   5530  C  CG  . GLU C 1 147 ? 33.597  -14.453 -26.500 1.00 24.36 ? 147 GLU C CG  1 
ATOM   5531  C  CD  . GLU C 1 147 ? 33.120  -15.603 -27.370 1.00 26.25 ? 147 GLU C CD  1 
ATOM   5532  O  OE1 . GLU C 1 147 ? 32.175  -15.447 -28.242 1.00 27.91 ? 147 GLU C OE1 1 
ATOM   5533  O  OE2 . GLU C 1 147 ? 33.736  -16.700 -27.257 1.00 34.62 ? 147 GLU C OE2 1 
ATOM   5534  N  N   . MET C 1 148 ? 32.515  -13.253 -23.308 1.00 27.53 ? 148 MET C N   1 
ATOM   5535  C  CA  . MET C 1 148 ? 32.663  -13.772 -21.939 1.00 29.33 ? 148 MET C CA  1 
ATOM   5536  C  C   . MET C 1 148 ? 33.163  -15.161 -22.037 1.00 28.49 ? 148 MET C C   1 
ATOM   5537  O  O   . MET C 1 148 ? 32.645  -16.003 -22.830 1.00 28.30 ? 148 MET C O   1 
ATOM   5538  C  CB  . MET C 1 148 ? 31.319  -13.781 -21.230 1.00 30.28 ? 148 MET C CB  1 
ATOM   5539  C  CG  . MET C 1 148 ? 31.418  -13.788 -19.735 1.00 37.26 ? 148 MET C CG  1 
ATOM   5540  S  SD  . MET C 1 148 ? 31.890  -15.363 -18.989 1.00 44.22 ? 148 MET C SD  1 
ATOM   5541  C  CE  . MET C 1 148 ? 31.017  -16.514 -20.049 1.00 40.04 ? 148 MET C CE  1 
ATOM   5542  N  N   . GLY C 1 149 ? 34.183  -15.465 -21.212 1.00 29.42 ? 149 GLY C N   1 
ATOM   5543  C  CA  . GLY C 1 149 ? 34.565  -16.866 -21.128 1.00 29.84 ? 149 GLY C CA  1 
ATOM   5544  C  C   . GLY C 1 149 ? 35.634  -17.043 -20.049 1.00 30.19 ? 149 GLY C C   1 
ATOM   5545  O  O   . GLY C 1 149 ? 35.481  -16.543 -18.904 1.00 29.97 ? 149 GLY C O   1 
ATOM   5546  N  N   . SER C 1 150 ? 36.740  -17.666 -20.457 1.00 32.06 ? 150 SER C N   1 
ATOM   5547  C  CA  . SER C 1 150 ? 37.931  -17.941 -19.591 1.00 31.21 ? 150 SER C CA  1 
ATOM   5548  C  C   . SER C 1 150 ? 38.678  -16.650 -19.322 1.00 31.77 ? 150 SER C C   1 
ATOM   5549  O  O   . SER C 1 150 ? 38.727  -15.796 -20.238 1.00 31.46 ? 150 SER C O   1 
ATOM   5550  C  CB  . SER C 1 150 ? 38.925  -18.818 -20.328 1.00 32.76 ? 150 SER C CB  1 
ATOM   5551  O  OG  . SER C 1 150 ? 38.506  -20.179 -20.455 1.00 35.69 ? 150 SER C OG  1 
ATOM   5552  N  N   . PHE C 1 151 ? 39.351  -16.577 -18.147 1.00 28.03 ? 151 PHE C N   1 
ATOM   5553  C  CA  . PHE C 1 151 ? 40.010  -15.361 -17.581 1.00 25.74 ? 151 PHE C CA  1 
ATOM   5554  C  C   . PHE C 1 151 ? 41.139  -15.095 -18.540 1.00 25.65 ? 151 PHE C C   1 
ATOM   5555  O  O   . PHE C 1 151 ? 41.682  -16.035 -19.075 1.00 25.25 ? 151 PHE C O   1 
ATOM   5556  C  CB  . PHE C 1 151 ? 40.593  -15.667 -16.134 1.00 26.27 ? 151 PHE C CB  1 
ATOM   5557  C  CG  . PHE C 1 151 ? 41.565  -14.630 -15.594 1.00 22.19 ? 151 PHE C CG  1 
ATOM   5558  C  CD1 . PHE C 1 151 ? 41.111  -13.395 -15.201 1.00 25.01 ? 151 PHE C CD1 1 
ATOM   5559  C  CD2 . PHE C 1 151 ? 42.935  -14.883 -15.534 1.00 25.30 ? 151 PHE C CD2 1 
ATOM   5560  C  CE1 . PHE C 1 151 ? 42.011  -12.363 -14.730 1.00 26.50 ? 151 PHE C CE1 1 
ATOM   5561  C  CE2 . PHE C 1 151 ? 43.808  -13.936 -15.071 1.00 27.18 ? 151 PHE C CE2 1 
ATOM   5562  C  CZ  . PHE C 1 151 ? 43.352  -12.632 -14.645 1.00 25.20 ? 151 PHE C CZ  1 
ATOM   5563  N  N   . ASN C 1 152 ? 41.486  -13.816 -18.786 1.00 23.64 ? 152 ASN C N   1 
ATOM   5564  C  CA  . ASN C 1 152 ? 42.566  -13.566 -19.742 1.00 21.98 ? 152 ASN C CA  1 
ATOM   5565  C  C   . ASN C 1 152 ? 43.716  -12.783 -19.158 1.00 21.33 ? 152 ASN C C   1 
ATOM   5566  O  O   . ASN C 1 152 ? 43.612  -11.517 -18.816 1.00 23.18 ? 152 ASN C O   1 
ATOM   5567  C  CB  . ASN C 1 152 ? 41.897  -12.890 -21.011 1.00 20.81 ? 152 ASN C CB  1 
ATOM   5568  C  CG  . ASN C 1 152 ? 42.825  -12.715 -22.166 1.00 23.23 ? 152 ASN C CG  1 
ATOM   5569  O  OD1 . ASN C 1 152 ? 44.010  -12.355 -21.985 1.00 27.14 ? 152 ASN C OD1 1 
ATOM   5570  N  ND2 . ASN C 1 152 ? 42.279  -12.909 -23.424 1.00 23.49 ? 152 ASN C ND2 1 
ATOM   5571  N  N   . PRO C 1 153 ? 44.835  -13.463 -18.893 1.00 23.79 ? 153 PRO C N   1 
ATOM   5572  C  CA  . PRO C 1 153 ? 45.942  -12.763 -18.261 1.00 24.30 ? 153 PRO C CA  1 
ATOM   5573  C  C   . PRO C 1 153 ? 46.526  -11.616 -19.040 1.00 25.42 ? 153 PRO C C   1 
ATOM   5574  O  O   . PRO C 1 153 ? 46.967  -10.586 -18.416 1.00 25.38 ? 153 PRO C O   1 
ATOM   5575  C  CB  . PRO C 1 153 ? 46.935  -13.895 -17.867 1.00 25.64 ? 153 PRO C CB  1 
ATOM   5576  C  CG  . PRO C 1 153 ? 46.496  -15.146 -18.543 1.00 24.79 ? 153 PRO C CG  1 
ATOM   5577  C  CD  . PRO C 1 153 ? 45.062  -14.926 -19.146 1.00 20.62 ? 153 PRO C CD  1 
ATOM   5578  N  N   . SER C 1 154 ? 46.390  -11.646 -20.380 1.00 24.93 ? 154 SER C N   1 
ATOM   5579  C  CA  . SER C 1 154 ? 46.911  -10.549 -21.225 1.00 22.99 ? 154 SER C CA  1 
ATOM   5580  C  C   . SER C 1 154 ? 46.074  -9.362  -21.029 1.00 21.60 ? 154 SER C C   1 
ATOM   5581  O  O   . SER C 1 154 ? 46.608  -8.253  -20.746 1.00 22.62 ? 154 SER C O   1 
ATOM   5582  C  CB  . SER C 1 154 ? 47.017  -11.003 -22.661 1.00 27.26 ? 154 SER C CB  1 
ATOM   5583  O  OG  . SER C 1 154 ? 47.811  -12.176 -22.655 1.00 31.61 ? 154 SER C OG  1 
ATOM   5584  N  N   . TYR C 1 155 ? 44.723  -9.506  -21.128 1.00 22.96 ? 155 TYR C N   1 
ATOM   5585  C  CA  . TYR C 1 155 ? 43.856  -8.354  -20.907 1.00 24.19 ? 155 TYR C CA  1 
ATOM   5586  C  C   . TYR C 1 155 ? 44.013  -7.804  -19.466 1.00 23.64 ? 155 TYR C C   1 
ATOM   5587  O  O   . TYR C 1 155 ? 43.766  -6.551  -19.185 1.00 22.48 ? 155 TYR C O   1 
ATOM   5588  C  CB  . TYR C 1 155 ? 42.366  -8.617  -21.261 1.00 21.84 ? 155 TYR C CB  1 
ATOM   5589  C  CG  . TYR C 1 155 ? 42.159  -8.562  -22.768 1.00 20.39 ? 155 TYR C CG  1 
ATOM   5590  C  CD1 . TYR C 1 155 ? 41.634  -7.430  -23.385 1.00 20.98 ? 155 TYR C CD1 1 
ATOM   5591  C  CD2 . TYR C 1 155 ? 42.538  -9.627  -23.580 1.00 17.36 ? 155 TYR C CD2 1 
ATOM   5592  C  CE1 . TYR C 1 155 ? 41.466  -7.374  -24.763 1.00 20.61 ? 155 TYR C CE1 1 
ATOM   5593  C  CE2 . TYR C 1 155 ? 42.374  -9.578  -24.957 1.00 23.97 ? 155 TYR C CE2 1 
ATOM   5594  C  CZ  . TYR C 1 155 ? 41.839  -8.450  -25.542 1.00 23.53 ? 155 TYR C CZ  1 
ATOM   5595  O  OH  . TYR C 1 155 ? 41.675  -8.402  -26.911 1.00 22.54 ? 155 TYR C OH  1 
ATOM   5596  N  N   . ASP C 1 156 ? 44.408  -8.646  -18.506 1.00 26.05 ? 156 ASP C N   1 
ATOM   5597  C  CA  . ASP C 1 156 ? 44.548  -8.135  -17.139 1.00 28.87 ? 156 ASP C CA  1 
ATOM   5598  C  C   . ASP C 1 156 ? 45.765  -7.227  -16.968 1.00 27.62 ? 156 ASP C C   1 
ATOM   5599  O  O   . ASP C 1 156 ? 45.798  -6.465  -15.959 1.00 28.10 ? 156 ASP C O   1 
ATOM   5600  C  CB  . ASP C 1 156 ? 44.572  -9.256  -16.103 1.00 28.55 ? 156 ASP C CB  1 
ATOM   5601  C  CG  . ASP C 1 156 ? 43.492  -9.055  -15.015 1.00 35.34 ? 156 ASP C CG  1 
ATOM   5602  O  OD1 . ASP C 1 156 ? 42.329  -8.650  -15.344 1.00 31.81 ? 156 ASP C OD1 1 
ATOM   5603  O  OD2 . ASP C 1 156 ? 43.809  -9.272  -13.822 1.00 38.04 ? 156 ASP C OD2 1 
ATOM   5604  N  N   . LYS C 1 157 ? 46.656  -7.187  -17.983 1.00 26.56 ? 157 LYS C N   1 
ATOM   5605  C  CA  . LYS C 1 157 ? 47.885  -6.334  -17.894 1.00 23.51 ? 157 LYS C CA  1 
ATOM   5606  C  C   . LYS C 1 157 ? 47.407  -4.924  -18.057 1.00 24.56 ? 157 LYS C C   1 
ATOM   5607  O  O   . LYS C 1 157 ? 48.060  -3.945  -17.511 1.00 25.45 ? 157 LYS C O   1 
ATOM   5608  C  CB  . LYS C 1 157 ? 48.945  -6.732  -18.892 1.00 25.58 ? 157 LYS C CB  1 
ATOM   5609  C  CG  . LYS C 1 157 ? 49.387  -8.241  -18.701 1.00 25.53 ? 157 LYS C CG  1 
ATOM   5610  C  CD  . LYS C 1 157 ? 50.414  -8.772  -19.696 1.00 26.31 ? 157 LYS C CD  1 
ATOM   5611  C  CE  . LYS C 1 157 ? 50.464  -10.280 -19.499 1.00 30.49 ? 157 LYS C CE  1 
ATOM   5612  N  NZ  . LYS C 1 157 ? 51.459  -10.933 -20.380 1.00 34.92 ? 157 LYS C NZ  1 
ATOM   5613  N  N   A ILE C 1 158 ? 46.284  -4.750  -18.754 0.50 22.37 ? 158 ILE C N   1 
ATOM   5614  N  N   B ILE C 1 158 ? 46.291  -4.771  -18.780 0.50 22.72 ? 158 ILE C N   1 
ATOM   5615  C  CA  A ILE C 1 158 ? 45.703  -3.402  -18.773 0.50 21.27 ? 158 ILE C CA  1 
ATOM   5616  C  CA  B ILE C 1 158 ? 45.620  -3.466  -18.811 0.50 23.20 ? 158 ILE C CA  1 
ATOM   5617  C  C   A ILE C 1 158 ? 44.679  -3.226  -17.648 0.50 22.16 ? 158 ILE C C   1 
ATOM   5618  C  C   B ILE C 1 158 ? 44.796  -3.320  -17.554 0.50 22.97 ? 158 ILE C C   1 
ATOM   5619  O  O   A ILE C 1 158 ? 44.627  -2.135  -17.010 0.50 21.56 ? 158 ILE C O   1 
ATOM   5620  O  O   B ILE C 1 158 ? 44.975  -2.343  -16.766 0.50 24.08 ? 158 ILE C O   1 
ATOM   5621  C  CB  A ILE C 1 158 ? 45.083  -3.037  -20.164 0.50 19.31 ? 158 ILE C CB  1 
ATOM   5622  C  CB  B ILE C 1 158 ? 44.627  -3.303  -20.041 0.50 21.19 ? 158 ILE C CB  1 
ATOM   5623  C  CG1 A ILE C 1 158 ? 46.144  -3.102  -21.222 0.50 17.94 ? 158 ILE C CG1 1 
ATOM   5624  C  CG1 B ILE C 1 158 ? 45.380  -3.338  -21.355 0.50 24.52 ? 158 ILE C CG1 1 
ATOM   5625  C  CG2 A ILE C 1 158 ? 44.631  -1.562  -20.179 0.50 17.91 ? 158 ILE C CG2 1 
ATOM   5626  C  CG2 B ILE C 1 158 ? 43.814  -1.973  -19.926 0.50 20.98 ? 158 ILE C CG2 1 
ATOM   5627  C  CD1 A ILE C 1 158 ? 45.489  -3.364  -22.579 0.50 17.03 ? 158 ILE C CD1 1 
ATOM   5628  C  CD1 B ILE C 1 158 ? 45.924  -4.726  -21.710 0.50 22.52 ? 158 ILE C CD1 1 
ATOM   5629  N  N   . PHE C 1 159 ? 43.842  -4.236  -17.423 1.00 23.58 ? 159 PHE C N   1 
ATOM   5630  C  CA  . PHE C 1 159 ? 42.651  -4.059  -16.556 1.00 22.68 ? 159 PHE C CA  1 
ATOM   5631  C  C   . PHE C 1 159 ? 43.071  -3.876  -15.056 1.00 24.66 ? 159 PHE C C   1 
ATOM   5632  O  O   . PHE C 1 159 ? 42.314  -3.236  -14.270 1.00 22.91 ? 159 PHE C O   1 
ATOM   5633  C  CB  . PHE C 1 159 ? 41.691  -5.261  -16.679 1.00 24.17 ? 159 PHE C CB  1 
ATOM   5634  C  CG  . PHE C 1 159 ? 41.003  -5.428  -18.067 1.00 24.48 ? 159 PHE C CG  1 
ATOM   5635  C  CD1 . PHE C 1 159 ? 40.778  -4.326  -18.951 1.00 25.00 ? 159 PHE C CD1 1 
ATOM   5636  C  CD2 . PHE C 1 159 ? 40.499  -6.703  -18.435 1.00 23.96 ? 159 PHE C CD2 1 
ATOM   5637  C  CE1 . PHE C 1 159 ? 40.121  -4.564  -20.210 1.00 23.97 ? 159 PHE C CE1 1 
ATOM   5638  C  CE2 . PHE C 1 159 ? 39.826  -6.888  -19.686 1.00 26.95 ? 159 PHE C CE2 1 
ATOM   5639  C  CZ  . PHE C 1 159 ? 39.690  -5.835  -20.534 1.00 24.96 ? 159 PHE C CZ  1 
ATOM   5640  N  N   . SER C 1 160 ? 44.296  -4.344  -14.750 1.00 25.02 ? 160 SER C N   1 
ATOM   5641  C  CA  . SER C 1 160 ? 44.862  -4.297  -13.416 1.00 26.00 ? 160 SER C CA  1 
ATOM   5642  C  C   . SER C 1 160 ? 45.256  -2.909  -13.021 1.00 27.56 ? 160 SER C C   1 
ATOM   5643  O  O   . SER C 1 160 ? 45.650  -2.696  -11.833 1.00 29.14 ? 160 SER C O   1 
ATOM   5644  C  CB  . SER C 1 160 ? 45.992  -5.286  -13.248 1.00 26.53 ? 160 SER C CB  1 
ATOM   5645  O  OG  . SER C 1 160 ? 47.177  -4.944  -13.972 1.00 27.40 ? 160 SER C OG  1 
ATOM   5646  N  N   . HIS C 1 161 ? 45.121  -1.952  -13.938 1.00 23.82 ? 161 HIS C N   1 
ATOM   5647  C  CA  . HIS C 1 161 ? 45.389  -0.529  -13.723 1.00 23.95 ? 161 HIS C CA  1 
ATOM   5648  C  C   . HIS C 1 161 ? 44.224  0.380   -13.721 1.00 23.24 ? 161 HIS C C   1 
ATOM   5649  O  O   . HIS C 1 161 ? 44.398  1.581   -13.507 1.00 23.18 ? 161 HIS C O   1 
ATOM   5650  C  CB  . HIS C 1 161 ? 46.537  -0.093  -14.687 1.00 25.67 ? 161 HIS C CB  1 
ATOM   5651  C  CG  . HIS C 1 161 ? 47.818  -0.857  -14.441 1.00 30.42 ? 161 HIS C CG  1 
ATOM   5652  N  ND1 . HIS C 1 161 ? 48.826  -0.376  -13.617 1.00 34.33 ? 161 HIS C ND1 1 
ATOM   5653  C  CD2 . HIS C 1 161 ? 48.187  -2.120  -14.797 1.00 33.44 ? 161 HIS C CD2 1 
ATOM   5654  C  CE1 . HIS C 1 161 ? 49.785  -1.287  -13.530 1.00 36.08 ? 161 HIS C CE1 1 
ATOM   5655  N  NE2 . HIS C 1 161 ? 49.422  -2.355  -14.226 1.00 36.23 ? 161 HIS C NE2 1 
ATOM   5656  N  N   . LEU C 1 162 ? 42.994  -0.127  -13.933 1.00 23.06 ? 162 LEU C N   1 
ATOM   5657  C  CA  . LEU C 1 162 ? 41.840  0.752   -14.117 1.00 23.24 ? 162 LEU C CA  1 
ATOM   5658  C  C   . LEU C 1 162 ? 41.541  1.590   -12.929 1.00 21.50 ? 162 LEU C C   1 
ATOM   5659  O  O   . LEU C 1 162 ? 41.068  2.773   -13.097 1.00 20.04 ? 162 LEU C O   1 
ATOM   5660  C  CB  . LEU C 1 162 ? 40.592  -0.018  -14.628 1.00 24.08 ? 162 LEU C CB  1 
ATOM   5661  C  CG  . LEU C 1 162 ? 40.832  -0.757  -15.966 1.00 27.40 ? 162 LEU C CG  1 
ATOM   5662  C  CD1 . LEU C 1 162 ? 39.737  -1.815  -16.316 1.00 27.15 ? 162 LEU C CD1 1 
ATOM   5663  C  CD2 . LEU C 1 162 ? 41.155  0.145   -17.164 1.00 29.01 ? 162 LEU C CD2 1 
ATOM   5664  N  N   . GLN C 1 163 ? 41.850  1.115   -11.689 1.00 22.28 ? 163 GLN C N   1 
ATOM   5665  C  CA  . GLN C 1 163 ? 41.466  1.945   -10.544 1.00 24.72 ? 163 GLN C CA  1 
ATOM   5666  C  C   . GLN C 1 163 ? 42.442  3.124   -10.379 1.00 21.17 ? 163 GLN C C   1 
ATOM   5667  O  O   . GLN C 1 163 ? 42.139  3.967   -9.476  1.00 25.23 ? 163 GLN C O   1 
ATOM   5668  C  CB  . GLN C 1 163 ? 41.277  1.153   -9.244  1.00 23.43 ? 163 GLN C CB  1 
ATOM   5669  C  CG  . GLN C 1 163 ? 40.158  0.048   -9.193  1.00 26.87 ? 163 GLN C CG  1 
ATOM   5670  C  CD  . GLN C 1 163 ? 38.737  0.537   -9.312  1.00 27.62 ? 163 GLN C CD  1 
ATOM   5671  O  OE1 . GLN C 1 163 ? 38.340  1.561   -8.749  1.00 25.22 ? 163 GLN C OE1 1 
ATOM   5672  N  NE2 . GLN C 1 163 ? 37.929  -0.229  -10.079 1.00 28.73 ? 163 GLN C NE2 1 
ATOM   5673  N  N   . HIS C 1 164 ? 43.556  3.159   -11.164 1.00 22.50 ? 164 HIS C N   1 
ATOM   5674  C  CA  . HIS C 1 164 ? 44.465  4.307   -11.215 1.00 24.85 ? 164 HIS C CA  1 
ATOM   5675  C  C   . HIS C 1 164 ? 44.008  5.469   -12.134 1.00 26.17 ? 164 HIS C C   1 
ATOM   5676  O  O   . HIS C 1 164 ? 44.458  6.586   -11.981 1.00 27.04 ? 164 HIS C O   1 
ATOM   5677  C  CB  . HIS C 1 164 ? 45.901  3.898   -11.461 1.00 26.33 ? 164 HIS C CB  1 
ATOM   5678  C  CG  . HIS C 1 164 ? 46.336  2.790   -10.545 1.00 23.35 ? 164 HIS C CG  1 
ATOM   5679  N  ND1 . HIS C 1 164 ? 46.329  2.892   -9.163  1.00 28.38 ? 164 HIS C ND1 1 
ATOM   5680  C  CD2 . HIS C 1 164 ? 46.787  1.553   -10.834 1.00 22.46 ? 164 HIS C CD2 1 
ATOM   5681  C  CE1 . HIS C 1 164 ? 46.687  1.725   -8.640  1.00 22.20 ? 164 HIS C CE1 1 
ATOM   5682  N  NE2 . HIS C 1 164 ? 47.001  0.907   -9.629  1.00 24.38 ? 164 HIS C NE2 1 
ATOM   5683  N  N   . VAL C 1 165 ? 43.065  5.161   -13.029 1.00 24.38 ? 165 VAL C N   1 
ATOM   5684  C  CA  . VAL C 1 165 ? 42.499  6.119   -13.940 1.00 24.21 ? 165 VAL C CA  1 
ATOM   5685  C  C   . VAL C 1 165 ? 40.955  6.241   -13.864 1.00 23.37 ? 165 VAL C C   1 
ATOM   5686  O  O   . VAL C 1 165 ? 40.262  6.463   -14.882 1.00 21.39 ? 165 VAL C O   1 
ATOM   5687  C  CB  . VAL C 1 165 ? 43.114  5.857   -15.336 1.00 24.20 ? 165 VAL C CB  1 
ATOM   5688  C  CG1 . VAL C 1 165 ? 44.596  6.352   -15.362 1.00 27.65 ? 165 VAL C CG1 1 
ATOM   5689  C  CG2 . VAL C 1 165 ? 43.086  4.323   -15.689 1.00 25.00 ? 165 VAL C CG2 1 
ATOM   5690  N  N   . LYS C 1 166 ? 40.382  6.237   -12.644 1.00 21.80 ? 166 LYS C N   1 
ATOM   5691  C  CA  . LYS C 1 166 ? 38.967  6.230   -12.534 1.00 23.55 ? 166 LYS C CA  1 
ATOM   5692  C  C   . LYS C 1 166 ? 38.290  7.466   -13.121 1.00 23.57 ? 166 LYS C C   1 
ATOM   5693  O  O   . LYS C 1 166 ? 37.097  7.419   -13.574 1.00 21.81 ? 166 LYS C O   1 
ATOM   5694  C  CB  . LYS C 1 166 ? 38.525  6.088   -11.037 1.00 25.86 ? 166 LYS C CB  1 
ATOM   5695  C  CG  . LYS C 1 166 ? 38.889  4.775   -10.410 1.00 25.75 ? 166 LYS C CG  1 
ATOM   5696  C  CD  . LYS C 1 166 ? 38.130  4.583   -9.009  1.00 29.06 ? 166 LYS C CD  1 
ATOM   5697  C  CE  . LYS C 1 166 ? 36.595  4.649   -9.115  1.00 31.34 ? 166 LYS C CE  1 
ATOM   5698  N  NZ  . LYS C 1 166 ? 36.075  3.310   -9.518  1.00 29.18 ? 166 LYS C NZ  1 
ATOM   5699  N  N   . TYR C 1 167 ? 38.990  8.587   -13.075 1.00 24.00 ? 167 TYR C N   1 
ATOM   5700  C  CA  . TYR C 1 167 ? 38.298  9.848   -13.441 1.00 25.44 ? 167 TYR C CA  1 
ATOM   5701  C  C   . TYR C 1 167 ? 38.870  10.467  -14.687 1.00 24.38 ? 167 TYR C C   1 
ATOM   5702  O  O   . TYR C 1 167 ? 40.098  10.313  -14.942 1.00 24.44 ? 167 TYR C O   1 
ATOM   5703  C  CB  . TYR C 1 167 ? 38.381  10.876  -12.305 1.00 26.96 ? 167 TYR C CB  1 
ATOM   5704  C  CG  . TYR C 1 167 ? 37.744  10.355  -11.064 1.00 28.52 ? 167 TYR C CG  1 
ATOM   5705  C  CD1 . TYR C 1 167 ? 36.349  10.283  -10.972 1.00 30.19 ? 167 TYR C CD1 1 
ATOM   5706  C  CD2 . TYR C 1 167 ? 38.539  9.843   -10.038 1.00 31.07 ? 167 TYR C CD2 1 
ATOM   5707  C  CE1 . TYR C 1 167 ? 35.728  9.757   -9.845  1.00 33.04 ? 167 TYR C CE1 1 
ATOM   5708  C  CE2 . TYR C 1 167 ? 37.956  9.304   -8.889  1.00 32.69 ? 167 TYR C CE2 1 
ATOM   5709  C  CZ  . TYR C 1 167 ? 36.536  9.260   -8.790  1.00 31.06 ? 167 TYR C CZ  1 
ATOM   5710  O  OH  . TYR C 1 167 ? 35.855  8.727   -7.706  1.00 32.23 ? 167 TYR C OH  1 
ATOM   5711  N  N   A LYS C 1 168 ? 38.033  11.271  -15.388 0.50 24.13 ? 168 LYS C N   1 
ATOM   5712  N  N   B LYS C 1 168 ? 38.040  11.262  -15.408 0.50 24.46 ? 168 LYS C N   1 
ATOM   5713  C  CA  A LYS C 1 168 ? 38.450  11.960  -16.617 0.50 24.93 ? 168 LYS C CA  1 
ATOM   5714  C  CA  B LYS C 1 168 ? 38.541  11.902  -16.626 0.50 25.35 ? 168 LYS C CA  1 
ATOM   5715  C  C   A LYS C 1 168 ? 39.704  12.822  -16.397 0.50 25.15 ? 168 LYS C C   1 
ATOM   5716  C  C   B LYS C 1 168 ? 39.791  12.697  -16.296 0.50 25.50 ? 168 LYS C C   1 
ATOM   5717  O  O   A LYS C 1 168 ? 39.698  13.721  -15.518 0.50 25.18 ? 168 LYS C O   1 
ATOM   5718  O  O   B LYS C 1 168 ? 39.878  13.414  -15.257 0.50 25.98 ? 168 LYS C O   1 
ATOM   5719  C  CB  A LYS C 1 168 ? 37.322  12.904  -17.106 0.50 24.65 ? 168 LYS C CB  1 
ATOM   5720  C  CB  B LYS C 1 168 ? 37.525  12.870  -17.280 0.50 25.52 ? 168 LYS C CB  1 
ATOM   5721  C  CG  A LYS C 1 168 ? 37.709  13.685  -18.369 0.50 24.92 ? 168 LYS C CG  1 
ATOM   5722  C  CG  B LYS C 1 168 ? 37.868  13.205  -18.770 0.50 25.63 ? 168 LYS C CG  1 
ATOM   5723  C  CD  A LYS C 1 168 ? 36.584  14.527  -18.949 0.50 24.73 ? 168 LYS C CD  1 
ATOM   5724  C  CD  B LYS C 1 168 ? 38.885  14.349  -18.941 0.50 25.60 ? 168 LYS C CD  1 
ATOM   5725  C  CE  A LYS C 1 168 ? 36.991  15.235  -20.259 0.50 27.44 ? 168 LYS C CE  1 
ATOM   5726  C  CE  B LYS C 1 168 ? 39.389  14.534  -20.375 0.50 24.47 ? 168 LYS C CE  1 
ATOM   5727  N  NZ  A LYS C 1 168 ? 35.935  16.240  -20.648 0.50 31.69 ? 168 LYS C NZ  1 
ATOM   5728  N  NZ  B LYS C 1 168 ? 40.880  14.672  -20.375 0.50 24.90 ? 168 LYS C NZ  1 
ATOM   5729  N  N   . GLY C 1 169 ? 40.753  12.588  -17.199 1.00 25.24 ? 169 GLY C N   1 
ATOM   5730  C  CA  . GLY C 1 169 ? 41.978  13.311  -17.086 1.00 25.93 ? 169 GLY C CA  1 
ATOM   5731  C  C   . GLY C 1 169 ? 43.034  12.558  -16.343 1.00 25.23 ? 169 GLY C C   1 
ATOM   5732  O  O   . GLY C 1 169 ? 44.206  12.951  -16.425 1.00 27.15 ? 169 GLY C O   1 
ATOM   5733  N  N   . GLN C 1 170 ? 42.704  11.451  -15.646 1.00 22.60 ? 170 GLN C N   1 
ATOM   5734  C  CA  . GLN C 1 170 ? 43.730  10.814  -14.860 1.00 22.63 ? 170 GLN C CA  1 
ATOM   5735  C  C   . GLN C 1 170 ? 44.552  9.941   -15.696 1.00 22.21 ? 170 GLN C C   1 
ATOM   5736  O  O   . GLN C 1 170 ? 44.056  9.426   -16.728 1.00 22.29 ? 170 GLN C O   1 
ATOM   5737  C  CB  . GLN C 1 170 ? 43.145  10.028  -13.643 1.00 23.46 ? 170 GLN C CB  1 
ATOM   5738  C  CG  . GLN C 1 170 ? 42.436  10.958  -12.616 1.00 20.16 ? 170 GLN C CG  1 
ATOM   5739  C  CD  . GLN C 1 170 ? 41.919  10.160  -11.416 1.00 24.25 ? 170 GLN C CD  1 
ATOM   5740  O  OE1 . GLN C 1 170 ? 41.540  8.989   -11.539 1.00 24.24 ? 170 GLN C OE1 1 
ATOM   5741  N  NE2 . GLN C 1 170 ? 41.983  10.779  -10.208 1.00 24.62 ? 170 GLN C NE2 1 
ATOM   5742  N  N   . GLU C 1 171 ? 45.807  9.780   -15.301 1.00 22.50 ? 171 GLU C N   1 
ATOM   5743  C  CA  . GLU C 1 171 ? 46.758  9.024   -16.047 1.00 24.05 ? 171 GLU C CA  1 
ATOM   5744  C  C   . GLU C 1 171 ? 47.458  8.065   -15.119 1.00 24.52 ? 171 GLU C C   1 
ATOM   5745  O  O   . GLU C 1 171 ? 47.645  8.360   -13.896 1.00 25.29 ? 171 GLU C O   1 
ATOM   5746  C  CB  . GLU C 1 171 ? 47.824  9.907   -16.739 1.00 26.45 ? 171 GLU C CB  1 
ATOM   5747  C  CG  . GLU C 1 171 ? 47.252  10.930  -17.697 1.00 26.27 ? 171 GLU C CG  1 
ATOM   5748  C  CD  . GLU C 1 171 ? 48.278  11.963  -18.211 1.00 26.38 ? 171 GLU C CD  1 
ATOM   5749  O  OE1 . GLU C 1 171 ? 49.397  12.068  -17.625 1.00 38.34 ? 171 GLU C OE1 1 
ATOM   5750  O  OE2 . GLU C 1 171 ? 47.887  12.650  -19.189 1.00 35.82 ? 171 GLU C OE2 1 
ATOM   5751  N  N   . ALA C 1 172 ? 47.954  6.998   -15.712 1.00 21.31 ? 172 ALA C N   1 
ATOM   5752  C  CA  . ALA C 1 172 ? 48.853  6.057   -15.017 1.00 25.42 ? 172 ALA C CA  1 
ATOM   5753  C  C   . ALA C 1 172 ? 49.797  5.415   -16.000 1.00 28.21 ? 172 ALA C C   1 
ATOM   5754  O  O   . ALA C 1 172 ? 49.701  5.659   -17.209 1.00 28.98 ? 172 ALA C O   1 
ATOM   5755  C  CB  . ALA C 1 172 ? 48.090  5.021   -14.163 1.00 26.35 ? 172 ALA C CB  1 
ATOM   5756  N  N   . PHE C 1 173 ? 50.788  4.668   -15.521 1.00 29.17 ? 173 PHE C N   1 
ATOM   5757  C  CA  . PHE C 1 173 ? 51.671  3.896   -16.427 1.00 29.74 ? 173 PHE C CA  1 
ATOM   5758  C  C   . PHE C 1 173 ? 51.343  2.411   -16.297 1.00 30.64 ? 173 PHE C C   1 
ATOM   5759  O  O   . PHE C 1 173 ? 50.981  1.933   -15.223 1.00 28.16 ? 173 PHE C O   1 
ATOM   5760  C  CB  . PHE C 1 173 ? 53.192  4.194   -16.309 1.00 29.79 ? 173 PHE C CB  1 
ATOM   5761  C  CG  . PHE C 1 173 ? 53.613  5.578   -16.834 1.00 27.90 ? 173 PHE C CG  1 
ATOM   5762  C  CD1 . PHE C 1 173 ? 54.064  5.741   -18.158 1.00 29.30 ? 173 PHE C CD1 1 
ATOM   5763  C  CD2 . PHE C 1 173 ? 53.548  6.724   -15.998 1.00 29.33 ? 173 PHE C CD2 1 
ATOM   5764  C  CE1 . PHE C 1 173 ? 54.428  7.023   -18.672 1.00 29.12 ? 173 PHE C CE1 1 
ATOM   5765  C  CE2 . PHE C 1 173 ? 53.914  8.030   -16.505 1.00 29.60 ? 173 PHE C CE2 1 
ATOM   5766  C  CZ  . PHE C 1 173 ? 54.368  8.180   -17.830 1.00 26.96 ? 173 PHE C CZ  1 
ATOM   5767  N  N   . VAL C 1 174 ? 51.352  1.752   -17.452 1.00 30.14 ? 174 VAL C N   1 
ATOM   5768  C  CA  . VAL C 1 174 ? 51.245  0.281   -17.557 1.00 31.03 ? 174 VAL C CA  1 
ATOM   5769  C  C   . VAL C 1 174 ? 52.575  -0.268  -18.027 1.00 30.53 ? 174 VAL C C   1 
ATOM   5770  O  O   . VAL C 1 174 ? 53.145  0.199   -19.029 1.00 31.92 ? 174 VAL C O   1 
ATOM   5771  C  CB  . VAL C 1 174 ? 50.157  -0.201  -18.612 1.00 28.69 ? 174 VAL C CB  1 
ATOM   5772  C  CG1 . VAL C 1 174 ? 50.338  -1.711  -18.956 1.00 27.58 ? 174 VAL C CG1 1 
ATOM   5773  C  CG2 . VAL C 1 174 ? 48.804  0.068   -18.081 1.00 31.80 ? 174 VAL C CG2 1 
ATOM   5774  N  N   . PRO C 1 175 ? 53.104  -1.311  -17.337 1.00 31.48 ? 175 PRO C N   1 
ATOM   5775  C  CA  . PRO C 1 175 ? 54.350  -1.827  -17.858 1.00 29.87 ? 175 PRO C CA  1 
ATOM   5776  C  C   . PRO C 1 175 ? 54.173  -2.480  -19.245 1.00 29.05 ? 175 PRO C C   1 
ATOM   5777  O  O   . PRO C 1 175 ? 53.121  -2.990  -19.492 1.00 28.58 ? 175 PRO C O   1 
ATOM   5778  C  CB  . PRO C 1 175 ? 54.780  -2.879  -16.787 1.00 30.69 ? 175 PRO C CB  1 
ATOM   5779  C  CG  . PRO C 1 175 ? 53.924  -2.553  -15.564 1.00 31.39 ? 175 PRO C CG  1 
ATOM   5780  C  CD  . PRO C 1 175 ? 52.674  -1.970  -16.100 1.00 31.19 ? 175 PRO C CD  1 
ATOM   5781  N  N   . GLY C 1 176 ? 55.242  -2.479  -20.047 1.00 28.84 ? 176 GLY C N   1 
ATOM   5782  C  CA  . GLY C 1 176 ? 55.359  -3.105  -21.368 1.00 27.82 ? 176 GLY C CA  1 
ATOM   5783  C  C   . GLY C 1 176 ? 54.910  -4.541  -21.267 1.00 29.12 ? 176 GLY C C   1 
ATOM   5784  O  O   . GLY C 1 176 ? 54.919  -5.161  -20.171 1.00 25.57 ? 176 GLY C O   1 
ATOM   5785  N  N   . PHE C 1 177 ? 54.364  -5.009  -22.393 1.00 27.29 ? 177 PHE C N   1 
ATOM   5786  C  CA  . PHE C 1 177 ? 54.100  -6.467  -22.609 1.00 27.47 ? 177 PHE C CA  1 
ATOM   5787  C  C   . PHE C 1 177 ? 53.882  -6.690  -24.126 1.00 27.00 ? 177 PHE C C   1 
ATOM   5788  O  O   . PHE C 1 177 ? 53.867  -5.717  -24.886 1.00 25.99 ? 177 PHE C O   1 
ATOM   5789  C  CB  . PHE C 1 177 ? 52.936  -6.935  -21.725 1.00 28.21 ? 177 PHE C CB  1 
ATOM   5790  C  CG  . PHE C 1 177 ? 51.567  -6.411  -22.113 1.00 30.33 ? 177 PHE C CG  1 
ATOM   5791  C  CD1 . PHE C 1 177 ? 50.672  -7.253  -22.759 1.00 30.63 ? 177 PHE C CD1 1 
ATOM   5792  C  CD2 . PHE C 1 177 ? 51.151  -5.132  -21.720 1.00 32.25 ? 177 PHE C CD2 1 
ATOM   5793  C  CE1 . PHE C 1 177 ? 49.424  -6.835  -23.123 1.00 29.71 ? 177 PHE C CE1 1 
ATOM   5794  C  CE2 . PHE C 1 177 ? 49.874  -4.679  -22.049 1.00 31.08 ? 177 PHE C CE2 1 
ATOM   5795  C  CZ  . PHE C 1 177 ? 48.998  -5.556  -22.771 1.00 27.78 ? 177 PHE C CZ  1 
ATOM   5796  N  N   . ASN C 1 178 ? 53.728  -7.953  -24.566 1.00 24.84 ? 178 ASN C N   1 
ATOM   5797  C  CA  . ASN C 1 178 ? 53.500  -8.259  -25.914 1.00 22.99 ? 178 ASN C CA  1 
ATOM   5798  C  C   . ASN C 1 178 ? 52.029  -8.033  -26.366 1.00 23.73 ? 178 ASN C C   1 
ATOM   5799  O  O   . ASN C 1 178 ? 51.082  -8.742  -25.926 1.00 22.15 ? 178 ASN C O   1 
ATOM   5800  C  CB  . ASN C 1 178 ? 53.818  -9.708  -26.080 1.00 23.83 ? 178 ASN C CB  1 
ATOM   5801  C  CG  . ASN C 1 178 ? 53.720  -10.108 -27.479 1.00 25.72 ? 178 ASN C CG  1 
ATOM   5802  O  OD1 . ASN C 1 178 ? 53.468  -9.269  -28.421 1.00 22.05 ? 178 ASN C OD1 1 
ATOM   5803  N  ND2 . ASN C 1 178 ? 53.841  -11.413 -27.692 1.00 28.45 ? 178 ASN C ND2 1 
ATOM   5804  N  N   . ILE C 1 179 ? 51.848  -6.931  -27.145 1.00 21.27 ? 179 ILE C N   1 
ATOM   5805  C  CA  . ILE C 1 179 ? 50.520  -6.527  -27.477 1.00 20.23 ? 179 ILE C CA  1 
ATOM   5806  C  C   . ILE C 1 179 ? 49.846  -7.619  -28.302 1.00 21.36 ? 179 ILE C C   1 
ATOM   5807  O  O   . ILE C 1 179 ? 48.565  -7.711  -28.355 1.00 18.14 ? 179 ILE C O   1 
ATOM   5808  C  CB  . ILE C 1 179 ? 50.602  -5.154  -28.169 1.00 20.79 ? 179 ILE C CB  1 
ATOM   5809  C  CG1 . ILE C 1 179 ? 51.117  -3.988  -27.234 1.00 16.80 ? 179 ILE C CG1 1 
ATOM   5810  C  CG2 . ILE C 1 179 ? 49.203  -4.753  -28.726 1.00 21.17 ? 179 ILE C CG2 1 
ATOM   5811  C  CD1 . ILE C 1 179 ? 50.398  -3.910  -25.840 1.00 19.58 ? 179 ILE C CD1 1 
ATOM   5812  N  N   . GLU C 1 180 ? 50.641  -8.445  -28.929 1.00 21.70 ? 180 GLU C N   1 
ATOM   5813  C  CA  . GLU C 1 180 ? 50.112  -9.496  -29.789 1.00 22.14 ? 180 GLU C CA  1 
ATOM   5814  C  C   . GLU C 1 180 ? 49.315  -10.533 -29.013 1.00 23.40 ? 180 GLU C C   1 
ATOM   5815  O  O   . GLU C 1 180 ? 48.543  -11.298 -29.624 1.00 22.38 ? 180 GLU C O   1 
ATOM   5816  C  CB  . GLU C 1 180 ? 51.160  -10.121 -30.641 1.00 20.27 ? 180 GLU C CB  1 
ATOM   5817  C  CG  . GLU C 1 180 ? 50.613  -11.172 -31.620 1.00 24.89 ? 180 GLU C CG  1 
ATOM   5818  C  CD  . GLU C 1 180 ? 51.665  -11.578 -32.663 1.00 30.78 ? 180 GLU C CD  1 
ATOM   5819  O  OE1 . GLU C 1 180 ? 52.843  -11.210 -32.494 1.00 28.92 ? 180 GLU C OE1 1 
ATOM   5820  O  OE2 . GLU C 1 180 ? 51.335  -12.361 -33.568 1.00 29.56 ? 180 GLU C OE2 1 
ATOM   5821  N  N   A GLU C 1 181 ? 49.454  -10.521 -27.673 0.50 20.68 ? 181 GLU C N   1 
ATOM   5822  N  N   B GLU C 1 181 ? 49.484  -10.604 -27.707 0.50 22.01 ? 181 GLU C N   1 
ATOM   5823  C  CA  A GLU C 1 181 ? 48.715  -11.386 -26.701 0.50 21.38 ? 181 GLU C CA  1 
ATOM   5824  C  CA  B GLU C 1 181 ? 48.699  -11.600 -27.026 0.50 22.95 ? 181 GLU C CA  1 
ATOM   5825  C  C   A GLU C 1 181 ? 47.222  -11.027 -26.617 0.50 19.97 ? 181 GLU C C   1 
ATOM   5826  C  C   B GLU C 1 181 ? 47.220  -11.222 -27.094 0.50 22.33 ? 181 GLU C C   1 
ATOM   5827  O  O   A GLU C 1 181 ? 46.382  -11.730 -26.067 0.50 14.71 ? 181 GLU C O   1 
ATOM   5828  O  O   B GLU C 1 181 ? 46.420  -12.170 -27.062 0.50 23.26 ? 181 GLU C O   1 
ATOM   5829  C  CB  A GLU C 1 181 ? 49.382  -11.224 -25.317 0.50 20.63 ? 181 GLU C CB  1 
ATOM   5830  C  CB  B GLU C 1 181 ? 49.170  -11.815 -25.586 0.50 23.68 ? 181 GLU C CB  1 
ATOM   5831  C  CG  A GLU C 1 181 ? 50.797  -11.852 -25.234 0.50 24.15 ? 181 GLU C CG  1 
ATOM   5832  C  CG  B GLU C 1 181 ? 50.461  -12.594 -25.464 0.50 25.82 ? 181 GLU C CG  1 
ATOM   5833  C  CD  A GLU C 1 181 ? 51.430  -11.723 -23.842 0.50 21.17 ? 181 GLU C CD  1 
ATOM   5834  C  CD  B GLU C 1 181 ? 50.672  -13.113 -24.037 0.50 24.92 ? 181 GLU C CD  1 
ATOM   5835  O  OE1 A GLU C 1 181 ? 50.717  -11.385 -22.864 0.50 19.57 ? 181 GLU C OE1 1 
ATOM   5836  O  OE1 B GLU C 1 181 ? 50.958  -14.312 -23.885 0.50 29.65 ? 181 GLU C OE1 1 
ATOM   5837  O  OE2 A GLU C 1 181 ? 52.657  -11.962 -23.714 0.50 20.97 ? 181 GLU C OE2 1 
ATOM   5838  O  OE2 B GLU C 1 181 ? 50.533  -12.345 -23.073 0.50 30.98 ? 181 GLU C OE2 1 
ATOM   5839  N  N   . LEU C 1 182 ? 46.911  -9.882  -27.188 1.00 20.06 ? 182 LEU C N   1 
ATOM   5840  C  CA  . LEU C 1 182 ? 45.493  -9.352  -27.172 1.00 18.65 ? 182 LEU C CA  1 
ATOM   5841  C  C   . LEU C 1 182 ? 44.696  -9.835  -28.385 1.00 19.77 ? 182 LEU C C   1 
ATOM   5842  O  O   . LEU C 1 182 ? 43.439  -9.737  -28.441 1.00 18.93 ? 182 LEU C O   1 
ATOM   5843  C  CB  . LEU C 1 182 ? 45.487  -7.804  -27.070 1.00 20.15 ? 182 LEU C CB  1 
ATOM   5844  C  CG  . LEU C 1 182 ? 46.168  -7.137  -25.877 1.00 16.99 ? 182 LEU C CG  1 
ATOM   5845  C  CD1 . LEU C 1 182 ? 46.176  -5.590  -25.844 1.00 16.51 ? 182 LEU C CD1 1 
ATOM   5846  C  CD2 . LEU C 1 182 ? 45.721  -7.673  -24.427 1.00 21.09 ? 182 LEU C CD2 1 
ATOM   5847  N  N   . LEU C 1 183 ? 45.407  -10.403 -29.369 1.00 18.39 ? 183 LEU C N   1 
ATOM   5848  C  CA  . LEU C 1 183 ? 44.878  -10.771 -30.699 1.00 19.70 ? 183 LEU C CA  1 
ATOM   5849  C  C   . LEU C 1 183 ? 44.322  -12.137 -30.511 1.00 19.97 ? 183 LEU C C   1 
ATOM   5850  O  O   . LEU C 1 183 ? 44.751  -12.849 -29.559 1.00 22.90 ? 183 LEU C O   1 
ATOM   5851  C  CB  . LEU C 1 183 ? 45.891  -10.682 -31.908 1.00 18.94 ? 183 LEU C CB  1 
ATOM   5852  C  CG  . LEU C 1 183 ? 46.549  -9.325  -32.026 1.00 21.15 ? 183 LEU C CG  1 
ATOM   5853  C  CD1 . LEU C 1 183 ? 47.306  -9.391  -33.293 1.00 26.53 ? 183 LEU C CD1 1 
ATOM   5854  C  CD2 . LEU C 1 183 ? 45.418  -8.378  -32.100 1.00 23.28 ? 183 LEU C CD2 1 
ATOM   5855  N  N   . PRO C 1 184 ? 43.278  -12.491 -31.258 1.00 21.21 ? 184 PRO C N   1 
ATOM   5856  C  CA  . PRO C 1 184 ? 42.615  -13.811 -31.214 1.00 21.12 ? 184 PRO C CA  1 
ATOM   5857  C  C   . PRO C 1 184 ? 43.346  -14.867 -31.988 1.00 24.33 ? 184 PRO C C   1 
ATOM   5858  O  O   . PRO C 1 184 ? 44.415  -14.633 -32.544 1.00 22.85 ? 184 PRO C O   1 
ATOM   5859  C  CB  . PRO C 1 184 ? 41.217  -13.534 -31.843 1.00 23.13 ? 184 PRO C CB  1 
ATOM   5860  C  CG  . PRO C 1 184 ? 41.580  -12.540 -32.833 1.00 19.41 ? 184 PRO C CG  1 
ATOM   5861  C  CD  . PRO C 1 184 ? 42.530  -11.573 -32.166 1.00 18.47 ? 184 PRO C CD  1 
ATOM   5862  N  N   . GLU C 1 185 ? 42.801  -16.059 -31.910 1.00 25.19 ? 185 GLU C N   1 
ATOM   5863  C  CA  . GLU C 1 185 ? 43.225  -17.187 -32.714 1.00 28.98 ? 185 GLU C CA  1 
ATOM   5864  C  C   . GLU C 1 185 ? 42.939  -16.986 -34.216 1.00 28.79 ? 185 GLU C C   1 
ATOM   5865  O  O   . GLU C 1 185 ? 41.964  -16.219 -34.621 1.00 27.92 ? 185 GLU C O   1 
ATOM   5866  C  CB  . GLU C 1 185 ? 42.439  -18.411 -32.267 1.00 29.77 ? 185 GLU C CB  1 
ATOM   5867  C  CG  . GLU C 1 185 ? 42.750  -18.854 -30.866 1.00 35.60 ? 185 GLU C CG  1 
ATOM   5868  C  CD  . GLU C 1 185 ? 44.069  -19.501 -30.794 1.00 44.77 ? 185 GLU C CD  1 
ATOM   5869  O  OE1 . GLU C 1 185 ? 45.079  -18.759 -30.639 1.00 49.02 ? 185 GLU C OE1 1 
ATOM   5870  O  OE2 . GLU C 1 185 ? 44.082  -20.750 -30.918 1.00 49.97 ? 185 GLU C OE2 1 
ATOM   5871  N  N   . ARG C 1 186 ? 43.791  -17.620 -35.035 1.00 27.21 ? 186 ARG C N   1 
ATOM   5872  C  CA  . ARG C 1 186 ? 43.770  -17.483 -36.505 1.00 28.40 ? 186 ARG C CA  1 
ATOM   5873  C  C   . ARG C 1 186 ? 43.585  -16.063 -37.052 1.00 26.06 ? 186 ARG C C   1 
ATOM   5874  O  O   . ARG C 1 186 ? 42.595  -15.766 -37.821 1.00 26.39 ? 186 ARG C O   1 
ATOM   5875  C  CB  . ARG C 1 186 ? 42.754  -18.420 -37.087 1.00 29.36 ? 186 ARG C CB  1 
ATOM   5876  C  CG  . ARG C 1 186 ? 42.998  -19.857 -36.672 1.00 33.61 ? 186 ARG C CG  1 
ATOM   5877  C  CD  . ARG C 1 186 ? 41.993  -20.816 -37.383 1.00 37.50 ? 186 ARG C CD  1 
ATOM   5878  N  NE  . ARG C 1 186 ? 40.647  -20.672 -36.777 1.00 48.47 ? 186 ARG C NE  1 
ATOM   5879  C  CZ  . ARG C 1 186 ? 39.496  -21.238 -37.192 1.00 52.49 ? 186 ARG C CZ  1 
ATOM   5880  N  NH1 . ARG C 1 186 ? 39.432  -22.044 -38.267 1.00 54.07 ? 186 ARG C NH1 1 
ATOM   5881  N  NH2 . ARG C 1 186 ? 38.368  -20.986 -36.508 1.00 54.72 ? 186 ARG C NH2 1 
ATOM   5882  N  N   . THR C 1 187 ? 44.546  -15.210 -36.729 1.00 25.84 ? 187 THR C N   1 
ATOM   5883  C  CA  . THR C 1 187 ? 44.451  -13.876 -37.198 1.00 22.96 ? 187 THR C CA  1 
ATOM   5884  C  C   . THR C 1 187 ? 44.357  -13.796 -38.735 1.00 21.33 ? 187 THR C C   1 
ATOM   5885  O  O   . THR C 1 187 ? 44.077  -12.732 -39.210 1.00 17.77 ? 187 THR C O   1 
ATOM   5886  C  CB  . THR C 1 187 ? 45.525  -12.970 -36.642 1.00 25.05 ? 187 THR C CB  1 
ATOM   5887  O  OG1 . THR C 1 187 ? 46.786  -13.558 -36.943 1.00 25.60 ? 187 THR C OG1 1 
ATOM   5888  C  CG2 . THR C 1 187 ? 45.354  -12.789 -35.124 1.00 25.15 ? 187 THR C CG2 1 
ATOM   5889  N  N   . ALA C 1 188 ? 44.624  -14.885 -39.473 1.00 18.78 ? 188 ALA C N   1 
ATOM   5890  C  CA  . ALA C 1 188 ? 44.542  -14.853 -40.939 1.00 19.82 ? 188 ALA C CA  1 
ATOM   5891  C  C   . ALA C 1 188 ? 43.092  -14.665 -41.405 1.00 17.02 ? 188 ALA C C   1 
ATOM   5892  O  O   . ALA C 1 188 ? 42.885  -14.258 -42.578 1.00 16.03 ? 188 ALA C O   1 
ATOM   5893  C  CB  . ALA C 1 188 ? 45.142  -16.164 -41.571 1.00 23.00 ? 188 ALA C CB  1 
ATOM   5894  N  N   . GLU C 1 189 ? 42.124  -14.913 -40.516 1.00 17.63 ? 189 GLU C N   1 
ATOM   5895  C  CA  . GLU C 1 189 ? 40.664  -14.923 -40.927 1.00 19.49 ? 189 GLU C CA  1 
ATOM   5896  C  C   . GLU C 1 189 ? 40.102  -13.580 -40.443 1.00 16.76 ? 189 GLU C C   1 
ATOM   5897  O  O   . GLU C 1 189 ? 40.097  -13.350 -39.232 1.00 15.24 ? 189 GLU C O   1 
ATOM   5898  C  CB  . GLU C 1 189 ? 39.899  -16.040 -40.276 1.00 21.94 ? 189 GLU C CB  1 
ATOM   5899  C  CG  . GLU C 1 189 ? 40.353  -17.346 -40.841 1.00 24.10 ? 189 GLU C CG  1 
ATOM   5900  C  CD  . GLU C 1 189 ? 39.893  -18.576 -40.027 1.00 32.79 ? 189 GLU C CD  1 
ATOM   5901  O  OE1 . GLU C 1 189 ? 39.013  -18.469 -39.146 1.00 32.23 ? 189 GLU C OE1 1 
ATOM   5902  O  OE2 . GLU C 1 189 ? 40.480  -19.679 -40.248 1.00 37.45 ? 189 GLU C OE2 1 
ATOM   5903  N  N   . TYR C 1 190 ? 39.814  -12.652 -41.367 1.00 14.59 ? 190 TYR C N   1 
ATOM   5904  C  CA  . TYR C 1 190 ? 39.302  -11.366 -40.931 1.00 13.27 ? 190 TYR C CA  1 
ATOM   5905  C  C   . TYR C 1 190 ? 38.374  -10.793 -42.029 1.00 12.48 ? 190 TYR C C   1 
ATOM   5906  O  O   . TYR C 1 190 ? 38.352  -11.179 -43.207 1.00 13.75 ? 190 TYR C O   1 
ATOM   5907  C  CB  . TYR C 1 190 ? 40.470  -10.404 -40.659 1.00 13.54 ? 190 TYR C CB  1 
ATOM   5908  C  CG  . TYR C 1 190 ? 41.434  -10.255 -41.818 1.00 15.42 ? 190 TYR C CG  1 
ATOM   5909  C  CD1 . TYR C 1 190 ? 41.190  -9.323  -42.857 1.00 14.61 ? 190 TYR C CD1 1 
ATOM   5910  C  CD2 . TYR C 1 190 ? 42.651  -10.999 -41.829 1.00 16.20 ? 190 TYR C CD2 1 
ATOM   5911  C  CE1 . TYR C 1 190 ? 42.150  -9.100  -43.913 1.00 14.38 ? 190 TYR C CE1 1 
ATOM   5912  C  CE2 . TYR C 1 190 ? 43.585  -10.809 -42.905 1.00 15.57 ? 190 TYR C CE2 1 
ATOM   5913  C  CZ  . TYR C 1 190 ? 43.336  -9.906  -43.904 1.00 17.07 ? 190 TYR C CZ  1 
ATOM   5914  O  OH  . TYR C 1 190 ? 44.220  -9.729  -44.939 1.00 17.99 ? 190 TYR C OH  1 
ATOM   5915  N  N   . TYR C 1 191 ? 37.633  -9.737  -41.545 1.00 11.02 ? 191 TYR C N   1 
ATOM   5916  C  CA  . TYR C 1 191 ? 36.815  -8.915  -42.420 1.00 11.67 ? 191 TYR C CA  1 
ATOM   5917  C  C   . TYR C 1 191 ? 37.606  -7.640  -42.674 1.00 10.72 ? 191 TYR C C   1 
ATOM   5918  O  O   . TYR C 1 191 ? 38.330  -7.124  -41.790 1.00 11.28 ? 191 TYR C O   1 
ATOM   5919  C  CB  . TYR C 1 191 ? 35.525  -8.521  -41.659 1.00 10.84 ? 191 TYR C CB  1 
ATOM   5920  C  CG  . TYR C 1 191 ? 34.667  -9.630  -41.127 1.00 10.69 ? 191 TYR C CG  1 
ATOM   5921  C  CD1 . TYR C 1 191 ? 33.559  -10.168 -41.852 1.00 10.14 ? 191 TYR C CD1 1 
ATOM   5922  C  CD2 . TYR C 1 191 ? 34.852  -10.039 -39.755 1.00 10.83 ? 191 TYR C CD2 1 
ATOM   5923  C  CE1 . TYR C 1 191 ? 32.805  -11.181 -41.271 1.00 10.43 ? 191 TYR C CE1 1 
ATOM   5924  C  CE2 . TYR C 1 191 ? 34.063  -11.011 -39.181 1.00 9.82  ? 191 TYR C CE2 1 
ATOM   5925  C  CZ  . TYR C 1 191 ? 33.019  -11.545 -39.929 1.00 13.50 ? 191 TYR C CZ  1 
ATOM   5926  O  OH  . TYR C 1 191 ? 32.202  -12.532 -39.382 1.00 14.37 ? 191 TYR C OH  1 
ATOM   5927  N  N   . ARG C 1 192 ? 37.379  -7.061  -43.842 1.00 11.00 ? 192 ARG C N   1 
ATOM   5928  C  CA  . ARG C 1 192 ? 38.095  -5.848  -44.243 1.00 9.84  ? 192 ARG C CA  1 
ATOM   5929  C  C   . ARG C 1 192 ? 37.152  -4.869  -44.925 1.00 9.52  ? 192 ARG C C   1 
ATOM   5930  O  O   . ARG C 1 192 ? 36.388  -5.284  -45.861 1.00 10.21 ? 192 ARG C O   1 
ATOM   5931  C  CB  . ARG C 1 192 ? 39.194  -6.230  -45.232 1.00 10.52 ? 192 ARG C CB  1 
ATOM   5932  C  CG  . ARG C 1 192 ? 39.828  -5.014  -45.981 1.00 10.85 ? 192 ARG C CG  1 
ATOM   5933  C  CD  . ARG C 1 192 ? 40.627  -4.042  -45.085 1.00 13.18 ? 192 ARG C CD  1 
ATOM   5934  N  NE  . ARG C 1 192 ? 41.632  -4.733  -44.215 1.00 12.53 ? 192 ARG C NE  1 
ATOM   5935  C  CZ  . ARG C 1 192 ? 42.787  -5.307  -44.635 1.00 14.73 ? 192 ARG C CZ  1 
ATOM   5936  N  NH1 . ARG C 1 192 ? 43.160  -5.190  -45.934 1.00 15.45 ? 192 ARG C NH1 1 
ATOM   5937  N  NH2 . ARG C 1 192 ? 43.648  -5.891  -43.753 1.00 15.64 ? 192 ARG C NH2 1 
ATOM   5938  N  N   . TYR C 1 193 ? 37.140  -3.588  -44.505 1.00 8.86  ? 193 TYR C N   1 
ATOM   5939  C  CA  . TYR C 1 193 ? 36.402  -2.599  -45.326 1.00 8.03  ? 193 TYR C CA  1 
ATOM   5940  C  C   . TYR C 1 193 ? 36.965  -1.200  -45.041 1.00 8.32  ? 193 TYR C C   1 
ATOM   5941  O  O   . TYR C 1 193 ? 37.640  -1.020  -44.002 1.00 9.42  ? 193 TYR C O   1 
ATOM   5942  C  CB  . TYR C 1 193 ? 34.848  -2.690  -45.013 1.00 8.75  ? 193 TYR C CB  1 
ATOM   5943  C  CG  . TYR C 1 193 ? 34.472  -2.132  -43.609 1.00 8.07  ? 193 TYR C CG  1 
ATOM   5944  C  CD1 . TYR C 1 193 ? 33.948  -0.837  -43.534 1.00 6.49  ? 193 TYR C CD1 1 
ATOM   5945  C  CD2 . TYR C 1 193 ? 34.663  -2.872  -42.445 1.00 7.89  ? 193 TYR C CD2 1 
ATOM   5946  C  CE1 . TYR C 1 193 ? 33.566  -0.325  -42.292 1.00 9.20  ? 193 TYR C CE1 1 
ATOM   5947  C  CE2 . TYR C 1 193 ? 34.286  -2.365  -41.178 1.00 6.51  ? 193 TYR C CE2 1 
ATOM   5948  C  CZ  . TYR C 1 193 ? 33.810  -1.065  -41.147 1.00 7.13  ? 193 TYR C CZ  1 
ATOM   5949  O  OH  . TYR C 1 193 ? 33.477  -0.466  -39.955 1.00 8.34  ? 193 TYR C OH  1 
ATOM   5950  N  N   . ARG C 1 194 ? 36.645  -0.233  -45.896 1.00 9.76  ? 194 ARG C N   1 
ATOM   5951  C  CA  . ARG C 1 194 ? 37.034  1.120   -45.694 1.00 8.42  ? 194 ARG C CA  1 
ATOM   5952  C  C   . ARG C 1 194 ? 35.946  1.815   -44.914 1.00 9.83  ? 194 ARG C C   1 
ATOM   5953  O  O   . ARG C 1 194 ? 34.754  1.804   -45.267 1.00 9.59  ? 194 ARG C O   1 
ATOM   5954  C  CB  . ARG C 1 194 ? 37.160  1.846   -47.048 1.00 10.46 ? 194 ARG C CB  1 
ATOM   5955  C  CG  . ARG C 1 194 ? 38.353  1.295   -47.742 1.00 15.38 ? 194 ARG C CG  1 
ATOM   5956  C  CD  . ARG C 1 194 ? 38.753  1.854   -49.098 1.00 27.64 ? 194 ARG C CD  1 
ATOM   5957  N  NE  . ARG C 1 194 ? 39.906  0.996   -49.477 1.00 39.42 ? 194 ARG C NE  1 
ATOM   5958  C  CZ  . ARG C 1 194 ? 41.187  1.184   -49.110 1.00 43.74 ? 194 ARG C CZ  1 
ATOM   5959  N  NH1 . ARG C 1 194 ? 41.572  2.273   -48.404 1.00 44.91 ? 194 ARG C NH1 1 
ATOM   5960  N  NH2 . ARG C 1 194 ? 42.112  0.301   -49.510 1.00 40.53 ? 194 ARG C NH2 1 
ATOM   5961  N  N   . GLY C 1 195 ? 36.327  2.478   -43.826 1.00 9.05  ? 195 GLY C N   1 
ATOM   5962  C  CA  . GLY C 1 195 ? 35.352  3.171   -42.970 1.00 8.71  ? 195 GLY C CA  1 
ATOM   5963  C  C   . GLY C 1 195 ? 35.912  4.378   -42.278 1.00 9.09  ? 195 GLY C C   1 
ATOM   5964  O  O   . GLY C 1 195 ? 36.755  5.123   -42.854 1.00 10.22 ? 195 GLY C O   1 
ATOM   5965  N  N   . SER C 1 196 ? 35.489  4.594   -40.997 1.00 8.79  ? 196 SER C N   1 
ATOM   5966  C  CA  . SER C 1 196 ? 35.746  5.897   -40.367 1.00 9.03  ? 196 SER C CA  1 
ATOM   5967  C  C   . SER C 1 196 ? 36.203  5.605   -38.921 1.00 8.61  ? 196 SER C C   1 
ATOM   5968  O  O   . SER C 1 196 ? 36.089  4.504   -38.421 1.00 9.86  ? 196 SER C O   1 
ATOM   5969  C  CB  . SER C 1 196 ? 34.479  6.764   -40.344 1.00 9.79  ? 196 SER C CB  1 
ATOM   5970  O  OG  . SER C 1 196 ? 33.556  6.316   -39.378 1.00 9.52  ? 196 SER C OG  1 
ATOM   5971  N  N   . LEU C 1 197 ? 36.724  6.647   -38.278 1.00 8.78  ? 197 LEU C N   1 
ATOM   5972  C  CA  . LEU C 1 197 ? 36.800  6.602   -36.814 1.00 10.49 ? 197 LEU C CA  1 
ATOM   5973  C  C   . LEU C 1 197 ? 35.304  6.399   -36.322 1.00 9.35  ? 197 LEU C C   1 
ATOM   5974  O  O   . LEU C 1 197 ? 34.371  6.951   -36.879 1.00 10.46 ? 197 LEU C O   1 
ATOM   5975  C  CB  . LEU C 1 197 ? 37.320  7.937   -36.160 1.00 12.84 ? 197 LEU C CB  1 
ATOM   5976  C  CG  . LEU C 1 197 ? 38.817  8.267   -36.382 1.00 11.84 ? 197 LEU C CG  1 
ATOM   5977  C  CD1 . LEU C 1 197 ? 39.096  8.829   -37.701 1.00 15.64 ? 197 LEU C CD1 1 
ATOM   5978  C  CD2 . LEU C 1 197 ? 39.156  9.261   -35.275 1.00 15.36 ? 197 LEU C CD2 1 
ATOM   5979  N  N   . THR C 1 198 ? 35.168  5.652   -35.237 1.00 8.97  ? 198 THR C N   1 
ATOM   5980  C  CA  . THR C 1 198 ? 33.848  5.478   -34.652 1.00 9.30  ? 198 THR C CA  1 
ATOM   5981  C  C   . THR C 1 198 ? 33.545  6.528   -33.577 1.00 12.13 ? 198 THR C C   1 
ATOM   5982  O  O   . THR C 1 198 ? 32.449  6.522   -32.936 1.00 12.05 ? 198 THR C O   1 
ATOM   5983  C  CB  . THR C 1 198 ? 33.685  4.141   -34.032 1.00 9.60  ? 198 THR C CB  1 
ATOM   5984  O  OG1 . THR C 1 198 ? 34.612  4.020   -32.981 1.00 9.60  ? 198 THR C OG1 1 
ATOM   5985  C  CG2 . THR C 1 198 ? 33.925  2.915   -34.978 1.00 9.18  ? 198 THR C CG2 1 
ATOM   5986  N  N   . THR C 1 199 ? 34.526  7.419   -33.346 1.00 12.46 ? 199 THR C N   1 
ATOM   5987  C  CA  . THR C 1 199 ? 34.332  8.587   -32.465 1.00 12.15 ? 199 THR C CA  1 
ATOM   5988  C  C   . THR C 1 199 ? 34.602  9.826   -33.193 1.00 12.11 ? 199 THR C C   1 
ATOM   5989  O  O   . THR C 1 199 ? 35.321  9.783   -34.210 1.00 12.08 ? 199 THR C O   1 
ATOM   5990  C  CB  . THR C 1 199 ? 35.424  8.543   -31.321 1.00 15.10 ? 199 THR C CB  1 
ATOM   5991  O  OG1 . THR C 1 199 ? 36.731  8.487   -31.930 1.00 16.54 ? 199 THR C OG1 1 
ATOM   5992  C  CG2 . THR C 1 199 ? 35.355  7.315   -30.512 1.00 12.10 ? 199 THR C CG2 1 
ATOM   5993  N  N   . PRO C 1 200 ? 34.157  10.974  -32.667 1.00 10.54 ? 200 PRO C N   1 
ATOM   5994  C  CA  . PRO C 1 200 ? 34.534  12.245  -33.275 1.00 12.49 ? 200 PRO C CA  1 
ATOM   5995  C  C   . PRO C 1 200 ? 36.058  12.279  -33.430 1.00 12.07 ? 200 PRO C C   1 
ATOM   5996  O  O   . PRO C 1 200 ? 36.750  11.764  -32.564 1.00 15.32 ? 200 PRO C O   1 
ATOM   5997  C  CB  . PRO C 1 200 ? 33.970  13.294  -32.270 1.00 10.60 ? 200 PRO C CB  1 
ATOM   5998  C  CG  . PRO C 1 200 ? 32.824  12.592  -31.642 1.00 12.52 ? 200 PRO C CG  1 
ATOM   5999  C  CD  . PRO C 1 200 ? 33.225  11.115  -31.542 1.00 11.38 ? 200 PRO C CD  1 
ATOM   6000  N  N   . PRO C 1 201 ? 36.531  12.916  -34.515 1.00 12.76 ? 201 PRO C N   1 
ATOM   6001  C  CA  . PRO C 1 201 ? 35.767  13.575  -35.573 1.00 12.91 ? 201 PRO C CA  1 
ATOM   6002  C  C   . PRO C 1 201 ? 35.199  12.729  -36.747 1.00 10.08 ? 201 PRO C C   1 
ATOM   6003  O  O   . PRO C 1 201 ? 34.679  13.294  -37.705 1.00 12.38 ? 201 PRO C O   1 
ATOM   6004  C  CB  . PRO C 1 201 ? 36.734  14.643  -36.154 1.00 12.02 ? 201 PRO C CB  1 
ATOM   6005  C  CG  . PRO C 1 201 ? 37.917  14.624  -35.185 1.00 15.52 ? 201 PRO C CG  1 
ATOM   6006  C  CD  . PRO C 1 201 ? 38.001  13.179  -34.648 1.00 12.69 ? 201 PRO C CD  1 
ATOM   6007  N  N   . CYS C 1 202 ? 35.246  11.395  -36.575 1.00 10.41 ? 202 CYS C N   1 
ATOM   6008  C  CA  . CYS C 1 202 ? 34.583  10.428  -37.503 1.00 11.22 ? 202 CYS C CA  1 
ATOM   6009  C  C   . CYS C 1 202 ? 35.163  10.464  -38.867 1.00 10.48 ? 202 CYS C C   1 
ATOM   6010  O  O   . CYS C 1 202 ? 34.456  10.179  -39.831 1.00 11.05 ? 202 CYS C O   1 
ATOM   6011  C  CB  . CYS C 1 202 ? 33.027  10.668  -37.611 1.00 11.55 ? 202 CYS C CB  1 
ATOM   6012  S  SG  . CYS C 1 202 ? 32.124  10.631  -36.008 1.00 10.78 ? 202 CYS C SG  1 
ATOM   6013  N  N   . ASN C 1 203 ? 36.435  10.889  -39.039 1.00 10.87 ? 203 ASN C N   1 
ATOM   6014  C  CA  . ASN C 1 203 ? 36.967  10.999  -40.368 1.00 11.28 ? 203 ASN C CA  1 
ATOM   6015  C  C   . ASN C 1 203 ? 36.917  9.671   -41.153 1.00 10.15 ? 203 ASN C C   1 
ATOM   6016  O  O   . ASN C 1 203 ? 37.172  8.615   -40.538 1.00 10.02 ? 203 ASN C O   1 
ATOM   6017  C  CB  . ASN C 1 203 ? 38.425  11.542  -40.331 1.00 13.71 ? 203 ASN C CB  1 
ATOM   6018  C  CG  . ASN C 1 203 ? 38.569  12.769  -39.392 1.00 12.15 ? 203 ASN C CG  1 
ATOM   6019  O  OD1 . ASN C 1 203 ? 38.621  12.629  -38.175 1.00 16.09 ? 203 ASN C OD1 1 
ATOM   6020  N  ND2 . ASN C 1 203 ? 38.452  13.923  -39.943 1.00 17.24 ? 203 ASN C ND2 1 
ATOM   6021  N  N   . PRO C 1 204 ? 36.531  9.773   -42.438 1.00 9.03  ? 204 PRO C N   1 
ATOM   6022  C  CA  . PRO C 1 204 ? 36.372  8.494   -43.243 1.00 9.98  ? 204 PRO C CA  1 
ATOM   6023  C  C   . PRO C 1 204 ? 37.741  8.070   -43.768 1.00 9.96  ? 204 PRO C C   1 
ATOM   6024  O  O   . PRO C 1 204 ? 37.915  7.872   -45.004 1.00 12.04 ? 204 PRO C O   1 
ATOM   6025  C  CB  . PRO C 1 204 ? 35.463  8.930   -44.368 1.00 11.90 ? 204 PRO C CB  1 
ATOM   6026  C  CG  . PRO C 1 204 ? 35.845  10.440  -44.621 1.00 10.66 ? 204 PRO C CG  1 
ATOM   6027  C  CD  . PRO C 1 204 ? 36.017  10.980  -43.166 1.00 10.93 ? 204 PRO C CD  1 
ATOM   6028  N  N   . THR C 1 205 ? 38.642  7.816   -42.860 1.00 9.45  ? 205 THR C N   1 
ATOM   6029  C  CA  . THR C 1 205 ? 40.067  7.639   -43.171 1.00 11.27 ? 205 THR C CA  1 
ATOM   6030  C  C   . THR C 1 205 ? 40.656  6.328   -42.598 1.00 10.83 ? 205 THR C C   1 
ATOM   6031  O  O   . THR C 1 205 ? 41.930  6.073   -42.584 1.00 11.82 ? 205 THR C O   1 
ATOM   6032  C  CB  . THR C 1 205 ? 40.875  8.848   -42.589 1.00 10.83 ? 205 THR C CB  1 
ATOM   6033  O  OG1 . THR C 1 205 ? 40.674  8.870   -41.210 1.00 12.64 ? 205 THR C OG1 1 
ATOM   6034  C  CG2 . THR C 1 205 ? 40.502  10.120  -43.319 1.00 15.24 ? 205 THR C CG2 1 
ATOM   6035  N  N   . VAL C 1 206 ? 39.802  5.350   -42.185 1.00 11.91 ? 206 VAL C N   1 
ATOM   6036  C  CA  . VAL C 1 206 ? 40.255  4.169   -41.530 1.00 9.76  ? 206 VAL C CA  1 
ATOM   6037  C  C   . VAL C 1 206 ? 40.085  2.938   -42.386 1.00 9.66  ? 206 VAL C C   1 
ATOM   6038  O  O   . VAL C 1 206 ? 38.978  2.608   -42.846 1.00 10.84 ? 206 VAL C O   1 
ATOM   6039  C  CB  . VAL C 1 206 ? 39.459  3.922   -40.204 1.00 9.69  ? 206 VAL C CB  1 
ATOM   6040  C  CG1 . VAL C 1 206 ? 39.916  2.622   -39.601 1.00 9.30  ? 206 VAL C CG1 1 
ATOM   6041  C  CG2 . VAL C 1 206 ? 39.659  5.105   -39.238 1.00 11.94 ? 206 VAL C CG2 1 
ATOM   6042  N  N   A LEU C 1 207 ? 41.173  2.193   -42.597 0.50 9.84  ? 207 LEU C N   1 
ATOM   6043  N  N   B LEU C 1 207 ? 41.150  2.189   -42.507 0.50 8.83  ? 207 LEU C N   1 
ATOM   6044  C  CA  A LEU C 1 207 ? 41.089  0.796   -43.116 0.50 9.73  ? 207 LEU C CA  1 
ATOM   6045  C  CA  B LEU C 1 207 ? 41.125  0.874   -43.103 0.50 9.03  ? 207 LEU C CA  1 
ATOM   6046  C  C   A LEU C 1 207 ? 40.785  -0.081  -41.938 0.50 10.07 ? 207 LEU C C   1 
ATOM   6047  C  C   B LEU C 1 207 ? 40.857  -0.177  -42.014 0.50 9.96  ? 207 LEU C C   1 
ATOM   6048  O  O   A LEU C 1 207 ? 41.598  -0.178  -40.995 0.50 7.72  ? 207 LEU C O   1 
ATOM   6049  O  O   B LEU C 1 207 ? 41.764  -0.474  -41.192 0.50 8.87  ? 207 LEU C O   1 
ATOM   6050  C  CB  A LEU C 1 207 ? 42.402  0.328   -43.798 0.50 12.25 ? 207 LEU C CB  1 
ATOM   6051  C  CB  B LEU C 1 207 ? 42.499  0.719   -43.731 0.50 11.34 ? 207 LEU C CB  1 
ATOM   6052  C  CG  A LEU C 1 207 ? 42.334  -0.883  -44.725 0.50 12.25 ? 207 LEU C CG  1 
ATOM   6053  C  CG  B LEU C 1 207 ? 42.482  -0.430  -44.719 0.50 11.03 ? 207 LEU C CG  1 
ATOM   6054  C  CD1 A LEU C 1 207 ? 41.473  -0.611  -45.943 0.50 10.58 ? 207 LEU C CD1 1 
ATOM   6055  C  CD1 B LEU C 1 207 ? 43.785  -0.452  -45.501 0.50 17.11 ? 207 LEU C CD1 1 
ATOM   6056  C  CD2 A LEU C 1 207 ? 43.721  -1.453  -45.206 0.50 11.72 ? 207 LEU C CD2 1 
ATOM   6057  C  CD2 B LEU C 1 207 ? 42.245  -1.768  -44.073 0.50 14.85 ? 207 LEU C CD2 1 
ATOM   6058  N  N   . TRP C 1 208 ? 39.629  -0.739  -41.940 1.00 10.10 ? 208 TRP C N   1 
ATOM   6059  C  CA  . TRP C 1 208 ? 39.277  -1.627  -40.815 1.00 7.84  ? 208 TRP C CA  1 
ATOM   6060  C  C   . TRP C 1 208 ? 39.619  -3.048  -41.078 1.00 9.86  ? 208 TRP C C   1 
ATOM   6061  O  O   . TRP C 1 208 ? 39.365  -3.585  -42.197 1.00 10.06 ? 208 TRP C O   1 
ATOM   6062  C  CB  . TRP C 1 208 ? 37.724  -1.566  -40.637 1.00 8.22  ? 208 TRP C CB  1 
ATOM   6063  C  CG  . TRP C 1 208 ? 37.290  -0.299  -39.870 1.00 8.21  ? 208 TRP C CG  1 
ATOM   6064  C  CD1 . TRP C 1 208 ? 36.845  0.862   -40.314 1.00 9.01  ? 208 TRP C CD1 1 
ATOM   6065  C  CD2 . TRP C 1 208 ? 37.382  -0.180  -38.426 1.00 6.80  ? 208 TRP C CD2 1 
ATOM   6066  N  NE1 . TRP C 1 208 ? 36.693  1.731   -39.305 1.00 10.80 ? 208 TRP C NE1 1 
ATOM   6067  C  CE2 . TRP C 1 208 ? 37.014  1.129   -38.122 1.00 7.73  ? 208 TRP C CE2 1 
ATOM   6068  C  CE3 . TRP C 1 208 ? 37.793  -1.046  -37.432 1.00 9.99  ? 208 TRP C CE3 1 
ATOM   6069  C  CZ2 . TRP C 1 208 ? 37.009  1.658   -36.772 1.00 10.08 ? 208 TRP C CZ2 1 
ATOM   6070  C  CZ3 . TRP C 1 208 ? 37.722  -0.602  -36.055 1.00 9.39  ? 208 TRP C CZ3 1 
ATOM   6071  C  CH2 . TRP C 1 208 ? 37.337  0.753   -35.763 1.00 9.26  ? 208 TRP C CH2 1 
ATOM   6072  N  N   . THR C 1 209 ? 40.188  -3.702  -40.082 1.00 9.59  ? 209 THR C N   1 
ATOM   6073  C  CA  . THR C 1 209 ? 40.373  -5.114  -40.083 1.00 10.28 ? 209 THR C CA  1 
ATOM   6074  C  C   . THR C 1 209 ? 39.746  -5.681  -38.850 1.00 11.76 ? 209 THR C C   1 
ATOM   6075  O  O   . THR C 1 209 ? 40.206  -5.250  -37.707 1.00 11.01 ? 209 THR C O   1 
ATOM   6076  C  CB  . THR C 1 209 ? 41.903  -5.470  -40.042 1.00 10.82 ? 209 THR C CB  1 
ATOM   6077  O  OG1 . THR C 1 209 ? 42.465  -5.017  -41.274 1.00 10.03 ? 209 THR C OG1 1 
ATOM   6078  C  CG2 . THR C 1 209 ? 42.070  -7.016  -39.999 1.00 11.68 ? 209 THR C CG2 1 
ATOM   6079  N  N   . VAL C 1 210 ? 38.643  -6.466  -38.994 1.00 11.08 ? 210 VAL C N   1 
ATOM   6080  C  CA  . VAL C 1 210 ? 37.965  -6.962  -37.790 1.00 10.08 ? 210 VAL C CA  1 
ATOM   6081  C  C   . VAL C 1 210 ? 38.233  -8.439  -37.814 1.00 11.90 ? 210 VAL C C   1 
ATOM   6082  O  O   . VAL C 1 210 ? 37.940  -9.140  -38.763 1.00 11.45 ? 210 VAL C O   1 
ATOM   6083  C  CB  . VAL C 1 210 ? 36.439  -6.722  -37.861 1.00 9.80  ? 210 VAL C CB  1 
ATOM   6084  C  CG1 . VAL C 1 210 ? 35.685  -7.400  -36.614 1.00 10.82 ? 210 VAL C CG1 1 
ATOM   6085  C  CG2 . VAL C 1 210 ? 36.206  -5.219  -38.002 1.00 11.22 ? 210 VAL C CG2 1 
ATOM   6086  N  N   . PHE C 1 211 ? 38.908  -8.955  -36.752 1.00 12.83 ? 211 PHE C N   1 
ATOM   6087  C  CA  . PHE C 1 211 ? 39.149  -10.373 -36.894 1.00 11.87 ? 211 PHE C CA  1 
ATOM   6088  C  C   . PHE C 1 211 ? 37.886  -11.237 -36.762 1.00 12.39 ? 211 PHE C C   1 
ATOM   6089  O  O   . PHE C 1 211 ? 36.996  -10.891 -36.023 1.00 14.36 ? 211 PHE C O   1 
ATOM   6090  C  CB  . PHE C 1 211 ? 40.203  -10.806 -35.800 1.00 13.07 ? 211 PHE C CB  1 
ATOM   6091  C  CG  . PHE C 1 211 ? 41.605  -10.207 -36.019 1.00 11.18 ? 211 PHE C CG  1 
ATOM   6092  C  CD1 . PHE C 1 211 ? 42.393  -10.686 -37.118 1.00 14.20 ? 211 PHE C CD1 1 
ATOM   6093  C  CD2 . PHE C 1 211 ? 42.075  -9.154  -35.262 1.00 11.88 ? 211 PHE C CD2 1 
ATOM   6094  C  CE1 . PHE C 1 211 ? 43.639  -10.126 -37.364 1.00 15.13 ? 211 PHE C CE1 1 
ATOM   6095  C  CE2 . PHE C 1 211 ? 43.423  -8.585  -35.560 1.00 14.68 ? 211 PHE C CE2 1 
ATOM   6096  C  CZ  . PHE C 1 211 ? 44.104  -9.124  -36.620 1.00 14.27 ? 211 PHE C CZ  1 
ATOM   6097  N  N   A ARG C 1 212 ? 37.869  -12.394 -37.430 0.50 13.24 ? 212 ARG C N   1 
ATOM   6098  N  N   B ARG C 1 212 ? 37.833  -12.382 -37.441 0.50 12.89 ? 212 ARG C N   1 
ATOM   6099  C  CA  A ARG C 1 212 ? 36.705  -13.277 -37.574 0.50 14.74 ? 212 ARG C CA  1 
ATOM   6100  C  CA  B ARG C 1 212 ? 36.626  -13.200 -37.500 0.50 14.84 ? 212 ARG C CA  1 
ATOM   6101  C  C   A ARG C 1 212 ? 36.360  -13.980 -36.228 0.50 14.97 ? 212 ARG C C   1 
ATOM   6102  C  C   B ARG C 1 212 ? 36.370  -13.748 -36.073 0.50 14.35 ? 212 ARG C C   1 
ATOM   6103  O  O   A ARG C 1 212 ? 35.181  -14.276 -35.947 0.50 14.66 ? 212 ARG C O   1 
ATOM   6104  O  O   B ARG C 1 212 ? 35.275  -13.683 -35.555 0.50 14.05 ? 212 ARG C O   1 
ATOM   6105  C  CB  A ARG C 1 212 ? 37.008  -14.363 -38.552 0.50 15.56 ? 212 ARG C CB  1 
ATOM   6106  C  CB  B ARG C 1 212 ? 36.825  -14.364 -38.424 0.50 14.00 ? 212 ARG C CB  1 
ATOM   6107  C  CG  A ARG C 1 212 ? 35.802  -15.234 -38.995 0.50 18.64 ? 212 ARG C CG  1 
ATOM   6108  C  CG  B ARG C 1 212 ? 35.546  -15.082 -38.971 0.50 15.36 ? 212 ARG C CG  1 
ATOM   6109  C  CD  A ARG C 1 212 ? 36.259  -16.714 -39.196 0.50 23.50 ? 212 ARG C CD  1 
ATOM   6110  C  CD  B ARG C 1 212 ? 35.896  -16.453 -39.642 0.50 18.51 ? 212 ARG C CD  1 
ATOM   6111  N  NE  A ARG C 1 212 ? 35.135  -17.642 -39.281 0.50 25.83 ? 212 ARG C NE  1 
ATOM   6112  N  NE  B ARG C 1 212 ? 34.704  -16.981 -40.278 0.50 18.29 ? 212 ARG C NE  1 
ATOM   6113  C  CZ  A ARG C 1 212 ? 35.027  -18.772 -38.577 0.50 31.26 ? 212 ARG C CZ  1 
ATOM   6114  C  CZ  B ARG C 1 212 ? 34.632  -18.054 -41.060 0.50 17.39 ? 212 ARG C CZ  1 
ATOM   6115  N  NH1 A ARG C 1 212 ? 35.990  -19.172 -37.741 0.50 29.90 ? 212 ARG C NH1 1 
ATOM   6116  N  NH1 B ARG C 1 212 ? 35.681  -18.827 -41.327 0.50 23.94 ? 212 ARG C NH1 1 
ATOM   6117  N  NH2 A ARG C 1 212 ? 33.955  -19.533 -38.731 0.50 31.03 ? 212 ARG C NH2 1 
ATOM   6118  N  NH2 B ARG C 1 212 ? 33.454  -18.317 -41.554 0.50 19.33 ? 212 ARG C NH2 1 
ATOM   6119  N  N   . ASN C 1 213 ? 37.442  -14.299 -35.466 1.00 15.85 ? 213 ASN C N   1 
ATOM   6120  C  CA  . ASN C 1 213 ? 37.294  -15.004 -34.122 1.00 15.79 ? 213 ASN C CA  1 
ATOM   6121  C  C   . ASN C 1 213 ? 37.456  -14.112 -32.929 1.00 16.63 ? 213 ASN C C   1 
ATOM   6122  O  O   . ASN C 1 213 ? 38.332  -13.252 -32.890 1.00 17.57 ? 213 ASN C O   1 
ATOM   6123  C  CB  . ASN C 1 213 ? 38.331  -16.176 -34.027 1.00 17.52 ? 213 ASN C CB  1 
ATOM   6124  C  CG  . ASN C 1 213 ? 38.276  -17.070 -35.242 1.00 18.98 ? 213 ASN C CG  1 
ATOM   6125  O  OD1 . ASN C 1 213 ? 39.326  -17.278 -35.913 1.00 23.67 ? 213 ASN C OD1 1 
ATOM   6126  N  ND2 . ASN C 1 213 ? 37.094  -17.545 -35.632 1.00 22.27 ? 213 ASN C ND2 1 
ATOM   6127  N  N   . PRO C 1 214 ? 36.553  -14.206 -31.910 1.00 17.17 ? 214 PRO C N   1 
ATOM   6128  C  CA  . PRO C 1 214 ? 36.577  -13.306 -30.773 1.00 17.00 ? 214 PRO C CA  1 
ATOM   6129  C  C   . PRO C 1 214 ? 37.648  -13.788 -29.723 1.00 16.46 ? 214 PRO C C   1 
ATOM   6130  O  O   . PRO C 1 214 ? 38.069  -14.948 -29.873 1.00 20.63 ? 214 PRO C O   1 
ATOM   6131  C  CB  . PRO C 1 214 ? 35.196  -13.522 -30.143 1.00 17.84 ? 214 PRO C CB  1 
ATOM   6132  C  CG  . PRO C 1 214 ? 34.930  -14.912 -30.496 1.00 17.63 ? 214 PRO C CG  1 
ATOM   6133  C  CD  . PRO C 1 214 ? 35.406  -15.126 -31.900 1.00 20.44 ? 214 PRO C CD  1 
ATOM   6134  N  N   . VAL C 1 215 ? 38.021  -12.930 -28.781 1.00 18.12 ? 215 VAL C N   1 
ATOM   6135  C  CA  . VAL C 1 215 ? 38.857  -13.328 -27.553 1.00 19.37 ? 215 VAL C CA  1 
ATOM   6136  C  C   . VAL C 1 215 ? 37.841  -13.374 -26.401 1.00 22.68 ? 215 VAL C C   1 
ATOM   6137  O  O   . VAL C 1 215 ? 36.726  -12.835 -26.478 1.00 21.64 ? 215 VAL C O   1 
ATOM   6138  C  CB  . VAL C 1 215 ? 40.025  -12.419 -27.216 1.00 20.49 ? 215 VAL C CB  1 
ATOM   6139  C  CG1 . VAL C 1 215 ? 41.096  -12.488 -28.320 1.00 20.54 ? 215 VAL C CG1 1 
ATOM   6140  C  CG2 . VAL C 1 215 ? 39.535  -11.007 -26.855 1.00 19.89 ? 215 VAL C CG2 1 
ATOM   6141  N  N   . GLN C 1 216 ? 38.249  -14.115 -25.348 1.00 22.81 ? 216 GLN C N   1 
ATOM   6142  C  CA  . GLN C 1 216 ? 37.502  -14.180 -24.079 1.00 24.49 ? 216 GLN C CA  1 
ATOM   6143  C  C   . GLN C 1 216 ? 38.170  -13.448 -22.896 1.00 23.96 ? 216 GLN C C   1 
ATOM   6144  O  O   . GLN C 1 216 ? 39.431  -13.437 -22.789 1.00 23.25 ? 216 GLN C O   1 
ATOM   6145  C  CB  . GLN C 1 216 ? 37.310  -15.631 -23.735 1.00 22.75 ? 216 GLN C CB  1 
ATOM   6146  C  CG  . GLN C 1 216 ? 36.819  -16.447 -24.839 1.00 26.01 ? 216 GLN C CG  1 
ATOM   6147  C  CD  . GLN C 1 216 ? 36.051  -17.609 -24.344 1.00 33.91 ? 216 GLN C CD  1 
ATOM   6148  O  OE1 . GLN C 1 216 ? 36.338  -18.152 -23.235 1.00 33.14 ? 216 GLN C OE1 1 
ATOM   6149  N  NE2 . GLN C 1 216 ? 35.020  -17.996 -25.106 1.00 31.45 ? 216 GLN C NE2 1 
ATOM   6150  N  N   . ILE C 1 217 ? 37.363  -12.884 -22.003 1.00 24.31 ? 217 ILE C N   1 
ATOM   6151  C  CA  . ILE C 1 217 ? 37.751  -12.303 -20.755 1.00 22.54 ? 217 ILE C CA  1 
ATOM   6152  C  C   . ILE C 1 217 ? 36.733  -12.890 -19.733 1.00 24.61 ? 217 ILE C C   1 
ATOM   6153  O  O   . ILE C 1 217 ? 35.560  -13.251 -20.122 1.00 25.47 ? 217 ILE C O   1 
ATOM   6154  C  CB  . ILE C 1 217 ? 37.809  -10.705 -20.699 1.00 24.10 ? 217 ILE C CB  1 
ATOM   6155  C  CG1 . ILE C 1 217 ? 36.484  -10.049 -21.100 1.00 16.35 ? 217 ILE C CG1 1 
ATOM   6156  C  CG2 . ILE C 1 217 ? 38.934  -10.160 -21.602 1.00 24.33 ? 217 ILE C CG2 1 
ATOM   6157  C  CD1 . ILE C 1 217 ? 36.469  -8.521  -20.756 1.00 22.13 ? 217 ILE C CD1 1 
ATOM   6158  N  N   . SER C 1 218 ? 37.161  -13.112 -18.478 1.00 25.55 ? 218 SER C N   1 
ATOM   6159  C  CA  . SER C 1 218 ? 36.215  -13.770 -17.576 1.00 26.86 ? 218 SER C CA  1 
ATOM   6160  C  C   . SER C 1 218 ? 34.998  -12.815 -17.396 1.00 25.66 ? 218 SER C C   1 
ATOM   6161  O  O   . SER C 1 218 ? 35.096  -11.606 -17.623 1.00 28.08 ? 218 SER C O   1 
ATOM   6162  C  CB  . SER C 1 218 ? 36.909  -14.038 -16.204 1.00 23.04 ? 218 SER C CB  1 
ATOM   6163  O  OG  . SER C 1 218 ? 37.210  -12.770 -15.595 1.00 25.29 ? 218 SER C OG  1 
ATOM   6164  N  N   . GLN C 1 219 ? 33.913  -13.322 -16.792 1.00 28.28 ? 219 GLN C N   1 
ATOM   6165  C  CA  . GLN C 1 219 ? 32.911  -12.464 -16.161 1.00 28.00 ? 219 GLN C CA  1 
ATOM   6166  C  C   . GLN C 1 219 ? 33.421  -11.376 -15.222 1.00 26.79 ? 219 GLN C C   1 
ATOM   6167  O  O   . GLN C 1 219 ? 32.887  -10.241 -15.231 1.00 29.14 ? 219 GLN C O   1 
ATOM   6168  C  CB  . GLN C 1 219 ? 31.735  -13.306 -15.551 1.00 29.77 ? 219 GLN C CB  1 
ATOM   6169  C  CG  . GLN C 1 219 ? 30.783  -12.576 -14.590 1.00 36.37 ? 219 GLN C CG  1 
ATOM   6170  C  CD  . GLN C 1 219 ? 31.257  -12.597 -13.115 1.00 39.04 ? 219 GLN C CD  1 
ATOM   6171  O  OE1 . GLN C 1 219 ? 31.406  -13.656 -12.538 1.00 40.31 ? 219 GLN C OE1 1 
ATOM   6172  N  NE2 . GLN C 1 219 ? 31.506  -11.414 -12.530 1.00 40.07 ? 219 GLN C NE2 1 
ATOM   6173  N  N   . GLU C 1 220 ? 34.438  -11.660 -14.362 1.00 26.90 ? 220 GLU C N   1 
ATOM   6174  C  CA  . GLU C 1 220 ? 34.893  -10.572 -13.510 1.00 26.93 ? 220 GLU C CA  1 
ATOM   6175  C  C   . GLU C 1 220 ? 35.637  -9.537  -14.183 1.00 22.55 ? 220 GLU C C   1 
ATOM   6176  O  O   . GLU C 1 220 ? 35.429  -8.384  -13.844 1.00 27.85 ? 220 GLU C O   1 
ATOM   6177  C  CB  . GLU C 1 220 ? 35.672  -10.901 -12.244 1.00 27.07 ? 220 GLU C CB  1 
ATOM   6178  C  CG  . GLU C 1 220 ? 35.960  -9.615  -11.470 1.00 34.34 ? 220 GLU C CG  1 
ATOM   6179  C  CD  . GLU C 1 220 ? 34.714  -8.882  -10.916 1.00 40.73 ? 220 GLU C CD  1 
ATOM   6180  O  OE1 . GLU C 1 220 ? 34.615  -7.594  -11.004 1.00 37.43 ? 220 GLU C OE1 1 
ATOM   6181  O  OE2 . GLU C 1 220 ? 33.868  -9.613  -10.314 1.00 48.74 ? 220 GLU C OE2 1 
ATOM   6182  N  N   . GLN C 1 221 ? 36.496  -9.937  -15.108 1.00 25.49 ? 221 GLN C N   1 
ATOM   6183  C  CA  . GLN C 1 221 ? 37.235  -9.020  -15.987 1.00 23.79 ? 221 GLN C CA  1 
ATOM   6184  C  C   . GLN C 1 221 ? 36.283  -8.054  -16.734 1.00 16.44 ? 221 GLN C C   1 
ATOM   6185  O  O   . GLN C 1 221 ? 36.387  -6.744  -16.611 1.00 20.79 ? 221 GLN C O   1 
ATOM   6186  C  CB  . GLN C 1 221 ? 38.050  -9.822  -16.933 1.00 23.97 ? 221 GLN C CB  1 
ATOM   6187  C  CG  . GLN C 1 221 ? 39.412  -10.324 -16.290 1.00 24.72 ? 221 GLN C CG  1 
ATOM   6188  C  CD  . GLN C 1 221 ? 40.280  -10.943 -17.313 1.00 26.41 ? 221 GLN C CD  1 
ATOM   6189  O  OE1 . GLN C 1 221 ? 39.859  -11.897 -17.997 1.00 27.14 ? 221 GLN C OE1 1 
ATOM   6190  N  NE2 . GLN C 1 221 ? 41.503  -10.417 -17.481 1.00 24.15 ? 221 GLN C NE2 1 
ATOM   6191  N  N   . LEU C 1 222 ? 35.243  -8.643  -17.282 1.00 23.03 ? 222 LEU C N   1 
ATOM   6192  C  CA  . LEU C 1 222 ? 34.143  -7.847  -17.931 1.00 22.24 ? 222 LEU C CA  1 
ATOM   6193  C  C   . LEU C 1 222 ? 33.426  -6.821  -17.087 1.00 18.80 ? 222 LEU C C   1 
ATOM   6194  O  O   . LEU C 1 222 ? 33.387  -5.555  -17.291 1.00 19.85 ? 222 LEU C O   1 
ATOM   6195  C  CB  . LEU C 1 222 ? 33.197  -8.786  -18.600 1.00 22.15 ? 222 LEU C CB  1 
ATOM   6196  C  CG  . LEU C 1 222 ? 32.074  -8.116  -19.391 1.00 23.86 ? 222 LEU C CG  1 
ATOM   6197  C  CD1 . LEU C 1 222 ? 32.611  -7.122  -20.470 1.00 21.58 ? 222 LEU C CD1 1 
ATOM   6198  C  CD2 . LEU C 1 222 ? 31.332  -9.288  -20.045 1.00 23.39 ? 222 LEU C CD2 1 
ATOM   6199  N  N   . LEU C 1 223 ? 32.919  -7.354  -15.926 1.00 23.67 ? 223 LEU C N   1 
ATOM   6200  C  CA  . LEU C 1 223 ? 32.393  -6.582  -14.798 1.00 24.33 ? 223 LEU C CA  1 
ATOM   6201  C  C   . LEU C 1 223 ? 33.276  -5.451  -14.354 1.00 19.95 ? 223 LEU C C   1 
ATOM   6202  O  O   . LEU C 1 223 ? 32.817  -4.283  -14.234 1.00 23.45 ? 223 LEU C O   1 
ATOM   6203  C  CB  . LEU C 1 223 ? 32.191  -7.583  -13.685 1.00 26.43 ? 223 LEU C CB  1 
ATOM   6204  C  CG  . LEU C 1 223 ? 31.063  -7.345  -12.731 1.00 31.95 ? 223 LEU C CG  1 
ATOM   6205  C  CD1 . LEU C 1 223 ? 29.733  -7.220  -13.440 1.00 28.75 ? 223 LEU C CD1 1 
ATOM   6206  C  CD2 . LEU C 1 223 ? 31.127  -8.537  -11.722 1.00 32.89 ? 223 LEU C CD2 1 
ATOM   6207  N  N   . ALA C 1 224 ? 34.563  -5.773  -14.181 1.00 24.68 ? 224 ALA C N   1 
ATOM   6208  C  CA  . ALA C 1 224 ? 35.641  -4.861  -13.768 1.00 26.05 ? 224 ALA C CA  1 
ATOM   6209  C  C   . ALA C 1 224 ? 35.695  -3.708  -14.734 1.00 24.45 ? 224 ALA C C   1 
ATOM   6210  O  O   . ALA C 1 224 ? 35.541  -2.552  -14.384 1.00 27.81 ? 224 ALA C O   1 
ATOM   6211  C  CB  . ALA C 1 224 ? 37.012  -5.651  -13.678 1.00 26.57 ? 224 ALA C CB  1 
ATOM   6212  N  N   . LEU C 1 225 ? 35.784  -4.068  -16.018 1.00 26.72 ? 225 LEU C N   1 
ATOM   6213  C  CA  . LEU C 1 225 ? 35.889  -3.095  -17.096 1.00 24.78 ? 225 LEU C CA  1 
ATOM   6214  C  C   . LEU C 1 225 ? 34.649  -2.232  -17.127 1.00 20.77 ? 225 LEU C C   1 
ATOM   6215  O  O   . LEU C 1 225 ? 34.698  -0.995  -17.201 1.00 23.63 ? 225 LEU C O   1 
ATOM   6216  C  CB  . LEU C 1 225 ? 36.043  -3.865  -18.437 1.00 24.76 ? 225 LEU C CB  1 
ATOM   6217  C  CG  . LEU C 1 225 ? 36.049  -2.974  -19.677 1.00 25.19 ? 225 LEU C CG  1 
ATOM   6218  C  CD1 . LEU C 1 225 ? 37.186  -1.984  -19.615 1.00 24.59 ? 225 LEU C CD1 1 
ATOM   6219  C  CD2 . LEU C 1 225 ? 36.079  -3.782  -20.968 1.00 23.21 ? 225 LEU C CD2 1 
ATOM   6220  N  N   . GLU C 1 226 ? 33.488  -2.899  -17.017 1.00 23.98 ? 226 GLU C N   1 
ATOM   6221  C  CA  . GLU C 1 226 ? 32.172  -2.244  -16.999 1.00 26.14 ? 226 GLU C CA  1 
ATOM   6222  C  C   . GLU C 1 226 ? 31.944  -1.286  -15.796 1.00 27.69 ? 226 GLU C C   1 
ATOM   6223  O  O   . GLU C 1 226 ? 31.145  -0.340  -15.840 1.00 28.23 ? 226 GLU C O   1 
ATOM   6224  C  CB  . GLU C 1 226 ? 31.064  -3.314  -17.078 1.00 25.98 ? 226 GLU C CB  1 
ATOM   6225  C  CG  . GLU C 1 226 ? 31.070  -4.155  -18.426 1.00 25.58 ? 226 GLU C CG  1 
ATOM   6226  C  CD  . GLU C 1 226 ? 30.125  -5.364  -18.413 1.00 28.63 ? 226 GLU C CD  1 
ATOM   6227  O  OE1 . GLU C 1 226 ? 29.917  -6.111  -17.368 1.00 24.55 ? 226 GLU C OE1 1 
ATOM   6228  O  OE2 . GLU C 1 226 ? 29.625  -5.718  -19.489 1.00 25.31 ? 226 GLU C OE2 1 
ATOM   6229  N  N   . THR C 1 227 ? 32.735  -1.537  -14.742 1.00 29.34 ? 227 THR C N   1 
ATOM   6230  C  CA  . THR C 1 227 ? 32.510  -1.013  -13.379 1.00 30.92 ? 227 THR C CA  1 
ATOM   6231  C  C   . THR C 1 227 ? 33.538  0.029   -12.788 1.00 30.55 ? 227 THR C C   1 
ATOM   6232  O  O   . THR C 1 227 ? 33.285  0.576   -11.742 1.00 31.99 ? 227 THR C O   1 
ATOM   6233  C  CB  . THR C 1 227 ? 32.113  -2.188  -12.308 1.00 28.82 ? 227 THR C CB  1 
ATOM   6234  O  OG1 . THR C 1 227 ? 33.128  -3.197  -12.210 1.00 31.16 ? 227 THR C OG1 1 
ATOM   6235  C  CG2 . THR C 1 227 ? 30.758  -2.843  -12.659 1.00 32.75 ? 227 THR C CG2 1 
ATOM   6236  N  N   . ALA C 1 228 ? 34.604  0.346   -13.515 1.00 29.76 ? 228 ALA C N   1 
ATOM   6237  C  CA  . ALA C 1 228 ? 35.778  0.970   -12.924 1.00 27.43 ? 228 ALA C CA  1 
ATOM   6238  C  C   . ALA C 1 228 ? 35.848  2.482   -13.222 1.00 28.47 ? 228 ALA C C   1 
ATOM   6239  O  O   . ALA C 1 228 ? 36.352  3.236   -12.371 1.00 28.84 ? 228 ALA C O   1 
ATOM   6240  C  CB  . ALA C 1 228 ? 37.020  0.266   -13.291 1.00 28.77 ? 228 ALA C CB  1 
ATOM   6241  N  N   . LEU C 1 229 ? 35.324  2.953   -14.375 1.00 24.68 ? 229 LEU C N   1 
ATOM   6242  C  CA  . LEU C 1 229 ? 35.554  4.328   -14.757 1.00 23.43 ? 229 LEU C CA  1 
ATOM   6243  C  C   . LEU C 1 229 ? 34.412  5.264   -14.763 1.00 25.51 ? 229 LEU C C   1 
ATOM   6244  O  O   . LEU C 1 229 ? 33.222  4.899   -14.839 1.00 23.34 ? 229 LEU C O   1 
ATOM   6245  C  CB  . LEU C 1 229 ? 36.228  4.394   -16.146 1.00 23.33 ? 229 LEU C CB  1 
ATOM   6246  C  CG  . LEU C 1 229 ? 37.323  3.309   -16.343 1.00 20.82 ? 229 LEU C CG  1 
ATOM   6247  C  CD1 . LEU C 1 229 ? 37.921  3.390   -17.774 1.00 24.92 ? 229 LEU C CD1 1 
ATOM   6248  C  CD2 . LEU C 1 229 ? 38.534  3.367   -15.331 1.00 22.37 ? 229 LEU C CD2 1 
ATOM   6249  N  N   . TYR C 1 230 ? 34.784  6.519   -14.786 1.00 27.25 ? 230 TYR C N   1 
ATOM   6250  C  CA  . TYR C 1 230 ? 33.831  7.564   -14.806 1.00 31.12 ? 230 TYR C CA  1 
ATOM   6251  C  C   . TYR C 1 230 ? 34.210  8.383   -15.979 1.00 30.12 ? 230 TYR C C   1 
ATOM   6252  O  O   . TYR C 1 230 ? 35.371  8.437   -16.364 1.00 32.53 ? 230 TYR C O   1 
ATOM   6253  C  CB  . TYR C 1 230 ? 33.791  8.329   -13.428 1.00 31.68 ? 230 TYR C CB  1 
ATOM   6254  C  CG  . TYR C 1 230 ? 33.369  7.286   -12.410 1.00 36.23 ? 230 TYR C CG  1 
ATOM   6255  C  CD1 . TYR C 1 230 ? 32.045  7.215   -11.925 1.00 35.14 ? 230 TYR C CD1 1 
ATOM   6256  C  CD2 . TYR C 1 230 ? 34.257  6.258   -12.069 1.00 38.01 ? 230 TYR C CD2 1 
ATOM   6257  C  CE1 . TYR C 1 230 ? 31.662  6.158   -11.050 1.00 35.29 ? 230 TYR C CE1 1 
ATOM   6258  C  CE2 . TYR C 1 230 ? 33.901  5.217   -11.235 1.00 40.39 ? 230 TYR C CE2 1 
ATOM   6259  C  CZ  . TYR C 1 230 ? 32.620  5.181   -10.709 1.00 38.20 ? 230 TYR C CZ  1 
ATOM   6260  O  OH  . TYR C 1 230 ? 32.378  4.129   -9.880  1.00 41.86 ? 230 TYR C OH  1 
ATOM   6261  N  N   A CYS C 1 231 ? 33.218  8.979   -16.591 0.50 30.73 ? 231 CYS C N   1 
ATOM   6262  N  N   B CYS C 1 231 ? 33.238  9.061   -16.578 0.50 30.86 ? 231 CYS C N   1 
ATOM   6263  C  CA  A CYS C 1 231 ? 33.532  9.875   -17.624 0.50 30.75 ? 231 CYS C CA  1 
ATOM   6264  C  CA  B CYS C 1 231 ? 33.518  9.958   -17.694 0.50 31.32 ? 231 CYS C CA  1 
ATOM   6265  C  C   A CYS C 1 231 ? 34.188  11.078  -16.953 0.50 31.60 ? 231 CYS C C   1 
ATOM   6266  C  C   B CYS C 1 231 ? 33.697  11.437  -17.239 0.50 31.18 ? 231 CYS C C   1 
ATOM   6267  O  O   A CYS C 1 231 ? 35.338  11.367  -17.260 0.50 31.57 ? 231 CYS C O   1 
ATOM   6268  O  O   B CYS C 1 231 ? 34.062  12.340  -18.005 0.50 30.46 ? 231 CYS C O   1 
ATOM   6269  C  CB  A CYS C 1 231 ? 32.283  10.240  -18.394 0.50 30.41 ? 231 CYS C CB  1 
ATOM   6270  C  CB  B CYS C 1 231 ? 32.475  9.796   -18.810 0.50 31.33 ? 231 CYS C CB  1 
ATOM   6271  S  SG  A CYS C 1 231 ? 31.844  8.972   -19.606 0.50 25.09 ? 231 CYS C SG  1 
ATOM   6272  S  SG  B CYS C 1 231 ? 30.723  9.710   -18.315 0.50 29.70 ? 231 CYS C SG  1 
ATOM   6273  N  N   . THR C 1 232 ? 33.473  11.635  -15.950 1.00 31.91 ? 232 THR C N   1 
ATOM   6274  C  CA  . THR C 1 232 ? 33.670  12.924  -15.291 1.00 31.52 ? 232 THR C CA  1 
ATOM   6275  C  C   . THR C 1 232 ? 34.955  13.052  -14.447 1.00 32.06 ? 232 THR C C   1 
ATOM   6276  O  O   . THR C 1 232 ? 35.584  11.994  -14.027 1.00 26.13 ? 232 THR C O   1 
ATOM   6277  C  CB  . THR C 1 232 ? 32.510  13.106  -14.346 1.00 32.79 ? 232 THR C CB  1 
ATOM   6278  O  OG1 . THR C 1 232 ? 32.358  11.896  -13.578 1.00 31.83 ? 232 THR C OG1 1 
ATOM   6279  C  CG2 . THR C 1 232 ? 31.222  13.395  -15.122 1.00 34.18 ? 232 THR C CG2 1 
ATOM   6280  N  N   A HIS C 1 233 ? 35.433  14.290  -14.226 0.50 32.96 ? 233 HIS C N   1 
ATOM   6281  N  N   B HIS C 1 233 ? 35.261  14.324  -14.115 0.50 31.53 ? 233 HIS C N   1 
ATOM   6282  C  CA  A HIS C 1 233 ? 36.636  14.360  -13.382 0.50 34.72 ? 233 HIS C CA  1 
ATOM   6283  C  CA  B HIS C 1 233 ? 36.423  14.685  -13.280 0.50 32.32 ? 233 HIS C CA  1 
ATOM   6284  C  C   A HIS C 1 233 ? 36.324  14.204  -11.888 0.50 35.34 ? 233 HIS C C   1 
ATOM   6285  C  C   B HIS C 1 233 ? 36.276  14.271  -11.798 0.50 33.89 ? 233 HIS C C   1 
ATOM   6286  O  O   A HIS C 1 233 ? 35.144  14.245  -11.452 0.50 35.23 ? 233 HIS C O   1 
ATOM   6287  O  O   B HIS C 1 233 ? 35.146  14.184  -11.269 0.50 34.03 ? 233 HIS C O   1 
ATOM   6288  C  CB  A HIS C 1 233 ? 37.629  15.493  -13.695 0.50 34.91 ? 233 HIS C CB  1 
ATOM   6289  C  CB  B HIS C 1 233 ? 36.730  16.178  -13.411 0.50 31.09 ? 233 HIS C CB  1 
ATOM   6290  C  CG  A HIS C 1 233 ? 38.992  15.277  -13.086 0.50 37.13 ? 233 HIS C CG  1 
ATOM   6291  C  CG  B HIS C 1 233 ? 37.104  16.579  -14.802 0.50 30.10 ? 233 HIS C CG  1 
ATOM   6292  N  ND1 A HIS C 1 233 ? 39.537  14.022  -12.897 0.50 33.44 ? 233 HIS C ND1 1 
ATOM   6293  N  ND1 B HIS C 1 233 ? 38.377  16.409  -15.309 0.50 27.74 ? 233 HIS C ND1 1 
ATOM   6294  C  CD2 A HIS C 1 233 ? 39.923  16.158  -12.633 0.50 37.59 ? 233 HIS C CD2 1 
ATOM   6295  C  CD2 B HIS C 1 233 ? 36.367  17.117  -15.804 0.50 26.45 ? 233 HIS C CD2 1 
ATOM   6296  C  CE1 A HIS C 1 233 ? 40.730  14.134  -12.343 0.50 34.48 ? 233 HIS C CE1 1 
ATOM   6297  C  CE1 B HIS C 1 233 ? 38.409  16.856  -16.553 0.50 22.89 ? 233 HIS C CE1 1 
ATOM   6298  N  NE2 A HIS C 1 233 ? 40.989  15.419  -12.167 0.50 36.75 ? 233 HIS C NE2 1 
ATOM   6299  N  NE2 B HIS C 1 233 ? 37.204  17.278  -16.878 0.50 25.56 ? 233 HIS C NE2 1 
ATOM   6300  N  N   . MET C 1 234 ? 37.411  14.130  -11.110 1.00 36.75 ? 234 MET C N   1 
ATOM   6301  C  CA  . MET C 1 234 ? 37.563  13.450  -9.797  1.00 40.53 ? 234 MET C CA  1 
ATOM   6302  C  C   . MET C 1 234 ? 36.598  13.674  -8.624  1.00 41.99 ? 234 MET C C   1 
ATOM   6303  O  O   . MET C 1 234 ? 36.448  12.808  -7.759  1.00 42.57 ? 234 MET C O   1 
ATOM   6304  C  CB  . MET C 1 234 ? 38.951  13.836  -9.260  1.00 40.03 ? 234 MET C CB  1 
ATOM   6305  C  CG  . MET C 1 234 ? 39.867  12.658  -8.984  1.00 43.70 ? 234 MET C CG  1 
ATOM   6306  S  SD  . MET C 1 234 ? 40.410  12.507  -7.267  1.00 46.60 ? 234 MET C SD  1 
ATOM   6307  C  CE  . MET C 1 234 ? 40.996  10.810  -7.211  1.00 38.15 ? 234 MET C CE  1 
ATOM   6308  N  N   . ASP C 1 235 ? 36.011  14.855  -8.556  1.00 43.92 ? 235 ASP C N   1 
ATOM   6309  C  CA  . ASP C 1 235 ? 35.199  15.279  -7.442  1.00 45.42 ? 235 ASP C CA  1 
ATOM   6310  C  C   . ASP C 1 235 ? 34.179  16.218  -8.058  1.00 45.76 ? 235 ASP C C   1 
ATOM   6311  O  O   . ASP C 1 235 ? 33.724  17.180  -7.417  1.00 45.51 ? 235 ASP C O   1 
ATOM   6312  C  CB  . ASP C 1 235 ? 36.072  15.968  -6.347  1.00 46.93 ? 235 ASP C CB  1 
ATOM   6313  C  CG  . ASP C 1 235 ? 37.326  16.687  -6.931  1.00 48.69 ? 235 ASP C CG  1 
ATOM   6314  O  OD1 . ASP C 1 235 ? 37.188  17.505  -7.868  1.00 50.96 ? 235 ASP C OD1 1 
ATOM   6315  O  OD2 . ASP C 1 235 ? 38.459  16.441  -6.440  1.00 52.57 ? 235 ASP C OD2 1 
ATOM   6316  N  N   . ASP C 1 236 ? 33.843  15.944  -9.336  1.00 44.83 ? 236 ASP C N   1 
ATOM   6317  C  CA  . ASP C 1 236 ? 32.507  16.302  -9.843  1.00 44.25 ? 236 ASP C CA  1 
ATOM   6318  C  C   . ASP C 1 236 ? 31.576  15.746  -8.742  1.00 43.53 ? 236 ASP C C   1 
ATOM   6319  O  O   . ASP C 1 236 ? 31.695  14.557  -8.395  1.00 42.34 ? 236 ASP C O   1 
ATOM   6320  C  CB  . ASP C 1 236 ? 32.207  15.625  -11.222 1.00 43.97 ? 236 ASP C CB  1 
ATOM   6321  C  CG  . ASP C 1 236 ? 31.028  16.274  -11.965 1.00 46.72 ? 236 ASP C CG  1 
ATOM   6322  O  OD1 . ASP C 1 236 ? 30.041  16.671  -11.279 1.00 51.11 ? 236 ASP C OD1 1 
ATOM   6323  O  OD2 . ASP C 1 236 ? 31.076  16.433  -13.233 1.00 43.80 ? 236 ASP C OD2 1 
ATOM   6324  N  N   . PRO C 1 237 ? 30.674  16.589  -8.173  1.00 43.18 ? 237 PRO C N   1 
ATOM   6325  C  CA  . PRO C 1 237 ? 29.711  16.013  -7.220  1.00 42.64 ? 237 PRO C CA  1 
ATOM   6326  C  C   . PRO C 1 237 ? 28.594  15.198  -7.933  1.00 42.62 ? 237 PRO C C   1 
ATOM   6327  O  O   . PRO C 1 237 ? 27.564  14.902  -7.337  1.00 41.52 ? 237 PRO C O   1 
ATOM   6328  C  CB  . PRO C 1 237 ? 29.120  17.250  -6.518  1.00 42.57 ? 237 PRO C CB  1 
ATOM   6329  C  CG  . PRO C 1 237 ? 29.199  18.354  -7.553  1.00 42.41 ? 237 PRO C CG  1 
ATOM   6330  C  CD  . PRO C 1 237 ? 30.448  18.038  -8.388  1.00 42.98 ? 237 PRO C CD  1 
ATOM   6331  N  N   . SER C 1 238 ? 28.794  14.884  -9.212  1.00 42.72 ? 238 SER C N   1 
ATOM   6332  C  CA  . SER C 1 238 ? 27.842  14.049  -9.961  1.00 42.11 ? 238 SER C CA  1 
ATOM   6333  C  C   . SER C 1 238 ? 28.573  13.217  -11.009 1.00 41.09 ? 238 SER C C   1 
ATOM   6334  O  O   . SER C 1 238 ? 28.578  13.569  -12.199 1.00 40.68 ? 238 SER C O   1 
ATOM   6335  C  CB  . SER C 1 238 ? 26.690  14.887  -10.542 1.00 42.59 ? 238 SER C CB  1 
ATOM   6336  O  OG  . SER C 1 238 ? 27.186  16.062  -11.155 1.00 44.86 ? 238 SER C OG  1 
ATOM   6337  N  N   . PRO C 1 239 ? 29.228  12.163  -10.533 1.00 38.59 ? 239 PRO C N   1 
ATOM   6338  C  CA  . PRO C 1 239 ? 30.081  11.318  -11.367 1.00 36.98 ? 239 PRO C CA  1 
ATOM   6339  C  C   . PRO C 1 239 ? 29.265  10.336  -12.182 1.00 36.71 ? 239 PRO C C   1 
ATOM   6340  O  O   . PRO C 1 239 ? 28.282  9.775   -11.698 1.00 36.82 ? 239 PRO C O   1 
ATOM   6341  C  CB  . PRO C 1 239 ? 30.933  10.568  -10.341 1.00 36.92 ? 239 PRO C CB  1 
ATOM   6342  C  CG  . PRO C 1 239 ? 30.076  10.503  -9.129  1.00 36.69 ? 239 PRO C CG  1 
ATOM   6343  C  CD  . PRO C 1 239 ? 29.292  11.785  -9.110  1.00 38.82 ? 239 PRO C CD  1 
ATOM   6344  N  N   . ARG C 1 240 ? 29.683  10.137  -13.423 1.00 35.91 ? 240 ARG C N   1 
ATOM   6345  C  CA  . ARG C 1 240 ? 29.002  9.234   -14.325 1.00 35.12 ? 240 ARG C CA  1 
ATOM   6346  C  C   . ARG C 1 240 ? 29.921  8.086   -14.718 1.00 33.12 ? 240 ARG C C   1 
ATOM   6347  O  O   . ARG C 1 240 ? 31.079  8.277   -15.081 1.00 34.53 ? 240 ARG C O   1 
ATOM   6348  C  CB  . ARG C 1 240 ? 28.414  9.940   -15.550 1.00 36.51 ? 240 ARG C CB  1 
ATOM   6349  C  CG  . ARG C 1 240 ? 28.819  11.401  -15.745 1.00 40.36 ? 240 ARG C CG  1 
ATOM   6350  C  CD  . ARG C 1 240 ? 28.709  11.733  -17.256 1.00 47.89 ? 240 ARG C CD  1 
ATOM   6351  N  NE  . ARG C 1 240 ? 29.597  12.840  -17.648 1.00 54.40 ? 240 ARG C NE  1 
ATOM   6352  C  CZ  . ARG C 1 240 ? 30.124  13.050  -18.862 1.00 56.47 ? 240 ARG C CZ  1 
ATOM   6353  N  NH1 . ARG C 1 240 ? 29.875  12.227  -19.891 1.00 58.12 ? 240 ARG C NH1 1 
ATOM   6354  N  NH2 . ARG C 1 240 ? 30.922  14.107  -19.052 1.00 55.65 ? 240 ARG C NH2 1 
ATOM   6355  N  N   . GLU C 1 241 ? 29.373  6.887   -14.602 1.00 29.55 ? 241 GLU C N   1 
ATOM   6356  C  CA  . GLU C 1 241 ? 30.021  5.681   -14.937 1.00 26.26 ? 241 GLU C CA  1 
ATOM   6357  C  C   . GLU C 1 241 ? 30.405  5.689   -16.439 1.00 23.26 ? 241 GLU C C   1 
ATOM   6358  O  O   . GLU C 1 241 ? 29.608  6.160   -17.268 1.00 24.90 ? 241 GLU C O   1 
ATOM   6359  C  CB  . GLU C 1 241 ? 29.093  4.509   -14.733 1.00 26.88 ? 241 GLU C CB  1 
ATOM   6360  C  CG  . GLU C 1 241 ? 28.928  4.068   -13.300 1.00 31.50 ? 241 GLU C CG  1 
ATOM   6361  C  CD  . GLU C 1 241 ? 27.572  3.447   -13.109 1.00 38.67 ? 241 GLU C CD  1 
ATOM   6362  O  OE1 . GLU C 1 241 ? 26.594  3.904   -13.746 1.00 44.26 ? 241 GLU C OE1 1 
ATOM   6363  O  OE2 . GLU C 1 241 ? 27.478  2.465   -12.359 1.00 45.90 ? 241 GLU C OE2 1 
ATOM   6364  N  N   A MET C 1 242 ? 31.590  5.090   -16.690 0.50 21.59 ? 242 MET C N   1 
ATOM   6365  N  N   B MET C 1 242 ? 31.598  5.318   -16.769 0.50 21.58 ? 242 MET C N   1 
ATOM   6366  C  CA  A MET C 1 242 ? 32.095  4.746   -18.045 0.50 19.86 ? 242 MET C CA  1 
ATOM   6367  C  CA  B MET C 1 242 ? 31.856  5.262   -18.173 0.50 17.67 ? 242 MET C CA  1 
ATOM   6368  C  C   A MET C 1 242 ? 31.436  3.474   -18.535 0.50 18.36 ? 242 MET C C   1 
ATOM   6369  C  C   B MET C 1 242 ? 31.457  3.831   -18.592 0.50 18.12 ? 242 MET C C   1 
ATOM   6370  O  O   A MET C 1 242 ? 31.927  2.299   -18.330 0.50 20.51 ? 242 MET C O   1 
ATOM   6371  O  O   B MET C 1 242 ? 32.120  2.907   -18.360 0.50 17.64 ? 242 MET C O   1 
ATOM   6372  C  CB  A MET C 1 242 ? 33.652  4.701   -18.182 0.50 17.56 ? 242 MET C CB  1 
ATOM   6373  C  CB  B MET C 1 242 ? 33.308  5.585   -18.393 0.50 15.07 ? 242 MET C CB  1 
ATOM   6374  C  CG  A MET C 1 242 ? 34.156  4.764   -19.713 0.50 19.12 ? 242 MET C CG  1 
ATOM   6375  C  CG  B MET C 1 242 ? 33.592  5.654   -19.852 0.50 11.70 ? 242 MET C CG  1 
ATOM   6376  S  SD  A MET C 1 242 ? 35.868  5.329   -19.968 0.50 19.03 ? 242 MET C SD  1 
ATOM   6377  S  SD  B MET C 1 242 ? 35.312  5.580   -20.022 0.50 14.48 ? 242 MET C SD  1 
ATOM   6378  C  CE  A MET C 1 242 ? 35.705  7.118   -19.559 0.50 9.64  ? 242 MET C CE  1 
ATOM   6379  C  CE  B MET C 1 242 ? 35.876  4.059   -19.844 0.50 2.00  ? 242 MET C CE  1 
ATOM   6380  N  N   . ILE C 1 243 ? 30.291  3.728   -19.210 1.00 19.22 ? 243 ILE C N   1 
ATOM   6381  C  CA  . ILE C 1 243 ? 29.615  2.548   -19.702 1.00 18.13 ? 243 ILE C CA  1 
ATOM   6382  C  C   . ILE C 1 243 ? 28.948  2.888   -21.086 1.00 15.36 ? 243 ILE C C   1 
ATOM   6383  O  O   . ILE C 1 243 ? 28.711  4.052   -21.399 1.00 15.50 ? 243 ILE C O   1 
ATOM   6384  C  CB  . ILE C 1 243 ? 28.480  2.017   -18.702 1.00 18.97 ? 243 ILE C CB  1 
ATOM   6385  C  CG1 . ILE C 1 243 ? 27.505  3.124   -18.443 1.00 20.71 ? 243 ILE C CG1 1 
ATOM   6386  C  CG2 . ILE C 1 243 ? 29.089  1.355   -17.403 1.00 18.79 ? 243 ILE C CG2 1 
ATOM   6387  C  CD1 . ILE C 1 243 ? 26.267  2.770   -17.575 1.00 20.06 ? 243 ILE C CD1 1 
ATOM   6388  N  N   . ASN C 1 244 ? 28.671  1.784   -21.811 1.00 15.15 ? 244 ASN C N   1 
ATOM   6389  C  CA  . ASN C 1 244 ? 27.966  1.936   -23.164 1.00 15.89 ? 244 ASN C CA  1 
ATOM   6390  C  C   . ASN C 1 244 ? 28.659  2.938   -24.112 1.00 14.52 ? 244 ASN C C   1 
ATOM   6391  O  O   . ASN C 1 244 ? 28.072  3.802   -24.715 1.00 15.78 ? 244 ASN C O   1 
ATOM   6392  C  CB  . ASN C 1 244 ? 26.497  2.314   -22.866 1.00 16.88 ? 244 ASN C CB  1 
ATOM   6393  C  CG  . ASN C 1 244 ? 25.781  1.279   -21.993 1.00 14.04 ? 244 ASN C CG  1 
ATOM   6394  O  OD1 . ASN C 1 244 ? 25.974  0.083   -22.044 1.00 18.90 ? 244 ASN C OD1 1 
ATOM   6395  N  ND2 . ASN C 1 244 ? 25.022  1.846   -21.015 1.00 21.34 ? 244 ASN C ND2 1 
ATOM   6396  N  N   . ASN C 1 245 ? 30.002  2.803   -24.117 1.00 16.90 ? 245 ASN C N   1 
ATOM   6397  C  CA  . ASN C 1 245 ? 30.822  3.788   -24.859 1.00 16.14 ? 245 ASN C CA  1 
ATOM   6398  C  C   . ASN C 1 245 ? 31.169  3.247   -26.251 1.00 15.01 ? 245 ASN C C   1 
ATOM   6399  O  O   . ASN C 1 245 ? 32.329  3.162   -26.652 1.00 16.20 ? 245 ASN C O   1 
ATOM   6400  C  CB  . ASN C 1 245 ? 32.059  4.206   -24.057 1.00 17.06 ? 245 ASN C CB  1 
ATOM   6401  C  CG  . ASN C 1 245 ? 32.935  3.043   -23.730 1.00 14.28 ? 245 ASN C CG  1 
ATOM   6402  O  OD1 . ASN C 1 245 ? 32.614  1.839   -23.683 1.00 16.65 ? 245 ASN C OD1 1 
ATOM   6403  N  ND2 . ASN C 1 245 ? 34.228  3.391   -23.464 1.00 18.57 ? 245 ASN C ND2 1 
ATOM   6404  N  N   . PHE C 1 246 ? 30.102  2.871   -26.940 1.00 13.07 ? 246 PHE C N   1 
ATOM   6405  C  CA  . PHE C 1 246 ? 30.202  2.302   -28.329 1.00 12.09 ? 246 PHE C CA  1 
ATOM   6406  C  C   . PHE C 1 246 ? 29.232  3.111   -29.119 1.00 12.15 ? 246 PHE C C   1 
ATOM   6407  O  O   . PHE C 1 246 ? 28.160  3.593   -28.621 1.00 11.81 ? 246 PHE C O   1 
ATOM   6408  C  CB  . PHE C 1 246 ? 29.863  0.777   -28.390 1.00 11.77 ? 246 PHE C CB  1 
ATOM   6409  C  CG  . PHE C 1 246 ? 28.443  0.463   -27.911 1.00 11.20 ? 246 PHE C CG  1 
ATOM   6410  C  CD1 . PHE C 1 246 ? 27.377  0.296   -28.830 1.00 12.10 ? 246 PHE C CD1 1 
ATOM   6411  C  CD2 . PHE C 1 246 ? 28.140  0.344   -26.526 1.00 14.73 ? 246 PHE C CD2 1 
ATOM   6412  C  CE1 . PHE C 1 246 ? 26.096  0.024   -28.382 1.00 16.11 ? 246 PHE C CE1 1 
ATOM   6413  C  CE2 . PHE C 1 246 ? 26.840  0.072   -26.086 1.00 15.73 ? 246 PHE C CE2 1 
ATOM   6414  C  CZ  . PHE C 1 246 ? 25.808  -0.101  -27.012 1.00 12.16 ? 246 PHE C CZ  1 
ATOM   6415  N  N   . ARG C 1 247 ? 29.521  3.231   -30.426 1.00 10.51 ? 247 ARG C N   1 
ATOM   6416  C  CA  . ARG C 1 247 ? 28.577  3.887   -31.355 1.00 9.83  ? 247 ARG C CA  1 
ATOM   6417  C  C   . ARG C 1 247 ? 27.609  2.832   -31.916 1.00 9.39  ? 247 ARG C C   1 
ATOM   6418  O  O   . ARG C 1 247 ? 27.994  1.651   -32.138 1.00 9.20  ? 247 ARG C O   1 
ATOM   6419  C  CB  . ARG C 1 247 ? 29.361  4.505   -32.531 1.00 10.05 ? 247 ARG C CB  1 
ATOM   6420  C  CG  . ARG C 1 247 ? 28.627  5.559   -33.347 1.00 10.03 ? 247 ARG C CG  1 
ATOM   6421  C  CD  . ARG C 1 247 ? 29.425  6.009   -34.578 1.00 6.52  ? 247 ARG C CD  1 
ATOM   6422  N  NE  . ARG C 1 247 ? 28.862  7.143   -35.202 1.00 9.28  ? 247 ARG C NE  1 
ATOM   6423  C  CZ  . ARG C 1 247 ? 29.339  7.699   -36.326 1.00 8.13  ? 247 ARG C CZ  1 
ATOM   6424  N  NH1 . ARG C 1 247 ? 30.380  7.135   -36.941 1.00 9.90  ? 247 ARG C NH1 1 
ATOM   6425  N  NH2 . ARG C 1 247 ? 28.788  8.812   -36.765 1.00 8.76  ? 247 ARG C NH2 1 
ATOM   6426  N  N   . GLN C 1 248 ? 26.336  3.270   -32.164 1.00 8.57  ? 248 GLN C N   1 
ATOM   6427  C  CA  . GLN C 1 248 ? 25.395  2.365   -32.877 1.00 9.10  ? 248 GLN C CA  1 
ATOM   6428  C  C   . GLN C 1 248 ? 25.906  2.033   -34.273 1.00 8.49  ? 248 GLN C C   1 
ATOM   6429  O  O   . GLN C 1 248 ? 26.634  2.856   -34.879 1.00 9.80  ? 248 GLN C O   1 
ATOM   6430  C  CB  . GLN C 1 248 ? 24.016  3.022   -33.027 1.00 9.81  ? 248 GLN C CB  1 
ATOM   6431  C  CG  . GLN C 1 248 ? 23.393  3.390   -31.645 1.00 9.18  ? 248 GLN C CG  1 
ATOM   6432  C  CD  . GLN C 1 248 ? 23.030  2.132   -30.847 1.00 10.02 ? 248 GLN C CD  1 
ATOM   6433  O  OE1 . GLN C 1 248 ? 23.720  1.729   -29.884 1.00 12.88 ? 248 GLN C OE1 1 
ATOM   6434  N  NE2 . GLN C 1 248 ? 21.853  1.545   -31.181 1.00 11.86 ? 248 GLN C NE2 1 
ATOM   6435  N  N   . VAL C 1 249 ? 25.479  0.873   -34.838 1.00 7.88  ? 249 VAL C N   1 
ATOM   6436  C  CA  . VAL C 1 249 ? 25.944  0.590   -36.196 1.00 8.65  ? 249 VAL C CA  1 
ATOM   6437  C  C   . VAL C 1 249 ? 25.332  1.597   -37.208 1.00 8.97  ? 249 VAL C C   1 
ATOM   6438  O  O   . VAL C 1 249 ? 24.199  2.128   -37.005 1.00 8.59  ? 249 VAL C O   1 
ATOM   6439  C  CB  . VAL C 1 249 ? 25.588  -0.834  -36.594 1.00 9.36  ? 249 VAL C CB  1 
ATOM   6440  C  CG1 . VAL C 1 249 ? 26.403  -1.900  -35.836 1.00 10.55 ? 249 VAL C CG1 1 
ATOM   6441  C  CG2 . VAL C 1 249 ? 24.098  -1.049  -36.531 1.00 11.13 ? 249 VAL C CG2 1 
ATOM   6442  N  N   . GLN C 1 250 ? 26.032  1.799   -38.302 1.00 7.71  ? 250 GLN C N   1 
ATOM   6443  C  CA  . GLN C 1 250 ? 25.626  2.782   -39.307 1.00 8.14  ? 250 GLN C CA  1 
ATOM   6444  C  C   . GLN C 1 250 ? 25.073  2.079   -40.482 1.00 8.56  ? 250 GLN C C   1 
ATOM   6445  O  O   . GLN C 1 250 ? 25.456  0.886   -40.736 1.00 10.46 ? 250 GLN C O   1 
ATOM   6446  C  CB  . GLN C 1 250 ? 26.925  3.501   -39.790 1.00 8.13  ? 250 GLN C CB  1 
ATOM   6447  C  CG  . GLN C 1 250 ? 27.753  4.050   -38.534 1.00 9.09  ? 250 GLN C CG  1 
ATOM   6448  C  CD  . GLN C 1 250 ? 27.044  5.250   -37.943 1.00 8.23  ? 250 GLN C CD  1 
ATOM   6449  O  OE1 . GLN C 1 250 ? 26.732  6.304   -38.636 1.00 8.85  ? 250 GLN C OE1 1 
ATOM   6450  N  NE2 . GLN C 1 250 ? 26.714  5.104   -36.665 1.00 9.65  ? 250 GLN C NE2 1 
ATOM   6451  N  N   . LYS C 1 251 ? 24.204  2.802   -41.217 1.00 8.80  ? 251 LYS C N   1 
ATOM   6452  C  CA  . LYS C 1 251 ? 23.783  2.207   -42.531 1.00 8.40  ? 251 LYS C CA  1 
ATOM   6453  C  C   . LYS C 1 251 ? 24.985  1.908   -43.402 1.00 10.84 ? 251 LYS C C   1 
ATOM   6454  O  O   . LYS C 1 251 ? 26.009  2.638   -43.405 1.00 10.16 ? 251 LYS C O   1 
ATOM   6455  C  CB  . LYS C 1 251 ? 22.798  3.123   -43.211 1.00 9.42  ? 251 LYS C CB  1 
ATOM   6456  C  CG  . LYS C 1 251 ? 21.419  3.089   -42.468 1.00 10.64 ? 251 LYS C CG  1 
ATOM   6457  C  CD  . LYS C 1 251 ? 20.452  4.018   -43.125 1.00 12.24 ? 251 LYS C CD  1 
ATOM   6458  C  CE  . LYS C 1 251 ? 18.967  3.734   -42.735 1.00 8.76  ? 251 LYS C CE  1 
ATOM   6459  N  NZ  . LYS C 1 251 ? 18.758  3.855   -41.257 1.00 8.43  ? 251 LYS C NZ  1 
ATOM   6460  N  N   . PHE C 1 252 ? 24.856  0.839   -44.209 1.00 10.79 ? 252 PHE C N   1 
ATOM   6461  C  CA  . PHE C 1 252 ? 25.917  0.389   -45.097 1.00 10.15 ? 252 PHE C CA  1 
ATOM   6462  C  C   . PHE C 1 252 ? 25.235  -0.251  -46.267 1.00 13.41 ? 252 PHE C C   1 
ATOM   6463  O  O   . PHE C 1 252 ? 24.924  -1.432  -46.166 1.00 17.53 ? 252 PHE C O   1 
ATOM   6464  C  CB  . PHE C 1 252 ? 26.738  -0.628  -44.361 1.00 13.16 ? 252 PHE C CB  1 
ATOM   6465  C  CG  . PHE C 1 252 ? 28.017  -1.072  -45.034 1.00 9.73  ? 252 PHE C CG  1 
ATOM   6466  C  CD1 . PHE C 1 252 ? 29.151  -0.348  -44.991 1.00 10.03 ? 252 PHE C CD1 1 
ATOM   6467  C  CD2 . PHE C 1 252 ? 28.021  -2.361  -45.632 1.00 14.81 ? 252 PHE C CD2 1 
ATOM   6468  C  CE1 . PHE C 1 252 ? 30.375  -0.788  -45.515 1.00 12.43 ? 252 PHE C CE1 1 
ATOM   6469  C  CE2 . PHE C 1 252 ? 29.259  -2.859  -46.209 1.00 13.35 ? 252 PHE C CE2 1 
ATOM   6470  C  CZ  . PHE C 1 252 ? 30.408  -2.071  -46.131 1.00 11.50 ? 252 PHE C CZ  1 
ATOM   6471  N  N   . ASP C 1 253 ? 24.999  0.520   -47.286 1.00 17.34 ? 253 ASP C N   1 
ATOM   6472  C  CA  . ASP C 1 253 ? 24.160  0.122   -48.420 1.00 16.87 ? 253 ASP C CA  1 
ATOM   6473  C  C   . ASP C 1 253 ? 24.921  0.131   -49.725 1.00 14.96 ? 253 ASP C C   1 
ATOM   6474  O  O   . ASP C 1 253 ? 25.782  0.985   -49.980 1.00 16.46 ? 253 ASP C O   1 
ATOM   6475  C  CB  . ASP C 1 253 ? 22.935  1.029   -48.447 1.00 22.49 ? 253 ASP C CB  1 
ATOM   6476  C  CG  . ASP C 1 253 ? 21.834  0.501   -49.339 1.00 25.84 ? 253 ASP C CG  1 
ATOM   6477  O  OD1 . ASP C 1 253 ? 21.289  -0.593  -49.082 1.00 27.67 ? 253 ASP C OD1 1 
ATOM   6478  O  OD2 . ASP C 1 253 ? 21.502  1.233   -50.272 1.00 29.45 ? 253 ASP C OD2 1 
ATOM   6479  N  N   A GLU C 1 254 ? 24.637  -0.935  -50.479 0.50 16.26 ? 254 GLU C N   1 
ATOM   6480  N  N   B GLU C 1 254 ? 24.657  -0.882  -50.531 0.50 15.34 ? 254 GLU C N   1 
ATOM   6481  C  CA  A GLU C 1 254 ? 25.231  -1.270  -51.771 0.50 17.18 ? 254 GLU C CA  1 
ATOM   6482  C  CA  B GLU C 1 254 ? 25.308  -0.998  -51.806 0.50 15.45 ? 254 GLU C CA  1 
ATOM   6483  C  C   A GLU C 1 254 ? 26.771  -1.335  -51.724 0.50 16.75 ? 254 GLU C C   1 
ATOM   6484  C  C   B GLU C 1 254 ? 26.839  -0.996  -51.628 0.50 14.77 ? 254 GLU C C   1 
ATOM   6485  O  O   A GLU C 1 254 ? 27.471  -1.073  -52.695 0.50 17.95 ? 254 GLU C O   1 
ATOM   6486  O  O   B GLU C 1 254 ? 27.595  -0.368  -52.418 0.50 14.90 ? 254 GLU C O   1 
ATOM   6487  C  CB  A GLU C 1 254 ? 24.753  -0.295  -52.854 0.50 17.32 ? 254 GLU C CB  1 
ATOM   6488  C  CB  B GLU C 1 254 ? 24.857  0.149   -52.721 0.50 16.17 ? 254 GLU C CB  1 
ATOM   6489  C  CG  A GLU C 1 254 ? 23.218  -0.234  -53.076 0.50 19.95 ? 254 GLU C CG  1 
ATOM   6490  C  CG  B GLU C 1 254 ? 23.300  0.224   -53.009 0.50 17.51 ? 254 GLU C CG  1 
ATOM   6491  C  CD  A GLU C 1 254 ? 22.859  0.663   -54.239 0.50 21.48 ? 254 GLU C CD  1 
ATOM   6492  C  CD  B GLU C 1 254 ? 22.766  -1.090  -53.619 0.50 21.53 ? 254 GLU C CD  1 
ATOM   6493  O  OE1 A GLU C 1 254 ? 23.782  1.098   -54.947 0.50 29.36 ? 254 GLU C OE1 1 
ATOM   6494  O  OE1 B GLU C 1 254 ? 23.529  -1.808  -54.289 0.50 28.78 ? 254 GLU C OE1 1 
ATOM   6495  O  OE2 A GLU C 1 254 ? 21.642  0.946   -54.462 0.50 28.50 ? 254 GLU C OE2 1 
ATOM   6496  O  OE2 B GLU C 1 254 ? 21.580  -1.423  -53.457 0.50 23.77 ? 254 GLU C OE2 1 
ATOM   6497  N  N   . ARG C 1 255 ? 27.267  -1.685  -50.553 1.00 14.32 ? 255 ARG C N   1 
ATOM   6498  C  CA  . ARG C 1 255 ? 28.699  -1.888  -50.333 1.00 14.32 ? 255 ARG C CA  1 
ATOM   6499  C  C   . ARG C 1 255 ? 28.958  -3.317  -49.870 1.00 12.55 ? 255 ARG C C   1 
ATOM   6500  O  O   . ARG C 1 255 ? 28.125  -4.034  -49.316 1.00 15.28 ? 255 ARG C O   1 
ATOM   6501  C  CB  . ARG C 1 255 ? 29.224  -0.883  -49.302 1.00 12.98 ? 255 ARG C CB  1 
ATOM   6502  C  CG  . ARG C 1 255 ? 29.092  0.581   -49.733 1.00 14.99 ? 255 ARG C CG  1 
ATOM   6503  C  CD  . ARG C 1 255 ? 29.746  1.529   -48.682 1.00 14.62 ? 255 ARG C CD  1 
ATOM   6504  N  NE  . ARG C 1 255 ? 31.125  1.130   -48.533 1.00 15.10 ? 255 ARG C NE  1 
ATOM   6505  C  CZ  . ARG C 1 255 ? 31.841  1.398   -47.420 1.00 15.69 ? 255 ARG C CZ  1 
ATOM   6506  N  NH1 . ARG C 1 255 ? 31.246  2.135   -46.439 1.00 14.29 ? 255 ARG C NH1 1 
ATOM   6507  N  NH2 . ARG C 1 255 ? 33.063  0.950   -47.361 1.00 14.07 ? 255 ARG C NH2 1 
ATOM   6508  N  N   . LEU C 1 256 ? 30.236  -3.725  -50.010 1.00 14.62 ? 256 LEU C N   1 
ATOM   6509  C  CA  . LEU C 1 256 ? 30.661  -5.050  -49.590 1.00 13.51 ? 256 LEU C CA  1 
ATOM   6510  C  C   . LEU C 1 256 ? 31.699  -4.977  -48.419 1.00 13.16 ? 256 LEU C C   1 
ATOM   6511  O  O   . LEU C 1 256 ? 32.407  -3.978  -48.217 1.00 13.23 ? 256 LEU C O   1 
ATOM   6512  C  CB  . LEU C 1 256 ? 31.404  -5.762  -50.737 1.00 14.76 ? 256 LEU C CB  1 
ATOM   6513  C  CG  . LEU C 1 256 ? 30.483  -6.055  -51.982 1.00 19.69 ? 256 LEU C CG  1 
ATOM   6514  C  CD1 . LEU C 1 256 ? 31.315  -6.416  -53.149 1.00 22.13 ? 256 LEU C CD1 1 
ATOM   6515  C  CD2 . LEU C 1 256 ? 29.515  -7.205  -51.655 1.00 21.07 ? 256 LEU C CD2 1 
ATOM   6516  N  N   . VAL C 1 257 ? 31.661  -6.064  -47.648 1.00 13.40 ? 257 VAL C N   1 
ATOM   6517  C  CA  . VAL C 1 257 ? 32.731  -6.325  -46.639 1.00 12.39 ? 257 VAL C CA  1 
ATOM   6518  C  C   . VAL C 1 257 ? 33.544  -7.483  -47.272 1.00 13.96 ? 257 VAL C C   1 
ATOM   6519  O  O   . VAL C 1 257 ? 32.981  -8.579  -47.545 1.00 14.41 ? 257 VAL C O   1 
ATOM   6520  C  CB  . VAL C 1 257 ? 32.212  -6.668  -45.336 1.00 12.17 ? 257 VAL C CB  1 
ATOM   6521  C  CG1 . VAL C 1 257 ? 33.342  -7.175  -44.371 1.00 13.85 ? 257 VAL C CG1 1 
ATOM   6522  C  CG2 . VAL C 1 257 ? 31.517  -5.416  -44.698 1.00 14.07 ? 257 VAL C CG2 1 
ATOM   6523  N  N   . TYR C 1 258 ? 34.876  -7.291  -47.376 1.00 11.08 ? 258 TYR C N   1 
ATOM   6524  C  CA  . TYR C 1 258 ? 35.719  -8.310  -48.053 1.00 12.34 ? 258 TYR C CA  1 
ATOM   6525  C  C   . TYR C 1 258 ? 36.247  -9.226  -46.918 1.00 12.50 ? 258 TYR C C   1 
ATOM   6526  O  O   . TYR C 1 258 ? 36.504  -8.807  -45.801 1.00 12.60 ? 258 TYR C O   1 
ATOM   6527  C  CB  . TYR C 1 258 ? 36.856  -7.616  -48.790 1.00 13.42 ? 258 TYR C CB  1 
ATOM   6528  C  CG  . TYR C 1 258 ? 36.262  -6.729  -49.833 1.00 16.17 ? 258 TYR C CG  1 
ATOM   6529  C  CD1 . TYR C 1 258 ? 35.755  -7.283  -51.030 1.00 16.54 ? 258 TYR C CD1 1 
ATOM   6530  C  CD2 . TYR C 1 258 ? 36.120  -5.374  -49.619 1.00 16.76 ? 258 TYR C CD2 1 
ATOM   6531  C  CE1 . TYR C 1 258 ? 35.126  -6.509  -51.973 1.00 18.87 ? 258 TYR C CE1 1 
ATOM   6532  C  CE2 . TYR C 1 258 ? 35.551  -4.563  -50.597 1.00 18.69 ? 258 TYR C CE2 1 
ATOM   6533  C  CZ  . TYR C 1 258 ? 35.034  -5.115  -51.766 1.00 21.11 ? 258 TYR C CZ  1 
ATOM   6534  O  OH  . TYR C 1 258 ? 34.387  -4.246  -52.703 1.00 21.14 ? 258 TYR C OH  1 
ATOM   6535  N  N   . THR C 1 259 ? 36.315  -10.546 -47.204 1.00 13.33 ? 259 THR C N   1 
ATOM   6536  C  CA  . THR C 1 259 ? 36.704  -11.499 -46.206 1.00 12.57 ? 259 THR C CA  1 
ATOM   6537  C  C   . THR C 1 259 ? 37.940  -12.285 -46.750 1.00 13.41 ? 259 THR C C   1 
ATOM   6538  O  O   . THR C 1 259 ? 38.051  -12.568 -47.955 1.00 15.47 ? 259 THR C O   1 
ATOM   6539  C  CB  . THR C 1 259 ? 35.587  -12.465 -45.868 1.00 13.98 ? 259 THR C CB  1 
ATOM   6540  O  OG1 . THR C 1 259 ? 35.177  -13.218 -47.090 1.00 15.62 ? 259 THR C OG1 1 
ATOM   6541  C  CG2 . THR C 1 259 ? 34.363  -11.689 -45.280 1.00 13.40 ? 259 THR C CG2 1 
ATOM   6542  N  N   . SER C 1 260 ? 38.854  -12.534 -45.779 1.00 14.49 ? 260 SER C N   1 
ATOM   6543  C  CA  . SER C 1 260 ? 40.097  -13.255 -46.129 1.00 16.78 ? 260 SER C CA  1 
ATOM   6544  C  C   . SER C 1 260 ? 39.770  -14.744 -46.092 1.00 19.45 ? 260 SER C C   1 
ATOM   6545  O  O   . SER C 1 260 ? 40.681  -15.602 -46.311 1.00 22.84 ? 260 SER C O   1 
ATOM   6546  C  CB  . SER C 1 260 ? 41.183  -12.957 -45.150 1.00 16.74 ? 260 SER C CB  1 
ATOM   6547  O  OG  . SER C 1 260 ? 40.792  -13.510 -43.925 1.00 15.08 ? 260 SER C OG  1 
ATOM   6548  N  N   . PHE C 1 261 ? 38.555  -15.091 -45.796 1.00 17.87 ? 261 PHE C N   1 
ATOM   6549  C  CA  . PHE C 1 261 ? 38.141  -16.502 -45.668 1.00 21.24 ? 261 PHE C CA  1 
ATOM   6550  C  C   . PHE C 1 261 ? 36.950  -16.773 -46.528 1.00 24.51 ? 261 PHE C C   1 
ATOM   6551  O  O   . PHE C 1 261 ? 36.214  -15.850 -46.890 1.00 25.05 ? 261 PHE C O   1 
ATOM   6552  C  CB  . PHE C 1 261 ? 37.801  -16.802 -44.192 1.00 19.84 ? 261 PHE C CB  1 
ATOM   6553  C  CG  . PHE C 1 261 ? 36.767  -15.864 -43.605 1.00 19.98 ? 261 PHE C CG  1 
ATOM   6554  C  CD1 . PHE C 1 261 ? 35.420  -16.114 -43.729 1.00 19.08 ? 261 PHE C CD1 1 
ATOM   6555  C  CD2 . PHE C 1 261 ? 37.172  -14.715 -42.990 1.00 17.91 ? 261 PHE C CD2 1 
ATOM   6556  C  CE1 . PHE C 1 261 ? 34.411  -15.244 -43.142 1.00 22.34 ? 261 PHE C CE1 1 
ATOM   6557  C  CE2 . PHE C 1 261 ? 36.214  -13.826 -42.373 1.00 15.96 ? 261 PHE C CE2 1 
ATOM   6558  C  CZ  . PHE C 1 261 ? 34.887  -14.046 -42.473 1.00 18.28 ? 261 PHE C CZ  1 
ATOM   6559  N  N   . SER C 1 262 ? 36.711  -18.041 -46.887 1.00 28.95 ? 262 SER C N   1 
ATOM   6560  C  CA  . SER C 1 262 ? 35.381  -18.409 -47.459 1.00 34.53 ? 262 SER C CA  1 
ATOM   6561  C  C   . SER C 1 262 ? 34.449  -19.381 -46.615 1.00 35.87 ? 262 SER C C   1 
ATOM   6562  O  O   . SER C 1 262 ? 34.741  -20.580 -46.439 1.00 38.86 ? 262 SER C O   1 
ATOM   6563  C  CB  . SER C 1 262 ? 35.571  -19.014 -48.856 1.00 33.78 ? 262 SER C CB  1 
ATOM   6564  O  OG  . SER C 1 262 ? 34.291  -19.357 -49.372 1.00 40.38 ? 262 SER C OG  1 
ATOM   6565  N  N   . LYS D 1 3   ? 13.999  19.493  -45.247 1.00 28.86 ? 3   LYS D N   1 
ATOM   6566  C  CA  . LYS D 1 3   ? 14.536  18.686  -46.314 1.00 25.98 ? 3   LYS D CA  1 
ATOM   6567  C  C   . LYS D 1 3   ? 15.337  17.525  -45.685 1.00 22.16 ? 3   LYS D C   1 
ATOM   6568  O  O   . LYS D 1 3   ? 16.269  17.020  -46.325 1.00 21.48 ? 3   LYS D O   1 
ATOM   6569  C  CB  . LYS D 1 3   ? 15.435  19.454  -47.310 1.00 27.83 ? 3   LYS D CB  1 
ATOM   6570  C  CG  . LYS D 1 3   ? 16.319  20.590  -46.798 1.00 29.54 ? 3   LYS D CG  1 
ATOM   6571  C  CD  . LYS D 1 3   ? 17.203  21.075  -47.967 1.00 31.67 ? 3   LYS D CD  1 
ATOM   6572  C  CE  . LYS D 1 3   ? 18.456  21.696  -47.495 1.00 38.05 ? 3   LYS D CE  1 
ATOM   6573  N  NZ  . LYS D 1 3   ? 19.431  20.601  -47.044 1.00 29.71 ? 3   LYS D NZ  1 
ATOM   6574  N  N   . TRP D 1 4   ? 14.954  17.098  -44.449 1.00 14.60 ? 4   TRP D N   1 
ATOM   6575  C  CA  . TRP D 1 4   ? 15.626  15.919  -43.871 1.00 12.34 ? 4   TRP D CA  1 
ATOM   6576  C  C   . TRP D 1 4   ? 15.309  14.701  -44.777 1.00 11.54 ? 4   TRP D C   1 
ATOM   6577  O  O   . TRP D 1 4   ? 14.340  14.639  -45.517 1.00 11.76 ? 4   TRP D O   1 
ATOM   6578  C  CB  . TRP D 1 4   ? 15.124  15.678  -42.474 1.00 10.00 ? 4   TRP D CB  1 
ATOM   6579  C  CG  . TRP D 1 4   ? 13.659  15.425  -42.319 1.00 9.50  ? 4   TRP D CG  1 
ATOM   6580  C  CD1 . TRP D 1 4   ? 12.618  16.290  -42.043 1.00 10.92 ? 4   TRP D CD1 1 
ATOM   6581  C  CD2 . TRP D 1 4   ? 13.043  14.078  -42.259 1.00 10.20 ? 4   TRP D CD2 1 
ATOM   6582  N  NE1 . TRP D 1 4   ? 11.449  15.628  -41.880 1.00 13.56 ? 4   TRP D NE1 1 
ATOM   6583  C  CE2 . TRP D 1 4   ? 11.674  14.264  -42.013 1.00 9.52  ? 4   TRP D CE2 1 
ATOM   6584  C  CE3 . TRP D 1 4   ? 13.516  12.760  -42.444 1.00 9.57  ? 4   TRP D CE3 1 
ATOM   6585  C  CZ2 . TRP D 1 4   ? 10.808  13.223  -41.869 1.00 10.97 ? 4   TRP D CZ2 1 
ATOM   6586  C  CZ3 . TRP D 1 4   ? 12.611  11.653  -42.278 1.00 10.34 ? 4   TRP D CZ3 1 
ATOM   6587  C  CH2 . TRP D 1 4   ? 11.269  11.908  -42.010 1.00 9.89  ? 4   TRP D CH2 1 
ATOM   6588  N  N   . THR D 1 5   ? 16.262  13.776  -44.744 1.00 11.93 ? 5   THR D N   1 
ATOM   6589  C  CA  . THR D 1 5   ? 16.247  12.540  -45.592 1.00 9.60  ? 5   THR D CA  1 
ATOM   6590  C  C   . THR D 1 5   ? 16.675  11.362  -44.740 1.00 11.72 ? 5   THR D C   1 
ATOM   6591  O  O   . THR D 1 5   ? 17.061  11.527  -43.553 1.00 9.58  ? 5   THR D O   1 
ATOM   6592  C  CB  . THR D 1 5   ? 17.152  12.595  -46.834 1.00 12.49 ? 5   THR D CB  1 
ATOM   6593  O  OG1 . THR D 1 5   ? 18.469  12.613  -46.318 1.00 11.62 ? 5   THR D OG1 1 
ATOM   6594  C  CG2 . THR D 1 5   ? 16.813  13.878  -47.631 1.00 12.42 ? 5   THR D CG2 1 
ATOM   6595  N  N   . TYR D 1 6   ? 16.741  10.199  -45.385 1.00 9.25  ? 6   TYR D N   1 
ATOM   6596  C  CA  . TYR D 1 6   ? 17.394  9.085   -44.789 1.00 9.76  ? 6   TYR D CA  1 
ATOM   6597  C  C   . TYR D 1 6   ? 18.745  8.646   -45.371 1.00 10.13 ? 6   TYR D C   1 
ATOM   6598  O  O   . TYR D 1 6   ? 19.333  7.588   -45.053 1.00 10.47 ? 6   TYR D O   1 
ATOM   6599  C  CB  . TYR D 1 6   ? 16.472  7.853   -44.899 1.00 9.35  ? 6   TYR D CB  1 
ATOM   6600  C  CG  . TYR D 1 6   ? 15.196  7.931   -44.041 1.00 7.50  ? 6   TYR D CG  1 
ATOM   6601  C  CD1 . TYR D 1 6   ? 15.239  7.390   -42.739 1.00 8.62  ? 6   TYR D CD1 1 
ATOM   6602  C  CD2 . TYR D 1 6   ? 13.988  8.467   -44.500 1.00 7.96  ? 6   TYR D CD2 1 
ATOM   6603  C  CE1 . TYR D 1 6   ? 14.104  7.381   -41.969 1.00 7.68  ? 6   TYR D CE1 1 
ATOM   6604  C  CE2 . TYR D 1 6   ? 12.846  8.491   -43.738 1.00 7.42  ? 6   TYR D CE2 1 
ATOM   6605  C  CZ  . TYR D 1 6   ? 12.930  7.981   -42.450 1.00 6.33  ? 6   TYR D CZ  1 
ATOM   6606  O  OH  . TYR D 1 6   ? 11.794  7.965   -41.737 1.00 7.94  ? 6   TYR D OH  1 
ATOM   6607  N  N   . PHE D 1 7   ? 19.226  9.497   -46.271 1.00 10.84 ? 7   PHE D N   1 
ATOM   6608  C  CA  . PHE D 1 7   ? 20.411  9.139   -47.015 1.00 15.27 ? 7   PHE D CA  1 
ATOM   6609  C  C   . PHE D 1 7   ? 21.177  10.427  -47.390 1.00 12.86 ? 7   PHE D C   1 
ATOM   6610  O  O   . PHE D 1 7   ? 20.584  11.352  -48.014 1.00 16.29 ? 7   PHE D O   1 
ATOM   6611  C  CB  . PHE D 1 7   ? 20.054  8.320   -48.285 1.00 16.19 ? 7   PHE D CB  1 
ATOM   6612  C  CG  . PHE D 1 7   ? 21.275  7.884   -49.055 1.00 19.62 ? 7   PHE D CG  1 
ATOM   6613  C  CD1 . PHE D 1 7   ? 22.149  6.932   -48.559 1.00 18.98 ? 7   PHE D CD1 1 
ATOM   6614  C  CD2 . PHE D 1 7   ? 21.568  8.547   -50.250 1.00 23.49 ? 7   PHE D CD2 1 
ATOM   6615  C  CE1 . PHE D 1 7   ? 23.326  6.583   -49.240 1.00 22.53 ? 7   PHE D CE1 1 
ATOM   6616  C  CE2 . PHE D 1 7   ? 22.712  8.198   -50.978 1.00 30.58 ? 7   PHE D CE2 1 
ATOM   6617  C  CZ  . PHE D 1 7   ? 23.561  7.198   -50.480 1.00 24.26 ? 7   PHE D CZ  1 
ATOM   6618  N  N   . GLY D 1 8   ? 22.474  10.437  -47.027 1.00 12.83 ? 8   GLY D N   1 
ATOM   6619  C  CA  . GLY D 1 8   ? 23.312  11.530  -47.544 1.00 16.17 ? 8   GLY D CA  1 
ATOM   6620  C  C   . GLY D 1 8   ? 23.464  12.632  -46.506 1.00 16.24 ? 8   GLY D C   1 
ATOM   6621  O  O   . GLY D 1 8   ? 23.245  12.431  -45.291 1.00 16.12 ? 8   GLY D O   1 
ATOM   6622  N  N   . PRO D 1 9   ? 23.876  13.825  -46.944 1.00 18.42 ? 9   PRO D N   1 
ATOM   6623  C  CA  . PRO D 1 9   ? 24.178  14.843  -45.981 1.00 18.35 ? 9   PRO D CA  1 
ATOM   6624  C  C   . PRO D 1 9   ? 23.112  15.254  -44.989 1.00 17.37 ? 9   PRO D C   1 
ATOM   6625  O  O   . PRO D 1 9   ? 23.438  15.782  -43.949 1.00 17.36 ? 9   PRO D O   1 
ATOM   6626  C  CB  . PRO D 1 9   ? 24.586  16.070  -46.885 1.00 17.01 ? 9   PRO D CB  1 
ATOM   6627  C  CG  . PRO D 1 9   ? 25.100  15.441  -48.129 1.00 23.74 ? 9   PRO D CG  1 
ATOM   6628  C  CD  . PRO D 1 9   ? 24.121  14.259  -48.346 1.00 19.46 ? 9   PRO D CD  1 
ATOM   6629  N  N   . ASP D 1 10  ? 21.805  15.133  -45.358 1.00 14.37 ? 10  ASP D N   1 
ATOM   6630  C  CA  . ASP D 1 10  ? 20.658  15.468  -44.532 1.00 13.72 ? 10  ASP D CA  1 
ATOM   6631  C  C   . ASP D 1 10  ? 20.027  14.216  -43.849 1.00 11.58 ? 10  ASP D C   1 
ATOM   6632  O  O   . ASP D 1 10  ? 18.946  14.322  -43.330 1.00 11.36 ? 10  ASP D O   1 
ATOM   6633  C  CB  . ASP D 1 10  ? 19.612  16.230  -45.359 1.00 13.93 ? 10  ASP D CB  1 
ATOM   6634  C  CG  . ASP D 1 10  ? 20.222  17.521  -45.985 1.00 19.96 ? 10  ASP D CG  1 
ATOM   6635  O  OD1 . ASP D 1 10  ? 21.027  18.219  -45.329 1.00 23.17 ? 10  ASP D OD1 1 
ATOM   6636  O  OD2 . ASP D 1 10  ? 19.934  17.726  -47.131 1.00 24.71 ? 10  ASP D OD2 1 
ATOM   6637  N  N   . GLY D 1 11  ? 20.787  13.137  -43.906 1.00 10.35 ? 11  GLY D N   1 
ATOM   6638  C  CA  . GLY D 1 11  ? 20.347  11.860  -43.305 1.00 9.55  ? 11  GLY D CA  1 
ATOM   6639  C  C   . GLY D 1 11  ? 20.443  11.876  -41.763 1.00 9.47  ? 11  GLY D C   1 
ATOM   6640  O  O   . GLY D 1 11  ? 20.559  12.946  -41.084 1.00 9.10  ? 11  GLY D O   1 
ATOM   6641  N  N   . GLU D 1 12  ? 20.145  10.753  -41.110 1.00 8.39  ? 12  GLU D N   1 
ATOM   6642  C  CA  . GLU D 1 12  ? 19.754  10.681  -39.721 1.00 8.48  ? 12  GLU D CA  1 
ATOM   6643  C  C   . GLU D 1 12  ? 20.806  11.146  -38.748 1.00 8.17  ? 12  GLU D C   1 
ATOM   6644  O  O   . GLU D 1 12  ? 20.416  11.644  -37.700 1.00 8.39  ? 12  GLU D O   1 
ATOM   6645  C  CB  . GLU D 1 12  ? 19.294  9.231   -39.305 1.00 8.26  ? 12  GLU D CB  1 
ATOM   6646  C  CG  . GLU D 1 12  ? 20.422  8.260   -39.241 1.00 7.65  ? 12  GLU D CG  1 
ATOM   6647  C  CD  . GLU D 1 12  ? 19.786  6.853   -39.228 1.00 7.10  ? 12  GLU D CD  1 
ATOM   6648  O  OE1 . GLU D 1 12  ? 19.400  6.359   -38.163 1.00 8.74  ? 12  GLU D OE1 1 
ATOM   6649  O  OE2 . GLU D 1 12  ? 19.654  6.324   -40.378 1.00 10.06 ? 12  GLU D OE2 1 
ATOM   6650  N  N   . ASN D 1 13  ? 22.104  11.033  -39.063 1.00 8.77  ? 13  ASN D N   1 
ATOM   6651  C  CA  . ASN D 1 13  ? 23.096  11.523  -38.115 1.00 8.34  ? 13  ASN D CA  1 
ATOM   6652  C  C   . ASN D 1 13  ? 23.145  13.073  -38.139 1.00 9.98  ? 13  ASN D C   1 
ATOM   6653  O  O   . ASN D 1 13  ? 23.746  13.594  -37.176 1.00 11.26 ? 13  ASN D O   1 
ATOM   6654  C  CB  . ASN D 1 13  ? 24.503  10.992  -38.513 1.00 9.35  ? 13  ASN D CB  1 
ATOM   6655  C  CG  . ASN D 1 13  ? 24.635  9.538   -38.252 1.00 8.47  ? 13  ASN D CG  1 
ATOM   6656  O  OD1 . ASN D 1 13  ? 23.740  8.914   -37.674 1.00 10.50 ? 13  ASN D OD1 1 
ATOM   6657  N  ND2 . ASN D 1 13  ? 25.831  9.020   -38.534 1.00 11.71 ? 13  ASN D ND2 1 
ATOM   6658  N  N   . SER D 1 14  ? 22.440  13.678  -39.080 1.00 10.06 ? 14  SER D N   1 
ATOM   6659  C  CA  . SER D 1 14  ? 22.436  15.189  -39.173 1.00 8.44  ? 14  SER D CA  1 
ATOM   6660  C  C   . SER D 1 14  ? 21.100  15.720  -38.689 1.00 10.14 ? 14  SER D C   1 
ATOM   6661  O  O   . SER D 1 14  ? 20.954  16.961  -38.582 1.00 10.02 ? 14  SER D O   1 
ATOM   6662  C  CB  . SER D 1 14  ? 22.700  15.637  -40.619 1.00 8.92  ? 14  SER D CB  1 
ATOM   6663  O  OG  . SER D 1 14  ? 24.030  15.347  -40.917 1.00 12.62 ? 14  SER D OG  1 
ATOM   6664  N  N   . TRP D 1 15  ? 20.076  14.922  -38.378 1.00 8.33  ? 15  TRP D N   1 
ATOM   6665  C  CA  . TRP D 1 15  ? 18.737  15.531  -38.069 1.00 9.44  ? 15  TRP D CA  1 
ATOM   6666  C  C   . TRP D 1 15  ? 18.834  16.434  -36.825 1.00 8.56  ? 15  TRP D C   1 
ATOM   6667  O  O   . TRP D 1 15  ? 18.080  17.439  -36.803 1.00 8.73  ? 15  TRP D O   1 
ATOM   6668  C  CB  . TRP D 1 15  ? 17.796  14.369  -37.623 1.00 9.56  ? 15  TRP D CB  1 
ATOM   6669  C  CG  . TRP D 1 15  ? 17.383  13.504  -38.791 1.00 10.38 ? 15  TRP D CG  1 
ATOM   6670  C  CD1 . TRP D 1 15  ? 17.613  13.688  -40.134 1.00 8.42  ? 15  TRP D CD1 1 
ATOM   6671  C  CD2 . TRP D 1 15  ? 16.607  12.267  -38.682 1.00 8.47  ? 15  TRP D CD2 1 
ATOM   6672  N  NE1 . TRP D 1 15  ? 17.013  12.629  -40.910 1.00 8.65  ? 15  TRP D NE1 1 
ATOM   6673  C  CE2 . TRP D 1 15  ? 16.373  11.802  -40.031 1.00 7.98  ? 15  TRP D CE2 1 
ATOM   6674  C  CE3 . TRP D 1 15  ? 16.026  11.583  -37.602 1.00 7.26  ? 15  TRP D CE3 1 
ATOM   6675  C  CZ2 . TRP D 1 15  ? 15.710  10.551  -40.287 1.00 8.50  ? 15  TRP D CZ2 1 
ATOM   6676  C  CZ3 . TRP D 1 15  ? 15.330  10.370  -37.843 1.00 8.25  ? 15  TRP D CZ3 1 
ATOM   6677  C  CH2 . TRP D 1 15  ? 15.131  9.923   -39.210 1.00 8.29  ? 15  TRP D CH2 1 
ATOM   6678  N  N   . SER D 1 16  ? 19.726  16.137  -35.881 1.00 9.89  ? 16  SER D N   1 
ATOM   6679  C  CA  . SER D 1 16  ? 19.791  16.929  -34.587 1.00 10.00 ? 16  SER D CA  1 
ATOM   6680  C  C   . SER D 1 16  ? 20.286  18.321  -34.919 1.00 10.47 ? 16  SER D C   1 
ATOM   6681  O  O   . SER D 1 16  ? 20.120  19.175  -34.030 1.00 10.97 ? 16  SER D O   1 
ATOM   6682  C  CB  . SER D 1 16  ? 20.724  16.294  -33.640 1.00 11.35 ? 16  SER D CB  1 
ATOM   6683  O  OG  . SER D 1 16  ? 22.047  16.337  -34.250 1.00 16.10 ? 16  SER D OG  1 
ATOM   6684  N  N   . LYS D 1 17  ? 20.824  18.602  -36.098 1.00 10.07 ? 17  LYS D N   1 
ATOM   6685  C  CA  . LYS D 1 17  ? 21.308  19.979  -36.361 1.00 10.93 ? 17  LYS D CA  1 
ATOM   6686  C  C   . LYS D 1 17  ? 20.127  20.906  -36.460 1.00 12.54 ? 17  LYS D C   1 
ATOM   6687  O  O   . LYS D 1 17  ? 20.282  22.166  -36.144 1.00 11.25 ? 17  LYS D O   1 
ATOM   6688  C  CB  . LYS D 1 17  ? 22.005  19.984  -37.702 1.00 11.07 ? 17  LYS D CB  1 
ATOM   6689  C  CG  . LYS D 1 17  ? 23.312  19.196  -37.694 1.00 12.38 ? 17  LYS D CG  1 
ATOM   6690  C  CD  . LYS D 1 17  ? 23.939  19.183  -39.137 1.00 11.42 ? 17  LYS D CD  1 
ATOM   6691  C  CE  . LYS D 1 17  ? 25.064  18.251  -39.248 1.00 12.77 ? 17  LYS D CE  1 
ATOM   6692  N  NZ  . LYS D 1 17  ? 25.770  18.405  -40.610 1.00 12.90 ? 17  LYS D NZ  1 
ATOM   6693  N  N   . LYS D 1 18  ? 18.963  20.461  -36.959 1.00 10.38 ? 18  LYS D N   1 
ATOM   6694  C  CA  . LYS D 1 18  ? 17.726  21.284  -37.050 1.00 10.37 ? 18  LYS D CA  1 
ATOM   6695  C  C   . LYS D 1 18  ? 16.675  20.880  -36.037 1.00 10.39 ? 18  LYS D C   1 
ATOM   6696  O  O   . LYS D 1 18  ? 15.738  21.681  -35.835 1.00 13.11 ? 18  LYS D O   1 
ATOM   6697  C  CB  . LYS D 1 18  ? 17.136  21.194  -38.487 1.00 11.97 ? 18  LYS D CB  1 
ATOM   6698  C  CG  . LYS D 1 18  ? 18.073  21.885  -39.558 1.00 19.35 ? 18  LYS D CG  1 
ATOM   6699  C  CD  . LYS D 1 18  ? 17.370  21.687  -40.931 1.00 19.46 ? 18  LYS D CD  1 
ATOM   6700  C  CE  . LYS D 1 18  ? 18.191  22.460  -42.006 1.00 26.62 ? 18  LYS D CE  1 
ATOM   6701  N  NZ  . LYS D 1 18  ? 17.671  22.031  -43.366 1.00 32.80 ? 18  LYS D NZ  1 
ATOM   6702  N  N   . TYR D 1 19  ? 16.728  19.630  -35.534 1.00 9.62  ? 19  TYR D N   1 
ATOM   6703  C  CA  . TYR D 1 19  ? 15.637  19.157  -34.717 1.00 9.96  ? 19  TYR D CA  1 
ATOM   6704  C  C   . TYR D 1 19  ? 16.249  18.676  -33.423 1.00 10.72 ? 19  TYR D C   1 
ATOM   6705  O  O   . TYR D 1 19  ? 16.721  17.500  -33.385 1.00 10.44 ? 19  TYR D O   1 
ATOM   6706  C  CB  . TYR D 1 19  ? 15.004  17.915  -35.495 1.00 8.89  ? 19  TYR D CB  1 
ATOM   6707  C  CG  . TYR D 1 19  ? 14.401  18.344  -36.742 1.00 7.45  ? 19  TYR D CG  1 
ATOM   6708  C  CD1 . TYR D 1 19  ? 13.202  19.060  -36.788 1.00 10.88 ? 19  TYR D CD1 1 
ATOM   6709  C  CD2 . TYR D 1 19  ? 15.083  18.098  -37.980 1.00 10.10 ? 19  TYR D CD2 1 
ATOM   6710  C  CE1 . TYR D 1 19  ? 12.613  19.439  -37.971 1.00 12.90 ? 19  TYR D CE1 1 
ATOM   6711  C  CE2 . TYR D 1 19  ? 14.476  18.511  -39.171 1.00 10.48 ? 19  TYR D CE2 1 
ATOM   6712  C  CZ  . TYR D 1 19  ? 13.273  19.223  -39.168 1.00 12.06 ? 19  TYR D CZ  1 
ATOM   6713  O  OH  . TYR D 1 19  ? 12.651  19.581  -40.392 1.00 16.38 ? 19  TYR D OH  1 
ATOM   6714  N  N   . PRO D 1 20  ? 16.462  19.506  -32.389 1.00 10.02 ? 20  PRO D N   1 
ATOM   6715  C  CA  . PRO D 1 20  ? 17.242  19.131  -31.254 1.00 10.57 ? 20  PRO D CA  1 
ATOM   6716  C  C   . PRO D 1 20  ? 16.777  17.835  -30.559 1.00 8.36  ? 20  PRO D C   1 
ATOM   6717  O  O   . PRO D 1 20  ? 17.621  17.140  -29.925 1.00 10.56 ? 20  PRO D O   1 
ATOM   6718  C  CB  . PRO D 1 20  ? 17.111  20.336  -30.263 1.00 10.59 ? 20  PRO D CB  1 
ATOM   6719  C  CG  . PRO D 1 20  ? 16.524  21.291  -31.039 1.00 13.51 ? 20  PRO D CG  1 
ATOM   6720  C  CD  . PRO D 1 20  ? 15.983  20.919  -32.360 1.00 10.33 ? 20  PRO D CD  1 
ATOM   6721  N  N   . SER D 1 21  ? 15.452  17.570  -30.546 1.00 9.92  ? 21  SER D N   1 
ATOM   6722  C  CA  . SER D 1 21  ? 15.021  16.283  -29.823 1.00 9.93  ? 21  SER D CA  1 
ATOM   6723  C  C   . SER D 1 21  ? 15.576  15.051  -30.501 1.00 9.15  ? 21  SER D C   1 
ATOM   6724  O  O   . SER D 1 21  ? 15.638  14.047  -29.842 1.00 11.00 ? 21  SER D O   1 
ATOM   6725  C  CB  . SER D 1 21  ? 13.533  16.155  -29.747 1.00 9.18  ? 21  SER D CB  1 
ATOM   6726  O  OG  . SER D 1 21  ? 13.020  17.249  -28.902 1.00 12.56 ? 21  SER D OG  1 
ATOM   6727  N  N   . CYS D 1 22  ? 15.969  15.088  -31.759 1.00 9.80  ? 22  CYS D N   1 
ATOM   6728  C  CA  . CYS D 1 22  ? 16.603  13.923  -32.449 1.00 9.91  ? 22  CYS D CA  1 
ATOM   6729  C  C   . CYS D 1 22  ? 17.945  13.612  -31.818 1.00 10.54 ? 22  CYS D C   1 
ATOM   6730  O  O   . CYS D 1 22  ? 18.430  12.497  -31.998 1.00 11.87 ? 22  CYS D O   1 
ATOM   6731  C  CB  . CYS D 1 22  ? 16.748  14.189  -33.922 1.00 12.17 ? 22  CYS D CB  1 
ATOM   6732  S  SG  . CYS D 1 22  ? 15.205  14.456  -34.801 1.00 9.32  ? 22  CYS D SG  1 
ATOM   6733  N  N   . GLY D 1 23  ? 18.578  14.558  -31.112 1.00 12.22 ? 23  GLY D N   1 
ATOM   6734  C  CA  . GLY D 1 23  ? 19.784  14.319  -30.300 1.00 11.29 ? 23  GLY D CA  1 
ATOM   6735  C  C   . GLY D 1 23  ? 19.523  14.230  -28.763 1.00 13.65 ? 23  GLY D C   1 
ATOM   6736  O  O   . GLY D 1 23  ? 20.535  14.278  -27.947 1.00 15.52 ? 23  GLY D O   1 
ATOM   6737  N  N   . GLY D 1 24  ? 18.250  14.164  -28.365 1.00 13.25 ? 24  GLY D N   1 
ATOM   6738  C  CA  . GLY D 1 24  ? 17.852  14.049  -26.940 1.00 16.12 ? 24  GLY D CA  1 
ATOM   6739  C  C   . GLY D 1 24  ? 17.631  12.655  -26.454 1.00 18.17 ? 24  GLY D C   1 
ATOM   6740  O  O   . GLY D 1 24  ? 18.136  11.700  -27.025 1.00 19.24 ? 24  GLY D O   1 
ATOM   6741  N  N   . LEU D 1 25  ? 16.966  12.547  -25.331 1.00 18.00 ? 25  LEU D N   1 
ATOM   6742  C  CA  . LEU D 1 25  ? 16.867  11.259  -24.733 1.00 18.77 ? 25  LEU D CA  1 
ATOM   6743  C  C   . LEU D 1 25  ? 15.609  10.590  -25.307 1.00 14.68 ? 25  LEU D C   1 
ATOM   6744  O  O   . LEU D 1 25  ? 14.732  11.207  -25.977 1.00 14.12 ? 25  LEU D O   1 
ATOM   6745  C  CB  . LEU D 1 25  ? 16.681  11.418  -23.175 1.00 20.11 ? 25  LEU D CB  1 
ATOM   6746  C  CG  . LEU D 1 25  ? 17.841  12.062  -22.302 1.00 23.60 ? 25  LEU D CG  1 
ATOM   6747  C  CD1 . LEU D 1 25  ? 17.579  11.924  -20.745 1.00 28.31 ? 25  LEU D CD1 1 
ATOM   6748  C  CD2 . LEU D 1 25  ? 19.218  11.524  -22.685 1.00 30.73 ? 25  LEU D CD2 1 
ATOM   6749  N  N   . LEU D 1 26  ? 15.528  9.297   -24.956 1.00 15.24 ? 26  LEU D N   1 
ATOM   6750  C  CA  . LEU D 1 26  ? 14.290  8.494   -25.097 1.00 14.55 ? 26  LEU D CA  1 
ATOM   6751  C  C   . LEU D 1 26  ? 13.846  8.284   -26.561 1.00 8.58  ? 26  LEU D C   1 
ATOM   6752  O  O   . LEU D 1 26  ? 12.659  8.337   -26.953 1.00 11.45 ? 26  LEU D O   1 
ATOM   6753  C  CB  . LEU D 1 26  ? 13.109  9.033   -24.334 1.00 15.48 ? 26  LEU D CB  1 
ATOM   6754  C  CG  . LEU D 1 26  ? 13.580  9.363   -22.892 1.00 21.19 ? 26  LEU D CG  1 
ATOM   6755  C  CD1 . LEU D 1 26  ? 12.319  9.725   -22.219 1.00 21.72 ? 26  LEU D CD1 1 
ATOM   6756  C  CD2 . LEU D 1 26  ? 14.240  8.189   -22.079 1.00 21.56 ? 26  LEU D CD2 1 
ATOM   6757  N  N   . GLN D 1 27  ? 14.885  8.106   -27.371 1.00 10.39 ? 27  GLN D N   1 
ATOM   6758  C  CA  . GLN D 1 27  ? 14.657  8.005   -28.834 1.00 9.28  ? 27  GLN D CA  1 
ATOM   6759  C  C   . GLN D 1 27  ? 14.219  6.595   -29.246 1.00 9.48  ? 27  GLN D C   1 
ATOM   6760  O  O   . GLN D 1 27  ? 14.631  5.575   -28.647 1.00 11.55 ? 27  GLN D O   1 
ATOM   6761  C  CB  . GLN D 1 27  ? 15.897  8.401   -29.627 1.00 9.14  ? 27  GLN D CB  1 
ATOM   6762  C  CG  . GLN D 1 27  ? 16.299  9.868   -29.347 1.00 10.38 ? 27  GLN D CG  1 
ATOM   6763  C  CD  . GLN D 1 27  ? 15.234  10.775  -29.968 1.00 10.03 ? 27  GLN D CD  1 
ATOM   6764  O  OE1 . GLN D 1 27  ? 15.269  10.945  -31.220 1.00 10.31 ? 27  GLN D OE1 1 
ATOM   6765  N  NE2 . GLN D 1 27  ? 14.280  11.352  -29.199 1.00 9.12  ? 27  GLN D NE2 1 
ATOM   6766  N  N   . SER D 1 28  ? 13.506  6.583   -30.379 1.00 7.52  ? 28  SER D N   1 
ATOM   6767  C  CA  . SER D 1 28  ? 13.059  5.330   -30.987 1.00 7.91  ? 28  SER D CA  1 
ATOM   6768  C  C   . SER D 1 28  ? 13.592  5.320   -32.409 1.00 8.36  ? 28  SER D C   1 
ATOM   6769  O  O   . SER D 1 28  ? 13.892  6.352   -33.017 1.00 8.51  ? 28  SER D O   1 
ATOM   6770  C  CB  . SER D 1 28  ? 11.526  5.300   -31.057 1.00 9.69  ? 28  SER D CB  1 
ATOM   6771  O  OG  . SER D 1 28  ? 11.025  5.250   -29.743 1.00 8.99  ? 28  SER D OG  1 
ATOM   6772  N  N   . PRO D 1 29  ? 13.692  4.181   -33.060 1.00 6.35  ? 29  PRO D N   1 
ATOM   6773  C  CA  . PRO D 1 29  ? 13.374  2.796   -32.550 1.00 6.56  ? 29  PRO D CA  1 
ATOM   6774  C  C   . PRO D 1 29  ? 14.488  2.255   -31.700 1.00 8.12  ? 29  PRO D C   1 
ATOM   6775  O  O   . PRO D 1 29  ? 15.532  2.829   -31.572 1.00 7.90  ? 29  PRO D O   1 
ATOM   6776  C  CB  . PRO D 1 29  ? 13.139  1.999   -33.888 1.00 9.12  ? 29  PRO D CB  1 
ATOM   6777  C  CG  . PRO D 1 29  ? 14.186  2.628   -34.760 1.00 7.84  ? 29  PRO D CG  1 
ATOM   6778  C  CD  . PRO D 1 29  ? 14.252  4.136   -34.431 1.00 7.50  ? 29  PRO D CD  1 
ATOM   6779  N  N   . ILE D 1 30  ? 14.225  0.998   -31.228 1.00 7.98  ? 30  ILE D N   1 
ATOM   6780  C  CA  . ILE D 1 30  ? 15.176  0.270   -30.387 1.00 9.45  ? 30  ILE D CA  1 
ATOM   6781  C  C   . ILE D 1 30  ? 15.174  -1.208  -30.830 1.00 7.99  ? 30  ILE D C   1 
ATOM   6782  O  O   . ILE D 1 30  ? 14.253  -1.667  -31.514 1.00 8.54  ? 30  ILE D O   1 
ATOM   6783  C  CB  . ILE D 1 30  ? 14.866  0.433   -28.873 1.00 10.17 ? 30  ILE D CB  1 
ATOM   6784  C  CG1 . ILE D 1 30  ? 13.434  -0.166  -28.634 1.00 11.92 ? 30  ILE D CG1 1 
ATOM   6785  C  CG2 . ILE D 1 30  ? 15.089  1.860   -28.396 1.00 12.20 ? 30  ILE D CG2 1 
ATOM   6786  C  CD1 . ILE D 1 30  ? 13.200  -0.251  -27.118 1.00 12.18 ? 30  ILE D CD1 1 
ATOM   6787  N  N   . ASP D 1 31  ? 16.252  -1.894  -30.408 1.00 8.45  ? 31  ASP D N   1 
ATOM   6788  C  CA  . ASP D 1 31  ? 16.327  -3.381  -30.561 1.00 8.68  ? 31  ASP D CA  1 
ATOM   6789  C  C   . ASP D 1 31  ? 15.675  -4.055  -29.366 1.00 11.16 ? 31  ASP D C   1 
ATOM   6790  O  O   . ASP D 1 31  ? 16.114  -3.836  -28.210 1.00 10.79 ? 31  ASP D O   1 
ATOM   6791  C  CB  . ASP D 1 31  ? 17.830  -3.813  -30.654 1.00 10.06 ? 31  ASP D CB  1 
ATOM   6792  C  CG  . ASP D 1 31  ? 17.941  -5.291  -30.780 1.00 12.46 ? 31  ASP D CG  1 
ATOM   6793  O  OD1 . ASP D 1 31  ? 17.377  -5.828  -31.700 1.00 9.87  ? 31  ASP D OD1 1 
ATOM   6794  O  OD2 . ASP D 1 31  ? 18.613  -5.825  -29.936 1.00 14.76 ? 31  ASP D OD2 1 
ATOM   6795  N  N   . LEU D 1 32  ? 14.733  -4.931  -29.621 1.00 9.59  ? 32  LEU D N   1 
ATOM   6796  C  CA  . LEU D 1 32  ? 14.017  -5.591  -28.527 1.00 9.19  ? 32  LEU D CA  1 
ATOM   6797  C  C   . LEU D 1 32  ? 14.739  -6.940  -28.288 1.00 9.87  ? 32  LEU D C   1 
ATOM   6798  O  O   . LEU D 1 32  ? 14.818  -7.777  -29.183 1.00 11.34 ? 32  LEU D O   1 
ATOM   6799  C  CB  . LEU D 1 32  ? 12.610  -5.845  -28.998 1.00 10.82 ? 32  LEU D CB  1 
ATOM   6800  C  CG  . LEU D 1 32  ? 11.856  -4.587  -29.492 1.00 12.10 ? 32  LEU D CG  1 
ATOM   6801  C  CD1 . LEU D 1 32  ? 10.533  -4.965  -30.151 1.00 12.38 ? 32  LEU D CD1 1 
ATOM   6802  C  CD2 . LEU D 1 32  ? 11.599  -3.666  -28.263 1.00 13.46 ? 32  LEU D CD2 1 
ATOM   6803  N  N   . HIS D 1 33  ? 15.479  -6.988  -27.172 1.00 11.30 ? 33  HIS D N   1 
ATOM   6804  C  CA  . HIS D 1 33  ? 16.292  -8.164  -26.912 1.00 12.67 ? 33  HIS D CA  1 
ATOM   6805  C  C   . HIS D 1 33  ? 16.179  -8.522  -25.432 1.00 13.99 ? 33  HIS D C   1 
ATOM   6806  O  O   . HIS D 1 33  ? 15.898  -7.661  -24.576 1.00 12.91 ? 33  HIS D O   1 
ATOM   6807  C  CB  . HIS D 1 33  ? 17.802  -7.997  -27.330 1.00 15.34 ? 33  HIS D CB  1 
ATOM   6808  C  CG  . HIS D 1 33  ? 18.512  -6.899  -26.604 1.00 13.43 ? 33  HIS D CG  1 
ATOM   6809  N  ND1 . HIS D 1 33  ? 18.421  -5.566  -26.948 1.00 13.89 ? 33  HIS D ND1 1 
ATOM   6810  C  CD2 . HIS D 1 33  ? 19.344  -6.931  -25.527 1.00 13.04 ? 33  HIS D CD2 1 
ATOM   6811  C  CE1 . HIS D 1 33  ? 19.152  -4.833  -26.121 1.00 21.04 ? 33  HIS D CE1 1 
ATOM   6812  N  NE2 . HIS D 1 33  ? 19.753  -5.656  -25.270 1.00 16.53 ? 33  HIS D NE2 1 
ATOM   6813  N  N   . SER D 1 34  ? 16.546  -9.805  -25.181 1.00 13.46 ? 34  SER D N   1 
ATOM   6814  C  CA  . SER D 1 34  ? 16.191  -10.383 -23.857 1.00 14.72 ? 34  SER D CA  1 
ATOM   6815  C  C   . SER D 1 34  ? 16.666  -9.546  -22.651 1.00 14.08 ? 34  SER D C   1 
ATOM   6816  O  O   . SER D 1 34  ? 15.898  -9.405  -21.639 1.00 14.78 ? 34  SER D O   1 
ATOM   6817  C  CB  . SER D 1 34  ? 16.686  -11.846 -23.823 1.00 14.06 ? 34  SER D CB  1 
ATOM   6818  O  OG  . SER D 1 34  ? 18.101  -11.742 -23.738 1.00 21.33 ? 34  SER D OG  1 
ATOM   6819  N  N   . ASP D 1 35  ? 17.893  -9.018  -22.671 1.00 12.14 ? 35  ASP D N   1 
ATOM   6820  C  CA  . ASP D 1 35  ? 18.453  -8.412  -21.466 1.00 14.10 ? 35  ASP D CA  1 
ATOM   6821  C  C   . ASP D 1 35  ? 17.616  -7.236  -20.971 1.00 13.90 ? 35  ASP D C   1 
ATOM   6822  O  O   . ASP D 1 35  ? 17.681  -6.852  -19.815 1.00 17.09 ? 35  ASP D O   1 
ATOM   6823  C  CB  . ASP D 1 35  ? 19.923  -7.873  -21.650 1.00 15.35 ? 35  ASP D CB  1 
ATOM   6824  C  CG  . ASP D 1 35  ? 20.804  -8.851  -22.342 1.00 20.94 ? 35  ASP D CG  1 
ATOM   6825  O  OD1 . ASP D 1 35  ? 21.770  -9.299  -21.678 1.00 20.17 ? 35  ASP D OD1 1 
ATOM   6826  O  OD2 . ASP D 1 35  ? 20.542  -9.155  -23.534 1.00 18.98 ? 35  ASP D OD2 1 
ATOM   6827  N  N   . ILE D 1 36  ? 16.818  -6.612  -21.862 1.00 13.06 ? 36  ILE D N   1 
ATOM   6828  C  CA  . ILE D 1 36  ? 16.141  -5.362  -21.490 1.00 13.57 ? 36  ILE D CA  1 
ATOM   6829  C  C   . ILE D 1 36  ? 14.667  -5.565  -21.370 1.00 13.89 ? 36  ILE D C   1 
ATOM   6830  O  O   . ILE D 1 36  ? 13.950  -4.554  -21.136 1.00 14.32 ? 36  ILE D O   1 
ATOM   6831  C  CB  . ILE D 1 36  ? 16.536  -4.079  -22.323 1.00 14.39 ? 36  ILE D CB  1 
ATOM   6832  C  CG1 . ILE D 1 36  ? 16.373  -4.322  -23.835 1.00 18.34 ? 36  ILE D CG1 1 
ATOM   6833  C  CG2 . ILE D 1 36  ? 17.944  -3.742  -22.045 1.00 18.43 ? 36  ILE D CG2 1 
ATOM   6834  C  CD1 . ILE D 1 36  ? 15.005  -4.601  -24.346 1.00 16.39 ? 36  ILE D CD1 1 
ATOM   6835  N  N   . LEU D 1 37  ? 14.193  -6.807  -21.556 1.00 13.32 ? 37  LEU D N   1 
ATOM   6836  C  CA  . LEU D 1 37  ? 12.740  -7.073  -21.434 1.00 14.41 ? 37  LEU D CA  1 
ATOM   6837  C  C   . LEU D 1 37  ? 12.351  -7.407  -20.007 1.00 14.99 ? 37  LEU D C   1 
ATOM   6838  O  O   . LEU D 1 37  ? 13.092  -8.080  -19.307 1.00 16.16 ? 37  LEU D O   1 
ATOM   6839  C  CB  . LEU D 1 37  ? 12.405  -8.227  -22.293 1.00 14.06 ? 37  LEU D CB  1 
ATOM   6840  C  CG  . LEU D 1 37  ? 12.699  -8.122  -23.782 1.00 14.45 ? 37  LEU D CG  1 
ATOM   6841  C  CD1 . LEU D 1 37  ? 12.279  -9.360  -24.525 1.00 17.31 ? 37  LEU D CD1 1 
ATOM   6842  C  CD2 . LEU D 1 37  ? 12.008  -6.883  -24.473 1.00 13.05 ? 37  LEU D CD2 1 
ATOM   6843  N  N   . GLN D 1 38  ? 11.164  -6.968  -19.610 1.00 13.15 ? 38  GLN D N   1 
ATOM   6844  C  CA  . GLN D 1 38  ? 10.644  -7.287  -18.265 1.00 12.79 ? 38  GLN D CA  1 
ATOM   6845  C  C   . GLN D 1 38  ? 9.153   -7.461  -18.334 1.00 12.99 ? 38  GLN D C   1 
ATOM   6846  O  O   . GLN D 1 38  ? 8.430   -6.584  -18.757 1.00 12.74 ? 38  GLN D O   1 
ATOM   6847  C  CB  . GLN D 1 38  ? 10.988  -6.211  -17.309 1.00 15.95 ? 38  GLN D CB  1 
ATOM   6848  C  CG  . GLN D 1 38  ? 10.602  -6.631  -15.912 1.00 21.29 ? 38  GLN D CG  1 
ATOM   6849  C  CD  . GLN D 1 38  ? 11.127  -5.689  -14.935 1.00 26.33 ? 38  GLN D CD  1 
ATOM   6850  O  OE1 . GLN D 1 38  ? 12.327  -5.692  -14.676 1.00 26.68 ? 38  GLN D OE1 1 
ATOM   6851  N  NE2 . GLN D 1 38  ? 10.259  -4.790  -14.432 1.00 28.80 ? 38  GLN D NE2 1 
ATOM   6852  N  N   . TYR D 1 39  ? 8.671   -8.623  -17.926 1.00 12.83 ? 39  TYR D N   1 
ATOM   6853  C  CA  . TYR D 1 39  ? 7.219   -8.882  -17.889 1.00 11.65 ? 39  TYR D CA  1 
ATOM   6854  C  C   . TYR D 1 39  ? 6.527   -7.893  -16.915 1.00 12.14 ? 39  TYR D C   1 
ATOM   6855  O  O   . TYR D 1 39  ? 7.047   -7.627  -15.807 1.00 12.48 ? 39  TYR D O   1 
ATOM   6856  C  CB  . TYR D 1 39  ? 6.999   -10.315 -17.401 1.00 12.45 ? 39  TYR D CB  1 
ATOM   6857  C  CG  . TYR D 1 39  ? 5.522   -10.565 -17.164 1.00 11.95 ? 39  TYR D CG  1 
ATOM   6858  C  CD1 . TYR D 1 39  ? 4.611   -10.613 -18.186 1.00 13.68 ? 39  TYR D CD1 1 
ATOM   6859  C  CD2 . TYR D 1 39  ? 5.059   -10.766 -15.822 1.00 13.58 ? 39  TYR D CD2 1 
ATOM   6860  C  CE1 . TYR D 1 39  ? 3.248   -10.837 -17.952 1.00 12.50 ? 39  TYR D CE1 1 
ATOM   6861  C  CE2 . TYR D 1 39  ? 3.753   -10.932 -15.613 1.00 11.41 ? 39  TYR D CE2 1 
ATOM   6862  C  CZ  . TYR D 1 39  ? 2.854   -10.988 -16.561 1.00 12.12 ? 39  TYR D CZ  1 
ATOM   6863  O  OH  . TYR D 1 39  ? 1.468   -11.181 -16.431 1.00 18.17 ? 39  TYR D OH  1 
ATOM   6864  N  N   . ASP D 1 40  ? 5.356   -7.362  -17.334 1.00 11.39 ? 40  ASP D N   1 
ATOM   6865  C  CA  . ASP D 1 40  ? 4.631   -6.409  -16.477 1.00 11.71 ? 40  ASP D CA  1 
ATOM   6866  C  C   . ASP D 1 40  ? 3.208   -6.790  -16.542 1.00 12.54 ? 40  ASP D C   1 
ATOM   6867  O  O   . ASP D 1 40  ? 2.522   -6.688  -17.616 1.00 13.04 ? 40  ASP D O   1 
ATOM   6868  C  CB  . ASP D 1 40  ? 4.880   -5.008  -17.015 1.00 11.03 ? 40  ASP D CB  1 
ATOM   6869  C  CG  . ASP D 1 40  ? 4.171   -3.936  -16.220 1.00 19.07 ? 40  ASP D CG  1 
ATOM   6870  O  OD1 . ASP D 1 40  ? 3.391   -4.277  -15.308 1.00 13.27 ? 40  ASP D OD1 1 
ATOM   6871  O  OD2 . ASP D 1 40  ? 4.396   -2.744  -16.514 1.00 18.36 ? 40  ASP D OD2 1 
ATOM   6872  N  N   . ALA D 1 41  ? 2.690   -7.258  -15.346 1.00 10.24 ? 41  ALA D N   1 
ATOM   6873  C  CA  . ALA D 1 41  ? 1.291   -7.676  -15.287 1.00 12.32 ? 41  ALA D CA  1 
ATOM   6874  C  C   . ALA D 1 41  ? 0.245   -6.565  -15.522 1.00 13.40 ? 41  ALA D C   1 
ATOM   6875  O  O   . ALA D 1 41  ? -0.936  -6.847  -15.781 1.00 13.07 ? 41  ALA D O   1 
ATOM   6876  C  CB  . ALA D 1 41  ? 1.073   -8.375  -13.900 1.00 12.32 ? 41  ALA D CB  1 
ATOM   6877  N  N   . SER D 1 42  ? 0.760   -5.309  -15.457 1.00 12.18 ? 42  SER D N   1 
ATOM   6878  C  CA  . SER D 1 42  ? -0.122  -4.106  -15.616 1.00 14.87 ? 42  SER D CA  1 
ATOM   6879  C  C   . SER D 1 42  ? -0.537  -3.928  -17.071 1.00 15.11 ? 42  SER D C   1 
ATOM   6880  O  O   . SER D 1 42  ? -1.425  -3.079  -17.403 1.00 18.44 ? 42  SER D O   1 
ATOM   6881  C  CB  . SER D 1 42  ? 0.482   -2.833  -14.988 1.00 15.27 ? 42  SER D CB  1 
ATOM   6882  O  OG  . SER D 1 42  ? 1.420   -2.344  -15.937 1.00 19.21 ? 42  SER D OG  1 
ATOM   6883  N  N   . LEU D 1 43  ? 0.192   -4.602  -17.984 1.00 13.49 ? 43  LEU D N   1 
ATOM   6884  C  CA  . LEU D 1 43  ? -0.059  -4.511  -19.445 1.00 15.24 ? 43  LEU D CA  1 
ATOM   6885  C  C   . LEU D 1 43  ? -1.138  -5.452  -19.915 1.00 14.03 ? 43  LEU D C   1 
ATOM   6886  O  O   . LEU D 1 43  ? -0.973  -6.551  -20.473 1.00 14.04 ? 43  LEU D O   1 
ATOM   6887  C  CB  . LEU D 1 43  ? 1.274   -4.840  -20.160 1.00 14.29 ? 43  LEU D CB  1 
ATOM   6888  C  CG  . LEU D 1 43  ? 2.362   -3.886  -19.933 1.00 14.97 ? 43  LEU D CG  1 
ATOM   6889  C  CD1 . LEU D 1 43  ? 3.521   -4.337  -20.814 1.00 12.78 ? 43  LEU D CD1 1 
ATOM   6890  C  CD2 . LEU D 1 43  ? 2.056   -2.405  -20.166 1.00 19.11 ? 43  LEU D CD2 1 
ATOM   6891  N  N   . THR D 1 44  ? -2.368  -4.871  -19.777 1.00 16.30 ? 44  THR D N   1 
ATOM   6892  C  CA  . THR D 1 44  ? -3.551  -5.608  -20.133 1.00 14.73 ? 44  THR D CA  1 
ATOM   6893  C  C   . THR D 1 44  ? -3.912  -5.438  -21.641 1.00 15.14 ? 44  THR D C   1 
ATOM   6894  O  O   . THR D 1 44  ? -3.370  -4.506  -22.265 1.00 14.51 ? 44  THR D O   1 
ATOM   6895  C  CB  . THR D 1 44  ? -4.796  -5.144  -19.243 1.00 13.12 ? 44  THR D CB  1 
ATOM   6896  O  OG1 . THR D 1 44  ? -4.841  -3.774  -19.333 1.00 18.65 ? 44  THR D OG1 1 
ATOM   6897  C  CG2 . THR D 1 44  ? -4.479  -5.450  -17.779 1.00 22.86 ? 44  THR D CG2 1 
ATOM   6898  N  N   . PRO D 1 45  ? -4.850  -6.177  -22.177 1.00 15.82 ? 45  PRO D N   1 
ATOM   6899  C  CA  . PRO D 1 45  ? -5.052  -6.149  -23.624 1.00 17.38 ? 45  PRO D CA  1 
ATOM   6900  C  C   . PRO D 1 45  ? -5.687  -4.831  -24.065 1.00 17.30 ? 45  PRO D C   1 
ATOM   6901  O  O   . PRO D 1 45  ? -6.589  -4.323  -23.402 1.00 18.47 ? 45  PRO D O   1 
ATOM   6902  C  CB  . PRO D 1 45  ? -6.042  -7.260  -23.857 1.00 18.13 ? 45  PRO D CB  1 
ATOM   6903  C  CG  . PRO D 1 45  ? -5.983  -8.102  -22.531 1.00 16.68 ? 45  PRO D CG  1 
ATOM   6904  C  CD  . PRO D 1 45  ? -5.682  -7.185  -21.486 1.00 15.74 ? 45  PRO D CD  1 
ATOM   6905  N  N   . LEU D 1 46  ? -5.223  -4.274  -25.186 1.00 14.69 ? 46  LEU D N   1 
ATOM   6906  C  CA  . LEU D 1 46  ? -5.830  -3.049  -25.739 1.00 15.35 ? 46  LEU D CA  1 
ATOM   6907  C  C   . LEU D 1 46  ? -7.094  -3.447  -26.481 1.00 15.31 ? 46  LEU D C   1 
ATOM   6908  O  O   . LEU D 1 46  ? -7.275  -4.562  -27.072 1.00 16.40 ? 46  LEU D O   1 
ATOM   6909  C  CB  . LEU D 1 46  ? -4.918  -2.477  -26.817 1.00 15.80 ? 46  LEU D CB  1 
ATOM   6910  C  CG  . LEU D 1 46  ? -3.633  -1.978  -26.199 1.00 14.97 ? 46  LEU D CG  1 
ATOM   6911  C  CD1 . LEU D 1 46  ? -2.802  -1.502  -27.418 1.00 20.17 ? 46  LEU D CD1 1 
ATOM   6912  C  CD2 . LEU D 1 46  ? -3.916  -0.783  -25.154 1.00 18.63 ? 46  LEU D CD2 1 
ATOM   6913  N  N   . GLU D 1 47  ? -7.964  -2.427  -26.498 1.00 16.96 ? 47  GLU D N   1 
ATOM   6914  C  CA  . GLU D 1 47  ? -9.138  -2.535  -27.280 1.00 17.19 ? 47  GLU D CA  1 
ATOM   6915  C  C   . GLU D 1 47  ? -9.159  -1.567  -28.524 1.00 14.31 ? 47  GLU D C   1 
ATOM   6916  O  O   . GLU D 1 47  ? -8.783  -0.311  -28.393 1.00 16.83 ? 47  GLU D O   1 
ATOM   6917  C  CB  . GLU D 1 47  ? -10.445 -2.415  -26.468 1.00 19.44 ? 47  GLU D CB  1 
ATOM   6918  C  CG  . GLU D 1 47  ? -10.863 -3.824  -25.786 1.00 26.76 ? 47  GLU D CG  1 
ATOM   6919  C  CD  . GLU D 1 47  ? -12.162 -3.816  -24.934 1.00 27.44 ? 47  GLU D CD  1 
ATOM   6920  O  OE1 . GLU D 1 47  ? -12.888 -4.841  -24.969 1.00 39.04 ? 47  GLU D OE1 1 
ATOM   6921  O  OE2 . GLU D 1 47  ? -12.461 -2.783  -24.263 1.00 42.51 ? 47  GLU D OE2 1 
ATOM   6922  N  N   . PHE D 1 48  ? -9.592  -2.140  -29.608 1.00 15.44 ? 48  PHE D N   1 
ATOM   6923  C  CA  . PHE D 1 48  ? -9.520  -1.396  -30.937 1.00 15.50 ? 48  PHE D CA  1 
ATOM   6924  C  C   . PHE D 1 48  ? -10.922 -0.945  -31.311 1.00 18.81 ? 48  PHE D C   1 
ATOM   6925  O  O   . PHE D 1 48  ? -11.646 -1.732  -31.799 1.00 21.87 ? 48  PHE D O   1 
ATOM   6926  C  CB  . PHE D 1 48  ? -8.856  -2.246  -32.037 1.00 15.52 ? 48  PHE D CB  1 
ATOM   6927  C  CG  . PHE D 1 48  ? -7.535  -2.781  -31.615 1.00 14.22 ? 48  PHE D CG  1 
ATOM   6928  C  CD1 . PHE D 1 48  ? -6.487  -1.925  -31.328 1.00 12.68 ? 48  PHE D CD1 1 
ATOM   6929  C  CD2 . PHE D 1 48  ? -7.404  -4.181  -31.301 1.00 16.98 ? 48  PHE D CD2 1 
ATOM   6930  C  CE1 . PHE D 1 48  ? -5.269  -2.355  -30.828 1.00 12.02 ? 48  PHE D CE1 1 
ATOM   6931  C  CE2 . PHE D 1 48  ? -6.206  -4.663  -30.760 1.00 16.12 ? 48  PHE D CE2 1 
ATOM   6932  C  CZ  . PHE D 1 48  ? -5.151  -3.752  -30.519 1.00 14.97 ? 48  PHE D CZ  1 
ATOM   6933  N  N   . GLN D 1 49  ? -11.220 0.350   -31.150 1.00 15.39 ? 49  GLN D N   1 
ATOM   6934  C  CA  . GLN D 1 49  ? -12.602 0.854   -31.385 1.00 18.36 ? 49  GLN D CA  1 
ATOM   6935  C  C   . GLN D 1 49  ? -12.691 1.694   -32.679 1.00 16.33 ? 49  GLN D C   1 
ATOM   6936  O  O   . GLN D 1 49  ? -11.888 2.560   -32.941 1.00 15.42 ? 49  GLN D O   1 
ATOM   6937  C  CB  . GLN D 1 49  ? -13.079 1.661   -30.190 1.00 19.70 ? 49  GLN D CB  1 
ATOM   6938  C  CG  . GLN D 1 49  ? -13.010 0.885   -28.874 1.00 22.41 ? 49  GLN D CG  1 
ATOM   6939  C  CD  . GLN D 1 49  ? -13.865 -0.394  -29.008 1.00 29.07 ? 49  GLN D CD  1 
ATOM   6940  O  OE1 . GLN D 1 49  ? -13.360 -1.539  -29.074 1.00 33.69 ? 49  GLN D OE1 1 
ATOM   6941  N  NE2 . GLN D 1 49  ? -15.204 -0.197  -29.090 1.00 32.08 ? 49  GLN D NE2 1 
ATOM   6942  N  N   . GLY D 1 50  ? -13.738 1.467   -33.481 1.00 16.94 ? 50  GLY D N   1 
ATOM   6943  C  CA  . GLY D 1 50  ? -13.983 2.267   -34.674 1.00 16.20 ? 50  GLY D CA  1 
ATOM   6944  C  C   . GLY D 1 50  ? -12.903 2.005   -35.720 1.00 12.83 ? 50  GLY D C   1 
ATOM   6945  O  O   . GLY D 1 50  ? -12.799 2.758   -36.670 1.00 13.87 ? 50  GLY D O   1 
ATOM   6946  N  N   . TYR D 1 51  ? -12.306 0.778   -35.624 1.00 12.91 ? 51  TYR D N   1 
ATOM   6947  C  CA  . TYR D 1 51  ? -11.281 0.364   -36.665 1.00 12.12 ? 51  TYR D CA  1 
ATOM   6948  C  C   . TYR D 1 51  ? -11.907 -0.100  -37.930 1.00 12.21 ? 51  TYR D C   1 
ATOM   6949  O  O   . TYR D 1 51  ? -11.290 -0.163  -38.993 1.00 12.20 ? 51  TYR D O   1 
ATOM   6950  C  CB  . TYR D 1 51  ? -10.303 -0.760  -36.111 1.00 12.40 ? 51  TYR D CB  1 
ATOM   6951  C  CG  . TYR D 1 51  ? -9.092  -0.187  -35.353 1.00 11.59 ? 51  TYR D CG  1 
ATOM   6952  C  CD1 . TYR D 1 51  ? -7.773  -0.674  -35.641 1.00 10.30 ? 51  TYR D CD1 1 
ATOM   6953  C  CD2 . TYR D 1 51  ? -9.206  0.844   -34.401 1.00 12.74 ? 51  TYR D CD2 1 
ATOM   6954  C  CE1 . TYR D 1 51  ? -6.689  -0.172  -34.999 1.00 10.90 ? 51  TYR D CE1 1 
ATOM   6955  C  CE2 . TYR D 1 51  ? -8.132  1.377   -33.765 1.00 11.89 ? 51  TYR D CE2 1 
ATOM   6956  C  CZ  . TYR D 1 51  ? -6.826  0.843   -34.073 1.00 12.33 ? 51  TYR D CZ  1 
ATOM   6957  O  OH  . TYR D 1 51  ? -5.674  1.320   -33.536 1.00 12.18 ? 51  TYR D OH  1 
ATOM   6958  N  N   . ASN D 1 52  ? -13.202 -0.489  -37.874 1.00 13.98 ? 52  ASN D N   1 
ATOM   6959  C  CA  . ASN D 1 52  ? -13.836 -1.046  -39.030 1.00 13.56 ? 52  ASN D CA  1 
ATOM   6960  C  C   . ASN D 1 52  ? -14.435 0.053   -39.904 1.00 16.17 ? 52  ASN D C   1 
ATOM   6961  O  O   . ASN D 1 52  ? -15.594 0.521   -39.715 1.00 16.84 ? 52  ASN D O   1 
ATOM   6962  C  CB  . ASN D 1 52  ? -14.961 -2.032  -38.599 1.00 15.31 ? 52  ASN D CB  1 
ATOM   6963  C  CG  . ASN D 1 52  ? -15.463 -2.837  -39.726 1.00 17.56 ? 52  ASN D CG  1 
ATOM   6964  O  OD1 . ASN D 1 52  ? -15.357 -2.557  -40.859 1.00 19.64 ? 52  ASN D OD1 1 
ATOM   6965  N  ND2 . ASN D 1 52  ? -16.193 -3.867  -39.334 1.00 23.45 ? 52  ASN D ND2 1 
ATOM   6966  N  N   . LEU D 1 53  ? -13.637 0.519   -40.821 1.00 14.71 ? 53  LEU D N   1 
ATOM   6967  C  CA  . LEU D 1 53  ? -14.044 1.738   -41.588 1.00 13.68 ? 53  LEU D CA  1 
ATOM   6968  C  C   . LEU D 1 53  ? -15.021 1.330   -42.746 1.00 15.72 ? 53  LEU D C   1 
ATOM   6969  O  O   . LEU D 1 53  ? -14.864 0.220   -43.353 1.00 15.72 ? 53  LEU D O   1 
ATOM   6970  C  CB  . LEU D 1 53  ? -12.819 2.454   -42.158 1.00 14.69 ? 53  LEU D CB  1 
ATOM   6971  C  CG  . LEU D 1 53  ? -11.816 2.807   -41.054 1.00 15.13 ? 53  LEU D CG  1 
ATOM   6972  C  CD1 . LEU D 1 53  ? -10.709 3.653   -41.770 1.00 14.19 ? 53  LEU D CD1 1 
ATOM   6973  C  CD2 . LEU D 1 53  ? -12.368 3.677   -39.955 1.00 14.20 ? 53  LEU D CD2 1 
ATOM   6974  N  N   . SER D 1 54  ? -16.019 2.139   -43.014 1.00 15.63 ? 54  SER D N   1 
ATOM   6975  C  CA  . SER D 1 54  ? -16.965 1.728   -44.046 1.00 15.48 ? 54  SER D CA  1 
ATOM   6976  C  C   . SER D 1 54  ? -16.370 1.760   -45.435 1.00 16.33 ? 54  SER D C   1 
ATOM   6977  O  O   . SER D 1 54  ? -15.768 2.786   -45.837 1.00 15.05 ? 54  SER D O   1 
ATOM   6978  C  CB  . SER D 1 54  ? -18.168 2.693   -43.988 1.00 15.54 ? 54  SER D CB  1 
ATOM   6979  O  OG  . SER D 1 54  ? -19.063 2.338   -45.033 1.00 16.95 ? 54  SER D OG  1 
ATOM   6980  N  N   . ALA D 1 55  ? -16.707 0.754   -46.217 1.00 19.89 ? 55  ALA D N   1 
ATOM   6981  C  CA  . ALA D 1 55  ? -16.403 0.742   -47.706 1.00 20.01 ? 55  ALA D CA  1 
ATOM   6982  C  C   . ALA D 1 55  ? -17.023 1.879   -48.534 1.00 20.18 ? 55  ALA D C   1 
ATOM   6983  O  O   . ALA D 1 55  ? -16.595 2.223   -49.657 1.00 18.45 ? 55  ALA D O   1 
ATOM   6984  C  CB  . ALA D 1 55  ? -16.754 -0.681  -48.298 1.00 23.09 ? 55  ALA D CB  1 
ATOM   6985  N  N   . ASN D 1 56  ? -18.038 2.529   -48.004 1.00 19.98 ? 56  ASN D N   1 
ATOM   6986  C  CA  . ASN D 1 56  ? -18.671 3.640   -48.700 1.00 19.78 ? 56  ASN D CA  1 
ATOM   6987  C  C   . ASN D 1 56  ? -18.097 4.961   -48.310 1.00 18.49 ? 56  ASN D C   1 
ATOM   6988  O  O   . ASN D 1 56  ? -18.478 5.976   -48.847 1.00 20.93 ? 56  ASN D O   1 
ATOM   6989  C  CB  . ASN D 1 56  ? -20.225 3.711   -48.458 1.00 19.62 ? 56  ASN D CB  1 
ATOM   6990  C  CG  . ASN D 1 56  ? -20.975 2.490   -49.049 1.00 30.57 ? 56  ASN D CG  1 
ATOM   6991  O  OD1 . ASN D 1 56  ? -20.496 1.841   -50.011 1.00 32.39 ? 56  ASN D OD1 1 
ATOM   6992  N  ND2 . ASN D 1 56  ? -22.205 2.215   -48.524 1.00 32.10 ? 56  ASN D ND2 1 
ATOM   6993  N  N   A LYS D 1 57  ? -17.132 4.936   -47.391 0.50 17.14 ? 57  LYS D N   1 
ATOM   6994  N  N   B LYS D 1 57  ? -17.167 4.953   -47.348 0.50 16.80 ? 57  LYS D N   1 
ATOM   6995  C  CA  A LYS D 1 57  ? -16.415 6.126   -47.009 0.50 16.49 ? 57  LYS D CA  1 
ATOM   6996  C  CA  B LYS D 1 57  ? -16.427 6.152   -47.010 0.50 15.55 ? 57  LYS D CA  1 
ATOM   6997  C  C   A LYS D 1 57  ? -15.005 5.995   -47.586 0.50 16.97 ? 57  LYS D C   1 
ATOM   6998  C  C   B LYS D 1 57  ? -15.043 6.012   -47.662 0.50 16.54 ? 57  LYS D C   1 
ATOM   6999  O  O   A LYS D 1 57  ? -14.580 4.892   -47.968 0.50 17.52 ? 57  LYS D O   1 
ATOM   7000  O  O   B LYS D 1 57  ? -14.680 4.930   -48.181 0.50 16.35 ? 57  LYS D O   1 
ATOM   7001  C  CB  A LYS D 1 57  ? -16.351 6.247   -45.490 0.50 16.83 ? 57  LYS D CB  1 
ATOM   7002  C  CB  B LYS D 1 57  ? -16.300 6.361   -45.483 0.50 15.48 ? 57  LYS D CB  1 
ATOM   7003  C  CG  A LYS D 1 57  ? -17.759 6.392   -44.908 0.50 17.81 ? 57  LYS D CG  1 
ATOM   7004  C  CG  B LYS D 1 57  ? -17.545 7.055   -44.890 0.50 14.81 ? 57  LYS D CG  1 
ATOM   7005  C  CD  A LYS D 1 57  ? -17.619 6.961   -43.514 0.50 19.58 ? 57  LYS D CD  1 
ATOM   7006  C  CD  B LYS D 1 57  ? -17.344 7.254   -43.429 0.50 15.79 ? 57  LYS D CD  1 
ATOM   7007  C  CE  A LYS D 1 57  ? -17.666 8.519   -43.491 0.50 21.18 ? 57  LYS D CE  1 
ATOM   7008  C  CE  B LYS D 1 57  ? -18.683 7.574   -42.785 0.50 16.97 ? 57  LYS D CE  1 
ATOM   7009  N  NZ  A LYS D 1 57  ? -19.097 8.995   -43.593 0.50 20.98 ? 57  LYS D NZ  1 
ATOM   7010  N  NZ  B LYS D 1 57  ? -18.539 8.074   -41.378 0.50 18.68 ? 57  LYS D NZ  1 
ATOM   7011  N  N   . GLN D 1 58  ? -14.354 7.142   -47.717 1.00 15.84 ? 58  GLN D N   1 
ATOM   7012  C  CA  . GLN D 1 58  ? -13.032 7.097   -48.331 1.00 17.94 ? 58  GLN D CA  1 
ATOM   7013  C  C   . GLN D 1 58  ? -12.057 7.923   -47.542 1.00 14.69 ? 58  GLN D C   1 
ATOM   7014  O  O   . GLN D 1 58  ? -12.394 8.839   -46.833 1.00 15.94 ? 58  GLN D O   1 
ATOM   7015  C  CB  . GLN D 1 58  ? -13.097 7.381   -49.796 1.00 21.65 ? 58  GLN D CB  1 
ATOM   7016  C  CG  . GLN D 1 58  ? -13.495 8.698   -50.129 1.00 24.70 ? 58  GLN D CG  1 
ATOM   7017  C  CD  . GLN D 1 58  ? -13.509 8.920   -51.678 1.00 26.67 ? 58  GLN D CD  1 
ATOM   7018  O  OE1 . GLN D 1 58  ? -13.308 7.960   -52.471 1.00 25.23 ? 58  GLN D OE1 1 
ATOM   7019  N  NE2 . GLN D 1 58  ? -13.768 10.193  -52.094 1.00 30.24 ? 58  GLN D NE2 1 
ATOM   7020  N  N   . PHE D 1 59  ? -10.797 7.493   -47.595 1.00 13.92 ? 59  PHE D N   1 
ATOM   7021  C  CA  . PHE D 1 59  ? -9.724  8.010   -46.685 1.00 12.54 ? 59  PHE D CA  1 
ATOM   7022  C  C   . PHE D 1 59  ? -8.545  8.409   -47.557 1.00 9.76  ? 59  PHE D C   1 
ATOM   7023  O  O   . PHE D 1 59  ? -8.229  7.740   -48.525 1.00 11.65 ? 59  PHE D O   1 
ATOM   7024  C  CB  . PHE D 1 59  ? -9.399  6.951   -45.633 1.00 12.01 ? 59  PHE D CB  1 
ATOM   7025  C  CG  . PHE D 1 59  ? -10.617 6.615   -44.835 1.00 11.27 ? 59  PHE D CG  1 
ATOM   7026  C  CD1 . PHE D 1 59  ? -11.528 5.671   -45.307 1.00 13.75 ? 59  PHE D CD1 1 
ATOM   7027  C  CD2 . PHE D 1 59  ? -10.903 7.412   -43.732 1.00 13.99 ? 59  PHE D CD2 1 
ATOM   7028  C  CE1 . PHE D 1 59  ? -12.745 5.439   -44.577 1.00 13.22 ? 59  PHE D CE1 1 
ATOM   7029  C  CE2 . PHE D 1 59  ? -12.028 7.204   -43.022 1.00 15.02 ? 59  PHE D CE2 1 
ATOM   7030  C  CZ  . PHE D 1 59  ? -12.985 6.223   -43.416 1.00 14.83 ? 59  PHE D CZ  1 
ATOM   7031  N  N   . LEU D 1 60  ? -7.957  9.544   -47.232 1.00 10.49 ? 60  LEU D N   1 
ATOM   7032  C  CA  . LEU D 1 60  ? -6.945  10.148  -48.085 1.00 12.79 ? 60  LEU D CA  1 
ATOM   7033  C  C   . LEU D 1 60  ? -5.570  9.513   -47.854 1.00 11.09 ? 60  LEU D C   1 
ATOM   7034  O  O   . LEU D 1 60  ? -5.016  9.502   -46.704 1.00 12.47 ? 60  LEU D O   1 
ATOM   7035  C  CB  . LEU D 1 60  ? -6.796  11.577  -47.644 1.00 13.28 ? 60  LEU D CB  1 
ATOM   7036  C  CG  . LEU D 1 60  ? -6.083  12.370  -48.732 1.00 18.61 ? 60  LEU D CG  1 
ATOM   7037  C  CD1 . LEU D 1 60  ? -6.824  12.385  -50.113 1.00 20.53 ? 60  LEU D CD1 1 
ATOM   7038  C  CD2 . LEU D 1 60  ? -5.812  13.767  -48.194 1.00 25.44 ? 60  LEU D CD2 1 
ATOM   7039  N  N   . LEU D 1 61  ? -5.000  8.993   -48.919 1.00 11.38 ? 61  LEU D N   1 
ATOM   7040  C  CA  . LEU D 1 61  ? -3.605  8.496   -48.947 1.00 11.98 ? 61  LEU D CA  1 
ATOM   7041  C  C   . LEU D 1 61  ? -2.762  9.545   -49.561 1.00 12.27 ? 61  LEU D C   1 
ATOM   7042  O  O   . LEU D 1 61  ? -3.142  10.175  -50.593 1.00 13.43 ? 61  LEU D O   1 
ATOM   7043  C  CB  . LEU D 1 61  ? -3.544  7.238   -49.793 1.00 12.67 ? 61  LEU D CB  1 
ATOM   7044  C  CG  . LEU D 1 61  ? -2.341  6.390   -49.882 1.00 14.07 ? 61  LEU D CG  1 
ATOM   7045  C  CD1 . LEU D 1 61  ? -2.213  5.612   -48.547 1.00 11.72 ? 61  LEU D CD1 1 
ATOM   7046  C  CD2 . LEU D 1 61  ? -2.428  5.330   -51.031 1.00 13.26 ? 61  LEU D CD2 1 
ATOM   7047  N  N   . THR D 1 62  ? -1.558  9.770   -48.981 1.00 11.28 ? 62  THR D N   1 
ATOM   7048  C  CA  . THR D 1 62  ? -0.723  10.799  -49.530 1.00 12.56 ? 62  THR D CA  1 
ATOM   7049  C  C   . THR D 1 62  ? 0.771   10.391  -49.404 1.00 14.43 ? 62  THR D C   1 
ATOM   7050  O  O   . THR D 1 62  ? 1.164   9.652   -48.491 1.00 14.94 ? 62  THR D O   1 
ATOM   7051  C  CB  . THR D 1 62  ? -0.859  11.979  -48.628 1.00 13.07 ? 62  THR D CB  1 
ATOM   7052  O  OG1 . THR D 1 62  ? -2.215  12.417  -48.433 1.00 20.54 ? 62  THR D OG1 1 
ATOM   7053  C  CG2 . THR D 1 62  ? 0.007   13.257  -49.016 1.00 20.02 ? 62  THR D CG2 1 
ATOM   7054  N  N   . ASN D 1 63  ? 1.541   10.797  -50.383 1.00 12.31 ? 63  ASN D N   1 
ATOM   7055  C  CA  . ASN D 1 63  ? 3.032   10.720  -50.305 1.00 11.57 ? 63  ASN D CA  1 
ATOM   7056  C  C   . ASN D 1 63  ? 3.564   11.991  -49.749 1.00 12.47 ? 63  ASN D C   1 
ATOM   7057  O  O   . ASN D 1 63  ? 3.380   13.090  -50.314 1.00 14.17 ? 63  ASN D O   1 
ATOM   7058  C  CB  . ASN D 1 63  ? 3.518   10.475  -51.777 1.00 12.37 ? 63  ASN D CB  1 
ATOM   7059  C  CG  . ASN D 1 63  ? 5.017   10.517  -51.927 1.00 11.57 ? 63  ASN D CG  1 
ATOM   7060  O  OD1 . ASN D 1 63  ? 5.726   11.088  -51.026 1.00 11.83 ? 63  ASN D OD1 1 
ATOM   7061  N  ND2 . ASN D 1 63  ? 5.513   9.814   -52.912 1.00 13.03 ? 63  ASN D ND2 1 
ATOM   7062  N  N   . ASN D 1 64  ? 4.115   11.963  -48.567 1.00 10.59 ? 64  ASN D N   1 
ATOM   7063  C  CA  . ASN D 1 64  ? 4.517   13.237  -47.938 1.00 12.95 ? 64  ASN D CA  1 
ATOM   7064  C  C   . ASN D 1 64  ? 6.022   13.561  -48.134 1.00 13.25 ? 64  ASN D C   1 
ATOM   7065  O  O   . ASN D 1 64  ? 6.596   14.405  -47.362 1.00 14.74 ? 64  ASN D O   1 
ATOM   7066  C  CB  . ASN D 1 64  ? 4.172   13.318  -46.443 1.00 15.01 ? 64  ASN D CB  1 
ATOM   7067  C  CG  . ASN D 1 64  ? 4.870   12.247  -45.627 1.00 16.89 ? 64  ASN D CG  1 
ATOM   7068  O  OD1 . ASN D 1 64  ? 5.736   11.484  -46.114 1.00 13.21 ? 64  ASN D OD1 1 
ATOM   7069  N  ND2 . ASN D 1 64  ? 4.585   12.241  -44.302 1.00 21.88 ? 64  ASN D ND2 1 
ATOM   7070  N  N   . GLY D 1 65  ? 6.640   12.785  -49.027 1.00 12.66 ? 65  GLY D N   1 
ATOM   7071  C  CA  . GLY D 1 65  ? 8.085   12.966  -49.179 1.00 12.85 ? 65  GLY D CA  1 
ATOM   7072  C  C   . GLY D 1 65  ? 8.944   12.013  -48.345 1.00 12.48 ? 65  GLY D C   1 
ATOM   7073  O  O   . GLY D 1 65  ? 10.135  11.908  -48.622 1.00 12.12 ? 65  GLY D O   1 
ATOM   7074  N  N   . HIS D 1 66  ? 8.324   11.355  -47.360 1.00 11.58 ? 66  HIS D N   1 
ATOM   7075  C  CA  . HIS D 1 66  ? 9.106   10.577  -46.407 1.00 10.85 ? 66  HIS D CA  1 
ATOM   7076  C  C   . HIS D 1 66  ? 8.549   9.145   -46.234 1.00 11.05 ? 66  HIS D C   1 
ATOM   7077  O  O   . HIS D 1 66  ? 9.256   8.209   -45.889 1.00 10.61 ? 66  HIS D O   1 
ATOM   7078  C  CB  . HIS D 1 66  ? 9.118   11.228  -45.009 1.00 11.35 ? 66  HIS D CB  1 
ATOM   7079  C  CG  . HIS D 1 66  ? 9.678   12.622  -45.035 1.00 12.30 ? 66  HIS D CG  1 
ATOM   7080  N  ND1 . HIS D 1 66  ? 11.032  12.872  -45.294 1.00 14.12 ? 66  HIS D ND1 1 
ATOM   7081  C  CD2 . HIS D 1 66  ? 9.067   13.792  -44.851 1.00 12.87 ? 66  HIS D CD2 1 
ATOM   7082  C  CE1 . HIS D 1 66  ? 11.209  14.181  -45.269 1.00 12.93 ? 66  HIS D CE1 1 
ATOM   7083  N  NE2 . HIS D 1 66  ? 10.029  14.742  -44.990 1.00 12.83 ? 66  HIS D NE2 1 
ATOM   7084  N  N   . SER D 1 67  ? 7.228   8.984   -46.434 1.00 11.38 ? 67  SER D N   1 
ATOM   7085  C  CA  . SER D 1 67  ? 6.581   7.635   -46.437 1.00 11.06 ? 67  SER D CA  1 
ATOM   7086  C  C   . SER D 1 67  ? 5.298   7.813   -47.271 1.00 13.00 ? 67  SER D C   1 
ATOM   7087  O  O   . SER D 1 67  ? 5.036   8.895   -47.735 1.00 12.73 ? 67  SER D O   1 
ATOM   7088  C  CB  . SER D 1 67  ? 6.139   7.337   -44.999 1.00 10.51 ? 67  SER D CB  1 
ATOM   7089  O  OG  . SER D 1 67  ? 5.628   6.005   -44.866 1.00 10.02 ? 67  SER D OG  1 
ATOM   7090  N  N   . VAL D 1 68  ? 4.451   6.804   -47.219 1.00 9.98  ? 68  VAL D N   1 
ATOM   7091  C  CA  . VAL D 1 68  ? 3.082   6.887   -47.741 1.00 10.69 ? 68  VAL D CA  1 
ATOM   7092  C  C   . VAL D 1 68  ? 2.183   6.823   -46.474 1.00 10.46 ? 68  VAL D C   1 
ATOM   7093  O  O   . VAL D 1 68  ? 2.360   5.950   -45.607 1.00 10.41 ? 68  VAL D O   1 
ATOM   7094  C  CB  . VAL D 1 68  ? 2.886   5.764   -48.774 1.00 10.36 ? 68  VAL D CB  1 
ATOM   7095  C  CG1 . VAL D 1 68  ? 3.024   4.377   -48.252 1.00 12.00 ? 68  VAL D CG1 1 
ATOM   7096  C  CG2 . VAL D 1 68  ? 1.447   5.884   -49.310 1.00 15.17 ? 68  VAL D CG2 1 
ATOM   7097  N  N   . LYS D 1 69  ? 1.232   7.778   -46.392 1.00 11.55 ? 69  LYS D N   1 
ATOM   7098  C  CA  . LYS D 1 69  ? 0.371   7.889   -45.185 1.00 11.06 ? 69  LYS D CA  1 
ATOM   7099  C  C   . LYS D 1 69  ? -1.118  7.826   -45.525 1.00 10.54 ? 69  LYS D C   1 
ATOM   7100  O  O   . LYS D 1 69  ? -1.496  8.291   -46.590 1.00 12.16 ? 69  LYS D O   1 
ATOM   7101  C  CB  . LYS D 1 69  ? 0.765   9.182   -44.467 1.00 16.07 ? 69  LYS D CB  1 
ATOM   7102  C  CG  . LYS D 1 69  ? -0.238  10.130  -44.030 1.00 20.19 ? 69  LYS D CG  1 
ATOM   7103  C  CD  . LYS D 1 69  ? 0.315   11.314  -43.277 1.00 16.21 ? 69  LYS D CD  1 
ATOM   7104  C  CE  . LYS D 1 69  ? -0.139  12.562  -43.985 1.00 27.21 ? 69  LYS D CE  1 
ATOM   7105  N  NZ  . LYS D 1 69  ? 0.319   13.623  -43.020 1.00 28.91 ? 69  LYS D NZ  1 
ATOM   7106  N  N   . LEU D 1 70  ? -1.878  7.103   -44.717 1.00 8.50  ? 70  LEU D N   1 
ATOM   7107  C  CA  . LEU D 1 70  ? -3.293  7.059   -44.840 1.00 8.14  ? 70  LEU D CA  1 
ATOM   7108  C  C   . LEU D 1 70  ? -3.915  7.821   -43.677 1.00 8.36  ? 70  LEU D C   1 
ATOM   7109  O  O   . LEU D 1 70  ? -3.667  7.462   -42.527 1.00 9.02  ? 70  LEU D O   1 
ATOM   7110  C  CB  . LEU D 1 70  ? -3.768  5.595   -44.858 1.00 8.90  ? 70  LEU D CB  1 
ATOM   7111  C  CG  . LEU D 1 70  ? -5.301  5.492   -44.999 1.00 8.74  ? 70  LEU D CG  1 
ATOM   7112  C  CD1 . LEU D 1 70  ? -5.721  5.899   -46.432 1.00 10.35 ? 70  LEU D CD1 1 
ATOM   7113  C  CD2 . LEU D 1 70  ? -5.668  3.965   -44.850 1.00 11.44 ? 70  LEU D CD2 1 
ATOM   7114  N  N   . ASN D 1 71  ? -4.716  8.850   -43.986 1.00 10.35 ? 71  ASN D N   1 
ATOM   7115  C  CA  . ASN D 1 71  ? -5.402  9.577   -42.904 1.00 9.97  ? 71  ASN D CA  1 
ATOM   7116  C  C   . ASN D 1 71  ? -6.472  8.737   -42.307 1.00 11.55 ? 71  ASN D C   1 
ATOM   7117  O  O   . ASN D 1 71  ? -7.133  7.959   -43.065 1.00 12.41 ? 71  ASN D O   1 
ATOM   7118  C  CB  . ASN D 1 71  ? -5.981  10.919  -43.383 1.00 13.55 ? 71  ASN D CB  1 
ATOM   7119  C  CG  . ASN D 1 71  ? -4.936  11.930  -43.596 1.00 16.25 ? 71  ASN D CG  1 
ATOM   7120  O  OD1 . ASN D 1 71  ? -3.796  11.709  -43.338 1.00 25.31 ? 71  ASN D OD1 1 
ATOM   7121  N  ND2 . ASN D 1 71  ? -5.367  13.133  -44.065 1.00 24.79 ? 71  ASN D ND2 1 
ATOM   7122  N  N   . LEU D 1 72  ? -6.660  8.835   -41.008 1.00 9.57  ? 72  LEU D N   1 
ATOM   7123  C  CA  . LEU D 1 72  ? -7.621  8.016   -40.263 1.00 9.69  ? 72  LEU D CA  1 
ATOM   7124  C  C   . LEU D 1 72  ? -8.549  8.947   -39.469 1.00 10.48 ? 72  LEU D C   1 
ATOM   7125  O  O   . LEU D 1 72  ? -8.155  10.034  -39.161 1.00 13.19 ? 72  LEU D O   1 
ATOM   7126  C  CB  . LEU D 1 72  ? -6.912  7.083   -39.224 1.00 9.49  ? 72  LEU D CB  1 
ATOM   7127  C  CG  . LEU D 1 72  ? -6.027  6.024   -39.995 1.00 11.40 ? 72  LEU D CG  1 
ATOM   7128  C  CD1 . LEU D 1 72  ? -5.197  5.316   -38.904 1.00 10.07 ? 72  LEU D CD1 1 
ATOM   7129  C  CD2 . LEU D 1 72  ? -6.846  5.000   -40.829 1.00 10.82 ? 72  LEU D CD2 1 
ATOM   7130  N  N   . PRO D 1 73  ? -9.777  8.509   -39.218 1.00 11.34 ? 73  PRO D N   1 
ATOM   7131  C  CA  . PRO D 1 73  ? -10.823 9.342   -38.559 1.00 14.81 ? 73  PRO D CA  1 
ATOM   7132  C  C   . PRO D 1 73  ? -10.595 9.331   -37.062 1.00 15.29 ? 73  PRO D C   1 
ATOM   7133  O  O   . PRO D 1 73  ? -10.229 8.252   -36.467 1.00 14.25 ? 73  PRO D O   1 
ATOM   7134  C  CB  . PRO D 1 73  ? -12.110 8.669   -38.988 1.00 14.33 ? 73  PRO D CB  1 
ATOM   7135  C  CG  . PRO D 1 73  ? -11.782 7.160   -39.059 1.00 13.88 ? 73  PRO D CG  1 
ATOM   7136  C  CD  . PRO D 1 73  ? -10.306 7.192   -39.708 1.00 10.49 ? 73  PRO D CD  1 
ATOM   7137  N  N   . SER D 1 74  ? -10.847 10.471  -36.381 1.00 16.17 ? 74  SER D N   1 
ATOM   7138  C  CA  . SER D 1 74  ? -10.645 10.546  -34.931 1.00 15.35 ? 74  SER D CA  1 
ATOM   7139  C  C   . SER D 1 74  ? -11.669 9.691   -34.124 1.00 16.37 ? 74  SER D C   1 
ATOM   7140  O  O   . SER D 1 74  ? -11.422 9.490   -32.898 1.00 19.22 ? 74  SER D O   1 
ATOM   7141  C  CB  . SER D 1 74  ? -10.543 12.006  -34.464 1.00 17.87 ? 74  SER D CB  1 
ATOM   7142  O  OG  . SER D 1 74  ? -11.807 12.663  -34.720 1.00 23.34 ? 74  SER D OG  1 
ATOM   7143  N  N   . ASP D 1 75  ? -12.733 9.200   -34.754 1.00 15.83 ? 75  ASP D N   1 
ATOM   7144  C  CA  . ASP D 1 75  ? -13.659 8.308   -34.102 1.00 19.17 ? 75  ASP D CA  1 
ATOM   7145  C  C   . ASP D 1 75  ? -12.964 6.989   -33.835 1.00 17.78 ? 75  ASP D C   1 
ATOM   7146  O  O   . ASP D 1 75  ? -13.343 6.265   -32.895 1.00 19.94 ? 75  ASP D O   1 
ATOM   7147  C  CB  . ASP D 1 75  ? -15.041 8.148   -34.803 1.00 19.87 ? 75  ASP D CB  1 
ATOM   7148  C  CG  . ASP D 1 75  ? -14.976 8.410   -36.343 1.00 31.36 ? 75  ASP D CG  1 
ATOM   7149  O  OD1 . ASP D 1 75  ? -14.841 9.635   -36.802 1.00 37.51 ? 75  ASP D OD1 1 
ATOM   7150  O  OD2 . ASP D 1 75  ? -15.026 7.382   -37.107 1.00 39.56 ? 75  ASP D OD2 1 
ATOM   7151  N  N   . MET D 1 76  ? -11.916 6.702   -34.601 1.00 15.33 ? 76  MET D N   1 
ATOM   7152  C  CA  . MET D 1 76  ? -11.222 5.424   -34.382 1.00 15.71 ? 76  MET D CA  1 
ATOM   7153  C  C   . MET D 1 76  ? -10.212 5.668   -33.199 1.00 11.05 ? 76  MET D C   1 
ATOM   7154  O  O   . MET D 1 76  ? -9.543  6.681   -33.077 1.00 13.34 ? 76  MET D O   1 
ATOM   7155  C  CB  . MET D 1 76  ? -10.556 5.102   -35.728 1.00 15.54 ? 76  MET D CB  1 
ATOM   7156  C  CG  . MET D 1 76  ? -9.594  3.928   -35.666 1.00 17.12 ? 76  MET D CG  1 
ATOM   7157  S  SD  . MET D 1 76  ? -8.864  3.773   -37.371 1.00 15.10 ? 76  MET D SD  1 
ATOM   7158  C  CE  . MET D 1 76  ? -7.424  2.744   -36.985 1.00 14.99 ? 76  MET D CE  1 
ATOM   7159  N  N   . HIS D 1 77  ? -10.176 4.689   -32.228 1.00 13.25 ? 77  HIS D N   1 
ATOM   7160  C  CA  . HIS D 1 77  ? -9.411  4.922   -31.035 1.00 12.93 ? 77  HIS D CA  1 
ATOM   7161  C  C   . HIS D 1 77  ? -8.977  3.671   -30.346 1.00 13.48 ? 77  HIS D C   1 
ATOM   7162  O  O   . HIS D 1 77  ? -9.571  2.633   -30.656 1.00 15.07 ? 77  HIS D O   1 
ATOM   7163  C  CB  . HIS D 1 77  ? -10.236 5.854   -30.068 1.00 16.67 ? 77  HIS D CB  1 
ATOM   7164  C  CG  . HIS D 1 77  ? -11.504 5.257   -29.494 1.00 19.13 ? 77  HIS D CG  1 
ATOM   7165  N  ND1 . HIS D 1 77  ? -12.714 5.236   -30.183 1.00 21.47 ? 77  HIS D ND1 1 
ATOM   7166  C  CD2 . HIS D 1 77  ? -11.782 4.783   -28.244 1.00 25.39 ? 77  HIS D CD2 1 
ATOM   7167  C  CE1 . HIS D 1 77  ? -13.654 4.684   -29.417 1.00 22.49 ? 77  HIS D CE1 1 
ATOM   7168  N  NE2 . HIS D 1 77  ? -13.107 4.375   -28.252 1.00 27.37 ? 77  HIS D NE2 1 
ATOM   7169  N  N   . ILE D 1 78  ? -8.010  3.838   -29.457 1.00 13.57 ? 78  ILE D N   1 
ATOM   7170  C  CA  . ILE D 1 78  ? -7.643  2.756   -28.569 1.00 15.20 ? 78  ILE D CA  1 
ATOM   7171  C  C   . ILE D 1 78  ? -8.101  3.076   -27.131 1.00 17.13 ? 78  ILE D C   1 
ATOM   7172  O  O   . ILE D 1 78  ? -7.915  4.215   -26.627 1.00 16.82 ? 78  ILE D O   1 
ATOM   7173  C  CB  . ILE D 1 78  ? -6.140  2.584   -28.507 1.00 15.03 ? 78  ILE D CB  1 
ATOM   7174  C  CG1 . ILE D 1 78  ? -5.437  2.270   -29.824 1.00 17.58 ? 78  ILE D CG1 1 
ATOM   7175  C  CG2 . ILE D 1 78  ? -5.775  1.442   -27.479 1.00 20.25 ? 78  ILE D CG2 1 
ATOM   7176  C  CD1 . ILE D 1 78  ? -3.955  2.720   -29.623 1.00 19.91 ? 78  ILE D CD1 1 
ATOM   7177  N  N   A GLN D 1 79  ? -8.468  1.959   -26.529 0.50 17.60 ? 79  GLN D N   1 
ATOM   7178  N  N   B GLN D 1 79  ? -8.533  2.031   -26.441 0.50 19.18 ? 79  GLN D N   1 
ATOM   7179  C  CA  A GLN D 1 79  ? -8.679  1.856   -25.143 0.50 19.00 ? 79  GLN D CA  1 
ATOM   7180  C  CA  B GLN D 1 79  ? -8.897  2.092   -25.023 0.50 21.83 ? 79  GLN D CA  1 
ATOM   7181  C  C   A GLN D 1 79  ? -7.635  1.028   -24.422 0.50 18.15 ? 79  GLN D C   1 
ATOM   7182  C  C   B GLN D 1 79  ? -8.125  0.994   -24.270 0.50 20.62 ? 79  GLN D C   1 
ATOM   7183  O  O   A GLN D 1 79  ? -7.090  0.039   -24.936 0.50 15.41 ? 79  GLN D O   1 
ATOM   7184  O  O   B GLN D 1 79  ? -8.182  -0.189  -24.780 0.50 23.46 ? 79  GLN D O   1 
ATOM   7185  C  CB  A GLN D 1 79  ? -10.045 1.229   -24.907 0.50 18.79 ? 79  GLN D CB  1 
ATOM   7186  C  CB  B GLN D 1 79  ? -10.409 1.819   -24.884 0.50 22.06 ? 79  GLN D CB  1 
ATOM   7187  C  CG  A GLN D 1 79  ? -10.558 1.803   -23.601 0.50 21.21 ? 79  GLN D CG  1 
ATOM   7188  C  CG  B GLN D 1 79  ? -10.945 0.643   -25.768 0.50 19.51 ? 79  GLN D CG  1 
ATOM   7189  C  CD  A GLN D 1 79  ? -12.026 1.563   -23.374 0.50 25.91 ? 79  GLN D CD  1 
ATOM   7190  C  CD  B GLN D 1 79  ? -12.423 0.313   -25.496 0.50 25.63 ? 79  GLN D CD  1 
ATOM   7191  O  OE1 A GLN D 1 79  ? -12.864 2.280   -23.919 0.50 25.50 ? 79  GLN D OE1 1 
ATOM   7192  O  OE1 B GLN D 1 79  ? -13.156 1.104   -24.856 0.50 31.46 ? 79  GLN D OE1 1 
ATOM   7193  N  NE2 A GLN D 1 79  ? -12.346 0.601   -22.522 0.50 26.62 ? 79  GLN D NE2 1 
ATOM   7194  N  NE2 B GLN D 1 79  ? -12.872 -0.850  -25.972 0.50 28.85 ? 79  GLN D NE2 1 
ATOM   7195  N  N   . GLY D 1 80  ? -7.381  1.386   -23.185 1.00 21.52 ? 80  GLY D N   1 
ATOM   7196  C  CA  . GLY D 1 80  ? -6.527  0.530   -22.384 1.00 19.87 ? 80  GLY D CA  1 
ATOM   7197  C  C   . GLY D 1 80  ? -5.390  1.295   -21.794 1.00 23.54 ? 80  GLY D C   1 
ATOM   7198  O  O   . GLY D 1 80  ? -4.698  0.787   -20.947 1.00 25.27 ? 80  GLY D O   1 
ATOM   7199  N  N   . LEU D 1 81  ? -5.071  2.460   -22.351 1.00 16.36 ? 81  LEU D N   1 
ATOM   7200  C  CA  . LEU D 1 81  ? -3.890  3.157   -21.921 1.00 17.89 ? 81  LEU D CA  1 
ATOM   7201  C  C   . LEU D 1 81  ? -4.272  4.183   -20.771 1.00 13.46 ? 81  LEU D C   1 
ATOM   7202  O  O   . LEU D 1 81  ? -5.368  4.169   -20.372 1.00 17.44 ? 81  LEU D O   1 
ATOM   7203  C  CB  . LEU D 1 81  ? -3.313  3.885   -23.115 1.00 16.15 ? 81  LEU D CB  1 
ATOM   7204  C  CG  . LEU D 1 81  ? -2.788  2.973   -24.269 1.00 15.76 ? 81  LEU D CG  1 
ATOM   7205  C  CD1 . LEU D 1 81  ? -2.463  3.885   -25.482 1.00 18.06 ? 81  LEU D CD1 1 
ATOM   7206  C  CD2 . LEU D 1 81  ? -1.595  2.105   -23.746 1.00 14.98 ? 81  LEU D CD2 1 
ATOM   7207  N  N   . GLN D 1 82  ? -3.381  5.094   -20.371 1.00 14.15 ? 82  GLN D N   1 
ATOM   7208  C  CA  . GLN D 1 82  ? -3.732  6.042   -19.245 1.00 13.91 ? 82  GLN D CA  1 
ATOM   7209  C  C   . GLN D 1 82  ? -4.678  7.163   -19.707 1.00 14.12 ? 82  GLN D C   1 
ATOM   7210  O  O   . GLN D 1 82  ? -5.320  7.770   -18.847 1.00 16.19 ? 82  GLN D O   1 
ATOM   7211  C  CB  . GLN D 1 82  ? -2.470  6.666   -18.672 1.00 15.17 ? 82  GLN D CB  1 
ATOM   7212  C  CG  . GLN D 1 82  ? -2.102  8.080   -19.316 1.00 19.25 ? 82  GLN D CG  1 
ATOM   7213  C  CD  . GLN D 1 82  ? -1.601  7.982   -20.784 1.00 23.40 ? 82  GLN D CD  1 
ATOM   7214  O  OE1 . GLN D 1 82  ? -1.328  6.893   -21.311 1.00 19.98 ? 82  GLN D OE1 1 
ATOM   7215  N  NE2 . GLN D 1 82  ? -1.453  9.138   -21.435 1.00 20.71 ? 82  GLN D NE2 1 
ATOM   7216  N  N   . SER D 1 83  ? -4.899  7.291   -21.035 1.00 14.11 ? 83  SER D N   1 
ATOM   7217  C  CA  . SER D 1 83  ? -5.872  8.333   -21.636 1.00 14.00 ? 83  SER D CA  1 
ATOM   7218  C  C   . SER D 1 83  ? -6.470  7.680   -22.874 1.00 13.60 ? 83  SER D C   1 
ATOM   7219  O  O   . SER D 1 83  ? -5.814  6.689   -23.417 1.00 13.05 ? 83  SER D O   1 
ATOM   7220  C  CB  . SER D 1 83  ? -5.097  9.588   -22.082 1.00 14.58 ? 83  SER D CB  1 
ATOM   7221  O  OG  . SER D 1 83  ? -4.454  10.256  -20.957 1.00 14.89 ? 83  SER D OG  1 
ATOM   7222  N  N   . ARG D 1 84  ? -7.554  8.204   -23.482 1.00 12.00 ? 84  ARG D N   1 
ATOM   7223  C  CA  . ARG D 1 84  ? -8.108  7.812   -24.822 1.00 14.11 ? 84  ARG D CA  1 
ATOM   7224  C  C   . ARG D 1 84  ? -7.113  8.392   -25.895 1.00 13.41 ? 84  ARG D C   1 
ATOM   7225  O  O   . ARG D 1 84  ? -6.751  9.559   -25.851 1.00 14.03 ? 84  ARG D O   1 
ATOM   7226  C  CB  . ARG D 1 84  ? -9.537  8.321   -25.161 1.00 14.38 ? 84  ARG D CB  1 
ATOM   7227  C  CG  . ARG D 1 84  ? -9.753  8.025   -26.612 1.00 17.27 ? 84  ARG D CG  1 
ATOM   7228  C  CD  . ARG D 1 84  ? -10.693 8.744   -27.545 1.00 32.79 ? 84  ARG D CD  1 
ATOM   7229  N  NE  . ARG D 1 84  ? -12.045 8.360   -27.512 1.00 38.69 ? 84  ARG D NE  1 
ATOM   7230  C  CZ  . ARG D 1 84  ? -12.843 8.401   -28.592 1.00 40.85 ? 84  ARG D CZ  1 
ATOM   7231  N  NH1 . ARG D 1 84  ? -12.401 8.743   -29.828 1.00 35.53 ? 84  ARG D NH1 1 
ATOM   7232  N  NH2 . ARG D 1 84  ? -14.117 8.072   -28.425 1.00 39.30 ? 84  ARG D NH2 1 
ATOM   7233  N  N   . TYR D 1 85  ? -6.632  7.491   -26.757 1.00 12.26 ? 85  TYR D N   1 
ATOM   7234  C  CA  . TYR D 1 85  ? -5.807  7.876   -27.856 1.00 10.67 ? 85  TYR D CA  1 
ATOM   7235  C  C   . TYR D 1 85  ? -6.648  7.610   -29.161 1.00 12.60 ? 85  TYR D C   1 
ATOM   7236  O  O   . TYR D 1 85  ? -7.100  6.547   -29.481 1.00 13.06 ? 85  TYR D O   1 
ATOM   7237  C  CB  . TYR D 1 85  ? -4.517  7.122   -27.906 1.00 11.24 ? 85  TYR D CB  1 
ATOM   7238  C  CG  . TYR D 1 85  ? -3.501  7.626   -26.860 1.00 8.89  ? 85  TYR D CG  1 
ATOM   7239  C  CD1 . TYR D 1 85  ? -2.533  8.572   -27.193 1.00 7.96  ? 85  TYR D CD1 1 
ATOM   7240  C  CD2 . TYR D 1 85  ? -3.528  7.173   -25.539 1.00 9.94  ? 85  TYR D CD2 1 
ATOM   7241  C  CE1 . TYR D 1 85  ? -1.602  9.040   -26.251 1.00 8.44  ? 85  TYR D CE1 1 
ATOM   7242  C  CE2 . TYR D 1 85  ? -2.596  7.643   -24.581 1.00 11.40 ? 85  TYR D CE2 1 
ATOM   7243  C  CZ  . TYR D 1 85  ? -1.633  8.577   -24.952 1.00 9.86  ? 85  TYR D CZ  1 
ATOM   7244  O  OH  . TYR D 1 85  ? -0.702  9.074   -24.061 1.00 13.30 ? 85  TYR D OH  1 
ATOM   7245  N  N   . SER D 1 86  ? -6.818  8.690   -29.930 1.00 10.20 ? 86  SER D N   1 
ATOM   7246  C  CA  . SER D 1 86  ? -7.601  8.664   -31.105 1.00 9.60  ? 86  SER D CA  1 
ATOM   7247  C  C   . SER D 1 86  ? -6.663  8.603   -32.415 1.00 8.98  ? 86  SER D C   1 
ATOM   7248  O  O   . SER D 1 86  ? -5.577  9.204   -32.462 1.00 9.85  ? 86  SER D O   1 
ATOM   7249  C  CB  . SER D 1 86  ? -8.380  10.010  -31.239 1.00 12.33 ? 86  SER D CB  1 
ATOM   7250  O  OG  . SER D 1 86  ? -9.409  9.994   -30.217 1.00 13.80 ? 86  SER D OG  1 
ATOM   7251  N  N   . ALA D 1 87  ? -7.126  7.831   -33.375 1.00 10.31 ? 87  ALA D N   1 
ATOM   7252  C  CA  . ALA D 1 87  ? -6.270  7.632   -34.577 1.00 11.97 ? 87  ALA D CA  1 
ATOM   7253  C  C   . ALA D 1 87  ? -6.061  8.913   -35.362 1.00 10.97 ? 87  ALA D C   1 
ATOM   7254  O  O   . ALA D 1 87  ? -6.999  9.779   -35.339 1.00 12.28 ? 87  ALA D O   1 
ATOM   7255  C  CB  . ALA D 1 87  ? -6.873  6.571   -35.379 1.00 12.17 ? 87  ALA D CB  1 
ATOM   7256  N  N   . THR D 1 88  ? -4.888  9.089   -35.984 1.00 10.21 ? 88  THR D N   1 
ATOM   7257  C  CA  . THR D 1 88  ? -4.664  10.185  -36.914 1.00 9.51  ? 88  THR D CA  1 
ATOM   7258  C  C   . THR D 1 88  ? -4.205  9.735   -38.302 1.00 8.99  ? 88  THR D C   1 
ATOM   7259  O  O   . THR D 1 88  ? -4.686  10.210  -39.331 1.00 10.44 ? 88  THR D O   1 
ATOM   7260  C  CB  . THR D 1 88  ? -3.779  11.240  -36.237 1.00 11.83 ? 88  THR D CB  1 
ATOM   7261  O  OG1 . THR D 1 88  ? -3.569  12.267  -37.247 1.00 15.01 ? 88  THR D OG1 1 
ATOM   7262  C  CG2 . THR D 1 88  ? -2.449  10.709  -35.754 1.00 13.16 ? 88  THR D CG2 1 
ATOM   7263  N  N   . GLN D 1 89  ? -3.303  8.736   -38.306 1.00 9.72  ? 89  GLN D N   1 
ATOM   7264  C  CA  . GLN D 1 89  ? -2.811  8.292   -39.616 1.00 8.18  ? 89  GLN D CA  1 
ATOM   7265  C  C   . GLN D 1 89  ? -2.045  6.960   -39.397 1.00 8.47  ? 89  GLN D C   1 
ATOM   7266  O  O   . GLN D 1 89  ? -1.654  6.665   -38.318 1.00 8.81  ? 89  GLN D O   1 
ATOM   7267  C  CB  . GLN D 1 89  ? -1.850  9.336   -40.276 1.00 8.80  ? 89  GLN D CB  1 
ATOM   7268  C  CG  . GLN D 1 89  ? -0.737  9.747   -39.438 1.00 9.26  ? 89  GLN D CG  1 
ATOM   7269  C  CD  . GLN D 1 89  ? 0.568   9.235   -39.862 1.00 11.13 ? 89  GLN D CD  1 
ATOM   7270  O  OE1 . GLN D 1 89  ? 0.656   8.067   -40.201 1.00 12.45 ? 89  GLN D OE1 1 
ATOM   7271  N  NE2 . GLN D 1 89  ? 1.598   10.027  -39.698 1.00 17.96 ? 89  GLN D NE2 1 
ATOM   7272  N  N   . LEU D 1 90  ? -1.921  6.215   -40.482 1.00 6.86  ? 90  LEU D N   1 
ATOM   7273  C  CA  . LEU D 1 90  ? -0.960  5.140   -40.549 1.00 7.57  ? 90  LEU D CA  1 
ATOM   7274  C  C   . LEU D 1 90  ? 0.034   5.301   -41.740 1.00 5.38  ? 90  LEU D C   1 
ATOM   7275  O  O   . LEU D 1 90  ? -0.273  5.988   -42.702 1.00 8.32  ? 90  LEU D O   1 
ATOM   7276  C  CB  . LEU D 1 90  ? -1.637  3.736   -40.539 1.00 8.27  ? 90  LEU D CB  1 
ATOM   7277  C  CG  . LEU D 1 90  ? -2.599  3.427   -41.598 1.00 5.30  ? 90  LEU D CG  1 
ATOM   7278  C  CD1 . LEU D 1 90  ? -1.918  3.062   -42.926 1.00 8.92  ? 90  LEU D CD1 1 
ATOM   7279  C  CD2 . LEU D 1 90  ? -3.444  2.164   -41.219 1.00 9.02  ? 90  LEU D CD2 1 
ATOM   7280  N  N   . HIS D 1 91  ? 1.235   4.718   -41.562 1.00 5.74  ? 91  HIS D N   1 
ATOM   7281  C  CA  . HIS D 1 91  ? 2.257   4.758   -42.655 1.00 6.28  ? 91  HIS D CA  1 
ATOM   7282  C  C   . HIS D 1 91  ? 3.156   3.585   -42.436 1.00 6.20  ? 91  HIS D C   1 
ATOM   7283  O  O   . HIS D 1 91  ? 3.017   2.848   -41.454 1.00 6.43  ? 91  HIS D O   1 
ATOM   7284  C  CB  . HIS D 1 91  ? 2.990   6.104   -42.564 1.00 6.48  ? 91  HIS D CB  1 
ATOM   7285  C  CG  . HIS D 1 91  ? 3.720   6.265   -41.256 1.00 5.06  ? 91  HIS D CG  1 
ATOM   7286  N  ND1 . HIS D 1 91  ? 3.152   6.881   -40.145 1.00 7.51  ? 91  HIS D ND1 1 
ATOM   7287  C  CD2 . HIS D 1 91  ? 4.955   5.820   -40.862 1.00 8.51  ? 91  HIS D CD2 1 
ATOM   7288  C  CE1 . HIS D 1 91  ? 4.017   6.790   -39.137 1.00 6.75  ? 91  HIS D CE1 1 
ATOM   7289  N  NE2 . HIS D 1 91  ? 5.110   6.155   -39.543 1.00 6.45  ? 91  HIS D NE2 1 
ATOM   7290  N  N   . LEU D 1 92  ? 4.146   3.496   -43.353 1.00 7.33  ? 92  LEU D N   1 
ATOM   7291  C  CA  . LEU D 1 92  ? 5.055   2.326   -43.291 1.00 7.98  ? 92  LEU D CA  1 
ATOM   7292  C  C   . LEU D 1 92  ? 6.513   2.761   -43.449 1.00 6.63  ? 92  LEU D C   1 
ATOM   7293  O  O   . LEU D 1 92  ? 6.847   3.917   -43.767 1.00 6.46  ? 92  LEU D O   1 
ATOM   7294  C  CB  . LEU D 1 92  ? 4.798   1.340   -44.461 1.00 9.57  ? 92  LEU D CB  1 
ATOM   7295  C  CG  . LEU D 1 92  ? 3.371   0.717   -44.310 1.00 7.98  ? 92  LEU D CG  1 
ATOM   7296  C  CD1 . LEU D 1 92  ? 2.477   1.380   -45.221 1.00 13.43 ? 92  LEU D CD1 1 
ATOM   7297  C  CD2 . LEU D 1 92  ? 3.458   -0.734  -44.509 1.00 11.61 ? 92  LEU D CD2 1 
ATOM   7298  N  N   . HIS D 1 93  ? 7.376   1.863   -43.160 1.00 7.06  ? 93  HIS D N   1 
ATOM   7299  C  CA  . HIS D 1 93  ? 8.885   2.045   -43.294 1.00 7.40  ? 93  HIS D CA  1 
ATOM   7300  C  C   . HIS D 1 93  ? 9.389   0.826   -43.956 1.00 7.54  ? 93  HIS D C   1 
ATOM   7301  O  O   . HIS D 1 93  ? 8.877   -0.295  -43.579 1.00 6.22  ? 93  HIS D O   1 
ATOM   7302  C  CB  . HIS D 1 93  ? 9.564   2.226   -41.907 1.00 7.74  ? 93  HIS D CB  1 
ATOM   7303  C  CG  . HIS D 1 93  ? 9.060   3.419   -41.140 1.00 8.73  ? 93  HIS D CG  1 
ATOM   7304  N  ND1 . HIS D 1 93  ? 9.642   4.683   -41.248 1.00 7.57  ? 93  HIS D ND1 1 
ATOM   7305  C  CD2 . HIS D 1 93  ? 8.023   3.548   -40.266 1.00 7.00  ? 93  HIS D CD2 1 
ATOM   7306  C  CE1 . HIS D 1 93  ? 8.967   5.527   -40.439 1.00 8.38  ? 93  HIS D CE1 1 
ATOM   7307  N  NE2 . HIS D 1 93  ? 8.000   4.880   -39.844 1.00 6.33  ? 93  HIS D NE2 1 
ATOM   7308  N  N   . TRP D 1 94  ? 10.330  0.905   -44.862 1.00 6.29  ? 94  TRP D N   1 
ATOM   7309  C  CA  . TRP D 1 94  ? 10.790  -0.294  -45.630 1.00 4.83  ? 94  TRP D CA  1 
ATOM   7310  C  C   . TRP D 1 94  ? 12.218  -0.017  -46.122 1.00 6.76  ? 94  TRP D C   1 
ATOM   7311  O  O   . TRP D 1 94  ? 12.827  1.013   -45.884 1.00 7.49  ? 94  TRP D O   1 
ATOM   7312  C  CB  . TRP D 1 94  ? 9.791   -0.588  -46.747 1.00 6.70  ? 94  TRP D CB  1 
ATOM   7313  C  CG  . TRP D 1 94  ? 9.688   0.614   -47.715 1.00 6.26  ? 94  TRP D CG  1 
ATOM   7314  C  CD1 . TRP D 1 94  ? 10.525  0.893   -48.822 1.00 7.89  ? 94  TRP D CD1 1 
ATOM   7315  C  CD2 . TRP D 1 94  ? 8.689   1.641   -47.665 1.00 6.81  ? 94  TRP D CD2 1 
ATOM   7316  N  NE1 . TRP D 1 94  ? 10.096  2.062   -49.473 1.00 7.92  ? 94  TRP D NE1 1 
ATOM   7317  C  CE2 . TRP D 1 94  ? 8.944   2.518   -48.818 1.00 6.86  ? 94  TRP D CE2 1 
ATOM   7318  C  CE3 . TRP D 1 94  ? 7.621   1.970   -46.809 1.00 8.59  ? 94  TRP D CE3 1 
ATOM   7319  C  CZ2 . TRP D 1 94  ? 8.173   3.684   -49.073 1.00 7.27  ? 94  TRP D CZ2 1 
ATOM   7320  C  CZ3 . TRP D 1 94  ? 6.813   3.135   -47.116 1.00 7.92  ? 94  TRP D CZ3 1 
ATOM   7321  C  CH2 . TRP D 1 94  ? 7.107   3.981   -48.212 1.00 8.63  ? 94  TRP D CH2 1 
ATOM   7322  N  N   . GLY D 1 95  ? 12.752  -1.093  -46.705 1.00 7.05  ? 95  GLY D N   1 
ATOM   7323  C  CA  . GLY D 1 95  ? 14.149  -1.125  -47.196 1.00 7.81  ? 95  GLY D CA  1 
ATOM   7324  C  C   . GLY D 1 95  ? 14.184  -0.908  -48.689 1.00 7.66  ? 95  GLY D C   1 
ATOM   7325  O  O   . GLY D 1 95  ? 13.724  0.124   -49.205 1.00 7.34  ? 95  GLY D O   1 
ATOM   7326  N  N   . ASN D 1 96  ? 14.772  -1.878  -49.454 1.00 9.26  ? 96  ASN D N   1 
ATOM   7327  C  CA  . ASN D 1 96  ? 14.846  -1.653  -50.915 1.00 10.51 ? 96  ASN D CA  1 
ATOM   7328  C  C   . ASN D 1 96  ? 14.981  -3.052  -51.511 1.00 10.57 ? 96  ASN D C   1 
ATOM   7329  O  O   . ASN D 1 96  ? 15.160  -3.996  -50.765 1.00 11.42 ? 96  ASN D O   1 
ATOM   7330  C  CB  . ASN D 1 96  ? 16.040  -0.762  -51.281 1.00 11.21 ? 96  ASN D CB  1 
ATOM   7331  C  CG  . ASN D 1 96  ? 17.369  -1.439  -51.040 1.00 14.39 ? 96  ASN D CG  1 
ATOM   7332  O  OD1 . ASN D 1 96  ? 17.808  -2.146  -51.970 1.00 22.34 ? 96  ASN D OD1 1 
ATOM   7333  N  ND2 . ASN D 1 96  ? 18.008  -1.274  -49.899 1.00 12.16 ? 96  ASN D ND2 1 
ATOM   7334  N  N   . PRO D 1 97  ? 14.881  -3.159  -52.875 1.00 13.43 ? 97  PRO D N   1 
ATOM   7335  C  CA  . PRO D 1 97  ? 14.882  -4.508  -53.426 1.00 16.48 ? 97  PRO D CA  1 
ATOM   7336  C  C   . PRO D 1 97  ? 16.190  -5.271  -53.110 1.00 16.71 ? 97  PRO D C   1 
ATOM   7337  O  O   . PRO D 1 97  ? 16.134  -6.497  -52.866 1.00 21.13 ? 97  PRO D O   1 
ATOM   7338  C  CB  . PRO D 1 97  ? 14.619  -4.276  -54.881 1.00 18.03 ? 97  PRO D CB  1 
ATOM   7339  C  CG  . PRO D 1 97  ? 14.092  -2.833  -55.068 1.00 18.75 ? 97  PRO D CG  1 
ATOM   7340  C  CD  . PRO D 1 97  ? 14.661  -2.064  -53.827 1.00 14.24 ? 97  PRO D CD  1 
ATOM   7341  N  N   . ASN D 1 98  ? 17.312  -4.614  -52.949 1.00 15.12 ? 98  ASN D N   1 
ATOM   7342  C  CA  . ASN D 1 98  ? 18.537  -5.344  -52.607 1.00 19.17 ? 98  ASN D CA  1 
ATOM   7343  C  C   . ASN D 1 98  ? 18.761  -5.595  -51.119 1.00 20.54 ? 98  ASN D C   1 
ATOM   7344  O  O   . ASN D 1 98  ? 19.785  -6.164  -50.675 1.00 19.74 ? 98  ASN D O   1 
ATOM   7345  C  CB  . ASN D 1 98  ? 19.742  -4.597  -53.148 1.00 21.03 ? 98  ASN D CB  1 
ATOM   7346  C  CG  . ASN D 1 98  ? 19.826  -4.762  -54.669 1.00 27.89 ? 98  ASN D CG  1 
ATOM   7347  O  OD1 . ASN D 1 98  ? 19.237  -5.723  -55.245 1.00 36.51 ? 98  ASN D OD1 1 
ATOM   7348  N  ND2 . ASN D 1 98  ? 20.508  -3.827  -55.322 1.00 35.71 ? 98  ASN D ND2 1 
ATOM   7349  N  N   . ASP D 1 99  ? 17.869  -5.049  -50.300 1.00 13.67 ? 99  ASP D N   1 
ATOM   7350  C  CA  . ASP D 1 99  ? 18.013  -5.298  -48.901 1.00 12.24 ? 99  ASP D CA  1 
ATOM   7351  C  C   . ASP D 1 99  ? 16.570  -5.132  -48.301 1.00 11.24 ? 99  ASP D C   1 
ATOM   7352  O  O   . ASP D 1 99  ? 16.224  -4.027  -47.788 1.00 10.89 ? 99  ASP D O   1 
ATOM   7353  C  CB  . ASP D 1 99  ? 18.919  -4.226  -48.262 1.00 14.11 ? 99  ASP D CB  1 
ATOM   7354  C  CG  . ASP D 1 99  ? 19.134  -4.443  -46.738 1.00 15.17 ? 99  ASP D CG  1 
ATOM   7355  O  OD1 . ASP D 1 99  ? 18.784  -5.557  -46.254 1.00 18.00 ? 99  ASP D OD1 1 
ATOM   7356  O  OD2 . ASP D 1 99  ? 19.414  -3.456  -45.963 1.00 21.80 ? 99  ASP D OD2 1 
ATOM   7357  N  N   . PRO D 1 100 ? 15.741  -6.108  -48.367 1.00 11.45 ? 100 PRO D N   1 
ATOM   7358  C  CA  . PRO D 1 100 ? 14.298  -5.986  -47.978 1.00 10.71 ? 100 PRO D CA  1 
ATOM   7359  C  C   . PRO D 1 100 ? 14.259  -6.236  -46.501 1.00 9.39  ? 100 PRO D C   1 
ATOM   7360  O  O   . PRO D 1 100 ? 13.616  -7.151  -45.996 1.00 11.41 ? 100 PRO D O   1 
ATOM   7361  C  CB  . PRO D 1 100 ? 13.585  -7.097  -48.771 1.00 12.91 ? 100 PRO D CB  1 
ATOM   7362  C  CG  . PRO D 1 100 ? 14.713  -8.099  -48.984 1.00 13.45 ? 100 PRO D CG  1 
ATOM   7363  C  CD  . PRO D 1 100 ? 16.022  -7.420  -49.023 1.00 14.16 ? 100 PRO D CD  1 
ATOM   7364  N  N   . HIS D 1 101 ? 14.911  -5.379  -45.736 1.00 10.75 ? 101 HIS D N   1 
ATOM   7365  C  CA  . HIS D 1 101 ? 15.036  -5.519  -44.263 1.00 10.88 ? 101 HIS D CA  1 
ATOM   7366  C  C   . HIS D 1 101 ? 14.995  -4.153  -43.617 1.00 11.60 ? 101 HIS D C   1 
ATOM   7367  O  O   . HIS D 1 101 ? 15.967  -3.738  -42.932 1.00 12.70 ? 101 HIS D O   1 
ATOM   7368  C  CB  . HIS D 1 101 ? 16.408  -6.233  -43.925 1.00 13.72 ? 101 HIS D CB  1 
ATOM   7369  C  CG  . HIS D 1 101 ? 16.467  -7.623  -44.534 1.00 15.03 ? 101 HIS D CG  1 
ATOM   7370  N  ND1 . HIS D 1 101 ? 15.740  -8.693  -44.070 1.00 19.11 ? 101 HIS D ND1 1 
ATOM   7371  C  CD2 . HIS D 1 101 ? 17.082  -8.068  -45.658 1.00 15.31 ? 101 HIS D CD2 1 
ATOM   7372  C  CE1 . HIS D 1 101 ? 15.919  -9.752  -44.853 1.00 18.66 ? 101 HIS D CE1 1 
ATOM   7373  N  NE2 . HIS D 1 101 ? 16.740  -9.405  -45.825 1.00 18.35 ? 101 HIS D NE2 1 
ATOM   7374  N  N   . GLY D 1 102 ? 13.841  -3.501  -43.748 1.00 7.45  ? 102 GLY D N   1 
ATOM   7375  C  CA  . GLY D 1 102 ? 13.734  -2.100  -43.408 1.00 7.50  ? 102 GLY D CA  1 
ATOM   7376  C  C   . GLY D 1 102 ? 12.734  -1.847  -42.287 1.00 7.10  ? 102 GLY D C   1 
ATOM   7377  O  O   . GLY D 1 102 ? 12.272  -0.706  -42.161 1.00 9.31  ? 102 GLY D O   1 
ATOM   7378  N  N   . SER D 1 103 ? 12.439  -2.793  -41.382 1.00 6.73  ? 103 SER D N   1 
ATOM   7379  C  CA  . SER D 1 103 ? 11.677  -2.410  -40.223 1.00 6.99  ? 103 SER D CA  1 
ATOM   7380  C  C   . SER D 1 103 ? 12.545  -1.394  -39.376 1.00 7.54  ? 103 SER D C   1 
ATOM   7381  O  O   . SER D 1 103 ? 13.802  -1.382  -39.486 1.00 7.81  ? 103 SER D O   1 
ATOM   7382  C  CB  . SER D 1 103 ? 11.415  -3.609  -39.310 1.00 7.39  ? 103 SER D CB  1 
ATOM   7383  O  OG  . SER D 1 103 ? 12.622  -4.227  -38.765 1.00 7.81  ? 103 SER D OG  1 
ATOM   7384  N  N   . GLU D 1 104 ? 11.862  -0.645  -38.501 1.00 6.40  ? 104 GLU D N   1 
ATOM   7385  C  CA  . GLU D 1 104 ? 12.573  0.229   -37.588 1.00 7.32  ? 104 GLU D CA  1 
ATOM   7386  C  C   . GLU D 1 104 ? 13.001  -0.458  -36.322 1.00 6.23  ? 104 GLU D C   1 
ATOM   7387  O  O   . GLU D 1 104 ? 14.162  -0.490  -35.992 1.00 7.45  ? 104 GLU D O   1 
ATOM   7388  C  CB  . GLU D 1 104 ? 11.673  1.446   -37.280 1.00 6.41  ? 104 GLU D CB  1 
ATOM   7389  C  CG  . GLU D 1 104 ? 11.299  2.177   -38.542 1.00 7.63  ? 104 GLU D CG  1 
ATOM   7390  C  CD  . GLU D 1 104 ? 11.268  3.696   -38.341 1.00 7.68  ? 104 GLU D CD  1 
ATOM   7391  O  OE1 . GLU D 1 104 ? 10.274  4.114   -37.715 1.00 8.94  ? 104 GLU D OE1 1 
ATOM   7392  O  OE2 . GLU D 1 104 ? 12.189  4.386   -38.714 1.00 7.76  ? 104 GLU D OE2 1 
ATOM   7393  N  N   . HIS D 1 105 ? 12.023  -1.056  -35.617 1.00 6.18  ? 105 HIS D N   1 
ATOM   7394  C  CA  . HIS D 1 105 ? 12.378  -1.936  -34.480 1.00 6.87  ? 105 HIS D CA  1 
ATOM   7395  C  C   . HIS D 1 105 ? 12.995  -3.221  -35.050 1.00 6.33  ? 105 HIS D C   1 
ATOM   7396  O  O   . HIS D 1 105 ? 12.624  -3.706  -36.123 1.00 8.62  ? 105 HIS D O   1 
ATOM   7397  C  CB  . HIS D 1 105 ? 11.151  -2.233  -33.596 1.00 6.96  ? 105 HIS D CB  1 
ATOM   7398  C  CG  . HIS D 1 105 ? 10.653  -0.976  -32.970 1.00 8.23  ? 105 HIS D CG  1 
ATOM   7399  N  ND1 . HIS D 1 105 ? 9.708   -0.164  -33.553 1.00 8.52  ? 105 HIS D ND1 1 
ATOM   7400  C  CD2 . HIS D 1 105 ? 10.959  -0.443  -31.750 1.00 7.72  ? 105 HIS D CD2 1 
ATOM   7401  C  CE1 . HIS D 1 105 ? 9.517   0.876   -32.734 1.00 8.50  ? 105 HIS D CE1 1 
ATOM   7402  N  NE2 . HIS D 1 105 ? 10.285  0.752   -31.650 1.00 9.99  ? 105 HIS D NE2 1 
ATOM   7403  N  N   . THR D 1 106 ? 13.934  -3.694  -34.236 1.00 6.93  ? 106 THR D N   1 
ATOM   7404  C  CA  . THR D 1 106 ? 14.530  -5.020  -34.523 1.00 8.04  ? 106 THR D CA  1 
ATOM   7405  C  C   . THR D 1 106 ? 14.299  -5.939  -33.326 1.00 8.68  ? 106 THR D C   1 
ATOM   7406  O  O   . THR D 1 106 ? 13.999  -5.432  -32.235 1.00 8.57  ? 106 THR D O   1 
ATOM   7407  C  CB  . THR D 1 106 ? 16.034  -4.866  -34.815 1.00 8.24  ? 106 THR D CB  1 
ATOM   7408  O  OG1 . THR D 1 106 ? 16.735  -4.245  -33.717 1.00 9.02  ? 106 THR D OG1 1 
ATOM   7409  C  CG2 . THR D 1 106 ? 16.262  -3.959  -36.072 1.00 10.25 ? 106 THR D CG2 1 
ATOM   7410  N  N   . VAL D 1 107 ? 14.346  -7.269  -33.595 1.00 9.81  ? 107 VAL D N   1 
ATOM   7411  C  CA  . VAL D 1 107 ? 14.164  -8.222  -32.504 1.00 10.12 ? 107 VAL D CA  1 
ATOM   7412  C  C   . VAL D 1 107 ? 15.431  -9.101  -32.485 1.00 10.41 ? 107 VAL D C   1 
ATOM   7413  O  O   . VAL D 1 107 ? 15.804  -9.692  -33.524 1.00 12.81 ? 107 VAL D O   1 
ATOM   7414  C  CB  . VAL D 1 107 ? 12.892  -9.090  -32.723 1.00 9.45  ? 107 VAL D CB  1 
ATOM   7415  C  CG1 . VAL D 1 107 ? 12.829  -10.020 -31.573 1.00 12.06 ? 107 VAL D CG1 1 
ATOM   7416  C  CG2 . VAL D 1 107 ? 11.575  -8.157  -32.687 1.00 12.84 ? 107 VAL D CG2 1 
ATOM   7417  N  N   . SER D 1 108 ? 16.054  -9.069  -31.336 1.00 10.97 ? 108 SER D N   1 
ATOM   7418  C  CA  . SER D 1 108 ? 17.359  -9.839  -31.146 1.00 11.60 ? 108 SER D CA  1 
ATOM   7419  C  C   . SER D 1 108 ? 18.307  -9.560  -32.285 1.00 12.70 ? 108 SER D C   1 
ATOM   7420  O  O   . SER D 1 108 ? 18.930  -10.444 -32.922 1.00 13.28 ? 108 SER D O   1 
ATOM   7421  C  CB  . SER D 1 108 ? 17.057  -11.352 -31.029 1.00 12.53 ? 108 SER D CB  1 
ATOM   7422  O  OG  . SER D 1 108 ? 16.157  -11.560 -29.979 1.00 15.69 ? 108 SER D OG  1 
ATOM   7423  N  N   . GLY D 1 109 ? 18.408  -8.275  -32.631 1.00 10.41 ? 109 GLY D N   1 
ATOM   7424  C  CA  . GLY D 1 109 ? 19.321  -7.870  -33.654 1.00 12.17 ? 109 GLY D CA  1 
ATOM   7425  C  C   . GLY D 1 109 ? 18.892  -7.993  -35.116 1.00 14.13 ? 109 GLY D C   1 
ATOM   7426  O  O   . GLY D 1 109 ? 19.670  -7.530  -36.001 1.00 16.80 ? 109 GLY D O   1 
ATOM   7427  N  N   . GLN D 1 110 ? 17.690  -8.459  -35.394 1.00 12.38 ? 110 GLN D N   1 
ATOM   7428  C  CA  . GLN D 1 110 ? 17.260  -8.767  -36.726 1.00 13.21 ? 110 GLN D CA  1 
ATOM   7429  C  C   . GLN D 1 110 ? 16.152  -7.806  -37.166 1.00 9.36  ? 110 GLN D C   1 
ATOM   7430  O  O   . GLN D 1 110 ? 15.170  -7.621  -36.373 1.00 9.60  ? 110 GLN D O   1 
ATOM   7431  C  CB  . GLN D 1 110 ? 16.667  -10.174 -36.808 1.00 13.42 ? 110 GLN D CB  1 
ATOM   7432  C  CG  . GLN D 1 110 ? 17.550  -11.370 -36.174 1.00 17.20 ? 110 GLN D CG  1 
ATOM   7433  C  CD  . GLN D 1 110 ? 18.994  -11.237 -36.634 1.00 25.36 ? 110 GLN D CD  1 
ATOM   7434  O  OE1 . GLN D 1 110 ? 19.929  -10.987 -35.830 1.00 28.00 ? 110 GLN D OE1 1 
ATOM   7435  N  NE2 . GLN D 1 110 ? 19.169  -11.374 -37.902 1.00 23.19 ? 110 GLN D NE2 1 
ATOM   7436  N  N   . HIS D 1 111 ? 16.336  -7.219  -38.379 1.00 9.33  ? 111 HIS D N   1 
ATOM   7437  C  CA  . HIS D 1 111 ? 15.254  -6.484  -38.979 1.00 9.55  ? 111 HIS D CA  1 
ATOM   7438  C  C   . HIS D 1 111 ? 14.225  -7.421  -39.511 1.00 12.39 ? 111 HIS D C   1 
ATOM   7439  O  O   . HIS D 1 111 ? 14.508  -8.580  -39.922 1.00 14.94 ? 111 HIS D O   1 
ATOM   7440  C  CB  . HIS D 1 111 ? 15.685  -5.703  -40.182 1.00 10.88 ? 111 HIS D CB  1 
ATOM   7441  C  CG  . HIS D 1 111 ? 16.448  -4.456  -39.829 1.00 10.22 ? 111 HIS D CG  1 
ATOM   7442  N  ND1 . HIS D 1 111 ? 15.826  -3.220  -39.629 1.00 9.86  ? 111 HIS D ND1 1 
ATOM   7443  C  CD2 . HIS D 1 111 ? 17.779  -4.270  -39.593 1.00 11.18 ? 111 HIS D CD2 1 
ATOM   7444  C  CE1 . HIS D 1 111 ? 16.757  -2.333  -39.308 1.00 11.29 ? 111 HIS D CE1 1 
ATOM   7445  N  NE2 . HIS D 1 111 ? 17.956  -2.933  -39.296 1.00 13.57 ? 111 HIS D NE2 1 
ATOM   7446  N  N   . PHE D 1 112 ? 12.997  -6.957  -39.487 1.00 9.20  ? 112 PHE D N   1 
ATOM   7447  C  CA  . PHE D 1 112 ? 11.982  -7.468  -40.384 1.00 9.39  ? 112 PHE D CA  1 
ATOM   7448  C  C   . PHE D 1 112 ? 11.942  -6.748  -41.743 1.00 8.06  ? 112 PHE D C   1 
ATOM   7449  O  O   . PHE D 1 112 ? 12.680  -5.768  -41.890 1.00 8.77  ? 112 PHE D O   1 
ATOM   7450  C  CB  . PHE D 1 112 ? 10.601  -7.412  -39.636 1.00 10.77 ? 112 PHE D CB  1 
ATOM   7451  C  CG  . PHE D 1 112 ? 10.505  -8.509  -38.558 1.00 11.44 ? 112 PHE D CG  1 
ATOM   7452  C  CD1 . PHE D 1 112 ? 9.886   -9.677  -38.869 1.00 17.12 ? 112 PHE D CD1 1 
ATOM   7453  C  CD2 . PHE D 1 112 ? 11.081  -8.367  -37.298 1.00 13.51 ? 112 PHE D CD2 1 
ATOM   7454  C  CE1 . PHE D 1 112 ? 9.766   -10.742 -37.956 1.00 18.49 ? 112 PHE D CE1 1 
ATOM   7455  C  CE2 . PHE D 1 112 ? 10.952  -9.454  -36.375 1.00 17.83 ? 112 PHE D CE2 1 
ATOM   7456  C  CZ  . PHE D 1 112 ? 10.325  -10.578 -36.748 1.00 14.57 ? 112 PHE D CZ  1 
ATOM   7457  N  N   . ALA D 1 113 ? 11.140  -7.227  -42.673 1.00 7.12  ? 113 ALA D N   1 
ATOM   7458  C  CA  . ALA D 1 113 ? 11.088  -6.614  -44.028 1.00 9.01  ? 113 ALA D CA  1 
ATOM   7459  C  C   . ALA D 1 113 ? 10.623  -5.170  -43.983 1.00 8.71  ? 113 ALA D C   1 
ATOM   7460  O  O   . ALA D 1 113 ? 11.141  -4.313  -44.740 1.00 7.56  ? 113 ALA D O   1 
ATOM   7461  C  CB  . ALA D 1 113 ? 10.272  -7.394  -44.967 1.00 10.09 ? 113 ALA D CB  1 
ATOM   7462  N  N   . ALA D 1 114 ? 9.590   -4.898  -43.191 1.00 6.56  ? 114 ALA D N   1 
ATOM   7463  C  CA  . ALA D 1 114 ? 9.025   -3.551  -43.185 1.00 6.12  ? 114 ALA D CA  1 
ATOM   7464  C  C   . ALA D 1 114 ? 8.303   -3.403  -41.847 1.00 7.71  ? 114 ALA D C   1 
ATOM   7465  O  O   . ALA D 1 114 ? 8.254   -4.305  -40.952 1.00 6.97  ? 114 ALA D O   1 
ATOM   7466  C  CB  . ALA D 1 114 ? 8.069   -3.380  -44.362 1.00 6.83  ? 114 ALA D CB  1 
ATOM   7467  N  N   . GLU D 1 115 ? 7.678   -2.219  -41.632 1.00 6.12  ? 115 GLU D N   1 
ATOM   7468  C  CA  . GLU D 1 115 ? 6.958   -1.933  -40.352 1.00 7.86  ? 115 GLU D CA  1 
ATOM   7469  C  C   . GLU D 1 115 ? 5.819   -1.012  -40.591 1.00 6.52  ? 115 GLU D C   1 
ATOM   7470  O  O   . GLU D 1 115 ? 5.986   -0.002  -41.347 1.00 6.91  ? 115 GLU D O   1 
ATOM   7471  C  CB  . GLU D 1 115 ? 7.981   -1.356  -39.337 1.00 7.48  ? 115 GLU D CB  1 
ATOM   7472  C  CG  . GLU D 1 115 ? 7.406   -1.191  -37.945 1.00 8.83  ? 115 GLU D CG  1 
ATOM   7473  C  CD  . GLU D 1 115 ? 8.460   -1.013  -36.880 1.00 7.77  ? 115 GLU D CD  1 
ATOM   7474  O  OE1 . GLU D 1 115 ? 9.624   -1.486  -37.058 1.00 8.29  ? 115 GLU D OE1 1 
ATOM   7475  O  OE2 . GLU D 1 115 ? 8.175   -0.364  -35.823 1.00 7.42  ? 115 GLU D OE2 1 
ATOM   7476  N  N   . LEU D 1 116 ? 4.658   -1.313  -40.024 1.00 6.81  ? 116 LEU D N   1 
ATOM   7477  C  CA  . LEU D 1 116 ? 3.464   -0.374  -40.083 1.00 6.72  ? 116 LEU D CA  1 
ATOM   7478  C  C   . LEU D 1 116 ? 3.312   0.316   -38.773 1.00 6.71  ? 116 LEU D C   1 
ATOM   7479  O  O   . LEU D 1 116 ? 3.502   -0.307  -37.665 1.00 7.76  ? 116 LEU D O   1 
ATOM   7480  C  CB  . LEU D 1 116 ? 2.204   -1.318  -40.233 1.00 6.72  ? 116 LEU D CB  1 
ATOM   7481  C  CG  . LEU D 1 116 ? 0.911   -0.542  -40.154 1.00 7.21  ? 116 LEU D CG  1 
ATOM   7482  C  CD1 . LEU D 1 116 ? 0.627   0.277   -41.345 1.00 8.88  ? 116 LEU D CD1 1 
ATOM   7483  C  CD2 . LEU D 1 116 ? -0.255  -1.434  -39.948 1.00 9.72  ? 116 LEU D CD2 1 
ATOM   7484  N  N   . HIS D 1 117 ? 3.137   1.692   -38.856 1.00 6.04  ? 117 HIS D N   1 
ATOM   7485  C  CA  . HIS D 1 117 ? 2.829   2.447   -37.620 1.00 6.80  ? 117 HIS D CA  1 
ATOM   7486  C  C   . HIS D 1 117 ? 1.419   3.039   -37.758 1.00 7.08  ? 117 HIS D C   1 
ATOM   7487  O  O   . HIS D 1 117 ? 1.108   3.722   -38.731 1.00 7.88  ? 117 HIS D O   1 
ATOM   7488  C  CB  . HIS D 1 117 ? 3.826   3.571   -37.533 1.00 7.27  ? 117 HIS D CB  1 
ATOM   7489  C  CG  . HIS D 1 117 ? 5.173   3.091   -37.209 1.00 6.24  ? 117 HIS D CG  1 
ATOM   7490  N  ND1 . HIS D 1 117 ? 6.352   3.817   -37.490 1.00 7.00  ? 117 HIS D ND1 1 
ATOM   7491  C  CD2 . HIS D 1 117 ? 5.579   1.906   -36.641 1.00 8.32  ? 117 HIS D CD2 1 
ATOM   7492  C  CE1 . HIS D 1 117 ? 7.401   3.113   -37.016 1.00 9.34  ? 117 HIS D CE1 1 
ATOM   7493  N  NE2 . HIS D 1 117 ? 6.956   1.943   -36.529 1.00 6.24  ? 117 HIS D NE2 1 
ATOM   7494  N  N   . ILE D 1 118 ? 0.608   2.707   -36.767 1.00 7.04  ? 118 ILE D N   1 
ATOM   7495  C  CA  . ILE D 1 118 ? -0.735  3.372   -36.644 1.00 7.83  ? 118 ILE D CA  1 
ATOM   7496  C  C   . ILE D 1 118 ? -0.652  4.406   -35.555 1.00 6.65  ? 118 ILE D C   1 
ATOM   7497  O  O   . ILE D 1 118 ? -0.495  4.036   -34.384 1.00 8.77  ? 118 ILE D O   1 
ATOM   7498  C  CB  . ILE D 1 118 ? -1.852  2.361   -36.426 1.00 8.00  ? 118 ILE D CB  1 
ATOM   7499  C  CG1 . ILE D 1 118 ? -1.688  1.141   -37.367 1.00 7.47  ? 118 ILE D CG1 1 
ATOM   7500  C  CG2 . ILE D 1 118 ? -3.227  3.109   -36.552 1.00 9.08  ? 118 ILE D CG2 1 
ATOM   7501  C  CD1 . ILE D 1 118 ? -2.828  0.032   -37.016 1.00 10.27 ? 118 ILE D CD1 1 
ATOM   7502  N  N   . VAL D 1 119 ? -0.610  5.682   -35.964 1.00 7.00  ? 119 VAL D N   1 
ATOM   7503  C  CA  . VAL D 1 119 ? -0.409  6.775   -35.021 1.00 7.39  ? 119 VAL D CA  1 
ATOM   7504  C  C   . VAL D 1 119 ? -1.726  7.313   -34.461 1.00 7.38  ? 119 VAL D C   1 
ATOM   7505  O  O   . VAL D 1 119 ? -2.675  7.507   -35.212 1.00 8.08  ? 119 VAL D O   1 
ATOM   7506  C  CB  . VAL D 1 119 ? 0.356   7.917   -35.754 1.00 7.28  ? 119 VAL D CB  1 
ATOM   7507  C  CG1 . VAL D 1 119 ? 0.638   9.118   -34.843 1.00 9.17  ? 119 VAL D CG1 1 
ATOM   7508  C  CG2 . VAL D 1 119 ? 1.609   7.383   -36.482 1.00 6.67  ? 119 VAL D CG2 1 
ATOM   7509  N  N   . HIS D 1 120 ? -1.661  7.494   -33.124 1.00 7.84  ? 120 HIS D N   1 
ATOM   7510  C  CA  . HIS D 1 120 ? -2.828  8.054   -32.354 1.00 8.53  ? 120 HIS D CA  1 
ATOM   7511  C  C   . HIS D 1 120 ? -2.308  9.164   -31.501 1.00 8.83  ? 120 HIS D C   1 
ATOM   7512  O  O   . HIS D 1 120 ? -1.140  9.216   -31.122 1.00 9.09  ? 120 HIS D O   1 
ATOM   7513  C  CB  . HIS D 1 120 ? -3.380  6.936   -31.406 1.00 9.31  ? 120 HIS D CB  1 
ATOM   7514  C  CG  . HIS D 1 120 ? -3.863  5.676   -32.099 1.00 8.71  ? 120 HIS D CG  1 
ATOM   7515  N  ND1 . HIS D 1 120 ? -2.963  4.736   -32.662 1.00 9.42  ? 120 HIS D ND1 1 
ATOM   7516  C  CD2 . HIS D 1 120 ? -5.104  5.197   -32.299 1.00 10.31 ? 120 HIS D CD2 1 
ATOM   7517  C  CE1 . HIS D 1 120 ? -3.690  3.736   -33.131 1.00 9.03  ? 120 HIS D CE1 1 
ATOM   7518  N  NE2 . HIS D 1 120 ? -5.001  3.939   -32.876 1.00 10.09 ? 120 HIS D NE2 1 
ATOM   7519  N  N   . TYR D 1 121 ? -3.257  10.061  -31.176 1.00 9.09  ? 121 TYR D N   1 
ATOM   7520  C  CA  . TYR D 1 121 ? -2.870  11.175  -30.295 1.00 10.55 ? 121 TYR D CA  1 
ATOM   7521  C  C   . TYR D 1 121 ? -3.845  11.226  -29.049 1.00 9.70  ? 121 TYR D C   1 
ATOM   7522  O  O   . TYR D 1 121 ? -4.933  10.683  -29.109 1.00 10.15 ? 121 TYR D O   1 
ATOM   7523  C  CB  . TYR D 1 121 ? -2.941  12.500  -31.120 1.00 11.03 ? 121 TYR D CB  1 
ATOM   7524  C  CG  . TYR D 1 121 ? -4.361  12.957  -31.458 1.00 9.88  ? 121 TYR D CG  1 
ATOM   7525  C  CD1 . TYR D 1 121 ? -5.041  13.909  -30.690 1.00 11.59 ? 121 TYR D CD1 1 
ATOM   7526  C  CD2 . TYR D 1 121 ? -5.028  12.410  -32.542 1.00 10.79 ? 121 TYR D CD2 1 
ATOM   7527  C  CE1 . TYR D 1 121 ? -6.346  14.307  -31.023 1.00 12.45 ? 121 TYR D CE1 1 
ATOM   7528  C  CE2 . TYR D 1 121 ? -6.314  12.795  -32.875 1.00 11.87 ? 121 TYR D CE2 1 
ATOM   7529  C  CZ  . TYR D 1 121 ? -6.979  13.740  -32.117 1.00 14.43 ? 121 TYR D CZ  1 
ATOM   7530  O  OH  . TYR D 1 121 ? -8.267  14.091  -32.492 1.00 16.83 ? 121 TYR D OH  1 
ATOM   7531  N  N   . ASN D 1 122 ? -3.313  11.879  -28.040 1.00 10.46 ? 122 ASN D N   1 
ATOM   7532  C  CA  . ASN D 1 122 ? -4.009  11.975  -26.684 1.00 11.19 ? 122 ASN D CA  1 
ATOM   7533  C  C   . ASN D 1 122 ? -5.140  13.027  -26.810 1.00 13.06 ? 122 ASN D C   1 
ATOM   7534  O  O   . ASN D 1 122 ? -4.865  14.214  -26.645 1.00 13.82 ? 122 ASN D O   1 
ATOM   7535  C  CB  . ASN D 1 122 ? -3.012  12.261  -25.584 1.00 10.86 ? 122 ASN D CB  1 
ATOM   7536  C  CG  . ASN D 1 122 ? -3.619  12.143  -24.202 1.00 12.63 ? 122 ASN D CG  1 
ATOM   7537  O  OD1 . ASN D 1 122 ? -4.813  12.337  -24.046 1.00 11.81 ? 122 ASN D OD1 1 
ATOM   7538  N  ND2 . ASN D 1 122 ? -2.765  11.884  -23.213 1.00 14.69 ? 122 ASN D ND2 1 
ATOM   7539  N  N   . SER D 1 123 ? -6.284  12.520  -27.181 1.00 11.18 ? 123 SER D N   1 
ATOM   7540  C  CA  . SER D 1 123 ? -7.491  13.362  -27.395 1.00 14.92 ? 123 SER D CA  1 
ATOM   7541  C  C   . SER D 1 123 ? -8.104  13.790  -26.066 1.00 14.79 ? 123 SER D C   1 
ATOM   7542  O  O   . SER D 1 123 ? -8.956  14.684  -26.067 1.00 16.08 ? 123 SER D O   1 
ATOM   7543  C  CB  . SER D 1 123 ? -8.495  12.757  -28.359 1.00 13.99 ? 123 SER D CB  1 
ATOM   7544  O  OG  . SER D 1 123 ? -8.852  11.415  -27.967 1.00 14.54 ? 123 SER D OG  1 
ATOM   7545  N  N   . ASP D 1 124 ? -7.690  13.235  -24.936 1.00 14.46 ? 124 ASP D N   1 
ATOM   7546  C  CA  . ASP D 1 124 ? -8.216  13.772  -23.625 1.00 14.63 ? 124 ASP D CA  1 
ATOM   7547  C  C   . ASP D 1 124 ? -7.490  15.081  -23.328 1.00 16.66 ? 124 ASP D C   1 
ATOM   7548  O  O   . ASP D 1 124 ? -8.056  15.922  -22.598 1.00 18.92 ? 124 ASP D O   1 
ATOM   7549  C  CB  . ASP D 1 124 ? -7.809  12.758  -22.544 1.00 15.62 ? 124 ASP D CB  1 
ATOM   7550  C  CG  . ASP D 1 124 ? -8.710  11.539  -22.547 1.00 11.61 ? 124 ASP D CG  1 
ATOM   7551  O  OD1 . ASP D 1 124 ? -9.733  11.565  -23.273 1.00 13.66 ? 124 ASP D OD1 1 
ATOM   7552  O  OD2 . ASP D 1 124 ? -8.393  10.558  -21.841 1.00 15.34 ? 124 ASP D OD2 1 
ATOM   7553  N  N   . LEU D 1 125 ? -6.277  15.259  -23.761 1.00 13.47 ? 125 LEU D N   1 
ATOM   7554  C  CA  . LEU D 1 125 ? -5.421  16.407  -23.466 1.00 16.30 ? 125 LEU D CA  1 
ATOM   7555  C  C   . LEU D 1 125 ? -5.348  17.409  -24.621 1.00 16.63 ? 125 LEU D C   1 
ATOM   7556  O  O   . LEU D 1 125 ? -5.140  18.625  -24.335 1.00 16.27 ? 125 LEU D O   1 
ATOM   7557  C  CB  . LEU D 1 125 ? -3.980  16.017  -23.116 1.00 14.83 ? 125 LEU D CB  1 
ATOM   7558  C  CG  . LEU D 1 125 ? -3.725  15.501  -21.680 1.00 17.12 ? 125 LEU D CG  1 
ATOM   7559  C  CD1 . LEU D 1 125 ? -4.690  14.393  -21.276 1.00 19.01 ? 125 LEU D CD1 1 
ATOM   7560  C  CD2 . LEU D 1 125 ? -2.277  15.127  -21.519 1.00 17.41 ? 125 LEU D CD2 1 
ATOM   7561  N  N   . TYR D 1 126 ? -5.436  16.951  -25.889 1.00 13.76 ? 126 TYR D N   1 
ATOM   7562  C  CA  . TYR D 1 126 ? -5.080  17.745  -26.987 1.00 14.22 ? 126 TYR D CA  1 
ATOM   7563  C  C   . TYR D 1 126 ? -6.127  17.701  -28.081 1.00 15.31 ? 126 TYR D C   1 
ATOM   7564  O  O   . TYR D 1 126 ? -6.806  16.755  -28.281 1.00 14.65 ? 126 TYR D O   1 
ATOM   7565  C  CB  . TYR D 1 126 ? -3.717  17.354  -27.571 1.00 11.88 ? 126 TYR D CB  1 
ATOM   7566  C  CG  . TYR D 1 126 ? -2.617  17.328  -26.534 1.00 12.00 ? 126 TYR D CG  1 
ATOM   7567  C  CD1 . TYR D 1 126 ? -2.192  18.487  -25.890 1.00 11.97 ? 126 TYR D CD1 1 
ATOM   7568  C  CD2 . TYR D 1 126 ? -2.111  16.090  -26.104 1.00 12.48 ? 126 TYR D CD2 1 
ATOM   7569  C  CE1 . TYR D 1 126 ? -1.313  18.453  -24.815 1.00 11.57 ? 126 TYR D CE1 1 
ATOM   7570  C  CE2 . TYR D 1 126 ? -1.110  16.029  -25.150 1.00 12.49 ? 126 TYR D CE2 1 
ATOM   7571  C  CZ  . TYR D 1 126 ? -0.718  17.206  -24.429 1.00 12.30 ? 126 TYR D CZ  1 
ATOM   7572  O  OH  . TYR D 1 126 ? 0.226   17.228  -23.399 1.00 11.62 ? 126 TYR D OH  1 
ATOM   7573  N  N   . PRO D 1 127 ? -6.262  18.822  -28.816 1.00 15.28 ? 127 PRO D N   1 
ATOM   7574  C  CA  . PRO D 1 127 ? -7.371  18.890  -29.826 1.00 15.88 ? 127 PRO D CA  1 
ATOM   7575  C  C   . PRO D 1 127 ? -7.062  18.237  -31.120 1.00 17.36 ? 127 PRO D C   1 
ATOM   7576  O  O   . PRO D 1 127 ? -7.972  18.072  -31.921 1.00 19.59 ? 127 PRO D O   1 
ATOM   7577  C  CB  . PRO D 1 127 ? -7.488  20.418  -30.105 1.00 18.51 ? 127 PRO D CB  1 
ATOM   7578  C  CG  . PRO D 1 127 ? -6.144  21.002  -29.645 1.00 18.31 ? 127 PRO D CG  1 
ATOM   7579  C  CD  . PRO D 1 127 ? -5.625  20.102  -28.512 1.00 17.04 ? 127 PRO D CD  1 
ATOM   7580  N  N   . ASP D 1 128 ? -5.799  17.946  -31.392 1.00 14.93 ? 128 ASP D N   1 
ATOM   7581  C  CA  . ASP D 1 128 ? -5.353  17.364  -32.621 1.00 15.16 ? 128 ASP D CA  1 
ATOM   7582  C  C   . ASP D 1 128 ? -3.949  16.792  -32.533 1.00 15.11 ? 128 ASP D C   1 
ATOM   7583  O  O   . ASP D 1 128 ? -3.176  17.110  -31.564 1.00 15.14 ? 128 ASP D O   1 
ATOM   7584  C  CB  . ASP D 1 128 ? -5.415  18.435  -33.762 1.00 17.54 ? 128 ASP D CB  1 
ATOM   7585  C  CG  . ASP D 1 128 ? -4.475  19.574  -33.485 1.00 17.45 ? 128 ASP D CG  1 
ATOM   7586  O  OD1 . ASP D 1 128 ? -4.868  20.550  -32.732 1.00 23.47 ? 128 ASP D OD1 1 
ATOM   7587  O  OD2 . ASP D 1 128 ? -3.371  19.531  -33.942 1.00 21.11 ? 128 ASP D OD2 1 
ATOM   7588  N  N   . ALA D 1 129 ? -3.524  15.983  -33.518 1.00 14.64 ? 129 ALA D N   1 
ATOM   7589  C  CA  . ALA D 1 129 ? -2.285  15.321  -33.415 1.00 13.77 ? 129 ALA D CA  1 
ATOM   7590  C  C   . ALA D 1 129 ? -1.069  16.200  -33.495 1.00 14.23 ? 129 ALA D C   1 
ATOM   7591  O  O   . ALA D 1 129 ? -0.030  15.972  -32.871 1.00 15.03 ? 129 ALA D O   1 
ATOM   7592  C  CB  . ALA D 1 129 ? -2.073  14.157  -34.427 1.00 18.08 ? 129 ALA D CB  1 
ATOM   7593  N  N   A SER D 1 130 ? -1.147  17.222  -34.366 0.50 16.34 ? 130 SER D N   1 
ATOM   7594  N  N   B SER D 1 130 ? -1.193  17.228  -34.367 0.50 15.89 ? 130 SER D N   1 
ATOM   7595  C  CA  A SER D 1 130 ? -0.008  18.123  -34.491 0.50 15.57 ? 130 SER D CA  1 
ATOM   7596  C  CA  B SER D 1 130 ? -0.101  18.179  -34.528 0.50 14.54 ? 130 SER D CA  1 
ATOM   7597  C  C   A SER D 1 130 ? 0.265   18.897  -33.172 0.50 13.12 ? 130 SER D C   1 
ATOM   7598  C  C   B SER D 1 130 ? 0.224   18.840  -33.167 0.50 12.91 ? 130 SER D C   1 
ATOM   7599  O  O   A SER D 1 130 ? 1.446   19.005  -32.737 0.50 14.61 ? 130 SER D O   1 
ATOM   7600  O  O   B SER D 1 130 ? 1.366   18.795  -32.687 0.50 14.76 ? 130 SER D O   1 
ATOM   7601  C  CB  A SER D 1 130 ? -0.205  19.075  -35.670 0.50 16.80 ? 130 SER D CB  1 
ATOM   7602  C  CB  B SER D 1 130 ? -0.428  19.276  -35.565 0.50 15.44 ? 130 SER D CB  1 
ATOM   7603  O  OG  A SER D 1 130 ? 0.376   18.468  -36.792 0.50 21.94 ? 130 SER D OG  1 
ATOM   7604  O  OG  B SER D 1 130 ? 0.804   19.935  -35.847 0.50 15.34 ? 130 SER D OG  1 
ATOM   7605  N  N   . THR D 1 131 ? -0.827  19.353  -32.546 1.00 12.16 ? 131 THR D N   1 
ATOM   7606  C  CA  . THR D 1 131 ? -0.696  19.995  -31.237 1.00 12.35 ? 131 THR D CA  1 
ATOM   7607  C  C   . THR D 1 131 ? -0.119  19.038  -30.156 1.00 12.87 ? 131 THR D C   1 
ATOM   7608  O  O   . THR D 1 131 ? 0.778   19.371  -29.299 1.00 13.50 ? 131 THR D O   1 
ATOM   7609  C  CB  . THR D 1 131 ? -1.991  20.573  -30.735 1.00 13.81 ? 131 THR D CB  1 
ATOM   7610  O  OG1 . THR D 1 131 ? -2.494  21.560  -31.688 1.00 17.12 ? 131 THR D OG1 1 
ATOM   7611  C  CG2 . THR D 1 131 ? -1.843  21.308  -29.338 1.00 13.48 ? 131 THR D CG2 1 
ATOM   7612  N  N   . ALA D 1 132 ? -0.561  17.813  -30.271 1.00 12.25 ? 132 ALA D N   1 
ATOM   7613  C  CA  . ALA D 1 132 ? -0.156  16.784  -29.271 1.00 12.02 ? 132 ALA D CA  1 
ATOM   7614  C  C   . ALA D 1 132 ? 1.298   16.394  -29.429 1.00 9.93  ? 132 ALA D C   1 
ATOM   7615  O  O   . ALA D 1 132 ? 1.961   15.922  -28.476 1.00 10.85 ? 132 ALA D O   1 
ATOM   7616  C  CB  . ALA D 1 132 ? -0.933  15.505  -29.522 1.00 9.98  ? 132 ALA D CB  1 
ATOM   7617  N  N   . SER D 1 133 ? 1.799   16.449  -30.672 1.00 10.17 ? 133 SER D N   1 
ATOM   7618  C  CA  . SER D 1 133 ? 3.051   15.788  -31.006 1.00 11.30 ? 133 SER D CA  1 
ATOM   7619  C  C   . SER D 1 133 ? 4.274   16.169  -30.223 1.00 11.83 ? 133 SER D C   1 
ATOM   7620  O  O   . SER D 1 133 ? 5.234   15.448  -30.084 1.00 12.41 ? 133 SER D O   1 
ATOM   7621  C  CB  . SER D 1 133 ? 3.286   15.900  -32.540 1.00 12.58 ? 133 SER D CB  1 
ATOM   7622  O  OG  . SER D 1 133 ? 3.693   17.247  -32.857 1.00 14.23 ? 133 SER D OG  1 
ATOM   7623  N  N   . ASN D 1 134 ? 4.329   17.463  -29.739 1.00 11.06 ? 134 ASN D N   1 
ATOM   7624  C  CA  . ASN D 1 134 ? 5.508   17.947  -28.981 1.00 13.27 ? 134 ASN D CA  1 
ATOM   7625  C  C   . ASN D 1 134 ? 5.195   18.158  -27.506 1.00 12.64 ? 134 ASN D C   1 
ATOM   7626  O  O   . ASN D 1 134 ? 5.991   18.761  -26.817 1.00 14.91 ? 134 ASN D O   1 
ATOM   7627  C  CB  . ASN D 1 134 ? 6.157   19.245  -29.568 1.00 12.89 ? 134 ASN D CB  1 
ATOM   7628  C  CG  . ASN D 1 134 ? 5.261   20.440  -29.411 1.00 16.88 ? 134 ASN D CG  1 
ATOM   7629  O  OD1 . ASN D 1 134 ? 4.054   20.320  -29.338 1.00 15.34 ? 134 ASN D OD1 1 
ATOM   7630  N  ND2 . ASN D 1 134 ? 5.865   21.648  -29.395 1.00 16.81 ? 134 ASN D ND2 1 
ATOM   7631  N  N   . LYS D 1 135 ? 4.126   17.515  -27.084 1.00 12.04 ? 135 LYS D N   1 
ATOM   7632  C  CA  . LYS D 1 135 ? 3.642   17.708  -25.690 1.00 11.93 ? 135 LYS D CA  1 
ATOM   7633  C  C   . LYS D 1 135 ? 3.565   16.396  -24.920 1.00 12.27 ? 135 LYS D C   1 
ATOM   7634  O  O   . LYS D 1 135 ? 3.483   15.278  -25.451 1.00 12.47 ? 135 LYS D O   1 
ATOM   7635  C  CB  . LYS D 1 135 ? 2.286   18.375  -25.734 1.00 12.37 ? 135 LYS D CB  1 
ATOM   7636  C  CG  . LYS D 1 135 ? 2.453   19.869  -26.276 1.00 12.67 ? 135 LYS D CG  1 
ATOM   7637  C  CD  . LYS D 1 135 ? 1.116   20.582  -26.327 1.00 15.68 ? 135 LYS D CD  1 
ATOM   7638  C  CE  . LYS D 1 135 ? 1.330   21.983  -27.017 1.00 14.01 ? 135 LYS D CE  1 
ATOM   7639  N  NZ  . LYS D 1 135 ? 1.732   21.798  -28.478 1.00 14.28 ? 135 LYS D NZ  1 
ATOM   7640  N  N   A SER D 1 136 ? 3.769   16.538  -23.615 0.50 12.28 ? 136 SER D N   1 
ATOM   7641  N  N   B SER D 1 136 ? 3.470   16.559  -23.612 0.50 12.01 ? 136 SER D N   1 
ATOM   7642  C  CA  A SER D 1 136 ? 3.785   15.392  -22.729 0.50 12.57 ? 136 SER D CA  1 
ATOM   7643  C  CA  B SER D 1 136 ? 3.491   15.445  -22.677 0.50 12.99 ? 136 SER D CA  1 
ATOM   7644  C  C   A SER D 1 136 ? 2.627   14.424  -22.968 0.50 12.19 ? 136 SER D C   1 
ATOM   7645  C  C   B SER D 1 136 ? 2.474   14.384  -22.958 0.50 12.35 ? 136 SER D C   1 
ATOM   7646  O  O   A SER D 1 136 ? 1.462   14.802  -23.078 0.50 12.12 ? 136 SER D O   1 
ATOM   7647  O  O   B SER D 1 136 ? 1.259   14.658  -23.095 0.50 11.17 ? 136 SER D O   1 
ATOM   7648  C  CB  A SER D 1 136 ? 3.693   15.960  -21.328 0.50 13.76 ? 136 SER D CB  1 
ATOM   7649  C  CB  B SER D 1 136 ? 3.208   16.035  -21.283 0.50 13.06 ? 136 SER D CB  1 
ATOM   7650  O  OG  A SER D 1 136 ? 3.539   14.964  -20.389 0.50 13.73 ? 136 SER D OG  1 
ATOM   7651  O  OG  B SER D 1 136 ? 4.407   16.563  -20.723 0.50 16.56 ? 136 SER D OG  1 
ATOM   7652  N  N   . GLU D 1 137 ? 2.913   13.099  -22.966 1.00 12.55 ? 137 GLU D N   1 
ATOM   7653  C  CA  . GLU D 1 137 ? 1.916   12.101  -23.225 1.00 12.07 ? 137 GLU D CA  1 
ATOM   7654  C  C   . GLU D 1 137 ? 1.096   12.249  -24.560 1.00 11.48 ? 137 GLU D C   1 
ATOM   7655  O  O   . GLU D 1 137 ? -0.003  11.746  -24.692 1.00 11.92 ? 137 GLU D O   1 
ATOM   7656  C  CB  . GLU D 1 137 ? 0.932   11.799  -22.084 1.00 13.21 ? 137 GLU D CB  1 
ATOM   7657  C  CG  . GLU D 1 137 ? 1.570   11.922  -20.727 1.00 14.96 ? 137 GLU D CG  1 
ATOM   7658  C  CD  . GLU D 1 137 ? 2.485   10.733  -20.366 1.00 19.65 ? 137 GLU D CD  1 
ATOM   7659  O  OE1 . GLU D 1 137 ? 2.272   9.660   -20.926 1.00 25.50 ? 137 GLU D OE1 1 
ATOM   7660  O  OE2 . GLU D 1 137 ? 3.505   10.997  -19.673 1.00 28.72 ? 137 GLU D OE2 1 
ATOM   7661  N  N   . GLY D 1 138 ? 1.723   12.906  -25.542 1.00 10.21 ? 138 GLY D N   1 
ATOM   7662  C  CA  . GLY D 1 138 ? 0.921   13.260  -26.674 1.00 11.55 ? 138 GLY D CA  1 
ATOM   7663  C  C   . GLY D 1 138 ? 0.459   12.143  -27.651 1.00 8.68  ? 138 GLY D C   1 
ATOM   7664  O  O   . GLY D 1 138 ? -0.577  12.246  -28.280 1.00 9.72  ? 138 GLY D O   1 
ATOM   7665  N  N   . LEU D 1 139 ? 1.335   11.139  -27.850 1.00 9.53  ? 139 LEU D N   1 
ATOM   7666  C  CA  . LEU D 1 139 ? 1.056   10.189  -28.996 1.00 9.90  ? 139 LEU D CA  1 
ATOM   7667  C  C   . LEU D 1 139 ? 1.174   8.757   -28.466 1.00 8.51  ? 139 LEU D C   1 
ATOM   7668  O  O   . LEU D 1 139 ? 1.919   8.483   -27.487 1.00 9.39  ? 139 LEU D O   1 
ATOM   7669  C  CB  . LEU D 1 139 ? 2.144   10.381  -30.058 1.00 8.53  ? 139 LEU D CB  1 
ATOM   7670  C  CG  . LEU D 1 139 ? 2.141   11.820  -30.686 1.00 9.24  ? 139 LEU D CG  1 
ATOM   7671  C  CD1 . LEU D 1 139 ? 3.392   11.907  -31.608 1.00 13.13 ? 139 LEU D CD1 1 
ATOM   7672  C  CD2 . LEU D 1 139 ? 0.856   12.027  -31.545 1.00 12.44 ? 139 LEU D CD2 1 
ATOM   7673  N  N   . ALA D 1 140 ? 0.532   7.831   -29.185 1.00 9.14  ? 140 ALA D N   1 
ATOM   7674  C  CA  . ALA D 1 140 ? 0.713   6.390   -28.954 1.00 7.99  ? 140 ALA D CA  1 
ATOM   7675  C  C   . ALA D 1 140 ? 0.676   5.824   -30.347 1.00 7.75  ? 140 ALA D C   1 
ATOM   7676  O  O   . ALA D 1 140 ? -0.185  6.076   -31.184 1.00 10.10 ? 140 ALA D O   1 
ATOM   7677  C  CB  . ALA D 1 140 ? -0.423  5.839   -28.139 1.00 10.44 ? 140 ALA D CB  1 
ATOM   7678  N  N   . VAL D 1 141 ? 1.671   4.935   -30.598 1.00 8.59  ? 141 VAL D N   1 
ATOM   7679  C  CA  . VAL D 1 141 ? 1.730   4.254   -31.868 1.00 8.15  ? 141 VAL D CA  1 
ATOM   7680  C  C   . VAL D 1 141 ? 1.544   2.725   -31.647 1.00 8.27  ? 141 VAL D C   1 
ATOM   7681  O  O   . VAL D 1 141 ? 2.143   2.150   -30.670 1.00 8.77  ? 141 VAL D O   1 
ATOM   7682  C  CB  . VAL D 1 141 ? 3.059   4.531   -32.522 1.00 5.90  ? 141 VAL D CB  1 
ATOM   7683  C  CG1 . VAL D 1 141 ? 3.165   3.808   -33.884 1.00 8.99  ? 141 VAL D CG1 1 
ATOM   7684  C  CG2 . VAL D 1 141 ? 3.212   6.045   -32.758 1.00 9.04  ? 141 VAL D CG2 1 
ATOM   7685  N  N   . LEU D 1 142 ? 0.814   2.122   -32.563 1.00 8.12  ? 142 LEU D N   1 
ATOM   7686  C  CA  . LEU D 1 142 ? 0.785   0.662   -32.659 1.00 8.10  ? 142 LEU D CA  1 
ATOM   7687  C  C   . LEU D 1 142 ? 1.713   0.282   -33.801 1.00 8.62  ? 142 LEU D C   1 
ATOM   7688  O  O   . LEU D 1 142 ? 1.591   0.810   -34.901 1.00 9.61  ? 142 LEU D O   1 
ATOM   7689  C  CB  . LEU D 1 142 ? -0.613  0.156   -32.985 1.00 9.01  ? 142 LEU D CB  1 
ATOM   7690  C  CG  . LEU D 1 142 ? -1.714  0.518   -31.959 1.00 9.88  ? 142 LEU D CG  1 
ATOM   7691  C  CD1 . LEU D 1 142 ? -3.009  -0.098  -32.479 1.00 10.86 ? 142 LEU D CD1 1 
ATOM   7692  C  CD2 . LEU D 1 142 ? -1.384  0.045   -30.516 1.00 12.76 ? 142 LEU D CD2 1 
ATOM   7693  N  N   . ALA D 1 143 ? 2.716   -0.533  -33.485 1.00 8.80  ? 143 ALA D N   1 
ATOM   7694  C  CA  . ALA D 1 143 ? 3.692   -0.990  -34.489 1.00 7.58  ? 143 ALA D CA  1 
ATOM   7695  C  C   . ALA D 1 143 ? 3.538   -2.456  -34.857 1.00 7.10  ? 143 ALA D C   1 
ATOM   7696  O  O   . ALA D 1 143 ? 3.477   -3.333  -33.950 1.00 7.84  ? 143 ALA D O   1 
ATOM   7697  C  CB  . ALA D 1 143 ? 5.153   -0.702  -33.957 1.00 8.72  ? 143 ALA D CB  1 
ATOM   7698  N  N   . VAL D 1 144 ? 3.406   -2.683  -36.168 1.00 6.77  ? 144 VAL D N   1 
ATOM   7699  C  CA  . VAL D 1 144 ? 3.304   -4.077  -36.640 1.00 8.81  ? 144 VAL D CA  1 
ATOM   7700  C  C   . VAL D 1 144 ? 4.587   -4.394  -37.456 1.00 7.45  ? 144 VAL D C   1 
ATOM   7701  O  O   . VAL D 1 144 ? 4.860   -3.775  -38.479 1.00 8.02  ? 144 VAL D O   1 
ATOM   7702  C  CB  . VAL D 1 144 ? 2.107   -4.294  -37.507 1.00 7.39  ? 144 VAL D CB  1 
ATOM   7703  C  CG1 . VAL D 1 144 ? 1.983   -5.811  -37.886 1.00 8.96  ? 144 VAL D CG1 1 
ATOM   7704  C  CG2 . VAL D 1 144 ? 0.820   -3.796  -36.733 1.00 9.28  ? 144 VAL D CG2 1 
ATOM   7705  N  N   . LEU D 1 145 ? 5.245   -5.497  -37.044 1.00 7.73  ? 145 LEU D N   1 
ATOM   7706  C  CA  . LEU D 1 145 ? 6.454   -5.931  -37.771 1.00 8.06  ? 145 LEU D CA  1 
ATOM   7707  C  C   . LEU D 1 145 ? 5.937   -6.725  -38.984 1.00 8.14  ? 145 LEU D C   1 
ATOM   7708  O  O   . LEU D 1 145 ? 4.997   -7.531  -38.842 1.00 8.66  ? 145 LEU D O   1 
ATOM   7709  C  CB  . LEU D 1 145 ? 7.305   -6.838  -36.841 1.00 9.79  ? 145 LEU D CB  1 
ATOM   7710  C  CG  . LEU D 1 145 ? 7.822   -6.031  -35.683 1.00 10.36 ? 145 LEU D CG  1 
ATOM   7711  C  CD1 . LEU D 1 145 ? 8.382   -7.032  -34.628 1.00 12.27 ? 145 LEU D CD1 1 
ATOM   7712  C  CD2 . LEU D 1 145 ? 8.935   -5.064  -36.107 1.00 13.41 ? 145 LEU D CD2 1 
ATOM   7713  N  N   . ILE D 1 146 ? 6.528   -6.520  -40.147 1.00 7.44  ? 146 ILE D N   1 
ATOM   7714  C  CA  . ILE D 1 146 ? 6.123   -7.103  -41.369 1.00 8.39  ? 146 ILE D CA  1 
ATOM   7715  C  C   . ILE D 1 146 ? 7.196   -8.002  -41.928 1.00 8.63  ? 146 ILE D C   1 
ATOM   7716  O  O   . ILE D 1 146 ? 8.322   -7.522  -42.191 1.00 8.17  ? 146 ILE D O   1 
ATOM   7717  C  CB  . ILE D 1 146 ? 5.735   -6.099  -42.426 1.00 8.59  ? 146 ILE D CB  1 
ATOM   7718  C  CG1 . ILE D 1 146 ? 4.563   -5.223  -41.931 1.00 9.18  ? 146 ILE D CG1 1 
ATOM   7719  C  CG2 . ILE D 1 146 ? 5.394   -6.758  -43.744 1.00 9.39  ? 146 ILE D CG2 1 
ATOM   7720  C  CD1 . ILE D 1 146 ? 4.346   -3.974  -42.870 1.00 9.52  ? 146 ILE D CD1 1 
ATOM   7721  N  N   A GLU D 1 147 ? 7.021   -9.334  -41.987 0.50 7.46  ? 147 GLU D N   1 
ATOM   7722  N  N   B GLU D 1 147 ? 6.816   -9.274  -42.178 0.50 7.26  ? 147 GLU D N   1 
ATOM   7723  C  CA  A GLU D 1 147 ? 8.068   -10.198 -42.554 0.50 10.22 ? 147 GLU D CA  1 
ATOM   7724  C  CA  B GLU D 1 147 ? 7.711   -10.325 -42.689 0.50 7.81  ? 147 GLU D CA  1 
ATOM   7725  C  C   A GLU D 1 147 ? 7.607   -10.649 -43.943 0.50 8.40  ? 147 GLU D C   1 
ATOM   7726  C  C   B GLU D 1 147 ? 7.472   -10.671 -44.140 0.50 7.02  ? 147 GLU D C   1 
ATOM   7727  O  O   A GLU D 1 147 ? 6.415   -10.703 -44.171 0.50 8.27  ? 147 GLU D O   1 
ATOM   7728  O  O   B GLU D 1 147 ? 6.347   -10.653 -44.638 0.50 6.31  ? 147 GLU D O   1 
ATOM   7729  C  CB  A GLU D 1 147 ? 8.276   -11.397 -41.645 0.50 10.61 ? 147 GLU D CB  1 
ATOM   7730  C  CB  B GLU D 1 147 ? 7.596   -11.582 -41.831 0.50 6.67  ? 147 GLU D CB  1 
ATOM   7731  C  CG  A GLU D 1 147 ? 7.451   -12.528 -41.934 0.50 16.99 ? 147 GLU D CG  1 
ATOM   7732  C  CG  B GLU D 1 147 ? 8.620   -12.658 -42.146 0.50 7.95  ? 147 GLU D CG  1 
ATOM   7733  C  CD  A GLU D 1 147 ? 7.589   -13.584 -40.849 0.50 19.70 ? 147 GLU D CD  1 
ATOM   7734  C  CD  B GLU D 1 147 ? 8.638   -13.736 -41.053 0.50 10.10 ? 147 GLU D CD  1 
ATOM   7735  O  OE1 A GLU D 1 147 ? 8.421   -13.433 -39.875 0.50 17.84 ? 147 GLU D OE1 1 
ATOM   7736  O  OE1 B GLU D 1 147 ? 7.670   -13.829 -40.250 0.50 14.59 ? 147 GLU D OE1 1 
ATOM   7737  O  OE2 A GLU D 1 147 ? 6.842   -14.532 -40.976 0.50 17.91 ? 147 GLU D OE2 1 
ATOM   7738  O  OE2 B GLU D 1 147 ? 9.541   -14.588 -41.088 0.50 18.38 ? 147 GLU D OE2 1 
ATOM   7739  N  N   . MET D 1 148 ? 8.558   -10.943 -44.876 1.00 9.34  ? 148 MET D N   1 
ATOM   7740  C  CA  . MET D 1 148 ? 8.289   -11.468 -46.220 1.00 9.16  ? 148 MET D CA  1 
ATOM   7741  C  C   . MET D 1 148 ? 7.673   -12.874 -46.101 1.00 8.02  ? 148 MET D C   1 
ATOM   7742  O  O   . MET D 1 148 ? 8.304   -13.743 -45.487 1.00 10.65 ? 148 MET D O   1 
ATOM   7743  C  CB  . MET D 1 148 ? 9.618   -11.531 -46.998 1.00 9.02  ? 148 MET D CB  1 
ATOM   7744  C  CG  . MET D 1 148 ? 9.378   -11.881 -48.356 1.00 9.22  ? 148 MET D CG  1 
ATOM   7745  S  SD  . MET D 1 148 ? 10.918  -11.985 -49.424 1.00 12.29 ? 148 MET D SD  1 
ATOM   7746  C  CE  . MET D 1 148 ? 11.387  -10.257 -49.393 1.00 13.71 ? 148 MET D CE  1 
ATOM   7747  N  N   . GLY D 1 149 ? 6.515   -13.047 -46.748 1.00 8.62  ? 149 GLY D N   1 
ATOM   7748  C  CA  . GLY D 1 149 ? 5.787   -14.315 -46.658 1.00 9.09  ? 149 GLY D CA  1 
ATOM   7749  C  C   . GLY D 1 149 ? 4.665   -14.396 -47.676 1.00 9.11  ? 149 GLY D C   1 
ATOM   7750  O  O   . GLY D 1 149 ? 4.844   -14.187 -48.815 1.00 9.49  ? 149 GLY D O   1 
ATOM   7751  N  N   . SER D 1 150 ? 3.466   -14.764 -47.248 1.00 9.96  ? 150 SER D N   1 
ATOM   7752  C  CA  . SER D 1 150 ? 2.288   -14.897 -48.073 1.00 8.93  ? 150 SER D CA  1 
ATOM   7753  C  C   . SER D 1 150 ? 1.716   -13.530 -48.437 1.00 9.22  ? 150 SER D C   1 
ATOM   7754  O  O   . SER D 1 150 ? 1.776   -12.586 -47.644 1.00 10.93 ? 150 SER D O   1 
ATOM   7755  C  CB  . SER D 1 150 ? 1.218   -15.733 -47.328 1.00 9.88  ? 150 SER D CB  1 
ATOM   7756  O  OG  . SER D 1 150 ? 1.611   -17.124 -47.214 1.00 10.97 ? 150 SER D OG  1 
ATOM   7757  N  N   . PHE D 1 151 ? 1.099   -13.548 -49.635 1.00 9.37  ? 151 PHE D N   1 
ATOM   7758  C  CA  . PHE D 1 151 ? 0.277   -12.400 -50.091 1.00 9.92  ? 151 PHE D CA  1 
ATOM   7759  C  C   . PHE D 1 151 ? -0.746  -12.025 -49.043 1.00 10.96 ? 151 PHE D C   1 
ATOM   7760  O  O   . PHE D 1 151 ? -1.350  -12.912 -48.411 1.00 11.75 ? 151 PHE D O   1 
ATOM   7761  C  CB  . PHE D 1 151 ? -0.342  -12.721 -51.416 1.00 10.91 ? 151 PHE D CB  1 
ATOM   7762  C  CG  . PHE D 1 151 ? -1.187  -11.586 -51.926 1.00 9.99  ? 151 PHE D CG  1 
ATOM   7763  C  CD1 . PHE D 1 151 ? -0.569  -10.507 -52.572 1.00 13.01 ? 151 PHE D CD1 1 
ATOM   7764  C  CD2 . PHE D 1 151 ? -2.553  -11.634 -51.794 1.00 13.76 ? 151 PHE D CD2 1 
ATOM   7765  C  CE1 . PHE D 1 151 ? -1.344  -9.396  -53.047 1.00 12.63 ? 151 PHE D CE1 1 
ATOM   7766  C  CE2 . PHE D 1 151 ? -3.296  -10.548 -52.257 1.00 11.43 ? 151 PHE D CE2 1 
ATOM   7767  C  CZ  . PHE D 1 151 ? -2.687  -9.494  -52.880 1.00 10.89 ? 151 PHE D CZ  1 
ATOM   7768  N  N   . ASN D 1 152 ? -0.874  -10.699 -48.820 1.00 8.23  ? 152 ASN D N   1 
ATOM   7769  C  CA  . ASN D 1 152 ? -1.746  -10.228 -47.812 1.00 9.07  ? 152 ASN D CA  1 
ATOM   7770  C  C   . ASN D 1 152 ? -2.804  -9.336  -48.432 1.00 10.35 ? 152 ASN D C   1 
ATOM   7771  O  O   . ASN D 1 152 ? -2.527  -8.147  -48.801 1.00 9.99  ? 152 ASN D O   1 
ATOM   7772  C  CB  . ASN D 1 152 ? -0.971  -9.445  -46.705 1.00 7.96  ? 152 ASN D CB  1 
ATOM   7773  C  CG  . ASN D 1 152 ? -1.777  -9.157  -45.448 1.00 9.48  ? 152 ASN D CG  1 
ATOM   7774  O  OD1 . ASN D 1 152 ? -2.892  -8.614  -45.570 1.00 9.84  ? 152 ASN D OD1 1 
ATOM   7775  N  ND2 . ASN D 1 152 ? -1.220  -9.449  -44.282 1.00 10.94 ? 152 ASN D ND2 1 
ATOM   7776  N  N   . PRO D 1 153 ? -4.058  -9.839  -48.583 1.00 11.24 ? 153 PRO D N   1 
ATOM   7777  C  CA  . PRO D 1 153 ? -5.058  -9.052  -49.252 1.00 10.58 ? 153 PRO D CA  1 
ATOM   7778  C  C   . PRO D 1 153 ? -5.474  -7.797  -48.529 1.00 10.99 ? 153 PRO D C   1 
ATOM   7779  O  O   . PRO D 1 153 ? -5.838  -6.801  -49.183 1.00 12.60 ? 153 PRO D O   1 
ATOM   7780  C  CB  . PRO D 1 153 ? -6.305  -9.983  -49.420 1.00 12.28 ? 153 PRO D CB  1 
ATOM   7781  C  CG  . PRO D 1 153 ? -5.710  -11.426 -49.229 1.00 15.64 ? 153 PRO D CG  1 
ATOM   7782  C  CD  . PRO D 1 153 ? -4.494  -11.237 -48.259 1.00 11.82 ? 153 PRO D CD  1 
ATOM   7783  N  N   . SER D 1 154 ? -5.317  -7.761  -47.220 1.00 9.69  ? 154 SER D N   1 
ATOM   7784  C  CA  . SER D 1 154 ? -5.766  -6.574  -46.453 1.00 10.93 ? 154 SER D CA  1 
ATOM   7785  C  C   . SER D 1 154 ? -4.689  -5.501  -46.719 1.00 11.93 ? 154 SER D C   1 
ATOM   7786  O  O   . SER D 1 154 ? -5.062  -4.337  -46.957 1.00 11.73 ? 154 SER D O   1 
ATOM   7787  C  CB  . SER D 1 154 ? -5.846  -6.885  -45.004 1.00 12.57 ? 154 SER D CB  1 
ATOM   7788  O  OG  . SER D 1 154 ? -6.869  -7.862  -44.783 1.00 15.65 ? 154 SER D OG  1 
ATOM   7789  N  N   . TYR D 1 155 ? -3.353  -5.801  -46.552 1.00 11.10 ? 155 TYR D N   1 
ATOM   7790  C  CA  . TYR D 1 155 ? -2.351  -4.745  -46.868 1.00 9.63  ? 155 TYR D CA  1 
ATOM   7791  C  C   . TYR D 1 155 ? -2.478  -4.345  -48.327 1.00 9.75  ? 155 TYR D C   1 
ATOM   7792  O  O   . TYR D 1 155 ? -2.225  -3.144  -48.677 1.00 10.09 ? 155 TYR D O   1 
ATOM   7793  C  CB  . TYR D 1 155 ? -0.951  -5.203  -46.557 1.00 9.46  ? 155 TYR D CB  1 
ATOM   7794  C  CG  . TYR D 1 155 ? -0.620  -5.076  -45.165 1.00 8.28  ? 155 TYR D CG  1 
ATOM   7795  C  CD1 . TYR D 1 155 ? 0.177   -3.942  -44.721 1.00 10.67 ? 155 TYR D CD1 1 
ATOM   7796  C  CD2 . TYR D 1 155 ? -1.062  -5.993  -44.164 1.00 9.63  ? 155 TYR D CD2 1 
ATOM   7797  C  CE1 . TYR D 1 155 ? 0.482   -3.814  -43.348 1.00 10.42 ? 155 TYR D CE1 1 
ATOM   7798  C  CE2 . TYR D 1 155 ? -0.757  -5.884  -42.836 1.00 10.94 ? 155 TYR D CE2 1 
ATOM   7799  C  CZ  . TYR D 1 155 ? 0.026   -4.770  -42.389 1.00 10.30 ? 155 TYR D CZ  1 
ATOM   7800  O  OH  . TYR D 1 155 ? 0.275   -4.628  -41.074 1.00 11.50 ? 155 TYR D OH  1 
ATOM   7801  N  N   . ASP D 1 156 ? -2.900  -5.208  -49.235 1.00 10.30 ? 156 ASP D N   1 
ATOM   7802  C  CA  . ASP D 1 156 ? -3.081  -4.789  -50.622 1.00 10.03 ? 156 ASP D CA  1 
ATOM   7803  C  C   . ASP D 1 156 ? -4.188  -3.671  -50.838 1.00 9.15  ? 156 ASP D C   1 
ATOM   7804  O  O   . ASP D 1 156 ? -4.179  -2.992  -51.915 1.00 12.77 ? 156 ASP D O   1 
ATOM   7805  C  CB  . ASP D 1 156 ? -3.299  -6.002  -51.553 1.00 12.32 ? 156 ASP D CB  1 
ATOM   7806  C  CG  . ASP D 1 156 ? -2.425  -5.913  -52.782 1.00 14.45 ? 156 ASP D CG  1 
ATOM   7807  O  OD1 . ASP D 1 156 ? -1.198  -5.755  -52.600 1.00 12.25 ? 156 ASP D OD1 1 
ATOM   7808  O  OD2 . ASP D 1 156 ? -2.950  -5.952  -53.915 1.00 15.86 ? 156 ASP D OD2 1 
ATOM   7809  N  N   . LYS D 1 157 ? -5.078  -3.564  -49.814 1.00 9.77  ? 157 LYS D N   1 
ATOM   7810  C  CA  . LYS D 1 157 ? -6.144  -2.554  -49.979 1.00 12.57 ? 157 LYS D CA  1 
ATOM   7811  C  C   . LYS D 1 157 ? -5.464  -1.158  -49.900 1.00 13.09 ? 157 LYS D C   1 
ATOM   7812  O  O   . LYS D 1 157 ? -5.960  -0.196  -50.554 1.00 15.62 ? 157 LYS D O   1 
ATOM   7813  C  CB  . LYS D 1 157 ? -7.176  -2.740  -48.890 1.00 12.02 ? 157 LYS D CB  1 
ATOM   7814  C  CG  . LYS D 1 157 ? -8.010  -3.978  -49.121 1.00 14.97 ? 157 LYS D CG  1 
ATOM   7815  C  CD  . LYS D 1 157 ? -8.947  -4.249  -47.872 1.00 19.55 ? 157 LYS D CD  1 
ATOM   7816  C  CE  . LYS D 1 157 ? -9.635  -5.636  -48.060 1.00 20.19 ? 157 LYS D CE  1 
ATOM   7817  N  NZ  . LYS D 1 157 ? -10.358 -6.094  -46.793 1.00 20.38 ? 157 LYS D NZ  1 
ATOM   7818  N  N   . ILE D 1 158 ? -4.244  -1.120  -49.367 1.00 12.05 ? 158 ILE D N   1 
ATOM   7819  C  CA  . ILE D 1 158 ? -3.428  0.127   -49.379 1.00 11.66 ? 158 ILE D CA  1 
ATOM   7820  C  C   . ILE D 1 158 ? -2.513  0.096   -50.589 1.00 10.46 ? 158 ILE D C   1 
ATOM   7821  O  O   . ILE D 1 158 ? -2.429  1.017   -51.417 1.00 10.92 ? 158 ILE D O   1 
ATOM   7822  C  CB  . ILE D 1 158 ? -2.608  0.255   -48.111 1.00 13.69 ? 158 ILE D CB  1 
ATOM   7823  C  CG1 . ILE D 1 158 ? -3.568  0.528   -46.904 1.00 16.11 ? 158 ILE D CG1 1 
ATOM   7824  C  CG2 . ILE D 1 158 ? -1.555  1.487   -48.208 1.00 11.37 ? 158 ILE D CG2 1 
ATOM   7825  C  CD1 . ILE D 1 158 ? -2.950  0.366   -45.537 1.00 19.99 ? 158 ILE D CD1 1 
ATOM   7826  N  N   . PHE D 1 159 ? -1.843  -1.076  -50.797 1.00 10.85 ? 159 PHE D N   1 
ATOM   7827  C  CA  . PHE D 1 159 ? -0.794  -1.071  -51.768 1.00 10.63 ? 159 PHE D CA  1 
ATOM   7828  C  C   . PHE D 1 159 ? -1.305  -0.933  -53.228 1.00 11.64 ? 159 PHE D C   1 
ATOM   7829  O  O   . PHE D 1 159 ? -0.578  -0.490  -54.120 1.00 12.52 ? 159 PHE D O   1 
ATOM   7830  C  CB  . PHE D 1 159 ? 0.098   -2.371  -51.693 1.00 11.48 ? 159 PHE D CB  1 
ATOM   7831  C  CG  . PHE D 1 159 ? 0.849   -2.579  -50.356 1.00 9.66  ? 159 PHE D CG  1 
ATOM   7832  C  CD1 . PHE D 1 159 ? 1.220   -1.522  -49.550 1.00 12.52 ? 159 PHE D CD1 1 
ATOM   7833  C  CD2 . PHE D 1 159 ? 1.158   -3.916  -49.932 1.00 9.93  ? 159 PHE D CD2 1 
ATOM   7834  C  CE1 . PHE D 1 159 ? 1.913   -1.730  -48.363 1.00 12.98 ? 159 PHE D CE1 1 
ATOM   7835  C  CE2 . PHE D 1 159 ? 1.837   -4.108  -48.737 1.00 11.25 ? 159 PHE D CE2 1 
ATOM   7836  C  CZ  . PHE D 1 159 ? 2.238   -3.018  -47.943 1.00 13.19 ? 159 PHE D CZ  1 
ATOM   7837  N  N   . SER D 1 160 ? -2.543  -1.321  -53.509 1.00 11.94 ? 160 SER D N   1 
ATOM   7838  C  CA  . SER D 1 160 ? -2.997  -1.176  -54.873 1.00 11.15 ? 160 SER D CA  1 
ATOM   7839  C  C   . SER D 1 160 ? -3.129  0.232   -55.353 1.00 12.33 ? 160 SER D C   1 
ATOM   7840  O  O   . SER D 1 160 ? -3.191  0.505   -56.560 1.00 14.55 ? 160 SER D O   1 
ATOM   7841  C  CB  . SER D 1 160 ? -4.402  -1.842  -54.974 1.00 14.13 ? 160 SER D CB  1 
ATOM   7842  O  OG  . SER D 1 160 ? -5.375  -1.209  -54.148 1.00 13.58 ? 160 SER D OG  1 
ATOM   7843  N  N   . HIS D 1 161 ? -3.038  1.144   -54.383 1.00 11.34 ? 161 HIS D N   1 
ATOM   7844  C  CA  . HIS D 1 161 ? -3.156  2.598   -54.667 1.00 12.28 ? 161 HIS D CA  1 
ATOM   7845  C  C   . HIS D 1 161 ? -1.816  3.281   -54.850 1.00 12.96 ? 161 HIS D C   1 
ATOM   7846  O  O   . HIS D 1 161 ? -1.799  4.494   -55.167 1.00 13.55 ? 161 HIS D O   1 
ATOM   7847  C  CB  . HIS D 1 161 ? -3.970  3.344   -53.562 1.00 12.10 ? 161 HIS D CB  1 
ATOM   7848  C  CG  . HIS D 1 161 ? -5.370  2.934   -53.531 1.00 15.62 ? 161 HIS D CG  1 
ATOM   7849  N  ND1 . HIS D 1 161 ? -6.347  3.558   -54.286 1.00 16.64 ? 161 HIS D ND1 1 
ATOM   7850  C  CD2 . HIS D 1 161 ? -5.969  1.926   -52.856 1.00 14.76 ? 161 HIS D CD2 1 
ATOM   7851  C  CE1 . HIS D 1 161 ? -7.511  2.966   -54.041 1.00 17.25 ? 161 HIS D CE1 1 
ATOM   7852  N  NE2 . HIS D 1 161 ? -7.320  1.952   -53.195 1.00 16.13 ? 161 HIS D NE2 1 
ATOM   7853  N  N   . LEU D 1 162 ? -0.704  2.567   -54.671 1.00 12.91 ? 162 LEU D N   1 
ATOM   7854  C  CA  . LEU D 1 162 ? 0.617   3.233   -54.631 1.00 15.64 ? 162 LEU D CA  1 
ATOM   7855  C  C   . LEU D 1 162 ? 0.929   3.965   -55.925 1.00 16.07 ? 162 LEU D C   1 
ATOM   7856  O  O   . LEU D 1 162 ? 1.642   5.008   -55.897 1.00 17.30 ? 162 LEU D O   1 
ATOM   7857  C  CB  . LEU D 1 162 ? 1.697   2.205   -54.346 1.00 15.90 ? 162 LEU D CB  1 
ATOM   7858  C  CG  . LEU D 1 162 ? 1.748   1.523   -52.996 1.00 16.43 ? 162 LEU D CG  1 
ATOM   7859  C  CD1 . LEU D 1 162 ? 2.739   0.293   -52.977 1.00 19.15 ? 162 LEU D CD1 1 
ATOM   7860  C  CD2 . LEU D 1 162 ? 2.058   2.537   -51.824 1.00 21.96 ? 162 LEU D CD2 1 
ATOM   7861  N  N   . GLN D 1 163 ? 0.530   3.433   -57.063 1.00 17.36 ? 163 GLN D N   1 
ATOM   7862  C  CA  . GLN D 1 163 ? 0.790   4.152   -58.372 1.00 20.22 ? 163 GLN D CA  1 
ATOM   7863  C  C   . GLN D 1 163 ? 0.184   5.560   -58.484 1.00 20.62 ? 163 GLN D C   1 
ATOM   7864  O  O   . GLN D 1 163 ? 0.704   6.458   -59.163 1.00 25.74 ? 163 GLN D O   1 
ATOM   7865  C  CB  . GLN D 1 163 ? 0.644   3.250   -59.608 1.00 22.55 ? 163 GLN D CB  1 
ATOM   7866  C  CG  . GLN D 1 163 ? 1.625   1.995   -59.546 1.00 29.30 ? 163 GLN D CG  1 
ATOM   7867  C  CD  . GLN D 1 163 ? 3.184   2.302   -59.496 1.00 33.73 ? 163 GLN D CD  1 
ATOM   7868  O  OE1 . GLN D 1 163 ? 3.664   3.339   -60.008 1.00 42.71 ? 163 GLN D OE1 1 
ATOM   7869  N  NE2 . GLN D 1 163 ? 3.947   1.394   -58.896 1.00 27.70 ? 163 GLN D NE2 1 
ATOM   7870  N  N   . HIS D 1 164 ? -0.818  5.825   -57.711 1.00 16.48 ? 164 HIS D N   1 
ATOM   7871  C  CA  . HIS D 1 164 ? -1.459  7.129   -57.749 1.00 16.07 ? 164 HIS D CA  1 
ATOM   7872  C  C   . HIS D 1 164 ? -0.863  8.126   -56.820 1.00 17.13 ? 164 HIS D C   1 
ATOM   7873  O  O   . HIS D 1 164 ? -1.339  9.290   -56.730 1.00 17.50 ? 164 HIS D O   1 
ATOM   7874  C  CB  . HIS D 1 164 ? -2.958  6.936   -57.489 1.00 17.52 ? 164 HIS D CB  1 
ATOM   7875  C  CG  . HIS D 1 164 ? -3.606  5.937   -58.431 1.00 20.18 ? 164 HIS D CG  1 
ATOM   7876  N  ND1 . HIS D 1 164 ? -3.811  6.192   -59.761 1.00 25.45 ? 164 HIS D ND1 1 
ATOM   7877  C  CD2 . HIS D 1 164 ? -4.027  4.659   -58.233 1.00 27.00 ? 164 HIS D CD2 1 
ATOM   7878  C  CE1 . HIS D 1 164 ? -4.374  5.147   -60.353 1.00 27.37 ? 164 HIS D CE1 1 
ATOM   7879  N  NE2 . HIS D 1 164 ? -4.489  4.185   -59.455 1.00 29.74 ? 164 HIS D NE2 1 
ATOM   7880  N  N   . VAL D 1 165 ? 0.137   7.695   -56.010 1.00 14.26 ? 165 VAL D N   1 
ATOM   7881  C  CA  . VAL D 1 165 ? 0.780   8.591   -55.108 1.00 14.06 ? 165 VAL D CA  1 
ATOM   7882  C  C   . VAL D 1 165 ? 2.345   8.509   -55.283 1.00 12.15 ? 165 VAL D C   1 
ATOM   7883  O  O   . VAL D 1 165 ? 3.087   8.690   -54.257 1.00 12.67 ? 165 VAL D O   1 
ATOM   7884  C  CB  . VAL D 1 165 ? 0.370   8.379   -53.643 1.00 15.33 ? 165 VAL D CB  1 
ATOM   7885  C  CG1 . VAL D 1 165 ? -1.143  8.767   -53.400 1.00 16.21 ? 165 VAL D CG1 1 
ATOM   7886  C  CG2 . VAL D 1 165 ? 0.636   6.942   -53.127 1.00 15.50 ? 165 VAL D CG2 1 
ATOM   7887  N  N   A LYS D 1 166 ? 2.832   8.313   -56.489 0.50 12.87 ? 166 LYS D N   1 
ATOM   7888  N  N   B LYS D 1 166 ? 2.753   8.438   -56.517 0.50 12.78 ? 166 LYS D N   1 
ATOM   7889  C  CA  A LYS D 1 166 ? 4.246   8.071   -56.617 0.50 13.63 ? 166 LYS D CA  1 
ATOM   7890  C  CA  B LYS D 1 166 ? 4.093   8.169   -56.879 0.50 12.88 ? 166 LYS D CA  1 
ATOM   7891  C  C   A LYS D 1 166 ? 5.067   9.289   -56.094 0.50 11.30 ? 166 LYS D C   1 
ATOM   7892  C  C   B LYS D 1 166 ? 5.105   9.243   -56.393 0.50 12.86 ? 166 LYS D C   1 
ATOM   7893  O  O   A LYS D 1 166 ? 6.081   9.107   -55.501 0.50 8.64  ? 166 LYS D O   1 
ATOM   7894  O  O   B LYS D 1 166 ? 6.293   8.892   -56.122 0.50 11.69 ? 166 LYS D O   1 
ATOM   7895  C  CB  A LYS D 1 166 ? 4.620   7.667   -58.064 0.50 13.31 ? 166 LYS D CB  1 
ATOM   7896  C  CB  B LYS D 1 166 ? 4.153   8.095   -58.401 0.50 12.58 ? 166 LYS D CB  1 
ATOM   7897  C  CG  A LYS D 1 166 ? 3.888   6.411   -58.579 0.50 13.07 ? 166 LYS D CG  1 
ATOM   7898  C  CG  B LYS D 1 166 ? 5.548   7.747   -58.802 0.50 11.08 ? 166 LYS D CG  1 
ATOM   7899  C  CD  A LYS D 1 166 ? 4.432   5.818   -59.905 0.50 19.14 ? 166 LYS D CD  1 
ATOM   7900  C  CD  B LYS D 1 166 ? 5.751   7.473   -60.305 0.50 16.13 ? 166 LYS D CD  1 
ATOM   7901  C  CE  A LYS D 1 166 ? 6.042   5.471   -59.826 0.50 21.36 ? 166 LYS D CE  1 
ATOM   7902  C  CE  B LYS D 1 166 ? 5.243   6.141   -60.824 0.50 22.76 ? 166 LYS D CE  1 
ATOM   7903  N  NZ  A LYS D 1 166 ? 6.658   4.031   -59.836 0.50 19.67 ? 166 LYS D NZ  1 
ATOM   7904  N  NZ  B LYS D 1 166 ? 5.853   4.926   -60.164 0.50 23.52 ? 166 LYS D NZ  1 
ATOM   7905  N  N   . TYR D 1 167 ? 4.667   10.517  -56.391 1.00 14.56 ? 167 TYR D N   1 
ATOM   7906  C  CA  . TYR D 1 167 ? 5.497   11.710  -56.024 1.00 12.76 ? 167 TYR D CA  1 
ATOM   7907  C  C   . TYR D 1 167 ? 5.008   12.530  -54.867 1.00 13.98 ? 167 TYR D C   1 
ATOM   7908  O  O   . TYR D 1 167 ? 3.848   12.534  -54.525 1.00 12.57 ? 167 TYR D O   1 
ATOM   7909  C  CB  . TYR D 1 167 ? 5.536   12.632  -57.277 1.00 15.21 ? 167 TYR D CB  1 
ATOM   7910  C  CG  . TYR D 1 167 ? 6.196   11.934  -58.403 1.00 15.11 ? 167 TYR D CG  1 
ATOM   7911  C  CD1 . TYR D 1 167 ? 7.596   11.791  -58.385 1.00 18.84 ? 167 TYR D CD1 1 
ATOM   7912  C  CD2 . TYR D 1 167 ? 5.485   11.535  -59.502 1.00 20.09 ? 167 TYR D CD2 1 
ATOM   7913  C  CE1 . TYR D 1 167 ? 8.264   11.177  -59.414 1.00 17.21 ? 167 TYR D CE1 1 
ATOM   7914  C  CE2 . TYR D 1 167 ? 6.103   10.924  -60.566 1.00 20.76 ? 167 TYR D CE2 1 
ATOM   7915  C  CZ  . TYR D 1 167 ? 7.511   10.718  -60.501 1.00 20.25 ? 167 TYR D CZ  1 
ATOM   7916  O  OH  . TYR D 1 167 ? 8.079   10.129  -61.615 1.00 24.34 ? 167 TYR D OH  1 
ATOM   7917  N  N   . LYS D 1 168 ? 5.943   13.238  -54.232 1.00 13.50 ? 168 LYS D N   1 
ATOM   7918  C  CA  . LYS D 1 168 ? 5.627   14.039  -53.093 1.00 14.63 ? 168 LYS D CA  1 
ATOM   7919  C  C   . LYS D 1 168 ? 4.466   14.907  -53.420 1.00 14.29 ? 168 LYS D C   1 
ATOM   7920  O  O   . LYS D 1 168 ? 4.445   15.554  -54.533 1.00 16.31 ? 168 LYS D O   1 
ATOM   7921  C  CB  . LYS D 1 168 ? 6.788   14.942  -52.704 1.00 15.02 ? 168 LYS D CB  1 
ATOM   7922  C  CG  . LYS D 1 168 ? 6.471   15.768  -51.503 1.00 17.79 ? 168 LYS D CG  1 
ATOM   7923  C  CD  . LYS D 1 168 ? 7.735   16.333  -50.879 1.00 17.68 ? 168 LYS D CD  1 
ATOM   7924  C  CE  . LYS D 1 168 ? 7.364   17.334  -49.856 1.00 24.01 ? 168 LYS D CE  1 
ATOM   7925  N  NZ  . LYS D 1 168 ? 8.512   17.925  -49.046 1.00 27.43 ? 168 LYS D NZ  1 
ATOM   7926  N  N   . GLY D 1 169 ? 3.528   14.953  -52.497 1.00 13.05 ? 169 GLY D N   1 
ATOM   7927  C  CA  . GLY D 1 169 ? 2.340   15.827  -52.660 1.00 14.82 ? 169 GLY D CA  1 
ATOM   7928  C  C   . GLY D 1 169 ? 1.104   15.256  -53.412 1.00 18.36 ? 169 GLY D C   1 
ATOM   7929  O  O   . GLY D 1 169 ? -0.020  15.789  -53.401 1.00 19.68 ? 169 GLY D O   1 
ATOM   7930  N  N   . GLN D 1 170 ? 1.288   14.108  -54.010 1.00 15.42 ? 170 GLN D N   1 
ATOM   7931  C  CA  . GLN D 1 170 ? 0.190   13.399  -54.682 1.00 13.23 ? 170 GLN D CA  1 
ATOM   7932  C  C   . GLN D 1 170 ? -0.692  12.669  -53.627 1.00 15.86 ? 170 GLN D C   1 
ATOM   7933  O  O   . GLN D 1 170 ? -0.183  12.277  -52.554 1.00 15.51 ? 170 GLN D O   1 
ATOM   7934  C  CB  . GLN D 1 170 ? 0.706   12.477  -55.730 1.00 11.31 ? 170 GLN D CB  1 
ATOM   7935  C  CG  . GLN D 1 170 ? 1.439   13.233  -56.904 1.00 12.34 ? 170 GLN D CG  1 
ATOM   7936  C  CD  . GLN D 1 170 ? 1.773   12.327  -58.036 1.00 16.83 ? 170 GLN D CD  1 
ATOM   7937  O  OE1 . GLN D 1 170 ? 2.049   11.179  -57.840 1.00 15.87 ? 170 GLN D OE1 1 
ATOM   7938  N  NE2 . GLN D 1 170 ? 1.721   12.858  -59.298 1.00 20.32 ? 170 GLN D NE2 1 
ATOM   7939  N  N   . GLU D 1 171 ? -1.999  12.544  -53.958 1.00 14.35 ? 171 GLU D N   1 
ATOM   7940  C  CA  . GLU D 1 171 ? -3.012  12.126  -52.990 1.00 15.88 ? 171 GLU D CA  1 
ATOM   7941  C  C   . GLU D 1 171 ? -3.959  11.205  -53.780 1.00 15.90 ? 171 GLU D C   1 
ATOM   7942  O  O   . GLU D 1 171 ? -4.104  11.329  -55.016 1.00 17.66 ? 171 GLU D O   1 
ATOM   7943  C  CB  . GLU D 1 171 ? -3.800  13.302  -52.446 1.00 18.15 ? 171 GLU D CB  1 
ATOM   7944  C  CG  . GLU D 1 171 ? -3.145  14.383  -51.696 1.00 23.55 ? 171 GLU D CG  1 
ATOM   7945  C  CD  . GLU D 1 171 ? -4.237  15.457  -51.414 1.00 28.27 ? 171 GLU D CD  1 
ATOM   7946  O  OE1 . GLU D 1 171 ? -5.239  15.532  -52.182 1.00 35.43 ? 171 GLU D OE1 1 
ATOM   7947  O  OE2 . GLU D 1 171 ? -4.147  16.085  -50.367 1.00 35.08 ? 171 GLU D OE2 1 
ATOM   7948  N  N   . ALA D 1 172 ? -4.521  10.241  -53.122 1.00 15.78 ? 172 ALA D N   1 
ATOM   7949  C  CA  . ALA D 1 172 ? -5.449  9.274   -53.727 1.00 16.63 ? 172 ALA D CA  1 
ATOM   7950  C  C   . ALA D 1 172 ? -6.428  8.884   -52.625 1.00 15.31 ? 172 ALA D C   1 
ATOM   7951  O  O   . ALA D 1 172 ? -6.143  9.047   -51.453 1.00 16.93 ? 172 ALA D O   1 
ATOM   7952  C  CB  . ALA D 1 172 ? -4.739  8.039   -54.269 1.00 17.51 ? 172 ALA D CB  1 
ATOM   7953  N  N   . PHE D 1 173 ? -7.627  8.460   -53.000 1.00 15.67 ? 173 PHE D N   1 
ATOM   7954  C  CA  . PHE D 1 173 ? -8.658  8.089   -51.997 1.00 14.48 ? 173 PHE D CA  1 
ATOM   7955  C  C   . PHE D 1 173 ? -8.730  6.642   -51.981 1.00 15.87 ? 173 PHE D C   1 
ATOM   7956  O  O   . PHE D 1 173 ? -8.747  6.033   -53.050 1.00 17.61 ? 173 PHE D O   1 
ATOM   7957  C  CB  . PHE D 1 173 ? -10.028 8.670   -52.361 1.00 16.40 ? 173 PHE D CB  1 
ATOM   7958  C  CG  . PHE D 1 173 ? -10.224 10.056  -51.860 1.00 16.91 ? 173 PHE D CG  1 
ATOM   7959  C  CD1 . PHE D 1 173 ? -10.340 10.327  -50.458 1.00 24.56 ? 173 PHE D CD1 1 
ATOM   7960  C  CD2 . PHE D 1 173 ? -10.182 11.135  -52.720 1.00 29.84 ? 173 PHE D CD2 1 
ATOM   7961  C  CE1 . PHE D 1 173 ? -10.501 11.624  -49.957 1.00 28.74 ? 173 PHE D CE1 1 
ATOM   7962  C  CE2 . PHE D 1 173 ? -10.341 12.476  -52.222 1.00 30.20 ? 173 PHE D CE2 1 
ATOM   7963  C  CZ  . PHE D 1 173 ? -10.516 12.716  -50.850 1.00 29.62 ? 173 PHE D CZ  1 
ATOM   7964  N  N   . VAL D 1 174 ? -8.765  6.135   -50.770 1.00 13.55 ? 174 VAL D N   1 
ATOM   7965  C  CA  . VAL D 1 174 ? -8.775  4.726   -50.478 1.00 13.58 ? 174 VAL D CA  1 
ATOM   7966  C  C   . VAL D 1 174 ? -10.156 4.455   -49.797 1.00 14.14 ? 174 VAL D C   1 
ATOM   7967  O  O   . VAL D 1 174 ? -10.485 5.025   -48.756 1.00 14.84 ? 174 VAL D O   1 
ATOM   7968  C  CB  . VAL D 1 174 ? -7.650  4.291   -49.467 1.00 14.10 ? 174 VAL D CB  1 
ATOM   7969  C  CG1 . VAL D 1 174 ? -7.762  2.809   -49.084 1.00 13.12 ? 174 VAL D CG1 1 
ATOM   7970  C  CG2 . VAL D 1 174 ? -6.262  4.589   -50.150 1.00 13.53 ? 174 VAL D CG2 1 
ATOM   7971  N  N   . PRO D 1 175 ? -10.960 3.521   -50.354 1.00 13.25 ? 175 PRO D N   1 
ATOM   7972  C  CA  . PRO D 1 175 ? -12.205 3.136   -49.642 1.00 12.78 ? 175 PRO D CA  1 
ATOM   7973  C  C   . PRO D 1 175 ? -11.912 2.559   -48.283 1.00 14.08 ? 175 PRO D C   1 
ATOM   7974  O  O   . PRO D 1 175 ? -10.940 1.855   -48.081 1.00 14.00 ? 175 PRO D O   1 
ATOM   7975  C  CB  . PRO D 1 175 ? -12.769 2.005   -50.523 1.00 15.15 ? 175 PRO D CB  1 
ATOM   7976  C  CG  . PRO D 1 175 ? -12.275 2.322   -51.913 1.00 16.44 ? 175 PRO D CG  1 
ATOM   7977  C  CD  . PRO D 1 175 ? -10.801 2.733   -51.572 1.00 12.51 ? 175 PRO D CD  1 
ATOM   7978  N  N   . GLY D 1 176 ? -12.817 2.756   -47.329 1.00 12.94 ? 176 GLY D N   1 
ATOM   7979  C  CA  . GLY D 1 176 ? -12.570 2.206   -45.975 1.00 11.92 ? 176 GLY D CA  1 
ATOM   7980  C  C   . GLY D 1 176 ? -12.540 0.693   -45.946 1.00 11.87 ? 176 GLY D C   1 
ATOM   7981  O  O   . GLY D 1 176 ? -13.223 0.002   -46.778 1.00 15.46 ? 176 GLY D O   1 
ATOM   7982  N  N   . PHE D 1 177 ? -11.822 0.213   -44.993 1.00 11.57 ? 177 PHE D N   1 
ATOM   7983  C  CA  . PHE D 1 177 ? -11.754 -1.255  -44.746 1.00 10.77 ? 177 PHE D CA  1 
ATOM   7984  C  C   . PHE D 1 177 ? -11.456 -1.404  -43.285 1.00 11.59 ? 177 PHE D C   1 
ATOM   7985  O  O   . PHE D 1 177 ? -11.242 -0.428  -42.507 1.00 13.10 ? 177 PHE D O   1 
ATOM   7986  C  CB  . PHE D 1 177 ? -10.751 -2.017  -45.657 1.00 13.26 ? 177 PHE D CB  1 
ATOM   7987  C  CG  . PHE D 1 177 ? -9.286  -1.646  -45.462 1.00 11.03 ? 177 PHE D CG  1 
ATOM   7988  C  CD1 . PHE D 1 177 ? -8.509  -2.463  -44.625 1.00 15.49 ? 177 PHE D CD1 1 
ATOM   7989  C  CD2 . PHE D 1 177 ? -8.750  -0.541  -46.067 1.00 15.21 ? 177 PHE D CD2 1 
ATOM   7990  C  CE1 . PHE D 1 177 ? -7.145  -2.168  -44.442 1.00 11.67 ? 177 PHE D CE1 1 
ATOM   7991  C  CE2 . PHE D 1 177 ? -7.412  -0.206  -45.832 1.00 16.38 ? 177 PHE D CE2 1 
ATOM   7992  C  CZ  . PHE D 1 177 ? -6.665  -0.990  -45.049 1.00 12.68 ? 177 PHE D CZ  1 
ATOM   7993  N  N   . ASN D 1 178 ? -11.527 -2.651  -42.840 1.00 14.43 ? 178 ASN D N   1 
ATOM   7994  C  CA  . ASN D 1 178 ? -11.338 -2.871  -41.451 1.00 13.43 ? 178 ASN D CA  1 
ATOM   7995  C  C   . ASN D 1 178 ? -9.812  -2.847  -41.158 1.00 11.96 ? 178 ASN D C   1 
ATOM   7996  O  O   . ASN D 1 178 ? -9.114  -3.832  -41.467 1.00 12.38 ? 178 ASN D O   1 
ATOM   7997  C  CB  . ASN D 1 178 ? -11.931 -4.234  -41.046 1.00 14.66 ? 178 ASN D CB  1 
ATOM   7998  C  CG  . ASN D 1 178 ? -11.744 -4.501  -39.655 1.00 12.58 ? 178 ASN D CG  1 
ATOM   7999  O  OD1 . ASN D 1 178 ? -11.351 -3.673  -38.768 1.00 14.95 ? 178 ASN D OD1 1 
ATOM   8000  N  ND2 . ASN D 1 178 ? -12.059 -5.790  -39.335 1.00 23.69 ? 178 ASN D ND2 1 
ATOM   8001  N  N   . ILE D 1 179 ? -9.344  -1.793  -40.545 1.00 12.49 ? 179 ILE D N   1 
ATOM   8002  C  CA  . ILE D 1 179 ? -7.903  -1.661  -40.196 1.00 11.76 ? 179 ILE D CA  1 
ATOM   8003  C  C   . ILE D 1 179 ? -7.394  -2.717  -39.251 1.00 13.48 ? 179 ILE D C   1 
ATOM   8004  O  O   . ILE D 1 179 ? -6.160  -2.993  -39.157 1.00 12.24 ? 179 ILE D O   1 
ATOM   8005  C  CB  . ILE D 1 179 ? -7.711  -0.208  -39.671 1.00 10.03 ? 179 ILE D CB  1 
ATOM   8006  C  CG1 . ILE D 1 179 ? -8.244  0.872   -40.641 1.00 11.05 ? 179 ILE D CG1 1 
ATOM   8007  C  CG2 . ILE D 1 179 ? -6.202  0.061   -39.232 1.00 10.66 ? 179 ILE D CG2 1 
ATOM   8008  C  CD1 . ILE D 1 179 ? -7.537  0.845   -42.005 1.00 15.90 ? 179 ILE D CD1 1 
ATOM   8009  N  N   A GLU D 1 180 ? -8.252  -3.339  -38.424 0.50 12.83 ? 180 GLU D N   1 
ATOM   8010  N  N   B GLU D 1 180 ? -8.331  -3.388  -38.552 0.50 13.39 ? 180 GLU D N   1 
ATOM   8011  C  CA  A GLU D 1 180 ? -7.742  -4.437  -37.556 0.50 10.49 ? 180 GLU D CA  1 
ATOM   8012  C  CA  B GLU D 1 180 ? -7.937  -4.459  -37.622 0.50 11.90 ? 180 GLU D CA  1 
ATOM   8013  C  C   A GLU D 1 180 ? -7.273  -5.653  -38.415 0.50 9.93  ? 180 GLU D C   1 
ATOM   8014  C  C   B GLU D 1 180 ? -7.288  -5.579  -38.398 0.50 11.09 ? 180 GLU D C   1 
ATOM   8015  O  O   A GLU D 1 180 ? -6.555  -6.505  -37.908 0.50 12.94 ? 180 GLU D O   1 
ATOM   8016  O  O   B GLU D 1 180 ? -6.437  -6.254  -37.799 0.50 12.14 ? 180 GLU D O   1 
ATOM   8017  C  CB  A GLU D 1 180 ? -8.773  -4.844  -36.481 0.50 11.45 ? 180 GLU D CB  1 
ATOM   8018  C  CB  B GLU D 1 180 ? -9.124  -5.011  -36.792 0.50 14.03 ? 180 GLU D CB  1 
ATOM   8019  C  CG  A GLU D 1 180 ? -8.295  -5.805  -35.454 0.50 12.91 ? 180 GLU D CG  1 
ATOM   8020  C  CG  B GLU D 1 180 ? -9.463  -4.160  -35.601 0.50 12.30 ? 180 GLU D CG  1 
ATOM   8021  C  CD  A GLU D 1 180 ? -9.381  -6.053  -34.422 0.50 14.79 ? 180 GLU D CD  1 
ATOM   8022  C  CD  B GLU D 1 180 ? -10.112 -4.883  -34.322 0.50 13.21 ? 180 GLU D CD  1 
ATOM   8023  O  OE1 A GLU D 1 180 ? -10.515 -5.537  -34.593 0.50 14.97 ? 180 GLU D OE1 1 
ATOM   8024  O  OE1 B GLU D 1 180 ? -9.554  -5.831  -33.707 0.50 15.51 ? 180 GLU D OE1 1 
ATOM   8025  O  OE2 A GLU D 1 180 ? -9.065  -6.725  -33.433 0.50 17.28 ? 180 GLU D OE2 1 
ATOM   8026  O  OE2 B GLU D 1 180 ? -11.158 -4.438  -33.929 0.50 22.97 ? 180 GLU D OE2 1 
ATOM   8027  N  N   . GLU D 1 181 ? -7.683  -5.687  -39.685 1.00 11.95 ? 181 GLU D N   1 
ATOM   8028  C  CA  . GLU D 1 181 ? -7.110  -6.718  -40.582 1.00 11.40 ? 181 GLU D CA  1 
ATOM   8029  C  C   . GLU D 1 181 ? -5.589  -6.555  -40.791 1.00 12.27 ? 181 GLU D C   1 
ATOM   8030  O  O   . GLU D 1 181 ? -4.941  -7.489  -41.248 1.00 12.73 ? 181 GLU D O   1 
ATOM   8031  C  CB  . GLU D 1 181 ? -7.734  -6.694  -41.931 1.00 13.67 ? 181 GLU D CB  1 
ATOM   8032  C  CG  . GLU D 1 181 ? -9.220  -7.186  -41.986 1.00 15.26 ? 181 GLU D CG  1 
ATOM   8033  C  CD  . GLU D 1 181 ? -9.868  -6.944  -43.339 1.00 19.79 ? 181 GLU D CD  1 
ATOM   8034  O  OE1 . GLU D 1 181 ? -9.150  -6.703  -44.380 1.00 22.44 ? 181 GLU D OE1 1 
ATOM   8035  O  OE2 . GLU D 1 181 ? -11.162 -6.984  -43.379 1.00 20.08 ? 181 GLU D OE2 1 
ATOM   8036  N  N   . LEU D 1 182 ? -5.046  -5.387  -40.469 1.00 10.16 ? 182 LEU D N   1 
ATOM   8037  C  CA  . LEU D 1 182 ? -3.589  -5.155  -40.562 1.00 9.13  ? 182 LEU D CA  1 
ATOM   8038  C  C   . LEU D 1 182 ? -2.808  -5.612  -39.368 1.00 9.97  ? 182 LEU D C   1 
ATOM   8039  O  O   . LEU D 1 182 ? -1.603  -5.627  -39.405 1.00 10.25 ? 182 LEU D O   1 
ATOM   8040  C  CB  . LEU D 1 182 ? -3.349  -3.641  -40.796 1.00 8.73  ? 182 LEU D CB  1 
ATOM   8041  C  CG  . LEU D 1 182 ? -3.990  -2.975  -42.010 1.00 8.84  ? 182 LEU D CG  1 
ATOM   8042  C  CD1 . LEU D 1 182 ? -3.621  -1.493  -42.033 1.00 9.89  ? 182 LEU D CD1 1 
ATOM   8043  C  CD2 . LEU D 1 182 ? -3.752  -3.703  -43.345 1.00 10.13 ? 182 LEU D CD2 1 
ATOM   8044  N  N   . LEU D 1 183 ? -3.474  -5.924  -38.235 1.00 10.70 ? 183 LEU D N   1 
ATOM   8045  C  CA  . LEU D 1 183 ? -2.859  -6.339  -37.035 1.00 9.87  ? 183 LEU D CA  1 
ATOM   8046  C  C   . LEU D 1 183 ? -2.616  -7.837  -37.029 1.00 9.31  ? 183 LEU D C   1 
ATOM   8047  O  O   . LEU D 1 183 ? -3.288  -8.590  -37.745 1.00 11.62 ? 183 LEU D O   1 
ATOM   8048  C  CB  . LEU D 1 183 ? -3.825  -6.010  -35.902 1.00 12.15 ? 183 LEU D CB  1 
ATOM   8049  C  CG  . LEU D 1 183 ? -4.083  -4.479  -35.706 1.00 11.63 ? 183 LEU D CG  1 
ATOM   8050  C  CD1 . LEU D 1 183 ? -4.726  -4.297  -34.315 1.00 17.37 ? 183 LEU D CD1 1 
ATOM   8051  C  CD2 . LEU D 1 183 ? -2.900  -3.600  -35.728 1.00 15.21 ? 183 LEU D CD2 1 
ATOM   8052  N  N   . PRO D 1 184 ? -1.594  -8.214  -36.286 1.00 10.09 ? 184 PRO D N   1 
ATOM   8053  C  CA  . PRO D 1 184 ? -1.232  -9.680  -36.218 1.00 11.71 ? 184 PRO D CA  1 
ATOM   8054  C  C   . PRO D 1 184 ? -2.068  -10.493 -35.259 1.00 14.64 ? 184 PRO D C   1 
ATOM   8055  O  O   . PRO D 1 184 ? -3.013  -9.993  -34.631 1.00 15.90 ? 184 PRO D O   1 
ATOM   8056  C  CB  . PRO D 1 184 ? 0.220   -9.629  -35.620 1.00 12.01 ? 184 PRO D CB  1 
ATOM   8057  C  CG  . PRO D 1 184 ? 0.167   -8.405  -34.753 1.00 13.70 ? 184 PRO D CG  1 
ATOM   8058  C  CD  . PRO D 1 184 ? -0.694  -7.388  -35.467 1.00 11.36 ? 184 PRO D CD  1 
ATOM   8059  N  N   A GLU D 1 185 ? -1.647  -11.772 -35.163 0.50 15.38 ? 185 GLU D N   1 
ATOM   8060  N  N   B GLU D 1 185 ? -1.782  -11.807 -35.243 0.50 15.37 ? 185 GLU D N   1 
ATOM   8061  C  CA  A GLU D 1 185 ? -2.203  -12.750 -34.237 0.50 16.36 ? 185 GLU D CA  1 
ATOM   8062  C  CA  B GLU D 1 185 ? -2.407  -12.694 -34.274 0.50 16.09 ? 185 GLU D CA  1 
ATOM   8063  C  C   A GLU D 1 185 ? -1.902  -12.352 -32.810 0.50 15.30 ? 185 GLU D C   1 
ATOM   8064  C  C   B GLU D 1 185 ? -1.976  -12.324 -32.870 0.50 15.37 ? 185 GLU D C   1 
ATOM   8065  O  O   A GLU D 1 185 ? -0.832  -11.772 -32.492 0.50 15.43 ? 185 GLU D O   1 
ATOM   8066  O  O   B GLU D 1 185 ? -0.893  -11.750 -32.635 0.50 16.45 ? 185 GLU D O   1 
ATOM   8067  C  CB  A GLU D 1 185 ? -1.664  -14.161 -34.555 0.50 16.05 ? 185 GLU D CB  1 
ATOM   8068  C  CB  B GLU D 1 185 ? -2.062  -14.161 -34.533 0.50 16.01 ? 185 GLU D CB  1 
ATOM   8069  C  CG  A GLU D 1 185 ? -1.945  -14.568 -35.984 0.50 19.04 ? 185 GLU D CG  1 
ATOM   8070  C  CG  B GLU D 1 185 ? -2.555  -14.695 -35.844 0.50 15.87 ? 185 GLU D CG  1 
ATOM   8071  C  CD  A GLU D 1 185 ? -2.313  -16.032 -36.203 0.50 25.59 ? 185 GLU D CD  1 
ATOM   8072  C  CD  B GLU D 1 185 ? -3.958  -14.258 -36.257 0.50 22.08 ? 185 GLU D CD  1 
ATOM   8073  O  OE1 A GLU D 1 185 ? -1.568  -16.925 -35.712 0.50 24.94 ? 185 GLU D OE1 1 
ATOM   8074  O  OE1 B GLU D 1 185 ? -4.913  -14.229 -35.449 0.50 24.11 ? 185 GLU D OE1 1 
ATOM   8075  O  OE2 A GLU D 1 185 ? -3.333  -16.244 -36.915 0.50 30.75 ? 185 GLU D OE2 1 
ATOM   8076  O  OE2 B GLU D 1 185 ? -4.119  -13.972 -37.461 0.50 27.57 ? 185 GLU D OE2 1 
ATOM   8077  N  N   . ARG D 1 186 ? -2.872  -12.618 -31.912 1.00 14.80 ? 186 ARG D N   1 
ATOM   8078  C  CA  . ARG D 1 186 ? -2.566  -12.477 -30.523 1.00 16.35 ? 186 ARG D CA  1 
ATOM   8079  C  C   . ARG D 1 186 ? -2.091  -11.092 -30.142 1.00 14.86 ? 186 ARG D C   1 
ATOM   8080  O  O   . ARG D 1 186 ? -1.018  -10.905 -29.512 1.00 14.61 ? 186 ARG D O   1 
ATOM   8081  C  CB  . ARG D 1 186 ? -1.591  -13.547 -30.025 1.00 18.23 ? 186 ARG D CB  1 
ATOM   8082  C  CG  . ARG D 1 186 ? -2.257  -14.941 -30.204 1.00 22.83 ? 186 ARG D CG  1 
ATOM   8083  C  CD  . ARG D 1 186 ? -1.345  -16.127 -29.710 1.00 22.39 ? 186 ARG D CD  1 
ATOM   8084  N  NE  . ARG D 1 186 ? -0.206  -16.243 -30.627 1.00 28.41 ? 186 ARG D NE  1 
ATOM   8085  C  CZ  . ARG D 1 186 ? -0.310  -16.752 -31.866 1.00 32.22 ? 186 ARG D CZ  1 
ATOM   8086  N  NH1 . ARG D 1 186 ? -1.490  -17.202 -32.319 1.00 33.85 ? 186 ARG D NH1 1 
ATOM   8087  N  NH2 . ARG D 1 186 ? 0.751   -16.800 -32.648 1.00 36.48 ? 186 ARG D NH2 1 
ATOM   8088  N  N   . THR D 1 187 ? -2.923  -10.119 -30.508 1.00 12.71 ? 187 THR D N   1 
ATOM   8089  C  CA  . THR D 1 187 ? -2.531  -8.770  -30.117 1.00 13.96 ? 187 THR D CA  1 
ATOM   8090  C  C   . THR D 1 187 ? -2.366  -8.442  -28.620 1.00 12.81 ? 187 THR D C   1 
ATOM   8091  O  O   . THR D 1 187 ? -1.774  -7.419  -28.205 1.00 13.13 ? 187 THR D O   1 
ATOM   8092  C  CB  . THR D 1 187 ? -3.561  -7.779  -30.733 1.00 14.83 ? 187 THR D CB  1 
ATOM   8093  O  OG1 . THR D 1 187 ? -4.903  -8.121  -30.329 1.00 15.81 ? 187 THR D OG1 1 
ATOM   8094  C  CG2 . THR D 1 187 ? -3.617  -7.777  -32.306 1.00 12.14 ? 187 THR D CG2 1 
ATOM   8095  N  N   . ALA D 1 188 ? -2.899  -9.338  -27.742 1.00 13.91 ? 188 ALA D N   1 
ATOM   8096  C  CA  . ALA D 1 188 ? -2.720  -9.138  -26.345 1.00 12.35 ? 188 ALA D CA  1 
ATOM   8097  C  C   . ALA D 1 188 ? -1.189  -9.278  -25.910 1.00 12.41 ? 188 ALA D C   1 
ATOM   8098  O  O   . ALA D 1 188 ? -0.778  -8.867  -24.808 1.00 13.25 ? 188 ALA D O   1 
ATOM   8099  C  CB  . ALA D 1 188 ? -3.552  -10.247 -25.564 1.00 13.69 ? 188 ALA D CB  1 
ATOM   8100  N  N   . GLU D 1 189 ? -0.425  -9.947  -26.804 1.00 12.09 ? 189 GLU D N   1 
ATOM   8101  C  CA  . GLU D 1 189 ? 1.020   -10.079 -26.516 1.00 10.80 ? 189 GLU D CA  1 
ATOM   8102  C  C   . GLU D 1 189 ? 1.810   -8.937  -27.294 1.00 8.81  ? 189 GLU D C   1 
ATOM   8103  O  O   . GLU D 1 189 ? 1.834   -8.885  -28.539 1.00 10.84 ? 189 GLU D O   1 
ATOM   8104  C  CB  . GLU D 1 189 ? 1.542   -11.389 -27.113 1.00 12.42 ? 189 GLU D CB  1 
ATOM   8105  C  CG  . GLU D 1 189 ? 0.725   -12.549 -26.445 1.00 12.80 ? 189 GLU D CG  1 
ATOM   8106  C  CD  . GLU D 1 189 ? 1.166   -13.912 -26.867 1.00 22.01 ? 189 GLU D CD  1 
ATOM   8107  O  OE1 . GLU D 1 189 ? 2.310   -14.122 -27.243 1.00 22.00 ? 189 GLU D OE1 1 
ATOM   8108  O  OE2 . GLU D 1 189 ? 0.331   -14.848 -26.675 1.00 30.36 ? 189 GLU D OE2 1 
ATOM   8109  N  N   . TYR D 1 190 ? 2.471   -8.117  -26.489 1.00 10.87 ? 190 TYR D N   1 
ATOM   8110  C  CA  . TYR D 1 190 ? 3.155   -6.954  -27.054 1.00 8.86  ? 190 TYR D CA  1 
ATOM   8111  C  C   . TYR D 1 190 ? 4.216   -6.474  -26.176 1.00 9.84  ? 190 TYR D C   1 
ATOM   8112  O  O   . TYR D 1 190 ? 4.313   -6.858  -24.966 1.00 9.57  ? 190 TYR D O   1 
ATOM   8113  C  CB  . TYR D 1 190 ? 2.162   -5.827  -27.320 1.00 10.54 ? 190 TYR D CB  1 
ATOM   8114  C  CG  . TYR D 1 190 ? 1.377   -5.343  -26.104 1.00 9.85  ? 190 TYR D CG  1 
ATOM   8115  C  CD1 . TYR D 1 190 ? 1.958   -4.470  -25.219 1.00 10.40 ? 190 TYR D CD1 1 
ATOM   8116  C  CD2 . TYR D 1 190 ? 0.045   -5.801  -25.932 1.00 10.50 ? 190 TYR D CD2 1 
ATOM   8117  C  CE1 . TYR D 1 190 ? 1.182   -4.007  -24.091 1.00 9.51  ? 190 TYR D CE1 1 
ATOM   8118  C  CE2 . TYR D 1 190 ? -0.680  -5.396  -24.792 1.00 9.42  ? 190 TYR D CE2 1 
ATOM   8119  C  CZ  . TYR D 1 190 ? -0.117  -4.512  -23.946 1.00 11.07 ? 190 TYR D CZ  1 
ATOM   8120  O  OH  . TYR D 1 190 ? -0.840  -4.051  -22.775 1.00 12.45 ? 190 TYR D OH  1 
ATOM   8121  N  N   . TYR D 1 191 ? 5.145   -5.681  -26.752 1.00 8.30  ? 191 TYR D N   1 
ATOM   8122  C  CA  . TYR D 1 191 ? 6.166   -4.975  -26.104 1.00 9.57  ? 191 TYR D CA  1 
ATOM   8123  C  C   . TYR D 1 191 ? 5.695   -3.490  -25.904 1.00 9.68  ? 191 TYR D C   1 
ATOM   8124  O  O   . TYR D 1 191 ? 5.024   -2.968  -26.794 1.00 9.37  ? 191 TYR D O   1 
ATOM   8125  C  CB  . TYR D 1 191 ? 7.477   -4.868  -26.970 1.00 8.33  ? 191 TYR D CB  1 
ATOM   8126  C  CG  . TYR D 1 191 ? 8.031   -6.173  -27.512 1.00 9.23  ? 191 TYR D CG  1 
ATOM   8127  C  CD1 . TYR D 1 191 ? 8.977   -6.917  -26.790 1.00 8.67  ? 191 TYR D CD1 1 
ATOM   8128  C  CD2 . TYR D 1 191 ? 7.576   -6.638  -28.737 1.00 9.14  ? 191 TYR D CD2 1 
ATOM   8129  C  CE1 . TYR D 1 191 ? 9.482   -8.060  -27.344 1.00 8.63  ? 191 TYR D CE1 1 
ATOM   8130  C  CE2 . TYR D 1 191 ? 8.117   -7.858  -29.283 1.00 8.63  ? 191 TYR D CE2 1 
ATOM   8131  C  CZ  . TYR D 1 191 ? 9.098   -8.463  -28.546 1.00 9.37  ? 191 TYR D CZ  1 
ATOM   8132  O  OH  . TYR D 1 191 ? 9.690   -9.651  -29.037 1.00 13.83 ? 191 TYR D OH  1 
ATOM   8133  N  N   . ARG D 1 192 ? 6.029   -2.883  -24.802 1.00 9.65  ? 192 ARG D N   1 
ATOM   8134  C  CA  . ARG D 1 192 ? 5.603   -1.488  -24.471 1.00 10.52 ? 192 ARG D CA  1 
ATOM   8135  C  C   . ARG D 1 192 ? 6.791   -0.725  -23.921 1.00 9.89  ? 192 ARG D C   1 
ATOM   8136  O  O   . ARG D 1 192 ? 7.517   -1.156  -23.006 1.00 10.97 ? 192 ARG D O   1 
ATOM   8137  C  CB  . ARG D 1 192 ? 4.500   -1.500  -23.448 1.00 10.71 ? 192 ARG D CB  1 
ATOM   8138  C  CG  . ARG D 1 192 ? 4.184   -0.286  -22.626 1.00 16.83 ? 192 ARG D CG  1 
ATOM   8139  C  CD  . ARG D 1 192 ? 3.534   0.670   -23.574 1.00 14.05 ? 192 ARG D CD  1 
ATOM   8140  N  NE  . ARG D 1 192 ? 2.293   0.156   -24.256 1.00 16.14 ? 192 ARG D NE  1 
ATOM   8141  C  CZ  . ARG D 1 192 ? 1.115   -0.229  -23.778 1.00 13.41 ? 192 ARG D CZ  1 
ATOM   8142  N  NH1 . ARG D 1 192 ? 0.806   -0.091  -22.432 1.00 19.58 ? 192 ARG D NH1 1 
ATOM   8143  N  NH2 . ARG D 1 192 ? 0.138   -0.761  -24.573 1.00 13.77 ? 192 ARG D NH2 1 
ATOM   8144  N  N   . TYR D 1 193 ? 6.999   0.492   -24.456 1.00 9.41  ? 193 TYR D N   1 
ATOM   8145  C  CA  . TYR D 1 193 ? 8.090   1.328   -23.902 1.00 8.60  ? 193 TYR D CA  1 
ATOM   8146  C  C   . TYR D 1 193 ? 7.837   2.808   -24.215 1.00 9.86  ? 193 TYR D C   1 
ATOM   8147  O  O   . TYR D 1 193 ? 7.031   3.134   -25.083 1.00 10.09 ? 193 TYR D O   1 
ATOM   8148  C  CB  . TYR D 1 193 ? 9.461   0.846   -24.386 1.00 10.24 ? 193 TYR D CB  1 
ATOM   8149  C  CG  . TYR D 1 193 ? 9.793   1.262   -25.806 1.00 8.89  ? 193 TYR D CG  1 
ATOM   8150  C  CD1 . TYR D 1 193 ? 10.597  2.365   -26.052 1.00 9.57  ? 193 TYR D CD1 1 
ATOM   8151  C  CD2 . TYR D 1 193 ? 9.307   0.551   -26.901 1.00 9.57  ? 193 TYR D CD2 1 
ATOM   8152  C  CE1 . TYR D 1 193 ? 10.912  2.750   -27.337 1.00 9.32  ? 193 TYR D CE1 1 
ATOM   8153  C  CE2 . TYR D 1 193 ? 9.620   0.936   -28.200 1.00 9.68  ? 193 TYR D CE2 1 
ATOM   8154  C  CZ  . TYR D 1 193 ? 10.426  2.038   -28.404 1.00 9.60  ? 193 TYR D CZ  1 
ATOM   8155  O  OH  . TYR D 1 193 ? 10.760  2.451   -29.678 1.00 8.94  ? 193 TYR D OH  1 
ATOM   8156  N  N   . ARG D 1 194 ? 8.577   3.634   -23.521 1.00 9.80  ? 194 ARG D N   1 
ATOM   8157  C  CA  . ARG D 1 194 ? 8.442   5.117   -23.761 1.00 11.07 ? 194 ARG D CA  1 
ATOM   8158  C  C   . ARG D 1 194 ? 9.530   5.546   -24.649 1.00 9.06  ? 194 ARG D C   1 
ATOM   8159  O  O   . ARG D 1 194 ? 10.725  5.306   -24.412 1.00 11.39 ? 194 ARG D O   1 
ATOM   8160  C  CB  . ARG D 1 194 ? 8.649   5.910   -22.480 1.00 13.25 ? 194 ARG D CB  1 
ATOM   8161  C  CG  . ARG D 1 194 ? 7.736   5.453   -21.408 1.00 19.59 ? 194 ARG D CG  1 
ATOM   8162  C  CD  . ARG D 1 194 ? 6.564   6.188   -21.570 1.00 26.73 ? 194 ARG D CD  1 
ATOM   8163  N  NE  . ARG D 1 194 ? 5.530   5.824   -20.613 1.00 35.89 ? 194 ARG D NE  1 
ATOM   8164  C  CZ  . ARG D 1 194 ? 4.497   6.621   -20.374 1.00 38.44 ? 194 ARG D CZ  1 
ATOM   8165  N  NH1 . ARG D 1 194 ? 4.466   7.803   -20.970 1.00 34.59 ? 194 ARG D NH1 1 
ATOM   8166  N  NH2 . ARG D 1 194 ? 3.528   6.257   -19.534 1.00 36.55 ? 194 ARG D NH2 1 
ATOM   8167  N  N   . GLY D 1 195 ? 9.111   6.149   -25.797 1.00 8.69  ? 195 GLY D N   1 
ATOM   8168  C  CA  . GLY D 1 195 ? 10.104  6.629   -26.800 1.00 9.80  ? 195 GLY D CA  1 
ATOM   8169  C  C   . GLY D 1 195 ? 9.671   7.884   -27.493 1.00 9.59  ? 195 GLY D C   1 
ATOM   8170  O  O   . GLY D 1 195 ? 9.017   8.764   -26.896 1.00 10.48 ? 195 GLY D O   1 
ATOM   8171  N  N   . SER D 1 196 ? 9.977   7.956   -28.769 1.00 8.27  ? 196 SER D N   1 
ATOM   8172  C  CA  . SER D 1 196 ? 9.881   9.203   -29.508 1.00 8.52  ? 196 SER D CA  1 
ATOM   8173  C  C   . SER D 1 196 ? 9.290   8.952   -30.877 1.00 8.01  ? 196 SER D C   1 
ATOM   8174  O  O   . SER D 1 196 ? 9.144   7.796   -31.349 1.00 8.68  ? 196 SER D O   1 
ATOM   8175  C  CB  . SER D 1 196 ? 11.266  9.801   -29.701 1.00 9.97  ? 196 SER D CB  1 
ATOM   8176  O  OG  . SER D 1 196 ? 12.045  9.043   -30.648 1.00 8.96  ? 196 SER D OG  1 
ATOM   8177  N  N   . LEU D 1 197 ? 8.999   9.990   -31.582 1.00 8.40  ? 197 LEU D N   1 
ATOM   8178  C  CA  . LEU D 1 197 ? 8.812   9.871   -33.032 1.00 7.41  ? 197 LEU D CA  1 
ATOM   8179  C  C   . LEU D 1 197 ? 10.159  9.399   -33.625 1.00 7.90  ? 197 LEU D C   1 
ATOM   8180  O  O   . LEU D 1 197 ? 11.228  9.753   -33.192 1.00 8.10  ? 197 LEU D O   1 
ATOM   8181  C  CB  . LEU D 1 197 ? 8.583   11.297  -33.666 1.00 8.38  ? 197 LEU D CB  1 
ATOM   8182  C  CG  . LEU D 1 197 ? 7.210   11.886  -33.568 1.00 8.45  ? 197 LEU D CG  1 
ATOM   8183  C  CD1 . LEU D 1 197 ? 7.025   12.642  -32.123 1.00 11.77 ? 197 LEU D CD1 1 
ATOM   8184  C  CD2 . LEU D 1 197 ? 7.020   12.945  -34.674 1.00 12.02 ? 197 LEU D CD2 1 
ATOM   8185  N  N   . THR D 1 198 ? 10.023  8.446   -34.602 1.00 6.70  ? 198 THR D N   1 
ATOM   8186  C  CA  . THR D 1 198 ? 11.233  8.016   -35.291 1.00 7.91  ? 198 THR D CA  1 
ATOM   8187  C  C   . THR D 1 198 ? 11.677  8.853   -36.436 1.00 7.11  ? 198 THR D C   1 
ATOM   8188  O  O   . THR D 1 198 ? 12.686  8.566   -37.111 1.00 8.37  ? 198 THR D O   1 
ATOM   8189  C  CB  . THR D 1 198 ? 11.145  6.611   -35.776 1.00 5.76  ? 198 THR D CB  1 
ATOM   8190  O  OG1 . THR D 1 198 ? 10.157  6.621   -36.785 1.00 6.90  ? 198 THR D OG1 1 
ATOM   8191  C  CG2 . THR D 1 198 ? 10.704  5.576   -34.699 1.00 8.64  ? 198 THR D CG2 1 
ATOM   8192  N  N   . THR D 1 199 ? 10.921  9.947   -36.627 1.00 7.16  ? 199 THR D N   1 
ATOM   8193  C  CA  . THR D 1 199 ? 11.305  10.945  -37.686 1.00 8.38  ? 199 THR D CA  1 
ATOM   8194  C  C   . THR D 1 199 ? 11.392  12.282  -37.022 1.00 7.79  ? 199 THR D C   1 
ATOM   8195  O  O   . THR D 1 199 ? 10.763  12.467  -35.970 1.00 10.02 ? 199 THR D O   1 
ATOM   8196  C  CB  . THR D 1 199 ? 10.185  11.115  -38.726 1.00 8.64  ? 199 THR D CB  1 
ATOM   8197  O  OG1 . THR D 1 199 ? 8.968   11.489  -38.096 1.00 12.10 ? 199 THR D OG1 1 
ATOM   8198  C  CG2 . THR D 1 199 ? 9.959   9.685   -39.423 1.00 10.57 ? 199 THR D CG2 1 
ATOM   8199  N  N   . PRO D 1 200 ? 12.089  13.222  -37.654 1.00 7.50  ? 200 PRO D N   1 
ATOM   8200  C  CA  . PRO D 1 200 ? 12.032  14.603  -37.133 1.00 8.67  ? 200 PRO D CA  1 
ATOM   8201  C  C   . PRO D 1 200 ? 10.575  14.994  -36.911 1.00 9.86  ? 200 PRO D C   1 
ATOM   8202  O  O   . PRO D 1 200 ? 9.755   14.695  -37.731 1.00 9.50  ? 200 PRO D O   1 
ATOM   8203  C  CB  . PRO D 1 200 ? 12.708  15.383  -38.255 1.00 7.37  ? 200 PRO D CB  1 
ATOM   8204  C  CG  . PRO D 1 200 ? 13.750  14.406  -38.809 1.00 9.55  ? 200 PRO D CG  1 
ATOM   8205  C  CD  . PRO D 1 200 ? 12.964  13.059  -38.814 1.00 9.33  ? 200 PRO D CD  1 
ATOM   8206  N  N   . PRO D 1 201 ? 10.302  15.824  -35.897 1.00 9.14  ? 201 PRO D N   1 
ATOM   8207  C  CA  . PRO D 1 201 ? 11.297  16.344  -34.921 1.00 8.37  ? 201 PRO D CA  1 
ATOM   8208  C  C   . PRO D 1 201 ? 11.707  15.486  -33.728 1.00 9.75  ? 201 PRO D C   1 
ATOM   8209  O  O   . PRO D 1 201 ? 12.372  15.921  -32.801 1.00 9.47  ? 201 PRO D O   1 
ATOM   8210  C  CB  . PRO D 1 201 ? 10.532  17.612  -34.322 1.00 8.63  ? 201 PRO D CB  1 
ATOM   8211  C  CG  . PRO D 1 201 ? 9.361   17.779  -35.211 1.00 12.10 ? 201 PRO D CG  1 
ATOM   8212  C  CD  . PRO D 1 201 ? 8.958   16.405  -35.667 1.00 10.60 ? 201 PRO D CD  1 
ATOM   8213  N  N   . CYS D 1 202 ? 11.358  14.179  -33.778 1.00 9.47  ? 202 CYS D N   1 
ATOM   8214  C  CA  . CYS D 1 202 ? 11.908  13.173  -32.805 1.00 9.18  ? 202 CYS D CA  1 
ATOM   8215  C  C   . CYS D 1 202 ? 11.377  13.384  -31.366 1.00 9.10  ? 202 CYS D C   1 
ATOM   8216  O  O   . CYS D 1 202 ? 12.053  13.014  -30.428 1.00 8.28  ? 202 CYS D O   1 
ATOM   8217  C  CB  . CYS D 1 202 ? 13.447  13.066  -32.767 1.00 9.74  ? 202 CYS D CB  1 
ATOM   8218  S  SG  . CYS D 1 202 ? 14.157  12.727  -34.471 1.00 9.70  ? 202 CYS D SG  1 
ATOM   8219  N  N   . ASN D 1 203 ? 10.241  14.058  -31.268 1.00 9.96  ? 203 ASN D N   1 
ATOM   8220  C  CA  . ASN D 1 203 ? 9.814   14.429  -29.873 1.00 10.91 ? 203 ASN D CA  1 
ATOM   8221  C  C   . ASN D 1 203 ? 9.673   13.196  -29.040 1.00 10.14 ? 203 ASN D C   1 
ATOM   8222  O  O   . ASN D 1 203 ? 9.137   12.201  -29.494 1.00 9.23  ? 203 ASN D O   1 
ATOM   8223  C  CB  . ASN D 1 203 ? 8.523   15.223  -29.914 1.00 11.48 ? 203 ASN D CB  1 
ATOM   8224  C  CG  . ASN D 1 203 ? 8.643   16.347  -30.837 1.00 11.75 ? 203 ASN D CG  1 
ATOM   8225  O  OD1 . ASN D 1 203 ? 8.456   16.204  -32.017 1.00 11.99 ? 203 ASN D OD1 1 
ATOM   8226  N  ND2 . ASN D 1 203 ? 9.018   17.468  -30.302 1.00 15.21 ? 203 ASN D ND2 1 
ATOM   8227  N  N   . PRO D 1 204 ? 10.167  13.240  -27.813 1.00 8.54  ? 204 PRO D N   1 
ATOM   8228  C  CA  . PRO D 1 204 ? 10.040  12.059  -26.901 1.00 9.59  ? 204 PRO D CA  1 
ATOM   8229  C  C   . PRO D 1 204 ? 8.659   11.929  -26.245 1.00 9.40  ? 204 PRO D C   1 
ATOM   8230  O  O   . PRO D 1 204 ? 8.580   11.993  -24.968 1.00 12.57 ? 204 PRO D O   1 
ATOM   8231  C  CB  . PRO D 1 204 ? 11.121  12.306  -25.798 1.00 9.54  ? 204 PRO D CB  1 
ATOM   8232  C  CG  . PRO D 1 204 ? 11.148  13.826  -25.752 1.00 11.31 ? 204 PRO D CG  1 
ATOM   8233  C  CD  . PRO D 1 204 ? 11.054  14.299  -27.196 1.00 9.75  ? 204 PRO D CD  1 
ATOM   8234  N  N   . THR D 1 205 ? 7.633   11.784  -27.046 1.00 8.24  ? 205 THR D N   1 
ATOM   8235  C  CA  . THR D 1 205 ? 6.249   11.903  -26.659 1.00 8.54  ? 205 THR D CA  1 
ATOM   8236  C  C   . THR D 1 205 ? 5.350   10.720  -26.996 1.00 9.58  ? 205 THR D C   1 
ATOM   8237  O  O   . THR D 1 205 ? 4.136   10.816  -26.982 1.00 9.78  ? 205 THR D O   1 
ATOM   8238  C  CB  . THR D 1 205 ? 5.645   13.175  -27.260 1.00 10.16 ? 205 THR D CB  1 
ATOM   8239  O  OG1 . THR D 1 205 ? 5.830   13.066  -28.695 1.00 10.78 ? 205 THR D OG1 1 
ATOM   8240  C  CG2 . THR D 1 205 ? 6.255   14.608  -26.761 1.00 10.56 ? 205 THR D CG2 1 
ATOM   8241  N  N   . VAL D 1 206 ? 6.044   9.622   -27.376 1.00 9.41  ? 206 VAL D N   1 
ATOM   8242  C  CA  . VAL D 1 206 ? 5.337   8.452   -27.862 1.00 8.94  ? 206 VAL D CA  1 
ATOM   8243  C  C   . VAL D 1 206 ? 5.381   7.236   -26.914 1.00 7.78  ? 206 VAL D C   1 
ATOM   8244  O  O   . VAL D 1 206 ? 6.436   6.898   -26.503 1.00 8.91  ? 206 VAL D O   1 
ATOM   8245  C  CB  . VAL D 1 206 ? 5.928   8.005   -29.247 1.00 8.25  ? 206 VAL D CB  1 
ATOM   8246  C  CG1 . VAL D 1 206 ? 5.198   6.820   -29.758 1.00 9.01  ? 206 VAL D CG1 1 
ATOM   8247  C  CG2 . VAL D 1 206 ? 5.978   9.182   -30.243 1.00 10.29 ? 206 VAL D CG2 1 
ATOM   8248  N  N   . LEU D 1 207 ? 4.183   6.805   -26.637 1.00 8.14  ? 207 LEU D N   1 
ATOM   8249  C  CA  . LEU D 1 207 ? 3.991   5.507   -25.977 1.00 9.68  ? 207 LEU D CA  1 
ATOM   8250  C  C   . LEU D 1 207 ? 3.938   4.435   -27.056 1.00 8.71  ? 207 LEU D C   1 
ATOM   8251  O  O   . LEU D 1 207 ? 2.976   4.384   -27.838 1.00 9.99  ? 207 LEU D O   1 
ATOM   8252  C  CB  . LEU D 1 207 ? 2.761   5.494   -25.125 1.00 11.57 ? 207 LEU D CB  1 
ATOM   8253  C  CG  . LEU D 1 207 ? 2.732   4.245   -24.197 1.00 14.07 ? 207 LEU D CG  1 
ATOM   8254  C  CD1 . LEU D 1 207 ? 3.994   4.129   -23.272 1.00 18.06 ? 207 LEU D CD1 1 
ATOM   8255  C  CD2 . LEU D 1 207 ? 1.532   4.291   -23.547 1.00 18.37 ? 207 LEU D CD2 1 
ATOM   8256  N  N   . TRP D 1 208 ? 5.004   3.673   -27.109 1.00 8.79  ? 208 TRP D N   1 
ATOM   8257  C  CA  . TRP D 1 208 ? 5.072   2.578   -28.133 1.00 8.90  ? 208 TRP D CA  1 
ATOM   8258  C  C   . TRP D 1 208 ? 4.493   1.217   -27.740 1.00 8.07  ? 208 TRP D C   1 
ATOM   8259  O  O   . TRP D 1 208 ? 4.835   0.770   -26.634 1.00 10.77 ? 208 TRP D O   1 
ATOM   8260  C  CB  . TRP D 1 208 ? 6.591   2.324   -28.493 1.00 8.83  ? 208 TRP D CB  1 
ATOM   8261  C  CG  . TRP D 1 208 ? 7.113   3.428   -29.448 1.00 8.29  ? 208 TRP D CG  1 
ATOM   8262  C  CD1 . TRP D 1 208 ? 7.786   4.579   -29.104 1.00 10.56 ? 208 TRP D CD1 1 
ATOM   8263  C  CD2 . TRP D 1 208 ? 6.927   3.445   -30.841 1.00 8.67  ? 208 TRP D CD2 1 
ATOM   8264  N  NE1 . TRP D 1 208 ? 8.032   5.339   -30.209 1.00 8.51  ? 208 TRP D NE1 1 
ATOM   8265  C  CE2 . TRP D 1 208 ? 7.496   4.686   -31.296 1.00 7.53  ? 208 TRP D CE2 1 
ATOM   8266  C  CE3 . TRP D 1 208 ? 6.364   2.576   -31.806 1.00 9.26  ? 208 TRP D CE3 1 
ATOM   8267  C  CZ2 . TRP D 1 208 ? 7.510   5.076   -32.663 1.00 8.38  ? 208 TRP D CZ2 1 
ATOM   8268  C  CZ3 . TRP D 1 208 ? 6.386   2.962   -33.172 1.00 8.40  ? 208 TRP D CZ3 1 
ATOM   8269  C  CH2 . TRP D 1 208 ? 6.960   4.202   -33.568 1.00 10.54 ? 208 TRP D CH2 1 
ATOM   8270  N  N   . THR D 1 209 ? 3.679   0.641   -28.626 1.00 5.91  ? 209 THR D N   1 
ATOM   8271  C  CA  . THR D 1 209 ? 3.255   -0.733  -28.431 1.00 7.18  ? 209 THR D CA  1 
ATOM   8272  C  C   . THR D 1 209 ? 3.668   -1.433  -29.730 1.00 8.01  ? 209 THR D C   1 
ATOM   8273  O  O   . THR D 1 209 ? 3.180   -1.126  -30.809 1.00 8.27  ? 209 THR D O   1 
ATOM   8274  C  CB  . THR D 1 209 ? 1.732   -0.818  -28.315 1.00 10.61 ? 209 THR D CB  1 
ATOM   8275  O  OG1 . THR D 1 209 ? 1.375   -0.049  -27.128 1.00 10.23 ? 209 THR D OG1 1 
ATOM   8276  C  CG2 . THR D 1 209 ? 1.231   -2.253  -28.140 1.00 10.09 ? 209 THR D CG2 1 
ATOM   8277  N  N   . VAL D 1 210 ? 4.577   -2.403  -29.578 1.00 8.83  ? 210 VAL D N   1 
ATOM   8278  C  CA  . VAL D 1 210 ? 5.039   -3.245  -30.659 1.00 8.71  ? 210 VAL D CA  1 
ATOM   8279  C  C   . VAL D 1 210 ? 4.446   -4.638  -30.514 1.00 8.37  ? 210 VAL D C   1 
ATOM   8280  O  O   . VAL D 1 210 ? 4.753   -5.277  -29.534 1.00 9.14  ? 210 VAL D O   1 
ATOM   8281  C  CB  . VAL D 1 210 ? 6.590   -3.280  -30.788 1.00 7.72  ? 210 VAL D CB  1 
ATOM   8282  C  CG1 . VAL D 1 210 ? 6.972   -4.072  -32.022 1.00 9.46  ? 210 VAL D CG1 1 
ATOM   8283  C  CG2 . VAL D 1 210 ? 7.133   -1.867  -30.834 1.00 8.90  ? 210 VAL D CG2 1 
ATOM   8284  N  N   . PHE D 1 211 ? 3.605   -5.093  -31.426 1.00 8.37  ? 211 PHE D N   1 
ATOM   8285  C  CA  . PHE D 1 211 ? 3.021   -6.409  -31.215 1.00 8.35  ? 211 PHE D CA  1 
ATOM   8286  C  C   . PHE D 1 211 ? 4.128   -7.472  -31.323 1.00 9.09  ? 211 PHE D C   1 
ATOM   8287  O  O   . PHE D 1 211 ? 5.084   -7.403  -32.125 1.00 9.89  ? 211 PHE D O   1 
ATOM   8288  C  CB  . PHE D 1 211 ? 1.918   -6.639  -32.260 1.00 9.28  ? 211 PHE D CB  1 
ATOM   8289  C  CG  . PHE D 1 211 ? 0.760   -5.761  -32.041 1.00 9.63  ? 211 PHE D CG  1 
ATOM   8290  C  CD1 . PHE D 1 211 ? -0.009  -5.923  -30.829 1.00 10.66 ? 211 PHE D CD1 1 
ATOM   8291  C  CD2 . PHE D 1 211 ? 0.471   -4.689  -32.912 1.00 12.85 ? 211 PHE D CD2 1 
ATOM   8292  C  CE1 . PHE D 1 211 ? -1.025  -5.068  -30.503 1.00 10.65 ? 211 PHE D CE1 1 
ATOM   8293  C  CE2 . PHE D 1 211 ? -0.627  -3.882  -32.552 1.00 12.78 ? 211 PHE D CE2 1 
ATOM   8294  C  CZ  . PHE D 1 211 ? -1.339  -4.053  -31.351 1.00 11.22 ? 211 PHE D CZ  1 
ATOM   8295  N  N   . ARG D 1 212 ? 3.959   -8.597  -30.576 1.00 9.90  ? 212 ARG D N   1 
ATOM   8296  C  CA  . ARG D 1 212 ? 4.998   -9.638  -30.521 1.00 9.83  ? 212 ARG D CA  1 
ATOM   8297  C  C   . ARG D 1 212 ? 5.060   -10.339 -31.867 1.00 10.05 ? 212 ARG D C   1 
ATOM   8298  O  O   . ARG D 1 212 ? 6.182   -10.714 -32.271 1.00 11.56 ? 212 ARG D O   1 
ATOM   8299  C  CB  . ARG D 1 212 ? 4.647   -10.603 -29.371 1.00 10.86 ? 212 ARG D CB  1 
ATOM   8300  C  CG  . ARG D 1 212 ? 5.717   -11.718 -29.367 1.00 9.99  ? 212 ARG D CG  1 
ATOM   8301  C  CD  . ARG D 1 212 ? 5.216   -12.772 -28.316 1.00 14.70 ? 212 ARG D CD  1 
ATOM   8302  N  NE  . ARG D 1 212 ? 6.292   -13.737 -27.996 1.00 15.96 ? 212 ARG D NE  1 
ATOM   8303  C  CZ  . ARG D 1 212 ? 6.119   -14.734 -27.117 1.00 19.94 ? 212 ARG D CZ  1 
ATOM   8304  N  NH1 . ARG D 1 212 ? 4.967   -14.958 -26.560 1.00 21.88 ? 212 ARG D NH1 1 
ATOM   8305  N  NH2 . ARG D 1 212 ? 7.117   -15.564 -26.876 1.00 22.81 ? 212 ARG D NH2 1 
ATOM   8306  N  N   . ASN D 1 213 ? 3.938   -10.624 -32.471 1.00 10.91 ? 213 ASN D N   1 
ATOM   8307  C  CA  . ASN D 1 213 ? 3.890   -11.406 -33.698 1.00 10.84 ? 213 ASN D CA  1 
ATOM   8308  C  C   . ASN D 1 213 ? 3.909   -10.479 -34.951 1.00 12.31 ? 213 ASN D C   1 
ATOM   8309  O  O   . ASN D 1 213 ? 3.161   -9.491  -34.990 1.00 10.77 ? 213 ASN D O   1 
ATOM   8310  C  CB  . ASN D 1 213 ? 2.626   -12.283 -33.681 1.00 14.05 ? 213 ASN D CB  1 
ATOM   8311  C  CG  . ASN D 1 213 ? 2.647   -13.236 -32.524 1.00 19.68 ? 213 ASN D CG  1 
ATOM   8312  O  OD1 . ASN D 1 213 ? 1.667   -13.298 -31.767 1.00 20.15 ? 213 ASN D OD1 1 
ATOM   8313  N  ND2 . ASN D 1 213 ? 3.762   -13.883 -32.343 1.00 18.15 ? 213 ASN D ND2 1 
ATOM   8314  N  N   . PRO D 1 214 ? 4.644   -10.861 -35.984 1.00 10.23 ? 214 PRO D N   1 
ATOM   8315  C  CA  . PRO D 1 214 ? 4.575   -10.172 -37.280 1.00 10.31 ? 214 PRO D CA  1 
ATOM   8316  C  C   . PRO D 1 214 ? 3.400   -10.557 -38.087 1.00 9.22  ? 214 PRO D C   1 
ATOM   8317  O  O   . PRO D 1 214 ? 2.807   -11.633 -37.842 1.00 11.68 ? 214 PRO D O   1 
ATOM   8318  C  CB  . PRO D 1 214 ? 5.911   -10.549 -37.984 1.00 9.78  ? 214 PRO D CB  1 
ATOM   8319  C  CG  . PRO D 1 214 ? 6.084   -11.986 -37.512 1.00 12.82 ? 214 PRO D CG  1 
ATOM   8320  C  CD  . PRO D 1 214 ? 5.608   -12.007 -35.986 1.00 12.99 ? 214 PRO D CD  1 
ATOM   8321  N  N   . VAL D 1 215 ? 3.083   -9.738  -39.095 1.00 9.69  ? 215 VAL D N   1 
ATOM   8322  C  CA  . VAL D 1 215 ? 2.262   -10.183 -40.214 1.00 9.03  ? 215 VAL D CA  1 
ATOM   8323  C  C   . VAL D 1 215 ? 3.160   -10.500 -41.375 1.00 7.49  ? 215 VAL D C   1 
ATOM   8324  O  O   . VAL D 1 215 ? 4.363   -10.232 -41.299 1.00 9.16  ? 215 VAL D O   1 
ATOM   8325  C  CB  . VAL D 1 215 ? 1.209   -9.175  -40.635 1.00 9.55  ? 215 VAL D CB  1 
ATOM   8326  C  CG1 . VAL D 1 215 ? 0.283   -8.817  -39.397 1.00 11.19 ? 215 VAL D CG1 1 
ATOM   8327  C  CG2 . VAL D 1 215 ? 1.886   -7.894  -41.221 1.00 10.62 ? 215 VAL D CG2 1 
ATOM   8328  N  N   . GLN D 1 216 ? 2.603   -11.066 -42.413 1.00 8.27  ? 216 GLN D N   1 
ATOM   8329  C  CA  . GLN D 1 216 ? 3.325   -11.396 -43.663 1.00 8.85  ? 216 GLN D CA  1 
ATOM   8330  C  C   . GLN D 1 216 ? 2.673   -10.594 -44.787 1.00 9.51  ? 216 GLN D C   1 
ATOM   8331  O  O   . GLN D 1 216 ? 1.443   -10.482 -44.912 1.00 10.01 ? 216 GLN D O   1 
ATOM   8332  C  CB  . GLN D 1 216 ? 3.255   -12.928 -44.062 1.00 10.41 ? 216 GLN D CB  1 
ATOM   8333  C  CG  . GLN D 1 216 ? 4.032   -13.737 -43.055 1.00 10.40 ? 216 GLN D CG  1 
ATOM   8334  C  CD  . GLN D 1 216 ? 3.989   -15.214 -43.443 1.00 13.09 ? 216 GLN D CD  1 
ATOM   8335  O  OE1 . GLN D 1 216 ? 3.435   -15.680 -44.487 1.00 12.92 ? 216 GLN D OE1 1 
ATOM   8336  N  NE2 . GLN D 1 216 ? 4.659   -15.990 -42.564 1.00 19.54 ? 216 GLN D NE2 1 
ATOM   8337  N  N   . ILE D 1 217 ? 3.520   -10.140 -45.689 1.00 8.08  ? 217 ILE D N   1 
ATOM   8338  C  CA  . ILE D 1 217 ? 3.112   -9.696  -47.062 1.00 8.56  ? 217 ILE D CA  1 
ATOM   8339  C  C   . ILE D 1 217 ? 4.062   -10.373 -48.076 1.00 7.16  ? 217 ILE D C   1 
ATOM   8340  O  O   . ILE D 1 217 ? 5.198   -10.777 -47.621 1.00 8.83  ? 217 ILE D O   1 
ATOM   8341  C  CB  . ILE D 1 217 ? 3.136   -8.124  -47.207 1.00 7.56  ? 217 ILE D CB  1 
ATOM   8342  C  CG1 . ILE D 1 217 ? 4.599   -7.626  -47.232 1.00 7.88  ? 217 ILE D CG1 1 
ATOM   8343  C  CG2 . ILE D 1 217 ? 2.199   -7.445  -46.157 1.00 9.68  ? 217 ILE D CG2 1 
ATOM   8344  C  CD1 . ILE D 1 217 ? 4.669   -5.986  -47.472 1.00 12.39 ? 217 ILE D CD1 1 
ATOM   8345  N  N   . SER D 1 218 ? 3.690   -10.460 -49.335 1.00 7.38  ? 218 SER D N   1 
ATOM   8346  C  CA  . SER D 1 218 ? 4.543   -11.190 -50.224 1.00 7.28  ? 218 SER D CA  1 
ATOM   8347  C  C   . SER D 1 218 ? 5.760   -10.469 -50.740 1.00 8.28  ? 218 SER D C   1 
ATOM   8348  O  O   . SER D 1 218 ? 5.814   -9.181  -50.665 1.00 9.06  ? 218 SER D O   1 
ATOM   8349  C  CB  . SER D 1 218 ? 3.748   -11.703 -51.417 1.00 9.25  ? 218 SER D CB  1 
ATOM   8350  O  OG  . SER D 1 218 ? 3.365   -10.624 -52.259 1.00 9.13  ? 218 SER D OG  1 
ATOM   8351  N  N   . GLN D 1 219 ? 6.725   -11.161 -51.310 1.00 9.71  ? 219 GLN D N   1 
ATOM   8352  C  CA  . GLN D 1 219 ? 7.836   -10.500 -51.944 1.00 9.31  ? 219 GLN D CA  1 
ATOM   8353  C  C   . GLN D 1 219 ? 7.349   -9.551  -53.073 1.00 8.71  ? 219 GLN D C   1 
ATOM   8354  O  O   . GLN D 1 219 ? 7.934   -8.417  -53.159 1.00 8.88  ? 219 GLN D O   1 
ATOM   8355  C  CB  . GLN D 1 219 ? 8.721   -11.556 -52.577 1.00 12.58 ? 219 GLN D CB  1 
ATOM   8356  C  CG  . GLN D 1 219 ? 10.124  -10.931 -53.143 1.00 16.25 ? 219 GLN D CG  1 
ATOM   8357  C  CD  . GLN D 1 219 ? 10.053  -10.221 -54.458 1.00 19.56 ? 219 GLN D CD  1 
ATOM   8358  O  OE1 . GLN D 1 219 ? 9.251   -10.605 -55.324 1.00 21.79 ? 219 GLN D OE1 1 
ATOM   8359  N  NE2 . GLN D 1 219 ? 10.779  -9.096  -54.545 1.00 20.69 ? 219 GLN D NE2 1 
ATOM   8360  N  N   . GLU D 1 220 ? 6.303   -9.870  -53.801 1.00 8.10  ? 220 GLU D N   1 
ATOM   8361  C  CA  . GLU D 1 220 ? 5.818   -8.997  -54.877 1.00 9.28  ? 220 GLU D CA  1 
ATOM   8362  C  C   . GLU D 1 220 ? 5.199   -7.745  -54.250 1.00 9.73  ? 220 GLU D C   1 
ATOM   8363  O  O   . GLU D 1 220 ? 5.418   -6.625  -54.790 1.00 10.36 ? 220 GLU D O   1 
ATOM   8364  C  CB  . GLU D 1 220 ? 4.746   -9.704  -55.692 1.00 9.53  ? 220 GLU D CB  1 
ATOM   8365  C  CG  . GLU D 1 220 ? 5.481   -10.844 -56.547 1.00 11.72 ? 220 GLU D CG  1 
ATOM   8366  C  CD  . GLU D 1 220 ? 5.695   -12.155 -55.813 1.00 18.43 ? 220 GLU D CD  1 
ATOM   8367  O  OE1 . GLU D 1 220 ? 5.258   -12.373 -54.702 1.00 16.54 ? 220 GLU D OE1 1 
ATOM   8368  O  OE2 . GLU D 1 220 ? 6.336   -13.044 -56.399 1.00 27.04 ? 220 GLU D OE2 1 
ATOM   8369  N  N   . GLN D 1 221 ? 4.554   -7.834  -53.076 1.00 7.56  ? 221 GLN D N   1 
ATOM   8370  C  CA  . GLN D 1 221 ? 4.024   -6.657  -52.418 1.00 9.13  ? 221 GLN D CA  1 
ATOM   8371  C  C   . GLN D 1 221 ? 5.150   -5.867  -51.898 1.00 9.17  ? 221 GLN D C   1 
ATOM   8372  O  O   . GLN D 1 221 ? 5.099   -4.593  -52.069 1.00 9.87  ? 221 GLN D O   1 
ATOM   8373  C  CB  . GLN D 1 221 ? 3.126   -7.120  -51.272 1.00 9.59  ? 221 GLN D CB  1 
ATOM   8374  C  CG  . GLN D 1 221 ? 1.764   -7.706  -51.800 1.00 8.68  ? 221 GLN D CG  1 
ATOM   8375  C  CD  . GLN D 1 221 ? 0.878   -8.072  -50.646 1.00 9.95  ? 221 GLN D CD  1 
ATOM   8376  O  OE1 . GLN D 1 221 ? 1.226   -9.001  -49.832 1.00 10.02 ? 221 GLN D OE1 1 
ATOM   8377  N  NE2 . GLN D 1 221 ? -0.217  -7.358  -50.459 1.00 9.51  ? 221 GLN D NE2 1 
ATOM   8378  N  N   . LEU D 1 222 ? 6.180   -6.456  -51.287 1.00 7.77  ? 222 LEU D N   1 
ATOM   8379  C  CA  . LEU D 1 222 ? 7.347   -5.681  -50.799 1.00 8.44  ? 222 LEU D CA  1 
ATOM   8380  C  C   . LEU D 1 222 ? 8.034   -4.983  -52.006 1.00 8.88  ? 222 LEU D C   1 
ATOM   8381  O  O   . LEU D 1 222 ? 8.431   -3.794  -51.894 1.00 9.63  ? 222 LEU D O   1 
ATOM   8382  C  CB  . LEU D 1 222 ? 8.307   -6.598  -50.076 1.00 9.34  ? 222 LEU D CB  1 
ATOM   8383  C  CG  . LEU D 1 222 ? 7.939   -6.765  -48.657 1.00 12.16 ? 222 LEU D CG  1 
ATOM   8384  C  CD1 . LEU D 1 222 ? 8.589   -8.081  -48.126 1.00 12.57 ? 222 LEU D CD1 1 
ATOM   8385  C  CD2 . LEU D 1 222 ? 8.358   -5.537  -47.764 1.00 12.69 ? 222 LEU D CD2 1 
ATOM   8386  N  N   . LEU D 1 223 ? 8.203   -5.604  -53.139 1.00 8.66  ? 223 LEU D N   1 
ATOM   8387  C  CA  . LEU D 1 223 ? 8.952   -5.012  -54.243 1.00 9.12  ? 223 LEU D CA  1 
ATOM   8388  C  C   . LEU D 1 223 ? 8.100   -3.858  -54.758 1.00 10.19 ? 223 LEU D C   1 
ATOM   8389  O  O   . LEU D 1 223 ? 8.686   -2.832  -55.205 1.00 10.26 ? 223 LEU D O   1 
ATOM   8390  C  CB  . LEU D 1 223 ? 9.169   -6.101  -55.353 1.00 8.64  ? 223 LEU D CB  1 
ATOM   8391  C  CG  . LEU D 1 223 ? 9.871   -5.523  -56.575 1.00 10.84 ? 223 LEU D CG  1 
ATOM   8392  C  CD1 . LEU D 1 223 ? 11.326  -5.095  -56.249 1.00 14.09 ? 223 LEU D CD1 1 
ATOM   8393  C  CD2 . LEU D 1 223 ? 9.955   -6.598  -57.680 1.00 11.13 ? 223 LEU D CD2 1 
ATOM   8394  N  N   . ALA D 1 224 ? 6.778   -4.019  -54.805 1.00 9.75  ? 224 ALA D N   1 
ATOM   8395  C  CA  . ALA D 1 224 ? 5.952   -2.850  -55.265 1.00 10.75 ? 224 ALA D CA  1 
ATOM   8396  C  C   . ALA D 1 224 ? 6.115   -1.679  -54.314 1.00 10.05 ? 224 ALA D C   1 
ATOM   8397  O  O   . ALA D 1 224 ? 6.342   -0.539  -54.773 1.00 12.65 ? 224 ALA D O   1 
ATOM   8398  C  CB  . ALA D 1 224 ? 4.463   -3.265  -55.392 1.00 11.79 ? 224 ALA D CB  1 
ATOM   8399  N  N   . LEU D 1 225 ? 6.019   -1.907  -53.018 1.00 9.13  ? 225 LEU D N   1 
ATOM   8400  C  CA  . LEU D 1 225 ? 6.239   -0.874  -52.028 1.00 11.05 ? 225 LEU D CA  1 
ATOM   8401  C  C   . LEU D 1 225 ? 7.581   -0.217  -52.201 1.00 10.28 ? 225 LEU D C   1 
ATOM   8402  O  O   . LEU D 1 225 ? 7.673   1.022   -52.193 1.00 12.23 ? 225 LEU D O   1 
ATOM   8403  C  CB  . LEU D 1 225 ? 6.004   -1.501  -50.668 1.00 10.09 ? 225 LEU D CB  1 
ATOM   8404  C  CG  . LEU D 1 225 ? 6.205   -0.516  -49.523 1.00 11.81 ? 225 LEU D CG  1 
ATOM   8405  C  CD1 . LEU D 1 225 ? 5.085   0.697   -49.647 1.00 13.03 ? 225 LEU D CD1 1 
ATOM   8406  C  CD2 . LEU D 1 225 ? 6.077   -1.242  -48.202 1.00 12.25 ? 225 LEU D CD2 1 
ATOM   8407  N  N   . GLU D 1 226 ? 8.622   -0.987  -52.437 1.00 9.79  ? 226 GLU D N   1 
ATOM   8408  C  CA  . GLU D 1 226 ? 10.015  -0.486  -52.474 1.00 9.19  ? 226 GLU D CA  1 
ATOM   8409  C  C   . GLU D 1 226 ? 10.340  0.234   -53.768 1.00 11.59 ? 226 GLU D C   1 
ATOM   8410  O  O   . GLU D 1 226 ? 11.430  0.797   -53.834 1.00 13.44 ? 226 GLU D O   1 
ATOM   8411  C  CB  . GLU D 1 226 ? 10.938  -1.754  -52.356 1.00 9.86  ? 226 GLU D CB  1 
ATOM   8412  C  CG  . GLU D 1 226 ? 11.042  -2.353  -50.970 1.00 8.57  ? 226 GLU D CG  1 
ATOM   8413  C  CD  . GLU D 1 226 ? 11.345  -3.860  -51.017 1.00 11.36 ? 226 GLU D CD  1 
ATOM   8414  O  OE1 . GLU D 1 226 ? 11.573  -4.448  -52.078 1.00 11.22 ? 226 GLU D OE1 1 
ATOM   8415  O  OE2 . GLU D 1 226 ? 11.343  -4.426  -49.934 1.00 12.71 ? 226 GLU D OE2 1 
ATOM   8416  N  N   . THR D 1 227 ? 9.510   0.144   -54.789 1.00 8.60  ? 227 THR D N   1 
ATOM   8417  C  CA  . THR D 1 227 ? 9.850   0.681   -56.111 1.00 9.61  ? 227 THR D CA  1 
ATOM   8418  C  C   . THR D 1 227 ? 8.786   1.696   -56.566 1.00 11.51 ? 227 THR D C   1 
ATOM   8419  O  O   . THR D 1 227 ? 8.999   2.316   -57.598 1.00 14.38 ? 227 THR D O   1 
ATOM   8420  C  CB  . THR D 1 227 ? 10.017  -0.412  -57.246 1.00 13.87 ? 227 THR D CB  1 
ATOM   8421  O  OG1 . THR D 1 227 ? 8.814   -1.124  -57.404 1.00 12.21 ? 227 THR D OG1 1 
ATOM   8422  C  CG2 . THR D 1 227 ? 11.184  -1.372  -56.944 1.00 13.94 ? 227 THR D CG2 1 
ATOM   8423  N  N   . ALA D 1 228 ? 7.683   1.847   -55.853 1.00 11.08 ? 228 ALA D N   1 
ATOM   8424  C  CA  . ALA D 1 228 ? 6.544   2.624   -56.378 1.00 11.88 ? 228 ALA D CA  1 
ATOM   8425  C  C   . ALA D 1 228 ? 6.814   4.126   -56.192 1.00 14.44 ? 228 ALA D C   1 
ATOM   8426  O  O   . ALA D 1 228 ? 6.152   4.921   -56.929 1.00 15.58 ? 228 ALA D O   1 
ATOM   8427  C  CB  . ALA D 1 228 ? 5.178   2.195   -55.696 1.00 13.03 ? 228 ALA D CB  1 
ATOM   8428  N  N   . LEU D 1 229 ? 7.544   4.506   -55.142 1.00 11.18 ? 229 LEU D N   1 
ATOM   8429  C  CA  . LEU D 1 229 ? 7.409   5.896   -54.675 1.00 11.65 ? 229 LEU D CA  1 
ATOM   8430  C  C   . LEU D 1 229 ? 8.748   6.660   -54.770 1.00 11.54 ? 229 LEU D C   1 
ATOM   8431  O  O   . LEU D 1 229 ? 9.817   6.086   -54.638 1.00 10.50 ? 229 LEU D O   1 
ATOM   8432  C  CB  . LEU D 1 229 ? 7.001   5.880   -53.207 1.00 10.94 ? 229 LEU D CB  1 
ATOM   8433  C  CG  . LEU D 1 229 ? 5.614   5.180   -52.886 1.00 12.80 ? 229 LEU D CG  1 
ATOM   8434  C  CD1 . LEU D 1 229 ? 5.293   5.134   -51.400 1.00 12.92 ? 229 LEU D CD1 1 
ATOM   8435  C  CD2 . LEU D 1 229 ? 4.430   5.678   -53.759 1.00 16.65 ? 229 LEU D CD2 1 
ATOM   8436  N  N   . TYR D 1 230 ? 8.574   8.013   -54.928 1.00 10.57 ? 230 TYR D N   1 
ATOM   8437  C  CA  . TYR D 1 230 ? 9.680   8.956   -54.830 1.00 11.69 ? 230 TYR D CA  1 
ATOM   8438  C  C   . TYR D 1 230 ? 9.487   9.929   -53.674 1.00 9.67  ? 230 TYR D C   1 
ATOM   8439  O  O   . TYR D 1 230 ? 8.346   10.336  -53.335 1.00 11.54 ? 230 TYR D O   1 
ATOM   8440  C  CB  . TYR D 1 230 ? 9.759   9.772   -56.162 1.00 12.11 ? 230 TYR D CB  1 
ATOM   8441  C  CG  . TYR D 1 230 ? 10.294  8.943   -57.242 1.00 13.77 ? 230 TYR D CG  1 
ATOM   8442  C  CD1 . TYR D 1 230 ? 11.644  8.929   -57.542 1.00 14.95 ? 230 TYR D CD1 1 
ATOM   8443  C  CD2 . TYR D 1 230 ? 9.418   8.035   -57.944 1.00 16.42 ? 230 TYR D CD2 1 
ATOM   8444  C  CE1 . TYR D 1 230 ? 12.174  8.074   -58.560 1.00 21.52 ? 230 TYR D CE1 1 
ATOM   8445  C  CE2 . TYR D 1 230 ? 9.978   7.133   -58.937 1.00 22.27 ? 230 TYR D CE2 1 
ATOM   8446  C  CZ  . TYR D 1 230 ? 11.317  7.171   -59.218 1.00 24.05 ? 230 TYR D CZ  1 
ATOM   8447  O  OH  . TYR D 1 230 ? 11.706  6.295   -60.219 1.00 27.94 ? 230 TYR D OH  1 
ATOM   8448  N  N   . CYS D 1 231 ? 10.620  10.408  -53.136 1.00 11.42 ? 231 CYS D N   1 
ATOM   8449  C  CA  . CYS D 1 231 ? 10.527  11.395  -52.076 1.00 11.76 ? 231 CYS D CA  1 
ATOM   8450  C  C   . CYS D 1 231 ? 10.308  12.818  -52.557 1.00 8.82  ? 231 CYS D C   1 
ATOM   8451  O  O   . CYS D 1 231 ? 9.952   13.676  -51.814 1.00 14.05 ? 231 CYS D O   1 
ATOM   8452  C  CB  . CYS D 1 231 ? 11.857  11.498  -51.299 1.00 11.35 ? 231 CYS D CB  1 
ATOM   8453  S  SG  . CYS D 1 231 ? 12.381  9.979   -50.453 1.00 13.12 ? 231 CYS D SG  1 
ATOM   8454  N  N   . THR D 1 232 ? 10.546  12.948  -53.855 1.00 10.41 ? 232 THR D N   1 
ATOM   8455  C  CA  . THR D 1 232 ? 10.632  14.325  -54.509 1.00 12.69 ? 232 THR D CA  1 
ATOM   8456  C  C   . THR D 1 232 ? 9.351   14.603  -55.275 1.00 13.57 ? 232 THR D C   1 
ATOM   8457  O  O   . THR D 1 232 ? 8.550   13.692  -55.600 1.00 14.15 ? 232 THR D O   1 
ATOM   8458  C  CB  . THR D 1 232 ? 11.881  14.305  -55.480 1.00 15.06 ? 232 THR D CB  1 
ATOM   8459  O  OG1 . THR D 1 232 ? 11.963  12.993  -56.104 1.00 12.87 ? 232 THR D OG1 1 
ATOM   8460  C  CG2 . THR D 1 232 ? 13.104  14.538  -54.658 1.00 14.96 ? 232 THR D CG2 1 
ATOM   8461  N  N   . HIS D 1 233 ? 9.108   15.872  -55.587 1.00 13.91 ? 233 HIS D N   1 
ATOM   8462  C  CA  . HIS D 1 233 ? 8.017   16.238  -56.443 1.00 13.47 ? 233 HIS D CA  1 
ATOM   8463  C  C   . HIS D 1 233 ? 8.265   15.763  -57.857 1.00 13.60 ? 233 HIS D C   1 
ATOM   8464  O  O   . HIS D 1 233 ? 9.411   15.588  -58.285 1.00 13.66 ? 233 HIS D O   1 
ATOM   8465  C  CB  . HIS D 1 233 ? 7.987   17.806  -56.408 1.00 14.19 ? 233 HIS D CB  1 
ATOM   8466  C  CG  . HIS D 1 233 ? 7.422   18.322  -55.115 1.00 19.68 ? 233 HIS D CG  1 
ATOM   8467  N  ND1 . HIS D 1 233 ? 8.116   19.183  -54.276 1.00 27.43 ? 233 HIS D ND1 1 
ATOM   8468  C  CD2 . HIS D 1 233 ? 6.231   18.076  -54.505 1.00 23.18 ? 233 HIS D CD2 1 
ATOM   8469  C  CE1 . HIS D 1 233 ? 7.385   19.420  -53.193 1.00 29.02 ? 233 HIS D CE1 1 
ATOM   8470  N  NE2 . HIS D 1 233 ? 6.240   18.763  -53.308 1.00 26.13 ? 233 HIS D NE2 1 
ATOM   8471  N  N   A MET D 1 234 ? 7.203   15.583  -58.652 0.50 16.50 ? 234 MET D N   1 
ATOM   8472  N  N   B MET D 1 234 ? 7.156   15.667  -58.574 0.50 16.63 ? 234 MET D N   1 
ATOM   8473  C  CA  A MET D 1 234 ? 7.354   15.094  -60.049 0.50 17.89 ? 234 MET D CA  1 
ATOM   8474  C  CA  B MET D 1 234 ? 7.127   15.132  -59.915 0.50 18.09 ? 234 MET D CA  1 
ATOM   8475  C  C   A MET D 1 234 ? 8.353   15.964  -60.802 0.50 18.35 ? 234 MET D C   1 
ATOM   8476  C  C   B MET D 1 234 ? 8.052   15.802  -60.900 0.50 19.73 ? 234 MET D C   1 
ATOM   8477  O  O   A MET D 1 234 ? 9.231   15.483  -61.539 0.50 16.00 ? 234 MET D O   1 
ATOM   8478  O  O   B MET D 1 234 ? 8.503   15.161  -61.840 0.50 21.40 ? 234 MET D O   1 
ATOM   8479  C  CB  A MET D 1 234 ? 5.992   15.076  -60.761 0.50 19.47 ? 234 MET D CB  1 
ATOM   8480  C  CB  B MET D 1 234 ? 5.715   15.205  -60.426 0.50 19.39 ? 234 MET D CB  1 
ATOM   8481  C  CG  A MET D 1 234 ? 5.990   15.294  -62.297 0.50 19.51 ? 234 MET D CG  1 
ATOM   8482  C  CG  B MET D 1 234 ? 5.533   14.344  -61.632 0.50 20.24 ? 234 MET D CG  1 
ATOM   8483  S  SD  A MET D 1 234 ? 4.375   14.948  -63.031 0.50 26.57 ? 234 MET D SD  1 
ATOM   8484  S  SD  B MET D 1 234 ? 3.777   14.441  -61.943 0.50 22.09 ? 234 MET D SD  1 
ATOM   8485  C  CE  A MET D 1 234 ? 4.253   13.172  -62.788 0.50 22.36 ? 234 MET D CE  1 
ATOM   8486  C  CE  B MET D 1 234 ? 3.602   16.162  -61.660 0.50 16.93 ? 234 MET D CE  1 
ATOM   8487  N  N   A ASP D 1 235 ? 8.221   17.272  -60.588 0.50 17.27 ? 235 ASP D N   1 
ATOM   8488  N  N   B ASP D 1 235 ? 8.348   17.094  -60.647 0.50 19.37 ? 235 ASP D N   1 
ATOM   8489  C  CA  A ASP D 1 235 ? 9.072   18.185  -61.312 0.50 18.98 ? 235 ASP D CA  1 
ATOM   8490  C  CA  B ASP D 1 235 ? 9.209   17.931  -61.502 0.50 19.86 ? 235 ASP D CA  1 
ATOM   8491  C  C   A ASP D 1 235 ? 10.494  18.404  -60.801 0.50 18.44 ? 235 ASP D C   1 
ATOM   8492  C  C   B ASP D 1 235 ? 10.625  18.190  -60.987 0.50 19.18 ? 235 ASP D C   1 
ATOM   8493  O  O   A ASP D 1 235 ? 11.166  19.279  -61.315 0.50 19.89 ? 235 ASP D O   1 
ATOM   8494  O  O   B ASP D 1 235 ? 11.415  18.889  -61.636 0.50 18.27 ? 235 ASP D O   1 
ATOM   8495  C  CB  A ASP D 1 235 ? 8.316   19.525  -61.542 0.50 19.33 ? 235 ASP D CB  1 
ATOM   8496  C  CB  B ASP D 1 235 ? 8.501   19.281  -61.745 0.50 22.23 ? 235 ASP D CB  1 
ATOM   8497  C  CG  A ASP D 1 235 ? 8.154   20.336  -60.307 0.50 19.76 ? 235 ASP D CG  1 
ATOM   8498  C  CG  B ASP D 1 235 ? 7.376   19.170  -62.745 0.50 22.97 ? 235 ASP D CG  1 
ATOM   8499  O  OD1 A ASP D 1 235 ? 8.582   19.919  -59.201 0.50 19.95 ? 235 ASP D OD1 1 
ATOM   8500  O  OD1 B ASP D 1 235 ? 7.526   18.415  -63.732 0.50 25.79 ? 235 ASP D OD1 1 
ATOM   8501  O  OD2 A ASP D 1 235 ? 7.533   21.422  -60.447 0.50 20.62 ? 235 ASP D OD2 1 
ATOM   8502  O  OD2 B ASP D 1 235 ? 6.365   19.817  -62.531 0.50 28.02 ? 235 ASP D OD2 1 
ATOM   8503  N  N   . ASP D 1 236 ? 10.995  17.593  -59.858 1.00 17.39 ? 236 ASP D N   1 
ATOM   8504  C  CA  . ASP D 1 236 ? 12.298  17.799  -59.306 1.00 17.95 ? 236 ASP D CA  1 
ATOM   8505  C  C   . ASP D 1 236 ? 13.368  17.302  -60.293 1.00 19.79 ? 236 ASP D C   1 
ATOM   8506  O  O   . ASP D 1 236 ? 13.288  16.159  -60.769 1.00 18.96 ? 236 ASP D O   1 
ATOM   8507  C  CB  . ASP D 1 236 ? 12.487  17.036  -57.970 1.00 15.80 ? 236 ASP D CB  1 
ATOM   8508  C  CG  . ASP D 1 236 ? 13.612  17.548  -57.204 1.00 17.66 ? 236 ASP D CG  1 
ATOM   8509  O  OD1 . ASP D 1 236 ? 14.762  17.643  -57.713 1.00 17.56 ? 236 ASP D OD1 1 
ATOM   8510  O  OD2 . ASP D 1 236 ? 13.381  17.762  -56.015 1.00 18.65 ? 236 ASP D OD2 1 
ATOM   8511  N  N   . PRO D 1 237 ? 14.391  18.143  -60.608 1.00 20.75 ? 237 PRO D N   1 
ATOM   8512  C  CA  . PRO D 1 237 ? 15.388  17.683  -61.560 1.00 19.74 ? 237 PRO D CA  1 
ATOM   8513  C  C   . PRO D 1 237 ? 16.338  16.635  -60.975 1.00 19.06 ? 237 PRO D C   1 
ATOM   8514  O  O   . PRO D 1 237 ? 17.131  16.009  -61.717 1.00 20.53 ? 237 PRO D O   1 
ATOM   8515  C  CB  . PRO D 1 237 ? 16.123  19.013  -61.940 1.00 21.11 ? 237 PRO D CB  1 
ATOM   8516  C  CG  . PRO D 1 237 ? 16.057  19.829  -60.692 1.00 22.11 ? 237 PRO D CG  1 
ATOM   8517  C  CD  . PRO D 1 237 ? 14.697  19.483  -60.076 1.00 20.52 ? 237 PRO D CD  1 
ATOM   8518  N  N   A SER D 1 238 ? 16.296  16.443  -59.650 0.50 18.78 ? 238 SER D N   1 
ATOM   8519  N  N   B SER D 1 238 ? 16.187  16.412  -59.669 0.50 18.23 ? 238 SER D N   1 
ATOM   8520  C  CA  A SER D 1 238 ? 17.110  15.419  -59.003 0.50 18.34 ? 238 SER D CA  1 
ATOM   8521  C  CA  B SER D 1 238 ? 17.054  15.537  -58.926 0.50 17.26 ? 238 SER D CA  1 
ATOM   8522  C  C   A SER D 1 238 ? 16.159  14.492  -58.263 0.50 15.94 ? 238 SER D C   1 
ATOM   8523  C  C   B SER D 1 238 ? 16.187  14.473  -58.216 0.50 15.21 ? 238 SER D C   1 
ATOM   8524  O  O   A SER D 1 238 ? 15.937  14.640  -57.104 0.50 16.06 ? 238 SER D O   1 
ATOM   8525  O  O   B SER D 1 238 ? 16.096  14.477  -57.026 0.50 15.74 ? 238 SER D O   1 
ATOM   8526  C  CB  A SER D 1 238 ? 18.124  15.993  -58.005 0.50 19.44 ? 238 SER D CB  1 
ATOM   8527  C  CB  B SER D 1 238 ? 17.911  16.356  -57.921 0.50 18.65 ? 238 SER D CB  1 
ATOM   8528  O  OG  A SER D 1 238 ? 19.039  15.005  -57.631 0.50 22.34 ? 238 SER D OG  1 
ATOM   8529  O  OG  B SER D 1 238 ? 18.953  17.071  -58.621 0.50 16.59 ? 238 SER D OG  1 
ATOM   8530  N  N   . PRO D 1 239 ? 15.557  13.555  -59.000 1.00 16.58 ? 239 PRO D N   1 
ATOM   8531  C  CA  . PRO D 1 239 ? 14.673  12.602  -58.297 1.00 16.16 ? 239 PRO D CA  1 
ATOM   8532  C  C   . PRO D 1 239 ? 15.341  11.735  -57.258 1.00 14.47 ? 239 PRO D C   1 
ATOM   8533  O  O   . PRO D 1 239 ? 16.479  11.291  -57.425 1.00 17.57 ? 239 PRO D O   1 
ATOM   8534  C  CB  . PRO D 1 239 ? 14.066  11.746  -59.424 1.00 16.03 ? 239 PRO D CB  1 
ATOM   8535  C  CG  . PRO D 1 239 ? 14.485  12.312  -60.725 1.00 19.67 ? 239 PRO D CG  1 
ATOM   8536  C  CD  . PRO D 1 239 ? 15.668  13.254  -60.448 1.00 18.62 ? 239 PRO D CD  1 
ATOM   8537  N  N   . ARG D 1 240 ? 14.584  11.431  -56.198 1.00 14.16 ? 240 ARG D N   1 
ATOM   8538  C  CA  . ARG D 1 240 ? 15.158  10.505  -55.163 1.00 13.73 ? 240 ARG D CA  1 
ATOM   8539  C  C   . ARG D 1 240 ? 14.085  9.406   -54.864 1.00 12.97 ? 240 ARG D C   1 
ATOM   8540  O  O   . ARG D 1 240 ? 12.929  9.765   -54.509 1.00 12.02 ? 240 ARG D O   1 
ATOM   8541  C  CB  . ARG D 1 240 ? 15.418  11.240  -53.862 1.00 12.14 ? 240 ARG D CB  1 
ATOM   8542  C  CG  . ARG D 1 240 ? 16.699  12.181  -54.000 1.00 17.85 ? 240 ARG D CG  1 
ATOM   8543  C  CD  . ARG D 1 240 ? 16.914  12.884  -52.646 1.00 20.67 ? 240 ARG D CD  1 
ATOM   8544  N  NE  . ARG D 1 240 ? 15.890  13.906  -52.398 1.00 19.79 ? 240 ARG D NE  1 
ATOM   8545  C  CZ  . ARG D 1 240 ? 14.968  13.868  -51.435 1.00 22.50 ? 240 ARG D CZ  1 
ATOM   8546  N  NH1 . ARG D 1 240 ? 14.901  12.847  -50.587 1.00 15.33 ? 240 ARG D NH1 1 
ATOM   8547  N  NH2 . ARG D 1 240 ? 14.103  14.869  -51.321 1.00 23.12 ? 240 ARG D NH2 1 
ATOM   8548  N  N   A GLU D 1 241 ? 14.500  8.144   -55.008 0.50 12.38 ? 241 GLU D N   1 
ATOM   8549  N  N   B GLU D 1 241 ? 14.437  8.133   -55.058 0.50 11.70 ? 241 GLU D N   1 
ATOM   8550  C  CA  A GLU D 1 241 ? 13.666  7.007   -54.587 0.50 13.36 ? 241 GLU D CA  1 
ATOM   8551  C  CA  B GLU D 1 241 ? 13.487  7.079   -54.671 0.50 11.85 ? 241 GLU D CA  1 
ATOM   8552  C  C   A GLU D 1 241 ? 13.295  7.001   -53.114 0.50 11.59 ? 241 GLU D C   1 
ATOM   8553  C  C   B GLU D 1 241 ? 13.327  6.933   -53.185 0.50 10.07 ? 241 GLU D C   1 
ATOM   8554  O  O   A GLU D 1 241 ? 14.097  7.330   -52.228 0.50 11.01 ? 241 GLU D O   1 
ATOM   8555  O  O   B GLU D 1 241 ? 14.349  7.051   -52.383 0.50 8.80  ? 241 GLU D O   1 
ATOM   8556  C  CB  A GLU D 1 241 ? 14.361  5.711   -54.945 0.50 12.70 ? 241 GLU D CB  1 
ATOM   8557  C  CB  B GLU D 1 241 ? 13.929  5.725   -55.172 0.50 10.95 ? 241 GLU D CB  1 
ATOM   8558  C  CG  A GLU D 1 241 ? 14.787  5.692   -56.485 0.50 17.15 ? 241 GLU D CG  1 
ATOM   8559  C  CG  B GLU D 1 241 ? 14.156  5.593   -56.719 0.50 13.33 ? 241 GLU D CG  1 
ATOM   8560  C  CD  A GLU D 1 241 ? 15.017  4.318   -57.119 0.50 18.91 ? 241 GLU D CD  1 
ATOM   8561  C  CD  B GLU D 1 241 ? 15.068  4.420   -57.076 0.50 16.39 ? 241 GLU D CD  1 
ATOM   8562  O  OE1 A GLU D 1 241 ? 15.244  3.299   -56.391 0.50 21.39 ? 241 GLU D OE1 1 
ATOM   8563  O  OE1 B GLU D 1 241 ? 14.557  3.380   -57.522 0.50 19.79 ? 241 GLU D OE1 1 
ATOM   8564  O  OE2 A GLU D 1 241 ? 14.996  4.266   -58.362 0.50 25.47 ? 241 GLU D OE2 1 
ATOM   8565  O  OE2 B GLU D 1 241 ? 16.287  4.448   -56.783 0.50 16.57 ? 241 GLU D OE2 1 
ATOM   8566  N  N   . MET D 1 242 ? 12.037  6.659   -52.829 1.00 9.79  ? 242 MET D N   1 
ATOM   8567  C  CA  . MET D 1 242 ? 11.617  6.488   -51.424 1.00 9.80  ? 242 MET D CA  1 
ATOM   8568  C  C   . MET D 1 242 ? 11.916  5.046   -50.987 1.00 9.35  ? 242 MET D C   1 
ATOM   8569  O  O   . MET D 1 242 ? 11.125  4.154   -51.139 1.00 10.71 ? 242 MET D O   1 
ATOM   8570  C  CB  . MET D 1 242 ? 10.155  6.885   -51.207 1.00 9.30  ? 242 MET D CB  1 
ATOM   8571  C  CG  . MET D 1 242 ? 9.861   6.966   -49.693 1.00 10.47 ? 242 MET D CG  1 
ATOM   8572  S  SD  . MET D 1 242 ? 8.114   7.245   -49.411 1.00 9.62  ? 242 MET D SD  1 
ATOM   8573  C  CE  . MET D 1 242 ? 8.017   8.975   -50.024 1.00 11.17 ? 242 MET D CE  1 
ATOM   8574  N  N   . ILE D 1 243 ? 13.146  4.847   -50.529 1.00 7.66  ? 243 ILE D N   1 
ATOM   8575  C  CA  . ILE D 1 243 ? 13.728  3.574   -50.137 1.00 8.98  ? 243 ILE D CA  1 
ATOM   8576  C  C   . ILE D 1 243 ? 14.491  3.805   -48.794 1.00 8.11  ? 243 ILE D C   1 
ATOM   8577  O  O   . ILE D 1 243 ? 14.965  4.906   -48.523 1.00 8.82  ? 243 ILE D O   1 
ATOM   8578  C  CB  . ILE D 1 243 ? 14.709  2.926   -51.194 1.00 9.92  ? 243 ILE D CB  1 
ATOM   8579  C  CG1 . ILE D 1 243 ? 15.829  3.936   -51.549 1.00 10.51 ? 243 ILE D CG1 1 
ATOM   8580  C  CG2 . ILE D 1 243 ? 13.872  2.435   -52.407 1.00 13.73 ? 243 ILE D CG2 1 
ATOM   8581  C  CD1 . ILE D 1 243 ? 16.904  3.341   -52.486 1.00 13.84 ? 243 ILE D CD1 1 
ATOM   8582  N  N   . ASN D 1 244 ? 14.586  2.679   -48.080 1.00 7.39  ? 244 ASN D N   1 
ATOM   8583  C  CA  . ASN D 1 244 ? 15.389  2.679   -46.864 1.00 7.16  ? 244 ASN D CA  1 
ATOM   8584  C  C   . ASN D 1 244 ? 15.010  3.807   -45.911 1.00 7.77  ? 244 ASN D C   1 
ATOM   8585  O  O   . ASN D 1 244 ? 15.844  4.469   -45.270 1.00 7.78  ? 244 ASN D O   1 
ATOM   8586  C  CB  . ASN D 1 244 ? 16.890  2.779   -47.185 1.00 7.40  ? 244 ASN D CB  1 
ATOM   8587  C  CG  . ASN D 1 244 ? 17.301  1.767   -48.117 1.00 9.40  ? 244 ASN D CG  1 
ATOM   8588  O  OD1 . ASN D 1 244 ? 16.901  0.576   -48.067 1.00 10.65 ? 244 ASN D OD1 1 
ATOM   8589  N  ND2 . ASN D 1 244 ? 18.133  2.222   -49.099 1.00 12.81 ? 244 ASN D ND2 1 
ATOM   8590  N  N   . ASN D 1 245 ? 13.691  3.978   -45.751 1.00 6.25  ? 245 ASN D N   1 
ATOM   8591  C  CA  . ASN D 1 245 ? 13.126  5.066   -44.948 1.00 6.27  ? 245 ASN D CA  1 
ATOM   8592  C  C   . ASN D 1 245 ? 12.847  4.603   -43.507 1.00 6.42  ? 245 ASN D C   1 
ATOM   8593  O  O   . ASN D 1 245 ? 11.729  4.705   -43.009 1.00 8.05  ? 245 ASN D O   1 
ATOM   8594  C  CB  . ASN D 1 245 ? 11.830  5.645   -45.611 1.00 6.75  ? 245 ASN D CB  1 
ATOM   8595  C  CG  . ASN D 1 245 ? 10.723  4.688   -45.783 1.00 8.36  ? 245 ASN D CG  1 
ATOM   8596  O  OD1 . ASN D 1 245 ? 10.920  3.478   -45.756 1.00 7.66  ? 245 ASN D OD1 1 
ATOM   8597  N  ND2 . ASN D 1 245 ? 9.504   5.171   -45.978 1.00 8.30  ? 245 ASN D ND2 1 
ATOM   8598  N  N   . PHE D 1 246 ? 13.901  4.025   -42.857 1.00 6.48  ? 246 PHE D N   1 
ATOM   8599  C  CA  . PHE D 1 246 ? 13.861  3.639   -41.471 1.00 5.37  ? 246 PHE D CA  1 
ATOM   8600  C  C   . PHE D 1 246 ? 15.057  4.259   -40.799 1.00 6.95  ? 246 PHE D C   1 
ATOM   8601  O  O   . PHE D 1 246 ? 16.120  4.379   -41.408 1.00 7.69  ? 246 PHE D O   1 
ATOM   8602  C  CB  . PHE D 1 246 ? 13.893  2.044   -41.421 1.00 6.67  ? 246 PHE D CB  1 
ATOM   8603  C  CG  . PHE D 1 246 ? 15.138  1.359   -42.023 1.00 5.53  ? 246 PHE D CG  1 
ATOM   8604  C  CD1 . PHE D 1 246 ? 16.215  1.034   -41.155 1.00 7.70  ? 246 PHE D CD1 1 
ATOM   8605  C  CD2 . PHE D 1 246 ? 15.264  1.127   -43.383 1.00 6.39  ? 246 PHE D CD2 1 
ATOM   8606  C  CE1 . PHE D 1 246 ? 17.370  0.462   -41.685 1.00 8.93  ? 246 PHE D CE1 1 
ATOM   8607  C  CE2 . PHE D 1 246 ? 16.389  0.527   -43.926 1.00 7.12  ? 246 PHE D CE2 1 
ATOM   8608  C  CZ  . PHE D 1 246 ? 17.457  0.256   -43.049 1.00 7.77  ? 246 PHE D CZ  1 
ATOM   8609  N  N   . ARG D 1 247 ? 14.867  4.518   -39.516 1.00 6.68  ? 247 ARG D N   1 
ATOM   8610  C  CA  . ARG D 1 247 ? 15.980  4.989   -38.685 1.00 6.94  ? 247 ARG D CA  1 
ATOM   8611  C  C   . ARG D 1 247 ? 16.706  3.872   -38.020 1.00 8.58  ? 247 ARG D C   1 
ATOM   8612  O  O   . ARG D 1 247 ? 16.062  2.887   -37.693 1.00 7.96  ? 247 ARG D O   1 
ATOM   8613  C  CB  . ARG D 1 247 ? 15.378  5.932   -37.607 1.00 7.19  ? 247 ARG D CB  1 
ATOM   8614  C  CG  . ARG D 1 247 ? 16.347  6.856   -36.822 1.00 7.06  ? 247 ARG D CG  1 
ATOM   8615  C  CD  . ARG D 1 247 ? 15.693  7.508   -35.692 1.00 7.89  ? 247 ARG D CD  1 
ATOM   8616  N  NE  . ARG D 1 247 ? 16.567  8.603   -35.150 1.00 9.20  ? 247 ARG D NE  1 
ATOM   8617  C  CZ  . ARG D 1 247 ? 16.247  9.317   -34.068 1.00 8.65  ? 247 ARG D CZ  1 
ATOM   8618  N  NH1 . ARG D 1 247 ? 15.116  9.054   -33.355 1.00 9.47  ? 247 ARG D NH1 1 
ATOM   8619  N  NH2 . ARG D 1 247 ? 17.054  10.325  -33.696 1.00 7.99  ? 247 ARG D NH2 1 
ATOM   8620  N  N   . GLN D 1 248 ? 18.029  4.026   -37.825 1.00 7.01  ? 248 GLN D N   1 
ATOM   8621  C  CA  . GLN D 1 248 ? 18.737  2.977   -37.042 1.00 7.15  ? 248 GLN D CA  1 
ATOM   8622  C  C   . GLN D 1 248 ? 18.248  2.946   -35.615 1.00 7.56  ? 248 GLN D C   1 
ATOM   8623  O  O   . GLN D 1 248 ? 17.688  3.919   -35.068 1.00 8.12  ? 248 GLN D O   1 
ATOM   8624  C  CB  . GLN D 1 248 ? 20.255  3.355   -37.001 1.00 7.35  ? 248 GLN D CB  1 
ATOM   8625  C  CG  . GLN D 1 248 ? 20.950  3.355   -38.370 1.00 7.52  ? 248 GLN D CG  1 
ATOM   8626  C  CD  . GLN D 1 248 ? 20.936  1.959   -38.999 1.00 8.48  ? 248 GLN D CD  1 
ATOM   8627  O  OE1 . GLN D 1 248 ? 20.011  1.647   -39.783 1.00 8.52  ? 248 GLN D OE1 1 
ATOM   8628  N  NE2 . GLN D 1 248 ? 21.954  1.198   -38.727 1.00 9.76  ? 248 GLN D NE2 1 
ATOM   8629  N  N   . VAL D 1 249 ? 18.456  1.809   -34.976 1.00 7.17  ? 249 VAL D N   1 
ATOM   8630  C  CA  . VAL D 1 249 ? 18.078  1.694   -33.548 1.00 7.83  ? 249 VAL D CA  1 
ATOM   8631  C  C   . VAL D 1 249 ? 18.977  2.586   -32.670 1.00 9.11  ? 249 VAL D C   1 
ATOM   8632  O  O   . VAL D 1 249 ? 20.093  2.927   -33.058 1.00 8.33  ? 249 VAL D O   1 
ATOM   8633  C  CB  . VAL D 1 249 ? 18.092  0.209   -33.038 1.00 8.27  ? 249 VAL D CB  1 
ATOM   8634  C  CG1 . VAL D 1 249 ? 17.054  -0.644  -33.748 1.00 9.37  ? 249 VAL D CG1 1 
ATOM   8635  C  CG2 . VAL D 1 249 ? 19.550  -0.400  -33.166 1.00 9.16  ? 249 VAL D CG2 1 
ATOM   8636  N  N   . GLN D 1 250 ? 18.384  2.938   -31.563 1.00 8.10  ? 250 GLN D N   1 
ATOM   8637  C  CA  . GLN D 1 250 ? 18.965  3.949   -30.642 1.00 9.47  ? 250 GLN D CA  1 
ATOM   8638  C  C   . GLN D 1 250 ? 19.443  3.395   -29.321 1.00 9.28  ? 250 GLN D C   1 
ATOM   8639  O  O   . GLN D 1 250 ? 19.031  2.325   -28.886 1.00 10.03 ? 250 GLN D O   1 
ATOM   8640  C  CB  . GLN D 1 250 ? 17.800  4.988   -30.291 1.00 9.19  ? 250 GLN D CB  1 
ATOM   8641  C  CG  . GLN D 1 250 ? 17.158  5.675   -31.564 1.00 9.49  ? 250 GLN D CG  1 
ATOM   8642  C  CD  . GLN D 1 250 ? 18.116  6.527   -32.262 1.00 8.18  ? 250 GLN D CD  1 
ATOM   8643  O  OE1 . GLN D 1 250 ? 18.574  7.567   -31.705 1.00 10.42 ? 250 GLN D OE1 1 
ATOM   8644  N  NE2 . GLN D 1 250 ? 18.347  6.258   -33.545 1.00 8.64  ? 250 GLN D NE2 1 
ATOM   8645  N  N   . LYS D 1 251 ? 20.311  4.151   -28.664 1.00 10.08 ? 251 LYS D N   1 
ATOM   8646  C  CA  . LYS D 1 251 ? 20.720  3.753   -27.289 1.00 11.39 ? 251 LYS D CA  1 
ATOM   8647  C  C   . LYS D 1 251 ? 19.493  3.660   -26.381 1.00 10.80 ? 251 LYS D C   1 
ATOM   8648  O  O   . LYS D 1 251 ? 18.555  4.445   -26.434 1.00 11.72 ? 251 LYS D O   1 
ATOM   8649  C  CB  . LYS D 1 251 ? 21.668  4.816   -26.732 1.00 13.59 ? 251 LYS D CB  1 
ATOM   8650  C  CG  . LYS D 1 251 ? 23.088  4.850   -27.400 1.00 15.21 ? 251 LYS D CG  1 
ATOM   8651  C  CD  . LYS D 1 251 ? 23.934  3.736   -26.849 1.00 15.19 ? 251 LYS D CD  1 
ATOM   8652  C  CE  . LYS D 1 251 ? 25.404  3.797   -27.245 1.00 14.12 ? 251 LYS D CE  1 
ATOM   8653  N  NZ  . LYS D 1 251 ? 25.452  3.666   -28.787 1.00 12.07 ? 251 LYS D NZ  1 
ATOM   8654  N  N   . PHE D 1 252 ? 19.576  2.715   -25.451 1.00 14.28 ? 252 PHE D N   1 
ATOM   8655  C  CA  . PHE D 1 252 ? 18.471  2.622   -24.492 1.00 14.98 ? 252 PHE D CA  1 
ATOM   8656  C  C   . PHE D 1 252 ? 18.281  3.744   -23.449 1.00 19.02 ? 252 PHE D C   1 
ATOM   8657  O  O   . PHE D 1 252 ? 17.183  3.923   -22.905 1.00 18.31 ? 252 PHE D O   1 
ATOM   8658  C  CB  . PHE D 1 252 ? 18.592  1.235   -23.805 1.00 18.50 ? 252 PHE D CB  1 
ATOM   8659  C  CG  . PHE D 1 252 ? 17.940  0.171   -24.649 1.00 21.15 ? 252 PHE D CG  1 
ATOM   8660  C  CD1 . PHE D 1 252 ? 16.603  -0.091  -24.430 1.00 25.72 ? 252 PHE D CD1 1 
ATOM   8661  C  CD2 . PHE D 1 252 ? 18.628  -0.473  -25.713 1.00 23.92 ? 252 PHE D CD2 1 
ATOM   8662  C  CE1 . PHE D 1 252 ? 15.952  -1.029  -25.210 1.00 23.29 ? 252 PHE D CE1 1 
ATOM   8663  C  CE2 . PHE D 1 252 ? 17.933  -1.491  -26.570 1.00 20.53 ? 252 PHE D CE2 1 
ATOM   8664  C  CZ  . PHE D 1 252 ? 16.619  -1.651  -26.313 1.00 21.20 ? 252 PHE D CZ  1 
ATOM   8665  N  N   . ASP D 1 253 ? 19.352  4.490   -23.091 1.00 19.21 ? 253 ASP D N   1 
ATOM   8666  C  CA  . ASP D 1 253 ? 19.229  5.588   -22.068 1.00 20.43 ? 253 ASP D CA  1 
ATOM   8667  C  C   . ASP D 1 253 ? 18.602  5.021   -20.777 1.00 21.99 ? 253 ASP D C   1 
ATOM   8668  O  O   . ASP D 1 253 ? 17.813  5.693   -20.152 1.00 24.96 ? 253 ASP D O   1 
ATOM   8669  C  CB  . ASP D 1 253 ? 18.393  6.764   -22.589 1.00 22.42 ? 253 ASP D CB  1 
ATOM   8670  C  CG  . ASP D 1 253 ? 19.046  7.400   -23.817 1.00 23.34 ? 253 ASP D CG  1 
ATOM   8671  O  OD1 . ASP D 1 253 ? 20.287  7.308   -23.985 1.00 25.57 ? 253 ASP D OD1 1 
ATOM   8672  O  OD2 . ASP D 1 253 ? 18.310  8.022   -24.580 1.00 20.67 ? 253 ASP D OD2 1 
ATOM   8673  N  N   . GLU D 1 254 ? 18.969  3.790   -20.415 1.00 21.50 ? 254 GLU D N   1 
ATOM   8674  C  CA  . GLU D 1 254 ? 18.539  3.192   -19.132 1.00 23.28 ? 254 GLU D CA  1 
ATOM   8675  C  C   . GLU D 1 254 ? 17.087  2.625   -19.113 1.00 21.99 ? 254 GLU D C   1 
ATOM   8676  O  O   . GLU D 1 254 ? 16.583  2.148   -18.063 1.00 22.42 ? 254 GLU D O   1 
ATOM   8677  C  CB  . GLU D 1 254 ? 18.733  4.176   -17.930 1.00 24.04 ? 254 GLU D CB  1 
ATOM   8678  C  CG  . GLU D 1 254 ? 20.235  4.364   -17.532 1.00 31.23 ? 254 GLU D CG  1 
ATOM   8679  C  CD  . GLU D 1 254 ? 20.425  4.260   -16.028 1.00 43.32 ? 254 GLU D CD  1 
ATOM   8680  O  OE1 . GLU D 1 254 ? 20.412  3.106   -15.456 1.00 47.39 ? 254 GLU D OE1 1 
ATOM   8681  O  OE2 . GLU D 1 254 ? 20.600  5.328   -15.404 1.00 43.63 ? 254 GLU D OE2 1 
ATOM   8682  N  N   . ARG D 1 255 ? 16.386  2.713   -20.239 1.00 18.31 ? 255 ARG D N   1 
ATOM   8683  C  CA  . ARG D 1 255 ? 15.016  2.173   -20.372 1.00 16.01 ? 255 ARG D CA  1 
ATOM   8684  C  C   . ARG D 1 255 ? 14.985  0.628   -20.283 1.00 17.26 ? 255 ARG D C   1 
ATOM   8685  O  O   . ARG D 1 255 ? 15.933  -0.135  -20.757 1.00 19.49 ? 255 ARG D O   1 
ATOM   8686  C  CB  . ARG D 1 255 ? 14.395  2.632   -21.750 1.00 16.50 ? 255 ARG D CB  1 
ATOM   8687  C  CG  . ARG D 1 255 ? 14.161  4.157   -21.795 1.00 15.99 ? 255 ARG D CG  1 
ATOM   8688  C  CD  . ARG D 1 255 ? 13.617  4.484   -23.247 1.00 15.34 ? 255 ARG D CD  1 
ATOM   8689  N  NE  . ARG D 1 255 ? 14.700  4.443   -24.202 1.00 17.01 ? 255 ARG D NE  1 
ATOM   8690  C  CZ  . ARG D 1 255 ? 14.583  4.841   -25.477 1.00 18.24 ? 255 ARG D CZ  1 
ATOM   8691  N  NH1 . ARG D 1 255 ? 13.348  5.166   -25.965 1.00 13.03 ? 255 ARG D NH1 1 
ATOM   8692  N  NH2 . ARG D 1 255 ? 15.701  4.878   -26.239 1.00 12.28 ? 255 ARG D NH2 1 
ATOM   8693  N  N   . LEU D 1 256 ? 13.885  0.129   -19.716 1.00 16.00 ? 256 LEU D N   1 
ATOM   8694  C  CA  . LEU D 1 256 ? 13.463  -1.220  -19.994 1.00 14.42 ? 256 LEU D CA  1 
ATOM   8695  C  C   . LEU D 1 256 ? 12.263  -1.237  -20.983 1.00 14.86 ? 256 LEU D C   1 
ATOM   8696  O  O   . LEU D 1 256 ? 11.624  -0.216  -21.282 1.00 15.80 ? 256 LEU D O   1 
ATOM   8697  C  CB  . LEU D 1 256 ? 13.061  -1.927  -18.719 1.00 16.19 ? 256 LEU D CB  1 
ATOM   8698  C  CG  . LEU D 1 256 ? 14.132  -1.956  -17.687 1.00 17.02 ? 256 LEU D CG  1 
ATOM   8699  C  CD1 . LEU D 1 256 ? 13.566  -2.598  -16.397 1.00 21.13 ? 256 LEU D CD1 1 
ATOM   8700  C  CD2 . LEU D 1 256 ? 15.379  -2.735  -18.268 1.00 21.10 ? 256 LEU D CD2 1 
ATOM   8701  N  N   . VAL D 1 257 ? 12.079  -2.374  -21.600 1.00 12.19 ? 257 VAL D N   1 
ATOM   8702  C  CA  . VAL D 1 257 ? 10.903  -2.638  -22.453 1.00 12.64 ? 257 VAL D CA  1 
ATOM   8703  C  C   . VAL D 1 257 ? 10.038  -3.644  -21.741 1.00 14.35 ? 257 VAL D C   1 
ATOM   8704  O  O   . VAL D 1 257 ? 10.509  -4.709  -21.308 1.00 13.68 ? 257 VAL D O   1 
ATOM   8705  C  CB  . VAL D 1 257 ? 11.227  -3.280  -23.838 1.00 13.79 ? 257 VAL D CB  1 
ATOM   8706  C  CG1 . VAL D 1 257 ? 9.966   -3.597  -24.604 1.00 12.49 ? 257 VAL D CG1 1 
ATOM   8707  C  CG2 . VAL D 1 257 ? 12.050  -2.275  -24.601 1.00 14.14 ? 257 VAL D CG2 1 
ATOM   8708  N  N   . TYR D 1 258 ? 8.786   -3.284  -21.478 1.00 12.13 ? 258 TYR D N   1 
ATOM   8709  C  CA  . TYR D 1 258 ? 7.900   -4.073  -20.627 1.00 12.57 ? 258 TYR D CA  1 
ATOM   8710  C  C   . TYR D 1 258 ? 7.079   -4.955  -21.520 1.00 12.20 ? 258 TYR D C   1 
ATOM   8711  O  O   . TYR D 1 258 ? 6.731   -4.503  -22.648 1.00 12.71 ? 258 TYR D O   1 
ATOM   8712  C  CB  . TYR D 1 258 ? 7.025   -3.155  -19.760 1.00 13.49 ? 258 TYR D CB  1 
ATOM   8713  C  CG  . TYR D 1 258 ? 7.886   -2.342  -18.869 1.00 14.75 ? 258 TYR D CG  1 
ATOM   8714  C  CD1 . TYR D 1 258 ? 8.397   -2.905  -17.666 1.00 15.78 ? 258 TYR D CD1 1 
ATOM   8715  C  CD2 . TYR D 1 258 ? 8.334   -1.048  -19.252 1.00 15.07 ? 258 TYR D CD2 1 
ATOM   8716  C  CE1 . TYR D 1 258 ? 9.315   -2.160  -16.902 1.00 18.77 ? 258 TYR D CE1 1 
ATOM   8717  C  CE2 . TYR D 1 258 ? 9.182   -0.366  -18.526 1.00 17.53 ? 258 TYR D CE2 1 
ATOM   8718  C  CZ  . TYR D 1 258 ? 9.660   -0.864  -17.336 1.00 18.90 ? 258 TYR D CZ  1 
ATOM   8719  O  OH  . TYR D 1 258 ? 10.533  -0.106  -16.594 1.00 23.16 ? 258 TYR D OH  1 
ATOM   8720  N  N   . THR D 1 259 ? 6.863   -6.244  -21.193 1.00 10.65 ? 259 THR D N   1 
ATOM   8721  C  CA  . THR D 1 259 ? 6.177   -7.156  -22.065 1.00 9.22  ? 259 THR D CA  1 
ATOM   8722  C  C   . THR D 1 259 ? 4.876   -7.681  -21.414 1.00 10.97 ? 259 THR D C   1 
ATOM   8723  O  O   . THR D 1 259 ? 4.858   -7.749  -20.163 1.00 11.80 ? 259 THR D O   1 
ATOM   8724  C  CB  . THR D 1 259 ? 7.005   -8.367  -22.485 1.00 10.75 ? 259 THR D CB  1 
ATOM   8725  O  OG1 . THR D 1 259 ? 7.473   -9.010  -21.276 1.00 13.21 ? 259 THR D OG1 1 
ATOM   8726  C  CG2 . THR D 1 259 ? 8.304   -7.841  -23.255 1.00 10.76 ? 259 THR D CG2 1 
ATOM   8727  N  N   . SER D 1 260 ? 3.875   -7.982  -22.210 1.00 11.83 ? 260 SER D N   1 
ATOM   8728  C  CA  . SER D 1 260 ? 2.598   -8.574  -21.671 1.00 11.99 ? 260 SER D CA  1 
ATOM   8729  C  C   . SER D 1 260 ? 2.668   -10.105 -21.663 1.00 14.64 ? 260 SER D C   1 
ATOM   8730  O  O   . SER D 1 260 ? 1.672   -10.714 -21.309 1.00 16.49 ? 260 SER D O   1 
ATOM   8731  C  CB  . SER D 1 260 ? 1.452   -8.139  -22.514 1.00 14.41 ? 260 SER D CB  1 
ATOM   8732  O  OG  . SER D 1 260 ? 1.648   -8.598  -23.854 1.00 14.44 ? 260 SER D OG  1 
ATOM   8733  N  N   . PHE D 1 261 ? 3.812   -10.683 -21.992 1.00 13.81 ? 261 PHE D N   1 
ATOM   8734  C  CA  . PHE D 1 261 ? 3.959   -12.149 -22.136 1.00 16.59 ? 261 PHE D CA  1 
ATOM   8735  C  C   . PHE D 1 261 ? 5.333   -12.459 -21.493 1.00 18.75 ? 261 PHE D C   1 
ATOM   8736  O  O   . PHE D 1 261 ? 6.187   -11.615 -21.299 1.00 16.95 ? 261 PHE D O   1 
ATOM   8737  C  CB  . PHE D 1 261 ? 3.988   -12.592 -23.612 1.00 15.65 ? 261 PHE D CB  1 
ATOM   8738  C  CG  . PHE D 1 261 ? 5.090   -11.882 -24.416 1.00 17.27 ? 261 PHE D CG  1 
ATOM   8739  C  CD1 . PHE D 1 261 ? 6.397   -12.390 -24.520 1.00 17.80 ? 261 PHE D CD1 1 
ATOM   8740  C  CD2 . PHE D 1 261 ? 4.842   -10.621 -25.001 1.00 15.33 ? 261 PHE D CD2 1 
ATOM   8741  C  CE1 . PHE D 1 261 ? 7.471   -11.717 -25.232 1.00 17.30 ? 261 PHE D CE1 1 
ATOM   8742  C  CE2 . PHE D 1 261 ? 5.908   -10.000 -25.724 1.00 13.10 ? 261 PHE D CE2 1 
ATOM   8743  C  CZ  . PHE D 1 261 ? 7.186   -10.470 -25.813 1.00 16.09 ? 261 PHE D CZ  1 
ATOM   8744  N  N   . SER D 1 262 ? 5.517   -13.715 -21.076 1.00 23.83 ? 262 SER D N   1 
ATOM   8745  C  CA  . SER D 1 262 ? 6.840   -14.160 -20.623 1.00 26.26 ? 262 SER D CA  1 
ATOM   8746  C  C   . SER D 1 262 ? 7.476   -15.038 -21.699 1.00 27.03 ? 262 SER D C   1 
ATOM   8747  O  O   . SER D 1 262 ? 6.792   -15.803 -22.368 1.00 29.68 ? 262 SER D O   1 
ATOM   8748  C  CB  . SER D 1 262 ? 6.753   -14.924 -19.319 1.00 28.02 ? 262 SER D CB  1 
ATOM   8749  O  OG  . SER D 1 262 ? 5.886   -14.192 -18.443 1.00 32.26 ? 262 SER D OG  1 
HETATM 8750  ZN ZN  . ZN  E 2 .   ? 22.987  0.758   12.251  1.00 7.22  ? 301 ZN  A ZN  1 
HETATM 8751  O  O18 . E1F F 3 .   ? 22.971  2.569   8.532   1.00 7.10  ? 302 E1F A O18 1 
HETATM 8752  C  C13 . E1F F 3 .   ? 28.370  12.256  9.769   1.00 31.30 ? 302 E1F A C13 1 
HETATM 8753  C  C1  . E1F F 3 .   ? 26.654  5.856   10.547  1.00 14.40 ? 302 E1F A C1  1 
HETATM 8754  C  C2  . E1F F 3 .   ? 25.820  4.104   9.043   1.00 10.92 ? 302 E1F A C2  1 
HETATM 8755  CL CL1 . E1F F 3 .   ? 25.986  3.277   7.625   1.00 12.13 ? 302 E1F A CL1 1 
HETATM 8756  C  C21 . E1F F 3 .   ? 26.717  5.192   9.344   1.00 13.40 ? 302 E1F A C21 1 
HETATM 8757  C  C5  . E1F F 3 .   ? 25.623  5.582   11.446  1.00 15.58 ? 302 E1F A C5  1 
HETATM 8758  C  C4  . E1F F 3 .   ? 24.721  4.469   11.230  1.00 10.45 ? 302 E1F A C4  1 
HETATM 8759  C  C3  . E1F F 3 .   ? 24.817  3.830   9.986   1.00 8.06  ? 302 E1F A C3  1 
HETATM 8760  S  S16 . E1F F 3 .   ? 23.737  2.376   9.833   1.00 9.34  ? 302 E1F A S16 1 
HETATM 8761  N  N19 . E1F F 3 .   ? 22.770  2.335   11.067  1.00 7.79  ? 302 E1F A N19 1 
HETATM 8762  O  O17 . E1F F 3 .   ? 24.695  1.176   9.860   1.00 8.94  ? 302 E1F A O17 1 
HETATM 8763  C  C6  . E1F F 3 .   ? 27.666  6.946   10.713  1.00 18.33 ? 302 E1F A C6  1 
HETATM 8764  O  O12 . E1F F 3 .   ? 27.550  7.551   11.780  1.00 23.70 ? 302 E1F A O12 1 
HETATM 8765  C  C7  . E1F F 3 .   ? 28.665  7.200   9.585   1.00 20.19 ? 302 E1F A C7  1 
HETATM 8766  S  S8  . E1F F 3 .   ? 29.837  8.585   10.055  1.00 29.03 ? 302 E1F A S8  1 
HETATM 8767  C  C9  . E1F F 3 .   ? 28.727  9.932   9.770   1.00 29.36 ? 302 E1F A C9  1 
HETATM 8768  N  N11 . E1F F 3 .   ? 27.471  9.750   9.245   1.00 33.34 ? 302 E1F A N11 1 
HETATM 8769  C  C14 . E1F F 3 .   ? 26.676  10.809  8.958   1.00 29.03 ? 302 E1F A C14 1 
HETATM 8770  C  C15 . E1F F 3 .   ? 27.097  12.092  9.218   1.00 25.99 ? 302 E1F A C15 1 
HETATM 8771  N  N10 . E1F F 3 .   ? 29.172  11.195  10.063  1.00 32.76 ? 302 E1F A N10 1 
HETATM 8772  C  C1  . EDO G 4 .   ? 23.601  5.187   15.533  1.00 19.46 ? 303 EDO A C1  1 
HETATM 8773  O  O1  . EDO G 4 .   ? 23.963  6.533   16.043  1.00 26.28 ? 303 EDO A O1  1 
HETATM 8774  C  C2  . EDO G 4 .   ? 24.804  4.603   14.758  1.00 26.42 ? 303 EDO A C2  1 
HETATM 8775  O  O2  . EDO G 4 .   ? 26.059  4.954   15.364  1.00 23.44 ? 303 EDO A O2  1 
HETATM 8776  C  C1  . EDO H 4 .   ? 27.407  -9.009  31.013  1.00 23.75 ? 304 EDO A C1  1 
HETATM 8777  O  O1  . EDO H 4 .   ? 28.756  -9.384  30.617  1.00 23.89 ? 304 EDO A O1  1 
HETATM 8778  C  C2  . EDO H 4 .   ? 26.443  -8.718  29.832  1.00 22.01 ? 304 EDO A C2  1 
HETATM 8779  O  O2  . EDO H 4 .   ? 26.062  -9.806  28.944  1.00 22.29 ? 304 EDO A O2  1 
HETATM 8780  ZN ZN  . ZN  I 2 .   ? -8.139  3.774   4.888   1.00 5.91  ? 301 ZN  B ZN  1 
HETATM 8781  O  O18 . E1F J 3 .   ? -7.644  5.725   8.471   1.00 5.71  ? 302 E1F B O18 1 
HETATM 8782  C  C13 . E1F J 3 .   ? -9.555  14.543  8.663   1.00 29.85 ? 302 E1F B C13 1 
HETATM 8783  C  C1  . E1F J 3 .   ? -10.553 9.620   6.578   1.00 12.82 ? 302 E1F B C1  1 
HETATM 8784  C  C2  . E1F J 3 .   ? -10.171 7.736   8.010   1.00 11.56 ? 302 E1F B C2  1 
HETATM 8785  CL CL1 . E1F J 3 .   ? -10.437 6.913   9.486   1.00 12.53 ? 302 E1F B CL1 1 
HETATM 8786  C  C21 . E1F J 3 .   ? -10.791 8.986   7.732   1.00 11.40 ? 302 E1F B C21 1 
HETATM 8787  C  C5  . E1F J 3 .   ? -9.691  9.176   5.590   1.00 15.35 ? 302 E1F B C5  1 
HETATM 8788  C  C4  . E1F J 3 .   ? -9.026  7.942   5.817   1.00 13.07 ? 302 E1F B C4  1 
HETATM 8789  C  C3  . E1F J 3 .   ? -9.231  7.285   7.070   1.00 8.69  ? 302 E1F B C3  1 
HETATM 8790  S  S16 . E1F J 3 .   ? -8.471  5.580   7.266   1.00 7.48  ? 302 E1F B S16 1 
HETATM 8791  N  N19 . E1F J 3 .   ? -7.587  5.310   5.939   1.00 8.71  ? 302 E1F B N19 1 
HETATM 8792  O  O17 . E1F J 3 .   ? -9.580  4.653   7.296   1.00 7.84  ? 302 E1F B O17 1 
HETATM 8793  C  C6  . E1F J 3 .   ? -11.269 10.945  6.437   1.00 18.66 ? 302 E1F B C6  1 
HETATM 8794  O  O12 . E1F J 3 .   ? -11.017 11.648  5.467   1.00 24.23 ? 302 E1F B O12 1 
HETATM 8795  C  C7  . E1F J 3 .   ? -12.299 11.318  7.451   1.00 18.14 ? 302 E1F B C7  1 
HETATM 8796  S  S8  . E1F J 3 .   ? -13.052 13.011  7.103   1.00 25.31 ? 302 E1F B S8  1 
HETATM 8797  C  C9  . E1F J 3 .   ? -11.705 14.129  7.583   1.00 32.47 ? 302 E1F B C9  1 
HETATM 8798  N  N11 . E1F J 3 .   ? -11.830 15.453  7.243   1.00 32.30 ? 302 E1F B N11 1 
HETATM 8799  C  C14 . E1F J 3 .   ? -10.849 16.310  7.605   1.00 30.30 ? 302 E1F B C14 1 
HETATM 8800  C  C15 . E1F J 3 .   ? -9.683  15.887  8.301   1.00 33.11 ? 302 E1F B C15 1 
HETATM 8801  N  N10 . E1F J 3 .   ? -10.554 13.690  8.261   1.00 34.74 ? 302 E1F B N10 1 
HETATM 8802  C  C1  . EDO K 4 .   ? -7.962  8.310   1.168   1.00 14.47 ? 303 EDO B C1  1 
HETATM 8803  O  O1  . EDO K 4 .   ? -8.287  9.707   1.139   1.00 26.35 ? 303 EDO B O1  1 
HETATM 8804  C  C2  . EDO K 4 .   ? -9.070  7.603   2.049   1.00 24.99 ? 303 EDO B C2  1 
HETATM 8805  O  O2  . EDO K 4 .   ? -10.466 8.191   2.081   1.00 18.29 ? 303 EDO B O2  1 
HETATM 8806  C  C1  . EDO L 4 .   ? -17.608 -3.696  21.526  1.00 19.29 ? 304 EDO B C1  1 
HETATM 8807  O  O1  . EDO L 4 .   ? -16.447 -3.651  20.587  1.00 15.56 ? 304 EDO B O1  1 
HETATM 8808  C  C2  . EDO L 4 .   ? -17.276 -3.240  22.976  1.00 24.11 ? 304 EDO B C2  1 
HETATM 8809  O  O2  . EDO L 4 .   ? -15.989 -2.577  22.982  1.00 24.84 ? 304 EDO B O2  1 
HETATM 8810  ZN ZN  . ZN  M 2 .   ? 37.573  2.544   -30.951 1.00 12.83 ? 301 ZN  C ZN  1 
HETATM 8811  O  O18 . E1F N 3 .   ? 37.829  4.225   -34.704 1.00 12.74 ? 302 E1F C O18 1 
HETATM 8812  C  C13 . E1F N 3 .   ? 41.196  12.530  -34.207 1.00 33.97 ? 302 E1F C C13 1 
HETATM 8813  C  C1  . E1F N 3 .   ? 41.319  7.616   -32.676 1.00 22.56 ? 302 E1F C C1  1 
HETATM 8814  C  C2  . E1F N 3 .   ? 40.489  5.827   -34.060 1.00 18.95 ? 302 E1F C C2  1 
HETATM 8815  CL CL1 . E1F N 3 .   ? 40.645  4.996   -35.569 1.00 14.88 ? 302 E1F C CL1 1 
HETATM 8816  C  C21 . E1F N 3 .   ? 41.360  6.883   -33.877 1.00 16.27 ? 302 E1F C C21 1 
HETATM 8817  C  C5  . E1F N 3 .   ? 40.371  7.264   -31.720 1.00 19.36 ? 302 E1F C C5  1 
HETATM 8818  C  C4  . E1F N 3 .   ? 39.439  6.240   -31.952 1.00 18.19 ? 302 E1F C C4  1 
HETATM 8819  C  C3  . E1F N 3 .   ? 39.492  5.516   -33.128 1.00 15.72 ? 302 E1F C C3  1 
HETATM 8820  S  S16 . E1F N 3 .   ? 38.399  4.063   -33.378 1.00 13.78 ? 302 E1F C S16 1 
HETATM 8821  N  N19 . E1F N 3 .   ? 37.354  4.060   -32.186 1.00 9.15  ? 302 E1F C N19 1 
HETATM 8822  O  O17 . E1F N 3 .   ? 39.311  2.845   -33.079 1.00 15.69 ? 302 E1F C O17 1 
HETATM 8823  C  C6  . E1F N 3 .   ? 42.284  8.698   -32.442 1.00 23.49 ? 302 E1F C C6  1 
HETATM 8824  O  O12 . E1F N 3 .   ? 42.407  9.018   -31.260 1.00 31.61 ? 302 E1F C O12 1 
HETATM 8825  C  C7  . E1F N 3 .   ? 43.132  9.181   -33.576 1.00 28.21 ? 302 E1F C C7  1 
HETATM 8826  S  S8  . E1F N 3 .   ? 44.373  10.479  -33.096 1.00 31.96 ? 302 E1F C S8  1 
HETATM 8827  C  C9  . E1F N 3 .   ? 43.290  11.829  -33.383 1.00 32.33 ? 302 E1F C C9  1 
HETATM 8828  N  N11 . E1F N 3 .   ? 43.718  13.108  -33.129 1.00 32.68 ? 302 E1F C N11 1 
HETATM 8829  C  C14 . E1F N 3 .   ? 42.849  14.114  -33.443 1.00 33.07 ? 302 E1F C C14 1 
HETATM 8830  C  C15 . E1F N 3 .   ? 41.573  13.841  -33.994 1.00 31.43 ? 302 E1F C C15 1 
HETATM 8831  N  N10 . E1F N 3 .   ? 42.052  11.535  -33.902 1.00 32.65 ? 302 E1F C N10 1 
HETATM 8832  S  S   . SO4 O 5 .   ? 34.983  -14.944 -13.269 1.00 67.21 ? 303 SO4 C S   1 
HETATM 8833  O  O1  . SO4 O 5 .   ? 36.024  -15.608 -14.071 1.00 67.94 ? 303 SO4 C O1  1 
HETATM 8834  O  O2  . SO4 O 5 .   ? 33.912  -14.523 -14.177 1.00 67.91 ? 303 SO4 C O2  1 
HETATM 8835  O  O3  . SO4 O 5 .   ? 34.466  -15.931 -12.309 1.00 64.86 ? 303 SO4 C O3  1 
HETATM 8836  O  O4  . SO4 O 5 .   ? 35.508  -13.753 -12.592 1.00 64.51 ? 303 SO4 C O4  1 
HETATM 8837  ZN ZN  . ZN  P 2 .   ? 6.697   5.579   -38.445 1.00 7.00  ? 301 ZN  D ZN  1 
HETATM 8838  O  O18 . E1F Q 3 .   ? 7.280   7.614   -34.885 1.00 7.69  ? 302 E1F D O18 1 
HETATM 8839  C  C13 . E1F Q 3 .   ? 5.445   16.177  -35.736 1.00 20.68 ? 302 E1F D C13 1 
HETATM 8840  C  C1  . E1F Q 3 .   ? 4.208   11.409  -36.835 1.00 13.38 ? 302 E1F D C1  1 
HETATM 8841  C  C2  . E1F Q 3 .   ? 4.742   9.600   -35.394 1.00 11.33 ? 302 E1F D C2  1 
HETATM 8842  CL CL1 . E1F Q 3 .   ? 4.561   8.892   -33.846 1.00 11.29 ? 302 E1F D CL1 1 
HETATM 8843  C  C21 . E1F Q 3 .   ? 4.023   10.759  -35.646 1.00 11.39 ? 302 E1F D C21 1 
HETATM 8844  C  C5  . E1F Q 3 .   ? 5.053   10.919  -37.808 1.00 13.22 ? 302 E1F D C5  1 
HETATM 8845  C  C4  . E1F Q 3 .   ? 5.736   9.694   -37.630 1.00 14.01 ? 302 E1F D C4  1 
HETATM 8846  C  C3  . E1F Q 3 .   ? 5.619   9.111   -36.366 1.00 8.98  ? 302 E1F D C3  1 
HETATM 8847  S  S16 . E1F Q 3 .   ? 6.430   7.451   -36.103 1.00 8.92  ? 302 E1F D S16 1 
HETATM 8848  N  N19 . E1F Q 3 .   ? 7.316   7.155   -37.400 1.00 7.29  ? 302 E1F D N19 1 
HETATM 8849  O  O17 . E1F Q 3 .   ? 5.292   6.515   -35.978 1.00 7.92  ? 302 E1F D O17 1 
HETATM 8850  C  C6  . E1F Q 3 .   ? 3.417   12.667  -37.048 1.00 19.49 ? 302 E1F D C6  1 
HETATM 8851  O  O12 . E1F Q 3 .   ? 3.567   13.225  -38.096 1.00 20.27 ? 302 E1F D O12 1 
HETATM 8852  C  C7  . E1F Q 3 .   ? 2.488   13.136  -35.980 1.00 17.16 ? 302 E1F D C7  1 
HETATM 8853  S  S8  . E1F Q 3 .   ? 1.815   14.806  -36.362 1.00 23.99 ? 302 E1F D S8  1 
HETATM 8854  C  C9  . E1F Q 3 .   ? 3.186   15.916  -36.236 1.00 19.56 ? 302 E1F D C9  1 
HETATM 8855  N  N11 . E1F Q 3 .   ? 3.028   17.215  -36.551 1.00 22.56 ? 302 E1F D N11 1 
HETATM 8856  C  C14 . E1F Q 3 .   ? 4.084   18.043  -36.466 1.00 23.69 ? 302 E1F D C14 1 
HETATM 8857  C  C15 . E1F Q 3 .   ? 5.310   17.512  -36.076 1.00 21.08 ? 302 E1F D C15 1 
HETATM 8858  N  N10 . E1F Q 3 .   ? 4.375   15.430  -35.853 1.00 21.32 ? 302 E1F D N10 1 
HETATM 8859  C  C1  . EDO R 4 .   ? 6.752   9.887   -42.222 1.00 21.32 ? 303 EDO D C1  1 
HETATM 8860  O  O1  . EDO R 4 .   ? 6.644   11.312  -42.460 1.00 25.31 ? 303 EDO D O1  1 
HETATM 8861  C  C2  . EDO R 4 .   ? 5.614   9.517   -41.232 1.00 23.38 ? 303 EDO D C2  1 
HETATM 8862  O  O2  . EDO R 4 .   ? 4.297   10.144  -41.338 1.00 21.98 ? 303 EDO D O2  1 
HETATM 8863  C  C1  . EDO S 4 .   ? -2.226  -1.420  -20.259 1.00 25.76 ? 304 EDO D C1  1 
HETATM 8864  O  O1  . EDO S 4 .   ? -1.449  -0.203  -20.327 1.00 32.64 ? 304 EDO D O1  1 
HETATM 8865  C  C2  . EDO S 4 .   ? -2.923  -1.600  -21.624 1.00 26.80 ? 304 EDO D C2  1 
HETATM 8866  O  O2  . EDO S 4 .   ? -1.930  -1.706  -22.655 1.00 30.31 ? 304 EDO D O2  1 
HETATM 8867  O  O   . HOH T 6 .   ? 15.256  -6.772  21.129  1.00 10.06 ? 401 HOH A O   1 
HETATM 8868  O  O   . HOH T 6 .   ? 10.977  11.227  8.143   1.00 9.69  ? 402 HOH A O   1 
HETATM 8869  O  O   . HOH T 6 .   ? 11.962  7.514   8.671   1.00 8.46  ? 403 HOH A O   1 
HETATM 8870  O  O   . HOH T 6 .   ? 13.892  1.802   -2.999  1.00 18.52 ? 404 HOH A O   1 
HETATM 8871  O  O   . HOH T 6 .   ? 19.673  -0.494  26.589  1.00 14.50 ? 405 HOH A O   1 
HETATM 8872  O  O   . HOH T 6 .   ? 11.318  5.253   2.177   1.00 9.92  ? 406 HOH A O   1 
HETATM 8873  O  O   . HOH T 6 .   ? 41.998  2.448   0.930   1.00 15.83 ? 407 HOH A O   1 
HETATM 8874  O  O   . HOH T 6 .   ? 8.657   2.955   7.359   1.00 7.39  ? 408 HOH A O   1 
HETATM 8875  O  O   . HOH T 6 .   ? 41.183  -10.306 9.727   1.00 14.65 ? 409 HOH A O   1 
HETATM 8876  O  O   . HOH T 6 .   ? 17.688  9.587   0.100   1.00 11.75 ? 410 HOH A O   1 
HETATM 8877  O  O   . HOH T 6 .   ? 28.537  -4.149  2.541   1.00 9.64  ? 411 HOH A O   1 
HETATM 8878  O  O   . HOH T 6 .   ? 19.339  14.234  5.055   1.00 12.52 ? 412 HOH A O   1 
HETATM 8879  O  O   . HOH T 6 .   ? 5.524   -12.027 13.353  1.00 16.65 ? 413 HOH A O   1 
HETATM 8880  O  O   . HOH T 6 .   ? 8.766   -6.375  7.520   1.00 15.91 ? 414 HOH A O   1 
HETATM 8881  O  O   . HOH T 6 .   ? 12.095  -10.475 27.354  1.00 13.37 ? 415 HOH A O   1 
HETATM 8882  O  O   . HOH T 6 .   ? 17.398  0.342   28.532  1.00 14.57 ? 416 HOH A O   1 
HETATM 8883  O  O   . HOH T 6 .   ? 36.381  -6.939  26.333  1.00 18.12 ? 417 HOH A O   1 
HETATM 8884  O  O   . HOH T 6 .   ? 13.655  16.550  11.825  1.00 14.91 ? 418 HOH A O   1 
HETATM 8885  O  O   . HOH T 6 .   ? 17.885  3.255   12.724  1.00 9.09  ? 419 HOH A O   1 
HETATM 8886  O  O   . HOH T 6 .   ? 30.483  -8.829  -2.576  1.00 15.00 ? 420 HOH A O   1 
HETATM 8887  O  O   . HOH T 6 .   ? 10.469  -3.378  2.685   1.00 11.83 ? 421 HOH A O   1 
HETATM 8888  O  O   . HOH T 6 .   ? 8.908   4.052   2.707   1.00 11.79 ? 422 HOH A O   1 
HETATM 8889  O  O   . HOH T 6 .   ? 10.590  6.268   15.438  1.00 10.74 ? 423 HOH A O   1 
HETATM 8890  O  O   . HOH T 6 .   ? 12.569  -10.584 30.024  1.00 17.61 ? 424 HOH A O   1 
HETATM 8891  O  O   . HOH T 6 .   ? 31.438  -19.026 4.251   1.00 21.93 ? 425 HOH A O   1 
HETATM 8892  O  O   . HOH T 6 .   ? 23.132  -12.315 9.781   1.00 9.96  ? 426 HOH A O   1 
HETATM 8893  O  O   . HOH T 6 .   ? 15.102  -15.840 15.109  1.00 16.88 ? 427 HOH A O   1 
HETATM 8894  O  O   . HOH T 6 .   ? 12.453  -2.622  11.049  1.00 7.81  ? 428 HOH A O   1 
HETATM 8895  O  O   . HOH T 6 .   ? 7.809   -8.183  11.848  1.00 19.87 ? 429 HOH A O   1 
HETATM 8896  O  O   . HOH T 6 .   ? 16.624  11.006  -3.133  1.00 24.00 ? 430 HOH A O   1 
HETATM 8897  O  O   . HOH T 6 .   ? 39.987  -12.098 11.613  1.00 18.46 ? 431 HOH A O   1 
HETATM 8898  O  O   . HOH T 6 .   ? 19.023  11.842  -0.765  1.00 17.54 ? 432 HOH A O   1 
HETATM 8899  O  O   . HOH T 6 .   ? 14.495  -9.836  26.066  1.00 13.23 ? 433 HOH A O   1 
HETATM 8900  O  O   . HOH T 6 .   ? 9.669   -2.575  10.430  1.00 18.25 ? 434 HOH A O   1 
HETATM 8901  O  O   . HOH T 6 .   ? 31.785  5.613   32.472  1.00 26.71 ? 435 HOH A O   1 
HETATM 8902  O  O   . HOH T 6 .   ? 18.142  -15.121 6.354   1.00 15.68 ? 436 HOH A O   1 
HETATM 8903  O  O   . HOH T 6 .   ? 10.299  4.799   8.777   1.00 9.46  ? 437 HOH A O   1 
HETATM 8904  O  O   . HOH T 6 .   ? 43.658  -4.078  12.778  1.00 18.24 ? 438 HOH A O   1 
HETATM 8905  O  O   . HOH T 6 .   ? 7.341   5.002   11.269  1.00 8.15  ? 439 HOH A O   1 
HETATM 8906  O  O   . HOH T 6 .   ? 25.686  -15.913 6.623   1.00 10.44 ? 440 HOH A O   1 
HETATM 8907  O  O   . HOH T 6 .   ? 12.509  14.577  2.351   1.00 11.85 ? 441 HOH A O   1 
HETATM 8908  O  O   . HOH T 6 .   ? 39.351  3.940   19.534  1.00 21.84 ? 442 HOH A O   1 
HETATM 8909  O  O   . HOH T 6 .   ? 29.838  -15.619 -1.653  1.00 20.06 ? 443 HOH A O   1 
HETATM 8910  O  O   . HOH T 6 .   ? 4.909   -9.115  25.681  1.00 22.94 ? 444 HOH A O   1 
HETATM 8911  O  O   . HOH T 6 .   ? 17.131  0.717   -0.488  1.00 13.65 ? 445 HOH A O   1 
HETATM 8912  O  O   . HOH T 6 .   ? 15.923  4.563   21.754  1.00 16.29 ? 446 HOH A O   1 
HETATM 8913  O  O   . HOH T 6 .   ? 11.924  -15.414 8.394   1.00 20.73 ? 447 HOH A O   1 
HETATM 8914  O  O   . HOH T 6 .   ? 38.178  -7.549  24.441  1.00 20.17 ? 448 HOH A O   1 
HETATM 8915  O  O   . HOH T 6 .   ? 43.520  -9.396  11.223  1.00 21.56 ? 449 HOH A O   1 
HETATM 8916  O  O   . HOH T 6 .   ? 11.562  7.994   1.681   1.00 11.73 ? 450 HOH A O   1 
HETATM 8917  O  O   . HOH T 6 .   ? 7.693   9.271   14.244  1.00 17.20 ? 451 HOH A O   1 
HETATM 8918  O  O   . HOH T 6 .   ? 23.997  -15.903 29.740  1.00 21.38 ? 452 HOH A O   1 
HETATM 8919  O  O   . HOH T 6 .   ? 15.972  -11.964 27.123  1.00 18.06 ? 453 HOH A O   1 
HETATM 8920  O  O   . HOH T 6 .   ? 12.151  -8.369  31.588  1.00 19.22 ? 454 HOH A O   1 
HETATM 8921  O  O   . HOH T 6 .   ? 13.894  1.575   -0.267  1.00 15.45 ? 455 HOH A O   1 
HETATM 8922  O  O   . HOH T 6 .   ? 25.270  -18.317 30.280  1.00 26.02 ? 456 HOH A O   1 
HETATM 8923  O  O   . HOH T 6 .   ? 39.518  -15.597 16.850  1.00 22.05 ? 457 HOH A O   1 
HETATM 8924  O  O   . HOH T 6 .   ? 7.445   -2.035  -0.777  1.00 18.80 ? 458 HOH A O   1 
HETATM 8925  O  O   . HOH T 6 .   ? 15.100  -13.567 16.644  1.00 12.73 ? 459 HOH A O   1 
HETATM 8926  O  O   . HOH T 6 .   ? 27.815  -20.982 24.547  1.00 25.96 ? 460 HOH A O   1 
HETATM 8927  O  O   . HOH T 6 .   ? 26.001  12.349  6.151   1.00 21.48 ? 461 HOH A O   1 
HETATM 8928  O  O   . HOH T 6 .   ? 19.388  9.824   32.263  1.00 18.05 ? 462 HOH A O   1 
HETATM 8929  O  O   . HOH T 6 .   ? 26.166  -17.752 17.499  1.00 17.04 ? 463 HOH A O   1 
HETATM 8930  O  O   . HOH T 6 .   ? 14.069  -16.069 26.885  1.00 21.42 ? 464 HOH A O   1 
HETATM 8931  O  O   . HOH T 6 .   ? 32.037  -16.658 20.628  1.00 29.43 ? 465 HOH A O   1 
HETATM 8932  O  O   . HOH T 6 .   ? 23.366  3.329   -2.088  1.00 14.55 ? 466 HOH A O   1 
HETATM 8933  O  O   . HOH T 6 .   ? 26.200  -18.462 20.501  1.00 16.56 ? 467 HOH A O   1 
HETATM 8934  O  O   . HOH T 6 .   ? 15.282  -14.299 19.281  1.00 15.07 ? 468 HOH A O   1 
HETATM 8935  O  O   . HOH T 6 .   ? 29.208  -14.893 16.984  1.00 16.66 ? 469 HOH A O   1 
HETATM 8936  O  O   . HOH T 6 .   ? 32.367  -16.815 10.330  1.00 26.47 ? 470 HOH A O   1 
HETATM 8937  O  O   . HOH T 6 .   ? 38.581  4.239   11.238  1.00 20.08 ? 471 HOH A O   1 
HETATM 8938  O  O   . HOH T 6 .   ? 31.549  -13.219 2.489   1.00 18.75 ? 472 HOH A O   1 
HETATM 8939  O  O   . HOH T 6 .   ? 28.553  2.459   -1.387  1.00 20.89 ? 473 HOH A O   1 
HETATM 8940  O  O   . HOH T 6 .   ? 25.740  -18.438 12.543  1.00 20.55 ? 474 HOH A O   1 
HETATM 8941  O  O   . HOH T 6 .   ? 36.720  -4.220  -0.887  1.00 16.60 ? 475 HOH A O   1 
HETATM 8942  O  O   . HOH T 6 .   ? 7.514   -6.771  2.356   1.00 19.09 ? 476 HOH A O   1 
HETATM 8943  O  O   . HOH T 6 .   ? 4.643   13.300  19.423  1.00 28.62 ? 477 HOH A O   1 
HETATM 8944  O  O   . HOH T 6 .   ? 11.027  -5.154  0.677   1.00 16.78 ? 478 HOH A O   1 
HETATM 8945  O  O   . HOH T 6 .   ? 20.720  -9.905  31.868  1.00 17.33 ? 479 HOH A O   1 
HETATM 8946  O  O   . HOH T 6 .   ? 5.955   -4.092  -8.267  1.00 22.62 ? 480 HOH A O   1 
HETATM 8947  O  O   . HOH T 6 .   ? 20.820  -2.587  -5.215  1.00 21.53 ? 481 HOH A O   1 
HETATM 8948  O  O   . HOH T 6 .   ? 13.220  -14.254 12.843  1.00 28.27 ? 482 HOH A O   1 
HETATM 8949  O  O   . HOH T 6 .   ? 7.637   -9.408  15.676  1.00 16.91 ? 483 HOH A O   1 
HETATM 8950  O  O   . HOH T 6 .   ? 33.230  -14.908 3.642   1.00 25.12 ? 484 HOH A O   1 
HETATM 8951  O  O   . HOH T 6 .   ? 28.943  -18.492 20.595  1.00 20.16 ? 485 HOH A O   1 
HETATM 8952  O  O   . HOH T 6 .   ? 16.943  -13.510 30.767  1.00 18.61 ? 486 HOH A O   1 
HETATM 8953  O  O   . HOH T 6 .   ? 6.520   15.867  15.934  1.00 29.40 ? 487 HOH A O   1 
HETATM 8954  O  O   . HOH T 6 .   ? 34.969  10.184  10.532  1.00 24.76 ? 488 HOH A O   1 
HETATM 8955  O  O   . HOH T 6 .   ? 10.732  -4.636  -4.984  1.00 27.96 ? 489 HOH A O   1 
HETATM 8956  O  O   . HOH T 6 .   ? 32.585  7.633   30.889  1.00 20.97 ? 490 HOH A O   1 
HETATM 8957  O  O   . HOH T 6 .   ? 12.783  -12.301 16.494  1.00 18.36 ? 491 HOH A O   1 
HETATM 8958  O  O   . HOH T 6 .   ? 11.302  9.737   -2.002  1.00 23.81 ? 492 HOH A O   1 
HETATM 8959  O  O   . HOH T 6 .   ? 13.759  -12.547 20.841  1.00 15.33 ? 493 HOH A O   1 
HETATM 8960  O  O   . HOH T 6 .   ? 14.415  4.387   -4.138  1.00 17.32 ? 494 HOH A O   1 
HETATM 8961  O  O   . HOH T 6 .   ? 9.147   11.463  1.058   1.00 14.76 ? 495 HOH A O   1 
HETATM 8962  O  O   . HOH T 6 .   ? 44.584  -3.609  -1.703  1.00 26.31 ? 496 HOH A O   1 
HETATM 8963  O  O   . HOH T 6 .   ? 39.994  -11.932 22.824  1.00 28.15 ? 497 HOH A O   1 
HETATM 8964  O  O   . HOH T 6 .   ? 7.876   6.689   15.577  1.00 14.17 ? 498 HOH A O   1 
HETATM 8965  O  O   . HOH T 6 .   ? 6.165   -2.932  13.265  1.00 19.67 ? 499 HOH A O   1 
HETATM 8966  O  O   . HOH T 6 .   ? 22.225  -19.131 15.123  1.00 26.22 ? 500 HOH A O   1 
HETATM 8967  O  O   . HOH T 6 .   ? 24.063  -20.986 26.491  1.00 24.18 ? 501 HOH A O   1 
HETATM 8968  O  O   . HOH T 6 .   ? 23.889  -15.493 -11.732 1.00 28.03 ? 502 HOH A O   1 
HETATM 8969  O  O   . HOH T 6 .   ? 18.665  20.613  8.154   1.00 24.52 ? 503 HOH A O   1 
HETATM 8970  O  O   . HOH T 6 .   ? 12.542  4.493   22.281  1.00 23.88 ? 504 HOH A O   1 
HETATM 8971  O  O   . HOH T 6 .   ? 18.288  5.529   20.677  1.00 15.02 ? 505 HOH A O   1 
HETATM 8972  O  O   . HOH T 6 .   ? 8.169   -10.385 26.521  1.00 23.88 ? 506 HOH A O   1 
HETATM 8973  O  O   . HOH T 6 .   ? 47.421  -4.380  -0.845  1.00 19.47 ? 507 HOH A O   1 
HETATM 8974  O  O   . HOH T 6 .   ? 24.602  -7.577  -7.654  1.00 33.83 ? 508 HOH A O   1 
HETATM 8975  O  O   . HOH T 6 .   ? 10.251  -4.030  19.546  1.00 19.60 ? 509 HOH A O   1 
HETATM 8976  O  O   . HOH T 6 .   ? 14.310  -1.956  28.882  1.00 18.77 ? 510 HOH A O   1 
HETATM 8977  O  O   . HOH T 6 .   ? 14.941  7.157   21.080  1.00 20.54 ? 511 HOH A O   1 
HETATM 8978  O  O   . HOH T 6 .   ? 32.975  5.122   20.154  1.00 21.26 ? 512 HOH A O   1 
HETATM 8979  O  O   . HOH T 6 .   ? 21.251  16.190  5.270   1.00 18.56 ? 513 HOH A O   1 
HETATM 8980  O  O   . HOH T 6 .   ? 23.726  15.038  4.487   1.00 22.23 ? 514 HOH A O   1 
HETATM 8981  O  O   . HOH T 6 .   ? 7.603   -15.722 7.347   1.00 24.57 ? 515 HOH A O   1 
HETATM 8982  O  O   . HOH T 6 .   ? 23.527  -10.104 32.450  1.00 24.37 ? 516 HOH A O   1 
HETATM 8983  O  O   . HOH T 6 .   ? 23.989  12.230  0.416   1.00 24.12 ? 517 HOH A O   1 
HETATM 8984  O  O   . HOH T 6 .   ? 24.835  16.409  2.271   1.00 25.23 ? 518 HOH A O   1 
HETATM 8985  O  O   . HOH T 6 .   ? 17.628  8.089   19.774  1.00 22.29 ? 519 HOH A O   1 
HETATM 8986  O  O   . HOH T 6 .   ? 19.020  10.257  -4.424  1.00 25.23 ? 520 HOH A O   1 
HETATM 8987  O  O   . HOH T 6 .   ? 11.072  12.515  20.478  1.00 25.42 ? 521 HOH A O   1 
HETATM 8988  O  O   . HOH T 6 .   ? 39.710  -12.590 19.795  1.00 19.55 ? 522 HOH A O   1 
HETATM 8989  O  O   . HOH T 6 .   ? 43.081  -10.079 18.998  1.00 26.79 ? 523 HOH A O   1 
HETATM 8990  O  O   . HOH T 6 .   ? 38.561  -13.191 5.568   1.00 25.49 ? 524 HOH A O   1 
HETATM 8991  O  O   . HOH T 6 .   ? 23.970  -21.549 -3.406  1.00 32.46 ? 525 HOH A O   1 
HETATM 8992  O  O   . HOH T 6 .   ? 38.786  -15.228 12.191  1.00 30.43 ? 526 HOH A O   1 
HETATM 8993  O  O   . HOH T 6 .   ? 21.139  11.892  -2.583  1.00 26.07 ? 527 HOH A O   1 
HETATM 8994  O  O   . HOH T 6 .   ? 32.343  -18.309 7.073   1.00 27.29 ? 528 HOH A O   1 
HETATM 8995  O  O   . HOH T 6 .   ? 13.538  -13.549 23.282  1.00 27.40 ? 529 HOH A O   1 
HETATM 8996  O  O   . HOH T 6 .   ? 20.745  17.727  7.455   1.00 26.97 ? 530 HOH A O   1 
HETATM 8997  O  O   . HOH T 6 .   ? 13.303  5.072   -0.472  1.00 20.57 ? 531 HOH A O   1 
HETATM 8998  O  O   . HOH T 6 .   ? 45.176  -4.517  7.363   1.00 21.25 ? 532 HOH A O   1 
HETATM 8999  O  O   . HOH T 6 .   ? 4.653   -0.218  -8.545  1.00 23.06 ? 533 HOH A O   1 
HETATM 9000  O  O   . HOH T 6 .   ? 19.928  14.079  28.416  1.00 21.39 ? 534 HOH A O   1 
HETATM 9001  O  O   . HOH T 6 .   ? 44.170  -9.720  8.024   1.00 22.43 ? 535 HOH A O   1 
HETATM 9002  O  O   . HOH T 6 .   ? 45.461  -13.563 17.760  1.00 39.85 ? 536 HOH A O   1 
HETATM 9003  O  O   . HOH T 6 .   ? 15.181  -17.141 19.570  1.00 28.25 ? 537 HOH A O   1 
HETATM 9004  O  O   . HOH T 6 .   ? 29.354  12.028  -4.745  1.00 31.10 ? 538 HOH A O   1 
HETATM 9005  O  O   . HOH T 6 .   ? 36.453  -14.391 -1.896  1.00 32.80 ? 539 HOH A O   1 
HETATM 9006  O  O   . HOH T 6 .   ? 11.175  3.391   19.001  1.00 20.33 ? 540 HOH A O   1 
HETATM 9007  O  O   . HOH T 6 .   ? 16.378  -16.539 8.000   1.00 22.52 ? 541 HOH A O   1 
HETATM 9008  O  O   . HOH T 6 .   ? 19.650  -18.365 26.355  1.00 18.04 ? 542 HOH A O   1 
HETATM 9009  O  O   . HOH T 6 .   ? 26.038  11.219  30.964  1.00 21.47 ? 543 HOH A O   1 
HETATM 9010  O  O   . HOH T 6 .   ? 27.413  -5.424  -5.221  1.00 20.65 ? 544 HOH A O   1 
HETATM 9011  O  O   . HOH T 6 .   ? 28.144  3.984   33.526  1.00 26.82 ? 545 HOH A O   1 
HETATM 9012  O  O   . HOH T 6 .   ? 7.351   -0.715  8.027   1.00 27.92 ? 546 HOH A O   1 
HETATM 9013  O  O   . HOH T 6 .   ? 26.527  5.623   -3.730  1.00 29.27 ? 547 HOH A O   1 
HETATM 9014  O  O   . HOH T 6 .   ? 27.303  -18.275 14.835  1.00 37.66 ? 548 HOH A O   1 
HETATM 9015  O  O   . HOH T 6 .   ? 15.536  -15.486 2.601   1.00 25.62 ? 549 HOH A O   1 
HETATM 9016  O  O   . HOH T 6 .   ? 12.427  11.543  -3.633  1.00 30.98 ? 550 HOH A O   1 
HETATM 9017  O  O   . HOH T 6 .   ? 9.737   -16.697 8.596   1.00 36.26 ? 551 HOH A O   1 
HETATM 9018  O  O   . HOH T 6 .   ? 20.798  4.189   16.472  1.00 17.10 ? 552 HOH A O   1 
HETATM 9019  O  O   . HOH T 6 .   ? 11.594  -12.990 25.890  1.00 23.17 ? 553 HOH A O   1 
HETATM 9020  O  O   . HOH T 6 .   ? 8.869   -14.094 1.858   1.00 31.67 ? 554 HOH A O   1 
HETATM 9021  O  O   . HOH T 6 .   ? 21.019  0.282   33.384  1.00 37.83 ? 555 HOH A O   1 
HETATM 9022  O  O   . HOH T 6 .   ? 5.821   -3.491  20.849  1.00 27.12 ? 556 HOH A O   1 
HETATM 9023  O  O   . HOH T 6 .   ? 11.961  10.288  22.956  1.00 31.32 ? 557 HOH A O   1 
HETATM 9024  O  O   . HOH T 6 .   ? 9.427   -10.994 14.285  1.00 25.61 ? 558 HOH A O   1 
HETATM 9025  O  O   . HOH T 6 .   ? 36.879  7.938   9.824   1.00 29.18 ? 559 HOH A O   1 
HETATM 9026  O  O   . HOH T 6 .   ? 11.413  3.816   -0.106  1.00 21.85 ? 560 HOH A O   1 
HETATM 9027  O  O   . HOH T 6 .   ? 17.815  -16.467 -3.455  1.00 39.27 ? 561 HOH A O   1 
HETATM 9028  O  O   . HOH T 6 .   ? 9.443   18.473  17.881  1.00 36.04 ? 562 HOH A O   1 
HETATM 9029  O  O   . HOH T 6 .   ? 20.864  -18.733 28.863  1.00 24.98 ? 563 HOH A O   1 
HETATM 9030  O  O   . HOH T 6 .   ? 24.512  -11.510 30.231  1.00 24.17 ? 564 HOH A O   1 
HETATM 9031  O  O   . HOH T 6 .   ? 14.979  -13.881 25.530  1.00 22.95 ? 565 HOH A O   1 
HETATM 9032  O  O   . HOH T 6 .   ? 11.899  5.331   -4.365  1.00 22.97 ? 566 HOH A O   1 
HETATM 9033  O  O   . HOH T 6 .   ? 32.588  -14.869 28.183  1.00 28.29 ? 567 HOH A O   1 
HETATM 9034  O  O   . HOH T 6 .   ? 14.682  -12.297 29.512  1.00 15.52 ? 568 HOH A O   1 
HETATM 9035  O  O   . HOH T 6 .   ? 33.852  -13.279 26.673  1.00 22.34 ? 569 HOH A O   1 
HETATM 9036  O  O   . HOH T 6 .   ? 19.614  -11.316 33.874  1.00 21.41 ? 570 HOH A O   1 
HETATM 9037  O  O   . HOH T 6 .   ? 9.654   -4.924  16.639  1.00 22.76 ? 571 HOH A O   1 
HETATM 9038  O  O   . HOH T 6 .   ? 18.422  -15.672 34.007  1.00 20.29 ? 572 HOH A O   1 
HETATM 9039  O  O   . HOH T 6 .   ? 11.451  2.405   -6.738  1.00 26.27 ? 573 HOH A O   1 
HETATM 9040  O  O   . HOH T 6 .   ? 7.893   -6.985  16.720  1.00 22.85 ? 574 HOH A O   1 
HETATM 9041  O  O   . HOH T 6 .   ? 13.432  -5.710  32.178  1.00 19.56 ? 575 HOH A O   1 
HETATM 9042  O  O   . HOH T 6 .   ? 44.352  -2.977  15.522  1.00 23.78 ? 576 HOH A O   1 
HETATM 9043  O  O   . HOH T 6 .   ? 31.775  10.120  31.959  1.00 24.70 ? 577 HOH A O   1 
HETATM 9044  O  O   . HOH T 6 .   ? 8.509   -0.193  24.537  1.00 25.76 ? 578 HOH A O   1 
HETATM 9045  O  O   . HOH T 6 .   ? 6.619   -9.742  4.462   1.00 23.59 ? 579 HOH A O   1 
HETATM 9046  O  O   . HOH T 6 .   ? 7.303   -5.655  5.149   1.00 23.51 ? 580 HOH A O   1 
HETATM 9047  O  O   . HOH T 6 .   ? 45.358  -5.732  13.344  1.00 29.46 ? 581 HOH A O   1 
HETATM 9048  O  O   . HOH T 6 .   ? 27.973  -4.660  31.268  1.00 24.18 ? 582 HOH A O   1 
HETATM 9049  O  O   . HOH T 6 .   ? 35.399  -0.789  30.605  1.00 25.49 ? 583 HOH A O   1 
HETATM 9050  O  O   . HOH T 6 .   ? 10.178  4.060   -2.521  1.00 29.36 ? 584 HOH A O   1 
HETATM 9051  O  O   . HOH T 6 .   ? 11.499  1.620   -4.153  1.00 28.43 ? 585 HOH A O   1 
HETATM 9052  O  O   . HOH T 6 .   ? 31.218  -20.874 8.577   1.00 28.93 ? 586 HOH A O   1 
HETATM 9053  O  O   . HOH T 6 .   ? 33.541  -18.297 27.721  1.00 31.36 ? 587 HOH A O   1 
HETATM 9054  O  O   . HOH T 6 .   ? 13.311  14.097  14.140  1.00 21.86 ? 588 HOH A O   1 
HETATM 9055  O  O   . HOH T 6 .   ? 30.236  -17.652 18.542  1.00 31.07 ? 589 HOH A O   1 
HETATM 9056  O  O   . HOH T 6 .   ? 45.496  1.659   21.397  1.00 29.30 ? 590 HOH A O   1 
HETATM 9057  O  O   . HOH T 6 .   ? 13.448  -14.702 29.425  1.00 29.88 ? 591 HOH A O   1 
HETATM 9058  O  O   . HOH T 6 .   ? 34.162  -10.548 28.096  1.00 34.07 ? 592 HOH A O   1 
HETATM 9059  O  O   . HOH T 6 .   ? 23.911  -19.661 16.550  1.00 31.54 ? 593 HOH A O   1 
HETATM 9060  O  O   . HOH T 6 .   ? 39.467  -9.792  24.702  1.00 28.89 ? 594 HOH A O   1 
HETATM 9061  O  O   . HOH T 6 .   ? 45.409  -6.452  5.930   1.00 23.70 ? 595 HOH A O   1 
HETATM 9062  O  O   . HOH T 6 .   ? 36.750  -15.356 6.249   1.00 34.50 ? 596 HOH A O   1 
HETATM 9063  O  O   . HOH T 6 .   ? 18.092  9.988   21.930  1.00 24.05 ? 597 HOH A O   1 
HETATM 9064  O  O   . HOH T 6 .   ? 12.706  -15.646 11.219  1.00 26.28 ? 598 HOH A O   1 
HETATM 9065  O  O   . HOH T 6 .   ? 29.383  -16.791 14.824  1.00 21.88 ? 599 HOH A O   1 
HETATM 9066  O  O   . HOH T 6 .   ? 29.238  10.306  22.656  1.00 41.59 ? 600 HOH A O   1 
HETATM 9067  O  O   . HOH T 6 .   ? 37.484  10.213  24.061  1.00 29.77 ? 601 HOH A O   1 
HETATM 9068  O  O   . HOH T 6 .   ? 42.128  -13.935 12.004  1.00 33.88 ? 602 HOH A O   1 
HETATM 9069  O  O   . HOH T 6 .   ? 9.249   2.291   -8.030  1.00 34.87 ? 603 HOH A O   1 
HETATM 9070  O  O   . HOH T 6 .   ? 14.528  13.908  38.769  1.00 29.07 ? 604 HOH A O   1 
HETATM 9071  O  O   . HOH T 6 .   ? 13.759  -17.035 7.288   1.00 24.67 ? 605 HOH A O   1 
HETATM 9072  O  O   . HOH T 6 .   ? 22.752  16.591  8.404   1.00 40.07 ? 606 HOH A O   1 
HETATM 9073  O  O   . HOH T 6 .   ? 9.657   -5.295  -1.435  1.00 29.88 ? 607 HOH A O   1 
HETATM 9074  O  O   . HOH T 6 .   ? 28.109  -2.626  36.903  1.00 31.22 ? 608 HOH A O   1 
HETATM 9075  O  O   . HOH T 6 .   ? 35.750  -16.320 13.452  1.00 40.38 ? 609 HOH A O   1 
HETATM 9076  O  O   . HOH T 6 .   ? 27.267  -15.916 -5.599  1.00 24.63 ? 610 HOH A O   1 
HETATM 9077  O  O   . HOH T 6 .   ? 45.733  0.024   5.795   1.00 29.54 ? 611 HOH A O   1 
HETATM 9078  O  O   . HOH T 6 .   ? 29.832  10.297  33.680  1.00 32.41 ? 612 HOH A O   1 
HETATM 9079  O  O   . HOH T 6 .   ? 30.371  14.704  4.451   1.00 30.63 ? 613 HOH A O   1 
HETATM 9080  O  O   . HOH T 6 .   ? 19.728  12.107  24.290  1.00 23.58 ? 614 HOH A O   1 
HETATM 9081  O  O   . HOH T 6 .   ? 25.447  -13.609 30.985  1.00 30.79 ? 615 HOH A O   1 
HETATM 9082  O  O   . HOH T 6 .   ? 24.321  -2.655  33.029  1.00 28.15 ? 616 HOH A O   1 
HETATM 9083  O  O   . HOH T 6 .   ? 36.207  -13.623 26.686  1.00 37.51 ? 617 HOH A O   1 
HETATM 9084  O  O   . HOH T 6 .   ? 11.395  -6.648  -7.867  1.00 26.99 ? 618 HOH A O   1 
HETATM 9085  O  O   . HOH T 6 .   ? 20.191  -19.897 9.025   1.00 28.44 ? 619 HOH A O   1 
HETATM 9086  O  O   . HOH T 6 .   ? 23.974  10.919  -2.103  1.00 34.69 ? 620 HOH A O   1 
HETATM 9087  O  O   . HOH T 6 .   ? 39.843  -1.658  28.957  1.00 29.42 ? 621 HOH A O   1 
HETATM 9088  O  O   . HOH T 6 .   ? 37.252  7.432   29.954  1.00 31.67 ? 622 HOH A O   1 
HETATM 9089  O  O   . HOH T 6 .   ? 52.137  -4.205  21.095  1.00 33.33 ? 623 HOH A O   1 
HETATM 9090  O  O   . HOH T 6 .   ? 16.064  17.950  39.011  1.00 37.02 ? 624 HOH A O   1 
HETATM 9091  O  O   . HOH T 6 .   ? 27.947  -17.762 30.797  1.00 35.60 ? 625 HOH A O   1 
HETATM 9092  O  O   . HOH T 6 .   ? 31.721  -17.238 -5.219  1.00 36.51 ? 626 HOH A O   1 
HETATM 9093  O  O   . HOH T 6 .   ? 19.164  -19.993 11.944  1.00 39.81 ? 627 HOH A O   1 
HETATM 9094  O  O   . HOH T 6 .   ? 34.245  -3.855  32.098  1.00 37.44 ? 628 HOH A O   1 
HETATM 9095  O  O   . HOH T 6 .   ? 17.230  -3.620  -8.371  1.00 40.17 ? 629 HOH A O   1 
HETATM 9096  O  O   . HOH T 6 .   ? 22.382  15.808  24.427  1.00 42.36 ? 630 HOH A O   1 
HETATM 9097  O  O   . HOH T 6 .   ? 10.383  -9.165  -8.000  1.00 28.29 ? 631 HOH A O   1 
HETATM 9098  O  O   . HOH T 6 .   ? 20.499  15.510  1.978   1.00 25.64 ? 632 HOH A O   1 
HETATM 9099  O  O   . HOH T 6 .   ? 23.250  -4.200  -5.554  1.00 32.88 ? 633 HOH A O   1 
HETATM 9100  O  O   . HOH T 6 .   ? 11.057  -14.616 17.279  1.00 31.84 ? 634 HOH A O   1 
HETATM 9101  O  O   . HOH T 6 .   ? 38.759  -5.096  -3.053  1.00 27.89 ? 635 HOH A O   1 
HETATM 9102  O  O   . HOH T 6 .   ? 13.263  5.966   24.471  1.00 29.15 ? 636 HOH A O   1 
HETATM 9103  O  O   . HOH T 6 .   ? 43.429  -4.490  28.851  1.00 28.34 ? 637 HOH A O   1 
HETATM 9104  O  O   . HOH T 6 .   ? 46.321  -8.967  16.369  1.00 43.35 ? 638 HOH A O   1 
HETATM 9105  O  O   . HOH T 6 .   ? 18.572  17.409  -0.063  1.00 27.75 ? 639 HOH A O   1 
HETATM 9106  O  O   . HOH T 6 .   ? 39.071  -4.009  30.406  1.00 30.85 ? 640 HOH A O   1 
HETATM 9107  O  O   . HOH T 6 .   ? 45.856  2.027   7.553   1.00 27.11 ? 641 HOH A O   1 
HETATM 9108  O  O   . HOH T 6 .   ? 13.769  21.343  11.393  1.00 25.90 ? 642 HOH A O   1 
HETATM 9109  O  O   . HOH T 6 .   ? 18.993  -6.379  -11.770 1.00 30.84 ? 643 HOH A O   1 
HETATM 9110  O  O   . HOH T 6 .   ? 29.762  -3.911  -5.612  1.00 32.51 ? 644 HOH A O   1 
HETATM 9111  O  O   . HOH T 6 .   ? 31.624  -2.330  -4.603  1.00 34.00 ? 645 HOH A O   1 
HETATM 9112  O  O   . HOH T 6 .   ? 30.227  -18.150 -2.569  1.00 31.14 ? 646 HOH A O   1 
HETATM 9113  O  O   . HOH T 6 .   ? 35.983  -14.645 4.114   1.00 28.32 ? 647 HOH A O   1 
HETATM 9114  O  O   . HOH T 6 .   ? 46.208  -6.522  8.404   1.00 39.87 ? 648 HOH A O   1 
HETATM 9115  O  O   . HOH T 6 .   ? 39.018  -3.318  -7.499  1.00 43.24 ? 649 HOH A O   1 
HETATM 9116  O  O   . HOH T 6 .   ? 7.103   -2.305  25.733  1.00 31.33 ? 650 HOH A O   1 
HETATM 9117  O  O   . HOH T 6 .   ? 7.017   -6.415  10.054  1.00 29.53 ? 651 HOH A O   1 
HETATM 9118  O  O   . HOH T 6 .   ? 10.942  -15.248 13.514  1.00 29.91 ? 652 HOH A O   1 
HETATM 9119  O  O   . HOH T 6 .   ? 30.647  -21.100 2.925   1.00 30.26 ? 653 HOH A O   1 
HETATM 9120  O  O   . HOH T 6 .   ? 23.866  8.413   11.677  1.00 27.40 ? 654 HOH A O   1 
HETATM 9121  O  O   . HOH T 6 .   ? 20.092  -7.266  32.324  1.00 25.05 ? 655 HOH A O   1 
HETATM 9122  O  O   . HOH T 6 .   ? 14.167  13.228  28.267  1.00 41.39 ? 656 HOH A O   1 
HETATM 9123  O  O   . HOH T 6 .   ? 12.201  5.337   28.964  1.00 37.98 ? 657 HOH A O   1 
HETATM 9124  O  O   . HOH T 6 .   ? 8.066   -1.816  15.206  1.00 26.18 ? 658 HOH A O   1 
HETATM 9125  O  O   . HOH T 6 .   ? 12.990  11.549  -6.257  1.00 31.01 ? 659 HOH A O   1 
HETATM 9126  O  O   . HOH T 6 .   ? 32.710  7.171   15.973  1.00 29.81 ? 660 HOH A O   1 
HETATM 9127  O  O   . HOH T 6 .   ? 40.487  8.775   8.790   1.00 37.61 ? 661 HOH A O   1 
HETATM 9128  O  O   . HOH T 6 .   ? 36.693  6.270   11.832  1.00 28.98 ? 662 HOH A O   1 
HETATM 9129  O  O   . HOH T 6 .   ? 30.345  14.738  10.320  1.00 36.00 ? 663 HOH A O   1 
HETATM 9130  O  O   . HOH T 6 .   ? 33.615  15.563  7.472   1.00 35.26 ? 664 HOH A O   1 
HETATM 9131  O  O   . HOH T 6 .   ? 32.590  6.834   12.870  1.00 27.31 ? 665 HOH A O   1 
HETATM 9132  O  O   . HOH T 6 .   ? 23.670  7.632   13.880  1.00 29.33 ? 666 HOH A O   1 
HETATM 9133  O  O   . HOH T 6 .   ? 4.390   13.780  22.323  1.00 36.95 ? 667 HOH A O   1 
HETATM 9134  O  O   . HOH T 6 .   ? 30.326  7.134   13.500  1.00 28.40 ? 668 HOH A O   1 
HETATM 9135  O  O   . HOH T 6 .   ? 28.471  8.898   17.349  1.00 33.98 ? 669 HOH A O   1 
HETATM 9136  O  O   . HOH T 6 .   ? 27.053  7.573   14.740  1.00 26.28 ? 670 HOH A O   1 
HETATM 9137  O  O   . HOH T 6 .   ? 27.301  13.668  24.692  1.00 39.88 ? 671 HOH A O   1 
HETATM 9138  O  O   . HOH T 6 .   ? 38.735  6.468   18.906  1.00 33.87 ? 672 HOH A O   1 
HETATM 9139  O  O   . HOH T 6 .   ? 33.567  -17.693 2.773   1.00 32.75 ? 673 HOH A O   1 
HETATM 9140  O  O   . HOH T 6 .   ? 18.452  -3.270  -5.630  1.00 25.57 ? 674 HOH A O   1 
HETATM 9141  O  O   . HOH T 6 .   ? 30.646  -3.012  35.733  1.00 27.80 ? 675 HOH A O   1 
HETATM 9142  O  O   . HOH T 6 .   ? 32.326  -16.481 17.409  1.00 27.69 ? 676 HOH A O   1 
HETATM 9143  O  O   . HOH T 6 .   ? 12.586  0.843   -9.125  1.00 38.61 ? 677 HOH A O   1 
HETATM 9144  O  O   . HOH T 6 .   ? 41.874  2.337   29.339  1.00 25.36 ? 678 HOH A O   1 
HETATM 9145  O  O   . HOH T 6 .   ? 17.434  -19.703 26.540  1.00 25.64 ? 679 HOH A O   1 
HETATM 9146  O  O   . HOH T 6 .   ? 22.409  7.263   -4.214  1.00 29.30 ? 680 HOH A O   1 
HETATM 9147  O  O   . HOH T 6 .   ? 20.938  -0.634  -7.276  1.00 34.43 ? 681 HOH A O   1 
HETATM 9148  O  O   . HOH T 6 .   ? 33.684  -15.287 8.502   1.00 30.31 ? 682 HOH A O   1 
HETATM 9149  O  O   . HOH T 6 .   ? 16.742  -20.380 21.353  1.00 37.82 ? 683 HOH A O   1 
HETATM 9150  O  O   . HOH T 6 .   ? 15.151  4.359   -6.610  1.00 30.10 ? 684 HOH A O   1 
HETATM 9151  O  O   . HOH T 6 .   ? 41.716  15.600  4.218   1.00 40.32 ? 685 HOH A O   1 
HETATM 9152  O  O   . HOH T 6 .   ? 24.209  -22.041 18.471  1.00 33.69 ? 686 HOH A O   1 
HETATM 9153  O  O   . HOH T 6 .   ? 28.447  -23.863 8.407   1.00 36.55 ? 687 HOH A O   1 
HETATM 9154  O  O   . HOH T 6 .   ? 25.022  14.220  33.077  1.00 33.85 ? 688 HOH A O   1 
HETATM 9155  O  O   . HOH T 6 .   ? 31.850  -20.035 -1.459  1.00 33.86 ? 689 HOH A O   1 
HETATM 9156  O  O   . HOH T 6 .   ? 21.655  2.320   -6.841  1.00 37.78 ? 690 HOH A O   1 
HETATM 9157  O  O   . HOH T 6 .   ? 17.597  -18.119 5.139   1.00 33.22 ? 691 HOH A O   1 
HETATM 9158  O  O   . HOH T 6 .   ? 42.827  9.548   5.837   1.00 35.21 ? 692 HOH A O   1 
HETATM 9159  O  O   . HOH T 6 .   ? 17.967  19.863  18.502  1.00 56.79 ? 693 HOH A O   1 
HETATM 9160  O  O   . HOH T 6 .   ? 18.261  12.577  20.796  1.00 25.28 ? 694 HOH A O   1 
HETATM 9161  O  O   . HOH T 6 .   ? 12.134  -6.202  -10.304 1.00 32.30 ? 695 HOH A O   1 
HETATM 9162  O  O   . HOH T 6 .   ? 12.674  -3.338  30.916  1.00 27.89 ? 696 HOH A O   1 
HETATM 9163  O  O   . HOH T 6 .   ? 34.707  3.871   31.646  1.00 25.34 ? 697 HOH A O   1 
HETATM 9164  O  O   . HOH T 6 .   ? 28.341  -21.541 2.230   1.00 32.43 ? 698 HOH A O   1 
HETATM 9165  O  O   . HOH T 6 .   ? 21.089  -4.347  32.511  1.00 30.74 ? 699 HOH A O   1 
HETATM 9166  O  O   . HOH T 6 .   ? 24.590  -23.302 10.697  1.00 29.82 ? 700 HOH A O   1 
HETATM 9167  O  O   . HOH T 6 .   ? 9.032   -5.317  -7.016  1.00 28.44 ? 701 HOH A O   1 
HETATM 9168  O  O   . HOH T 6 .   ? 41.122  10.604  0.531   1.00 37.14 ? 702 HOH A O   1 
HETATM 9169  O  O   . HOH T 6 .   ? 35.691  14.864  8.163   1.00 50.12 ? 703 HOH A O   1 
HETATM 9170  O  O   . HOH T 6 .   ? 23.038  15.072  0.307   1.00 31.22 ? 704 HOH A O   1 
HETATM 9171  O  O   . HOH T 6 .   ? 42.525  -0.007  5.517   1.00 29.83 ? 705 HOH A O   1 
HETATM 9172  O  O   . HOH T 6 .   ? 11.723  16.332  15.042  1.00 31.09 ? 706 HOH A O   1 
HETATM 9173  O  O   . HOH T 6 .   ? 43.193  -5.959  0.874   1.00 31.11 ? 707 HOH A O   1 
HETATM 9174  O  O   . HOH T 6 .   ? 20.678  18.059  3.642   1.00 39.17 ? 708 HOH A O   1 
HETATM 9175  O  O   . HOH T 6 .   ? 25.827  14.994  6.584   1.00 34.70 ? 709 HOH A O   1 
HETATM 9176  O  O   . HOH T 6 .   ? 17.495  -16.648 -8.228  1.00 40.20 ? 710 HOH A O   1 
HETATM 9177  O  O   . HOH T 6 .   ? 37.012  5.218   14.121  1.00 29.22 ? 711 HOH A O   1 
HETATM 9178  O  O   . HOH T 6 .   ? 42.532  -2.669  -2.351  1.00 32.28 ? 712 HOH A O   1 
HETATM 9179  O  O   . HOH T 6 .   ? 13.126  -14.363 2.346   1.00 25.93 ? 713 HOH A O   1 
HETATM 9180  O  O   . HOH T 6 .   ? 23.495  -19.862 28.608  1.00 33.23 ? 714 HOH A O   1 
HETATM 9181  O  O   . HOH T 6 .   ? 38.953  -16.360 20.917  1.00 42.98 ? 715 HOH A O   1 
HETATM 9182  O  O   . HOH T 6 .   ? 37.248  1.086   30.148  1.00 27.95 ? 716 HOH A O   1 
HETATM 9183  O  O   . HOH T 6 .   ? 32.858  -15.947 12.769  1.00 29.74 ? 717 HOH A O   1 
HETATM 9184  O  O   . HOH T 6 .   ? 16.820  -18.593 12.476  1.00 28.15 ? 718 HOH A O   1 
HETATM 9185  O  O   . HOH T 6 .   ? 17.875  -6.328  33.720  1.00 32.46 ? 719 HOH A O   1 
HETATM 9186  O  O   . HOH T 6 .   ? 15.566  13.904  -0.564  1.00 33.90 ? 720 HOH A O   1 
HETATM 9187  O  O   . HOH T 6 .   ? 38.236  -11.423 26.669  1.00 32.14 ? 721 HOH A O   1 
HETATM 9188  O  O   . HOH T 6 .   ? 33.761  10.459  21.829  1.00 32.35 ? 722 HOH A O   1 
HETATM 9189  O  O   . HOH T 6 .   ? 41.561  6.203   5.594   1.00 27.50 ? 723 HOH A O   1 
HETATM 9190  O  O   . HOH T 6 .   ? 31.983  -12.310 30.292  1.00 35.79 ? 724 HOH A O   1 
HETATM 9191  O  O   . HOH T 6 .   ? 15.524  16.741  31.192  1.00 34.40 ? 725 HOH A O   1 
HETATM 9192  O  O   . HOH T 6 .   ? 4.883   9.241   14.398  1.00 12.27 ? 726 HOH A O   1 
HETATM 9193  O  O   . HOH T 6 .   ? 4.794   -5.840  9.015   1.00 21.38 ? 727 HOH A O   1 
HETATM 9194  O  O   . HOH T 6 .   ? 31.172  -4.168  37.814  1.00 41.13 ? 728 HOH A O   1 
HETATM 9195  O  O   . HOH U 6 .   ? -22.042 -13.729 -9.173  1.00 41.36 ? 401 HOH B O   1 
HETATM 9196  O  O   . HOH U 6 .   ? 6.595   4.880   13.828  1.00 11.42 ? 402 HOH B O   1 
HETATM 9197  O  O   . HOH U 6 .   ? 4.266   8.204   7.745   1.00 8.49  ? 403 HOH B O   1 
HETATM 9198  O  O   . HOH U 6 .   ? -2.622  5.221   4.045   1.00 7.99  ? 404 HOH B O   1 
HETATM 9199  O  O   . HOH U 6 .   ? 6.036   11.738  7.883   1.00 9.28  ? 405 HOH B O   1 
HETATM 9200  O  O   . HOH U 6 .   ? 7.772   21.475  7.823   1.00 12.02 ? 406 HOH B O   1 
HETATM 9201  O  O   . HOH U 6 .   ? -17.031 -10.449 20.208  1.00 13.03 ? 407 HOH B O   1 
HETATM 9202  O  O   . HOH U 6 .   ? -10.338 -8.968  8.183   1.00 7.41  ? 408 HOH B O   1 
HETATM 9203  O  O   . HOH U 6 .   ? 5.754   12.345  -4.343  1.00 16.43 ? 409 HOH B O   1 
HETATM 9204  O  O   . HOH U 6 .   ? -1.559  16.638  11.103  1.00 11.33 ? 410 HOH B O   1 
HETATM 9205  O  O   . HOH U 6 .   ? -16.963 -10.683 1.335   1.00 12.32 ? 411 HOH B O   1 
HETATM 9206  O  O   . HOH U 6 .   ? 5.367   5.507   7.716   1.00 8.41  ? 412 HOH B O   1 
HETATM 9207  O  O   . HOH U 6 .   ? 3.716   -2.081  13.945  1.00 13.13 ? 413 HOH B O   1 
HETATM 9208  O  O   . HOH U 6 .   ? -4.057  16.095  -11.319 1.00 14.08 ? 414 HOH B O   1 
HETATM 9209  O  O   . HOH U 6 .   ? 5.157   6.357   1.023   1.00 9.64  ? 415 HOH B O   1 
HETATM 9210  O  O   . HOH U 6 .   ? -22.005 1.592   18.692  1.00 20.02 ? 416 HOH B O   1 
HETATM 9211  O  O   . HOH U 6 .   ? -6.769  11.036  -19.615 1.00 12.71 ? 417 HOH B O   1 
HETATM 9212  O  O   . HOH U 6 .   ? 1.731   -1.542  5.853   1.00 8.08  ? 418 HOH B O   1 
HETATM 9213  O  O   . HOH U 6 .   ? -18.328 -8.080  16.070  1.00 15.45 ? 419 HOH B O   1 
HETATM 9214  O  O   . HOH U 6 .   ? -13.956 0.388   15.136  1.00 9.34  ? 420 HOH B O   1 
HETATM 9215  O  O   . HOH U 6 .   ? 1.568   14.391  -11.247 1.00 16.61 ? 421 HOH B O   1 
HETATM 9216  O  O   . HOH U 6 .   ? 5.888   -2.339  1.777   1.00 22.76 ? 422 HOH B O   1 
HETATM 9217  O  O   . HOH U 6 .   ? 6.612   3.367   9.137   1.00 6.52  ? 423 HOH B O   1 
HETATM 9218  O  O   . HOH U 6 .   ? -0.721  12.059  16.235  1.00 11.80 ? 424 HOH B O   1 
HETATM 9219  O  O   . HOH U 6 .   ? 5.914   -9.342  13.542  1.00 13.41 ? 425 HOH B O   1 
HETATM 9220  O  O   . HOH U 6 .   ? -1.094  5.854   -4.936  1.00 11.45 ? 426 HOH B O   1 
HETATM 9221  O  O   . HOH U 6 .   ? 4.204   10.090  -6.783  1.00 15.57 ? 427 HOH B O   1 
HETATM 9222  O  O   . HOH U 6 .   ? -26.158 -9.650  5.971   1.00 21.87 ? 428 HOH B O   1 
HETATM 9223  O  O   . HOH U 6 .   ? -19.643 -13.671 14.363  1.00 19.39 ? 429 HOH B O   1 
HETATM 9224  O  O   . HOH U 6 .   ? -5.576  6.584   0.456   1.00 11.35 ? 430 HOH B O   1 
HETATM 9225  O  O   . HOH U 6 .   ? -13.378 -11.907 11.677  1.00 10.52 ? 431 HOH B O   1 
HETATM 9226  O  O   . HOH U 6 .   ? -12.291 -13.506 -11.331 1.00 15.74 ? 432 HOH B O   1 
HETATM 9227  O  O   . HOH U 6 .   ? 8.091   4.652   5.193   1.00 8.51  ? 433 HOH B O   1 
HETATM 9228  O  O   . HOH U 6 .   ? -30.878 7.334   -4.548  1.00 22.96 ? 434 HOH B O   1 
HETATM 9229  O  O   . HOH U 6 .   ? -21.762 -8.645  -8.464  1.00 17.67 ? 435 HOH B O   1 
HETATM 9230  O  O   . HOH U 6 .   ? -3.596  2.240   -12.038 1.00 12.30 ? 436 HOH B O   1 
HETATM 9231  O  O   . HOH U 6 .   ? -5.791  -12.578 11.819  1.00 14.95 ? 437 HOH B O   1 
HETATM 9232  O  O   . HOH U 6 .   ? -17.803 9.322   -2.657  1.00 16.90 ? 438 HOH B O   1 
HETATM 9233  O  O   . HOH U 6 .   ? -14.070 -14.659 5.855   1.00 16.88 ? 439 HOH B O   1 
HETATM 9234  O  O   . HOH U 6 .   ? 4.283   3.363   -5.929  1.00 18.24 ? 440 HOH B O   1 
HETATM 9235  O  O   . HOH U 6 .   ? -21.427 -11.941 15.903  1.00 23.63 ? 441 HOH B O   1 
HETATM 9236  O  O   . HOH U 6 .   ? -8.893  -20.387 -0.857  1.00 16.80 ? 442 HOH B O   1 
HETATM 9237  O  O   . HOH U 6 .   ? -5.525  1.555   -9.869  1.00 10.47 ? 443 HOH B O   1 
HETATM 9238  O  O   . HOH U 6 .   ? -3.081  7.272   -3.819  1.00 11.14 ? 444 HOH B O   1 
HETATM 9239  O  O   . HOH U 6 .   ? -4.417  11.219  -15.017 1.00 15.22 ? 445 HOH B O   1 
HETATM 9240  O  O   . HOH U 6 .   ? -24.637 -2.424  -6.538  1.00 14.52 ? 446 HOH B O   1 
HETATM 9241  O  O   . HOH U 6 .   ? 8.654   8.769   1.953   1.00 15.75 ? 447 HOH B O   1 
HETATM 9242  O  O   . HOH U 6 .   ? 6.929   -11.429 17.306  1.00 18.85 ? 448 HOH B O   1 
HETATM 9243  O  O   . HOH U 6 .   ? -3.578  13.878  -7.159  1.00 23.54 ? 449 HOH B O   1 
HETATM 9244  O  O   . HOH U 6 .   ? 1.663   9.040   -6.874  1.00 13.60 ? 450 HOH B O   1 
HETATM 9245  O  O   . HOH U 6 .   ? 4.416   6.480   14.164  1.00 10.75 ? 451 HOH B O   1 
HETATM 9246  O  O   . HOH U 6 .   ? -17.608 -12.821 21.197  1.00 22.29 ? 452 HOH B O   1 
HETATM 9247  O  O   . HOH U 6 .   ? -2.860  -5.328  -4.080  1.00 9.14  ? 453 HOH B O   1 
HETATM 9248  O  O   . HOH U 6 .   ? -22.961 -2.101  -8.721  1.00 15.07 ? 454 HOH B O   1 
HETATM 9249  O  O   . HOH U 6 .   ? -12.111 -6.575  30.288  1.00 27.90 ? 455 HOH B O   1 
HETATM 9250  O  O   . HOH U 6 .   ? -20.963 -5.096  21.924  1.00 19.61 ? 456 HOH B O   1 
HETATM 9251  O  O   . HOH U 6 .   ? -3.219  -12.597 -0.984  1.00 17.95 ? 457 HOH B O   1 
HETATM 9252  O  O   . HOH U 6 .   ? -23.129 9.654   6.401   1.00 17.64 ? 458 HOH B O   1 
HETATM 9253  O  O   . HOH U 6 .   ? -5.176  17.857  -7.652  1.00 36.58 ? 459 HOH B O   1 
HETATM 9254  O  O   . HOH U 6 .   ? -20.389 -9.600  15.017  1.00 17.02 ? 460 HOH B O   1 
HETATM 9255  O  O   . HOH U 6 .   ? 2.279   6.067   -12.561 1.00 17.71 ? 461 HOH B O   1 
HETATM 9256  O  O   . HOH U 6 .   ? 1.777   6.554   -8.186  1.00 15.37 ? 462 HOH B O   1 
HETATM 9257  O  O   . HOH U 6 .   ? 5.397   19.953  10.731  1.00 19.67 ? 463 HOH B O   1 
HETATM 9258  O  O   . HOH U 6 .   ? 9.174   7.162   8.486   1.00 12.62 ? 464 HOH B O   1 
HETATM 9259  O  O   . HOH U 6 .   ? -0.028  -13.787 8.819   1.00 28.57 ? 465 HOH B O   1 
HETATM 9260  O  O   . HOH U 6 .   ? -25.190 -7.428  12.756  1.00 21.55 ? 466 HOH B O   1 
HETATM 9261  O  O   . HOH U 6 .   ? -17.808 -10.270 28.606  1.00 18.43 ? 467 HOH B O   1 
HETATM 9262  O  O   . HOH U 6 .   ? -29.567 9.219   6.226   1.00 39.60 ? 468 HOH B O   1 
HETATM 9263  O  O   . HOH U 6 .   ? 6.992   -1.085  17.669  1.00 18.43 ? 469 HOH B O   1 
HETATM 9264  O  O   . HOH U 6 .   ? -23.824 -7.843  20.203  1.00 26.72 ? 470 HOH B O   1 
HETATM 9265  O  O   . HOH U 6 .   ? -17.458 -12.610 3.434   1.00 19.03 ? 471 HOH B O   1 
HETATM 9266  O  O   . HOH U 6 .   ? 5.807   -0.428  -2.399  1.00 19.27 ? 472 HOH B O   1 
HETATM 9267  O  O   . HOH U 6 .   ? -27.624 -4.274  8.507   1.00 15.98 ? 473 HOH B O   1 
HETATM 9268  O  O   . HOH U 6 .   ? -3.755  12.619  -18.297 1.00 17.68 ? 474 HOH B O   1 
HETATM 9269  O  O   . HOH U 6 .   ? -8.988  -7.903  -14.363 1.00 15.57 ? 475 HOH B O   1 
HETATM 9270  O  O   . HOH U 6 .   ? -19.080 -15.999 15.584  1.00 32.30 ? 476 HOH B O   1 
HETATM 9271  O  O   . HOH U 6 .   ? -12.885 -9.114  -12.715 1.00 21.14 ? 477 HOH B O   1 
HETATM 9272  O  O   . HOH U 6 .   ? -13.417 -11.807 -13.091 1.00 23.19 ? 478 HOH B O   1 
HETATM 9273  O  O   . HOH U 6 .   ? -14.316 -10.882 23.844  1.00 20.37 ? 479 HOH B O   1 
HETATM 9274  O  O   . HOH U 6 .   ? -1.467  14.643  17.029  1.00 19.36 ? 480 HOH B O   1 
HETATM 9275  O  O   . HOH U 6 .   ? -1.185  -0.642  -12.589 1.00 16.57 ? 481 HOH B O   1 
HETATM 9276  O  O   . HOH U 6 .   ? -24.551 -1.135  -11.600 1.00 21.89 ? 482 HOH B O   1 
HETATM 9277  O  O   . HOH U 6 .   ? -26.958 -6.205  6.596   1.00 15.20 ? 483 HOH B O   1 
HETATM 9278  O  O   . HOH U 6 .   ? -10.798 17.189  -7.912  1.00 29.64 ? 484 HOH B O   1 
HETATM 9279  O  O   . HOH U 6 .   ? -1.943  -11.444 -3.134  1.00 14.14 ? 485 HOH B O   1 
HETATM 9280  O  O   . HOH U 6 .   ? -24.166 9.026   -1.719  1.00 17.92 ? 486 HOH B O   1 
HETATM 9281  O  O   . HOH U 6 .   ? -13.418 7.512   -15.702 1.00 22.63 ? 487 HOH B O   1 
HETATM 9282  O  O   . HOH U 6 .   ? -20.958 -10.772 -9.875  1.00 23.88 ? 488 HOH B O   1 
HETATM 9283  O  O   . HOH U 6 .   ? -11.200 11.006  2.416   1.00 23.51 ? 489 HOH B O   1 
HETATM 9284  O  O   . HOH U 6 .   ? -10.430 14.314  -13.711 1.00 14.76 ? 490 HOH B O   1 
HETATM 9285  O  O   . HOH U 6 .   ? 7.816   -3.218  3.494   1.00 16.93 ? 491 HOH B O   1 
HETATM 9286  O  O   . HOH U 6 .   ? 5.339   -13.045 15.800  1.00 20.50 ? 492 HOH B O   1 
HETATM 9287  O  O   . HOH U 6 .   ? -3.762  -8.811  -9.120  1.00 22.41 ? 493 HOH B O   1 
HETATM 9288  O  O   . HOH U 6 .   ? -0.404  -13.206 22.641  1.00 31.35 ? 494 HOH B O   1 
HETATM 9289  O  O   . HOH U 6 .   ? 10.039  3.093   22.484  1.00 24.32 ? 495 HOH B O   1 
HETATM 9290  O  O   . HOH U 6 .   ? -30.697 8.170   -11.518 1.00 24.49 ? 496 HOH B O   1 
HETATM 9291  O  O   . HOH U 6 .   ? 0.581   8.136   -4.438  1.00 17.09 ? 497 HOH B O   1 
HETATM 9292  O  O   . HOH U 6 .   ? -17.606 12.615  -12.705 1.00 25.33 ? 498 HOH B O   1 
HETATM 9293  O  O   . HOH U 6 .   ? 2.267   5.173   -5.689  1.00 14.76 ? 499 HOH B O   1 
HETATM 9294  O  O   . HOH U 6 .   ? -0.282  -13.220 -4.197  1.00 24.38 ? 500 HOH B O   1 
HETATM 9295  O  O   . HOH U 6 .   ? 7.796   6.044   0.825   1.00 17.44 ? 501 HOH B O   1 
HETATM 9296  O  O   . HOH U 6 .   ? 3.745   3.481   -2.482  1.00 16.35 ? 502 HOH B O   1 
HETATM 9297  O  O   . HOH U 6 .   ? -24.071 0.828   21.087  1.00 23.10 ? 503 HOH B O   1 
HETATM 9298  O  O   . HOH U 6 .   ? -14.850 -14.645 -2.544  1.00 14.80 ? 504 HOH B O   1 
HETATM 9299  O  O   . HOH U 6 .   ? -2.077  11.734  -5.175  1.00 17.14 ? 505 HOH B O   1 
HETATM 9300  O  O   . HOH U 6 .   ? 5.834   2.181   -3.579  1.00 22.79 ? 506 HOH B O   1 
HETATM 9301  O  O   . HOH U 6 .   ? -13.976 11.093  3.821   1.00 25.94 ? 507 HOH B O   1 
HETATM 9302  O  O   . HOH U 6 .   ? 2.788   -13.156 15.902  1.00 18.21 ? 508 HOH B O   1 
HETATM 9303  O  O   . HOH U 6 .   ? -0.055  16.719  -11.157 1.00 21.63 ? 509 HOH B O   1 
HETATM 9304  O  O   . HOH U 6 .   ? -5.614  -11.594 -14.971 1.00 24.73 ? 510 HOH B O   1 
HETATM 9305  O  O   . HOH U 6 .   ? -3.604  15.321  18.420  1.00 29.29 ? 511 HOH B O   1 
HETATM 9306  O  O   . HOH U 6 .   ? -16.525 -12.336 25.603  1.00 19.57 ? 512 HOH B O   1 
HETATM 9307  O  O   . HOH U 6 .   ? -1.901  9.606   -3.266  1.00 14.52 ? 513 HOH B O   1 
HETATM 9308  O  O   . HOH U 6 .   ? -26.277 9.239   16.562  1.00 27.67 ? 514 HOH B O   1 
HETATM 9309  O  O   . HOH U 6 .   ? -5.826  15.582  -0.828  1.00 38.16 ? 515 HOH B O   1 
HETATM 9310  O  O   . HOH U 6 .   ? -7.707  -10.065 -15.968 1.00 19.57 ? 516 HOH B O   1 
HETATM 9311  O  O   . HOH U 6 .   ? -14.559 -14.058 0.759   1.00 14.83 ? 517 HOH B O   1 
HETATM 9312  O  O   . HOH U 6 .   ? 7.307   -11.291 24.136  1.00 21.45 ? 518 HOH B O   1 
HETATM 9313  O  O   . HOH U 6 .   ? -15.821 -0.263  -14.896 1.00 22.39 ? 519 HOH B O   1 
HETATM 9314  O  O   . HOH U 6 .   ? -3.247  2.622   21.333  1.00 23.44 ? 520 HOH B O   1 
HETATM 9315  O  O   . HOH U 6 .   ? 11.366  14.585  -0.182  1.00 22.70 ? 521 HOH B O   1 
HETATM 9316  O  O   . HOH U 6 .   ? 7.791   11.926  14.887  1.00 20.95 ? 522 HOH B O   1 
HETATM 9317  O  O   . HOH U 6 .   ? -10.692 -10.430 29.702  1.00 20.64 ? 523 HOH B O   1 
HETATM 9318  O  O   . HOH U 6 .   ? -2.709  -0.280  25.307  1.00 31.15 ? 524 HOH B O   1 
HETATM 9319  O  O   . HOH U 6 .   ? -20.257 -11.825 8.122   1.00 23.73 ? 525 HOH B O   1 
HETATM 9320  O  O   . HOH U 6 .   ? -0.657  -14.298 6.419   1.00 32.22 ? 526 HOH B O   1 
HETATM 9321  O  O   . HOH U 6 .   ? -15.597 -14.641 3.466   1.00 25.94 ? 527 HOH B O   1 
HETATM 9322  O  O   . HOH U 6 .   ? -18.628 -11.894 23.725  1.00 25.41 ? 528 HOH B O   1 
HETATM 9323  O  O   . HOH U 6 .   ? -21.674 -13.582 18.340  1.00 37.28 ? 529 HOH B O   1 
HETATM 9324  O  O   . HOH U 6 .   ? 4.355   -2.089  6.477   1.00 15.55 ? 530 HOH B O   1 
HETATM 9325  O  O   . HOH U 6 .   ? -4.788  0.346   21.969  1.00 20.33 ? 531 HOH B O   1 
HETATM 9326  O  O   . HOH U 6 .   ? 4.008   -2.282  -3.289  1.00 24.93 ? 532 HOH B O   1 
HETATM 9327  O  O   . HOH U 6 .   ? -17.720 -3.859  26.717  1.00 20.60 ? 533 HOH B O   1 
HETATM 9328  O  O   . HOH U 6 .   ? 5.636   -8.189  -1.333  1.00 25.04 ? 534 HOH B O   1 
HETATM 9329  O  O   . HOH U 6 .   ? -29.237 -7.552  6.366   1.00 24.31 ? 535 HOH B O   1 
HETATM 9330  O  O   . HOH U 6 .   ? 5.251   16.002  13.422  1.00 23.80 ? 536 HOH B O   1 
HETATM 9331  O  O   . HOH U 6 .   ? -20.957 3.821   -12.988 1.00 18.42 ? 537 HOH B O   1 
HETATM 9332  O  O   . HOH U 6 .   ? -23.371 -8.966  14.318  1.00 26.16 ? 538 HOH B O   1 
HETATM 9333  O  O   . HOH U 6 .   ? -11.538 -8.248  -15.008 1.00 24.14 ? 539 HOH B O   1 
HETATM 9334  O  O   . HOH U 6 .   ? -20.928 -11.040 5.652   1.00 30.89 ? 540 HOH B O   1 
HETATM 9335  O  O   . HOH U 6 .   ? -4.671  14.344  -4.680  1.00 31.39 ? 541 HOH B O   1 
HETATM 9336  O  O   . HOH U 6 .   ? -27.301 6.694   -11.924 1.00 30.64 ? 542 HOH B O   1 
HETATM 9337  O  O   . HOH U 6 .   ? -3.705  19.202  -20.010 1.00 25.38 ? 543 HOH B O   1 
HETATM 9338  O  O   . HOH U 6 .   ? 8.821   6.450   -2.064  1.00 26.87 ? 544 HOH B O   1 
HETATM 9339  O  O   . HOH U 6 .   ? 2.918   -3.389  16.406  1.00 26.12 ? 545 HOH B O   1 
HETATM 9340  O  O   . HOH U 6 .   ? 4.768   -9.664  -12.215 1.00 21.11 ? 546 HOH B O   1 
HETATM 9341  O  O   . HOH U 6 .   ? -12.516 -0.558  22.799  1.00 22.08 ? 547 HOH B O   1 
HETATM 9342  O  O   . HOH U 6 .   ? -17.031 11.320  1.839   1.00 29.47 ? 548 HOH B O   1 
HETATM 9343  O  O   . HOH U 6 .   ? -0.808  16.055  -8.666  1.00 23.23 ? 549 HOH B O   1 
HETATM 9344  O  O   . HOH U 6 .   ? -23.899 -10.834 5.362   1.00 35.01 ? 550 HOH B O   1 
HETATM 9345  O  O   . HOH U 6 .   ? -16.066 14.573  -14.231 1.00 33.94 ? 551 HOH B O   1 
HETATM 9346  O  O   . HOH U 6 .   ? -35.278 7.127   2.964   1.00 25.79 ? 552 HOH B O   1 
HETATM 9347  O  O   . HOH U 6 .   ? -13.284 -3.089  27.128  1.00 39.53 ? 553 HOH B O   1 
HETATM 9348  O  O   . HOH U 6 .   ? -19.473 -0.564  -16.348 1.00 29.62 ? 554 HOH B O   1 
HETATM 9349  O  O   . HOH U 6 .   ? 3.375   -11.271 3.464   1.00 31.30 ? 555 HOH B O   1 
HETATM 9350  O  O   . HOH U 6 .   ? 4.113   -9.212  3.119   1.00 20.46 ? 556 HOH B O   1 
HETATM 9351  O  O   . HOH U 6 .   ? 1.175   13.124  19.587  1.00 26.81 ? 557 HOH B O   1 
HETATM 9352  O  O   . HOH U 6 .   ? -10.865 16.954  -18.585 1.00 30.91 ? 558 HOH B O   1 
HETATM 9353  O  O   . HOH U 6 .   ? -27.063 -7.271  10.441  1.00 35.68 ? 559 HOH B O   1 
HETATM 9354  O  O   . HOH U 6 .   ? -0.482  -12.437 15.402  1.00 28.74 ? 560 HOH B O   1 
HETATM 9355  O  O   . HOH U 6 .   ? 6.018   -6.009  14.792  1.00 18.30 ? 561 HOH B O   1 
HETATM 9356  O  O   . HOH U 6 .   ? -1.489  13.996  -4.507  1.00 23.37 ? 562 HOH B O   1 
HETATM 9357  O  O   . HOH U 6 .   ? -3.082  -12.849 15.338  1.00 22.78 ? 563 HOH B O   1 
HETATM 9358  O  O   . HOH U 6 .   ? -31.826 5.508   -7.710  1.00 22.22 ? 564 HOH B O   1 
HETATM 9359  O  O   . HOH U 6 .   ? -5.950  11.298  20.749  1.00 27.36 ? 565 HOH B O   1 
HETATM 9360  O  O   . HOH U 6 .   ? -8.801  1.633   -19.533 1.00 35.19 ? 566 HOH B O   1 
HETATM 9361  O  O   . HOH U 6 .   ? -21.440 -9.930  9.861   1.00 30.95 ? 567 HOH B O   1 
HETATM 9362  O  O   . HOH U 6 .   ? 13.100  13.619  -1.976  1.00 29.16 ? 568 HOH B O   1 
HETATM 9363  O  O   . HOH U 6 .   ? -3.875  20.965  -18.318 1.00 32.87 ? 569 HOH B O   1 
HETATM 9364  O  O   . HOH U 6 .   ? 5.011   -7.278  1.211   1.00 18.85 ? 570 HOH B O   1 
HETATM 9365  O  O   . HOH U 6 .   ? -17.623 -14.143 -2.197  1.00 22.49 ? 571 HOH B O   1 
HETATM 9366  O  O   . HOH U 6 .   ? 2.705   6.743   16.736  1.00 23.21 ? 572 HOH B O   1 
HETATM 9367  O  O   . HOH U 6 .   ? -2.722  1.553   -14.432 1.00 26.00 ? 573 HOH B O   1 
HETATM 9368  O  O   . HOH U 6 .   ? -26.578 10.609  5.049   1.00 35.20 ? 574 HOH B O   1 
HETATM 9369  O  O   . HOH U 6 .   ? -10.459 -13.194 30.542  1.00 23.04 ? 575 HOH B O   1 
HETATM 9370  O  O   . HOH U 6 .   ? -20.099 -11.782 0.576   1.00 31.57 ? 576 HOH B O   1 
HETATM 9371  O  O   . HOH U 6 .   ? 4.083   11.302  -13.358 1.00 30.46 ? 577 HOH B O   1 
HETATM 9372  O  O   . HOH U 6 .   ? -26.858 9.789   12.459  1.00 33.11 ? 578 HOH B O   1 
HETATM 9373  O  O   . HOH U 6 .   ? -17.531 14.672  6.931   1.00 31.51 ? 579 HOH B O   1 
HETATM 9374  O  O   . HOH U 6 .   ? -5.866  -15.296 13.151  1.00 25.90 ? 580 HOH B O   1 
HETATM 9375  O  O   . HOH U 6 .   ? 2.228   -15.893 16.428  1.00 29.19 ? 581 HOH B O   1 
HETATM 9376  O  O   . HOH U 6 .   ? -19.339 -16.540 -3.943  1.00 27.85 ? 582 HOH B O   1 
HETATM 9377  O  O   . HOH U 6 .   ? 6.516   0.965   22.092  1.00 31.52 ? 583 HOH B O   1 
HETATM 9378  O  O   . HOH U 6 .   ? 3.678   18.123  -15.497 1.00 28.38 ? 584 HOH B O   1 
HETATM 9379  O  O   . HOH U 6 .   ? -6.587  -8.899  -18.351 1.00 22.04 ? 585 HOH B O   1 
HETATM 9380  O  O   . HOH U 6 .   ? -8.097  -5.564  -15.510 1.00 23.49 ? 586 HOH B O   1 
HETATM 9381  O  O   . HOH U 6 .   ? 5.392   11.397  -11.094 1.00 45.28 ? 587 HOH B O   1 
HETATM 9382  O  O   . HOH U 6 .   ? -13.443 -6.811  -11.179 1.00 18.39 ? 588 HOH B O   1 
HETATM 9383  O  O   . HOH U 6 .   ? 3.510   21.349  9.534   1.00 23.63 ? 589 HOH B O   1 
HETATM 9384  O  O   . HOH U 6 .   ? -26.691 -6.998  -1.530  1.00 22.03 ? 590 HOH B O   1 
HETATM 9385  O  O   . HOH U 6 .   ? -22.705 6.008   -12.606 1.00 23.81 ? 591 HOH B O   1 
HETATM 9386  O  O   . HOH U 6 .   ? -7.099  7.083   19.156  1.00 21.83 ? 592 HOH B O   1 
HETATM 9387  O  O   . HOH U 6 .   ? -9.563  16.717  -16.101 1.00 22.21 ? 593 HOH B O   1 
HETATM 9388  O  O   . HOH U 6 .   ? -30.230 -3.634  9.944   1.00 24.93 ? 594 HOH B O   1 
HETATM 9389  O  O   . HOH U 6 .   ? -16.116 -5.840  -12.907 1.00 22.04 ? 595 HOH B O   1 
HETATM 9390  O  O   . HOH U 6 .   ? -27.193 -10.020 1.601   1.00 25.79 ? 596 HOH B O   1 
HETATM 9391  O  O   . HOH U 6 .   ? -14.505 13.854  -16.116 1.00 25.34 ? 597 HOH B O   1 
HETATM 9392  O  O   . HOH U 6 .   ? 4.447   17.148  3.613   1.00 22.57 ? 598 HOH B O   1 
HETATM 9393  O  O   . HOH U 6 .   ? -29.299 2.475   5.615   1.00 22.95 ? 599 HOH B O   1 
HETATM 9394  O  O   . HOH U 6 .   ? -3.566  16.305  -8.683  1.00 21.37 ? 600 HOH B O   1 
HETATM 9395  O  O   . HOH U 6 .   ? -3.026  18.957  10.747  1.00 24.42 ? 601 HOH B O   1 
HETATM 9396  O  O   . HOH U 6 .   ? -7.611  -7.646  28.450  1.00 28.58 ? 602 HOH B O   1 
HETATM 9397  O  O   . HOH U 6 .   ? 1.147   18.069  -13.893 1.00 24.62 ? 603 HOH B O   1 
HETATM 9398  O  O   . HOH U 6 .   ? 4.999   -3.231  17.504  1.00 25.63 ? 604 HOH B O   1 
HETATM 9399  O  O   . HOH U 6 .   ? 5.781   9.957   -9.000  1.00 26.97 ? 605 HOH B O   1 
HETATM 9400  O  O   . HOH U 6 .   ? -29.755 -3.062  6.969   1.00 22.86 ? 606 HOH B O   1 
HETATM 9401  O  O   . HOH U 6 .   ? -29.164 7.371   -1.648  1.00 25.73 ? 607 HOH B O   1 
HETATM 9402  O  O   . HOH U 6 .   ? -30.900 2.241   1.982   1.00 29.70 ? 608 HOH B O   1 
HETATM 9403  O  O   . HOH U 6 .   ? -24.765 8.433   1.034   1.00 24.86 ? 609 HOH B O   1 
HETATM 9404  O  O   . HOH U 6 .   ? 3.737   15.097  1.624   1.00 29.97 ? 610 HOH B O   1 
HETATM 9405  O  O   . HOH U 6 .   ? -14.629 -13.499 23.953  1.00 27.34 ? 611 HOH B O   1 
HETATM 9406  O  O   . HOH U 6 .   ? -22.891 -4.412  -10.322 1.00 24.67 ? 612 HOH B O   1 
HETATM 9407  O  O   . HOH U 6 .   ? -29.935 -1.451  -9.817  1.00 25.81 ? 613 HOH B O   1 
HETATM 9408  O  O   . HOH U 6 .   ? -27.230 -3.489  -5.784  1.00 23.82 ? 614 HOH B O   1 
HETATM 9409  O  O   . HOH U 6 .   ? -2.656  -10.797 -14.882 1.00 28.05 ? 615 HOH B O   1 
HETATM 9410  O  O   . HOH U 6 .   ? -20.039 -12.226 -2.236  1.00 28.41 ? 616 HOH B O   1 
HETATM 9411  O  O   . HOH U 6 .   ? -29.549 7.246   1.109   1.00 28.17 ? 617 HOH B O   1 
HETATM 9412  O  O   . HOH U 6 .   ? -23.288 11.520  -1.219  1.00 23.62 ? 618 HOH B O   1 
HETATM 9413  O  O   . HOH U 6 .   ? 4.660   -11.878 24.859  1.00 31.36 ? 619 HOH B O   1 
HETATM 9414  O  O   . HOH U 6 .   ? -1.448  -9.802  -10.477 1.00 29.58 ? 620 HOH B O   1 
HETATM 9415  O  O   . HOH U 6 .   ? -17.255 -16.826 3.477   1.00 32.17 ? 621 HOH B O   1 
HETATM 9416  O  O   . HOH U 6 .   ? -11.073 -17.944 21.130  1.00 41.09 ? 622 HOH B O   1 
HETATM 9417  O  O   . HOH U 6 .   ? -18.647 6.444   23.479  1.00 30.15 ? 623 HOH B O   1 
HETATM 9418  O  O   . HOH U 6 .   ? 8.380   10.526  -7.558  1.00 36.95 ? 624 HOH B O   1 
HETATM 9419  O  O   . HOH U 6 .   ? -20.190 13.123  7.658   1.00 24.26 ? 625 HOH B O   1 
HETATM 9420  O  O   . HOH U 6 .   ? -27.364 -6.240  -4.697  1.00 24.80 ? 626 HOH B O   1 
HETATM 9421  O  O   . HOH U 6 .   ? -17.617 13.444  -4.355  1.00 30.42 ? 627 HOH B O   1 
HETATM 9422  O  O   . HOH U 6 .   ? -17.137 9.622   23.485  1.00 33.30 ? 628 HOH B O   1 
HETATM 9423  O  O   . HOH U 6 .   ? -11.717 -19.851 24.840  1.00 35.28 ? 629 HOH B O   1 
HETATM 9424  O  O   . HOH U 6 .   ? -5.373  6.232   23.551  1.00 47.02 ? 630 HOH B O   1 
HETATM 9425  O  O   . HOH U 6 .   ? 4.483   15.364  17.969  1.00 28.07 ? 631 HOH B O   1 
HETATM 9426  O  O   . HOH U 6 .   ? -31.889 -0.712  14.134  1.00 25.66 ? 632 HOH B O   1 
HETATM 9427  O  O   . HOH U 6 .   ? -5.913  2.412   -16.882 1.00 30.56 ? 633 HOH B O   1 
HETATM 9428  O  O   . HOH U 6 .   ? 1.302   0.550   -16.191 1.00 28.41 ? 634 HOH B O   1 
HETATM 9429  O  O   . HOH U 6 .   ? 4.173   -4.727  0.847   1.00 28.05 ? 635 HOH B O   1 
HETATM 9430  O  O   . HOH U 6 .   ? 4.305   14.901  -10.728 1.00 35.38 ? 636 HOH B O   1 
HETATM 9431  O  O   . HOH U 6 .   ? -30.618 2.169   10.457  1.00 28.03 ? 637 HOH B O   1 
HETATM 9432  O  O   . HOH U 6 .   ? -13.873 13.745  -2.535  1.00 35.07 ? 638 HOH B O   1 
HETATM 9433  O  O   . HOH U 6 .   ? -13.854 9.607   -18.066 1.00 35.25 ? 639 HOH B O   1 
HETATM 9434  O  O   . HOH U 6 .   ? -7.864  18.060  10.789  1.00 31.95 ? 640 HOH B O   1 
HETATM 9435  O  O   . HOH U 6 .   ? -8.691  14.800  -2.040  1.00 30.43 ? 641 HOH B O   1 
HETATM 9436  O  O   . HOH U 6 .   ? 1.431   -0.629  -11.952 1.00 26.56 ? 642 HOH B O   1 
HETATM 9437  O  O   . HOH U 6 .   ? -1.827  20.709  13.052  1.00 35.81 ? 643 HOH B O   1 
HETATM 9438  O  O   . HOH U 6 .   ? -4.271  -12.760 28.575  1.00 26.42 ? 644 HOH B O   1 
HETATM 9439  O  O   . HOH U 6 .   ? -27.913 7.066   19.591  1.00 42.20 ? 645 HOH B O   1 
HETATM 9440  O  O   . HOH U 6 .   ? -6.621  -11.449 29.163  1.00 27.73 ? 646 HOH B O   1 
HETATM 9441  O  O   . HOH U 6 .   ? 3.690   6.219   -10.044 1.00 25.22 ? 647 HOH B O   1 
HETATM 9442  O  O   . HOH U 6 .   ? 1.236   22.502  9.781   1.00 30.65 ? 648 HOH B O   1 
HETATM 9443  O  O   . HOH U 6 .   ? -27.775 -8.417  -6.207  1.00 44.41 ? 649 HOH B O   1 
HETATM 9444  O  O   . HOH U 6 .   ? -31.520 -6.361  -5.460  1.00 35.86 ? 650 HOH B O   1 
HETATM 9445  O  O   . HOH U 6 .   ? 6.666   -13.494 20.104  1.00 27.05 ? 651 HOH B O   1 
HETATM 9446  O  O   . HOH U 6 .   ? -10.261 -3.963  -15.853 1.00 29.62 ? 652 HOH B O   1 
HETATM 9447  O  O   . HOH U 6 .   ? -12.985 -17.393 6.992   1.00 33.75 ? 653 HOH B O   1 
HETATM 9448  O  O   . HOH U 6 .   ? 0.789   15.593  17.835  1.00 38.05 ? 654 HOH B O   1 
HETATM 9449  O  O   . HOH U 6 .   ? -0.471  3.929   -16.812 1.00 26.47 ? 655 HOH B O   1 
HETATM 9450  O  O   . HOH U 6 .   ? -10.991 15.096  -5.307  1.00 35.52 ? 656 HOH B O   1 
HETATM 9451  O  O   . HOH U 6 .   ? -28.670 -6.662  15.569  1.00 31.97 ? 657 HOH B O   1 
HETATM 9452  O  O   . HOH U 6 .   ? 2.768   15.855  16.478  1.00 35.27 ? 658 HOH B O   1 
HETATM 9453  O  O   . HOH U 6 .   ? -26.545 -3.098  -10.758 1.00 29.89 ? 659 HOH B O   1 
HETATM 9454  O  O   . HOH U 6 .   ? -34.977 5.680   -5.158  1.00 28.77 ? 660 HOH B O   1 
HETATM 9455  O  O   . HOH U 6 .   ? 5.030   21.998  12.704  1.00 36.83 ? 661 HOH B O   1 
HETATM 9456  O  O   . HOH U 6 .   ? 8.484   -13.743 17.586  1.00 38.53 ? 662 HOH B O   1 
HETATM 9457  O  O   . HOH U 6 .   ? 6.112   20.482  -5.485  1.00 23.57 ? 663 HOH B O   1 
HETATM 9458  O  O   . HOH U 6 .   ? -2.110  10.989  21.142  1.00 36.76 ? 664 HOH B O   1 
HETATM 9459  O  O   . HOH U 6 .   ? -4.427  -13.691 9.639   1.00 32.77 ? 665 HOH B O   1 
HETATM 9460  O  O   . HOH U 6 .   ? -2.375  -12.593 24.709  1.00 34.25 ? 666 HOH B O   1 
HETATM 9461  O  O   . HOH U 6 .   ? -20.466 -4.285  26.069  1.00 26.49 ? 667 HOH B O   1 
HETATM 9462  O  O   . HOH U 6 .   ? -2.411  -14.623 9.216   1.00 34.04 ? 668 HOH B O   1 
HETATM 9463  O  O   . HOH U 6 .   ? -21.601 -6.840  -9.938  1.00 31.61 ? 669 HOH B O   1 
HETATM 9464  O  O   . HOH U 6 .   ? -19.885 -7.628  -11.570 1.00 32.77 ? 670 HOH B O   1 
HETATM 9465  O  O   . HOH U 6 .   ? -25.321 5.702   -12.919 1.00 32.30 ? 671 HOH B O   1 
HETATM 9466  O  O   . HOH U 6 .   ? -15.729 8.478   -16.910 1.00 33.64 ? 672 HOH B O   1 
HETATM 9467  O  O   . HOH U 6 .   ? -20.766 7.869   -14.204 1.00 32.50 ? 673 HOH B O   1 
HETATM 9468  O  O   . HOH U 6 .   ? -16.655 -16.803 16.601  1.00 33.62 ? 674 HOH B O   1 
HETATM 9469  O  O   . HOH U 6 .   ? -1.760  20.437  8.473   1.00 27.49 ? 675 HOH B O   1 
HETATM 9470  O  O   . HOH U 6 .   ? 0.883   -12.784 -7.117  1.00 35.70 ? 676 HOH B O   1 
HETATM 9471  O  O   . HOH U 6 .   ? -0.487  -12.200 -8.800  1.00 22.56 ? 677 HOH B O   1 
HETATM 9472  O  O   . HOH U 6 .   ? -8.078  -1.399  -15.853 1.00 36.45 ? 678 HOH B O   1 
HETATM 9473  O  O   . HOH U 6 .   ? -0.865  18.092  0.821   1.00 35.06 ? 679 HOH B O   1 
HETATM 9474  O  O   . HOH U 6 .   ? 0.980   24.235  -4.427  1.00 32.12 ? 680 HOH B O   1 
HETATM 9475  O  O   . HOH U 6 .   ? 3.076   24.982  -1.258  1.00 26.84 ? 681 HOH B O   1 
HETATM 9476  O  O   . HOH U 6 .   ? 6.212   16.845  0.870   1.00 21.84 ? 682 HOH B O   1 
HETATM 9477  O  O   . HOH U 6 .   ? -16.981 11.303  4.613   1.00 37.86 ? 683 HOH B O   1 
HETATM 9478  O  O   . HOH U 6 .   ? -12.064 12.161  0.306   1.00 30.25 ? 684 HOH B O   1 
HETATM 9479  O  O   . HOH U 6 .   ? -17.618 -16.656 -6.012  1.00 26.80 ? 685 HOH B O   1 
HETATM 9480  O  O   . HOH U 6 .   ? 4.189   -13.396 22.543  1.00 35.89 ? 686 HOH B O   1 
HETATM 9481  O  O   . HOH U 6 .   ? -21.401 15.776  -5.668  1.00 31.10 ? 687 HOH B O   1 
HETATM 9482  O  O   . HOH U 6 .   ? -5.517  18.248  11.861  1.00 29.92 ? 688 HOH B O   1 
HETATM 9483  O  O   . HOH U 6 .   ? -20.297 -13.316 11.607  1.00 27.77 ? 689 HOH B O   1 
HETATM 9484  O  O   . HOH U 6 .   ? 2.431   -11.421 -11.868 1.00 32.40 ? 690 HOH B O   1 
HETATM 9485  O  O   . HOH U 6 .   ? 3.707   -13.881 -12.170 1.00 38.01 ? 691 HOH B O   1 
HETATM 9486  O  O   . HOH U 6 .   ? -33.514 3.126   2.628   1.00 31.20 ? 692 HOH B O   1 
HETATM 9487  O  O   . HOH U 6 .   ? 6.255   -9.786  -9.879  1.00 32.35 ? 693 HOH B O   1 
HETATM 9488  O  O   . HOH U 6 .   ? -16.270 5.433   21.962  1.00 28.18 ? 694 HOH B O   1 
HETATM 9489  O  O   . HOH U 6 .   ? -9.486  7.617   19.770  1.00 38.05 ? 695 HOH B O   1 
HETATM 9490  O  O   . HOH U 6 .   ? -4.115  19.322  8.220   1.00 31.51 ? 696 HOH B O   1 
HETATM 9491  O  O   . HOH U 6 .   ? -26.478 9.166   -2.941  1.00 28.19 ? 697 HOH B O   1 
HETATM 9492  O  O   . HOH U 6 .   ? -13.491 20.486  14.273  1.00 33.86 ? 698 HOH B O   1 
HETATM 9493  O  O   . HOH U 6 .   ? -13.606 15.567  -18.181 1.00 36.51 ? 699 HOH B O   1 
HETATM 9494  O  O   . HOH U 6 .   ? 1.918   -15.184 23.058  1.00 30.53 ? 700 HOH B O   1 
HETATM 9495  O  O   . HOH U 6 .   ? -29.270 4.177   17.369  1.00 39.89 ? 701 HOH B O   1 
HETATM 9496  O  O   . HOH U 6 .   ? -13.174 17.906  -8.750  1.00 27.31 ? 702 HOH B O   1 
HETATM 9497  O  O   . HOH U 6 .   ? -29.315 -5.903  -2.744  1.00 32.80 ? 703 HOH B O   1 
HETATM 9498  O  O   . HOH U 6 .   ? -8.572  -16.777 9.633   1.00 42.80 ? 704 HOH B O   1 
HETATM 9499  O  O   . HOH U 6 .   ? -1.546  18.155  14.231  1.00 30.50 ? 705 HOH B O   1 
HETATM 9500  O  O   . HOH U 6 .   ? 13.390  15.736  -3.977  1.00 27.97 ? 706 HOH B O   1 
HETATM 9501  O  O   . HOH U 6 .   ? -10.262 -3.050  24.683  1.00 34.97 ? 707 HOH B O   1 
HETATM 9502  O  O   . HOH U 6 .   ? 3.950   -14.703 9.726   1.00 35.37 ? 708 HOH B O   1 
HETATM 9503  O  O   . HOH U 6 .   ? 1.881   -11.391 24.861  1.00 32.37 ? 709 HOH B O   1 
HETATM 9504  O  O   . HOH U 6 .   ? -14.166 -2.051  -13.657 1.00 38.23 ? 710 HOH B O   1 
HETATM 9505  O  O   . HOH U 6 .   ? 5.981   2.933   -8.047  1.00 34.07 ? 711 HOH B O   1 
HETATM 9506  O  O   . HOH U 6 .   ? -19.905 -15.849 10.387  1.00 27.42 ? 712 HOH B O   1 
HETATM 9507  O  O   . HOH U 6 .   ? -0.688  22.450  0.392   1.00 50.79 ? 713 HOH B O   1 
HETATM 9508  O  O   . HOH U 6 .   ? 2.770   15.857  -5.013  1.00 38.56 ? 714 HOH B O   1 
HETATM 9509  O  O   . HOH U 6 .   ? 6.239   18.909  2.268   1.00 35.89 ? 715 HOH B O   1 
HETATM 9510  O  O   . HOH U 6 .   ? 4.194   -6.040  24.759  1.00 31.21 ? 716 HOH B O   1 
HETATM 9511  O  O   . HOH U 6 .   ? -1.622  -8.124  -8.977  1.00 24.14 ? 717 HOH B O   1 
HETATM 9512  O  O   . HOH U 6 .   ? -13.889 -4.967  -12.956 1.00 37.54 ? 718 HOH B O   1 
HETATM 9513  O  O   . HOH U 6 .   ? -16.596 6.629   -18.334 1.00 39.16 ? 719 HOH B O   1 
HETATM 9514  O  O   . HOH U 6 .   ? -13.249 13.861  -5.302  1.00 37.56 ? 720 HOH B O   1 
HETATM 9515  O  O   . HOH U 6 .   ? -19.142 -15.698 6.544   1.00 39.60 ? 721 HOH B O   1 
HETATM 9516  O  O   . HOH U 6 .   ? -9.496  -17.968 12.674  1.00 40.25 ? 722 HOH B O   1 
HETATM 9517  O  O   . HOH U 6 .   ? -5.935  15.328  2.154   1.00 40.88 ? 723 HOH B O   1 
HETATM 9518  O  O   . HOH U 6 .   ? -7.894  -20.959 17.005  1.00 35.26 ? 724 HOH B O   1 
HETATM 9519  O  O   . HOH U 6 .   ? 9.645   -13.491 24.166  1.00 37.58 ? 725 HOH B O   1 
HETATM 9520  O  O   . HOH U 6 .   ? 0.930   -8.854  25.440  1.00 32.24 ? 726 HOH B O   1 
HETATM 9521  O  O   . HOH U 6 .   ? -17.211 9.903   -14.398 1.00 37.95 ? 727 HOH B O   1 
HETATM 9522  O  O   . HOH U 6 .   ? -6.526  15.703  15.742  1.00 29.33 ? 728 HOH B O   1 
HETATM 9523  O  O   . HOH U 6 .   ? -14.655 -14.340 19.847  1.00 32.83 ? 729 HOH B O   1 
HETATM 9524  O  O   . HOH U 6 .   ? -5.184  18.246  3.390   1.00 40.45 ? 730 HOH B O   1 
HETATM 9525  O  O   . HOH U 6 .   ? -8.847  14.555  0.718   1.00 41.98 ? 731 HOH B O   1 
HETATM 9526  O  O   . HOH V 6 .   ? 25.882  12.856  -35.377 1.00 11.69 ? 401 HOH C O   1 
HETATM 9527  O  O   . HOH V 6 .   ? 32.527  11.208  -43.296 1.00 11.29 ? 402 HOH C O   1 
HETATM 9528  O  O   . HOH V 6 .   ? 26.731  9.251   -34.739 1.00 11.87 ? 403 HOH C O   1 
HETATM 9529  O  O   . HOH V 6 .   ? 26.167  6.882   -41.215 1.00 10.76 ? 404 HOH C O   1 
HETATM 9530  O  O   . HOH V 6 .   ? 25.225  -1.768  -40.702 1.00 10.17 ? 405 HOH C O   1 
HETATM 9531  O  O   . HOH V 6 .   ? 20.192  -10.253 -29.852 1.00 20.84 ? 406 HOH C O   1 
HETATM 9532  O  O   . HOH V 6 .   ? 34.157  15.903  -38.407 1.00 12.84 ? 407 HOH C O   1 
HETATM 9533  O  O   . HOH V 6 .   ? 43.296  -2.536  -40.471 1.00 12.83 ? 408 HOH C O   1 
HETATM 9534  O  O   . HOH V 6 .   ? 25.068  6.430   -34.642 1.00 10.65 ? 409 HOH C O   1 
HETATM 9535  O  O   . HOH V 6 .   ? 23.730  5.638   -40.726 1.00 11.98 ? 410 HOH C O   1 
HETATM 9536  O  O   . HOH V 6 .   ? 31.973  2.357   -43.790 1.00 13.18 ? 411 HOH C O   1 
HETATM 9537  O  O   . HOH V 6 .   ? 23.426  4.660   -36.015 1.00 7.80  ? 412 HOH C O   1 
HETATM 9538  O  O   . HOH V 6 .   ? 24.288  -0.831  -32.918 1.00 17.16 ? 413 HOH C O   1 
HETATM 9539  O  O   . HOH V 6 .   ? 27.125  -0.962  -32.228 1.00 9.33  ? 414 HOH C O   1 
HETATM 9540  O  O   . HOH V 6 .   ? 28.677  3.585   -46.282 1.00 16.55 ? 415 HOH C O   1 
HETATM 9541  O  O   . HOH V 6 .   ? 29.714  -5.122  -22.123 1.00 18.13 ? 416 HOH C O   1 
HETATM 9542  O  O   . HOH V 6 .   ? 28.460  18.172  -31.678 1.00 17.27 ? 417 HOH C O   1 
HETATM 9543  O  O   . HOH V 6 .   ? 39.639  17.922  -40.794 1.00 25.99 ? 418 HOH C O   1 
HETATM 9544  O  O   . HOH V 6 .   ? 22.550  10.838  -29.267 1.00 15.96 ? 419 HOH C O   1 
HETATM 9545  O  O   . HOH V 6 .   ? 38.318  4.843   -45.255 1.00 15.87 ? 420 HOH C O   1 
HETATM 9546  O  O   . HOH V 6 .   ? 25.917  -3.504  -42.676 1.00 15.74 ? 421 HOH C O   1 
HETATM 9547  O  O   . HOH V 6 .   ? 33.856  13.394  -44.228 1.00 16.94 ? 422 HOH C O   1 
HETATM 9548  O  O   . HOH V 6 .   ? 26.501  9.577   -41.842 1.00 13.86 ? 423 HOH C O   1 
HETATM 9549  O  O   . HOH V 6 .   ? 29.250  5.953   -47.407 1.00 16.03 ? 424 HOH C O   1 
HETATM 9550  O  O   . HOH V 6 .   ? 28.656  3.158   -43.534 1.00 14.23 ? 425 HOH C O   1 
HETATM 9551  O  O   . HOH V 6 .   ? 35.644  -13.715 -54.552 1.00 20.56 ? 426 HOH C O   1 
HETATM 9552  O  O   . HOH V 6 .   ? 35.819  -1.179  -48.473 1.00 16.05 ? 427 HOH C O   1 
HETATM 9553  O  O   . HOH V 6 .   ? 23.500  -4.706  -35.944 1.00 17.06 ? 428 HOH C O   1 
HETATM 9554  O  O   . HOH V 6 .   ? 22.307  -6.393  -31.520 1.00 18.05 ? 429 HOH C O   1 
HETATM 9555  O  O   . HOH V 6 .   ? 25.387  8.100   -28.038 1.00 18.53 ? 430 HOH C O   1 
HETATM 9556  O  O   . HOH V 6 .   ? 23.960  8.868   -34.931 1.00 14.16 ? 431 HOH C O   1 
HETATM 9557  O  O   . HOH V 6 .   ? 22.155  6.749   -32.202 1.00 11.23 ? 432 HOH C O   1 
HETATM 9558  O  O   . HOH V 6 .   ? 28.057  -10.803 -22.459 1.00 23.06 ? 433 HOH C O   1 
HETATM 9559  O  O   . HOH V 6 .   ? 20.622  -2.159  -50.941 1.00 28.67 ? 434 HOH C O   1 
HETATM 9560  O  O   . HOH V 6 .   ? 22.192  -0.418  -44.261 1.00 17.46 ? 435 HOH C O   1 
HETATM 9561  O  O   . HOH V 6 .   ? 22.244  -13.855 -35.919 1.00 32.83 ? 436 HOH C O   1 
HETATM 9562  O  O   . HOH V 6 .   ? 44.693  -14.153 -44.674 1.00 21.59 ? 437 HOH C O   1 
HETATM 9563  O  O   . HOH V 6 .   ? 45.297  -7.153  -45.543 1.00 18.74 ? 438 HOH C O   1 
HETATM 9564  O  O   . HOH V 6 .   ? 27.394  16.206  -41.206 1.00 14.19 ? 439 HOH C O   1 
HETATM 9565  O  O   . HOH V 6 .   ? 32.554  5.093   -30.648 1.00 15.76 ? 440 HOH C O   1 
HETATM 9566  O  O   . HOH V 6 .   ? 27.309  -10.353 -26.751 1.00 26.16 ? 441 HOH C O   1 
HETATM 9567  O  O   . HOH V 6 .   ? 32.759  -13.496 -37.007 1.00 20.01 ? 442 HOH C O   1 
HETATM 9568  O  O   . HOH V 6 .   ? 24.004  12.996  -42.456 1.00 16.11 ? 443 HOH C O   1 
HETATM 9569  O  O   . HOH V 6 .   ? 22.714  -0.014  -28.074 1.00 23.49 ? 444 HOH C O   1 
HETATM 9570  O  O   . HOH V 6 .   ? 55.759  -8.204  -32.631 1.00 24.37 ? 445 HOH C O   1 
HETATM 9571  O  O   . HOH V 6 .   ? 26.554  -13.564 -34.516 1.00 20.60 ? 446 HOH C O   1 
HETATM 9572  O  O   . HOH V 6 .   ? 24.876  -2.063  -23.671 1.00 23.31 ? 447 HOH C O   1 
HETATM 9573  O  O   . HOH V 6 .   ? 58.099  -7.244  -31.197 1.00 29.95 ? 448 HOH C O   1 
HETATM 9574  O  O   . HOH V 6 .   ? 31.571  12.689  -46.606 1.00 21.14 ? 449 HOH C O   1 
HETATM 9575  O  O   . HOH V 6 .   ? 19.671  -7.860  -17.508 1.00 28.22 ? 450 HOH C O   1 
HETATM 9576  O  O   . HOH V 6 .   ? 51.313  7.418   -28.692 1.00 27.41 ? 451 HOH C O   1 
HETATM 9577  O  O   . HOH V 6 .   ? 39.907  -12.084 -55.055 1.00 22.44 ? 452 HOH C O   1 
HETATM 9578  O  O   . HOH V 6 .   ? 29.456  -13.954 -28.058 1.00 28.09 ? 453 HOH C O   1 
HETATM 9579  O  O   . HOH V 6 .   ? 27.687  -12.379 -29.817 1.00 25.33 ? 454 HOH C O   1 
HETATM 9580  O  O   . HOH V 6 .   ? 55.868  12.002  -42.591 1.00 36.63 ? 455 HOH C O   1 
HETATM 9581  O  O   . HOH V 6 .   ? 37.781  -10.537 -33.263 1.00 17.44 ? 456 HOH C O   1 
HETATM 9582  O  O   . HOH V 6 .   ? 50.176  -4.226  -15.857 1.00 45.75 ? 457 HOH C O   1 
HETATM 9583  O  O   . HOH V 6 .   ? 25.538  -3.181  -48.297 1.00 19.65 ? 458 HOH C O   1 
HETATM 9584  O  O   . HOH V 6 .   ? 53.397  6.228   -23.540 1.00 24.64 ? 459 HOH C O   1 
HETATM 9585  O  O   . HOH V 6 .   ? 43.687  4.051   -44.387 1.00 17.74 ? 460 HOH C O   1 
HETATM 9586  O  O   . HOH V 6 .   ? 40.442  -14.144 -36.226 1.00 19.48 ? 461 HOH C O   1 
HETATM 9587  O  O   . HOH V 6 .   ? 28.327  6.658   -44.088 1.00 18.64 ? 462 HOH C O   1 
HETATM 9588  O  O   . HOH V 6 .   ? 22.206  -7.600  -27.518 1.00 17.27 ? 463 HOH C O   1 
HETATM 9589  O  O   . HOH V 6 .   ? 40.785  14.049  -37.173 1.00 22.56 ? 464 HOH C O   1 
HETATM 9590  O  O   . HOH V 6 .   ? 41.191  7.274   -46.932 1.00 25.32 ? 465 HOH C O   1 
HETATM 9591  O  O   . HOH V 6 .   ? 38.510  16.654  -38.884 1.00 21.00 ? 466 HOH C O   1 
HETATM 9592  O  O   . HOH V 6 .   ? 40.450  -16.539 -30.196 1.00 22.63 ? 467 HOH C O   1 
HETATM 9593  O  O   . HOH V 6 .   ? 51.478  -2.557  -43.687 1.00 22.45 ? 468 HOH C O   1 
HETATM 9594  O  O   . HOH V 6 .   ? 26.211  11.355  -45.596 1.00 28.78 ? 469 HOH C O   1 
HETATM 9595  O  O   . HOH V 6 .   ? 22.343  -5.354  -41.064 1.00 20.67 ? 470 HOH C O   1 
HETATM 9596  O  O   . HOH V 6 .   ? 26.112  5.422   -43.416 1.00 19.75 ? 471 HOH C O   1 
HETATM 9597  O  O   . HOH V 6 .   ? 49.550  12.180  -32.793 1.00 26.48 ? 472 HOH C O   1 
HETATM 9598  O  O   . HOH V 6 .   ? 47.105  9.171   -27.262 1.00 25.10 ? 473 HOH C O   1 
HETATM 9599  O  O   . HOH V 6 .   ? 31.052  -21.097 -48.401 1.00 32.98 ? 474 HOH C O   1 
HETATM 9600  O  O   . HOH V 6 .   ? 46.253  -11.377 -40.431 1.00 24.37 ? 475 HOH C O   1 
HETATM 9601  O  O   . HOH V 6 .   ? 46.483  -17.136 -38.474 1.00 29.54 ? 476 HOH C O   1 
HETATM 9602  O  O   . HOH V 6 .   ? 42.767  -1.067  -11.132 1.00 38.03 ? 477 HOH C O   1 
HETATM 9603  O  O   . HOH V 6 .   ? 22.234  -8.906  -39.838 1.00 26.15 ? 478 HOH C O   1 
HETATM 9604  O  O   . HOH V 6 .   ? 20.944  -1.287  -30.090 1.00 19.42 ? 479 HOH C O   1 
HETATM 9605  O  O   . HOH V 6 .   ? 56.421  9.080   -40.274 1.00 26.32 ? 480 HOH C O   1 
HETATM 9606  O  O   . HOH V 6 .   ? 56.680  4.430   -42.039 1.00 20.15 ? 481 HOH C O   1 
HETATM 9607  O  O   . HOH V 6 .   ? 26.249  3.150   -47.389 1.00 21.86 ? 482 HOH C O   1 
HETATM 9608  O  O   . HOH V 6 .   ? 32.612  7.310   -22.611 1.00 26.19 ? 483 HOH C O   1 
HETATM 9609  O  O   . HOH V 6 .   ? 25.036  5.644   -45.830 1.00 28.55 ? 484 HOH C O   1 
HETATM 9610  O  O   . HOH V 6 .   ? 27.353  12.939  -47.161 1.00 28.64 ? 485 HOH C O   1 
HETATM 9611  O  O   . HOH V 6 .   ? 47.046  -13.041 -52.959 1.00 18.44 ? 486 HOH C O   1 
HETATM 9612  O  O   . HOH V 6 .   ? 26.875  7.004   -47.638 1.00 25.33 ? 487 HOH C O   1 
HETATM 9613  O  O   . HOH V 6 .   ? 39.281  -19.805 -46.106 1.00 38.49 ? 488 HOH C O   1 
HETATM 9614  O  O   . HOH V 6 .   ? 33.252  -1.736  -48.865 1.00 19.90 ? 489 HOH C O   1 
HETATM 9615  O  O   . HOH V 6 .   ? 36.025  17.787  -38.259 1.00 23.72 ? 490 HOH C O   1 
HETATM 9616  O  O   . HOH V 6 .   ? 23.849  -8.950  -29.041 1.00 25.98 ? 491 HOH C O   1 
HETATM 9617  O  O   . HOH V 6 .   ? 19.636  1.208   -51.707 1.00 21.81 ? 492 HOH C O   1 
HETATM 9618  O  O   . HOH V 6 .   ? 33.375  12.156  -11.231 1.00 31.50 ? 493 HOH C O   1 
HETATM 9619  O  O   . HOH V 6 .   ? 40.528  16.677  -36.953 1.00 28.15 ? 494 HOH C O   1 
HETATM 9620  O  O   . HOH V 6 .   ? 33.860  1.753   -16.633 1.00 23.48 ? 495 HOH C O   1 
HETATM 9621  O  O   . HOH V 6 .   ? 34.063  11.866  -47.832 1.00 25.42 ? 496 HOH C O   1 
HETATM 9622  O  O   . HOH V 6 .   ? 33.714  22.202  -35.089 1.00 31.88 ? 497 HOH C O   1 
HETATM 9623  O  O   . HOH V 6 .   ? 59.999  -2.355  -35.580 1.00 25.16 ? 498 HOH C O   1 
HETATM 9624  O  O   . HOH V 6 .   ? 22.931  1.436   -18.944 1.00 28.70 ? 499 HOH C O   1 
HETATM 9625  O  O   . HOH V 6 .   ? 28.006  15.124  -45.504 1.00 27.23 ? 500 HOH C O   1 
HETATM 9626  O  O   . HOH V 6 .   ? 54.213  5.281   -26.235 1.00 31.25 ? 501 HOH C O   1 
HETATM 9627  O  O   . HOH V 6 .   ? 38.599  10.258  -31.770 1.00 27.48 ? 502 HOH C O   1 
HETATM 9628  O  O   . HOH V 6 .   ? 27.499  -13.907 -31.668 1.00 36.57 ? 503 HOH C O   1 
HETATM 9629  O  O   . HOH V 6 .   ? 38.824  13.875  -42.955 1.00 23.97 ? 504 HOH C O   1 
HETATM 9630  O  O   . HOH V 6 .   ? 38.928  2.464   -5.985  1.00 23.42 ? 505 HOH C O   1 
HETATM 9631  O  O   . HOH V 6 .   ? 54.577  -9.747  -30.943 1.00 35.71 ? 506 HOH C O   1 
HETATM 9632  O  O   . HOH V 6 .   ? 42.109  -4.103  -48.380 1.00 21.17 ? 507 HOH C O   1 
HETATM 9633  O  O   . HOH V 6 .   ? 21.941  -4.011  -38.157 1.00 20.52 ? 508 HOH C O   1 
HETATM 9634  O  O   . HOH V 6 .   ? 35.473  19.420  -35.900 1.00 32.13 ? 509 HOH C O   1 
HETATM 9635  O  O   . HOH V 6 .   ? 29.717  -12.657 -23.917 1.00 21.85 ? 510 HOH C O   1 
HETATM 9636  O  O   . HOH V 6 .   ? 24.324  -3.716  -44.724 1.00 24.26 ? 511 HOH C O   1 
HETATM 9637  O  O   . HOH V 6 .   ? 29.724  -11.799 -26.595 1.00 22.99 ? 512 HOH C O   1 
HETATM 9638  O  O   . HOH V 6 .   ? 40.810  4.157   -6.726  1.00 24.79 ? 513 HOH C O   1 
HETATM 9639  O  O   . HOH V 6 .   ? 22.767  -11.456 -44.658 1.00 28.43 ? 514 HOH C O   1 
HETATM 9640  O  O   . HOH V 6 .   ? 53.062  6.171   -31.603 1.00 24.39 ? 515 HOH C O   1 
HETATM 9641  O  O   . HOH V 6 .   ? 62.082  -0.560  -35.693 1.00 22.52 ? 516 HOH C O   1 
HETATM 9642  O  O   . HOH V 6 .   ? 37.340  8.849   -47.529 1.00 24.78 ? 517 HOH C O   1 
HETATM 9643  O  O   . HOH V 6 .   ? 29.991  5.837   -50.004 1.00 23.30 ? 518 HOH C O   1 
HETATM 9644  O  O   . HOH V 6 .   ? 35.920  13.502  -46.077 1.00 29.55 ? 519 HOH C O   1 
HETATM 9645  O  O   . HOH V 6 .   ? 54.992  6.551   -49.211 1.00 23.74 ? 520 HOH C O   1 
HETATM 9646  O  O   . HOH V 6 .   ? 28.716  -8.097  -17.198 1.00 25.74 ? 521 HOH C O   1 
HETATM 9647  O  O   . HOH V 6 .   ? 23.842  3.499   -51.210 1.00 40.32 ? 522 HOH C O   1 
HETATM 9648  O  O   . HOH V 6 .   ? 45.723  -6.295  -48.208 1.00 43.93 ? 523 HOH C O   1 
HETATM 9649  O  O   . HOH V 6 .   ? 24.131  -3.163  -27.394 1.00 29.94 ? 524 HOH C O   1 
HETATM 9650  O  O   . HOH V 6 .   ? 42.405  16.780  -44.684 1.00 32.55 ? 525 HOH C O   1 
HETATM 9651  O  O   . HOH V 6 .   ? 47.917  -13.228 -39.262 1.00 31.39 ? 526 HOH C O   1 
HETATM 9652  O  O   . HOH V 6 .   ? 30.383  6.278   -21.689 1.00 26.08 ? 527 HOH C O   1 
HETATM 9653  O  O   . HOH V 6 .   ? 27.627  13.034  -49.784 1.00 30.43 ? 528 HOH C O   1 
HETATM 9654  O  O   . HOH V 6 .   ? 58.453  -1.865  -30.016 1.00 31.01 ? 529 HOH C O   1 
HETATM 9655  O  O   . HOH V 6 .   ? 51.339  8.372   -31.289 1.00 26.09 ? 530 HOH C O   1 
HETATM 9656  O  O   . HOH V 6 .   ? 52.573  5.033   -48.962 1.00 23.49 ? 531 HOH C O   1 
HETATM 9657  O  O   . HOH V 6 .   ? 32.300  -1.530  -52.360 1.00 31.15 ? 532 HOH C O   1 
HETATM 9658  O  O   . HOH V 6 .   ? 53.124  -11.327 -36.984 1.00 33.88 ? 533 HOH C O   1 
HETATM 9659  O  O   . HOH V 6 .   ? 52.760  8.601   -24.097 1.00 29.41 ? 534 HOH C O   1 
HETATM 9660  O  O   . HOH V 6 .   ? 48.037  18.846  -40.695 1.00 34.88 ? 535 HOH C O   1 
HETATM 9661  O  O   . HOH V 6 .   ? 26.129  3.865   -49.980 1.00 27.50 ? 536 HOH C O   1 
HETATM 9662  O  O   . HOH V 6 .   ? 34.351  9.191   -47.907 1.00 30.01 ? 537 HOH C O   1 
HETATM 9663  O  O   . HOH V 6 .   ? 53.925  7.185   -27.888 1.00 28.47 ? 538 HOH C O   1 
HETATM 9664  O  O   . HOH V 6 .   ? 35.254  17.051  -41.687 1.00 28.37 ? 539 HOH C O   1 
HETATM 9665  O  O   . HOH V 6 .   ? 43.962  -3.908  -9.351  1.00 44.14 ? 540 HOH C O   1 
HETATM 9666  O  O   . HOH V 6 .   ? 44.472  -15.061 -50.328 1.00 31.60 ? 541 HOH C O   1 
HETATM 9667  O  O   . HOH V 6 .   ? 27.295  2.502   -52.235 1.00 28.50 ? 542 HOH C O   1 
HETATM 9668  O  O   . HOH V 6 .   ? 28.185  -15.285 -35.838 1.00 31.40 ? 543 HOH C O   1 
HETATM 9669  O  O   . HOH V 6 .   ? 53.707  -9.916  -22.478 1.00 28.42 ? 544 HOH C O   1 
HETATM 9670  O  O   . HOH V 6 .   ? 26.367  -5.313  -51.254 1.00 27.14 ? 545 HOH C O   1 
HETATM 9671  O  O   . HOH V 6 .   ? 39.948  -17.901 -23.361 1.00 29.93 ? 546 HOH C O   1 
HETATM 9672  O  O   . HOH V 6 .   ? 32.565  -15.088 -9.634  1.00 33.31 ? 547 HOH C O   1 
HETATM 9673  O  O   . HOH V 6 .   ? 34.529  20.682  -30.992 1.00 36.35 ? 548 HOH C O   1 
HETATM 9674  O  O   . HOH V 6 .   ? 41.030  4.374   -45.737 1.00 30.87 ? 549 HOH C O   1 
HETATM 9675  O  O   . HOH V 6 .   ? 51.662  9.961   -33.429 1.00 30.06 ? 550 HOH C O   1 
HETATM 9676  O  O   . HOH V 6 .   ? 31.865  18.595  -28.669 1.00 37.58 ? 551 HOH C O   1 
HETATM 9677  O  O   . HOH V 6 .   ? 28.056  15.646  -29.194 1.00 26.32 ? 552 HOH C O   1 
HETATM 9678  O  O   . HOH V 6 .   ? 29.309  9.048   -22.330 1.00 28.50 ? 553 HOH C O   1 
HETATM 9679  O  O   . HOH V 6 .   ? 25.878  5.113   -24.313 1.00 28.91 ? 554 HOH C O   1 
HETATM 9680  O  O   . HOH V 6 .   ? 20.484  17.709  -29.920 1.00 29.49 ? 555 HOH C O   1 
HETATM 9681  O  O   . HOH V 6 .   ? 24.611  -13.144 -41.562 1.00 30.98 ? 556 HOH C O   1 
HETATM 9682  O  O   . HOH V 6 .   ? 28.102  -7.290  -55.468 1.00 36.03 ? 557 HOH C O   1 
HETATM 9683  O  O   . HOH V 6 .   ? 42.218  -14.214 -48.666 1.00 31.58 ? 558 HOH C O   1 
HETATM 9684  O  O   . HOH V 6 .   ? 46.278  -15.644 -48.244 1.00 28.13 ? 559 HOH C O   1 
HETATM 9685  O  O   . HOH V 6 .   ? 58.521  -9.687  -35.091 1.00 42.16 ? 560 HOH C O   1 
HETATM 9686  O  O   . HOH V 6 .   ? 59.045  -7.551  -34.494 1.00 30.42 ? 561 HOH C O   1 
HETATM 9687  O  O   . HOH V 6 .   ? 40.534  6.920   -27.849 1.00 29.16 ? 562 HOH C O   1 
HETATM 9688  O  O   . HOH V 6 .   ? 28.740  -0.643  -14.441 1.00 28.71 ? 563 HOH C O   1 
HETATM 9689  O  O   . HOH V 6 .   ? 22.046  -1.026  -23.861 1.00 31.01 ? 564 HOH C O   1 
HETATM 9690  O  O   . HOH V 6 .   ? 51.920  12.865  -47.380 1.00 33.40 ? 565 HOH C O   1 
HETATM 9691  O  O   . HOH V 6 .   ? 49.445  12.173  -48.556 1.00 31.71 ? 566 HOH C O   1 
HETATM 9692  O  O   . HOH V 6 .   ? 41.859  -20.023 -19.238 1.00 44.68 ? 567 HOH C O   1 
HETATM 9693  O  O   . HOH V 6 .   ? 43.103  -17.593 -23.050 1.00 34.83 ? 568 HOH C O   1 
HETATM 9694  O  O   . HOH V 6 .   ? 40.737  -15.492 -25.199 1.00 27.31 ? 569 HOH C O   1 
HETATM 9695  O  O   . HOH V 6 .   ? 42.536  -16.315 -27.925 1.00 39.18 ? 570 HOH C O   1 
HETATM 9696  O  O   . HOH V 6 .   ? 43.626  -12.707 -25.908 1.00 26.24 ? 571 HOH C O   1 
HETATM 9697  O  O   . HOH V 6 .   ? 46.340  -13.722 -21.321 1.00 42.74 ? 572 HOH C O   1 
HETATM 9698  O  O   . HOH V 6 .   ? 38.982  -10.717 -13.039 1.00 40.86 ? 573 HOH C O   1 
HETATM 9699  O  O   . HOH V 6 .   ? 41.989  6.677   -10.598 1.00 36.39 ? 574 HOH C O   1 
HETATM 9700  O  O   . HOH V 6 .   ? 30.931  -14.868 -35.300 1.00 29.93 ? 575 HOH C O   1 
HETATM 9701  O  O   . HOH V 6 .   ? 33.779  -15.808 -16.513 1.00 31.54 ? 576 HOH C O   1 
HETATM 9702  O  O   . HOH V 6 .   ? 32.674  12.525  -8.393  1.00 40.12 ? 577 HOH C O   1 
HETATM 9703  O  O   . HOH V 6 .   ? 23.171  4.143   -46.555 1.00 33.46 ? 578 HOH C O   1 
HETATM 9704  O  O   . HOH V 6 .   ? 22.697  -3.091  -50.183 1.00 29.46 ? 579 HOH C O   1 
HETATM 9705  O  O   . HOH V 6 .   ? 21.170  -3.927  -32.152 1.00 33.44 ? 580 HOH C O   1 
HETATM 9706  O  O   . HOH V 6 .   ? 41.514  9.627   -28.447 1.00 30.01 ? 581 HOH C O   1 
HETATM 9707  O  O   . HOH V 6 .   ? 42.159  12.120  -25.922 1.00 38.54 ? 582 HOH C O   1 
HETATM 9708  O  O   . HOH V 6 .   ? 47.203  7.584   -22.994 1.00 24.28 ? 583 HOH C O   1 
HETATM 9709  O  O   . HOH V 6 .   ? 39.902  16.400  -32.883 1.00 37.36 ? 584 HOH C O   1 
HETATM 9710  O  O   . HOH V 6 .   ? 37.828  18.234  -34.365 1.00 46.54 ? 585 HOH C O   1 
HETATM 9711  O  O   . HOH V 6 .   ? 47.064  -14.726 -32.197 1.00 39.33 ? 586 HOH C O   1 
HETATM 9712  O  O   . HOH V 6 .   ? 43.966  -14.656 -27.617 1.00 33.03 ? 587 HOH C O   1 
HETATM 9713  O  O   . HOH V 6 .   ? 48.095  -13.566 -29.924 1.00 32.86 ? 588 HOH C O   1 
HETATM 9714  O  O   . HOH V 6 .   ? 29.989  -10.883 -16.776 1.00 40.97 ? 589 HOH C O   1 
HETATM 9715  O  O   . HOH V 6 .   ? 58.037  -4.129  -41.873 1.00 38.11 ? 590 HOH C O   1 
HETATM 9716  O  O   . HOH V 6 .   ? 53.574  -4.208  -46.336 1.00 34.91 ? 591 HOH C O   1 
HETATM 9717  O  O   . HOH V 6 .   ? 50.467  -12.972 -16.228 1.00 37.79 ? 592 HOH C O   1 
HETATM 9718  O  O   . HOH V 6 .   ? 47.867  -14.327 -23.111 1.00 36.35 ? 593 HOH C O   1 
HETATM 9719  O  O   . HOH V 6 .   ? 35.833  1.194   -50.244 1.00 32.67 ? 594 HOH C O   1 
HETATM 9720  O  O   . HOH V 6 .   ? 51.243  -12.529 -51.465 1.00 31.48 ? 595 HOH C O   1 
HETATM 9721  O  O   . HOH V 6 .   ? 43.400  -19.751 -40.576 1.00 31.84 ? 596 HOH C O   1 
HETATM 9722  O  O   . HOH V 6 .   ? 40.611  -16.106 -21.980 1.00 34.56 ? 597 HOH C O   1 
HETATM 9723  O  O   . HOH V 6 .   ? 31.756  1.790   -14.482 1.00 30.75 ? 598 HOH C O   1 
HETATM 9724  O  O   . HOH V 6 .   ? 56.109  -7.487  -21.151 1.00 40.81 ? 599 HOH C O   1 
HETATM 9725  O  O   . HOH V 6 .   ? 51.993  -12.490 -44.324 1.00 44.53 ? 600 HOH C O   1 
HETATM 9726  O  O   . HOH V 6 .   ? 46.259  -1.855  -47.684 1.00 39.08 ? 601 HOH C O   1 
HETATM 9727  O  O   . HOH V 6 .   ? 32.650  0.213   -50.871 1.00 39.25 ? 602 HOH C O   1 
HETATM 9728  O  O   . HOH V 6 .   ? 45.152  -16.240 -45.512 1.00 31.75 ? 603 HOH C O   1 
HETATM 9729  O  O   . HOH V 6 .   ? 38.160  -2.894  -48.828 1.00 31.06 ? 604 HOH C O   1 
HETATM 9730  O  O   . HOH V 6 .   ? 57.350  11.825  -37.197 1.00 36.00 ? 605 HOH C O   1 
HETATM 9731  O  O   . HOH V 6 .   ? 33.501  -18.389 -30.917 1.00 40.46 ? 606 HOH C O   1 
HETATM 9732  O  O   . HOH V 6 .   ? 33.863  7.971   -50.332 1.00 32.99 ? 607 HOH C O   1 
HETATM 9733  O  O   . HOH V 6 .   ? 54.429  9.763   -34.245 1.00 34.86 ? 608 HOH C O   1 
HETATM 9734  O  O   . HOH V 6 .   ? 30.296  -13.881 -52.471 1.00 44.51 ? 609 HOH C O   1 
HETATM 9735  O  O   . HOH V 6 .   ? 30.122  15.410  -43.859 1.00 27.23 ? 610 HOH C O   1 
HETATM 9736  O  O   . HOH V 6 .   ? 37.794  16.277  -43.213 1.00 31.88 ? 611 HOH C O   1 
HETATM 9737  O  O   . HOH V 6 .   ? 33.060  12.576  -50.691 1.00 35.65 ? 612 HOH C O   1 
HETATM 9738  O  O   . HOH V 6 .   ? 48.232  -16.276 -40.254 1.00 32.93 ? 613 HOH C O   1 
HETATM 9739  O  O   . HOH V 6 .   ? 57.042  -8.113  -23.710 1.00 41.90 ? 614 HOH C O   1 
HETATM 9740  O  O   . HOH V 6 .   ? 56.314  7.427   -37.440 1.00 36.74 ? 615 HOH C O   1 
HETATM 9741  O  O   . HOH V 6 .   ? 25.697  -10.658 -16.729 1.00 39.78 ? 616 HOH C O   1 
HETATM 9742  O  O   . HOH V 6 .   ? 24.523  -14.839 -35.032 1.00 36.83 ? 617 HOH C O   1 
HETATM 9743  O  O   . HOH V 6 .   ? 52.461  17.365  -41.932 1.00 39.90 ? 618 HOH C O   1 
HETATM 9744  O  O   . HOH V 6 .   ? 44.987  16.701  -38.768 1.00 30.46 ? 619 HOH C O   1 
HETATM 9745  O  O   . HOH V 6 .   ? 38.935  -2.673  -11.388 1.00 35.63 ? 620 HOH C O   1 
HETATM 9746  O  O   . HOH V 6 .   ? 40.366  -1.870  -48.564 1.00 39.57 ? 621 HOH C O   1 
HETATM 9747  O  O   . HOH V 6 .   ? 36.680  15.902  -26.186 1.00 42.09 ? 622 HOH C O   1 
HETATM 9748  O  O   . HOH V 6 .   ? 38.453  -18.694 -16.168 1.00 31.91 ? 623 HOH C O   1 
HETATM 9749  O  O   . HOH V 6 .   ? 38.614  -14.156 -13.389 1.00 36.37 ? 624 HOH C O   1 
HETATM 9750  O  O   . HOH V 6 .   ? 52.639  1.382   -13.104 1.00 39.35 ? 625 HOH C O   1 
HETATM 9751  O  O   . HOH V 6 .   ? 24.565  5.024   -20.863 1.00 37.95 ? 626 HOH C O   1 
HETATM 9752  O  O   . HOH W 6 .   ? 20.903  13.461  -35.622 1.00 10.03 ? 401 HOH D O   1 
HETATM 9753  O  O   . HOH W 6 .   ? 19.092  9.972   -35.700 1.00 9.54  ? 402 HOH D O   1 
HETATM 9754  O  O   . HOH W 6 .   ? 16.411  0.194   -37.476 1.00 8.77  ? 403 HOH D O   1 
HETATM 9755  O  O   . HOH W 6 .   ? 22.787  23.137  -35.636 1.00 10.87 ? 404 HOH D O   1 
HETATM 9756  O  O   . HOH W 6 .   ? 13.476  18.467  -32.408 1.00 10.66 ? 405 HOH D O   1 
HETATM 9757  O  O   . HOH W 6 .   ? -7.198  -7.033  -51.489 1.00 19.04 ? 406 HOH D O   1 
HETATM 9758  O  O   . HOH W 6 .   ? 9.272   8.180   -42.931 1.00 13.17 ? 407 HOH D O   1 
HETATM 9759  O  O   . HOH W 6 .   ? 12.227  6.960   -39.323 1.00 8.89  ? 408 HOH D O   1 
HETATM 9760  O  O   . HOH W 6 .   ? 2.591   9.335   -24.814 1.00 14.37 ? 409 HOH D O   1 
HETATM 9761  O  O   . HOH W 6 .   ? -2.449  -8.748  -41.682 1.00 15.74 ? 410 HOH D O   1 
HETATM 9762  O  O   . HOH W 6 .   ? 0.966   2.427   -28.106 1.00 11.15 ? 411 HOH D O   1 
HETATM 9763  O  O   . HOH W 6 .   ? -10.407 11.761  -26.028 1.00 19.98 ? 412 HOH D O   1 
HETATM 9764  O  O   . HOH W 6 .   ? 19.945  8.002   -42.414 1.00 10.71 ? 413 HOH D O   1 
HETATM 9765  O  O   . HOH W 6 .   ? 20.207  7.264   -35.674 1.00 12.34 ? 414 HOH D O   1 
HETATM 9766  O  O   . HOH W 6 .   ? 21.380  6.592   -29.696 1.00 13.82 ? 415 HOH D O   1 
HETATM 9767  O  O   . HOH W 6 .   ? 18.459  -0.368  -29.424 1.00 14.05 ? 416 HOH D O   1 
HETATM 9768  O  O   . HOH W 6 .   ? 5.871   -6.483  -57.495 1.00 13.41 ? 417 HOH D O   1 
HETATM 9769  O  O   . HOH W 6 .   ? 2.222   -11.919 -54.264 1.00 15.59 ? 418 HOH D O   1 
HETATM 9770  O  O   . HOH W 6 .   ? 1.161   -9.968  -31.234 1.00 12.11 ? 419 HOH D O   1 
HETATM 9771  O  O   . HOH W 6 .   ? 13.696  7.406   -48.342 1.00 12.02 ? 420 HOH D O   1 
HETATM 9772  O  O   . HOH W 6 .   ? 10.889  13.313  -58.539 1.00 18.86 ? 421 HOH D O   1 
HETATM 9773  O  O   . HOH W 6 .   ? 14.482  13.750  -27.205 1.00 13.99 ? 422 HOH D O   1 
HETATM 9774  O  O   . HOH W 6 .   ? -2.276  -7.971  -22.591 1.00 16.08 ? 423 HOH D O   1 
HETATM 9775  O  O   . HOH W 6 .   ? 22.922  6.292   -38.240 1.00 9.61  ? 424 HOH D O   1 
HETATM 9776  O  O   . HOH W 6 .   ? 11.887  -3.666  -47.249 1.00 10.00 ? 425 HOH D O   1 
HETATM 9777  O  O   . HOH W 6 .   ? 4.321   -7.002  -34.848 1.00 9.74  ? 426 HOH D O   1 
HETATM 9778  O  O   . HOH W 6 .   ? 12.585  -9.797  -46.088 1.00 15.87 ? 427 HOH D O   1 
HETATM 9779  O  O   . HOH W 6 .   ? 8.738   -10.832 -31.157 1.00 15.16 ? 428 HOH D O   1 
HETATM 9780  O  O   . HOH W 6 .   ? 4.540   19.108  -22.670 1.00 23.04 ? 429 HOH D O   1 
HETATM 9781  O  O   . HOH W 6 .   ? 20.591  13.921  -47.799 1.00 16.80 ? 430 HOH D O   1 
HETATM 9782  O  O   . HOH W 6 .   ? -12.883 -1.735  -34.150 1.00 19.64 ? 431 HOH D O   1 
HETATM 9783  O  O   . HOH W 6 .   ? 12.283  1.841   -18.047 1.00 18.32 ? 432 HOH D O   1 
HETATM 9784  O  O   . HOH W 6 .   ? -8.547  -0.188  -51.750 1.00 16.31 ? 433 HOH D O   1 
HETATM 9785  O  O   . HOH W 6 .   ? -14.510 4.810   -37.230 1.00 21.90 ? 434 HOH D O   1 
HETATM 9786  O  O   . HOH W 6 .   ? 11.759  8.802   -47.187 1.00 11.84 ? 435 HOH D O   1 
HETATM 9787  O  O   . HOH W 6 .   ? 11.189  -10.571 -43.536 1.00 20.25 ? 436 HOH D O   1 
HETATM 9788  O  O   . HOH W 6 .   ? 11.206  3.640   -55.186 1.00 13.70 ? 437 HOH D O   1 
HETATM 9789  O  O   . HOH W 6 .   ? 0.459   -12.732 -37.018 1.00 15.51 ? 438 HOH D O   1 
HETATM 9790  O  O   . HOH W 6 .   ? 14.176  19.862  -42.674 1.00 29.77 ? 439 HOH D O   1 
HETATM 9791  O  O   . HOH W 6 .   ? 19.020  11.568  -50.242 1.00 17.16 ? 440 HOH D O   1 
HETATM 9792  O  O   . HOH W 6 .   ? 1.045   -5.122  -54.402 1.00 20.52 ? 441 HOH D O   1 
HETATM 9793  O  O   . HOH W 6 .   ? 19.150  4.719   -49.306 1.00 18.16 ? 442 HOH D O   1 
HETATM 9794  O  O   . HOH W 6 .   ? 23.884  18.329  -42.653 1.00 18.26 ? 443 HOH D O   1 
HETATM 9795  O  O   . HOH W 6 .   ? 23.526  10.426  -41.517 1.00 16.83 ? 444 HOH D O   1 
HETATM 9796  O  O   . HOH W 6 .   ? 15.403  9.810   -47.876 1.00 15.28 ? 445 HOH D O   1 
HETATM 9797  O  O   . HOH W 6 .   ? 0.587   -8.319  -18.955 1.00 18.51 ? 446 HOH D O   1 
HETATM 9798  O  O   . HOH W 6 .   ? 13.819  16.247  -26.351 1.00 20.71 ? 447 HOH D O   1 
HETATM 9799  O  O   . HOH W 6 .   ? -10.007 -0.360  -49.501 1.00 17.88 ? 448 HOH D O   1 
HETATM 9800  O  O   . HOH W 6 .   ? 20.445  -7.749  -29.742 1.00 14.86 ? 449 HOH D O   1 
HETATM 9801  O  O   . HOH W 6 .   ? 4.705   15.933  -57.288 1.00 19.77 ? 450 HOH D O   1 
HETATM 9802  O  O   . HOH W 6 .   ? 16.494  10.577  -50.221 1.00 14.85 ? 451 HOH D O   1 
HETATM 9803  O  O   . HOH W 6 .   ? 19.289  8.301   -29.147 1.00 14.41 ? 452 HOH D O   1 
HETATM 9804  O  O   . HOH W 6 .   ? 17.153  7.575   -55.710 1.00 21.37 ? 453 HOH D O   1 
HETATM 9805  O  O   . HOH W 6 .   ? -12.745 8.578   -55.140 1.00 26.40 ? 454 HOH D O   1 
HETATM 9806  O  O   . HOH W 6 .   ? -0.262  -12.817 -45.363 1.00 14.71 ? 455 HOH D O   1 
HETATM 9807  O  O   . HOH W 6 .   ? 18.884  16.665  -41.873 1.00 25.34 ? 456 HOH D O   1 
HETATM 9808  O  O   . HOH W 6 .   ? 2.346   11.275  -61.727 1.00 28.87 ? 457 HOH D O   1 
HETATM 9809  O  O   . HOH W 6 .   ? 19.812  11.024  -29.040 1.00 16.79 ? 458 HOH D O   1 
HETATM 9810  O  O   . HOH W 6 .   ? -12.632 -4.448  -47.523 1.00 24.98 ? 459 HOH D O   1 
HETATM 9811  O  O   . HOH W 6 .   ? 18.529  5.131   -45.710 1.00 15.23 ? 460 HOH D O   1 
HETATM 9812  O  O   . HOH W 6 .   ? 19.054  -0.309  -36.788 1.00 16.23 ? 461 HOH D O   1 
HETATM 9813  O  O   . HOH W 6 .   ? 21.409  5.047   -34.237 1.00 8.63  ? 462 HOH D O   1 
HETATM 9814  O  O   . HOH W 6 .   ? -7.949  11.853  -36.923 1.00 16.92 ? 463 HOH D O   1 
HETATM 9815  O  O   . HOH W 6 .   ? -8.177  19.367  -25.959 1.00 32.72 ? 464 HOH D O   1 
HETATM 9816  O  O   . HOH W 6 .   ? -5.793  -7.020  -27.807 1.00 19.21 ? 465 HOH D O   1 
HETATM 9817  O  O   . HOH W 6 .   ? -3.609  -5.734  -26.879 1.00 14.32 ? 466 HOH D O   1 
HETATM 9818  O  O   . HOH W 6 .   ? -5.658  -11.183 -31.039 1.00 29.38 ? 467 HOH D O   1 
HETATM 9819  O  O   . HOH W 6 .   ? 14.189  -11.653 -47.230 1.00 27.61 ? 468 HOH D O   1 
HETATM 9820  O  O   . HOH W 6 .   ? 10.087  -11.941 -33.355 1.00 28.90 ? 469 HOH D O   1 
HETATM 9821  O  O   . HOH W 6 .   ? 4.070   18.747  -51.155 1.00 31.20 ? 470 HOH D O   1 
HETATM 9822  O  O   . HOH W 6 .   ? 9.070   3.239   -53.032 1.00 10.97 ? 471 HOH D O   1 
HETATM 9823  O  O   . HOH W 6 .   ? 12.044  20.724  -32.435 1.00 17.78 ? 472 HOH D O   1 
HETATM 9824  O  O   . HOH W 6 .   ? 17.176  6.640   -49.044 1.00 15.34 ? 473 HOH D O   1 
HETATM 9825  O  O   . HOH W 6 .   ? 11.873  -7.024  -52.135 1.00 18.56 ? 474 HOH D O   1 
HETATM 9826  O  O   . HOH W 6 .   ? -5.392  -13.675 -32.558 1.00 29.14 ? 475 HOH D O   1 
HETATM 9827  O  O   . HOH W 6 .   ? -3.822  10.031  -17.450 1.00 16.38 ? 476 HOH D O   1 
HETATM 9828  O  O   . HOH W 6 .   ? 7.078   -4.293  -58.558 1.00 23.56 ? 477 HOH D O   1 
HETATM 9829  O  O   . HOH W 6 .   ? 14.630  -12.039 -34.541 1.00 27.17 ? 478 HOH D O   1 
HETATM 9830  O  O   . HOH W 6 .   ? 11.138  17.707  -54.790 1.00 19.25 ? 479 HOH D O   1 
HETATM 9831  O  O   . HOH W 6 .   ? -6.467  -9.113  -53.026 1.00 24.51 ? 480 HOH D O   1 
HETATM 9832  O  O   . HOH W 6 .   ? 21.236  2.183   -21.236 1.00 27.58 ? 481 HOH D O   1 
HETATM 9833  O  O   . HOH W 6 .   ? 9.449   20.091  -31.727 1.00 16.17 ? 482 HOH D O   1 
HETATM 9834  O  O   . HOH W 6 .   ? 10.546  -10.724 -17.245 1.00 22.20 ? 483 HOH D O   1 
HETATM 9835  O  O   . HOH W 6 .   ? -15.370 -2.131  -43.778 1.00 24.85 ? 484 HOH D O   1 
HETATM 9836  O  O   . HOH W 6 .   ? 19.450  -4.235  -34.336 1.00 22.98 ? 485 HOH D O   1 
HETATM 9837  O  O   . HOH W 6 .   ? -6.218  5.303   -56.300 1.00 21.70 ? 486 HOH D O   1 
HETATM 9838  O  O   . HOH W 6 .   ? 10.289  2.211   -21.430 1.00 17.31 ? 487 HOH D O   1 
HETATM 9839  O  O   . HOH W 6 .   ? -2.916  -10.564 -39.478 1.00 23.13 ? 488 HOH D O   1 
HETATM 9840  O  O   . HOH W 6 .   ? 16.133  24.060  -34.185 1.00 22.53 ? 489 HOH D O   1 
HETATM 9841  O  O   . HOH W 6 .   ? 6.453   17.924  -32.976 1.00 19.51 ? 490 HOH D O   1 
HETATM 9842  O  O   . HOH W 6 .   ? 13.633  1.094   -55.774 1.00 20.01 ? 491 HOH D O   1 
HETATM 9843  O  O   . HOH W 6 .   ? -5.066  -11.293 -28.302 1.00 21.23 ? 492 HOH D O   1 
HETATM 9844  O  O   . HOH W 6 .   ? 12.846  13.322  -48.459 1.00 17.85 ? 493 HOH D O   1 
HETATM 9845  O  O   . HOH W 6 .   ? -2.851  11.158  -46.140 1.00 21.11 ? 494 HOH D O   1 
HETATM 9846  O  O   . HOH W 6 .   ? 18.427  22.985  -34.055 1.00 20.69 ? 495 HOH D O   1 
HETATM 9847  O  O   . HOH W 6 .   ? 2.026   -15.414 -29.700 1.00 23.23 ? 496 HOH D O   1 
HETATM 9848  O  O   . HOH W 6 .   ? -8.379  9.256   -55.708 1.00 23.56 ? 497 HOH D O   1 
HETATM 9849  O  O   . HOH W 6 .   ? 5.987   21.360  -25.686 1.00 19.69 ? 498 HOH D O   1 
HETATM 9850  O  O   . HOH W 6 .   ? 8.729   21.589  -29.626 1.00 17.50 ? 499 HOH D O   1 
HETATM 9851  O  O   . HOH W 6 .   ? 3.215   -6.744  -58.097 1.00 21.58 ? 500 HOH D O   1 
HETATM 9852  O  O   . HOH W 6 .   ? -9.136  11.199  -45.120 1.00 20.94 ? 501 HOH D O   1 
HETATM 9853  O  O   . HOH W 6 .   ? -2.526  13.885  -56.556 1.00 22.45 ? 502 HOH D O   1 
HETATM 9854  O  O   . HOH W 6 .   ? -0.145  -10.467 -18.186 1.00 27.28 ? 503 HOH D O   1 
HETATM 9855  O  O   . HOH W 6 .   ? 14.070  -11.401 -20.723 1.00 32.36 ? 504 HOH D O   1 
HETATM 9856  O  O   . HOH W 6 .   ? 3.291   -15.563 -22.062 1.00 42.32 ? 505 HOH D O   1 
HETATM 9857  O  O   . HOH W 6 .   ? 8.562   -16.421 -45.156 1.00 25.23 ? 506 HOH D O   1 
HETATM 9858  O  O   . HOH W 6 .   ? 16.624  8.052   -51.501 1.00 16.66 ? 507 HOH D O   1 
HETATM 9859  O  O   . HOH W 6 .   ? -9.139  -5.400  -22.894 1.00 39.68 ? 508 HOH D O   1 
HETATM 9860  O  O   . HOH W 6 .   ? 14.980  24.471  -31.713 1.00 23.85 ? 509 HOH D O   1 
HETATM 9861  O  O   . HOH W 6 .   ? 20.220  21.602  -32.812 1.00 29.98 ? 510 HOH D O   1 
HETATM 9862  O  O   . HOH W 6 .   ? 16.420  15.900  -54.652 1.00 24.19 ? 511 HOH D O   1 
HETATM 9863  O  O   . HOH W 6 .   ? -6.001  4.276   -24.370 1.00 21.89 ? 512 HOH D O   1 
HETATM 9864  O  O   . HOH W 6 .   ? -6.525  12.325  -40.072 1.00 24.41 ? 513 HOH D O   1 
HETATM 9865  O  O   . HOH W 6 .   ? -15.847 9.734   -47.408 1.00 27.28 ? 514 HOH D O   1 
HETATM 9866  O  O   . HOH W 6 .   ? -5.730  15.544  -35.549 1.00 26.09 ? 515 HOH D O   1 
HETATM 9867  O  O   . HOH W 6 .   ? -11.732 -7.515  -36.748 1.00 28.81 ? 516 HOH D O   1 
HETATM 9868  O  O   . HOH W 6 .   ? 18.642  -7.646  -40.142 1.00 19.31 ? 517 HOH D O   1 
HETATM 9869  O  O   . HOH W 6 .   ? 8.972   -10.149 -58.046 1.00 17.02 ? 518 HOH D O   1 
HETATM 9870  O  O   . HOH W 6 .   ? 1.071   9.237   -59.395 1.00 26.50 ? 519 HOH D O   1 
HETATM 9871  O  O   . HOH W 6 .   ? 20.586  3.738   -46.912 1.00 20.90 ? 520 HOH D O   1 
HETATM 9872  O  O   . HOH W 6 .   ? 1.071   -17.531 -27.023 1.00 35.82 ? 521 HOH D O   1 
HETATM 9873  O  O   . HOH W 6 .   ? 22.655  8.540   -27.797 1.00 18.73 ? 522 HOH D O   1 
HETATM 9874  O  O   . HOH W 6 .   ? -12.462 -7.835  -41.136 1.00 23.14 ? 523 HOH D O   1 
HETATM 9875  O  O   . HOH W 6 .   ? 18.635  -0.769  -46.311 1.00 20.21 ? 524 HOH D O   1 
HETATM 9876  O  O   . HOH W 6 .   ? -1.844  -8.979  -16.720 1.00 23.53 ? 525 HOH D O   1 
HETATM 9877  O  O   . HOH W 6 .   ? 20.363  -6.706  -44.508 1.00 27.24 ? 526 HOH D O   1 
HETATM 9878  O  O   . HOH W 6 .   ? 1.392   7.452   -22.482 1.00 27.98 ? 527 HOH D O   1 
HETATM 9879  O  O   . HOH W 6 .   ? 14.917  26.213  -35.162 1.00 24.93 ? 528 HOH D O   1 
HETATM 9880  O  O   . HOH W 6 .   ? 2.739   21.461  -31.942 1.00 35.52 ? 529 HOH D O   1 
HETATM 9881  O  O   . HOH W 6 .   ? 7.865   9.061   -24.268 1.00 18.66 ? 530 HOH D O   1 
HETATM 9882  O  O   . HOH W 6 .   ? 18.832  -13.219 -32.998 1.00 29.23 ? 531 HOH D O   1 
HETATM 9883  O  O   . HOH W 6 .   ? 17.975  7.285   -27.164 1.00 18.95 ? 532 HOH D O   1 
HETATM 9884  O  O   . HOH W 6 .   ? 17.410  -11.509 -27.355 1.00 22.77 ? 533 HOH D O   1 
HETATM 9885  O  O   . HOH W 6 .   ? 12.918  11.263  -46.683 1.00 16.06 ? 534 HOH D O   1 
HETATM 9886  O  O   . HOH W 6 .   ? 10.611  3.883   -19.212 1.00 24.43 ? 535 HOH D O   1 
HETATM 9887  O  O   . HOH W 6 .   ? -13.411 12.576  -32.293 1.00 28.09 ? 536 HOH D O   1 
HETATM 9888  O  O   . HOH W 6 .   ? -6.822  -9.321  -26.787 1.00 25.22 ? 537 HOH D O   1 
HETATM 9889  O  O   . HOH W 6 .   ? -5.578  -9.873  -34.753 1.00 26.92 ? 538 HOH D O   1 
HETATM 9890  O  O   . HOH W 6 .   ? 18.901  -3.483  -43.103 1.00 19.11 ? 539 HOH D O   1 
HETATM 9891  O  O   . HOH W 6 .   ? 12.610  19.804  -29.141 1.00 22.16 ? 540 HOH D O   1 
HETATM 9892  O  O   . HOH W 6 .   ? -5.758  -5.806  -53.720 1.00 28.08 ? 541 HOH D O   1 
HETATM 9893  O  O   . HOH W 6 .   ? -2.599  -0.599  -16.702 1.00 25.34 ? 542 HOH D O   1 
HETATM 9894  O  O   . HOH W 6 .   ? 5.874   -0.265  -57.978 1.00 22.91 ? 543 HOH D O   1 
HETATM 9895  O  O   . HOH W 6 .   ? -12.361 -3.891  -36.223 1.00 22.97 ? 544 HOH D O   1 
HETATM 9896  O  O   . HOH W 6 .   ? -2.085  12.877  -41.385 1.00 28.48 ? 545 HOH D O   1 
HETATM 9897  O  O   . HOH W 6 .   ? -6.403  -9.075  -37.472 1.00 27.26 ? 546 HOH D O   1 
HETATM 9898  O  O   . HOH W 6 .   ? 18.780  -4.658  -18.203 1.00 31.06 ? 547 HOH D O   1 
HETATM 9899  O  O   . HOH W 6 .   ? -11.586 -2.546  -49.582 1.00 22.80 ? 548 HOH D O   1 
HETATM 9900  O  O   . HOH W 6 .   ? -9.955  15.201  -20.874 1.00 22.53 ? 549 HOH D O   1 
HETATM 9901  O  O   . HOH W 6 .   ? 21.577  -9.789  -25.957 1.00 21.79 ? 550 HOH D O   1 
HETATM 9902  O  O   . HOH W 6 .   ? 21.741  0.714   -25.592 1.00 24.66 ? 551 HOH D O   1 
HETATM 9903  O  O   . HOH W 6 .   ? -10.639 19.471  -30.886 1.00 27.53 ? 552 HOH D O   1 
HETATM 9904  O  O   . HOH W 6 .   ? 20.359  1.149   -45.635 1.00 21.69 ? 553 HOH D O   1 
HETATM 9905  O  O   . HOH W 6 .   ? -9.780  8.402   -20.673 1.00 24.86 ? 554 HOH D O   1 
HETATM 9906  O  O   . HOH W 6 .   ? 8.711   17.785  -27.308 1.00 20.00 ? 555 HOH D O   1 
HETATM 9907  O  O   . HOH W 6 .   ? -16.268 4.331   -41.132 1.00 21.43 ? 556 HOH D O   1 
HETATM 9908  O  O   . HOH W 6 .   ? -3.011  -12.368 -45.399 1.00 26.81 ? 557 HOH D O   1 
HETATM 9909  O  O   . HOH W 6 .   ? -11.364 12.908  -38.148 1.00 25.70 ? 558 HOH D O   1 
HETATM 9910  O  O   . HOH W 6 .   ? 5.032   -2.367  -59.013 1.00 22.65 ? 559 HOH D O   1 
HETATM 9911  O  O   . HOH W 6 .   ? -2.684  -14.652 -39.550 1.00 29.88 ? 560 HOH D O   1 
HETATM 9912  O  O   . HOH W 6 .   ? 1.185   -10.111 -56.062 1.00 21.88 ? 561 HOH D O   1 
HETATM 9913  O  O   . HOH W 6 .   ? 4.246   -0.842  -14.651 1.00 29.79 ? 562 HOH D O   1 
HETATM 9914  O  O   . HOH W 6 .   ? 14.308  5.827   -60.139 1.00 27.62 ? 563 HOH D O   1 
HETATM 9915  O  O   . HOH W 6 .   ? -8.623  12.763  -40.936 1.00 30.89 ? 564 HOH D O   1 
HETATM 9916  O  O   . HOH W 6 .   ? 11.175  13.958  -61.321 1.00 27.89 ? 565 HOH D O   1 
HETATM 9917  O  O   . HOH W 6 .   ? -6.415  8.010   -57.495 1.00 34.22 ? 566 HOH D O   1 
HETATM 9918  O  O   . HOH W 6 .   ? -18.117 10.428  -46.985 1.00 40.63 ? 567 HOH D O   1 
HETATM 9919  O  O   . HOH W 6 .   ? 19.411  18.845  -39.822 1.00 23.83 ? 568 HOH D O   1 
HETATM 9920  O  O   . HOH W 6 .   ? 20.711  -4.295  -28.618 1.00 22.85 ? 569 HOH D O   1 
HETATM 9921  O  O   . HOH W 6 .   ? -10.662 -4.594  -29.631 1.00 22.56 ? 570 HOH D O   1 
HETATM 9922  O  O   . HOH W 6 .   ? 22.285  3.482   -23.429 1.00 25.54 ? 571 HOH D O   1 
HETATM 9923  O  O   . HOH W 6 .   ? -12.406 -4.770  -44.413 1.00 21.01 ? 572 HOH D O   1 
HETATM 9924  O  O   . HOH W 6 .   ? 13.956  -10.731 -27.766 1.00 37.82 ? 573 HOH D O   1 
HETATM 9925  O  O   . HOH W 6 .   ? -16.937 4.358   -51.757 1.00 25.37 ? 574 HOH D O   1 
HETATM 9926  O  O   . HOH W 6 .   ? 1.937   6.675   -61.534 1.00 33.98 ? 575 HOH D O   1 
HETATM 9927  O  O   . HOH W 6 .   ? 9.668   -13.452 -55.466 1.00 27.93 ? 576 HOH D O   1 
HETATM 9928  O  O   . HOH W 6 .   ? -20.641 5.961   -51.034 1.00 22.42 ? 577 HOH D O   1 
HETATM 9929  O  O   . HOH W 6 .   ? 6.068   -14.632 -33.604 1.00 43.18 ? 578 HOH D O   1 
HETATM 9930  O  O   . HOH W 6 .   ? 4.261   23.983  -25.806 1.00 25.37 ? 579 HOH D O   1 
HETATM 9931  O  O   . HOH W 6 .   ? -14.086 11.799  -49.530 1.00 42.56 ? 580 HOH D O   1 
HETATM 9932  O  O   . HOH W 6 .   ? -7.020  0.307   -56.170 1.00 27.42 ? 581 HOH D O   1 
HETATM 9933  O  O   . HOH W 6 .   ? 11.444  -11.155 -27.822 1.00 25.57 ? 582 HOH D O   1 
HETATM 9934  O  O   . HOH W 6 .   ? -3.112  -9.896  -21.090 1.00 26.27 ? 583 HOH D O   1 
HETATM 9935  O  O   . HOH W 6 .   ? 1.815   -7.461  -55.714 1.00 25.16 ? 584 HOH D O   1 
HETATM 9936  O  O   . HOH W 6 .   ? 7.436   20.526  -33.580 1.00 25.41 ? 585 HOH D O   1 
HETATM 9937  O  O   . HOH W 6 .   ? -3.887  -8.910  -18.611 1.00 28.48 ? 586 HOH D O   1 
HETATM 9938  O  O   . HOH W 6 .   ? -1.090  15.878  -57.777 1.00 34.34 ? 587 HOH D O   1 
HETATM 9939  O  O   . HOH W 6 .   ? 12.041  -12.640 -56.683 1.00 22.03 ? 588 HOH D O   1 
HETATM 9940  O  O   . HOH W 6 .   ? 6.986   -8.558  -59.022 1.00 18.57 ? 589 HOH D O   1 
HETATM 9941  O  O   . HOH W 6 .   ? 20.833  -1.561  -42.251 1.00 25.00 ? 590 HOH D O   1 
HETATM 9942  O  O   . HOH W 6 .   ? -0.112  -12.242 -42.272 1.00 17.03 ? 591 HOH D O   1 
HETATM 9943  O  O   . HOH W 6 .   ? 16.814  22.802  -27.693 1.00 22.06 ? 592 HOH D O   1 
HETATM 9944  O  O   . HOH W 6 .   ? -7.535  3.569   -21.262 1.00 27.49 ? 593 HOH D O   1 
HETATM 9945  O  O   . HOH W 6 .   ? 5.536   12.184  -22.921 1.00 21.10 ? 594 HOH D O   1 
HETATM 9946  O  O   . HOH W 6 .   ? 19.673  -5.888  -41.889 1.00 18.45 ? 595 HOH D O   1 
HETATM 9947  O  O   . HOH W 6 .   ? -13.879 -1.282  -49.214 1.00 22.32 ? 596 HOH D O   1 
HETATM 9948  O  O   . HOH W 6 .   ? 22.592  7.625   -42.544 1.00 18.88 ? 597 HOH D O   1 
HETATM 9949  O  O   . HOH W 6 .   ? 0.885   12.956  -39.664 1.00 22.29 ? 598 HOH D O   1 
HETATM 9950  O  O   . HOH W 6 .   ? 12.979  22.807  -30.831 1.00 20.21 ? 599 HOH D O   1 
HETATM 9951  O  O   . HOH W 6 .   ? -2.996  22.317  -35.055 1.00 20.93 ? 600 HOH D O   1 
HETATM 9952  O  O   . HOH W 6 .   ? 26.094  16.132  -43.617 1.00 20.67 ? 601 HOH D O   1 
HETATM 9953  O  O   . HOH W 6 .   ? -5.646  -10.122 -45.292 1.00 28.88 ? 602 HOH D O   1 
HETATM 9954  O  O   . HOH W 6 .   ? 11.478  22.082  -61.727 1.00 27.78 ? 603 HOH D O   1 
HETATM 9955  O  O   . HOH W 6 .   ? 22.938  13.572  -28.502 1.00 29.14 ? 604 HOH D O   1 
HETATM 9956  O  O   . HOH W 6 .   ? 22.574  -1.674  -39.996 1.00 21.02 ? 605 HOH D O   1 
HETATM 9957  O  O   . HOH W 6 .   ? -14.216 7.963   -25.546 1.00 31.43 ? 606 HOH D O   1 
HETATM 9958  O  O   . HOH W 6 .   ? 5.097   9.166   -23.598 1.00 23.78 ? 607 HOH D O   1 
HETATM 9959  O  O   . HOH W 6 .   ? -15.159 6.939   -40.966 1.00 29.04 ? 608 HOH D O   1 
HETATM 9960  O  O   . HOH W 6 .   ? 4.224   13.006  -18.483 1.00 26.42 ? 609 HOH D O   1 
HETATM 9961  O  O   . HOH W 6 .   ? -12.208 10.247  -23.301 1.00 24.79 ? 610 HOH D O   1 
HETATM 9962  O  O   . HOH W 6 .   ? 0.920   24.279  -29.872 1.00 31.19 ? 611 HOH D O   1 
HETATM 9963  O  O   . HOH W 6 .   ? 20.207  -1.263  -39.780 1.00 23.14 ? 612 HOH D O   1 
HETATM 9964  O  O   . HOH W 6 .   ? 5.675   18.922  -59.042 1.00 28.10 ? 613 HOH D O   1 
HETATM 9965  O  O   . HOH W 6 .   ? -2.209  11.558  -20.214 1.00 26.47 ? 614 HOH D O   1 
HETATM 9966  O  O   . HOH W 6 .   ? 16.148  14.937  -23.875 1.00 31.71 ? 615 HOH D O   1 
HETATM 9967  O  O   . HOH W 6 .   ? 10.172  -11.095 -20.681 1.00 31.24 ? 616 HOH D O   1 
HETATM 9968  O  O   . HOH W 6 .   ? 4.824   -16.516 -30.160 1.00 37.03 ? 617 HOH D O   1 
HETATM 9969  O  O   . HOH W 6 .   ? -9.813  10.417  -42.221 1.00 30.54 ? 618 HOH D O   1 
HETATM 9970  O  O   . HOH W 6 .   ? 0.763   19.379  -21.749 1.00 24.08 ? 619 HOH D O   1 
HETATM 9971  O  O   . HOH W 6 .   ? 0.549   15.447  -59.704 1.00 29.70 ? 620 HOH D O   1 
HETATM 9972  O  O   . HOH W 6 .   ? -10.796 22.067  -29.989 1.00 23.07 ? 621 HOH D O   1 
HETATM 9973  O  O   . HOH W 6 .   ? 21.026  18.552  -42.693 1.00 23.64 ? 622 HOH D O   1 
HETATM 9974  O  O   . HOH W 6 .   ? -11.003 4.862   -24.623 1.00 41.19 ? 623 HOH D O   1 
HETATM 9975  O  O   . HOH W 6 .   ? 4.409   17.223  -18.144 1.00 32.20 ? 624 HOH D O   1 
HETATM 9976  O  O   . HOH W 6 .   ? 20.983  9.460   -25.845 1.00 27.46 ? 625 HOH D O   1 
HETATM 9977  O  O   . HOH W 6 .   ? 8.644   -13.585 -29.811 1.00 29.15 ? 626 HOH D O   1 
HETATM 9978  O  O   . HOH W 6 .   ? 5.093   -15.655 -36.172 1.00 37.44 ? 627 HOH D O   1 
HETATM 9979  O  O   . HOH W 6 .   ? 7.554   -5.122  -14.477 1.00 23.34 ? 628 HOH D O   1 
HETATM 9980  O  O   . HOH W 6 .   ? 21.526  -5.270  -57.575 1.00 33.19 ? 629 HOH D O   1 
HETATM 9981  O  O   . HOH W 6 .   ? 11.415  15.397  -50.228 1.00 37.42 ? 630 HOH D O   1 
HETATM 9982  O  O   . HOH W 6 .   ? 14.255  2.661   -16.542 1.00 30.19 ? 631 HOH D O   1 
HETATM 9983  O  O   . HOH W 6 .   ? 23.582  8.287   -45.411 1.00 26.22 ? 632 HOH D O   1 
HETATM 9984  O  O   . HOH W 6 .   ? 22.987  12.039  -51.017 1.00 33.16 ? 633 HOH D O   1 
HETATM 9985  O  O   . HOH W 6 .   ? -18.784 5.587   -40.738 1.00 31.03 ? 634 HOH D O   1 
HETATM 9986  O  O   . HOH W 6 .   ? 13.959  21.967  -28.362 1.00 20.41 ? 635 HOH D O   1 
HETATM 9987  O  O   . HOH W 6 .   ? 18.478  -0.337  -20.468 1.00 26.82 ? 636 HOH D O   1 
HETATM 9988  O  O   . HOH W 6 .   ? 0.870   -14.824 -41.692 1.00 33.46 ? 637 HOH D O   1 
HETATM 9989  O  O   . HOH W 6 .   ? 11.880  6.054   -19.469 1.00 28.61 ? 638 HOH D O   1 
HETATM 9990  O  O   . HOH W 6 .   ? -2.930  -14.902 -49.077 1.00 26.69 ? 639 HOH D O   1 
HETATM 9991  O  O   . HOH W 6 .   ? -14.437 9.862   -44.748 1.00 37.10 ? 640 HOH D O   1 
HETATM 9992  O  O   . HOH W 6 .   ? -9.625  16.119  -28.477 1.00 25.89 ? 641 HOH D O   1 
HETATM 9993  O  O   . HOH W 6 .   ? -6.347  -2.703  -21.238 1.00 24.22 ? 642 HOH D O   1 
HETATM 9994  O  O   . HOH W 6 .   ? 8.468   -9.213  -14.002 1.00 27.29 ? 643 HOH D O   1 
HETATM 9995  O  O   . HOH W 6 .   ? 14.221  -8.432  -52.507 1.00 20.62 ? 644 HOH D O   1 
HETATM 9996  O  O   . HOH W 6 .   ? 16.501  19.671  -56.768 1.00 29.51 ? 645 HOH D O   1 
HETATM 9997  O  O   . HOH W 6 .   ? 7.536   20.756  -36.387 1.00 30.96 ? 646 HOH D O   1 
HETATM 9998  O  O   . HOH W 6 .   ? -4.516  -14.227 -41.628 1.00 32.41 ? 647 HOH D O   1 
HETATM 9999  O  O   . HOH W 6 .   ? 9.186   17.394  -44.467 1.00 33.66 ? 648 HOH D O   1 
HETATM 10000 O  O   . HOH W 6 .   ? 21.706  -9.843  -19.181 1.00 34.38 ? 649 HOH D O   1 
HETATM 10001 O  O   . HOH W 6 .   ? -2.378  11.202  -58.191 1.00 29.39 ? 650 HOH D O   1 
HETATM 10002 O  O   . HOH W 6 .   ? 17.108  18.911  -42.813 1.00 36.14 ? 651 HOH D O   1 
HETATM 10003 O  O   . HOH W 6 .   ? -2.607  21.876  -25.935 1.00 30.71 ? 652 HOH D O   1 
HETATM 10004 O  O   . HOH W 6 .   ? 20.626  11.746  -52.321 1.00 40.46 ? 653 HOH D O   1 
HETATM 10005 O  O   . HOH W 6 .   ? -4.538  -14.651 -46.359 1.00 39.65 ? 654 HOH D O   1 
HETATM 10006 O  O   . HOH W 6 .   ? 17.815  -10.667 -48.399 1.00 36.42 ? 655 HOH D O   1 
HETATM 10007 O  O   . HOH W 6 .   ? 22.700  -5.061  -26.660 1.00 25.83 ? 656 HOH D O   1 
HETATM 10008 O  O   . HOH W 6 .   ? 20.307  -6.712  -38.296 1.00 29.42 ? 657 HOH D O   1 
HETATM 10009 O  O   . HOH W 6 .   ? 18.000  16.729  -48.910 1.00 55.33 ? 658 HOH D O   1 
HETATM 10010 O  O   . HOH W 6 .   ? 11.533  17.879  -45.829 1.00 51.19 ? 659 HOH D O   1 
HETATM 10011 O  O   . HOH W 6 .   ? 12.449  12.725  -22.267 1.00 30.97 ? 660 HOH D O   1 
HETATM 10012 O  O   . HOH W 6 .   ? 9.610   12.535  -22.487 1.00 26.39 ? 661 HOH D O   1 
HETATM 10013 O  O   . HOH W 6 .   ? 19.882  -11.340 -27.564 1.00 29.35 ? 662 HOH D O   1 
HETATM 10014 O  O   . HOH W 6 .   ? 0.569   -12.117 -14.160 1.00 33.97 ? 663 HOH D O   1 
HETATM 10015 O  O   . HOH W 6 .   ? -8.705  -6.465  -28.400 1.00 36.20 ? 664 HOH D O   1 
HETATM 10016 O  O   . HOH W 6 .   ? -15.541 -1.187  -32.996 1.00 28.10 ? 665 HOH D O   1 
HETATM 10017 O  O   . HOH W 6 .   ? -17.139 -4.583  -36.423 1.00 30.79 ? 666 HOH D O   1 
HETATM 10018 O  O   . HOH W 6 .   ? 2.683   14.077  -43.246 1.00 32.61 ? 667 HOH D O   1 
HETATM 10019 O  O   . HOH W 6 .   ? 0.868   14.871  -45.952 1.00 40.54 ? 668 HOH D O   1 
HETATM 10020 O  O   . HOH W 6 .   ? -15.994 10.129  -34.134 1.00 41.54 ? 669 HOH D O   1 
HETATM 10021 O  O   . HOH W 6 .   ? -9.964  14.957  -30.723 1.00 27.22 ? 670 HOH D O   1 
HETATM 10022 O  O   . HOH W 6 .   ? -14.542 9.416   -42.096 1.00 35.30 ? 671 HOH D O   1 
HETATM 10023 O  O   . HOH W 6 .   ? -2.020  -4.233  -55.853 1.00 35.45 ? 672 HOH D O   1 
HETATM 10024 O  O   . HOH W 6 .   ? 0.786   -3.355  -56.407 1.00 29.08 ? 673 HOH D O   1 
HETATM 10025 O  O   . HOH W 6 .   ? -1.043  9.805   -60.595 1.00 38.97 ? 674 HOH D O   1 
HETATM 10026 O  O   . HOH W 6 .   ? -18.375 -1.444  -45.218 1.00 36.32 ? 675 HOH D O   1 
HETATM 10027 O  O   . HOH W 6 .   ? 3.428   -13.893 -39.215 1.00 29.77 ? 676 HOH D O   1 
HETATM 10028 O  O   . HOH W 6 .   ? 9.454   -17.714 -22.295 1.00 46.18 ? 677 HOH D O   1 
HETATM 10029 O  O   . HOH W 6 .   ? 3.911   12.675  -41.051 1.00 23.66 ? 678 HOH D O   1 
HETATM 10030 O  O   . HOH W 6 .   ? 10.193  15.997  -48.043 1.00 34.53 ? 679 HOH D O   1 
HETATM 10031 O  O   . HOH W 6 .   ? 11.395  17.768  -51.980 1.00 28.27 ? 680 HOH D O   1 
HETATM 10032 O  O   . HOH W 6 .   ? 6.951   22.989  -32.725 1.00 39.43 ? 681 HOH D O   1 
HETATM 10033 O  O   . HOH W 6 .   ? -0.685  13.050  -37.480 1.00 36.06 ? 682 HOH D O   1 
HETATM 10034 O  O   . HOH W 6 .   ? 3.910   16.773  -49.005 1.00 38.86 ? 683 HOH D O   1 
HETATM 10035 O  O   . HOH W 6 .   ? 5.963   16.301  -45.720 1.00 35.47 ? 684 HOH D O   1 
HETATM 10036 O  O   . HOH W 6 .   ? -1.197  -12.560 -39.236 1.00 24.18 ? 685 HOH D O   1 
HETATM 10037 O  O   . HOH W 6 .   ? 15.813  1.825   -59.402 1.00 30.00 ? 686 HOH D O   1 
HETATM 10038 O  O   . HOH W 6 .   ? 2.788   1.741   -19.946 1.00 34.06 ? 687 HOH D O   1 
HETATM 10039 O  O   . HOH W 6 .   ? -1.690  2.411   -58.383 1.00 40.54 ? 688 HOH D O   1 
HETATM 10040 O  O   . HOH W 6 .   ? 0.194   -0.054  -56.765 1.00 29.73 ? 689 HOH D O   1 
HETATM 10041 O  O   . HOH W 6 .   ? -12.423 -4.670  -31.949 1.00 37.35 ? 690 HOH D O   1 
HETATM 10042 O  O   . HOH W 6 .   ? -14.185 3.159   -26.123 1.00 35.72 ? 691 HOH D O   1 
HETATM 10043 O  O   . HOH W 6 .   ? 7.048   -15.405 -30.925 1.00 38.30 ? 692 HOH D O   1 
HETATM 10044 O  O   . HOH W 6 .   ? -16.255 3.132   -38.584 1.00 29.81 ? 693 HOH D O   1 
HETATM 10045 O  O   . HOH W 6 .   ? 20.177  -2.696  -36.325 1.00 31.61 ? 694 HOH D O   1 
HETATM 10046 O  O   . HOH W 6 .   ? 21.603  -11.837 -23.221 1.00 32.24 ? 695 HOH D O   1 
HETATM 10047 O  O   . HOH W 6 .   ? -4.610  -14.376 -27.775 1.00 44.67 ? 696 HOH D O   1 
HETATM 10048 O  O   . HOH W 6 .   ? -3.004  8.415   -61.160 1.00 36.46 ? 697 HOH D O   1 
HETATM 10049 O  O   . HOH W 6 .   ? -3.546  -15.786 -43.763 1.00 34.84 ? 698 HOH D O   1 
HETATM 10050 O  O   . HOH W 6 .   ? -11.323 12.381  -30.585 1.00 30.80 ? 699 HOH D O   1 
HETATM 10051 O  O   . HOH W 6 .   ? -7.313  4.862   -18.957 1.00 31.69 ? 700 HOH D O   1 
HETATM 10052 O  O   . HOH W 6 .   ? -2.628  -14.463 -26.176 1.00 31.06 ? 701 HOH D O   1 
HETATM 10053 O  O   . HOH W 6 .   ? 13.682  -11.360 -38.609 1.00 35.40 ? 702 HOH D O   1 
HETATM 10054 O  O   . HOH W 6 .   ? 10.851  -0.600  -13.883 1.00 32.42 ? 703 HOH D O   1 
HETATM 10055 O  O   . HOH W 6 .   ? 3.162   21.610  -23.050 1.00 36.09 ? 704 HOH D O   1 
HETATM 10056 O  O   . HOH W 6 .   ? 18.638  7.540   -53.073 1.00 31.14 ? 705 HOH D O   1 
HETATM 10057 O  O   . HOH W 6 .   ? -9.988  -1.401  -21.818 1.00 36.72 ? 706 HOH D O   1 
HETATM 10058 O  O   . HOH W 6 .   ? 1.557   -15.689 -39.735 1.00 32.90 ? 707 HOH D O   1 
HETATM 10059 O  O   . HOH W 6 .   ? 14.690  -0.590  -57.879 1.00 34.86 ? 708 HOH D O   1 
HETATM 10060 O  O   . HOH W 6 .   ? 9.077   16.525  -40.012 1.00 41.55 ? 709 HOH D O   1 
HETATM 10061 O  O   . HOH W 6 .   ? 16.168  -14.075 -33.904 1.00 39.46 ? 710 HOH D O   1 
HETATM 10062 O  O   . HOH W 6 .   ? -5.505  19.616  -21.953 1.00 28.51 ? 711 HOH D O   1 
HETATM 10063 O  O   . HOH W 6 .   ? 12.389  21.364  -44.196 1.00 56.37 ? 712 HOH D O   1 
HETATM 10064 O  O   . HOH W 6 .   ? -1.634  2.382   -19.684 1.00 32.45 ? 713 HOH D O   1 
HETATM 10065 O  O   . HOH W 6 .   ? -3.912  -11.731 -42.827 1.00 31.52 ? 714 HOH D O   1 
HETATM 10066 O  O   . HOH W 6 .   ? -8.319  -10.593 -41.774 1.00 32.90 ? 715 HOH D O   1 
HETATM 10067 O  O   . HOH W 6 .   ? -5.947  -9.957  -41.245 1.00 39.07 ? 716 HOH D O   1 
HETATM 10068 O  O   . HOH W 6 .   ? -6.810  -11.534 -24.763 1.00 46.47 ? 717 HOH D O   1 
HETATM 10069 O  O   . HOH W 6 .   ? 19.997  14.086  -54.552 1.00 42.04 ? 718 HOH D O   1 
HETATM 10070 O  O   . HOH W 6 .   ? 15.258  6.032   -18.974 1.00 32.28 ? 719 HOH D O   1 
HETATM 10071 O  O   . HOH W 6 .   ? 13.260  22.275  -34.818 1.00 31.15 ? 720 HOH D O   1 
HETATM 10072 O  O   . HOH W 6 .   ? -21.313 0.654   -46.307 1.00 32.88 ? 721 HOH D O   1 
# 
